data_7HCJ
# 
_entry.id   7HCJ 
# 
_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   7HCJ         pdb_00007hcj 10.2210/pdb7hcj/pdb 
WWPDB D_1001407301 ?            ?                   
# 
_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                        7HCJ 
_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 '(2R)-2-methyl-3-[(2-oxo-1,2,3,4-tetrahydroquinoline-6-carbonyl)amino]propanoic acid' 276.288   1   ? ? ? ? 
3 non-polymer syn '(2S)-2-methyl-3-[(2-oxo-1,2,3,4-tetrahydroquinoline-6-carbonyl)amino]propanoic acid' 276.288   1   ? ? ? ? 
4 water       nat water                                                                                 18.015    417 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(2R)-2-methyl-3-[(2-oxo-1,2,3,4-tetrahydroquinoline-6-carbonyl)amino]propanoic acid' A1A5D 
3 '(2S)-2-methyl-3-[(2-oxo-1,2,3,4-tetrahydroquinoline-6-carbonyl)amino]propanoic acid' A1A5E 
4 water                                                                                 HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1A5D non-polymer         . '(2R)-2-methyl-3-[(2-oxo-1,2,3,4-tetrahydroquinoline-6-carbonyl)amino]propanoic acid' ? 
'C14 H16 N2 O4'  276.288 
A1A5E non-polymer         . '(2S)-2-methyl-3-[(2-oxo-1,2,3,4-tetrahydroquinoline-6-carbonyl)amino]propanoic acid' ? 
'C14 H16 N2 O4'  276.288 
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 A1A5D 1   201 201  A1A5D LA1 A . 
D 3 A1A5E 1   202 301  A1A5E LA2 A . 
E 4 HOH   1   301 8    HOH   HOH A . 
E 4 HOH   2   302 93   HOH   HOH A . 
E 4 HOH   3   303 196  HOH   HOH A . 
E 4 HOH   4   304 192  HOH   HOH A . 
E 4 HOH   5   305 493  HOH   HOH A . 
E 4 HOH   6   306 292  HOH   HOH A . 
E 4 HOH   7   307 229  HOH   HOH A . 
E 4 HOH   8   308 625  HOH   HOH A . 
E 4 HOH   9   309 85   HOH   HOH A . 
E 4 HOH   10  310 209  HOH   HOH A . 
E 4 HOH   11  311 86   HOH   HOH A . 
E 4 HOH   12  312 1275 HOH   HOH A . 
E 4 HOH   13  313 109  HOH   HOH A . 
E 4 HOH   14  314 132  HOH   HOH A . 
E 4 HOH   15  315 1301 HOH   HOH A . 
E 4 HOH   16  316 76   HOH   HOH A . 
E 4 HOH   17  317 225  HOH   HOH A . 
E 4 HOH   18  318 661  HOH   HOH A . 
E 4 HOH   19  319 1283 HOH   HOH A . 
E 4 HOH   20  320 105  HOH   HOH A . 
E 4 HOH   21  321 136  HOH   HOH A . 
E 4 HOH   22  322 236  HOH   HOH A . 
E 4 HOH   23  323 337  HOH   HOH A . 
E 4 HOH   24  324 662  HOH   HOH A . 
E 4 HOH   25  325 15   HOH   HOH A . 
E 4 HOH   26  326 140  HOH   HOH A . 
E 4 HOH   27  327 124  HOH   HOH A . 
E 4 HOH   28  328 153  HOH   HOH A . 
E 4 HOH   29  329 964  HOH   HOH A . 
E 4 HOH   30  330 195  HOH   HOH A . 
E 4 HOH   31  331 151  HOH   HOH A . 
E 4 HOH   32  332 1295 HOH   HOH A . 
E 4 HOH   33  333 36   HOH   HOH A . 
E 4 HOH   34  334 393  HOH   HOH A . 
E 4 HOH   35  335 241  HOH   HOH A . 
E 4 HOH   36  336 164  HOH   HOH A . 
E 4 HOH   37  337 247  HOH   HOH A . 
E 4 HOH   38  338 320  HOH   HOH A . 
E 4 HOH   39  339 354  HOH   HOH A . 
E 4 HOH   40  340 21   HOH   HOH A . 
E 4 HOH   41  341 26   HOH   HOH A . 
E 4 HOH   42  342 1300 HOH   HOH A . 
E 4 HOH   43  343 939  HOH   HOH A . 
E 4 HOH   44  344 396  HOH   HOH A . 
E 4 HOH   45  345 66   HOH   HOH A . 
E 4 HOH   46  346 1309 HOH   HOH A . 
E 4 HOH   47  347 630  HOH   HOH A . 
E 4 HOH   48  348 42   HOH   HOH A . 
E 4 HOH   49  349 17   HOH   HOH A . 
E 4 HOH   50  350 469  HOH   HOH A . 
E 4 HOH   51  351 92   HOH   HOH A . 
E 4 HOH   52  352 296  HOH   HOH A . 
E 4 HOH   53  353 139  HOH   HOH A . 
E 4 HOH   54  354 165  HOH   HOH A . 
E 4 HOH   55  355 81   HOH   HOH A . 
E 4 HOH   56  356 162  HOH   HOH A . 
E 4 HOH   57  357 155  HOH   HOH A . 
E 4 HOH   58  358 102  HOH   HOH A . 
E 4 HOH   59  359 57   HOH   HOH A . 
E 4 HOH   60  360 2    HOH   HOH A . 
E 4 HOH   61  361 45   HOH   HOH A . 
E 4 HOH   62  362 18   HOH   HOH A . 
E 4 HOH   63  363 78   HOH   HOH A . 
E 4 HOH   64  364 138  HOH   HOH A . 
E 4 HOH   65  365 19   HOH   HOH A . 
E 4 HOH   66  366 148  HOH   HOH A . 
E 4 HOH   67  367 281  HOH   HOH A . 
E 4 HOH   68  368 186  HOH   HOH A . 
E 4 HOH   69  369 169  HOH   HOH A . 
E 4 HOH   70  370 5    HOH   HOH A . 
E 4 HOH   71  371 49   HOH   HOH A . 
E 4 HOH   72  372 3    HOH   HOH A . 
E 4 HOH   73  373 27   HOH   HOH A . 
E 4 HOH   74  374 1289 HOH   HOH A . 
E 4 HOH   75  375 56   HOH   HOH A . 
E 4 HOH   76  376 159  HOH   HOH A . 
E 4 HOH   77  377 39   HOH   HOH A . 
E 4 HOH   78  378 218  HOH   HOH A . 
E 4 HOH   79  379 366  HOH   HOH A . 
E 4 HOH   80  380 46   HOH   HOH A . 
E 4 HOH   81  381 1290 HOH   HOH A . 
E 4 HOH   82  382 4    HOH   HOH A . 
E 4 HOH   83  383 62   HOH   HOH A . 
E 4 HOH   84  384 6    HOH   HOH A . 
E 4 HOH   85  385 116  HOH   HOH A . 
E 4 HOH   86  386 154  HOH   HOH A . 
E 4 HOH   87  387 35   HOH   HOH A . 
E 4 HOH   88  388 134  HOH   HOH A . 
E 4 HOH   89  389 33   HOH   HOH A . 
E 4 HOH   90  390 409  HOH   HOH A . 
E 4 HOH   91  391 1315 HOH   HOH A . 
E 4 HOH   92  392 405  HOH   HOH A . 
E 4 HOH   93  393 12   HOH   HOH A . 
E 4 HOH   94  394 1238 HOH   HOH A . 
E 4 HOH   95  395 74   HOH   HOH A . 
E 4 HOH   96  396 24   HOH   HOH A . 
E 4 HOH   97  397 9    HOH   HOH A . 
E 4 HOH   98  398 58   HOH   HOH A . 
E 4 HOH   99  399 83   HOH   HOH A . 
E 4 HOH   100 400 67   HOH   HOH A . 
E 4 HOH   101 401 34   HOH   HOH A . 
E 4 HOH   102 402 1308 HOH   HOH A . 
E 4 HOH   103 403 96   HOH   HOH A . 
E 4 HOH   104 404 199  HOH   HOH A . 
E 4 HOH   105 405 1279 HOH   HOH A . 
E 4 HOH   106 406 3    HOH   HOH A . 
E 4 HOH   107 407 381  HOH   HOH A . 
E 4 HOH   108 408 461  HOH   HOH A . 
E 4 HOH   109 409 68   HOH   HOH A . 
E 4 HOH   110 410 333  HOH   HOH A . 
E 4 HOH   111 411 8    HOH   HOH A . 
E 4 HOH   112 412 1    HOH   HOH A . 
E 4 HOH   113 413 582  HOH   HOH A . 
E 4 HOH   114 414 397  HOH   HOH A . 
E 4 HOH   115 415 121  HOH   HOH A . 
E 4 HOH   116 416 1310 HOH   HOH A . 
E 4 HOH   117 417 1313 HOH   HOH A . 
E 4 HOH   118 418 303  HOH   HOH A . 
E 4 HOH   119 419 123  HOH   HOH A . 
E 4 HOH   120 420 1068 HOH   HOH A . 
E 4 HOH   121 421 1222 HOH   HOH A . 
E 4 HOH   122 422 51   HOH   HOH A . 
E 4 HOH   123 423 351  HOH   HOH A . 
E 4 HOH   124 424 25   HOH   HOH A . 
E 4 HOH   125 425 122  HOH   HOH A . 
E 4 HOH   126 426 53   HOH   HOH A . 
E 4 HOH   127 427 278  HOH   HOH A . 
E 4 HOH   128 428 212  HOH   HOH A . 
E 4 HOH   129 429 125  HOH   HOH A . 
E 4 HOH   130 430 95   HOH   HOH A . 
E 4 HOH   131 431 156  HOH   HOH A . 
E 4 HOH   132 432 115  HOH   HOH A . 
E 4 HOH   133 433 1189 HOH   HOH A . 
E 4 HOH   134 434 7    HOH   HOH A . 
E 4 HOH   135 435 952  HOH   HOH A . 
E 4 HOH   136 436 70   HOH   HOH A . 
E 4 HOH   137 437 1094 HOH   HOH A . 
E 4 HOH   138 438 6    HOH   HOH A . 
E 4 HOH   139 439 188  HOH   HOH A . 
E 4 HOH   140 440 16   HOH   HOH A . 
E 4 HOH   141 441 40   HOH   HOH A . 
E 4 HOH   142 442 80   HOH   HOH A . 
E 4 HOH   143 443 1286 HOH   HOH A . 
E 4 HOH   144 444 944  HOH   HOH A . 
E 4 HOH   145 445 71   HOH   HOH A . 
E 4 HOH   146 446 576  HOH   HOH A . 
E 4 HOH   147 447 94   HOH   HOH A . 
E 4 HOH   148 448 97   HOH   HOH A . 
E 4 HOH   149 449 104  HOH   HOH A . 
E 4 HOH   150 450 1296 HOH   HOH A . 
E 4 HOH   151 451 73   HOH   HOH A . 
E 4 HOH   152 452 10   HOH   HOH A . 
E 4 HOH   153 453 79   HOH   HOH A . 
E 4 HOH   154 454 330  HOH   HOH A . 
E 4 HOH   155 455 1119 HOH   HOH A . 
E 4 HOH   156 456 107  HOH   HOH A . 
E 4 HOH   157 457 509  HOH   HOH A . 
E 4 HOH   158 458 1134 HOH   HOH A . 
E 4 HOH   159 459 163  HOH   HOH A . 
E 4 HOH   160 460 408  HOH   HOH A . 
E 4 HOH   161 461 726  HOH   HOH A . 
E 4 HOH   162 462 756  HOH   HOH A . 
E 4 HOH   163 463 556  HOH   HOH A . 
E 4 HOH   164 464 63   HOH   HOH A . 
E 4 HOH   165 465 801  HOH   HOH A . 
E 4 HOH   166 466 126  HOH   HOH A . 
E 4 HOH   167 467 7    HOH   HOH A . 
E 4 HOH   168 468 280  HOH   HOH A . 
E 4 HOH   169 469 361  HOH   HOH A . 
E 4 HOH   170 470 319  HOH   HOH A . 
E 4 HOH   171 471 5    HOH   HOH A . 
E 4 HOH   172 472 250  HOH   HOH A . 
E 4 HOH   173 473 1307 HOH   HOH A . 
E 4 HOH   174 474 1276 HOH   HOH A . 
E 4 HOH   175 475 342  HOH   HOH A . 
E 4 HOH   176 476 1306 HOH   HOH A . 
E 4 HOH   177 477 1287 HOH   HOH A . 
E 4 HOH   178 478 224  HOH   HOH A . 
E 4 HOH   179 479 370  HOH   HOH A . 
E 4 HOH   180 480 267  HOH   HOH A . 
E 4 HOH   181 481 919  HOH   HOH A . 
E 4 HOH   182 482 135  HOH   HOH A . 
E 4 HOH   183 483 2    HOH   HOH A . 
E 4 HOH   184 484 695  HOH   HOH A . 
E 4 HOH   185 485 711  HOH   HOH A . 
E 4 HOH   186 486 674  HOH   HOH A . 
E 4 HOH   187 487 202  HOH   HOH A . 
E 4 HOH   188 488 318  HOH   HOH A . 
E 4 HOH   189 489 309  HOH   HOH A . 
E 4 HOH   190 490 805  HOH   HOH A . 
E 4 HOH   191 491 521  HOH   HOH A . 
E 4 HOH   192 492 1299 HOH   HOH A . 
E 4 HOH   193 493 331  HOH   HOH A . 
E 4 HOH   194 494 315  HOH   HOH A . 
E 4 HOH   195 495 263  HOH   HOH A . 
E 4 HOH   196 496 152  HOH   HOH A . 
E 4 HOH   197 497 1314 HOH   HOH A . 
E 4 HOH   198 498 208  HOH   HOH A . 
E 4 HOH   199 499 941  HOH   HOH A . 
E 4 HOH   200 500 356  HOH   HOH A . 
E 4 HOH   201 501 326  HOH   HOH A . 
E 4 HOH   202 502 1071 HOH   HOH A . 
E 4 HOH   203 503 350  HOH   HOH A . 
E 4 HOH   204 504 180  HOH   HOH A . 
E 4 HOH   205 505 371  HOH   HOH A . 
E 4 HOH   206 506 363  HOH   HOH A . 
E 4 HOH   207 507 1284 HOH   HOH A . 
E 4 HOH   208 508 313  HOH   HOH A . 
E 4 HOH   209 509 185  HOH   HOH A . 
E 4 HOH   210 510 429  HOH   HOH A . 
E 4 HOH   211 511 772  HOH   HOH A . 
E 4 HOH   212 512 4    HOH   HOH A . 
E 4 HOH   213 513 376  HOH   HOH A . 
E 4 HOH   214 514 1074 HOH   HOH A . 
E 4 HOH   215 515 346  HOH   HOH A . 
E 4 HOH   216 516 1292 HOH   HOH A . 
E 4 HOH   217 517 1078 HOH   HOH A . 
F 4 HOH   1   201 64   HOH   HOH B . 
F 4 HOH   2   202 358  HOH   HOH B . 
F 4 HOH   3   203 654  HOH   HOH B . 
F 4 HOH   4   204 758  HOH   HOH B . 
F 4 HOH   5   205 900  HOH   HOH B . 
F 4 HOH   6   206 549  HOH   HOH B . 
F 4 HOH   7   207 364  HOH   HOH B . 
F 4 HOH   8   208 398  HOH   HOH B . 
F 4 HOH   9   209 743  HOH   HOH B . 
F 4 HOH   10  210 343  HOH   HOH B . 
F 4 HOH   11  211 120  HOH   HOH B . 
F 4 HOH   12  212 1249 HOH   HOH B . 
F 4 HOH   13  213 264  HOH   HOH B . 
F 4 HOH   14  214 240  HOH   HOH B . 
F 4 HOH   15  215 353  HOH   HOH B . 
F 4 HOH   16  216 282  HOH   HOH B . 
F 4 HOH   17  217 232  HOH   HOH B . 
F 4 HOH   18  218 50   HOH   HOH B . 
F 4 HOH   19  219 131  HOH   HOH B . 
F 4 HOH   20  220 1140 HOH   HOH B . 
F 4 HOH   21  221 1278 HOH   HOH B . 
F 4 HOH   22  222 332  HOH   HOH B . 
F 4 HOH   23  223 452  HOH   HOH B . 
F 4 HOH   24  224 276  HOH   HOH B . 
F 4 HOH   25  225 444  HOH   HOH B . 
F 4 HOH   26  226 205  HOH   HOH B . 
F 4 HOH   27  227 531  HOH   HOH B . 
F 4 HOH   28  228 1312 HOH   HOH B . 
F 4 HOH   29  229 723  HOH   HOH B . 
F 4 HOH   30  230 54   HOH   HOH B . 
F 4 HOH   31  231 75   HOH   HOH B . 
F 4 HOH   32  232 272  HOH   HOH B . 
F 4 HOH   33  233 127  HOH   HOH B . 
F 4 HOH   34  234 82   HOH   HOH B . 
F 4 HOH   35  235 60   HOH   HOH B . 
F 4 HOH   36  236 128  HOH   HOH B . 
F 4 HOH   37  237 110  HOH   HOH B . 
F 4 HOH   38  238 166  HOH   HOH B . 
F 4 HOH   39  239 1    HOH   HOH B . 
F 4 HOH   40  240 30   HOH   HOH B . 
F 4 HOH   41  241 69   HOH   HOH B . 
F 4 HOH   42  242 181  HOH   HOH B . 
F 4 HOH   43  243 133  HOH   HOH B . 
F 4 HOH   44  244 9    HOH   HOH B . 
F 4 HOH   45  245 14   HOH   HOH B . 
F 4 HOH   46  246 231  HOH   HOH B . 
F 4 HOH   47  247 252  HOH   HOH B . 
F 4 HOH   48  248 72   HOH   HOH B . 
F 4 HOH   49  249 129  HOH   HOH B . 
F 4 HOH   50  250 172  HOH   HOH B . 
F 4 HOH   51  251 31   HOH   HOH B . 
F 4 HOH   52  252 325  HOH   HOH B . 
F 4 HOH   53  253 300  HOH   HOH B . 
F 4 HOH   54  254 52   HOH   HOH B . 
F 4 HOH   55  255 144  HOH   HOH B . 
F 4 HOH   56  256 143  HOH   HOH B . 
F 4 HOH   57  257 47   HOH   HOH B . 
F 4 HOH   58  258 10   HOH   HOH B . 
F 4 HOH   59  259 221  HOH   HOH B . 
F 4 HOH   60  260 61   HOH   HOH B . 
F 4 HOH   61  261 347  HOH   HOH B . 
F 4 HOH   62  262 150  HOH   HOH B . 
F 4 HOH   63  263 11   HOH   HOH B . 
F 4 HOH   64  264 391  HOH   HOH B . 
F 4 HOH   65  265 59   HOH   HOH B . 
F 4 HOH   66  266 77   HOH   HOH B . 
F 4 HOH   67  267 20   HOH   HOH B . 
F 4 HOH   68  268 41   HOH   HOH B . 
F 4 HOH   69  269 302  HOH   HOH B . 
F 4 HOH   70  270 103  HOH   HOH B . 
F 4 HOH   71  271 242  HOH   HOH B . 
F 4 HOH   72  272 271  HOH   HOH B . 
F 4 HOH   73  273 175  HOH   HOH B . 
F 4 HOH   74  274 216  HOH   HOH B . 
F 4 HOH   75  275 114  HOH   HOH B . 
F 4 HOH   76  276 1305 HOH   HOH B . 
F 4 HOH   77  277 84   HOH   HOH B . 
F 4 HOH   78  278 43   HOH   HOH B . 
F 4 HOH   79  279 1106 HOH   HOH B . 
F 4 HOH   80  280 1277 HOH   HOH B . 
F 4 HOH   81  281 243  HOH   HOH B . 
F 4 HOH   82  282 416  HOH   HOH B . 
F 4 HOH   83  283 387  HOH   HOH B . 
F 4 HOH   84  284 635  HOH   HOH B . 
F 4 HOH   85  285 287  HOH   HOH B . 
F 4 HOH   86  286 147  HOH   HOH B . 
F 4 HOH   87  287 160  HOH   HOH B . 
F 4 HOH   88  288 22   HOH   HOH B . 
F 4 HOH   89  289 117  HOH   HOH B . 
F 4 HOH   90  290 106  HOH   HOH B . 
F 4 HOH   91  291 220  HOH   HOH B . 
F 4 HOH   92  292 137  HOH   HOH B . 
F 4 HOH   93  293 13   HOH   HOH B . 
F 4 HOH   94  294 112  HOH   HOH B . 
F 4 HOH   95  295 88   HOH   HOH B . 
F 4 HOH   96  296 99   HOH   HOH B . 
F 4 HOH   97  297 316  HOH   HOH B . 
F 4 HOH   98  298 1066 HOH   HOH B . 
F 4 HOH   99  299 32   HOH   HOH B . 
F 4 HOH   100 300 341  HOH   HOH B . 
F 4 HOH   101 301 235  HOH   HOH B . 
F 4 HOH   102 302 142  HOH   HOH B . 
F 4 HOH   103 303 89   HOH   HOH B . 
F 4 HOH   104 304 299  HOH   HOH B . 
F 4 HOH   105 305 297  HOH   HOH B . 
F 4 HOH   106 306 141  HOH   HOH B . 
F 4 HOH   107 307 215  HOH   HOH B . 
F 4 HOH   108 308 1291 HOH   HOH B . 
F 4 HOH   109 309 91   HOH   HOH B . 
F 4 HOH   110 310 118  HOH   HOH B . 
F 4 HOH   111 311 101  HOH   HOH B . 
F 4 HOH   112 312 38   HOH   HOH B . 
F 4 HOH   113 313 48   HOH   HOH B . 
F 4 HOH   114 314 311  HOH   HOH B . 
F 4 HOH   115 315 37   HOH   HOH B . 
F 4 HOH   116 316 1126 HOH   HOH B . 
F 4 HOH   117 317 704  HOH   HOH B . 
F 4 HOH   118 318 170  HOH   HOH B . 
F 4 HOH   119 319 161  HOH   HOH B . 
F 4 HOH   120 320 28   HOH   HOH B . 
F 4 HOH   121 321 23   HOH   HOH B . 
F 4 HOH   122 322 44   HOH   HOH B . 
F 4 HOH   123 323 177  HOH   HOH B . 
F 4 HOH   124 324 100  HOH   HOH B . 
F 4 HOH   125 325 334  HOH   HOH B . 
F 4 HOH   126 326 1294 HOH   HOH B . 
F 4 HOH   127 327 29   HOH   HOH B . 
F 4 HOH   128 328 1274 HOH   HOH B . 
F 4 HOH   129 329 1285 HOH   HOH B . 
F 4 HOH   130 330 717  HOH   HOH B . 
F 4 HOH   131 331 98   HOH   HOH B . 
F 4 HOH   132 332 55   HOH   HOH B . 
F 4 HOH   133 333 339  HOH   HOH B . 
F 4 HOH   134 334 182  HOH   HOH B . 
F 4 HOH   135 335 197  HOH   HOH B . 
F 4 HOH   136 336 65   HOH   HOH B . 
F 4 HOH   137 337 207  HOH   HOH B . 
F 4 HOH   138 338 445  HOH   HOH B . 
F 4 HOH   139 339 234  HOH   HOH B . 
F 4 HOH   140 340 619  HOH   HOH B . 
F 4 HOH   141 341 1293 HOH   HOH B . 
F 4 HOH   142 342 362  HOH   HOH B . 
F 4 HOH   143 343 178  HOH   HOH B . 
F 4 HOH   144 344 90   HOH   HOH B . 
F 4 HOH   145 345 463  HOH   HOH B . 
F 4 HOH   146 346 623  HOH   HOH B . 
F 4 HOH   147 347 1304 HOH   HOH B . 
F 4 HOH   148 348 191  HOH   HOH B . 
F 4 HOH   149 349 960  HOH   HOH B . 
F 4 HOH   150 350 1046 HOH   HOH B . 
F 4 HOH   151 351 335  HOH   HOH B . 
F 4 HOH   152 352 541  HOH   HOH B . 
F 4 HOH   153 353 304  HOH   HOH B . 
F 4 HOH   154 354 1280 HOH   HOH B . 
F 4 HOH   155 355 290  HOH   HOH B . 
F 4 HOH   156 356 203  HOH   HOH B . 
F 4 HOH   157 357 87   HOH   HOH B . 
F 4 HOH   158 358 389  HOH   HOH B . 
F 4 HOH   159 359 479  HOH   HOH B . 
F 4 HOH   160 360 718  HOH   HOH B . 
F 4 HOH   161 361 1077 HOH   HOH B . 
F 4 HOH   162 362 283  HOH   HOH B . 
F 4 HOH   163 363 1072 HOH   HOH B . 
F 4 HOH   164 364 898  HOH   HOH B . 
F 4 HOH   165 365 373  HOH   HOH B . 
F 4 HOH   166 366 340  HOH   HOH B . 
F 4 HOH   167 367 667  HOH   HOH B . 
F 4 HOH   168 368 1316 HOH   HOH B . 
F 4 HOH   169 369 190  HOH   HOH B . 
F 4 HOH   170 370 291  HOH   HOH B . 
F 4 HOH   171 371 615  HOH   HOH B . 
F 4 HOH   172 372 1303 HOH   HOH B . 
F 4 HOH   173 373 310  HOH   HOH B . 
F 4 HOH   174 374 149  HOH   HOH B . 
F 4 HOH   175 375 431  HOH   HOH B . 
F 4 HOH   176 376 1163 HOH   HOH B . 
F 4 HOH   177 377 183  HOH   HOH B . 
F 4 HOH   178 378 1173 HOH   HOH B . 
F 4 HOH   179 379 418  HOH   HOH B . 
F 4 HOH   180 380 176  HOH   HOH B . 
F 4 HOH   181 381 1000 HOH   HOH B . 
F 4 HOH   182 382 1311 HOH   HOH B . 
F 4 HOH   183 383 424  HOH   HOH B . 
F 4 HOH   184 384 1298 HOH   HOH B . 
F 4 HOH   185 385 265  HOH   HOH B . 
F 4 HOH   186 386 248  HOH   HOH B . 
F 4 HOH   187 387 491  HOH   HOH B . 
F 4 HOH   188 388 981  HOH   HOH B . 
F 4 HOH   189 389 470  HOH   HOH B . 
F 4 HOH   190 390 184  HOH   HOH B . 
F 4 HOH   191 391 360  HOH   HOH B . 
F 4 HOH   192 392 410  HOH   HOH B . 
F 4 HOH   193 393 355  HOH   HOH B . 
F 4 HOH   194 394 274  HOH   HOH B . 
F 4 HOH   195 395 566  HOH   HOH B . 
F 4 HOH   196 396 314  HOH   HOH B . 
F 4 HOH   197 397 792  HOH   HOH B . 
F 4 HOH   198 398 157  HOH   HOH B . 
F 4 HOH   199 399 321  HOH   HOH B . 
F 4 HOH   200 400 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HCJ 
_cell.length_a           88.770 
_cell.length_b           88.770 
_cell.length_c           39.620 
_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                         7HCJ 
_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          7HCJ 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.81 
_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                     7HCJ 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.380 
_reflns.d_resolution_high            1.020 
_reflns.number_obs                   156563 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.800 
_reflns.pdbx_Rmerge_I_obs            0.041 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        18.400 
_reflns.B_iso_Wilson_estimate        11.910 
_reflns.pdbx_redundancy              6.500 
_reflns.pdbx_Rrim_I_all              0.045 
_reflns.pdbx_Rpim_I_all              0.017 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1019706 
_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 1.020 1.040  ? 43504 7640 ? 0.790 ? ? ? 5.700 ? 1.700  ? ? ? ? ? ? 98.700 0.871 0.358 0.861 ? 
1 2 5.590 44.380 ? 7049  1030 ? 0.033 ? ? ? 6.800 ? 54.200 ? ? ? ? ? ? 99.300 0.036 0.014 0.999 ? 
# 
_refine.entry_id                                 7HCJ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0200 
_refine.ls_d_res_low                             39.7000 
_refine.pdbx_ls_sigma_F                          1.350 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.6800 
_refine.ls_number_reflns_obs                     156493 
_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                          0.1403 
_refine.ls_R_factor_R_work                       0.1396 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1534 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7543 
_refine.ls_number_reflns_R_work                  148950 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.5593 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.0900 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                61.100 
_refine.B_iso_min                                8.830 
_refine.pdbx_overall_phase_error                 15.6400 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0200 
_refine_hist.d_res_low                        39.7000 
_refine_hist.pdbx_number_atoms_ligand         70 
_refine_hist.number_atoms_solvent             417 
_refine_hist.number_atoms_total               3029 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           13.62 
_refine_hist.pdbx_B_iso_mean_solvent          29.80 
_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 
1.0200 1.0300  30 98.0000  4896 . 0.3049 0.3193 . 196 0.0000 5092 . 'X-RAY DIFFRACTION' . 
1.0300 1.0400  30 100.0000 4967 . 0.2453 0.2664 . 287 0.0000 5254 . 'X-RAY DIFFRACTION' . 
1.0400 1.0600  30 100.0000 4869 . 0.2094 0.2113 . 279 0.0000 5148 . 'X-RAY DIFFRACTION' . 
1.0600 1.0700  30 100.0000 4973 . 0.1853 0.2022 . 275 0.0000 5248 . 'X-RAY DIFFRACTION' . 
1.0700 1.0800  30 100.0000 4904 . 0.1686 0.1858 . 233 0.0000 5137 . 'X-RAY DIFFRACTION' . 
1.0800 1.1000  30 100.0000 4963 . 0.1578 0.1881 . 251 0.0000 5214 . 'X-RAY DIFFRACTION' . 
1.1000 1.1100  30 100.0000 4950 . 0.1447 0.1671 . 248 0.0000 5198 . 'X-RAY DIFFRACTION' . 
1.1100 1.1300  30 100.0000 5013 . 0.1422 0.1591 . 230 0.0000 5243 . 'X-RAY DIFFRACTION' . 
1.1300 1.1500  30 100.0000 4926 . 0.1328 0.1523 . 241 0.0000 5167 . 'X-RAY DIFFRACTION' . 
1.1500 1.1700  30 100.0000 4991 . 0.1343 0.1519 . 249 0.0000 5240 . 'X-RAY DIFFRACTION' . 
1.1700 1.1900  30 100.0000 4931 . 0.1317 0.1590 . 250 0.0000 5181 . 'X-RAY DIFFRACTION' . 
1.1900 1.2100  30 100.0000 4898 . 0.1277 0.1629 . 274 0.0000 5172 . 'X-RAY DIFFRACTION' . 
1.2100 1.2300  30 100.0000 5005 . 0.1258 0.1426 . 223 0.0000 5228 . 'X-RAY DIFFRACTION' . 
1.2300 1.2600  30 100.0000 4964 . 0.1274 0.1398 . 257 0.0000 5221 . 'X-RAY DIFFRACTION' . 
1.2600 1.2900  30 100.0000 4935 . 0.1246 0.1378 . 249 0.0000 5184 . 'X-RAY DIFFRACTION' . 
1.2900 1.3200  30 100.0000 4975 . 0.1200 0.1352 . 263 0.0000 5238 . 'X-RAY DIFFRACTION' . 
1.3200 1.3500  30 100.0000 4961 . 0.1202 0.1478 . 257 0.0000 5218 . 'X-RAY DIFFRACTION' . 
1.3500 1.3800  30 100.0000 4963 . 0.1195 0.1445 . 257 0.0000 5220 . 'X-RAY DIFFRACTION' . 
1.3800 1.4300  30 100.0000 4969 . 0.1182 0.1422 . 237 0.0000 5206 . 'X-RAY DIFFRACTION' . 
1.4300 1.4700  30 100.0000 4971 . 0.1185 0.1284 . 254 0.0000 5225 . 'X-RAY DIFFRACTION' . 
1.4700 1.5200  30 100.0000 4975 . 0.1197 0.1358 . 235 0.0000 5210 . 'X-RAY DIFFRACTION' . 
1.5200 1.5800  30 100.0000 4985 . 0.1210 0.1353 . 262 0.0000 5247 . 'X-RAY DIFFRACTION' . 
1.5800 1.6600  30 100.0000 4949 . 0.1184 0.1238 . 258 0.0000 5207 . 'X-RAY DIFFRACTION' . 
1.6600 1.7400  30 100.0000 5013 . 0.1263 0.1364 . 203 0.0000 5216 . 'X-RAY DIFFRACTION' . 
1.7400 1.8500  30 99.0000  4931 . 0.1290 0.1342 . 292 0.0000 5223 . 'X-RAY DIFFRACTION' . 
1.8500 2.0000  30 99.0000  4962 . 0.1370 0.1379 . 248 0.0000 5210 . 'X-RAY DIFFRACTION' . 
2.0000 2.2000  30 99.0000  4947 . 0.1377 0.1407 . 284 0.0000 5231 . 'X-RAY DIFFRACTION' . 
2.2000 2.5200  30 99.0000  5010 . 0.1394 0.1417 . 251 0.0000 5261 . 'X-RAY DIFFRACTION' . 
2.5200 3.1700  30 99.0000  5013 . 0.1508 0.1652 . 251 0.0000 5264 . 'X-RAY DIFFRACTION' . 
3.1700 39.7000 30 99.0000  5141 . 0.1483 0.1753 . 249 0.0000 5390 . 'X-RAY DIFFRACTION' . 
# 
_struct.entry_id                  7HCJ 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0000328' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HCJ 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HCJ A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HCJ 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 7HCJ SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HCJ MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HCJ SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HCJ MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E 
2 1 B,F     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N 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 LEU B 93  ? O LEU B 93  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HCJ 
_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 1.56 
2 1 O  A ASP 66 ? ? 1_555 HG  B SER 1  ? B 2_655 1.59 
# 
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  ? ? 55.60 -132.96 
2 1 SER A 128 ? B 63.77 -6.43   
3 1 HIS B 86  ? ? 57.81 -128.42 
# 
_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 515 ? 5.94 . 
2 1 O ? A HOH 516 ? 6.03 . 
3 1 O ? A HOH 517 ? 7.33 . 
4 1 O ? B HOH 400 ? 6.22 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A SER 1 ? A SER 1 
2 1 Y 1 A MET 2 ? A MET 2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1A5D N2   N N N 1   
A1A5D C3   C N N 2   
A1A5D C6   C Y N 3   
A1A5D C9   C N N 4   
A1A5D C12  C Y N 5   
A1A5D C14  C N N 6   
A1A5D C1   C N N 7   
A1A5D C10  C N N 8   
A1A5D C11  C N N 9   
A1A5D C13  C Y N 10  
A1A5D C2   C N R 11  
A1A5D C4   C N N 12  
A1A5D C5   C Y N 13  
A1A5D C7   C Y N 14  
A1A5D C8   C Y N 15  
A1A5D N1   N N N 16  
A1A5D O1   O N N 17  
A1A5D O2   O N N 18  
A1A5D O3   O N N 19  
A1A5D O4   O N N 20  
A1A5D H10  H N N 21  
A1A5D H5   H N N 22  
A1A5D H6   H N N 23  
A1A5D H8   H N N 24  
A1A5D H2   H N N 25  
A1A5D H3   H N N 26  
A1A5D H4   H N N 27  
A1A5D H12  H N N 28  
A1A5D H11  H N N 29  
A1A5D H13  H N N 30  
A1A5D H14  H N N 31  
A1A5D H15  H N N 32  
A1A5D H1   H N N 33  
A1A5D H9   H N N 34  
A1A5D H7   H N N 35  
A1A5D H16  H N N 36  
A1A5E O1   O N N 37  
A1A5E C1   C N N 38  
A1A5E C2   C N S 39  
A1A5E C3   C N N 40  
A1A5E C4   C N N 41  
A1A5E C5   C Y N 42  
A1A5E C6   C Y N 43  
A1A5E C7   C Y N 44  
A1A5E C8   C Y N 45  
A1A5E C10  C N N 46  
A1A5E C11  C N N 47  
A1A5E C12  C Y N 48  
A1A5E C13  C Y N 49  
A1A5E C14  C N N 50  
A1A5E C9   C N N 51  
A1A5E N1   N N N 52  
A1A5E N2   N N N 53  
A1A5E O2   O N N 54  
A1A5E O3   O N N 55  
A1A5E O4   O N N 56  
A1A5E H3   H N N 57  
A1A5E H2   H N N 58  
A1A5E H4   H N N 59  
A1A5E H1   H N N 60  
A1A5E H5   H N N 61  
A1A5E H6   H N N 62  
A1A5E H8   H N N 63  
A1A5E H9   H N N 64  
A1A5E H12  H N N 65  
A1A5E H11  H N N 66  
A1A5E H13  H N N 67  
A1A5E H14  H N N 68  
A1A5E H15  H N N 69  
A1A5E H7   H N N 70  
A1A5E H10  H N N 71  
A1A5E H16  H N N 72  
ALA   N    N N N 73  
ALA   CA   C N S 74  
ALA   C    C N N 75  
ALA   O    O N N 76  
ALA   CB   C N N 77  
ALA   OXT  O N N 78  
ALA   H    H N N 79  
ALA   H2   H N N 80  
ALA   HA   H N N 81  
ALA   HB1  H N N 82  
ALA   HB2  H N N 83  
ALA   HB3  H N N 84  
ALA   HXT  H N N 85  
ARG   N    N N N 86  
ARG   CA   C N S 87  
ARG   C    C N N 88  
ARG   O    O N N 89  
ARG   CB   C N N 90  
ARG   CG   C N N 91  
ARG   CD   C N N 92  
ARG   NE   N N N 93  
ARG   CZ   C N N 94  
ARG   NH1  N N N 95  
ARG   NH2  N N N 96  
ARG   OXT  O N N 97  
ARG   H    H N N 98  
ARG   H2   H N N 99  
ARG   HA   H N N 100 
ARG   HB2  H N N 101 
ARG   HB3  H N N 102 
ARG   HG2  H N N 103 
ARG   HG3  H N N 104 
ARG   HD2  H N N 105 
ARG   HD3  H N N 106 
ARG   HE   H N N 107 
ARG   HH11 H N N 108 
ARG   HH12 H N N 109 
ARG   HH21 H N N 110 
ARG   HH22 H N N 111 
ARG   HXT  H N N 112 
ASN   N    N N N 113 
ASN   CA   C N S 114 
ASN   C    C N N 115 
ASN   O    O N N 116 
ASN   CB   C N N 117 
ASN   CG   C N N 118 
ASN   OD1  O N N 119 
ASN   ND2  N N N 120 
ASN   OXT  O N N 121 
ASN   H    H N N 122 
ASN   H2   H N N 123 
ASN   HA   H N N 124 
ASN   HB2  H N N 125 
ASN   HB3  H N N 126 
ASN   HD21 H N N 127 
ASN   HD22 H N N 128 
ASN   HXT  H N N 129 
ASP   N    N N N 130 
ASP   CA   C N S 131 
ASP   C    C N N 132 
ASP   O    O N N 133 
ASP   CB   C N N 134 
ASP   CG   C N N 135 
ASP   OD1  O N N 136 
ASP   OD2  O N N 137 
ASP   OXT  O N N 138 
ASP   H    H N N 139 
ASP   H2   H N N 140 
ASP   HA   H N N 141 
ASP   HB2  H N N 142 
ASP   HB3  H N N 143 
ASP   HD2  H N N 144 
ASP   HXT  H N N 145 
CYS   N    N N N 146 
CYS   CA   C N R 147 
CYS   C    C N N 148 
CYS   O    O N N 149 
CYS   CB   C N N 150 
CYS   SG   S N N 151 
CYS   OXT  O N N 152 
CYS   H    H N N 153 
CYS   H2   H N N 154 
CYS   HA   H N N 155 
CYS   HB2  H N N 156 
CYS   HB3  H N N 157 
CYS   HG   H N N 158 
CYS   HXT  H N N 159 
GLN   N    N N N 160 
GLN   CA   C N S 161 
GLN   C    C N N 162 
GLN   O    O N N 163 
GLN   CB   C N N 164 
GLN   CG   C N N 165 
GLN   CD   C N N 166 
GLN   OE1  O N N 167 
GLN   NE2  N N N 168 
GLN   OXT  O N N 169 
GLN   H    H N N 170 
GLN   H2   H N N 171 
GLN   HA   H N N 172 
GLN   HB2  H N N 173 
GLN   HB3  H N N 174 
GLN   HG2  H N N 175 
GLN   HG3  H N N 176 
GLN   HE21 H N N 177 
GLN   HE22 H N N 178 
GLN   HXT  H N N 179 
GLU   N    N N N 180 
GLU   CA   C N S 181 
GLU   C    C N N 182 
GLU   O    O N N 183 
GLU   CB   C N N 184 
GLU   CG   C N N 185 
GLU   CD   C N N 186 
GLU   OE1  O N N 187 
GLU   OE2  O N N 188 
GLU   OXT  O N N 189 
GLU   H    H N N 190 
GLU   H2   H N N 191 
GLU   HA   H N N 192 
GLU   HB2  H N N 193 
GLU   HB3  H N N 194 
GLU   HG2  H N N 195 
GLU   HG3  H N N 196 
GLU   HE2  H N N 197 
GLU   HXT  H N N 198 
GLY   N    N N N 199 
GLY   CA   C N N 200 
GLY   C    C N N 201 
GLY   O    O N N 202 
GLY   OXT  O N N 203 
GLY   H    H N N 204 
GLY   H2   H N N 205 
GLY   HA2  H N N 206 
GLY   HA3  H N N 207 
GLY   HXT  H N N 208 
HIS   N    N N N 209 
HIS   CA   C N S 210 
HIS   C    C N N 211 
HIS   O    O N N 212 
HIS   CB   C N N 213 
HIS   CG   C Y N 214 
HIS   ND1  N Y N 215 
HIS   CD2  C Y N 216 
HIS   CE1  C Y N 217 
HIS   NE2  N Y N 218 
HIS   OXT  O N N 219 
HIS   H    H N N 220 
HIS   H2   H N N 221 
HIS   HA   H N N 222 
HIS   HB2  H N N 223 
HIS   HB3  H N N 224 
HIS   HD1  H N N 225 
HIS   HD2  H N N 226 
HIS   HE1  H N N 227 
HIS   HE2  H N N 228 
HIS   HXT  H N N 229 
HOH   O    O N N 230 
HOH   H1   H N N 231 
HOH   H2   H N N 232 
ILE   N    N N N 233 
ILE   CA   C N S 234 
ILE   C    C N N 235 
ILE   O    O N N 236 
ILE   CB   C N S 237 
ILE   CG1  C N N 238 
ILE   CG2  C N N 239 
ILE   CD1  C N N 240 
ILE   OXT  O N N 241 
ILE   H    H N N 242 
ILE   H2   H N N 243 
ILE   HA   H N N 244 
ILE   HB   H N N 245 
ILE   HG12 H N N 246 
ILE   HG13 H N N 247 
ILE   HG21 H N N 248 
ILE   HG22 H N N 249 
ILE   HG23 H N N 250 
ILE   HD11 H N N 251 
ILE   HD12 H N N 252 
ILE   HD13 H N N 253 
ILE   HXT  H N N 254 
LEU   N    N N N 255 
LEU   CA   C N S 256 
LEU   C    C N N 257 
LEU   O    O N N 258 
LEU   CB   C N N 259 
LEU   CG   C N N 260 
LEU   CD1  C N N 261 
LEU   CD2  C N N 262 
LEU   OXT  O N N 263 
LEU   H    H N N 264 
LEU   H2   H N N 265 
LEU   HA   H N N 266 
LEU   HB2  H N N 267 
LEU   HB3  H N N 268 
LEU   HG   H N N 269 
LEU   HD11 H N N 270 
LEU   HD12 H N N 271 
LEU   HD13 H N N 272 
LEU   HD21 H N N 273 
LEU   HD22 H N N 274 
LEU   HD23 H N N 275 
LEU   HXT  H N N 276 
LYS   N    N N N 277 
LYS   CA   C N S 278 
LYS   C    C N N 279 
LYS   O    O N N 280 
LYS   CB   C N N 281 
LYS   CG   C N N 282 
LYS   CD   C N N 283 
LYS   CE   C N N 284 
LYS   NZ   N N N 285 
LYS   OXT  O N N 286 
LYS   H    H N N 287 
LYS   H2   H N N 288 
LYS   HA   H N N 289 
LYS   HB2  H N N 290 
LYS   HB3  H N N 291 
LYS   HG2  H N N 292 
LYS   HG3  H N N 293 
LYS   HD2  H N N 294 
LYS   HD3  H N N 295 
LYS   HE2  H N N 296 
LYS   HE3  H N N 297 
LYS   HZ1  H N N 298 
LYS   HZ2  H N N 299 
LYS   HZ3  H N N 300 
LYS   HXT  H N N 301 
MET   N    N N N 302 
MET   CA   C N S 303 
MET   C    C N N 304 
MET   O    O N N 305 
MET   CB   C N N 306 
MET   CG   C N N 307 
MET   SD   S N N 308 
MET   CE   C N N 309 
MET   OXT  O N N 310 
MET   H    H N N 311 
MET   H2   H N N 312 
MET   HA   H N N 313 
MET   HB2  H N N 314 
MET   HB3  H N N 315 
MET   HG2  H N N 316 
MET   HG3  H N N 317 
MET   HE1  H N N 318 
MET   HE2  H N N 319 
MET   HE3  H N N 320 
MET   HXT  H N N 321 
PHE   N    N N N 322 
PHE   CA   C N S 323 
PHE   C    C N N 324 
PHE   O    O N N 325 
PHE   CB   C N N 326 
PHE   CG   C Y N 327 
PHE   CD1  C Y N 328 
PHE   CD2  C Y N 329 
PHE   CE1  C Y N 330 
PHE   CE2  C Y N 331 
PHE   CZ   C Y N 332 
PHE   OXT  O N N 333 
PHE   H    H N N 334 
PHE   H2   H N N 335 
PHE   HA   H N N 336 
PHE   HB2  H N N 337 
PHE   HB3  H N N 338 
PHE   HD1  H N N 339 
PHE   HD2  H N N 340 
PHE   HE1  H N N 341 
PHE   HE2  H N N 342 
PHE   HZ   H N N 343 
PHE   HXT  H N N 344 
PRO   N    N N N 345 
PRO   CA   C N S 346 
PRO   C    C N N 347 
PRO   O    O N N 348 
PRO   CB   C N N 349 
PRO   CG   C N N 350 
PRO   CD   C N N 351 
PRO   OXT  O N N 352 
PRO   H    H N N 353 
PRO   HA   H N N 354 
PRO   HB2  H N N 355 
PRO   HB3  H N N 356 
PRO   HG2  H N N 357 
PRO   HG3  H N N 358 
PRO   HD2  H N N 359 
PRO   HD3  H N N 360 
PRO   HXT  H N N 361 
SER   N    N N N 362 
SER   CA   C N S 363 
SER   C    C N N 364 
SER   O    O N N 365 
SER   CB   C N N 366 
SER   OG   O N N 367 
SER   OXT  O N N 368 
SER   H    H N N 369 
SER   H2   H N N 370 
SER   HA   H N N 371 
SER   HB2  H N N 372 
SER   HB3  H N N 373 
SER   HG   H N N 374 
SER   HXT  H N N 375 
THR   N    N N N 376 
THR   CA   C N S 377 
THR   C    C N N 378 
THR   O    O N N 379 
THR   CB   C N R 380 
THR   OG1  O N N 381 
THR   CG2  C N N 382 
THR   OXT  O N N 383 
THR   H    H N N 384 
THR   H2   H N N 385 
THR   HA   H N N 386 
THR   HB   H N N 387 
THR   HG1  H N N 388 
THR   HG21 H N N 389 
THR   HG22 H N N 390 
THR   HG23 H N N 391 
THR   HXT  H N N 392 
TYR   N    N N N 393 
TYR   CA   C N S 394 
TYR   C    C N N 395 
TYR   O    O N N 396 
TYR   CB   C N N 397 
TYR   CG   C Y N 398 
TYR   CD1  C Y N 399 
TYR   CD2  C Y N 400 
TYR   CE1  C Y N 401 
TYR   CE2  C Y N 402 
TYR   CZ   C Y N 403 
TYR   OH   O N N 404 
TYR   OXT  O N N 405 
TYR   H    H N N 406 
TYR   H2   H N N 407 
TYR   HA   H N N 408 
TYR   HB2  H N N 409 
TYR   HB3  H N N 410 
TYR   HD1  H N N 411 
TYR   HD2  H N N 412 
TYR   HE1  H N N 413 
TYR   HE2  H N N 414 
TYR   HH   H N N 415 
TYR   HXT  H N N 416 
VAL   N    N N N 417 
VAL   CA   C N S 418 
VAL   C    C N N 419 
VAL   O    O N N 420 
VAL   CB   C N N 421 
VAL   CG1  C N N 422 
VAL   CG2  C N N 423 
VAL   OXT  O N N 424 
VAL   H    H N N 425 
VAL   H2   H N N 426 
VAL   HA   H N N 427 
VAL   HB   H N N 428 
VAL   HG11 H N N 429 
VAL   HG12 H N N 430 
VAL   HG13 H N N 431 
VAL   HG21 H N N 432 
VAL   HG22 H N N 433 
VAL   HG23 H N N 434 
VAL   HXT  H N N 435 
# 
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 
A1A5D C1  C2   sing N N 1   
A1A5D C3  C2   sing N N 2   
A1A5D C3  N1   sing N N 3   
A1A5D C2  C14  sing N N 4   
A1A5D N1  C4   sing N N 5   
A1A5D C6  C7   doub Y N 6   
A1A5D C6  C5   sing Y N 7   
A1A5D C14 O3   doub N N 8   
A1A5D C14 O4   sing N N 9   
A1A5D C4  O1   doub N N 10  
A1A5D C4  C5   sing N N 11  
A1A5D C7  C8   sing Y N 12  
A1A5D C5  C13  doub Y N 13  
A1A5D C8  N2   sing N N 14  
A1A5D C8  C12  doub Y N 15  
A1A5D C13 C12  sing Y N 16  
A1A5D N2  C9   sing N N 17  
A1A5D C12 C11  sing N N 18  
A1A5D C9  O2   doub N N 19  
A1A5D C9  C10  sing N N 20  
A1A5D C11 C10  sing N N 21  
A1A5D N2  H10  sing N N 22  
A1A5D C3  H5   sing N N 23  
A1A5D C3  H6   sing N N 24  
A1A5D C6  H8   sing N N 25  
A1A5D C1  H2   sing N N 26  
A1A5D C1  H3   sing N N 27  
A1A5D C1  H4   sing N N 28  
A1A5D C10 H12  sing N N 29  
A1A5D C10 H11  sing N N 30  
A1A5D C11 H13  sing N N 31  
A1A5D C11 H14  sing N N 32  
A1A5D C13 H15  sing N N 33  
A1A5D C2  H1   sing N N 34  
A1A5D C7  H9   sing N N 35  
A1A5D N1  H7   sing N N 36  
A1A5D O4  H16  sing N N 37  
A1A5E O3  C14  doub N N 38  
A1A5E O4  C14  sing N N 39  
A1A5E C14 C2   sing N N 40  
A1A5E C3  C2   sing N N 41  
A1A5E C3  N1   sing N N 42  
A1A5E O1  C4   doub N N 43  
A1A5E C2  C1   sing N N 44  
A1A5E N1  C4   sing N N 45  
A1A5E C4  C5   sing N N 46  
A1A5E C5  C13  doub Y N 47  
A1A5E C5  C6   sing Y N 48  
A1A5E C13 C12  sing Y N 49  
A1A5E C6  C7   doub Y N 50  
A1A5E C12 C11  sing N N 51  
A1A5E C12 C8   doub Y N 52  
A1A5E C11 C10  sing N N 53  
A1A5E C7  C8   sing Y N 54  
A1A5E C8  N2   sing N N 55  
A1A5E C10 C9   sing N N 56  
A1A5E N2  C9   sing N N 57  
A1A5E C9  O2   doub N N 58  
A1A5E C1  H3   sing N N 59  
A1A5E C1  H2   sing N N 60  
A1A5E C1  H4   sing N N 61  
A1A5E C2  H1   sing N N 62  
A1A5E C3  H5   sing N N 63  
A1A5E C3  H6   sing N N 64  
A1A5E C6  H8   sing N N 65  
A1A5E C7  H9   sing N N 66  
A1A5E C10 H12  sing N N 67  
A1A5E C10 H11  sing N N 68  
A1A5E C11 H13  sing N N 69  
A1A5E C11 H14  sing N N 70  
A1A5E C13 H15  sing N N 71  
A1A5E N1  H7   sing N N 72  
A1A5E N2  H10  sing N N 73  
A1A5E O4  H16  sing N N 74  
ALA   N   CA   sing N N 75  
ALA   N   H    sing N N 76  
ALA   N   H2   sing N N 77  
ALA   CA  C    sing N N 78  
ALA   CA  CB   sing N N 79  
ALA   CA  HA   sing N N 80  
ALA   C   O    doub N N 81  
ALA   C   OXT  sing N N 82  
ALA   CB  HB1  sing N N 83  
ALA   CB  HB2  sing N N 84  
ALA   CB  HB3  sing N N 85  
ALA   OXT HXT  sing N N 86  
ARG   N   CA   sing N N 87  
ARG   N   H    sing N N 88  
ARG   N   H2   sing N N 89  
ARG   CA  C    sing N N 90  
ARG   CA  CB   sing N N 91  
ARG   CA  HA   sing N N 92  
ARG   C   O    doub N N 93  
ARG   C   OXT  sing N N 94  
ARG   CB  CG   sing N N 95  
ARG   CB  HB2  sing N N 96  
ARG   CB  HB3  sing N N 97  
ARG   CG  CD   sing N N 98  
ARG   CG  HG2  sing N N 99  
ARG   CG  HG3  sing N N 100 
ARG   CD  NE   sing N N 101 
ARG   CD  HD2  sing N N 102 
ARG   CD  HD3  sing N N 103 
ARG   NE  CZ   sing N N 104 
ARG   NE  HE   sing N N 105 
ARG   CZ  NH1  sing N N 106 
ARG   CZ  NH2  doub N N 107 
ARG   NH1 HH11 sing N N 108 
ARG   NH1 HH12 sing N N 109 
ARG   NH2 HH21 sing N N 110 
ARG   NH2 HH22 sing N N 111 
ARG   OXT HXT  sing N N 112 
ASN   N   CA   sing N N 113 
ASN   N   H    sing N N 114 
ASN   N   H2   sing N N 115 
ASN   CA  C    sing N N 116 
ASN   CA  CB   sing N N 117 
ASN   CA  HA   sing N N 118 
ASN   C   O    doub N N 119 
ASN   C   OXT  sing N N 120 
ASN   CB  CG   sing N N 121 
ASN   CB  HB2  sing N N 122 
ASN   CB  HB3  sing N N 123 
ASN   CG  OD1  doub N N 124 
ASN   CG  ND2  sing N N 125 
ASN   ND2 HD21 sing N N 126 
ASN   ND2 HD22 sing N N 127 
ASN   OXT HXT  sing N N 128 
ASP   N   CA   sing N N 129 
ASP   N   H    sing N N 130 
ASP   N   H2   sing N N 131 
ASP   CA  C    sing N N 132 
ASP   CA  CB   sing N N 133 
ASP   CA  HA   sing N N 134 
ASP   C   O    doub N N 135 
ASP   C   OXT  sing N N 136 
ASP   CB  CG   sing N N 137 
ASP   CB  HB2  sing N N 138 
ASP   CB  HB3  sing N N 139 
ASP   CG  OD1  doub N N 140 
ASP   CG  OD2  sing N N 141 
ASP   OD2 HD2  sing N N 142 
ASP   OXT HXT  sing N N 143 
CYS   N   CA   sing N N 144 
CYS   N   H    sing N N 145 
CYS   N   H2   sing N N 146 
CYS   CA  C    sing N N 147 
CYS   CA  CB   sing N N 148 
CYS   CA  HA   sing N N 149 
CYS   C   O    doub N N 150 
CYS   C   OXT  sing N N 151 
CYS   CB  SG   sing N N 152 
CYS   CB  HB2  sing N N 153 
CYS   CB  HB3  sing N N 154 
CYS   SG  HG   sing N N 155 
CYS   OXT HXT  sing N N 156 
GLN   N   CA   sing N N 157 
GLN   N   H    sing N N 158 
GLN   N   H2   sing N N 159 
GLN   CA  C    sing N N 160 
GLN   CA  CB   sing N N 161 
GLN   CA  HA   sing N N 162 
GLN   C   O    doub N N 163 
GLN   C   OXT  sing N N 164 
GLN   CB  CG   sing N N 165 
GLN   CB  HB2  sing N N 166 
GLN   CB  HB3  sing N N 167 
GLN   CG  CD   sing N N 168 
GLN   CG  HG2  sing N N 169 
GLN   CG  HG3  sing N N 170 
GLN   CD  OE1  doub N N 171 
GLN   CD  NE2  sing N N 172 
GLN   NE2 HE21 sing N N 173 
GLN   NE2 HE22 sing N N 174 
GLN   OXT HXT  sing N N 175 
GLU   N   CA   sing N N 176 
GLU   N   H    sing N N 177 
GLU   N   H2   sing N N 178 
GLU   CA  C    sing N N 179 
GLU   CA  CB   sing N N 180 
GLU   CA  HA   sing N N 181 
GLU   C   O    doub N N 182 
GLU   C   OXT  sing N N 183 
GLU   CB  CG   sing N N 184 
GLU   CB  HB2  sing N N 185 
GLU   CB  HB3  sing N N 186 
GLU   CG  CD   sing N N 187 
GLU   CG  HG2  sing N N 188 
GLU   CG  HG3  sing N N 189 
GLU   CD  OE1  doub N N 190 
GLU   CD  OE2  sing N N 191 
GLU   OE2 HE2  sing N N 192 
GLU   OXT HXT  sing N N 193 
GLY   N   CA   sing N N 194 
GLY   N   H    sing N N 195 
GLY   N   H2   sing N N 196 
GLY   CA  C    sing N N 197 
GLY   CA  HA2  sing N N 198 
GLY   CA  HA3  sing N N 199 
GLY   C   O    doub N N 200 
GLY   C   OXT  sing N N 201 
GLY   OXT HXT  sing N N 202 
HIS   N   CA   sing N N 203 
HIS   N   H    sing N N 204 
HIS   N   H2   sing N N 205 
HIS   CA  C    sing N N 206 
HIS   CA  CB   sing N N 207 
HIS   CA  HA   sing N N 208 
HIS   C   O    doub N N 209 
HIS   C   OXT  sing N N 210 
HIS   CB  CG   sing N N 211 
HIS   CB  HB2  sing N N 212 
HIS   CB  HB3  sing N N 213 
HIS   CG  ND1  sing Y N 214 
HIS   CG  CD2  doub Y N 215 
HIS   ND1 CE1  doub Y N 216 
HIS   ND1 HD1  sing N N 217 
HIS   CD2 NE2  sing Y N 218 
HIS   CD2 HD2  sing N N 219 
HIS   CE1 NE2  sing Y N 220 
HIS   CE1 HE1  sing N N 221 
HIS   NE2 HE2  sing N N 222 
HIS   OXT HXT  sing N N 223 
HOH   O   H1   sing N N 224 
HOH   O   H2   sing N N 225 
ILE   N   CA   sing N N 226 
ILE   N   H    sing N N 227 
ILE   N   H2   sing N N 228 
ILE   CA  C    sing N N 229 
ILE   CA  CB   sing N N 230 
ILE   CA  HA   sing N N 231 
ILE   C   O    doub N N 232 
ILE   C   OXT  sing N N 233 
ILE   CB  CG1  sing N N 234 
ILE   CB  CG2  sing N N 235 
ILE   CB  HB   sing N N 236 
ILE   CG1 CD1  sing N N 237 
ILE   CG1 HG12 sing N N 238 
ILE   CG1 HG13 sing N N 239 
ILE   CG2 HG21 sing N N 240 
ILE   CG2 HG22 sing N N 241 
ILE   CG2 HG23 sing N N 242 
ILE   CD1 HD11 sing N N 243 
ILE   CD1 HD12 sing N N 244 
ILE   CD1 HD13 sing N N 245 
ILE   OXT HXT  sing N N 246 
LEU   N   CA   sing N N 247 
LEU   N   H    sing N N 248 
LEU   N   H2   sing N N 249 
LEU   CA  C    sing N N 250 
LEU   CA  CB   sing N N 251 
LEU   CA  HA   sing N N 252 
LEU   C   O    doub N N 253 
LEU   C   OXT  sing N N 254 
LEU   CB  CG   sing N N 255 
LEU   CB  HB2  sing N N 256 
LEU   CB  HB3  sing N N 257 
LEU   CG  CD1  sing N N 258 
LEU   CG  CD2  sing N N 259 
LEU   CG  HG   sing N N 260 
LEU   CD1 HD11 sing N N 261 
LEU   CD1 HD12 sing N N 262 
LEU   CD1 HD13 sing N N 263 
LEU   CD2 HD21 sing N N 264 
LEU   CD2 HD22 sing N N 265 
LEU   CD2 HD23 sing N N 266 
LEU   OXT HXT  sing N N 267 
LYS   N   CA   sing N N 268 
LYS   N   H    sing N N 269 
LYS   N   H2   sing N N 270 
LYS   CA  C    sing N N 271 
LYS   CA  CB   sing N N 272 
LYS   CA  HA   sing N N 273 
LYS   C   O    doub N N 274 
LYS   C   OXT  sing N N 275 
LYS   CB  CG   sing N N 276 
LYS   CB  HB2  sing N N 277 
LYS   CB  HB3  sing N N 278 
LYS   CG  CD   sing N N 279 
LYS   CG  HG2  sing N N 280 
LYS   CG  HG3  sing N N 281 
LYS   CD  CE   sing N N 282 
LYS   CD  HD2  sing N N 283 
LYS   CD  HD3  sing N N 284 
LYS   CE  NZ   sing N N 285 
LYS   CE  HE2  sing N N 286 
LYS   CE  HE3  sing N N 287 
LYS   NZ  HZ1  sing N N 288 
LYS   NZ  HZ2  sing N N 289 
LYS   NZ  HZ3  sing N N 290 
LYS   OXT HXT  sing N N 291 
MET   N   CA   sing N N 292 
MET   N   H    sing N N 293 
MET   N   H2   sing N N 294 
MET   CA  C    sing N N 295 
MET   CA  CB   sing N N 296 
MET   CA  HA   sing N N 297 
MET   C   O    doub N N 298 
MET   C   OXT  sing N N 299 
MET   CB  CG   sing N N 300 
MET   CB  HB2  sing N N 301 
MET   CB  HB3  sing N N 302 
MET   CG  SD   sing N N 303 
MET   CG  HG2  sing N N 304 
MET   CG  HG3  sing N N 305 
MET   SD  CE   sing N N 306 
MET   CE  HE1  sing N N 307 
MET   CE  HE2  sing N N 308 
MET   CE  HE3  sing N N 309 
MET   OXT HXT  sing N N 310 
PHE   N   CA   sing N N 311 
PHE   N   H    sing N N 312 
PHE   N   H2   sing N N 313 
PHE   CA  C    sing N N 314 
PHE   CA  CB   sing N N 315 
PHE   CA  HA   sing N N 316 
PHE   C   O    doub N N 317 
PHE   C   OXT  sing N N 318 
PHE   CB  CG   sing N N 319 
PHE   CB  HB2  sing N N 320 
PHE   CB  HB3  sing N N 321 
PHE   CG  CD1  doub Y N 322 
PHE   CG  CD2  sing Y N 323 
PHE   CD1 CE1  sing Y N 324 
PHE   CD1 HD1  sing N N 325 
PHE   CD2 CE2  doub Y N 326 
PHE   CD2 HD2  sing N N 327 
PHE   CE1 CZ   doub Y N 328 
PHE   CE1 HE1  sing N N 329 
PHE   CE2 CZ   sing Y N 330 
PHE   CE2 HE2  sing N N 331 
PHE   CZ  HZ   sing N N 332 
PHE   OXT HXT  sing N N 333 
PRO   N   CA   sing N N 334 
PRO   N   CD   sing N N 335 
PRO   N   H    sing N N 336 
PRO   CA  C    sing N N 337 
PRO   CA  CB   sing N N 338 
PRO   CA  HA   sing N N 339 
PRO   C   O    doub N N 340 
PRO   C   OXT  sing N N 341 
PRO   CB  CG   sing N N 342 
PRO   CB  HB2  sing N N 343 
PRO   CB  HB3  sing N N 344 
PRO   CG  CD   sing N N 345 
PRO   CG  HG2  sing N N 346 
PRO   CG  HG3  sing N N 347 
PRO   CD  HD2  sing N N 348 
PRO   CD  HD3  sing N N 349 
PRO   OXT HXT  sing N N 350 
SER   N   CA   sing N N 351 
SER   N   H    sing N N 352 
SER   N   H2   sing N N 353 
SER   CA  C    sing N N 354 
SER   CA  CB   sing N N 355 
SER   CA  HA   sing N N 356 
SER   C   O    doub N N 357 
SER   C   OXT  sing N N 358 
SER   CB  OG   sing N N 359 
SER   CB  HB2  sing N N 360 
SER   CB  HB3  sing N N 361 
SER   OG  HG   sing N N 362 
SER   OXT HXT  sing N N 363 
THR   N   CA   sing N N 364 
THR   N   H    sing N N 365 
THR   N   H2   sing N N 366 
THR   CA  C    sing N N 367 
THR   CA  CB   sing N N 368 
THR   CA  HA   sing N N 369 
THR   C   O    doub N N 370 
THR   C   OXT  sing N N 371 
THR   CB  OG1  sing N N 372 
THR   CB  CG2  sing N N 373 
THR   CB  HB   sing N N 374 
THR   OG1 HG1  sing N N 375 
THR   CG2 HG21 sing N N 376 
THR   CG2 HG22 sing N N 377 
THR   CG2 HG23 sing N N 378 
THR   OXT HXT  sing N N 379 
TYR   N   CA   sing N N 380 
TYR   N   H    sing N N 381 
TYR   N   H2   sing N N 382 
TYR   CA  C    sing N N 383 
TYR   CA  CB   sing N N 384 
TYR   CA  HA   sing N N 385 
TYR   C   O    doub N N 386 
TYR   C   OXT  sing N N 387 
TYR   CB  CG   sing N N 388 
TYR   CB  HB2  sing N N 389 
TYR   CB  HB3  sing N N 390 
TYR   CG  CD1  doub Y N 391 
TYR   CG  CD2  sing Y N 392 
TYR   CD1 CE1  sing Y N 393 
TYR   CD1 HD1  sing N N 394 
TYR   CD2 CE2  doub Y N 395 
TYR   CD2 HD2  sing N N 396 
TYR   CE1 CZ   doub Y N 397 
TYR   CE1 HE1  sing N N 398 
TYR   CE2 CZ   sing Y N 399 
TYR   CE2 HE2  sing N N 400 
TYR   CZ  OH   sing N N 401 
TYR   OH  HH   sing N N 402 
TYR   OXT HXT  sing N N 403 
VAL   N   CA   sing N N 404 
VAL   N   H    sing N N 405 
VAL   N   H2   sing N N 406 
VAL   CA  C    sing N N 407 
VAL   CA  CB   sing N N 408 
VAL   CA  HA   sing N N 409 
VAL   C   O    doub N N 410 
VAL   C   OXT  sing N N 411 
VAL   CB  CG1  sing N N 412 
VAL   CB  CG2  sing N N 413 
VAL   CB  HB   sing N N 414 
VAL   CG1 HG11 sing N N 415 
VAL   CG1 HG12 sing N N 416 
VAL   CG1 HG13 sing N N 417 
VAL   CG2 HG21 sing N N 418 
VAL   CG2 HG22 sing N N 419 
VAL   CG2 HG23 sing N N 420 
VAL   OXT HXT  sing N N 421 
# 
_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                    7HCJ 
_atom_sites.fract_transf_matrix[1][1]   0.011265 
_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]   0.011265 
_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]   0.025240 
_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   ? 19.702 -16.335 22.313  0.78 46.26 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.663 -16.312 22.369  0.22 43.80 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.742 -15.249 22.473  0.78 45.74 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.724 -15.214 22.562  0.22 43.49 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.405 -13.908 22.180  0.78 44.10 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.389 -13.884 22.232  0.22 42.26 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.520 -13.646 22.634  0.78 44.49 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.504 -13.612 22.678  0.22 42.54 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.103 -15.269 23.878  0.78 46.43 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.155 -15.210 23.994  0.22 44.13 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 17.099 -14.132 24.029  0.78 46.61 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 17.175 -14.058 24.176  0.22 44.31 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.435 -16.612 24.138  0.78 46.55 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.485 -16.539 24.304  0.22 44.29 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 18.028 -15.366 21.831  0.78 54.90 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.979 -15.327 21.954  0.22 52.20 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.795 -15.146 24.546  0.78 55.73 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.881 -15.087 24.625  0.22 52.97 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.580 -14.275 24.837  0.78 55.94 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.693 -14.183 25.008  0.22 53.18 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.577 -13.291 24.090  0.78 55.94 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.667 -13.223 24.203  0.22 53.18 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.511 -14.126 23.258  0.78 55.94 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.552 -14.053 23.432  0.22 53.18 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 16.985 -16.580 24.997  0.78 55.87 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 17.077 -16.490 25.183  0.22 53.17 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.792 -16.784 23.433  0.78 55.87 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.806 -16.713 23.633  0.22 53.17 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.113 -17.305 24.145  0.78 55.87 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.154 -17.241 24.289  0.22 53.17 ?  3   VAL   A HG23 1 
ATOM   31   N N    A ASN   A 1 4   ? 18.719 -13.065 21.410  0.78 41.63 ?  4   ASN   A N    1 
ATOM   32   N N    B ASN   A 1 4   ? 18.701 -13.060 21.446  0.22 40.52 ?  4   ASN   A N    1 
ATOM   33   C CA   A ASN   A 1 4   ? 19.173 -11.712 21.118  0.78 38.90 ?  4   ASN   A CA   1 
ATOM   34   C CA   B ASN   A 1 4   ? 19.159 -11.716 21.122  0.22 38.61 ?  4   ASN   A CA   1 
ATOM   35   C C    A ASN   A 1 4   ? 18.026 -10.736 21.365  0.78 36.73 ?  4   ASN   A C    1 
ATOM   36   C C    B ASN   A 1 4   ? 18.018 -10.733 21.363  0.22 36.82 ?  4   ASN   A C    1 
ATOM   37   O O    A ASN   A 1 4   ? 16.904 -11.132 21.696  0.78 36.30 ?  4   ASN   A O    1 
ATOM   38   O O    B ASN   A 1 4   ? 16.893 -11.121 21.692  0.22 36.86 ?  4   ASN   A O    1 
ATOM   39   C CB   A ASN   A 1 4   ? 19.735 -11.593 19.694  0.78 38.15 ?  4   ASN   A CB   1 
ATOM   40   C CB   B ASN   A 1 4   ? 19.708 -11.630 19.691  0.22 38.28 ?  4   ASN   A CB   1 
ATOM   41   C CG   A ASN   A 1 4   ? 18.721 -11.955 18.628  0.78 37.25 ?  4   ASN   A CG   1 
ATOM   42   C CG   B ASN   A 1 4   ? 18.683 -12.009 18.643  0.22 37.93 ?  4   ASN   A CG   1 
ATOM   43   O OD1  A ASN   A 1 4   ? 17.614 -11.417 18.597  0.78 36.91 ?  4   ASN   A OD1  1 
ATOM   44   O OD1  B ASN   A 1 4   ? 17.582 -11.459 18.602  0.22 37.84 ?  4   ASN   A OD1  1 
ATOM   45   N ND2  A ASN   A 1 4   ? 19.097 -12.874 17.743  0.78 36.93 ?  4   ASN   A ND2  1 
ATOM   46   N ND2  B ASN   A 1 4   ? 19.042 -12.958 17.785  0.22 37.82 ?  4   ASN   A ND2  1 
ATOM   47   H H    A ASN   A 1 4   ? 17.969 -13.263 21.036  0.78 49.97 ?  4   ASN   A H    1 
ATOM   48   H H    B ASN   A 1 4   ? 17.945 -13.263 21.084  0.22 48.64 ?  4   ASN   A H    1 
ATOM   49   H HA   A ASN   A 1 4   ? 19.890 -11.491 21.730  0.78 46.69 ?  4   ASN   A HA   1 
ATOM   50   H HA   B ASN   A 1 4   ? 19.882 -11.486 21.722  0.22 46.34 ?  4   ASN   A HA   1 
ATOM   51   H HB2  A ASN   A 1 4   ? 20.015 -10.676 19.542  0.78 45.80 ?  4   ASN   A HB2  1 
ATOM   52   H HB2  B ASN   A 1 4   ? 19.994 -10.717 19.518  0.22 45.95 ?  4   ASN   A HB2  1 
ATOM   53   H HB3  A ASN   A 1 4   ? 20.492 -12.191 19.605  0.78 45.80 ?  4   ASN   A HB3  1 
ATOM   54   H HB3  B ASN   A 1 4   ? 20.463 -12.233 19.607  0.22 45.95 ?  4   ASN   A HB3  1 
ATOM   55   H HD21 A ASN   A 1 4   ? 18.560 -13.115 17.116  0.78 44.33 ?  4   ASN   A HD21 1 
ATOM   56   H HD21 B ASN   A 1 4   ? 18.498 -13.209 17.168  0.22 45.40 ?  4   ASN   A HD21 1 
ATOM   57   H HD22 A ASN   A 1 4   ? 19.881 -13.226 17.796  0.78 44.33 ?  4   ASN   A HD22 1 
ATOM   58   H HD22 B ASN   A 1 4   ? 19.819 -13.322 17.846  0.22 45.40 ?  4   ASN   A HD22 1 
ATOM   59   N N    . SER   A 1 5   ? 18.314 -9.446  21.195  1.00 34.71 ?  5   SER   A N    1 
ATOM   60   C CA   . SER   A 1 5   ? 17.389 -8.381  21.564  1.00 31.01 ?  5   SER   A CA   1 
ATOM   61   C C    . SER   A 1 5   ? 16.484 -7.918  20.425  1.00 26.39 ?  5   SER   A C    1 
ATOM   62   O O    . SER   A 1 5   ? 15.774 -6.922  20.591  1.00 26.77 ?  5   SER   A O    1 
ATOM   63   C CB   . SER   A 1 5   ? 18.156 -7.186  22.137  1.00 32.31 ?  5   SER   A CB   1 
ATOM   64   O OG   . SER   A 1 5   ? 19.098 -6.695  21.202  1.00 32.65 ?  5   SER   A OG   1 
ATOM   65   H H    A SER   A 1 5   ? 19.052 -9.160  20.859  0.78 41.67 ?  5   SER   A H    1 
ATOM   66   H H    B SER   A 1 5   ? 19.055 -9.162  20.864  0.22 41.67 ?  5   SER   A H    1 
ATOM   67   H HA   . SER   A 1 5   ? 16.812 -8.709  22.268  1.00 37.22 ?  5   SER   A HA   1 
ATOM   68   H HB2  . SER   A 1 5   ? 17.528 -6.475  22.353  1.00 38.79 ?  5   SER   A HB2  1 
ATOM   69   H HB3  . SER   A 1 5   ? 18.624 -7.463  22.942  1.00 38.79 ?  5   SER   A HB3  1 
ATOM   70   H HG   . SER   A 1 5   ? 19.514 -6.040  21.530  1.00 39.19 ?  5   SER   A HG   1 
ATOM   71   N N    A PHE   A 1 6   ? 16.538 -8.574  19.268  0.78 22.81 ?  6   PHE   A N    1 
ATOM   72   N N    B PHE   A 1 6   ? 16.430 -8.635  19.309  0.22 25.06 ?  6   PHE   A N    1 
ATOM   73   C CA   A PHE   A 1 6   ? 15.669 -8.200  18.160  0.78 19.95 ?  6   PHE   A CA   1 
ATOM   74   C CA   B PHE   A 1 6   ? 15.471 -8.295  18.265  0.22 23.65 ?  6   PHE   A CA   1 
ATOM   75   C C    A PHE   A 1 6   ? 14.227 -8.552  18.512  0.78 20.40 ?  6   PHE   A C    1 
ATOM   76   C C    B PHE   A 1 6   ? 14.075 -8.764  18.661  0.22 23.55 ?  6   PHE   A C    1 
ATOM   77   O O    A PHE   A 1 6   ? 13.939 -9.678  18.927  0.78 21.44 ?  6   PHE   A O    1 
ATOM   78   O O    B PHE   A 1 6   ? 13.902 -9.864  19.193  0.22 23.95 ?  6   PHE   A O    1 
ATOM   79   C CB   A PHE   A 1 6   ? 16.097 -8.925  16.884  0.78 17.87 ?  6   PHE   A CB   1 
ATOM   80   C CB   B PHE   A 1 6   ? 15.877 -8.920  16.933  0.22 22.35 ?  6   PHE   A CB   1 
ATOM   81   C CG   A PHE   A 1 6   ? 17.379 -8.401  16.279  0.78 16.40 ?  6   PHE   A CG   1 
ATOM   82   C CG   B PHE   A 1 6   ? 17.099 -8.298  16.323  0.22 21.18 ?  6   PHE   A CG   1 
ATOM   83   C CD1  A PHE   A 1 6   ? 17.395 -7.203  15.584  0.78 16.22 ?  6   PHE   A CD1  1 
ATOM   84   C CD1  B PHE   A 1 6   ? 17.027 -7.058  15.708  0.22 20.74 ?  6   PHE   A CD1  1 
ATOM   85   C CD2  A PHE   A 1 6   ? 18.560 -9.121  16.388  0.78 16.96 ?  6   PHE   A CD2  1 
ATOM   86   C CD2  B PHE   A 1 6   ? 18.318 -8.952  16.364  0.22 20.81 ?  6   PHE   A CD2  1 
ATOM   87   C CE1  A PHE   A 1 6   ? 18.567 -6.725  15.021  0.78 16.24 ?  6   PHE   A CE1  1 
ATOM   88   C CE1  B PHE   A 1 6   ? 18.151 -6.483  15.146  0.22 20.48 ?  6   PHE   A CE1  1 
ATOM   89   C CE2  A PHE   A 1 6   ? 19.733 -8.649  15.827  0.78 17.13 ?  6   PHE   A CE2  1 
ATOM   90   C CE2  B PHE   A 1 6   ? 19.443 -8.382  15.803  0.22 20.51 ?  6   PHE   A CE2  1 
ATOM   91   C CZ   A PHE   A 1 6   ? 19.737 -7.449  15.141  0.78 16.84 ?  6   PHE   A CZ   1 
ATOM   92   C CZ   B PHE   A 1 6   ? 19.360 -7.146  15.194  0.22 20.42 ?  6   PHE   A CZ   1 
ATOM   93   H H    A PHE   A 1 6   ? 17.058 -9.238  19.105  0.78 27.39 ?  6   PHE   A H    1 
ATOM   94   H H    B PHE   A 1 6   ? 16.924 -9.317  19.135  0.22 30.09 ?  6   PHE   A H    1 
ATOM   95   H HA   A PHE   A 1 6   ? 15.727 -7.248  18.010  0.78 23.96 ?  6   PHE   A HA   1 
ATOM   96   H HA   B PHE   A 1 6   ? 15.446 -7.334  18.156  0.22 28.39 ?  6   PHE   A HA   1 
ATOM   97   H HB2  A PHE   A 1 6   ? 16.227 -9.867  17.088  0.78 21.46 ?  6   PHE   A HB2  1 
ATOM   98   H HB2  B PHE   A 1 6   ? 16.062 -9.862  17.071  0.22 26.84 ?  6   PHE   A HB2  1 
ATOM   99   H HB3  A PHE   A 1 6   ? 15.396 -8.831  16.221  0.78 21.46 ?  6   PHE   A HB3  1 
ATOM   100  H HB3  B PHE   A 1 6   ? 15.146 -8.818  16.303  0.22 26.84 ?  6   PHE   A HB3  1 
ATOM   101  H HD1  A PHE   A 1 6   ? 16.610 -6.713  15.499  0.78 19.48 ?  6   PHE   A HD1  1 
ATOM   102  H HD1  B PHE   A 1 6   ? 16.213 -6.607  15.674  0.22 24.90 ?  6   PHE   A HD1  1 
ATOM   103  H HD2  A PHE   A 1 6   ? 18.565 -9.931  16.850  0.78 20.37 ?  6   PHE   A HD2  1 
ATOM   104  H HD2  B PHE   A 1 6   ? 18.377 -9.784  16.774  0.22 24.99 ?  6   PHE   A HD2  1 
ATOM   105  H HE1  A PHE   A 1 6   ? 18.569 -5.919  14.560  0.78 19.51 ?  6   PHE   A HE1  1 
ATOM   106  H HE1  B PHE   A 1 6   ? 18.091 -5.650  14.736  0.22 24.59 ?  6   PHE   A HE1  1 
ATOM   107  H HE2  A PHE   A 1 6   ? 20.521 -9.140  15.913  0.78 20.57 ?  6   PHE   A HE2  1 
ATOM   108  H HE2  B PHE   A 1 6   ? 20.257 -8.832  15.838  0.22 24.62 ?  6   PHE   A HE2  1 
ATOM   109  H HZ   A PHE   A 1 6   ? 20.528 -7.132  14.766  0.78 20.22 ?  6   PHE   A HZ   1 
ATOM   110  H HZ   B PHE   A 1 6   ? 20.117 -6.761  14.816  0.22 24.52 ?  6   PHE   A HZ   1 
ATOM   111  N N    A SER   A 1 7   ? 13.320 -7.589  18.351  0.78 20.05 ?  7   SER   A N    1 
ATOM   112  N N    B SER   A 1 7   ? 13.077 -7.917  18.403  0.22 22.96 ?  7   SER   A N    1 
ATOM   113  C CA   A SER   A 1 7   ? 11.957 -7.711  18.850  0.78 20.76 ?  7   SER   A CA   1 
ATOM   114  C CA   B SER   A 1 7   ? 11.701 -8.203  18.788  0.22 22.37 ?  7   SER   A CA   1 
ATOM   115  C C    A SER   A 1 7   ? 10.949 -7.458  17.737  0.78 19.51 ?  7   SER   A C    1 
ATOM   116  C C    B SER   A 1 7   ? 10.743 -7.723  17.708  0.22 21.43 ?  7   SER   A C    1 
ATOM   117  O O    A SER   A 1 7   ? 11.153 -6.584  16.890  0.78 19.54 ?  7   SER   A O    1 
ATOM   118  O O    B SER   A 1 7   ? 10.983 -6.708  17.048  0.22 21.39 ?  7   SER   A O    1 
ATOM   119  C CB   A SER   A 1 7   ? 11.723 -6.713  19.992  0.78 22.87 ?  7   SER   A CB   1 
ATOM   120  C CB   B SER   A 1 7   ? 11.343 -7.529  20.121  0.22 22.71 ?  7   SER   A CB   1 
ATOM   121  O OG   A SER   A 1 7   ? 10.383 -6.758  20.439  0.78 24.64 ?  7   SER   A OG   1 
ATOM   122  O OG   B SER   A 1 7   ? 9.954  -7.632  20.387  0.22 22.95 ?  7   SER   A OG   1 
ATOM   123  H H    A SER   A 1 7   ? 13.476 -6.844  17.944  0.78 24.07 ?  7   SER   A H    1 
ATOM   124  H H    B SER   A 1 7   ? 13.175 -7.159  18.004  0.22 27.57 ?  7   SER   A H    1 
ATOM   125  H HA   A SER   A 1 7   ? 11.815 -8.604  19.191  0.78 24.93 ?  7   SER   A HA   1 
ATOM   126  H HA   B SER   A 1 7   ? 11.585 -9.158  18.894  0.22 26.86 ?  7   SER   A HA   1 
ATOM   127  H HB2  A SER   A 1 7   ? 12.311 -6.936  20.733  0.78 27.46 ?  7   SER   A HB2  1 
ATOM   128  H HB2  B SER   A 1 7   ? 11.833 -7.965  20.836  0.22 27.26 ?  7   SER   A HB2  1 
ATOM   129  H HB3  A SER   A 1 7   ? 11.920 -5.817  19.676  0.78 27.46 ?  7   SER   A HB3  1 
ATOM   130  H HB3  B SER   A 1 7   ? 11.585 -6.591  20.079  0.22 27.26 ?  7   SER   A HB3  1 
ATOM   131  H HG   A SER   A 1 7   ? 10.268 -6.209  21.064  0.78 29.58 ?  7   SER   A HG   1 
ATOM   132  H HG   B SER   A 1 7   ? 9.726  -8.439  20.434  0.22 27.56 ?  7   SER   A HG   1 
ATOM   133  N N    A GLY   A 1 8   ? 9.860  -8.226  17.747  0.78 18.77 ?  8   GLY   A N    1 
ATOM   134  N N    B GLY   A 1 8   ? 9.647  -8.470  17.534  0.22 20.58 ?  8   GLY   A N    1 
ATOM   135  C CA   A GLY   A 1 8   ? 8.771  -7.993  16.825  0.78 18.40 ?  8   GLY   A CA   1 
ATOM   136  C CA   B GLY   A 1 8   ? 8.578  -8.090  16.634  0.22 19.96 ?  8   GLY   A CA   1 
ATOM   137  C C    A GLY   A 1 8   ? 8.971  -8.508  15.420  0.78 17.35 ?  8   GLY   A C    1 
ATOM   138  C C    B GLY   A 1 8   ? 8.724  -8.571  15.209  0.22 19.14 ?  8   GLY   A C    1 
ATOM   139  O O    A GLY   A 1 8   ? 8.238  -8.089  14.516  0.78 18.16 ?  8   GLY   A O    1 
ATOM   140  O O    B GLY   A 1 8   ? 7.790  -8.397  14.416  0.22 19.02 ?  8   GLY   A O    1 
ATOM   141  H H    A GLY   A 1 8   ? 9.741  -8.882  18.280  0.78 22.53 ?  8   GLY   A H    1 
ATOM   142  H H    B GLY   A 1 8   ? 9.503  -9.219  17.935  0.22 24.71 ?  8   GLY   A H    1 
ATOM   143  H HA2  A GLY   A 1 8   ? 7.974  -8.413  17.180  0.78 22.09 ?  8   GLY   A HA2  1 
ATOM   144  H HA2  B GLY   A 1 8   ? 7.735  -8.420  16.986  0.22 23.96 ?  8   GLY   A HA2  1 
ATOM   145  H HA3  A GLY   A 1 8   ? 8.607  -7.040  16.766  0.78 22.09 ?  8   GLY   A HA3  1 
ATOM   146  H HA3  B GLY   A 1 8   ? 8.528  -7.126  16.589  0.22 23.96 ?  8   GLY   A HA3  1 
ATOM   147  N N    A TYR   A 1 9   ? 9.945  -9.391  15.195  0.78 15.92 ?  9   TYR   A N    1 
ATOM   148  N N    B TYR   A 1 9   ? 9.860  -9.161  14.852  0.22 18.73 ?  9   TYR   A N    1 
ATOM   149  C CA   A TYR   A 1 9   ? 10.204 -9.926  13.864  0.78 14.42 ?  9   TYR   A CA   1 
ATOM   150  C CA   B TYR   A 1 9   ? 10.103 -9.561  13.474  0.22 18.27 ?  9   TYR   A CA   1 
ATOM   151  C C    A TYR   A 1 9   ? 9.318  -11.130 13.569  0.78 14.61 ?  9   TYR   A C    1 
ATOM   152  C C    B TYR   A 1 9   ? 9.288  -10.803 13.128  0.22 18.46 ?  9   TYR   A C    1 
ATOM   153  O O    A TYR   A 1 9   ? 8.979  -11.918 14.457  0.78 15.61 ?  9   TYR   A O    1 
ATOM   154  O O    B TYR   A 1 9   ? 9.400  -11.837 13.797  0.22 18.98 ?  9   TYR   A O    1 
ATOM   155  C CB   A TYR   A 1 9   ? 11.680 -10.327 13.699  0.78 14.27 ?  9   TYR   A CB   1 
ATOM   156  C CB   B TYR   A 1 9   ? 11.593 -9.830  13.275  0.22 17.61 ?  9   TYR   A CB   1 
ATOM   157  C CG   A TYR   A 1 9   ? 12.594 -9.137  13.534  0.78 13.66 ?  9   TYR   A CG   1 
ATOM   158  C CG   B TYR   A 1 9   ? 12.467 -8.593  13.253  0.22 17.26 ?  9   TYR   A CG   1 
ATOM   159  C CD1  A TYR   A 1 9   ? 12.923 -8.346  14.622  0.78 13.76 ?  9   TYR   A CD1  1 
ATOM   160  C CD1  B TYR   A 1 9   ? 12.649 -7.821  14.392  0.22 17.18 ?  9   TYR   A CD1  1 
ATOM   161  C CD2  A TYR   A 1 9   ? 13.100 -8.787  12.288  0.78 13.27 ?  9   TYR   A CD2  1 
ATOM   162  C CD2  B TYR   A 1 9   ? 13.119 -8.203  12.088  0.22 16.98 ?  9   TYR   A CD2  1 
ATOM   163  C CE1  A TYR   A 1 9   ? 13.735 -7.241  14.481  0.78 13.94 ?  9   TYR   A CE1  1 
ATOM   164  C CE1  B TYR   A 1 9   ? 13.445 -6.692  14.370  0.22 17.01 ?  9   TYR   A CE1  1 
ATOM   165  C CE2  A TYR   A 1 9   ? 13.914 -7.682  12.134  0.78 13.23 ?  9   TYR   A CE2  1 
ATOM   166  C CE2  B TYR   A 1 9   ? 13.917 -7.075  12.057  0.22 16.72 ?  9   TYR   A CE2  1 
ATOM   167  C CZ   A TYR   A 1 9   ? 14.222 -6.911  13.233  0.78 14.13 ?  9   TYR   A CZ   1 
ATOM   168  C CZ   B TYR   A 1 9   ? 14.077 -6.326  13.201  0.22 16.82 ?  9   TYR   A CZ   1 
ATOM   169  O OH   A TYR   A 1 9   ? 15.023 -5.813  13.081  0.78 15.40 ?  9   TYR   A OH   1 
ATOM   170  O OH   B TYR   A 1 9   ? 14.870 -5.203  13.175  0.22 17.03 ?  9   TYR   A OH   1 
ATOM   171  H H    A TYR   A 1 9   ? 10.481 -9.691  15.800  0.78 19.12 ?  9   TYR   A H    1 
ATOM   172  H H    B TYR   A 1 9   ? 10.509 -9.333  15.383  0.22 22.49 ?  9   TYR   A H    1 
ATOM   173  H HA   A TYR   A 1 9   ? 10.015 -9.237  13.205  0.78 17.32 ?  9   TYR   A HA   1 
ATOM   174  H HA   B TYR   A 1 9   ? 9.837  -8.851  12.871  0.22 21.94 ?  9   TYR   A HA   1 
ATOM   175  H HB2  A TYR   A 1 9   ? 11.965 -10.822 14.483  0.78 17.14 ?  9   TYR   A HB2  1 
ATOM   176  H HB2  B TYR   A 1 9   ? 11.922 -10.437 13.963  0.22 21.15 ?  9   TYR   A HB2  1 
ATOM   177  H HB3  A TYR   A 1 9   ? 11.763 -10.883 12.908  0.78 17.14 ?  9   TYR   A HB3  1 
ATOM   178  H HB3  B TYR   A 1 9   ? 11.679 -10.225 12.402  0.22 21.15 ?  9   TYR   A HB3  1 
ATOM   179  H HD1  A TYR   A 1 9   ? 12.583 -8.559  15.460  0.78 16.53 ?  9   TYR   A HD1  1 
ATOM   180  H HD1  B TYR   A 1 9   ? 12.227 -8.065  15.182  0.22 20.63 ?  9   TYR   A HD1  1 
ATOM   181  H HD2  A TYR   A 1 9   ? 12.887 -9.309  11.545  0.78 15.94 ?  9   TYR   A HD2  1 
ATOM   182  H HD2  B TYR   A 1 9   ? 13.015 -8.706  11.312  0.22 20.39 ?  9   TYR   A HD2  1 
ATOM   183  H HE1  A TYR   A 1 9   ? 13.945 -6.718  15.218  0.78 16.74 ?  9   TYR   A HE1  1 
ATOM   184  H HE1  B TYR   A 1 9   ? 13.558 -6.182  15.140  0.22 20.42 ?  9   TYR   A HE1  1 
ATOM   185  H HE2  A TYR   A 1 9   ? 14.254 -7.465  11.294  0.78 15.89 ?  9   TYR   A HE2  1 
ATOM   186  H HE2  B TYR   A 1 9   ? 14.346 -6.822  11.270  0.22 20.08 ?  9   TYR   A HE2  1 
ATOM   187  H HH   A TYR   A 1 9   ? 15.148 -5.441  13.826  0.78 18.49 ?  9   TYR   A HH   1 
ATOM   188  H HH   B TYR   A 1 9   ? 14.879 -4.838  13.932  0.22 20.44 ?  9   TYR   A HH   1 
ATOM   189  N N    A LEU   A 1 10  ? 8.954  -11.272 12.296  0.78 13.95 ?  10  LEU   A N    1 
ATOM   190  N N    B LEU   A 1 10  ? 8.458  -10.695 12.091  0.22 18.27 ?  10  LEU   A N    1 
ATOM   191  C CA   A LEU   A 1 10  ? 8.313  -12.481 11.800  0.78 13.73 ?  10  LEU   A CA   1 
ATOM   192  C CA   B LEU   A 1 10  ? 7.800  -11.867 11.530  0.22 17.83 ?  10  LEU   A CA   1 
ATOM   193  C C    A LEU   A 1 10  ? 9.412  -13.433 11.330  0.78 12.45 ?  10  LEU   A C    1 
ATOM   194  C C    B LEU   A 1 10  ? 8.845  -12.896 11.122  0.22 17.11 ?  10  LEU   A C    1 
ATOM   195  O O    A LEU   A 1 10  ? 10.338 -13.024 10.624  0.78 12.71 ?  10  LEU   A O    1 
ATOM   196  O O    B LEU   A 1 10  ? 9.941  -12.548 10.676  0.22 16.87 ?  10  LEU   A O    1 
ATOM   197  C CB   A LEU   A 1 10  ? 7.370  -12.129 10.647  0.78 15.18 ?  10  LEU   A CB   1 
ATOM   198  C CB   B LEU   A 1 10  ? 6.977  -11.461 10.302  0.22 18.47 ?  10  LEU   A CB   1 
ATOM   199  C CG   A LEU   A 1 10  ? 6.668  -13.307 9.960   0.78 18.03 ?  10  LEU   A CG   1 
ATOM   200  C CG   B LEU   A 1 10  ? 5.499  -11.124 10.510  0.22 19.03 ?  10  LEU   A CG   1 
ATOM   201  C CD1  A LEU   A 1 10  ? 5.609  -13.936 10.859  0.78 20.08 ?  10  LEU   A CD1  1 
ATOM   202  C CD1  B LEU   A 1 10  ? 4.802  -10.909 9.184   0.22 19.21 ?  10  LEU   A CD1  1 
ATOM   203  C CD2  A LEU   A 1 10  ? 6.072  -12.887 8.622   0.78 19.91 ?  10  LEU   A CD2  1 
ATOM   204  C CD2  B LEU   A 1 10  ? 4.836  -12.247 11.248  0.22 19.42 ?  10  LEU   A CD2  1 
ATOM   205  H H    A LEU   A 1 10  ? 9.081  -10.665 11.687  0.78 16.75 ?  10  LEU   A H    1 
ATOM   206  H H    B LEU   A 1 10  ? 8.255  -9.956  11.702  0.22 21.94 ?  10  LEU   A H    1 
ATOM   207  H HA   A LEU   A 1 10  ? 7.804  -12.895 12.512  0.78 16.49 ?  10  LEU   A HA   1 
ATOM   208  H HA   B LEU   A 1 10  ? 7.223  -12.268 12.197  0.22 21.41 ?  10  LEU   A HA   1 
ATOM   209  H HB2  A LEU   A 1 10  ? 6.676  -11.539 10.987  0.78 18.23 ?  10  LEU   A HB2  1 
ATOM   210  H HB2  B LEU   A 1 10  ? 7.390  -10.675 9.908   0.22 22.18 ?  10  LEU   A HB2  1 
ATOM   211  H HB3  A LEU   A 1 10  ? 7.879  -11.662 9.967   0.78 18.23 ?  10  LEU   A HB3  1 
ATOM   212  H HB3  B LEU   A 1 10  ? 7.008  -12.188 9.663   0.22 22.18 ?  10  LEU   A HB3  1 
ATOM   213  H HG   A LEU   A 1 10  ? 7.328  -13.992 9.778   0.78 21.65 ?  10  LEU   A HG   1 
ATOM   214  H HG   B LEU   A 1 10  ? 5.416  -10.309 11.035  0.22 22.86 ?  10  LEU   A HG   1 
ATOM   215  H HD11 A LEU   A 1 10  ? 5.260  -14.732 10.428  0.78 24.11 ?  10  LEU   A HD11 1 
ATOM   216  H HD11 B LEU   A 1 10  ? 3.877  -10.664 9.349   0.22 23.07 ?  10  LEU   A HD11 1 
ATOM   217  H HD12 A LEU   A 1 10  ? 6.015  -14.173 11.709  0.78 24.11 ?  10  LEU   A HD12 1 
ATOM   218  H HD12 B LEU   A 1 10  ? 5.253  -10.203 8.701   0.22 23.07 ?  10  LEU   A HD12 1 
ATOM   219  H HD13 A LEU   A 1 10  ? 4.895  -13.296 11.003  0.78 24.11 ?  10  LEU   A HD13 1 
ATOM   220  H HD13 B LEU   A 1 10  ? 4.838  -11.736 8.676   0.22 23.07 ?  10  LEU   A HD13 1 
ATOM   221  H HD21 A LEU   A 1 10  ? 5.637  -13.655 8.221   0.78 23.91 ?  10  LEU   A HD21 1 
ATOM   222  H HD21 B LEU   A 1 10  ? 3.880  -12.132 11.193  0.22 23.32 ?  10  LEU   A HD21 1 
ATOM   223  H HD22 A LEU   A 1 10  ? 5.429  -12.180 8.773   0.78 23.91 ?  10  LEU   A HD22 1 
ATOM   224  H HD22 B LEU   A 1 10  ? 5.100  -13.081 10.831  0.22 23.32 ?  10  LEU   A HD22 1 
ATOM   225  H HD23 A LEU   A 1 10  ? 6.788  -12.573 8.049   0.78 23.91 ?  10  LEU   A HD23 1 
ATOM   226  H HD23 B LEU   A 1 10  ? 5.125  -12.231 12.170  0.22 23.32 ?  10  LEU   A HD23 1 
ATOM   227  N N    A LYS   A 1 11  ? 9.320  -14.688 11.740  0.78 12.69 ?  11  LYS   A N    1 
ATOM   228  N N    B LYS   A 1 11  ? 8.508  -14.171 11.284  0.22 16.74 ?  11  LYS   A N    1 
ATOM   229  C CA   A LYS   A 1 11  ? 10.306 -15.693 11.363  0.78 12.32 ?  11  LYS   A CA   1 
ATOM   230  C CA   B LYS   A 1 11  ? 9.425  -15.259 10.974  0.22 16.10 ?  11  LYS   A CA   1 
ATOM   231  C C    A LYS   A 1 11  ? 9.931  -16.265 10.004  0.78 12.03 ?  11  LYS   A C    1 
ATOM   232  C C    B LYS   A 1 11  ? 9.129  -15.793 9.578   0.22 15.83 ?  11  LYS   A C    1 
ATOM   233  O O    A LYS   A 1 11  ? 8.852  -16.841 9.859   0.78 13.95 ?  11  LYS   A O    1 
ATOM   234  O O    B LYS   A 1 11  ? 8.024  -16.282 9.315   0.22 15.74 ?  11  LYS   A O    1 
ATOM   235  C CB   A LYS   A 1 11  ? 10.325 -16.785 12.429  0.78 12.59 ?  11  LYS   A CB   1 
ATOM   236  C CB   B LYS   A 1 11  ? 9.308  -16.377 12.007  0.22 16.02 ?  11  LYS   A CB   1 
ATOM   237  C CG   A LYS   A 1 11  ? 11.335 -17.900 12.206  0.78 12.60 ?  11  LYS   A CG   1 
ATOM   238  C CG   B LYS   A 1 11  ? 10.360 -17.458 11.851  0.22 16.11 ?  11  LYS   A CG   1 
ATOM   239  C CD   A LYS   A 1 11  ? 11.438 -18.749 13.475  0.78 12.88 ?  11  LYS   A CD   1 
ATOM   240  C CD   B LYS   A 1 11  ? 10.247 -18.516 12.936  0.22 16.09 ?  11  LYS   A CD   1 
ATOM   241  C CE   A LYS   A 1 11  ? 12.413 -19.901 13.335  0.78 13.02 ?  11  LYS   A CE   1 
ATOM   242  C CE   B LYS   A 1 11  ? 11.350 -19.553 12.804  0.22 15.99 ?  11  LYS   A CE   1 
ATOM   243  N NZ   A LYS   A 1 11  ? 13.787 -19.441 13.035  0.78 13.17 ?  11  LYS   A NZ   1 
ATOM   244  N NZ   B LYS   A 1 11  ? 12.706 -18.938 12.842  0.22 15.92 ?  11  LYS   A NZ   1 
ATOM   245  H H    A LYS   A 1 11  ? 8.680  -14.981 12.240  0.78 15.25 ?  11  LYS   A H    1 
ATOM   246  H H    B LYS   A 1 11  ? 7.746  -14.432 11.589  0.22 20.10 ?  11  LYS   A H    1 
ATOM   247  H HA   A LYS   A 1 11  ? 11.176 -15.285 11.303  0.78 14.80 ?  11  LYS   A HA   1 
ATOM   248  H HA   B LYS   A 1 11  ? 10.335 -14.921 10.988  0.22 19.33 ?  11  LYS   A HA   1 
ATOM   249  H HB2  A LYS   A 1 11  ? 10.525 -16.370 13.282  0.78 15.12 ?  11  LYS   A HB2  1 
ATOM   250  H HB2  B LYS   A 1 11  ? 9.402  -15.993 12.893  0.22 19.23 ?  11  LYS   A HB2  1 
ATOM   251  H HB3  A LYS   A 1 11  ? 9.439  -17.187 12.469  0.78 15.12 ?  11  LYS   A HB3  1 
ATOM   252  H HB3  B LYS   A 1 11  ? 8.437  -16.790 11.918  0.22 19.23 ?  11  LYS   A HB3  1 
ATOM   253  H HG2  A LYS   A 1 11  ? 11.031 -18.468 11.476  0.78 15.13 ?  11  LYS   A HG2  1 
ATOM   254  H HG2  B LYS   A 1 11  ? 10.248 -17.893 10.992  0.22 19.35 ?  11  LYS   A HG2  1 
ATOM   255  H HG3  A LYS   A 1 11  ? 12.199 -17.521 12.011  0.78 15.13 ?  11  LYS   A HG3  1 
ATOM   256  H HG3  B LYS   A 1 11  ? 11.239 -17.053 11.910  0.22 19.35 ?  11  LYS   A HG3  1 
ATOM   257  H HD2  A LYS   A 1 11  ? 11.734 -18.182 14.203  0.78 15.48 ?  11  LYS   A HD2  1 
ATOM   258  H HD2  B LYS   A 1 11  ? 10.325 -18.095 13.807  0.22 19.32 ?  11  LYS   A HD2  1 
ATOM   259  H HD3  A LYS   A 1 11  ? 10.559 -19.115 13.678  0.78 15.48 ?  11  LYS   A HD3  1 
ATOM   260  H HD3  B LYS   A 1 11  ? 9.391  -18.967 12.857  0.22 19.32 ?  11  LYS   A HD3  1 
ATOM   261  H HE2  A LYS   A 1 11  ? 12.434 -20.396 14.169  0.78 15.64 ?  11  LYS   A HE2  1 
ATOM   262  H HE2  B LYS   A 1 11  ? 11.284 -20.184 13.538  0.22 19.20 ?  11  LYS   A HE2  1 
ATOM   263  H HE3  A LYS   A 1 11  ? 12.119 -20.478 12.613  0.78 15.64 ?  11  LYS   A HE3  1 
ATOM   264  H HE3  B LYS   A 1 11  ? 11.252 -20.014 11.957  0.22 19.20 ?  11  LYS   A HE3  1 
ATOM   265  H HZ1  A LYS   A 1 11  ? 14.332 -20.141 12.967  0.78 15.81 ?  11  LYS   A HZ1  1 
ATOM   266  H HZ1  B LYS   A 1 11  ? 13.328 -19.571 12.791  0.22 19.12 ?  11  LYS   A HZ1  1 
ATOM   267  H HZ2  A LYS   A 1 11  ? 13.795 -18.993 12.264  0.78 15.81 ?  11  LYS   A HZ2  1 
ATOM   268  H HZ2  B LYS   A 1 11  ? 12.808 -18.378 12.157  0.22 19.12 ?  11  LYS   A HZ2  1 
ATOM   269  H HZ3  A LYS   A 1 11  ? 14.078 -18.907 13.682  0.78 15.81 ?  11  LYS   A HZ3  1 
ATOM   270  H HZ3  B LYS   A 1 11  ? 12.814 -18.488 13.603  0.22 19.12 ?  11  LYS   A HZ3  1 
ATOM   271  N N    A LEU   A 1 12  ? 10.806 -16.120 9.009   0.78 11.09 ?  12  LEU   A N    1 
ATOM   272  N N    B LEU   A 1 12  ? 10.114 -15.693 8.686   0.22 15.89 ?  12  LEU   A N    1 
ATOM   273  C CA   A LEU   A 1 12  ? 10.530 -16.688 7.692   0.78 11.56 ?  12  LEU   A CA   1 
ATOM   274  C CA   B LEU   A 1 12  ? 10.013 -16.248 7.342   0.22 15.73 ?  12  LEU   A CA   1 
ATOM   275  C C    A LEU   A 1 12  ? 11.108 -18.089 7.531   0.78 11.42 ?  12  LEU   A C    1 
ATOM   276  C C    B LEU   A 1 12  ? 10.630 -17.640 7.242   0.22 15.20 ?  12  LEU   A C    1 
ATOM   277  O O    A LEU   A 1 12  ? 10.476 -18.959 6.921   0.78 12.18 ?  12  LEU   A O    1 
ATOM   278  O O    B LEU   A 1 12  ? 9.972  -18.573 6.771   0.22 15.02 ?  12  LEU   A O    1 
ATOM   279  C CB   A LEU   A 1 12  ? 11.074 -15.780 6.584   0.78 11.98 ?  12  LEU   A CB   1 
ATOM   280  C CB   B LEU   A 1 12  ? 10.658 -15.297 6.325   0.22 15.93 ?  12  LEU   A CB   1 
ATOM   281  C CG   A LEU   A 1 12  ? 10.422 -14.405 6.432   0.78 12.84 ?  12  LEU   A CG   1 
ATOM   282  C CG   B LEU   A 1 12  ? 9.996  -13.927 6.157   0.22 16.08 ?  12  LEU   A CG   1 
ATOM   283  C CD1  A LEU   A 1 12  ? 11.152 -13.603 5.369   0.78 13.67 ?  12  LEU   A CD1  1 
ATOM   284  C CD1  B LEU   A 1 12  ? 10.811 -13.070 5.204   0.22 16.05 ?  12  LEU   A CD1  1 
ATOM   285  C CD2  A LEU   A 1 12  ? 8.951  -14.539 6.077   0.78 14.00 ?  12  LEU   A CD2  1 
ATOM   286  C CD2  B LEU   A 1 12  ? 8.566  -14.073 5.655   0.22 16.18 ?  12  LEU   A CD2  1 
ATOM   287  H H    A LEU   A 1 12  ? 11.560 -15.698 9.069   0.78 13.33 ?  12  LEU   A H    1 
ATOM   288  H H    B LEU   A 1 12  ? 10.856 -15.291 8.842   0.22 19.08 ?  12  LEU   A H    1 
ATOM   289  H HA   A LEU   A 1 12  ? 9.569  -16.750 7.575   0.78 13.88 ?  12  LEU   A HA   1 
ATOM   290  H HA   B LEU   A 1 12  ? 9.074  -16.326 7.111   0.22 18.89 ?  12  LEU   A HA   1 
ATOM   291  H HB2  A LEU   A 1 12  ? 12.014 -15.631 6.747   0.78 14.39 ?  12  LEU   A HB2  1 
ATOM   292  H HB2  B LEU   A 1 12  ? 11.574 -15.135 6.590   0.22 19.13 ?  12  LEU   A HB2  1 
ATOM   293  H HB3  A LEU   A 1 12  ? 10.963 -16.242 5.736   0.78 14.39 ?  12  LEU   A HB3  1 
ATOM   294  H HB3  B LEU   A 1 12  ? 10.642 -15.723 5.454   0.22 19.13 ?  12  LEU   A HB3  1 
ATOM   295  H HG   A LEU   A 1 12  ? 10.486 -13.922 7.268   0.78 15.42 ?  12  LEU   A HG   1 
ATOM   296  H HG   B LEU   A 1 12  ? 9.966  -13.474 7.017   0.22 19.31 ?  12  LEU   A HG   1 
ATOM   297  H HD11 A LEU   A 1 12  ? 10.730 -12.732 5.280   0.78 16.42 ?  12  LEU   A HD11 1 
ATOM   298  H HD11 B LEU   A 1 12  ? 10.339 -12.238 5.042   0.22 19.28 ?  12  LEU   A HD11 1 
ATOM   299  H HD12 A LEU   A 1 12  ? 12.078 -13.494 5.637   0.78 16.42 ?  12  LEU   A HD12 1 
ATOM   300  H HD12 B LEU   A 1 12  ? 11.675 -12.889 5.605   0.22 19.28 ?  12  LEU   A HD12 1 
ATOM   301  H HD13 A LEU   A 1 12  ? 11.106 -14.078 4.523   0.78 16.42 ?  12  LEU   A HD13 1 
ATOM   302  H HD13 B LEU   A 1 12  ? 10.925 -13.553 4.371   0.22 19.28 ?  12  LEU   A HD13 1 
ATOM   303  H HD21 A LEU   A 1 12  ? 8.594  -13.661 5.860   0.78 16.81 ?  12  LEU   A HD21 1 
ATOM   304  H HD21 B LEU   A 1 12  ? 8.218  -13.198 5.425   0.22 19.43 ?  12  LEU   A HD21 1 
ATOM   305  H HD22 A LEU   A 1 12  ? 8.861  -15.129 5.312   0.78 16.81 ?  12  LEU   A HD22 1 
ATOM   306  H HD22 B LEU   A 1 12  ? 8.567  -14.646 4.871   0.22 19.43 ?  12  LEU   A HD22 1 
ATOM   307  H HD23 A LEU   A 1 12  ? 8.475  -14.908 6.837   0.78 16.81 ?  12  LEU   A HD23 1 
ATOM   308  H HD23 B LEU   A 1 12  ? 8.025  -14.472 6.354   0.22 19.43 ?  12  LEU   A HD23 1 
ATOM   309  N N    A THR   A 1 13  ? 12.315 -18.305 8.042   0.78 11.24 ?  13  THR   A N    1 
ATOM   310  N N    B THR   A 1 13  ? 11.878 -17.803 7.669   0.22 15.31 ?  13  THR   A N    1 
ATOM   311  C CA   A THR   A 1 13  ? 13.007 -19.582 7.928   0.78 11.56 ?  13  THR   A CA   1 
ATOM   312  C CA   B THR   A 1 13  ? 12.521 -19.114 7.700   0.22 15.18 ?  13  THR   A CA   1 
ATOM   313  C C    A THR   A 1 13  ? 13.788 -19.818 9.213   0.78 11.94 ?  13  THR   A C    1 
ATOM   314  C C    B THR   A 1 13  ? 13.193 -19.327 9.054   0.22 15.24 ?  13  THR   A C    1 
ATOM   315  O O    A THR   A 1 13  ? 13.716 -19.041 10.169  0.78 11.81 ?  13  THR   A O    1 
ATOM   316  O O    B THR   A 1 13  ? 12.934 -18.619 10.035  0.22 15.37 ?  13  THR   A O    1 
ATOM   317  C CB   A THR   A 1 13  ? 13.972 -19.617 6.734   0.78 12.24 ?  13  THR   A CB   1 
ATOM   318  C CB   B THR   A 1 13  ? 13.545 -19.249 6.571   0.22 15.00 ?  13  THR   A CB   1 
ATOM   319  O OG1  A THR   A 1 13  ? 15.045 -18.712 6.989   0.78 12.53 ?  13  THR   A OG1  1 
ATOM   320  O OG1  B THR   A 1 13  ? 14.596 -18.298 6.773   0.22 15.15 ?  13  THR   A OG1  1 
ATOM   321  C CG2  A THR   A 1 13  ? 13.290 -19.237 5.430   0.78 13.42 ?  13  THR   A CG2  1 
ATOM   322  C CG2  B THR   A 1 13  ? 12.899 -19.010 5.225   0.22 14.93 ?  13  THR   A CG2  1 
ATOM   323  H H    A THR   A 1 13  ? 12.777 -17.701 8.451   0.78 13.50 ?  13  THR   A H    1 
ATOM   324  H H    B THR   A 1 13  ? 12.386 -17.154 7.926   0.22 18.38 ?  13  THR   A H    1 
ATOM   325  H HA   A THR   A 1 13  ? 12.363 -20.293 7.819   0.78 13.88 ?  13  THR   A HA   1 
ATOM   326  H HA   B THR   A 1 13  ? 11.842 -19.800 7.594   0.22 18.23 ?  13  THR   A HA   1 
ATOM   327  H HB   A THR   A 1 13  ? 14.334 -20.511 6.633   0.78 14.71 ?  13  THR   A HB   1 
ATOM   328  H HB   B THR   A 1 13  ? 13.916 -20.145 6.593   0.22 18.01 ?  13  THR   A HB   1 
ATOM   329  H HG1  A THR   A 1 13  ? 15.728 -19.130 7.246   0.78 15.05 ?  13  THR   A HG1  1 
ATOM   330  H HG1  B THR   A 1 13  ? 15.167 -18.372 6.166   0.22 18.20 ?  13  THR   A HG1  1 
ATOM   331  H HG21 A THR   A 1 13  ? 13.891 -19.398 4.682   0.78 16.12 ?  13  THR   A HG21 1 
ATOM   332  H HG21 B THR   A 1 13  ? 13.504 -19.290 4.523   0.22 17.94 ?  13  THR   A HG21 1 
ATOM   333  H HG22 A THR   A 1 13  ? 12.492 -19.774 5.310   0.78 16.12 ?  13  THR   A HG22 1 
ATOM   334  H HG22 B THR   A 1 13  ? 12.078 -19.520 5.157   0.22 17.94 ?  13  THR   A HG22 1 
ATOM   335  H HG23 A THR   A 1 13  ? 13.046 -18.301 5.441   0.78 16.12 ?  13  THR   A HG23 1 
ATOM   336  H HG23 B THR   A 1 13  ? 12.697 -18.068 5.116   0.22 17.94 ?  13  THR   A HG23 1 
ATOM   337  N N    A ASP   A 1 14  ? 14.592 -20.879 9.205   0.78 12.16 ?  14  ASP   A N    1 
ATOM   338  N N    B ASP   A 1 14  ? 14.093 -20.315 9.113   0.22 15.52 ?  14  ASP   A N    1 
ATOM   339  C CA   A ASP   A 1 14  ? 15.453 -21.168 10.342  0.78 12.68 ?  14  ASP   A CA   1 
ATOM   340  C CA   B ASP   A 1 14  ? 14.743 -20.631 10.380  0.22 15.93 ?  14  ASP   A CA   1 
ATOM   341  C C    A ASP   A 1 14  ? 16.311 -19.970 10.731  0.78 11.96 ?  14  ASP   A C    1 
ATOM   342  C C    B ASP   A 1 14  ? 15.699 -19.530 10.820  0.22 14.81 ?  14  ASP   A C    1 
ATOM   343  O O    A ASP   A 1 14  ? 16.572 -19.752 11.918  0.78 13.35 ?  14  ASP   A O    1 
ATOM   344  O O    B ASP   A 1 14  ? 15.904 -19.339 12.024  0.22 14.36 ?  14  ASP   A O    1 
ATOM   345  C CB   A ASP   A 1 14  ? 16.349 -22.359 10.016  0.78 15.12 ?  14  ASP   A CB   1 
ATOM   346  C CB   B ASP   A 1 14  ? 15.482 -21.966 10.290  0.22 17.51 ?  14  ASP   A CB   1 
ATOM   347  C CG   A ASP   A 1 14  ? 17.252 -22.724 11.163  0.78 18.97 ?  14  ASP   A CG   1 
ATOM   348  C CG   B ASP   A 1 14  ? 16.183 -22.327 11.583  0.22 19.14 ?  14  ASP   A CG   1 
ATOM   349  O OD1  A ASP   A 1 14  ? 16.724 -23.129 12.222  0.78 20.02 ?  14  ASP   A OD1  1 
ATOM   350  O OD1  B ASP   A 1 14  ? 15.487 -22.672 12.560  0.22 19.61 ?  14  ASP   A OD1  1 
ATOM   351  O OD2  A ASP   A 1 14  ? 18.482 -22.589 11.005  0.78 21.56 -1 14  ASP   A OD2  1 
ATOM   352  O OD2  B ASP   A 1 14  ? 17.428 -22.261 11.625  0.22 19.74 -1 14  ASP   A OD2  1 
ATOM   353  H H    A ASP   A 1 14  ? 14.665 -21.433 8.551   0.78 14.60 ?  14  ASP   A H    1 
ATOM   354  H H    B ASP   A 1 14  ? 14.347 -20.808 8.446   0.22 18.64 ?  14  ASP   A H    1 
ATOM   355  H HA   A ASP   A 1 14  ? 14.899 -21.402 11.103  0.78 15.24 ?  14  ASP   A HA   1 
ATOM   356  H HA   B ASP   A 1 14  ? 14.059 -20.716 11.056  0.22 19.13 ?  14  ASP   A HA   1 
ATOM   357  H HB2  A ASP   A 1 14  ? 15.785 -23.130 9.814   0.78 18.16 ?  14  ASP   A HB2  1 
ATOM   358  H HB2  B ASP   A 1 14  ? 14.846 -22.669 10.089  0.22 21.02 ?  14  ASP   A HB2  1 
ATOM   359  H HB3  A ASP   A 1 14  ? 16.900 -22.145 9.252   0.78 18.16 ?  14  ASP   A HB3  1 
ATOM   360  H HB3  B ASP   A 1 14  ? 16.155 -21.914 9.594   0.22 21.02 ?  14  ASP   A HB3  1 
ATOM   361  N N    A ASN   A 1 15  ? 16.766 -19.180 9.747   0.78 11.32 ?  15  ASN   A N    1 
ATOM   362  N N    B ASN   A 1 15  ? 16.286 -18.795 9.874   0.22 14.13 ?  15  ASN   A N    1 
ATOM   363  C CA   A ASN   A 1 15  ? 17.761 -18.147 10.009  0.78 12.03 ?  15  ASN   A CA   1 
ATOM   364  C CA   B ASN   A 1 15  ? 17.288 -17.789 10.198  0.22 13.77 ?  15  ASN   A CA   1 
ATOM   365  C C    A ASN   A 1 15  ? 17.390 -16.751 9.528   0.78 12.32 ?  15  ASN   A C    1 
ATOM   366  C C    B ASN   A 1 15  ? 16.957 -16.398 9.679   0.22 13.59 ?  15  ASN   A C    1 
ATOM   367  O O    A ASN   A 1 15  ? 18.159 -15.820 9.779   0.78 13.44 ?  15  ASN   A O    1 
ATOM   368  O O    B ASN   A 1 15  ? 17.713 -15.460 9.957   0.22 13.98 ?  15  ASN   A O    1 
ATOM   369  C CB   A ASN   A 1 15  ? 19.126 -18.540 9.409   0.78 11.80 ?  15  ASN   A CB   1 
ATOM   370  C CB   B ASN   A 1 15  ? 18.668 -18.213 9.677   0.22 13.91 ?  15  ASN   A CB   1 
ATOM   371  C CG   A ASN   A 1 15  ? 19.098 -18.622 7.900   0.78 11.99 ?  15  ASN   A CG   1 
ATOM   372  C CG   B ASN   A 1 15  ? 18.701 -18.373 8.170   0.22 14.02 ?  15  ASN   A CG   1 
ATOM   373  O OD1  A ASN   A 1 15  ? 18.370 -19.433 7.322   0.78 12.74 ?  15  ASN   A OD1  1 
ATOM   374  O OD1  B ASN   A 1 15  ? 17.914 -19.126 7.595   0.22 13.96 ?  15  ASN   A OD1  1 
ATOM   375  N ND2  A ASN   A 1 15  ? 19.888 -17.778 7.247   0.78 12.44 ?  15  ASN   A ND2  1 
ATOM   376  N ND2  B ASN   A 1 15  ? 19.609 -17.652 7.520   0.22 13.96 ?  15  ASN   A ND2  1 
ATOM   377  H H    A ASN   A 1 15  ? 16.521 -19.238 8.928   0.78 13.60 ?  15  ASN   A H    1 
ATOM   378  H H    B ASN   A 1 15  ? 16.112 -18.856 9.032   0.22 16.97 ?  15  ASN   A H    1 
ATOM   379  H HA   A ASN   A 1 15  ? 17.894 -18.094 10.968  0.78 14.45 ?  15  ASN   A HA   1 
ATOM   380  H HA   B ASN   A 1 15  ? 17.354 -17.722 11.162  0.22 16.54 ?  15  ASN   A HA   1 
ATOM   381  H HB2  A ASN   A 1 15  ? 19.789 -17.872 9.665   0.78 14.18 ?  15  ASN   A HB2  1 
ATOM   382  H HB2  B ASN   A 1 15  ? 19.318 -17.537 9.924   0.22 16.71 ?  15  ASN   A HB2  1 
ATOM   383  H HB3  A ASN   A 1 15  ? 19.394 -19.410 9.753   0.78 14.18 ?  15  ASN   A HB3  1 
ATOM   384  H HB3  B ASN   A 1 15  ? 18.904 -19.064 10.073  0.22 16.71 ?  15  ASN   A HB3  1 
ATOM   385  H HD21 A ASN   A 1 15  ? 19.908 -17.785 6.387   0.78 14.94 ?  15  ASN   A HD21 1 
ATOM   386  H HD21 B ASN   A 1 15  ? 19.669 -17.704 6.662   0.22 16.77 ?  15  ASN   A HD21 1 
ATOM   387  H HD22 A ASN   A 1 15  ? 20.386 -17.221 7.680   0.78 14.94 ?  15  ASN   A HD22 1 
ATOM   388  H HD22 B ASN   A 1 15  ? 20.142 -17.135 7.955   0.22 16.77 ?  15  ASN   A HD22 1 
ATOM   389  N N    A VAL   A 1 16  ? 16.256 -16.569 8.858   0.78 11.78 ?  16  VAL   A N    1 
ATOM   390  N N    B VAL   A 1 16  ? 15.851 -16.223 8.959   0.22 13.10 ?  16  VAL   A N    1 
ATOM   391  C CA   A VAL   A 1 16  ? 15.865 -15.279 8.302   0.78 11.70 ?  16  VAL   A CA   1 
ATOM   392  C CA   B VAL   A 1 16  ? 15.495 -14.946 8.354   0.22 12.99 ?  16  VAL   A CA   1 
ATOM   393  C C    A VAL   A 1 16  ? 14.594 -14.793 8.989   0.78 11.37 ?  16  VAL   A C    1 
ATOM   394  C C    B VAL   A 1 16  ? 14.213 -14.440 8.999   0.22 13.13 ?  16  VAL   A C    1 
ATOM   395  O O    A VAL   A 1 16  ? 13.594 -15.521 9.070   0.78 11.70 ?  16  VAL   A O    1 
ATOM   396  O O    B VAL   A 1 16  ? 13.197 -15.145 9.014   0.22 13.09 ?  16  VAL   A O    1 
ATOM   397  C CB   A VAL   A 1 16  ? 15.671 -15.344 6.777   0.78 12.22 ?  16  VAL   A CB   1 
ATOM   398  C CB   B VAL   A 1 16  ? 15.338 -15.063 6.827   0.22 13.01 ?  16  VAL   A CB   1 
ATOM   399  C CG1  A VAL   A 1 16  ? 15.227 -13.987 6.235   0.78 13.21 ?  16  VAL   A CG1  1 
ATOM   400  C CG1  B VAL   A 1 16  ? 14.965 -13.714 6.227   0.22 13.22 ?  16  VAL   A CG1  1 
ATOM   401  C CG2  A VAL   A 1 16  ? 16.942 -15.811 6.087   0.78 13.30 ?  16  VAL   A CG2  1 
ATOM   402  C CG2  B VAL   A 1 16  ? 16.620 -15.595 6.203   0.22 13.14 ?  16  VAL   A CG2  1 
ATOM   403  H H    A VAL   A 1 16  ? 15.688 -17.199 8.721   0.78 14.15 ?  16  VAL   A H    1 
ATOM   404  H H    B VAL   A 1 16  ? 15.275 -16.843 8.810   0.22 15.74 ?  16  VAL   A H    1 
ATOM   405  H HA   A VAL   A 1 16  ? 16.578 -14.638 8.483   0.78 14.05 ?  16  VAL   A HA   1 
ATOM   406  H HA   B VAL   A 1 16  ? 16.193 -14.298 8.531   0.22 15.61 ?  16  VAL   A HA   1 
ATOM   407  H HB   A VAL   A 1 16  ? 14.977 -15.989 6.583   0.78 14.68 ?  16  VAL   A HB   1 
ATOM   408  H HB   B VAL   A 1 16  ? 14.623 -15.687 6.629   0.22 15.63 ?  16  VAL   A HB   1 
ATOM   409  H HG11 A VAL   A 1 16  ? 15.308 -13.997 5.270   0.78 15.87 ?  16  VAL   A HG11 1 
ATOM   410  H HG11 B VAL   A 1 16  ? 15.054 -13.765 5.264   0.22 15.88 ?  16  VAL   A HG11 1 
ATOM   411  H HG12 A VAL   A 1 16  ? 14.302 -13.836 6.487   0.78 15.87 ?  16  VAL   A HG12 1 
ATOM   412  H HG12 B VAL   A 1 16  ? 14.047 -13.505 6.462   0.22 15.88 ?  16  VAL   A HG12 1 
ATOM   413  H HG13 A VAL   A 1 16  ? 15.792 -13.297 6.610   0.78 15.87 ?  16  VAL   A HG13 1 
ATOM   414  H HG13 B VAL   A 1 16  ? 15.561 -13.036 6.580   0.22 15.88 ?  16  VAL   A HG13 1 
ATOM   415  H HG21 A VAL   A 1 16  ? 16.809 -15.776 5.128   0.78 15.97 ?  16  VAL   A HG21 1 
ATOM   416  H HG21 B VAL   A 1 16  ? 16.533 -15.578 5.238   0.22 15.79 ?  16  VAL   A HG21 1 
ATOM   417  H HG22 A VAL   A 1 16  ? 17.674 -15.226 6.341   0.78 15.97 ?  16  VAL   A HG22 1 
ATOM   418  H HG22 B VAL   A 1 16  ? 17.361 -15.035 6.479   0.22 15.79 ?  16  VAL   A HG22 1 
ATOM   419  H HG23 A VAL   A 1 16  ? 17.137 -16.720 6.363   0.78 15.97 ?  16  VAL   A HG23 1 
ATOM   420  H HG23 B VAL   A 1 16  ? 16.764 -16.505 6.507   0.22 15.79 ?  16  VAL   A HG23 1 
ATOM   421  N N    A TYR   A 1 17  ? 14.640 -13.533 9.432   0.78 11.22 ?  17  TYR   A N    1 
ATOM   422  N N    B TYR   A 1 17  ? 14.268 -13.216 9.525   0.22 13.54 ?  17  TYR   A N    1 
ATOM   423  C CA   A TYR   A 1 17  ? 13.574 -12.848 10.145  0.78 11.49 ?  17  TYR   A CA   1 
ATOM   424  C CA   B TYR   A 1 17  ? 13.130 -12.548 10.137  0.22 14.16 ?  17  TYR   A CA   1 
ATOM   425  C C    A TYR   A 1 17  ? 13.305 -11.514 9.459   0.78 11.79 ?  17  TYR   A C    1 
ATOM   426  C C    B TYR   A 1 17  ? 12.929 -11.198 9.464   0.22 13.90 ?  17  TYR   A C    1 
ATOM   427  O O    A TYR   A 1 17  ? 14.204 -10.946 8.833   0.78 11.96 ?  17  TYR   A O    1 
ATOM   428  O O    B TYR   A 1 17  ? 13.889 -10.568 9.010   0.22 14.05 ?  17  TYR   A O    1 
ATOM   429  C CB   A TYR   A 1 17  ? 14.012 -12.591 11.589  0.78 11.80 ?  17  TYR   A CB   1 
ATOM   430  C CB   B TYR   A 1 17  ? 13.366 -12.340 11.634  0.22 15.12 ?  17  TYR   A CB   1 
ATOM   431  C CG   A TYR   A 1 17  ? 14.202 -13.853 12.394  0.78 12.41 ?  17  TYR   A CG   1 
ATOM   432  C CG   B TYR   A 1 17  ? 13.318 -13.608 12.447  0.22 16.09 ?  17  TYR   A CG   1 
ATOM   433  C CD1  A TYR   A 1 17  ? 15.366 -14.609 12.295  0.78 13.10 ?  17  TYR   A CD1  1 
ATOM   434  C CD1  B TYR   A 1 17  ? 14.406 -14.466 12.495  0.22 16.60 ?  17  TYR   A CD1  1 
ATOM   435  C CD2  A TYR   A 1 17  ? 13.205 -14.304 13.247  0.78 12.77 ?  17  TYR   A CD2  1 
ATOM   436  C CD2  B TYR   A 1 17  ? 12.183 -13.946 13.171  0.22 16.40 ?  17  TYR   A CD2  1 
ATOM   437  C CE1  A TYR   A 1 17  ? 15.524 -15.779 13.027  0.78 13.57 ?  17  TYR   A CE1  1 
ATOM   438  C CE1  B TYR   A 1 17  ? 14.365 -15.629 13.238  0.22 17.07 ?  17  TYR   A CE1  1 
ATOM   439  C CE2  A TYR   A 1 17  ? 13.358 -15.464 13.983  0.78 13.43 ?  17  TYR   A CE2  1 
ATOM   440  C CE2  B TYR   A 1 17  ? 12.131 -15.107 13.917  0.22 16.89 ?  17  TYR   A CE2  1 
ATOM   441  C CZ   A TYR   A 1 17  ? 14.516 -16.199 13.871  0.78 13.65 ?  17  TYR   A CZ   1 
ATOM   442  C CZ   B TYR   A 1 17  ? 13.226 -15.944 13.948  0.22 17.31 ?  17  TYR   A CZ   1 
ATOM   443  O OH   A TYR   A 1 17  ? 14.664 -17.354 14.603  0.78 14.64 ?  17  TYR   A OH   1 
ATOM   444  O OH   B TYR   A 1 17  ? 13.184 -17.104 14.689  0.22 17.54 ?  17  TYR   A OH   1 
ATOM   445  H H    A TYR   A 1 17  ? 15.335 -13.027 9.317   0.78 13.48 ?  17  TYR   A H    1 
ATOM   446  H H    B TYR   A 1 17  ? 14.982 -12.737 9.542   0.22 16.26 ?  17  TYR   A H    1 
ATOM   447  H HA   A TYR   A 1 17  ? 12.770 -13.389 10.136  0.78 13.81 ?  17  TYR   A HA   1 
ATOM   448  H HA   B TYR   A 1 17  ? 12.327 -13.078 10.020  0.22 17.01 ?  17  TYR   A HA   1 
ATOM   449  H HB2  A TYR   A 1 17  ? 14.854 -12.117 11.584  0.78 14.18 ?  17  TYR   A HB2  1 
ATOM   450  H HB2  B TYR   A 1 17  ? 14.228 -11.914 11.772  0.22 18.16 ?  17  TYR   A HB2  1 
ATOM   451  H HB3  A TYR   A 1 17  ? 13.333 -12.061 12.028  0.78 14.18 ?  17  TYR   A HB3  1 
ATOM   452  H HB3  B TYR   A 1 17  ? 12.666 -11.778 11.970  0.22 18.16 ?  17  TYR   A HB3  1 
ATOM   453  H HD1  A TYR   A 1 17  ? 16.042 -14.336 11.723  0.78 15.74 ?  17  TYR   A HD1  1 
ATOM   454  H HD1  B TYR   A 1 17  ? 15.174 -14.252 12.017  0.22 19.93 ?  17  TYR   A HD1  1 
ATOM   455  H HD2  A TYR   A 1 17  ? 12.415 -13.820 13.332  0.78 15.33 ?  17  TYR   A HD2  1 
ATOM   456  H HD2  B TYR   A 1 17  ? 11.442 -13.381 13.151  0.22 19.69 ?  17  TYR   A HD2  1 
ATOM   457  H HE1  A TYR   A 1 17  ? 16.310 -16.280 12.951  0.78 16.30 ?  17  TYR   A HE1  1 
ATOM   458  H HE1  B TYR   A 1 17  ? 15.101 -16.195 13.260  0.22 20.50 ?  17  TYR   A HE1  1 
ATOM   459  H HE2  A TYR   A 1 17  ? 12.679 -15.754 14.556  0.78 16.13 ?  17  TYR   A HE2  1 
ATOM   460  H HE2  B TYR   A 1 17  ? 11.363 -15.321 14.396  0.22 20.28 ?  17  TYR   A HE2  1 
ATOM   461  H HH   A TYR   A 1 17  ? 15.425 -17.691 14.471  0.78 17.59 ?  17  TYR   A HH   1 
ATOM   462  H HH   B TYR   A 1 17  ? 12.441 -17.167 15.077  0.22 21.06 ?  17  TYR   A HH   1 
ATOM   463  N N    A ILE   A 1 18  ? 12.079 -10.993 9.584   0.78 11.98 ?  18  ILE   A N    1 
ATOM   464  N N    B ILE   A 1 18  ? 11.673 -10.750 9.407   0.22 13.66 ?  18  ILE   A N    1 
ATOM   465  C CA   A ILE   A 1 18  ? 11.695 -9.781  8.859   0.78 12.39 ?  18  ILE   A CA   1 
ATOM   466  C CA   B ILE   A 1 18  ? 11.311 -9.541  8.677   0.22 14.03 ?  18  ILE   A CA   1 
ATOM   467  C C    A ILE   A 1 18  ? 10.741 -8.935  9.696   0.78 12.67 ?  18  ILE   A C    1 
ATOM   468  C C    B ILE   A 1 18  ? 10.395 -8.679  9.538   0.22 14.38 ?  18  ILE   A C    1 
ATOM   469  O O    A ILE   A 1 18  ? 9.916  -9.455  10.454  0.78 13.32 ?  18  ILE   A O    1 
ATOM   470  O O    B ILE   A 1 18  ? 9.484  -9.191  10.198  0.22 14.43 ?  18  ILE   A O    1 
ATOM   471  C CB   A ILE   A 1 18  ? 11.112 -10.142 7.472   0.78 12.74 ?  18  ILE   A CB   1 
ATOM   472  C CB   B ILE   A 1 18  ? 10.665 -9.882  7.313   0.22 14.58 ?  18  ILE   A CB   1 
ATOM   473  C CG1  A ILE   A 1 18  ? 11.065 -8.925  6.550   0.78 13.81 ?  18  ILE   A CG1  1 
ATOM   474  C CG1  B ILE   A 1 18  ? 10.790 -8.707  6.343   0.22 14.91 ?  18  ILE   A CG1  1 
ATOM   475  C CG2  A ILE   A 1 18  ? 9.741  -10.814 7.613   0.78 12.79 ?  18  ILE   A CG2  1 
ATOM   476  C CG2  B ILE   A 1 18  ? 9.199  -10.312 7.467   0.22 15.06 ?  18  ILE   A CG2  1 
ATOM   477  C CD1  A ILE   A 1 18  ? 10.721 -9.290  5.126   0.78 15.35 ?  18  ILE   A CD1  1 
ATOM   478  C CD1  B ILE   A 1 18  ? 11.056 -9.143  4.916   0.22 15.32 ?  18  ILE   A CD1  1 
ATOM   479  H H    A ILE   A 1 18  ? 11.458 -11.337 10.069  0.78 14.40 ?  18  ILE   A H    1 
ATOM   480  H H    B ILE   A 1 18  ? 11.003 -11.140 9.786   0.22 16.41 ?  18  ILE   A H    1 
ATOM   481  H HA   A ILE   A 1 18  ? 12.508 -9.260  8.709   0.78 14.89 ?  18  ILE   A HA   1 
ATOM   482  H HA   B ILE   A 1 18  ? 12.117 -9.033  8.507   0.22 16.86 ?  18  ILE   A HA   1 
ATOM   483  H HB   A ILE   A 1 18  ? 11.711 -10.786 7.066   0.78 15.30 ?  18  ILE   A HB   1 
ATOM   484  H HB   B ILE   A 1 18  ? 11.151 -10.626 6.937   0.22 17.52 ?  18  ILE   A HB   1 
ATOM   485  H HG12 A ILE   A 1 18  ? 10.403 -8.302  6.873   0.78 16.59 ?  18  ILE   A HG12 1 
ATOM   486  H HG12 B ILE   A 1 18  ? 9.964  -8.200  6.350   0.22 17.90 ?  18  ILE   A HG12 1 
ATOM   487  H HG13 A ILE   A 1 18  ? 11.945 -8.499  6.543   0.78 16.59 ?  18  ILE   A HG13 1 
ATOM   488  H HG13 B ILE   A 1 18  ? 11.527 -8.139  6.620   0.22 17.90 ?  18  ILE   A HG13 1 
ATOM   489  H HG21 A ILE   A 1 18  ? 9.486  -11.188 6.754   0.78 15.36 ?  18  ILE   A HG21 1 
ATOM   490  H HG21 B ILE   A 1 18  ? 8.896  -10.697 6.626   0.22 18.08 ?  18  ILE   A HG21 1 
ATOM   491  H HG22 A ILE   A 1 18  ? 9.801  -11.516 8.276   0.78 15.36 ?  18  ILE   A HG22 1 
ATOM   492  H HG22 B ILE   A 1 18  ? 9.136  -10.974 8.171   0.22 18.08 ?  18  ILE   A HG22 1 
ATOM   493  H HG23 A ILE   A 1 18  ? 9.090  -10.149 7.890   0.78 15.36 ?  18  ILE   A HG23 1 
ATOM   494  H HG23 B ILE   A 1 18  ? 8.656  -9.540  7.687   0.22 18.08 ?  18  ILE   A HG23 1 
ATOM   495  H HD11 A ILE   A 1 18  ? 10.802 -8.496  4.567   0.78 18.43 ?  18  ILE   A HD11 1 
ATOM   496  H HD11 B ILE   A 1 18  ? 11.133 -8.357  4.354   0.22 18.40 ?  18  ILE   A HD11 1 
ATOM   497  H HD12 A ILE   A 1 18  ? 11.332 -9.974  4.813   0.78 18.43 ?  18  ILE   A HD12 1 
ATOM   498  H HD12 B ILE   A 1 18  ? 11.882 -9.651  4.890   0.22 18.40 ?  18  ILE   A HD12 1 
ATOM   499  H HD13 A ILE   A 1 18  ? 9.810  -9.618  5.096   0.78 18.43 ?  18  ILE   A HD13 1 
ATOM   500  H HD13 B ILE   A 1 18  ? 10.318 -9.696  4.613   0.22 18.40 ?  18  ILE   A HD13 1 
ATOM   501  N N    A LYS   A 1 19  ? 10.839 -7.613  9.524   0.78 13.50 ?  19  LYS   A N    1 
ATOM   502  N N    B LYS   A 1 19  ? 10.644 -7.367  9.535   0.22 14.61 ?  19  LYS   A N    1 
ATOM   503  C CA   A LYS   A 1 19  ? 10.026 -6.662  10.274  0.78 14.89 ?  19  LYS   A CA   1 
ATOM   504  C CA   B LYS   A 1 19  ? 9.867  -6.422  10.326  0.22 15.16 ?  19  LYS   A CA   1 
ATOM   505  C C    A LYS   A 1 19  ? 9.807  -5.410  9.434   0.78 14.86 ?  19  LYS   A C    1 
ATOM   506  C C    B LYS   A 1 19  ? 9.728  -5.118  9.557   0.22 15.01 ?  19  LYS   A C    1 
ATOM   507  O O    A LYS   A 1 19  ? 10.675 -5.011  8.655   0.78 14.75 ?  19  LYS   A O    1 
ATOM   508  O O    B LYS   A 1 19  ? 10.690 -4.638  8.951   0.22 15.06 ?  19  LYS   A O    1 
ATOM   509  C CB   A LYS   A 1 19  ? 10.747 -6.287  11.575  0.78 16.23 ?  19  LYS   A CB   1 
ATOM   510  C CB   B LYS   A 1 19  ? 10.532 -6.141  11.684  0.22 15.92 ?  19  LYS   A CB   1 
ATOM   511  C CG   A LYS   A 1 19  ? 10.010 -5.370  12.537  0.78 17.84 ?  19  LYS   A CG   1 
ATOM   512  C CG   B LYS   A 1 19  ? 9.772  -5.166  12.575  0.22 16.76 ?  19  LYS   A CG   1 
ATOM   513  C CD   A LYS   A 1 19  ? 10.925 -5.084  13.727  0.78 18.89 ?  19  LYS   A CD   1 
ATOM   514  C CD   B LYS   A 1 19  ? 10.580 -4.826  13.819  0.22 17.57 ?  19  LYS   A CD   1 
ATOM   515  C CE   A LYS   A 1 19  ? 10.299 -4.165  14.761  0.78 19.42 ?  19  LYS   A CE   1 
ATOM   516  C CE   B LYS   A 1 19  ? 9.837  -3.863  14.729  0.22 17.96 ?  19  LYS   A CE   1 
ATOM   517  N NZ   A LYS   A 1 19  ? 11.222 -3.967  15.919  0.78 19.23 ?  19  LYS   A NZ   1 
ATOM   518  N NZ   B LYS   A 1 19  ? 10.660 -3.476  15.910  0.22 18.01 ?  19  LYS   A NZ   1 
ATOM   519  H H    A LYS   A 1 19  ? 11.390 -7.242  8.971   0.78 16.22 ?  19  LYS   A H    1 
ATOM   520  H H    B LYS   A 1 19  ? 11.265 -6.992  9.067   0.22 17.54 ?  19  LYS   A H    1 
ATOM   521  H HA   A LYS   A 1 19  ? 9.171  -7.068  10.486  0.78 17.88 ?  19  LYS   A HA   1 
ATOM   522  H HA   B LYS   A 1 19  ? 8.982  -6.781  10.487  0.22 18.21 ?  19  LYS   A HA   1 
ATOM   523  H HB2  A LYS   A 1 19  ? 10.942 -7.105  12.057  0.78 19.49 ?  19  LYS   A HB2  1 
ATOM   524  H HB2  B LYS   A 1 19  ? 10.605 -6.975  12.172  0.22 19.12 ?  19  LYS   A HB2  1 
ATOM   525  H HB3  A LYS   A 1 19  ? 11.578 -5.848  11.340  0.78 19.49 ?  19  LYS   A HB3  1 
ATOM   526  H HB3  B LYS   A 1 19  ? 11.414 -5.773  11.533  0.22 19.12 ?  19  LYS   A HB3  1 
ATOM   527  H HG2  A LYS   A 1 19  ? 9.794  -4.533  12.097  0.78 21.42 ?  19  LYS   A HG2  1 
ATOM   528  H HG2  B LYS   A 1 19  ? 9.605  -4.342  12.092  0.22 20.12 ?  19  LYS   A HG2  1 
ATOM   529  H HG3  A LYS   A 1 19  ? 9.204  -5.808  12.858  0.78 21.42 ?  19  LYS   A HG3  1 
ATOM   530  H HG3  B LYS   A 1 19  ? 8.935  -5.569  12.856  0.22 20.12 ?  19  LYS   A HG3  1 
ATOM   531  H HD2  A LYS   A 1 19  ? 11.138 -5.922  14.166  0.78 22.68 ?  19  LYS   A HD2  1 
ATOM   532  H HD2  B LYS   A 1 19  ? 10.755 -5.640  14.318  0.22 21.10 ?  19  LYS   A HD2  1 
ATOM   533  H HD3  A LYS   A 1 19  ? 11.734 -4.663  13.404  0.78 22.68 ?  19  LYS   A HD3  1 
ATOM   534  H HD3  B LYS   A 1 19  ? 11.415 -4.411  13.553  0.22 21.10 ?  19  LYS   A HD3  1 
ATOM   535  H HE2  A LYS   A 1 19  ? 10.124 -3.298  14.360  0.78 23.32 ?  19  LYS   A HE2  1 
ATOM   536  H HE2  B LYS   A 1 19  ? 9.620  -3.058  14.234  0.22 21.56 ?  19  LYS   A HE2  1 
ATOM   537  H HE3  A LYS   A 1 19  ? 9.475  -4.557  15.090  0.78 23.32 ?  19  LYS   A HE3  1 
ATOM   538  H HE3  B LYS   A 1 19  ? 9.027  -4.288  15.051  0.22 21.56 ?  19  LYS   A HE3  1 
ATOM   539  H HZ1  A LYS   A 1 19  ? 10.838 -3.443  16.528  0.78 23.09 ?  19  LYS   A HZ1  1 
ATOM   540  H HZ1  B LYS   A 1 19  ? 10.204 -2.914  16.428  0.22 21.63 ?  19  LYS   A HZ1  1 
ATOM   541  H HZ2  A LYS   A 1 19  ? 11.411 -4.752  16.293  0.78 23.09 ?  19  LYS   A HZ2  1 
ATOM   542  H HZ2  B LYS   A 1 19  ? 10.872 -4.199  16.384  0.22 21.63 ?  19  LYS   A HZ2  1 
ATOM   543  H HZ3  A LYS   A 1 19  ? 11.977 -3.587  15.646  0.78 23.09 ?  19  LYS   A HZ3  1 
ATOM   544  H HZ3  B LYS   A 1 19  ? 11.410 -3.078  15.641  0.22 21.63 ?  19  LYS   A HZ3  1 
ATOM   545  N N    A ASN   A 1 20  ? 8.636  -4.795  9.587   0.78 15.88 ?  20  ASN   A N    1 
ATOM   546  N N    B ASN   A 1 20  ? 8.521  -4.554  9.583   0.22 15.02 ?  20  ASN   A N    1 
ATOM   547  C CA   A ASN   A 1 20  ? 8.399  -3.468  9.027   0.78 17.21 ?  20  ASN   A CA   1 
ATOM   548  C CA   B ASN   A 1 20  ? 8.241  -3.255  8.974   0.22 15.28 ?  20  ASN   A CA   1 
ATOM   549  C C    A ASN   A 1 20  ? 9.027  -2.459  9.976   0.78 17.04 ?  20  ASN   A C    1 
ATOM   550  C C    B ASN   A 1 20  ? 8.757  -2.175  9.921   0.22 15.89 ?  20  ASN   A C    1 
ATOM   551  O O    A ASN   A 1 20  ? 8.518  -2.235  11.080  0.78 17.58 ?  20  ASN   A O    1 
ATOM   552  O O    B ASN   A 1 20  ? 8.026  -1.616  10.742  0.22 15.98 ?  20  ASN   A O    1 
ATOM   553  C CB   A ASN   A 1 20  ? 6.904  -3.212  8.855   0.78 18.85 ?  20  ASN   A CB   1 
ATOM   554  C CB   B ASN   A 1 20  ? 6.744  -3.116  8.724   0.22 15.14 ?  20  ASN   A CB   1 
ATOM   555  C CG   A ASN   A 1 20  ? 6.583  -1.759  8.512   0.78 20.74 ?  20  ASN   A CG   1 
ATOM   556  C CG   B ASN   A 1 20  ? 6.369  -1.815  8.036   0.22 15.00 ?  20  ASN   A CG   1 
ATOM   557  O OD1  A ASN   A 1 20  ? 5.652  -1.177  9.071   0.78 22.15 ?  20  ASN   A OD1  1 
ATOM   558  O OD1  B ASN   A 1 20  ? 5.221  -1.368  8.127   0.22 14.89 ?  20  ASN   A OD1  1 
ATOM   559  N ND2  A ASN   A 1 20  ? 7.349  -1.171  7.595   0.78 21.49 ?  20  ASN   A ND2  1 
ATOM   560  N ND2  B ASN   A 1 20  ? 7.323  -1.203  7.344   0.22 15.45 ?  20  ASN   A ND2  1 
ATOM   561  H H    A ASN   A 1 20  ? 7.966  -5.130  10.009  0.78 19.07 ?  20  ASN   A H    1 
ATOM   562  H H    B ASN   A 1 20  ? 7.835  -4.917  9.946   0.22 18.04 ?  20  ASN   A H    1 
ATOM   563  H HA   A ASN   A 1 20  ? 8.832  -3.399  8.160   0.78 20.67 ?  20  ASN   A HA   1 
ATOM   564  H HA   B ASN   A 1 20  ? 8.713  -3.193  8.130   0.22 18.36 ?  20  ASN   A HA   1 
ATOM   565  H HB2  A ASN   A 1 20  ? 6.571  -3.771  8.136   0.78 22.63 ?  20  ASN   A HB2  1 
ATOM   566  H HB2  B ASN   A 1 20  ? 6.453  -3.847  8.171   0.22 18.18 ?  20  ASN   A HB2  1 
ATOM   567  H HB3  A ASN   A 1 20  ? 6.452  -3.432  9.683   0.78 22.63 ?  20  ASN   A HB3  1 
ATOM   568  H HB3  B ASN   A 1 20  ? 6.279  -3.148  9.570   0.22 18.18 ?  20  ASN   A HB3  1 
ATOM   569  H HD21 A ASN   A 1 20  ? 7.201  -0.354  7.368   0.78 25.80 ?  20  ASN   A HD21 1 
ATOM   570  H HD21 B ASN   A 1 20  ? 7.147  -0.468  6.943   0.22 18.55 ?  20  ASN   A HD21 1 
ATOM   571  H HD22 A ASN   A 1 20  ? 7.994  -1.607  7.226   0.78 25.80 ?  20  ASN   A HD22 1 
ATOM   572  H HD22 B ASN   A 1 20  ? 8.113  -1.536  7.295   0.22 18.55 ?  20  ASN   A HD22 1 
ATOM   573  N N    A ALA   A 1 21  ? 10.145 -1.868  9.565   0.78 17.29 ?  21  ALA   A N    1 
ATOM   574  N N    B ALA   A 1 21  ? 10.050 -1.877  9.798   0.22 16.44 ?  21  ALA   A N    1 
ATOM   575  C CA   A ALA   A 1 21  ? 10.849 -0.956  10.451  0.78 17.27 ?  21  ALA   A CA   1 
ATOM   576  C CA   B ALA   A 1 21  ? 10.708 -0.981  10.737  0.22 16.82 ?  21  ALA   A CA   1 
ATOM   577  C C    A ALA   A 1 21  ? 11.800 -0.091  9.647   0.78 16.51 ?  21  ALA   A C    1 
ATOM   578  C C    B ALA   A 1 21  ? 11.764 -0.146  10.030  0.22 16.56 ?  21  ALA   A C    1 
ATOM   579  O O    A ALA   A 1 21  ? 12.216 -0.447  8.540   0.78 16.72 ?  21  ALA   A O    1 
ATOM   580  O O    B ALA   A 1 21  ? 12.330 -0.554  9.013   0.22 16.53 ?  21  ALA   A O    1 
ATOM   581  C CB   A ALA   A 1 21  ? 11.621 -1.715  11.533  0.78 18.49 ?  21  ALA   A CB   1 
ATOM   582  C CB   B ALA   A 1 21  ? 11.352 -1.758  11.889  0.22 17.37 ?  21  ALA   A CB   1 
ATOM   583  H H    A ALA   A 1 21  ? 10.508 -1.974  8.789   0.78 20.76 ?  21  ALA   A H    1 
ATOM   584  H H    B ALA   A 1 21  ? 10.562 -2.180  9.179   0.22 19.74 ?  21  ALA   A H    1 
ATOM   585  H HA   A ALA   A 1 21  ? 10.201 -0.378  10.886  0.78 20.73 ?  21  ALA   A HA   1 
ATOM   586  H HA   B ALA   A 1 21  ? 10.055 -0.373  11.111  0.22 20.20 ?  21  ALA   A HA   1 
ATOM   587  H HB1  A ALA   A 1 21  ? 12.013 -1.072  12.139  0.78 22.20 ?  21  ALA   A HB1  1 
ATOM   588  H HB1  B ALA   A 1 21  ? 11.778 -1.130  12.491  0.22 20.85 ?  21  ALA   A HB1  1 
ATOM   589  H HB2  A ALA   A 1 21  ? 11.001 -2.289  12.014  0.78 22.20 ?  21  ALA   A HB2  1 
ATOM   590  H HB2  B ALA   A 1 21  ? 10.662 -2.252  12.356  0.22 20.85 ?  21  ALA   A HB2  1 
ATOM   591  H HB3  A ALA   A 1 21  ? 12.309 -2.250  11.113  0.78 22.20 ?  21  ALA   A HB3  1 
ATOM   592  H HB3  B ALA   A 1 21  ? 12.012 -2.370  11.526  0.22 20.85 ?  21  ALA   A HB3  1 
ATOM   593  N N    A ASP   A 1 22  ? 12.124 1.061   10.232  0.78 16.58 ?  22  ASP   A N    1 
ATOM   594  N N    B ASP   A 1 22  ? 12.012 1.036   10.594  0.22 16.58 ?  22  ASP   A N    1 
ATOM   595  C CA   A ASP   A 1 22  ? 13.158 1.953   9.735   0.78 17.01 ?  22  ASP   A CA   1 
ATOM   596  C CA   B ASP   A 1 22  ? 13.072 1.932   10.150  0.22 16.52 ?  22  ASP   A CA   1 
ATOM   597  C C    A ASP   A 1 22  ? 14.488 1.467   10.300  0.78 15.80 ?  22  ASP   A C    1 
ATOM   598  C C    B ASP   A 1 22  ? 14.412 1.348   10.581  0.22 16.32 ?  22  ASP   A C    1 
ATOM   599  O O    A ASP   A 1 22  ? 14.683 1.466   11.520  0.78 16.37 ?  22  ASP   A O    1 
ATOM   600  O O    B ASP   A 1 22  ? 14.705 1.271   11.779  0.22 16.58 ?  22  ASP   A O    1 
ATOM   601  C CB   A ASP   A 1 22  ? 12.839 3.366   10.223  0.78 19.52 ?  22  ASP   A CB   1 
ATOM   602  C CB   B ASP   A 1 22  ? 12.839 3.289   10.809  0.22 16.56 ?  22  ASP   A CB   1 
ATOM   603  C CG   A ASP   A 1 22  ? 13.856 4.399   9.765   0.78 22.20 ?  22  ASP   A CG   1 
ATOM   604  C CG   B ASP   A 1 22  ? 13.715 4.380   10.243  0.22 16.43 ?  22  ASP   A CG   1 
ATOM   605  O OD1  A ASP   A 1 22  ? 14.883 4.020   9.167   0.78 22.34 ?  22  ASP   A OD1  1 
ATOM   606  O OD1  B ASP   A 1 22  ? 14.885 4.102   9.909   0.22 15.62 ?  22  ASP   A OD1  1 
ATOM   607  O OD2  A ASP   A 1 22  ? 13.632 5.603   10.022  0.78 24.37 -1 22  ASP   A OD2  1 
ATOM   608  O OD2  B ASP   A 1 22  ? 13.230 5.527   10.139  0.22 16.98 -1 22  ASP   A OD2  1 
ATOM   609  H H    A ASP   A 1 22  ? 11.732 1.352   10.949  0.78 19.91 ?  22  ASP   A H    1 
ATOM   610  H H    B ASP   A 1 22  ? 11.560 1.352   11.252  0.22 19.91 ?  22  ASP   A H    1 
ATOM   611  H HA   A ASP   A 1 22  ? 13.183 1.933   8.767   0.78 20.43 ?  22  ASP   A HA   1 
ATOM   612  H HA   B ASP   A 1 22  ? 13.056 2.040   9.182   0.22 19.84 ?  22  ASP   A HA   1 
ATOM   613  H HB2  A ASP   A 1 22  ? 11.952 3.613   9.905   0.78 23.44 ?  22  ASP   A HB2  1 
ATOM   614  H HB2  B ASP   A 1 22  ? 11.917 3.556   10.677  0.22 19.89 ?  22  ASP   A HB2  1 
ATOM   615  H HB3  A ASP   A 1 22  ? 12.848 3.369   11.194  0.78 23.44 ?  22  ASP   A HB3  1 
ATOM   616  H HB3  B ASP   A 1 22  ? 13.026 3.216   11.759  0.22 19.89 ?  22  ASP   A HB3  1 
ATOM   617  N N    A ILE   A 1 23  ? 15.392 1.035   9.416   0.78 15.46 ?  23  ILE   A N    1 
ATOM   618  N N    B ILE   A 1 23  ? 15.230 0.927   9.612   0.22 16.30 ?  23  ILE   A N    1 
ATOM   619  C CA   A ILE   A 1 23  ? 16.649 0.431   9.855   0.78 14.54 ?  23  ILE   A CA   1 
ATOM   620  C CA   B ILE   A 1 23  ? 16.497 0.279   9.949   0.22 16.06 ?  23  ILE   A CA   1 
ATOM   621  C C    A ILE   A 1 23  ? 17.451 1.382   10.734  0.78 14.58 ?  23  ILE   A C    1 
ATOM   622  C C    B ILE   A 1 23  ? 17.404 1.220   10.729  0.22 16.16 ?  23  ILE   A C    1 
ATOM   623  O O    A ILE   A 1 23  ? 18.181 0.942   11.631  0.78 14.91 ?  23  ILE   A O    1 
ATOM   624  O O    B ILE   A 1 23  ? 18.227 0.774   11.538  0.22 16.13 ?  23  ILE   A O    1 
ATOM   625  C CB   A ILE   A 1 23  ? 17.451 -0.073  8.634   0.78 13.79 ?  23  ILE   A CB   1 
ATOM   626  C CB   B ILE   A 1 23  ? 17.179 -0.285  8.685   0.22 15.73 ?  23  ILE   A CB   1 
ATOM   627  C CG1  A ILE   A 1 23  ? 18.621 -0.954  9.078   0.78 14.15 ?  23  ILE   A CG1  1 
ATOM   628  C CG1  B ILE   A 1 23  ? 18.311 -1.237  9.073   0.22 15.32 ?  23  ILE   A CG1  1 
ATOM   629  C CG2  A ILE   A 1 23  ? 17.930 1.095   7.770   0.78 14.09 ?  23  ILE   A CG2  1 
ATOM   630  C CG2  B ILE   A 1 23  ? 17.707 0.838   7.803   0.22 15.86 ?  23  ILE   A CG2  1 
ATOM   631  C CD1  A ILE   A 1 23  ? 19.345 -1.624  7.925   0.78 14.08 ?  23  ILE   A CD1  1 
ATOM   632  C CD1  B ILE   A 1 23  ? 18.932 -1.942  7.897   0.22 15.13 ?  23  ILE   A CD1  1 
ATOM   633  H H    A ILE   A 1 23  ? 15.292 1.075   8.570   0.78 18.57 ?  23  ILE   A H    1 
ATOM   634  H H    B ILE   A 1 23  ? 15.075 1.002   8.771   0.22 19.58 ?  23  ILE   A H    1 
ATOM   635  H HA   A ILE   A 1 23  ? 16.441 -0.343  10.398  0.78 17.46 ?  23  ILE   A HA   1 
ATOM   636  H HA   B ILE   A 1 23  ? 16.305 -0.474  10.525  0.22 19.28 ?  23  ILE   A HA   1 
ATOM   637  H HB   A ILE   A 1 23  ? 16.857 -0.619  8.096   0.78 16.56 ?  23  ILE   A HB   1 
ATOM   638  H HB   B ILE   A 1 23  ? 16.522 -0.785  8.179   0.22 18.88 ?  23  ILE   A HB   1 
ATOM   639  H HG12 A ILE   A 1 23  ? 19.266 -0.407  9.553   0.78 17.00 ?  23  ILE   A HG12 1 
ATOM   640  H HG12 B ILE   A 1 23  ? 19.010 -0.733  9.518   0.22 18.40 ?  23  ILE   A HG12 1 
ATOM   641  H HG13 A ILE   A 1 23  ? 18.288 -1.653  9.662   0.78 17.00 ?  23  ILE   A HG13 1 
ATOM   642  H HG13 B ILE   A 1 23  ? 17.960 -1.914  9.673   0.22 18.40 ?  23  ILE   A HG13 1 
ATOM   643  H HG21 A ILE   A 1 23  ? 18.275 0.745   6.932   0.78 16.93 ?  23  ILE   A HG21 1 
ATOM   644  H HG21 B ILE   A 1 23  ? 17.864 0.493   6.907   0.22 19.04 ?  23  ILE   A HG21 1 
ATOM   645  H HG22 A ILE   A 1 23  ? 17.180 1.685   7.596   0.78 16.93 ?  23  ILE   A HG22 1 
ATOM   646  H HG22 B ILE   A 1 23  ? 17.046 1.545   7.773   0.22 19.04 ?  23  ILE   A HG22 1 
ATOM   647  H HG23 A ILE   A 1 23  ? 18.627 1.573   8.242   0.78 16.93 ?  23  ILE   A HG23 1 
ATOM   648  H HG23 B ILE   A 1 23  ? 18.536 1.175   8.176   0.22 19.04 ?  23  ILE   A HG23 1 
ATOM   649  H HD11 A ILE   A 1 23  ? 20.006 -2.237  8.280   0.78 16.91 ?  23  ILE   A HD11 1 
ATOM   650  H HD11 B ILE   A 1 23  ? 19.568 -2.596  8.223   0.22 18.17 ?  23  ILE   A HD11 1 
ATOM   651  H HD12 A ILE   A 1 23  ? 18.701 -2.105  7.385   0.78 16.91 ?  23  ILE   A HD12 1 
ATOM   652  H HD12 B ILE   A 1 23  ? 18.230 -2.383  7.392   0.22 18.17 ?  23  ILE   A HD12 1 
ATOM   653  H HD13 A ILE   A 1 23  ? 19.782 -0.942  7.388   0.78 16.91 ?  23  ILE   A HD13 1 
ATOM   654  H HD13 B ILE   A 1 23  ? 19.381 -1.289  7.339   0.22 18.17 ?  23  ILE   A HD13 1 
ATOM   655  N N    A VAL   A 1 24  ? 17.327 2.692   10.504  0.78 15.71 ?  24  VAL   A N    1 
ATOM   656  N N    B VAL   A 1 24  ? 17.270 2.527   10.507  0.22 16.73 ?  24  VAL   A N    1 
ATOM   657  C CA   A VAL   A 1 24  ? 18.014 3.664   11.352  0.78 17.41 ?  24  VAL   A CA   1 
ATOM   658  C CA   B VAL   A 1 24  ? 18.029 3.498   11.288  0.22 17.38 ?  24  VAL   A CA   1 
ATOM   659  C C    A VAL   A 1 24  ? 17.500 3.573   12.782  0.78 18.19 ?  24  VAL   A C    1 
ATOM   660  C C    B VAL   A 1 24  ? 17.589 3.462   12.747  0.22 18.07 ?  24  VAL   A C    1 
ATOM   661  O O    A VAL   A 1 24  ? 18.276 3.483   13.740  0.78 18.11 ?  24  VAL   A O    1 
ATOM   662  O O    B VAL   A 1 24  ? 18.418 3.443   13.665  0.22 18.06 ?  24  VAL   A O    1 
ATOM   663  C CB   A VAL   A 1 24  ? 17.849 5.085   10.782  0.78 18.58 ?  24  VAL   A CB   1 
ATOM   664  C CB   B VAL   A 1 24  ? 17.872 4.903   10.680  0.22 17.57 ?  24  VAL   A CB   1 
ATOM   665  C CG1  A VAL   A 1 24  ? 18.337 6.132   11.781  0.78 19.39 ?  24  VAL   A CG1  1 
ATOM   666  C CG1  B VAL   A 1 24  ? 18.670 5.915   11.475  0.22 17.79 ?  24  VAL   A CG1  1 
ATOM   667  C CG2  A VAL   A 1 24  ? 18.587 5.215   9.458   0.78 19.64 ?  24  VAL   A CG2  1 
ATOM   668  C CG2  B VAL   A 1 24  ? 18.293 4.898   9.213   0.22 17.66 ?  24  VAL   A CG2  1 
ATOM   669  H H    A VAL   A 1 24  ? 16.854 3.039   9.877   0.78 18.87 ?  24  VAL   A H    1 
ATOM   670  H H    B VAL   A 1 24  ? 16.755 2.873   9.915   0.22 20.09 ?  24  VAL   A H    1 
ATOM   671  H HA   A VAL   A 1 24  ? 18.962 3.459   11.363  0.78 20.91 ?  24  VAL   A HA   1 
ATOM   672  H HA   B VAL   A 1 24  ? 18.971 3.266   11.256  0.22 20.88 ?  24  VAL   A HA   1 
ATOM   673  H HB   A VAL   A 1 24  ? 16.909 5.248   10.612  0.78 22.31 ?  24  VAL   A HB   1 
ATOM   674  H HB   B VAL   A 1 24  ? 16.939 5.162   10.720  0.22 21.10 ?  24  VAL   A HB   1 
ATOM   675  H HG11 A VAL   A 1 24  ? 18.485 6.967   11.311  0.78 23.29 ?  24  VAL   A HG11 1 
ATOM   676  H HG11 B VAL   A 1 24  ? 18.662 6.759   11.000  0.22 21.36 ?  24  VAL   A HG11 1 
ATOM   677  H HG12 A VAL   A 1 24  ? 17.661 6.254   12.465  0.78 23.29 ?  24  VAL   A HG12 1 
ATOM   678  H HG12 B VAL   A 1 24  ? 18.261 6.023   12.347  0.22 21.36 ?  24  VAL   A HG12 1 
ATOM   679  H HG13 A VAL   A 1 24  ? 19.165 5.825   12.179  0.78 23.29 ?  24  VAL   A HG13 1 
ATOM   680  H HG13 B VAL   A 1 24  ? 19.578 5.592   11.568  0.22 21.36 ?  24  VAL   A HG13 1 
ATOM   681  H HG21 A VAL   A 1 24  ? 18.440 6.103   9.099   0.78 23.58 ?  24  VAL   A HG21 1 
ATOM   682  H HG21 B VAL   A 1 24  ? 18.680 5.759   8.987   0.22 21.21 ?  24  VAL   A HG21 1 
ATOM   683  H HG22 A VAL   A 1 24  ? 19.535 5.072   9.610   0.78 23.58 ?  24  VAL   A HG22 1 
ATOM   684  H HG22 B VAL   A 1 24  ? 18.946 4.195   9.077   0.22 21.21 ?  24  VAL   A HG22 1 
ATOM   685  H HG23 A VAL   A 1 24  ? 18.248 4.548   8.839   0.78 23.58 ?  24  VAL   A HG23 1 
ATOM   686  H HG23 B VAL   A 1 24  ? 17.513 4.728   8.663   0.22 21.21 ?  24  VAL   A HG23 1 
ATOM   687  N N    A GLU   A 1 25  ? 16.177 3.591   12.945  0.78 19.49 ?  25  GLU   A N    1 
ATOM   688  N N    B GLU   A 1 25  ? 16.275 3.450   12.982  0.22 18.97 ?  25  GLU   A N    1 
ATOM   689  C CA   A GLU   A 1 25  ? 15.598 3.509   14.281  0.78 21.17 ?  25  GLU   A CA   1 
ATOM   690  C CA   B GLU   A 1 25  ? 15.764 3.406   14.349  0.22 20.12 ?  25  GLU   A CA   1 
ATOM   691  C C    A GLU   A 1 25  ? 15.833 2.137   14.901  0.78 20.15 ?  25  GLU   A C    1 
ATOM   692  C C    B GLU   A 1 25  ? 16.067 2.066   15.010  0.22 19.76 ?  25  GLU   A C    1 
ATOM   693  O O    A GLU   A 1 25  ? 16.070 2.029   16.109  0.78 20.59 ?  25  GLU   A O    1 
ATOM   694  O O    B GLU   A 1 25  ? 16.408 2.016   16.197  0.22 19.66 ?  25  GLU   A O    1 
ATOM   695  C CB   A GLU   A 1 25  ? 14.108 3.851   14.227  0.78 23.85 ?  25  GLU   A CB   1 
ATOM   696  C CB   B GLU   A 1 25  ? 14.259 3.676   14.350  0.22 21.50 ?  25  GLU   A CB   1 
ATOM   697  C CG   A GLU   A 1 25  ? 13.839 5.284   13.798  0.78 26.99 ?  25  GLU   A CG   1 
ATOM   698  C CG   B GLU   A 1 25  ? 13.878 5.091   13.942  0.22 22.85 ?  25  GLU   A CG   1 
ATOM   699  C CD   A GLU   A 1 25  ? 14.616 6.298   14.622  0.78 29.75 ?  25  GLU   A CD   1 
ATOM   700  C CD   B GLU   A 1 25  ? 14.156 6.104   15.035  0.22 24.02 ?  25  GLU   A CD   1 
ATOM   701  O OE1  A GLU   A 1 25  ? 14.683 6.140   15.859  0.78 30.83 ?  25  GLU   A OE1  1 
ATOM   702  O OE1  B GLU   A 1 25  ? 14.393 5.686   16.189  0.22 24.23 ?  25  GLU   A OE1  1 
ATOM   703  O OE2  A GLU   A 1 25  ? 15.178 7.242   14.029  0.78 30.84 -1 25  GLU   A OE2  1 
ATOM   704  O OE2  B GLU   A 1 25  ? 14.141 7.318   14.741  0.22 24.47 -1 25  GLU   A OE2  1 
ATOM   705  H H    A GLU   A 1 25  ? 15.605 3.651   12.308  0.78 23.40 ?  25  GLU   A H    1 
ATOM   706  H H    B GLU   A 1 25  ? 15.670 3.466   12.373  0.22 22.78 ?  25  GLU   A H    1 
ATOM   707  H HA   A GLU   A 1 25  ? 16.031 4.160   14.850  0.78 25.42 ?  25  GLU   A HA   1 
ATOM   708  H HA   B GLU   A 1 25  ? 16.192 4.103   14.869  0.22 24.16 ?  25  GLU   A HA   1 
ATOM   709  H HB2  A GLU   A 1 25  ? 13.669 3.265   13.589  0.78 28.64 ?  25  GLU   A HB2  1 
ATOM   710  H HB2  B GLU   A 1 25  ? 13.832 3.064   13.734  0.22 25.81 ?  25  GLU   A HB2  1 
ATOM   711  H HB3  A GLU   A 1 25  ? 13.721 3.728   15.108  0.78 28.64 ?  25  GLU   A HB3  1 
ATOM   712  H HB3  B GLU   A 1 25  ? 13.917 3.528   15.244  0.22 25.81 ?  25  GLU   A HB3  1 
ATOM   713  H HG2  A GLU   A 1 25  ? 14.114 5.394   12.877  0.78 32.41 ?  25  GLU   A HG2  1 
ATOM   714  H HG2  B GLU   A 1 25  ? 14.396 5.349   13.164  0.22 27.44 ?  25  GLU   A HG2  1 
ATOM   715  H HG3  A GLU   A 1 25  ? 12.889 5.467   13.888  0.78 32.41 ?  25  GLU   A HG3  1 
ATOM   716  H HG3  B GLU   A 1 25  ? 12.930 5.117   13.732  0.22 27.44 ?  25  GLU   A HG3  1 
ATOM   717  N N    A GLU   A 1 26  ? 15.792 1.079   14.089  0.78 19.65 ?  26  GLU   A N    1 
ATOM   718  N N    B GLU   A 1 26  ? 15.948 0.970   14.257  0.22 19.61 ?  26  GLU   A N    1 
ATOM   719  C CA   A GLU   A 1 26  ? 16.106 -0.256  14.593  0.78 19.16 ?  26  GLU   A CA   1 
ATOM   720  C CA   B GLU   A 1 26  ? 16.265 -0.345  14.807  0.22 19.66 ?  26  GLU   A CA   1 
ATOM   721  C C    A GLU   A 1 26  ? 17.534 -0.316  15.125  0.78 17.61 ?  26  GLU   A C    1 
ATOM   722  C C    B GLU   A 1 26  ? 17.727 -0.430  15.217  0.22 19.17 ?  26  GLU   A C    1 
ATOM   723  O O    A GLU   A 1 26  ? 17.784 -0.840  16.217  0.78 17.48 ?  26  GLU   A O    1 
ATOM   724  O O    B GLU   A 1 26  ? 18.059 -1.024  16.250  0.22 19.01 ?  26  GLU   A O    1 
ATOM   725  C CB   A GLU   A 1 26  ? 15.927 -1.295  13.483  0.78 20.95 ?  26  GLU   A CB   1 
ATOM   726  C CB   B GLU   A 1 26  ? 15.946 -1.428  13.779  0.22 20.35 ?  26  GLU   A CB   1 
ATOM   727  C CG   A GLU   A 1 26  ? 14.546 -1.912  13.358  0.78 22.87 ?  26  GLU   A CG   1 
ATOM   728  C CG   B GLU   A 1 26  ? 14.465 -1.644  13.552  0.22 21.43 ?  26  GLU   A CG   1 
ATOM   729  C CD   A GLU   A 1 26  ? 14.108 -2.683  14.595  0.78 23.45 ?  26  GLU   A CD   1 
ATOM   730  C CD   B GLU   A 1 26  ? 13.786 -2.367  14.699  0.22 21.97 ?  26  GLU   A CD   1 
ATOM   731  O OE1  A GLU   A 1 26  ? 14.565 -3.828  14.844  0.78 23.79 ?  26  GLU   A OE1  1 
ATOM   732  O OE1  B GLU   A 1 26  ? 14.417 -3.261  15.300  0.22 22.19 ?  26  GLU   A OE1  1 
ATOM   733  O OE2  A GLU   A 1 26  ? 13.277 -2.127  15.321  0.78 24.00 -1 26  GLU   A OE2  1 
ATOM   734  O OE2  B GLU   A 1 26  ? 12.621 -2.034  14.999  0.22 22.38 -1 26  GLU   A OE2  1 
ATOM   735  H H    A GLU   A 1 26  ? 15.587 1.111   13.255  0.78 23.60 ?  26  GLU   A H    1 
ATOM   736  H H    B GLU   A 1 26  ? 15.694 0.963   13.437  0.22 23.55 ?  26  GLU   A H    1 
ATOM   737  H HA   A GLU   A 1 26  ? 15.501 -0.472  15.315  0.78 23.01 ?  26  GLU   A HA   1 
ATOM   738  H HA   B GLU   A 1 26  ? 15.720 -0.502  15.593  0.22 23.61 ?  26  GLU   A HA   1 
ATOM   739  H HB2  A GLU   A 1 26  ? 16.133 -0.872  12.633  0.78 25.16 ?  26  GLU   A HB2  1 
ATOM   740  H HB2  B GLU   A 1 26  ? 16.344 -1.176  12.929  0.22 24.44 ?  26  GLU   A HB2  1 
ATOM   741  H HB3  A GLU   A 1 26  ? 16.553 -2.017  13.641  0.78 25.16 ?  26  GLU   A HB3  1 
ATOM   742  H HB3  B GLU   A 1 26  ? 16.330 -2.266  14.082  0.22 24.44 ?  26  GLU   A HB3  1 
ATOM   743  H HG2  A GLU   A 1 26  ? 13.904 -1.198  13.205  0.78 27.46 ?  26  GLU   A HG2  1 
ATOM   744  H HG2  B GLU   A 1 26  ? 14.035 -0.782  13.461  0.22 25.73 ?  26  GLU   A HG2  1 
ATOM   745  H HG3  A GLU   A 1 26  ? 14.539 -2.527  12.611  0.78 27.46 ?  26  GLU   A HG3  1 
ATOM   746  H HG3  B GLU   A 1 26  ? 14.348 -2.167  12.745  0.22 25.73 ?  26  GLU   A HG3  1 
ATOM   747  N N    A ALA   A 1 27  ? 18.491 0.213   14.361  0.78 16.34 ?  27  ALA   A N    1 
ATOM   748  N N    B ALA   A 1 27  ? 18.621 0.146   14.412  0.22 18.86 ?  27  ALA   A N    1 
ATOM   749  C CA   A ALA   A 1 27  ? 19.885 0.149   14.789  0.78 15.98 ?  27  ALA   A CA   1 
ATOM   750  C CA   B ALA   A 1 27  ? 20.029 0.180   14.786  0.22 18.78 ?  27  ALA   A CA   1 
ATOM   751  C C    A ALA   A 1 27  ? 20.104 0.940   16.073  0.78 17.14 ?  27  ALA   A C    1 
ATOM   752  C C    B ALA   A 1 27  ? 20.237 1.014   16.041  0.22 19.04 ?  27  ALA   A C    1 
ATOM   753  O O    A ALA   A 1 27  ? 20.770 0.465   17.000  0.78 17.17 ?  27  ALA   A O    1 
ATOM   754  O O    B ALA   A 1 27  ? 21.023 0.640   16.920  0.22 19.03 ?  27  ALA   A O    1 
ATOM   755  C CB   A ALA   A 1 27  ? 20.803 0.652   13.674  0.78 15.67 ?  27  ALA   A CB   1 
ATOM   756  C CB   B ALA   A 1 27  ? 20.868 0.721   13.628  0.22 18.66 ?  27  ALA   A CB   1 
ATOM   757  H H    A ALA   A 1 27  ? 18.360 0.611   13.610  0.78 19.63 ?  27  ALA   A H    1 
ATOM   758  H H    B ALA   A 1 27  ? 18.441 0.514   13.658  0.22 22.65 ?  27  ALA   A H    1 
ATOM   759  H HA   A ALA   A 1 27  ? 20.111 -0.773  14.971  0.78 19.19 ?  27  ALA   A HA   1 
ATOM   760  H HA   B ALA   A 1 27  ? 20.328 -0.722  14.977  0.22 22.54 ?  27  ALA   A HA   1 
ATOM   761  H HB1  A ALA   A 1 27  ? 21.724 0.599   13.980  0.78 18.82 ?  27  ALA   A HB1  1 
ATOM   762  H HB1  B ALA   A 1 27  ? 21.803 0.724   13.891  0.22 22.41 ?  27  ALA   A HB1  1 
ATOM   763  H HB2  A ALA   A 1 27  ? 20.682 0.092   12.893  0.78 18.82 ?  27  ALA   A HB2  1 
ATOM   764  H HB2  B ALA   A 1 27  ? 20.745 0.146   12.857  0.22 22.41 ?  27  ALA   A HB2  1 
ATOM   765  H HB3  A ALA   A 1 27  ? 20.576 1.570   13.466  0.78 18.82 ?  27  ALA   A HB3  1 
ATOM   766  H HB3  B ALA   A 1 27  ? 20.579 1.622   13.421  0.22 22.41 ?  27  ALA   A HB3  1 
ATOM   767  N N    . LYS   A 1 28  ? 19.535 2.146   16.152  1.00 19.60 ?  28  LYS   A N    1 
ATOM   768  C CA   . LYS   A 1 28  ? 19.680 2.969   17.349  1.00 22.97 ?  28  LYS   A CA   1 
ATOM   769  C C    . LYS   A 1 28  ? 19.157 2.257   18.590  1.00 23.99 ?  28  LYS   A C    1 
ATOM   770  O O    . LYS   A 1 28  ? 19.721 2.417   19.678  1.00 25.76 ?  28  LYS   A O    1 
ATOM   771  C CB   . LYS   A 1 28  ? 18.981 4.319   17.158  1.00 25.70 ?  28  LYS   A CB   1 
ATOM   772  C CG   . LYS   A 1 28  ? 19.761 5.279   16.271  1.00 28.26 ?  28  LYS   A CG   1 
ATOM   773  C CD   . LYS   A 1 28  ? 19.273 6.714   16.398  1.00 31.26 ?  28  LYS   A CD   1 
ATOM   774  C CE   . LYS   A 1 28  ? 18.005 6.945   15.602  1.00 33.69 ?  28  LYS   A CE   1 
ATOM   775  N NZ   . LYS   A 1 28  ? 17.647 8.391   15.560  1.00 35.18 ?  28  LYS   A NZ   1 
ATOM   776  H H    A LYS   A 1 28  ? 19.062 2.506   15.532  0.78 23.54 ?  28  LYS   A H    1 
ATOM   777  H H    B LYS   A 1 28  ? 18.983 2.449   15.568  0.22 23.54 ?  28  LYS   A H    1 
ATOM   778  H HA   . LYS   A 1 28  ? 20.619 3.148   17.495  1.00 27.58 ?  28  LYS   A HA   1 
ATOM   779  H HB2  . LYS   A 1 28  ? 18.116 4.172   16.745  1.00 30.86 ?  28  LYS   A HB2  1 
ATOM   780  H HB3  . LYS   A 1 28  ? 18.866 4.743   18.023  1.00 30.86 ?  28  LYS   A HB3  1 
ATOM   781  H HG2  . LYS   A 1 28  ? 20.696 5.257   16.525  1.00 33.92 ?  28  LYS   A HG2  1 
ATOM   782  H HG3  . LYS   A 1 28  ? 19.659 5.009   15.345  1.00 33.92 ?  28  LYS   A HG3  1 
ATOM   783  H HD2  . LYS   A 1 28  ? 19.086 6.908   17.331  1.00 37.53 ?  28  LYS   A HD2  1 
ATOM   784  H HD3  . LYS   A 1 28  ? 19.956 7.315   16.062  1.00 37.53 ?  28  LYS   A HD3  1 
ATOM   785  H HE2  . LYS   A 1 28  ? 18.138 6.638   14.692  1.00 40.44 ?  28  LYS   A HE2  1 
ATOM   786  H HE3  . LYS   A 1 28  ? 17.273 6.462   16.017  1.00 40.44 ?  28  LYS   A HE3  1 
ATOM   787  H HZ1  . LYS   A 1 28  ? 16.902 8.507   15.088  1.00 42.23 ?  28  LYS   A HZ1  1 
ATOM   788  H HZ2  . LYS   A 1 28  ? 17.518 8.697   16.386  1.00 42.23 ?  28  LYS   A HZ2  1 
ATOM   789  H HZ3  . LYS   A 1 28  ? 18.305 8.856   15.180  1.00 42.23 ?  28  LYS   A HZ3  1 
ATOM   790  N N    . LYS   A 1 29  ? 18.099 1.457   18.445  1.00 24.57 ?  29  LYS   A N    1 
ATOM   791  C CA   . LYS   A 1 29  ? 17.512 0.759   19.586  1.00 26.52 ?  29  LYS   A CA   1 
ATOM   792  C C    . LYS   A 1 29  ? 18.323 -0.475  19.968  1.00 24.69 ?  29  LYS   A C    1 
ATOM   793  O O    . LYS   A 1 29  ? 18.615 -0.698  21.149  1.00 25.37 ?  29  LYS   A O    1 
ATOM   794  C CB   . LYS   A 1 29  ? 16.074 0.356   19.246  1.00 30.45 ?  29  LYS   A CB   1 
ATOM   795  C CG   . LYS   A 1 29  ? 15.320 -0.324  20.382  1.00 34.46 ?  29  LYS   A CG   1 
ATOM   796  C CD   . LYS   A 1 29  ? 14.899 0.678   21.445  1.00 38.07 ?  29  LYS   A CD   1 
ATOM   797  C CE   . LYS   A 1 29  ? 14.002 0.037   22.493  1.00 40.59 ?  29  LYS   A CE   1 
ATOM   798  N NZ   . LYS   A 1 29  ? 13.517 1.031   23.490  1.00 41.97 ?  29  LYS   A NZ   1 
ATOM   799  H H    . LYS   A 1 29  ? 17.707 1.301   17.695  1.00 29.49 ?  29  LYS   A H    1 
ATOM   800  H HA   . LYS   A 1 29  ? 17.486 1.356   20.347  1.00 31.84 ?  29  LYS   A HA   1 
ATOM   801  H HB2  . LYS   A 1 29  ? 15.577 1.152   19.002  1.00 36.55 ?  29  LYS   A HB2  1 
ATOM   802  H HB3  . LYS   A 1 29  ? 16.092 -0.260  18.497  1.00 36.55 ?  29  LYS   A HB3  1 
ATOM   803  H HG2  . LYS   A 1 29  ? 14.519 -0.743  20.027  1.00 41.37 ?  29  LYS   A HG2  1 
ATOM   804  H HG3  . LYS   A 1 29  ? 15.886 -0.993  20.800  1.00 41.37 ?  29  LYS   A HG3  1 
ATOM   805  H HD2  . LYS   A 1 29  ? 15.689 1.023   21.890  1.00 45.70 ?  29  LYS   A HD2  1 
ATOM   806  H HD3  . LYS   A 1 29  ? 14.407 1.401   21.024  1.00 45.70 ?  29  LYS   A HD3  1 
ATOM   807  H HE2  . LYS   A 1 29  ? 13.229 -0.355  22.056  1.00 48.72 ?  29  LYS   A HE2  1 
ATOM   808  H HE3  . LYS   A 1 29  ? 14.501 -0.648  22.965  1.00 48.72 ?  29  LYS   A HE3  1 
ATOM   809  H HZ1  . LYS   A 1 29  ? 12.996 0.631   24.090  1.00 50.38 ?  29  LYS   A HZ1  1 
ATOM   810  H HZ2  . LYS   A 1 29  ? 14.209 1.402   23.909  1.00 50.38 ?  29  LYS   A HZ2  1 
ATOM   811  H HZ3  . LYS   A 1 29  ? 13.050 1.669   23.081  1.00 50.38 ?  29  LYS   A HZ3  1 
ATOM   812  N N    . VAL   A 1 30  ? 18.674 -1.297  18.981  1.00 23.21 ?  30  VAL   A N    1 
ATOM   813  C CA   . VAL   A 1 30  ? 19.302 -2.583  19.258  1.00 22.21 ?  30  VAL   A CA   1 
ATOM   814  C C    . VAL   A 1 30  ? 20.811 -2.452  19.444  1.00 20.98 ?  30  VAL   A C    1 
ATOM   815  O O    . VAL   A 1 30  ? 21.410 -3.199  20.227  1.00 21.16 ?  30  VAL   A O    1 
ATOM   816  C CB   . VAL   A 1 30  ? 18.955 -3.558  18.119  1.00 22.77 ?  30  VAL   A CB   1 
ATOM   817  C CG1  . VAL   A 1 30  ? 19.690 -4.881  18.291  1.00 23.10 ?  30  VAL   A CG1  1 
ATOM   818  C CG2  . VAL   A 1 30  ? 17.448 -3.778  18.052  1.00 23.60 ?  30  VAL   A CG2  1 
ATOM   819  H H    . VAL   A 1 30  ? 18.549 -1.139  18.143  1.00 27.87 ?  30  VAL   A H    1 
ATOM   820  H HA   . VAL   A 1 30  ? 18.925 -2.943  20.075  1.00 26.67 ?  30  VAL   A HA   1 
ATOM   821  H HB   . VAL   A 1 30  ? 19.233 -3.172  17.275  1.00 27.33 ?  30  VAL   A HB   1 
ATOM   822  H HG11 . VAL   A 1 30  ? 19.292 -5.541  17.699  1.00 27.74 ?  30  VAL   A HG11 1 
ATOM   823  H HG12 . VAL   A 1 30  ? 20.623 -4.758  18.064  1.00 27.74 ?  30  VAL   A HG12 1 
ATOM   824  H HG13 . VAL   A 1 30  ? 19.604 -5.172  19.212  1.00 27.74 ?  30  VAL   A HG13 1 
ATOM   825  H HG21 . VAL   A 1 30  ? 17.254 -4.444  17.374  1.00 28.33 ?  30  VAL   A HG21 1 
ATOM   826  H HG22 . VAL   A 1 30  ? 17.135 -4.087  18.917  1.00 28.33 ?  30  VAL   A HG22 1 
ATOM   827  H HG23 . VAL   A 1 30  ? 17.016 -2.940  17.824  1.00 28.33 ?  30  VAL   A HG23 1 
ATOM   828  N N    A LYS   A 1 31  ? 21.446 -1.515  18.749  0.78 19.74 ?  31  LYS   A N    1 
ATOM   829  N N    B LYS   A 1 31  ? 21.439 -1.503  18.760  0.22 21.41 ?  31  LYS   A N    1 
ATOM   830  C CA   A LYS   A 1 31  ? 22.900 -1.419  18.688  0.78 20.15 ?  31  LYS   A CA   1 
ATOM   831  C CA   B LYS   A 1 31  ? 22.891 -1.411  18.677  0.22 22.17 ?  31  LYS   A CA   1 
ATOM   832  C C    A LYS   A 1 31  ? 23.503 -2.776  18.312  0.78 18.42 ?  31  LYS   A C    1 
ATOM   833  C C    B LYS   A 1 31  ? 23.490 -2.773  18.317  0.22 19.75 ?  31  LYS   A C    1 
ATOM   834  O O    A LYS   A 1 31  ? 24.290 -3.348  19.073  0.78 19.05 ?  31  LYS   A O    1 
ATOM   835  O O    B LYS   A 1 31  ? 24.268 -3.342  19.088  0.22 20.18 ?  31  LYS   A O    1 
ATOM   836  C CB   A LYS   A 1 31  ? 23.491 -0.894  19.989  0.78 24.94 ?  31  LYS   A CB   1 
ATOM   837  C CB   B LYS   A 1 31  ? 23.501 -0.863  19.960  0.22 25.67 ?  31  LYS   A CB   1 
ATOM   838  C CG   A LYS   A 1 31  ? 22.770 0.334   20.537  0.78 30.73 ?  31  LYS   A CG   1 
ATOM   839  C CG   B LYS   A 1 31  ? 22.846 0.423   20.449  0.22 29.02 ?  31  LYS   A CG   1 
ATOM   840  C CD   A LYS   A 1 31  ? 23.728 1.487   20.807  0.78 35.12 ?  31  LYS   A CD   1 
ATOM   841  C CD   B LYS   A 1 31  ? 23.876 1.427   20.944  0.22 31.59 ?  31  LYS   A CD   1 
ATOM   842  C CE   A LYS   A 1 31  ? 23.102 2.534   21.724  0.78 38.02 ?  31  LYS   A CE   1 
ATOM   843  C CE   B LYS   A 1 31  ? 23.230 2.537   21.763  0.22 33.24 ?  31  LYS   A CE   1 
ATOM   844  N NZ   A LYS   A 1 31  ? 21.866 3.143   21.156  0.78 39.60 ?  31  LYS   A NZ   1 
ATOM   845  N NZ   B LYS   A 1 31  ? 22.107 3.206   21.049  0.22 34.17 ?  31  LYS   A NZ   1 
ATOM   846  H H    A LYS   A 1 31  ? 21.044 -0.905  18.297  0.78 23.71 ?  31  LYS   A H    1 
ATOM   847  H H    B LYS   A 1 31  ? 21.032 -0.882  18.328  0.22 25.71 ?  31  LYS   A H    1 
ATOM   848  H HA   A LYS   A 1 31  ? 23.131 -0.794  17.990  0.78 24.20 ?  31  LYS   A HA   1 
ATOM   849  H HA   B LYS   A 1 31  ? 23.113 -0.796  17.967  0.22 26.62 ?  31  LYS   A HA   1 
ATOM   850  H HB2  A LYS   A 1 31  ? 23.448 -1.589  20.660  0.78 29.94 ?  31  LYS   A HB2  1 
ATOM   851  H HB2  B LYS   A 1 31  ? 23.414 -1.525  20.661  0.22 30.81 ?  31  LYS   A HB2  1 
ATOM   852  H HB3  A LYS   A 1 31  ? 24.418 -0.646  19.830  0.78 29.94 ?  31  LYS   A HB3  1 
ATOM   853  H HB3  B LYS   A 1 31  ? 24.440 -0.673  19.800  0.22 30.81 ?  31  LYS   A HB3  1 
ATOM   854  H HG2  A LYS   A 1 31  ? 22.113 0.636   19.891  0.78 36.88 ?  31  LYS   A HG2  1 
ATOM   855  H HG2  B LYS   A 1 31  ? 22.354 0.830   19.719  0.22 34.84 ?  31  LYS   A HG2  1 
ATOM   856  H HG3  A LYS   A 1 31  ? 22.334 0.100   21.371  0.78 36.88 ?  31  LYS   A HG3  1 
ATOM   857  H HG3  B LYS   A 1 31  ? 22.247 0.217   21.183  0.22 34.84 ?  31  LYS   A HG3  1 
ATOM   858  H HD2  A LYS   A 1 31  ? 24.528 1.148   21.237  0.78 42.15 ?  31  LYS   A HD2  1 
ATOM   859  H HD2  B LYS   A 1 31  ? 24.522 0.971   21.506  0.22 37.92 ?  31  LYS   A HD2  1 
ATOM   860  H HD3  A LYS   A 1 31  ? 23.955 1.917   19.966  0.78 42.15 ?  31  LYS   A HD3  1 
ATOM   861  H HD3  B LYS   A 1 31  ? 24.321 1.831   20.182  0.22 37.92 ?  31  LYS   A HD3  1 
ATOM   862  H HE2  A LYS   A 1 31  ? 22.867 2.114   22.567  0.78 45.64 ?  31  LYS   A HE2  1 
ATOM   863  H HE2  B LYS   A 1 31  ? 22.879 2.160   22.585  0.22 39.90 ?  31  LYS   A HE2  1 
ATOM   864  H HE3  A LYS   A 1 31  ? 23.743 3.246   21.875  0.78 45.64 ?  31  LYS   A HE3  1 
ATOM   865  H HE3  B LYS   A 1 31  ? 23.899 3.210   21.966  0.22 39.90 ?  31  LYS   A HE3  1 
ATOM   866  H HZ1  A LYS   A 1 31  ? 21.536 3.746   21.722  0.78 47.54 ?  31  LYS   A HZ1  1 
ATOM   867  H HZ1  B LYS   A 1 31  ? 21.775 3.862   21.551  0.22 41.02 ?  31  LYS   A HZ1  1 
ATOM   868  H HZ2  A LYS   A 1 31  ? 22.051 3.543   20.383  0.78 47.54 ?  31  LYS   A HZ2  1 
ATOM   869  H HZ2  B LYS   A 1 31  ? 22.395 3.548   20.280  0.22 41.02 ?  31  LYS   A HZ2  1 
ATOM   870  H HZ3  A LYS   A 1 31  ? 21.252 2.513   21.016  0.78 47.54 ?  31  LYS   A HZ3  1 
ATOM   871  H HZ3  B LYS   A 1 31  ? 21.460 2.618   20.879  0.22 41.02 ?  31  LYS   A HZ3  1 
ATOM   872  N N    . PRO   A 1 32  ? 23.143 -3.316  17.154  1.00 17.05 ?  32  PRO   A N    1 
ATOM   873  C CA   . PRO   A 1 32  ? 23.615 -4.650  16.787  1.00 16.70 ?  32  PRO   A CA   1 
ATOM   874  C C    . PRO   A 1 32  ? 25.111 -4.662  16.552  1.00 16.53 ?  32  PRO   A C    1 
ATOM   875  O O    . PRO   A 1 32  ? 25.746 -3.631  16.323  1.00 16.50 ?  32  PRO   A O    1 
ATOM   876  C CB   . PRO   A 1 32  ? 22.859 -4.935  15.486  1.00 17.26 ?  32  PRO   A CB   1 
ATOM   877  C CG   . PRO   A 1 32  ? 22.661 -3.568  14.887  1.00 16.25 ?  32  PRO   A CG   1 
ATOM   878  C CD   . PRO   A 1 32  ? 22.397 -2.672  16.061  1.00 16.26 ?  32  PRO   A CD   1 
ATOM   879  H HA   . PRO   A 1 32  ? 23.386 -5.303  17.464  1.00 20.06 ?  32  PRO   A HA   1 
ATOM   880  H HB2  . PRO   A 1 32  ? 23.395 -5.503  14.907  1.00 20.73 ?  32  PRO   A HB2  1 
ATOM   881  H HB3  . PRO   A 1 32  ? 22.008 -5.359  15.690  1.00 20.73 ?  32  PRO   A HB3  1 
ATOM   882  H HG2  . PRO   A 1 32  ? 23.463 -3.309  14.413  1.00 19.51 ?  32  PRO   A HG2  1 
ATOM   883  H HG3  . PRO   A 1 32  ? 21.897 -3.594  14.286  1.00 19.51 ?  32  PRO   A HG3  1 
ATOM   884  H HD2  . PRO   A 1 32  ? 22.749 -1.788  15.874  1.00 19.53 ?  32  PRO   A HD2  1 
ATOM   885  H HD3  . PRO   A 1 32  ? 21.454 -2.653  16.258  1.00 19.53 ?  32  PRO   A HD3  1 
ATOM   886  N N    . THR   A 1 33  ? 25.673 -5.869  16.589  1.00 16.43 ?  33  THR   A N    1 
ATOM   887  C CA   . THR   A 1 33  ? 27.078 -6.027  16.244  1.00 16.76 ?  33  THR   A CA   1 
ATOM   888  C C    . THR   A 1 33  ? 27.346 -5.554  14.823  1.00 15.23 ?  33  THR   A C    1 
ATOM   889  O O    . THR   A 1 33  ? 28.370 -4.909  14.563  1.00 15.20 ?  33  THR   A O    1 
