data_7HDM
# 
_entry.id   7HDM 
# 
_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   7HDM         pdb_00007hdm 10.2210/pdb7hdm/pdb 
WWPDB D_1001407340 ?            ?                   
# 
_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                        7HDM 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Fraser 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              jaimefraser@gmail.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5080-2859 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Correy, G.J.' 1 ? 
'Fraser, J.S.' 2 ? 
# 
_citation.id                        primary 
_citation.title                     
;Exploration of structure-activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment linking and active learning.
;
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_volume            11 
_citation.page_first                eads7187 
_citation.page_last                 eads7187 
_citation.year                      2025 
_citation.pdbx_database_id_PubMed   40435250 
_citation.pdbx_database_id_DOI      10.1126/sciadv.ads7187 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Correy, G.J.'    0000-0001-5155-7325 1  
primary 'Rachman, M.M.'   0000-0003-3671-8885 2  
primary 'Togo, T.'        0000-0003-0243-0760 3  
primary 'Gahbauer, S.'    0000-0002-3115-9757 4  
primary 'Doruk, Y.U.'     0000-0002-3388-7803 5  
primary 'Stevens, M.G.V.' 0009-0004-9732-0349 6  
primary 'Jaishankar, P.'  0009-0005-2013-8941 7  
primary 'Kelley, B.'      ?                   8  
primary 'Goldman, B.'     0009-0006-6465-6959 9  
primary 'Schmidt, M.'     ?                   10 
primary 'Kramer, T.'      0009-0002-5932-7406 11 
primary 'Radchenko, D.S.' 0000-0001-5444-7754 12 
primary 'Moroz, Y.S.'     0000-0001-6073-002X 13 
primary 'Ashworth, A.'    0000-0003-1446-7878 14 
primary 'Riley, P.'       0000-0003-0797-0272 15 
primary 'Shoichet, B.K.'  0000-0002-6098-7367 16 
primary 'Renslo, A.R.'    0000-0002-1240-2846 17 
primary 'Walters, W.P.'   0000-0003-2860-7958 18 
primary 'Fraser, J.S.'    0000-0002-5080-2859 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Non-structural protein 3'                                     18178.766 2   '3.4.19.121, 3.4.22.-' ? ? 
'HIS6 purification tag and linker (MHHHHHHSSGVDLGTENLYFQ) cleaved with TEV protease' 
2 non-polymer syn 'trifluoroacetic acid'                                         114.023   1   ?                      ? ? ? 
3 non-polymer syn '(4S)-4-hydroxy-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-D-proline' 248.238   1   ?                      ? ? ? 
4 water       nat water                                                          18.015    418 ?                      ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'trifluoroacetic acid'                                         TFA   
3 '(4S)-4-hydroxy-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-D-proline' A1A8K 
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 
A1A8K non-polymer         . '(4S)-4-hydroxy-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-D-proline' ? 'C11 H12 N4 O3'  248.238 
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 
TFA   non-polymer         . 'trifluoroacetic acid'                                         ? 'C2 H F3 O2'     114.023 
THR   'L-peptide linking' y THREONINE                                                      ? 'C4 H9 N O3'     119.119 
TYR   'L-peptide linking' y TYROSINE                                                       ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                         ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 TFA   1   201 201  TFA   TFA A . 
D 3 A1A8K 1   202 201  A1A8K LA1 A . 
E 4 HOH   1   301 36   HOH   HOH A . 
E 4 HOH   2   302 292  HOH   HOH A . 
E 4 HOH   3   303 229  HOH   HOH A . 
E 4 HOH   4   304 196  HOH   HOH A . 
E 4 HOH   5   305 625  HOH   HOH A . 
E 4 HOH   6   306 209  HOH   HOH A . 
E 4 HOH   7   307 661  HOH   HOH A . 
E 4 HOH   8   308 493  HOH   HOH A . 
E 4 HOH   9   309 1301 HOH   HOH A . 
E 4 HOH   10  310 86   HOH   HOH A . 
E 4 HOH   11  311 1290 HOH   HOH A . 
E 4 HOH   12  312 93   HOH   HOH A . 
E 4 HOH   13  313 405  HOH   HOH A . 
E 4 HOH   14  314 662  HOH   HOH A . 
E 4 HOH   15  315 1283 HOH   HOH A . 
E 4 HOH   16  316 3    HOH   HOH A . 
E 4 HOH   17  317 74   HOH   HOH A . 
E 4 HOH   18  318 1289 HOH   HOH A . 
E 4 HOH   19  319 76   HOH   HOH A . 
E 4 HOH   20  320 236  HOH   HOH A . 
E 4 HOH   21  321 247  HOH   HOH A . 
E 4 HOH   22  322 124  HOH   HOH A . 
E 4 HOH   23  323 109  HOH   HOH A . 
E 4 HOH   24  324 136  HOH   HOH A . 
E 4 HOH   25  325 1295 HOH   HOH A . 
E 4 HOH   26  326 192  HOH   HOH A . 
E 4 HOH   27  327 21   HOH   HOH A . 
E 4 HOH   28  328 225  HOH   HOH A . 
E 4 HOH   29  329 151  HOH   HOH A . 
E 4 HOH   30  330 57   HOH   HOH A . 
E 4 HOH   31  331 469  HOH   HOH A . 
E 4 HOH   32  332 337  HOH   HOH A . 
E 4 HOH   33  333 15   HOH   HOH A . 
E 4 HOH   34  334 140  HOH   HOH A . 
E 4 HOH   35  335 24   HOH   HOH A . 
E 4 HOH   36  336 164  HOH   HOH A . 
E 4 HOH   37  337 320  HOH   HOH A . 
E 4 HOH   38  338 241  HOH   HOH A . 
E 4 HOH   39  339 630  HOH   HOH A . 
E 4 HOH   40  340 351  HOH   HOH A . 
E 4 HOH   41  341 964  HOH   HOH A . 
E 4 HOH   42  342 165  HOH   HOH A . 
E 4 HOH   43  343 1300 HOH   HOH A . 
E 4 HOH   44  344 33   HOH   HOH A . 
E 4 HOH   45  345 18   HOH   HOH A . 
E 4 HOH   46  346 42   HOH   HOH A . 
E 4 HOH   47  347 153  HOH   HOH A . 
E 4 HOH   48  348 409  HOH   HOH A . 
E 4 HOH   49  349 1309 HOH   HOH A . 
E 4 HOH   50  350 92   HOH   HOH A . 
E 4 HOH   51  351 396  HOH   HOH A . 
E 4 HOH   52  352 39   HOH   HOH A . 
E 4 HOH   53  353 139  HOH   HOH A . 
E 4 HOH   54  354 2    HOH   HOH A . 
E 4 HOH   55  355 354  HOH   HOH A . 
E 4 HOH   56  356 66   HOH   HOH A . 
E 4 HOH   57  357 19   HOH   HOH A . 
E 4 HOH   58  358 1275 HOH   HOH A . 
E 4 HOH   59  359 17   HOH   HOH A . 
E 4 HOH   60  360 155  HOH   HOH A . 
E 4 HOH   61  361 169  HOH   HOH A . 
E 4 HOH   62  362 102  HOH   HOH A . 
E 4 HOH   63  363 393  HOH   HOH A . 
E 4 HOH   64  364 162  HOH   HOH A . 
E 4 HOH   65  365 939  HOH   HOH A . 
E 4 HOH   66  366 5    HOH   HOH A . 
E 4 HOH   67  367 148  HOH   HOH A . 
E 4 HOH   68  368 138  HOH   HOH A . 
E 4 HOH   69  369 56   HOH   HOH A . 
E 4 HOH   70  370 218  HOH   HOH A . 
E 4 HOH   71  371 159  HOH   HOH A . 
E 4 HOH   72  372 45   HOH   HOH A . 
E 4 HOH   73  373 154  HOH   HOH A . 
E 4 HOH   74  374 461  HOH   HOH A . 
E 4 HOH   75  375 78   HOH   HOH A . 
E 4 HOH   76  376 81   HOH   HOH A . 
E 4 HOH   77  377 46   HOH   HOH A . 
E 4 HOH   78  378 115  HOH   HOH A . 
E 4 HOH   79  379 296  HOH   HOH A . 
E 4 HOH   80  380 49   HOH   HOH A . 
E 4 HOH   81  381 134  HOH   HOH A . 
E 4 HOH   82  382 26   HOH   HOH A . 
E 4 HOH   83  383 27   HOH   HOH A . 
E 4 HOH   84  384 140  HOH   HOH A . 
E 4 HOH   85  385 1308 HOH   HOH A . 
E 4 HOH   86  386 4    HOH   HOH A . 
E 4 HOH   87  387 62   HOH   HOH A . 
E 4 HOH   88  388 34   HOH   HOH A . 
E 4 HOH   89  389 35   HOH   HOH A . 
E 4 HOH   90  390 8    HOH   HOH A . 
E 4 HOH   91  391 186  HOH   HOH A . 
E 4 HOH   92  392 366  HOH   HOH A . 
E 4 HOH   93  393 8    HOH   HOH A . 
E 4 HOH   94  394 121  HOH   HOH A . 
E 4 HOH   95  395 116  HOH   HOH A . 
E 4 HOH   96  396 70   HOH   HOH A . 
E 4 HOH   97  397 12   HOH   HOH A . 
E 4 HOH   98  398 303  HOH   HOH A . 
E 4 HOH   99  399 195  HOH   HOH A . 
E 4 HOH   100 400 6    HOH   HOH A . 
E 4 HOH   101 401 83   HOH   HOH A . 
E 4 HOH   102 402 58   HOH   HOH A . 
E 4 HOH   103 403 3    HOH   HOH A . 
E 4 HOH   104 404 85   HOH   HOH A . 
E 4 HOH   105 405 105  HOH   HOH A . 
E 4 HOH   106 406 1310 HOH   HOH A . 
E 4 HOH   107 407 67   HOH   HOH A . 
E 4 HOH   108 408 96   HOH   HOH A . 
E 4 HOH   109 409 7    HOH   HOH A . 
E 4 HOH   110 410 122  HOH   HOH A . 
E 4 HOH   111 411 1068 HOH   HOH A . 
E 4 HOH   112 412 1315 HOH   HOH A . 
E 4 HOH   113 413 582  HOH   HOH A . 
E 4 HOH   114 414 132  HOH   HOH A . 
E 4 HOH   115 415 333  HOH   HOH A . 
E 4 HOH   116 416 25   HOH   HOH A . 
E 4 HOH   117 417 199  HOH   HOH A . 
E 4 HOH   118 418 397  HOH   HOH A . 
E 4 HOH   119 419 68   HOH   HOH A . 
E 4 HOH   120 420 156  HOH   HOH A . 
E 4 HOH   121 421 123  HOH   HOH A . 
E 4 HOH   122 422 278  HOH   HOH A . 
E 4 HOH   123 423 281  HOH   HOH A . 
E 4 HOH   124 424 53   HOH   HOH A . 
E 4 HOH   125 425 95   HOH   HOH A . 
E 4 HOH   126 426 7    HOH   HOH A . 
E 4 HOH   127 427 4    HOH   HOH A . 
E 4 HOH   128 428 125  HOH   HOH A . 
E 4 HOH   129 429 1222 HOH   HOH A . 
E 4 HOH   130 430 1279 HOH   HOH A . 
E 4 HOH   131 431 1313 HOH   HOH A . 
E 4 HOH   132 432 51   HOH   HOH A . 
E 4 HOH   133 433 1    HOH   HOH A . 
E 4 HOH   134 434 381  HOH   HOH A . 
E 4 HOH   135 435 212  HOH   HOH A . 
E 4 HOH   136 436 1286 HOH   HOH A . 
E 4 HOH   137 437 1189 HOH   HOH A . 
E 4 HOH   138 438 1296 HOH   HOH A . 
E 4 HOH   139 439 16   HOH   HOH A . 
E 4 HOH   140 440 71   HOH   HOH A . 
E 4 HOH   141 441 40   HOH   HOH A . 
E 4 HOH   142 442 80   HOH   HOH A . 
E 4 HOH   143 443 944  HOH   HOH A . 
E 4 HOH   144 444 188  HOH   HOH A . 
E 4 HOH   145 445 1094 HOH   HOH A . 
E 4 HOH   146 446 94   HOH   HOH A . 
E 4 HOH   147 447 952  HOH   HOH A . 
E 4 HOH   148 448 73   HOH   HOH A . 
E 4 HOH   149 449 79   HOH   HOH A . 
E 4 HOH   150 450 1238 HOH   HOH A . 
E 4 HOH   151 451 576  HOH   HOH A . 
E 4 HOH   152 452 104  HOH   HOH A . 
E 4 HOH   153 453 97   HOH   HOH A . 
E 4 HOH   154 454 9    HOH   HOH A . 
E 4 HOH   155 455 6    HOH   HOH A . 
E 4 HOH   156 456 330  HOH   HOH A . 
E 4 HOH   157 457 1119 HOH   HOH A . 
E 4 HOH   158 458 107  HOH   HOH A . 
E 4 HOH   159 459 509  HOH   HOH A . 
E 4 HOH   160 460 726  HOH   HOH A . 
E 4 HOH   161 461 163  HOH   HOH A . 
E 4 HOH   162 462 1134 HOH   HOH A . 
E 4 HOH   163 463 408  HOH   HOH A . 
E 4 HOH   164 464 756  HOH   HOH A . 
E 4 HOH   165 465 280  HOH   HOH A . 
E 4 HOH   166 466 801  HOH   HOH A . 
E 4 HOH   167 467 319  HOH   HOH A . 
E 4 HOH   168 468 361  HOH   HOH A . 
E 4 HOH   169 469 1307 HOH   HOH A . 
E 4 HOH   170 470 126  HOH   HOH A . 
E 4 HOH   171 471 556  HOH   HOH A . 
E 4 HOH   172 472 342  HOH   HOH A . 
E 4 HOH   173 473 1276 HOH   HOH A . 
E 4 HOH   174 474 63   HOH   HOH A . 
E 4 HOH   175 475 250  HOH   HOH A . 
E 4 HOH   176 476 202  HOH   HOH A . 
E 4 HOH   177 477 370  HOH   HOH A . 
E 4 HOH   178 478 1306 HOH   HOH A . 
E 4 HOH   179 479 1287 HOH   HOH A . 
E 4 HOH   180 480 267  HOH   HOH A . 
E 4 HOH   181 481 695  HOH   HOH A . 
E 4 HOH   182 482 224  HOH   HOH A . 
E 4 HOH   183 483 5    HOH   HOH A . 
E 4 HOH   184 484 919  HOH   HOH A . 
E 4 HOH   185 485 674  HOH   HOH A . 
E 4 HOH   186 486 326  HOH   HOH A . 
E 4 HOH   187 487 805  HOH   HOH A . 
E 4 HOH   188 488 2    HOH   HOH A . 
E 4 HOH   189 489 309  HOH   HOH A . 
E 4 HOH   190 490 135  HOH   HOH A . 
E 4 HOH   191 491 331  HOH   HOH A . 
E 4 HOH   192 492 1299 HOH   HOH A . 
E 4 HOH   193 493 318  HOH   HOH A . 
E 4 HOH   194 494 208  HOH   HOH A . 
E 4 HOH   195 495 315  HOH   HOH A . 
E 4 HOH   196 496 521  HOH   HOH A . 
E 4 HOH   197 497 941  HOH   HOH A . 
E 4 HOH   198 498 263  HOH   HOH A . 
E 4 HOH   199 499 711  HOH   HOH A . 
E 4 HOH   200 500 1314 HOH   HOH A . 
E 4 HOH   201 501 152  HOH   HOH A . 
E 4 HOH   202 502 180  HOH   HOH A . 
E 4 HOH   203 503 1071 HOH   HOH A . 
E 4 HOH   204 504 1284 HOH   HOH A . 
E 4 HOH   205 505 350  HOH   HOH A . 
E 4 HOH   206 506 356  HOH   HOH A . 
E 4 HOH   207 507 363  HOH   HOH A . 
E 4 HOH   208 508 313  HOH   HOH A . 
E 4 HOH   209 509 371  HOH   HOH A . 
E 4 HOH   210 510 376  HOH   HOH A . 
E 4 HOH   211 511 185  HOH   HOH A . 
E 4 HOH   212 512 429  HOH   HOH A . 
E 4 HOH   213 513 70   HOH   HOH A . 
E 4 HOH   214 514 772  HOH   HOH A . 
E 4 HOH   215 515 1074 HOH   HOH A . 
E 4 HOH   216 516 346  HOH   HOH A . 
E 4 HOH   217 517 1292 HOH   HOH A . 
E 4 HOH   218 518 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   203 549  HOH   HOH B . 
F 4 HOH   4   204 240  HOH   HOH B . 
F 4 HOH   5   205 398  HOH   HOH B . 
F 4 HOH   6   206 364  HOH   HOH B . 
F 4 HOH   7   207 900  HOH   HOH B . 
F 4 HOH   8   208 1249 HOH   HOH B . 
F 4 HOH   9   209 758  HOH   HOH B . 
F 4 HOH   10  210 654  HOH   HOH B . 
F 4 HOH   11  211 120  HOH   HOH B . 
F 4 HOH   12  212 531  HOH   HOH B . 
F 4 HOH   13  213 743  HOH   HOH B . 
F 4 HOH   14  214 50   HOH   HOH B . 
F 4 HOH   15  215 452  HOH   HOH B . 
F 4 HOH   16  216 264  HOH   HOH B . 
F 4 HOH   17  217 343  HOH   HOH B . 
F 4 HOH   18  218 444  HOH   HOH B . 
F 4 HOH   19  219 332  HOH   HOH B . 
F 4 HOH   20  220 353  HOH   HOH B . 
F 4 HOH   21  221 1140 HOH   HOH B . 
F 4 HOH   22  222 131  HOH   HOH B . 
F 4 HOH   23  223 54   HOH   HOH B . 
F 4 HOH   24  224 276  HOH   HOH B . 
F 4 HOH   25  225 282  HOH   HOH B . 
F 4 HOH   26  226 75   HOH   HOH B . 
F 4 HOH   27  227 232  HOH   HOH B . 
F 4 HOH   28  228 252  HOH   HOH B . 
F 4 HOH   29  229 82   HOH   HOH B . 
F 4 HOH   30  230 1278 HOH   HOH B . 
F 4 HOH   31  231 272  HOH   HOH B . 
F 4 HOH   32  232 300  HOH   HOH B . 
F 4 HOH   33  233 205  HOH   HOH B . 
F 4 HOH   34  234 110  HOH   HOH B . 
F 4 HOH   35  235 127  HOH   HOH B . 
F 4 HOH   36  236 69   HOH   HOH B . 
F 4 HOH   37  237 723  HOH   HOH B . 
F 4 HOH   38  238 1    HOH   HOH B . 
F 4 HOH   39  239 60   HOH   HOH B . 
F 4 HOH   40  240 181  HOH   HOH B . 
F 4 HOH   41  241 1312 HOH   HOH B . 
F 4 HOH   42  242 128  HOH   HOH B . 
F 4 HOH   43  243 14   HOH   HOH B . 
F 4 HOH   44  244 133  HOH   HOH B . 
F 4 HOH   45  245 144  HOH   HOH B . 
F 4 HOH   46  246 166  HOH   HOH B . 
F 4 HOH   47  247 9    HOH   HOH B . 
F 4 HOH   48  248 30   HOH   HOH B . 
F 4 HOH   49  249 129  HOH   HOH B . 
F 4 HOH   50  250 150  HOH   HOH B . 
F 4 HOH   51  251 52   HOH   HOH B . 
F 4 HOH   52  252 325  HOH   HOH B . 
F 4 HOH   53  253 143  HOH   HOH B . 
F 4 HOH   54  254 47   HOH   HOH B . 
F 4 HOH   55  255 31   HOH   HOH B . 
F 4 HOH   56  256 20   HOH   HOH B . 
F 4 HOH   57  257 41   HOH   HOH B . 
F 4 HOH   58  258 10   HOH   HOH B . 
F 4 HOH   59  259 72   HOH   HOH B . 
F 4 HOH   60  260 103  HOH   HOH B . 
F 4 HOH   61  261 231  HOH   HOH B . 
F 4 HOH   62  262 221  HOH   HOH B . 
F 4 HOH   63  263 391  HOH   HOH B . 
F 4 HOH   64  264 302  HOH   HOH B . 
F 4 HOH   65  265 175  HOH   HOH B . 
F 4 HOH   66  266 114  HOH   HOH B . 
F 4 HOH   67  267 271  HOH   HOH B . 
F 4 HOH   68  268 1277 HOH   HOH B . 
F 4 HOH   69  269 61   HOH   HOH B . 
F 4 HOH   70  270 11   HOH   HOH B . 
F 4 HOH   71  271 287  HOH   HOH B . 
F 4 HOH   72  272 242  HOH   HOH B . 
F 4 HOH   73  273 347  HOH   HOH B . 
F 4 HOH   74  274 147  HOH   HOH B . 
F 4 HOH   75  275 59   HOH   HOH B . 
F 4 HOH   76  276 77   HOH   HOH B . 
F 4 HOH   77  277 172  HOH   HOH B . 
F 4 HOH   78  278 117  HOH   HOH B . 
F 4 HOH   79  279 243  HOH   HOH B . 
F 4 HOH   80  280 84   HOH   HOH B . 
F 4 HOH   81  281 43   HOH   HOH B . 
F 4 HOH   82  282 416  HOH   HOH B . 
F 4 HOH   83  283 1066 HOH   HOH B . 
F 4 HOH   84  284 22   HOH   HOH B . 
F 4 HOH   85  285 1305 HOH   HOH B . 
F 4 HOH   86  286 341  HOH   HOH B . 
F 4 HOH   87  287 1106 HOH   HOH B . 
F 4 HOH   88  288 106  HOH   HOH B . 
F 4 HOH   89  289 235  HOH   HOH B . 
F 4 HOH   90  290 88   HOH   HOH B . 
F 4 HOH   91  291 220  HOH   HOH B . 
F 4 HOH   92  292 13   HOH   HOH B . 
F 4 HOH   93  293 89   HOH   HOH B . 
F 4 HOH   94  294 297  HOH   HOH B . 
F 4 HOH   95  295 99   HOH   HOH B . 
F 4 HOH   96  296 137  HOH   HOH B . 
F 4 HOH   97  297 216  HOH   HOH B . 
F 4 HOH   98  298 311  HOH   HOH B . 
F 4 HOH   99  299 112  HOH   HOH B . 
F 4 HOH   100 300 32   HOH   HOH B . 
F 4 HOH   101 301 387  HOH   HOH B . 
F 4 HOH   102 302 160  HOH   HOH B . 
F 4 HOH   103 303 142  HOH   HOH B . 
F 4 HOH   104 304 299  HOH   HOH B . 
F 4 HOH   105 305 635  HOH   HOH B . 
F 4 HOH   106 306 316  HOH   HOH B . 
F 4 HOH   107 307 1126 HOH   HOH B . 
F 4 HOH   108 308 118  HOH   HOH B . 
F 4 HOH   109 309 215  HOH   HOH B . 
F 4 HOH   110 310 101  HOH   HOH B . 
F 4 HOH   111 311 170  HOH   HOH B . 
F 4 HOH   112 312 37   HOH   HOH B . 
F 4 HOH   113 313 1291 HOH   HOH B . 
F 4 HOH   114 314 44   HOH   HOH B . 
F 4 HOH   115 315 48   HOH   HOH B . 
F 4 HOH   116 316 91   HOH   HOH B . 
F 4 HOH   117 317 704  HOH   HOH B . 
F 4 HOH   118 318 141  HOH   HOH B . 
F 4 HOH   119 319 23   HOH   HOH B . 
F 4 HOH   120 320 177  HOH   HOH B . 
F 4 HOH   121 321 38   HOH   HOH B . 
F 4 HOH   122 322 1294 HOH   HOH B . 
F 4 HOH   123 323 28   HOH   HOH B . 
F 4 HOH   124 324 1285 HOH   HOH B . 
F 4 HOH   125 325 100  HOH   HOH B . 
F 4 HOH   126 326 197  HOH   HOH B . 
F 4 HOH   127 327 182  HOH   HOH B . 
F 4 HOH   128 328 29   HOH   HOH B . 
F 4 HOH   129 329 1274 HOH   HOH B . 
F 4 HOH   130 330 161  HOH   HOH B . 
F 4 HOH   131 331 98   HOH   HOH B . 
F 4 HOH   132 332 334  HOH   HOH B . 
F 4 HOH   133 333 717  HOH   HOH B . 
F 4 HOH   134 334 339  HOH   HOH B . 
F 4 HOH   135 335 55   HOH   HOH B . 
F 4 HOH   136 336 65   HOH   HOH B . 
F 4 HOH   137 337 1293 HOH   HOH B . 
F 4 HOH   138 338 960  HOH   HOH B . 
F 4 HOH   139 339 207  HOH   HOH B . 
F 4 HOH   140 340 445  HOH   HOH B . 
F 4 HOH   141 341 234  HOH   HOH B . 
F 4 HOH   142 342 619  HOH   HOH B . 
F 4 HOH   143 343 362  HOH   HOH B . 
F 4 HOH   144 344 178  HOH   HOH B . 
F 4 HOH   145 345 90   HOH   HOH B . 
F 4 HOH   146 346 1304 HOH   HOH B . 
F 4 HOH   147 347 463  HOH   HOH B . 
F 4 HOH   148 348 191  HOH   HOH B . 
F 4 HOH   149 349 623  HOH   HOH B . 
F 4 HOH   150 350 335  HOH   HOH B . 
F 4 HOH   151 351 87   HOH   HOH B . 
F 4 HOH   152 352 1046 HOH   HOH B . 
F 4 HOH   153 353 304  HOH   HOH B . 
F 4 HOH   154 354 203  HOH   HOH B . 
F 4 HOH   155 355 1280 HOH   HOH B . 
F 4 HOH   156 356 541  HOH   HOH B . 
F 4 HOH   157 357 290  HOH   HOH B . 
F 4 HOH   158 358 1077 HOH   HOH B . 
F 4 HOH   159 359 479  HOH   HOH B . 
F 4 HOH   160 360 389  HOH   HOH B . 
F 4 HOH   161 361 718  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 1316 HOH   HOH B . 
F 4 HOH   165 365 291  HOH   HOH B . 
F 4 HOH   166 366 340  HOH   HOH B . 
F 4 HOH   167 367 615  HOH   HOH B . 
F 4 HOH   168 368 373  HOH   HOH B . 
F 4 HOH   169 369 667  HOH   HOH B . 
F 4 HOH   170 370 190  HOH   HOH B . 
F 4 HOH   171 371 898  HOH   HOH B . 
F 4 HOH   172 372 310  HOH   HOH B . 
F 4 HOH   173 373 1303 HOH   HOH B . 
F 4 HOH   174 374 431  HOH   HOH B . 
F 4 HOH   175 375 183  HOH   HOH B . 
F 4 HOH   176 376 149  HOH   HOH B . 
F 4 HOH   177 377 1173 HOH   HOH B . 
F 4 HOH   178 378 1163 HOH   HOH B . 
F 4 HOH   179 379 418  HOH   HOH B . 
F 4 HOH   180 380 1000 HOH   HOH B . 
F 4 HOH   181 381 1311 HOH   HOH B . 
F 4 HOH   182 382 424  HOH   HOH B . 
F 4 HOH   183 383 176  HOH   HOH B . 
F 4 HOH   184 384 981  HOH   HOH B . 
F 4 HOH   185 385 491  HOH   HOH B . 
F 4 HOH   186 386 248  HOH   HOH B . 
F 4 HOH   187 387 470  HOH   HOH B . 
F 4 HOH   188 388 1298 HOH   HOH B . 
F 4 HOH   189 389 265  HOH   HOH B . 
F 4 HOH   190 390 184  HOH   HOH B . 
F 4 HOH   191 391 360  HOH   HOH B . 
F 4 HOH   192 392 355  HOH   HOH B . 
F 4 HOH   193 393 410  HOH   HOH B . 
F 4 HOH   194 394 274  HOH   HOH B . 
F 4 HOH   195 395 314  HOH   HOH B . 
F 4 HOH   196 396 566  HOH   HOH B . 
F 4 HOH   197 397 157  HOH   HOH B . 
F 4 HOH   198 398 792  HOH   HOH B . 
F 4 HOH   199 399 321  HOH   HOH B . 
F 4 HOH   200 400 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HDM 
_cell.length_a           88.761 
_cell.length_b           88.761 
_cell.length_c           39.598 
_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                         7HDM 
_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          7HDM 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.76 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-05-20 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.88557 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HDM 
_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                   156496 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.800 
_reflns.pdbx_Rmerge_I_obs            0.057 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        11.500 
_reflns.B_iso_Wilson_estimate        12.460 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.062 
_reflns.pdbx_Rpim_I_all              0.024 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1001355 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.020 1.040  ? 41174 7489 ? 1.566 ? ? ? 5.500 ? 0.700  ? ? ? ? ? ? 96.900 1.729 0.718 0.606 
1 2 5.590 44.380 ? 7113  1040 ? 0.028 ? ? ? 6.800 ? 42.700 ? ? ? ? ? ? 99.900 0.030 0.011 0.999 
# 
_refine.entry_id                                 7HDM 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0200 
_refine.ls_d_res_low                             44.3800 
_refine.pdbx_ls_sigma_F                          1.350 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.7500 
_refine.ls_number_reflns_obs                     156406 
_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                          0.1484 
_refine.ls_R_factor_R_work                       0.1476 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1636 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7546 
_refine.ls_number_reflns_R_work                  148860 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               19.1665 
_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                            0.1300 
_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                                69.840 
_refine.B_iso_min                                8.820 
_refine.pdbx_overall_phase_error                 18.6000 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0200 
_refine_hist.d_res_low                        44.3800 
_refine_hist.pdbx_number_atoms_ligand         36 
_refine_hist.number_atoms_solvent             418 
_refine_hist.number_atoms_total               2996 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           19.50 
_refine_hist.pdbx_B_iso_mean_solvent          30.44 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.0200 1.0300  30 95.0000  4715 . 0.4641 0.4364 . 193 0.0000 4908 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 4962 . 0.3908 0.3976 . 280 0.0000 5242 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 4872 . 0.3208 0.3003 . 279 0.0000 5151 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 4956 . 0.2875 0.2982 . 277 0.0000 5233 . 'X-RAY DIFFRACTION' 
1.0700 1.0800  30 100.0000 4893 . 0.2625 0.2915 . 239 0.0000 5132 . 'X-RAY DIFFRACTION' 
1.0800 1.1000  30 100.0000 4995 . 0.2320 0.2495 . 240 0.0000 5235 . 'X-RAY DIFFRACTION' 
1.1000 1.1100  30 100.0000 4905 . 0.2098 0.2244 . 257 0.0000 5162 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5005 . 0.1917 0.2226 . 222 0.0000 5227 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 4927 . 0.1732 0.1891 . 249 0.0000 5176 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 4995 . 0.1591 0.1860 . 254 0.0000 5249 . 'X-RAY DIFFRACTION' 
1.1700 1.1900  30 100.0000 4939 . 0.1526 0.1895 . 238 0.0000 5177 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 4896 . 0.1410 0.1786 . 285 0.0000 5181 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5002 . 0.1365 0.1582 . 216 0.0000 5218 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 4926 . 0.1348 0.1539 . 253 0.0000 5179 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 4957 . 0.1442 0.1610 . 246 0.0000 5203 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 4962 . 0.1361 0.1604 . 264 0.0000 5226 . 'X-RAY DIFFRACTION' 
1.3200 1.3500  30 100.0000 4955 . 0.1368 0.1602 . 260 0.0000 5215 . 'X-RAY DIFFRACTION' 
1.3500 1.3800  30 100.0000 4964 . 0.1373 0.1829 . 255 0.0000 5219 . 'X-RAY DIFFRACTION' 
1.3800 1.4300  30 100.0000 4966 . 0.1301 0.1664 . 239 0.0000 5205 . 'X-RAY DIFFRACTION' 
1.4300 1.4700  30 100.0000 4969 . 0.1247 0.1363 . 250 0.0000 5219 . 'X-RAY DIFFRACTION' 
1.4700 1.5200  30 100.0000 4982 . 0.1182 0.1428 . 236 0.0000 5218 . 'X-RAY DIFFRACTION' 
1.5200 1.5800  30 100.0000 4976 . 0.1187 0.1346 . 263 0.0000 5239 . 'X-RAY DIFFRACTION' 
1.5800 1.6600  30 100.0000 4959 . 0.1191 0.1344 . 264 0.0000 5223 . 'X-RAY DIFFRACTION' 
1.6600 1.7400  30 100.0000 5033 . 0.1273 0.1369 . 202 0.0000 5235 . 'X-RAY DIFFRACTION' 
1.7400 1.8500  30 100.0000 4967 . 0.1299 0.1433 . 294 0.0000 5261 . 'X-RAY DIFFRACTION' 
1.8500 2.0000  30 100.0000 4968 . 0.1332 0.1425 . 246 0.0000 5214 . 'X-RAY DIFFRACTION' 
2.0000 2.2000  30 100.0000 4974 . 0.1353 0.1444 . 288 0.0000 5262 . 'X-RAY DIFFRACTION' 
2.2000 2.5200  30 100.0000 5022 . 0.1369 0.1442 . 252 0.0000 5274 . 'X-RAY DIFFRACTION' 
2.5200 3.1700  30 100.0000 5034 . 0.1506 0.1647 . 251 0.0000 5285 . 'X-RAY DIFFRACTION' 
3.1700 44.3800 30 100.0000 5184 . 0.1497 0.1720 . 254 0.0000 5438 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HDM 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003732' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HDM 
_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 7HDM A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HDM 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 7HDM SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HDM MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HDM SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HDM 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 ALA B 124 ? N ALA B 124 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HDM 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O2 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   A1A8K 
_pdbx_validate_close_contact.auth_seq_id_1    202 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   B 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    301 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.09 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ASP 
_pdbx_validate_symm_contact.auth_seq_id_1     66 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    HG 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    SER 
_pdbx_validate_symm_contact.auth_seq_id_2     1 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    B 
_pdbx_validate_symm_contact.site_symmetry_2   2_655 
_pdbx_validate_symm_contact.dist              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 ? ? 56.38 -133.30 
2 1 HIS B 86 ? ? 57.17 -127.74 
# 
_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 516 ? 5.83 . 
2 1 O ? A HOH 517 ? 6.09 . 
3 1 O ? A HOH 518 ? 7.62 . 
4 1 O ? B HOH 400 ? 6.30 . 
# 
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 
A1A8K N2   N Y N 1   
A1A8K C3   C N N 2   
A1A8K C6   C Y N 3   
A1A8K C9   C Y N 4   
A1A8K C1   C N N 5   
A1A8K C10  C Y N 6   
A1A8K C11  C Y N 7   
A1A8K C2   C N R 8   
A1A8K C4   C N S 9   
A1A8K C5   C N N 10  
A1A8K C7   C Y N 11  
A1A8K C8   C Y N 12  
A1A8K N1   N N N 13  
A1A8K N3   N Y N 14  
A1A8K N4   N Y N 15  
A1A8K O1   O N N 16  
A1A8K O2   O N N 17  
A1A8K O3   O N N 18  
A1A8K H3   H N N 19  
A1A8K H4   H N N 20  
A1A8K H9   H N N 21  
A1A8K H10  H N N 22  
A1A8K H1   H N N 23  
A1A8K H2   H N N 24  
A1A8K H6   H N N 25  
A1A8K H7   H N N 26  
A1A8K H8   H N N 27  
A1A8K H11  H N N 28  
A1A8K H12  H N N 29  
A1A8K H5   H N N 30  
ALA   N    N N N 31  
ALA   CA   C N S 32  
ALA   C    C N N 33  
ALA   O    O N N 34  
ALA   CB   C N N 35  
ALA   OXT  O N N 36  
ALA   H    H N N 37  
ALA   H2   H N N 38  
ALA   HA   H N N 39  
ALA   HB1  H N N 40  
ALA   HB2  H N N 41  
ALA   HB3  H N N 42  
ALA   HXT  H N N 43  
ARG   N    N N N 44  
ARG   CA   C N S 45  
ARG   C    C N N 46  
ARG   O    O N N 47  
ARG   CB   C N N 48  
ARG   CG   C N N 49  
ARG   CD   C N N 50  
ARG   NE   N N N 51  
ARG   CZ   C N N 52  
ARG   NH1  N N N 53  
ARG   NH2  N N N 54  
ARG   OXT  O N N 55  
ARG   H    H N N 56  
ARG   H2   H N N 57  
ARG   HA   H N N 58  
ARG   HB2  H N N 59  
ARG   HB3  H N N 60  
ARG   HG2  H N N 61  
ARG   HG3  H N N 62  
ARG   HD2  H N N 63  
ARG   HD3  H N N 64  
ARG   HE   H N N 65  
ARG   HH11 H N N 66  
ARG   HH12 H N N 67  
ARG   HH21 H N N 68  
ARG   HH22 H N N 69  
ARG   HXT  H N N 70  
ASN   N    N N N 71  
ASN   CA   C N S 72  
ASN   C    C N N 73  
ASN   O    O N N 74  
ASN   CB   C N N 75  
ASN   CG   C N N 76  
ASN   OD1  O N N 77  
ASN   ND2  N N N 78  
ASN   OXT  O N N 79  
ASN   H    H N N 80  
ASN   H2   H N N 81  
ASN   HA   H N N 82  
ASN   HB2  H N N 83  
ASN   HB3  H N N 84  
ASN   HD21 H N N 85  
ASN   HD22 H N N 86  
ASN   HXT  H N N 87  
ASP   N    N N N 88  
ASP   CA   C N S 89  
ASP   C    C N N 90  
ASP   O    O N N 91  
ASP   CB   C N N 92  
ASP   CG   C N N 93  
ASP   OD1  O N N 94  
ASP   OD2  O N N 95  
ASP   OXT  O N N 96  
ASP   H    H N N 97  
ASP   H2   H N N 98  
ASP   HA   H N N 99  
ASP   HB2  H N N 100 
ASP   HB3  H N N 101 
ASP   HD2  H N N 102 
ASP   HXT  H N N 103 
CYS   N    N N N 104 
CYS   CA   C N R 105 
CYS   C    C N N 106 
CYS   O    O N N 107 
CYS   CB   C N N 108 
CYS   SG   S N N 109 
CYS   OXT  O N N 110 
CYS   H    H N N 111 
CYS   H2   H N N 112 
CYS   HA   H N N 113 
CYS   HB2  H N N 114 
CYS   HB3  H N N 115 
CYS   HG   H N N 116 
CYS   HXT  H N N 117 
GLN   N    N N N 118 
GLN   CA   C N S 119 
GLN   C    C N N 120 
GLN   O    O N N 121 
GLN   CB   C N N 122 
GLN   CG   C N N 123 
GLN   CD   C N N 124 
GLN   OE1  O N N 125 
GLN   NE2  N N N 126 
GLN   OXT  O N N 127 
GLN   H    H N N 128 
GLN   H2   H N N 129 
GLN   HA   H N N 130 
GLN   HB2  H N N 131 
GLN   HB3  H N N 132 
GLN   HG2  H N N 133 
GLN   HG3  H N N 134 
GLN   HE21 H N N 135 
GLN   HE22 H N N 136 
GLN   HXT  H N N 137 
GLU   N    N N N 138 
GLU   CA   C N S 139 
GLU   C    C N N 140 
GLU   O    O N N 141 
GLU   CB   C N N 142 
GLU   CG   C N N 143 
GLU   CD   C N N 144 
GLU   OE1  O N N 145 
GLU   OE2  O N N 146 
GLU   OXT  O N N 147 
GLU   H    H N N 148 
GLU   H2   H N N 149 
GLU   HA   H N N 150 
GLU   HB2  H N N 151 
GLU   HB3  H N N 152 
GLU   HG2  H N N 153 
GLU   HG3  H N N 154 
GLU   HE2  H N N 155 
GLU   HXT  H N N 156 
GLY   N    N N N 157 
GLY   CA   C N N 158 
GLY   C    C N N 159 
GLY   O    O N N 160 
GLY   OXT  O N N 161 
GLY   H    H N N 162 
GLY   H2   H N N 163 
GLY   HA2  H N N 164 
GLY   HA3  H N N 165 
GLY   HXT  H N N 166 
HIS   N    N N N 167 
HIS   CA   C N S 168 
HIS   C    C N N 169 
HIS   O    O N N 170 
HIS   CB   C N N 171 
HIS   CG   C Y N 172 
HIS   ND1  N Y N 173 
HIS   CD2  C Y N 174 
HIS   CE1  C Y N 175 
HIS   NE2  N Y N 176 
HIS   OXT  O N N 177 
HIS   H    H N N 178 
HIS   H2   H N N 179 
HIS   HA   H N N 180 
HIS   HB2  H N N 181 
HIS   HB3  H N N 182 
HIS   HD1  H N N 183 
HIS   HD2  H N N 184 
HIS   HE1  H N N 185 
HIS   HE2  H N N 186 
HIS   HXT  H N N 187 
HOH   O    O N N 188 
HOH   H1   H N N 189 
HOH   H2   H N N 190 
ILE   N    N N N 191 
ILE   CA   C N S 192 
ILE   C    C N N 193 
ILE   O    O N N 194 
ILE   CB   C N S 195 
ILE   CG1  C N N 196 
ILE   CG2  C N N 197 
ILE   CD1  C N N 198 
ILE   OXT  O N N 199 
ILE   H    H N N 200 
ILE   H2   H N N 201 
ILE   HA   H N N 202 
ILE   HB   H N N 203 
ILE   HG12 H N N 204 
ILE   HG13 H N N 205 
ILE   HG21 H N N 206 
ILE   HG22 H N N 207 
ILE   HG23 H N N 208 
ILE   HD11 H N N 209 
ILE   HD12 H N N 210 
ILE   HD13 H N N 211 
ILE   HXT  H N N 212 
LEU   N    N N N 213 
LEU   CA   C N S 214 
LEU   C    C N N 215 
LEU   O    O N N 216 
LEU   CB   C N N 217 
LEU   CG   C N N 218 
LEU   CD1  C N N 219 
LEU   CD2  C N N 220 
LEU   OXT  O N N 221 
LEU   H    H N N 222 
LEU   H2   H N N 223 
LEU   HA   H N N 224 
LEU   HB2  H N N 225 
LEU   HB3  H N N 226 
LEU   HG   H N N 227 
LEU   HD11 H N N 228 
LEU   HD12 H N N 229 
LEU   HD13 H N N 230 
LEU   HD21 H N N 231 
LEU   HD22 H N N 232 
LEU   HD23 H N N 233 
LEU   HXT  H N N 234 
LYS   N    N N N 235 
LYS   CA   C N S 236 
LYS   C    C N N 237 
LYS   O    O N N 238 
LYS   CB   C N N 239 
LYS   CG   C N N 240 
LYS   CD   C N N 241 
LYS   CE   C N N 242 
LYS   NZ   N N N 243 
LYS   OXT  O N N 244 
LYS   H    H N N 245 
LYS   H2   H N N 246 
LYS   HA   H N N 247 
LYS   HB2  H N N 248 
LYS   HB3  H N N 249 
LYS   HG2  H N N 250 
LYS   HG3  H N N 251 
LYS   HD2  H N N 252 
LYS   HD3  H N N 253 
LYS   HE2  H N N 254 
LYS   HE3  H N N 255 
LYS   HZ1  H N N 256 
LYS   HZ2  H N N 257 
LYS   HZ3  H N N 258 
LYS   HXT  H N N 259 
MET   N    N N N 260 
MET   CA   C N S 261 
MET   C    C N N 262 
MET   O    O N N 263 
MET   CB   C N N 264 
MET   CG   C N N 265 
MET   SD   S N N 266 
MET   CE   C N N 267 
MET   OXT  O N N 268 
MET   H    H N N 269 
MET   H2   H N N 270 
MET   HA   H N N 271 
MET   HB2  H N N 272 
MET   HB3  H N N 273 
MET   HG2  H N N 274 
MET   HG3  H N N 275 
MET   HE1  H N N 276 
MET   HE2  H N N 277 
MET   HE3  H N N 278 
MET   HXT  H N N 279 
PHE   N    N N N 280 
PHE   CA   C N S 281 
PHE   C    C N N 282 
PHE   O    O N N 283 
PHE   CB   C N N 284 
PHE   CG   C Y N 285 
PHE   CD1  C Y N 286 
PHE   CD2  C Y N 287 
PHE   CE1  C Y N 288 
PHE   CE2  C Y N 289 
PHE   CZ   C Y N 290 
PHE   OXT  O N N 291 
PHE   H    H N N 292 
PHE   H2   H N N 293 
PHE   HA   H N N 294 
PHE   HB2  H N N 295 
PHE   HB3  H N N 296 
PHE   HD1  H N N 297 
PHE   HD2  H N N 298 
PHE   HE1  H N N 299 
PHE   HE2  H N N 300 
PHE   HZ   H N N 301 
PHE   HXT  H N N 302 
PRO   N    N N N 303 
PRO   CA   C N S 304 
PRO   C    C N N 305 
PRO   O    O N N 306 
PRO   CB   C N N 307 
PRO   CG   C N N 308 
PRO   CD   C N N 309 
PRO   OXT  O N N 310 
PRO   H    H N N 311 
PRO   HA   H N N 312 
PRO   HB2  H N N 313 
PRO   HB3  H N N 314 
PRO   HG2  H N N 315 
PRO   HG3  H N N 316 
PRO   HD2  H N N 317 
PRO   HD3  H N N 318 
PRO   HXT  H N N 319 
SER   N    N N N 320 
SER   CA   C N S 321 
SER   C    C N N 322 
SER   O    O N N 323 
SER   CB   C N N 324 
SER   OG   O N N 325 
SER   OXT  O N N 326 
SER   H    H N N 327 
SER   H2   H N N 328 
SER   HA   H N N 329 
SER   HB2  H N N 330 
SER   HB3  H N N 331 
SER   HG   H N N 332 
SER   HXT  H N N 333 
TFA   C1   C N N 334 
TFA   C2   C N N 335 
TFA   O    O N N 336 
TFA   F1   F N N 337 
TFA   F2   F N N 338 
TFA   F3   F N N 339 
TFA   OXT  O N N 340 
TFA   HXT  H N N 341 
THR   N    N N N 342 
THR   CA   C N S 343 
THR   C    C N N 344 
THR   O    O N N 345 
THR   CB   C N R 346 
THR   OG1  O N N 347 
THR   CG2  C N N 348 
THR   OXT  O N N 349 
THR   H    H N N 350 
THR   H2   H N N 351 
THR   HA   H N N 352 
THR   HB   H N N 353 
THR   HG1  H N N 354 
THR   HG21 H N N 355 
THR   HG22 H N N 356 
THR   HG23 H N N 357 
THR   HXT  H N N 358 
TYR   N    N N N 359 
TYR   CA   C N S 360 
TYR   C    C N N 361 
TYR   O    O N N 362 
TYR   CB   C N N 363 
TYR   CG   C Y N 364 
TYR   CD1  C Y N 365 
TYR   CD2  C Y N 366 
TYR   CE1  C Y N 367 
TYR   CE2  C Y N 368 
TYR   CZ   C Y N 369 
TYR   OH   O N N 370 
TYR   OXT  O N N 371 
TYR   H    H N N 372 
TYR   H2   H N N 373 
TYR   HA   H N N 374 
TYR   HB2  H N N 375 
TYR   HB3  H N N 376 
TYR   HD1  H N N 377 
TYR   HD2  H N N 378 
TYR   HE1  H N N 379 
TYR   HE2  H N N 380 
TYR   HH   H N N 381 
TYR   HXT  H N N 382 
VAL   N    N N N 383 
VAL   CA   C N S 384 
VAL   C    C N N 385 
VAL   O    O N N 386 
VAL   CB   C N N 387 
VAL   CG1  C N N 388 
VAL   CG2  C N N 389 
VAL   OXT  O N N 390 
VAL   H    H N N 391 
VAL   H2   H N N 392 
VAL   HA   H N N 393 
VAL   HB   H N N 394 
VAL   HG11 H N N 395 
VAL   HG12 H N N 396 
VAL   HG13 H N N 397 
VAL   HG21 H N N 398 
VAL   HG22 H N N 399 
VAL   HG23 H N N 400 
VAL   HXT  H N N 401 
# 
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 
A1A8K O2  C4   sing N N 1   
A1A8K C4  C3   sing N N 2   
A1A8K C4  C5   sing N N 3   
A1A8K C3  C2   sing N N 4   
A1A8K O3  C1   doub N N 5   
A1A8K C5  N1   sing N N 6   
A1A8K C1  C2   sing N N 7   
A1A8K C1  O1   sing N N 8   
A1A8K C2  N1   sing N N 9   
A1A8K N1  C6   sing N N 10  
A1A8K C6  C9   doub Y N 11  
A1A8K C6  N2   sing Y N 12  
A1A8K C10 C9   sing Y N 13  
A1A8K C10 C11  doub Y N 14  
A1A8K C9  C8   sing Y N 15  
A1A8K N2  C7   doub Y N 16  
A1A8K C11 N4   sing Y N 17  
A1A8K C7  N3   sing Y N 18  
A1A8K C8  N4   sing Y N 19  
A1A8K C8  N3   doub Y N 20  
A1A8K C3  H3   sing N N 21  
A1A8K C3  H4   sing N N 22  
A1A8K C10 H9   sing N N 23  
A1A8K C11 H10  sing N N 24  
A1A8K C2  H1   sing N N 25  
A1A8K C4  H2   sing N N 26  
A1A8K C5  H6   sing N N 27  
A1A8K C5  H7   sing N N 28  
A1A8K C7  H8   sing N N 29  
A1A8K N4  H11  sing N N 30  
A1A8K O1  H12  sing N N 31  
A1A8K O2  H5   sing N N 32  
ALA   N   CA   sing N N 33  
ALA   N   H    sing N N 34  
ALA   N   H2   sing N N 35  
ALA   CA  C    sing N N 36  
ALA   CA  CB   sing N N 37  
ALA   CA  HA   sing N N 38  
ALA   C   O    doub N N 39  
ALA   C   OXT  sing N N 40  
ALA   CB  HB1  sing N N 41  
ALA   CB  HB2  sing N N 42  
ALA   CB  HB3  sing N N 43  
ALA   OXT HXT  sing N N 44  
ARG   N   CA   sing N N 45  
ARG   N   H    sing N N 46  
ARG   N   H2   sing N N 47  
ARG   CA  C    sing N N 48  
ARG   CA  CB   sing N N 49  
ARG   CA  HA   sing N N 50  
ARG   C   O    doub N N 51  
ARG   C   OXT  sing N N 52  
ARG   CB  CG   sing N N 53  
ARG   CB  HB2  sing N N 54  
ARG   CB  HB3  sing N N 55  
ARG   CG  CD   sing N N 56  
ARG   CG  HG2  sing N N 57  
ARG   CG  HG3  sing N N 58  
ARG   CD  NE   sing N N 59  
ARG   CD  HD2  sing N N 60  
ARG   CD  HD3  sing N N 61  
ARG   NE  CZ   sing N N 62  
ARG   NE  HE   sing N N 63  
ARG   CZ  NH1  sing N N 64  
ARG   CZ  NH2  doub N N 65  
ARG   NH1 HH11 sing N N 66  
ARG   NH1 HH12 sing N N 67  
ARG   NH2 HH21 sing N N 68  
ARG   NH2 HH22 sing N N 69  
ARG   OXT HXT  sing N N 70  
ASN   N   CA   sing N N 71  
ASN   N   H    sing N N 72  
ASN   N   H2   sing N N 73  
ASN   CA  C    sing N N 74  
ASN   CA  CB   sing N N 75  
ASN   CA  HA   sing N N 76  
ASN   C   O    doub N N 77  
ASN   C   OXT  sing N N 78  
ASN   CB  CG   sing N N 79  
ASN   CB  HB2  sing N N 80  
ASN   CB  HB3  sing N N 81  
ASN   CG  OD1  doub N N 82  
ASN   CG  ND2  sing N N 83  
ASN   ND2 HD21 sing N N 84  
ASN   ND2 HD22 sing N N 85  
ASN   OXT HXT  sing N N 86  
ASP   N   CA   sing N N 87  
ASP   N   H    sing N N 88  
ASP   N   H2   sing N N 89  
ASP   CA  C    sing N N 90  
ASP   CA  CB   sing N N 91  
ASP   CA  HA   sing N N 92  
ASP   C   O    doub N N 93  
ASP   C   OXT  sing N N 94  
ASP   CB  CG   sing N N 95  
ASP   CB  HB2  sing N N 96  
ASP   CB  HB3  sing N N 97  
ASP   CG  OD1  doub N N 98  
ASP   CG  OD2  sing N N 99  
ASP   OD2 HD2  sing N N 100 
ASP   OXT HXT  sing N N 101 
CYS   N   CA   sing N N 102 
CYS   N   H    sing N N 103 
CYS   N   H2   sing N N 104 
CYS   CA  C    sing N N 105 
CYS   CA  CB   sing N N 106 
CYS   CA  HA   sing N N 107 
CYS   C   O    doub N N 108 
CYS   C   OXT  sing N N 109 
CYS   CB  SG   sing N N 110 
CYS   CB  HB2  sing N N 111 
CYS   CB  HB3  sing N N 112 
CYS   SG  HG   sing N N 113 
CYS   OXT HXT  sing N N 114 
GLN   N   CA   sing N N 115 
GLN   N   H    sing N N 116 
GLN   N   H2   sing N N 117 
GLN   CA  C    sing N N 118 
GLN   CA  CB   sing N N 119 
GLN   CA  HA   sing N N 120 
GLN   C   O    doub N N 121 
GLN   C   OXT  sing N N 122 
GLN   CB  CG   sing N N 123 
GLN   CB  HB2  sing N N 124 
GLN   CB  HB3  sing N N 125 
GLN   CG  CD   sing N N 126 
GLN   CG  HG2  sing N N 127 
GLN   CG  HG3  sing N N 128 
GLN   CD  OE1  doub N N 129 
GLN   CD  NE2  sing N N 130 
GLN   NE2 HE21 sing N N 131 
GLN   NE2 HE22 sing N N 132 
GLN   OXT HXT  sing N N 133 
GLU   N   CA   sing N N 134 
GLU   N   H    sing N N 135 
GLU   N   H2   sing N N 136 
GLU   CA  C    sing N N 137 
GLU   CA  CB   sing N N 138 
GLU   CA  HA   sing N N 139 
GLU   C   O    doub N N 140 
GLU   C   OXT  sing N N 141 
GLU   CB  CG   sing N N 142 
GLU   CB  HB2  sing N N 143 
GLU   CB  HB3  sing N N 144 
GLU   CG  CD   sing N N 145 
GLU   CG  HG2  sing N N 146 
GLU   CG  HG3  sing N N 147 
GLU   CD  OE1  doub N N 148 
GLU   CD  OE2  sing N N 149 
GLU   OE2 HE2  sing N N 150 
GLU   OXT HXT  sing N N 151 
GLY   N   CA   sing N N 152 
GLY   N   H    sing N N 153 
GLY   N   H2   sing N N 154 
GLY   CA  C    sing N N 155 
GLY   CA  HA2  sing N N 156 
GLY   CA  HA3  sing N N 157 
GLY   C   O    doub N N 158 
GLY   C   OXT  sing N N 159 
GLY   OXT HXT  sing N N 160 
HIS   N   CA   sing N N 161 
HIS   N   H    sing N N 162 
HIS   N   H2   sing N N 163 
HIS   CA  C    sing N N 164 
HIS   CA  CB   sing N N 165 
HIS   CA  HA   sing N N 166 
HIS   C   O    doub N N 167 
HIS   C   OXT  sing N N 168 
HIS   CB  CG   sing N N 169 
HIS   CB  HB2  sing N N 170 
HIS   CB  HB3  sing N N 171 
HIS   CG  ND1  sing Y N 172 
HIS   CG  CD2  doub Y N 173 
HIS   ND1 CE1  doub Y N 174 
HIS   ND1 HD1  sing N N 175 
HIS   CD2 NE2  sing Y N 176 
HIS   CD2 HD2  sing N N 177 
HIS   CE1 NE2  sing Y N 178 
HIS   CE1 HE1  sing N N 179 
HIS   NE2 HE2  sing N N 180 
HIS   OXT HXT  sing N N 181 
HOH   O   H1   sing N N 182 
HOH   O   H2   sing N N 183 
ILE   N   CA   sing N N 184 
ILE   N   H    sing N N 185 
ILE   N   H2   sing N N 186 
ILE   CA  C    sing N N 187 
ILE   CA  CB   sing N N 188 
ILE   CA  HA   sing N N 189 
ILE   C   O    doub N N 190 
ILE   C   OXT  sing N N 191 
ILE   CB  CG1  sing N N 192 
ILE   CB  CG2  sing N N 193 
ILE   CB  HB   sing N N 194 
ILE   CG1 CD1  sing N N 195 
ILE   CG1 HG12 sing N N 196 
ILE   CG1 HG13 sing N N 197 
ILE   CG2 HG21 sing N N 198 
ILE   CG2 HG22 sing N N 199 
ILE   CG2 HG23 sing N N 200 
ILE   CD1 HD11 sing N N 201 
ILE   CD1 HD12 sing N N 202 
ILE   CD1 HD13 sing N N 203 
ILE   OXT HXT  sing N N 204 
LEU   N   CA   sing N N 205 
LEU   N   H    sing N N 206 
LEU   N   H2   sing N N 207 
LEU   CA  C    sing N N 208 
LEU   CA  CB   sing N N 209 
LEU   CA  HA   sing N N 210 
LEU   C   O    doub N N 211 
LEU   C   OXT  sing N N 212 
LEU   CB  CG   sing N N 213 
LEU   CB  HB2  sing N N 214 
LEU   CB  HB3  sing N N 215 
LEU   CG  CD1  sing N N 216 
LEU   CG  CD2  sing N N 217 
LEU   CG  HG   sing N N 218 
LEU   CD1 HD11 sing N N 219 
LEU   CD1 HD12 sing N N 220 
LEU   CD1 HD13 sing N N 221 
LEU   CD2 HD21 sing N N 222 
LEU   CD2 HD22 sing N N 223 
LEU   CD2 HD23 sing N N 224 
LEU   OXT HXT  sing N N 225 
LYS   N   CA   sing N N 226 
LYS   N   H    sing N N 227 
LYS   N   H2   sing N N 228 
LYS   CA  C    sing N N 229 
LYS   CA  CB   sing N N 230 
LYS   CA  HA   sing N N 231 
LYS   C   O    doub N N 232 
LYS   C   OXT  sing N N 233 
LYS   CB  CG   sing N N 234 
LYS   CB  HB2  sing N N 235 
LYS   CB  HB3  sing N N 236 
LYS   CG  CD   sing N N 237 
LYS   CG  HG2  sing N N 238 
LYS   CG  HG3  sing N N 239 
LYS   CD  CE   sing N N 240 
LYS   CD  HD2  sing N N 241 
LYS   CD  HD3  sing N N 242 
LYS   CE  NZ   sing N N 243 
LYS   CE  HE2  sing N N 244 
LYS   CE  HE3  sing N N 245 
LYS   NZ  HZ1  sing N N 246 
LYS   NZ  HZ2  sing N N 247 
LYS   NZ  HZ3  sing N N 248 
LYS   OXT HXT  sing N N 249 
MET   N   CA   sing N N 250 
MET   N   H    sing N N 251 
MET   N   H2   sing N N 252 
MET   CA  C    sing N N 253 
MET   CA  CB   sing N N 254 
MET   CA  HA   sing N N 255 
MET   C   O    doub N N 256 
MET   C   OXT  sing N N 257 
MET   CB  CG   sing N N 258 
MET   CB  HB2  sing N N 259 
MET   CB  HB3  sing N N 260 
MET   CG  SD   sing N N 261 
MET   CG  HG2  sing N N 262 
MET   CG  HG3  sing N N 263 
MET   SD  CE   sing N N 264 
MET   CE  HE1  sing N N 265 
MET   CE  HE2  sing N N 266 
MET   CE  HE3  sing N N 267 
MET   OXT HXT  sing N N 268 
PHE   N   CA   sing N N 269 
PHE   N   H    sing N N 270 
PHE   N   H2   sing N N 271 
PHE   CA  C    sing N N 272 
PHE   CA  CB   sing N N 273 
PHE   CA  HA   sing N N 274 
PHE   C   O    doub N N 275 
PHE   C   OXT  sing N N 276 
PHE   CB  CG   sing N N 277 
PHE   CB  HB2  sing N N 278 
PHE   CB  HB3  sing N N 279 
PHE   CG  CD1  doub Y N 280 
PHE   CG  CD2  sing Y N 281 
PHE   CD1 CE1  sing Y N 282 
PHE   CD1 HD1  sing N N 283 
PHE   CD2 CE2  doub Y N 284 
PHE   CD2 HD2  sing N N 285 
PHE   CE1 CZ   doub Y N 286 
PHE   CE1 HE1  sing N N 287 
PHE   CE2 CZ   sing Y N 288 
PHE   CE2 HE2  sing N N 289 
PHE   CZ  HZ   sing N N 290 
PHE   OXT HXT  sing N N 291 
PRO   N   CA   sing N N 292 
PRO   N   CD   sing N N 293 
PRO   N   H    sing N N 294 
PRO   CA  C    sing N N 295 
PRO   CA  CB   sing N N 296 
PRO   CA  HA   sing N N 297 
PRO   C   O    doub N N 298 
PRO   C   OXT  sing N N 299 
PRO   CB  CG   sing N N 300 
PRO   CB  HB2  sing N N 301 
PRO   CB  HB3  sing N N 302 
PRO   CG  CD   sing N N 303 
PRO   CG  HG2  sing N N 304 
PRO   CG  HG3  sing N N 305 
PRO   CD  HD2  sing N N 306 
PRO   CD  HD3  sing N N 307 
PRO   OXT HXT  sing N N 308 
SER   N   CA   sing N N 309 
SER   N   H    sing N N 310 
SER   N   H2   sing N N 311 
SER   CA  C    sing N N 312 
SER   CA  CB   sing N N 313 
SER   CA  HA   sing N N 314 
SER   C   O    doub N N 315 
SER   C   OXT  sing N N 316 
SER   CB  OG   sing N N 317 
SER   CB  HB2  sing N N 318 
SER   CB  HB3  sing N N 319 
SER   OG  HG   sing N N 320 
SER   OXT HXT  sing N N 321 
TFA   C1  C2   sing N N 322 
TFA   C1  O    doub N N 323 
TFA   C1  OXT  sing N N 324 
TFA   C2  F1   sing N N 325 
TFA   C2  F2   sing N N 326 
TFA   C2  F3   sing N N 327 
TFA   OXT HXT  sing N N 328 
THR   N   CA   sing N N 329 
THR   N   H    sing N N 330 
THR   N   H2   sing N N 331 
THR   CA  C    sing N N 332 
THR   CA  CB   sing N N 333 
THR   CA  HA   sing N N 334 
THR   C   O    doub N N 335 
THR   C   OXT  sing N N 336 
THR   CB  OG1  sing N N 337 
THR   CB  CG2  sing N N 338 
THR   CB  HB   sing N N 339 
THR   OG1 HG1  sing N N 340 
THR   CG2 HG21 sing N N 341 
THR   CG2 HG22 sing N N 342 
THR   CG2 HG23 sing N N 343 
THR   OXT HXT  sing N N 344 
TYR   N   CA   sing N N 345 
TYR   N   H    sing N N 346 
TYR   N   H2   sing N N 347 
TYR   CA  C    sing N N 348 
TYR   CA  CB   sing N N 349 
TYR   CA  HA   sing N N 350 
TYR   C   O    doub N N 351 
TYR   C   OXT  sing N N 352 
TYR   CB  CG   sing N N 353 
TYR   CB  HB2  sing N N 354 
TYR   CB  HB3  sing N N 355 
TYR   CG  CD1  doub Y N 356 
TYR   CG  CD2  sing Y N 357 
TYR   CD1 CE1  sing Y N 358 
TYR   CD1 HD1  sing N N 359 
TYR   CD2 CE2  doub Y N 360 
TYR   CD2 HD2  sing N N 361 
TYR   CE1 CZ   doub Y N 362 
TYR   CE1 HE1  sing N N 363 
TYR   CE2 CZ   sing Y N 364 
TYR   CE2 HE2  sing N N 365 
TYR   CZ  OH   sing N N 366 
TYR   OH  HH   sing N N 367 
TYR   OXT HXT  sing N N 368 
VAL   N   CA   sing N N 369 
VAL   N   H    sing N N 370 
VAL   N   H2   sing N N 371 
VAL   CA  C    sing N N 372 
VAL   CA  CB   sing N N 373 
VAL   CA  HA   sing N N 374 
VAL   C   O    doub N N 375 
VAL   C   OXT  sing N N 376 
VAL   CB  CG1  sing N N 377 
VAL   CB  CG2  sing N N 378 
VAL   CB  HB   sing N N 379 
VAL   CG1 HG11 sing N N 380 
VAL   CG1 HG12 sing N N 381 
VAL   CG1 HG13 sing N N 382 
VAL   CG2 HG21 sing N N 383 
VAL   CG2 HG22 sing N N 384 
VAL   CG2 HG23 sing N N 385 
VAL   OXT HXT  sing N N 386 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171110 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_title         
'PanDDA analysis group deposition of SARS-CoV-2 NSP3 macrodomain ligand screen - FrankenROCS hits and analogues of AVI-313' 
_pdbx_deposit_group.group_description   
'SARS-CoV-2 NSP3 macrodomain in complex with ligands identified by X-ray diffraction using ALS 8.3.1,  SSRL 9-2, and SSRL 12-2' 
_pdbx_deposit_group.group_type          'changed state' 
_pdbx_deposit_group.group_id            G_1002304 
# 
_atom_sites.entry_id                    7HDM 
_atom_sites.fract_transf_matrix[1][1]   0.011266 
_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]   0.011266 
_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]   0.025254 
_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 
F 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    A VAL   A 1 3   ? 19.691 -16.256 22.260  0.68 54.08 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.641 -16.240 22.324  0.32 53.22 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.718 -15.183 22.426  0.68 53.65 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.699 -15.143 22.510  0.32 52.89 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.370 -13.833 22.149  0.68 52.05 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.364 -13.815 22.173  0.32 51.61 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.477 -13.560 22.614  0.68 52.47 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.479 -13.540 22.618  0.32 51.97 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.070 -15.226 23.826  0.68 54.47 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.129 -15.131 23.943  0.32 53.55 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 17.041 -14.113 23.974  0.68 54.71 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 17.120 -14.002 24.106  0.32 53.75 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.428 -16.584 24.070  0.68 54.72 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.495 -16.473 24.277  0.32 53.76 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 18.009 -15.299 21.779  0.68 64.35 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.955 -15.261 21.903  0.32 63.44 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.755 -15.093 24.500  0.68 65.34 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.852 -14.977 24.571  0.32 64.24 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.531 -14.261 24.786  0.68 65.63 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.653 -14.117 24.949  0.32 64.48 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.500 -13.260 24.024  0.68 65.63 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.589 -13.153 24.102  0.32 64.48 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.449 -14.127 23.206  0.68 65.63 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.488 -14.036 23.371  0.32 64.48 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 16.959 -16.564 24.919  0.68 65.64 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 17.077 -16.416 25.150  0.32 64.49 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.802 -16.770 23.352  0.68 65.64 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.829 -16.683 23.604  0.32 64.49 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.120 -17.263 24.090  0.68 65.64 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.184 -17.155 24.284  0.32 64.49 ?  3   VAL   A HG23 1 
ATOM   31   N N    . ASN   A 1 4   ? 18.678 -12.995 21.379  1.00 49.66 ?  4   ASN   A N    1 
ATOM   32   C CA   . ASN   A 1 4   ? 19.138 -11.650 21.050  1.00 45.01 ?  4   ASN   A CA   1 
ATOM   33   C C    . ASN   A 1 4   ? 18.003 -10.663 21.302  1.00 41.20 ?  4   ASN   A C    1 
ATOM   34   O O    . ASN   A 1 4   ? 16.887 -11.045 21.670  1.00 40.98 ?  4   ASN   A O    1 
ATOM   35   C CB   . ASN   A 1 4   ? 19.675 -11.558 19.614  1.00 43.93 ?  4   ASN   A CB   1 
ATOM   36   C CG   . ASN   A 1 4   ? 18.650 -11.956 18.576  1.00 42.90 ?  4   ASN   A CG   1 
ATOM   37   O OD1  . ASN   A 1 4   ? 17.526 -11.452 18.572  1.00 42.57 ?  4   ASN   A OD1  1 
ATOM   38   N ND2  . ASN   A 1 4   ? 19.033 -12.867 17.686  1.00 42.58 ?  4   ASN   A ND2  1 
ATOM   39   H H    A ASN   A 1 4   ? 17.916 -13.191 21.028  0.68 59.56 ?  4   ASN   A H    1 
ATOM   40   H H    B ASN   A 1 4   ? 17.924 -13.200 21.015  0.32 59.56 ?  4   ASN   A H    1 
ATOM   41   H HA   . ASN   A 1 4   ? 19.864 -11.418 21.642  1.00 53.99 ?  4   ASN   A HA   1 
ATOM   42   H HB2  . ASN   A 1 4   ? 19.940 -10.640 19.434  1.00 52.69 ?  4   ASN   A HB2  1 
ATOM   43   H HB3  . ASN   A 1 4   ? 20.438 -12.147 19.523  1.00 52.69 ?  4   ASN   A HB3  1 
ATOM   44   H HD21 . ASN   A 1 4   ? 18.489 -13.128 17.073  1.00 51.08 ?  4   ASN   A HD21 1 
ATOM   45   H HD22 . ASN   A 1 4   ? 19.828 -13.196 17.723  1.00 51.08 ?  4   ASN   A HD22 1 
ATOM   46   N N    . SER   A 1 5   ? 18.294 -9.379  21.098  1.00 37.43 ?  5   SER   A N    1 
ATOM   47   C CA   . SER   A 1 5   ? 17.386 -8.309  21.488  1.00 33.85 ?  5   SER   A CA   1 
ATOM   48   C C    . SER   A 1 5   ? 16.475 -7.833  20.359  1.00 29.48 ?  5   SER   A C    1 
ATOM   49   O O    . SER   A 1 5   ? 15.735 -6.864  20.548  1.00 30.18 ?  5   SER   A O    1 
ATOM   50   C CB   . SER   A 1 5   ? 18.170 -7.129  22.073  1.00 34.84 ?  5   SER   A CB   1 
ATOM   51   O OG   . SER   A 1 5   ? 19.053 -6.571  21.118  1.00 35.35 ?  5   SER   A OG   1 
ATOM   52   H H    . SER   A 1 5   ? 19.022 -9.103  20.728  1.00 44.90 ?  5   SER   A H    1 
ATOM   53   H HA   . SER   A 1 5   ? 16.814 -8.642  22.191  1.00 40.60 ?  5   SER   A HA   1 
ATOM   54   H HB2  . SER   A 1 5   ? 17.544 -6.447  22.363  1.00 41.78 ?  5   SER   A HB2  1 
ATOM   55   H HB3  . SER   A 1 5   ? 18.689 -7.441  22.834  1.00 41.78 ?  5   SER   A HB3  1 
ATOM   56   H HG   . SER   A 1 5   ? 19.473 -5.923  21.458  1.00 42.40 ?  5   SER   A HG   1 
ATOM   57   N N    A PHE   A 1 6   ? 16.475 -8.501  19.208  0.68 26.31 ?  6   PHE   A N    1 
ATOM   58   N N    B PHE   A 1 6   ? 16.540 -8.470  19.191  0.32 27.00 ?  6   PHE   A N    1 
ATOM   59   C CA   A PHE   A 1 6   ? 15.555 -8.121  18.141  0.68 23.18 ?  6   PHE   A CA   1 
ATOM   60   C CA   B PHE   A 1 6   ? 15.632 -8.155  18.094  0.32 24.50 ?  6   PHE   A CA   1 
ATOM   61   C C    A PHE   A 1 6   ? 14.120 -8.472  18.533  0.68 23.11 ?  6   PHE   A C    1 
ATOM   62   C C    B PHE   A 1 6   ? 14.223 -8.573  18.492  0.32 23.77 ?  6   PHE   A C    1 
ATOM   63   O O    A PHE   A 1 6   ? 13.867 -9.505  19.157  0.68 24.39 ?  6   PHE   A O    1 
ATOM   64   O O    B PHE   A 1 6   ? 13.939 -9.766  18.632  0.32 23.53 ?  6   PHE   A O    1 
ATOM   65   C CB   A PHE   A 1 6   ? 15.932 -8.828  16.841  0.68 21.13 ?  6   PHE   A CB   1 
ATOM   66   C CB   B PHE   A 1 6   ? 16.071 -8.889  16.832  0.32 23.10 ?  6   PHE   A CB   1 
ATOM   67   C CG   A PHE   A 1 6   ? 17.220 -8.336  16.233  0.68 19.43 ?  6   PHE   A CG   1 
ATOM   68   C CG   B PHE   A 1 6   ? 17.321 -8.333  16.208  0.32 21.87 ?  6   PHE   A CG   1 
ATOM   69   C CD1  A PHE   A 1 6   ? 17.248 -7.169  15.492  0.68 18.52 ?  6   PHE   A CD1  1 
ATOM   70   C CD1  B PHE   A 1 6   ? 17.294 -7.120  15.542  0.32 21.33 ?  6   PHE   A CD1  1 
ATOM   71   C CD2  A PHE   A 1 6   ? 18.396 -9.045  16.400  0.68 19.77 ?  6   PHE   A CD2  1 
ATOM   72   C CD2  B PHE   A 1 6   ? 18.516 -9.028  16.276  0.32 21.63 ?  6   PHE   A CD2  1 
ATOM   73   C CE1  A PHE   A 1 6   ? 18.430 -6.715  14.930  0.68 18.50 ?  6   PHE   A CE1  1 
ATOM   74   C CE1  B PHE   A 1 6   ? 18.439 -6.605  14.962  0.32 21.18 ?  6   PHE   A CE1  1 
ATOM   75   C CE2  A PHE   A 1 6   ? 19.578 -8.599  15.841  0.68 19.92 ?  6   PHE   A CE2  1 
ATOM   76   C CE2  B PHE   A 1 6   ? 19.665 -8.520  15.697  0.32 21.58 ?  6   PHE   A CE2  1 
ATOM   77   C CZ   A PHE   A 1 6   ? 19.595 -7.432  15.104  0.68 19.16 ?  6   PHE   A CZ   1 
ATOM   78   C CZ   B PHE   A 1 6   ? 19.626 -7.307  15.039  0.32 21.32 ?  6   PHE   A CZ   1 
ATOM   79   H H    A PHE   A 1 6   ? 16.984 -9.170  19.025  0.68 31.55 ?  6   PHE   A H    1 
ATOM   80   H H    B PHE   A 1 6   ? 17.106 -9.091  19.008  0.32 32.38 ?  6   PHE   A H    1 
ATOM   81   H HA   A PHE   A 1 6   ? 15.606 -7.168  17.999  0.68 27.79 ?  6   PHE   A HA   1 
ATOM   82   H HA   B PHE   A 1 6   ? 15.641 -7.201  17.924  0.32 29.37 ?  6   PHE   A HA   1 
ATOM   83   H HB2  A PHE   A 1 6   ? 16.027 -9.779  17.019  0.68 25.33 ?  6   PHE   A HB2  1 
ATOM   84   H HB2  B PHE   A 1 6   ? 16.237 -9.819  17.055  0.32 27.70 ?  6   PHE   A HB2  1 
ATOM   85   H HB3  A PHE   A 1 6   ? 15.222 -8.687  16.194  0.68 25.33 ?  6   PHE   A HB3  1 
ATOM   86   H HB3  B PHE   A 1 6   ? 15.359 -8.830  16.177  0.32 27.70 ?  6   PHE   A HB3  1 
ATOM   87   H HD1  A PHE   A 1 6   ? 16.463 -6.685  15.371  0.68 22.21 ?  6   PHE   A HD1  1 
ATOM   88   H HD1  B PHE   A 1 6   ? 16.496 -6.646  15.489  0.32 25.57 ?  6   PHE   A HD1  1 
ATOM   89   H HD2  A PHE   A 1 6   ? 18.387 -9.834  16.899  0.68 23.70 ?  6   PHE   A HD2  1 
ATOM   90   H HD2  B PHE   A 1 6   ? 18.546 -9.846  16.720  0.32 25.93 ?  6   PHE   A HD2  1 
ATOM   91   H HE1  A PHE   A 1 6   ? 18.437 -5.930  14.433  0.68 22.17 ?  6   PHE   A HE1  1 
ATOM   92   H HE1  B PHE   A 1 6   ? 18.408 -5.788  14.519  0.32 25.40 ?  6   PHE   A HE1  1 
ATOM   93   H HE2  A PHE   A 1 6   ? 20.362 -9.083  15.963  0.68 23.88 ?  6   PHE   A HE2  1 
ATOM   94   H HE2  B PHE   A 1 6   ? 20.463 -8.995  15.752  0.32 25.87 ?  6   PHE   A HE2  1 
ATOM   95   H HZ   A PHE   A 1 6   ? 20.388 -7.128  14.728  0.68 22.97 ?  6   PHE   A HZ   1 
ATOM   96   H HZ   B PHE   A 1 6   ? 20.397 -6.962  14.649  0.32 25.57 ?  6   PHE   A HZ   1 
ATOM   97   N N    A SER   A 1 7   ? 13.173 -7.607  18.158  0.68 22.05 ?  7   SER   A N    1 
ATOM   98   N N    B SER   A 1 7   ? 13.339 -7.596  18.667  0.32 23.36 ?  7   SER   A N    1 
ATOM   99   C CA   A SER   A 1 7   ? 11.796 -7.720  18.629  0.68 22.19 ?  7   SER   A CA   1 
ATOM   100  C CA   B SER   A 1 7   ? 12.004 -7.835  19.188  0.32 23.41 ?  7   SER   A CA   1 
ATOM   101  C C    A SER   A 1 7   ? 10.804 -7.466  17.499  0.68 20.11 ?  7   SER   A C    1 
ATOM   102  C C    B SER   A 1 7   ? 10.960 -7.501  18.131  0.32 22.31 ?  7   SER   A C    1 
ATOM   103  O O    A SER   A 1 7   ? 11.013 -6.586  16.663  0.68 20.05 ?  7   SER   A O    1 
ATOM   104  O O    B SER   A 1 7   ? 11.133 -6.579  17.329  0.32 22.20 ?  7   SER   A O    1 
ATOM   105  C CB   A SER   A 1 7   ? 11.539 -6.721  19.768  0.68 24.04 ?  7   SER   A CB   1 
ATOM   106  C CB   B SER   A 1 7   ? 11.755 -6.992  20.446  0.32 24.32 ?  7   SER   A CB   1 
ATOM   107  O OG   A SER   A 1 7   ? 10.194 -6.774  20.205  0.68 25.47 ?  7   SER   A OG   1 
ATOM   108  O OG   B SER   A 1 7   ? 10.533 -7.347  21.066  0.32 25.13 ?  7   SER   A OG   1 
ATOM   109  H H    A SER   A 1 7   ? 13.309 -6.944  17.623  0.68 26.43 ?  7   SER   A H    1 
ATOM   110  H H    B SER   A 1 7   ? 13.495 -6.770  18.480  0.32 28.01 ?  7   SER   A H    1 
ATOM   111  H HA   A SER   A 1 7   ? 11.644 -8.612  18.968  0.68 26.61 ?  7   SER   A HA   1 
ATOM   112  H HA   B SER   A 1 7   ? 11.912 -8.769  19.427  0.32 28.07 ?  7   SER   A HA   1 
ATOM   113  H HB2  A SER   A 1 7   ? 12.124 -6.938  20.514  0.68 28.82 ?  7   SER   A HB2  1 
ATOM   114  H HB2  B SER   A 1 7   ? 12.482 -7.141  21.074  0.32 29.16 ?  7   SER   A HB2  1 
ATOM   115  H HB3  A SER   A 1 7   ? 11.733 -5.823  19.452  0.68 28.82 ?  7   SER   A HB3  1 
ATOM   116  H HB3  B SER   A 1 7   ? 11.723 -6.055  20.197  0.32 29.16 ?  7   SER   A HB3  1 
ATOM   117  H HG   A SER   A 1 7   ? 10.075 -6.225  20.830  0.68 30.54 ?  7   SER   A HG   1 
ATOM   118  H HG   B SER   A 1 7   ? 10.414 -6.878  21.752  0.32 30.13 ?  7   SER   A HG   1 
ATOM   119  N N    A GLY   A 1 8   ? 9.713  -8.235  17.490  0.68 18.83 ?  8   GLY   A N    1 
ATOM   120  N N    B GLY   A 1 8   ? 9.873  -8.269  18.136  0.32 21.27 ?  8   GLY   A N    1 
ATOM   121  C CA   A GLY   A 1 8   ? 8.628  -8.001  16.556  0.68 18.10 ?  8   GLY   A CA   1 
ATOM   122  C CA   B GLY   A 1 8   ? 8.754  -7.993  17.258  0.32 20.10 ?  8   GLY   A CA   1 
ATOM   123  C C    A GLY   A 1 8   ? 8.845  -8.526  15.156  0.68 17.19 ?  8   GLY   A C    1 
ATOM   124  C C    B GLY   A 1 8   ? 8.924  -8.415  15.818  0.32 18.87 ?  8   GLY   A C    1 
ATOM   125  O O    A GLY   A 1 8   ? 8.122  -8.122  14.239  0.68 17.57 ?  8   GLY   A O    1 
ATOM   126  O O    B GLY   A 1 8   ? 8.166  -7.952  14.961  0.32 18.78 ?  8   GLY   A O    1 
ATOM   127  H H    A GLY   A 1 8   ? 9.584  -8.897  18.019  0.68 22.58 ?  8   GLY   A H    1 
ATOM   128  H H    B GLY   A 1 8   ? 9.763  -8.951  18.648  0.32 25.50 ?  8   GLY   A H    1 
ATOM   129  H HA2  A GLY   A 1 8   ? 7.818  -8.407  16.910  0.68 21.70 ?  8   GLY   A HA2  1 
ATOM   130  H HA2  B GLY   A 1 8   ? 7.972  -8.450  17.599  0.32 24.09 ?  8   GLY   A HA2  1 
ATOM   131  H HA3  A GLY   A 1 8   ? 8.470  -7.045  16.488  0.68 21.70 ?  8   GLY   A HA3  1 
ATOM   132  H HA3  B GLY   A 1 8   ? 8.576  -7.040  17.273  0.32 24.09 ?  8   GLY   A HA3  1 
ATOM   133  N N    A TYR   A 1 9   ? 9.822  -9.410  14.952  0.68 15.80 ?  9   TYR   A N    1 
ATOM   134  N N    B TYR   A 1 9   ? 9.884  -9.284  15.518  0.32 18.14 ?  9   TYR   A N    1 
ATOM   135  C CA   A TYR   A 1 9   ? 10.102 -9.962  13.633  0.68 14.43 ?  9   TYR   A CA   1 
ATOM   136  C CA   B TYR   A 1 9   ? 10.100 -9.736  14.151  0.32 17.21 ?  9   TYR   A CA   1 
ATOM   137  C C    A TYR   A 1 9   ? 9.267  -11.205 13.356  0.68 13.96 ?  9   TYR   A C    1 
ATOM   138  C C    B TYR   A 1 9   ? 9.189  -10.912 13.813  0.32 16.24 ?  9   TYR   A C    1 
ATOM   139  O O    A TYR   A 1 9   ? 9.022  -12.029 14.244  0.68 15.41 ?  9   TYR   A O    1 
ATOM   140  O O    B TYR   A 1 9   ? 8.837  -11.724 14.673  0.32 16.58 ?  9   TYR   A O    1 
ATOM   141  C CB   A TYR   A 1 9   ? 11.585 -10.318 13.482  0.68 14.24 ?  9   TYR   A CB   1 
ATOM   142  C CB   B TYR   A 1 9   ? 11.558 -10.156 13.943  0.32 17.47 ?  9   TYR   A CB   1 
ATOM   143  C CG   A TYR   A 1 9   ? 12.473 -9.111  13.320  0.68 14.79 ?  9   TYR   A CG   1 
ATOM   144  C CG   B TYR   A 1 9   ? 12.508 -9.001  13.725  0.32 17.38 ?  9   TYR   A CG   1 
ATOM   145  C CD1  A TYR   A 1 9   ? 12.817 -8.340  14.417  0.68 15.38 ?  9   TYR   A CD1  1 
ATOM   146  C CD1  B TYR   A 1 9   ? 12.801 -8.117  14.753  0.32 17.66 ?  9   TYR   A CD1  1 
ATOM   147  C CD2  A TYR   A 1 9   ? 12.950 -8.731  12.074  0.68 14.72 ?  9   TYR   A CD2  1 
ATOM   148  C CD2  B TYR   A 1 9   ? 13.114 -8.798  12.492  0.32 16.84 ?  9   TYR   A CD2  1 
ATOM   149  C CE1  A TYR   A 1 9   ? 13.618 -7.223  14.282  0.68 16.01 ?  9   TYR   A CE1  1 
ATOM   150  C CE1  B TYR   A 1 9   ? 13.670 -7.063  14.560  0.32 17.66 ?  9   TYR   A CE1  1 
ATOM   151  C CE2  A TYR   A 1 9   ? 13.753 -7.614  11.926  0.68 14.93 ?  9   TYR   A CE2  1 
ATOM   152  C CE2  B TYR   A 1 9   ? 13.978 -7.742  12.287  0.32 16.95 ?  9   TYR   A CE2  1 
ATOM   153  C CZ   A TYR   A 1 9   ? 14.078 -6.861  13.031  0.68 15.78 ?  9   TYR   A CZ   1 
ATOM   154  C CZ   B TYR   A 1 9   ? 14.252 -6.879  13.324  0.32 17.50 ?  9   TYR   A CZ   1 
ATOM   155  O OH   A TYR   A 1 9   ? 14.865 -5.749  12.878  0.68 16.96 ?  9   TYR   A OH   1 
ATOM   156  O OH   B TYR   A 1 9   ? 15.116 -5.830  13.126  0.32 18.24 ?  9   TYR   A OH   1 
ATOM   157  H H    A TYR   A 1 9   ? 10.327 -9.716  15.572  0.68 18.94 ?  9   TYR   A H    1 
ATOM   158  H H    B TYR   A 1 9   ? 10.428 -9.629  16.092  0.32 21.74 ?  9   TYR   A H    1 
ATOM   159  H HA   A TYR   A 1 9   ? 9.881  -9.304  12.959  0.68 17.29 ?  9   TYR   A HA   1 
ATOM   160  H HA   B TYR   A 1 9   ? 9.905  -9.007  13.541  0.32 20.63 ?  9   TYR   A HA   1 
ATOM   161  H HB2  A TYR   A 1 9   ? 11.876 -10.811 14.265  0.68 17.06 ?  9   TYR   A HB2  1 
ATOM   162  H HB2  B TYR   A 1 9   ? 11.861 -10.646 14.721  0.32 20.94 ?  9   TYR   A HB2  1 
ATOM   163  H HB3  A TYR   A 1 9   ? 11.678 -10.867 12.689  0.68 17.06 ?  9   TYR   A HB3  1 
ATOM   164  H HB3  B TYR   A 1 9   ? 11.606 -10.726 13.159  0.32 20.94 ?  9   TYR   A HB3  1 
ATOM   165  H HD1  A TYR   A 1 9   ? 12.497 -8.581  15.260  0.68 18.43 ?  9   TYR   A HD1  1 
ATOM   166  H HD1  B TYR   A 1 9   ? 12.405 -8.237  15.586  0.32 21.17 ?  9   TYR   A HD1  1 
ATOM   167  H HD2  A TYR   A 1 9   ? 12.721 -9.234  11.323  0.68 17.64 ?  9   TYR   A HD2  1 
ATOM   168  H HD2  B TYR   A 1 9   ? 12.932 -9.380  11.789  0.32 20.18 ?  9   TYR   A HD2  1 
ATOM   169  H HE1  A TYR   A 1 9   ? 13.835 -6.717  15.030  0.68 19.19 ?  9   TYR   A HE1  1 
ATOM   170  H HE1  B TYR   A 1 9   ? 13.852 -6.475  15.257  0.32 21.17 ?  9   TYR   A HE1  1 
ATOM   171  H HE2  A TYR   A 1 9   ? 14.062 -7.368  11.083  0.68 17.89 ?  9   TYR   A HE2  1 
ATOM   172  H HE2  B TYR   A 1 9   ? 14.380 -7.618  11.457  0.32 20.32 ?  9   TYR   A HE2  1 
ATOM   173  H HH   A TYR   A 1 9   ? 15.002 -5.393  13.626  0.68 20.32 ?  9   TYR   A HH   1 
ATOM   174  H HH   B TYR   A 1 9   ? 15.191 -5.389  13.835  0.32 21.87 ?  9   TYR   A HH   1 
ATOM   175  N N    A LEU   A 1 10  ? 8.864  -11.342 12.101  0.68 13.40 ?  10  LEU   A N    1 
ATOM   176  N N    B LEU   A 1 10  ? 8.796  -10.978 12.542  0.32 15.33 ?  10  LEU   A N    1 
ATOM   177  C CA   A LEU   A 1 10  ? 8.271  -12.568 11.597  0.68 13.04 ?  10  LEU   A CA   1 
ATOM   178  C CA   B LEU   A 1 10  ? 8.116  -12.139 11.983  0.32 15.36 ?  10  LEU   A CA   1 
ATOM   179  C C    A LEU   A 1 10  ? 9.398  -13.501 11.169  0.68 12.94 ?  10  LEU   A C    1 
ATOM   180  C C    B LEU   A 1 10  ? 9.173  -13.111 11.470  0.32 14.48 ?  10  LEU   A C    1 
ATOM   181  O O    A LEU   A 1 10  ? 10.368 -13.069 10.542  0.68 13.14 ?  10  LEU   A O    1 
ATOM   182  O O    B LEU   A 1 10  ? 10.077 -12.721 10.725  0.32 14.48 ?  10  LEU   A O    1 
ATOM   183  C CB   A LEU   A 1 10  ? 7.395  -12.232 10.391  0.68 13.44 ?  10  LEU   A CB   1 
ATOM   184  C CB   B LEU   A 1 10  ? 7.203  -11.690 10.840  0.32 16.52 ?  10  LEU   A CB   1 
ATOM   185  C CG   A LEU   A 1 10  ? 6.668  -13.388 9.722   0.68 15.59 ?  10  LEU   A CG   1 
ATOM   186  C CG   B LEU   A 1 10  ? 6.408  -12.691 9.998   0.32 18.30 ?  10  LEU   A CG   1 
ATOM   187  C CD1  A LEU   A 1 10  ? 5.628  -13.959 10.662  0.68 17.06 ?  10  LEU   A CD1  1 
ATOM   188  C CD1  B LEU   A 1 10  ? 5.162  -11.999 9.479   0.32 18.90 ?  10  LEU   A CD1  1 
ATOM   189  C CD2  A LEU   A 1 10  ? 6.039  -12.926 8.420   0.68 16.97 ?  10  LEU   A CD2  1 
ATOM   190  C CD2  B LEU   A 1 10  ? 7.215  -13.218 8.829   0.32 18.97 ?  10  LEU   A CD2  1 
ATOM   191  H H    A LEU   A 1 10  ? 8.940  -10.735 11.497  0.68 16.06 ?  10  LEU   A H    1 
ATOM   192  H H    B LEU   A 1 10  ? 8.906  -10.335 11.976  0.32 18.37 ?  10  LEU   A H    1 
ATOM   193  H HA   A LEU   A 1 10  ? 7.744  -13.005 12.281  0.68 15.63 ?  10  LEU   A HA   1 
ATOM   194  H HA   B LEU   A 1 10  ? 7.574  -12.572 12.667  0.32 18.41 ?  10  LEU   A HA   1 
ATOM   195  H HB2  A LEU   A 1 10  ? 6.728  -11.601 10.678  0.68 16.10 ?  10  LEU   A HB2  1 
ATOM   196  H HB2  B LEU   A 1 10  ? 6.549  -11.081 11.218  0.32 19.80 ?  10  LEU   A HB2  1 
ATOM   197  H HB3  A LEU   A 1 10  ? 7.961  -11.826 9.715   0.68 16.10 ?  10  LEU   A HB3  1 
ATOM   198  H HB3  B LEU   A 1 10  ? 7.756  -11.198 10.217  0.32 19.80 ?  10  LEU   A HB3  1 
ATOM   199  H HG   A LEU   A 1 10  ? 7.302  -14.093 9.514   0.68 18.68 ?  10  LEU   A HG   1 
ATOM   200  H HG   B LEU   A 1 10  ? 6.131  -13.439 10.550  0.32 21.94 ?  10  LEU   A HG   1 
ATOM   201  H HD11 A LEU   A 1 10  ? 5.182  -14.704 10.229  0.68 20.45 ?  10  LEU   A HD11 1 
ATOM   202  H HD11 B LEU   A 1 10  ? 4.721  -12.580 8.841   0.32 22.65 ?  10  LEU   A HD11 1 
ATOM   203  H HD12 A LEU   A 1 10  ? 6.063  -14.264 11.474  0.68 20.45 ?  10  LEU   A HD12 1 
ATOM   204  H HD12 B LEU   A 1 10  ? 4.569  -11.810 10.222  0.32 22.65 ?  10  LEU   A HD12 1 
ATOM   205  H HD13 A LEU   A 1 10  ? 4.980  -13.268 10.876  0.68 20.45 ?  10  LEU   A HD13 1 
ATOM   206  H HD13 B LEU   A 1 10  ? 5.421  -11.169 9.044   0.32 22.65 ?  10  LEU   A HD13 1 
ATOM   207  H HD21 A LEU   A 1 10  ? 5.574  -13.675 8.014   0.68 20.34 ?  10  LEU   A HD21 1 
ATOM   208  H HD21 B LEU   A 1 10  ? 6.640  -13.764 8.270   0.32 22.74 ?  10  LEU   A HD21 1 
ATOM   209  H HD22 A LEU   A 1 10  ? 5.413  -12.212 8.611   0.68 20.34 ?  10  LEU   A HD22 1 
ATOM   210  H HD22 B LEU   A 1 10  ? 7.552  -12.464 8.316   0.32 22.74 ?  10  LEU   A HD22 1 
ATOM   211  H HD23 A LEU   A 1 10  ? 6.738  -12.609 7.829   0.68 20.34 ?  10  LEU   A HD23 1 
ATOM   212  H HD23 B LEU   A 1 10  ? 7.951  -13.746 9.165   0.32 22.74 ?  10  LEU   A HD23 1 
ATOM   213  N N    A LYS   A 1 11  ? 9.279  -14.777 11.527  0.68 12.89 ?  11  LYS   A N    1 
ATOM   214  N N    B LYS   A 1 11  ? 9.069  -14.367 11.885  0.32 13.94 ?  11  LYS   A N    1 
ATOM   215  C CA   A LYS   A 1 11  ? 10.281 -15.783 11.191  0.68 13.22 ?  11  LYS   A CA   1 
ATOM   216  C CA   B LYS   A 1 11  ? 10.044 -15.380 11.504  0.32 13.44 ?  11  LYS   A CA   1 
ATOM   217  C C    A LYS   A 1 11  ? 9.928  -16.385 9.838   0.68 13.06 ?  11  LYS   A C    1 
ATOM   218  C C    B LYS   A 1 11  ? 9.694  -15.930 10.125  0.32 12.82 ?  11  LYS   A C    1 
ATOM   219  O O    A LYS   A 1 11  ? 8.872  -17.008 9.694   0.68 15.13 ?  11  LYS   A O    1 
ATOM   220  O O    B LYS   A 1 11  ? 8.586  -16.437 9.918   0.32 12.87 ?  11  LYS   A O    1 
ATOM   221  C CB   A LYS   A 1 11  ? 10.315 -16.855 12.280  0.68 13.57 ?  11  LYS   A CB   1 
ATOM   222  C CB   B LYS   A 1 11  ? 10.049 -16.494 12.547  0.32 13.70 ?  11  LYS   A CB   1 
ATOM   223  C CG   A LYS   A 1 11  ? 11.367 -17.940 12.126  0.68 14.10 ?  11  LYS   A CG   1 
ATOM   224  C CG   B LYS   A 1 11  ? 10.996 -17.629 12.241  0.32 14.11 ?  11  LYS   A CG   1 
ATOM   225  C CD   A LYS   A 1 11  ? 11.461 -18.727 13.435  0.68 14.14 ?  11  LYS   A CD   1 
ATOM   226  C CD   B LYS   A 1 11  ? 10.941 -18.667 13.339  0.32 14.65 ?  11  LYS   A CD   1 
ATOM   227  C CE   A LYS   A 1 11  ? 12.435 -19.897 13.368  0.68 14.39 ?  11  LYS   A CE   1 
ATOM   228  C CE   B LYS   A 1 11  ? 12.015 -19.717 13.156  0.32 14.80 ?  11  LYS   A CE   1 
ATOM   229  N NZ   A LYS   A 1 11  ? 13.787 -19.460 12.958  0.68 14.18 ?  11  LYS   A NZ   1 
ATOM   230  N NZ   B LYS   A 1 11  ? 13.385 -19.140 13.238  0.32 14.91 ?  11  LYS   A NZ   1 
ATOM   231  H H    A LYS   A 1 11  ? 8.610  -15.102 11.960  0.68 15.45 ?  11  LYS   A H    1 
ATOM   232  H H    B LYS   A 1 11  ? 8.434  -14.656 12.388  0.32 16.71 ?  11  LYS   A H    1 
ATOM   233  H HA   A LYS   A 1 11  ? 11.157 -15.374 11.127  0.68 15.84 ?  11  LYS   A HA   1 
ATOM   234  H HA   B LYS   A 1 11  ? 10.927 -14.979 11.470  0.32 16.11 ?  11  LYS   A HA   1 
ATOM   235  H HB2  A LYS   A 1 11  ? 10.481 -16.419 13.128  0.68 16.27 ?  11  LYS   A HB2  1 
ATOM   236  H HB2  B LYS   A 1 11  ? 10.307 -16.116 13.405  0.32 16.42 ?  11  LYS   A HB2  1 
ATOM   237  H HB3  A LYS   A 1 11  ? 9.454  -17.298 12.304  0.68 16.27 ?  11  LYS   A HB3  1 
ATOM   238  H HB3  B LYS   A 1 11  ? 9.157  -16.864 12.610  0.32 16.42 ?  11  LYS   A HB3  1 
ATOM   239  H HG2  A LYS   A 1 11  ? 11.115 -18.550 11.414  0.68 16.89 ?  11  LYS   A HG2  1 
ATOM   240  H HG2  B LYS   A 1 11  ? 10.739 -18.052 11.406  0.32 16.91 ?  11  LYS   A HG2  1 
ATOM   241  H HG3  A LYS   A 1 11  ? 12.233 -17.540 11.942  0.68 16.89 ?  11  LYS   A HG3  1 
ATOM   242  H HG3  B LYS   A 1 11  ? 11.902 -17.286 12.183  0.32 16.91 ?  11  LYS   A HG3  1 
ATOM   243  H HD2  A LYS   A 1 11  ? 11.759 -18.132 14.140  0.68 16.95 ?  11  LYS   A HD2  1 
ATOM   244  H HD2  B LYS   A 1 11  ? 11.075 -18.234 14.196  0.32 17.55 ?  11  LYS   A HD2  1 
ATOM   245  H HD3  A LYS   A 1 11  ? 10.585 -19.084 13.650  0.68 16.95 ?  11  LYS   A HD3  1 
ATOM   246  H HD3  B LYS   A 1 11  ? 10.075 -19.107 13.317  0.32 17.55 ?  11  LYS   A HD3  1 
ATOM   247  H HE2  A LYS   A 1 11  ? 12.506 -20.307 14.247  0.68 17.25 ?  11  LYS   A HE2  1 
ATOM   248  H HE2  B LYS   A 1 11  ? 11.926 -20.384 13.852  0.32 17.73 ?  11  LYS   A HE2  1 
ATOM   249  H HE3  A LYS   A 1 11  ? 12.118 -20.545 12.722  0.68 17.25 ?  11  LYS   A HE3  1 
ATOM   250  H HE3  B LYS   A 1 11  ? 11.912 -20.126 12.283  0.32 17.73 ?  11  LYS   A HE3  1 
ATOM   251  H HZ1  A LYS   A 1 11  ? 14.337 -20.161 12.928  0.68 16.99 ?  11  LYS   A HZ1  1 
ATOM   252  H HZ1  B LYS   A 1 11  ? 13.990 -19.790 13.202  0.32 17.86 ?  11  LYS   A HZ1  1 
ATOM   253  H HZ2  A LYS   A 1 11  ? 13.754 -19.086 12.152  0.68 16.99 ?  11  LYS   A HZ2  1 
ATOM   254  H HZ2  B LYS   A 1 11  ? 13.522 -18.579 12.561  0.32 17.86 ?  11  LYS   A HZ2  1 
ATOM   255  H HZ3  A LYS   A 1 11  ? 14.107 -18.868 13.539  0.68 16.99 ?  11  LYS   A HZ3  1 
ATOM   256  H HZ3  B LYS   A 1 11  ? 13.483 -18.697 14.005  0.32 17.86 ?  11  LYS   A HZ3  1 
ATOM   257  N N    A LEU   A 1 12  ? 10.804 -16.209 8.846   0.68 12.16 ?  12  LEU   A N    1 
ATOM   258  N N    B LEU   A 1 12  ? 10.624 -15.817 9.176   0.32 13.24 ?  12  LEU   A N    1 
ATOM   259  C CA   A LEU   A 1 12  ? 10.551 -16.792 7.531   0.68 12.35 ?  12  LEU   A CA   1 
ATOM   260  C CA   B LEU   A 1 12  ? 10.396 -16.335 7.829   0.32 13.33 ?  12  LEU   A CA   1 