ATOM   890  C CB   . THR   A 1 33  ? 27.493 -7.486  16.427  1.00 18.41 ?  33  THR   A CB   1 
ATOM   891  O OG1  . THR   A 1 33  ? 27.174 -7.897  17.760  1.00 20.34 ?  33  THR   A OG1  1 
ATOM   892  C CG2  . THR   A 1 33  ? 28.988 -7.663  16.183  1.00 19.92 ?  33  THR   A CG2  1 
ATOM   893  H H    . THR   A 1 33  ? 25.272 -6.600  16.792  1.00 19.73 ?  33  THR   A H    1 
ATOM   894  H HA   . THR   A 1 33  ? 27.619 -5.491  16.842  1.00 20.13 ?  33  THR   A HA   1 
ATOM   895  H HB   . THR   A 1 33  ? 27.018 -8.050  15.795  1.00 22.11 ?  33  THR   A HB   1 
ATOM   896  H HG1  . THR   A 1 33  ? 27.598 -7.428  18.317  1.00 24.42 ?  33  THR   A HG1  1 
ATOM   897  H HG21 . THR   A 1 33  ? 29.268 -8.556  16.445  1.00 23.92 ?  33  THR   A HG21 1 
ATOM   898  H HG22 . THR   A 1 33  ? 29.192 -7.536  15.243  1.00 23.92 ?  33  THR   A HG22 1 
ATOM   899  H HG23 . THR   A 1 33  ? 29.487 -7.015  16.705  1.00 23.92 ?  33  THR   A HG23 1 
ATOM   900  N N    . VAL   A 1 34  ? 26.437 -5.857  13.896  1.00 13.60 ?  34  VAL   A N    1 
ATOM   901  C CA   . VAL   A 1 34  ? 26.598 -5.512  12.488  1.00 12.51 ?  34  VAL   A CA   1 
ATOM   902  C C    . VAL   A 1 34  ? 25.288 -4.943  11.949  1.00 11.82 ?  34  VAL   A C    1 
ATOM   903  O O    . VAL   A 1 34  ? 24.246 -5.609  12.005  1.00 12.58 ?  34  VAL   A O    1 
ATOM   904  C CB   . VAL   A 1 34  ? 27.040 -6.717  11.632  1.00 13.39 ?  34  VAL   A CB   1 
ATOM   905  C CG1  . VAL   A 1 34  ? 27.212 -6.295  10.180  1.00 13.31 ?  34  VAL   A CG1  1 
ATOM   906  C CG2  . VAL   A 1 34  ? 28.329 -7.344  12.173  1.00 14.52 ?  34  VAL   A CG2  1 
ATOM   907  H H    . VAL   A 1 34  ? 25.704 -6.278  14.061  1.00 16.33 ?  34  VAL   A H    1 
ATOM   908  H HA   . VAL   A 1 34  ? 27.280 -4.824  12.404  1.00 15.02 ?  34  VAL   A HA   1 
ATOM   909  H HB   . VAL   A 1 34  ? 26.349 -7.391  11.659  1.00 16.08 ?  34  VAL   A HB   1 
ATOM   910  H HG11 . VAL   A 1 34  ? 27.701 -6.987  9.704   1.00 15.99 ?  34  VAL   A HG11 1 
ATOM   911  H HG12 . VAL   A 1 34  ? 26.343 -6.166  9.776   1.00 15.99 ?  34  VAL   A HG12 1 
ATOM   912  H HG13 . VAL   A 1 34  ? 27.719 -5.463  10.149  1.00 15.99 ?  34  VAL   A HG13 1 
ATOM   913  H HG21 . VAL   A 1 34  ? 28.598 -8.075  11.590  1.00 17.44 ?  34  VAL   A HG21 1 
ATOM   914  H HG22 . VAL   A 1 34  ? 29.029 -6.671  12.196  1.00 17.44 ?  34  VAL   A HG22 1 
ATOM   915  H HG23 . VAL   A 1 34  ? 28.167 -7.682  13.068  1.00 17.44 ?  34  VAL   A HG23 1 
ATOM   916  N N    . VAL   A 1 35  ? 25.345 -3.730  11.398  1.00 11.25 ?  35  VAL   A N    1 
ATOM   917  C CA   . VAL   A 1 35  ? 24.296 -3.211  10.527  1.00 10.69 ?  35  VAL   A CA   1 
ATOM   918  C C    . VAL   A 1 35  ? 24.837 -3.202  9.107   1.00 10.21 ?  35  VAL   A C    1 
ATOM   919  O O    . VAL   A 1 35  ? 25.981 -2.797  8.873   1.00 10.89 ?  35  VAL   A O    1 
ATOM   920  C CB   . VAL   A 1 35  ? 23.770 -1.822  10.954  1.00 11.90 ?  35  VAL   A CB   1 
ATOM   921  C CG1  . VAL   A 1 35  ? 24.837 -0.720  10.819  1.00 12.37 ?  35  VAL   A CG1  1 
ATOM   922  C CG2  . VAL   A 1 35  ? 22.520 -1.466  10.152  1.00 12.37 ?  35  VAL   A CG2  1 
ATOM   923  H H    . VAL   A 1 35  ? 25.995 -3.179  11.511  1.00 13.51 ?  35  VAL   A H    1 
ATOM   924  H HA   . VAL   A 1 35  ? 23.543 -3.825  10.549  1.00 12.85 ?  35  VAL   A HA   1 
ATOM   925  H HB   . VAL   A 1 35  ? 23.505 -1.864  11.885  1.00 14.29 ?  35  VAL   A HB   1 
ATOM   926  H HG11 . VAL   A 1 35  ? 24.489 0.107   11.197  1.00 14.86 ?  35  VAL   A HG11 1 
ATOM   927  H HG12 . VAL   A 1 35  ? 25.633 -0.991  11.298  1.00 14.86 ?  35  VAL   A HG12 1 
ATOM   928  H HG13 . VAL   A 1 35  ? 25.043 -0.586  9.879   1.00 14.86 ?  35  VAL   A HG13 1 
ATOM   929  H HG21 . VAL   A 1 35  ? 22.164 -0.622  10.471  1.00 14.85 ?  35  VAL   A HG21 1 
ATOM   930  H HG22 . VAL   A 1 35  ? 22.756 -1.387  9.211   1.00 14.85 ?  35  VAL   A HG22 1 
ATOM   931  H HG23 . VAL   A 1 35  ? 21.857 -2.167  10.264  1.00 14.85 ?  35  VAL   A HG23 1 
ATOM   932  N N    . VAL   A 1 36  ? 24.013 -3.638  8.162   1.00 10.05 ?  36  VAL   A N    1 
ATOM   933  C CA   . VAL   A 1 36  ? 24.380 -3.645  6.753   1.00 9.42  ?  36  VAL   A CA   1 
ATOM   934  C C    . VAL   A 1 36  ? 23.919 -2.349  6.100   1.00 9.53  ?  36  VAL   A C    1 
ATOM   935  O O    . VAL   A 1 36  ? 22.761 -1.937  6.258   1.00 10.65 ?  36  VAL   A O    1 
ATOM   936  C CB   . VAL   A 1 36  ? 23.759 -4.856  6.036   1.00 9.62  ?  36  VAL   A CB   1 
ATOM   937  C CG1  . VAL   A 1 36  ? 24.003 -4.776  4.550   1.00 10.35 ?  36  VAL   A CG1  1 
ATOM   938  C CG2  . VAL   A 1 36  ? 24.313 -6.152  6.602   1.00 10.47 ?  36  VAL   A CG2  1 
ATOM   939  H H    . VAL   A 1 36  ? 23.220 -3.949  8.312   1.00 12.08 ?  36  VAL   A H    1 
ATOM   940  H HA   . VAL   A 1 36  ? 25.345 -3.709  6.670   1.00 11.32 ?  36  VAL   A HA   1 
ATOM   941  H HB   . VAL   A 1 36  ? 22.801 -4.851  6.177   1.00 11.55 ?  36  VAL   A HB   1 
ATOM   942  H HG11 . VAL   A 1 36  ? 23.861 -5.651  4.156   1.00 12.44 ?  36  VAL   A HG11 1 
ATOM   943  H HG12 . VAL   A 1 36  ? 23.389 -4.135  4.155   1.00 12.44 ?  36  VAL   A HG12 1 
ATOM   944  H HG13 . VAL   A 1 36  ? 24.920 -4.493  4.393   1.00 12.44 ?  36  VAL   A HG13 1 
ATOM   945  H HG21 . VAL   A 1 36  ? 23.920 -6.905  6.127   1.00 12.58 ?  36  VAL   A HG21 1 
ATOM   946  H HG22 . VAL   A 1 36  ? 25.278 -6.166  6.490   1.00 12.58 ?  36  VAL   A HG22 1 
ATOM   947  H HG23 . VAL   A 1 36  ? 24.092 -6.211  7.546   1.00 12.58 ?  36  VAL   A HG23 1 
ATOM   948  N N    . ASN   A 1 37  ? 24.823 -1.725  5.347   1.00 9.38  ?  37  ASN   A N    1 
ATOM   949  C CA   . ASN   A 1 37  ? 24.494 -0.595  4.495   1.00 9.25  ?  37  ASN   A CA   1 
ATOM   950  C C    . ASN   A 1 37  ? 24.349 -1.050  3.053   1.00 9.33  ?  37  ASN   A C    1 
ATOM   951  O O    . ASN   A 1 37  ? 25.122 -1.880  2.563   1.00 9.94  ?  37  ASN   A O    1 
ATOM   952  C CB   . ASN   A 1 37  ? 25.576 0.480   4.579   1.00 9.60  ?  37  ASN   A CB   1 
ATOM   953  C CG   . ASN   A 1 37  ? 25.249 1.689   3.736   1.00 9.76  ?  37  ASN   A CG   1 
ATOM   954  O OD1  . ASN   A 1 37  ? 24.079 2.042   3.567   1.00 10.46 ?  37  ASN   A OD1  1 
ATOM   955  N ND2  . ASN   A 1 37  ? 26.278 2.341   3.216   1.00 10.08 ?  37  ASN   A ND2  1 
ATOM   956  H H    . ASN   A 1 37  ? 25.657 -1.946  5.320   1.00 11.27 ?  37  ASN   A H    1 
ATOM   957  H HA   . ASN   A 1 37  ? 23.660 -0.206  4.787   1.00 11.12 ?  37  ASN   A HA   1 
ATOM   958  H HB2  . ASN   A 1 37  ? 25.665 0.773   5.504   1.00 11.53 ?  37  ASN   A HB2  1 
ATOM   959  H HB3  . ASN   A 1 37  ? 26.421 0.113   4.270   1.00 11.53 ?  37  ASN   A HB3  1 
ATOM   960  H HD21 . ASN   A 1 37  ? 26.137 3.035   2.725   1.00 12.11 ?  37  ASN   A HD21 1 
ATOM   961  H HD22 . ASN   A 1 37  ? 27.074 2.074   3.354   1.00 12.11 ?  37  ASN   A HD22 1 
ATOM   962  N N    A ALA   A 1 38  ? 23.345 -0.481  2.380   0.78 9.67  ?  38  ALA   A N    1 
ATOM   963  N N    B ALA   A 1 38  ? 23.332 -0.519  2.374   0.22 9.63  ?  38  ALA   A N    1 
ATOM   964  C CA   A ALA   A 1 38  ? 23.130 -0.610  0.939   0.78 9.88  ?  38  ALA   A CA   1 
ATOM   965  C CA   B ALA   A 1 38  ? 23.141 -0.768  0.945   0.22 10.02 ?  38  ALA   A CA   1 
ATOM   966  C C    A ALA   A 1 38  ? 24.057 0.371   0.223   0.78 9.68  ?  38  ALA   A C    1 
ATOM   967  C C    B ALA   A 1 38  ? 23.956 0.273   0.180   0.22 9.94  ?  38  ALA   A C    1 
ATOM   968  O O    A ALA   A 1 38  ? 23.664 1.468   -0.185  0.78 9.89  ?  38  ALA   A O    1 
ATOM   969  O O    B ALA   A 1 38  ? 23.454 1.304   -0.274  0.22 9.86  ?  38  ALA   A O    1 
ATOM   970  C CB   A ALA   A 1 38  ? 21.670 -0.327  0.606   0.78 10.94 ?  38  ALA   A CB   1 
ATOM   971  C CB   B ALA   A 1 38  ? 21.661 -0.718  0.590   0.22 10.56 ?  38  ALA   A CB   1 
ATOM   972  H H    A ALA   A 1 38  ? 22.762 0.025   2.758   0.78 11.62 ?  38  ALA   A H    1 
ATOM   973  H H    B ALA   A 1 38  ? 22.735 -0.005  2.723   0.22 11.57 ?  38  ALA   A H    1 
ATOM   974  H HA   A ALA   A 1 38  ? 23.350 -1.507  0.653   0.78 11.87 ?  38  ALA   A HA   1 
ATOM   975  H HA   B ALA   A 1 38  ? 23.480 -1.652  0.725   0.22 12.04 ?  38  ALA   A HA   1 
ATOM   976  H HB1  A ALA   A 1 38  ? 21.535 -0.424  -0.348  0.78 13.14 ?  38  ALA   A HB1  1 
ATOM   977  H HB1  B ALA   A 1 38  ? 21.567 -0.795  -0.370  0.22 12.69 ?  38  ALA   A HB1  1 
ATOM   978  H HB2  A ALA   A 1 38  ? 21.108 -0.961  1.085   0.78 13.14 ?  38  ALA   A HB2  1 
ATOM   979  H HB2  B ALA   A 1 38  ? 21.199 -1.452  1.029   0.22 12.69 ?  38  ALA   A HB2  1 
ATOM   980  H HB3  A ALA   A 1 38  ? 21.448 0.578   0.882   0.78 13.14 ?  38  ALA   A HB3  1 
ATOM   981  H HB3  B ALA   A 1 38  ? 21.294 0.129   0.888   0.22 12.69 ?  38  ALA   A HB3  1 
ATOM   982  N N    A ALA   A 1 39  ? 25.313 -0.030  0.079   0.78 9.73  ?  39  ALA   A N    1 
ATOM   983  N N    B ALA   A 1 39  ? 25.245 -0.010  0.043   0.22 10.13 ?  39  ALA   A N    1 
ATOM   984  C CA   A ALA   A 1 39  ? 26.376 0.830   -0.417  0.78 9.65  ?  39  ALA   A CA   1 
ATOM   985  C CA   B ALA   A 1 39  ? 26.209 0.965   -0.442  0.22 10.40 ?  39  ALA   A CA   1 
ATOM   986  C C    A ALA   A 1 39  ? 26.476 0.789   -1.941  0.78 9.50  ?  39  ALA   A C    1 
ATOM   987  C C    B ALA   A 1 39  ? 26.447 0.818   -1.940  0.22 10.00 ?  39  ALA   A C    1 
ATOM   988  O O    A ALA   A 1 39  ? 25.975 -0.122  -2.605  0.78 10.04 ?  39  ALA   A O    1 
ATOM   989  O O    B ALA   A 1 39  ? 26.012 -0.140  -2.584  0.22 10.04 ?  39  ALA   A O    1 
ATOM   990  C CB   A ALA   A 1 39  ? 27.706 0.401   0.206   0.78 9.92  ?  39  ALA   A CB   1 
ATOM   991  C CB   B ALA   A 1 39  ? 27.531 0.821   0.315   0.22 10.96 ?  39  ALA   A CB   1 
ATOM   992  H H    A ALA   A 1 39  ? 25.579 -0.828  0.271   0.78 11.69 ?  39  ALA   A H    1 
ATOM   993  H H    B ALA   A 1 39  ? 25.588 -0.779  0.226   0.22 12.17 ?  39  ALA   A H    1 
ATOM   994  H HA   A ALA   A 1 39  ? 26.194 1.744   -0.150  0.78 11.59 ?  39  ALA   A HA   1 
ATOM   995  H HA   B ALA   A 1 39  ? 25.862 1.854   -0.277  0.22 12.49 ?  39  ALA   A HA   1 
ATOM   996  H HB1  A ALA   A 1 39  ? 28.409 0.981   -0.126  0.78 11.92 ?  39  ALA   A HB1  1 
ATOM   997  H HB1  B ALA   A 1 39  ? 28.155 1.484   -0.017  0.22 13.17 ?  39  ALA   A HB1  1 
ATOM   998  H HB2  A ALA   A 1 39  ? 27.641 0.486   1.174   0.78 11.92 ?  39  ALA   A HB2  1 
ATOM   999  H HB2  B ALA   A 1 39  ? 27.369 0.961   1.261   0.22 13.17 ?  39  ALA   A HB2  1 
ATOM   1000 H HB3  A ALA   A 1 39  ? 27.888 -0.517  -0.033  0.78 11.92 ?  39  ALA   A HB3  1 
ATOM   1001 H HB3  B ALA   A 1 39  ? 27.884 -0.070  0.168   0.22 13.17 ?  39  ALA   A HB3  1 
ATOM   1002 N N    . ASN   A 1 40  ? 27.161 1.796   -2.489  1.00 10.03 ?  40  ASN   A N    1 
ATOM   1003 C CA   . ASN   A 1 40  ? 27.670 1.755   -3.854  1.00 10.15 ?  40  ASN   A CA   1 
ATOM   1004 C C    . ASN   A 1 40  ? 29.196 1.639   -3.813  1.00 9.94  ?  40  ASN   A C    1 
ATOM   1005 O O    . ASN   A 1 40  ? 29.816 1.734   -2.753  1.00 10.03 ?  40  ASN   A O    1 
ATOM   1006 C CB   . ASN   A 1 40  ? 27.182 2.944   -4.696  1.00 11.11 ?  40  ASN   A CB   1 
ATOM   1007 C CG   . ASN   A 1 40  ? 27.565 4.288   -4.111  1.00 11.87 ?  40  ASN   A CG   1 
ATOM   1008 O OD1  . ASN   A 1 40  ? 28.738 4.547   -3.819  1.00 13.05 ?  40  ASN   A OD1  1 
ATOM   1009 N ND2  . ASN   A 1 40  ? 26.571 5.160   -3.950  1.00 12.77 ?  40  ASN   A ND2  1 
ATOM   1010 H H    A ASN   A 1 40  ? 27.343 2.525   -2.081  0.78 12.05 ?  40  ASN   A H    1 
ATOM   1011 H H    B ASN   A 1 40  ? 27.381 2.510   -2.072  0.22 12.05 ?  40  ASN   A H    1 
ATOM   1012 H HA   . ASN   A 1 40  ? 27.335 0.949   -4.285  1.00 12.19 ?  40  ASN   A HA   1 
ATOM   1013 H HB2  . ASN   A 1 40  ? 27.568 2.877   -5.588  1.00 13.35 ?  40  ASN   A HB2  1 
ATOM   1014 H HB3  . ASN   A 1 40  ? 26.214 2.908   -4.760  1.00 13.35 ?  40  ASN   A HB3  1 
ATOM   1015 H HD21 . ASN   A 1 40  ? 26.737 5.943   -3.635  1.00 15.34 ?  40  ASN   A HD21 1 
ATOM   1016 H HD22 . ASN   A 1 40  ? 25.770 4.947   -4.174  1.00 15.34 ?  40  ASN   A HD22 1 
ATOM   1017 N N    A VAL   A 1 41  ? 29.808 1.392   -4.977  0.78 10.38 ?  41  VAL   A N    1 
ATOM   1018 N N    B VAL   A 1 41  ? 29.782 1.423   -4.994  0.22 10.09 ?  41  VAL   A N    1 
ATOM   1019 C CA   A VAL   A 1 41  ? 31.242 1.085   -4.997  0.78 11.03 ?  41  VAL   A CA   1 
ATOM   1020 C CA   B VAL   A 1 41  ? 31.202 1.102   -5.094  0.22 10.34 ?  41  VAL   A CA   1 
ATOM   1021 C C    A VAL   A 1 41  ? 32.097 2.243   -4.523  0.78 11.11 ?  41  VAL   A C    1 
ATOM   1022 C C    B VAL   A 1 41  ? 32.102 2.233   -4.617  0.22 10.32 ?  41  VAL   A C    1 
ATOM   1023 O O    A VAL   A 1 41  ? 33.242 2.029   -4.103  0.78 11.75 ?  41  VAL   A O    1 
ATOM   1024 O O    B VAL   A 1 41  ? 33.256 1.983   -4.248  0.22 10.32 ?  41  VAL   A O    1 
ATOM   1025 C CB   A VAL   A 1 41  ? 31.750 0.585   -6.370  0.78 11.88 ?  41  VAL   A CB   1 
ATOM   1026 C CB   B VAL   A 1 41  ? 31.560 0.663   -6.530  0.22 10.80 ?  41  VAL   A CB   1 
ATOM   1027 C CG1  A VAL   A 1 41  ? 31.030 -0.691  -6.784  0.78 12.63 ?  41  VAL   A CG1  1 
ATOM   1028 C CG1  B VAL   A 1 41  ? 30.910 -0.676  -6.847  0.22 11.42 ?  41  VAL   A CG1  1 
ATOM   1029 C CG2  A VAL   A 1 41  ? 31.652 1.665   -7.444  0.78 12.27 ?  41  VAL   A CG2  1 
ATOM   1030 C CG2  B VAL   A 1 41  ? 31.141 1.722   -7.544  0.22 10.63 ?  41  VAL   A CG2  1 
ATOM   1031 H H    A VAL   A 1 41  ? 29.423 1.390   -5.750  0.78 12.47 ?  41  VAL   A H    1 
ATOM   1032 H H    B VAL   A 1 41  ? 29.369 1.446   -5.749  0.22 12.12 ?  41  VAL   A H    1 
ATOM   1033 H HA   A VAL   A 1 41  ? 31.393 0.362   -4.372  0.78 13.25 ?  41  VAL   A HA   1 
ATOM   1034 H HA   B VAL   A 1 41  ? 31.374 0.344   -4.517  0.22 12.43 ?  41  VAL   A HA   1 
ATOM   1035 H HB   A VAL   A 1 41  ? 32.687 0.356   -6.279  0.78 14.27 ?  41  VAL   A HB   1 
ATOM   1036 H HB   B VAL   A 1 41  ? 32.521 0.546   -6.594  0.22 12.98 ?  41  VAL   A HB   1 
ATOM   1037 H HG11 A VAL   A 1 41  ? 31.375 -0.994  -7.638  0.78 15.17 ?  41  VAL   A HG11 1 
ATOM   1038 H HG11 B VAL   A 1 41  ? 31.215 -0.981  -7.715  0.22 13.72 ?  41  VAL   A HG11 1 
ATOM   1039 H HG12 A VAL   A 1 41  ? 31.177 -1.375  -6.109  0.78 15.17 ?  41  VAL   A HG12 1 
ATOM   1040 H HG12 B VAL   A 1 41  ? 31.158 -1.320  -6.164  0.22 13.72 ?  41  VAL   A HG12 1 
ATOM   1041 H HG13 A VAL   A 1 41  ? 30.077 -0.509  -6.861  0.78 15.17 ?  41  VAL   A HG13 1 
ATOM   1042 H HG13 B VAL   A 1 41  ? 29.945 -0.564  -6.856  0.22 13.72 ?  41  VAL   A HG13 1 
ATOM   1043 H HG21 A VAL   A 1 41  ? 31.854 1.269   -8.310  0.78 14.74 ?  41  VAL   A HG21 1 
ATOM   1044 H HG21 B VAL   A 1 41  ? 31.511 1.490   -8.410  0.22 12.77 ?  41  VAL   A HG21 1 
ATOM   1045 H HG22 A VAL   A 1 41  ? 30.758 2.029   -7.448  0.78 14.74 ?  41  VAL   A HG22 1 
ATOM   1046 H HG22 B VAL   A 1 41  ? 30.173 1.751   -7.596  0.22 12.77 ?  41  VAL   A HG22 1 
ATOM   1047 H HG23 A VAL   A 1 41  ? 32.298 2.362   -7.247  0.78 14.74 ?  41  VAL   A HG23 1 
ATOM   1048 H HG23 B VAL   A 1 41  ? 31.485 2.580   -7.257  0.22 12.77 ?  41  VAL   A HG23 1 
ATOM   1049 N N    A TYR   A 1 42  ? 31.584 3.472   -4.605  0.78 10.94 ?  42  TYR   A N    1 
ATOM   1050 N N    B TYR   A 1 42  ? 31.616 3.475   -4.625  0.22 10.41 ?  42  TYR   A N    1 
ATOM   1051 C CA   A TYR   A 1 42  ? 32.318 4.663   -4.196  0.78 10.89 ?  42  TYR   A CA   1 
ATOM   1052 C CA   B TYR   A 1 42  ? 32.401 4.619   -4.174  0.22 10.58 ?  42  TYR   A CA   1 
ATOM   1053 C C    A TYR   A 1 42  ? 32.084 5.024   -2.739  0.78 10.61 ?  42  TYR   A C    1 
ATOM   1054 C C    B TYR   A 1 42  ? 32.068 5.036   -2.746  0.22 10.41 ?  42  TYR   A C    1 
ATOM   1055 O O    A TYR   A 1 42  ? 32.665 6.000   -2.245  0.78 11.36 ?  42  TYR   A O    1 
ATOM   1056 O O    B TYR   A 1 42  ? 32.573 6.062   -2.276  0.22 10.57 ?  42  TYR   A O    1 
ATOM   1057 C CB   A TYR   A 1 42  ? 31.944 5.852   -5.101  0.78 11.42 ?  42  TYR   A CB   1 
ATOM   1058 C CB   B TYR   A 1 42  ? 32.222 5.803   -5.129  0.22 11.05 ?  42  TYR   A CB   1 
ATOM   1059 C CG   A TYR   A 1 42  ? 32.117 5.554   -6.577  0.78 12.30 ?  42  TYR   A CG   1 
ATOM   1060 C CG   B TYR   A 1 42  ? 32.469 5.452   -6.578  0.22 11.23 ?  42  TYR   A CG   1 
ATOM   1061 C CD1  A TYR   A 1 42  ? 33.374 5.357   -7.125  0.78 12.81 ?  42  TYR   A CD1  1 
ATOM   1062 C CD1  B TYR   A 1 42  ? 33.758 5.256   -7.056  0.22 11.74 ?  42  TYR   A CD1  1 
ATOM   1063 C CD2  A TYR   A 1 42  ? 31.018 5.442   -7.418  0.78 13.61 ?  42  TYR   A CD2  1 
ATOM   1064 C CD2  B TYR   A 1 42  ? 31.412 5.309   -7.466  0.22 11.34 ?  42  TYR   A CD2  1 
ATOM   1065 C CE1  A TYR   A 1 42  ? 33.535 5.064   -8.469  0.78 13.05 ?  42  TYR   A CE1  1 
ATOM   1066 C CE1  B TYR   A 1 42  ? 33.984 4.924   -8.380  0.22 11.82 ?  42  TYR   A CE1  1 
ATOM   1067 C CE2  A TYR   A 1 42  ? 31.170 5.165   -8.764  0.78 14.40 ?  42  TYR   A CE2  1 
ATOM   1068 C CE2  B TYR   A 1 42  ? 31.629 4.982   -8.790  0.22 11.50 ?  42  TYR   A CE2  1 
ATOM   1069 C CZ   A TYR   A 1 42  ? 32.429 4.967   -9.282  0.78 14.12 ?  42  TYR   A CZ   1 
ATOM   1070 C CZ   B TYR   A 1 42  ? 32.915 4.792   -9.243  0.22 11.61 ?  42  TYR   A CZ   1 
ATOM   1071 O OH   A TYR   A 1 42  ? 32.576 4.683   -10.622 0.78 15.68 ?  42  TYR   A OH   1 
ATOM   1072 O OH   B TYR   A 1 42  ? 33.129 4.460   -10.560 0.22 12.11 ?  42  TYR   A OH   1 
ATOM   1073 H H    A TYR   A 1 42  ? 30.790 3.642   -4.904  0.78 13.14 ?  42  TYR   A H    1 
ATOM   1074 H H    B TYR   A 1 42  ? 30.824 3.682   -4.898  0.22 12.51 ?  42  TYR   A H    1 
ATOM   1075 H HA   A TYR   A 1 42  ? 33.262 4.501   -4.316  0.78 13.08 ?  42  TYR   A HA   1 
ATOM   1076 H HA   B TYR   A 1 42  ? 33.336 4.374   -4.196  0.22 12.71 ?  42  TYR   A HA   1 
ATOM   1077 H HB2  A TYR   A 1 42  ? 31.014 6.092   -4.955  0.78 13.72 ?  42  TYR   A HB2  1 
ATOM   1078 H HB2  B TYR   A 1 42  ? 31.314 6.135   -5.056  0.22 13.27 ?  42  TYR   A HB2  1 
ATOM   1079 H HB3  A TYR   A 1 42  ? 32.515 6.610   -4.887  0.78 13.72 ?  42  TYR   A HB3  1 
ATOM   1080 H HB3  B TYR   A 1 42  ? 32.850 6.502   -4.882  0.22 13.27 ?  42  TYR   A HB3  1 
ATOM   1081 H HD1  A TYR   A 1 42  ? 34.125 5.413   -6.579  0.78 15.39 ?  42  TYR   A HD1  1 
ATOM   1082 H HD1  B TYR   A 1 42  ? 34.481 5.344   -6.475  0.22 14.10 ?  42  TYR   A HD1  1 
ATOM   1083 H HD2  A TYR   A 1 42  ? 30.163 5.578   -7.077  0.78 16.34 ?  42  TYR   A HD2  1 
ATOM   1084 H HD2  B TYR   A 1 42  ? 30.543 5.437   -7.162  0.22 13.62 ?  42  TYR   A HD2  1 
ATOM   1085 H HE1  A TYR   A 1 42  ? 34.389 4.931   -8.822  0.78 15.67 ?  42  TYR   A HE1  1 
ATOM   1086 H HE1  B TYR   A 1 42  ? 34.854 4.799   -8.687  0.22 14.20 ?  42  TYR   A HE1  1 
ATOM   1087 H HE2  A TYR   A 1 42  ? 30.423 5.096   -9.320  0.78 17.30 ?  42  TYR   A HE2  1 
ATOM   1088 H HE2  B TYR   A 1 42  ? 30.910 4.892   -9.372  0.22 13.81 ?  42  TYR   A HE2  1 
ATOM   1089 H HH   A TYR   A 1 42  ? 33.392 4.586   -10.811 0.78 18.83 ?  42  TYR   A HH   1 
ATOM   1090 H HH   B TYR   A 1 42  ? 33.887 4.115   -10.644 0.22 14.55 ?  42  TYR   A HH   1 
ATOM   1091 N N    . LEU   A 1 43  ? 31.233 4.264   -2.049  1.00 10.53 ?  43  LEU   A N    1 
ATOM   1092 C CA   . LEU   A 1 43  ? 30.794 4.598   -0.697  1.00 10.22 ?  43  LEU   A CA   1 
ATOM   1093 C C    . LEU   A 1 43  ? 30.309 6.043   -0.590  1.00 10.21 ?  43  LEU   A C    1 
ATOM   1094 O O    . LEU   A 1 43  ? 30.582 6.738   0.389   1.00 11.33 ?  43  LEU   A O    1 
ATOM   1095 C CB   . LEU   A 1 43  ? 31.852 4.285   0.359   1.00 10.46 ?  43  LEU   A CB   1 
ATOM   1096 C CG   . LEU   A 1 43  ? 32.334 2.834   0.438   1.00 10.77 ?  43  LEU   A CG   1 
ATOM   1097 C CD1  . LEU   A 1 43  ? 33.400 2.704   1.522   1.00 11.96 ?  43  LEU   A CD1  1 
ATOM   1098 C CD2  . LEU   A 1 43  ? 31.192 1.859   0.692   1.00 11.59 ?  43  LEU   A CD2  1 
ATOM   1099 H H    A LEU   A 1 43  ? 30.889 3.531   -2.348  0.78 12.64 ?  43  LEU   A H    1 
ATOM   1100 H H    B LEU   A 1 43  ? 30.899 3.525   -2.344  0.22 12.64 ?  43  LEU   A H    1 
ATOM   1101 H HA   . LEU   A 1 43  ? 30.029 4.036   -0.493  1.00 12.28 ?  43  LEU   A HA   1 
ATOM   1102 H HB2  . LEU   A 1 43  ? 32.628 4.840   0.192   1.00 12.57 ?  43  LEU   A HB2  1 
ATOM   1103 H HB3  . LEU   A 1 43  ? 31.482 4.505   1.231   1.00 12.57 ?  43  LEU   A HB3  1 
ATOM   1104 H HG   . LEU   A 1 43  ? 32.752 2.596   -0.405  1.00 12.94 ?  43  LEU   A HG   1 
ATOM   1105 H HD11 . LEU   A 1 43  ? 33.702 1.781   1.562   1.00 14.37 ?  43  LEU   A HD11 1 
ATOM   1106 H HD12 . LEU   A 1 43  ? 34.146 3.285   1.310   1.00 14.37 ?  43  LEU   A HD12 1 
ATOM   1107 H HD13 . LEU   A 1 43  ? 33.014 2.959   2.377   1.00 14.37 ?  43  LEU   A HD13 1 
ATOM   1108 H HD21 . LEU   A 1 43  ? 31.564 0.971   0.832   1.00 13.92 ?  43  LEU   A HD21 1 
ATOM   1109 H HD22 . LEU   A 1 43  ? 30.709 2.142   1.482   1.00 13.92 ?  43  LEU   A HD22 1 
ATOM   1110 H HD23 . LEU   A 1 43  ? 30.608 1.856   -0.078  1.00 13.92 ?  43  LEU   A HD23 1 
ATOM   1111 N N    A LYS   A 1 44  ? 29.583 6.491   -1.619  0.78 10.12 ?  44  LYS   A N    1 
ATOM   1112 N N    B LYS   A 1 44  ? 29.556 6.490   -1.592  0.22 11.21 ?  44  LYS   A N    1 
ATOM   1113 C CA   A LYS   A 1 44  ? 28.937 7.803   -1.620  0.78 10.43 ?  44  LYS   A CA   1 
ATOM   1114 C CA   B LYS   A 1 44  ? 28.918 7.803   -1.551  0.22 12.48 ?  44  LYS   A CA   1 
ATOM   1115 C C    A LYS   A 1 44  ? 27.515 7.606   -1.110  0.78 9.87  ?  44  LYS   A C    1 
ATOM   1116 C C    B LYS   A 1 44  ? 27.498 7.629   -1.029  0.22 11.97 ?  44  LYS   A C    1 
ATOM   1117 O O    A LYS   A 1 44  ? 26.646 7.086   -1.818  0.78 11.07 ?  44  LYS   A O    1 
ATOM   1118 O O    B LYS   A 1 44  ? 26.617 7.141   -1.744  0.22 11.98 ?  44  LYS   A O    1 
ATOM   1119 C CB   A LYS   A 1 44  ? 28.963 8.425   -3.010  0.78 12.70 ?  44  LYS   A CB   1 
ATOM   1120 C CB   B LYS   A 1 44  ? 28.938 8.459   -2.930  0.22 14.41 ?  44  LYS   A CB   1 
ATOM   1121 C CG   A LYS   A 1 44  ? 30.331 8.928   -3.447  0.78 16.29 ?  44  LYS   A CG   1 
ATOM   1122 C CG   B LYS   A 1 44  ? 30.329 8.871   -3.396  0.22 16.39 ?  44  LYS   A CG   1 
ATOM   1123 C CD   A LYS   A 1 44  ? 30.988 9.847   -2.414  0.78 22.22 ?  44  LYS   A CD   1 
ATOM   1124 C CD   B LYS   A 1 44  ? 31.110 9.572   -2.288  0.22 18.80 ?  44  LYS   A CD   1 
ATOM   1125 C CE   A LYS   A 1 44  ? 32.322 10.373  -2.914  0.78 25.74 ?  44  LYS   A CE   1 
ATOM   1126 C CE   B LYS   A 1 44  ? 32.466 10.042  -2.769  0.22 20.11 ?  44  LYS   A CE   1 
ATOM   1127 N NZ   A LYS   A 1 44  ? 33.150 10.942  -1.817  0.78 27.56 ?  44  LYS   A NZ   1 
ATOM   1128 N NZ   B LYS   A 1 44  ? 33.312 10.530  -1.646  0.22 20.28 ?  44  LYS   A NZ   1 
ATOM   1129 H H    A LYS   A 1 44  ? 29.455 6.044   -2.344  0.78 12.15 ?  44  LYS   A H    1 
ATOM   1130 H H    B LYS   A 1 44  ? 29.401 6.048   -2.313  0.22 13.47 ?  44  LYS   A H    1 
ATOM   1131 H HA   A LYS   A 1 44  ? 29.392 8.386   -0.994  0.78 12.54 ?  44  LYS   A HA   1 
ATOM   1132 H HA   B LYS   A 1 44  ? 29.380 8.370   -0.917  0.22 14.99 ?  44  LYS   A HA   1 
ATOM   1133 H HB2  A LYS   A 1 44  ? 28.679 7.764   -3.658  0.78 15.26 ?  44  LYS   A HB2  1 
ATOM   1134 H HB2  B LYS   A 1 44  ? 28.582 7.834   -3.583  0.22 17.30 ?  44  LYS   A HB2  1 
ATOM   1135 H HB3  A LYS   A 1 44  ? 28.358 9.183   -3.026  0.78 15.26 ?  44  LYS   A HB3  1 
ATOM   1136 H HB3  B LYS   A 1 44  ? 28.387 9.258   -2.908  0.22 17.30 ?  44  LYS   A HB3  1 
ATOM   1137 H HG2  A LYS   A 1 44  ? 30.920 8.174   -3.594  0.78 19.56 ?  44  LYS   A HG2  1 
ATOM   1138 H HG2  B LYS   A 1 44  ? 30.823 8.081   -3.663  0.22 19.68 ?  44  LYS   A HG2  1 
ATOM   1139 H HG3  A LYS   A 1 44  ? 30.237 9.438   -4.272  0.78 19.56 ?  44  LYS   A HG3  1 
ATOM   1140 H HG3  B LYS   A 1 44  ? 30.247 9.485   -4.145  0.22 19.68 ?  44  LYS   A HG3  1 
ATOM   1141 H HD2  A LYS   A 1 44  ? 30.401 10.596  -2.231  0.78 26.68 ?  44  LYS   A HD2  1 
ATOM   1142 H HD2  B LYS   A 1 44  ? 30.599 10.339  -1.973  0.22 22.57 ?  44  LYS   A HD2  1 
ATOM   1143 H HD3  A LYS   A 1 44  ? 31.157 9.342   -1.600  0.78 26.68 ?  44  LYS   A HD3  1 
ATOM   1144 H HD3  B LYS   A 1 44  ? 31.265 8.952   -1.558  0.22 22.57 ?  44  LYS   A HD3  1 
ATOM   1145 H HE2  A LYS   A 1 44  ? 32.820 9.642   -3.317  0.78 30.91 ?  44  LYS   A HE2  1 
ATOM   1146 H HE2  B LYS   A 1 44  ? 32.923 9.301   -3.194  0.22 24.15 ?  44  LYS   A HE2  1 
ATOM   1147 H HE3  A LYS   A 1 44  ? 32.163 11.068  -3.567  0.78 30.91 ?  44  LYS   A HE3  1 
ATOM   1148 H HE3  B LYS   A 1 44  ? 32.344 10.769  -3.397  0.22 24.15 ?  44  LYS   A HE3  1 
ATOM   1149 H HZ1  A LYS   A 1 44  ? 33.922 11.241  -2.144  0.78 33.09 ?  44  LYS   A HZ1  1 
ATOM   1150 H HZ1  B LYS   A 1 44  ? 34.101 10.800  -1.956  0.22 24.35 ?  44  LYS   A HZ1  1 
ATOM   1151 H HZ2  A LYS   A 1 44  ? 32.718 11.619  -1.432  0.78 33.09 ?  44  LYS   A HZ2  1 
ATOM   1152 H HZ2  B LYS   A 1 44  ? 32.912 11.215  -1.239  0.22 24.35 ?  44  LYS   A HZ2  1 
ATOM   1153 H HZ3  A LYS   A 1 44  ? 33.316 10.320  -1.204  0.78 33.09 ?  44  LYS   A HZ3  1 
ATOM   1154 H HZ3  B LYS   A 1 44  ? 33.439 9.878   -1.054  0.22 24.35 ?  44  LYS   A HZ3  1 
ATOM   1155 N N    A HIS   A 1 45  ? 27.282 8.004   0.134   0.78 9.68  ?  45  HIS   A N    1 
ATOM   1156 N N    B HIS   A 1 45  ? 27.277 8.028   0.221   0.22 12.04 ?  45  HIS   A N    1 
ATOM   1157 C CA   A HIS   A 1 45  ? 26.054 7.646   0.845   0.78 9.77  ?  45  HIS   A CA   1 
ATOM   1158 C CA   B HIS   A 1 45  ? 26.015 7.772   0.913   0.22 12.16 ?  45  HIS   A CA   1 
ATOM   1159 C C    A HIS   A 1 45  ? 25.013 8.759   0.691   0.78 10.59 ?  45  HIS   A C    1 
ATOM   1160 C C    B HIS   A 1 45  ? 25.126 8.999   0.760   0.22 12.93 ?  45  HIS   A C    1 
ATOM   1161 O O    A HIS   A 1 45  ? 24.686 9.491   1.628   0.78 11.80 ?  45  HIS   A O    1 
ATOM   1162 O O    B HIS   A 1 45  ? 25.103 9.883   1.616   0.22 13.62 ?  45  HIS   A O    1 
ATOM   1163 C CB   A HIS   A 1 45  ? 26.367 7.387   2.307   0.78 9.79  ?  45  HIS   A CB   1 
ATOM   1164 C CB   B HIS   A 1 45  ? 26.270 7.448   2.376   0.22 11.65 ?  45  HIS   A CB   1 
ATOM   1165 C CG   A HIS   A 1 45  ? 27.477 6.408   2.524   0.78 9.55  ?  45  HIS   A CG   1 
ATOM   1166 C CG   B HIS   A 1 45  ? 27.407 6.502   2.592   0.22 10.92 ?  45  HIS   A CG   1 
ATOM   1167 N ND1  A HIS   A 1 45  ? 27.456 5.120   2.026   0.78 9.88  ?  45  HIS   A ND1  1 
ATOM   1168 N ND1  B HIS   A 1 45  ? 27.415 5.218   2.090   0.22 10.79 ?  45  HIS   A ND1  1 
ATOM   1169 C CD2  A HIS   A 1 45  ? 28.646 6.543   3.194   0.78 10.11 ?  45  HIS   A CD2  1 
ATOM   1170 C CD2  B HIS   A 1 45  ? 28.578 6.658   3.252   0.22 10.49 ?  45  HIS   A CD2  1 
ATOM   1171 C CE1  A HIS   A 1 45  ? 28.576 4.511   2.384   0.78 9.97  ?  45  HIS   A CE1  1 
ATOM   1172 C CE1  B HIS   A 1 45  ? 28.543 4.623   2.436   0.22 10.13 ?  45  HIS   A CE1  1 
ATOM   1173 N NE2  A HIS   A 1 45  ? 29.311 5.348   3.097   0.78 10.17 ?  45  HIS   A NE2  1 
ATOM   1174 N NE2  B HIS   A 1 45  ? 29.266 5.475   3.143   0.22 10.09 ?  45  HIS   A NE2  1 
ATOM   1175 H H    A HIS   A 1 45  ? 27.820 8.490   0.597   0.78 11.63 ?  45  HIS   A H    1 
ATOM   1176 H H    B HIS   A 1 45  ? 27.853 8.463   0.699   0.22 14.47 ?  45  HIS   A H    1 
ATOM   1177 H HA   A HIS   A 1 45  ? 25.688 6.832   0.464   0.78 11.74 ?  45  HIS   A HA   1 
ATOM   1178 H HA   B HIS   A 1 45  ? 25.571 7.019   0.500   0.22 14.60 ?  45  HIS   A HA   1 
ATOM   1179 H HB2  A HIS   A 1 45  ? 26.619 8.225   2.726   0.78 11.76 ?  45  HIS   A HB2  1 
ATOM   1180 H HB2  B HIS   A 1 45  ? 26.473 8.269   2.848   0.22 14.00 ?  45  HIS   A HB2  1 
ATOM   1181 H HB3  A HIS   A 1 45  ? 25.572 7.032   2.739   0.78 11.76 ?  45  HIS   A HB3  1 
ATOM   1182 H HB3  B HIS   A 1 45  ? 25.472 7.043   2.746   0.22 14.00 ?  45  HIS   A HB3  1 
ATOM   1183 H HD2  A HIS   A 1 45  ? 28.948 7.307   3.637   0.78 12.14 ?  45  HIS   A HD2  1 
ATOM   1184 H HD2  B HIS   A 1 45  ? 28.861 7.424   3.697   0.22 12.60 ?  45  HIS   A HD2  1 
ATOM   1185 H HE1  A HIS   A 1 45  ? 28.798 3.629   2.187   0.78 11.97 ?  45  HIS   A HE1  1 
ATOM   1186 H HE1  B HIS   A 1 45  ? 28.784 3.751   2.221   0.22 12.17 ?  45  HIS   A HE1  1 
ATOM   1187 H HE2  A HIS   A 1 45  ? 30.082 5.172   3.439   0.78 12.22 ?  45  HIS   A HE2  1 
ATOM   1188 H HE2  B HIS   A 1 45  ? 30.040 5.315   3.478   0.22 12.12 ?  45  HIS   A HE2  1 
ATOM   1189 N N    A GLY   A 1 46  ? 24.489 8.870   -0.524  0.78 11.80 ?  46  GLY   A N    1 
ATOM   1190 N N    B GLY   A 1 46  ? 24.382 9.045   -0.339  0.22 13.10 ?  46  GLY   A N    1 
ATOM   1191 C CA   A GLY   A 1 46  ? 23.688 10.031  -0.870  0.78 12.80 ?  46  GLY   A CA   1 
ATOM   1192 C CA   B GLY   A 1 46  ? 23.525 10.181  -0.611  0.22 12.82 ?  46  GLY   A CA   1 
ATOM   1193 C C    A GLY   A 1 46  ? 22.204 9.928   -0.583  0.78 12.57 ?  46  GLY   A C    1 
ATOM   1194 C C    B GLY   A 1 46  ? 22.049 9.908   -0.409  0.22 12.10 ?  46  GLY   A C    1 
ATOM   1195 O O    A GLY   A 1 46  ? 21.543 10.936  -0.316  0.78 12.79 ?  46  GLY   A O    1 
ATOM   1196 O O    B GLY   A 1 46  ? 21.330 10.752  0.132   0.22 11.85 ?  46  GLY   A O    1 
ATOM   1197 H H    A GLY   A 1 46  ? 24.569 8.291   -1.153  0.78 14.18 ?  46  GLY   A H    1 
ATOM   1198 H H    B GLY   A 1 46  ? 24.362 8.430   -0.941  0.22 15.73 ?  46  GLY   A H    1 
ATOM   1199 H HA2  A GLY   A 1 46  ? 24.026 10.799  -0.381  0.78 15.37 ?  46  GLY   A HA2  1 
ATOM   1200 H HA2  B GLY   A 1 46  ? 23.773 10.917  -0.029  0.22 15.39 ?  46  GLY   A HA2  1 
ATOM   1201 H HA3  A GLY   A 1 46  ? 23.788 10.210  -1.814  0.78 15.37 ?  46  GLY   A HA3  1 
ATOM   1202 H HA3  B GLY   A 1 46  ? 23.659 10.463  -1.526  0.22 15.39 ?  46  GLY   A HA3  1 
ATOM   1203 N N    A GLY   A 1 47  ? 21.664 8.717   -0.654  0.78 12.71 ?  47  GLY   A N    1 
ATOM   1204 N N    B GLY   A 1 47  ? 21.582 8.732   -0.840  0.22 12.10 ?  47  GLY   A N    1 
ATOM   1205 C CA   A GLY   A 1 47  ? 20.228 8.533   -0.581  0.78 13.43 ?  47  GLY   A CA   1 
ATOM   1206 C CA   B GLY   A 1 47  ? 20.170 8.419   -0.796  0.22 12.19 ?  47  GLY   A CA   1 
ATOM   1207 C C    A GLY   A 1 47  ? 19.887 7.091   -0.268  0.78 12.33 ?  47  GLY   A C    1 
ATOM   1208 C C    B GLY   A 1 47  ? 19.927 7.006   -0.301  0.22 11.98 ?  47  GLY   A C    1 
ATOM   1209 O O    A GLY   A 1 47  ? 20.762 6.253   -0.036  0.78 12.24 ?  47  GLY   A O    1 
ATOM   1210 O O    B GLY   A 1 47  ? 20.853 6.207   -0.147  0.22 12.15 ?  47  GLY   A O    1 
ATOM   1211 H H    A GLY   A 1 47  ? 22.108 7.997   -0.738  0.78 15.27 ?  47  GLY   A H    1 
ATOM   1212 H H    B GLY   A 1 47  ? 22.073 8.103   -1.158  0.22 14.53 ?  47  GLY   A H    1 
ATOM   1213 H HA2  A GLY   A 1 47  ? 19.855 9.100   0.114   0.78 16.14 ?  47  GLY   A HA2  1 
ATOM   1214 H HA2  B GLY   A 1 47  ? 19.710 9.043   -0.212  0.22 14.64 ?  47  GLY   A HA2  1 
ATOM   1215 H HA3  A GLY   A 1 47  ? 19.824 8.780   -1.430  0.78 16.14 ?  47  GLY   A HA3  1 
ATOM   1216 H HA3  B GLY   A 1 47  ? 19.794 8.497   -1.688  0.22 14.64 ?  47  GLY   A HA3  1 
ATOM   1217 N N    A GLY   A 1 48  ? 18.591 6.801   -0.273  0.78 12.63 ?  48  GLY   A N    1 
ATOM   1218 N N    B GLY   A 1 48  ? 18.651 6.710   -0.063  0.22 11.80 ?  48  GLY   A N    1 
ATOM   1219 C CA   A GLY   A 1 48  ? 18.169 5.473   0.110   0.78 12.32 ?  48  GLY   A CA   1 
ATOM   1220 C CA   B GLY   A 1 48  ? 18.244 5.388   0.379   0.22 11.44 ?  48  GLY   A CA   1 
ATOM   1221 C C    A GLY   A 1 48  ? 18.622 5.150   1.520   0.78 11.53 ?  48  GLY   A C    1 
ATOM   1222 C C    B GLY   A 1 48  ? 18.754 5.046   1.770   0.22 10.94 ?  48  GLY   A C    1 
ATOM   1223 O O    A GLY   A 1 48  ? 18.792 6.032   2.371   0.78 12.10 ?  48  GLY   A O    1 
ATOM   1224 O O    B GLY   A 1 48  ? 18.865 5.898   2.659   0.22 11.14 ?  48  GLY   A O    1 
ATOM   1225 H H    A GLY   A 1 48  ? 17.957 7.342   -0.480  0.78 15.17 ?  48  GLY   A H    1 
ATOM   1226 H H    B GLY   A 1 48  ? 18.003 7.262   -0.163  0.22 14.17 ?  48  GLY   A H    1 
ATOM   1227 H HA2  A GLY   A 1 48  ? 17.203 5.402   0.068   0.78 14.80 ?  48  GLY   A HA2  1 
ATOM   1228 H HA2  B GLY   A 1 48  ? 17.275 5.340   0.389   0.22 13.75 ?  48  GLY   A HA2  1 
ATOM   1229 H HA3  A GLY   A 1 48  ? 18.556 4.813   -0.489  0.78 14.80 ?  48  GLY   A HA3  1 
ATOM   1230 H HA3  B GLY   A 1 48  ? 18.575 4.722   -0.247  0.22 13.75 ?  48  GLY   A HA3  1 
ATOM   1231 N N    A VAL   A 1 49  ? 18.820 3.855   1.771   0.78 10.82 ?  49  VAL   A N    1 
ATOM   1232 N N    B VAL   A 1 49  ? 19.050 3.759   1.961   0.22 10.65 ?  49  VAL   A N    1 
ATOM   1233 C CA   A VAL   A 1 49  ? 19.290 3.410   3.078   0.78 10.85 ?  49  VAL   A CA   1 
ATOM   1234 C CA   B VAL   A 1 49  ? 19.602 3.291   3.230   0.22 10.21 ?  49  VAL   A CA   1 
ATOM   1235 C C    A VAL   A 1 49  ? 20.609 4.082   3.438   0.78 9.93  ?  49  VAL   A C    1 
ATOM   1236 C C    B VAL   A 1 49  ? 20.881 4.048   3.565   0.22 9.50  ?  49  VAL   A C    1 
ATOM   1237 O O    A VAL   A 1 49  ? 20.813 4.492   4.585   0.78 10.44 ?  49  VAL   A O    1 
ATOM   1238 O O    B VAL   A 1 49  ? 21.083 4.493   4.701   0.22 9.57  ?  49  VAL   A O    1 
ATOM   1239 C CB   A VAL   A 1 49  ? 19.414 1.874   3.108   0.78 12.16 ?  49  VAL   A CB   1 
ATOM   1240 C CB   B VAL   A 1 49  ? 19.849 1.772   3.176   0.22 10.02 ?  49  VAL   A CB   1 
ATOM   1241 C CG1  A VAL   A 1 49  ? 20.160 1.420   4.361   0.78 12.95 ?  49  VAL   A CG1  1 
ATOM   1242 C CG1  B VAL   A 1 49  ? 20.617 1.313   4.410   0.22 9.45  ?  49  VAL   A CG1  1 
ATOM   1243 C CG2  A VAL   A 1 49  ? 18.042 1.236   3.031   0.78 14.43 ?  49  VAL   A CG2  1 
ATOM   1244 C CG2  B VAL   A 1 49  ? 18.537 1.014   3.037   0.22 10.42 ?  49  VAL   A CG2  1 
ATOM   1245 H H    A VAL   A 1 49  ? 18.696 3.212   1.208   0.78 13.00 ?  49  VAL   A H    1 
ATOM   1246 H H    B VAL   A 1 49  ? 18.940 3.141   1.374   0.22 12.80 ?  49  VAL   A H    1 
ATOM   1247 H HA   A VAL   A 1 49  ? 18.642 3.659   3.752   0.78 13.04 ?  49  VAL   A HA   1 
ATOM   1248 H HA   B VAL   A 1 49  ? 18.965 3.464   3.937   0.22 12.26 ?  49  VAL   A HA   1 
ATOM   1249 H HB   A VAL   A 1 49  ? 19.933 1.580   2.342   0.78 14.61 ?  49  VAL   A HB   1 
ATOM   1250 H HB   B VAL   A 1 49  ? 20.392 1.569   2.399   0.22 12.04 ?  49  VAL   A HB   1 
ATOM   1251 H HG11 A VAL   A 1 49  ? 19.983 0.477   4.509   0.78 15.55 ?  49  VAL   A HG11 1 
ATOM   1252 H HG11 B VAL   A 1 49  ? 20.507 0.355   4.513   0.22 11.35 ?  49  VAL   A HG11 1 
ATOM   1253 H HG12 A VAL   A 1 49  ? 21.111 1.562   4.244   0.78 15.55 ?  49  VAL   A HG12 1 
ATOM   1254 H HG12 B VAL   A 1 49  ? 21.558 1.524   4.299   0.22 11.35 ?  49  VAL   A HG12 1 
ATOM   1255 H HG13 A VAL   A 1 49  ? 19.838 1.934   5.122   0.78 15.55 ?  49  VAL   A HG13 1 
ATOM   1256 H HG13 B VAL   A 1 49  ? 20.264 1.769   5.190   0.22 11.35 ?  49  VAL   A HG13 1 
ATOM   1257 H HG21 A VAL   A 1 49  ? 18.142 0.271   3.057   0.78 17.33 ?  49  VAL   A HG21 1 
ATOM   1258 H HG21 B VAL   A 1 49  ? 18.726 0.066   2.957   0.22 12.52 ?  49  VAL   A HG21 1 
ATOM   1259 H HG22 A VAL   A 1 49  ? 17.515 1.536   3.787   0.78 17.33 ?  49  VAL   A HG22 1 
ATOM   1260 H HG22 B VAL   A 1 49  ? 17.996 1.177   3.826   0.22 12.52 ?  49  VAL   A HG22 1 
ATOM   1261 H HG23 A VAL   A 1 49  ? 17.623 1.505   2.202   0.78 17.33 ?  49  VAL   A HG23 1 
ATOM   1262 H HG23 B VAL   A 1 49  ? 18.073 1.328   2.246   0.22 12.52 ?  49  VAL   A HG23 1 
ATOM   1263 N N    A ALA   A 1 50  ? 21.537 4.161   2.481   0.78 9.74  ?  50  ALA   A N    1 
ATOM   1264 N N    B ALA   A 1 50  ? 21.771 4.191   2.580   0.22 9.26  ?  50  ALA   A N    1 
ATOM   1265 C CA   A ALA   A 1 50  ? 22.860 4.708   2.772   0.78 9.78  ?  50  ALA   A CA   1 
ATOM   1266 C CA   B ALA   A 1 50  ? 23.071 4.801   2.840   0.22 9.35  ?  50  ALA   A CA   1 
ATOM   1267 C C    A ALA   A 1 50  ? 22.775 6.161   3.210   0.78 9.59  ?  50  ALA   A C    1 
ATOM   1268 C C    B ALA   A 1 50  ? 22.918 6.255   3.266   0.22 9.28  ?  50  ALA   A C    1 
ATOM   1269 O O    A ALA   A 1 50  ? 23.425 6.571   4.179   0.78 10.21 ?  50  ALA   A O    1 
ATOM   1270 O O    B ALA   A 1 50  ? 23.521 6.694   4.252   0.22 9.07  ?  50  ALA   A O    1 
ATOM   1271 C CB   A ALA   A 1 50  ? 23.759 4.579   1.544   0.78 9.55  ?  50  ALA   A CB   1 
ATOM   1272 C CB   B ALA   A 1 50  ? 23.964 4.681   1.603   0.22 9.30  ?  50  ALA   A CB   1 
ATOM   1273 H H    A ALA   A 1 50  ? 21.427 3.899   1.669   0.78 11.70 ?  50  ALA   A H    1 
ATOM   1274 H H    B ALA   A 1 50  ? 21.643 3.953   1.764   0.22 11.13 ?  50  ALA   A H    1 
ATOM   1275 H HA   A ALA   A 1 50  ? 23.261 4.207   3.496   0.78 11.75 ?  50  ALA   A HA   1 
ATOM   1276 H HA   B ALA   A 1 50  ? 23.504 4.330   3.563   0.22 11.23 ?  50  ALA   A HA   1 
ATOM   1277 H HB1  A ALA   A 1 50  ? 24.631 4.951   1.752   0.78 11.48 ?  50  ALA   A HB1  1 
ATOM   1278 H HB1  B ALA   A 1 50  ? 24.828 5.081   1.794   0.22 11.18 ?  50  ALA   A HB1  1 
ATOM   1279 H HB2  A ALA   A 1 50  ? 23.844 3.643   1.312   0.78 11.48 ?  50  ALA   A HB2  1 
ATOM   1280 H HB2  B ALA   A 1 50  ? 24.080 3.741   1.386   0.22 11.18 ?  50  ALA   A HB2  1 
ATOM   1281 H HB3  A ALA   A 1 50  ? 23.359 5.069   0.807   0.78 11.48 ?  50  ALA   A HB3  1 
ATOM   1282 H HB3  B ALA   A 1 50  ? 23.545 5.141   0.859   0.22 11.18 ?  50  ALA   A HB3  1 
ATOM   1283 N N    A GLY   A 1 51  ? 22.000 6.971   2.488   0.78 9.93  ?  51  GLY   A N    1 
ATOM   1284 N N    B GLY   A 1 51  ? 22.108 7.019   2.532   0.22 9.72  ?  51  GLY   A N    1 
ATOM   1285 C CA   A GLY   A 1 51  ? 21.863 8.363   2.877   0.78 10.70 ?  51  GLY   A CA   1 
ATOM   1286 C CA   B GLY   A 1 51  ? 21.884 8.404   2.907   0.22 10.24 ?  51  GLY   A CA   1 
ATOM   1287 C C    A GLY   A 1 51  ? 21.272 8.504   4.263   0.78 10.53 ?  51  GLY   A C    1 
ATOM   1288 C C    B GLY   A 1 51  ? 21.247 8.534   4.276   0.22 10.44 ?  51  GLY   A C    1 
ATOM   1289 O O    A GLY   A 1 51  ? 21.668 9.385   5.031   0.78 11.13 ?  51  GLY   A O    1 
ATOM   1290 O O    B GLY   A 1 51  ? 21.590 9.434   5.048   0.22 10.70 ?  51  GLY   A O    1 
ATOM   1291 H H    A GLY   A 1 51  ? 21.563 6.744   1.780   0.78 11.93 ?  51  GLY   A H    1 
ATOM   1292 H H    B GLY   A 1 51  ? 21.687 6.762   1.826   0.22 11.68 ?  51  GLY   A H    1 
ATOM   1293 H HA2  A GLY   A 1 51  ? 22.733 8.791   2.870   0.78 12.86 ?  51  GLY   A HA2  1 
ATOM   1294 H HA2  B GLY   A 1 51  ? 22.731 8.878   2.917   0.22 12.30 ?  51  GLY   A HA2  1 
ATOM   1295 H HA3  A GLY   A 1 51  ? 21.287 8.823   2.246   0.78 12.86 ?  51  GLY   A HA3  1 
ATOM   1296 H HA3  B GLY   A 1 51  ? 21.303 8.826   2.255   0.22 12.30 ?  51  GLY   A HA3  1 
ATOM   1297 N N    . ALA   A 1 52  ? 20.313 7.635   4.599   1.00 10.68 ?  52  ALA   A N    1 
ATOM   1298 C CA   . ALA   A 1 52  ? 19.672 7.685   5.907   1.00 11.27 ?  52  ALA   A CA   1 
ATOM   1299 C C    . ALA   A 1 52  ? 20.627 7.269   7.023   1.00 10.44 ?  52  ALA   A C    1 
ATOM   1300 O O    . ALA   A 1 52  ? 20.696 7.924   8.068   1.00 11.62 ?  52  ALA   A O    1 
ATOM   1301 C CB   . ALA   A 1 52  ? 18.430 6.800   5.893   1.00 12.64 ?  52  ALA   A CB   1 
ATOM   1302 H H    A ALA   A 1 52  ? 20.031 6.999   4.087   0.78 12.83 ?  52  ALA   A H    1 
ATOM   1303 H H    B ALA   A 1 52  ? 20.051 6.989   4.089   0.22 12.83 ?  52  ALA   A H    1 
ATOM   1304 H HA   . ALA   A 1 52  ? 19.389 8.589   6.080   1.00 13.53 ?  52  ALA   A HA   1 
ATOM   1305 H HB1  . ALA   A 1 52  ? 18.002 6.845   6.762   1.00 15.18 ?  52  ALA   A HB1  1 
ATOM   1306 H HB2  . ALA   A 1 52  ? 17.825 7.117   5.206   1.00 15.18 ?  52  ALA   A HB2  1 
ATOM   1307 H HB3  . ALA   A 1 52  ? 18.693 5.883   5.703   1.00 15.18 ?  52  ALA   A HB3  1 
ATOM   1308 N N    A LEU   A 1 53  ? 21.345 6.159   6.838   0.78 10.20 ?  53  LEU   A N    1 
ATOM   1309 N N    B LEU   A 1 53  ? 21.384 6.186   6.821   0.22 10.32 ?  53  LEU   A N    1 
ATOM   1310 C CA   A LEU   A 1 53  ? 22.311 5.739   7.852   0.78 10.71 ?  53  LEU   A CA   1 
ATOM   1311 C CA   B LEU   A 1 53  ? 22.378 5.795   7.818   0.22 10.40 ?  53  LEU   A CA   1 
ATOM   1312 C C    A LEU   A 1 53  ? 23.374 6.808   8.049   0.78 10.43 ?  53  LEU   A C    1 
ATOM   1313 C C    B LEU   A 1 53  ? 23.407 6.902   8.020   0.22 10.16 ?  53  LEU   A C    1 
ATOM   1314 O O    A LEU   A 1 53  ? 23.726 7.148   9.184   0.78 11.50 ?  53  LEU   A O    1 
ATOM   1315 O O    B LEU   A 1 53  ? 23.695 7.301   9.154   0.22 10.21 ?  53  LEU   A O    1 
ATOM   1316 C CB   A LEU   A 1 53  ? 22.965 4.409   7.467   0.78 11.09 ?  53  LEU   A CB   1 
ATOM   1317 C CB   B LEU   A 1 53  ? 23.070 4.488   7.410   0.22 10.49 ?  53  LEU   A CB   1 
ATOM   1318 C CG   A LEU   A 1 53  ? 22.073 3.167   7.521   0.78 11.78 ?  53  LEU   A CG   1 
ATOM   1319 C CG   B LEU   A 1 53  ? 22.277 3.178   7.480   0.22 10.66 ?  53  LEU   A CG   1 
ATOM   1320 C CD1  A LEU   A 1 53  ? 22.766 1.994   6.846   0.78 11.86 ?  53  LEU   A CD1  1 
ATOM   1321 C CD1  B LEU   A 1 53  ? 23.176 1.990   7.123   0.22 9.86  ?  53  LEU   A CD1  1 
ATOM   1322 C CD2  A LEU   A 1 53  ? 21.721 2.797   8.955   0.78 12.95 ?  53  LEU   A CD2  1 
ATOM   1323 C CD2  B LEU   A 1 53  ? 21.633 2.978   8.849   0.22 11.60 ?  53  LEU   A CD2  1 
ATOM   1324 H H    A LEU   A 1 53  ? 21.300 5.641   6.147   0.78 12.25 ?  53  LEU   A H    1 
ATOM   1325 H H    B LEU   A 1 53  ? 21.344 5.671   6.130   0.22 12.40 ?  53  LEU   A H    1 
ATOM   1326 H HA   A LEU   A 1 53  ? 21.852 5.615   8.693   0.78 12.86 ?  53  LEU   A HA   1 
ATOM   1327 H HA   B LEU   A 1 53  ? 21.933 5.650   8.666   0.22 12.49 ?  53  LEU   A HA   1 
ATOM   1328 H HB2  A LEU   A 1 53  ? 23.299 4.482   6.558   0.78 13.32 ?  53  LEU   A HB2  1 
ATOM   1329 H HB2  B LEU   A 1 53  ? 23.366 4.582   6.491   0.22 12.60 ?  53  LEU   A HB2  1 
ATOM   1330 H HB3  A LEU   A 1 53  ? 23.710 4.248   8.069   0.78 13.32 ?  53  LEU   A HB3  1 
ATOM   1331 H HB3  B LEU   A 1 53  ? 23.847 4.373   7.980   0.22 12.60 ?  53  LEU   A HB3  1 
ATOM   1332 H HG   A LEU   A 1 53  ? 21.245 3.349   7.041   0.78 14.15 ?  53  LEU   A HG   1 
ATOM   1333 H HG   B LEU   A 1 53  ? 21.567 3.207   6.824   0.22 12.81 ?  53  LEU   A HG   1 
ATOM   1334 H HD11 A LEU   A 1 53  ? 22.183 1.219   6.891   0.78 14.25 ?  53  LEU   A HD11 1 
ATOM   1335 H HD11 B LEU   A 1 53  ? 22.657 1.170   7.174   0.22 11.84 ?  53  LEU   A HD11 1 
ATOM   1336 H HD12 A LEU   A 1 53  ? 22.938 2.223   5.919   0.78 14.25 ?  53  LEU   A HD12 1 
ATOM   1337 H HD12 B LEU   A 1 53  ? 23.515 2.108   6.221   0.22 11.84 ?  53  LEU   A HD12 1 
ATOM   1338 H HD13 A LEU   A 1 53  ? 23.596 1.815   7.306   0.78 14.25 ?  53  LEU   A HD13 1 
ATOM   1339 H HD13 B LEU   A 1 53  ? 23.917 1.949   7.750   0.22 11.84 ?  53  LEU   A HD13 1 
ATOM   1340 H HD21 A LEU   A 1 53  ? 21.185 1.990   8.950   0.78 15.55 ?  53  LEU   A HD21 1 
ATOM   1341 H HD21 B LEU   A 1 53  ? 21.123 2.153   8.842   0.22 13.94 ?  53  LEU   A HD21 1 
ATOM   1342 H HD22 A LEU   A 1 53  ? 22.542 2.648   9.449   0.78 15.55 ?  53  LEU   A HD22 1 
ATOM   1343 H HD22 B LEU   A 1 53  ? 22.329 2.930   9.522   0.22 13.94 ?  53  LEU   A HD22 1 
ATOM   1344 H HD23 A LEU   A 1 53  ? 21.221 3.525   9.356   0.78 15.55 ?  53  LEU   A HD23 1 
ATOM   1345 H HD23 B LEU   A 1 53  ? 21.044 3.725   9.036   0.22 13.94 ?  53  LEU   A HD23 1 
ATOM   1346 N N    A ASN   A 1 54  ? 23.882 7.365   6.953   0.78 9.77  ?  54  ASN   A N    1 
ATOM   1347 N N    B ASN   A 1 54  ? 23.963 7.420   6.923   0.22 10.03 ?  54  ASN   A N    1 
ATOM   1348 C CA   A ASN   A 1 54  ? 24.937 8.360   7.081   0.78 9.90  ?  54  ASN   A CA   1 
ATOM   1349 C CA   B ASN   A 1 54  ? 25.003 8.438   7.038   0.22 9.99  ?  54  ASN   A CA   1 
ATOM   1350 C C    A ASN   A 1 54  ? 24.436 9.604   7.810   0.78 10.45 ?  54  ASN   A C    1 
ATOM   1351 C C    B ASN   A 1 54  ? 24.482 9.688   7.737   0.22 10.30 ?  54  ASN   A C    1 
ATOM   1352 O O    A ASN   A 1 54  ? 25.122 10.135  8.694   0.78 10.75 ?  54  ASN   A O    1 
ATOM   1353 O O    B ASN   A 1 54  ? 25.199 10.308  8.533   0.22 10.37 ?  54  ASN   A O    1 
ATOM   1354 C CB   A ASN   A 1 54  ? 25.494 8.727   5.716   0.78 10.19 ?  54  ASN   A CB   1 
ATOM   1355 C CB   B ASN   A 1 54  ? 25.564 8.781   5.660   0.22 10.20 ?  54  ASN   A CB   1 
ATOM   1356 C CG   A ASN   A 1 54  ? 26.530 9.812   5.825   0.78 9.99  ?  54  ASN   A CG   1 
ATOM   1357 C CG   B ASN   A 1 54  ? 26.510 9.962   5.704   0.22 10.36 ?  54  ASN   A CG   1 
ATOM   1358 O OD1  A ASN   A 1 54  ? 27.517 9.667   6.553   0.78 9.53  ?  54  ASN   A OD1  1 
ATOM   1359 O OD1  B ASN   A 1 54  ? 27.591 9.881   6.285   0.22 10.66 ?  54  ASN   A OD1  1 
ATOM   1360 N ND2  A ASN   A 1 54  ? 26.305 10.920  5.141   0.78 11.14 ?  54  ASN   A ND2  1 
ATOM   1361 N ND2  B ASN   A 1 54  ? 26.106 11.070  5.095   0.22 10.53 ?  54  ASN   A ND2  1 
ATOM   1362 H H    A ASN   A 1 54  ? 23.636 7.189   6.146   0.78 11.74 ?  54  ASN   A H    1 
ATOM   1363 H H    B ASN   A 1 54  ? 23.759 7.201   6.119   0.22 12.05 ?  54  ASN   A H    1 
ATOM   1364 H HA   A ASN   A 1 54  ? 25.656 7.980   7.604   0.78 11.89 ?  54  ASN   A HA   1 
ATOM   1365 H HA   B ASN   A 1 54  ? 25.726 8.086   7.576   0.22 12.00 ?  54  ASN   A HA   1 
ATOM   1366 H HB2  A ASN   A 1 54  ? 25.915 7.935   5.323   0.78 12.24 ?  54  ASN   A HB2  1 
ATOM   1367 H HB2  B ASN   A 1 54  ? 26.055 8.013   5.322   0.22 12.25 ?  54  ASN   A HB2  1 
ATOM   1368 H HB3  A ASN   A 1 54  ? 24.781 9.037   5.145   0.78 12.24 ?  54  ASN   A HB3  1 
ATOM   1369 H HB3  B ASN   A 1 54  ? 24.833 8.998   5.064   0.22 12.25 ?  54  ASN   A HB3  1 
ATOM   1370 H HD21 A ASN   A 1 54  ? 26.871 11.564  5.178   0.78 13.38 ?  54  ASN   A HD21 1 
ATOM   1371 H HD21 B ASN   A 1 54  ? 26.609 11.767  5.096   0.22 12.65 ?  54  ASN   A HD21 1 
ATOM   1372 H HD22 A ASN   A 1 54  ? 25.600 10.989  4.657   0.78 13.38 ?  54  ASN   A HD22 1 
ATOM   1373 H HD22 B ASN   A 1 54  ? 25.345 11.088  4.696   0.22 12.65 ?  54  ASN   A HD22 1 
ATOM   1374 N N    . LYS   A 1 55  ? 23.234 10.076  7.458   1.00 10.61 ?  55  LYS   A N    1 
ATOM   1375 C CA   . LYS   A 1 55  ? 22.658 11.233  8.131   1.00 11.30 ?  55  LYS   A CA   1 
ATOM   1376 C C    . LYS   A 1 55  ? 22.571 10.993  9.632   1.00 11.44 ?  55  LYS   A C    1 
ATOM   1377 O O    . LYS   A 1 55  ? 22.855 11.891  10.433  1.00 12.25 ?  55  LYS   A O    1 
ATOM   1378 C CB   . LYS   A 1 55  ? 21.283 11.533  7.526   1.00 12.31 ?  55  LYS   A CB   1 
ATOM   1379 C CG   . LYS   A 1 55  ? 20.551 12.708  8.144   1.00 13.64 ?  55  LYS   A CG   1 
ATOM   1380 C CD   . LYS   A 1 55  ? 19.225 12.957  7.419   1.00 15.04 ?  55  LYS   A CD   1 
ATOM   1381 C CE   . LYS   A 1 55  ? 18.410 14.061  8.073   1.00 17.06 ?  55  LYS   A CE   1 
ATOM   1382 N NZ   . LYS   A 1 55  ? 17.079 14.231  7.419   1.00 17.85 ?  55  LYS   A NZ   1 
ATOM   1383 H H    A LYS   A 1 55  ? 22.732 9.737   6.841   0.78 12.75 ?  55  LYS   A H    1 
ATOM   1384 H H    B LYS   A 1 55  ? 22.704 9.682   6.899   0.22 12.75 ?  55  LYS   A H    1 
ATOM   1385 H HA   . LYS   A 1 55  ? 23.225 12.002  7.980   1.00 13.58 ?  55  LYS   A HA   1 
ATOM   1386 H HB2  . LYS   A 1 55  ? 21.396 11.729  6.583   1.00 14.78 ?  55  LYS   A HB2  1 
ATOM   1387 H HB3  . LYS   A 1 55  ? 20.719 10.751  7.630   1.00 14.78 ?  55  LYS   A HB3  1 
ATOM   1388 H HG2  . LYS   A 1 55  ? 20.355 12.510  9.075   1.00 16.38 ?  55  LYS   A HG2  1 
ATOM   1389 H HG3  . LYS   A 1 55  ? 21.096 13.502  8.072   1.00 16.38 ?  55  LYS   A HG3  1 
ATOM   1390 H HD2  . LYS   A 1 55  ? 19.413 13.216  6.503   1.00 18.07 ?  55  LYS   A HD2  1 
ATOM   1391 H HD3  . LYS   A 1 55  ? 18.700 12.140  7.431   1.00 18.07 ?  55  LYS   A HD3  1 
ATOM   1392 H HE2  . LYS   A 1 55  ? 18.265 13.837  9.007   1.00 20.49 ?  55  LYS   A HE2  1 
ATOM   1393 H HE3  . LYS   A 1 55  ? 18.895 14.897  8.002   1.00 20.49 ?  55  LYS   A HE3  1 
ATOM   1394 H HZ1  . LYS   A 1 55  ? 16.624 14.881  7.821   1.00 21.44 ?  55  LYS   A HZ1  1 
ATOM   1395 H HZ2  . LYS   A 1 55  ? 17.187 14.440  6.561   1.00 21.44 ?  55  LYS   A HZ2  1 
ATOM   1396 H HZ3  . LYS   A 1 55  ? 16.613 13.474  7.476   1.00 21.44 ?  55  LYS   A HZ3  1 
ATOM   1397 N N    . ALA   A 1 56  ? 22.189 9.779   10.031  1.00 11.54 ?  56  ALA   A N    1 
ATOM   1398 C CA   . ALA   A 1 56  ? 22.075 9.447   11.446  1.00 12.48 ?  56  ALA   A CA   1 
ATOM   1399 C C    . ALA   A 1 56  ? 23.417 9.471   12.168  1.00 12.34 ?  56  ALA   A C    1 
ATOM   1400 O O    . ALA   A 1 56  ? 23.442 9.662   13.388  1.00 13.78 ?  56  ALA   A O    1 
ATOM   1401 C CB   . ALA   A 1 56  ? 21.391 8.085   11.610  1.00 13.81 ?  56  ALA   A CB   1 
ATOM   1402 H H    . ALA   A 1 56  ? 21.993 9.132   9.497   1.00 13.86 ?  56  ALA   A H    1 
ATOM   1403 H HA   . ALA   A 1 56  ? 21.508 10.101  11.870  1.00 14.99 ?  56  ALA   A HA   1 
ATOM   1404 H HB1  . ALA   A 1 56  ? 21.319 7.877   12.558  1.00 16.58 ?  56  ALA   A HB1  1 
ATOM   1405 H HB2  . ALA   A 1 56  ? 20.503 8.125   11.217  1.00 16.58 ?  56  ALA   A HB2  1 
ATOM   1406 H HB3  . ALA   A 1 56  ? 21.917 7.402   11.164  1.00 16.58 ?  56  ALA   A HB3  1 
ATOM   1407 N N    . THR   A 1 57  ? 24.527 9.286   11.449  1.00 11.52 ?  57  THR   A N    1 
ATOM   1408 C CA   . THR   A 1 57  ? 25.868 9.409   12.022  1.00 11.49 ?  57  THR   A CA   1 
ATOM   1409 C C    . THR   A 1 57  ? 26.418 10.826  11.947  1.00 11.80 ?  57  THR   A C    1 
ATOM   1410 O O    . THR   A 1 57  ? 27.601 11.032  12.244  1.00 12.42 ?  57  THR   A O    1 
ATOM   1411 C CB   . THR   A 1 57  ? 26.878 8.464   11.344  1.00 11.40 ?  57  THR   A CB   1 
ATOM   1412 O OG1  . THR   A 1 57  ? 27.251 8.965   10.049  1.00 11.25 ?  57  THR   A OG1  1 
ATOM   1413 C CG2  . THR   A 1 57  ? 26.329 7.057   11.225  1.00 11.52 ?  57  THR   A CG2  1 
ATOM   1414 H H    . THR   A 1 57  ? 24.528 9.071   10.612  1.00 13.84 ?  57  THR   A H    1 
ATOM   1415 H HA   . THR   A 1 57  ? 25.820 9.146   12.960  1.00 13.80 ?  57  THR   A HA   1 
ATOM   1416 H HB   . THR   A 1 57  ? 27.674 8.407   11.902  1.00 13.69 ?  57  THR   A HB   1 
ATOM   1417 H HG1  . THR   A 1 57  ? 26.572 9.021   9.565   1.00 13.52 ?  57  THR   A HG1  1 
ATOM   1418 H HG21 . THR   A 1 57  ? 27.041 6.429   11.032  1.00 13.84 ?  57  THR   A HG21 1 
ATOM   1419 H HG22 . THR   A 1 57  ? 25.893 6.793   12.053  1.00 13.84 ?  57  THR   A HG22 1 
ATOM   1420 H HG23 . THR   A 1 57  ? 25.675 7.016   10.507  1.00 13.84 ?  57  THR   A HG23 1 
ATOM   1421 N N    . ASN   A 1 58  ? 25.603 11.802  11.550  1.00 12.34 ?  58  ASN   A N    1 
ATOM   1422 C CA   . ASN   A 1 58  ? 26.066 13.182  11.449  1.00 12.97 ?  58  ASN   A CA   1 
ATOM   1423 C C    . ASN   A 1 58  ? 27.211 13.309  10.438  1.00 11.81 ?  58  ASN   A C    1 
ATOM   1424 O O    . ASN   A 1 58  ? 28.109 14.142  10.593  1.00 12.78 ?  58  ASN   A O    1 
ATOM   1425 C CB   . ASN   A 1 58  ? 26.448 13.720  12.841  1.00 16.22 ?  58  ASN   A CB   1 
ATOM   1426 C CG   . ASN   A 1 58  ? 26.857 15.176  12.834  1.00 19.95 ?  58  ASN   A CG   1 
ATOM   1427 O OD1  . ASN   A 1 58  ? 26.220 16.002  12.192  1.00 21.30 ?  58  ASN   A OD1  1 
ATOM   1428 N ND2  . ASN   A 1 58  ? 27.928 15.500  13.563  1.00 21.18 ?  58  ASN   A ND2  1 
ATOM   1429 H H    . ASN   A 1 58  ? 24.780 11.679  11.324  1.00 14.82 ?  58  ASN   A H    1 
ATOM   1430 H HA   . ASN   A 1 58  ? 25.327 13.716  11.124  1.00 15.58 ?  58  ASN   A HA   1 
ATOM   1431 H HB2  . ASN   A 1 58  ? 25.680 13.622  13.434  1.00 19.47 ?  58  ASN   A HB2  1 
ATOM   1432 H HB3  . ASN   A 1 58  ? 27.191 13.206  13.187  1.00 19.47 ?  58  ASN   A HB3  1 
ATOM   1433 H HD21 . ASN   A 1 58  ? 28.193 16.318  13.597  1.00 25.43 ?  58  ASN   A HD21 1 
ATOM   1434 H HD22 . ASN   A 1 58  ? 28.345 14.892  14.001  1.00 25.43 ?  58  ASN   A HD22 1 
ATOM   1435 N N    . ASN   A 1 59  ? 27.184 12.491  9.382   1.00 11.03 ?  59  ASN   A N    1 
ATOM   1436 C CA   . ASN   A 1 59  ? 28.157 12.474  8.280   1.00 11.02 ?  59  ASN   A CA   1 
ATOM   1437 C C    . ASN   A 1 59  ? 29.475 11.793  8.658   1.00 10.64 ?  59  ASN   A C    1 
ATOM   1438 O O    . ASN   A 1 59  ? 30.388 11.751  7.827   1.00 10.80 ?  59  ASN   A O    1 
ATOM   1439 C CB   . ASN   A 1 59  ? 28.438 13.861  7.674   1.00 11.27 ?  59  ASN   A CB   1 
ATOM   1440 C CG   . ASN   A 1 59  ? 28.785 13.795  6.204   1.00 11.26 ?  59  ASN   A CG   1 
ATOM   1441 O OD1  . ASN   A 1 59  ? 28.072 13.178  5.413   1.00 11.87 ?  59  ASN   A OD1  1 
ATOM   1442 N ND2  . ASN   A 1 59  ? 29.876 14.449  5.823   1.00 12.14 ?  59  ASN   A ND2  1 
ATOM   1443 H H    . ASN   A 1 59  ? 26.567 11.901  9.269   1.00 13.25 ?  59  ASN   A H    1 
ATOM   1444 H HA   . ASN   A 1 59  ? 27.771 11.943  7.569   1.00 13.24 ?  59  ASN   A HA   1 
ATOM   1445 H HB2  . ASN   A 1 59  ? 27.647 14.415  7.761   1.00 13.54 ?  59  ASN   A HB2  1 
ATOM   1446 H HB3  . ASN   A 1 59  ? 29.184 14.268  8.135   1.00 13.54 ?  59  ASN   A HB3  1 
ATOM   1447 H HD21 . ASN   A 1 59  ? 30.122 14.443  4.997   1.00 14.59 ?  59  ASN   A HD21 1 
ATOM   1448 H HD22 . ASN   A 1 59  ? 30.358 14.868  6.405   1.00 14.59 ?  59  ASN   A HD22 1 
ATOM   1449 N N    . ALA   A 1 60  ? 29.604 11.244  9.864   1.00 10.66 ?  60  ALA   A N    1 
ATOM   1450 C CA   . ALA   A 1 60  ? 30.841 10.553  10.216  1.00 11.07 ?  60  ALA   A CA   1 
ATOM   1451 C C    . ALA   A 1 60  ? 31.061 9.318   9.349   1.00 10.95 ?  60  ALA   A C    1 
ATOM   1452 O O    . ALA   A 1 60  ? 32.205 8.993   9.007   1.00 11.35 ?  60  ALA   A O    1 
ATOM   1453 C CB   . ALA   A 1 60  ? 30.836 10.185  11.698  1.00 11.72 ?  60  ALA   A CB   1 
ATOM   1454 H H    . ALA   A 1 60  ? 29.008 11.256  10.482  1.00 12.80 ?  60  ALA   A H    1 
ATOM   1455 H HA   . ALA   A 1 60  ? 31.588 11.156  10.061  1.00 13.30 ?  60  ALA   A HA   1 
ATOM   1456 H HB1  . ALA   A 1 60  ? 31.665 9.730   11.912  1.00 14.07 ?  60  ALA   A HB1  1 
ATOM   1457 H HB2  . ALA   A 1 60  ? 30.761 10.999  12.224  1.00 14.07 ?  60  ALA   A HB2  1 
ATOM   1458 H HB3  . ALA   A 1 60  ? 30.082 9.605   11.876  1.00 14.07 ?  60  ALA   A HB3  1 
ATOM   1459 N N    . MET   A 1 61  ? 29.985 8.627   8.970   1.00 10.53 ?  61  MET   A N    1 
ATOM   1460 C CA   . MET   A 1 61  ? 30.124 7.493   8.063   1.00 10.30 ?  61  MET   A CA   1 
ATOM   1461 C C    . MET   A 1 61  ? 30.755 7.922   6.740   1.00 10.03 ?  61  MET   A C    1 
ATOM   1462 O O    . MET   A 1 61  ? 31.644 7.240   6.216   1.00 10.57 ?  61  MET   A O    1 
ATOM   1463 C CB   . MET   A 1 61  ? 28.759 6.834   7.851   1.00 10.33 ?  61  MET   A CB   1 
ATOM   1464 C CG   . MET   A 1 61  ? 28.766 5.675   6.865   1.00 11.07 ?  61  MET   A CG   1 
ATOM   1465 S SD   . MET   A 1 61  ? 27.141 4.938   6.644   1.00 11.98 ?  61  MET   A SD   1 
ATOM   1466 C CE   . MET   A 1 61  ? 26.969 4.031   8.178   1.00 13.67 ?  61  MET   A CE   1 
ATOM   1467 H H    . MET   A 1 61  ? 29.175 8.798   9.212   1.00 12.65 ?  61  MET   A H    1 
ATOM   1468 H HA   . MET   A 1 61  ? 30.701 6.836   8.483   1.00 12.38 ?  61  MET   A HA   1 
ATOM   1469 H HB2  . MET   A 1 61  ? 28.445 6.491   8.703   1.00 12.41 ?  61  MET   A HB2  1 
ATOM   1470 H HB3  . MET   A 1 61  ? 28.140 7.499   7.518   1.00 12.41 ?  61  MET   A HB3  1 
ATOM   1471 H HG2  . MET   A 1 61  ? 29.062 5.991   5.999   1.00 13.29 ?  61  MET   A HG2  1 
ATOM   1472 H HG3  . MET   A 1 61  ? 29.361 4.983   7.190   1.00 13.29 ?  61  MET   A HG3  1 
ATOM   1473 H HE1  . MET   A 1 61  ? 26.121 3.553   8.172   1.00 16.42 ?  61  MET   A HE1  1 
ATOM   1474 H HE2  . MET   A 1 61  ? 27.700 3.399   8.253   1.00 16.42 ?  61  MET   A HE2  1 
ATOM   1475 H HE3  . MET   A 1 61  ? 26.988 4.651   8.924   1.00 16.42 ?  61  MET   A HE3  1 
ATOM   1476 N N    . GLN   A 1 62  ? 30.314 9.057   6.188   1.00 9.99  ?  62  GLN   A N    1 
ATOM   1477 C CA   . GLN   A 1 62  ? 30.873 9.530   4.924   1.00 10.22 ?  62  GLN   A CA   1 
ATOM   1478 C C    . GLN   A 1 62  ? 32.341 9.907   5.066   1.00 10.55 ?  62  GLN   A C    1 
ATOM   1479 O O    . GLN   A 1 62  ? 33.144 9.608   4.178   1.00 10.81 ?  62  GLN   A O    1 
ATOM   1480 C CB   . GLN   A 1 62  ? 30.066 10.714  4.391   1.00 10.32 ?  62  GLN   A CB   1 
ATOM   1481 C CG   . GLN   A 1 62  ? 30.443 11.088  2.967   1.00 10.40 ?  62  GLN   A CG   1 
ATOM   1482 C CD   . GLN   A 1 62  ? 30.115 9.966   2.015   1.00 10.50 ?  62  GLN   A CD   1 
ATOM   1483 O OE1  . GLN   A 1 62  ? 28.935 9.665   1.802   1.00 11.29 ?  62  GLN   A OE1  1 
ATOM   1484 N NE2  . GLN   A 1 62  ? 31.132 9.294   1.486   1.00 11.46 ?  62  GLN   A NE2  1 
ATOM   1485 H H    . GLN   A 1 62  ? 29.703 9.557   6.522   1.00 12.01 ?  62  GLN   A H    1 
ATOM   1486 H HA   . GLN   A 1 62  ? 30.818 8.810   4.275   1.00 12.27 ?  62  GLN   A HA   1 
ATOM   1487 H HB2  . GLN   A 1 62  ? 29.126 10.493  4.408   1.00 12.40 ?  62  GLN   A HB2  1 
ATOM   1488 H HB3  . GLN   A 1 62  ? 30.236 11.489  4.954   1.00 12.40 ?  62  GLN   A HB3  1 
ATOM   1489 H HG2  . GLN   A 1 62  ? 29.936 11.866  2.694   1.00 12.49 ?  62  GLN   A HG2  1 
ATOM   1490 H HG3  . GLN   A 1 62  ? 31.393 11.263  2.914   1.00 12.49 ?  62  GLN   A HG3  1 
ATOM   1491 H HE21 . GLN   A 1 62  ? 31.942 9.522   1.673   1.00 13.77 ?  62  GLN   A HE21 1 
ATOM   1492 H HE22 . GLN   A 1 62  ? 30.986 8.641   0.946   1.00 13.77 ?  62  GLN   A HE22 1 
ATOM   1493 N N    . VAL   A 1 63  ? 32.706 10.582  6.161   1.00 10.87 ?  63  VAL   A N    1 
ATOM   1494 C CA   . VAL   A 1 63  ? 34.099 10.972  6.375   1.00 11.60 ?  63  VAL   A CA   1 
ATOM   1495 C C    . VAL   A 1 63  ? 34.996 9.736   6.420   1.00 11.10 ?  63  VAL   A C    1 
ATOM   1496 O O    . VAL   A 1 63  ? 36.045 9.678   5.763   1.00 11.48 ?  63  VAL   A O    1 
ATOM   1497 C CB   . VAL   A 1 63  ? 34.210 11.833  7.647   1.00 13.24 ?  63  VAL   A CB   1 
ATOM   1498 C CG1  . VAL   A 1 63  ? 35.654 12.069  8.011   1.00 15.15 ?  63  VAL   A CG1  1 
ATOM   1499 C CG2  . VAL   A 1 63  ? 33.486 13.159  7.441   1.00 13.89 ?  63  VAL   A CG2  1 
ATOM   1500 H H    . VAL   A 1 63  ? 32.162 10.830  6.785   1.00 13.06 ?  63  VAL   A H    1 
ATOM   1501 H HA   . VAL   A 1 63  ? 34.380 11.517  5.628   1.00 13.93 ?  63  VAL   A HA   1 
ATOM   1502 H HB   . VAL   A 1 63  ? 33.786 11.369  8.387   1.00 15.91 ?  63  VAL   A HB   1 
ATOM   1503 H HG11 . VAL   A 1 63  ? 35.700 12.795  8.655   1.00 18.20 ?  63  VAL   A HG11 1 
ATOM   1504 H HG12 . VAL   A 1 63  ? 36.024 11.262  8.395   1.00 18.20 ?  63  VAL   A HG12 1 
ATOM   1505 H HG13 . VAL   A 1 63  ? 36.144 12.314  7.209   1.00 18.20 ?  63  VAL   A HG13 1 
ATOM   1506 H HG21 . VAL   A 1 63  ? 33.576 13.699  8.244   1.00 16.69 ?  63  VAL   A HG21 1 
ATOM   1507 H HG22 . VAL   A 1 63  ? 33.880 13.623  6.686   1.00 16.69 ?  63  VAL   A HG22 1 
ATOM   1508 H HG23 . VAL   A 1 63  ? 32.546 12.985  7.268   1.00 16.69 ?  63  VAL   A HG23 1 
ATOM   1509 N N    . GLU   A 1 64  ? 34.583 8.724   7.185   1.00 11.07 ?  64  GLU   A N    1 
ATOM   1510 C CA   . GLU   A 1 64  ? 35.344 7.486   7.268   1.00 11.09 ?  64  GLU   A CA   1 
ATOM   1511 C C    . GLU   A 1 64  ? 35.418 6.799   5.910   1.00 10.65 ?  64  GLU   A C    1 
ATOM   1512 O O    . GLU   A 1 64  ? 36.466 6.255   5.525   1.00 11.17 ?  64  GLU   A O    1 
ATOM   1513 C CB   . GLU   A 1 64  ? 34.665 6.578   8.293   1.00 11.82 ?  64  GLU   A CB   1 
ATOM   1514 C CG   . GLU   A 1 64  ? 35.321 5.229   8.453   1.00 12.86 ?  64  GLU   A CG   1 
ATOM   1515 C CD   . GLU   A 1 64  ? 34.437 4.233   9.177   1.00 13.35 ?  64  GLU   A CD   1 
ATOM   1516 O OE1  . GLU   A 1 64  ? 33.196 4.335   9.045   1.00 14.11 ?  64  GLU   A OE1  1 
ATOM   1517 O OE2  . GLU   A 1 64  ? 34.985 3.334   9.867   1.00 13.64 -1 64  GLU   A OE2  1 
ATOM   1518 H H    . GLU   A 1 64  ? 33.860 8.729   7.652   1.00 13.30 ?  64  GLU   A H    1 
ATOM   1519 H HA   . GLU   A 1 64  ? 36.246 7.683   7.573   1.00 13.32 ?  64  GLU   A HA   1 
ATOM   1520 H HB2  . GLU   A 1 64  ? 34.685 7.024   9.161   1.00 14.20 ?  64  GLU   A HB2  1 
ATOM   1521 H HB3  . GLU   A 1 64  ? 33.747 6.442   8.021   1.00 14.20 ?  64  GLU   A HB3  1 
ATOM   1522 H HG2  . GLU   A 1 64  ? 35.530 4.858   7.580   1.00 15.44 ?  64  GLU   A HG2  1 
ATOM   1523 H HG3  . GLU   A 1 64  ? 36.137 5.331   8.969   1.00 15.44 ?  64  GLU   A HG3  1 
ATOM   1524 N N    . SER   A 1 65  ? 34.301 6.800   5.182   1.00 10.47 ?  65  SER   A N    1 
ATOM   1525 C CA   . SER   A 1 65  ? 34.245 6.147   3.879   1.00 10.37 ?  65  SER   A CA   1 
ATOM   1526 C C    . SER   A 1 65  ? 35.164 6.819   2.871   1.00 10.72 ?  65  SER   A C    1 
ATOM   1527 O O    . SER   A 1 65  ? 35.803 6.144   2.057   1.00 11.45 ?  65  SER   A O    1 
ATOM   1528 C CB   . SER   A 1 65  ? 32.810 6.161   3.352   1.00 10.30 ?  65  SER   A CB   1 
ATOM   1529 O OG   . SER   A 1 65  ? 31.965 5.334   4.142   1.00 10.94 ?  65  SER   A OG   1 
ATOM   1530 H H    . SER   A 1 65  ? 33.564 7.177   5.420   1.00 12.57 ?  65  SER   A H    1 
ATOM   1531 H HA   . SER   A 1 65  ? 34.526 5.224   3.973   1.00 12.46 ?  65  SER   A HA   1 
ATOM   1532 H HB2  . SER   A 1 65  ? 32.476 7.069   3.372   1.00 12.37 ?  65  SER   A HB2  1 
ATOM   1533 H HB3  . SER   A 1 65  ? 32.812 5.827   2.440   1.00 12.37 ?  65  SER   A HB3  1 
ATOM   1534 H HG   . SER   A 1 65  ? 31.961 5.616   4.938   1.00 13.14 ?  65  SER   A HG   1 
ATOM   1535 N N    . ASP   A 1 66  ? 35.237 8.151   2.896   1.00 10.73 ?  66  ASP   A N    1 
ATOM   1536 C CA   . ASP   A 1 66  ? 36.095 8.853   1.947   1.00 11.70 ?  66  ASP   A CA   1 
ATOM   1537 C C    . ASP   A 1 66  ? 37.558 8.493   2.172   1.00 11.58 ?  66  ASP   A C    1 
ATOM   1538 O O    . ASP   A 1 66  ? 38.321 8.321   1.214   1.00 12.39 ?  66  ASP   A O    1 
ATOM   1539 C CB   . ASP   A 1 66  ? 35.880 10.360  2.063   1.00 12.83 ?  66  ASP   A CB   1 
ATOM   1540 C CG   . ASP   A 1 66  ? 34.547 10.827  1.469   1.00 14.58 ?  66  ASP   A CG   1 
ATOM   1541 O OD1  . ASP   A 1 66  ? 33.814 10.040  0.829   1.00 15.03 ?  66  ASP   A OD1  1 
ATOM   1542 O OD2  . ASP   A 1 66  ? 34.250 12.028  1.630   1.00 17.57 -1 66  ASP   A OD2  1 
ATOM   1543 H H    . ASP   A 1 66  ? 34.796 8.665   3.436   1.00 12.89 ?  66  ASP   A H    1 
ATOM   1544 H HA   . ASP   A 1 66  ? 35.849 8.586   1.047   1.00 14.06 ?  66  ASP   A HA   1 
ATOM   1545 H HB2  . ASP   A 1 66  ? 35.888 10.612  2.999   1.00 15.41 ?  66  ASP   A HB2  1 
ATOM   1546 H HB3  . ASP   A 1 66  ? 36.595 10.817  1.591   1.00 15.41 ?  66  ASP   A HB3  1 
ATOM   1547 N N    . ASP   A 1 67  ? 37.965 8.362   3.434   1.00 11.73 ?  67  ASP   A N    1 
ATOM   1548 C CA   . ASP   A 1 67  ? 39.320 7.911   3.725   1.00 12.47 ?  67  ASP   A CA   1 
ATOM   1549 C C    . ASP   A 1 67  ? 39.538 6.479   3.249   1.00 12.34 ?  67  ASP   A C    1 
ATOM   1550 O O    . ASP   A 1 67  ? 40.596 6.157   2.695   1.00 12.94 ?  67  ASP   A O    1 
ATOM   1551 C CB   . ASP   A 1 67  ? 39.591 8.033   5.220   1.00 13.78 ?  67  ASP   A CB   1 
ATOM   1552 C CG   . ASP   A 1 67  ? 40.891 7.375   5.629   1.00 15.32 ?  67  ASP   A CG   1 
ATOM   1553 O OD1  . ASP   A 1 67  ? 41.969 7.992   5.460   1.00 17.83 ?  67  ASP   A OD1  1 
ATOM   1554 O OD2  . ASP   A 1 67  ? 40.845 6.220   6.108   1.00 14.90 -1 67  ASP   A OD2  1 
ATOM   1555 H H    . ASP   A 1 67  ? 37.484 8.527   4.123   1.00 14.10 ?  67  ASP   A H    1 
ATOM   1556 H HA   . ASP   A 1 67  ? 39.948 8.474   3.252   1.00 14.97 ?  67  ASP   A HA   1 
ATOM   1557 H HB2  . ASP   A 1 67  ? 39.639 8.970   5.448   1.00 16.55 ?  67  ASP   A HB2  1 
ATOM   1558 H HB3  . ASP   A 1 67  ? 38.868 7.603   5.705   1.00 16.55 ?  67  ASP   A HB3  1 
ATOM   1559 N N    . TYR   A 1 68  ? 38.547 5.601   3.451   1.00 11.78 ?  68  TYR   A N    1 
ATOM   1560 C CA   . TYR   A 1 68  ? 38.663 4.220   2.972   1.00 11.84 ?  68  TYR   A CA   1 
ATOM   1561 C C    . TYR   A 1 68  ? 38.898 4.174   1.463   1.00 11.82 ?  68  TYR   A C    1 
ATOM   1562 O O    . TYR   A 1 68  ? 39.775 3.443   0.979   1.00 12.21 ?  68  TYR   A O    1 
ATOM   1563 C CB   . TYR   A 1 68  ? 37.413 3.395   3.356   1.00 12.30 ?  68  TYR   A CB   1 
ATOM   1564 C CG   . TYR   A 1 68  ? 37.437 2.010   2.723   1.00 13.55 ?  68  TYR   A CG   1 
ATOM   1565 C CD1  . TYR   A 1 68  ? 36.971 1.822   1.425   1.00 14.83 ?  68  TYR   A CD1  1 
ATOM   1566 C CD2  . TYR   A 1 68  ? 37.979 0.917   3.386   1.00 15.31 ?  68  TYR   A CD2  1 
ATOM   1567 C CE1  . TYR   A 1 68  ? 37.033 0.611   0.806   1.00 16.12 ?  68  TYR   A CE1  1 
ATOM   1568 C CE2  . TYR   A 1 68  ? 38.037 -0.338  2.763   1.00 15.79 ?  68  TYR   A CE2  1 
ATOM   1569 C CZ   . TYR   A 1 68  ? 37.569 -0.460  1.473   1.00 16.15 ?  68  TYR   A CZ   1 
ATOM   1570 O OH   . TYR   A 1 68  ? 37.640 -1.668  0.841   1.00 17.53 ?  68  TYR   A OH   1 
ATOM   1571 H H    . TYR   A 1 68  ? 37.802 5.772   3.852   1.00 14.15 ?  68  TYR   A H    1 
ATOM   1572 H HA   . TYR   A 1 68  ? 39.423 3.805   3.399   1.00 14.22 ?  68  TYR   A HA   1 
ATOM   1573 H HB2  . TYR   A 1 68  ? 37.388 3.282   4.320   1.00 14.77 ?  68  TYR   A HB2  1 
ATOM   1574 H HB3  . TYR   A 1 68  ? 36.615 3.852   3.051   1.00 14.77 ?  68  TYR   A HB3  1 
ATOM   1575 H HD1  . TYR   A 1 68  ? 36.624 2.554   0.963   1.00 17.81 ?  68  TYR   A HD1  1 
ATOM   1576 H HD2  . TYR   A 1 68  ? 38.311 1.018   4.247   1.00 18.38 ?  68  TYR   A HD2  1 
ATOM   1577 H HE1  . TYR   A 1 68  ? 36.710 0.514   -0.061  1.00 19.36 ?  68  TYR   A HE1  1 
ATOM   1578 H HE2  . TYR   A 1 68  ? 38.398 -1.073  3.200   1.00 18.97 ?  68  TYR   A HE2  1 
ATOM   1579 H HH   . TYR   A 1 68  ? 37.967 -2.244  1.361   1.00 21.05 ?  68  TYR   A HH   1 
ATOM   1580 N N    . ILE   A 1 69  ? 38.109 4.937   0.697   1.00 11.64 ?  69  ILE   A N    1 
ATOM   1581 C CA   . ILE   A 1 69  ? 38.237 4.927   -0.758  1.00 11.50 ?  69  ILE   A CA   1 
ATOM   1582 C C    . ILE   A 1 69  ? 39.568 5.537   -1.191  1.00 11.33 ?  69  ILE   A C    1 
ATOM   1583 O O    . ILE   A 1 69  ? 40.212 5.056   -2.129  1.00 11.86 ?  69  ILE   A O    1 
ATOM   1584 C CB   . ILE   A 1 69  ? 37.039 5.639   -1.417  1.00 12.25 ?  69  ILE   A CB   1 
ATOM   1585 C CG1  . ILE   A 1 69  ? 35.725 4.905   -1.135  1.00 12.72 ?  69  ILE   A CG1  1 
ATOM   1586 C CG2  . ILE   A 1 69  ? 37.279 5.823   -2.920  1.00 14.06 ?  69  ILE   A CG2  1 
ATOM   1587 C CD1  . ILE   A 1 69  ? 35.557 3.615   -1.910  1.00 13.46 ?  69  ILE   A CD1  1 
ATOM   1588 H H    . ILE   A 1 69  ? 37.503 5.466   0.995   1.00 13.99 ?  69  ILE   A H    1 
ATOM   1589 H HA   . ILE   A 1 69  ? 38.233 4.003   -1.059  1.00 13.82 ?  69  ILE   A HA   1 
ATOM   1590 H HB   . ILE   A 1 69  ? 36.971 6.517   -1.025  1.00 14.71 ?  69  ILE   A HB   1 
ATOM   1591 H HG12 . ILE   A 1 69  ? 35.690 4.686   -0.189  1.00 15.28 ?  69  ILE   A HG12 1 
ATOM   1592 H HG13 . ILE   A 1 69  ? 34.989 5.487   -1.365  1.00 15.28 ?  69  ILE   A HG13 1 
ATOM   1593 H HG21 . ILE   A 1 69  ? 36.433 6.022   -3.352  1.00 16.88 ?  69  ILE   A HG21 1 
ATOM   1594 H HG22 . ILE   A 1 69  ? 37.895 6.564   -3.054  1.00 16.88 ?  69  ILE   A HG22 1 
ATOM   1595 H HG23 . ILE   A 1 69  ? 37.655 5.010   -3.287  1.00 16.88 ?  69  ILE   A HG23 1 
ATOM   1596 H HD11 . ILE   A 1 69  ? 34.762 3.162   -1.589  1.00 16.16 ?  69  ILE   A HD11 1 
ATOM   1597 H HD12 . ILE   A 1 69  ? 35.460 3.824   -2.852  1.00 16.16 ?  69  ILE   A HD12 1 
ATOM   1598 H HD13 . ILE   A 1 69  ? 36.336 3.056   -1.770  1.00 16.16 ?  69  ILE   A HD13 1 
ATOM   1599 N N    . ALA   A 1 70  ? 39.989 6.618   -0.536  1.00 12.00 ?  70  ALA   A N    1 
ATOM   1600 C CA   . ALA   A 1 70  ? 41.264 7.227   -0.898  1.00 12.72 ?  70  ALA   A CA   1 
ATOM   1601 C C    . ALA   A 1 70  ? 42.414 6.242   -0.732  1.00 12.99 ?  70  ALA   A C    1 
ATOM   1602 O O    . ALA   A 1 70  ? 43.370 6.261   -1.510  1.00 14.62 ?  70  ALA   A O    1 
ATOM   1603 C CB   . ALA   A 1 70  ? 41.514 8.477   -0.057  1.00 13.30 ?  70  ALA   A CB   1 
ATOM   1604 H H    . ALA   A 1 70  ? 39.569 7.009   0.102   1.00 14.42 ?  70  ALA   A H    1 
ATOM   1605 H HA   . ALA   A 1 70  ? 41.233 7.500   -1.830  1.00 15.28 ?  70  ALA   A HA   1 
ATOM   1606 H HB1  . ALA   A 1 70  ? 42.373 8.863   -0.317  1.00 15.98 ?  70  ALA   A HB1  1 
ATOM   1607 H HB2  . ALA   A 1 70  ? 40.808 9.115   -0.214  1.00 15.98 ?  70  ALA   A HB2  1 
ATOM   1608 H HB3  . ALA   A 1 70  ? 41.543 8.227   0.879   1.00 15.98 ?  70  ALA   A HB3  1 
ATOM   1609 N N    . THR   A 1 71  ? 42.320 5.352   0.253   1.00 12.39 ?  71  THR   A N    1 
ATOM   1610 C CA   . THR   A 1 71  ? 43.374 4.374   0.499   1.00 13.80 ?  71  THR   A CA   1 
ATOM   1611 C C    . THR   A 1 71  ? 43.252 3.149   -0.400  1.00 13.81 ?  71  THR   A C    1 
ATOM   1612 O O    . THR   A 1 71  ? 44.262 2.643   -0.907  1.00 15.75 ?  71  THR   A O    1 
ATOM   1613 C CB   . THR   A 1 71  ? 43.312 3.931   1.958   1.00 15.53 ?  71  THR   A CB   1 
ATOM   1614 O OG1  . THR   A 1 71  ? 43.568 5.059   2.800   1.00 16.71 ?  71  THR   A OG1  1 
ATOM   1615 C CG2  . THR   A 1 71  ? 44.322 2.826   2.244   1.00 17.21 ?  71  THR   A CG2  1 
ATOM   1616 H H    . THR   A 1 71  ? 41.651 5.285   0.784   1.00 14.89 ?  71  THR   A H    1 
ATOM   1617 H HA   . THR   A 1 71  ? 44.238 4.779   0.336   1.00 16.57 ?  71  THR   A HA   1 
ATOM   1618 H HB   . THR   A 1 71  ? 42.424 3.577   2.141   1.00 18.65 ?  71  THR   A HB   1 
ATOM   1619 H HG1  . THR   A 1 71  ? 42.981 5.646   2.668   1.00 20.06 ?  71  THR   A HG1  1 
ATOM   1620 H HG21 . THR   A 1 71  ? 44.460 2.747   3.201   1.00 20.67 ?  71  THR   A HG21 1 
ATOM   1621 H HG22 . THR   A 1 71  ? 44.005 1.975   1.902   1.00 20.67 ?  71  THR   A HG22 1 
ATOM   1622 H HG23 . THR   A 1 71  ? 45.173 3.037   1.824   1.00 20.67 ?  71  THR   A HG23 1 
ATOM   1623 N N    . ASN   A 1 72  ? 42.030 2.643   -0.587  1.00 12.87 ?  72  ASN   A N    1 
ATOM   1624 C CA   . ASN   A 1 72  ? 41.812 1.318   -1.147  1.00 13.19 ?  72  ASN   A CA   1 
ATOM   1625 C C    . ASN   A 1 72  ? 41.179 1.308   -2.525  1.00 13.44 ?  72  ASN   A C    1 
ATOM   1626 O O    . ASN   A 1 72  ? 41.180 0.253   -3.174  1.00 14.69 ?  72  ASN   A O    1 
ATOM   1627 C CB   . ASN   A 1 72  ? 40.933 0.496   -0.196  1.00 13.79 ?  72  ASN   A CB   1 
ATOM   1628 C CG   . ASN   A 1 72  ? 41.557 0.350   1.168   1.00 14.80 ?  72  ASN   A CG   1 
ATOM   1629 O OD1  . ASN   A 1 72  ? 41.100 0.944   2.144   1.00 16.75 ?  72  ASN   A OD1  1 
ATOM   1630 N ND2  . ASN   A 1 72  ? 42.621 -0.417  1.241   1.00 15.62 ?  72  ASN   A ND2  1 
ATOM   1631 H H    . ASN   A 1 72  ? 41.299 3.064   -0.400  1.00 15.46 ?  72  ASN   A H    1 
ATOM   1632 H HA   . ASN   A 1 72  ? 42.665 0.867   -1.220  1.00 15.84 ?  72  ASN   A HA   1 
ATOM   1633 H HB2  . ASN   A 1 72  ? 40.076 0.935   -0.092  1.00 16.56 ?  72  ASN   A HB2  1 
ATOM   1634 H HB3  . ASN   A 1 72  ? 40.810 -0.394  -0.567  1.00 16.56 ?  72  ASN   A HB3  1 
ATOM   1635 H HD21 . ASN   A 1 72  ? 43.021 -0.524  1.998   1.00 18.75 ?  72  ASN   A HD21 1 
ATOM   1636 H HD22 . ASN   A 1 72  ? 42.927 -0.802  0.537   1.00 18.75 ?  72  ASN   A HD22 1 
ATOM   1637 N N    . GLY   A 1 73  ? 40.625 2.422   -2.980  1.00 12.66 ?  73  GLY   A N    1 
ATOM   1638 C CA   . GLY   A 1 73  ? 39.887 2.440   -4.215  1.00 12.41 ?  73  GLY   A CA   1 
ATOM   1639 C C    . GLY   A 1 73  ? 38.495 1.859   -4.050  1.00 11.99 ?  73  GLY   A C    1 
ATOM   1640 O O    . GLY   A 1 73  ? 38.108 1.400   -2.969  1.00 12.78 ?  73  GLY   A O    1 
ATOM   1641 H H    . GLY   A 1 73  ? 40.667 3.192   -2.589  1.00 15.20 ?  73  GLY   A H    1 
ATOM   1642 H HA2  . GLY   A 1 73  ? 39.808 3.353   -4.534  1.00 14.91 ?  73  GLY   A HA2  1 
ATOM   1643 H HA3  . GLY   A 1 73  ? 40.362 1.921   -4.886  1.00 14.91 ?  73  GLY   A HA3  1 
ATOM   1644 N N    . PRO   A 1 74  ? 37.718 1.881   -5.133  1.00 12.43 ?  74  PRO   A N    1 
ATOM   1645 C CA   . PRO   A 1 74  ? 36.319 1.453   -5.057  1.00 12.36 ?  74  PRO   A CA   1 
ATOM   1646 C C    . PRO   A 1 74  ? 36.168 -0.029  -4.747  1.00 11.92 ?  74  PRO   A C    1 
ATOM   1647 O O    . PRO   A 1 74  ? 37.036 -0.861  -5.033  1.00 12.97 ?  74  PRO   A O    1 
ATOM   1648 C CB   . PRO   A 1 74  ? 35.774 1.768   -6.457  1.00 14.18 ?  74  PRO   A CB   1 
ATOM   1649 C CG   . PRO   A 1 74  ? 36.736 2.745   -7.056  1.00 16.85 ?  74  PRO   A CG   1 
ATOM   1650 C CD   . PRO   A 1 74  ? 38.069 2.395   -6.469  1.00 14.37 ?  74  PRO   A CD   1 
ATOM   1651 H HA   . PRO   A 1 74  ? 35.836 1.979   -4.397  1.00 14.85 ?  74  PRO   A HA   1 
ATOM   1652 H HB2  . PRO   A 1 74  ? 35.736 0.956   -6.984  1.00 17.03 ?  74  PRO   A HB2  1 
ATOM   1653 H HB3  . PRO   A 1 74  ? 34.889 2.168   -6.383  1.00 17.03 ?  74  PRO   A HB3  1 
ATOM   1654 H HG2  . PRO   A 1 74  ? 36.755 2.642   -8.020  1.00 20.23 ?  74  PRO   A HG2  1 
ATOM   1655 H HG3  . PRO   A 1 74  ? 36.488 3.648   -6.812  1.00 20.23 ?  74  PRO   A HG3  1 
ATOM   1656 H HD2  . PRO   A 1 74  ? 38.505 1.702   -6.995  1.00 17.26 ?  74  PRO   A HD2  1 
ATOM   1657 H HD3  . PRO   A 1 74  ? 38.625 3.189   -6.403  1.00 17.26 ?  74  PRO   A HD3  1 
ATOM   1658 N N    . LEU   A 1 75  ? 35.020 -0.352  -4.159  1.00 11.21 ?  75  LEU   A N    1 
ATOM   1659 C CA   . LEU   A 1 75  ? 34.617 -1.740  -4.008  1.00 10.96 ?  75  LEU   A CA   1 
ATOM   1660 C C    . LEU   A 1 75  ? 34.221 -2.314  -5.366  1.00 11.50 ?  75  LEU   A C    1 
ATOM   1661 O O    . LEU   A 1 75  ? 34.108 -1.600  -6.368  1.00 12.92 ?  75  LEU   A O    1 
ATOM   1662 C CB   . LEU   A 1 75  ? 33.429 -1.857  -3.053  1.00 11.12 ?  75  LEU   A CB   1 
ATOM   1663 C CG   . LEU   A 1 75  ? 33.655 -1.447  -1.601  1.00 12.95 ?  75  LEU   A CG   1 
ATOM   1664 C CD1  . LEU   A 1 75  ? 32.370 -1.615  -0.793  1.00 14.94 ?  75  LEU   A CD1  1 
ATOM   1665 C CD2  . LEU   A 1 75  ? 34.795 -2.189  -0.957  1.00 16.35 ?  75  LEU   A CD2  1 
ATOM   1666 H H    . LEU   A 1 75  ? 34.457 0.219   -3.845  1.00 13.46 ?  75  LEU   A H    1 
ATOM   1667 H HA   . LEU   A 1 75  ? 35.355 -2.254  -3.661  1.00 13.17 ?  75  LEU   A HA   1 
ATOM   1668 H HB2  . LEU   A 1 75  ? 32.709 -1.303  -3.398  1.00 13.36 ?  75  LEU   A HB2  1 
ATOM   1669 H HB3  . LEU   A 1 75  ? 33.140 -2.783  -3.050  1.00 13.36 ?  75  LEU   A HB3  1 
ATOM   1670 H HG   . LEU   A 1 75  ? 33.887 -0.505  -1.587  1.00 15.55 ?  75  LEU   A HG   1 
ATOM   1671 H HD11 . LEU   A 1 75  ? 32.539 -1.346  0.124   1.00 17.94 ?  75  LEU   A HD11 1 
ATOM   1672 H HD12 . LEU   A 1 75  ? 31.682 -1.050  -1.180  1.00 17.94 ?  75  LEU   A HD12 1 
ATOM   1673 H HD13 . LEU   A 1 75  ? 32.096 -2.542  -0.823  1.00 17.94 ?  75  LEU   A HD13 1 
ATOM   1674 H HD21 . LEU   A 1 75  ? 34.846 -1.941  -0.022  1.00 19.63 ?  75  LEU   A HD21 1 
ATOM   1675 H HD22 . LEU   A 1 75  ? 34.642 -3.143  -1.041  1.00 19.63 ?  75  LEU   A HD22 1 
ATOM   1676 H HD23 . LEU   A 1 75  ? 35.625 -1.950  -1.406  1.00 19.63 ?  75  LEU   A HD23 1 
ATOM   1677 N N    . LYS   A 1 76  ? 34.023 -3.631  -5.384  1.00 12.19 ?  76  LYS   A N    1 
ATOM   1678 C CA   . LYS   A 1 76  ? 33.415 -4.345  -6.502  1.00 12.59 ?  76  LYS   A CA   1 
ATOM   1679 C C    . LYS   A 1 76  ? 31.905 -4.423  -6.294  1.00 11.33 ?  76  LYS   A C    1 
ATOM   1680 O O    . LYS   A 1 76  ? 31.436 -4.554  -5.167  1.00 11.36 ?  76  LYS   A O    1 
ATOM   1681 C CB   . LYS   A 1 76  ? 33.955 -5.788  -6.558  1.00 14.36 ?  76  LYS   A CB   1 
ATOM   1682 C CG   . LYS   A 1 76  ? 35.462 -5.905  -6.746  1.00 16.33 ?  76  LYS   A CG   1 
ATOM   1683 C CD   . LYS   A 1 76  ? 35.977 -7.314  -6.560  1.00 17.62 ?  76  LYS   A CD   1 
ATOM   1684 C CE   . LYS   A 1 76  ? 37.473 -7.360  -6.756  1.00 20.43 ?  76  LYS   A CE   1 
ATOM   1685 N NZ   . LYS   A 1 76  ? 38.000 -8.717  -6.556  1.00 21.55 ?  76  LYS   A NZ   1 
ATOM   1686 H H    . LYS   A 1 76  ? 34.245 -4.150  -4.736  1.00 14.64 ?  76  LYS   A H    1 
ATOM   1687 H HA   . LYS   A 1 76  ? 33.609 -3.894  -7.341  1.00 15.12 ?  76  LYS   A HA   1 
ATOM   1688 H HB2  . LYS   A 1 76  ? 33.727 -6.233  -5.728  1.00 17.25 ?  76  LYS   A HB2  1 
ATOM   1689 H HB3  . LYS   A 1 76  ? 33.530 -6.245  -7.302  1.00 17.25 ?  76  LYS   A HB3  1 
ATOM   1690 H HG2  . LYS   A 1 76  ? 35.691 -5.616  -7.645  1.00 19.61 ?  76  LYS   A HG2  1 
ATOM   1691 H HG3  . LYS   A 1 76  ? 35.907 -5.335  -6.096  1.00 19.61 ?  76  LYS   A HG3  1 
ATOM   1692 H HD2  . LYS   A 1 76  ? 35.773 -7.619  -5.662  1.00 21.16 ?  76  LYS   A HD2  1 
ATOM   1693 H HD3  . LYS   A 1 76  ? 35.562 -7.899  -7.217  1.00 21.16 ?  76  LYS   A HD3  1 
ATOM   1694 H HE2  . LYS   A 1 76  ? 37.686 -7.077  -7.659  1.00 24.53 ?  76  LYS   A HE2  1 
ATOM   1695 H HE3  . LYS   A 1 76  ? 37.896 -6.771  -6.111  1.00 24.53 ?  76  LYS   A HE3  1 
ATOM   1696 H HZ1  . LYS   A 1 76  ? 38.880 -8.729  -6.676  1.00 25.88 ?  76  LYS   A HZ1  1 
ATOM   1697 H HZ2  . LYS   A 1 76  ? 37.815 -9.002  -5.732  1.00 25.88 ?  76  LYS   A HZ2  1 
ATOM   1698 H HZ3  . LYS   A 1 76  ? 37.624 -9.281  -7.141  1.00 25.88 ?  76  LYS   A HZ3  1 
ATOM   1699 N N    . VAL   A 1 77  ? 31.142 -4.383  -7.391  1.00 11.42 ?  77  VAL   A N    1 
ATOM   1700 C CA   . VAL   A 1 77  ? 29.736 -4.773  -7.302  1.00 11.41 ?  77  VAL   A CA   1 
ATOM   1701 C C    . VAL   A 1 77  ? 29.677 -6.226  -6.858  1.00 10.97 ?  77  VAL   A C    1 
ATOM   1702 O O    . VAL   A 1 77  ? 30.342 -7.095  -7.437  1.00 11.53 ?  77  VAL   A O    1 
ATOM   1703 C CB   . VAL   A 1 77  ? 29.006 -4.552  -8.636  1.00 12.80 ?  77  VAL   A CB   1 
ATOM   1704 C CG1  . VAL   A 1 77  ? 27.549 -4.996  -8.518  1.00 13.46 ?  77  VAL   A CG1  1 
ATOM   1705 C CG2  . VAL   A 1 77  ? 29.081 -3.095  -9.053  1.00 14.27 ?  77  VAL   A CG2  1 
ATOM   1706 H H    . VAL   A 1 77  ? 31.416 -4.132  -8.168  1.00 13.72 ?  77  VAL   A H    1 
ATOM   1707 H HA   . VAL   A 1 77  ? 29.306 -4.229  -6.625  1.00 13.71 ?  77  VAL   A HA   1 
ATOM   1708 H HB   . VAL   A 1 77  ? 29.437 -5.085  -9.323  1.00 15.37 ?  77  VAL   A HB   1 
ATOM   1709 H HG11 . VAL   A 1 77  ? 27.067 -4.698  -9.300  1.00 16.17 ?  77  VAL   A HG11 1 
ATOM   1710 H HG12 . VAL   A 1 77  ? 27.518 -5.965  -8.456  1.00 16.17 ?  77  VAL   A HG12 1 
ATOM   1711 H HG13 . VAL   A 1 77  ? 27.165 -4.603  -7.718  1.00 16.17 ?  77  VAL   A HG13 1 
ATOM   1712 H HG21 . VAL   A 1 77  ? 28.572 -2.978  -9.867  1.00 17.14 ?  77  VAL   A HG21 1 
ATOM   1713 H HG22 . VAL   A 1 77  ? 28.708 -2.548  -8.344  1.00 17.14 ?  77  VAL   A HG22 1 
ATOM   1714 H HG23 . VAL   A 1 77  ? 30.009 -2.855  -9.202  1.00 17.14 ?  77  VAL   A HG23 1 
ATOM   1715 N N    . GLY   A 1 78  ? 28.890 -6.497  -5.812  1.00 11.00 ?  78  GLY   A N    1 
ATOM   1716 C CA   . GLY   A 1 78  ? 28.869 -7.788  -5.154  1.00 11.13 ?  78  GLY   A CA   1 
ATOM   1717 C C    . GLY   A 1 78  ? 29.797 -7.888  -3.963  1.00 10.55 ?  78  GLY   A C    1 
ATOM   1718 O O    . GLY   A 1 78  ? 29.747 -8.896  -3.239  1.00 11.18 ?  78  GLY   A O    1 
ATOM   1719 H H    . GLY   A 1 78  ? 28.339 -5.923  -5.473  1.00 13.21 ?  78  GLY   A H    1 
ATOM   1720 H HA2  . GLY   A 1 78  ? 27.967 -7.969  -4.856  1.00 13.37 ?  78  GLY   A HA2  1 
ATOM   1721 H HA3  . GLY   A 1 78  ? 29.121 -8.467  -5.798  1.00 13.37 ?  78  GLY   A HA3  1 
ATOM   1722 N N    . GLY   A 1 79  ? 30.654 -6.888  -3.749  1.00 10.54 ?  79  GLY   A N    1 
ATOM   1723 C CA   . GLY   A 1 79  ? 31.622 -6.908  -2.678  1.00 10.92 ?  79  GLY   A CA   1 
ATOM   1724 C C    . GLY   A 1 79  ? 31.180 -6.113  -1.462  1.00 10.39 ?  79  GLY   A C    1 
ATOM   1725 O O    . GLY   A 1 79  ? 30.058 -5.605  -1.376  1.00 11.03 ?  79  GLY   A O    1 
ATOM   1726 H H    . GLY   A 1 79  ? 30.694 -6.168  -4.227  1.00 12.67 ?  79  GLY   A H    1 
ATOM   1727 H HA2  . GLY   A 1 79  ? 31.778 -7.833  -2.409  1.00 13.12 ?  79  GLY   A HA2  1 
ATOM   1728 H HA3  . GLY   A 1 79  ? 32.462 -6.543  -2.993  1.00 13.12 ?  79  GLY   A HA3  1 
ATOM   1729 N N    . SER   A 1 80  ? 32.094 -6.020  -0.497  1.00 11.13 ?  80  SER   A N    1 
ATOM   1730 C CA   . SER   A 1 80  ? 31.787 -5.394  0.777   1.00 10.59 ?  80  SER   A CA   1 
ATOM   1731 C C    . SER   A 1 80  ? 33.064 -4.954  1.471   1.00 10.84 ?  80  SER   A C    1 
ATOM   1732 O O    . SER   A 1 80  ? 34.174 -5.379  1.129   1.00 12.13 ?  80  SER   A O    1 
ATOM   1733 C CB   . SER   A 1 80  ? 31.032 -6.359  1.698   1.00 11.75 ?  80  SER   A CB   1 
ATOM   1734 O OG   . SER   A 1 80  ? 31.872 -7.406  2.166   1.00 13.67 ?  80  SER   A OG   1 
ATOM   1735 H H    . SER   A 1 80  ? 32.907 -6.300  -0.566  1.00 13.37 ?  80  SER   A H    1 
ATOM   1736 H HA   . SER   A 1 80  ? 31.239 -4.611  0.613   1.00 12.72 ?  80  SER   A HA   1 
ATOM   1737 H HB2  . SER   A 1 80  ? 30.692 -5.865  2.458   1.00 14.12 ?  80  SER   A HB2  1 
ATOM   1738 H HB3  . SER   A 1 80  ? 30.292 -6.747  1.201   1.00 14.12 ?  80  SER   A HB3  1 
ATOM   1739 H HG   . SER   A 1 80  ? 32.170 -7.841  1.509   1.00 16.42 ?  80  SER   A HG   1 
ATOM   1740 N N    . CYS   A 1 81  ? 32.882 -4.108  2.482   1.00 10.44 ?  81  CYS   A N    1 
ATOM   1741 C CA   . CYS   A 1 81  ? 33.938 -3.824  3.438   1.00 10.77 ?  81  CYS   A CA   1 
ATOM   1742 C C    . CYS   A 1 81  ? 33.303 -3.588  4.797   1.00 10.36 ?  81  CYS   A C    1 
ATOM   1743 O O    . CYS   A 1 81  ? 32.138 -3.192  4.892   1.00 11.57 ?  81  CYS   A O    1 
ATOM   1744 C CB   . CYS   A 1 81  ? 34.810 -2.631  3.021   1.00 11.61 ?  81  CYS   A CB   1 
ATOM   1745 S SG   . CYS   A 1 81  ? 33.925 -1.058  3.042   1.00 11.61 ?  81  CYS   A SG   1 
ATOM   1746 H H    . CYS   A 1 81  ? 32.146 -3.686  2.638   1.00 12.55 ?  81  CYS   A H    1 
ATOM   1747 H HA   . CYS   A 1 81  ? 34.514 -4.600  3.505   1.00 12.94 ?  81  CYS   A HA   1 
ATOM   1748 H HB2  . CYS   A 1 81  ? 35.562 -2.564  3.634   1.00 13.94 ?  81  CYS   A HB2  1 
ATOM   1749 H HB3  . CYS   A 1 81  ? 35.141 -2.783  2.119   1.00 13.94 ?  81  CYS   A HB3  1 
ATOM   1750 H HG   . CYS   A 1 81  ? 34.679 -0.184  2.705   1.00 13.95 ?  81  CYS   A HG   1 
ATOM   1751 N N    . VAL   A 1 82  ? 34.074 -3.855  5.846   1.00 10.72 ?  82  VAL   A N    1 
ATOM   1752 C CA   . VAL   A 1 82  ? 33.656 -3.613  7.220   1.00 11.41 ?  82  VAL   A CA   1 
ATOM   1753 C C    . VAL   A 1 82  ? 34.266 -2.302  7.690   1.00 11.58 ?  82  VAL   A C    1 
ATOM   1754 O O    . VAL   A 1 82  ? 35.493 -2.136  7.668   1.00 12.49 ?  82  VAL   A O    1 
ATOM   1755 C CB   . VAL   A 1 82  ? 34.087 -4.754  8.153   1.00 12.94 ?  82  VAL   A CB   1 
ATOM   1756 C CG1  . VAL   A 1 82  ? 33.629 -4.461  9.574   1.00 14.32 ?  82  VAL   A CG1  1 
ATOM   1757 C CG2  . VAL   A 1 82  ? 33.539 -6.085  7.674   1.00 13.91 ?  82  VAL   A CG2  1 
ATOM   1758 H H    . VAL   A 1 82  ? 34.870 -4.192  5.782   1.00 12.87 ?  82  VAL   A H    1 
ATOM   1759 H HA   . VAL   A 1 82  ? 32.691 -3.535  7.251   1.00 13.70 ?  82  VAL   A HA   1 
ATOM   1760 H HB   . VAL   A 1 82  ? 35.055 -4.808  8.158   1.00 15.54 ?  82  VAL   A HB   1 
ATOM   1761 H HG11 . VAL   A 1 82  ? 33.715 -5.268  10.105  1.00 17.20 ?  82  VAL   A HG11 1 
ATOM   1762 H HG12 . VAL   A 1 82  ? 34.179 -3.757  9.951   1.00 17.20 ?  82  VAL   A HG12 1 
ATOM   1763 H HG13 . VAL   A 1 82  ? 32.699 -4.179  9.555   1.00 17.20 ?  82  VAL   A HG13 1 
ATOM   1764 H HG21 . VAL   A 1 82  ? 33.791 -6.773  8.310   1.00 16.71 ?  82  VAL   A HG21 1 
ATOM   1765 H HG22 . VAL   A 1 82  ? 32.575 -6.025  7.613   1.00 16.71 ?  82  VAL   A HG22 1 
ATOM   1766 H HG23 . VAL   A 1 82  ? 33.917 -6.285  6.804   1.00 16.71 ?  82  VAL   A HG23 1 
ATOM   1767 N N    . LEU   A 1 83  ? 33.414 -1.380  8.126   1.00 10.91 ?  83  LEU   A N    1 
ATOM   1768 C CA   . LEU   A 1 83  ? 33.839 -0.119  8.714   1.00 11.06 ?  83  LEU   A CA   1 
ATOM   1769 C C    . LEU   A 1 83  ? 33.137 0.055   10.056  1.00 11.20 ?  83  LEU   A C    1 
ATOM   1770 O O    . LEU   A 1 83  ? 32.419 -0.833  10.528  1.00 11.94 ?  83  LEU   A O    1 
ATOM   1771 C CB   . LEU   A 1 83  ? 33.595 1.045   7.741   1.00 11.71 ?  83  LEU   A CB   1 
ATOM   1772 C CG   . LEU   A 1 83  ? 34.482 1.044   6.489   1.00 12.60 ?  83  LEU   A CG   1 
ATOM   1773 C CD1  . LEU   A 1 83  ? 34.040 2.108   5.499   1.00 13.25 ?  83  LEU   A CD1  1 
ATOM   1774 C CD2  . LEU   A 1 83  ? 35.954 1.242   6.853   1.00 13.21 ?  83  LEU   A CD2  1 
ATOM   1775 H H    . LEU   A 1 83  ? 32.558 -1.467  8.080   1.00 13.10 ?  83  LEU   A H    1 
ATOM   1776 H HA   . LEU   A 1 83  ? 34.791 -0.159  8.880   1.00 13.29 ?  83  LEU   A HA   1 
ATOM   1777 H HB2  . LEU   A 1 83  ? 32.675 1.019   7.438   1.00 14.07 ?  83  LEU   A HB2  1 
ATOM   1778 H HB3  . LEU   A 1 83  ? 33.759 1.881   8.207   1.00 14.07 ?  83  LEU   A HB3  1 
ATOM   1779 H HG   . LEU   A 1 83  ? 34.405 0.186   6.050   1.00 15.13 ?  83  LEU   A HG   1 
ATOM   1780 H HD11 . LEU   A 1 83  ? 34.621 2.076   4.719   1.00 15.91 ?  83  LEU   A HD11 1 
ATOM   1781 H HD12 . LEU   A 1 83  ? 33.126 1.932   5.235   1.00 15.91 ?  83  LEU   A HD12 1 
ATOM   1782 H HD13 . LEU   A 1 83  ? 34.105 2.980   5.919   1.00 15.91 ?  83  LEU   A HD13 1 
ATOM   1783 H HD21 . LEU   A 1 83  ? 36.469 1.389   6.039   1.00 15.87 ?  83  LEU   A HD21 1 
ATOM   1784 H HD22 . LEU   A 1 83  ? 36.039 2.017   7.434   1.00 15.87 ?  83  LEU   A HD22 1 
ATOM   1785 H HD23 . LEU   A 1 83  ? 36.281 0.452   7.309   1.00 15.87 ?  83  LEU   A HD23 1 
ATOM   1786 N N    . SER   A 1 84  ? 33.360 1.202   10.689  1.00 11.77 ?  84  SER   A N    1 
ATOM   1787 C CA   . SER   A 1 84  ? 32.723 1.457   11.971  1.00 12.09 ?  84  SER   A CA   1 
ATOM   1788 C C    . SER   A 1 84  ? 31.205 1.536   11.830  1.00 11.80 ?  84  SER   A C    1 
ATOM   1789 O O    . SER   A 1 84  ? 30.672 1.996   10.822  1.00 12.11 ?  84  SER   A O    1 
ATOM   1790 C CB   . SER   A 1 84  ? 33.223 2.777   12.545  1.00 13.36 ?  84  SER   A CB   1 
ATOM   1791 O OG   . SER   A 1 84  ? 32.584 3.053   13.778  1.00 14.22 ?  84  SER   A OG   1 
ATOM   1792 H H    . SER   A 1 84  ? 33.866 1.841   10.392  1.00 14.14 ?  84  SER   A H    1 
ATOM   1793 H HA   . SER   A 1 84  ? 32.947 0.743   12.581  1.00 14.52 ?  84  SER   A HA   1 
ATOM   1794 H HB2  . SER   A 1 84  ? 34.183 2.716   12.685  1.00 16.04 ?  84  SER   A HB2  1 
ATOM   1795 H HB3  . SER   A 1 84  ? 33.029 3.491   11.913  1.00 16.04 ?  84  SER   A HB3  1 
ATOM   1796 H HG   . SER   A 1 84  ? 32.865 3.779   14.086  1.00 17.07 ?  84  SER   A HG   1 
ATOM   1797 N N    . GLY   A 1 85  ? 30.507 1.116   12.879  1.00 12.37 ?  85  GLY   A N    1 
ATOM   1798 C CA   . GLY   A 1 85  ? 29.086 1.351   12.982  1.00 13.24 ?  85  GLY   A CA   1 
ATOM   1799 C C    . GLY   A 1 85  ? 28.718 2.662   13.633  1.00 12.73 ?  85  GLY   A C    1 
ATOM   1800 O O    . GLY   A 1 85  ? 27.528 2.972   13.752  1.00 13.34 ?  85  GLY   A O    1 
ATOM   1801 H H    . GLY   A 1 85  ? 30.846 0.683   13.541  1.00 14.86 ?  85  GLY   A H    1 
ATOM   1802 H HA2  . GLY   A 1 85  ? 28.701 1.337   12.093  1.00 15.90 ?  85  GLY   A HA2  1 
ATOM   1803 H HA3  . GLY   A 1 85  ? 28.688 0.638   13.497  1.00 15.90 ?  85  GLY   A HA3  1 
ATOM   1804 N N    . HIS   A 1 86  ? 29.703 3.440   14.071  1.00 12.38 ?  86  HIS   A N    1 
ATOM   1805 C CA   . HIS   A 1 86  ? 29.472 4.775   14.641  1.00 13.06 ?  86  HIS   A CA   1 
ATOM   1806 C C    . HIS   A 1 86  ? 28.491 4.643   15.798  1.00 13.90 ?  86  HIS   A C    1 
ATOM   1807 O O    . HIS   A 1 86  ? 28.679 3.760   16.652  1.00 14.87 ?  86  HIS   A O    1 
ATOM   1808 C CB   . HIS   A 1 86  ? 29.082 5.755   13.541  1.00 13.47 ?  86  HIS   A CB   1 
ATOM   1809 C CG   . HIS   A 1 86  ? 30.123 5.858   12.488  1.00 13.35 ?  86  HIS   A CG   1 
ATOM   1810 N ND1  . HIS   A 1 86  ? 31.209 6.698   12.604  1.00 14.35 ?  86  HIS   A ND1  1 
ATOM   1811 C CD2  . HIS   A 1 86  ? 30.292 5.170   11.338  1.00 13.07 ?  86  HIS   A CD2  1 
ATOM   1812 C CE1  . HIS   A 1 86  ? 31.991 6.536   11.552  1.00 14.30 ?  86  HIS   A CE1  1 
ATOM   1813 N NE2  . HIS   A 1 86  ? 31.463 5.608   10.775  1.00 13.58 ?  86  HIS   A NE2  1 
ATOM   1814 H H    . HIS   A 1 86  ? 30.531 3.217   14.067  1.00 14.87 ?  86  HIS   A H    1 
ATOM   1815 H HA   . HIS   A 1 86  ? 30.307 5.094   15.018  1.00 15.69 ?  86  HIS   A HA   1 
ATOM   1816 H HB2  . HIS   A 1 86  ? 28.256 5.463   13.125  1.00 16.18 ?  86  HIS   A HB2  1 
ATOM   1817 H HB3  . HIS   A 1 86  ? 28.960 6.642   13.927  1.00 16.18 ?  86  HIS   A HB3  1 
ATOM   1818 H HD2  . HIS   A 1 86  ? 29.730 4.505   10.998  1.00 15.70 ?  86  HIS   A HD2  1 
ATOM   1819 H HE1  . HIS   A 1 86  ? 32.778 7.000   11.375  1.00 17.17 ?  86  HIS   A HE1  1 
ATOM   1820 H HE2  . HIS   A 1 86  ? 31.790 5.334   10.022  1.00 16.31 ?  86  HIS   A HE2  1 
ATOM   1821 N N    . ASN   A 1 87  ? 27.468 5.484   15.873  1.00 14.63 ?  87  ASN   A N    1 
ATOM   1822 C CA   . ASN   A 1 87  ? 26.483 5.464   16.937  1.00 15.88 ?  87  ASN   A CA   1 
ATOM   1823 C C    . ASN   A 1 87  ? 25.358 4.477   16.680  1.00 16.72 ?  87  ASN   A C    1 
ATOM   1824 O O    . ASN   A 1 87  ? 24.417 4.420   17.476  1.00 19.27 ?  87  ASN   A O    1 
ATOM   1825 C CB   . ASN   A 1 87  ? 25.885 6.865   17.115  1.00 16.72 ?  87  ASN   A CB   1 
ATOM   1826 C CG   . ASN   A 1 87  ? 25.372 7.459   15.809  1.00 17.55 ?  87  ASN   A CG   1 
ATOM   1827 O OD1  . ASN   A 1 87  ? 26.009 7.345   14.764  1.00 18.26 ?  87  ASN   A OD1  1 
ATOM   1828 N ND2  . ASN   A 1 87  ? 24.220 8.099   15.868  1.00 18.50 ?  87  ASN   A ND2  1 
ATOM   1829 H H    . ASN   A 1 87  ? 27.314 6.091   15.292  1.00 17.57 ?  87  ASN   A H    1 
ATOM   1830 H HA   . ASN   A 1 87  ? 26.912 5.214   17.773  1.00 19.06 ?  87  ASN   A HA   1 
ATOM   1831 H HB2  . ASN   A 1 87  ? 25.137 6.811   17.742  1.00 20.08 ?  87  ASN   A HB2  1 
ATOM   1832 H HB3  . ASN   A 1 87  ? 26.566 7.453   17.473  1.00 20.08 ?  87  ASN   A HB3  1 
ATOM   1833 H HD21 . ASN   A 1 87  ? 23.892 8.450   15.158  1.00 22.21 ?  87  ASN   A HD21 1 
ATOM   1834 H HD22 . ASN   A 1 87  ? 23.799 8.164   16.617  1.00 22.21 ?  87  ASN   A HD22 1 
ATOM   1835 N N    . LEU   A 1 88  ? 25.433 3.691   15.609  1.00 15.82 ?  88  LEU   A N    1 
ATOM   1836 C CA   . LEU   A 1 88  ? 24.336 2.814   15.215  1.00 16.09 ?  88  LEU   A CA   1 
ATOM   1837 C C    . LEU   A 1 88  ? 24.567 1.342   15.516  1.00 15.54 ?  88  LEU   A C    1 
ATOM   1838 O O    . LEU   A 1 88  ? 23.595 0.605   15.689  1.00 16.92 ?  88  LEU   A O    1 
ATOM   1839 C CB   . LEU   A 1 88  ? 24.070 2.962   13.713  1.00 17.22 ?  88  LEU   A CB   1 
ATOM   1840 C CG   . LEU   A 1 88  ? 23.779 4.380   13.216  1.00 18.96 ?  88  LEU   A CG   1 
ATOM   1841 C CD1  . LEU   A 1 88  ? 23.595 4.388   11.707  1.00 19.24 ?  88  LEU   A CD1  1 
ATOM   1842 C CD2  . LEU   A 1 88  ? 22.551 4.960   13.909  1.00 20.71 ?  88  LEU   A CD2  1 
ATOM   1843 H H    . LEU   A 1 88  ? 26.121 3.648   15.091  1.00 19.00 ?  88  LEU   A H    1 
ATOM   1844 H HA   . LEU   A 1 88  ? 23.538 3.088   15.689  1.00 19.33 ?  88  LEU   A HA   1 
ATOM   1845 H HB2  . LEU   A 1 88  ? 24.846 2.646   13.230  1.00 20.67 ?  88  LEU   A HB2  1 
ATOM   1846 H HB3  . LEU   A 1 88  ? 23.301 2.418   13.486  1.00 20.67 ?  88  LEU   A HB3  1 
ATOM   1847 H HG   . LEU   A 1 88  ? 24.533 4.950   13.423  1.00 22.77 ?  88  LEU   A HG   1 
ATOM   1848 H HD11 . LEU   A 1 88  ? 23.499 5.306   11.402  1.00 23.10 ?  88  LEU   A HD11 1 
ATOM   1849 H HD12 . LEU   A 1 88  ? 24.371 3.982   11.290  1.00 23.10 ?  88  LEU   A HD12 1 
ATOM   1850 H HD13 . LEU   A 1 88  ? 22.797 3.883   11.483  1.00 23.10 ?  88  LEU   A HD13 1 
ATOM   1851 H HD21 . LEU   A 1 88  ? 22.332 5.813   13.502  1.00 24.87 ?  88  LEU   A HD21 1 
ATOM   1852 H HD22 . LEU   A 1 88  ? 21.810 4.343   13.807  1.00 24.87 ?  88  LEU   A HD22 1 
ATOM   1853 H HD23 . LEU   A 1 88  ? 22.752 5.084   14.850  1.00 24.87 ?  88  LEU   A HD23 1 
ATOM   1854 N N    . ALA   A 1 89  ? 25.819 0.900   15.575  1.00 14.51 ?  89  ALA   A N    1 
ATOM   1855 C CA   . ALA   A 1 89  ? 26.166 -0.513  15.664  1.00 14.48 ?  89  ALA   A CA   1 
ATOM   1856 C C    . ALA   A 1 89  ? 27.653 -0.578  15.973  1.00 14.81 ?  89  ALA   A C    1 
ATOM   1857 O O    . ALA   A 1 89  ? 28.359 0.425   15.870  1.00 15.49 ?  89  ALA   A O    1 
ATOM   1858 C CB   . ALA   A 1 89  ? 25.872 -1.221  14.342  1.00 14.04 ?  89  ALA   A CB   1 
ATOM   1859 H H    . ALA   A 1 89  ? 26.509 1.416   15.556  1.00 17.43 ?  89  ALA   A H    1 
ATOM   1860 H HA   . ALA   A 1 89  ? 25.668 -0.938  16.381  1.00 17.39 ?  89  ALA   A HA   1 
ATOM   1861 H HB1  . ALA   A 1 89  ? 26.133 -2.154  14.419  1.00 16.86 ?  89  ALA   A HB1  1 
ATOM   1862 H HB2  . ALA   A 1 89  ? 24.920 -1.162  14.156  1.00 16.86 ?  89  ALA   A HB2  1 
ATOM   1863 H HB3  . ALA   A 1 89  ? 26.376 -0.795  13.635  1.00 16.86 ?  89  ALA   A HB3  1 
ATOM   1864 N N    . LYS   A 1 90  ? 28.137 -1.764  16.343  1.00 15.40 ?  90  LYS   A N    1 
ATOM   1865 C CA   . LYS   A 1 90  ? 29.582 -1.917  16.477  1.00 16.55 ?  90  LYS   A CA   1 
ATOM   1866 C C    . LYS   A 1 90  ? 30.266 -1.714  15.127  1.00 15.19 ?  90  LYS   A C    1 
ATOM   1867 O O    . LYS   A 1 90  ? 31.190 -0.897  14.996  1.00 16.25 ?  90  LYS   A O    1 
ATOM   1868 C CB   . LYS   A 1 90  ? 29.927 -3.280  17.085  1.00 19.90 ?  90  LYS   A CB   1 
ATOM   1869 C CG   . LYS   A 1 90  ? 31.402 -3.425  17.426  1.00 24.87 ?  90  LYS   A CG   1 
ATOM   1870 C CD   . LYS   A 1 90  ? 31.648 -4.647  18.294  1.00 30.07 ?  90  LYS   A CD   1 
ATOM   1871 C CE   . LYS   A 1 90  ? 33.061 -4.665  18.856  1.00 34.36 ?  90  LYS   A CE   1 
ATOM   1872 N NZ   . LYS   A 1 90  ? 34.081 -5.002  17.827  1.00 36.34 ?  90  LYS   A NZ   1 
ATOM   1873 H H    . LYS   A 1 90  ? 27.672 -2.465  16.512  1.00 18.49 ?  90  LYS   A H    1 
ATOM   1874 H HA   . LYS   A 1 90  ? 29.914 -1.237  17.081  1.00 19.88 ?  90  LYS   A HA   1 
ATOM   1875 H HB2  . LYS   A 1 90  ? 29.418 -3.399  17.906  1.00 23.89 ?  90  LYS   A HB2  1 
ATOM   1876 H HB3  . LYS   A 1 90  ? 29.696 -3.979  16.453  1.00 23.89 ?  90  LYS   A HB3  1 
ATOM   1877 H HG2  . LYS   A 1 90  ? 31.913 -3.524  16.608  1.00 29.85 ?  90  LYS   A HG2  1 
ATOM   1878 H HG3  . LYS   A 1 90  ? 31.698 -2.640  17.915  1.00 29.85 ?  90  LYS   A HG3  1 
ATOM   1879 H HD2  . LYS   A 1 90  ? 31.025 -4.642  19.038  1.00 36.10 ?  90  LYS   A HD2  1 
ATOM   1880 H HD3  . LYS   A 1 90  ? 31.523 -5.448  17.760  1.00 36.10 ?  90  LYS   A HD3  1 
ATOM   1881 H HE2  . LYS   A 1 90  ? 33.272 -3.787  19.211  1.00 41.25 ?  90  LYS   A HE2  1 
ATOM   1882 H HE3  . LYS   A 1 90  ? 33.113 -5.330  19.561  1.00 41.25 ?  90  LYS   A HE3  1 
ATOM   1883 H HZ1  . LYS   A 1 90  ? 33.915 -5.809  17.488  1.00 43.62 ?  90  LYS   A HZ1  1 
ATOM   1884 H HZ2  . LYS   A 1 90  ? 34.060 -4.403  17.170  1.00 43.62 ?  90  LYS   A HZ2  1 
ATOM   1885 H HZ3  . LYS   A 1 90  ? 34.893 -5.004  18.192  1.00 43.62 ?  90  LYS   A HZ3  1 
ATOM   1886 N N    . HIS   A 1 91  ? 29.790 -2.422  14.105  1.00 13.36 ?  91  HIS   A N    1 
ATOM   1887 C CA   . HIS   A 1 91  ? 30.353 -2.387  12.770  1.00 12.91 ?  91  HIS   A CA   1 
ATOM   1888 C C    . HIS   A 1 91  ? 29.254 -2.102  11.764  1.00 11.62 ?  91  HIS   A C    1 
ATOM   1889 O O    . HIS   A 1 91  ? 28.090 -2.461  11.975  1.00 12.27 ?  91  HIS   A O    1 
ATOM   1890 C CB   . HIS   A 1 91  ? 30.952 -3.751  12.392  1.00 15.28 ?  91  HIS   A CB   1 
ATOM   1891 C CG   . HIS   A 1 91  ? 31.947 -4.276  13.379  1.00 19.46 ?  91  HIS   A CG   1 
ATOM   1892 N ND1  . HIS   A 1 91  ? 33.230 -3.783  13.476  1.00 21.42 ?  91  HIS   A ND1  1 
ATOM   1893 C CD2  . HIS   A 1 91  ? 31.854 -5.263  14.302  1.00 21.30 ?  91  HIS   A CD2  1 
ATOM   1894 C CE1  . HIS   A 1 91  ? 33.884 -4.439  14.419  1.00 22.32 ?  91  HIS   A CE1  1 
ATOM   1895 N NE2  . HIS   A 1 91  ? 33.070 -5.343  14.936  1.00 22.49 ?  91  HIS   A NE2  1 
ATOM   1896 H H    . HIS   A 1 91  ? 29.123 -2.969  14.177  1.00 16.04 ?  91  HIS   A H    1 
ATOM   1897 H HA   . HIS   A 1 91  ? 31.039 -1.710  12.708  1.00 15.51 ?  91  HIS   A HA   1 
ATOM   1898 H HB2  . HIS   A 1 91  ? 30.238 -4.405  12.326  1.00 18.35 ?  91  HIS   A HB2  1 
ATOM   1899 H HB3  . HIS   A 1 91  ? 31.404 -3.671  11.538  1.00 18.35 ?  91  HIS   A HB3  1 
ATOM   1900 H HD1  . HIS   A 1 91  ? 33.558 -3.148  12.996  1.00 25.72 ?  91  HIS   A HD1  1 
ATOM   1901 H HD2  . HIS   A 1 91  ? 31.112 -5.789  14.478  1.00 25.58 ?  91  HIS   A HD2  1 
ATOM   1902 H HE1  . HIS   A 1 91  ? 34.768 -4.285  14.677  1.00 26.79 ?  91  HIS   A HE1  1 
ATOM   1903 N N    . CYS   A 1 92  ? 29.645 -1.500  10.645  1.00 11.14 ?  92  CYS   A N    1 
ATOM   1904 C CA   . CYS   A 1 92  ? 28.793 -1.415  9.468   1.00 10.94 ?  92  CYS   A CA   1 
ATOM   1905 C C    . CYS   A 1 92  ? 29.431 -2.236  8.357   1.00 10.52 ?  92  CYS   A C    1 
ATOM   1906 O O    . CYS   A 1 92  ? 30.585 -1.981  7.979   1.00 10.97 ?  92  CYS   A O    1 
ATOM   1907 C CB   . CYS   A 1 92  ? 28.594 0.031   9.014   1.00 11.39 ?  92  CYS   A CB   1 
ATOM   1908 S SG   . CYS   A 1 92  ? 27.552 0.148   7.527   1.00 10.88 ?  92  CYS   A SG   1 
ATOM   1909 H H    . CYS   A 1 92  ? 30.414 -1.123  10.549  1.00 13.38 ?  92  CYS   A H    1 
ATOM   1910 H HA   . CYS   A 1 92  ? 27.926 -1.793  9.675   1.00 13.14 ?  92  CYS   A HA   1 
ATOM   1911 H HB2  . CYS   A 1 92  ? 28.159 0.531   9.723   1.00 13.68 ?  92  CYS   A HB2  1 
ATOM   1912 H HB3  . CYS   A 1 92  ? 29.457 0.423   8.811   1.00 13.68 ?  92  CYS   A HB3  1 
ATOM   1913 H HG   . CYS   A 1 92  ? 27.436 1.302   7.235   1.00 13.07 ?  92  CYS   A HG   1 
ATOM   1914 N N    . LEU   A 1 93  ? 28.685 -3.218  7.852   1.00 10.18 ?  93  LEU   A N    1 
ATOM   1915 C CA   . LEU   A 1 93  ? 29.076 -3.971  6.667   1.00 9.90  ?  93  LEU   A CA   1 
ATOM   1916 C C    . LEU   A 1 93  ? 28.477 -3.266  5.457   1.00 9.53  ?  93  LEU   A C    1 
ATOM   1917 O O    . LEU   A 1 93  ? 27.261 -3.318  5.238   1.00 9.84  ?  93  LEU   A O    1 
ATOM   1918 C CB   . LEU   A 1 93  ? 28.590 -5.415  6.772   1.00 10.42 ?  93  LEU   A CB   1 
ATOM   1919 C CG   . LEU   A 1 93  ? 28.972 -6.313  5.598   1.00 10.70 ?  93  LEU   A CG   1 
ATOM   1920 C CD1  . LEU   A 1 93  ? 30.475 -6.565  5.586   1.00 11.84 ?  93  LEU   A CD1  1 
ATOM   1921 C CD2  . LEU   A 1 93  ? 28.198 -7.633  5.627   1.00 11.35 ?  93  LEU   A CD2  1 
ATOM   1922 H H    . LEU   A 1 93  ? 27.933 -3.463  8.193   1.00 12.24 ?  93  LEU   A H    1 
ATOM   1923 H HA   . LEU   A 1 93  ? 30.038 -3.965  6.588   1.00 11.90 ?  93  LEU   A HA   1 
ATOM   1924 H HB2  . LEU   A 1 93  ? 28.967 -5.805  7.579   1.00 12.52 ?  93  LEU   A HB2  1 
ATOM   1925 H HB3  . LEU   A 1 93  ? 27.623 -5.411  6.837   1.00 12.52 ?  93  LEU   A HB3  1 
ATOM   1926 H HG   . LEU   A 1 93  ? 28.750 -5.864  4.774   1.00 12.85 ?  93  LEU   A HG   1 
ATOM   1927 H HD11 . LEU   A 1 93  ? 30.694 -7.190  4.878   1.00 14.22 ?  93  LEU   A HD11 1 
ATOM   1928 H HD12 . LEU   A 1 93  ? 30.942 -5.726  5.442   1.00 14.22 ?  93  LEU   A HD12 1 
ATOM   1929 H HD13 . LEU   A 1 93  ? 30.746 -6.942  6.446   1.00 14.22 ?  93  LEU   A HD13 1 
ATOM   1930 H HD21 . LEU   A 1 93  ? 28.475 -8.175  4.866   1.00 13.63 ?  93  LEU   A HD21 1 
ATOM   1931 H HD22 . LEU   A 1 93  ? 28.399 -8.103  6.451   1.00 13.63 ?  93  LEU   A HD22 1 
ATOM   1932 H HD23 . LEU   A 1 93  ? 27.251 -7.446  5.570   1.00 13.63 ?  93  LEU   A HD23 1 
ATOM   1933 N N    . HIS   A 1 94  ? 29.324 -2.574  4.698   1.00 9.43  ?  94  HIS   A N    1 
ATOM   1934 C CA   . HIS   A 1 94  ? 28.895 -1.894  3.478   1.00 9.44  ?  94  HIS   A CA   1 
ATOM   1935 C C    . HIS   A 1 94  ? 28.898 -2.923  2.365   1.00 9.50  ?  94  HIS   A C    1 
ATOM   1936 O O    . HIS   A 1 94  ? 29.962 -3.438  2.013   1.00 11.06 ?  94  HIS   A O    1 
ATOM   1937 C CB   . HIS   A 1 94  ? 29.857 -0.756  3.144   1.00 9.75  ?  94  HIS   A CB   1 
ATOM   1938 C CG   . HIS   A 1 94  ? 29.853 0.334   4.158   1.00 9.82  ?  94  HIS   A CG   1 
ATOM   1939 N ND1  . HIS   A 1 94  ? 28.981 1.401   4.103   1.00 9.86  ?  94  HIS   A ND1  1 
ATOM   1940 C CD2  . HIS   A 1 94  ? 30.592 0.494   5.278   1.00 10.32 ?  94  HIS   A CD2  1 
ATOM   1941 C CE1  . HIS   A 1 94  ? 29.201 2.175   5.150   1.00 10.01 ?  94  HIS   A CE1  1 
ATOM   1942 N NE2  . HIS   A 1 94  ? 30.175 1.652   5.875   1.00 10.48 ?  94  HIS   A NE2  1 
ATOM   1943 H H    . HIS   A 1 94  ? 30.161 -2.483  4.869   1.00 11.33 ?  94  HIS   A H    1 
ATOM   1944 H HA   . HIS   A 1 94  ? 27.994 -1.549  3.585   1.00 11.34 ?  94  HIS   A HA   1 
ATOM   1945 H HB2  . HIS   A 1 94  ? 30.749 -1.112  3.088   1.00 11.72 ?  94  HIS   A HB2  1 
ATOM   1946 H HB3  . HIS   A 1 94  ? 29.590 -0.373  2.293   1.00 11.72 ?  94  HIS   A HB3  1 
ATOM   1947 H HD2  . HIS   A 1 94  ? 31.261 -0.070  5.581   1.00 12.40 ?  94  HIS   A HD2  1 
ATOM   1948 H HE1  . HIS   A 1 94  ? 28.745 2.968   5.345   1.00 12.02 ?  94  HIS   A HE1  1 
ATOM   1949 H HE2  . HIS   A 1 94  ? 30.493 1.989   6.600   1.00 12.59 ?  94  HIS   A HE2  1 
ATOM   1950 N N    . VAL   A 1 95  ? 27.723 -3.243  1.824   1.00 8.90  ?  95  VAL   A N    1 
ATOM   1951 C CA   . VAL   A 1 95  ? 27.571 -4.279  0.803   1.00 9.25  ?  95  VAL   A CA   1 
ATOM   1952 C C    . VAL   A 1 95  ? 27.026 -3.633  -0.458  1.00 8.83  ?  95  VAL   A C    1 
ATOM   1953 O O    . VAL   A 1 95  ? 26.028 -2.905  -0.398  1.00 9.82  ?  95  VAL   A O    1 
ATOM   1954 C CB   . VAL   A 1 95  ? 26.634 -5.420  1.253   1.00 9.86  ?  95  VAL   A CB   1 
ATOM   1955 C CG1  . VAL   A 1 95  ? 26.515 -6.454  0.153   1.00 10.54 ?  95  VAL   A CG1  1 
ATOM   1956 C CG2  . VAL   A 1 95  ? 27.140 -6.044  2.540   1.00 10.37 ?  95  VAL   A CG2  1 
ATOM   1957 H H    . VAL   A 1 95  ? 26.975 -2.867  2.033   1.00 10.70 ?  95  VAL   A H    1 
ATOM   1958 H HA   . VAL   A 1 95  ? 28.433 -4.662  0.595   1.00 11.11 ?  95  VAL   A HA   1 
ATOM   1959 H HB   . VAL   A 1 95  ? 25.751 -5.061  1.423   1.00 11.84 ?  95  VAL   A HB   1 
ATOM   1960 H HG11 . VAL   A 1 95  ? 26.123 -7.266  0.520   1.00 12.67 ?  95  VAL   A HG11 1 
ATOM   1961 H HG12 . VAL   A 1 95  ? 25.946 -6.110  -0.554  1.00 12.67 ?  95  VAL   A HG12 1 
ATOM   1962 H HG13 . VAL   A 1 95  ? 27.398 -6.652  -0.199  1.00 12.67 ?  95  VAL   A HG13 1 
ATOM   1963 H HG21 . VAL   A 1 95  ? 26.577 -6.799  2.769   1.00 12.46 ?  95  VAL   A HG21 1 
ATOM   1964 H HG22 . VAL   A 1 95  ? 28.055 -6.338  2.411   1.00 12.46 ?  95  VAL   A HG22 1 
ATOM   1965 H HG23 . VAL   A 1 95  ? 27.104 -5.378  3.246   1.00 12.46 ?  95  VAL   A HG23 1 
ATOM   1966 N N    . VAL   A 1 96  ? 27.652 -3.917  -1.599  1.00 9.05  ?  96  VAL   A N    1 
ATOM   1967 C CA   . VAL   A 1 96  ? 27.241 -3.357  -2.881  1.00 9.71  ?  96  VAL   A CA   1 
ATOM   1968 C C    . VAL   A 1 96  ? 26.421 -4.395  -3.639  1.00 9.65  ?  96  VAL   A C    1 
ATOM   1969 O O    . VAL   A 1 96  ? 26.966 -5.333  -4.228  1.00 10.74 ?  96  VAL   A O    1 
ATOM   1970 C CB   . VAL   A 1 96  ? 28.434 -2.889  -3.711  1.00 10.25 ?  96  VAL   A CB   1 
ATOM   1971 C CG1  . VAL   A 1 96  ? 27.934 -2.238  -4.984  1.00 10.49 ?  96  VAL   A CG1  1 
ATOM   1972 C CG2  . VAL   A 1 96  ? 29.304 -1.919  -2.911  1.00 10.77 ?  96  VAL   A CG2  1 
ATOM   1973 H H    . VAL   A 1 96  ? 28.345 -4.430  -1.654  1.00 10.88 ?  96  VAL   A H    1 
ATOM   1974 H HA   . VAL   A 1 96  ? 26.676 -2.586  -2.720  1.00 11.66 ?  96  VAL   A HA   1 
ATOM   1975 H HB   . VAL   A 1 96  ? 28.981 -3.649  -3.953  1.00 12.31 ?  96  VAL   A HB   1 
ATOM   1976 H HG11 . VAL   A 1 96  ? 28.680 -1.775  -5.407  1.00 12.60 ?  96  VAL   A HG11 1 
ATOM   1977 H HG12 . VAL   A 1 96  ? 27.595 -2.921  -5.574  1.00 12.60 ?  96  VAL   A HG12 1 
ATOM   1978 H HG13 . VAL   A 1 96  ? 27.241 -1.602  -4.760  1.00 12.60 ?  96  VAL   A HG13 1 
ATOM   1979 H HG21 . VAL   A 1 96  ? 30.009 -1.572  -3.480  1.00 12.94 ?  96  VAL   A HG21 1 
ATOM   1980 H HG22 . VAL   A 1 96  ? 28.751 -1.183  -2.591  1.00 12.94 ?  96  VAL   A HG22 1 
ATOM   1981 H HG23 . VAL   A 1 96  ? 29.692 -2.386  -2.153  1.00 12.94 ?  96  VAL   A HG23 1 
ATOM   1982 N N    . GLY   A 1 97  ? 25.105 -4.234  -3.648  1.00 10.07 ?  97  GLY   A N    1 
ATOM   1983 C CA   . GLY   A 1 97  ? 24.284 -4.994  -4.557  1.00 10.76 ?  97  GLY   A CA   1 
ATOM   1984 C C    . GLY   A 1 97  ? 24.279 -4.331  -5.923  1.00 10.70 ?  97  GLY   A C    1 
ATOM   1985 O O    . GLY   A 1 97  ? 24.561 -3.133  -6.060  1.00 11.65 ?  97  GLY   A O    1 
ATOM   1986 H H    . GLY   A 1 97  ? 24.665 -3.688  -3.138  1.00 12.10 ?  97  GLY   A H    1 
ATOM   1987 H HA2  . GLY   A 1 97  ? 24.639 -5.893  -4.635  1.00 12.93 ?  97  GLY   A HA2  1 
ATOM   1988 H HA3  . GLY   A 1 97  ? 23.375 -5.045  -4.217  1.00 12.93 ?  97  GLY   A HA3  1 
ATOM   1989 N N    . PRO   A 1 98  ? 23.936 -5.084  -6.962  1.00 10.82 ?  98  PRO   A N    1 
ATOM   1990 C CA   . PRO   A 1 98  ? 23.829 -4.474  -8.290  1.00 11.98 ?  98  PRO   A CA   1 
ATOM   1991 C C    . PRO   A 1 98  ? 22.712 -3.439  -8.343  1.00 12.15 ?  98  PRO   A C    1 
ATOM   1992 O O    . PRO   A 1 98  ? 21.636 -3.616  -7.765  1.00 11.97 ?  98  PRO   A O    1 
ATOM   1993 C CB   . PRO   A 1 98  ? 23.526 -5.669  -9.202  1.00 12.52 ?  98  PRO   A CB   1 
ATOM   1994 C CG   . PRO   A 1 98  ? 22.882 -6.682  -8.298  1.00 12.63 ?  98  PRO   A CG   1 
ATOM   1995 C CD   . PRO   A 1 98  ? 23.623 -6.526  -6.989  1.00 11.41 ?  98  PRO   A CD   1 
ATOM   1996 H HA   . PRO   A 1 98  ? 24.672 -4.069  -8.543  1.00 14.39 ?  98  PRO   A HA   1 
ATOM   1997 H HB2  . PRO   A 1 98  ? 22.913 -5.391  -9.901  1.00 15.03 ?  98  PRO   A HB2  1 
ATOM   1998 H HB3  . PRO   A 1 98  ? 24.349 -6.012  -9.574  1.00 15.03 ?  98  PRO   A HB3  1 
ATOM   1999 H HG2  . PRO   A 1 98  ? 21.940 -6.472  -8.186  1.00 15.17 ?  98  PRO   A HG2  1 
ATOM   2000 H HG3  . PRO   A 1 98  ? 23.001 -7.569  -8.661  1.00 15.17 ?  98  PRO   A HG3  1 
ATOM   2001 H HD2  . PRO   A 1 98  ? 23.051 -6.774  -6.243  1.00 13.71 ?  98  PRO   A HD2  1 
ATOM   2002 H HD3  . PRO   A 1 98  ? 24.439 -7.050  -6.998  1.00 13.71 ?  98  PRO   A HD3  1 
ATOM   2003 N N    A ASN   A 1 99  ? 22.988 -2.329  -9.029  0.78 13.15 ?  99  ASN   A N    1 
ATOM   2004 N N    B ASN   A 1 99  ? 22.972 -2.368  -9.080  0.22 13.18 ?  99  ASN   A N    1 
ATOM   2005 C CA   A ASN   A 1 99  ? 22.019 -1.248  -9.231  0.78 14.18 ?  99  ASN   A CA   1 
ATOM   2006 C CA   B ASN   A 1 99  ? 21.974 -1.349  -9.366  0.22 14.29 ?  99  ASN   A CA   1 
ATOM   2007 C C    A ASN   A 1 99  ? 21.467 -1.385  -10.648 0.78 15.26 ?  99  ASN   A C    1 
ATOM   2008 C C    B ASN   A 1 99  ? 21.360 -1.660  -10.725 0.22 15.34 ?  99  ASN   A C    1 
ATOM   2009 O O    A ASN   A 1 99  ? 22.141 -1.056  -11.629 0.78 15.98 ?  99  ASN   A O    1 
ATOM   2010 O O    B ASN   A 1 99  ? 22.071 -1.715  -11.735 0.22 15.06 ?  99  ASN   A O    1 
ATOM   2011 C CB   A ASN   A 1 99  ? 22.661 0.119   -8.996  0.78 14.32 ?  99  ASN   A CB   1 
ATOM   2012 C CB   B ASN   A 1 99  ? 22.618 0.036   -9.363  0.22 14.85 ?  99  ASN   A CB   1 
ATOM   2013 C CG   A ASN   A 1 99  ? 21.646 1.265   -9.011  0.78 15.02 ?  99  ASN   A CG   1 
ATOM   2014 C CG   B ASN   A 1 99  ? 21.597 1.156   -9.307  0.22 15.37 ?  99  ASN   A CG   1 
ATOM   2015 O OD1  A ASN   A 1 99  ? 20.652 1.218   -9.734  0.78 15.95 ?  99  ASN   A OD1  1 
ATOM   2016 O OD1  B ASN   A 1 99  ? 20.570 1.113   -9.985  0.22 15.54 ?  99  ASN   A OD1  1 
ATOM   2017 N ND2  A ASN   A 1 99  ? 21.905 2.299   -8.211  0.78 15.78 ?  99  ASN   A ND2  1 
ATOM   2018 N ND2  B ASN   A 1 99  ? 21.873 2.164   -8.486  0.22 15.74 ?  99  ASN   A ND2  1 
ATOM   2019 H H    A ASN   A 1 99  ? 23.755 -2.168  -9.387  0.78 15.80 ?  99  ASN   A H    1 
ATOM   2020 H H    B ASN   A 1 99  ? 23.741 -2.207  -9.432  0.22 15.83 ?  99  ASN   A H    1 
ATOM   2021 H HA   A ASN   A 1 99  ? 21.290 -1.353  -8.589  0.78 17.03 ?  99  ASN   A HA   1 
ATOM   2022 H HA   B ASN   A 1 99  ? 21.278 -1.371  -8.690  0.22 17.16 ?  99  ASN   A HA   1 
ATOM   2023 H HB2  A ASN   A 1 99  ? 23.106 0.125   -8.133  0.78 17.19 ?  99  ASN   A HB2  1 
ATOM   2024 H HB2  B ASN   A 1 99  ? 23.195 0.115   -8.586  0.22 17.84 ?  99  ASN   A HB2  1 
ATOM   2025 H HB3  A ASN   A 1 99  ? 23.307 0.286   -9.700  0.78 17.19 ?  99  ASN   A HB3  1 
ATOM   2026 H HB3  B ASN   A 1 99  ? 23.142 0.140   -10.170 0.22 17.84 ?  99  ASN   A HB3  1 
ATOM   2027 H HD21 A ASN   A 1 99  ? 21.366 2.969   -8.184  0.78 18.95 ?  99  ASN   A HD21 1 
ATOM   2028 H HD21 B ASN   A 1 99  ? 21.327 2.823   -8.414  0.22 18.90 ?  99  ASN   A HD21 1 
ATOM   2029 H HD22 A ASN   A 1 99  ? 22.614 2.298   -7.723  0.78 18.95 ?  99  ASN   A HD22 1 
ATOM   2030 H HD22 B ASN   A 1 99  ? 22.601 2.156   -8.024  0.22 18.90 ?  99  ASN   A HD22 1 
ATOM   2031 N N    A VAL   A 1 100 ? 20.232 -1.887  -10.739 0.78 15.65 ?  100 VAL   A N    1 
ATOM   2032 N N    B VAL   A 1 100 ? 20.049 -1.896  -10.742 0.22 16.83 ?  100 VAL   A N    1 
ATOM   2033 C CA   A VAL   A 1 100 ? 19.586 -2.094  -12.030 0.78 17.91 ?  100 VAL   A CA   1 
ATOM   2034 C CA   B VAL   A 1 100 ? 19.362 -2.156  -12.002 0.22 18.61 ?  100 VAL   A CA   1 
ATOM   2035 C C    A VAL   A 1 100 ? 19.491 -0.791  -12.809 0.78 18.34 ?  100 VAL   A C    1 
ATOM   2036 C C    B VAL   A 1 100 ? 19.158 -0.865  -12.790 0.22 19.65 ?  100 VAL   A C    1 
ATOM   2037 O O    A VAL   A 1 100 ? 19.564 -0.791  -14.042 0.78 19.48 ?  100 VAL   A O    1 
ATOM   2038 O O    B VAL   A 1 100 ? 19.135 -0.886  -14.026 0.22 19.97 ?  100 VAL   A O    1 
ATOM   2039 C CB   A VAL   A 1 100 ? 18.209 -2.761  -11.827 0.78 19.65 ?  100 VAL   A CB   1 
ATOM   2040 C CB   B VAL   A 1 100 ? 18.040 -2.902  -11.749 0.22 19.36 ?  100 VAL   A CB   1 
ATOM   2041 C CG1  A VAL   A 1 100 ? 17.474 -2.911  -13.152 0.78 20.45 ?  100 VAL   A CG1  1 
ATOM   2042 C CG1  B VAL   A 1 100 ? 17.349 -3.242  -13.061 0.22 19.69 ?  100 VAL   A CG1  1 
ATOM   2043 C CG2  A VAL   A 1 100 ? 18.379 -4.113  -11.157 0.78 20.69 ?  100 VAL   A CG2  1 
ATOM   2044 C CG2  B VAL   A 1 100 ? 18.293 -4.163  -10.937 0.22 19.85 ?  100 VAL   A CG2  1 
ATOM   2045 H H    A VAL   A 1 100 ? 19.746 -2.120  -10.060 0.78 18.80 ?  100 VAL   A H    1 
ATOM   2046 H H    B VAL   A 1 100 ? 19.547 -1.924  -10.045 0.22 20.22 ?  100 VAL   A H    1 
ATOM   2047 H HA   A VAL   A 1 100 ? 20.130 -2.701  -12.548 0.78 21.50 ?  100 VAL   A HA   1 
ATOM   2048 H HA   B VAL   A 1 100 ? 19.920 -2.735  -12.538 0.22 22.34 ?  100 VAL   A HA   1 
ATOM   2049 H HB   A VAL   A 1 100 ? 17.669 -2.204  -11.247 0.78 23.59 ?  100 VAL   A HB   1 
ATOM   2050 H HB   B VAL   A 1 100 ? 17.446 -2.333  -11.242 0.22 23.24 ?  100 VAL   A HB   1 
ATOM   2051 H HG11 A VAL   A 1 100 ? 16.710 -3.496  -13.023 0.78 24.55 ?  100 VAL   A HG11 1 
ATOM   2052 H HG11 B VAL   A 1 100 ? 16.594 -3.823  -12.876 0.22 23.65 ?  100 VAL   A HG11 1 
ATOM   2053 H HG12 A VAL   A 1 100 ? 17.175 -2.039  -13.452 0.78 24.55 ?  100 VAL   A HG12 1 
ATOM   2054 H HG12 B VAL   A 1 100 ? 17.041 -2.423  -13.479 0.22 23.65 ?  100 VAL   A HG12 1 
ATOM   2055 H HG13 A VAL   A 1 100 ? 18.077 -3.299  -13.806 0.78 24.55 ?  100 VAL   A HG13 1 
ATOM   2056 H HG13 B VAL   A 1 100 ? 17.980 -3.695  -13.640 0.22 23.65 ?  100 VAL   A HG13 1 
ATOM   2057 H HG21 A VAL   A 1 100 ? 17.515 -4.551  -11.108 0.78 24.84 ?  100 VAL   A HG21 1 
ATOM   2058 H HG21 B VAL   A 1 100 ? 17.470 -4.674  -10.883 0.22 23.83 ?  100 VAL   A HG21 1 
ATOM   2059 H HG22 A VAL   A 1 100 ? 18.994 -4.650  -11.680 0.78 24.84 ?  100 VAL   A HG22 1 
ATOM   2060 H HG22 B VAL   A 1 100 ? 18.980 -4.688  -11.377 0.22 23.83 ?  100 VAL   A HG22 1 
ATOM   2061 H HG23 A VAL   A 1 100 ? 18.733 -3.981  -10.263 0.78 24.84 ?  100 VAL   A HG23 1 
ATOM   2062 H HG23 B VAL   A 1 100 ? 18.586 -3.914  -10.047 0.22 23.83 ?  100 VAL   A HG23 1 
ATOM   2063 N N    A ASN   A 1 101 ? 19.337 0.336   -12.119 0.78 19.86 ?  101 ASN   A N    1 
ATOM   2064 N N    B ASN   A 1 101 ? 19.010 0.269   -12.104 0.22 20.52 ?  101 ASN   A N    1 
ATOM   2065 C CA   A ASN   A 1 101 ? 19.286 1.612   -12.823 0.78 21.79 ?  101 ASN   A CA   1 
ATOM   2066 C CA   B ASN   A 1 101 ? 18.889 1.551   -12.788 0.22 21.30 ?  101 ASN   A CA   1 
ATOM   2067 C C    A ASN   A 1 101 ? 20.649 2.041   -13.370 0.78 23.84 ?  101 ASN   A C    1 
ATOM   2068 C C    B ASN   A 1 101 ? 20.214 2.033   -13.364 0.22 22.86 ?  101 ASN   A C    1 
ATOM   2069 O O    A ASN   A 1 101 ? 20.736 3.097   -14.012 0.78 25.37 ?  101 ASN   A O    1 
ATOM   2070 O O    B ASN   A 1 101 ? 20.212 2.959   -14.182 0.22 23.11 ?  101 ASN   A O    1 
ATOM   2071 C CB   A ASN   A 1 101 ? 18.662 2.668   -11.912 0.78 21.55 ?  101 ASN   A CB   1 
ATOM   2072 C CB   B ASN   A 1 101 ? 18.290 2.591   -11.840 0.22 20.70 ?  101 ASN   A CB   1 
ATOM   2073 C CG   A ASN   A 1 101 ? 17.290 2.246   -11.400 0.78 20.88 ?  101 ASN   A CG   1 
ATOM   2074 C CG   B ASN   A 1 101 ? 16.947 2.155   -11.280 0.22 20.03 ?  101 ASN   A CG   1 
ATOM   2075 O OD1  A ASN   A 1 101 ? 16.464 1.722   -12.155 0.78 21.27 ?  101 ASN   A OD1  1 
ATOM   2076 O OD1  B ASN   A 1 101 ? 16.115 1.599   -11.999 0.22 19.74 ?  101 ASN   A OD1  1 
ATOM   2077 N ND2  A ASN   A 1 101 ? 17.050 2.450   -10.112 0.78 20.51 ?  101 ASN   A ND2  1 
ATOM   2078 N ND2  B ASN   A 1 101 ? 16.737 2.389   -9.991  0.22 19.66 ?  101 ASN   A ND2  1 
ATOM   2079 H H    A ASN   A 1 101 ? 19.259 0.391   -11.264 0.78 23.84 ?  101 ASN   A H    1 
ATOM   2080 H H    B ASN   A 1 101 ? 18.969 0.319   -11.248 0.22 24.64 ?  101 ASN   A H    1 
ATOM   2081 H HA   A ASN   A 1 101 ? 18.698 1.509   -13.583 0.78 26.16 ?  101 ASN   A HA   1 
ATOM   2082 H HA   B ASN   A 1 101 ? 18.273 1.446   -13.527 0.22 25.57 ?  101 ASN   A HA   1 
ATOM   2083 H HB2  A ASN   A 1 101 ? 19.243 2.818   -11.151 0.78 25.88 ?  101 ASN   A HB2  1 
ATOM   2084 H HB2  B ASN   A 1 101 ? 18.895 2.734   -11.097 0.22 24.86 ?  101 ASN   A HB2  1 
ATOM   2085 H HB3  A ASN   A 1 101 ? 18.559 3.496   -12.416 0.78 25.88 ?  101 ASN   A HB3  1 
ATOM   2086 H HB3  B ASN   A 1 101 ? 18.158 3.423   -12.326 0.22 24.86 ?  101 ASN   A HB3  1 
ATOM   2087 H HD21 A ASN   A 1 101 ? 16.292 2.228   -9.779  0.78 24.63 ?  101 ASN   A HD21 1 
ATOM   2088 H HD21 B ASN   A 1 101 ? 15.992 2.157   -9.629  0.22 23.61 ?  101 ASN   A HD21 1 
ATOM   2089 H HD22 A ASN   A 1 101 ? 17.649 2.819   -9.616  0.78 24.63 ?  101 ASN   A HD22 1 
ATOM   2090 H HD22 B ASN   A 1 101 ? 17.343 2.774   -9.520  0.22 23.61 ?  101 ASN   A HD22 1 
ATOM   2091 N N    A LYS   A 1 102 ? 21.697 1.241   -13.146 0.78 25.46 ?  102 LYS   A N    1 
ATOM   2092 N N    B LYS   A 1 102 ? 21.334 1.434   -12.955 0.22 24.23 ?  102 LYS   A N    1 
ATOM   2093 C CA   A LYS   A 1 102 ? 22.990 1.401   -13.800 0.78 26.77 ?  102 LYS   A CA   1 
ATOM   2094 C CA   B LYS   A 1 102 ? 22.615 1.626   -13.621 0.22 25.42 ?  102 LYS   A CA   1 
ATOM   2095 C C    A LYS   A 1 102 ? 23.291 0.282   -14.789 0.78 27.21 ?  102 LYS   A C    1 
ATOM   2096 C C    B LYS   A 1 102 ? 22.907 0.546   -14.652 0.22 25.65 ?  102 LYS   A C    1 
ATOM   2097 O O    A LYS   A 1 102 ? 24.385 0.259   -15.360 0.78 27.80 ?  102 LYS   A O    1 
ATOM   2098 O O    B LYS   A 1 102 ? 23.906 0.654   -15.372 0.22 25.70 ?  102 LYS   A O    1 
ATOM   2099 C CB   A LYS   A 1 102 ? 24.119 1.448   -12.762 0.78 28.29 ?  102 LYS   A CB   1 
ATOM   2100 C CB   B LYS   A 1 102 ? 23.756 1.642   -12.596 0.22 26.25 ?  102 LYS   A CB   1 
ATOM   2101 C CG   A LYS   A 1 102 ? 24.014 2.575   -11.753 0.78 29.56 ?  102 LYS   A CG   1 
ATOM   2102 C CG   B LYS   A 1 102 ? 23.748 2.829   -11.647 0.22 26.93 ?  102 LYS   A CG   1 
ATOM   2103 C CD   A LYS   A 1 102 ? 25.166 2.519   -10.755 0.78 30.96 ?  102 LYS   A CD   1 
ATOM   2104 C CD   B LYS   A 1 102 ? 24.845 2.686   -10.601 0.22 27.52 ?  102 LYS   A CD   1 
ATOM   2105 C CE   A LYS   A 1 102 ? 25.087 3.646   -9.737  0.78 32.19 ?  102 LYS   A CE   1 
ATOM   2106 C CE   B LYS   A 1 102 ? 24.844 3.845   -9.619  0.22 28.03 ?  102 LYS   A CE   1 
ATOM   2107 N NZ   A LYS   A 1 102 ? 26.196 3.578   -8.740  0.78 32.83 ?  102 LYS   A NZ   1 
ATOM   2108 N NZ   B LYS   A 1 102 ? 25.759 3.590   -8.471  0.22 28.29 ?  102 LYS   A NZ   1 
ATOM   2109 H H    A LYS   A 1 102 ? 21.681 0.573   -12.602 0.78 30.57 ?  102 LYS   A H    1 
ATOM   2110 H H    B LYS   A 1 102 ? 21.374 0.903   -12.281 0.22 29.09 ?  102 LYS   A H    1 
ATOM   2111 H HA   A LYS   A 1 102 ? 22.999 2.239   -14.283 0.78 32.14 ?  102 LYS   A HA   1 
ATOM   2112 H HA   B LYS   A 1 102 ? 22.613 2.478   -14.078 0.22 30.52 ?  102 LYS   A HA   1 
ATOM   2113 H HB2  A LYS   A 1 102 ? 24.122 0.612   -12.271 0.78 33.97 ?  102 LYS   A HB2  1 
ATOM   2114 H HB2  B LYS   A 1 102 ? 23.706 0.834   -12.065 0.22 31.51 ?  102 LYS   A HB2  1 
ATOM   2115 H HB3  A LYS   A 1 102 ? 24.964 1.551   -13.230 0.78 33.97 ?  102 LYS   A HB3  1 
ATOM   2116 H HB3  B LYS   A 1 102 ? 24.598 1.661   -13.074 0.22 31.51 ?  102 LYS   A HB3  1 
ATOM   2117 H HG2  A LYS   A 1 102 ? 24.050 3.425   -12.218 0.78 35.49 ?  102 LYS   A HG2  1 
ATOM   2118 H HG2  B LYS   A 1 102 ? 23.908 3.644   -12.149 0.22 32.33 ?  102 LYS   A HG2  1 
ATOM   2119 H HG3  A LYS   A 1 102 ? 23.181 2.490   -11.265 0.78 35.49 ?  102 LYS   A HG3  1 
ATOM   2120 H HG3  B LYS   A 1 102 ? 22.893 2.875   -11.191 0.22 32.33 ?  102 LYS   A HG3  1 
ATOM   2121 H HD2  A LYS   A 1 102 ? 25.135 1.675   -10.277 0.78 37.17 ?  102 LYS   A HD2  1 
ATOM   2122 H HD2  B LYS   A 1 102 ? 24.705 1.866   -10.102 0.22 33.04 ?  102 LYS   A HD2  1 
ATOM   2123 H HD3  A LYS   A 1 102 ? 26.007 2.600   -11.234 0.78 37.17 ?  102 LYS   A HD3  1 
ATOM   2124 H HD3  B LYS   A 1 102 ? 25.708 2.665   -11.044 0.22 33.04 ?  102 LYS   A HD3  1 
ATOM   2125 H HE2  A LYS   A 1 102 ? 25.146 4.497   -10.200 0.78 38.64 ?  102 LYS   A HE2  1 
ATOM   2126 H HE2  B LYS   A 1 102 ? 25.143 4.649   -10.074 0.22 33.65 ?  102 LYS   A HE2  1 
ATOM   2127 H HE3  A LYS   A 1 102 ? 24.245 3.584   -9.259  0.78 38.64 ?  102 LYS   A HE3  1 
ATOM   2128 H HE3  B LYS   A 1 102 ? 23.947 3.969   -9.272  0.22 33.65 ?  102 LYS   A HE3  1 
ATOM   2129 H HZ1  A LYS   A 1 102 ? 26.124 4.248   -8.159  0.78 39.41 ?  102 LYS   A HZ1  1 
ATOM   2130 H HZ1  B LYS   A 1 102 ? 25.704 4.256   -7.884  0.22 33.96 ?  102 LYS   A HZ1  1 
ATOM   2131 H HZ2  A LYS   A 1 102 ? 26.160 2.806   -8.298  0.78 39.41 ?  102 LYS   A HZ2  1 
ATOM   2132 H HZ2  B LYS   A 1 102 ? 25.534 2.829   -8.067  0.22 33.96 ?  102 LYS   A HZ2  1 
ATOM   2133 H HZ3  A LYS   A 1 102 ? 26.981 3.638   -9.154  0.78 39.41 ?  102 LYS   A HZ3  1 
ATOM   2134 H HZ3  B LYS   A 1 102 ? 26.599 3.525   -8.760  0.22 33.96 ?  102 LYS   A HZ3  1 
ATOM   2135 N N    A GLY   A 1 103 ? 22.369 -0.657  -14.989 0.78 27.50 ?  103 GLY   A N    1 
ATOM   2136 N N    B GLY   A 1 103 ? 22.072 -0.486  -14.738 0.22 25.98 ?  103 GLY   A N    1 
ATOM   2137 C CA   A GLY   A 1 103 ? 22.585 -1.748  -15.921 0.78 27.48 ?  103 GLY   A CA   1 
ATOM   2138 C CA   B GLY   A 1 103 ? 22.304 -1.567  -15.676 0.22 26.10 ?  103 GLY   A CA   1 
ATOM   2139 C C    A GLY   A 1 103 ? 23.376 -2.918  -15.380 0.78 27.17 ?  103 GLY   A C    1 
ATOM   2140 C C    B GLY   A 1 103 ? 23.294 -2.605  -15.197 0.22 26.26 ?  103 GLY   A C    1 
ATOM   2141 O O    A GLY   A 1 103 ? 23.828 -3.759  -16.163 0.78 28.18 ?  103 GLY   A O    1 
ATOM   2142 O O    B GLY   A 1 103 ? 24.062 -3.140  -16.007 0.22 26.49 ?  103 GLY   A O    1 
ATOM   2143 H H    A GLY   A 1 103 ? 21.613 -0.685  -14.588 0.78 33.01 ?  103 GLY   A H    1 
ATOM   2144 H H    B GLY   A 1 103 ? 21.360 -0.582  -14.265 0.22 31.19 ?  103 GLY   A H    1 
ATOM   2145 H HA2  A GLY   A 1 103 ? 21.726 -2.093  -16.207 0.78 33.00 ?  103 GLY   A HA2  1 
ATOM   2146 H HA2  B GLY   A 1 103 ? 21.460 -2.006  -15.869 0.22 31.33 ?  103 GLY   A HA2  1 
ATOM   2147 H HA3  A GLY   A 1 103 ? 23.044 -1.406  -16.707 0.78 33.00 ?  103 GLY   A HA3  1 
ATOM   2148 H HA3  B GLY   A 1 103 ? 22.649 -1.201  -16.503 0.22 31.33 ?  103 GLY   A HA3  1 
ATOM   2149 N N    A GLU   A 1 104 ? 23.540 -3.014  -14.065 0.78 24.86 ?  104 GLU   A N    1 
ATOM   2150 N N    B GLU   A 1 104 ? 23.305 -2.905  -13.901 0.22 25.90 ?  104 GLU   A N    1 
ATOM   2151 C CA   A GLU   A 1 104 ? 24.419 -4.016  -13.479 0.78 23.31 ?  104 GLU   A CA   1 
ATOM   2152 C CA   B GLU   A 1 104 ? 24.255 -3.848  -13.328 0.22 25.53 ?  104 GLU   A CA   1 
ATOM   2153 C C    A GLU   A 1 104 ? 23.726 -5.373  -13.378 0.78 23.41 ?  104 GLU   A C    1 
ATOM   2154 C C    B GLU   A 1 104 ? 23.617 -5.223  -13.161 0.22 25.93 ?  104 GLU   A C    1 
ATOM   2155 O O    A GLU   A 1 104 ? 22.501 -5.468  -13.250 0.78 23.96 ?  104 GLU   A O    1 
ATOM   2156 O O    B GLU   A 1 104 ? 22.434 -5.340  -12.825 0.22 25.88 ?  104 GLU   A O    1 
ATOM   2157 C CB   A GLU   A 1 104 ? 24.934 -3.533  -12.119 0.78 21.62 ?  104 GLU   A CB   1 
ATOM   2158 C CB   B GLU   A 1 104 ? 24.802 -3.317  -11.999 0.22 24.84 ?  104 GLU   A CB   1 
ATOM   2159 C CG   A GLU   A 1 104 ? 25.848 -2.309  -12.272 0.78 20.96 ?  104 GLU   A CG   1 
ATOM   2160 C CG   B GLU   A 1 104 ? 25.662 -2.069  -12.185 0.22 24.42 ?  104 GLU   A CG   1 
ATOM   2161 C CD   A GLU   A 1 104 ? 26.178 -1.567  -10.984 0.78 20.06 ?  104 GLU   A CD   1 
ATOM   2162 C CD   B GLU   A 1 104 ? 26.051 -1.402  -10.879 0.22 24.03 ?  104 GLU   A CD   1 
ATOM   2163 O OE1  A GLU   A 1 104 ? 25.582 -1.851  -9.924  0.78 18.72 ?  104 GLU   A OE1  1 
ATOM   2164 O OE1  B GLU   A 1 104 ? 25.501 -1.777  -9.823  0.22 23.65 ?  104 GLU   A OE1  1 
ATOM   2165 O OE2  A GLU   A 1 104 ? 27.051 -0.670  -11.055 0.78 21.07 -1 104 GLU   A OE2  1 
ATOM   2166 O OE2  B GLU   A 1 104 ? 26.908 -0.493  -10.911 0.22 24.23 -1 104 GLU   A OE2  1 
ATOM   2167 H H    A GLU   A 1 104 ? 23.146 -2.512  -13.493 0.78 29.85 ?  104 GLU   A H    1 
ATOM   2168 H H    B GLU   A 1 104 ? 22.770 -2.560  -13.320 0.22 31.09 ?  104 GLU   A H    1 
ATOM   2169 H HA   A GLU   A 1 104 ? 25.189 -4.126  -14.059 0.78 27.98 ?  104 GLU   A HA   1 
ATOM   2170 H HA   B GLU   A 1 104 ? 25.004 -3.945  -13.932 0.22 30.65 ?  104 GLU   A HA   1 
ATOM   2171 H HB2  A GLU   A 1 104 ? 24.181 -3.288  -11.564 0.78 25.96 ?  104 GLU   A HB2  1 
ATOM   2172 H HB2  B GLU   A 1 104 ? 24.064 -3.086  -11.413 0.22 29.82 ?  104 GLU   A HB2  1 
ATOM   2173 H HB3  A GLU   A 1 104 ? 25.444 -4.247  -11.704 0.78 25.96 ?  104 GLU   A HB3  1 
ATOM   2174 H HB3  B GLU   A 1 104 ? 25.355 -3.999  -11.583 0.22 29.82 ?  104 GLU   A HB3  1 
ATOM   2175 H HG2  A GLU   A 1 104 ? 26.687 -2.600  -12.660 0.78 25.17 ?  104 GLU   A HG2  1 
ATOM   2176 H HG2  B GLU   A 1 104 ? 26.477 -2.315  -12.654 0.22 29.31 ?  104 GLU   A HG2  1 
ATOM   2177 H HG3  A GLU   A 1 104 ? 25.416 -1.674  -12.862 0.78 25.17 ?  104 GLU   A HG3  1 
ATOM   2178 H HG3  B GLU   A 1 104 ? 25.167 -1.421  -12.711 0.22 29.31 ?  104 GLU   A HG3  1 
ATOM   2179 N N    A ASP   A 1 105 ? 24.535 -6.429  -13.436 0.78 24.21 ?  105 ASP   A N    1 
ATOM   2180 N N    B ASP   A 1 105 ? 24.417 -6.260  -13.405 0.22 26.34 ?  105 ASP   A N    1 
ATOM   2181 C CA   A ASP   A 1 105 ? 24.034 -7.792  -13.567 0.78 25.55 ?  105 ASP   A CA   1 
ATOM   2182 C CA   B ASP   A 1 105 ? 23.925 -7.631  -13.465 0.22 26.85 ?  105 ASP   A CA   1 
ATOM   2183 C C    A ASP   A 1 105 ? 23.336 -8.233  -12.285 0.78 23.06 ?  105 ASP   A C    1 
ATOM   2184 C C    B ASP   A 1 105 ? 23.256 -8.025  -12.154 0.22 26.12 ?  105 ASP   A C    1 
ATOM   2185 O O    A ASP   A 1 105 ? 23.967 -8.326  -11.230 0.78 20.78 ?  105 ASP   A O    1 
ATOM   2186 O O    B ASP   A 1 105 ? 23.891 -8.020  -11.096 0.22 26.02 ?  105 ASP   A O    1 
ATOM   2187 C CB   A ASP   A 1 105 ? 25.207 -8.719  -13.875 0.78 29.23 ?  105 ASP   A CB   1 
ATOM   2188 C CB   B ASP   A 1 105 ? 25.099 -8.565  -13.764 0.22 27.92 ?  105 ASP   A CB   1 
ATOM   2189 C CG   A ASP   A 1 105 ? 24.769 -10.130 -14.192 0.78 32.36 ?  105 ASP   A CG   1 
ATOM   2190 C CG   B ASP   A 1 105 ? 24.700 -10.028 -13.757 0.22 28.84 ?  105 ASP   A CG   1 
ATOM   2191 O OD1  A ASP   A 1 105 ? 23.547 -10.357 -14.306 0.78 32.92 ?  105 ASP   A OD1  1 
ATOM   2192 O OD1  B ASP   A 1 105 ? 23.499 -10.322 -13.932 0.22 29.10 ?  105 ASP   A OD1  1 
ATOM   2193 O OD2  A ASP   A 1 105 ? 25.650 -11.007 -14.333 0.78 34.08 -1 105 ASP   A OD2  1 
ATOM   2194 O OD2  B ASP   A 1 105 ? 25.590 -10.884 -13.571 0.22 29.27 -1 105 ASP   A OD2  1 
ATOM   2195 H H    A ASP   A 1 105 ? 25.395 -6.378  -13.403 0.78 29.07 ?  105 ASP   A H    1 
ATOM   2196 H H    B ASP   A 1 105 ? 25.259 -6.192  -13.536 0.22 31.62 ?  105 ASP   A H    1 
ATOM   2197 H HA   A ASP   A 1 105 ? 23.400 -7.840  -14.296 0.78 30.67 ?  105 ASP   A HA   1 
ATOM   2198 H HA   B ASP   A 1 105 ? 23.279 -7.719  -14.180 0.22 32.23 ?  105 ASP   A HA   1 
ATOM   2199 H HB2  A ASP   A 1 105 ? 25.686 -8.380  -14.648 0.78 35.09 ?  105 ASP   A HB2  1 
ATOM   2200 H HB2  B ASP   A 1 105 ? 25.452 -8.360  -14.647 0.22 33.52 ?  105 ASP   A HB2  1 
ATOM   2201 H HB3  A ASP   A 1 105 ? 25.801 -8.748  -13.107 0.78 35.09 ?  105 ASP   A HB3  1 
ATOM   2202 H HB3  B ASP   A 1 105 ? 25.792 -8.434  -13.096 0.22 33.52 ?  105 ASP   A HB3  1 
ATOM   2203 N N    A ILE   A 1 106 ? 22.039 -8.535  -12.383 0.78 22.97 ?  106 ILE   A N    1 
ATOM   2204 N N    B ILE   A 1 106 ? 21.967 -8.372  -12.229 0.22 25.51 ?  106 ILE   A N    1 
ATOM   2205 C CA   A ILE   A 1 106 ? 21.274 -8.952  -11.213 0.78 22.37 ?  106 ILE   A CA   1 
ATOM   2206 C CA   B ILE   A 1 106 ? 21.238 -8.792  -11.038 0.22 24.78 ?  106 ILE   A CA   1 
ATOM   2207 C C    A ILE   A 1 106 ? 21.813 -10.242 -10.621 0.78 21.60 ?  106 ILE   A C    1 
ATOM   2208 C C    B ILE   A 1 106 ? 21.744 -10.123 -10.495 0.22 24.11 ?  106 ILE   A C    1 
ATOM   2209 O O    A ILE   A 1 106 ? 21.611 -10.500 -9.431  0.78 20.73 ?  106 ILE   A O    1 
ATOM   2210 O O    B ILE   A 1 106 ? 21.535 -10.421 -9.314  0.22 23.75 ?  106 ILE   A O    1 
ATOM   2211 C CB   A ILE   A 1 106 ? 19.768 -9.058  -11.548 0.78 23.81 ?  106 ILE   A CB   1 
ATOM   2212 C CB   B ILE   A 1 106 ? 19.717 -8.814  -11.301 0.22 24.94 ?  106 ILE   A CB   1 
ATOM   2213 C CG1  A ILE   A 1 106 ? 18.928 -9.146  -10.270 0.78 24.24 ?  106 ILE   A CG1  1 
ATOM   2214 C CG1  B ILE   A 1 106 ? 18.937 -8.891  -9.983  0.22 24.93 ?  106 ILE   A CG1  1 
ATOM   2215 C CG2  A ILE   A 1 106 ? 19.494 -10.273 -12.416 0.78 24.56 ?  106 ILE   A CG2  1 
ATOM   2216 C CG2  B ILE   A 1 106 ? 19.344 -9.987  -12.194 0.22 25.18 ?  106 ILE   A CG2  1 
ATOM   2217 C CD1  A ILE   A 1 106 ? 19.062 -7.945  -9.366  0.78 24.45 ?  106 ILE   A CD1  1 
ATOM   2218 C CD1  B ILE   A 1 106 ? 19.293 -7.800  -8.991  0.22 24.90 ?  106 ILE   A CD1  1 
ATOM   2219 H H    A ILE   A 1 106 ? 21.590 -8.504  -13.108 0.78 27.58 ?  106 ILE   A H    1 
ATOM   2220 H H    B ILE   A 1 106 ? 21.494 -8.353  -12.946 0.22 30.62 ?  106 ILE   A H    1 
ATOM   2221 H HA   A ILE   A 1 106 ? 21.377 -8.278  -10.533 0.78 26.86 ?  106 ILE   A HA   1 
ATOM   2222 H HA   B ILE   A 1 106 ? 21.406 -8.135  -10.354 0.22 29.75 ?  106 ILE   A HA   1 
ATOM   2223 H HB   A ILE   A 1 106 ? 19.506 -8.264  -12.037 0.78 28.59 ?  106 ILE   A HB   1 
ATOM   2224 H HB   B ILE   A 1 106 ? 19.471 -7.994  -11.754 0.22 29.94 ?  106 ILE   A HB   1 
ATOM   2225 H HG12 A ILE   A 1 106 ? 17.994 -9.226  -10.516 0.78 29.11 ?  106 ILE   A HG12 1 
ATOM   2226 H HG12 B ILE   A 1 106 ? 17.988 -8.814  -10.177 0.22 29.93 ?  106 ILE   A HG12 1 
ATOM   2227 H HG13 A ILE   A 1 106 ? 19.203 -9.928  -9.767  0.78 29.11 ?  106 ILE   A HG13 1 
ATOM   2228 H HG13 B ILE   A 1 106 ? 19.115 -9.746  -9.561  0.22 29.93 ?  106 ILE   A HG13 1 
ATOM   2229 H HG21 A ILE   A 1 106 ? 18.609 -10.188 -12.802 0.78 29.49 ?  106 ILE   A HG21 1 
ATOM   2230 H HG21 B ILE   A 1 106 ? 18.438 -9.861  -12.519 0.22 30.23 ?  106 ILE   A HG21 1 
ATOM   2231 H HG22 A ILE   A 1 106 ? 20.161 -10.311 -13.117 0.78 29.49 ?  106 ILE   A HG22 1 
ATOM   2232 H HG22 B ILE   A 1 106 ? 19.961 -10.021 -12.941 0.22 30.23 ?  106 ILE   A HG22 1 
ATOM   2233 H HG23 A ILE   A 1 106 ? 19.542 -11.070 -11.867 0.78 29.49 ?  106 ILE   A HG23 1 
ATOM   2234 H HG23 B ILE   A 1 106 ? 19.399 -10.809 -11.682 0.22 30.23 ?  106 ILE   A HG23 1 
ATOM   2235 H HD11 A ILE   A 1 106 ? 18.324 -7.941  -8.739  0.78 29.35 ?  106 ILE   A HD11 1 
ATOM   2236 H HD11 B ILE   A 1 106 ? 18.576 -7.715  -8.346  0.22 29.90 ?  106 ILE   A HD11 1 
ATOM   2237 H HD12 A ILE   A 1 106 ? 19.904 -8.003  -8.884  0.78 29.35 ?  106 ILE   A HD12 1 
ATOM   2238 H HD12 B ILE   A 1 106 ? 20.118 -8.040  -8.539  0.22 29.90 ?  106 ILE   A HD12 1 
ATOM   2239 H HD13 A ILE   A 1 106 ? 19.043 -7.140  -9.906  0.78 29.35 ?  106 ILE   A HD13 1 
ATOM   2240 H HD13 B ILE   A 1 106 ? 19.407 -6.964  -9.470  0.22 29.90 ?  106 ILE   A HD13 1 
ATOM   2241 N N    A GLN   A 1 107 ? 22.498 -11.064 -11.426 0.78 22.51 ?  107 GLN   A N    1 
ATOM   2242 N N    B GLN   A 1 107 ? 22.411 -10.935 -11.321 0.22 24.14 ?  107 GLN   A N    1 
ATOM   2243 C CA   A GLN   A 1 107 ? 23.131 -12.270 -10.905 0.78 24.99 ?  107 GLN   A CA   1 
ATOM   2244 C CA   B GLN   A 1 107 ? 22.984 -12.180 -10.820 0.22 24.12 ?  107 GLN   A CA   1 
ATOM   2245 C C    A GLN   A 1 107 ? 24.106 -11.952 -9.784  0.78 22.56 ?  107 GLN   A C    1 
ATOM   2246 C C    B GLN   A 1 107 ? 24.053 -11.927 -9.766  0.22 21.50 ?  107 GLN   A C    1 
ATOM   2247 O O    A GLN   A 1 107 ? 24.351 -12.808 -8.927  0.78 23.99 ?  107 GLN   A O    1 
ATOM   2248 O O    B GLN   A 1 107 ? 24.334 -12.817 -8.957  0.22 22.09 ?  107 GLN   A O    1 
ATOM   2249 C CB   A GLN   A 1 107 ? 23.858 -13.013 -12.033 0.78 29.67 ?  107 GLN   A CB   1 
ATOM   2250 C CB   B GLN   A 1 107 ? 23.554 -13.010 -11.974 0.22 26.70 ?  107 GLN   A CB   1 
ATOM   2251 C CG   A GLN   A 1 107 ? 22.996 -13.276 -13.262 0.78 34.58 ?  107 GLN   A CG   1 
ATOM   2252 C CG   B GLN   A 1 107 ? 22.555 -13.285 -13.089 0.22 29.24 ?  107 GLN   A CG   1 
ATOM   2253 C CD   A GLN   A 1 107 ? 21.749 -14.074 -12.941 0.78 38.71 ?  107 GLN   A CD   1 
ATOM   2254 C CD   B GLN   A 1 107 ? 21.254 -13.878 -12.582 0.22 31.28 ?  107 GLN   A CD   1 
ATOM   2255 O OE1  A GLN   A 1 107 ? 21.815 -15.120 -12.295 0.78 40.15 ?  107 GLN   A OE1  1 
ATOM   2256 O OE1  B GLN   A 1 107 ? 21.249 -14.722 -11.686 0.22 32.00 ?  107 GLN   A OE1  1 
ATOM   2257 N NE2  A GLN   A 1 107 ? 20.600 -13.577 -13.386 0.78 40.00 ?  107 GLN   A NE2  1 
ATOM   2258 N NE2  B GLN   A 1 107 ? 20.140 -13.430 -13.150 0.22 31.94 ?  107 GLN   A NE2  1 
ATOM   2259 H H    A GLN   A 1 107 ? 22.611 -10.946 -12.266 0.78 27.02 ?  107 GLN   A H    1 
ATOM   2260 H H    B GLN   A 1 107 ? 22.541 -10.790 -12.158 0.22 28.98 ?  107 GLN   A H    1 
ATOM   2261 H HA   A GLN   A 1 107 ? 22.458 -12.866 -10.547 0.78 30.00 ?  107 GLN   A HA   1 
ATOM   2262 H HA   B GLN   A 1 107 ? 22.284 -12.700 -10.400 0.22 28.96 ?  107 GLN   A HA   1 
ATOM   2263 H HB2  A GLN   A 1 107 ? 24.623 -12.487 -12.317 0.78 35.62 ?  107 GLN   A HB2  1 
ATOM   2264 H HB2  B GLN   A 1 107 ? 24.306 -12.537 -12.362 0.22 32.06 ?  107 GLN   A HB2  1 
ATOM   2265 H HB3  A GLN   A 1 107 ? 24.163 -13.875 -11.702 0.78 35.62 ?  107 GLN   A HB3  1 
ATOM   2266 H HB3  B GLN   A 1 107 ? 23.851 -13.867 -11.627 0.22 32.06 ?  107 GLN   A HB3  1 
ATOM   2267 H HG2  A GLN   A 1 107 ? 22.719 -12.430 -13.646 0.78 41.51 ?  107 GLN   A HG2  1 
ATOM   2268 H HG2  B GLN   A 1 107 ? 22.348 -12.453 -13.541 0.22 35.10 ?  107 GLN   A HG2  1 
ATOM   2269 H HG3  A GLN   A 1 107 ? 23.516 -13.777 -13.910 0.78 41.51 ?  107 GLN   A HG3  1 
ATOM   2270 H HG3  B GLN   A 1 107 ? 22.946 -13.915 -13.715 0.22 35.10 ?  107 GLN   A HG3  1 
ATOM   2271 H HE21 A GLN   A 1 107 ? 20.592 -12.843 -13.833 0.78 48.02 ?  107 GLN   A HE21 1 
ATOM   2272 H HE21 B GLN   A 1 107 ? 20.183 -12.838 -13.772 0.22 38.34 ?  107 GLN   A HE21 1 
ATOM   2273 H HE22 A GLN   A 1 107 ? 19.864 -13.993 -13.228 0.78 48.02 ?  107 GLN   A HE22 1 
ATOM   2274 H HE22 B GLN   A 1 107 ? 19.376 -13.734 -12.897 0.22 38.34 ?  107 GLN   A HE22 1 
ATOM   2275 N N    . LEU   A 1 108 ? 24.645 -10.731 -9.750  1.00 18.24 ?  108 LEU   A N    1 
ATOM   2276 C CA   . LEU   A 1 108 ? 25.579 -10.359 -8.700  1.00 14.81 ?  108 LEU   A CA   1 
ATOM   2277 C C    . LEU   A 1 108 ? 24.895 -10.208 -7.353  1.00 13.14 ?  108 LEU   A C    1 
ATOM   2278 O O    . LEU   A 1 108 ? 25.589 -10.063 -6.344  1.00 13.29 ?  108 LEU   A O    1 
ATOM   2279 C CB   . LEU   A 1 108 ? 26.318 -9.071  -9.079  1.00 14.43 ?  108 LEU   A CB   1 
ATOM   2280 C CG   . LEU   A 1 108 ? 27.309 -9.264  -10.230 1.00 16.30 ?  108 LEU   A CG   1 
ATOM   2281 C CD1  . LEU   A 1 108 ? 27.801 -7.928  -10.773 1.00 17.45 ?  108 LEU   A CD1  1 
ATOM   2282 C CD2  . LEU   A 1 108 ? 28.492 -10.114 -9.783  1.00 18.28 ?  108 LEU   A CD2  1 
ATOM   2283 H H    A LEU   A 1 108 ? 24.481 -10.109 -10.315 0.78 21.91 ?  108 LEU   A H    1 
ATOM   2284 H H    B LEU   A 1 108 ? 24.523 -10.122 -10.339 0.22 21.91 ?  108 LEU   A H    1 
ATOM   2285 H HA   . LEU   A 1 108 ? 26.237 -11.062 -8.602  1.00 17.78 ?  108 LEU   A HA   1 
ATOM   2286 H HB2  . LEU   A 1 108 ? 25.668 -8.406  -9.356  1.00 17.33 ?  108 LEU   A HB2  1 
ATOM   2287 H HB3  . LEU   A 1 108 ? 26.811 -8.752  -8.309  1.00 17.33 ?  108 LEU   A HB3  1 
ATOM   2288 H HG   . LEU   A 1 108 ? 26.865 -9.737  -10.953 1.00 19.57 ?  108 LEU   A HG   1 
ATOM   2289 H HD11 . LEU   A 1 108 ? 28.398 -8.090  -11.524 1.00 20.96 ?  108 LEU   A HD11 1 
ATOM   2290 H HD12 . LEU   A 1 108 ? 27.039 -7.406  -11.066 1.00 20.96 ?  108 LEU   A HD12 1 
ATOM   2291 H HD13 . LEU   A 1 108 ? 28.277 -7.456  -10.072 1.00 20.96 ?  108 LEU   A HD13 1 
ATOM   2292 H HD21 . LEU   A 1 108 ? 29.183 -10.070 -10.459 1.00 21.95 ?  108 LEU   A HD21 1 
ATOM   2293 H HD22 . LEU   A 1 108 ? 28.825 -9.767  -8.942  1.00 21.95 ?  108 LEU   A HD22 1 
ATOM   2294 H HD23 . LEU   A 1 108 ? 28.196 -11.032 -9.669  1.00 21.95 ?  108 LEU   A HD23 1 
ATOM   2295 N N    . LEU   A 1 109 ? 23.562 -10.261 -7.304  1.00 12.53 ?  109 LEU   A N    1 
ATOM   2296 C CA   . LEU   A 1 109 ? 22.873 -10.142 -6.025  1.00 11.86 ?  109 LEU   A CA   1 
ATOM   2297 C C    . LEU   A 1 109 ? 23.233 -11.295 -5.095  1.00 11.04 ?  109 LEU   A C    1 
ATOM   2298 O O    . LEU   A 1 109 ? 23.376 -11.098 -3.883  1.00 11.43 ?  109 LEU   A O    1 
ATOM   2299 C CB   . LEU   A 1 109 ? 21.367 -10.055 -6.261  1.00 12.52 ?  109 LEU   A CB   1 
ATOM   2300 C CG   . LEU   A 1 109 ? 20.493 -9.765  -5.045  1.00 12.72 ?  109 LEU   A CG   1 
ATOM   2301 C CD1  . LEU   A 1 109 ? 20.952 -8.497  -4.339  1.00 13.13 ?  109 LEU   A CD1  1 
ATOM   2302 C CD2  . LEU   A 1 109 ? 19.041 -9.641  -5.465  1.00 13.66 ?  109 LEU   A CD2  1 
ATOM   2303 H H    . LEU   A 1 109 ? 23.043 -10.363 -7.981  1.00 15.05 ?  109 LEU   A H    1 
ATOM   2304 H HA   . LEU   A 1 109 ? 23.157 -9.319  -5.597  1.00 14.25 ?  109 LEU   A HA   1 
ATOM   2305 H HB2  . LEU   A 1 109 ? 21.202 -9.344  -6.902  1.00 15.04 ?  109 LEU   A HB2  1 
ATOM   2306 H HB3  . LEU   A 1 109 ? 21.067 -10.896 -6.630  1.00 15.04 ?  109 LEU   A HB3  1 
ATOM   2307 H HG   . LEU   A 1 109 ? 20.565 -10.499 -4.418  1.00 15.28 ?  109 LEU   A HG   1 
ATOM   2308 H HD11 . LEU   A 1 109 ? 20.274 -8.213  -3.710  1.00 15.77 ?  109 LEU   A HD11 1 
ATOM   2309 H HD12 . LEU   A 1 109 ? 21.785 -8.678  -3.868  1.00 15.77 ?  109 LEU   A HD12 1 
ATOM   2310 H HD13 . LEU   A 1 109 ? 21.099 -7.801  -5.002  1.00 15.77 ?  109 LEU   A HD13 1 
ATOM   2311 H HD21 . LEU   A 1 109 ? 18.512 -9.349  -4.704  1.00 16.41 ?  109 LEU   A HD21 1 
ATOM   2312 H HD22 . LEU   A 1 109 ? 18.970 -8.991  -6.182  1.00 16.41 ?  109 LEU   A HD22 1 
ATOM   2313 H HD23 . LEU   A 1 109 ? 18.724 -10.506 -5.773  1.00 16.41 ?  109 LEU   A HD23 1 
ATOM   2314 N N    . LYS   A 1 110 ? 23.385 -12.506 -5.635  1.00 11.00 ?  110 LYS   A N    1 
ATOM   2315 C CA   . LYS   A 1 110 ? 23.764 -13.631 -4.786  1.00 11.06 ?  110 LYS   A CA   1 
ATOM   2316 C C    . LYS   A 1 110 ? 25.147 -13.410 -4.180  1.00 10.50 ?  110 LYS   A C    1 
ATOM   2317 O O    . LYS   A 1 110 ? 25.347 -13.604 -2.979  1.00 10.77 ?  110 LYS   A O    1 
ATOM   2318 C CB   . LYS   A 1 110 ? 23.676 -14.949 -5.561  1.00 11.57 ?  110 LYS   A CB   1 
ATOM   2319 C CG   . LYS   A 1 110 ? 23.908 -16.163 -4.665  1.00 11.99 ?  110 LYS   A CG   1 
ATOM   2320 C CD   . LYS   A 1 110 ? 23.659 -17.481 -5.371  1.00 12.53 ?  110 LYS   A CD   1 
ATOM   2321 C CE   . LYS   A 1 110 ? 23.766 -18.666 -4.419  1.00 13.29 ?  110 LYS   A CE   1 
ATOM   2322 N NZ   . LYS   A 1 110 ? 22.583 -18.786 -3.528  1.00 13.93 ?  110 LYS   A NZ   1 
ATOM   2323 H H    . LYS   A 1 110 ? 23.271 -12.696 -6.467  1.00 13.21 ?  110 LYS   A H    1 
ATOM   2324 H HA   . LYS   A 1 110 ? 23.126 -13.687 -4.054  1.00 13.29 ?  110 LYS   A HA   1 
ATOM   2325 H HB2  . LYS   A 1 110 ? 22.793 -15.031 -5.956  1.00 13.90 ?  110 LYS   A HB2  1 
ATOM   2326 H HB3  . LYS   A 1 110 ? 24.353 -14.952 -6.257  1.00 13.90 ?  110 LYS   A HB3  1 
ATOM   2327 H HG2  . LYS   A 1 110 ? 24.832 -16.159 -4.362  1.00 14.41 ?  110 LYS   A HG2  1 
ATOM   2328 H HG3  . LYS   A 1 110 ? 23.312 -16.114 -3.904  1.00 14.41 ?  110 LYS   A HG3  1 
ATOM   2329 H HD2  . LYS   A 1 110 ? 22.768 -17.475 -5.749  1.00 15.06 ?  110 LYS   A HD2  1 
ATOM   2330 H HD3  . LYS   A 1 110 ? 24.321 -17.597 -6.071  1.00 15.06 ?  110 LYS   A HD3  1 
ATOM   2331 H HE2  . LYS   A 1 110 ? 23.837 -19.484 -4.934  1.00 15.97 ?  110 LYS   A HE2  1 
ATOM   2332 H HE3  . LYS   A 1 110 ? 24.552 -18.556 -3.859  1.00 15.97 ?  110 LYS   A HE3  1 
ATOM   2333 H HZ1  . LYS   A 1 110 ? 22.675 -19.483 -2.986  1.00 16.73 ?  110 LYS   A HZ1  1 
ATOM   2334 H HZ2  . LYS   A 1 110 ? 22.496 -18.046 -3.036  1.00 16.73 ?  110 LYS   A HZ2  1 
ATOM   2335 H HZ3  . LYS   A 1 110 ? 21.845 -18.892 -4.016  1.00 16.73 ?  110 LYS   A HZ3  1 
ATOM   2336 N N    . SER   A 1 111 ? 26.106 -12.968 -4.999  1.00 10.70 ?  111 SER   A N    1 
ATOM   2337 C CA   . SER   A 1 111 ? 27.439 -12.665 -4.486  1.00 10.89 ?  111 SER   A CA   1 
ATOM   2338 C C    . SER   A 1 111 ? 27.373 -11.620 -3.377  1.00 10.81 ?  111 SER   A C    1 
ATOM   2339 O O    . SER   A 1 111 ? 28.074 -11.724 -2.365  1.00 11.13 ?  111 SER   A O    1 
ATOM   2340 C CB   . SER   A 1 111 ? 28.329 -12.168 -5.626  1.00 12.24 ?  111 SER   A CB   1 
ATOM   2341 O OG   . SER   A 1 111 ? 28.444 -13.164 -6.631  1.00 14.50 ?  111 SER   A OG   1 
ATOM   2342 H H    . SER   A 1 111 ? 26.007 -12.844 -5.841  1.00 12.86 ?  111 SER   A H    1 
ATOM   2343 H HA   . SER   A 1 111 ? 27.834 -13.474 -4.121  1.00 13.09 ?  111 SER   A HA   1 
ATOM   2344 H HB2  . SER   A 1 111 ? 27.926 -11.380 -6.020  1.00 14.70 ?  111 SER   A HB2  1 
ATOM   2345 H HB3  . SER   A 1 111 ? 29.205 -11.954 -5.271  1.00 14.70 ?  111 SER   A HB3  1 
ATOM   2346 H HG   . SER   A 1 111 ? 28.956 -12.882 -7.247  1.00 17.42 ?  111 SER   A HG   1 
ATOM   2347 N N    . ALA   A 1 112 ? 26.532 -10.600 -3.556  1.00 10.76 ?  112 ALA   A N    1 
ATOM   2348 C CA   . ALA   A 1 112 ? 26.389 -9.564  -2.536  1.00 10.48 ?  112 ALA   A CA   1 
ATOM   2349 C C    . ALA   A 1 112 ? 25.912 -10.163 -1.215  1.00 10.28 ?  112 ALA   A C    1 
ATOM   2350 O O    . ALA   A 1 112 ? 26.468 -9.880  -0.148  1.00 10.61 ?  112 ALA   A O    1 
ATOM   2351 C CB   . ALA   A 1 112 ? 25.436 -8.476  -3.032  1.00 11.06 ?  112 ALA   A CB   1 
ATOM   2352 H H    . ALA   A 1 112 ? 26.040 -10.482 -4.250  1.00 12.93 ?  112 ALA   A H    1 
ATOM   2353 H HA   . ALA   A 1 112 ? 27.252 -9.149  -2.381  1.00 12.59 ?  112 ALA   A HA   1 
ATOM   2354 H HB1  . ALA   A 1 112 ? 25.357 -7.782  -2.349  1.00 13.29 ?  112 ALA   A HB1  1 
ATOM   2355 H HB2  . ALA   A 1 112 ? 25.789 -8.085  -3.848  1.00 13.29 ?  112 ALA   A HB2  1 
ATOM   2356 H HB3  . ALA   A 1 112 ? 24.564 -8.863  -3.203  1.00 13.29 ?  112 ALA   A HB3  1 
ATOM   2357 N N    . TYR   A 1 113 ? 24.880 -11.010 -1.263  1.00 10.48 ?  113 TYR   A N    1 
ATOM   2358 C CA   . TYR   A 1 113 ? 24.374 -11.617 -0.032  1.00 10.42 ?  113 TYR   A CA   1 
ATOM   2359 C C    . TYR   A 1 113 ? 25.380 -12.570 0.609   1.00 9.99  ?  113 TYR   A C    1 
ATOM   2360 O O    . TYR   A 1 113 ? 25.344 -12.761 1.828   1.00 10.51 ?  113 TYR   A O    1 
ATOM   2361 C CB   . TYR   A 1 113 ? 23.055 -12.348 -0.290  1.00 10.81 ?  113 TYR   A CB   1 
ATOM   2362 C CG   . TYR   A 1 113 ? 21.836 -11.456 -0.182  1.00 10.48 ?  113 TYR   A CG   1 
ATOM   2363 C CD1  . TYR   A 1 113 ? 21.483 -10.874 1.029   1.00 10.76 ?  113 TYR   A CD1  1 
ATOM   2364 C CD2  . TYR   A 1 113 ? 21.024 -11.214 -1.283  1.00 10.93 ?  113 TYR   A CD2  1 
ATOM   2365 C CE1  . TYR   A 1 113 ? 20.362 -10.073 1.138   1.00 10.76 ?  113 TYR   A CE1  1 
ATOM   2366 C CE2  . TYR   A 1 113 ? 19.879 -10.415 -1.176  1.00 11.05 ?  113 TYR   A CE2  1 
ATOM   2367 C CZ   . TYR   A 1 113 ? 19.562 -9.851  0.037   1.00 10.76 ?  113 TYR   A CZ   1 
ATOM   2368 O OH   . TYR   A 1 113 ? 18.439 -9.059  0.176   1.00 11.62 ?  113 TYR   A OH   1 
ATOM   2369 H H    . TYR   A 1 113 ? 24.470 -11.250 -1.980  1.00 12.59 ?  113 TYR   A H    1 
ATOM   2370 H HA   . TYR   A 1 113 ? 24.202 -10.907 0.606   1.00 12.52 ?  113 TYR   A HA   1 
ATOM   2371 H HB2  . TYR   A 1 113 ? 23.071 -12.713 -1.185  1.00 12.99 ?  113 TYR   A HB2  1 
ATOM   2372 H HB3  . TYR   A 1 113 ? 22.961 -13.056 0.360   1.00 12.99 ?  113 TYR   A HB3  1 
ATOM   2373 H HD1  . TYR   A 1 113 ? 22.017 -11.017 1.779   1.00 12.93 ?  113 TYR   A HD1  1 
ATOM   2374 H HD2  . TYR   A 1 113 ? 21.228 -11.604 -2.097  1.00 13.13 ?  113 TYR   A HD2  1 
ATOM   2375 H HE1  . TYR   A 1 113 ? 20.141 -9.685  1.960   1.00 12.93 ?  113 TYR   A HE1  1 
ATOM   2376 H HE2  . TYR   A 1 113 ? 19.332 -10.259 -1.915  1.00 13.28 ?  113 TYR   A HE2  1 
ATOM   2377 H HH   . TYR   A 1 113 ? 18.040 -8.999  -0.567  1.00 13.96 ?  113 TYR   A HH   1 
ATOM   2378 N N    . GLU   A 1 114 ? 26.279 -13.181 -0.178  1.00 10.32 ?  114 GLU   A N    1 
ATOM   2379 C CA   . GLU   A 1 114 ? 27.267 -14.085 0.414   1.00 10.47 ?  114 GLU   A CA   1 
ATOM   2380 C C    . GLU   A 1 114 ? 28.120 -13.378 1.464   1.00 10.51 ?  114 GLU   A C    1 
ATOM   2381 O O    . GLU   A 1 114 ? 28.602 -14.017 2.407   1.00 10.90 ?  114 GLU   A O    1 
ATOM   2382 C CB   . GLU   A 1 114 ? 28.136 -14.726 -0.677  1.00 10.62 ?  114 GLU   A CB   1 
ATOM   2383 C CG   . GLU   A 1 114 ? 27.362 -15.777 -1.461  1.00 10.93 ?  114 GLU   A CG   1 
ATOM   2384 C CD   . GLU   A 1 114 ? 28.063 -16.310 -2.707  1.00 11.36 ?  114 GLU   A CD   1 
ATOM   2385 O OE1  . GLU   A 1 114 ? 29.025 -15.685 -3.207  1.00 11.67 ?  114 GLU   A OE1  1 
ATOM   2386 O OE2  . GLU   A 1 114 ? 27.623 -17.378 -3.193  1.00 12.56 -1 114 GLU   A OE2  1 
ATOM   2387 H H    . GLU   A 1 114 ? 26.331 -13.083 -1.037  1.00 12.40 ?  114 GLU   A H    1 
ATOM   2388 H HA   . GLU   A 1 114 ? 26.789 -14.796 0.855   1.00 12.58 ?  114 GLU   A HA   1 
ATOM   2389 H HB2  . GLU   A 1 114 ? 28.431 -14.045 -1.304  1.00 12.75 ?  114 GLU   A HB2  1 
ATOM   2390 H HB3  . GLU   A 1 114 ? 28.898 -15.159 -0.268  1.00 12.75 ?  114 GLU   A HB3  1 
ATOM   2391 H HG2  . GLU   A 1 114 ? 27.194 -16.537 -0.883  1.00 13.13 ?  114 GLU   A HG2  1 
ATOM   2392 H HG3  . GLU   A 1 114 ? 26.519 -15.397 -1.751  1.00 13.13 ?  114 GLU   A HG3  1 
ATOM   2393 N N    . ASN   A 1 115 ? 28.301 -12.057 1.340   1.00 10.37 ?  115 ASN   A N    1 
ATOM   2394 C CA   . ASN   A 1 115 ? 29.075 -11.333 2.345   1.00 10.51 ?  115 ASN   A CA   1 
ATOM   2395 C C    . ASN   A 1 115 ? 28.466 -11.473 3.734   1.00 10.30 ?  115 ASN   A C    1 
ATOM   2396 O O    . ASN   A 1 115 ? 29.184 -11.401 4.738   1.00 10.93 ?  115 ASN   A O    1 
ATOM   2397 C CB   . ASN   A 1 115 ? 29.177 -9.855  1.969   1.00 10.75 ?  115 ASN   A CB   1 
ATOM   2398 C CG   . ASN   A 1 115 ? 29.971 -9.631  0.707   1.00 11.65 ?  115 ASN   A CG   1 
ATOM   2399 O OD1  . ASN   A 1 115 ? 31.188 -9.742  0.712   1.00 15.04 ?  115 ASN   A OD1  1 
ATOM   2400 N ND2  . ASN   A 1 115 ? 29.290 -9.327  -0.380  1.00 11.34 ?  115 ASN   A ND2  1 
ATOM   2401 H H    . ASN   A 1 115 ? 27.983 -11.567 0.704   1.00 12.46 ?  115 ASN   A H    1 
ATOM   2402 H HA   . ASN   A 1 115 ? 29.967 -11.701 2.376   1.00 12.63 ?  115 ASN   A HA   1 
ATOM   2403 H HB2  . ASN   A 1 115 ? 28.283 -9.499  1.841   1.00 12.91 ?  115 ASN   A HB2  1 
ATOM   2404 H HB3  . ASN   A 1 115 ? 29.619 -9.380  2.694   1.00 12.91 ?  115 ASN   A HB3  1 
ATOM   2405 H HD21 . ASN   A 1 115 ? 29.698 -9.182  -1.120  1.00 13.62 ?  115 ASN   A HD21 1 
ATOM   2406 H HD22 . ASN   A 1 115 ? 28.428 -9.266  -0.346  1.00 13.62 ?  115 ASN   A HD22 1 
ATOM   2407 N N    . PHE   A 1 116 ? 27.141 -11.644 3.817   1.00 10.47 ?  116 PHE   A N    1 
ATOM   2408 C CA   . PHE   A 1 116 ? 26.490 -11.746 5.118   1.00 10.40 ?  116 PHE   A CA   1 
ATOM   2409 C C    . PHE   A 1 116 ? 26.971 -12.977 5.883   1.00 10.64 ?  116 PHE   A C    1 
ATOM   2410 O O    . PHE   A 1 116 ? 26.899 -12.999 7.111   1.00 11.20 ?  116 PHE   A O    1 
ATOM   2411 C CB   . PHE   A 1 116 ? 24.963 -11.875 4.977   1.00 10.63 ?  116 PHE   A CB   1 
ATOM   2412 C CG   . PHE   A 1 116 ? 24.208 -10.626 4.533   1.00 10.35 ?  116 PHE   A CG   1 
ATOM   2413 C CD1  . PHE   A 1 116 ? 24.779 -9.594  3.799   1.00 10.46 ?  116 PHE   A CD1  1 
ATOM   2414 C CD2  . PHE   A 1 116 ? 22.856 -10.530 4.855   1.00 11.14 ?  116 PHE   A CD2  1 
ATOM   2415 C CE1  . PHE   A 1 116 ? 24.009 -8.502  3.399   1.00 10.82 ?  116 PHE   A CE1  1 
ATOM   2416 C CE2  . PHE   A 1 116 ? 22.090 -9.450  4.459   1.00 11.22 ?  116 PHE   A CE2  1 
ATOM   2417 C CZ   . PHE   A 1 116 ? 22.661 -8.437  3.730   1.00 10.74 ?  116 PHE   A CZ   1 
ATOM   2418 H H    . PHE   A 1 116 ? 26.602 -11.690 3.139   1.00 12.57 ?  116 PHE   A H    1 
ATOM   2419 H HA   . PHE   A 1 116 ? 26.680 -10.954 5.643   1.00 12.50 ?  116 PHE   A HA   1 
ATOM   2420 H HB2  . PHE   A 1 116 ? 24.777 -12.573 4.324   1.00 12.77 ?  116 PHE   A HB2  1 
ATOM   2421 H HB3  . PHE   A 1 116 ? 24.600 -12.144 5.836   1.00 12.77 ?  116 PHE   A HB3  1 
ATOM   2422 H HD1  . PHE   A 1 116 ? 25.676 -9.650  3.562   1.00 12.56 ?  116 PHE   A HD1  1 
ATOM   2423 H HD2  . PHE   A 1 116 ? 22.451 -11.223 5.337   1.00 13.38 ?  116 PHE   A HD2  1 
ATOM   2424 H HE1  . PHE   A 1 116 ? 24.404 -7.821  2.908   1.00 13.00 ?  116 PHE   A HE1  1 
ATOM   2425 H HE2  . PHE   A 1 116 ? 21.187 -9.414  4.692   1.00 13.48 ?  116 PHE   A HE2  1 
ATOM   2426 H HZ   . PHE   A 1 116 ? 22.154 -7.702  3.475   1.00 12.90 ?  116 PHE   A HZ   1 
ATOM   2427 N N    . ASN   A 1 117 ? 27.405 -14.029 5.176   1.00 10.82 ?  117 ASN   A N    1 
ATOM   2428 C CA   . ASN   A 1 117 ? 27.780 -15.278 5.836   1.00 10.94 ?  117 ASN   A CA   1 
ATOM   2429 C C    . ASN   A 1 117 ? 29.048 -15.158 6.658   1.00 11.61 ?  117 ASN   A C    1 
ATOM   2430 O O    . ASN   A 1 117 ? 29.356 -16.078 7.425   1.00 12.35 ?  117 ASN   A O    1 
ATOM   2431 C CB   . ASN   A 1 117 ? 27.886 -16.397 4.807   1.00 11.31 ?  117 ASN   A CB   1 
ATOM   2432 C CG   . ASN   A 1 117 ? 26.528 -16.782 4.279   1.00 11.28 ?  117 ASN   A CG   1 
ATOM   2433 O OD1  . ASN   A 1 117 ? 25.564 -16.819 5.037   1.00 12.04 ?  117 ASN   A OD1  1 
ATOM   2434 N ND2  . ASN   A 1 117 ? 26.430 -17.040 2.989   1.00 11.28 ?  117 ASN   A ND2  1 
ATOM   2435 H H    . ASN   A 1 117 ? 27.474 -14.041 4.317   1.00 13.00 ?  117 ASN   A H    1 
ATOM   2436 H HA   . ASN   A 1 117 ? 27.067 -15.515 6.445   1.00 13.14 ?  117 ASN   A HA   1 
ATOM   2437 H HB2  . ASN   A 1 117 ? 28.430 -16.096 4.061   1.00 13.58 ?  117 ASN   A HB2  1 
ATOM   2438 H HB3  . ASN   A 1 117 ? 28.285 -17.173 5.224   1.00 13.58 ?  117 ASN   A HB3  1 
ATOM   2439 H HD21 . ASN   A 1 117 ? 25.673 -17.256 2.651   1.00 13.55 ?  117 ASN   A HD21 1 
ATOM   2440 H HD22 . ASN   A 1 117 ? 27.130 -16.993 2.488   1.00 13.55 ?  117 ASN   A HD22 1 
ATOM   2441 N N    . GLN   A 1 118 ? 29.778 -14.049 6.532   1.00 11.63 ?  118 GLN   A N    1 
ATOM   2442 C CA   . GLN   A 1 118 ? 30.961 -13.811 7.347   1.00 12.23 ?  118 GLN   A CA   1 
ATOM   2443 C C    . GLN   A 1 118 ? 30.627 -13.239 8.717   1.00 12.11 ?  118 GLN   A C    1 
ATOM   2444 O O    . GLN   A 1 118 ? 31.544 -12.948 9.491   1.00 13.76 ?  118 GLN   A O    1 
ATOM   2445 C CB   . GLN   A 1 118 ? 31.949 -12.900 6.609   1.00 12.12 ?  118 GLN   A CB   1 
ATOM   2446 C CG   . GLN   A 1 118 ? 32.427 -13.480 5.290   1.00 12.28 ?  118 GLN   A CG   1 
ATOM   2447 C CD   . GLN   A 1 118 ? 33.241 -14.745 5.470   1.00 12.58 ?  118 GLN   A CD   1 
ATOM   2448 O OE1  . GLN   A 1 118 ? 34.101 -14.824 6.354   1.00 13.42 ?  118 GLN   A OE1  1 
ATOM   2449 N NE2  . GLN   A 1 118 ? 32.982 -15.740 4.624   1.00 12.62 ?  118 GLN   A NE2  1 
ATOM   2450 H H    . GLN   A 1 118 ? 29.595 -13.401 5.984   1.00 13.97 ?  118 GLN   A H    1 
ATOM   2451 H HA   . GLN   A 1 118 ? 31.399 -14.663 7.486   1.00 14.69 ?  118 GLN   A HA   1 
ATOM   2452 H HB2  . GLN   A 1 118 ? 31.520 -12.052 6.424   1.00 14.55 ?  118 GLN   A HB2  1 
ATOM   2453 H HB3  . GLN   A 1 118 ? 32.727 -12.762 7.173   1.00 14.55 ?  118 GLN   A HB3  1 
ATOM   2454 H HG2  . GLN   A 1 118 ? 31.660 -13.689 4.734   1.00 14.76 ?  118 GLN   A HG2  1 
ATOM   2455 H HG3  . GLN   A 1 118 ? 32.992 -12.829 4.841   1.00 14.76 ?  118 GLN   A HG3  1 
ATOM   2456 H HE21 . GLN   A 1 118 ? 32.373 -15.644 4.016   1.00 15.16 ?  118 GLN   A HE21 1 
ATOM   2457 H HE22 . GLN   A 1 118 ? 33.409 -16.482 4.682   1.00 15.16 ?  118 GLN   A HE22 1 
ATOM   2458 N N    . HIS   A 1 119 ? 29.343 -13.098 9.043   1.00 11.65 ?  119 HIS   A N    1 
ATOM   2459 C CA   . HIS   A 1 119 ? 28.894 -12.493 10.293  1.00 12.39 ?  119 HIS   A CA   1 
ATOM   2460 C C    . HIS   A 1 119 ? 27.765 -13.322 10.875  1.00 12.24 ?  119 HIS   A C    1 
ATOM   2461 O O    . HIS   A 1 119 ? 26.806 -13.645 10.171  1.00 12.79 ?  119 HIS   A O    1 
ATOM   2462 C CB   . HIS   A 1 119 ? 28.434 -11.059 10.028  1.00 12.69 ?  119 HIS   A CB   1 
ATOM   2463 C CG   . HIS   A 1 119 ? 29.509 -10.242 9.412   1.00 14.30 ?  119 HIS   A CG   1 
ATOM   2464 N ND1  . HIS   A 1 119 ? 30.490 -9.639  10.164  1.00 16.56 ?  119 HIS   A ND1  1 
ATOM   2465 C CD2  . HIS   A 1 119 ? 29.840 -10.040 8.117   1.00 15.32 ?  119 HIS   A CD2  1 
ATOM   2466 C CE1  . HIS   A 1 119 ? 31.352 -9.050  9.355   1.00 17.11 ?  119 HIS   A CE1  1 
ATOM   2467 N NE2  . HIS   A 1 119 ? 30.989 -9.289  8.108   1.00 16.77 ?  119 HIS   A NE2  1 
ATOM   2468 H H    . HIS   A 1 119 ? 28.693 -13.363 8.544   1.00 14.00 ?  119 HIS   A H    1 
ATOM   2469 H HA   . HIS   A 1 119 ? 29.630 -12.479 10.928  1.00 14.88 ?  119 HIS   A HA   1 
ATOM   2470 H HB2  . HIS   A 1 119 ? 27.677 -11.081 9.424   1.00 15.24 ?  119 HIS   A HB2  1 
ATOM   2471 H HB3  . HIS   A 1 119 ? 28.183 -10.652 10.871  1.00 15.24 ?  119 HIS   A HB3  1 
ATOM   2472 H HD2  . HIS   A 1 119 ? 29.375 -10.352 7.372   1.00 18.40 ?  119 HIS   A HD2  1 
ATOM   2473 H HE1  . HIS   A 1 119 ? 32.089 -8.549  9.617   1.00 20.55 ?  119 HIS   A HE1  1 
ATOM   2474 H HE2  . HIS   A 1 119 ? 31.385 -8.992  7.404   1.00 20.13 ?  119 HIS   A HE2  1 
ATOM   2475 N N    . GLU   A 1 120 ? 27.871 -13.654 12.161  1.00 13.08 ?  120 GLU   A N    1 
ATOM   2476 C CA   . GLU   A 1 120 ? 26.918 -14.596 12.746  1.00 15.87 ?  120 GLU   A CA   1 
ATOM   2477 C C    . GLU   A 1 120 ? 25.503 -14.030 12.830  1.00 13.83 ?  120 GLU   A C    1 
ATOM   2478 O O    . GLU   A 1 120 ? 24.525 -14.791 12.722  1.00 14.00 ?  120 GLU   A O    1 
ATOM   2479 C CB   . GLU   A 1 120 ? 27.397 -15.032 14.134  1.00 23.67 ?  120 GLU   A CB   1 
ATOM   2480 C CG   . GLU   A 1 120 ? 28.605 -15.957 14.118  1.00 34.42 ?  120 GLU   A CG   1 
ATOM   2481 C CD   . GLU   A 1 120 ? 28.804 -16.665 15.445  1.00 44.33 ?  120 GLU   A CD   1 
ATOM   2482 O OE1  . GLU   A 1 120 ? 28.378 -16.114 16.483  1.00 46.42 ?  120 GLU   A OE1  1 
ATOM   2483 O OE2  . GLU   A 1 120 ? 29.379 -17.773 15.451  1.00 51.36 -1 120 GLU   A OE2  1 
ATOM   2484 H H    . GLU   A 1 120 ? 28.478 -13.363 12.704  1.00 15.71 ?  120 GLU   A H    1 
ATOM   2485 H HA   . GLU   A 1 120 ? 26.886 -15.388 12.189  1.00 19.06 ?  120 GLU   A HA   1 
ATOM   2486 H HB2  . GLU   A 1 120 ? 27.641 -14.248 14.650  1.00 28.42 ?  120 GLU   A HB2  1 
ATOM   2487 H HB3  . GLU   A 1 120 ? 26.677 -15.506 14.582  1.00 28.42 ?  120 GLU   A HB3  1 
ATOM   2488 H HG2  . GLU   A 1 120 ? 28.488 -16.626 13.423  1.00 41.31 ?  120 GLU   A HG2  1 
ATOM   2489 H HG3  . GLU   A 1 120 ? 29.406 -15.438 13.947  1.00 41.31 ?  120 GLU   A HG3  1 
ATOM   2490 N N    . VAL   A 1 121 ? 25.378 -12.721 13.063  1.00 13.17 ?  121 VAL   A N    1 
ATOM   2491 C CA   . VAL   A 1 121 ? 24.092 -12.045 13.210  1.00 13.30 ?  121 VAL   A CA   1 
ATOM   2492 C C    . VAL   A 1 121 ? 24.200 -10.662 12.575  1.00 12.29 ?  121 VAL   A C    1 
ATOM   2493 O O    . VAL   A 1 121 ? 25.176 -9.944  12.809  1.00 13.09 ?  121 VAL   A O    1 
ATOM   2494 C CB   . VAL   A 1 121 ? 23.686 -11.897 14.695  1.00 16.42 ?  121 VAL   A CB   1 
ATOM   2495 C CG1  . VAL   A 1 121 ? 22.318 -11.234 14.816  1.00 17.22 ?  121 VAL   A CG1  1 
ATOM   2496 C CG2  . VAL   A 1 121 ? 23.686 -13.233 15.415  1.00 18.60 ?  121 VAL   A CG2  1 
ATOM   2497 H H    . VAL   A 1 121 ? 26.049 -12.185 13.144  1.00 15.82 ?  121 VAL   A H    1 
ATOM   2498 H HA   . VAL   A 1 121 ? 23.407 -12.550 12.750  1.00 15.97 ?  121 VAL   A HA   1 
ATOM   2499 H HB   . VAL   A 1 121 ? 24.327 -11.323 15.139  1.00 19.72 ?  121 VAL   A HB   1 
ATOM   2500 H HG11 . VAL   A 1 121 ? 22.017 -11.298 15.737  1.00 20.68 ?  121 VAL   A HG11 1 
ATOM   2501 H HG12 . VAL   A 1 121 ? 22.392 -10.301 14.560  1.00 20.68 ?  121 VAL   A HG12 1 
ATOM   2502 H HG13 . VAL   A 1 121 ? 21.692 -11.690 14.233  1.00 20.68 ?  121 VAL   A HG13 1 
ATOM   2503 H HG21 . VAL   A 1 121 ? 23.360 -13.106 16.325  1.00 22.34 ?  121 VAL   A HG21 1 
ATOM   2504 H HG22 . VAL   A 1 121 ? 23.099 -13.850 14.945  1.00 22.34 ?  121 VAL   A HG22 1 
ATOM   2505 H HG23 . VAL   A 1 121 ? 24.587 -13.586 15.437  1.00 22.34 ?  121 VAL   A HG23 1 
ATOM   2506 N N    . LEU   A 1 122 ? 23.183 -10.266 11.803  1.00 12.02 ?  122 LEU   A N    1 
ATOM   2507 C CA   . LEU   A 1 122 ? 23.181 -8.963  11.142  1.00 11.77 ?  122 LEU   A CA   1 
ATOM   2508 C C    . LEU   A 1 122 ? 21.784 -8.370  11.097  1.00 11.68 ?  122 LEU   A C    1 
ATOM   2509 O O    . LEU   A 1 122 ? 20.793 -9.089  10.965  1.00 13.03 ?  122 LEU   A O    1 
ATOM   2510 C CB   . LEU   A 1 122 ? 23.595 -9.037  9.667   1.00 13.83 ?  122 LEU   A CB   1 
ATOM   2511 C CG   . LEU   A 1 122 ? 24.787 -9.896  9.269   1.00 13.58 ?  122 LEU   A CG   1 
ATOM   2512 C CD1  . LEU   A 1 122 ? 24.364 -11.338 9.045   1.00 14.17 ?  122 LEU   A CD1  1 
ATOM   2513 C CD2  . LEU   A 1 122 ? 25.436 -9.329  8.018   1.00 13.12 ?  122 LEU   A CD2  1 
ATOM   2514 H H    . LEU   A 1 122 ? 22.481 -10.739 11.644  1.00 14.44 ?  122 LEU   A H    1 
ATOM   2515 H HA   . LEU   A 1 122 ? 23.771 -8.351  11.607  1.00 14.13 ?  122 LEU   A HA   1 
ATOM   2516 H HB2  . LEU   A 1 122 ? 22.846 -9.368  9.160   1.00 16.61 ?  122 LEU   A HB2  1 
ATOM   2517 H HB3  . LEU   A 1 122 ? 23.805 -8.135  9.374   1.00 16.61 ?  122 LEU   A HB3  1 
ATOM   2518 H HG   . LEU   A 1 122 ? 25.457 -9.881  9.976   1.00 16.31 ?  122 LEU   A HG   1 
ATOM   2519 H HD11 . LEU   A 1 122 ? 25.129 -11.850 8.738   1.00 17.01 ?  122 LEU   A HD11 1 
ATOM   2520 H HD12 . LEU   A 1 122 ? 24.040 -11.701 9.883   1.00 17.01 ?  122 LEU   A HD12 1 
ATOM   2521 H HD13 . LEU   A 1 122 ? 23.662 -11.357 8.379   1.00 17.01 ?  122 LEU   A HD13 1 
ATOM   2522 H HD21 . LEU   A 1 122 ? 26.173 -9.907  7.745   1.00 15.76 ?  122 LEU   A HD21 1 
ATOM   2523 H HD22 . LEU   A 1 122 ? 24.777 -9.287  7.308   1.00 15.76 ?  122 LEU   A HD22 1 
ATOM   2524 H HD23 . LEU   A 1 122 ? 25.777 -8.439  8.206   1.00 15.76 ?  122 LEU   A HD23 1 
ATOM   2525 N N    A LEU   A 1 123 ? 21.725 -7.044  11.209  0.78 11.17 ?  123 LEU   A N    1 
ATOM   2526 N N    B LEU   A 1 123 ? 21.733 -7.039  11.165  0.22 11.77 ?  123 LEU   A N    1 
ATOM   2527 C CA   A LEU   A 1 123 ? 20.558 -6.242  10.846  0.78 11.22 ?  123 LEU   A CA   1 
ATOM   2528 C CA   B LEU   A 1 123 ? 20.540 -6.253  10.870  0.22 11.93 ?  123 LEU   A CA   1 
ATOM   2529 C C    A LEU   A 1 123 ? 20.788 -5.706  9.440   0.78 10.33 ?  123 LEU   A C    1 
ATOM   2530 C C    B LEU   A 1 123 ? 20.741 -5.625  9.496   0.22 11.63 ?  123 LEU   A C    1 
ATOM   2531 O O    A LEU   A 1 123 ? 21.853 -5.147  9.169   0.78 10.32 ?  123 LEU   A O    1 
ATOM   2532 O O    B LEU   A 1 123 ? 21.645 -4.802  9.320   0.22 11.55 ?  123 LEU   A O    1 
ATOM   2533 C CB   A LEU   A 1 123 ? 20.431 -5.060  11.805  0.78 11.77 ?  123 LEU   A CB   1 
ATOM   2534 C CB   B LEU   A 1 123 ? 20.364 -5.158  11.923  0.22 12.34 ?  123 LEU   A CB   1 
ATOM   2535 C CG   A LEU   A 1 123 ? 19.354 -4.020  11.488  0.78 12.79 ?  123 LEU   A CG   1 
ATOM   2536 C CG   B LEU   A 1 123 ? 19.412 -4.007  11.575  0.22 12.38 ?  123 LEU   A CG   1 
ATOM   2537 C CD1  A LEU   A 1 123 ? 17.965 -4.642  11.501  0.78 13.72 ?  123 LEU   A CD1  1 
ATOM   2538 C CD1  B LEU   A 1 123 ? 17.966 -4.483  11.527  0.22 12.63 ?  123 LEU   A CD1  1 
ATOM   2539 C CD2  A LEU   A 1 123 ? 19.430 -2.859  12.472  0.78 13.32 ?  123 LEU   A CD2  1 
ATOM   2540 C CD2  B LEU   A 1 123 ? 19.578 -2.856  12.555  0.22 12.50 ?  123 LEU   A CD2  1 
ATOM   2541 H H    A LEU   A 1 123 ? 22.381 -6.565  11.495  0.78 13.42 ?  123 LEU   A H    1 
ATOM   2542 H H    B LEU   A 1 123 ? 22.409 -6.549  11.375  0.22 14.13 ?  123 LEU   A H    1 
ATOM   2543 H HA   A LEU   A 1 123 ? 19.752 -6.784  10.862  0.78 13.48 ?  123 LEU   A HA   1 
ATOM   2544 H HA   B LEU   A 1 123 ? 19.751 -6.817  10.854  0.22 14.33 ?  123 LEU   A HA   1 
ATOM   2545 H HB2  A LEU   A 1 123 ? 20.232 -5.412  12.684  0.78 14.13 ?  123 LEU   A HB2  1 
ATOM   2546 H HB2  B LEU   A 1 123 ? 20.027 -5.571  12.735  0.22 14.82 ?  123 LEU   A HB2  1 
ATOM   2547 H HB3  A LEU   A 1 123 ? 21.275 -4.594  11.823  0.78 14.13 ?  123 LEU   A HB3  1 
ATOM   2548 H HB3  B LEU   A 1 123 ? 21.233 -4.765  12.102  0.22 14.82 ?  123 LEU   A HB3  1 
ATOM   2549 H HG   A LEU   A 1 123 ? 19.502 -3.659  10.598  0.78 15.36 ?  123 LEU   A HG   1 
ATOM   2550 H HG   B LEU   A 1 123 ? 19.632 -3.661  10.697  0.22 14.87 ?  123 LEU   A HG   1 
ATOM   2551 H HD11 A LEU   A 1 123 ? 17.300 -3.949  11.346  0.78 16.48 ?  123 LEU   A HD11 1 
ATOM   2552 H HD11 B LEU   A 1 123 ? 17.392 -3.732  11.305  0.22 15.17 ?  123 LEU   A HD11 1 
ATOM   2553 H HD12 A LEU   A 1 123 ? 17.907 -5.312  10.801  0.78 16.48 ?  123 LEU   A HD12 1 
ATOM   2554 H HD12 B LEU   A 1 123 ? 17.881 -5.175  10.851  0.22 15.17 ?  123 LEU   A HD12 1 
ATOM   2555 H HD13 A LEU   A 1 123 ? 17.810 -5.056  12.366  0.78 16.48 ?  123 LEU   A HD13 1 
ATOM   2556 H HD13 B LEU   A 1 123 ? 17.721 -4.840  12.396  0.22 15.17 ?  123 LEU   A HD13 1 
ATOM   2557 H HD21 A LEU   A 1 123 ? 18.739 -2.213  12.258  0.78 16.00 ?  123 LEU   A HD21 1 
ATOM   2558 H HD21 B LEU   A 1 123 ? 18.964 -2.146  12.312  0.22 15.01 ?  123 LEU   A HD21 1 
ATOM   2559 H HD22 A LEU   A 1 123 ? 19.291 -3.203  13.371  0.78 16.00 ?  123 LEU   A HD22 1 
ATOM   2560 H HD22 B LEU   A 1 123 ? 19.382 -3.174  13.450  0.22 15.01 ?  123 LEU   A HD22 1 
ATOM   2561 H HD23 A LEU   A 1 123 ? 20.304 -2.449  12.406  0.78 16.00 ?  123 LEU   A HD23 1 
ATOM   2562 H HD23 B LEU   A 1 123 ? 20.492 -2.535  12.509  0.22 15.01 ?  123 LEU   A HD23 1 
ATOM   2563 N N    A ALA   A 1 124 ? 19.796 -5.840  8.556   0.78 10.35 ?  124 ALA   A N    1 
ATOM   2564 N N    B ALA   A 1 124 ? 19.904 -5.999  8.530   0.22 11.62 ?  124 ALA   A N    1 
ATOM   2565 C CA   A ALA   A 1 124 ? 20.062 -5.556  7.152   0.78 10.35 ?  124 ALA   A CA   1 
ATOM   2566 C CA   B ALA   A 1 124 ? 20.143 -5.644  7.139   0.22 11.84 ?  124 ALA   A CA   1 
ATOM   2567 C C    A ALA   A 1 124 ? 18.819 -5.102  6.404   0.78 10.37 ?  124 ALA   A C    1 
ATOM   2568 C C    B ALA   A 1 124 ? 18.874 -5.158  6.457   0.22 11.70 ?  124 ALA   A C    1 
ATOM   2569 O O    A ALA   A 1 124 ? 17.691 -5.464  6.773   0.78 11.34 ?  124 ALA   A O    1 
ATOM   2570 O O    B ALA   A 1 124 ? 17.762 -5.517  6.864   0.22 11.67 ?  124 ALA   A O    1 
ATOM   2571 C CB   A ALA   A 1 124 ? 20.637 -6.791  6.443   0.78 11.04 ?  124 ALA   A CB   1 
ATOM   2572 C CB   B ALA   A 1 124 ? 20.685 -6.848  6.354   0.22 12.10 ?  124 ALA   A CB   1 
ATOM   2573 H H    A ALA   A 1 124 ? 18.985 -6.073  8.735   0.78 12.44 ?  124 ALA   A H    1 
ATOM   2574 H H    B ALA   A 1 124 ? 19.193 -6.463  8.654   0.22 13.96 ?  124 ALA   A H    1 
ATOM   2575 H HA   A ALA   A 1 124 ? 20.733 -4.858  7.107   0.78 12.44 ?  124 ALA   A HA   1 
ATOM   2576 H HA   B ALA   A 1 124 ? 20.803 -4.940  7.103   0.22 14.22 ?  124 ALA   A HA   1 
ATOM   2577 H HB1  A ALA   A 1 124 ? 20.817 -6.579  5.511   0.78 13.26 ?  124 ALA   A HB1  1 
ATOM   2578 H HB1  B ALA   A 1 124 ? 20.835 -6.585  5.433   0.22 14.53 ?  124 ALA   A HB1  1 
ATOM   2579 H HB2  A ALA   A 1 124 ? 21.474 -7.056  6.876   0.78 13.26 ?  124 ALA   A HB2  1 
ATOM   2580 H HB2  B ALA   A 1 124 ? 21.521 -7.135  6.756   0.22 14.53 ?  124 ALA   A HB2  1 
ATOM   2581 H HB3  A ALA   A 1 124 ? 20.004 -7.523  6.497   0.78 13.26 ?  124 ALA   A HB3  1 
ATOM   2582 H HB3  B ALA   A 1 124 ? 20.037 -7.569  6.391   0.22 14.53 ?  124 ALA   A HB3  1 
ATOM   2583 N N    A PRO   A 1 125 ? 19.005 -4.350  5.322   0.78 10.35 ?  125 PRO   A N    1 
ATOM   2584 N N    B PRO   A 1 125 ? 19.016 -4.335  5.405   0.22 11.74 ?  125 PRO   A N    1 
ATOM   2585 C CA   A PRO   A 1 125 ? 17.941 -4.098  4.352   0.78 10.81 ?  125 PRO   A CA   1 
ATOM   2586 C CA   B PRO   A 1 125 ? 17.881 -4.042  4.524   0.22 11.76 ?  125 PRO   A CA   1 
ATOM   2587 C C    A PRO   A 1 125 ? 17.993 -5.166  3.265   0.78 10.55 ?  125 PRO   A C    1 
ATOM   2588 C C    B PRO   A 1 125 ? 17.852 -5.026  3.369   0.22 11.34 ?  125 PRO   A C    1 
ATOM   2589 O O    A PRO   A 1 125 ? 18.967 -5.909  3.135   0.78 10.95 ?  125 PRO   A O    1 
ATOM   2590 O O    B PRO   A 1 125 ? 18.702 -5.919  3.301   0.22 11.55 ?  125 PRO   A O    1 
ATOM   2591 C CB   A PRO   A 1 125 ? 18.379 -2.753  3.762   0.78 10.53 ?  125 PRO   A CB   1 
ATOM   2592 C CB   B PRO   A 1 125 ? 18.203 -2.630  4.027   0.22 12.12 ?  125 PRO   A CB   1 
ATOM   2593 C CG   A PRO   A 1 125 ? 19.894 -2.914  3.665   0.78 10.48 ?  125 PRO   A CG   1 
ATOM   2594 C CG   B PRO   A 1 125 ? 19.700 -2.651  3.908   0.22 12.31 ?  125 PRO   A CG   1 
ATOM   2595 C CD   A PRO   A 1 125 ? 20.280 -3.737  4.892   0.78 10.67 ?  125 PRO   A CD   1 
ATOM   2596 C CD   B PRO   A 1 125 ? 20.208 -3.558  5.019   0.22 12.05 ?  125 PRO   A CD   1 
ATOM   2597 H HA   A PRO   A 1 125 ? 17.062 -4.049  4.767   0.78 12.98 ?  125 PRO   A HA   1 
ATOM   2598 H HA   B PRO   A 1 125 ? 17.037 -4.053  5.001   0.22 14.13 ?  125 PRO   A HA   1 
ATOM   2599 H HB2  A PRO   A 1 125 ? 17.979 -2.629  2.887   0.78 12.65 ?  125 PRO   A HB2  1 
ATOM   2600 H HB2  B PRO   A 1 125 ? 17.786 -2.473  3.164   0.22 14.56 ?  125 PRO   A HB2  1 
ATOM   2601 H HB3  A PRO   A 1 125 ? 18.136 -2.034  4.365   0.78 12.65 ?  125 PRO   A HB3  1 
ATOM   2602 H HB3  B PRO   A 1 125 ? 17.913 -1.973  4.680   0.22 14.56 ?  125 PRO   A HB3  1 
ATOM   2603 H HG2  A PRO   A 1 125 ? 20.124 -3.389  2.850   0.78 12.59 ?  125 PRO   A HG2  1 
ATOM   2604 H HG2  B PRO   A 1 125 ? 19.948 -3.006  3.040   0.22 14.78 ?  125 PRO   A HG2  1 
ATOM   2605 H HG3  A PRO   A 1 125 ? 20.319 -2.045  3.688   0.78 12.59 ?  125 PRO   A HG3  1 
ATOM   2606 H HG3  B PRO   A 1 125 ? 20.046 -1.754  4.019   0.22 14.78 ?  125 PRO   A HG3  1 
ATOM   2607 H HD2  A PRO   A 1 125 ? 20.929 -4.419  4.650   0.78 12.82 ?  125 PRO   A HD2  1 
ATOM   2608 H HD2  B PRO   A 1 125 ? 20.904 -4.145  4.681   0.22 14.47 ?  125 PRO   A HD2  1 
ATOM   2609 H HD3  A PRO   A 1 125 ? 20.623 -3.155  5.589   0.78 12.82 ?  125 PRO   A HD3  1 
ATOM   2610 H HD3  B PRO   A 1 125 ? 20.521 -3.030  5.768   0.22 14.47 ?  125 PRO   A HD3  1 
ATOM   2611 N N    A LEU   A 1 126 ? 16.934 -5.216  2.462   0.78 10.61 ?  126 LEU   A N    1 
ATOM   2612 N N    B LEU   A 1 126 ? 16.903 -4.874  2.448   0.22 11.03 ?  126 LEU   A N    1 
ATOM   2613 C CA   A LEU   A 1 126 ? 16.962 -6.042  1.262   0.78 11.28 ?  126 LEU   A CA   1 
ATOM   2614 C CA   B LEU   A 1 126 ? 16.824 -5.740  1.276   0.22 10.48 ?  126 LEU   A CA   1 
ATOM   2615 C C    A LEU   A 1 126 ? 17.899 -5.419  0.229   0.78 11.41 ?  126 LEU   A C    1 
ATOM   2616 C C    B LEU   A 1 126 ? 17.726 -5.181  0.180   0.22 9.97  ?  126 LEU   A C    1 
ATOM   2617 O O    A LEU   A 1 126 ? 17.708 -4.277  -0.200  0.78 12.00 ?  126 LEU   A O    1 
ATOM   2618 O O    B LEU   A 1 126 ? 17.401 -4.166  -0.446  0.22 10.21 ?  126 LEU   A O    1 
ATOM   2619 C CB   A LEU   A 1 126 ? 15.562 -6.205  0.685   0.78 11.85 ?  126 LEU   A CB   1 
ATOM   2620 C CB   B LEU   A 1 126 ? 15.384 -5.850  0.792   0.22 10.82 ?  126 LEU   A CB   1 
ATOM   2621 C CG   A LEU   A 1 126 ? 14.646 -7.197  1.410   0.78 13.12 ?  126 LEU   A CG   1 
ATOM   2622 C CG   B LEU   A 1 126 ? 14.511 -6.776  1.632   0.22 10.65 ?  126 LEU   A CG   1 
ATOM   2623 C CD1  A LEU   A 1 126 ? 13.228 -7.082  0.881   0.78 14.70 ?  126 LEU   A CD1  1 
ATOM   2624 C CD1  B LEU   A 1 126 ? 13.078 -6.681  1.162   0.22 10.73 ?  126 LEU   A CD1  1 
ATOM   2625 C CD2  A LEU   A 1 126 ? 15.140 -8.631  1.260   0.78 12.88 ?  126 LEU   A CD2  1 
ATOM   2626 C CD2  B LEU   A 1 126 ? 15.006 -8.214  1.543   0.22 10.60 ?  126 LEU   A CD2  1 
ATOM   2627 H H    A LEU   A 1 126 ? 16.197 -4.788  2.586   0.78 12.75 ?  126 LEU   A H    1 
ATOM   2628 H H    B LEU   A 1 126 ? 16.279 -4.274  2.482   0.22 13.25 ?  126 LEU   A H    1 
ATOM   2629 H HA   A LEU   A 1 126 ? 17.304 -6.920  1.485   0.78 13.55 ?  126 LEU   A HA   1 
ATOM   2630 H HA   B LEU   A 1 126 ? 17.140 -6.626  1.514   0.22 12.59 ?  126 LEU   A HA   1 
ATOM   2631 H HB2  A LEU   A 1 126 ? 15.115 -5.345  0.711   0.78 14.23 ?  126 LEU   A HB2  1 
ATOM   2632 H HB2  B LEU   A 1 126 ? 14.980 -4.968  0.813   0.22 13.00 ?  126 LEU   A HB2  1 
ATOM   2633 H HB3  A LEU   A 1 126 ? 15.635 -6.506  -0.230  0.78 14.23 ?  126 LEU   A HB3  1 
ATOM   2634 H HB3  B LEU   A 1 126 ? 15.384 -6.189  -0.116  0.22 13.00 ?  126 LEU   A HB3  1 
ATOM   2635 H HG   A LEU   A 1 126 ? 14.627 -6.990  2.358   0.78 15.76 ?  126 LEU   A HG   1 
ATOM   2636 H HG   B LEU   A 1 126 ? 14.546 -6.499  2.563   0.22 12.79 ?  126 LEU   A HG   1 
ATOM   2637 H HD11 A LEU   A 1 126 ? 12.660 -7.719  1.346   0.78 17.66 ?  126 LEU   A HD11 1 
ATOM   2638 H HD11 B LEU   A 1 126 ? 12.532 -7.279  1.694   0.22 12.89 ?  126 LEU   A HD11 1 
ATOM   2639 H HD12 A LEU   A 1 126 ? 12.908 -6.180  1.036   0.78 17.66 ?  126 LEU   A HD12 1 
ATOM   2640 H HD12 B LEU   A 1 126 ? 12.774 -5.768  1.266   0.22 12.89 ?  126 LEU   A HD12 1 
ATOM   2641 H HD13 A LEU   A 1 126 ? 13.230 -7.275  -0.070  0.78 17.66 ?  126 LEU   A HD13 1 
ATOM   2642 H HD13 B LEU   A 1 126 ? 13.040 -6.940  0.227   0.22 12.89 ?  126 LEU   A HD13 1 
ATOM   2643 H HD21 A LEU   A 1 126 ? 14.480 -9.239  1.625   0.78 15.47 ?  126 LEU   A HD21 1 
ATOM   2644 H HD21 B LEU   A 1 126 ? 14.314 -8.808  1.866   0.22 12.73 ?  126 LEU   A HD21 1 
ATOM   2645 H HD22 A LEU   A 1 126 ? 15.280 -8.819  0.318   0.78 15.47 ?  126 LEU   A HD22 1 
ATOM   2646 H HD22 B LEU   A 1 126 ? 15.213 -8.417  0.616   0.22 12.73 ?  126 LEU   A HD22 1 
ATOM   2647 H HD23 A LEU   A 1 126 ? 15.980 -8.727  1.741   0.78 15.47 ?  126 LEU   A HD23 1 
ATOM   2648 H HD23 B LEU   A 1 126 ? 15.805 -8.309  2.086   0.22 12.73 ?  126 LEU   A HD23 1 
ATOM   2649 N N    A LEU   A 1 127 ? 18.912 -6.177  -0.174  0.78 10.94 ?  127 LEU   A N    1 
ATOM   2650 N N    B LEU   A 1 127 ? 18.850 -5.852  -0.061  0.22 9.66  ?  127 LEU   A N    1 
ATOM   2651 C CA   A LEU   A 1 127 ? 19.901 -5.674  -1.114  0.78 10.66 ?  127 LEU   A CA   1 
ATOM   2652 C CA   B LEU   A 1 127 ? 19.811 -5.367  -1.042  0.22 9.93  ?  127 LEU   A CA   1 
ATOM   2653 C C    A LEU   A 1 127 ? 19.280 -5.455  -2.487  0.78 10.20 ?  127 LEU   A C    1 
ATOM   2654 C C    B LEU   A 1 127 ? 19.204 -5.333  -2.446  0.22 10.37 ?  127 LEU   A C    1 
ATOM   2655 O O    A LEU   A 1 127 ? 18.461 -6.245  -2.968  0.78 10.45 ?  127 LEU   A O    1 
ATOM   2656 O O    B LEU   A 1 127 ? 18.288 -6.089  -2.781  0.22 10.86 ?  127 LEU   A O    1 
ATOM   2657 C CB   A LEU   A 1 127 ? 21.073 -6.650  -1.226  0.78 10.80 ?  127 LEU   A CB   1 
ATOM   2658 C CB   B LEU   A 1 127 ? 21.062 -6.249  -1.028  0.22 10.22 ?  127 LEU   A CB   1 
ATOM   2659 C CG   A LEU   A 1 127 ? 21.877 -6.889  0.051   0.78 11.05 ?  127 LEU   A CG   1 
ATOM   2660 C CG   B LEU   A 1 127 ? 21.846 -6.276  0.288   0.22 10.26 ?  127 LEU   A CG   1 
ATOM   2661 C CD1  A LEU   A 1 127 ? 22.983 -7.879  -0.224  0.78 11.64 ?  127 LEU   A CD1  1 
ATOM   2662 C CD1  B LEU   A 1 127 ? 23.039 -7.210  0.175   0.22 10.31 ?  127 LEU   A CD1  1 
ATOM   2663 C CD2  A LEU   A 1 127 ? 22.456 -5.588  0.576   0.78 11.78 ?  127 LEU   A CD2  1 
ATOM   2664 C CD2  B LEU   A 1 127 ? 22.292 -4.873  0.682   0.22 10.31 ?  127 LEU   A CD2  1 
ATOM   2665 H H    A LEU   A 1 127 ? 19.047 -6.985  0.090   0.78 13.14 ?  127 LEU   A H    1 
ATOM   2666 H H    B LEU   A 1 127 ? 19.087 -6.580  0.344   0.22 11.61 ?  127 LEU   A H    1 
ATOM   2667 H HA   A LEU   A 1 127 ? 20.240 -4.826  -0.793  0.78 12.81 ?  127 LEU   A HA   1 
ATOM   2668 H HA   B LEU   A 1 127 ? 20.077 -4.463  -0.797  0.22 11.94 ?  127 LEU   A HA   1 
ATOM   2669 H HB2  A LEU   A 1 127 ? 20.727 -7.510  -1.514  0.78 12.98 ?  127 LEU   A HB2  1 
ATOM   2670 H HB2  B LEU   A 1 127 ? 20.796 -7.160  -1.222  0.22 12.28 ?  127 LEU   A HB2  1 
ATOM   2671 H HB3  A LEU   A 1 127 ? 21.688 -6.310  -1.892  0.78 12.98 ?  127 LEU   A HB3  1 
ATOM   2672 H HB3  B LEU   A 1 127 ? 21.667 -5.932  -1.715  0.22 12.28 ?  127 LEU   A HB3  1 
ATOM   2673 H HG   A LEU   A 1 127 ? 21.293 -7.262  0.737   0.78 13.28 ?  127 LEU   A HG   1 
ATOM   2674 H HG   B LEU   A 1 127 ? 21.271 -6.614  0.994   0.22 12.33 ?  127 LEU   A HG   1 
ATOM   2675 H HD11 A LEU   A 1 127 ? 23.471 -8.048  0.600   0.78 13.98 ?  127 LEU   A HD11 1 
ATOM   2676 H HD11 B LEU   A 1 127 ? 23.565 -7.148  0.987   0.22 12.39 ?  127 LEU   A HD11 1 
ATOM   2677 H HD12 A LEU   A 1 127 ? 22.593 -8.708  -0.549  0.78 13.98 ?  127 LEU   A HD12 1 
ATOM   2678 H HD12 B LEU   A 1 127 ? 22.716 -8.118  0.057   0.22 12.39 ?  127 LEU   A HD12 1 
ATOM   2679 H HD13 A LEU   A 1 127 ? 23.578 -7.510  -0.891  0.78 13.98 ?  127 LEU   A HD13 1 
ATOM   2680 H HD13 B LEU   A 1 127 ? 23.573 -6.945  -0.588  0.22 12.39 ?  127 LEU   A HD13 1 
ATOM   2681 H HD21 A LEU   A 1 127 ? 23.079 -5.784  1.292   0.78 14.16 ?  127 LEU   A HD21 1 
ATOM   2682 H HD21 B LEU   A 1 127 ? 22.918 -4.936  1.421   0.22 12.38 ?  127 LEU   A HD21 1 
ATOM   2683 H HD22 A LEU   A 1 127 ? 22.918 -5.137  -0.150  0.78 14.16 ?  127 LEU   A HD22 1 
ATOM   2684 H HD22 B LEU   A 1 127 ? 22.720 -4.455  -0.080  0.22 12.38 ?  127 LEU   A HD22 1 
ATOM   2685 H HD23 A LEU   A 1 127 ? 21.736 -5.028  0.906   0.78 14.16 ?  127 LEU   A HD23 1 
ATOM   2686 H HD23 B LEU   A 1 127 ? 21.515 -4.359  0.951   0.22 12.38 ?  127 LEU   A HD23 1 
ATOM   2687 N N    A SER   A 1 128 ? 19.693 -4.363  -3.117  0.78 10.21 ?  128 SER   A N    1 
ATOM   2688 N N    B SER   A 1 128 ? 19.734 -4.419  -3.262  0.22 10.19 ?  128 SER   A N    1 
ATOM   2689 C CA   A SER   A 1 128 ? 19.286 -3.952  -4.452  0.78 10.46 ?  128 SER   A CA   1 
ATOM   2690 C CA   B SER   A 1 128 ? 19.345 -4.171  -4.652  0.22 9.89  ?  128 SER   A CA   1 
ATOM   2691 C C    A SER   A 1 128 ? 17.831 -3.499  -4.524  0.78 10.83 ?  128 SER   A C    1 
ATOM   2692 C C    B SER   A 1 128 ? 17.912 -3.675  -4.844  0.22 9.95  ?  128 SER   A C    1 
ATOM   2693 O O    A SER   A 1 128 ? 17.350 -3.200  -5.612  0.78 12.04 ?  128 SER   A O    1 
ATOM   2694 O O    B SER   A 1 128 ? 17.540 -3.308  -5.963  0.22 10.52 ?  128 SER   A O    1 
ATOM   2695 C CB   A SER   A 1 128 ? 19.624 -4.986  -5.538  0.78 10.70 ?  128 SER   A CB   1 
ATOM   2696 C CB   B SER   A 1 128 ? 19.644 -5.361  -5.576  0.22 9.88  ?  128 SER   A CB   1 
ATOM   2697 O OG   A SER   A 1 128 ? 21.034 -5.179  -5.621  0.78 11.28 ?  128 SER   A OG   1 
ATOM   2698 O OG   B SER   A 1 128 ? 21.043 -5.532  -5.741  0.22 9.97  ?  128 SER   A OG   1 
ATOM   2699 H H    A SER   A 1 128 ? 20.261 -3.811  -2.770  0.78 12.27 ?  128 SER   A H    1 
ATOM   2700 H H    B SER   A 1 128 ? 20.368 -3.900  -3.008  0.22 12.24 ?  128 SER   A H    1 
ATOM   2701 H HA   A SER   A 1 128 ? 19.815 -3.173  -4.668  0.78 12.56 ?  128 SER   A HA   1 
ATOM   2702 H HA   B SER   A 1 128 ? 19.914 -3.459  -4.960  0.22 11.88 ?  128 SER   A HA   1 
ATOM   2703 H HB2  A SER   A 1 128 ? 19.192 -5.826  -5.327  0.78 12.85 ?  128 SER   A HB2  1 
ATOM   2704 H HB2  B SER   A 1 128 ? 19.268 -6.171  -5.209  0.22 11.87 ?  128 SER   A HB2  1 
ATOM   2705 H HB3  A SER   A 1 128 ? 19.297 -4.655  -6.397  0.78 12.85 ?  128 SER   A HB3  1 
ATOM   2706 H HB3  B SER   A 1 128 ? 19.249 -5.182  -6.454  0.22 11.87 ?  128 SER   A HB3  1 
ATOM   2707 H HG   A SER   A 1 128 ? 21.410 -4.455  -5.806  0.78 13.55 ?  128 SER   A HG   1 
ATOM   2708 H HG   B SER   A 1 128 ? 21.383 -4.836  -6.069  0.22 11.97 ?  128 SER   A HG   1 
ATOM   2709 N N    A ALA   A 1 129 ? 17.137 -3.398  -3.390  0.78 11.27 ?  129 ALA   A N    1 
ATOM   2710 N N    B ALA   A 1 129 ? 17.111 -3.636  -3.781  0.22 9.93  ?  129 ALA   A N    1 
ATOM   2711 C CA   A ALA   A 1 129 ? 15.776 -2.888  -3.366  0.78 11.47 ?  129 ALA   A CA   1 
ATOM   2712 C CA   B ALA   A 1 129 ? 15.754 -3.115  -3.866  0.22 10.33 ?  129 ALA   A CA   1 
ATOM   2713 C C    A ALA   A 1 129 ? 15.781 -1.358  -3.370  0.78 11.04 ?  129 ALA   A C    1 
ATOM   2714 C C    B ALA   A 1 129 ? 15.787 -1.590  -3.752  0.22 10.87 ?  129 ALA   A C    1 
ATOM   2715 O O    A ALA   A 1 129 ? 16.828 -0.708  -3.468  0.78 11.39 ?  129 ALA   A O    1 
ATOM   2716 O O    B ALA   A 1 129 ? 16.850 -0.963  -3.749  0.22 10.78 ?  129 ALA   A O    1 
ATOM   2717 C CB   A ALA   A 1 129 ? 15.021 -3.450  -2.160  0.78 12.74 ?  129 ALA   A CB   1 
ATOM   2718 C CB   B ALA   A 1 129 ? 14.867 -3.782  -2.815  0.22 10.31 ?  129 ALA   A CB   1 
ATOM   2719 H H    A ALA   A 1 129 ? 17.440 -3.619  -2.611  0.78 13.54 ?  129 ALA   A H    1 
ATOM   2720 H H    B ALA   A 1 129 ? 17.323 -3.906  -2.993  0.22 11.92 ?  129 ALA   A H    1 
ATOM   2721 H HA   A ALA   A 1 129 ? 15.319 -3.188  -4.163  0.78 13.78 ?  129 ALA   A HA   1 
ATOM   2722 H HA   B ALA   A 1 129 ? 15.390 -3.337  -4.735  0.22 12.41 ?  129 ALA   A HA   1 
ATOM   2723 H HB1  A ALA   A 1 129 ? 14.109 -3.111  -2.170  0.78 15.31 ?  129 ALA   A HB1  1 
ATOM   2724 H HB1  B ALA   A 1 129 ? 13.967 -3.425  -2.889  0.22 12.39 ?  129 ALA   A HB1  1 
ATOM   2725 H HB2  A ALA   A 1 129 ? 15.008 -4.419  -2.215  0.78 15.31 ?  129 ALA   A HB2  1 
ATOM   2726 H HB2  B ALA   A 1 129 ? 14.856 -4.739  -2.970  0.22 12.39 ?  129 ALA   A HB2  1 
ATOM   2727 H HB3  A ALA   A 1 129 ? 15.465 -3.172  -1.344  0.78 15.31 ?  129 ALA   A HB3  1 
ATOM   2728 H HB3  B ALA   A 1 129 ? 15.225 -3.594  -1.933  0.22 12.39 ?  129 ALA   A HB3  1 
ATOM   2729 N N    A GLY   A 1 130 ? 14.590 -0.776  -3.276  0.78 12.00 ?  130 GLY   A N    1 
ATOM   2730 N N    B GLY   A 1 130 ? 14.610 -0.972  -3.672  0.22 11.03 ?  130 GLY   A N    1 
ATOM   2731 C CA   A GLY   A 1 130 ? 14.491 0.672   -3.267  0.78 12.95 ?  130 GLY   A CA   1 
ATOM   2732 C CA   B GLY   A 1 130 ? 14.553 0.475   -3.548  0.22 11.65 ?  130 GLY   A CA   1 
ATOM   2733 C C    A GLY   A 1 130 ? 15.112 1.270   -4.511  0.78 12.20 ?  130 GLY   A C    1 
ATOM   2734 C C    B GLY   A 1 130 ? 15.073 1.150   -4.803  0.22 11.97 ?  130 GLY   A C    1 
ATOM   2735 O O    A GLY   A 1 130 ? 14.876 0.809   -5.631  0.78 12.28 ?  130 GLY   A O    1 
ATOM   2736 O O    B GLY   A 1 130 ? 14.762 0.748   -5.929  0.22 12.12 ?  130 GLY   A O    1 
ATOM   2737 H H    A GLY   A 1 130 ? 13.837 -1.189  -3.211  0.78 14.42 ?  130 GLY   A H    1 
ATOM   2738 H H    B GLY   A 1 130 ? 13.847 -1.362  -3.692  0.22 13.26 ?  130 GLY   A H    1 
ATOM   2739 H HA2  A GLY   A 1 130 ? 13.553 0.931   -3.225  0.78 15.55 ?  130 GLY   A HA2  1 
ATOM   2740 H HA2  B GLY   A 1 130 ? 13.631 0.749   -3.382  0.22 13.99 ?  130 GLY   A HA2  1 
ATOM   2741 H HA3  A GLY   A 1 130 ? 14.946 1.026   -2.494  0.78 15.55 ?  130 GLY   A HA3  1 
ATOM   2742 H HA3  B GLY   A 1 130 ? 15.094 0.764   -2.799  0.22 13.99 ?  130 GLY   A HA3  1 
ATOM   2743 N N    A ILE   A 1 131 ? 15.917 2.320   -4.314  0.78 12.29 ?  131 ILE   A N    1 
ATOM   2744 N N    B ILE   A 1 131 ? 15.887 2.190   -4.612  0.22 12.49 ?  131 ILE   A N    1 
ATOM   2745 C CA   A ILE   A 1 131 ? 16.486 3.063   -5.436  0.78 11.96 ?  131 ILE   A CA   1 
ATOM   2746 C CA   B ILE   A 1 131 ? 16.420 2.961   -5.734  0.22 12.90 ?  131 ILE   A CA   1 
ATOM   2747 C C    A ILE   A 1 131 ? 17.497 2.269   -6.250  0.78 11.45 ?  131 ILE   A C    1 
ATOM   2748 C C    B ILE   A 1 131 ? 17.494 2.194   -6.503  0.22 13.08 ?  131 ILE   A C    1 
ATOM   2749 O O    A ILE   A 1 131 ? 17.911 2.744   -7.314  0.78 12.91 ?  131 ILE   A O    1 
ATOM   2750 O O    B ILE   A 1 131 ? 18.016 2.694   -7.507  0.22 13.44 ?  131 ILE   A O    1 
ATOM   2751 C CB   A ILE   A 1 131 ? 17.082 4.420   -5.000  0.78 13.38 ?  131 ILE   A CB   1 
ATOM   2752 C CB   B ILE   A 1 131 ? 16.926 4.350   -5.294  0.22 13.37 ?  131 ILE   A CB   1 
ATOM   2753 C CG1  A ILE   A 1 131 ? 18.360 4.235   -4.171  0.78 15.20 ?  131 ILE   A CG1  1 
ATOM   2754 C CG1  B ILE   A 1 131 ? 18.026 4.224   -4.237  0.22 14.08 ?  131 ILE   A CG1  1 
ATOM   2755 C CG2  A ILE   A 1 131 ? 16.049 5.231   -4.232  0.78 14.27 ?  131 ILE   A CG2  1 
ATOM   2756 C CG2  B ILE   A 1 131 ? 15.769 5.204   -4.780  0.22 12.94 ?  131 ILE   A CG2  1 
ATOM   2757 C CD1  A ILE   A 1 131 ? 19.051 5.548   -3.801  0.78 16.60 ?  131 ILE   A CD1  1 
ATOM   2758 C CD1  B ILE   A 1 131 ? 18.521 5.558   -3.711  0.22 14.64 ?  131 ILE   A CD1  1 
ATOM   2759 H H    A ILE   A 1 131 ? 16.133 2.618   -3.540  0.78 14.76 ?  131 ILE   A H    1 
ATOM   2760 H H    B ILE   A 1 131 ? 16.124 2.481   -3.833  0.22 15.01 ?  131 ILE   A H    1 
ATOM   2761 H HA   A ILE   A 1 131 ? 15.760 3.269   -6.039  0.78 14.37 ?  131 ILE   A HA   1 
ATOM   2762 H HA   B ILE   A 1 131 ? 15.692 3.114   -6.349  0.22 15.50 ?  131 ILE   A HA   1 
ATOM   2763 H HB   A ILE   A 1 131 ? 17.312 4.914   -5.802  0.78 16.07 ?  131 ILE   A HB   1 
ATOM   2764 H HB   B ILE   A 1 131 ? 17.305 4.787   -6.073  0.22 16.06 ?  131 ILE   A HB   1 
ATOM   2765 H HG12 A ILE   A 1 131 ? 18.133 3.774   -3.349  0.78 18.26 ?  131 ILE   A HG12 1 
ATOM   2766 H HG12 B ILE   A 1 131 ? 17.685 3.719   -3.483  0.22 16.91 ?  131 ILE   A HG12 1 
ATOM   2767 H HG13 A ILE   A 1 131 ? 18.994 3.707   -4.680  0.78 18.26 ?  131 ILE   A HG13 1 
ATOM   2768 H HG13 B ILE   A 1 131 ? 18.784 3.760   -4.628  0.22 16.91 ?  131 ILE   A HG13 1 
ATOM   2769 H HG21 A ILE   A 1 131 ? 16.379 6.135   -4.118  0.78 17.14 ?  131 ILE   A HG21 1 
ATOM   2770 H HG21 B ILE   A 1 131 ? 16.086 6.106   -4.617  0.22 15.54 ?  131 ILE   A HG21 1 
ATOM   2771 H HG22 A ILE   A 1 131 ? 15.221 5.241   -4.735  0.78 17.14 ?  131 ILE   A HG22 1 
ATOM   2772 H HG22 B ILE   A 1 131 ? 15.071 5.221   -5.451  0.22 15.54 ?  131 ILE   A HG22 1 
ATOM   2773 H HG23 A ILE   A 1 131 ? 15.905 4.817   -3.366  0.78 17.14 ?  131 ILE   A HG23 1 
ATOM   2774 H HG23 B ILE   A 1 131 ? 15.431 4.816   -3.959  0.22 15.54 ?  131 ILE   A HG23 1 
ATOM   2775 H HD11 A ILE   A 1 131 ? 19.902 5.348   -3.379  0.78 19.93 ?  131 ILE   A HD11 1 
ATOM   2776 H HD11 B ILE   A 1 131 ? 19.335 5.415   -3.206  0.22 17.59 ?  131 ILE   A HD11 1 
ATOM   2777 H HD12 A ILE   A 1 131 ? 19.197 6.068   -4.606  0.78 19.93 ?  131 ILE   A HD12 1 
ATOM   2778 H HD12 B ILE   A 1 131 ? 18.695 6.147   -4.461  0.22 17.59 ?  131 ILE   A HD12 1 
ATOM   2779 H HD13 A ILE   A 1 131 ? 18.487 6.043   -3.186  0.78 19.93 ?  131 ILE   A HD13 1 
ATOM   2780 H HD13 B ILE   A 1 131 ? 17.839 5.945   -3.138  0.22 17.59 ?  131 ILE   A HD13 1 
ATOM   2781 N N    A PHE   A 1 132 ? 17.899 1.072   -5.798  0.78 10.83 ?  132 PHE   A N    1 
ATOM   2782 N N    B PHE   A 1 132 ? 17.834 0.980   -6.052  0.22 12.98 ?  132 PHE   A N    1 
ATOM   2783 C CA   A PHE   A 1 132 ? 18.736 0.209   -6.625  0.78 11.09 ?  132 PHE   A CA   1 
ATOM   2784 C CA   B PHE   A 1 132 ? 18.765 0.143   -6.803  0.22 12.97 ?  132 PHE   A CA   1 
ATOM   2785 C C    A PHE   A 1 132 ? 17.937 -0.552  -7.685  0.78 11.64 ?  132 PHE   A C    1 
ATOM   2786 C C    B PHE   A 1 132 ? 18.103 -0.575  -7.975  0.22 13.13 ?  132 PHE   A C    1 
ATOM   2787 O O    A PHE   A 1 132 ? 18.542 -1.216  -8.532  0.78 12.24 ?  132 PHE   A O    1 
ATOM   2788 O O    B PHE   A 1 132 ? 18.811 -1.050  -8.870  0.22 13.54 ?  132 PHE   A O    1 
ATOM   2789 C CB   A PHE   A 1 132 ? 19.555 -0.769  -5.767  0.78 10.77 ?  132 PHE   A CB   1 
ATOM   2790 C CB   B PHE   A 1 132 ? 19.456 -0.863  -5.878  0.22 12.81 ?  132 PHE   A CB   1 
ATOM   2791 C CG   A PHE   A 1 132 ? 20.792 -0.163  -5.116  0.78 10.79 ?  132 PHE   A CG   1 
ATOM   2792 C CG   B PHE   A 1 132 ? 20.618 -0.290  -5.117  0.22 12.60 ?  132 PHE   A CG   1 
ATOM   2793 C CD1  A PHE   A 1 132 ? 20.686 0.880   -4.211  0.78 11.97 ?  132 PHE   A CD1  1 
ATOM   2794 C CD1  B PHE   A 1 132 ? 20.417 0.628   -4.100  0.22 12.63 ?  132 PHE   A CD1  1 
ATOM   2795 C CD2  A PHE   A 1 132 ? 22.053 -0.689  -5.374  0.78 11.80 ?  132 PHE   A CD2  1 
ATOM   2796 C CD2  B PHE   A 1 132 ? 21.913 -0.683  -5.411  0.22 12.67 ?  132 PHE   A CD2  1 
ATOM   2797 C CE1  A PHE   A 1 132 ? 21.818 1.408   -3.603  0.78 12.23 ?  132 PHE   A CE1  1 
ATOM   2798 C CE1  B PHE   A 1 132 ? 21.487 1.151   -3.398  0.22 12.47 ?  132 PHE   A CE1  1 
ATOM   2799 C CE2  A PHE   A 1 132 ? 23.181 -0.173  -4.768  0.78 12.39 ?  132 PHE   A CE2  1 
ATOM   2800 C CE2  B PHE   A 1 132 ? 22.986 -0.168  -4.711  0.22 12.55 ?  132 PHE   A CE2  1 
ATOM   2801 C CZ   A PHE   A 1 132 ? 23.062 0.884   -3.884  0.78 12.19 ?  132 PHE   A CZ   1 
ATOM   2802 C CZ   B PHE   A 1 132 ? 22.772 0.753   -3.703  0.22 12.36 ?  132 PHE   A CZ   1 
ATOM   2803 H H    A PHE   A 1 132 ? 17.699 0.746   -5.023  0.78 13.01 ?  132 PHE   A H    1 
ATOM   2804 H H    B PHE   A 1 132 ? 17.558 0.624   -5.317  0.22 15.59 ?  132 PHE   A H    1 
ATOM   2805 H HA   A PHE   A 1 132 ? 19.369 0.773   -7.089  0.78 13.33 ?  132 PHE   A HA   1 
ATOM   2806 H HA   B PHE   A 1 132 ? 19.456 0.710   -7.171  0.22 15.57 ?  132 PHE   A HA   1 
ATOM   2807 H HB2  A PHE   A 1 132 ? 18.989 -1.107  -5.055  0.78 12.94 ?  132 PHE   A HB2  1 
ATOM   2808 H HB2  B PHE   A 1 132 ? 18.814 -1.185  -5.229  0.22 15.39 ?  132 PHE   A HB2  1 
ATOM   2809 H HB3  A PHE   A 1 132 ? 19.845 -1.507  -6.330  0.78 12.94 ?  132 PHE   A HB3  1 
ATOM   2810 H HB3  B PHE   A 1 132 ? 19.789 -1.605  -6.409  0.22 15.39 ?  132 PHE   A HB3  1 
ATOM   2811 H HD1  A PHE   A 1 132 ? 19.855 1.235   -4.018  0.78 14.38 ?  132 PHE   A HD1  1 
ATOM   2812 H HD1  B PHE   A 1 132 ? 19.553 0.899   -3.891  0.22 15.17 ?  132 PHE   A HD1  1 
ATOM   2813 H HD2  A PHE   A 1 132 ? 22.143 -1.404  -5.974  0.78 14.17 ?  132 PHE   A HD2  1 
ATOM   2814 H HD2  B PHE   A 1 132 ? 22.063 -1.303  -6.090  0.22 15.22 ?  132 PHE   A HD2  1 
ATOM   2815 H HE1  A PHE   A 1 132 ? 21.742 2.115   -3.006  0.78 14.70 ?  132 PHE   A HE1  1 
ATOM   2816 H HE1  B PHE   A 1 132 ? 21.341 1.768   -2.719  0.22 14.98 ?  132 PHE   A HE1  1 
ATOM   2817 H HE2  A PHE   A 1 132 ? 24.022 -0.527  -4.965  0.78 14.88 ?  132 PHE   A HE2  1 
ATOM   2818 H HE2  B PHE   A 1 132 ? 23.851 -0.438  -4.923  0.22 15.08 ?  132 PHE   A HE2  1 
ATOM   2819 H HZ   A PHE   A 1 132 ? 23.823 1.239   -3.479  0.78 14.64 ?  132 PHE   A HZ   1 
ATOM   2820 H HZ   B PHE   A 1 132 ? 23.493 1.103   -3.232  0.22 14.85 ?  132 PHE   A HZ   1 
ATOM   2821 N N    A GLY   A 1 133 ? 16.606 -0.498  -7.649  0.78 11.69 ?  133 GLY   A N    1 
ATOM   2822 N N    B GLY   A 1 133 ? 16.775 -0.677  -7.990  0.22 12.55 ?  133 GLY   A N    1 
ATOM   2823 C CA   A GLY   A 1 133 ? 15.793 -0.856  -8.794  0.78 12.75 ?  133 GLY   A CA   1 
ATOM   2824 C CA   B GLY   A 1 133 ? 16.053 -1.065  -9.183  0.22 12.45 ?  133 GLY   A CA   1 
ATOM   2825 C C    A GLY   A 1 133 ? 15.443 -2.315  -8.977  0.78 13.33 ?  133 GLY   A C    1 
ATOM   2826 C C    B GLY   A 1 133 ? 15.561 -2.496  -9.256  0.22 12.73 ?  133 GLY   A C    1 
ATOM   2827 O O    A GLY   A 1 133 ? 14.721 -2.628  -9.930  0.78 14.86 ?  133 GLY   A O    1 
ATOM   2828 O O    B GLY   A 1 133 ? 14.924 -2.850  -10.255 0.22 13.23 ?  133 GLY   A O    1 
ATOM   2829 H H    A GLY   A 1 133 ? 16.146 -0.256  -6.960  0.78 14.04 ?  133 GLY   A H    1 
ATOM   2830 H H    B GLY   A 1 133 ? 16.270 -0.519  -7.311  0.22 15.08 ?  133 GLY   A H    1 
ATOM   2831 H HA2  A GLY   A 1 133 ? 14.950 -0.383  -8.734  0.78 15.32 ?  133 GLY   A HA2  1 
ATOM   2832 H HA2  B GLY   A 1 133 ? 15.288 -0.482  -9.275  0.22 14.95 ?  133 GLY   A HA2  1 
ATOM   2833 H HA3  A GLY   A 1 133 ? 16.242 -0.563  -9.599  0.78 15.32 ?  133 GLY   A HA3  1 
ATOM   2834 H HA3  B GLY   A 1 133 ? 16.626 -0.921  -9.948  0.22 14.95 ?  133 GLY   A HA3  1 
ATOM   2835 N N    A ALA   A 1 134 ? 15.920 -3.219  -8.122  0.78 13.01 ?  134 ALA   A N    1 
ATOM   2836 N N    B ALA   A 1 134 ? 15.835 -3.331  -8.258  0.22 12.29 ?  134 ALA   A N    1 
ATOM   2837 C CA   A ALA   A 1 134 ? 15.581 -4.623  -8.294  0.78 13.65 ?  134 ALA   A CA   1 
ATOM   2838 C CA   B ALA   A 1 134 ? 15.405 -4.722  -8.297  0.22 12.31 ?  134 ALA   A CA   1 
ATOM   2839 C C    A ALA   A 1 134 ? 14.210 -4.916  -7.685  0.78 13.83 ?  134 ALA   A C    1 
ATOM   2840 C C    B ALA   A 1 134 ? 14.128 -4.928  -7.490  0.22 12.26 ?  134 ALA   A C    1 
ATOM   2841 O O    A ALA   A 1 134 ? 13.643 -4.116  -6.934  0.78 14.85 ?  134 ALA   A O    1 
ATOM   2842 O O    B ALA   A 1 134 ? 13.803 -4.163  -6.578  0.22 12.47 ?  134 ALA   A O    1 
ATOM   2843 C CB   A ALA   A 1 134 ? 16.653 -5.523  -7.677  0.78 14.94 ?  134 ALA   A CB   1 
ATOM   2844 C CB   B ALA   A 1 134 ? 16.499 -5.657  -7.779  0.22 12.65 ?  134 ALA   A CB   1 
ATOM   2845 H H    A ALA   A 1 134 ? 16.437 -3.048  -7.451  0.78 15.62 ?  134 ALA   A H    1 
ATOM   2846 H H    B ALA   A 1 134 ? 16.280 -3.122  -7.549  0.22 14.76 ?  134 ALA   A H    1 
ATOM   2847 H HA   A ALA   A 1 134 ? 15.537 -4.825  -9.243  0.78 16.40 ?  134 ALA   A HA   1 
ATOM   2848 H HA   B ALA   A 1 134 ? 15.214 -4.966  -9.214  0.22 14.79 ?  134 ALA   A HA   1 
ATOM   2849 H HB1  A ALA   A 1 134 ? 16.408 -6.451  -7.820  0.78 17.94 ?  134 ALA   A HB1  1 
ATOM   2850 H HB1  B ALA   A 1 134 ? 16.189 -6.575  -7.850  0.22 15.19 ?  134 ALA   A HB1  1 
ATOM   2851 H HB2  A ALA   A 1 134 ? 17.507 -5.340  -8.107  0.78 17.94 ?  134 ALA   A HB2  1 
ATOM   2852 H HB2  B ALA   A 1 134 ? 17.294 -5.535  -8.321  0.22 15.19 ?  134 ALA   A HB2  1 
ATOM   2853 H HB3  A ALA   A 1 134 ? 16.717 -5.338  -6.729  0.78 17.94 ?  134 ALA   A HB3  1 
ATOM   2854 H HB3  B ALA   A 1 134 ? 16.690 -5.443  -6.855  0.22 15.19 ?  134 ALA   A HB3  1 
ATOM   2855 N N    A ASP   A 1 135 ? 13.676 -6.086  -8.024  0.78 14.50 ?  135 ASP   A N    1 
ATOM   2856 N N    B ASP   A 1 135 ? 13.411 -5.991  -7.841  0.22 12.33 ?  135 ASP   A N    1 
ATOM   2857 C CA   A ASP   A 1 135 ? 12.414 -6.559  -7.456  0.78 15.56 ?  135 ASP   A CA   1 
ATOM   2858 C CA   B ASP   A 1 135 ? 12.173 -6.346  -7.160  0.22 12.65 ?  135 ASP   A CA   1 
ATOM   2859 C C    A ASP   A 1 135 ? 12.656 -7.008  -6.020  0.78 15.04 ?  135 ASP   A C    1 
ATOM   2860 C C    B ASP   A 1 135 ? 12.485 -6.844  -5.754  0.22 12.36 ?  135 ASP   A C    1 
ATOM   2861 O O    A ASP   A 1 135 ? 13.416 -7.960  -5.803  0.78 14.99 ?  135 ASP   A O    1 
ATOM   2862 O O    B ASP   A 1 135 ? 13.268 -7.792  -5.605  0.22 12.20 ?  135 ASP   A O    1 
ATOM   2863 C CB   A ASP   A 1 135 ? 11.918 -7.735  -8.297  0.78 18.00 ?  135 ASP   A CB   1 
ATOM   2864 C CB   B ASP   A 1 135 ? 11.479 -7.447  -7.956  0.22 13.17 ?  135 ASP   A CB   1 
ATOM   2865 C CG   A ASP   A 1 135 ? 10.645 -8.384  -7.747  0.78 20.62 ?  135 ASP   A CG   1 
ATOM   2866 C CG   B ASP   A 1 135 ? 10.108 -7.790  -7.406  0.22 13.93 ?  135 ASP   A CG   1 
ATOM   2867 O OD1  A ASP   A 1 135 ? 10.091 -7.903  -6.738  0.78 20.92 ?  135 ASP   A OD1  1 
ATOM   2868 O OD1  B ASP   A 1 135 ? 9.776  -7.340  -6.288  0.22 14.20 ?  135 ASP   A OD1  1 
ATOM   2869 O OD2  A ASP   A 1 135 ? 10.201 -9.392  -8.340  0.78 23.37 -1 135 ASP   A OD2  1 
ATOM   2870 O OD2  B ASP   A 1 135 ? 9.357  -8.507  -8.100  0.22 14.41 -1 135 ASP   A OD2  1 
ATOM   2871 H H    A ASP   A 1 135 ? 14.026 -6.632  -8.587  0.78 17.41 ?  135 ASP   A H    1 
ATOM   2872 H H    B ASP   A 1 135 ? 13.617 -6.534  -8.479  0.22 14.82 ?  135 ASP   A H    1 
ATOM   2873 H HA   A ASP   A 1 135 ? 11.755 -5.845  -7.481  0.78 18.69 ?  135 ASP   A HA   1 
ATOM   2874 H HA   B ASP   A 1 135 ? 11.584 -5.574  -7.123  0.22 15.20 ?  135 ASP   A HA   1 
ATOM   2875 H HB2  A ASP   A 1 135 ? 11.737 -7.417  -9.194  0.78 21.61 ?  135 ASP   A HB2  1 
ATOM   2876 H HB2  B ASP   A 1 135 ? 11.370 -7.155  -8.875  0.22 15.82 ?  135 ASP   A HB2  1 
ATOM   2877 H HB3  A ASP   A 1 135 ? 12.608 -8.412  -8.315  0.78 21.61 ?  135 ASP   A HB3  1 
ATOM   2878 H HB3  B ASP   A 1 135 ? 12.026 -8.250  -7.929  0.22 15.82 ?  135 ASP   A HB3  1 
ATOM   2879 N N    A PRO   A 1 136 ? 12.047 -6.368  -5.017  0.78 15.27 ?  136 PRO   A N    1 
ATOM   2880 N N    B PRO   A 1 136 ? 11.909 -6.251  -4.704  0.22 12.48 ?  136 PRO   A N    1 
ATOM   2881 C CA   A PRO   A 1 136 ? 12.313 -6.774  -3.624  0.78 15.45 ?  136 PRO   A CA   1 
ATOM   2882 C CA   B PRO   A 1 136 ? 12.172 -6.758  -3.346  0.22 12.79 ?  136 PRO   A CA   1 
ATOM   2883 C C    A PRO   A 1 136 ? 11.864 -8.188  -3.297  0.78 14.78 ?  136 PRO   A C    1 
ATOM   2884 C C    B PRO   A 1 136 ? 11.804 -8.220  -3.144  0.22 13.02 ?  136 PRO   A C    1 
ATOM   2885 O O    A PRO   A 1 136 ? 12.458 -8.825  -2.419  0.78 14.34 ?  136 PRO   A O    1 
ATOM   2886 O O    B PRO   A 1 136 ? 12.439 -8.896  -2.324  0.22 12.71 ?  136 PRO   A O    1 
ATOM   2887 C CB   A PRO   A 1 136 ? 11.560 -5.719  -2.798  0.78 16.84 ?  136 PRO   A CB   1 
ATOM   2888 C CB   B PRO   A 1 136 ? 11.342 -5.822  -2.451  0.22 13.14 ?  136 PRO   A CB   1 
ATOM   2889 C CG   A PRO   A 1 136 ? 10.509 -5.195  -3.722  0.78 18.15 ?  136 PRO   A CG   1 
ATOM   2890 C CG   B PRO   A 1 136 ? 10.344 -5.180  -3.373  0.22 13.42 ?  136 PRO   A CG   1 
ATOM   2891 C CD   A PRO   A 1 136 ? 11.110 -5.235  -5.093  0.78 16.88 ?  136 PRO   A CD   1 
ATOM   2892 C CD   B PRO   A 1 136 ? 11.055 -5.053  -4.682  0.22 12.81 ?  136 PRO   A CD   1 
ATOM   2893 H HA   A PRO   A 1 136 ? 13.263 -6.696  -3.429  0.78 18.56 ?  136 PRO   A HA   1 
ATOM   2894 H HA   B PRO   A 1 136 ? 13.110 -6.643  -3.128  0.22 15.36 ?  136 PRO   A HA   1 
ATOM   2895 H HB2  A PRO   A 1 136 ? 11.158 -6.137  -2.018  0.78 20.23 ?  136 PRO   A HB2  1 
ATOM   2896 H HB2  B PRO   A 1 136 ? 10.894 -6.337  -1.763  0.22 15.78 ?  136 PRO   A HB2  1 
ATOM   2897 H HB3  A PRO   A 1 136 ? 12.170 -5.012  -2.530  0.78 20.23 ?  136 PRO   A HB3  1 
ATOM   2898 H HB3  B PRO   A 1 136 ? 11.922 -5.153  -2.055  0.22 15.78 ?  136 PRO   A HB3  1 
ATOM   2899 H HG2  A PRO   A 1 136 ? 9.726  -5.765  -3.677  0.78 21.80 ?  136 PRO   A HG2  1 
ATOM   2900 H HG2  B PRO   A 1 136 ? 9.565  -5.752  -3.463  0.22 16.12 ?  136 PRO   A HG2  1 
ATOM   2901 H HG3  A PRO   A 1 136 ? 10.284 -4.286  -3.475  0.78 21.80 ?  136 PRO   A HG3  1 
ATOM   2902 H HG3  B PRO   A 1 136 ? 10.096 -4.308  -3.034  0.22 16.12 ?  136 PRO   A HG3  1 
ATOM   2903 H HD2  A PRO   A 1 136 ? 10.421 -5.415  -5.755  0.78 20.27 ?  136 PRO   A HD2  1 
ATOM   2904 H HD2  B PRO   A 1 136 ? 10.417 -5.072  -5.414  0.22 15.39 ?  136 PRO   A HD2  1 
ATOM   2905 H HD3  A PRO   A 1 136 ? 11.579 -4.408  -5.284  0.78 20.27 ?  136 PRO   A HD3  1 
ATOM   2906 H HD3  B PRO   A 1 136 ? 11.599 -4.248  -4.705  0.22 15.39 ?  136 PRO   A HD3  1 
ATOM   2907 N N    A ILE   A 1 137 ? 10.817 -8.694  -3.955  0.78 14.87 ?  137 ILE   A N    1 
ATOM   2908 N N    B ILE   A 1 137 ? 10.792 -8.729  -3.852  0.22 13.60 ?  137 ILE   A N    1 
ATOM   2909 C CA   A ILE   A 1 137 ? 10.431 -10.090 -3.757  0.78 15.29 ?  137 ILE   A CA   1 
ATOM   2910 C CA   B ILE   A 1 137 ? 10.431 -10.140 -3.722  0.22 14.26 ?  137 ILE   A CA   1 
ATOM   2911 C C    A ILE   A 1 137 ? 11.571 -11.012 -4.169  0.78 14.46 ?  137 ILE   A C    1 
ATOM   2912 C C    B ILE   A 1 137 ? 11.590 -11.023 -4.164  0.22 13.88 ?  137 ILE   A C    1 
ATOM   2913 O O    A ILE   A 1 137 ? 11.871 -12.005 -3.493  0.78 14.62 ?  137 ILE   A O    1 
ATOM   2914 O O    B ILE   A 1 137 ? 11.916 -12.023 -3.511  0.22 13.91 ?  137 ILE   A O    1 
ATOM   2915 C CB   A ILE   A 1 137 ? 9.133  -10.406 -4.525  0.78 16.78 ?  137 ILE   A CB   1 
ATOM   2916 C CB   B ILE   A 1 137 ? 9.144  -10.442 -4.515  0.22 15.36 ?  137 ILE   A CB   1 
ATOM   2917 C CG1  A ILE   A 1 137 ? 7.957  -9.597  -3.965  0.78 18.97 ?  137 ILE   A CG1  1 
ATOM   2918 C CG1  B ILE   A 1 137 ? 7.990  -9.560  -4.030  0.22 16.50 ?  137 ILE   A CG1  1 
ATOM   2919 C CG2  A ILE   A 1 137 ? 8.830  -11.903 -4.476  0.78 17.40 ?  137 ILE   A CG2  1 
ATOM   2920 C CG2  B ILE   A 1 137 ? 8.774  -11.920 -4.399  0.22 15.63 ?  137 ILE   A CG2  1 
ATOM   2921 C CD1  A ILE   A 1 137 ? 6.672  -9.771  -4.742  0.78 20.65 ?  137 ILE   A CD1  1 
ATOM   2922 C CD1  B ILE   A 1 137 ? 6.782  -9.587  -4.940  0.22 17.31 ?  137 ILE   A CD1  1 
ATOM   2923 H H    A ILE   A 1 137 ? 10.327 -8.256  -4.508  0.78 17.86 ?  137 ILE   A H    1 
ATOM   2924 H H    B ILE   A 1 137 ? 10.307 -8.286  -4.405  0.22 16.34 ?  137 ILE   A H    1 
ATOM   2925 H HA   A ILE   A 1 137 ? 10.261 -10.235 -2.814  0.78 18.37 ?  137 ILE   A HA   1 
ATOM   2926 H HA   B ILE   A 1 137 ? 10.253 -10.336 -2.791  0.22 17.13 ?  137 ILE   A HA   1 
ATOM   2927 H HB   A ILE   A 1 137 ? 9.258  -10.151 -5.451  0.78 20.14 ?  137 ILE   A HB   1 
ATOM   2928 H HB   B ILE   A 1 137 ? 9.303  -10.244 -5.449  0.22 18.45 ?  137 ILE   A HB   1 
ATOM   2929 H HG12 A ILE   A 1 137 ? 7.794  -9.870  -3.050  0.78 22.77 ?  137 ILE   A HG12 1 
ATOM   2930 H HG12 B ILE   A 1 137 ? 7.709  -9.864  -3.153  0.22 19.81 ?  137 ILE   A HG12 1 
ATOM   2931 H HG13 A ILE   A 1 137 ? 8.190  -8.651  -3.988  0.78 22.77 ?  137 ILE   A HG13 1 
ATOM   2932 H HG13 B ILE   A 1 137 ? 8.294  -8.640  -3.976  0.22 19.81 ?  137 ILE   A HG13 1 
ATOM   2933 H HG21 A ILE   A 1 137 ? 7.924  -12.070 -4.778  0.78 20.89 ?  137 ILE   A HG21 1 
ATOM   2934 H HG21 B ILE   A 1 137 ? 7.922  -12.074 -4.836  0.22 18.77 ?  137 ILE   A HG21 1 
ATOM   2935 H HG22 A ILE   A 1 137 ? 9.453  -12.365 -5.054  0.78 20.89 ?  137 ILE   A HG22 1 
ATOM   2936 H HG22 B ILE   A 1 137 ? 9.460  -12.454 -4.831  0.22 18.77 ?  137 ILE   A HG22 1 
ATOM   2937 H HG23 A ILE   A 1 137 ? 8.930  -12.209 -3.564  0.78 20.89 ?  137 ILE   A HG23 1 
ATOM   2938 H HG23 B ILE   A 1 137 ? 8.711  -12.157 -3.461  0.22 18.77 ?  137 ILE   A HG23 1 
ATOM   2939 H HD11 A ILE   A 1 137 ? 5.970  -10.053 -4.135  0.78 24.79 ?  137 ILE   A HD11 1 
ATOM   2940 H HD11 B ILE   A 1 137 ? 6.094  -9.022  -4.560  0.22 20.79 ?  137 ILE   A HD11 1 
ATOM   2941 H HD12 A ILE   A 1 137 ? 6.447  -8.922  -5.146  0.78 24.79 ?  137 ILE   A HD12 1 
ATOM   2942 H HD12 B ILE   A 1 137 ? 7.039  -9.258  -5.816  0.22 20.79 ?  137 ILE   A HD12 1 
ATOM   2943 H HD13 A ILE   A 1 137 ? 6.797  -10.434 -5.439  0.78 24.79 ?  137 ILE   A HD13 1 
ATOM   2944 H HD13 B ILE   A 1 137 ? 6.455  -10.497 -5.011  0.22 20.79 ?  137 ILE   A HD13 1 
ATOM   2945 N N    A HIS   A 1 138 ? 12.217 -10.698 -5.294  0.78 14.27 ?  138 HIS   A N    1 
ATOM   2946 N N    B HIS   A 1 138 ? 12.224 -10.672 -5.284  0.22 13.71 ?  138 HIS   A N    1 
ATOM   2947 C CA   A HIS   A 1 138 ? 13.382 -11.461 -5.725  0.78 13.88 ?  138 HIS   A CA   1 
ATOM   2948 C CA   B HIS   A 1 138 ? 13.380 -11.427 -5.753  0.22 13.36 ?  138 HIS   A CA   1 
ATOM   2949 C C    A HIS   A 1 138 ? 14.532 -11.326 -4.734  0.78 13.07 ?  138 HIS   A C    1 
ATOM   2950 C C    B HIS   A 1 138 ? 14.545 -11.313 -4.777  0.22 12.93 ?  138 HIS   A C    1 
ATOM   2951 O O    A HIS   A 1 138 ? 15.196 -12.315 -4.404  0.78 13.26 ?  138 HIS   A O    1 
ATOM   2952 O O    B HIS   A 1 138 ? 15.231 -12.303 -4.498  0.22 12.91 ?  138 HIS   A O    1 
ATOM   2953 C CB   A HIS   A 1 138 ? 13.803 -11.020 -7.126  0.78 14.69 ?  138 HIS   A CB   1 
ATOM   2954 C CB   B HIS   A 1 138 ? 13.784 -10.933 -7.142  0.22 13.61 ?  138 HIS   A CB   1 
ATOM   2955 C CG   A HIS   A 1 138 ? 15.060 -11.671 -7.604  0.78 15.50 ?  138 HIS   A CG   1 
ATOM   2956 C CG   B HIS   A 1 138 ? 15.070 -11.516 -7.637  0.22 13.94 ?  138 HIS   A CG   1 
ATOM   2957 N ND1  A HIS   A 1 138 ? 15.150 -13.024 -7.852  0.78 16.84 ?  138 HIS   A ND1  1 
ATOM   2958 N ND1  B HIS   A 1 138 ? 15.227 -12.859 -7.897  0.22 14.39 ?  138 HIS   A ND1  1 
ATOM   2959 C CD2  A HIS   A 1 138 ? 16.287 -11.158 -7.856  0.78 15.58 ?  138 HIS   A CD2  1 
ATOM   2960 C CD2  B HIS   A 1 138 ? 16.261 -10.937 -7.914  0.22 13.91 ?  138 HIS   A CD2  1 
ATOM   2961 C CE1  A HIS   A 1 138 ? 16.377 -13.314 -8.247  0.78 17.04 ?  138 HIS   A CE1  1 
ATOM   2962 C CE1  B HIS   A 1 138 ? 16.460 -13.083 -8.316  0.22 14.31 ?  138 HIS   A CE1  1 
ATOM   2963 N NE2  A HIS   A 1 138 ? 17.087 -12.200 -8.258  0.78 16.46 ?  138 HIS   A NE2  1 
ATOM   2964 N NE2  B HIS   A 1 138 ? 17.108 -11.932 -8.335  0.22 14.12 ?  138 HIS   A NE2  1 
ATOM   2965 H H    A HIS   A 1 138 ? 11.999 -10.050 -5.822  0.78 17.13 ?  138 HIS   A H    1 
ATOM   2966 H H    B HIS   A 1 138 ? 12.004 -10.008 -5.784  0.22 16.47 ?  138 HIS   A H    1 
ATOM   2967 H HA   A HIS   A 1 138 ? 13.135 -12.395 -5.774  0.78 16.67 ?  138 HIS   A HA   1 
ATOM   2968 H HA   B HIS   A 1 138 ? 13.139 -12.363 -5.826  0.22 16.05 ?  138 HIS   A HA   1 
ATOM   2969 H HB2  A HIS   A 1 138 ? 13.092 -11.248 -7.754  0.78 17.64 ?  138 HIS   A HB2  1 
ATOM   2970 H HB2  B HIS   A 1 138 ? 13.087 -11.172 -7.775  0.22 16.35 ?  138 HIS   A HB2  1 
ATOM   2971 H HB3  A HIS   A 1 138 ? 13.941 -10.061 -7.129  0.78 17.64 ?  138 HIS   A HB3  1 
ATOM   2972 H HB3  B HIS   A 1 138 ? 13.885 -9.969  -7.115  0.22 16.35 ?  138 HIS   A HB3  1 
ATOM   2973 H HD1  A HIS   A 1 138 ? 14.508 -13.590 -7.767  0.78 20.22 ?  138 HIS   A HD1  1 
ATOM   2974 H HD2  A HIS   A 1 138 ? 16.534 -10.266 -7.775  0.78 18.71 ?  138 HIS   A HD2  1 
ATOM   2975 H HD2  B HIS   A 1 138 ? 16.466 -10.033 -7.835  0.22 16.71 ?  138 HIS   A HD2  1 
ATOM   2976 H HE1  A HIS   A 1 138 ? 16.688 -14.158 -8.477  0.78 20.46 ?  138 HIS   A HE1  1 
ATOM   2977 H HE1  B HIS   A 1 138 ? 16.811 -13.910 -8.555  0.22 17.19 ?  138 HIS   A HE1  1 
ATOM   2978 H HE2  B HIS   A 1 138 ? 17.926 -11.824 -8.572  0.22 16.95 ?  138 HIS   A HE2  1 
ATOM   2979 N N    . SER   A 1 139 ? 14.782 -10.112 -4.244  1.00 12.70 ?  139 SER   A N    1 
ATOM   2980 C CA   . SER   A 1 139 ? 15.862 -9.932  -3.284  1.00 12.27 ?  139 SER   A CA   1 
ATOM   2981 C C    . SER   A 1 139 ? 15.652 -10.787 -2.039  1.00 11.83 ?  139 SER   A C    1 
ATOM   2982 O O    . SER   A 1 139 ? 16.606 -11.384 -1.524  1.00 12.01 ?  139 SER   A O    1 
ATOM   2983 C CB   . SER   A 1 139 ? 15.995 -8.459  -2.919  1.00 12.81 ?  139 SER   A CB   1 
ATOM   2984 O OG   . SER   A 1 139 ? 17.091 -8.298  -2.038  1.00 12.90 ?  139 SER   A OG   1 
ATOM   2985 H H    A SER   A 1 139 ? 14.350 -9.395  -4.444  0.78 15.25 ?  139 SER   A H    1 
ATOM   2986 H H    B SER   A 1 139 ? 14.336 -9.397  -4.422  0.22 15.25 ?  139 SER   A H    1 
ATOM   2987 H HA   . SER   A 1 139 ? 16.697 -10.205 -3.694  1.00 14.74 ?  139 SER   A HA   1 
ATOM   2988 H HB2  . SER   A 1 139 ? 16.150 -7.933  -3.723  1.00 15.38 ?  139 SER   A HB2  1 
ATOM   2989 H HB3  . SER   A 1 139 ? 15.183 -8.155  -2.477  1.00 15.38 ?  139 SER   A HB3  1 
ATOM   2990 H HG   . SER   A 1 139 ? 17.177 -7.482  -1.828  1.00 15.49 ?  139 SER   A HG   1 
ATOM   2991 N N    . LEU   A 1 140 ? 14.417 -10.846 -1.535  1.00 11.99 ?  140 LEU   A N    1 
ATOM   2992 C CA   . LEU   A 1 140 ? 14.143 -11.672 -0.364  1.00 11.91 ?  140 LEU   A CA   1 
ATOM   2993 C C    . LEU   A 1 140 ? 14.399 -13.148 -0.661  1.00 11.99 ?  140 LEU   A C    1 
ATOM   2994 O O    . LEU   A 1 140 ? 14.956 -13.876 0.172   1.00 12.44 ?  140 LEU   A O    1 
ATOM   2995 C CB   . LEU   A 1 140 ? 12.707 -11.443 0.107   1.00 12.34 ?  140 LEU   A CB   1 
ATOM   2996 C CG   . LEU   A 1 140 ? 12.251 -12.304 1.281   1.00 12.99 ?  140 LEU   A CG   1 
ATOM   2997 C CD1  . LEU   A 1 140 ? 13.158 -12.138 2.490   1.00 13.01 ?  140 LEU   A CD1  1 
ATOM   2998 C CD2  . LEU   A 1 140 ? 10.799 -11.993 1.643   1.00 13.94 ?  140 LEU   A CD2  1 
ATOM   2999 H H    . LEU   A 1 140 ? 13.735 -10.421 -1.846  1.00 14.40 ?  140 LEU   A H    1 
ATOM   3000 H HA   . LEU   A 1 140 ? 14.735 -11.405 0.353   1.00 14.31 ?  140 LEU   A HA   1 
ATOM   3001 H HB2  . LEU   A 1 140 ? 12.615 -10.520 0.378   1.00 14.82 ?  140 LEU   A HB2  1 
ATOM   3002 H HB3  . LEU   A 1 140 ? 12.108 -11.626 -0.634  1.00 14.82 ?  140 LEU   A HB3  1 
ATOM   3003 H HG   . LEU   A 1 140 ? 12.279 -13.240 1.015   1.00 15.61 ?  140 LEU   A HG   1 
ATOM   3004 H HD11 . LEU   A 1 140 ? 12.780 -12.630 3.238   1.00 15.63 ?  140 LEU   A HD11 1 
ATOM   3005 H HD12 . LEU   A 1 140 ? 14.034 -12.499 2.273   1.00 15.63 ?  140 LEU   A HD12 1 
ATOM   3006 H HD13 . LEU   A 1 140 ? 13.226 -11.201 2.707   1.00 15.63 ?  140 LEU   A HD13 1 
ATOM   3007 H HD21 . LEU   A 1 140 ? 10.511 -12.599 2.351   1.00 16.74 ?  140 LEU   A HD21 1 
ATOM   3008 H HD22 . LEU   A 1 140 ? 10.736 -11.078 1.948   1.00 16.74 ?  140 LEU   A HD22 1 
ATOM   3009 H HD23 . LEU   A 1 140 ? 10.239 -12.125 0.860   1.00 16.74 ?  140 LEU   A HD23 1 
ATOM   3010 N N    . ARG   A 1 141 ? 14.004 -13.605 -1.852  1.00 12.63 ?  141 ARG   A N    1 
ATOM   3011 C CA   . ARG   A 1 141 ? 14.235 -14.992 -2.240  1.00 13.53 ?  141 ARG   A CA   1 
ATOM   3012 C C    . ARG   A 1 141 ? 15.730 -15.304 -2.262  1.00 12.47 ?  141 ARG   A C    1 
ATOM   3013 O O    . ARG   A 1 141 ? 16.180 -16.318 -1.712  1.00 12.70 ?  141 ARG   A O    1 
ATOM   3014 C CB   . ARG   A 1 141 ? 13.603 -15.220 -3.616  1.00 15.20 ?  141 ARG   A CB   1 
ATOM   3015 C CG   . ARG   A 1 141 ? 13.586 -16.647 -4.102  1.00 18.05 ?  141 ARG   A CG   1 
ATOM   3016 C CD   . ARG   A 1 141 ? 12.562 -17.439 -3.353  1.00 19.61 ?  141 ARG   A CD   1 
ATOM   3017 N NE   . ARG   A 1 141 ? 13.175 -18.202 -2.280  1.00 20.00 ?  141 ARG   A NE   1 
ATOM   3018 C CZ   . ARG   A 1 141 ? 12.488 -18.787 -1.308  1.00 20.64 ?  141 ARG   A CZ   1 
ATOM   3019 N NH1  . ARG   A 1 141 ? 11.193 -18.572 -1.152  1.00 20.73 ?  141 ARG   A NH1  1 
ATOM   3020 N NH2  . ARG   A 1 141 ? 13.119 -19.601 -0.467  1.00 21.40 ?  141 ARG   A NH2  1 
ATOM   3021 H H    . ARG   A 1 141 ? 13.604 -13.131 -2.449  1.00 15.17 ?  141 ARG   A H    1 
ATOM   3022 H HA   . ARG   A 1 141 ? 13.809 -15.582 -1.603  1.00 16.26 ?  141 ARG   A HA   1 
ATOM   3023 H HB2  . ARG   A 1 141 ? 12.685 -14.904 -3.589  1.00 18.25 ?  141 ARG   A HB2  1 
ATOM   3024 H HB3  . ARG   A 1 141 ? 14.099 -14.696 -4.267  1.00 18.25 ?  141 ARG   A HB3  1 
ATOM   3025 H HG2  . ARG   A 1 141 ? 13.362 -16.663 -5.049  1.00 21.67 ?  141 ARG   A HG2  1 
ATOM   3026 H HG3  . ARG   A 1 141 ? 14.460 -17.050 -3.960  1.00 21.67 ?  141 ARG   A HG3  1 
ATOM   3027 H HD2  . ARG   A 1 141 ? 11.911 -16.837 -2.958  1.00 23.55 ?  141 ARG   A HD2  1 
ATOM   3028 H HD3  . ARG   A 1 141 ? 12.122 -18.054 -3.961  1.00 23.55 ?  141 ARG   A HD3  1 
ATOM   3029 H HE   . ARG   A 1 141 ? 14.010 -18.388 -2.348  1.00 24.02 ?  141 ARG   A HE   1 
ATOM   3030 H HH11 . ARG   A 1 141 ? 10.769 -18.060 -1.699  1.00 24.89 ?  141 ARG   A HH11 1 
ATOM   3031 H HH12 . ARG   A 1 141 ? 10.766 -18.960 -0.514  1.00 24.89 ?  141 ARG   A HH12 1 
ATOM   3032 H HH21 . ARG   A 1 141 ? 13.963 -19.742 -0.554  1.00 25.70 ?  141 ARG   A HH21 1 
ATOM   3033 H HH22 . ARG   A 1 141 ? 12.686 -19.974 0.178   1.00 25.70 ?  141 ARG   A HH22 1 
ATOM   3034 N N    . VAL   A 1 142 ? 16.524 -14.429 -2.887  1.00 12.16 ?  142 VAL   A N    1 
ATOM   3035 C CA   . VAL   A 1 142 ? 17.968 -14.642 -2.927  1.00 12.05 ?  142 VAL   A CA   1 
ATOM   3036 C C    . VAL   A 1 142 ? 18.547 -14.635 -1.519  1.00 11.52 ?  142 VAL   A C    1 
ATOM   3037 O O    . VAL   A 1 142 ? 19.405 -15.460 -1.181  1.00 11.82 ?  142 VAL   A O    1 
ATOM   3038 C CB   . VAL   A 1 142 ? 18.661 -13.620 -3.849  1.00 12.28 ?  142 VAL   A CB   1 
ATOM   3039 C CG1  . VAL   A 1 142 ? 20.166 -13.845 -3.820  1.00 12.53 ?  142 VAL   A CG1  1 
ATOM   3040 C CG2  . VAL   A 1 142 ? 18.149 -13.755 -5.275  1.00 13.53 ?  142 VAL   A CG2  1 
ATOM   3041 H H    . VAL   A 1 142 ? 16.257 -13.706 -3.283  1.00 14.61 ?  142 VAL   A H    1 
ATOM   3042 H HA   . VAL   A 1 142 ? 18.135 -15.516 -3.307  1.00 14.47 ?  142 VAL   A HA   1 
ATOM   3043 H HB   . VAL   A 1 142 ? 18.480 -12.714 -3.540  1.00 14.76 ?  142 VAL   A HB   1 
ATOM   3044 H HG11 . VAL   A 1 142 ? 20.573 -13.366 -4.561  1.00 15.05 ?  142 VAL   A HG11 1 
ATOM   3045 H HG12 . VAL   A 1 142 ? 20.523 -13.509 -2.980  1.00 15.05 ?  142 VAL   A HG12 1 
ATOM   3046 H HG13 . VAL   A 1 142 ? 20.345 -14.792 -3.902  1.00 15.05 ?  142 VAL   A HG13 1 
ATOM   3047 H HG21 . VAL   A 1 142 ? 18.610 -13.110 -5.836  1.00 16.25 ?  142 VAL   A HG21 1 
ATOM   3048 H HG22 . VAL   A 1 142 ? 18.337 -14.655 -5.585  1.00 16.25 ?  142 VAL   A HG22 1 
ATOM   3049 H HG23 . VAL   A 1 142 ? 17.200 -13.588 -5.283  1.00 16.25 ?  142 VAL   A HG23 1 
ATOM   3050 N N    . CYS   A 1 143 ? 18.085 -13.713 -0.672  1.00 11.51 ?  143 CYS   A N    1 
ATOM   3051 C CA   . CYS   A 1 143 ? 18.554 -13.677 0.708   1.00 11.53 ?  143 CYS   A CA   1 
ATOM   3052 C C    . CYS   A 1 143 ? 18.336 -15.023 1.394   1.00 11.41 ?  143 CYS   A C    1 
ATOM   3053 O O    . CYS   A 1 143 ? 19.264 -15.610 1.961   1.00 11.62 ?  143 CYS   A O    1 
ATOM   3054 C CB   . CYS   A 1 143 ? 17.823 -12.569 1.462   1.00 12.07 ?  143 CYS   A CB   1 
ATOM   3055 S SG   . CYS   A 1 143 ? 18.324 -12.403 3.185   1.00 12.56 ?  143 CYS   A SG   1 
ATOM   3056 H H    . CYS   A 1 143 ? 17.506 -13.111 -0.875  1.00 13.83 ?  143 CYS   A H    1 
ATOM   3057 H HA   . CYS   A 1 143 ? 19.500 -13.486 0.717   1.00 13.86 ?  143 CYS   A HA   1 
ATOM   3058 H HB2  . CYS   A 1 143 ? 17.988 -11.724 1.015   1.00 14.50 ?  143 CYS   A HB2  1 
ATOM   3059 H HB3  . CYS   A 1 143 ? 16.873 -12.759 1.451   1.00 14.50 ?  143 CYS   A HB3  1 
ATOM   3060 H HG   . CYS   A 1 143 ? 17.744 -11.468 3.667   1.00 15.09 ?  143 CYS   A HG   1 
ATOM   3061 N N    . VAL   A 1 144 ? 17.102 -15.521 1.356   1.00 12.00 ?  144 VAL   A N    1 
ATOM   3062 C CA   . VAL   A 1 144 ? 16.772 -16.755 2.056   1.00 13.21 ?  144 VAL   A CA   1 
ATOM   3063 C C    . VAL   A 1 144 ? 17.582 -17.921 1.515   1.00 12.85 ?  144 VAL   A C    1 
ATOM   3064 O O    . VAL   A 1 144 ? 17.959 -18.832 2.264   1.00 13.82 ?  144 VAL   A O    1 
ATOM   3065 C CB   . VAL   A 1 144 ? 15.256 -16.997 1.952   1.00 16.40 ?  144 VAL   A CB   1 
ATOM   3066 C CG1  . VAL   A 1 144 ? 14.899 -18.422 2.309   1.00 18.20 ?  144 VAL   A CG1  1 
ATOM   3067 C CG2  . VAL   A 1 144 ? 14.513 -15.984 2.827   1.00 16.26 ?  144 VAL   A CG2  1 
ATOM   3068 H H    . VAL   A 1 144 ? 16.437 -15.161 0.932   1.00 14.42 ?  144 VAL   A H    1 
ATOM   3069 H HA   . VAL   A 1 144 ? 16.983 -16.647 2.992   1.00 15.87 ?  144 VAL   A HA   1 
ATOM   3070 H HB   . VAL   A 1 144 ? 14.970 -16.840 1.034   1.00 19.70 ?  144 VAL   A HB   1 
ATOM   3071 H HG11 . VAL   A 1 144 ? 13.941 -18.477 2.475   1.00 21.86 ?  144 VAL   A HG11 1 
ATOM   3072 H HG12 . VAL   A 1 144 ? 15.133 -19.005 1.571   1.00 21.86 ?  144 VAL   A HG12 1 
ATOM   3073 H HG13 . VAL   A 1 144 ? 15.384 -18.679 3.108   1.00 21.86 ?  144 VAL   A HG13 1 
ATOM   3074 H HG21 . VAL   A 1 144 ? 13.557 -16.159 2.784   1.00 19.52 ?  144 VAL   A HG21 1 
ATOM   3075 H HG22 . VAL   A 1 144 ? 14.820 -16.068 3.742   1.00 19.52 ?  144 VAL   A HG22 1 
ATOM   3076 H HG23 . VAL   A 1 144 ? 14.693 -15.084 2.501   1.00 19.52 ?  144 VAL   A HG23 1 
ATOM   3077 N N    . ASP   A 1 145 ? 17.832 -17.936 0.209   1.00 13.11 ?  145 ASP   A N    1 
ATOM   3078 C CA   . ASP   A 1 145 ? 18.537 -19.037 -0.436  1.00 13.87 ?  145 ASP   A CA   1 
ATOM   3079 C C    . ASP   A 1 145 ? 20.057 -18.895 -0.407  1.00 13.48 ?  145 ASP   A C    1 
ATOM   3080 O O    . ASP   A 1 145 ? 20.758 -19.785 -0.899  1.00 15.59 ?  145 ASP   A O    1 
ATOM   3081 C CB   . ASP   A 1 145 ? 18.077 -19.179 -1.890  1.00 15.52 ?  145 ASP   A CB   1 
ATOM   3082 C CG   . ASP   A 1 145 ? 16.618 -19.583 -2.007  1.00 17.42 ?  145 ASP   A CG   1 
ATOM   3083 O OD1  . ASP   A 1 145 ? 16.069 -20.136 -1.031  1.00 17.80 ?  145 ASP   A OD1  1 
ATOM   3084 O OD2  . ASP   A 1 145 ? 16.019 -19.355 -3.078  1.00 18.72 -1 145 ASP   A OD2  1 
ATOM   3085 H H    . ASP   A 1 145 ? 17.587 -17.313 -0.336  1.00 15.75 ?  145 ASP   A H    1 
ATOM   3086 H HA   . ASP   A 1 145 ? 18.306 -19.858 0.027   1.00 16.66 ?  145 ASP   A HA   1 
ATOM   3087 H HB2  . ASP   A 1 145 ? 18.198 -18.331 -2.342  1.00 18.64 ?  145 ASP   A HB2  1 
ATOM   3088 H HB3  . ASP   A 1 145 ? 18.605 -19.868 -2.318  1.00 18.64 ?  145 ASP   A HB3  1 
ATOM   3089 N N    . THR   A 1 146 ? 20.589 -17.811 0.148   1.00 11.98 ?  146 THR   A N    1 
ATOM   3090 C CA   . THR   A 1 146 ? 22.030 -17.565 0.159   1.00 11.36 ?  146 THR   A CA   1 
ATOM   3091 C C    . THR   A 1 146 ? 22.593 -17.389 1.555   1.00 11.39 ?  146 THR   A C    1 
ATOM   3092 O O    . THR   A 1 146 ? 23.673 -17.914 1.853   1.00 12.37 ?  146 THR   A O    1 
ATOM   3093 C CB   . THR   A 1 146 ? 22.353 -16.307 -0.675  1.00 11.49 ?  146 THR   A CB   1 
ATOM   3094 O OG1  . THR   A 1 146 ? 21.821 -16.457 -1.992  1.00 12.17 ?  146 THR   A OG1  1 
ATOM   3095 C CG2  . THR   A 1 146 ? 23.856 -16.075 -0.773  1.00 11.93 ?  146 THR   A CG2  1 
ATOM   3096 H H    . THR   A 1 146 ? 20.130 -17.188 0.529   1.00 14.39 ?  146 THR   A H    1 
ATOM   3097 H HA   . THR   A 1 146 ? 22.482 -18.315 -0.250  1.00 13.64 ?  146 THR   A HA   1 
ATOM   3098 H HB   . THR   A 1 146 ? 21.956 -15.530 -0.257  1.00 13.80 ?  146 THR   A HB   1 
ATOM   3099 H HG1  . THR   A 1 146 ? 20.982 -16.534 -1.957  1.00 14.62 ?  146 THR   A HG1  1 
ATOM   3100 H HG21 . THR   A 1 146 ? 24.044 -15.400 -1.443  1.00 14.33 ?  146 THR   A HG21 1 
ATOM   3101 H HG22 . THR   A 1 146 ? 24.203 -15.778 0.081   1.00 14.33 ?  146 THR   A HG22 1 
ATOM   3102 H HG23 . THR   A 1 146 ? 24.302 -16.901 -1.027  1.00 14.33 ?  146 THR   A HG23 1 
ATOM   3103 N N    . VAL   A 1 147 ? 21.918 -16.614 2.398   1.00 11.28 ?  147 VAL   A N    1 
ATOM   3104 C CA   . VAL   A 1 147 ? 22.409 -16.321 3.736   1.00 11.30 ?  147 VAL   A CA   1 
ATOM   3105 C C    . VAL   A 1 147 ? 22.091 -17.494 4.651   1.00 11.47 ?  147 VAL   A C    1 
ATOM   3106 O O    . VAL   A 1 147 ? 20.945 -17.959 4.717   1.00 12.42 ?  147 VAL   A O    1 
ATOM   3107 C CB   . VAL   A 1 147 ? 21.796 -15.016 4.264   1.00 11.63 ?  147 VAL   A CB   1 
ATOM   3108 C CG1  . VAL   A 1 147 ? 22.339 -14.705 5.640   1.00 12.43 ?  147 VAL   A CG1  1 
ATOM   3109 C CG2  . VAL   A 1 147 ? 22.061 -13.867 3.302   1.00 11.71 ?  147 VAL   A CG2  1 
ATOM   3110 H H    . VAL   A 1 147 ? 21.158 -16.248 2.220   1.00 13.56 ?  147 VAL   A H    1 
ATOM   3111 H HA   . VAL   A 1 147 ? 23.372 -16.209 3.704   1.00 13.58 ?  147 VAL   A HA   1 
ATOM   3112 H HB   . VAL   A 1 147 ? 20.836 -15.123 4.343   1.00 13.97 ?  147 VAL   A HB   1 
ATOM   3113 H HG11 . VAL   A 1 147 ? 22.088 -13.800 5.884   1.00 14.94 ?  147 VAL   A HG11 1 
ATOM   3114 H HG12 . VAL   A 1 147 ? 21.959 -15.332 6.280   1.00 14.94 ?  147 VAL   A HG12 1 
ATOM   3115 H HG13 . VAL   A 1 147 ? 23.303 -14.790 5.628   1.00 14.94 ?  147 VAL   A HG13 1 
ATOM   3116 H HG21 . VAL   A 1 147 ? 21.736 -13.042 3.700   1.00 14.07 ?  147 VAL   A HG21 1 
ATOM   3117 H HG22 . VAL   A 1 147 ? 23.014 -13.804 3.143   1.00 14.07 ?  147 VAL   A HG22 1 
ATOM   3118 H HG23 . VAL   A 1 147 ? 21.594 -14.040 2.472   1.00 14.07 ?  147 VAL   A HG23 1 
ATOM   3119 N N    . ARG   A 1 148 ? 23.119 -17.978 5.348   1.00 11.80 ?  148 ARG   A N    1 
ATOM   3120 C CA   . ARG   A 1 148 ? 22.990 -19.057 6.314   1.00 12.24 ?  148 ARG   A CA   1 
ATOM   3121 C C    . ARG   A 1 148 ? 23.132 -18.586 7.750   1.00 12.66 ?  148 ARG   A C    1 
ATOM   3122 O O    . ARG   A 1 148 ? 22.724 -19.305 8.668   1.00 14.23 ?  148 ARG   A O    1 
ATOM   3123 C CB   . ARG   A 1 148 ? 24.023 -20.153 6.023   1.00 13.02 ?  148 ARG   A CB   1 
ATOM   3124 C CG   . ARG   A 1 148 ? 23.846 -20.785 4.652   1.00 13.94 ?  148 ARG   A CG   1 
ATOM   3125 C CD   . ARG   A 1 148 ? 24.917 -21.821 4.347   1.00 15.10 ?  148 ARG   A CD   1 
ATOM   3126 N NE   . ARG   A 1 148 ? 26.255 -21.246 4.363   1.00 14.67 ?  148 ARG   A NE   1 
ATOM   3127 C CZ   . ARG   A 1 148 ? 26.757 -20.494 3.391   1.00 14.07 ?  148 ARG   A CZ   1 
ATOM   3128 N NH1  . ARG   A 1 148 ? 26.074 -20.247 2.284   1.00 14.61 ?  148 ARG   A NH1  1 
ATOM   3129 N NH2  . ARG   A 1 148 ? 27.974 -19.972 3.535   1.00 14.42 ?  148 ARG   A NH2  1 
ATOM   3130 H H    . ARG   A 1 148 ? 23.930 -17.688 5.263   1.00 14.17 ?  148 ARG   A H    1 
ATOM   3131 H HA   . ARG   A 1 148 ? 22.112 -19.449 6.218   1.00 14.70 ?  148 ARG   A HA   1 
ATOM   3132 H HB2  . ARG   A 1 148 ? 24.912 -19.778 6.068   1.00 15.64 ?  148 ARG   A HB2  1 
ATOM   3133 H HB3  . ARG   A 1 148 ? 23.925 -20.860 6.684   1.00 15.64 ?  148 ARG   A HB3  1 
ATOM   3134 H HG2  . ARG   A 1 148 ? 22.980 -21.216 4.610   1.00 16.74 ?  148 ARG   A HG2  1 
ATOM   3135 H HG3  . ARG   A 1 148 ? 23.902 -20.085 3.978   1.00 16.74 ?  148 ARG   A HG3  1 
ATOM   3136 H HD2  . ARG   A 1 148 ? 24.882 -22.521 5.018   1.00 18.13 ?  148 ARG   A HD2  1 
ATOM   3137 H HD3  . ARG   A 1 148 ? 24.756 -22.196 3.465   1.00 18.13 ?  148 ARG   A HD3  1 
ATOM   3138 H HE   . ARG   A 1 148 ? 26.750 -21.398 5.045   1.00 17.61 ?  148 ARG   A HE   1 
ATOM   3139 H HH11 . ARG   A 1 148 ? 25.285 -20.570 2.179   1.00 17.55 ?  148 ARG   A HH11 1 
ATOM   3140 H HH12 . ARG   A 1 148 ? 26.418 -19.751 1.667   1.00 17.55 ?  148 ARG   A HH12 1 
ATOM   3141 H HH21 . ARG   A 1 148 ? 28.423 -20.119 4.250   1.00 17.31 ?  148 ARG   A HH21 1 
ATOM   3142 H HH22 . ARG   A 1 148 ? 28.308 -19.477 2.911   1.00 17.31 ?  148 ARG   A HH22 1 
ATOM   3143 N N    . THR   A 1 149 ? 23.687 -17.400 7.962   1.00 12.48 ?  149 THR   A N    1 
ATOM   3144 C CA   . THR   A 1 149 ? 23.776 -16.807 9.281   1.00 12.64 ?  149 THR   A CA   1 
ATOM   3145 C C    . THR   A 1 149 ? 22.457 -16.107 9.605   1.00 12.29 ?  149 THR   A C    1 
ATOM   3146 O O    . THR   A 1 149 ? 21.512 -16.101 8.807   1.00 13.33 ?  149 THR   A O    1 
ATOM   3147 C CB   . THR   A 1 149 ? 24.975 -15.868 9.336   1.00 13.21 ?  149 THR   A CB   1 
ATOM   3148 O OG1  . THR   A 1 149 ? 24.839 -14.923 8.273   1.00 13.08 ?  149 THR   A OG1  1 
ATOM   3149 C CG2  . THR   A 1 149 ? 26.285 -16.652 9.190   1.00 13.92 ?  149 THR   A CG2  1 
ATOM   3150 H H    . THR   A 1 149 ? 24.028 -16.907 7.338   1.00 14.99 ?  149 THR   A H    1 
ATOM   3151 H HA   . THR   A 1 149 ? 23.909 -17.513 9.932   1.00 15.19 ?  149 THR   A HA   1 
ATOM   3152 H HB   . THR   A 1 149 ? 24.976 -15.406 10.187  1.00 15.87 ?  149 THR   A HB   1 
ATOM   3153 H HG1  . THR   A 1 149 ? 25.492 -14.390 8.280   1.00 15.71 ?  149 THR   A HG1  1 
ATOM   3154 H HG21 . THR   A 1 149 ? 27.039 -16.048 9.245   1.00 16.72 ?  149 THR   A HG21 1 
ATOM   3155 H HG22 . THR   A 1 149 ? 26.359 -17.314 9.898   1.00 16.72 ?  149 THR   A HG22 1 
ATOM   3156 H HG23 . THR   A 1 149 ? 26.307 -17.109 8.333   1.00 16.72 ?  149 THR   A HG23 1 
ATOM   3157 N N    . ASN   A 1 150 ? 22.353 -15.564 10.809  1.00 12.63 ?  150 ASN   A N    1 
ATOM   3158 C CA   . ASN   A 1 150 ? 21.075 -15.067 11.316  1.00 13.38 ?  150 ASN   A CA   1 
ATOM   3159 C C    . ASN   A 1 150 ? 20.883 -13.625 10.868  1.00 12.56 ?  150 ASN   A C    1 
ATOM   3160 O O    . ASN   A 1 150 ? 21.618 -12.729 11.300  1.00 14.46 ?  150 ASN   A O    1 
ATOM   3161 C CB   . ASN   A 1 150 ? 21.037 -15.192 12.834  1.00 15.83 ?  150 ASN   A CB   1 
ATOM   3162 C CG   . ASN   A 1 150 ? 20.891 -16.622 13.284  1.00 20.33 ?  150 ASN   A CG   1 
ATOM   3163 O OD1  . ASN   A 1 150 ? 20.274 -17.430 12.595  1.00 21.99 ?  150 ASN   A OD1  1 
ATOM   3164 N ND2  . ASN   A 1 150 ? 21.474 -16.954 14.433  1.00 22.80 ?  150 ASN   A ND2  1 
ATOM   3165 H H    . ASN   A 1 150 ? 23.006 -15.475 11.361  1.00 15.17 ?  150 ASN   A H    1 
ATOM   3166 H HA   . ASN   A 1 150 ? 20.350 -15.606 10.952  1.00 16.07 ?  150 ASN   A HA   1 
ATOM   3167 H HB2  . ASN   A 1 150 ? 21.863 -14.847 13.205  1.00 19.02 ?  150 ASN   A HB2  1 
ATOM   3168 H HB3  . ASN   A 1 150 ? 20.280 -14.695 13.180  1.00 19.02 ?  150 ASN   A HB3  1 
ATOM   3169 H HD21 . ASN   A 1 150 ? 21.420 -17.763 14.735  1.00 27.38 ?  150 ASN   A HD21 1 
ATOM   3170 H HD22 . ASN   A 1 150 ? 21.902 -16.363 14.889  1.00 27.38 ?  150 ASN   A HD22 1 
ATOM   3171 N N    . VAL   A 1 151 ? 19.900 -13.394 10.006  1.00 12.33 ?  151 VAL   A N    1 
ATOM   3172 C CA   . VAL   A 1 151 ? 19.691 -12.080 9.415   1.00 12.46 ?  151 VAL   A CA   1 
ATOM   3173 C C    . VAL   A 1 151 ? 18.308 -11.566 9.794   1.00 12.23 ?  151 VAL   A C    1 
ATOM   3174 O O    . VAL   A 1 151 ? 17.300 -12.277 9.659   1.00 13.34 ?  151 VAL   A O    1 
ATOM   3175 C CB   . VAL   A 1 151 ? 19.958 -12.068 7.896   1.00 13.68 ?  151 VAL   A CB   1 
ATOM   3176 C CG1  . VAL   A 1 151 ? 19.123 -13.094 7.160   1.00 14.87 ?  151 VAL   A CG1  1 
ATOM   3177 C CG2  . VAL   A 1 151 ? 19.748 -10.667 7.323   1.00 13.97 ?  151 VAL   A CG2  1 
ATOM   3178 H H    . VAL   A 1 151 ? 19.335 -13.992 9.747   1.00 14.81 ?  151 VAL   A H    1 
ATOM   3179 H HA   . VAL   A 1 151 ? 20.331 -11.474 9.809   1.00 14.96 ?  151 VAL   A HA   1 
ATOM   3180 H HB   . VAL   A 1 151 ? 20.890 -12.299 7.749   1.00 16.43 ?  151 VAL   A HB   1 
ATOM   3181 H HG11 . VAL   A 1 151 ? 19.309 -13.039 6.209   1.00 17.85 ?  151 VAL   A HG11 1 
ATOM   3182 H HG12 . VAL   A 1 151 ? 19.352 -13.984 7.486   1.00 17.85 ?  151 VAL   A HG12 1 
ATOM   3183 H HG13 . VAL   A 1 151 ? 18.183 -12.920 7.323   1.00 17.85 ?  151 VAL   A HG13 1 
ATOM   3184 H HG21 . VAL   A 1 151 ? 20.063 -10.651 6.404   1.00 16.78 ?  151 VAL   A HG21 1 
ATOM   3185 H HG22 . VAL   A 1 151 ? 18.803 -10.450 7.348   1.00 16.78 ?  151 VAL   A HG22 1 
ATOM   3186 H HG23 . VAL   A 1 151 ? 20.250 -10.029 7.853   1.00 16.78 ?  151 VAL   A HG23 1 
ATOM   3187 N N    . TYR   A 1 152 ? 18.296 -10.325 10.288  1.00 12.12 ?  152 TYR   A N    1 
ATOM   3188 C CA   . TYR   A 1 152 ? 17.109 -9.586  10.686  1.00 12.10 ?  152 TYR   A CA   1 
ATOM   3189 C C    . TYR   A 1 152 ? 16.904 -8.475  9.665   1.00 11.78 ?  152 TYR   A C    1 
ATOM   3190 O O    . TYR   A 1 152 ? 17.675 -7.511  9.619   1.00 12.32 ?  152 TYR   A O    1 
ATOM   3191 C CB   . TYR   A 1 152 ? 17.292 -9.046  12.103  1.00 12.30 ?  152 TYR   A CB   1 
ATOM   3192 C CG   . TYR   A 1 152 ? 17.253 -10.179 13.095  1.00 13.17 ?  152 TYR   A CG   1 
ATOM   3193 C CD1  . TYR   A 1 152 ? 18.383 -10.939 13.366  1.00 14.49 ?  152 TYR   A CD1  1 
ATOM   3194 C CD2  . TYR   A 1 152 ? 16.069 -10.532 13.720  1.00 13.56 ?  152 TYR   A CD2  1 
ATOM   3195 C CE1  . TYR   A 1 152 ? 18.341 -12.006 14.244  1.00 16.12 ?  152 TYR   A CE1  1 
ATOM   3196 C CE2  . TYR   A 1 152 ? 16.011 -11.608 14.604  1.00 15.02 ?  152 TYR   A CE2  1 
ATOM   3197 C CZ   . TYR   A 1 152 ? 17.153 -12.341 14.862  1.00 16.07 ?  152 TYR   A CZ   1 
ATOM   3198 O OH   . TYR   A 1 152 ? 17.100 -13.409 15.735  1.00 18.31 ?  152 TYR   A OH   1 
ATOM   3199 H H    . TYR   A 1 152 ? 19.018 -9.854  10.385  1.00 14.56 ?  152 TYR   A H    1 
ATOM   3200 H HA   . TYR   A 1 152 ? 16.341 -10.172 10.666  1.00 14.54 ?  152 TYR   A HA   1 
ATOM   3201 H HB2  . TYR   A 1 152 ? 18.147 -8.606  12.177  1.00 14.77 ?  152 TYR   A HB2  1 
ATOM   3202 H HB3  . TYR   A 1 152 ? 16.569 -8.432  12.310  1.00 14.77 ?  152 TYR   A HB3  1 
ATOM   3203 H HD1  . TYR   A 1 152 ? 19.181 -10.720 12.941  1.00 17.40 ?  152 TYR   A HD1  1 
ATOM   3204 H HD2  . TYR   A 1 152 ? 15.290 -10.045 13.542  1.00 16.28 ?  152 TYR   A HD2  1 
ATOM   3205 H HE1  . TYR   A 1 152 ? 19.111 -12.491 14.417  1.00 19.35 ?  152 TYR   A HE1  1 
ATOM   3206 H HE2  . TYR   A 1 152 ? 15.209 -11.819 15.023  1.00 18.04 ?  152 TYR   A HE2  1 
ATOM   3207 H HH   . TYR   A 1 152 ? 16.322 -13.473 16.045  1.00 21.99 ?  152 TYR   A HH   1 
ATOM   3208 N N    . LEU   A 1 153 ? 15.882 -8.629  8.832   1.00 11.84 ?  153 LEU   A N    1 
ATOM   3209 C CA   . LEU   A 1 153 ? 15.608 -7.717  7.731   1.00 12.10 ?  153 LEU   A CA   1 
ATOM   3210 C C    . LEU   A 1 153 ? 14.616 -6.645  8.155   1.00 12.49 ?  153 LEU   A C    1 
ATOM   3211 O O    . LEU   A 1 153 ? 13.523 -6.952  8.641   1.00 13.47 ?  153 LEU   A O    1 
ATOM   3212 C CB   . LEU   A 1 153 ? 15.033 -8.483  6.538   1.00 12.61 ?  153 LEU   A CB   1 
ATOM   3213 C CG   . LEU   A 1 153 ? 15.964 -9.496  5.865   1.00 12.69 ?  153 LEU   A CG   1 
ATOM   3214 C CD1  . LEU   A 1 153 ? 15.171 -10.366 4.905   1.00 13.28 ?  153 LEU   A CD1  1 
ATOM   3215 C CD2  . LEU   A 1 153 ? 17.084 -8.780  5.125   1.00 12.72 ?  153 LEU   A CD2  1 
ATOM   3216 H H    . LEU   A 1 153 ? 15.308 -9.274  8.895   1.00 14.22 ?  153 LEU   A H    1 
ATOM   3217 H HA   . LEU   A 1 153 ? 16.432 -7.298  7.463   1.00 14.54 ?  153 LEU   A HA   1 
ATOM   3218 H HB2  . LEU   A 1 153 ? 14.245 -8.963  6.838   1.00 15.14 ?  153 LEU   A HB2  1 
ATOM   3219 H HB3  . LEU   A 1 153 ? 14.774 -7.831  5.864   1.00 15.14 ?  153 LEU   A HB3  1 
ATOM   3220 H HG   . LEU   A 1 153 ? 16.360 -10.064 6.545   1.00 15.24 ?  153 LEU   A HG   1 
ATOM   3221 H HD11 . LEU   A 1 153 ? 15.746 -11.062 4.565   1.00 15.95 ?  153 LEU   A HD11 1 
ATOM   3222 H HD12 . LEU   A 1 153 ? 14.420 -10.750 5.380   1.00 15.95 ?  153 LEU   A HD12 1 
ATOM   3223 H HD13 . LEU   A 1 153 ? 14.851 -9.809  4.175   1.00 15.95 ?  153 LEU   A HD13 1 
ATOM   3224 H HD21 . LEU   A 1 153 ? 17.643 -9.442  4.695   1.00 15.28 ?  153 LEU   A HD21 1 
ATOM   3225 H HD22 . LEU   A 1 153 ? 16.694 -8.190  4.464   1.00 15.28 ?  153 LEU   A HD22 1 
ATOM   3226 H HD23 . LEU   A 1 153 ? 17.606 -8.268  5.762   1.00 15.28 ?  153 LEU   A HD23 1 
ATOM   3227 N N    A ALA   A 1 154 ? 14.992 -5.392  7.932   0.78 12.61 ?  154 ALA   A N    1 
ATOM   3228 N N    B ALA   A 1 154 ? 15.001 -5.384  7.970   0.22 12.68 ?  154 ALA   A N    1 
ATOM   3229 C CA   A ALA   A 1 154 ? 14.120 -4.249  8.157   0.78 13.57 ?  154 ALA   A CA   1 
ATOM   3230 C CA   B ALA   A 1 154 ? 14.176 -4.235  8.332   0.22 13.27 ?  154 ALA   A CA   1 
ATOM   3231 C C    A ALA   A 1 154 ? 13.619 -3.746  6.812   0.78 13.53 ?  154 ALA   A C    1 
ATOM   3232 C C    B ALA   A 1 154 ? 13.633 -3.617  7.050   0.22 13.51 ?  154 ALA   A C    1 
ATOM   3233 O O    A ALA   A 1 154 ? 14.420 -3.434  5.922   0.78 13.89 ?  154 ALA   A O    1 
ATOM   3234 O O    B ALA   A 1 154 ? 14.387 -3.018  6.274   0.22 13.27 ?  154 ALA   A O    1 
ATOM   3235 C CB   A ALA   A 1 154 ? 14.876 -3.128  8.870   0.78 14.13 ?  154 ALA   A CB   1 
ATOM   3236 C CB   B ALA   A 1 154 ? 14.988 -3.214  9.125   0.22 13.48 ?  154 ALA   A CB   1 
ATOM   3237 H H    A ALA   A 1 154 ? 15.771 -5.172  7.636   0.78 15.14 ?  154 ALA   A H    1 
ATOM   3238 H H    B ALA   A 1 154 ? 15.757 -5.164  7.624   0.22 15.23 ?  154 ALA   A H    1 
ATOM   3239 H HA   A ALA   A 1 154 ? 13.362 -4.508  8.702   0.78 16.30 ?  154 ALA   A HA   1 
ATOM   3240 H HA   B ALA   A 1 154 ? 13.429 -4.525  8.877   0.22 15.94 ?  154 ALA   A HA   1 
ATOM   3241 H HB1  A ALA   A 1 154 ? 14.278 -2.377  9.007   0.78 16.98 ?  154 ALA   A HB1  1 
ATOM   3242 H HB1  B ALA   A 1 154 ? 14.420 -2.458  9.341   0.22 16.19 ?  154 ALA   A HB1  1 
ATOM   3243 H HB2  A ALA   A 1 154 ? 15.200 -3.455  9.723   0.78 16.98 ?  154 ALA   A HB2  1 
ATOM   3244 H HB2  B ALA   A 1 154 ? 15.311 -3.630  9.940   0.22 16.19 ?  154 ALA   A HB2  1 
ATOM   3245 H HB3  A ALA   A 1 154 ? 15.628 -2.852  8.317   0.78 16.98 ?  154 ALA   A HB3  1 
ATOM   3246 H HB3  B ALA   A 1 154 ? 15.739 -2.919  8.585   0.22 16.19 ?  154 ALA   A HB3  1 
ATOM   3247 N N    A VAL   A 1 155 ? 12.301 -3.652  6.677   0.78 14.10 ?  155 VAL   A N    1 
ATOM   3248 N N    B VAL   A 1 155 ? 12.327 -3.752  6.837   0.22 14.09 ?  155 VAL   A N    1 
ATOM   3249 C CA   A VAL   A 1 155 ? 11.654 -3.174  5.463   0.78 14.97 ?  155 VAL   A CA   1 
ATOM   3250 C CA   B VAL   A 1 155 ? 11.656 -3.229  5.653   0.22 14.57 ?  155 VAL   A CA   1 
ATOM   3251 C C    A VAL   A 1 155 ? 10.914 -1.893  5.822   0.78 16.44 ?  155 VAL   A C    1 
ATOM   3252 C C    B VAL   A 1 155 ? 11.033 -1.887  6.007   0.22 15.27 ?  155 VAL   A C    1 
ATOM   3253 O O    A VAL   A 1 155 ? 9.964  -1.922  6.614   0.78 16.21 ?  155 VAL   A O    1 
ATOM   3254 O O    B VAL   A 1 155 ? 10.255 -1.787  6.963   0.22 14.62 ?  155 VAL   A O    1 
ATOM   3255 C CB   A VAL   A 1 155 ? 10.715 -4.229  4.864   0.78 14.89 ?  155 VAL   A CB   1 
ATOM   3256 C CB   B VAL   A 1 155 ? 10.594 -4.213  5.135   0.22 14.55 ?  155 VAL   A CB   1 
ATOM   3257 C CG1  A VAL   A 1 155 ? 9.995  -3.667  3.654   0.78 15.82 ?  155 VAL   A CG1  1 
ATOM   3258 C CG1  B VAL   A 1 155 ? 9.797  -3.584  4.003   0.22 14.95 ?  155 VAL   A CG1  1 
ATOM   3259 C CG2  A VAL   A 1 155 ? 11.514 -5.474  4.483   0.78 15.88 ?  155 VAL   A CG2  1 
ATOM   3260 C CG2  B VAL   A 1 155 ? 11.250 -5.507  4.676   0.22 14.68 ?  155 VAL   A CG2  1 
ATOM   3261 H H    A VAL   A 1 155 ? 11.741 -3.865  7.299   0.78 16.93 ?  155 VAL   A H    1 
ATOM   3262 H H    B VAL   A 1 155 ? 11.795 -4.146  7.384   0.22 16.92 ?  155 VAL   A H    1 
ATOM   3263 H HA   A VAL   A 1 155 ? 12.329 -2.955  4.803   0.78 17.98 ?  155 VAL   A HA   1 
ATOM   3264 H HA   B VAL   A 1 155 ? 12.308 -3.088  4.949   0.22 17.50 ?  155 VAL   A HA   1 
ATOM   3265 H HB   A VAL   A 1 155 ? 10.050 -4.484  5.528   0.78 17.88 ?  155 VAL   A HB   1 
ATOM   3266 H HB   B VAL   A 1 155 ? 9.980  -4.425  5.856   0.22 17.48 ?  155 VAL   A HB   1 
ATOM   3267 H HG11 A VAL   A 1 155 ? 9.573  -4.395  3.172   0.78 18.99 ?  155 VAL   A HG11 1 
ATOM   3268 H HG11 B VAL   A 1 155 ? 9.317  -4.283  3.532   0.22 17.96 ?  155 VAL   A HG11 1 
ATOM   3269 H HG12 A VAL   A 1 155 ? 9.317  -3.036  3.951   0.78 18.99 ?  155 VAL   A HG12 1 
ATOM   3270 H HG12 B VAL   A 1 155 ? 9.168  -2.944  4.372   0.22 17.96 ?  155 VAL   A HG12 1 
ATOM   3271 H HG13 A VAL   A 1 155 ? 10.637 -3.220  3.084   0.78 18.99 ?  155 VAL   A HG13 1 
ATOM   3272 H HG13 B VAL   A 1 155 ? 10.409 -3.138  3.396   0.22 17.96 ?  155 VAL   A HG13 1 
ATOM   3273 H HG21 A VAL   A 1 155 ? 10.917 -6.118  4.075   0.78 19.08 ?  155 VAL   A HG21 1 
ATOM   3274 H HG21 B VAL   A 1 155 ? 10.566 -6.102  4.333   0.22 17.63 ?  155 VAL   A HG21 1 
ATOM   3275 H HG22 A VAL   A 1 155 ? 12.207 -5.217  3.853   0.78 19.08 ?  155 VAL   A HG22 1 
ATOM   3276 H HG22 B VAL   A 1 155 ? 11.892 -5.303  3.978   0.22 17.63 ?  155 VAL   A HG22 1 
ATOM   3277 H HG23 A VAL   A 1 155 ? 11.915 -5.848  5.282   0.78 19.08 ?  155 VAL   A HG23 1 
ATOM   3278 H HG23 B VAL   A 1 155 ? 11.700 -5.918  5.430   0.22 17.63 ?  155 VAL   A HG23 1 
ATOM   3279 N N    A PHE   A 1 156 ? 11.359 -0.768  5.254   0.78 18.31 ?  156 PHE   A N    1 
ATOM   3280 N N    B PHE   A 1 156 ? 11.365 -0.857  5.228   0.22 16.62 ?  156 PHE   A N    1 
ATOM   3281 C CA   A PHE   A 1 156 ? 10.810 0.538   5.618   0.78 20.09 ?  156 PHE   A CA   1 
ATOM   3282 C CA   B PHE   A 1 156 ? 10.912 0.494   5.537   0.22 17.91 ?  156 PHE   A CA   1 
ATOM   3283 C C    A PHE   A 1 156 ? 9.341  0.671   5.231   0.78 20.30 ?  156 PHE   A C    1 
ATOM   3284 C C    B PHE   A 1 156 ? 9.491  0.741   5.045   0.22 18.34 ?  156 PHE   A C    1 
ATOM   3285 O O    A PHE   A 1 156 ? 8.532  1.191   6.009   0.78 21.11 ?  156 PHE   A O    1 
ATOM   3286 O O    B PHE   A 1 156 ? 8.671  1.317   5.769   0.22 18.70 ?  156 PHE   A O    1 
ATOM   3287 C CB   A PHE   A 1 156 ? 11.636 1.632   4.940   0.78 21.91 ?  156 PHE   A CB   1 
ATOM   3288 C CB   B PHE   A 1 156 ? 11.873 1.502   4.911   0.22 18.72 ?  156 PHE   A CB   1 
ATOM   3289 C CG   A PHE   A 1 156 ? 11.174 3.026   5.252   0.78 23.94 ?  156 PHE   A CG   1 
ATOM   3290 C CG   B PHE   A 1 156 ? 11.600 2.926   5.297   0.22 19.66 ?  156 PHE   A CG   1 
ATOM   3291 C CD1  A PHE   A 1 156 ? 11.152 3.476   6.559   0.78 25.10 ?  156 PHE   A CD1  1 
ATOM   3292 C CD1  B PHE   A 1 156 ? 11.786 3.353   6.599   0.22 20.13 ?  156 PHE   A CD1  1 
ATOM   3293 C CD2  A PHE   A 1 156 ? 10.777 3.889   4.240   0.78 25.36 ?  156 PHE   A CD2  1 
ATOM   3294 C CD2  B PHE   A 1 156 ? 11.177 3.841   4.352   0.22 20.13 ?  156 PHE   A CD2  1 
ATOM   3295 C CE1  A PHE   A 1 156 ? 10.733 4.757   6.858   0.78 26.00 ?  156 PHE   A CE1  1 
ATOM   3296 C CE1  B PHE   A 1 156 ? 11.536 4.671   6.955   0.22 20.29 ?  156 PHE   A CE1  1 
ATOM   3297 C CE2  A PHE   A 1 156 ? 10.358 5.177   4.531   0.78 26.35 ?  156 PHE   A CE2  1 
ATOM   3298 C CE2  B PHE   A 1 156 ? 10.937 5.158   4.697   0.22 20.35 ?  156 PHE   A CE2  1 
ATOM   3299 C CZ   A PHE   A 1 156 ? 10.340 5.612   5.843   0.78 26.34 ?  156 PHE   A CZ   1 
ATOM   3300 C CZ   B PHE   A 1 156 ? 11.124 5.574   5.999   0.22 20.29 ?  156 PHE   A CZ   1 
ATOM   3301 H H    A PHE   A 1 156 ? 11.986 -0.734  4.670   0.78 21.99 ?  156 PHE   A H    1 
ATOM   3302 H H    B PHE   A 1 156 ? 11.848 -0.916  4.520   0.22 19.96 ?  156 PHE   A H    1 
ATOM   3303 H HA   A PHE   A 1 156 ? 10.880 0.661   6.576   0.78 24.13 ?  156 PHE   A HA   1 
ATOM   3304 H HA   B PHE   A 1 156 ? 10.925 0.621   6.497   0.22 21.51 ?  156 PHE   A HA   1 
ATOM   3305 H HB2  A PHE   A 1 156 ? 12.558 1.556   5.230   0.78 26.31 ?  156 PHE   A HB2  1 
ATOM   3306 H HB2  B PHE   A 1 156 ? 12.776 1.287   5.192   0.22 22.48 ?  156 PHE   A HB2  1 
ATOM   3307 H HB3  A PHE   A 1 156 ? 11.584 1.515   3.978   0.78 26.31 ?  156 PHE   A HB3  1 
ATOM   3308 H HB3  B PHE   A 1 156 ? 11.808 1.442   3.944   0.22 22.48 ?  156 PHE   A HB3  1 
ATOM   3309 H HD1  A PHE   A 1 156 ? 11.416 2.906   7.245   0.78 30.14 ?  156 PHE   A HD1  1 
ATOM   3310 H HD1  B PHE   A 1 156 ? 12.086 2.750   7.245   0.22 24.17 ?  156 PHE   A HD1  1 
ATOM   3311 H HD2  A PHE   A 1 156 ? 10.793 3.598   3.356   0.78 30.44 ?  156 PHE   A HD2  1 
ATOM   3312 H HD2  B PHE   A 1 156 ? 11.051 3.566   3.473   0.22 24.17 ?  156 PHE   A HD2  1 
ATOM   3313 H HE1  A PHE   A 1 156 ? 10.719 5.049   7.742   0.78 31.21 ?  156 PHE   A HE1  1 
ATOM   3314 H HE1  B PHE   A 1 156 ? 11.685 4.947   7.832   0.22 24.36 ?  156 PHE   A HE1  1 
ATOM   3315 H HE2  A PHE   A 1 156 ? 10.094 5.746   3.846   0.78 31.63 ?  156 PHE   A HE2  1 
ATOM   3316 H HE2  B PHE   A 1 156 ? 10.649 5.761   4.051   0.22 24.43 ?  156 PHE   A HE2  1 
ATOM   3317 H HZ   A PHE   A 1 156 ? 10.055 6.474   6.043   0.78 31.62 ?  156 PHE   A HZ   1 
ATOM   3318 H HZ   B PHE   A 1 156 ? 10.965 6.458   6.234   0.22 24.36 ?  156 PHE   A HZ   1 
ATOM   3319 N N    A ASP   A 1 157 ? 8.985  0.225   4.030   0.78 20.30 ?  157 ASP   A N    1 
ATOM   3320 N N    B ASP   A 1 157 ? 9.187  0.320   3.821   0.22 18.41 ?  157 ASP   A N    1 
ATOM   3321 C CA   A ASP   A 1 157 ? 7.663  0.472   3.467   0.78 21.52 ?  157 ASP   A CA   1 
ATOM   3322 C CA   B ASP   A 1 157 ? 7.885  0.576   3.224   0.22 18.55 ?  157 ASP   A CA   1 
ATOM   3323 C C    A ASP   A 1 157 ? 6.677  -0.576  3.976   0.78 21.26 ?  157 ASP   A C    1 
ATOM   3324 C C    B ASP   A 1 157 ? 6.851  -0.398  3.777   0.22 19.23 ?  157 ASP   A C    1 
ATOM   3325 O O    A ASP   A 1 157 ? 6.848  -1.773  3.712   0.78 20.54 ?  157 ASP   A O    1 
ATOM   3326 O O    B ASP   A 1 157 ? 7.038  -1.618  3.720   0.22 19.14 ?  157 ASP   A O    1 
ATOM   3327 C CB   A ASP   A 1 157 ? 7.767  0.418   1.945   0.78 23.09 ?  157 ASP   A CB   1 
ATOM   3328 C CB   B ASP   A 1 157 ? 7.985  0.438   1.707   0.22 17.98 ?  157 ASP   A CB   1 
ATOM   3329 C CG   A ASP   A 1 157 ? 6.534  0.953   1.259   0.78 25.14 ?  157 ASP   A CG   1 
ATOM   3330 C CG   B ASP   A 1 157 ? 6.745  0.918   0.997   0.22 17.55 ?  157 ASP   A CG   1 
ATOM   3331 O OD1  A ASP   A 1 157 ? 6.377  2.189   1.196   0.78 26.93 ?  157 ASP   A OD1  1 
ATOM   3332 O OD1  B ASP   A 1 157 ? 5.663  0.334   1.221   0.22 17.75 ?  157 ASP   A OD1  1 
ATOM   3333 O OD2  A ASP   A 1 157 ? 5.713  0.135   0.787   0.78 25.59 -1 157 ASP   A OD2  1 
ATOM   3334 O OD2  B ASP   A 1 157 ? 6.851  1.891   0.222   0.22 17.00 -1 157 ASP   A OD2  1 
ATOM   3335 H H    A ASP   A 1 157 ? 9.503  -0.230  3.514   0.78 24.38 ?  157 ASP   A H    1 
ATOM   3336 H H    B ASP   A 1 157 ? 9.726  -0.114  3.311   0.22 22.11 ?  157 ASP   A H    1 
ATOM   3337 H HA   A ASP   A 1 157 ? 7.352  1.351   3.728   0.78 25.84 ?  157 ASP   A HA   1 
ATOM   3338 H HA   B ASP   A 1 157 ? 7.601  1.479   3.429   0.22 22.27 ?  157 ASP   A HA   1 
ATOM   3339 H HB2  A ASP   A 1 157 ? 8.540  0.939   1.664   0.78 27.72 ?  157 ASP   A HB2  1 
ATOM   3340 H HB2  B ASP   A 1 157 ? 8.733  0.963   1.387   0.22 21.59 ?  157 ASP   A HB2  1 
ATOM   3341 H HB3  A ASP   A 1 157 ? 7.880  -0.503  1.667   0.78 27.72 ?  157 ASP   A HB3  1 
ATOM   3342 H HB3  B ASP   A 1 157 ? 8.124  -0.493  1.482   0.22 21.59 ?  157 ASP   A HB3  1 
ATOM   3343 N N    A LYS   A 1 158 ? 5.646  -0.129  4.703   0.78 22.62 ?  158 LYS   A N    1 
ATOM   3344 N N    B LYS   A 1 158 ? 5.755  0.147   4.310   0.22 20.20 ?  158 LYS   A N    1 
ATOM   3345 C CA   A LYS   A 1 158 ? 4.676  -1.064  5.267   0.78 23.49 ?  158 LYS   A CA   1 
ATOM   3346 C CA   B LYS   A 1 158 ? 4.727  -0.697  4.910   0.22 21.12 ?  158 LYS   A CA   1 
ATOM   3347 C C    A LYS   A 1 158 ? 3.954  -1.834  4.168   0.78 22.82 ?  158 LYS   A C    1 
ATOM   3348 C C    B LYS   A 1 158 ? 4.037  -1.564  3.863   0.22 21.46 ?  158 LYS   A C    1 
ATOM   3349 O O    A LYS   A 1 158 ? 3.774  -3.054  4.267   0.78 22.61 ?  158 LYS   A O    1 
ATOM   3350 O O    B LYS   A 1 158 ? 3.804  -2.756  4.092   0.22 21.42 ?  158 LYS   A O    1 
ATOM   3351 C CB   A LYS   A 1 158 ? 3.685  -0.315  6.163   0.78 24.85 ?  158 LYS   A CB   1 
ATOM   3352 C CB   B LYS   A 1 158 ? 3.707  0.168   5.652   0.22 21.73 ?  158 LYS   A CB   1 
ATOM   3353 C CG   A LYS   A 1 158 ? 2.472  -1.135  6.609   0.78 26.62 ?  158 LYS   A CG   1 
ATOM   3354 C CG   B LYS   A 1 158 ? 2.521  -0.612  6.205   0.22 22.31 ?  158 LYS   A CG   1 
ATOM   3355 C CD   A LYS   A 1 158 ? 2.865  -2.381  7.397   0.78 28.11 ?  158 LYS   A CD   1 
ATOM   3356 C CD   B LYS   A 1 158 ? 1.530  0.298   6.908   0.22 22.81 ?  158 LYS   A CD   1 
ATOM   3357 C CE   A LYS   A 1 158 ? 1.629  -3.076  7.958   0.78 29.20 ?  158 LYS   A CE   1 
ATOM   3358 C CE   B LYS   A 1 158 ? 0.321  -0.478  7.406   0.22 23.13 ?  158 LYS   A CE   1 
ATOM   3359 N NZ   A LYS   A 1 158 ? 1.931  -4.407  8.555   0.78 29.77 ?  158 LYS   A NZ   1 
ATOM   3360 N NZ   B LYS   A 1 158 ? -0.450 -1.100  6.294   0.22 23.32 ?  158 LYS   A NZ   1 
ATOM   3361 H H    A LYS   A 1 158 ? 5.496  0.698   4.877   0.78 27.16 ?  158 LYS   A H    1 
ATOM   3362 H H    B LYS   A 1 158 ? 5.587  0.989   4.335   0.22 24.25 ?  158 LYS   A H    1 
ATOM   3363 H HA   A LYS   A 1 158 ? 5.147  -1.705  5.823   0.78 28.20 ?  158 LYS   A HA   1 
ATOM   3364 H HA   B LYS   A 1 158 ? 5.142  -1.285  5.559   0.22 25.36 ?  158 LYS   A HA   1 
ATOM   3365 H HB2  A LYS   A 1 158 ? 4.150  -0.021  6.965   0.78 29.83 ?  158 LYS   A HB2  1 
ATOM   3366 H HB2  B LYS   A 1 158 ? 4.150  0.601   6.401   0.22 26.09 ?  158 LYS   A HB2  1 
ATOM   3367 H HB3  A LYS   A 1 158 ? 3.356  0.461   5.681   0.78 29.83 ?  158 LYS   A HB3  1 
ATOM   3368 H HB3  B LYS   A 1 158 ? 3.362  0.839   5.044   0.22 26.09 ?  158 LYS   A HB3  1 
ATOM   3369 H HG2  A LYS   A 1 158 ? 1.917  -0.583  7.181   0.78 31.96 ?  158 LYS   A HG2  1 
ATOM   3370 H HG2  B LYS   A 1 158 ? 2.056  -1.052  5.477   0.22 26.78 ?  158 LYS   A HG2  1 
ATOM   3371 H HG3  A LYS   A 1 158 ? 1.965  -1.412  5.830   0.78 31.96 ?  158 LYS   A HG3  1 
ATOM   3372 H HG3  B LYS   A 1 158 ? 2.841  -1.267  6.845   0.22 26.78 ?  158 LYS   A HG3  1 
ATOM   3373 H HD2  A LYS   A 1 158 ? 3.326  -3.001  6.812   0.78 33.75 ?  158 LYS   A HD2  1 
ATOM   3374 H HD2  B LYS   A 1 158 ? 1.962  0.714   7.670   0.22 27.39 ?  158 LYS   A HD2  1 
ATOM   3375 H HD3  A LYS   A 1 158 ? 3.438  -2.124  8.137   0.78 33.75 ?  158 LYS   A HD3  1 
ATOM   3376 H HD3  B LYS   A 1 158 ? 1.222  0.977   6.286   0.22 27.39 ?  158 LYS   A HD3  1 
ATOM   3377 H HE2  A LYS   A 1 158 ? 1.233  -2.516  8.645   0.78 35.06 ?  158 LYS   A HE2  1 
ATOM   3378 H HE2  B LYS   A 1 158 ? 0.620  -1.186  7.998   0.22 27.77 ?  158 LYS   A HE2  1 
ATOM   3379 H HE3  A LYS   A 1 158 ? 0.994  -3.208  7.240   0.78 35.06 ?  158 LYS   A HE3  1 
ATOM   3380 H HE3  B LYS   A 1 158 ? -0.270 0.126   7.881   0.22 27.77 ?  158 LYS   A HE3  1 
ATOM   3381 H HZ1  A LYS   A 1 158 ? 1.184  -4.775  8.869   0.78 35.74 ?  158 LYS   A HZ1  1 
ATOM   3382 H HZ1  B LYS   A 1 158 ? -1.170 -1.512  6.617   0.22 28.00 ?  158 LYS   A HZ1  1 
ATOM   3383 H HZ2  A LYS   A 1 158 ? 2.279  -4.944  7.935   0.78 35.74 ?  158 LYS   A HZ2  1 
ATOM   3384 H HZ2  B LYS   A 1 158 ? -0.709 -0.474  5.717   0.22 28.00 ?  158 LYS   A HZ2  1 
ATOM   3385 H HZ3  A LYS   A 1 158 ? 2.514  -4.318  9.221   0.78 35.74 ?  158 LYS   A HZ3  1 
ATOM   3386 H HZ3  B LYS   A 1 158 ? 0.056  -1.695  5.868   0.22 28.00 ?  158 LYS   A HZ3  1 
ATOM   3387 N N    A ASN   A 1 159 ? 3.540  -1.142  3.107   0.78 23.14 ?  159 ASN   A N    1 
ATOM   3388 N N    B ASN   A 1 159 ? 3.699  -0.984  2.709   0.22 22.01 ?  159 ASN   A N    1 
ATOM   3389 C CA   A ASN   A 1 159 ? 2.879  -1.832  2.006   0.78 23.52 ?  159 ASN   A CA   1 
ATOM   3390 C CA   B ASN   A 1 159 ? 2.991  -1.747  1.687   0.22 22.66 ?  159 ASN   A CA   1 
ATOM   3391 C C    A ASN   A 1 159 ? 3.783  -2.910  1.412   0.78 22.23 ?  159 ASN   A C    1 
ATOM   3392 C C    B ASN   A 1 159 ? 3.890  -2.786  1.030   0.22 22.03 ?  159 ASN   A C    1 
ATOM   3393 O O    A ASN   A 1 159 ? 3.335  -4.030  1.140   0.78 21.53 ?  159 ASN   A O    1 
ATOM   3394 O O    B ASN   A 1 159 ? 3.410  -3.854  0.635   0.22 21.89 ?  159 ASN   A O    1 
ATOM   3395 C CB   A ASN   A 1 159 ? 2.422  -0.818  0.953   0.78 25.56 ?  159 ASN   A CB   1 
ATOM   3396 C CB   B ASN   A 1 159 ? 2.386  -0.805  0.648   0.22 23.99 ?  159 ASN   A CB   1 
ATOM   3397 C CG   A ASN   A 1 159 ? 1.193  -0.036  1.394   0.78 28.04 ?  159 ASN   A CG   1 
ATOM   3398 C CG   B ASN   A 1 159 ? 1.233  0.008   1.205   0.22 25.19 ?  159 ASN   A CG   1 
ATOM   3399 O OD1  A ASN   A 1 159 ? 0.339  -0.563  2.105   0.78 29.02 ?  159 ASN   A OD1  1 
ATOM   3400 O OD1  B ASN   A 1 159 ? 0.472  -0.472  2.045   0.22 25.65 ?  159 ASN   A OD1  1 
ATOM   3401 N ND2  A ASN   A 1 159 ? 1.098  1.223   0.972   0.78 29.11 ?  159 ASN   A ND2  1 
ATOM   3402 N ND2  B ASN   A 1 159 ? 1.099  1.243   0.743   0.22 25.63 ?  159 ASN   A ND2  1 
ATOM   3403 H H    A ASN   A 1 159 ? 3.632  -0.293  3.007   0.78 27.78 ?  159 ASN   A H    1 
ATOM   3404 H H    B ASN   A 1 159 ? 3.863  -0.168  2.502   0.22 26.43 ?  159 ASN   A H    1 
ATOM   3405 H HA   A ASN   A 1 159 ? 2.086  -2.271  2.351   0.78 28.24 ?  159 ASN   A HA   1 
ATOM   3406 H HA   B ASN   A 1 159 ? 2.261  -2.224  2.109   0.22 27.20 ?  159 ASN   A HA   1 
ATOM   3407 H HB2  A ASN   A 1 159 ? 3.135  -0.182  0.791   0.78 30.68 ?  159 ASN   A HB2  1 
ATOM   3408 H HB2  B ASN   A 1 159 ? 3.069  -0.188  0.344   0.22 28.80 ?  159 ASN   A HB2  1 
ATOM   3409 H HB3  A ASN   A 1 159 ? 2.200  -1.289  0.136   0.78 30.68 ?  159 ASN   A HB3  1 
ATOM   3410 H HB3  B ASN   A 1 159 ? 2.054  -1.329  -0.098  0.22 28.80 ?  159 ASN   A HB3  1 
ATOM   3411 H HD21 A ASN   A 1 159 ? 0.421  1.702   1.195   0.78 34.95 ?  159 ASN   A HD21 1 
ATOM   3412 H HD21 B ASN   A 1 159 ? 0.460  1.741   1.030   0.22 30.77 ?  159 ASN   A HD21 1 
ATOM   3413 H HD22 A ASN   A 1 159 ? 1.716  1.558   0.479   0.78 34.95 ?  159 ASN   A HD22 1 
ATOM   3414 H HD22 B ASN   A 1 159 ? 1.651  1.544   0.158   0.22 30.77 ?  159 ASN   A HD22 1 
ATOM   3415 N N    A LEU   A 1 160 ? 5.069  -2.604  1.239   0.78 20.55 ?  160 LEU   A N    1 
ATOM   3416 N N    B LEU   A 1 160 ? 5.187  -2.498  0.898   0.22 21.44 ?  160 LEU   A N    1 
ATOM   3417 C CA   A LEU   A 1 160 ? 5.987  -3.600  0.698   0.78 19.55 ?  160 LEU   A CA   1 
ATOM   3418 C CA   B LEU   A 1 160 ? 6.115  -3.524  0.432   0.22 20.98 ?  160 LEU   A CA   1 
ATOM   3419 C C    A LEU   A 1 160 ? 6.174  -4.761  1.664   0.78 18.30 ?  160 LEU   A C    1 
ATOM   3420 C C    B LEU   A 1 160 ? 6.254  -4.638  1.459   0.22 19.98 ?  160 LEU   A C    1 
ATOM   3421 O O    A LEU   A 1 160 ? 6.194  -5.926  1.247   0.78 18.83 ?  160 LEU   A O    1 
ATOM   3422 O O    B LEU   A 1 160 ? 6.293  -5.821  1.101   0.22 19.86 ?  160 LEU   A O    1 
ATOM   3423 C CB   A LEU   A 1 160 ? 7.330  -2.955  0.368   0.78 19.47 ?  160 LEU   A CB   1 
ATOM   3424 C CB   B LEU   A 1 160 ? 7.478  -2.904  0.125   0.22 21.38 ?  160 LEU   A CB   1 
ATOM   3425 C CG   A LEU   A 1 160 ? 8.404  -3.941  -0.088  0.78 19.73 ?  160 LEU   A CG   1 
ATOM   3426 C CG   B LEU   A 1 160 ? 7.583  -2.054  -1.144  0.22 21.74 ?  160 LEU   A CG   1 
ATOM   3427 C CD1  A LEU   A 1 160 ? 7.951  -4.687  -1.327  0.78 20.22 ?  160 LEU   A CD1  1 
ATOM   3428 C CD1  B LEU   A 1 160 ? 8.967  -1.438  -1.261  0.22 21.86 ?  160 LEU   A CD1  1 
ATOM   3429 C CD2  A LEU   A 1 160 ? 9.714  -3.219  -0.346  0.78 19.71 ?  160 LEU   A CD2  1 
ATOM   3430 C CD2  B LEU   A 1 160 ? 7.271  -2.894  -2.372  0.22 21.89 ?  160 LEU   A CD2  1 
ATOM   3431 H H    A LEU   A 1 160 ? 5.427  -1.844  1.433   0.78 24.68 ?  160 LEU   A H    1 
ATOM   3432 H H    B LEU   A 1 160 ? 5.544  -1.734  1.066   0.22 25.75 ?  160 LEU   A H    1 
ATOM   3433 H HA   A LEU   A 1 160 ? 5.613  -3.951  -0.119  0.78 23.47 ?  160 LEU   A HA   1 
ATOM   3434 H HA   B LEU   A 1 160 ? 5.771  -3.912  -0.384  0.22 25.19 ?  160 LEU   A HA   1 
ATOM   3435 H HB2  A LEU   A 1 160 ? 7.201  -2.301  -0.339  0.78 23.37 ?  160 LEU   A HB2  1 
ATOM   3436 H HB2  B LEU   A 1 160 ? 7.734  -2.352  0.877   0.22 25.67 ?  160 LEU   A HB2  1 
ATOM   3437 H HB3  A LEU   A 1 160 ? 7.664  -2.518  1.164   0.78 23.37 ?  160 LEU   A HB3  1 
ATOM   3438 H HB3  B LEU   A 1 160 ? 8.119  -3.622  0.032   0.22 25.67 ?  160 LEU   A HB3  1 
ATOM   3439 H HG   A LEU   A 1 160 ? 8.564  -4.591  0.613   0.78 23.69 ?  160 LEU   A HG   1 
ATOM   3440 H HG   B LEU   A 1 160 ? 6.938  -1.332  -1.101  0.22 26.10 ?  160 LEU   A HG   1 
ATOM   3441 H HD11 A LEU   A 1 160 ? 8.689  -5.221  -1.657  0.78 24.28 ?  160 LEU   A HD11 1 
ATOM   3442 H HD11 B LEU   A 1 160 ? 9.016  -0.923  -2.082  0.22 26.25 ?  160 LEU   A HD11 1 
ATOM   3443 H HD12 A LEU   A 1 160 ? 7.205  -5.261  -1.095  0.78 24.28 ?  160 LEU   A HD12 1 
ATOM   3444 H HD12 B LEU   A 1 160 ? 9.123  -0.860  -0.499  0.22 26.25 ?  160 LEU   A HD12 1 
ATOM   3445 H HD13 A LEU   A 1 160 ? 7.680  -4.043  -2.000  0.78 24.28 ?  160 LEU   A HD13 1 
ATOM   3446 H HD13 B LEU   A 1 160 ? 9.628  -2.148  -1.278  0.22 26.25 ?  160 LEU   A HD13 1 
ATOM   3447 H HD21 A LEU   A 1 160 ? 10.380 -3.865  -0.632  0.78 23.67 ?  160 LEU   A HD21 1 
ATOM   3448 H HD21 B LEU   A 1 160 ? 7.526  -2.399  -3.166  0.22 26.28 ?  160 LEU   A HD21 1 
ATOM   3449 H HD22 A LEU   A 1 160 ? 9.578  -2.555  -1.040  0.78 23.67 ?  160 LEU   A HD22 1 
ATOM   3450 H HD22 B LEU   A 1 160 ? 7.775  -3.722  -2.323  0.22 26.28 ?  160 LEU   A HD22 1 
ATOM   3451 H HD23 A LEU   A 1 160 ? 10.004 -2.787  0.473   0.78 23.67 ?  160 LEU   A HD23 1 
ATOM   3452 H HD23 B LEU   A 1 160 ? 6.322  -3.086  -2.391  0.22 26.28 ?  160 LEU   A HD23 1 
ATOM   3453 N N    A TYR   A 1 161 ? 6.321  -4.467  2.956   0.78 17.23 ?  161 TYR   A N    1 
ATOM   3454 N N    B TYR   A 1 161 ? 6.331  -4.278  2.742   0.22 19.21 ?  161 TYR   A N    1 
ATOM   3455 C CA   A TYR   A 1 161 ? 6.460  -5.526  3.949   0.78 17.07 ?  161 TYR   A CA   1 
ATOM   3456 C CA   B TYR   A 1 161 ? 6.399  -5.282  3.798   0.22 18.68 ?  161 TYR   A CA   1 
ATOM   3457 C C    A TYR   A 1 161 ? 5.309  -6.525  3.857   0.78 17.76 ?  161 TYR   A C    1 
ATOM   3458 C C    B TYR   A 1 161 ? 5.210  -6.232  3.724   0.22 18.33 ?  161 TYR   A C    1 
ATOM   3459 O O    A TYR   A 1 161 ? 5.524  -7.740  3.834   0.78 17.64 ?  161 TYR   A O    1 
ATOM   3460 O O    B TYR   A 1 161 ? 5.369  -7.455  3.818   0.22 17.83 ?  161 TYR   A O    1 
ATOM   3461 C CB   A TYR   A 1 161 ? 6.557  -4.915  5.350   0.78 17.16 ?  161 TYR   A CB   1 
ATOM   3462 C CB   B TYR   A 1 161 ? 6.457  -4.584  5.156   0.22 18.82 ?  161 TYR   A CB   1 
ATOM   3463 C CG   A TYR   A 1 161 ? 6.459  -5.928  6.457   0.78 16.64 ?  161 TYR   A CG   1 
ATOM   3464 C CG   B TYR   A 1 161 ? 6.160  -5.481  6.334   0.22 19.05 ?  161 TYR   A CG   1 
ATOM   3465 C CD1  A TYR   A 1 161 ? 7.581  -6.625  6.893   0.78 16.17 ?  161 TYR   A CD1  1 
ATOM   3466 C CD1  B TYR   A 1 161 ? 7.143  -6.296  6.880   0.22 19.33 ?  161 TYR   A CD1  1 
ATOM   3467 C CD2  A TYR   A 1 161 ? 5.244  -6.192  7.069   0.78 16.49 ?  161 TYR   A CD2  1 
ATOM   3468 C CD2  B TYR   A 1 161 ? 4.902  -5.486  6.926   0.22 19.32 ?  161 TYR   A CD2  1 
ATOM   3469 C CE1  A TYR   A 1 161 ? 7.487  -7.565  7.900   0.78 16.06 ?  161 TYR   A CE1  1 
ATOM   3470 C CE1  B TYR   A 1 161 ? 6.875  -7.104  7.969   0.22 19.69 ?  161 TYR   A CE1  1 
ATOM   3471 C CE2  A TYR   A 1 161 ? 5.139  -7.126  8.074   0.78 16.29 ?  161 TYR   A CE2  1 
ATOM   3472 C CE2  B TYR   A 1 161 ? 4.628  -6.286  8.015   0.22 19.73 ?  161 TYR   A CE2  1 
ATOM   3473 C CZ   A TYR   A 1 161 ? 6.262  -7.811  8.488   0.78 16.51 ?  161 TYR   A CZ   1 
ATOM   3474 C CZ   B TYR   A 1 161 ? 5.616  -7.094  8.532   0.22 19.93 ?  161 TYR   A CZ   1 
ATOM   3475 O OH   A TYR   A 1 161 ? 6.166  -8.747  9.494   0.78 17.44 ?  161 TYR   A OH   1 
ATOM   3476 O OH   B TYR   A 1 161 ? 5.340  -7.895  9.616   0.22 20.42 ?  161 TYR   A OH   1 
ATOM   3477 H H    A TYR   A 1 161 ? 6.336  -3.676  3.284   0.78 20.69 ?  161 TYR   A H    1 
ATOM   3478 H H    B TYR   A 1 161 ? 6.346  -3.466  3.022   0.22 23.06 ?  161 TYR   A H    1 
ATOM   3479 H HA   A TYR   A 1 161 ? 7.284  -6.012  3.782   0.78 20.50 ?  161 TYR   A HA   1 
ATOM   3480 H HA   B TYR   A 1 161 ? 7.212  -5.801  3.694   0.22 22.43 ?  161 TYR   A HA   1 
ATOM   3481 H HB2  A TYR   A 1 161 ? 7.414  -4.469  5.438   0.78 20.60 ?  161 TYR   A HB2  1 
ATOM   3482 H HB2  B TYR   A 1 161 ? 7.348  -4.219  5.282   0.22 22.59 ?  161 TYR   A HB2  1 
ATOM   3483 H HB3  A TYR   A 1 161 ? 5.837  -4.282  5.469   0.78 20.60 ?  161 TYR   A HB3  1 
ATOM   3484 H HB3  B TYR   A 1 161 ? 5.808  -3.863  5.165   0.22 22.59 ?  161 TYR   A HB3  1 
ATOM   3485 H HD1  A TYR   A 1 161 ? 8.406  -6.467  6.496   0.78 19.41 ?  161 TYR   A HD1  1 
ATOM   3486 H HD1  B TYR   A 1 161 ? 7.993  -6.302  6.504   0.22 23.21 ?  161 TYR   A HD1  1 
ATOM   3487 H HD2  A TYR   A 1 161 ? 4.483  -5.742  6.792   0.78 19.80 ?  161 TYR   A HD2  1 
ATOM   3488 H HD2  B TYR   A 1 161 ? 4.235  -4.936  6.585   0.22 23.20 ?  161 TYR   A HD2  1 
ATOM   3489 H HE1  A TYR   A 1 161 ? 8.244  -8.029  8.187   0.78 19.28 ?  161 TYR   A HE1  1 
ATOM   3490 H HE1  B TYR   A 1 161 ? 7.540  -7.649  8.321   0.22 23.64 ?  161 TYR   A HE1  1 
ATOM   3491 H HE2  A TYR   A 1 161 ? 4.311  -7.295  8.476   0.78 19.56 ?  161 TYR   A HE2  1 
ATOM   3492 H HE2  B TYR   A 1 161 ? 3.780  -6.279  8.398   0.22 23.68 ?  161 TYR   A HE2  1 
ATOM   3493 H HH   A TYR   A 1 161 ? 6.912  -9.090  9.654   0.78 20.94 ?  161 TYR   A HH   1 
ATOM   3494 H HH   B TYR   A 1 161 ? 4.544  -7.785  9.856   0.22 24.52 ?  161 TYR   A HH   1 
ATOM   3495 N N    A ASP   A 1 162 ? 4.074  -6.032  3.793   0.78 18.67 ?  162 ASP   A N    1 
ATOM   3496 N N    B ASP   A 1 162 ? 4.006  -5.685  3.549   0.22 18.39 ?  162 ASP   A N    1 
ATOM   3497 C CA   A ASP   A 1 162 ? 2.927  -6.936  3.738   0.78 19.54 ?  162 ASP   A CA   1 
ATOM   3498 C CA   B ASP   A 1 162 ? 2.821  -6.531  3.439   0.22 18.74 ?  162 ASP   A CA   1 
ATOM   3499 C C    A ASP   A 1 162 ? 2.955  -7.794  2.478   0.78 19.53 ?  162 ASP   A C    1 
ATOM   3500 C C    B ASP   A 1 162 ? 2.918  -7.457  2.233   0.22 19.21 ?  162 ASP   A C    1 
ATOM   3501 O O    A ASP   A 1 162 ? 2.597  -8.978  2.515   0.78 20.20 ?  162 ASP   A O    1 
ATOM   3502 O O    B ASP   A 1 162 ? 2.564  -8.639  2.317   0.22 19.16 ?  162 ASP   A O    1 
ATOM   3503 C CB   A ASP   A 1 162 ? 1.620  -6.143  3.803   0.78 20.52 ?  162 ASP   A CB   1 
ATOM   3504 C CB   B ASP   A 1 162 ? 1.564  -5.666  3.340   0.22 18.93 ?  162 ASP   A CB   1 
ATOM   3505 C CG   A ASP   A 1 162 ? 1.332  -5.579  5.183   0.78 21.84 ?  162 ASP   A CG   1 
ATOM   3506 C CG   B ASP   A 1 162 ? 1.256  -4.923  4.630   0.22 18.91 ?  162 ASP   A CG   1 
ATOM   3507 O OD1  A ASP   A 1 162 ? 1.997  -5.986  6.158   0.78 22.78 ?  162 ASP   A OD1  1 
ATOM   3508 O OD1  B ASP   A 1 162 ? 1.703  -5.375  5.705   0.22 18.83 ?  162 ASP   A OD1  1 
ATOM   3509 O OD2  A ASP   A 1 162 ? 0.423  -4.725  5.288   0.78 22.91 -1 162 ASP   A OD2  1 
ATOM   3510 O OD2  B ASP   A 1 162 ? 0.558  -3.888  4.571   0.22 19.13 -1 162 ASP   A OD2  1 
ATOM   3511 H H    A ASP   A 1 162 ? 3.876  -5.206  3.781   0.78 22.42 ?  162 ASP   A H    1 
ATOM   3512 H H    B ASP   A 1 162 ? 3.853  -4.841  3.490   0.22 22.09 ?  162 ASP   A H    1 
ATOM   3513 H HA   A ASP   A 1 162 ? 2.950  -7.540  4.500   0.78 23.46 ?  162 ASP   A HA   1 
ATOM   3514 H HA   B ASP   A 1 162 ? 2.750  -7.080  4.234   0.22 22.51 ?  162 ASP   A HA   1 
ATOM   3515 H HB2  A ASP   A 1 162 ? 1.674  -5.402  3.184   0.78 24.63 ?  162 ASP   A HB2  1 
ATOM   3516 H HB2  B ASP   A 1 162 ? 1.689  -5.009  2.638   0.22 22.73 ?  162 ASP   A HB2  1 
ATOM   3517 H HB3  A ASP   A 1 162 ? 0.883  -6.728  3.560   0.78 24.63 ?  162 ASP   A HB3  1 
ATOM   3518 H HB3  B ASP   A 1 162 ? 0.808  -6.237  3.129   0.22 22.73 ?  162 ASP   A HB3  1 
ATOM   3519 N N    A LYS   A 1 163 ? 3.368  -7.215  1.350   0.78 20.37 ?  163 LYS   A N    1 
ATOM   3520 N N    B LYS   A 1 163 ? 3.390  -6.937  1.098   0.22 20.01 ?  163 LYS   A N    1 
ATOM   3521 C CA   A LYS   A 1 163 ? 3.448  -7.988  0.114   0.78 21.23 ?  163 LYS   A CA   1 
ATOM   3522 C CA   B LYS   A 1 163 ? 3.490  -7.756  -0.106  0.22 20.63 ?  163 LYS   A CA   1 
ATOM   3523 C C    A LYS   A 1 163 ? 4.549  -9.040  0.190   0.78 20.04 ?  163 LYS   A C    1 
ATOM   3524 C C    B LYS   A 1 163 ? 4.567  -8.823  0.040   0.22 19.28 ?  163 LYS   A C    1 
ATOM   3525 O O    A LYS   A 1 163 ? 4.392  -10.148 -0.335  0.78 20.45 ?  163 LYS   A O    1 
ATOM   3526 O O    B LYS   A 1 163 ? 4.387  -9.960  -0.410  0.22 19.21 ?  163 LYS   A O    1 
ATOM   3527 C CB   A LYS   A 1 163 ? 3.680  -7.052  -1.071  0.78 24.11 ?  163 LYS   A CB   1 
ATOM   3528 C CB   B LYS   A 1 163 ? 3.774  -6.865  -1.314  0.22 22.72 ?  163 LYS   A CB   1 
ATOM   3529 C CG   A LYS   A 1 163 ? 3.749  -7.758  -2.415  0.78 27.20 ?  163 LYS   A CG   1 
ATOM   3530 C CG   B LYS   A 1 163 ? 3.684  -7.561  -2.663  0.22 24.68 ?  163 LYS   A CG   1 
ATOM   3531 C CD   A LYS   A 1 163 ? 4.106  -6.791  -3.531  0.78 30.39 ?  163 LYS   A CD   1 
ATOM   3532 C CD   B LYS   A 1 163 ? 3.406  -6.543  -3.760  0.22 26.40 ?  163 LYS   A CD   1 
ATOM   3533 C CE   A LYS   A 1 163 ? 3.997  -7.456  -4.894  0.78 32.96 ?  163 LYS   A CE   1 
ATOM   3534 C CE   B LYS   A 1 163 ? 3.345  -7.179  -5.139  0.22 27.67 ?  163 LYS   A CE   1 
ATOM   3535 N NZ   A LYS   A 1 163 ? 4.567  -6.612  -5.982  0.78 34.11 ?  163 LYS   A NZ   1 
ATOM   3536 N NZ   B LYS   A 1 163 ? 4.678  -7.219  -5.800  0.22 28.36 ?  163 LYS   A NZ   1 
ATOM   3537 H H    A LYS   A 1 163 ? 3.603  -6.392  1.277   0.78 24.46 ?  163 LYS   A H    1 
ATOM   3538 H H    B LYS   A 1 163 ? 3.651  -6.124  1.000   0.22 24.02 ?  163 LYS   A H    1 
ATOM   3539 H HA   A LYS   A 1 163 ? 2.604  -8.445  -0.026  0.78 25.49 ?  163 LYS   A HA   1 
ATOM   3540 H HA   B LYS   A 1 163 ? 2.643  -8.204  -0.254  0.22 24.77 ?  163 LYS   A HA   1 
ATOM   3541 H HB2  A LYS   A 1 163 ? 2.947  -6.413  -1.112  0.78 28.95 ?  163 LYS   A HB2  1 
ATOM   3542 H HB2  B LYS   A 1 163 ? 3.133  -6.139  -1.318  0.22 27.28 ?  163 LYS   A HB2  1 
ATOM   3543 H HB3  A LYS   A 1 163 ? 4.516  -6.582  -0.941  0.78 28.95 ?  163 LYS   A HB3  1 
ATOM   3544 H HB3  B LYS   A 1 163 ? 4.671  -6.508  -1.229  0.22 27.28 ?  163 LYS   A HB3  1 
ATOM   3545 H HG2  A LYS   A 1 163 ? 4.431  -8.446  -2.385  0.78 32.65 ?  163 LYS   A HG2  1 
ATOM   3546 H HG2  B LYS   A 1 163 ? 4.527  -8.003  -2.858  0.22 29.63 ?  163 LYS   A HG2  1 
ATOM   3547 H HG3  A LYS   A 1 163 ? 2.884  -8.150  -2.616  0.78 32.65 ?  163 LYS   A HG3  1 
ATOM   3548 H HG3  B LYS   A 1 163 ? 2.959  -8.207  -2.649  0.22 29.63 ?  163 LYS   A HG3  1 
ATOM   3549 H HD2  A LYS   A 1 163 ? 3.493  -6.038  -3.512  0.78 36.48 ?  163 LYS   A HD2  1 
ATOM   3550 H HD2  B LYS   A 1 163 ? 2.554  -6.116  -3.586  0.22 31.70 ?  163 LYS   A HD2  1 
ATOM   3551 H HD3  A LYS   A 1 163 ? 5.018  -6.484  -3.411  0.78 36.48 ?  163 LYS   A HD3  1 
ATOM   3552 H HD3  B LYS   A 1 163 ? 4.116  -5.881  -3.764  0.22 31.70 ?  163 LYS   A HD3  1 
ATOM   3553 H HE2  A LYS   A 1 163 ? 4.467  -8.303  -4.877  0.78 39.57 ?  163 LYS   A HE2  1 
ATOM   3554 H HE2  B LYS   A 1 163 ? 3.021  -8.089  -5.056  0.22 33.22 ?  163 LYS   A HE2  1 
ATOM   3555 H HE3  A LYS   A 1 163 ? 3.063  -7.606  -5.095  0.78 39.57 ?  163 LYS   A HE3  1 
ATOM   3556 H HE3  B LYS   A 1 163 ? 2.746  -6.661  -5.700  0.22 33.22 ?  163 LYS   A HE3  1 
ATOM   3557 H HZ1  A LYS   A 1 163 ? 4.490  -7.031  -6.764  0.78 40.95 ?  163 LYS   A HZ1  1 
ATOM   3558 H HZ1  B LYS   A 1 163 ? 4.787  -6.494  -6.305  0.22 34.04 ?  163 LYS   A HZ1  1 
ATOM   3559 H HZ2  A LYS   A 1 163 ? 4.130  -5.838  -6.025  0.78 40.95 ?  163 LYS   A HZ2  1 
ATOM   3560 H HZ2  B LYS   A 1 163 ? 5.321  -7.242  -5.186  0.22 34.04 ?  163 LYS   A HZ2  1 
ATOM   3561 H HZ3  A LYS   A 1 163 ? 5.428  -6.451  -5.825  0.78 40.95 ?  163 LYS   A HZ3  1 
ATOM   3562 H HZ3  B LYS   A 1 163 ? 4.740  -7.941  -6.316  0.22 34.04 ?  163 LYS   A HZ3  1 
ATOM   3563 N N    A LEU   A 1 164 ? 5.672  -8.708  0.831   0.78 18.16 ?  164 LEU   A N    1 
ATOM   3564 N N    B LEU   A 1 164 ? 5.695  -8.475  0.663   0.22 17.85 ?  164 LEU   A N    1 
ATOM   3565 C CA   A LEU   A 1 164 ? 6.774  -9.661  0.956   0.78 17.08 ?  164 LEU   A CA   1 
ATOM   3566 C CA   B LEU   A 1 164 ? 6.757  -9.454  0.872   0.22 16.83 ?  164 LEU   A CA   1 
ATOM   3567 C C    A LEU   A 1 164 ? 6.365  -10.867 1.788   0.78 17.11 ?  164 LEU   A C    1 
ATOM   3568 C C    B LEU   A 1 164 ? 6.300  -10.574 1.795   0.22 16.06 ?  164 LEU   A C    1 
ATOM   3569 O O    A LEU   A 1 164 ? 6.666  -12.013 1.434   0.78 17.72 ?  164 LEU   A O    1 
ATOM   3570 O O    B LEU   A 1 164 ? 6.637  -11.744 1.578   0.22 15.83 ?  164 LEU   A O    1 
ATOM   3571 C CB   A LEU   A 1 164 ? 7.974  -8.973  1.601   0.78 16.35 ?  164 LEU   A CB   1 
ATOM   3572 C CB   B LEU   A 1 164 ? 7.989  -8.762  1.450   0.22 16.67 ?  164 LEU   A CB   1 
ATOM   3573 C CG   A LEU   A 1 164 ? 8.732  -7.994  0.706   0.78 16.52 ?  164 LEU   A CG   1 
ATOM   3574 C CG   B LEU   A 1 164 ? 8.735  -7.831  0.498   0.22 16.68 ?  164 LEU   A CG   1 
ATOM   3575 C CD1  A LEU   A 1 164 ? 9.662  -7.122  1.532   0.78 16.50 ?  164 LEU   A CD1  1 
ATOM   3576 C CD1  B LEU   A 1 164 ? 9.542  -6.824  1.293   0.22 16.44 ?  164 LEU   A CD1  1 
ATOM   3577 C CD2  A LEU   A 1 164 ? 9.508  -8.739  -0.369  0.78 16.82 ?  164 LEU   A CD2  1 
ATOM   3578 C CD2  B LEU   A 1 164 ? 9.636  -8.632  -0.429  0.22 16.82 ?  164 LEU   A CD2  1 
ATOM   3579 H H    A LEU   A 1 164 ? 5.817  -7.947  1.203   0.78 21.81 ?  164 LEU   A H    1 
ATOM   3580 H H    B LEU   A 1 164 ? 5.867  -7.690  0.967   0.22 21.43 ?  164 LEU   A H    1 
ATOM   3581 H HA   A LEU   A 1 164 ? 7.033  -9.968  0.075   0.78 20.51 ?  164 LEU   A HA   1 
ATOM   3582 H HA   B LEU   A 1 164 ? 7.002  -9.846  0.021   0.22 20.21 ?  164 LEU   A HA   1 
ATOM   3583 H HB2  A LEU   A 1 164 ? 7.667  -8.477  2.375   0.78 19.64 ?  164 LEU   A HB2  1 
ATOM   3584 H HB2  B LEU   A 1 164 ? 7.714  -8.233  2.214   0.22 20.02 ?  164 LEU   A HB2  1 
ATOM   3585 H HB3  A LEU   A 1 164 ? 8.604  -9.655  1.883   0.78 19.64 ?  164 LEU   A HB3  1 
ATOM   3586 H HB3  B LEU   A 1 164 ? 8.616  -9.444  1.737   0.22 20.02 ?  164 LEU   A HB3  1 
ATOM   3587 H HG   A LEU   A 1 164 ? 8.099  -7.412  0.264   0.78 19.83 ?  164 LEU   A HG   1 
ATOM   3588 H HG   B LEU   A 1 164 ? 8.094  -7.348  -0.046  0.22 20.03 ?  164 LEU   A HG   1 
ATOM   3589 H HD11 A LEU   A 1 164 ? 10.137 -6.514  0.942   0.78 19.82 ?  164 LEU   A HD11 1 
ATOM   3590 H HD11 B LEU   A 1 164 ? 10.035 -6.260  0.678   0.22 19.74 ?  164 LEU   A HD11 1 
ATOM   3591 H HD12 A LEU   A 1 164 ? 9.138  -6.618  2.173   0.78 19.82 ?  164 LEU   A HD12 1 
ATOM   3592 H HD12 B LEU   A 1 164 ? 8.935  -6.285  1.824   0.22 19.74 ?  164 LEU   A HD12 1 
ATOM   3593 H HD13 A LEU   A 1 164 ? 10.299 -7.688  1.999   0.78 19.82 ?  164 LEU   A HD13 1 
ATOM   3594 H HD13 B LEU   A 1 164 ? 10.156 -7.301  1.873   0.22 19.74 ?  164 LEU   A HD13 1 
ATOM   3595 H HD21 A LEU   A 1 164 ? 10.049 -8.104  -0.868  0.78 20.20 ?  164 LEU   A HD21 1 
ATOM   3596 H HD21 B LEU   A 1 164 ? 9.734  -8.152  -1.265  0.22 20.20 ?  164 LEU   A HD21 1 
ATOM   3597 H HD22 A LEU   A 1 164 ? 10.081 -9.399  0.051   0.78 20.20 ?  164 LEU   A HD22 1 
ATOM   3598 H HD22 B LEU   A 1 164 ? 10.503 -8.746  -0.008  0.22 20.20 ?  164 LEU   A HD22 1 
ATOM   3599 H HD23 A LEU   A 1 164 ? 8.882  -9.177  -0.966  0.78 20.20 ?  164 LEU   A HD23 1 
ATOM   3600 H HD23 B LEU   A 1 164 ? 9.231  -9.497  -0.593  0.22 20.20 ?  164 LEU   A HD23 1 
ATOM   3601 N N    A VAL   A 1 165 ? 5.692  -10.624 2.910   0.78 16.70 ?  165 VAL   A N    1 
ATOM   3602 N N    B VAL   A 1 165 ? 5.535  -10.237 2.834   0.22 15.39 ?  165 VAL   A N    1 
ATOM   3603 C CA   A VAL   A 1 165 ? 5.215  -11.714 3.751   0.78 16.65 ?  165 VAL   A CA   1 
ATOM   3604 C CA   B VAL   A 1 165 ? 5.067  -11.258 3.765   0.22 15.12 ?  165 VAL   A CA   1 
ATOM   3605 C C    A VAL   A 1 165 ? 4.163  -12.526 3.013   0.78 16.58 ?  165 VAL   A C    1 
ATOM   3606 C C    B VAL   A 1 165 ? 4.079  -12.195 3.082   0.22 14.74 ?  165 VAL   A C    1 
ATOM   3607 O O    A VAL   A 1 165 ? 4.242  -13.758 2.937   0.78 16.41 ?  165 VAL   A O    1 
ATOM   3608 O O    B VAL   A 1 165 ? 4.206  -13.422 3.159   0.22 14.63 ?  165 VAL   A O    1 
ATOM   3609 C CB   A VAL   A 1 165 ? 4.668  -11.141 5.070   0.78 16.87 ?  165 VAL   A CB   1 
ATOM   3610 C CB   B VAL   A 1 165 ? 4.469  -10.606 5.024   0.22 15.32 ?  165 VAL   A CB   1 
ATOM   3611 C CG1  A VAL   A 1 165 ? 3.907  -12.204 5.850   0.78 17.22 ?  165 VAL   A CG1  1 
ATOM   3612 C CG1  B VAL   A 1 165 ? 3.689  -11.635 5.834   0.22 15.48 ?  165 VAL   A CG1  1 
ATOM   3613 C CG2  A VAL   A 1 165 ? 5.797  -10.535 5.897   0.78 17.60 ?  165 VAL   A CG2  1 
ATOM   3614 C CG2  B VAL   A 1 165 ? 5.573  -9.980  5.863   0.22 15.29 ?  165 VAL   A CG2  1 
ATOM   3615 H H    A VAL   A 1 165 ? 5.511  -9.846  3.204   0.78 20.05 ?  165 VAL   A H    1 
ATOM   3616 H H    B VAL   A 1 165 ? 5.283  -9.434  3.021   0.22 18.48 ?  165 VAL   A H    1 
ATOM   3617 H HA   A VAL   A 1 165 ? 5.955  -12.308 3.965   0.78 19.99 ?  165 VAL   A HA   1 
ATOM   3618 H HA   B VAL   A 1 165 ? 5.827  -11.786 4.050   0.22 18.16 ?  165 VAL   A HA   1 
ATOM   3619 H HB   A VAL   A 1 165 ? 4.044  -10.431 4.860   0.78 20.25 ?  165 VAL   A HB   1 
ATOM   3620 H HB   B VAL   A 1 165 ? 3.856  -9.900  4.762   0.22 18.40 ?  165 VAL   A HB   1 
ATOM   3621 H HG11 A VAL   A 1 165 ? 3.813  -11.909 6.769   0.78 20.67 ?  165 VAL   A HG11 1 
ATOM   3622 H HG11 B VAL   A 1 165 ? 3.557  -11.294 6.732   0.22 18.59 ?  165 VAL   A HG11 1 
ATOM   3623 H HG12 A VAL   A 1 165 ? 3.027  -12.319 5.452   0.78 20.67 ?  165 VAL   A HG12 1 
ATOM   3624 H HG12 B VAL   A 1 165 ? 2.829  -11.788 5.412   0.22 18.59 ?  165 VAL   A HG12 1 
ATOM   3625 H HG13 A VAL   A 1 165 ? 4.399  -13.036 5.816   0.78 20.67 ?  165 VAL   A HG13 1 
ATOM   3626 H HG13 B VAL   A 1 165 ? 4.197  -12.461 5.867   0.22 18.59 ?  165 VAL   A HG13 1 
ATOM   3627 H HG21 A VAL   A 1 165 ? 5.431  -10.189 6.726   0.78 21.13 ?  165 VAL   A HG21 1 
ATOM   3628 H HG21 B VAL   A 1 165 ? 5.173  -9.452  6.570   0.22 18.36 ?  165 VAL   A HG21 1 
ATOM   3629 H HG22 A VAL   A 1 165 ? 6.454  -11.223 6.087   0.78 21.13 ?  165 VAL   A HG22 1 
ATOM   3630 H HG22 B VAL   A 1 165 ? 6.120  -10.686 6.243   0.22 18.36 ?  165 VAL   A HG22 1 
ATOM   3631 H HG23 A VAL   A 1 165 ? 6.207  -9.816  5.390   0.78 21.13 ?  165 VAL   A HG23 1 
ATOM   3632 H HG23 B VAL   A 1 165 ? 6.116  -9.411  5.294   0.22 18.36 ?  165 VAL   A HG23 1 
ATOM   3633 N N    A SER   A 1 166 ? 3.159  -11.845 2.458   0.78 17.33 ?  166 SER   A N    1 
ATOM   3634 N N    B SER   A 1 166 ? 3.082  -11.633 2.396   0.22 14.74 ?  166 SER   A N    1 
ATOM   3635 C CA   A SER   A 1 166 ? 2.015  -12.541 1.877   0.78 18.82 ?  166 SER   A CA   1 
ATOM   3636 C CA   B SER   A 1 166 ? 1.994  -12.461 1.888   0.22 15.24 ?  166 SER   A CA   1 
ATOM   3637 C C    A SER   A 1 166 ? 2.404  -13.367 0.663   0.78 19.39 ?  166 SER   A C    1 
ATOM   3638 C C    B SER   A 1 166 ? 2.426  -13.324 0.709   0.22 16.72 ?  166 SER   A C    1 
ATOM   3639 O O    A SER   A 1 166 ? 1.714  -14.341 0.336   0.78 21.11 ?  166 SER   A O    1 
ATOM   3640 O O    B SER   A 1 166 ? 1.826  -14.378 0.469   0.22 17.70 ?  166 SER   A O    1 
ATOM   3641 C CB   A SER   A 1 166 ? 0.925  -11.537 1.492   0.78 20.67 ?  166 SER   A CB   1 
ATOM   3642 C CB   B SER   A 1 166 ? 0.806  -11.589 1.490   0.22 14.57 ?  166 SER   A CB   1 
ATOM   3643 O OG   A SER   A 1 166 ? 0.306  -10.974 2.638   0.78 22.71 ?  166 SER   A OG   1 
ATOM   3644 O OG   B SER   A 1 166 ? 1.123  -10.780 0.374   0.22 13.82 ?  166 SER   A OG   1 
ATOM   3645 H H    A SER   A 1 166 ? 3.108  -10.995 2.420   0.78 20.81 ?  166 SER   A H    1 