ATOM   261  C C    A LEU   A 1 12  ? 11.144 -18.187 7.388   0.68 12.22 ?  12  LEU   A C    1 
ATOM   262  C C    B LEU   A 1 12  ? 10.947 -17.747 7.649   0.32 12.98 ?  12  LEU   A C    1 
ATOM   263  O O    A LEU   A 1 12  ? 10.516 -19.065 6.788   0.68 12.39 ?  12  LEU   A O    1 
ATOM   264  O O    B LEU   A 1 12  ? 10.255 -18.625 7.122   0.32 13.31 ?  12  LEU   A O    1 
ATOM   265  C CB   A LEU   A 1 12  ? 11.109 -15.897 6.419   0.68 13.01 ?  12  LEU   A CB   1 
ATOM   266  C CB   B LEU   A 1 12  ? 11.003 -15.399 6.780   0.32 14.46 ?  12  LEU   A CB   1 
ATOM   267  C CG   A LEU   A 1 12  ? 10.477 -14.513 6.275   0.68 14.21 ?  12  LEU   A CG   1 
ATOM   268  C CG   B LEU   A 1 12  ? 10.218 -14.126 6.463   0.32 15.16 ?  12  LEU   A CG   1 
ATOM   269  C CD1  A LEU   A 1 12  ? 11.173 -13.741 5.164   0.68 15.01 ?  12  LEU   A CD1  1 
ATOM   270  C CD1  B LEU   A 1 12  ? 11.009 -13.242 5.522   0.32 15.53 ?  12  LEU   A CD1  1 
ATOM   271  C CD2  A LEU   A 1 12  ? 8.985  -14.627 6.010   0.68 15.55 ?  12  LEU   A CD2  1 
ATOM   272  C CD2  B LEU   A 1 12  ? 8.865  -14.465 5.854   0.32 15.86 ?  12  LEU   A CD2  1 
ATOM   273  H H    A LEU   A 1 12  ? 11.542 -15.757 8.903   0.68 14.57 ?  12  LEU   A H    1 
ATOM   274  H H    B LEU   A 1 12  ? 11.381 -15.420 9.284   0.32 15.87 ?  12  LEU   A H    1 
ATOM   275  H HA   A LEU   A 1 12  ? 9.595  -16.866 7.403   0.68 14.80 ?  12  LEU   A HA   1 
ATOM   276  H HA   B LEU   A 1 12  ? 9.441  -16.368 7.674   0.32 15.98 ?  12  LEU   A HA   1 
ATOM   277  H HB2  A LEU   A 1 12  ? 12.056 -15.769 6.580   0.68 15.59 ?  12  LEU   A HB2  1 
ATOM   278  H HB2  B LEU   A 1 12  ? 11.881 -15.125 7.083   0.32 17.33 ?  12  LEU   A HB2  1 
ATOM   279  H HB3  A LEU   A 1 12  ? 10.989 -16.359 5.572   0.68 15.59 ?  12  LEU   A HB3  1 
ATOM   280  H HB3  B LEU   A 1 12  ? 11.088 -15.893 5.949   0.32 17.33 ?  12  LEU   A HB3  1 
ATOM   281  H HG   A LEU   A 1 12  ? 10.601 -14.025 7.102   0.68 17.03 ?  12  LEU   A HG   1 
ATOM   282  H HG   B LEU   A 1 12  ? 10.066 -13.629 7.283   0.32 18.17 ?  12  LEU   A HG   1 
ATOM   283  H HD11 A LEU   A 1 12  ? 10.767 -12.865 5.083   0.68 17.99 ?  12  LEU   A HD11 1 
ATOM   284  H HD11 B LEU   A 1 12  ? 10.499 -12.437 5.339   0.32 18.61 ?  12  LEU   A HD11 1 
ATOM   285  H HD12 A LEU   A 1 12  ? 12.116 -13.649 5.383   0.68 17.99 ?  12  LEU   A HD12 1 
ATOM   286  H HD12 B LEU   A 1 12  ? 11.853 -13.009 5.942   0.32 18.61 ?  12  LEU   A HD12 1 
ATOM   287  H HD13 A LEU   A 1 12  ? 11.078 -14.229 4.329   0.68 17.99 ?  12  LEU   A HD13 1 
ATOM   288  H HD13 B LEU   A 1 12  ? 11.173 -13.726 4.698   0.32 18.61 ?  12  LEU   A HD13 1 
ATOM   289  H HD21 A LEU   A 1 12  ? 8.640  -13.755 5.770   0.68 18.63 ?  12  LEU   A HD21 1 
ATOM   290  H HD21 B LEU   A 1 12  ? 8.474  -13.661 5.479   0.32 19.01 ?  12  LEU   A HD21 1 
ATOM   291  H HD22 A LEU   A 1 12  ? 8.841  -15.252 5.280   0.68 18.63 ?  12  LEU   A HD22 1 
ATOM   292  H HD22 B LEU   A 1 12  ? 8.993  -15.127 5.154   0.32 19.01 ?  12  LEU   A HD22 1 
ATOM   293  H HD23 A LEU   A 1 12  ? 8.545  -14.950 6.811   0.68 18.63 ?  12  LEU   A HD23 1 
ATOM   294  H HD23 B LEU   A 1 12  ? 8.287  -14.824 6.545   0.32 19.01 ?  12  LEU   A HD23 1 
ATOM   295  N N    A THR   A 1 13  ? 12.355 -18.390 7.901   0.68 12.71 ?  13  THR   A N    1 
ATOM   296  N N    B THR   A 1 13  ? 12.192 -17.975 8.054   0.32 12.84 ?  13  THR   A N    1 
ATOM   297  C CA   A THR   A 1 13  ? 13.054 -19.669 7.827   0.68 13.15 ?  13  THR   A CA   1 
ATOM   298  C CA   B THR   A 1 13  ? 12.810 -19.289 7.960   0.32 13.11 ?  13  THR   A CA   1 
ATOM   299  C C    A THR   A 1 13  ? 13.828 -19.872 9.125   0.68 13.28 ?  13  THR   A C    1 
ATOM   300  C C    B THR   A 1 13  ? 13.573 -19.551 9.252   0.32 13.79 ?  13  THR   A C    1 
ATOM   301  O O    A THR   A 1 13  ? 13.723 -19.085 10.071  0.68 13.57 ?  13  THR   A O    1 
ATOM   302  O O    B THR   A 1 13  ? 13.471 -18.803 10.231  0.32 14.38 ?  13  THR   A O    1 
ATOM   303  C CB   A THR   A 1 13  ? 14.030 -19.732 6.645   0.68 14.22 ?  13  THR   A CB   1 
ATOM   304  C CB   B THR   A 1 13  ? 13.748 -19.386 6.748   0.32 13.23 ?  13  THR   A CB   1 
ATOM   305  O OG1  A THR   A 1 13  ? 15.105 -18.821 6.881   0.68 14.82 ?  13  THR   A OG1  1 
ATOM   306  O OG1  B THR   A 1 13  ? 14.851 -18.495 6.933   0.32 13.20 ?  13  THR   A OG1  1 
ATOM   307  C CG2  A THR   A 1 13  ? 13.359 -19.385 5.334   0.68 14.99 ?  13  THR   A CG2  1 
ATOM   308  C CG2  B THR   A 1 13  ? 13.023 -19.040 5.448   0.32 13.42 ?  13  THR   A CG2  1 
ATOM   309  H H    A THR   A 1 13  ? 12.806 -17.786 8.298   0.68 15.23 ?  13  THR   A H    1 
ATOM   310  H H    B THR   A 1 13  ? 12.703 -17.370 8.385   0.32 15.38 ?  13  THR   A H    1 
ATOM   311  H HA   A THR   A 1 13  ? 12.411 -20.396 7.733   0.68 15.76 ?  13  THR   A HA   1 
ATOM   312  H HA   B THR   A 1 13  ? 12.117 -19.960 7.862   0.32 15.71 ?  13  THR   A HA   1 
ATOM   313  H HB   A THR   A 1 13  ? 14.389 -20.631 6.571   0.68 17.04 ?  13  THR   A HB   1 
ATOM   314  H HB   B THR   A 1 13  ? 14.080 -20.293 6.672   0.32 15.85 ?  13  THR   A HB   1 
ATOM   315  H HG1  A THR   A 1 13  ? 15.650 -18.843 6.237   0.68 17.76 ?  13  THR   A HG1  1 
ATOM   316  H HG1  B THR   A 1 13  ? 15.369 -18.538 6.271   0.32 15.82 ?  13  THR   A HG1  1 
ATOM   317  H HG21 A THR   A 1 13  ? 13.973 -19.545 4.598   0.68 17.96 ?  13  THR   A HG21 1 
ATOM   318  H HG21 B THR   A 1 13  ? 13.622 -19.162 4.692   0.32 16.08 ?  13  THR   A HG21 1 
ATOM   319  H HG22 A THR   A 1 13  ? 12.573 -19.940 5.211   0.68 17.96 ?  13  THR   A HG22 1 
ATOM   320  H HG22 B THR   A 1 13  ? 12.254 -19.623 5.332   0.32 16.08 ?  13  THR   A HG22 1 
ATOM   321  H HG23 A THR   A 1 13  ? 13.096 -18.455 5.332   0.68 17.96 ?  13  THR   A HG23 1 
ATOM   322  H HG23 B THR   A 1 13  ? 12.722 -18.121 5.467   0.32 16.08 ?  13  THR   A HG23 1 
ATOM   323  N N    A ASP   A 1 14  ? 14.644 -20.928 9.153   0.68 13.89 ?  14  ASP   A N    1 
ATOM   324  N N    B ASP   A 1 14  ? 14.353 -20.631 9.240   0.32 14.48 ?  14  ASP   A N    1 
ATOM   325  C CA   A ASP   A 1 14  ? 15.473 -21.186 10.323  0.68 14.86 ?  14  ASP   A CA   1 
ATOM   326  C CA   B ASP   A 1 14  ? 15.200 -20.964 10.377  0.32 15.24 ?  14  ASP   A CA   1 
ATOM   327  C C    A ASP   A 1 14  ? 16.305 -19.972 10.726  0.68 14.25 ?  14  ASP   A C    1 
ATOM   328  C C    B ASP   A 1 14  ? 16.096 -19.790 10.755  0.32 14.41 ?  14  ASP   A C    1 
ATOM   329  O O    A ASP   A 1 14  ? 16.591 -19.786 11.915  0.68 14.98 ?  14  ASP   A O    1 
ATOM   330  O O    B ASP   A 1 14  ? 16.229 -19.456 11.938  0.32 14.36 ?  14  ASP   A O    1 
ATOM   331  C CB   A ASP   A 1 14  ? 16.406 -22.360 10.048  0.68 17.79 ?  14  ASP   A CB   1 
ATOM   332  C CB   B ASP   A 1 14  ? 16.044 -22.189 10.019  0.32 17.03 ?  14  ASP   A CB   1 
ATOM   333  C CG   A ASP   A 1 14  ? 17.358 -22.597 11.179  0.68 21.32 ?  14  ASP   A CG   1 
ATOM   334  C CG   B ASP   A 1 14  ? 16.880 -22.700 11.190  0.32 18.77 ?  14  ASP   A CG   1 
ATOM   335  O OD1  A ASP   A 1 14  ? 16.907 -23.035 12.259  0.68 22.60 ?  14  ASP   A OD1  1 
ATOM   336  O OD1  B ASP   A 1 14  ? 16.333 -22.834 12.306  0.32 19.56 ?  14  ASP   A OD1  1 
ATOM   337  O OD2  A ASP   A 1 14  ? 18.557 -22.334 10.984  0.68 22.95 -1 14  ASP   A OD2  1 
ATOM   338  O OD2  B ASP   A 1 14  ? 18.082 -22.993 10.989  0.32 19.56 -1 14  ASP   A OD2  1 
ATOM   339  H H    A ASP   A 1 14  ? 14.747 -21.497 8.511   0.68 16.65 ?  14  ASP   A H    1 
ATOM   340  H H    B ASP   A 1 14  ? 14.405 -21.174 8.581   0.32 17.36 ?  14  ASP   A H    1 
ATOM   341  H HA   A ASP   A 1 14  ? 14.909 -21.427 11.071  0.68 17.81 ?  14  ASP   A HA   1 
ATOM   342  H HA   B ASP   A 1 14  ? 14.637 -21.182 11.138  0.32 18.26 ?  14  ASP   A HA   1 
ATOM   343  H HB2  A ASP   A 1 14  ? 15.877 -23.175 9.923   0.68 21.32 ?  14  ASP   A HB2  1 
ATOM   344  H HB2  B ASP   A 1 14  ? 15.445 -22.894 9.710   0.32 20.41 ?  14  ASP   A HB2  1 
ATOM   345  H HB3  A ASP   A 1 14  ? 16.930 -22.190 9.252   0.68 21.32 ?  14  ASP   A HB3  1 
ATOM   346  H HB3  B ASP   A 1 14  ? 16.654 -21.945 9.307   0.32 20.41 ?  14  ASP   A HB3  1 
ATOM   347  N N    . ASN   A 1 15  ? 16.703 -19.137 9.761   1.00 14.00 ?  15  ASN   A N    1 
ATOM   348  C CA   . ASN   A 1 15  ? 17.690 -18.091 10.012  1.00 14.66 ?  15  ASN   A CA   1 
ATOM   349  C C    . ASN   A 1 15  ? 17.325 -16.705 9.493   1.00 14.78 ?  15  ASN   A C    1 
ATOM   350  O O    . ASN   A 1 15  ? 18.096 -15.769 9.726   1.00 16.13 ?  15  ASN   A O    1 
ATOM   351  C CB   . ASN   A 1 15  ? 19.058 -18.493 9.430   1.00 14.55 ?  15  ASN   A CB   1 
ATOM   352  C CG   . ASN   A 1 15  ? 19.043 -18.584 7.920   1.00 14.60 ?  15  ASN   A CG   1 
ATOM   353  O OD1  . ASN   A 1 15  ? 18.325 -19.405 7.346   1.00 15.63 ?  15  ASN   A OD1  1 
ATOM   354  N ND2  . ASN   A 1 15  ? 19.834 -17.737 7.262   1.00 14.49 ?  15  ASN   A ND2  1 
ATOM   355  H H    A ASN   A 1 15  ? 16.400 -19.150 8.960   0.68 16.77 ?  15  ASN   A H    1 
ATOM   356  H H    B ASN   A 1 15  ? 16.560 -19.288 8.930   0.32 16.77 ?  15  ASN   A H    1 
ATOM   357  H HA   . ASN   A 1 15  ? 17.813 -18.005 10.968  1.00 17.57 ?  15  ASN   A HA   1 
ATOM   358  H HB2  . ASN   A 1 15  ? 19.723 -17.826 9.689   1.00 17.44 ?  15  ASN   A HB2  1 
ATOM   359  H HB3  . ASN   A 1 15  ? 19.316 -19.360 9.782   1.00 17.44 ?  15  ASN   A HB3  1 
ATOM   360  H HD21 . ASN   A 1 15  ? 19.857 -17.748 6.402   1.00 17.36 ?  15  ASN   A HD21 1 
ATOM   361  H HD22 . ASN   A 1 15  ? 20.325 -17.172 7.694   1.00 17.36 ?  15  ASN   A HD22 1 
ATOM   362  N N    A VAL   A 1 16  ? 16.185 -16.526 8.828   0.68 14.24 ?  16  VAL   A N    1 
ATOM   363  N N    B VAL   A 1 16  ? 16.205 -16.552 8.791   0.32 14.18 ?  16  VAL   A N    1 
ATOM   364  C CA   A VAL   A 1 16  ? 15.797 -15.237 8.263   0.68 14.01 ?  16  VAL   A CA   1 
ATOM   365  C CA   B VAL   A 1 16  ? 15.801 -15.283 8.195   0.32 13.86 ?  16  VAL   A CA   1 
ATOM   366  C C    A VAL   A 1 16  ? 14.517 -14.746 8.929   0.68 13.94 ?  16  VAL   A C    1 
ATOM   367  C C    B VAL   A 1 16  ? 14.563 -14.768 8.915   0.32 13.58 ?  16  VAL   A C    1 
ATOM   368  O O    A VAL   A 1 16  ? 13.521 -15.480 9.009   0.68 14.34 ?  16  VAL   A O    1 
ATOM   369  O O    B VAL   A 1 16  ? 13.541 -15.463 8.996   0.32 13.74 ?  16  VAL   A O    1 
ATOM   370  C CB   A VAL   A 1 16  ? 15.630 -15.294 6.735   0.68 14.35 ?  16  VAL   A CB   1 
ATOM   371  C CB   B VAL   A 1 16  ? 15.541 -15.420 6.685   0.32 14.19 ?  16  VAL   A CB   1 
ATOM   372  C CG1  A VAL   A 1 16  ? 15.227 -13.923 6.192   0.68 15.00 ?  16  VAL   A CG1  1 
ATOM   373  C CG1  B VAL   A 1 16  ? 15.061 -14.093 6.111   0.32 14.51 ?  16  VAL   A CG1  1 
ATOM   374  C CG2  A VAL   A 1 16  ? 16.910 -15.777 6.074   0.68 15.21 ?  16  VAL   A CG2  1 
ATOM   375  C CG2  B VAL   A 1 16  ? 16.793 -15.897 5.964   0.32 14.49 ?  16  VAL   A CG2  1 
ATOM   376  H H    A VAL   A 1 16  ? 15.604 -17.147 8.704   0.68 17.06 ?  16  VAL   A H    1 
ATOM   377  H H    B VAL   A 1 16  ? 15.651 -17.193 8.645   0.32 16.99 ?  16  VAL   A H    1 
ATOM   378  H HA   A VAL   A 1 16  ? 16.493 -14.589 8.456   0.68 16.79 ?  16  VAL   A HA   1 
ATOM   379  H HA   B VAL   A 1 16  ? 16.511 -14.638 8.319   0.32 16.61 ?  16  VAL   A HA   1 
ATOM   380  H HB   A VAL   A 1 16  ? 14.923 -15.922 6.522   0.68 17.19 ?  16  VAL   A HB   1 
ATOM   381  H HB   B VAL   A 1 16  ? 14.844 -16.078 6.543   0.32 17.01 ?  16  VAL   A HB   1 
ATOM   382  H HG11 A VAL   A 1 16  ? 15.324 -13.934 5.228   0.68 17.98 ?  16  VAL   A HG11 1 
ATOM   383  H HG11 B VAL   A 1 16  ? 15.108 -14.137 5.144   0.32 17.39 ?  16  VAL   A HG11 1 
ATOM   384  H HG12 A VAL   A 1 16  ? 14.304 -13.748 6.430   0.68 17.98 ?  16  VAL   A HG12 1 
ATOM   385  H HG12 B VAL   A 1 16  ? 14.146 -13.939 6.391   0.32 17.39 ?  16  VAL   A HG12 1 
ATOM   386  H HG13 A VAL   A 1 16  ? 15.806 -13.251 6.578   0.68 17.98 ?  16  VAL   A HG13 1 
ATOM   387  H HG13 B VAL   A 1 16  ? 15.635 -13.384 6.439   0.32 17.39 ?  16  VAL   A HG13 1 
ATOM   388  H HG21 A VAL   A 1 16  ? 16.810 -15.715 5.113   0.68 18.23 ?  16  VAL   A HG21 1 
ATOM   389  H HG21 B VAL   A 1 16  ? 16.627 -15.895 5.009   0.32 17.36 ?  16  VAL   A HG21 1 
ATOM   390  H HG22 A VAL   A 1 16  ? 17.647 -15.221 6.369   0.68 18.23 ?  16  VAL   A HG22 1 
ATOM   391  H HG22 B VAL   A 1 16  ? 17.526 -15.296 6.173   0.32 17.36 ?  16  VAL   A HG22 1 
ATOM   392  H HG23 A VAL   A 1 16  ? 17.069 -16.699 6.334   0.68 18.23 ?  16  VAL   A HG23 1 
ATOM   393  H HG23 B VAL   A 1 16  ? 17.008 -16.795 6.262   0.32 17.36 ?  16  VAL   A HG23 1 
ATOM   394  N N    A TYR   A 1 17  ? 14.545 -13.479 9.351   0.68 13.52 ?  17  TYR   A N    1 
ATOM   395  N N    B TYR   A 1 17  ? 14.654 -13.537 9.413   0.32 13.23 ?  17  TYR   A N    1 
ATOM   396  C CA   A TYR   A 1 17  ? 13.469 -12.796 10.054  0.68 13.54 ?  17  TYR   A CA   1 
ATOM   397  C CA   B TYR   A 1 17  ? 13.577 -12.842 10.098  0.32 13.25 ?  17  TYR   A CA   1 
ATOM   398  C C    A TYR   A 1 17  ? 13.208 -11.464 9.363   0.68 13.72 ?  17  TYR   A C    1 
ATOM   399  C C    B TYR   A 1 17  ? 13.284 -11.533 9.368   0.32 13.02 ?  17  TYR   A C    1 
ATOM   400  O O    A TYR   A 1 17  ? 14.136 -10.854 8.830   0.68 13.18 ?  17  TYR   A O    1 
ATOM   401  O O    B TYR   A 1 17  ? 14.085 -11.066 8.554   0.32 12.60 ?  17  TYR   A O    1 
ATOM   402  C CB   A TYR   A 1 17  ? 13.889 -12.538 11.504  0.68 14.35 ?  17  TYR   A CB   1 
ATOM   403  C CB   B TYR   A 1 17  ? 13.967 -12.549 11.557  0.32 14.30 ?  17  TYR   A CB   1 
ATOM   404  C CG   A TYR   A 1 17  ? 14.073 -13.799 12.314  0.68 14.86 ?  17  TYR   A CG   1 
ATOM   405  C CG   B TYR   A 1 17  ? 14.323 -13.780 12.377  0.32 15.43 ?  17  TYR   A CG   1 
ATOM   406  C CD1  A TYR   A 1 17  ? 15.237 -14.552 12.221  0.68 15.58 ?  17  TYR   A CD1  1 
ATOM   407  C CD1  B TYR   A 1 17  ? 15.560 -14.401 12.239  0.32 16.34 ?  17  TYR   A CD1  1 
ATOM   408  C CD2  A TYR   A 1 17  ? 13.073 -14.247 13.165  0.68 14.87 ?  17  TYR   A CD2  1 
ATOM   409  C CD2  B TYR   A 1 17  ? 13.427 -14.313 13.299  0.32 16.07 ?  17  TYR   A CD2  1 
ATOM   410  C CE1  A TYR   A 1 17  ? 15.403 -15.715 12.957  0.68 15.41 ?  17  TYR   A CE1  1 
ATOM   411  C CE1  B TYR   A 1 17  ? 15.891 -15.521 12.984  0.32 17.04 ?  17  TYR   A CE1  1 
ATOM   412  C CE2  A TYR   A 1 17  ? 13.227 -15.415 13.905  0.68 15.01 ?  17  TYR   A CE2  1 
ATOM   413  C CE2  B TYR   A 1 17  ? 13.751 -15.435 14.051  0.32 16.85 ?  17  TYR   A CE2  1 
ATOM   414  C CZ   A TYR   A 1 17  ? 14.397 -16.142 13.797  0.68 15.03 ?  17  TYR   A CZ   1 
ATOM   415  C CZ   B TYR   A 1 17  ? 14.984 -16.031 13.888  0.32 17.41 ?  17  TYR   A CZ   1 
ATOM   416  O OH   A TYR   A 1 17  ? 14.572 -17.291 14.531  0.68 15.15 ?  17  TYR   A OH   1 
ATOM   417  O OH   B TYR   A 1 17  ? 15.308 -17.143 14.633  0.32 18.15 ?  17  TYR   A OH   1 
ATOM   418  H H    A TYR   A 1 17  ? 15.223 -12.954 9.221   0.68 16.20 ?  17  TYR   A H    1 
ATOM   419  H H    B TYR   A 1 17  ? 15.371 -13.068 9.353   0.32 15.86 ?  17  TYR   A H    1 
ATOM   420  H HA   A TYR   A 1 17  ? 12.660 -13.329 10.038  0.68 16.22 ?  17  TYR   A HA   1 
ATOM   421  H HA   B TYR   A 1 17  ? 12.778 -13.394 10.091  0.32 15.87 ?  17  TYR   A HA   1 
ATOM   422  H HB2  A TYR   A 1 17  ? 14.731 -12.061 11.506  0.68 17.20 ?  17  TYR   A HB2  1 
ATOM   423  H HB2  B TYR   A 1 17  ? 14.738 -11.962 11.556  0.32 17.13 ?  17  TYR   A HB2  1 
ATOM   424  H HB3  A TYR   A 1 17  ? 13.209 -12.007 11.939  0.68 17.20 ?  17  TYR   A HB3  1 
ATOM   425  H HB3  B TYR   A 1 17  ? 13.221 -12.110 11.992  0.32 17.13 ?  17  TYR   A HB3  1 
ATOM   426  H HD1  A TYR   A 1 17  ? 15.920 -14.270 11.653  0.68 18.68 ?  17  TYR   A HD1  1 
ATOM   427  H HD1  B TYR   A 1 17  ? 16.175 -14.066 11.632  0.32 19.59 ?  17  TYR   A HD1  1 
ATOM   428  H HD2  A TYR   A 1 17  ? 12.281 -13.765 13.241  0.68 17.82 ?  17  TYR   A HD2  1 
ATOM   429  H HD2  B TYR   A 1 17  ? 12.595 -13.916 13.414  0.32 19.26 ?  17  TYR   A HD2  1 
ATOM   430  H HE1  A TYR   A 1 17  ? 16.195 -16.205 12.884  0.68 18.47 ?  17  TYR   A HE1  1 
ATOM   431  H HE1  B TYR   A 1 17  ? 16.722 -15.929 12.879  0.32 20.43 ?  17  TYR   A HE1  1 
ATOM   432  H HE2  A TYR   A 1 17  ? 12.551 -15.701 14.475  0.68 17.99 ?  17  TYR   A HE2  1 
ATOM   433  H HE2  B TYR   A 1 17  ? 13.142 -15.784 14.665  0.32 20.19 ?  17  TYR   A HE2  1 
ATOM   434  H HH   A TYR   A 1 17  ? 13.840 -17.518 14.883  0.68 18.16 ?  17  TYR   A HH   1 
ATOM   435  H HH   B TYR   A 1 17  ? 16.084 -17.409 14.436  0.32 21.75 ?  17  TYR   A HH   1 
ATOM   436  N N    A ILE   A 1 18  ? 11.951 -10.996 9.376   0.68 13.06 ?  18  ILE   A N    1 
ATOM   437  N N    B ILE   A 1 18  ? 12.131 -10.928 9.668   0.32 12.72 ?  18  ILE   A N    1 
ATOM   438  C CA   A ILE   A 1 18  ? 11.574 -9.805  8.615   0.68 12.96 ?  18  ILE   A CA   1 
ATOM   439  C CA   B ILE   A 1 18  ? 11.714 -9.694  9.003   0.32 12.58 ?  18  ILE   A CA   1 
ATOM   440  C C    A ILE   A 1 18  ? 10.597 -8.940  9.408   0.68 13.03 ?  18  ILE   A C    1 
ATOM   441  C C    B ILE   A 1 18  ? 10.810 -8.885  9.924   0.32 12.52 ?  18  ILE   A C    1 
ATOM   442  O O    A ILE   A 1 18  ? 9.761  -9.444  10.166  0.68 13.18 ?  18  ILE   A O    1 
ATOM   443  O O    B ILE   A 1 18  ? 10.015 -9.437  10.691  0.32 13.15 ?  18  ILE   A O    1 
ATOM   444  C CB   A ILE   A 1 18  ? 11.035 -10.216 7.222   0.68 12.91 ?  18  ILE   A CB   1 
ATOM   445  C CB   B ILE   A 1 18  ? 11.012 -9.975  7.655   0.32 11.87 ?  18  ILE   A CB   1 
ATOM   446  C CG1  A ILE   A 1 18  ? 10.984 -9.020  6.273   0.68 13.30 ?  18  ILE   A CG1  1 
ATOM   447  C CG1  B ILE   A 1 18  ? 10.971 -8.713  6.793   0.32 11.92 ?  18  ILE   A CG1  1 
ATOM   448  C CG2  A ILE   A 1 18  ? 9.709  -10.965 7.342   0.68 12.88 ?  18  ILE   A CG2  1 
ATOM   449  C CG2  B ILE   A 1 18  ? 9.604  -10.519 7.878   0.32 12.39 ?  18  ILE   A CG2  1 
ATOM   450  C CD1  A ILE   A 1 18  ? 10.796 -9.419  4.835   0.68 14.39 ?  18  ILE   A CD1  1 
ATOM   451  C CD1  B ILE   A 1 18  ? 10.511 -8.980  5.378   0.32 12.47 ?  18  ILE   A CD1  1 
ATOM   452  H H    A ILE   A 1 18  ? 11.300 -11.368 9.804   0.68 15.65 ?  18  ILE   A H    1 
ATOM   453  H H    B ILE   A 1 18  ? 11.586 -11.215 10.256  0.32 15.24 ?  18  ILE   A H    1 
ATOM   454  H HA   A ILE   A 1 18  ? 12.375 -9.281  8.465   0.68 15.53 ?  18  ILE   A HA   1 
ATOM   455  H HA   B ILE   A 1 18  ? 12.508 -9.163  8.818   0.32 15.07 ?  18  ILE   A HA   1 
ATOM   456  H HB   A ILE   A 1 18  ? 11.674 -10.845 6.846   0.68 15.47 ?  18  ILE   A HB   1 
ATOM   457  H HB   B ILE   A 1 18  ? 11.523 -10.641 7.183   0.32 14.23 ?  18  ILE   A HB   1 
ATOM   458  H HG12 A ILE   A 1 18  ? 10.249 -8.450  6.523   0.68 15.93 ?  18  ILE   A HG12 1 
ATOM   459  H HG12 B ILE   A 1 18  ? 10.360 -8.072  7.191   0.32 14.28 ?  18  ILE   A HG12 1 
ATOM   460  H HG13 A ILE   A 1 18  ? 11.824 -8.537  6.334   0.68 15.93 ?  18  ILE   A HG13 1 
ATOM   461  H HG13 B ILE   A 1 18  ? 11.864 -8.329  6.750   0.32 14.28 ?  18  ILE   A HG13 1 
ATOM   462  H HG21 A ILE   A 1 18  ? 9.463  -11.318 6.470   0.68 15.44 ?  18  ILE   A HG21 1 
ATOM   463  H HG21 B ILE   A 1 18  ? 9.285  -10.912 7.049   0.32 14.85 ?  18  ILE   A HG21 1 
ATOM   464  H HG22 A ILE   A 1 18  ? 9.816  -11.701 7.970   0.68 15.44 ?  18  ILE   A HG22 1 
ATOM   465  H HG22 B ILE   A 1 18  ? 9.634  -11.193 8.573   0.32 14.85 ?  18  ILE   A HG22 1 
ATOM   466  H HG23 A ILE   A 1 18  ? 9.026  -10.358 7.658   0.68 15.44 ?  18  ILE   A HG23 1 
ATOM   467  H HG23 B ILE   A 1 18  ? 9.017  -9.793  8.145   0.32 14.85 ?  18  ILE   A HG23 1 
ATOM   468  H HD11 A ILE   A 1 18  ? 10.824 -8.621  4.283   0.68 17.24 ?  18  ILE   A HD11 1 
ATOM   469  H HD11 B ILE   A 1 18  ? 10.581 -8.163  4.862   0.32 14.94 ?  18  ILE   A HD11 1 
ATOM   470  H HD12 A ILE   A 1 18  ? 11.505 -10.026 4.576   0.68 17.24 ?  18  ILE   A HD12 1 
ATOM   471  H HD12 B ILE   A 1 18  ? 11.077 -9.666  4.988   0.32 14.94 ?  18  ILE   A HD12 1 
ATOM   472  H HD13 A ILE   A 1 18  ? 9.934  -9.855  4.740   0.68 17.24 ?  18  ILE   A HD13 1 
ATOM   473  H HD13 B ILE   A 1 18  ? 9.591  -9.283  5.397   0.32 14.94 ?  18  ILE   A HD13 1 
ATOM   474  N N    A LYS   A 1 19  ? 10.700 -7.619  9.215   0.68 12.61 ?  19  LYS   A N    1 
ATOM   475  N N    B LYS   A 1 19  ? 10.919 -7.560  9.816   0.32 12.99 ?  19  LYS   A N    1 
ATOM   476  C CA   A LYS   A 1 19  ? 9.890  -6.651  9.952   0.68 13.59 ?  19  LYS   A CA   1 
ATOM   477  C CA   B LYS   A 1 19  ? 10.127 -6.634  10.614  0.32 14.04 ?  19  LYS   A CA   1 
ATOM   478  C C    A LYS   A 1 19  ? 9.706  -5.396  9.107   0.68 13.39 ?  19  LYS   A C    1 
ATOM   479  C C    B LYS   A 1 19  ? 9.878  -5.385  9.784   0.32 14.29 ?  19  LYS   A C    1 
ATOM   480  O O    A LYS   A 1 19  ? 10.602 -5.012  8.356   0.68 13.15 ?  19  LYS   A O    1 
ATOM   481  O O    B LYS   A 1 19  ? 10.748 -4.960  9.021   0.32 13.79 ?  19  LYS   A O    1 
ATOM   482  C CB   A LYS   A 1 19  ? 10.592 -6.281  11.269  0.68 14.58 ?  19  LYS   A CB   1 
ATOM   483  C CB   B LYS   A 1 19  ? 10.862 -6.263  11.912  0.32 14.82 ?  19  LYS   A CB   1 
ATOM   484  C CG   A LYS   A 1 19  ? 9.819  -5.369  12.212  0.68 16.32 ?  19  LYS   A CG   1 
ATOM   485  C CG   B LYS   A 1 19  ? 10.119 -5.322  12.853  0.32 15.78 ?  19  LYS   A CG   1 
ATOM   486  C CD   A LYS   A 1 19  ? 10.666 -5.087  13.450  0.68 18.02 ?  19  LYS   A CD   1 
ATOM   487  C CD   B LYS   A 1 19  ? 11.061 -4.840  13.951  0.32 16.68 ?  19  LYS   A CD   1 
ATOM   488  C CE   A LYS   A 1 19  ? 9.998  -4.121  14.410  0.68 19.33 ?  19  LYS   A CE   1 
ATOM   489  C CE   B LYS   A 1 19  ? 10.337 -4.138  15.084  0.32 17.31 ?  19  LYS   A CE   1 
ATOM   490  N NZ   A LYS   A 1 19  ? 10.871 -3.836  15.585  0.68 19.72 ?  19  LYS   A NZ   1 
ATOM   491  N NZ   B LYS   A 1 19  ? 11.255 -3.918  16.240  0.32 17.56 ?  19  LYS   A NZ   1 
ATOM   492  H H    A LYS   A 1 19  ? 11.251 -7.259  8.656   0.68 15.11 ?  19  LYS   A H    1 
ATOM   493  H H    B LYS   A 1 19  ? 11.460 -7.159  9.271   0.32 15.56 ?  19  LYS   A H    1 
ATOM   494  H HA   A LYS   A 1 19  ? 9.025  -7.039  10.145  0.68 16.29 ?  19  LYS   A HA   1 
ATOM   495  H HA   B LYS   A 1 19  ? 9.278  -7.029  10.838  0.32 16.83 ?  19  LYS   A HA   1 
ATOM   496  H HB2  A LYS   A 1 19  ? 10.774 -7.100  11.753  0.68 17.48 ?  19  LYS   A HB2  1 
ATOM   497  H HB2  B LYS   A 1 19  ? 11.029 -7.078  12.409  0.32 17.76 ?  19  LYS   A HB2  1 
ATOM   498  H HB3  A LYS   A 1 19  ? 11.425 -5.838  11.055  0.68 17.48 ?  19  LYS   A HB3  1 
ATOM   499  H HB3  B LYS   A 1 19  ? 11.706 -5.840  11.689  0.32 17.76 ?  19  LYS   A HB3  1 
ATOM   500  H HG2  A LYS   A 1 19  ? 9.627  -4.527  11.770  0.68 19.56 ?  19  LYS   A HG2  1 
ATOM   501  H HG2  B LYS   A 1 19  ? 9.800  -4.549  12.364  0.32 18.91 ?  19  LYS   A HG2  1 
ATOM   502  H HG3  A LYS   A 1 19  ? 8.998  -5.805  12.491  0.68 19.56 ?  19  LYS   A HG3  1 
ATOM   503  H HG3  B LYS   A 1 19  ? 9.380  -5.793  13.269  0.32 18.91 ?  19  LYS   A HG3  1 
ATOM   504  H HD2  A LYS   A 1 19  ? 10.824 -5.920  13.924  0.68 21.60 ?  19  LYS   A HD2  1 
ATOM   505  H HD2  B LYS   A 1 19  ? 11.518 -5.605  14.326  0.32 19.99 ?  19  LYS   A HD2  1 
ATOM   506  H HD3  A LYS   A 1 19  ? 11.513 -4.699  13.174  0.68 21.60 ?  19  LYS   A HD3  1 
ATOM   507  H HD3  B LYS   A 1 19  ? 11.705 -4.220  13.570  0.32 19.99 ?  19  LYS   A HD3  1 
ATOM   508  H HE2  A LYS   A 1 19  ? 9.823  -3.283  13.953  0.68 23.17 ?  19  LYS   A HE2  1 
ATOM   509  H HE2  B LYS   A 1 19  ? 10.016 -3.276  14.778  0.32 20.75 ?  19  LYS   A HE2  1 
ATOM   510  H HE3  A LYS   A 1 19  ? 9.172  -4.509  14.734  0.68 23.17 ?  19  LYS   A HE3  1 
ATOM   511  H HE3  B LYS   A 1 19  ? 9.596  -4.689  15.382  0.32 20.75 ?  19  LYS   A HE3  1 
ATOM   512  H HZ1  A LYS   A 1 19  ? 10.462 -3.275  16.141  0.68 23.64 ?  19  LYS   A HZ1  1 
ATOM   513  H HZ1  B LYS   A 1 19  ? 10.816 -3.523  16.906  0.32 21.05 ?  19  LYS   A HZ1  1 
ATOM   514  H HZ2  A LYS   A 1 19  ? 11.054 -4.592  16.019  0.68 23.64 ?  19  LYS   A HZ2  1 
ATOM   515  H HZ2  B LYS   A 1 19  ? 11.575 -4.697  16.527  0.32 21.05 ?  19  LYS   A HZ2  1 
ATOM   516  H HZ3  A LYS   A 1 19  ? 11.636 -3.468  15.314  0.68 23.64 ?  19  LYS   A HZ3  1 
ATOM   517  H HZ3  B LYS   A 1 19  ? 11.935 -3.399  15.994  0.32 21.05 ?  19  LYS   A HZ3  1 
ATOM   518  N N    A ASN   A 1 20  ? 8.536  -4.762  9.224   0.68 14.56 ?  20  ASN   A N    1 
ATOM   519  N N    B ASN   A 1 20  ? 8.685  -4.812  9.921   0.32 15.66 ?  20  ASN   A N    1 
ATOM   520  C CA   A ASN   A 1 20  ? 8.313  -3.440  8.639   0.68 16.25 ?  20  ASN   A CA   1 
ATOM   521  C CA   B ASN   A 1 20  ? 8.381  -3.524  9.306   0.32 17.13 ?  20  ASN   A CA   1 
ATOM   522  C C    A ASN   A 1 20  ? 8.909  -2.417  9.595   0.68 17.13 ?  20  ASN   A C    1 
ATOM   523  C C    B ASN   A 1 20  ? 8.956  -2.448  10.217  0.32 17.41 ?  20  ASN   A C    1 
ATOM   524  O O    A ASN   A 1 20  ? 8.348  -2.158  10.663  0.68 18.87 ?  20  ASN   A O    1 
ATOM   525  O O    B ASN   A 1 20  ? 8.396  -2.144  11.273  0.32 17.82 ?  20  ASN   A O    1 
ATOM   526  C CB   A ASN   A 1 20  ? 6.815  -3.205  8.435   0.68 17.26 ?  20  ASN   A CB   1 
ATOM   527  C CB   B ASN   A 1 20  ? 6.876  -3.369  9.108   0.32 18.33 ?  20  ASN   A CB   1 
ATOM   528  C CG   A ASN   A 1 20  ? 6.484  -1.781  7.981   0.68 18.62 ?  20  ASN   A CG   1 
ATOM   529  C CG   B ASN   A 1 20  ? 6.462  -1.939  8.818   0.32 19.27 ?  20  ASN   A CG   1 
ATOM   530  O OD1  A ASN   A 1 20  ? 5.475  -1.206  8.395   0.68 20.23 ?  20  ASN   A OD1  1 
ATOM   531  O OD1  B ASN   A 1 20  ? 5.584  -1.392  9.487   0.32 19.98 ?  20  ASN   A OD1  1 
ATOM   532  N ND2  A ASN   A 1 20  ? 7.326  -1.215  7.123   0.68 18.90 ?  20  ASN   A ND2  1 
ATOM   533  N ND2  B ASN   A 1 20  ? 7.091  -1.325  7.822   0.32 19.59 ?  20  ASN   A ND2  1 
ATOM   534  H H    A ASN   A 1 20  ? 7.858  -5.087  9.640   0.68 17.45 ?  20  ASN   A H    1 
ATOM   535  H H    B ASN   A 1 20  ? 8.035  -5.151  10.361  0.32 18.77 ?  20  ASN   A H    1 
ATOM   536  H HA   A ASN   A 1 20  ? 8.767  -3.382  7.785   0.68 19.48 ?  20  ASN   A HA   1 
ATOM   537  H HA   B ASN   A 1 20  ? 8.813  -3.465  8.442   0.32 20.53 ?  20  ASN   A HA   1 
ATOM   538  H HB2  A ASN   A 1 20  ? 6.493  -3.812  7.759   0.68 20.69 ?  20  ASN   A HB2  1 
ATOM   539  H HB2  B ASN   A 1 20  ? 6.599  -3.922  8.359   0.32 21.98 ?  20  ASN   A HB2  1 
ATOM   540  H HB3  A ASN   A 1 20  ? 6.363  -3.377  9.276   0.68 20.69 ?  20  ASN   A HB3  1 
ATOM   541  H HB3  B ASN   A 1 20  ? 6.419  -3.644  9.914   0.32 21.98 ?  20  ASN   A HB3  1 
ATOM   542  H HD21 A ASN   A 1 20  ? 7.177  -0.416  6.853   0.68 22.66 ?  20  ASN   A HD21 1 
ATOM   543  H HD21 B ASN   A 1 20  ? 6.887  -0.514  7.619   0.32 23.48 ?  20  ASN   A HD21 1 
ATOM   544  H HD22 A ASN   A 1 20  ? 8.016  -1.646  6.845   0.68 22.66 ?  20  ASN   A HD22 1 
ATOM   545  H HD22 B ASN   A 1 20  ? 7.701  -1.738  7.379   0.32 23.48 ?  20  ASN   A HD22 1 
ATOM   546  N N    A ALA   A 1 21  ? 10.064 -1.859  9.239   0.68 16.60 ?  21  ALA   A N    1 
ATOM   547  N N    B ALA   A 1 21  ? 10.103 -1.895  9.830   0.32 17.59 ?  21  ALA   A N    1 
ATOM   548  C CA   A ALA   A 1 21  ? 10.750 -0.962  10.159  0.68 16.45 ?  21  ALA   A CA   1 
ATOM   549  C CA   B ALA   A 1 21  ? 10.756 -0.867  10.627  0.32 17.75 ?  21  ALA   A CA   1 
ATOM   550  C C    A ALA   A 1 21  ? 11.715 -0.075  9.394   0.68 16.29 ?  21  ALA   A C    1 
ATOM   551  C C    B ALA   A 1 21  ? 11.847 -0.210  9.796   0.32 17.19 ?  21  ALA   A C    1 
ATOM   552  O O    A ALA   A 1 21  ? 12.177 -0.423  8.305   0.68 16.36 ?  21  ALA   A O    1 
ATOM   553  O O    B ALA   A 1 21  ? 12.390 -0.819  8.870   0.32 16.53 ?  21  ALA   A O    1 
ATOM   554  C CB   A ALA   A 1 21  ? 11.508 -1.738  11.239  0.68 17.36 ?  21  ALA   A CB   1 
ATOM   555  C CB   B ALA   A 1 21  ? 11.356 -1.456  11.911  0.32 18.50 ?  21  ALA   A CB   1 
ATOM   556  H H    A ALA   A 1 21  ? 10.464 -1.985  8.486   0.68 19.90 ?  21  ALA   A H    1 
ATOM   557  H H    B ALA   A 1 21  ? 10.529 -2.105  9.111   0.32 21.09 ?  21  ALA   A H    1 
ATOM   558  H HA   A ALA   A 1 21  ? 10.089 -0.396  10.595  0.68 19.71 ?  21  ALA   A HA   1 
ATOM   559  H HA   B ALA   A 1 21  ? 10.110 -0.187  10.874  0.32 21.27 ?  21  ALA   A HA   1 
ATOM   560  H HB1  A ALA   A 1 21  ? 11.935 -1.103  11.835  0.68 20.81 ?  21  ALA   A HB1  1 
ATOM   561  H HB1  B ALA   A 1 21  ? 11.785 -0.747  12.415  0.32 22.18 ?  21  ALA   A HB1  1 
ATOM   562  H HB2  A ALA   A 1 21  ? 10.875 -2.282  11.737  0.68 20.81 ?  21  ALA   A HB2  1 
ATOM   563  H HB2  B ALA   A 1 21  ? 10.646 -1.855  12.438  0.32 22.18 ?  21  ALA   A HB2  1 
ATOM   564  H HB3  A ALA   A 1 21  ? 12.170 -2.300  10.816  0.68 20.81 ?  21  ALA   A HB3  1 
ATOM   565  H HB3  B ALA   A 1 21  ? 12.010 -2.133  11.672  0.32 22.18 ?  21  ALA   A HB3  1 
ATOM   566  N N    A ASP   A 1 22  ? 11.997 1.080   9.998   0.68 17.05 ?  22  ASP   A N    1 
ATOM   567  N N    B ASP   A 1 22  ? 12.137 1.047   10.125  0.32 17.24 ?  22  ASP   A N    1 
ATOM   568  C CA   A ASP   A 1 22  ? 13.040 1.989   9.548   0.68 16.85 ?  22  ASP   A CA   1 
ATOM   569  C CA   B ASP   A 1 22  ? 13.300 1.730   9.574   0.32 17.05 ?  22  ASP   A CA   1 
ATOM   570  C C    A ASP   A 1 22  ? 14.366 1.506   10.124  0.68 15.87 ?  22  ASP   A C    1 
ATOM   571  C C    B ASP   A 1 22  ? 14.560 1.090   10.142  0.32 15.54 ?  22  ASP   A C    1 
ATOM   572  O O    A ASP   A 1 22  ? 14.550 1.497   11.345  0.68 16.38 ?  22  ASP   A O    1 
ATOM   573  O O    B ASP   A 1 22  ? 14.707 0.965   11.362  0.32 15.19 ?  22  ASP   A O    1 
ATOM   574  C CB   A ASP   A 1 22  ? 12.705 3.392   10.050  0.68 18.63 ?  22  ASP   A CB   1 
ATOM   575  C CB   B ASP   A 1 22  ? 13.251 3.207   9.970   0.32 18.34 ?  22  ASP   A CB   1 
ATOM   576  C CG   A ASP   A 1 22  ? 13.754 4.425   9.671   0.68 20.10 ?  22  ASP   A CG   1 
ATOM   577  C CG   B ASP   A 1 22  ? 14.232 4.069   9.189   0.32 19.37 ?  22  ASP   A CG   1 
ATOM   578  O OD1  A ASP   A 1 22  ? 14.842 4.058   9.189   0.68 20.41 ?  22  ASP   A OD1  1 
ATOM   579  O OD1  B ASP   A 1 22  ? 15.268 3.540   8.736   0.32 19.18 ?  22  ASP   A OD1  1 
ATOM   580  O OD2  A ASP   A 1 22  ? 13.484 5.628   9.858   0.68 21.72 -1 22  ASP   A OD2  1 
ATOM   581  O OD2  B ASP   A 1 22  ? 13.972 5.283   9.037   0.32 20.39 -1 22  ASP   A OD2  1 
ATOM   582  H H    A ASP   A 1 22  ? 11.569 1.367   10.693  0.68 20.44 ?  22  ASP   A H    1 
ATOM   583  H H    B ASP   A 1 22  ? 11.661 1.528   10.657  0.32 20.66 ?  22  ASP   A H    1 
ATOM   584  H HA   A ASP   A 1 22  ? 13.086 1.996   8.579   0.68 20.19 ?  22  ASP   A HA   1 
ATOM   585  H HA   B ASP   A 1 22  ? 13.301 1.649   8.605   0.32 20.44 ?  22  ASP   A HA   1 
ATOM   586  H HB2  A ASP   A 1 22  ? 11.850 3.670   9.673   0.68 22.33 ?  22  ASP   A HB2  1 
ATOM   587  H HB2  B ASP   A 1 22  ? 12.359 3.544   9.812   0.32 21.98 ?  22  ASP   A HB2  1 
ATOM   588  H HB3  A ASP   A 1 22  ? 12.637 3.373   11.020  0.68 22.33 ?  22  ASP   A HB3  1 
ATOM   589  H HB3  B ASP   A 1 22  ? 13.479 3.281   10.908  0.32 21.98 ?  22  ASP   A HB3  1 
ATOM   590  N N    A ILE   A 1 23  ? 15.283 1.095   9.245   0.68 15.20 ?  23  ILE   A N    1 
ATOM   591  N N    B ILE   A 1 23  ? 15.470 0.674   9.257   0.32 14.70 ?  23  ILE   A N    1 
ATOM   592  C CA   A ILE   A 1 23  ? 16.538 0.496   9.694   0.68 14.42 ?  23  ILE   A CA   1 
ATOM   593  C CA   B ILE   A 1 23  ? 16.698 0.029   9.712   0.32 13.98 ?  23  ILE   A CA   1 
ATOM   594  C C    A ILE   A 1 23  ? 17.325 1.450   10.580  0.68 14.48 ?  23  ILE   A C    1 
ATOM   595  C C    B ILE   A 1 23  ? 17.483 0.961   10.624  0.32 14.13 ?  23  ILE   A C    1 
ATOM   596  O O    A ILE   A 1 23  ? 18.048 1.012   11.483  0.68 14.84 ?  23  ILE   A O    1 
ATOM   597  O O    B ILE   A 1 23  ? 18.158 0.511   11.558  0.32 13.75 ?  23  ILE   A O    1 
ATOM   598  C CB   A ILE   A 1 23  ? 17.356 -0.006  8.484   0.68 13.62 ?  23  ILE   A CB   1 
ATOM   599  C CB   B ILE   A 1 23  ? 17.538 -0.483  8.521   0.32 13.26 ?  23  ILE   A CB   1 
ATOM   600  C CG1  A ILE   A 1 23  ? 18.495 -0.916  8.942   0.68 13.71 ?  23  ILE   A CG1  1 
ATOM   601  C CG1  B ILE   A 1 23  ? 18.635 -1.418  9.035   0.32 12.70 ?  23  ILE   A CG1  1 
ATOM   602  C CG2  A ILE   A 1 23  ? 17.867 1.168   7.650   0.68 13.40 ?  23  ILE   A CG2  1 
ATOM   603  C CG2  B ILE   A 1 23  ? 18.131 0.674   7.718   0.32 13.60 ?  23  ILE   A CG2  1 
ATOM   604  C CD1  A ILE   A 1 23  ? 19.199 -1.625  7.796   0.68 14.00 ?  23  ILE   A CD1  1 
ATOM   605  C CD1  B ILE   A 1 23  ? 19.531 -1.982  7.963   0.32 12.43 ?  23  ILE   A CD1  1 
ATOM   606  H H    A ILE   A 1 23  ? 15.196 1.153   8.398   0.68 18.22 ?  23  ILE   A H    1 
ATOM   607  H H    B ILE   A 1 23  ? 15.402 0.753   8.413   0.32 17.61 ?  23  ILE   A H    1 
ATOM   608  H HA   A ILE   A 1 23  ? 16.325 -0.275  10.236  0.68 17.28 ?  23  ILE   A HA   1 
ATOM   609  H HA   B ILE   A 1 23  ? 16.451 -0.747  10.233  0.32 16.75 ?  23  ILE   A HA   1 
ATOM   610  H HB   A ILE   A 1 23  ? 16.764 -0.527  7.927   0.68 16.32 ?  23  ILE   A HB   1 
ATOM   611  H HB   B ILE   A 1 23  ? 16.959 -0.995  7.932   0.32 15.89 ?  23  ILE   A HB   1 
ATOM   612  H HG12 A ILE   A 1 23  ? 19.158 -0.382  9.410   0.68 16.42 ?  23  ILE   A HG12 1 
ATOM   613  H HG12 B ILE   A 1 23  ? 19.197 -0.932  9.657   0.32 15.22 ?  23  ILE   A HG12 1 
ATOM   614  H HG13 A ILE   A 1 23  ? 18.138 -1.593  9.535   0.68 16.42 ?  23  ILE   A HG13 1 
ATOM   615  H HG13 B ILE   A 1 23  ? 18.216 -2.166  9.487   0.32 15.22 ?  23  ILE   A HG13 1 
ATOM   616  H HG21 A ILE   A 1 23  ? 18.227 0.830   6.815   0.68 16.06 ?  23  ILE   A HG21 1 
ATOM   617  H HG21 B ILE   A 1 23  ? 18.472 0.332   6.872   0.32 16.29 ?  23  ILE   A HG21 1 
ATOM   618  H HG22 A ILE   A 1 23  ? 17.129 1.773   7.466   0.68 16.06 ?  23  ILE   A HG22 1 
ATOM   619  H HG22 B ILE   A 1 23  ? 17.439 1.329   7.551   0.32 16.29 ?  23  ILE   A HG22 1 
ATOM   620  H HG23 A ILE   A 1 23  ? 18.559 1.637   8.142   0.68 16.06 ?  23  ILE   A HG23 1 
ATOM   621  H HG23 B ILE   A 1 23  ? 18.854 1.074   8.224   0.32 16.29 ?  23  ILE   A HG23 1 
ATOM   622  H HD11 A ILE   A 1 23  ? 19.859 -2.233  8.160   0.68 16.78 ?  23  ILE   A HD11 1 
ATOM   623  H HD11 B ILE   A 1 23  ? 20.117 -2.647  8.360   0.32 14.90 ?  23  ILE   A HD11 1 
ATOM   624  H HD12 A ILE   A 1 23  ? 18.541 -2.118  7.282   0.68 16.78 ?  23  ILE   A HD12 1 
ATOM   625  H HD12 B ILE   A 1 23  ? 18.981 -2.392  7.279   0.32 14.90 ?  23  ILE   A HD12 1 
ATOM   626  H HD13 A ILE   A 1 23  ? 19.631 -0.964  7.233   0.68 16.78 ?  23  ILE   A HD13 1 
ATOM   627  H HD13 B ILE   A 1 23  ? 20.058 -1.264  7.580   0.32 14.90 ?  23  ILE   A HD13 1 
ATOM   628  N N    A VAL   A 1 24  ? 17.190 2.760   10.359  0.68 15.16 ?  24  VAL   A N    1 
ATOM   629  N N    B VAL   A 1 24  ? 17.391 2.269   10.385  0.32 15.11 ?  24  VAL   A N    1 
ATOM   630  C CA   A VAL   A 1 24  ? 17.877 3.730   11.210  0.68 16.49 ?  24  VAL   A CA   1 
ATOM   631  C CA   B VAL   A 1 24  ? 18.042 3.239   11.262  0.32 16.27 ?  24  VAL   A CA   1 
ATOM   632  C C    A VAL   A 1 24  ? 17.362 3.640   12.639  0.68 17.24 ?  24  VAL   A C    1 
ATOM   633  C C    B VAL   A 1 24  ? 17.448 3.165   12.663  0.32 16.81 ?  24  VAL   A C    1 
ATOM   634  O O    A VAL   A 1 24  ? 18.141 3.571   13.599  0.68 17.75 ?  24  VAL   A O    1 
ATOM   635  O O    B VAL   A 1 24  ? 18.171 3.145   13.666  0.32 17.00 ?  24  VAL   A O    1 
ATOM   636  C CB   A VAL   A 1 24  ? 17.722 5.151   10.639  0.68 17.35 ?  24  VAL   A CB   1 
ATOM   637  C CB   B VAL   A 1 24  ? 17.929 4.651   10.661  0.32 17.00 ?  24  VAL   A CB   1 
ATOM   638  C CG1  A VAL   A 1 24  ? 18.210 6.190   11.646  0.68 17.78 ?  24  VAL   A CG1  1 
ATOM   639  C CG1  B VAL   A 1 24  ? 18.612 5.666   11.556  0.32 17.75 ?  24  VAL   A CG1  1 
ATOM   640  C CG2  A VAL   A 1 24  ? 18.475 5.277   9.326   0.68 18.12 ?  24  VAL   A CG2  1 
ATOM   641  C CG2  B VAL   A 1 24  ? 18.519 4.674   9.254   0.32 17.02 ?  24  VAL   A CG2  1 
ATOM   642  H H    A VAL   A 1 24  ? 16.715 3.109   9.732   0.68 18.17 ?  24  VAL   A H    1 