ATOM   3646 H H    B SER   A 1 166 ? 3.010  -10.793 2.221   0.22 17.70 ?  166 SER   A H    1 
ATOM   3647 H HA   A SER   A 1 166 ? 1.634  -13.150 2.532   0.78 22.59 ?  166 SER   A HA   1 
ATOM   3648 H HA   B SER   A 1 166 ? 1.701  -13.053 2.595   0.22 18.31 ?  166 SER   A HA   1 
ATOM   3649 H HB2  A SER   A 1 166 ? 1.321  -10.825 0.968   0.78 24.81 ?  166 SER   A HB2  1 
ATOM   3650 H HB2  B SER   A 1 166 ? 0.057  -12.165 1.259   0.22 17.50 ?  166 SER   A HB2  1 
ATOM   3651 H HB3  A SER   A 1 166 ? 0.243  -11.989 0.968   0.78 24.81 ?  166 SER   A HB3  1 
ATOM   3652 H HB3  B SER   A 1 166 ? 0.566  -11.021 2.238   0.22 17.50 ?  166 SER   A HB3  1 
ATOM   3653 H HG   A SER   A 1 166 ? 0.881  -10.567 3.101   0.78 27.27 ?  166 SER   A HG   1 
ATOM   3654 H HG   B SER   A 1 166 ? 0.460  -10.305 0.166   0.22 16.60 ?  166 SER   A HG   1 
ATOM   3655 N N    A SER   A 1 167 ? 3.483  -12.998 -0.024  0.78 18.70 ?  167 SER   A N    1 
ATOM   3656 N N    B SER   A 1 167 ? 3.451  -12.908 -0.032  0.22 17.30 ?  167 SER   A N    1 
ATOM   3657 C CA   A SER   A 1 167 ? 3.923  -13.720 -1.208  0.78 19.44 ?  167 SER   A CA   1 
ATOM   3658 C CA   B SER   A 1 167 ? 3.866  -13.608 -1.241  0.22 18.26 ?  167 SER   A CA   1 
ATOM   3659 C C    A SER   A 1 167 ? 5.068  -14.681 -0.922  0.78 19.23 ?  167 SER   A C    1 
ATOM   3660 C C    B SER   A 1 167 ? 5.062  -14.527 -1.025  0.22 18.97 ?  167 SER   A C    1 
ATOM   3661 O O    A SER   A 1 167 ? 5.560  -15.329 -1.851  0.78 20.28 ?  167 SER   A O    1 
ATOM   3662 O O    B SER   A 1 167 ? 5.539  -15.132 -1.990  0.22 19.11 ?  167 SER   A O    1 
ATOM   3663 C CB   A SER   A 1 167 ? 4.325  -12.737 -2.317  0.78 20.43 ?  167 SER   A CB   1 
ATOM   3664 C CB   B SER   A 1 167 ? 4.188  -12.606 -2.355  0.22 18.57 ?  167 SER   A CB   1 
ATOM   3665 O OG   A SER   A 1 167 ? 5.414  -11.922 -1.910  0.78 20.78 ?  167 SER   A OG   1 
ATOM   3666 O OG   B SER   A 1 167 ? 5.333  -11.834 -2.036  0.22 18.73 ?  167 SER   A OG   1 
ATOM   3667 H H    A SER   A 1 167 ? 3.976  -12.321 0.180   0.78 22.45 ?  167 SER   A H    1 
ATOM   3668 H H    B SER   A 1 167 ? 3.926  -12.214 0.148   0.22 20.77 ?  167 SER   A H    1 
ATOM   3669 H HA   A SER   A 1 167 ? 3.181  -14.242 -1.543  0.78 23.34 ?  167 SER   A HA   1 
ATOM   3670 H HA   B SER   A 1 167 ? 3.127  -14.154 -1.548  0.22 21.92 ?  167 SER   A HA   1 
ATOM   3671 H HB2  A SER   A 1 167 ? 4.587  -13.242 -3.104  0.78 24.53 ?  167 SER   A HB2  1 
ATOM   3672 H HB2  B SER   A 1 167 ? 4.357  -13.095 -3.177  0.22 22.30 ?  167 SER   A HB2  1 
ATOM   3673 H HB3  A SER   A 1 167 ? 3.557  -12.175 -2.535  0.78 24.53 ?  167 SER   A HB3  1 
ATOM   3674 H HB3  B SER   A 1 167 ? 3.430  -12.013 -2.474  0.22 22.30 ?  167 SER   A HB3  1 
ATOM   3675 H HG   A SER   A 1 167 ? 5.183  -11.461 -1.242  0.78 24.95 ?  167 SER   A HG   1 
ATOM   3676 H HG   B SER   A 1 167 ? 5.200  -11.406 -1.326  0.22 22.49 ?  167 SER   A HG   1 
ATOM   3677 N N    A PHE   A 1 168 ? 5.496  -14.802 0.331   0.78 18.41 ?  168 PHE   A N    1 
ATOM   3678 N N    B PHE   A 1 168 ? 5.556  -14.652 0.204   0.22 19.63 ?  168 PHE   A N    1 
ATOM   3679 C CA   A PHE   A 1 168 ? 6.683  -15.594 0.626   0.78 18.84 ?  168 PHE   A CA   1 
ATOM   3680 C CA   B PHE   A 1 168 ? 6.730  -15.479 0.450   0.22 20.63 ?  168 PHE   A CA   1 
ATOM   3681 C C    A PHE   A 1 168 ? 6.382  -17.080 0.526   0.78 20.61 ?  168 PHE   A C    1 
ATOM   3682 C C    B PHE   A 1 168 ? 6.391  -16.951 0.253   0.22 22.77 ?  168 PHE   A C    1 
ATOM   3683 O O    A PHE   A 1 168 ? 5.444  -17.581 1.154   0.78 21.51 ?  168 PHE   A O    1 
ATOM   3684 O O    B PHE   A 1 168 ? 5.366  -17.436 0.740   0.22 22.97 ?  168 PHE   A O    1 
ATOM   3685 C CB   A PHE   A 1 168 ? 7.215  -15.291 2.022   0.78 18.14 ?  168 PHE   A CB   1 
ATOM   3686 C CB   B PHE   A 1 168 ? 7.254  -15.250 1.866   0.22 19.59 ?  168 PHE   A CB   1 
ATOM   3687 C CG   A PHE   A 1 168 ? 8.479  -16.037 2.339   0.78 17.16 ?  168 PHE   A CG   1 
ATOM   3688 C CG   B PHE   A 1 168 ? 8.510  -16.016 2.172   0.22 18.63 ?  168 PHE   A CG   1 
ATOM   3689 C CD1  A PHE   A 1 168 ? 9.664  -15.690 1.717   0.78 17.59 ?  168 PHE   A CD1  1 
ATOM   3690 C CD1  B PHE   A 1 168 ? 9.731  -15.589 1.677   0.22 18.55 ?  168 PHE   A CD1  1 
ATOM   3691 C CD2  A PHE   A 1 168 ? 8.486  -17.105 3.222   0.78 16.43 ?  168 PHE   A CD2  1 
ATOM   3692 C CD2  B PHE   A 1 168 ? 8.472  -17.162 2.950   0.22 18.14 ?  168 PHE   A CD2  1 
ATOM   3693 C CE1  A PHE   A 1 168 ? 10.832 -16.375 1.983   0.78 17.24 ?  168 PHE   A CE1  1 
ATOM   3694 C CE1  B PHE   A 1 168 ? 10.889 -16.289 1.951   0.22 18.36 ?  168 PHE   A CE1  1 
ATOM   3695 C CE2  A PHE   A 1 168 ? 9.660  -17.790 3.495   0.78 16.85 ?  168 PHE   A CE2  1 
ATOM   3696 C CE2  B PHE   A 1 168 ? 9.630  -17.866 3.228   0.22 17.98 ?  168 PHE   A CE2  1 
ATOM   3697 C CZ   A PHE   A 1 168 ? 10.830 -17.423 2.870   0.78 16.88 ?  168 PHE   A CZ   1 
ATOM   3698 C CZ   B PHE   A 1 168 ? 10.840 -17.428 2.727   0.22 18.07 ?  168 PHE   A CZ   1 
ATOM   3699 H H    A PHE   A 1 168 ? 5.130  -14.433 1.017   0.78 22.11 ?  168 PHE   A H    1 
ATOM   3700 H H    B PHE   A 1 168 ? 5.236  -14.270 0.904   0.22 23.57 ?  168 PHE   A H    1 
ATOM   3701 H HA   A PHE   A 1 168 ? 7.379  -15.380 -0.017  0.78 22.62 ?  168 PHE   A HA   1 
ATOM   3702 H HA   B PHE   A 1 168 ? 7.428  -15.240 -0.177  0.22 24.77 ?  168 PHE   A HA   1 
ATOM   3703 H HB2  A PHE   A 1 168 ? 7.406  -14.342 2.090   0.78 21.78 ?  168 PHE   A HB2  1 
ATOM   3704 H HB2  B PHE   A 1 168 ? 7.446  -14.306 1.979   0.22 23.52 ?  168 PHE   A HB2  1 
ATOM   3705 H HB3  A PHE   A 1 168 ? 6.547  -15.544 2.677   0.78 21.78 ?  168 PHE   A HB3  1 
ATOM   3706 H HB3  B PHE   A 1 168 ? 6.575  -15.527 2.501   0.22 23.52 ?  168 PHE   A HB3  1 
ATOM   3707 H HD1  A PHE   A 1 168 ? 9.679  -14.981 1.117   0.78 21.13 ?  168 PHE   A HD1  1 
ATOM   3708 H HD1  B PHE   A 1 168 ? 9.771  -14.822 1.153   0.22 22.28 ?  168 PHE   A HD1  1 
ATOM   3709 H HD2  A PHE   A 1 168 ? 7.696  -17.357 3.647   0.78 19.73 ?  168 PHE   A HD2  1 
ATOM   3710 H HD2  B PHE   A 1 168 ? 7.660  -17.461 3.289   0.22 21.78 ?  168 PHE   A HD2  1 
ATOM   3711 H HE1  A PHE   A 1 168 ? 11.628 -16.127 1.566   0.78 20.70 ?  168 PHE   A HE1  1 
ATOM   3712 H HE1  B PHE   A 1 168 ? 11.704 -15.993 1.613   0.22 22.05 ?  168 PHE   A HE1  1 
ATOM   3713 H HE2  A PHE   A 1 168 ? 9.650  -18.504 4.096   0.78 20.23 ?  168 PHE   A HE2  1 
ATOM   3714 H HE2  B PHE   A 1 168 ? 9.593  -18.635 3.752   0.22 21.59 ?  168 PHE   A HE2  1 
ATOM   3715 H HZ   A PHE   A 1 168 ? 11.618 -17.886 3.054   0.78 20.27 ?  168 PHE   A HZ   1 
ATOM   3716 H HZ   B PHE   A 1 168 ? 11.620 -17.901 2.913   0.22 21.70 ?  168 PHE   A HZ   1 
ATOM   3717 N N    A LEU   A 1 169 ? 7.207  -17.794 -0.233  0.78 23.77 ?  169 LEU   A N    1 
ATOM   3718 N N    B LEU   A 1 169 ? 7.258  -17.661 -0.463  0.22 24.85 ?  169 LEU   A N    1 
ATOM   3719 C CA   A LEU   A 1 169 ? 7.032  -19.227 -0.382  0.78 28.97 ?  169 LEU   A CA   1 
ATOM   3720 C CA   B LEU   A 1 169 ? 7.065  -19.085 -0.711  0.22 27.16 ?  169 LEU   A CA   1 
ATOM   3721 C C    A LEU   A 1 169 ? 7.927  -19.963 0.605   0.78 30.75 ?  169 LEU   A C    1 
ATOM   3722 C C    B LEU   A 1 169 ? 7.962  -19.911 0.202   0.22 27.92 ?  169 LEU   A C    1 
ATOM   3723 O O    A LEU   A 1 169 ? 7.465  -20.393 1.663   0.78 31.46 ?  169 LEU   A O    1 
ATOM   3724 O O    B LEU   A 1 169 ? 7.506  -20.460 1.206   0.22 28.23 ?  169 LEU   A O    1 
ATOM   3725 C CB   A LEU   A 1 169 ? 7.334  -19.658 -1.820  0.78 31.50 ?  169 LEU   A CB   1 
ATOM   3726 C CB   B LEU   A 1 169 ? 7.353  -19.418 -2.177  0.22 28.42 ?  169 LEU   A CB   1 
ATOM   3727 C CG   A LEU   A 1 169 ? 7.008  -21.113 -2.163  0.78 33.61 ?  169 LEU   A CG   1 
ATOM   3728 C CG   B LEU   A 1 169 ? 7.301  -20.895 -2.579  0.22 29.51 ?  169 LEU   A CG   1 
ATOM   3729 C CD1  A LEU   A 1 169 ? 5.582  -21.456 -1.760  0.78 34.26 ?  169 LEU   A CD1  1 
ATOM   3730 C CD1  B LEU   A 1 169 ? 5.995  -21.540 -2.138  0.22 29.85 ?  169 LEU   A CD1  1 
ATOM   3731 C CD2  A LEU   A 1 169 ? 7.219  -21.371 -3.648  0.78 34.16 ?  169 LEU   A CD2  1 
ATOM   3732 C CD2  B LEU   A 1 169 ? 7.486  -21.042 -4.083  0.22 29.86 ?  169 LEU   A CD2  1 
ATOM   3733 O OXT  A LEU   A 1 169 ? 9.126  -20.132 0.380   0.78 30.66 -1 169 LEU   A OXT  1 
ATOM   3734 O OXT  B LEU   A 1 169 ? 9.162  -20.043 -0.037  0.22 28.12 -1 169 LEU   A OXT  1 
ATOM   3735 H H    A LEU   A 1 169 ? 7.872  -17.468 -0.668  0.78 28.54 ?  169 LEU   A H    1 
ATOM   3736 H H    B LEU   A 1 169 ? 7.972  -17.337 -0.819  0.22 29.83 ?  169 LEU   A H    1 
ATOM   3737 H HA   A LEU   A 1 169 ? 6.114  -19.454 -0.178  0.78 34.78 ?  169 LEU   A HA   1 
ATOM   3738 H HA   B LEU   A 1 169 ? 6.144  -19.317 -0.524  0.22 32.60 ?  169 LEU   A HA   1 
ATOM   3739 H HB2  A LEU   A 1 169 ? 6.818  -19.097 -2.421  0.78 37.81 ?  169 LEU   A HB2  1 
ATOM   3740 H HB2  B LEU   A 1 169 ? 6.702  -18.952 -2.723  0.22 34.12 ?  169 LEU   A HB2  1 
ATOM   3741 H HB3  A LEU   A 1 169 ? 8.279  -19.526 -1.987  0.78 37.81 ?  169 LEU   A HB3  1 
ATOM   3742 H HB3  B LEU   A 1 169 ? 8.241  -19.096 -2.391  0.22 34.12 ?  169 LEU   A HB3  1 
ATOM   3743 H HG   A LEU   A 1 169 ? 7.607  -21.696 -1.671  0.78 40.35 ?  169 LEU   A HG   1 
ATOM   3744 H HG   B LEU   A 1 169 ? 8.028  -21.367 -2.145  0.22 35.43 ?  169 LEU   A HG   1 
ATOM   3745 H HD11 A LEU   A 1 169 ? 5.326  -22.289 -2.184  0.78 41.13 ?  169 LEU   A HD11 1 
ATOM   3746 H HD11 B LEU   A 1 169 ? 5.949  -22.439 -2.500  0.22 35.83 ?  169 LEU   A HD11 1 
ATOM   3747 H HD12 A LEU   A 1 169 ? 5.540  -21.550 -0.795  0.78 41.13 ?  169 LEU   A HD12 1 
ATOM   3748 H HD12 B LEU   A 1 169 ? 5.970  -21.573 -1.169  0.22 35.83 ?  169 LEU   A HD12 1 
ATOM   3749 H HD13 A LEU   A 1 169 ? 4.992  -20.742 -2.050  0.78 41.13 ?  169 LEU   A HD13 1 
ATOM   3750 H HD13 B LEU   A 1 169 ? 5.254  -21.011 -2.471  0.22 35.83 ?  169 LEU   A HD13 1 
ATOM   3751 H HD21 A LEU   A 1 169 ? 7.014  -22.300 -3.839  0.78 41.00 ?  169 LEU   A HD21 1 
ATOM   3752 H HD21 B LEU   A 1 169 ? 7.451  -21.983 -4.316  0.22 35.85 ?  169 LEU   A HD21 1 
ATOM   3753 H HD22 A LEU   A 1 169 ? 6.629  -20.791 -4.155  0.78 41.00 ?  169 LEU   A HD22 1 
ATOM   3754 H HD22 B LEU   A 1 169 ? 6.775  -20.563 -4.537  0.22 35.85 ?  169 LEU   A HD22 1 
ATOM   3755 H HD23 A LEU   A 1 169 ? 8.143  -21.182 -3.873  0.78 41.00 ?  169 LEU   A HD23 1 
ATOM   3756 H HD23 B LEU   A 1 169 ? 8.347  -20.671 -4.333  0.22 35.85 ?  169 LEU   A HD23 1 
ATOM   3757 N N    A SER   B 1 1   ? 50.765 -9.204  -23.755 0.78 27.87 ?  1   SER   B N    1 
ATOM   3758 N N    B SER   B 1 1   ? 50.774 -9.238  -23.811 0.22 28.55 ?  1   SER   B N    1 
ATOM   3759 C CA   A SER   B 1 1   ? 51.230 -10.269 -22.848 0.78 27.48 ?  1   SER   B CA   1 
ATOM   3760 C CA   B SER   B 1 1   ? 51.234 -10.231 -22.816 0.22 28.55 ?  1   SER   B CA   1 
ATOM   3761 C C    A SER   B 1 1   ? 50.136 -11.298 -22.606 0.78 26.00 ?  1   SER   B C    1 
ATOM   3762 C C    B SER   B 1 1   ? 50.156 -11.278 -22.580 0.22 28.18 ?  1   SER   B C    1 
ATOM   3763 O O    A SER   B 1 1   ? 48.948 -11.091 -22.913 0.78 25.49 ?  1   SER   B O    1 
ATOM   3764 O O    B SER   B 1 1   ? 49.008 -11.116 -22.997 0.22 27.96 ?  1   SER   B O    1 
ATOM   3765 C CB   A SER   B 1 1   ? 51.688 -9.689  -21.512 0.78 28.36 ?  1   SER   B CB   1 
ATOM   3766 C CB   B SER   B 1 1   ? 51.591 -9.548  -21.500 0.22 28.73 ?  1   SER   B CB   1 
ATOM   3767 O OG   A SER   B 1 1   ? 50.577 -9.402  -20.686 0.78 30.63 ?  1   SER   B OG   1 
ATOM   3768 O OG   B SER   B 1 1   ? 50.450 -9.428  -20.672 0.22 29.35 ?  1   SER   B OG   1 
ATOM   3769 H H1   A SER   B 1 1   ? 50.508 -9.569  -24.521 0.78 33.45 ?  1   SER   B H1   1 
ATOM   3770 H H1   B SER   B 1 1   ? 51.457 -8.713  -24.028 0.22 34.27 ?  1   SER   B H1   1 
ATOM   3771 H H2   A SER   B 1 1   ? 50.087 -8.779  -23.376 0.78 33.45 ?  1   SER   B H2   1 
ATOM   3772 H H2   B SER   B 1 1   ? 50.482 -9.666  -24.532 0.22 34.27 ?  1   SER   B H2   1 
ATOM   3773 H H3   A SER   B 1 1   ? 51.435 -8.638  -23.900 0.78 33.45 ?  1   SER   B H3   1 
ATOM   3774 H H3   B SER   B 1 1   ? 50.120 -8.756  -23.458 0.22 34.27 ?  1   SER   B H3   1 
ATOM   3775 H HA   A SER   B 1 1   ? 51.986 -10.711 -23.262 0.78 32.99 ?  1   SER   B HA   1 
ATOM   3776 H HA   B SER   B 1 1   ? 52.021 -10.668 -23.163 0.22 34.28 ?  1   SER   B HA   1 
ATOM   3777 H HB2  A SER   B 1 1   ? 52.253 -10.341 -21.069 0.78 34.05 ?  1   SER   B HB2  1 
ATOM   3778 H HB2  B SER   B 1 1   ? 52.268 -10.079 -21.053 0.22 34.49 ?  1   SER   B HB2  1 
ATOM   3779 H HB3  A SER   B 1 1   ? 52.184 -8.872  -21.672 0.78 34.05 ?  1   SER   B HB3  1 
ATOM   3780 H HB3  B SER   B 1 1   ? 51.935 -8.660  -21.685 0.22 34.49 ?  1   SER   B HB3  1 
ATOM   3781 H HG   A SER   B 1 1   ? 50.801 -8.844  -20.097 0.78 36.77 ?  1   SER   B HG   1 
ATOM   3782 H HG   B SER   B 1 1   ? 50.577 -8.829  -20.099 0.22 35.24 ?  1   SER   B HG   1 
ATOM   3783 N N    A MET   B 1 2   ? 50.563 -12.412 -22.034 0.78 25.75 ?  2   MET   B N    1 
ATOM   3784 N N    B MET   B 1 2   ? 50.538 -12.350 -21.894 0.22 27.99 ?  2   MET   B N    1 
ATOM   3785 C CA   A MET   B 1 2   ? 49.736 -13.598 -21.870 0.78 25.81 ?  2   MET   B CA   1 
ATOM   3786 C CA   B MET   B 1 2   ? 49.701 -13.534 -21.733 0.22 27.69 ?  2   MET   B CA   1 
ATOM   3787 C C    A MET   B 1 2   ? 49.498 -13.796 -20.381 0.78 23.24 ?  2   MET   B C    1 
ATOM   3788 C C    B MET   B 1 2   ? 49.431 -13.742 -20.249 0.22 25.42 ?  2   MET   B C    1 
ATOM   3789 O O    A MET   B 1 2   ? 50.435 -14.091 -19.634 0.78 23.69 ?  2   MET   B O    1 
ATOM   3790 O O    B MET   B 1 2   ? 50.327 -14.152 -19.502 0.22 25.71 ?  2   MET   B O    1 
ATOM   3791 C CB   A MET   B 1 2   ? 50.463 -14.793 -22.475 0.78 30.08 ?  2   MET   B CB   1 
ATOM   3792 C CB   B MET   B 1 2   ? 50.419 -14.739 -22.327 0.22 29.81 ?  2   MET   B CB   1 
ATOM   3793 C CG   A MET   B 1 2   ? 49.605 -16.024 -22.701 0.78 33.97 ?  2   MET   B CG   1 
ATOM   3794 C CG   B MET   B 1 2   ? 49.516 -15.884 -22.748 0.22 31.75 ?  2   MET   B CG   1 
ATOM   3795 S SD   A MET   B 1 2   ? 50.462 -17.234 -23.725 0.78 37.56 ?  2   MET   B SD   1 
ATOM   3796 S SD   B MET   B 1 2   ? 50.402 -17.079 -23.760 0.22 33.41 ?  2   MET   B SD   1 
ATOM   3797 C CE   A MET   B 1 2   ? 51.062 -16.167 -25.027 0.78 37.92 ?  2   MET   B CE   1 
ATOM   3798 C CE   B MET   B 1 2   ? 51.327 -15.975 -24.822 0.22 33.79 ?  2   MET   B CE   1 
ATOM   3799 H H    A MET   B 1 2   ? 51.360 -12.518 -21.720 0.78 30.91 ?  2   MET   B H    1 
ATOM   3800 H H    B MET   B 1 2   ? 51.305 -12.420 -21.512 0.22 33.61 ?  2   MET   B H    1 
ATOM   3801 H HA   A MET   B 1 2   ? 48.893 -13.488 -22.330 0.78 30.99 ?  2   MET   B HA   1 
ATOM   3802 H HA   B MET   B 1 2   ? 48.867 -13.414 -22.213 0.22 33.24 ?  2   MET   B HA   1 
ATOM   3803 H HB2  A MET   B 1 2   ? 50.819 -14.496 -23.322 0.78 36.11 ?  2   MET   B HB2  1 
ATOM   3804 H HB2  B MET   B 1 2   ? 50.903 -14.410 -23.095 0.22 35.79 ?  2   MET   B HB2  1 
ATOM   3805 H HB3  A MET   B 1 2   ? 51.188 -15.061 -21.894 0.78 36.11 ?  2   MET   B HB3  1 
ATOM   3806 H HB3  B MET   B 1 2   ? 51.043 -15.099 -21.682 0.22 35.79 ?  2   MET   B HB3  1 
ATOM   3807 H HG2  A MET   B 1 2   ? 49.402 -16.433 -21.842 0.78 40.77 ?  2   MET   B HG2  1 
ATOM   3808 H HG2  B MET   B 1 2   ? 49.188 -16.338 -21.956 0.22 38.11 ?  2   MET   B HG2  1 
ATOM   3809 H HG3  A MET   B 1 2   ? 48.788 -15.776 -23.158 0.78 40.77 ?  2   MET   B HG3  1 
ATOM   3810 H HG3  B MET   B 1 2   ? 48.774 -15.545 -23.267 0.22 38.11 ?  2   MET   B HG3  1 
ATOM   3811 H HE1  A MET   B 1 2   ? 51.232 -16.701 -25.806 0.78 45.51 ?  2   MET   B HE1  1 
ATOM   3812 H HE1  B MET   B 1 2   ? 51.601 -16.458 -25.603 0.22 40.57 ?  2   MET   B HE1  1 
ATOM   3813 H HE2  A MET   B 1 2   ? 50.379 -15.501 -25.217 0.78 45.51 ?  2   MET   B HE2  1 
ATOM   3814 H HE2  B MET   B 1 2   ? 50.758 -15.225 -25.074 0.22 40.57 ?  2   MET   B HE2  1 
ATOM   3815 H HE3  A MET   B 1 2   ? 51.879 -15.724 -24.737 0.78 45.51 ?  2   MET   B HE3  1 
ATOM   3816 H HE3  B MET   B 1 2   ? 52.107 -15.649 -24.337 0.22 40.57 ?  2   MET   B HE3  1 
ATOM   3817 N N    A VAL   B 1 3   ? 48.251 -13.607 -19.952 0.78 21.08 ?  3   VAL   B N    1 
ATOM   3818 N N    B VAL   B 1 3   ? 48.204 -13.455 -19.824 0.22 22.87 ?  3   VAL   B N    1 
ATOM   3819 C CA   A VAL   B 1 3   ? 47.837 -13.857 -18.578 0.78 19.86 ?  3   VAL   B CA   1 
ATOM   3820 C CA   B VAL   B 1 3   ? 47.764 -13.725 -18.462 0.22 20.49 ?  3   VAL   B CA   1 
ATOM   3821 C C    A VAL   B 1 3   ? 46.606 -14.753 -18.604 0.78 18.05 ?  3   VAL   B C    1 
ATOM   3822 C C    B VAL   B 1 3   ? 46.521 -14.601 -18.508 0.22 18.00 ?  3   VAL   B C    1 
ATOM   3823 O O    A VAL   B 1 3   ? 45.877 -14.825 -19.596 0.78 18.51 ?  3   VAL   B O    1 
ATOM   3824 O O    B VAL   B 1 3   ? 45.695 -14.500 -19.420 0.22 17.65 ?  3   VAL   B O    1 
ATOM   3825 C CB   A VAL   B 1 3   ? 47.548 -12.554 -17.797 0.78 21.75 ?  3   VAL   B CB   1 
ATOM   3826 C CB   B VAL   B 1 3   ? 47.489 -12.439 -17.650 0.22 20.85 ?  3   VAL   B CB   1 
ATOM   3827 C CG1  A VAL   B 1 3   ? 48.813 -11.700 -17.700 0.78 22.40 ?  3   VAL   B CG1  1 
ATOM   3828 C CG1  B VAL   B 1 3   ? 48.751 -11.599 -17.535 0.22 21.00 ?  3   VAL   B CG1  1 
ATOM   3829 C CG2  A VAL   B 1 3   ? 46.410 -11.774 -18.448 0.78 22.58 ?  3   VAL   B CG2  1 
ATOM   3830 C CG2  B VAL   B 1 3   ? 46.355 -11.643 -18.277 0.22 21.05 ?  3   VAL   B CG2  1 
ATOM   3831 H H    A VAL   B 1 3   ? 47.610 -13.336 -20.455 0.78 25.31 ?  3   VAL   B H    1 
ATOM   3832 H H    B VAL   B 1 3   ? 47.605 -13.091 -20.322 0.22 27.46 ?  3   VAL   B H    1 
ATOM   3833 H HA   A VAL   B 1 3   ? 48.541 -14.334 -18.110 0.78 23.85 ?  3   VAL   B HA   1 
ATOM   3834 H HA   B VAL   B 1 3   ? 48.462 -14.218 -18.006 0.22 24.61 ?  3   VAL   B HA   1 
ATOM   3835 H HB   A VAL   B 1 3   ? 47.280 -12.782 -16.893 0.78 26.11 ?  3   VAL   B HB   1 
ATOM   3836 H HB   B VAL   B 1 3   ? 47.216 -12.693 -16.755 0.22 25.04 ?  3   VAL   B HB   1 
ATOM   3837 H HG11 A VAL   B 1 3   ? 48.613 -10.895 -17.197 0.78 26.89 ?  3   VAL   B HG11 1 
ATOM   3838 H HG11 B VAL   B 1 3   ? 48.556 -10.810 -17.006 0.22 25.21 ?  3   VAL   B HG11 1 
ATOM   3839 H HG12 A VAL   B 1 3   ? 49.506 -12.209 -17.249 0.78 26.89 ?  3   VAL   B HG12 1 
ATOM   3840 H HG12 B VAL   B 1 3   ? 49.442 -12.125 -17.103 0.22 25.21 ?  3   VAL   B HG12 1 
ATOM   3841 H HG13 A VAL   B 1 3   ? 49.105 -11.467 -18.595 0.78 26.89 ?  3   VAL   B HG13 1 
ATOM   3842 H HG13 B VAL   B 1 3   ? 49.039 -11.339 -18.424 0.22 25.21 ?  3   VAL   B HG13 1 
ATOM   3843 H HG21 A VAL   B 1 3   ? 46.357 -10.896 -18.039 0.78 27.12 ?  3   VAL   B HG21 1 
ATOM   3844 H HG21 B VAL   B 1 3   ? 46.299 -10.781 -17.840 0.22 25.28 ?  3   VAL   B HG21 1 
ATOM   3845 H HG22 A VAL   B 1 3   ? 46.589 -11.688 -19.396 0.78 27.12 ?  3   VAL   B HG22 1 
ATOM   3846 H HG22 B VAL   B 1 3   ? 46.537 -11.525 -19.222 0.22 25.28 ?  3   VAL   B HG22 1 
ATOM   3847 H HG23 A VAL   B 1 3   ? 45.579 -12.255 -18.309 0.78 27.12 ?  3   VAL   B HG23 1 
ATOM   3848 H HG23 B VAL   B 1 3   ? 45.523 -12.129 -18.159 0.22 25.28 ?  3   VAL   B HG23 1 
ATOM   3849 N N    . ASN   B 1 4   ? 46.387 -15.457 -17.497 1.00 16.11 ?  4   ASN   B N    1 
ATOM   3850 C CA   . ASN   B 1 4   ? 45.258 -16.382 -17.389 1.00 15.16 ?  4   ASN   B CA   1 
ATOM   3851 C C    . ASN   B 1 4   ? 45.209 -17.344 -18.577 1.00 15.34 ?  4   ASN   B C    1 
ATOM   3852 O O    . ASN   B 1 4   ? 44.148 -17.611 -19.139 1.00 16.35 ?  4   ASN   B O    1 
ATOM   3853 C CB   . ASN   B 1 4   ? 43.928 -15.639 -17.219 1.00 14.84 ?  4   ASN   B CB   1 
ATOM   3854 C CG   . ASN   B 1 4   ? 43.889 -14.810 -15.953 1.00 13.96 ?  4   ASN   B CG   1 
ATOM   3855 O OD1  . ASN   B 1 4   ? 44.180 -15.311 -14.872 1.00 13.54 ?  4   ASN   B OD1  1 
ATOM   3856 N ND2  . ASN   B 1 4   ? 43.547 -13.532 -16.083 1.00 15.03 ?  4   ASN   B ND2  1 
ATOM   3857 H H    A ASN   B 1 4   ? 46.886 -15.430 -16.798 0.78 19.35 ?  4   ASN   B H    1 
ATOM   3858 H H    B ASN   B 1 4   ? 46.942 -15.514 -16.843 0.22 19.35 ?  4   ASN   B H    1 
ATOM   3859 H HA   . ASN   B 1 4   ? 45.388 -16.921 -16.592 1.00 18.20 ?  4   ASN   B HA   1 
ATOM   3860 H HB2  . ASN   B 1 4   ? 43.794 -15.044 -17.970 1.00 17.82 ?  4   ASN   B HB2  1 
ATOM   3861 H HB3  . ASN   B 1 4   ? 43.204 -16.288 -17.176 1.00 17.82 ?  4   ASN   B HB3  1 
ATOM   3862 H HD21 . ASN   B 1 4   ? 43.512 -13.019 -15.390 1.00 18.05 ?  4   ASN   B HD21 1 
ATOM   3863 H HD22 . ASN   B 1 4   ? 43.354 -13.214 -16.858 1.00 18.05 ?  4   ASN   B HD22 1 
ATOM   3864 N N    . SER   B 1 5   ? 46.370 -17.867 -18.967 1.00 16.73 ?  5   SER   B N    1 
ATOM   3865 C CA   . SER   B 1 5   ? 46.462 -18.792 -20.100 1.00 19.26 ?  5   SER   B CA   1 
ATOM   3866 C C    . SER   B 1 5   ? 46.463 -20.227 -19.581 1.00 20.39 ?  5   SER   B C    1 
ATOM   3867 O O    . SER   B 1 5   ? 47.481 -20.912 -19.550 1.00 22.58 ?  5   SER   B O    1 
ATOM   3868 C CB   . SER   B 1 5   ? 47.708 -18.497 -20.932 1.00 21.17 ?  5   SER   B CB   1 
ATOM   3869 O OG   . SER   B 1 5   ? 48.881 -18.645 -20.151 1.00 23.89 ?  5   SER   B OG   1 
ATOM   3870 H H    . SER   B 1 5   ? 47.126 -17.700 -18.592 1.00 20.09 ?  5   SER   B H    1 
ATOM   3871 H HA   . SER   B 1 5   ? 45.690 -18.680 -20.672 1.00 23.13 ?  5   SER   B HA   1 
ATOM   3872 H HB2  . SER   B 1 5   ? 47.742 -19.112 -21.685 1.00 25.42 ?  5   SER   B HB2  1 
ATOM   3873 H HB3  . SER   B 1 5   ? 47.650 -17.587 -21.258 1.00 25.42 ?  5   SER   B HB3  1 
ATOM   3874 H HG   . SER   B 1 5   ? 48.957 -19.441 -19.895 1.00 28.68 ?  5   SER   B HG   1 
ATOM   3875 N N    . PHE   B 1 6   ? 45.283 -20.665 -19.155 1.00 20.42 ?  6   PHE   B N    1 
ATOM   3876 C CA   . PHE   B 1 6   ? 45.114 -22.011 -18.625 1.00 19.81 ?  6   PHE   B CA   1 
ATOM   3877 C C    . PHE   B 1 6   ? 45.051 -23.004 -19.775 1.00 22.87 ?  6   PHE   B C    1 
ATOM   3878 O O    . PHE   B 1 6   ? 44.363 -22.768 -20.772 1.00 24.90 ?  6   PHE   B O    1 
ATOM   3879 C CB   . PHE   B 1 6   ? 43.828 -22.088 -17.802 1.00 18.01 ?  6   PHE   B CB   1 
ATOM   3880 C CG   . PHE   B 1 6   ? 43.836 -21.213 -16.577 1.00 16.01 ?  6   PHE   B CG   1 
ATOM   3881 C CD1  . PHE   B 1 6   ? 44.351 -21.686 -15.385 1.00 14.70 ?  6   PHE   B CD1  1 
ATOM   3882 C CD2  . PHE   B 1 6   ? 43.332 -19.919 -16.619 1.00 15.49 ?  6   PHE   B CD2  1 
ATOM   3883 C CE1  . PHE   B 1 6   ? 44.352 -20.894 -14.249 1.00 14.36 ?  6   PHE   B CE1  1 
ATOM   3884 C CE2  . PHE   B 1 6   ? 43.340 -19.116 -15.488 1.00 15.96 ?  6   PHE   B CE2  1 
ATOM   3885 C CZ   . PHE   B 1 6   ? 43.856 -19.598 -14.305 1.00 14.91 ?  6   PHE   B CZ   1 
ATOM   3886 H H    . PHE   B 1 6   ? 44.556 -20.205 -19.171 1.00 24.52 ?  6   PHE   B H    1 
ATOM   3887 H HA   . PHE   B 1 6   ? 45.863 -22.239 -18.052 1.00 23.79 ?  6   PHE   B HA   1 
ATOM   3888 H HB2  . PHE   B 1 6   ? 43.081 -21.812 -18.355 1.00 21.62 ?  6   PHE   B HB2  1 
ATOM   3889 H HB3  . PHE   B 1 6   ? 43.696 -23.005 -17.507 1.00 21.62 ?  6   PHE   B HB3  1 
ATOM   3890 H HD1  . PHE   B 1 6   ? 44.693 -22.550 -15.337 1.00 17.65 ?  6   PHE   B HD1  1 
ATOM   3891 H HD2  . PHE   B 1 6   ? 42.982 -19.592 -17.413 1.00 18.61 ?  6   PHE   B HD2  1 
ATOM   3892 H HE1  . PHE   B 1 6   ? 44.712 -21.215 -13.448 1.00 17.25 ?  6   PHE   B HE1  1 
ATOM   3893 H HE2  . PHE   B 1 6   ? 42.999 -18.251 -15.529 1.00 19.16 ?  6   PHE   B HE2  1 
ATOM   3894 H HZ   . PHE   B 1 6   ? 43.864 -19.061 -13.543 1.00 17.91 ?  6   PHE   B HZ   1 
ATOM   3895 N N    A SER   B 1 7   ? 45.767 -24.120 -19.634 0.78 22.97 ?  7   SER   B N    1 
ATOM   3896 N N    B SER   B 1 7   ? 45.776 -24.114 -19.635 0.22 23.76 ?  7   SER   B N    1 
ATOM   3897 C CA   A SER   B 1 7   ? 45.834 -25.124 -20.686 0.78 24.74 ?  7   SER   B CA   1 
ATOM   3898 C CA   B SER   B 1 7   ? 45.876 -25.118 -20.684 0.22 24.88 ?  7   SER   B CA   1 
ATOM   3899 C C    A SER   B 1 7   ? 45.801 -26.519 -20.078 0.78 23.95 ?  7   SER   B C    1 
ATOM   3900 C C    B SER   B 1 7   ? 45.841 -26.508 -20.070 0.22 24.54 ?  7   SER   B C    1 
ATOM   3901 O O    A SER   B 1 7   ? 46.382 -26.759 -19.015 0.78 24.95 ?  7   SER   B O    1 
ATOM   3902 O O    B SER   B 1 7   ? 46.424 -26.743 -19.008 0.22 24.91 ?  7   SER   B O    1 
ATOM   3903 C CB   A SER   B 1 7   ? 47.108 -24.957 -21.526 0.78 27.48 ?  7   SER   B CB   1 
ATOM   3904 C CB   B SER   B 1 7   ? 47.176 -24.952 -21.482 0.22 26.10 ?  7   SER   B CB   1 
ATOM   3905 O OG   A SER   B 1 7   ? 47.072 -25.779 -22.677 0.78 29.76 ?  7   SER   B OG   1 
ATOM   3906 O OG   B SER   B 1 7   ? 47.312 -25.971 -22.457 0.22 27.03 ?  7   SER   B OG   1 
ATOM   3907 H H    A SER   B 1 7   ? 46.225 -24.316 -18.932 0.78 27.58 ?  7   SER   B H    1 
ATOM   3908 H H    B SER   B 1 7   ? 46.228 -24.308 -18.928 0.22 28.52 ?  7   SER   B H    1 
ATOM   3909 H HA   A SER   B 1 7   ? 45.068 -25.031 -21.270 0.78 29.71 ?  7   SER   B HA   1 
ATOM   3910 H HA   B SER   B 1 7   ? 45.126 -25.030 -21.291 0.22 29.87 ?  7   SER   B HA   1 
ATOM   3911 H HB2  A SER   B 1 7   ? 47.180 -24.030 -21.805 0.78 32.99 ?  7   SER   B HB2  1 
ATOM   3912 H HB2  B SER   B 1 7   ? 47.164 -24.090 -21.927 0.22 31.34 ?  7   SER   B HB2  1 
ATOM   3913 H HB3  A SER   B 1 7   ? 47.876 -25.199 -20.985 0.78 32.99 ?  7   SER   B HB3  1 
ATOM   3914 H HB3  B SER   B 1 7   ? 47.928 -24.999 -20.872 0.22 31.34 ?  7   SER   B HB3  1 
ATOM   3915 H HG   A SER   B 1 7   ? 47.776 -25.680 -23.124 0.78 35.73 ?  7   SER   B HG   1 
ATOM   3916 H HG   B SER   B 1 7   ? 48.027 -25.865 -22.885 0.22 32.45 ?  7   SER   B HG   1 
ATOM   3917 N N    A GLY   B 1 8   ? 45.120 -27.436 -20.763 0.78 23.98 ?  8   GLY   B N    1 
ATOM   3918 N N    B GLY   B 1 8   ? 45.154 -27.426 -20.747 0.22 24.12 ?  8   GLY   B N    1 
ATOM   3919 C CA   A GLY   B 1 8   ? 45.104 -28.824 -20.353 0.78 23.43 ?  8   GLY   B CA   1 
ATOM   3920 C CA   B GLY   B 1 8   ? 45.129 -28.810 -20.324 0.22 23.35 ?  8   GLY   B CA   1 
ATOM   3921 C C    A GLY   B 1 8   ? 44.127 -29.160 -19.254 0.78 22.31 ?  8   GLY   B C    1 
ATOM   3922 C C    B GLY   B 1 8   ? 44.171 -29.124 -19.201 0.22 22.31 ?  8   GLY   B C    1 
ATOM   3923 O O    A GLY   B 1 8   ? 44.237 -30.237 -18.655 0.78 23.43 ?  8   GLY   B O    1 
ATOM   3924 O O    B GLY   B 1 8   ? 44.347 -30.142 -18.524 0.22 22.74 ?  8   GLY   B O    1 
ATOM   3925 H H    A GLY   B 1 8   ? 44.660 -27.270 -21.469 0.78 28.79 ?  8   GLY   B H    1 
ATOM   3926 H H    B GLY   B 1 8   ? 44.694 -27.266 -21.456 0.22 28.96 ?  8   GLY   B H    1 
ATOM   3927 H HA2  A GLY   B 1 8   ? 44.884 -29.374 -21.122 0.78 28.13 ?  8   GLY   B HA2  1 
ATOM   3928 H HA2  B GLY   B 1 8   ? 44.894 -29.366 -21.084 0.22 28.04 ?  8   GLY   B HA2  1 
ATOM   3929 H HA3  A GLY   B 1 8   ? 45.988 -29.074 -20.049 0.78 28.13 ?  8   GLY   B HA3  1 
ATOM   3930 H HA3  B GLY   B 1 8   ? 46.015 -29.065 -20.028 0.22 28.04 ?  8   GLY   B HA3  1 
ATOM   3931 N N    . TYR   B 1 9   ? 43.160 -28.290 -18.978 1.00 21.11 ?  9   TYR   B N    1 
ATOM   3932 C CA   . TYR   B 1 9   ? 42.180 -28.553 -17.937 1.00 18.91 ?  9   TYR   B CA   1 
ATOM   3933 C C    . TYR   B 1 9   ? 40.999 -29.339 -18.477 1.00 18.25 ?  9   TYR   B C    1 
ATOM   3934 O O    . TYR   B 1 9   ? 40.594 -29.188 -19.633 1.00 20.40 ?  9   TYR   B O    1 
ATOM   3935 C CB   . TYR   B 1 9   ? 41.668 -27.258 -17.312 1.00 18.39 ?  9   TYR   B CB   1 
ATOM   3936 C CG   . TYR   B 1 9   ? 42.678 -26.630 -16.385 1.00 17.78 ?  9   TYR   B CG   1 
ATOM   3937 C CD1  . TYR   B 1 9   ? 43.785 -25.965 -16.891 1.00 18.45 ?  9   TYR   B CD1  1 
ATOM   3938 C CD2  . TYR   B 1 9   ? 42.549 -26.730 -15.007 1.00 16.90 ?  9   TYR   B CD2  1 
ATOM   3939 C CE1  . TYR   B 1 9   ? 44.727 -25.409 -16.056 1.00 18.58 ?  9   TYR   B CE1  1 
ATOM   3940 C CE2  . TYR   B 1 9   ? 43.488 -26.173 -14.160 1.00 17.51 ?  9   TYR   B CE2  1 
ATOM   3941 C CZ   . TYR   B 1 9   ? 44.575 -25.509 -14.693 1.00 18.56 ?  9   TYR   B CZ   1 
ATOM   3942 O OH   . TYR   B 1 9   ? 45.519 -24.958 -13.864 1.00 19.42 ?  9   TYR   B OH   1 
ATOM   3943 H H    A TYR   B 1 9   ? 43.039 -27.546 -19.392 0.78 25.34 ?  9   TYR   B H    1 
ATOM   3944 H H    B TYR   B 1 9   ? 43.014 -27.569 -19.423 0.22 25.34 ?  9   TYR   B H    1 
ATOM   3945 H HA   . TYR   B 1 9   ? 42.590 -29.075 -17.234 1.00 22.71 ?  9   TYR   B HA   1 
ATOM   3946 H HB2  . TYR   B 1 9   ? 41.460 -26.616 -18.011 1.00 22.08 ?  9   TYR   B HB2  1 
ATOM   3947 H HB3  . TYR   B 1 9   ? 40.876 -27.457 -16.794 1.00 22.08 ?  9   TYR   B HB3  1 
ATOM   3948 H HD1  . TYR   B 1 9   ? 43.892 -25.894 -17.812 1.00 22.16 ?  9   TYR   B HD1  1 
ATOM   3949 H HD2  . TYR   B 1 9   ? 41.814 -27.180 -14.648 1.00 20.30 ?  9   TYR   B HD2  1 
ATOM   3950 H HE1  . TYR   B 1 9   ? 45.457 -24.965 -16.409 1.00 22.31 ?  9   TYR   B HE1  1 
ATOM   3951 H HE2  . TYR   B 1 9   ? 43.379 -26.250 -13.238 1.00 21.03 ?  9   TYR   B HE2  1 
ATOM   3952 H HH   . TYR   B 1 9   ? 46.115 -24.596 -14.321 1.00 23.32 ?  9   TYR   B HH   1 
ATOM   3953 N N    . LEU   B 1 10  ? 40.450 -30.180 -17.613 1.00 16.43 ?  10  LEU   B N    1 
ATOM   3954 C CA   . LEU   B 1 10  ? 39.241 -30.932 -17.896 1.00 16.40 ?  10  LEU   B CA   1 
ATOM   3955 C C    . LEU   B 1 10  ? 38.052 -30.164 -17.335 1.00 15.76 ?  10  LEU   B C    1 
ATOM   3956 O O    . LEU   B 1 10  ? 38.063 -29.752 -16.170 1.00 15.80 ?  10  LEU   B O    1 
ATOM   3957 C CB   . LEU   B 1 10  ? 39.339 -32.309 -17.242 1.00 17.37 ?  10  LEU   B CB   1 
ATOM   3958 C CG   . LEU   B 1 10  ? 38.175 -33.245 -17.539 1.00 19.41 ?  10  LEU   B CG   1 
ATOM   3959 C CD1  . LEU   B 1 10  ? 38.243 -33.745 -18.975 1.00 21.14 ?  10  LEU   B CD1  1 
ATOM   3960 C CD2  . LEU   B 1 10  ? 38.147 -34.401 -16.557 1.00 20.66 ?  10  LEU   B CD2  1 
ATOM   3961 H H    . LEU   B 1 10  ? 40.769 -30.338 -16.823 1.00 19.73 ?  10  LEU   B H    1 
ATOM   3962 H HA   . LEU   B 1 10  ? 39.130 -31.042 -18.851 1.00 19.69 ?  10  LEU   B HA   1 
ATOM   3963 H HB2  . LEU   B 1 10  ? 40.151 -32.744 -17.551 1.00 20.86 ?  10  LEU   B HB2  1 
ATOM   3964 H HB3  . LEU   B 1 10  ? 39.384 -32.195 -16.277 1.00 20.86 ?  10  LEU   B HB3  1 
ATOM   3965 H HG   . LEU   B 1 10  ? 37.345 -32.755 -17.437 1.00 23.31 ?  10  LEU   B HG   1 
ATOM   3966 H HD11 . LEU   B 1 10  ? 37.518 -34.371 -19.123 1.00 25.38 ?  10  LEU   B HD11 1 
ATOM   3967 H HD12 . LEU   B 1 10  ? 38.154 -32.987 -19.576 1.00 25.38 ?  10  LEU   B HD12 1 
ATOM   3968 H HD13 . LEU   B 1 10  ? 39.095 -34.182 -19.116 1.00 25.38 ?  10  LEU   B HD13 1 
ATOM   3969 H HD21 . LEU   B 1 10  ? 37.400 -34.978 -16.776 1.00 24.80 ?  10  LEU   B HD21 1 
ATOM   3970 H HD22 . LEU   B 1 10  ? 38.979 -34.889 -16.625 1.00 24.80 ?  10  LEU   B HD22 1 
ATOM   3971 H HD23 . LEU   B 1 10  ? 38.040 -34.044 -15.661 1.00 24.80 ?  10  LEU   B HD23 1 
ATOM   3972 N N    . LYS   B 1 11  ? 37.029 -29.980 -18.159 1.00 16.85 ?  11  LYS   B N    1 
ATOM   3973 C CA   . LYS   B 1 11  ? 35.837 -29.256 -17.745 1.00 18.64 ?  11  LYS   B CA   1 
ATOM   3974 C C    . LYS   B 1 11  ? 34.937 -30.180 -16.929 1.00 17.88 ?  11  LYS   B C    1 
ATOM   3975 O O    . LYS   B 1 11  ? 34.534 -31.245 -17.408 1.00 19.79 ?  11  LYS   B O    1 
ATOM   3976 C CB   . LYS   B 1 11  ? 35.109 -28.751 -18.990 1.00 22.30 ?  11  LYS   B CB   1 
ATOM   3977 C CG   . LYS   B 1 11  ? 33.940 -27.824 -18.726 1.00 25.70 ?  11  LYS   B CG   1 
ATOM   3978 C CD   . LYS   B 1 11  ? 33.211 -27.501 -20.024 1.00 28.67 ?  11  LYS   B CD   1 
ATOM   3979 C CE   . LYS   B 1 11  ? 32.156 -26.428 -19.825 1.00 30.94 ?  11  LYS   B CE   1 
ATOM   3980 N NZ   . LYS   B 1 11  ? 32.765 -25.107 -19.519 1.00 32.25 ?  11  LYS   B NZ   1 
ATOM   3981 H H    . LYS   B 1 11  ? 36.997 -30.275 -18.967 1.00 20.23 ?  11  LYS   B H    1 
ATOM   3982 H HA   . LYS   B 1 11  ? 36.088 -28.496 -17.197 1.00 22.38 ?  11  LYS   B HA   1 
ATOM   3983 H HB2  . LYS   B 1 11  ? 35.744 -28.268 -19.542 1.00 26.78 ?  11  LYS   B HB2  1 
ATOM   3984 H HB3  . LYS   B 1 11  ? 34.770 -29.515 -19.480 1.00 26.78 ?  11  LYS   B HB3  1 
ATOM   3985 H HG2  . LYS   B 1 11  ? 33.315 -28.255 -18.124 1.00 30.86 ?  11  LYS   B HG2  1 
ATOM   3986 H HG3  . LYS   B 1 11  ? 34.265 -26.995 -18.343 1.00 30.86 ?  11  LYS   B HG3  1 
ATOM   3987 H HD2  . LYS   B 1 11  ? 33.852 -27.179 -20.679 1.00 34.42 ?  11  LYS   B HD2  1 
ATOM   3988 H HD3  . LYS   B 1 11  ? 32.773 -28.303 -20.352 1.00 34.42 ?  11  LYS   B HD3  1 
ATOM   3989 H HE2  . LYS   B 1 11  ? 31.631 -26.341 -20.637 1.00 37.15 ?  11  LYS   B HE2  1 
ATOM   3990 H HE3  . LYS   B 1 11  ? 31.584 -26.680 -19.083 1.00 37.15 ?  11  LYS   B HE3  1 
ATOM   3991 H HZ1  . LYS   B 1 11  ? 32.132 -24.483 -19.476 1.00 38.72 ?  11  LYS   B HZ1  1 
ATOM   3992 H HZ2  . LYS   B 1 11  ? 33.192 -25.141 -18.740 1.00 38.72 ?  11  LYS   B HZ2  1 
ATOM   3993 H HZ3  . LYS   B 1 11  ? 33.345 -24.886 -20.158 1.00 38.72 ?  11  LYS   B HZ3  1 
ATOM   3994 N N    . LEU   B 1 12  ? 34.611 -29.769 -15.703 1.00 16.44 ?  12  LEU   B N    1 
ATOM   3995 C CA   . LEU   B 1 12  ? 33.657 -30.485 -14.862 1.00 16.38 ?  12  LEU   B CA   1 
ATOM   3996 C C    . LEU   B 1 12  ? 32.262 -29.887 -14.950 1.00 16.62 ?  12  LEU   B C    1 
ATOM   3997 O O    . LEU   B 1 12  ? 31.278 -30.613 -15.107 1.00 17.28 ?  12  LEU   B O    1 
ATOM   3998 C CB   . LEU   B 1 12  ? 34.117 -30.496 -13.401 1.00 15.98 ?  12  LEU   B CB   1 
ATOM   3999 C CG   . LEU   B 1 12  ? 35.453 -31.179 -13.116 1.00 15.89 ?  12  LEU   B CG   1 
ATOM   4000 C CD1  . LEU   B 1 12  ? 35.768 -31.136 -11.633 1.00 15.98 ?  12  LEU   B CD1  1 
ATOM   4001 C CD2  . LEU   B 1 12  ? 35.450 -32.613 -13.627 1.00 16.78 ?  12  LEU   B CD2  1 
ATOM   4002 H H    . LEU   B 1 12  ? 34.930 -29.060 -15.334 1.00 19.75 ?  12  LEU   B H    1 
ATOM   4003 H HA   . LEU   B 1 12  ? 33.598 -31.402 -15.170 1.00 19.67 ?  12  LEU   B HA   1 
ATOM   4004 H HB2  . LEU   B 1 12  ? 34.191 -29.576 -13.101 1.00 19.20 ?  12  LEU   B HB2  1 
ATOM   4005 H HB3  . LEU   B 1 12  ? 33.440 -30.951 -12.876 1.00 19.20 ?  12  LEU   B HB3  1 
ATOM   4006 H HG   . LEU   B 1 12  ? 36.155 -30.699 -13.583 1.00 19.08 ?  12  LEU   B HG   1 
ATOM   4007 H HD11 . LEU   B 1 12  ? 36.623 -31.575 -11.480 1.00 19.19 ?  12  LEU   B HD11 1 
ATOM   4008 H HD12 . LEU   B 1 12  ? 35.815 -30.214 -11.344 1.00 19.19 ?  12  LEU   B HD12 1 
ATOM   4009 H HD13 . LEU   B 1 12  ? 35.069 -31.603 -11.147 1.00 19.19 ?  12  LEU   B HD13 1 
ATOM   4010 H HD21 . LEU   B 1 12  ? 36.244 -33.062 -13.301 1.00 20.15 ?  12  LEU   B HD21 1 
ATOM   4011 H HD22 . LEU   B 1 12  ? 34.655 -33.059 -13.303 1.00 20.15 ?  12  LEU   B HD22 1 
ATOM   4012 H HD23 . LEU   B 1 12  ? 35.452 -32.599 -14.598 1.00 20.15 ?  12  LEU   B HD23 1 
ATOM   4013 N N    . THR   B 1 13  ? 32.167 -28.567 -14.840 1.00 16.71 ?  13  THR   B N    1 
ATOM   4014 C CA   . THR   B 1 13  ? 30.935 -27.819 -15.035 1.00 16.41 ?  13  THR   B CA   1 
ATOM   4015 C C    . THR   B 1 13  ? 31.260 -26.611 -15.906 1.00 18.13 ?  13  THR   B C    1 
ATOM   4016 O O    . THR   B 1 13  ? 32.404 -26.406 -16.327 1.00 18.82 ?  13  THR   B O    1 
ATOM   4017 C CB   . THR   B 1 13  ? 30.345 -27.354 -13.699 1.00 15.99 ?  13  THR   B CB   1 
ATOM   4018 O OG1  . THR   B 1 13  ? 31.187 -26.326 -13.154 1.00 15.79 ?  13  THR   B OG1  1 
ATOM   4019 C CG2  . THR   B 1 13  ? 30.244 -28.514 -12.706 1.00 16.54 ?  13  THR   B CG2  1 
ATOM   4020 H H    . THR   B 1 13  ? 32.834 -28.059 -14.640 1.00 20.06 ?  13  THR   B H    1 
ATOM   4021 H HA   . THR   B 1 13  ? 30.280 -28.375 -15.485 1.00 19.71 ?  13  THR   B HA   1 
ATOM   4022 H HB   . THR   B 1 13  ? 29.454 -26.994 -13.845 1.00 19.20 ?  13  THR   B HB   1 
ATOM   4023 H HG1  . THR   B 1 13  ? 30.856 -25.565 -13.318 1.00 18.96 ?  13  THR   B HG1  1 
ATOM   4024 H HG21 . THR   B 1 13  ? 29.725 -28.244 -11.933 1.00 19.87 ?  13  THR   B HG21 1 
ATOM   4025 H HG22 . THR   B 1 13  ? 29.812 -29.271 -13.128 1.00 19.87 ?  13  THR   B HG22 1 
ATOM   4026 H HG23 . THR   B 1 13  ? 31.131 -28.779 -12.415 1.00 19.87 ?  13  THR   B HG23 1 
ATOM   4027 N N    A ASP   B 1 14  ? 30.240 -25.790 -16.162 0.78 19.30 ?  14  ASP   B N    1 
ATOM   4028 N N    B ASP   B 1 14  ? 30.245 -25.779 -16.155 0.22 18.85 ?  14  ASP   B N    1 
ATOM   4029 C CA   A ASP   B 1 14  ? 30.439 -24.617 -17.008 0.78 20.91 ?  14  ASP   B CA   1 
ATOM   4030 C CA   B ASP   B 1 14  ? 30.434 -24.615 -17.014 0.22 19.63 ?  14  ASP   B CA   1 
ATOM   4031 C C    A ASP   B 1 14  ? 31.531 -23.699 -16.474 0.78 18.73 ?  14  ASP   B C    1 
ATOM   4032 C C    B ASP   B 1 14  ? 31.437 -23.618 -16.450 0.22 17.82 ?  14  ASP   B C    1 
ATOM   4033 O O    A ASP   B 1 14  ? 32.161 -22.974 -17.255 0.78 20.40 ?  14  ASP   B O    1 
ATOM   4034 O O    B ASP   B 1 14  ? 31.888 -22.735 -17.188 0.22 18.10 ?  14  ASP   B O    1 
ATOM   4035 C CB   A ASP   B 1 14  ? 29.126 -23.847 -17.154 0.78 25.01 ?  14  ASP   B CB   1 
ATOM   4036 C CB   B ASP   B 1 14  ? 29.103 -23.900 -17.252 0.22 22.13 ?  14  ASP   B CB   1 
ATOM   4037 C CG   A ASP   B 1 14  ? 28.163 -24.510 -18.112 0.78 29.24 ?  14  ASP   B CG   1 
ATOM   4038 C CG   B ASP   B 1 14  ? 28.216 -24.636 -18.237 0.22 24.38 ?  14  ASP   B CG   1 
ATOM   4039 O OD1  A ASP   B 1 14  ? 28.555 -25.482 -18.795 0.78 30.63 ?  14  ASP   B OD1  1 
ATOM   4040 O OD1  B ASP   B 1 14  ? 28.758 -25.318 -19.132 0.22 25.09 ?  14  ASP   B OD1  1 
ATOM   4041 O OD2  A ASP   B 1 14  ? 27.004 -24.058 -18.177 0.78 30.86 -1 14  ASP   B OD2  1 
ATOM   4042 O OD2  B ASP   B 1 14  ? 26.977 -24.535 -18.117 0.22 25.16 -1 14  ASP   B OD2  1 
ATOM   4043 H H    A ASP   B 1 14  ? 29.444 -25.877 -15.849 0.78 23.17 ?  14  ASP   B H    1 
ATOM   4044 H H    B ASP   B 1 14  ? 29.450 -25.861 -15.839 0.22 22.64 ?  14  ASP   B H    1 
ATOM   4045 H HA   A ASP   B 1 14  ? 30.710 -24.909 -17.889 0.78 25.11 ?  14  ASP   B HA   1 
ATOM   4046 H HA   B ASP   B 1 14  ? 30.765 -24.916 -17.874 0.22 23.57 ?  14  ASP   B HA   1 
ATOM   4047 H HB2  A ASP   B 1 14  ? 28.683 -23.798 -16.293 0.78 30.03 ?  14  ASP   B HB2  1 
ATOM   4048 H HB2  B ASP   B 1 14  ? 28.626 -23.835 -16.411 0.22 26.57 ?  14  ASP   B HB2  1 
ATOM   4049 H HB3  A ASP   B 1 14  ? 29.314 -22.953 -17.482 0.78 30.03 ?  14  ASP   B HB3  1 
ATOM   4050 H HB3  B ASP   B 1 14  ? 29.284 -23.007 -17.597 0.22 26.57 ?  14  ASP   B HB3  1 
ATOM   4051 N N    . ASN   B 1 15  ? 31.776 -23.713 -15.161 1.00 16.07 ?  15  ASN   B N    1 
ATOM   4052 C CA   . ASN   B 1 15  ? 32.733 -22.790 -14.560 1.00 13.94 ?  15  ASN   B CA   1 
ATOM   4053 C C    . ASN   B 1 15  ? 33.826 -23.441 -13.721 1.00 13.01 ?  15  ASN   B C    1 
ATOM   4054 O O    . ASN   B 1 15  ? 34.661 -22.710 -13.181 1.00 13.78 ?  15  ASN   B O    1 
ATOM   4055 C CB   . ASN   B 1 15  ? 32.012 -21.736 -13.705 1.00 14.29 ?  15  ASN   B CB   1 
ATOM   4056 C CG   . ASN   B 1 15  ? 31.391 -22.334 -12.465 1.00 14.11 ?  15  ASN   B CG   1 
ATOM   4057 O OD1  . ASN   B 1 15  ? 30.441 -23.128 -12.549 1.00 15.75 ?  15  ASN   B OD1  1 
ATOM   4058 N ND2  . ASN   B 1 15  ? 31.922 -21.986 -11.307 1.00 13.69 ?  15  ASN   B ND2  1 
ATOM   4059 H H    A ASN   B 1 15  ? 31.399 -24.249 -14.599 0.78 19.29 ?  15  ASN   B H    1 
ATOM   4060 H H    B ASN   B 1 15  ? 31.441 -24.286 -14.610 0.22 19.29 ?  15  ASN   B H    1 
ATOM   4061 H HA   . ASN   B 1 15  ? 33.179 -22.310 -15.267 1.00 16.75 ?  15  ASN   B HA   1 
ATOM   4062 H HB2  . ASN   B 1 15  ? 32.652 -21.058 -13.427 1.00 17.17 ?  15  ASN   B HB2  1 
ATOM   4063 H HB3  . ASN   B 1 15  ? 31.304 -21.323 -14.227 1.00 17.17 ?  15  ASN   B HB3  1 
ATOM   4064 H HD21 . ASN   B 1 15  ? 31.604 -22.296 -10.569 1.00 16.44 ?  15  ASN   B HD21 1 
ATOM   4065 H HD22 . ASN   B 1 15  ? 32.590 -21.436 -11.281 1.00 16.44 ?  15  ASN   B HD22 1 
ATOM   4066 N N    . VAL   B 1 16  ? 33.855 -24.765 -13.590 1.00 13.00 ?  16  VAL   B N    1 
ATOM   4067 C CA   . VAL   B 1 16  ? 34.853 -25.454 -12.777 1.00 12.72 ?  16  VAL   B CA   1 
ATOM   4068 C C    . VAL   B 1 16  ? 35.650 -26.390 -13.671 1.00 12.70 ?  16  VAL   B C    1 
ATOM   4069 O O    . VAL   B 1 16  ? 35.073 -27.259 -14.343 1.00 13.96 ?  16  VAL   B O    1 
ATOM   4070 C CB   . VAL   B 1 16  ? 34.217 -26.226 -11.608 1.00 13.17 ?  16  VAL   B CB   1 
ATOM   4071 C CG1  . VAL   B 1 16  ? 35.293 -26.958 -10.800 1.00 13.44 ?  16  VAL   B CG1  1 
ATOM   4072 C CG2  . VAL   B 1 16  ? 33.394 -25.288 -10.724 1.00 13.99 ?  16  VAL   B CG2  1 
ATOM   4073 H H    . VAL   B 1 16  ? 33.295 -25.299 -13.970 1.00 15.61 ?  16  VAL   B H    1 
ATOM   4074 H HA   . VAL   B 1 16  ? 35.465 -24.795 -12.402 1.00 15.28 ?  16  VAL   B HA   1 
ATOM   4075 H HB   . VAL   B 1 16  ? 33.619 -26.895 -11.972 1.00 15.82 ?  16  VAL   B HB   1 
ATOM   4076 H HG11 . VAL   B 1 16  ? 34.901 -27.270 -9.968  1.00 16.14 ?  16  VAL   B HG11 1 
ATOM   4077 H HG12 . VAL   B 1 16  ? 35.621 -27.711 -11.312 1.00 16.14 ?  16  VAL   B HG12 1 
ATOM   4078 H HG13 . VAL   B 1 16  ? 36.019 -26.342 -10.609 1.00 16.14 ?  16  VAL   B HG13 1 
ATOM   4079 H HG21 . VAL   B 1 16  ? 33.044 -25.793 -9.971  1.00 16.80 ?  16  VAL   B HG21 1 
ATOM   4080 H HG22 . VAL   B 1 16  ? 33.955 -24.568 -10.410 1.00 16.80 ?  16  VAL   B HG22 1 
ATOM   4081 H HG23 . VAL   B 1 16  ? 32.655 -24.931 -11.247 1.00 16.80 ?  16  VAL   B HG23 1 
ATOM   4082 N N    . TYR   B 1 17  ? 36.975 -26.232 -13.634 1.00 13.18 ?  17  TYR   B N    1 
ATOM   4083 C CA   . TYR   B 1 17  ? 37.924 -26.979 -14.447 1.00 13.49 ?  17  TYR   B CA   1 
ATOM   4084 C C    . TYR   B 1 17  ? 38.966 -27.595 -13.527 1.00 12.62 ?  17  TYR   B C    1 
ATOM   4085 O O    . TYR   B 1 17  ? 39.235 -27.063 -12.446 1.00 13.08 ?  17  TYR   B O    1 
ATOM   4086 C CB   . TYR   B 1 17  ? 38.633 -26.042 -15.431 1.00 15.60 ?  17  TYR   B CB   1 
ATOM   4087 C CG   . TYR   B 1 17  ? 37.701 -25.274 -16.334 1.00 18.61 ?  17  TYR   B CG   1 
ATOM   4088 C CD1  . TYR   B 1 17  ? 37.099 -24.092 -15.913 1.00 19.48 ?  17  TYR   B CD1  1 
ATOM   4089 C CD2  . TYR   B 1 17  ? 37.424 -25.732 -17.613 1.00 20.59 ?  17  TYR   B CD2  1 
ATOM   4090 C CE1  . TYR   B 1 17  ? 36.243 -23.391 -16.745 1.00 21.20 ?  17  TYR   B CE1  1 
ATOM   4091 C CE2  . TYR   B 1 17  ? 36.577 -25.038 -18.452 1.00 22.08 ?  17  TYR   B CE2  1 
ATOM   4092 C CZ   . TYR   B 1 17  ? 35.987 -23.872 -18.013 1.00 22.73 ?  17  TYR   B CZ   1 
ATOM   4093 O OH   . TYR   B 1 17  ? 35.144 -23.182 -18.848 1.00 24.57 ?  17  TYR   B OH   1 
ATOM   4094 H H    . TYR   B 1 17  ? 37.371 -25.664 -13.113 1.00 15.83 ?  17  TYR   B H    1 
ATOM   4095 H HA   . TYR   B 1 17  ? 37.467 -27.684 -14.938 1.00 16.20 ?  17  TYR   B HA   1 
ATOM   4096 H HB2  . TYR   B 1 17  ? 39.161 -25.403 -14.932 1.00 18.74 ?  17  TYR   B HB2  1 
ATOM   4097 H HB3  . TYR   B 1 17  ? 39.208 -26.573 -16.000 1.00 18.74 ?  17  TYR   B HB3  1 
ATOM   4098 H HD1  . TYR   B 1 17  ? 37.271 -23.767 -15.059 1.00 23.39 ?  17  TYR   B HD1  1 
ATOM   4099 H HD2  . TYR   B 1 17  ? 37.814 -26.518 -17.915 1.00 24.72 ?  17  TYR   B HD2  1 
ATOM   4100 H HE1  . TYR   B 1 17  ? 35.846 -22.600 -16.454 1.00 25.46 ?  17  TYR   B HE1  1 
ATOM   4101 H HE2  . TYR   B 1 17  ? 36.395 -25.358 -19.308 1.00 26.52 ?  17  TYR   B HE2  1 
ATOM   4102 H HH   . TYR   B 1 17  ? 35.070 -23.576 -19.584 1.00 29.50 ?  17  TYR   B HH   1 
ATOM   4103 N N    . ILE   B 1 18  ? 39.587 -28.695 -13.960 1.00 12.66 ?  18  ILE   B N    1 
ATOM   4104 C CA   . ILE   B 1 18  ? 40.518 -29.416 -13.096 1.00 12.56 ?  18  ILE   B CA   1 
ATOM   4105 C C    . ILE   B 1 18  ? 41.685 -29.963 -13.910 1.00 13.02 ?  18  ILE   B C    1 
ATOM   4106 O O    . ILE   B 1 18  ? 41.530 -30.366 -15.068 1.00 14.35 ?  18  ILE   B O    1 
ATOM   4107 C CB   . ILE   B 1 18  ? 39.770 -30.520 -12.308 1.00 13.35 ?  18  ILE   B CB   1 
ATOM   4108 C CG1  . ILE   B 1 18  ? 40.623 -31.068 -11.160 1.00 13.87 ?  18  ILE   B CG1  1 
ATOM   4109 C CG2  . ILE   B 1 18  ? 39.280 -31.630 -13.247 1.00 13.83 ?  18  ILE   B CG2  1 
ATOM   4110 C CD1  . ILE   B 1 18  ? 39.799 -31.844 -10.138 1.00 15.63 ?  18  ILE   B CD1  1 
ATOM   4111 H H    . ILE   B 1 18  ? 39.497 -29.039 -14.743 1.00 15.20 ?  18  ILE   B H    1 
ATOM   4112 H HA   . ILE   B 1 18  ? 40.880 -28.800 -12.440 1.00 15.08 ?  18  ILE   B HA   1 
ATOM   4113 H HB   . ILE   B 1 18  ? 38.984 -30.120 -11.911 1.00 16.04 ?  18  ILE   B HB   1 
ATOM   4114 H HG12 . ILE   B 1 18  ? 41.296 -31.664 -11.517 1.00 16.65 ?  18  ILE   B HG12 1 
ATOM   4115 H HG13 . ILE   B 1 18  ? 41.044 -30.324 -10.700 1.00 16.65 ?  18  ILE   B HG13 1 
ATOM   4116 H HG21 . ILE   B 1 18  ? 38.689 -32.222 -12.755 1.00 16.61 ?  18  ILE   B HG21 1 
ATOM   4117 H HG22 . ILE   B 1 18  ? 38.804 -31.224 -13.986 1.00 16.61 ?  18  ILE   B HG22 1 
ATOM   4118 H HG23 . ILE   B 1 18  ? 40.045 -32.127 -13.576 1.00 16.61 ?  18  ILE   B HG23 1 
ATOM   4119 H HD11 . ILE   B 1 18  ? 40.381 -32.136 -9.419  1.00 18.77 ?  18  ILE   B HD11 1 
ATOM   4120 H HD12 . ILE   B 1 18  ? 39.105 -31.263 -9.785  1.00 18.77 ?  18  ILE   B HD12 1 
ATOM   4121 H HD13 . ILE   B 1 18  ? 39.397 -32.612 -10.573 1.00 18.77 ?  18  ILE   B HD13 1 
ATOM   4122 N N    . LYS   B 1 19  ? 42.863 -29.994 -13.284 1.00 13.47 ?  19  LYS   B N    1 
ATOM   4123 C CA   . LYS   B 1 19  ? 44.075 -30.476 -13.936 1.00 14.24 ?  19  LYS   B CA   1 
ATOM   4124 C C    . LYS   B 1 19  ? 44.968 -31.152 -12.909 1.00 13.92 ?  19  LYS   B C    1 
ATOM   4125 O O    . LYS   B 1 19  ? 45.047 -30.713 -11.761 1.00 13.58 ?  19  LYS   B O    1 
ATOM   4126 C CB   . LYS   B 1 19  ? 44.849 -29.314 -14.575 1.00 15.81 ?  19  LYS   B CB   1 
ATOM   4127 C CG   . LYS   B 1 19  ? 46.081 -29.717 -15.370 1.00 17.45 ?  19  LYS   B CG   1 
ATOM   4128 C CD   . LYS   B 1 19  ? 46.789 -28.482 -15.913 1.00 19.06 ?  19  LYS   B CD   1 
ATOM   4129 C CE   . LYS   B 1 19  ? 47.956 -28.850 -16.810 1.00 21.01 ?  19  LYS   B CE   1 
ATOM   4130 N NZ   . LYS   B 1 19  ? 48.713 -27.654 -17.269 1.00 22.14 ?  19  LYS   B NZ   1 
ATOM   4131 H H    . LYS   B 1 19  ? 42.981 -29.742 -12.466 1.00 16.18 ?  19  LYS   B H    1 
ATOM   4132 H HA   . LYS   B 1 19  ? 43.842 -31.119 -14.623 1.00 17.11 ?  19  LYS   B HA   1 
ATOM   4133 H HB2  . LYS   B 1 19  ? 44.250 -28.846 -15.178 1.00 18.98 ?  19  LYS   B HB2  1 
ATOM   4134 H HB3  . LYS   B 1 19  ? 45.133 -28.710 -13.868 1.00 18.98 ?  19  LYS   B HB3  1 
ATOM   4135 H HG2  . LYS   B 1 19  ? 46.693 -30.198 -14.793 1.00 20.96 ?  19  LYS   B HG2  1 
ATOM   4136 H HG3  . LYS   B 1 19  ? 45.809 -30.273 -16.117 1.00 20.96 ?  19  LYS   B HG3  1 
ATOM   4137 H HD2  . LYS   B 1 19  ? 46.159 -27.954 -16.430 1.00 22.89 ?  19  LYS   B HD2  1 
ATOM   4138 H HD3  . LYS   B 1 19  ? 47.130 -27.959 -15.169 1.00 22.89 ?  19  LYS   B HD3  1 
ATOM   4139 H HE2  . LYS   B 1 19  ? 48.562 -29.426 -16.320 1.00 25.23 ?  19  LYS   B HE2  1 
ATOM   4140 H HE3  . LYS   B 1 19  ? 47.616 -29.314 -17.593 1.00 25.23 ?  19  LYS   B HE3  1 
ATOM   4141 H HZ1  . LYS   B 1 19  ? 49.349 -27.900 -17.841 1.00 26.58 ?  19  LYS   B HZ1  1 
ATOM   4142 H HZ2  . LYS   B 1 19  ? 48.164 -27.083 -17.674 1.00 26.58 ?  19  LYS   B HZ2  1 
ATOM   4143 H HZ3  . LYS   B 1 19  ? 49.091 -27.250 -16.573 1.00 26.58 ?  19  LYS   B HZ3  1 
ATOM   4144 N N    . ASN   B 1 20  ? 45.655 -32.209 -13.337 1.00 14.90 ?  20  ASN   B N    1 
ATOM   4145 C CA   . ASN   B 1 20  ? 46.693 -32.834 -12.523 1.00 15.75 ?  20  ASN   B CA   1 
ATOM   4146 C C    . ASN   B 1 20  ? 47.961 -32.009 -12.711 1.00 16.39 ?  20  ASN   B C    1 
ATOM   4147 O O    . ASN   B 1 20  ? 48.616 -32.091 -13.754 1.00 18.55 ?  20  ASN   B O    1 
ATOM   4148 C CB   . ASN   B 1 20  ? 46.882 -34.280 -12.972 1.00 17.23 ?  20  ASN   B CB   1 
ATOM   4149 C CG   . ASN   B 1 20  ? 48.032 -34.984 -12.276 1.00 18.79 ?  20  ASN   B CG   1 
ATOM   4150 O OD1  . ASN   B 1 20  ? 48.699 -35.834 -12.873 1.00 21.30 ?  20  ASN   B OD1  1 
ATOM   4151 N ND2  . ASN   B 1 20  ? 48.260 -34.660 -11.014 1.00 18.20 ?  20  ASN   B ND2  1 
ATOM   4152 H H    . ASN   B 1 20  ? 45.547 -32.576 -14.105 1.00 17.89 ?  20  ASN   B H    1 
ATOM   4153 H HA   . ASN   B 1 20  ? 46.425 -32.821 -11.589 1.00 18.91 ?  20  ASN   B HA   1 
ATOM   4154 H HB2  . ASN   B 1 20  ? 46.071 -34.776 -12.778 1.00 20.68 ?  20  ASN   B HB2  1 
ATOM   4155 H HB3  . ASN   B 1 20  ? 47.055 -34.288 -13.925 1.00 20.68 ?  20  ASN   B HB3  1 
ATOM   4156 H HD21 . ASN   B 1 20  ? 48.906 -35.027 -10.587 1.00 21.85 ?  20  ASN   B HD21 1 
ATOM   4157 H HD22 . ASN   B 1 20  ? 47.769 -34.068 -10.621 1.00 21.85 ?  20  ASN   B HD22 1 
ATOM   4158 N N    . ALA   B 1 21  ? 48.303 -31.192 -11.711 1.00 16.07 ?  21  ALA   B N    1 
ATOM   4159 C CA   . ALA   B 1 21  ? 49.404 -30.252 -11.858 1.00 16.71 ?  21  ALA   B CA   1 
ATOM   4160 C C    . ALA   B 1 21  ? 49.859 -29.766 -10.492 1.00 15.96 ?  21  ALA   B C    1 
ATOM   4161 O O    . ALA   B 1 21  ? 49.107 -29.797 -9.514  1.00 16.05 ?  21  ALA   B O    1 
ATOM   4162 C CB   . ALA   B 1 21  ? 48.998 -29.062 -12.727 1.00 18.11 ?  21  ALA   B CB   1 
ATOM   4163 H H    . ALA   B 1 21  ? 47.907 -31.167 -10.941 1.00 19.30 ?  21  ALA   B H    1 
ATOM   4164 H HA   . ALA   B 1 21  ? 50.147 -30.706 -12.280 1.00 20.07 ?  21  ALA   B HA   1 
ATOM   4165 H HB1  . ALA   B 1 21  ? 49.778 -28.513 -12.874 1.00 21.75 ?  21  ALA   B HB1  1 
ATOM   4166 H HB2  . ALA   B 1 21  ? 48.659 -29.397 -13.570 1.00 21.75 ?  21  ALA   B HB2  1 
ATOM   4167 H HB3  . ALA   B 1 21  ? 48.307 -28.558 -12.267 1.00 21.75 ?  21  ALA   B HB3  1 
ATOM   4168 N N    . ASP   B 1 22  ? 51.119 -29.324 -10.459 1.00 15.73 ?  22  ASP   B N    1 
ATOM   4169 C CA   . ASP   B 1 22  ? 51.724 -28.625 -9.332  1.00 15.22 ?  22  ASP   B CA   1 
ATOM   4170 C C    . ASP   B 1 22  ? 51.319 -27.155 -9.426  1.00 14.02 ?  22  ASP   B C    1 
ATOM   4171 O O    . ASP   B 1 22  ? 51.637 -26.484 -10.413 1.00 14.32 ?  22  ASP   B O    1 
ATOM   4172 C CB   . ASP   B 1 22  ? 53.241 -28.807 -9.477  1.00 16.94 ?  22  ASP   B CB   1 
ATOM   4173 C CG   . ASP   B 1 22  ? 54.066 -28.039 -8.450  1.00 18.66 ?  22  ASP   B CG   1 
ATOM   4174 O OD1  . ASP   B 1 22  ? 53.693 -26.928 -8.043  1.00 19.03 ?  22  ASP   B OD1  1 
ATOM   4175 O OD2  . ASP   B 1 22  ? 55.149 -28.544 -8.080  1.00 20.86 -1 22  ASP   B OD2  1 
ATOM   4176 H H    . ASP   B 1 22  ? 51.667 -29.432 -11.116 1.00 18.89 ?  22  ASP   B H    1 
ATOM   4177 H HA   . ASP   B 1 22  ? 51.428 -29.006 -8.488  1.00 18.28 ?  22  ASP   B HA   1 
ATOM   4178 H HB2  . ASP   B 1 22  ? 53.459 -29.745 -9.387  1.00 20.35 ?  22  ASP   B HB2  1 
ATOM   4179 H HB3  . ASP   B 1 22  ? 53.509 -28.489 -10.354 1.00 20.35 ?  22  ASP   B HB3  1 
ATOM   4180 N N    . ILE   B 1 23  ? 50.606 -26.658 -8.411  1.00 13.11 ?  23  ILE   B N    1 
ATOM   4181 C CA   . ILE   B 1 23  ? 50.011 -25.323 -8.492  1.00 12.73 ?  23  ILE   B CA   1 
ATOM   4182 C C    . ILE   B 1 23  ? 51.065 -24.232 -8.628  1.00 12.25 ?  23  ILE   B C    1 
ATOM   4183 O O    . ILE   B 1 23  ? 50.795 -23.187 -9.229  1.00 11.94 ?  23  ILE   B O    1 
ATOM   4184 C CB   . ILE   B 1 23  ? 49.071 -25.081 -7.298  1.00 13.05 ?  23  ILE   B CB   1 
ATOM   4185 C CG1  . ILE   B 1 23  ? 48.231 -23.820 -7.509  1.00 13.67 ?  23  ILE   B CG1  1 
ATOM   4186 C CG2  . ILE   B 1 23  ? 49.841 -25.037 -5.994  1.00 14.13 ?  23  ILE   B CG2  1 
ATOM   4187 C CD1  . ILE   B 1 23  ? 47.130 -23.657 -6.480  1.00 14.54 ?  23  ILE   B CD1  1 
ATOM   4188 H H    . ILE   B 1 23  ? 50.463 -27.072 -7.670  1.00 15.74 ?  23  ILE   B H    1 
ATOM   4189 H HA   . ILE   B 1 23  ? 49.471 -25.294 -9.294  1.00 15.29 ?  23  ILE   B HA   1 
ATOM   4190 H HB   . ILE   B 1 23  ? 48.460 -25.833 -7.256  1.00 15.68 ?  23  ILE   B HB   1 
ATOM   4191 H HG12 . ILE   B 1 23  ? 48.811 -23.041 -7.455  1.00 16.42 ?  23  ILE   B HG12 1 
ATOM   4192 H HG13 . ILE   B 1 23  ? 47.819 -23.857 -8.390  1.00 16.42 ?  23  ILE   B HG13 1 
ATOM   4193 H HG21 . ILE   B 1 23  ? 49.211 -25.042 -5.258  1.00 16.98 ?  23  ILE   B HG21 1 
ATOM   4194 H HG22 . ILE   B 1 23  ? 50.418 -25.815 -5.942  1.00 16.98 ?  23  ILE   B HG22 1 
ATOM   4195 H HG23 . ILE   B 1 23  ? 50.375 -24.228 -5.970  1.00 16.98 ?  23  ILE   B HG23 1 
ATOM   4196 H HD11 . ILE   B 1 23  ? 46.580 -22.901 -6.727  1.00 17.46 ?  23  ILE   B HD11 1 
ATOM   4197 H HD12 . ILE   B 1 23  ? 46.597 -24.468 -6.469  1.00 17.46 ?  23  ILE   B HD12 1 
ATOM   4198 H HD13 . ILE   B 1 23  ? 47.533 -23.512 -5.613  1.00 17.46 ?  23  ILE   B HD13 1 
ATOM   4199 N N    . VAL   B 1 24  ? 52.260 -24.430 -8.063  1.00 12.61 ?  24  VAL   B N    1 
ATOM   4200 C CA   . VAL   B 1 24  ? 53.334 -23.448 -8.234  1.00 13.30 ?  24  VAL   B CA   1 
ATOM   4201 C C    . VAL   B 1 24  ? 53.783 -23.402 -9.688  1.00 13.55 ?  24  VAL   B C    1 
ATOM   4202 O O    . VAL   B 1 24  ? 53.929 -22.325 -10.283 1.00 14.13 ?  24  VAL   B O    1 
ATOM   4203 C CB   . VAL   B 1 24  ? 54.514 -23.767 -7.295  1.00 14.57 ?  24  VAL   B CB   1 
ATOM   4204 C CG1  . VAL   B 1 24  ? 55.730 -22.901 -7.642  1.00 15.27 ?  24  VAL   B CG1  1 
ATOM   4205 C CG2  . VAL   B 1 24  ? 54.111 -23.567 -5.853  1.00 15.71 ?  24  VAL   B CG2  1 
ATOM   4206 H H    . VAL   B 1 24  ? 52.469 -25.109 -7.579  1.00 15.15 ?  24  VAL   B H    1 
ATOM   4207 H HA   . VAL   B 1 24  ? 52.999 -22.572 -7.997  1.00 15.97 ?  24  VAL   B HA   1 
ATOM   4208 H HB   . VAL   B 1 24  ? 54.767 -24.699 -7.403  1.00 17.50 ?  24  VAL   B HB   1 
ATOM   4209 H HG11 . VAL   B 1 24  ? 56.326 -22.877 -6.877  1.00 18.34 ?  24  VAL   B HG11 1 
ATOM   4210 H HG12 . VAL   B 1 24  ? 56.187 -23.296 -8.401  1.00 18.34 ?  24  VAL   B HG12 1 
ATOM   4211 H HG13 . VAL   B 1 24  ? 55.429 -22.007 -7.856  1.00 18.34 ?  24  VAL   B HG13 1 
ATOM   4212 H HG21 . VAL   B 1 24  ? 54.840 -23.843 -5.276  1.00 18.87 ?  24  VAL   B HG21 1 
ATOM   4213 H HG22 . VAL   B 1 24  ? 53.911 -22.629 -5.708  1.00 18.87 ?  24  VAL   B HG22 1 
ATOM   4214 H HG23 . VAL   B 1 24  ? 53.323 -24.105 -5.666  1.00 18.87 ?  24  VAL   B HG23 1 
ATOM   4215 N N    . GLU   B 1 25  ? 54.045 -24.574 -10.273 1.00 14.50 ?  25  GLU   B N    1 
ATOM   4216 C CA   . GLU   B 1 25  ? 54.438 -24.615 -11.675 1.00 15.92 ?  25  GLU   B CA   1 
ATOM   4217 C C    . GLU   B 1 25  ? 53.332 -24.068 -12.564 1.00 14.51 ?  25  GLU   B C    1 
ATOM   4218 O O    . GLU   B 1 25  ? 53.600 -23.361 -13.544 1.00 15.50 ?  25  GLU   B O    1 
ATOM   4219 C CB   . GLU   B 1 25  ? 54.822 -26.043 -12.061 1.00 20.62 ?  25  GLU   B CB   1 
ATOM   4220 C CG   . GLU   B 1 25  ? 56.120 -26.498 -11.409 1.00 27.27 ?  25  GLU   B CG   1 
ATOM   4221 C CD   . GLU   B 1 25  ? 57.234 -25.464 -11.510 1.00 33.40 ?  25  GLU   B CD   1 
ATOM   4222 O OE1  . GLU   B 1 25  ? 57.613 -25.094 -12.642 1.00 35.68 ?  25  GLU   B OE1  1 
ATOM   4223 O OE2  . GLU   B 1 25  ? 57.716 -25.001 -10.451 1.00 35.67 -1 25  GLU   B OE2  1 
ATOM   4224 H H    . GLU   B 1 25  ? 53.999 -25.342 -9.883  1.00 17.41 ?  25  GLU   B H    1 
ATOM   4225 H HA   . GLU   B 1 25  ? 55.201 -24.037 -11.798 1.00 19.12 ?  25  GLU   B HA   1 
ATOM   4226 H HB2  . GLU   B 1 25  ? 54.117 -26.650 -11.775 1.00 24.76 ?  25  GLU   B HB2  1 
ATOM   4227 H HB3  . GLU   B 1 25  ? 54.931 -26.093 -13.021 1.00 24.76 ?  25  GLU   B HB3  1 
ATOM   4228 H HG2  . GLU   B 1 25  ? 55.963 -26.655 -10.470 1.00 32.74 ?  25  GLU   B HG2  1 
ATOM   4229 H HG3  . GLU   B 1 25  ? 56.420 -27.309 -11.845 1.00 32.74 ?  25  GLU   B HG3  1 
ATOM   4230 N N    . GLU   B 1 26  ? 52.079 -24.375 -12.228 1.00 13.75 ?  26  GLU   B N    1 
ATOM   4231 C CA   . GLU   B 1 26  ? 50.957 -23.843 -12.992 1.00 14.25 ?  26  GLU   B CA   1 
ATOM   4232 C C    . GLU   B 1 26  ? 50.911 -22.325 -12.912 1.00 13.68 ?  26  GLU   B C    1 
ATOM   4233 O O    . GLU   B 1 26  ? 50.710 -21.645 -13.923 1.00 15.11 ?  26  GLU   B O    1 
ATOM   4234 C CB   . GLU   B 1 26  ? 49.646 -24.425 -12.465 1.00 15.87 ?  26  GLU   B CB   1 
ATOM   4235 C CG   . GLU   B 1 26  ? 49.219 -25.716 -13.121 1.00 19.42 ?  26  GLU   B CG   1 
ATOM   4236 C CD   . GLU   B 1 26  ? 48.974 -25.577 -14.622 1.00 21.06 ?  26  GLU   B CD   1 
ATOM   4237 O OE1  . GLU   B 1 26  ? 48.003 -24.916 -15.050 1.00 21.51 ?  26  GLU   B OE1  1 
ATOM   4238 O OE2  . GLU   B 1 26  ? 49.759 -26.157 -15.380 1.00 22.98 -1 26  GLU   B OE2  1 
ATOM   4239 H H    . GLU   B 1 26  ? 51.854 -24.885 -11.566 1.00 16.52 ?  26  GLU   B H    1 
ATOM   4240 H HA   . GLU   B 1 26  ? 51.056 -24.098 -13.919 1.00 17.12 ?  26  GLU   B HA   1 
ATOM   4241 H HB2  . GLU   B 1 26  ? 49.736 -24.597 -11.514 1.00 19.06 ?  26  GLU   B HB2  1 
ATOM   4242 H HB3  . GLU   B 1 26  ? 48.937 -23.776 -12.610 1.00 19.06 ?  26  GLU   B HB3  1 
ATOM   4243 H HG2  . GLU   B 1 26  ? 49.919 -26.369 -12.989 1.00 23.32 ?  26  GLU   B HG2  1 
ATOM   4244 H HG3  . GLU   B 1 26  ? 48.394 -26.021 -12.711 1.00 23.32 ?  26  GLU   B HG3  1 
ATOM   4245 N N    . ALA   B 1 27  ? 51.062 -21.777 -11.706 1.00 13.03 ?  27  ALA   B N    1 
ATOM   4246 C CA   . ALA   B 1 27  ? 51.021 -20.328 -11.558 1.00 13.46 ?  27  ALA   B CA   1 
ATOM   4247 C C    . ALA   B 1 27  ? 52.091 -19.663 -12.413 1.00 14.35 ?  27  ALA   B C    1 
ATOM   4248 O O    . ALA   B 1 27  ? 51.825 -18.665 -13.099 1.00 14.93 ?  27  ALA   B O    1 
ATOM   4249 C CB   . ALA   B 1 27  ? 51.176 -19.951 -10.086 1.00 13.91 ?  27  ALA   B CB   1 
ATOM   4250 H H    . ALA   B 1 27  ? 51.188 -22.215 -10.974 1.00 15.65 ?  27  ALA   B H    1 
ATOM   4251 H HA   . ALA   B 1 27  ? 50.161 -20.005 -11.855 1.00 16.16 ?  27  ALA   B HA   1 
ATOM   4252 H HB1  . ALA   B 1 27  ? 51.139 -18.987 -9.999  1.00 16.70 ?  27  ALA   B HB1  1 
ATOM   4253 H HB2  . ALA   B 1 27  ? 50.448 -20.354 -9.580  1.00 16.70 ?  27  ALA   B HB2  1 
ATOM   4254 H HB3  . ALA   B 1 27  ? 52.025 -20.283 -9.758  1.00 16.70 ?  27  ALA   B HB3  1 
ATOM   4255 N N    . LYS   B 1 28  ? 53.309 -20.205 -12.393 1.00 15.67 ?  28  LYS   B N    1 
ATOM   4256 C CA   . LYS   B 1 28  ? 54.387 -19.587 -13.156 1.00 18.29 ?  28  LYS   B CA   1 
ATOM   4257 C C    . LYS   B 1 28  ? 54.128 -19.657 -14.655 1.00 19.16 ?  28  LYS   B C    1 
ATOM   4258 O O    . LYS   B 1 28  ? 54.553 -18.762 -15.399 1.00 19.97 ?  28  LYS   B O    1 
ATOM   4259 C CB   . LYS   B 1 28  ? 55.741 -20.196 -12.777 1.00 21.39 ?  28  LYS   B CB   1 
ATOM   4260 C CG   . LYS   B 1 28  ? 56.135 -19.893 -11.335 1.00 24.51 ?  28  LYS   B CG   1 
ATOM   4261 C CD   . LYS   B 1 28  ? 57.563 -20.303 -11.002 1.00 29.30 ?  28  LYS   B CD   1 
ATOM   4262 C CE   . LYS   B 1 28  ? 57.668 -21.782 -10.705 1.00 32.89 ?  28  LYS   B CE   1 
ATOM   4263 N NZ   . LYS   B 1 28  ? 59.025 -22.149 -10.206 1.00 34.64 ?  28  LYS   B NZ   1 
ATOM   4264 H H    . LYS   B 1 28  ? 53.538 -20.904 -11.947 1.00 18.82 ?  28  LYS   B H    1 
ATOM   4265 H HA   . LYS   B 1 28  ? 54.428 -18.645 -12.925 1.00 21.96 ?  28  LYS   B HA   1 
ATOM   4266 H HB2  . LYS   B 1 28  ? 55.698 -21.156 -12.880 1.00 25.69 ?  28  LYS   B HB2  1 
ATOM   4267 H HB3  . LYS   B 1 28  ? 56.429 -19.828 -13.357 1.00 25.69 ?  28  LYS   B HB3  1 
ATOM   4268 H HG2  . LYS   B 1 28  ? 56.053 -18.938 -11.184 1.00 29.43 ?  28  LYS   B HG2  1 
ATOM   4269 H HG3  . LYS   B 1 28  ? 55.538 -20.374 -10.743 1.00 29.43 ?  28  LYS   B HG3  1 
ATOM   4270 H HD2  . LYS   B 1 28  ? 58.135 -20.100 -11.759 1.00 35.17 ?  28  LYS   B HD2  1 
ATOM   4271 H HD3  . LYS   B 1 28  ? 57.856 -19.810 -10.219 1.00 35.17 ?  28  LYS   B HD3  1 
ATOM   4272 H HE2  . LYS   B 1 28  ? 57.020 -22.017 -10.022 1.00 39.49 ?  28  LYS   B HE2  1 
ATOM   4273 H HE3  . LYS   B 1 28  ? 57.497 -22.285 -11.516 1.00 39.49 ?  28  LYS   B HE3  1 
ATOM   4274 H HZ1  . LYS   B 1 28  ? 59.063 -23.022 -10.038 1.00 41.59 ?  28  LYS   B HZ1  1 
ATOM   4275 H HZ2  . LYS   B 1 28  ? 59.640 -21.946 -10.817 1.00 41.59 ?  28  LYS   B HZ2  1 
ATOM   4276 H HZ3  . LYS   B 1 28  ? 59.205 -21.703 -9.456  1.00 41.59 ?  28  LYS   B HZ3  1 
ATOM   4277 N N    A LYS   B 1 29  ? 53.418 -20.687 -15.114 0.78 19.72 ?  29  LYS   B N    1 
ATOM   4278 N N    B LYS   B 1 29  ? 53.409 -20.684 -15.115 0.22 20.35 ?  29  LYS   B N    1 
ATOM   4279 C CA   A LYS   B 1 29  ? 53.133 -20.833 -16.536 0.78 22.02 ?  29  LYS   B CA   1 
ATOM   4280 C CA   B LYS   B 1 29  ? 53.131 -20.825 -16.540 0.22 22.02 ?  29  LYS   B CA   1 
ATOM   4281 C C    A LYS   B 1 29  ? 51.879 -20.079 -16.968 0.78 20.95 ?  29  LYS   B C    1 
ATOM   4282 C C    B LYS   B 1 29  ? 51.873 -20.079 -16.971 0.22 20.88 ?  29  LYS   B C    1 
ATOM   4283 O O    A LYS   B 1 29  ? 51.881 -19.442 -18.027 0.78 22.28 ?  29  LYS   B O    1 
ATOM   4284 O O    B LYS   B 1 29  ? 51.865 -19.443 -18.031 0.22 21.39 ?  29  LYS   B O    1 
ATOM   4285 C CB   A LYS   B 1 29  ? 53.009 -22.315 -16.898 0.78 26.24 ?  29  LYS   B CB   1 
ATOM   4286 C CB   B LYS   B 1 29  ? 53.014 -22.306 -16.912 0.22 25.13 ?  29  LYS   B CB   1 
ATOM   4287 C CG   A LYS   B 1 29  ? 52.798 -22.573 -18.377 0.78 30.23 ?  29  LYS   B CG   1 
ATOM   4288 C CG   B LYS   B 1 29  ? 52.881 -22.560 -18.407 0.22 27.98 ?  29  LYS   B CG   1 
ATOM   4289 C CD   A LYS   B 1 29  ? 53.021 -24.039 -18.721 0.78 33.25 ?  29  LYS   B CD   1 
ATOM   4290 C CD   B LYS   B 1 29  ? 53.105 -24.030 -18.738 0.22 30.13 ?  29  LYS   B CD   1 
ATOM   4291 C CE   A LYS   B 1 29  ? 51.907 -24.927 -18.188 0.78 35.39 ?  29  LYS   B CE   1 
ATOM   4292 C CE   B LYS   B 1 29  ? 52.017 -24.915 -18.150 0.22 31.63 ?  29  LYS   B CE   1 
ATOM   4293 N NZ   A LYS   B 1 29  ? 52.119 -26.358 -18.559 0.78 36.61 ?  29  LYS   B NZ   1 
ATOM   4294 N NZ   B LYS   B 1 29  ? 52.230 -26.350 -18.493 0.22 32.57 ?  29  LYS   B NZ   1 
ATOM   4295 H H    A LYS   B 1 29  ? 53.088 -21.308 -14.616 0.78 23.68 ?  29  LYS   B H    1 
ATOM   4296 H H    B LYS   B 1 29  ? 53.074 -21.311 -14.620 0.22 24.44 ?  29  LYS   B H    1 
ATOM   4297 H HA   A LYS   B 1 29  ? 53.877 -20.473 -17.034 0.78 26.43 ?  29  LYS   B HA   1 
ATOM   4298 H HA   B LYS   B 1 29  ? 53.875 -20.458 -17.033 0.22 26.44 ?  29  LYS   B HA   1 
ATOM   4299 H HB2  A LYS   B 1 29  ? 53.829 -22.765 -16.636 0.78 31.50 ?  29  LYS   B HB2  1 
ATOM   4300 H HB2  B LYS   B 1 29  ? 53.810 -22.769 -16.605 0.22 30.17 ?  29  LYS   B HB2  1 
ATOM   4301 H HB3  A LYS   B 1 29  ? 52.258 -22.693 -16.422 0.78 31.50 ?  29  LYS   B HB3  1 
ATOM   4302 H HB3  B LYS   B 1 29  ? 52.231 -22.677 -16.479 0.22 30.17 ?  29  LYS   B HB3  1 
ATOM   4303 H HG2  A LYS   B 1 29  ? 51.888 -22.337 -18.615 0.78 36.29 ?  29  LYS   B HG2  1 
ATOM   4304 H HG2  B LYS   B 1 29  ? 51.988 -22.315 -18.698 0.22 33.59 ?  29  LYS   B HG2  1 
ATOM   4305 H HG3  A LYS   B 1 29  ? 53.428 -22.040 -18.889 0.78 36.29 ?  29  LYS   B HG3  1 
ATOM   4306 H HG3  B LYS   B 1 29  ? 53.544 -22.035 -18.884 0.22 33.59 ?  29  LYS   B HG3  1 
ATOM   4307 H HD2  A LYS   B 1 29  ? 53.052 -24.139 -19.684 0.78 39.92 ?  29  LYS   B HD2  1 
ATOM   4308 H HD2  B LYS   B 1 29  ? 53.102 -24.146 -19.701 0.22 36.17 ?  29  LYS   B HD2  1 
ATOM   4309 H HD3  A LYS   B 1 29  ? 53.857 -24.337 -18.327 0.78 39.92 ?  29  LYS   B HD3  1 
ATOM   4310 H HD3  B LYS   B 1 29  ? 53.958 -24.313 -18.370 0.22 36.17 ?  29  LYS   B HD3  1 
ATOM   4311 H HE2  A LYS   B 1 29  ? 51.881 -24.866 -17.220 0.78 42.49 ?  29  LYS   B HE2  1 
ATOM   4312 H HE2  B LYS   B 1 29  ? 52.023 -24.833 -17.183 0.22 37.97 ?  29  LYS   B HE2  1 
ATOM   4313 H HE3  A LYS   B 1 29  ? 51.060 -24.639 -18.565 0.78 42.49 ?  29  LYS   B HE3  1 
ATOM   4314 H HE3  B LYS   B 1 29  ? 51.156 -24.641 -18.504 0.22 37.97 ?  29  LYS   B HE3  1 
ATOM   4315 H HZ1  A LYS   B 1 29  ? 51.456 -26.858 -18.238 0.78 43.95 ?  29  LYS   B HZ1  1 
ATOM   4316 H HZ1  B LYS   B 1 29  ? 51.582 -26.847 -18.138 0.22 39.10 ?  29  LYS   B HZ1  1 
ATOM   4317 H HZ2  A LYS   B 1 29  ? 52.142 -26.443 -19.445 0.78 43.95 ?  29  LYS   B HZ2  1 
ATOM   4318 H HZ2  B LYS   B 1 29  ? 52.224 -26.455 -19.377 0.22 39.10 ?  29  LYS   B HZ2  1 
ATOM   4319 H HZ3  A LYS   B 1 29  ? 52.889 -26.649 -18.221 0.78 43.95 ?  29  LYS   B HZ3  1 
ATOM   4320 H HZ3  B LYS   B 1 29  ? 53.014 -26.626 -18.174 0.22 39.10 ?  29  LYS   B HZ3  1 
ATOM   4321 N N    . VAL   B 1 30  ? 50.809 -20.145 -16.169 1.00 19.58 ?  30  VAL   B N    1 
ATOM   4322 C CA   . VAL   B 1 30  ? 49.527 -19.538 -16.546 1.00 19.43 ?  30  VAL   B CA   1 
ATOM   4323 C C    . VAL   B 1 30  ? 49.525 -18.022 -16.385 1.00 18.47 ?  30  VAL   B C    1 
ATOM   4324 O O    . VAL   B 1 30  ? 48.778 -17.316 -17.082 1.00 19.52 ?  30  VAL   B O    1 
ATOM   4325 C CB   . VAL   B 1 30  ? 48.413 -20.166 -15.685 1.00 20.39 ?  30  VAL   B CB   1 
ATOM   4326 C CG1  . VAL   B 1 30  ? 47.123 -19.363 -15.784 1.00 20.52 ?  30  VAL   B CG1  1 
ATOM   4327 C CG2  . VAL   B 1 30  ? 48.188 -21.619 -16.076 1.00 20.86 ?  30  VAL   B CG2  1 
ATOM   4328 H H    A VAL   B 1 30  ? 50.789 -20.558 -15.407 0.78 23.51 ?  30  VAL   B H    1 
ATOM   4329 H H    B VAL   B 1 30  ? 50.794 -20.548 -15.402 0.22 23.51 ?  30  VAL   B H    1 
ATOM   4330 H HA   . VAL   B 1 30  ? 49.336 -19.759 -17.471 1.00 23.34 ?  30  VAL   B HA   1 
ATOM   4331 H HB   . VAL   B 1 30  ? 48.690 -20.161 -14.755 1.00 24.48 ?  30  VAL   B HB   1 
ATOM   4332 H HG11 . VAL   B 1 30  ? 46.377 -19.948 -15.574 1.00 24.64 ?  30  VAL   B HG11 1 
ATOM   4333 H HG12 . VAL   B 1 30  ? 47.153 -18.632 -15.150 1.00 24.64 ?  30  VAL   B HG12 1 
ATOM   4334 H HG13 . VAL   B 1 30  ? 47.024 -19.030 -16.685 1.00 24.64 ?  30  VAL   B HG13 1 
ATOM   4335 H HG21 . VAL   B 1 30  ? 47.485 -21.996 -15.518 1.00 25.05 ?  30  VAL   B HG21 1 
ATOM   4336 H HG22 . VAL   B 1 30  ? 47.919 -21.659 -17.008 1.00 25.05 ?  30  VAL   B HG22 1 
ATOM   4337 H HG23 . VAL   B 1 30  ? 49.010 -22.115 -15.947 1.00 25.05 ?  30  VAL   B HG23 1 
ATOM   4338 N N    . LYS   B 1 31  ? 50.306 -17.513 -15.444 1.00 18.11 ?  31  LYS   B N    1 
ATOM   4339 C CA   . LYS   B 1 31  ? 50.329 -16.104 -15.082 1.00 18.79 ?  31  LYS   B CA   1 
ATOM   4340 C C    . LYS   B 1 31  ? 48.925 -15.642 -14.693 1.00 16.49 ?  31  LYS   B C    1 
ATOM   4341 O O    . LYS   B 1 31  ? 48.367 -14.735 -15.324 1.00 17.67 ?  31  LYS   B O    1 
ATOM   4342 C CB   . LYS   B 1 31  ? 50.957 -15.278 -16.211 1.00 22.24 ?  31  LYS   B CB   1 
ATOM   4343 C CG   . LYS   B 1 31  ? 52.370 -15.746 -16.560 1.00 25.78 ?  31  LYS   B CG   1 
ATOM   4344 C CD   . LYS   B 1 31  ? 52.942 -14.998 -17.743 1.00 29.41 ?  31  LYS   B CD   1 
ATOM   4345 C CE   . LYS   B 1 31  ? 54.421 -15.281 -17.899 1.00 32.22 ?  31  LYS   B CE   1 
ATOM   4346 N NZ   . LYS   B 1 31  ? 55.171 -14.861 -16.684 1.00 33.55 ?  31  LYS   B NZ   1 
ATOM   4347 H H    . LYS   B 1 31  ? 50.847 -17.994 -14.988 1.00 21.75 ?  31  LYS   B H    1 
ATOM   4348 H HA   . LYS   B 1 31  ? 50.884 -16.014 -14.307 1.00 22.57 ?  31  LYS   B HA   1 
ATOM   4349 H HB2  . LYS   B 1 31  ? 50.408 -15.354 -17.008 1.00 26.70 ?  31  LYS   B HB2  1 
ATOM   4350 H HB3  . LYS   B 1 31  ? 51.005 -14.354 -15.926 1.00 26.70 ?  31  LYS   B HB3  1 
ATOM   4351 H HG2  . LYS   B 1 31  ? 52.944 -15.601 -15.792 1.00 30.95 ?  31  LYS   B HG2  1 
ATOM   4352 H HG3  . LYS   B 1 31  ? 52.347 -16.692 -16.782 1.00 30.95 ?  31  LYS   B HG3  1 
ATOM   4353 H HD2  . LYS   B 1 31  ? 52.486 -15.285 -18.549 1.00 35.31 ?  31  LYS   B HD2  1 
ATOM   4354 H HD3  . LYS   B 1 31  ? 52.822 -14.048 -17.604 1.00 35.31 ?  31  LYS   B HD3  1 
ATOM   4355 H HE2  . LYS   B 1 31  ? 54.556 -16.234 -18.029 1.00 38.68 ?  31  LYS   B HE2  1 
ATOM   4356 H HE3  . LYS   B 1 31  ? 54.763 -14.785 -18.658 1.00 38.68 ?  31  LYS   B HE3  1 
ATOM   4357 H HZ1  . LYS   B 1 31  ? 56.045 -14.874 -16.846 1.00 40.27 ?  31  LYS   B HZ1  1 
ATOM   4358 H HZ2  . LYS   B 1 31  ? 54.932 -14.036 -16.450 1.00 40.27 ?  31  LYS   B HZ2  1 
ATOM   4359 H HZ3  . LYS   B 1 31  ? 54.994 -15.414 -16.009 1.00 40.27 ?  31  LYS   B HZ3  1 
ATOM   4360 N N    . PRO   B 1 32  ? 48.320 -16.249 -13.665 1.00 14.10 ?  32  PRO   B N    1 
ATOM   4361 C CA   . PRO   B 1 32  ? 46.938 -15.903 -13.308 1.00 13.22 ?  32  PRO   B CA   1 
ATOM   4362 C C    . PRO   B 1 32  ? 46.846 -14.560 -12.603 1.00 13.38 ?  32  PRO   B C    1 
ATOM   4363 O O    . PRO   B 1 32  ? 47.768 -14.129 -11.903 1.00 14.37 ?  32  PRO   B O    1 
ATOM   4364 C CB   . PRO   B 1 32  ? 46.545 -17.027 -12.339 1.00 13.35 ?  32  PRO   B CB   1 
ATOM   4365 C CG   . PRO   B 1 32  ? 47.843 -17.366 -11.663 1.00 13.65 ?  32  PRO   B CG   1 
ATOM   4366 C CD   . PRO   B 1 32  ? 48.887 -17.254 -12.743 1.00 13.83 ?  32  PRO   B CD   1 
ATOM   4367 H HA   . PRO   B 1 32  ? 46.354 -15.919 -14.087 1.00 15.87 ?  32  PRO   B HA   1 
ATOM   4368 H HB2  . PRO   B 1 32  ? 45.891 -16.704 -11.698 1.00 16.04 ?  32  PRO   B HB2  1 
ATOM   4369 H HB3  . PRO   B 1 32  ? 46.201 -17.789 -12.831 1.00 16.04 ?  32  PRO   B HB3  1 
ATOM   4370 H HG2  . PRO   B 1 32  ? 48.019 -16.729 -10.949 1.00 16.40 ?  32  PRO   B HG2  1 
ATOM   4371 H HG3  . PRO   B 1 32  ? 47.808 -18.270 -11.310 1.00 16.40 ?  32  PRO   B HG3  1 
ATOM   4372 H HD2  . PRO   B 1 32  ? 49.719 -16.936 -12.372 1.00 16.61 ?  32  PRO   B HD2  1 
ATOM   4373 H HD3  . PRO   B 1 32  ? 48.990 -18.106 -13.190 1.00 16.61 ?  32  PRO   B HD3  1 
ATOM   4374 N N    . THR   B 1 33  ? 45.695 -13.907 -12.780 1.00 12.73 ?  33  THR   B N    1 
ATOM   4375 C CA   . THR   B 1 33  ? 45.389 -12.731 -11.974 1.00 13.00 ?  33  THR   B CA   1 
ATOM   4376 C C    . THR   B 1 33  ? 45.345 -13.084 -10.494 1.00 12.71 ?  33  THR   B C    1 
ATOM   4377 O O    . THR   B 1 33  ? 45.816 -12.305 -9.651  1.00 13.65 ?  33  THR   B O    1 
ATOM   4378 C CB   . THR   B 1 33  ? 44.065 -12.108 -12.427 1.00 13.66 ?  33  THR   B CB   1 
ATOM   4379 O OG1  . THR   B 1 33  ? 44.123 -11.847 -13.831 1.00 13.65 ?  33  THR   B OG1  1 
ATOM   4380 C CG2  . THR   B 1 33  ? 43.786 -10.812 -11.670 1.00 15.27 ?  33  THR   B CG2  1 
ATOM   4381 H H    . THR   B 1 33  ? 45.075 -14.127 -13.343 1.00 15.29 ?  33  THR   B H    1 
ATOM   4382 H HA   . THR   B 1 33  ? 46.083 -12.074 -12.103 1.00 15.62 ?  33  THR   B HA   1 
ATOM   4383 H HB   . THR   B 1 33  ? 43.336 -12.728 -12.245 1.00 16.40 ?  33  THR   B HB   1 
ATOM   4384 H HG1  . THR   B 1 33  ? 43.400 -11.487 -14.086 1.00 16.40 ?  33  THR   B HG1  1 
ATOM   4385 H HG21 . THR   B 1 33  ? 43.023 -10.360 -12.060 1.00 18.34 ?  33  THR   B HG21 1 
ATOM   4386 H HG22 . THR   B 1 33  ? 43.598 -11.003 -10.738 1.00 18.34 ?  33  THR   B HG22 1 
ATOM   4387 H HG23 . THR   B 1 33  ? 44.560 -10.229 -11.724 1.00 18.34 ?  33  THR   B HG23 1 
ATOM   4388 N N    . VAL   B 1 34  ? 44.801 -14.257 -10.157 1.00 11.85 ?  34  VAL   B N    1 
ATOM   4389 C CA   . VAL   B 1 34  ? 44.612 -14.660 -8.767  1.00 11.38 ?  34  VAL   B CA   1 
ATOM   4390 C C    . VAL   B 1 34  ? 45.046 -16.105 -8.603  1.00 10.51 ?  34  VAL   B C    1 
ATOM   4391 O O    . VAL   B 1 34  ? 44.527 -16.994 -9.288  1.00 11.23 ?  34  VAL   B O    1 
ATOM   4392 C CB   . VAL   B 1 34  ? 43.143 -14.524 -8.317  1.00 12.66 ?  34  VAL   B CB   1 
ATOM   4393 C CG1  . VAL   B 1 34  ? 42.980 -14.973 -6.869  1.00 12.96 ?  34  VAL   B CG1  1 
ATOM   4394 C CG2  . VAL   B 1 34  ? 42.638 -13.099 -8.509  1.00 13.74 ?  34  VAL   B CG2  1 
ATOM   4395 H H    . VAL   B 1 34  ? 44.540 -14.850 -10.725 1.00 14.23 ?  34  VAL   B H    1 
ATOM   4396 H HA   . VAL   B 1 34  ? 45.167 -14.108 -8.191  1.00 13.67 ?  34  VAL   B HA   1 
ATOM   4397 H HB   . VAL   B 1 34  ? 42.599 -15.104 -8.867  1.00 15.21 ?  34  VAL   B HB   1 
ATOM   4398 H HG11 . VAL   B 1 34  ? 42.116 -14.670 -6.541  1.00 15.57 ?  34  VAL   B HG11 1 
ATOM   4399 H HG12 . VAL   B 1 34  ? 43.023 -15.941 -6.827  1.00 15.57 ?  34  VAL   B HG12 1 
ATOM   4400 H HG13 . VAL   B 1 34  ? 43.687 -14.584 -6.332  1.00 15.57 ?  34  VAL   B HG13 1 
ATOM   4401 H HG21 . VAL   B 1 34  ? 41.724 -13.043 -8.189  1.00 16.50 ?  34  VAL   B HG21 1 
ATOM   4402 H HG22 . VAL   B 1 34  ? 43.203 -12.492 -8.007  1.00 16.50 ?  34  VAL   B HG22 1 
ATOM   4403 H HG23 . VAL   B 1 34  ? 42.672 -12.877 -9.454  1.00 16.50 ?  34  VAL   B HG23 1 
ATOM   4404 N N    . VAL   B 1 35  ? 45.955 -16.352 -7.664  1.00 10.34 ?  35  VAL   B N    1 
ATOM   4405 C CA   . VAL   B 1 35  ? 46.195 -17.694 -7.148  1.00 10.12 ?  35  VAL   B CA   1 
ATOM   4406 C C    . VAL   B 1 35  ? 45.660 -17.756 -5.725  1.00 9.82  ?  35  VAL   B C    1 
ATOM   4407 O O    . VAL   B 1 35  ? 45.880 -16.833 -4.931  1.00 10.36 ?  35  VAL   B O    1 
ATOM   4408 C CB   . VAL   B 1 35  ? 47.681 -18.116 -7.227  1.00 10.89 ?  35  VAL   B CB   1 
ATOM   4409 C CG1  . VAL   B 1 35  ? 48.576 -17.266 -6.316  1.00 11.23 ?  35  VAL   B CG1  1 
ATOM   4410 C CG2  . VAL   B 1 35  ? 47.831 -19.605 -6.902  1.00 11.28 ?  35  VAL   B CG2  1 
ATOM   4411 H H    . VAL   B 1 35  ? 46.460 -15.748 -7.309  1.00 12.42 ?  35  VAL   B H    1 
ATOM   4412 H HA   . VAL   B 1 35  ? 45.683 -18.325 -7.682  1.00 12.15 ?  35  VAL   B HA   1 
ATOM   4413 H HB   . VAL   B 1 35  ? 47.988 -17.992 -8.140  1.00 13.09 ?  35  VAL   B HB   1 
ATOM   4414 H HG11 . VAL   B 1 35  ? 49.501 -17.489 -6.491  1.00 13.49 ?  35  VAL   B HG11 1 
ATOM   4415 H HG12 . VAL   B 1 35  ? 48.412 -16.332 -6.503  1.00 13.49 ?  35  VAL   B HG12 1 
ATOM   4416 H HG13 . VAL   B 1 35  ? 48.356 -17.464 -5.391  1.00 13.49 ?  35  VAL   B HG13 1 
ATOM   4417 H HG21 . VAL   B 1 35  ? 48.754 -19.868 -7.010  1.00 13.55 ?  35  VAL   B HG21 1 
ATOM   4418 H HG22 . VAL   B 1 35  ? 47.550 -19.760 -5.980  1.00 13.55 ?  35  VAL   B HG22 1 
ATOM   4419 H HG23 . VAL   B 1 35  ? 47.265 -20.125 -7.500  1.00 13.55 ?  35  VAL   B HG23 1 
ATOM   4420 N N    . VAL   B 1 36  ? 44.944 -18.836 -5.408  1.00 9.71  ?  36  VAL   B N    1 
ATOM   4421 C CA   . VAL   B 1 36  ? 44.397 -19.042 -4.079  1.00 9.59  ?  36  VAL   B CA   1 
ATOM   4422 C C    . VAL   B 1 36  ? 45.402 -19.803 -3.228  1.00 9.18  ?  36  VAL   B C    1 
ATOM   4423 O O    . VAL   B 1 36  ? 45.949 -20.829 -3.657  1.00 10.38 ?  36  VAL   B O    1 
ATOM   4424 C CB   . VAL   B 1 36  ? 43.060 -19.800 -4.155  1.00 10.06 ?  36  VAL   B CB   1 
ATOM   4425 C CG1  . VAL   B 1 36  ? 42.562 -20.168 -2.764  1.00 10.73 ?  36  VAL   B CG1  1 
ATOM   4426 C CG2  . VAL   B 1 36  ? 42.027 -18.968 -4.897  1.00 10.40 ?  36  VAL   B CG2  1 
ATOM   4427 H H    . VAL   B 1 36  ? 44.766 -19.476 -5.959  1.00 11.67 ?  36  VAL   B H    1 
ATOM   4428 H HA   . VAL   B 1 36  ? 44.233 -18.178 -3.665  1.00 11.52 ?  36  VAL   B HA   1 
ATOM   4429 H HB   . VAL   B 1 36  ? 43.190 -20.618 -4.654  1.00 12.09 ?  36  VAL   B HB   1 
ATOM   4430 H HG11 . VAL   B 1 36  ? 41.620 -20.394 -2.819  1.00 12.90 ?  36  VAL   B HG11 1 
ATOM   4431 H HG12 . VAL   B 1 36  ? 43.067 -20.920 -2.434  1.00 12.90 ?  36  VAL   B HG12 1 
ATOM   4432 H HG13 . VAL   B 1 36  ? 42.678 -19.400 -2.177  1.00 12.90 ?  36  VAL   B HG13 1 
ATOM   4433 H HG21 . VAL   B 1 36  ? 41.185 -19.448 -4.921  1.00 12.50 ?  36  VAL   B HG21 1 
ATOM   4434 H HG22 . VAL   B 1 36  ? 41.908 -18.119 -4.437  1.00 12.50 ?  36  VAL   B HG22 1 
ATOM   4435 H HG23 . VAL   B 1 36  ? 42.338 -18.804 -5.804  1.00 12.50 ?  36  VAL   B HG23 1 
ATOM   4436 N N    . ASN   B 1 37  ? 45.623 -19.311 -2.013  1.00 9.71  ?  37  ASN   B N    1 
ATOM   4437 C CA   . ASN   B 1 37  ? 46.376 -20.035 -1.003  1.00 10.14 ?  37  ASN   B CA   1 
ATOM   4438 C C    . ASN   B 1 37  ? 45.435 -20.709 -0.015  1.00 9.75  ?  37  ASN   B C    1 
ATOM   4439 O O    . ASN   B 1 37  ? 44.427 -20.131 0.402   1.00 10.48 ?  37  ASN   B O    1 
ATOM   4440 C CB   . ASN   B 1 37  ? 47.308 -19.089 -0.245  1.00 10.02 ?  37  ASN   B CB   1 
ATOM   4441 C CG   . ASN   B 1 37  ? 48.158 -19.804 0.772   1.00 10.28 ?  37  ASN   B CG   1 
ATOM   4442 O OD1  . ASN   B 1 37  ? 48.503 -20.979 0.594   1.00 11.12 ?  37  ASN   B OD1  1 
ATOM   4443 N ND2  . ASN   B 1 37  ? 48.508 -19.103 1.841   1.00 10.58 ?  37  ASN   B ND2  1 
ATOM   4444 H H    . ASN   B 1 37  ? 45.335 -18.543 -1.738  1.00 11.67 ?  37  ASN   B H    1 
ATOM   4445 H HA   . ASN   B 1 37  ? 46.909 -20.724 -1.429  1.00 12.18 ?  37  ASN   B HA   1 
ATOM   4446 H HB2  . ASN   B 1 37  ? 47.898 -18.661 -0.883  1.00 12.04 ?  37  ASN   B HB2  1 
ATOM   4447 H HB3  . ASN   B 1 37  ? 46.778 -18.428 0.220   1.00 12.04 ?  37  ASN   B HB3  1 
ATOM   4448 H HD21 . ASN   B 1 37  ? 48.996 -19.466 2.450   1.00 12.71 ?  37  ASN   B HD21 1 
ATOM   4449 H HD22 . ASN   B 1 37  ? 48.247 -18.296 1.931   1.00 12.71 ?  37  ASN   B HD22 1 
ATOM   4450 N N    . ALA   B 1 38  ? 45.792 -21.937 0.364   1.00 10.02 ?  38  ALA   B N    1 
ATOM   4451 C CA   . ALA   B 1 38  ? 45.130 -22.689 1.432   1.00 10.36 ?  38  ALA   B CA   1 
ATOM   4452 C C    . ALA   B 1 38  ? 45.712 -22.206 2.759   1.00 10.32 ?  38  ALA   B C    1 
ATOM   4453 O O    . ALA   B 1 38  ? 46.617 -22.812 3.342   1.00 11.26 ?  38  ALA   B O    1 
ATOM   4454 C CB   . ALA   B 1 38  ? 45.345 -24.183 1.234   1.00 11.82 ?  38  ALA   B CB   1 
ATOM   4455 H H    . ALA   B 1 38  ? 46.452 -22.369 0.017   1.00 12.04 ?  38  ALA   B H    1 
ATOM   4456 H HA   . ALA   B 1 38  ? 44.176 -22.505 1.420   1.00 12.45 ?  38  ALA   B HA   1 
ATOM   4457 H HB1  . ALA   B 1 38  ? 44.891 -24.665 1.951   1.00 14.20 ?  38  ALA   B HB1  1 
ATOM   4458 H HB2  . ALA   B 1 38  ? 44.967 -24.446 0.379   1.00 14.20 ?  38  ALA   B HB2  1 
ATOM   4459 H HB3  . ALA   B 1 38  ? 46.290 -24.376 1.256   1.00 14.20 ?  38  ALA   B HB3  1 
ATOM   4460 N N    . ALA   B 1 39  ? 45.191 -21.071 3.222   1.00 10.28 ?  39  ALA   B N    1 
ATOM   4461 C CA   . ALA   B 1 39  ? 45.745 -20.342 4.354   1.00 10.79 ?  39  ALA   B CA   1 
ATOM   4462 C C    . ALA   B 1 39  ? 45.129 -20.792 5.676   1.00 10.54 ?  39  ALA   B C    1 
ATOM   4463 O O    . ALA   B 1 39  ? 44.101 -21.466 5.719   1.00 11.50 ?  39  ALA   B O    1 
ATOM   4464 C CB   . ALA   B 1 39  ? 45.502 -18.840 4.169   1.00 11.55 ?  39  ALA   B CB   1 
ATOM   4465 H H    . ALA   B 1 39  ? 44.490 -20.697 2.884   1.00 12.35 ?  39  ALA   B H    1 
ATOM   4466 H HA   . ALA   B 1 39  ? 46.694 -20.493 4.396   1.00 12.96 ?  39  ALA   B HA   1 
ATOM   4467 H HB1  . ALA   B 1 39  ? 45.875 -18.364 4.928   1.00 13.88 ?  39  ALA   B HB1  1 
ATOM   4468 H HB2  . ALA   B 1 39  ? 45.938 -18.548 3.351   1.00 13.88 ?  39  ALA   B HB2  1 
ATOM   4469 H HB3  . ALA   B 1 39  ? 44.548 -18.672 4.110   1.00 13.88 ?  39  ALA   B HB3  1 
ATOM   4470 N N    . ASN   B 1 40  ? 45.767 -20.365 6.765   1.00 11.51 ?  40  ASN   B N    1 
ATOM   4471 C CA   . ASN   B 1 40  ? 45.208 -20.421 8.107   1.00 11.96 ?  40  ASN   B CA   1 
ATOM   4472 C C    . ASN   B 1 40  ? 45.026 -18.995 8.632   1.00 11.68 ?  40  ASN   B C    1 
ATOM   4473 O O    . ASN   B 1 40  ? 45.438 -18.013 8.005   1.00 11.73 ?  40  ASN   B O    1 
ATOM   4474 C CB   . ASN   B 1 40  ? 46.057 -21.300 9.044   1.00 13.01 ?  40  ASN   B CB   1 
ATOM   4475 C CG   . ASN   B 1 40  ? 47.513 -20.902 9.067   1.00 13.83 ?  40  ASN   B CG   1 
ATOM   4476 O OD1  . ASN   B 1 40  ? 47.834 -19.725 9.133   1.00 15.61 ?  40  ASN   B OD1  1 
ATOM   4477 N ND2  . ASN   B 1 40  ? 48.403 -21.880 9.022   1.00 14.02 ?  40  ASN   B ND2  1 
ATOM   4478 H H    . ASN   B 1 40  ? 46.557 -20.032 6.744   1.00 13.82 ?  40  ASN   B H    1 
ATOM   4479 H HA   . ASN   B 1 40  ? 44.327 -20.822 8.059   1.00 14.36 ?  40  ASN   B HA   1 
ATOM   4480 H HB2  . ASN   B 1 40  ? 45.710 -21.223 9.946   1.00 15.62 ?  40  ASN   B HB2  1 
ATOM   4481 H HB3  . ASN   B 1 40  ? 46.003 -22.220 8.744   1.00 15.62 ?  40  ASN   B HB3  1 
ATOM   4482 H HD21 . ASN   B 1 40  ? 49.245 -21.702 9.031   1.00 16.84 ?  40  ASN   B HD21 1 
ATOM   4483 H HD22 . ASN   B 1 40  ? 48.140 -22.699 8.972   1.00 16.84 ?  40  ASN   B HD22 1 
ATOM   4484 N N    . VAL   B 1 41  ? 44.373 -18.869 9.789   1.00 12.05 ?  41  VAL   B N    1 
ATOM   4485 C CA   . VAL   B 1 41  ? 43.916 -17.548 10.229  1.00 12.60 ?  41  VAL   B CA   1 
ATOM   4486 C C    . VAL   B 1 41  ? 45.067 -16.600 10.538  1.00 12.58 ?  41  VAL   B C    1 
ATOM   4487 O O    . VAL   B 1 41  ? 44.891 -15.378 10.461  1.00 12.79 ?  41  VAL   B O    1 
ATOM   4488 C CB   . VAL   B 1 41  ? 42.923 -17.619 11.405  1.00 14.19 ?  41  VAL   B CB   1 
ATOM   4489 C CG1  . VAL   B 1 41  ? 41.629 -18.299 10.983  1.00 14.64 ?  41  VAL   B CG1  1 
ATOM   4490 C CG2  . VAL   B 1 41  ? 43.551 -18.305 12.611  1.00 15.21 ?  41  VAL   B CG2  1 
ATOM   4491 H H    . VAL   B 1 41  ? 44.192 -19.510 10.327  1.00 14.47 ?  41  VAL   B H    1 
ATOM   4492 H HA   . VAL   B 1 41  ? 43.434 -17.148 9.494   1.00 15.14 ?  41  VAL   B HA   1 
ATOM   4493 H HB   . VAL   B 1 41  ? 42.697 -16.715 11.676  1.00 17.04 ?  41  VAL   B HB   1 
ATOM   4494 H HG11 . VAL   B 1 41  ? 41.009 -18.294 11.729  1.00 17.58 ?  41  VAL   B HG11 1 
ATOM   4495 H HG12 . VAL   B 1 41  ? 41.250 -17.816 10.233  1.00 17.58 ?  41  VAL   B HG12 1 
ATOM   4496 H HG13 . VAL   B 1 41  ? 41.825 -19.214 10.722  1.00 17.58 ?  41  VAL   B HG13 1 
ATOM   4497 H HG21 . VAL   B 1 41  ? 42.901 -18.335 13.330  1.00 18.27 ?  41  VAL   B HG21 1 
ATOM   4498 H HG22 . VAL   B 1 41  ? 43.812 -19.205 12.362  1.00 18.27 ?  41  VAL   B HG22 1 
ATOM   4499 H HG23 . VAL   B 1 41  ? 44.330 -17.799 12.890  1.00 18.27 ?  41  VAL   B HG23 1 
ATOM   4500 N N    . TYR   B 1 42  ? 46.232 -17.118 10.926  1.00 12.91 ?  42  TYR   B N    1 
ATOM   4501 C CA   . TYR   B 1 42  ? 47.387 -16.271 11.197  1.00 13.50 ?  42  TYR   B CA   1 
ATOM   4502 C C    . TYR   B 1 42  ? 48.353 -16.198 10.019  1.00 12.52 ?  42  TYR   B C    1 
ATOM   4503 O O    . TYR   B 1 42  ? 49.441 -15.624 10.156  1.00 13.87 ?  42  TYR   B O    1 
ATOM   4504 C CB   . TYR   B 1 42  ? 48.081 -16.672 12.507  1.00 15.75 ?  42  TYR   B CB   1 
ATOM   4505 C CG   . TYR   B 1 42  ? 47.470 -15.987 13.726  1.00 16.01 ?  42  TYR   B CG   1 
ATOM   4506 C CD1  . TYR   B 1 42  ? 47.698 -14.637 13.972  1.00 15.26 ?  42  TYR   B CD1  1 
ATOM   4507 C CD2  . TYR   B 1 42  ? 46.667 -16.682 14.617  1.00 17.93 ?  42  TYR   B CD2  1 
ATOM   4508 C CE1  . TYR   B 1 42  ? 47.143 -13.998 15.069  1.00 16.57 ?  42  TYR   B CE1  1 
ATOM   4509 C CE2  . TYR   B 1 42  ? 46.110 -16.052 15.718  1.00 18.33 ?  42  TYR   B CE2  1 
ATOM   4510 C CZ   . TYR   B 1 42  ? 46.349 -14.708 15.939  1.00 18.43 ?  42  TYR   B CZ   1 
ATOM   4511 O OH   . TYR   B 1 42  ? 45.804 -14.077 17.037  1.00 21.46 ?  42  TYR   B OH   1 
ATOM   4512 H H    . TYR   B 1 42  ? 46.377 -17.963 11.034  1.00 15.50 ?  42  TYR   B H    1 
ATOM   4513 H HA   . TYR   B 1 42  ? 47.060 -15.372 11.330  1.00 16.21 ?  42  TYR   B HA   1 
ATOM   4514 H HB2  . TYR   B 1 42  ? 48.002 -17.628 12.630  1.00 18.91 ?  42  TYR   B HB2  1 
ATOM   4515 H HB3  . TYR   B 1 42  ? 49.016 -16.416 12.458  1.00 18.91 ?  42  TYR   B HB3  1 
ATOM   4516 H HD1  . TYR   B 1 42  ? 48.235 -14.151 13.381  1.00 18.32 ?  42  TYR   B HD1  1 
ATOM   4517 H HD2  . TYR   B 1 42  ? 46.499 -17.585 14.468  1.00 21.54 ?  42  TYR   B HD2  1 
ATOM   4518 H HE1  . TYR   B 1 42  ? 47.312 -13.095 15.214  1.00 19.90 ?  42  TYR   B HE1  1 
ATOM   4519 H HE2  . TYR   B 1 42  ? 45.573 -16.535 16.303  1.00 22.01 ?  42  TYR   B HE2  1 
ATOM   4520 H HH   . TYR   B 1 42  ? 46.037 -13.271 17.039  1.00 25.77 ?  42  TYR   B HH   1 
ATOM   4521 N N    . LEU   B 1 43  ? 47.958 -16.712 8.856   1.00 11.74 ?  43  LEU   B N    1 
ATOM   4522 C CA   . LEU   B 1 43  ? 48.767 -16.636 7.645   1.00 11.72 ?  43  LEU   B CA   1 
ATOM   4523 C C    . LEU   B 1 43  ? 50.180 -17.144 7.900   1.00 12.03 ?  43  LEU   B C    1 
ATOM   4524 O O    . LEU   B 1 43  ? 51.161 -16.545 7.462   1.00 12.75 ?  43  LEU   B O    1 
ATOM   4525 C CB   . LEU   B 1 43  ? 48.779 -15.227 7.048   1.00 11.78 ?  43  LEU   B CB   1 
ATOM   4526 C CG   . LEU   B 1 43  ? 47.423 -14.623 6.665   1.00 12.01 ?  43  LEU   B CG   1 
ATOM   4527 C CD1  . LEU   B 1 43  ? 47.630 -13.220 6.098   1.00 13.26 ?  43  LEU   B CD1  1 
ATOM   4528 C CD2  . LEU   B 1 43  ? 46.682 -15.514 5.673   1.00 11.95 ?  43  LEU   B CD2  1 
ATOM   4529 H H    . LEU   B 1 43  ? 47.216 -17.131 8.743   1.00 14.11 ?  43  LEU   B H    1 
ATOM   4530 H HA   . LEU   B 1 43  ? 48.370 -17.222 6.979   1.00 14.08 ?  43  LEU   B HA   1 
ATOM   4531 H HB2  . LEU   B 1 43  ? 49.188 -14.629 7.692   1.00 14.16 ?  43  LEU   B HB2  1 
ATOM   4532 H HB3  . LEU   B 1 43  ? 49.319 -15.247 6.242   1.00 14.16 ?  43  LEU   B HB3  1 
ATOM   4533 H HG   . LEU   B 1 43  ? 46.878 -14.543 7.460   1.00 14.43 ?  43  LEU   B HG   1 
ATOM   4534 H HD11 . LEU   B 1 43  ? 46.770 -12.843 5.859   1.00 15.93 ?  43  LEU   B HD11 1 
ATOM   4535 H HD12 . LEU   B 1 43  ? 48.056 -12.666 6.775   1.00 15.93 ?  43  LEU   B HD12 1 
ATOM   4536 H HD13 . LEU   B 1 43  ? 48.199 -13.273 5.314   1.00 15.93 ?  43  LEU   B HD13 1 
ATOM   4537 H HD21 . LEU   B 1 43  ? 45.882 -15.055 5.367   1.00 14.35 ?  43  LEU   B HD21 1 
ATOM   4538 H HD22 . LEU   B 1 43  ? 47.261 -15.703 4.917   1.00 14.35 ?  43  LEU   B HD22 1 
ATOM   4539 H HD23 . LEU   B 1 43  ? 46.436 -16.344 6.114   1.00 14.35 ?  43  LEU   B HD23 1 
ATOM   4540 N N    . LYS   B 1 44  ? 50.282 -18.272 8.610   1.00 11.95 ?  44  LYS   B N    1 
ATOM   4541 C CA   . LYS   B 1 44  ? 51.552 -18.948 8.846   1.00 12.69 ?  44  LYS   B CA   1 
ATOM   4542 C C    . LYS   B 1 44  ? 51.669 -20.062 7.814   1.00 12.19 ?  44  LYS   B C    1 
ATOM   4543 O O    . LYS   B 1 44  ? 50.971 -21.080 7.895   1.00 13.30 ?  44  LYS   B O    1 
ATOM   4544 C CB   . LYS   B 1 44  ? 51.625 -19.470 10.280  1.00 14.32 ?  44  LYS   B CB   1 
ATOM   4545 C CG   . LYS   B 1 44  ? 51.813 -18.365 11.313  1.00 17.35 ?  44  LYS   B CG   1 
ATOM   4546 C CD   . LYS   B 1 44  ? 53.023 -17.499 10.946  1.00 20.25 ?  44  LYS   B CD   1 
ATOM   4547 C CE   . LYS   B 1 44  ? 53.451 -16.573 12.057  1.00 22.98 ?  44  LYS   B CE   1 
ATOM   4548 N NZ   . LYS   B 1 44  ? 54.669 -15.801 11.693  1.00 24.38 ?  44  LYS   B NZ   1 
ATOM   4549 H H    . LYS   B 1 44  ? 49.611 -18.661 8.977   1.00 14.35 ?  44  LYS   B H    1 
ATOM   4550 H HA   . LYS   B 1 44  ? 52.281 -18.327 8.683   1.00 15.24 ?  44  LYS   B HA   1 
ATOM   4551 H HB2  . LYS   B 1 44  ? 50.793 -19.928 10.485  1.00 17.20 ?  44  LYS   B HB2  1 
ATOM   4552 H HB3  . LYS   B 1 44  ? 52.368 -20.081 10.353  1.00 17.20 ?  44  LYS   B HB3  1 
ATOM   4553 H HG2  . LYS   B 1 44  ? 51.026 -17.805 11.340  1.00 20.83 ?  44  LYS   B HG2  1 
ATOM   4554 H HG3  . LYS   B 1 44  ? 51.977 -18.768 12.184  1.00 20.83 ?  44  LYS   B HG3  1 
ATOM   4555 H HD2  . LYS   B 1 44  ? 53.769 -18.084 10.718  1.00 24.31 ?  44  LYS   B HD2  1 
ATOM   4556 H HD3  . LYS   B 1 44  ? 52.791 -16.949 10.181  1.00 24.31 ?  44  LYS   B HD3  1 
ATOM   4557 H HE2  . LYS   B 1 44  ? 52.738 -15.944 12.228  1.00 27.59 ?  44  LYS   B HE2  1 
ATOM   4558 H HE3  . LYS   B 1 44  ? 53.645 -17.096 12.849  1.00 27.59 ?  44  LYS   B HE3  1 
ATOM   4559 H HZ1  . LYS   B 1 44  ? 54.898 -15.261 12.363  1.00 29.27 ?  44  LYS   B HZ1  1 
ATOM   4560 H HZ2  . LYS   B 1 44  ? 55.345 -16.353 11.522  1.00 29.27 ?  44  LYS   B HZ2  1 
ATOM   4561 H HZ3  . LYS   B 1 44  ? 54.512 -15.306 10.967  1.00 29.27 ?  44  LYS   B HZ3  1 
ATOM   4562 N N    . HIS   B 1 45  ? 52.524 -19.838 6.818   1.00 11.88 ?  45  HIS   B N    1 
ATOM   4563 C CA   . HIS   B 1 45  ? 52.551 -20.665 5.613   1.00 12.10 ?  45  HIS   B CA   1 
ATOM   4564 C C    . HIS   B 1 45  ? 53.568 -21.789 5.773   1.00 14.02 ?  45  HIS   B C    1 
ATOM   4565 O O    . HIS   B 1 45  ? 54.625 -21.805 5.151   1.00 16.38 ?  45  HIS   B O    1 
ATOM   4566 C CB   . HIS   B 1 45  ? 52.867 -19.806 4.402   1.00 12.15 ?  45  HIS   B CB   1 
ATOM   4567 C CG   . HIS   B 1 45  ? 51.992 -18.605 4.290   1.00 11.87 ?  45  HIS   B CG   1 
ATOM   4568 N ND1  . HIS   B 1 45  ? 50.615 -18.684 4.252   1.00 12.11 ?  45  HIS   B ND1  1 
ATOM   4569 C CD2  . HIS   B 1 45  ? 52.306 -17.292 4.226   1.00 12.93 ?  45  HIS   B CD2  1 
ATOM   4570 C CE1  . HIS   B 1 45  ? 50.124 -17.462 4.149   1.00 11.76 ?  45  HIS   B CE1  1 
ATOM   4571 N NE2  . HIS   B 1 45  ? 51.126 -16.599 4.130   1.00 12.28 ?  45  HIS   B NE2  1 
ATOM   4572 H H    . HIS   B 1 45  ? 53.101 -19.200 6.814   1.00 14.27 ?  45  HIS   B H    1 
ATOM   4573 H HA   . HIS   B 1 45  ? 51.674 -21.060 5.480   1.00 14.53 ?  45  HIS   B HA   1 
ATOM   4574 H HB2  . HIS   B 1 45  ? 53.786 -19.505 4.460   1.00 14.60 ?  45  HIS   B HB2  1 
ATOM   4575 H HB3  . HIS   B 1 45  ? 52.749 -20.344 3.598   1.00 14.60 ?  45  HIS   B HB3  1 
ATOM   4576 H HD2  . HIS   B 1 45  ? 53.162 -16.927 4.239   1.00 15.53 ?  45  HIS   B HD2  1 
ATOM   4577 H HE1  . HIS   B 1 45  ? 49.223 -17.247 4.085   1.00 14.13 ?  45  HIS   B HE1  1 
ATOM   4578 H HE2  . HIS   B 1 45  ? 51.050 -15.745 4.076   1.00 14.75 ?  45  HIS   B HE2  1 
ATOM   4579 N N    . GLY   B 1 46  ? 53.210 -22.753 6.615   1.00 15.09 ?  46  GLY   B N    1 
ATOM   4580 C CA   . GLY   B 1 46  ? 54.133 -23.813 6.969   1.00 16.55 ?  46  GLY   B CA   1 
ATOM   4581 C C    . GLY   B 1 46  ? 54.181 -25.000 6.029   1.00 18.10 ?  46  GLY   B C    1 
ATOM   4582 O O    . GLY   B 1 46  ? 55.253 -25.396 5.561   1.00 21.60 ?  46  GLY   B O    1 
ATOM   4583 H H    . GLY   B 1 46  ? 52.443 -22.796 7.014   1.00 18.12 ?  46  GLY   B H    1 
ATOM   4584 H HA2  . GLY   B 1 46  ? 55.026 -23.440 7.029   1.00 19.88 ?  46  GLY   B HA2  1 
ATOM   4585 H HA3  . GLY   B 1 46  ? 53.894 -24.154 7.846   1.00 19.88 ?  46  GLY   B HA3  1 
ATOM   4586 N N    . GLY   B 1 47  ? 53.025 -25.593 5.745   1.00 17.54 ?  47  GLY   B N    1 
ATOM   4587 C CA   . GLY   B 1 47  ? 52.972 -26.878 5.078   1.00 15.63 ?  47  GLY   B CA   1 
ATOM   4588 C C    . GLY   B 1 47  ? 52.048 -26.861 3.877   1.00 13.48 ?  47  GLY   B C    1 
ATOM   4589 O O    . GLY   B 1 47  ? 51.390 -25.861 3.590   1.00 13.46 ?  47  GLY   B O    1 
ATOM   4590 H H    . GLY   B 1 47  ? 52.254 -25.279 5.960   1.00 21.06 ?  47  GLY   B H    1 
ATOM   4591 H HA2  . GLY   B 1 47  ? 53.865 -27.127 4.781   1.00 18.77 ?  47  GLY   B HA2  1 
ATOM   4592 H HA3  . GLY   B 1 47  ? 52.663 -27.554 5.703   1.00 18.77 ?  47  GLY   B HA3  1 
ATOM   4593 N N    . GLY   B 1 48  ? 52.015 -27.998 3.182   1.00 12.78 ?  48  GLY   B N    1 
ATOM   4594 C CA   . GLY   B 1 48  ? 51.083 -28.145 2.080   1.00 12.59 ?  48  GLY   B CA   1 
ATOM   4595 C C    . GLY   B 1 48  ? 51.214 -27.034 1.063   1.00 12.01 ?  48  GLY   B C    1 
ATOM   4596 O O    . GLY   B 1 48  ? 52.315 -26.568 0.746   1.00 12.46 ?  48  GLY   B O    1 
ATOM   4597 H H    . GLY   B 1 48  ? 52.529 -28.672 3.320   1.00 15.35 ?  48  GLY   B H    1 
ATOM   4598 H HA2  . GLY   B 1 48  ? 51.242 -28.996 1.638   1.00 15.12 ?  48  GLY   B HA2  1 
ATOM   4599 H HA3  . GLY   B 1 48  ? 50.178 -28.144 2.425   1.00 15.12 ?  48  GLY   B HA3  1 
ATOM   4600 N N    . VAL   B 1 49  ? 50.066 -26.611 0.533   1.00 11.97 ?  49  VAL   B N    1 
ATOM   4601 C CA   . VAL   B 1 49  ? 50.046 -25.589 -0.509  1.00 11.94 ?  49  VAL   B CA   1 
ATOM   4602 C C    . VAL   B 1 49  ? 50.703 -24.302 -0.023  1.00 11.11 ?  49  VAL   B C    1 
ATOM   4603 O O    . VAL   B 1 49  ? 51.491 -23.683 -0.747  1.00 11.75 ?  49  VAL   B O    1 
ATOM   4604 C CB   . VAL   B 1 49  ? 48.602 -25.339 -0.986  1.00 13.35 ?  49  VAL   B CB   1 
ATOM   4605 C CG1  . VAL   B 1 49  ? 48.524 -24.086 -1.854  1.00 13.42 ?  49  VAL   B CG1  1 
ATOM   4606 C CG2  . VAL   B 1 49  ? 48.065 -26.552 -1.740  1.00 14.95 ?  49  VAL   B CG2  1 
ATOM   4607 H H    . VAL   B 1 49  ? 49.283 -26.900 0.756   1.00 14.38 ?  49  VAL   B H    1 
ATOM   4608 H HA   . VAL   B 1 49  ? 50.550 -25.906 -1.270  1.00 14.34 ?  49  VAL   B HA   1 
ATOM   4609 H HB   . VAL   B 1 49  ? 48.032 -25.197 -0.217  1.00 16.04 ?  49  VAL   B HB   1 
ATOM   4610 H HG11 . VAL   B 1 49  ? 47.696 -24.100 -2.362  1.00 16.12 ?  49  VAL   B HG11 1 
ATOM   4611 H HG12 . VAL   B 1 49  ? 48.544 -23.300 -1.284  1.00 16.12 ?  49  VAL   B HG12 1 
ATOM   4612 H HG13 . VAL   B 1 49  ? 49.280 -24.072 -2.463  1.00 16.12 ?  49  VAL   B HG13 1 
ATOM   4613 H HG21 . VAL   B 1 49  ? 47.158 -26.372 -2.031  1.00 17.95 ?  49  VAL   B HG21 1 
ATOM   4614 H HG22 . VAL   B 1 49  ? 48.631 -26.721 -2.512  1.00 17.95 ?  49  VAL   B HG22 1 
ATOM   4615 H HG23 . VAL   B 1 49  ? 48.078 -27.320 -1.149  1.00 17.95 ?  49  VAL   B HG23 1 
ATOM   4616 N N    . ALA   B 1 50  ? 50.363 -23.858 1.188   1.00 11.06 ?  50  ALA   B N    1 
ATOM   4617 C CA   . ALA   B 1 50  ? 50.881 -22.581 1.666   1.00 11.05 ?  50  ALA   B CA   1 
ATOM   4618 C C    . ALA   B 1 50  ? 52.400 -22.605 1.768   1.00 11.26 ?  50  ALA   B C    1 
ATOM   4619 O O    . ALA   B 1 50  ? 53.076 -21.635 1.398   1.00 11.19 ?  50  ALA   B O    1 
ATOM   4620 C CB   . ALA   B 1 50  ? 50.250 -22.223 3.010   1.00 11.43 ?  50  ALA   B CB   1 
ATOM   4621 H H    . ALA   B 1 50  ? 49.847 -24.269 1.742   1.00 13.28 ?  50  ALA   B H    1 
ATOM   4622 H HA   . ALA   B 1 50  ? 50.645 -21.888 1.036   1.00 13.27 ?  50  ALA   B HA   1 
ATOM   4623 H HB1  . ALA   B 1 50  ? 50.604 -21.370 3.313   1.00 13.73 ?  50  ALA   B HB1  1 
ATOM   4624 H HB2  . ALA   B 1 50  ? 49.286 -22.154 2.899   1.00 13.73 ?  50  ALA   B HB2  1 
ATOM   4625 H HB3  . ALA   B 1 50  ? 50.457 -22.914 3.658   1.00 13.73 ?  50  ALA   B HB3  1 
ATOM   4626 N N    . GLY   B 1 51  ? 52.953 -23.695 2.290   1.00 11.64 ?  51  GLY   B N    1 
ATOM   4627 C CA   . GLY   B 1 51  ? 54.397 -23.800 2.358   1.00 12.32 ?  51  GLY   B CA   1 
ATOM   4628 C C    . GLY   B 1 51  ? 55.041 -23.744 0.989   1.00 12.25 ?  51  GLY   B C    1 
ATOM   4629 O O    . GLY   B 1 51  ? 56.082 -23.108 0.806   1.00 13.13 ?  51  GLY   B O    1 
ATOM   4630 H H    . GLY   B 1 51  ? 52.528 -24.373 2.604   1.00 13.98 ?  51  GLY   B H    1 
ATOM   4631 H HA2  . GLY   B 1 51  ? 54.754 -23.072 2.894   1.00 14.80 ?  51  GLY   B HA2  1 
ATOM   4632 H HA3  . GLY   B 1 51  ? 54.646 -24.639 2.781   1.00 14.80 ?  51  GLY   B HA3  1 
ATOM   4633 N N    . ALA   B 1 52  ? 54.433 -24.406 0.007   1.00 11.87 ?  52  ALA   B N    1 
ATOM   4634 C CA   . ALA   B 1 52  ? 54.990 -24.420 -1.339  1.00 12.23 ?  52  ALA   B CA   1 
ATOM   4635 C C    . ALA   B 1 52  ? 54.916 -23.045 -1.991  1.00 11.69 ?  52  ALA   B C    1 
ATOM   4636 O O    . ALA   B 1 52  ? 55.887 -22.593 -2.617  1.00 12.33 ?  52  ALA   B O    1 
ATOM   4637 C CB   . ALA   B 1 52  ? 54.278 -25.461 -2.195  1.00 13.14 ?  52  ALA   B CB   1 
ATOM   4638 H H    . ALA   B 1 52  ? 53.696 -24.845 0.094   1.00 14.26 ?  52  ALA   B H    1 
ATOM   4639 H HA   . ALA   B 1 52  ? 55.924 -24.669 -1.283  1.00 14.69 ?  52  ALA   B HA   1 
ATOM   4640 H HB1  . ALA   B 1 52  ? 54.665 -25.452 -3.085  1.00 15.78 ?  52  ALA   B HB1  1 
ATOM   4641 H HB2  . ALA   B 1 52  ? 54.393 -26.333 -1.790  1.00 15.78 ?  52  ALA   B HB2  1 
ATOM   4642 H HB3  . ALA   B 1 52  ? 53.335 -25.238 -2.242  1.00 15.78 ?  52  ALA   B HB3  1 
ATOM   4643 N N    . LEU   B 1 53  ? 53.768 -22.371 -1.876  1.00 11.24 ?  53  LEU   B N    1 
ATOM   4644 C CA   . LEU   B 1 53  ? 53.657 -21.028 -2.438  1.00 11.66 ?  53  LEU   B CA   1 
ATOM   4645 C C    . LEU   B 1 53  ? 54.664 -20.088 -1.789  1.00 11.51 ?  53  LEU   B C    1 
ATOM   4646 O O    . LEU   B 1 53  ? 55.368 -19.338 -2.476  1.00 12.08 ?  53  LEU   B O    1 
ATOM   4647 C CB   . LEU   B 1 53  ? 52.233 -20.485 -2.266  1.00 11.98 ?  53  LEU   B CB   1 
ATOM   4648 C CG   . LEU   B 1 53  ? 51.108 -21.212 -3.005  1.00 11.99 ?  53  LEU   B CG   1 
ATOM   4649 C CD1  . LEU   B 1 53  ? 49.760 -20.623 -2.633  1.00 13.86 ?  53  LEU   B CD1  1 
ATOM   4650 C CD2  . LEU   B 1 53  ? 51.310 -21.169 -4.514  1.00 14.13 ?  53  LEU   B CD2  1 
ATOM   4651 H H    . LEU   B 1 53  ? 53.061 -22.657 -1.482  1.00 13.51 ?  53  LEU   B H    1 
ATOM   4652 H HA   . LEU   B 1 53  ? 53.852 -21.064 -3.390  1.00 14.01 ?  53  LEU   B HA   1 
ATOM   4653 H HB2  . LEU   B 1 53  ? 52.015 -20.513 -1.322  1.00 14.39 ?  53  LEU   B HB2  1 
ATOM   4654 H HB3  . LEU   B 1 53  ? 52.221 -19.567 -2.570  1.00 14.39 ?  53  LEU   B HB3  1 
ATOM   4655 H HG   . LEU   B 1 53  ? 51.103 -22.144 -2.732  1.00 14.40 ?  53  LEU   B HG   1 
ATOM   4656 H HD11 . LEU   B 1 53  ? 49.061 -21.103 -3.108  1.00 16.65 ?  53  LEU   B HD11 1 
ATOM   4657 H HD12 . LEU   B 1 53  ? 49.626 -20.717 -1.674  1.00 16.65 ?  53  LEU   B HD12 1 
ATOM   4658 H HD13 . LEU   B 1 53  ? 49.743 -19.687 -2.878  1.00 16.65 ?  53  LEU   B HD13 1 
ATOM   4659 H HD21 . LEU   B 1 53  ? 50.588 -21.656 -4.943  1.00 16.97 ?  53  LEU   B HD21 1 
ATOM   4660 H HD22 . LEU   B 1 53  ? 51.301 -20.245 -4.805  1.00 16.97 ?  53  LEU   B HD22 1 
ATOM   4661 H HD23 . LEU   B 1 53  ? 52.159 -21.580 -4.732  1.00 16.97 ?  53  LEU   B HD23 1 
ATOM   4662 N N    . ASN   B 1 54  ? 54.750 -20.115 -0.459  1.00 11.17 ?  54  ASN   B N    1 
ATOM   4663 C CA   . ASN   B 1 54  ? 55.664 -19.208 0.216   1.00 11.99 ?  54  ASN   B CA   1 
ATOM   4664 C C    . ASN   B 1 54  ? 57.106 -19.482 -0.181  1.00 12.09 ?  54  ASN   B C    1 
ATOM   4665 O O    . ASN   B 1 54  ? 57.879 -18.542 -0.412  1.00 12.71 ?  54  ASN   B O    1 
ATOM   4666 C CB   . ASN   B 1 54  ? 55.502 -19.291 1.726   1.00 12.66 ?  54  ASN   B CB   1 
ATOM   4667 C CG   . ASN   B 1 54  ? 56.475 -18.376 2.444   1.00 12.52 ?  54  ASN   B CG   1 
ATOM   4668 O OD1  . ASN   B 1 54  ? 56.498 -17.166 2.198   1.00 12.84 ?  54  ASN   B OD1  1 
ATOM   4669 N ND2  . ASN   B 1 54  ? 57.306 -18.945 3.303   1.00 14.07 ?  54  ASN   B ND2  1 
ATOM   4670 H H    . ASN   B 1 54  ? 54.297 -20.638 0.056   1.00 13.42 ?  54  ASN   B H    1 
ATOM   4671 H HA   . ASN   B 1 54  ? 55.449 -18.303 -0.053  1.00 14.40 ?  54  ASN   B HA   1 
ATOM   4672 H HB2  . ASN   B 1 54  ? 54.595 -19.021 1.965   1.00 15.20 ?  54  ASN   B HB2  1 
ATOM   4673 H HB3  . ASN   B 1 54  ? 55.663 -20.200 2.018   1.00 15.20 ?  54  ASN   B HB3  1 
ATOM   4674 H HD21 . ASN   B 1 54  ? 57.876 -18.464 3.733   1.00 16.90 ?  54  ASN   B HD21 1 
ATOM   4675 H HD22 . ASN   B 1 54  ? 57.268 -19.793 3.445   1.00 16.90 ?  54  ASN   B HD22 1 
ATOM   4676 N N    . LYS   B 1 55  ? 57.494 -20.757 -0.255  1.00 12.60 ?  55  LYS   B N    1 
ATOM   4677 C CA   . LYS   B 1 55  ? 58.851 -21.089 -0.672  1.00 13.68 ?  55  LYS   B CA   1 
ATOM   4678 C C    . LYS   B 1 55  ? 59.147 -20.548 -2.066  1.00 13.35 ?  55  LYS   B C    1 
ATOM   4679 O O    . LYS   B 1 55  ? 60.246 -20.045 -2.321  1.00 13.76 ?  55  LYS   B O    1 
ATOM   4680 C CB   . LYS   B 1 55  ? 59.053 -22.602 -0.622  1.00 15.04 ?  55  LYS   B CB   1 
ATOM   4681 C CG   . LYS   B 1 55  ? 60.440 -23.057 -1.033  1.00 18.83 ?  55  LYS   B CG   1 
ATOM   4682 C CD   . LYS   B 1 55  ? 60.602 -24.559 -0.888  1.00 22.25 ?  55  LYS   B CD   1 
ATOM   4683 C CE   . LYS   B 1 55  ? 60.545 -24.995 0.571   1.00 25.69 ?  55  LYS   B CE   1 
ATOM   4684 N NZ   . LYS   B 1 55  ? 60.991 -26.397 0.749   1.00 27.37 ?  55  LYS   B NZ   1 
ATOM   4685 H H    . LYS   B 1 55  ? 56.993 -21.435 -0.074  1.00 15.13 ?  55  LYS   B H    1 
ATOM   4686 H HA   . LYS   B 1 55  ? 59.476 -20.682 -0.055  1.00 16.43 ?  55  LYS   B HA   1 
ATOM   4687 H HB2  . LYS   B 1 55  ? 58.897 -22.901 0.288   1.00 18.06 ?  55  LYS   B HB2  1 
ATOM   4688 H HB3  . LYS   B 1 55  ? 58.416 -23.024 -1.218  1.00 18.06 ?  55  LYS   B HB3  1 
ATOM   4689 H HG2  . LYS   B 1 55  ? 60.593 -22.826 -1.963  1.00 22.61 ?  55  LYS   B HG2  1 
ATOM   4690 H HG3  . LYS   B 1 55  ? 61.100 -22.623 -0.468  1.00 22.61 ?  55  LYS   B HG3  1 
ATOM   4691 H HD2  . LYS   B 1 55  ? 59.887 -25.008 -1.366  1.00 26.71 ?  55  LYS   B HD2  1 
ATOM   4692 H HD3  . LYS   B 1 55  ? 61.464 -24.827 -1.247  1.00 26.71 ?  55  LYS   B HD3  1 
ATOM   4693 H HE2  . LYS   B 1 55  ? 61.123 -24.415 1.096   1.00 30.85 ?  55  LYS   B HE2  1 
ATOM   4694 H HE3  . LYS   B 1 55  ? 59.628 -24.920 0.886   1.00 30.85 ?  55  LYS   B HE3  1 
ATOM   4695 H HZ1  . LYS   B 1 55  ? 60.902 -26.634 1.602   1.00 32.85 ?  55  LYS   B HZ1  1 
ATOM   4696 H HZ2  . LYS   B 1 55  ? 60.494 -26.935 0.244   1.00 32.85 ?  55  LYS   B HZ2  1 
ATOM   4697 H HZ3  . LYS   B 1 55  ? 61.841 -26.475 0.510   1.00 32.85 ?  55  LYS   B HZ3  1 
ATOM   4698 N N    . ALA   B 1 56  ? 58.179 -20.639 -2.982  1.00 13.08 ?  56  ALA   B N    1 
ATOM   4699 C CA   . ALA   B 1 56  ? 58.393 -20.132 -4.332  1.00 13.72 ?  56  ALA   B CA   1 
ATOM   4700 C C    . ALA   B 1 56  ? 58.662 -18.634 -4.330  1.00 13.43 ?  56  ALA   B C    1 
ATOM   4701 O O    . ALA   B 1 56  ? 59.383 -18.131 -5.204  1.00 14.62 ?  56  ALA   B O    1 
ATOM   4702 C CB   . ALA   B 1 56  ? 57.196 -20.459 -5.222  1.00 14.70 ?  56  ALA   B CB   1 
ATOM   4703 H H    . ALA   B 1 56  ? 57.398 -20.980 -2.846  1.00 15.71 ?  56  ALA   B H    1 
ATOM   4704 H HA   . ALA   B 1 56  ? 59.174 -20.564 -4.704  1.00 16.47 ?  56  ALA   B HA   1 
ATOM   4705 H HB1  . ALA   B 1 56  ? 57.369 -20.116 -6.116  1.00 17.66 ?  56  ALA   B HB1  1 
ATOM   4706 H HB2  . ALA   B 1 56  ? 57.087 -21.421 -5.254  1.00 17.66 ?  56  ALA   B HB2  1 
ATOM   4707 H HB3  . ALA   B 1 56  ? 56.405 -20.043 -4.855  1.00 17.66 ?  56  ALA   B HB3  1 
ATOM   4708 N N    . THR   B 1 57  ? 58.101 -17.906 -3.362  1.00 13.34 ?  57  THR   B N    1 
ATOM   4709 C CA   . THR   B 1 57  ? 58.332 -16.470 -3.235  1.00 13.37 ?  57  THR   B CA   1 
ATOM   4710 C C    . THR   B 1 57  ? 59.583 -16.143 -2.427  1.00 14.11 ?  57  THR   B C    1 
ATOM   4711 O O    . THR   B 1 57  ? 59.817 -14.965 -2.121  1.00 14.66 ?  57  THR   B O    1 
ATOM   4712 C CB   . THR   B 1 57  ? 57.132 -15.747 -2.597  1.00 12.61 ?  57  THR   B CB   1 
ATOM   4713 O OG1  . THR   B 1 57  ? 57.112 -15.961 -1.179  1.00 12.91 ?  57  THR   B OG1  1 
ATOM   4714 C CG2  . THR   B 1 57  ? 55.809 -16.158 -3.228  1.00 12.70 ?  57  THR   B CG2  1 
ATOM   4715 H H    . THR   B 1 57  ? 57.561 -18.220 -2.767  1.00 16.02 ?  57  THR   B H    1 
ATOM   4716 H HA   . THR   B 1 57  ? 58.450 -16.101 -4.124  1.00 16.06 ?  57  THR   B HA   1 
ATOM   4717 H HB   . THR   B 1 57  ? 57.235 -14.797 -2.756  1.00 15.15 ?  57  THR   B HB   1 
ATOM   4718 H HG1  . THR   B 1 57  ? 57.048 -16.784 -1.014  1.00 15.51 ?  57  THR   B HG1  1 
ATOM   4719 H HG21 . THR   B 1 57  ? 55.080 -15.647 -2.843  1.00 15.25 ?  57  THR   B HG21 1 
ATOM   4720 H HG22 . THR   B 1 57  ? 55.830 -16.005 -4.186  1.00 15.25 ?  57  THR   B HG22 1 
ATOM   4721 H HG23 . THR   B 1 57  ? 55.641 -17.104 -3.071  1.00 15.25 ?  57  THR   B HG23 1 
ATOM   4722 N N    . ASN   B 1 58  ? 60.382 -17.148 -2.068  1.00 14.85 ?  58  ASN   B N    1 
ATOM   4723 C CA   . ASN   B 1 58  ? 61.581 -16.926 -1.265  1.00 18.43 ?  58  ASN   B CA   1 
ATOM   4724 C C    . ASN   B 1 58  ? 61.242 -16.215 0.045   1.00 15.83 ?  58  ASN   B C    1 
ATOM   4725 O O    . ASN   B 1 58  ? 61.977 -15.340 0.511   1.00 16.32 ?  58  ASN   B O    1 
ATOM   4726 C CB   . ASN   B 1 58  ? 62.658 -16.171 -2.051  1.00 28.59 ?  58  ASN   B CB   1 
ATOM   4727 C CG   . ASN   B 1 58  ? 64.025 -16.259 -1.399  1.00 38.59 ?  58  ASN   B CG   1 
ATOM   4728 O OD1  . ASN   B 1 58  ? 64.341 -17.237 -0.722  1.00 42.27 ?  58  ASN   B OD1  1 
ATOM   4729 N ND2  . ASN   B 1 58  ? 64.844 -15.230 -1.600  1.00 43.01 ?  58  ASN   B ND2  1 
ATOM   4730 H H    . ASN   B 1 58  ? 60.253 -17.975 -2.276  1.00 17.84 ?  58  ASN   B H    1 
ATOM   4731 H HA   . ASN   B 1 58  ? 61.954 -17.792 -1.037  1.00 22.13 ?  58  ASN   B HA   1 
ATOM   4732 H HB2  . ASN   B 1 58  ? 62.728 -16.551 -2.943  1.00 34.33 ?  58  ASN   B HB2  1 
ATOM   4733 H HB3  . ASN   B 1 58  ? 62.416 -15.235 -2.108  1.00 34.33 ?  58  ASN   B HB3  1 
ATOM   4734 H HD21 . ASN   B 1 58  ? 65.632 -15.231 -1.253  1.00 51.63 ?  58  ASN   B HD21 1 
ATOM   4735 H HD22 . ASN   B 1 58  ? 64.587 -14.563 -2.077  1.00 51.63 ?  58  ASN   B HD22 1 
ATOM   4736 N N    . ASN   B 1 59  ? 60.119 -16.604 0.649   1.00 14.48 ?  59  ASN   B N    1 
ATOM   4737 C CA   . ASN   B 1 59  ? 59.642 -16.136 1.952   1.00 14.43 ?  59  ASN   B CA   1 
ATOM   4738 C C    . ASN   B 1 59  ? 59.049 -14.729 1.901   1.00 13.99 ?  59  ASN   B C    1 
ATOM   4739 O O    . ASN   B 1 59  ? 58.610 -14.233 2.946   1.00 14.12 ?  59  ASN   B O    1 
ATOM   4740 C CB   . ASN   B 1 59  ? 60.712 -16.196 3.058   1.00 15.63 ?  59  ASN   B CB   1 
ATOM   4741 C CG   . ASN   B 1 59  ? 60.119 -16.385 4.437   1.00 17.11 ?  59  ASN   B CG   1 
ATOM   4742 O OD1  . ASN   B 1 59  ? 59.295 -17.278 4.654   1.00 16.97 ?  59  ASN   B OD1  1 
ATOM   4743 N ND2  . ASN   B 1 59  ? 60.526 -15.538 5.380   1.00 17.98 ?  59  ASN   B ND2  1 
ATOM   4744 H H    . ASN   B 1 59  ? 59.582 -17.180 0.301   1.00 17.40 ?  59  ASN   B H    1 
ATOM   4745 H HA   . ASN   B 1 59  ? 58.934 -16.732 2.232   1.00 17.33 ?  59  ASN   B HA   1 
ATOM   4746 H HB2  . ASN   B 1 59  ? 61.306 -16.945 2.894   1.00 18.78 ?  59  ASN   B HB2  1 
ATOM   4747 H HB3  . ASN   B 1 59  ? 61.215 -15.368 3.069   1.00 18.78 ?  59  ASN   B HB3  1 
ATOM   4748 H HD21 . ASN   B 1 59  ? 60.212 -15.598 6.183   1.00 21.59 ?  59  ASN   B HD21 1 
ATOM   4749 H HD22 . ASN   B 1 59  ? 61.097 -14.925 5.191   1.00 21.59 ?  59  ASN   B HD22 1 
ATOM   4750 N N    . ALA   B 1 60  ? 58.987 -14.081 0.733   1.00 13.76 ?  60  ALA   B N    1 
ATOM   4751 C CA   . ALA   B 1 60  ? 58.386 -12.751 0.664   1.00 13.62 ?  60  ALA   B CA   1 
ATOM   4752 C C    . ALA   B 1 60  ? 56.914 -12.780 1.063   1.00 12.98 ?  60  ALA   B C    1 
ATOM   4753 O O    . ALA   B 1 60  ? 56.405 -11.829 1.675   1.00 13.21 ?  60  ALA   B O    1 
ATOM   4754 C CB   . ALA   B 1 60  ? 58.555 -12.171 -0.740  1.00 14.60 ?  60  ALA   B CB   1 
ATOM   4755 H H    . ALA   B 1 60  ? 59.284 -14.389 -0.012  1.00 16.53 ?  60  ALA   B H    1 
ATOM   4756 H HA   . ALA   B 1 60  ? 58.847 -12.171 1.286   1.00 16.36 ?  60  ALA   B HA   1 
ATOM   4757 H HB1  . ALA   B 1 60  ? 58.154 -11.292 -0.767  1.00 17.54 ?  60  ALA   B HB1  1 
ATOM   4758 H HB2  . ALA   B 1 60  ? 59.505 -12.110 -0.942  1.00 17.54 ?  60  ALA   B HB2  1 
ATOM   4759 H HB3  . ALA   B 1 60  ? 58.121 -12.757 -1.380  1.00 17.54 ?  60  ALA   B HB3  1 
ATOM   4760 N N    . MET   B 1 61  ? 56.210 -13.856 0.711   1.00 12.42 ?  61  MET   B N    1 
ATOM   4761 C CA   . MET   B 1 61  ? 54.816 -13.984 1.113   1.00 12.19 ?  61  MET   B CA   1 
ATOM   4762 C C    . MET   B 1 61  ? 54.684 -13.993 2.637   1.00 12.26 ?  61  MET   B C    1 
ATOM   4763 O O    . MET   B 1 61  ? 53.784 -13.349 3.193   1.00 12.16 ?  61  MET   B O    1 
ATOM   4764 C CB   . MET   B 1 61  ? 54.233 -15.253 0.485   1.00 12.24 ?  61  MET   B CB   1 
ATOM   4765 C CG   . MET   B 1 61  ? 52.797 -15.546 0.904   1.00 12.13 ?  61  MET   B CG   1 
ATOM   4766 S SD   . MET   B 1 61  ? 52.157 -17.053 0.152   1.00 12.55 ?  61  MET   B SD   1 
ATOM   4767 C CE   . MET   B 1 61  ? 51.903 -16.491 -1.531  1.00 13.94 ?  61  MET   B CE   1 
ATOM   4768 H H    . MET   B 1 61  ? 56.512 -14.521 0.248   1.00 14.92 ?  61  MET   B H    1 
ATOM   4769 H HA   . MET   B 1 61  ? 54.318 -13.232 0.755   1.00 14.64 ?  61  MET   B HA   1 
ATOM   4770 H HB2  . MET   B 1 61  ? 54.243 -15.161 -0.484  1.00 14.71 ?  61  MET   B HB2  1 
ATOM   4771 H HB3  . MET   B 1 61  ? 54.777 -16.012 0.743   1.00 14.71 ?  61  MET   B HB3  1 
ATOM   4772 H HG2  . MET   B 1 61  ? 52.756 -15.663 1.866   1.00 14.58 ?  61  MET   B HG2  1 
ATOM   4773 H HG3  . MET   B 1 61  ? 52.225 -14.810 0.634   1.00 14.58 ?  61  MET   B HG3  1 
ATOM   4774 H HE1  . MET   B 1 61  ? 51.523 -17.220 -2.051  1.00 16.75 ?  61  MET   B HE1  1 
ATOM   4775 H HE2  . MET   B 1 61  ? 51.294 -15.738 -1.527  1.00 16.75 ?  61  MET   B HE2  1 
ATOM   4776 H HE3  . MET   B 1 61  ? 52.756 -16.228 -1.910  1.00 16.75 ?  61  MET   B HE3  1 
ATOM   4777 N N    . GLN   B 1 62  ? 55.567 -14.714 3.334   1.00 12.17 ?  62  GLN   B N    1 
ATOM   4778 C CA   . GLN   B 1 62  ? 55.462 -14.777 4.789   1.00 12.56 ?  62  GLN   B CA   1 
ATOM   4779 C C    . GLN   B 1 62  ? 55.745 -13.424 5.428   1.00 12.97 ?  62  GLN   B C    1 
ATOM   4780 O O    . GLN   B 1 62  ? 55.065 -13.032 6.381   1.00 13.13 ?  62  GLN   B O    1 
ATOM   4781 C CB   . GLN   B 1 62  ? 56.412 -15.834 5.349   1.00 12.72 ?  62  GLN   B CB   1 
ATOM   4782 C CG   . GLN   B 1 62  ? 56.192 -16.097 6.831   1.00 12.99 ?  62  GLN   B CG   1 
ATOM   4783 C CD   . GLN   B 1 62  ? 54.823 -16.691 7.083   1.00 12.39 ?  62  GLN   B CD   1 
ATOM   4784 O OE1  . GLN   B 1 62  ? 54.570 -17.846 6.739   1.00 13.02 ?  62  GLN   B OE1  1 
ATOM   4785 N NE2  . GLN   B 1 62  ? 53.916 -15.899 7.641   1.00 12.82 ?  62  GLN   B NE2  1 
ATOM   4786 H H    . GLN   B 1 62  ? 56.216 -15.164 2.991   1.00 14.62 ?  62  GLN   B H    1 
ATOM   4787 H HA   . GLN   B 1 62  ? 54.555 -15.033 5.018   1.00 15.08 ?  62  GLN   B HA   1 
ATOM   4788 H HB2  . GLN   B 1 62  ? 56.277 -16.669 4.873   1.00 15.28 ?  62  GLN   B HB2  1 
ATOM   4789 H HB3  . GLN   B 1 62  ? 57.328 -15.531 5.228   1.00 15.28 ?  62  GLN   B HB3  1 
ATOM   4790 H HG2  . GLN   B 1 62  ? 56.862 -16.724 7.143   1.00 15.61 ?  62  GLN   B HG2  1 
ATOM   4791 H HG3  . GLN   B 1 62  ? 56.263 -15.261 7.319   1.00 15.61 ?  62  GLN   B HG3  1 
ATOM   4792 H HE21 . GLN   B 1 62  ? 54.128 -15.092 7.860   1.00 15.39 ?  62  GLN   B HE21 1 
ATOM   4793 H HE22 . GLN   B 1 62  ? 53.128 -16.194 7.800   1.00 15.39 ?  62  GLN   B HE22 1 
ATOM   4794 N N    . VAL   B 1 63  ? 56.756 -12.708 4.939   1.00 13.39 ?  63  VAL   B N    1 
ATOM   4795 C CA   . VAL   B 1 63  ? 57.056 -11.394 5.502   1.00 14.11 ?  63  VAL   B CA   1 
ATOM   4796 C C    . VAL   B 1 63  ? 55.864 -10.462 5.323   1.00 13.32 ?  63  VAL   B C    1 
ATOM   4797 O O    . VAL   B 1 63  ? 55.457 -9.751  6.252   1.00 14.18 ?  63  VAL   B O    1 
ATOM   4798 C CB   . VAL   B 1 63  ? 58.347 -10.831 4.884   1.00 15.49 ?  63  VAL   B CB   1 
ATOM   4799 C CG1  . VAL   B 1 63  ? 58.582 -9.398  5.340   1.00 16.18 ?  63  VAL   B CG1  1 
ATOM   4800 C CG2  . VAL   B 1 63  ? 59.528 -11.702 5.276   1.00 16.21 ?  63  VAL   B CG2  1 
ATOM   4801 H H    . VAL   B 1 63  ? 57.271 -12.955 4.294   1.00 16.09 ?  63  VAL   B H    1 
ATOM   4802 H HA   . VAL   B 1 63  ? 57.211 -11.497 6.452   1.00 16.95 ?  63  VAL   B HA   1 
ATOM   4803 H HB   . VAL   B 1 63  ? 58.280 -10.838 3.918   1.00 18.60 ?  63  VAL   B HB   1 
ATOM   4804 H HG11 . VAL   B 1 63  ? 59.499 -9.147  5.139   1.00 19.44 ?  63  VAL   B HG11 1 
ATOM   4805 H HG12 . VAL   B 1 63  ? 57.970 -8.812  4.873   1.00 19.44 ?  63  VAL   B HG12 1 
ATOM   4806 H HG13 . VAL   B 1 63  ? 58.432 -9.343  6.298   1.00 19.44 ?  63  VAL   B HG13 1 
ATOM   4807 H HG21 . VAL   B 1 63  ? 60.343 -11.325 4.901   1.00 19.47 ?  63  VAL   B HG21 1 
ATOM   4808 H HG22 . VAL   B 1 63  ? 59.598 -11.725 6.247   1.00 19.47 ?  63  VAL   B HG22 1 
ATOM   4809 H HG23 . VAL   B 1 63  ? 59.394 -12.598 4.935   1.00 19.47 ?  63  VAL   B HG23 1 
ATOM   4810 N N    . GLU   B 1 64  ? 55.290 -10.451 4.120   1.00 12.99 ?  64  GLU   B N    1 
ATOM   4811 C CA   . GLU   B 1 64  ? 54.127 -9.609  3.850   1.00 12.65 ?  64  GLU   B CA   1 
ATOM   4812 C C    . GLU   B 1 64  ? 52.946 -10.010 4.728   1.00 12.33 ?  64  GLU   B C    1 
ATOM   4813 O O    . GLU   B 1 64  ? 52.209 -9.150  5.240   1.00 13.01 ?  64  GLU   B O    1 
ATOM   4814 C CB   . GLU   B 1 64  ? 53.764 -9.758  2.373   1.00 13.00 ?  64  GLU   B CB   1 
ATOM   4815 C CG   . GLU   B 1 64  ? 52.523 -9.002  1.935   1.00 13.38 ?  64  GLU   B CG   1 
ATOM   4816 C CD   . GLU   B 1 64  ? 51.963 -9.504  0.611   1.00 14.06 ?  64  GLU   B CD   1 
ATOM   4817 O OE1  . GLU   B 1 64  ? 52.149 -10.708 0.282   1.00 14.99 ?  64  GLU   B OE1  1 
ATOM   4818 O OE2  . GLU   B 1 64  ? 51.329 -8.685  -0.098  1.00 14.86 -1 64  GLU   B OE2  1 
ATOM   4819 H H    . GLU   B 1 64  ? 55.557 -10.920 3.445   1.00 15.61 ?  64  GLU   B H    1 
ATOM   4820 H HA   . GLU   B 1 64  ? 54.349 -8.683  4.024   1.00 15.19 ?  64  GLU   B HA   1 
ATOM   4821 H HB2  . GLU   B 1 64  ? 54.507 -9.426  1.835   1.00 15.61 ?  64  GLU   B HB2  1 
ATOM   4822 H HB3  . GLU   B 1 64  ? 53.622 -10.695 2.182   1.00 15.61 ?  64  GLU   B HB3  1 
ATOM   4823 H HG2  . GLU   B 1 64  ? 51.827 -9.104  2.601   1.00 16.07 ?  64  GLU   B HG2  1 
ATOM   4824 H HG3  . GLU   B 1 64  ? 52.746 -8.065  1.828   1.00 16.07 ?  64  GLU   B HG3  1 
ATOM   4825 N N    . SER   B 1 65  ? 52.756 -11.317 4.906   1.00 12.02 ?  65  SER   B N    1 
ATOM   4826 C CA   . SER   B 1 65  ? 51.655 -11.828 5.710   1.00 12.20 ?  65  SER   B CA   1 
ATOM   4827 C C    . SER   B 1 65  ? 51.798 -11.432 7.173   1.00 12.19 ?  65  SER   B C    1 
ATOM   4828 O O    . SER   B 1 65  ? 50.806 -11.060 7.816   1.00 12.63 ?  65  SER   B O    1 
ATOM   4829 C CB   . SER   B 1 65  ? 51.585 -13.349 5.576   1.00 12.70 ?  65  SER   B CB   1 
ATOM   4830 O OG   . SER   B 1 65  ? 51.225 -13.740 4.259   1.00 12.56 ?  65  SER   B OG   1 
ATOM   4831 H H    . SER   B 1 65  ? 53.259 -11.936 4.572   1.00 14.44 ?  65  SER   B H    1 
ATOM   4832 H HA   . SER   B 1 65  ? 50.821 -11.460 5.377   1.00 14.65 ?  65  SER   B HA   1 
ATOM   4833 H HB2  . SER   B 1 65  ? 52.451 -13.725 5.787   1.00 15.25 ?  65  SER   B HB2  1 
ATOM   4834 H HB3  . SER   B 1 65  ? 50.917 -13.688 6.193   1.00 15.25 ?  65  SER   B HB3  1 
ATOM   4835 H HG   . SER   B 1 65  ? 51.796 -13.451 3.706   1.00 15.09 ?  65  SER   B HG   1 
ATOM   4836 N N    . ASP   B 1 66  ? 53.011 -11.530 7.726   1.00 12.68 ?  66  ASP   B N    1 
ATOM   4837 C CA   . ASP   B 1 66  ? 53.210 -11.146 9.120   1.00 13.10 ?  66  ASP   B CA   1 
ATOM   4838 C C    . ASP   B 1 66  ? 52.892 -9.672  9.332   1.00 13.18 ?  66  ASP   B C    1 
ATOM   4839 O O    . ASP   B 1 66  ? 52.314 -9.292  10.357  1.00 13.63 ?  66  ASP   B O    1 
ATOM   4840 C CB   . ASP   B 1 66  ? 54.643 -11.453 9.553   1.00 14.57 ?  66  ASP   B CB   1 
ATOM   4841 C CG   . ASP   B 1 66  ? 54.907 -12.940 9.721   1.00 16.46 ?  66  ASP   B CG   1 
ATOM   4842 O OD1  . ASP   B 1 66  ? 53.954 -13.748 9.642   1.00 17.37 ?  66  ASP   B OD1  1 
ATOM   4843 O OD2  . ASP   B 1 66  ? 56.084 -13.303 9.942   1.00 19.25 -1 66  ASP   B OD2  1 
ATOM   4844 H H    . ASP   B 1 66  ? 53.716 -11.816 7.324   1.00 15.23 ?  66  ASP   B H    1 
ATOM   4845 H HA   . ASP   B 1 66  ? 52.613 -11.660 9.683   1.00 15.73 ?  66  ASP   B HA   1 
ATOM   4846 H HB2  . ASP   B 1 66  ? 55.259 -11.123 8.881   1.00 17.49 ?  66  ASP   B HB2  1 
ATOM   4847 H HB3  . ASP   B 1 66  ? 54.820 -11.019 10.405  1.00 17.49 ?  66  ASP   B HB3  1 
ATOM   4848 N N    . ASP   B 1 67  ? 53.262 -8.821  8.374   1.00 12.77 ?  67  ASP   B N    1 
ATOM   4849 C CA   . ASP   B 1 67  ? 52.916 -7.411  8.476   1.00 13.56 ?  67  ASP   B CA   1 
ATOM   4850 C C    . ASP   B 1 67  ? 51.404 -7.204  8.396   1.00 13.64 ?  67  ASP   B C    1 
ATOM   4851 O O    . ASP   B 1 67  ? 50.842 -6.394  9.142   1.00 14.07 ?  67  ASP   B O    1 
ATOM   4852 C CB   . ASP   B 1 67  ? 53.632 -6.627  7.385   1.00 15.04 ?  67  ASP   B CB   1 
ATOM   4853 C CG   . ASP   B 1 67  ? 53.205 -5.190  7.354   1.00 16.33 ?  67  ASP   B CG   1 
ATOM   4854 O OD1  . ASP   B 1 67  ? 53.707 -4.385  8.177   1.00 17.34 ?  67  ASP   B OD1  1 
ATOM   4855 O OD2  . ASP   B 1 67  ? 52.337 -4.879  6.521   1.00 17.51 -1 67  ASP   B OD2  1 
ATOM   4856 H H    . ASP   B 1 67  ? 53.716 -9.034  7.674   1.00 15.34 ?  67  ASP   B H    1 
ATOM   4857 H HA   . ASP   B 1 67  ? 53.221 -7.072  9.331   1.00 16.29 ?  67  ASP   B HA   1 
ATOM   4858 H HB2  . ASP   B 1 67  ? 54.590 -6.648  7.547   1.00 18.06 ?  67  ASP   B HB2  1 
ATOM   4859 H HB3  . ASP   B 1 67  ? 53.437 -7.027  6.519   1.00 18.06 ?  67  ASP   B HB3  1 
ATOM   4860 N N    . TYR   B 1 68  ? 50.725 -7.938  7.509   1.00 13.11 ?  68  TYR   B N    1 
ATOM   4861 C CA   . TYR   B 1 68  ? 49.267 -7.858  7.437   1.00 13.92 ?  68  TYR   B CA   1 
ATOM   4862 C C    . TYR   B 1 68  ? 48.632 -8.200  8.781   1.00 13.42 ?  68  TYR   B C    1 
ATOM   4863 O O    . TYR   B 1 68  ? 47.703 -7.522  9.236   1.00 14.03 ?  68  TYR   B O    1 
ATOM   4864 C CB   . TYR   B 1 68  ? 48.736 -8.793  6.345   1.00 14.50 ?  68  TYR   B CB   1 
ATOM   4865 C CG   . TYR   B 1 68  ? 47.229 -8.941  6.402   1.00 15.62 ?  68  TYR   B CG   1 
ATOM   4866 C CD1  . TYR   B 1 68  ? 46.634 -9.897  7.222   1.00 16.53 ?  68  TYR   B CD1  1 
ATOM   4867 C CD2  . TYR   B 1 68  ? 46.404 -8.104  5.672   1.00 16.88 ?  68  TYR   B CD2  1 
ATOM   4868 C CE1  . TYR   B 1 68  ? 45.266 -10.015 7.307   1.00 17.97 ?  68  TYR   B CE1  1 
ATOM   4869 C CE2  . TYR   B 1 68  ? 45.024 -8.227  5.743   1.00 17.33 ?  68  TYR   B CE2  1 
ATOM   4870 C CZ   . TYR   B 1 68  ? 44.472 -9.178  6.566   1.00 17.58 ?  68  TYR   B CZ   1 
ATOM   4871 O OH   . TYR   B 1 68  ? 43.105 -9.289  6.650   1.00 18.61 ?  68  TYR   B OH   1 
ATOM   4872 H H    . TYR   B 1 68  ? 51.081 -8.490  6.948   1.00 15.74 ?  68  TYR   B H    1 
ATOM   4873 H HA   . TYR   B 1 68  ? 49.017 -6.952  7.212   1.00 16.72 ?  68  TYR   B HA   1 
ATOM   4874 H HB2  . TYR   B 1 68  ? 48.968 -8.429  5.481   1.00 17.42 ?  68  TYR   B HB2  1 
ATOM   4875 H HB3  . TYR   B 1 68  ? 49.130 -9.671  6.461   1.00 17.42 ?  68  TYR   B HB3  1 
ATOM   4876 H HD1  . TYR   B 1 68  ? 47.174 -10.467 7.730   1.00 19.85 ?  68  TYR   B HD1  1 
ATOM   4877 H HD2  . TYR   B 1 68  ? 46.784 -7.454  5.132   1.00 20.27 ?  68  TYR   B HD2  1 
ATOM   4878 H HE1  . TYR   B 1 68  ? 44.883 -10.670 7.851   1.00 21.58 ?  68  TYR   B HE1  1 
ATOM   4879 H HE2  . TYR   B 1 68  ? 44.480 -7.658  5.253   1.00 20.81 ?  68  TYR   B HE2  1 
ATOM   4880 H HH   . TYR   B 1 68  ? 42.730 -8.732  6.137   1.00 22.34 ?  68  TYR   B HH   1 
ATOM   4881 N N    . ILE   B 1 69  ? 49.109 -9.271  9.421   1.00 13.33 ?  69  ILE   B N    1 
ATOM   4882 C CA   . ILE   B 1 69  ? 48.554 -9.701  10.701  1.00 13.84 ?  69  ILE   B CA   1 
ATOM   4883 C C    . ILE   B 1 69  ? 48.814 -8.661  11.782  1.00 13.61 ?  69  ILE   B C    1 
ATOM   4884 O O    . ILE   B 1 69  ? 47.946 -8.385  12.614  1.00 13.85 ?  69  ILE   B O    1 
ATOM   4885 C CB   . ILE   B 1 69  ? 49.127 -11.078 11.086  1.00 14.91 ?  69  ILE   B CB   1 
ATOM   4886 C CG1  . ILE   B 1 69  ? 48.590 -12.174 10.156  1.00 14.89 ?  69  ILE   B CG1  1 
ATOM   4887 C CG2  . ILE   B 1 69  ? 48.847 -11.392 12.550  1.00 15.83 ?  69  ILE   B CG2  1 
ATOM   4888 C CD1  . ILE   B 1 69  ? 47.129 -12.502 10.343  1.00 15.23 ?  69  ILE   B CD1  1 
ATOM   4889 H H    . ILE   B 1 69  ? 49.754 -9.760  9.142   1.00 16.01 ?  69  ILE   B H    1 
ATOM   4890 H HA   . ILE   B 1 69  ? 47.593 -9.793  10.609  1.00 16.63 ?  69  ILE   B HA   1 
ATOM   4891 H HB   . ILE   B 1 69  ? 50.089 -11.036 10.973  1.00 17.90 ?  69  ILE   B HB   1 
ATOM   4892 H HG12 . ILE   B 1 69  ? 48.711 -11.882 9.238   1.00 17.89 ?  69  ILE   B HG12 1 
ATOM   4893 H HG13 . ILE   B 1 69  ? 49.098 -12.984 10.310  1.00 17.89 ?  69  ILE   B HG13 1 
ATOM   4894 H HG21 . ILE   B 1 69  ? 48.982 -12.343 12.693  1.00 19.01 ?  69  ILE   B HG21 1 
ATOM   4895 H HG22 . ILE   B 1 69  ? 49.462 -10.889 13.108  1.00 19.01 ?  69  ILE   B HG22 1 
ATOM   4896 H HG23 . ILE   B 1 69  ? 47.933 -11.153 12.758  1.00 19.01 ?  69  ILE   B HG23 1 
ATOM   4897 H HD11 . ILE   B 1 69  ? 46.880 -13.188 9.705   1.00 18.29 ?  69  ILE   B HD11 1 
ATOM   4898 H HD12 . ILE   B 1 69  ? 46.990 -12.828 11.247  1.00 18.29 ?  69  ILE   B HD12 1 
ATOM   4899 H HD13 . ILE   B 1 69  ? 46.599 -11.705 10.193  1.00 18.29 ?  69  ILE   B HD13 1 
ATOM   4900 N N    . ALA   B 1 70  ? 50.011 -8.076  11.802  1.00 13.69 ?  70  ALA   B N    1 
ATOM   4901 C CA   . ALA   B 1 70  ? 50.298 -7.045  12.794  1.00 13.53 ?  70  ALA   B CA   1 
ATOM   4902 C C    . ALA   B 1 70  ? 49.306 -5.892  12.690  1.00 13.78 ?  70  ALA   B C    1 
ATOM   4903 O O    . ALA   B 1 70  ? 48.877 -5.341  13.708  1.00 14.21 ?  70  ALA   B O    1 
ATOM   4904 C CB   . ALA   B 1 70  ? 51.731 -6.544  12.621  1.00 14.14 ?  70  ALA   B CB   1 
ATOM   4905 H H    . ALA   B 1 70  ? 50.650 -8.257  11.271  1.00 16.44 ?  70  ALA   B H    1 
ATOM   4906 H HA   . ALA   B 1 70  ? 50.223 -7.426  13.684  1.00 16.26 ?  70  ALA   B HA   1 
ATOM   4907 H HB1  . ALA   B 1 70  ? 51.921 -5.879  13.301  1.00 16.98 ?  70  ALA   B HB1  1 
ATOM   4908 H HB2  . ALA   B 1 70  ? 52.342 -7.295  12.716  1.00 16.98 ?  70  ALA   B HB2  1 
ATOM   4909 H HB3  . ALA   B 1 70  ? 51.826 -6.154  11.738  1.00 16.98 ?  70  ALA   B HB3  1 
ATOM   4910 N N    . THR   B 1 71  ? 48.922 -5.526  11.469  1.00 14.33 ?  71  THR   B N    1 
ATOM   4911 C CA   . THR   B 1 71  ? 48.034 -4.386  11.264  1.00 15.18 ?  71  THR   B CA   1 
ATOM   4912 C C    . THR   B 1 71  ? 46.567 -4.750  11.465  1.00 15.52 ?  71  THR   B C    1 
ATOM   4913 O O    . THR   B 1 71  ? 45.787 -3.934  11.969  1.00 17.14 ?  71  THR   B O    1 
ATOM   4914 C CB   . THR   B 1 71  ? 48.255 -3.824  9.859   1.00 17.09 ?  71  THR   B CB   1 
ATOM   4915 O OG1  . THR   B 1 71  ? 49.581 -3.292  9.763   1.00 19.07 ?  71  THR   B OG1  1 
ATOM   4916 C CG2  . THR   B 1 71  ? 47.237 -2.738  9.527   1.00 18.52 ?  71  THR   B CG2  1 
ATOM   4917 H H    . THR   B 1 71  ? 49.164 -5.919  10.748  1.00 17.21 ?  71  THR   B H    1 
ATOM   4918 H HA   . THR   B 1 71  ? 48.259 -3.689  11.901  1.00 18.23 ?  71  THR   B HA   1 
ATOM   4919 H HB   . THR   B 1 71  ? 48.161 -4.534  9.208   1.00 20.53 ?  71  THR   B HB   1 
ATOM   4920 H HG1  . THR   B 1 71  ? 49.713 -2.965  8.998   1.00 22.90 ?  71  THR   B HG1  1 
ATOM   4921 H HG21 . THR   B 1 71  ? 47.542 -2.218  8.764   1.00 22.23 ?  71  THR   B HG21 1 
ATOM   4922 H HG22 . THR   B 1 71  ? 46.380 -3.134  9.313   1.00 22.23 ?  71  THR   B HG22 1 
ATOM   4923 H HG23 . THR   B 1 71  ? 47.131 -2.139  10.285  1.00 22.23 ?  71  THR   B HG23 1 
ATOM   4924 N N    . ASN   B 1 72  ? 46.173 -5.962  11.065  1.00 15.12 ?  72  ASN   B N    1 
ATOM   4925 C CA   . ASN   B 1 72  ? 44.770 -6.319  10.931  1.00 15.63 ?  72  ASN   B CA   1 
ATOM   4926 C C    . ASN   B 1 72  ? 44.296 -7.421  11.865  1.00 16.20 ?  72  ASN   B C    1 
ATOM   4927 O O    . ASN   B 1 72  ? 43.080 -7.584  12.022  1.00 17.38 ?  72  ASN   B O    1 
ATOM   4928 C CB   . ASN   B 1 72  ? 44.473 -6.739  9.483   1.00 16.41 ?  72  ASN   B CB   1 
ATOM   4929 C CG   . ASN   B 1 72  ? 44.754 -5.630  8.498   1.00 17.51 ?  72  ASN   B CG   1 
ATOM   4930 O OD1  . ASN   B 1 72  ? 45.772 -5.633  7.800   1.00 18.84 ?  72  ASN   B OD1  1 
ATOM   4931 N ND2  . ASN   B 1 72  ? 43.875 -4.650  8.465   1.00 19.16 ?  72  ASN   B ND2  1 
ATOM   4932 H H    . ASN   B 1 72  ? 46.717 -6.603  10.856  1.00 18.16 ?  72  ASN   B H    1 
ATOM   4933 H HA   . ASN   B 1 72  ? 44.239 -5.533  11.117  1.00 18.77 ?  72  ASN   B HA   1 
ATOM   4934 H HB2  . ASN   B 1 72  ? 45.033 -7.498  9.250   1.00 19.71 ?  72  ASN   B HB2  1 
ATOM   4935 H HB3  . ASN   B 1 72  ? 43.538 -6.979  9.409   1.00 19.71 ?  72  ASN   B HB3  1 
ATOM   4936 H HD21 . ASN   B 1 72  ? 43.983 -3.991  7.922   1.00 23.00 ?  72  ASN   B HD21 1 
ATOM   4937 H HD22 . ASN   B 1 72  ? 43.178 -4.677  8.971   1.00 23.00 ?  72  ASN   B HD22 1 
ATOM   4938 N N    . GLY   B 1 73  ? 45.198 -8.175  12.487  1.00 15.79 ?  73  GLY   B N    1 
ATOM   4939 C CA   . GLY   B 1 73  ? 44.799 -9.317  13.273  1.00 15.37 ?  73  GLY   B CA   1 
ATOM   4940 C C    . GLY   B 1 73  ? 44.435 -10.499 12.401  1.00 14.04 ?  73  GLY   B C    1 
ATOM   4941 O O    . GLY   B 1 73  ? 44.428 -10.414 11.171  1.00 13.90 ?  73  GLY   B O    1 
ATOM   4942 H H    . GLY   B 1 73  ? 46.049 -8.039  12.463  1.00 18.96 ?  73  GLY   B H    1 
ATOM   4943 H HA2  . GLY   B 1 73  ? 45.527 -9.573  13.861  1.00 18.46 ?  73  GLY   B HA2  1 
ATOM   4944 H HA3  . GLY   B 1 73  ? 44.030 -9.083  13.815  1.00 18.46 ?  73  GLY   B HA3  1 
ATOM   4945 N N    . PRO   B 1 74  ? 44.126 -11.627 13.033  1.00 14.10 ?  74  PRO   B N    1 
ATOM   4946 C CA   . PRO   B 1 74  ? 43.883 -12.857 12.280  1.00 13.69 ?  74  PRO   B CA   1 
ATOM   4947 C C    . PRO   B 1 74  ? 42.578 -12.806 11.496  1.00 13.08 ?  74  PRO   B C    1 
ATOM   4948 O O    . PRO   B 1 74  ? 41.633 -12.072 11.819  1.00 14.31 ?  74  PRO   B O    1 
ATOM   4949 C CB   . PRO   B 1 74  ? 43.827 -13.928 13.376  1.00 14.68 ?  74  PRO   B CB   1 
ATOM   4950 C CG   . PRO   B 1 74  ? 43.366 -13.190 14.588  1.00 15.98 ?  74  PRO   B CG   1 
ATOM   4951 C CD   . PRO   B 1 74  ? 44.014 -11.837 14.486  1.00 15.61 ?  74  PRO   B CD   1 
ATOM   4952 H HA   . PRO   B 1 74  ? 44.627 -13.041 11.677  1.00 16.45 ?  74  PRO   B HA   1 
ATOM   4953 H HB2  . PRO   B 1 74  ? 43.195 -14.618 13.126  1.00 17.63 ?  74  PRO   B HB2  1 
ATOM   4954 H HB3  . PRO   B 1 74  ? 44.713 -14.304 13.515  1.00 17.63 ?  74  PRO   B HB3  1 
ATOM   4955 H HG2  . PRO   B 1 74  ? 42.400 -13.114 14.573  1.00 19.20 ?  74  PRO   B HG2  1 
ATOM   4956 H HG3  . PRO   B 1 74  ? 43.664 -13.655 15.384  1.00 19.20 ?  74  PRO   B HG3  1 
ATOM   4957 H HD2  . PRO   B 1 74  ? 43.440 -11.159 14.886  1.00 18.75 ?  74  PRO   B HD2  1 
ATOM   4958 H HD3  . PRO   B 1 74  ? 44.890 -11.845 14.898  1.00 18.75 ?  74  PRO   B HD3  1 
ATOM   4959 N N    . LEU   B 1 75  ? 42.550 -13.613 10.439  1.00 12.43 ?  75  LEU   B N    1 
ATOM   4960 C CA   . LEU   B 1 75  ? 41.335 -13.838 9.674   1.00 12.79 ?  75  LEU   B CA   1 
ATOM   4961 C C    . LEU   B 1 75  ? 40.370 -14.706 10.478  1.00 13.00 ?  75  LEU   B C    1 
ATOM   4962 O O    . LEU   B 1 75  ? 40.710 -15.248 11.531  1.00 14.14 ?  75  LEU   B O    1 
ATOM   4963 C CB   . LEU   B 1 75  ? 41.665 -14.545 8.360   1.00 12.81 ?  75  LEU   B CB   1 
ATOM   4964 C CG   . LEU   B 1 75  ? 42.508 -13.783 7.332   1.00 14.26 ?  75  LEU   B CG   1 
ATOM   4965 C CD1  . LEU   B 1 75  ? 42.677 -14.608 6.064   1.00 15.73 ?  75  LEU   B CD1  1 
ATOM   4966 C CD2  . LEU   B 1 75  ? 41.921 -12.433 7.007   1.00 17.57 ?  75  LEU   B CD2  1 
ATOM   4967 H H    . LEU   B 1 75  ? 43.228 -14.050 10.142  1.00 14.93 ?  75  LEU   B H    1 
ATOM   4968 H HA   . LEU   B 1 75  ? 40.902 -12.993 9.482   1.00 15.37 ?  75  LEU   B HA   1 
ATOM   4969 H HB2  . LEU   B 1 75  ? 42.143 -15.362 8.571   1.00 15.38 ?  75  LEU   B HB2  1 
ATOM   4970 H HB3  . LEU   B 1 75  ? 40.826 -14.776 7.925   1.00 15.38 ?  75  LEU   B HB3  1 
ATOM   4971 H HG   . LEU   B 1 75  ? 43.389 -13.636 7.705   1.00 17.13 ?  75  LEU   B HG   1 
ATOM   4972 H HD11 . LEU   B 1 75  ? 43.217 -14.106 5.429   1.00 18.89 ?  75  LEU   B HD11 1 
ATOM   4973 H HD12 . LEU   B 1 75  ? 43.120 -15.442 6.284   1.00 18.89 ?  75  LEU   B HD12 1 
ATOM   4974 H HD13 . LEU   B 1 75  ? 41.804 -14.788 5.681   1.00 18.89 ?  75  LEU   B HD13 1 
ATOM   4975 H HD21 . LEU   B 1 75  ? 42.430 -12.032 6.287   1.00 21.10 ?  75  LEU   B HD21 1 
ATOM   4976 H HD22 . LEU   B 1 75  ? 40.996 -12.547 6.738   1.00 21.10 ?  75  LEU   B HD22 1 
ATOM   4977 H HD23 . LEU   B 1 75  ? 41.966 -11.870 7.798   1.00 21.10 ?  75  LEU   B HD23 1 
ATOM   4978 N N    . LYS   B 1 76  ? 39.145 -14.825 9.965   1.00 14.02 ?  76  LYS   B N    1 
ATOM   4979 C CA   . LYS   B 1 76  ? 38.162 -15.789 10.443  1.00 15.25 ?  76  LYS   B CA   1 
ATOM   4980 C C    . LYS   B 1 76  ? 38.240 -17.052 9.590   1.00 13.56 ?  76  LYS   B C    1 
ATOM   4981 O O    . LYS   B 1 76  ? 38.496 -16.980 8.387   1.00 13.37 ?  76  LYS   B O    1 
ATOM   4982 C CB   . LYS   B 1 76  ? 36.742 -15.219 10.282  1.00 18.06 ?  76  LYS   B CB   1 
ATOM   4983 C CG   . LYS   B 1 76  ? 36.479 -13.834 10.894  1.00 20.75 ?  76  LYS   B CG   1 
ATOM   4984 C CD   . LYS   B 1 76  ? 35.077 -13.298 10.539  1.00 22.73 ?  76  LYS   B CD   1 
ATOM   4985 C CE   . LYS   B 1 76  ? 34.799 -11.951 11.193  1.00 24.84 ?  76  LYS   B CE   1 
ATOM   4986 N NZ   . LYS   B 1 76  ? 33.534 -11.330 10.711  1.00 25.87 ?  76  LYS   B NZ   1 
ATOM   4987 H H    . LYS   B 1 76  ? 38.853 -14.346 9.319   1.00 16.84 ?  76  LYS   B H    1 
ATOM   4988 H HA   . LYS   B 1 76  ? 38.316 -16.016 11.376  1.00 18.31 ?  76  LYS   B HA   1 
ATOM   4989 H HB2  . LYS   B 1 76  ? 36.548 -15.153 9.332   1.00 21.68 ?  76  LYS   B HB2  1 
ATOM   4990 H HB3  . LYS   B 1 76  ? 36.114 -15.835 10.692  1.00 21.68 ?  76  LYS   B HB3  1 
ATOM   4991 H HG2  . LYS   B 1 76  ? 36.546 -13.894 11.859  1.00 24.91 ?  76  LYS   B HG2  1 
ATOM   4992 H HG3  . LYS   B 1 76  ? 37.138 -13.206 10.553  1.00 24.91 ?  76  LYS   B HG3  1 
ATOM   4993 H HD2  . LYS   B 1 76  ? 35.014 -13.186 9.577   1.00 27.30 ?  76  LYS   B HD2  1 
ATOM   4994 H HD3  . LYS   B 1 76  ? 34.409 -13.929 10.847  1.00 27.30 ?  76  LYS   B HD3  1 
ATOM   4995 H HE2  . LYS   B 1 76  ? 34.728 -12.076 12.152  1.00 29.82 ?  76  LYS   B HE2  1 
ATOM   4996 H HE3  . LYS   B 1 76  ? 35.529 -11.345 10.990  1.00 29.82 ?  76  LYS   B HE3  1 
ATOM   4997 H HZ1  . LYS   B 1 76  ? 33.405 -10.546 11.116  1.00 31.06 ?  76  LYS   B HZ1  1 
ATOM   4998 H HZ2  . LYS   B 1 76  ? 33.573 -11.196 9.832   1.00 31.06 ?  76  LYS   B HZ2  1 
ATOM   4999 H HZ3  . LYS   B 1 76  ? 32.843 -11.862 10.891  1.00 31.06 ?  76  LYS   B HZ3  1 
ATOM   5000 N N    . VAL   B 1 77  ? 37.985 -18.214 10.207  1.00 13.91 ?  77  VAL   B N    1 
ATOM   5001 C CA   . VAL   B 1 77  ? 37.765 -19.420 9.411   1.00 13.78 ?  77  VAL   B CA   1 
ATOM   5002 C C    . VAL   B 1 77  ? 36.574 -19.172 8.497   1.00 12.91 ?  77  VAL   B C    1 
ATOM   5003 O O    . VAL   B 1 77  ? 35.515 -18.714 8.944   1.00 13.27 ?  77  VAL   B O    1 
ATOM   5004 C CB   . VAL   B 1 77  ? 37.576 -20.657 10.305  1.00 15.04 ?  77  VAL   B CB   1 
ATOM   5005 C CG1  . VAL   B 1 77  ? 37.289 -21.880 9.446   1.00 15.97 ?  77  VAL   B CG1  1 
ATOM   5006 C CG2  . VAL   B 1 77  ? 38.812 -20.896 11.166  1.00 16.74 ?  77  VAL   B CG2  1 
ATOM   5007 H H    . VAL   B 1 77  ? 37.945 -18.324 11.059  1.00 16.70 ?  77  VAL   B H    1 
ATOM   5008 H HA   . VAL   B 1 77  ? 38.537 -19.570 8.852   1.00 16.55 ?  77  VAL   B HA   1 
ATOM   5009 H HB   . VAL   B 1 77  ? 36.815 -20.511 10.894  1.00 18.06 ?  77  VAL   B HB   1 
ATOM   5010 H HG11 . VAL   B 1 77  ? 37.345 -22.671 10.002  1.00 19.18 ?  77  VAL   B HG11 1 
ATOM   5011 H HG12 . VAL   B 1 77  ? 36.393 -21.804 9.074   1.00 19.18 ?  77  VAL   B HG12 1 
ATOM   5012 H HG13 . VAL   B 1 77  ? 37.941 -21.924 8.734   1.00 19.18 ?  77  VAL   B HG13 1 
ATOM   5013 H HG21 . VAL   B 1 77  ? 38.675 -21.699 11.692  1.00 20.10 ?  77  VAL   B HG21 1 
ATOM   5014 H HG22 . VAL   B 1 77  ? 39.579 -21.003 10.586  1.00 20.10 ?  77  VAL   B HG22 1 
ATOM   5015 H HG23 . VAL   B 1 77  ? 38.940 -20.133 11.751  1.00 20.10 ?  77  VAL   B HG23 1 
ATOM   5016 N N    . GLY   B 1 78  ? 36.752 -19.447 7.207   1.00 12.47 ?  78  GLY   B N    1 
ATOM   5017 C CA   . GLY   B 1 78  ? 35.778 -19.111 6.195   1.00 12.38 ?  78  GLY   B CA   1 
ATOM   5018 C C    . GLY   B 1 78  ? 36.030 -17.791 5.504   1.00 11.80 ?  78  GLY   B C    1 
ATOM   5019 O O    . GLY   B 1 78  ? 35.357 -17.496 4.510   1.00 12.34 ?  78  GLY   B O    1 
ATOM   5020 H H    . GLY   B 1 78  ? 37.452 -19.836 6.896   1.00 14.98 ?  78  GLY   B H    1 
ATOM   5021 H HA2  . GLY   B 1 78  ? 35.773 -19.807 5.523   1.00 14.87 ?  78  GLY   B HA2  1 
ATOM   5022 H HA3  . GLY   B 1 78  ? 34.900 -19.072 6.602   1.00 14.87 ?  78  GLY   B HA3  1 
ATOM   5023 N N    . GLY   B 1 79  ? 36.977 -16.992 6.000   1.00 11.86 ?  79  GLY   B N    1 