ATOM   643  H H    B VAL   A 1 24  ? 16.961 2.615   9.728   0.32 18.11 ?  24  VAL   A H    1 
ATOM   644  H HA   A VAL   A 1 24  ? 18.822 3.525   11.223  0.68 19.76 ?  24  VAL   A HA   1 
ATOM   645  H HA   B VAL   A 1 24  ? 18.984 3.016   11.326  0.32 19.50 ?  24  VAL   A HA   1 
ATOM   646  H HB   A VAL   A 1 24  ? 16.784 5.327   10.461  0.68 20.80 ?  24  VAL   A HB   1 
ATOM   647  H HB   B VAL   A 1 24  ? 16.991 4.889   10.592  0.32 20.37 ?  24  VAL   A HB   1 
ATOM   648  H HG11 A VAL   A 1 24  ? 18.377 7.025   11.181  0.68 21.32 ?  24  VAL   A HG11 1 
ATOM   649  H HG11 B VAL   A 1 24  ? 18.679 6.506   11.078  0.32 21.27 ?  24  VAL   A HG11 1 
ATOM   650  H HG12 A VAL   A 1 24  ? 17.528 6.321   12.323  0.68 21.32 ?  24  VAL   A HG12 1 
ATOM   651  H HG12 B VAL   A 1 24  ? 18.083 5.782   12.359  0.32 21.27 ?  24  VAL   A HG12 1 
ATOM   652  H HG13 A VAL   A 1 24  ? 19.030 5.871   12.053  0.68 21.32 ?  24  VAL   A HG13 1 
ATOM   653  H HG13 B VAL   A 1 24  ? 19.496 5.339   11.781  0.32 21.27 ?  24  VAL   A HG13 1 
ATOM   654  H HG21 A VAL   A 1 24  ? 18.283 6.142   8.930   0.68 21.72 ?  24  VAL   A HG21 1 
ATOM   655  H HG21 B VAL   A 1 24  ? 18.551 5.589   8.940   0.32 20.40 ?  24  VAL   A HG21 1 
ATOM   656  H HG22 A VAL   A 1 24  ? 19.428 5.201   9.500   0.68 21.72 ?  24  VAL   A HG22 1 
ATOM   657  H HG22 B VAL   A 1 24  ? 19.415 4.302   9.282   0.32 20.40 ?  24  VAL   A HG22 1 
ATOM   658  H HG23 A VAL   A 1 24  ? 18.191 4.570   8.727   0.68 21.72 ?  24  VAL   A HG23 1 
ATOM   659  H HG23 B VAL   A 1 24  ? 17.962 4.141   8.664   0.32 20.40 ?  24  VAL   A HG23 1 
ATOM   660  N N    A GLU   A 1 25  ? 16.038 3.650   12.802  0.68 18.18 ?  25  GLU   A N    1 
ATOM   661  N N    B GLU   A 1 25  ? 16.117 3.106   12.751  0.32 17.12 ?  25  GLU   A N    1 
ATOM   662  C CA   A GLU   A 1 25  ? 15.457 3.580   14.137  0.68 19.46 ?  25  GLU   A CA   1 
ATOM   663  C CA   B GLU   A 1 25  ? 15.464 2.987   14.050  0.32 18.06 ?  25  GLU   A CA   1 
ATOM   664  C C    A GLU   A 1 25  ? 15.700 2.224   14.785  0.68 18.29 ?  25  GLU   A C    1 
ATOM   665  C C    B GLU   A 1 25  ? 15.760 1.638   14.692  0.32 17.43 ?  25  GLU   A C    1 
ATOM   666  O O    A GLU   A 1 25  ? 15.893 2.151   16.004  0.68 19.05 ?  25  GLU   A O    1 
ATOM   667  O O    B GLU   A 1 25  ? 16.069 1.572   15.887  0.32 17.62 ?  25  GLU   A O    1 
ATOM   668  C CB   A GLU   A 1 25  ? 13.965 3.918   14.080  0.68 21.70 ?  25  GLU   A CB   1 
ATOM   669  C CB   B GLU   A 1 25  ? 13.959 3.222   13.909  0.32 19.12 ?  25  GLU   A CB   1 
ATOM   670  C CG   A GLU   A 1 25  ? 13.697 5.371   13.704  0.68 24.70 ?  25  GLU   A CG   1 
ATOM   671  C CG   B GLU   A 1 25  ? 13.606 4.647   13.514  0.32 20.76 ?  25  GLU   A CG   1 
ATOM   672  C CD   A GLU   A 1 25  ? 14.487 6.347   14.556  0.68 27.16 ?  25  GLU   A CD   1 
ATOM   673  C CD   B GLU   A 1 25  ? 14.063 5.670   14.538  0.32 22.13 ?  25  GLU   A CD   1 
ATOM   674  O OE1  A GLU   A 1 25  ? 14.507 6.180   15.795  0.68 27.84 ?  25  GLU   A OE1  1 
ATOM   675  O OE1  B GLU   A 1 25  ? 14.008 5.368   15.750  0.32 22.36 ?  25  GLU   A OE1  1 
ATOM   676  O OE2  A GLU   A 1 25  ? 15.112 7.265   13.983  0.68 28.25 -1 25  GLU   A OE2  1 
ATOM   677  O OE2  B GLU   A 1 25  ? 14.482 6.774   14.131  0.32 22.91 -1 25  GLU   A OE2  1 
ATOM   678  H H    A GLU   A 1 25  ? 15.464 3.705   12.162  0.68 21.79 ?  25  GLU   A H    1 
ATOM   679  H H    B GLU   A 1 25  ? 15.580 3.126   12.083  0.32 20.52 ?  25  GLU   A H    1 
ATOM   680  H HA   A GLU   A 1 25  ? 15.886 4.240   14.698  0.68 23.33 ?  25  GLU   A HA   1 
ATOM   681  H HA   B GLU   A 1 25  ? 15.817 3.663   14.641  0.32 21.65 ?  25  GLU   A HA   1 
ATOM   682  H HB2  A GLU   A 1 25  ? 13.535 3.356   13.414  0.68 26.02 ?  25  GLU   A HB2  1 
ATOM   683  H HB2  B GLU   A 1 25  ? 13.609 2.631   13.224  0.32 22.92 ?  25  GLU   A HB2  1 
ATOM   684  H HB3  A GLU   A 1 25  ? 13.568 3.759   14.951  0.68 26.02 ?  25  GLU   A HB3  1 
ATOM   685  H HB3  B GLU   A 1 25  ? 13.528 3.035   14.757  0.32 22.92 ?  25  GLU   A HB3  1 
ATOM   686  H HG2  A GLU   A 1 25  ? 13.957 5.514   12.782  0.68 29.61 ?  25  GLU   A HG2  1 
ATOM   687  H HG2  B GLU   A 1 25  ? 14.039 4.858   12.672  0.32 24.89 ?  25  GLU   A HG2  1 
ATOM   688  H HG3  A GLU   A 1 25  ? 12.750 5.560   13.817  0.68 29.61 ?  25  GLU   A HG3  1 
ATOM   689  H HG3  B GLU   A 1 25  ? 12.644 4.722   13.422  0.32 24.89 ?  25  GLU   A HG3  1 
ATOM   690  N N    A GLU   A 1 26  ? 15.721 1.151   13.992  0.68 18.10 ?  26  GLU   A N    1 
ATOM   691  N N    B GLU   A 1 26  ? 15.687 0.551   13.917  0.32 17.26 ?  26  GLU   A N    1 
ATOM   692  C CA   A GLU   A 1 26  ? 15.998 -0.175  14.541  0.68 18.01 ?  26  GLU   A CA   1 
ATOM   693  C CA   B GLU   A 1 26  ? 16.131 -0.735  14.441  0.32 17.50 ?  26  GLU   A CA   1 
ATOM   694  C C    A GLU   A 1 26  ? 17.420 -0.263  15.090  0.68 17.21 ?  26  GLU   A C    1 
ATOM   695  C C    B GLU   A 1 26  ? 17.558 -0.642  14.953  0.32 17.19 ?  26  GLU   A C    1 
ATOM   696  O O    A GLU   A 1 26  ? 17.637 -0.737  16.211  0.68 16.93 ?  26  GLU   A O    1 
ATOM   697  O O    B GLU   A 1 26  ? 17.902 -1.266  15.963  0.32 16.95 ?  26  GLU   A O    1 
ATOM   698  C CB   A GLU   A 1 26  ? 15.794 -1.233  13.457  0.68 19.51 ?  26  GLU   A CB   1 
ATOM   699  C CB   B GLU   A 1 26  ? 16.020 -1.832  13.376  0.32 18.28 ?  26  GLU   A CB   1 
ATOM   700  C CG   A GLU   A 1 26  ? 14.366 -1.694  13.265  0.68 22.48 ?  26  GLU   A CG   1 
ATOM   701  C CG   B GLU   A 1 26  ? 14.625 -2.373  13.176  0.32 18.04 ?  26  GLU   A CG   1 
ATOM   702  C CD   A GLU   A 1 26  ? 13.822 -2.449  14.456  0.68 24.57 ?  26  GLU   A CD   1 
ATOM   703  C CD   B GLU   A 1 26  ? 14.066 -2.990  14.441  0.32 17.39 ?  26  GLU   A CD   1 
ATOM   704  O OE1  A GLU   A 1 26  ? 14.417 -3.473  14.852  0.68 25.27 ?  26  GLU   A OE1  1 
ATOM   705  O OE1  B GLU   A 1 26  ? 14.462 -4.124  14.811  0.32 17.10 ?  26  GLU   A OE1  1 
ATOM   706  O OE2  A GLU   A 1 26  ? 12.796 -1.994  15.000  0.68 26.18 -1 26  GLU   A OE2  1 
ATOM   707  O OE2  B GLU   A 1 26  ? 13.237 -2.323  15.076  0.32 16.97 -1 26  GLU   A OE2  1 
ATOM   708  H H    A GLU   A 1 26  ? 15.586 1.169   13.141  0.68 21.70 ?  26  GLU   A H    1 
ATOM   709  H H    B GLU   A 1 26  ? 15.396 0.527   13.109  0.32 20.69 ?  26  GLU   A H    1 
ATOM   710  H HA   A GLU   A 1 26  ? 15.381 -0.353  15.262  0.68 21.59 ?  26  GLU   A HA   1 
ATOM   711  H HA   B GLU   A 1 26  ? 15.576 -0.984  15.194  0.32 20.98 ?  26  GLU   A HA   1 
ATOM   712  H HB2  A GLU   A 1 26  ? 16.096 -0.867  12.608  0.68 23.39 ?  26  GLU   A HB2  1 
ATOM   713  H HB2  B GLU   A 1 26  ? 16.319 -1.478  12.528  0.32 21.91 ?  26  GLU   A HB2  1 
ATOM   714  H HB3  A GLU   A 1 26  ? 16.330 -2.008  13.682  0.68 23.39 ?  26  GLU   A HB3  1 
ATOM   715  H HB3  B GLU   A 1 26  ? 16.583 -2.582  13.636  0.32 21.91 ?  26  GLU   A HB3  1 
ATOM   716  H HG2  A GLU   A 1 26  ? 13.792 -0.927  13.169  0.68 26.95 ?  26  GLU   A HG2  1 
ATOM   717  H HG2  B GLU   A 1 26  ? 14.043 -1.650  12.880  0.32 21.62 ?  26  GLU   A HG2  1 
ATOM   718  H HG3  A GLU   A 1 26  ? 14.320 -2.250  12.467  0.68 26.95 ?  26  GLU   A HG3  1 
ATOM   719  H HG3  B GLU   A 1 26  ? 14.639 -3.075  12.510  0.32 21.62 ?  26  GLU   A HG3  1 
ATOM   720  N N    . ALA   A 1 27  ? 18.404 0.152   14.289  1.00 17.06 ?  27  ALA   A N    1 
ATOM   721  C CA   . ALA   A 1 27  ? 19.797 0.170   14.722  1.00 16.97 ?  27  ALA   A CA   1 
ATOM   722  C C    . ALA   A 1 27  ? 19.966 0.968   16.009  1.00 19.17 ?  27  ALA   A C    1 
ATOM   723  O O    . ALA   A 1 27  ? 20.640 0.522   16.944  1.00 19.00 ?  27  ALA   A O    1 
ATOM   724  C CB   . ALA   A 1 27  ? 20.695 0.717   13.607  1.00 16.40 ?  27  ALA   A CB   1 
ATOM   725  H H    A ALA   A 1 27  ? 18.287 0.423   13.477  0.68 20.45 ?  27  ALA   A H    1 
ATOM   726  H H    B ALA   A 1 27  ? 18.206 0.666   13.625  0.32 20.45 ?  27  ALA   A H    1 
ATOM   727  H HA   . ALA   A 1 27  ? 20.077 -0.739  14.898  1.00 20.34 ?  27  ALA   A HA   1 
ATOM   728  H HB1  . ALA   A 1 27  ? 21.618 0.721   13.917  1.00 19.66 ?  27  ALA   A HB1  1 
ATOM   729  H HB2  . ALA   A 1 27  ? 20.618 0.147   12.825  1.00 19.66 ?  27  ALA   A HB2  1 
ATOM   730  H HB3  . ALA   A 1 27  ? 20.421 1.620   13.386  1.00 19.66 ?  27  ALA   A HB3  1 
ATOM   731  N N    A LYS   A 1 28  ? 19.349 2.150   16.081  0.68 20.70 ?  28  LYS   A N    1 
ATOM   732  N N    B LYS   A 1 28  ? 19.352 2.152   16.079  0.32 21.25 ?  28  LYS   A N    1 
ATOM   733  C CA   A LYS   A 1 28  ? 19.479 2.967   17.282  0.68 23.67 ?  28  LYS   A CA   1 
ATOM   734  C CA   B LYS   A 1 28  ? 19.473 2.973   17.280  0.32 23.93 ?  28  LYS   A CA   1 
ATOM   735  C C    A LYS   A 1 28  ? 18.928 2.255   18.509  0.68 24.61 ?  28  LYS   A C    1 
ATOM   736  C C    B LYS   A 1 28  ? 18.925 2.259   18.509  0.32 24.71 ?  28  LYS   A C    1 
ATOM   737  O O    A LYS   A 1 28  ? 19.465 2.418   19.611  0.68 25.98 ?  28  LYS   A O    1 
ATOM   738  O O    B LYS   A 1 28  ? 19.454 2.433   19.613  0.32 25.53 ?  28  LYS   A O    1 
ATOM   739  C CB   A LYS   A 1 28  ? 18.808 4.328   17.078  0.68 25.98 ?  28  LYS   A CB   1 
ATOM   740  C CB   B LYS   A 1 28  ? 18.775 4.320   17.077  0.32 25.80 ?  28  LYS   A CB   1 
ATOM   741  C CG   A LYS   A 1 28  ? 19.629 5.269   16.210  0.68 28.23 ?  28  LYS   A CG   1 
ATOM   742  C CG   B LYS   A 1 28  ? 19.540 5.270   16.167  0.32 27.53 ?  28  LYS   A CG   1 
ATOM   743  C CD   A LYS   A 1 28  ? 19.135 6.704   16.278  0.68 30.68 ?  28  LYS   A CD   1 
ATOM   744  C CD   B LYS   A 1 28  ? 19.027 6.699   16.266  0.32 29.25 ?  28  LYS   A CD   1 
ATOM   745  C CE   A LYS   A 1 28  ? 17.866 6.891   15.475  0.68 32.35 ?  28  LYS   A CE   1 
ATOM   746  C CE   B LYS   A 1 28  ? 17.739 6.890   15.489  0.32 30.44 ?  28  LYS   A CE   1 
ATOM   747  N NZ   A LYS   A 1 28  ? 17.461 8.322   15.417  0.68 33.46 ?  28  LYS   A NZ   1 
ATOM   748  N NZ   B LYS   A 1 28  ? 17.356 8.328   15.411  0.32 31.18 ?  28  LYS   A NZ   1 
ATOM   749  H H    A LYS   A 1 28  ? 18.861 2.490   15.463  0.68 24.82 ?  28  LYS   A H    1 
ATOM   750  H H    B LYS   A 1 28  ? 18.871 2.494   15.456  0.32 25.48 ?  28  LYS   A H    1 
ATOM   751  H HA   A LYS   A 1 28  ? 20.417 3.129   17.449  0.68 28.38 ?  28  LYS   A HA   1 
ATOM   752  H HA   B LYS   A 1 28  ? 20.410 3.151   17.445  0.32 28.69 ?  28  LYS   A HA   1 
ATOM   753  H HB2  A LYS   A 1 28  ? 17.951 4.198   16.646  0.68 31.15 ?  28  LYS   A HB2  1 
ATOM   754  H HB2  B LYS   A 1 28  ? 17.905 4.168   16.679  0.32 30.94 ?  28  LYS   A HB2  1 
ATOM   755  H HB3  A LYS   A 1 28  ? 18.684 4.753   17.941  0.68 31.15 ?  28  LYS   A HB3  1 
ATOM   756  H HB3  B LYS   A 1 28  ? 18.672 4.754   17.938  0.32 30.94 ?  28  LYS   A HB3  1 
ATOM   757  H HG2  A LYS   A 1 28  ? 20.551 5.255   16.510  0.68 33.85 ?  28  LYS   A HG2  1 
ATOM   758  H HG2  B LYS   A 1 28  ? 20.476 5.268   16.420  0.32 33.02 ?  28  LYS   A HG2  1 
ATOM   759  H HG3  A LYS   A 1 28  ? 19.575 4.977   15.287  0.68 33.85 ?  28  LYS   A HG3  1 
ATOM   760  H HG3  B LYS   A 1 28  ? 19.442 4.978   15.247  0.32 33.02 ?  28  LYS   A HG3  1 
ATOM   761  H HD2  A LYS   A 1 28  ? 18.948 6.935   17.202  0.68 36.79 ?  28  LYS   A HD2  1 
ATOM   762  H HD2  B LYS   A 1 28  ? 18.854 6.914   17.197  0.32 35.08 ?  28  LYS   A HD2  1 
ATOM   763  H HD3  A LYS   A 1 28  ? 19.815 7.294   15.916  0.68 36.79 ?  28  LYS   A HD3  1 
ATOM   764  H HD3  B LYS   A 1 28  ? 19.693 7.304   15.903  0.32 35.08 ?  28  LYS   A HD3  1 
ATOM   765  H HE2  A LYS   A 1 28  ? 18.014 6.580   14.568  0.68 38.79 ?  28  LYS   A HE2  1 
ATOM   766  H HE2  B LYS   A 1 28  ? 17.858 6.558   14.586  0.32 36.51 ?  28  LYS   A HE2  1 
ATOM   767  H HE3  A LYS   A 1 28  ? 17.148 6.388   15.890  0.68 38.79 ?  28  LYS   A HE3  1 
ATOM   768  H HE3  B LYS   A 1 28  ? 17.023 6.409   15.932  0.32 36.51 ?  28  LYS   A HE3  1 
ATOM   769  H HZ1  A LYS   A 1 28  ? 16.715 8.407   14.940  0.68 40.13 ?  28  LYS   A HZ1  1 
ATOM   770  H HZ1  B LYS   A 1 28  ? 16.600 8.417   14.951  0.32 37.40 ?  28  LYS   A HZ1  1 
ATOM   771  H HZ2  A LYS   A 1 28  ? 17.317 8.630   16.239  0.68 40.13 ?  28  LYS   A HZ2  1 
ATOM   772  H HZ2  B LYS   A 1 28  ? 17.238 8.656   16.230  0.32 37.40 ?  28  LYS   A HZ2  1 
ATOM   773  H HZ3  A LYS   A 1 28  ? 18.105 8.805   15.036  0.68 40.13 ?  28  LYS   A HZ3  1 
ATOM   774  H HZ3  B LYS   A 1 28  ? 17.999 8.791   15.004  0.32 37.40 ?  28  LYS   A HZ3  1 
ATOM   775  N N    . LYS   A 1 29  ? 17.879 1.450   18.341  1.00 24.85 ?  29  LYS   A N    1 
ATOM   776  C CA   . LYS   A 1 29  ? 17.289 0.741   19.474  1.00 27.23 ?  29  LYS   A CA   1 
ATOM   777  C C    . LYS   A 1 29  ? 18.114 -0.484  19.861  1.00 26.37 ?  29  LYS   A C    1 
ATOM   778  O O    . LYS   A 1 29  ? 18.403 -0.702  21.043  1.00 27.68 ?  29  LYS   A O    1 
ATOM   779  C CB   . LYS   A 1 29  ? 15.857 0.324   19.128  1.00 30.76 ?  29  LYS   A CB   1 
ATOM   780  C CG   . LYS   A 1 29  ? 15.102 -0.344  20.268  1.00 34.32 ?  29  LYS   A CG   1 
ATOM   781  C CD   . LYS   A 1 29  ? 14.725 0.660   21.343  1.00 37.44 ?  29  LYS   A CD   1 
ATOM   782  C CE   . LYS   A 1 29  ? 13.843 0.027   22.409  1.00 39.53 ?  29  LYS   A CE   1 
ATOM   783  N NZ   . LYS   A 1 29  ? 13.428 1.016   23.442  1.00 40.78 ?  29  LYS   A NZ   1 
ATOM   784  H H    A LYS   A 1 29  ? 17.494 1.296   17.588  0.68 29.80 ?  29  LYS   A H    1 
ATOM   785  H H    B LYS   A 1 29  ? 17.492 1.297   17.588  0.32 29.80 ?  29  LYS   A H    1 
ATOM   786  H HA   . LYS   A 1 29  ? 17.251 1.335   20.238  1.00 32.65 ?  29  LYS   A HA   1 
ATOM   787  H HB2  . LYS   A 1 29  ? 15.355 1.115   18.872  1.00 36.89 ?  29  LYS   A HB2  1 
ATOM   788  H HB3  . LYS   A 1 29  ? 15.882 -0.301  18.388  1.00 36.89 ?  29  LYS   A HB3  1 
ATOM   789  H HG2  . LYS   A 1 29  ? 14.286 -0.740  19.923  1.00 41.16 ?  29  LYS   A HG2  1 
ATOM   790  H HG3  . LYS   A 1 29  ? 15.658 -1.030  20.673  1.00 41.16 ?  29  LYS   A HG3  1 
ATOM   791  H HD2  . LYS   A 1 29  ? 15.531 0.989   21.771  1.00 44.90 ?  29  LYS   A HD2  1 
ATOM   792  H HD3  . LYS   A 1 29  ? 14.235 1.393   20.938  1.00 44.90 ?  29  LYS   A HD3  1 
ATOM   793  H HE2  . LYS   A 1 29  ? 13.043 -0.329  21.991  1.00 47.42 ?  29  LYS   A HE2  1 
ATOM   794  H HE3  . LYS   A 1 29  ? 14.335 -0.683  22.850  1.00 47.42 ?  29  LYS   A HE3  1 
ATOM   795  H HZ1  . LYS   A 1 29  ? 12.914 0.621   24.052  1.00 48.92 ?  29  LYS   A HZ1  1 
ATOM   796  H HZ2  . LYS   A 1 29  ? 14.146 1.355   23.844  1.00 48.92 ?  29  LYS   A HZ2  1 
ATOM   797  H HZ3  . LYS   A 1 29  ? 12.970 1.678   23.062  1.00 48.92 ?  29  LYS   A HZ3  1 
ATOM   798  N N    . VAL   A 1 30  ? 18.484 -1.303  18.878  1.00 24.93 ?  30  VAL   A N    1 
ATOM   799  C CA   . VAL   A 1 30  ? 19.135 -2.575  19.169  1.00 24.17 ?  30  VAL   A CA   1 
ATOM   800  C C    . VAL   A 1 30  ? 20.638 -2.414  19.387  1.00 23.24 ?  30  VAL   A C    1 
ATOM   801  O O    . VAL   A 1 30  ? 21.231 -3.143  20.190  1.00 23.75 ?  30  VAL   A O    1 
ATOM   802  C CB   . VAL   A 1 30  ? 18.834 -3.573  18.036  1.00 25.12 ?  30  VAL   A CB   1 
ATOM   803  C CG1  . VAL   A 1 30  ? 19.586 -4.877  18.250  1.00 25.77 ?  30  VAL   A CG1  1 
ATOM   804  C CG2  . VAL   A 1 30  ? 17.336 -3.826  17.932  1.00 25.57 ?  30  VAL   A CG2  1 
ATOM   805  H H    . VAL   A 1 30  ? 18.351 -1.155  18.041  1.00 29.89 ?  30  VAL   A H    1 
ATOM   806  H HA   . VAL   A 1 30  ? 18.751 -2.939  19.981  1.00 28.98 ?  30  VAL   A HA   1 
ATOM   807  H HB   . VAL   A 1 30  ? 19.133 -3.195  17.196  1.00 30.12 ?  30  VAL   A HB   1 
ATOM   808  H HG11 . VAL   A 1 30  ? 19.204 -5.557  17.672  1.00 30.90 ?  30  VAL   A HG11 1 
ATOM   809  H HG12 . VAL   A 1 30  ? 20.520 -4.746  18.032  1.00 30.90 ?  30  VAL   A HG12 1 
ATOM   810  H HG13 . VAL   A 1 30  ? 19.493 -5.146  19.177  1.00 30.90 ?  30  VAL   A HG13 1 
ATOM   811  H HG21 . VAL   A 1 30  ? 17.176 -4.498  17.250  1.00 30.66 ?  30  VAL   A HG21 1 
ATOM   812  H HG22 . VAL   A 1 30  ? 17.009 -4.142  18.789  1.00 30.66 ?  30  VAL   A HG22 1 
ATOM   813  H HG23 . VAL   A 1 30  ? 16.892 -2.999  17.692  1.00 30.66 ?  30  VAL   A HG23 1 
ATOM   814  N N    . LYS   A 1 31  ? 21.275 -1.474  18.698  1.00 21.91 ?  31  LYS   A N    1 
ATOM   815  C CA   . LYS   A 1 31  ? 22.729 -1.369  18.656  1.00 22.61 ?  31  LYS   A CA   1 
ATOM   816  C C    . LYS   A 1 31  ? 23.338 -2.726  18.292  1.00 19.99 ?  31  LYS   A C    1 
ATOM   817  O O    . LYS   A 1 31  ? 24.115 -3.295  19.065  1.00 21.18 ?  31  LYS   A O    1 
ATOM   818  C CB   . LYS   A 1 31  ? 23.301 -0.848  19.967  1.00 27.58 ?  31  LYS   A CB   1 
ATOM   819  C CG   . LYS   A 1 31  ? 22.602 0.396   20.500  1.00 33.09 ?  31  LYS   A CG   1 
ATOM   820  C CD   . LYS   A 1 31  ? 23.587 1.526   20.766  1.00 37.53 ?  31  LYS   A CD   1 
ATOM   821  C CE   . LYS   A 1 31  ? 22.991 2.575   21.696  1.00 40.44 ?  31  LYS   A CE   1 
ATOM   822  N NZ   . LYS   A 1 31  ? 21.721 3.152   21.177  1.00 41.59 ?  31  LYS   A NZ   1 
ATOM   823  H H    . LYS   A 1 31  ? 20.875 -0.864  18.242  1.00 26.27 ?  31  LYS   A H    1 
ATOM   824  H HA   . LYS   A 1 31  ? 22.968 -0.740  17.963  1.00 27.11 ?  31  LYS   A HA   1 
ATOM   825  H HB2  . LYS   A 1 31  ? 23.227 -1.543  20.635  1.00 33.07 ?  31  LYS   A HB2  1 
ATOM   826  H HB3  . LYS   A 1 31  ? 24.237 -0.625  19.831  1.00 33.07 ?  31  LYS   A HB3  1 
ATOM   827  H HG2  . LYS   A 1 31  ? 21.957 0.707   19.846  1.00 39.69 ?  31  LYS   A HG2  1 
ATOM   828  H HG3  . LYS   A 1 31  ? 22.156 0.180   21.334  1.00 39.69 ?  31  LYS   A HG3  1 
ATOM   829  H HD2  . LYS   A 1 31  ? 24.385 1.167   21.186  1.00 45.01 ?  31  LYS   A HD2  1 
ATOM   830  H HD3  . LYS   A 1 31  ? 23.815 1.957   19.926  1.00 45.01 ?  31  LYS   A HD3  1 
ATOM   831  H HE2  . LYS   A 1 31  ? 22.805 2.165   22.555  1.00 48.50 ?  31  LYS   A HE2  1 
ATOM   832  H HE3  . LYS   A 1 31  ? 23.627 3.299   21.804  1.00 48.50 ?  31  LYS   A HE3  1 
ATOM   833  H HZ1  . LYS   A 1 31  ? 21.412 3.766   21.742  1.00 49.88 ?  31  LYS   A HZ1  1 
ATOM   834  H HZ2  . LYS   A 1 31  ? 21.860 3.532   20.385  1.00 49.88 ?  31  LYS   A HZ2  1 
ATOM   835  H HZ3  . LYS   A 1 31  ? 21.110 2.511   21.086  1.00 49.88 ?  31  LYS   A HZ3  1 
ATOM   836  N N    . PRO   A 1 32  ? 22.991 -3.272  17.131  1.00 17.69 ?  32  PRO   A N    1 
ATOM   837  C CA   . PRO   A 1 32  ? 23.469 -4.606  16.772  1.00 18.16 ?  32  PRO   A CA   1 
ATOM   838  C C    . PRO   A 1 32  ? 24.970 -4.614  16.566  1.00 17.55 ?  32  PRO   A C    1 
ATOM   839  O O    . PRO   A 1 32  ? 25.610 -3.579  16.369  1.00 17.47 ?  32  PRO   A O    1 
ATOM   840  C CB   . PRO   A 1 32  ? 22.743 -4.890  15.454  1.00 18.11 ?  32  PRO   A CB   1 
ATOM   841  C CG   . PRO   A 1 32  ? 22.553 -3.530  14.856  1.00 16.79 ?  32  PRO   A CG   1 
ATOM   842  C CD   . PRO   A 1 32  ? 22.251 -2.643  16.025  1.00 16.62 ?  32  PRO   A CD   1 
ATOM   843  H HA   . PRO   A 1 32  ? 23.221 -5.260  17.442  1.00 21.77 ?  32  PRO   A HA   1 
ATOM   844  H HB2  . PRO   A 1 32  ? 23.297 -5.450  14.884  1.00 21.71 ?  32  PRO   A HB2  1 
ATOM   845  H HB3  . PRO   A 1 32  ? 21.890 -5.319  15.633  1.00 21.71 ?  32  PRO   A HB3  1 
ATOM   846  H HG2  . PRO   A 1 32  ? 23.365 -3.259  14.407  1.00 20.12 ?  32  PRO   A HG2  1 
ATOM   847  H HG3  . PRO   A 1 32  ? 21.805 -3.556  14.235  1.00 20.12 ?  32  PRO   A HG3  1 
ATOM   848  H HD2  . PRO   A 1 32  ? 22.585 -1.749  15.851  1.00 19.92 ?  32  PRO   A HD2  1 
ATOM   849  H HD3  . PRO   A 1 32  ? 21.301 -2.641  16.207  1.00 19.92 ?  32  PRO   A HD3  1 
ATOM   850  N N    . THR   A 1 33  ? 25.529 -5.821  16.591  1.00 17.77 ?  33  THR   A N    1 
ATOM   851  C CA   . THR   A 1 33  ? 26.939 -5.981  16.266  1.00 17.85 ?  33  THR   A CA   1 
ATOM   852  C C    . THR   A 1 33  ? 27.228 -5.510  14.848  1.00 16.13 ?  33  THR   A C    1 
ATOM   853  O O    . THR   A 1 33  ? 28.255 -4.860  14.599  1.00 16.54 ?  33  THR   A O    1 
ATOM   854  C CB   . THR   A 1 33  ? 27.343 -7.444  16.451  1.00 19.60 ?  33  THR   A CB   1 
ATOM   855  O OG1  . THR   A 1 33  ? 27.040 -7.854  17.787  1.00 21.32 ?  33  THR   A OG1  1 
ATOM   856  C CG2  . THR   A 1 33  ? 28.832 -7.635  16.192  1.00 20.56 ?  33  THR   A CG2  1 
ATOM   857  H H    . THR   A 1 33  ? 25.120 -6.551  16.783  1.00 21.30 ?  33  THR   A H    1 
ATOM   858  H HA   . THR   A 1 33  ? 27.473 -5.447  16.874  1.00 21.40 ?  33  THR   A HA   1 
ATOM   859  H HB   . THR   A 1 33  ? 26.849 -8.001  15.824  1.00 23.49 ?  33  THR   A HB   1 
ATOM   860  H HG1  . THR   A 1 33  ? 27.464 -7.381  18.337  1.00 25.56 ?  33  THR   A HG1  1 
ATOM   861  H HG21 . THR   A 1 33  ? 29.103 -8.526  16.464  1.00 24.65 ?  33  THR   A HG21 1 
ATOM   862  H HG22 . THR   A 1 33  ? 29.023 -7.524  15.248  1.00 24.65 ?  33  THR   A HG22 1 
ATOM   863  H HG23 . THR   A 1 33  ? 29.338 -6.983  16.699  1.00 24.65 ?  33  THR   A HG23 1 
ATOM   864  N N    . VAL   A 1 34  ? 26.330 -5.816  13.910  1.00 14.30 ?  34  VAL   A N    1 
ATOM   865  C CA   . VAL   A 1 34  ? 26.517 -5.482  12.502  1.00 13.07 ?  34  VAL   A CA   1 
ATOM   866  C C    . VAL   A 1 34  ? 25.214 -4.925  11.940  1.00 12.56 ?  34  VAL   A C    1 
ATOM   867  O O    . VAL   A 1 34  ? 24.173 -5.594  11.994  1.00 13.25 ?  34  VAL   A O    1 
ATOM   868  C CB   . VAL   A 1 34  ? 26.968 -6.689  11.656  1.00 13.66 ?  34  VAL   A CB   1 
ATOM   869  C CG1  . VAL   A 1 34  ? 27.144 -6.285  10.201  1.00 14.03 ?  34  VAL   A CG1  1 
ATOM   870  C CG2  . VAL   A 1 34  ? 28.249 -7.308  12.213  1.00 15.26 ?  34  VAL   A CG2  1 
ATOM   871  H H    . VAL   A 1 34  ? 25.586 -6.225  14.069  1.00 17.14 ?  34  VAL   A H    1 
ATOM   872  H HA   . VAL   A 1 34  ? 27.192 -4.789  12.424  1.00 15.66 ?  34  VAL   A HA   1 
ATOM   873  H HB   . VAL   A 1 34  ? 26.272 -7.365  11.694  1.00 16.37 ?  34  VAL   A HB   1 
ATOM   874  H HG11 . VAL   A 1 34  ? 27.635 -6.982  9.741   1.00 16.81 ?  34  VAL   A HG11 1 
ATOM   875  H HG12 . VAL   A 1 34  ? 26.273 -6.167  9.793   1.00 16.81 ?  34  VAL   A HG12 1 
ATOM   876  H HG13 . VAL   A 1 34  ? 27.644 -5.452  10.164  1.00 16.81 ?  34  VAL   A HG13 1 
ATOM   877  H HG21 . VAL   A 1 34  ? 28.519 -8.040  11.638  1.00 18.29 ?  34  VAL   A HG21 1 
ATOM   878  H HG22 . VAL   A 1 34  ? 28.943 -6.630  12.236  1.00 18.29 ?  34  VAL   A HG22 1 
ATOM   879  H HG23 . VAL   A 1 34  ? 28.079 -7.637  13.110  1.00 18.29 ?  34  VAL   A HG23 1 
ATOM   880  N N    . VAL   A 1 35  ? 25.272 -3.711  11.390  1.00 11.79 ?  35  VAL   A N    1 
ATOM   881  C CA   . VAL   A 1 35  ? 24.237 -3.190  10.505  1.00 11.49 ?  35  VAL   A CA   1 
ATOM   882  C C    . VAL   A 1 35  ? 24.791 -3.190  9.087   1.00 10.68 ?  35  VAL   A C    1 
ATOM   883  O O    . VAL   A 1 35  ? 25.938 -2.794  8.860   1.00 11.42 ?  35  VAL   A O    1 
ATOM   884  C CB   . VAL   A 1 35  ? 23.708 -1.798  10.920  1.00 12.37 ?  35  VAL   A CB   1 
ATOM   885  C CG1  . VAL   A 1 35  ? 24.771 -0.705  10.788  1.00 12.49 ?  35  VAL   A CG1  1 
ATOM   886  C CG2  . VAL   A 1 35  ? 22.459 -1.440  10.104  1.00 13.06 ?  35  VAL   A CG2  1 
ATOM   887  H H    . VAL   A 1 35  ? 25.916 -3.156  11.512  1.00 14.12 ?  35  VAL   A H    1 
ATOM   888  H HA   . VAL   A 1 35  ? 23.477 -3.797  10.520  1.00 13.76 ?  35  VAL   A HA   1 
ATOM   889  H HB   . VAL   A 1 35  ? 23.438 -1.830  11.847  1.00 14.82 ?  35  VAL   A HB   1 
ATOM   890  H HG11 . VAL   A 1 35  ? 24.427 0.123   11.161  1.00 14.97 ?  35  VAL   A HG11 1 
ATOM   891  H HG12 . VAL   A 1 35  ? 25.565 -0.979  11.271  1.00 14.97 ?  35  VAL   A HG12 1 
ATOM   892  H HG13 . VAL   A 1 35  ? 24.985 -0.575  9.848   1.00 14.97 ?  35  VAL   A HG13 1 
ATOM   893  H HG21 . VAL   A 1 35  ? 22.112 -0.590  10.410  1.00 15.64 ?  35  VAL   A HG21 1 
ATOM   894  H HG22 . VAL   A 1 35  ? 22.705 -1.376  9.163   1.00 15.64 ?  35  VAL   A HG22 1 
ATOM   895  H HG23 . VAL   A 1 35  ? 21.795 -2.135  10.223  1.00 15.64 ?  35  VAL   A HG23 1 
ATOM   896  N N    . VAL   A 1 36  ? 23.978 -3.642  8.138   1.00 9.97  ?  36  VAL   A N    1 
ATOM   897  C CA   . VAL   A 1 36  ? 24.348 -3.652  6.733   1.00 10.00 ?  36  VAL   A CA   1 
ATOM   898  C C    . VAL   A 1 36  ? 23.885 -2.360  6.073   1.00 10.47 ?  36  VAL   A C    1 
ATOM   899  O O    . VAL   A 1 36  ? 22.724 -1.951  6.215   1.00 11.00 ?  36  VAL   A O    1 
ATOM   900  C CB   . VAL   A 1 36  ? 23.743 -4.869  6.011   1.00 10.12 ?  36  VAL   A CB   1 
ATOM   901  C CG1  . VAL   A 1 36  ? 23.998 -4.787  4.520   1.00 10.56 ?  36  VAL   A CG1  1 
ATOM   902  C CG2  . VAL   A 1 36  ? 24.294 -6.166  6.580   1.00 10.96 ?  36  VAL   A CG2  1 
ATOM   903  H H    . VAL   A 1 36  ? 23.184 -3.959  8.286   1.00 11.94 ?  36  VAL   A H    1 
ATOM   904  H HA   . VAL   A 1 36  ? 25.314 -3.712  6.655   1.00 11.98 ?  36  VAL   A HA   1 
ATOM   905  H HB   . VAL   A 1 36  ? 22.781 -4.871  6.146   1.00 12.12 ?  36  VAL   A HB   1 
ATOM   906  H HG11 . VAL   A 1 36  ? 23.864 -5.663  4.125   1.00 12.65 ?  36  VAL   A HG11 1 
ATOM   907  H HG12 . VAL   A 1 36  ? 23.382 -4.150  4.123   1.00 12.65 ?  36  VAL   A HG12 1 
ATOM   908  H HG13 . VAL   A 1 36  ? 24.914 -4.498  4.372   1.00 12.65 ?  36  VAL   A HG13 1 
ATOM   909  H HG21 . VAL   A 1 36  ? 23.903 -6.921  6.104   1.00 13.13 ?  36  VAL   A HG21 1 
ATOM   910  H HG22 . VAL   A 1 36  ? 25.260 -6.181  6.471   1.00 13.13 ?  36  VAL   A HG22 1 
ATOM   911  H HG23 . VAL   A 1 36  ? 24.070 -6.227  7.523   1.00 13.13 ?  36  VAL   A HG23 1 
ATOM   912  N N    . ASN   A 1 37  ? 24.797 -1.728  5.335   1.00 9.62  ?  37  ASN   A N    1 
ATOM   913  C CA   . ASN   A 1 37  ? 24.465 -0.606  4.474   1.00 9.69  ?  37  ASN   A CA   1 
ATOM   914  C C    . ASN   A 1 37  ? 24.326 -1.072  3.035   1.00 9.81  ?  37  ASN   A C    1 
ATOM   915  O O    . ASN   A 1 37  ? 25.111 -1.898  2.557   1.00 10.27 ?  37  ASN   A O    1 
ATOM   916  C CB   . ASN   A 1 37  ? 25.544 0.476   4.553   1.00 9.77  ?  37  ASN   A CB   1 
ATOM   917  C CG   . ASN   A 1 37  ? 25.219 1.669   3.707   1.00 10.36 ?  37  ASN   A CG   1 
ATOM   918  O OD1  . ASN   A 1 37  ? 24.045 2.004   3.525   1.00 10.88 ?  37  ASN   A OD1  1 
ATOM   919  N ND2  . ASN   A 1 37  ? 26.247 2.325   3.186   1.00 10.61 ?  37  ASN   A ND2  1 
ATOM   920  H H    . ASN   A 1 37  ? 25.637 -1.931  5.329   1.00 11.52 ?  37  ASN   A H    1 
ATOM   921  H HA   . ASN   A 1 37  ? 23.625 -0.216  4.763   1.00 11.60 ?  37  ASN   A HA   1 
ATOM   922  H HB2  . ASN   A 1 37  ? 25.629 0.775   5.478   1.00 11.70 ?  37  ASN   A HB2  1 
ATOM   923  H HB3  . ASN   A 1 37  ? 26.390 0.107   4.251   1.00 11.70 ?  37  ASN   A HB3  1 
ATOM   924  H HD21 . ASN   A 1 37  ? 26.111 3.018   2.690   1.00 12.71 ?  37  ASN   A HD21 1 
ATOM   925  H HD22 . ASN   A 1 37  ? 27.048 2.067   3.336   1.00 12.71 ?  37  ASN   A HD22 1 
ATOM   926  N N    . ALA   A 1 38  ? 23.308 -0.539  2.354   1.00 10.30 ?  38  ALA   A N    1 
ATOM   927  C CA   . ALA   A 1 38  ? 23.121 -0.697  0.912   1.00 10.32 ?  38  ALA   A CA   1 
ATOM   928  C C    . ALA   A 1 38  ? 24.016 0.314   0.196   1.00 10.07 ?  38  ALA   A C    1 
ATOM   929  O O    . ALA   A 1 38  ? 23.586 1.395   -0.215  1.00 10.53 ?  38  ALA   A O    1 
ATOM   930  C CB   . ALA   A 1 38  ? 21.656 -0.486  0.557   1.00 11.66 ?  38  ALA   A CB   1 
ATOM   931  H H    . ALA   A 1 38  ? 22.702 -0.055  2.724   1.00 12.34 ?  38  ALA   A H    1 
ATOM   932  H HA   . ALA   A 1 38  ? 23.381 -1.594  0.646   1.00 12.36 ?  38  ALA   A HA   1 
ATOM   933  H HB1  . ALA   A 1 38  ? 21.540 -0.608  -0.398  1.00 13.97 ?  38  ALA   A HB1  1 
ATOM   934  H HB2  . ALA   A 1 38  ? 21.114 -1.132  1.040   1.00 13.97 ?  38  ALA   A HB2  1 
ATOM   935  H HB3  . ALA   A 1 38  ? 21.395 0.414   0.810   1.00 13.97 ?  38  ALA   A HB3  1 
ATOM   936  N N    A ALA   A 1 39  ? 25.283 -0.060  0.041   0.68 10.32 ?  39  ALA   A N    1 
ATOM   937  N N    B ALA   A 1 39  ? 25.289 -0.036  0.065   0.32 10.18 ?  39  ALA   A N    1 
ATOM   938  C CA   A ALA   A 1 39  ? 26.330 0.828   -0.435  0.68 10.45 ?  39  ALA   A CA   1 
ATOM   939  C CA   B ALA   A 1 39  ? 26.282 0.904   -0.431  0.32 10.49 ?  39  ALA   A CA   1 
ATOM   940  C C    A ALA   A 1 39  ? 26.443 0.797   -1.957  0.68 10.32 ?  39  ALA   A C    1 
ATOM   941  C C    B ALA   A 1 39  ? 26.465 0.774   -1.936  0.32 9.89  ?  39  ALA   A C    1 
ATOM   942  O O    A ALA   A 1 39  ? 25.923 -0.093  -2.634  0.68 10.84 ?  39  ALA   A O    1 
ATOM   943  O O    B ALA   A 1 39  ? 26.099 -0.231  -2.550  0.32 9.51  ?  39  ALA   A O    1 
ATOM   944  C CB   A ALA   A 1 39  ? 27.662 0.418   0.197   0.68 10.81 ?  39  ALA   A CB   1 
ATOM   945  C CB   B ALA   A 1 39  ? 27.623 0.662   0.256   0.32 11.35 ?  39  ALA   A CB   1 
ATOM   946  H H    A ALA   A 1 39  ? 25.562 -0.860  0.212   0.68 12.36 ?  39  ALA   A H    1 
ATOM   947  H H    B ALA   A 1 39  ? 25.602 -0.818  0.256   0.32 12.20 ?  39  ALA   A H    1 
ATOM   948  H HA   A ALA   A 1 39  ? 26.120 1.735   -0.159  0.68 12.51 ?  39  ALA   A HA   1 
ATOM   949  H HA   B ALA   A 1 39  ? 25.990 1.806   -0.230  0.32 12.56 ?  39  ALA   A HA   1 
ATOM   950  H HB1  A ALA   A 1 39  ? 28.352 1.020   -0.121  0.68 12.95 ?  39  ALA   A HB1  1 
ATOM   951  H HB1  B ALA   A 1 39  ? 28.267 1.299   -0.089  0.32 13.60 ?  39  ALA   A HB1  1 
ATOM   952  H HB2  A ALA   A 1 39  ? 27.585 0.486   1.164   0.68 12.95 ?  39  ALA   A HB2  1 
ATOM   953  H HB2  B ALA   A 1 39  ? 27.512 0.784   1.210   0.32 13.60 ?  39  ALA   A HB2  1 
ATOM   954  H HB3  A ALA   A 1 39  ? 27.865 -0.491  -0.057  0.68 12.95 ?  39  ALA   A HB3  1 
ATOM   955  H HB3  B ALA   A 1 39  ? 27.914 -0.242  0.066   0.32 13.60 ?  39  ALA   A HB3  1 
ATOM   956  N N    A ASN   A 1 40  ? 27.146 1.797   -2.493  0.68 10.77 ?  40  ASN   A N    1 
ATOM   957  N N    B ASN   A 1 40  ? 27.054 1.815   -2.528  0.32 10.25 ?  40  ASN   A N    1 
ATOM   958  C CA   A ASN   A 1 40  ? 27.686 1.746   -3.847  0.68 10.61 ?  40  ASN   A CA   1 
ATOM   959  C CA   B ASN   A 1 40  ? 27.577 1.747   -3.883  0.32 10.52 ?  40  ASN   A CA   1 
ATOM   960  C C    A ASN   A 1 40  ? 29.209 1.627   -3.780  0.68 10.04 ?  40  ASN   A C    1 
ATOM   961  C C    B ASN   A 1 40  ? 29.102 1.618   -3.834  0.32 10.31 ?  40  ASN   A C    1 
ATOM   962  O O    A ASN   A 1 40  ? 29.808 1.755   -2.710  0.68 10.55 ?  40  ASN   A O    1 
ATOM   963  O O    B ASN   A 1 40  ? 29.723 1.667   -2.770  0.32 10.48 ?  40  ASN   A O    1 
ATOM   964  C CB   A ASN   A 1 40  ? 27.223 2.941   -4.699  0.68 11.61 ?  40  ASN   A CB   1 
ATOM   965  C CB   B ASN   A 1 40  ? 27.123 2.949   -4.717  0.32 11.46 ?  40  ASN   A CB   1 
ATOM   966  C CG   A ASN   A 1 40  ? 27.617 4.284   -4.114  0.68 12.59 ?  40  ASN   A CG   1 
ATOM   967  C CG   B ASN   A 1 40  ? 27.451 4.274   -4.064  0.32 12.22 ?  40  ASN   A CG   1 
ATOM   968  O OD1  A ASN   A 1 40  ? 28.782 4.511   -3.778  0.68 13.18 ?  40  ASN   A OD1  1 
ATOM   969  O OD1  B ASN   A 1 40  ? 28.620 4.617   -3.882  0.32 12.83 ?  40  ASN   A OD1  1 
ATOM   970  N ND2  A ASN   A 1 40  ? 26.638 5.187   -3.999  0.68 12.99 ?  40  ASN   A ND2  1 
ATOM   971  N ND2  B ASN   A 1 40  ? 26.417 5.033   -3.719  0.32 12.43 ?  40  ASN   A ND2  1 
ATOM   972  H H    A ASN   A 1 40  ? 27.333 2.521   -2.077  0.68 12.91 ?  40  ASN   A H    1 
ATOM   973  H H    B ASN   A 1 40  ? 27.161 2.583   -2.151  0.32 12.27 ?  40  ASN   A H    1 
ATOM   974  H HA   A ASN   A 1 40  ? 27.357 0.944   -4.277  0.68 12.71 ?  40  ASN   A HA   1 
ATOM   975  H HA   B ASN   A 1 40  ? 27.233 0.944   -4.309  0.32 12.60 ?  40  ASN   A HA   1 
ATOM   976  H HB2  A ASN   A 1 40  ? 27.614 2.867   -5.583  0.68 13.91 ?  40  ASN   A HB2  1 
ATOM   977  H HB2  B ASN   A 1 40  ? 27.565 2.920   -5.578  0.32 13.73 ?  40  ASN   A HB2  1 
ATOM   978  H HB3  A ASN   A 1 40  ? 26.254 2.917   -4.766  0.68 13.91 ?  40  ASN   A HB3  1 
ATOM   979  H HB3  B ASN   A 1 40  ? 26.160 2.901   -4.839  0.32 13.73 ?  40  ASN   A HB3  1 
ATOM   980  H HD21 A ASN   A 1 40  ? 26.807 5.969   -3.677  0.68 15.57 ?  40  ASN   A HD21 1 
ATOM   981  H HD21 B ASN   A 1 40  ? 26.552 5.794   -3.344  0.32 14.90 ?  40  ASN   A HD21 1 
ATOM   982  H HD22 A ASN   A 1 40  ? 25.835 4.986   -4.234  0.68 15.57 ?  40  ASN   A HD22 1 
ATOM   983  H HD22 B ASN   A 1 40  ? 25.613 4.763   -3.868  0.32 14.90 ?  40  ASN   A HD22 1 
ATOM   984  N N    A VAL   A 1 41  ? 29.834 1.351   -4.931  0.68 10.60 ?  41  VAL   A N    1 
ATOM   985  N N    B VAL   A 1 41  ? 29.711 1.456   -5.013  0.32 10.50 ?  41  VAL   A N    1 
ATOM   986  C CA   A VAL   A 1 41  ? 31.268 1.055   -4.943  0.68 11.20 ?  41  VAL   A CA   1 
ATOM   987  C CA   B VAL   A 1 41  ? 31.129 1.104   -5.089  0.32 10.75 ?  41  VAL   A CA   1 
ATOM   988  C C    A VAL   A 1 41  ? 32.101 2.230   -4.474  0.68 11.40 ?  41  VAL   A C    1 
ATOM   989  C C    B VAL   A 1 41  ? 32.047 2.210   -4.576  0.32 10.71 ?  41  VAL   A C    1 
ATOM   990  O O    A VAL   A 1 41  ? 33.239 2.033   -4.028  0.68 12.02 ?  41  VAL   A O    1 
ATOM   991  O O    B VAL   A 1 41  ? 33.193 1.935   -4.198  0.32 10.49 ?  41  VAL   A O    1 
ATOM   992  C CB   A VAL   A 1 41  ? 31.786 0.556   -6.313  0.68 11.69 ?  41  VAL   A CB   1 
ATOM   993  C CB   B VAL   A 1 41  ? 31.504 0.699   -6.527  0.32 11.56 ?  41  VAL   A CB   1 
ATOM   994  C CG1  A VAL   A 1 41  ? 31.089 -0.730  -6.728  0.68 12.65 ?  41  VAL   A CG1  1 
ATOM   995  C CG1  B VAL   A 1 41  ? 30.863 -0.633  -6.884  0.32 12.57 ?  41  VAL   A CG1  1 
ATOM   996  C CG2  A VAL   A 1 41  ? 31.679 1.632   -7.393  0.68 11.24 ?  41  VAL   A CG2  1 
ATOM   997  C CG2  B VAL   A 1 41  ? 31.094 1.779   -7.522  0.32 12.06 ?  41  VAL   A CG2  1 
ATOM   998  H H    A VAL   A 1 41  ? 29.456 1.316   -5.703  0.68 12.70 ?  41  VAL   A H    1 
ATOM   999  H H    B VAL   A 1 41  ? 29.313 1.538   -5.773  0.32 12.58 ?  41  VAL   A H    1 
ATOM   1000 H HA   A VAL   A 1 41  ? 31.432 0.336   -4.315  0.68 13.42 ?  41  VAL   A HA   1 
ATOM   1001 H HA   B VAL   A 1 41  ? 31.266 0.327   -4.528  0.32 12.88 ?  41  VAL   A HA   1 
ATOM   1002 H HB   A VAL   A 1 41  ? 32.730 0.342   -6.222  0.68 14.00 ?  41  VAL   A HB   1 
ATOM   1003 H HB   B VAL   A 1 41  ? 32.465 0.589   -6.582  0.32 13.85 ?  41  VAL   A HB   1 
ATOM   1004 H HG11 A VAL   A 1 41  ? 31.444 -1.027  -7.581  0.68 15.15 ?  41  VAL   A HG11 1 
ATOM   1005 H HG11 B VAL   A 1 41  ? 31.142 -0.889  -7.777  0.32 15.06 ?  41  VAL   A HG11 1 
ATOM   1006 H HG12 A VAL   A 1 41  ? 31.244 -1.407  -6.051  0.68 15.15 ?  41  VAL   A HG12 1 
ATOM   1007 H HG12 B VAL   A 1 41  ? 31.149 -1.304  -6.244  0.32 15.06 ?  41  VAL   A HG12 1 
ATOM   1008 H HG13 A VAL   A 1 41  ? 30.136 -0.558  -6.811  0.68 15.15 ?  41  VAL   A HG13 1 
ATOM   1009 H HG13 B VAL   A 1 41  ? 29.898 -0.539  -6.854  0.32 15.06 ?  41  VAL   A HG13 1 
ATOM   1010 H HG21 A VAL   A 1 41  ? 31.883 1.237   -8.258  0.68 13.46 ?  41  VAL   A HG21 1 
ATOM   1011 H HG21 B VAL   A 1 41  ? 31.520 1.598   -8.374  0.32 14.45 ?  41  VAL   A HG21 1 
ATOM   1012 H HG22 A VAL   A 1 41  ? 30.780 1.988   -7.396  0.68 13.46 ?  41  VAL   A HG22 1 
ATOM   1013 H HG22 B VAL   A 1 41  ? 30.129 1.766   -7.630  0.32 14.45 ?  41  VAL   A HG22 1 
ATOM   1014 H HG23 A VAL   A 1 41  ? 32.316 2.339   -7.199  0.68 13.46 ?  41  VAL   A HG23 1 
ATOM   1015 H HG23 B VAL   A 1 41  ? 31.379 2.641   -7.186  0.32 14.45 ?  41  VAL   A HG23 1 
ATOM   1016 N N    . TYR   A 1 42  ? 31.575 3.455   -4.574  1.00 11.25 ?  42  TYR   A N    1 
ATOM   1017 C CA   . TYR   A 1 42  ? 32.320 4.640   -4.160  1.00 11.42 ?  42  TYR   A CA   1 
ATOM   1018 C C    . TYR   A 1 42  ? 32.069 5.013   -2.709  1.00 11.13 ?  42  TYR   A C    1 
ATOM   1019 O O    . TYR   A 1 42  ? 32.628 6.009   -2.228  1.00 11.75 ?  42  TYR   A O    1 
ATOM   1020 C CB   . TYR   A 1 42  ? 31.972 5.832   -5.073  1.00 12.03 ?  42  TYR   A CB   1 
ATOM   1021 C CG   . TYR   A 1 42  ? 32.164 5.519   -6.542  1.00 12.77 ?  42  TYR   A CG   1 
ATOM   1022 C CD1  . TYR   A 1 42  ? 33.428 5.323   -7.072  1.00 13.66 ?  42  TYR   A CD1  1 
ATOM   1023 C CD2  . TYR   A 1 42  ? 31.075 5.400   -7.395  1.00 14.48 ?  42  TYR   A CD2  1 
ATOM   1024 C CE1  . TYR   A 1 42  ? 33.600 5.018   -8.411  1.00 14.39 ?  42  TYR   A CE1  1 
ATOM   1025 C CE2  . TYR   A 1 42  ? 31.242 5.104   -8.735  1.00 15.46 ?  42  TYR   A CE2  1 
ATOM   1026 C CZ   . TYR   A 1 42  ? 32.507 4.911   -9.238  1.00 15.50 ?  42  TYR   A CZ   1 
ATOM   1027 O OH   . TYR   A 1 42  ? 32.675 4.608   -10.571 1.00 17.33 ?  42  TYR   A OH   1 
ATOM   1028 H H    A TYR   A 1 42  ? 30.782 3.621   -4.873  0.68 13.47 ?  42  TYR   A H    1 
ATOM   1029 H H    B TYR   A 1 42  ? 30.780 3.649   -4.850  0.32 13.47 ?  42  TYR   A H    1 
ATOM   1030 H HA   . TYR   A 1 42  ? 33.265 4.465   -4.262  1.00 13.68 ?  42  TYR   A HA   1 
ATOM   1031 H HB2  . TYR   A 1 42  ? 31.041 6.078   -4.937  1.00 14.42 ?  42  TYR   A HB2  1 
ATOM   1032 H HB3  . TYR   A 1 42  ? 32.545 6.584   -4.848  1.00 14.42 ?  42  TYR   A HB3  1 
ATOM   1033 H HD1  . TYR   A 1 42  ? 34.171 5.387   -6.516  1.00 16.37 ?  42  TYR   A HD1  1 
ATOM   1034 H HD2  . TYR   A 1 42  ? 30.219 5.536   -7.059  1.00 17.35 ?  42  TYR   A HD2  1 
ATOM   1035 H HE1  . TYR   A 1 42  ? 34.458 4.888   -8.752  1.00 17.25 ?  42  TYR   A HE1  1 
ATOM   1036 H HE2  . TYR   A 1 42  ? 30.502 5.037   -9.295  1.00 18.53 ?  42  TYR   A HE2  1 
ATOM   1037 H HH   . TYR   A 1 42  ? 33.497 4.515   -10.740 1.00 20.77 ?  42  TYR   A HH   1 
ATOM   1038 N N    . LEU   A 1 43  ? 31.218 4.249   -2.021  1.00 10.85 ?  43  LEU   A N    1 
ATOM   1039 C CA   . LEU   A 1 43  ? 30.765 4.580   -0.673  1.00 10.61 ?  43  LEU   A CA   1 
ATOM   1040 C C    . LEU   A 1 43  ? 30.279 6.024   -0.571  1.00 10.55 ?  43  LEU   A C    1 
ATOM   1041 O O    . LEU   A 1 43  ? 30.540 6.722   0.411   1.00 12.08 ?  43  LEU   A O    1 
ATOM   1042 C CB   . LEU   A 1 43  ? 31.812 4.274   0.396   1.00 11.63 ?  43  LEU   A CB   1 
ATOM   1043 C CG   . LEU   A 1 43  ? 32.314 2.826   0.477   1.00 11.27 ?  43  LEU   A CG   1 
ATOM   1044 C CD1  . LEU   A 1 43  ? 33.358 2.720   1.568   1.00 12.38 ?  43  LEU   A CD1  1 
ATOM   1045 C CD2  . LEU   A 1 43  ? 31.178 1.838   0.725   1.00 11.73 ?  43  LEU   A CD2  1 
ATOM   1046 H H    . LEU   A 1 43  ? 30.880 3.510   -2.320  1.00 13.00 ?  43  LEU   A H    1 
ATOM   1047 H HA   . LEU   A 1 43  ? 29.999 4.014   -0.472  1.00 12.71 ?  43  LEU   A HA   1 
ATOM   1048 H HB2  . LEU   A 1 43  ? 32.584 4.840   0.236   1.00 13.94 ?  43  LEU   A HB2  1 
ATOM   1049 H HB3  . LEU   A 1 43  ? 31.432 4.492   1.264   1.00 13.94 ?  43  LEU   A HB3  1 
ATOM   1050 H HG   . LEU   A 1 43  ? 32.741 2.593   -0.360  1.00 13.50 ?  43  LEU   A HG   1 
ATOM   1051 H HD11 . LEU   A 1 43  ? 33.677 1.802   1.616   1.00 14.84 ?  43  LEU   A HD11 1 
ATOM   1052 H HD12 . LEU   A 1 43  ? 34.100 3.312   1.362   1.00 14.84 ?  43  LEU   A HD12 1 
ATOM   1053 H HD13 . LEU   A 1 43  ? 32.962 2.972   2.417   1.00 14.84 ?  43  LEU   A HD13 1 
ATOM   1054 H HD21 . LEU   A 1 43  ? 31.555 0.954   0.862   1.00 14.05 ?  43  LEU   A HD21 1 
ATOM   1055 H HD22 . LEU   A 1 43  ? 30.689 2.115   1.515   1.00 14.05 ?  43  LEU   A HD22 1 
ATOM   1056 H HD23 . LEU   A 1 43  ? 30.594 1.835   -0.046  1.00 14.05 ?  43  LEU   A HD23 1 
ATOM   1057 N N    A LYS   A 1 44  ? 29.561 6.473   -1.598  0.68 10.64 ?  44  LYS   A N    1 
ATOM   1058 N N    B LYS   A 1 44  ? 29.545 6.466   -1.593  0.32 11.36 ?  44  LYS   A N    1 
ATOM   1059 C CA   A LYS   A 1 44  ? 28.937 7.794   -1.593  0.68 10.99 ?  44  LYS   A CA   1 
ATOM   1060 C CA   B LYS   A 1 44  ? 28.863 7.755   -1.571  0.32 12.41 ?  44  LYS   A CA   1 
ATOM   1061 C C    A LYS   A 1 44  ? 27.504 7.623   -1.106  0.68 10.05 ?  44  LYS   A C    1 
ATOM   1062 C C    B LYS   A 1 44  ? 27.455 7.518   -1.035  0.32 11.81 ?  44  LYS   A C    1 
ATOM   1063 O O    A LYS   A 1 44  ? 26.640 7.124   -1.832  0.68 11.56 ?  44  LYS   A O    1 
ATOM   1064 O O    B LYS   A 1 44  ? 26.601 6.962   -1.734  0.32 12.10 ?  44  LYS   A O    1 
ATOM   1065 C CB   A LYS   A 1 44  ? 29.002 8.420   -2.980  0.68 13.34 ?  44  LYS   A CB   1 
ATOM   1066 C CB   B LYS   A 1 44  ? 28.810 8.362   -2.970  0.32 14.39 ?  44  LYS   A CB   1 
ATOM   1067 C CG   A LYS   A 1 44  ? 30.388 8.899   -3.378  0.68 16.83 ?  44  LYS   A CG   1 
ATOM   1068 C CG   B LYS   A 1 44  ? 30.152 8.802   -3.532  0.32 16.79 ?  44  LYS   A CG   1 
ATOM   1069 C CD   A LYS   A 1 44  ? 31.029 9.782   -2.313  0.68 21.51 ?  44  LYS   A CD   1 
ATOM   1070 C CD   B LYS   A 1 44  ? 30.827 9.857   -2.669  0.32 19.52 ?  44  LYS   A CD   1 
ATOM   1071 C CE   A LYS   A 1 44  ? 32.382 10.290  -2.765  0.68 23.99 ?  44  LYS   A CE   1 
ATOM   1072 C CE   B LYS   A 1 44  ? 31.987 10.498  -3.417  0.32 21.28 ?  44  LYS   A CE   1 
ATOM   1073 N NZ   A LYS   A 1 44  ? 33.144 10.919  -1.655  0.68 25.29 ?  44  LYS   A NZ   1 
ATOM   1074 N NZ   B LYS   A 1 44  ? 33.080 10.948  -2.512  0.32 22.51 ?  44  LYS   A NZ   1 
ATOM   1075 H H    A LYS   A 1 44  ? 29.426 6.026   -2.321  0.68 12.74 ?  44  LYS   A H    1 
ATOM   1076 H H    B LYS   A 1 44  ? 29.419 6.022   -2.320  0.32 13.61 ?  44  LYS   A H    1 
ATOM   1077 H HA   A LYS   A 1 44  ? 29.393 8.360   -0.953  0.68 13.16 ?  44  LYS   A HA   1 
ATOM   1078 H HA   B LYS   A 1 44  ? 29.325 8.364   -0.975  0.32 14.87 ?  44  LYS   A HA   1 
ATOM   1079 H HB2  A LYS   A 1 44  ? 28.715 7.764   -3.634  0.68 15.98 ?  44  LYS   A HB2  1 
ATOM   1080 H HB2  B LYS   A 1 44  ? 28.441 7.706   -3.579  0.32 17.24 ?  44  LYS   A HB2  1 
ATOM   1081 H HB3  A LYS   A 1 44  ? 28.407 9.187   -3.002  0.68 15.98 ?  44  LYS   A HB3  1 
ATOM   1082 H HB3  B LYS   A 1 44  ? 28.236 9.144   -2.946  0.32 17.24 ?  44  LYS   A HB3  1 
ATOM   1083 H HG2  A LYS   A 1 44  ? 30.963 8.130   -3.519  0.68 20.17 ?  44  LYS   A HG2  1 
ATOM   1084 H HG2  B LYS   A 1 44  ? 30.743 8.034   -3.585  0.32 20.12 ?  44  LYS   A HG2  1 
ATOM   1085 H HG3  A LYS   A 1 44  ? 30.322 9.418   -4.198  0.68 20.17 ?  44  LYS   A HG3  1 
ATOM   1086 H HG3  B LYS   A 1 44  ? 30.019 9.180   -4.416  0.32 20.12 ?  44  LYS   A HG3  1 
ATOM   1087 H HD2  A LYS   A 1 44  ? 30.446 10.538  -2.134  0.68 25.79 ?  44  LYS   A HD2  1 
ATOM   1088 H HD2  B LYS   A 1 44  ? 30.187 10.548  -2.441  0.32 23.40 ?  44  LYS   A HD2  1 
ATOM   1089 H HD3  A LYS   A 1 44  ? 31.167 9.263   -1.504  0.68 25.79 ?  44  LYS   A HD3  1 
ATOM   1090 H HD3  B LYS   A 1 44  ? 31.176 9.440   -1.863  0.32 23.40 ?  44  LYS   A HD3  1 
ATOM   1091 H HE2  A LYS   A 1 44  ? 32.902 9.544   -3.104  0.68 28.77 ?  44  LYS   A HE2  1 
ATOM   1092 H HE2  B LYS   A 1 44  ? 32.358 9.852   -4.038  0.32 25.52 ?  44  LYS   A HE2  1 
ATOM   1093 H HE3  A LYS   A 1 44  ? 32.254 10.952  -3.461  0.68 28.77 ?  44  LYS   A HE3  1 
ATOM   1094 H HE3  B LYS   A 1 44  ? 31.660 11.273  -3.900  0.32 25.52 ?  44  LYS   A HE3  1 
ATOM   1095 H HZ1  A LYS   A 1 44  ? 33.931 11.207  -1.954  0.68 30.32 ?  44  LYS   A HZ1  1 
ATOM   1096 H HZ1  B LYS   A 1 44  ? 33.737 11.316  -2.988  0.32 26.99 ?  44  LYS   A HZ1  1 
ATOM   1097 H HZ2  A LYS   A 1 44  ? 32.688 11.612  -1.329  0.68 30.32 ?  44  LYS   A HZ2  1 
ATOM   1098 H HZ2  B LYS   A 1 44  ? 32.770 11.549  -1.934  0.32 26.99 ?  44  LYS   A HZ2  1 
ATOM   1099 H HZ3  A LYS   A 1 44  ? 33.278 10.329  -1.004  0.68 30.32 ?  44  LYS   A HZ3  1 
ATOM   1100 H HZ3  B LYS   A 1 44  ? 33.406 10.254  -2.060  0.32 26.99 ?  44  LYS   A HZ3  1 
ATOM   1101 N N    A HIS   A 1 45  ? 27.258 8.028   0.139   0.68 9.92  ?  45  HIS   A N    1 
ATOM   1102 N N    B HIS   A 1 45  ? 27.217 7.926   0.211   0.32 11.86 ?  45  HIS   A N    1 
ATOM   1103 C CA   A HIS   A 1 45  ? 26.033 7.654   0.848   0.68 10.21 ?  45  HIS   A CA   1 
ATOM   1104 C CA   B HIS   A 1 45  ? 25.948 7.661   0.886   0.32 11.96 ?  45  HIS   A CA   1 
ATOM   1105 C C    A HIS   A 1 45  ? 24.963 8.738   0.697   0.68 11.28 ?  45  HIS   A C    1 
ATOM   1106 C C    B HIS   A 1 45  ? 25.034 8.862   0.667   0.32 12.60 ?  45  HIS   A C    1 
ATOM   1107 O O    A HIS   A 1 45  ? 24.616 9.460   1.632   0.68 12.77 ?  45  HIS   A O    1 
ATOM   1108 O O    B HIS   A 1 45  ? 24.918 9.763   1.501   0.32 13.31 ?  45  HIS   A O    1 
ATOM   1109 C CB   A HIS   A 1 45  ? 26.347 7.386   2.307   0.68 10.28 ?  45  HIS   A CB   1 
ATOM   1110 C CB   B HIS   A 1 45  ? 26.191 7.395   2.363   0.32 11.58 ?  45  HIS   A CB   1 
ATOM   1111 C CG   A HIS   A 1 45  ? 27.452 6.400   2.511   0.68 10.17 ?  45  HIS   A CG   1 
ATOM   1112 C CG   B HIS   A 1 45  ? 27.337 6.471   2.622   0.32 10.64 ?  45  HIS   A CG   1 
ATOM   1113 N ND1  A HIS   A 1 45  ? 27.413 5.112   2.015   0.68 10.49 ?  45  HIS   A ND1  1 
ATOM   1114 N ND1  B HIS   A 1 45  ? 27.391 5.190   2.117   0.32 10.93 ?  45  HIS   A ND1  1 
ATOM   1115 C CD2  A HIS   A 1 45  ? 28.638 6.530   3.150   0.68 10.62 ?  45  HIS   A CD2  1 
ATOM   1116 C CD2  B HIS   A 1 45  ? 28.482 6.652   3.322   0.32 9.68  ?  45  HIS   A CD2  1 
ATOM   1117 C CE1  A HIS   A 1 45  ? 28.530 4.492   2.355   0.68 10.66 ?  45  HIS   A CE1  1 
ATOM   1118 C CE1  B HIS   A 1 45  ? 28.519 4.620   2.502   0.32 9.79  ?  45  HIS   A CE1  1 
ATOM   1119 N NE2  A HIS   A 1 45  ? 29.290 5.329   3.042   0.68 10.94 ?  45  HIS   A NE2  1 
ATOM   1120 N NE2  B HIS   A 1 45  ? 29.199 5.485   3.234   0.32 9.35  ?  45  HIS   A NE2  1 
ATOM   1121 H H    A HIS   A 1 45  ? 27.787 8.533   0.599   0.68 11.88 ?  45  HIS   A H    1 
ATOM   1122 H H    B HIS   A 1 45  ? 27.773 8.375   0.687   0.32 14.20 ?  45  HIS   A H    1 
ATOM   1123 H HA   A HIS   A 1 45  ? 25.686 6.839   0.461   0.68 12.22 ?  45  HIS   A HA   1 
ATOM   1124 H HA   B HIS   A 1 45  ? 25.534 6.870   0.498   0.32 14.33 ?  45  HIS   A HA   1 
ATOM   1125 H HB2  A HIS   A 1 45  ? 26.604 8.219   2.734   0.68 12.31 ?  45  HIS   A HB2  1 
ATOM   1126 H HB2  B HIS   A 1 45  ? 26.382 8.237   2.805   0.32 13.87 ?  45  HIS   A HB2  1 
ATOM   1127 H HB3  A HIS   A 1 45  ? 25.552 7.030   2.737   0.68 12.31 ?  45  HIS   A HB3  1 
ATOM   1128 H HB3  B HIS   A 1 45  ? 25.396 6.995   2.748   0.32 13.87 ?  45  HIS   A HB3  1 
ATOM   1129 H HD2  A HIS   A 1 45  ? 28.959 7.295   3.581   0.68 12.72 ?  45  HIS   A HD2  1 
ATOM   1130 H HD2  B HIS   A 1 45  ? 28.738 7.425   3.776   0.32 11.59 ?  45  HIS   A HD2  1 
ATOM   1131 H HE1  A HIS   A 1 45  ? 28.742 3.610   2.156   0.68 12.77 ?  45  HIS   A HE1  1 
ATOM   1132 H HE1  B HIS   A 1 45  ? 28.786 3.755   2.296   0.32 11.72 ?  45  HIS   A HE1  1 
ATOM   1133 H HE2  A HIS   A 1 45  ? 30.068 5.149   3.369   0.68 13.10 ?  45  HIS   A HE2  1 
ATOM   1134 H HE2  B HIS   A 1 45  ? 29.965 5.341   3.596   0.32 11.20 ?  45  HIS   A HE2  1 
ATOM   1135 N N    A GLY   A 1 46  ? 24.417 8.824   -0.511  0.68 12.73 ?  46  GLY   A N    1 
ATOM   1136 N N    B GLY   A 1 46  ? 24.390 8.880   -0.495  0.32 12.99 ?  46  GLY   A N    1 
ATOM   1137 C CA   A GLY   A 1 46  ? 23.570 9.951   -0.859  0.68 13.67 ?  46  GLY   A CA   1 
ATOM   1138 C CA   B GLY   A 1 46  ? 23.567 10.016  -0.864  0.32 13.08 ?  46  GLY   A CA   1 
ATOM   1139 C C    A GLY   A 1 46  ? 22.087 9.784   -0.613  0.68 13.95 ?  46  GLY   A C    1 
ATOM   1140 C C    B GLY   A 1 46  ? 22.105 9.912   -0.472  0.32 12.75 ?  46  GLY   A C    1 
ATOM   1141 O O    A GLY   A 1 46  ? 21.411 10.748  -0.233  0.68 15.35 ?  46  GLY   A O    1 
ATOM   1142 O O    B GLY   A 1 46  ? 21.474 10.930  -0.169  0.32 13.43 ?  46  GLY   A O    1 
ATOM   1143 H H    A GLY   A 1 46  ? 24.515 8.247   -1.140  0.68 15.26 ?  46  GLY   A H    1 
ATOM   1144 H H    B GLY   A 1 46  ? 24.429 8.256   -1.090  0.32 15.57 ?  46  GLY   A H    1 
ATOM   1145 H HA2  A GLY   A 1 46  ? 23.852 10.727  -0.353  0.68 16.38 ?  46  GLY   A HA2  1 
ATOM   1146 H HA2  B GLY   A 1 46  ? 23.933 10.813  -0.445  0.32 15.67 ?  46  GLY   A HA2  1 
ATOM   1147 H HA3  A GLY   A 1 46  ? 23.677 10.149  -1.798  0.68 16.38 ?  46  GLY   A HA3  1 
ATOM   1148 H HA3  B GLY   A 1 46  ? 23.611 10.135  -1.823  0.32 15.67 ?  46  GLY   A HA3  1 
ATOM   1149 N N    A GLY   A 1 47  ? 21.560 8.586   -0.845  0.68 13.31 ?  47  GLY   A N    1 
ATOM   1150 N N    B GLY   A 1 47  ? 21.553 8.704   -0.486  0.32 12.11 ?  47  GLY   A N    1 
ATOM   1151 C CA   A GLY   A 1 47  ? 20.130 8.375   -0.790  0.68 12.97 ?  47  GLY   A CA   1 
ATOM   1152 C CA   B GLY   A 1 47  ? 20.136 8.525   -0.250  0.32 11.82 ?  47  GLY   A CA   1 
ATOM   1153 C C    A GLY   A 1 47  ? 19.812 6.955   -0.382  0.68 12.34 ?  47  GLY   A C    1 
ATOM   1154 C C    B GLY   A 1 47  ? 19.803 7.090   0.101   0.32 11.38 ?  47  GLY   A C    1 
ATOM   1155 O O    A GLY   A 1 47  ? 20.704 6.128   -0.176  0.68 12.20 ?  47  GLY   A O    1 
ATOM   1156 O O    B GLY   A 1 47  ? 20.690 6.260   0.317   0.32 10.99 ?  47  GLY   A O    1 
ATOM   1157 H H    A GLY   A 1 47  ? 22.012 7.872   -1.026  0.68 15.95 ?  47  GLY   A H    1 
ATOM   1158 H H    B GLY   A 1 47  ? 21.986 7.976   -0.629  0.32 14.51 ?  47  GLY   A H    1 
ATOM   1159 H HA2  A GLY   A 1 47  ? 19.726 8.981   -0.148  0.68 15.54 ?  47  GLY   A HA2  1 
ATOM   1160 H HA2  B GLY   A 1 47  ? 19.850 9.083   0.488   0.32 14.16 ?  47  GLY   A HA2  1 
ATOM   1161 H HA3  A GLY   A 1 47  ? 19.738 8.535   -1.661  0.68 15.54 ?  47  GLY   A HA3  1 
ATOM   1162 H HA3  B GLY   A 1 47  ? 19.637 8.783   -1.044  0.32 14.16 ?  47  GLY   A HA3  1 
ATOM   1163 N N    A GLY   A 1 48  ? 18.518 6.670   -0.286  0.68 12.53 ?  48  GLY   A N    1 
ATOM   1164 N N    B GLY   A 1 48  ? 18.501 6.813   0.172   0.32 11.99 ?  48  GLY   A N    1 
ATOM   1165 C CA   A GLY   A 1 48  ? 18.108 5.357   0.148   0.68 12.89 ?  48  GLY   A CA   1 
ATOM   1166 C CA   B GLY   A 1 48  ? 18.050 5.474   0.513   0.32 12.01 ?  48  GLY   A CA   1 
ATOM   1167 C C    A GLY   A 1 48  ? 18.592 5.072   1.554   0.68 11.86 ?  48  GLY   A C    1 
ATOM   1168 C C    B GLY   A 1 48  ? 18.551 5.065   1.883   0.32 11.65 ?  48  GLY   A C    1 
ATOM   1169 O O    A GLY   A 1 48  ? 18.779 5.974   2.382   0.68 11.98 ?  48  GLY   A O    1 
ATOM   1170 O O    B GLY   A 1 48  ? 18.655 5.881   2.809   0.32 11.68 ?  48  GLY   A O    1 
ATOM   1171 H H    A GLY   A 1 48  ? 17.869 7.213   -0.452  0.68 15.01 ?  48  GLY   A H    1 
ATOM   1172 H H    B GLY   A 1 48  ? 17.865 7.380   0.039   0.32 14.37 ?  48  GLY   A H    1 
ATOM   1173 H HA2  A GLY   A 1 48  ? 17.142 5.285   0.137   0.68 15.44 ?  48  GLY   A HA2  1 
ATOM   1174 H HA2  B GLY   A 1 48  ? 17.076 5.440   0.497   0.32 14.39 ?  48  GLY   A HA2  1 
ATOM   1175 H HA3  A GLY   A 1 48  ? 18.480 4.685   -0.442  0.68 15.44 ?  48  GLY   A HA3  1 
ATOM   1176 H HA3  B GLY   A 1 48  ? 18.386 4.836   -0.137  0.32 14.39 ?  48  GLY   A HA3  1 
ATOM   1177 N N    A VAL   A 1 49  ? 18.805 3.782   1.823   0.68 11.83 ?  49  VAL   A N    1 
ATOM   1178 N N    B VAL   A 1 49  ? 18.875 3.777   2.012   0.32 11.10 ?  49  VAL   A N    1 
ATOM   1179 C CA   A VAL   A 1 49  ? 19.320 3.346   3.119   0.68 11.78 ?  49  VAL   A CA   1 
ATOM   1180 C CA   B VAL   A 1 49  ? 19.441 3.263   3.257   0.32 10.81 ?  49  VAL   A CA   1 
ATOM   1181 C C    A VAL   A 1 49  ? 20.626 4.057   3.449   0.68 10.61 ?  49  VAL   A C    1 
ATOM   1182 C C    B VAL   A 1 49  ? 20.740 3.982   3.590   0.32 9.87  ?  49  VAL   A C    1 
ATOM   1183 O O    A VAL   A 1 49  ? 20.825 4.523   4.575   0.68 10.92 ?  49  VAL   A O    1 
ATOM   1184 O O    B VAL   A 1 49  ? 20.990 4.336   4.748   0.32 9.77  ?  49  VAL   A O    1 
ATOM   1185 C CB   A VAL   A 1 49  ? 19.493 1.815   3.136   0.68 12.18 ?  49  VAL   A CB   1 
ATOM   1186 C CB   B VAL   A 1 49  ? 19.649 1.739   3.157   0.32 11.35 ?  49  VAL   A CB   1 
ATOM   1187 C CG1  A VAL   A 1 49  ? 20.241 1.370   4.399   0.68 12.16 ?  49  VAL   A CG1  1 
ATOM   1188 C CG1  B VAL   A 1 49  ? 20.675 1.273   4.173   0.32 10.99 ?  49  VAL   A CG1  1 
ATOM   1189 C CG2  A VAL   A 1 49  ? 18.141 1.113   3.010   0.68 13.78 ?  49  VAL   A CG2  1 
ATOM   1190 C CG2  B VAL   A 1 49  ? 18.347 1.005   3.378   0.32 12.71 ?  49  VAL   A CG2  1 
ATOM   1191 H H    A VAL   A 1 49  ? 18.664 3.141   1.273   0.68 14.17 ?  49  VAL   A H    1 
ATOM   1192 H H    B VAL   A 1 49  ? 18.786 3.187   1.393   0.32 13.30 ?  49  VAL   A H    1 
ATOM   1193 H HA   A VAL   A 1 49  ? 18.681 3.576   3.811   0.68 14.11 ?  49  VAL   A HA   1 
ATOM   1194 H HA   B VAL   A 1 49  ? 18.815 3.426   3.978   0.32 12.95 ?  49  VAL   A HA   1 
ATOM   1195 H HB   A VAL   A 1 49  ? 20.037 1.555   2.375   0.68 14.60 ?  49  VAL   A HB   1 
ATOM   1196 H HB   B VAL   A 1 49  ? 19.980 1.517   2.271   0.32 13.60 ?  49  VAL   A HB   1 
ATOM   1197 H HG11 A VAL   A 1 49  ? 20.099 0.421   4.530   0.68 14.57 ?  49  VAL   A HG11 1 
ATOM   1198 H HG11 B VAL   A 1 49  ? 20.592 0.314   4.284   0.32 13.17 ?  49  VAL   A HG11 1 
ATOM   1199 H HG12 A VAL   A 1 49  ? 21.188 1.552   4.292   0.68 14.57 ?  49  VAL   A HG12 1 
ATOM   1200 H HG12 B VAL   A 1 49  ? 21.567 1.487   3.851   0.32 13.17 ?  49  VAL   A HG12 1 
ATOM   1201 H HG13 A VAL   A 1 49  ? 19.892 1.864   5.160   0.68 14.57 ?  49  VAL   A HG13 1 
ATOM   1202 H HG13 B VAL   A 1 49  ? 20.509 1.716   5.019   0.32 13.17 ?  49  VAL   A HG13 1 
ATOM   1203 H HG21 A VAL   A 1 49  ? 18.283 0.154   3.038   0.68 16.51 ?  49  VAL   A HG21 1 
ATOM   1204 H HG21 B VAL   A 1 49  ? 18.340 0.207   2.825   0.32 15.23 ?  49  VAL   A HG21 1 
ATOM   1205 H HG22 A VAL   A 1 49  ? 17.578 1.388   3.750   0.68 16.51 ?  49  VAL   A HG22 1 
ATOM   1206 H HG22 B VAL   A 1 49  ? 18.278 0.760   4.313   0.32 15.23 ?  49  VAL   A HG22 1 
ATOM   1207 H HG23 A VAL   A 1 49  ? 17.736 1.367   2.169   0.68 16.51 ?  49  VAL   A HG23 1 
ATOM   1208 H HG23 B VAL   A 1 49  ? 17.618 1.592   3.132   0.32 15.23 ?  49  VAL   A HG23 1 
ATOM   1209 N N    A ALA   A 1 50  ? 21.549 4.111   2.485   0.68 10.80 ?  50  ALA   A N    1 
ATOM   1210 N N    B ALA   A 1 50  ? 21.597 4.184   2.586   0.32 9.96  ?  50  ALA   A N    1 
ATOM   1211 C CA   A ALA   A 1 50  ? 22.868 4.673   2.760   0.68 10.60 ?  50  ALA   A CA   1 
ATOM   1212 C CA   B ALA   A 1 50  ? 22.907 4.772   2.838   0.32 9.51  ?  50  ALA   A CA   1 
ATOM   1213 C C    A ALA   A 1 50  ? 22.773 6.136   3.170   0.68 10.41 ?  50  ALA   A C    1 
ATOM   1214 C C    B ALA   A 1 50  ? 22.784 6.216   3.303   0.32 9.02  ?  50  ALA   A C    1 
ATOM   1215 O O    A ALA   A 1 50  ? 23.417 6.563   4.135   0.68 11.48 ?  50  ALA   A O    1 
ATOM   1216 O O    B ALA   A 1 50  ? 23.408 6.618   4.293   0.32 8.82  ?  50  ALA   A O    1 
ATOM   1217 C CB   A ALA   A 1 50  ? 23.758 4.533   1.530   0.68 10.91 ?  50  ALA   A CB   1 
ATOM   1218 C CB   B ALA   A 1 50  ? 23.765 4.685   1.577   0.32 9.35  ?  50  ALA   A CB   1 
ATOM   1219 H H    A ALA   A 1 50  ? 21.442 3.834   1.682   0.68 12.94 ?  50  ALA   A H    1 
ATOM   1220 H H    B ALA   A 1 50  ? 21.440 3.994   1.761   0.32 11.93 ?  50  ALA   A H    1 
ATOM   1221 H HA   A ALA   A 1 50  ? 23.281 4.190   3.494   0.68 12.69 ?  50  ALA   A HA   1 
ATOM   1222 H HA   B ALA   A 1 50  ? 23.349 4.274   3.539   0.32 11.39 ?  50  ALA   A HA   1 
ATOM   1223 H HB1  A ALA   A 1 50  ? 24.628 4.917   1.729   0.68 13.07 ?  50  ALA   A HB1  1 
ATOM   1224 H HB1  B ALA   A 1 50  ? 24.639 5.064   1.763   0.32 11.20 ?  50  ALA   A HB1  1 
ATOM   1225 H HB2  A ALA   A 1 50  ? 23.847 3.597   1.315   0.68 13.07 ?  50  ALA   A HB2  1 
ATOM   1226 H HB2  B ALA   A 1 50  ? 23.857 3.753   1.323   0.32 11.20 ?  50  ALA   A HB2  1 
ATOM   1227 H HB3  A ALA   A 1 50  ? 23.347 5.013   0.794   0.68 13.07 ?  50  ALA   A HB3  1 
ATOM   1228 H HB3  B ALA   A 1 50  ? 23.334 5.181   0.864   0.32 11.20 ?  50  ALA   A HB3  1 
ATOM   1229 N N    A GLY   A 1 51  ? 21.989 6.926   2.439   0.68 10.79 ?  51  GLY   A N    1 
ATOM   1230 N N    B GLY   A 1 51  ? 21.984 7.014   2.596   0.32 10.15 ?  51  GLY   A N    1 
ATOM   1231 C CA   A GLY   A 1 51  ? 21.832 8.319   2.815   0.68 11.17 ?  51  GLY   A CA   1 
ATOM   1232 C CA   B GLY   A 1 51  ? 21.812 8.399   2.997   0.32 10.70 ?  51  GLY   A CA   1 
ATOM   1233 C C    A GLY   A 1 51  ? 21.226 8.469   4.195   0.68 11.22 ?  51  GLY   A C    1 
ATOM   1234 C C    B GLY   A 1 51  ? 21.228 8.519   4.390   0.32 11.06 ?  51  GLY   A C    1 
ATOM   1235 O O    A GLY   A 1 51  ? 21.589 9.373   4.952   0.68 12.06 ?  51  GLY   A O    1 
ATOM   1236 O O    B GLY   A 1 51  ? 21.655 9.361   5.186   0.32 11.48 ?  51  GLY   A O    1 
ATOM   1237 H H    A GLY   A 1 51  ? 21.556 6.687   1.740   0.68 12.92 ?  51  GLY   A H    1 
ATOM   1238 H H    B GLY   A 1 51  ? 21.538 6.779   1.899   0.32 12.16 ?  51  GLY   A H    1 
ATOM   1239 H HA2  A GLY   A 1 51  ? 22.695 8.761   2.811   0.68 13.38 ?  51  GLY   A HA2  1 
ATOM   1240 H HA2  B GLY   A 1 51  ? 22.671 8.849   2.982   0.32 12.81 ?  51  GLY   A HA2  1 
ATOM   1241 H HA3  A GLY   A 1 51  ? 21.253 8.768   2.176   0.68 13.38 ?  51  GLY   A HA3  1 
ATOM   1242 H HA3  B GLY   A 1 51  ? 21.222 8.847   2.365   0.32 12.81 ?  51  GLY   A HA3  1 
ATOM   1243 N N    A ALA   A 1 52  ? 20.281 7.587   4.537   0.68 11.53 ?  52  ALA   A N    1 
ATOM   1244 N N    B ALA   A 1 52  ? 20.244 7.672   4.708   0.32 10.92 ?  52  ALA   A N    1 
ATOM   1245 C CA   A ALA   A 1 52  ? 19.629 7.645   5.841   0.68 11.95 ?  52  ALA   A CA   1 
ATOM   1246 C CA   B ALA   A 1 52  ? 19.622 7.728   6.027   0.32 11.30 ?  52  ALA   A CA   1 
ATOM   1247 C C    A ALA   A 1 52  ? 20.592 7.274   6.967   0.68 11.64 ?  52  ALA   A C    1 
ATOM   1248 C C    B ALA   A 1 52  ? 20.567 7.224   7.116   0.32 10.92 ?  52  ALA   A C    1 
ATOM   1249 O O    A ALA   A 1 52  ? 20.683 7.982   7.976   0.68 12.43 ?  52  ALA   A O    1 
ATOM   1250 O O    B ALA   A 1 52  ? 20.621 7.797   8.212   0.32 11.21 ?  52  ALA   A O    1 
ATOM   1251 C CB   A ALA   A 1 52  ? 18.408 6.724   5.843   0.68 13.19 ?  52  ALA   A CB   1 
ATOM   1252 C CB   B ALA   A 1 52  ? 18.309 6.946   6.018   0.32 12.03 ?  52  ALA   A CB   1 
ATOM   1253 H H    A ALA   A 1 52  ? 20.020 6.940   4.040   0.68 13.81 ?  52  ALA   A H    1 
ATOM   1254 H H    B ALA   A 1 52  ? 19.932 7.062   4.183   0.32 13.08 ?  52  ALA   A H    1 
ATOM   1255 H HA   A ALA   A 1 52  ? 19.321 8.549   5.998   0.68 14.32 ?  52  ALA   A HA   1 
ATOM   1256 H HA   B ALA   A 1 52  ? 19.414 8.651   6.224   0.32 13.54 ?  52  ALA   A HA   1 
ATOM   1257 H HB1  A ALA   A 1 52  ? 17.975 6.778   6.710   0.68 15.80 ?  52  ALA   A HB1  1 
ATOM   1258 H HB1  B ALA   A 1 52  ? 17.912 6.994   6.901   0.32 14.41 ?  52  ALA   A HB1  1 
ATOM   1259 H HB2  A ALA   A 1 52  ? 17.796 7.014   5.150   0.68 15.80 ?  52  ALA   A HB2  1 
ATOM   1260 H HB2  B ALA   A 1 52  ? 17.711 7.342   5.363   0.32 14.41 ?  52  ALA   A HB2  1 
ATOM   1261 H HB3  A ALA   A 1 52  ? 18.697 5.815   5.673   0.68 15.80 ?  52  ALA   A HB3  1 
ATOM   1262 H HB3  B ALA   A 1 52  ? 18.490 6.023   5.784   0.32 14.41 ?  52  ALA   A HB3  1 
ATOM   1263 N N    A LEU   A 1 53  ? 21.308 6.154   6.829   0.68 11.30 ?  53  LEU   A N    1 
ATOM   1264 N N    B LEU   A 1 53  ? 21.317 6.150   6.845   0.32 10.81 ?  53  LEU   A N    1 
ATOM   1265 C CA   A LEU   A 1 53  ? 22.273 5.770   7.859   0.68 11.38 ?  53  LEU   A CA   1 
ATOM   1266 C CA   B LEU   A 1 53  ? 22.312 5.697   7.815   0.32 10.99 ?  53  LEU   A CA   1 
ATOM   1267 C C    A LEU   A 1 53  ? 23.315 6.861   8.046   0.68 10.12 ?  53  LEU   A C    1 
ATOM   1268 C C    B LEU   A 1 53  ? 23.384 6.757   8.028   0.32 10.66 ?  53  LEU   A C    1 
ATOM   1269 O O    A LEU   A 1 53  ? 23.619 7.266   9.174   0.68 11.17 ?  53  LEU   A O    1 
ATOM   1270 O O    B LEU   A 1 53  ? 23.783 7.030   9.166   0.32 11.41 ?  53  LEU   A O    1 
ATOM   1271 C CB   A LEU   A 1 53  ? 22.951 4.441   7.497   0.68 11.72 ?  53  LEU   A CB   1 
ATOM   1272 C CB   B LEU   A 1 53  ? 22.957 4.386   7.358   0.32 10.84 ?  53  LEU   A CB   1 
ATOM   1273 C CG   A LEU   A 1 53  ? 22.066 3.188   7.467   0.68 12.95 ?  53  LEU   A CG   1 
ATOM   1274 C CG   B LEU   A 1 53  ? 22.193 3.073   7.552   0.32 10.56 ?  53  LEU   A CG   1 
ATOM   1275 C CD1  A LEU   A 1 53  ? 22.839 2.003   6.913   0.68 13.11 ?  53  LEU   A CD1  1 
ATOM   1276 C CD1  B LEU   A 1 53  ? 22.955 1.944   6.881   0.32 10.82 ?  53  LEU   A CD1  1 
ATOM   1277 C CD2  A LEU   A 1 53  ? 21.526 2.862   8.847   0.68 14.28 ?  53  LEU   A CD2  1 
ATOM   1278 C CD2  B LEU   A 1 53  ? 21.987 2.757   9.021   0.32 10.43 ?  53  LEU   A CD2  1 
ATOM   1279 H H    A LEU   A 1 53  ? 21.252 5.610   6.165   0.68 13.54 ?  53  LEU   A H    1 
ATOM   1280 H H    B LEU   A 1 53  ? 21.264 5.673   6.127   0.32 12.95 ?  53  LEU   A H    1 
ATOM   1281 H HA   A LEU   A 1 53  ? 21.808 5.649   8.701   0.68 13.64 ?  53  LEU   A HA   1 
ATOM   1282 H HA   B LEU   A 1 53  ? 21.874 5.535   8.663   0.32 13.17 ?  53  LEU   A HA   1 
ATOM   1283 H HB2  A LEU   A 1 53  ? 23.346 4.532   6.614   0.68 14.04 ?  53  LEU   A HB2  1 
ATOM   1284 H HB2  B LEU   A 1 53  ? 23.140 4.462   6.410   0.32 12.98 ?  53  LEU   A HB2  1 
ATOM   1285 H HB3  A LEU   A 1 53  ? 23.655 4.273   8.142   0.68 14.04 ?  53  LEU   A HB3  1 
ATOM   1286 H HB3  B LEU   A 1 53  ? 23.794 4.289   7.835   0.32 12.98 ?  53  LEU   A HB3  1 
ATOM   1287 H HG   A LEU   A 1 53  ? 21.313 3.352   6.876   0.68 15.52 ?  53  LEU   A HG   1 
ATOM   1288 H HG   B LEU   A 1 53  ? 21.323 3.141   7.127   0.32 12.64 ?  53  LEU   A HG   1 
ATOM   1289 H HD11 A LEU   A 1 53  ? 22.258 1.225   6.902   0.68 15.71 ?  53  LEU   A HD11 1 
ATOM   1290 H HD11 B LEU   A 1 53  ? 22.468 1.115   7.011   0.32 12.96 ?  53  LEU   A HD11 1 
ATOM   1291 H HD12 A LEU   A 1 53  ? 23.133 2.208   6.011   0.68 15.71 ?  53  LEU   A HD12 1 
ATOM   1292 H HD12 B LEU   A 1 53  ? 23.037 2.136   5.935   0.32 12.96 ?  53  LEU   A HD12 1 
ATOM   1293 H HD13 A LEU   A 1 53  ? 23.607 1.834   7.481   0.68 15.71 ?  53  LEU   A HD13 1 
ATOM   1294 H HD13 B LEU   A 1 53  ? 23.835 1.877   7.284   0.32 12.96 ?  53  LEU   A HD13 1 
ATOM   1295 H HD21 A LEU   A 1 53  ? 21.020 2.036   8.800   0.68 17.12 ?  53  LEU   A HD21 1 
ATOM   1296 H HD21 B LEU   A 1 53  ? 21.486 1.929   9.099   0.32 12.50 ?  53  LEU   A HD21 1 
ATOM   1297 H HD22 A LEU   A 1 53  ? 22.269 2.763   9.461   0.68 17.12 ?  53  LEU   A HD22 1 
ATOM   1298 H HD22 B LEU   A 1 53  ? 22.851 2.662   9.448   0.32 12.50 ?  53  LEU   A HD22 1 
ATOM   1299 H HD23 A LEU   A 1 53  ? 20.949 3.586   9.138   0.68 17.12 ?  53  LEU   A HD23 1 
ATOM   1300 H HD23 B LEU   A 1 53  ? 21.490 3.481   9.435   0.32 12.50 ?  53  LEU   A HD23 1 
ATOM   1301 N N    . ASN   A 1 54  ? 23.865 7.364   6.943   1.00 10.56 ?  54  ASN   A N    1 
ATOM   1302 C CA   . ASN   A 1 54  ? 24.911 8.368   7.070   1.00 10.27 ?  54  ASN   A CA   1 
ATOM   1303 C C    . ASN   A 1 54  ? 24.402 9.612   7.797   1.00 11.12 ?  54  ASN   A C    1 
ATOM   1304 O O    . ASN   A 1 54  ? 25.098 10.163  8.663   1.00 11.68 ?  54  ASN   A O    1 
ATOM   1305 C CB   . ASN   A 1 54  ? 25.469 8.733   5.710   1.00 10.59 ?  54  ASN   A CB   1 
ATOM   1306 C CG   . ASN   A 1 54  ? 26.484 9.836   5.820   1.00 11.04 ?  54  ASN   A CG   1 
ATOM   1307 O OD1  . ASN   A 1 54  ? 27.494 9.693   6.523   1.00 11.36 ?  54  ASN   A OD1  1 
ATOM   1308 N ND2  . ASN   A 1 54  ? 26.229 10.950  5.156   1.00 12.05 ?  54  ASN   A ND2  1 
ATOM   1309 H H    A ASN   A 1 54  ? 23.651 7.148   6.139   0.68 12.65 ?  54  ASN   A H    1 
ATOM   1310 H H    B ASN   A 1 54  ? 23.598 7.216   6.140   0.32 12.65 ?  54  ASN   A H    1 
ATOM   1311 H HA   . ASN   A 1 54  ? 25.631 7.998   7.597   1.00 12.31 ?  54  ASN   A HA   1 
ATOM   1312 H HB2  . ASN   A 1 54  ? 25.901 7.950   5.326   1.00 12.69 ?  54  ASN   A HB2  1 
ATOM   1313 H HB3  . ASN   A 1 54  ? 24.748 9.031   5.135   1.00 12.69 ?  54  ASN   A HB3  1 
ATOM   1314 H HD21 . ASN   A 1 54  ? 26.779 11.606  5.199   1.00 14.44 ?  54  ASN   A HD21 1 
ATOM   1315 H HD22 . ASN   A 1 54  ? 25.509 11.018  4.690   1.00 14.44 ?  54  ASN   A HD22 1 
ATOM   1316 N N    . LYS   A 1 55  ? 23.192 10.074  7.453   1.00 11.51 ?  55  LYS   A N    1 
ATOM   1317 C CA   . LYS   A 1 55  ? 22.615 11.230  8.126   1.00 12.56 ?  55  LYS   A CA   1 
ATOM   1318 C C    . LYS   A 1 55  ? 22.519 10.987  9.625   1.00 12.30 ?  55  LYS   A C    1 
ATOM   1319 O O    . LYS   A 1 55  ? 22.801 11.884  10.429  1.00 13.16 ?  55  LYS   A O    1 
ATOM   1320 C CB   . LYS   A 1 55  ? 21.243 11.538  7.517   1.00 13.72 ?  55  LYS   A CB   1 
ATOM   1321 C CG   . LYS   A 1 55  ? 20.505 12.715  8.128   1.00 15.83 ?  55  LYS   A CG   1 
ATOM   1322 C CD   . LYS   A 1 55  ? 19.173 12.950  7.405   1.00 17.68 ?  55  LYS   A CD   1 
ATOM   1323 C CE   . LYS   A 1 55  ? 18.352 14.065  8.033   1.00 19.52 ?  55  LYS   A CE   1 
ATOM   1324 N NZ   . LYS   A 1 55  ? 16.997 14.174  7.406   1.00 20.08 ?  55  LYS   A NZ   1 
ATOM   1325 H H    . LYS   A 1 55  ? 22.684 9.726   6.843   1.00 13.79 ?  55  LYS   A H    1 
ATOM   1326 H HA   . LYS   A 1 55  ? 23.187 11.997  7.977   1.00 15.05 ?  55  LYS   A HA   1 
ATOM   1327 H HB2  . LYS   A 1 55  ? 21.361 11.731  6.574   1.00 16.44 ?  55  LYS   A HB2  1 
ATOM   1328 H HB3  . LYS   A 1 55  ? 20.678 10.757  7.619   1.00 16.44 ?  55  LYS   A HB3  1 
ATOM   1329 H HG2  . LYS   A 1 55  ? 20.317 12.527  9.063   1.00 18.97 ?  55  LYS   A HG2  1 
ATOM   1330 H HG3  . LYS   A 1 55  ? 21.047 13.514  8.046   1.00 18.97 ?  55  LYS   A HG3  1 
ATOM   1331 H HD2  . LYS   A 1 55  ? 19.358 13.188  6.482   1.00 21.19 ?  55  LYS   A HD2  1 
ATOM   1332 H HD3  . LYS   A 1 55  ? 18.652 12.131  7.437   1.00 21.19 ?  55  LYS   A HD3  1 
ATOM   1333 H HE2  . LYS   A 1 55  ? 18.236 13.882  8.977   1.00 23.40 ?  55  LYS   A HE2  1 
ATOM   1334 H HE3  . LYS   A 1 55  ? 18.813 14.909  7.907   1.00 23.40 ?  55  LYS   A HE3  1 
ATOM   1335 H HZ1  . LYS   A 1 55  ? 16.447 14.621  7.947   1.00 24.07 ?  55  LYS   A HZ1  1 
ATOM   1336 H HZ2  . LYS   A 1 55  ? 17.050 14.609  6.631   1.00 24.07 ?  55  LYS   A HZ2  1 
ATOM   1337 H HZ3  . LYS   A 1 55  ? 16.658 13.364  7.261   1.00 24.07 ?  55  LYS   A HZ3  1 
ATOM   1338 N N    . ALA   A 1 56  ? 22.129 9.774   10.020  1.00 13.15 ?  56  ALA   A N    1 
ATOM   1339 C CA   . ALA   A 1 56  ? 22.008 9.439   11.430  1.00 13.51 ?  56  ALA   A CA   1 
ATOM   1340 C C    . ALA   A 1 56  ? 23.348 9.466   12.160  1.00 13.31 ?  56  ALA   A C    1 
ATOM   1341 O O    . ALA   A 1 56  ? 23.363 9.657   13.380  1.00 14.56 ?  56  ALA   A O    1 
ATOM   1342 C CB   . ALA   A 1 56  ? 21.315 8.081   11.591  1.00 14.40 ?  56  ALA   A CB   1 
ATOM   1343 H H    . ALA   A 1 56  ? 21.934 9.136   9.485   1.00 15.76 ?  56  ALA   A H    1 
ATOM   1344 H HA   . ALA   A 1 56  ? 21.444 10.098  11.851  1.00 16.18 ?  56  ALA   A HA   1 
ATOM   1345 H HB1  . ALA   A 1 56  ? 21.242 7.874   12.536  1.00 17.26 ?  56  ALA   A HB1  1 
ATOM   1346 H HB2  . ALA   A 1 56  ? 20.429 8.131   11.196  1.00 17.26 ?  56  ALA   A HB2  1 
ATOM   1347 H HB3  . ALA   A 1 56  ? 21.838 7.399   11.142  1.00 17.26 ?  56  ALA   A HB3  1 
ATOM   1348 N N    . THR   A 1 57  ? 24.468 9.283   11.450  1.00 12.09 ?  57  THR   A N    1 
ATOM   1349 C CA   . THR   A 1 57  ? 25.806 9.410   12.034  1.00 12.42 ?  57  THR   A CA   1 
ATOM   1350 C C    . THR   A 1 57  ? 26.357 10.829  11.962  1.00 12.86 ?  57  THR   A C    1 
ATOM   1351 O O    . THR   A 1 57  ? 27.543 11.039  12.258  1.00 13.34 ?  57  THR   A O    1 
ATOM   1352 C CB   . THR   A 1 57  ? 26.823 8.464   11.364  1.00 11.96 ?  57  THR   A CB   1 
ATOM   1353 O OG1  . THR   A 1 57  ? 27.198 8.959   10.067  1.00 12.05 ?  57  THR   A OG1  1 
ATOM   1354 C CG2  . THR   A 1 57  ? 26.292 7.044   11.255  1.00 12.09 ?  57  THR   A CG2  1 
ATOM   1355 H H    . THR   A 1 57  ? 24.478 9.062   10.615  1.00 14.48 ?  57  THR   A H    1 
ATOM   1356 H HA   . THR   A 1 57  ? 25.755 9.155   12.972  1.00 14.88 ?  57  THR   A HA   1 
ATOM   1357 H HB   . THR   A 1 57  ? 27.620 8.423   11.923  1.00 14.33 ?  57  THR   A HB   1 
ATOM   1358 H HG1  . THR   A 1 57  ? 26.515 9.017   9.582   1.00 14.44 ?  57  THR   A HG1  1 
ATOM   1359 H HG21 . THR   A 1 57  ? 26.933 6.477   10.792  1.00 14.49 ?  57  THR   A HG21 1 
ATOM   1360 H HG22 . THR   A 1 57  ? 26.131 6.671   12.138  1.00 14.49 ?  57  THR   A HG22 1 
ATOM   1361 H HG23 . THR   A 1 57  ? 25.458 7.032   10.760  1.00 14.49 ?  57  THR   A HG23 1 
ATOM   1362 N N    . ASN   A 1 58  ? 25.541 11.799  11.555  1.00 13.41 ?  58  ASN   A N    1 
ATOM   1363 C CA   . ASN   A 1 58  ? 25.995 13.183  11.455  1.00 14.14 ?  58  ASN   A CA   1 
ATOM   1364 C C    . ASN   A 1 58  ? 27.147 13.313  10.455  1.00 12.89 ?  58  ASN   A C    1 
ATOM   1365 O O    . ASN   A 1 58  ? 28.042 14.149  10.614  1.00 13.60 ?  58  ASN   A O    1 
ATOM   1366 C CB   . ASN   A 1 58  ? 26.352 13.735  12.846  1.00 16.56 ?  58  ASN   A CB   1 
ATOM   1367 C CG   . ASN   A 1 58  ? 26.726 15.198  12.830  1.00 20.82 ?  58  ASN   A CG   1 
ATOM   1368 O OD1  . ASN   A 1 58  ? 26.091 15.999  12.154  1.00 22.77 ?  58  ASN   A OD1  1 
ATOM   1369 N ND2  . ASN   A 1 58  ? 27.758 15.560  13.592  1.00 22.33 ?  58  ASN   A ND2  1 
ATOM   1370 H H    . ASN   A 1 58  ? 24.718 11.670  11.324  1.00 16.07 ?  58  ASN   A H    1 
ATOM   1371 H HA   . ASN   A 1 58  ? 25.255 13.704  11.116  1.00 16.94 ?  58  ASN   A HA   1 
ATOM   1372 H HB2  . ASN   A 1 58  ? 25.580 13.624  13.434  1.00 19.85 ?  58  ASN   A HB2  1 
ATOM   1373 H HB3  . ASN   A 1 58  ? 27.103 13.244  13.202  1.00 19.85 ?  58  ASN   A HB3  1 
ATOM   1374 H HD21 . ASN   A 1 58  ? 28.002 16.386  13.621  1.00 26.77 ?  58  ASN   A HD21 1 
ATOM   1375 H HD22 . ASN   A 1 58  ? 28.170 14.971  14.055  1.00 26.77 ?  58  ASN   A HD22 1 
ATOM   1376 N N    . ASN   A 1 59  ? 27.123 12.499  9.398   1.00 11.84 ?  59  ASN   A N    1 
ATOM   1377 C CA   . ASN   A 1 59  ? 28.103 12.482  8.305   1.00 11.66 ?  59  ASN   A CA   1 
ATOM   1378 C C    . ASN   A 1 59  ? 29.420 11.793  8.687   1.00 11.30 ?  59  ASN   A C    1 
ATOM   1379 O O    . ASN   A 1 59  ? 30.345 11.760  7.861   1.00 11.37 ?  59  ASN   A O    1 
ATOM   1380 C CB   . ASN   A 1 59  ? 28.384 13.870  7.696   1.00 11.53 ?  59  ASN   A CB   1 
ATOM   1381 C CG   . ASN   A 1 59  ? 28.744 13.800  6.227   1.00 12.04 ?  59  ASN   A CG   1 
ATOM   1382 O OD1  . ASN   A 1 59  ? 28.033 13.184  5.426   1.00 12.51 ?  59  ASN   A OD1  1 
ATOM   1383 N ND2  . ASN   A 1 59  ? 29.836 14.463  5.854   1.00 12.89 ?  59  ASN   A ND2  1 
ATOM   1384 H H    . ASN   A 1 59  ? 26.508 11.906  9.278   1.00 14.19 ?  59  ASN   A H    1 
ATOM   1385 H HA   . ASN   A 1 59  ? 27.727 11.954  7.588   1.00 13.97 ?  59  ASN   A HA   1 
ATOM   1386 H HB2  . ASN   A 1 59  ? 27.593 14.425  7.777   1.00 13.81 ?  59  ASN   A HB2  1 
ATOM   1387 H HB3  . ASN   A 1 59  ? 29.128 14.285  8.161   1.00 13.81 ?  59  ASN   A HB3  1 
ATOM   1388 H HD21 . ASN   A 1 59  ? 30.087 14.457  5.030   1.00 15.44 ?  59  ASN   A HD21 1 
ATOM   1389 H HD22 . ASN   A 1 59  ? 30.310 14.888  6.438   1.00 15.44 ?  59  ASN   A HD22 1 
ATOM   1390 N N    . ALA   A 1 60  ? 29.549 11.248  9.896   1.00 11.23 ?  60  ALA   A N    1 
ATOM   1391 C CA   . ALA   A 1 60  ? 30.787 10.562  10.251  1.00 11.40 ?  60  ALA   A CA   1 
ATOM   1392 C C    . ALA   A 1 60  ? 31.011 9.328   9.382   1.00 11.52 ?  60  ALA   A C    1 
ATOM   1393 O O    . ALA   A 1 60  ? 32.158 9.003   9.055   1.00 11.92 ?  60  ALA   A O    1 
ATOM   1394 C CB   . ALA   A 1 60  ? 30.780 10.194  11.731  1.00 11.92 ?  60  ALA   A CB   1 
ATOM   1395 H H    . ALA   A 1 60  ? 28.954 11.267  10.514  1.00 13.45 ?  60  ALA   A H    1 
ATOM   1396 H HA   . ALA   A 1 60  ? 31.534 11.170  10.101  1.00 13.65 ?  60  ALA   A HA   1 
ATOM   1397 H HB1  . ALA   A 1 60  ? 31.605 9.741   11.951  1.00 14.29 ?  60  ALA   A HB1  1 
ATOM   1398 H HB2  . ALA   A 1 60  ? 30.696 11.006  12.260  1.00 14.29 ?  60  ALA   A HB2  1 
ATOM   1399 H HB3  . ALA   A 1 60  ? 30.022 9.611   11.906  1.00 14.29 ?  60  ALA   A HB3  1 
ATOM   1400 N N    . MET   A 1 61  ? 29.938 8.634   8.998   1.00 10.89 ?  61  MET   A N    1 
ATOM   1401 C CA   . MET   A 1 61  ? 30.080 7.500   8.091   1.00 10.75 ?  61  MET   A CA   1 
ATOM   1402 C C    . MET   A 1 61  ? 30.708 7.930   6.767   1.00 10.73 ?  61  MET   A C    1 
ATOM   1403 O O    . MET   A 1 61  ? 31.598 7.249   6.243   1.00 11.26 ?  61  MET   A O    1 
ATOM   1404 C CB   . MET   A 1 61  ? 28.717 6.839   7.879   1.00 10.79 ?  61  MET   A CB   1 
ATOM   1405 C CG   . MET   A 1 61  ? 28.722 5.681   6.893   1.00 11.51 ?  61  MET   A CG   1 
ATOM   1406 S SD   . MET   A 1 61  ? 27.100 4.924   6.695   1.00 12.40 ?  61  MET   A SD   1 