ATOM   5024 C CA   . GLY   B 1 79  ? 37.279 -15.696 5.432   1.00 11.78 ?  79  GLY   B CA   1 
ATOM   5025 C C    . GLY   B 1 79  ? 38.512 -15.705 4.537   1.00 11.32 ?  79  GLY   B C    1 
ATOM   5026 O O    . GLY   B 1 79  ? 39.123 -16.739 4.269   1.00 11.75 ?  79  GLY   B O    1 
ATOM   5027 H H    . GLY   B 1 79  ? 37.475 -17.189 6.669   1.00 14.24 ?  79  GLY   B H    1 
ATOM   5028 H HA2  . GLY   B 1 79  ? 36.525 -15.388 4.900   1.00 14.15 ?  79  GLY   B HA2  1 
ATOM   5029 H HA3  . GLY   B 1 79  ? 37.429 -15.057 6.143   1.00 14.15 ?  79  GLY   B HA3  1 
ATOM   5030 N N    . SER   B 1 80  ? 38.873 -14.506 4.068   1.00 11.52 ?  80  SER   B N    1 
ATOM   5031 C CA   . SER   B 1 80  ? 39.979 -14.369 3.131   1.00 11.54 ?  80  SER   B CA   1 
ATOM   5032 C C    . SER   B 1 80  ? 40.560 -12.964 3.199   1.00 11.55 ?  80  SER   B C    1 
ATOM   5033 O O    . SER   B 1 80  ? 39.940 -12.034 3.722   1.00 12.66 ?  80  SER   B O    1 
ATOM   5034 C CB   . SER   B 1 80  ? 39.534 -14.651 1.692   1.00 11.77 ?  80  SER   B CB   1 
ATOM   5035 O OG   . SER   B 1 80  ? 38.696 -13.623 1.192   1.00 12.94 ?  80  SER   B OG   1 
ATOM   5036 H H    . SER   B 1 80  ? 38.495 -13.763 4.274   1.00 13.83 ?  80  SER   B H    1 
ATOM   5037 H HA   . SER   B 1 80  ? 40.672 -15.000 3.371   1.00 13.86 ?  80  SER   B HA   1 
ATOM   5038 H HB2  . SER   B 1 80  ? 40.317 -14.721 1.125   1.00 14.14 ?  80  SER   B HB2  1 
ATOM   5039 H HB3  . SER   B 1 80  ? 39.045 -15.494 1.676   1.00 14.14 ?  80  SER   B HB3  1 
ATOM   5040 H HG   . SER   B 1 80  ? 38.007 -13.563 1.671   1.00 15.55 ?  80  SER   B HG   1 
ATOM   5041 N N    . CYS   B 1 81  ? 41.748 -12.814 2.612   1.00 11.20 ?  81  CYS   B N    1 
ATOM   5042 C CA   . CYS   B 1 81  ? 42.290 -11.499 2.307   1.00 11.44 ?  81  CYS   B CA   1 
ATOM   5043 C C    . CYS   B 1 81  ? 43.064 -11.580 1.000   1.00 10.57 ?  81  CYS   B C    1 
ATOM   5044 O O    . CYS   B 1 81  ? 43.577 -12.640 0.626   1.00 11.63 ?  81  CYS   B O    1 
ATOM   5045 C CB   . CYS   B 1 81  ? 43.181 -10.943 3.429   1.00 12.15 ?  81  CYS   B CB   1 
ATOM   5046 S SG   . CYS   B 1 81  ? 44.699 -11.880 3.684   1.00 12.37 ?  81  CYS   B SG   1 
ATOM   5047 H H    . CYS   B 1 81  ? 42.261 -13.464 2.369   1.00 13.45 ?  81  CYS   B H    1 
ATOM   5048 H HA   . CYS   B 1 81  ? 41.554 -10.873 2.180   1.00 13.74 ?  81  CYS   B HA   1 
ATOM   5049 H HB2  . CYS   B 1 81  ? 43.430 -10.033 3.211   1.00 14.60 ?  81  CYS   B HB2  1 
ATOM   5050 H HB3  . CYS   B 1 81  ? 42.677 -10.955 4.260   1.00 14.60 ?  81  CYS   B HB3  1 
ATOM   5051 H HG   . CYS   B 1 81  ? 45.323 -11.380 4.585   1.00 14.85 ?  81  CYS   B HG   1 
ATOM   5052 N N    . VAL   B 1 82  ? 43.173 -10.434 0.329   1.00 11.05 ?  82  VAL   B N    1 
ATOM   5053 C CA   . VAL   B 1 82  ? 43.931 -10.310 -0.911  1.00 11.09 ?  82  VAL   B CA   1 
ATOM   5054 C C    . VAL   B 1 82  ? 45.272 -9.668  -0.588  1.00 11.42 ?  82  VAL   B C    1 
ATOM   5055 O O    . VAL   B 1 82  ? 45.319 -8.547  -0.058  1.00 12.37 ?  82  VAL   B O    1 
ATOM   5056 C CB   . VAL   B 1 82  ? 43.185 -9.466  -1.955  1.00 12.57 ?  82  VAL   B CB   1 
ATOM   5057 C CG1  . VAL   B 1 82  ? 44.041 -9.305  -3.210  1.00 13.96 ?  82  VAL   B CG1  1 
ATOM   5058 C CG2  . VAL   B 1 82  ? 41.833 -10.068 -2.283  1.00 13.50 ?  82  VAL   B CG2  1 
ATOM   5059 H H    . VAL   B 1 82  ? 42.802 -9.693  0.575   1.00 13.27 ?  82  VAL   B H    1 
ATOM   5060 H HA   . VAL   B 1 82  ? 44.088 -11.191 -1.284  1.00 13.32 ?  82  VAL   B HA   1 
ATOM   5061 H HB   . VAL   B 1 82  ? 43.031 -8.583  -1.588  1.00 15.10 ?  82  VAL   B HB   1 
ATOM   5062 H HG11 . VAL   B 1 82  ? 43.481 -8.998  -3.939  1.00 16.76 ?  82  VAL   B HG11 1 
ATOM   5063 H HG12 . VAL   B 1 82  ? 44.739 -8.647  -3.036  1.00 16.76 ?  82  VAL   B HG12 1 
ATOM   5064 H HG13 . VAL   B 1 82  ? 44.441 -10.157 -3.435  1.00 16.76 ?  82  VAL   B HG13 1 
ATOM   5065 H HG21 . VAL   B 1 82  ? 41.402 -9.526  -2.965  1.00 16.21 ?  82  VAL   B HG21 1 
ATOM   5066 H HG22 . VAL   B 1 82  ? 41.958 -10.971 -2.611  1.00 16.21 ?  82  VAL   B HG22 1 
ATOM   5067 H HG23 . VAL   B 1 82  ? 41.288 -10.079 -1.480  1.00 16.21 ?  82  VAL   B HG23 1 
ATOM   5068 N N    . LEU   B 1 83  ? 46.354 -10.347 -0.959  1.00 11.03 ?  83  LEU   B N    1 
ATOM   5069 C CA   . LEU   B 1 83  ? 47.707 -9.829  -0.837  1.00 10.80 ?  83  LEU   B CA   1 
ATOM   5070 C C    . LEU   B 1 83  ? 48.411 -9.964  -2.186  1.00 11.12 ?  83  LEU   B C    1 
ATOM   5071 O O    . LEU   B 1 83  ? 47.815 -10.384 -3.184  1.00 11.09 ?  83  LEU   B O    1 
ATOM   5072 C CB   . LEU   B 1 83  ? 48.458 -10.505 0.320   1.00 11.67 ?  83  LEU   B CB   1 
ATOM   5073 C CG   . LEU   B 1 83  ? 47.931 -10.150 1.716   1.00 13.08 ?  83  LEU   B CG   1 
ATOM   5074 C CD1  . LEU   B 1 83  ? 48.552 -11.033 2.786   1.00 13.74 ?  83  LEU   B CD1  1 
ATOM   5075 C CD2  . LEU   B 1 83  ? 48.146 -8.671  2.054   1.00 13.95 ?  83  LEU   B CD2  1 
ATOM   5076 H H    . LEU   B 1 83  ? 46.316 -11.146 -1.292  1.00 13.25 ?  83  LEU   B H    1 
ATOM   5077 H HA   . LEU   B 1 83  ? 47.650 -8.884  -0.640  1.00 12.98 ?  83  LEU   B HA   1 
ATOM   5078 H HB2  . LEU   B 1 83  ? 48.395 -11.464 0.216   1.00 14.02 ?  83  LEU   B HB2  1 
ATOM   5079 H HB3  . LEU   B 1 83  ? 49.389 -10.232 0.281   1.00 14.02 ?  83  LEU   B HB3  1 
ATOM   5080 H HG   . LEU   B 1 83  ? 46.976 -10.312 1.727   1.00 15.71 ?  83  LEU   B HG   1 
ATOM   5081 H HD11 . LEU   B 1 83  ? 48.186 -10.786 3.650   1.00 16.50 ?  83  LEU   B HD11 1 
ATOM   5082 H HD12 . LEU   B 1 83  ? 48.331 -11.962 2.592   1.00 16.50 ?  83  LEU   B HD12 1 
ATOM   5083 H HD13 . LEU   B 1 83  ? 49.510 -10.914 2.782   1.00 16.50 ?  83  LEU   B HD13 1 
ATOM   5084 H HD21 . LEU   B 1 83  ? 47.918 -8.527  2.985   1.00 16.75 ?  83  LEU   B HD21 1 
ATOM   5085 H HD22 . LEU   B 1 83  ? 49.077 -8.446  1.901   1.00 16.75 ?  83  LEU   B HD22 1 
ATOM   5086 H HD23 . LEU   B 1 83  ? 47.576 -8.132  1.485   1.00 16.75 ?  83  LEU   B HD23 1 
ATOM   5087 N N    . SER   B 1 84  ? 49.686 -9.585  -2.233  1.00 12.02 ?  84  SER   B N    1 
ATOM   5088 C CA   . SER   B 1 84  ? 50.429 -9.692  -3.482  1.00 12.39 ?  84  SER   B CA   1 
ATOM   5089 C C    . SER   B 1 84  ? 50.568 -11.149 -3.910  1.00 11.64 ?  84  SER   B C    1 
ATOM   5090 O O    . SER   B 1 84  ? 50.683 -12.056 -3.088  1.00 11.68 ?  84  SER   B O    1 
ATOM   5091 C CB   . SER   B 1 84  ? 51.828 -9.103  -3.323  1.00 14.29 ?  84  SER   B CB   1 
ATOM   5092 O OG   . SER   B 1 84  ? 52.576 -9.301  -4.509  1.00 16.33 ?  84  SER   B OG   1 
ATOM   5093 H H    . SER   B 1 84  ? 50.130 -9.257  -1.574  1.00 14.43 ?  84  SER   B H    1 
ATOM   5094 H HA   . SER   B 1 84  ? 49.965 -9.213  -4.181  1.00 14.88 ?  84  SER   B HA   1 
ATOM   5095 H HB2  . SER   B 1 84  ? 51.754 -8.151  -3.148  1.00 17.17 ?  84  SER   B HB2  1 
ATOM   5096 H HB3  . SER   B 1 84  ? 52.282 -9.544  -2.590  1.00 17.17 ?  84  SER   B HB3  1 
ATOM   5097 H HG   . SER   B 1 84  ? 53.345 -8.968  -4.428  1.00 19.62 ?  84  SER   B HG   1 
ATOM   5098 N N    . GLY   B 1 85  ? 50.627 -11.359 -5.220  1.00 12.67 ?  85  GLY   B N    1 
ATOM   5099 C CA   . GLY   B 1 85  ? 50.979 -12.645 -5.778  1.00 13.37 ?  85  GLY   B CA   1 
ATOM   5100 C C    . GLY   B 1 85  ? 52.451 -12.845 -6.069  1.00 12.63 ?  85  GLY   B C    1 
ATOM   5101 O O    . GLY   B 1 85  ? 52.827 -13.926 -6.526  1.00 13.24 ?  85  GLY   B O    1 
ATOM   5102 H H    . GLY   B 1 85  ? 50.482 -10.755 -5.807  1.00 15.22 ?  85  GLY   B H    1 
ATOM   5103 H HA2  . GLY   B 1 85  ? 50.707 -13.341 -5.163  1.00 16.06 ?  85  GLY   B HA2  1 
ATOM   5104 H HA3  . GLY   B 1 85  ? 50.502 -12.768 -6.606  1.00 16.06 ?  85  GLY   B HA3  1 
ATOM   5105 N N    . HIS   B 1 86  ? 53.303 -11.848 -5.839  1.00 12.30 ?  86  HIS   B N    1 
ATOM   5106 C CA   . HIS   B 1 86  ? 54.765 -12.027 -5.913  1.00 12.56 ?  86  HIS   B CA   1 
ATOM   5107 C C    . HIS   B 1 86  ? 55.136 -12.534 -7.305  1.00 12.69 ?  86  HIS   B C    1 
ATOM   5108 O O    . HIS   B 1 86  ? 54.745 -11.913 -8.306  1.00 13.38 ?  86  HIS   B O    1 
ATOM   5109 C CB   . HIS   B 1 86  ? 55.247 -12.879 -4.742  1.00 12.79 ?  86  HIS   B CB   1 
ATOM   5110 C CG   . HIS   B 1 86  ? 54.932 -12.282 -3.413  1.00 12.99 ?  86  HIS   B CG   1 
ATOM   5111 N ND1  . HIS   B 1 86  ? 55.749 -11.357 -2.797  1.00 14.64 ?  86  HIS   B ND1  1 
ATOM   5112 C CD2  . HIS   B 1 86  ? 53.861 -12.444 -2.601  1.00 13.43 ?  86  HIS   B CD2  1 
ATOM   5113 C CE1  . HIS   B 1 86  ? 55.191 -10.979 -1.662  1.00 14.44 ?  86  HIS   B CE1  1 
ATOM   5114 N NE2  . HIS   B 1 86  ? 54.048 -11.624 -1.518  1.00 13.61 ?  86  HIS   B NE2  1 
ATOM   5115 H H    . HIS   B 1 86  ? 53.069 -11.047 -5.644  1.00 14.77 ?  86  HIS   B H    1 
ATOM   5116 H HA   . HIS   B 1 86  ? 55.183 -11.154 -5.814  1.00 15.09 ?  86  HIS   B HA   1 
ATOM   5117 H HB2  . HIS   B 1 86  ? 54.825 -13.747 -4.789  1.00 15.36 ?  86  HIS   B HB2  1 
ATOM   5118 H HB3  . HIS   B 1 86  ? 56.213 -12.975 -4.798  1.00 15.36 ?  86  HIS   B HB3  1 
ATOM   5119 H HD2  . HIS   B 1 86  ? 53.128 -13.001 -2.755  1.00 16.13 ?  86  HIS   B HD2  1 
ATOM   5120 H HE1  . HIS   B 1 86  ? 55.547 -10.373 -1.054  1.00 17.34 ?  86  HIS   B HE1  1 
ATOM   5121 H HE2  . HIS   B 1 86  ? 53.506 -11.551 -0.848  1.00 16.35 ?  86  HIS   B HE2  1 
ATOM   5122 N N    . ASN   B 1 87  ? 55.900 -13.618 -7.419  1.00 12.83 ?  87  ASN   B N    1 
ATOM   5123 C CA   . ASN   B 1 87  ? 56.296 -14.187 -8.700  1.00 13.70 ?  87  ASN   B CA   1 
ATOM   5124 C C    . ASN   B 1 87  ? 55.311 -15.226 -9.207  1.00 13.18 ?  87  ASN   B C    1 
ATOM   5125 O O    . ASN   B 1 87  ? 55.625 -15.938 -10.167 1.00 14.72 ?  87  ASN   B O    1 
ATOM   5126 C CB   . ASN   B 1 87  ? 57.693 -14.815 -8.588  1.00 15.39 ?  87  ASN   B CB   1 
ATOM   5127 C CG   . ASN   B 1 87  ? 57.746 -15.944 -7.563  1.00 16.41 ?  87  ASN   B CG   1 
ATOM   5128 O OD1  . ASN   B 1 87  ? 57.104 -15.876 -6.509  1.00 15.43 ?  87  ASN   B OD1  1 
ATOM   5129 N ND2  . ASN   B 1 87  ? 58.486 -17.004 -7.887  1.00 18.56 ?  87  ASN   B ND2  1 
ATOM   5130 H H    . ASN   B 1 87  ? 56.215 -14.056 -6.745  1.00 15.42 ?  87  ASN   B H    1 
ATOM   5131 H HA   . ASN   B 1 87  ? 56.340 -13.478 -9.357  1.00 16.45 ?  87  ASN   B HA   1 
ATOM   5132 H HB2  . ASN   B 1 87  ? 57.944 -15.179 -9.453  1.00 18.48 ?  87  ASN   B HB2  1 
ATOM   5133 H HB3  . ASN   B 1 87  ? 58.325 -14.134 -8.318  1.00 18.48 ?  87  ASN   B HB3  1 
ATOM   5134 H HD21 . ASN   B 1 87  ? 58.550 -17.666 -7.344  1.00 22.28 ?  87  ASN   B HD21 1 
ATOM   5135 H HD22 . ASN   B 1 87  ? 58.913 -17.020 -8.636  1.00 22.28 ?  87  ASN   B HD22 1 
ATOM   5136 N N    . LEU   B 1 88  ? 54.135 -15.327 -8.586  1.00 12.30 ?  88  LEU   B N    1 
ATOM   5137 C CA   . LEU   B 1 88  ? 53.155 -16.356 -8.916  1.00 12.28 ?  88  LEU   B CA   1 
ATOM   5138 C C    . LEU   B 1 88  ? 51.922 -15.837 -9.637  1.00 12.10 ?  88  LEU   B C    1 
ATOM   5139 O O    . LEU   B 1 88  ? 51.317 -16.586 -10.415 1.00 13.93 ?  88  LEU   B O    1 
ATOM   5140 C CB   . LEU   B 1 88  ? 52.685 -17.053 -7.634  1.00 13.39 ?  88  LEU   B CB   1 
ATOM   5141 C CG   . LEU   B 1 88  ? 53.806 -17.696 -6.826  1.00 15.76 ?  88  LEU   B CG   1 
ATOM   5142 C CD1  . LEU   B 1 88  ? 53.300 -18.058 -5.440  1.00 17.63 ?  88  LEU   B CD1  1 
ATOM   5143 C CD2  . LEU   B 1 88  ? 54.336 -18.915 -7.551  1.00 18.72 ?  88  LEU   B CD2  1 
ATOM   5144 H H    . LEU   B 1 88  ? 53.879 -14.801 -7.947  1.00 14.77 ?  88  LEU   B H    1 
ATOM   5145 H HA   . LEU   B 1 88  ? 53.573 -17.018 -9.477  1.00 14.75 ?  88  LEU   B HA   1 
ATOM   5146 H HB2  . LEU   B 1 88  ? 52.246 -16.403 -7.062  1.00 16.08 ?  88  LEU   B HB2  1 
ATOM   5147 H HB3  . LEU   B 1 88  ? 52.058 -17.753 -7.873  1.00 16.08 ?  88  LEU   B HB3  1 
ATOM   5148 H HG   . LEU   B 1 88  ? 54.532 -17.060 -6.723  1.00 18.92 ?  88  LEU   B HG   1 
ATOM   5149 H HD11 . LEU   B 1 88  ? 53.949 -18.634 -5.007  1.00 21.17 ?  88  LEU   B HD11 1 
ATOM   5150 H HD12 . LEU   B 1 88  ? 53.180 -17.246 -4.924  1.00 21.17 ?  88  LEU   B HD12 1 
ATOM   5151 H HD13 . LEU   B 1 88  ? 52.452 -18.521 -5.529  1.00 21.17 ?  88  LEU   B HD13 1 
ATOM   5152 H HD21 . LEU   B 1 88  ? 54.995 -19.353 -6.991  1.00 22.48 ?  88  LEU   B HD21 1 
ATOM   5153 H HD22 . LEU   B 1 88  ? 53.600 -19.519 -7.731  1.00 22.48 ?  88  LEU   B HD22 1 
ATOM   5154 H HD23 . LEU   B 1 88  ? 54.745 -18.633 -8.384  1.00 22.48 ?  88  LEU   B HD23 1 
ATOM   5155 N N    . ALA   B 1 89  ? 51.513 -14.603 -9.369  1.00 11.64 ?  89  ALA   B N    1 
ATOM   5156 C CA   . ALA   B 1 89  ? 50.219 -14.111 -9.818  1.00 11.32 ?  89  ALA   B CA   1 
ATOM   5157 C C    . ALA   B 1 89  ? 50.189 -12.620 -9.543  1.00 11.64 ?  89  ALA   B C    1 
ATOM   5158 O O    . ALA   B 1 89  ? 51.028 -12.099 -8.808  1.00 12.59 ?  89  ALA   B O    1 
ATOM   5159 C CB   . ALA   B 1 89  ? 49.084 -14.793 -9.057  1.00 11.37 ?  89  ALA   B CB   1 
ATOM   5160 H H    . ALA   B 1 89  ? 51.960 -14.026 -8.912  1.00 13.99 ?  89  ALA   B H    1 
ATOM   5161 H HA   . ALA   B 1 89  ? 50.108 -14.262 -10.770 1.00 13.60 ?  89  ALA   B HA   1 
ATOM   5162 H HB1  . ALA   B 1 89  ? 48.233 -14.463 -9.394  1.00 13.66 ?  89  ALA   B HB1  1 
ATOM   5163 H HB2  . ALA   B 1 89  ? 49.141 -15.753 -9.202  1.00 13.66 ?  89  ALA   B HB2  1 
ATOM   5164 H HB3  . ALA   B 1 89  ? 49.167 -14.594 -8.116  1.00 13.66 ?  89  ALA   B HB3  1 
ATOM   5165 N N    . LYS   B 1 90  ? 49.188 -11.935 -10.092 1.00 12.50 ?  90  LYS   B N    1 
ATOM   5166 C CA   . LYS   B 1 90  ? 48.997 -10.546 -9.690  1.00 12.85 ?  90  LYS   B CA   1 
ATOM   5167 C C    . LYS   B 1 90  ? 48.678 -10.468 -8.202  1.00 12.92 ?  90  LYS   B C    1 
ATOM   5168 O O    . LYS   B 1 90  ? 49.307 -9.704  -7.455  1.00 14.31 ?  90  LYS   B O    1 
ATOM   5169 C CB   . LYS   B 1 90  ? 47.912 -9.890  -10.542 1.00 14.55 ?  90  LYS   B CB   1 
ATOM   5170 C CG   . LYS   B 1 90  ? 47.630 -8.443  -10.179 1.00 15.27 ?  90  LYS   B CG   1 
ATOM   5171 C CD   . LYS   B 1 90  ? 48.841 -7.553  -10.279 1.00 17.97 ?  90  LYS   B CD   1 
ATOM   5172 C CE   . LYS   B 1 90  ? 48.421 -6.117  -10.064 1.00 20.30 ?  90  LYS   B CE   1 
ATOM   5173 N NZ   . LYS   B 1 90  ? 49.590 -5.210  -9.976  1.00 20.55 ?  90  LYS   B NZ   1 
ATOM   5174 H H    . LYS   B 1 90  ? 48.628 -12.239 -10.668 1.00 15.02 ?  90  LYS   B H    1 
ATOM   5175 H HA   . LYS   B 1 90  ? 49.821 -10.068 -9.834  1.00 15.44 ?  90  LYS   B HA   1 
ATOM   5176 H HB2  . LYS   B 1 90  ? 48.197 -9.910  -11.472 1.00 17.48 ?  90  LYS   B HB2  1 
ATOM   5177 H HB3  . LYS   B 1 90  ? 47.087 -10.390 -10.446 1.00 17.48 ?  90  LYS   B HB3  1 
ATOM   5178 H HG2  . LYS   B 1 90  ? 46.953 -8.099  -10.783 1.00 18.34 ?  90  LYS   B HG2  1 
ATOM   5179 H HG3  . LYS   B 1 90  ? 47.301 -8.408  -9.265  1.00 18.34 ?  90  LYS   B HG3  1 
ATOM   5180 H HD2  . LYS   B 1 90  ? 49.482 -7.796  -9.591  1.00 21.58 ?  90  LYS   B HD2  1 
ATOM   5181 H HD3  . LYS   B 1 90  ? 49.236 -7.637  -11.160 1.00 21.58 ?  90  LYS   B HD3  1 
ATOM   5182 H HE2  . LYS   B 1 90  ? 47.872 -5.824  -10.811 1.00 24.38 ?  90  LYS   B HE2  1 
ATOM   5183 H HE3  . LYS   B 1 90  ? 47.923 -6.042  -9.236  1.00 24.38 ?  90  LYS   B HE3  1 
ATOM   5184 H HZ1  . LYS   B 1 90  ? 49.324 -4.368  -9.853  1.00 24.68 ?  90  LYS   B HZ1  1 
ATOM   5185 H HZ2  . LYS   B 1 90  ? 50.114 -5.448  -9.296  1.00 24.68 ?  90  LYS   B HZ2  1 
ATOM   5186 H HZ3  . LYS   B 1 90  ? 50.068 -5.250  -10.731 1.00 24.68 ?  90  LYS   B HZ3  1 
ATOM   5187 N N    . HIS   B 1 91  ? 47.727 -11.292 -7.752  1.00 11.18 ?  91  HIS   B N    1 
ATOM   5188 C CA   . HIS   B 1 91  ? 47.269 -11.316 -6.376  1.00 11.41 ?  91  HIS   B CA   1 
ATOM   5189 C C    . HIS   B 1 91  ? 47.273 -12.744 -5.861  1.00 10.43 ?  91  HIS   B C    1 
ATOM   5190 O O    . HIS   B 1 91  ? 47.035 -13.699 -6.612  1.00 11.10 ?  91  HIS   B O    1 
ATOM   5191 C CB   . HIS   B 1 91  ? 45.819 -10.842 -6.256  1.00 13.18 ?  91  HIS   B CB   1 
ATOM   5192 C CG   . HIS   B 1 91  ? 45.602 -9.442  -6.713  1.00 16.67 ?  91  HIS   B CG   1 
ATOM   5193 N ND1  . HIS   B 1 91  ? 46.192 -8.360  -6.098  1.00 19.32 ?  91  HIS   B ND1  1 
ATOM   5194 C CD2  . HIS   B 1 91  ? 44.829 -8.938  -7.701  1.00 19.27 ?  91  HIS   B CD2  1 
ATOM   5195 C CE1  . HIS   B 1 91  ? 45.810 -7.247  -6.702  1.00 20.17 ?  91  HIS   B CE1  1 
ATOM   5196 N NE2  . HIS   B 1 91  ? 44.975 -7.572  -7.674  1.00 20.36 ?  91  HIS   B NE2  1 
ATOM   5197 H H    . HIS   B 1 91  ? 47.314 -11.864 -8.247  1.00 13.43 ?  91  HIS   B H    1 
ATOM   5198 H HA   . HIS   B 1 91  ? 47.840 -10.760 -5.812  1.00 13.70 ?  91  HIS   B HA   1 
ATOM   5199 H HB2  . HIS   B 1 91  ? 45.257 -11.418 -6.792  1.00 15.83 ?  91  HIS   B HB2  1 
ATOM   5200 H HB3  . HIS   B 1 91  ? 45.547 -10.895 -5.322  1.00 15.83 ?  91  HIS   B HB3  1 
ATOM   5201 H HD1  . HIS   B 1 91  ? 46.733 -8.399  -5.426  1.00 23.20 ?  91  HIS   B HD1  1 
ATOM   5202 H HD2  . HIS   B 1 91  ? 44.305 -9.420  -8.293  1.00 23.14 ?  91  HIS   B HD2  1 
ATOM   5203 H HE1  . HIS   B 1 91  ? 46.078 -6.383  -6.474  1.00 24.22 ?  91  HIS   B HE1  1 
ATOM   5204 N N    . CYS   B 1 92  ? 47.471 -12.880 -4.559  1.00 10.47 ?  92  CYS   B N    1 
ATOM   5205 C CA   . CYS   B 1 92  ? 47.176 -14.122 -3.856  1.00 10.11 ?  92  CYS   B CA   1 
ATOM   5206 C C    . CYS   B 1 92  ? 45.958 -13.894 -2.969  1.00 9.82  ?  92  CYS   B C    1 
ATOM   5207 O O    . CYS   B 1 92  ? 45.956 -12.990 -2.121  1.00 10.80 ?  92  CYS   B O    1 
ATOM   5208 C CB   . CYS   B 1 92  ? 48.358 -14.579 -3.010  1.00 10.64 ?  92  CYS   B CB   1 
ATOM   5209 S SG   . CYS   B 1 92  ? 48.007 -16.115 -2.107  1.00 10.86 ?  92  CYS   B SG   1 
ATOM   5210 H H    . CYS   B 1 92  ? 47.779 -12.258 -4.046  1.00 12.58 ?  92  CYS   B H    1 
ATOM   5211 H HA   . CYS   B 1 92  ? 46.973 -14.815 -4.503  1.00 12.15 ?  92  CYS   B HA   1 
ATOM   5212 H HB2  . CYS   B 1 92  ? 49.119 -14.735 -3.586  1.00 12.78 ?  92  CYS   B HB2  1 
ATOM   5213 H HB3  . CYS   B 1 92  ? 48.562 -13.890 -2.359  1.00 12.78 ?  92  CYS   B HB3  1 
ATOM   5214 H HG   . CYS   B 1 92  ? 48.993 -16.425 -1.490  1.00 13.05 ?  92  CYS   B HG   1 
ATOM   5215 N N    . LEU   B 1 93  ? 44.923 -14.702 -3.183  1.00 9.78  ?  93  LEU   B N    1 
ATOM   5216 C CA   . LEU   B 1 93  ? 43.751 -14.717 -2.320  1.00 9.99  ?  93  LEU   B CA   1 
ATOM   5217 C C    . LEU   B 1 93  ? 43.982 -15.786 -1.259  1.00 9.45  ?  93  LEU   B C    1 
ATOM   5218 O O    . LEU   B 1 93  ? 43.934 -16.989 -1.555  1.00 10.20 ?  93  LEU   B O    1 
ATOM   5219 C CB   . LEU   B 1 93  ? 42.490 -15.004 -3.131  1.00 10.34 ?  93  LEU   B CB   1 
ATOM   5220 C CG   . LEU   B 1 93  ? 41.192 -15.035 -2.327  1.00 10.94 ?  93  LEU   B CG   1 
ATOM   5221 C CD1  . LEU   B 1 93  ? 40.840 -13.645 -1.834  1.00 11.49 ?  93  LEU   B CD1  1 
ATOM   5222 C CD2  . LEU   B 1 93  ? 40.067 -15.618 -3.165  1.00 11.45 ?  93  LEU   B CD2  1 
ATOM   5223 H H    . LEU   B 1 93  ? 44.880 -15.279 -3.831  1.00 11.75 ?  93  LEU   B H    1 
ATOM   5224 H HA   . LEU   B 1 93  ? 43.659 -13.853 -1.888  1.00 12.00 ?  93  LEU   B HA   1 
ATOM   5225 H HB2  . LEU   B 1 93  ? 42.396 -14.309 -3.807  1.00 12.42 ?  93  LEU   B HB2  1 
ATOM   5226 H HB3  . LEU   B 1 93  ? 42.589 -15.863 -3.562  1.00 12.42 ?  93  LEU   B HB3  1 
ATOM   5227 H HG   . LEU   B 1 93  ? 41.314 -15.602 -1.552  1.00 13.14 ?  93  LEU   B HG   1 
ATOM   5228 H HD11 . LEU   B 1 93  ? 39.986 -13.672 -1.386  1.00 13.81 ?  93  LEU   B HD11 1 
ATOM   5229 H HD12 . LEU   B 1 93  ? 41.531 -13.342 -1.219  1.00 13.81 ?  93  LEU   B HD12 1 
ATOM   5230 H HD13 . LEU   B 1 93  ? 40.798 -13.040 -2.596  1.00 13.81 ?  93  LEU   B HD13 1 
ATOM   5231 H HD21 . LEU   B 1 93  ? 39.252 -15.623 -2.637  1.00 13.75 ?  93  LEU   B HD21 1 
ATOM   5232 H HD22 . LEU   B 1 93  ? 39.944 -15.069 -3.956  1.00 13.75 ?  93  LEU   B HD22 1 
ATOM   5233 H HD23 . LEU   B 1 93  ? 40.300 -16.522 -3.422  1.00 13.75 ?  93  LEU   B HD23 1 
ATOM   5234 N N    . HIS   B 1 94  ? 44.247 -15.351 -0.034  1.00 9.55  ?  94  HIS   B N    1 
ATOM   5235 C CA   . HIS   B 1 94  ? 44.470 -16.259 1.084   1.00 9.63  ?  94  HIS   B CA   1 
ATOM   5236 C C    . HIS   B 1 94  ? 43.110 -16.617 1.662   1.00 10.27 ?  94  HIS   B C    1 
ATOM   5237 O O    . HIS   B 1 94  ? 42.436 -15.745 2.212   1.00 11.69 ?  94  HIS   B O    1 
ATOM   5238 C CB   . HIS   B 1 94  ? 45.342 -15.582 2.140   1.00 10.27 ?  94  HIS   B CB   1 
ATOM   5239 C CG   . HIS   B 1 94  ? 46.722 -15.276 1.666   1.00 10.39 ?  94  HIS   B CG   1 
ATOM   5240 N ND1  . HIS   B 1 94  ? 47.750 -16.191 1.748   1.00 10.64 ?  94  HIS   B ND1  1 
ATOM   5241 C CD2  . HIS   B 1 94  ? 47.229 -14.169 1.070   1.00 10.52 ?  94  HIS   B CD2  1 
ATOM   5242 C CE1  . HIS   B 1 94  ? 48.839 -15.642 1.233   1.00 10.72 ?  94  HIS   B CE1  1 
ATOM   5243 N NE2  . HIS   B 1 94  ? 48.551 -14.418 0.818   1.00 10.60 ?  94  HIS   B NE2  1 
ATOM   5244 H H    . HIS   B 1 94  ? 44.303 -14.515 0.177   1.00 11.47 ?  94  HIS   B H    1 
ATOM   5245 H HA   . HIS   B 1 94  ? 44.903 -17.065 0.771   1.00 11.57 ?  94  HIS   B HA   1 
ATOM   5246 H HB2  . HIS   B 1 94  ? 44.929 -14.750 2.401   1.00 12.34 ?  94  HIS   B HB2  1 
ATOM   5247 H HB3  . HIS   B 1 94  ? 45.416 -16.175 2.902   1.00 12.34 ?  94  HIS   B HB3  1 
ATOM   5248 H HD2  . HIS   B 1 94  ? 46.772 -13.387 0.873   1.00 12.64 ?  94  HIS   B HD2  1 
ATOM   5249 H HE1  . HIS   B 1 94  ? 49.676 -16.054 1.166   1.00 12.88 ?  94  HIS   B HE1  1 
ATOM   5250 H HE2  . HIS   B 1 94  ? 49.106 -13.875 0.445   1.00 12.74 ?  94  HIS   B HE2  1 
ATOM   5251 N N    . VAL   B 1 95  ? 42.683 -17.875 1.511   1.00 10.07 ?  95  VAL   B N    1 
ATOM   5252 C CA   . VAL   B 1 95  ? 41.353 -18.315 1.940   1.00 10.16 ?  95  VAL   B CA   1 
ATOM   5253 C C    . VAL   B 1 95  ? 41.525 -19.354 3.033   1.00 10.28 ?  95  VAL   B C    1 
ATOM   5254 O O    . VAL   B 1 95  ? 42.297 -20.305 2.871   1.00 10.95 ?  95  VAL   B O    1 
ATOM   5255 C CB   . VAL   B 1 95  ? 40.535 -18.916 0.779   1.00 10.42 ?  95  VAL   B CB   1 
ATOM   5256 C CG1  . VAL   B 1 95  ? 39.159 -19.381 1.263   1.00 11.72 ?  95  VAL   B CG1  1 
ATOM   5257 C CG2  . VAL   B 1 95  ? 40.407 -17.931 -0.356  1.00 11.10 ?  95  VAL   B CG2  1 
ATOM   5258 H H    . VAL   B 1 95  ? 43.148 -18.499 1.149   1.00 12.10 ?  95  VAL   B H    1 
ATOM   5259 H HA   . VAL   B 1 95  ? 40.859 -17.562 2.307   1.00 12.21 ?  95  VAL   B HA   1 
ATOM   5260 H HB   . VAL   B 1 95  ? 41.003 -19.691 0.441   1.00 12.52 ?  95  VAL   B HB   1 
ATOM   5261 H HG11 . VAL   B 1 95  ? 38.602 -19.581 0.490   1.00 14.08 ?  95  VAL   B HG11 1 
ATOM   5262 H HG12 . VAL   B 1 95  ? 39.262 -20.182 1.803   1.00 14.08 ?  95  VAL   B HG12 1 
ATOM   5263 H HG13 . VAL   B 1 95  ? 38.747 -18.678 1.787   1.00 14.08 ?  95  VAL   B HG13 1 
ATOM   5264 H HG21 . VAL   B 1 95  ? 39.833 -18.314 -1.040  1.00 13.34 ?  95  VAL   B HG21 1 
ATOM   5265 H HG22 . VAL   B 1 95  ? 40.014 -17.110 -0.018  1.00 13.34 ?  95  VAL   B HG22 1 
ATOM   5266 H HG23 . VAL   B 1 95  ? 41.285 -17.755 -0.720  1.00 13.34 ?  95  VAL   B HG23 1 
ATOM   5267 N N    . VAL   B 1 96  ? 40.792 -19.189 4.130   1.00 10.60 ?  96  VAL   B N    1 
ATOM   5268 C CA   . VAL   B 1 96  ? 40.873 -20.109 5.264   1.00 11.22 ?  96  VAL   B CA   1 
ATOM   5269 C C    . VAL   B 1 96  ? 39.687 -21.071 5.213   1.00 11.30 ?  96  VAL   B C    1 
ATOM   5270 O O    . VAL   B 1 96  ? 38.567 -20.720 5.594   1.00 11.87 ?  96  VAL   B O    1 
ATOM   5271 C CB   . VAL   B 1 96  ? 40.919 -19.364 6.601   1.00 11.73 ?  96  VAL   B CB   1 
ATOM   5272 C CG1  . VAL   B 1 96  ? 41.108 -20.357 7.742   1.00 12.46 ?  96  VAL   B CG1  1 
ATOM   5273 C CG2  . VAL   B 1 96  ? 42.033 -18.325 6.608   1.00 12.91 ?  96  VAL   B CG2  1 
ATOM   5274 H H    . VAL   B 1 96  ? 40.234 -18.548 4.244   1.00 12.74 ?  96  VAL   B H    1 
ATOM   5275 H HA   . VAL   B 1 96  ? 41.688 -20.632 5.193   1.00 13.48 ?  96  VAL   B HA   1 
ATOM   5276 H HB   . VAL   B 1 96  ? 40.075 -18.903 6.740   1.00 14.09 ?  96  VAL   B HB   1 
ATOM   5277 H HG11 . VAL   B 1 96  ? 41.288 -19.862 8.562   1.00 14.97 ?  96  VAL   B HG11 1 
ATOM   5278 H HG12 . VAL   B 1 96  ? 40.302 -20.881 7.847   1.00 14.97 ?  96  VAL   B HG12 1 
ATOM   5279 H HG13 . VAL   B 1 96  ? 41.861 -20.932 7.538   1.00 14.97 ?  96  VAL   B HG13 1 
ATOM   5280 H HG21 . VAL   B 1 96  ? 42.088 -17.916 7.489   1.00 15.50 ?  96  VAL   B HG21 1 
ATOM   5281 H HG22 . VAL   B 1 96  ? 42.874 -18.753 6.392   1.00 15.50 ?  96  VAL   B HG22 1 
ATOM   5282 H HG23 . VAL   B 1 96  ? 41.835 -17.638 5.946   1.00 15.50 ?  96  VAL   B HG23 1 
ATOM   5283 N N    . GLY   B 1 97  ? 39.929 -22.305 4.782   1.00 11.49 ?  97  GLY   B N    1 
ATOM   5284 C CA   . GLY   B 1 97  ? 38.953 -23.362 4.934   1.00 11.65 ?  97  GLY   B CA   1 
ATOM   5285 C C    . GLY   B 1 97  ? 39.064 -23.968 6.314   1.00 12.56 ?  97  GLY   B C    1 
ATOM   5286 O O    . GLY   B 1 97  ? 40.104 -23.847 6.974   1.00 12.97 ?  97  GLY   B O    1 
ATOM   5287 H H    . GLY   B 1 97  ? 40.663 -22.545 4.394   1.00 13.80 ?  97  GLY   B H    1 
ATOM   5288 H HA2  . GLY   B 1 97  ? 38.064 -22.993 4.809   1.00 13.99 ?  97  GLY   B HA2  1 
ATOM   5289 H HA3  . GLY   B 1 97  ? 39.108 -24.044 4.263   1.00 13.99 ?  97  GLY   B HA3  1 
ATOM   5290 N N    . PRO   B 1 98  ? 38.017 -24.656 6.770   1.00 12.93 ?  98  PRO   B N    1 
ATOM   5291 C CA   . PRO   B 1 98  ? 38.106 -25.351 8.058   1.00 13.79 ?  98  PRO   B CA   1 
ATOM   5292 C C    . PRO   B 1 98  ? 39.134 -26.471 8.016   1.00 13.30 ?  98  PRO   B C    1 
ATOM   5293 O O    . PRO   B 1 98  ? 39.241 -27.207 7.036   1.00 13.48 ?  98  PRO   B O    1 
ATOM   5294 C CB   . PRO   B 1 98  ? 36.690 -25.899 8.259   1.00 14.00 ?  98  PRO   B CB   1 
ATOM   5295 C CG   . PRO   B 1 98  ? 36.144 -26.044 6.879   1.00 13.70 ?  98  PRO   B CG   1 
ATOM   5296 C CD   . PRO   B 1 98  ? 36.707 -24.855 6.129   1.00 12.94 ?  98  PRO   B CD   1 
ATOM   5297 H HA   . PRO   B 1 98  ? 38.328 -24.729 8.762   1.00 16.56 ?  98  PRO   B HA   1 
ATOM   5298 H HB2  . PRO   B 1 98  ? 36.734 -26.761 8.705   1.00 16.81 ?  98  PRO   B HB2  1 
ATOM   5299 H HB3  . PRO   B 1 98  ? 36.167 -25.268 8.771   1.00 16.81 ?  98  PRO   B HB3  1 
ATOM   5300 H HG2  . PRO   B 1 98  ? 36.457 -26.880 6.489   1.00 16.46 ?  98  PRO   B HG2  1 
ATOM   5301 H HG3  . PRO   B 1 98  ? 35.179 -26.014 6.903   1.00 16.46 ?  98  PRO   B HG3  1 
ATOM   5302 H HD2  . PRO   B 1 98  ? 36.813 -25.070 5.184   1.00 15.54 ?  98  PRO   B HD2  1 
ATOM   5303 H HD3  . PRO   B 1 98  ? 36.150 -24.076 6.257   1.00 15.54 ?  98  PRO   B HD3  1 
ATOM   5304 N N    . ASN   B 1 99  ? 39.885 -26.595 9.103   1.00 14.14 ?  99  ASN   B N    1 
ATOM   5305 C CA   . ASN   B 1 99  ? 40.859 -27.670 9.271   1.00 14.67 ?  99  ASN   B CA   1 
ATOM   5306 C C    . ASN   B 1 99  ? 40.219 -28.754 10.137  1.00 16.50 ?  99  ASN   B C    1 
ATOM   5307 O O    . ASN   B 1 99  ? 40.121 -28.613 11.358  1.00 17.28 ?  99  ASN   B O    1 
ATOM   5308 C CB   . ASN   B 1 99  ? 42.130 -27.116 9.898   1.00 15.13 ?  99  ASN   B CB   1 
ATOM   5309 C CG   . ASN   B 1 99  ? 43.256 -28.123 9.910   1.00 15.92 ?  99  ASN   B CG   1 
ATOM   5310 O OD1  . ASN   B 1 99  ? 43.020 -29.321 10.065  1.00 17.17 ?  99  ASN   B OD1  1 
ATOM   5311 N ND2  . ASN   B 1 99  ? 44.487 -27.647 9.741   1.00 16.43 ?  99  ASN   B ND2  1 
ATOM   5312 H H    . ASN   B 1 99  ? 39.855 -26.052 9.769   1.00 16.99 ?  99  ASN   B H    1 
ATOM   5313 H HA   . ASN   B 1 99  ? 41.082 -28.056 8.413   1.00 17.62 ?  99  ASN   B HA   1 
ATOM   5314 H HB2  . ASN   B 1 99  ? 42.422 -26.344 9.395   1.00 18.17 ?  99  ASN   B HB2  1 
ATOM   5315 H HB3  . ASN   B 1 99  ? 41.944 -26.860 10.819  1.00 18.17 ?  99  ASN   B HB3  1 
ATOM   5316 H HD21 . ASN   B 1 99  ? 45.161 -28.179 9.743   1.00 19.73 ?  99  ASN   B HD21 1 
ATOM   5317 H HD22 . ASN   B 1 99  ? 44.607 -26.800 9.636   1.00 19.73 ?  99  ASN   B HD22 1 
ATOM   5318 N N    A VAL   B 1 100 ? 39.760 -29.831 9.493   0.78 18.26 ?  100 VAL   B N    1 
ATOM   5319 N N    B VAL   B 1 100 ? 39.772 -29.835 9.490   0.22 18.47 ?  100 VAL   B N    1 
ATOM   5320 C CA   A VAL   B 1 100 ? 39.133 -30.932 10.222  0.78 21.23 ?  100 VAL   B CA   1 
ATOM   5321 C CA   B VAL   B 1 100 ? 39.141 -30.940 10.210  0.22 20.80 ?  100 VAL   B CA   1 
ATOM   5322 C C    A VAL   B 1 100 ? 40.126 -31.604 11.163  0.78 21.64 ?  100 VAL   B C    1 
ATOM   5323 C C    B VAL   B 1 100 ? 40.127 -31.605 11.158  0.22 21.53 ?  100 VAL   B C    1 
ATOM   5324 O O    A VAL   B 1 100 ? 39.739 -32.126 12.215  0.78 22.40 ?  100 VAL   B O    1 
ATOM   5325 O O    B VAL   B 1 100 ? 39.738 -32.109 12.219  0.22 21.80 ?  100 VAL   B O    1 
ATOM   5326 C CB   A VAL   B 1 100 ? 38.499 -31.933 9.233   0.78 24.09 ?  100 VAL   B CB   1 
ATOM   5327 C CB   B VAL   B 1 100 ? 38.524 -31.943 9.212   0.22 22.38 ?  100 VAL   B CB   1 
ATOM   5328 C CG1  A VAL   B 1 100 ? 38.027 -33.187 9.959   0.78 25.28 ?  100 VAL   B CG1  1 
ATOM   5329 C CG1  B VAL   B 1 100 ? 37.980 -33.169 9.939   0.22 23.01 ?  100 VAL   B CG1  1 
ATOM   5330 C CG2  A VAL   B 1 100 ? 37.342 -31.284 8.485   0.78 24.95 ?  100 VAL   B CG2  1 
ATOM   5331 C CG2  B VAL   B 1 100 ? 37.424 -31.275 8.402   0.22 22.89 ?  100 VAL   B CG2  1 
ATOM   5332 H H    A VAL   B 1 100 ? 39.787 -29.939 8.640   0.78 21.92 ?  100 VAL   B H    1 
ATOM   5333 H H    B VAL   B 1 100 ? 39.821 -29.949 8.641   0.22 22.17 ?  100 VAL   B H    1 
ATOM   5334 H HA   A VAL   B 1 100 ? 38.414 -30.573 10.767  0.78 25.49 ?  100 VAL   B HA   1 
ATOM   5335 H HA   B VAL   B 1 100 ? 38.417 -30.587 10.747  0.22 24.97 ?  100 VAL   B HA   1 
ATOM   5336 H HB   A VAL   B 1 100 ? 39.165 -32.203 8.585   0.78 28.92 ?  100 VAL   B HB   1 
ATOM   5337 H HB   B VAL   B 1 100 ? 39.209 -32.244 8.596   0.22 26.87 ?  100 VAL   B HB   1 
ATOM   5338 H HG11 A VAL   B 1 100 ? 37.435 -33.687 9.373   0.78 30.36 ?  100 VAL   B HG11 1 
ATOM   5339 H HG11 B VAL   B 1 100 ? 37.416 -33.673 9.329   0.22 27.63 ?  100 VAL   B HG11 1 
ATOM   5340 H HG12 A VAL   B 1 100 ? 38.795 -33.734 10.191  0.78 30.36 ?  100 VAL   B HG12 1 
ATOM   5341 H HG12 B VAL   B 1 100 ? 38.721 -33.723 10.231  0.22 27.63 ?  100 VAL   B HG12 1 
ATOM   5342 H HG13 A VAL   B 1 100 ? 37.549 -32.929 10.763  0.78 30.36 ?  100 VAL   B HG13 1 
ATOM   5343 H HG13 B VAL   B 1 100 ? 37.459 -32.879 10.703  0.22 27.63 ?  100 VAL   B HG13 1 
ATOM   5344 H HG21 A VAL   B 1 100 ? 36.958 -31.933 7.873   0.78 29.96 ?  100 VAL   B HG21 1 
ATOM   5345 H HG21 B VAL   B 1 100 ? 37.030 -31.929 7.804   0.22 27.48 ?  100 VAL   B HG21 1 
ATOM   5346 H HG22 A VAL   B 1 100 ? 36.670 -31.001 9.126   0.78 29.96 ?  100 VAL   B HG22 1 
ATOM   5347 H HG22 B VAL   B 1 100 ? 36.749 -30.934 9.010   0.22 27.48 ?  100 VAL   B HG22 1 
ATOM   5348 H HG23 A VAL   B 1 100 ? 37.674 -30.520 7.993   0.78 29.96 ?  100 VAL   B HG23 1 
ATOM   5349 H HG23 B VAL   B 1 100 ? 37.809 -30.547 7.891   0.22 27.48 ?  100 VAL   B HG23 1 
ATOM   5350 N N    . ASN   B 1 101 ? 41.413 -31.626 10.798  1.00 22.13 ?  101 ASN   B N    1 
ATOM   5351 C CA   . ASN   B 1 101 ? 42.432 -32.171 11.694  1.00 24.58 ?  101 ASN   B CA   1 
ATOM   5352 C C    . ASN   B 1 101 ? 42.597 -31.337 12.960  1.00 26.86 ?  101 ASN   B C    1 
ATOM   5353 O O    . ASN   B 1 101 ? 43.193 -31.819 13.932  1.00 27.89 ?  101 ASN   B O    1 
ATOM   5354 C CB   . ASN   B 1 101 ? 43.772 -32.305 10.966  1.00 24.77 ?  101 ASN   B CB   1 
ATOM   5355 C CG   . ASN   B 1 101 ? 43.763 -33.413 9.929   1.00 24.38 ?  101 ASN   B CG   1 
ATOM   5356 O OD1  . ASN   B 1 101 ? 43.079 -34.420 10.092  1.00 25.45 ?  101 ASN   B OD1  1 
ATOM   5357 N ND2  . ASN   B 1 101 ? 44.524 -33.231 8.858   1.00 24.38 ?  101 ASN   B ND2  1 
ATOM   5358 H H    A ASN   B 1 101 ? 41.710 -31.350 10.040  0.78 26.57 ?  101 ASN   B H    1 
ATOM   5359 H H    B ASN   B 1 101 ? 41.713 -31.341 10.045  0.22 26.57 ?  101 ASN   B H    1 
ATOM   5360 H HA   . ASN   B 1 101 ? 42.158 -33.056 11.967  1.00 29.51 ?  101 ASN   B HA   1 
ATOM   5361 H HB2  . ASN   B 1 101 ? 43.979 -31.474 10.512  1.00 29.74 ?  101 ASN   B HB2  1 
ATOM   5362 H HB3  . ASN   B 1 101 ? 44.465 -32.509 11.615  1.00 29.74 ?  101 ASN   B HB3  1 
ATOM   5363 H HD21 . ASN   B 1 101 ? 44.552 -33.831 8.242   1.00 29.27 ?  101 ASN   B HD21 1 
ATOM   5364 H HD22 . ASN   B 1 101 ? 44.988 -32.510 8.776   1.00 29.27 ?  101 ASN   B HD22 1 
ATOM   5365 N N    A LYS   B 1 102 ? 42.109 -30.095 12.957  0.78 28.46 ?  102 LYS   B N    1 
ATOM   5366 N N    B LYS   B 1 102 ? 42.080 -30.107 12.971  0.22 28.42 ?  102 LYS   B N    1 
ATOM   5367 C CA   A LYS   B 1 102 ? 42.108 -29.233 14.132  0.78 30.66 ?  102 LYS   B CA   1 
ATOM   5368 C CA   B LYS   B 1 102 ? 42.023 -29.283 14.171  0.22 30.02 ?  102 LYS   B CA   1 
ATOM   5369 C C    A LYS   B 1 102 ? 40.741 -29.174 14.805  0.78 30.20 ?  102 LYS   B C    1 
ATOM   5370 C C    B LYS   B 1 102 ? 40.643 -29.282 14.815  0.22 29.58 ?  102 LYS   B C    1 
ATOM   5371 O O    A LYS   B 1 102 ? 40.542 -28.358 15.710  0.78 31.20 ?  102 LYS   B O    1 
ATOM   5372 O O    B LYS   B 1 102 ? 40.430 -28.557 15.792  0.22 29.79 ?  102 LYS   B O    1 
ATOM   5373 C CB   A LYS   B 1 102 ? 42.534 -27.812 13.754  0.78 33.89 ?  102 LYS   B CB   1 
ATOM   5374 C CB   B LYS   B 1 102 ? 42.430 -27.839 13.849  0.22 32.10 ?  102 LYS   B CB   1 
ATOM   5375 C CG   A LYS   B 1 102 ? 44.007 -27.634 13.420  0.78 37.03 ?  102 LYS   B CG   1 
ATOM   5376 C CG   B LYS   B 1 102 ? 43.886 -27.660 13.451  0.22 33.97 ?  102 LYS   B CG   1 
ATOM   5377 C CD   A LYS   B 1 102 ? 44.290 -26.186 13.034  0.78 39.92 ?  102 LYS   B CD   1 
ATOM   5378 C CD   B LYS   B 1 102 ? 44.157 -26.222 13.041  0.22 35.61 ?  102 LYS   B CD   1 
ATOM   5379 C CE   A LYS   B 1 102 ? 45.768 -25.937 12.777  0.78 42.12 ?  102 LYS   B CE   1 
ATOM   5380 C CE   B LYS   B 1 102 ? 45.627 -25.990 12.737  0.22 36.82 ?  102 LYS   B CE   1 
ATOM   5381 N NZ   A LYS   B 1 102 ? 46.025 -24.524 12.371  0.78 43.39 ?  102 LYS   B NZ   1 
ATOM   5382 N NZ   B LYS   B 1 102 ? 45.878 -24.592 12.288  0.22 37.48 ?  102 LYS   B NZ   1 
ATOM   5383 H H    A LYS   B 1 102 ? 41.761 -29.719 12.264  0.78 34.17 ?  102 LYS   B H    1 
ATOM   5384 H H    B LYS   B 1 102 ? 41.747 -29.718 12.277  0.22 34.12 ?  102 LYS   B H    1 
ATOM   5385 H HA   A LYS   B 1 102 ? 42.756 -29.575 14.768  0.78 36.80 ?  102 LYS   B HA   1 
ATOM   5386 H HA   B LYS   B 1 102 ? 42.654 -29.631 14.820  0.22 36.04 ?  102 LYS   B HA   1 
ATOM   5387 H HB2  A LYS   B 1 102 ? 42.024 -27.534 12.979  0.78 40.69 ?  102 LYS   B HB2  1 
ATOM   5388 H HB2  B LYS   B 1 102 ? 41.885 -27.518 13.115  0.22 38.53 ?  102 LYS   B HB2  1 
ATOM   5389 H HB3  A LYS   B 1 102 ? 42.335 -27.223 14.500  0.78 40.69 ?  102 LYS   B HB3  1 
ATOM   5390 H HB3  B LYS   B 1 102 ? 42.274 -27.290 14.635  0.22 38.53 ?  102 LYS   B HB3  1 
ATOM   5391 H HG2  A LYS   B 1 102 ? 44.546 -27.855 14.196  0.78 44.45 ?  102 LYS   B HG2  1 
ATOM   5392 H HG2  B LYS   B 1 102 ? 44.458 -27.875 14.205  0.22 40.77 ?  102 LYS   B HG2  1 
ATOM   5393 H HG3  A LYS   B 1 102 ? 44.241 -28.203 12.670  0.78 44.45 ?  102 LYS   B HG3  1 
ATOM   5394 H HG3  B LYS   B 1 102 ? 44.090 -28.236 12.698  0.22 40.77 ?  102 LYS   B HG3  1 
ATOM   5395 H HD2  A LYS   B 1 102 ? 43.803 -25.971 12.223  0.78 47.92 ?  102 LYS   B HD2  1 
ATOM   5396 H HD2  B LYS   B 1 102 ? 43.646 -26.015 12.243  0.22 42.75 ?  102 LYS   B HD2  1 
ATOM   5397 H HD3  A LYS   B 1 102 ? 44.007 -25.603 13.756  0.78 47.92 ?  102 LYS   B HD3  1 
ATOM   5398 H HD3  B LYS   B 1 102 ? 43.900 -25.629 13.765  0.22 42.75 ?  102 LYS   B HD3  1 
ATOM   5399 H HE2  A LYS   B 1 102 ? 46.268 -26.116 13.589  0.78 50.56 ?  102 LYS   B HE2  1 
ATOM   5400 H HE2  B LYS   B 1 102 ? 46.149 -26.150 13.539  0.22 44.19 ?  102 LYS   B HE2  1 
ATOM   5401 H HE3  A LYS   B 1 102 ? 46.070 -26.518 12.062  0.78 50.56 ?  102 LYS   B HE3  1 
ATOM   5402 H HE3  B LYS   B 1 102 ? 45.906 -26.591 12.029  0.22 44.19 ?  102 LYS   B HE3  1 
ATOM   5403 H HZ1  A LYS   B 1 102 ? 46.895 -24.402 12.226  0.78 52.08 ?  102 LYS   B HZ1  1 
ATOM   5404 H HZ1  B LYS   B 1 102 ? 46.744 -24.479 12.116  0.22 44.99 ?  102 LYS   B HZ1  1 
ATOM   5405 H HZ2  A LYS   B 1 102 ? 45.578 -24.335 11.624  0.78 52.08 ?  102 LYS   B HZ2  1 
ATOM   5406 H HZ2  B LYS   B 1 102 ? 45.411 -24.422 11.550  0.22 44.99 ?  102 LYS   B HZ2  1 
ATOM   5407 H HZ3  A LYS   B 1 102 ? 45.759 -23.969 13.014  0.78 52.08 ?  102 LYS   B HZ3  1 
ATOM   5408 H HZ3  B LYS   B 1 102 ? 45.632 -24.020 12.924  0.22 44.99 ?  102 LYS   B HZ3  1 
ATOM   5409 N N    A GLY   B 1 103 ? 39.792 -29.998 14.370  0.78 29.15 ?  103 GLY   B N    1 
ATOM   5410 N N    B GLY   B 1 103 ? 39.703 -30.068 14.295  0.22 28.93 ?  103 GLY   B N    1 
ATOM   5411 C CA   A GLY   B 1 103 ? 38.470 -30.024 14.960  0.78 28.85 ?  103 GLY   B CA   1 
ATOM   5412 C CA   B GLY   B 1 103 ? 38.370 -30.124 14.862  0.22 28.35 ?  103 GLY   B CA   1 
ATOM   5413 C C    A GLY   B 1 103 ? 37.517 -28.963 14.455  0.78 27.80 ?  103 GLY   B C    1 
ATOM   5414 C C    B GLY   B 1 103 ? 37.446 -29.006 14.441  0.22 27.52 ?  103 GLY   B C    1 
ATOM   5415 O O    A GLY   B 1 103 ? 36.403 -28.853 14.982  0.78 28.62 ?  103 GLY   B O    1 
ATOM   5416 O O    B GLY   B 1 103 ? 36.416 -28.795 15.090  0.22 27.77 ?  103 GLY   B O    1 
ATOM   5417 H H    A GLY   B 1 103 ? 39.897 -30.555 13.727  0.78 35.00 ?  103 GLY   B H    1 
ATOM   5418 H H    B GLY   B 1 103 ? 39.817 -30.583 13.615  0.22 34.73 ?  103 GLY   B H    1 
ATOM   5419 H HA2  A GLY   B 1 103 ? 38.069 -30.890 14.786  0.78 34.64 ?  103 GLY   B HA2  1 
ATOM   5420 H HA2  B GLY   B 1 103 ? 37.958 -30.964 14.610  0.22 34.04 ?  103 GLY   B HA2  1 
ATOM   5421 H HA3  A GLY   B 1 103 ? 38.555 -29.926 15.924  0.78 34.64 ?  103 GLY   B HA3  1 
ATOM   5422 H HA3  B GLY   B 1 103 ? 38.440 -30.104 15.829  0.22 34.04 ?  103 GLY   B HA3  1 
ATOM   5423 N N    A GLU   B 1 104 ? 37.909 -28.185 13.450  0.78 25.94 ?  104 GLU   B N    1 
ATOM   5424 N N    B GLU   B 1 104 ? 37.773 -28.283 13.374  0.22 26.28 ?  104 GLU   B N    1 
ATOM   5425 C CA   A GLU   B 1 104 ? 37.070 -27.096 12.975  0.78 24.26 ?  104 GLU   B CA   1 
ATOM   5426 C CA   B GLU   B 1 104 ? 36.949 -27.169 12.934  0.22 25.12 ?  104 GLU   B CA   1 
ATOM   5427 C C    A GLU   B 1 104 ? 35.899 -27.635 12.154  0.78 25.10 ?  104 GLU   B C    1 
ATOM   5428 C C    B GLU   B 1 104 ? 35.790 -27.664 12.075  0.22 25.16 ?  104 GLU   B C    1 
ATOM   5429 O O    A GLU   B 1 104 ? 35.947 -28.731 11.586  0.78 26.23 ?  104 GLU   B O    1 
ATOM   5430 O O    B GLU   B 1 104 ? 35.881 -28.692 11.398  0.22 25.24 ?  104 GLU   B O    1 
ATOM   5431 C CB   A GLU   B 1 104 ? 37.909 -26.097 12.180  0.78 22.78 ?  104 GLU   B CB   1 
ATOM   5432 C CB   B GLU   B 1 104 ? 37.800 -26.157 12.168  0.22 24.14 ?  104 GLU   B CB   1 
ATOM   5433 C CG   A GLU   B 1 104 ? 39.025 -25.500 13.027  0.78 21.70 ?  104 GLU   B CG   1 
ATOM   5434 C CG   B GLU   B 1 104 ? 38.920 -25.574 13.020  0.22 23.38 ?  104 GLU   B CG   1 
ATOM   5435 C CD   A GLU   B 1 104 ? 39.969 -24.601 12.261  0.78 20.43 ?  104 GLU   B CD   1 
ATOM   5436 C CD   B GLU   B 1 104 ? 39.851 -24.662 12.245  0.22 22.78 ?  104 GLU   B CD   1 
ATOM   5437 O OE1  A GLU   B 1 104 ? 39.970 -24.620 11.011  0.78 18.51 ?  104 GLU   B OE1  1 
ATOM   5438 O OE1  B GLU   B 1 104 ? 39.781 -24.642 10.998  0.22 22.41 ?  104 GLU   B OE1  1 
ATOM   5439 O OE2  A GLU   B 1 104 ? 40.720 -23.865 12.932  0.78 21.50 -1 104 GLU   B OE2  1 
ATOM   5440 O OE2  B GLU   B 1 104 ? 40.657 -23.962 12.892  0.22 22.79 -1 104 GLU   B OE2  1 
ATOM   5441 H H    A GLU   B 1 104 ? 38.659 -28.264 13.037  0.78 31.14 ?  104 GLU   B H    1 
ATOM   5442 H H    B GLU   B 1 104 ? 38.472 -28.416 12.891  0.22 31.55 ?  104 GLU   B H    1 
ATOM   5443 H HA   A GLU   B 1 104 ? 36.708 -26.628 13.746  0.78 29.13 ?  104 GLU   B HA   1 
ATOM   5444 H HA   B GLU   B 1 104 ? 36.579 -26.722 13.710  0.22 30.16 ?  104 GLU   B HA   1 
ATOM   5445 H HB2  A GLU   B 1 104 ? 38.310 -26.546 11.422  0.78 27.35 ?  104 GLU   B HB2  1 
ATOM   5446 H HB2  B GLU   B 1 104 ? 38.202 -26.594 11.402  0.22 28.99 ?  104 GLU   B HB2  1 
ATOM   5447 H HB3  A GLU   B 1 104 ? 37.338 -25.372 11.878  0.78 27.35 ?  104 GLU   B HB3  1 
ATOM   5448 H HB3  B GLU   B 1 104 ? 37.235 -25.425 11.874  0.22 28.99 ?  104 GLU   B HB3  1 
ATOM   5449 H HG2  A GLU   B 1 104 ? 38.633 -24.970 13.740  0.78 26.05 ?  104 GLU   B HG2  1 
ATOM   5450 H HG2  B GLU   B 1 104 ? 38.529 -25.057 13.743  0.22 28.07 ?  104 GLU   B HG2  1 
ATOM   5451 H HG3  A GLU   B 1 104 ? 39.556 -26.216 13.407  0.78 26.05 ?  104 GLU   B HG3  1 
ATOM   5452 H HG3  B GLU   B 1 104 ? 39.449 -26.301 13.387  0.22 28.07 ?  104 GLU   B HG3  1 
ATOM   5453 N N    A ASP   B 1 105 ? 34.832 -26.841 12.101  0.78 25.24 ?  105 ASP   B N    1 
ATOM   5454 N N    B ASP   B 1 105 ? 34.691 -26.914 12.111  0.22 25.22 ?  105 ASP   B N    1 
ATOM   5455 C CA   A ASP   B 1 105 ? 33.550 -27.297 11.578  0.78 25.91 ?  105 ASP   B CA   1 
ATOM   5456 C CA   B ASP   B 1 105 ? 33.437 -27.371 11.523  0.22 25.51 ?  105 ASP   B CA   1 
ATOM   5457 C C    A ASP   B 1 105 ? 33.585 -27.341 10.053  0.78 24.04 ?  105 ASP   B C    1 
ATOM   5458 C C    B ASP   B 1 105 ? 33.540 -27.391 10.002  0.22 24.72 ?  105 ASP   B C    1 
ATOM   5459 O O    A ASP   B 1 105 ? 33.724 -26.303 9.396   0.78 23.36 ?  105 ASP   B O    1 
ATOM   5460 O O    B ASP   B 1 105 ? 33.763 -26.353 9.370   0.22 24.30 ?  105 ASP   B O    1 
ATOM   5461 C CB   A ASP   B 1 105 ? 32.442 -26.364 12.067  0.78 29.26 ?  105 ASP   B CB   1 
ATOM   5462 C CB   B ASP   B 1 105 ? 32.295 -26.461 11.971  0.22 26.56 ?  105 ASP   B CB   1 
ATOM   5463 C CG   A ASP   B 1 105 ? 31.057 -26.826 11.649  0.78 32.17 ?  105 ASP   B CG   1 
ATOM   5464 C CG   B ASP   B 1 105 ? 30.929 -27.047 11.663  0.22 27.55 ?  105 ASP   B CG   1 
ATOM   5465 O OD1  A ASP   B 1 105 ? 30.945 -27.888 11.001  0.78 32.57 ?  105 ASP   B OD1  1 
ATOM   5466 O OD1  B ASP   B 1 105 ? 30.864 -28.047 10.917  0.22 27.79 ?  105 ASP   B OD1  1 
ATOM   5467 O OD2  A ASP   B 1 105 ? 30.075 -26.123 11.972  0.78 33.92 -1 105 ASP   B OD2  1 
ATOM   5468 O OD2  B ASP   B 1 105 ? 29.921 -26.514 12.174  0.22 27.81 -1 105 ASP   B OD2  1 
ATOM   5469 H H    A ASP   B 1 105 ? 34.834 -26.019 12.356  0.78 30.30 ?  105 ASP   B H    1 
ATOM   5470 H H    B ASP   B 1 105 ? 34.647 -26.134 12.469  0.22 30.28 ?  105 ASP   B H    1 
ATOM   5471 H HA   A ASP   B 1 105 ? 33.369 -28.191 11.909  0.78 31.11 ?  105 ASP   B HA   1 
ATOM   5472 H HA   B ASP   B 1 105 ? 33.246 -28.271 11.828  0.22 30.63 ?  105 ASP   B HA   1 
ATOM   5473 H HB2  A ASP   B 1 105 ? 32.482 -26.311 13.038  0.78 35.12 ?  105 ASP   B HB2  1 
ATOM   5474 H HB2  B ASP   B 1 105 ? 32.359 -26.322 12.931  0.22 31.89 ?  105 ASP   B HB2  1 
ATOM   5475 H HB3  A ASP   B 1 105 ? 32.579 -25.486 11.683  0.78 35.12 ?  105 ASP   B HB3  1 
ATOM   5476 H HB3  B ASP   B 1 105 ? 32.367 -25.610 11.510  0.22 31.89 ?  105 ASP   B HB3  1 
ATOM   5477 N N    A ILE   B 1 106 ? 33.442 -28.546 9.494   0.78 23.35 ?  106 ILE   B N    1 
ATOM   5478 N N    B ILE   B 1 106 ? 33.368 -28.579 9.416   0.22 24.32 ?  106 ILE   B N    1 
ATOM   5479 C CA   A ILE   B 1 106 ? 33.429 -28.724 8.045   0.78 22.24 ?  106 ILE   B CA   1 
ATOM   5480 C CA   B ILE   B 1 106 ? 33.388 -28.730 7.966   0.22 23.95 ?  106 ILE   B CA   1 
ATOM   5481 C C    A ILE   B 1 106 ? 32.330 -27.901 7.377   0.78 20.97 ?  106 ILE   B C    1 
ATOM   5482 C C    B ILE   B 1 106 ? 32.296 -27.903 7.300   0.22 23.56 ?  106 ILE   B C    1 
ATOM   5483 O O    A ILE   B 1 106 ? 32.428 -27.582 6.186   0.78 19.80 ?  106 ILE   B O    1 
ATOM   5484 O O    B ILE   B 1 106 ? 32.390 -27.601 6.105   0.22 23.28 ?  106 ILE   B O    1 
ATOM   5485 C CB   A ILE   B 1 106 ? 33.327 -30.232 7.716   0.78 23.44 ?  106 ILE   B CB   1 
ATOM   5486 C CB   B ILE   B 1 106 ? 33.287 -30.229 7.601   0.22 24.18 ?  106 ILE   B CB   1 
ATOM   5487 C CG1  A ILE   B 1 106 ? 33.571 -30.487 6.229   0.78 23.90 ?  106 ILE   B CG1  1 
ATOM   5488 C CG1  B ILE   B 1 106 ? 33.555 -30.453 6.110   0.22 24.16 ?  106 ILE   B CG1  1 
ATOM   5489 C CG2  A ILE   B 1 106 ? 31.973 -30.790 8.145   0.78 24.59 ?  106 ILE   B CG2  1 
ATOM   5490 C CG2  B ILE   B 1 106 ? 31.922 -30.785 7.986   0.22 24.55 ?  106 ILE   B CG2  1 
ATOM   5491 C CD1  A ILE   B 1 106 ? 34.929 -30.029 5.757   0.78 24.06 ?  106 ILE   B CD1  1 
ATOM   5492 C CD1  B ILE   B 1 106 ? 34.923 -29.993 5.662   0.22 24.13 ?  106 ILE   B CD1  1 
ATOM   5493 H H    A ILE   B 1 106 ? 33.364 -29.276 9.940   0.78 28.03 ?  106 ILE   B H    1 
ATOM   5494 H H    B ILE   B 1 106 ? 33.248 -29.314 9.842   0.22 29.20 ?  106 ILE   B H    1 
ATOM   5495 H HA   A ILE   B 1 106 ? 34.276 -28.410 7.702   0.78 26.70 ?  106 ILE   B HA   1 
ATOM   5496 H HA   B ILE   B 1 106 ? 34.238 -28.402 7.641   0.22 28.76 ?  106 ILE   B HA   1 
ATOM   5497 H HB   A ILE   B 1 106 ? 34.012 -30.702 8.220   0.78 28.15 ?  106 ILE   B HB   1 
ATOM   5498 H HB   B ILE   B 1 106 ? 33.961 -30.711 8.104   0.22 29.03 ?  106 ILE   B HB   1 
ATOM   5499 H HG12 A ILE   B 1 106 ? 33.508 -31.444 6.062   0.78 28.69 ?  106 ILE   B HG12 1 
ATOM   5500 H HG12 B ILE   B 1 106 ? 33.489 -31.404 5.921   0.22 29.01 ?  106 ILE   B HG12 1 
ATOM   5501 H HG13 A ILE   B 1 106 ? 32.900 -30.020 5.714   0.78 28.69 ?  106 ILE   B HG13 1 
ATOM   5502 H HG13 B ILE   B 1 106 ? 32.894 -29.970 5.593   0.22 29.01 ?  106 ILE   B HG13 1 
ATOM   5503 H HG21 A ILE   B 1 106 ? 31.980 -31.756 8.041   0.78 29.52 ?  106 ILE   B HG21 1 
ATOM   5504 H HG21 B ILE   B 1 106 ? 31.935 -31.749 7.883   0.22 29.47 ?  106 ILE   B HG21 1 
ATOM   5505 H HG22 A ILE   B 1 106 ? 31.817 -30.563 9.077   0.78 29.52 ?  106 ILE   B HG22 1 
ATOM   5506 H HG22 B ILE   B 1 106 ? 31.738 -30.554 8.910   0.22 29.47 ?  106 ILE   B HG22 1 
ATOM   5507 H HG23 A ILE   B 1 106 ? 31.278 -30.405 7.591   0.78 29.52 ?  106 ILE   B HG23 1 
ATOM   5508 H HG23 B ILE   B 1 106 ? 31.247 -30.400 7.407   0.22 29.47 ?  106 ILE   B HG23 1 
ATOM   5509 H HD11 A ILE   B 1 106 ? 35.121 -30.443 4.902   0.78 28.88 ?  106 ILE   B HD11 1 
ATOM   5510 H HD11 B ILE   B 1 106 ? 35.115 -30.377 4.793   0.22 28.97 ?  106 ILE   B HD11 1 
ATOM   5511 H HD12 A ILE   B 1 106 ? 34.922 -29.064 5.663   0.78 28.88 ?  106 ILE   B HD12 1 
ATOM   5512 H HD12 B ILE   B 1 106 ? 34.928 -29.025 5.604   0.22 28.97 ?  106 ILE   B HD12 1 
ATOM   5513 H HD13 A ILE   B 1 106 ? 35.598 -30.295 6.409   0.78 28.88 ?  106 ILE   B HD13 1 
ATOM   5514 H HD13 B ILE   B 1 106 ? 35.583 -30.291 6.308   0.22 28.97 ?  106 ILE   B HD13 1 
ATOM   5515 N N    A GLN   B 1 107 ? 31.288 -27.529 8.122   0.78 22.07 ?  107 GLN   B N    1 
ATOM   5516 N N    B GLN   B 1 107 ? 31.257 -27.525 8.047   0.22 23.64 ?  107 GLN   B N    1 
ATOM   5517 C CA   A GLN   B 1 107 ? 30.210 -26.728 7.551   0.78 22.93 ?  107 GLN   B CA   1 
ATOM   5518 C CA   B GLN   B 1 107 ? 30.185 -26.709 7.488   0.22 23.66 ?  107 GLN   B CA   1 
ATOM   5519 C C    A GLN   B 1 107 ? 30.698 -25.382 7.020   0.78 20.82 ?  107 GLN   B C    1 
ATOM   5520 C C    B GLN   B 1 107 ? 30.677 -25.343 7.022   0.22 21.18 ?  107 GLN   B C    1 
ATOM   5521 O O    A GLN   B 1 107 ? 30.065 -24.815 6.126   0.78 21.71 ?  107 GLN   B O    1 
ATOM   5522 O O    B GLN   B 1 107 ? 30.017 -24.713 6.189   0.22 21.48 ?  107 GLN   B O    1 
ATOM   5523 C CB   A GLN   B 1 107 ? 29.113 -26.528 8.603   0.78 27.31 ?  107 GLN   B CB   1 
ATOM   5524 C CB   B GLN   B 1 107 ? 29.067 -26.550 8.525   0.22 26.40 ?  107 GLN   B CB   1 
ATOM   5525 C CG   A GLN   B 1 107 ? 27.784 -26.022 8.057   0.78 31.99 ?  107 GLN   B CG   1 
ATOM   5526 C CG   B GLN   B 1 107 ? 27.749 -26.024 7.969   0.22 28.95 ?  107 GLN   B CG   1 
ATOM   5527 C CD   A GLN   B 1 107 ? 27.728 -24.509 7.943   0.78 35.74 ?  107 GLN   B CD   1 
ATOM   5528 C CD   B GLN   B 1 107 ? 27.660 -24.509 7.988   0.22 30.99 ?  107 GLN   B CD   1 
ATOM   5529 O OE1  A GLN   B 1 107 ? 28.559 -23.799 8.513   0.78 37.01 ?  107 GLN   B OE1  1 
ATOM   5530 O OE1  B GLN   B 1 107 ? 28.499 -23.832 8.584   0.22 31.72 ?  107 GLN   B OE1  1 
ATOM   5531 N NE2  A GLN   B 1 107 ? 26.742 -24.008 7.205   0.78 36.88 ?  107 GLN   B NE2  1 
ATOM   5532 N NE2  B GLN   B 1 107 ? 26.636 -23.970 7.337   0.22 31.71 ?  107 GLN   B NE2  1 
ATOM   5533 H H    A GLN   B 1 107 ? 31.188 -27.722 8.951   0.78 26.50 ?  107 GLN   B H    1 
ATOM   5534 H H    B GLN   B 1 107 ? 31.146 -27.735 8.872   0.22 28.38 ?  107 GLN   B H    1 
ATOM   5535 H HA   A GLN   B 1 107 ? 29.820 -27.218 6.810   0.78 27.53 ?  107 GLN   B HA   1 
ATOM   5536 H HA   B GLN   B 1 107 ? 29.808 -27.170 6.722   0.22 28.41 ?  107 GLN   B HA   1 
ATOM   5537 H HB2  A GLN   B 1 107 ? 28.944 -27.377 9.036   0.78 32.79 ?  107 GLN   B HB2  1 
ATOM   5538 H HB2  B GLN   B 1 107 ? 28.889 -27.416 8.921   0.22 31.69 ?  107 GLN   B HB2  1 
ATOM   5539 H HB3  A GLN   B 1 107 ? 29.427 -25.886 9.259   0.78 32.79 ?  107 GLN   B HB3  1 
ATOM   5540 H HB3  B GLN   B 1 107 ? 29.365 -25.934 9.213   0.22 31.69 ?  107 GLN   B HB3  1 
ATOM   5541 H HG2  A GLN   B 1 107 ? 27.642 -26.392 7.172   0.78 38.41 ?  107 GLN   B HG2  1 
ATOM   5542 H HG2  B GLN   B 1 107 ? 27.654 -26.317 7.050   0.22 34.75 ?  107 GLN   B HG2  1 
ATOM   5543 H HG3  A GLN   B 1 107 ? 27.069 -26.308 8.652   0.78 38.41 ?  107 GLN   B HG3  1 
ATOM   5544 H HG3  B GLN   B 1 107 ? 27.018 -26.377 8.504   0.22 34.75 ?  107 GLN   B HG3  1 
ATOM   5545 H HE21 A GLN   B 1 107 ? 26.181 -24.535 6.820   0.78 44.28 ?  107 GLN   B HE21 1 
ATOM   5546 H HE21 B GLN   B 1 107 ? 26.069 -24.474 6.931   0.22 38.06 ?  107 GLN   B HE21 1 
ATOM   5547 H HE22 A GLN   B 1 107 ? 26.663 -23.157 7.113   0.78 44.28 ?  107 GLN   B HE22 1 
ATOM   5548 H HE22 B GLN   B 1 107 ? 26.538 -23.116 7.321   0.22 38.06 ?  107 GLN   B HE22 1 
ATOM   5549 N N    . LEU   B 1 108 ? 31.817 -24.870 7.530   1.00 18.62 ?  108 LEU   B N    1 
ATOM   5550 C CA   . LEU   B 1 108 ? 32.363 -23.576 7.119   1.00 16.59 ?  108 LEU   B CA   1 
ATOM   5551 C C    . LEU   B 1 108 ? 33.021 -23.604 5.747   1.00 14.78 ?  108 LEU   B C    1 
ATOM   5552 O O    . LEU   B 1 108 ? 33.446 -22.546 5.254   1.00 14.67 ?  108 LEU   B O    1 
ATOM   5553 C CB   . LEU   B 1 108 ? 33.361 -23.084 8.161   1.00 17.12 ?  108 LEU   B CB   1 
ATOM   5554 C CG   . LEU   B 1 108 ? 32.734 -22.677 9.493   1.00 18.46 ?  108 LEU   B CG   1 
ATOM   5555 C CD1  . LEU   B 1 108 ? 33.780 -22.590 10.589  1.00 18.90 ?  108 LEU   B CD1  1 
ATOM   5556 C CD2  . LEU   B 1 108 ? 32.021 -21.344 9.338   1.00 19.90 ?  108 LEU   B CD2  1 
ATOM   5557 H H    A LEU   B 1 108 ? 32.280 -25.263 8.134   0.78 22.36 ?  108 LEU   B H    1 
ATOM   5558 H H    B LEU   B 1 108 ? 32.283 -25.280 8.120   0.22 22.36 ?  108 LEU   B H    1 
ATOM   5559 H HA   . LEU   B 1 108 ? 31.634 -22.940 7.080   1.00 19.92 ?  108 LEU   B HA   1 
ATOM   5560 H HB2  . LEU   B 1 108 ? 33.994 -23.792 8.344   1.00 20.56 ?  108 LEU   B HB2  1 
ATOM   5561 H HB3  . LEU   B 1 108 ? 33.819 -22.310 7.805   1.00 20.56 ?  108 LEU   B HB3  1 
ATOM   5562 H HG   . LEU   B 1 108 ? 32.073 -23.339 9.756   1.00 22.17 ?  108 LEU   B HG   1 
ATOM   5563 H HD11 . LEU   B 1 108 ? 33.347 -22.344 11.424  1.00 22.69 ?  108 LEU   B HD11 1 
ATOM   5564 H HD12 . LEU   B 1 108 ? 34.211 -23.453 10.683  1.00 22.69 ?  108 LEU   B HD12 1 
ATOM   5565 H HD13 . LEU   B 1 108 ? 34.435 -21.916 10.348  1.00 22.69 ?  108 LEU   B HD13 1 
ATOM   5566 H HD21 . LEU   B 1 108 ? 31.699 -21.054 10.206  1.00 23.90 ?  108 LEU   B HD21 1 
ATOM   5567 H HD22 . LEU   B 1 108 ? 32.645 -20.693 8.983   1.00 23.90 ?  108 LEU   B HD22 1 
ATOM   5568 H HD23 . LEU   B 1 108 ? 31.273 -21.453 8.729   1.00 23.90 ?  108 LEU   B HD23 1 
ATOM   5569 N N    . LEU   B 1 109 ? 33.100 -24.776 5.121   1.00 13.97 ?  109 LEU   B N    1 
ATOM   5570 C CA   . LEU   B 1 109 ? 33.724 -24.882 3.811   1.00 13.32 ?  109 LEU   B CA   1 
ATOM   5571 C C    . LEU   B 1 109 ? 32.959 -24.092 2.754   1.00 12.55 ?  109 LEU   B C    1 
ATOM   5572 O O    . LEU   B 1 109 ? 33.576 -23.494 1.865   1.00 12.33 ?  109 LEU   B O    1 
ATOM   5573 C CB   . LEU   B 1 109 ? 33.841 -26.356 3.428   1.00 13.39 ?  109 LEU   B CB   1 
ATOM   5574 C CG   . LEU   B 1 109 ? 34.623 -26.686 2.158   1.00 13.21 ?  109 LEU   B CG   1 
ATOM   5575 C CD1  . LEU   B 1 109 ? 36.001 -26.045 2.174   1.00 13.36 ?  109 LEU   B CD1  1 
ATOM   5576 C CD2  . LEU   B 1 109 ? 34.745 -28.191 2.005   1.00 13.63 ?  109 LEU   B CD2  1 
ATOM   5577 H H    . LEU   B 1 109 ? 32.808 -25.525 5.429   1.00 16.77 ?  109 LEU   B H    1 
ATOM   5578 H HA   . LEU   B 1 109 ? 34.619 -24.516 3.858   1.00 16.00 ?  109 LEU   B HA   1 
ATOM   5579 H HB2  . LEU   B 1 109 ? 34.280 -26.826 4.154   1.00 16.09 ?  109 LEU   B HB2  1 
ATOM   5580 H HB3  . LEU   B 1 109 ? 32.948 -26.715 3.309   1.00 16.09 ?  109 LEU   B HB3  1 
ATOM   5581 H HG   . LEU   B 1 109 ? 34.140 -26.349 1.384   1.00 15.86 ?  109 LEU   B HG   1 
ATOM   5582 H HD11 . LEU   B 1 109 ? 36.528 -26.404 1.442   1.00 16.04 ?  109 LEU   B HD11 1 
ATOM   5583 H HD12 . LEU   B 1 109 ? 35.903 -25.086 2.069   1.00 16.04 ?  109 LEU   B HD12 1 
ATOM   5584 H HD13 . LEU   B 1 109 ? 36.431 -26.246 3.019   1.00 16.04 ?  109 LEU   B HD13 1 
ATOM   5585 H HD21 . LEU   B 1 109 ? 35.313 -28.388 1.241   1.00 16.37 ?  109 LEU   B HD21 1 
ATOM   5586 H HD22 . LEU   B 1 109 ? 35.135 -28.560 2.810   1.00 16.37 ?  109 LEU   B HD22 1 
ATOM   5587 H HD23 . LEU   B 1 109 ? 33.861 -28.568 1.862   1.00 16.37 ?  109 LEU   B HD23 1 
ATOM   5588 N N    . LYS   B 1 110 ? 31.624 -24.067 2.829   1.00 12.37 ?  110 LYS   B N    1 
ATOM   5589 C CA   . LYS   B 1 110 ? 30.865 -23.303 1.843   1.00 12.28 ?  110 LYS   B CA   1 
ATOM   5590 C C    . LYS   B 1 110 ? 31.203 -21.812 1.932   1.00 11.93 ?  110 LYS   B C    1 
ATOM   5591 O O    . LYS   B 1 110 ? 31.461 -21.162 0.915   1.00 11.66 ?  110 LYS   B O    1 
ATOM   5592 C CB   . LYS   B 1 110 ? 29.363 -23.554 1.998   1.00 12.98 ?  110 LYS   B CB   1 
ATOM   5593 C CG   . LYS   B 1 110 ? 28.546 -22.920 0.877   1.00 13.54 ?  110 LYS   B CG   1 
ATOM   5594 C CD   . LYS   B 1 110 ? 27.092 -23.372 0.893   1.00 13.88 ?  110 LYS   B CD   1 
ATOM   5595 C CE   . LYS   B 1 110 ? 26.316 -22.837 -0.315  1.00 14.53 ?  110 LYS   B CE   1 
ATOM   5596 N NZ   . LYS   B 1 110 ? 26.656 -23.529 -1.588  1.00 14.72 ?  110 LYS   B NZ   1 
ATOM   5597 H H    . LYS   B 1 110 ? 31.151 -24.482 3.415   1.00 14.86 ?  110 LYS   B H    1 
ATOM   5598 H HA   . LYS   B 1 110 ? 31.119 -23.607 0.954   1.00 14.76 ?  110 LYS   B HA   1 
ATOM   5599 H HB2  . LYS   B 1 110 ? 29.199 -24.514 1.979   1.00 15.59 ?  110 LYS   B HB2  1 
ATOM   5600 H HB3  . LYS   B 1 110 ? 29.063 -23.184 2.839   1.00 15.59 ?  110 LYS   B HB3  1 
ATOM   5601 H HG2  . LYS   B 1 110 ? 28.554 -21.954 0.983   1.00 16.26 ?  110 LYS   B HG2  1 
ATOM   5602 H HG3  . LYS   B 1 110 ? 28.924 -23.164 0.020   1.00 16.26 ?  110 LYS   B HG3  1 
ATOM   5603 H HD2  . LYS   B 1 110 ? 27.059 -24.347 0.872   1.00 16.67 ?  110 LYS   B HD2  1 
ATOM   5604 H HD3  . LYS   B 1 110 ? 26.660 -23.049 1.702   1.00 16.67 ?  110 LYS   B HD3  1 
ATOM   5605 H HE2  . LYS   B 1 110 ? 25.366 -22.961 -0.156  1.00 17.45 ?  110 LYS   B HE2  1 
ATOM   5606 H HE3  . LYS   B 1 110 ? 26.517 -21.899 -0.421  1.00 17.45 ?  110 LYS   B HE3  1 
ATOM   5607 H HZ1  . LYS   B 1 110 ? 26.185 -23.184 -2.255  1.00 17.68 ?  110 LYS   B HZ1  1 
ATOM   5608 H HZ2  . LYS   B 1 110 ? 27.525 -23.430 -1.762  1.00 17.68 ?  110 LYS   B HZ2  1 
ATOM   5609 H HZ3  . LYS   B 1 110 ? 26.475 -24.398 -1.521  1.00 17.68 ?  110 LYS   B HZ3  1 
ATOM   5610 N N    . SER   B 1 111 ? 31.234 -21.262 3.152   1.00 12.40 ?  111 SER   B N    1 
ATOM   5611 C CA   . SER   B 1 111 ? 31.617 -19.861 3.331   1.00 12.28 ?  111 SER   B CA   1 
ATOM   5612 C C    . SER   B 1 111 ? 33.001 -19.596 2.749   1.00 11.63 ?  111 SER   B C    1 
ATOM   5613 O O    . SER   B 1 111 ? 33.227 -18.562 2.104   1.00 11.98 ?  111 SER   B O    1 
ATOM   5614 C CB   . SER   B 1 111 ? 31.594 -19.508 4.817   1.00 13.27 ?  111 SER   B CB   1 
ATOM   5615 O OG   . SER   B 1 111 ? 30.275 -19.505 5.323   1.00 15.53 ?  111 SER   B OG   1 
ATOM   5616 H H    . SER   B 1 111 ? 31.041 -21.680 3.878   1.00 14.89 ?  111 SER   B H    1 
ATOM   5617 H HA   . SER   B 1 111 ? 30.983 -19.298 2.872   1.00 14.76 ?  111 SER   B HA   1 
ATOM   5618 H HB2  . SER   B 1 111 ? 32.115 -20.166 5.307   1.00 15.94 ?  111 SER   B HB2  1 
ATOM   5619 H HB3  . SER   B 1 111 ? 31.973 -18.628 4.937   1.00 15.94 ?  111 SER   B HB3  1 
ATOM   5620 H HG   . SER   B 1 111 ? 30.277 -19.315 6.144   1.00 18.65 ?  111 SER   B HG   1 
ATOM   5621 N N    . ALA   B 1 112 ? 33.937 -20.520 2.966   1.00 11.65 ?  112 ALA   B N    1 
ATOM   5622 C CA   . ALA   B 1 112 ? 35.280 -20.349 2.423   1.00 11.36 ?  112 ALA   B CA   1 
ATOM   5623 C C    . ALA   B 1 112 ? 35.247 -20.251 0.902   1.00 10.68 ?  112 ALA   B C    1 
ATOM   5624 O O    . ALA   B 1 112 ? 35.871 -19.359 0.311   1.00 11.43 ?  112 ALA   B O    1 
ATOM   5625 C CB   . ALA   B 1 112 ? 36.185 -21.491 2.889   1.00 12.20 ?  112 ALA   B CB   1 
ATOM   5626 H H    . ALA   B 1 112 ? 33.824 -21.244 3.422   1.00 13.99 ?  112 ALA   B H    1 
ATOM   5627 H HA   . ALA   B 1 112 ? 35.649 -19.520 2.766   1.00 13.65 ?  112 ALA   B HA   1 
ATOM   5628 H HB1  . ALA   B 1 112 ? 37.075 -21.353 2.524   1.00 14.66 ?  112 ALA   B HB1  1 
ATOM   5629 H HB2  . ALA   B 1 112 ? 36.225 -21.484 3.860   1.00 14.66 ?  112 ALA   B HB2  1 
ATOM   5630 H HB3  . ALA   B 1 112 ? 35.823 -22.331 2.577   1.00 14.66 ?  112 ALA   B HB3  1 
ATOM   5631 N N    . TYR   B 1 113 ? 34.516 -21.155 0.244   1.00 10.89 ?  113 TYR   B N    1 
ATOM   5632 C CA   . TYR   B 1 113 ? 34.444 -21.100 -1.210  1.00 10.51 ?  113 TYR   B CA   1 
ATOM   5633 C C    . TYR   B 1 113 ? 33.735 -19.851 -1.727  1.00 10.42 ?  113 TYR   B C    1 
ATOM   5634 O O    . TYR   B 1 113 ? 34.006 -19.415 -2.852  1.00 10.66 ?  113 TYR   B O    1 
ATOM   5635 C CB   . TYR   B 1 113 ? 33.767 -22.357 -1.758  1.00 11.11 ?  113 TYR   B CB   1 
ATOM   5636 C CG   . TYR   B 1 113 ? 34.730 -23.505 -2.026  1.00 11.35 ?  113 TYR   B CG   1 
ATOM   5637 C CD1  . TYR   B 1 113 ? 35.719 -23.398 -3.000  1.00 12.08 ?  113 TYR   B CD1  1 
ATOM   5638 C CD2  . TYR   B 1 113 ? 34.637 -24.698 -1.320  1.00 11.63 ?  113 TYR   B CD2  1 
ATOM   5639 C CE1  . TYR   B 1 113 ? 36.603 -24.439 -3.252  1.00 11.84 ?  113 TYR   B CE1  1 
ATOM   5640 C CE2  . TYR   B 1 113 ? 35.507 -25.751 -1.573  1.00 11.87 ?  113 TYR   B CE2  1 
ATOM   5641 C CZ   . TYR   B 1 113 ? 36.486 -25.616 -2.539  1.00 12.01 ?  113 TYR   B CZ   1 
ATOM   5642 O OH   . TYR   B 1 113 ? 37.357 -26.639 -2.813  1.00 12.44 ?  113 TYR   B OH   1 
ATOM   5643 H H    . TYR   B 1 113 ? 34.057 -21.787 0.614   1.00 13.08 ?  113 TYR   B H    1 
ATOM   5644 H HA   . TYR   B 1 113 ? 35.346 -21.086 -1.548  1.00 12.62 ?  113 TYR   B HA   1 
ATOM   5645 H HB2  . TYR   B 1 113 ? 33.110 -22.673 -1.114  1.00 13.35 ?  113 TYR   B HB2  1 
ATOM   5646 H HB3  . TYR   B 1 113 ? 33.326 -22.138 -2.592  1.00 13.35 ?  113 TYR   B HB3  1 
ATOM   5647 H HD1  . TYR   B 1 113 ? 35.797 -22.607 -3.487  1.00 14.51 ?  113 TYR   B HD1  1 
ATOM   5648 H HD2  . TYR   B 1 113 ? 33.975 -24.792 -0.677  1.00 13.97 ?  113 TYR   B HD2  1 
ATOM   5649 H HE1  . TYR   B 1 113 ? 37.252 -24.351 -3.918  1.00 14.22 ?  113 TYR   B HE1  1 
ATOM   5650 H HE2  . TYR   B 1 113 ? 35.425 -26.546 -1.102  1.00 14.26 ?  113 TYR   B HE2  1 
ATOM   5651 H HH   . TYR   B 1 113 ? 37.148 -27.318 -2.366  1.00 14.95 ?  113 TYR   B HH   1 
ATOM   5652 N N    . GLU   B 1 114 ? 32.809 -19.273 -0.953  1.00 10.64 ?  114 GLU   B N    1 
ATOM   5653 C CA   . GLU   B 1 114 ? 32.124 -18.068 -1.413  1.00 10.62 ?  114 GLU   B CA   1 
ATOM   5654 C C    . GLU   B 1 114 ? 33.102 -16.942 -1.703  1.00 10.62 ?  114 GLU   B C    1 
ATOM   5655 O O    . GLU   B 1 114 ? 32.818 -16.081 -2.541  1.00 11.07 ?  114 GLU   B O    1 
ATOM   5656 C CB   . GLU   B 1 114 ? 31.058 -17.641 -0.400  1.00 11.39 ?  114 GLU   B CB   1 
ATOM   5657 C CG   . GLU   B 1 114 ? 29.849 -18.569 -0.451  1.00 11.62 ?  114 GLU   B CG   1 
ATOM   5658 C CD   . GLU   B 1 114 ? 28.827 -18.371 0.659   1.00 11.57 ?  114 GLU   B CD   1 
ATOM   5659 O OE1  . GLU   B 1 114 ? 29.119 -17.753 1.705   1.00 12.14 ?  114 GLU   B OE1  1 
ATOM   5660 O OE2  . GLU   B 1 114 ? 27.700 -18.899 0.495   1.00 12.51 -1 114 GLU   B OE2  1 
ATOM   5661 H H    . GLU   B 1 114 ? 32.555 -19.564 -0.182  1.00 12.78 ?  114 GLU   B H    1 
ATOM   5662 H HA   . GLU   B 1 114 ? 31.672 -18.272 -2.242  1.00 12.76 ?  114 GLU   B HA   1 
ATOM   5663 H HB2  . GLU   B 1 114 ? 31.434 -17.680 0.496   1.00 13.68 ?  114 GLU   B HB2  1 
ATOM   5664 H HB3  . GLU   B 1 114 ? 30.761 -16.745 -0.604  1.00 13.68 ?  114 GLU   B HB3  1 
ATOM   5665 H HG2  . GLU   B 1 114 ? 29.398 -18.439 -1.296  1.00 13.96 ?  114 GLU   B HG2  1 
ATOM   5666 H HG3  . GLU   B 1 114 ? 30.168 -19.490 -0.394  1.00 13.96 ?  114 GLU   B HG3  1 
ATOM   5667 N N    . ASN   B 1 115 ? 34.268 -16.936 -1.049  1.00 10.66 ?  115 ASN   B N    1 
ATOM   5668 C CA   . ASN   B 1 115 ? 35.257 -15.901 -1.346  1.00 10.68 ?  115 ASN   B CA   1 
ATOM   5669 C C    . ASN   B 1 115 ? 35.667 -15.918 -2.811  1.00 10.32 ?  115 ASN   B C    1 
ATOM   5670 O O    . ASN   B 1 115 ? 36.060 -14.879 -3.359  1.00 11.00 ?  115 ASN   B O    1 
ATOM   5671 C CB   . ASN   B 1 115 ? 36.497 -16.077 -0.465  1.00 11.07 ?  115 ASN   B CB   1 
ATOM   5672 C CG   . ASN   B 1 115 ? 36.227 -15.822 0.997   1.00 11.78 ?  115 ASN   B CG   1 
ATOM   5673 O OD1  . ASN   B 1 115 ? 36.218 -14.682 1.441   1.00 13.75 ?  115 ASN   B OD1  1 
ATOM   5674 N ND2  . ASN   B 1 115 ? 36.069 -16.890 1.767   1.00 11.92 ?  115 ASN   B ND2  1 
ATOM   5675 H H    . ASN   B 1 115 ? 34.503 -17.500 -0.435  1.00 12.81 ?  115 ASN   B H    1 
ATOM   5676 H HA   . ASN   B 1 115 ? 34.879 -15.032 -1.150  1.00 12.83 ?  115 ASN   B HA   1 
ATOM   5677 H HB2  . ASN   B 1 115 ? 36.826 -16.987 -0.557  1.00 13.30 ?  115 ASN   B HB2  1 
ATOM   5678 H HB3  . ASN   B 1 115 ? 37.181 -15.451 -0.752  1.00 13.30 ?  115 ASN   B HB3  1 
ATOM   5679 H HD21 . ASN   B 1 115 ? 35.924 -16.797 2.610   1.00 14.32 ?  115 ASN   B HD21 1 
ATOM   5680 H HD22 . ASN   B 1 115 ? 36.101 -17.682 1.425   1.00 14.32 ?  115 ASN   B HD22 1 
ATOM   5681 N N    . PHE   B 1 116 ? 35.646 -17.094 -3.448  1.00 10.10 ?  116 PHE   B N    1 
ATOM   5682 C CA   . PHE   B 1 116 ? 36.074 -17.186 -4.839  1.00 10.48 ?  116 PHE   B CA   1 
ATOM   5683 C C    . PHE   B 1 116 ? 35.172 -16.360 -5.749  1.00 10.23 ?  116 PHE   B C    1 
ATOM   5684 O O    . PHE   B 1 116 ? 35.605 -15.931 -6.822  1.00 10.65 ?  116 PHE   B O    1 
ATOM   5685 C CB   . PHE   B 1 116 ? 36.041 -18.633 -5.361  1.00 10.23 ?  116 PHE   B CB   1 
ATOM   5686 C CG   . PHE   B 1 116 ? 37.109 -19.588 -4.812  1.00 10.26 ?  116 PHE   B CG   1 
ATOM   5687 C CD1  . PHE   B 1 116 ? 37.763 -19.402 -3.604  1.00 11.03 ?  116 PHE   B CD1  1 
ATOM   5688 C CD2  . PHE   B 1 116 ? 37.410 -20.720 -5.549  1.00 10.48 ?  116 PHE   B CD2  1 
ATOM   5689 C CE1  . PHE   B 1 116 ? 38.698 -20.336 -3.150  1.00 11.21 ?  116 PHE   B CE1  1 
ATOM   5690 C CE2  . PHE   B 1 116 ? 38.337 -21.653 -5.104  1.00 10.65 ?  116 PHE   B CE2  1 
ATOM   5691 C CZ   . PHE   B 1 116 ? 38.977 -21.467 -3.907  1.00 10.90 ?  116 PHE   B CZ   1 
ATOM   5692 H H    . PHE   B 1 116 ? 35.382 -17.844 -3.103  1.00 12.14 ?  116 PHE   B H    1 
ATOM   5693 H HA   . PHE   B 1 116 ? 36.981 -16.855 -4.918  1.00 12.60 ?  116 PHE   B HA   1 
ATOM   5694 H HB2  . PHE   B 1 116 ? 35.171 -19.012 -5.143  1.00 12.29 ?  116 PHE   B HB2  1 
ATOM   5695 H HB3  . PHE   B 1 116 ? 36.140 -18.607 -6.327  1.00 12.29 ?  116 PHE   B HB3  1 
ATOM   5696 H HD1  . PHE   B 1 116 ? 37.567 -18.648 -3.089  1.00 13.25 ?  116 PHE   B HD1  1 
ATOM   5697 H HD2  . PHE   B 1 116 ? 36.970 -20.873 -6.356  1.00 12.59 ?  116 PHE   B HD2  1 
ATOM   5698 H HE1  . PHE   B 1 116 ? 39.136 -20.195 -2.341  1.00 13.47 ?  116 PHE   B HE1  1 
ATOM   5699 H HE2  . PHE   B 1 116 ? 38.526 -22.407 -5.616  1.00 12.80 ?  116 PHE   B HE2  1 
ATOM   5700 H HZ   . PHE   B 1 116 ? 39.613 -22.077 -3.610  1.00 13.09 ?  116 PHE   B HZ   1 
ATOM   5701 N N    . ASN   B 1 117 ? 33.906 -16.160 -5.360  1.00 10.58 ?  117 ASN   B N    1 
ATOM   5702 C CA   . ASN   B 1 117 ? 32.960 -15.461 -6.228  1.00 10.82 ?  117 ASN   B CA   1 
ATOM   5703 C C    . ASN   B 1 117 ? 33.268 -13.979 -6.376  1.00 11.12 ?  117 ASN   B C    1 
ATOM   5704 O O    . ASN   B 1 117 ? 32.672 -13.326 -7.236  1.00 12.25 ?  117 ASN   B O    1 
ATOM   5705 C CB   . ASN   B 1 117 ? 31.540 -15.686 -5.734  1.00 10.92 ?  117 ASN   B CB   1 
ATOM   5706 C CG   . ASN   B 1 117 ? 31.090 -17.094 -5.985  1.00 11.18 ?  117 ASN   B CG   1 
ATOM   5707 O OD1  . ASN   B 1 117 ? 31.433 -17.677 -7.014  1.00 12.13 ?  117 ASN   B OD1  1 
ATOM   5708 N ND2  . ASN   B 1 117 ? 30.354 -17.668 -5.045  1.00 11.43 ?  117 ASN   B ND2  1 
ATOM   5709 H H    . ASN   B 1 117 ? 33.585 -16.409 -4.600  1.00 12.71 ?  117 ASN   B H    1 
ATOM   5710 H HA   . ASN   B 1 117 ? 33.027 -15.858 -7.107  1.00 13.00 ?  117 ASN   B HA   1 
ATOM   5711 H HB2  . ASN   B 1 117 ? 31.500 -15.515 -4.779  1.00 13.11 ?  117 ASN   B HB2  1 
ATOM   5712 H HB3  . ASN   B 1 117 ? 30.944 -15.078 -6.206  1.00 13.11 ?  117 ASN   B HB3  1 
ATOM   5713 H HD21 . ASN   B 1 117 ? 30.071 -18.473 -5.146  1.00 13.73 ?  117 ASN   B HD21 1 
ATOM   5714 H HD22 . ASN   B 1 117 ? 30.138 -17.225 -4.336  1.00 13.73 ?  117 ASN   B HD22 1 
ATOM   5715 N N    . GLN   B 1 118 ? 34.213 -13.452 -5.606  1.00 10.88 ?  118 GLN   B N    1 
ATOM   5716 C CA   . GLN   B 1 118 ? 34.636 -12.066 -5.740  1.00 11.41 ?  118 GLN   B CA   1 
ATOM   5717 C C    . GLN   B 1 118 ? 35.704 -11.875 -6.812  1.00 11.54 ?  118 GLN   B C    1 
ATOM   5718 O O    . GLN   B 1 118 ? 36.178 -10.747 -6.995  1.00 12.92 ?  118 GLN   B O    1 
ATOM   5719 C CB   . GLN   B 1 118 ? 35.116 -11.535 -4.386  1.00 11.97 ?  118 GLN   B CB   1 
ATOM   5720 C CG   . GLN   B 1 118 ? 34.034 -11.568 -3.319  1.00 12.15 ?  118 GLN   B CG   1 
ATOM   5721 C CD   . GLN   B 1 118 ? 32.860 -10.663 -3.646  1.00 11.84 ?  118 GLN   B CD   1 
ATOM   5722 O OE1  . GLN   B 1 118 ? 33.045 -9.523  -4.084  1.00 12.71 ?  118 GLN   B OE1  1 
ATOM   5723 N NE2  . GLN   B 1 118 ? 31.649 -11.153 -3.433  1.00 12.42 ?  118 GLN   B NE2  1 
ATOM   5724 H H    . GLN   B 1 118 ? 34.639 -13.884 -4.988  1.00 13.08 ?  118 GLN   B H    1 
ATOM   5725 H HA   . GLN   B 1 118 ? 33.867 -11.539 -6.004  1.00 13.71 ?  118 GLN   B HA   1 
ATOM   5726 H HB2  . GLN   B 1 118 ? 35.859 -12.072 -4.078  1.00 14.38 ?  118 GLN   B HB2  1 
ATOM   5727 H HB3  . GLN   B 1 118 ? 35.397 -10.609 -4.491  1.00 14.38 ?  118 GLN   B HB3  1 
ATOM   5728 H HG2  . GLN   B 1 118 ? 33.704 -12.477 -3.238  1.00 14.59 ?  118 GLN   B HG2  1 
ATOM   5729 H HG3  . GLN   B 1 118 ? 34.419 -11.279 -2.475  1.00 14.59 ?  118 GLN   B HG3  1 
ATOM   5730 H HE21 . GLN   B 1 118 ? 31.560 -11.952 -3.128  1.00 14.91 ?  118 GLN   B HE21 1 
ATOM   5731 H HE22 . GLN   B 1 118 ? 30.962 -10.674 -3.604  1.00 14.91 ?  118 GLN   B HE22 1 
ATOM   5732 N N    . HIS   B 1 119 ? 36.061 -12.934 -7.541  1.00 10.71 ?  119 HIS   B N    1 
ATOM   5733 C CA   . HIS   B 1 119 ? 37.101 -12.889 -8.560  1.00 11.27 ?  119 HIS   B CA   1 
ATOM   5734 C C    . HIS   B 1 119 ? 36.622 -13.622 -9.797  1.00 11.28 ?  119 HIS   B C    1 
ATOM   5735 O O    . HIS   B 1 119 ? 36.117 -14.739 -9.690  1.00 12.09 ?  119 HIS   B O    1 
ATOM   5736 C CB   . HIS   B 1 119 ? 38.384 -13.515 -8.018  1.00 11.81 ?  119 HIS   B CB   1 
ATOM   5737 C CG   . HIS   B 1 119 ? 38.872 -12.812 -6.799  1.00 13.05 ?  119 HIS   B CG   1 
ATOM   5738 N ND1  . HIS   B 1 119 ? 39.650 -11.676 -6.862  1.00 14.56 ?  119 HIS   B ND1  1 
ATOM   5739 C CD2  . HIS   B 1 119 ? 38.594 -13.008 -5.490  1.00 14.16 ?  119 HIS   B CD2  1 
ATOM   5740 C CE1  . HIS   B 1 119 ? 39.866 -11.231 -5.639  1.00 15.75 ?  119 HIS   B CE1  1 
ATOM   5741 N NE2  . HIS   B 1 119 ? 39.233 -12.017 -4.788  1.00 15.70 ?  119 HIS   B NE2  1 
ATOM   5742 H H    . HIS   B 1 119 ? 35.693 -13.714 -7.472  1.00 12.86 ?  119 HIS   B H    1 
ATOM   5743 H HA   . HIS   B 1 119 ? 37.278 -11.962 -8.801  1.00 13.54 ?  119 HIS   B HA   1 
ATOM   5744 H HB2  . HIS   B 1 119 ? 38.212 -14.436 -7.789  1.00 14.18 ?  119 HIS   B HB2  1 
ATOM   5745 H HB3  . HIS   B 1 119 ? 39.073 -13.456 -8.699  1.00 14.18 ?  119 HIS   B HB3  1 
ATOM   5746 H HD2  . HIS   B 1 119 ? 38.074 -13.694 -5.138  1.00 17.01 ?  119 HIS   B HD2  1 
ATOM   5747 H HE1  . HIS   B 1 119 ? 40.390 -10.496 -5.410  1.00 18.91 ?  119 HIS   B HE1  1 
ATOM   5748 H HE2  . HIS   B 1 119 ? 39.245 -11.941 -3.932  1.00 18.86 ?  119 HIS   B HE2  1 
ATOM   5749 N N    . GLU   B 1 120 ? 36.777 -13.010 -10.969 1.00 11.71 ?  120 GLU   B N    1 
ATOM   5750 C CA   . GLU   B 1 120 ? 36.178 -13.595 -12.164 1.00 13.56 ?  120 GLU   B CA   1 
ATOM   5751 C C    . GLU   B 1 120 ? 36.856 -14.894 -12.581 1.00 12.08 ?  120 GLU   B C    1 
ATOM   5752 O O    . GLU   B 1 120 ? 36.197 -15.765 -13.159 1.00 12.30 ?  120 GLU   B O    1 
ATOM   5753 C CB   . GLU   B 1 120 ? 36.173 -12.590 -13.313 1.00 19.22 ?  120 GLU   B CB   1 
ATOM   5754 C CG   . GLU   B 1 120 ? 35.225 -11.425 -13.074 1.00 26.73 ?  120 GLU   B CG   1 
ATOM   5755 C CD   . GLU   B 1 120 ? 35.019 -10.550 -14.294 1.00 34.85 ?  120 GLU   B CD   1 
ATOM   5756 O OE1  . GLU   B 1 120 ? 35.999 -10.295 -15.024 1.00 37.74 ?  120 GLU   B OE1  1 
ATOM   5757 O OE2  . GLU   B 1 120 ? 33.868 -10.116 -14.519 1.00 38.39 -1 120 GLU   B OE2  1 
ATOM   5758 H H    . GLU   B 1 120 ? 37.203 -12.273 -11.098 1.00 14.06 ?  120 GLU   B H    1 
ATOM   5759 H HA   . GLU   B 1 120 ? 35.255 -13.810 -11.970 1.00 16.28 ?  120 GLU   B HA   1 
ATOM   5760 H HB2  . GLU   B 1 120 ? 37.063 -12.226 -13.426 1.00 23.07 ?  120 GLU   B HB2  1 
ATOM   5761 H HB3  . GLU   B 1 120 ? 35.890 -13.036 -14.128 1.00 23.07 ?  120 GLU   B HB3  1 
ATOM   5762 H HG2  . GLU   B 1 120 ? 34.357 -11.774 -12.816 1.00 32.09 ?  120 GLU   B HG2  1 
ATOM   5763 H HG3  . GLU   B 1 120 ? 35.582 -10.869 -12.368 1.00 32.09 ?  120 GLU   B HG3  1 
ATOM   5764 N N    . VAL   B 1 121 ? 38.156 -15.033 -12.321 1.00 11.53 ?  121 VAL   B N    1 
ATOM   5765 C CA   . VAL   B 1 121 ? 38.903 -16.241 -12.666 1.00 11.56 ?  121 VAL   B CA   1 
ATOM   5766 C C    . VAL   B 1 121 ? 40.011 -16.441 -11.640 1.00 10.95 ?  121 VAL   B C    1 
ATOM   5767 O O    . VAL   B 1 121 ? 40.684 -15.481 -11.248 1.00 11.87 ?  121 VAL   B O    1 
ATOM   5768 C CB   . VAL   B 1 121 ? 39.424 -16.203 -14.122 1.00 13.28 ?  121 VAL   B CB   1 
ATOM   5769 C CG1  . VAL   B 1 121 ? 40.289 -14.975 -14.374 1.00 14.67 ?  121 VAL   B CG1  1 
ATOM   5770 C CG2  . VAL   B 1 121 ? 40.175 -17.477 -14.464 1.00 14.82 ?  121 VAL   B CG2  1 
ATOM   5771 H H    . VAL   B 1 121 ? 38.640 -14.426 -11.947 1.00 13.85 ?  121 VAL   B H    1 
ATOM   5772 H HA   . VAL   B 1 121 ? 38.301 -16.995 -12.598 1.00 13.89 ?  121 VAL   B HA   1 
ATOM   5773 H HB   . VAL   B 1 121 ? 38.660 -16.145 -14.722 1.00 15.95 ?  121 VAL   B HB   1 
ATOM   5774 H HG11 . VAL   B 1 121 ? 40.599 -14.987 -15.294 1.00 17.62 ?  121 VAL   B HG11 1 
ATOM   5775 H HG12 . VAL   B 1 121 ? 39.762 -14.174 -14.217 1.00 17.62 ?  121 VAL   B HG12 1 
ATOM   5776 H HG13 . VAL   B 1 121 ? 41.049 -14.992 -13.771 1.00 17.62 ?  121 VAL   B HG13 1 
ATOM   5777 H HG21 . VAL   B 1 121 ? 40.370 -17.482 -15.416 1.00 17.79 ?  121 VAL   B HG21 1 
ATOM   5778 H HG22 . VAL   B 1 121 ? 41.005 -17.499 -13.960 1.00 17.79 ?  121 VAL   B HG22 1 
ATOM   5779 H HG23 . VAL   B 1 121 ? 39.625 -18.239 -14.235 1.00 17.79 ?  121 VAL   B HG23 1 
ATOM   5780 N N    . LEU   B 1 122 ? 40.199 -17.694 -11.206 1.00 10.68 ?  122 LEU   B N    1 
ATOM   5781 C CA   . LEU   B 1 122 ? 41.180 -18.043 -10.181 1.00 10.67 ?  122 LEU   B CA   1 
ATOM   5782 C C    . LEU   B 1 122 ? 41.838 -19.373 -10.506 1.00 10.38 ?  122 LEU   B C    1 
ATOM   5783 O O    . LEU   B 1 122 ? 41.182 -20.295 -11.008 1.00 11.57 ?  122 LEU   B O    1 
ATOM   5784 C CB   . LEU   B 1 122 ? 40.516 -18.276 -8.808  1.00 12.40 ?  122 LEU   B CB   1 
ATOM   5785 C CG   . LEU   B 1 122 ? 39.491 -17.247 -8.320  1.00 12.23 ?  122 LEU   B CG   1 
ATOM   5786 C CD1  . LEU   B 1 122 ? 38.095 -17.606 -8.790  1.00 13.26 ?  122 LEU   B CD1  1 
ATOM   5787 C CD2  . LEU   B 1 122 ? 39.547 -17.145 -6.813  1.00 12.06 ?  122 LEU   B CD2  1 
ATOM   5788 H H    . LEU   B 1 122 ? 39.755 -18.370 -11.497 1.00 12.83 ?  122 LEU   B H    1 
ATOM   5789 H HA   . LEU   B 1 122 ? 41.854 -17.349 -10.101 1.00 12.82 ?  122 LEU   B HA   1 
ATOM   5790 H HB2  . LEU   B 1 122 ? 40.064 -19.129 -8.838  1.00 14.90 ?  122 LEU   B HB2  1 
ATOM   5791 H HB3  . LEU   B 1 122 ? 41.218 -18.307 -8.141  1.00 14.90 ?  122 LEU   B HB3  1 
ATOM   5792 H HG   . LEU   B 1 122 ? 39.712 -16.376 -8.683  1.00 14.69 ?  122 LEU   B HG   1 
ATOM   5793 H HD11 . LEU   B 1 122 ? 37.467 -16.955 -8.439  1.00 15.92 ?  122 LEU   B HD11 1 
ATOM   5794 H HD12 . LEU   B 1 122 ? 38.077 -17.593 -9.759  1.00 15.92 ?  122 LEU   B HD12 1 
ATOM   5795 H HD13 . LEU   B 1 122 ? 37.871 -18.491 -8.465  1.00 15.92 ?  122 LEU   B HD13 1 
ATOM   5796 H HD21 . LEU   B 1 122 ? 38.867 -16.525 -6.508  1.00 14.49 ?  122 LEU   B HD21 1 
ATOM   5797 H HD22 . LEU   B 1 122 ? 39.392 -18.023 -6.429  1.00 14.49 ?  122 LEU   B HD22 1 
ATOM   5798 H HD23 . LEU   B 1 122 ? 40.427 -16.824 -6.550  1.00 14.49 ?  122 LEU   B HD23 1 
ATOM   5799 N N    . LEU   B 1 123 ? 43.127 -19.477 -10.154 1.00 10.27 ?  123 LEU   B N    1 
ATOM   5800 C CA   . LEU   B 1 123 ? 43.843 -20.744 -10.029 1.00 10.52 ?  123 LEU   B CA   1 
ATOM   5801 C C    . LEU   B 1 123 ? 43.815 -21.142 -8.557  1.00 10.14 ?  123 LEU   B C    1 
ATOM   5802 O O    . LEU   B 1 123 ? 44.172 -20.318 -7.701  1.00 10.94 ?  123 LEU   B O    1 
ATOM   5803 C CB   . LEU   B 1 123 ? 45.290 -20.557 -10.488 1.00 11.11 ?  123 LEU   B CB   1 
ATOM   5804 C CG   . LEU   B 1 123 ? 46.232 -21.736 -10.240 1.00 11.29 ?  123 LEU   B CG   1 
ATOM   5805 C CD1  . LEU   B 1 123 ? 45.815 -22.977 -11.032 1.00 11.84 ?  123 LEU   B CD1  1 
ATOM   5806 C CD2  . LEU   B 1 123 ? 47.652 -21.335 -10.583 1.00 12.14 ?  123 LEU   B CD2  1 
ATOM   5807 H H    . LEU   B 1 123 ? 43.621 -18.796 -9.962  1.00 12.34 ?  123 LEU   B H    1 
ATOM   5808 H HA   . LEU   B 1 123 ? 43.408 -21.431 -10.564 1.00 12.63 ?  123 LEU   B HA   1 
ATOM   5809 H HB2  . LEU   B 1 123 ? 45.284 -20.387 -11.443 1.00 13.34 ?  123 LEU   B HB2  1 
ATOM   5810 H HB3  . LEU   B 1 123 ? 45.657 -19.792 -10.024 1.00 13.34 ?  123 LEU   B HB3  1 
ATOM   5811 H HG   . LEU   B 1 123 ? 46.212 -21.970 -9.299  1.00 13.57 ?  123 LEU   B HG   1 
ATOM   5812 H HD11 . LEU   B 1 123 ? 46.452 -23.686 -10.858 1.00 14.22 ?  123 LEU   B HD11 1 
ATOM   5813 H HD12 . LEU   B 1 123 ? 44.929 -23.247 -10.747 1.00 14.22 ?  123 LEU   B HD12 1 
ATOM   5814 H HD13 . LEU   B 1 123 ? 45.810 -22.757 -11.975 1.00 14.22 ?  123 LEU   B HD13 1 
ATOM   5815 H HD21 . LEU   B 1 123 ? 48.242 -22.087 -10.424 1.00 14.59 ?  123 LEU   B HD21 1 
ATOM   5816 H HD22 . LEU   B 1 123 ? 47.691 -21.072 -11.515 1.00 14.59 ?  123 LEU   B HD22 1 
ATOM   5817 H HD23 . LEU   B 1 123 ? 47.912 -20.587 -10.019 1.00 14.59 ?  123 LEU   B HD23 1 
ATOM   5818 N N    . ALA   B 1 124 ? 43.389 -22.375 -8.250  1.00 10.21 ?  124 ALA   B N    1 
ATOM   5819 C CA   . ALA   B 1 124 ? 43.124 -22.690 -6.854  1.00 10.46 ?  124 ALA   B CA   1 
ATOM   5820 C C    . ALA   B 1 124 ? 43.404 -24.149 -6.532  1.00 10.09 ?  124 ALA   B C    1 
ATOM   5821 O O    . ALA   B 1 124 ? 43.274 -25.026 -7.399  1.00 10.55 ?  124 ALA   B O    1 
ATOM   5822 C CB   . ALA   B 1 124 ? 41.667 -22.383 -6.493  1.00 10.72 ?  124 ALA   B CB   1 
ATOM   5823 H H    . ALA   B 1 124 ? 43.237 -23.022 -8.809  1.00 12.27 ?  124 ALA   B H    1 
ATOM   5824 H HA   . ALA   B 1 124 ? 43.694 -22.133 -6.308  1.00 12.56 ?  124 ALA   B HA   1 
ATOM   5825 H HB1  . ALA   B 1 124 ? 41.513 -22.591 -5.558  1.00 12.88 ?  124 ALA   B HB1  1 
ATOM   5826 H HB2  . ALA   B 1 124 ? 41.495 -21.433 -6.645  1.00 12.88 ?  124 ALA   B HB2  1 
ATOM   5827 H HB3  . ALA   B 1 124 ? 41.076 -22.910 -7.051  1.00 12.88 ?  124 ALA   B HB3  1 
ATOM   5828 N N    . PRO   B 1 125 ? 43.693 -24.444 -5.267  1.00 10.14 ?  125 PRO   B N    1 
ATOM   5829 C CA   . PRO   B 1 125 ? 43.636 -25.809 -4.745  1.00 11.09 ?  125 PRO   B CA   1 
ATOM   5830 C C    . PRO   B 1 125 ? 42.235 -26.089 -4.203  1.00 10.91 ?  125 PRO   B C    1 
ATOM   5831 O O    . PRO   B 1 125 ? 41.430 -25.177 -3.996  1.00 11.69 ?  125 PRO   B O    1 
ATOM   5832 C CB   . PRO   B 1 125 ? 44.623 -25.728 -3.575  1.00 12.27 ?  125 PRO   B CB   1 
ATOM   5833 C CG   . PRO   B 1 125 ? 44.350 -24.345 -2.999  1.00 12.14 ?  125 PRO   B CG   1 
ATOM   5834 C CD   . PRO   B 1 125 ? 44.015 -23.470 -4.205  1.00 11.10 ?  125 PRO   B CD   1 
ATOM   5835 H HA   . PRO   B 1 125 ? 43.911 -26.472 -5.393  1.00 13.33 ?  125 PRO   B HA   1 
ATOM   5836 H HB2  . PRO   B 1 125 ? 44.426 -26.417 -2.920  1.00 14.73 ?  125 PRO   B HB2  1 
ATOM   5837 H HB3  . PRO   B 1 125 ? 45.531 -25.794 -3.897  1.00 14.73 ?  125 PRO   B HB3  1 
ATOM   5838 H HG2  . PRO   B 1 125 ? 43.593 -24.377 -2.386  1.00 14.58 ?  125 PRO   B HG2  1 
ATOM   5839 H HG3  . PRO   B 1 125 ? 45.139 -24.009 -2.541  1.00 14.58 ?  125 PRO   B HG3  1 
ATOM   5840 H HD2  . PRO   B 1 125 ? 43.251 -22.899 -4.019  1.00 13.33 ?  125 PRO   B HD2  1 
ATOM   5841 H HD3  . PRO   B 1 125 ? 44.792 -22.936 -4.463  1.00 13.33 ?  125 PRO   B HD3  1 
ATOM   5842 N N    . LEU   B 1 126 ? 41.968 -27.371 -3.935  1.00 11.49 ?  126 LEU   B N    1 
ATOM   5843 C CA   . LEU   B 1 126 ? 40.747 -27.741 -3.226  1.00 12.05 ?  126 LEU   B CA   1 
ATOM   5844 C C    . LEU   B 1 126 ? 40.860 -27.341 -1.761  1.00 12.00 ?  126 LEU   B C    1 
ATOM   5845 O O    . LEU   B 1 126 ? 41.754 -27.798 -1.043  1.00 13.78 ?  126 LEU   B O    1 
ATOM   5846 C CB   . LEU   B 1 126 ? 40.487 -29.237 -3.350  1.00 13.33 ?  126 LEU   B CB   1 
ATOM   5847 C CG   . LEU   B 1 126 ? 39.954 -29.718 -4.701  1.00 14.22 ?  126 LEU   B CG   1 
ATOM   5848 C CD1  . LEU   B 1 126 ? 40.019 -31.231 -4.790  1.00 15.90 ?  126 LEU   B CD1  1 
ATOM   5849 C CD2  . LEU   B 1 126 ? 38.530 -29.236 -4.929  1.00 14.49 ?  126 LEU   B CD2  1 
ATOM   5850 H H    . LEU   B 1 126 ? 42.481 -28.038 -4.131  1.00 13.80 ?  126 LEU   B H    1 
ATOM   5851 H HA   . LEU   B 1 126 ? 40.001 -27.264 -3.613  1.00 14.47 ?  126 LEU   B HA   1 
ATOM   5852 H HB2  . LEU   B 1 126 ? 41.317 -29.706 -3.184  1.00 16.02 ?  126 LEU   B HB2  1 
ATOM   5853 H HB3  . LEU   B 1 126 ? 39.833 -29.489 -2.677  1.00 16.02 ?  126 LEU   B HB3  1 
ATOM   5854 H HG   . LEU   B 1 126 ? 40.510 -29.355 -5.408  1.00 17.08 ?  126 LEU   B HG   1 
ATOM   5855 H HD11 . LEU   B 1 126 ? 39.674 -31.515 -5.652  1.00 19.10 ?  126 LEU   B HD11 1 
ATOM   5856 H HD12 . LEU   B 1 126 ? 40.940 -31.517 -4.692  1.00 19.10 ?  126 LEU   B HD12 1 
ATOM   5857 H HD13 . LEU   B 1 126 ? 39.477 -31.614 -4.078  1.00 19.10 ?  126 LEU   B HD13 1 
ATOM   5858 H HD21 . LEU   B 1 126 ? 38.186 -29.633 -5.745  1.00 17.41 ?  126 LEU   B HD21 1 
ATOM   5859 H HD22 . LEU   B 1 126 ? 37.980 -29.501 -4.176  1.00 17.41 ?  126 LEU   B HD22 1 
ATOM   5860 H HD23 . LEU   B 1 126 ? 38.531 -28.268 -5.011  1.00 17.41 ?  126 LEU   B HD23 1 
ATOM   5861 N N    . LEU   B 1 127 ? 39.936 -26.502 -1.308  1.00 11.81 ?  127 LEU   B N    1 
ATOM   5862 C CA   . LEU   B 1 127 ? 39.982 -26.019 0.060   1.00 12.20 ?  127 LEU   B CA   1 
ATOM   5863 C C    . LEU   B 1 127 ? 39.713 -27.145 1.053   1.00 12.00 ?  127 LEU   B C    1 
ATOM   5864 O O    . LEU   B 1 127 ? 38.894 -28.045 0.820   1.00 12.21 ?  127 LEU   B O    1 
ATOM   5865 C CB   . LEU   B 1 127 ? 38.966 -24.892 0.271   1.00 12.76 ?  127 LEU   B CB   1 
ATOM   5866 C CG   . LEU   B 1 127 ? 39.138 -23.630 -0.577  1.00 13.42 ?  127 LEU   B CG   1 
ATOM   5867 C CD1  . LEU   B 1 127 ? 38.020 -22.662 -0.239  1.00 13.35 ?  127 LEU   B CD1  1 
ATOM   5868 C CD2  . LEU   B 1 127 ? 40.503 -22.990 -0.361  1.00 14.15 ?  127 LEU   B CD2  1 
ATOM   5869 H H    . LEU   B 1 127 ? 39.276 -26.190 -1.770  1.00 14.19 ?  127 LEU   B H    1 
ATOM   5870 H HA   . LEU   B 1 127 ? 40.866 -25.661 0.242   1.00 14.66 ?  127 LEU   B HA   1 
ATOM   5871 H HB2  . LEU   B 1 127 ? 38.083 -25.242 0.084   1.00 15.32 ?  127 LEU   B HB2  1 
ATOM   5872 H HB3  . LEU   B 1 127 ? 39.009 -24.614 1.201   1.00 15.32 ?  127 LEU   B HB3  1 
ATOM   5873 H HG   . LEU   B 1 127 ? 39.049 -23.862 -1.512  1.00 16.12 ?  127 LEU   B HG   1 
ATOM   5874 H HD11 . LEU   B 1 127 ? 38.124 -21.857 -0.772  1.00 16.04 ?  127 LEU   B HD11 1 
ATOM   5875 H HD12 . LEU   B 1 127 ? 37.164 -23.077 -0.434  1.00 16.04 ?  127 LEU   B HD12 1 
ATOM   5876 H HD13 . LEU   B 1 127 ? 38.067 -22.437 0.706   1.00 16.04 ?  127 LEU   B HD13 1 
ATOM   5877 H HD21 . LEU   B 1 127 ? 40.535 -22.146 -0.840  1.00 16.99 ?  127 LEU   B HD21 1 
ATOM   5878 H HD22 . LEU   B 1 127 ? 40.635 -22.836 0.588   1.00 16.99 ?  127 LEU   B HD22 1 
ATOM   5879 H HD23 . LEU   B 1 127 ? 41.185 -23.589 -0.699  1.00 16.99 ?  127 LEU   B HD23 1 
ATOM   5880 N N    . SER   B 1 128 ? 40.396 -27.056 2.186   1.00 12.01 ?  128 SER   B N    1 
ATOM   5881 C CA   . SER   B 1 128 ? 40.295 -27.977 3.308   1.00 12.55 ?  128 SER   B CA   1 
ATOM   5882 C C    . SER   B 1 128 ? 40.783 -29.383 2.980   1.00 13.34 ?  128 SER   B C    1 
ATOM   5883 O O    . SER   B 1 128 ? 40.708 -30.260 3.837   1.00 14.84 ?  128 SER   B O    1 
ATOM   5884 C CB   . SER   B 1 128 ? 38.901 -27.988 3.947   1.00 12.99 ?  128 SER   B CB   1 
ATOM   5885 O OG   . SER   B 1 128 ? 38.577 -26.716 4.493   1.00 13.51 ?  128 SER   B OG   1 
ATOM   5886 H H    . SER   B 1 128 ? 40.959 -26.421 2.343   1.00 14.43 ?  128 SER   B H    1 
ATOM   5887 H HA   . SER   B 1 128 ? 40.889 -27.642 3.995   1.00 15.07 ?  128 SER   B HA   1 
ATOM   5888 H HB2  . SER   B 1 128 ? 38.242 -28.229 3.278   1.00 15.60 ?  128 SER   B HB2  1 
ATOM   5889 H HB3  . SER   B 1 128 ? 38.889 -28.658 4.665   1.00 15.60 ?  128 SER   B HB3  1 
ATOM   5890 H HG   . SER   B 1 128 ? 39.142 -26.514 5.082   1.00 16.23 ?  128 SER   B HG   1 
ATOM   5891 N N    . ALA   B 1 129 ? 41.355 -29.601 1.795   1.00 14.12 ?  129 ALA   B N    1 
ATOM   5892 C CA   . ALA   B 1 129 ? 41.907 -30.895 1.434   1.00 15.11 ?  129 ALA   B CA   1 
ATOM   5893 C C    . ALA   B 1 129 ? 43.299 -31.068 2.032   1.00 14.18 ?  129 ALA   B C    1 
ATOM   5894 O O    . ALA   B 1 129 ? 43.863 -30.162 2.663   1.00 14.46 ?  129 ALA   B O    1 
ATOM   5895 C CB   . ALA   B 1 129 ? 41.952 -31.046 -0.083  1.00 16.98 ?  129 ALA   B CB   1 
ATOM   5896 H H    . ALA   B 1 129 ? 41.433 -29.005 1.181   1.00 16.96 ?  129 ALA   B H    1 
ATOM   5897 H HA   . ALA   B 1 129 ? 41.337 -31.591 1.790   1.00 18.15 ?  129 ALA   B HA   1 
ATOM   5898 H HB1  . ALA   B 1 129 ? 42.316 -31.918 -0.302  1.00 20.39 ?  129 ALA   B HB1  1 
ATOM   5899 H HB2  . ALA   B 1 129 ? 41.051 -30.966 -0.434  1.00 20.39 ?  129 ALA   B HB2  1 
ATOM   5900 H HB3  . ALA   B 1 129 ? 42.515 -30.349 -0.454  1.00 20.39 ?  129 ALA   B HB3  1 
ATOM   5901 N N    . GLY   B 1 130 ? 43.848 -32.265 1.832   1.00 14.00 ?  130 GLY   B N    1 
ATOM   5902 C CA   . GLY   B 1 130 ? 45.238 -32.502 2.175   1.00 14.74 ?  130 GLY   B CA   1 
ATOM   5903 C C    . GLY   B 1 130 ? 45.455 -32.404 3.668   1.00 14.81 ?  130 GLY   B C    1 
ATOM   5904 O O    . GLY   B 1 130 ? 44.758 -33.047 4.468   1.00 15.86 ?  130 GLY   B O    1 
ATOM   5905 H H    . GLY   B 1 130 ? 43.441 -32.943 1.495   1.00 16.81 ?  130 GLY   B H    1 
ATOM   5906 H HA2  . GLY   B 1 130 ? 45.502 -33.390 1.878   1.00 17.71 ?  130 GLY   B HA2  1 
ATOM   5907 H HA3  . GLY   B 1 130 ? 45.804 -31.849 1.730   1.00 17.71 ?  130 GLY   B HA3  1 
ATOM   5908 N N    . ILE   B 1 131 ? 46.428 -31.573 4.057   1.00 15.41 ?  131 ILE   B N    1 
ATOM   5909 C CA   . ILE   B 1 131 ? 46.776 -31.436 5.464   1.00 16.00 ?  131 ILE   B CA   1 
ATOM   5910 C C    . ILE   B 1 131 ? 45.656 -30.841 6.297   1.00 15.31 ?  131 ILE   B C    1 
ATOM   5911 O O    . ILE   B 1 131 ? 45.730 -30.911 7.529   1.00 16.70 ?  131 ILE   B O    1 
ATOM   5912 C CB   . ILE   B 1 131 ? 48.090 -30.650 5.672   1.00 18.13 ?  131 ILE   B CB   1 
ATOM   5913 C CG1  . ILE   B 1 131 ? 47.923 -29.171 5.294   1.00 19.09 ?  131 ILE   B CG1  1 
ATOM   5914 C CG2  . ILE   B 1 131 ? 49.227 -31.295 4.879   1.00 19.14 ?  131 ILE   B CG2  1 
ATOM   5915 C CD1  . ILE   B 1 131 ? 49.143 -28.319 5.612   1.00 20.06 ?  131 ILE   B CD1  1 
ATOM   5916 H H    . ILE   B 1 131 ? 46.896 -31.082 3.524   1.00 18.51 ?  131 ILE   B H    1 
ATOM   5917 H HA   . ILE   B 1 131 ? 46.924 -32.327 5.811   1.00 19.21 ?  131 ILE   B HA   1 
ATOM   5918 H HB   . ILE   B 1 131 ? 48.312 -30.695 6.615   1.00 21.77 ?  131 ILE   B HB   1 
ATOM   5919 H HG12 . ILE   B 1 131 ? 47.753 -29.111 4.341   1.00 22.92 ?  131 ILE   B HG12 1 
ATOM   5920 H HG13 . ILE   B 1 131 ? 47.171 -28.797 5.783   1.00 22.92 ?  131 ILE   B HG13 1 
ATOM   5921 H HG21 . ILE   B 1 131 ? 50.065 -30.894 5.151   1.00 22.98 ?  131 ILE   B HG21 1 
ATOM   5922 H HG22 . ILE   B 1 131 ? 49.236 -32.245 5.062   1.00 22.98 ?  131 ILE   B HG22 1 
ATOM   5923 H HG23 . ILE   B 1 131 ? 49.074 -31.141 3.933   1.00 22.98 ?  131 ILE   B HG23 1 
ATOM   5924 H HD11 . ILE   B 1 131 ? 48.927 -27.389 5.444   1.00 24.08 ?  131 ILE   B HD11 1 
ATOM   5925 H HD12 . ILE   B 1 131 ? 49.377 -28.443 6.545   1.00 24.08 ?  131 ILE   B HD12 1 
ATOM   5926 H HD13 . ILE   B 1 131 ? 49.877 -28.598 5.045   1.00 24.08 ?  131 ILE   B HD13 1 
ATOM   5927 N N    . PHE   B 1 132 ? 44.628 -30.256 5.667   1.00 13.97 ?  132 PHE   B N    1 
ATOM   5928 C CA   . PHE   B 1 132 ? 43.463 -29.760 6.394   1.00 14.34 ?  132 PHE   B CA   1 
ATOM   5929 C C    . PHE   B 1 132 ? 42.438 -30.855 6.710   1.00 15.42 ?  132 PHE   B C    1 
ATOM   5930 O O    . PHE   B 1 132 ? 41.518 -30.606 7.499   1.00 17.13 ?  132 PHE   B O    1 
ATOM   5931 C CB   . PHE   B 1 132 ? 42.790 -28.626 5.609   1.00 13.56 ?  132 PHE   B CB   1 
ATOM   5932 C CG   . PHE   B 1 132 ? 43.486 -27.284 5.724   1.00 13.61 ?  132 PHE   B CG   1 
ATOM   5933 C CD1  . PHE   B 1 132 ? 44.780 -27.096 5.254   1.00 14.93 ?  132 PHE   B CD1  1 
ATOM   5934 C CD2  . PHE   B 1 132 ? 42.813 -26.189 6.251   1.00 13.40 ?  132 PHE   B CD2  1 
ATOM   5935 C CE1  . PHE   B 1 132 ? 45.399 -25.853 5.350   1.00 15.59 ?  132 PHE   B CE1  1 
ATOM   5936 C CE2  . PHE   B 1 132 ? 43.425 -24.945 6.343   1.00 13.90 ?  132 PHE   B CE2  1 
ATOM   5937 C CZ   . PHE   B 1 132 ? 44.714 -24.781 5.890   1.00 15.06 ?  132 PHE   B CZ   1 
ATOM   5938 H H    . PHE   B 1 132 ? 44.585 -30.137 4.813   1.00 16.78 ?  132 PHE   B H    1 
ATOM   5939 H HA   . PHE   B 1 132 ? 43.766 -29.387 7.234   1.00 17.22 ?  132 PHE   B HA   1 
ATOM   5940 H HB2  . PHE   B 1 132 ? 42.780 -28.865 4.670   1.00 16.29 ?  132 PHE   B HB2  1 
ATOM   5941 H HB3  . PHE   B 1 132 ? 41.884 -28.516 5.933   1.00 16.29 ?  132 PHE   B HB3  1 
ATOM   5942 H HD1  . PHE   B 1 132 ? 45.248 -27.818 4.892   1.00 17.94 ?  132 PHE   B HD1  1 
ATOM   5943 H HD2  . PHE   B 1 132 ? 41.943 -26.295 6.559   1.00 16.09 ?  132 PHE   B HD2  1 
ATOM   5944 H HE1  . PHE   B 1 132 ? 46.272 -25.746 5.044   1.00 18.72 ?  132 PHE   B HE1  1 
ATOM   5945 H HE2  . PHE   B 1 132 ? 42.966 -24.222 6.710   1.00 16.69 ?  132 PHE   B HE2  1 
ATOM   5946 H HZ   . PHE   B 1 132 ? 45.131 -23.947 5.955   1.00 18.09 ?  132 PHE   B HZ   1 
ATOM   5947 N N    . GLY   B 1 133 ? 42.547 -32.045 6.106   1.00 15.26 ?  133 GLY   B N    1 
ATOM   5948 C CA   . GLY   B 1 133 ? 41.837 -33.218 6.589   1.00 15.88 ?  133 GLY   B CA   1 
ATOM   5949 C C    . GLY   B 1 133 ? 40.439 -33.475 6.056   1.00 15.93 ?  133 GLY   B C    1 
ATOM   5950 O O    . GLY   B 1 133 ? 39.843 -34.490 6.430   1.00 18.21 ?  133 GLY   B O    1 
ATOM   5951 H H    . GLY   B 1 133 ? 43.044 -32.190 5.416   1.00 18.32 ?  133 GLY   B H    1 
ATOM   5952 H HA2  . GLY   B 1 133 ? 42.373 -33.997 6.382   1.00 19.07 ?  133 GLY   B HA2  1 
ATOM   5953 H HA3  . GLY   B 1 133 ? 41.776 -33.152 7.554   1.00 19.07 ?  133 GLY   B HA3  1 
ATOM   5954 N N    . ALA   B 1 134 ? 39.883 -32.608 5.216   1.00 15.15 ?  134 ALA   B N    1 
ATOM   5955 C CA   . ALA   B 1 134 ? 38.558 -32.882 4.680   1.00 15.54 ?  134 ALA   B CA   1 
ATOM   5956 C C    . ALA   B 1 134 ? 38.638 -33.878 3.528   1.00 15.72 ?  134 ALA   B C    1 
ATOM   5957 O O    . ALA   B 1 134 ? 39.689 -34.077 2.915   1.00 17.16 ?  134 ALA   B O    1 
ATOM   5958 C CB   . ALA   B 1 134 ? 37.887 -31.594 4.205   1.00 16.18 ?  134 ALA   B CB   1 
ATOM   5959 H H    . ALA   B 1 134 ? 40.244 -31.867 4.949   1.00 18.20 ?  134 ALA   B H    1 
ATOM   5960 H HA   . ALA   B 1 134 ? 38.009 -33.264 5.382   1.00 18.67 ?  134 ALA   B HA   1 
ATOM   5961 H HB1  . ALA   B 1 134 ? 37.002 -31.806 3.868   1.00 19.43 ?  134 ALA   B HB1  1 
ATOM   5962 H HB2  . ALA   B 1 134 ? 37.816 -30.977 4.952   1.00 19.43 ?  134 ALA   B HB2  1 
ATOM   5963 H HB3  . ALA   B 1 134 ? 38.423 -31.198 3.500   1.00 19.43 ?  134 ALA   B HB3  1 
ATOM   5964 N N    . ASP   B 1 135 ? 37.504 -34.503 3.240   1.00 15.60 ?  135 ASP   B N    1 
ATOM   5965 C CA   . ASP   B 1 135 ? 37.405 -35.405 2.099   1.00 16.38 ?  135 ASP   B CA   1 
ATOM   5966 C C    . ASP   B 1 135 ? 37.509 -34.570 0.830   1.00 15.25 ?  135 ASP   B C    1 
ATOM   5967 O O    . ASP   B 1 135 ? 36.662 -33.693 0.609   1.00 15.44 ?  135 ASP   B O    1 
ATOM   5968 C CB   . ASP   B 1 135 ? 36.060 -36.133 2.156   1.00 18.05 ?  135 ASP   B CB   1 
ATOM   5969 C CG   . ASP   B 1 135 ? 35.863 -37.115 1.012   1.00 20.18 ?  135 ASP   B CG   1 
ATOM   5970 O OD1  . ASP   B 1 135 ? 36.736 -37.184 0.119   1.00 20.00 ?  135 ASP   B OD1  1 
ATOM   5971 O OD2  . ASP   B 1 135 ? 34.834 -37.837 1.022   1.00 23.19 -1 135 ASP   B OD2  1 
ATOM   5972 H H    . ASP   B 1 135 ? 36.776 -34.426 3.692   1.00 18.74 ?  135 ASP   B H    1 
ATOM   5973 H HA   . ASP   B 1 135 ? 38.123 -36.060 2.134   1.00 19.67 ?  135 ASP   B HA   1 
ATOM   5974 H HB2  . ASP   B 1 135 ? 36.009 -36.625 2.987   1.00 21.67 ?  135 ASP   B HB2  1 
ATOM   5975 H HB3  . ASP   B 1 135 ? 35.352 -35.472 2.114   1.00 21.67 ?  135 ASP   B HB3  1 
ATOM   5976 N N    . PRO   B 1 136 ? 38.524 -34.777 -0.016  1.00 15.33 ?  136 PRO   B N    1 
ATOM   5977 C CA   . PRO   B 1 136 ? 38.625 -33.953 -1.231  1.00 14.74 ?  136 PRO   B CA   1 
ATOM   5978 C C    . PRO   B 1 136 ? 37.437 -34.104 -2.160  1.00 14.23 ?  136 PRO   B C    1 
ATOM   5979 O O    . PRO   B 1 136 ? 37.118 -33.155 -2.886  1.00 13.61 ?  136 PRO   B O    1 
ATOM   5980 C CB   . PRO   B 1 136 ? 39.933 -34.433 -1.877  1.00 15.87 ?  136 PRO   B CB   1 
ATOM   5981 C CG   . PRO   B 1 136 ? 40.130 -35.826 -1.342  1.00 16.87 ?  136 PRO   B CG   1 
ATOM   5982 C CD   . PRO   B 1 136 ? 39.602 -35.777 0.064   1.00 16.36 ?  136 PRO   B CD   1 
ATOM   5983 H HA   . PRO   B 1 136 ? 38.717 -33.016 -0.996  1.00 17.71 ?  136 PRO   B HA   1 
ATOM   5984 H HB2  . PRO   B 1 136 ? 39.838 -34.446 -2.845  1.00 19.06 ?  136 PRO   B HB2  1 
ATOM   5985 H HB3  . PRO   B 1 136 ? 40.662 -33.852 -1.612  1.00 19.06 ?  136 PRO   B HB3  1 
ATOM   5986 H HG2  . PRO   B 1 136 ? 39.626 -36.461 -1.874  1.00 20.26 ?  136 PRO   B HG2  1 
ATOM   5987 H HG3  . PRO   B 1 136 ? 41.075 -36.050 -1.344  1.00 20.26 ?  136 PRO   B HG3  1 
ATOM   5988 H HD2  . PRO   B 1 136 ? 39.244 -36.639 0.325   1.00 19.65 ?  136 PRO   B HD2  1 
ATOM   5989 H HD3  . PRO   B 1 136 ? 40.291 -35.477 0.681   1.00 19.65 ?  136 PRO   B HD3  1 
ATOM   5990 N N    . ILE   B 1 137 ? 36.775 -35.266 -2.163  1.00 14.58 ?  137 ILE   B N    1 
ATOM   5991 C CA   . ILE   B 1 137 ? 35.562 -35.431 -2.962  1.00 15.17 ?  137 ILE   B CA   1 
ATOM   5992 C C    . ILE   B 1 137 ? 34.485 -34.463 -2.490  1.00 14.54 ?  137 ILE   B C    1 
ATOM   5993 O O    . ILE   B 1 137 ? 33.775 -33.846 -3.295  1.00 14.28 ?  137 ILE   B O    1 
ATOM   5994 C CB   . ILE   B 1 137 ? 35.088 -36.898 -2.907  1.00 17.34 ?  137 ILE   B CB   1 
ATOM   5995 C CG1  . ILE   B 1 137 ? 36.100 -37.801 -3.622  1.00 19.90 ?  137 ILE   B CG1  1 
ATOM   5996 C CG2  . ILE   B 1 137 ? 33.695 -37.037 -3.513  1.00 17.88 ?  137 ILE   B CG2  1 
ATOM   5997 C CD1  . ILE   B 1 137 ? 35.787 -39.283 -3.531  1.00 22.37 ?  137 ILE   B CD1  1 
ATOM   5998 H H    . ILE   B 1 137 ? 37.003 -35.964 -1.720  1.00 17.51 ?  137 ILE   B H    1 
ATOM   5999 H HA   . ILE   B 1 137 ? 35.759 -35.223 -3.889  1.00 18.22 ?  137 ILE   B HA   1 
ATOM   6000 H HB   . ILE   B 1 137 ? 35.039 -37.170 -1.982  1.00 20.82 ?  137 ILE   B HB   1 
ATOM   6001 H HG12 . ILE   B 1 137 ? 36.126 -37.563 -4.562  1.00 23.89 ?  137 ILE   B HG12 1 
ATOM   6002 H HG13 . ILE   B 1 137 ? 36.973 -37.661 -3.224  1.00 23.89 ?  137 ILE   B HG13 1 
ATOM   6003 H HG21 . ILE   B 1 137 ? 33.482 -37.981 -3.623  1.00 21.47 ?  137 ILE   B HG21 1 
ATOM   6004 H HG22 . ILE   B 1 137 ? 33.044 -36.633 -2.919  1.00 21.47 ?  137 ILE   B HG22 1 
ATOM   6005 H HG23 . ILE   B 1 137 ? 33.676 -36.598 -4.377  1.00 21.47 ?  137 ILE   B HG23 1 
ATOM   6006 H HD11 . ILE   B 1 137 ? 36.562 -39.784 -3.827  1.00 26.86 ?  137 ILE   B HD11 1 
ATOM   6007 H HD12 . ILE   B 1 137 ? 35.580 -39.507 -2.610  1.00 26.86 ?  137 ILE   B HD12 1 
ATOM   6008 H HD13 . ILE   B 1 137 ? 35.028 -39.485 -4.100  1.00 26.86 ?  137 ILE   B HD13 1 
ATOM   6009 N N    . HIS   B 1 138 ? 34.351 -34.315 -1.175  1.00 14.50 ?  138 HIS   B N    1 
ATOM   6010 C CA   . HIS   B 1 138 ? 33.406 -33.346 -0.637  1.00 14.79 ?  138 HIS   B CA   1 
ATOM   6011 C C    . HIS   B 1 138 ? 33.829 -31.917 -0.952  1.00 13.98 ?  138 HIS   B C    1 
ATOM   6012 O O    . HIS   B 1 138 ? 32.983 -31.070 -1.254  1.00 14.77 ?  138 HIS   B O    1 
ATOM   6013 C CB   . HIS   B 1 138 ? 33.281 -33.522 0.869   1.00 16.04 ?  138 HIS   B CB   1 
ATOM   6014 C CG   . HIS   B 1 138 ? 32.339 -32.549 1.498   1.00 16.95 ?  138 HIS   B CG   1 
ATOM   6015 N ND1  . HIS   B 1 138 ? 31.000 -32.493 1.174   1.00 18.36 ?  138 HIS   B ND1  1 
ATOM   6016 C CD2  . HIS   B 1 138 ? 32.548 -31.565 2.404   1.00 17.72 ?  138 HIS   B CD2  1 
ATOM   6017 C CE1  . HIS   B 1 138 ? 30.420 -31.531 1.868   1.00 18.44 ?  138 HIS   B CE1  1 
ATOM   6018 N NE2  . HIS   B 1 138 ? 31.339 -30.951 2.622   1.00 18.00 ?  138 HIS   B NE2  1 
ATOM   6019 H H    . HIS   B 1 138 ? 34.792 -34.756 -0.586  1.00 17.42 ?  138 HIS   B H    1 
ATOM   6020 H HA   . HIS   B 1 138 ? 32.533 -33.502 -1.036  1.00 17.76 ?  138 HIS   B HA   1 
ATOM   6021 H HB2  . HIS   B 1 138 ? 32.950 -34.414 1.054   1.00 19.26 ?  138 HIS   B HB2  1 
ATOM   6022 H HB3  . HIS   B 1 138 ? 34.151 -33.398 1.272   1.00 19.26 ?  138 HIS   B HB3  1 
ATOM   6023 H HD1  . HIS   B 1 138 ? 30.603 -33.014 0.613   1.00 22.04 ?  138 HIS   B HD1  1 
ATOM   6024 H HD2  . HIS   B 1 138 ? 33.350 -31.346 2.812   1.00 21.28 ?  138 HIS   B HD2  1 
ATOM   6025 H HE1  . HIS   B 1 138 ? 29.514 -31.307 1.831   1.00 22.15 ?  138 HIS   B HE1  1 
ATOM   6026 N N    . SER   B 1 139 ? 35.122 -31.618 -0.868  1.00 13.61 ?  139 SER   B N    1 
ATOM   6027 C CA   . SER   B 1 139 ? 35.562 -30.268 -1.188  1.00 12.92 ?  139 SER   B CA   1 
ATOM   6028 C C    . SER   B 1 139 ? 35.221 -29.918 -2.628  1.00 12.30 ?  139 SER   B C    1 
ATOM   6029 O O    . SER   B 1 139 ? 34.769 -28.803 -2.906  1.00 12.52 ?  139 SER   B O    1 
ATOM   6030 C CB   . SER   B 1 139 ? 37.055 -30.129 -0.917  1.00 13.33 ?  139 SER   B CB   1 
ATOM   6031 O OG   . SER   B 1 139 ? 37.463 -28.808 -1.199  1.00 13.54 ?  139 SER   B OG   1 
ATOM   6032 H H    . SER   B 1 139 ? 35.742 -32.166 -0.645  1.00 16.35 ?  139 SER   B H    1 
ATOM   6033 H HA   . SER   B 1 139 ? 35.093 -29.646 -0.619  1.00 15.52 ?  139 SER   B HA   1 
ATOM   6034 H HB2  . SER   B 1 139 ? 37.231 -30.321 0.017   1.00 16.01 ?  139 SER   B HB2  1 
ATOM   6035 H HB3  . SER   B 1 139 ? 37.549 -30.742 -1.485  1.00 16.01 ?  139 SER   B HB3  1 
ATOM   6036 H HG   . SER   B 1 139 ? 37.086 -28.266 -0.679  1.00 16.26 ?  139 SER   B HG   1 
ATOM   6037 N N    . LEU   B 1 140 ? 35.413 -30.858 -3.555  1.00 12.08 ?  140 LEU   B N    1 
ATOM   6038 C CA   . LEU   B 1 140 ? 35.050 -30.610 -4.943  1.00 12.24 ?  140 LEU   B CA   1 
ATOM   6039 C C    . LEU   B 1 140 ? 33.547 -30.384 -5.077  1.00 12.61 ?  140 LEU   B C    1 
ATOM   6040 O O    . LEU   B 1 140 ? 33.106 -29.501 -5.818  1.00 12.65 ?  140 LEU   B O    1 
ATOM   6041 C CB   . LEU   B 1 140 ? 35.526 -31.770 -5.820  1.00 12.63 ?  140 LEU   B CB   1 
ATOM   6042 C CG   . LEU   B 1 140 ? 35.152 -31.664 -7.295  1.00 12.65 ?  140 LEU   B CG   1 
ATOM   6043 C CD1  . LEU   B 1 140 ? 35.728 -30.394 -7.903  1.00 13.54 ?  140 LEU   B CD1  1 
ATOM   6044 C CD2  . LEU   B 1 140 ? 35.640 -32.893 -8.033  1.00 13.87 ?  140 LEU   B CD2  1 
ATOM   6045 H H    . LEU   B 1 140 ? 35.745 -31.638 -3.408  1.00 14.51 ?  140 LEU   B H    1 
ATOM   6046 H HA   . LEU   B 1 140 ? 35.503 -29.806 -5.246  1.00 14.70 ?  140 LEU   B HA   1 
ATOM   6047 H HB2  . LEU   B 1 140 ? 36.497 -31.820 -5.771  1.00 15.17 ?  140 LEU   B HB2  1 
ATOM   6048 H HB3  . LEU   B 1 140 ? 35.144 -32.594 -5.484  1.00 15.17 ?  140 LEU   B HB3  1 
ATOM   6049 H HG   . LEU   B 1 140 ? 34.188 -31.620 -7.375  1.00 15.20 ?  140 LEU   B HG   1 
ATOM   6050 H HD11 . LEU   B 1 140 ? 35.593 -30.417 -8.862  1.00 16.26 ?  140 LEU   B HD11 1 
ATOM   6051 H HD12 . LEU   B 1 140 ? 35.271 -29.624 -7.525  1.00 16.26 ?  140 LEU   B HD12 1 
ATOM   6052 H HD13 . LEU   B 1 140 ? 36.675 -30.347 -7.702  1.00 16.26 ?  140 LEU   B HD13 1 
ATOM   6053 H HD21 . LEU   B 1 140 ? 35.391 -32.812 -8.968  1.00 16.66 ?  140 LEU   B HD21 1 
ATOM   6054 H HD22 . LEU   B 1 140 ? 36.598 -32.956 -7.945  1.00 16.66 ?  140 LEU   B HD22 1 
ATOM   6055 H HD23 . LEU   B 1 140 ? 35.213 -33.674 -7.645  1.00 16.66 ?  140 LEU   B HD23 1 
ATOM   6056 N N    . ARG   B 1 141 ? 32.747 -31.173 -4.356  1.00 12.69 ?  141 ARG   B N    1 
ATOM   6057 C CA   . ARG   B 1 141 ? 31.296 -31.002 -4.345  1.00 13.84 ?  141 ARG   B CA   1 
ATOM   6058 C C    . ARG   B 1 141 ? 30.917 -29.591 -3.917  1.00 13.32 ?  141 ARG   B C    1 
ATOM   6059 O O    . ARG   B 1 141 ? 30.111 -28.912 -4.574  1.00 13.49 ?  141 ARG   B O    1 
ATOM   6060 C CB   . ARG   B 1 141 ? 30.708 -32.028 -3.367  1.00 15.47 ?  141 ARG   B CB   1 
ATOM   6061 C CG   . ARG   B 1 141 ? 29.242 -31.910 -3.030  1.00 17.49 ?  141 ARG   B CG   1 
ATOM   6062 C CD   . ARG   B 1 141 ? 28.425 -32.543 -4.087  1.00 19.52 ?  141 ARG   B CD   1 
ATOM   6063 N NE   . ARG   B 1 141 ? 28.163 -31.633 -5.191  1.00 20.42 ?  141 ARG   B NE   1 
ATOM   6064 C CZ   . ARG   B 1 141 ? 28.161 -31.984 -6.469  1.00 20.18 ?  141 ARG   B CZ   1 
ATOM   6065 N NH1  . ARG   B 1 141 ? 28.599 -33.170 -6.864  1.00 20.09 ?  141 ARG   B NH1  1 
ATOM   6066 N NH2  . ARG   B 1 141 ? 27.706 -31.122 -7.374  1.00 20.97 ?  141 ARG   B NH2  1 
ATOM   6067 H H    . ARG   B 1 141 ? 33.026 -31.815 -3.860  1.00 15.24 ?  141 ARG   B H    1 
ATOM   6068 H HA   . ARG   B 1 141 ? 30.936 -31.169 -5.227  1.00 16.62 ?  141 ARG   B HA   1 
ATOM   6069 H HB2  . ARG   B 1 141 ? 30.853 -32.915 -3.737  1.00 18.58 ?  141 ARG   B HB2  1 
ATOM   6070 H HB3  . ARG   B 1 141 ? 31.196 -31.960 -2.531  1.00 18.58 ?  141 ARG   B HB3  1 
ATOM   6071 H HG2  . ARG   B 1 141 ? 29.073 -32.356 -2.189  1.00 21.00 ?  141 ARG   B HG2  1 
ATOM   6072 H HG3  . ARG   B 1 141 ? 28.992 -30.970 -2.964  1.00 21.00 ?  141 ARG   B HG3  1 
ATOM   6073 H HD2  . ARG   B 1 141 ? 28.898 -33.324 -4.426  1.00 23.44 ?  141 ARG   B HD2  1 
ATOM   6074 H HD3  . ARG   B 1 141 ? 27.581 -32.820 -3.706  1.00 23.44 ?  141 ARG   B HD3  1 
ATOM   6075 H HE   . ARG   B 1 141 ? 27.978 -30.816 -4.996  1.00 24.52 ?  141 ARG   B HE   1 
ATOM   6076 H HH11 . ARG   B 1 141 ? 28.884 -33.743 -6.292  1.00 24.12 ?  141 ARG   B HH11 1 
ATOM   6077 H HH12 . ARG   B 1 141 ? 28.597 -33.366 -7.699  1.00 24.12 ?  141 ARG   B HH12 1 
ATOM   6078 H HH21 . ARG   B 1 141 ? 27.425 -30.345 -7.128  1.00 25.18 ?  141 ARG   B HH21 1 
ATOM   6079 H HH22 . ARG   B 1 141 ? 27.721 -31.326 -8.210  1.00 25.18 ?  141 ARG   B HH22 1 
ATOM   6080 N N    . VAL   B 1 142 ? 31.469 -29.142 -2.792  1.00 12.92 ?  142 VAL   B N    1 
ATOM   6081 C CA   . VAL   B 1 142 ? 31.129 -27.813 -2.305  1.00 12.57 ?  142 VAL   B CA   1 
ATOM   6082 C C    . VAL   B 1 142 ? 31.598 -26.751 -3.292  1.00 12.58 ?  142 VAL   B C    1 
ATOM   6083 O O    . VAL   B 1 142 ? 30.894 -25.764 -3.545  1.00 12.82 ?  142 VAL   B O    1 
ATOM   6084 C CB   . VAL   B 1 142 ? 31.672 -27.583 -0.882  1.00 13.52 ?  142 VAL   B CB   1 
ATOM   6085 C CG1  . VAL   B 1 142 ? 31.340 -26.162 -0.410  1.00 13.38 ?  142 VAL   B CG1  1 
ATOM   6086 C CG2  . VAL   B 1 142 ? 31.104 -28.617 0.085   1.00 14.28 ?  142 VAL   B CG2  1 
ATOM   6087 H H    . VAL   B 1 142 ? 32.036 -29.576 -2.308  1.00 15.52 ?  142 VAL   B H    1 
ATOM   6088 H HA   . VAL   B 1 142 ? 30.171 -27.747 -2.251  1.00 15.10 ?  142 VAL   B HA   1 
ATOM   6089 H HB   . VAL   B 1 142 ? 32.640 -27.676 -0.885  1.00 16.23 ?  142 VAL   B HB   1 
ATOM   6090 H HG11 . VAL   B 1 142 ? 31.507 -26.100 0.542   1.00 16.08 ?  142 VAL   B HG11 1 
ATOM   6091 H HG12 . VAL   B 1 142 ? 31.902 -25.531 -0.887  1.00 16.08 ?  142 VAL   B HG12 1 
ATOM   6092 H HG13 . VAL   B 1 142 ? 30.406 -25.982 -0.597  1.00 16.08 ?  142 VAL   B HG13 1 
ATOM   6093 H HG21 . VAL   B 1 142 ? 31.431 -28.430 0.978   1.00 17.15 ?  142 VAL   B HG21 1 
ATOM   6094 H HG22 . VAL   B 1 142 ? 30.136 -28.562 0.068   1.00 17.15 ?  142 VAL   B HG22 1 
ATOM   6095 H HG23 . VAL   B 1 142 ? 31.390 -29.501 -0.195  1.00 17.15 ?  142 VAL   B HG23 1 
ATOM   6096 N N    . CYS   B 1 143 ? 32.783 -26.942 -3.880  1.00 12.15 ?  143 CYS   B N    1 
ATOM   6097 C CA   . CYS   B 1 143 ? 33.274 -26.001 -4.881  1.00 12.22 ?  143 CYS   B CA   1 
ATOM   6098 C C    . CYS   B 1 143 ? 32.273 -25.852 -6.020  1.00 11.92 ?  143 CYS   B C    1 
ATOM   6099 O O    . CYS   B 1 143 ? 31.871 -24.740 -6.377  1.00 12.27 ?  143 CYS   B O    1 
ATOM   6100 C CB   . CYS   B 1 143 ? 34.625 -26.489 -5.415  1.00 12.70 ?  143 CYS   B CB   1 
ATOM   6101 S SG   . CYS   B 1 143 ? 35.381 -25.381 -6.620  1.00 12.92 ?  143 CYS   B SG   1 
ATOM   6102 H H    . CYS   B 1 143 ? 33.317 -27.596 -3.717  1.00 14.59 ?  143 CYS   B H    1 
ATOM   6103 H HA   . CYS   B 1 143 ? 33.411 -25.130 -4.475  1.00 14.68 ?  143 CYS   B HA   1 
ATOM   6104 H HB2  . CYS   B 1 143 ? 35.247 -26.588 -4.673  1.00 15.26 ?  143 CYS   B HB2  1 
ATOM   6105 H HB3  . CYS   B 1 143 ? 34.502 -27.349 -5.844  1.00 15.26 ?  143 CYS   B HB3  1 
ATOM   6106 H HG   . CYS   B 1 143 ? 36.447 -25.829 -6.950  1.00 15.52 ?  143 CYS   B HG   1 
ATOM   6107 N N    . VAL   B 1 144 ? 31.868 -26.974 -6.613  1.00 12.48 ?  144 VAL   B N    1 
ATOM   6108 C CA   . VAL   B 1 144 ? 30.961 -26.914 -7.756  1.00 13.46 ?  144 VAL   B CA   1 
ATOM   6109 C C    . VAL   B 1 144 ? 29.621 -26.302 -7.377  1.00 13.62 ?  144 VAL   B C    1 
ATOM   6110 O O    . VAL   B 1 144 ? 29.007 -25.588 -8.183  1.00 14.93 ?  144 VAL   B O    1 
ATOM   6111 C CB   . VAL   B 1 144 ? 30.803 -28.321 -8.345  1.00 15.92 ?  144 VAL   B CB   1 
ATOM   6112 C CG1  . VAL   B 1 144 ? 29.549 -28.431 -9.206  1.00 18.57 ?  144 VAL   B CG1  1 
ATOM   6113 C CG2  . VAL   B 1 144 ? 32.061 -28.712 -9.114  1.00 15.96 ?  144 VAL   B CG2  1 
ATOM   6114 H H    . VAL   B 1 144 ? 32.101 -27.769 -6.380  1.00 15.00 ?  144 VAL   B H    1 
ATOM   6115 H HA   . VAL   B 1 144 ? 31.355 -26.354 -8.441  1.00 16.17 ?  144 VAL   B HA   1 
ATOM   6116 H HB   . VAL   B 1 144 ? 30.707 -28.953 -7.614  1.00 19.12 ?  144 VAL   B HB   1 
ATOM   6117 H HG11 . VAL   B 1 144 ? 29.636 -29.206 -9.786  1.00 22.30 ?  144 VAL   B HG11 1 
ATOM   6118 H HG12 . VAL   B 1 144 ? 28.780 -28.539 -8.628  1.00 22.30 ?  144 VAL   B HG12 1 
ATOM   6119 H HG13 . VAL   B 1 144 ? 29.461 -27.629 -9.741  1.00 22.30 ?  144 VAL   B HG13 1 
ATOM   6120 H HG21 . VAL   B 1 144 ? 31.948 -29.607 -9.472  1.00 19.17 ?  144 VAL   B HG21 1 
ATOM   6121 H HG22 . VAL   B 1 144 ? 32.194 -28.081 -9.840  1.00 19.17 ?  144 VAL   B HG22 1 
ATOM   6122 H HG23 . VAL   B 1 144 ? 32.819 -28.689 -8.511  1.00 19.17 ?  144 VAL   B HG23 1 
ATOM   6123 N N    . ASP   B 1 145 ? 29.154 -26.551 -6.157  1.00 13.56 ?  145 ASP   B N    1 
ATOM   6124 C CA   . ASP   B 1 145 ? 27.843 -26.081 -5.731  1.00 14.09 ?  145 ASP   B CA   1 
ATOM   6125 C C    . ASP   B 1 145 ? 27.872 -24.659 -5.182  1.00 13.75 ?  145 ASP   B C    1 
ATOM   6126 O O    . ASP   B 1 145 ? 26.808 -24.117 -4.858  1.00 15.72 ?  145 ASP   B O    1 
ATOM   6127 C CB   . ASP   B 1 145 ? 27.254 -26.998 -4.652  1.00 15.70 ?  145 ASP   B CB   1 
ATOM   6128 C CG   . ASP   B 1 145 ? 26.906 -28.378 -5.159  1.00 17.51 ?  145 ASP   B CG   1 
ATOM   6129 O OD1  . ASP   B 1 145 ? 26.806 -28.580 -6.385  1.00 17.73 ?  145 ASP   B OD1  1 
ATOM   6130 O OD2  . ASP   B 1 145 ? 26.720 -29.268 -4.304  1.00 20.02 -1 145 ASP   B OD2  1 
ATOM   6131 H H    . ASP   B 1 145 ? 29.587 -26.980 -5.553  1.00 16.29 ?  145 ASP   B H    1 
ATOM   6132 H HA   . ASP   B 1 145 ? 27.249 -26.078 -6.498  1.00 16.93 ?  145 ASP   B HA   1 
ATOM   6133 H HB2  . ASP   B 1 145 ? 27.893 -27.104 -3.946  1.00 18.86 ?  145 ASP   B HB2  1 
ATOM   6134 H HB3  . ASP   B 1 145 ? 26.436 -26.592 -4.318  1.00 18.86 ?  145 ASP   B HB3  1 
ATOM   6135 N N    . THR   B 1 146 ? 29.048 -24.043 -5.065  1.00 12.40 ?  146 THR   B N    1 
ATOM   6136 C CA   . THR   B 1 146 ? 29.180 -22.724 -4.453  1.00 12.06 ?  146 THR   B CA   1 
ATOM   6137 C C    . THR   B 1 146 ? 29.811 -21.690 -5.369  1.00 11.92 ?  146 THR   B C    1 
ATOM   6138 O O    . THR   B 1 146 ? 29.364 -20.530 -5.402  1.00 12.49 ?  146 THR   B O    1 
ATOM   6139 C CB   . THR   B 1 146 ? 30.014 -22.830 -3.166  1.00 12.61 ?  146 THR   B CB   1 
ATOM   6140 O OG1  . THR   B 1 146 ? 29.445 -23.821 -2.304  1.00 12.77 ?  146 THR   B OG1  1 
ATOM   6141 C CG2  . THR   B 1 146 ? 30.079 -21.495 -2.446  1.00 12.91 ?  146 THR   B CG2  1 
ATOM   6142 H H    . THR   B 1 146 ? 29.800 -24.377 -5.332  1.00 14.90 ?  146 THR   B H    1 
ATOM   6143 H HA   . THR   B 1 146 ? 28.305 -22.402 -4.212  1.00 14.49 ?  146 THR   B HA   1 
ATOM   6144 H HB   . THR   B 1 146 ? 30.922 -23.086 -3.394  1.00 15.14 ?  146 THR   B HB   1 
ATOM   6145 H HG1  . THR   B 1 146 ? 29.477 -24.580 -2.688  1.00 15.34 ?  146 THR   B HG1  1 
ATOM   6146 H HG21 . THR   B 1 146 ? 30.435 -21.617 -1.553  1.00 15.51 ?  146 THR   B HG21 1 
ATOM   6147 H HG22 . THR   B 1 146 ? 30.660 -20.881 -2.931  1.00 15.51 ?  146 THR   B HG22 1 
ATOM   6148 H HG23 . THR   B 1 146 ? 29.194 -21.107 -2.384  1.00 15.51 ?  146 THR   B HG23 1 
ATOM   6149 N N    . VAL   B 1 147 ? 30.871 -22.063 -6.076  1.00 11.91 ?  147 VAL   B N    1 
ATOM   6150 C CA   . VAL   B 1 147 ? 31.602 -21.118 -6.908  1.00 11.67 ?  147 VAL   B CA   1 
ATOM   6151 C C    . VAL   B 1 147 ? 30.875 -20.988 -8.232  1.00 11.73 ?  147 VAL   B C    1 
ATOM   6152 O O    . VAL   B 1 147 ? 30.510 -21.993 -8.857  1.00 12.68 ?  147 VAL   B O    1 
ATOM   6153 C CB   . VAL   B 1 147 ? 33.053 -21.580 -7.112  1.00 11.89 ?  147 VAL   B CB   1 
ATOM   6154 C CG1  . VAL   B 1 147 ? 33.823 -20.558 -7.937  1.00 12.07 ?  147 VAL   B CG1  1 
ATOM   6155 C CG2  . VAL   B 1 147 ? 33.733 -21.797 -5.776  1.00 11.96 ?  147 VAL   B CG2  1 
ATOM   6156 H H    . VAL   B 1 147 ? 31.194 -22.865 -6.096  1.00 14.31 ?  147 VAL   B H    1 
ATOM   6157 H HA   . VAL   B 1 147 ? 31.621 -20.251 -6.477  1.00 14.02 ?  147 VAL   B HA   1 
ATOM   6158 H HB   . VAL   B 1 147 ? 33.062 -22.427 -7.595  1.00 14.28 ?  147 VAL   B HB   1 
ATOM   6159 H HG11 . VAL   B 1 147 ? 34.768 -20.786 -7.924  1.00 14.49 ?  147 VAL   B HG11 1 
ATOM   6160 H HG12 . VAL   B 1 147 ? 33.496 -20.574 -8.850  1.00 14.49 ?  147 VAL   B HG12 1 
ATOM   6161 H HG13 . VAL   B 1 147 ? 33.691 -19.680 -7.550  1.00 14.49 ?  147 VAL   B HG13 1 
ATOM   6162 H HG21 . VAL   B 1 147 ? 34.672 -21.999 -5.923  1.00 14.37 ?  147 VAL   B HG21 1 
ATOM   6163 H HG22 . VAL   B 1 147 ? 33.649 -20.989 -5.247  1.00 14.37 ?  147 VAL   B HG22 1 
ATOM   6164 H HG23 . VAL   B 1 147 ? 33.307 -22.539 -5.318  1.00 14.37 ?  147 VAL   B HG23 1 
ATOM   6165 N N    . ARG   B 1 148 ? 30.660 -19.741 -8.651  1.00 11.78 ?  148 ARG   B N    1 
ATOM   6166 C CA   . ARG   B 1 148 ? 30.035 -19.421 -9.924  1.00 11.91 ?  148 ARG   B CA   1 
ATOM   6167 C C    . ARG   B 1 148 ? 30.991 -18.749 -10.899 1.00 11.82 ?  148 ARG   B C    1 
ATOM   6168 O O    . ARG   B 1 148 ? 30.712 -18.734 -12.099 1.00 13.29 ?  148 ARG   B O    1 
ATOM   6169 C CB   . ARG   B 1 148 ? 28.802 -18.529 -9.700  1.00 12.68 ?  148 ARG   B CB   1 
ATOM   6170 C CG   . ARG   B 1 148 ? 27.723 -19.225 -8.881  1.00 13.52 ?  148 ARG   B CG   1 
ATOM   6171 C CD   . ARG   B 1 148 ? 26.520 -18.335 -8.581  1.00 14.20 ?  148 ARG   B CD   1 
ATOM   6172 N NE   . ARG   B 1 148 ? 26.905 -17.136 -7.849  1.00 13.90 ?  148 ARG   B NE   1 
ATOM   6173 C CZ   . ARG   B 1 148 ? 27.208 -17.105 -6.557  1.00 13.13 ?  148 ARG   B CZ   1 
ATOM   6174 N NH1  . ARG   B 1 148 ? 27.130 -18.188 -5.799  1.00 13.33 ?  148 ARG   B NH1  1 
ATOM   6175 N NH2  . ARG   B 1 148 ? 27.612 -15.960 -6.014  1.00 13.25 ?  148 ARG   B NH2  1 
ATOM   6176 H H    . ARG   B 1 148 ? 30.884 -19.042 -8.195  1.00 14.15 ?  148 ARG   B H    1 
ATOM   6177 H HA   . ARG   B 1 148 ? 29.732 -20.244 -10.331 1.00 14.31 ?  148 ARG   B HA   1 
ATOM   6178 H HB2  . ARG   B 1 148 ? 29.070 -17.727 -9.224  1.00 15.24 ?  148 ARG   B HB2  1 
ATOM   6179 H HB3  . ARG   B 1 148 ? 28.421 -18.294 -10.560 1.00 15.24 ?  148 ARG   B HB3  1 
ATOM   6180 H HG2  . ARG   B 1 148 ? 27.405 -20.001 -9.372  1.00 16.23 ?  148 ARG   B HG2  1 
ATOM   6181 H HG3  . ARG   B 1 148 ? 28.101 -19.508 -8.033  1.00 16.23 ?  148 ARG   B HG3  1 
ATOM   6182 H HD2  . ARG   B 1 148 ? 26.109 -18.062 -9.417  1.00 17.06 ?  148 ARG   B HD2  1 
ATOM   6183 H HD3  . ARG   B 1 148 ? 25.879 -18.832 -8.044  1.00 17.06 ?  148 ARG   B HD3  1 
ATOM   6184 H HE   . ARG   B 1 148 ? 26.935 -16.397 -8.282  1.00 16.69 ?  148 ARG   B HE   1 
ATOM   6185 H HH11 . ARG   B 1 148 ? 26.860 -18.937 -6.132  1.00 16.01 ?  148 ARG   B HH11 1 
ATOM   6186 H HH12 . ARG   B 1 148 ? 27.320 -18.144 -4.959  1.00 16.01 ?  148 ARG   B HH12 1 
ATOM   6187 H HH21 . ARG   B 1 148 ? 27.665 -15.253 -6.499  1.00 15.91 ?  148 ARG   B HH21 1 
ATOM   6188 H HH22 . ARG   B 1 148 ? 27.805 -15.925 -5.178  1.00 15.91 ?  148 ARG   B HH22 1 
ATOM   6189 N N    . THR   B 1 149 ? 32.101 -18.198 -10.412 1.00 11.92 ?  149 THR   B N    1 
ATOM   6190 C CA   . THR   B 1 149 ? 33.140 -17.639 -11.260 1.00 12.19 ?  149 THR   B CA   1 
ATOM   6191 C C    . THR   B 1 149 ? 34.035 -18.776 -11.757 1.00 11.80 ?  149 THR   B C    1 
ATOM   6192 O O    . THR   B 1 149 ? 33.848 -19.944 -11.403 1.00 12.05 ?  149 THR   B O    1 
ATOM   6193 C CB   . THR   B 1 149 ? 33.911 -16.581 -10.481 1.00 12.12 ?  149 THR   B CB   1 
ATOM   6194 O OG1  . THR   B 1 149 ? 34.373 -17.179 -9.265  1.00 12.29 ?  149 THR   B OG1  1 
ATOM   6195 C CG2  . THR   B 1 149 ? 33.025 -15.371 -10.190 1.00 12.92 ?  149 THR   B CG2  1 
ATOM   6196 H H    . THR   B 1 149 ? 32.267 -18.128 -9.570  1.00 14.32 ?  149 THR   B H    1 
ATOM   6197 H HA   . THR   B 1 149 ? 32.728 -17.209 -12.028 1.00 14.64 ?  149 THR   B HA   1 
ATOM   6198 H HB   . THR   B 1 149 ? 34.674 -16.294 -11.005 1.00 14.56 ?  149 THR   B HB   1 
ATOM   6199 H HG1  . THR   B 1 149 ? 34.794 -16.604 -8.812  1.00 14.77 ?  149 THR   B HG1  1 
ATOM   6200 H HG21 . THR   B 1 149 ? 33.534 -14.701 -9.709  1.00 15.51 ?  149 THR   B HG21 1 
ATOM   6201 H HG22 . THR   B 1 149 ? 32.709 -14.986 -11.025 1.00 15.51 ?  149 THR   B HG22 1 
ATOM   6202 H HG23 . THR   B 1 149 ? 32.264 -15.637 -9.657  1.00 15.51 ?  149 THR   B HG23 1 
ATOM   6203 N N    . ASN   B 1 150 ? 34.997 -18.458 -12.610 1.00 11.84 ?  150 ASN   B N    1 
ATOM   6204 C CA   . ASN   B 1 150 ? 35.755 -19.489 -13.306 1.00 12.16 ?  150 ASN   B CA   1 
ATOM   6205 C C    . ASN   B 1 150 ? 36.916 -19.938 -12.432 1.00 11.74 ?  150 ASN   B C    1 
ATOM   6206 O O    . ASN   B 1 150 ? 37.838 -19.163 -12.167 1.00 12.84 ?  150 ASN   B O    1 
ATOM   6207 C CB   . ASN   B 1 150 ? 36.228 -18.967 -14.653 1.00 13.88 ?  150 ASN   B CB   1 
ATOM   6208 C CG   . ASN   B 1 150 ? 35.084 -18.735 -15.593 1.00 16.45 ?  150 ASN   B CG   1 
ATOM   6209 O OD1  . ASN   B 1 150 ? 34.194 -19.568 -15.700 1.00 17.88 ?  150 ASN   B OD1  1 
ATOM   6210 N ND2  . ASN   B 1 150 ? 35.069 -17.584 -16.247 1.00 17.95 ?  150 ASN   B ND2  1 
ATOM   6211 H H    . ASN   B 1 150 ? 35.242 -17.648 -12.795 1.00 14.23 ?  150 ASN   B H    1 
ATOM   6212 H HA   . ASN   B 1 150 ? 35.173 -20.252 -13.463 1.00 14.61 ?  150 ASN   B HA   1 
ATOM   6213 H HB2  . ASN   B 1 150 ? 36.685 -18.121 -14.523 1.00 16.67 ?  150 ASN   B HB2  1 
ATOM   6214 H HB3  . ASN   B 1 150 ? 36.822 -19.614 -15.055 1.00 16.67 ?  150 ASN   B HB3  1 
ATOM   6215 H HD21 . ASN   B 1 150 ? 34.430 -17.403 -16.797 1.00 21.55 ?  150 ASN   B HD21 1 
ATOM   6216 H HD22 . ASN   B 1 150 ? 35.707 -17.016 -16.137 1.00 21.55 ?  150 ASN   B HD22 1 
ATOM   6217 N N    . VAL   B 1 151 ? 36.883 -21.188 -11.986 1.00 11.35 ?  151 VAL   B N    1 
ATOM   6218 C CA   . VAL   B 1 151 ? 37.907 -21.711 -11.096 1.00 11.55 ?  151 VAL   B CA   1 
ATOM   6219 C C    . VAL   B 1 151 ? 38.614 -22.879 -11.769 1.00 11.54 ?  151 VAL   B C    1 
ATOM   6220 O O    . VAL   B 1 151 ? 37.976 -23.815 -12.275 1.00 12.50 ?  151 VAL   B O    1 
ATOM   6221 C CB   . VAL   B 1 151 ? 37.347 -22.045 -9.697  1.00 13.00 ?  151 VAL   B CB   1 
ATOM   6222 C CG1  . VAL   B 1 151 ? 36.190 -23.038 -9.778  1.00 14.03 ?  151 VAL   B CG1  1 
ATOM   6223 C CG2  . VAL   B 1 151 ? 38.456 -22.530 -8.775  1.00 13.37 ?  151 VAL   B CG2  1 
ATOM   6224 H H    . VAL   B 1 151 ? 36.265 -21.755 -12.188 1.00 13.64 ?  151 VAL   B H    1 
ATOM   6225 H HA   . VAL   B 1 151 ? 38.571 -21.013 -10.968 1.00 13.87 ?  151 VAL   B HA   1 
ATOM   6226 H HB   . VAL   B 1 151 ? 36.995 -21.226 -9.311  1.00 15.61 ?  151 VAL   B HB   1 
ATOM   6227 H HG11 . VAL   B 1 151 ? 35.874 -23.229 -8.881  1.00 16.85 ?  151 VAL   B HG11 1 
ATOM   6228 H HG12 . VAL   B 1 151 ? 35.473 -22.649 -10.305 1.00 16.85 ?  151 VAL   B HG12 1 
ATOM   6229 H HG13 . VAL   B 1 151 ? 36.503 -23.855 -10.199 1.00 16.85 ?  151 VAL   B HG13 1 
ATOM   6230 H HG21 . VAL   B 1 151 ? 38.102 -22.610 -7.875  1.00 16.06 ?  151 VAL   B HG21 1 
ATOM   6231 H HG22 . VAL   B 1 151 ? 38.771 -23.392 -9.085  1.00 16.06 ?  151 VAL   B HG22 1 
ATOM   6232 H HG23 . VAL   B 1 151 ? 39.182 -21.886 -8.787  1.00 16.06 ?  151 VAL   B HG23 1 
ATOM   6233 N N    . TYR   B 1 152 ? 39.943 -22.787 -11.791 1.00 11.07 ?  152 TYR   B N    1 
ATOM   6234 C CA   . TYR   B 1 152 ? 40.850 -23.767 -12.369 1.00 11.42 ?  152 TYR   B CA   1 
ATOM   6235 C C    . TYR   B 1 152 ? 41.569 -24.442 -11.205 1.00 10.79 ?  152 TYR   B C    1 
ATOM   6236 O O    . TYR   B 1 152 ? 42.406 -23.822 -10.541 1.00 11.25 ?  152 TYR   B O    1 
ATOM   6237 C CB   . TYR   B 1 152 ? 41.824 -23.051 -13.308 1.00 12.28 ?  152 TYR   B CB   1 
ATOM   6238 C CG   . TYR   B 1 152 ? 41.143 -22.593 -14.576 1.00 12.65 ?  152 TYR   B CG   1 
ATOM   6239 C CD1  . TYR   B 1 152 ? 40.465 -21.378 -14.642 1.00 13.22 ?  152 TYR   B CD1  1 
ATOM   6240 C CD2  . TYR   B 1 152 ? 41.152 -23.399 -15.702 1.00 13.57 ?  152 TYR   B CD2  1 
ATOM   6241 C CE1  . TYR   B 1 152 ? 39.817 -20.991 -15.805 1.00 14.45 ?  152 TYR   B CE1  1 
ATOM   6242 C CE2  . TYR   B 1 152 ? 40.517 -23.021 -16.862 1.00 14.74 ?  152 TYR   B CE2  1 
ATOM   6243 C CZ   . TYR   B 1 152 ? 39.853 -21.816 -16.916 1.00 14.84 ?  152 TYR   B CZ   1 
ATOM   6244 O OH   . TYR   B 1 152 ? 39.219 -21.452 -18.081 1.00 17.23 ?  152 TYR   B OH   1 
ATOM   6245 H H    . TYR   B 1 152 ? 40.371 -22.120 -11.446 1.00 13.30 ?  152 TYR   B H    1 
ATOM   6246 H HA   . TYR   B 1 152 ? 40.345 -24.433 -12.871 1.00 13.71 ?  152 TYR   B HA   1 
ATOM   6247 H HB2  . TYR   B 1 152 ? 42.178 -22.271 -12.853 1.00 14.75 ?  152 TYR   B HB2  1 
ATOM   6248 H HB3  . TYR   B 1 152 ? 42.541 -23.656 -13.545 1.00 14.75 ?  152 TYR   B HB3  1 
ATOM   6249 H HD1  . TYR   B 1 152 ? 40.433 -20.827 -13.891 1.00 15.88 ?  152 TYR   B HD1  1 
ATOM   6250 H HD2  . TYR   B 1 152 ? 41.595 -24.219 -15.669 1.00 16.30 ?  152 TYR   B HD2  1 
ATOM   6251 H HE1  . TYR   B 1 152 ? 39.370 -20.176 -15.839 1.00 17.35 ?  152 TYR   B HE1  1 
ATOM   6252 H HE2  . TYR   B 1 152 ? 40.540 -23.575 -17.606 1.00 17.71 ?  152 TYR   B HE2  1 
ATOM   6253 H HH   . TYR   B 1 152 ? 38.857 -20.702 -17.980 1.00 20.70 ?  152 TYR   B HH   1 
ATOM   6254 N N    . LEU   B 1 153 ? 41.215 -25.703 -10.942 1.00 11.06 ?  153 LEU   B N    1 
ATOM   6255 C CA   . LEU   B 1 153 ? 41.715 -26.447 -9.797  1.00 11.03 ?  153 LEU   B CA   1 
ATOM   6256 C C    . LEU   B 1 153 ? 42.944 -27.253 -10.188 1.00 11.23 ?  153 LEU   B C    1 
ATOM   6257 O O    . LEU   B 1 153 ? 42.924 -27.981 -11.182 1.00 12.34 ?  153 LEU   B O    1 
ATOM   6258 C CB   . LEU   B 1 153 ? 40.636 -27.400 -9.280  1.00 11.44 ?  153 LEU   B CB   1 
ATOM   6259 C CG   . LEU   B 1 153 ? 39.370 -26.745 -8.727  1.00 12.06 ?  153 LEU   B CG   1 
ATOM   6260 C CD1  . LEU   B 1 153 ? 38.281 -27.792 -8.589  1.00 12.80 ?  153 LEU   B CD1  1 
ATOM   6261 C CD2  . LEU   B 1 153 ? 39.660 -26.086 -7.385  1.00 12.82 ?  153 LEU   B CD2  1 
ATOM   6262 H H    . LEU   B 1 153 ? 40.655 -26.158 -11.425 1.00 13.28 ?  153 LEU   B H    1 
ATOM   6263 H HA   . LEU   B 1 153 ? 41.947 -25.827 -9.088  1.00 13.25 ?  153 LEU   B HA   1 
ATOM   6264 H HB2  . LEU   B 1 153 ? 40.367 -27.981 -10.007 1.00 13.74 ?  153 LEU   B HB2  1 
ATOM   6265 H HB3  . LEU   B 1 153 ? 41.019 -27.936 -8.565  1.00 13.74 ?  153 LEU   B HB3  1 
ATOM   6266 H HG   . LEU   B 1 153 ? 39.062 -26.058 -9.342  1.00 14.49 ?  153 LEU   B HG   1 
ATOM   6267 H HD11 . LEU   B 1 153 ? 37.475 -27.362 -8.261  1.00 15.38 ?  153 LEU   B HD11 1 
ATOM   6268 H HD12 . LEU   B 1 153 ? 38.118 -28.184 -9.458  1.00 15.38 ?  153 LEU   B HD12 1 
ATOM   6269 H HD13 . LEU   B 1 153 ? 38.577 -28.467 -7.964  1.00 15.38 ?  153 LEU   B HD13 1 
ATOM   6270 H HD21 . LEU   B 1 153 ? 38.842 -25.704 -7.033  1.00 15.39 ?  153 LEU   B HD21 1 
ATOM   6271 H HD22 . LEU   B 1 153 ? 40.004 -26.755 -6.773  1.00 15.39 ?  153 LEU   B HD22 1 
ATOM   6272 H HD23 . LEU   B 1 153 ? 40.322 -25.385 -7.512  1.00 15.39 ?  153 LEU   B HD23 1 
ATOM   6273 N N    . ALA   B 1 154 ? 43.997 -27.141 -9.387  1.00 11.34 ?  154 ALA   B N    1 
ATOM   6274 C CA   . ALA   B 1 154 ? 45.228 -27.902 -9.567  1.00 12.30 ?  154 ALA   B CA   1 
ATOM   6275 C C    . ALA   B 1 154 ? 45.295 -28.977 -8.490  1.00 12.61 ?  154 ALA   B C    1 
ATOM   6276 O O    . ALA   B 1 154 ? 45.208 -28.677 -7.294  1.00 14.09 ?  154 ALA   B O    1 
ATOM   6277 C CB   . ALA   B 1 154 ? 46.447 -26.984 -9.501  1.00 13.41 ?  154 ALA   B CB   1 
ATOM   6278 H H    . ALA   B 1 154 ? 44.022 -26.607 -8.708  1.00 13.62 ?  154 ALA   B H    1 
ATOM   6279 H HA   . ALA   B 1 154 ? 45.219 -28.330 -10.434 1.00 14.77 ?  154 ALA   B HA   1 
ATOM   6280 H HB1  . ALA   B 1 154 ? 47.252 -27.513 -9.623  1.00 16.11 ?  154 ALA   B HB1  1 
ATOM   6281 H HB2  . ALA   B 1 154 ? 46.385 -26.315 -10.203 1.00 16.11 ?  154 ALA   B HB2  1 
ATOM   6282 H HB3  . ALA   B 1 154 ? 46.472 -26.545 -8.633  1.00 16.11 ?  154 ALA   B HB3  1 
ATOM   6283 N N    . VAL   B 1 155 ? 45.424 -30.223 -8.921  1.00 12.05 ?  155 VAL   B N    1 
ATOM   6284 C CA   . VAL   B 1 155 ? 45.533 -31.368 -8.028  1.00 12.12 ?  155 VAL   B CA   1 
ATOM   6285 C C    . VAL   B 1 155 ? 46.875 -32.038 -8.302  1.00 11.92 ?  155 VAL   B C    1 
ATOM   6286 O O    . VAL   B 1 155 ? 47.117 -32.527 -9.413  1.00 13.76 ?  155 VAL   B O    1 
ATOM   6287 C CB   . VAL   B 1 155 ? 44.378 -32.364 -8.230  1.00 13.77 ?  155 VAL   B CB   1 
ATOM   6288 C CG1  . VAL   B 1 155 ? 44.561 -33.566 -7.321  1.00 13.66 ?  155 VAL   B CG1  1 
ATOM   6289 C CG2  . VAL   B 1 155 ? 43.038 -31.678 -7.976  1.00 14.69 ?  155 VAL   B CG2  1 
ATOM   6290 H H    . VAL   B 1 155 ? 45.459 -30.438 -9.754  1.00 14.47 ?  155 VAL   B H    1 
ATOM   6291 H HA   . VAL   B 1 155 ? 45.521 -31.069 -7.105  1.00 14.55 ?  155 VAL   B HA   1 
ATOM   6292 H HB   . VAL   B 1 155 ? 44.386 -32.673 -9.150  1.00 16.54 ?  155 VAL   B HB   1 
ATOM   6293 H HG11 . VAL   B 1 155 ? 43.733 -34.071 -7.289  1.00 16.41 ?  155 VAL   B HG11 1 
ATOM   6294 H HG12 . VAL   B 1 155 ? 45.273 -34.131 -7.674  1.00 16.41 ?  155 VAL   B HG12 1 
ATOM   6295 H HG13 . VAL   B 1 155 ? 44.796 -33.263 -6.430  1.00 16.41 ?  155 VAL   B HG13 1 
ATOM   6296 H HG21 . VAL   B 1 155 ? 42.329 -32.333 -8.068  1.00 17.64 ?  155 VAL   B HG21 1 
ATOM   6297 H HG22 . VAL   B 1 155 ? 43.038 -31.315 -7.076  1.00 17.64 ?  155 VAL   B HG22 1 
ATOM   6298 H HG23 . VAL   B 1 155 ? 42.919 -30.966 -8.622  1.00 17.64 ?  155 VAL   B HG23 1 
ATOM   6299 N N    . PHE   B 1 156 ? 47.741 -32.068 -7.287  1.00 12.52 ?  156 PHE   B N    1 
ATOM   6300 C CA   . PHE   B 1 156 ? 49.119 -32.526 -7.482  1.00 13.61 ?  156 PHE   B CA   1 
ATOM   6301 C C    . PHE   B 1 156 ? 49.219 -34.028 -7.760  1.00 14.50 ?  156 PHE   B C    1 
ATOM   6302 O O    . PHE   B 1 156 ? 49.964 -34.454 -8.654  1.00 16.39 ?  156 PHE   B O    1 
ATOM   6303 C CB   . PHE   B 1 156 ? 49.949 -32.154 -6.255  1.00 14.16 ?  156 PHE   B CB   1 
ATOM   6304 C CG   . PHE   B 1 156 ? 51.373 -32.621 -6.311  1.00 14.66 ?  156 PHE   B CG   1 
ATOM   6305 C CD1  . PHE   B 1 156 ? 52.256 -32.089 -7.230  1.00 16.46 ?  156 PHE   B CD1  1 
ATOM   6306 C CD2  . PHE   B 1 156 ? 51.832 -33.577 -5.426  1.00 15.16 ?  156 PHE   B CD2  1 
ATOM   6307 C CE1  . PHE   B 1 156 ? 53.575 -32.497 -7.275  1.00 17.59 ?  156 PHE   B CE1  1 
ATOM   6308 C CE2  . PHE   B 1 156 ? 53.149 -33.995 -5.464  1.00 16.61 ?  156 PHE   B CE2  1 
ATOM   6309 C CZ   . PHE   B 1 156 ? 54.016 -33.457 -6.395  1.00 17.44 ?  156 PHE   B CZ   1 
ATOM   6310 H H    . PHE   B 1 156 ? 47.553 -31.839 -6.479  1.00 15.03 ?  156 PHE   B H    1 
ATOM   6311 H HA   . PHE   B 1 156 ? 49.492 -32.060 -8.243  1.00 16.35 ?  156 PHE   B HA   1 
ATOM   6312 H HB2  . PHE   B 1 156 ? 49.959 -31.187 -6.172  1.00 17.01 ?  156 PHE   B HB2  1 
ATOM   6313 H HB3  . PHE   B 1 156 ? 49.538 -32.546 -5.469  1.00 17.01 ?  156 PHE   B HB3  1 
ATOM   6314 H HD1  . PHE   B 1 156 ? 51.964 -31.437 -7.826  1.00 19.77 ?  156 PHE   B HD1  1 
ATOM   6315 H HD2  . PHE   B 1 156 ? 51.242 -33.944 -4.803  1.00 18.20 ?  156 PHE   B HD2  1 
ATOM   6316 H HE1  . PHE   B 1 156 ? 54.159 -32.133 -7.902  1.00 21.13 ?  156 PHE   B HE1  1 
ATOM   6317 H HE2  . PHE   B 1 156 ? 53.443 -34.652 -4.869  1.00 19.95 ?  156 PHE   B HE2  1 
ATOM   6318 H HZ   . PHE   B 1 156 ? 54.902 -33.745 -6.422  1.00 20.94 ?  156 PHE   B HZ   1 
ATOM   6319 N N    . ASP   B 1 157 ? 48.544 -34.850 -6.966  1.00 14.92 ?  157 ASP   B N    1 
ATOM   6320 C CA   . ASP   B 1 157 ? 48.694 -36.298 -7.061  1.00 16.15 ?  157 ASP   B CA   1 
ATOM   6321 C C    . ASP   B 1 157 ? 47.784 -36.839 -8.159  1.00 16.19 ?  157 ASP   B C    1 
ATOM   6322 O O    . ASP   B 1 157 ? 46.558 -36.724 -8.062  1.00 15.73 ?  157 ASP   B O    1 
ATOM   6323 C CB   . ASP   B 1 157 ? 48.320 -36.911 -5.718  1.00 17.88 ?  157 ASP   B CB   1 
ATOM   6324 C CG   . ASP   B 1 157 ? 48.473 -38.417 -5.692  1.00 19.82 ?  157 ASP   B CG   1 
ATOM   6325 O OD1  . ASP   B 1 157 ? 48.810 -39.025 -6.735  1.00 20.25 ?  157 ASP   B OD1  1 
ATOM   6326 O OD2  . ASP   B 1 157 ? 48.283 -38.992 -4.602  1.00 22.12 -1 157 ASP   B OD2  1 
ATOM   6327 H H    . ASP   B 1 157 ? 47.996 -34.593 -6.361  1.00 17.92 ?  157 ASP   B H    1 
ATOM   6328 H HA   . ASP   B 1 157 ? 49.616 -36.528 -7.269  1.00 19.40 ?  157 ASP   B HA   1 
ATOM   6329 H HB2  . ASP   B 1 157 ? 48.886 -36.529 -5.034  1.00 21.47 ?  157 ASP   B HB2  1 
ATOM   6330 H HB3  . ASP   B 1 157 ? 47.388 -36.701 -5.531  1.00 21.47 ?  157 ASP   B HB3  1 
ATOM   6331 N N    . LYS   B 1 158 ? 48.384 -37.460 -9.184  1.00 17.29 ?  158 LYS   B N    1 
ATOM   6332 C CA   . LYS   B 1 158 ? 47.609 -38.076 -10.265 1.00 18.34 ?  158 LYS   B CA   1 
ATOM   6333 C C    . LYS   B 1 158 ? 46.549 -39.042 -9.734  1.00 17.85 ?  158 LYS   B C    1 
ATOM   6334 O O    . LYS   B 1 158 ? 45.444 -39.132 -10.283 1.00 18.23 ?  158 LYS   B O    1 
ATOM   6335 C CB   . LYS   B 1 158 ? 48.560 -38.790 -11.235 1.00 20.35 ?  158 LYS   B CB   1 
ATOM   6336 C CG   . LYS   B 1 158 ? 47.885 -39.682 -12.268 1.00 23.31 ?  158 LYS   B CG   1 
ATOM   6337 C CD   . LYS   B 1 158 ? 47.037 -38.898 -13.246 1.00 26.48 ?  158 LYS   B CD   1 
ATOM   6338 C CE   . LYS   B 1 158 ? 46.432 -39.816 -14.297 1.00 29.04 ?  158 LYS   B CE   1 
ATOM   6339 N NZ   . LYS   B 1 158 ? 45.378 -39.131 -15.097 1.00 29.98 ?  158 LYS   B NZ   1 
ATOM   6340 H H    . LYS   B 1 158 ? 49.238 -37.536 -9.278  1.00 20.76 ?  158 LYS   B H    1 
ATOM   6341 H HA   . LYS   B 1 158 ? 47.157 -37.376 -10.766 1.00 22.02 ?  158 LYS   B HA   1 
ATOM   6342 H HB2  . LYS   B 1 158 ? 49.069 -38.119 -11.725 1.00 24.43 ?  158 LYS   B HB2  1 
ATOM   6343 H HB3  . LYS   B 1 158 ? 49.169 -39.343 -10.724 1.00 24.43 ?  158 LYS   B HB3  1 
ATOM   6344 H HG2  . LYS   B 1 158 ? 48.571 -40.145 -12.777 1.00 27.99 ?  158 LYS   B HG2  1 
ATOM   6345 H HG3  . LYS   B 1 158 ? 47.319 -40.335 -11.825 1.00 27.99 ?  158 LYS   B HG3  1 
ATOM   6346 H HD2  . LYS   B 1 158 ? 46.316 -38.461 -12.769 1.00 31.79 ?  158 LYS   B HD2  1 
ATOM   6347 H HD3  . LYS   B 1 158 ? 47.592 -38.243 -13.698 1.00 31.79 ?  158 LYS   B HD3  1 
ATOM   6348 H HE2  . LYS   B 1 158 ? 47.128 -40.110 -14.904 1.00 34.86 ?  158 LYS   B HE2  1 
ATOM   6349 H HE3  . LYS   B 1 158 ? 46.028 -40.582 -13.858 1.00 34.86 ?  158 LYS   B HE3  1 
ATOM   6350 H HZ1  . LYS   B 1 158 ? 45.042 -39.691 -15.701 1.00 35.99 ?  158 LYS   B HZ1  1 
ATOM   6351 H HZ2  . LYS   B 1 158 ? 44.722 -38.855 -14.563 1.00 35.99 ?  158 LYS   B HZ2  1 
ATOM   6352 H HZ3  . LYS   B 1 158 ? 45.725 -38.427 -15.517 1.00 35.99 ?  158 LYS   B HZ3  1 
ATOM   6353 N N    . ASN   B 1 159 ? 46.872 -39.799 -8.686  1.00 18.19 ?  159 ASN   B N    1 
ATOM   6354 C CA   . ASN   B 1 159 ? 45.917 -40.780 -8.179  1.00 18.81 ?  159 ASN   B CA   1 
ATOM   6355 C C    . ASN   B 1 159 ? 44.716 -40.108 -7.513  1.00 17.59 ?  159 ASN   B C    1 
ATOM   6356 O O    . ASN   B 1 159 ? 43.584 -40.601 -7.621  1.00 18.23 ?  159 ASN   B O    1 
ATOM   6357 C CB   . ASN   B 1 159 ? 46.623 -41.751 -7.239  1.00 20.87 ?  159 ASN   B CB   1 
ATOM   6358 C CG   . ASN   B 1 159 ? 47.659 -42.589 -7.953  1.00 23.08 ?  159 ASN   B CG   1 
ATOM   6359 O OD1  . ASN   B 1 159 ? 47.410 -43.091 -9.056  1.00 23.93 ?  159 ASN   B OD1  1 
ATOM   6360 N ND2  . ASN   B 1 159 ? 48.827 -42.755 -7.331  1.00 24.07 ?  159 ASN   B ND2  1 
ATOM   6361 H H    . ASN   B 1 159 ? 47.615 -39.752 -8.264  1.00 21.85 ?  159 ASN   B H    1 
ATOM   6362 H HA   . ASN   B 1 159 ? 45.584 -41.290 -8.935  1.00 22.58 ?  159 ASN   B HA   1 
ATOM   6363 H HB2  . ASN   B 1 159 ? 47.069 -41.256 -6.541  1.00 25.06 ?  159 ASN   B HB2  1 
ATOM   6364 H HB3  . ASN   B 1 159 ? 45.968 -42.356 -6.863  1.00 25.06 ?  159 ASN   B HB3  1 
ATOM   6365 H HD21 . ASN   B 1 159 ? 49.455 -43.224 -7.695  1.00 28.90 ?  159 ASN   B HD21 1 
ATOM   6366 H HD22 . ASN   B 1 159 ? 48.957 -42.402 -6.557  1.00 28.90 ?  159 ASN   B HD22 1 
ATOM   6367 N N    . LEU   B 1 160 ? 44.927 -38.973 -6.835  1.00 16.55 ?  160 LEU   B N    1 
ATOM   6368 C CA   . LEU   B 1 160 ? 43.793 -38.239 -6.289  1.00 15.75 ?  160 LEU   B CA   1 
ATOM   6369 C C    . LEU   B 1 160 ? 43.000 -37.574 -7.402  1.00 15.02 ?  160 LEU   B C    1 
ATOM   6370 O O    . LEU   B 1 160 ? 41.762 -37.588 -7.390  1.00 14.79 ?  160 LEU   B O    1 
ATOM   6371 C CB   . LEU   B 1 160 ? 44.253 -37.211 -5.256  1.00 15.37 ?  160 LEU   B CB   1 
ATOM   6372 C CG   . LEU   B 1 160 ? 43.125 -36.322 -4.716  1.00 15.17 ?  160 LEU   B CG   1 
ATOM   6373 C CD1  . LEU   B 1 160 ? 41.994 -37.147 -4.108  1.00 15.72 ?  160 LEU   B CD1  1 
ATOM   6374 C CD2  . LEU   B 1 160 ? 43.665 -35.328 -3.701  1.00 15.77 ?  160 LEU   B CD2  1 
ATOM   6375 H H    . LEU   B 1 160 ? 45.702 -38.618 -6.687  1.00 19.87 ?  160 LEU   B H    1 
ATOM   6376 H HA   . LEU   B 1 160 ? 43.208 -38.868 -5.847  1.00 18.91 ?  160 LEU   B HA   1 
ATOM   6377 H HB2  . LEU   B 1 160 ? 44.650 -37.684 -4.505  1.00 18.46 ?  160 LEU   B HB2  1 
ATOM   6378 H HB3  . LEU   B 1 160 ? 44.920 -36.634 -5.664  1.00 18.46 ?  160 LEU   B HB3  1 
ATOM   6379 H HG   . LEU   B 1 160 ? 42.753 -35.813 -5.450  1.00 18.21 ?  160 LEU   B HG   1 
ATOM   6380 H HD11 . LEU   B 1 160 ? 41.358 -36.550 -3.692  1.00 18.88 ?  160 LEU   B HD11 1 
ATOM   6381 H HD12 . LEU   B 1 160 ? 41.559 -37.659 -4.810  1.00 18.88 ?  160 LEU   B HD12 1 
ATOM   6382 H HD13 . LEU   B 1 160 ? 42.365 -37.753 -3.443  1.00 18.88 ?  160 LEU   B HD13 1 
ATOM   6383 H HD21 . LEU   B 1 160 ? 42.938 -34.763 -3.397  1.00 18.94 ?  160 LEU   B HD21 1 
ATOM   6384 H HD22 . LEU   B 1 160 ? 44.043 -35.814 -2.951  1.00 18.94 ?  160 LEU   B HD22 1 
ATOM   6385 H HD23 . LEU   B 1 160 ? 44.351 -34.787 -4.124  1.00 18.94 ?  160 LEU   B HD23 1 
ATOM   6386 N N    . TYR   B 1 161 ? 43.697 -37.000 -8.382  1.00 15.10 ?  161 TYR   B N    1 
ATOM   6387 C CA   . TYR   B 1 161 ? 43.028 -36.439 -9.549  1.00 15.02 ?  161 TYR   B CA   1 
ATOM   6388 C C    . TYR   B 1 161 ? 42.089 -37.465 -10.173 1.00 14.83 ?  161 TYR   B C    1 
ATOM   6389 O O    . TYR   B 1 161 ? 40.920 -37.170 -10.447 1.00 14.63 ?  161 TYR   B O    1 
ATOM   6390 C CB   . TYR   B 1 161 ? 44.078 -35.957 -10.561 1.00 15.61 ?  161 TYR   B CB   1 
ATOM   6391 C CG   . TYR   B 1 161 ? 43.505 -35.491 -11.880 1.00 16.01 ?  161 TYR   B CG   1 
ATOM   6392 C CD1  . TYR   B 1 161 ? 43.091 -34.176 -12.047 1.00 15.88 ?  161 TYR   B CD1  1 
ATOM   6393 C CD2  . TYR   B 1 161 ? 43.364 -36.363 -12.955 1.00 16.76 ?  161 TYR   B CD2  1 
ATOM   6394 C CE1  . TYR   B 1 161 ? 42.560 -33.744 -13.239 1.00 16.99 ?  161 TYR   B CE1  1 
ATOM   6395 C CE2  . TYR   B 1 161 ? 42.828 -35.937 -14.150 1.00 18.01 ?  161 TYR   B CE2  1 
ATOM   6396 C CZ   . TYR   B 1 161 ? 42.431 -34.625 -14.288 1.00 17.68 ?  161 TYR   B CZ   1 
ATOM   6397 O OH   . TYR   B 1 161 ? 41.898 -34.185 -15.474 1.00 19.80 ?  161 TYR   B OH   1 
ATOM   6398 H H    . TYR   B 1 161 ? 44.553 -36.929 -8.401  1.00 18.14 ?  161 TYR   B H    1 
ATOM   6399 H HA   . TYR   B 1 161 ? 42.501 -35.672 -9.282  1.00 18.03 ?  161 TYR   B HA   1 
ATOM   6400 H HB2  . TYR   B 1 161 ? 44.567 -35.208 -10.176 1.00 18.75 ?  161 TYR   B HB2  1 
ATOM   6401 H HB3  . TYR   B 1 161 ? 44.693 -36.681 -10.753 1.00 18.75 ?  161 TYR   B HB3  1 