ATOM   1407 C CE   . MET   A 1 61  ? 26.971 4.025   8.240   1.00 13.81 ?  61  MET   A CE   1 
ATOM   1408 H H    . MET   A 1 61  ? 29.128 8.801   9.242   1.00 13.04 ?  61  MET   A H    1 
ATOM   1409 H HA   . MET   A 1 61  ? 30.659 6.844   8.507   1.00 12.87 ?  61  MET   A HA   1 
ATOM   1410 H HB2  . MET   A 1 61  ? 28.402 6.497   8.729   1.00 12.92 ?  61  MET   A HB2  1 
ATOM   1411 H HB3  . MET   A 1 61  ? 28.096 7.504   7.544   1.00 12.92 ?  61  MET   A HB3  1 
ATOM   1412 H HG2  . MET   A 1 61  ? 29.000 5.998   6.021   1.00 13.79 ?  61  MET   A HG2  1 
ATOM   1413 H HG3  . MET   A 1 61  ? 29.328 4.993   7.208   1.00 13.79 ?  61  MET   A HG3  1 
ATOM   1414 H HE1  . MET   A 1 61  ? 26.131 3.539   8.256   1.00 16.55 ?  61  MET   A HE1  1 
ATOM   1415 H HE2  . MET   A 1 61  ? 27.714 3.403   8.304   1.00 16.55 ?  61  MET   A HE2  1 
ATOM   1416 H HE3  . MET   A 1 61  ? 27.002 4.653   8.980   1.00 16.55 ?  61  MET   A HE3  1 
ATOM   1417 N N    . GLN   A 1 62  ? 30.272 9.066   6.217   1.00 10.87 ?  62  GLN   A N    1 
ATOM   1418 C CA   . GLN   A 1 62  ? 30.828 9.531   4.951   1.00 11.05 ?  62  GLN   A CA   1 
ATOM   1419 C C    . GLN   A 1 62  ? 32.297 9.911   5.092   1.00 10.82 ?  62  GLN   A C    1 
ATOM   1420 O O    . GLN   A 1 62  ? 33.106 9.606   4.209   1.00 11.44 ?  62  GLN   A O    1 
ATOM   1421 C CB   . GLN   A 1 62  ? 30.022 10.714  4.415   1.00 11.26 ?  62  GLN   A CB   1 
ATOM   1422 C CG   . GLN   A 1 62  ? 30.396 11.083  2.996   1.00 11.23 ?  62  GLN   A CG   1 
ATOM   1423 C CD   . GLN   A 1 62  ? 30.064 9.958   2.042   1.00 11.37 ?  62  GLN   A CD   1 
ATOM   1424 O OE1  . GLN   A 1 62  ? 28.888 9.652   1.825   1.00 12.13 ?  62  GLN   A OE1  1 
ATOM   1425 N NE2  . GLN   A 1 62  ? 31.087 9.292   1.513   1.00 12.06 ?  62  GLN   A NE2  1 
ATOM   1426 H H    . GLN   A 1 62  ? 29.659 9.569   6.549   1.00 13.02 ?  62  GLN   A H    1 
ATOM   1427 H HA   . GLN   A 1 62  ? 30.770 8.812   4.303   1.00 13.24 ?  62  GLN   A HA   1 
ATOM   1428 H HB2  . GLN   A 1 62  ? 29.079 10.489  4.428   1.00 13.49 ?  62  GLN   A HB2  1 
ATOM   1429 H HB3  . GLN   A 1 62  ? 30.185 11.489  4.978   1.00 13.49 ?  62  GLN   A HB3  1 
ATOM   1430 H HG2  . GLN   A 1 62  ? 29.895 11.866  2.728   1.00 13.45 ?  62  GLN   A HG2  1 
ATOM   1431 H HG3  . GLN   A 1 62  ? 31.349 11.255  2.948   1.00 13.45 ?  62  GLN   A HG3  1 
ATOM   1432 H HE21 . GLN   A 1 62  ? 31.895 9.526   1.700   1.00 14.45 ?  62  GLN   A HE21 1 
ATOM   1433 H HE22 . GLN   A 1 62  ? 30.943 8.640   0.973   1.00 14.45 ?  62  GLN   A HE22 1 
ATOM   1434 N N    . VAL   A 1 63  ? 32.658 10.593  6.183   1.00 11.40 ?  63  VAL   A N    1 
ATOM   1435 C CA   . VAL   A 1 63  ? 34.051 10.981  6.404   1.00 12.27 ?  63  VAL   A CA   1 
ATOM   1436 C C    . VAL   A 1 63  ? 34.946 9.744   6.469   1.00 11.58 ?  63  VAL   A C    1 
ATOM   1437 O O    . VAL   A 1 63  ? 36.000 9.678   5.820   1.00 12.03 ?  63  VAL   A O    1 
ATOM   1438 C CB   . VAL   A 1 63  ? 34.161 11.855  7.667   1.00 14.23 ?  63  VAL   A CB   1 
ATOM   1439 C CG1  . VAL   A 1 63  ? 35.608 12.103  8.031   1.00 15.45 ?  63  VAL   A CG1  1 
ATOM   1440 C CG2  . VAL   A 1 63  ? 33.416 13.178  7.460   1.00 14.43 ?  63  VAL   A CG2  1 
ATOM   1441 H H    . VAL   A 1 63  ? 32.110 10.841  6.805   1.00 13.66 ?  63  VAL   A H    1 
ATOM   1442 H HA   . VAL   A 1 63  ? 34.339 11.516  5.652   1.00 14.70 ?  63  VAL   A HA   1 
ATOM   1443 H HB   . VAL   A 1 63  ? 33.741 11.394  8.410   1.00 17.05 ?  63  VAL   A HB   1 
ATOM   1444 H HG11 . VAL   A 1 63  ? 35.651 12.837  8.663   1.00 18.52 ?  63  VAL   A HG11 1 
ATOM   1445 H HG12 . VAL   A 1 63  ? 35.977 11.301  8.429   1.00 18.52 ?  63  VAL   A HG12 1 
ATOM   1446 H HG13 . VAL   A 1 63  ? 36.099 12.333  7.226   1.00 18.52 ?  63  VAL   A HG13 1 
ATOM   1447 H HG21 . VAL   A 1 63  ? 33.508 13.722  8.259   1.00 17.29 ?  63  VAL   A HG21 1 
ATOM   1448 H HG22 . VAL   A 1 63  ? 33.800 13.641  6.699   1.00 17.29 ?  63  VAL   A HG22 1 
ATOM   1449 H HG23 . VAL   A 1 63  ? 32.478 12.992  7.294   1.00 17.29 ?  63  VAL   A HG23 1 
ATOM   1450 N N    . GLU   A 1 64  ? 34.523 8.733   7.231   1.00 11.61 ?  64  GLU   A N    1 
ATOM   1451 C CA   . GLU   A 1 64  ? 35.292 7.496   7.322   1.00 11.05 ?  64  GLU   A CA   1 
ATOM   1452 C C    . GLU   A 1 64  ? 35.378 6.807   5.964   1.00 10.98 ?  64  GLU   A C    1 
ATOM   1453 O O    . GLU   A 1 64  ? 36.431 6.265   5.585   1.00 11.86 ?  64  GLU   A O    1 
ATOM   1454 C CB   . GLU   A 1 64  ? 34.602 6.586   8.338   1.00 12.13 ?  64  GLU   A CB   1 
ATOM   1455 C CG   . GLU   A 1 64  ? 35.263 5.242   8.489   1.00 13.13 ?  64  GLU   A CG   1 
ATOM   1456 C CD   . GLU   A 1 64  ? 34.387 4.242   9.210   1.00 13.60 ?  64  GLU   A CD   1 
ATOM   1457 O OE1  . GLU   A 1 64  ? 33.150 4.331   9.085   1.00 14.16 ?  64  GLU   A OE1  1 
ATOM   1458 O OE2  . GLU   A 1 64  ? 34.929 3.345   9.890   1.00 14.00 -1 64  GLU   A OE2  1 
ATOM   1459 H H    . GLU   A 1 64  ? 33.794 8.735   7.690   1.00 13.91 ?  64  GLU   A H    1 
ATOM   1460 H HA   . GLU   A 1 64  ? 36.191 7.700   7.637   1.00 13.23 ?  64  GLU   A HA   1 
ATOM   1461 H HB2  . GLU   A 1 64  ? 34.617 7.028   9.209   1.00 14.54 ?  64  GLU   A HB2  1 
ATOM   1462 H HB3  . GLU   A 1 64  ? 33.686 6.453   8.058   1.00 14.54 ?  64  GLU   A HB3  1 
ATOM   1463 H HG2  . GLU   A 1 64  ? 35.468 4.880   7.610   1.00 15.73 ?  64  GLU   A HG2  1 
ATOM   1464 H HG3  . GLU   A 1 64  ? 36.080 5.349   8.997   1.00 15.73 ?  64  GLU   A HG3  1 
ATOM   1465 N N    . SER   A 1 65  ? 34.259 6.798   5.233   1.00 10.95 ?  65  SER   A N    1 
ATOM   1466 C CA   . SER   A 1 65  ? 34.206 6.150   3.930   1.00 10.76 ?  65  SER   A CA   1 
ATOM   1467 C C    . SER   A 1 65  ? 35.129 6.823   2.923   1.00 11.02 ?  65  SER   A C    1 
ATOM   1468 O O    . SER   A 1 65  ? 35.762 6.145   2.106   1.00 11.76 ?  65  SER   A O    1 
ATOM   1469 C CB   . SER   A 1 65  ? 32.772 6.163   3.397   1.00 10.85 ?  65  SER   A CB   1 
ATOM   1470 O OG   . SER   A 1 65  ? 31.911 5.341   4.176   1.00 11.47 ?  65  SER   A OG   1 
ATOM   1471 H H    . SER   A 1 65  ? 33.523 7.168   5.476   1.00 13.12 ?  65  SER   A H    1 
ATOM   1472 H HA   . SER   A 1 65  ? 34.488 5.229   4.024   1.00 12.89 ?  65  SER   A HA   1 
ATOM   1473 H HB2  . SER   A 1 65  ? 32.436 7.073   3.416   1.00 12.99 ?  65  SER   A HB2  1 
ATOM   1474 H HB3  . SER   A 1 65  ? 32.777 5.834   2.484   1.00 12.99 ?  65  SER   A HB3  1 
ATOM   1475 H HG   . SER   A 1 65  ? 31.901 5.614   4.975   1.00 13.75 ?  65  SER   A HG   1 
ATOM   1476 N N    . ASP   A 1 66  ? 35.203 8.157   2.945   1.00 11.16 ?  66  ASP   A N    1 
ATOM   1477 C CA   . ASP   A 1 66  ? 36.058 8.854   1.992   1.00 12.15 ?  66  ASP   A CA   1 
ATOM   1478 C C    . ASP   A 1 66  ? 37.521 8.506   2.226   1.00 11.90 ?  66  ASP   A C    1 
ATOM   1479 O O    . ASP   A 1 66  ? 38.289 8.338   1.271   1.00 13.10 ?  66  ASP   A O    1 
ATOM   1480 C CB   . ASP   A 1 66  ? 35.842 10.361  2.091   1.00 13.72 ?  66  ASP   A CB   1 
ATOM   1481 C CG   . ASP   A 1 66  ? 34.502 10.825  1.491   1.00 15.63 ?  66  ASP   A CG   1 
ATOM   1482 O OD1  . ASP   A 1 66  ? 33.791 10.033  0.831   1.00 15.94 ?  66  ASP   A OD1  1 
ATOM   1483 O OD2  . ASP   A 1 66  ? 34.184 12.018  1.662   1.00 18.73 -1 66  ASP   A OD2  1 
ATOM   1484 H H    . ASP   A 1 66  ? 34.770 8.672   3.487   1.00 13.37 ?  66  ASP   A H    1 
ATOM   1485 H HA   . ASP   A 1 66  ? 35.822 8.576   1.093   1.00 14.56 ?  66  ASP   A HA   1 
ATOM   1486 H HB2  . ASP   A 1 66  ? 35.855 10.621  3.026   1.00 16.44 ?  66  ASP   A HB2  1 
ATOM   1487 H HB3  . ASP   A 1 66  ? 36.557 10.814  1.613   1.00 16.44 ?  66  ASP   A HB3  1 
ATOM   1488 N N    . ASP   A 1 67  ? 37.922 8.369   3.491   1.00 12.12 ?  67  ASP   A N    1 
ATOM   1489 C CA   . ASP   A 1 67  ? 39.278 7.924   3.789   1.00 13.07 ?  67  ASP   A CA   1 
ATOM   1490 C C    . ASP   A 1 67  ? 39.501 6.491   3.318   1.00 12.79 ?  67  ASP   A C    1 
ATOM   1491 O O    . ASP   A 1 67  ? 40.567 6.170   2.779   1.00 13.50 ?  67  ASP   A O    1 
ATOM   1492 C CB   . ASP   A 1 67  ? 39.546 8.054   5.286   1.00 14.63 ?  67  ASP   A CB   1 
ATOM   1493 C CG   . ASP   A 1 67  ? 40.843 7.395   5.704   1.00 15.62 ?  67  ASP   A CG   1 
ATOM   1494 O OD1  . ASP   A 1 67  ? 41.919 8.022   5.559   1.00 18.59 ?  67  ASP   A OD1  1 
ATOM   1495 O OD2  . ASP   A 1 67  ? 40.788 6.235   6.169   1.00 15.31 -1 67  ASP   A OD2  1 
ATOM   1496 H H    . ASP   A 1 67  ? 37.436 8.526   4.180   1.00 14.53 ?  67  ASP   A H    1 
ATOM   1497 H HA   . ASP   A 1 67  ? 39.907 8.491   3.316   1.00 15.66 ?  67  ASP   A HA   1 
ATOM   1498 H HB2  . ASP   A 1 67  ? 39.601 8.992   5.511   1.00 17.54 ?  67  ASP   A HB2  1 
ATOM   1499 H HB3  . ASP   A 1 67  ? 38.819 7.632   5.771   1.00 17.54 ?  67  ASP   A HB3  1 
ATOM   1500 N N    . TYR   A 1 68  ? 38.508 5.611   3.509   1.00 12.30 ?  68  TYR   A N    1 
ATOM   1501 C CA   . TYR   A 1 68  ? 38.627 4.231   3.032   1.00 12.70 ?  68  TYR   A CA   1 
ATOM   1502 C C    . TYR   A 1 68  ? 38.864 4.187   1.524   1.00 12.25 ?  68  TYR   A C    1 
ATOM   1503 O O    . TYR   A 1 68  ? 39.743 3.458   1.044   1.00 12.80 ?  68  TYR   A O    1 
ATOM   1504 C CB   . TYR   A 1 68  ? 37.383 3.403   3.411   1.00 13.31 ?  68  TYR   A CB   1 
ATOM   1505 C CG   . TYR   A 1 68  ? 37.417 2.018   2.783   1.00 14.74 ?  68  TYR   A CG   1 
ATOM   1506 C CD1  . TYR   A 1 68  ? 36.962 1.826   1.483   1.00 16.19 ?  68  TYR   A CD1  1 
ATOM   1507 C CD2  . TYR   A 1 68  ? 37.957 0.935   3.453   1.00 16.27 ?  68  TYR   A CD2  1 
ATOM   1508 C CE1  . TYR   A 1 68  ? 37.025 0.606   0.872   1.00 17.67 ?  68  TYR   A CE1  1 
ATOM   1509 C CE2  . TYR   A 1 68  ? 38.013 -0.327  2.844   1.00 17.07 ?  68  TYR   A CE2  1 
ATOM   1510 C CZ   . TYR   A 1 68  ? 37.562 -0.465  1.549   1.00 17.84 ?  68  TYR   A CZ   1 
ATOM   1511 O OH   . TYR   A 1 68  ? 37.636 -1.679  0.917   1.00 19.52 ?  68  TYR   A OH   1 
ATOM   1512 H H    . TYR   A 1 68  ? 37.763 5.785   3.908   1.00 14.74 ?  68  TYR   A H    1 
ATOM   1513 H HA   . TYR   A 1 68  ? 39.388 3.819   3.462   1.00 15.22 ?  68  TYR   A HA   1 
ATOM   1514 H HB2  . TYR   A 1 68  ? 37.349 3.294   4.374   1.00 15.95 ?  68  TYR   A HB2  1 
ATOM   1515 H HB3  . TYR   A 1 68  ? 36.583 3.858   3.098   1.00 15.95 ?  68  TYR   A HB3  1 
ATOM   1516 H HD1  . TYR   A 1 68  ? 36.610 2.553   1.015   1.00 19.40 ?  68  TYR   A HD1  1 
ATOM   1517 H HD2  . TYR   A 1 68  ? 38.281 1.041   4.315   1.00 19.51 ?  68  TYR   A HD2  1 
ATOM   1518 H HE1  . TYR   A 1 68  ? 36.710 0.505   0.003   1.00 21.18 ?  68  TYR   A HE1  1 
ATOM   1519 H HE2  . TYR   A 1 68  ? 38.385 -1.055  3.286   1.00 20.46 ?  68  TYR   A HE2  1 
ATOM   1520 H HH   . TYR   A 1 68  ? 37.965 -2.248  1.435   1.00 23.40 ?  68  TYR   A HH   1 
ATOM   1521 N N    . ILE   A 1 69  ? 38.081 4.951   0.756   1.00 11.85 ?  69  ILE   A N    1 
ATOM   1522 C CA   . ILE   A 1 69  ? 38.216 4.936   -0.699  1.00 12.18 ?  69  ILE   A CA   1 
ATOM   1523 C C    . ILE   A 1 69  ? 39.545 5.549   -1.132  1.00 12.07 ?  69  ILE   A C    1 
ATOM   1524 O O    . ILE   A 1 69  ? 40.184 5.075   -2.080  1.00 12.26 ?  69  ILE   A O    1 
ATOM   1525 C CB   . ILE   A 1 69  ? 37.016 5.642   -1.364  1.00 13.11 ?  69  ILE   A CB   1 
ATOM   1526 C CG1  . ILE   A 1 69  ? 35.705 4.909   -1.076  1.00 13.65 ?  69  ILE   A CG1  1 
ATOM   1527 C CG2  . ILE   A 1 69  ? 37.247 5.809   -2.866  1.00 14.75 ?  69  ILE   A CG2  1 
ATOM   1528 C CD1  . ILE   A 1 69  ? 35.543 3.617   -1.842  1.00 14.52 ?  69  ILE   A CD1  1 
ATOM   1529 H H    . ILE   A 1 69  ? 37.477 5.487   1.055   1.00 14.20 ?  69  ILE   A H    1 
ATOM   1530 H HA   . ILE   A 1 69  ? 38.215 4.014   -0.994  1.00 14.59 ?  69  ILE   A HA   1 
ATOM   1531 H HB   . ILE   A 1 69  ? 36.944 6.525   -0.978  1.00 15.71 ?  69  ILE   A HB   1 
ATOM   1532 H HG12 . ILE   A 1 69  ? 35.667 4.698   -0.127  1.00 16.36 ?  69  ILE   A HG12 1 
ATOM   1533 H HG13 . ILE   A 1 69  ? 34.965 5.490   -1.309  1.00 16.36 ?  69  ILE   A HG13 1 
ATOM   1534 H HG21 . ILE   A 1 69  ? 36.396 6.010   -3.296  1.00 17.67 ?  69  ILE   A HG21 1 
ATOM   1535 H HG22 . ILE   A 1 69  ? 37.863 6.547   -3.013  1.00 17.67 ?  69  ILE   A HG22 1 
ATOM   1536 H HG23 . ILE   A 1 69  ? 37.613 4.992   -3.229  1.00 17.67 ?  69  ILE   A HG23 1 
ATOM   1537 H HD11 . ILE   A 1 69  ? 34.757 3.153   -1.508  1.00 17.40 ?  69  ILE   A HD11 1 
ATOM   1538 H HD12 . ILE   A 1 69  ? 35.425 3.821   -2.784  1.00 17.40 ?  69  ILE   A HD12 1 
ATOM   1539 H HD13 . ILE   A 1 69  ? 36.328 3.068   -1.714  1.00 17.40 ?  69  ILE   A HD13 1 
ATOM   1540 N N    . ALA   A 1 70  ? 39.962 6.630   -0.473  1.00 12.58 ?  70  ALA   A N    1 
ATOM   1541 C CA   . ALA   A 1 70  ? 41.239 7.245   -0.823  1.00 13.32 ?  70  ALA   A CA   1 
ATOM   1542 C C    . ALA   A 1 70  ? 42.391 6.262   -0.653  1.00 13.48 ?  70  ALA   A C    1 
ATOM   1543 O O    . ALA   A 1 70  ? 43.360 6.302   -1.415  1.00 15.48 ?  70  ALA   A O    1 
ATOM   1544 C CB   . ALA   A 1 70  ? 41.477 8.499   0.019   1.00 14.15 ?  70  ALA   A CB   1 
ATOM   1545 H H    . ALA   A 1 70  ? 39.529 7.023   0.159   1.00 15.07 ?  70  ALA   A H    1 
ATOM   1546 H HA   . ALA   A 1 70  ? 41.209 7.521   -1.754  1.00 15.96 ?  70  ALA   A HA   1 
ATOM   1547 H HB1  . ALA   A 1 70  ? 42.337 8.885   -0.231  1.00 16.96 ?  70  ALA   A HB1  1 
ATOM   1548 H HB2  . ALA   A 1 70  ? 40.770 9.136   -0.145  1.00 16.96 ?  70  ALA   A HB2  1 
ATOM   1549 H HB3  . ALA   A 1 70  ? 41.495 8.250   0.957   1.00 16.96 ?  70  ALA   A HB3  1 
ATOM   1550 N N    . THR   A 1 71  ? 42.294 5.362   0.322   1.00 13.05 ?  71  THR   A N    1 
ATOM   1551 C CA   . THR   A 1 71  ? 43.351 4.387   0.568   1.00 14.15 ?  71  THR   A CA   1 
ATOM   1552 C C    . THR   A 1 71  ? 43.229 3.165   -0.332  1.00 14.43 ?  71  THR   A C    1 
ATOM   1553 O O    . THR   A 1 71  ? 44.240 2.663   -0.841  1.00 16.67 ?  71  THR   A O    1 
ATOM   1554 C CB   . THR   A 1 71  ? 43.296 3.942   2.027   1.00 16.49 ?  71  THR   A CB   1 
ATOM   1555 O OG1  . THR   A 1 71  ? 43.541 5.072   2.871   1.00 18.13 ?  71  THR   A OG1  1 
ATOM   1556 C CG2  . THR   A 1 71  ? 44.321 2.845   2.313   1.00 17.98 ?  71  THR   A CG2  1 
ATOM   1557 H H    . THR   A 1 71  ? 41.618 5.287   0.846   1.00 15.64 ?  71  THR   A H    1 
ATOM   1558 H HA   . THR   A 1 71  ? 44.211 4.799   0.403   1.00 16.96 ?  71  THR   A HA   1 
ATOM   1559 H HB   . THR   A 1 71  ? 42.413 3.579   2.212   1.00 19.77 ?  71  THR   A HB   1 
ATOM   1560 H HG1  . THR   A 1 71  ? 42.942 5.649   2.744   1.00 21.73 ?  71  THR   A HG1  1 
ATOM   1561 H HG21 . THR   A 1 71  ? 44.456 2.763   3.270   1.00 21.56 ?  71  THR   A HG21 1 
ATOM   1562 H HG22 . THR   A 1 71  ? 44.014 1.994   1.965   1.00 21.56 ?  71  THR   A HG22 1 
ATOM   1563 H HG23 . THR   A 1 71  ? 45.170 3.069   1.897   1.00 21.56 ?  71  THR   A HG23 1 
ATOM   1564 N N    . ASN   A 1 72  ? 42.009 2.658   -0.523  1.00 13.44 ?  72  ASN   A N    1 
ATOM   1565 C CA   . ASN   A 1 72  ? 41.796 1.333   -1.091  1.00 14.01 ?  72  ASN   A CA   1 
ATOM   1566 C C    . ASN   A 1 72  ? 41.177 1.326   -2.478  1.00 13.96 ?  72  ASN   A C    1 
ATOM   1567 O O    . ASN   A 1 72  ? 41.178 0.270   -3.126  1.00 15.12 ?  72  ASN   A O    1 
ATOM   1568 C CB   . ASN   A 1 72  ? 40.908 0.503   -0.155  1.00 14.60 ?  72  ASN   A CB   1 
ATOM   1569 C CG   . ASN   A 1 72  ? 41.518 0.351   1.212   1.00 15.99 ?  72  ASN   A CG   1 
ATOM   1570 O OD1  . ASN   A 1 72  ? 41.067 0.954   2.183   1.00 17.65 ?  72  ASN   A OD1  1 
ATOM   1571 N ND2  . ASN   A 1 72  ? 42.574 -0.427  1.289   1.00 16.20 ?  72  ASN   A ND2  1 
ATOM   1572 H H    . ASN   A 1 72  ? 41.277 3.076   -0.335  1.00 16.10 ?  72  ASN   A H    1 
ATOM   1573 H HA   . ASN   A 1 72  ? 42.650 0.887   -1.161  1.00 16.78 ?  72  ASN   A HA   1 
ATOM   1574 H HB2  . ASN   A 1 72  ? 40.049 0.939   -0.059  1.00 17.50 ?  72  ASN   A HB2  1 
ATOM   1575 H HB3  . ASN   A 1 72  ? 40.794 -0.384  -0.533  1.00 17.50 ?  72  ASN   A HB3  1 
ATOM   1576 H HD21 . ASN   A 1 72  ? 42.966 -0.542  2.047   1.00 19.41 ?  72  ASN   A HD21 1 
ATOM   1577 H HD22 . ASN   A 1 72  ? 42.871 -0.823  0.587   1.00 19.41 ?  72  ASN   A HD22 1 
ATOM   1578 N N    . GLY   A 1 73  ? 40.619 2.441   -2.933  1.00 13.55 ?  73  GLY   A N    1 
ATOM   1579 C CA   . GLY   A 1 73  ? 39.877 2.463   -4.169  1.00 13.12 ?  73  GLY   A CA   1 
ATOM   1580 C C    . GLY   A 1 73  ? 38.487 1.874   -4.001  1.00 12.61 ?  73  GLY   A C    1 
ATOM   1581 O O    . GLY   A 1 73  ? 38.102 1.413   -2.920  1.00 13.28 ?  73  GLY   A O    1 
ATOM   1582 H H    . GLY   A 1 73  ? 40.658 3.212   -2.540  1.00 16.23 ?  73  GLY   A H    1 
ATOM   1583 H HA2  . GLY   A 1 73  ? 39.793 3.382   -4.480  1.00 15.72 ?  73  GLY   A HA2  1 
ATOM   1584 H HA3  . GLY   A 1 73  ? 40.354 1.955   -4.843  1.00 15.72 ?  73  GLY   A HA3  1 
ATOM   1585 N N    . PRO   A 1 74  ? 37.708 1.888   -5.082  1.00 13.43 ?  74  PRO   A N    1 
ATOM   1586 C CA   . PRO   A 1 74  ? 36.312 1.454   -5.000  1.00 13.47 ?  74  PRO   A CA   1 
ATOM   1587 C C    . PRO   A 1 74  ? 36.171 -0.028  -4.688  1.00 12.55 ?  74  PRO   A C    1 
ATOM   1588 O O    . PRO   A 1 74  ? 37.041 -0.854  -4.984  1.00 13.44 ?  74  PRO   A O    1 
ATOM   1589 C CB   . PRO   A 1 74  ? 35.768 1.753   -6.402  1.00 15.53 ?  74  PRO   A CB   1 
ATOM   1590 C CG   . PRO   A 1 74  ? 36.700 2.763   -6.988  1.00 18.13 ?  74  PRO   A CG   1 
ATOM   1591 C CD   . PRO   A 1 74  ? 38.042 2.428   -6.411  1.00 15.41 ?  74  PRO   A CD   1 
ATOM   1592 H HA   . PRO   A 1 74  ? 35.829 1.978   -4.341  1.00 16.14 ?  74  PRO   A HA   1 
ATOM   1593 H HB2  . PRO   A 1 74  ? 35.765 0.940   -6.930  1.00 18.62 ?  74  PRO   A HB2  1 
ATOM   1594 H HB3  . PRO   A 1 74  ? 34.870 2.118   -6.331  1.00 18.62 ?  74  PRO   A HB3  1 
ATOM   1595 H HG2  . PRO   A 1 74  ? 36.713 2.679   -7.953  1.00 21.74 ?  74  PRO   A HG2  1 
ATOM   1596 H HG3  . PRO   A 1 74  ? 36.429 3.654   -6.723  1.00 21.74 ?  74  PRO   A HG3  1 
ATOM   1597 H HD2  . PRO   A 1 74  ? 38.490 1.755   -6.951  1.00 18.47 ?  74  PRO   A HD2  1 
ATOM   1598 H HD3  . PRO   A 1 74  ? 38.584 3.233   -6.336  1.00 18.47 ?  74  PRO   A HD3  1 
ATOM   1599 N N    . LEU   A 1 75  ? 35.028 -0.358  -4.098  1.00 11.77 ?  75  LEU   A N    1 
ATOM   1600 C CA   . LEU   A 1 75  ? 34.637 -1.748  -3.956  1.00 11.58 ?  75  LEU   A CA   1 
ATOM   1601 C C    . LEU   A 1 75  ? 34.249 -2.323  -5.316  1.00 11.91 ?  75  LEU   A C    1 
ATOM   1602 O O    . LEU   A 1 75  ? 34.114 -1.605  -6.311  1.00 13.50 ?  75  LEU   A O    1 
ATOM   1603 C CB   . LEU   A 1 75  ? 33.455 -1.877  -2.999  1.00 11.85 ?  75  LEU   A CB   1 
ATOM   1604 C CG   . LEU   A 1 75  ? 33.655 -1.455  -1.548  1.00 13.62 ?  75  LEU   A CG   1 
ATOM   1605 C CD1  . LEU   A 1 75  ? 32.377 -1.676  -0.748  1.00 15.68 ?  75  LEU   A CD1  1 
ATOM   1606 C CD2  . LEU   A 1 75  ? 34.820 -2.138  -0.885  1.00 16.93 ?  75  LEU   A CD2  1 
ATOM   1607 H H    . LEU   A 1 75  ? 34.464 0.208   -3.782  1.00 14.10 ?  75  LEU   A H    1 
ATOM   1608 H HA   . LEU   A 1 75  ? 35.381 -2.256  -3.613  1.00 13.87 ?  75  LEU   A HA   1 
ATOM   1609 H HB2  . LEU   A 1 75  ? 32.726 -1.348  -3.351  1.00 14.20 ?  75  LEU   A HB2  1 
ATOM   1610 H HB3  . LEU   A 1 75  ? 33.192 -2.812  -2.986  1.00 14.20 ?  75  LEU   A HB3  1 
ATOM   1611 H HG   . LEU   A 1 75  ? 33.842 -0.501  -1.537  1.00 16.32 ?  75  LEU   A HG   1 
ATOM   1612 H HD11 . LEU   A 1 75  ? 32.528 -1.396  0.168   1.00 18.79 ?  75  LEU   A HD11 1 
ATOM   1613 H HD12 . LEU   A 1 75  ? 31.666 -1.147  -1.143  1.00 18.79 ?  75  LEU   A HD12 1 
ATOM   1614 H HD13 . LEU   A 1 75  ? 32.149 -2.616  -0.776  1.00 18.79 ?  75  LEU   A HD13 1 
ATOM   1615 H HD21 . LEU   A 1 75  ? 34.871 -1.851  0.041   1.00 20.29 ?  75  LEU   A HD21 1 
ATOM   1616 H HD22 . LEU   A 1 75  ? 34.694 -3.096  -0.930  1.00 20.29 ?  75  LEU   A HD22 1 
ATOM   1617 H HD23 . LEU   A 1 75  ? 35.641 -1.891  -1.348  1.00 20.29 ?  75  LEU   A HD23 1 
ATOM   1618 N N    . LYS   A 1 76  ? 34.073 -3.643  -5.342  1.00 11.95 ?  76  LYS   A N    1 
ATOM   1619 C CA   . LYS   A 1 76  ? 33.468 -4.361  -6.456  1.00 12.70 ?  76  LYS   A CA   1 
ATOM   1620 C C    . LYS   A 1 76  ? 31.957 -4.440  -6.258  1.00 11.24 ?  76  LYS   A C    1 
ATOM   1621 O O    . LYS   A 1 76  ? 31.477 -4.562  -5.132  1.00 11.66 ?  76  LYS   A O    1 
ATOM   1622 C CB   . LYS   A 1 76  ? 34.013 -5.800  -6.504  1.00 14.47 ?  76  LYS   A CB   1 
ATOM   1623 C CG   . LYS   A 1 76  ? 35.523 -5.917  -6.701  1.00 15.74 ?  76  LYS   A CG   1 
ATOM   1624 C CD   . LYS   A 1 76  ? 36.033 -7.329  -6.508  1.00 17.14 ?  76  LYS   A CD   1 
ATOM   1625 C CE   . LYS   A 1 76  ? 37.532 -7.387  -6.702  1.00 19.68 ?  76  LYS   A CE   1 
ATOM   1626 N NZ   . LYS   A 1 76  ? 38.069 -8.738  -6.495  1.00 20.70 ?  76  LYS   A NZ   1 
ATOM   1627 H H    . LYS   A 1 76  ? 34.310 -4.162  -4.695  1.00 14.32 ?  76  LYS   A H    1 
ATOM   1628 H HA   . LYS   A 1 76  ? 33.665 -3.915  -7.295  1.00 15.22 ?  76  LYS   A HA   1 
ATOM   1629 H HB2  . LYS   A 1 76  ? 33.793 -6.239  -5.667  1.00 17.35 ?  76  LYS   A HB2  1 
ATOM   1630 H HB3  . LYS   A 1 76  ? 33.586 -6.266  -7.238  1.00 17.35 ?  76  LYS   A HB3  1 
ATOM   1631 H HG2  . LYS   A 1 76  ? 35.745 -5.635  -7.601  1.00 18.87 ?  76  LYS   A HG2  1 
ATOM   1632 H HG3  . LYS   A 1 76  ? 35.970 -5.346  -6.055  1.00 18.87 ?  76  LYS   A HG3  1 
ATOM   1633 H HD2  . LYS   A 1 76  ? 35.825 -7.627  -5.609  1.00 20.54 ?  76  LYS   A HD2  1 
ATOM   1634 H HD3  . LYS   A 1 76  ? 35.616 -7.913  -7.163  1.00 20.54 ?  76  LYS   A HD3  1 
ATOM   1635 H HE2  . LYS   A 1 76  ? 37.745 -7.110  -7.606  1.00 23.60 ?  76  LYS   A HE2  1 
ATOM   1636 H HE3  . LYS   A 1 76  ? 37.955 -6.794  -6.061  1.00 23.60 ?  76  LYS   A HE3  1 
ATOM   1637 H HZ1  . LYS   A 1 76  ? 38.949 -8.745  -6.616  1.00 24.81 ?  76  LYS   A HZ1  1 
ATOM   1638 H HZ2  . LYS   A 1 76  ? 37.888 -9.021  -5.669  1.00 24.81 ?  76  LYS   A HZ2  1 
ATOM   1639 H HZ3  . LYS   A 1 76  ? 37.696 -9.309  -7.076  1.00 24.81 ?  76  LYS   A HZ3  1 
ATOM   1640 N N    . VAL   A 1 77  ? 31.203 -4.406  -7.363  1.00 12.09 ?  77  VAL   A N    1 
ATOM   1641 C CA   . VAL   A 1 77  ? 29.795 -4.787  -7.270  1.00 11.79 ?  77  VAL   A CA   1 
ATOM   1642 C C    . VAL   A 1 77  ? 29.726 -6.243  -6.835  1.00 11.88 ?  77  VAL   A C    1 
ATOM   1643 O O    . VAL   A 1 77  ? 30.384 -7.111  -7.421  1.00 12.18 ?  77  VAL   A O    1 
ATOM   1644 C CB   . VAL   A 1 77  ? 29.065 -4.562  -8.603  1.00 13.12 ?  77  VAL   A CB   1 
ATOM   1645 C CG1  . VAL   A 1 77  ? 27.604 -4.996  -8.490  1.00 14.25 ?  77  VAL   A CG1  1 
ATOM   1646 C CG2  . VAL   A 1 77  ? 29.149 -3.103  -9.027  1.00 14.64 ?  77  VAL   A CG2  1 
ATOM   1647 H H    . VAL   A 1 77  ? 31.478 -4.177  -8.145  1.00 14.48 ?  77  VAL   A H    1 
ATOM   1648 H HA   . VAL   A 1 77  ? 29.367 -4.244  -6.591  1.00 14.13 ?  77  VAL   A HA   1 
ATOM   1649 H HB   . VAL   A 1 77  ? 29.490 -5.097  -9.292  1.00 15.73 ?  77  VAL   A HB   1 
ATOM   1650 H HG11 . VAL   A 1 77  ? 27.124 -4.682  -9.268  1.00 17.08 ?  77  VAL   A HG11 1 
ATOM   1651 H HG12 . VAL   A 1 77  ? 27.567 -5.964  -8.443  1.00 17.08 ?  77  VAL   A HG12 1 
ATOM   1652 H HG13 . VAL   A 1 77  ? 27.226 -4.609  -7.685  1.00 17.08 ?  77  VAL   A HG13 1 
ATOM   1653 H HG21 . VAL   A 1 77  ? 28.644 -2.984  -9.848  1.00 17.54 ?  77  VAL   A HG21 1 
ATOM   1654 H HG22 . VAL   A 1 77  ? 28.771 -2.548  -8.325  1.00 17.54 ?  77  VAL   A HG22 1 
ATOM   1655 H HG23 . VAL   A 1 77  ? 30.077 -2.865  -9.172  1.00 17.54 ?  77  VAL   A HG23 1 
ATOM   1656 N N    . GLY   A 1 78  ? 28.943 -6.518  -5.792  1.00 11.39 ?  78  GLY   A N    1 
ATOM   1657 C CA   . GLY   A 1 78  ? 28.924 -7.808  -5.141  1.00 11.81 ?  78  GLY   A CA   1 
ATOM   1658 C C    . GLY   A 1 78  ? 29.845 -7.904  -3.945  1.00 11.13 ?  78  GLY   A C    1 
ATOM   1659 O O    . GLY   A 1 78  ? 29.784 -8.903  -3.215  1.00 11.97 ?  78  GLY   A O    1 
ATOM   1660 H H    . GLY   A 1 78  ? 28.394 -5.949  -5.448  1.00 13.64 ?  78  GLY   A H    1 
ATOM   1661 H HA2  . GLY   A 1 78  ? 28.022 -8.000  -4.846  1.00 14.15 ?  78  GLY   A HA2  1 
ATOM   1662 H HA3  . GLY   A 1 78  ? 29.184 -8.489  -5.782  1.00 14.15 ?  78  GLY   A HA3  1 
ATOM   1663 N N    . GLY   A 1 79  ? 30.699 -6.900  -3.724  1.00 11.03 ?  79  GLY   A N    1 
ATOM   1664 C CA   . GLY   A 1 79  ? 31.659 -6.915  -2.645  1.00 11.20 ?  79  GLY   A CA   1 
ATOM   1665 C C    . GLY   A 1 79  ? 31.205 -6.120  -1.432  1.00 10.70 ?  79  GLY   A C    1 
ATOM   1666 O O    . GLY   A 1 79  ? 30.083 -5.618  -1.353  1.00 11.66 ?  79  GLY   A O    1 
ATOM   1667 H H    . GLY   A 1 79  ? 30.740 -6.184  -4.206  1.00 13.22 ?  79  GLY   A H    1 
ATOM   1668 H HA2  . GLY   A 1 79  ? 31.816 -7.838  -2.376  1.00 13.42 ?  79  GLY   A HA2  1 
ATOM   1669 H HA3  . GLY   A 1 79  ? 32.500 -6.548  -2.959  1.00 13.42 ?  79  GLY   A HA3  1 
ATOM   1670 N N    . SER   A 1 80  ? 32.109 -6.025  -0.461  1.00 11.41 ?  80  SER   A N    1 
ATOM   1671 C CA   . SER   A 1 80  ? 31.790 -5.396  0.809   1.00 10.76 ?  80  SER   A CA   1 
ATOM   1672 C C    . SER   A 1 80  ? 33.060 -4.950  1.511   1.00 10.79 ?  80  SER   A C    1 
ATOM   1673 O O    . SER   A 1 80  ? 34.176 -5.379  1.180   1.00 12.35 ?  80  SER   A O    1 
ATOM   1674 C CB   . SER   A 1 80  ? 31.029 -6.366  1.727   1.00 12.06 ?  80  SER   A CB   1 
ATOM   1675 O OG   . SER   A 1 80  ? 31.866 -7.418  2.194   1.00 13.71 ?  80  SER   A OG   1 
ATOM   1676 H H    . SER   A 1 80  ? 32.923 -6.307  -0.518  1.00 13.67 ?  80  SER   A H    1 
ATOM   1677 H HA   . SER   A 1 80  ? 31.235 -4.619  0.637   1.00 12.89 ?  80  SER   A HA   1 
ATOM   1678 H HB2  . SER   A 1 80  ? 30.691 -5.871  2.489   1.00 14.45 ?  80  SER   A HB2  1 
ATOM   1679 H HB3  . SER   A 1 80  ? 30.288 -6.746  1.228   1.00 14.45 ?  80  SER   A HB3  1 
ATOM   1680 H HG   . SER   A 1 80  ? 32.159 -7.854  1.537   1.00 16.43 ?  80  SER   A HG   1 
ATOM   1681 N N    . CYS   A 1 81  ? 32.867 -4.104  2.521   1.00 10.57 ?  81  CYS   A N    1 
ATOM   1682 C CA   . CYS   A 1 81  ? 33.918 -3.820  3.484   1.00 10.76 ?  81  CYS   A CA   1 
ATOM   1683 C C    . CYS   A 1 81  ? 33.286 -3.586  4.846   1.00 10.66 ?  81  CYS   A C    1 
ATOM   1684 O O    . CYS   A 1 81  ? 32.120 -3.186  4.942   1.00 11.98 ?  81  CYS   A O    1 
ATOM   1685 C CB   . CYS   A 1 81  ? 34.794 -2.633  3.066   1.00 11.87 ?  81  CYS   A CB   1 
ATOM   1686 S SG   . CYS   A 1 81  ? 33.902 -1.055  3.094   1.00 11.88 ?  81  CYS   A SG   1 
ATOM   1687 H H    . CYS   A 1 81  ? 32.129 -3.675  2.672   1.00 12.67 ?  81  CYS   A H    1 
ATOM   1688 H HA   . CYS   A 1 81  ? 34.493 -4.598  3.551   1.00 12.89 ?  81  CYS   A HA   1 
ATOM   1689 H HB2  . CYS   A 1 81  ? 35.551 -2.565  3.679   1.00 14.22 ?  81  CYS   A HB2  1 
ATOM   1690 H HB3  . CYS   A 1 81  ? 35.126 -2.783  2.162   1.00 14.22 ?  81  CYS   A HB3  1 
ATOM   1691 H HG   . CYS   A 1 81  ? 34.648 -0.175  2.756   1.00 14.23 ?  81  CYS   A HG   1 
ATOM   1692 N N    . VAL   A 1 82  ? 34.053 -3.856  5.897   1.00 11.10 ?  82  VAL   A N    1 
ATOM   1693 C CA   . VAL   A 1 82  ? 33.633 -3.618  7.269   1.00 11.58 ?  82  VAL   A CA   1 
ATOM   1694 C C    . VAL   A 1 82  ? 34.235 -2.305  7.743   1.00 12.03 ?  82  VAL   A C    1 
ATOM   1695 O O    . VAL   A 1 82  ? 35.461 -2.134  7.731   1.00 12.62 ?  82  VAL   A O    1 
ATOM   1696 C CB   . VAL   A 1 82  ? 34.057 -4.765  8.197   1.00 13.29 ?  82  VAL   A CB   1 
ATOM   1697 C CG1  . VAL   A 1 82  ? 33.606 -4.481  9.618   1.00 14.70 ?  82  VAL   A CG1  1 
ATOM   1698 C CG2  . VAL   A 1 82  ? 33.497 -6.095  7.707   1.00 14.44 ?  82  VAL   A CG2  1 
ATOM   1699 H H    . VAL   A 1 82  ? 34.845 -4.204  5.838   1.00 13.30 ?  82  VAL   A H    1 
ATOM   1700 H HA   . VAL   A 1 82  ? 32.665 -3.541  7.297   1.00 13.87 ?  82  VAL   A HA   1 
ATOM   1701 H HB   . VAL   A 1 82  ? 35.021 -4.827  8.200   1.00 15.93 ?  82  VAL   A HB   1 
ATOM   1702 H HG11 . VAL   A 1 82  ? 33.690 -5.291  10.145  1.00 17.62 ?  82  VAL   A HG11 1 
ATOM   1703 H HG12 . VAL   A 1 82  ? 34.158 -3.781  9.998   1.00 17.62 ?  82  VAL   A HG12 1 
ATOM   1704 H HG13 . VAL   A 1 82  ? 32.675 -4.196  9.606   1.00 17.62 ?  82  VAL   A HG13 1 
ATOM   1705 H HG21 . VAL   A 1 82  ? 33.736 -6.790  8.339   1.00 17.30 ?  82  VAL   A HG21 1 
ATOM   1706 H HG22 . VAL   A 1 82  ? 32.530 -6.027  7.642   1.00 17.30 ?  82  VAL   A HG22 1 
ATOM   1707 H HG23 . VAL   A 1 82  ? 33.873 -6.294  6.836   1.00 17.30 ?  82  VAL   A HG23 1 
ATOM   1708 N N    . LEU   A 1 83  ? 33.375 -1.381  8.163   1.00 11.42 ?  83  LEU   A N    1 
ATOM   1709 C CA   . LEU   A 1 83  ? 33.795 -0.117  8.744   1.00 11.27 ?  83  LEU   A CA   1 
ATOM   1710 C C    . LEU   A 1 83  ? 33.077 0.058   10.078  1.00 11.56 ?  83  LEU   A C    1 
ATOM   1711 O O    . LEU   A 1 83  ? 32.352 -0.832  10.541  1.00 12.46 ?  83  LEU   A O    1 
ATOM   1712 C CB   . LEU   A 1 83  ? 33.546 1.041   7.766   1.00 12.05 ?  83  LEU   A CB   1 
ATOM   1713 C CG   . LEU   A 1 83  ? 34.443 1.046   6.522   1.00 12.83 ?  83  LEU   A CG   1 
ATOM   1714 C CD1  . LEU   A 1 83  ? 33.998 2.091   5.517   1.00 13.21 ?  83  LEU   A CD1  1 
ATOM   1715 C CD2  . LEU   A 1 83  ? 35.912 1.269   6.895   1.00 13.96 ?  83  LEU   A CD2  1 
ATOM   1716 H H    . LEU   A 1 83  ? 32.517 -1.467  8.116   1.00 13.68 ?  83  LEU   A H    1 
ATOM   1717 H HA   . LEU   A 1 83  ? 34.746 -0.150  8.918   1.00 13.50 ?  83  LEU   A HA   1 
ATOM   1718 H HB2  . LEU   A 1 83  ? 32.626 1.000   7.454   1.00 14.44 ?  83  LEU   A HB2  1 
ATOM   1719 H HB3  . LEU   A 1 83  ? 33.689 1.883   8.228   1.00 14.44 ?  83  LEU   A HB3  1 
ATOM   1720 H HG   . LEU   A 1 83  ? 34.380 0.182   6.092   1.00 15.37 ?  83  LEU   A HG   1 
ATOM   1721 H HD11 . LEU   A 1 83  ? 34.588 2.055   4.745   1.00 15.83 ?  83  LEU   A HD11 1 
ATOM   1722 H HD12 . LEU   A 1 83  ? 33.089 1.897   5.246   1.00 15.83 ?  83  LEU   A HD12 1 
ATOM   1723 H HD13 . LEU   A 1 83  ? 34.045 2.966   5.929   1.00 15.83 ?  83  LEU   A HD13 1 
ATOM   1724 H HD21 . LEU   A 1 83  ? 36.427 1.410   6.083   1.00 16.73 ?  83  LEU   A HD21 1 
ATOM   1725 H HD22 . LEU   A 1 83  ? 35.979 2.052   7.465   1.00 16.73 ?  83  LEU   A HD22 1 
ATOM   1726 H HD23 . LEU   A 1 83  ? 36.243 0.489   7.364   1.00 16.73 ?  83  LEU   A HD23 1 
ATOM   1727 N N    . SER   A 1 84  ? 33.291 1.208   10.711  1.00 12.18 ?  84  SER   A N    1 
ATOM   1728 C CA   . SER   A 1 84  ? 32.646 1.465   11.988  1.00 12.45 ?  84  SER   A CA   1 
ATOM   1729 C C    . SER   A 1 84  ? 31.129 1.549   11.842  1.00 11.95 ?  84  SER   A C    1 
ATOM   1730 O O    . SER   A 1 84  ? 30.603 2.017   10.832  1.00 12.34 ?  84  SER   A O    1 
ATOM   1731 C CB   . SER   A 1 84  ? 33.146 2.784   12.567  1.00 13.48 ?  84  SER   A CB   1 
ATOM   1732 O OG   . SER   A 1 84  ? 32.509 3.061   13.798  1.00 14.23 ?  84  SER   A OG   1 
ATOM   1733 H H    . SER   A 1 84  ? 33.795 1.848   10.420  1.00 14.59 ?  84  SER   A H    1 
ATOM   1734 H HA   . SER   A 1 84  ? 32.862 0.749   12.600  1.00 14.92 ?  84  SER   A HA   1 
ATOM   1735 H HB2  . SER   A 1 84  ? 34.105 2.722   12.702  1.00 16.16 ?  84  SER   A HB2  1 
ATOM   1736 H HB3  . SER   A 1 84  ? 32.947 3.498   11.939  1.00 16.16 ?  84  SER   A HB3  1 
ATOM   1737 H HG   . SER   A 1 84  ? 32.799 3.785   14.111  1.00 17.05 ?  84  SER   A HG   1 
ATOM   1738 N N    . GLY   A 1 85  ? 30.426 1.140   12.896  1.00 12.82 ?  85  GLY   A N    1 
ATOM   1739 C CA   . GLY   A 1 85  ? 29.002 1.373   12.989  1.00 13.67 ?  85  GLY   A CA   1 
ATOM   1740 C C    . GLY   A 1 85  ? 28.630 2.686   13.641  1.00 13.64 ?  85  GLY   A C    1 
ATOM   1741 O O    . GLY   A 1 85  ? 27.440 3.002   13.754  1.00 14.23 ?  85  GLY   A O    1 
ATOM   1742 H H    . GLY   A 1 85  ? 30.763 0.716   13.568  1.00 15.36 ?  85  GLY   A H    1 
ATOM   1743 H HA2  . GLY   A 1 85  ? 28.623 1.352   12.094  1.00 16.38 ?  85  GLY   A HA2  1 
ATOM   1744 H HA3  . GLY   A 1 85  ? 28.598 0.658   13.500  1.00 16.38 ?  85  GLY   A HA3  1 
ATOM   1745 N N    . HIS   A 1 86  ? 29.618 3.456   14.086  1.00 13.33 ?  86  HIS   A N    1 
ATOM   1746 C CA   . HIS   A 1 86  ? 29.398 4.793   14.650  1.00 14.01 ?  86  HIS   A CA   1 
ATOM   1747 C C    . HIS   A 1 86  ? 28.420 4.665   15.811  1.00 15.06 ?  86  HIS   A C    1 
ATOM   1748 O O    . HIS   A 1 86  ? 28.609 3.779   16.660  1.00 15.90 ?  86  HIS   A O    1 
ATOM   1749 C CB   . HIS   A 1 86  ? 29.022 5.779   13.553  1.00 13.73 ?  86  HIS   A CB   1 
ATOM   1750 C CG   . HIS   A 1 86  ? 30.073 5.877   12.505  1.00 13.77 ?  86  HIS   A CG   1 
ATOM   1751 N ND1  . HIS   A 1 86  ? 31.170 6.704   12.632  1.00 14.76 ?  86  HIS   A ND1  1 
ATOM   1752 C CD2  . HIS   A 1 86  ? 30.247 5.188   11.356  1.00 13.58 ?  86  HIS   A CD2  1 
ATOM   1753 C CE1  . HIS   A 1 86  ? 31.949 6.549   11.578  1.00 14.59 ?  86  HIS   A CE1  1 
ATOM   1754 N NE2  . HIS   A 1 86  ? 31.422 5.624   10.798  1.00 14.30 ?  86  HIS   A NE2  1 
ATOM   1755 H H    . HIS   A 1 86  ? 30.441 3.228   14.074  1.00 15.97 ?  86  HIS   A H    1 
ATOM   1756 H HA   . HIS   A 1 86  ? 30.237 5.102   15.017  1.00 16.78 ?  86  HIS   A HA   1 
ATOM   1757 H HB2  . HIS   A 1 86  ? 28.195 5.498   13.127  1.00 16.45 ?  86  HIS   A HB2  1 
ATOM   1758 H HB3  . HIS   A 1 86  ? 28.904 6.667   13.939  1.00 16.45 ?  86  HIS   A HB3  1 
ATOM   1759 H HD2  . HIS   A 1 86  ? 29.678 4.533   11.007  1.00 16.27 ?  86  HIS   A HD2  1 
ATOM   1760 H HE1  . HIS   A 1 86  ? 32.741 7.005   11.408  1.00 17.49 ?  86  HIS   A HE1  1 
ATOM   1761 H HE2  . HIS   A 1 86  ? 31.750 5.348   10.043  1.00 17.13 ?  86  HIS   A HE2  1 
ATOM   1762 N N    . ASN   A 1 87  ? 27.404 5.514   15.892  1.00 16.10 ?  87  ASN   A N    1 
ATOM   1763 C CA   . ASN   A 1 87  ? 26.425 5.497   16.964  1.00 17.11 ?  87  ASN   A CA   1 
ATOM   1764 C C    . ASN   A 1 87  ? 25.312 4.486   16.733  1.00 18.48 ?  87  ASN   A C    1 
ATOM   1765 O O    . ASN   A 1 87  ? 24.412 4.392   17.570  1.00 20.64 ?  87  ASN   A O    1 
ATOM   1766 C CB   . ASN   A 1 87  ? 25.816 6.899   17.130  1.00 18.38 ?  87  ASN   A CB   1 
ATOM   1767 C CG   . ASN   A 1 87  ? 25.314 7.484   15.815  1.00 19.07 ?  87  ASN   A CG   1 
ATOM   1768 O OD1  . ASN   A 1 87  ? 25.970 7.381   14.780  1.00 19.54 ?  87  ASN   A OD1  1 
ATOM   1769 N ND2  . ASN   A 1 87  ? 24.149 8.110   15.856  1.00 19.77 ?  87  ASN   A ND2  1 
ATOM   1770 H H    . ASN   A 1 87  ? 27.258 6.131   15.315  1.00 19.30 ?  87  ASN   A H    1 
ATOM   1771 H HA   . ASN   A 1 87  ? 26.864 5.262   17.799  1.00 20.50 ?  87  ASN   A HA   1 
ATOM   1772 H HB2  . ASN   A 1 87  ? 25.064 6.846   17.747  1.00 22.03 ?  87  ASN   A HB2  1 
ATOM   1773 H HB3  . ASN   A 1 87  ? 26.491 7.495   17.486  1.00 22.03 ?  87  ASN   A HB3  1 
ATOM   1774 H HD21 . ASN   A 1 87  ? 23.823 8.454   15.141  1.00 23.70 ?  87  ASN   A HD21 1 
ATOM   1775 H HD22 . ASN   A 1 87  ? 23.719 8.173   16.600  1.00 23.70 ?  87  ASN   A HD22 1 
ATOM   1776 N N    . LEU   A 1 88  ? 25.354 3.725   15.644  1.00 17.42 ?  88  LEU   A N    1 
ATOM   1777 C CA   . LEU   A 1 88  ? 24.239 2.869   15.252  1.00 16.86 ?  88  LEU   A CA   1 
ATOM   1778 C C    . LEU   A 1 88  ? 24.458 1.389   15.540  1.00 16.47 ?  88  LEU   A C    1 
ATOM   1779 O O    . LEU   A 1 88  ? 23.483 0.656   15.729  1.00 17.73 ?  88  LEU   A O    1 
ATOM   1780 C CB   . LEU   A 1 88  ? 23.969 3.046   13.755  1.00 17.51 ?  88  LEU   A CB   1 
ATOM   1781 C CG   . LEU   A 1 88  ? 23.664 4.470   13.283  1.00 19.09 ?  88  LEU   A CG   1 
ATOM   1782 C CD1  . LEU   A 1 88  ? 23.510 4.490   11.777  1.00 19.54 ?  88  LEU   A CD1  1 
ATOM   1783 C CD2  . LEU   A 1 88  ? 22.419 5.033   13.961  1.00 20.57 ?  88  LEU   A CD2  1 
ATOM   1784 H H    . LEU   A 1 88  ? 26.028 3.690   15.112  1.00 20.88 ?  88  LEU   A H    1 
ATOM   1785 H HA   . LEU   A 1 88  ? 23.447 3.153   15.733  1.00 20.20 ?  88  LEU   A HA   1 
ATOM   1786 H HB2  . LEU   A 1 88  ? 24.744 2.745   13.262  1.00 20.99 ?  88  LEU   A HB2  1 
ATOM   1787 H HB3  . LEU   A 1 88  ? 23.202 2.500   13.518  1.00 20.99 ?  88  LEU   A HB3  1 
ATOM   1788 H HG   . LEU   A 1 88  ? 24.409 5.045   13.510  1.00 22.88 ?  88  LEU   A HG   1 
ATOM   1789 H HD11 . LEU   A 1 88  ? 23.319 5.398   11.491  1.00 23.43 ?  88  LEU   A HD11 1 
ATOM   1790 H HD12 . LEU   A 1 88  ? 24.337 4.184   11.373  1.00 23.43 ?  88  LEU   A HD12 1 
ATOM   1791 H HD13 . LEU   A 1 88  ? 22.780 3.903   11.526  1.00 23.43 ?  88  LEU   A HD13 1 
ATOM   1792 H HD21 . LEU   A 1 88  ? 22.214 5.899   13.574  1.00 24.66 ?  88  LEU   A HD21 1 
ATOM   1793 H HD22 . LEU   A 1 88  ? 21.681 4.422   13.819  1.00 24.66 ?  88  LEU   A HD22 1 
ATOM   1794 H HD23 . LEU   A 1 88  ? 22.596 5.127   14.909  1.00 24.66 ?  88  LEU   A HD23 1 
ATOM   1795 N N    . ALA   A 1 89  ? 25.707 0.939   15.567  1.00 15.43 ?  89  ALA   A N    1 
ATOM   1796 C CA   . ALA   A 1 89  ? 26.052 -0.472  15.665  1.00 14.95 ?  89  ALA   A CA   1 
ATOM   1797 C C    . ALA   A 1 89  ? 27.537 -0.532  15.985  1.00 15.28 ?  89  ALA   A C    1 
ATOM   1798 O O    . ALA   A 1 89  ? 28.246 0.470   15.887  1.00 16.22 ?  89  ALA   A O    1 
ATOM   1799 C CB   . ALA   A 1 89  ? 25.779 -1.186  14.342  1.00 14.08 ?  89  ALA   A CB   1 
ATOM   1800 H H    . ALA   A 1 89  ? 26.393 1.454   15.518  1.00 18.50 ?  89  ALA   A H    1 
ATOM   1801 H HA   . ALA   A 1 89  ? 25.540 -0.894  16.377  1.00 17.91 ?  89  ALA   A HA   1 
ATOM   1802 H HB1  . ALA   A 1 89  ? 26.030 -2.120  14.430  1.00 16.87 ?  89  ALA   A HB1  1 
ATOM   1803 H HB2  . ALA   A 1 89  ? 24.834 -1.119  14.128  1.00 16.87 ?  89  ALA   A HB2  1 
ATOM   1804 H HB3  . ALA   A 1 89  ? 26.306 -0.769  13.643  1.00 16.87 ?  89  ALA   A HB3  1 
ATOM   1805 N N    . LYS   A 1 90  ? 28.019 -1.717  16.354  1.00 16.13 ?  90  LYS   A N    1 
ATOM   1806 C CA   . LYS   A 1 90  ? 29.462 -1.864  16.500  1.00 16.12 ?  90  LYS   A CA   1 
ATOM   1807 C C    . LYS   A 1 90  ? 30.158 -1.674  15.155  1.00 14.97 ?  90  LYS   A C    1 
ATOM   1808 O O    . LYS   A 1 90  ? 31.101 -0.872  15.031  1.00 17.01 ?  90  LYS   A O    1 
ATOM   1809 C CB   . LYS   A 1 90  ? 29.803 -3.220  17.117  1.00 19.25 ?  90  LYS   A CB   1 
ATOM   1810 C CG   . LYS   A 1 90  ? 31.282 -3.366  17.442  1.00 23.96 ?  90  LYS   A CG   1 
ATOM   1811 C CD   . LYS   A 1 90  ? 31.533 -4.580  18.323  1.00 29.04 ?  90  LYS   A CD   1 
ATOM   1812 C CE   . LYS   A 1 90  ? 32.950 -4.597  18.880  1.00 32.65 ?  90  LYS   A CE   1 
ATOM   1813 N NZ   . LYS   A 1 90  ? 33.958 -5.014  17.869  1.00 34.58 ?  90  LYS   A NZ   1 
ATOM   1814 H H    . LYS   A 1 90  ? 27.547 -2.418  16.519  1.00 19.33 ?  90  LYS   A H    1 
ATOM   1815 H HA   . LYS   A 1 90  ? 29.783 -1.175  17.099  1.00 19.32 ?  90  LYS   A HA   1 
ATOM   1816 H HB2  . LYS   A 1 90  ? 29.301 -3.325  17.944  1.00 23.08 ?  90  LYS   A HB2  1 
ATOM   1817 H HB3  . LYS   A 1 90  ? 29.560 -3.922  16.495  1.00 23.08 ?  90  LYS   A HB3  1 
ATOM   1818 H HG2  . LYS   A 1 90  ? 31.781 -3.476  16.619  1.00 28.73 ?  90  LYS   A HG2  1 
ATOM   1819 H HG3  . LYS   A 1 90  ? 31.584 -2.576  17.918  1.00 28.73 ?  90  LYS   A HG3  1 
ATOM   1820 H HD2  . LYS   A 1 90  ? 30.914 -4.567  19.070  1.00 34.82 ?  90  LYS   A HD2  1 
ATOM   1821 H HD3  . LYS   A 1 90  ? 31.404 -5.386  17.798  1.00 34.82 ?  90  LYS   A HD3  1 
ATOM   1822 H HE2  . LYS   A 1 90  ? 33.181 -3.705  19.185  1.00 39.16 ?  90  LYS   A HE2  1 
ATOM   1823 H HE3  . LYS   A 1 90  ? 32.992 -5.222  19.621  1.00 39.16 ?  90  LYS   A HE3  1 
ATOM   1824 H HZ1  . LYS   A 1 90  ? 33.772 -5.832  17.573  1.00 41.48 ?  90  LYS   A HZ1  1 
ATOM   1825 H HZ2  . LYS   A 1 90  ? 33.952 -4.449  17.182  1.00 41.48 ?  90  LYS   A HZ2  1 
ATOM   1826 H HZ3  . LYS   A 1 90  ? 34.771 -5.017  18.233  1.00 41.48 ?  90  LYS   A HZ3  1 
ATOM   1827 N N    . HIS   A 1 91  ? 29.687 -2.385  14.131  1.00 13.05 ?  91  HIS   A N    1 
ATOM   1828 C CA   . HIS   A 1 91  ? 30.260 -2.358  12.804  1.00 12.58 ?  91  HIS   A CA   1 
ATOM   1829 C C    . HIS   A 1 91  ? 29.171 -2.084  11.787  1.00 11.22 ?  91  HIS   A C    1 
ATOM   1830 O O    . HIS   A 1 91  ? 28.006 -2.445  11.986  1.00 12.27 ?  91  HIS   A O    1 
ATOM   1831 C CB   . HIS   A 1 91  ? 30.867 -3.721  12.428  1.00 14.99 ?  91  HIS   A CB   1 
ATOM   1832 C CG   . HIS   A 1 91  ? 31.872 -4.232  13.408  1.00 19.70 ?  91  HIS   A CG   1 
ATOM   1833 N ND1  . HIS   A 1 91  ? 33.143 -3.710  13.514  1.00 22.29 ?  91  HIS   A ND1  1 
ATOM   1834 C CD2  . HIS   A 1 91  ? 31.800 -5.230  14.320  1.00 21.62 ?  91  HIS   A CD2  1 
ATOM   1835 C CE1  . HIS   A 1 91  ? 33.809 -4.360  14.452  1.00 23.16 ?  91  HIS   A CE1  1 
ATOM   1836 N NE2  . HIS   A 1 91  ? 33.015 -5.289  14.957  1.00 23.07 ?  91  HIS   A NE2  1 
ATOM   1837 H H    . HIS   A 1 91  ? 29.013 -2.934  14.199  1.00 15.64 ?  91  HIS   A H    1 
ATOM   1838 H HA   . HIS   A 1 91  ? 30.944 -1.682  12.742  1.00 15.07 ?  91  HIS   A HA   1 
ATOM   1839 H HB2  . HIS   A 1 91  ? 30.156 -4.382  12.370  1.00 17.97 ?  91  HIS   A HB2  1 
ATOM   1840 H HB3  . HIS   A 1 91  ? 31.309 -3.644  11.567  1.00 17.97 ?  91  HIS   A HB3  1 
ATOM   1841 H HD1  . HIS   A 1 91  ? 33.456 -3.062  13.041  1.00 26.72 ?  91  HIS   A HD1  1 
ATOM   1842 H HD2  . HIS   A 1 91  ? 31.070 -5.776  14.490  1.00 25.92 ?  91  HIS   A HD2  1 
ATOM   1843 H HE1  . HIS   A 1 91  ? 34.690 -4.189  14.713  1.00 27.77 ?  91  HIS   A HE1  1 
ATOM   1844 N N    . CYS   A 1 92  ? 29.569 -1.486  10.674  1.00 11.27 ?  92  CYS   A N    1 
ATOM   1845 C CA   . CYS   A 1 92  ? 28.735 -1.410  9.485   1.00 11.03 ?  92  CYS   A CA   1 
ATOM   1846 C C    . CYS   A 1 92  ? 29.384 -2.226  8.375   1.00 10.66 ?  92  CYS   A C    1 
ATOM   1847 O O    . CYS   A 1 92  ? 30.543 -1.977  8.011   1.00 11.78 ?  92  CYS   A O    1 
ATOM   1848 C CB   . CYS   A 1 92  ? 28.524 0.034   9.027   1.00 11.94 ?  92  CYS   A CB   1 
ATOM   1849 S SG   . CYS   A 1 92  ? 27.507 0.150   7.520   1.00 11.41 ?  92  CYS   A SG   1 
ATOM   1850 H H    . CYS   A 1 92  ? 30.335 -1.096  10.584  1.00 13.50 ?  92  CYS   A H    1 
ATOM   1851 H HA   . CYS   A 1 92  ? 27.868 -1.791  9.676   1.00 13.21 ?  92  CYS   A HA   1 
ATOM   1852 H HB2  . CYS   A 1 92  ? 28.071 0.532   9.726   1.00 14.31 ?  92  CYS   A HB2  1 
ATOM   1853 H HB3  . CYS   A 1 92  ? 29.383 0.441   8.832   1.00 14.31 ?  92  CYS   A HB3  1 
ATOM   1854 H HG   . CYS   A 1 92  ? 27.373 1.305   7.231   1.00 13.67 ?  92  CYS   A HG   1 
ATOM   1855 N N    . LEU   A 1 93  ? 28.646 -3.212  7.866   1.00 10.69 ?  93  LEU   A N    1 
ATOM   1856 C CA   . LEU   A 1 93  ? 29.050 -3.965  6.684   1.00 9.83  ?  93  LEU   A CA   1 
ATOM   1857 C C    . LEU   A 1 93  ? 28.456 -3.267  5.466   1.00 9.83  ?  93  LEU   A C    1 
ATOM   1858 O O    . LEU   A 1 93  ? 27.239 -3.329  5.244   1.00 10.28 ?  93  LEU   A O    1 
ATOM   1859 C CB   . LEU   A 1 93  ? 28.571 -5.413  6.789   1.00 10.80 ?  93  LEU   A CB   1 
ATOM   1860 C CG   . LEU   A 1 93  ? 28.963 -6.309  5.618   1.00 10.91 ?  93  LEU   A CG   1 
ATOM   1861 C CD1  . LEU   A 1 93  ? 30.470 -6.564  5.612   1.00 12.10 ?  93  LEU   A CD1  1 
ATOM   1862 C CD2  . LEU   A 1 93  ? 28.186 -7.624  5.649   1.00 11.91 ?  93  LEU   A CD2  1 
ATOM   1863 H H    . LEU   A 1 93  ? 27.897 -3.466  8.204   1.00 12.80 ?  93  LEU   A H    1 
ATOM   1864 H HA   . LEU   A 1 93  ? 30.011 -3.955  6.608   1.00 11.77 ?  93  LEU   A HA   1 
ATOM   1865 H HB2  . LEU   A 1 93  ? 28.950 -5.799  7.596   1.00 12.93 ?  93  LEU   A HB2  1 
ATOM   1866 H HB3  . LEU   A 1 93  ? 27.606 -5.417  6.849   1.00 12.93 ?  93  LEU   A HB3  1 
ATOM   1867 H HG   . LEU   A 1 93  ? 28.747 -5.859  4.792   1.00 13.07 ?  93  LEU   A HG   1 
ATOM   1868 H HD11 . LEU   A 1 93  ? 30.690 -7.177  4.893   1.00 14.50 ?  93  LEU   A HD11 1 
ATOM   1869 H HD12 . LEU   A 1 93  ? 30.940 -5.726  5.489   1.00 14.50 ?  93  LEU   A HD12 1 
ATOM   1870 H HD13 . LEU   A 1 93  ? 30.731 -6.962  6.466   1.00 14.50 ?  93  LEU   A HD13 1 
ATOM   1871 H HD21 . LEU   A 1 93  ? 28.461 -8.171  4.894   1.00 14.27 ?  93  LEU   A HD21 1 
ATOM   1872 H HD22 . LEU   A 1 93  ? 28.377 -8.089  6.479   1.00 14.27 ?  93  LEU   A HD22 1 
ATOM   1873 H HD23 . LEU   A 1 93  ? 27.238 -7.431  5.587   1.00 14.27 ?  93  LEU   A HD23 1 
ATOM   1874 N N    . HIS   A 1 94  ? 29.304 -2.569  4.707   1.00 9.74  ?  94  HIS   A N    1 
ATOM   1875 C CA   . HIS   A 1 94  ? 28.875 -1.894  3.485   1.00 10.05 ?  94  HIS   A CA   1 
ATOM   1876 C C    . HIS   A 1 94  ? 28.885 -2.928  2.376   1.00 9.98  ?  94  HIS   A C    1 
ATOM   1877 O O    . HIS   A 1 94  ? 29.952 -3.442  2.028   1.00 11.52 ?  94  HIS   A O    1 
ATOM   1878 C CB   . HIS   A 1 94  ? 29.834 -0.746  3.156   1.00 10.01 ?  94  HIS   A CB   1 
ATOM   1879 C CG   . HIS   A 1 94  ? 29.823 0.342   4.171   1.00 10.13 ?  94  HIS   A CG   1 
ATOM   1880 N ND1  . HIS   A 1 94  ? 28.942 1.403   4.122   1.00 10.10 ?  94  HIS   A ND1  1 
ATOM   1881 C CD2  . HIS   A 1 94  ? 30.561 0.506   5.289   1.00 10.84 ?  94  HIS   A CD2  1 
ATOM   1882 C CE1  . HIS   A 1 94  ? 29.160 2.183   5.166   1.00 10.43 ?  94  HIS   A CE1  1 
ATOM   1883 N NE2  . HIS   A 1 94  ? 30.139 1.663   5.886   1.00 10.70 ?  94  HIS   A NE2  1 
ATOM   1884 H H    . HIS   A 1 94  ? 30.140 -2.468  4.886   1.00 11.67 ?  94  HIS   A H    1 
ATOM   1885 H HA   . HIS   A 1 94  ? 27.975 -1.545  3.590   1.00 12.04 ?  94  HIS   A HA   1 
ATOM   1886 H HB2  . HIS   A 1 94  ? 30.732 -1.093  3.103   1.00 11.99 ?  94  HIS   A HB2  1 
ATOM   1887 H HB3  . HIS   A 1 94  ? 29.572 -0.359  2.304   1.00 11.99 ?  94  HIS   A HB3  1 
ATOM   1888 H HD2  . HIS   A 1 94  ? 31.241 -0.045  5.588   1.00 12.98 ?  94  HIS   A HD2  1 
ATOM   1889 H HE1  . HIS   A 1 94  ? 28.692 2.969   5.360   1.00 12.49 ?  94  HIS   A HE1  1 
ATOM   1890 H HE2  . HIS   A 1 94  ? 30.454 2.005   6.609   1.00 12.81 ?  94  HIS   A HE2  1 
ATOM   1891 N N    . VAL   A 1 95  ? 27.717 -3.253  1.831   1.00 9.28  ?  95  VAL   A N    1 
ATOM   1892 C CA   . VAL   A 1 95  ? 27.580 -4.287  0.809   1.00 9.68  ?  95  VAL   A CA   1 
ATOM   1893 C C    . VAL   A 1 95  ? 27.032 -3.648  -0.455  1.00 9.26  ?  95  VAL   A C    1 
ATOM   1894 O O    . VAL   A 1 95  ? 26.024 -2.928  -0.398  1.00 10.38 ?  95  VAL   A O    1 
ATOM   1895 C CB   . VAL   A 1 95  ? 26.649 -5.432  1.257   1.00 10.44 ?  95  VAL   A CB   1 
ATOM   1896 C CG1  . VAL   A 1 95  ? 26.538 -6.474  0.154   1.00 11.02 ?  95  VAL   A CG1  1 
ATOM   1897 C CG2  . VAL   A 1 95  ? 27.144 -6.052  2.543   1.00 10.79 ?  95  VAL   A CG2  1 
ATOM   1898 H H    . VAL   A 1 95  ? 26.970 -2.884  2.044   1.00 11.11 ?  95  VAL   A H    1 
ATOM   1899 H HA   . VAL   A 1 95  ? 28.451 -4.662  0.607   1.00 11.60 ?  95  VAL   A HA   1 
ATOM   1900 H HB   . VAL   A 1 95  ? 25.766 -5.077  1.416   1.00 12.51 ?  95  VAL   A HB   1 
ATOM   1901 H HG11 . VAL   A 1 95  ? 26.144 -7.284  0.518   1.00 13.20 ?  95  VAL   A HG11 1 
ATOM   1902 H HG12 . VAL   A 1 95  ? 25.978 -6.132  -0.561  1.00 13.20 ?  95  VAL   A HG12 1 
ATOM   1903 H HG13 . VAL   A 1 95  ? 27.427 -6.674  -0.191  1.00 13.20 ?  95  VAL   A HG13 1 
ATOM   1904 H HG21 . VAL   A 1 95  ? 26.576 -6.808  2.766   1.00 12.92 ?  95  VAL   A HG21 1 
ATOM   1905 H HG22 . VAL   A 1 95  ? 28.058 -6.348  2.423   1.00 12.92 ?  95  VAL   A HG22 1 
ATOM   1906 H HG23 . VAL   A 1 95  ? 27.098 -5.387  3.248   1.00 12.92 ?  95  VAL   A HG23 1 
ATOM   1907 N N    . VAL   A 1 96  ? 27.657 -3.937  -1.595  1.00 9.21  ?  96  VAL   A N    1 
ATOM   1908 C CA   . VAL   A 1 96  ? 27.248 -3.380  -2.877  1.00 10.25 ?  96  VAL   A CA   1 
ATOM   1909 C C    . VAL   A 1 96  ? 26.441 -4.427  -3.633  1.00 10.52 ?  96  VAL   A C    1 
ATOM   1910 O O    . VAL   A 1 96  ? 27.000 -5.366  -4.207  1.00 11.43 ?  96  VAL   A O    1 
ATOM   1911 C CB   . VAL   A 1 96  ? 28.442 -2.908  -3.706  1.00 10.59 ?  96  VAL   A CB   1 
ATOM   1912 C CG1  . VAL   A 1 96  ? 27.939 -2.262  -4.978  1.00 10.76 ?  96  VAL   A CG1  1 
ATOM   1913 C CG2  . VAL   A 1 96  ? 29.314 -1.952  -2.909  1.00 11.29 ?  96  VAL   A CG2  1 
ATOM   1914 H H    . VAL   A 1 96  ? 28.340 -4.463  -1.652  1.00 11.03 ?  96  VAL   A H    1 
ATOM   1915 H HA   . VAL   A 1 96  ? 26.675 -2.613  -2.720  1.00 12.27 ?  96  VAL   A HA   1 
ATOM   1916 H HB   . VAL   A 1 96  ? 28.981 -3.674  -3.955  1.00 12.69 ?  96  VAL   A HB   1 
ATOM   1917 H HG11 . VAL   A 1 96  ? 28.680 -1.799  -5.408  1.00 12.89 ?  96  VAL   A HG11 1 
ATOM   1918 H HG12 . VAL   A 1 96  ? 27.589 -2.941  -5.570  1.00 12.89 ?  96  VAL   A HG12 1 
ATOM   1919 H HG13 . VAL   A 1 96  ? 27.244 -1.620  -4.755  1.00 12.89 ?  96  VAL   A HG13 1 
ATOM   1920 H HG21 . VAL   A 1 96  ? 30.014 -1.605  -3.481  1.00 13.52 ?  96  VAL   A HG21 1 
ATOM   1921 H HG22 . VAL   A 1 96  ? 28.763 -1.222  -2.579  1.00 13.52 ?  96  VAL   A HG22 1 
ATOM   1922 H HG23 . VAL   A 1 96  ? 29.704 -2.431  -2.159  1.00 13.52 ?  96  VAL   A HG23 1 
ATOM   1923 N N    . GLY   A 1 97  ? 25.122 -4.270  -3.658  1.00 10.65 ?  97  GLY   A N    1 
ATOM   1924 C CA   . GLY   A 1 97  ? 24.307 -5.026  -4.571  1.00 10.87 ?  97  GLY   A CA   1 
ATOM   1925 C C    . GLY   A 1 97  ? 24.320 -4.376  -5.940  1.00 11.17 ?  97  GLY   A C    1 
ATOM   1926 O O    . GLY   A 1 97  ? 24.596 -3.179  -6.074  1.00 12.05 ?  97  GLY   A O    1 
ATOM   1927 H H    . GLY   A 1 97  ? 24.678 -3.726  -3.146  1.00 12.76 ?  97  GLY   A H    1 
ATOM   1928 H HA2  . GLY   A 1 97  ? 24.657 -5.929  -4.636  1.00 13.02 ?  97  GLY   A HA2  1 
ATOM   1929 H HA3  . GLY   A 1 97  ? 23.394 -5.068  -4.242  1.00 13.02 ?  97  GLY   A HA3  1 
ATOM   1930 N N    . PRO   A 1 98  ? 24.000 -5.135  -6.983  1.00 11.03 ?  98  PRO   A N    1 
ATOM   1931 C CA   . PRO   A 1 98  ? 23.902 -4.539  -8.318  1.00 12.42 ?  98  PRO   A CA   1 
ATOM   1932 C C    . PRO   A 1 98  ? 22.785 -3.507  -8.390  1.00 12.89 ?  98  PRO   A C    1 
ATOM   1933 O O    . PRO   A 1 98  ? 21.708 -3.679  -7.812  1.00 12.89 ?  98  PRO   A O    1 
ATOM   1934 C CB   . PRO   A 1 98  ? 23.608 -5.741  -9.224  1.00 12.79 ?  98  PRO   A CB   1 
ATOM   1935 C CG   . PRO   A 1 98  ? 22.956 -6.743  -8.314  1.00 13.01 ?  98  PRO   A CG   1 
ATOM   1936 C CD   . PRO   A 1 98  ? 23.676 -6.573  -6.995  1.00 11.47 ?  98  PRO   A CD   1 
ATOM   1937 H HA   . PRO   A 1 98  ? 24.747 -4.132  -8.570  1.00 14.88 ?  98  PRO   A HA   1 
ATOM   1938 H HB2  . PRO   A 1 98  ? 23.004 -5.471  -9.932  1.00 15.33 ?  98  PRO   A HB2  1 
ATOM   1939 H HB3  . PRO   A 1 98  ? 24.436 -6.089  -9.585  1.00 15.33 ?  98  PRO   A HB3  1 
ATOM   1940 H HG2  . PRO   A 1 98  ? 22.011 -6.536  -8.220  1.00 15.58 ?  98  PRO   A HG2  1 
ATOM   1941 H HG3  . PRO   A 1 98  ? 23.082 -7.636  -8.664  1.00 15.58 ?  98  PRO   A HG3  1 
ATOM   1942 H HD2  . PRO   A 1 98  ? 23.081 -6.799  -6.257  1.00 13.74 ?  98  PRO   A HD2  1 
ATOM   1943 H HD3  . PRO   A 1 98  ? 24.482 -7.109  -6.977  1.00 13.74 ?  98  PRO   A HD3  1 
ATOM   1944 N N    A ASN   A 1 99  ? 23.064 -2.394  -9.069  0.68 13.36 ?  99  ASN   A N    1 
ATOM   1945 N N    B ASN   A 1 99  ? 23.053 -2.453  -9.150  0.32 13.97 ?  99  ASN   A N    1 
ATOM   1946 C CA   A ASN   A 1 99  ? 22.089 -1.320  -9.257  0.68 14.11 ?  99  ASN   A CA   1 
ATOM   1947 C CA   B ASN   A 1 99  ? 22.069 -1.436  -9.481  0.32 15.17 ?  99  ASN   A CA   1 
ATOM   1948 C C    A ASN   A 1 99  ? 21.544 -1.451  -10.676 0.68 15.52 ?  99  ASN   A C    1 
ATOM   1949 C C    B ASN   A 1 99  ? 21.472 -1.772  -10.842 0.32 16.35 ?  99  ASN   A C    1 
ATOM   1950 O O    A ASN   A 1 99  ? 22.220 -1.112  -11.653 0.68 16.35 ?  99  ASN   A O    1 
ATOM   1951 O O    B ASN   A 1 99  ? 22.185 -1.796  -11.852 0.32 16.01 ?  99  ASN   A O    1 
ATOM   1952 C CB   A ASN   A 1 99  ? 22.721 0.049   -9.005  0.68 14.40 ?  99  ASN   A CB   1 
ATOM   1953 C CB   B ASN   A 1 99  ? 22.735 -0.062  -9.519  0.32 16.05 ?  99  ASN   A CB   1 
ATOM   1954 C CG   A ASN   A 1 99  ? 21.692 1.191   -8.993  0.68 15.41 ?  99  ASN   A CG   1 
ATOM   1955 C CG   B ASN   A 1 99  ? 21.732 1.069   -9.576  0.32 16.85 ?  99  ASN   A CG   1 
ATOM   1956 O OD1  A ASN   A 1 99  ? 20.677 1.138   -9.690  0.68 16.38 ?  99  ASN   A OD1  1 
ATOM   1957 O OD1  B ASN   A 1 99  ? 20.714 0.978   -10.261 0.32 17.20 ?  99  ASN   A OD1  1 
ATOM   1958 N ND2  A ASN   A 1 99  ? 21.966 2.231   -8.204  0.68 15.86 ?  99  ASN   A ND2  1 
ATOM   1959 N ND2  B ASN   A 1 99  ? 22.012 2.143   -8.845  0.32 17.26 ?  99  ASN   A ND2  1 
ATOM   1960 H H    A ASN   A 1 99  ? 23.827 -2.231  -9.429  0.68 16.00 ?  99  ASN   A H    1 
ATOM   1961 H H    B ASN   A 1 99  ? 23.829 -2.301  -9.487  0.32 16.74 ?  99  ASN   A H    1 
ATOM   1962 H HA   A ASN   A 1 99  ? 21.359 -1.437  -8.625  0.68 16.91 ?  99  ASN   A HA   1 
ATOM   1963 H HA   B ASN   A 1 99  ? 21.365 -1.431  -8.813  0.32 18.18 ?  99  ASN   A HA   1 
ATOM   1964 H HB2  A ASN   A 1 99  ? 23.168 0.047   -8.145  0.68 17.25 ?  99  ASN   A HB2  1 
ATOM   1965 H HB2  B ASN   A 1 99  ? 23.277 0.049   -8.719  0.32 19.24 ?  99  ASN   A HB2  1 
ATOM   1966 H HB3  A ASN   A 1 99  ? 23.365 0.235   -9.710  0.68 17.25 ?  99  ASN   A HB3  1 
ATOM   1967 H HB3  B ASN   A 1 99  ? 23.294 -0.005  -10.308 0.32 19.24 ?  99  ASN   A HB3  1 
ATOM   1968 H HD21 A ASN   A 1 99  ? 21.426 2.901   -8.165  0.68 19.01 ?  99  ASN   A HD21 1 
ATOM   1969 H HD21 B ASN   A 1 99  ? 21.473 2.810   -8.835  0.32 20.69 ?  99  ASN   A HD21 1 
ATOM   1970 H HD22 A ASN   A 1 99  ? 22.687 2.236   -7.734  0.68 19.01 ?  99  ASN   A HD22 1 
ATOM   1971 H HD22 B ASN   A 1 99  ? 22.738 2.169   -8.380  0.32 20.69 ?  99  ASN   A HD22 1 
ATOM   1972 N N    A VAL   A 1 100 ? 20.316 -1.970  -10.776 0.68 16.93 ?  100 VAL   A N    1 
ATOM   1973 N N    B VAL   A 1 100 ? 20.166 -2.041  -10.861 0.32 17.88 ?  100 VAL   A N    1 
ATOM   1974 C CA   A VAL   A 1 100 ? 19.683 -2.184  -12.075 0.68 19.20 ?  100 VAL   A CA   1 
ATOM   1975 C CA   B VAL   A 1 100 ? 19.484 -2.370  -12.109 0.32 19.85 ?  100 VAL   A CA   1 
ATOM   1976 C C    A VAL   A 1 100 ? 19.546 -0.871  -12.833 0.68 19.74 ?  100 VAL   A C    1 
ATOM   1977 C C    B VAL   A 1 100 ? 19.532 -1.192  -13.070 0.32 21.42 ?  100 VAL   A C    1 
ATOM   1978 O O    A VAL   A 1 100 ? 19.621 -0.844  -14.067 0.68 20.84 ?  100 VAL   A O    1 
ATOM   1979 O O    B VAL   A 1 100 ? 19.700 -1.367  -14.283 0.32 22.16 ?  100 VAL   A O    1 
ATOM   1980 C CB   A VAL   A 1 100 ? 18.335 -2.915  -11.891 0.68 20.89 ?  100 VAL   A CB   1 
ATOM   1981 C CB   B VAL   A 1 100 ? 18.037 -2.810  -11.821 0.32 20.28 ?  100 VAL   A CB   1 
ATOM   1982 C CG1  A VAL   A 1 100 ? 17.646 -3.144  -13.230 0.68 21.78 ?  100 VAL   A CG1  1 
ATOM   1983 C CG1  B VAL   A 1 100 ? 17.207 -2.812  -13.097 0.32 20.51 ?  100 VAL   A CG1  1 
ATOM   1984 C CG2  A VAL   A 1 100 ? 18.556 -4.241  -11.175 0.68 21.07 ?  100 VAL   A CG2  1 
ATOM   1985 C CG2  B VAL   A 1 100 ? 18.023 -4.174  -11.164 0.32 20.54 ?  100 VAL   A CG2  1 
ATOM   1986 H H    A VAL   A 1 100 ? 19.830 -2.211  -10.101 0.68 20.29 ?  100 VAL   A H    1 
ATOM   1987 H H    B VAL   A 1 100 ? 19.660 -2.041  -10.167 0.32 21.44 ?  100 VAL   A H    1 
ATOM   1988 H HA   A VAL   A 1 100 ? 20.253 -2.762  -12.600 0.68 23.01 ?  100 VAL   A HA   1 
ATOM   1989 H HA   B VAL   A 1 100 ? 19.941 -3.111  -12.530 0.32 23.80 ?  100 VAL   A HA   1 
ATOM   1990 H HB   A VAL   A 1 100 ? 17.748 -2.374  -11.339 0.68 25.05 ?  100 VAL   A HB   1 
ATOM   1991 H HB   B VAL   A 1 100 ? 17.641 -2.178  -11.210 0.32 24.31 ?  100 VAL   A HB   1 
ATOM   1992 H HG11 A VAL   A 1 100 ? 16.885 -3.734  -13.099 0.68 26.11 ?  100 VAL   A HG11 1 
ATOM   1993 H HG11 B VAL   A 1 100 ? 16.408 -3.340  -12.947 0.32 24.58 ?  100 VAL   A HG11 1 
ATOM   1994 H HG12 A VAL   A 1 100 ? 17.343 -2.293  -13.582 0.68 26.11 ?  100 VAL   A HG12 1 
ATOM   1995 H HG12 B VAL   A 1 100 ? 16.961 -1.900  -13.322 0.32 24.58 ?  100 VAL   A HG12 1 
ATOM   1996 H HG13 A VAL   A 1 100 ? 18.275 -3.553  -13.844 0.68 26.11 ?  100 VAL   A HG13 1 
ATOM   1997 H HG13 B VAL   A 1 100 ? 17.731 -3.203  -13.812 0.32 24.58 ?  100 VAL   A HG13 1 
ATOM   1998 H HG21 A VAL   A 1 100 ? 17.724 -4.741  -11.171 0.68 25.26 ?  100 VAL   A HG21 1 
ATOM   1999 H HG21 B VAL   A 1 100 ? 17.106 -4.426  -10.982 0.32 24.63 ?  100 VAL   A HG21 1 
ATOM   2000 H HG22 A VAL   A 1 100 ? 19.240 -4.742  -11.646 0.68 25.26 ?  100 VAL   A HG22 1 
ATOM   2001 H HG22 B VAL   A 1 100 ? 18.432 -4.814  -11.766 0.32 24.63 ?  100 VAL   A HG22 1 
ATOM   2002 H HG23 A VAL   A 1 100 ? 18.840 -4.067  -10.264 0.68 25.26 ?  100 VAL   A HG23 1 
ATOM   2003 H HG23 B VAL   A 1 100 ? 18.526 -4.129  -10.335 0.32 24.63 ?  100 VAL   A HG23 1 
ATOM   2004 N N    A ASN   A 1 101 ? 19.359 0.239   -12.122 0.68 20.52 ?  101 ASN   A N    1 
ATOM   2005 N N    B ASN   A 1 101 ? 19.376 0.025   -12.545 0.32 22.23 ?  101 ASN   A N    1 
ATOM   2006 C CA   A ASN   A 1 101 ? 19.296 1.527   -12.801 0.68 21.94 ?  101 ASN   A CA   1 
ATOM   2007 C CA   B ASN   A 1 101 ? 19.322 1.205   -13.400 0.32 23.03 ?  101 ASN   A CA   1 
ATOM   2008 C C    A ASN   A 1 101 ? 20.654 1.971   -13.351 0.68 23.90 ?  101 ASN   A C    1 
ATOM   2009 C C    B ASN   A 1 101 ? 20.644 1.440   -14.119 0.32 23.92 ?  101 ASN   A C    1 
ATOM   2010 O O    A ASN   A 1 101 ? 20.733 3.046   -13.963 0.68 25.30 ?  101 ASN   A O    1 
ATOM   2011 O O    B ASN   A 1 101 ? 20.650 1.947   -15.246 0.32 23.15 ?  101 ASN   A O    1 
ATOM   2012 C CB   A ASN   A 1 101 ? 18.651 2.563   -11.874 0.68 21.49 ?  101 ASN   A CB   1 
ATOM   2013 C CB   B ASN   A 1 101 ? 18.914 2.423   -12.569 0.32 22.82 ?  101 ASN   A CB   1 
ATOM   2014 C CG   A ASN   A 1 101 ? 17.265 2.125   -11.389 0.68 20.94 ?  101 ASN   A CG   1 
ATOM   2015 C CG   B ASN   A 1 101 ? 17.618 2.198   -11.814 0.32 22.60 ?  101 ASN   A CG   1 
ATOM   2016 O OD1  A ASN   A 1 101 ? 16.469 1.569   -12.153 0.68 21.87 ?  101 ASN   A OD1  1 
ATOM   2017 O OD1  B ASN   A 1 101 ? 16.570 1.965   -12.417 0.32 22.57 ?  101 ASN   A OD1  1 
ATOM   2018 N ND2  A ASN   A 1 101 ? 16.981 2.355   -10.111 0.68 20.73 ?  101 ASN   A ND2  1 
ATOM   2019 N ND2  B ASN   A 1 101 ? 17.682 2.269   -10.488 0.32 22.61 ?  101 ASN   A ND2  1 
ATOM   2020 H H    A ASN   A 1 101 ? 19.265 0.270   -11.267 0.68 24.60 ?  101 ASN   A H    1 
ATOM   2021 H H    B ASN   A 1 101 ? 19.300 0.193   -11.705 0.32 26.65 ?  101 ASN   A H    1 
ATOM   2022 H HA   A ASN   A 1 101 ? 18.709 1.432   -13.562 0.68 26.30 ?  101 ASN   A HA   1 
ATOM   2023 H HA   B ASN   A 1 101 ? 18.643 1.074   -14.077 0.32 27.61 ?  101 ASN   A HA   1 
ATOM   2024 H HB2  A ASN   A 1 101 ? 19.212 2.697   -11.095 0.68 25.76 ?  101 ASN   A HB2  1 
ATOM   2025 H HB2  B ASN   A 1 101 ? 19.608 2.614   -11.919 0.32 27.36 ?  101 ASN   A HB2  1 
ATOM   2026 H HB3  A ASN   A 1 101 ? 18.553 3.403   -12.357 0.68 25.76 ?  101 ASN   A HB3  1 
ATOM   2027 H HB3  B ASN   A 1 101 ? 18.786 3.184   -13.154 0.32 27.36 ?  101 ASN   A HB3  1 
ATOM   2028 H HD21 A ASN   A 1 101 ? 16.212 2.133   -9.796  0.68 24.85 ?  101 ASN   A HD21 1 
ATOM   2029 H HD21 B ASN   A 1 101 ? 16.974 2.144   -10.013 0.32 27.11 ?  101 ASN   A HD21 1 
ATOM   2030 H HD22 A ASN   A 1 101 ? 17.560 2.737   -9.603  0.68 24.85 ?  101 ASN   A HD22 1 
ATOM   2031 H HD22 B ASN   A 1 101 ? 18.431 2.443   -10.102 0.32 27.11 ?  101 ASN   A HD22 1 
ATOM   2032 N N    A LYS   A 1 102 ? 21.702 1.154   -13.177 0.68 25.98 ?  102 LYS   A N    1 
ATOM   2033 N N    B LYS   A 1 102 ? 21.763 1.074   -13.498 0.32 25.63 ?  102 LYS   A N    1 
ATOM   2034 C CA   A LYS   A 1 102 ? 23.000 1.362   -13.810 0.68 27.49 ?  102 LYS   A CA   1 
ATOM   2035 C CA   B LYS   A 1 102 ? 23.072 1.170   -14.127 0.32 26.79 ?  102 LYS   A CA   1 
ATOM   2036 C C    A LYS   A 1 102 ? 23.349 0.288   -14.835 0.68 28.22 ?  102 LYS   A C    1 
ATOM   2037 C C    B LYS   A 1 102 ? 23.395 -0.057  -14.970 0.32 26.88 ?  102 LYS   A C    1 
ATOM   2038 O O    A LYS   A 1 102 ? 24.397 0.395   -15.481 0.68 28.93 ?  102 LYS   A O    1 
ATOM   2039 O O    B LYS   A 1 102 ? 24.548 -0.234  -15.377 0.32 26.61 ?  102 LYS   A O    1 
ATOM   2040 C CB   A LYS   A 1 102 ? 24.119 1.415   -12.759 0.68 28.61 ?  102 LYS   A CB   1 
ATOM   2041 C CB   B LYS   A 1 102 ? 24.156 1.360   -13.064 0.32 28.11 ?  102 LYS   A CB   1 
ATOM   2042 C CG   A LYS   A 1 102 ? 24.005 2.535   -11.744 0.68 29.55 ?  102 LYS   A CG   1 
ATOM   2043 C CG   B LYS   A 1 102 ? 23.895 2.521   -12.126 0.32 29.33 ?  102 LYS   A CG   1 
ATOM   2044 C CD   A LYS   A 1 102 ? 25.179 2.495   -10.768 0.68 30.65 ?  102 LYS   A CD   1 
ATOM   2045 C CD   B LYS   A 1 102 ? 24.981 2.648   -11.076 0.32 30.56 ?  102 LYS   A CD   1 
ATOM   2046 C CE   A LYS   A 1 102 ? 25.095 3.608   -9.735  0.68 31.44 ?  102 LYS   A CE   1 
ATOM   2047 C CE   B LYS   A 1 102 ? 24.743 3.858   -10.190 0.32 31.47 ?  102 LYS   A CE   1 
ATOM   2048 N NZ   A LYS   A 1 102 ? 26.201 3.528   -8.735  0.68 31.65 ?  102 LYS   A NZ   1 
ATOM   2049 N NZ   B LYS   A 1 102 ? 26.011 4.375   -9.609  0.32 31.94 ?  102 LYS   A NZ   1 
ATOM   2050 H H    A LYS   A 1 102 ? 21.681 0.446   -12.684 0.68 31.15 ?  102 LYS   A H    1 
ATOM   2051 H H    B LYS   A 1 102 ? 21.785 0.751   -12.703 0.32 30.73 ?  102 LYS   A H    1 
ATOM   2052 H HA   A LYS   A 1 102 ? 22.988 2.209   -14.272 0.68 32.96 ?  102 LYS   A HA   1 
ATOM   2053 H HA   B LYS   A 1 102 ? 23.083 1.956   -14.700 0.32 32.13 ?  102 LYS   A HA   1 
ATOM   2054 H HB2  A LYS   A 1 102 ? 24.125 0.579   -12.270 0.68 34.31 ?  102 LYS   A HB2  1 
ATOM   2055 H HB2  B LYS   A 1 102 ? 24.214 0.553   -12.531 0.32 33.70 ?  102 LYS   A HB2  1 
ATOM   2056 H HB3  A LYS   A 1 102 ? 24.965 1.527   -13.221 0.68 34.31 ?  102 LYS   A HB3  1 
ATOM   2057 H HB3  B LYS   A 1 102 ? 25.004 1.522   -13.510 0.32 33.70 ?  102 LYS   A HB3  1 
ATOM   2058 H HG2  A LYS   A 1 102 ? 24.015 3.389   -12.203 0.68 35.44 ?  102 LYS   A HG2  1 
ATOM   2059 H HG2  B LYS   A 1 102 ? 23.870 3.345   -12.638 0.32 35.18 ?  102 LYS   A HG2  1 
ATOM   2060 H HG3  A LYS   A 1 102 ? 23.183 2.430   -11.240 0.68 35.44 ?  102 LYS   A HG3  1 
ATOM   2061 H HG3  B LYS   A 1 102 ? 23.049 2.382   -11.673 0.32 35.18 ?  102 LYS   A HG3  1 
ATOM   2062 H HD2  A LYS   A 1 102 ? 25.176 1.645   -10.301 0.68 36.75 ?  102 LYS   A HD2  1 
ATOM   2063 H HD2  B LYS   A 1 102 ? 24.981 1.855   -10.516 0.32 36.65 ?  102 LYS   A HD2  1 
ATOM   2064 H HD3  A LYS   A 1 102 ? 26.007 2.601   -11.263 0.68 36.75 ?  102 LYS   A HD3  1 
ATOM   2065 H HD3  B LYS   A 1 102 ? 25.841 2.752   -11.511 0.32 36.65 ?  102 LYS   A HD3  1 
ATOM   2066 H HE2  A LYS   A 1 102 ? 25.155 4.465   -10.186 0.68 37.70 ?  102 LYS   A HE2  1 
ATOM   2067 H HE2  B LYS   A 1 102 ? 24.340 4.565   -10.718 0.32 37.74 ?  102 LYS   A HE2  1 
ATOM   2068 H HE3  A LYS   A 1 102 ? 24.251 3.538   -9.261  0.68 37.70 ?  102 LYS   A HE3  1 
ATOM   2069 H HE3  B LYS   A 1 102 ? 24.154 3.609   -9.460  0.32 37.74 ?  102 LYS   A HE3  1 
ATOM   2070 H HZ1  A LYS   A 1 102 ? 26.126 4.189   -8.145  0.68 37.95 ?  102 LYS   A HZ1  1 
ATOM   2071 H HZ1  B LYS   A 1 102 ? 25.843 5.083   -9.097  0.32 38.31 ?  102 LYS   A HZ1  1 
ATOM   2072 H HZ2  A LYS   A 1 102 ? 26.165 2.749   -8.304  0.68 37.95 ?  102 LYS   A HZ2  1 
ATOM   2073 H HZ2  B LYS   A 1 102 ? 26.398 3.744   -9.116  0.32 38.31 ?  102 LYS   A HZ2  1 
ATOM   2074 H HZ3  A LYS   A 1 102 ? 26.988 3.594   -9.146  0.68 37.95 ?  102 LYS   A HZ3  1 
ATOM   2075 H HZ3  B LYS   A 1 102 ? 26.567 4.615   -10.262 0.32 38.31 ?  102 LYS   A HZ3  1 
ATOM   2076 N N    A GLY   A 1 103 ? 22.523 -0.746  -14.992 0.68 28.58 ?  103 GLY   A N    1 
ATOM   2077 N N    B GLY   A 1 103 ? 22.409 -0.915  -15.222 0.32 27.28 ?  103 GLY   A N    1 
ATOM   2078 C CA   A GLY   A 1 103 ? 22.798 -1.807  -15.946 0.68 28.31 ?  103 GLY   A CA   1 
ATOM   2079 C CA   B GLY   A 1 103 ? 22.630 -2.088  -16.040 0.32 27.33 ?  103 GLY   A CA   1 
ATOM   2080 C C    A GLY   A 1 103 ? 23.602 -2.973  -15.410 0.68 28.13 ?  103 GLY   A C    1 
ATOM   2081 C C    B GLY   A 1 103 ? 23.500 -3.153  -15.415 0.32 27.09 ?  103 GLY   A C    1 
ATOM   2082 O O    A GLY   A 1 103 ? 24.165 -3.734  -16.204 0.68 29.35 ?  103 GLY   A O    1 
ATOM   2083 O O    B GLY   A 1 103 ? 24.020 -4.010  -16.134 0.32 27.60 ?  103 GLY   A O    1 
ATOM   2084 H H    A GLY   A 1 103 ? 21.792 -0.859  -14.553 0.68 34.28 ?  103 GLY   A H    1 
ATOM   2085 H H    B GLY   A 1 103 ? 21.605 -0.834  -14.929 0.32 32.71 ?  103 GLY   A H    1 
ATOM   2086 H HA2  A GLY   A 1 103 ? 21.955 -2.149  -16.289 0.68 33.95 ?  103 GLY   A HA2  1 
ATOM   2087 H HA2  B GLY   A 1 103 ? 21.775 -2.495  -16.245 0.32 32.77 ?  103 GLY   A HA2  1 
ATOM   2088 H HA3  A GLY   A 1 103 ? 23.293 -1.438  -16.694 0.68 33.95 ?  103 GLY   A HA3  1 
ATOM   2089 H HA3  B GLY   A 1 103 ? 23.037 -1.810  -16.877 0.32 32.77 ?  103 GLY   A HA3  1 
ATOM   2090 N N    . GLU   A 1 104 ? 23.668 -3.143  -14.095 1.00 25.82 ?  104 GLU   A N    1 
ATOM   2091 C CA   . GLU   A 1 104 ? 24.525 -4.138  -13.464 1.00 23.40 ?  104 GLU   A CA   1 
ATOM   2092 C C    . GLU   A 1 104 ? 23.839 -5.503  -13.378 1.00 23.53 ?  104 GLU   A C    1 
ATOM   2093 O O    . GLU   A 1 104 ? 22.619 -5.606  -13.225 1.00 23.91 ?  104 GLU   A O    1 
ATOM   2094 C CB   . GLU   A 1 104 ? 25.006 -3.632  -12.100 1.00 21.36 ?  104 GLU   A CB   1 
ATOM   2095 C CG   . GLU   A 1 104 ? 25.920 -2.410  -12.263 1.00 20.88 ?  104 GLU   A CG   1 
ATOM   2096 C CD   . GLU   A 1 104 ? 26.240 -1.639  -10.988 1.00 20.07 ?  104 GLU   A CD   1 
ATOM   2097 O OE1  . GLU   A 1 104 ? 25.671 -1.924  -9.919  1.00 18.72 ?  104 GLU   A OE1  1 
ATOM   2098 O OE2  . GLU   A 1 104 ? 27.075 -0.707  -11.081 1.00 21.51 -1 104 GLU   A OE2  1 
ATOM   2099 H H    A GLU   A 1 104 ? 23.225 -2.665  -13.534 0.68 30.97 ?  104 GLU   A H    1 
ATOM   2100 H H    B GLU   A 1 104 ? 23.291 -2.591  -13.554 0.32 30.97 ?  104 GLU   A H    1 
ATOM   2101 H HA   . GLU   A 1 104 ? 25.310 -4.248  -14.022 1.00 28.06 ?  104 GLU   A HA   1 
ATOM   2102 H HB2  . GLU   A 1 104 ? 24.237 -3.380  -11.565 1.00 25.60 ?  104 GLU   A HB2  1 
ATOM   2103 H HB3  . GLU   A 1 104 ? 25.506 -4.339  -11.660 1.00 25.60 ?  104 GLU   A HB3  1 
ATOM   2104 H HG2  . GLU   A 1 104 ? 26.760 -2.707  -12.638 1.00 25.03 ?  104 GLU   A HG2  1 
ATOM   2105 H HG3  . GLU   A 1 104 ? 25.491 -1.788  -12.869 1.00 25.03 ?  104 GLU   A HG3  1 
ATOM   2106 N N    A ASP   A 1 105 ? 24.654 -6.553  -13.460 0.68 24.12 ?  105 ASP   A N    1 
ATOM   2107 N N    B ASP   A 1 105 ? 24.651 -6.554  -13.488 0.32 24.78 ?  105 ASP   A N    1 
ATOM   2108 C CA   A ASP   A 1 105 ? 24.159 -7.920  -13.590 0.68 24.91 ?  105 ASP   A CA   1 
ATOM   2109 C CA   B ASP   A 1 105 ? 24.146 -7.920  -13.566 0.32 26.01 ?  105 ASP   A CA   1 
ATOM   2110 C C    A ASP   A 1 105 ? 23.456 -8.358  -12.307 0.68 22.50 ?  105 ASP   A C    1 
ATOM   2111 C C    B ASP   A 1 105 ? 23.423 -8.293  -12.278 0.32 25.37 ?  105 ASP   A C    1 
ATOM   2112 O O    A ASP   A 1 105 ? 24.080 -8.437  -11.245 0.68 20.10 ?  105 ASP   A O    1 
ATOM   2113 O O    B ASP   A 1 105 ? 24.006 -8.246  -11.191 0.32 25.09 ?  105 ASP   A O    1 
ATOM   2114 C CB   A ASP   A 1 105 ? 25.340 -8.841  -13.892 0.68 28.01 ?  105 ASP   A CB   1 
ATOM   2115 C CB   B ASP   A 1 105 ? 25.323 -8.866  -13.807 0.32 27.64 ?  105 ASP   A CB   1 
ATOM   2116 C CG   A ASP   A 1 105 ? 24.916 -10.255 -14.211 0.68 30.71 ?  105 ASP   A CG   1 
ATOM   2117 C CG   B ASP   A 1 105 ? 24.908 -10.325 -13.858 0.32 29.03 ?  105 ASP   A CG   1 
ATOM   2118 O OD1  A ASP   A 1 105 ? 23.698 -10.496 -14.326 0.68 31.38 ?  105 ASP   A OD1  1 
ATOM   2119 O OD1  B ASP   A 1 105 ? 23.696 -10.606 -13.972 0.32 29.23 ?  105 ASP   A OD1  1 
ATOM   2120 O OD2  A ASP   A 1 105 ? 25.809 -11.121 -14.351 0.68 32.10 -1 105 ASP   A OD2  1 
ATOM   2121 O OD2  B ASP   A 1 105 ? 25.803 -11.193 -13.775 0.32 29.87 -1 105 ASP   A OD2  1 
ATOM   2122 H H    A ASP   A 1 105 ? 25.512 -6.497  -13.439 0.68 28.92 ?  105 ASP   A H    1 
ATOM   2123 H H    B ASP   A 1 105 ? 25.509 -6.498  -13.514 0.32 29.72 ?  105 ASP   A H    1 
ATOM   2124 H HA   A ASP   A 1 105 ? 23.528 -7.975  -14.322 0.68 29.86 ?  105 ASP   A HA   1 
ATOM   2125 H HA   B ASP   A 1 105 ? 23.528 -8.001  -14.310 0.32 31.19 ?  105 ASP   A HA   1 
ATOM   2126 H HB2  A ASP   A 1 105 ? 25.819 -8.497  -14.663 0.68 33.58 ?  105 ASP   A HB2  1 
ATOM   2127 H HB2  B ASP   A 1 105 ? 25.746 -8.638  -14.652 0.32 33.14 ?  105 ASP   A HB2  1 
ATOM   2128 H HB3  A ASP   A 1 105 ? 25.927 -8.868  -13.121 0.68 33.58 ?  105 ASP   A HB3  1 
ATOM   2129 H HB3  B ASP   A 1 105 ? 25.960 -8.770  -13.083 0.32 33.14 ?  105 ASP   A HB3  1 
ATOM   2130 N N    A ILE   A 1 106 ? 22.159 -8.662  -12.408 0.68 22.37 ?  106 ILE   A N    1 
ATOM   2131 N N    B ILE   A 1 106 ? 22.148 -8.672  -12.403 0.32 24.98 ?  106 ILE   A N    1 
ATOM   2132 C CA   A ILE   A 1 106 ? 21.388 -9.058  -11.235 0.68 21.93 ?  106 ILE   A CA   1 
ATOM   2133 C CA   B ILE   A 1 106 ? 21.368 -9.056  -11.232 0.32 24.49 ?  106 ILE   A CA   1 
ATOM   2134 C C    A ILE   A 1 106 ? 21.912 -10.347 -10.625 0.68 21.07 ?  106 ILE   A C    1 
ATOM   2135 C C    B ILE   A 1 106 ? 21.901 -10.334 -10.599 0.32 23.78 ?  106 ILE   A C    1 
ATOM   2136 O O    A ILE   A 1 106 ? 21.694 -10.593 -9.436  0.68 19.91 ?  106 ILE   A O    1 
ATOM   2137 O O    B ILE   A 1 106 ? 21.692 -10.560 -9.402  0.32 23.40 ?  106 ILE   A O    1 
ATOM   2138 C CB   A ILE   A 1 106 ? 19.880 -9.139  -11.571 0.68 23.46 ?  106 ILE   A CB   1 
ATOM   2139 C CB   B ILE   A 1 106 ? 19.868 -9.162  -11.578 0.32 25.06 ?  106 ILE   A CB   1 
ATOM   2140 C CG1  A ILE   A 1 106 ? 19.036 -9.208  -10.293 0.68 24.42 ?  106 ILE   A CG1  1 
ATOM   2141 C CG1  B ILE   A 1 106 ? 19.019 -9.268  -10.307 0.32 25.39 ?  106 ILE   A CG1  1 
ATOM   2142 C CG2  A ILE   A 1 106 ? 19.587 -10.340 -12.455 0.68 23.92 ?  106 ILE   A CG2  1 
ATOM   2143 C CG2  B ILE   A 1 106 ? 19.606 -10.363 -12.467 0.32 25.26 ?  106 ILE   A CG2  1 
ATOM   2144 C CD1  A ILE   A 1 106 ? 19.143 -7.979  -9.414  0.68 25.11 ?  106 ILE   A CD1  1 
ATOM   2145 C CD1  B ILE   A 1 106 ? 19.091 -8.050  -9.411  0.32 25.57 ?  106 ILE   A CD1  1 
ATOM   2146 H H    A ILE   A 1 106 ? 21.712 -8.642  -13.137 0.68 26.82 ?  106 ILE   A H    1 
ATOM   2147 H H    B ILE   A 1 106 ? 21.720 -8.712  -13.145 0.32 29.95 ?  106 ILE   A H    1 
ATOM   2148 H HA   A ILE   A 1 106 ? 21.500 -8.378  -10.562 0.68 26.29 ?  106 ILE   A HA   1 
ATOM   2149 H HA   B ILE   A 1 106 ? 21.463 -8.358  -10.571 0.32 29.36 ?  106 ILE   A HA   1 
ATOM   2150 H HB   A ILE   A 1 106 ? 19.635 -8.336  -12.055 0.68 28.13 ?  106 ILE   A HB   1 
ATOM   2151 H HB   B ILE   A 1 106 ? 19.604 -8.360  -12.057 0.32 30.05 ?  106 ILE   A HB   1 
ATOM   2152 H HG12 A ILE   A 1 106 ? 18.104 -9.310  -10.540 0.68 29.28 ?  106 ILE   A HG12 1 
ATOM   2153 H HG12 B ILE   A 1 106 ? 18.090 -9.387  -10.562 0.32 30.45 ?  106 ILE   A HG12 1 
ATOM   2154 H HG13 A ILE   A 1 106 ? 19.320 -9.972  -9.768  0.68 29.28 ?  106 ILE   A HG13 1 
ATOM   2155 H HG13 B ILE   A 1 106 ? 19.315 -10.033 -9.791  0.32 30.45 ?  106 ILE   A HG13 1 
ATOM   2156 H HG21 A ILE   A 1 106 ? 18.688 -10.257 -12.808 0.68 28.68 ?  106 ILE   A HG21 1 
ATOM   2157 H HG21 B ILE   A 1 106 ? 18.708 -10.296 -12.826 0.32 30.29 ?  106 ILE   A HG21 1 
ATOM   2158 H HG22 A ILE   A 1 106 ? 20.228 -10.358 -13.181 0.68 28.68 ?  106 ILE   A HG22 1 
ATOM   2159 H HG22 B ILE   A 1 106 ? 20.253 -10.365 -13.187 0.32 30.29 ?  106 ILE   A HG22 1 
ATOM   2160 H HG23 A ILE   A 1 106 ? 19.662 -11.149 -11.926 0.68 28.68 ?  106 ILE   A HG23 1 
ATOM   2161 H HG23 B ILE   A 1 106 ? 19.693 -11.171 -11.939 0.32 30.29 ?  106 ILE   A HG23 1 
ATOM   2162 H HD11 A ILE   A 1 106 ? 18.424 -7.991  -8.765  0.68 30.11 ?  106 ILE   A HD11 1 
ATOM   2163 H HD11 B ILE   A 1 106 ? 18.375 -8.096  -8.759  0.32 30.67 ?  106 ILE   A HD11 1 
ATOM   2164 H HD12 A ILE   A 1 106 ? 20.000 -7.988  -8.957  0.68 30.11 ?  106 ILE   A HD12 1 
ATOM   2165 H HD12 B ILE   A 1 106 ? 19.949 -8.040  -8.958  0.32 30.67 ?  106 ILE   A HD12 1 
ATOM   2166 H HD13 A ILE   A 1 106 ? 19.074 -7.186  -9.970  0.68 30.11 ?  106 ILE   A HD13 1 
ATOM   2167 H HD13 B ILE   A 1 106 ? 18.993 -7.252  -9.954  0.32 30.67 ?  106 ILE   A HD13 1 
ATOM   2168 N N    A GLN   A 1 107 ? 22.618 -11.172 -11.409 0.68 22.19 ?  107 GLN   A N    1 
ATOM   2169 N N    B GLN   A 1 107 ? 22.596 -11.176 -11.370 0.32 23.69 ?  107 GLN   A N    1 
ATOM   2170 C CA   A GLN   A 1 107 ? 23.244 -12.371 -10.864 0.68 24.64 ?  107 GLN   A CA   1 