ATOM   6402 H HD1  . TYR   B 1 161 ? 43.179 -33.568 -11.345 1.00 19.08 ?  161 TYR   B HD1  1 
ATOM   6403 H HD2  . TYR   B 1 161 ? 43.627 -37.248 -12.867 1.00 20.12 ?  161 TYR   B HD2  1 
ATOM   6404 H HE1  . TYR   B 1 161 ? 42.292 -32.852 -13.335 1.00 20.40 ?  161 TYR   B HE1  1 
ATOM   6405 H HE2  . TYR   B 1 161 ? 42.736 -36.526 -14.862 1.00 21.63 ?  161 TYR   B HE2  1 
ATOM   6406 H HH   . TYR   B 1 161 ? 41.869 -34.820 -16.029 1.00 23.77 ?  161 TYR   B HH   1 
ATOM   6407 N N    . ASP   B 1 162 ? 42.586 -38.685 -10.392 1.00 15.38 ?  162 ASP   B N    1 
ATOM   6408 C CA   . ASP   B 1 162 ? 41.761 -39.721 -11.006 1.00 16.26 ?  162 ASP   B CA   1 
ATOM   6409 C C    . ASP   B 1 162 ? 40.553 -40.062 -10.142 1.00 15.60 ?  162 ASP   B C    1 
ATOM   6410 O O    . ASP   B 1 162 ? 39.449 -40.278 -10.660 1.00 15.91 ?  162 ASP   B O    1 
ATOM   6411 C CB   . ASP   B 1 162 ? 42.591 -40.982 -11.253 1.00 17.85 ?  162 ASP   B CB   1 
ATOM   6412 C CG   . ASP   B 1 162 ? 43.597 -40.820 -12.379 1.00 19.30 ?  162 ASP   B CG   1 
ATOM   6413 O OD1  . ASP   B 1 162 ? 43.466 -39.878 -13.183 1.00 19.67 ?  162 ASP   B OD1  1 
ATOM   6414 O OD2  . ASP   B 1 162 ? 44.511 -41.662 -12.474 1.00 21.19 -1 162 ASP   B OD2  1 
ATOM   6415 H H    . ASP   B 1 162 ? 43.387 -38.930 -10.197 1.00 18.48 ?  162 ASP   B H    1 
ATOM   6416 H HA   . ASP   B 1 162 ? 41.435 -39.401 -11.859 1.00 19.53 ?  162 ASP   B HA   1 
ATOM   6417 H HB2  . ASP   B 1 162 ? 43.081 -41.201 -10.444 1.00 21.43 ?  162 ASP   B HB2  1 
ATOM   6418 H HB3  . ASP   B 1 162 ? 41.995 -41.708 -11.488 1.00 21.43 ?  162 ASP   B HB3  1 
ATOM   6419 N N    . LYS   B 1 163 ? 40.739 -40.128 -8.821  1.00 15.22 ?  163 LYS   B N    1 
ATOM   6420 C CA   . LYS   B 1 163 ? 39.614 -40.406 -7.935  1.00 15.60 ?  163 LYS   B CA   1 
ATOM   6421 C C    . LYS   B 1 163 ? 38.566 -39.301 -8.004  1.00 14.41 ?  163 LYS   B C    1 
ATOM   6422 O O    . LYS   B 1 163 ? 37.359 -39.578 -8.012  1.00 15.34 ?  163 LYS   B O    1 
ATOM   6423 C CB   . LYS   B 1 163 ? 40.099 -40.586 -6.500  1.00 18.75 ?  163 LYS   B CB   1 
ATOM   6424 C CG   . LYS   B 1 163 ? 39.009 -41.092 -5.580  1.00 24.96 ?  163 LYS   B CG   1 
ATOM   6425 C CD   . LYS   B 1 163 ? 39.487 -41.289 -4.155  1.00 31.35 ?  163 LYS   B CD   1 
ATOM   6426 C CE   . LYS   B 1 163 ? 38.413 -41.988 -3.332  1.00 36.20 ?  163 LYS   B CE   1 
ATOM   6427 N NZ   . LYS   B 1 163 ? 38.458 -41.613 -1.892  1.00 39.37 ?  163 LYS   B NZ   1 
ATOM   6428 H H    . LYS   B 1 163 ? 41.496 -40.016 -8.422  1.00 18.28 ?  163 LYS   B H    1 
ATOM   6429 H HA   . LYS   B 1 163 ? 39.196 -41.233 -8.217  1.00 18.74 ?  163 LYS   B HA   1 
ATOM   6430 H HB2  . LYS   B 1 163 ? 40.825 -41.231 -6.490  1.00 22.51 ?  163 LYS   B HB2  1 
ATOM   6431 H HB3  . LYS   B 1 163 ? 40.408 -39.733 -6.160  1.00 22.51 ?  163 LYS   B HB3  1 
ATOM   6432 H HG2  . LYS   B 1 163 ? 38.281 -40.452 -5.565  1.00 29.96 ?  163 LYS   B HG2  1 
ATOM   6433 H HG3  . LYS   B 1 163 ? 38.689 -41.949 -5.910  1.00 29.96 ?  163 LYS   B HG3  1 
ATOM   6434 H HD2  . LYS   B 1 163 ? 40.285 -41.843 -4.154  1.00 37.64 ?  163 LYS   B HD2  1 
ATOM   6435 H HD3  . LYS   B 1 163 ? 39.672 -40.427 -3.753  1.00 37.64 ?  163 LYS   B HD3  1 
ATOM   6436 H HE2  . LYS   B 1 163 ? 37.539 -41.750 -3.681  1.00 43.45 ?  163 LYS   B HE2  1 
ATOM   6437 H HE3  . LYS   B 1 163 ? 38.542 -42.947 -3.396  1.00 43.45 ?  163 LYS   B HE3  1 
ATOM   6438 H HZ1  . LYS   B 1 163 ? 37.815 -42.040 -1.447  1.00 47.25 ?  163 LYS   B HZ1  1 
ATOM   6439 H HZ2  . LYS   B 1 163 ? 39.246 -41.834 -1.545  1.00 47.25 ?  163 LYS   B HZ2  1 
ATOM   6440 H HZ3  . LYS   B 1 163 ? 38.337 -40.736 -1.802  1.00 47.25 ?  163 LYS   B HZ3  1 
ATOM   6441 N N    . LEU   B 1 164 ? 39.015 -38.044 -8.063  1.00 13.75 ?  164 LEU   B N    1 
ATOM   6442 C CA   . LEU   B 1 164 ? 38.103 -36.905 -8.120  1.00 13.41 ?  164 LEU   B CA   1 
ATOM   6443 C C    . LEU   B 1 164 ? 37.322 -36.890 -9.428  1.00 13.40 ?  164 LEU   B C    1 
ATOM   6444 O O    . LEU   B 1 164 ? 36.098 -36.695 -9.434  1.00 14.53 ?  164 LEU   B O    1 
ATOM   6445 C CB   . LEU   B 1 164 ? 38.905 -35.615 -7.961  1.00 12.98 ?  164 LEU   B CB   1 
ATOM   6446 C CG   . LEU   B 1 164 ? 39.427 -35.340 -6.555  1.00 13.78 ?  164 LEU   B CG   1 
ATOM   6447 C CD1  . LEU   B 1 164 ? 40.522 -34.285 -6.604  1.00 13.94 ?  164 LEU   B CD1  1 
ATOM   6448 C CD2  . LEU   B 1 164 ? 38.303 -34.899 -5.635  1.00 15.47 ?  164 LEU   B CD2  1 
ATOM   6449 H H    . LEU   B 1 164 ? 39.852 -37.826 -8.069  1.00 16.51 ?  164 LEU   B H    1 
ATOM   6450 H HA   . LEU   B 1 164 ? 37.475 -36.966 -7.392  1.00 16.10 ?  164 LEU   B HA   1 
ATOM   6451 H HB2  . LEU   B 1 164 ? 39.675 -35.652 -8.555  1.00 15.59 ?  164 LEU   B HB2  1 
ATOM   6452 H HB3  . LEU   B 1 164 ? 38.341 -34.869 -8.215  1.00 15.59 ?  164 LEU   B HB3  1 
ATOM   6453 H HG   . LEU   B 1 164 ? 39.813 -36.149 -6.195  1.00 16.55 ?  164 LEU   B HG   1 
ATOM   6454 H HD11 . LEU   B 1 164 ? 40.838 -34.110 -5.703  1.00 16.75 ?  164 LEU   B HD11 1 
ATOM   6455 H HD12 . LEU   B 1 164 ? 41.257 -34.614 -7.150  1.00 16.75 ?  164 LEU   B HD12 1 
ATOM   6456 H HD13 . LEU   B 1 164 ? 40.166 -33.470 -6.993  1.00 16.75 ?  164 LEU   B HD13 1 
ATOM   6457 H HD21 . LEU   B 1 164 ? 38.672 -34.669 -4.768  1.00 18.58 ?  164 LEU   B HD21 1 
ATOM   6458 H HD22 . LEU   B 1 164 ? 37.859 -34.127 -6.020  1.00 18.58 ?  164 LEU   B HD22 1 
ATOM   6459 H HD23 . LEU   B 1 164 ? 37.670 -35.629 -5.541  1.00 18.58 ?  164 LEU   B HD23 1 
ATOM   6460 N N    . VAL   B 1 165 ? 38.018 -37.064 -10.553 1.00 14.72 ?  165 VAL   B N    1 
ATOM   6461 C CA   . VAL   B 1 165 ? 37.366 -37.006 -11.858 1.00 15.78 ?  165 VAL   B CA   1 
ATOM   6462 C C    . VAL   B 1 165 ? 36.445 -38.205 -12.043 1.00 17.17 ?  165 VAL   B C    1 
ATOM   6463 O O    . VAL   B 1 165 ? 35.288 -38.071 -12.463 1.00 18.05 ?  165 VAL   B O    1 
ATOM   6464 C CB   . VAL   B 1 165 ? 38.422 -36.918 -12.976 1.00 16.76 ?  165 VAL   B CB   1 
ATOM   6465 C CG1  . VAL   B 1 165 ? 37.773 -37.011 -14.339 1.00 18.07 ?  165 VAL   B CG1  1 
ATOM   6466 C CG2  . VAL   B 1 165 ? 39.226 -35.634 -12.851 1.00 16.65 ?  165 VAL   B CG2  1 
ATOM   6467 H H    . VAL   B 1 165 ? 38.868 -37.206 -10.588 1.00 17.68 ?  165 VAL   B H    1 
ATOM   6468 H HA   . VAL   B 1 165 ? 36.825 -36.204 -11.904 1.00 18.95 ?  165 VAL   B HA   1 
ATOM   6469 H HB   . VAL   B 1 165 ? 39.041 -37.659 -12.887 1.00 20.13 ?  165 VAL   B HB   1 
ATOM   6470 H HG11 . VAL   B 1 165 ? 38.410 -36.731 -15.011 1.00 21.70 ?  165 VAL   B HG11 1 
ATOM   6471 H HG12 . VAL   B 1 165 ? 37.514 -37.935 -14.497 1.00 21.70 ?  165 VAL   B HG12 1 
ATOM   6472 H HG13 . VAL   B 1 165 ? 36.994 -36.440 -14.355 1.00 21.70 ?  165 VAL   B HG13 1 
ATOM   6473 H HG21 . VAL   B 1 165 ? 39.866 -35.585 -13.580 1.00 19.99 ?  165 VAL   B HG21 1 
ATOM   6474 H HG22 . VAL   B 1 165 ? 38.621 -34.875 -12.894 1.00 19.99 ?  165 VAL   B HG22 1 
ATOM   6475 H HG23 . VAL   B 1 165 ? 39.696 -35.632 -12.001 1.00 19.99 ?  165 VAL   B HG23 1 
ATOM   6476 N N    . SER   B 1 166 ? 36.951 -39.400 -11.730 1.00 17.77 ?  166 SER   B N    1 
ATOM   6477 C CA   . SER   B 1 166 ? 36.193 -40.612 -12.003 1.00 19.38 ?  166 SER   B CA   1 
ATOM   6478 C C    . SER   B 1 166 ? 34.935 -40.696 -11.153 1.00 19.83 ?  166 SER   B C    1 
ATOM   6479 O O    . SER   B 1 166 ? 33.963 -41.315 -11.578 1.00 21.55 ?  166 SER   B O    1 
ATOM   6480 C CB   . SER   B 1 166 ? 37.054 -41.866 -11.825 1.00 20.26 ?  166 SER   B CB   1 
ATOM   6481 O OG   . SER   B 1 166 ? 37.432 -42.065 -10.475 1.00 20.65 ?  166 SER   B OG   1 
ATOM   6482 H H    . SER   B 1 166 ? 37.725 -39.531 -11.376 1.00 21.33 ?  166 SER   B H    1 
ATOM   6483 H HA   . SER   B 1 166 ? 35.913 -40.590 -12.932 1.00 23.27 ?  166 SER   B HA   1 
ATOM   6484 H HB2  . SER   B 1 166 ? 36.541 -42.637 -12.122 1.00 24.32 ?  166 SER   B HB2  1 
ATOM   6485 H HB3  . SER   B 1 166 ? 37.851 -41.779 -12.370 1.00 24.32 ?  166 SER   B HB3  1 
ATOM   6486 H HG   . SER   B 1 166 ? 37.888 -41.414 -10.211 1.00 24.79 ?  166 SER   B HG   1 
ATOM   6487 N N    . SER   B 1 167 ? 34.915 -40.082 -9.972  1.00 18.75 ?  167 SER   B N    1 
ATOM   6488 C CA   . SER   B 1 167 ? 33.756 -40.140 -9.088  1.00 18.01 ?  167 SER   B CA   1 
ATOM   6489 C C    . SER   B 1 167 ? 32.836 -38.925 -9.193  1.00 17.65 ?  167 SER   B C    1 
ATOM   6490 O O    . SER   B 1 167 ? 31.758 -38.925 -8.585  1.00 17.60 ?  167 SER   B O    1 
ATOM   6491 C CB   . SER   B 1 167 ? 34.198 -40.323 -7.631  1.00 17.82 ?  167 SER   B CB   1 
ATOM   6492 O OG   . SER   B 1 167 ? 34.880 -39.172 -7.152  1.00 17.52 ?  167 SER   B OG   1 
ATOM   6493 H H    . SER   B 1 167 ? 35.563 -39.618 -9.663  1.00 22.52 ?  167 SER   B H    1 
ATOM   6494 H HA   . SER   B 1 167 ? 33.227 -40.920 -9.330  1.00 21.63 ?  167 SER   B HA   1 
ATOM   6495 H HB2  . SER   B 1 167 ? 33.410 -40.481 -7.085  1.00 21.39 ?  167 SER   B HB2  1 
ATOM   6496 H HB3  . SER   B 1 167 ? 34.789 -41.094 -7.582  1.00 21.39 ?  167 SER   B HB3  1 
ATOM   6497 H HG   . SER   B 1 167 ? 35.562 -39.036 -7.623  1.00 21.04 ?  167 SER   B HG   1 
ATOM   6498 N N    . PHE   B 1 168 ? 33.213 -37.897 -9.954  1.00 17.28 ?  168 PHE   B N    1 
ATOM   6499 C CA   . PHE   B 1 168 ? 32.387 -36.692 -10.022 1.00 16.97 ?  168 PHE   B CA   1 
ATOM   6500 C C    . PHE   B 1 168 ? 31.070 -36.953 -10.747 1.00 15.29 ?  168 PHE   B C    1 
ATOM   6501 O O    . PHE   B 1 168 ? 30.032 -36.358 -10.406 1.00 16.11 ?  168 PHE   B O    1 
ATOM   6502 C CB   . PHE   B 1 168 ? 33.149 -35.561 -10.710 1.00 17.56 ?  168 PHE   B CB   1 
ATOM   6503 C CG   . PHE   B 1 168 ? 32.348 -34.311 -10.830 1.00 17.79 ?  168 PHE   B CG   1 
ATOM   6504 C CD1  . PHE   B 1 168 ? 32.034 -33.575 -9.697  1.00 18.81 ?  168 PHE   B CD1  1 
ATOM   6505 C CD2  . PHE   B 1 168 ? 31.884 -33.877 -12.057 1.00 17.14 ?  168 PHE   B CD2  1 
ATOM   6506 C CE1  . PHE   B 1 168 ? 31.272 -32.425 -9.783  1.00 19.36 ?  168 PHE   B CE1  1 
ATOM   6507 C CE2  . PHE   B 1 168 ? 31.132 -32.710 -12.155 1.00 18.05 ?  168 PHE   B CE2  1 
ATOM   6508 C CZ   . PHE   B 1 168 ? 30.824 -31.985 -11.015 1.00 18.53 ?  168 PHE   B CZ   1 
ATOM   6509 H H    . PHE   B 1 168 ? 33.936 -37.867 -10.425 1.00 20.75 ?  168 PHE   B H    1 
ATOM   6510 H HA   . PHE   B 1 168 ? 32.177 -36.406 -9.123  1.00 20.38 ?  168 PHE   B HA   1 
ATOM   6511 H HB2  . PHE   B 1 168 ? 33.943 -35.355 -10.193 1.00 21.09 ?  168 PHE   B HB2  1 
ATOM   6512 H HB3  . PHE   B 1 168 ? 33.396 -35.840 -11.603 1.00 21.09 ?  168 PHE   B HB3  1 
ATOM   6513 H HD1  . PHE   B 1 168 ? 32.330 -33.870 -8.866  1.00 22.59 ?  168 PHE   B HD1  1 
ATOM   6514 H HD2  . PHE   B 1 168 ? 32.088 -34.358 -12.825 1.00 20.59 ?  168 PHE   B HD2  1 
ATOM   6515 H HE1  . PHE   B 1 168 ? 31.069 -31.941 -9.015  1.00 23.24 ?  168 PHE   B HE1  1 
ATOM   6516 H HE2  . PHE   B 1 168 ? 30.823 -32.424 -12.987 1.00 21.67 ?  168 PHE   B HE2  1 
ATOM   6517 H HZ   . PHE   B 1 168 ? 30.311 -31.211 -11.080 1.00 22.25 ?  168 PHE   B HZ   1 
ATOM   6518 N N    . LEU   B 1 169 ? 31.094 -37.844 -11.736 1.00 16.13 ?  169 LEU   B N    1 
ATOM   6519 C CA   . LEU   B 1 169 ? 29.915 -38.149 -12.533 1.00 18.43 ?  169 LEU   B CA   1 
ATOM   6520 C C    . LEU   B 1 169 ? 29.911 -39.592 -13.025 1.00 21.20 ?  169 LEU   B C    1 
ATOM   6521 O O    . LEU   B 1 169 ? 29.027 -40.007 -13.775 1.00 23.70 ?  169 LEU   B O    1 
ATOM   6522 C CB   . LEU   B 1 169 ? 29.834 -37.197 -13.727 1.00 20.19 ?  169 LEU   B CB   1 
ATOM   6523 C CG   . LEU   B 1 169 ? 28.566 -36.347 -13.821 1.00 23.22 ?  169 LEU   B CG   1 
ATOM   6524 C CD1  . LEU   B 1 169 ? 28.543 -35.604 -15.143 1.00 24.47 ?  169 LEU   B CD1  1 
ATOM   6525 C CD2  . LEU   B 1 169 ? 27.315 -37.189 -13.654 1.00 23.43 ?  169 LEU   B CD2  1 
ATOM   6526 O OXT  . LEU   B 1 169 ? 30.801 -40.369 -12.690 1.00 22.19 -1 169 LEU   B OXT  1 
ATOM   6527 H H    . LEU   B 1 169 ? 31.799 -38.285 -11.977 1.00 19.37 ?  169 LEU   B H    1 
ATOM   6528 H HA   . LEU   B 1 169 ? 29.132 -38.016 -11.982 1.00 22.13 ?  169 LEU   B HA   1 
ATOM   6529 H HB2  . LEU   B 1 169 ? 30.587 -36.586 -13.689 1.00 24.24 ?  169 LEU   B HB2  1 
ATOM   6530 H HB3  . LEU   B 1 169 ? 29.885 -37.720 -14.543 1.00 24.24 ?  169 LEU   B HB3  1 
ATOM   6531 H HG   . LEU   B 1 169 ? 28.579 -35.684 -13.111 1.00 27.88 ?  169 LEU   B HG   1 
ATOM   6532 H HD11 . LEU   B 1 169 ? 27.746 -35.054 -15.181 1.00 29.38 ?  169 LEU   B HD11 1 
ATOM   6533 H HD12 . LEU   B 1 169 ? 29.334 -35.048 -15.206 1.00 29.38 ?  169 LEU   B HD12 1 
ATOM   6534 H HD13 . LEU   B 1 169 ? 28.534 -36.251 -15.865 1.00 29.38 ?  169 LEU   B HD13 1 
ATOM   6535 H HD21 . LEU   B 1 169 ? 26.561 -36.720 -14.039 1.00 28.13 ?  169 LEU   B HD21 1 
ATOM   6536 H HD22 . LEU   B 1 169 ? 27.445 -38.039 -14.107 1.00 28.13 ?  169 LEU   B HD22 1 
ATOM   6537 H HD23 . LEU   B 1 169 ? 27.164 -37.341 -12.708 1.00 28.13 ?  169 LEU   B HD23 1 
HETATM 6538 N N2   B A1A5D C 2 .   ? 15.439 5.560   4.463   0.11 11.76 ?  201 A1A5D A N2   1 
HETATM 6539 C C3   B A1A5D C 2 .   ? 14.005 -0.953  0.279   0.11 11.44 ?  201 A1A5D A C3   1 
HETATM 6540 C C6   B A1A5D C 2 .   ? 15.177 2.856   1.917   0.11 10.77 ?  201 A1A5D A C6   1 
HETATM 6541 C C9   B A1A5D C 2 .   ? 15.247 5.823   5.767   0.11 12.18 ?  201 A1A5D A C9   1 
HETATM 6542 C C12  B A1A5D C 2 .   ? 15.375 3.118   4.713   0.11 11.22 ?  201 A1A5D A C12  1 
HETATM 6543 C C14  B A1A5D C 2 .   ? 12.093 -1.143  1.953   0.11 9.97  ?  201 A1A5D A C14  1 
HETATM 6544 C C1   B A1A5D C 2 .   ? 12.276 -2.832  0.070   0.11 11.26 ?  201 A1A5D A C1   1 
HETATM 6545 C C10  B A1A5D C 2 .   ? 14.966 4.653   6.715   0.11 12.18 ?  201 A1A5D A C10  1 
HETATM 6546 C C11  B A1A5D C 2 .   ? 15.488 3.292   6.218   0.11 11.41 ?  201 A1A5D A C11  1 
HETATM 6547 C C13  B A1A5D C 2 .   ? 15.287 1.839   4.130   0.11 10.96 ?  201 A1A5D A C13  1 
HETATM 6548 C C2   B A1A5D C 2 .   ? 12.536 -1.378  0.496   0.11 10.95 ?  201 A1A5D A C2   1 
HETATM 6549 C C4   B A1A5D C 2 .   ? 15.087 0.322   2.120   0.11 11.14 ?  201 A1A5D A C4   1 
HETATM 6550 C C5   B A1A5D C 2 .   ? 15.192 1.694   2.726   0.11 10.82 ?  201 A1A5D A C5   1 
HETATM 6551 C C7   B A1A5D C 2 .   ? 15.264 4.134   2.501   0.11 10.71 ?  201 A1A5D A C7   1 
HETATM 6552 C C8   B A1A5D C 2 .   ? 15.373 4.267   3.894   0.11 11.19 ?  201 A1A5D A C8   1 
HETATM 6553 N N1   B A1A5D C 2 .   ? 14.295 0.255   1.041   0.11 11.68 ?  201 A1A5D A N1   1 
HETATM 6554 O O1   B A1A5D C 2 .   ? 15.663 -0.651  2.599   0.11 11.01 ?  201 A1A5D A O1   1 
HETATM 6555 O O2   B A1A5D C 2 .   ? 15.293 6.962   6.221   0.11 12.24 ?  201 A1A5D A O2   1 
HETATM 6556 O O3   B A1A5D C 2 .   ? 10.996 -0.575  2.151   0.11 10.68 ?  201 A1A5D A O3   1 
HETATM 6557 O O4   B A1A5D C 2 .   ? 12.871 -1.534  2.854   0.11 8.87  ?  201 A1A5D A O4   1 
HETATM 6558 H H10  B A1A5D C 2 .   ? 15.623 6.338   3.844   0.11 14.12 ?  201 A1A5D A H10  1 
HETATM 6559 H H5   B A1A5D C 2 .   ? 14.202 -0.758  -0.777  0.11 13.74 ?  201 A1A5D A H5   1 
HETATM 6560 H H6   B A1A5D C 2 .   ? 14.677 -1.752  0.592   0.11 13.74 ?  201 A1A5D A H6   1 
HETATM 6561 H H8   B A1A5D C 2 .   ? 15.105 2.786   0.842   0.11 12.94 ?  201 A1A5D A H8   1 
HETATM 6562 H H2   B A1A5D C 2 .   ? 12.449 -2.970  -0.996  0.11 13.53 ?  201 A1A5D A H2   1 
HETATM 6563 H H3   B A1A5D C 2 .   ? 11.243 -3.110  0.273   0.11 13.53 ?  201 A1A5D A H3   1 
HETATM 6564 H H4   B A1A5D C 2 .   ? 12.918 -3.527  0.610   0.11 13.53 ?  201 A1A5D A H4   1 
HETATM 6565 H H12  B A1A5D C 2 .   ? 13.900 4.616   6.865   0.11 14.63 ?  201 A1A5D A H12  1 
HETATM 6566 H H11  B A1A5D C 2 .   ? 15.383 4.874   7.691   0.11 14.63 ?  201 A1A5D A H11  1 
HETATM 6567 H H13  B A1A5D C 2 .   ? 16.540 3.202   6.490   0.11 13.71 ?  201 A1A5D A H13  1 
HETATM 6568 H H14  B A1A5D C 2 .   ? 14.960 2.482   6.726   0.11 13.71 ?  201 A1A5D A H14  1 
HETATM 6569 H H15  B A1A5D C 2 .   ? 15.302 0.969   4.767   0.11 13.17 ?  201 A1A5D A H15  1 
HETATM 6570 H H1   B A1A5D C 2 .   ? 11.912 -0.732  -0.127  0.11 13.15 ?  201 A1A5D A H1   1 
HETATM 6571 H H9   B A1A5D C 2 .   ? 15.255 5.015   1.875   0.11 12.87 ?  201 A1A5D A H9   1 
HETATM 6572 H H7   B A1A5D C 2 .   ? 13.846 1.103   0.726   0.11 14.04 ?  201 A1A5D A H7   1 
HETATM 6573 O O1   C A1A5E D 3 .   ? 15.092 4.946   1.890   0.11 13.34 ?  202 A1A5E A O1   1 
HETATM 6574 C C1   C A1A5E D 3 .   ? 15.524 -0.266  2.647   0.11 14.08 ?  202 A1A5E A C1   1 
HETATM 6575 C C2   C A1A5E D 3 .   ? 14.496 0.672   1.985   0.11 14.35 ?  202 A1A5E A C2   1 
HETATM 6576 C C3   C A1A5E D 3 .   ? 15.092 2.077   1.718   0.11 13.93 ?  202 A1A5E A C3   1 
HETATM 6577 C C4   C A1A5E D 3 .   ? 15.132 4.257   2.911   0.11 12.98 ?  202 A1A5E A C4   1 
HETATM 6578 C C5   C A1A5E D 3 .   ? 15.191 4.912   4.262   0.11 12.63 ?  202 A1A5E A C5   1 
HETATM 6579 C C6   C A1A5E D 3 .   ? 15.420 4.148   5.431   0.11 12.64 ?  202 A1A5E A C6   1 
HETATM 6580 C C7   C A1A5E D 3 .   ? 15.474 4.766   6.690   0.11 13.05 ?  202 A1A5E A C7   1 
HETATM 6581 C C8   C A1A5E D 3 .   ? 15.305 6.158   6.797   0.11 13.38 ?  202 A1A5E A C8   1 
HETATM 6582 C C10  C A1A5E D 3 .   ? 15.158 9.052   7.137   0.11 14.54 ?  202 A1A5E A C10  1 
HETATM 6583 C C11  C A1A5E D 3 .   ? 14.914 8.438   5.742   0.11 14.12 ?  202 A1A5E A C11  1 
HETATM 6584 C C12  C A1A5E D 3 .   ? 15.086 6.933   5.639   0.11 13.41 ?  202 A1A5E A C12  1 
HETATM 6585 C C13  C A1A5E D 3 .   ? 15.028 6.311   4.376   0.11 13.06 ?  202 A1A5E A C13  1 
HETATM 6586 C C14  C A1A5E D 3 .   ? 13.896 0.039   0.711   0.11 14.50 ?  202 A1A5E A C14  1 
HETATM 6587 C C9   C A1A5E D 3 .   ? 15.316 8.074   8.312   0.11 14.60 ?  202 A1A5E A C9   1 
HETATM 6588 N N1   C A1A5E D 3 .   ? 15.136 2.912   2.908   0.11 13.39 ?  202 A1A5E A N1   1 
HETATM 6589 N N2   C A1A5E D 3 .   ? 15.374 6.755   8.074   0.11 13.93 ?  202 A1A5E A N2   1 
HETATM 6590 O O2   C A1A5E D 3 .   ? 15.391 8.520   9.455   0.11 15.11 ?  202 A1A5E A O2   1 
HETATM 6591 O O3   C A1A5E D 3 .   ? 13.402 0.801   -0.150  0.11 14.42 ?  202 A1A5E A O3   1 
HETATM 6592 O O4   C A1A5E D 3 .   ? 13.942 -1.208  0.617   0.11 14.65 ?  202 A1A5E A O4   1 
HETATM 6593 H H3   C A1A5E D 3 .   ? 15.165 -1.296  2.688   0.11 16.91 ?  202 A1A5E A H3   1 
HETATM 6594 H H2   C A1A5E D 3 .   ? 15.759 0.045   3.666   0.11 16.91 ?  202 A1A5E A H2   1 
HETATM 6595 H H4   C A1A5E D 3 .   ? 16.462 -0.268  2.089   0.11 16.91 ?  202 A1A5E A H4   1 
HETATM 6596 H H1   C A1A5E D 3 .   ? 13.673 0.795   2.691   0.11 17.23 ?  202 A1A5E A H1   1 
HETATM 6597 H H5   C A1A5E D 3 .   ? 14.505 2.587   0.958   0.11 16.74 ?  202 A1A5E A H5   1 
HETATM 6598 H H6   C A1A5E D 3 .   ? 16.108 1.988   1.326   0.11 16.74 ?  202 A1A5E A H6   1 
HETATM 6599 H H8   C A1A5E D 3 .   ? 15.540 3.072   5.376   0.11 15.18 ?  202 A1A5E A H8   1 
HETATM 6600 H H9   C A1A5E D 3 .   ? 15.635 4.161   7.569   0.11 15.67 ?  202 A1A5E A H9   1 
HETATM 6601 H H12  C A1A5E D 3 .   ? 14.378 9.776   7.368   0.11 17.47 ?  202 A1A5E A H12  1 
HETATM 6602 H H11  C A1A5E D 3 .   ? 16.085 9.627   7.098   0.11 17.47 ?  202 A1A5E A H11  1 
HETATM 6603 H H13  C A1A5E D 3 .   ? 13.908 8.696   5.413   0.11 16.96 ?  202 A1A5E A H13  1 
HETATM 6604 H H14  C A1A5E D 3 .   ? 15.587 8.894   5.015   0.11 16.96 ?  202 A1A5E A H14  1 
HETATM 6605 H H15  C A1A5E D 3 .   ? 14.861 6.913   3.494   0.11 15.69 ?  202 A1A5E A H15  1 
HETATM 6606 H H7   C A1A5E D 3 .   ? 15.173 2.422   3.788   0.11 16.08 ?  202 A1A5E A H7   1 
HETATM 6607 H H10  C A1A5E D 3 .   ? 15.480 6.136   8.863   0.11 16.73 ?  202 A1A5E A H10  1 
HETATM 6608 O O    B HOH   E 4 .   ? 15.494 -1.338  5.362   0.22 24.40 ?  301 HOH   A O    1 
HETATM 6609 O O    . HOH   E 4 .   ? 26.858 11.421  1.667   1.00 16.86 ?  302 HOH   A O    1 
HETATM 6610 O O    . HOH   E 4 .   ? 4.798  3.896   0.854   1.00 26.52 ?  303 HOH   A O    1 
HETATM 6611 O O    . HOH   E 4 .   ? 14.171 -4.506  -11.827 1.00 29.33 ?  304 HOH   A O    1 
HETATM 6612 O O    . HOH   E 4 .   ? 7.592  -6.323  -6.545  1.00 42.95 ?  305 HOH   A O    1 
HETATM 6613 O O    . HOH   E 4 .   ? 14.845 -4.670  20.599  1.00 43.33 ?  306 HOH   A O    1 
HETATM 6614 O O    . HOH   E 4 .   ? 12.127 0.358   15.005  1.00 35.61 ?  307 HOH   A O    1 
HETATM 6615 O O    . HOH   E 4 .   ? 34.478 -1.895  12.493  1.00 39.01 ?  308 HOH   A O    1 
HETATM 6616 O O    . HOH   E 4 .   ? 24.535 2.004   -6.977  1.00 18.09 ?  309 HOH   A O    1 
HETATM 6617 O O    . HOH   E 4 .   ? 15.227 -12.286 18.780  1.00 30.23 ?  310 HOH   A O    1 
HETATM 6618 O O    . HOH   E 4 .   ? 7.014  -8.156  12.007  1.00 22.67 ?  311 HOH   A O    1 
HETATM 6619 O O    . HOH   E 4 .   ? 14.424 -24.772 11.586  1.00 35.49 ?  312 HOH   A O    1 
HETATM 6620 O O    . HOH   E 4 .   ? 28.922 0.486   -9.684  1.00 20.65 ?  313 HOH   A O    1 
HETATM 6621 O O    . HOH   E 4 .   ? 11.075 1.574   12.909  1.00 23.36 ?  314 HOH   A O    1 
HETATM 6622 O O    . HOH   E 4 .   ? 11.594 -10.760 -10.044 1.00 40.74 ?  315 HOH   A O    1 
HETATM 6623 O O    . HOH   E 4 .   ? 42.492 10.522  5.233   1.00 19.80 ?  316 HOH   A O    1 
HETATM 6624 O O    . HOH   E 4 .   ? 34.000 -1.014  -8.901  1.00 27.20 ?  317 HOH   A O    1 
HETATM 6625 O O    . HOH   E 4 .   ? 9.107  -10.241 19.378  1.00 46.45 ?  318 HOH   A O    1 
HETATM 6626 O O    . HOH   E 4 .   ? 15.230 3.933   17.951  1.00 41.93 ?  319 HOH   A O    1 
HETATM 6627 O O    . HOH   E 4 .   ? 7.951  -12.546 -0.810  1.00 20.34 ?  320 HOH   A O    1 
HETATM 6628 O O    . HOH   E 4 .   ? 14.736 -14.045 16.724  1.00 24.68 ?  321 HOH   A O    1 
HETATM 6629 O O    . HOH   E 4 .   ? 36.198 -5.069  -0.550  1.00 30.50 ?  322 HOH   A O    1 
HETATM 6630 O O    . HOH   E 4 .   ? 18.927 -21.991 6.898   1.00 33.48 ?  323 HOH   A O    1 
HETATM 6631 O O    . HOH   E 4 .   ? 8.044  -21.491 4.010   1.00 47.52 ?  324 HOH   A O    1 
HETATM 6632 O O    . HOH   E 4 .   ? 26.453 -19.330 -1.821  1.00 13.72 ?  325 HOH   A O    1 
HETATM 6633 O O    . HOH   E 4 .   ? 30.964 -18.168 7.773   1.00 26.23 ?  326 HOH   A O    1 
HETATM 6634 O O    . HOH   E 4 .   ? 30.225 -13.277 -8.605  1.00 19.41 ?  327 HOH   A O    1 
HETATM 6635 O O    . HOH   E 4 .   ? 17.184 -18.100 15.030  1.00 26.25 ?  328 HOH   A O    1 
HETATM 6636 O O    . HOH   E 4 .   ? 28.239 -0.069  -13.363 1.00 34.91 ?  329 HOH   A O    1 
HETATM 6637 O O    . HOH   E 4 .   ? 14.460 -0.490  -12.042 1.00 24.03 ?  330 HOH   A O    1 
HETATM 6638 O O    . HOH   E 4 .   ? 19.794 -12.416 -9.006  1.00 24.72 ?  331 HOH   A O    1 
HETATM 6639 O O    . HOH   E 4 .   ? 28.267 -6.376  19.659  1.00 44.32 ?  332 HOH   A O    1 
HETATM 6640 O O    . HOH   E 4 .   ? 17.481 -1.676  0.507   1.00 17.78 ?  333 HOH   A O    1 
HETATM 6641 O O    A HOH   E 4 .   ? 3.608  -9.454  9.804   0.78 30.69 ?  334 HOH   A O    1 
HETATM 6642 O O    . HOH   E 4 .   ? 27.294 13.779  2.927   1.00 28.60 ?  335 HOH   A O    1 
HETATM 6643 O O    . HOH   E 4 .   ? 37.576 2.735   10.148  1.00 30.07 ?  336 HOH   A O    1 
HETATM 6644 O O    . HOH   E 4 .   ? 0.797  -4.408  0.353   1.00 30.83 ?  337 HOH   A O    1 
HETATM 6645 O O    . HOH   E 4 .   ? 20.561 -19.694 -5.074  1.00 27.26 ?  338 HOH   A O    1 
HETATM 6646 O O    . HOH   E 4 .   ? 42.612 4.316   5.359   1.00 31.03 ?  339 HOH   A O    1 
HETATM 6647 O O    . HOH   E 4 .   ? 14.596 -3.595  3.180   1.00 18.31 ?  340 HOH   A O    1 
HETATM 6648 O O    . HOH   E 4 .   ? 25.658 -0.736  -7.323  1.00 14.55 ?  341 HOH   A O    1 
HETATM 6649 O O    . HOH   E 4 .   ? 22.453 5.303   19.129  1.00 42.59 ?  342 HOH   A O    1 
HETATM 6650 O O    . HOH   E 4 .   ? 37.205 -2.798  9.669   1.00 41.60 ?  343 HOH   A O    1 
HETATM 6651 O O    . HOH   E 4 .   ? 22.339 -19.268 11.357  1.00 33.59 ?  344 HOH   A O    1 
HETATM 6652 O O    . HOH   E 4 .   ? 35.751 -12.706 6.781   1.00 15.93 ?  345 HOH   A O    1 
HETATM 6653 O O    . HOH   E 4 .   ? 10.439 -22.161 -1.166  1.00 41.32 ?  346 HOH   A O    1 
HETATM 6654 O O    . HOH   E 4 .   ? 18.731 -19.461 13.551  1.00 38.29 ?  347 HOH   A O    1 
HETATM 6655 O O    . HOH   E 4 .   ? 38.596 4.934   6.947   1.00 15.57 ?  348 HOH   A O    1 
HETATM 6656 O O    . HOH   E 4 .   ? 21.215 -2.355  -2.082  1.00 15.07 ?  349 HOH   A O    1 
HETATM 6657 O O    . HOH   E 4 .   ? 38.333 10.054  7.195   1.00 32.92 ?  350 HOH   A O    1 
HETATM 6658 O O    . HOH   E 4 .   ? 39.751 -0.998  -5.231  1.00 19.55 ?  351 HOH   A O    1 
HETATM 6659 O O    . HOH   E 4 .   ? 15.555 12.062  8.071   1.00 38.05 ?  352 HOH   A O    1 
HETATM 6660 O O    . HOH   E 4 .   ? 17.093 -17.778 -5.032  1.00 26.38 ?  353 HOH   A O    1 
HETATM 6661 O O    . HOH   E 4 .   ? 44.359 7.106   6.441   1.00 25.76 ?  354 HOH   A O    1 
HETATM 6662 O O    . HOH   E 4 .   ? 31.736 -9.317  -6.670  1.00 20.38 ?  355 HOH   A O    1 
HETATM 6663 O O    . HOH   E 4 .   ? 37.444 11.897  4.975   1.00 31.56 ?  356 HOH   A O    1 
HETATM 6664 O O    . HOH   E 4 .   ? 13.504 -15.179 -7.466  1.00 26.46 ?  357 HOH   A O    1 
HETATM 6665 O O    . HOH   E 4 .   ? 31.720 8.211   14.836  1.00 25.69 ?  358 HOH   A O    1 
HETATM 6666 O O    . HOH   E 4 .   ? 9.838  -21.344 5.719   1.00 18.18 ?  359 HOH   A O    1 
HETATM 6667 O O    . HOH   E 4 .   ? 23.996 -2.059  -2.040  1.00 10.42 ?  360 HOH   A O    1 
HETATM 6668 O O    . HOH   E 4 .   ? 33.652 -7.165  4.246   1.00 16.28 ?  361 HOH   A O    1 
HETATM 6669 O O    . HOH   E 4 .   ? 22.765 12.528  1.667   1.00 14.92 ?  362 HOH   A O    1 
HETATM 6670 O O    . HOH   E 4 .   ? 20.049 4.551   -7.572  1.00 17.61 ?  363 HOH   A O    1 
HETATM 6671 O O    . HOH   E 4 .   ? 21.872 -21.911 8.394   1.00 28.51 ?  364 HOH   A O    1 
HETATM 6672 O O    . HOH   E 4 .   ? 31.035 -13.926 -2.530  1.00 12.89 ?  365 HOH   A O    1 
HETATM 6673 O O    . HOH   E 4 .   ? 14.045 -5.030  17.627  1.00 23.20 ?  366 HOH   A O    1 
HETATM 6674 O O    . HOH   E 4 .   ? 31.023 6.187   -12.334 1.00 30.76 ?  367 HOH   A O    1 
HETATM 6675 O O    . HOH   E 4 .   ? 16.460 -22.020 0.951   1.00 28.31 ?  368 HOH   A O    1 
HETATM 6676 O O    . HOH   E 4 .   ? 14.279 -21.172 -4.221  1.00 30.09 ?  369 HOH   A O    1 
HETATM 6677 O O    . HOH   E 4 .   ? 30.845 3.074   8.282   1.00 12.10 ?  370 HOH   A O    1 
HETATM 6678 O O    . HOH   E 4 .   ? 16.997 -19.283 4.925   1.00 14.99 ?  371 HOH   A O    1 
HETATM 6679 O O    B HOH   E 4 .   ? 13.294 -1.459  -6.866  0.22 12.50 ?  372 HOH   A O    1 
HETATM 6680 O O    . HOH   E 4 .   ? 24.405 3.601   -1.786  1.00 15.03 ?  373 HOH   A O    1 
HETATM 6681 O O    . HOH   E 4 .   ? 18.610 -2.364  -16.313 1.00 42.29 ?  374 HOH   A O    1 
HETATM 6682 O O    . HOH   E 4 .   ? 18.583 9.465   8.996   1.00 21.06 ?  375 HOH   A O    1 
HETATM 6683 O O    . HOH   E 4 .   ? 43.931 8.429   -3.149  1.00 23.86 ?  376 HOH   A O    1 
HETATM 6684 O O    A HOH   E 4 .   ? 13.291 -1.400  -6.453  0.78 16.08 ?  377 HOH   A O    1 
HETATM 6685 O O    . HOH   E 4 .   ? 43.396 7.835   2.663   1.00 24.23 ?  378 HOH   A O    1 
HETATM 6686 O O    . HOH   E 4 .   ? 21.291 10.303  15.044  1.00 37.19 ?  379 HOH   A O    1 
HETATM 6687 O O    . HOH   E 4 .   ? 27.573 -10.673 14.039  1.00 16.73 ?  380 HOH   A O    1 
HETATM 6688 O O    . HOH   E 4 .   ? -0.664 -8.382  2.261   1.00 44.46 ?  381 HOH   A O    1 
HETATM 6689 O O    . HOH   E 4 .   ? 18.891 -0.635  -1.584  1.00 13.38 ?  382 HOH   A O    1 
HETATM 6690 O O    . HOH   E 4 .   ? 33.492 -17.003 7.996   1.00 19.06 ?  383 HOH   A O    1 
HETATM 6691 O O    . HOH   E 4 .   ? 21.349 3.151   -0.284  1.00 12.41 ?  384 HOH   A O    1 
HETATM 6692 O O    . HOH   E 4 .   ? 37.547 -2.000  5.761   1.00 25.33 ?  385 HOH   A O    1 
HETATM 6693 O O    . HOH   E 4 .   ? 24.755 -17.588 12.679  1.00 23.56 ?  386 HOH   A O    1 
HETATM 6694 O O    . HOH   E 4 .   ? 24.331 -7.835  14.459  1.00 16.97 ?  387 HOH   A O    1 
HETATM 6695 O O    . HOH   E 4 .   ? 31.664 -7.277  -9.908  1.00 20.46 ?  388 HOH   A O    1 
HETATM 6696 O O    A HOH   E 4 .   ? 14.286 0.581   6.873   0.78 20.57 ?  389 HOH   A O    1 
HETATM 6697 O O    A HOH   E 4 .   ? -0.477 -3.065  3.195   0.78 35.54 ?  390 HOH   A O    1 
HETATM 6698 O O    . HOH   E 4 .   ? 27.435 2.296   18.716  1.00 29.09 ?  391 HOH   A O    1 
HETATM 6699 O O    . HOH   E 4 .   ? 8.936  -11.985 17.276  1.00 47.02 ?  392 HOH   A O    1 
HETATM 6700 O O    . HOH   E 4 .   ? 23.476 11.401  4.123   1.00 12.43 ?  393 HOH   A O    1 
HETATM 6701 O O    . HOH   E 4 .   ? 18.408 4.965   -15.051 1.00 44.80 ?  394 HOH   A O    1 
HETATM 6702 O O    A HOH   E 4 .   ? 15.208 -21.608 14.187  0.78 16.43 ?  395 HOH   A O    1 
HETATM 6703 O O    . HOH   E 4 .   ? 6.519  -5.622  11.294  1.00 20.87 ?  396 HOH   A O    1 
HETATM 6704 O O    B HOH   E 4 .   ? 14.267 -0.174  6.964   0.22 22.94 ?  397 HOH   A O    1 
HETATM 6705 O O    . HOH   E 4 .   ? 32.781 -9.265  5.898   1.00 19.94 ?  398 HOH   A O    1 
HETATM 6706 O O    . HOH   E 4 .   ? 30.769 1.811   16.678  1.00 20.80 ?  399 HOH   A O    1 
HETATM 6707 O O    . HOH   E 4 .   ? 20.556 -20.035 2.788   1.00 16.62 ?  400 HOH   A O    1 
HETATM 6708 O O    . HOH   E 4 .   ? 14.047 -23.061 7.431   1.00 17.69 ?  401 HOH   A O    1 
HETATM 6709 O O    . HOH   E 4 .   ? 27.291 -5.870  -13.999 1.00 35.67 ?  402 HOH   A O    1 
HETATM 6710 O O    . HOH   E 4 .   ? 15.091 -8.043  -9.571  1.00 21.44 ?  403 HOH   A O    1 
HETATM 6711 O O    . HOH   E 4 .   ? 23.972 -15.660 -9.213  1.00 31.45 ?  404 HOH   A O    1 
HETATM 6712 O O    . HOH   E 4 .   ? 44.933 -0.657  2.941   1.00 41.19 ?  405 HOH   A O    1 
HETATM 6713 O O    . HOH   E 4 .   ? 26.932 4.175   -0.644  1.00 12.49 ?  406 HOH   A O    1 
HETATM 6714 O O    A HOH   E 4 .   ? 5.312  2.654   5.368   0.78 30.50 ?  407 HOH   A O    1 
HETATM 6715 O O    . HOH   E 4 .   ? 22.714 -11.954 21.837  1.00 38.80 ?  408 HOH   A O    1 
HETATM 6716 O O    . HOH   E 4 .   ? 38.132 -1.400  -1.989  1.00 18.51 ?  409 HOH   A O    1 
HETATM 6717 O O    . HOH   E 4 .   ? 21.725 -13.741 -8.137  1.00 35.20 ?  410 HOH   A O    1 
HETATM 6718 O O    . HOH   E 4 .   ? 27.920 0.863   -7.134  1.00 13.48 ?  411 HOH   A O    1 
HETATM 6719 O O    B HOH   E 4 .   ? 11.893 -1.911  -3.358  0.22 10.54 ?  412 HOH   A O    1 
HETATM 6720 O O    . HOH   E 4 .   ? 16.276 -14.184 20.327  1.00 46.13 ?  413 HOH   A O    1 
HETATM 6721 O O    . HOH   E 4 .   ? 41.615 1.522   4.939   1.00 36.15 ?  414 HOH   A O    1 
HETATM 6722 O O    . HOH   E 4 .   ? 30.131 -10.158 12.998  1.00 20.86 ?  415 HOH   A O    1 
HETATM 6723 O O    . HOH   E 4 .   ? 28.504 -10.569 -13.976 1.00 44.09 ?  416 HOH   A O    1 
HETATM 6724 O O    . HOH   E 4 .   ? 15.859 2.106   24.841  1.00 49.34 ?  417 HOH   A O    1 
HETATM 6725 O O    A HOH   E 4 .   ? 15.806 -0.935  5.337   0.78 22.30 ?  418 HOH   A O    1 
HETATM 6726 O O    . HOH   E 4 .   ? 30.391 -13.004 13.482  1.00 19.38 ?  419 HOH   A O    1 
HETATM 6727 O O    . HOH   E 4 .   ? 40.869 -8.206  -6.721  1.00 37.86 ?  420 HOH   A O    1 
HETATM 6728 O O    . HOH   E 4 .   ? 22.770 8.142   18.401  1.00 47.26 ?  421 HOH   A O    1 
HETATM 6729 O O    . HOH   E 4 .   ? 10.368 -13.679 -1.630  1.00 16.97 ?  422 HOH   A O    1 
HETATM 6730 O O    . HOH   E 4 .   ? 6.754  -3.397  13.099  1.00 30.55 ?  423 HOH   A O    1 
HETATM 6731 O O    . HOH   E 4 .   ? 23.902 -20.284 -1.392  1.00 15.67 ?  424 HOH   A O    1 
HETATM 6732 O O    . HOH   E 4 .   ? 24.041 3.950   -4.776  1.00 19.83 ?  425 HOH   A O    1 
HETATM 6733 O O    . HOH   E 4 .   ? 34.979 -5.213  -3.112  1.00 17.61 ?  426 HOH   A O    1 
HETATM 6734 O O    . HOH   E 4 .   ? 16.255 16.739  8.688   1.00 30.01 ?  427 HOH   A O    1 
HETATM 6735 O O    . HOH   E 4 .   ? 27.221 -3.277  19.282  1.00 33.94 ?  428 HOH   A O    1 
HETATM 6736 O O    . HOH   E 4 .   ? 32.610 -4.257  -9.942  1.00 26.22 ?  429 HOH   A O    1 
HETATM 6737 O O    . HOH   E 4 .   ? 36.736 -5.022  5.355   1.00 23.73 ?  430 HOH   A O    1 
HETATM 6738 O O    . HOH   E 4 .   ? 32.553 -10.658 3.164   1.00 29.92 ?  431 HOH   A O    1 
HETATM 6739 O O    A HOH   E 4 .   ? 11.067 -0.360  2.011   0.89 24.59 ?  432 HOH   A O    1 
HETATM 6740 O O    . HOH   E 4 .   ? 20.593 -17.759 24.804  1.00 51.70 ?  433 HOH   A O    1 
HETATM 6741 O O    A HOH   E 4 .   ? 16.025 6.969   3.073   0.78 18.11 ?  434 HOH   A O    1 
HETATM 6742 O O    . HOH   E 4 .   ? 9.470  -16.242 -1.949  1.00 35.20 ?  435 HOH   A O    1 
HETATM 6743 O O    . HOH   E 4 .   ? 11.834 -10.849 17.035  1.00 26.10 ?  436 HOH   A O    1 
HETATM 6744 O O    . HOH   E 4 .   ? -1.258 -4.565  7.789   1.00 51.34 ?  437 HOH   A O    1 
HETATM 6745 O O    B HOH   E 4 .   ? 15.875 3.096   -1.732  0.22 10.66 ?  438 HOH   A O    1 
HETATM 6746 O O    . HOH   E 4 .   ? 23.203 7.556   -3.113  1.00 32.06 ?  439 HOH   A O    1 
HETATM 6747 O O    . HOH   E 4 .   ? 18.850 2.066   -0.675  1.00 13.47 ?  440 HOH   A O    1 
HETATM 6748 O O    A HOH   E 4 .   ? 16.254 2.971   -1.366  0.78 14.69 ?  441 HOH   A O    1 
HETATM 6749 O O    . HOH   E 4 .   ? 23.283 -20.958 1.298   1.00 17.04 ?  442 HOH   A O    1 
HETATM 6750 O O    . HOH   E 4 .   ? 21.358 -9.259  21.355  1.00 49.05 ?  443 HOH   A O    1 
HETATM 6751 O O    . HOH   E 4 .   ? 18.436 -16.072 16.407  1.00 36.47 ?  444 HOH   A O    1 
HETATM 6752 O O    . HOH   E 4 .   ? 23.635 -8.099  17.092  1.00 21.82 ?  445 HOH   A O    1 
HETATM 6753 O O    . HOH   E 4 .   ? 21.596 -14.678 18.047  1.00 47.75 ?  446 HOH   A O    1 
HETATM 6754 O O    . HOH   E 4 .   ? 34.403 -8.080  -0.611  1.00 26.93 ?  447 HOH   A O    1 
HETATM 6755 O O    . HOH   E 4 .   ? 30.618 14.773  2.822   1.00 18.40 ?  448 HOH   A O    1 
HETATM 6756 O O    . HOH   E 4 .   ? 31.329 -12.765 -0.016  1.00 19.07 ?  449 HOH   A O    1 
HETATM 6757 O O    . HOH   E 4 .   ? 19.475 -11.082 24.224  1.00 61.10 ?  450 HOH   A O    1 
HETATM 6758 O O    . HOH   E 4 .   ? 37.666 -8.790  -3.426  1.00 24.09 ?  451 HOH   A O    1 
HETATM 6759 O O    B HOH   E 4 .   ? 5.696  3.319   4.639   0.22 25.86 ?  452 HOH   A O    1 
HETATM 6760 O O    A HOH   E 4 .   ? 14.030 -0.324  3.534   0.78 33.43 ?  453 HOH   A O    1 
HETATM 6761 O O    . HOH   E 4 .   ? 29.834 -16.075 10.627  1.00 35.77 ?  454 HOH   A O    1 
HETATM 6762 O O    . HOH   E 4 .   ? 27.785 7.072   -6.357  1.00 36.12 ?  455 HOH   A O    1 
HETATM 6763 O O    . HOH   E 4 .   ? 25.420 8.239   -4.767  1.00 28.66 ?  456 HOH   A O    1 
HETATM 6764 O O    . HOH   E 4 .   ? 32.485 -15.958 10.766  1.00 38.72 ?  457 HOH   A O    1 
HETATM 6765 O O    . HOH   E 4 .   ? 29.730 -1.996  -12.737 1.00 44.09 ?  458 HOH   A O    1 
HETATM 6766 O O    . HOH   E 4 .   ? 19.828 -17.306 -5.074  1.00 23.31 ?  459 HOH   A O    1 
HETATM 6767 O O    . HOH   E 4 .   ? 23.150 -22.305 -3.292  1.00 34.46 ?  460 HOH   A O    1 
HETATM 6768 O O    . HOH   E 4 .   ? 24.974 5.649   20.805  1.00 50.16 ?  461 HOH   A O    1 
HETATM 6769 O O    . HOH   E 4 .   ? 24.618 14.519  7.879   1.00 34.79 ?  462 HOH   A O    1 
HETATM 6770 O O    . HOH   E 4 .   ? 39.595 -7.077  -3.661  1.00 47.79 ?  463 HOH   A O    1 
HETATM 6771 O O    . HOH   E 4 .   ? 23.519 13.747  5.510   1.00 19.58 ?  464 HOH   A O    1 
HETATM 6772 O O    . HOH   E 4 .   ? 27.482 -11.420 16.521  1.00 36.47 ?  465 HOH   A O    1 
HETATM 6773 O O    . HOH   E 4 .   ? 15.748 -21.528 3.708   1.00 25.25 ?  466 HOH   A O    1 
HETATM 6774 O O    B HOH   E 4 .   ? 15.200 5.443   -0.923  0.22 18.64 ?  467 HOH   A O    1 
HETATM 6775 O O    . HOH   E 4 .   ? 21.981 5.295   -5.895  1.00 27.36 ?  468 HOH   A O    1 
HETATM 6776 O O    . HOH   E 4 .   ? 26.897 11.698  -1.397  1.00 28.25 ?  469 HOH   A O    1 
HETATM 6777 O O    . HOH   E 4 .   ? 18.750 10.844  11.315  1.00 35.33 ?  470 HOH   A O    1 
HETATM 6778 O O    B HOH   E 4 .   ? 11.252 0.570   -2.483  0.22 18.56 ?  471 HOH   A O    1 
HETATM 6779 O O    . HOH   E 4 .   ? 25.812 10.785  -3.754  1.00 27.15 ?  472 HOH   A O    1 
HETATM 6780 O O    . HOH   E 4 .   ? 12.338 1.540   17.427  1.00 44.02 ?  473 HOH   A O    1 
HETATM 6781 O O    . HOH   E 4 .   ? 12.054 -13.395 16.540  1.00 51.21 ?  474 HOH   A O    1 
HETATM 6782 O O    . HOH   E 4 .   ? 10.922 -14.979 -6.043  1.00 35.37 ?  475 HOH   A O    1 
HETATM 6783 O O    . HOH   E 4 .   ? 35.170 7.423   12.291  1.00 51.36 ?  476 HOH   A O    1 
HETATM 6784 O O    . HOH   E 4 .   ? 28.958 8.918   17.525  1.00 40.16 ?  477 HOH   A O    1 
HETATM 6785 O O    . HOH   E 4 .   ? 15.653 -17.003 -6.982  1.00 29.51 ?  478 HOH   A O    1 
HETATM 6786 O O    . HOH   E 4 .   ? 18.004 -16.184 -8.757  1.00 38.55 ?  479 HOH   A O    1 
HETATM 6787 O O    . HOH   E 4 .   ? 14.009 -10.247 -10.853 1.00 32.10 ?  480 HOH   A O    1 
HETATM 6788 O O    . HOH   E 4 .   ? 30.779 0.669   19.222  1.00 39.09 ?  481 HOH   A O    1 
HETATM 6789 O O    . HOH   E 4 .   ? 23.123 11.803  -4.069  1.00 19.07 ?  482 HOH   A O    1 
HETATM 6790 O O    B HOH   E 4 .   ? 10.682 -1.588  -5.596  0.22 13.74 ?  483 HOH   A O    1 
HETATM 6791 O O    . HOH   E 4 .   ? 17.383 -18.770 19.855  1.00 45.83 ?  484 HOH   A O    1 
HETATM 6792 O O    . HOH   E 4 .   ? 15.946 -6.615  -11.755 1.00 36.87 ?  485 HOH   A O    1 
HETATM 6793 O O    . HOH   E 4 .   ? 40.901 -3.991  -0.361  1.00 38.12 ?  486 HOH   A O    1 
HETATM 6794 O O    . HOH   E 4 .   ? 16.832 -20.625 16.177  1.00 28.14 ?  487 HOH   A O    1 
HETATM 6795 O O    . HOH   E 4 .   ? 44.557 10.411  -1.608  1.00 28.60 ?  488 HOH   A O    1 
HETATM 6796 O O    . HOH   E 4 .   ? 41.697 9.274   -4.116  1.00 30.99 ?  489 HOH   A O    1 
HETATM 6797 O O    . HOH   E 4 .   ? 18.375 -23.185 1.947   1.00 37.10 ?  490 HOH   A O    1 
HETATM 6798 O O    . HOH   E 4 .   ? 28.522 -4.614  -12.334 1.00 35.33 ?  491 HOH   A O    1 
HETATM 6799 O O    . HOH   E 4 .   ? 23.341 -12.843 19.342  1.00 44.35 ?  492 HOH   A O    1 
HETATM 6800 O O    . HOH   E 4 .   ? 39.170 2.382   7.492   1.00 32.08 ?  493 HOH   A O    1 
HETATM 6801 O O    . HOH   E 4 .   ? 31.433 -0.538  -10.565 1.00 27.47 ?  494 HOH   A O    1 
HETATM 6802 O O    . HOH   E 4 .   ? 40.554 -0.238  -7.790  1.00 35.93 ?  495 HOH   A O    1 
HETATM 6803 O O    . HOH   E 4 .   ? 19.966 -22.328 4.124   1.00 27.37 ?  496 HOH   A O    1 
HETATM 6804 O O    . HOH   E 4 .   ? 28.648 -7.807  -15.291 1.00 45.52 ?  497 HOH   A O    1 
HETATM 6805 O O    . HOH   E 4 .   ? 16.168 -23.359 5.759   1.00 28.12 ?  498 HOH   A O    1 
HETATM 6806 O O    . HOH   E 4 .   ? 14.035 -25.382 8.903   1.00 29.18 ?  499 HOH   A O    1 
HETATM 6807 O O    . HOH   E 4 .   ? 30.773 5.854   -14.657 1.00 35.35 ?  500 HOH   A O    1 
HETATM 6808 O O    . HOH   E 4 .   ? 20.449 -16.057 -7.358  1.00 29.02 ?  501 HOH   A O    1 
HETATM 6809 O O    . HOH   E 4 .   ? 30.692 -5.763  -11.843 1.00 46.83 ?  502 HOH   A O    1 
HETATM 6810 O O    . HOH   E 4 .   ? 23.079 -23.747 1.648   1.00 29.62 ?  503 HOH   A O    1 
HETATM 6811 O O    . HOH   E 4 .   ? 37.386 -6.682  7.517   1.00 25.86 ?  504 HOH   A O    1 
HETATM 6812 O O    . HOH   E 4 .   ? 28.939 14.364  0.955   1.00 46.54 ?  505 HOH   A O    1 
HETATM 6813 O O    . HOH   E 4 .   ? 39.554 -0.035  6.598   1.00 28.96 ?  506 HOH   A O    1 
HETATM 6814 O O    . HOH   E 4 .   ? 8.190  -2.949  -5.646  1.00 48.49 ?  507 HOH   A O    1 
HETATM 6815 O O    . HOH   E 4 .   ? 38.087 13.913  6.758   1.00 41.36 ?  508 HOH   A O    1 
HETATM 6816 O O    . HOH   E 4 .   ? 21.977 -24.075 4.374   1.00 24.16 ?  509 HOH   A O    1 
HETATM 6817 O O    . HOH   E 4 .   ? 36.496 -6.490  10.187  1.00 44.60 ?  510 HOH   A O    1 
HETATM 6818 O O    . HOH   E 4 .   ? 17.340 -6.629  -14.138 1.00 35.72 ?  511 HOH   A O    1 
HETATM 6819 O O    B HOH   E 4 .   ? 9.456  0.899   -5.105  0.22 16.73 ?  512 HOH   A O    1 
HETATM 6820 O O    A HOH   E 4 .   ? 14.863 8.662   4.978   0.78 42.57 ?  513 HOH   A O    1 
HETATM 6821 O O    . HOH   E 4 .   ? 24.062 8.964   -7.214  1.00 35.00 ?  514 HOH   A O    1 
HETATM 6822 O O    . HOH   E 4 .   ? 16.294 -21.230 18.795  1.00 39.03 ?  515 HOH   A O    1 
HETATM 6823 O O    . HOH   E 4 .   ? 15.903 -12.283 27.535  1.00 43.68 ?  516 HOH   A O    1 
HETATM 6824 O O    . HOH   E 4 .   ? 14.705 -22.835 19.848  1.00 36.63 ?  517 HOH   A O    1 
HETATM 6825 O O    . HOH   F 4 .   ? 29.752 -22.425 5.393   1.00 19.72 ?  201 HOH   B O    1 
HETATM 6826 O O    . HOH   F 4 .   ? 48.158 -6.885  15.550  1.00 33.64 ?  202 HOH   B O    1 
HETATM 6827 O O    . HOH   F 4 .   ? 47.352 -7.468  -4.035  1.00 39.00 ?  203 HOH   B O    1 
HETATM 6828 O O    . HOH   F 4 .   ? 41.391 -7.781  5.473   1.00 39.06 ?  204 HOH   B O    1 
HETATM 6829 O O    . HOH   F 4 .   ? 49.332 -22.680 -19.766 1.00 48.77 ?  205 HOH   B O    1 
HETATM 6830 O O    . HOH   F 4 .   ? 41.776 -35.941 -17.345 1.00 29.40 ?  206 HOH   B O    1 
HETATM 6831 O O    . HOH   F 4 .   ? 59.155 -18.710 6.786   1.00 37.64 ?  207 HOH   B O    1 
HETATM 6832 O O    . HOH   F 4 .   ? 27.816 -41.805 -15.172 1.00 38.03 ?  208 HOH   B O    1 
HETATM 6833 O O    . HOH   F 4 .   ? 56.296 -19.708 7.343   1.00 34.20 ?  209 HOH   B O    1 
HETATM 6834 O O    . HOH   F 4 .   ? 55.383 -16.489 -14.396 1.00 36.72 ?  210 HOH   B O    1 
HETATM 6835 O O    . HOH   F 4 .   ? 54.434 -9.361  -8.826  1.00 18.64 ?  211 HOH   B O    1 
HETATM 6836 O O    . HOH   F 4 .   ? 37.872 -39.514 -0.293  1.00 41.53 ?  212 HOH   B O    1 
HETATM 6837 O O    . HOH   F 4 .   ? 58.168 -12.886 8.393   1.00 37.16 ?  213 HOH   B O    1 
HETATM 6838 O O    . HOH   F 4 .   ? 27.761 -29.196 -1.874  1.00 37.11 ?  214 HOH   B O    1 
HETATM 6839 O O    . HOH   F 4 .   ? 50.260 -3.366  7.169   1.00 38.75 ?  215 HOH   B O    1 
HETATM 6840 O O    . HOH   F 4 .   ? 35.922 -43.199 -8.612  1.00 27.99 ?  216 HOH   B O    1 
HETATM 6841 O O    . HOH   F 4 .   ? 29.865 -26.318 3.945   1.00 27.00 ?  217 HOH   B O    1 
HETATM 6842 O O    . HOH   F 4 .   ? 30.214 -41.052 -8.168  1.00 16.18 ?  218 HOH   B O    1 
HETATM 6843 O O    . HOH   F 4 .   ? 50.699 -6.118  0.227   1.00 28.28 ?  219 HOH   B O    1 
HETATM 6844 O O    . HOH   F 4 .   ? 57.136 -26.792 -7.642  1.00 42.84 ?  220 HOH   B O    1 
HETATM 6845 O O    . HOH   F 4 .   ? 37.100 -19.802 -18.067 1.00 36.21 ?  221 HOH   B O    1 
HETATM 6846 O O    . HOH   F 4 .   ? 56.698 -30.722 -7.792  1.00 35.64 ?  222 HOH   B O    1 
HETATM 6847 O O    . HOH   F 4 .   ? 57.702 -24.442 4.992   1.00 32.22 ?  223 HOH   B O    1 
HETATM 6848 O O    . HOH   F 4 .   ? 29.713 -34.198 -0.460  1.00 33.94 ?  224 HOH   B O    1 
HETATM 6849 O O    . HOH   F 4 .   ? 44.419 -7.314  2.169   1.00 31.75 ?  225 HOH   B O    1 
HETATM 6850 O O    . HOH   F 4 .   ? 30.820 -28.776 4.242   1.00 24.27 ?  226 HOH   B O    1 
HETATM 6851 O O    . HOH   F 4 .   ? 52.947 -13.425 -20.394 1.00 37.94 ?  227 HOH   B O    1 
HETATM 6852 O O    . HOH   F 4 .   ? 48.444 -36.516 -15.481 1.00 42.34 ?  228 HOH   B O    1 
HETATM 6853 O O    . HOH   F 4 .   ? 45.165 -34.950 6.866   1.00 40.51 ?  229 HOH   B O    1 
HETATM 6854 O O    . HOH   F 4 .   ? 57.386 -16.203 -12.212 1.00 18.86 ?  230 HOH   B O    1 
HETATM 6855 O O    . HOH   F 4 .   ? 34.529 -36.350 -7.244  1.00 16.70 ?  231 HOH   B O    1 
HETATM 6856 O O    . HOH   F 4 .   ? 39.280 -10.905 6.108   1.00 30.26 ?  232 HOH   B O    1 
HETATM 6857 O O    . HOH   F 4 .   ? 41.307 -9.669  13.068  1.00 21.90 ?  233 HOH   B O    1 
HETATM 6858 O O    . HOH   F 4 .   ? 41.492 -39.151 -14.920 1.00 21.01 ?  234 HOH   B O    1 
HETATM 6859 O O    . HOH   F 4 .   ? 51.660 -6.495  4.426   1.00 19.68 ?  235 HOH   B O    1 
HETATM 6860 O O    . HOH   F 4 .   ? 40.615 -16.041 14.147  1.00 25.10 ?  236 HOH   B O    1 
HETATM 6861 O O    . HOH   F 4 .   ? 35.073 -7.993  -3.068  1.00 18.21 ?  237 HOH   B O    1 
HETATM 6862 O O    . HOH   F 4 .   ? 44.989 -43.516 -10.517 1.00 26.97 ?  238 HOH   B O    1 
HETATM 6863 O O    . HOH   F 4 .   ? 50.691 -12.960 -0.501  1.00 12.33 ?  239 HOH   B O    1 
HETATM 6864 O O    . HOH   F 4 .   ? 39.447 -11.139 0.306   1.00 16.77 ?  240 HOH   B O    1 
HETATM 6865 O O    . HOH   F 4 .   ? 32.856 -43.818 -11.375 1.00 19.09 ?  241 HOH   B O    1 
HETATM 6866 O O    . HOH   F 4 .   ? 28.349 -19.685 -13.121 1.00 22.77 ?  242 HOH   B O    1 
HETATM 6867 O O    . HOH   F 4 .   ? 44.488 -27.782 -0.785  1.00 22.59 ?  243 HOH   B O    1 
HETATM 6868 O O    . HOH   F 4 .   ? 42.615 -22.875 3.804   1.00 11.50 ?  244 HOH   B O    1 
HETATM 6869 O O    . HOH   F 4 .   ? 42.542 -25.379 2.599   1.00 15.11 ?  245 HOH   B O    1 
HETATM 6870 O O    . HOH   F 4 .   ? 51.520 -13.877 10.928  1.00 30.66 ?  246 HOH   B O    1 
HETATM 6871 O O    . HOH   F 4 .   ? 48.070 -24.483 -17.774 1.00 28.39 ?  247 HOH   B O    1 
HETATM 6872 O O    . HOH   F 4 .   ? 41.833 -23.536 9.275   1.00 16.27 ?  248 HOH   B O    1 
HETATM 6873 O O    . HOH   F 4 .   ? 43.088 -43.246 -8.287  1.00 27.66 ?  249 HOH   B O    1 
HETATM 6874 O O    . HOH   F 4 .   ? 34.811 -24.653 13.806  1.00 30.72 ?  250 HOH   B O    1 
HETATM 6875 O O    . HOH   F 4 .   ? 40.281 -12.749 -11.543 1.00 14.45 ?  251 HOH   B O    1 
HETATM 6876 O O    . HOH   F 4 .   ? 46.395 -1.568  13.292  1.00 28.34 ?  252 HOH   B O    1 
HETATM 6877 O O    . HOH   F 4 .   ? 25.437 -26.020 -1.401  1.00 32.20 ?  253 HOH   B O    1 
HETATM 6878 O O    . HOH   F 4 .   ? 57.546 -24.431 -3.882  1.00 21.33 ?  254 HOH   B O    1 
HETATM 6879 O O    . HOH   F 4 .   ? 34.169 -18.571 11.373  1.00 21.91 ?  255 HOH   B O    1 
HETATM 6880 O O    . HOH   F 4 .   ? 43.190 -32.352 -17.120 1.00 21.58 ?  256 HOH   B O    1 
HETATM 6881 O O    . HOH   F 4 .   ? 29.694 -25.240 -10.892 1.00 15.60 ?  257 HOH   B O    1 
HETATM 6882 O O    . HOH   F 4 .   ? 30.838 -15.745 2.595   1.00 13.23 ?  258 HOH   B O    1 
HETATM 6883 O O    . HOH   F 4 .   ? 30.627 -42.251 -10.638 1.00 29.20 ?  259 HOH   B O    1 
HETATM 6884 O O    . HOH   F 4 .   ? 57.456 -9.254  1.421   1.00 19.25 ?  260 HOH   B O    1 
HETATM 6885 O O    . HOH   F 4 .   ? 38.874 -12.034 12.302  1.00 31.99 ?  261 HOH   B O    1 
HETATM 6886 O O    . HOH   F 4 .   ? 58.115 -10.610 -4.115  1.00 20.62 ?  262 HOH   B O    1 
HETATM 6887 O O    . HOH   F 4 .   ? 43.319 -15.780 -12.182 1.00 13.81 ?  263 HOH   B O    1 
HETATM 6888 O O    . HOH   F 4 .   ? 50.970 -39.958 -8.276  1.00 30.49 ?  264 HOH   B O    1 
HETATM 6889 O O    . HOH   F 4 .   ? 47.971 -22.774 5.808   1.00 16.84 ?  265 HOH   B O    1 
HETATM 6890 O O    . HOH   F 4 .   ? 28.261 -34.356 -9.512  1.00 19.61 ?  266 HOH   B O    1 
HETATM 6891 O O    . HOH   F 4 .   ? 49.315 -28.687 -6.930  1.00 15.29 ?  267 HOH   B O    1 
HETATM 6892 O O    . HOH   F 4 .   ? 38.425 -11.040 -2.266  1.00 18.51 ?  268 HOH   B O    1 
HETATM 6893 O O    . HOH   F 4 .   ? 49.778 -0.525  10.286  1.00 30.14 ?  269 HOH   B O    1 
HETATM 6894 O O    . HOH   F 4 .   ? 27.138 -31.842 -10.048 1.00 19.49 ?  270 HOH   B O    1 
HETATM 6895 O O    . HOH   F 4 .   ? 56.159 -23.435 -14.744 1.00 25.47 ?  271 HOH   B O    1 
HETATM 6896 O O    . HOH   F 4 .   ? 31.800 -17.953 -14.593 1.00 32.20 ?  272 HOH   B O    1 
HETATM 6897 O O    . HOH   F 4 .   ? 34.425 -12.790 2.562   1.00 26.31 ?  273 HOH   B O    1 
HETATM 6898 O O    . HOH   F 4 .   ? 59.746 -15.405 8.108   1.00 34.19 ?  274 HOH   B O    1 
HETATM 6899 O O    . HOH   F 4 .   ? 46.619 -31.250 -4.808  1.00 20.29 ?  275 HOH   B O    1 
HETATM 6900 O O    . HOH   F 4 .   ? 41.169 -5.541  11.508  1.00 48.99 ?  276 HOH   B O    1 
HETATM 6901 O O    . HOH   F 4 .   ? 56.895 -8.669  8.455   1.00 19.87 ?  277 HOH   B O    1 
HETATM 6902 O O    . HOH   F 4 .   ? 27.934 -22.907 -8.058  1.00 16.83 ?  278 HOH   B O    1 
HETATM 6903 O O    . HOH   F 4 .   ? 57.069 -12.127 12.351  1.00 39.35 ?  279 HOH   B O    1 
HETATM 6904 O O    . HOH   F 4 .   ? 34.903 -33.399 -19.248 1.00 28.64 ?  280 HOH   B O    1 
HETATM 6905 O O    . HOH   F 4 .   ? 28.450 -30.851 -14.776 1.00 29.00 ?  281 HOH   B O    1 
HETATM 6906 O O    . HOH   F 4 .   ? 42.858 -20.337 -20.817 1.00 35.99 ?  282 HOH   B O    1 
HETATM 6907 O O    . HOH   F 4 .   ? 42.186 -10.071 -14.972 1.00 35.35 ?  283 HOH   B O    1 
HETATM 6908 O O    . HOH   F 4 .   ? 37.312 -35.646 7.125   1.00 33.11 ?  284 HOH   B O    1 
HETATM 6909 O O    . HOH   F 4 .   ? 46.863 -29.567 9.799   1.00 31.57 ?  285 HOH   B O    1 
HETATM 6910 O O    . HOH   F 4 .   ? 42.374 -34.691 3.738   1.00 25.79 ?  286 HOH   B O    1 
HETATM 6911 O O    . HOH   F 4 .   ? 42.630 -12.332 -18.530 1.00 30.65 ?  287 HOH   B O    1 
HETATM 6912 O O    . HOH   F 4 .   ? 48.390 -25.061 3.079   1.00 12.65 ?  288 HOH   B O    1 
HETATM 6913 O O    . HOH   F 4 .   ? 42.254 -9.866  9.367   1.00 21.00 ?  289 HOH   B O    1 
HETATM 6914 O O    . HOH   F 4 .   ? 33.477 -15.305 -13.986 1.00 20.36 ?  290 HOH   B O    1 
HETATM 6915 O O    . HOH   F 4 .   ? 49.964 -24.629 5.769   1.00 32.92 ?  291 HOH   B O    1 
HETATM 6916 O O    . HOH   F 4 .   ? 51.238 -37.606 -9.576  1.00 24.63 ?  292 HOH   B O    1 
HETATM 6917 O O    . HOH   F 4 .   ? 48.680 -20.050 5.901   1.00 13.74 ?  293 HOH   B O    1 
HETATM 6918 O O    . HOH   F 4 .   ? 44.595 -27.462 1.934   1.00 15.03 ?  294 HOH   B O    1 
HETATM 6919 O O    . HOH   F 4 .   ? 52.515 -10.461 12.995  1.00 22.68 ?  295 HOH   B O    1 
HETATM 6920 O O    . HOH   F 4 .   ? 45.353 -33.392 -15.960 1.00 22.79 ?  296 HOH   B O    1 
HETATM 6921 O O    . HOH   F 4 .   ? 52.591 -35.662 -8.548  1.00 26.59 ?  297 HOH   B O    1 
HETATM 6922 O O    . HOH   F 4 .   ? 36.773 -12.757 -1.522  1.00 25.93 ?  298 HOH   B O    1 
HETATM 6923 O O    . HOH   F 4 .   ? 40.188 -10.813 -9.574  1.00 16.43 ?  299 HOH   B O    1 
HETATM 6924 O O    . HOH   F 4 .   ? 43.522 -15.404 18.243  1.00 30.70 ?  300 HOH   B O    1 
HETATM 6925 O O    . HOH   F 4 .   ? 27.537 -26.732 -15.677 1.00 31.52 ?  301 HOH   B O    1 
HETATM 6926 O O    . HOH   F 4 .   ? 44.018 -29.354 -4.733  1.00 22.77 ?  302 HOH   B O    1 
HETATM 6927 O O    . HOH   F 4 .   ? 47.061 -33.967 -4.624  1.00 16.35 ?  303 HOH   B O    1 
HETATM 6928 O O    . HOH   F 4 .   ? 45.917 -40.393 -3.632  1.00 29.05 ?  304 HOH   B O    1 
HETATM 6929 O O    . HOH   F 4 .   ? 35.017 -33.569 4.456   1.00 24.67 ?  305 HOH   B O    1 
HETATM 6930 O O    . HOH   F 4 .   ? 57.685 -22.121 3.050   1.00 24.98 ?  306 HOH   B O    1 
HETATM 6931 O O    . HOH   F 4 .   ? 53.100 -16.044 -12.774 1.00 28.36 ?  307 HOH   B O    1 
HETATM 6932 O O    . HOH   F 4 .   ? 48.135 -32.644 -16.596 1.00 43.09 ?  308 HOH   B O    1 
HETATM 6933 O O    . HOH   F 4 .   ? 41.661 -8.117  1.317   1.00 24.60 ?  309 HOH   B O    1 
HETATM 6934 O O    . HOH   F 4 .   ? 52.553 -29.221 -13.024 1.00 23.15 ?  310 HOH   B O    1 
HETATM 6935 O O    . HOH   F 4 .   ? 53.463 -30.195 4.496   1.00 18.22 ?  311 HOH   B O    1 
HETATM 6936 O O    . HOH   F 4 .   ? 25.916 -21.476 -3.560  1.00 15.71 ?  312 HOH   B O    1 
HETATM 6937 O O    . HOH   F 4 .   ? 32.797 -34.574 -5.972  1.00 15.79 ?  313 HOH   B O    1 
HETATM 6938 O O    . HOH   F 4 .   ? 37.491 -18.266 13.110  1.00 27.33 ?  314 HOH   B O    1 
HETATM 6939 O O    . HOH   F 4 .   ? 37.800 -10.250 -10.788 1.00 16.52 ?  315 HOH   B O    1 
HETATM 6940 O O    . HOH   F 4 .   ? 41.166 -24.520 15.776  1.00 41.93 ?  316 HOH   B O    1 
HETATM 6941 O O    . HOH   F 4 .   ? 62.812 -20.123 -0.858  1.00 38.03 ?  317 HOH   B O    1 
HETATM 6942 O O    . HOH   F 4 .   ? 62.655 -13.596 4.652   1.00 27.53 ?  318 HOH   B O    1 
HETATM 6943 O O    . HOH   F 4 .   ? 59.917 -17.172 -10.492 1.00 34.89 ?  319 HOH   B O    1 
HETATM 6944 O O    . HOH   F 4 .   ? 26.311 -21.015 -6.285  1.00 16.05 ?  320 HOH   B O    1 
HETATM 6945 O O    . HOH   F 4 .   ? 43.159 -21.467 10.630  1.00 15.60 ?  321 HOH   B O    1 
HETATM 6946 O O    . HOH   F 4 .   ? 38.326 -12.830 7.889   1.00 18.71 ?  322 HOH   B O    1 
HETATM 6947 O O    . HOH   F 4 .   ? 37.224 -30.597 -21.086 1.00 31.28 ?  323 HOH   B O    1 
HETATM 6948 O O    . HOH   F 4 .   ? 44.553 -24.648 9.556   1.00 18.86 ?  324 HOH   B O    1 
HETATM 6949 O O    . HOH   F 4 .   ? 27.919 -14.782 -9.423  1.00 32.32 ?  325 HOH   B O    1 
HETATM 6950 O O    . HOH   F 4 .   ? 44.208 -1.789  7.568   1.00 44.83 ?  326 HOH   B O    1 
HETATM 6951 O O    . HOH   F 4 .   ? 36.678 -12.443 4.245   1.00 18.31 ?  327 HOH   B O    1 
HETATM 6952 O O    . HOH   F 4 .   ? 51.402 -32.895 -10.804 1.00 36.94 ?  328 HOH   B O    1 
HETATM 6953 O O    . HOH   F 4 .   ? 51.712 -5.904  -7.897  1.00 49.70 ?  329 HOH   B O    1 
HETATM 6954 O O    . HOH   F 4 .   ? 33.582 -31.188 11.015  1.00 33.25 ?  330 HOH   B O    1 
HETATM 6955 O O    . HOH   F 4 .   ? 47.126 -24.503 8.123   1.00 24.89 ?  331 HOH   B O    1 
HETATM 6956 O O    . HOH   F 4 .   ? 43.101 -34.649 0.073   1.00 19.99 ?  332 HOH   B O    1 
HETATM 6957 O O    . HOH   F 4 .   ? 39.438 -23.518 -20.326 1.00 35.15 ?  333 HOH   B O    1 
HETATM 6958 O O    . HOH   F 4 .   ? 38.333 -9.342  -13.286 1.00 27.33 ?  334 HOH   B O    1 
HETATM 6959 O O    . HOH   F 4 .   ? 53.633 -12.534 -22.330 1.00 36.89 ?  335 HOH   B O    1 
HETATM 6960 O O    . HOH   F 4 .   ? 47.453 -27.444 1.975   1.00 14.52 ?  336 HOH   B O    1 
HETATM 6961 O O    . HOH   F 4 .   ? 48.554 -11.861 -13.863 1.00 26.80 ?  337 HOH   B O    1 
HETATM 6962 O O    . HOH   F 4 .   ? 45.755 -36.248 -16.204 1.00 34.18 ?  338 HOH   B O    1 
HETATM 6963 O O    . HOH   F 4 .   ? 42.898 -43.503 -14.411 1.00 42.99 ?  339 HOH   B O    1 
HETATM 6964 O O    . HOH   F 4 .   ? 46.819 -19.903 12.271  1.00 28.91 ?  340 HOH   B O    1 
HETATM 6965 O O    . HOH   F 4 .   ? 36.959 -15.067 -16.533 1.00 36.72 ?  341 HOH   B O    1 
HETATM 6966 O O    . HOH   F 4 .   ? 28.854 -42.952 -12.440 1.00 42.83 ?  342 HOH   B O    1 
HETATM 6967 O O    . HOH   F 4 .   ? 37.101 -45.280 -9.837  1.00 35.92 ?  343 HOH   B O    1 
HETATM 6968 O O    . HOH   F 4 .   ? 32.946 -14.689 1.004   1.00 18.50 ?  344 HOH   B O    1 
HETATM 6969 O O    . HOH   F 4 .   ? 39.791 -44.324 -11.230 1.00 36.46 ?  345 HOH   B O    1 
HETATM 6970 O O    . HOH   F 4 .   ? 33.714 -9.355  -8.817  1.00 32.37 ?  346 HOH   B O    1 
HETATM 6971 O O    . HOH   F 4 .   ? 38.570 -22.332 15.048  1.00 39.24 ?  347 HOH   B O    1 
HETATM 6972 O O    . HOH   F 4 .   ? 40.413 -43.481 -9.143  1.00 26.81 ?  348 HOH   B O    1 
HETATM 6973 O O    . HOH   F 4 .   ? 38.427 -12.314 -16.253 1.00 41.01 ?  349 HOH   B O    1 
HETATM 6974 O O    . HOH   F 4 .   ? 62.461 -20.123 -4.897  1.00 42.17 ?  350 HOH   B O    1 
HETATM 6975 O O    . HOH   F 4 .   ? 27.736 -26.635 -0.638  1.00 31.99 ?  351 HOH   B O    1 
HETATM 6976 O O    . HOH   F 4 .   ? 35.959 -8.656  -9.699  1.00 35.41 ?  352 HOH   B O    1 
HETATM 6977 O O    . HOH   F 4 .   ? 55.612 -8.284  10.866  1.00 25.03 ?  353 HOH   B O    1 
HETATM 6978 O O    . HOH   F 4 .   ? 44.128 -37.296 -17.807 1.00 31.96 ?  354 HOH   B O    1 
HETATM 6979 O O    . HOH   F 4 .   ? 56.538 -7.317  3.110   1.00 27.26 ?  355 HOH   B O    1 
HETATM 6980 O O    . HOH   F 4 .   ? 23.161 -23.662 6.761   1.00 34.66 ?  356 HOH   B O    1 
HETATM 6981 O O    . HOH   F 4 .   ? 34.670 -10.303 7.417   1.00 24.37 ?  357 HOH   B O    1 
HETATM 6982 O O    . HOH   F 4 .   ? 61.436 -19.862 1.613   1.00 31.93 ?  358 HOH   B O    1 
HETATM 6983 O O    . HOH   F 4 .   ? 43.087 -12.628 -21.205 1.00 41.64 ?  359 HOH   B O    1 
HETATM 6984 O O    . HOH   F 4 .   ? 56.912 -21.503 -16.466 1.00 41.18 ?  360 HOH   B O    1 
HETATM 6985 O O    . HOH   F 4 .   ? 34.204 -7.670  11.427  1.00 41.52 ?  361 HOH   B O    1 
HETATM 6986 O O    . HOH   F 4 .   ? 40.164 -8.856  9.960   1.00 38.98 ?  362 HOH   B O    1 
HETATM 6987 O O    . HOH   F 4 .   ? 27.101 -25.997 -11.524 1.00 31.60 ?  363 HOH   B O    1 
HETATM 6988 O O    . HOH   F 4 .   ? 32.425 -23.643 14.071  1.00 40.68 ?  364 HOH   B O    1 
HETATM 6989 O O    . HOH   F 4 .   ? 58.863 -10.467 9.193   1.00 41.06 ?  365 HOH   B O    1 
HETATM 6990 O O    . HOH   F 4 .   ? 36.134 -8.703  8.961   1.00 40.52 ?  366 HOH   B O    1 
HETATM 6991 O O    . HOH   F 4 .   ? 39.838 -7.098  7.840   1.00 46.63 ?  367 HOH   B O    1 
HETATM 6992 O O    . HOH   F 4 .   ? 54.191 -5.802  2.949   1.00 37.67 ?  368 HOH   B O    1 
HETATM 6993 O O    . HOH   F 4 .   ? 56.012 -7.819  -0.580  1.00 39.55 ?  369 HOH   B O    1 
HETATM 6994 O O    . HOH   F 4 .   ? 39.961 -11.410 -13.997 1.00 31.17 ?  370 HOH   B O    1 
HETATM 6995 O O    . HOH   F 4 .   ? 48.402 -26.504 8.776   1.00 36.75 ?  371 HOH   B O    1 
HETATM 6996 O O    . HOH   F 4 .   ? 41.801 -9.956  -17.422 1.00 54.37 ?  372 HOH   B O    1 
HETATM 6997 O O    . HOH   F 4 .   ? 52.036 -12.954 13.312  1.00 32.54 ?  373 HOH   B O    1 
HETATM 6998 O O    . HOH   F 4 .   ? 38.024 -10.649 10.072  1.00 29.27 ?  374 HOH   B O    1 
HETATM 6999 O O    . HOH   F 4 .   ? 62.985 -12.404 6.903   1.00 37.20 ?  375 HOH   B O    1 
HETATM 7000 O O    . HOH   F 4 .   ? 44.086 -5.650  -3.506  1.00 42.62 ?  376 HOH   B O    1 
HETATM 7001 O O    . HOH   F 4 .   ? 36.510 -22.811 13.327  1.00 23.77 ?  377 HOH   B O    1 
HETATM 7002 O O    . HOH   F 4 .   ? 41.798 -6.840  -4.817  1.00 47.71 ?  378 HOH   B O    1 
HETATM 7003 O O    . HOH   F 4 .   ? 40.106 -7.723  3.226   1.00 36.83 ?  379 HOH   B O    1 
HETATM 7004 O O    . HOH   F 4 .   ? 52.808 -29.879 7.119   1.00 23.17 ?  380 HOH   B O    1 
HETATM 7005 O O    . HOH   F 4 .   ? 42.609 -17.052 -23.280 1.00 42.14 ?  381 HOH   B O    1 
HETATM 7006 O O    . HOH   F 4 .   ? 39.805 -14.073 15.741  1.00 49.21 ?  382 HOH   B O    1 
HETATM 7007 O O    . HOH   F 4 .   ? 60.451 -22.269 2.757   1.00 46.86 ?  383 HOH   B O    1 
HETATM 7008 O O    . HOH   F 4 .   ? 40.955 -9.817  15.765  1.00 47.00 ?  384 HOH   B O    1 
HETATM 7009 O O    . HOH   F 4 .   ? 35.320 -20.312 13.281  1.00 28.02 ?  385 HOH   B O    1 
HETATM 7010 O O    . HOH   F 4 .   ? 23.896 -20.825 -7.707  1.00 27.12 ?  386 HOH   B O    1 
HETATM 7011 O O    . HOH   F 4 .   ? 46.724 -5.330  2.923   1.00 41.45 ?  387 HOH   B O    1 
HETATM 7012 O O    . HOH   F 4 .   ? 25.745 -18.855 -11.975 1.00 35.63 ?  388 HOH   B O    1 
HETATM 7013 O O    . HOH   F 4 .   ? 35.305 -33.721 7.225   1.00 39.02 ?  389 HOH   B O    1 
HETATM 7014 O O    . HOH   F 4 .   ? 40.713 -6.616  -0.913  1.00 23.99 ?  390 HOH   B O    1 
HETATM 7015 O O    . HOH   F 4 .   ? 44.068 -31.706 -3.845  1.00 30.38 ?  391 HOH   B O    1 
HETATM 7016 O O    . HOH   F 4 .   ? 27.913 -27.094 2.204   1.00 30.63 ?  392 HOH   B O    1 
HETATM 7017 O O    . HOH   F 4 .   ? 26.623 -27.989 -13.582 1.00 37.89 ?  393 HOH   B O    1 
HETATM 7018 O O    . HOH   F 4 .   ? 24.576 -20.610 -10.483 1.00 37.16 ?  394 HOH   B O    1 
HETATM 7019 O O    . HOH   F 4 .   ? 34.367 -33.431 9.549   1.00 32.82 ?  395 HOH   B O    1 
HETATM 7020 O O    . HOH   F 4 .   ? 50.602 -30.840 8.679   1.00 28.10 ?  396 HOH   B O    1 
HETATM 7021 O O    . HOH   F 4 .   ? 45.738 -20.317 15.148  1.00 49.61 ?  397 HOH   B O    1 
HETATM 7022 O O    . HOH   F 4 .   ? 26.843 -30.710 -12.673 1.00 27.23 ?  398 HOH   B O    1 
HETATM 7023 O O    . HOH   F 4 .   ? 57.739 -6.534  -2.371  1.00 36.34 ?  399 HOH   B O    1 
HETATM 7024 O O    . HOH   F 4 .   ? 40.891 -11.864 -22.370 1.00 42.32 ?  400 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   A VAL   A 3   ? 0.5625 0.5552 0.6401 0.0130  -0.0529 0.0990  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.5369 0.5352 0.5922 -0.0042 -0.0158 0.0296  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.5604 0.5537 0.6238 0.0103  -0.0502 0.0984  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.5351 0.5338 0.5834 -0.0054 -0.0151 0.0298  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.5471 0.5428 0.5856 0.0011  -0.0515 0.1054  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.5253 0.5269 0.5534 -0.0105 -0.0161 0.0329  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.5487 0.5440 0.5976 0.0036  -0.0545 0.1085  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.5269 0.5280 0.5614 -0.0095 -0.0168 0.0334  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.5690 0.5612 0.6338 0.0152  -0.0455 0.0912  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.5410 0.5380 0.5978 -0.0023 -0.0135 0.0273  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.5722 0.5638 0.6347 0.0174  -0.0442 0.0886  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.5431 0.5394 0.6010 -0.0011 -0.0131 0.0262  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.5713 0.5636 0.6337 0.0165  -0.0440 0.0898  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.5428 0.5394 0.6007 -0.0013 -0.0130 0.0268  3   VAL   A CG2 
31   N N   A ASN   A 4   ? 0.5295 0.5288 0.5234 -0.0102 -0.0489 0.1081  4   ASN   A N   
32   N N   B ASN   A 4   ? 0.5120 0.5178 0.5098 -0.0167 -0.0163 0.0358  4   ASN   A N   
33   C CA  A ASN   A 4   ? 0.5101 0.5132 0.4547 -0.0222 -0.0434 0.1073  4   ASN   A CA  
34   C CA  B ASN   A 4   ? 0.4972 0.5073 0.4623 -0.0230 -0.0163 0.0384  4   ASN   A CA  
35   C C   A ASN   A 4   ? 0.4823 0.4963 0.4169 -0.0301 -0.0300 0.0780  4   ASN   A C   
36   C C   B ASN   A 4   ? 0.4760 0.4939 0.4290 -0.0302 -0.0147 0.0405  4   ASN   A C   
37   O O   A ASN   A 4   ? 0.4827 0.4961 0.4003 -0.0320 -0.0322 0.0848  4   ASN   A O   
38   O O   B ASN   A 4   ? 0.4771 0.4961 0.4272 -0.0312 -0.0140 0.0403  4   ASN   A O   
39   C CB  A ASN   A 4   ? 0.5158 0.5127 0.4212 -0.0262 -0.0499 0.1324  4   ASN   A CB  
40   C CB  B ASN   A 4   ? 0.5016 0.5080 0.4450 -0.0223 -0.0177 0.0390  4   ASN   A CB  
41   C CG  A ASN   A 4   ? 0.5190 0.5097 0.3864 -0.0302 -0.0556 0.1573  4   ASN   A CG  
42   C CG  B ASN   A 4   ? 0.5046 0.5076 0.4290 -0.0219 -0.0192 0.0403  4   ASN   A CG  
43   O OD1 A ASN   A 4   ? 0.5219 0.5077 0.3729 -0.0320 -0.0571 0.1672  4   ASN   A OD1 
44   O OD1 B ASN   A 4   ? 0.5062 0.5076 0.4241 -0.0217 -0.0199 0.0409  4   ASN   A OD1 
45   N ND2 A ASN   A 4   ? 0.5183 0.5077 0.3773 -0.0303 -0.0589 0.1687  4   ASN   A ND2 
46   N ND2 B ASN   A 4   ? 0.5051 0.5071 0.4246 -0.0216 -0.0196 0.0412  4   ASN   A ND2 
59   N N   . SER   A 5   ? 0.4515 0.4746 0.3927 -0.0372 -0.0143 0.0448  5   SER   A N   
60   C CA  . SER   A 5   ? 0.3955 0.4387 0.3440 -0.0504 0.0020  0.0110  5   SER   A CA  
61   C C   . SER   A 5   ? 0.3396 0.3814 0.2817 -0.0503 0.0148  -0.0116 5   SER   A C   
62   O O   . SER   A 5   ? 0.3448 0.3907 0.2815 -0.0365 0.0167  -0.0295 5   SER   A O   
63   C CB  . SER   A 5   ? 0.3981 0.4631 0.3664 -0.0601 0.0065  0.0018  5   SER   A CB  
64   O OG  . SER   A 5   ? 0.4011 0.4668 0.3726 -0.0639 0.0145  -0.0015 5   SER   A OG  
71   N N   A PHE   A 6   ? 0.2951 0.3416 0.2301 -0.0641 0.0337  -0.0085 6   PHE   A N   
72   N N   B PHE   A 6   ? 0.3197 0.3568 0.2756 -0.0463 0.0116  -0.0105 6   PHE   A N   
73   C CA  A PHE   A 6   ? 0.2580 0.3030 0.1972 -0.0719 0.0466  0.0069  6   PHE   A CA  
74   C CA  B PHE   A 6   ? 0.2996 0.3309 0.2680 -0.0414 0.0073  -0.0054 6   PHE   A CA  
75   C C   A PHE   A 6   ? 0.2562 0.3018 0.2171 -0.0834 0.0647  0.0088  6   PHE   A C   
76   C C   B PHE   A 6   ? 0.2917 0.3180 0.2850 -0.0415 0.0108  -0.0048 6   PHE   A C   
77   O O   A PHE   A 6   ? 0.2593 0.3062 0.2491 -0.0877 0.0596  0.0274  6   PHE   A O   
78   O O   B PHE   A 6   ? 0.2917 0.3198 0.2985 -0.0410 0.0107  -0.0052 6   PHE   A O   
79   C CB  A PHE   A 6   ? 0.2306 0.2686 0.1798 -0.0604 0.0406  0.0155  6   PHE   A CB  
80   C CB  B PHE   A 6   ? 0.2880 0.3163 0.2449 -0.0369 0.0039  0.0001  6   PHE   A CB  
81   C CG  A PHE   A 6   ? 0.2110 0.2431 0.1691 -0.0496 0.0278  0.0191  6   PHE   A CG  
82   C CG  B PHE   A 6   ? 0.2785 0.3035 0.2228 -0.0337 0.0003  0.0066  6   PHE   A CG  
83   C CD1 A PHE   A 6   ? 0.2058 0.2358 0.1748 -0.0430 0.0221  0.0286  6   PHE   A CD1 
84   C CD1 B PHE   A 6   ? 0.2741 0.2988 0.2150 -0.0313 -0.0002 0.0102  6   PHE   A CD1 
85   C CD2 A PHE   A 6   ? 0.2115 0.2343 0.1987 -0.0338 0.0248  0.0147  6   PHE   A CD2 
86   C CD2 B PHE   A 6   ? 0.2756 0.2983 0.2169 -0.0317 -0.0020 0.0102  6   PHE   A CD2 
87   C CE1 A PHE   A 6   ? 0.2045 0.2289 0.1838 -0.0408 0.0205  0.0254  6   PHE   A CE1 
88   C CE1 B PHE   A 6   ? 0.2715 0.2954 0.2111 -0.0301 -0.0016 0.0123  6   PHE   A CE1 
89   C CE2 A PHE   A 6   ? 0.2106 0.2301 0.2100 -0.0316 0.0222  0.0091  6   PHE   A CE2 
90   C CE2 B PHE   A 6   ? 0.2727 0.2953 0.2111 -0.0302 -0.0028 0.0120  6   PHE   A CE2 
91   C CZ  A PHE   A 6   ? 0.2080 0.2291 0.2028 -0.0360 0.0189  0.0128  6   PHE   A CZ  
92   C CZ  B PHE   A 6   ? 0.2714 0.2944 0.2101 -0.0294 -0.0037 0.0123  6   PHE   A CZ  
111  N N   A SER   A 7   ? 0.2507 0.2938 0.2173 -0.0870 0.0795  -0.0041 7   SER   A N   
112  N N   B SER   A 7   ? 0.2835 0.3033 0.2855 -0.0420 0.0145  -0.0022 7   SER   A N   
113  C CA  A SER   A 7   ? 0.2549 0.2908 0.2432 -0.0827 0.0826  -0.0267 7   SER   A CA  
114  C CA  B SER   A 7   ? 0.2750 0.2892 0.2857 -0.0424 0.0155  0.0010  7   SER   A CA  
115  C C   A SER   A 7   ? 0.2416 0.2620 0.2379 -0.0871 0.0931  -0.0266 7   SER   A C   
116  C C   B SER   A 7   ? 0.2664 0.2768 0.2709 -0.0399 0.0191  0.0079  7   SER   A C   
117  O O   A SER   A 7   ? 0.2476 0.2522 0.2424 -0.0929 0.0987  -0.0181 7   SER   A O   
118  O O   B SER   A 7   ? 0.2676 0.2765 0.2684 -0.0391 0.0213  0.0087  7   SER   A O   
119  C CB  A SER   A 7   ? 0.2736 0.3174 0.2781 -0.0709 0.0816  -0.0308 7   SER   A CB  
120  C CB  B SER   A 7   ? 0.2759 0.2866 0.3003 -0.0450 0.0120  -0.0032 7   SER   A CB  
121  O OG  A SER   A 7   ? 0.2899 0.3337 0.3125 -0.0593 0.0798  -0.0353 7   SER   A OG  
122  O OG  B SER   A 7   ? 0.2775 0.2856 0.3090 -0.0489 0.0078  -0.0048 7   SER   A OG  
133  N N   A GLY   A 8   ? 0.2300 0.2498 0.2333 -0.0821 0.0903  -0.0377 8   GLY   A N   
134  N N   B GLY   A 8   ? 0.2586 0.2653 0.2579 -0.0375 0.0201  0.0127  8   GLY   A N   
135  C CA  A GLY   A 8   ? 0.2223 0.2378 0.2389 -0.0647 0.0801  -0.0295 8   GLY   A CA  
136  C CA  B GLY   A 8   ? 0.2536 0.2548 0.2499 -0.0305 0.0239  0.0210  8   GLY   A CA  
137  C C   A GLY   A 8   ? 0.2063 0.2261 0.2269 -0.0534 0.0659  -0.0192 8   GLY   A C   
138  C C   B GLY   A 8   ? 0.2472 0.2435 0.2365 -0.0255 0.0279  0.0285  8   GLY   A C   
139  O O   A GLY   A 8   ? 0.1973 0.2347 0.2579 -0.0468 0.0593  -0.0377 8   GLY   A O   
140  O O   B GLY   A 8   ? 0.2446 0.2428 0.2353 -0.0255 0.0295  0.0303  8   GLY   A O   
147  N N   A TYR   A 9   ? 0.1976 0.2024 0.2048 -0.0416 0.0523  0.0037  9   TYR   A N   
148  N N   B TYR   A 9   ? 0.2456 0.2340 0.2322 -0.0193 0.0261  0.0298  9   TYR   A N   
149  C CA  A TYR   A 9   ? 0.1884 0.1750 0.1845 -0.0330 0.0398  0.0161  9   TYR   A CA  
150  C CA  B TYR   A 9   ? 0.2447 0.2245 0.2251 -0.0154 0.0256  0.0252  9   TYR   A CA  
151  C C   A TYR   A 9   ? 0.1959 0.1643 0.1950 -0.0352 0.0397  0.0311  9   TYR   A C   
152  C C   B TYR   A 9   ? 0.2481 0.2203 0.2329 -0.0120 0.0287  0.0129  9   TYR   A C   
153  O O   A TYR   A 9   ? 0.2159 0.1862 0.1910 -0.0475 0.0567  0.0256  9   TYR   A O   
154  O O   B TYR   A 9   ? 0.2502 0.2281 0.2430 -0.0137 0.0336  0.0049  9   TYR   A O   
155  C CB  A TYR   A 9   ? 0.1747 0.1773 0.1904 -0.0195 0.0372  0.0201  9   TYR   A CB  
156  C CB  B TYR   A 9   ? 0.2405 0.2209 0.2079 -0.0122 0.0243  0.0338  9   TYR   A CB  
157  C CG  A TYR   A 9   ? 0.1624 0.1727 0.1839 -0.0064 0.0374  0.0182  9   TYR   A CG  
158  C CG  B TYR   A 9   ? 0.2359 0.2171 0.2029 -0.0082 0.0219  0.0358  9   TYR   A CG  
159  C CD1 A TYR   A 9   ? 0.1598 0.1764 0.1867 -0.0078 0.0376  0.0164  9   TYR   A CD1 
160  C CD1 B TYR   A 9   ? 0.2341 0.2153 0.2034 -0.0057 0.0240  0.0360  9   TYR   A CD1 
161  C CD2 A TYR   A 9   ? 0.1603 0.1652 0.1789 -0.0022 0.0259  0.0259  9   TYR   A CD2 
162  C CD2 B TYR   A 9   ? 0.2329 0.2149 0.1975 -0.0062 0.0206  0.0374  9   TYR   A CD2 
163  C CE1 A TYR   A 9   ? 0.1594 0.1800 0.1901 -0.0102 0.0322  0.0047  9   TYR   A CE1 
164  C CE1 B TYR   A 9   ? 0.2312 0.2116 0.2034 -0.0042 0.0271  0.0363  9   TYR   A CE1 
165  C CE2 A TYR   A 9   ? 0.1541 0.1721 0.1766 -0.0048 0.0299  0.0177  9   TYR   A CE2 
166  C CE2 B TYR   A 9   ? 0.2293 0.2111 0.1950 -0.0050 0.0241  0.0407  9   TYR   A CE2 
167  C CZ  A TYR   A 9   ? 0.1582 0.1805 0.1981 -0.0181 0.0342  0.0116  9   TYR   A CZ  
168  C CZ  B TYR   A 9   ? 0.2277 0.2096 0.2017 -0.0022 0.0300  0.0370  9   TYR   A CZ  
169  O OH  A TYR   A 9   ? 0.1662 0.1930 0.2259 -0.0306 0.0393  -0.0023 9   TYR   A OH  
170  O OH  B TYR   A 9   ? 0.2252 0.2081 0.2136 0.0004  0.0339  0.0337  9   TYR   A OH  
189  N N   A LEU   A 10  ? 0.1751 0.1553 0.1995 -0.0257 0.0304  0.0379  10  LEU   A N   
190  N N   B LEU   A 10  ? 0.2494 0.2098 0.2349 -0.0066 0.0287  0.0066  10  LEU   A N   
191  C CA  A LEU   A 10  ? 0.1548 0.1605 0.2064 -0.0271 0.0231  0.0468  10  LEU   A CA  
192  C CA  B LEU   A 10  ? 0.2481 0.1996 0.2298 -0.0035 0.0304  0.0046  10  LEU   A CA  
193  C C   A LEU   A 10  ? 0.1339 0.1549 0.1841 -0.0237 0.0140  0.0427  10  LEU   A C   
194  C C   B LEU   A 10  ? 0.2433 0.1866 0.2202 -0.0014 0.0333  0.0140  10  LEU   A C   
195  O O   A LEU   A 10  ? 0.1395 0.1454 0.1980 -0.0187 0.0230  0.0441  10  LEU   A O   
196  O O   B LEU   A 10  ? 0.2436 0.1807 0.2166 -0.0074 0.0319  0.0203  10  LEU   A O   
197  C CB  A LEU   A 10  ? 0.1525 0.1627 0.2616 -0.0318 -0.0025 0.0624  10  LEU   A CB  
198  C CB  B LEU   A 10  ? 0.2533 0.2023 0.2463 -0.0040 0.0252  -0.0058 10  LEU   A CB  
199  C CG  A LEU   A 10  ? 0.1789 0.1885 0.3176 -0.0285 -0.0389 0.0740  10  LEU   A CG  
200  C CG  B LEU   A 10  ? 0.2558 0.2034 0.2640 -0.0076 0.0162  -0.0111 10  LEU   A CG  
201  C CD1 A LEU   A 10  ? 0.1989 0.2060 0.3580 -0.0322 -0.0339 0.0701  10  LEU   A CD1 
202  C CD1 B LEU   A 10  ? 0.2568 0.2052 0.2680 -0.0074 0.0146  -0.0119 10  LEU   A CD1 
203  C CD2 A LEU   A 10  ? 0.2018 0.2133 0.3414 -0.0152 -0.0333 0.0573  10  LEU   A CD2 
204  C CD2 B LEU   A 10  ? 0.2572 0.2046 0.2761 -0.0111 0.0141  -0.0133 10  LEU   A CD2 
227  N N   A LYS   A 11  ? 0.1409 0.1645 0.1770 -0.0217 0.0181  0.0417  11  LYS   A N   
228  N N   B LYS   A 11  ? 0.2364 0.1821 0.2175 0.0024  0.0389  0.0183  11  LYS   A N   
229  C CA  A LYS   A 11  ? 0.1400 0.1584 0.1697 -0.0296 0.0184  0.0417  11  LYS   A CA  
230  C CA  B LYS   A 11  ? 0.2256 0.1778 0.2082 0.0017  0.0447  0.0234  11  LYS   A CA  
231  C C   A LYS   A 11  ? 0.1318 0.1556 0.1698 -0.0255 0.0189  0.0384  11  LYS   A C   
232  C C   B LYS   A 11  ? 0.2186 0.1801 0.2029 0.0004  0.0489  0.0233  11  LYS   A C   
233  O O   A LYS   A 11  ? 0.1373 0.1808 0.2119 -0.0561 0.0253  0.0305  11  LYS   A O   
234  O O   B LYS   A 11  ? 0.2202 0.1766 0.2013 0.0007  0.0572  0.0190  11  LYS   A O   
235  C CB  A LYS   A 11  ? 0.1605 0.1504 0.1673 -0.0307 0.0088  0.0323  11  LYS   A CB  
236  C CB  B LYS   A 11  ? 0.2243 0.1735 0.2108 0.0019  0.0415  0.0230  11  LYS   A CB  
237  C CG  A LYS   A 11  ? 0.1681 0.1453 0.1653 -0.0289 0.0165  0.0343  11  LYS   A CG  
238  C CG  B LYS   A 11  ? 0.2251 0.1734 0.2138 0.0013  0.0368  0.0251  11  LYS   A CG  
239  C CD  A LYS   A 11  ? 0.1799 0.1485 0.1611 -0.0285 0.0090  0.0287  11  LYS   A CD  
240  C CD  B LYS   A 11  ? 0.2266 0.1737 0.2110 -0.0006 0.0341  0.0261  11  LYS   A CD  
241  C CE  A LYS   A 11  ? 0.1859 0.1461 0.1628 -0.0183 -0.0008 0.0359  11  LYS   A CE  
242  C CE  B LYS   A 11  ? 0.2283 0.1737 0.2055 -0.0038 0.0334  0.0267  11  LYS   A CE  
243  N NZ  A LYS   A 11  ? 0.1846 0.1436 0.1720 -0.0093 -0.0089 0.0308  11  LYS   A NZ  
244  N NZ  B LYS   A 11  ? 0.2303 0.1726 0.2021 -0.0037 0.0314  0.0213  11  LYS   A NZ  
271  N N   A LEU   A 12  ? 0.1189 0.1477 0.1549 -0.0257 0.0128  0.0285  12  LEU   A N   
272  N N   B LEU   A 12  ? 0.2129 0.1873 0.2036 -0.0024 0.0495  0.0243  12  LEU   A N   
273  C CA  A LEU   A 12  ? 0.1217 0.1571 0.1602 -0.0173 0.0112  0.0359  12  LEU   A CA  
274  C CA  B LEU   A 12  ? 0.2053 0.1923 0.2000 -0.0015 0.0456  0.0266  12  LEU   A CA  
275  C C   A LEU   A 12  ? 0.1296 0.1469 0.1574 -0.0274 0.0122  0.0356  12  LEU   A C   
276  C C   B LEU   A 12  ? 0.1980 0.1965 0.1829 -0.0001 0.0484  0.0220  12  LEU   A C   
277  O O   A LEU   A 12  ? 0.1371 0.1539 0.1716 -0.0284 0.0061  0.0277  12  LEU   A O   
278  O O   B LEU   A 12  ? 0.1974 0.1948 0.1784 -0.0001 0.0493  0.0246  12  LEU   A O   
279  C CB  A LEU   A 12  ? 0.1247 0.1571 0.1733 -0.0120 -0.0021 0.0397  12  LEU   A CB  
280  C CB  B LEU   A 12  ? 0.2008 0.1935 0.2110 -0.0008 0.0430  0.0306  12  LEU   A CB  
281  C CG  A LEU   A 12  ? 0.1359 0.1636 0.1884 -0.0071 0.0029  0.0430  12  LEU   A CG  
282  C CG  B LEU   A 12  ? 0.1976 0.1934 0.2199 0.0020  0.0455  0.0298  12  LEU   A CG  
283  C CD1 A LEU   A 12  ? 0.1535 0.1663 0.1998 0.0018  0.0155  0.0515  12  LEU   A CD1 
284  C CD1 B LEU   A 12  ? 0.1964 0.1947 0.2187 0.0069  0.0464  0.0275  12  LEU   A CD1 
285  C CD2 A LEU   A 12  ? 0.1400 0.1769 0.2150 -0.0072 -0.0050 0.0383  12  LEU   A CD2 
286  C CD2 B LEU   A 12  ? 0.1952 0.1923 0.2273 -0.0022 0.0463  0.0367  12  LEU   A CD2 
309  N N   A THR   A 13  ? 0.1236 0.1421 0.1613 -0.0266 0.0080  0.0277  13  THR   A N   
310  N N   B THR   A 13  ? 0.1943 0.2011 0.1862 0.0032  0.0422  0.0158  13  THR   A N   
311  C CA  A THR   A 13  ? 0.1269 0.1432 0.1691 -0.0236 0.0102  0.0288  13  THR   A CA  
312  C CA  B THR   A 13  ? 0.1911 0.2038 0.1820 0.0041  0.0381  0.0167  13  THR   A CA  
313  C C   A THR   A 13  ? 0.1337 0.1432 0.1769 -0.0257 0.0095  0.0305  13  THR   A C   
314  C C   B THR   A 13  ? 0.1906 0.2038 0.1847 0.0039  0.0377  0.0200  13  THR   A C   
315  O O   A THR   A 13  ? 0.1354 0.1398 0.1734 -0.0245 0.0060  0.0322  13  THR   A O   
316  O O   B THR   A 13  ? 0.1913 0.2046 0.1881 0.0037  0.0401  0.0205  13  THR   A O   
317  C CB  A THR   A 13  ? 0.1342 0.1540 0.1769 -0.0224 0.0094  0.0339  13  THR   A CB  
318  C CB  B THR   A 13  ? 0.1884 0.2070 0.1744 0.0080  0.0381  0.0148  13  THR   A CB  
319  O OG1 A THR   A 13  ? 0.1357 0.1514 0.1888 -0.0251 -0.0041 0.0355  13  THR   A OG1 
320  O OG1 B THR   A 13  ? 0.1846 0.2091 0.1820 0.0075  0.0438  0.0153  13  THR   A OG1 
321  C CG2 A THR   A 13  ? 0.1445 0.1726 0.1929 -0.0212 0.0091  0.0202  13  THR   A CG2 
322  C CG2 B THR   A 13  ? 0.1886 0.2077 0.1711 0.0108  0.0397  0.0141  13  THR   A CG2 
337  N N   A ASP   A 14  ? 0.1422 0.1329 0.1869 -0.0270 -0.0011 0.0385  14  ASP   A N   
338  N N   B ASP   A 14  ? 0.1933 0.2024 0.1939 0.0045  0.0294  0.0219  14  ASP   A N   
339  C CA  A ASP   A 14  ? 0.1415 0.1415 0.1990 -0.0230 -0.0007 0.0405  14  ASP   A CA  
340  C CA  B ASP   A 14  ? 0.1978 0.1995 0.2078 0.0050  0.0281  0.0334  14  ASP   A CA  
341  C C   A ASP   A 14  ? 0.1373 0.1405 0.1766 -0.0181 -0.0072 0.0412  14  ASP   A C   
342  C C   B ASP   A 14  ? 0.1927 0.1847 0.1854 0.0055  0.0308  0.0384  14  ASP   A C   
343  O O   A ASP   A 14  ? 0.1547 0.1607 0.1917 -0.0272 -0.0150 0.0428  14  ASP   A O   
344  O O   B ASP   A 14  ? 0.1906 0.1793 0.1758 0.0055  0.0311  0.0403  14  ASP   A O   
345  C CB  A ASP   A 14  ? 0.1643 0.1611 0.2491 -0.0259 0.0031  0.0528  14  ASP   A CB  
346  C CB  B ASP   A 14  ? 0.2056 0.2111 0.2485 0.0049  0.0220  0.0384  14  ASP   A CB  
347  C CG  A ASP   A 14  ? 0.1845 0.2101 0.3262 -0.0307 -0.0047 0.0492  14  ASP   A CG  
348  C CG  B ASP   A 14  ? 0.2161 0.2226 0.2884 0.0028  0.0172  0.0390  14  ASP   A CG  
349  O OD1 A ASP   A 14  ? 0.1990 0.2207 0.3411 -0.0186 -0.0194 0.0548  14  ASP   A OD1 
350  O OD1 B ASP   A 14  ? 0.2206 0.2277 0.2967 0.0006  0.0141  0.0418  14  ASP   A OD1 
351  O OD2 A ASP   A 14  ? 0.2006 0.2492 0.3694 -0.0212 -0.0069 0.0366  14  ASP   A OD2 
352  O OD2 B ASP   A 14  ? 0.2180 0.2246 0.3074 0.0010  0.0160  0.0353  14  ASP   A OD2 
361  N N   A ASN   A 15  ? 0.1313 0.1243 0.1746 -0.0145 0.0022  0.0387  15  ASN   A N   
362  N N   B ASN   A 15  ? 0.1878 0.1726 0.1763 0.0064  0.0336  0.0418  15  ASN   A N   
363  C CA  A ASN   A 15  ? 0.1289 0.1336 0.1944 -0.0176 -0.0042 0.0284  15  ASN   A CA  
364  C CA  B ASN   A 15  ? 0.1839 0.1650 0.1743 0.0101  0.0337  0.0303  15  ASN   A CA  
365  C C   A ASN   A 15  ? 0.1283 0.1278 0.2121 -0.0181 0.0015  0.0287  15  ASN   A C   
366  C C   B ASN   A 15  ? 0.1810 0.1617 0.1735 0.0056  0.0373  0.0242  15  ASN   A C   
367  O O   A ASN   A 15  ? 0.1307 0.1292 0.2509 -0.0099 -0.0145 0.0253  15  ASN   A O   
368  O O   B ASN   A 15  ? 0.1816 0.1632 0.1863 0.0017  0.0359  0.0161  15  ASN   A O   
369  C CB  A ASN   A 15  ? 0.1237 0.1318 0.1928 -0.0117 0.0007  0.0256  15  ASN   A CB  
370  C CB  B ASN   A 15  ? 0.1852 0.1657 0.1777 0.0133  0.0301  0.0327  15  ASN   A CB  
371  C CG  A ASN   A 15  ? 0.1284 0.1371 0.1901 -0.0064 0.0070  0.0134  15  ASN   A CG  
372  C CG  B ASN   A 15  ? 0.1857 0.1686 0.1782 0.0140  0.0285  0.0314  15  ASN   A CG  
373  O OD1 A ASN   A 15  ? 0.1363 0.1474 0.2004 -0.0237 0.0102  0.0109  15  ASN   A OD1 
374  O OD1 B ASN   A 15  ? 0.1846 0.1659 0.1797 0.0179  0.0324  0.0379  15  ASN   A OD1 
375  N ND2 A ASN   A 15  ? 0.1334 0.1561 0.1830 -0.0179 0.0137  0.0112  15  ASN   A ND2 
376  N ND2 B ASN   A 15  ? 0.1853 0.1708 0.1744 0.0126  0.0268  0.0338  15  ASN   A ND2 
389  N N   A VAL   A 16  ? 0.1284 0.1218 0.1974 -0.0140 -0.0014 0.0344  16  VAL   A N   
390  N N   B VAL   A 16  ? 0.1795 0.1600 0.1584 0.0061  0.0424  0.0274  16  VAL   A N   
391  C CA  A VAL   A 16  ? 0.1252 0.1351 0.1843 -0.0125 0.0070  0.0303  16  VAL   A CA  
392  C CA  B VAL   A 16  ? 0.1802 0.1616 0.1518 0.0102  0.0458  0.0299  16  VAL   A CA  
393  C C   A VAL   A 16  ? 0.1173 0.1325 0.1824 -0.0171 0.0031  0.0291  16  VAL   A C   
394  C C   B VAL   A 16  ? 0.1829 0.1654 0.1507 0.0099  0.0474  0.0262  16  VAL   A C   
395  O O   A VAL   A 16  ? 0.1111 0.1329 0.2007 -0.0160 0.0069  0.0265  16  VAL   A O   
396  O O   B VAL   A 16  ? 0.1821 0.1647 0.1505 0.0150  0.0501  0.0278  16  VAL   A O   
397  C CB  A VAL   A 16  ? 0.1279 0.1523 0.1841 0.0021  0.0252  0.0393  16  VAL   A CB  
398  C CB  B VAL   A 16  ? 0.1795 0.1619 0.1531 0.0130  0.0461  0.0297  16  VAL   A CB  
399  C CG1 A VAL   A 16  ? 0.1419 0.1651 0.1949 0.0115  0.0153  0.0420  16  VAL   A CG1 
400  C CG1 B VAL   A 16  ? 0.1805 0.1631 0.1587 0.0150  0.0394  0.0298  16  VAL   A CG1 
401  C CG2 A VAL   A 16  ? 0.1368 0.1690 0.1994 0.0082  0.0351  0.0333  16  VAL   A CG2 
402  C CG2 B VAL   A 16  ? 0.1769 0.1650 0.1575 0.0144  0.0464  0.0300  16  VAL   A CG2 
421  N N   A TYR   A 17  ? 0.1189 0.1285 0.1788 -0.0144 0.0155  0.0285  17  TYR   A N   
422  N N   B TYR   A 17  ? 0.1885 0.1689 0.1571 0.0021  0.0455  0.0260  17  TYR   A N   
423  C CA  A TYR   A 17  ? 0.1223 0.1359 0.1785 -0.0191 0.0116  0.0386  17  TYR   A CA  
424  C CA  B TYR   A 17  ? 0.1940 0.1776 0.1665 -0.0002 0.0430  0.0238  17  TYR   A CA  
425  C C   A TYR   A 17  ? 0.1222 0.1372 0.1883 -0.0133 0.0117  0.0253  17  TYR   A C   
426  C C   B TYR   A 17  ? 0.1864 0.1778 0.1640 -0.0122 0.0560  0.0281  17  TYR   A C   
427  O O   A TYR   A 17  ? 0.1258 0.1283 0.2004 -0.0068 0.0202  0.0358  17  TYR   A O   
428  O O   B TYR   A 17  ? 0.1830 0.1791 0.1717 -0.0157 0.0629  0.0231  17  TYR   A O   
429  C CB  A TYR   A 17  ? 0.1350 0.1413 0.1721 -0.0147 0.0056  0.0336  17  TYR   A CB  
430  C CB  B TYR   A 17  ? 0.2067 0.1845 0.1833 0.0049  0.0258  0.0245  17  TYR   A CB  
431  C CG  A TYR   A 17  ? 0.1543 0.1524 0.1650 -0.0200 -0.0038 0.0258  17  TYR   A CG  
432  C CG  B TYR   A 17  ? 0.2191 0.1913 0.2010 0.0103  0.0122  0.0218  17  TYR   A CG  
433  C CD1 A TYR   A 17  ? 0.1652 0.1585 0.1742 -0.0097 -0.0063 0.0265  17  TYR   A CD1 
434  C CD1 B TYR   A 17  ? 0.2251 0.1961 0.2096 0.0115  0.0059  0.0225  17  TYR   A CD1 
435  C CD2 A TYR   A 17  ? 0.1700 0.1576 0.1574 -0.0321 0.0001  0.0303  17  TYR   A CD2 
436  C CD2 B TYR   A 17  ? 0.2231 0.1941 0.2058 0.0123  0.0084  0.0215  17  TYR   A CD2 
437  C CE1 A TYR   A 17  ? 0.1801 0.1578 0.1778 -0.0175 -0.0170 0.0312  17  TYR   A CE1 
438  C CE1 B TYR   A 17  ? 0.2314 0.1992 0.2179 0.0111  0.0006  0.0211  17  TYR   A CE1 
439  C CE2 A TYR   A 17  ? 0.1915 0.1556 0.1632 -0.0369 -0.0018 0.0224  17  TYR   A CE2 
440  C CE2 B TYR   A 17  ? 0.2296 0.1977 0.2143 0.0090  0.0056  0.0209  17  TYR   A CE2 
441  C CZ  A TYR   A 17  ? 0.1967 0.1504 0.1713 -0.0317 -0.0161 0.0364  17  TYR   A CZ  
442  C CZ  B TYR   A 17  ? 0.2350 0.2002 0.2223 0.0083  0.0005  0.0177  17  TYR   A CZ  
443  O OH  A TYR   A 17  ? 0.2175 0.1522 0.1868 -0.0251 -0.0210 0.0417  17  TYR   A OH  
444  O OH  B TYR   A 17  ? 0.2402 0.2018 0.2245 0.0042  -0.0015 0.0135  17  TYR   A OH  
463  N N   A ILE   A 18  ? 0.1231 0.1411 0.1911 -0.0189 0.0096  0.0389  18  ILE   A N   
464  N N   B ILE   A 18  ? 0.1836 0.1766 0.1589 -0.0177 0.0543  0.0404  18  ILE   A N   
465  C CA  A ILE   A 18  ? 0.1287 0.1489 0.1934 -0.0142 0.0201  0.0380  18  ILE   A CA  
466  C CA  B ILE   A 18  ? 0.1835 0.1774 0.1723 -0.0219 0.0502  0.0376  18  ILE   A CA  
467  C C   A ILE   A 18  ? 0.1275 0.1538 0.1999 -0.0143 0.0162  0.0318  18  ILE   A C   
468  C C   B ILE   A 18  ? 0.1856 0.1828 0.1780 -0.0244 0.0566  0.0324  18  ILE   A C   
469  O O   A ILE   A 18  ? 0.1256 0.1681 0.2122 -0.0199 0.0260  0.0384  18  ILE   A O   
470  O O   B ILE   A 18  ? 0.1830 0.1854 0.1800 -0.0266 0.0574  0.0369  18  ILE   A O   
471  C CB  A ILE   A 18  ? 0.1382 0.1566 0.1892 -0.0020 0.0133  0.0453  18  ILE   A CB  
472  C CB  B ILE   A 18  ? 0.1887 0.1775 0.1879 -0.0198 0.0382  0.0292  18  ILE   A CB  
473  C CG1 A ILE   A 18  ? 0.1598 0.1676 0.1973 0.0017  -0.0029 0.0602  18  ILE   A CG1 
474  C CG1 B ILE   A 18  ? 0.1913 0.1806 0.1944 -0.0243 0.0274  0.0228  18  ILE   A CG1 
475  C CG2 A ILE   A 18  ? 0.1353 0.1564 0.1943 -0.0006 0.0086  0.0500  18  ILE   A CG2 
476  C CG2 B ILE   A 18  ? 0.1909 0.1797 0.2015 -0.0194 0.0398  0.0285  18  ILE   A CG2 
477  C CD1 A ILE   A 18  ? 0.1838 0.1824 0.2171 -0.0053 -0.0096 0.0598  18  ILE   A CD1 
478  C CD1 B ILE   A 18  ? 0.1941 0.1857 0.2023 -0.0247 0.0224  0.0141  18  ILE   A CD1 
501  N N   A LYS   A 19  ? 0.1375 0.1558 0.2198 -0.0088 0.0319  0.0298  19  LYS   A N   
502  N N   B LYS   A 19  ? 0.1871 0.1872 0.1807 -0.0213 0.0631  0.0210  19  LYS   A N   
503  C CA  A LYS   A 19  ? 0.1527 0.1720 0.2410 0.0000  0.0426  0.0328  19  LYS   A CA  
504  C CA  B LYS   A 19  ? 0.1903 0.1945 0.1912 -0.0154 0.0607  0.0107  19  LYS   A CA  
505  C C   A LYS   A 19  ? 0.1411 0.1656 0.2579 0.0042  0.0436  0.0345  19  LYS   A C   
506  C C   B LYS   A 19  ? 0.1864 0.1893 0.1947 -0.0166 0.0564  0.0147  19  LYS   A C   
507  O O   A LYS   A 19  ? 0.1398 0.1604 0.2604 -0.0001 0.0432  0.0308  19  LYS   A O   
508  O O   B LYS   A 19  ? 0.1889 0.1849 0.1985 -0.0198 0.0562  0.0111  19  LYS   A O   
509  C CB  A LYS   A 19  ? 0.1715 0.1956 0.2495 -0.0057 0.0518  0.0265  19  LYS   A CB  
510  C CB  B LYS   A 19  ? 0.1976 0.2063 0.2009 -0.0098 0.0593  -0.0042 19  LYS   A CB  
511  C CG  A LYS   A 19  ? 0.2097 0.2136 0.2546 -0.0016 0.0490  0.0149  19  LYS   A CG  
512  C CG  B LYS   A 19  ? 0.2078 0.2167 0.2122 -0.0064 0.0536  -0.0177 19  LYS   A CG  
513  C CD  A LYS   A 19  ? 0.2347 0.2303 0.2527 0.0013  0.0569  0.0122  19  LYS   A CD  
514  C CD  B LYS   A 19  ? 0.2173 0.2260 0.2244 -0.0053 0.0461  -0.0245 19  LYS   A CD  
515  C CE  A LYS   A 19  ? 0.2513 0.2346 0.2520 -0.0022 0.0566  0.0058  19  LYS   A CE  
516  C CE  B LYS   A 19  ? 0.2217 0.2302 0.2304 -0.0060 0.0431  -0.0268 19  LYS   A CE  
517  N NZ  A LYS   A 19  ? 0.2601 0.2344 0.2362 -0.0141 0.0624  -0.0010 19  LYS   A NZ  
518  N NZ  B LYS   A 19  ? 0.2224 0.2310 0.2311 -0.0065 0.0395  -0.0284 19  LYS   A NZ  
545  N N   A ASN   A 20  ? 0.1510 0.1678 0.2847 0.0039  0.0444  0.0430  20  ASN   A N   
546  N N   B ASN   A 20  ? 0.1832 0.1911 0.1964 -0.0162 0.0501  0.0209  20  ASN   A N   
547  C CA  A ASN   A 20  ? 0.1691 0.1873 0.2977 0.0238  0.0546  0.0315  20  ASN   A CA  
548  C CA  B ASN   A 20  ? 0.1811 0.1989 0.2007 -0.0080 0.0384  0.0207  20  ASN   A CA  
549  C C   A ASN   A 20  ? 0.1839 0.1829 0.2806 0.0156  0.0652  0.0278  20  ASN   A C   
550  C C   B ASN   A 20  ? 0.1882 0.2047 0.2110 -0.0035 0.0364  0.0128  20  ASN   A C   
551  O O   A ASN   A 20  ? 0.2006 0.1886 0.2789 0.0005  0.0636  0.0240  20  ASN   A O   
552  O O   B ASN   A 20  ? 0.1862 0.2045 0.2164 0.0019  0.0420  0.0162  20  ASN   A O   
553  C CB  A ASN   A 20  ? 0.1780 0.2109 0.3273 0.0395  0.0613  0.0363  20  ASN   A CB  
554  C CB  B ASN   A 20  ? 0.1742 0.2028 0.1983 -0.0048 0.0300  0.0296  20  ASN   A CB  
555  C CG  A ASN   A 20  ? 0.1987 0.2291 0.3603 0.0523  0.0661  0.0400  20  ASN   A CG  
556  C CG  B ASN   A 20  ? 0.1684 0.2059 0.1959 0.0009  0.0196  0.0333  20  ASN   A CG  
557  O OD1 A ASN   A 20  ? 0.2206 0.2399 0.3811 0.0607  0.0657  0.0381  20  ASN   A OD1 
558  O OD1 B ASN   A 20  ? 0.1653 0.2058 0.1947 0.0046  0.0126  0.0268  20  ASN   A OD1 
559  N ND2 A ASN   A 20  ? 0.2056 0.2326 0.3783 0.0542  0.0566  0.0468  20  ASN   A ND2 
560  N ND2 B ASN   A 20  ? 0.1712 0.2079 0.2079 0.0016  0.0159  0.0401  20  ASN   A ND2 
573  N N   A ALA   A 21  ? 0.1896 0.1859 0.2815 0.0100  0.0668  0.0164  21  ALA   A N   
574  N N   B ALA   A 21  ? 0.1950 0.2097 0.2197 -0.0030 0.0208  0.0054  21  ALA   A N   
575  C CA  A ALA   A 21  ? 0.1934 0.1887 0.2739 -0.0016 0.0734  0.0198  21  ALA   A CA  
576  C CA  B ALA   A 21  ? 0.1999 0.2153 0.2240 -0.0036 0.0113  0.0019  21  ALA   A CA  
577  C C   A ALA   A 21  ? 0.1853 0.1855 0.2564 -0.0036 0.0745  0.0204  21  ALA   A C   
578  C C   B ALA   A 21  ? 0.1969 0.2143 0.2179 -0.0023 0.0078  0.0014  21  ALA   A C   
579  O O   A ALA   A 21  ? 0.1878 0.2000 0.2473 0.0041  0.0580  0.0195  21  ALA   A O   
580  O O   B ALA   A 21  ? 0.1988 0.2167 0.2124 -0.0004 0.0091  0.0072  21  ALA   A O   
581  C CB  A ALA   A 21  ? 0.2145 0.2020 0.2860 -0.0121 0.0587  0.0305  21  ALA   A CB  
582  C CB  B ALA   A 21  ? 0.2071 0.2213 0.2314 -0.0054 0.0049  0.0024  21  ALA   A CB  
593  N N   A ASP   A 22  ? 0.1876 0.1828 0.2597 -0.0196 0.0705  0.0213  22  ASP   A N   
594  N N   B ASP   A 22  ? 0.1943 0.2142 0.2216 -0.0074 0.0043  -0.0029 22  ASP   A N   
595  C CA  A ASP   A 22  ? 0.1999 0.1931 0.2534 -0.0234 0.0597  0.0194  22  ASP   A CA  
596  C CA  B ASP   A 22  ? 0.1921 0.2165 0.2191 -0.0121 0.0048  -0.0022 22  ASP   A CA  
597  C C   A ASP   A 22  ? 0.1842 0.2062 0.2097 -0.0249 0.0600  0.0235  22  ASP   A C   
598  C C   B ASP   A 22  ? 0.1908 0.2178 0.2114 -0.0206 0.0051  -0.0003 22  ASP   A C   
599  O O   A ASP   A 22  ? 0.1892 0.2231 0.2096 -0.0215 0.0611  0.0300  22  ASP   A O   
600  O O   B ASP   A 22  ? 0.1913 0.2215 0.2172 -0.0226 0.0096  0.0039  22  ASP   A O   
601  C CB  A ASP   A 22  ? 0.2325 0.2026 0.3067 -0.0234 0.0487  0.0200  22  ASP   A CB  
602  C CB  B ASP   A 22  ? 0.1906 0.2168 0.2219 -0.0093 0.0082  -0.0003 22  ASP   A CB  
603  C CG  A ASP   A 22  ? 0.2572 0.2149 0.3715 -0.0278 0.0300  0.0275  22  ASP   A CG  
604  C CG  B ASP   A 22  ? 0.1844 0.2162 0.2237 -0.0089 0.0115  0.0033  22  ASP   A CG  
605  O OD1 A ASP   A 22  ? 0.2550 0.2114 0.3827 -0.0400 0.0190  0.0502  22  ASP   A OD1 
606  O OD1 B ASP   A 22  ? 0.1742 0.2101 0.2091 -0.0101 0.0049  0.0033  22  ASP   A OD1 
607  O OD2 A ASP   A 22  ? 0.2762 0.2331 0.4165 -0.0239 0.0270  0.0141  22  ASP   A OD2 
608  O OD2 B ASP   A 22  ? 0.1867 0.2223 0.2361 -0.0080 0.0225  0.0028  22  ASP   A OD2 
617  N N   A ILE   A 23  ? 0.1792 0.2079 0.2004 -0.0246 0.0556  0.0206  23  ILE   A N   
618  N N   B ILE   A 23  ? 0.1924 0.2179 0.2090 -0.0242 0.0068  0.0026  23  ILE   A N   
619  C CA  A ILE   A 23  ? 0.1743 0.1998 0.1784 -0.0173 0.0465  0.0227  23  ILE   A CA  
620  C CA  B ILE   A 23  ? 0.1912 0.2177 0.2013 -0.0252 0.0117  0.0030  23  ILE   A CA  
621  C C   A ILE   A 23  ? 0.1785 0.2076 0.1679 -0.0182 0.0552  0.0169  23  ILE   A C   
622  C C   B ILE   A 23  ? 0.1920 0.2205 0.2017 -0.0267 0.0161  0.0030  23  ILE   A C   
623  O O   A ILE   A 23  ? 0.1897 0.2094 0.1674 -0.0097 0.0496  0.0061  23  ILE   A O   
624  O O   B ILE   A 23  ? 0.1921 0.2194 0.2014 -0.0235 0.0170  0.0010  23  ILE   A O   
625  C CB  A ILE   A 23  ? 0.1735 0.1932 0.1574 -0.0166 0.0312  0.0243  23  ILE   A CB  
626  C CB  B ILE   A 23  ? 0.1930 0.2160 0.1885 -0.0242 0.0120  -0.0017 23  ILE   A CB  
627  C CG1 A ILE   A 23  ? 0.1785 0.1929 0.1663 -0.0090 0.0211  0.0102  23  ILE   A CG1 
628  C CG1 B ILE   A 23  ? 0.1904 0.2136 0.1782 -0.0265 0.0170  -0.0086 23  ILE   A CG1 
629  C CG2 A ILE   A 23  ? 0.1768 0.1934 0.1653 -0.0164 0.0266  0.0240  23  ILE   A CG2 
630  C CG2 B ILE   A 23  ? 0.1936 0.2168 0.1920 -0.0230 0.0104  -0.0042 23  ILE   A CG2 
631  C CD1 A ILE   A 23  ? 0.1813 0.1880 0.1658 -0.0142 0.0022  0.0003  23  ILE   A CD1 
632  C CD1 B ILE   A 23  ? 0.1902 0.2115 0.1732 -0.0265 0.0192  -0.0100 23  ILE   A CD1 
655  N N   A VAL   A 24  ? 0.1870 0.2155 0.1946 -0.0303 0.0596  0.0135  24  VAL   A N   
656  N N   B VAL   A 24  ? 0.1976 0.2258 0.2123 -0.0316 0.0158  0.0026  24  VAL   A N   
657  C CA  A VAL   A 24  ? 0.2088 0.2227 0.2301 -0.0355 0.0564  0.0049  24  VAL   A CA  
658  C CA  B VAL   A 24  ? 0.2062 0.2321 0.2222 -0.0339 0.0165  0.0043  24  VAL   A CA  
659  C C   A VAL   A 24  ? 0.2202 0.2362 0.2346 -0.0424 0.0588  -0.0078 24  VAL   A C   
660  C C   B VAL   A 24  ? 0.2163 0.2440 0.2263 -0.0315 0.0186  -0.0029 24  VAL   A C   
661  O O   A VAL   A 24  ? 0.2304 0.2317 0.2259 -0.0329 0.0623  -0.0125 24  VAL   A O   
662  O O   B VAL   A 24  ? 0.2179 0.2428 0.2254 -0.0268 0.0179  -0.0029 24  VAL   A O   
663  C CB  A VAL   A 24  ? 0.2161 0.2281 0.2619 -0.0366 0.0581  0.0123  24  VAL   A CB  
664  C CB  B VAL   A 24  ? 0.2047 0.2318 0.2312 -0.0382 0.0145  0.0132  24  VAL   A CB  
665  C CG1 A VAL   A 24  ? 0.2250 0.2345 0.2773 -0.0353 0.0577  0.0055  24  VAL   A CG1 
666  C CG1 B VAL   A 24  ? 0.2070 0.2332 0.2355 -0.0392 0.0126  0.0172  24  VAL   A CG1 
667  C CG2 A VAL   A 24  ? 0.2295 0.2392 0.2775 -0.0333 0.0658  0.0242  24  VAL   A CG2 
668  C CG2 B VAL   A 24  ? 0.2047 0.2332 0.2331 -0.0411 0.0139  0.0121  24  VAL   A CG2 
687  N N   A GLU   A 25  ? 0.2306 0.2682 0.2415 -0.0448 0.0758  -0.0145 25  GLU   A N   
688  N N   B GLU   A 25  ? 0.2272 0.2604 0.2330 -0.0309 0.0260  -0.0086 25  GLU   A N   
689  C CA  A GLU   A 25  ? 0.2501 0.3029 0.2512 -0.0405 0.0898  -0.0182 25  GLU   A CA  
690  C CA  B GLU   A 25  ? 0.2410 0.2783 0.2452 -0.0301 0.0318  -0.0117 25  GLU   A CA  
691  C C   A GLU   A 25  ? 0.2438 0.3035 0.2185 -0.0523 0.0967  -0.0170 25  GLU   A C   
692  C C   B GLU   A 25  ? 0.2427 0.2856 0.2224 -0.0333 0.0416  -0.0148 25  GLU   A C   
693  O O   A GLU   A 25  ? 0.2496 0.3113 0.2214 -0.0509 0.0925  -0.0194 25  GLU   A O   
694  O O   B GLU   A 25  ? 0.2434 0.2882 0.2155 -0.0326 0.0484  -0.0179 25  GLU   A O   
695  C CB  A GLU   A 25  ? 0.2754 0.3320 0.2989 -0.0292 0.0964  -0.0124 25  GLU   A CB  
696  C CB  B GLU   A 25  ? 0.2517 0.2868 0.2783 -0.0276 0.0277  -0.0083 25  GLU   A CB  
697  C CG  A GLU   A 25  ? 0.3030 0.3568 0.3660 -0.0213 0.0823  -0.0073 25  GLU   A CG  
698  C CG  B GLU   A 25  ? 0.2610 0.2947 0.3125 -0.0270 0.0178  -0.0040 25  GLU   A CG  
699  C CD  A GLU   A 25  ? 0.3243 0.3774 0.4289 -0.0160 0.0699  0.0000  25  GLU   A CD  
700  C CD  B GLU   A 25  ? 0.2679 0.3016 0.3430 -0.0275 0.0087  -0.0008 25  GLU   A CD  
701  O OE1 A GLU   A 25  ? 0.3344 0.3871 0.4500 -0.0123 0.0545  0.0006  25  GLU   A OE1 
702  O OE1 B GLU   A 25  ? 0.2709 0.3029 0.3470 -0.0280 0.0074  0.0016  25  GLU   A OE1 
703  O OE2 A GLU   A 25  ? 0.3299 0.3824 0.4595 -0.0149 0.0675  -0.0026 25  GLU   A OE2 
704  O OE2 B GLU   A 25  ? 0.2696 0.3044 0.3556 -0.0276 0.0059  -0.0009 25  GLU   A OE2 
717  N N   A GLU   A 26  ? 0.2379 0.2910 0.2178 -0.0673 0.0955  -0.0191 26  GLU   A N   
718  N N   B GLU   A 26  ? 0.2440 0.2891 0.2120 -0.0385 0.0427  -0.0165 26  GLU   A N   
719  C CA  A GLU   A 26  ? 0.2449 0.2791 0.2042 -0.0798 0.0887  -0.0108 26  GLU   A CA  
720  C CA  B GLU   A 26  ? 0.2484 0.2922 0.2064 -0.0432 0.0435  -0.0143 26  GLU   A CA  
721  C C   A GLU   A 26  ? 0.2338 0.2606 0.1747 -0.0772 0.0769  -0.0125 26  GLU   A C   
722  C C   B GLU   A 26  ? 0.2515 0.2834 0.1934 -0.0414 0.0435  -0.0142 26  GLU   A C   
723  O O   A GLU   A 26  ? 0.2331 0.2580 0.1732 -0.0865 0.0698  -0.0083 26  GLU   A O   
724  O O   B GLU   A 26  ? 0.2487 0.2811 0.1924 -0.0414 0.0429  -0.0131 26  GLU   A O   
725  C CB  A GLU   A 26  ? 0.2709 0.2771 0.2481 -0.0906 0.0752  -0.0075 26  GLU   A CB  
726  C CB  B GLU   A 26  ? 0.2511 0.3027 0.2196 -0.0480 0.0423  -0.0121 26  GLU   A CB  
727  C CG  A GLU   A 26  ? 0.2968 0.2779 0.2942 -0.0953 0.0836  -0.0131 26  GLU   A CG  
728  C CG  B GLU   A 26  ? 0.2570 0.3113 0.2459 -0.0516 0.0352  -0.0101 26  GLU   A CG  
729  C CD  A GLU   A 26  ? 0.3074 0.2724 0.3113 -0.1039 0.1085  -0.0161 26  GLU   A CD  
730  C CD  B GLU   A 26  ? 0.2592 0.3170 0.2585 -0.0563 0.0329  -0.0087 26  GLU   A CD  
731  O OE1 A GLU   A 26  ? 0.2992 0.2931 0.3116 -0.0914 0.1266  -0.0671 26  GLU   A OE1 
732  O OE1 B GLU   A 26  ? 0.2631 0.3243 0.2555 -0.0548 0.0327  -0.0123 26  GLU   A OE1 
733  O OE2 A GLU   A 26  ? 0.3230 0.2698 0.3192 -0.1024 0.1127  0.0008  26  GLU   A OE2 
734  O OE2 B GLU   A 26  ? 0.2583 0.3168 0.2752 -0.0615 0.0232  -0.0100 26  GLU   A OE2 
747  N N   A ALA   A 27  ? 0.2193 0.2344 0.1673 -0.0742 0.0692  -0.0170 27  ALA   A N   
748  N N   B ALA   A 27  ? 0.2566 0.2749 0.1853 -0.0427 0.0444  -0.0161 27  ALA   A N   
749  C CA  A ALA   A 27  ? 0.2261 0.2308 0.1500 -0.0661 0.0651  -0.0142 27  ALA   A CA  
750  C CA  B ALA   A 27  ? 0.2657 0.2707 0.1770 -0.0444 0.0474  -0.0191 27  ALA   A CA  
751  C C   A ALA   A 27  ? 0.2561 0.2395 0.1556 -0.0683 0.0615  -0.0256 27  ALA   A C   
752  C C   B ALA   A 27  ? 0.2795 0.2696 0.1744 -0.0498 0.0523  -0.0295 27  ALA   A C   
753  O O   A ALA   A 27  ? 0.2616 0.2301 0.1606 -0.0774 0.0457  -0.0197 27  ALA   A O   
754  O O   B ALA   A 27  ? 0.2824 0.2702 0.1703 -0.0488 0.0519  -0.0252 27  ALA   A O   
755  C CB  A ALA   A 27  ? 0.2143 0.2239 0.1571 -0.0596 0.0502  -0.0183 27  ALA   A CB  
756  C CB  B ALA   A 27  ? 0.2635 0.2689 0.1767 -0.0419 0.0453  -0.0156 27  ALA   A CB  
767  N N   . LYS   A 28  ? 0.2926 0.2694 0.1829 -0.0565 0.0524  -0.0459 28  LYS   A N   
768  C CA  . LYS   A 28  ? 0.3425 0.3132 0.2172 -0.0518 0.0584  -0.0692 28  LYS   A CA  
769  C C   . LYS   A 28  ? 0.3631 0.3463 0.2020 -0.0596 0.0740  -0.0548 28  LYS   A C   
770  O O   . LYS   A 28  ? 0.3717 0.3581 0.2490 -0.0611 0.0512  -0.0434 28  LYS   A O   
771  C CB  . LYS   A 28  ? 0.3716 0.3342 0.2708 -0.0370 0.0506  -0.0934 28  LYS   A CB  
772  C CG  . LYS   A 28  ? 0.3950 0.3516 0.3271 -0.0251 0.0407  -0.1068 28  LYS   A CG  
773  C CD  . LYS   A 28  ? 0.4139 0.3715 0.4023 -0.0158 0.0267  -0.1068 28  LYS   A CD  
774  C CE  . LYS   A 28  ? 0.4305 0.3897 0.4598 -0.0091 0.0177  -0.1077 28  LYS   A CE  
775  N NZ  . LYS   A 28  ? 0.4402 0.3996 0.4968 -0.0039 0.0142  -0.1091 28  LYS   A NZ  
790  N N   . LYS   A 29  ? 0.3726 0.3689 0.1919 -0.0677 0.1004  -0.0353 29  LYS   A N   
791  C CA  . LYS   A 29  ? 0.3902 0.3976 0.2198 -0.0706 0.1167  -0.0198 29  LYS   A CA  
792  C C   . LYS   A 29  ? 0.3793 0.3831 0.1757 -0.0798 0.1064  -0.0154 29  LYS   A C   
793  O O   . LYS   A 29  ? 0.3896 0.3930 0.1813 -0.0711 0.0950  -0.0149 29  LYS   A O   
794  C CB  . LYS   A 29  ? 0.4140 0.4388 0.3040 -0.0629 0.1355  -0.0096 29  LYS   A CB  
795  C CG  . LYS   A 29  ? 0.4375 0.4722 0.3999 -0.0561 0.1386  -0.0041 29  LYS   A CG  
796  C CD  . LYS   A 29  ? 0.4601 0.4995 0.4870 -0.0509 0.1366  -0.0026 29  LYS   A CD  
797  C CE  . LYS   A 29  ? 0.4743 0.5211 0.5469 -0.0475 0.1375  -0.0030 29  LYS   A CE  
798  N NZ  . LYS   A 29  ? 0.4800 0.5311 0.5834 -0.0457 0.1369  -0.0046 29  LYS   A NZ  
812  N N   . VAL   A 30  ? 0.3566 0.3576 0.1676 -0.0938 0.0922  -0.0155 30  VAL   A N   
813  C CA  . VAL   A 30  ? 0.3438 0.3349 0.1653 -0.1058 0.0649  0.0017  30  VAL   A CA  
814  C C   . VAL   A 30  ? 0.3440 0.3142 0.1391 -0.1015 0.0499  0.0092  30  VAL   A C   
815  O O   . VAL   A 30  ? 0.3491 0.3194 0.1355 -0.1007 0.0468  0.0170  30  VAL   A O   
816  C CB  . VAL   A 30  ? 0.3330 0.3338 0.1982 -0.1207 0.0417  0.0070  30  VAL   A CB  
817  C CG1 . VAL   A 30  ? 0.3324 0.3318 0.2136 -0.1241 0.0166  0.0096  30  VAL   A CG1 
818  C CG2 . VAL   A 30  ? 0.3304 0.3393 0.2269 -0.1239 0.0466  0.0093  30  VAL   A CG2 
828  N N   A LYS   A 31  ? 0.3368 0.2934 0.1200 -0.1020 0.0352  -0.0008 31  LYS   A N   
829  N N   B LYS   A 31  ? 0.3434 0.3064 0.1639 -0.0940 0.0366  0.0066  31  LYS   A N   
830  C CA  A LYS   A 31  ? 0.3478 0.2898 0.1280 -0.0931 0.0069  -0.0086 31  LYS   A CA  
831  C CA  B LYS   A 31  ? 0.3450 0.3012 0.1962 -0.0835 0.0193  0.0038  31  LYS   A CA  
832  C C   A LYS   A 31  ? 0.3249 0.2719 0.1030 -0.0805 0.0102  0.0278  31  LYS   A C   
833  C C   B LYS   A 31  ? 0.3245 0.2792 0.1466 -0.0795 0.0159  0.0137  31  LYS   A C   
834  O O   A LYS   A 31  ? 0.3288 0.2800 0.1152 -0.0740 -0.0107 0.0435  31  LYS   A O   
835  O O   B LYS   A 31  ? 0.3282 0.2834 0.1550 -0.0783 0.0107  0.0155  31  LYS   A O   
836  C CB  A LYS   A 31  ? 0.3888 0.3156 0.2432 -0.0863 -0.0225 -0.0333 31  LYS   A CB  
837  C CB  B LYS   A 31  ? 0.3689 0.3199 0.2863 -0.0756 0.0046  -0.0062 31  LYS   A CB  
838  C CG  A LYS   A 31  ? 0.4321 0.3455 0.3898 -0.0724 -0.0463 -0.0446 31  LYS   A CG  
839  C CG  B LYS   A 31  ? 0.3896 0.3380 0.3752 -0.0658 -0.0086 -0.0134 31  LYS   A CG  
840  C CD  A LYS   A 31  ? 0.4644 0.3676 0.5022 -0.0612 -0.0643 -0.0518 31  LYS   A CD  
841  C CD  B LYS   A 31  ? 0.4048 0.3518 0.4436 -0.0582 -0.0185 -0.0183 31  LYS   A CD  
842  C CE  A LYS   A 31  ? 0.4867 0.3860 0.5719 -0.0524 -0.0783 -0.0584 31  LYS   A CE  
843  C CE  B LYS   A 31  ? 0.4142 0.3613 0.4874 -0.0527 -0.0255 -0.0215 31  LYS   A CE  
844  N NZ  A LYS   A 31  ? 0.4975 0.3962 0.6110 -0.0474 -0.0852 -0.0617 31  LYS   A NZ  
845  N NZ  B LYS   A 31  ? 0.4188 0.3674 0.5123 -0.0500 -0.0292 -0.0230 31  LYS   A NZ  
872  N N   . PRO   A 32  ? 0.2993 0.2536 0.0948 -0.0769 0.0149  0.0196  32  PRO   A N   
873  C CA  . PRO   A 32  ? 0.2841 0.2334 0.1171 -0.0693 -0.0000 0.0209  32  PRO   A CA  
874  C C   . PRO   A 32  ? 0.2757 0.2247 0.1277 -0.0553 -0.0143 0.0349  32  PRO   A C   
875  O O   . PRO   A 32  ? 0.2672 0.2175 0.1420 -0.0597 -0.0262 0.0411  32  PRO   A O   
876  C CB  . PRO   A 32  ? 0.2787 0.2415 0.1355 -0.0701 -0.0002 0.0170  32  PRO   A CB  
877  C CG  . PRO   A 32  ? 0.2773 0.2482 0.0918 -0.0637 -0.0060 0.0114  32  PRO   A CG  
878  C CD  . PRO   A 32  ? 0.2833 0.2467 0.0879 -0.0690 0.0061  0.0202  32  PRO   A CD  
886  N N   . THR   A 33  ? 0.2819 0.2158 0.1266 -0.0462 -0.0120 0.0360  33  THR   A N   
887  C CA  . THR   A 33  ? 0.2778 0.2190 0.1401 -0.0335 -0.0244 0.0430  33  THR   A CA  
888  C C   . THR   A 33  ? 0.2462 0.1990 0.1336 -0.0350 -0.0255 0.0284  33  THR   A C   
889  O O   . THR   A 33  ? 0.2422 0.1944 0.1407 -0.0316 -0.0387 0.0355  33  THR   A O   
890  C CB  . THR   A 33  ? 0.3041 0.2429 0.1527 -0.0216 -0.0397 0.0642  33  THR   A CB  
891  O OG1 . THR   A 33  ? 0.3270 0.2555 0.1902 -0.0135 -0.0302 0.0763  33  THR   A OG1 
892  C CG2 . THR   A 33  ? 0.3087 0.2587 0.1894 -0.0157 -0.0500 0.0554  33  THR   A CG2 
900  N N   . VAL   A 34  ? 0.2145 0.1853 0.1168 -0.0374 -0.0194 0.0326  34  VAL   A N   
901  C CA  . VAL   A 34  ? 0.1938 0.1694 0.1120 -0.0318 -0.0074 0.0312  34  VAL   A CA  
902  C C   . VAL   A 34  ? 0.1823 0.1596 0.1070 -0.0286 -0.0003 0.0184  34  VAL   A C   
903  O O   . VAL   A 34  ? 0.1847 0.1636 0.1299 -0.0345 0.0009  0.0299  34  VAL   A O   
904  C CB  . VAL   A 34  ? 0.1989 0.1673 0.1424 -0.0221 -0.0063 0.0171  34  VAL   A CB  
905  C CG1 . VAL   A 34  ? 0.2042 0.1706 0.1309 -0.0223 0.0058  0.0093  34  VAL   A CG1 
906  C CG2 . VAL   A 34  ? 0.2028 0.1776 0.1714 -0.0084 -0.0197 0.0212  34  VAL   A CG2 
916  N N   . VAL   A 35  ? 0.1682 0.1497 0.1094 -0.0305 -0.0065 0.0236  35  VAL   A N   
917  C CA  . VAL   A 35  ? 0.1552 0.1460 0.1051 -0.0227 0.0006  0.0144  35  VAL   A CA  
918  C C   . VAL   A 35  ? 0.1459 0.1308 0.1111 -0.0199 0.0024  0.0129  35  VAL   A C   
919  O O   . VAL   A 35  ? 0.1417 0.1423 0.1296 -0.0241 0.0094  0.0071  35  VAL   A O   
920  C CB  . VAL   A 35  ? 0.1646 0.1587 0.1287 -0.0176 0.0076  0.0034  35  VAL   A CB  
921  C CG1 . VAL   A 35  ? 0.1727 0.1574 0.1398 -0.0092 0.0034  0.0024  35  VAL   A CG1 
922  C CG2 . VAL   A 35  ? 0.1622 0.1644 0.1433 -0.0175 0.0202  0.0025  35  VAL   A CG2 
932  N N   . VAL   A 36  ? 0.1349 0.1359 0.1111 -0.0192 0.0075  0.0171  36  VAL   A N   
933  C CA  . VAL   A 36  ? 0.1255 0.1236 0.1088 -0.0103 0.0099  0.0124  36  VAL   A CA  
934  C C   . VAL   A 36  ? 0.1236 0.1266 0.1118 -0.0157 0.0143  0.0065  36  VAL   A C   
935  O O   . VAL   A 36  ? 0.1331 0.1271 0.1443 -0.0074 0.0206  0.0127  36  VAL   A O   
936  C CB  . VAL   A 36  ? 0.1312 0.1164 0.1177 -0.0102 0.0043  0.0116  36  VAL   A CB  
937  C CG1 . VAL   A 36  ? 0.1423 0.1153 0.1358 -0.0092 0.0030  0.0050  36  VAL   A CG1 
938  C CG2 . VAL   A 36  ? 0.1419 0.1204 0.1358 -0.0121 -0.0041 0.0156  36  VAL   A CG2 
948  N N   . ASN   A 37  ? 0.1195 0.1175 0.1195 -0.0059 0.0061  0.0097  37  ASN   A N   
949  C CA  . ASN   A 37  ? 0.1211 0.1136 0.1169 0.0006  0.0053  0.0161  37  ASN   A CA  
950  C C   . ASN   A 37  ? 0.1185 0.1121 0.1238 -0.0031 0.0119  0.0194  37  ASN   A C   
951  O O   . ASN   A 37  ? 0.1305 0.1248 0.1224 0.0080  0.0124  0.0087  37  ASN   A O   
952  C CB  . ASN   A 37  ? 0.1224 0.1133 0.1289 0.0052  0.0026  0.0093  37  ASN   A CB  
953  C CG  . ASN   A 37  ? 0.1225 0.1153 0.1330 -0.0008 0.0089  0.0072  37  ASN   A CG  
954  O OD1 . ASN   A 37  ? 0.1211 0.1172 0.1590 -0.0010 0.0086  0.0164  37  ASN   A OD1 
955  N ND2 . ASN   A 37  ? 0.1250 0.1165 0.1416 -0.0037 -0.0018 0.0254  37  ASN   A ND2 
962  N N   A ALA   A 38  ? 0.1199 0.1249 0.1227 0.0033  0.0153  0.0044  38  ALA   A N   
963  N N   B ALA   A 38  ? 0.1230 0.1210 0.1219 -0.0038 0.0089  0.0113  38  ALA   A N   
964  C CA  A ALA   A 38  ? 0.1239 0.1275 0.1238 -0.0009 0.0004  0.0016  38  ALA   A CA  
965  C CA  B ALA   A 38  ? 0.1270 0.1278 0.1260 -0.0074 -0.0007 0.0093  38  ALA   A CA  
966  C C   A ALA   A 38  ? 0.1212 0.1267 0.1200 0.0028  -0.0031 0.0031  38  ALA   A C   
967  C C   B ALA   A 38  ? 0.1271 0.1262 0.1242 -0.0071 -0.0028 0.0086  38  ALA   A C   
968  O O   A ALA   A 38  ? 0.1216 0.1211 0.1330 0.0058  -0.0085 -0.0005 38  ALA   A O   
969  O O   B ALA   A 38  ? 0.1219 0.1241 0.1287 -0.0098 -0.0125 0.0118  38  ALA   A O   
970  C CB  A ALA   A 38  ? 0.1286 0.1474 0.1395 -0.0126 0.0022  0.0061  38  ALA   A CB  
971  C CB  B ALA   A 38  ? 0.1299 0.1358 0.1357 -0.0089 -0.0052 0.0041  38  ALA   A CB  
982  N N   A ALA   A 39  ? 0.1171 0.1196 0.1331 0.0035  0.0023  0.0079  39  ALA   A N   
983  N N   B ALA   A 39  ? 0.1310 0.1264 0.1274 -0.0061 0.0072  0.0122  39  ALA   A N   
984  C CA  A ALA   A 39  ? 0.1196 0.1183 0.1287 0.0051  0.0030  0.0012  39  ALA   A CA  
985  C CA  B ALA   A 39  ? 0.1354 0.1304 0.1293 -0.0066 0.0127  0.0097  39  ALA   A CA  
986  C C   A ALA   A 39  ? 0.1218 0.1155 0.1238 0.0028  0.0012  0.0013  39  ALA   A C   
987  C C   B ALA   A 39  ? 0.1323 0.1251 0.1225 -0.0080 0.0144  0.0049  39  ALA   A C   
988  O O   A ALA   A 39  ? 0.1324 0.1196 0.1295 -0.0018 0.0082  0.0043  39  ALA   A O   
989  O O   B ALA   A 39  ? 0.1332 0.1270 0.1214 -0.0126 0.0180  0.0070  39  ALA   A O   
990  C CB  A ALA   A 39  ? 0.1173 0.1220 0.1376 0.0091  -0.0045 -0.0043 39  ALA   A CB  
991  C CB  B ALA   A 39  ? 0.1409 0.1347 0.1410 -0.0039 0.0156  0.0056  39  ALA   A CB  
1002 N N   . ASN   A 40  ? 0.1352 0.1212 0.1248 -0.0082 0.0197  0.0019  40  ASN   A N   
1003 C CA  . ASN   A 40  ? 0.1411 0.1161 0.1284 0.0023  0.0138  0.0035  40  ASN   A CA  
1004 C C   . ASN   A 40  ? 0.1468 0.1087 0.1221 -0.0064 0.0259  0.0107  40  ASN   A C   
1005 O O   . ASN   A 40  ? 0.1400 0.1127 0.1283 -0.0070 0.0193  0.0130  40  ASN   A O   
1006 C CB  . ASN   A 40  ? 0.1540 0.1207 0.1475 0.0051  0.0022  0.0085  40  ASN   A CB  
1007 C CG  . ASN   A 40  ? 0.1591 0.1200 0.1717 0.0032  -0.0015 0.0113  40  ASN   A CG  
1008 O OD1 . ASN   A 40  ? 0.1700 0.1285 0.1975 0.0020  -0.0077 0.0028  40  ASN   A OD1 
1009 N ND2 . ASN   A 40  ? 0.1627 0.1349 0.1878 0.0041  -0.0015 -0.0003 40  ASN   A ND2 
1017 N N   A VAL   A 41  ? 0.1539 0.1153 0.1253 -0.0103 0.0302  0.0096  41  VAL   A N   
1018 N N   B VAL   A 41  ? 0.1521 0.1110 0.1202 -0.0071 0.0292  0.0105  41  VAL   A N   
1019 C CA  A VAL   A 41  ? 0.1561 0.1204 0.1425 -0.0071 0.0325  0.0050  41  VAL   A CA  
1020 C CA  B VAL   A 41  ? 0.1528 0.1130 0.1272 -0.0072 0.0323  0.0099  41  VAL   A CA  
1021 C C   A VAL   A 41  ? 0.1475 0.1200 0.1548 -0.0042 0.0299  0.0074  41  VAL   A C   
1022 C C   B VAL   A 41  ? 0.1490 0.1107 0.1322 -0.0070 0.0288  0.0082  41  VAL   A C   
1023 O O   A VAL   A 41  ? 0.1495 0.1183 0.1788 -0.0004 0.0304  -0.0012 41  VAL   A O   
1024 O O   B VAL   A 41  ? 0.1494 0.1068 0.1360 -0.0047 0.0287  0.0021  41  VAL   A O   
1025 C CB  A VAL   A 41  ? 0.1696 0.1343 0.1475 -0.0075 0.0369  0.0020  41  VAL   A CB  
1026 C CB  B VAL   A 41  ? 0.1577 0.1199 0.1329 -0.0075 0.0388  0.0096  41  VAL   A CB  
1027 C CG1 A VAL   A 41  ? 0.1846 0.1438 0.1515 -0.0100 0.0395  -0.0066 41  VAL   A CG1 
1028 C CG1 B VAL   A 41  ? 0.1682 0.1247 0.1412 -0.0078 0.0423  0.0043  41  VAL   A CG1 
1029 C CG2 A VAL   A 41  ? 0.1806 0.1435 0.1422 -0.0143 0.0439  -0.0016 41  VAL   A CG2 
1030 C CG2 B VAL   A 41  ? 0.1535 0.1226 0.1277 -0.0123 0.0395  0.0141  41  VAL   A CG2 
1049 N N   A TYR   A 42  ? 0.1378 0.1124 0.1654 -0.0054 0.0324  0.0197  42  TYR   A N   
1050 N N   B TYR   A 42  ? 0.1447 0.1109 0.1401 -0.0091 0.0264  0.0147  42  TYR   A N   
1051 C CA  A TYR   A 42  ? 0.1375 0.1102 0.1660 -0.0013 0.0285  0.0178  42  TYR   A CA  
1052 C CA  B TYR   A 42  ? 0.1423 0.1132 0.1464 -0.0091 0.0247  0.0154  42  TYR   A CA  
1053 C C   A TYR   A 42  ? 0.1304 0.1125 0.1605 -0.0005 0.0218  0.0205  42  TYR   A C   
1054 C C   B TYR   A 42  ? 0.1385 0.1134 0.1439 -0.0090 0.0215  0.0145  42  TYR   A C   
1055 O O   A TYR   A 42  ? 0.1286 0.1149 0.1881 -0.0127 0.0166  0.0052  42  TYR   A O   
1056 O O   B TYR   A 42  ? 0.1375 0.1157 0.1484 -0.0139 0.0229  0.0111  42  TYR   A O   
1057 C CB  A TYR   A 42  ? 0.1497 0.1239 0.1604 -0.0028 0.0268  0.0252  42  TYR   A CB  
1058 C CB  B TYR   A 42  ? 0.1448 0.1213 0.1535 -0.0091 0.0280  0.0146  42  TYR   A CB  
1059 C CG  A TYR   A 42  ? 0.1666 0.1385 0.1624 0.0007  0.0177  0.0320  42  TYR   A CG  
1060 C CG  B TYR   A 42  ? 0.1445 0.1292 0.1530 -0.0085 0.0274  0.0142  42  TYR   A CG  
1061 C CD1 A TYR   A 42  ? 0.1740 0.1506 0.1621 -0.0022 0.0247  0.0345  42  TYR   A CD1 
1062 C CD1 B TYR   A 42  ? 0.1493 0.1396 0.1571 -0.0090 0.0270  0.0038  42  TYR   A CD1 
1063 C CD2 A TYR   A 42  ? 0.1717 0.1635 0.1818 0.0089  0.0190  0.0191  42  TYR   A CD2 
1064 C CD2 B TYR   A 42  ? 0.1440 0.1362 0.1505 -0.0041 0.0248  0.0129  42  TYR   A CD2 
1065 C CE1 A TYR   A 42  ? 0.1746 0.1637 0.1574 -0.0028 0.0313  0.0305  42  TYR   A CE1 
1066 C CE1 B TYR   A 42  ? 0.1506 0.1458 0.1528 -0.0100 0.0245  0.0020  42  TYR   A CE1 
1067 C CE2 A TYR   A 42  ? 0.1818 0.1753 0.1902 0.0039  0.0161  0.0168  42  TYR   A CE2 
1068 C CE2 B TYR   A 42  ? 0.1452 0.1419 0.1498 -0.0077 0.0241  0.0107  42  TYR   A CE2 
1069 C CZ  A TYR   A 42  ? 0.1849 0.1766 0.1752 -0.0051 0.0274  0.0215  42  TYR   A CZ  
1070 C CZ  B TYR   A 42  ? 0.1490 0.1454 0.1466 -0.0076 0.0219  0.0056  42  TYR   A CZ  
1071 O OH  A TYR   A 42  ? 0.1949 0.2033 0.1975 -0.0150 0.0265  0.0180  42  TYR   A OH  
1072 O OH  B TYR   A 42  ? 0.1522 0.1527 0.1553 -0.0024 0.0167  0.0024  42  TYR   A OH  
1091 N N   . LEU   A 43  ? 0.1386 0.1113 0.1500 -0.0105 0.0178  0.0079  43  LEU   A N   
1092 C CA  . LEU   A 43  ? 0.1264 0.1123 0.1496 -0.0065 0.0175  0.0064  43  LEU   A CA  
1093 C C   . LEU   A 43  ? 0.1264 0.1156 0.1461 -0.0012 0.0106  0.0034  43  LEU   A C   
1094 O O   . LEU   A 43  ? 0.1470 0.1203 0.1633 0.0041  -0.0045 -0.0012 43  LEU   A O   
1095 C CB  . LEU   A 43  ? 0.1321 0.1110 0.1543 -0.0095 0.0095  0.0049  43  LEU   A CB  
1096 C CG  . LEU   A 43  ? 0.1356 0.1105 0.1631 -0.0048 0.0072  0.0050  43  LEU   A CG  
1097 C CD1 . LEU   A 43  ? 0.1463 0.1295 0.1786 -0.0024 -0.0021 0.0107  43  LEU   A CD1 
1098 C CD2 . LEU   A 43  ? 0.1495 0.1207 0.1702 -0.0027 0.0087  0.0100  43  LEU   A CD2 
1111 N N   A LYS   A 44  ? 0.1301 0.1125 0.1418 -0.0030 0.0087  0.0079  44  LYS   A N   
1112 N N   B LYS   A 44  ? 0.1424 0.1329 0.1508 -0.0004 0.0103  0.0036  44  LYS   A N   
1113 C CA  A LYS   A 44  ? 0.1398 0.1080 0.1486 -0.0069 0.0109  0.0222  44  LYS   A CA  
1114 C CA  B LYS   A 44  ? 0.1591 0.1501 0.1650 0.0006  0.0091  0.0030  44  LYS   A CA  
1115 C C   A LYS   A 44  ? 0.1269 0.1099 0.1382 0.0026  0.0038  0.0137  44  LYS   A C   
1116 C C   B LYS   A 44  ? 0.1574 0.1515 0.1460 0.0042  0.0069  -0.0001 44  LYS   A C   
1117 O O   A LYS   A 44  ? 0.1393 0.1259 0.1555 -0.0014 0.0060  0.0039  44  LYS   A O   
1118 O O   B LYS   A 44  ? 0.1596 0.1549 0.1406 0.0043  0.0084  -0.0033 44  LYS   A O   
1119 C CB  A LYS   A 44  ? 0.1674 0.1200 0.1952 -0.0003 0.0259  0.0343  44  LYS   A CB  
1120 C CB  B LYS   A 44  ? 0.1775 0.1680 0.2018 0.0030  0.0116  0.0028  44  LYS   A CB  
1121 C CG  A LYS   A 44  ? 0.1981 0.1454 0.2754 -0.0078 0.0467  0.0447  44  LYS   A CG  
1122 C CG  B LYS   A 44  ? 0.1957 0.1832 0.2438 0.0054  0.0156  0.0028  44  LYS   A CG  
1123 C CD  A LYS   A 44  ? 0.2407 0.2059 0.3978 -0.0084 0.0315  0.0328  44  LYS   A CD  
1124 C CD  B LYS   A 44  ? 0.2152 0.2025 0.2966 0.0094  0.0101  0.0010  44  LYS   A CD  
1125 C CE  A LYS   A 44  ? 0.2601 0.2378 0.4803 -0.0075 0.0244  0.0263  44  LYS   A CE  
1126 C CE  B LYS   A 44  ? 0.2238 0.2096 0.3308 0.0141  0.0100  -0.0011 44  LYS   A CE  
1127 N NZ  A LYS   A 44  ? 0.2677 0.2618 0.5176 -0.0129 0.0236  0.0245  44  LYS   A NZ  
1128 N NZ  B LYS   A 44  ? 0.2235 0.2063 0.3408 0.0180  0.0088  -0.0013 44  LYS   A NZ  
1155 N N   A HIS   A 45  ? 0.1181 0.1075 0.1421 0.0019  0.0029  0.0200  45  HIS   A N   
1156 N N   B HIS   A 45  ? 0.1571 0.1529 0.1476 0.0058  0.0048  0.0005  45  HIS   A N   
1157 C CA  A HIS   A 45  ? 0.1192 0.1099 0.1421 -0.0005 0.0003  0.0134  45  HIS   A CA  
1158 C CA  B HIS   A 45  ? 0.1579 0.1539 0.1502 0.0048  0.0016  -0.0032 45  HIS   A CA  
1159 C C   A HIS   A 45  ? 0.1261 0.1165 0.1599 0.0058  -0.0005 0.0192  45  HIS   A C   
1160 C C   B HIS   A 45  ? 0.1636 0.1595 0.1680 0.0070  0.0066  -0.0051 45  HIS   A C   
1161 O O   A HIS   A 45  ? 0.1353 0.1206 0.1925 0.0108  0.0027  -0.0017 45  HIS   A O   
1162 O O   B HIS   A 45  ? 0.1683 0.1574 0.1920 0.0051  0.0049  -0.0103 45  HIS   A O   
1163 C CB  A HIS   A 45  ? 0.1210 0.1097 0.1412 0.0052  0.0130  0.0088  45  HIS   A CB  
1164 C CB  B HIS   A 45  ? 0.1529 0.1492 0.1406 0.0060  -0.0049 -0.0042 45  HIS   A CB  
1165 C CG  A HIS   A 45  ? 0.1209 0.1111 0.1308 -0.0035 0.0083  0.0124  45  HIS   A CG  
1166 C CG  B HIS   A 45  ? 0.1451 0.1449 0.1250 0.0033  -0.0052 -0.0026 45  HIS   A CG  
1167 N ND1 A HIS   A 45  ? 0.1168 0.1136 0.1451 -0.0007 0.0114  0.0074  45  HIS   A ND1 
1168 N ND1 B HIS   A 45  ? 0.1406 0.1428 0.1264 0.0042  -0.0094 0.0035  45  HIS   A ND1 
1169 C CD2 A HIS   A 45  ? 0.1197 0.1175 0.1469 -0.0120 0.0011  0.0215  45  HIS   A CD2 
1170 C CD2 B HIS   A 45  ? 0.1404 0.1399 0.1182 0.0013  -0.0053 -0.0075 45  HIS   A CD2 
1171 C CE1 A HIS   A 45  ? 0.1160 0.1197 0.1430 -0.0102 0.0047  0.0170  45  HIS   A CE1 
1172 C CE1 B HIS   A 45  ? 0.1376 0.1360 0.1112 0.0003  -0.0113 -0.0054 45  HIS   A CE1 
1173 N NE2 A HIS   A 45  ? 0.1183 0.1229 0.1454 -0.0036 0.0056  0.0295  45  HIS   A NE2 
1174 N NE2 B HIS   A 45  ? 0.1373 0.1368 0.1093 -0.0001 -0.0076 -0.0111 45  HIS   A NE2 
1189 N N   A GLY   A 46  ? 0.1362 0.1408 0.1715 0.0189  -0.0105 0.0256  46  GLY   A N   
1190 N N   B GLY   A 46  ? 0.1668 0.1661 0.1648 0.0119  0.0088  0.0018  46  GLY   A N   
1191 C CA  A GLY   A 46  ? 0.1451 0.1466 0.1947 0.0253  -0.0095 0.0313  46  GLY   A CA  
1192 C CA  B GLY   A 46  ? 0.1633 0.1663 0.1573 0.0130  0.0113  0.0072  46  GLY   A CA  
1193 C C   A GLY   A 46  ? 0.1499 0.1396 0.1882 0.0309  -0.0180 0.0391  46  GLY   A C   
1194 C C   B GLY   A 46  ? 0.1587 0.1595 0.1414 0.0131  0.0082  0.0035  46  GLY   A C   
1195 O O   A GLY   A 46  ? 0.1406 0.1439 0.2015 0.0237  -0.0229 0.0281  46  GLY   A O   
1196 O O   B GLY   A 46  ? 0.1539 0.1598 0.1366 0.0113  0.0109  0.0003  46  GLY   A O   
1203 N N   A GLY   A 47  ? 0.1581 0.1381 0.1867 0.0296  -0.0304 0.0223  47  GLY   A N   
1204 N N   B GLY   A 47  ? 0.1610 0.1546 0.1440 0.0122  -0.0027 -0.0037 47  GLY   A N   
1205 C CA  A GLY   A 47  ? 0.1696 0.1471 0.1938 0.0254  -0.0475 0.0119  47  GLY   A CA  
1206 C CA  B GLY   A 47  ? 0.1605 0.1515 0.1511 0.0097  -0.0162 -0.0119 47  GLY   A CA  
1207 C C   A GLY   A 47  ? 0.1626 0.1333 0.1727 0.0320  -0.0436 0.0041  47  GLY   A C   
1208 C C   B GLY   A 47  ? 0.1542 0.1456 0.1553 0.0117  -0.0194 -0.0116 47  GLY   A C   
1209 O O   A GLY   A 47  ? 0.1621 0.1342 0.1686 0.0335  -0.0272 0.0126  47  GLY   A O   
1210 O O   B GLY   A 47  ? 0.1542 0.1462 0.1610 0.0116  -0.0162 -0.0063 47  GLY   A O   
1217 N N   A GLY   A 48  ? 0.1621 0.1411 0.1768 0.0300  -0.0444 0.0012  48  GLY   A N   
1218 N N   B GLY   A 48  ? 0.1483 0.1444 0.1556 0.0170  -0.0217 -0.0105 48  GLY   A N   
1219 C CA  A GLY   A 48  ? 0.1522 0.1376 0.1784 0.0187  -0.0389 -0.0056 48  GLY   A CA  
1220 C CA  B GLY   A 48  ? 0.1403 0.1434 0.1511 0.0129  -0.0195 -0.0112 48  GLY   A CA  
1221 C C   A GLY   A 48  ? 0.1379 0.1357 0.1644 0.0121  -0.0098 -0.0040 48  GLY   A C   
1222 C C   B GLY   A 48  ? 0.1295 0.1439 0.1423 0.0132  -0.0107 -0.0054 48  GLY   A C   
1223 O O   A GLY   A 48  ? 0.1525 0.1323 0.1749 0.0135  -0.0132 -0.0050 48  GLY   A O   
1224 O O   B GLY   A 48  ? 0.1356 0.1456 0.1421 0.0143  -0.0121 -0.0079 48  GLY   A O   
1231 N N   A VAL   A 49  ? 0.1144 0.1292 0.1676 0.0029  -0.0105 -0.0046 49  VAL   A N   
1232 N N   B VAL   A 49  ? 0.1196 0.1422 0.1430 0.0060  -0.0086 -0.0003 49  VAL   A N   
1233 C CA  A VAL   A 49  ? 0.1274 0.1277 0.1573 -0.0035 0.0135  0.0017  49  VAL   A CA  
1234 C CA  B VAL   A 49  ? 0.1099 0.1429 0.1350 0.0087  -0.0017 0.0104  49  VAL   A CA  
1235 C C   A VAL   A 49  ? 0.1262 0.1106 0.1405 0.0024  0.0071  0.0047  49  VAL   A C   
1236 C C   B VAL   A 49  ? 0.1113 0.1354 0.1143 0.0150  0.0056  -0.0011 49  VAL   A C   
1237 O O   A VAL   A 49  ? 0.1317 0.1208 0.1441 -0.0123 0.0157  -0.0014 49  VAL   A O   
1238 O O   B VAL   A 49  ? 0.1146 0.1393 0.1097 0.0221  0.0063  0.0025  49  VAL   A O   
1239 C CB  A VAL   A 49  ? 0.1480 0.1309 0.1831 -0.0103 0.0054  0.0008  49  VAL   A CB  
1240 C CB  B VAL   A 49  ? 0.0974 0.1400 0.1433 0.0071  -0.0091 0.0241  49  VAL   A CB  
1241 C CG1 A VAL   A 49  ? 0.1639 0.1275 0.2007 -0.0081 0.0023  0.0065  49  VAL   A CG1 
1242 C CG1 B VAL   A 49  ? 0.0801 0.1343 0.1446 0.0146  -0.0120 0.0303  49  VAL   A CG1 
1243 C CG2 A VAL   A 49  ? 0.1621 0.1534 0.2326 -0.0230 -0.0008 0.0032  49  VAL   A CG2 
1244 C CG2 B VAL   A 49  ? 0.0993 0.1456 0.1509 0.0028  -0.0062 0.0341  49  VAL   A CG2 
1263 N N   A ALA   A 50  ? 0.1185 0.1100 0.1416 -0.0064 -0.0137 0.0114  50  ALA   A N   
1264 N N   B ALA   A 50  ? 0.1191 0.1295 0.1033 0.0127  0.0107  -0.0050 50  ALA   A N   
1265 C CA  A ALA   A 50  ? 0.1145 0.1087 0.1483 -0.0093 -0.0011 0.0143  50  ALA   A CA  
1266 C CA  B ALA   A 50  ? 0.1263 0.1245 0.1044 0.0079  0.0037  -0.0067 50  ALA   A CA  
1267 C C   A ALA   A 50  ? 0.1080 0.1153 0.1410 -0.0090 -0.0009 0.0117  50  ALA   A C   
1268 C C   B ALA   A 50  ? 0.1293 0.1216 0.1017 0.0082  0.0017  -0.0102 50  ALA   A C   
1269 O O   A ALA   A 50  ? 0.1147 0.1168 0.1565 -0.0023 -0.0046 0.0074  50  ALA   A O   
1270 O O   B ALA   A 50  ? 0.1304 0.1157 0.0985 0.0055  0.0076  -0.0104 50  ALA   A O   
1271 C CB  A ALA   A 50  ? 0.1162 0.1058 0.1409 -0.0052 0.0000  0.0025  50  ALA   A CB  
1272 C CB  B ALA   A 50  ? 0.1287 0.1215 0.1032 0.0081  0.0057  -0.0061 50  ALA   A CB  
1283 N N   A GLY   A 51  ? 0.1179 0.1053 0.1539 0.0023  -0.0030 0.0055  51  GLY   A N   
1284 N N   B GLY   A 51  ? 0.1324 0.1205 0.1164 0.0086  -0.0049 -0.0127 51  GLY   A N   
1285 C CA  A GLY   A 51  ? 0.1319 0.1087 0.1660 0.0057  -0.0108 0.0093  51  GLY   A CA  
1286 C CA  B GLY   A 51  ? 0.1353 0.1235 0.1300 0.0084  -0.0056 -0.0107 51  GLY   A CA  
1287 C C   A GLY   A 51  ? 0.1255 0.1166 0.1579 0.0056  0.0005  -0.0010 51  GLY   A C   
1288 C C   B GLY   A 51  ? 0.1322 0.1272 0.1373 0.0069  -0.0012 -0.0111 51  GLY   A C   
1289 O O   A GLY   A 51  ? 0.1305 0.1215 0.1709 0.0009  -0.0031 -0.0111 51  GLY   A O   
1290 O O   B GLY   A 51  ? 0.1357 0.1298 0.1409 0.0046  -0.0070 -0.0157 51  GLY   A O   
1297 N N   . ALA   A 52  ? 0.1282 0.1292 0.1485 0.0055  0.0082  -0.0097 52  ALA   A N   
1298 C CA  . ALA   A 52  ? 0.1274 0.1391 0.1616 0.0003  0.0102  -0.0125 52  ALA   A CA  
1299 C C   . ALA   A 52  ? 0.1216 0.1357 0.1394 -0.0098 0.0118  -0.0108 52  ALA   A C   
1300 O O   . ALA   A 52  ? 0.1358 0.1442 0.1614 -0.0034 0.0119  -0.0154 52  ALA   A O   
1301 C CB  . ALA   A 52  ? 0.1317 0.1680 0.1804 -0.0112 0.0107  -0.0172 52  ALA   A CB  
1308 N N   A LEU   A 53  ? 0.1233 0.1280 0.1362 -0.0026 0.0079  -0.0073 53  LEU   A N   
1309 N N   B LEU   A 53  ? 0.1250 0.1360 0.1310 -0.0090 0.0057  -0.0074 53  LEU   A N   
1310 C CA  A LEU   A 53  ? 0.1354 0.1328 0.1387 -0.0065 0.0125  0.0016  53  LEU   A CA  
1311 C CA  B LEU   A 53  ? 0.1287 0.1395 0.1268 -0.0101 0.0021  -0.0048 53  LEU   A CA  
1312 C C   A LEU   A 53  ? 0.1387 0.1369 0.1206 0.0012  0.0109  0.0029  53  LEU   A C   
1313 C C   B LEU   A 53  ? 0.1313 0.1399 0.1149 -0.0056 0.0026  -0.0028 53  LEU   A C   
1314 O O   A LEU   A 53  ? 0.1524 0.1488 0.1357 -0.0087 0.0105  0.0024  53  LEU   A O   
1315 O O   B LEU   A 53  ? 0.1368 0.1417 0.1093 -0.0056 -0.0001 -0.0035 53  LEU   A O   
1316 C CB  A LEU   A 53  ? 0.1476 0.1326 0.1410 -0.0087 0.0186  0.0071  53  LEU   A CB  
1317 C CB  B LEU   A 53  ? 0.1303 0.1412 0.1269 -0.0157 -0.0047 -0.0029 53  LEU   A CB  
1318 C CG  A LEU   A 53  ? 0.1631 0.1346 0.1498 -0.0123 0.0148  0.0075  53  LEU   A CG  
1319 C CG  B LEU   A 53  ? 0.1345 0.1436 0.1270 -0.0201 -0.0119 -0.0049 53  LEU   A CG  
1320 C CD1 A LEU   A 53  ? 0.1647 0.1373 0.1486 -0.0050 -0.0047 0.0106  53  LEU   A CD1 
1321 C CD1 B LEU   A 53  ? 0.1273 0.1406 0.1065 -0.0212 -0.0253 -0.0163 53  LEU   A CD1 
1322 C CD2 A LEU   A 53  ? 0.1899 0.1458 0.1564 -0.0188 0.0223  0.0102  53  LEU   A CD2 
1323 C CD2 B LEU   A 53  ? 0.1487 0.1497 0.1425 -0.0247 -0.0065 -0.0003 53  LEU   A CD2 
1346 N N   A ASN   A 54  ? 0.1266 0.1250 0.1195 -0.0051 0.0053  0.0014  54  ASN   A N   
1347 N N   B ASN   A 54  ? 0.1275 0.1379 0.1157 -0.0048 0.0051  -0.0011 54  ASN   A N   
1348 C CA  A ASN   A 54  ? 0.1184 0.1204 0.1373 -0.0028 -0.0057 0.0018  54  ASN   A CA  
1349 C CA  B ASN   A 54  ? 0.1258 0.1363 0.1174 -0.0040 0.0047  0.0021  54  ASN   A CA  
1350 C C   A ASN   A 54  ? 0.1267 0.1262 0.1442 -0.0110 -0.0036 -0.0009 54  ASN   A C   
1351 C C   B ASN   A 54  ? 0.1304 0.1341 0.1268 -0.0068 0.0008  -0.0009 54  ASN   A C   
1352 O O   A ASN   A 54  ? 0.1274 0.1322 0.1488 -0.0057 0.0011  -0.0051 54  ASN   A O   
1353 O O   B ASN   A 54  ? 0.1313 0.1347 0.1279 -0.0080 -0.0007 0.0012  54  ASN   A O   
1354 C CB  A ASN   A 54  ? 0.1115 0.1181 0.1575 -0.0052 -0.0094 -0.0057 54  ASN   A CB  
1355 C CB  B ASN   A 54  ? 0.1260 0.1395 0.1219 -0.0004 0.0091  0.0053  54  ASN   A CB  
1356 C CG  A ASN   A 54  ? 0.1169 0.1133 0.1495 -0.0002 -0.0072 -0.0040 54  ASN   A CG  
1357 C CG  B ASN   A 54  ? 0.1272 0.1418 0.1249 0.0058  0.0105  0.0052  54  ASN   A CG  
1358 O OD1 A ASN   A 54  ? 0.1150 0.1146 0.1324 -0.0057 -0.0042 0.0011  54  ASN   A OD1 
1359 O OD1 B ASN   A 54  ? 0.1270 0.1469 0.1313 0.0026  0.0159  0.0050  54  ASN   A OD1 
1360 N ND2 A ASN   A 54  ? 0.1207 0.1235 0.1789 -0.0090 -0.0218 0.0053  54  ASN   A ND2 
1361 N ND2 B ASN   A 54  ? 0.1295 0.1421 0.1284 0.0092  0.0053  0.0077  54  ASN   A ND2 
1374 N N   . LYS   A 55  ? 0.1308 0.1320 0.1403 -0.0020 -0.0020 -0.0103 55  LYS   A N   
1375 C CA  . LYS   A 55  ? 0.1406 0.1397 0.1491 0.0032  -0.0027 -0.0164 55  LYS   A CA  
1376 C C   . LYS   A 55  ? 0.1375 0.1450 0.1522 -0.0027 0.0080  -0.0225 55  LYS   A C   
1377 O O   . LYS   A 55  ? 0.1486 0.1531 0.1638 0.0049  0.0001  -0.0299 55  LYS   A O   
1378 C CB  . LYS   A 55  ? 0.1492 0.1466 0.1718 0.0121  -0.0041 -0.0188 55  LYS   A CB  
1379 C CG  . LYS   A 55  ? 0.1572 0.1752 0.1860 0.0236  -0.0133 -0.0278 55  LYS   A CG  
1380 C CD  . LYS   A 55  ? 0.1699 0.2059 0.1958 0.0371  -0.0093 -0.0260 55  LYS   A CD  
1381 C CE  . LYS   A 55  ? 0.1936 0.2412 0.2133 0.0459  -0.0210 -0.0289 55  LYS   A CE  
1382 N NZ  . LYS   A 55  ? 0.2051 0.2552 0.2180 0.0520  -0.0217 -0.0232 55  LYS   A NZ  
1397 N N   . ALA   A 56  ? 0.1381 0.1534 0.1469 -0.0078 0.0125  -0.0234 56  ALA   A N   
1398 C CA  . ALA   A 56  ? 0.1531 0.1687 0.1524 -0.0095 0.0159  -0.0137 56  ALA   A CA  
1399 C C   . ALA   A 56  ? 0.1579 0.1793 0.1317 -0.0089 0.0153  -0.0195 56  ALA   A C   
1400 O O   . ALA   A 56  ? 0.1645 0.2143 0.1449 0.0036  0.0195  -0.0178 56  ALA   A O   
1401 C CB  . ALA   A 56  ? 0.1641 0.1906 0.1699 -0.0212 0.0113  -0.0085 56  ALA   A CB  
1407 N N   . THR   A 57  ? 0.1430 0.1606 0.1342 -0.0050 0.0129  -0.0163 57  THR   A N   
1408 C CA  . THR   A 57  ? 0.1487 0.1519 0.1359 -0.0096 -0.0047 -0.0132 57  THR   A CA  
1409 C C   . THR   A 57  ? 0.1501 0.1576 0.1406 -0.0031 -0.0057 -0.0196 57  THR   A C   
1410 O O   . THR   A 57  ? 0.1446 0.1633 0.1639 -0.0053 -0.0071 -0.0287 57  THR   A O   
1411 C CB  . THR   A 57  ? 0.1478 0.1495 0.1357 -0.0035 0.0019  -0.0117 57  THR   A CB  
1412 O OG1 . THR   A 57  ? 0.1382 0.1442 0.1451 -0.0049 0.0033  -0.0093 57  THR   A OG1 
1413 C CG2 . THR   A 57  ? 0.1516 0.1605 0.1256 -0.0051 0.0011  -0.0015 57  THR   A CG2 
1421 N N   . ASN   A 58  ? 0.1530 0.1571 0.1587 -0.0060 0.0034  -0.0308 58  ASN   A N   
1422 C CA  . ASN   A 58  ? 0.1667 0.1483 0.1778 -0.0075 0.0109  -0.0409 58  ASN   A CA  
1423 C C   . ASN   A 58  ? 0.1439 0.1395 0.1652 0.0001  -0.0033 -0.0282 58  ASN   A C   
1424 O O   . ASN   A 58  ? 0.1448 0.1523 0.1885 -0.0153 -0.0041 -0.0339 58  ASN   A O   
1425 C CB  . ASN   A 58  ? 0.2135 0.1731 0.2296 -0.0176 0.0389  -0.0539 58  ASN   A CB  
1426 C CG  . ASN   A 58  ? 0.2545 0.1941 0.3095 -0.0147 0.0496  -0.0447 58  ASN   A CG  
1427 O OD1 . ASN   A 58  ? 0.2812 0.1883 0.3397 0.0157  0.0807  -0.0428 58  ASN   A OD1 
1428 N ND2 . ASN   A 58  ? 0.2648 0.2031 0.3367 -0.0172 0.0350  -0.0458 58  ASN   A ND2 
1435 N N   . ASN   A 59  ? 0.1274 0.1327 0.1591 -0.0041 -0.0099 -0.0209 59  ASN   A N   
1436 C CA  . ASN   A 59  ? 0.1300 0.1222 0.1666 -0.0040 -0.0053 -0.0116 59  ASN   A CA  
1437 C C   . ASN   A 59  ? 0.1289 0.1219 0.1534 -0.0039 -0.0056 -0.0063 59  ASN   A C   
1438 O O   . ASN   A 59  ? 0.1286 0.1279 0.1537 -0.0034 -0.0010 -0.0040 59  ASN   A O   
1439 C CB  . ASN   A 59  ? 0.1319 0.1210 0.1753 0.0035  -0.0215 -0.0150 59  ASN   A CB  
1440 C CG  . ASN   A 59  ? 0.1361 0.1259 0.1659 -0.0010 -0.0275 -0.0001 59  ASN   A CG  
1441 O OD1 . ASN   A 59  ? 0.1556 0.1315 0.1638 -0.0119 -0.0303 0.0065  59  ASN   A OD1 
1442 N ND2 . ASN   A 59  ? 0.1496 0.1337 0.1782 -0.0101 -0.0181 -0.0005 59  ASN   A ND2 
1449 N N   . ALA   A 60  ? 0.1296 0.1276 0.1477 -0.0011 -0.0063 -0.0050 60  ALA   A N   
1450 C CA  . ALA   A 60  ? 0.1311 0.1301 0.1594 -0.0013 -0.0104 -0.0095 60  ALA   A CA  
1451 C C   . ALA   A 60  ? 0.1312 0.1248 0.1601 -0.0001 -0.0054 -0.0080 60  ALA   A C   
1452 O O   . ALA   A 60  ? 0.1261 0.1272 0.1780 0.0005  -0.0076 -0.0083 60  ALA   A O   
1453 C CB  . ALA   A 60  ? 0.1442 0.1471 0.1539 -0.0009 -0.0152 -0.0163 60  ALA   A CB  
1459 N N   . MET   A 61  ? 0.1291 0.1229 0.1480 -0.0021 0.0002  -0.0095 61  MET   A N   
1460 C CA  . MET   A 61  ? 0.1310 0.1196 0.1408 -0.0054 0.0038  -0.0017 61  MET   A CA  
1461 C C   . MET   A 61  ? 0.1234 0.1149 0.1430 -0.0034 -0.0018 -0.0074 61  MET   A C   
1462 O O   . MET   A 61  ? 0.1314 0.1155 0.1547 -0.0015 0.0061  -0.0038 61  MET   A O   
1463 C CB  . MET   A 61  ? 0.1326 0.1211 0.1389 -0.0035 0.0028  -0.0068 61  MET   A CB  
1464 C CG  . MET   A 61  ? 0.1336 0.1330 0.1538 0.0043  0.0035  -0.0034 61  MET   A CG  
1465 S SD  . MET   A 61  ? 0.1393 0.1312 0.1849 -0.0115 -0.0012 -0.0207 61  MET   A SD  
1466 C CE  . MET   A 61  ? 0.1594 0.1489 0.2110 -0.0118 0.0158  -0.0108 61  MET   A CE  
1476 N N   . GLN   A 62  ? 0.1249 0.1151 0.1397 -0.0045 0.0011  -0.0095 62  GLN   A N   
1477 C CA  . GLN   A 62  ? 0.1302 0.1123 0.1456 -0.0044 0.0025  -0.0020 62  GLN   A CA  
1478 C C   . GLN   A 62  ? 0.1290 0.1087 0.1629 -0.0027 0.0113  -0.0013 62  GLN   A C   
1479 O O   . GLN   A 62  ? 0.1279 0.1205 0.1622 -0.0004 0.0063  0.0014  62  GLN   A O   
1480 C CB  . GLN   A 62  ? 0.1286 0.1088 0.1548 0.0001  -0.0031 0.0027  62  GLN   A CB  
1481 C CG  . GLN   A 62  ? 0.1333 0.1057 0.1561 -0.0038 -0.0025 0.0150  62  GLN   A CG  
1482 C CD  . GLN   A 62  ? 0.1402 0.1107 0.1480 -0.0008 0.0035  0.0098  62  GLN   A CD  
1483 O OE1 . GLN   A 62  ? 0.1433 0.1271 0.1584 -0.0041 0.0012  0.0045  62  GLN   A OE1 
1484 N NE2 . GLN   A 62  ? 0.1461 0.1185 0.1709 0.0033  0.0002  -0.0060 62  GLN   A NE2 
1493 N N   . VAL   A 63  ? 0.1221 0.1169 0.1739 -0.0022 0.0104  -0.0188 63  VAL   A N   
1494 C CA  . VAL   A 63  ? 0.1256 0.1248 0.1902 -0.0124 0.0017  -0.0175 63  VAL   A CA  
1495 C C   . VAL   A 63  ? 0.1199 0.1228 0.1792 -0.0127 -0.0075 -0.0178 63  VAL   A C   
1496 O O   . VAL   A 63  ? 0.1183 0.1226 0.1954 -0.0159 -0.0006 -0.0125 63  VAL   A O   
1497 C CB  . VAL   A 63  ? 0.1392 0.1407 0.2233 -0.0092 -0.0020 -0.0418 63  VAL   A CB  
1498 C CG1 . VAL   A 63  ? 0.1573 0.1687 0.2497 -0.0101 -0.0051 -0.0636 63  VAL   A CG1 
1499 C CG2 . VAL   A 63  ? 0.1537 0.1365 0.2377 -0.0143 0.0141  -0.0439 63  VAL   A CG2 
1509 N N   . GLU   A 64  ? 0.1227 0.1327 0.1652 -0.0013 -0.0025 -0.0136 64  GLU   A N   
1510 C CA  . GLU   A 64  ? 0.1234 0.1260 0.1718 -0.0011 -0.0060 -0.0048 64  GLU   A CA  
1511 C C   . GLU   A 64  ? 0.1173 0.1240 0.1633 -0.0058 0.0060  -0.0045 64  GLU   A C   
1512 O O   . GLU   A 64  ? 0.1238 0.1294 0.1710 0.0009  0.0026  -0.0047 64  GLU   A O   
1513 C CB  . GLU   A 64  ? 0.1348 0.1403 0.1741 -0.0063 -0.0008 -0.0092 64  GLU   A CB  
1514 C CG  . GLU   A 64  ? 0.1494 0.1491 0.1901 -0.0105 0.0088  -0.0053 64  GLU   A CG  
1515 C CD  . GLU   A 64  ? 0.1599 0.1556 0.1918 -0.0148 0.0106  -0.0056 64  GLU   A CD  
1516 O OE1 . GLU   A 64  ? 0.1569 0.1672 0.2120 -0.0239 0.0148  -0.0110 64  GLU   A OE1 
1517 O OE2 . GLU   A 64  ? 0.1793 0.1535 0.1853 -0.0251 0.0007  0.0022  64  GLU   A OE2 
1524 N N   . SER   A 65  ? 0.1136 0.1237 0.1603 0.0020  0.0010  -0.0067 65  SER   A N   
1525 C CA  . SER   A 65  ? 0.1249 0.1164 0.1528 -0.0015 0.0006  -0.0072 65  SER   A CA  
1526 C C   . SER   A 65  ? 0.1246 0.1257 0.1569 -0.0006 -0.0018 -0.0048 65  SER   A C   
1527 O O   . SER   A 65  ? 0.1317 0.1283 0.1751 0.0030  0.0101  -0.0092 65  SER   A O   
1528 C CB  . SER   A 65  ? 0.1275 0.1143 0.1496 -0.0039 0.0091  0.0018  65  SER   A CB  
1529 O OG  . SER   A 65  ? 0.1221 0.1285 0.1650 -0.0108 -0.0023 0.0076  65  SER   A OG  
1535 N N   . ASP   A 66  ? 0.1279 0.1225 0.1571 -0.0029 0.0139  0.0035  66  ASP   A N   
1536 C CA  . ASP   A 66  ? 0.1363 0.1335 0.1749 -0.0030 0.0067  0.0079  66  ASP   A CA  
1537 C C   . ASP   A 66  ? 0.1333 0.1255 0.1814 -0.0065 0.0161  0.0173  66  ASP   A C   
1538 O O   . ASP   A 66  ? 0.1396 0.1375 0.1935 -0.0031 0.0277  0.0183  66  ASP   A O   
1539 C CB  . ASP   A 66  ? 0.1479 0.1429 0.1967 0.0067  0.0076  0.0211  66  ASP   A CB  
1540 C CG  . ASP   A 66  ? 0.1687 0.1574 0.2278 0.0066  -0.0047 0.0404  66  ASP   A CG  
1541 O OD1 . ASP   A 66  ? 0.1677 0.1867 0.2165 -0.0016 -0.0038 0.0462  66  ASP   A OD1 
1542 O OD2 . ASP   A 66  ? 0.1887 0.1675 0.3113 0.0201  -0.0228 0.0153  66  ASP   A OD2 
1547 N N   . ASP   A 67  ? 0.1255 0.1282 0.1921 0.0009  0.0136  0.0087  67  ASP   A N   
1548 C CA  . ASP   A 67  ? 0.1291 0.1448 0.1998 -0.0035 0.0067  0.0213  67  ASP   A CA  
1549 C C   . ASP   A 67  ? 0.1274 0.1430 0.1986 -0.0014 0.0097  0.0202  67  ASP   A C   
1550 O O   . ASP   A 67  ? 0.1242 0.1505 0.2171 0.0013  0.0259  0.0267  67  ASP   A O   
1551 C CB  . ASP   A 67  ? 0.1368 0.1510 0.2358 -0.0038 -0.0149 0.0184  67  ASP   A CB  
1552 C CG  . ASP   A 67  ? 0.1385 0.1647 0.2790 -0.0069 -0.0270 0.0228  67  ASP   A CG  
1553 O OD1 . ASP   A 67  ? 0.1426 0.1813 0.3533 -0.0069 -0.0349 0.0341  67  ASP   A OD1 
1554 O OD2 . ASP   A 67  ? 0.1389 0.1714 0.2560 0.0042  -0.0189 0.0156  67  ASP   A OD2 
1559 N N   . TYR   A 68  ? 0.1288 0.1315 0.1873 0.0035  0.0142  0.0224  68  TYR   A N   
1560 C CA  . TYR   A 68  ? 0.1401 0.1286 0.1810 0.0033  0.0177  0.0233  68  TYR   A CA  
1561 C C   . TYR   A 68  ? 0.1342 0.1302 0.1846 0.0009  0.0208  0.0190  68  TYR   A C   
1562 O O   . TYR   A 68  ? 0.1400 0.1337 0.1903 0.0096  0.0312  0.0206  68  TYR   A O   
1563 C CB  . TYR   A 68  ? 0.1415 0.1269 0.1989 0.0096  0.0358  0.0267  68  TYR   A CB  
1564 C CG  . TYR   A 68  ? 0.1467 0.1419 0.2261 0.0089  0.0493  0.0293  68  TYR   A CG  
1565 C CD1 . TYR   A 68  ? 0.1621 0.1549 0.2465 -0.0174 0.0369  -0.0061 68  TYR   A CD1 
1566 C CD2 . TYR   A 68  ? 0.1746 0.1397 0.2672 0.0157  0.0411  0.0389  68  TYR   A CD2 
1567 C CE1 . TYR   A 68  ? 0.1697 0.1662 0.2766 -0.0172 0.0411  -0.0093 68  TYR   A CE1 
1568 C CE2 . TYR   A 68  ? 0.1697 0.1518 0.2786 0.0045  0.0569  0.0221  68  TYR   A CE2 
1569 C CZ  . TYR   A 68  ? 0.1709 0.1532 0.2897 -0.0196 0.0445  -0.0048 68  TYR   A CZ  
1570 O OH  . TYR   A 68  ? 0.2037 0.1506 0.3118 -0.0095 0.0194  -0.0222 68  TYR   A OH  
1580 N N   . ILE   A 69  ? 0.1292 0.1224 0.1908 -0.0009 0.0195  0.0216  69  ILE   A N   
1581 C CA  . ILE   A 69  ? 0.1364 0.1247 0.1760 0.0017  0.0101  0.0057  69  ILE   A CA  
1582 C C   . ILE   A 69  ? 0.1373 0.1275 0.1656 0.0058  0.0166  0.0113  69  ILE   A C   
1583 O O   . ILE   A 69  ? 0.1480 0.1368 0.1659 -0.0023 0.0222  0.0145  69  ILE   A O   
1584 C CB  . ILE   A 69  ? 0.1442 0.1464 0.1747 0.0072  0.0110  -0.0074 69  ILE   A CB  
1585 C CG1 . ILE   A 69  ? 0.1404 0.1620 0.1811 0.0076  0.0167  -0.0156 69  ILE   A CG1 
1586 C CG2 . ILE   A 69  ? 0.1664 0.1714 0.1963 0.0135  -0.0010 -0.0128 69  ILE   A CG2 
1587 C CD1 . ILE   A 69  ? 0.1400 0.1715 0.1997 -0.0061 0.0188  -0.0200 69  ILE   A CD1 
1599 N N   . ALA   A 70  ? 0.1447 0.1290 0.1823 -0.0058 0.0193  0.0179  70  ALA   A N   
1600 C CA  . ALA   A 70  ? 0.1483 0.1379 0.1971 -0.0140 0.0310  0.0200  70  ALA   A CA  
1601 C C   . ALA   A 70  ? 0.1425 0.1536 0.1974 -0.0130 0.0276  0.0172  70  ALA   A C   
1602 O O   . ALA   A 70  ? 0.1557 0.1862 0.2137 0.0018  0.0426  0.0320  70  ALA   A O   
1603 C CB  . ALA   A 70  ? 0.1552 0.1302 0.2201 -0.0161 0.0234  0.0091  70  ALA   A CB  
1609 N N   . THR   A 71  ? 0.1388 0.1493 0.1828 -0.0054 0.0210  0.0197  71  THR   A N   
1610 C CA  . THR   A 71  ? 0.1429 0.1659 0.2154 0.0052  0.0247  0.0211  71  THR   A CA  
1611 C C   . THR   A 71  ? 0.1351 0.1611 0.2285 0.0100  0.0352  0.0176  71  THR   A C   
1612 O O   . THR   A 71  ? 0.1412 0.1859 0.2713 0.0068  0.0362  -0.0121 71  THR   A O   
1613 C CB  . THR   A 71  ? 0.1667 0.1893 0.2339 0.0166  -0.0064 0.0287  71  THR   A CB  
1614 O OG1 . THR   A 71  ? 0.1884 0.2072 0.2391 0.0093  -0.0330 0.0206  71  THR   A OG1 
1615 C CG2 . THR   A 71  ? 0.1829 0.2111 0.2600 0.0251  -0.0146 0.0395  71  THR   A CG2 
1623 N N   . ASN   A 72  ? 0.1413 0.1394 0.2082 0.0131  0.0314  0.0152  72  ASN   A N   
1624 C CA  . ASN   A 72  ? 0.1497 0.1426 0.2089 0.0167  0.0336  0.0162  72  ASN   A CA  
1625 C C   . ASN   A 72  ? 0.1592 0.1422 0.2092 0.0064  0.0447  0.0036  72  ASN   A C   
1626 O O   . ASN   A 72  ? 0.1730 0.1437 0.2415 0.0132  0.0429  -0.0038 72  ASN   A O   
1627 C CB  . ASN   A 72  ? 0.1656 0.1452 0.2132 0.0116  0.0336  0.0136  72  ASN   A CB  
1628 C CG  . ASN   A 72  ? 0.1913 0.1558 0.2151 0.0238  0.0283  0.0177  72  ASN   A CG  
1629 O OD1 . ASN   A 72  ? 0.2092 0.1955 0.2319 0.0230  0.0391  0.0227  72  ASN   A OD1 
1630 N ND2 . ASN   A 72  ? 0.2087 0.1634 0.2212 0.0456  0.0138  0.0017  72  ASN   A ND2 
1637 N N   . GLY   A 73  ? 0.1556 0.1376 0.1878 0.0008  0.0366  0.0011  73  GLY   A N   
1638 C CA  . GLY   A 73  ? 0.1601 0.1431 0.1683 -0.0062 0.0394  0.0043  73  GLY   A CA  
1639 C C   . GLY   A 73  ? 0.1571 0.1318 0.1667 0.0004  0.0493  0.0170  73  GLY   A C   
1640 O O   . GLY   A 73  ? 0.1572 0.1402 0.1882 0.0092  0.0426  0.0263  73  GLY   A O   
1644 N N   . PRO   A 74  ? 0.1689 0.1347 0.1688 -0.0133 0.0463  0.0093  74  PRO   A N   
1645 C CA  . PRO   A 74  ? 0.1641 0.1302 0.1752 -0.0019 0.0432  0.0140  74  PRO   A CA  
1646 C C   . PRO   A 74  ? 0.1549 0.1210 0.1769 0.0005  0.0297  0.0007  74  PRO   A C   
1647 O O   . PRO   A 74  ? 0.1645 0.1286 0.1996 0.0053  0.0366  -0.0093 74  PRO   A O   
1648 C CB  . PRO   A 74  ? 0.1798 0.1604 0.1987 -0.0030 0.0407  0.0268  74  PRO   A CB  
1649 C CG  . PRO   A 74  ? 0.2067 0.1962 0.2373 -0.0172 0.0268  0.0146  74  PRO   A CG  
1650 C CD  . PRO   A 74  ? 0.1883 0.1729 0.1850 -0.0253 0.0361  0.0048  74  PRO   A CD  
1658 N N   . LEU   A 75  ? 0.1522 0.1140 0.1596 0.0017  0.0225  0.0046  75  LEU   A N   
1659 C CA  . LEU   A 75  ? 0.1576 0.1164 0.1426 -0.0016 0.0076  0.0041  75  LEU   A CA  
1660 C C   . LEU   A 75  ? 0.1635 0.1245 0.1491 0.0055  0.0126  0.0112  75  LEU   A C   
1661 O O   . LEU   A 75  ? 0.1985 0.1433 0.1491 0.0125  0.0110  0.0062  75  LEU   A O   
1662 C CB  . LEU   A 75  ? 0.1627 0.1193 0.1407 -0.0102 0.0096  0.0117  75  LEU   A CB  
1663 C CG  . LEU   A 75  ? 0.1799 0.1567 0.1554 -0.0376 0.0107  0.0107  75  LEU   A CG  
1664 C CD1 . LEU   A 75  ? 0.1912 0.2063 0.1701 -0.0351 -0.0002 -0.0073 75  LEU   A CD1 
1665 C CD2 . LEU   A 75  ? 0.2059 0.2014 0.2140 -0.0168 0.0182  0.0141  75  LEU   A CD2 
1677 N N   . LYS   A 76  ? 0.1699 0.1266 0.1665 -0.0104 0.0138  -0.0061 76  LYS   A N   
1678 C CA  . LYS   A 76  ? 0.1692 0.1460 0.1630 -0.0102 0.0141  -0.0178 76  LYS   A CA  
1679 C C   . LYS   A 76  ? 0.1624 0.1289 0.1391 -0.0019 0.0139  0.0011  76  LYS   A C   
1680 O O   . LYS   A 76  ? 0.1630 0.1279 0.1409 -0.0005 0.0212  0.0086  76  LYS   A O   
1681 C CB  . LYS   A 76  ? 0.1711 0.1712 0.2033 0.0002  0.0136  -0.0457 76  LYS   A CB  
1682 C CG  . LYS   A 76  ? 0.1824 0.1702 0.2677 0.0086  0.0109  -0.0470 76  LYS   A CG  
1683 C CD  . LYS   A 76  ? 0.1879 0.1676 0.3141 0.0152  0.0022  -0.0547 76  LYS   A CD  
1684 C CE  . LYS   A 76  ? 0.2084 0.1910 0.3768 0.0023  0.0024  -0.0534 76  LYS   A CE  
1685 N NZ  . LYS   A 76  ? 0.2107 0.1892 0.4189 -0.0168 -0.0060 -0.0590 76  LYS   A NZ  
1699 N N   . VAL   A 77  ? 0.1698 0.1308 0.1334 0.0003  0.0236  0.0084  77  VAL   A N   
1700 C CA  . VAL   A 77  ? 0.1676 0.1315 0.1345 0.0080  0.0197  0.0091  77  VAL   A CA  
1701 C C   . VAL   A 77  ? 0.1611 0.1306 0.1252 0.0096  0.0103  0.0031  77  VAL   A C   
1702 O O   . VAL   A 77  ? 0.1685 0.1363 0.1334 0.0106  0.0258  -0.0018 77  VAL   A O   
1703 C CB  . VAL   A 77  ? 0.1875 0.1581 0.1407 0.0079  0.0083  0.0128  77  VAL   A CB  
1704 C CG1 . VAL   A 77  ? 0.1798 0.1716 0.1601 0.0160  -0.0081 0.0029  77  VAL   A CG1 
1705 C CG2 . VAL   A 77  ? 0.2187 0.1699 0.1538 0.0042  -0.0034 0.0250  77  VAL   A CG2 
1715 N N   . GLY   A 78  ? 0.1617 0.1284 0.1278 0.0049  0.0238  0.0054  78  GLY   A N   
1716 C CA  . GLY   A 78  ? 0.1547 0.1269 0.1413 0.0005  0.0191  0.0100  78  GLY   A CA  
1717 C C   . GLY   A 78  ? 0.1487 0.1208 0.1315 0.0043  0.0238  0.0068  78  GLY   A C   
1718 O O   . GLY   A 78  ? 0.1460 0.1268 0.1522 -0.0005 0.0146  0.0178  78  GLY   A O   
1722 N N   . GLY   A 79  ? 0.1497 0.1209 0.1300 0.0005  0.0163  0.0099  79  GLY   A N   
1723 C CA  . GLY   A 79  ? 0.1400 0.1269 0.1480 -0.0034 0.0205  0.0071  79  GLY   A CA  
1724 C C   . GLY   A 79  ? 0.1332 0.1187 0.1428 -0.0027 0.0120  0.0050  79  GLY   A C   
1725 O O   . GLY   A 79  ? 0.1377 0.1292 0.1522 0.0206  0.0140  0.0072  79  GLY   A O   
1729 N N   . SER   A 80  ? 0.1295 0.1339 0.1594 0.0013  0.0189  -0.0074 80  SER   A N   
1730 C CA  . SER   A 80  ? 0.1256 0.1252 0.1515 -0.0024 0.0098  0.0019  80  SER   A CA  
1731 C C   . SER   A 80  ? 0.1256 0.1279 0.1582 -0.0052 0.0026  0.0095  80  SER   A C   
1732 O O   . SER   A 80  ? 0.1221 0.1489 0.1898 0.0048  0.0121  -0.0077 80  SER   A O   
1733 C CB  . SER   A 80  ? 0.1411 0.1265 0.1790 -0.0004 0.0035  -0.0009 80  SER   A CB  
1734 O OG  . SER   A 80  ? 0.1720 0.1308 0.2166 0.0027  -0.0093 0.0155  80  SER   A OG  
1740 N N   . CYS   A 81  ? 0.1229 0.1238 0.1501 0.0002  -0.0084 0.0077  81  CYS   A N   
1741 C CA  . CYS   A 81  ? 0.1262 0.1325 0.1504 -0.0060 -0.0106 0.0134  81  CYS   A CA  
1742 C C   . CYS   A 81  ? 0.1239 0.1212 0.1484 -0.0093 -0.0070 0.0226  81  CYS   A C   
1743 O O   . CYS   A 81  ? 0.1240 0.1522 0.1632 -0.0019 -0.0014 0.0310  81  CYS   A O   
1744 C CB  . CYS   A 81  ? 0.1328 0.1422 0.1659 -0.0141 -0.0022 0.0137  81  CYS   A CB  
1745 S SG  . CYS   A 81  ? 0.1488 0.1261 0.1663 -0.0128 0.0011  0.0096  81  CYS   A SG  
1751 N N   . VAL   A 82  ? 0.1286 0.1329 0.1457 -0.0004 -0.0153 0.0131  82  VAL   A N   
1752 C CA  . VAL   A 82  ? 0.1437 0.1374 0.1523 0.0001  -0.0074 0.0242  82  VAL   A CA  
1753 C C   . VAL   A 82  ? 0.1391 0.1416 0.1595 0.0011  -0.0130 0.0234  82  VAL   A C   
1754 O O   . VAL   A 82  ? 0.1308 0.1556 0.1879 0.0001  -0.0109 0.0002  82  VAL   A O   
1755 C CB  . VAL   A 82  ? 0.1788 0.1498 0.1628 -0.0004 -0.0035 0.0229  82  VAL   A CB  
1756 C CG1 . VAL   A 82  ? 0.1962 0.1654 0.1824 0.0011  -0.0006 0.0238  82  VAL   A CG1 
1757 C CG2 . VAL   A 82  ? 0.1850 0.1527 0.1909 -0.0021 -0.0104 0.0270  82  VAL   A CG2 
1767 N N   . LEU   A 83  ? 0.1336 0.1352 0.1457 -0.0046 -0.0115 0.0132  83  LEU   A N   
1768 C CA  . LEU   A 83  ? 0.1343 0.1373 0.1488 -0.0068 -0.0159 0.0053  83  LEU   A CA  
1769 C C   . LEU   A 83  ? 0.1414 0.1407 0.1433 -0.0096 -0.0132 0.0056  83  LEU   A C   
1770 O O   . LEU   A 83  ? 0.1568 0.1438 0.1532 -0.0138 -0.0056 0.0108  83  LEU   A O   
1771 C CB  . LEU   A 83  ? 0.1479 0.1431 0.1541 -0.0093 -0.0114 0.0098  83  LEU   A CB  
1772 C CG  . LEU   A 83  ? 0.1646 0.1535 0.1607 -0.0106 0.0028  0.0046  83  LEU   A CG  
1773 C CD1 . LEU   A 83  ? 0.1736 0.1629 0.1668 -0.0232 0.0051  0.0169  83  LEU   A CD1 
1774 C CD2 . LEU   A 83  ? 0.1606 0.1653 0.1760 -0.0095 0.0144  0.0164  83  LEU   A CD2 
1786 N N   . SER   A 84  ? 0.1558 0.1445 0.1470 -0.0140 -0.0058 0.0114  84  SER   A N   
1787 C CA  . SER   A 84  ? 0.1699 0.1519 0.1376 -0.0112 -0.0092 0.0057  84  SER   A CA  
1788 C C   . SER   A 84  ? 0.1755 0.1482 0.1246 -0.0162 0.0010  0.0043  84  SER   A C   
1789 O O   . SER   A 84  ? 0.1716 0.1619 0.1268 -0.0155 -0.0116 -0.0002 84  SER   A O   
1790 C CB  . SER   A 84  ? 0.1817 0.1787 0.1471 -0.0147 -0.0066 -0.0036 84  SER   A CB  
1791 O OG  . SER   A 84  ? 0.1856 0.1984 0.1561 -0.0102 -0.0175 -0.0134 84  SER   A OG  
1797 N N   . GLY   A 85  ? 0.1855 0.1593 0.1254 -0.0204 0.0088  0.0032  85  GLY   A N   
1798 C CA  . GLY   A 85  ? 0.1909 0.1733 0.1387 -0.0288 0.0144  -0.0033 85  GLY   A CA  
1799 C C   . GLY   A 85  ? 0.1825 0.1787 0.1226 -0.0212 0.0056  -0.0035 85  GLY   A C   
1800 O O   . GLY   A 85  ? 0.1813 0.1871 0.1385 -0.0288 0.0144  -0.0158 85  GLY   A O   
1804 N N   . HIS   A 86  ? 0.1828 0.1650 0.1224 -0.0170 -0.0001 -0.0018 86  HIS   A N   
1805 C CA  . HIS   A 86  ? 0.2009 0.1728 0.1225 -0.0151 0.0037  -0.0050 86  HIS   A CA  
1806 C C   . HIS   A 86  ? 0.2208 0.1859 0.1216 -0.0189 -0.0053 -0.0086 86  HIS   A C   
1807 O O   . HIS   A 86  ? 0.2275 0.2083 0.1290 -0.0097 0.0021  -0.0053 86  HIS   A O   
1808 C CB  . HIS   A 86  ? 0.1992 0.1678 0.1448 -0.0078 0.0078  -0.0042 86  HIS   A CB  
1809 C CG  . HIS   A 86  ? 0.1943 0.1647 0.1484 -0.0038 0.0090  0.0045  86  HIS   A CG  
1810 N ND1 . HIS   A 86  ? 0.1958 0.1696 0.1799 -0.0167 0.0012  0.0077  86  HIS   A ND1 
1811 C CD2 . HIS   A 86  ? 0.1951 0.1575 0.1439 0.0030  0.0124  0.0109  86  HIS   A CD2 
1812 C CE1 . HIS   A 86  ? 0.1989 0.1664 0.1780 -0.0126 0.0237  0.0129  86  HIS   A CE1 
1813 N NE2 . HIS   A 86  ? 0.1970 0.1550 0.1640 -0.0014 0.0244  0.0248  86  HIS   A NE2 
1821 N N   . ASN   A 87  ? 0.2332 0.1926 0.1300 -0.0165 0.0189  -0.0107 87  ASN   A N   
1822 C CA  . ASN   A 87  ? 0.2523 0.2069 0.1440 -0.0088 0.0398  -0.0146 87  ASN   A CA  
1823 C C   . ASN   A 87  ? 0.2519 0.2238 0.1598 -0.0127 0.0590  -0.0038 87  ASN   A C   
1824 O O   . ASN   A 87  ? 0.2762 0.2440 0.2118 -0.0186 0.0869  -0.0110 87  ASN   A O   
1825 C CB  . ASN   A 87  ? 0.2692 0.2171 0.1489 0.0007  0.0412  -0.0173 87  ASN   A CB  
1826 C CG  . ASN   A 87  ? 0.2825 0.2304 0.1541 0.0121  0.0480  -0.0163 87  ASN   A CG  
1827 O OD1 . ASN   A 87  ? 0.2974 0.2304 0.1661 0.0324  0.0447  -0.0059 87  ASN   A OD1 
1828 N ND2 . ASN   A 87  ? 0.2858 0.2527 0.1643 0.0084  0.0468  -0.0048 87  ASN   A ND2 
1835 N N   . LEU   A 88  ? 0.2267 0.2196 0.1549 -0.0235 0.0350  0.0102  88  LEU   A N   
1836 C CA  . LEU   A 88  ? 0.2135 0.2181 0.1799 -0.0375 0.0225  0.0335  88  LEU   A CA  
1837 C C   . LEU   A 88  ? 0.2095 0.2157 0.1654 -0.0358 0.0213  0.0380  88  LEU   A C   
1838 O O   . LEU   A 88  ? 0.2158 0.2267 0.2005 -0.0386 0.0237  0.0540  88  LEU   A O   
1839 C CB  . LEU   A 88  ? 0.2194 0.2297 0.2050 -0.0428 -0.0160 0.0459  88  LEU   A CB  
1840 C CG  . LEU   A 88  ? 0.2344 0.2432 0.2429 -0.0419 -0.0275 0.0483  88  LEU   A CG  
1841 C CD1 . LEU   A 88  ? 0.2451 0.2485 0.2374 -0.0408 -0.0306 0.0383  88  LEU   A CD1 
1842 C CD2 . LEU   A 88  ? 0.2461 0.2544 0.2866 -0.0351 -0.0257 0.0391  88  LEU   A CD2 
1854 N N   . ALA   A 89  ? 0.2065 0.2023 0.1426 -0.0359 0.0180  0.0084  89  ALA   A N   
1855 C CA  . ALA   A 89  ? 0.2175 0.1990 0.1337 -0.0307 0.0092  0.0110  89  ALA   A CA  
1856 C C   . ALA   A 89  ? 0.2246 0.2032 0.1350 -0.0222 -0.0100 0.0084  89  ALA   A C   
1857 O O   . ALA   A 89  ? 0.2196 0.1989 0.1700 -0.0240 -0.0199 -0.0099 89  ALA   A O   
1858 C CB  . ALA   A 89  ? 0.2133 0.2000 0.1202 -0.0277 -0.0029 0.0108  89  ALA   A CB  
1864 N N   . LYS   A 90  ? 0.2391 0.2172 0.1287 -0.0279 -0.0236 0.0170  90  LYS   A N   
1865 C CA  . LYS   A 90  ? 0.2504 0.2362 0.1424 -0.0277 -0.0419 0.0172  90  LYS   A CA  
1866 C C   . LYS   A 90  ? 0.2218 0.2137 0.1417 -0.0292 -0.0353 0.0098  90  LYS   A C   
1867 O O   . LYS   A 90  ? 0.2207 0.2272 0.1694 -0.0306 -0.0356 -0.0058 90  LYS   A O   
1868 C CB  . LYS   A 90  ? 0.2915 0.2807 0.1838 -0.0280 -0.0535 0.0305  90  LYS   A CB  
1869 C CG  . LYS   A 90  ? 0.3324 0.3228 0.2896 -0.0301 -0.0502 0.0405  90  LYS   A CG  
1870 C CD  . LYS   A 90  ? 0.3749 0.3668 0.4007 -0.0346 -0.0370 0.0427  90  LYS   A CD  
1871 C CE  . LYS   A 90  ? 0.4151 0.4099 0.4806 -0.0381 -0.0275 0.0392  90  LYS   A CE  
1872 N NZ  . LYS   A 90  ? 0.4270 0.4205 0.5331 -0.0395 -0.0251 0.0372  90  LYS   A NZ  
1886 N N   . HIS   A 91  ? 0.2059 0.1851 0.1165 -0.0270 -0.0319 0.0111  91  HIS   A N   
1887 C CA  . HIS   A 91  ? 0.1926 0.1734 0.1245 -0.0181 -0.0290 0.0168  91  HIS   A CA  
1888 C C   . HIS   A 91  ? 0.1695 0.1551 0.1169 -0.0198 -0.0158 0.0158  91  HIS   A C   
1889 O O   . HIS   A 91  ? 0.1673 0.1704 0.1286 -0.0192 -0.0028 0.0167  91  HIS   A O   
1890 C CB  . HIS   A 91  ? 0.2094 0.2033 0.1678 0.0036  -0.0443 0.0094  91  HIS   A CB  
1891 C CG  . HIS   A 91  ? 0.2458 0.2496 0.2438 0.0162  -0.0655 0.0025  91  HIS   A CG  
1892 N ND1 . HIS   A 91  ? 0.2560 0.2764 0.2815 0.0193  -0.0727 -0.0156 91  HIS   A ND1 
1893 C CD2 . HIS   A 91  ? 0.2694 0.2696 0.2705 0.0222  -0.0733 0.0066  91  HIS   A CD2 
1894 C CE1 . HIS   A 91  ? 0.2696 0.2840 0.2942 0.0226  -0.0758 -0.0071 91  HIS   A CE1 
1895 N NE2 . HIS   A 91  ? 0.2800 0.2838 0.2909 0.0260  -0.0788 -0.0017 91  HIS   A NE2 
1903 N N   . CYS   A 92  ? 0.1566 0.1437 0.1229 -0.0194 -0.0117 0.0116  92  CYS   A N   
1904 C CA  . CYS   A 92  ? 0.1445 0.1399 0.1312 -0.0108 -0.0048 0.0080  92  CYS   A CA  
1905 C C   . CYS   A 92  ? 0.1385 0.1363 0.1248 -0.0100 -0.0014 0.0129  92  CYS   A C   
1906 O O   . CYS   A 92  ? 0.1373 0.1393 0.1400 -0.0141 -0.0097 0.0083  92  CYS   A O   
1907 C CB  . CYS   A 92  ? 0.1490 0.1443 0.1393 -0.0018 -0.0068 0.0038  92  CYS   A CB  
1908 S SG  . CYS   A 92  ? 0.1489 0.1338 0.1308 -0.0094 -0.0027 0.0081  92  CYS   A SG  
1914 N N   . LEU   A 93  ? 0.1373 0.1236 0.1261 -0.0097 0.0040  0.0115  93  LEU   A N   
1915 C CA  . LEU   A 93  ? 0.1282 0.1204 0.1277 -0.0073 -0.0008 0.0118  93  LEU   A CA  
1916 C C   . LEU   A 93  ? 0.1229 0.1126 0.1266 -0.0015 0.0020  0.0063  93  LEU   A C   
1917 O O   . LEU   A 93  ? 0.1210 0.1203 0.1327 -0.0047 -0.0023 0.0115  93  LEU   A O   
1918 C CB  . LEU   A 93  ? 0.1321 0.1208 0.1431 -0.0028 -0.0065 0.0218  93  LEU   A CB  
1919 C CG  . LEU   A 93  ? 0.1420 0.1211 0.1433 -0.0021 0.0022  0.0245  93  LEU   A CG  
1920 C CD1 . LEU   A 93  ? 0.1450 0.1285 0.1763 -0.0012 0.0064  0.0144  93  LEU   A CD1 
1921 C CD2 . LEU   A 93  ? 0.1526 0.1269 0.1518 -0.0087 -0.0028 0.0138  93  LEU   A CD2 
1933 N N   . HIS   A 94  ? 0.1175 0.1096 0.1311 -0.0051 0.0058  0.0106  94  HIS   A N   
1934 C CA  . HIS   A 94  ? 0.1187 0.1130 0.1270 -0.0058 -0.0030 0.0110  94  HIS   A CA  
1935 C C   . HIS   A 94  ? 0.1143 0.1099 0.1366 -0.0073 -0.0002 0.0068  94  HIS   A C   
1936 O O   . HIS   A 94  ? 0.1150 0.1397 0.1654 0.0001  0.0001  -0.0125 94  HIS   A O   
1937 C CB  . HIS   A 94  ? 0.1214 0.1085 0.1406 -0.0008 -0.0015 0.0119  94  HIS   A CB  
1938 C CG  . HIS   A 94  ? 0.1254 0.1148 0.1330 -0.0059 -0.0062 0.0151  94  HIS   A CG  
1939 N ND1 . HIS   A 94  ? 0.1239 0.1118 0.1388 0.0014  0.0049  0.0133  94  HIS   A ND1 
1940 C CD2 . HIS   A 94  ? 0.1314 0.1233 0.1374 0.0004  -0.0084 0.0027  94  HIS   A CD2 
1941 C CE1 . HIS   A 94  ? 0.1270 0.1164 0.1369 -0.0081 -0.0068 -0.0026 94  HIS   A CE1 
1942 N NE2 . HIS   A 94  ? 0.1345 0.1178 0.1459 -0.0046 -0.0152 0.0026  94  HIS   A NE2 
1950 N N   . VAL   A 95  ? 0.1124 0.1062 0.1197 -0.0039 0.0080  0.0075  95  VAL   A N   
1951 C CA  . VAL   A 95  ? 0.1221 0.1076 0.1217 -0.0030 0.0100  0.0058  95  VAL   A CA  
1952 C C   . VAL   A 95  ? 0.1206 0.1092 0.1058 -0.0103 0.0023  0.0066  95  VAL   A C   
1953 O O   . VAL   A 95  ? 0.1282 0.1259 0.1191 0.0095  0.0068  0.0047  95  VAL   A O   
1954 C CB  . VAL   A 95  ? 0.1258 0.1110 0.1378 -0.0094 0.0037  0.0098  95  VAL   A CB  
1955 C CG1 . VAL   A 95  ? 0.1404 0.1206 0.1396 -0.0127 0.0031  0.0015  95  VAL   A CG1 
1956 C CG2 . VAL   A 95  ? 0.1328 0.1169 0.1444 -0.0133 0.0050  0.0184  95  VAL   A CG2 
1966 N N   . VAL   A 96  ? 0.1276 0.1084 0.1080 -0.0074 0.0064  0.0090  96  VAL   A N   
1967 C CA  . VAL   A 96  ? 0.1326 0.1120 0.1242 -0.0018 0.0123  0.0166  96  VAL   A CA  
1968 C C   . VAL   A 96  ? 0.1330 0.1196 0.1140 -0.0037 0.0131  0.0133  96  VAL   A C   
1969 O O   . VAL   A 96  ? 0.1412 0.1265 0.1405 -0.0058 0.0160  -0.0076 96  VAL   A O   
1970 C CB  . VAL   A 96  ? 0.1338 0.1185 0.1372 0.0007  0.0198  0.0140  96  VAL   A CB  
1971 C CG1 . VAL   A 96  ? 0.1396 0.1258 0.1333 -0.0022 0.0193  0.0100  96  VAL   A CG1 
1972 C CG2 . VAL   A 96  ? 0.1354 0.1242 0.1496 -0.0170 0.0126  0.0148  96  VAL   A CG2 
1982 N N   . GLY   A 97  ? 0.1295 0.1233 0.1300 -0.0086 0.0093  0.0075  97  GLY   A N   
1983 C CA  . GLY   A 97  ? 0.1405 0.1378 0.1307 -0.0049 0.0059  0.0116  97  GLY   A CA  
1984 C C   . GLY   A 97  ? 0.1401 0.1486 0.1177 -0.0042 0.0042  0.0109  97  GLY   A C   
1985 O O   . GLY   A 97  ? 0.1545 0.1494 0.1386 -0.0094 -0.0005 0.0168  97  GLY   A O   
1989 N N   . PRO   A 98  ? 0.1466 0.1527 0.1116 0.0011  -0.0010 0.0183  98  PRO   A N   
1990 C CA  . PRO   A 98  ? 0.1621 0.1723 0.1207 -0.0011 0.0027  0.0091  98  PRO   A CA  
1991 C C   . PRO   A 98  ? 0.1676 0.1814 0.1125 -0.0135 0.0009  0.0278  98  PRO   A C   
1992 O O   . PRO   A 98  ? 0.1558 0.1593 0.1396 -0.0101 -0.0021 0.0238  98  PRO   A O   
1993 C CB  . PRO   A 98  ? 0.1770 0.1852 0.1134 -0.0006 -0.0047 -0.0062 98  PRO   A CB  
1994 C CG  . PRO   A 98  ? 0.1751 0.1731 0.1318 0.0038  -0.0066 -0.0096 98  PRO   A CG  
1995 C CD  . PRO   A 98  ? 0.1559 0.1548 0.1228 0.0052  -0.0054 0.0076  98  PRO   A CD  
2003 N N   A ASN   A 99  ? 0.1734 0.2085 0.1179 -0.0115 0.0015  0.0460  99  ASN   A N   
2004 N N   B ASN   A 99  ? 0.1817 0.1923 0.1268 -0.0060 -0.0078 0.0375  99  ASN   A N   
2005 C CA  A ASN   A 99  ? 0.1921 0.2230 0.1237 -0.0119 0.0022  0.0582  99  ASN   A CA  
2006 C CA  B ASN   A 99  ? 0.1982 0.1984 0.1462 -0.0004 -0.0159 0.0443  99  ASN   A CA  
2007 C C   A ASN   A 99  ? 0.2073 0.2605 0.1120 -0.0228 0.0081  0.0553  99  ASN   A C   
2008 C C   B ASN   A 99  ? 0.2162 0.2071 0.1597 -0.0016 -0.0149 0.0377  99  ASN   A C   
2009 O O   A ASN   A 99  ? 0.2130 0.2773 0.1169 -0.0179 0.0082  0.0564  99  ASN   A O   
2010 O O   B ASN   A 99  ? 0.2170 0.1965 0.1586 0.0039  -0.0172 0.0365  99  ASN   A O   
2011 C CB  A ASN   A 99  ? 0.1918 0.2091 0.1430 -0.0133 -0.0083 0.0602  99  ASN   A CB  
2012 C CB  B ASN   A 99  ? 0.1968 0.1997 0.1677 0.0028  -0.0246 0.0550  99  ASN   A CB  
2013 C CG  A ASN   A 99  ? 0.1934 0.2059 0.1713 -0.0160 -0.0204 0.0414  99  ASN   A CG  
2014 C CG  B ASN   A 99  ? 0.1962 0.2031 0.1847 0.0057  -0.0292 0.0621  99  ASN   A CG  
2015 O OD1 A ASN   A 99  ? 0.2064 0.2170 0.1827 -0.0087 -0.0286 0.0320  99  ASN   A OD1 
2016 O OD1 B ASN   A 99  ? 0.2001 0.2073 0.1831 0.0063  -0.0333 0.0638  99  ASN   A OD1 
2017 N ND2 A ASN   A 99  ? 0.1966 0.2030 0.1999 -0.0171 -0.0259 0.0402  99  ASN   A ND2 
2018 N ND2 B ASN   A 99  ? 0.1952 0.2049 0.1979 0.0094  -0.0278 0.0618  99  ASN   A ND2 
2031 N N   A VAL   A 100 ? 0.2206 0.2735 0.1006 -0.0384 -0.0141 0.0457  100 VAL   A N   
2032 N N   B VAL   A 100 ? 0.2326 0.2280 0.1790 -0.0069 -0.0171 0.0316  100 VAL   A N   
2033 C CA  A VAL   A 100 ? 0.2485 0.3018 0.1300 -0.0498 -0.0243 0.0390  100 VAL   A CA  
2034 C CA  B VAL   A 100 ? 0.2498 0.2528 0.2043 -0.0127 -0.0162 0.0267  100 VAL   A CA  
2035 C C   A VAL   A 100 ? 0.2549 0.3235 0.1186 -0.0600 -0.0327 0.0703  100 VAL   A C   
2036 C C   B VAL   A 100 ? 0.2612 0.2725 0.2129 -0.0136 -0.0181 0.0331  100 VAL   A C   
2037 O O   A VAL   A 100 ? 0.2645 0.3387 0.1368 -0.0584 -0.0076 0.0684  100 VAL   A O   
2038 O O   B VAL   A 100 ? 0.2634 0.2795 0.2160 -0.0116 -0.0144 0.0355  100 VAL   A O   
2039 C CB  A VAL   A 100 ? 0.2707 0.3003 0.1755 -0.0565 -0.0362 0.0265  100 VAL   A CB  
2040 C CB  B VAL   A 100 ? 0.2559 0.2560 0.2236 -0.0176 -0.0175 0.0241  100 VAL   A CB  
2041 C CG1 A VAL   A 100 ? 0.2712 0.3077 0.1980 -0.0617 -0.0304 0.0248  100 VAL   A CG1 
2042 C CG1 B VAL   A 100 ? 0.2560 0.2585 0.2337 -0.0211 -0.0165 0.0243  100 VAL   A CG1 
2043 C CG2 A VAL   A 100 ? 0.2862 0.3046 0.1952 -0.0582 -0.0343 0.0198  100 VAL   A CG2 
2044 C CG2 B VAL   A 100 ? 0.2606 0.2582 0.2354 -0.0189 -0.0172 0.0212  100 VAL   A CG2 
2063 N N   A ASN   A 101 ? 0.2628 0.3290 0.1627 -0.0617 -0.0438 0.1055  101 ASN   A N   
2064 N N   B ASN   A 101 ? 0.2697 0.2840 0.2259 -0.0171 -0.0222 0.0386  101 ASN   A N   
2065 C CA  A ASN   A 101 ? 0.2873 0.3392 0.2013 -0.0659 -0.0413 0.1266  101 ASN   A CA  
2066 C CA  B ASN   A 101 ? 0.2791 0.2963 0.2337 -0.0219 -0.0283 0.0431  101 ASN   A CA  
2067 C C   A ASN   A 101 ? 0.3123 0.3660 0.2274 -0.0665 -0.0012 0.1539  101 ASN   A C   
2068 C C   B ASN   A 101 ? 0.2933 0.3186 0.2568 -0.0221 -0.0275 0.0486  101 ASN   A C   
2069 O O   A ASN   A 101 ? 0.3270 0.3732 0.2639 -0.0689 0.0000  0.1585  101 ASN   A O   
2070 O O   B ASN   A 101 ? 0.2944 0.3213 0.2625 -0.0243 -0.0305 0.0497  101 ASN   A O   
2071 C CB  A ASN   A 101 ? 0.2893 0.3249 0.2048 -0.0625 -0.0706 0.1085  101 ASN   A CB  
2072 C CB  B ASN   A 101 ? 0.2739 0.2861 0.2266 -0.0271 -0.0324 0.0391  101 ASN   A CB  
2073 C CG  A ASN   A 101 ? 0.2929 0.3098 0.1907 -0.0633 -0.0818 0.0777  101 ASN   A CG  
2074 C CG  B ASN   A 101 ? 0.2682 0.2756 0.2172 -0.0335 -0.0368 0.0285  101 ASN   A CG  
2075 O OD1 A ASN   A 101 ? 0.2923 0.3172 0.1987 -0.0531 -0.0701 0.0362  101 ASN   A OD1 
2076 O OD1 B ASN   A 101 ? 0.2652 0.2714 0.2133 -0.0342 -0.0391 0.0208  101 ASN   A OD1 
2077 N ND2 A ASN   A 101 ? 0.3000 0.2939 0.1854 -0.0721 -0.0800 0.0839  101 ASN   A ND2 
2078 N ND2 B ASN   A 101 ? 0.2656 0.2707 0.2108 -0.0379 -0.0349 0.0268  101 ASN   A ND2 
2091 N N   A LYS   A 102 ? 0.3226 0.4006 0.2443 -0.0734 0.0241  0.1575  102 LYS   A N   
2092 N N   B LYS   A 102 ? 0.3059 0.3376 0.2770 -0.0199 -0.0221 0.0458  102 LYS   A N   
2093 C CA  A LYS   A 102 ? 0.3393 0.4359 0.2421 -0.0753 0.0389  0.1531  102 LYS   A CA  
2094 C CA  B LYS   A 102 ? 0.3178 0.3547 0.2935 -0.0180 -0.0153 0.0408  102 LYS   A CA  
2095 C C   A LYS   A 102 ? 0.3504 0.4615 0.2220 -0.0602 0.0384  0.1419  102 LYS   A C   
2096 C C   B LYS   A 102 ? 0.3222 0.3650 0.2874 -0.0121 -0.0104 0.0391  102 LYS   A C   
2097 O O   A LYS   A 102 ? 0.3542 0.4776 0.2246 -0.0545 0.0450  0.1329  102 LYS   A O   
2098 O O   B LYS   A 102 ? 0.3223 0.3685 0.2857 -0.0096 -0.0093 0.0408  102 LYS   A O   
2099 C CB  A LYS   A 102 ? 0.3516 0.4467 0.2767 -0.0868 0.0356  0.1339  102 LYS   A CB  
2100 C CB  B LYS   A 102 ? 0.3241 0.3598 0.3133 -0.0214 -0.0111 0.0344  102 LYS   A CB  
2101 C CG  A LYS   A 102 ? 0.3625 0.4540 0.3067 -0.0958 0.0285  0.1104  102 LYS   A CG  
2102 C CG  B LYS   A 102 ? 0.3298 0.3641 0.3293 -0.0249 -0.0078 0.0274  102 LYS   A CG  
2103 C CD  A LYS   A 102 ? 0.3773 0.4631 0.3361 -0.0971 0.0169  0.0798  102 LYS   A CD  
2104 C CD  B LYS   A 102 ? 0.3359 0.3687 0.3411 -0.0263 -0.0042 0.0197  102 LYS   A CD  
2105 C CE  A LYS   A 102 ? 0.3901 0.4708 0.3622 -0.0956 0.0077  0.0565  102 LYS   A CE  
2106 C CE  B LYS   A 102 ? 0.3410 0.3725 0.3514 -0.0263 -0.0020 0.0133  102 LYS   A CE  
2107 N NZ  A LYS   A 102 ? 0.3981 0.4748 0.3744 -0.0963 0.0047  0.0415  102 LYS   A NZ  
2108 N NZ  B LYS   A 102 ? 0.3444 0.3751 0.3555 -0.0262 -0.0007 0.0087  102 LYS   A NZ  
2135 N N   A GLY   A 103 ? 0.3517 0.4734 0.2197 -0.0465 0.0251  0.1106  103 GLY   A N   
2136 N N   B GLY   A 103 ? 0.3254 0.3712 0.2905 -0.0090 -0.0095 0.0297  103 GLY   A N   
2137 C CA  A GLY   A 103 ? 0.3517 0.4775 0.2151 -0.0349 0.0204  0.0831  103 GLY   A CA  
2138 C CA  B GLY   A 103 ? 0.3272 0.3749 0.2894 -0.0061 -0.0058 0.0219  103 GLY   A CA  
2139 C C   A GLY   A 103 ? 0.3454 0.4784 0.2085 -0.0292 0.0256  0.0552  103 GLY   A C   
2140 C C   B GLY   A 103 ? 0.3278 0.3782 0.2916 -0.0047 -0.0001 0.0135  103 GLY   A C   
2141 O O   A GLY   A 103 ? 0.3548 0.4846 0.2314 -0.0268 0.0182  0.0417  103 GLY   A O   
2142 O O   B GLY   A 103 ? 0.3294 0.3801 0.2970 -0.0045 0.0029  0.0083  103 GLY   A O   
2149 N N   A GLU   A 104 ? 0.3254 0.4661 0.1531 -0.0293 0.0336  0.0401  104 GLU   A N   
2150 N N   B GLU   A 104 ? 0.3258 0.3773 0.2809 -0.0052 0.0017  0.0085  104 GLU   A N   
2151 C CA  A GLU   A 104 ? 0.3018 0.4499 0.1339 -0.0382 0.0312  0.0283  104 GLU   A CA  
2152 C CA  B GLU   A 104 ? 0.3221 0.3751 0.2728 -0.0073 0.0029  0.0032  104 GLU   A CA  
2153 C C   A GLU   A 104 ? 0.3020 0.4597 0.1280 -0.0413 0.0322  0.0011  104 GLU   A C   
2154 C C   B GLU   A 104 ? 0.3259 0.3800 0.2793 -0.0099 0.0026  -0.0056 104 GLU   A C   
2155 O O   A GLU   A 104 ? 0.2957 0.4642 0.1503 -0.0428 0.0238  -0.0074 104 GLU   A O   
2156 O O   B GLU   A 104 ? 0.3253 0.3812 0.2767 -0.0108 0.0026  -0.0044 104 GLU   A O   
2157 C CB  A GLU   A 104 ? 0.2730 0.4201 0.1283 -0.0458 0.0334  0.0502  104 GLU   A CB  
2158 C CB  B GLU   A 104 ? 0.3148 0.3683 0.2606 -0.0071 0.0031  0.0066  104 GLU   A CB  
2159 C CG  A GLU   A 104 ? 0.2539 0.4006 0.1420 -0.0496 0.0263  0.0663  104 GLU   A CG  
2160 C CG  B GLU   A 104 ? 0.3096 0.3622 0.2559 -0.0060 0.0034  0.0101  104 GLU   A CG  
2161 C CD  A GLU   A 104 ? 0.2337 0.3821 0.1463 -0.0508 0.0256  0.0765  104 GLU   A CD  
2162 C CD  B GLU   A 104 ? 0.3049 0.3565 0.2517 -0.0051 0.0045  0.0135  104 GLU   A CD  
2163 O OE1 A GLU   A 104 ? 0.2151 0.3684 0.1278 -0.0472 0.0154  0.0743  104 GLU   A OE1 
2164 O OE1 B GLU   A 104 ? 0.3017 0.3527 0.2442 -0.0038 0.0046  0.0152  104 GLU   A OE1 
2165 O OE2 A GLU   A 104 ? 0.2477 0.3809 0.1721 -0.0556 0.0237  0.0925  104 GLU   A OE2 
2166 O OE2 B GLU   A 104 ? 0.3066 0.3561 0.2578 -0.0051 0.0047  0.0145  104 GLU   A OE2 
2179 N N   A ASP   A 105 ? 0.3091 0.4665 0.1443 -0.0421 0.0387  -0.0236 105 ASP   A N   
2180 N N   B ASP   A 105 ? 0.3302 0.3831 0.2876 -0.0115 0.0049  -0.0173 105 ASP   A N   
2181 C CA  A ASP   A 105 ? 0.3092 0.4675 0.1940 -0.0389 0.0398  -0.0515 105 ASP   A CA  
2182 C CA  B ASP   A 105 ? 0.3343 0.3851 0.3008 -0.0134 0.0050  -0.0297 105 ASP   A CA  
2183 C C   A ASP   A 105 ? 0.2680 0.4435 0.1645 -0.0478 0.0201  -0.0634 105 ASP   A C   
2184 C C   B ASP   A 105 ? 0.3256 0.3782 0.2887 -0.0170 0.0045  -0.0308 105 ASP   A C   
2185 O O   A ASP   A 105 ? 0.2368 0.4181 0.1345 -0.0481 0.0133  -0.0814 105 ASP   A O   
2186 O O   B ASP   A 105 ? 0.3240 0.3782 0.2866 -0.0166 0.0029  -0.0304 105 ASP   A O   
2187 C CB  A ASP   A 105 ? 0.3462 0.4924 0.2720 -0.0281 0.0598  -0.0704 105 ASP   A CB  
2188 C CB  B ASP   A 105 ? 0.3450 0.3917 0.3240 -0.0118 0.0056  -0.0433 105 ASP   A CB  
2189 C CG  A ASP   A 105 ? 0.3774 0.5108 0.3415 -0.0176 0.0669  -0.0896 105 ASP   A CG  
2190 C CG  B ASP   A 105 ? 0.3536 0.3974 0.3450 -0.0109 0.0033  -0.0565 105 ASP   A CG  
2191 O OD1 A ASP   A 105 ? 0.3848 0.5187 0.3475 -0.0163 0.0692  -0.1041 105 ASP   A OD1 
2192 O OD1 B ASP   A 105 ? 0.3562 0.4001 0.3492 -0.0105 0.0032  -0.0635 105 ASP   A OD1 
2193 O OD2 A ASP   A 105 ? 0.3902 0.5187 0.3858 -0.0154 0.0712  -0.0865 105 ASP   A OD2 
2194 O OD2 B ASP   A 105 ? 0.3581 0.3990 0.3549 -0.0119 0.0013  -0.0609 105 ASP   A OD2 
2203 N N   A ILE   A 106 ? 0.2541 0.4359 0.1827 -0.0568 -0.0065 -0.0588 106 ILE   A N   
2204 N N   B ILE   A 106 ? 0.3177 0.3697 0.2817 -0.0216 0.0036  -0.0329 106 ILE   A N   
2205 C CA  A ILE   A 106 ? 0.2271 0.4183 0.2045 -0.0705 -0.0255 -0.0714 106 ILE   A CA  
2206 C CA  B ILE   A 106 ? 0.3067 0.3575 0.2775 -0.0259 0.0051  -0.0389 106 ILE   A CA  
2207 C C   A ILE   A 106 ? 0.2112 0.3883 0.2210 -0.0872 -0.0197 -0.0999 106 ILE   A C   
2208 C C   B ILE   A 106 ? 0.2974 0.3404 0.2784 -0.0313 0.0117  -0.0523 106 ILE   A C   
2209 O O   A ILE   A 106 ? 0.1894 0.3728 0.2254 -0.0912 -0.0036 -0.1118 106 ILE   A O   
2210 O O   B ILE   A 106 ? 0.2950 0.3357 0.2716 -0.0298 0.0144  -0.0575 106 ILE   A O   
2211 C CB  A ILE   A 106 ? 0.2275 0.4270 0.2502 -0.0601 -0.0452 -0.0415 106 ILE   A CB  
2212 C CB  B ILE   A 106 ? 0.3060 0.3605 0.2811 -0.0238 0.0009  -0.0316 106 ILE   A CB  
2213 C CG1 A ILE   A 106 ? 0.2201 0.4240 0.2771 -0.0472 -0.0520 -0.0168 106 ILE   A CG1 
2214 C CG1 B ILE   A 106 ? 0.3037 0.3579 0.2858 -0.0222 -0.0017 -0.0264 106 ILE   A CG1 
2215 C CG2 A ILE   A 106 ? 0.2350 0.4331 0.2651 -0.0595 -0.0542 -0.0386 106 ILE   A CG2 
2216 C CG2 B ILE   A 106 ? 0.3085 0.3639 0.2843 -0.0232 -0.0007 -0.0292 106 ILE   A CG2 
2217 C CD1 A ILE   A 106 ? 0.2197 0.4177 0.2915 -0.0378 -0.0432 -0.0010 106 ILE   A CD1 
2218 C CD1 B ILE   A 106 ? 0.3031 0.3551 0.2879 -0.0210 -0.0021 -0.0225 106 ILE   A CD1 
2241 N N   A GLN   A 107 ? 0.2325 0.3744 0.2484 -0.0880 -0.0090 -0.1167 107 GLN   A N   
2242 N N   B GLN   A 107 ? 0.2914 0.3286 0.2971 -0.0373 0.0176  -0.0595 107 GLN   A N   
2243 C CA  A GLN   A 107 ? 0.2607 0.3562 0.3326 -0.0736 0.0210  -0.1123 107 GLN   A CA  
2244 C CA  B GLN   A 107 ? 0.2828 0.3134 0.3202 -0.0396 0.0261  -0.0664 107 GLN   A CA  
2245 C C   A GLN   A 107 ? 0.2376 0.2968 0.3227 -0.0613 0.0411  -0.0840 107 GLN   A C   
2246 C C   B GLN   A 107 ? 0.2477 0.2784 0.2911 -0.0457 0.0377  -0.0678 107 GLN   A C   
2247 O O   A GLN   A 107 ? 0.2424 0.2859 0.3834 -0.0561 0.0574  -0.0754 107 GLN   A O   
2248 O O   B GLN   A 107 ? 0.2510 0.2769 0.3115 -0.0441 0.0445  -0.0648 107 GLN   A O   
2249 C CB  A GLN   A 107 ? 0.3038 0.3912 0.4326 -0.0805 0.0133  -0.1198 107 GLN   A CB  
2250 C CB  B GLN   A 107 ? 0.3071 0.3307 0.3767 -0.0381 0.0175  -0.0637 107 GLN   A CB  
2251 C CG  A GLN   A 107 ? 0.3447 0.4255 0.5437 -0.0818 0.0050  -0.1142 107 GLN   A CG  
2252 C CG  B GLN   A 107 ? 0.3283 0.3465 0.4361 -0.0355 0.0094  -0.0587 107 GLN   A CG  
2253 C CD  A GLN   A 107 ? 0.3789 0.4534 0.6384 -0.0811 0.0020  -0.1033 107 GLN   A CD  
2254 C CD  B GLN   A 107 ? 0.3450 0.3585 0.4851 -0.0325 0.0028  -0.0519 107 GLN   A CD  
2255 O OE1 A GLN   A 107 ? 0.3901 0.4597 0.6756 -0.0812 0.0020  -0.1018 107 GLN   A OE1 
2256 O OE1 B GLN   A 107 ? 0.3513 0.3616 0.5029 -0.0326 0.0018  -0.0486 107 GLN   A OE1 
2257 N NE2 A GLN   A 107 ? 0.3885 0.4611 0.6704 -0.0819 -0.0011 -0.1011 107 GLN   A NE2 
2258 N NE2 B GLN   A 107 ? 0.3501 0.3624 0.5010 -0.0310 0.0008  -0.0517 107 GLN   A NE2 
2275 N N   . LEU   A 108 ? 0.2086 0.2411 0.2434 -0.0534 0.0412  -0.0774 108 LEU   A N   
2276 C CA  . LEU   A 108 ? 0.1807 0.1814 0.2005 -0.0191 0.0359  -0.0248 108 LEU   A CA  
2277 C C   . LEU   A 108 ? 0.1564 0.1413 0.2016 -0.0054 0.0214  0.0052  108 LEU   A C   
2278 O O   . LEU   A 108 ? 0.1492 0.1440 0.2115 -0.0024 0.0263  0.0102  108 LEU   A O   
2279 C CB  . LEU   A 108 ? 0.1830 0.1901 0.1753 -0.0222 0.0373  -0.0174 108 LEU   A CB  
2280 C CG  . LEU   A 108 ? 0.2017 0.2175 0.2000 -0.0254 0.0442  -0.0215 108 LEU   A CG  
2281 C CD1 . LEU   A 108 ? 0.2256 0.2294 0.2080 -0.0340 0.0512  -0.0193 108 LEU   A CD1 
2282 C CD2 . LEU   A 108 ? 0.2053 0.2411 0.2482 -0.0171 0.0422  -0.0099 108 LEU   A CD2 
2295 N N   . LEU   A 109 ? 0.1416 0.1391 0.1954 0.0010  0.0155  0.0212  109 LEU   A N   
2296 C CA  . LEU   A 109 ? 0.1419 0.1318 0.1771 0.0008  0.0085  0.0198  109 LEU   A CA  
2297 C C   . LEU   A 109 ? 0.1321 0.1259 0.1614 -0.0083 0.0071  0.0124  109 LEU   A C   
2298 O O   . LEU   A 109 ? 0.1419 0.1172 0.1752 -0.0024 -0.0064 0.0060  109 LEU   A O   
2299 C CB  . LEU   A 109 ? 0.1462 0.1432 0.1863 0.0069  -0.0033 0.0323  109 LEU   A CB  
2300 C CG  . LEU   A 109 ? 0.1378 0.1473 0.1984 0.0019  0.0100  0.0350  109 LEU   A CG  
2301 C CD1 . LEU   A 109 ? 0.1390 0.1430 0.2167 0.0036  0.0186  0.0153  109 LEU   A CD1 
2302 C CD2 . LEU   A 109 ? 0.1402 0.1694 0.2094 0.0040  0.0025  0.0295  109 LEU   A CD2 
2314 N N   . LYS   A 110 ? 0.1347 0.1201 0.1632 -0.0051 0.0055  0.0068  110 LYS   A N   
2315 C CA  . LYS   A 110 ? 0.1299 0.1213 0.1691 -0.0063 0.0042  0.0096  110 LYS   A CA  
2316 C C   . LYS   A 110 ? 0.1293 0.1183 0.1512 -0.0088 0.0017  -0.0008 110 LYS   A C   
2317 O O   . LYS   A 110 ? 0.1304 0.1171 0.1616 -0.0107 0.0062  -0.0004 110 LYS   A O   
2318 C CB  . LYS   A 110 ? 0.1411 0.1219 0.1767 -0.0104 -0.0045 -0.0025 110 LYS   A CB  
2319 C CG  . LYS   A 110 ? 0.1461 0.1254 0.1843 -0.0060 -0.0087 -0.0046 110 LYS   A CG  
2320 C CD  . LYS   A 110 ? 0.1484 0.1290 0.1989 -0.0081 -0.0092 -0.0070 110 LYS   A CD  
2321 C CE  . LYS   A 110 ? 0.1566 0.1312 0.2173 -0.0052 0.0055  -0.0068 110 LYS   A CE  
2322 N NZ  . LYS   A 110 ? 0.1580 0.1342 0.2369 -0.0131 0.0114  -0.0020 110 LYS   A NZ  
2336 N N   . SER   A 111 ? 0.1298 0.1254 0.1515 -0.0034 0.0000  0.0031  111 SER   A N   
2337 C CA  . SER   A 111 ? 0.1233 0.1266 0.1640 0.0010  0.0020  0.0054  111 SER   A CA  
2338 C C   . SER   A 111 ? 0.1252 0.1195 0.1661 -0.0089 0.0047  0.0065  111 SER   A C   
2339 O O   . SER   A 111 ? 0.1345 0.1136 0.1749 -0.0033 0.0076  0.0115  111 SER   A O   
2340 C CB  . SER   A 111 ? 0.1468 0.1444 0.1737 -0.0005 0.0141  -0.0059 111 SER   A CB  
2341 O OG  . SER   A 111 ? 0.1950 0.1693 0.1867 -0.0006 0.0291  -0.0114 111 SER   A OG  
2347 N N   . ALA   A 112 ? 0.1270 0.1094 0.1724 -0.0039 0.0064  0.0107  112 ALA   A N   
2348 C CA  . ALA   A 112 ? 0.1299 0.1119 0.1565 -0.0037 0.0104  0.0081  112 ALA   A CA  
2349 C C   . ALA   A 112 ? 0.1249 0.1052 0.1605 -0.0038 0.0072  0.0036  112 ALA   A C   
2350 O O   . ALA   A 112 ? 0.1292 0.1084 0.1655 -0.0087 0.0047  0.0093  112 ALA   A O   
2351 C CB  . ALA   A 112 ? 0.1424 0.1104 0.1674 -0.0067 0.0133  0.0049  112 ALA   A CB  
2357 N N   . TYR   A 113 ? 0.1178 0.1148 0.1654 -0.0022 0.0081  0.0079  113 TYR   A N   
2358 C CA  . TYR   A 113 ? 0.1177 0.1107 0.1675 -0.0021 0.0132  0.0126  113 TYR   A CA  
2359 C C   . TYR   A 113 ? 0.1147 0.1114 0.1535 -0.0082 0.0054  0.0035  113 TYR   A C   
2360 O O   . TYR   A 113 ? 0.1214 0.1146 0.1633 -0.0045 0.0079  0.0059  113 TYR   A O   
2361 C CB  . TYR   A 113 ? 0.1197 0.1219 0.1692 -0.0025 -0.0020 0.0171  113 TYR   A CB  
2362 C CG  . TYR   A 113 ? 0.1178 0.1262 0.1543 -0.0136 0.0029  0.0206  113 TYR   A CG  
2363 C CD1 . TYR   A 113 ? 0.1232 0.1334 0.1523 -0.0065 0.0060  0.0226  113 TYR   A CD1 
2364 C CD2 . TYR   A 113 ? 0.1269 0.1290 0.1593 -0.0101 0.0038  0.0170  113 TYR   A CD2 
2365 C CE1 . TYR   A 113 ? 0.1232 0.1385 0.1471 -0.0067 0.0058  0.0262  113 TYR   A CE1 
2366 C CE2 . TYR   A 113 ? 0.1240 0.1340 0.1620 -0.0124 -0.0032 0.0210  113 TYR   A CE2 
2367 C CZ  . TYR   A 113 ? 0.1226 0.1363 0.1498 -0.0020 0.0113  0.0237  113 TYR   A CZ  
2368 O OH  . TYR   A 113 ? 0.1235 0.1477 0.1705 0.0066  0.0143  0.0258  113 TYR   A OH  
2378 N N   . GLU   A 114 ? 0.1206 0.1095 0.1621 -0.0034 0.0051  0.0133  114 GLU   A N   
2379 C CA  . GLU   A 114 ? 0.1248 0.1048 0.1682 0.0014  0.0041  0.0132  114 GLU   A CA  
2380 C C   . GLU   A 114 ? 0.1191 0.1152 0.1651 0.0035  0.0083  0.0107  114 GLU   A C   
2381 O O   . GLU   A 114 ? 0.1327 0.1190 0.1622 -0.0022 0.0013  0.0058  114 GLU   A O   
2382 C CB  . GLU   A 114 ? 0.1253 0.1122 0.1659 -0.0038 -0.0010 0.0090  114 GLU   A CB  
2383 C CG  . GLU   A 114 ? 0.1344 0.1114 0.1695 0.0026  0.0027  0.0004  114 GLU   A CG  
2384 C CD  . GLU   A 114 ? 0.1394 0.1156 0.1768 -0.0088 -0.0007 0.0044  114 GLU   A CD  
2385 O OE1 . GLU   A 114 ? 0.1415 0.1167 0.1851 -0.0084 0.0120  -0.0056 114 GLU   A OE1 
2386 O OE2 . GLU   A 114 ? 0.1571 0.1211 0.1992 -0.0146 0.0050  -0.0095 114 GLU   A OE2 
2393 N N   . ASN   A 115 ? 0.1213 0.1121 0.1607 -0.0037 0.0050  0.0063  115 ASN   A N   
2394 C CA  . ASN   A 115 ? 0.1218 0.1148 0.1629 -0.0085 -0.0013 0.0098  115 ASN   A CA  
2395 C C   . ASN   A 115 ? 0.1272 0.1105 0.1534 -0.0082 0.0016  0.0060  115 ASN   A C   
2396 O O   . ASN   A 115 ? 0.1276 0.1299 0.1577 -0.0142 0.0033  0.0146  115 ASN   A O   
2397 C CB  . ASN   A 115 ? 0.1313 0.1241 0.1531 -0.0169 0.0045  0.0010  115 ASN   A CB  
2398 C CG  . ASN   A 115 ? 0.1319 0.1483 0.1624 -0.0180 0.0176  0.0045  115 ASN   A CG  
2399 O OD1 . ASN   A 115 ? 0.1367 0.2440 0.1909 -0.0158 0.0219  0.0211  115 ASN   A OD1 
2400 N ND2 . ASN   A 115 ? 0.1331 0.1332 0.1645 -0.0153 0.0209  0.0082  115 ASN   A ND2 
2407 N N   . PHE   A 116 ? 0.1261 0.1134 0.1582 -0.0025 0.0106  0.0155  116 PHE   A N   
2408 C CA  . PHE   A 116 ? 0.1260 0.1249 0.1444 -0.0046 0.0166  0.0166  116 PHE   A CA  
2409 C C   . PHE   A 116 ? 0.1248 0.1286 0.1507 -0.0106 0.0097  0.0145  116 PHE   A C   
2410 O O   . PHE   A 116 ? 0.1310 0.1345 0.1599 0.0004  0.0083  0.0163  116 PHE   A O   
2411 C CB  . PHE   A 116 ? 0.1251 0.1134 0.1655 -0.0043 0.0125  0.0140  116 PHE   A CB  
2412 C CG  . PHE   A 116 ? 0.1243 0.1181 0.1510 -0.0094 0.0098  0.0091  116 PHE   A CG  
2413 C CD1 . PHE   A 116 ? 0.1267 0.1176 0.1530 -0.0090 0.0152  0.0092  116 PHE   A CD1 
2414 C CD2 . PHE   A 116 ? 0.1336 0.1228 0.1667 -0.0107 0.0123  0.0126  116 PHE   A CD2 
2415 C CE1 . PHE   A 116 ? 0.1297 0.1189 0.1624 -0.0105 0.0089  0.0067  116 PHE   A CE1 
2416 C CE2 . PHE   A 116 ? 0.1319 0.1219 0.1724 -0.0042 0.0148  0.0108  116 PHE   A CE2 
2417 C CZ  . PHE   A 116 ? 0.1328 0.1117 0.1635 -0.0001 0.0042  0.0148  116 PHE   A CZ  
2427 N N   . ASN   A 117 ? 0.1253 0.1213 0.1645 -0.0064 0.0078  0.0148  117 ASN   A N   
2428 C CA  . ASN   A 117 ? 0.1230 0.1192 0.1733 -0.0010 0.0074  0.0234  117 ASN   A CA  
2429 C C   . ASN   A 117 ? 0.1295 0.1254 0.1862 -0.0041 0.0096  0.0205  117 ASN   A C   
2430 O O   . ASN   A 117 ? 0.1374 0.1336 0.1984 -0.0074 -0.0100 0.0349  117 ASN   A O   
2431 C CB  . ASN   A 117 ? 0.1277 0.1252 0.1767 -0.0032 0.0054  0.0237  117 ASN   A CB  
2432 C CG  . ASN   A 117 ? 0.1274 0.1251 0.1759 -0.0047 0.0094  0.0252  117 ASN   A CG  
2433 O OD1 . ASN   A 117 ? 0.1301 0.1465 0.1811 -0.0163 0.0089  0.0163  117 ASN   A OD1 
2434 N ND2 . ASN   A 117 ? 0.1230 0.1268 0.1788 -0.0010 0.0073  0.0202  117 ASN   A ND2 
2441 N N   . GLN   A 118 ? 0.1249 0.1272 0.1899 -0.0071 -0.0051 0.0246  118 GLN   A N   
2442 C CA  . GLN   A 118 ? 0.1361 0.1413 0.1873 -0.0056 -0.0088 0.0160  118 GLN   A CA  
2443 C C   . GLN   A 118 ? 0.1412 0.1481 0.1707 -0.0051 -0.0117 0.0176  118 GLN   A C   
2444 O O   . GLN   A 118 ? 0.1461 0.1803 0.1965 0.0010  -0.0183 0.0003  118 GLN   A O   
2445 C CB  . GLN   A 118 ? 0.1289 0.1454 0.1861 -0.0057 -0.0081 0.0204  118 GLN   A CB  
2446 C CG  . GLN   A 118 ? 0.1243 0.1475 0.1949 -0.0090 -0.0032 0.0177  118 GLN   A CG  
2447 C CD  . GLN   A 118 ? 0.1227 0.1492 0.2063 0.0002  0.0028  0.0148  118 GLN   A CD  
2448 O OE1 . GLN   A 118 ? 0.1323 0.1583 0.2194 0.0047  -0.0079 0.0090  118 GLN   A OE1 
2449 N NE2 . GLN   A 118 ? 0.1358 0.1434 0.2003 0.0033  -0.0012 0.0207  118 GLN   A NE2 
2458 N N   . HIS   A 119 ? 0.1452 0.1397 0.1578 -0.0086 -0.0033 0.0206  119 HIS   A N   
2459 C CA  . HIS   A 119 ? 0.1522 0.1507 0.1678 -0.0080 -0.0045 0.0255  119 HIS   A CA  
2460 C C   . HIS   A 119 ? 0.1593 0.1519 0.1540 -0.0120 -0.0049 0.0162  119 HIS   A C   
2461 O O   . HIS   A 119 ? 0.1624 0.1627 0.1609 -0.0267 -0.0051 0.0291  119 HIS   A O   
2462 C CB  . HIS   A 119 ? 0.1565 0.1461 0.1796 -0.0063 0.0141  0.0312  119 HIS   A CB  
2463 C CG  . HIS   A 119 ? 0.1593 0.1509 0.2330 -0.0016 0.0102  0.0353  119 HIS   A CG  
2464 N ND1 . HIS   A 119 ? 0.1704 0.1725 0.2861 -0.0101 0.0112  0.0176  119 HIS   A ND1 
2465 C CD2 . HIS   A 119 ? 0.1661 0.1601 0.2558 0.0158  0.0311  0.0509  119 HIS   A CD2 
2466 C CE1 . HIS   A 119 ? 0.1698 0.1721 0.3082 -0.0154 0.0252  0.0388  119 HIS   A CE1 
2467 N NE2 . HIS   A 119 ? 0.1772 0.1619 0.2979 0.0053  0.0442  0.0597  119 HIS   A NE2 
2475 N N   . GLU   A 120 ? 0.1705 0.1732 0.1534 -0.0075 -0.0088 0.0384  120 GLU   A N   
2476 C CA  . GLU   A 120 ? 0.2094 0.2132 0.1806 0.0008  -0.0182 0.0809  120 GLU   A CA  
2477 C C   . GLU   A 120 ? 0.1768 0.1895 0.1592 -0.0219 -0.0024 0.0722  120 GLU   A C   
2478 O O   . GLU   A 120 ? 0.1743 0.1829 0.1748 -0.0201 -0.0047 0.0618  120 GLU   A O   
2479 C CB  . GLU   A 120 ? 0.3189 0.3164 0.2642 0.0248  -0.0333 0.1254  120 GLU   A CB  
2480 C CG  . GLU   A 120 ? 0.4408 0.4398 0.4270 0.0311  -0.0305 0.1122  120 GLU   A CG  
2481 C CD  . GLU   A 120 ? 0.5499 0.5453 0.5892 0.0315  -0.0225 0.0893  120 GLU   A CD  
2482 O OE1 . GLU   A 120 ? 0.5801 0.5671 0.6164 0.0315  -0.0205 0.0818  120 GLU   A OE1 
2483 O OE2 . GLU   A 120 ? 0.6376 0.6376 0.6762 0.0309  -0.0187 0.0816  120 GLU   A OE2 
2490 N N   . VAL   A 121 ? 0.1688 0.1896 0.1421 -0.0184 -0.0008 0.0539  121 VAL   A N   
2491 C CA  . VAL   A 121 ? 0.1766 0.1960 0.1326 -0.0204 0.0108  0.0498  121 VAL   A CA  
2492 C C   . VAL   A 121 ? 0.1649 0.1764 0.1255 -0.0228 0.0022  0.0331  121 VAL   A C   
2493 O O   . VAL   A 121 ? 0.1672 0.1819 0.1480 -0.0266 -0.0085 0.0271  121 VAL   A O   
2494 C CB  . VAL   A 121 ? 0.2164 0.2346 0.1730 -0.0047 0.0298  0.0581  121 VAL   A CB  
2495 C CG1 . VAL   A 121 ? 0.2232 0.2499 0.1812 0.0016  0.0318  0.0647  121 VAL   A CG1 
2496 C CG2 . VAL   A 121 ? 0.2369 0.2506 0.2192 -0.0108 0.0284  0.0385  121 VAL   A CG2 
2506 N N   . LEU   A 122 ? 0.1542 0.1529 0.1497 -0.0248 0.0066  0.0323  122 LEU   A N   
2507 C CA  . LEU   A 122 ? 0.1602 0.1431 0.1437 -0.0216 0.0237  0.0284  122 LEU   A CA  
2508 C C   . LEU   A 122 ? 0.1579 0.1449 0.1411 -0.0277 0.0041  0.0212  122 LEU   A C   
2509 O O   . LEU   A 122 ? 0.1613 0.1571 0.1765 -0.0276 0.0075  0.0289  122 LEU   A O   
2510 C CB  . LEU   A 122 ? 0.1847 0.1541 0.1866 -0.0131 0.0162  0.0405  122 LEU   A CB  
2511 C CG  . LEU   A 122 ? 0.1841 0.1588 0.1729 -0.0124 0.0244  0.0200  122 LEU   A CG  
2512 C CD1 . LEU   A 122 ? 0.1984 0.1543 0.1855 -0.0187 0.0246  0.0187  122 LEU   A CD1 
2513 C CD2 . LEU   A 122 ? 0.1784 0.1498 0.1702 -0.0165 0.0332  0.0175  122 LEU   A CD2 
2525 N N   A LEU   A 123 ? 0.1473 0.1427 0.1345 -0.0240 0.0003  0.0225  123 LEU   A N   
2526 N N   B LEU   A 123 ? 0.1593 0.1460 0.1417 -0.0231 0.0047  0.0156  123 LEU   A N   
2527 C CA  A LEU   A 123 ? 0.1490 0.1465 0.1309 -0.0232 0.0148  0.0241  123 LEU   A CA  
2528 C CA  B LEU   A 123 ? 0.1612 0.1476 0.1443 -0.0203 0.0091  0.0103  123 LEU   A CA  
2529 C C   A LEU   A 123 ? 0.1372 0.1361 0.1192 -0.0145 0.0156  0.0236  123 LEU   A C   
2530 C C   B LEU   A 123 ? 0.1600 0.1426 0.1391 -0.0159 0.0124  0.0071  123 LEU   A C   
2531 O O   A LEU   A 123 ? 0.1319 0.1380 0.1221 -0.0181 0.0069  0.0239  123 LEU   A O   
2532 O O   B LEU   A 123 ? 0.1604 0.1371 0.1416 -0.0126 0.0166  -0.0013 123 LEU   A O   
2533 C CB  A LEU   A 123 ? 0.1599 0.1578 0.1294 -0.0262 0.0206  0.0238  123 LEU   A CB  
2534 C CB  B LEU   A 123 ? 0.1644 0.1535 0.1510 -0.0211 0.0076  0.0069  123 LEU   A CB  
2535 C CG  A LEU   A 123 ? 0.1656 0.1746 0.1457 -0.0200 0.0252  0.0140  123 LEU   A CG  
2536 C CG  B LEU   A 123 ? 0.1629 0.1576 0.1498 -0.0216 0.0095  0.0058  123 LEU   A CG  
2537 C CD1 A LEU   A 123 ? 0.1686 0.1859 0.1667 -0.0100 0.0222  0.0072  123 LEU   A CD1 
2538 C CD1 B LEU   A 123 ? 0.1644 0.1608 0.1548 -0.0200 0.0094  0.0056  123 LEU   A CD1 
2539 C CD2 A LEU   A 123 ? 0.1782 0.1829 0.1451 -0.0143 0.0178  -0.0003 123 LEU   A CD2 
2540 C CD2 B LEU   A 123 ? 0.1643 0.1601 0.1504 -0.0207 0.0098  -0.0002 123 LEU   A CD2 
2563 N N   A ALA   A 124 ? 0.1342 0.1319 0.1272 -0.0160 0.0133  0.0228  124 ALA   A N   
2564 N N   B ALA   A 124 ? 0.1585 0.1447 0.1383 -0.0168 0.0057  0.0107  124 ALA   A N   
2565 C CA  A ALA   A 124 ? 0.1268 0.1342 0.1324 -0.0084 0.0106  0.0259  124 ALA   A CA  
2566 C CA  B ALA   A 124 ? 0.1583 0.1516 0.1398 -0.0176 0.0013  0.0140  124 ALA   A CA  
2567 C C   A ALA   A 124 ? 0.1210 0.1346 0.1385 -0.0137 0.0142  0.0277  124 ALA   A C   
2568 C C   B ALA   A 124 ? 0.1556 0.1538 0.1350 -0.0135 0.0037  0.0120  124 ALA   A C   
2569 O O   A ALA   A 124 ? 0.1281 0.1437 0.1590 -0.0072 0.0176  0.0331  124 ALA   A O   
2570 O O   B ALA   A 124 ? 0.1541 0.1546 0.1348 -0.0084 0.0015  0.0096  124 ALA   A O   
2571 C CB  A ALA   A 124 ? 0.1290 0.1338 0.1566 -0.0094 0.0083  0.0248  124 ALA   A CB  
2572 C CB  B ALA   A 124 ? 0.1605 0.1527 0.1464 -0.0217 -0.0019 0.0165  124 ALA   A CB  
2583 N N   A PRO   A 125 ? 0.1192 0.1358 0.1380 -0.0073 0.0048  0.0403  125 PRO   A N   
2584 N N   B PRO   A 125 ? 0.1560 0.1586 0.1314 -0.0079 0.0028  0.0128  125 PRO   A N   
2585 C CA  A PRO   A 125 ? 0.1284 0.1372 0.1451 -0.0047 0.0072  0.0339  125 PRO   A CA  
2586 C CA  B PRO   A 125 ? 0.1559 0.1598 0.1313 -0.0051 0.0047  0.0059  125 PRO   A CA  
2587 C C   A PRO   A 125 ? 0.1195 0.1393 0.1421 -0.0080 0.0064  0.0316  125 PRO   A C   
2588 C C   B PRO   A 125 ? 0.1471 0.1566 0.1272 -0.0044 0.0056  0.0058  125 PRO   A C   
2589 O O   A PRO   A 125 ? 0.1221 0.1380 0.1561 -0.0031 0.0078  0.0299  125 PRO   A O   
2590 O O   B PRO   A 125 ? 0.1459 0.1573 0.1356 -0.0065 0.0063  0.0090  125 PRO   A O   
2591 C CB  A PRO   A 125 ? 0.1392 0.1294 0.1313 -0.0055 0.0192  0.0296  125 PRO   A CB  
2592 C CB  B PRO   A 125 ? 0.1608 0.1618 0.1379 -0.0034 0.0116  0.0045  125 PRO   A CB  
2593 C CG  A PRO   A 125 ? 0.1349 0.1202 0.1430 -0.0112 0.0166  0.0232  125 PRO   A CG  
2594 C CG  B PRO   A 125 ? 0.1649 0.1618 0.1409 -0.0059 0.0088  0.0062  125 PRO   A CG  
2595 C CD  A PRO   A 125 ? 0.1285 0.1306 0.1464 -0.0153 0.0079  0.0281  125 PRO   A CD  
2596 C CD  B PRO   A 125 ? 0.1612 0.1616 0.1349 -0.0079 0.0063  0.0103  125 PRO   A CD  
2611 N N   A LEU   A 126 ? 0.1144 0.1407 0.1481 -0.0053 0.0100  0.0276  126 LEU   A N   
2612 N N   B LEU   A 126 ? 0.1438 0.1505 0.1247 -0.0026 0.0017  0.0027  126 LEU   A N   
2613 C CA  A LEU   A 126 ? 0.1211 0.1455 0.1621 -0.0063 0.0099  0.0288  126 LEU   A CA  
2614 C CA  B LEU   A 126 ? 0.1357 0.1410 0.1214 0.0016  0.0044  -0.0043 126 LEU   A CA  
2615 C C   A LEU   A 126 ? 0.1260 0.1382 0.1692 0.0028  0.0096  0.0302  126 LEU   A C   
2616 C C   B LEU   A 126 ? 0.1332 0.1282 0.1174 0.0063  0.0024  -0.0031 126 LEU   A C   
2617 O O   A LEU   A 126 ? 0.1329 0.1410 0.1821 0.0170  0.0215  0.0371  126 LEU   A O   
2618 O O   B LEU   A 126 ? 0.1393 0.1269 0.1218 0.0005  -0.0115 0.0028  126 LEU   A O   
2619 C CB  A LEU   A 126 ? 0.1308 0.1517 0.1677 -0.0033 0.0047  0.0289  126 LEU   A CB  
2620 C CB  B LEU   A 126 ? 0.1345 0.1478 0.1287 -0.0030 0.0065  -0.0139 126 LEU   A CB  
2621 C CG  A LEU   A 126 ? 0.1328 0.1725 0.1933 -0.0040 0.0160  0.0155  126 LEU   A CG  
2622 C CG  B LEU   A 126 ? 0.1271 0.1471 0.1303 -0.0042 0.0105  -0.0259 126 LEU   A CG  
2623 C CD1 A LEU   A 126 ? 0.1397 0.1906 0.2282 -0.0045 0.0110  0.0102  126 LEU   A CD1 
2624 C CD1 B LEU   A 126 ? 0.1235 0.1461 0.1381 -0.0041 0.0133  -0.0363 126 LEU   A CD1 
2625 C CD2 A LEU   A 126 ? 0.1390 0.1632 0.1870 -0.0154 0.0189  0.0202  126 LEU   A CD2 
2626 C CD2 B LEU   A 126 ? 0.1268 0.1479 0.1280 -0.0044 0.0067  -0.0238 126 LEU   A CD2 
2649 N N   A LEU   A 127 ? 0.1257 0.1318 0.1581 -0.0018 0.0072  0.0249  127 LEU   A N   
2650 N N   B LEU   A 127 ? 0.1272 0.1219 0.1180 0.0115  0.0088  0.0045  127 LEU   A N   
2651 C CA  A LEU   A 127 ? 0.1285 0.1360 0.1405 -0.0055 0.0019  0.0120  127 LEU   A CA  
2652 C CA  B LEU   A 127 ? 0.1295 0.1239 0.1241 0.0138  0.0000  0.0122  127 LEU   A CA  
2653 C C   A LEU   A 127 ? 0.1223 0.1296 0.1358 -0.0091 -0.0010 0.0109  127 LEU   A C   
2654 C C   B LEU   A 127 ? 0.1328 0.1258 0.1353 0.0084  -0.0125 0.0139  127 LEU   A C   
2655 O O   A LEU   A 127 ? 0.1316 0.1311 0.1345 -0.0139 0.0035  0.0161  127 LEU   A O   
2656 O O   B LEU   A 127 ? 0.1359 0.1286 0.1482 0.0117  -0.0091 0.0193  127 LEU   A O   
2657 C CB  A LEU   A 127 ? 0.1327 0.1335 0.1443 0.0015  0.0056  0.0139  127 LEU   A CB  
2658 C CB  B LEU   A 127 ? 0.1296 0.1335 0.1252 0.0147  -0.0048 0.0097  127 LEU   A CB  
2659 C CG  A LEU   A 127 ? 0.1369 0.1358 0.1473 0.0074  0.0022  0.0212  127 LEU   A CG  
2660 C CG  B LEU   A 127 ? 0.1287 0.1434 0.1177 0.0175  -0.0109 0.0078  127 LEU   A CG  
2661 C CD1 A LEU   A 127 ? 0.1416 0.1326 0.1681 0.0029  0.0119  0.0191  127 LEU   A CD1 
2662 C CD1 B LEU   A 127 ? 0.1238 0.1472 0.1209 0.0212  -0.0042 0.0097  127 LEU   A CD1 
2663 C CD2 A LEU   A 127 ? 0.1519 0.1342 0.1617 0.0201  -0.0142 0.0145  127 LEU   A CD2 
2664 C CD2 B LEU   A 127 ? 0.1369 0.1503 0.1044 0.0177  -0.0241 0.0014  127 LEU   A CD2 
2687 N N   A SER   A 128 ? 0.1281 0.1303 0.1296 -0.0105 0.0024  0.0164  128 SER   A N   
2688 N N   B SER   A 128 ? 0.1357 0.1224 0.1291 0.0009  -0.0237 0.0156  128 SER   A N   
2689 C CA  A SER   A 128 ? 0.1400 0.1305 0.1268 -0.0048 -0.0012 0.0108  128 SER   A CA  
2690 C CA  B SER   A 128 ? 0.1386 0.1196 0.1176 0.0001  -0.0259 0.0116  128 SER   A CA  
2691 C C   A SER   A 128 ? 0.1485 0.1350 0.1279 -0.0012 -0.0005 0.0144  128 SER   A C   
2692 C C   B SER   A 128 ? 0.1354 0.1230 0.1195 -0.0014 -0.0306 0.0068  128 SER   A C   
2693 O O   A SER   A 128 ? 0.1660 0.1490 0.1426 0.0025  -0.0072 0.0132  128 SER   A O   
2694 O O   B SER   A 128 ? 0.1334 0.1273 0.1391 0.0059  -0.0275 0.0058  128 SER   A O   
2695 C CB  A SER   A 128 ? 0.1364 0.1322 0.1380 -0.0105 0.0031  0.0133  128 SER   A CB  
2696 C CB  B SER   A 128 ? 0.1433 0.1207 0.1113 -0.0007 -0.0207 0.0186  128 SER   A CB  
2697 O OG  A SER   A 128 ? 0.1359 0.1434 0.1491 -0.0097 0.0004  -0.0006 128 SER   A OG  
2698 O OG  B SER   A 128 ? 0.1457 0.1232 0.1097 -0.0056 -0.0120 0.0293  128 SER   A OG  
2709 N N   A ALA   A 129 ? 0.1386 0.1418 0.1477 0.0027  0.0004  0.0165  129 ALA   A N   
2710 N N   B ALA   A 129 ? 0.1327 0.1246 0.1198 -0.0028 -0.0320 0.0022  129 ALA   A N   
2711 C CA  A ALA   A 129 ? 0.1360 0.1529 0.1469 -0.0012 0.0055  0.0205  129 ALA   A CA  
2712 C CA  B ALA   A 129 ? 0.1367 0.1327 0.1231 -0.0029 -0.0248 0.0013  129 ALA   A CA  
2713 C C   A ALA   A 129 ? 0.1365 0.1451 0.1377 -0.0002 -0.0023 0.0103  129 ALA   A C   
2714 C C   B ALA   A 129 ? 0.1471 0.1423 0.1238 -0.0010 -0.0279 0.0080  129 ALA   A C   
2715 O O   A ALA   A 129 ? 0.1416 0.1474 0.1436 -0.0100 0.0019  0.0125  129 ALA   A O   
2716 O O   B ALA   A 129 ? 0.1491 0.1436 0.1167 -0.0025 -0.0343 0.0163  129 ALA   A O   
2717 C CB  A ALA   A 129 ? 0.1431 0.1667 0.1744 0.0034  0.0082  0.0222  129 ALA   A CB  
2718 C CB  B ALA   A 129 ? 0.1376 0.1357 0.1186 -0.0048 -0.0194 -0.0006 129 ALA   A CB  
2729 N N   A GLY   A 130 ? 0.1407 0.1417 0.1736 -0.0008 0.0041  -0.0021 130 GLY   A N   
2730 N N   B GLY   A 130 ? 0.1519 0.1466 0.1207 -0.0025 -0.0286 0.0067  130 GLY   A N   
2731 C CA  A GLY   A 130 ? 0.1634 0.1437 0.1849 0.0065  0.0005  -0.0090 130 GLY   A CA  
2732 C CA  B GLY   A 130 ? 0.1625 0.1530 0.1271 -0.0033 -0.0283 0.0012  130 GLY   A CA  
2733 C C   A GLY   A 130 ? 0.1649 0.1335 0.1652 0.0111  -0.0129 -0.0086 130 GLY   A C   
2734 C C   B GLY   A 130 ? 0.1682 0.1577 0.1291 -0.0060 -0.0354 0.0000  130 GLY   A C   
2735 O O   A GLY   A 130 ? 0.1746 0.1302 0.1618 0.0019  -0.0272 -0.0103 130 GLY   A O   
2736 O O   B GLY   A 130 ? 0.1713 0.1584 0.1309 -0.0121 -0.0418 0.0020  130 GLY   A O   
2743 N N   A ILE   A 131 ? 0.1756 0.1291 0.1622 0.0017  -0.0204 0.0005  131 ILE   A N   
2744 N N   B ILE   A 131 ? 0.1751 0.1597 0.1399 -0.0082 -0.0346 0.0025  131 ILE   A N   
2745 C CA  A ILE   A 131 ? 0.1938 0.1233 0.1374 -0.0077 -0.0338 -0.0016 131 ILE   A CA  
2746 C CA  B ILE   A 131 ? 0.1839 0.1608 0.1456 -0.0090 -0.0318 0.0031  131 ILE   A CA  
2747 C C   A ILE   A 131 ? 0.1834 0.1269 0.1248 -0.0146 -0.0303 0.0096  131 ILE   A C   
2748 C C   B ILE   A 131 ? 0.1866 0.1616 0.1488 -0.0104 -0.0185 0.0179  131 ILE   A C   
2749 O O   A ILE   A 131 ? 0.1934 0.1399 0.1574 -0.0026 -0.0218 0.0225  131 ILE   A O   
2750 O O   B ILE   A 131 ? 0.1910 0.1647 0.1550 -0.0100 -0.0152 0.0278  131 ILE   A O   
2751 C CB  A ILE   A 131 ? 0.2180 0.1468 0.1438 -0.0213 -0.0411 -0.0077 131 ILE   A CB  
2752 C CB  B ILE   A 131 ? 0.1893 0.1671 0.1514 -0.0083 -0.0323 -0.0087 131 ILE   A CB  
2753 C CG1 A ILE   A 131 ? 0.2240 0.1856 0.1681 -0.0341 -0.0417 -0.0060 131 ILE   A CG1 
2754 C CG1 B ILE   A 131 ? 0.1911 0.1832 0.1606 -0.0073 -0.0299 -0.0174 131 ILE   A CG1 
2755 C CG2 A ILE   A 131 ? 0.2335 0.1381 0.1707 -0.0131 -0.0335 -0.0234 131 ILE   A CG2 
2756 C CG2 B ILE   A 131 ? 0.1908 0.1591 0.1416 -0.0048 -0.0377 -0.0148 131 ILE   A CG2 
2757 C CD1 A ILE   A 131 ? 0.2284 0.2002 0.2021 -0.0445 -0.0409 -0.0179 131 ILE   A CD1 
2758 C CD1 B ILE   A 131 ? 0.1896 0.1921 0.1747 -0.0053 -0.0304 -0.0235 131 ILE   A CD1 
2781 N N   A PHE   A 132 ? 0.1745 0.1288 0.1080 -0.0042 -0.0218 0.0131  132 PHE   A N   
2782 N N   B PHE   A 132 ? 0.1866 0.1594 0.1470 -0.0079 -0.0134 0.0139  132 PHE   A N   
2783 C CA  A PHE   A 132 ? 0.1697 0.1387 0.1131 -0.0139 -0.0099 0.0123  132 PHE   A CA  
2784 C CA  B PHE   A 132 ? 0.1865 0.1601 0.1461 -0.0072 -0.0107 0.0122  132 PHE   A CA  
2785 C C   A PHE   A 132 ? 0.1741 0.1600 0.1081 -0.0052 -0.0006 0.0067  132 PHE   A C   
2786 C C   B PHE   A 132 ? 0.1875 0.1630 0.1485 -0.0097 -0.0158 0.0165  132 PHE   A C   
2787 O O   A PHE   A 132 ? 0.1763 0.1697 0.1191 -0.0115 0.0047  0.0058  132 PHE   A O   
2788 O O   B PHE   A 132 ? 0.1916 0.1704 0.1524 -0.0135 -0.0108 0.0284  132 PHE   A O   
2789 C CB  A PHE   A 132 ? 0.1575 0.1328 0.1189 -0.0104 -0.0117 0.0193  132 PHE   A CB  
2790 C CB  B PHE   A 132 ? 0.1849 0.1597 0.1423 -0.0000 -0.0022 0.0082  132 PHE   A CB  
2791 C CG  A PHE   A 132 ? 0.1552 0.1333 0.1216 -0.0050 -0.0154 0.0151  132 PHE   A CG  
2792 C CG  B PHE   A 132 ? 0.1839 0.1583 0.1367 0.0079  0.0096  0.0026  132 PHE   A CG  
2793 C CD1 A PHE   A 132 ? 0.1564 0.1450 0.1532 -0.0007 -0.0154 -0.0000 132 PHE   A CD1 
2794 C CD1 B PHE   A 132 ? 0.1810 0.1583 0.1407 0.0074  0.0118  0.0004  132 PHE   A CD1 
2795 C CD2 A PHE   A 132 ? 0.1598 0.1477 0.1409 0.0013  -0.0161 0.0011  132 PHE   A CD2 
2796 C CD2 B PHE   A 132 ? 0.1835 0.1599 0.1380 0.0116  0.0174  -0.0022 132 PHE   A CD2 
2797 C CE1 A PHE   A 132 ? 0.1566 0.1474 0.1608 -0.0023 -0.0157 -0.0068 132 PHE   A CE1 
2798 C CE1 B PHE   A 132 ? 0.1796 0.1586 0.1356 0.0094  0.0155  -0.0007 132 PHE   A CE1 
2799 C CE2 A PHE   A 132 ? 0.1571 0.1544 0.1591 0.0041  -0.0176 0.0027  132 PHE   A CE2 
2800 C CE2 B PHE   A 132 ? 0.1815 0.1599 0.1355 0.0141  0.0187  -0.0004 132 PHE   A CE2 
2801 C CZ  A PHE   A 132 ? 0.1530 0.1471 0.1629 -0.0063 -0.0234 0.0035  132 PHE   A CZ  
2802 C CZ  B PHE   A 132 ? 0.1795 0.1583 0.1319 0.0131  0.0159  0.0009  132 PHE   A CZ  
2821 N N   A GLY   A 133 ? 0.1758 0.1564 0.1121 -0.0032 -0.0192 0.0071  133 GLY   A N   
2822 N N   B GLY   A 133 ? 0.1836 0.1535 0.1398 -0.0091 -0.0241 0.0117  133 GLY   A N   
2823 C CA  A GLY   A 133 ? 0.1853 0.1684 0.1308 0.0024  -0.0242 -0.0050 133 GLY   A CA  
2824 C CA  B GLY   A 133 ? 0.1819 0.1499 0.1411 -0.0101 -0.0269 0.0034  133 GLY   A CA  
2825 C C   A GLY   A 133 ? 0.1878 0.1781 0.1406 -0.0026 -0.0312 -0.0144 133 GLY   A C   
2826 C C   B GLY   A 133 ? 0.1806 0.1507 0.1526 -0.0135 -0.0299 -0.0045 133 GLY   A C   
2827 O O   A GLY   A 133 ? 0.2091 0.1922 0.1633 -0.0014 -0.0458 -0.0343 133 GLY   A O   
2828 O O   B GLY   A 133 ? 0.1888 0.1599 0.1541 -0.0090 -0.0320 -0.0093 133 GLY   A O   
2835 N N   A ALA   A 134 ? 0.1770 0.1706 0.1466 -0.0079 -0.0220 -0.0110 134 ALA   A N   
2836 N N   B ALA   A 134 ? 0.1729 0.1413 0.1527 -0.0213 -0.0283 -0.0060 134 ALA   A N   
2837 C CA  A ALA   A 134 ? 0.1749 0.1719 0.1719 -0.0074 -0.0219 -0.0126 134 ALA   A CA  
2838 C CA  B ALA   A 134 ? 0.1708 0.1376 0.1594 -0.0240 -0.0280 -0.0115 134 ALA   A CA  
2839 C C   A ALA   A 134 ? 0.1710 0.1802 0.1741 -0.0061 -0.0220 0.0125  134 ALA   A C   
2840 C C   B ALA   A 134 ? 0.1694 0.1403 0.1562 -0.0164 -0.0282 -0.0142 134 ALA   A C   
2841 O O   A ALA   A 134 ? 0.1788 0.1921 0.1935 -0.0037 -0.0022 0.0139  134 ALA   A O   
2842 O O   B ALA   A 134 ? 0.1706 0.1431 0.1600 -0.0148 -0.0181 -0.0144 134 ALA   A O   
2843 C CB  A ALA   A 134 ? 0.1847 0.1705 0.2123 -0.0030 -0.0198 -0.0201 134 ALA   A CB  
2844 C CB  B ALA   A 134 ? 0.1701 0.1360 0.1746 -0.0279 -0.0248 -0.0123 134 ALA   A CB  
2855 N N   A ASP   A 135 ? 0.1755 0.1861 0.1893 -0.0161 -0.0246 0.0234  135 ASP   A N   
2856 N N   B ASP   A 135 ? 0.1699 0.1436 0.1552 -0.0144 -0.0310 -0.0092 135 ASP   A N   
2857 C CA  A ASP   A 135 ? 0.1701 0.1966 0.2246 -0.0229 -0.0387 0.0335  135 ASP   A CA  
2858 C CA  B ASP   A 135 ? 0.1666 0.1508 0.1634 -0.0104 -0.0320 -0.0026 135 ASP   A CA  
2859 C C   A ASP   A 135 ? 0.1594 0.1863 0.2260 -0.0219 -0.0259 0.0462  135 ASP   A C   
2860 C C   B ASP   A 135 ? 0.1610 0.1449 0.1637 -0.0015 -0.0145 0.0037  135 ASP   A C   
2861 O O   A ASP   A 135 ? 0.1574 0.1776 0.2344 -0.0175 -0.0310 0.0432  135 ASP   A O   
2862 O O   B ASP   A 135 ? 0.1575 0.1432 0.1628 0.0008  -0.0140 -0.0006 135 ASP   A O   
2863 C CB  A ASP   A 135 ? 0.1931 0.2271 0.2637 -0.0349 -0.0546 0.0189  135 ASP   A CB  
2864 C CB  B ASP   A 135 ? 0.1704 0.1636 0.1664 -0.0103 -0.0466 -0.0077 135 ASP   A CB  
2865 C CG  A ASP   A 135 ? 0.2148 0.2567 0.3119 -0.0414 -0.0543 0.0146  135 ASP   A CG  
2866 C CG  B ASP   A 135 ? 0.1749 0.1804 0.1740 -0.0093 -0.0582 -0.0164 135 ASP   A CG  
2867 O OD1 A ASP   A 135 ? 0.2124 0.2690 0.3133 -0.0439 -0.0609 0.0316  135 ASP   A OD1 
2868 O OD1 B ASP   A 135 ? 0.1780 0.1796 0.1821 -0.0036 -0.0558 -0.0165 135 ASP   A OD1 
2869 O OD2 A ASP   A 135 ? 0.2459 0.2756 0.3663 -0.0390 -0.0341 0.0112  135 ASP   A OD2 
2870 O OD2 B ASP   A 135 ? 0.1755 0.1920 0.1801 -0.0102 -0.0685 -0.0254 135 ASP   A OD2 
2879 N N   A PRO   A 136 ? 0.1479 0.1955 0.2368 -0.0037 -0.0110 0.0559  136 PRO   A N   
2880 N N   B PRO   A 136 ? 0.1591 0.1462 0.1689 0.0092  0.0046  0.0152  136 PRO   A N   
2881 C CA  A PRO   A 136 ? 0.1443 0.1995 0.2434 -0.0096 0.0034  0.0503  136 PRO   A CA  
2882 C CA  B PRO   A 136 ? 0.1604 0.1507 0.1749 0.0080  0.0109  0.0160  136 PRO   A CA  
2883 C C   A PRO   A 136 ? 0.1246 0.1937 0.2434 -0.0043 0.0040  0.0448  136 PRO   A C   
2884 C C   B PRO   A 136 ? 0.1606 0.1559 0.1780 0.0077  0.0055  0.0206  136 PRO   A C   
2885 O O   A PRO   A 136 ? 0.1229 0.1871 0.2348 -0.0086 0.0028  0.0418  136 PRO   A O   
2886 O O   B PRO   A 136 ? 0.1597 0.1534 0.1699 0.0067  0.0026  0.0190  136 PRO   A O   
2887 C CB  A PRO   A 136 ? 0.1695 0.2071 0.2633 -0.0009 0.0049  0.0552  136 PRO   A CB  
2888 C CB  B PRO   A 136 ? 0.1652 0.1507 0.1832 0.0112  0.0191  0.0156  136 PRO   A CB  
2889 C CG  A PRO   A 136 ? 0.1842 0.2203 0.2853 0.0082  0.0042  0.0505  136 PRO   A CG  
2890 C CG  B PRO   A 136 ? 0.1673 0.1538 0.1889 0.0132  0.0222  0.0179  136 PRO   A CG  
2891 C CD  A PRO   A 136 ? 0.1686 0.2079 0.2647 0.0121  0.0018  0.0634  136 PRO   A CD  
2892 C CD  B PRO   A 136 ? 0.1636 0.1477 0.1755 0.0149  0.0171  0.0258  136 PRO   A CD  
2907 N N   A ILE   A 137 ? 0.1206 0.1958 0.2488 -0.0027 -0.0093 0.0410  137 ILE   A N   
2908 N N   B ILE   A 137 ? 0.1639 0.1634 0.1896 0.0063  -0.0040 0.0252  137 ILE   A N   
2909 C CA  A ILE   A 137 ? 0.1242 0.2043 0.2526 -0.0139 -0.0174 0.0333  137 ILE   A CA  
2910 C CA  B ILE   A 137 ? 0.1672 0.1726 0.2021 0.0009  -0.0103 0.0247  137 ILE   A CA  
2911 C C   A ILE   A 137 ? 0.1272 0.1893 0.2328 -0.0221 -0.0171 0.0322  137 ILE   A C   
2912 C C   B ILE   A 137 ? 0.1638 0.1706 0.1928 -0.0021 -0.0104 0.0264  137 ILE   A C   
2913 O O   A ILE   A 137 ? 0.1339 0.1856 0.2362 -0.0254 -0.0136 0.0315  137 ILE   A O   
2914 O O   B ILE   A 137 ? 0.1667 0.1693 0.1924 -0.0017 -0.0097 0.0298  137 ILE   A O   
2915 C CB  A ILE   A 137 ? 0.1269 0.2289 0.2816 -0.0173 -0.0328 0.0307  137 ILE   A CB  
2916 C CB  B ILE   A 137 ? 0.1742 0.1837 0.2257 -0.0016 -0.0194 0.0218  137 ILE   A CB  
2917 C CG1 A ILE   A 137 ? 0.1364 0.2553 0.3290 -0.0088 -0.0351 0.0303  137 ILE   A CG1 
2918 C CG1 B ILE   A 137 ? 0.1804 0.1960 0.2504 -0.0002 -0.0222 0.0192  137 ILE   A CG1 
2919 C CG2 A ILE   A 137 ? 0.1401 0.2299 0.2909 -0.0263 -0.0441 0.0333  137 ILE   A CG2 
2920 C CG2 B ILE   A 137 ? 0.1782 0.1841 0.2315 -0.0054 -0.0246 0.0221  137 ILE   A CG2 
2921 C CD1 A ILE   A 137 ? 0.1549 0.2733 0.3564 0.0016  -0.0302 0.0337  137 ILE   A CD1 
2922 C CD1 B ILE   A 137 ? 0.1868 0.2048 0.2661 0.0017  -0.0210 0.0196  137 ILE   A CD1 
2945 N N   A HIS   A 138 ? 0.1278 0.1925 0.2218 -0.0197 -0.0086 0.0280  138 HIS   A N   
2946 N N   B HIS   A 138 ? 0.1586 0.1733 0.1890 -0.0039 -0.0074 0.0228  138 HIS   A N   
2947 C CA  A HIS   A 138 ? 0.1417 0.1880 0.1975 -0.0224 -0.0098 0.0263  138 HIS   A CA  
2948 C CA  B HIS   A 138 ? 0.1553 0.1720 0.1804 -0.0073 -0.0069 0.0199  138 HIS   A CA  
2949 C C   A HIS   A 138 ? 0.1329 0.1766 0.1872 -0.0100 -0.0041 0.0280  138 HIS   A C   
2950 C C   B HIS   A 138 ? 0.1418 0.1709 0.1785 -0.0066 -0.0056 0.0279  138 HIS   A C   
2951 O O   A HIS   A 138 ? 0.1438 0.1734 0.1865 -0.0097 0.0011  0.0164  138 HIS   A O   
2952 O O   B HIS   A 138 ? 0.1457 0.1719 0.1730 -0.0078 -0.0037 0.0258  138 HIS   A O   
2953 C CB  A HIS   A 138 ? 0.1588 0.2037 0.1957 -0.0243 -0.0184 0.0146  138 HIS   A CB  
2954 C CB  B HIS   A 138 ? 0.1627 0.1748 0.1798 -0.0068 -0.0090 0.0062  138 HIS   A CB  
2955 C CG  A HIS   A 138 ? 0.1781 0.2123 0.1985 -0.0257 -0.0205 0.0088  138 HIS   A CG  
2956 C CG  B HIS   A 138 ? 0.1710 0.1752 0.1833 -0.0062 -0.0104 -0.0059 138 HIS   A CG  
2957 N ND1 A HIS   A 138 ? 0.1879 0.2261 0.2257 -0.0278 -0.0246 -0.0042 138 HIS   A ND1 
2958 N ND1 B HIS   A 138 ? 0.1747 0.1789 0.1932 -0.0063 -0.0120 -0.0143 138 HIS   A ND1 
2959 C CD2 A HIS   A 138 ? 0.1824 0.2136 0.1958 -0.0143 -0.0155 0.0175  138 HIS   A CD2 
2960 C CD2 B HIS   A 138 ? 0.1734 0.1725 0.1827 -0.0022 -0.0093 -0.0071 138 HIS   A CD2 
2961 C CE1 A HIS   A 138 ? 0.1941 0.2293 0.2240 -0.0132 -0.0245 -0.0022 138 HIS   A CE1 
2962 C CE1 B HIS   A 138 ? 0.1762 0.1770 0.1907 -0.0024 -0.0142 -0.0141 138 HIS   A CE1 
2963 N NE2 A HIS   A 138 ? 0.1929 0.2258 0.2065 -0.0091 -0.0106 0.0055  138 HIS   A NE2 
2964 N NE2 B HIS   A 138 ? 0.1766 0.1748 0.1850 -0.0009 -0.0109 -0.0122 138 HIS   A NE2 
2979 N N   . SER   A 139 ? 0.1282 0.1668 0.1874 -0.0081 -0.0069 0.0367  139 SER   A N   
2980 C CA  . SER   A 139 ? 0.1238 0.1598 0.1825 -0.0094 -0.0047 0.0368  139 SER   A CA  
2981 C C   . SER   A 139 ? 0.1176 0.1483 0.1836 -0.0067 0.0011  0.0224  139 SER   A C   
2982 O O   . SER   A 139 ? 0.1163 0.1422 0.1980 -0.0080 0.0054  0.0278  139 SER   A O   
2983 C CB  . SER   A 139 ? 0.1298 0.1635 0.1933 -0.0156 -0.0079 0.0381  139 SER   A CB  
2984 O OG  . SER   A 139 ? 0.1365 0.1583 0.1952 -0.0198 -0.0088 0.0480  139 SER   A OG  
2991 N N   . LEU   A 140 ? 0.1173 0.1555 0.1826 -0.0074 -0.0005 0.0378  140 LEU   A N   
2992 C CA  . LEU   A 140 ? 0.1219 0.1536 0.1771 -0.0071 0.0065  0.0322  140 LEU   A CA  
2993 C C   . LEU   A 140 ? 0.1156 0.1593 0.1806 -0.0150 0.0043  0.0327  140 LEU   A C   
2994 O O   . LEU   A 140 ? 0.1211 0.1566 0.1949 -0.0067 -0.0000 0.0336  140 LEU   A O   
2995 C CB  . LEU   A 140 ? 0.1227 0.1656 0.1804 -0.0073 0.0066  0.0271  140 LEU   A CB  
2996 C CG  . LEU   A 140 ? 0.1243 0.1804 0.1889 -0.0147 0.0132  0.0352  140 LEU   A CG  
2997 C CD1 . LEU   A 140 ? 0.1283 0.1830 0.1832 -0.0146 0.0077  0.0345  140 LEU   A CD1 
2998 C CD2 . LEU   A 140 ? 0.1273 0.1965 0.2058 -0.0100 0.0218  0.0408  140 LEU   A CD2 
3010 N N   . ARG   A 141 ? 0.1240 0.1648 0.1911 -0.0141 0.0031  0.0326  141 ARG   A N   
3011 C CA  . ARG   A 141 ? 0.1357 0.1741 0.2045 -0.0238 -0.0064 0.0117  141 ARG   A CA  
3012 C C   . ARG   A 141 ? 0.1364 0.1525 0.1847 -0.0173 -0.0133 0.0150  141 ARG   A C   
3013 O O   . ARG   A 141 ? 0.1332 0.1502 0.1992 -0.0172 0.0009  0.0099  141 ARG   A O   
3014 C CB  . ARG   A 141 ? 0.1456 0.1974 0.2345 -0.0284 -0.0163 -0.0003 141 ARG   A CB  
3015 C CG  . ARG   A 141 ? 0.1840 0.2332 0.2686 -0.0308 -0.0053 -0.0120 141 ARG   A CG  
3016 C CD  . ARG   A 141 ? 0.2111 0.2534 0.2808 -0.0383 0.0005  -0.0139 141 ARG   A CD  
3017 N NE  . ARG   A 141 ? 0.2074 0.2662 0.2865 -0.0443 -0.0023 -0.0080 141 ARG   A NE  
3018 C CZ  . ARG   A 141 ? 0.2082 0.2847 0.2915 -0.0556 0.0058  0.0015  141 ARG   A CZ  
3019 N NH1 . ARG   A 141 ? 0.2025 0.2901 0.2949 -0.0637 0.0230  -0.0138 141 ARG   A NH1 
3020 N NH2 . ARG   A 141 ? 0.2125 0.2931 0.3076 -0.0472 -0.0088 0.0156  141 ARG   A NH2 
3034 N N   . VAL   A 142 ? 0.1276 0.1496 0.1848 -0.0129 -0.0034 0.0107  142 VAL   A N   
3035 C CA  . VAL   A 142 ? 0.1318 0.1429 0.1831 -0.0123 0.0092  0.0138  142 VAL   A CA  
3036 C C   . VAL   A 142 ? 0.1209 0.1387 0.1781 -0.0171 0.0096  0.0154  142 VAL   A C   
3037 O O   . VAL   A 142 ? 0.1242 0.1438 0.1811 -0.0023 0.0090  0.0166  142 VAL   A O   
3038 C CB  . VAL   A 142 ? 0.1391 0.1542 0.1735 -0.0121 0.0095  0.0137  142 VAL   A CB  
3039 C CG1 . VAL   A 142 ? 0.1438 0.1516 0.1807 -0.0160 0.0130  0.0166  142 VAL   A CG1 
3040 C CG2 . VAL   A 142 ? 0.1541 0.1716 0.1884 -0.0021 0.0047  0.0186  142 VAL   A CG2 
3050 N N   . CYS   A 143 ? 0.1249 0.1438 0.1687 -0.0122 0.0044  0.0138  143 CYS   A N   
3051 C CA  . CYS   A 143 ? 0.1284 0.1424 0.1674 -0.0156 0.0063  0.0103  143 CYS   A CA  
3052 C C   . CYS   A 143 ? 0.1221 0.1367 0.1747 -0.0114 0.0042  0.0170  143 CYS   A C   
3053 O O   . CYS   A 143 ? 0.1233 0.1384 0.1799 -0.0093 0.0055  0.0292  143 CYS   A O   
3054 C CB  . CYS   A 143 ? 0.1410 0.1430 0.1745 -0.0145 0.0136  0.0210  143 CYS   A CB  
3055 S SG  . CYS   A 143 ? 0.1592 0.1536 0.1645 -0.0024 0.0136  0.0148  143 CYS   A SG  
3061 N N   . VAL   A 144 ? 0.1229 0.1459 0.1872 -0.0109 0.0054  0.0307  144 VAL   A N   
3062 C CA  . VAL   A 144 ? 0.1270 0.1510 0.2239 -0.0186 0.0132  0.0376  144 VAL   A CA  
3063 C C   . VAL   A 144 ? 0.1355 0.1417 0.2109 -0.0240 -0.0085 0.0262  144 VAL   A C   
3064 O O   . VAL   A 144 ? 0.1519 0.1512 0.2221 -0.0121 -0.0112 0.0371  144 VAL   A O   
3065 C CB  . VAL   A 144 ? 0.1509 0.1805 0.2918 -0.0077 0.0243  0.0466  144 VAL   A CB  
3066 C CG1 . VAL   A 144 ? 0.1600 0.2023 0.3293 -0.0134 0.0062  0.0510  144 VAL   A CG1 
3067 C CG2 . VAL   A 144 ? 0.1361 0.1898 0.2919 -0.0066 0.0321  0.0541  144 VAL   A CG2 
3077 N N   . ASP   A 145 ? 0.1399 0.1431 0.2151 -0.0254 -0.0013 0.0203  145 ASP   A N   
3078 C CA  . ASP   A 145 ? 0.1538 0.1456 0.2278 -0.0282 -0.0088 0.0100  145 ASP   A CA  
3079 C C   . ASP   A 145 ? 0.1559 0.1329 0.2232 -0.0157 -0.0074 -0.0019 145 ASP   A C   
3080 O O   . ASP   A 145 ? 0.1649 0.1471 0.2803 -0.0226 -0.0106 -0.0328 145 ASP   A O   
3081 C CB  . ASP   A 145 ? 0.1734 0.1698 0.2467 -0.0308 -0.0230 0.0009  145 ASP   A CB  
3082 C CG  . ASP   A 145 ? 0.1881 0.2030 0.2706 -0.0484 -0.0350 0.0184  145 ASP   A CG  
3083 O OD1 . ASP   A 145 ? 0.1826 0.2152 0.2784 -0.0616 -0.0221 0.0209  145 ASP   A OD1 
3084 O OD2 . ASP   A 145 ? 0.2044 0.2255 0.2814 -0.0588 -0.0470 0.0231  145 ASP   A OD2 
3089 N N   . THR   A 146 ? 0.1367 0.1302 0.1881 -0.0133 -0.0000 0.0070  146 THR   A N   
3090 C CA  . THR   A 146 ? 0.1308 0.1275 0.1732 -0.0086 -0.0000 0.0022  146 THR   A CA  
3091 C C   . THR   A 146 ? 0.1278 0.1249 0.1800 -0.0052 0.0029  0.0112  146 THR   A C   
3092 O O   . THR   A 146 ? 0.1407 0.1386 0.1909 0.0063  -0.0064 0.0078  146 THR   A O   
3093 C CB  . THR   A 146 ? 0.1321 0.1331 0.1714 -0.0051 0.0017  0.0112  146 THR   A CB  
3094 O OG1 . THR   A 146 ? 0.1281 0.1481 0.1862 -0.0024 0.0018  0.0081  146 THR   A OG1 
3095 C CG2 . THR   A 146 ? 0.1340 0.1325 0.1869 -0.0111 0.0000  0.0081  146 THR   A CG2 
3103 N N   . VAL   A 147 ? 0.1240 0.1304 0.1744 -0.0021 0.0063  0.0149  147 VAL   A N   
3104 C CA  . VAL   A 147 ? 0.1298 0.1329 0.1668 -0.0094 0.0140  0.0252  147 VAL   A CA  
3105 C C   . VAL   A 147 ? 0.1299 0.1269 0.1792 -0.0157 0.0099  0.0228  147 VAL   A C   
3106 O O   . VAL   A 147 ? 0.1343 0.1340 0.2036 -0.0181 0.0068  0.0223  147 VAL   A O   
3107 C CB  . VAL   A 147 ? 0.1427 0.1318 0.1674 -0.0144 0.0187  0.0197  147 VAL   A CB  
3108 C CG1 . VAL   A 147 ? 0.1663 0.1376 0.1686 -0.0087 0.0155  0.0264  147 VAL   A CG1 
3109 C CG2 . VAL   A 147 ? 0.1496 0.1292 0.1661 -0.0169 0.0052  0.0187  147 VAL   A CG2 
3119 N N   . ARG   A 148 ? 0.1293 0.1281 0.1909 -0.0129 0.0080  0.0322  148 ARG   A N   
3120 C CA  . ARG   A 148 ? 0.1394 0.1327 0.1929 -0.0091 0.0017  0.0386  148 ARG   A CA  
3121 C C   . ARG   A 148 ? 0.1533 0.1378 0.1900 -0.0177 0.0043  0.0498  148 ARG   A C   
3122 O O   . ARG   A 148 ? 0.1828 0.1535 0.2045 -0.0228 0.0076  0.0474  148 ARG   A O   
3123 C CB  . ARG   A 148 ? 0.1425 0.1348 0.2174 -0.0070 0.0113  0.0386  148 ARG   A CB  
3124 C CG  . ARG   A 148 ? 0.1540 0.1334 0.2421 -0.0095 0.0185  0.0222  148 ARG   A CG  
3125 C CD  . ARG   A 148 ? 0.1723 0.1387 0.2627 -0.0086 0.0258  0.0366  148 ARG   A CD  
3126 N NE  . ARG   A 148 ? 0.1608 0.1396 0.2569 0.0080  0.0356  0.0416  148 ARG   A NE  
3127 C CZ  . ARG   A 148 ? 0.1609 0.1299 0.2438 0.0001  0.0356  0.0326  148 ARG   A CZ  
3128 N NH1 . ARG   A 148 ? 0.1726 0.1324 0.2502 -0.0082 0.0358  0.0127  148 ARG   A NH1 
3129 N NH2 . ARG   A 148 ? 0.1595 0.1505 0.2377 0.0109  0.0360  0.0423  148 ARG   A NH2 
3143 N N   . THR   A 149 ? 0.1580 0.1433 0.1727 -0.0210 -0.0016 0.0419  149 THR   A N   
3144 C CA  . THR   A 149 ? 0.1573 0.1511 0.1719 -0.0169 -0.0000 0.0429  149 THR   A CA  
3145 C C   . THR   A 149 ? 0.1517 0.1516 0.1636 -0.0244 -0.0009 0.0470  149 THR   A C   
3146 O O   . THR   A 149 ? 0.1510 0.1591 0.1962 -0.0238 0.0022  0.0430  149 THR   A O   
3147 C CB  . THR   A 149 ? 0.1553 0.1660 0.1808 -0.0175 -0.0003 0.0320  149 THR   A CB  
3148 O OG1 . THR   A 149 ? 0.1574 0.1508 0.1888 -0.0260 -0.0004 0.0292  149 THR   A OG1 
3149 C CG2 . THR   A 149 ? 0.1526 0.1774 0.1990 -0.0087 -0.0080 0.0296  149 THR   A CG2 
3157 N N   . ASN   A 150 ? 0.1552 0.1565 0.1682 -0.0151 0.0006  0.0458  150 ASN   A N   
3158 C CA  . ASN   A 150 ? 0.1683 0.1644 0.1758 -0.0186 0.0088  0.0414  150 ASN   A CA  
3159 C C   . ASN   A 150 ? 0.1508 0.1540 0.1723 -0.0181 0.0029  0.0350  150 ASN   A C   
3160 O O   . ASN   A 150 ? 0.1620 0.1618 0.2257 -0.0189 -0.0112 0.0288  150 ASN   A O   
3161 C CB  . ASN   A 150 ? 0.2073 0.1926 0.2017 -0.0223 0.0327  0.0613  150 ASN   A CB  
3162 C CG  . ASN   A 150 ? 0.2623 0.2305 0.2797 -0.0185 0.0139  0.0763  150 ASN   A CG  
3163 O OD1 . ASN   A 150 ? 0.2868 0.2427 0.3059 -0.0262 0.0103  0.0892  150 ASN   A OD1 
3164 N ND2 . ASN   A 150 ? 0.2922 0.2555 0.3187 -0.0109 0.0019  0.0765  150 ASN   A ND2 
3171 N N   . VAL   A 151 ? 0.1484 0.1442 0.1760 -0.0217 0.0034  0.0346  151 VAL   A N   
3172 C CA  . VAL   A 151 ? 0.1548 0.1469 0.1716 -0.0250 0.0024  0.0337  151 VAL   A CA  
3173 C C   . VAL   A 151 ? 0.1493 0.1419 0.1734 -0.0330 0.0005  0.0374  151 VAL   A C   
3174 O O   . VAL   A 151 ? 0.1587 0.1517 0.1966 -0.0231 0.0017  0.0293  151 VAL   A O   
3175 C CB  . VAL   A 151 ? 0.1808 0.1653 0.1736 -0.0056 0.0045  0.0326  151 VAL   A CB  
3176 C CG1 . VAL   A 151 ? 0.1773 0.1887 0.1989 -0.0099 -0.0000 0.0203  151 VAL   A CG1 
3177 C CG2 . VAL   A 151 ? 0.1913 0.1667 0.1728 -0.0025 0.0228  0.0318  151 VAL   A CG2 
3187 N N   . TYR   A 152 ? 0.1486 0.1457 0.1662 -0.0239 0.0096  0.0323  152 TYR   A N   
3188 C CA  . TYR   A 152 ? 0.1502 0.1519 0.1577 -0.0229 0.0146  0.0314  152 TYR   A CA  
3189 C C   . TYR   A 152 ? 0.1446 0.1481 0.1549 -0.0242 0.0205  0.0319  152 TYR   A C   
3190 O O   . TYR   A 152 ? 0.1556 0.1470 0.1654 -0.0292 0.0205  0.0268  152 TYR   A O   
3191 C CB  . TYR   A 152 ? 0.1607 0.1532 0.1533 -0.0154 0.0166  0.0310  152 TYR   A CB  
3192 C CG  . TYR   A 152 ? 0.1737 0.1732 0.1534 -0.0244 0.0259  0.0293  152 TYR   A CG  
3193 C CD1 . TYR   A 152 ? 0.1873 0.1987 0.1646 -0.0139 0.0192  0.0410  152 TYR   A CD1 
3194 C CD2 . TYR   A 152 ? 0.1785 0.1890 0.1476 -0.0331 0.0205  0.0248  152 TYR   A CD2 
3195 C CE1 . TYR   A 152 ? 0.2186 0.2127 0.1811 -0.0085 0.0090  0.0520  152 TYR   A CE1 
3196 C CE2 . TYR   A 152 ? 0.2047 0.2049 0.1611 -0.0363 0.0216  0.0348  152 TYR   A CE2 
3197 C CZ  . TYR   A 152 ? 0.2339 0.2085 0.1680 -0.0280 0.0058  0.0569  152 TYR   A CZ  
3198 O OH  . TYR   A 152 ? 0.2710 0.2299 0.1950 -0.0267 0.0148  0.0717  152 TYR   A OH  
3208 N N   . LEU   A 153 ? 0.1370 0.1514 0.1613 -0.0222 0.0173  0.0343  153 LEU   A N   
3209 C CA  . LEU   A 153 ? 0.1376 0.1480 0.1743 -0.0153 0.0169  0.0316  153 LEU   A CA  
3210 C C   . LEU   A 153 ? 0.1365 0.1578 0.1804 -0.0108 0.0254  0.0341  153 LEU   A C   
3211 O O   . LEU   A 153 ? 0.1379 0.1732 0.2008 -0.0107 0.0344  0.0309  153 LEU   A O   
3212 C CB  . LEU   A 153 ? 0.1359 0.1537 0.1894 -0.0140 0.0098  0.0300  153 LEU   A CB  
3213 C CG  . LEU   A 153 ? 0.1449 0.1538 0.1833 -0.0178 0.0192  0.0246  153 LEU   A CG  
3214 C CD1 . LEU   A 153 ? 0.1475 0.1592 0.1977 -0.0181 0.0140  0.0314  153 LEU   A CD1 
3215 C CD2 . LEU   A 153 ? 0.1503 0.1525 0.1807 -0.0168 0.0237  0.0098  153 LEU   A CD2 
3227 N N   A ALA   A 154 ? 0.1405 0.1492 0.1893 -0.0104 0.0249  0.0337  154 ALA   A N   
3228 N N   B ALA   A 154 ? 0.1449 0.1635 0.1733 -0.0004 0.0224  0.0295  154 ALA   A N   
3229 C CA  A ALA   A 154 ? 0.1514 0.1555 0.2087 -0.0057 0.0332  0.0327  154 ALA   A CA  
3230 C CA  B ALA   A 154 ? 0.1546 0.1720 0.1777 0.0077  0.0210  0.0239  154 ALA   A CA  
3231 C C   A ALA   A 154 ? 0.1459 0.1558 0.2122 0.0023  0.0306  0.0383  154 ALA   A C   
3232 C C   B ALA   A 154 ? 0.1588 0.1776 0.1767 0.0114  0.0179  0.0239  154 ALA   A C   
3233 O O   A ALA   A 154 ? 0.1533 0.1667 0.2079 0.0014  0.0363  0.0332  154 ALA   A O   
3234 O O   B ALA   A 154 ? 0.1623 0.1750 0.1671 0.0106  0.0203  0.0275  154 ALA   A O   
3235 C CB  A ALA   A 154 ? 0.1605 0.1562 0.2203 0.0008  0.0186  0.0274  154 ALA   A CB  
3236 C CB  B ALA   A 154 ? 0.1583 0.1722 0.1818 0.0113  0.0166  0.0204  154 ALA   A CB  
3247 N N   A VAL   A 155 ? 0.1536 0.1576 0.2245 0.0084  0.0332  0.0559  155 VAL   A N   
3248 N N   B VAL   A 155 ? 0.1652 0.1849 0.1852 0.0125  0.0121  0.0209  155 VAL   A N   
3249 C CA  A VAL   A 155 ? 0.1584 0.1656 0.2448 0.0115  0.0303  0.0618  155 VAL   A CA  
3250 C CA  B VAL   A 155 ? 0.1716 0.1921 0.1897 0.0115  0.0093  0.0226  155 VAL   A CA  
3251 C C   A VAL   A 155 ? 0.1744 0.1745 0.2757 0.0206  0.0270  0.0653  155 VAL   A C   
3252 C C   B VAL   A 155 ? 0.1805 0.2004 0.1994 0.0177  0.0038  0.0265  155 VAL   A C   
3253 O O   A VAL   A 155 ? 0.1677 0.1801 0.2681 0.0255  0.0319  0.0465  155 VAL   A O   
3254 O O   B VAL   A 155 ? 0.1737 0.2012 0.1807 0.0230  -0.0010 0.0221  155 VAL   A O   
3255 C CB  A VAL   A 155 ? 0.1563 0.1726 0.2367 0.0136  0.0184  0.0570  155 VAL   A CB  
3256 C CB  B VAL   A 155 ? 0.1724 0.1933 0.1874 0.0072  0.0076  0.0195  155 VAL   A CB  
3257 C CG1 A VAL   A 155 ? 0.1681 0.1845 0.2483 0.0156  0.0156  0.0620  155 VAL   A CG1 
3258 C CG1 B VAL   A 155 ? 0.1775 0.1967 0.1938 0.0072  0.0085  0.0205  155 VAL   A CG1 
3259 C CG2 A VAL   A 155 ? 0.1698 0.1856 0.2481 0.0268  0.0061  0.0447  155 VAL   A CG2 
3260 C CG2 B VAL   A 155 ? 0.1746 0.1947 0.1886 0.0070  0.0068  0.0199  155 VAL   A CG2 
3279 N N   A PHE   A 156 ? 0.1920 0.1833 0.3205 0.0177  0.0242  0.0807  156 PHE   A N   
3280 N N   B PHE   A 156 ? 0.1956 0.2087 0.2271 0.0156  0.0046  0.0342  156 PHE   A N   
3281 C CA  A PHE   A 156 ? 0.2134 0.1856 0.3645 0.0230  0.0271  0.0922  156 PHE   A CA  
3282 C CA  B PHE   A 156 ? 0.2118 0.2145 0.2544 0.0152  0.0091  0.0380  156 PHE   A CA  
3283 C C   A PHE   A 156 ? 0.2043 0.1932 0.3739 0.0357  0.0442  0.1010  156 PHE   A C   
3284 C C   B PHE   A 156 ? 0.2165 0.2186 0.2619 0.0157  0.0207  0.0404  156 PHE   A C   
3285 O O   A PHE   A 156 ? 0.2087 0.2022 0.3911 0.0367  0.0562  0.0762  156 PHE   A O   
3286 O O   B PHE   A 156 ? 0.2196 0.2190 0.2719 0.0137  0.0268  0.0325  156 PHE   A O   
3287 C CB  A PHE   A 156 ? 0.2484 0.1933 0.3907 0.0195  0.0021  0.1006  156 PHE   A CB  
3288 C CB  B PHE   A 156 ? 0.2213 0.2175 0.2725 0.0171  0.0004  0.0383  156 PHE   A CB  
3289 C CG  A PHE   A 156 ? 0.2880 0.2036 0.4182 0.0357  -0.0302 0.0920  156 PHE   A CG  
3290 C CG  B PHE   A 156 ? 0.2321 0.2242 0.2907 0.0215  -0.0101 0.0318  156 PHE   A CG  
3291 C CD1 A PHE   A 156 ? 0.3073 0.2123 0.4341 0.0467  -0.0381 0.0770  156 PHE   A CD1 
3292 C CD1 B PHE   A 156 ? 0.2375 0.2270 0.3004 0.0259  -0.0156 0.0258  156 PHE   A CD1 
3293 C CD2 A PHE   A 156 ? 0.3097 0.2151 0.4386 0.0373  -0.0417 0.0871  156 PHE   A CD2 
3294 C CD2 B PHE   A 156 ? 0.2381 0.2270 0.2998 0.0203  -0.0142 0.0306  156 PHE   A CD2 
3295 C CE1 A PHE   A 156 ? 0.3213 0.2184 0.4480 0.0485  -0.0368 0.0649  156 PHE   A CE1 
3296 C CE1 B PHE   A 156 ? 0.2394 0.2277 0.3038 0.0237  -0.0215 0.0243  156 PHE   A CE1 
3297 C CE2 A PHE   A 156 ? 0.3242 0.2247 0.4521 0.0437  -0.0438 0.0686  156 PHE   A CE2 
3298 C CE2 B PHE   A 156 ? 0.2398 0.2285 0.3047 0.0207  -0.0175 0.0279  156 PHE   A CE2 
3299 C CZ  A PHE   A 156 ? 0.3259 0.2223 0.4525 0.0528  -0.0403 0.0566  156 PHE   A CZ  
3300 C CZ  B PHE   A 156 ? 0.2395 0.2277 0.3036 0.0197  -0.0210 0.0246  156 PHE   A CZ  
3319 N N   A ASP   A 157 ? 0.1994 0.2024 0.3695 0.0343  0.0411  0.1191  157 ASP   A N   
3320 N N   B ASP   A 157 ? 0.2168 0.2240 0.2589 0.0171  0.0204  0.0465  157 ASP   A N   
3321 C CA  A ASP   A 157 ? 0.2125 0.2237 0.3813 0.0335  0.0314  0.1237  157 ASP   A CA  
3322 C CA  B ASP   A 157 ? 0.2191 0.2302 0.2554 0.0212  0.0183  0.0492  157 ASP   A CA  
3323 C C   A ASP   A 157 ? 0.1949 0.2326 0.3802 0.0433  0.0415  0.1238  157 ASP   A C   
3324 C C   B ASP   A 157 ? 0.2282 0.2427 0.2597 0.0218  0.0145  0.0468  157 ASP   A C   
3325 O O   A ASP   A 157 ? 0.1811 0.2212 0.3783 0.0418  0.0450  0.1195  157 ASP   A O   
3326 O O   B ASP   A 157 ? 0.2256 0.2416 0.2599 0.0223  0.0155  0.0442  157 ASP   A O   
3327 C CB  A ASP   A 157 ? 0.2370 0.2336 0.4065 0.0377  0.0077  0.1230  157 ASP   A CB  
3328 C CB  B ASP   A 157 ? 0.2099 0.2240 0.2493 0.0275  0.0184  0.0567  157 ASP   A CB  
3329 C CG  A ASP   A 157 ? 0.2648 0.2409 0.4494 0.0416  -0.0114 0.1129  157 ASP   A CG  
3330 C CG  B ASP   A 157 ? 0.2003 0.2163 0.2501 0.0335  0.0167  0.0648  157 ASP   A CG  
3331 O OD1 A ASP   A 157 ? 0.2933 0.2514 0.4784 0.0393  -0.0279 0.0980  157 ASP   A OD1 
3332 O OD1 B ASP   A 157 ? 0.1984 0.2118 0.2644 0.0307  0.0135  0.0574  157 ASP   A OD1 
3333 O OD2 A ASP   A 157 ? 0.2612 0.2383 0.4727 0.0375  -0.0079 0.1169  157 ASP   A OD2 
3334 O OD2 B ASP   A 157 ? 0.1944 0.2143 0.2372 0.0405  0.0165  0.0779  157 ASP   A OD2 
3343 N N   A LYS   A 158 ? 0.2041 0.2582 0.3973 0.0503  0.0506  0.1122  158 LYS   A N   
3344 N N   B LYS   A 158 ? 0.2399 0.2566 0.2710 0.0216  0.0126  0.0419  158 LYS   A N   
3345 C CA  A LYS   A 158 ? 0.2032 0.2817 0.4075 0.0622  0.0652  0.1091  158 LYS   A CA  
3346 C CA  B LYS   A 158 ? 0.2480 0.2696 0.2850 0.0221  0.0131  0.0363  158 LYS   A CA  
3347 C C   A LYS   A 158 ? 0.1840 0.2903 0.3928 0.0688  0.0611  0.1270  158 LYS   A C   
3348 C C   B LYS   A 158 ? 0.2508 0.2777 0.2867 0.0228  0.0145  0.0359  158 LYS   A C   
3349 O O   A LYS   A 158 ? 0.1766 0.2932 0.3894 0.0553  0.0684  0.1297  158 LYS   A O   
3350 O O   B LYS   A 158 ? 0.2504 0.2781 0.2852 0.0231  0.0125  0.0313  158 LYS   A O   
3351 C CB  A LYS   A 158 ? 0.2237 0.2915 0.4289 0.0659  0.0897  0.0989  158 LYS   A CB  
3352 C CB  B LYS   A 158 ? 0.2534 0.2741 0.2983 0.0184  0.0168  0.0294  158 LYS   A CB  
3353 C CG  A LYS   A 158 ? 0.2493 0.3065 0.4556 0.0670  0.1094  0.0855  158 LYS   A CG  
3354 C CG  B LYS   A 158 ? 0.2579 0.2778 0.3119 0.0155  0.0173  0.0248  158 LYS   A CG  
3355 C CD  A LYS   A 158 ? 0.2716 0.3213 0.4753 0.0651  0.1267  0.0805  158 LYS   A CD  
3356 C CD  B LYS   A 158 ? 0.2620 0.2822 0.3224 0.0130  0.0192  0.0226  158 LYS   A CD  
3357 C CE  A LYS   A 158 ? 0.2876 0.3306 0.4914 0.0627  0.1389  0.0848  158 LYS   A CE  
3358 C CE  B LYS   A 158 ? 0.2641 0.2845 0.3301 0.0107  0.0187  0.0216  158 LYS   A CE  
3359 N NZ  A LYS   A 158 ? 0.2975 0.3356 0.4981 0.0568  0.1430  0.0920  158 LYS   A NZ  
3360 N NZ  B LYS   A 158 ? 0.2653 0.2858 0.3348 0.0086  0.0185  0.0220  158 LYS   A NZ  
3387 N N   A ASN   A 159 ? 0.1829 0.2996 0.3967 0.0737  0.0433  0.1285  159 ASN   A N   
3388 N N   B ASN   A 159 ? 0.2548 0.2853 0.2964 0.0207  0.0164  0.0364  159 ASN   A N   
3389 C CA  A ASN   A 159 ? 0.1856 0.3068 0.4014 0.0672  0.0249  0.1419  159 ASN   A CA  
3390 C CA  B ASN   A 159 ? 0.2597 0.2929 0.3081 0.0159  0.0176  0.0367  159 ASN   A CA  
3391 C C   A ASN   A 159 ? 0.1697 0.3070 0.3681 0.0545  0.0236  0.1262  159 ASN   A C   
3392 C C   B ASN   A 159 ? 0.2548 0.2941 0.2882 0.0110  0.0192  0.0280  159 ASN   A C   
3393 O O   A ASN   A 159 ? 0.1517 0.3163 0.3500 0.0553  0.0083  0.1156  159 ASN   A O   
3394 O O   B ASN   A 159 ? 0.2523 0.2952 0.2841 0.0095  0.0187  0.0248  159 ASN   A O   
3395 C CB  A ASN   A 159 ? 0.2056 0.3164 0.4491 0.0673  0.0248  0.1624  159 ASN   A CB  
3396 C CB  B ASN   A 159 ? 0.2697 0.2996 0.3420 0.0155  0.0178  0.0437  159 ASN   A CB  
3397 C CG  A ASN   A 159 ? 0.2289 0.3297 0.5069 0.0600  0.0309  0.1679  159 ASN   A CG  
3398 C CG  B ASN   A 159 ? 0.2781 0.3049 0.3742 0.0142  0.0191  0.0466  159 ASN   A CG  
3399 O OD1 A ASN   A 159 ? 0.2343 0.3371 0.5313 0.0549  0.0416  0.1685  159 ASN   A OD1 
3400 O OD1 B ASN   A 159 ? 0.2798 0.3082 0.3864 0.0133  0.0242  0.0472  159 ASN   A OD1 
3401 N ND2 A ASN   A 159 ? 0.2393 0.3346 0.5321 0.0579  0.0278  0.1653  159 ASN   A ND2 
3402 N ND2 B ASN   A 159 ? 0.2817 0.3070 0.3852 0.0136  0.0164  0.0466  159 ASN   A ND2 
3415 N N   A LEU   A 160 ? 0.1563 0.2867 0.3379 0.0473  0.0119  0.1276  160 LEU   A N   
3416 N N   B LEU   A 160 ? 0.2495 0.2917 0.2735 0.0075  0.0178  0.0237  160 LEU   A N   
3417 C CA  A LEU   A 160 ? 0.1579 0.2725 0.3124 0.0326  0.0151  0.1205  160 LEU   A CA  
3418 C CA  B LEU   A 160 ? 0.2457 0.2873 0.2642 0.0022  0.0189  0.0203  160 LEU   A CA  
3419 C C   A LEU   A 160 ? 0.1391 0.2569 0.2992 0.0163  0.0281  0.1108  160 LEU   A C   
3420 C C   B LEU   A 160 ? 0.2369 0.2773 0.2450 -0.0022 0.0204  0.0260  160 LEU   A C   
3421 O O   A LEU   A 160 ? 0.1358 0.2618 0.3179 0.0083  0.0215  0.0959  160 LEU   A O   
3422 O O   B LEU   A 160 ? 0.2361 0.2781 0.2404 -0.0017 0.0172  0.0255  160 LEU   A O   
3423 C CB  A LEU   A 160 ? 0.1725 0.2748 0.2923 0.0229  0.0237  0.1151  160 LEU   A CB  
3424 C CB  B LEU   A 160 ? 0.2485 0.2915 0.2722 -0.0007 0.0205  0.0118  160 LEU   A CB  
3425 C CG  A LEU   A 160 ? 0.1835 0.2775 0.2884 0.0139  0.0337  0.0953  160 LEU   A CG  
3426 C CG  B LEU   A 160 ? 0.2504 0.2940 0.2815 -0.0030 0.0222  0.0015  160 LEU   A CG  
3427 C CD1 A LEU   A 160 ? 0.1935 0.2835 0.2912 0.0134  0.0333  0.0852  160 LEU   A CD1 
3428 C CD1 B LEU   A 160 ? 0.2496 0.2949 0.2862 -0.0024 0.0222  -0.0025 160 LEU   A CD1 
3429 C CD2 A LEU   A 160 ? 0.1847 0.2789 0.2854 0.0115  0.0459  0.0817  160 LEU   A CD2 
3430 C CD2 B LEU   A 160 ? 0.2516 0.2959 0.2841 -0.0039 0.0240  -0.0020 160 LEU   A CD2 
3453 N N   A TYR   A 161 ? 0.1339 0.2352 0.2855 0.0197  0.0321  0.1071  161 TYR   A N   
3454 N N   B TYR   A 161 ? 0.2302 0.2659 0.2337 -0.0034 0.0225  0.0310  161 TYR   A N   
3455 C CA  A TYR   A 161 ? 0.1348 0.2270 0.2868 0.0141  0.0316  0.1005  161 TYR   A CA  
3456 C CA  B TYR   A 161 ? 0.2246 0.2574 0.2278 -0.0029 0.0208  0.0359  161 TYR   A CA  
3457 C C   A TYR   A 161 ? 0.1296 0.2416 0.3035 0.0171  0.0287  0.0936  161 TYR   A C   
3458 C C   B TYR   A 161 ? 0.2152 0.2569 0.2243 -0.0011 0.0206  0.0417  161 TYR   A C   
3459 O O   A TYR   A 161 ? 0.1274 0.2372 0.3055 0.0115  0.0281  0.0836  161 TYR   A O   
3460 O O   B TYR   A 161 ? 0.2099 0.2522 0.2152 -0.0005 0.0209  0.0393  161 TYR   A O   
3461 C CB  A TYR   A 161 ? 0.1409 0.2161 0.2949 0.0124  0.0249  0.0812  161 TYR   A CB  
3462 C CB  B TYR   A 161 ? 0.2306 0.2527 0.2315 -0.0031 0.0177  0.0334  161 TYR   A CB  
3463 C CG  A TYR   A 161 ? 0.1400 0.2091 0.2832 0.0110  0.0180  0.0629  161 TYR   A CG  
3464 C CG  B TYR   A 161 ? 0.2363 0.2492 0.2382 -0.0025 0.0125  0.0310  161 TYR   A CG  
3465 C CD1 A TYR   A 161 ? 0.1349 0.1986 0.2807 0.0113  0.0173  0.0516  161 TYR   A CD1 
3466 C CD1 B TYR   A 161 ? 0.2397 0.2483 0.2464 -0.0040 0.0087  0.0323  161 TYR   A CD1 
3467 C CD2 A TYR   A 161 ? 0.1393 0.2108 0.2766 0.0202  0.0088  0.0559  161 TYR   A CD2 
3468 C CD2 B TYR   A 161 ? 0.2404 0.2489 0.2448 -0.0036 0.0111  0.0313  161 TYR   A CD2 
3469 C CE1 A TYR   A 161 ? 0.1383 0.1951 0.2766 0.0135  0.0116  0.0533  161 TYR   A CE1 
3470 C CE1 B TYR   A 161 ? 0.2430 0.2505 0.2546 -0.0044 0.0042  0.0342  161 TYR   A CE1 
3471 C CE2 A TYR   A 161 ? 0.1425 0.2015 0.2748 0.0151  0.0061  0.0640  161 TYR   A CE2 
3472 C CE2 B TYR   A 161 ? 0.2430 0.2508 0.2556 -0.0045 0.0066  0.0317  161 TYR   A CE2 
3473 C CZ  A TYR   A 161 ? 0.1505 0.1944 0.2823 0.0065  0.0066  0.0660  161 TYR   A CZ  
3474 C CZ  B TYR   A 161 ? 0.2438 0.2522 0.2612 -0.0046 0.0038  0.0335  161 TYR   A CZ  
3475 O OH  A TYR   A 161 ? 0.1671 0.1987 0.2968 -0.0003 -0.0066 0.0800  161 TYR   A OH  
3476 O OH  B TYR   A 161 ? 0.2455 0.2546 0.2757 -0.0041 0.0011  0.0332  161 TYR   A OH  
3495 N N   A ASP   A 162 ? 0.1294 0.2592 0.3209 0.0184  0.0323  0.0978  162 ASP   A N   
3496 N N   B ASP   A 162 ? 0.2098 0.2618 0.2273 -0.0005 0.0229  0.0510  162 ASP   A N   
3497 C CA  A ASP   A 162 ? 0.1312 0.2808 0.3303 0.0150  0.0374  0.1004  162 ASP   A CA  
3498 C CA  B ASP   A 162 ? 0.2068 0.2679 0.2374 0.0032  0.0223  0.0541  162 ASP   A CA  
3499 C C   A ASP   A 162 ? 0.1200 0.2967 0.3251 0.0083  0.0338  0.1035  162 ASP   A C   
3500 C C   B ASP   A 162 ? 0.2137 0.2748 0.2412 0.0039  0.0165  0.0464  162 ASP   A C   
3501 O O   A ASP   A 162 ? 0.1217 0.2973 0.3485 -0.0041 0.0300  0.0952  162 ASP   A O   
3502 O O   B ASP   A 162 ? 0.2140 0.2764 0.2375 0.0053  0.0139  0.0430  162 ASP   A O   
3503 C CB  A ASP   A 162 ? 0.1488 0.2877 0.3431 0.0204  0.0499  0.0953  162 ASP   A CB  
3504 C CB  B ASP   A 162 ? 0.1983 0.2674 0.2535 0.0070  0.0263  0.0618  162 ASP   A CB  
3505 C CG  A ASP   A 162 ? 0.1656 0.3024 0.3618 0.0270  0.0533  0.0842  162 ASP   A CG  
3506 C CG  B ASP   A 162 ? 0.1900 0.2660 0.2626 0.0106  0.0280  0.0708  162 ASP   A CG  
3507 O OD1 A ASP   A 162 ? 0.1881 0.3080 0.3693 0.0168  0.0455  0.0893  162 ASP   A OD1 
3508 O OD1 B ASP   A 162 ? 0.1848 0.2653 0.2653 0.0152  0.0304  0.0757  162 ASP   A OD1 
3509 O OD2 A ASP   A 162 ? 0.1779 0.3103 0.3824 0.0399  0.0611  0.0698  162 ASP   A OD2 
3510 O OD2 B ASP   A 162 ? 0.1903 0.2672 0.2694 0.0116  0.0260  0.0741  162 ASP   A OD2 
3519 N N   A LYS   A 163 ? 0.1320 0.3160 0.3261 0.0051  0.0046  0.1020  163 LYS   A N   
3520 N N   B LYS   A 163 ? 0.2236 0.2814 0.2551 0.0020  0.0114  0.0407  163 LYS   A N   
3521 C CA  A LYS   A 163 ? 0.1499 0.3351 0.3215 -0.0029 -0.0041 0.0947  163 LYS   A CA  
3522 C CA  B LYS   A 163 ? 0.2331 0.2867 0.2640 -0.0004 0.0098  0.0336  163 LYS   A CA  
3523 C C   A LYS   A 163 ? 0.1351 0.3228 0.3035 -0.0112 0.0125  0.0885  163 LYS   A C   
3524 C C   B LYS   A 163 ? 0.2232 0.2738 0.2356 -0.0013 0.0114  0.0312  163 LYS   A C   
3525 O O   A LYS   A 163 ? 0.1272 0.3355 0.3141 -0.0216 0.0083  0.0743  163 LYS   A O   
3526 O O   B LYS   A 163 ? 0.2232 0.2762 0.2307 -0.0026 0.0099  0.0276  163 LYS   A O   
3527 C CB  A LYS   A 163 ? 0.1942 0.3631 0.3589 0.0081  -0.0274 0.0922  163 LYS   A CB  
3528 C CB  B LYS   A 163 ? 0.2535 0.3031 0.3066 0.0004  0.0075  0.0288  163 LYS   A CB  
3529 C CG  A LYS   A 163 ? 0.2392 0.3871 0.4071 0.0050  -0.0242 0.0862  163 LYS   A CG  
3530 C CG  B LYS   A 163 ? 0.2713 0.3169 0.3494 -0.0015 0.0092  0.0236  163 LYS   A CG  
3531 C CD  A LYS   A 163 ? 0.2834 0.4059 0.4653 0.0024  -0.0254 0.0784  163 LYS   A CD  
3532 C CD  B LYS   A 163 ? 0.2849 0.3275 0.3908 -0.0029 0.0076  0.0196  163 LYS   A CD  
3533 C CE  A LYS   A 163 ? 0.3237 0.4190 0.5097 -0.0009 -0.0228 0.0740  163 LYS   A CE  
3534 C CE  B LYS   A 163 ? 0.2956 0.3345 0.4214 -0.0042 0.0071  0.0186  163 LYS   A CE  
3535 N NZ  A LYS   A 163 ? 0.3341 0.4267 0.5354 -0.0039 -0.0216 0.0742  163 LYS   A NZ  
3536 N NZ  B LYS   A 163 ? 0.3023 0.3376 0.4376 -0.0047 0.0084  0.0204  163 LYS   A NZ  
3563 N N   A LEU   A 164 ? 0.1184 0.2899 0.2817 -0.0172 0.0126  0.0835  164 LEU   A N   
3564 N N   B LEU   A 164 ? 0.2095 0.2556 0.2130 -0.0013 0.0108  0.0270  164 LEU   A N   
3565 C CA  A LEU   A 164 ? 0.1215 0.2627 0.2649 -0.0275 0.0229  0.0674  164 LEU   A CA  
3566 C CA  B LEU   A 164 ? 0.1995 0.2394 0.2007 -0.0040 0.0135  0.0182  164 LEU   A CA  
3567 C C   A LEU   A 164 ? 0.1332 0.2564 0.2607 -0.0237 0.0266  0.0583  164 LEU   A C   
3568 C C   B LEU   A 164 ? 0.1902 0.2289 0.1911 -0.0055 0.0135  0.0145  164 LEU   A C   
3569 O O   A LEU   A 164 ? 0.1482 0.2632 0.2619 -0.0268 0.0426  0.0338  164 LEU   A O   
3570 O O   B LEU   A 164 ? 0.1900 0.2285 0.1827 -0.0074 0.0196  0.0077  164 LEU   A O   
3571 C CB  A LEU   A 164 ? 0.1238 0.2448 0.2527 -0.0245 0.0273  0.0621  164 LEU   A CB  
3572 C CB  B LEU   A 164 ? 0.1989 0.2327 0.2019 -0.0026 0.0128  0.0130  164 LEU   A CB  
3573 C CG  A LEU   A 164 ? 0.1355 0.2345 0.2575 -0.0187 0.0227  0.0575  164 LEU   A CG  
3574 C CG  B LEU   A 164 ? 0.1998 0.2285 0.2053 -0.0032 0.0103  0.0112  164 LEU   A CG  
3575 C CD1 A LEU   A 164 ? 0.1265 0.2318 0.2688 -0.0117 0.0162  0.0492  164 LEU   A CD1 
3576 C CD1 B LEU   A 164 ? 0.1964 0.2267 0.2015 -0.0031 0.0055  0.0132  164 LEU   A CD1 
3577 C CD2 A LEU   A 164 ? 0.1528 0.2324 0.2540 -0.0198 0.0296  0.0561  164 LEU   A CD2 
3578 C CD2 B LEU   A 164 ? 0.2029 0.2271 0.2090 -0.0048 0.0128  0.0089  164 LEU   A CD2 
3601 N N   A VAL   A 165 ? 0.1334 0.2466 0.2544 -0.0251 0.0168  0.0641  165 VAL   A N   
3602 N N   B VAL   A 165 ? 0.1804 0.2199 0.1844 -0.0091 0.0078  0.0186  165 VAL   A N   
3603 C CA  A VAL   A 165 ? 0.1418 0.2454 0.2453 -0.0206 0.0220  0.0637  165 VAL   A CA  
3604 C CA  B VAL   A 165 ? 0.1777 0.2143 0.1825 -0.0096 0.0012  0.0216  165 VAL   A CA  
3605 C C   A VAL   A 165 ? 0.1287 0.2620 0.2394 -0.0139 0.0272  0.0644  165 VAL   A C   
3606 C C   B VAL   A 165 ? 0.1686 0.2109 0.1805 -0.0115 0.0030  0.0224  165 VAL   A C   
3607 O O   A VAL   A 165 ? 0.1327 0.2587 0.2319 -0.0160 0.0282  0.0565  165 VAL   A O   
3608 O O   B VAL   A 165 ? 0.1675 0.2068 0.1817 -0.0137 0.0061  0.0116  165 VAL   A O   
3609 C CB  A VAL   A 165 ? 0.1605 0.2325 0.2478 -0.0190 0.0260  0.0588  165 VAL   A CB  
3610 C CB  B VAL   A 165 ? 0.1846 0.2147 0.1828 -0.0109 -0.0018 0.0254  165 VAL   A CB  
3611 C CG1 A VAL   A 165 ? 0.1698 0.2310 0.2533 -0.0182 0.0328  0.0482  165 VAL   A CG1 
3612 C CG1 B VAL   A 165 ? 0.1882 0.2167 0.1832 -0.0126 -0.0013 0.0237  165 VAL   A CG1 
3613 C CG2 A VAL   A 165 ? 0.1739 0.2327 0.2619 -0.0199 0.0222  0.0594  165 VAL   A CG2 
3614 C CG2 B VAL   A 165 ? 0.1851 0.2124 0.1833 -0.0074 -0.0075 0.0249  165 VAL   A CG2 
3633 N N   A SER   A 166 ? 0.1143 0.2808 0.2635 -0.0116 0.0275  0.0636  166 SER   A N   
3634 N N   B SER   A 166 ? 0.1607 0.2155 0.1838 -0.0108 0.0023  0.0302  166 SER   A N   
3635 C CA  A SER   A 166 ? 0.1264 0.3080 0.2805 -0.0125 0.0208  0.0525  166 SER   A CA  
3636 C CA  B SER   A 166 ? 0.1592 0.2253 0.1946 -0.0113 0.0008  0.0299  166 SER   A CA  
3637 C C   A SER   A 166 ? 0.1308 0.3275 0.2784 -0.0194 0.0078  0.0449  166 SER   A C   
3638 C C   B SER   A 166 ? 0.1779 0.2434 0.2140 -0.0093 0.0012  0.0262  166 SER   A C   
3639 O O   A SER   A 166 ? 0.1498 0.3437 0.3086 -0.0351 0.0138  0.0167  166 SER   A O   
3640 O O   B SER   A 166 ? 0.1848 0.2525 0.2353 -0.0131 0.0045  0.0126  166 SER   A O   
3641 C CB  A SER   A 166 ? 0.1485 0.3186 0.3181 -0.0061 0.0124  0.0416  166 SER   A CB  
3642 C CB  B SER   A 166 ? 0.1410 0.2174 0.1952 -0.0130 -0.0062 0.0285  166 SER   A CB  
3643 O OG  A SER   A 166 ? 0.1867 0.3283 0.3479 -0.0077 0.0132  0.0443  166 SER   A OG  
3644 O OG  B SER   A 166 ? 0.1235 0.2101 0.1915 -0.0165 -0.0087 0.0322  166 SER   A OG  
3655 N N   A SER   A 167 ? 0.1356 0.3317 0.2432 -0.0042 -0.0080 0.0618  167 SER   A N   
3656 N N   B SER   A 167 ? 0.1934 0.2520 0.2117 -0.0025 -0.0011 0.0344  167 SER   A N   
3657 C CA  A SER   A 167 ? 0.1560 0.3409 0.2417 0.0028  -0.0056 0.0527  167 SER   A CA  
3658 C CA  B SER   A 167 ? 0.2122 0.2613 0.2202 0.0012  0.0018  0.0323  167 SER   A CA  
3659 C C   A SER   A 167 ? 0.1586 0.3374 0.2346 0.0095  0.0113  0.0474  167 SER   A C   
3660 C C   B SER   A 167 ? 0.2274 0.2662 0.2272 0.0015  0.0048  0.0273  167 SER   A C   
3661 O O   A SER   A 167 ? 0.1780 0.3378 0.2545 0.0139  -0.0009 0.0507  167 SER   A O   
3662 O O   B SER   A 167 ? 0.2314 0.2643 0.2306 0.0041  0.0040  0.0281  167 SER   A O   
3663 C CB  A SER   A 167 ? 0.1698 0.3533 0.2531 0.0088  0.0044  0.0576  167 SER   A CB  
3664 C CB  B SER   A 167 ? 0.2166 0.2660 0.2231 0.0043  0.0069  0.0384  167 SER   A CB  
3665 O OG  A SER   A 167 ? 0.1725 0.3586 0.2584 0.0085  0.0310  0.0684  167 SER   A OG  
3666 O OG  B SER   A 167 ? 0.2173 0.2679 0.2265 0.0054  0.0140  0.0452  167 SER   A OG  
3677 N N   A PHE   A 168 ? 0.1466 0.3326 0.2204 0.0169  0.0142  0.0402  168 PHE   A N   
3678 N N   B PHE   A 168 ? 0.2387 0.2722 0.2348 0.0007  0.0043  0.0237  168 PHE   A N   
3679 C CA  A PHE   A 168 ? 0.1472 0.3313 0.2374 0.0118  0.0208  0.0251  168 PHE   A CA  
3680 C CA  B PHE   A 168 ? 0.2514 0.2804 0.2519 -0.0028 0.0026  0.0161  168 PHE   A CA  
3681 C C   A PHE   A 168 ? 0.1572 0.3558 0.2701 0.0082  0.0582  -0.0018 168 PHE   A C   
3682 C C   B PHE   A 168 ? 0.2724 0.3005 0.2923 -0.0046 0.0039  0.0104  168 PHE   A C   
3683 O O   A PHE   A 168 ? 0.1570 0.3581 0.3022 -0.0070 0.0629  0.0100  168 PHE   A O   
3684 O O   B PHE   A 168 ? 0.2755 0.3002 0.2972 -0.0072 0.0051  0.0132  168 PHE   A O   
3685 C CB  A PHE   A 168 ? 0.1508 0.3084 0.2299 0.0021  -0.0018 0.0239  168 PHE   A CB  
3686 C CB  B PHE   A 168 ? 0.2441 0.2694 0.2308 -0.0051 -0.0003 0.0132  168 PHE   A CB  
3687 C CG  A PHE   A 168 ? 0.1454 0.2891 0.2176 -0.0094 -0.0083 0.0303  168 PHE   A CG  
3688 C CG  B PHE   A 168 ? 0.2363 0.2601 0.2113 -0.0068 0.0007  0.0124  168 PHE   A CG  
3689 C CD1 A PHE   A 168 ? 0.1458 0.2905 0.2321 -0.0221 -0.0104 0.0412  168 PHE   A CD1 
3690 C CD1 B PHE   A 168 ? 0.2344 0.2593 0.2112 -0.0087 0.0014  0.0158  168 PHE   A CD1 
3691 C CD2 A PHE   A 168 ? 0.1392 0.2781 0.2069 -0.0116 0.0044  0.0313  168 PHE   A CD2 
3692 C CD2 B PHE   A 168 ? 0.2317 0.2552 0.2022 -0.0070 0.0033  0.0110  168 PHE   A CD2 
3693 C CE1 A PHE   A 168 ? 0.1353 0.2863 0.2333 -0.0209 -0.0118 0.0451  168 PHE   A CE1 
3694 C CE1 B PHE   A 168 ? 0.2316 0.2569 0.2092 -0.0080 0.0017  0.0172  168 PHE   A CE1 
3695 C CE2 A PHE   A 168 ? 0.1450 0.2722 0.2229 -0.0123 0.0033  0.0419  168 PHE   A CE2 
3696 C CE2 B PHE   A 168 ? 0.2305 0.2523 0.2003 -0.0073 0.0050  0.0133  168 PHE   A CE2 
3697 C CZ  A PHE   A 168 ? 0.1379 0.2766 0.2268 -0.0191 -0.0038 0.0456  168 PHE   A CZ  
3698 C CZ  B PHE   A 168 ? 0.2297 0.2535 0.2032 -0.0079 0.0030  0.0158  168 PHE   A CZ  
3717 N N   A LEU   A 169 ? 0.2097 0.3794 0.3141 0.0049  0.0615  -0.0281 169 LEU   A N   
3718 N N   B LEU   A 169 ? 0.2929 0.3191 0.3320 -0.0049 0.0029  0.0030  169 LEU   A N   
3719 C CA  A LEU   A 169 ? 0.2852 0.4091 0.4065 0.0053  0.0220  -0.0416 169 LEU   A CA  
3720 C CA  B LEU   A 169 ? 0.3153 0.3387 0.3778 -0.0039 -0.0011 -0.0006 169 LEU   A CA  
3721 C C   A LEU   A 169 ? 0.3021 0.4153 0.4509 0.0045  0.0103  -0.0359 169 LEU   A C   
3722 C C   B LEU   A 169 ? 0.3196 0.3447 0.3967 -0.0029 -0.0045 0.0030  169 LEU   A C   
3723 O O   A LEU   A 169 ? 0.3115 0.4187 0.4650 0.0058  0.0097  -0.0396 169 LEU   A O   
3724 O O   B LEU   A 169 ? 0.3229 0.3488 0.4008 -0.0022 -0.0066 0.0015  169 LEU   A O   
3725 C CB  A LEU   A 169 ? 0.3304 0.4292 0.4373 0.0047  -0.0031 -0.0574 169 LEU   A CB  
3726 C CB  B LEU   A 169 ? 0.3304 0.3505 0.3991 -0.0043 -0.0004 -0.0081 169 LEU   A CB  
3727 C CG  A LEU   A 169 ? 0.3695 0.4453 0.4624 0.0007  -0.0246 -0.0740 169 LEU   A CG  
3728 C CG  B LEU   A 169 ? 0.3422 0.3602 0.4190 -0.0056 -0.0007 -0.0157 169 LEU   A CG  
3729 C CD1 A LEU   A 169 ? 0.3798 0.4498 0.4723 -0.0000 -0.0322 -0.0765 169 LEU   A CD1 
3730 C CD1 B LEU   A 169 ? 0.3453 0.3634 0.4254 -0.0055 -0.0004 -0.0171 169 LEU   A CD1 
3731 C CD2 A LEU   A 169 ? 0.3803 0.4521 0.4654 -0.0016 -0.0324 -0.0807 169 LEU   A CD2 
3732 C CD2 B LEU   A 169 ? 0.3462 0.3640 0.4244 -0.0061 -0.0007 -0.0185 169 LEU   A CD2 
3733 O OXT A LEU   A 169 ? 0.2908 0.4164 0.4579 0.0047  0.0047  -0.0318 169 LEU   A OXT 
3734 O OXT B LEU   A 169 ? 0.3179 0.3457 0.4046 -0.0020 -0.0053 0.0047  169 LEU   A OXT 
3757 N N   A SER   B 1   ? 0.3431 0.3452 0.3704 -0.1219 -0.1019 0.0625  1   SER   B N   
3758 N N   B SER   B 1   ? 0.3694 0.3624 0.3527 -0.0421 -0.0368 0.0245  1   SER   B N   
3759 C CA  A SER   B 1   ? 0.3283 0.3445 0.3712 -0.1307 -0.1086 0.0556  1   SER   B CA  
3760 C CA  B SER   B 1   ? 0.3659 0.3618 0.3572 -0.0425 -0.0362 0.0232  1   SER   B CA  
3761 C C   A SER   B 1   ? 0.3013 0.3478 0.3388 -0.1313 -0.1157 0.0765  1   SER   B C   
3762 C C   B SER   B 1   ? 0.3597 0.3604 0.3507 -0.0405 -0.0384 0.0295  1   SER   B C   
3763 O O   A SER   B 1   ? 0.3119 0.3465 0.3102 -0.1214 -0.1117 0.0767  1   SER   B O   
3764 O O   B SER   B 1   ? 0.3618 0.3603 0.3403 -0.0397 -0.0391 0.0290  1   SER   B O   
3765 C CB  A SER   B 1   ? 0.3383 0.3402 0.3992 -0.1340 -0.0962 0.0337  1   SER   B CB  
3766 C CB  B SER   B 1   ? 0.3675 0.3620 0.3620 -0.0437 -0.0319 0.0157  1   SER   B CB  
3767 O OG  A SER   B 1   ? 0.3594 0.3527 0.4518 -0.1267 -0.0795 0.0265  1   SER   B OG  
3768 O OG  B SER   B 1   ? 0.3714 0.3657 0.3782 -0.0444 -0.0294 0.0121  1   SER   B OG  
3783 N N   A MET   B 2   ? 0.2778 0.3529 0.3475 -0.1271 -0.1058 0.1160  2   MET   B N   
3784 N N   B MET   B 2   ? 0.3515 0.3581 0.3540 -0.0382 -0.0378 0.0391  2   MET   B N   
3785 C CA  A MET   B 2   ? 0.2608 0.3558 0.3642 -0.1041 -0.1043 0.1359  2   MET   B CA  
3786 C CA  B MET   B 2   ? 0.3408 0.3529 0.3585 -0.0340 -0.0367 0.0458  2   MET   B CA  
3787 C C   A MET   B 2   ? 0.2256 0.3254 0.3322 -0.0832 -0.1104 0.1630  2   MET   B C   
3788 C C   B MET   B 2   ? 0.3156 0.3301 0.3202 -0.0336 -0.0369 0.0525  2   MET   B C   
3789 O O   A MET   B 2   ? 0.2207 0.3405 0.3388 -0.0663 -0.1127 0.1646  2   MET   B O   
3790 O O   B MET   B 2   ? 0.3192 0.3349 0.3228 -0.0315 -0.0332 0.0511  2   MET   B O   
3791 C CB  A MET   B 2   ? 0.2961 0.3964 0.4504 -0.0820 -0.0865 0.1067  2   MET   B CB  
3792 C CB  B MET   B 2   ? 0.3558 0.3700 0.4070 -0.0280 -0.0350 0.0433  2   MET   B CB  
3793 C CG  A MET   B 2   ? 0.3300 0.4362 0.5243 -0.0586 -0.0702 0.0877  2   MET   B CG  
3794 C CG  B MET   B 2   ? 0.3706 0.3859 0.4497 -0.0222 -0.0334 0.0424  2   MET   B CG  
3795 S SD  A MET   B 2   ? 0.3608 0.4733 0.5930 -0.0379 -0.0562 0.0726  2   MET   B SD  
3796 S SD  B MET   B 2   ? 0.3831 0.3997 0.4867 -0.0169 -0.0326 0.0420  2   MET   B SD  
3797 C CE  A MET   B 2   ? 0.3627 0.4779 0.6000 -0.0358 -0.0516 0.0696  2   MET   B CE  
3798 C CE  B MET   B 2   ? 0.3850 0.4027 0.4964 -0.0169 -0.0319 0.0401  2   MET   B CE  
3817 N N   A VAL   B 3   ? 0.2025 0.2788 0.3196 -0.0848 -0.0998 0.1673  3   VAL   B N   
3818 N N   B VAL   B 3   ? 0.2855 0.3002 0.2834 -0.0362 -0.0403 0.0592  3   VAL   B N   
3819 C CA  A VAL   B 3   ? 0.2020 0.2393 0.3132 -0.0728 -0.0833 0.1436  3   VAL   B CA  
3820 C CA  B VAL   B 3   ? 0.2556 0.2696 0.2534 -0.0369 -0.0426 0.0617  3   VAL   B CA  
3821 C C   A VAL   B 3   ? 0.1920 0.2288 0.2652 -0.0580 -0.0770 0.1169  3   VAL   B C   
3822 C C   B VAL   B 3   ? 0.2212 0.2412 0.2217 -0.0393 -0.0524 0.0712  3   VAL   B C   
3823 O O   A VAL   B 3   ? 0.1908 0.2382 0.2743 -0.0568 -0.0795 0.1190  3   VAL   B O   
3824 O O   B VAL   B 3   ? 0.2208 0.2449 0.2048 -0.0319 -0.0513 0.0694  3   VAL   B O   
3825 C CB  A VAL   B 3   ? 0.2275 0.2300 0.3689 -0.0676 -0.0740 0.1229  3   VAL   B CB  
3826 C CB  B VAL   B 3   ? 0.2617 0.2684 0.2623 -0.0354 -0.0363 0.0553  3   VAL   B CB  
3827 C CG1 A VAL   B 3   ? 0.2391 0.2206 0.3913 -0.0717 -0.0695 0.1125  3   VAL   B CG1 
3828 C CG1 B VAL   B 3   ? 0.2643 0.2672 0.2664 -0.0362 -0.0333 0.0521  3   VAL   B CG1 
3829 C CG2 A VAL   B 3   ? 0.2323 0.2363 0.3895 -0.0608 -0.0717 0.1231  3   VAL   B CG2 
3830 C CG2 B VAL   B 3   ? 0.2640 0.2697 0.2662 -0.0334 -0.0351 0.0551  3   VAL   B CG2 
3849 N N   . ASN   B 4   ? 0.1876 0.2073 0.2173 -0.0511 -0.0666 0.0820  4   ASN   B N   
3850 C CA  . ASN   B 4   ? 0.1836 0.2009 0.1915 -0.0490 -0.0525 0.0410  4   ASN   B CA  
3851 C C   . ASN   B 4   ? 0.1916 0.2121 0.1792 -0.0469 -0.0350 0.0276  4   ASN   B C   
3852 O O   . ASN   B 4   ? 0.1941 0.2195 0.2075 -0.0418 -0.0218 0.0085  4   ASN   B O   
3853 C CB  . ASN   B 4   ? 0.1818 0.1967 0.1854 -0.0394 -0.0510 0.0363  4   ASN   B CB  
3854 C CG  . ASN   B 4   ? 0.1796 0.1805 0.1702 -0.0379 -0.0455 0.0270  4   ASN   B CG  
3855 O OD1 . ASN   B 4   ? 0.1779 0.1661 0.1704 -0.0356 -0.0443 0.0225  4   ASN   B OD1 
3856 N ND2 . ASN   B 4   ? 0.2001 0.1857 0.1853 -0.0183 -0.0345 0.0208  4   ASN   B ND2 
3864 N N   . SER   B 5   ? 0.2139 0.2339 0.1879 -0.0461 -0.0139 0.0292  5   SER   B N   
3865 C CA  . SER   B 5   ? 0.2411 0.2662 0.2246 -0.0376 0.0015  0.0339  5   SER   B CA  
3866 C C   . SER   B 5   ? 0.2535 0.2652 0.2559 -0.0568 0.0247  0.0378  5   SER   B C   
3867 O O   . SER   B 5   ? 0.2681 0.2633 0.3265 -0.0529 0.0565  0.0397  5   SER   B O   
3868 C CB  . SER   B 5   ? 0.2558 0.2948 0.2538 -0.0288 0.0081  0.0444  5   SER   B CB  
3869 O OG  . SER   B 5   ? 0.2780 0.3208 0.3088 -0.0204 0.0078  0.0467  5   SER   B OG  
3875 N N   . PHE   B 6   ? 0.2682 0.2807 0.2271 -0.0597 0.0313  0.0401  6   PHE   B N   
3876 C CA  . PHE   B 6   ? 0.2771 0.2803 0.1954 -0.0758 0.0339  0.0191  6   PHE   B CA  
3877 C C   . PHE   B 6   ? 0.3317 0.3069 0.2305 -0.0819 0.0532  -0.0128 6   PHE   B C   
3878 O O   . PHE   B 6   ? 0.3467 0.3375 0.2621 -0.0726 0.0366  -0.0273 6   PHE   B O   
3879 C CB  . PHE   B 6   ? 0.2418 0.2580 0.1844 -0.0671 0.0187  0.0146  6   PHE   B CB  
3880 C CG  . PHE   B 6   ? 0.2080 0.2241 0.1762 -0.0629 0.0077  0.0095  6   PHE   B CG  
3881 C CD1 . PHE   B 6   ? 0.2048 0.2009 0.1528 -0.0557 -0.0062 0.0062  6   PHE   B CD1 
3882 C CD2 . PHE   B 6   ? 0.1875 0.2213 0.1799 -0.0516 0.0086  0.0357  6   PHE   B CD2 
3883 C CE1 . PHE   B 6   ? 0.2005 0.1821 0.1630 -0.0429 -0.0113 -0.0038 6   PHE   B CE1 
3884 C CE2 . PHE   B 6   ? 0.1907 0.2082 0.2075 -0.0340 0.0068  0.0227  6   PHE   B CE2 
3885 C CZ  . PHE   B 6   ? 0.1954 0.1873 0.1840 -0.0367 0.0022  -0.0046 6   PHE   B CZ  
3895 N N   A SER   B 7   ? 0.3586 0.2887 0.2254 -0.1007 0.0765  -0.0440 7   SER   B N   
3896 N N   B SER   B 7   ? 0.3430 0.3027 0.2570 -0.0854 0.0568  -0.0143 7   SER   B N   
3897 C CA  A SER   B 7   ? 0.3852 0.2921 0.2629 -0.0981 0.0974  -0.0534 7   SER   B CA  
3898 C CA  B SER   B 7   ? 0.3532 0.3021 0.2900 -0.0822 0.0581  -0.0130 7   SER   B CA  
3899 C C   A SER   B 7   ? 0.3841 0.2820 0.2438 -0.0956 0.1122  -0.0578 7   SER   B C   
3900 C C   B SER   B 7   ? 0.3539 0.2927 0.2859 -0.0815 0.0600  -0.0171 7   SER   B C   
3901 O O   A SER   B 7   ? 0.3891 0.2868 0.2720 -0.0936 0.1118  -0.0534 7   SER   B O   
3902 O O   B SER   B 7   ? 0.3560 0.2952 0.2951 -0.0811 0.0575  -0.0139 7   SER   B O   
3903 C CB  A SER   B 7   ? 0.4049 0.3060 0.3333 -0.0927 0.1090  -0.0550 7   SER   B CB  
3904 C CB  B SER   B 7   ? 0.3599 0.3097 0.3222 -0.0781 0.0583  -0.0090 7   SER   B CB  
3905 O OG  A SER   B 7   ? 0.4186 0.3260 0.3864 -0.0885 0.1095  -0.0489 7   SER   B OG  
3906 O OG  B SER   B 7   ? 0.3645 0.3175 0.3449 -0.0748 0.0561  -0.0053 7   SER   B OG  
3917 N N   A GLY   B 8   ? 0.3814 0.2726 0.2570 -0.0841 0.1187  -0.0595 8   GLY   B N   
3918 N N   B GLY   B 8   ? 0.3525 0.2806 0.2834 -0.0785 0.0648  -0.0256 8   GLY   B N   
3919 C CA  A GLY   B 8   ? 0.3669 0.2578 0.2656 -0.0802 0.1190  -0.0640 8   GLY   B CA  
3920 C CA  B GLY   B 8   ? 0.3468 0.2652 0.2754 -0.0776 0.0712  -0.0368 8   GLY   B CA  
3921 C C   A GLY   B 8   ? 0.3468 0.2360 0.2648 -0.0814 0.1188  -0.0562 8   GLY   B C   
3922 C C   B GLY   B 8   ? 0.3385 0.2471 0.2619 -0.0773 0.0809  -0.0465 8   GLY   B C   
3923 O O   A GLY   B 8   ? 0.3542 0.2341 0.3019 -0.0753 0.1239  -0.0553 8   GLY   B O   
3924 O O   B GLY   B 8   ? 0.3418 0.2505 0.2718 -0.0746 0.0779  -0.0456 8   GLY   B O   
3931 N N   . TYR   B 9   ? 0.3287 0.2282 0.2451 -0.0748 0.0908  -0.0603 9   TYR   B N   
3932 C CA  . TYR   B 9   ? 0.3013 0.1997 0.2176 -0.0604 0.0720  -0.0438 9   TYR   B CA  
3933 C C   . TYR   B 9   ? 0.2905 0.2065 0.1965 -0.0527 0.0438  -0.0336 9   TYR   B C   
3934 O O   . TYR   B 9   ? 0.3066 0.2329 0.2356 -0.0546 0.0409  -0.0193 9   TYR   B O   
3935 C CB  . TYR   B 9   ? 0.2944 0.1753 0.2291 -0.0490 0.0694  -0.0321 9   TYR   B CB  
3936 C CG  . TYR   B 9   ? 0.2875 0.1579 0.2304 -0.0503 0.0668  -0.0395 9   TYR   B CG  
3937 C CD1 . TYR   B 9   ? 0.2933 0.1568 0.2510 -0.0661 0.0608  -0.0372 9   TYR   B CD1 
3938 C CD2 . TYR   B 9   ? 0.2703 0.1487 0.2233 -0.0424 0.0657  -0.0433 9   TYR   B CD2 
3939 C CE1 . TYR   B 9   ? 0.2871 0.1641 0.2546 -0.0728 0.0661  -0.0504 9   TYR   B CE1 
3940 C CE2 . TYR   B 9   ? 0.2712 0.1525 0.2418 -0.0428 0.0643  -0.0465 9   TYR   B CE2 
3941 C CZ  . TYR   B 9   ? 0.2788 0.1682 0.2582 -0.0618 0.0630  -0.0569 9   TYR   B CZ  
3942 O OH  . TYR   B 9   ? 0.2750 0.1909 0.2719 -0.0723 0.0626  -0.0737 9   TYR   B OH  
3953 N N   . LEU   B 10  ? 0.2649 0.1805 0.1789 -0.0438 0.0202  -0.0382 10  LEU   B N   
3954 C CA  . LEU   B 10  ? 0.2598 0.1779 0.1853 -0.0520 -0.0103 -0.0358 10  LEU   B CA  
3955 C C   . LEU   B 10  ? 0.2385 0.1728 0.1874 -0.0475 -0.0232 -0.0328 10  LEU   B C   
3956 O O   . LEU   B 10  ? 0.2224 0.1746 0.2033 -0.0365 -0.0212 -0.0270 10  LEU   B O   
3957 C CB  . LEU   B 10  ? 0.2807 0.1736 0.2058 -0.0589 -0.0324 -0.0246 10  LEU   B CB  
3958 C CG  . LEU   B 10  ? 0.3078 0.1816 0.2482 -0.0559 -0.0580 -0.0121 10  LEU   B CG  
3959 C CD1 . LEU   B 10  ? 0.3245 0.1966 0.2819 -0.0508 -0.0561 -0.0156 10  LEU   B CD1 
3960 C CD2 . LEU   B 10  ? 0.3198 0.1856 0.2794 -0.0577 -0.0509 0.0083  10  LEU   B CD2 
3972 N N   . LYS   B 11  ? 0.2513 0.2009 0.1880 -0.0403 -0.0298 -0.0236 11  LYS   B N   
3973 C CA  . LYS   B 11  ? 0.2724 0.2293 0.2064 -0.0281 -0.0473 -0.0250 11  LYS   B CA  
3974 C C   . LYS   B 11  ? 0.2572 0.2096 0.2125 -0.0520 -0.0473 -0.0349 11  LYS   B C   
3975 O O   . LYS   B 11  ? 0.2751 0.2262 0.2506 -0.0680 -0.0418 -0.0689 11  LYS   B O   
3976 C CB  . LYS   B 11  ? 0.3097 0.2828 0.2549 0.0037  -0.0467 -0.0169 11  LYS   B CB  
3977 C CG  . LYS   B 11  ? 0.3433 0.3212 0.3121 0.0217  -0.0433 -0.0174 11  LYS   B CG  
3978 C CD  . LYS   B 11  ? 0.3674 0.3491 0.3729 0.0311  -0.0379 -0.0204 11  LYS   B CD  
3979 C CE  . LYS   B 11  ? 0.3865 0.3682 0.4210 0.0324  -0.0356 -0.0230 11  LYS   B CE  
3980 N NZ  . LYS   B 11  ? 0.3978 0.3787 0.4490 0.0321  -0.0352 -0.0236 11  LYS   B NZ  
3994 N N   . LEU   B 12  ? 0.2248 0.1835 0.2164 -0.0500 -0.0397 -0.0379 12  LEU   B N   
3995 C CA  . LEU   B 12  ? 0.2136 0.1686 0.2401 -0.0482 -0.0319 -0.0322 12  LEU   B CA  
3996 C C   . LEU   B 12  ? 0.2074 0.1700 0.2541 -0.0489 -0.0467 -0.0274 12  LEU   B C   
3997 O O   . LEU   B 12  ? 0.2048 0.1747 0.2771 -0.0605 -0.0607 -0.0206 12  LEU   B O   
3998 C CB  . LEU   B 12  ? 0.2159 0.1511 0.2403 -0.0384 -0.0177 -0.0373 12  LEU   B CB  
3999 C CG  . LEU   B 12  ? 0.2137 0.1499 0.2402 -0.0365 -0.0121 -0.0248 12  LEU   B CG  
4000 C CD1 . LEU   B 12  ? 0.2256 0.1492 0.2325 -0.0279 -0.0138 -0.0122 12  LEU   B CD1 
4001 C CD2 . LEU   B 12  ? 0.2155 0.1571 0.2649 -0.0340 -0.0113 -0.0357 12  LEU   B CD2 
4013 N N   . THR   B 13  ? 0.2002 0.1754 0.2592 -0.0501 -0.0468 -0.0390 13  THR   B N   
4014 C CA  . THR   B 13  ? 0.1978 0.1809 0.2449 -0.0533 -0.0524 -0.0213 13  THR   B CA  
4015 C C   . THR   B 13  ? 0.2345 0.1941 0.2602 -0.0571 -0.0676 -0.0208 13  THR   B C   
4016 O O   . THR   B 13  ? 0.2495 0.1952 0.2702 -0.0518 -0.0292 -0.0204 13  THR   B O   
4017 C CB  . THR   B 13  ? 0.1821 0.1817 0.2437 -0.0464 -0.0525 -0.0159 13  THR   B CB  
4018 O OG1 . THR   B 13  ? 0.1724 0.1776 0.2499 -0.0369 -0.0402 -0.0192 13  THR   B OG1 
4019 C CG2 . THR   B 13  ? 0.1929 0.1853 0.2503 -0.0469 -0.0353 -0.0057 13  THR   B CG2 
4027 N N   A ASP   B 14  ? 0.2491 0.2073 0.2767 -0.0609 -0.1076 -0.0137 14  ASP   B N   
4028 N N   B ASP   B 14  ? 0.2425 0.2013 0.2725 -0.0532 -0.0739 -0.0133 14  ASP   B N   
4029 C CA  A ASP   B 14  ? 0.2644 0.2267 0.3035 -0.0598 -0.1203 0.0085  14  ASP   B CA  
4030 C CA  B ASP   B 14  ? 0.2494 0.2101 0.2862 -0.0502 -0.0734 -0.0030 14  ASP   B CA  
4031 C C   A ASP   B 14  ? 0.2514 0.2045 0.2556 -0.0642 -0.0946 0.0073  14  ASP   B C   
4032 C C   B ASP   B 14  ? 0.2352 0.1931 0.2490 -0.0521 -0.0740 0.0006  14  ASP   B C   
4033 O O   A ASP   B 14  ? 0.2812 0.2260 0.2679 -0.0654 -0.0877 0.0205  14  ASP   B O   
4034 O O   B ASP   B 14  ? 0.2445 0.1971 0.2459 -0.0511 -0.0744 0.0034  14  ASP   B O   
4035 C CB  A ASP   B 14  ? 0.2888 0.2697 0.3918 -0.0563 -0.1401 0.0116  14  ASP   B CB  
4036 C CB  B ASP   B 14  ? 0.2682 0.2355 0.3371 -0.0464 -0.0695 -0.0009 14  ASP   B CB  
4037 C CG  A ASP   B 14  ? 0.3214 0.3083 0.4813 -0.0486 -0.1331 -0.0010 14  ASP   B CG  
4038 C CG  B ASP   B 14  ? 0.2877 0.2559 0.3828 -0.0416 -0.0615 -0.0022 14  ASP   B CG  
4039 O OD1 A ASP   B 14  ? 0.3404 0.3215 0.5018 -0.0495 -0.1282 -0.0169 14  ASP   B OD1 
4040 O OD1 B ASP   B 14  ? 0.2951 0.2647 0.3935 -0.0412 -0.0575 -0.0058 14  ASP   B OD1 
4041 O OD2 A ASP   B 14  ? 0.3268 0.3231 0.5227 -0.0473 -0.1300 0.0004  14  ASP   B OD2 
4042 O OD2 B ASP   B 14  ? 0.2940 0.2624 0.3997 -0.0410 -0.0597 0.0004  14  ASP   B OD2 
4051 N N   . ASN   B 15  ? 0.2113 0.1752 0.2239 -0.0488 -0.0755 0.0062  15  ASN   B N   
4052 C CA  . ASN   B 15  ? 0.1719 0.1511 0.2068 -0.0332 -0.0513 0.0006  15  ASN   B CA  
4053 C C   . ASN   B 15  ? 0.1536 0.1447 0.1960 -0.0202 -0.0357 -0.0068 15  ASN   B C   
4054 O O   . ASN   B 15  ? 0.1569 0.1409 0.2258 -0.0206 -0.0473 -0.0182 15  ASN   B O   
4055 C CB  . ASN   B 15  ? 0.1682 0.1498 0.2250 -0.0121 -0.0566 0.0017  15  ASN   B CB  
4056 C CG  . ASN   B 15  ? 0.1571 0.1527 0.2265 -0.0160 -0.0290 0.0031  15  ASN   B CG  
4057 O OD1 . ASN   B 15  ? 0.1621 0.1808 0.2556 -0.0352 -0.0311 0.0103  15  ASN   B OD1 
4058 N ND2 . ASN   B 15  ? 0.1583 0.1352 0.2266 -0.0115 -0.0039 -0.0156 15  ASN   B ND2 
4066 N N   . VAL   B 16  ? 0.1568 0.1385 0.1985 -0.0252 -0.0430 -0.0030 16  VAL   B N   
4067 C CA  . VAL   B 16  ? 0.1574 0.1359 0.1900 -0.0222 -0.0350 -0.0212 16  VAL   B CA  
4068 C C   . VAL   B 16  ? 0.1563 0.1436 0.1826 -0.0322 -0.0331 -0.0165 16  VAL   B C   
4069 O O   . VAL   B 16  ? 0.1643 0.1568 0.2094 -0.0293 -0.0288 -0.0250 16  VAL   B O   
4070 C CB  . VAL   B 16  ? 0.1676 0.1380 0.1950 -0.0138 -0.0247 -0.0158 16  VAL   B CB  
4071 C CG1 . VAL   B 16  ? 0.1798 0.1388 0.1920 0.0055  -0.0226 -0.0136 16  VAL   B CG1 
4072 C CG2 . VAL   B 16  ? 0.1706 0.1449 0.2161 -0.0127 -0.0117 -0.0142 16  VAL   B CG2 
4082 N N   . TYR   B 17  ? 0.1639 0.1510 0.1859 -0.0249 -0.0294 -0.0212 17  TYR   B N   
4083 C CA  . TYR   B 17  ? 0.1708 0.1654 0.1765 -0.0325 -0.0291 -0.0008 17  TYR   B CA  
4084 C C   . TYR   B 17  ? 0.1612 0.1420 0.1761 -0.0316 -0.0218 -0.0073 17  TYR   B C   
4085 O O   . TYR   B 17  ? 0.1604 0.1474 0.1890 -0.0210 -0.0343 -0.0347 17  TYR   B O   
4086 C CB  . TYR   B 17  ? 0.2002 0.2018 0.1909 -0.0158 -0.0272 0.0275  17  TYR   B CB  
4087 C CG  . TYR   B 17  ? 0.2291 0.2489 0.2289 -0.0049 -0.0345 0.0312  17  TYR   B CG  
4088 C CD1 . TYR   B 17  ? 0.2421 0.2578 0.2403 -0.0030 -0.0397 0.0474  17  TYR   B CD1 
4089 C CD2 . TYR   B 17  ? 0.2537 0.2770 0.2515 0.0017  -0.0418 0.0294  17  TYR   B CD2 
4090 C CE1 . TYR   B 17  ? 0.2633 0.2858 0.2564 0.0024  -0.0501 0.0461  17  TYR   B CE1 
4091 C CE2 . TYR   B 17  ? 0.2699 0.2975 0.2717 0.0093  -0.0554 0.0379  17  TYR   B CE2 
4092 C CZ  . TYR   B 17  ? 0.2790 0.3086 0.2761 0.0123  -0.0612 0.0466  17  TYR   B CZ  
4093 O OH  . TYR   B 17  ? 0.3000 0.3311 0.3024 0.0202  -0.0657 0.0491  17  TYR   B OH  
4103 N N   . ILE   B 18  ? 0.1703 0.1412 0.1695 -0.0231 -0.0139 -0.0258 18  ILE   B N   
4104 C CA  . ILE   B 18  ? 0.1743 0.1393 0.1636 -0.0259 -0.0131 -0.0170 18  ILE   B CA  
4105 C C   . ILE   B 18  ? 0.1877 0.1390 0.1681 -0.0319 -0.0111 -0.0251 18  ILE   B C   
4106 O O   . ILE   B 18  ? 0.2129 0.1544 0.1778 -0.0303 -0.0004 -0.0320 18  ILE   B O   
4107 C CB  . ILE   B 18  ? 0.1852 0.1419 0.1802 -0.0392 -0.0122 -0.0126 18  ILE   B CB  
4108 C CG1 . ILE   B 18  ? 0.1892 0.1485 0.1892 -0.0390 -0.0066 0.0007  18  ILE   B CG1 
4109 C CG2 . ILE   B 18  ? 0.1893 0.1445 0.1916 -0.0424 -0.0142 -0.0105 18  ILE   B CG2 
4110 C CD1 . ILE   B 18  ? 0.1965 0.1795 0.2180 -0.0315 -0.0234 0.0174  18  ILE   B CD1 
4122 N N   . LYS   B 19  ? 0.1797 0.1422 0.1898 -0.0175 0.0143  -0.0284 19  LYS   B N   
4123 C CA  . LYS   B 19  ? 0.1898 0.1494 0.2021 -0.0232 0.0148  -0.0263 19  LYS   B CA  
4124 C C   . LYS   B 19  ? 0.1767 0.1484 0.2040 -0.0205 0.0231  -0.0351 19  LYS   B C   
4125 O O   . LYS   B 19  ? 0.1766 0.1498 0.1895 -0.0124 0.0121  -0.0330 19  LYS   B O   
4126 C CB  . LYS   B 19  ? 0.2146 0.1671 0.2189 -0.0277 0.0274  -0.0164 19  LYS   B CB  
4127 C CG  . LYS   B 19  ? 0.2385 0.1875 0.2372 -0.0389 0.0363  -0.0168 19  LYS   B CG  
4128 C CD  . LYS   B 19  ? 0.2656 0.2155 0.2430 -0.0471 0.0435  -0.0170 19  LYS   B CD  
4129 C CE  . LYS   B 19  ? 0.2928 0.2417 0.2639 -0.0471 0.0439  -0.0181 19  LYS   B CE  
4130 N NZ  . LYS   B 19  ? 0.3096 0.2580 0.2736 -0.0500 0.0475  -0.0149 19  LYS   B NZ  
4144 N N   . ASN   B 20  ? 0.1727 0.1576 0.2357 -0.0118 0.0323  -0.0509 20  ASN   B N   
4145 C CA  . ASN   B 20  ? 0.1714 0.1700 0.2570 -0.0024 0.0376  -0.0581 20  ASN   B CA  
4146 C C   . ASN   B 20  ? 0.1673 0.1873 0.2681 -0.0139 0.0384  -0.0655 20  ASN   B C   
4147 O O   . ASN   B 20  ? 0.1882 0.2254 0.2912 -0.0317 0.0430  -0.0665 20  ASN   B O   
4148 C CB  . ASN   B 20  ? 0.1997 0.1726 0.2822 0.0088  0.0326  -0.0580 20  ASN   B CB  
4149 C CG  . ASN   B 20  ? 0.2255 0.1808 0.3074 0.0366  0.0344  -0.0636 20  ASN   B CG  
4150 O OD1 . ASN   B 20  ? 0.2591 0.2115 0.3388 0.0532  0.0276  -0.0657 20  ASN   B OD1 
4151 N ND2 . ASN   B 20  ? 0.2137 0.1804 0.2973 0.0371  0.0232  -0.0650 20  ASN   B ND2 
4158 N N   . ALA   B 21  ? 0.1755 0.1649 0.2703 -0.0191 0.0396  -0.0505 21  ALA   B N   
4159 C CA  . ALA   B 21  ? 0.1851 0.1716 0.2782 -0.0298 0.0298  -0.0377 21  ALA   B CA  
4160 C C   . ALA   B 21  ? 0.1918 0.1509 0.2637 -0.0202 0.0280  -0.0227 21  ALA   B C   
4161 O O   . ALA   B 21  ? 0.1960 0.1410 0.2729 -0.0290 0.0276  -0.0208 21  ALA   B O   
4162 C CB  . ALA   B 21  ? 0.2046 0.2004 0.2833 -0.0361 0.0338  -0.0245 21  ALA   B CB  
4168 N N   . ASP   B 22  ? 0.1884 0.1470 0.2621 -0.0226 0.0196  -0.0179 22  ASP   B N   
4169 C CA  . ASP   B 22  ? 0.1801 0.1436 0.2546 -0.0082 0.0139  -0.0139 22  ASP   B CA  
4170 C C   . ASP   B 22  ? 0.1741 0.1453 0.2133 -0.0132 0.0086  -0.0086 22  ASP   B C   
4171 O O   . ASP   B 22  ? 0.1747 0.1488 0.2205 -0.0104 0.0033  -0.0025 22  ASP   B O   
4172 C CB  . ASP   B 22  ? 0.1898 0.1537 0.3004 -0.0051 0.0067  0.0048  22  ASP   B CB  
4173 C CG  . ASP   B 22  ? 0.1912 0.1713 0.3465 -0.0006 -0.0177 0.0073  22  ASP   B CG  
4174 O OD1 . ASP   B 22  ? 0.2032 0.1712 0.3486 0.0033  -0.0347 0.0033  22  ASP   B OD1 
4175 O OD2 . ASP   B 22  ? 0.2008 0.2034 0.3882 0.0071  -0.0222 -0.0070 22  ASP   B OD2 
4180 N N   . ILE   B 23  ? 0.1765 0.1331 0.1884 -0.0125 0.0021  0.0145  23  ILE   B N   
4181 C CA  . ILE   B 23  ? 0.1687 0.1372 0.1777 -0.0104 -0.0083 0.0100  23  ILE   B CA  
4182 C C   . ILE   B 23  ? 0.1576 0.1348 0.1731 -0.0079 -0.0124 0.0033  23  ILE   B C   
4183 O O   . ILE   B 23  ? 0.1555 0.1325 0.1655 -0.0078 -0.0015 0.0085  23  ILE   B O   
4184 C CB  . ILE   B 23  ? 0.1629 0.1442 0.1888 -0.0187 -0.0104 0.0170  23  ILE   B CB  
4185 C CG1 . ILE   B 23  ? 0.1690 0.1519 0.1986 -0.0199 -0.0011 0.0295  23  ILE   B CG1 
4186 C CG2 . ILE   B 23  ? 0.1703 0.1647 0.2021 -0.0160 -0.0044 0.0058  23  ILE   B CG2 
4187 C CD1 . ILE   B 23  ? 0.1709 0.1644 0.2171 -0.0122 0.0036  0.0247  23  ILE   B CD1 
4199 N N   . VAL   B 24  ? 0.1597 0.1346 0.1850 -0.0077 -0.0158 0.0031  24  VAL   B N   
4200 C CA  . VAL   B 24  ? 0.1544 0.1381 0.2127 -0.0047 -0.0226 0.0015  24  VAL   B CA  
4201 C C   . VAL   B 24  ? 0.1520 0.1413 0.2217 -0.0094 -0.0230 0.0057  24  VAL   B C   
4202 O O   . VAL   B 24  ? 0.1487 0.1496 0.2385 -0.0148 -0.0173 0.0146  24  VAL   B O   
4203 C CB  . VAL   B 24  ? 0.1643 0.1624 0.2270 0.0053  -0.0302 0.0058  24  VAL   B CB  
4204 C CG1 . VAL   B 24  ? 0.1609 0.1697 0.2495 -0.0009 -0.0257 0.0026  24  VAL   B CG1 
4205 C CG2 . VAL   B 24  ? 0.1751 0.1905 0.2314 0.0046  -0.0231 0.0009  24  VAL   B CG2 
4215 N N   . GLU   B 25  ? 0.1783 0.1558 0.2167 -0.0053 -0.0136 0.0072  25  GLU   B N   
4216 C CA  . GLU   B 25  ? 0.1922 0.1786 0.2340 0.0074  -0.0019 0.0034  25  GLU   B CA  
4217 C C   . GLU   B 25  ? 0.1820 0.1672 0.2020 -0.0030 0.0044  0.0110  25  GLU   B C   
4218 O O   . GLU   B 25  ? 0.1880 0.1881 0.2127 -0.0035 0.0104  0.0174  25  GLU   B O   
4219 C CB  . GLU   B 25  ? 0.2472 0.2309 0.3053 0.0390  0.0098  -0.0005 25  GLU   B CB  
4220 C CG  . GLU   B 25  ? 0.3076 0.3057 0.4228 0.0527  0.0093  -0.0045 25  GLU   B CG  
4221 C CD  . GLU   B 25  ? 0.3641 0.3733 0.5318 0.0551  0.0060  -0.0064 25  GLU   B CD  
4222 O OE1 . GLU   B 25  ? 0.3887 0.4015 0.5657 0.0604  0.0075  -0.0062 25  GLU   B OE1 
4223 O OE2 . GLU   B 25  ? 0.3893 0.3980 0.5681 0.0547  0.0044  -0.0122 25  GLU   B OE2 
4230 N N   . GLU   B 26  ? 0.1760 0.1612 0.1854 -0.0229 -0.0004 0.0086  26  GLU   B N   
4231 C CA  . GLU   B 26  ? 0.1728 0.1791 0.1896 -0.0323 -0.0107 0.0089  26  GLU   B CA  
4232 C C   . GLU   B 26  ? 0.1601 0.1734 0.1863 -0.0205 0.0007  0.0259  26  GLU   B C   
4233 O O   . GLU   B 26  ? 0.1818 0.1998 0.1926 -0.0219 -0.0072 0.0355  26  GLU   B O   
4234 C CB  . GLU   B 26  ? 0.2007 0.1973 0.2051 -0.0446 -0.0100 0.0123  26  GLU   B CB  
4235 C CG  . GLU   B 26  ? 0.2454 0.2337 0.2588 -0.0465 0.0011  -0.0139 26  GLU   B CG  
4236 C CD  . GLU   B 26  ? 0.2713 0.2558 0.2732 -0.0677 0.0174  -0.0455 26  GLU   B CD  
4237 O OE1 . GLU   B 26  ? 0.2917 0.2392 0.2864 -0.0771 0.0584  -0.0390 26  GLU   B OE1 
4238 O OE2 . GLU   B 26  ? 0.2695 0.2945 0.3092 -0.0631 0.0131  -0.0364 26  GLU   B OE2 
4245 N N   . ALA   B 27  ? 0.1434 0.1580 0.1937 -0.0194 0.0049  0.0236  27  ALA   B N   
4246 C CA  . ALA   B 27  ? 0.1478 0.1532 0.2103 -0.0147 0.0006  0.0331  27  ALA   B CA  
4247 C C   . ALA   B 27  ? 0.1520 0.1645 0.2288 -0.0097 0.0110  0.0424  27  ALA   B C   
4248 O O   . ALA   B 27  ? 0.1657 0.1680 0.2338 0.0038  0.0115  0.0482  27  ALA   B O   
4249 C CB  . ALA   B 27  ? 0.1666 0.1429 0.2189 -0.0177 -0.0025 0.0283  27  ALA   B CB  
4255 N N   . LYS   B 28  ? 0.1455 0.1820 0.2680 -0.0159 0.0188  0.0606  28  LYS   B N   
4256 C CA  . LYS   B 28  ? 0.1742 0.2254 0.2952 -0.0069 0.0529  0.0897  28  LYS   B CA  
4257 C C   . LYS   B 28  ? 0.2039 0.2466 0.2776 0.0056  0.0593  0.0803  28  LYS   B C   
4258 O O   . LYS   B 28  ? 0.2226 0.2453 0.2910 -0.0016 0.0525  0.0792  28  LYS   B O   
4259 C CB  . LYS   B 28  ? 0.2008 0.2617 0.3504 0.0096  0.0837  0.1102  28  LYS   B CB  
4260 C CG  . LYS   B 28  ? 0.2405 0.3055 0.3854 0.0239  0.0976  0.1249  28  LYS   B CG  
4261 C CD  . LYS   B 28  ? 0.3074 0.3616 0.4442 0.0315  0.1120  0.1268  28  LYS   B CD  
4262 C CE  . LYS   B 28  ? 0.3568 0.4007 0.4924 0.0376  0.1133  0.1332  28  LYS   B CE  
4263 N NZ  . LYS   B 28  ? 0.3829 0.4174 0.5160 0.0421  0.1101  0.1389  28  LYS   B NZ  
4277 N N   A LYS   B 29  ? 0.2153 0.2615 0.2724 0.0305  0.0602  0.0715  29  LYS   B N   
4278 N N   B LYS   B 29  ? 0.2235 0.2683 0.2815 0.0120  0.0534  0.0728  29  LYS   B N   
4279 C CA  A LYS   B 29  ? 0.2546 0.2909 0.2911 0.0318  0.0614  0.0640  29  LYS   B CA  
4280 C CA  B LYS   B 29  ? 0.2485 0.2926 0.2956 0.0141  0.0477  0.0656  29  LYS   B CA  
4281 C C   A LYS   B 29  ? 0.2483 0.2939 0.2536 0.0284  0.0509  0.0760  29  LYS   B C   
4282 C C   B LYS   B 29  ? 0.2403 0.2917 0.2616 0.0164  0.0454  0.0727  29  LYS   B C   
4283 O O   A LYS   B 29  ? 0.2663 0.3135 0.2669 0.0309  0.0487  0.0758  29  LYS   B O   
4284 O O   B LYS   B 29  ? 0.2491 0.3004 0.2632 0.0174  0.0440  0.0718  29  LYS   B O   
4285 C CB  A LYS   B 29  ? 0.3072 0.3240 0.3658 0.0306  0.0593  0.0459  29  LYS   B CB  
4286 C CB  B LYS   B 29  ? 0.2832 0.3187 0.3530 0.0136  0.0408  0.0507  29  LYS   B CB  
4287 C CG  A LYS   B 29  ? 0.3507 0.3517 0.4463 0.0265  0.0621  0.0371  29  LYS   B CG  
4288 C CG  B LYS   B 29  ? 0.3123 0.3405 0.4104 0.0125  0.0364  0.0396  29  LYS   B CG  
4289 C CD  A LYS   B 29  ? 0.3840 0.3690 0.5105 0.0209  0.0709  0.0278  29  LYS   B CD  
4290 C CD  B LYS   B 29  ? 0.3324 0.3557 0.4566 0.0105  0.0345  0.0297  29  LYS   B CD  
4291 C CE  A LYS   B 29  ? 0.4099 0.3795 0.5554 0.0169  0.0792  0.0218  29  LYS   B CE  
4292 C CE  B LYS   B 29  ? 0.3467 0.3662 0.4888 0.0088  0.0343  0.0231  29  LYS   B CE  
4293 N NZ  A LYS   B 29  ? 0.4202 0.3866 0.5842 0.0158  0.0816  0.0177  29  LYS   B NZ  
4294 N NZ  B LYS   B 29  ? 0.3556 0.3731 0.5089 0.0086  0.0336  0.0196  29  LYS   B NZ  
4321 N N   . VAL   B 30  ? 0.2213 0.2815 0.2411 0.0154  0.0443  0.0776  30  VAL   B N   
4322 C CA  . VAL   B 30  ? 0.1999 0.2707 0.2678 0.0021  0.0089  0.0769  30  VAL   B CA  
4323 C C   . VAL   B 30  ? 0.1733 0.2632 0.2654 -0.0002 0.0144  0.0964  30  VAL   B C   
4324 O O   . VAL   B 30  ? 0.1892 0.2806 0.2720 0.0113  0.0126  0.1114  30  VAL   B O   
4325 C CB  . VAL   B 30  ? 0.2063 0.2648 0.3036 -0.0125 -0.0258 0.0678  30  VAL   B CB  
4326 C CG1 . VAL   B 30  ? 0.2090 0.2699 0.3008 -0.0151 -0.0286 0.0641  30  VAL   B CG1 
4327 C CG2 . VAL   B 30  ? 0.2153 0.2615 0.3158 -0.0185 -0.0442 0.0566  30  VAL   B CG2 
4338 N N   . LYS   B 31  ? 0.1667 0.2254 0.2961 -0.0217 0.0095  0.1041  31  LYS   B N   
4339 C CA  . LYS   B 31  ? 0.1609 0.2232 0.3300 -0.0396 0.0006  0.1029  31  LYS   B CA  
4340 C C   . LYS   B 31  ? 0.1512 0.1853 0.2901 -0.0306 -0.0242 0.0852  31  LYS   B C   
4341 O O   . LYS   B 31  ? 0.1653 0.1953 0.3109 -0.0239 -0.0199 0.1060  31  LYS   B O   
4342 C CB  . LYS   B 31  ? 0.1877 0.2754 0.3820 -0.0379 0.0189  0.1190  31  LYS   B CB  
4343 C CG  . LYS   B 31  ? 0.2256 0.3312 0.4226 -0.0372 0.0265  0.1162  31  LYS   B CG  
4344 C CD  . LYS   B 31  ? 0.2702 0.3906 0.4567 -0.0322 0.0168  0.1061  31  LYS   B CD  
4345 C CE  . LYS   B 31  ? 0.3055 0.4282 0.4907 -0.0305 0.0037  0.0972  31  LYS   B CE  
4346 N NZ  . LYS   B 31  ? 0.3209 0.4490 0.5047 -0.0272 -0.0072 0.0894  31  LYS   B NZ  
4360 N N   . PRO   B 32  ? 0.1612 0.1512 0.2232 -0.0298 -0.0398 0.0449  32  PRO   B N   
4361 C CA  . PRO   B 32  ? 0.1685 0.1465 0.1871 -0.0285 -0.0421 0.0295  32  PRO   B CA  
4362 C C   . PRO   B 32  ? 0.1802 0.1365 0.1916 -0.0324 -0.0519 0.0315  32  PRO   B C   
4363 O O   . PRO   B 32  ? 0.1893 0.1381 0.2186 -0.0333 -0.0703 0.0347  32  PRO   B O   
4364 C CB  . PRO   B 32  ? 0.1883 0.1386 0.1804 -0.0292 -0.0341 0.0209  32  PRO   B CB  
4365 C CG  . PRO   B 32  ? 0.2043 0.1285 0.1859 -0.0254 -0.0502 0.0257  32  PRO   B CG  
4366 C CD  . PRO   B 32  ? 0.1899 0.1373 0.1984 -0.0173 -0.0551 0.0300  32  PRO   B CD  
4374 N N   . THR   B 33  ? 0.1850 0.1263 0.1726 -0.0254 -0.0506 0.0218  33  THR   B N   
4375 C CA  . THR   B 33  ? 0.1917 0.1329 0.1695 -0.0299 -0.0414 0.0238  33  THR   B CA  
4376 C C   . THR   B 33  ? 0.1964 0.1199 0.1668 -0.0255 -0.0445 0.0175  33  THR   B C   
4377 O O   . THR   B 33  ? 0.2185 0.1234 0.1766 -0.0344 -0.0523 0.0178  33  THR   B O   
4378 C CB  . THR   B 33  ? 0.1996 0.1411 0.1782 -0.0099 -0.0529 0.0276  33  THR   B CB  
4379 O OG1 . THR   B 33  ? 0.1904 0.1473 0.1809 -0.0163 -0.0454 0.0329  33  THR   B OG1 
4380 C CG2 . THR   B 33  ? 0.2210 0.1485 0.2106 -0.0042 -0.0503 0.0222  33  THR   B CG2 
4388 N N   . VAL   B 34  ? 0.1795 0.1222 0.1484 -0.0273 -0.0372 0.0085  34  VAL   B N   
4389 C CA  . VAL   B 34  ? 0.1633 0.1220 0.1470 -0.0211 -0.0345 0.0052  34  VAL   B CA  
4390 C C   . VAL   B 34  ? 0.1467 0.1170 0.1358 -0.0262 -0.0219 0.0056  34  VAL   B C   
4391 O O   . VAL   B 34  ? 0.1645 0.1159 0.1462 -0.0195 -0.0350 0.0059  34  VAL   B O   
4392 C CB  . VAL   B 34  ? 0.1668 0.1355 0.1788 -0.0093 -0.0324 0.0005  34  VAL   B CB  
4393 C CG1 . VAL   B 34  ? 0.1641 0.1508 0.1777 -0.0031 -0.0239 -0.0051 34  VAL   B CG1 
4394 C CG2 . VAL   B 34  ? 0.1796 0.1370 0.2054 -0.0059 -0.0312 0.0009  34  VAL   B CG2 
4404 N N   . VAL   B 35  ? 0.1419 0.1156 0.1354 -0.0267 -0.0167 0.0068  35  VAL   B N   
4405 C CA  . VAL   B 35  ? 0.1372 0.1144 0.1327 -0.0178 -0.0157 0.0057  35  VAL   B CA  
4406 C C   . VAL   B 35  ? 0.1283 0.1088 0.1361 -0.0130 -0.0123 0.0062  35  VAL   B C   
4407 O O   . VAL   B 35  ? 0.1340 0.1142 0.1455 -0.0210 -0.0063 -0.0033 35  VAL   B O   
4408 C CB  . VAL   B 35  ? 0.1394 0.1350 0.1395 -0.0157 -0.0044 0.0037  35  VAL   B CB  
4409 C CG1 . VAL   B 35  ? 0.1310 0.1421 0.1537 -0.0177 -0.0037 0.0047  35  VAL   B CG1 
4410 C CG2 . VAL   B 35  ? 0.1361 0.1361 0.1564 -0.0044 -0.0064 0.0004  35  VAL   B CG2 
4420 N N   . VAL   B 36  ? 0.1323 0.1070 0.1295 -0.0148 -0.0151 0.0070  36  VAL   B N   
4421 C CA  . VAL   B 36  ? 0.1300 0.1042 0.1300 -0.0123 -0.0124 0.0064  36  VAL   B CA  
4422 C C   . VAL   B 36  ? 0.1252 0.1034 0.1201 -0.0124 -0.0083 0.0045  36  VAL   B C   
4423 O O   . VAL   B 36  ? 0.1316 0.1158 0.1469 -0.0117 -0.0070 -0.0040 36  VAL   B O   
4424 C CB  . VAL   B 36  ? 0.1279 0.1131 0.1411 -0.0119 -0.0111 0.0044  36  VAL   B CB  
4425 C CG1 . VAL   B 36  ? 0.1244 0.1252 0.1583 -0.0160 -0.0094 0.0038  36  VAL   B CG1 
4426 C CG2 . VAL   B 36  ? 0.1333 0.1182 0.1438 -0.0113 -0.0183 0.0126  36  VAL   B CG2 
4436 N N   . ASN   B 37  ? 0.1257 0.1165 0.1268 -0.0028 -0.0101 0.0044  37  ASN   B N   
4437 C CA  . ASN   B 37  ? 0.1266 0.1166 0.1420 0.0019  -0.0176 0.0066  37  ASN   B CA  
4438 C C   . ASN   B 37  ? 0.1220 0.1179 0.1307 0.0022  -0.0092 0.0036  37  ASN   B C   
4439 O O   . ASN   B 37  ? 0.1324 0.1255 0.1403 0.0017  -0.0067 0.0090  37  ASN   B O   
4440 C CB  . ASN   B 37  ? 0.1258 0.1195 0.1355 0.0050  -0.0171 0.0042  37  ASN   B CB  
4441 C CG  . ASN   B 37  ? 0.1296 0.1206 0.1404 -0.0004 -0.0190 0.0013  37  ASN   B CG  
4442 O OD1 . ASN   B 37  ? 0.1408 0.1308 0.1510 0.0066  -0.0219 0.0046  37  ASN   B OD1 
4443 N ND2 . ASN   B 37  ? 0.1383 0.1204 0.1434 0.0013  -0.0271 0.0131  37  ASN   B ND2 
4450 N N   . ALA   B 38  ? 0.1317 0.1130 0.1360 0.0069  -0.0040 0.0019  38  ALA   B N   
4451 C CA  . ALA   B 38  ? 0.1437 0.1141 0.1359 -0.0017 0.0035  0.0087  38  ALA   B CA  
4452 C C   . ALA   B 38  ? 0.1390 0.1149 0.1381 -0.0023 -0.0017 0.0041  38  ALA   B C   
4453 O O   . ALA   B 38  ? 0.1460 0.1278 0.1541 0.0057  -0.0040 0.0122  38  ALA   B O   
4454 C CB  . ALA   B 38  ? 0.1661 0.1264 0.1566 -0.0057 0.0095  0.0055  38  ALA   B CB  
4460 N N   . ALA   B 39  ? 0.1415 0.1205 0.1286 0.0055  -0.0076 0.0027  39  ALA   B N   
4461 C CA  . ALA   B 39  ? 0.1507 0.1289 0.1301 0.0030  -0.0116 0.0092  39  ALA   B CA  
4462 C C   . ALA   B 39  ? 0.1459 0.1347 0.1200 0.0039  -0.0094 -0.0004 39  ALA   B C   
4463 O O   . ALA   B 39  ? 0.1480 0.1419 0.1470 -0.0007 -0.0064 0.0103  39  ALA   B O   
4464 C CB  . ALA   B 39  ? 0.1534 0.1340 0.1516 -0.0063 -0.0017 -0.0023 39  ALA   B CB  
4470 N N   . ASN   B 40  ? 0.1515 0.1561 0.1296 -0.0089 -0.0046 -0.0053 40  ASN   B N   
4471 C CA  . ASN   B 40  ? 0.1561 0.1593 0.1388 -0.0040 -0.0119 -0.0058 40  ASN   B CA  
4472 C C   . ASN   B 40  ? 0.1615 0.1619 0.1205 0.0008  -0.0113 0.0000  40  ASN   B C   
4473 O O   . ASN   B 40  ? 0.1586 0.1493 0.1376 0.0018  -0.0183 0.0008  40  ASN   B O   
4474 C CB  . ASN   B 40  ? 0.1759 0.1548 0.1635 0.0078  -0.0161 0.0084  40  ASN   B CB  
4475 C CG  . ASN   B 40  ? 0.1792 0.1605 0.1856 0.0021  -0.0290 0.0125  40  ASN   B CG  
4476 O OD1 . ASN   B 40  ? 0.1747 0.1580 0.2604 0.0052  -0.0337 0.0126  40  ASN   B OD1 
4477 N ND2 . ASN   B 40  ? 0.1837 0.1604 0.1885 0.0045  -0.0204 0.0139  40  ASN   B ND2 
4484 N N   . VAL   B 41  ? 0.1699 0.1639 0.1241 0.0075  -0.0018 0.0016  41  VAL   B N   
4485 C CA  . VAL   B 41  ? 0.1741 0.1745 0.1303 0.0081  -0.0013 -0.0110 41  VAL   B CA  
4486 C C   . VAL   B 41  ? 0.1747 0.1717 0.1314 0.0130  -0.0085 -0.0137 41  VAL   B C   
4487 O O   . VAL   B 41  ? 0.1740 0.1696 0.1423 0.0099  -0.0159 -0.0170 41  VAL   B O   
4488 C CB  . VAL   B 41  ? 0.1888 0.1943 0.1560 -0.0035 0.0128  -0.0234 41  VAL   B CB  
4489 C CG1 . VAL   B 41  ? 0.1852 0.1984 0.1727 -0.0072 0.0202  -0.0238 41  VAL   B CG1 
4490 C CG2 . VAL   B 41  ? 0.1986 0.2129 0.1665 -0.0126 0.0135  -0.0234 41  VAL   B CG2 
4500 N N   . TYR   B 42  ? 0.1793 0.1725 0.1386 0.0127  -0.0220 -0.0007 42  TYR   B N   
4501 C CA  . TYR   B 42  ? 0.1845 0.1831 0.1452 0.0106  -0.0304 -0.0159 42  TYR   B CA  
4502 C C   . TYR   B 42  ? 0.1657 0.1580 0.1521 0.0185  -0.0254 -0.0150 42  TYR   B C   
4503 O O   . TYR   B 42  ? 0.1725 0.1701 0.1844 0.0105  -0.0318 -0.0206 42  TYR   B O   
4504 C CB  . TYR   B 42  ? 0.2168 0.2168 0.1648 0.0048  -0.0374 -0.0056 42  TYR   B CB  
4505 C CG  . TYR   B 42  ? 0.2184 0.2308 0.1591 -0.0046 -0.0332 0.0037  42  TYR   B CG  
4506 C CD1 . TYR   B 42  ? 0.2169 0.2281 0.1347 -0.0106 -0.0216 -0.0087 42  TYR   B CD1 
4507 C CD2 . TYR   B 42  ? 0.2298 0.2462 0.2054 -0.0057 -0.0136 0.0133  42  TYR   B CD2 
4508 C CE1 . TYR   B 42  ? 0.2294 0.2462 0.1539 -0.0047 -0.0139 -0.0017 42  TYR   B CE1 
4509 C CE2 . TYR   B 42  ? 0.2346 0.2546 0.2072 -0.0019 0.0031  0.0228  42  TYR   B CE2 
4510 C CZ  . TYR   B 42  ? 0.2453 0.2666 0.1885 0.0127  0.0091  0.0115  42  TYR   B CZ  
4511 O OH  . TYR   B 42  ? 0.2812 0.2944 0.2399 0.0306  0.0224  0.0248  42  TYR   B OH  
4521 N N   . LEU   B 43  ? 0.1549 0.1455 0.1458 0.0096  -0.0243 -0.0173 43  LEU   B N   
4522 C CA  . LEU   B 43  ? 0.1586 0.1437 0.1430 -0.0008 -0.0189 -0.0048 43  LEU   B CA  
4523 C C   . LEU   B 43  ? 0.1643 0.1496 0.1431 0.0024  -0.0160 -0.0033 43  LEU   B C   
4524 O O   . LEU   B 43  ? 0.1566 0.1576 0.1702 0.0045  -0.0221 0.0059  43  LEU   B O   
4525 C CB  . LEU   B 43  ? 0.1584 0.1371 0.1523 -0.0041 -0.0272 -0.0067 43  LEU   B CB  
4526 C CG  . LEU   B 43  ? 0.1625 0.1391 0.1548 0.0024  -0.0279 -0.0035 43  LEU   B CG  
4527 C CD1 . LEU   B 43  ? 0.1691 0.1412 0.1936 0.0027  -0.0344 -0.0066 43  LEU   B CD1 
4528 C CD2 . LEU   B 43  ? 0.1614 0.1351 0.1575 -0.0044 -0.0287 -0.0122 43  LEU   B CD2 
4540 N N   . LYS   B 44  ? 0.1629 0.1425 0.1486 0.0033  -0.0127 -0.0074 44  LYS   B N   
4541 C CA  . LYS   B 44  ? 0.1753 0.1514 0.1553 0.0035  -0.0159 0.0075  44  LYS   B CA  
4542 C C   . LYS   B 44  ? 0.1606 0.1476 0.1551 0.0104  -0.0179 0.0036  44  LYS   B C   
4543 O O   . LYS   B 44  ? 0.1775 0.1484 0.1795 -0.0002 -0.0108 0.0013  44  LYS   B O   
4544 C CB  . LYS   B 44  ? 0.2049 0.1749 0.1644 0.0158  -0.0243 0.0079  44  LYS   B CB  
4545 C CG  . LYS   B 44  ? 0.2477 0.2052 0.2063 0.0126  -0.0490 0.0059  44  LYS   B CG  
4546 C CD  . LYS   B 44  ? 0.2842 0.2269 0.2581 -0.0034 -0.0613 0.0041  44  LYS   B CD  
4547 C CE  . LYS   B 44  ? 0.3182 0.2529 0.3022 -0.0118 -0.0675 0.0153  44  LYS   B CE  
4548 N NZ  . LYS   B 44  ? 0.3322 0.2634 0.3306 -0.0110 -0.0720 0.0290  44  LYS   B NZ  
4562 N N   . HIS   B 45  ? 0.1586 0.1524 0.1403 0.0041  -0.0183 0.0108  45  HIS   B N   
4563 C CA  . HIS   B 45  ? 0.1645 0.1474 0.1478 0.0084  -0.0136 -0.0027 45  HIS   B CA  
4564 C C   . HIS   B 45  ? 0.1894 0.1623 0.1809 0.0141  -0.0222 -0.0049 45  HIS   B C   
4565 O O   . HIS   B 45  ? 0.1997 0.1914 0.2314 0.0407  0.0042  0.0026  45  HIS   B O   
4566 C CB  . HIS   B 45  ? 0.1583 0.1527 0.1507 -0.0002 -0.0111 -0.0023 45  HIS   B CB  
4567 C CG  . HIS   B 45  ? 0.1588 0.1441 0.1481 -0.0088 -0.0131 0.0007  45  HIS   B CG  
4568 N ND1 . HIS   B 45  ? 0.1601 0.1373 0.1627 -0.0015 -0.0178 -0.0075 45  HIS   B ND1 
4569 C CD2 . HIS   B 45  ? 0.1679 0.1469 0.1765 -0.0126 -0.0182 0.0009  45  HIS   B CD2 
4570 C CE1 . HIS   B 45  ? 0.1664 0.1313 0.1492 -0.0010 -0.0253 -0.0096 45  HIS   B CE1 
4571 N NE2 . HIS   B 45  ? 0.1695 0.1382 0.1590 -0.0039 -0.0246 -0.0051 45  HIS   B NE2 
4579 N N   . GLY   B 46  ? 0.2038 0.1566 0.2128 0.0151  -0.0449 0.0046  46  GLY   B N   
4580 C CA  . GLY   B 46  ? 0.2128 0.1706 0.2455 0.0133  -0.0584 0.0023  46  GLY   B CA  
4581 C C   . GLY   B 46  ? 0.2044 0.1879 0.2955 0.0290  -0.0518 0.0016  46  GLY   B C   
4582 O O   . GLY   B 46  ? 0.2170 0.2164 0.3872 0.0301  -0.0268 -0.0263 46  GLY   B O   
4586 N N   . GLY   B 47  ? 0.1966 0.2005 0.2694 0.0147  -0.0235 -0.0018 47  GLY   B N   
4587 C CA  . GLY   B 47  ? 0.1868 0.1776 0.2295 0.0068  -0.0186 -0.0004 47  GLY   B CA  
4588 C C   . GLY   B 47  ? 0.1655 0.1500 0.1968 0.0078  -0.0029 0.0083  47  GLY   B C   
4589 O O   . GLY   B 47  ? 0.1791 0.1358 0.1966 0.0063  -0.0050 0.0140  47  GLY   B O   
4593 N N   . GLY   B 48  ? 0.1485 0.1429 0.1940 0.0094  -0.0124 0.0191  48  GLY   B N   
4594 C CA  . GLY   B 48  ? 0.1539 0.1315 0.1930 0.0000  -0.0092 0.0135  48  GLY   B CA  
4595 C C   . GLY   B 48  ? 0.1450 0.1285 0.1828 0.0005  0.0001  0.0035  48  GLY   B C   
4596 O O   . GLY   B 48  ? 0.1393 0.1356 0.1984 0.0034  -0.0073 0.0109  48  GLY   B O   
4600 N N   . VAL   B 49  ? 0.1490 0.1357 0.1702 0.0135  -0.0036 0.0094  49  VAL   B N   
4601 C CA  . VAL   B 49  ? 0.1490 0.1420 0.1627 0.0073  -0.0195 -0.0028 49  VAL   B CA  
4602 C C   . VAL   B 49  ? 0.1407 0.1355 0.1458 0.0128  -0.0117 0.0033  49  VAL   B C   
4603 O O   . VAL   B 49  ? 0.1506 0.1401 0.1558 0.0058  -0.0095 0.0096  49  VAL   B O   
4604 C CB  . VAL   B 49  ? 0.1543 0.1635 0.1895 -0.0003 -0.0295 0.0017  49  VAL   B CB  
4605 C CG1 . VAL   B 49  ? 0.1536 0.1744 0.1818 0.0059  -0.0339 0.0075  49  VAL   B CG1 
4606 C CG2 . VAL   B 49  ? 0.1740 0.1736 0.2203 -0.0059 -0.0487 -0.0020 49  VAL   B CG2 
4616 N N   . ALA   B 50  ? 0.1399 0.1292 0.1510 0.0048  -0.0041 0.0044  50  ALA   B N   
4617 C CA  . ALA   B 50  ? 0.1415 0.1247 0.1536 0.0050  -0.0121 0.0081  50  ALA   B CA  
4618 C C   . ALA   B 50  ? 0.1480 0.1293 0.1507 0.0063  -0.0062 0.0088  50  ALA   B C   
4619 O O   . ALA   B 50  ? 0.1446 0.1311 0.1494 0.0080  -0.0065 0.0049  50  ALA   B O   
4620 C CB  . ALA   B 50  ? 0.1425 0.1238 0.1679 0.0024  -0.0030 0.0151  50  ALA   B CB  
4626 N N   . GLY   B 51  ? 0.1424 0.1373 0.1625 0.0093  -0.0138 0.0129  51  GLY   B N   
4627 C CA  . GLY   B 51  ? 0.1420 0.1405 0.1857 0.0136  -0.0213 0.0127  51  GLY   B CA  
4628 C C   . GLY   B 51  ? 0.1419 0.1437 0.1800 0.0145  -0.0118 0.0104  51  GLY   B C   
4629 O O   . GLY   B 51  ? 0.1474 0.1518 0.1995 0.0115  -0.0136 0.0031  51  GLY   B O   
4633 N N   . ALA   B 52  ? 0.1413 0.1335 0.1764 0.0143  -0.0097 0.0176  52  ALA   B N   
4634 C CA  . ALA   B 52  ? 0.1456 0.1458 0.1734 0.0177  -0.0062 0.0064  52  ALA   B CA  
4635 C C   . ALA   B 52  ? 0.1358 0.1452 0.1633 0.0091  -0.0053 0.0040  52  ALA   B C   
4636 O O   . ALA   B 52  ? 0.1440 0.1482 0.1764 0.0157  0.0007  0.0037  52  ALA   B O   
4637 C CB  . ALA   B 52  ? 0.1676 0.1516 0.1799 0.0084  0.0042  0.0016  52  ALA   B CB  
4643 N N   . LEU   B 53  ? 0.1340 0.1391 0.1541 0.0138  -0.0012 0.0105  53  LEU   B N   
4644 C CA  . LEU   B 53  ? 0.1380 0.1475 0.1575 0.0075  -0.0106 0.0099  53  LEU   B CA  
4645 C C   . LEU   B 53  ? 0.1441 0.1398 0.1533 0.0113  -0.0034 0.0129  53  LEU   B C   
4646 O O   . LEU   B 53  ? 0.1465 0.1483 0.1643 0.0011  0.0008  0.0154  53  LEU   B O   
4647 C CB  . LEU   B 53  ? 0.1367 0.1484 0.1699 0.0060  -0.0058 0.0180  53  LEU   B CB  
4648 C CG  . LEU   B 53  ? 0.1346 0.1603 0.1606 0.0008  -0.0079 0.0205  53  LEU   B CG  
4649 C CD1 . LEU   B 53  ? 0.1440 0.1885 0.1942 0.0062  -0.0074 0.0053  53  LEU   B CD1 
4650 C CD2 . LEU   B 53  ? 0.1525 0.1926 0.1917 -0.0095 -0.0120 -0.0116 53  LEU   B CD2 
4662 N N   . ASN   B 54  ? 0.1402 0.1343 0.1499 -0.0012 -0.0083 0.0077  54  ASN   B N   
4663 C CA  . ASN   B 54  ? 0.1441 0.1455 0.1660 -0.0009 -0.0111 0.0054  54  ASN   B CA  
4664 C C   . ASN   B 54  ? 0.1362 0.1437 0.1795 0.0012  -0.0059 0.0096  54  ASN   B C   
4665 O O   . ASN   B 54  ? 0.1368 0.1510 0.1952 0.0009  -0.0028 0.0049  54  ASN   B O   
4666 C CB  . ASN   B 54  ? 0.1506 0.1568 0.1735 0.0017  -0.0068 0.0072  54  ASN   B CB  
4667 C CG  . ASN   B 54  ? 0.1420 0.1650 0.1688 0.0022  -0.0125 0.0013  54  ASN   B CG  
4668 O OD1 . ASN   B 54  ? 0.1424 0.1651 0.1802 0.0027  -0.0178 -0.0112 54  ASN   B OD1 
4669 N ND2 . ASN   B 54  ? 0.1526 0.1855 0.1966 -0.0032 -0.0364 0.0128  54  ASN   B ND2 
4676 N N   . LYS   B 55  ? 0.1366 0.1517 0.1904 0.0084  -0.0065 0.0091  55  LYS   B N   
4677 C CA  . LYS   B 55  ? 0.1413 0.1662 0.2123 0.0174  -0.0113 0.0113  55  LYS   B CA  
4678 C C   . LYS   B 55  ? 0.1368 0.1637 0.2066 0.0139  -0.0062 -0.0000 55  LYS   B C   
4679 O O   . LYS   B 55  ? 0.1324 0.1745 0.2159 0.0120  -0.0031 -0.0045 55  LYS   B O   
4680 C CB  . LYS   B 55  ? 0.1564 0.1770 0.2380 0.0284  0.0009  0.0218  55  LYS   B CB  
4681 C CG  . LYS   B 55  ? 0.1996 0.2040 0.3120 0.0383  0.0206  0.0355  55  LYS   B CG  
4682 C CD  . LYS   B 55  ? 0.2364 0.2267 0.3822 0.0479  0.0407  0.0422  55  LYS   B CD  
4683 C CE  . LYS   B 55  ? 0.2673 0.2538 0.4552 0.0472  0.0545  0.0401  55  LYS   B CE  
4684 N NZ  . LYS   B 55  ? 0.2792 0.2700 0.4906 0.0427  0.0446  0.0454  55  LYS   B NZ  
4698 N N   . ALA   B 56  ? 0.1409 0.1691 0.1871 0.0062  -0.0028 -0.0042 56  ALA   B N   
4699 C CA  . ALA   B 56  ? 0.1550 0.1825 0.1837 0.0019  -0.0010 -0.0016 56  ALA   B CA  
4700 C C   . ALA   B 56  ? 0.1524 0.1774 0.1803 0.0063  0.0065  0.0064  56  ALA   B C   
4701 O O   . ALA   B 56  ? 0.1693 0.1841 0.2020 0.0124  0.0259  0.0110  56  ALA   B O   
4702 C CB  . ALA   B 56  ? 0.1694 0.2064 0.1830 -0.0127 -0.0013 -0.0031 56  ALA   B CB  
4708 N N   . THR   B 57  ? 0.1485 0.1685 0.1897 0.0073  0.0084  0.0106  57  THR   B N   
4709 C CA  . THR   B 57  ? 0.1525 0.1664 0.1890 0.0026  0.0135  0.0198  57  THR   B CA  
4710 C C   . THR   B 57  ? 0.1512 0.1754 0.2096 0.0006  0.0125  0.0202  57  THR   B C   
4711 O O   . THR   B 57  ? 0.1632 0.1740 0.2199 -0.0175 0.0133  0.0132  57  THR   B O   
4712 C CB  . THR   B 57  ? 0.1565 0.1506 0.1720 -0.0004 0.0132  0.0186  57  THR   B CB  
4713 O OG1 . THR   B 57  ? 0.1561 0.1473 0.1871 0.0008  0.0092  0.0080  57  THR   B OG1 
4714 C CG2 . THR   B 57  ? 0.1533 0.1529 0.1763 -0.0052 0.0037  0.0135  57  THR   B CG2 
4722 N N   . ASN   B 58  ? 0.1310 0.2020 0.2313 -0.0129 -0.0012 0.0069  58  ASN   B N   
4723 C CA  . ASN   B 58  ? 0.1678 0.2561 0.2764 -0.0271 0.0200  0.0181  58  ASN   B CA  
4724 C C   . ASN   B 58  ? 0.1407 0.2217 0.2391 -0.0180 -0.0074 0.0078  58  ASN   B C   
4725 O O   . ASN   B 58  ? 0.1469 0.2240 0.2491 -0.0227 -0.0030 0.0045  58  ASN   B O   
4726 C CB  . ASN   B 58  ? 0.2994 0.3652 0.4218 -0.0400 0.0500  0.0330  58  ASN   B CB  
4727 C CG  . ASN   B 58  ? 0.4275 0.4616 0.5771 -0.0416 0.0701  0.0481  58  ASN   B CG  
4728 O OD1 . ASN   B 58  ? 0.4832 0.4916 0.6313 -0.0422 0.0753  0.0529  58  ASN   B OD1 
4729 N ND2 . ASN   B 58  ? 0.5013 0.5013 0.6317 -0.0423 0.0769  0.0513  58  ASN   B ND2 
4736 N N   . ASN   B 59  ? 0.1352 0.1969 0.2183 -0.0105 -0.0101 0.0085  59  ASN   B N   
4737 C CA  . ASN   B 59  ? 0.1381 0.1977 0.2124 -0.0135 -0.0161 0.0210  59  ASN   B CA  
4738 C C   . ASN   B 59  ? 0.1358 0.1891 0.2066 -0.0137 -0.0161 0.0095  59  ASN   B C   
4739 O O   . ASN   B 59  ? 0.1406 0.1910 0.2050 -0.0121 -0.0162 0.0027  59  ASN   B O   
4740 C CB  . ASN   B 59  ? 0.1538 0.2155 0.2248 -0.0084 -0.0277 0.0231  59  ASN   B CB  
4741 C CG  . ASN   B 59  ? 0.1706 0.2349 0.2445 -0.0040 -0.0372 0.0168  59  ASN   B CG  
4742 O OD1 . ASN   B 59  ? 0.1760 0.2401 0.2286 -0.0003 -0.0259 0.0297  59  ASN   B OD1 
4743 N ND2 . ASN   B 59  ? 0.1793 0.2428 0.2610 -0.0134 -0.0425 0.0145  59  ASN   B ND2 
4750 N N   . ALA   B 60  ? 0.1440 0.1764 0.2025 -0.0124 -0.0084 0.0110  60  ALA   B N   
4751 C CA  . ALA   B 60  ? 0.1509 0.1640 0.2025 -0.0204 -0.0033 0.0117  60  ALA   B CA  
4752 C C   . ALA   B 60  ? 0.1541 0.1539 0.1851 -0.0126 -0.0134 0.0094  60  ALA   B C   
4753 O O   . ALA   B 60  ? 0.1537 0.1577 0.1905 -0.0170 -0.0033 -0.0053 60  ALA   B O   
4754 C CB  . ALA   B 60  ? 0.1632 0.1622 0.2294 -0.0177 0.0049  0.0152  60  ALA   B CB  
4760 N N   . MET   B 61  ? 0.1441 0.1462 0.1816 -0.0121 -0.0084 0.0070  61  MET   B N   
4761 C CA  . MET   B 61  ? 0.1397 0.1442 0.1793 -0.0069 -0.0156 0.0105  61  MET   B CA  
4762 C C   . MET   B 61  ? 0.1442 0.1451 0.1764 -0.0079 -0.0127 0.0123  61  MET   B C   
4763 O O   . MET   B 61  ? 0.1492 0.1421 0.1709 -0.0068 -0.0081 -0.0027 61  MET   B O   
4764 C CB  . MET   B 61  ? 0.1387 0.1491 0.1774 -0.0047 -0.0170 0.0048  61  MET   B CB  
4765 C CG  . MET   B 61  ? 0.1419 0.1530 0.1662 -0.0020 -0.0137 0.0040  61  MET   B CG  
4766 S SD  . MET   B 61  ? 0.1422 0.1508 0.1840 -0.0042 -0.0095 -0.0072 61  MET   B SD  
4767 C CE  . MET   B 61  ? 0.1513 0.1715 0.2069 0.0035  -0.0055 -0.0223 61  MET   B CE  
4777 N N   . GLN   B 62  ? 0.1426 0.1474 0.1726 -0.0021 -0.0179 0.0115  62  GLN   B N   
4778 C CA  . GLN   B 62  ? 0.1419 0.1501 0.1851 -0.0015 -0.0206 -0.0040 62  GLN   B CA  
4779 C C   . GLN   B 62  ? 0.1483 0.1572 0.1873 -0.0089 -0.0246 -0.0063 62  GLN   B C   
4780 O O   . GLN   B 62  ? 0.1593 0.1554 0.1843 -0.0066 -0.0319 -0.0164 62  GLN   B O   
4781 C CB  . GLN   B 62  ? 0.1476 0.1565 0.1793 0.0019  -0.0231 0.0017  62  GLN   B CB  
4782 C CG  . GLN   B 62  ? 0.1514 0.1632 0.1791 0.0004  -0.0243 -0.0058 62  GLN   B CG  
4783 C CD  . GLN   B 62  ? 0.1538 0.1546 0.1625 0.0012  -0.0277 0.0067  62  GLN   B CD  
4784 O OE1 . GLN   B 62  ? 0.1556 0.1531 0.1861 -0.0018 -0.0268 -0.0032 62  GLN   B OE1 
4785 N NE2 . GLN   B 62  ? 0.1558 0.1568 0.1744 -0.0012 -0.0270 -0.0052 62  GLN   B NE2 
4794 N N   . VAL   B 63  ? 0.1470 0.1638 0.1982 -0.0122 -0.0265 -0.0112 63  VAL   B N   
4795 C CA  . VAL   B 63  ? 0.1618 0.1609 0.2135 -0.0173 -0.0327 -0.0065 63  VAL   B CA  
4796 C C   . VAL   B 63  ? 0.1623 0.1457 0.1983 -0.0190 -0.0402 -0.0148 63  VAL   B C   
4797 O O   . VAL   B 63  ? 0.1748 0.1498 0.2142 -0.0138 -0.0509 -0.0165 63  VAL   B O   
4798 C CB  . VAL   B 63  ? 0.1615 0.1769 0.2502 -0.0226 -0.0295 -0.0061 63  VAL   B CB  
4799 C CG1 . VAL   B 63  ? 0.1701 0.1796 0.2652 -0.0343 -0.0239 -0.0127 63  VAL   B CG1 
4800 C CG2 . VAL   B 63  ? 0.1565 0.1931 0.2664 -0.0139 -0.0302 -0.0044 63  VAL   B CG2 
4810 N N   . GLU   B 64  ? 0.1588 0.1402 0.1947 -0.0143 -0.0266 -0.0107 64  GLU   B N   
4811 C CA  . GLU   B 64  ? 0.1615 0.1367 0.1824 -0.0125 -0.0286 -0.0085 64  GLU   B CA  
4812 C C   . GLU   B 64  ? 0.1563 0.1354 0.1769 -0.0095 -0.0249 -0.0187 64  GLU   B C   
4813 O O   . GLU   B 64  ? 0.1691 0.1440 0.1813 -0.0124 -0.0288 -0.0137 64  GLU   B O   
4814 C CB  . GLU   B 64  ? 0.1674 0.1451 0.1814 -0.0158 -0.0243 -0.0019 64  GLU   B CB  
4815 C CG  . GLU   B 64  ? 0.1723 0.1523 0.1837 -0.0276 -0.0276 -0.0065 64  GLU   B CG  
4816 C CD  . GLU   B 64  ? 0.1762 0.1638 0.1943 -0.0303 -0.0298 -0.0120 64  GLU   B CD  
4817 O OE1 . GLU   B 64  ? 0.1803 0.1817 0.2076 -0.0336 -0.0252 -0.0268 64  GLU   B OE1 
4818 O OE2 . GLU   B 64  ? 0.1903 0.1793 0.1950 -0.0335 -0.0481 -0.0085 64  GLU   B OE2 
4825 N N   . SER   B 65  ? 0.1542 0.1284 0.1743 -0.0071 -0.0124 -0.0160 65  SER   B N   
4826 C CA  . SER   B 65  ? 0.1565 0.1320 0.1749 -0.0049 -0.0204 -0.0153 65  SER   B CA  
4827 C C   . SER   B 65  ? 0.1587 0.1358 0.1688 -0.0009 -0.0294 -0.0150 65  SER   B C   
4828 O O   . SER   B 65  ? 0.1612 0.1459 0.1727 -0.0028 -0.0265 -0.0258 65  SER   B O   
4829 C CB  . SER   B 65  ? 0.1613 0.1427 0.1785 -0.0103 -0.0216 -0.0118 65  SER   B CB  
4830 O OG  . SER   B 65  ? 0.1594 0.1423 0.1756 -0.0089 -0.0225 -0.0220 65  SER   B OG  
4836 N N   . ASP   B 66  ? 0.1658 0.1423 0.1738 -0.0032 -0.0310 -0.0154 66  ASP   B N   
4837 C CA  . ASP   B 66  ? 0.1744 0.1547 0.1684 -0.0009 -0.0312 -0.0121 66  ASP   B CA  
4838 C C   . ASP   B 66  ? 0.1767 0.1588 0.1651 -0.0047 -0.0268 -0.0124 66  ASP   B C   
4839 O O   . ASP   B 66  ? 0.1810 0.1622 0.1746 0.0005  -0.0286 -0.0230 66  ASP   B O   
4840 C CB  . ASP   B 66  ? 0.1958 0.1725 0.1851 0.0082  -0.0439 -0.0166 66  ASP   B CB  
4841 C CG  . ASP   B 66  ? 0.2264 0.1902 0.2090 0.0160  -0.0690 0.0006  66  ASP   B CG  
4842 O OD1 . ASP   B 66  ? 0.2490 0.1833 0.2279 0.0097  -0.0608 0.0045  66  ASP   B OD1 
4843 O OD2 . ASP   B 66  ? 0.2450 0.2171 0.2694 0.0311  -0.0712 -0.0069 66  ASP   B OD2 
4848 N N   . ASP   B 67  ? 0.1712 0.1503 0.1639 -0.0145 -0.0244 -0.0166 67  ASP   B N   
4849 C CA  . ASP   B 67  ? 0.1909 0.1462 0.1781 -0.0105 -0.0275 -0.0099 67  ASP   B CA  
4850 C C   . ASP   B 67  ? 0.1865 0.1457 0.1863 -0.0032 -0.0261 -0.0175 67  ASP   B C   
4851 O O   . ASP   B 67  ? 0.1892 0.1541 0.1914 -0.0046 -0.0194 -0.0265 67  ASP   B O   
4852 C CB  . ASP   B 67  ? 0.2150 0.1537 0.2026 -0.0163 -0.0420 -0.0061 67  ASP   B CB  
4853 C CG  . ASP   B 67  ? 0.2451 0.1616 0.2136 -0.0168 -0.0678 -0.0114 67  ASP   B CG  
4854 O OD1 . ASP   B 67  ? 0.2647 0.1691 0.2250 -0.0182 -0.0632 -0.0036 67  ASP   B OD1 
4855 O OD2 . ASP   B 67  ? 0.2624 0.1699 0.2330 -0.0051 -0.0716 -0.0126 67  ASP   B OD2 
4860 N N   . TYR   B 68  ? 0.1783 0.1484 0.1713 -0.0034 -0.0393 -0.0233 68  TYR   B N   
4861 C CA  . TYR   B 68  ? 0.1751 0.1637 0.1903 0.0028  -0.0390 -0.0347 68  TYR   B CA  
4862 C C   . TYR   B 68  ? 0.1675 0.1612 0.1811 0.0002  -0.0396 -0.0406 68  TYR   B C   
4863 O O   . TYR   B 68  ? 0.1744 0.1720 0.1867 0.0064  -0.0332 -0.0524 68  TYR   B O   
4864 C CB  . TYR   B 68  ? 0.1781 0.1854 0.1876 0.0045  -0.0413 -0.0438 68  TYR   B CB  
4865 C CG  . TYR   B 68  ? 0.1889 0.1998 0.2049 0.0091  -0.0326 -0.0659 68  TYR   B CG  
4866 C CD1 . TYR   B 68  ? 0.1912 0.2060 0.2309 -0.0082 -0.0327 -0.0737 68  TYR   B CD1 
4867 C CD2 . TYR   B 68  ? 0.1951 0.2174 0.2288 0.0172  -0.0448 -0.0646 68  TYR   B CD2 
4868 C CE1 . TYR   B 68  ? 0.2006 0.2243 0.2580 -0.0022 -0.0331 -0.0670 68  TYR   B CE1 
4869 C CE2 . TYR   B 68  ? 0.1985 0.2260 0.2338 0.0141  -0.0379 -0.0704 68  TYR   B CE2 
4870 C CZ  . TYR   B 68  ? 0.1926 0.2272 0.2482 0.0031  -0.0419 -0.0727 68  TYR   B CZ  
4871 O OH  . TYR   B 68  ? 0.1874 0.2452 0.2744 0.0049  -0.0332 -0.0507 68  TYR   B OH  
4881 N N   . ILE   B 69  ? 0.1674 0.1511 0.1879 0.0004  -0.0310 -0.0397 69  ILE   B N   
4882 C CA  . ILE   B 69  ? 0.1760 0.1557 0.1943 -0.0051 -0.0229 -0.0407 69  ILE   B CA  
4883 C C   . ILE   B 69  ? 0.1737 0.1547 0.1888 0.0064  -0.0343 -0.0310 69  ILE   B C   
4884 O O   . ILE   B 69  ? 0.1749 0.1631 0.1881 -0.0003 -0.0238 -0.0345 69  ILE   B O   
4885 C CB  . ILE   B 69  ? 0.1837 0.1648 0.2178 -0.0072 -0.0041 -0.0295 69  ILE   B CB  
4886 C CG1 . ILE   B 69  ? 0.1783 0.1676 0.2200 -0.0073 -0.0006 -0.0299 69  ILE   B CG1 
4887 C CG2 . ILE   B 69  ? 0.2010 0.1690 0.2314 -0.0043 -0.0071 -0.0268 69  ILE   B CG2 
4888 C CD1 . ILE   B 69  ? 0.1674 0.1724 0.2388 -0.0189 0.0027  -0.0316 69  ILE   B CD1 
4900 N N   . ALA   B 70  ? 0.1751 0.1539 0.1912 0.0031  -0.0402 -0.0275 70  ALA   B N   
4901 C CA  . ALA   B 70  ? 0.1785 0.1572 0.1785 -0.0001 -0.0426 -0.0230 70  ALA   B CA  
4902 C C   . ALA   B 70  ? 0.1837 0.1545 0.1854 -0.0038 -0.0528 -0.0270 70  ALA   B C   
4903 O O   . ALA   B 70  ? 0.1921 0.1520 0.1960 -0.0009 -0.0450 -0.0348 70  ALA   B O   
4904 C CB  . ALA   B 70  ? 0.1788 0.1744 0.1841 -0.0033 -0.0447 -0.0226 70  ALA   B CB  
4910 N N   . THR   B 71  ? 0.1888 0.1574 0.1982 0.0027  -0.0567 -0.0291 71  THR   B N   
4911 C CA  . THR   B 71  ? 0.2033 0.1584 0.2151 0.0065  -0.0706 -0.0337 71  THR   B CA  
4912 C C   . THR   B 71  ? 0.1960 0.1613 0.2323 0.0263  -0.0602 -0.0501 71  THR   B C   
4913 O O   . THR   B 71  ? 0.2047 0.1719 0.2747 0.0299  -0.0535 -0.0692 71  THR   B O   
4914 C CB  . THR   B 71  ? 0.2300 0.1834 0.2362 -0.0052 -0.0832 -0.0130 71  THR   B CB  
4915 O OG1 . THR   B 71  ? 0.2430 0.2120 0.2696 -0.0199 -0.0778 0.0132  71  THR   B OG1 
4916 C CG2 . THR   B 71  ? 0.2501 0.1839 0.2695 0.0013  -0.0703 -0.0018 71  THR   B CG2 
4924 N N   . ASN   B 72  ? 0.1811 0.1679 0.2255 0.0139  -0.0556 -0.0676 72  ASN   B N   
4925 C CA  . ASN   B 72  ? 0.1854 0.1850 0.2233 0.0181  -0.0464 -0.0711 72  ASN   B CA  
4926 C C   . ASN   B 72  ? 0.1864 0.1948 0.2342 0.0042  -0.0300 -0.0730 72  ASN   B C   
4927 O O   . ASN   B 72  ? 0.1859 0.2122 0.2623 0.0058  -0.0181 -0.0747 72  ASN   B O   
4928 C CB  . ASN   B 72  ? 0.1903 0.2017 0.2315 0.0180  -0.0586 -0.0635 72  ASN   B CB  
4929 C CG  . ASN   B 72  ? 0.2054 0.2202 0.2395 0.0320  -0.0663 -0.0391 72  ASN   B CG  
4930 O OD1 . ASN   B 72  ? 0.2288 0.2404 0.2469 0.0156  -0.0487 -0.0414 72  ASN   B OD1 
4931 N ND2 . ASN   B 72  ? 0.2200 0.2264 0.2815 0.0410  -0.0530 -0.0108 72  ASN   B ND2 
4938 N N   . GLY   B 73  ? 0.1901 0.1941 0.2157 -0.0042 -0.0364 -0.0659 73  GLY   B N   
4939 C CA  . GLY   B 73  ? 0.1884 0.1998 0.1959 -0.0056 -0.0356 -0.0528 73  GLY   B CA  
4940 C C   . GLY   B 73  ? 0.1788 0.1979 0.1569 0.0043  -0.0304 -0.0470 73  GLY   B C   
4941 O O   . GLY   B 73  ? 0.1739 0.1875 0.1666 0.0068  -0.0232 -0.0345 73  GLY   B O   
4945 N N   . PRO   B 74  ? 0.1774 0.2070 0.1514 0.0055  -0.0299 -0.0353 74  PRO   B N   
4946 C CA  . PRO   B 74  ? 0.1709 0.2055 0.1439 0.0055  -0.0277 -0.0229 74  PRO   B CA  
4947 C C   . PRO   B 74  ? 0.1576 0.1913 0.1481 0.0051  -0.0208 -0.0218 74  PRO   B C   
4948 O O   . PRO   B 74  ? 0.1610 0.1928 0.1897 0.0057  -0.0194 -0.0329 74  PRO   B O   
4949 C CB  . PRO   B 74  ? 0.1900 0.2247 0.1432 0.0048  -0.0276 -0.0180 74  PRO   B CB  
4950 C CG  . PRO   B 74  ? 0.2042 0.2325 0.1706 0.0062  -0.0167 -0.0190 74  PRO   B CG  
4951 C CD  . PRO   B 74  ? 0.2038 0.2254 0.1639 0.0091  -0.0151 -0.0292 74  PRO   B CD  
4959 N N   . LEU   B 75  ? 0.1550 0.1846 0.1325 0.0031  -0.0200 -0.0222 75  LEU   B N   
4960 C CA  . LEU   B 75  ? 0.1611 0.1831 0.1419 -0.0022 -0.0158 -0.0071 75  LEU   B CA  
4961 C C   . LEU   B 75  ? 0.1652 0.1923 0.1362 0.0008  -0.0073 -0.0122 75  LEU   B C   
4962 O O   . LEU   B 75  ? 0.1825 0.2099 0.1449 0.0009  -0.0066 -0.0041 75  LEU   B O   
4963 C CB  . LEU   B 75  ? 0.1691 0.1838 0.1337 -0.0111 -0.0249 0.0092  75  LEU   B CB  
4964 C CG  . LEU   B 75  ? 0.2006 0.2000 0.1414 -0.0326 -0.0155 0.0002  75  LEU   B CG  
4965 C CD1 . LEU   B 75  ? 0.2309 0.2168 0.1502 -0.0412 0.0067  -0.0068 75  LEU   B CD1 
4966 C CD2 . LEU   B 75  ? 0.2371 0.2200 0.2106 -0.0263 -0.0009 0.0119  75  LEU   B CD2 
4978 N N   . LYS   B 76  ? 0.1620 0.2102 0.1607 0.0004  -0.0064 -0.0073 76  LYS   B N   
4979 C CA  . LYS   B 76  ? 0.1722 0.2194 0.1877 -0.0085 0.0164  -0.0077 76  LYS   B CA  
4980 C C   . LYS   B 76  ? 0.1593 0.1999 0.1559 0.0034  0.0015  0.0116  76  LYS   B C   
4981 O O   . LYS   B 76  ? 0.1599 0.1861 0.1618 -0.0024 -0.0067 0.0107  76  LYS   B O   
4982 C CB  . LYS   B 76  ? 0.1912 0.2309 0.2640 -0.0136 0.0370  -0.0429 76  LYS   B CB  
4983 C CG  . LYS   B 76  ? 0.2042 0.2533 0.3309 -0.0007 0.0262  -0.0538 76  LYS   B CG  
4984 C CD  . LYS   B 76  ? 0.2097 0.2672 0.3869 0.0064  0.0071  -0.0687 76  LYS   B CD  
4985 C CE  . LYS   B 76  ? 0.2136 0.2868 0.4434 0.0077  -0.0091 -0.0786 76  LYS   B CE  
4986 N NZ  . LYS   B 76  ? 0.2128 0.2957 0.4747 0.0047  -0.0302 -0.0982 76  LYS   B NZ  
5000 N N   . VAL   B 77  ? 0.1718 0.2107 0.1459 0.0127  0.0021  0.0116  77  VAL   B N   
5001 C CA  . VAL   B 77  ? 0.1676 0.1984 0.1576 0.0247  0.0100  0.0307  77  VAL   B CA  
5002 C C   . VAL   B 77  ? 0.1590 0.1803 0.1514 0.0209  0.0096  0.0299  77  VAL   B C   
5003 O O   . VAL   B 77  ? 0.1626 0.1783 0.1631 0.0297  0.0192  0.0222  77  VAL   B O   
5004 C CB  . VAL   B 77  ? 0.1795 0.2057 0.1862 0.0239  0.0270  0.0493  77  VAL   B CB  
5005 C CG1 . VAL   B 77  ? 0.1904 0.1942 0.2223 0.0156  0.0297  0.0639  77  VAL   B CG1 
5006 C CG2 . VAL   B 77  ? 0.1910 0.2290 0.2159 0.0226  0.0097  0.0492  77  VAL   B CG2 
5016 N N   . GLY   B 78  ? 0.1510 0.1712 0.1517 0.0157  0.0124  0.0210  78  GLY   B N   
5017 C CA  . GLY   B 78  ? 0.1492 0.1652 0.1559 0.0129  0.0093  0.0128  78  GLY   B CA  
5018 C C   . GLY   B 78  ? 0.1456 0.1546 0.1480 0.0086  0.0075  0.0109  78  GLY   B C   
5019 O O   . GLY   B 78  ? 0.1564 0.1487 0.1639 0.0138  0.0067  0.0137  78  GLY   B O   
5023 N N   . GLY   B 79  ? 0.1440 0.1575 0.1490 0.0089  0.0122  0.0066  79  GLY   B N   
5024 C CA  . GLY   B 79  ? 0.1484 0.1504 0.1486 0.0136  0.0036  0.0037  79  GLY   B CA  
5025 C C   . GLY   B 79  ? 0.1365 0.1403 0.1532 0.0117  0.0006  0.0009  79  GLY   B C   
5026 O O   . GLY   B 79  ? 0.1456 0.1384 0.1625 0.0073  0.0127  0.0141  79  GLY   B O   
5030 N N   . SER   B 80  ? 0.1393 0.1311 0.1672 0.0038  0.0076  -0.0002 80  SER   B N   
5031 C CA  . SER   B 80  ? 0.1412 0.1280 0.1692 0.0027  -0.0025 0.0025  80  SER   B CA  
5032 C C   . SER   B 80  ? 0.1423 0.1317 0.1647 0.0078  -0.0156 -0.0028 80  SER   B C   
5033 O O   . SER   B 80  ? 0.1567 0.1338 0.1906 0.0082  -0.0032 -0.0114 80  SER   B O   
5034 C CB  . SER   B 80  ? 0.1430 0.1331 0.1712 -0.0034 -0.0060 0.0035  80  SER   B CB  
5035 O OG  . SER   B 80  ? 0.1504 0.1511 0.1904 -0.0040 -0.0158 0.0140  80  SER   B OG  
5041 N N   . CYS   B 81  ? 0.1391 0.1139 0.1724 -0.0039 -0.0071 -0.0031 81  CYS   B N   
5042 C CA  . CYS   B 81  ? 0.1464 0.1156 0.1728 0.0034  -0.0165 -0.0012 81  CYS   B CA  
5043 C C   . CYS   B 81  ? 0.1413 0.1136 0.1466 0.0030  -0.0208 -0.0019 81  CYS   B C   
5044 O O   . CYS   B 81  ? 0.1680 0.1173 0.1567 0.0079  -0.0107 -0.0096 81  CYS   B O   
5045 C CB  . CYS   B 81  ? 0.1597 0.1307 0.1714 -0.0074 -0.0203 -0.0051 81  CYS   B CB  
5046 S SG  . CYS   B 81  ? 0.1603 0.1514 0.1581 -0.0061 -0.0276 -0.0104 81  CYS   B SG  
5052 N N   . VAL   B 82  ? 0.1494 0.1144 0.1559 -0.0009 -0.0180 -0.0057 82  VAL   B N   
5053 C CA  . VAL   B 82  ? 0.1509 0.1181 0.1524 -0.0056 -0.0123 0.0031  82  VAL   B CA  
5054 C C   . VAL   B 82  ? 0.1551 0.1138 0.1650 -0.0006 -0.0074 -0.0033 82  VAL   B C   
5055 O O   . VAL   B 82  ? 0.1656 0.1150 0.1892 -0.0015 -0.0078 -0.0145 82  VAL   B O   
5056 C CB  . VAL   B 82  ? 0.1601 0.1447 0.1729 -0.0026 -0.0125 0.0093  82  VAL   B CB  
5057 C CG1 . VAL   B 82  ? 0.1811 0.1680 0.1813 0.0018  -0.0102 0.0142  82  VAL   B CG1 
5058 C CG2 . VAL   B 82  ? 0.1689 0.1586 0.1854 -0.0065 -0.0230 0.0137  82  VAL   B CG2 
5068 N N   . LEU   B 83  ? 0.1426 0.1142 0.1623 -0.0156 -0.0198 -0.0093 83  LEU   B N   
5069 C CA  . LEU   B 83  ? 0.1428 0.1177 0.1500 -0.0115 -0.0195 -0.0031 83  LEU   B CA  
5070 C C   . LEU   B 83  ? 0.1504 0.1173 0.1547 -0.0182 -0.0165 -0.0026 83  LEU   B C   
5071 O O   . LEU   B 83  ? 0.1530 0.1295 0.1388 -0.0211 -0.0137 0.0092  83  LEU   B O   
5072 C CB  . LEU   B 83  ? 0.1550 0.1334 0.1550 -0.0127 -0.0271 -0.0115 83  LEU   B CB  
5073 C CG  . LEU   B 83  ? 0.1763 0.1574 0.1635 -0.0184 -0.0209 -0.0086 83  LEU   B CG  
5074 C CD1 . LEU   B 83  ? 0.1848 0.1658 0.1713 -0.0136 -0.0293 -0.0070 83  LEU   B CD1 
5075 C CD2 . LEU   B 83  ? 0.1908 0.1631 0.1760 -0.0117 -0.0118 -0.0237 83  LEU   B CD2 
5087 N N   . SER   B 84  ? 0.1535 0.1288 0.1743 -0.0239 -0.0161 0.0017  84  SER   B N   
5088 C CA  . SER   B 84  ? 0.1548 0.1474 0.1685 -0.0247 -0.0116 0.0134  84  SER   B CA  
5089 C C   . SER   B 84  ? 0.1427 0.1644 0.1354 -0.0198 -0.0165 0.0210  84  SER   B C   
5090 O O   . SER   B 84  ? 0.1517 0.1500 0.1420 -0.0189 -0.0168 0.0013  84  SER   B O   
5091 C CB  . SER   B 84  ? 0.1726 0.1524 0.2181 -0.0295 0.0086  0.0121  84  SER   B CB  
5092 O OG  . SER   B 84  ? 0.1760 0.1652 0.2794 -0.0318 0.0148  0.0182  84  SER   B OG  
5098 N N   . GLY   B 85  ? 0.1490 0.1867 0.1457 -0.0246 -0.0160 0.0165  85  GLY   B N   
5099 C CA  . GLY   B 85  ? 0.1540 0.1945 0.1595 -0.0390 -0.0059 -0.0041 85  GLY   B CA  
5100 C C   . GLY   B 85  ? 0.1497 0.1759 0.1544 -0.0396 -0.0055 0.0090  85  GLY   B C   
5101 O O   . GLY   B 85  ? 0.1586 0.1785 0.1661 -0.0575 0.0086  -0.0073 85  GLY   B O   
5105 N N   . HIS   B 86  ? 0.1490 0.1552 0.1632 -0.0309 -0.0225 0.0217  86  HIS   B N   
5106 C CA  . HIS   B 86  ? 0.1482 0.1545 0.1746 -0.0303 -0.0199 0.0227  86  HIS   B CA  
5107 C C   . HIS   B 86  ? 0.1501 0.1669 0.1651 -0.0419 -0.0167 0.0363  86  HIS   B C   
5108 O O   . HIS   B 86  ? 0.1635 0.1769 0.1679 -0.0306 -0.0045 0.0387  86  HIS   B O   
5109 C CB  . HIS   B 86  ? 0.1568 0.1585 0.1705 -0.0189 -0.0234 0.0107  86  HIS   B CB  
5110 C CG  . HIS   B 86  ? 0.1621 0.1690 0.1625 -0.0072 -0.0284 0.0088  86  HIS   B CG  
5111 N ND1 . HIS   B 86  ? 0.1773 0.1910 0.1877 -0.0209 -0.0320 -0.0072 86  HIS   B ND1 
5112 C CD2 . HIS   B 86  ? 0.1651 0.1772 0.1681 -0.0058 -0.0226 0.0098  86  HIS   B CD2 
5113 C CE1 . HIS   B 86  ? 0.1826 0.1884 0.1776 -0.0159 -0.0214 -0.0206 86  HIS   B CE1 
5114 N NE2 . HIS   B 86  ? 0.1727 0.1830 0.1616 0.0000  -0.0194 0.0009  86  HIS   B NE2 
5122 N N   . ASN   B 87  ? 0.1505 0.1719 0.1653 -0.0346 -0.0119 0.0282  87  ASN   B N   
5123 C CA  . ASN   B 87  ? 0.1558 0.1925 0.1721 -0.0322 0.0117  0.0218  87  ASN   B CA  
5124 C C   . ASN   B 87  ? 0.1679 0.1748 0.1580 -0.0269 0.0191  0.0165  87  ASN   B C   
5125 O O   . ASN   B 87  ? 0.1913 0.1825 0.1852 -0.0245 0.0394  0.0124  87  ASN   B O   
5126 C CB  . ASN   B 87  ? 0.1572 0.2257 0.2017 -0.0312 0.0156  0.0093  87  ASN   B CB  
5127 C CG  . ASN   B 87  ? 0.1656 0.2464 0.2115 0.0029  0.0271  0.0288  87  ASN   B CG  
5128 O OD1 . ASN   B 87  ? 0.1599 0.2286 0.1977 0.0084  0.0379  0.0491  87  ASN   B OD1 
5129 N ND2 . ASN   B 87  ? 0.2000 0.2607 0.2443 0.0066  0.0253  0.0271  87  ASN   B ND2 
5136 N N   . LEU   B 88  ? 0.1575 0.1638 0.1459 -0.0299 0.0108  0.0121  88  LEU   B N   
5137 C CA  . LEU   B 88  ? 0.1626 0.1574 0.1466 -0.0313 -0.0011 0.0011  88  LEU   B CA  
5138 C C   . LEU   B 88  ? 0.1664 0.1478 0.1455 -0.0316 -0.0037 0.0061  88  LEU   B C   
5139 O O   . LEU   B 88  ? 0.1963 0.1554 0.1776 -0.0202 -0.0308 -0.0046 88  LEU   B O   
5140 C CB  . LEU   B 88  ? 0.1761 0.1646 0.1680 -0.0364 -0.0110 0.0158  88  LEU   B CB  
5141 C CG  . LEU   B 88  ? 0.2135 0.1975 0.1877 -0.0346 -0.0265 0.0320  88  LEU   B CG  
5142 C CD1 . LEU   B 88  ? 0.2288 0.2297 0.2114 -0.0416 -0.0190 0.0416  88  LEU   B CD1 
5143 C CD2 . LEU   B 88  ? 0.2481 0.2257 0.2375 0.0055  -0.0560 0.0126  88  LEU   B CD2 
5155 N N   . ALA   B 89  ? 0.1563 0.1422 0.1439 -0.0337 0.0093  0.0082  89  ALA   B N   
5156 C CA  . ALA   B 89  ? 0.1571 0.1430 0.1300 -0.0309 -0.0042 0.0107  89  ALA   B CA  
5157 C C   . ALA   B 89  ? 0.1620 0.1465 0.1336 -0.0354 0.0102  0.0082  89  ALA   B C   
5158 O O   . ALA   B 89  ? 0.1503 0.1594 0.1687 -0.0375 0.0090  -0.0241 89  ALA   B O   
5159 C CB  . ALA   B 89  ? 0.1455 0.1433 0.1433 -0.0331 -0.0003 0.0161  89  ALA   B CB  
5165 N N   . LYS   B 90  ? 0.1964 0.1330 0.1457 -0.0362 -0.0046 0.0115  90  LYS   B N   
5166 C CA  . LYS   B 90  ? 0.2126 0.1289 0.1469 -0.0382 -0.0080 0.0089  90  LYS   B CA  
5167 C C   . LYS   B 90  ? 0.2035 0.1192 0.1682 -0.0417 -0.0081 -0.0030 90  LYS   B C   
5168 O O   . LYS   B 90  ? 0.2168 0.1484 0.1785 -0.0676 0.0001  0.0003  90  LYS   B O   
5169 C CB  . LYS   B 90  ? 0.2360 0.1373 0.1797 -0.0291 0.0014  0.0213  90  LYS   B CB  
5170 C CG  . LYS   B 90  ? 0.2454 0.1528 0.1820 -0.0181 0.0279  0.0213  90  LYS   B CG  
5171 C CD  . LYS   B 90  ? 0.2791 0.1798 0.2238 -0.0179 0.0537  -0.0022 90  LYS   B CD  
5172 C CE  . LYS   B 90  ? 0.2908 0.2005 0.2801 -0.0260 0.0620  -0.0112 90  LYS   B CE  
5173 N NZ  . LYS   B 90  ? 0.3001 0.1952 0.2856 -0.0371 0.0755  -0.0089 90  LYS   B NZ  
5187 N N   . HIS   B 91  ? 0.1697 0.1131 0.1419 -0.0271 -0.0173 0.0020  91  HIS   B N   
5188 C CA  . HIS   B 91  ? 0.1586 0.1197 0.1550 -0.0218 -0.0147 0.0019  91  HIS   B CA  
5189 C C   . HIS   B 91  ? 0.1452 0.1193 0.1319 -0.0255 -0.0154 -0.0018 91  HIS   B C   
5190 O O   . HIS   B 91  ? 0.1595 0.1286 0.1337 -0.0262 -0.0247 0.0078  91  HIS   B O   
5191 C CB  . HIS   B 91  ? 0.1771 0.1234 0.2002 -0.0051 -0.0066 0.0097  91  HIS   B CB  
5192 C CG  . HIS   B 91  ? 0.2220 0.1390 0.2725 0.0071  0.0220  0.0261  91  HIS   B CG  
5193 N ND1 . HIS   B 91  ? 0.2561 0.1491 0.3289 0.0055  0.0270  0.0146  91  HIS   B ND1 
5194 C CD2 . HIS   B 91  ? 0.2402 0.1739 0.3181 0.0225  0.0110  0.0576  91  HIS   B CD2 
5195 C CE1 . HIS   B 91  ? 0.2619 0.1636 0.3409 0.0212  0.0236  0.0283  91  HIS   B CE1 
5196 N NE2 . HIS   B 91  ? 0.2507 0.1795 0.3432 0.0342  0.0199  0.0662  91  HIS   B NE2 
5204 N N   . CYS   B 92  ? 0.1416 0.1200 0.1362 -0.0243 -0.0235 -0.0014 92  CYS   B N   
5205 C CA  . CYS   B 92  ? 0.1377 0.1139 0.1325 -0.0220 -0.0126 0.0013  92  CYS   B CA  
5206 C C   . CYS   B 92  ? 0.1374 0.1047 0.1312 -0.0109 -0.0119 0.0062  92  CYS   B C   
5207 O O   . CYS   B 92  ? 0.1411 0.1137 0.1557 -0.0138 -0.0092 0.0017  92  CYS   B O   
5208 C CB  . CYS   B 92  ? 0.1377 0.1282 0.1385 -0.0155 -0.0113 0.0015  92  CYS   B CB  
5209 S SG  . CYS   B 92  ? 0.1424 0.1310 0.1393 -0.0098 -0.0157 0.0071  92  CYS   B SG  
5215 N N   . LEU   B 93  ? 0.1268 0.1133 0.1316 -0.0097 -0.0142 -0.0009 93  LEU   B N   
5216 C CA  . LEU   B 93  ? 0.1294 0.1153 0.1349 -0.0030 -0.0090 0.0026  93  LEU   B CA  
5217 C C   . LEU   B 93  ? 0.1250 0.1103 0.1239 0.0001  -0.0111 0.0025  93  LEU   B C   
5218 O O   . LEU   B 93  ? 0.1301 0.1109 0.1465 -0.0049 -0.0085 0.0007  93  LEU   B O   
5219 C CB  . LEU   B 93  ? 0.1282 0.1199 0.1448 -0.0043 -0.0127 0.0017  93  LEU   B CB  
5220 C CG  . LEU   B 93  ? 0.1302 0.1322 0.1533 -0.0015 -0.0107 0.0130  93  LEU   B CG  
5221 C CD1 . LEU   B 93  ? 0.1375 0.1405 0.1587 0.0070  -0.0096 -0.0025 93  LEU   B CD1 
5222 C CD2 . LEU   B 93  ? 0.1290 0.1383 0.1676 -0.0023 -0.0089 0.0047  93  LEU   B CD2 
5234 N N   . HIS   B 94  ? 0.1273 0.1129 0.1225 -0.0052 -0.0141 0.0057  94  HIS   B N   
5235 C CA  . HIS   B 94  ? 0.1280 0.1094 0.1284 -0.0030 -0.0108 0.0041  94  HIS   B CA  
5236 C C   . HIS   B 94  ? 0.1264 0.1088 0.1549 -0.0040 -0.0100 0.0040  94  HIS   B C   
5237 O O   . HIS   B 94  ? 0.1322 0.1247 0.1872 -0.0051 0.0092  -0.0093 94  HIS   B O   
5238 C CB  . HIS   B 94  ? 0.1299 0.1215 0.1390 -0.0031 -0.0121 0.0035  94  HIS   B CB  
5239 C CG  . HIS   B 94  ? 0.1342 0.1164 0.1442 -0.0059 -0.0290 0.0062  94  HIS   B CG  
5240 N ND1 . HIS   B 94  ? 0.1384 0.1254 0.1406 -0.0069 -0.0268 0.0001  94  HIS   B ND1 
5241 C CD2 . HIS   B 94  ? 0.1397 0.1146 0.1456 -0.0040 -0.0239 0.0065  94  HIS   B CD2 
5242 C CE1 . HIS   B 94  ? 0.1356 0.1238 0.1480 -0.0141 -0.0255 -0.0007 94  HIS   B CE1 
5243 N NE2 . HIS   B 94  ? 0.1320 0.1216 0.1493 -0.0157 -0.0192 0.0078  94  HIS   B NE2 
5251 N N   . VAL   B 95  ? 0.1234 0.1106 0.1485 0.0007  -0.0031 0.0013  95  VAL   B N   
5252 C CA  . VAL   B 95  ? 0.1240 0.1151 0.1470 0.0011  -0.0044 0.0110  95  VAL   B CA  
5253 C C   . VAL   B 95  ? 0.1293 0.1161 0.1451 -0.0018 0.0018  0.0008  95  VAL   B C   
5254 O O   . VAL   B 95  ? 0.1376 0.1181 0.1604 0.0024  0.0033  0.0149  95  VAL   B O   
5255 C CB  . VAL   B 95  ? 0.1312 0.1163 0.1485 -0.0032 -0.0133 0.0021  95  VAL   B CB  
5256 C CG1 . VAL   B 95  ? 0.1396 0.1374 0.1684 -0.0135 -0.0071 0.0140  95  VAL   B CG1 
5257 C CG2 . VAL   B 95  ? 0.1418 0.1207 0.1593 0.0036  -0.0131 0.0023  95  VAL   B CG2 
5267 N N   . VAL   B 96  ? 0.1363 0.1252 0.1413 0.0075  -0.0022 0.0101  96  VAL   B N   
5268 C CA  . VAL   B 96  ? 0.1437 0.1390 0.1438 0.0061  -0.0056 0.0156  96  VAL   B CA  
5269 C C   . VAL   B 96  ? 0.1429 0.1422 0.1443 0.0067  0.0039  0.0135  96  VAL   B C   
5270 O O   . VAL   B 96  ? 0.1448 0.1443 0.1618 0.0051  0.0129  0.0042  96  VAL   B O   
5271 C CB  . VAL   B 96  ? 0.1495 0.1526 0.1435 0.0050  -0.0041 0.0046  96  VAL   B CB  
5272 C CG1 . VAL   B 96  ? 0.1511 0.1697 0.1527 0.0097  0.0030  0.0021  96  VAL   B CG1 
5273 C CG2 . VAL   B 96  ? 0.1653 0.1656 0.1595 0.0017  0.0021  0.0005  96  VAL   B CG2 
5283 N N   . GLY   B 97  ? 0.1481 0.1412 0.1472 0.0027  0.0019  0.0178  97  GLY   B N   
5284 C CA  . GLY   B 97  ? 0.1570 0.1377 0.1479 -0.0062 0.0124  0.0140  97  GLY   B CA  
5285 C C   . GLY   B 97  ? 0.1693 0.1471 0.1609 0.0040  0.0001  0.0125  97  GLY   B C   
5286 O O   . GLY   B 97  ? 0.1793 0.1579 0.1554 0.0024  0.0023  0.0143  97  GLY   B O   
5290 N N   . PRO   B 98  ? 0.1813 0.1526 0.1573 0.0030  0.0171  0.0225  98  PRO   B N   
5291 C CA  . PRO   B 98  ? 0.1929 0.1667 0.1642 0.0075  0.0256  0.0156  98  PRO   B CA  
5292 C C   . PRO   B 98  ? 0.2011 0.1683 0.1359 0.0163  0.0225  0.0326  98  PRO   B C   
5293 O O   . PRO   B 98  ? 0.1922 0.1628 0.1573 0.0173  0.0206  0.0295  98  PRO   B O   
5294 C CB  . PRO   B 98  ? 0.1828 0.1675 0.1814 0.0037  0.0327  0.0203  98  PRO   B CB  
5295 C CG  . PRO   B 98  ? 0.1777 0.1618 0.1811 -0.0001 0.0246  0.0268  98  PRO   B CG  
5296 C CD  . PRO   B 98  ? 0.1607 0.1539 0.1770 0.0076  0.0214  0.0258  98  PRO   B CD  
5304 N N   . ASN   B 99  ? 0.2114 0.1781 0.1479 0.0274  0.0205  0.0178  99  ASN   B N   
5305 C CA  . ASN   B 99  ? 0.2243 0.1812 0.1518 0.0352  0.0168  0.0324  99  ASN   B CA  
5306 C C   . ASN   B 99  ? 0.2472 0.2117 0.1680 0.0296  0.0289  0.0527  99  ASN   B C   
5307 O O   . ASN   B 99  ? 0.2598 0.2175 0.1793 0.0278  0.0213  0.0536  99  ASN   B O   
5308 C CB  . ASN   B 99  ? 0.2342 0.1774 0.1631 0.0335  0.0059  0.0344  99  ASN   B CB  
5309 C CG  . ASN   B 99  ? 0.2347 0.1859 0.1844 0.0292  -0.0059 0.0354  99  ASN   B CG  
5310 O OD1 . ASN   B 99  ? 0.2434 0.1908 0.2181 0.0313  -0.0100 0.0408  99  ASN   B OD1 
5311 N ND2 . ASN   B 99  ? 0.2307 0.1877 0.2057 0.0345  -0.0254 0.0259  99  ASN   B ND2 
5318 N N   A VAL   B 100 ? 0.2635 0.2240 0.2062 0.0165  0.0275  0.0636  100 VAL   B N   
5319 N N   B VAL   B 100 ? 0.2716 0.2272 0.2029 0.0231  0.0260  0.0647  100 VAL   B N   
5320 C CA  A VAL   B 100 ? 0.2987 0.2413 0.2667 0.0074  0.0365  0.0770  100 VAL   B CA  
5321 C CA  B VAL   B 100 ? 0.3007 0.2428 0.2466 0.0184  0.0239  0.0745  100 VAL   B CA  
5322 C C   A VAL   B 100 ? 0.3213 0.2442 0.2568 0.0185  0.0379  0.0954  100 VAL   B C   
5323 C C   B VAL   B 100 ? 0.3217 0.2480 0.2483 0.0245  0.0251  0.0915  100 VAL   B C   
5324 O O   A VAL   B 100 ? 0.3301 0.2509 0.2702 0.0116  0.0524  0.0896  100 VAL   B O   
5325 O O   B VAL   B 100 ? 0.3262 0.2523 0.2499 0.0216  0.0283  0.0904  100 VAL   B O   
5326 C CB  A VAL   B 100 ? 0.3142 0.2615 0.3395 -0.0128 0.0351  0.0817  100 VAL   B CB  
5327 C CB  B VAL   B 100 ? 0.3091 0.2538 0.2873 0.0077  0.0190  0.0706  100 VAL   B CB  
5328 C CG1 A VAL   B 100 ? 0.3215 0.2694 0.3697 -0.0150 0.0379  0.0811  100 VAL   B CG1 
5329 C CG1 B VAL   B 100 ? 0.3128 0.2577 0.3038 0.0056  0.0180  0.0689  100 VAL   B CG1 
5330 C CG2 A VAL   B 100 ? 0.3182 0.2685 0.3614 -0.0195 0.0377  0.0873  100 VAL   B CG2 
5331 C CG2 B VAL   B 100 ? 0.3115 0.2575 0.3008 0.0040  0.0186  0.0701  100 VAL   B CG2 
5350 N N   . ASN   B 101 ? 0.3377 0.2508 0.2521 0.0322  0.0231  0.1033  101 ASN   B N   
5351 C CA  . ASN   B 101 ? 0.3801 0.2758 0.2780 0.0437  0.0057  0.1195  101 ASN   B CA  
5352 C C   . ASN   B 101 ? 0.4236 0.3203 0.2766 0.0477  -0.0102 0.1300  101 ASN   B C   
5353 O O   . ASN   B 101 ? 0.4295 0.3348 0.2953 0.0542  -0.0205 0.1106  101 ASN   B O   
5354 C CB  . ASN   B 101 ? 0.3801 0.2652 0.2957 0.0424  0.0127  0.1117  101 ASN   B CB  
5355 C CG  . ASN   B 101 ? 0.3796 0.2524 0.2944 0.0412  0.0230  0.1182  101 ASN   B CG  
5356 O OD1 . ASN   B 101 ? 0.3863 0.2535 0.3271 0.0311  0.0433  0.1066  101 ASN   B OD1 
5357 N ND2 . ASN   B 101 ? 0.3764 0.2571 0.2929 0.0423  0.0219  0.1012  101 ASN   B ND2 
5365 N N   A LYS   B 102 ? 0.4531 0.3424 0.2858 0.0429  -0.0004 0.1326  102 LYS   B N   
5366 N N   B LYS   B 102 ? 0.4298 0.3404 0.3098 0.0396  -0.0043 0.1053  102 LYS   B N   
5367 C CA  A LYS   B 102 ? 0.4826 0.3760 0.3062 0.0303  0.0189  0.1124  102 LYS   B CA  
5368 C CA  B LYS   B 102 ? 0.4346 0.3620 0.3441 0.0295  0.0044  0.0745  102 LYS   B CA  
5369 C C   A LYS   B 102 ? 0.4846 0.3805 0.2823 0.0331  0.0317  0.1206  102 LYS   B C   
5370 C C   B LYS   B 102 ? 0.4264 0.3614 0.3361 0.0264  0.0092  0.0646  102 LYS   B C   
5371 O O   A LYS   B 102 ? 0.4949 0.3899 0.3005 0.0361  0.0217  0.1085  102 LYS   B O   
5372 O O   B LYS   B 102 ? 0.4298 0.3647 0.3374 0.0264  0.0086  0.0621  102 LYS   B O   
5373 C CB  A LYS   B 102 ? 0.5074 0.4039 0.3766 0.0156  0.0324  0.0712  102 LYS   B CB  
5374 C CB  B LYS   B 102 ? 0.4461 0.3821 0.3914 0.0230  0.0095  0.0509  102 LYS   B CB  
5375 C CG  A LYS   B 102 ? 0.5275 0.4288 0.4506 0.0048  0.0455  0.0313  102 LYS   B CG  
5376 C CG  B LYS   B 102 ? 0.4558 0.3991 0.4357 0.0183  0.0141  0.0296  102 LYS   B CG  
5377 C CD  A LYS   B 102 ? 0.5432 0.4485 0.5251 -0.0027 0.0580  -0.0012 102 LYS   B CD  
5378 C CD  B LYS   B 102 ? 0.4635 0.4118 0.4777 0.0152  0.0181  0.0128  102 LYS   B CD  
5379 C CE  A LYS   B 102 ? 0.5554 0.4619 0.5830 -0.0087 0.0670  -0.0251 102 LYS   B CE  
5380 C CE  B LYS   B 102 ? 0.4692 0.4206 0.5091 0.0129  0.0212  0.0005  102 LYS   B CE  
5381 N NZ  A LYS   B 102 ? 0.5629 0.4696 0.6160 -0.0119 0.0704  -0.0386 102 LYS   B NZ  
5382 N NZ  B LYS   B 102 ? 0.4725 0.4256 0.5260 0.0119  0.0225  -0.0062 102 LYS   B NZ  
5409 N N   A GLY   B 103 ? 0.4728 0.3734 0.2616 0.0325  0.0585  0.1315  103 GLY   B N   
5410 N N   B GLY   B 103 ? 0.4133 0.3555 0.3303 0.0234  0.0148  0.0570  103 GLY   B N   
5411 C CA  A GLY   B 103 ? 0.4603 0.3679 0.2680 0.0336  0.0850  0.1194  103 GLY   B CA  
5412 C CA  B GLY   B 103 ? 0.4005 0.3488 0.3279 0.0201  0.0198  0.0455  103 GLY   B CA  
5413 C C   A GLY   B 103 ? 0.4416 0.3560 0.2586 0.0313  0.1115  0.1029  103 GLY   B C   
5414 C C   B GLY   B 103 ? 0.3858 0.3396 0.3204 0.0155  0.0240  0.0331  103 GLY   B C   
5415 O O   A GLY   B 103 ? 0.4472 0.3655 0.2746 0.0296  0.1137  0.0976  103 GLY   B O   
5416 O O   B GLY   B 103 ? 0.3870 0.3417 0.3265 0.0165  0.0253  0.0320  103 GLY   B O   
5423 N N   A GLU   B 104 ? 0.4142 0.3319 0.2394 0.0328  0.1241  0.0805  104 GLU   B N   
5424 N N   B GLU   B 104 ? 0.3689 0.3264 0.3031 0.0092  0.0237  0.0207  104 GLU   B N   
5425 C CA  A GLU   B 104 ? 0.3870 0.3136 0.2212 0.0352  0.1261  0.0520  104 GLU   B CA  
5426 C CA  B GLU   B 104 ? 0.3530 0.3148 0.2867 0.0020  0.0220  0.0100  104 GLU   B CA  
5427 C C   A GLU   B 104 ? 0.3954 0.3168 0.2415 0.0234  0.1454  0.0374  104 GLU   B C   
5428 C C   B GLU   B 104 ? 0.3507 0.3152 0.2899 -0.0026 0.0302  0.0046  104 GLU   B C   
5429 O O   A GLU   B 104 ? 0.4019 0.3214 0.2734 0.0214  0.1380  0.0209  104 GLU   B O   
5430 O O   B GLU   B 104 ? 0.3519 0.3162 0.2909 -0.0032 0.0302  0.0006  104 GLU   B O   
5431 C CB  A GLU   B 104 ? 0.3580 0.2918 0.2158 0.0471  0.0926  0.0302  104 GLU   B CB  
5432 C CB  B GLU   B 104 ? 0.3420 0.3033 0.2721 -0.0021 0.0121  0.0040  104 GLU   B CB  
5433 C CG  A GLU   B 104 ? 0.3342 0.2781 0.2122 0.0550  0.0488  0.0016  104 GLU   B CG  
5434 C CG  B GLU   B 104 ? 0.3341 0.2947 0.2595 -0.0067 0.0019  -0.0026 104 GLU   B CG  
5435 C CD  A GLU   B 104 ? 0.3117 0.2620 0.2026 0.0596  0.0116  -0.0082 104 GLU   B CD  
5436 C CD  B GLU   B 104 ? 0.3283 0.2871 0.2500 -0.0120 -0.0055 -0.0045 104 GLU   B CD  
5437 O OE1 A GLU   B 104 ? 0.2857 0.2424 0.1752 0.0633  0.0154  0.0003  104 GLU   B OE1 
5438 O OE1 B GLU   B 104 ? 0.3243 0.2821 0.2451 -0.0155 -0.0036 -0.0023 104 GLU   B OE1 
5439 O OE2 A GLU   B 104 ? 0.3179 0.2756 0.2234 0.0536  -0.0227 -0.0183 104 GLU   B OE2 
5440 O OE2 B GLU   B 104 ? 0.3281 0.2877 0.2503 -0.0138 -0.0134 -0.0071 104 GLU   B OE2 
5453 N N   A ASP   B 105 ? 0.3943 0.3194 0.2453 0.0071  0.1624  0.0458  105 ASP   B N   
5454 N N   B ASP   B 105 ? 0.3477 0.3162 0.2942 -0.0077 0.0373  0.0052  105 ASP   B N   
5455 C CA  A ASP   B 105 ? 0.3958 0.3203 0.2684 -0.0068 0.1832  0.0345  105 ASP   B CA  
5456 C CA  B ASP   B 105 ? 0.3464 0.3173 0.3057 -0.0121 0.0431  0.0027  105 ASP   B CA  
5457 C C   A ASP   B 105 ? 0.3767 0.2834 0.2533 -0.0211 0.1699  0.0207  105 ASP   B C   
5458 C C   B ASP   B 105 ? 0.3402 0.3105 0.2887 -0.0138 0.0419  -0.0005 105 ASP   B C   
5459 O O   A ASP   B 105 ? 0.3655 0.2738 0.2483 -0.0240 0.1666  0.0192  105 ASP   B O   
5460 O O   B ASP   B 105 ? 0.3377 0.3077 0.2778 -0.0155 0.0408  -0.0018 105 ASP   B O   
5461 C CB  A ASP   B 105 ? 0.4139 0.3545 0.3433 0.0016  0.1976  0.0146  105 ASP   B CB  
5462 C CB  B ASP   B 105 ? 0.3497 0.3240 0.3354 -0.0129 0.0506  0.0016  105 ASP   B CB  
5463 C CG  A ASP   B 105 ? 0.4286 0.3807 0.4131 0.0059  0.2162  0.0023  105 ASP   B CG  
5464 C CG  B ASP   B 105 ? 0.3530 0.3284 0.3651 -0.0149 0.0577  0.0029  105 ASP   B CG  
5465 O OD1 A ASP   B 105 ? 0.4312 0.3883 0.4180 -0.0026 0.2290  0.0140  105 ASP   B OD1 
5466 O OD1 B ASP   B 105 ? 0.3540 0.3306 0.3711 -0.0182 0.0600  0.0059  105 ASP   B OD1 
5467 O OD2 A ASP   B 105 ? 0.4375 0.3932 0.4580 0.0140  0.2070  -0.0133 105 ASP   B OD2 
5468 O OD2 B ASP   B 105 ? 0.3533 0.3296 0.3740 -0.0154 0.0609  0.0034  105 ASP   B OD2 
5477 N N   A ILE   B 106 ? 0.3636 0.2535 0.2700 -0.0281 0.1502  0.0141  106 ILE   B N   
5478 N N   B ILE   B 106 ? 0.3354 0.3062 0.2825 -0.0123 0.0391  -0.0017 106 ILE   B N   
5479 C CA  A ILE   B 106 ? 0.3388 0.2220 0.2840 -0.0446 0.1468  0.0091  106 ILE   B CA  
5480 C CA  B ILE   B 106 ? 0.3274 0.3017 0.2810 -0.0118 0.0391  -0.0026 106 ILE   B CA  
5481 C C   A ILE   B 106 ? 0.3004 0.2215 0.2750 -0.0409 0.1350  -0.0151 106 ILE   B C   
5482 C C   B ILE   B 106 ? 0.3138 0.3015 0.2797 -0.0100 0.0376  -0.0074 106 ILE   B C   
5483 O O   A ILE   B 106 ? 0.2877 0.1937 0.2710 -0.0431 0.1147  -0.0257 106 ILE   B O   
5484 O O   B ILE   B 106 ? 0.3123 0.2992 0.2732 -0.0112 0.0322  -0.0087 106 ILE   B O   
5485 C CB  A ILE   B 106 ? 0.3605 0.2109 0.3194 -0.0511 0.1411  0.0188  106 ILE   B CB  
5486 C CB  B ILE   B 106 ? 0.3335 0.2997 0.2853 -0.0120 0.0406  0.0002  106 ILE   B CB  
5487 C CG1 A ILE   B 106 ? 0.3681 0.2089 0.3311 -0.0381 0.1331  0.0161  106 ILE   B CG1 
5488 C CG1 B ILE   B 106 ? 0.3339 0.2975 0.2867 -0.0096 0.0397  0.0015  106 ILE   B CG1 
5489 C CG2 A ILE   B 106 ? 0.3708 0.2170 0.3465 -0.0602 0.1431  0.0266  106 ILE   B CG2 
5490 C CG2 B ILE   B 106 ? 0.3378 0.3024 0.2926 -0.0132 0.0422  0.0013  106 ILE   B CG2 
5491 C CD1 A ILE   B 106 ? 0.3720 0.2125 0.3296 -0.0253 0.1306  0.0172  106 ILE   B CD1 
5492 C CD1 B ILE   B 106 ? 0.3341 0.2971 0.2857 -0.0072 0.0395  0.0029  106 ILE   B CD1 
5515 N N   A GLN   B 107 ? 0.2867 0.2570 0.2948 -0.0355 0.1243  -0.0199 107 GLN   B N   
5516 N N   B GLN   B 107 ? 0.3028 0.3037 0.2916 -0.0085 0.0390  -0.0102 107 GLN   B N   
5517 C CA  A GLN   B 107 ? 0.2703 0.2873 0.3137 -0.0331 0.1147  -0.0100 107 GLN   B CA  
5518 C CA  B GLN   B 107 ? 0.2912 0.3031 0.3048 -0.0066 0.0411  -0.0096 107 GLN   B CA  
5519 C C   A GLN   B 107 ? 0.2404 0.2672 0.2835 -0.0207 0.0769  -0.0155 107 GLN   B C   
5520 C C   B GLN   B 107 ? 0.2574 0.2778 0.2695 -0.0044 0.0461  -0.0149 107 GLN   B C   
5521 O O   A GLN   B 107 ? 0.2346 0.2666 0.3238 -0.0117 0.0528  -0.0247 107 GLN   B O   
5522 O O   B GLN   B 107 ? 0.2585 0.2813 0.2762 -0.0031 0.0400  -0.0199 107 GLN   B O   
5523 C CB  A GLN   B 107 ? 0.3038 0.3391 0.3948 -0.0314 0.1042  0.0003  107 GLN   B CB  
5524 C CB  B GLN   B 107 ? 0.3141 0.3265 0.3624 -0.0056 0.0343  -0.0047 107 GLN   B CB  
5525 C CG  A GLN   B 107 ? 0.3423 0.3896 0.4837 -0.0227 0.0700  0.0061  107 GLN   B CG  
5526 C CG  B GLN   B 107 ? 0.3350 0.3466 0.4181 -0.0034 0.0242  0.0001  107 GLN   B CG  
5527 C CD  A GLN   B 107 ? 0.3711 0.4302 0.5566 -0.0198 0.0458  0.0131  107 GLN   B CD  
5528 C CD  B GLN   B 107 ? 0.3510 0.3619 0.4644 -0.0029 0.0168  0.0045  107 GLN   B CD  
5529 O OE1 A GLN   B 107 ? 0.3800 0.4417 0.5846 -0.0184 0.0428  0.0127  107 GLN   B OE1 
5530 O OE1 B GLN   B 107 ? 0.3566 0.3674 0.4811 -0.0029 0.0164  0.0049  107 GLN   B OE1 
5531 N NE2 A GLN   B 107 ? 0.3817 0.4392 0.5805 -0.0150 0.0349  0.0202  107 GLN   B NE2 
5532 N NE2 B GLN   B 107 ? 0.3571 0.3671 0.4804 -0.0012 0.0139  0.0077  107 GLN   B NE2 
5549 N N   . LEU   B 108 ? 0.2213 0.2464 0.2399 0.0004  0.0564  -0.0158 108 LEU   B N   
5550 C CA  . LEU   B 108 ? 0.2070 0.2143 0.2091 0.0180  0.0342  -0.0014 108 LEU   B CA  
5551 C C   . LEU   B 108 ? 0.1823 0.1729 0.2065 0.0214  0.0183  0.0231  108 LEU   B C   
5552 O O   . LEU   B 108 ? 0.1883 0.1640 0.2050 0.0206  0.0097  0.0155  108 LEU   B O   
5553 C CB  . LEU   B 108 ? 0.2215 0.2305 0.1985 0.0141  0.0315  -0.0014 108 LEU   B CB  
5554 C CG  . LEU   B 108 ? 0.2398 0.2594 0.2024 0.0150  0.0274  -0.0215 108 LEU   B CG  
5555 C CD1 . LEU   B 108 ? 0.2477 0.2779 0.1924 0.0042  0.0329  -0.0208 108 LEU   B CD1 
5556 C CD2 . LEU   B 108 ? 0.2599 0.2728 0.2235 0.0251  0.0172  -0.0288 108 LEU   B CD2 
5569 N N   . LEU   B 109 ? 0.1706 0.1566 0.2035 0.0131  0.0224  0.0199  109 LEU   B N   
5570 C CA  . LEU   B 109 ? 0.1569 0.1364 0.2129 0.0100  0.0134  0.0230  109 LEU   B CA  
5571 C C   . LEU   B 109 ? 0.1445 0.1264 0.2058 0.0027  0.0154  0.0151  109 LEU   B C   
5572 O O   . LEU   B 109 ? 0.1422 0.1251 0.2013 0.0061  0.0178  0.0290  109 LEU   B O   
5573 C CB  . LEU   B 109 ? 0.1605 0.1297 0.2187 0.0082  0.0124  0.0335  109 LEU   B CB  
5574 C CG  . LEU   B 109 ? 0.1596 0.1337 0.2085 0.0028  0.0065  0.0190  109 LEU   B CG  
5575 C CD1 . LEU   B 109 ? 0.1556 0.1455 0.2065 0.0155  0.0126  0.0178  109 LEU   B CD1 
5576 C CD2 . LEU   B 109 ? 0.1680 0.1378 0.2120 0.0027  0.0033  0.0111  109 LEU   B CD2 
5588 N N   . LYS   B 110 ? 0.1417 0.1245 0.2038 0.0004  0.0249  0.0207  110 LYS   B N   
5589 C CA  . LYS   B 110 ? 0.1423 0.1204 0.2041 -0.0022 0.0139  0.0163  110 LYS   B CA  
5590 C C   . LYS   B 110 ? 0.1390 0.1254 0.1887 0.0013  0.0126  0.0108  110 LYS   B C   
5591 O O   . LYS   B 110 ? 0.1332 0.1271 0.1829 -0.0056 0.0093  0.0082  110 LYS   B O   
5592 C CB  . LYS   B 110 ? 0.1374 0.1246 0.2312 -0.0026 0.0198  0.0052  110 LYS   B CB  
5593 C CG  . LYS   B 110 ? 0.1406 0.1261 0.2477 -0.0050 0.0086  0.0095  110 LYS   B CG  
5594 C CD  . LYS   B 110 ? 0.1402 0.1302 0.2570 -0.0035 0.0040  0.0082  110 LYS   B CD  
5595 C CE  . LYS   B 110 ? 0.1374 0.1462 0.2683 0.0005  0.0095  0.0030  110 LYS   B CE  
5596 N NZ  . LYS   B 110 ? 0.1416 0.1578 0.2599 0.0030  -0.0030 -0.0033 110 LYS   B NZ  
5610 N N   . SER   B 111 ? 0.1427 0.1268 0.2015 -0.0026 0.0188  0.0076  111 SER   B N   
5611 C CA  . SER   B 111 ? 0.1477 0.1308 0.1883 0.0024  0.0059  0.0117  111 SER   B CA  
5612 C C   . SER   B 111 ? 0.1430 0.1235 0.1754 0.0003  0.0004  0.0038  111 SER   B C   
5613 O O   . SER   B 111 ? 0.1425 0.1262 0.1865 -0.0031 0.0009  0.0087  111 SER   B O   
5614 C CB  . SER   B 111 ? 0.1585 0.1536 0.1922 0.0037  0.0190  0.0255  111 SER   B CB  
5615 O OG  . SER   B 111 ? 0.1801 0.1978 0.2123 0.0061  0.0314  0.0190  111 SER   B OG  
5621 N N   . ALA   B 112 ? 0.1309 0.1259 0.1858 0.0054  0.0077  0.0147  112 ALA   B N   
5622 C CA  . ALA   B 112 ? 0.1298 0.1279 0.1739 -0.0004 0.0008  0.0048  112 ALA   B CA  
5623 C C   . ALA   B 112 ? 0.1216 0.1186 0.1654 0.0017  0.0029  -0.0008 112 ALA   B C   
5624 O O   . ALA   B 112 ? 0.1280 0.1219 0.1843 -0.0059 -0.0022 -0.0033 112 ALA   B O   
5625 C CB  . ALA   B 112 ? 0.1372 0.1377 0.1887 0.0067  -0.0003 0.0108  112 ALA   B CB  
5631 N N   . TYR   B 113 ? 0.1207 0.1116 0.1814 -0.0049 0.0030  0.0041  113 TYR   B N   
5632 C CA  . TYR   B 113 ? 0.1206 0.1083 0.1704 -0.0035 0.0029  0.0025  113 TYR   B CA  
5633 C C   . TYR   B 113 ? 0.1186 0.1058 0.1717 -0.0045 -0.0011 0.0043  113 TYR   B C   
5634 O O   . TYR   B 113 ? 0.1220 0.1112 0.1720 -0.0014 0.0002  0.0006  113 TYR   B O   
5635 C CB  . TYR   B 113 ? 0.1289 0.1059 0.1872 -0.0029 0.0064  0.0029  113 TYR   B CB  
5636 C CG  . TYR   B 113 ? 0.1275 0.1087 0.1950 -0.0087 0.0008  0.0034  113 TYR   B CG  
5637 C CD1 . TYR   B 113 ? 0.1346 0.1122 0.2120 -0.0051 0.0087  0.0052  113 TYR   B CD1 
5638 C CD2 . TYR   B 113 ? 0.1404 0.1076 0.1937 -0.0035 -0.0011 0.0047  113 TYR   B CD2 
5639 C CE1 . TYR   B 113 ? 0.1330 0.1164 0.2005 -0.0041 0.0074  0.0062  113 TYR   B CE1 
5640 C CE2 . TYR   B 113 ? 0.1404 0.1055 0.2051 0.0010  0.0004  0.0088  113 TYR   B CE2 
5641 C CZ  . TYR   B 113 ? 0.1315 0.1128 0.2120 0.0072  -0.0009 0.0063  113 TYR   B CZ  
5642 O OH  . TYR   B 113 ? 0.1358 0.1136 0.2234 0.0089  0.0037  0.0063  113 TYR   B OH  
5652 N N   . GLU   B 114 ? 0.1181 0.1069 0.1792 -0.0002 0.0012  0.0043  114 GLU   B N   
5653 C CA  . GLU   B 114 ? 0.1150 0.1060 0.1827 0.0035  0.0017  0.0013  114 GLU   B CA  
5654 C C   . GLU   B 114 ? 0.1184 0.1084 0.1769 -0.0015 0.0016  -0.0006 114 GLU   B C   
5655 O O   . GLU   B 114 ? 0.1229 0.1093 0.1883 0.0019  0.0007  0.0085  114 GLU   B O   
5656 C CB  . GLU   B 114 ? 0.1206 0.1154 0.1966 -0.0037 0.0005  0.0087  114 GLU   B CB  
5657 C CG  . GLU   B 114 ? 0.1275 0.1212 0.1928 0.0002  0.0054  0.0069  114 GLU   B CG  
5658 C CD  . GLU   B 114 ? 0.1246 0.1271 0.1880 -0.0053 -0.0025 0.0076  114 GLU   B CD  
5659 O OE1 . GLU   B 114 ? 0.1266 0.1392 0.1954 -0.0110 0.0150  0.0057  114 GLU   B OE1 
5660 O OE2 . GLU   B 114 ? 0.1271 0.1419 0.2064 -0.0133 0.0068  0.0116  114 GLU   B OE2 
5667 N N   . ASN   B 115 ? 0.1209 0.1016 0.1825 -0.0007 -0.0067 0.0041  115 ASN   B N   
5668 C CA  . ASN   B 115 ? 0.1242 0.1124 0.1690 -0.0066 -0.0059 0.0010  115 ASN   B CA  
5669 C C   . ASN   B 115 ? 0.1217 0.1054 0.1647 -0.0087 -0.0079 -0.0003 115 ASN   B C   
5670 O O   . ASN   B 115 ? 0.1344 0.1098 0.1738 -0.0129 -0.0048 0.0014  115 ASN   B O   
5671 C CB  . ASN   B 115 ? 0.1335 0.1223 0.1647 -0.0104 -0.0064 -0.0017 115 ASN   B CB  
5672 C CG  . ASN   B 115 ? 0.1505 0.1302 0.1669 0.0022  -0.0044 -0.0027 115 ASN   B CG  
5673 O OD1 . ASN   B 115 ? 0.1965 0.1378 0.1880 -0.0003 0.0130  -0.0124 115 ASN   B OD1 
5674 N ND2 . ASN   B 115 ? 0.1493 0.1387 0.1649 -0.0052 0.0029  -0.0005 115 ASN   B ND2 
5681 N N   . PHE   B 116 ? 0.1158 0.1100 0.1581 -0.0045 -0.0032 -0.0010 116 PHE   B N   
5682 C CA  . PHE   B 116 ? 0.1229 0.1108 0.1648 -0.0031 -0.0056 0.0009  116 PHE   B CA  
5683 C C   . PHE   B 116 ? 0.1258 0.1007 0.1621 -0.0079 -0.0061 0.0104  116 PHE   B C   
5684 O O   . PHE   B 116 ? 0.1283 0.1116 0.1647 0.0006  -0.0052 0.0027  116 PHE   B O   
5685 C CB  . PHE   B 116 ? 0.1220 0.1117 0.1549 -0.0054 -0.0153 0.0043  116 PHE   B CB  
5686 C CG  . PHE   B 116 ? 0.1135 0.1110 0.1654 -0.0023 -0.0068 0.0011  116 PHE   B CG  
5687 C CD1 . PHE   B 116 ? 0.1254 0.1135 0.1800 0.0006  -0.0063 0.0063  116 PHE   B CD1 
5688 C CD2 . PHE   B 116 ? 0.1197 0.1168 0.1615 -0.0025 -0.0050 -0.0004 116 PHE   B CD2 
5689 C CE1 . PHE   B 116 ? 0.1278 0.1185 0.1797 -0.0047 -0.0106 0.0025  116 PHE   B CE1 
5690 C CE2 . PHE   B 116 ? 0.1227 0.1176 0.1644 -0.0018 -0.0030 -0.0015 116 PHE   B CE2 
5691 C CZ  . PHE   B 116 ? 0.1175 0.1189 0.1776 -0.0027 -0.0138 0.0066  116 PHE   B CZ  
5701 N N   . ASN   B 117 ? 0.1201 0.1082 0.1735 -0.0017 -0.0119 0.0017  117 ASN   B N   
5702 C CA  . ASN   B 117 ? 0.1290 0.1087 0.1735 0.0028  -0.0129 -0.0026 117 ASN   B CA  
5703 C C   . ASN   B 117 ? 0.1342 0.1094 0.1789 0.0037  -0.0043 0.0074  117 ASN   B C   
5704 O O   . ASN   B 117 ? 0.1461 0.1158 0.2035 0.0011  -0.0279 0.0054  117 ASN   B O   
5705 C CB  . ASN   B 117 ? 0.1322 0.1131 0.1694 0.0002  -0.0103 -0.0091 117 ASN   B CB  
5706 C CG  . ASN   B 117 ? 0.1295 0.1157 0.1794 0.0029  -0.0073 -0.0102 117 ASN   B CG  
5707 O OD1 . ASN   B 117 ? 0.1559 0.1136 0.1915 -0.0122 -0.0035 -0.0078 117 ASN   B OD1 
5708 N ND2 . ASN   B 117 ? 0.1323 0.1179 0.1841 -0.0014 0.0027  -0.0063 117 ASN   B ND2 
5715 N N   . GLN   B 118 ? 0.1321 0.1073 0.1742 -0.0072 -0.0179 -0.0048 118 GLN   B N   
5716 C CA  . GLN   B 118 ? 0.1383 0.1103 0.1849 0.0006  -0.0127 -0.0009 118 GLN   B CA  
5717 C C   . GLN   B 118 ? 0.1433 0.1098 0.1855 0.0016  -0.0101 -0.0008 118 GLN   B C   
5718 O O   . GLN   B 118 ? 0.1643 0.1077 0.2188 -0.0065 0.0001  0.0020  118 GLN   B O   
5719 C CB  . GLN   B 118 ? 0.1444 0.1197 0.1909 0.0012  -0.0189 -0.0026 118 GLN   B CB  
5720 C CG  . GLN   B 118 ? 0.1501 0.1165 0.1949 0.0075  -0.0128 -0.0067 118 GLN   B CG  
5721 C CD  . GLN   B 118 ? 0.1554 0.1117 0.1828 0.0030  -0.0105 -0.0117 118 GLN   B CD  
5722 O OE1 . GLN   B 118 ? 0.1645 0.1103 0.2080 0.0004  0.0012  0.0035  118 GLN   B OE1 
5723 N NE2 . GLN   B 118 ? 0.1644 0.1154 0.1920 0.0101  -0.0145 0.0031  118 GLN   B NE2 
5732 N N   . HIS   B 119 ? 0.1399 0.1120 0.1549 -0.0040 -0.0085 0.0070  119 HIS   B N   
5733 C CA  . HIS   B 119 ? 0.1465 0.1265 0.1553 -0.0019 -0.0161 0.0026  119 HIS   B CA  
5734 C C   . HIS   B 119 ? 0.1513 0.1225 0.1547 0.0003  -0.0226 0.0019  119 HIS   B C   
5735 O O   . HIS   B 119 ? 0.1612 0.1231 0.1750 -0.0176 -0.0195 0.0084  119 HIS   B O   
5736 C CB  . HIS   B 119 ? 0.1470 0.1369 0.1647 0.0022  -0.0233 -0.0037 119 HIS   B CB  
5737 C CG  . HIS   B 119 ? 0.1567 0.1572 0.1818 0.0099  -0.0267 -0.0132 119 HIS   B CG  
5738 N ND1 . HIS   B 119 ? 0.1687 0.1793 0.2052 0.0024  -0.0373 -0.0360 119 HIS   B ND1 
5739 C CD2 . HIS   B 119 ? 0.1762 0.1752 0.1867 0.0316  -0.0367 -0.0200 119 HIS   B CD2 
5740 C CE1 . HIS   B 119 ? 0.1915 0.1920 0.2148 0.0158  -0.0434 -0.0489 119 HIS   B CE1 
5741 N NE2 . HIS   B 119 ? 0.1938 0.2049 0.1981 0.0286  -0.0451 -0.0418 119 HIS   B NE2 
5749 N N   . GLU   B 120 ? 0.1669 0.1291 0.1488 -0.0072 -0.0346 0.0100  120 GLU   B N   
5750 C CA  . GLU   B 120 ? 0.1998 0.1451 0.1702 -0.0001 -0.0439 0.0319  120 GLU   B CA  
5751 C C   . GLU   B 120 ? 0.1698 0.1287 0.1606 -0.0100 -0.0276 0.0255  120 GLU   B C   
5752 O O   . GLU   B 120 ? 0.1661 0.1404 0.1610 -0.0137 -0.0260 0.0132  120 GLU   B O   
5753 C CB  . GLU   B 120 ? 0.2801 0.1953 0.2547 0.0269  -0.0796 0.0740  120 GLU   B CB  
5754 C CG  . GLU   B 120 ? 0.3454 0.2873 0.3827 0.0360  -0.1096 0.1072  120 GLU   B CG  
5755 C CD  . GLU   B 120 ? 0.4104 0.3907 0.5231 0.0341  -0.1202 0.1141  120 GLU   B CD  
5756 O OE1 . GLU   B 120 ? 0.4417 0.4271 0.5653 0.0316  -0.1198 0.1205  120 GLU   B OE1 
5757 O OE2 . GLU   B 120 ? 0.4400 0.4282 0.5902 0.0341  -0.1194 0.1070  120 GLU   B OE2 
5764 N N   . VAL   B 121 ? 0.1607 0.1218 0.1556 -0.0134 -0.0165 0.0168  121 VAL   B N   
5765 C CA  . VAL   B 121 ? 0.1594 0.1351 0.1449 -0.0113 -0.0161 0.0115  121 VAL   B CA  
5766 C C   . VAL   B 121 ? 0.1477 0.1264 0.1419 -0.0183 -0.0132 0.0065  121 VAL   B C   
5767 O O   . VAL   B 121 ? 0.1556 0.1231 0.1724 -0.0240 -0.0237 0.0039  121 VAL   B O   
5768 C CB  . VAL   B 121 ? 0.1821 0.1696 0.1530 -0.0015 -0.0249 0.0160  121 VAL   B CB  
5769 C CG1 . VAL   B 121 ? 0.1830 0.1832 0.1914 -0.0081 -0.0112 0.0107  121 VAL   B CG1 
5770 C CG2 . VAL   B 121 ? 0.2063 0.1938 0.1628 0.0068  -0.0164 0.0035  121 VAL   B CG2 
5780 N N   . LEU   B 122 ? 0.1394 0.1237 0.1426 -0.0137 -0.0269 0.0020  122 LEU   B N   
5781 C CA  . LEU   B 122 ? 0.1366 0.1297 0.1392 -0.0191 -0.0187 0.0029  122 LEU   B CA  
5782 C C   . LEU   B 122 ? 0.1355 0.1179 0.1411 -0.0241 -0.0166 0.0055  122 LEU   B C   
5783 O O   . LEU   B 122 ? 0.1464 0.1233 0.1698 -0.0254 -0.0261 0.0023  122 LEU   B O   
5784 C CB  . LEU   B 122 ? 0.1648 0.1391 0.1672 -0.0088 -0.0266 0.0099  122 LEU   B CB  
5785 C CG  . LEU   B 122 ? 0.1501 0.1448 0.1697 -0.0149 -0.0097 0.0046  122 LEU   B CG  
5786 C CD1 . LEU   B 122 ? 0.1529 0.1670 0.1837 -0.0159 -0.0147 0.0001  122 LEU   B CD1 
5787 C CD2 . LEU   B 122 ? 0.1535 0.1520 0.1528 -0.0110 -0.0082 -0.0065 122 LEU   B CD2 
5799 N N   . LEU   B 123 ? 0.1382 0.1085 0.1436 -0.0181 -0.0124 0.0010  123 LEU   B N   
5800 C CA  . LEU   B 123 ? 0.1402 0.1151 0.1443 -0.0207 -0.0175 -0.0001 123 LEU   B CA  
5801 C C   . LEU   B 123 ? 0.1355 0.1144 0.1352 -0.0195 -0.0144 -0.0009 123 LEU   B C   
5802 O O   . LEU   B 123 ? 0.1481 0.1175 0.1501 -0.0274 -0.0170 -0.0004 123 LEU   B O   
5803 C CB  . LEU   B 123 ? 0.1440 0.1191 0.1590 -0.0159 -0.0110 -0.0030 123 LEU   B CB  
5804 C CG  . LEU   B 123 ? 0.1395 0.1238 0.1658 -0.0134 -0.0108 0.0098  123 LEU   B CG  
5805 C CD1 . LEU   B 123 ? 0.1548 0.1239 0.1711 -0.0097 -0.0028 -0.0114 123 LEU   B CD1 
5806 C CD2 . LEU   B 123 ? 0.1429 0.1334 0.1851 -0.0072 -0.0058 0.0180  123 LEU   B CD2 
5818 N N   . ALA   B 124 ? 0.1387 0.1093 0.1401 -0.0209 -0.0078 -0.0008 124 ALA   B N   
5819 C CA  . ALA   B 124 ? 0.1276 0.1108 0.1588 -0.0166 -0.0065 -0.0117 124 ALA   B CA  
5820 C C   . ALA   B 124 ? 0.1266 0.1104 0.1464 -0.0147 -0.0127 -0.0110 124 ALA   B C   
5821 O O   . ALA   B 124 ? 0.1358 0.1137 0.1514 -0.0117 -0.0159 -0.0011 124 ALA   B O   
5822 C CB  . ALA   B 124 ? 0.1336 0.1163 0.1574 -0.0071 -0.0005 -0.0025 124 ALA   B CB  
5828 N N   . PRO   B 125 ? 0.1345 0.1119 0.1390 -0.0153 -0.0199 0.0099  125 PRO   B N   
5829 C CA  . PRO   B 125 ? 0.1460 0.1176 0.1579 -0.0131 -0.0171 0.0198  125 PRO   B CA  
5830 C C   . PRO   B 125 ? 0.1372 0.1071 0.1701 -0.0158 -0.0144 0.0042  125 PRO   B C   
5831 O O   . PRO   B 125 ? 0.1422 0.1069 0.1952 -0.0082 -0.0086 0.0091  125 PRO   B O   
5832 C CB  . PRO   B 125 ? 0.1509 0.1404 0.1748 -0.0174 -0.0231 0.0316  125 PRO   B CB  
5833 C CG  . PRO   B 125 ? 0.1509 0.1428 0.1676 -0.0297 -0.0219 0.0134  125 PRO   B CG  
5834 C CD  . PRO   B 125 ? 0.1468 0.1250 0.1499 -0.0285 -0.0125 0.0068  125 PRO   B CD  
5842 N N   . LEU   B 126 ? 0.1403 0.1067 0.1896 -0.0157 -0.0001 0.0107  126 LEU   B N   
5843 C CA  . LEU   B 126 ? 0.1446 0.1208 0.1924 -0.0101 0.0107  0.0127  126 LEU   B CA  
5844 C C   . LEU   B 126 ? 0.1369 0.1278 0.1913 -0.0010 0.0080  0.0120  126 LEU   B C   
5845 O O   . LEU   B 126 ? 0.1617 0.1548 0.2073 0.0181  -0.0106 -0.0100 126 LEU   B O   
5846 C CB  . LEU   B 126 ? 0.1620 0.1237 0.2209 -0.0119 0.0204  0.0050  126 LEU   B CB  
5847 C CG  . LEU   B 126 ? 0.1811 0.1320 0.2274 -0.0231 0.0222  -0.0130 126 LEU   B CG  
5848 C CD1 . LEU   B 126 ? 0.1957 0.1383 0.2703 -0.0266 0.0132  -0.0236 126 LEU   B CD1 
5849 C CD2 . LEU   B 126 ? 0.1807 0.1479 0.2220 -0.0309 0.0126  -0.0105 126 LEU   B CD2 
5861 N N   . LEU   B 127 ? 0.1344 0.1173 0.1971 -0.0006 0.0133  0.0132  127 LEU   B N   
5862 C CA  . LEU   B 127 ? 0.1352 0.1253 0.2031 -0.0031 0.0134  0.0156  127 LEU   B CA  
5863 C C   . LEU   B 127 ? 0.1330 0.1252 0.1979 -0.0036 0.0097  0.0179  127 LEU   B C   
5864 O O   . LEU   B 127 ? 0.1406 0.1296 0.1937 -0.0159 0.0004  0.0176  127 LEU   B O   
5865 C CB  . LEU   B 127 ? 0.1480 0.1248 0.2118 -0.0016 0.0101  0.0220  127 LEU   B CB  
5866 C CG  . LEU   B 127 ? 0.1612 0.1251 0.2237 0.0044  0.0111  0.0176  127 LEU   B CG  
5867 C CD1 . LEU   B 127 ? 0.1687 0.1257 0.2130 0.0047  0.0062  0.0087  127 LEU   B CD1 
5868 C CD2 . LEU   B 127 ? 0.1605 0.1349 0.2422 -0.0068 0.0196  0.0254  127 LEU   B CD2 
5880 N N   . SER   B 128 ? 0.1420 0.1187 0.1957 -0.0005 -0.0074 0.0146  128 SER   B N   
5881 C CA  . SER   B 128 ? 0.1554 0.1272 0.1943 0.0037  -0.0099 0.0159  128 SER   B CA  
5882 C C   . SER   B 128 ? 0.1647 0.1299 0.2120 0.0060  -0.0298 0.0134  128 SER   B C   
5883 O O   . SER   B 128 ? 0.1825 0.1329 0.2486 0.0058  -0.0150 0.0298  128 SER   B O   
5884 C CB  . SER   B 128 ? 0.1680 0.1309 0.1947 0.0054  -0.0056 0.0277  128 SER   B CB  
5885 O OG  . SER   B 128 ? 0.1745 0.1430 0.1960 0.0086  0.0035  0.0291  128 SER   B OG  
5891 N N   . ALA   B 129 ? 0.1727 0.1399 0.2239 0.0231  -0.0203 0.0053  129 ALA   B N   
5892 C CA  . ALA   B 129 ? 0.1866 0.1489 0.2388 0.0266  -0.0177 -0.0055 129 ALA   B CA  
5893 C C   . ALA   B 129 ? 0.1731 0.1380 0.2276 0.0160  0.0017  0.0005  129 ALA   B C   
5894 O O   . ALA   B 129 ? 0.1648 0.1407 0.2440 0.0146  -0.0053 0.0097  129 ALA   B O   
5895 C CB  . ALA   B 129 ? 0.2085 0.1717 0.2651 0.0314  -0.0093 -0.0177 129 ALA   B CB  
5901 N N   . GLY   B 130 ? 0.1684 0.1332 0.2303 0.0193  0.0064  -0.0008 130 GLY   B N   
5902 C CA  . GLY   B 130 ? 0.1731 0.1438 0.2433 0.0222  0.0273  0.0041  130 GLY   B CA  
5903 C C   . GLY   B 130 ? 0.1831 0.1436 0.2361 0.0154  0.0122  0.0068  130 GLY   B C   
5904 O O   . GLY   B 130 ? 0.2032 0.1571 0.2424 0.0161  0.0105  0.0193  130 GLY   B O   
5908 N N   . ILE   B 131 ? 0.1795 0.1550 0.2509 0.0264  0.0047  0.0038  131 ILE   B N   
5909 C CA  . ILE   B 131 ? 0.1909 0.1722 0.2448 0.0256  -0.0121 0.0181  131 ILE   B CA  
5910 C C   . ILE   B 131 ? 0.2042 0.1660 0.2115 0.0152  -0.0134 0.0231  131 ILE   B C   
5911 O O   . ILE   B 131 ? 0.2307 0.1816 0.2222 0.0208  -0.0247 0.0203  131 ILE   B O   
5912 C CB  . ILE   B 131 ? 0.1901 0.2127 0.2861 0.0244  -0.0174 0.0252  131 ILE   B CB  
5913 C CG1 . ILE   B 131 ? 0.1929 0.2327 0.2996 0.0008  -0.0089 0.0289  131 ILE   B CG1 
5914 C CG2 . ILE   B 131 ? 0.1881 0.2297 0.3095 0.0307  -0.0150 0.0195  131 ILE   B CG2 
5915 C CD1 . ILE   B 131 ? 0.2014 0.2512 0.3095 -0.0159 -0.0115 0.0376  131 ILE   B CD1 
5927 N N   . PHE   B 132 ? 0.1823 0.1466 0.2021 0.0098  0.0036  0.0256  132 PHE   B N   
5928 C CA  . PHE   B 132 ? 0.1941 0.1492 0.2016 0.0082  0.0216  0.0140  132 PHE   B CA  
5929 C C   . PHE   B 132 ? 0.2112 0.1622 0.2126 0.0107  0.0301  0.0166  132 PHE   B C   
5930 O O   . PHE   B 132 ? 0.2314 0.1841 0.2354 0.0064  0.0380  0.0220  132 PHE   B O   
5931 C CB  . PHE   B 132 ? 0.1767 0.1469 0.1918 0.0120  0.0195  0.0174  132 PHE   B CB  
5932 C CG  . PHE   B 132 ? 0.1750 0.1524 0.1895 0.0154  0.0160  0.0147  132 PHE   B CG  
5933 C CD1 . PHE   B 132 ? 0.1847 0.1573 0.2254 0.0097  0.0220  0.0126  132 PHE   B CD1 
5934 C CD2 . PHE   B 132 ? 0.1758 0.1528 0.1803 0.0199  0.0067  0.0214  132 PHE   B CD2 
5935 C CE1 . PHE   B 132 ? 0.1885 0.1625 0.2412 0.0069  0.0136  0.0100  132 PHE   B CE1 
5936 C CE2 . PHE   B 132 ? 0.1831 0.1624 0.1826 0.0181  0.0062  0.0174  132 PHE   B CE2 
5937 C CZ  . PHE   B 132 ? 0.1889 0.1625 0.2208 0.0081  -0.0026 0.0211  132 PHE   B CZ  
5947 N N   . GLY   B 133 ? 0.2121 0.1552 0.2124 0.0080  0.0139  0.0302  133 GLY   B N   
5948 C CA  . GLY   B 133 ? 0.2209 0.1631 0.2194 -0.0144 0.0106  0.0368  133 GLY   B CA  
5949 C C   . GLY   B 133 ? 0.2264 0.1658 0.2130 -0.0239 0.0161  0.0310  133 GLY   B C   
5950 O O   . GLY   B 133 ? 0.2501 0.1830 0.2588 -0.0377 0.0208  0.0488  133 GLY   B O   
5954 N N   . ALA   B 134 ? 0.2060 0.1687 0.2010 -0.0240 0.0190  0.0203  134 ALA   B N   
5955 C CA  . ALA   B 134 ? 0.1981 0.1701 0.2224 -0.0186 0.0256  0.0048  134 ALA   B CA  
5956 C C   . ALA   B 134 ? 0.2062 0.1610 0.2301 -0.0070 0.0246  0.0176  134 ALA   B C   
5957 O O   . ALA   B 134 ? 0.2134 0.1849 0.2537 0.0063  0.0275  0.0130  134 ALA   B O   
5958 C CB  . ALA   B 134 ? 0.1946 0.1722 0.2480 -0.0096 0.0175  -0.0092 134 ALA   B CB  
5964 N N   . ASP   B 135 ? 0.2157 0.1544 0.2228 -0.0118 0.0092  0.0271  135 ASP   B N   
5965 C CA  . ASP   B 135 ? 0.2340 0.1439 0.2444 -0.0115 -0.0044 0.0340  135 ASP   B CA  
5966 C C   . ASP   B 135 ? 0.2160 0.1354 0.2282 -0.0017 -0.0037 0.0259  135 ASP   B C   
5967 O O   . ASP   B 135 ? 0.2093 0.1332 0.2444 -0.0005 -0.0001 0.0248  135 ASP   B O   
5968 C CB  . ASP   B 135 ? 0.2616 0.1552 0.2689 -0.0333 -0.0099 0.0349  135 ASP   B CB  
5969 C CG  . ASP   B 135 ? 0.2934 0.1600 0.3135 -0.0512 -0.0096 0.0251  135 ASP   B CG  
5970 O OD1 . ASP   B 135 ? 0.3034 0.1475 0.3089 -0.0368 -0.0159 0.0253  135 ASP   B OD1 
5971 O OD2 . ASP   B 135 ? 0.3188 0.1987 0.3638 -0.0610 -0.0141 0.0034  135 ASP   B OD2 
5976 N N   . PRO   B 136 ? 0.2087 0.1374 0.2363 0.0188  -0.0120 0.0186  136 PRO   B N   
5977 C CA  . PRO   B 136 ? 0.1880 0.1341 0.2380 0.0147  -0.0104 0.0013  136 PRO   B CA  
5978 C C   . PRO   B 136 ? 0.1740 0.1210 0.2458 0.0121  -0.0056 0.0020  136 PRO   B C   
5979 O O   . PRO   B 136 ? 0.1596 0.1197 0.2378 0.0071  -0.0012 0.0078  136 PRO   B O   
5980 C CB  . PRO   B 136 ? 0.1960 0.1583 0.2486 0.0245  -0.0163 -0.0050 136 PRO   B CB  
5981 C CG  . PRO   B 136 ? 0.2154 0.1628 0.2628 0.0317  -0.0108 -0.0062 136 PRO   B CG  
5982 C CD  . PRO   B 136 ? 0.2169 0.1550 0.2497 0.0388  -0.0055 0.0071  136 PRO   B CD  
5990 N N   . ILE   B 137 ? 0.1806 0.1170 0.2565 0.0112  -0.0138 0.0048  137 ILE   B N   
5991 C CA  . ILE   B 137 ? 0.1893 0.1200 0.2671 -0.0003 -0.0050 -0.0019 137 ILE   B CA  
5992 C C   . ILE   B 137 ? 0.1804 0.1230 0.2489 -0.0057 0.0043  0.0128  137 ILE   B C   
5993 O O   . ILE   B 137 ? 0.1671 0.1297 0.2457 -0.0085 0.0023  0.0050  137 ILE   B O   
5994 C CB  . ILE   B 137 ? 0.2132 0.1277 0.3178 -0.0036 -0.0081 -0.0033 137 ILE   B CB  
5995 C CG1 . ILE   B 137 ? 0.2456 0.1407 0.3698 -0.0010 -0.0028 -0.0163 137 ILE   B CG1 
5996 C CG2 . ILE   B 137 ? 0.2164 0.1294 0.3336 -0.0230 -0.0139 -0.0023 137 ILE   B CG2 
5997 C CD1 . ILE   B 137 ? 0.2708 0.1697 0.4096 0.0129  -0.0061 -0.0053 137 ILE   B CD1 
6009 N N   . HIS   B 138 ? 0.1862 0.1193 0.2456 -0.0057 0.0102  0.0129  138 HIS   B N   
6010 C CA  . HIS   B 138 ? 0.1930 0.1295 0.2394 -0.0034 0.0184  0.0077  138 HIS   B CA  
6011 C C   . HIS   B 138 ? 0.1794 0.1263 0.2255 -0.0004 0.0206  0.0207  138 HIS   B C   
6012 O O   . HIS   B 138 ? 0.1705 0.1327 0.2582 0.0034  0.0211  0.0346  138 HIS   B O   
6013 C CB  . HIS   B 138 ? 0.2146 0.1432 0.2516 -0.0085 0.0298  0.0065  138 HIS   B CB  
6014 C CG  . HIS   B 138 ? 0.2334 0.1580 0.2528 -0.0111 0.0444  0.0268  138 HIS   B CG  
6015 N ND1 . HIS   B 138 ? 0.2403 0.1754 0.2817 -0.0123 0.0600  0.0194  138 HIS   B ND1 
6016 C CD2 . HIS   B 138 ? 0.2478 0.1699 0.2558 -0.0108 0.0545  0.0188  138 HIS   B CD2 
6017 C CE1 . HIS   B 138 ? 0.2465 0.1791 0.2752 -0.0139 0.0633  0.0243  138 HIS   B CE1 
6018 N NE2 . HIS   B 138 ? 0.2542 0.1670 0.2627 -0.0038 0.0628  0.0151  138 HIS   B NE2 
6026 N N   . SER   B 139 ? 0.1732 0.1188 0.2251 0.0021  0.0177  0.0113  139 SER   B N   
6027 C CA  . SER   B 139 ? 0.1652 0.1149 0.2109 -0.0035 0.0149  0.0016  139 SER   B CA  
6028 C C   . SER   B 139 ? 0.1444 0.1061 0.2169 -0.0020 0.0117  0.0012  139 SER   B C   
6029 O O   . SER   B 139 ? 0.1453 0.1088 0.2214 0.0020  0.0007  0.0050  139 SER   B O   
6030 C CB  . SER   B 139 ? 0.1793 0.1144 0.2128 0.0043  -0.0004 0.0074  139 SER   B CB  
6031 O OG  . SER   B 139 ? 0.1849 0.1140 0.2156 0.0046  -0.0139 0.0080  139 SER   B OG  
6037 N N   . LEU   B 140 ? 0.1444 0.1034 0.2111 -0.0061 0.0066  -0.0035 140 LEU   B N   
6038 C CA  . LEU   B 140 ? 0.1403 0.1047 0.2199 -0.0043 0.0038  -0.0000 140 LEU   B CA  
6039 C C   . LEU   B 140 ? 0.1391 0.1082 0.2316 -0.0025 -0.0039 -0.0027 140 LEU   B C   
6040 O O   . LEU   B 140 ? 0.1338 0.1166 0.2302 0.0001  -0.0070 -0.0004 140 LEU   B O   
6041 C CB  . LEU   B 140 ? 0.1380 0.1078 0.2340 -0.0107 0.0067  -0.0094 140 LEU   B CB  
6042 C CG  . LEU   B 140 ? 0.1498 0.1098 0.2211 -0.0104 -0.0032 0.0051  140 LEU   B CG  
6043 C CD1 . LEU   B 140 ? 0.1637 0.1202 0.2304 -0.0171 -0.0016 -0.0018 140 LEU   B CD1 
6044 C CD2 . LEU   B 140 ? 0.1689 0.1252 0.2330 -0.0096 -0.0074 -0.0032 140 LEU   B CD2 
6056 N N   . ARG   B 141 ? 0.1306 0.1141 0.2375 -0.0066 0.0112  -0.0041 141 ARG   B N   
6057 C CA  . ARG   B 141 ? 0.1354 0.1119 0.2785 -0.0146 0.0206  -0.0041 141 ARG   B CA  
6058 C C   . ARG   B 141 ? 0.1279 0.1172 0.2609 -0.0134 0.0092  -0.0017 141 ARG   B C   
6059 O O   . ARG   B 141 ? 0.1406 0.1190 0.2529 -0.0137 -0.0006 -0.0143 141 ARG   B O   
6060 C CB  . ARG   B 141 ? 0.1538 0.1251 0.3089 -0.0153 0.0342  0.0006  141 ARG   B CB  
6061 C CG  . ARG   B 141 ? 0.1841 0.1474 0.3329 -0.0209 0.0361  0.0011  141 ARG   B CG  
6062 C CD  . ARG   B 141 ? 0.2302 0.1722 0.3392 -0.0111 0.0219  -0.0152 141 ARG   B CD  
6063 N NE  . ARG   B 141 ? 0.2598 0.1767 0.3394 -0.0301 0.0316  -0.0206 141 ARG   B NE  
6064 C CZ  . ARG   B 141 ? 0.2775 0.1596 0.3295 -0.0265 0.0486  -0.0279 141 ARG   B CZ  
6065 N NH1 . ARG   B 141 ? 0.2866 0.1537 0.3228 -0.0293 0.0459  -0.0280 141 ARG   B NH1 
6066 N NH2 . ARG   B 141 ? 0.2867 0.1695 0.3407 -0.0124 0.0418  -0.0170 141 ARG   B NH2 
6080 N N   . VAL   B 142 ? 0.1346 0.1100 0.2462 -0.0046 0.0112  -0.0046 142 VAL   B N   
6081 C CA  . VAL   B 142 ? 0.1307 0.1147 0.2320 -0.0055 0.0149  -0.0019 142 VAL   B CA  
6082 C C   . VAL   B 142 ? 0.1339 0.1149 0.2291 -0.0015 0.0062  -0.0070 142 VAL   B C   
6083 O O   . VAL   B 142 ? 0.1395 0.1086 0.2392 0.0034  0.0075  -0.0028 142 VAL   B O   
6084 C CB  . VAL   B 142 ? 0.1476 0.1258 0.2401 -0.0022 0.0136  0.0070  142 VAL   B CB  
6085 C CG1 . VAL   B 142 ? 0.1480 0.1208 0.2398 0.0060  0.0138  0.0022  142 VAL   B CG1 
6086 C CG2 . VAL   B 142 ? 0.1660 0.1292 0.2475 -0.0016 0.0144  0.0199  142 VAL   B CG2 
6096 N N   . CYS   B 143 ? 0.1283 0.1118 0.2215 -0.0008 0.0007  0.0068  143 CYS   B N   
6097 C CA  . CYS   B 143 ? 0.1276 0.1119 0.2248 -0.0039 -0.0013 0.0046  143 CYS   B CA  
6098 C C   . CYS   B 143 ? 0.1202 0.1109 0.2219 -0.0044 0.0006  -0.0016 143 CYS   B C   
6099 O O   . CYS   B 143 ? 0.1288 0.1155 0.2220 -0.0050 -0.0057 0.0001  143 CYS   B O   
6100 C CB  . CYS   B 143 ? 0.1335 0.1229 0.2262 -0.0050 -0.0026 -0.0001 143 CYS   B CB  
6101 S SG  . CYS   B 143 ? 0.1379 0.1380 0.2152 -0.0047 0.0018  0.0033  143 CYS   B SG  
6107 N N   . VAL   B 144 ? 0.1290 0.1163 0.2291 -0.0024 0.0019  -0.0170 144 VAL   B N   
6108 C CA  . VAL   B 144 ? 0.1331 0.1250 0.2533 -0.0120 -0.0111 -0.0194 144 VAL   B CA  
6109 C C   . VAL   B 144 ? 0.1315 0.1269 0.2593 -0.0095 -0.0108 -0.0052 144 VAL   B C   
6110 O O   . VAL   B 144 ? 0.1456 0.1473 0.2743 0.0023  -0.0084 0.0088  144 VAL   B O   
6111 C CB  . VAL   B 144 ? 0.1579 0.1375 0.3096 -0.0145 -0.0181 -0.0346 144 VAL   B CB  
6112 C CG1 . VAL   B 144 ? 0.1826 0.1798 0.3432 -0.0107 -0.0256 -0.0319 144 VAL   B CG1 
6113 C CG2 . VAL   B 144 ? 0.1753 0.1328 0.2983 0.0022  -0.0321 -0.0425 144 VAL   B CG2 
6123 N N   . ASP   B 145 ? 0.1342 0.1158 0.2654 -0.0064 -0.0114 -0.0146 145 ASP   B N   
6124 C CA  . ASP   B 145 ? 0.1305 0.1241 0.2809 -0.0088 -0.0014 -0.0154 145 ASP   B CA  
6125 C C   . ASP   B 145 ? 0.1252 0.1288 0.2684 -0.0056 -0.0012 -0.0118 145 ASP   B C   
6126 O O   . ASP   B 145 ? 0.1313 0.1433 0.3226 -0.0112 0.0024  -0.0275 145 ASP   B O   
6127 C CB  . ASP   B 145 ? 0.1475 0.1317 0.3174 -0.0140 0.0114  -0.0156 145 ASP   B CB  
6128 C CG  . ASP   B 145 ? 0.1630 0.1392 0.3631 -0.0185 0.0217  -0.0038 145 ASP   B CG  
6129 O OD1 . ASP   B 145 ? 0.1625 0.1449 0.3661 -0.0208 -0.0124 -0.0164 145 ASP   B OD1 
6130 O OD2 . ASP   B 145 ? 0.1957 0.1504 0.4148 -0.0210 0.0480  0.0025  145 ASP   B OD2 
6135 N N   . THR   B 146 ? 0.1230 0.1196 0.2286 -0.0050 -0.0008 -0.0045 146 THR   B N   
6136 C CA  . THR   B 146 ? 0.1309 0.1143 0.2131 -0.0052 0.0063  -0.0038 146 THR   B CA  
6137 C C   . THR   B 146 ? 0.1288 0.1126 0.2116 -0.0035 -0.0027 0.0017  146 THR   B C   
6138 O O   . THR   B 146 ? 0.1354 0.1153 0.2238 -0.0045 -0.0011 -0.0004 146 THR   B O   
6139 C CB  . THR   B 146 ? 0.1411 0.1151 0.2229 -0.0078 0.0089  0.0020  146 THR   B CB  
6140 O OG1 . THR   B 146 ? 0.1440 0.1127 0.2284 -0.0078 0.0066  0.0066  146 THR   B OG1 
6141 C CG2 . THR   B 146 ? 0.1527 0.1204 0.2174 -0.0093 0.0138  0.0013  146 THR   B CG2 
6149 N N   . VAL   B 147 ? 0.1337 0.1169 0.2020 -0.0054 0.0053  0.0019  147 VAL   B N   
6150 C CA  . VAL   B 147 ? 0.1383 0.1105 0.1947 -0.0083 -0.0060 -0.0005 147 VAL   B CA  
6151 C C   . VAL   B 147 ? 0.1311 0.1121 0.2025 -0.0145 -0.0096 -0.0043 147 VAL   B C   
6152 O O   . VAL   B 147 ? 0.1431 0.1262 0.2126 -0.0171 -0.0282 -0.0166 147 VAL   B O   
6153 C CB  . VAL   B 147 ? 0.1450 0.1254 0.1811 -0.0114 -0.0158 -0.0016 147 VAL   B CB  
6154 C CG1 . VAL   B 147 ? 0.1417 0.1408 0.1760 -0.0132 -0.0122 0.0063  147 VAL   B CG1 
6155 C CG2 . VAL   B 147 ? 0.1456 0.1267 0.1822 -0.0093 -0.0111 0.0001  147 VAL   B CG2 
6165 N N   . ARG   B 148 ? 0.1349 0.1140 0.1987 -0.0076 -0.0209 -0.0134 148 ARG   B N   
6166 C CA  . ARG   B 148 ? 0.1349 0.1253 0.1923 -0.0070 -0.0248 -0.0135 148 ARG   B CA  
6167 C C   . ARG   B 148 ? 0.1379 0.1343 0.1770 -0.0051 -0.0209 -0.0078 148 ARG   B C   
6168 O O   . ARG   B 148 ? 0.1570 0.1660 0.1819 -0.0172 -0.0316 -0.0048 148 ARG   B O   
6169 C CB  . ARG   B 148 ? 0.1404 0.1345 0.2071 -0.0052 -0.0289 -0.0171 148 ARG   B CB  
6170 C CG  . ARG   B 148 ? 0.1398 0.1519 0.2218 -0.0104 -0.0228 -0.0303 148 ARG   B CG  
6171 C CD  . ARG   B 148 ? 0.1423 0.1669 0.2303 0.0094  -0.0259 -0.0318 148 ARG   B CD  
6172 N NE  . ARG   B 148 ? 0.1458 0.1633 0.2190 0.0230  -0.0255 -0.0280 148 ARG   B NE  
6173 C CZ  . ARG   B 148 ? 0.1461 0.1563 0.1963 0.0166  -0.0230 -0.0201 148 ARG   B CZ  
6174 N NH1 . ARG   B 148 ? 0.1435 0.1591 0.2039 0.0010  -0.0118 -0.0177 148 ARG   B NH1 
6175 N NH2 . ARG   B 148 ? 0.1662 0.1462 0.1908 0.0166  -0.0144 -0.0083 148 ARG   B NH2 
6189 N N   . THR   B 149 ? 0.1409 0.1303 0.1817 -0.0098 -0.0214 -0.0027 149 THR   B N   
6190 C CA  . THR   B 149 ? 0.1462 0.1326 0.1844 -0.0113 -0.0193 0.0009  149 THR   B CA  
6191 C C   . THR   B 149 ? 0.1466 0.1259 0.1758 -0.0139 -0.0251 -0.0020 149 THR   B C   
6192 O O   . THR   B 149 ? 0.1513 0.1282 0.1784 -0.0185 -0.0169 -0.0039 149 THR   B O   
6193 C CB  . THR   B 149 ? 0.1469 0.1285 0.1852 -0.0149 -0.0218 -0.0016 149 THR   B CB  
6194 O OG1 . THR   B 149 ? 0.1519 0.1341 0.1811 -0.0179 -0.0285 -0.0019 149 THR   B OG1 
6195 C CG2 . THR   B 149 ? 0.1547 0.1341 0.2020 -0.0043 -0.0149 -0.0031 149 THR   B CG2 
6203 N N   . ASN   B 150 ? 0.1533 0.1277 0.1691 -0.0100 -0.0295 -0.0005 150 ASN   B N   
6204 C CA  . ASN   B 150 ? 0.1593 0.1370 0.1658 -0.0131 -0.0294 -0.0094 150 ASN   B CA  
6205 C C   . ASN   B 150 ? 0.1439 0.1325 0.1697 -0.0125 -0.0279 -0.0047 150 ASN   B C   
6206 O O   . ASN   B 150 ? 0.1563 0.1365 0.1951 -0.0202 -0.0440 -0.0041 150 ASN   B O   
6207 C CB  . ASN   B 150 ? 0.1814 0.1740 0.1719 -0.0137 -0.0362 0.0033  150 ASN   B CB  
6208 C CG  . ASN   B 150 ? 0.2070 0.2153 0.2027 -0.0172 -0.0359 0.0187  150 ASN   B CG  
6209 O OD1 . ASN   B 150 ? 0.2172 0.2347 0.2273 -0.0282 -0.0552 0.0112  150 ASN   B OD1 
6210 N ND2 . ASN   B 150 ? 0.2165 0.2319 0.2337 -0.0049 -0.0362 0.0550  150 ASN   B ND2 
6217 N N   . VAL   B 151 ? 0.1394 0.1309 0.1611 -0.0140 -0.0258 -0.0047 151 VAL   B N   
6218 C CA  . VAL   B 151 ? 0.1413 0.1337 0.1637 -0.0174 -0.0267 -0.0042 151 VAL   B CA  
6219 C C   . VAL   B 151 ? 0.1448 0.1233 0.1702 -0.0269 -0.0244 -0.0101 151 VAL   B C   
6220 O O   . VAL   B 151 ? 0.1513 0.1365 0.1871 -0.0211 -0.0215 -0.0124 151 VAL   B O   
6221 C CB  . VAL   B 151 ? 0.1619 0.1509 0.1810 -0.0073 -0.0241 -0.0035 151 VAL   B CB  
6222 C CG1 . VAL   B 151 ? 0.1743 0.1498 0.2090 -0.0137 -0.0159 -0.0163 151 VAL   B CG1 
6223 C CG2 . VAL   B 151 ? 0.1728 0.1664 0.1689 0.0052  -0.0200 0.0089  151 VAL   B CG2 
6233 N N   . TYR   B 152 ? 0.1414 0.1145 0.1648 -0.0179 -0.0231 -0.0085 152 TYR   B N   
6234 C CA  . TYR   B 152 ? 0.1460 0.1317 0.1561 -0.0215 -0.0167 -0.0123 152 TYR   B CA  
6235 C C   . TYR   B 152 ? 0.1409 0.1215 0.1475 -0.0135 -0.0137 -0.0092 152 TYR   B C   
6236 O O   . TYR   B 152 ? 0.1468 0.1244 0.1562 -0.0209 -0.0174 -0.0054 152 TYR   B O   
6237 C CB  . TYR   B 152 ? 0.1599 0.1390 0.1677 -0.0199 -0.0184 0.0020  152 TYR   B CB  
6238 C CG  . TYR   B 152 ? 0.1713 0.1479 0.1614 -0.0298 -0.0179 0.0016  152 TYR   B CG  
6239 C CD1 . TYR   B 152 ? 0.1824 0.1628 0.1573 -0.0164 -0.0246 0.0052  152 TYR   B CD1 
6240 C CD2 . TYR   B 152 ? 0.1920 0.1641 0.1597 -0.0317 -0.0079 -0.0009 152 TYR   B CD2 
6241 C CE1 . TYR   B 152 ? 0.1995 0.1788 0.1707 -0.0176 -0.0274 0.0134  152 TYR   B CE1 
6242 C CE2 . TYR   B 152 ? 0.2028 0.1854 0.1720 -0.0281 -0.0154 -0.0051 152 TYR   B CE2 
6243 C CZ  . TYR   B 152 ? 0.2057 0.1969 0.1612 -0.0255 -0.0385 0.0173  152 TYR   B CZ  
6244 O OH  . TYR   B 152 ? 0.2239 0.2351 0.1959 -0.0161 -0.0441 0.0180  152 TYR   B OH  
6254 N N   . LEU   B 153 ? 0.1403 0.1159 0.1639 -0.0248 -0.0156 -0.0056 153 LEU   B N   
6255 C CA  . LEU   B 153 ? 0.1443 0.1169 0.1580 -0.0188 -0.0082 -0.0097 153 LEU   B CA  
6256 C C   . LEU   B 153 ? 0.1428 0.1140 0.1699 -0.0191 -0.0079 -0.0187 153 LEU   B C   
6257 O O   . LEU   B 153 ? 0.1518 0.1337 0.1832 -0.0073 -0.0101 -0.0351 153 LEU   B O   
6258 C CB  . LEU   B 153 ? 0.1450 0.1177 0.1720 -0.0192 -0.0060 -0.0023 153 LEU   B CB  
6259 C CG  . LEU   B 153 ? 0.1398 0.1256 0.1930 -0.0196 -0.0056 0.0003  153 LEU   B CG  
6260 C CD1 . LEU   B 153 ? 0.1491 0.1425 0.1949 -0.0249 0.0035  0.0019  153 LEU   B CD1 
6261 C CD2 . LEU   B 153 ? 0.1462 0.1429 0.1979 -0.0199 0.0023  -0.0051 153 LEU   B CD2 
6273 N N   . ALA   B 154 ? 0.1400 0.1166 0.1743 -0.0069 -0.0172 -0.0087 154 ALA   B N   
6274 C CA  . ALA   B 154 ? 0.1554 0.1257 0.1861 0.0006  -0.0149 -0.0210 154 ALA   B CA  
6275 C C   . ALA   B 154 ? 0.1630 0.1272 0.1890 0.0013  -0.0276 -0.0206 154 ALA   B C   
6276 O O   . ALA   B 154 ? 0.1950 0.1317 0.2087 0.0047  -0.0127 -0.0122 154 ALA   B O   
6277 C CB  . ALA   B 154 ? 0.1470 0.1478 0.2147 -0.0058 -0.0135 -0.0238 154 ALA   B CB  
6283 N N   . VAL   B 155 ? 0.1342 0.1165 0.2071 -0.0027 -0.0095 -0.0170 155 VAL   B N   
6284 C CA  . VAL   B 155 ? 0.1339 0.1177 0.2088 -0.0038 -0.0176 -0.0082 155 VAL   B CA  
6285 C C   . VAL   B 155 ? 0.1358 0.1149 0.2022 -0.0064 -0.0157 -0.0142 155 VAL   B C   
6286 O O   . VAL   B 155 ? 0.1526 0.1349 0.2354 0.0009  -0.0147 -0.0248 155 VAL   B O   
6287 C CB  . VAL   B 155 ? 0.1368 0.1339 0.2525 -0.0062 -0.0177 0.0015  155 VAL   B CB  
6288 C CG1 . VAL   B 155 ? 0.1411 0.1288 0.2491 -0.0138 -0.0181 -0.0041 155 VAL   B CG1 
6289 C CG2 . VAL   B 155 ? 0.1303 0.1415 0.2863 -0.0065 -0.0151 0.0247  155 VAL   B CG2 
6299 N N   . PHE   B 156 ? 0.1233 0.1300 0.2222 0.0019  -0.0129 -0.0096 156 PHE   B N   
6300 C CA  . PHE   B 156 ? 0.1270 0.1365 0.2538 0.0047  -0.0093 -0.0101 156 PHE   B CA  
6301 C C   . PHE   B 156 ? 0.1257 0.1463 0.2788 0.0116  -0.0170 -0.0287 156 PHE   B C   
6302 O O   . PHE   B 156 ? 0.1485 0.1689 0.3053 0.0225  -0.0007 -0.0347 156 PHE   B O   
6303 C CB  . PHE   B 156 ? 0.1376 0.1373 0.2631 -0.0040 -0.0235 -0.0064 156 PHE   B CB  
6304 C CG  . PHE   B 156 ? 0.1371 0.1433 0.2768 -0.0077 -0.0195 0.0122  156 PHE   B CG  
6305 C CD1 . PHE   B 156 ? 0.1372 0.1750 0.3131 -0.0010 -0.0101 0.0475  156 PHE   B CD1 
6306 C CD2 . PHE   B 156 ? 0.1412 0.1548 0.2798 -0.0014 -0.0253 0.0226  156 PHE   B CD2 
6307 C CE1 . PHE   B 156 ? 0.1421 0.1918 0.3346 0.0032  -0.0063 0.0506  156 PHE   B CE1 
6308 C CE2 . PHE   B 156 ? 0.1489 0.1756 0.3067 0.0036  -0.0202 0.0236  156 PHE   B CE2 
6309 C CZ  . PHE   B 156 ? 0.1419 0.1893 0.3313 0.0132  -0.0204 0.0370  156 PHE   B CZ  
6319 N N   . ASP   B 157 ? 0.1270 0.1340 0.3060 0.0125  -0.0242 -0.0111 157 ASP   B N   
6320 C CA  . ASP   B 157 ? 0.1385 0.1391 0.3362 0.0072  -0.0296 -0.0154 157 ASP   B CA  
6321 C C   . ASP   B 157 ? 0.1390 0.1338 0.3424 0.0115  -0.0259 -0.0316 157 ASP   B C   
6322 O O   . ASP   B 157 ? 0.1335 0.1382 0.3260 0.0067  -0.0235 -0.0277 157 ASP   B O   
6323 C CB  . ASP   B 157 ? 0.1662 0.1587 0.3545 0.0062  -0.0503 -0.0044 157 ASP   B CB  
6324 C CG  . ASP   B 157 ? 0.2020 0.1684 0.3826 -0.0007 -0.0381 -0.0018 157 ASP   B CG  
6325 O OD1 . ASP   B 157 ? 0.2089 0.1631 0.3975 0.0036  -0.0326 -0.0012 157 ASP   B OD1 
6326 O OD2 . ASP   B 157 ? 0.2335 0.1967 0.4103 -0.0013 -0.0147 -0.0012 157 ASP   B OD2 
6331 N N   . LYS   B 158 ? 0.1428 0.1580 0.3560 0.0065  -0.0061 -0.0523 158 LYS   B N   
6332 C CA  . LYS   B 158 ? 0.1564 0.1770 0.3633 0.0053  0.0004  -0.0752 158 LYS   B CA  
6333 C C   . LYS   B 158 ? 0.1535 0.1614 0.3633 0.0089  -0.0082 -0.0689 158 LYS   B C   
6334 O O   . LYS   B 158 ? 0.1598 0.1633 0.3694 -0.0004 -0.0098 -0.0721 158 LYS   B O   
6335 C CB  . LYS   B 158 ? 0.1839 0.2221 0.3670 0.0080  0.0075  -0.1038 158 LYS   B CB  
6336 C CG  . LYS   B 158 ? 0.2332 0.2709 0.3817 0.0128  0.0108  -0.1159 158 LYS   B CG  
6337 C CD  . LYS   B 158 ? 0.2815 0.3264 0.3980 0.0170  0.0180  -0.1230 158 LYS   B CD  
6338 C CE  . LYS   B 158 ? 0.3143 0.3668 0.4223 0.0247  0.0226  -0.1219 158 LYS   B CE  
6339 N NZ  . LYS   B 158 ? 0.3241 0.3862 0.4289 0.0273  0.0250  -0.1195 158 LYS   B NZ  
6353 N N   . ASN   B 159 ? 0.1591 0.1523 0.3799 0.0074  -0.0107 -0.0520 159 ASN   B N   
6354 C CA  . ASN   B 159 ? 0.1690 0.1471 0.3984 0.0173  -0.0235 -0.0394 159 ASN   B CA  
6355 C C   . ASN   B 159 ? 0.1542 0.1355 0.3787 0.0156  -0.0359 -0.0330 159 ASN   B C   
6356 O O   . ASN   B 159 ? 0.1599 0.1342 0.3987 -0.0036 -0.0389 -0.0251 159 ASN   B O   
6357 C CB  . ASN   B 159 ? 0.1914 0.1650 0.4368 0.0202  -0.0306 -0.0352 159 ASN   B CB  
6358 C CG  . ASN   B 159 ? 0.2166 0.1848 0.4754 0.0222  -0.0461 -0.0550 159 ASN   B CG  
6359 O OD1 . ASN   B 159 ? 0.2349 0.1955 0.4789 0.0306  -0.0479 -0.0684 159 ASN   B OD1 
6360 N ND2 . ASN   B 159 ? 0.2199 0.1993 0.4954 0.0284  -0.0522 -0.0534 159 ASN   B ND2 
6367 N N   . LEU   B 160 ? 0.1460 0.1295 0.3533 0.0079  -0.0350 -0.0277 160 LEU   B N   
6368 C CA  . LEU   B 160 ? 0.1412 0.1393 0.3178 0.0071  -0.0293 -0.0164 160 LEU   B CA  
6369 C C   . LEU   B 160 ? 0.1373 0.1289 0.3047 -0.0006 -0.0284 -0.0277 160 LEU   B C   
6370 O O   . LEU   B 160 ? 0.1302 0.1347 0.2971 -0.0045 -0.0271 -0.0205 160 LEU   B O   
6371 C CB  . LEU   B 160 ? 0.1437 0.1485 0.2919 0.0025  -0.0358 -0.0100 160 LEU   B CB  
6372 C CG  . LEU   B 160 ? 0.1425 0.1613 0.2723 0.0083  -0.0331 -0.0038 160 LEU   B CG  
6373 C CD1 . LEU   B 160 ? 0.1552 0.1763 0.2658 -0.0008 -0.0213 -0.0043 160 LEU   B CD1 
6374 C CD2 . LEU   B 160 ? 0.1469 0.1691 0.2834 0.0156  -0.0333 -0.0166 160 LEU   B CD2 
6386 N N   . TYR   B 161 ? 0.1327 0.1366 0.3046 -0.0044 -0.0061 -0.0389 161 TYR   B N   
6387 C CA  . TYR   B 161 ? 0.1415 0.1330 0.2960 -0.0099 0.0044  -0.0373 161 TYR   B CA  
6388 C C   . TYR   B 161 ? 0.1438 0.1341 0.2855 -0.0079 0.0050  -0.0371 161 TYR   B C   
6389 O O   . TYR   B 161 ? 0.1475 0.1344 0.2740 -0.0107 -0.0008 -0.0300 161 TYR   B O   
6390 C CB  . TYR   B 161 ? 0.1543 0.1413 0.2975 -0.0160 0.0176  -0.0439 161 TYR   B CB  
6391 C CG  . TYR   B 161 ? 0.1746 0.1463 0.2873 -0.0208 0.0294  -0.0486 161 TYR   B CG  
6392 C CD1 . TYR   B 161 ? 0.1828 0.1439 0.2768 -0.0347 0.0284  -0.0474 161 TYR   B CD1 
6393 C CD2 . TYR   B 161 ? 0.2004 0.1565 0.2797 -0.0210 0.0174  -0.0494 161 TYR   B CD2 
6394 C CE1 . TYR   B 161 ? 0.2017 0.1654 0.2784 -0.0365 0.0220  -0.0444 161 TYR   B CE1 
6395 C CE2 . TYR   B 161 ? 0.2200 0.1759 0.2885 -0.0311 0.0192  -0.0467 161 TYR   B CE2 
6396 C CZ  . TYR   B 161 ? 0.2122 0.1777 0.2819 -0.0413 0.0168  -0.0366 161 TYR   B CZ  
6397 O OH  . TYR   B 161 ? 0.2455 0.2030 0.3037 -0.0393 0.0194  -0.0278 161 TYR   B OH  
6407 N N   . ASP   B 162 ? 0.1491 0.1303 0.3052 -0.0077 -0.0062 -0.0445 162 ASP   B N   
6408 C CA  . ASP   B 162 ? 0.1650 0.1387 0.3143 -0.0031 -0.0034 -0.0472 162 ASP   B CA  
6409 C C   . ASP   B 162 ? 0.1574 0.1299 0.3056 -0.0060 -0.0082 -0.0436 162 ASP   B C   
6410 O O   . ASP   B 162 ? 0.1660 0.1387 0.2999 -0.0179 -0.0143 -0.0309 162 ASP   B O   
6411 C CB  . ASP   B 162 ? 0.1808 0.1572 0.3401 0.0036  -0.0045 -0.0615 162 ASP   B CB  
6412 C CG  . ASP   B 162 ? 0.1863 0.1882 0.3586 0.0117  -0.0050 -0.0789 162 ASP   B CG  
6413 O OD1 . ASP   B 162 ? 0.1844 0.2117 0.3512 0.0068  0.0047  -0.0680 162 ASP   B OD1 
6414 O OD2 . ASP   B 162 ? 0.2063 0.2085 0.3903 0.0272  0.0050  -0.0823 162 ASP   B OD2 
6419 N N   . LYS   B 163 ? 0.1534 0.1216 0.3032 -0.0071 -0.0223 -0.0307 163 LYS   B N   
6420 C CA  . LYS   B 163 ? 0.1647 0.1285 0.2997 -0.0203 -0.0197 -0.0125 163 LYS   B CA  
6421 C C   . LYS   B 163 ? 0.1409 0.1234 0.2833 -0.0169 -0.0172 -0.0074 163 LYS   B C   
6422 O O   . LYS   B 163 ? 0.1416 0.1389 0.3023 -0.0220 -0.0188 -0.0047 163 LYS   B O   
6423 C CB  . LYS   B 163 ? 0.2103 0.1662 0.3358 -0.0189 -0.0250 0.0168  163 LYS   B CB  
6424 C CG  . LYS   B 163 ? 0.2875 0.2538 0.4069 -0.0247 -0.0181 0.0309  163 LYS   B CG  
6425 C CD  . LYS   B 163 ? 0.3665 0.3410 0.4838 -0.0358 -0.0186 0.0304  163 LYS   B CD  
6426 C CE  . LYS   B 163 ? 0.4275 0.4124 0.5356 -0.0453 -0.0136 0.0350  163 LYS   B CE  
6427 N NZ  . LYS   B 163 ? 0.4623 0.4623 0.5712 -0.0506 -0.0116 0.0345  163 LYS   B NZ  
6441 N N   . LEU   B 164 ? 0.1289 0.1203 0.2731 -0.0097 -0.0192 -0.0103 164 LEU   B N   
6442 C CA  . LEU   B 164 ? 0.1371 0.1185 0.2538 -0.0073 -0.0257 -0.0064 164 LEU   B CA  
6443 C C   . LEU   B 164 ? 0.1365 0.1238 0.2489 -0.0139 -0.0258 -0.0024 164 LEU   B C   
6444 O O   . LEU   B 164 ? 0.1369 0.1468 0.2683 -0.0083 -0.0298 -0.0069 164 LEU   B O   
6445 C CB  . LEU   B 164 ? 0.1305 0.1248 0.2379 -0.0082 -0.0237 -0.0045 164 LEU   B CB  
6446 C CG  . LEU   B 164 ? 0.1409 0.1408 0.2418 -0.0113 -0.0185 -0.0025 164 LEU   B CG  
6447 C CD1 . LEU   B 164 ? 0.1478 0.1359 0.2461 -0.0106 -0.0250 -0.0048 164 LEU   B CD1 
6448 C CD2 . LEU   B 164 ? 0.1540 0.1813 0.2526 -0.0052 -0.0084 -0.0182 164 LEU   B CD2 
6460 N N   . VAL   B 165 ? 0.1599 0.1320 0.2675 -0.0122 -0.0271 -0.0187 165 VAL   B N   
6461 C CA  . VAL   B 165 ? 0.1903 0.1449 0.2643 -0.0179 -0.0455 -0.0145 165 VAL   B CA  
6462 C C   . VAL   B 165 ? 0.2128 0.1552 0.2843 -0.0285 -0.0672 -0.0128 165 VAL   B C   
6463 O O   . VAL   B 165 ? 0.2282 0.1675 0.2901 -0.0382 -0.0761 0.0010  165 VAL   B O   
6464 C CB  . VAL   B 165 ? 0.2118 0.1621 0.2629 -0.0091 -0.0168 -0.0141 165 VAL   B CB  
6465 C CG1 . VAL   B 165 ? 0.2295 0.1739 0.2832 -0.0139 -0.0049 -0.0087 165 VAL   B CG1 
6466 C CG2 . VAL   B 165 ? 0.2033 0.1651 0.2641 -0.0086 -0.0096 -0.0111 165 VAL   B CG2 
6476 N N   . SER   B 166 ? 0.2231 0.1419 0.3099 -0.0289 -0.0726 -0.0359 166 SER   B N   
6477 C CA  . SER   B 166 ? 0.2210 0.1485 0.3670 -0.0317 -0.0706 -0.0395 166 SER   B CA  
6478 C C   . SER   B 166 ? 0.2048 0.1540 0.3945 -0.0337 -0.0734 -0.0129 166 SER   B C   
6479 O O   . SER   B 166 ? 0.2078 0.1806 0.4303 -0.0436 -0.0923 -0.0253 166 SER   B O   
6480 C CB  . SER   B 166 ? 0.2276 0.1553 0.3867 -0.0294 -0.0673 -0.0501 166 SER   B CB  
6481 O OG  . SER   B 166 ? 0.2201 0.1537 0.4106 -0.0222 -0.0651 -0.0268 166 SER   B OG  
6487 N N   . SER   B 167 ? 0.1901 0.1493 0.3731 -0.0323 -0.0728 0.0163  167 SER   B N   
6488 C CA  . SER   B 167 ? 0.1840 0.1512 0.3491 -0.0348 -0.0552 0.0178  167 SER   B CA  
6489 C C   . SER   B 167 ? 0.1769 0.1611 0.3328 -0.0419 -0.0497 0.0339  167 SER   B C   
6490 O O   . SER   B 167 ? 0.1798 0.1749 0.3139 -0.0448 -0.0391 0.0351  167 SER   B O   
6491 C CB  . SER   B 167 ? 0.1764 0.1619 0.3386 -0.0303 -0.0293 0.0201  167 SER   B CB  
6492 O OG  . SER   B 167 ? 0.1709 0.1735 0.3213 -0.0168 -0.0156 0.0190  167 SER   B OG  
6498 N N   . PHE   B 168 ? 0.1725 0.1560 0.3281 -0.0341 -0.0400 0.0445  168 PHE   B N   
6499 C CA  . PHE   B 168 ? 0.1804 0.1564 0.3082 -0.0360 -0.0318 0.0302  168 PHE   B CA  
6500 C C   . PHE   B 168 ? 0.1571 0.1472 0.2767 -0.0188 -0.0118 0.0146  168 PHE   B C   
6501 O O   . PHE   B 168 ? 0.1851 0.1445 0.2826 0.0071  -0.0187 -0.0004 168 PHE   B O   
6502 C CB  . PHE   B 168 ? 0.1977 0.1610 0.3085 -0.0465 -0.0438 0.0440  168 PHE   B CB  
6503 C CG  . PHE   B 168 ? 0.2257 0.1500 0.3004 -0.0433 -0.0469 0.0147  168 PHE   B CG  
6504 C CD1 . PHE   B 168 ? 0.2600 0.1542 0.3006 -0.0383 -0.0558 0.0102  168 PHE   B CD1 
6505 C CD2 . PHE   B 168 ? 0.2131 0.1445 0.2938 -0.0356 -0.0482 0.0160  168 PHE   B CD2 
6506 C CE1 . PHE   B 168 ? 0.2717 0.1639 0.2998 -0.0227 -0.0522 0.0111  168 PHE   B CE1 
6507 C CE2 . PHE   B 168 ? 0.2370 0.1520 0.2967 -0.0238 -0.0613 0.0071  168 PHE   B CE2 
6508 C CZ  . PHE   B 168 ? 0.2563 0.1493 0.2985 -0.0115 -0.0638 0.0214  168 PHE   B CZ  
6518 N N   . LEU   B 169 ? 0.1640 0.1686 0.2801 -0.0002 -0.0035 -0.0048 169 LEU   B N   
6519 C CA  . LEU   B 169 ? 0.1842 0.1978 0.3184 -0.0095 -0.0040 -0.0258 169 LEU   B CA  
6520 C C   . LEU   B 169 ? 0.2069 0.2219 0.3766 0.0086  -0.0120 -0.0546 169 LEU   B C   
6521 O O   . LEU   B 169 ? 0.2299 0.2446 0.4261 0.0037  -0.0086 -0.0763 169 LEU   B O   
6522 C CB  . LEU   B 169 ? 0.2011 0.2348 0.3312 -0.0193 -0.0166 -0.0012 169 LEU   B CB  
6523 C CG  . LEU   B 169 ? 0.2423 0.2718 0.3682 -0.0079 -0.0221 0.0080  169 LEU   B CG  
6524 C CD1 . LEU   B 169 ? 0.2589 0.2934 0.3774 -0.0037 -0.0268 0.0232  169 LEU   B CD1 
6525 C CD2 . LEU   B 169 ? 0.2375 0.2789 0.3739 0.0022  -0.0119 -0.0017 169 LEU   B CD2 
6526 O OXT . LEU   B 169 ? 0.2275 0.2346 0.3809 0.0355  -0.0146 -0.0531 169 LEU   B OXT 
6538 N N2  B A1A5D C .   ? 0.1228 0.1648 0.1591 0.0184  0.0156  0.0561  201 A1A5D A N2  
6539 C C3  B A1A5D C .   ? 0.1202 0.1515 0.1628 -0.0166 0.0029  0.0084  201 A1A5D A C3  
6540 C C6  B A1A5D C .   ? 0.1050 0.1540 0.1501 0.0066  0.0082  0.0526  201 A1A5D A C6  
6541 C C9  B A1A5D C .   ? 0.1288 0.1673 0.1667 0.0203  0.0153  0.0559  201 A1A5D A C9  
6542 C C12 B A1A5D C .   ? 0.1168 0.1594 0.1501 0.0104  0.0152  0.0533  201 A1A5D A C12 
6543 C C14 B A1A5D C .   ? 0.1027 0.1330 0.1432 -0.0133 0.0125  0.0110  201 A1A5D A C14 
6544 C C1  B A1A5D C .   ? 0.1229 0.1469 0.1582 -0.0123 0.0157  0.0050  201 A1A5D A C1  
6545 C C10 B A1A5D C .   ? 0.1321 0.1676 0.1631 0.0204  0.0124  0.0576  201 A1A5D A C10 
6546 C C11 B A1A5D C .   ? 0.1234 0.1611 0.1489 0.0170  0.0075  0.0649  201 A1A5D A C11 
6547 C C13 B A1A5D C .   ? 0.1127 0.1566 0.1473 0.0050  0.0124  0.0479  201 A1A5D A C13 
6548 C C2  B A1A5D C .   ? 0.1160 0.1438 0.1562 -0.0143 0.0094  0.0062  201 A1A5D A C2  
6549 C C4  B A1A5D C .   ? 0.1086 0.1531 0.1614 -0.0145 0.0088  0.0257  201 A1A5D A C4  
6550 C C5  B A1A5D C .   ? 0.1074 0.1539 0.1499 -0.0012 0.0113  0.0425  201 A1A5D A C5  
6551 C C7  B A1A5D C .   ? 0.1068 0.1527 0.1475 0.0083  0.0092  0.0610  201 A1A5D A C7  
6552 C C8  B A1A5D C .   ? 0.1144 0.1592 0.1517 0.0091  0.0208  0.0558  201 A1A5D A C8  
6553 N N1  B A1A5D C .   ? 0.1211 0.1555 0.1674 -0.0163 0.0013  0.0129  201 A1A5D A N1  
6554 O O1  B A1A5D C .   ? 0.1069 0.1476 0.1637 -0.0279 0.0161  0.0281  201 A1A5D A O1  
6555 O O2  B A1A5D C .   ? 0.1309 0.1655 0.1686 0.0232  0.0087  0.0631  201 A1A5D A O2  
6556 O O3  B A1A5D C .   ? 0.1079 0.1414 0.1564 -0.0104 0.0135  0.0083  201 A1A5D A O3  
6557 O O4  B A1A5D C .   ? 0.0853 0.1203 0.1313 -0.0106 0.0165  0.0183  201 A1A5D A O4  
6573 O O1  C A1A5E D .   ? 0.1454 0.1908 0.1705 -0.0105 0.0128  0.0189  202 A1A5E A O1  
6574 C C1  C A1A5E D .   ? 0.1626 0.1936 0.1789 0.0055  0.0223  0.0036  202 A1A5E A C1  
6575 C C2  C A1A5E D .   ? 0.1657 0.1933 0.1860 0.0059  0.0164  -0.0010 202 A1A5E A C2  
6576 C C3  C A1A5E D .   ? 0.1553 0.1917 0.1824 0.0045  0.0198  -0.0015 202 A1A5E A C3  
6577 C C4  C A1A5E D .   ? 0.1401 0.1852 0.1677 -0.0061 0.0187  0.0209  202 A1A5E A C4  
6578 C C5  C A1A5E D .   ? 0.1320 0.1819 0.1661 -0.0080 0.0241  0.0233  202 A1A5E A C5  
6579 C C6  C A1A5E D .   ? 0.1298 0.1824 0.1679 -0.0029 0.0216  0.0208  202 A1A5E A C6  
6580 C C7  C A1A5E D .   ? 0.1302 0.1847 0.1808 -0.0077 0.0200  0.0153  202 A1A5E A C7  
6581 C C8  C A1A5E D .   ? 0.1361 0.1860 0.1861 -0.0095 0.0233  0.0120  202 A1A5E A C8  
6582 C C10 C A1A5E D .   ? 0.1527 0.1919 0.2080 -0.0057 0.0177  0.0081  202 A1A5E A C10 
6583 C C11 C A1A5E D .   ? 0.1456 0.1887 0.2023 -0.0082 0.0165  0.0052  202 A1A5E A C11 
6584 C C12 C A1A5E D .   ? 0.1363 0.1851 0.1881 -0.0088 0.0179  0.0101  202 A1A5E A C12 
6585 C C13 C A1A5E D .   ? 0.1328 0.1839 0.1795 -0.0083 0.0184  0.0162  202 A1A5E A C13 
6586 C C14 C A1A5E D .   ? 0.1699 0.1891 0.1920 0.0045  0.0114  0.0022  202 A1A5E A C14 
6587 C C9  C A1A5E D .   ? 0.1556 0.1920 0.2069 -0.0065 0.0258  0.0079  202 A1A5E A C9  
6588 N N1  C A1A5E D .   ? 0.1453 0.1881 0.1752 0.0018  0.0197  0.0076  202 A1A5E A N1  
6589 N N2  C A1A5E D .   ? 0.1450 0.1877 0.1966 -0.0108 0.0259  0.0112  202 A1A5E A N2  
6590 O O2  C A1A5E D .   ? 0.1665 0.1968 0.2109 -0.0018 0.0310  0.0058  202 A1A5E A O2  
6591 O O3  C A1A5E D .   ? 0.1710 0.1865 0.1902 0.0050  0.0120  0.0063  202 A1A5E A O3  
6592 O O4  C A1A5E D .   ? 0.1729 0.1880 0.1959 -0.0000 0.0091  0.0051  202 A1A5E A O4  
6608 O O   B HOH   E .   ? 0.2028 0.4043 0.3199 -0.0698 -0.0012 0.0343  301 HOH   A O   
6609 O O   . HOH   E .   ? 0.2342 0.1631 0.2433 0.0259  -0.0443 -0.0126 302 HOH   A O   
6610 O O   . HOH   E .   ? 0.3583 0.2330 0.4164 -0.0053 -0.0205 0.0755  303 HOH   A O   
6611 O O   . HOH   E .   ? 0.4257 0.3833 0.3053 -0.0575 -0.0577 -0.0409 304 HOH   A O   
6612 O O   . HOH   E .   ? 0.3047 0.7322 0.5950 -0.0109 -0.0764 0.1271  305 HOH   A O   
6613 O O   . HOH   E .   ? 0.4209 0.7534 0.4721 -0.1217 0.1093  0.0265  306 HOH   A O   
6614 O O   . HOH   E .   ? 0.4845 0.3363 0.5322 -0.0201 0.1141  -0.0589 307 HOH   A O   
6615 O O   . HOH   E .   ? 0.6378 0.4679 0.3767 0.2025  -0.1061 0.0860  308 HOH   A O   
6616 O O   . HOH   E .   ? 0.2077 0.2014 0.2782 -0.0006 -0.0456 0.0374  309 HOH   A O   
6617 O O   . HOH   E .   ? 0.4510 0.2968 0.4007 -0.0127 0.0884  0.0613  310 HOH   A O   
6618 O O   . HOH   E .   ? 0.2833 0.2749 0.3031 -0.0462 0.0588  0.0538  311 HOH   A O   
6619 O O   . HOH   E .   ? 0.5094 0.3404 0.4986 0.0511  0.1768  -0.0651 312 HOH   A O   
6620 O O   . HOH   E .   ? 0.2949 0.3173 0.1724 -0.0293 0.0495  0.0505  313 HOH   A O   
6621 O O   . HOH   E .   ? 0.2790 0.2873 0.3213 -0.0167 0.0974  -0.0229 314 HOH   A O   
6622 O O   . HOH   E .   ? 0.5807 0.5885 0.3787 -0.1197 -0.1139 -0.0622 315 HOH   A O   
6623 O O   . HOH   E .   ? 0.2101 0.1754 0.3667 -0.0391 0.0034  -0.0240 316 HOH   A O   
6624 O O   . HOH   E .   ? 0.3349 0.4386 0.2599 -0.0210 0.0555  0.0552  317 HOH   A O   
6625 O O   . HOH   E .   ? 0.6566 0.6508 0.4576 -0.1278 0.1853  0.2142  318 HOH   A O   
6626 O O   . HOH   E .   ? 0.4644 0.5248 0.6040 0.1689  0.1226  -0.0985 319 HOH   A O   
6627 O O   . HOH   E .   ? 0.1445 0.3568 0.2715 -0.0033 0.0283  0.0670  320 HOH   A O   
6628 O O   . HOH   E .   ? 0.3723 0.3219 0.2436 -0.1346 0.0227  0.0569  321 HOH   A O   
6629 O O   . HOH   E .   ? 0.4857 0.3449 0.3284 -0.0733 0.1957  -0.0224 322 HOH   A O   
6630 O O   . HOH   E .   ? 0.6061 0.2004 0.4657 0.0685  0.0138  0.0113  323 HOH   A O   
6631 O O   . HOH   E .   ? 0.8039 0.3844 0.6171 -0.0550 -0.1353 0.0474  324 HOH   A O   
6632 O O   . HOH   E .   ? 0.1541 0.1504 0.2168 -0.0194 -0.0030 0.0077  325 HOH   A O   
6633 O O   . HOH   E .   ? 0.4812 0.2727 0.2429 0.1679  0.0253  0.0414  326 HOH   A O   
6634 O O   . HOH   E .   ? 0.1728 0.2714 0.2931 0.0207  -0.0169 -0.0269 327 HOH   A O   
6635 O O   . HOH   E .   ? 0.3047 0.2298 0.4627 -0.0259 -0.1121 0.0988  328 HOH   A O   
6636 O O   . HOH   E .   ? 0.4708 0.5392 0.3163 -0.1473 0.1436  0.0615  329 HOH   A O   
6637 O O   . HOH   E .   ? 0.3874 0.2870 0.2386 0.0186  -0.1109 0.0063  330 HOH   A O   
6638 O O   . HOH   E .   ? 0.1761 0.3426 0.4204 -0.0176 0.0179  -0.1201 331 HOH   A O   
6639 O O   . HOH   E .   ? 0.8383 0.5063 0.3394 0.0253  -0.0676 0.0844  332 HOH   A O   
6640 O O   . HOH   E .   ? 0.3142 0.1609 0.2004 0.0021  0.0246  0.0186  333 HOH   A O   
6641 O O   A HOH   E .   ? 0.2368 0.3697 0.5595 -0.0173 0.0993  0.1869  334 HOH   A O   
6642 O O   . HOH   E .   ? 0.4275 0.2077 0.4514 0.0095  -0.1535 0.0562  335 HOH   A O   
6643 O O   . HOH   E .   ? 0.2786 0.4908 0.3732 0.0781  -0.0571 0.1344  336 HOH   A O   
6644 O O   . HOH   E .   ? 0.2372 0.5405 0.3938 0.0115  -0.0544 0.0688  337 HOH   A O   
6645 O O   . HOH   E .   ? 0.3003 0.3566 0.3788 -0.0833 -0.1006 -0.0358 338 HOH   A O   
6646 O O   . HOH   E .   ? 0.3553 0.4627 0.3610 0.1935  0.0287  0.0317  339 HOH   A O   
6647 O O   . HOH   E .   ? 0.1647 0.2877 0.2432 0.0509  0.0465  0.0845  340 HOH   A O   
6648 O O   . HOH   E .   ? 0.1765 0.2072 0.1692 -0.0104 0.0043  0.0532  341 HOH   A O   
6649 O O   . HOH   E .   ? 0.5760 0.4895 0.5526 0.0968  0.2352  -0.1312 342 HOH   A O   
6650 O O   . HOH   E .   ? 0.3661 0.7155 0.4992 -0.0468 -0.1631 0.0333  343 HOH   A O   
6651 O O   . HOH   E .   ? 0.5814 0.4120 0.2831 0.0610  0.1026  0.1367  344 HOH   A O   
6652 O O   . HOH   E .   ? 0.1500 0.1814 0.2740 0.0077  -0.0150 0.0087  345 HOH   A O   
6653 O O   . HOH   E .   ? 0.4604 0.5169 0.5927 -0.0412 0.0872  0.0494  346 HOH   A O   
6654 O O   . HOH   E .   ? 0.5979 0.4374 0.4196 -0.1828 -0.1082 0.2129  347 HOH   A O   
6655 O O   . HOH   E .   ? 0.1554 0.2242 0.2121 0.0060  -0.0089 0.0480  348 HOH   A O   
6656 O O   . HOH   E .   ? 0.1500 0.1607 0.2618 0.0040  -0.0316 -0.0404 349 HOH   A O   
6657 O O   . HOH   E .   ? 0.3892 0.4345 0.4271 -0.0197 -0.1394 -0.1334 350 HOH   A O   
6658 O O   . HOH   E .   ? 0.2011 0.1923 0.3495 0.0185  0.0810  -0.0169 351 HOH   A O   
6659 O O   . HOH   E .   ? 0.2769 0.7240 0.4447 -0.0525 -0.0661 0.1994  352 HOH   A O   
6660 O O   . HOH   E .   ? 0.2643 0.4341 0.3037 -0.0492 0.0604  0.0036  353 HOH   A O   
6661 O O   . HOH   E .   ? 0.2516 0.3840 0.3433 0.0934  -0.0630 -0.0184 354 HOH   A O   
6662 O O   . HOH   E .   ? 0.3742 0.1969 0.2032 0.1052  0.0312  0.0163  355 HOH   A O   
6663 O O   . HOH   E .   ? 0.5399 0.2768 0.3823 -0.1788 0.1803  -0.0739 356 HOH   A O   
6664 O O   . HOH   E .   ? 0.3379 0.2909 0.3764 -0.1024 -0.0200 -0.0288 357 HOH   A O   
6665 O O   . HOH   E .   ? 0.3300 0.4257 0.2206 -0.1249 -0.0315 -0.0459 358 HOH   A O   
6666 O O   . HOH   E .   ? 0.2463 0.2003 0.2442 -0.0285 0.0085  -0.0176 359 HOH   A O   
6667 O O   . HOH   E .   ? 0.1357 0.1237 0.1365 -0.0049 0.0123  0.0082  360 HOH   A O   
6668 O O   . HOH   E .   ? 0.2072 0.1842 0.2272 -0.0420 0.0008  0.0286  361 HOH   A O   
6669 O O   . HOH   E .   ? 0.1839 0.1596 0.2234 0.0093  -0.0245 0.0206  362 HOH   A O   
6670 O O   . HOH   E .   ? 0.2266 0.2022 0.2405 0.0088  -0.0020 0.0393  363 HOH   A O   
6671 O O   . HOH   E .   ? 0.4009 0.2202 0.4621 -0.1084 0.0559  0.0370  364 HOH   A O   
6672 O O   . HOH   E .   ? 0.1516 0.1211 0.2173 -0.0080 0.0087  -0.0092 365 HOH   A O   
6673 O O   . HOH   E .   ? 0.2694 0.2658 0.3461 -0.0565 0.0709  -0.0022 366 HOH   A O   
6674 O O   . HOH   E .   ? 0.5494 0.3014 0.3182 -0.1142 0.1103  0.0482  367 HOH   A O   
6675 O O   . HOH   E .   ? 0.3471 0.2186 0.5101 -0.0723 -0.0548 0.0542  368 HOH   A O   
6676 O O   . HOH   E .   ? 0.2938 0.3265 0.5231 -0.0657 -0.1084 -0.0676 369 HOH   A O   
6677 O O   . HOH   E .   ? 0.1545 0.1439 0.1612 -0.0062 -0.0159 -0.0073 370 HOH   A O   
6678 O O   . HOH   E .   ? 0.1880 0.1814 0.2002 -0.0329 0.0088  0.0329  371 HOH   A O   
6679 O O   B HOH   E .   ? 0.1768 0.1519 0.1461 -0.0019 -0.0476 0.0048  372 HOH   A O   
6680 O O   . HOH   E .   ? 0.2068 0.1956 0.1686 0.0015  0.0083  0.0128  373 HOH   A O   
6681 O O   . HOH   E .   ? 0.6498 0.5038 0.4534 -0.0664 -0.0142 0.2131  374 HOH   A O   
6682 O O   . HOH   E .   ? 0.2071 0.2404 0.3528 0.0355  0.0918  -0.0345 375 HOH   A O   
6683 O O   . HOH   E .   ? 0.2449 0.3999 0.2617 0.0166  0.0399  0.1397  376 HOH   A O   
6684 O O   A HOH   E .   ? 0.2139 0.1777 0.2192 -0.0118 -0.0392 -0.0227 377 HOH   A O   
6685 O O   . HOH   E .   ? 0.2160 0.3297 0.3748 -0.0258 -0.0032 0.0593  378 HOH   A O   
6686 O O   . HOH   E .   ? 0.3489 0.6197 0.4444 0.0844  0.1164  -0.1393 379 HOH   A O   
6687 O O   . HOH   E .   ? 0.2091 0.2177 0.2090 -0.0274 -0.0418 0.0337  380 HOH   A O   
6688 O O   . HOH   E .   ? 0.5408 0.4835 0.6649 -0.0060 -0.0998 0.0351  381 HOH   A O   
6689 O O   . HOH   E .   ? 0.1538 0.1587 0.1960 -0.0029 -0.0248 0.0062  382 HOH   A O   
6690 O O   . HOH   E .   ? 0.1887 0.2617 0.2736 0.0515  0.0440  0.0921  383 HOH   A O   
6691 O O   . HOH   E .   ? 0.1353 0.1634 0.1730 0.0048  -0.0179 -0.0281 384 HOH   A O   
6692 O O   . HOH   E .   ? 0.2843 0.3592 0.3188 -0.0205 0.0996  -0.0653 385 HOH   A O   
6693 O O   . HOH   E .   ? 0.3250 0.2174 0.3529 -0.0150 -0.0414 0.0843  386 HOH   A O   
6694 O O   . HOH   E .   ? 0.2797 0.1963 0.1689 -0.0597 0.0304  0.0151  387 HOH   A O   
6695 O O   . HOH   E .   ? 0.2840 0.2836 0.2097 0.0278  0.0718  0.0091  388 HOH   A O   
6696 O O   A HOH   E .   ? 0.1888 0.3682 0.2247 0.0557  0.0303  0.0378  389 HOH   A O   
6697 O O   A HOH   E .   ? 0.2547 0.4976 0.5981 0.1007  0.0555  0.1377  390 HOH   A O   
6698 O O   . HOH   E .   ? 0.5551 0.3542 0.1959 -0.0271 0.1120  0.0423  391 HOH   A O   
6699 O O   . HOH   E .   ? 0.6323 0.4373 0.7169 -0.0810 -0.0094 -0.0797 392 HOH   A O   
6700 O O   . HOH   E .   ? 0.1394 0.1436 0.1891 0.0026  -0.0146 0.0097  393 HOH   A O   
6701 O O   . HOH   E .   ? 0.5854 0.7460 0.3706 0.1653  -0.1128 0.1798  394 HOH   A O   
6702 O O   A HOH   E .   ? 0.1904 0.2093 0.2247 -0.0206 -0.0141 0.0777  395 HOH   A O   
6703 O O   . HOH   E .   ? 0.1667 0.3043 0.3219 -0.0280 0.0570  0.0480  396 HOH   A O   
6704 O O   B HOH   E .   ? 0.3077 0.3271 0.2370 0.0083  -0.0423 0.0004  397 HOH   A O   
6705 O O   . HOH   E .   ? 0.1974 0.1847 0.3756 0.0423  0.1047  0.0990  398 HOH   A O   
6706 O O   . HOH   E .   ? 0.3142 0.2596 0.2167 -0.0655 -0.0830 0.0278  399 HOH   A O   
6707 O O   . HOH   E .   ? 0.2137 0.1652 0.2524 -0.0017 -0.0317 0.0086  400 HOH   A O   
6708 O O   . HOH   E .   ? 0.2478 0.1812 0.2429 -0.0240 0.0031  0.0135  401 HOH   A O   
6709 O O   . HOH   E .   ? 0.3684 0.5840 0.4028 -0.0604 0.0013  0.1381  402 HOH   A O   
6710 O O   . HOH   E .   ? 0.2399 0.2824 0.2923 0.0122  -0.0221 -0.0542 403 HOH   A O   
6711 O O   . HOH   E .   ? 0.5618 0.2772 0.3559 0.0970  -0.1079 -0.0580 404 HOH   A O   
6712 O O   . HOH   E .   ? 0.6946 0.3633 0.5070 0.1546  -0.0741 0.1418  405 HOH   A O   
6713 O O   . HOH   E .   ? 0.1885 0.1277 0.1584 -0.0187 0.0126  -0.0028 406 HOH   A O   
6714 O O   A HOH   E .   ? 0.3851 0.2453 0.5284 0.0715  0.0556  -0.0113 407 HOH   A O   
6715 O O   . HOH   E .   ? 0.4617 0.4986 0.5137 -0.0313 -0.0366 0.1037  408 HOH   A O   
6716 O O   . HOH   E .   ? 0.2541 0.2037 0.2453 -0.0547 0.0097  0.0491  409 HOH   A O   
6717 O O   . HOH   E .   ? 0.3213 0.5453 0.4710 -0.0658 0.0493  0.1298  410 HOH   A O   
6718 O O   . HOH   E .   ? 0.2005 0.1627 0.1492 -0.0014 0.0151  0.0102  411 HOH   A O   
6719 O O   B HOH   E .   ? 0.0695 0.1046 0.2265 0.0062  0.0189  0.0741  412 HOH   A O   
6720 O O   . HOH   E .   ? 0.7086 0.4939 0.5503 -0.1456 -0.0919 -0.1299 413 HOH   A O   
6721 O O   . HOH   E .   ? 0.4147 0.6034 0.3554 -0.0499 -0.0255 0.1339  414 HOH   A O   
6722 O O   . HOH   E .   ? 0.2012 0.2463 0.3452 -0.0169 -0.0274 0.0007  415 HOH   A O   
6723 O O   . HOH   E .   ? 0.6392 0.6273 0.4087 0.2038  -0.0824 -0.0438 416 HOH   A O   
6724 O O   . HOH   E .   ? 0.6247 0.6781 0.5717 0.0741  0.0522  0.0061  417 HOH   A O   
6725 O O   A HOH   E .   ? 0.2203 0.2349 0.3920 -0.0167 0.0948  -0.0306 418 HOH   A O   
6726 O O   . HOH   E .   ? 0.2259 0.2740 0.2365 -0.0113 -0.0631 0.0385  419 HOH   A O   
6727 O O   . HOH   E .   ? 0.3287 0.3690 0.7406 -0.0049 0.1151  -0.0296 420 HOH   A O   
6728 O O   . HOH   E .   ? 0.5975 0.7492 0.4489 0.0980  0.2661  -0.1272 421 HOH   A O   
6729 O O   . HOH   E .   ? 0.1551 0.1978 0.2919 -0.0132 0.0065  0.0343  422 HOH   A O   
6730 O O   . HOH   E .   ? 0.3239 0.4087 0.4283 -0.0611 0.1290  -0.0356 423 HOH   A O   
6731 O O   . HOH   E .   ? 0.1525 0.1716 0.2714 -0.0021 -0.0032 0.0206  424 HOH   A O   
6732 O O   . HOH   E .   ? 0.2095 0.2133 0.3306 0.0050  -0.0263 -0.0329 425 HOH   A O   
6733 O O   . HOH   E .   ? 0.3238 0.1261 0.2192 0.0018  -0.0476 0.0078  426 HOH   A O   
6734 O O   . HOH   E .   ? 0.3935 0.4360 0.3110 0.1500  -0.0856 -0.1307 427 HOH   A O   
6735 O O   . HOH   E .   ? 0.5402 0.4749 0.2743 0.0518  -0.1407 0.0129  428 HOH   A O   
6736 O O   . HOH   E .   ? 0.2959 0.5351 0.1651 -0.0607 0.0515  -0.0277 429 HOH   A O   
6737 O O   . HOH   E .   ? 0.2355 0.4239 0.2422 0.1454  -0.0187 0.0242  430 HOH   A O   
6738 O O   . HOH   E .   ? 0.4366 0.2168 0.4834 -0.0866 -0.2166 0.1015  431 HOH   A O   
6739 O O   A HOH   E .   ? 0.3453 0.2240 0.3650 0.0456  0.0637  0.1031  432 HOH   A O   
6740 O O   . HOH   E .   ? 0.7002 0.7030 0.5614 0.1671  -0.1256 0.0491  433 HOH   A O   
6741 O O   A HOH   E .   ? 0.2111 0.1782 0.2986 0.0444  -0.0866 -0.0032 434 HOH   A O   
6742 O O   . HOH   E .   ? 0.4373 0.2561 0.6440 0.0410  -0.0585 -0.0775 435 HOH   A O   
6743 O O   . HOH   E .   ? 0.4620 0.2728 0.2570 -0.0102 0.0429  0.0346  436 HOH   A O   
6744 O O   . HOH   E .   ? 0.7174 0.7384 0.4949 -0.1248 0.0205  0.0562  437 HOH   A O   
6745 O O   B HOH   E .   ? 0.1915 0.1227 0.0910 -0.0152 -0.0671 0.0122  438 HOH   A O   
6746 O O   . HOH   E .   ? 0.3238 0.3434 0.5508 -0.0220 0.1684  -0.1342 439 HOH   A O   
6747 O O   . HOH   E .   ? 0.1931 0.1446 0.1743 -0.0014 -0.0158 -0.0042 440 HOH   A O   
6748 O O   A HOH   E .   ? 0.2070 0.1644 0.1867 0.0186  -0.0851 -0.0214 441 HOH   A O   
6749 O O   . HOH   E .   ? 0.2418 0.1532 0.2526 0.0030  -0.0036 -0.0004 442 HOH   A O   
6750 O O   . HOH   E .   ? 0.6399 0.6341 0.5896 -0.1466 0.0467  -0.1244 443 HOH   A O   
6751 O O   . HOH   E .   ? 0.4727 0.4289 0.4842 -0.1232 -0.1135 -0.1223 444 HOH   A O   
6752 O O   . HOH   E .   ? 0.3833 0.2739 0.1719 -0.1016 0.0418  0.0410  445 HOH   A O   
6753 O O   . HOH   E .   ? 0.5994 0.4621 0.7529 0.0258  -0.1358 0.1389  446 HOH   A O   
6754 O O   . HOH   E .   ? 0.3897 0.3167 0.3168 0.1952  -0.0634 -0.0540 447 HOH   A O   
6755 O O   . HOH   E .   ? 0.2601 0.1843 0.2546 0.0084  0.0390  0.0137  448 HOH   A O   
6756 O O   . HOH   E .   ? 0.2282 0.2525 0.2441 -0.0013 -0.0232 -0.0486 449 HOH   A O   
6757 O O   . HOH   E .   ? 0.8615 0.8079 0.6522 -0.0441 -0.0103 -0.0719 450 HOH   A O   
6758 O O   . HOH   E .   ? 0.1801 0.2220 0.5133 -0.0279 -0.0725 0.0758  451 HOH   A O   
6759 O O   B HOH   E .   ? 0.3804 0.3785 0.2237 0.1509  -0.0020 0.0381  452 HOH   A O   
6760 O O   A HOH   E .   ? 0.5588 0.3241 0.3871 0.1994  0.1254  0.1329  453 HOH   A O   
6761 O O   . HOH   E .   ? 0.5534 0.2930 0.5128 -0.0266 -0.0006 0.1141  454 HOH   A O   
6762 O O   . HOH   E .   ? 0.5026 0.4571 0.4127 0.0271  -0.0250 0.1297  455 HOH   A O   
6763 O O   . HOH   E .   ? 0.2538 0.3918 0.4432 0.0557  -0.0202 0.1671  456 HOH   A O   
6764 O O   . HOH   E .   ? 0.5525 0.3627 0.5561 0.0127  -0.0143 0.0788  457 HOH   A O   
6765 O O   . HOH   E .   ? 0.6710 0.5348 0.4695 -0.0984 0.1682  0.0332  458 HOH   A O   
6766 O O   . HOH   E .   ? 0.2910 0.2635 0.3312 -0.0570 0.0113  -0.0592 459 HOH   A O   
6767 O O   . HOH   E .   ? 0.3197 0.4486 0.5411 -0.1414 0.0651  -0.1906 460 HOH   A O   
6768 O O   . HOH   E .   ? 0.6568 0.7823 0.4667 -0.0443 -0.0597 -0.0134 461 HOH   A O   
6769 O O   . HOH   E .   ? 0.3568 0.4659 0.4990 0.1027  -0.0251 0.1515  462 HOH   A O   
6770 O O   . HOH   E .   ? 0.6848 0.3621 0.7688 -0.0056 0.0402  0.2628  463 HOH   A O   
6771 O O   . HOH   E .   ? 0.3052 0.1762 0.2626 0.0351  -0.0958 -0.0327 464 HOH   A O   
6772 O O   . HOH   E .   ? 0.4390 0.5602 0.3863 -0.1094 -0.0498 0.1896  465 HOH   A O   
6773 O O   . HOH   E .   ? 0.2876 0.2976 0.3741 -0.1310 0.0842  -0.0748 466 HOH   A O   
6774 O O   B HOH   E .   ? 0.2008 0.2805 0.2269 -0.0353 -0.0115 0.1019  467 HOH   A O   
6775 O O   . HOH   E .   ? 0.2778 0.2515 0.5104 0.0621  -0.1412 -0.0668 468 HOH   A O   
6776 O O   . HOH   E .   ? 0.2355 0.3918 0.4461 -0.0281 -0.0164 -0.0349 469 HOH   A O   
6777 O O   . HOH   E .   ? 0.3079 0.3879 0.6468 0.0676  0.0778  -0.1835 470 HOH   A O   
6778 O O   B HOH   E .   ? 0.2056 0.2501 0.2494 -0.0168 0.0465  -0.0016 471 HOH   A O   
6779 O O   . HOH   E .   ? 0.3559 0.2306 0.4451 -0.0052 0.1092  -0.0151 472 HOH   A O   
6780 O O   . HOH   E .   ? 0.7228 0.4938 0.4560 0.0766  0.1779  0.0898  473 HOH   A O   
6781 O O   . HOH   E .   ? 0.7831 0.5450 0.6176 0.1592  0.1799  0.1567  474 HOH   A O   
6782 O O   . HOH   E .   ? 0.3764 0.6139 0.3536 0.0656  -0.0459 -0.0827 475 HOH   A O   
6783 O O   . HOH   E .   ? 0.5940 0.6912 0.6663 -0.1451 -0.1012 0.0205  476 HOH   A O   
6784 O O   . HOH   E .   ? 0.4777 0.5061 0.5422 -0.2124 -0.0919 -0.0347 477 HOH   A O   
6785 O O   . HOH   E .   ? 0.4468 0.4272 0.2471 -0.0581 0.0055  0.0005  478 HOH   A O   
6786 O O   . HOH   E .   ? 0.4222 0.5732 0.4693 0.1220  -0.0437 -0.1022 479 HOH   A O   
6787 O O   . HOH   E .   ? 0.4726 0.4231 0.3239 -0.0794 -0.0971 -0.0311 480 HOH   A O   
6788 O O   . HOH   E .   ? 0.7813 0.3979 0.3061 -0.0815 -0.1074 0.0238  481 HOH   A O   
6789 O O   . HOH   E .   ? 0.2321 0.2359 0.2565 0.0138  0.0051  -0.0038 482 HOH   A O   
6790 O O   B HOH   E .   ? 0.1622 0.1518 0.2083 0.0594  0.0025  0.0800  483 HOH   A O   
6791 O O   . HOH   E .   ? 0.6107 0.4581 0.6726 -0.0985 0.0218  -0.0808 484 HOH   A O   
6792 O O   . HOH   E .   ? 0.5203 0.4669 0.4138 -0.0355 -0.0563 -0.0601 485 HOH   A O   
6793 O O   . HOH   E .   ? 0.6272 0.4411 0.3801 0.0968  0.0380  -0.1361 486 HOH   A O   
6794 O O   . HOH   E .   ? 0.4685 0.2738 0.3270 -0.0701 -0.0756 0.0684  487 HOH   A O   
6795 O O   . HOH   E .   ? 0.2436 0.3955 0.4477 0.0203  0.0669  0.1166  488 HOH   A O   
6796 O O   . HOH   E .   ? 0.2790 0.5347 0.3635 0.1296  0.0949  0.2441  489 HOH   A O   
6797 O O   . HOH   E .   ? 0.4479 0.3904 0.5713 -0.0955 -0.1244 0.0633  490 HOH   A O   
6798 O O   . HOH   E .   ? 0.5358 0.4104 0.3962 0.0214  0.1208  0.0183  491 HOH   A O   
6799 O O   . HOH   E .   ? 0.5287 0.7060 0.4502 -0.1336 0.0832  0.0858  492 HOH   A O   
6800 O O   . HOH   E .   ? 0.2937 0.2524 0.6727 -0.0074 -0.1219 0.0338  493 HOH   A O   
6801 O O   . HOH   E .   ? 0.4212 0.3636 0.2590 -0.0745 0.1286  -0.0452 494 HOH   A O   
6802 O O   . HOH   E .   ? 0.5172 0.3233 0.5248 -0.0357 0.2542  0.0138  495 HOH   A O   
6803 O O   . HOH   E .   ? 0.2745 0.2186 0.5468 0.0219  0.0516  0.1184  496 HOH   A O   
6804 O O   . HOH   E .   ? 0.5152 0.6010 0.6135 0.1085  0.1132  -0.1159 497 HOH   A O   
6805 O O   . HOH   E .   ? 0.2527 0.3260 0.4898 -0.0254 0.0936  -0.0568 498 HOH   A O   
6806 O O   . HOH   E .   ? 0.3886 0.2941 0.4259 -0.0859 0.0447  0.0699  499 HOH   A O   
6807 O O   . HOH   E .   ? 0.6425 0.2596 0.4411 -0.0706 0.0086  0.0830  500 HOH   A O   
6808 O O   . HOH   E .   ? 0.3248 0.4425 0.3355 -0.0456 0.0103  -0.0979 501 HOH   A O   
6809 O O   . HOH   E .   ? 0.4011 0.8662 0.5120 -0.0960 -0.0573 0.3056  502 HOH   A O   
6810 O O   . HOH   E .   ? 0.5047 0.2146 0.4059 -0.1187 0.0019  0.0260  503 HOH   A O   
6811 O O   . HOH   E .   ? 0.2775 0.3089 0.3961 0.0613  -0.0745 0.0407  504 HOH   A O   
6812 O O   . HOH   E .   ? 0.5078 0.6914 0.5693 0.0584  -0.0993 0.1331  505 HOH   A O   
6813 O O   . HOH   E .   ? 0.3423 0.3951 0.3628 0.0807  0.0139  0.0291  506 HOH   A O   
6814 O O   . HOH   E .   ? 0.6746 0.6537 0.5142 0.0530  -0.1436 0.1229  507 HOH   A O   
6815 O O   . HOH   E .   ? 0.6114 0.4426 0.5176 0.0366  0.1511  0.0217  508 HOH   A O   
6816 O O   . HOH   E .   ? 0.2713 0.2357 0.4108 -0.0084 0.0032  0.0616  509 HOH   A O   
6817 O O   . HOH   E .   ? 0.5480 0.6719 0.4748 0.3331  0.0169  0.1185  510 HOH   A O   
6818 O O   . HOH   E .   ? 0.4680 0.4530 0.4362 -0.0002 -0.0265 -0.1274 511 HOH   A O   
6819 O O   B HOH   E .   ? 0.2670 0.1464 0.2222 0.0666  -0.0097 0.0393  512 HOH   A O   
6820 O O   A HOH   E .   ? 0.3313 0.8798 0.4065 0.0936  0.1233  -0.0077 513 HOH   A O   
6821 O O   . HOH   E .   ? 0.2854 0.6967 0.3477 0.0576  0.0323  -0.0144 514 HOH   A O   
6822 O O   . HOH   E .   ? 0.4730 0.5219 0.4881 0.1430  -0.1004 0.1240  515 HOH   A O   
6823 O O   . HOH   E .   ? 0.4444 0.6487 0.5664 -0.0815 -0.1018 -0.0055 516 HOH   A O   
6824 O O   . HOH   E .   ? 0.3757 0.4650 0.5513 -0.0606 -0.1142 0.2778  517 HOH   A O   
6825 O O   . HOH   F .   ? 0.2312 0.2141 0.3040 0.0270  0.0741  0.0437  201 HOH   B O   
6826 O O   . HOH   F .   ? 0.5415 0.4601 0.2764 0.0746  -0.0308 -0.1180 202 HOH   B O   
6827 O O   . HOH   F .   ? 0.4965 0.3925 0.5930 0.0344  -0.1203 0.2459  203 HOH   B O   
6828 O O   . HOH   F .   ? 0.4516 0.6201 0.4124 0.2679  -0.1078 0.0201  204 HOH   B O   
6829 O O   . HOH   F .   ? 0.6332 0.6346 0.5852 0.2476  0.0094  0.1152  205 HOH   B O   
6830 O O   . HOH   F .   ? 0.4614 0.3144 0.3414 -0.0269 0.0096  -0.1171 206 HOH   B O   
6831 O O   . HOH   F .   ? 0.3486 0.7082 0.3735 0.0533  -0.0117 0.2679  207 HOH   B O   
6832 O O   . HOH   F .   ? 0.3181 0.5880 0.5389 -0.0167 0.1992  -0.1462 208 HOH   B O   
6833 O O   . HOH   F .   ? 0.2950 0.2993 0.7052 0.0791  -0.1425 0.0281  209 HOH   B O   
6834 O O   . HOH   F .   ? 0.6547 0.3258 0.4145 -0.1995 0.0649  0.0585  210 HOH   B O   
6835 O O   . HOH   F .   ? 0.2120 0.2431 0.2530 0.0165  0.0080  -0.0322 211 HOH   B O   
6836 O O   . HOH   F .   ? 0.7253 0.3578 0.4950 0.0241  0.1516  -0.0181 212 HOH   B O   
6837 O O   . HOH   F .   ? 0.6180 0.3841 0.4096 -0.0813 -0.1305 0.0839  213 HOH   B O   
6838 O O   . HOH   F .   ? 0.3568 0.3915 0.6616 -0.0837 0.0672  -0.0810 214 HOH   B O   
6839 O O   . HOH   F .   ? 0.4416 0.5638 0.4669 0.2759  -0.0053 0.0942  215 HOH   B O   
6840 O O   . HOH   F .   ? 0.2467 0.2604 0.5563 -0.0142 0.0671  0.0409  216 HOH   B O   
6841 O O   . HOH   F .   ? 0.2893 0.2025 0.5340 0.0259  0.1593  0.1045  217 HOH   B O   
6842 O O   . HOH   F .   ? 0.1516 0.1795 0.2838 -0.0157 -0.0032 0.0018  218 HOH   B O   
6843 O O   . HOH   F .   ? 0.4584 0.1958 0.4202 -0.0251 -0.1109 0.0218  219 HOH   B O   
6844 O O   . HOH   F .   ? 0.5299 0.4601 0.6377 -0.0230 -0.1450 -0.1258 220 HOH   B O   
6845 O O   . HOH   F .   ? 0.3481 0.6620 0.3658 0.2057  0.0029  -0.0644 221 HOH   B O   
6846 O O   . HOH   F .   ? 0.3039 0.4518 0.5986 0.0621  -0.1089 0.0843  222 HOH   B O   
6847 O O   . HOH   F .   ? 0.2716 0.5496 0.4030 0.1222  0.0097  -0.0902 223 HOH   B O   
6848 O O   . HOH   F .   ? 0.3484 0.4240 0.5172 -0.1608 -0.0204 0.0673  224 HOH   B O   
6849 O O   . HOH   F .   ? 0.3606 0.4341 0.4115 -0.0051 0.0909  -0.1166 225 HOH   B O   
6850 O O   . HOH   F .   ? 0.3029 0.2079 0.4115 0.0043  0.1430  0.0146  226 HOH   B O   
6851 O O   . HOH   F .   ? 0.3909 0.4404 0.6103 -0.0982 -0.0805 -0.1526 227 HOH   B O   
6852 O O   . HOH   F .   ? 0.6515 0.3822 0.5749 0.0767  -0.0148 -0.0746 228 HOH   B O   
6853 O O   . HOH   F .   ? 0.6369 0.5892 0.3132 0.1561  -0.0480 0.0403  229 HOH   B O   
6854 O O   . HOH   F .   ? 0.2524 0.1762 0.2880 -0.0378 0.1045  -0.0087 230 HOH   B O   
6855 O O   . HOH   F .   ? 0.1571 0.1996 0.2778 -0.0090 -0.0005 -0.0019 231 HOH   B O   
6856 O O   . HOH   F .   ? 0.2707 0.4634 0.4155 -0.1112 0.0368  -0.0233 232 HOH   B O   
6857 O O   . HOH   F .   ? 0.2785 0.2354 0.3180 0.0352  0.0185  -0.0746 233 HOH   B O   
6858 O O   . HOH   F .   ? 0.2109 0.2118 0.3757 -0.0312 -0.0273 -0.0572 234 HOH   B O   
6859 O O   . HOH   F .   ? 0.3629 0.1717 0.2130 0.0019  -0.0741 0.0008  235 HOH   B O   
6860 O O   . HOH   F .   ? 0.3571 0.3499 0.2466 0.0408  0.0579  0.0448  236 HOH   B O   
6861 O O   . HOH   F .   ? 0.2155 0.1259 0.3506 0.0110  -0.0738 -0.0265 237 HOH   B O   
6862 O O   . HOH   F .   ? 0.3952 0.2269 0.4025 0.0742  -0.0345 -0.0686 238 HOH   B O   
6863 O O   . HOH   F .   ? 0.1487 0.1438 0.1758 -0.0168 -0.0057 0.0043  239 HOH   B O   
6864 O O   . HOH   F .   ? 0.2165 0.1991 0.2217 -0.0291 -0.0489 0.0099  240 HOH   B O   
6865 O O   . HOH   F .   ? 0.2013 0.2117 0.3122 -0.0431 -0.0007 -0.0358 241 HOH   B O   
6866 O O   . HOH   F .   ? 0.2265 0.3568 0.2818 -0.0412 -0.0563 -0.0379 242 HOH   B O   
6867 O O   . HOH   F .   ? 0.1955 0.4220 0.2409 -0.0347 -0.0301 0.0722  243 HOH   B O   
6868 O O   . HOH   F .   ? 0.1411 0.1263 0.1697 -0.0050 -0.0087 0.0082  244 HOH   B O   
6869 O O   . HOH   F .   ? 0.1571 0.1444 0.2724 -0.0085 0.0007  -0.0173 245 HOH   B O   
6870 O O   . HOH   F .   ? 0.2878 0.4784 0.3989 -0.1138 -0.0447 -0.0995 246 HOH   B O   
6871 O O   . HOH   F .   ? 0.4201 0.2992 0.3593 -0.0716 0.0449  -0.0632 247 HOH   B O   
6872 O O   . HOH   F .   ? 0.2152 0.2079 0.1951 0.0064  -0.0081 -0.0011 248 HOH   B O   
6873 O O   . HOH   F .   ? 0.2896 0.1674 0.5941 -0.0122 -0.1251 -0.0321 249 HOH   B O   
6874 O O   . HOH   F .   ? 0.6161 0.3099 0.2413 0.0511  0.0598  -0.0287 250 HOH   B O   
6875 O O   . HOH   F .   ? 0.2031 0.1428 0.2032 -0.0238 -0.0319 0.0249  251 HOH   B O   
6876 O O   . HOH   F .   ? 0.3538 0.3413 0.3816 0.0569  -0.1028 -0.1515 252 HOH   B O   
6877 O O   . HOH   F .   ? 0.5440 0.2845 0.3948 -0.2118 0.0085  -0.0097 253 HOH   B O   
6878 O O   . HOH   F .   ? 0.2912 0.2238 0.2955 0.0894  0.0825  0.0177  254 HOH   B O   
6879 O O   . HOH   F .   ? 0.3032 0.3209 0.2083 0.0550  0.0514  0.0059  255 HOH   B O   
6880 O O   . HOH   F .   ? 0.2896 0.2309 0.2996 -0.0193 -0.0008 -0.0555 256 HOH   B O   
6881 O O   . HOH   F .   ? 0.1603 0.1652 0.2673 -0.0163 -0.0241 0.0057  257 HOH   B O   
6882 O O   . HOH   F .   ? 0.1378 0.1585 0.2063 -0.0073 -0.0004 0.0057  258 HOH   B O   
6883 O O   . HOH   F .   ? 0.4132 0.4372 0.2591 0.0609  0.0065  -0.1426 259 HOH   B O   
6884 O O   . HOH   F .   ? 0.2533 0.1914 0.2868 -0.0654 0.0056  -0.0103 260 HOH   B O   
6885 O O   . HOH   F .   ? 0.2788 0.4152 0.5215 0.0304  0.0283  -0.1253 261 HOH   B O   
6886 O O   . HOH   F .   ? 0.2213 0.3277 0.2344 -0.0550 0.0232  0.0530  262 HOH   B O   
6887 O O   . HOH   F .   ? 0.1822 0.1712 0.1713 -0.0407 -0.0412 0.0113  263 HOH   B O   
6888 O O   . HOH   F .   ? 0.2393 0.3590 0.5604 0.0953  -0.0770 -0.1088 264 HOH   B O   
6889 O O   . HOH   F .   ? 0.2408 0.2018 0.1971 0.0078  -0.0151 0.0058  265 HOH   B O   
6890 O O   . HOH   F .   ? 0.1728 0.1362 0.4360 -0.0078 -0.0253 -0.0079 266 HOH   B O   
6891 O O   . HOH   F .   ? 0.2055 0.1414 0.2338 -0.0224 -0.0251 0.0120  267 HOH   B O   
6892 O O   . HOH   F .   ? 0.2334 0.2210 0.2490 0.0802  -0.0762 -0.0640 268 HOH   B O   
6893 O O   . HOH   F .   ? 0.4168 0.2463 0.4822 -0.0217 -0.1290 -0.0724 269 HOH   B O   
6894 O O   . HOH   F .   ? 0.2195 0.1836 0.3376 -0.0051 -0.0651 -0.0386 270 HOH   B O   
6895 O O   . HOH   F .   ? 0.2447 0.3633 0.3599 0.0104  0.0921  0.0155  271 HOH   B O   
6896 O O   . HOH   F .   ? 0.3091 0.5164 0.3981 -0.0569 -0.1113 0.1568  272 HOH   B O   
6897 O O   . HOH   F .   ? 0.2592 0.4179 0.3227 -0.0822 0.0535  -0.1510 273 HOH   B O   
6898 O O   . HOH   F .   ? 0.2458 0.7742 0.2789 0.0686  -0.0243 -0.0908 274 HOH   B O   
6899 O O   . HOH   F .   ? 0.2451 0.3113 0.2144 0.1118  -0.0178 -0.0155 275 HOH   B O   
6900 O O   . HOH   F .   ? 0.3064 0.7768 0.7783 0.1852  -0.0704 -0.1295 276 HOH   B O   
6901 O O   . HOH   F .   ? 0.2500 0.2484 0.2564 -0.0440 -0.0704 -0.0247 277 HOH   B O   
6902 O O   . HOH   F .   ? 0.1571 0.1546 0.3277 -0.0139 0.0044  -0.0081 278 HOH   B O   
6903 O O   . HOH   F .   ? 0.3880 0.5292 0.5779 -0.0152 -0.1383 0.0271  279 HOH   B O   
6904 O O   . HOH   F .   ? 0.2612 0.3232 0.5037 -0.0227 -0.0449 -0.1516 280 HOH   B O   
6905 O O   . HOH   F .   ? 0.1936 0.4211 0.4873 -0.0474 -0.0236 -0.1630 281 HOH   B O   
6906 O O   . HOH   F .   ? 0.4663 0.6421 0.2592 0.1084  0.0208  0.1088  282 HOH   B O   
6907 O O   . HOH   F .   ? 0.2919 0.7583 0.2931 0.0845  -0.0599 0.0807  283 HOH   B O   
6908 O O   . HOH   F .   ? 0.4561 0.3059 0.4963 -0.1213 -0.0306 0.1070  284 HOH   B O   
6909 O O   . HOH   F .   ? 0.3771 0.3708 0.4516 0.1361  -0.0961 -0.0952 285 HOH   B O   
6910 O O   . HOH   F .   ? 0.2455 0.2171 0.5171 0.0145  0.0671  0.0413  286 HOH   B O   
6911 O O   . HOH   F .   ? 0.5243 0.3912 0.2491 0.1351  -0.1197 0.0413  287 HOH   B O   
6912 O O   . HOH   F .   ? 0.1590 0.1427 0.1790 0.0008  -0.0004 0.0003  288 HOH   B O   
6913 O O   . HOH   F .   ? 0.2713 0.2787 0.2478 -0.0431 -0.0890 0.0122  289 HOH   B O   
6914 O O   . HOH   F .   ? 0.2357 0.2605 0.2773 0.0154  -0.0746 0.0160  290 HOH   B O   
6915 O O   . HOH   F .   ? 0.5764 0.3782 0.2960 0.2553  0.0926  0.0909  291 HOH   B O   
6916 O O   . HOH   F .   ? 0.1592 0.3026 0.4741 0.0178  -0.0076 -0.1137 292 HOH   B O   
6917 O O   . HOH   F .   ? 0.1561 0.2045 0.1617 -0.0163 -0.0215 0.0061  293 HOH   B O   
6918 O O   . HOH   F .   ? 0.1776 0.1538 0.2398 0.0045  -0.0041 0.0063  294 HOH   B O   
6919 O O   . HOH   F .   ? 0.3526 0.3013 0.2078 0.0434  -0.0677 -0.0171 295 HOH   B O   
6920 O O   . HOH   F .   ? 0.3057 0.2736 0.2867 0.0062  -0.0013 -0.1252 296 HOH   B O   
6921 O O   . HOH   F .   ? 0.1976 0.2543 0.5585 0.0418  -0.0410 -0.0733 297 HOH   B O   
6922 O O   . HOH   F .   ? 0.3749 0.2063 0.4039 -0.0874 -0.2036 0.0589  298 HOH   B O   
6923 O O   . HOH   F .   ? 0.2131 0.1482 0.2629 -0.0173 -0.0301 -0.0068 299 HOH   B O   
6924 O O   . HOH   F .   ? 0.4991 0.4192 0.2483 0.1285  -0.0663 -0.0345 300 HOH   B O   
6925 O O   . HOH   F .   ? 0.2464 0.4512 0.5000 -0.0769 -0.1180 0.1045  301 HOH   B O   
6926 O O   . HOH   F .   ? 0.3508 0.1806 0.3338 0.0675  0.1125  0.0404  302 HOH   B O   
6927 O O   . HOH   F .   ? 0.1543 0.1908 0.2763 0.0171  -0.0107 0.0152  303 HOH   B O   
6928 O O   . HOH   F .   ? 0.2930 0.2867 0.5238 -0.0110 -0.0643 0.1156  304 HOH   B O   
6929 O O   . HOH   F .   ? 0.2799 0.2686 0.3887 -0.0746 0.1012  -0.0459 305 HOH   B O   
6930 O O   . HOH   F .   ? 0.2579 0.3022 0.3892 -0.0365 -0.1181 0.0758  306 HOH   B O   
6931 O O   . HOH   F .   ? 0.4934 0.3221 0.2620 -0.1830 0.0705  -0.0038 307 HOH   B O   
6932 O O   . HOH   F .   ? 0.7440 0.4132 0.4799 0.1853  0.0701  -0.0152 308 HOH   B O   
6933 O O   . HOH   F .   ? 0.4238 0.2269 0.2840 0.1534  0.1000  0.0297  309 HOH   B O   
6934 O O   . HOH   F .   ? 0.2692 0.2872 0.3233 -0.0474 0.0723  -0.0695 310 HOH   B O   
6935 O O   . HOH   F .   ? 0.2088 0.1517 0.3319 0.0339  -0.1001 0.0005  311 HOH   B O   
6936 O O   . HOH   F .   ? 0.1614 0.1460 0.2893 0.0045  -0.0074 -0.0062 312 HOH   B O   
6937 O O   . HOH   F .   ? 0.1548 0.1876 0.2576 -0.0257 -0.0179 0.0055  313 HOH   B O   
6938 O O   . HOH   F .   ? 0.3941 0.4606 0.1837 -0.0461 0.0390  0.0205  314 HOH   B O   
6939 O O   . HOH   F .   ? 0.2379 0.1432 0.2468 -0.0117 -0.0155 0.0269  315 HOH   B O   
6940 O O   . HOH   F .   ? 0.6170 0.5178 0.4583 -0.1212 -0.0319 0.1001  316 HOH   B O   
6941 O O   . HOH   F .   ? 0.3554 0.3729 0.7167 0.0763  -0.0358 0.0693  317 HOH   B O   
6942 O O   . HOH   F .   ? 0.2384 0.3071 0.5004 -0.0192 -0.0575 -0.0023 318 HOH   B O   
6943 O O   . HOH   F .   ? 0.4499 0.3078 0.5678 0.1117  0.2375  0.1854  319 HOH   B O   
6944 O O   . HOH   F .   ? 0.1552 0.1627 0.2917 -0.0103 -0.0184 -0.0148 320 HOH   B O   
6945 O O   . HOH   F .   ? 0.2103 0.1935 0.1890 -0.0089 0.0164  0.0195  321 HOH   B O   
6946 O O   . HOH   F .   ? 0.1748 0.2930 0.2430 -0.0263 -0.0287 0.0789  322 HOH   B O   
6947 O O   . HOH   F .   ? 0.4491 0.5100 0.2295 0.0877  -0.0615 -0.0924 323 HOH   B O   
6948 O O   . HOH   F .   ? 0.2550 0.2104 0.2512 0.0065  -0.0253 0.0251  324 HOH   B O   
6949 O O   . HOH   F .   ? 0.7686 0.1934 0.2659 0.0118  -0.0286 0.0056  325 HOH   B O   
6950 O O   . HOH   F .   ? 0.6059 0.5045 0.5929 0.0954  -0.1361 0.2159  326 HOH   B O   
6951 O O   . HOH   F .   ? 0.2061 0.1957 0.2940 0.0277  0.0404  0.0302  327 HOH   B O   
6952 O O   . HOH   F .   ? 0.3047 0.3428 0.7561 -0.0361 -0.0828 0.1995  328 HOH   B O   
6953 O O   . HOH   F .   ? 0.7196 0.6612 0.5074 0.3572  -0.0303 -0.0787 329 HOH   B O   
6954 O O   . HOH   F .   ? 0.6086 0.3260 0.3287 -0.0564 0.0862  0.0966  330 HOH   B O   
6955 O O   . HOH   F .   ? 0.2416 0.2027 0.5012 0.0004  0.0066  0.0336  331 HOH   B O   
6956 O O   . HOH   F .   ? 0.1711 0.2822 0.3061 0.0179  -0.0071 -0.0657 332 HOH   B O   
6957 O O   . HOH   F .   ? 0.4799 0.5405 0.3149 -0.0353 -0.1075 0.0372  333 HOH   B O   
6958 O O   . HOH   F .   ? 0.5124 0.2356 0.2904 0.0530  0.0176  0.0749  334 HOH   B O   
6959 O O   . HOH   F .   ? 0.2274 0.6219 0.5523 -0.0834 0.0133  0.0162  335 HOH   B O   
6960 O O   . HOH   F .   ? 0.1706 0.1411 0.2399 0.0044  -0.0294 0.0048  336 HOH   B O   
6961 O O   . HOH   F .   ? 0.2423 0.2227 0.5532 -0.0375 0.0207  0.1407  337 HOH   B O   
6962 O O   . HOH   F .   ? 0.6019 0.3179 0.3791 0.0234  0.0446  -0.1454 338 HOH   B O   
6963 O O   . HOH   F .   ? 0.5734 0.4445 0.6155 -0.0815 -0.0040 -0.1322 339 HOH   B O   
6964 O O   . HOH   F .   ? 0.4899 0.3090 0.2994 0.0506  -0.1153 -0.0559 340 HOH   B O   
6965 O O   . HOH   F .   ? 0.4339 0.6521 0.3094 -0.0056 -0.0375 0.1370  341 HOH   B O   
6966 O O   . HOH   F .   ? 0.2286 0.7003 0.6986 0.0681  -0.1000 0.0109  342 HOH   B O   
6967 O O   . HOH   F .   ? 0.3736 0.6185 0.3725 -0.0720 -0.1015 -0.0911 343 HOH   B O   
6968 O O   . HOH   F .   ? 0.2133 0.1900 0.2996 -0.0119 0.0483  -0.0003 344 HOH   B O   
6969 O O   . HOH   F .   ? 0.4191 0.5032 0.4630 0.0349  -0.0707 0.0761  345 HOH   B O   
6970 O O   . HOH   F .   ? 0.2621 0.6039 0.3638 0.1767  -0.0446 -0.1468 346 HOH   B O   
6971 O O   . HOH   F .   ? 0.4752 0.5502 0.4654 -0.1236 0.0504  0.0806  347 HOH   B O   
6972 O O   . HOH   F .   ? 0.2816 0.2246 0.5126 -0.0232 -0.1002 -0.0565 348 HOH   B O   
6973 O O   . HOH   F .   ? 0.6888 0.5972 0.2722 0.0012  -0.0972 0.1473  349 HOH   B O   
6974 O O   . HOH   F .   ? 0.4068 0.5485 0.6471 -0.0015 -0.0114 -0.1145 350 HOH   B O   
6975 O O   . HOH   F .   ? 0.2034 0.3994 0.6127 0.0379  0.0419  0.0544  351 HOH   B O   
6976 O O   . HOH   F .   ? 0.5445 0.3760 0.4249 0.1209  0.1413  -0.0329 352 HOH   B O   
6977 O O   . HOH   F .   ? 0.3772 0.2066 0.3671 -0.0794 0.0117  -0.0839 353 HOH   B O   
6978 O O   . HOH   F .   ? 0.3362 0.3922 0.4858 -0.1438 -0.0029 -0.0186 354 HOH   B O   
6979 O O   . HOH   F .   ? 0.3570 0.2609 0.4178 -0.0736 -0.0280 -0.0516 355 HOH   B O   
6980 O O   . HOH   F .   ? 0.4786 0.2950 0.5434 -0.1274 0.1330  0.0561  356 HOH   B O   
6981 O O   . HOH   F .   ? 0.3444 0.1942 0.3872 0.0386  -0.1376 -0.0528 357 HOH   B O   
6982 O O   . HOH   F .   ? 0.4240 0.3332 0.4560 0.0541  -0.1780 0.0069  358 HOH   B O   
6983 O O   . HOH   F .   ? 0.5145 0.5741 0.4937 -0.1137 -0.0233 -0.0601 359 HOH   B O   
6984 O O   . HOH   F .   ? 0.4592 0.3846 0.7207 0.0469  0.1072  0.1383  360 HOH   B O   
6985 O O   . HOH   F .   ? 0.4212 0.5708 0.5858 0.1532  -0.1522 0.1496  361 HOH   B O   
6986 O O   . HOH   F .   ? 0.4358 0.7186 0.3268 0.2174  0.0096  0.0716  362 HOH   B O   
6987 O O   . HOH   F .   ? 0.2108 0.3335 0.6564 -0.0532 -0.0713 -0.0850 363 HOH   B O   
6988 O O   . HOH   F .   ? 0.6144 0.4768 0.4545 0.1286  0.1091  0.0803  364 HOH   B O   
6989 O O   . HOH   F .   ? 0.6159 0.5797 0.3645 0.1959  -0.1313 0.0716  365 HOH   B O   
6990 O O   . HOH   F .   ? 0.6179 0.4296 0.4923 -0.0073 -0.1586 0.0694  366 HOH   B O   
6991 O O   . HOH   F .   ? 0.4740 0.6265 0.6713 0.2986  0.1223  0.1293  367 HOH   B O   
6992 O O   . HOH   F .   ? 0.5064 0.3106 0.6143 -0.1572 -0.0630 0.0068  368 HOH   B O   
6993 O O   . HOH   F .   ? 0.7321 0.4475 0.3231 -0.1133 -0.1094 -0.1006 369 HOH   B O   
6994 O O   . HOH   F .   ? 0.6146 0.2006 0.3691 0.0112  -0.0037 0.0507  370 HOH   B O   
6995 O O   . HOH   F .   ? 0.4521 0.5109 0.4333 -0.0249 -0.0343 -0.1028 371 HOH   B O   
6996 O O   . HOH   F .   ? 0.7739 0.7862 0.5056 0.1521  -0.1421 0.0739  372 HOH   B O   
6997 O O   . HOH   F .   ? 0.4426 0.3228 0.4710 0.0829  -0.1462 -0.0404 373 HOH   B O   
6998 O O   . HOH   F .   ? 0.2363 0.4223 0.4536 0.0379  -0.0820 -0.0796 374 HOH   B O   
6999 O O   . HOH   F .   ? 0.4675 0.5093 0.4367 -0.1245 -0.1110 0.0398  375 HOH   B O   
7000 O O   . HOH   F .   ? 0.6871 0.3592 0.5730 -0.0623 -0.0321 -0.0142 376 HOH   B O   
7001 O O   . HOH   F .   ? 0.3064 0.3753 0.2214 0.0467  0.0253  0.0007  377 HOH   B O   
7002 O O   . HOH   F .   ? 0.4936 0.6788 0.6405 0.1800  0.0968  0.3224  378 HOH   B O   
7003 O O   . HOH   F .   ? 0.3420 0.5609 0.4964 0.1589  -0.0217 0.0438  379 HOH   B O   
7004 O O   . HOH   F .   ? 0.2984 0.2549 0.3269 0.0067  0.0071  0.0537  380 HOH   B O   
7005 O O   . HOH   F .   ? 0.5470 0.6930 0.3611 -0.1357 0.0340  -0.1525 381 HOH   B O   
7006 O O   . HOH   F .   ? 0.5720 0.6847 0.6130 0.0679  0.1962  0.1616  382 HOH   B O   
7007 O O   . HOH   F .   ? 0.3853 0.8325 0.5625 -0.0501 0.1792  0.0810  383 HOH   B O   
7008 O O   . HOH   F .   ? 0.7425 0.6275 0.4157 0.1623  -0.0177 -0.0020 384 HOH   B O   
7009 O O   . HOH   F .   ? 0.4096 0.3499 0.3049 0.0166  0.0089  -0.0013 385 HOH   B O   
7010 O O   . HOH   F .   ? 0.2504 0.4419 0.3383 -0.0885 -0.1027 -0.0165 386 HOH   B O   
7011 O O   . HOH   F .   ? 0.7433 0.3625 0.4690 0.0084  0.0681  -0.1223 387 HOH   B O   
7012 O O   . HOH   F .   ? 0.4800 0.4740 0.3997 -0.0522 -0.1082 -0.0120 388 HOH   B O   
7013 O O   . HOH   F .   ? 0.5024 0.4227 0.5574 -0.0663 -0.0219 -0.0095 389 HOH   B O   
7014 O O   . HOH   F .   ? 0.3644 0.2125 0.3346 0.0580  -0.0395 0.0064  390 HOH   B O   
7015 O O   . HOH   F .   ? 0.4273 0.3877 0.3394 -0.0557 0.0013  0.0336  391 HOH   B O   
7016 O O   . HOH   F .   ? 0.3979 0.2396 0.5263 -0.0483 0.0475  0.0475  392 HOH   B O   
7017 O O   . HOH   F .   ? 0.2310 0.5783 0.6303 -0.1520 -0.0683 -0.0330 393 HOH   B O   
7018 O O   . HOH   F .   ? 0.4767 0.6168 0.3183 0.1655  -0.0146 -0.0954 394 HOH   B O   
7019 O O   . HOH   F .   ? 0.4219 0.4194 0.4058 -0.0143 0.1013  0.0902  395 HOH   B O   
7020 O O   . HOH   F .   ? 0.3124 0.3938 0.3616 0.0530  -0.0166 -0.0514 396 HOH   B O   
7021 O O   . HOH   F .   ? 0.5656 0.5943 0.7250 0.0779  -0.0890 0.1953  397 HOH   B O   
7022 O O   . HOH   F .   ? 0.2286 0.2955 0.5104 -0.0631 -0.0939 -0.0076 398 HOH   B O   
7023 O O   . HOH   F .   ? 0.6044 0.4351 0.3414 -0.2098 0.0111  0.1246  399 HOH   B O   
7024 O O   . HOH   F .   ? 0.6306 0.5864 0.3909 0.1765  -0.0592 -0.0175 400 HOH   B O   
# 