ATOM   2171 C CA   B GLN   A 1 107 ? 23.200 -12.375 -10.800 0.32 24.01 ?  107 GLN   A CA   1 
ATOM   2172 C C    A GLN   A 1 107 ? 24.215 -12.036 -9.740  0.68 22.12 ?  107 GLN   A C    1 
ATOM   2173 C C    B GLN   A 1 107 ? 24.224 -12.039 -9.725  0.32 21.56 ?  107 GLN   A C    1 
ATOM   2174 O O    A GLN   A 1 107 ? 24.448 -12.873 -8.861  0.68 23.29 ?  107 GLN   A O    1 
ATOM   2175 O O    B GLN   A 1 107 ? 24.519 -12.888 -8.877  0.32 22.26 ?  107 GLN   A O    1 
ATOM   2176 C CB   A GLN   A 1 107 ? 23.965 -13.138 -11.982 0.68 29.14 ?  107 GLN   A CB   1 
ATOM   2177 C CB   B GLN   A 1 107 ? 23.838 -13.223 -11.905 0.32 26.55 ?  107 GLN   A CB   1 
ATOM   2178 C CG   A GLN   A 1 107 ? 23.119 -13.358 -13.234 0.68 33.92 ?  107 GLN   A CG   1 
ATOM   2179 C CG   B GLN   A 1 107 ? 22.839 -13.739 -12.930 0.32 29.06 ?  107 GLN   A CG   1 
ATOM   2180 C CD   A GLN   A 1 107 ? 21.838 -14.116 -12.951 0.68 37.60 ?  107 GLN   A CD   1 
ATOM   2181 C CD   B GLN   A 1 107 ? 21.676 -14.472 -12.290 0.32 31.30 ?  107 GLN   A CD   1 
ATOM   2182 O OE1  A GLN   A 1 107 ? 21.857 -15.183 -12.337 0.68 38.96 ?  107 GLN   A OE1  1 
ATOM   2183 O OE1  B GLN   A 1 107 ? 21.862 -15.275 -11.375 0.32 32.09 ?  107 GLN   A OE1  1 
ATOM   2184 N NE2  A GLN   A 1 107 ? 20.714 -13.564 -13.395 0.68 38.79 ?  107 GLN   A NE2  1 
ATOM   2185 N NE2  B GLN   A 1 107 ? 20.467 -14.187 -12.759 0.32 31.98 ?  107 GLN   A NE2  1 
ATOM   2186 H H    A GLN   A 1 107 ? 22.752 -11.054 -12.249 0.68 26.60 ?  107 GLN   A H    1 
ATOM   2187 H H    B GLN   A 1 107 ? 22.730 -11.074 -12.214 0.32 28.40 ?  107 GLN   A H    1 
ATOM   2188 H HA   A GLN   A 1 107 ? 22.565 -12.957 -10.501 0.68 29.55 ?  107 GLN   A HA   1 
ATOM   2189 H HA   B GLN   A 1 107 ? 22.508 -12.903 -10.381 0.32 28.79 ?  107 GLN   A HA   1 
ATOM   2190 H HB2  A GLN   A 1 107 ? 24.755 -12.643 -12.248 0.68 34.95 ?  107 GLN   A HB2  1 
ATOM   2191 H HB2  B GLN   A 1 107 ? 24.494 -12.686 -12.378 0.32 31.84 ?  107 GLN   A HB2  1 
ATOM   2192 H HB3  A GLN   A 1 107 ? 24.223 -14.014 -11.652 0.68 34.95 ?  107 GLN   A HB3  1 
ATOM   2193 H HB3  B GLN   A 1 107 ? 24.271 -13.992 -11.503 0.32 31.84 ?  107 GLN   A HB3  1 
ATOM   2194 H HG2  A GLN   A 1 107 ? 22.878 -12.500 -13.616 0.68 40.68 ?  107 GLN   A HG2  1 
ATOM   2195 H HG2  B GLN   A 1 107 ? 22.484 -12.987 -13.431 0.32 34.85 ?  107 GLN   A HG2  1 
ATOM   2196 H HG3  A GLN   A 1 107 ? 23.634 -13.869 -13.876 0.68 40.68 ?  107 GLN   A HG3  1 
ATOM   2197 H HG3  B GLN   A 1 107 ? 23.289 -14.355 -13.529 0.32 34.85 ?  107 GLN   A HG3  1 
ATOM   2198 H HE21 A GLN   A 1 107 ? 20.738 -12.817 -13.820 0.68 46.53 ?  107 GLN   A HE21 1 
ATOM   2199 H HE21 B GLN   A 1 107 ? 20.377 -13.617 -13.398 0.32 38.36 ?  107 GLN   A HE21 1 
ATOM   2200 H HE22 A GLN   A 1 107 ? 19.961 -13.957 -13.259 0.68 46.53 ?  107 GLN   A HE22 1 
ATOM   2201 H HE22 B GLN   A 1 107 ? 19.774 -14.572 -12.426 0.32 38.36 ?  107 GLN   A HE22 1 
ATOM   2202 N N    . LEU   A 1 108 ? 24.757 -10.816 -9.727  1.00 18.50 ?  108 LEU   A N    1 
ATOM   2203 C CA   . LEU   A 1 108 ? 25.673 -10.399 -8.676  1.00 15.57 ?  108 LEU   A CA   1 
ATOM   2204 C C    . LEU   A 1 108 ? 24.975 -10.232 -7.337  1.00 13.52 ?  108 LEU   A C    1 
ATOM   2205 O O    . LEU   A 1 108 ? 25.657 -10.075 -6.321  1.00 14.29 ?  108 LEU   A O    1 
ATOM   2206 C CB   . LEU   A 1 108 ? 26.391 -9.104  -9.072  1.00 15.60 ?  108 LEU   A CB   1 
ATOM   2207 C CG   . LEU   A 1 108 ? 27.400 -9.293  -10.207 1.00 17.50 ?  108 LEU   A CG   1 
ATOM   2208 C CD1  . LEU   A 1 108 ? 27.895 -7.963  -10.752 1.00 18.30 ?  108 LEU   A CD1  1 
ATOM   2209 C CD2  . LEU   A 1 108 ? 28.578 -10.137 -9.745  1.00 19.62 ?  108 LEU   A CD2  1 
ATOM   2210 H H    A LEU   A 1 108 ? 24.599 -10.212 -10.312 0.68 22.17 ?  108 LEU   A H    1 
ATOM   2211 H H    B LEU   A 1 108 ? 24.605 -10.219 -10.322 0.32 22.17 ?  108 LEU   A H    1 
ATOM   2212 H HA   . LEU   A 1 108 ? 26.343 -11.088 -8.559  1.00 18.66 ?  108 LEU   A HA   1 
ATOM   2213 H HB2  . LEU   A 1 108 ? 25.730 -8.457  -9.367  1.00 18.69 ?  108 LEU   A HB2  1 
ATOM   2214 H HB3  . LEU   A 1 108 ? 26.867 -8.761  -8.302  1.00 18.69 ?  108 LEU   A HB3  1 
ATOM   2215 H HG   . LEU   A 1 108 ? 26.968 -9.766  -10.934 1.00 20.98 ?  108 LEU   A HG   1 
ATOM   2216 H HD11 . LEU   A 1 108 ? 28.510 -8.131  -11.487 1.00 21.93 ?  108 LEU   A HD11 1 
ATOM   2217 H HD12 . LEU   A 1 108 ? 27.138 -7.447  -11.068 1.00 21.93 ?  108 LEU   A HD12 1 
ATOM   2218 H HD13 . LEU   A 1 108 ? 28.354 -7.481  -10.046 1.00 21.93 ?  108 LEU   A HD13 1 
ATOM   2219 H HD21 . LEU   A 1 108 ? 29.285 -10.077 -10.403 1.00 23.52 ?  108 LEU   A HD21 1 
ATOM   2220 H HD22 . LEU   A 1 108 ? 28.889 -9.798  -8.891  1.00 23.52 ?  108 LEU   A HD22 1 
ATOM   2221 H HD23 . LEU   A 1 108 ? 28.288 -11.057 -9.649  1.00 23.52 ?  108 LEU   A HD23 1 
ATOM   2222 N N    . LEU   A 1 109 ? 23.641 -10.290 -7.301  1.00 12.88 ?  109 LEU   A N    1 
ATOM   2223 C CA   . LEU   A 1 109 ? 22.942 -10.167 -6.029  1.00 12.15 ?  109 LEU   A CA   1 
ATOM   2224 C C    . LEU   A 1 109 ? 23.287 -11.320 -5.094  1.00 11.47 ?  109 LEU   A C    1 
ATOM   2225 O O    . LEU   A 1 109 ? 23.422 -11.125 -3.881  1.00 12.08 ?  109 LEU   A O    1 
ATOM   2226 C CB   . LEU   A 1 109 ? 21.436 -10.085 -6.281  1.00 13.30 ?  109 LEU   A CB   1 
ATOM   2227 C CG   . LEU   A 1 109 ? 20.543 -9.801  -5.075  1.00 13.71 ?  109 LEU   A CG   1 
ATOM   2228 C CD1  . LEU   A 1 109 ? 20.996 -8.547  -4.356  1.00 13.41 ?  109 LEU   A CD1  1 
ATOM   2229 C CD2  . LEU   A 1 109 ? 19.087 -9.667  -5.510  1.00 14.70 ?  109 LEU   A CD2  1 
ATOM   2230 H H    . LEU   A 1 109 ? 23.127 -10.402 -7.982  1.00 15.44 ?  109 LEU   A H    1 
ATOM   2231 H HA   . LEU   A 1 109 ? 23.223 -9.343  -5.600  1.00 14.55 ?  109 LEU   A HA   1 
ATOM   2232 H HB2  . LEU   A 1 109 ? 21.279 -9.376  -6.923  1.00 15.94 ?  109 LEU   A HB2  1 
ATOM   2233 H HB3  . LEU   A 1 109 ? 21.147 -10.928 -6.656  1.00 15.94 ?  109 LEU   A HB3  1 
ATOM   2234 H HG   . LEU   A 1 109 ? 20.599 -10.541 -4.454  1.00 16.43 ?  109 LEU   A HG   1 
ATOM   2235 H HD11 . LEU   A 1 109 ? 20.321 -8.281  -3.716  1.00 16.07 ?  109 LEU   A HD11 1 
ATOM   2236 H HD12 . LEU   A 1 109 ? 21.834 -8.726  -3.902  1.00 16.07 ?  109 LEU   A HD12 1 
ATOM   2237 H HD13 . LEU   A 1 109 ? 21.123 -7.835  -5.011  1.00 16.07 ?  109 LEU   A HD13 1 
ATOM   2238 H HD21 . LEU   A 1 109 ? 18.554 -9.377  -4.752  1.00 17.62 ?  109 LEU   A HD21 1 
ATOM   2239 H HD22 . LEU   A 1 109 ? 19.025 -9.014  -6.224  1.00 17.62 ?  109 LEU   A HD22 1 
ATOM   2240 H HD23 . LEU   A 1 109 ? 18.768 -10.530 -5.824  1.00 17.62 ?  109 LEU   A HD23 1 
ATOM   2241 N N    . LYS   A 1 110 ? 23.434 -12.535 -5.633  1.00 11.67 ?  110 LYS   A N    1 
ATOM   2242 C CA   . LYS   A 1 110 ? 23.812 -13.659 -4.781  1.00 11.80 ?  110 LYS   A CA   1 
ATOM   2243 C C    . LYS   A 1 110 ? 25.195 -13.438 -4.178  1.00 11.25 ?  110 LYS   A C    1 
ATOM   2244 O O    . LYS   A 1 110 ? 25.394 -13.641 -2.978  1.00 11.54 ?  110 LYS   A O    1 
ATOM   2245 C CB   . LYS   A 1 110 ? 23.735 -14.985 -5.544  1.00 12.81 ?  110 LYS   A CB   1 
ATOM   2246 C CG   . LYS   A 1 110 ? 23.944 -16.197 -4.638  1.00 12.92 ?  110 LYS   A CG   1 
ATOM   2247 C CD   . LYS   A 1 110 ? 23.701 -17.514 -5.354  1.00 13.93 ?  110 LYS   A CD   1 
ATOM   2248 C CE   . LYS   A 1 110 ? 23.809 -18.701 -4.412  1.00 14.76 ?  110 LYS   A CE   1 
ATOM   2249 N NZ   . LYS   A 1 110 ? 22.628 -18.840 -3.522  1.00 14.93 ?  110 LYS   A NZ   1 
ATOM   2250 H H    . LYS   A 1 110 ? 23.318 -12.727 -6.461  1.00 13.98 ?  110 LYS   A H    1 
ATOM   2251 H HA   . LYS   A 1 110 ? 23.176 -13.714 -4.047  1.00 14.13 ?  110 LYS   A HA   1 
ATOM   2252 H HB2  . LYS   A 1 110 ? 22.858 -15.063 -5.953  1.00 15.35 ?  110 LYS   A HB2  1 
ATOM   2253 H HB3  . LYS   A 1 110 ? 24.423 -14.996 -6.224  1.00 15.35 ?  110 LYS   A HB3  1 
ATOM   2254 H HG2  . LYS   A 1 110 ? 24.856 -16.195 -4.312  1.00 15.49 ?  110 LYS   A HG2  1 
ATOM   2255 H HG3  . LYS   A 1 110 ? 23.325 -16.143 -3.892  1.00 15.49 ?  110 LYS   A HG3  1 
ATOM   2256 H HD2  . LYS   A 1 110 ? 22.810 -17.509 -5.735  1.00 16.69 ?  110 LYS   A HD2  1 
ATOM   2257 H HD3  . LYS   A 1 110 ? 24.365 -17.619 -6.054  1.00 16.69 ?  110 LYS   A HD3  1 
ATOM   2258 H HE2  . LYS   A 1 110 ? 23.893 -19.514 -4.933  1.00 17.68 ?  110 LYS   A HE2  1 
ATOM   2259 H HE3  . LYS   A 1 110 ? 24.594 -18.588 -3.848  1.00 17.68 ?  110 LYS   A HE3  1 
ATOM   2260 H HZ1  . LYS   A 1 110 ? 22.722 -19.541 -2.988  1.00 17.90 ?  110 LYS   A HZ1  1 
ATOM   2261 H HZ2  . LYS   A 1 110 ? 22.528 -18.106 -3.026  1.00 17.90 ?  110 LYS   A HZ2  1 
ATOM   2262 H HZ3  . LYS   A 1 110 ? 21.889 -18.950 -4.015  1.00 17.90 ?  110 LYS   A HZ3  1 
ATOM   2263 N N    . SER   A 1 111 ? 26.156 -12.992 -4.991  1.00 11.43 ?  111 SER   A N    1 
ATOM   2264 C CA   . SER   A 1 111 ? 27.485 -12.685 -4.469  1.00 11.47 ?  111 SER   A CA   1 
ATOM   2265 C C    . SER   A 1 111 ? 27.419 -11.638 -3.365  1.00 11.15 ?  111 SER   A C    1 
ATOM   2266 O O    . SER   A 1 111 ? 28.117 -11.741 -2.352  1.00 11.97 ?  111 SER   A O    1 
ATOM   2267 C CB   . SER   A 1 111 ? 28.390 -12.193 -5.598  1.00 13.07 ?  111 SER   A CB   1 
ATOM   2268 O OG   . SER   A 1 111 ? 28.478 -13.165 -6.629  1.00 15.26 ?  111 SER   A OG   1 
ATOM   2269 H H    . SER   A 1 111 ? 26.058 -12.863 -5.834  1.00 13.69 ?  111 SER   A H    1 
ATOM   2270 H HA   . SER   A 1 111 ? 27.874 -13.494 -4.097  1.00 13.74 ?  111 SER   A HA   1 
ATOM   2271 H HB2  . SER   A 1 111 ? 28.015 -11.383 -5.971  1.00 15.67 ?  111 SER   A HB2  1 
ATOM   2272 H HB3  . SER   A 1 111 ? 29.273 -12.016 -5.236  1.00 15.67 ?  111 SER   A HB3  1 
ATOM   2273 H HG   . SER   A 1 111 ? 29.002 -12.884 -7.237  1.00 18.29 ?  111 SER   A HG   1 
ATOM   2274 N N    . ALA   A 1 112 ? 26.572 -10.620 -3.543  1.00 11.35 ?  112 ALA   A N    1 
ATOM   2275 C CA   . ALA   A 1 112 ? 26.427 -9.583  -2.524  1.00 10.99 ?  112 ALA   A CA   1 
ATOM   2276 C C    . ALA   A 1 112 ? 25.948 -10.181 -1.203  1.00 11.05 ?  112 ALA   A C    1 
ATOM   2277 O O    . ALA   A 1 112 ? 26.496 -9.884  -0.132  1.00 11.41 ?  112 ALA   A O    1 
ATOM   2278 C CB   . ALA   A 1 112 ? 25.468 -8.498  -3.022  1.00 11.60 ?  112 ALA   A CB   1 
ATOM   2279 H H    . ALA   A 1 112 ? 26.079 -10.506 -4.238  1.00 13.59 ?  112 ALA   A H    1 
ATOM   2280 H HA   . ALA   A 1 112 ? 27.286 -9.162  -2.370  1.00 13.16 ?  112 ALA   A HA   1 
ATOM   2281 H HB1  . ALA   A 1 112 ? 25.391 -7.800  -2.345  1.00 13.89 ?  112 ALA   A HB1  1 
ATOM   2282 H HB2  . ALA   A 1 112 ? 25.809 -8.116  -3.845  1.00 13.89 ?  112 ALA   A HB2  1 
ATOM   2283 H HB3  . ALA   A 1 112 ? 24.591 -8.890  -3.180  1.00 13.89 ?  112 ALA   A HB3  1 
ATOM   2284 N N    . TYR   A 1 113 ? 24.921 -11.037 -1.257  1.00 10.99 ?  113 TYR   A N    1 
ATOM   2285 C CA   . TYR   A 1 113 ? 24.401 -11.638 -0.031  1.00 10.76 ?  113 TYR   A CA   1 
ATOM   2286 C C    . TYR   A 1 113 ? 25.399 -12.592 0.619   1.00 10.70 ?  113 TYR   A C    1 
ATOM   2287 O O    . TYR   A 1 113 ? 25.361 -12.775 1.838   1.00 11.31 ?  113 TYR   A O    1 
ATOM   2288 C CB   . TYR   A 1 113 ? 23.092 -12.378 -0.307  1.00 11.43 ?  113 TYR   A CB   1 
ATOM   2289 C CG   . TYR   A 1 113 ? 21.870 -11.490 -0.213  1.00 10.95 ?  113 TYR   A CG   1 
ATOM   2290 C CD1  . TYR   A 1 113 ? 21.512 -10.906 0.991   1.00 11.39 ?  113 TYR   A CD1  1 
ATOM   2291 C CD2  . TYR   A 1 113 ? 21.059 -11.266 -1.316  1.00 11.36 ?  113 TYR   A CD2  1 
ATOM   2292 C CE1  . TYR   A 1 113 ? 20.379 -10.109 1.094   1.00 11.86 ?  113 TYR   A CE1  1 
ATOM   2293 C CE2  . TYR   A 1 113 ? 19.912 -10.466 -1.223  1.00 11.77 ?  113 TYR   A CE2  1 
ATOM   2294 C CZ   . TYR   A 1 113 ? 19.585 -9.902  -0.015  1.00 11.60 ?  113 TYR   A CZ   1 
ATOM   2295 O OH   . TYR   A 1 113 ? 18.456 -9.115  0.103   1.00 12.65 ?  113 TYR   A OH   1 
ATOM   2296 H H    . TYR   A 1 113 ? 24.519 -11.278 -1.979  1.00 13.17 ?  113 TYR   A H    1 
ATOM   2297 H HA   . TYR   A 1 113 ? 24.218 -10.933 0.604   1.00 12.89 ?  113 TYR   A HA   1 
ATOM   2298 H HB2  . TYR   A 1 113 ? 23.117 -12.743 -1.203  1.00 13.70 ?  113 TYR   A HB2  1 
ATOM   2299 H HB3  . TYR   A 1 113 ? 22.993 -13.091 0.341   1.00 13.70 ?  113 TYR   A HB3  1 
ATOM   2300 H HD1  . TYR   A 1 113 ? 22.045 -11.052 1.746   1.00 13.64 ?  113 TYR   A HD1  1 
ATOM   2301 H HD2  . TYR   A 1 113 ? 21.278 -11.658 -2.125  1.00 13.61 ?  113 TYR   A HD2  1 
ATOM   2302 H HE1  . TYR   A 1 113 ? 20.156 -9.725  1.912   1.00 14.21 ?  113 TYR   A HE1  1 
ATOM   2303 H HE2  . TYR   A 1 113 ? 19.375 -10.324 -1.966  1.00 14.10 ?  113 TYR   A HE2  1 
ATOM   2304 H HH   . TYR   A 1 113 ? 18.065 -9.069  -0.644  1.00 15.16 ?  113 TYR   A HH   1 
ATOM   2305 N N    . GLU   A 1 114 ? 26.300 -13.206 -0.164  1.00 10.79 ?  114 GLU   A N    1 
ATOM   2306 C CA   . GLU   A 1 114 ? 27.298 -14.098 0.431   1.00 11.10 ?  114 GLU   A CA   1 
ATOM   2307 C C    . GLU   A 1 114 ? 28.146 -13.389 1.481   1.00 10.76 ?  114 GLU   A C    1 
ATOM   2308 O O    . GLU   A 1 114 ? 28.621 -14.026 2.433   1.00 11.39 ?  114 GLU   A O    1 
ATOM   2309 C CB   . GLU   A 1 114 ? 28.170 -14.738 -0.655  1.00 11.04 ?  114 GLU   A CB   1 
ATOM   2310 C CG   . GLU   A 1 114 ? 27.406 -15.784 -1.442  1.00 11.62 ?  114 GLU   A CG   1 
ATOM   2311 C CD   . GLU   A 1 114 ? 28.122 -16.321 -2.674  1.00 12.18 ?  114 GLU   A CD   1 
ATOM   2312 O OE1  . GLU   A 1 114 ? 29.078 -15.688 -3.164  1.00 12.41 ?  114 GLU   A OE1  1 
ATOM   2313 O OE2  . GLU   A 1 114 ? 27.689 -17.385 -3.175  1.00 13.26 -1 114 GLU   A OE2  1 
ATOM   2314 H H    . GLU   A 1 114 ? 26.350 -13.123 -1.027  1.00 12.92 ?  114 GLU   A H    1 
ATOM   2315 H HA   . GLU   A 1 114 ? 26.831 -14.814 0.873   1.00 13.30 ?  114 GLU   A HA   1 
ATOM   2316 H HB2  . GLU   A 1 114 ? 28.468 -14.053 -1.281  1.00 13.23 ?  114 GLU   A HB2  1 
ATOM   2317 H HB3  . GLU   A 1 114 ? 28.934 -15.169 -0.246  1.00 13.23 ?  114 GLU   A HB3  1 
ATOM   2318 H HG2  . GLU   A 1 114 ? 27.231 -16.540 -0.862  1.00 13.93 ?  114 GLU   A HG2  1 
ATOM   2319 H HG3  . GLU   A 1 114 ? 26.564 -15.399 -1.737  1.00 13.93 ?  114 GLU   A HG3  1 
ATOM   2320 N N    . ASN   A 1 115 ? 28.332 -12.073 1.348   1.00 10.50 ?  115 ASN   A N    1 
ATOM   2321 C CA   . ASN   A 1 115 ? 29.097 -11.344 2.355   1.00 10.85 ?  115 ASN   A CA   1 
ATOM   2322 C C    . ASN   A 1 115 ? 28.477 -11.478 3.742   1.00 10.66 ?  115 ASN   A C    1 
ATOM   2323 O O    . ASN   A 1 115 ? 29.188 -11.405 4.752   1.00 11.63 ?  115 ASN   A O    1 
ATOM   2324 C CB   . ASN   A 1 115 ? 29.187 -9.867  1.977   1.00 10.96 ?  115 ASN   A CB   1 
ATOM   2325 C CG   . ASN   A 1 115 ? 29.989 -9.645  0.726   1.00 11.83 ?  115 ASN   A CG   1 
ATOM   2326 O OD1  . ASN   A 1 115 ? 31.205 -9.756  0.753   1.00 15.39 ?  115 ASN   A OD1  1 
ATOM   2327 N ND2  . ASN   A 1 115 ? 29.330 -9.325  -0.371  1.00 11.75 ?  115 ASN   A ND2  1 
ATOM   2328 H H    . ASN   A 1 115 ? 28.021 -11.586 0.705   1.00 12.58 ?  115 ASN   A H    1 
ATOM   2329 H HA   . ASN   A 1 115 ? 29.992 -11.706 2.391   1.00 13.00 ?  115 ASN   A HA   1 
ATOM   2330 H HB2  . ASN   A 1 115 ? 28.291 -9.522  1.835   1.00 13.13 ?  115 ASN   A HB2  1 
ATOM   2331 H HB3  . ASN   A 1 115 ? 29.612 -9.385  2.707   1.00 13.13 ?  115 ASN   A HB3  1 
ATOM   2332 H HD21 . ASN   A 1 115 ? 29.760 -9.183  -1.101  1.00 14.08 ?  115 ASN   A HD21 1 
ATOM   2333 H HD22 . ASN   A 1 115 ? 28.473 -9.272  -0.356  1.00 14.08 ?  115 ASN   A HD22 1 
ATOM   2334 N N    . PHE   A 1 116 ? 27.150 -11.645 3.818   1.00 11.01 ?  116 PHE   A N    1 
ATOM   2335 C CA   . PHE   A 1 116 ? 26.494 -11.750 5.121   1.00 10.99 ?  116 PHE   A CA   1 
ATOM   2336 C C    . PHE   A 1 116 ? 26.972 -12.983 5.888   1.00 11.03 ?  116 PHE   A C    1 
ATOM   2337 O O    . PHE   A 1 116 ? 26.898 -13.007 7.118   1.00 11.81 ?  116 PHE   A O    1 
ATOM   2338 C CB   . PHE   A 1 116 ? 24.960 -11.874 4.987   1.00 11.36 ?  116 PHE   A CB   1 
ATOM   2339 C CG   . PHE   A 1 116 ? 24.208 -10.627 4.520   1.00 11.16 ?  116 PHE   A CG   1 
ATOM   2340 C CD1  . PHE   A 1 116 ? 24.784 -9.604  3.785   1.00 11.17 ?  116 PHE   A CD1  1 
ATOM   2341 C CD2  . PHE   A 1 116 ? 22.853 -10.525 4.831   1.00 11.63 ?  116 PHE   A CD2  1 
ATOM   2342 C CE1  . PHE   A 1 116 ? 24.021 -8.525  3.368   1.00 11.24 ?  116 PHE   A CE1  1 
ATOM   2343 C CE2  . PHE   A 1 116 ? 22.086 -9.452  4.419   1.00 11.82 ?  116 PHE   A CE2  1 
ATOM   2344 C CZ   . PHE   A 1 116 ? 22.664 -8.446  3.686   1.00 11.34 ?  116 PHE   A CZ   1 
ATOM   2345 H H    . PHE   A 1 116 ? 26.616 -11.686 3.143   1.00 13.19 ?  116 PHE   A H    1 
ATOM   2346 H HA   . PHE   A 1 116 ? 26.687 -10.960 5.649   1.00 13.17 ?  116 PHE   A HA   1 
ATOM   2347 H HB2  . PHE   A 1 116 ? 24.766 -12.582 4.351   1.00 13.61 ?  116 PHE   A HB2  1 
ATOM   2348 H HB3  . PHE   A 1 116 ? 24.599 -12.122 5.855   1.00 13.61 ?  116 PHE   A HB3  1 
ATOM   2349 H HD1  . PHE   A 1 116 ? 25.681 -9.664  3.559   1.00 13.38 ?  116 PHE   A HD1  1 
ATOM   2350 H HD2  . PHE   A 1 116 ? 22.445 -11.217 5.321   1.00 13.93 ?  116 PHE   A HD2  1 
ATOM   2351 H HE1  . PHE   A 1 116 ? 24.424 -7.848  2.876   1.00 13.46 ?  116 PHE   A HE1  1 
ATOM   2352 H HE2  . PHE   A 1 116 ? 21.180 -9.414  4.648   1.00 14.16 ?  116 PHE   A HE2  1 
ATOM   2353 H HZ   . PHE   A 1 116 ? 22.162 -7.713  3.418   1.00 13.58 ?  116 PHE   A HZ   1 
ATOM   2354 N N    . ASN   A 1 117 ? 27.415 -14.028 5.182   1.00 11.40 ?  117 ASN   A N    1 
ATOM   2355 C CA   . ASN   A 1 117 ? 27.783 -15.274 5.845   1.00 11.69 ?  117 ASN   A CA   1 
ATOM   2356 C C    . ASN   A 1 117 ? 29.047 -15.155 6.673   1.00 12.26 ?  117 ASN   A C    1 
ATOM   2357 O O    . ASN   A 1 117 ? 29.353 -16.076 7.437   1.00 13.78 ?  117 ASN   A O    1 
ATOM   2358 C CB   . ASN   A 1 117 ? 27.896 -16.394 4.818   1.00 12.19 ?  117 ASN   A CB   1 
ATOM   2359 C CG   . ASN   A 1 117 ? 26.546 -16.783 4.288   1.00 12.19 ?  117 ASN   A CG   1 
ATOM   2360 O OD1  . ASN   A 1 117 ? 25.573 -16.823 5.040   1.00 12.75 ?  117 ASN   A OD1  1 
ATOM   2361 N ND2  . ASN   A 1 117 ? 26.463 -17.039 2.996   1.00 11.94 ?  117 ASN   A ND2  1 
ATOM   2362 H H    . ASN   A 1 117 ? 27.492 -14.035 4.323   1.00 13.66 ?  117 ASN   A H    1 
ATOM   2363 H HA   . ASN   A 1 117 ? 27.062 -15.510 6.447   1.00 14.01 ?  117 ASN   A HA   1 
ATOM   2364 H HB2  . ASN   A 1 117 ? 28.445 -16.090 4.073   1.00 14.61 ?  117 ASN   A HB2  1 
ATOM   2365 H HB3  . ASN   A 1 117 ? 28.296 -17.166 5.236   1.00 14.61 ?  117 ASN   A HB3  1 
ATOM   2366 H HD21 . ASN   A 1 117 ? 25.713 -17.258 2.653   1.00 14.31 ?  117 ASN   A HD21 1 
ATOM   2367 H HD22 . ASN   A 1 117 ? 27.169 -16.985 2.501   1.00 14.31 ?  117 ASN   A HD22 1 
ATOM   2368 N N    . GLN   A 1 118 ? 29.775 -14.046 6.555   1.00 11.97 ?  118 GLN   A N    1 
ATOM   2369 C CA   . GLN   A 1 118 ? 30.949 -13.814 7.379   1.00 12.73 ?  118 GLN   A CA   1 
ATOM   2370 C C    . GLN   A 1 118 ? 30.604 -13.243 8.749   1.00 12.78 ?  118 GLN   A C    1 
ATOM   2371 O O    . GLN   A 1 118 ? 31.519 -12.960 9.531   1.00 14.10 ?  118 GLN   A O    1 
ATOM   2372 C CB   . GLN   A 1 118 ? 31.946 -12.911 6.645   1.00 12.90 ?  118 GLN   A CB   1 
ATOM   2373 C CG   . GLN   A 1 118 ? 32.412 -13.490 5.324   1.00 13.17 ?  118 GLN   A CG   1 
ATOM   2374 C CD   . GLN   A 1 118 ? 33.249 -14.743 5.503   1.00 13.60 ?  118 GLN   A CD   1 
ATOM   2375 O OE1  . GLN   A 1 118 ? 34.107 -14.806 6.392   1.00 14.34 ?  118 GLN   A OE1  1 
ATOM   2376 N NE2  . GLN   A 1 118 ? 33.005 -15.746 4.662   1.00 13.85 ?  118 GLN   A NE2  1 
ATOM   2377 H H    . GLN   A 1 118 ? 29.600 -13.402 6.002   1.00 14.35 ?  118 GLN   A H    1 
ATOM   2378 H HA   . GLN   A 1 118 ? 31.379 -14.671 7.523   1.00 15.25 ?  118 GLN   A HA   1 
ATOM   2379 H HB2  . GLN   A 1 118 ? 31.524 -12.058 6.470   1.00 15.46 ?  118 GLN   A HB2  1 
ATOM   2380 H HB3  . GLN   A 1 118 ? 32.724 -12.790 7.211   1.00 15.46 ?  118 GLN   A HB3  1 
ATOM   2381 H HG2  . GLN   A 1 118 ? 31.637 -13.714 4.782   1.00 15.78 ?  118 GLN   A HG2  1 
ATOM   2382 H HG3  . GLN   A 1 118 ? 32.956 -12.831 4.866   1.00 15.78 ?  118 GLN   A HG3  1 
ATOM   2383 H HE21 . GLN   A 1 118 ? 32.392 -15.666 4.057   1.00 16.60 ?  118 GLN   A HE21 1 
ATOM   2384 H HE22 . GLN   A 1 118 ? 33.445 -16.482 4.723   1.00 16.60 ?  118 GLN   A HE22 1 
ATOM   2385 N N    . HIS   A 1 119 ? 29.315 -13.094 9.066   1.00 12.23 ?  119 HIS   A N    1 
ATOM   2386 C CA   . HIS   A 1 119 ? 28.864 -12.489 10.314  1.00 12.86 ?  119 HIS   A CA   1 
ATOM   2387 C C    . HIS   A 1 119 ? 27.724 -13.307 10.893  1.00 13.41 ?  119 HIS   A C    1 
ATOM   2388 O O    . HIS   A 1 119 ? 26.771 -13.631 10.182  1.00 14.08 ?  119 HIS   A O    1 
ATOM   2389 C CB   . HIS   A 1 119 ? 28.405 -11.056 10.047  1.00 13.35 ?  119 HIS   A CB   1 
ATOM   2390 C CG   . HIS   A 1 119 ? 29.487 -10.237 9.445   1.00 14.77 ?  119 HIS   A CG   1 
ATOM   2391 N ND1  . HIS   A 1 119 ? 30.465 -9.646  10.209  1.00 17.12 ?  119 HIS   A ND1  1 
ATOM   2392 C CD2  . HIS   A 1 119 ? 29.829 -10.027 8.154   1.00 15.63 ?  119 HIS   A CD2  1 
ATOM   2393 C CE1  . HIS   A 1 119 ? 31.334 -9.052  9.412   1.00 17.17 ?  119 HIS   A CE1  1 
ATOM   2394 N NE2  . HIS   A 1 119 ? 30.981 -9.280  8.160   1.00 16.84 ?  119 HIS   A NE2  1 
ATOM   2395 H H    . HIS   A 1 119 ? 28.661 -13.350 8.559   1.00 14.65 ?  119 HIS   A H    1 
ATOM   2396 H HA   . HIS   A 1 119 ? 29.596 -12.479 10.952  1.00 15.41 ?  119 HIS   A HA   1 
ATOM   2397 H HB2  . HIS   A 1 119 ? 27.650 -11.080 9.436   1.00 15.99 ?  119 HIS   A HB2  1 
ATOM   2398 H HB3  . HIS   A 1 119 ? 28.139 -10.654 10.890  1.00 15.99 ?  119 HIS   A HB3  1 
ATOM   2399 H HD1  . HIS   A 1 119 ? 30.490 -9.649  11.070  1.00 20.52 ?  119 HIS   A HD1  1 
ATOM   2400 H HD2  . HIS   A 1 119 ? 29.363 -10.326 7.405   1.00 18.73 ?  119 HIS   A HD2  1 
ATOM   2401 H HE1  . HIS   A 1 119 ? 32.068 -8.559  9.688   1.00 20.58 ?  119 HIS   A HE1  1 
ATOM   2402 N N    . GLU   A 1 120 ? 27.823 -13.629 12.184  1.00 14.33 ?  120 GLU   A N    1 
ATOM   2403 C CA   . GLU   A 1 120 ? 26.871 -14.560 12.786  1.00 16.62 ?  120 GLU   A CA   1 
ATOM   2404 C C    . GLU   A 1 120 ? 25.453 -13.998 12.836  1.00 15.07 ?  120 GLU   A C    1 
ATOM   2405 O O    . GLU   A 1 120 ? 24.479 -14.756 12.719  1.00 15.20 ?  120 GLU   A O    1 
ATOM   2406 C CB   . GLU   A 1 120 ? 27.340 -14.951 14.188  1.00 21.59 ?  120 GLU   A CB   1 
ATOM   2407 C CG   . GLU   A 1 120 ? 28.527 -15.897 14.201  1.00 28.98 ?  120 GLU   A CG   1 
ATOM   2408 C CD   . GLU   A 1 120 ? 28.664 -16.641 15.515  1.00 35.29 ?  120 GLU   A CD   1 
ATOM   2409 O OE1  . GLU   A 1 120 ? 28.273 -16.082 16.563  1.00 37.09 ?  120 GLU   A OE1  1 
ATOM   2410 O OE2  . GLU   A 1 120 ? 29.159 -17.789 15.499  1.00 39.00 -1 120 GLU   A OE2  1 
ATOM   2411 H H    . GLU   A 1 120 ? 28.432 -13.338 12.722  1.00 17.17 ?  120 GLU   A H    1 
ATOM   2412 H HA   . GLU   A 1 120 ? 26.849 -15.370 12.258  1.00 19.92 ?  120 GLU   A HA   1 
ATOM   2413 H HB2  . GLU   A 1 120 ? 27.601 -14.156 14.676  1.00 25.89 ?  120 GLU   A HB2  1 
ATOM   2414 H HB3  . GLU   A 1 120 ? 26.612 -15.396 14.656  1.00 25.89 ?  120 GLU   A HB3  1 
ATOM   2415 H HG2  . GLU   A 1 120 ? 28.429 -16.547 13.487  1.00 34.75 ?  120 GLU   A HG2  1 
ATOM   2416 H HG3  . GLU   A 1 120 ? 29.344 -15.393 14.084  1.00 34.75 ?  120 GLU   A HG3  1 
ATOM   2417 N N    . VAL   A 1 121 ? 25.317 -12.690 13.057  1.00 14.61 ?  121 VAL   A N    1 
ATOM   2418 C CA   . VAL   A 1 121 ? 24.022 -12.024 13.175  1.00 14.48 ?  121 VAL   A CA   1 
ATOM   2419 C C    . VAL   A 1 121 ? 24.133 -10.638 12.547  1.00 13.34 ?  121 VAL   A C    1 
ATOM   2420 O O    . VAL   A 1 121 ? 25.105 -9.915  12.793  1.00 14.39 ?  121 VAL   A O    1 
ATOM   2421 C CB   . VAL   A 1 121 ? 23.582 -11.884 14.649  1.00 17.87 ?  121 VAL   A CB   1 
ATOM   2422 C CG1  . VAL   A 1 121 ? 22.192 -11.273 14.739  1.00 18.57 ?  121 VAL   A CG1  1 
ATOM   2423 C CG2  . VAL   A 1 121 ? 23.613 -13.216 15.380  1.00 20.15 ?  121 VAL   A CG2  1 
ATOM   2424 H H    . VAL   A 1 121 ? 25.981 -12.149 13.144  1.00 17.51 ?  121 VAL   A H    1 
ATOM   2425 H HA   . VAL   A 1 121 ? 23.348 -12.537 12.700  1.00 17.35 ?  121 VAL   A HA   1 
ATOM   2426 H HB   . VAL   A 1 121 ? 24.192 -11.288 15.105  1.00 21.43 ?  121 VAL   A HB   1 
ATOM   2427 H HG11 . VAL   A 1 121 ? 21.876 -11.335 15.657  1.00 22.26 ?  121 VAL   A HG11 1 
ATOM   2428 H HG12 . VAL   A 1 121 ? 22.234 -10.344 14.469  1.00 22.26 ?  121 VAL   A HG12 1 
ATOM   2429 H HG13 . VAL   A 1 121 ? 21.591 -11.763 14.155  1.00 22.26 ?  121 VAL   A HG13 1 
ATOM   2430 H HG21 . VAL   A 1 121 ? 23.258 -13.095 16.280  1.00 24.15 ?  121 VAL   A HG21 1 
ATOM   2431 H HG22 . VAL   A 1 121 ? 23.063 -13.857 14.900  1.00 24.15 ?  121 VAL   A HG22 1 
ATOM   2432 H HG23 . VAL   A 1 121 ? 24.526 -13.532 15.429  1.00 24.15 ?  121 VAL   A HG23 1 
ATOM   2433 N N    . LEU   A 1 122 ? 23.119 -10.245 11.770  1.00 12.70 ?  122 LEU   A N    1 
ATOM   2434 C CA   . LEU   A 1 122 ? 23.126 -8.944  11.104  1.00 12.70 ?  122 LEU   A CA   1 
ATOM   2435 C C    . LEU   A 1 122 ? 21.726 -8.354  11.070  1.00 12.63 ?  122 LEU   A C    1 
ATOM   2436 O O    . LEU   A 1 122 ? 20.737 -9.077  10.929  1.00 13.96 ?  122 LEU   A O    1 
ATOM   2437 C CB   . LEU   A 1 122 ? 23.559 -9.027  9.637   1.00 14.17 ?  122 LEU   A CB   1 
ATOM   2438 C CG   . LEU   A 1 122 ? 24.756 -9.886  9.265   1.00 14.27 ?  122 LEU   A CG   1 
ATOM   2439 C CD1  . LEU   A 1 122 ? 24.338 -11.330 9.044   1.00 15.22 ?  122 LEU   A CD1  1 
ATOM   2440 C CD2  . LEU   A 1 122 ? 25.410 -9.311  8.018   1.00 13.61 ?  122 LEU   A CD2  1 
ATOM   2441 H H    . LEU   A 1 122 ? 22.415 -10.717 11.605  1.00 15.22 ?  122 LEU   A H    1 
ATOM   2442 H HA   . LEU   A 1 122 ? 23.716 -8.332  11.573  1.00 15.22 ?  122 LEU   A HA   1 
ATOM   2443 H HB2  . LEU   A 1 122 ? 22.817 -9.366  9.124   1.00 16.98 ?  122 LEU   A HB2  1 
ATOM   2444 H HB3  . LEU   A 1 122 ? 23.767 -8.127  9.338   1.00 16.98 ?  122 LEU   A HB3  1 
ATOM   2445 H HG   . LEU   A 1 122 ? 25.419 -9.861  9.976   1.00 17.11 ?  122 LEU   A HG   1 
ATOM   2446 H HD11 . LEU   A 1 122 ? 25.103 -11.845 8.744   1.00 18.24 ?  122 LEU   A HD11 1 
ATOM   2447 H HD12 . LEU   A 1 122 ? 24.004 -11.690 9.879   1.00 18.24 ?  122 LEU   A HD12 1 
ATOM   2448 H HD13 . LEU   A 1 122 ? 23.639 -11.356 8.369   1.00 18.24 ?  122 LEU   A HD13 1 
ATOM   2449 H HD21 . LEU   A 1 122 ? 26.148 -9.887  7.742   1.00 16.30 ?  122 LEU   A HD21 1 
ATOM   2450 H HD22 . LEU   A 1 122 ? 24.754 -9.261  7.305   1.00 16.30 ?  122 LEU   A HD22 1 
ATOM   2451 H HD23 . LEU   A 1 122 ? 25.753 -8.421  8.212   1.00 16.30 ?  122 LEU   A HD23 1 
ATOM   2452 N N    . LEU   A 1 123 ? 21.664 -7.027  11.175  1.00 12.27 ?  123 LEU   A N    1 
ATOM   2453 C CA   . LEU   A 1 123 ? 20.494 -6.227  10.816  1.00 12.27 ?  123 LEU   A CA   1 
ATOM   2454 C C    . LEU   A 1 123 ? 20.729 -5.694  9.410   1.00 11.53 ?  123 LEU   A C    1 
ATOM   2455 O O    . LEU   A 1 123 ? 21.775 -5.095  9.158   1.00 12.32 ?  123 LEU   A O    1 
ATOM   2456 C CB   . LEU   A 1 123 ? 20.366 -5.053  11.790  1.00 12.36 ?  123 LEU   A CB   1 
ATOM   2457 C CG   . LEU   A 1 123 ? 19.315 -3.997  11.450  1.00 13.15 ?  123 LEU   A CG   1 
ATOM   2458 C CD1  . LEU   A 1 123 ? 17.914 -4.588  11.444  1.00 13.91 ?  123 LEU   A CD1  1 
ATOM   2459 C CD2  . LEU   A 1 123 ? 19.407 -2.840  12.434  1.00 14.29 ?  123 LEU   A CD2  1 
ATOM   2460 H H    . LEU   A 1 123 ? 22.322 -6.545  11.455  1.00 14.70 ?  123 LEU   A H    1 
ATOM   2461 H HA   . LEU   A 1 123 ? 19.689 -6.767  10.837  1.00 14.70 ?  123 LEU   A HA   1 
ATOM   2462 H HB2  . LEU   A 1 123 ? 20.138 -5.408  12.664  1.00 14.81 ?  123 LEU   A HB2  1 
ATOM   2463 H HB3  . LEU   A 1 123 ? 21.219 -4.601  11.838  1.00 14.81 ?  123 LEU   A HB3  1 
ATOM   2464 H HG   . LEU   A 1 123 ? 19.490 -3.642  10.563  1.00 15.76 ?  123 LEU   A HG   1 
ATOM   2465 H HD11 . LEU   A 1 123 ? 17.271 -3.887  11.263  1.00 16.67 ?  123 LEU   A HD11 1 
ATOM   2466 H HD12 . LEU   A 1 123 ? 17.861 -5.271  10.754  1.00 16.67 ?  123 LEU   A HD12 1 
ATOM   2467 H HD13 . LEU   A 1 123 ? 17.736 -4.986  12.312  1.00 16.67 ?  123 LEU   A HD13 1 
ATOM   2468 H HD21 . LEU   A 1 123 ? 18.737 -2.179  12.210  1.00 17.13 ?  123 LEU   A HD21 1 
ATOM   2469 H HD22 . LEU   A 1 123 ? 19.251 -3.181  13.331  1.00 17.13 ?  123 LEU   A HD22 1 
ATOM   2470 H HD23 . LEU   A 1 123 ? 20.293 -2.452  12.378  1.00 17.13 ?  123 LEU   A HD23 1 
ATOM   2471 N N    . ALA   A 1 124 ? 19.775 -5.890  8.502   1.00 10.97 ?  124 ALA   A N    1 
ATOM   2472 C CA   . ALA   A 1 124 ? 20.045 -5.594  7.104   1.00 11.15 ?  124 ALA   A CA   1 
ATOM   2473 C C    . ALA   A 1 124 ? 18.809 -5.137  6.347   1.00 11.07 ?  124 ALA   A C    1 
ATOM   2474 O O    . ALA   A 1 124 ? 17.683 -5.498  6.714   1.00 11.92 ?  124 ALA   A O    1 
ATOM   2475 C CB   . ALA   A 1 124 ? 20.618 -6.820  6.385   1.00 11.81 ?  124 ALA   A CB   1 
ATOM   2476 H H    . ALA   A 1 124 ? 18.982 -6.191  8.666   1.00 13.14 ?  124 ALA   A H    1 
ATOM   2477 H HA   . ALA   A 1 124 ? 20.715 -4.893  7.075   1.00 13.35 ?  124 ALA   A HA   1 
ATOM   2478 H HB1  . ALA   A 1 124 ? 20.792 -6.594  5.457   1.00 14.14 ?  124 ALA   A HB1  1 
ATOM   2479 H HB2  . ALA   A 1 124 ? 21.452 -7.078  6.819   1.00 14.14 ?  124 ALA   A HB2  1 
ATOM   2480 H HB3  . ALA   A 1 124 ? 19.982 -7.546  6.438   1.00 14.14 ?  124 ALA   A HB3  1 
ATOM   2481 N N    A PRO   A 1 125 ? 18.999 -4.427  5.234   0.68 10.92 ?  125 PRO   A N    1 
ATOM   2482 N N    B PRO   A 1 125 ? 18.977 -4.299  5.335   0.32 10.81 ?  125 PRO   A N    1 
ATOM   2483 C CA   A PRO   A 1 125 ? 17.933 -4.204  4.258   0.68 11.18 ?  125 PRO   A CA   1 
ATOM   2484 C CA   B PRO   A 1 125 ? 17.879 -4.008  4.416   0.32 10.88 ?  125 PRO   A CA   1 
ATOM   2485 C C    A PRO   A 1 125 ? 17.991 -5.270  3.168   0.68 11.21 ?  125 PRO   A C    1 
ATOM   2486 C C    B PRO   A 1 125 ? 17.916 -5.034  3.290   0.32 10.96 ?  125 PRO   A C    1 
ATOM   2487 O O    A PRO   A 1 125 ? 18.960 -6.024  3.050   0.68 11.79 ?  125 PRO   A O    1 
ATOM   2488 O O    B PRO   A 1 125 ? 18.844 -5.838  3.177   0.32 11.31 ?  125 PRO   A O    1 
ATOM   2489 C CB   A PRO   A 1 125 ? 18.351 -2.853  3.660   0.68 11.41 ?  125 PRO   A CB   1 
ATOM   2490 C CB   B PRO   A 1 125 ? 18.265 -2.625  3.883   0.32 11.12 ?  125 PRO   A CB   1 
ATOM   2491 C CG   A PRO   A 1 125 ? 19.869 -2.986  3.567   0.68 10.90 ?  125 PRO   A CG   1 
ATOM   2492 C CG   B PRO   A 1 125 ? 19.756 -2.697  3.808   0.32 11.14 ?  125 PRO   A CG   1 
ATOM   2493 C CD   A PRO   A 1 125 ? 20.269 -3.813  4.789   0.68 10.90 ?  125 PRO   A CD   1 
ATOM   2494 C CD   B PRO   A 1 125 ? 20.195 -3.546  4.977   0.32 10.89 ?  125 PRO   A CD   1 
ATOM   2495 H HA   A PRO   A 1 125 ? 17.054 -4.167  4.666   0.68 13.39 ?  125 PRO   A HA   1 
ATOM   2496 H HA   B PRO   A 1 125 ? 17.014 -3.988  4.868   0.32 13.03 ?  125 PRO   A HA   1 
ATOM   2497 H HB2  A PRO   A 1 125 ? 17.948 -2.739  2.783   0.68 13.66 ?  125 PRO   A HB2  1 
ATOM   2498 H HB2  B PRO   A 1 125 ? 17.874 -2.489  3.005   0.32 13.32 ?  125 PRO   A HB2  1 
ATOM   2499 H HB3  A PRO   A 1 125 ? 18.093 -2.137  4.260   0.68 13.66 ?  125 PRO   A HB3  1 
ATOM   2500 H HB3  B PRO   A 1 125 ? 17.976 -1.935  4.503   0.32 13.32 ?  125 PRO   A HB3  1 
ATOM   2501 H HG2  A PRO   A 1 125 ? 20.109 -3.446  2.743   0.68 13.05 ?  125 PRO   A HG2  1 
ATOM   2502 H HG2  B PRO   A 1 125 ? 20.018 -3.112  2.972   0.32 13.35 ?  125 PRO   A HG2  1 
ATOM   2503 H HG3  A PRO   A 1 125 ? 20.277 -2.106  3.594   0.68 13.05 ?  125 PRO   A HG3  1 
ATOM   2504 H HG3  B PRO   A 1 125 ? 20.128 -1.806  3.877   0.32 13.35 ?  125 PRO   A HG3  1 
ATOM   2505 H HD2  A PRO   A 1 125 ? 20.918 -4.494  4.535   0.68 13.06 ?  125 PRO   A HD2  1 
ATOM   2506 H HD2  B PRO   A 1 125 ? 20.901 -4.153  4.705   0.32 13.04 ?  125 PRO   A HD2  1 
ATOM   2507 H HD3  A PRO   A 1 125 ? 20.625 -3.234  5.482   0.68 13.06 ?  125 PRO   A HD3  1 
ATOM   2508 H HD3  B PRO   A 1 125 ? 20.480 -2.984  5.714   0.32 13.04 ?  125 PRO   A HD3  1 
ATOM   2509 N N    A LEU   A 1 126 ? 16.939 -5.308  2.352   0.68 11.21 ?  126 LEU   A N    1 
ATOM   2510 N N    B LEU   A 1 126 ? 16.890 -4.990  2.448   0.32 11.37 ?  126 LEU   A N    1 
ATOM   2511 C CA   A LEU   A 1 126 ? 16.956 -6.125  1.146   0.68 11.48 ?  126 LEU   A CA   1 
ATOM   2512 C CA   B LEU   A 1 126 ? 16.898 -5.836  1.263   0.32 11.10 ?  126 LEU   A CA   1 
ATOM   2513 C C    A LEU   A 1 126 ? 17.869 -5.494  0.098   0.68 11.92 ?  126 LEU   A C    1 
ATOM   2514 C C    B LEU   A 1 126 ? 17.877 -5.277  0.239   0.32 11.47 ?  126 LEU   A C    1 
ATOM   2515 O O    A LEU   A 1 126 ? 17.598 -4.399  -0.409  0.68 12.63 ?  126 LEU   A O    1 
ATOM   2516 O O    B LEU   A 1 126 ? 17.790 -4.110  -0.149  0.32 12.19 ?  126 LEU   A O    1 
ATOM   2517 C CB   A LEU   A 1 126 ? 15.542 -6.294  0.602   0.68 12.31 ?  126 LEU   A CB   1 
ATOM   2518 C CB   B LEU   A 1 126 ? 15.503 -5.912  0.655   0.32 11.57 ?  126 LEU   A CB   1 
ATOM   2519 C CG   A LEU   A 1 126 ? 14.662 -7.269  1.391   0.68 13.08 ?  126 LEU   A CG   1 
ATOM   2520 C CG   B LEU   A 1 126 ? 14.501 -6.830  1.353   0.32 11.59 ?  126 LEU   A CG   1 
ATOM   2521 C CD1  A LEU   A 1 126 ? 13.221 -7.137  0.968   0.68 14.47 ?  126 LEU   A CD1  1 
ATOM   2522 C CD1  B LEU   A 1 126 ? 13.170 -6.778  0.622   0.32 11.90 ?  126 LEU   A CD1  1 
ATOM   2523 C CD2  A LEU   A 1 126 ? 15.150 -8.703  1.198   0.68 13.09 ?  126 LEU   A CD2  1 
ATOM   2524 C CD2  B LEU   A 1 126 ? 15.011 -8.266  1.431   0.32 11.78 ?  126 LEU   A CD2  1 
ATOM   2525 H H    A LEU   A 1 126 ? 16.211 -4.871  2.471   0.68 13.43 ?  126 LEU   A H    1 
ATOM   2526 H H    B LEU   A 1 126 ? 16.193 -4.489  2.541   0.32 13.63 ?  126 LEU   A H    1 
ATOM   2527 H HA   A LEU   A 1 126 ? 17.304 -7.005  1.354   0.68 13.75 ?  126 LEU   A HA   1 
ATOM   2528 H HA   B LEU   A 1 126 ? 17.183 -6.729  1.512   0.32 13.30 ?  126 LEU   A HA   1 
ATOM   2529 H HB2  A LEU   A 1 126 ? 15.095 -5.431  0.615   0.68 14.74 ?  126 LEU   A HB2  1 
ATOM   2530 H HB2  B LEU   A 1 126 ? 15.124 -5.020  0.656   0.32 13.86 ?  126 LEU   A HB2  1 
ATOM   2531 H HB3  A LEU   A 1 126 ? 15.588 -6.619  -0.312  0.68 14.74 ?  126 LEU   A HB3  1 
ATOM   2532 H HB3  B LEU   A 1 126 ? 15.593 -6.226  -0.256  0.32 13.86 ?  126 LEU   A HB3  1 
ATOM   2533 H HG   A LEU   A 1 126 ? 14.722 -7.061  2.337   0.68 15.68 ?  126 LEU   A HG   1 
ATOM   2534 H HG   B LEU   A 1 126 ? 14.355 -6.512  2.258   0.32 13.89 ?  126 LEU   A HG   1 
ATOM   2535 H HD11 A LEU   A 1 126 ? 12.685 -7.768  1.474   0.68 17.34 ?  126 LEU   A HD11 1 
ATOM   2536 H HD11 B LEU   A 1 126 ? 12.538 -7.360  1.073   0.32 14.26 ?  126 LEU   A HD11 1 
ATOM   2537 H HD12 A LEU   A 1 126 ? 12.926 -6.233  1.144   0.68 17.34 ?  126 LEU   A HD12 1 
ATOM   2538 H HD12 B LEU   A 1 126 ? 12.842 -5.867  0.622   0.32 14.26 ?  126 LEU   A HD12 1 
ATOM   2539 H HD13 A LEU   A 1 126 ? 13.155 -7.332  0.020   0.68 17.34 ?  126 LEU   A HD13 1 
ATOM   2540 H HD13 B LEU   A 1 126 ? 13.302 -7.082  -0.292  0.32 14.26 ?  126 LEU   A HD13 1 
ATOM   2541 H HD21 A LEU   A 1 126 ? 14.505 -9.313  1.580   0.68 15.68 ?  126 LEU   A HD21 1 
ATOM   2542 H HD21 B LEU   A 1 126 ? 14.279 -8.849  1.677   0.32 14.12 ?  126 LEU   A HD21 1 
ATOM   2543 H HD22 A LEU   A 1 126 ? 15.250 -8.875  0.247   0.68 15.68 ?  126 LEU   A HD22 1 
ATOM   2544 H HD22 B LEU   A 1 126 ? 15.364 -8.521  0.564   0.32 14.12 ?  126 LEU   A HD22 1 
ATOM   2545 H HD23 A LEU   A 1 126 ? 16.010 -8.808  1.641   0.68 15.68 ?  126 LEU   A HD23 1 
ATOM   2546 H HD23 B LEU   A 1 126 ? 15.714 -8.314  2.099   0.32 14.12 ?  126 LEU   A HD23 1 
ATOM   2547 N N    A LEU   A 1 127 ? 18.949 -6.193  -0.237  0.68 11.89 ?  127 LEU   A N    1 
ATOM   2548 N N    B LEU   A 1 127 ? 18.818 -6.107  -0.200  0.32 11.79 ?  127 LEU   A N    1 
ATOM   2549 C CA   A LEU   A 1 127 ? 19.924 -5.656  -1.172  0.68 11.52 ?  127 LEU   A CA   1 
ATOM   2550 C CA   B LEU   A 1 127 ? 19.821 -5.640  -1.145  0.32 11.73 ?  127 LEU   A CA   1 
ATOM   2551 C C    A LEU   A 1 127 ? 19.305 -5.477  -2.549  0.68 11.19 ?  127 LEU   A C    1 
ATOM   2552 C C    B LEU   A 1 127 ? 19.218 -5.433  -2.530  0.32 11.45 ?  127 LEU   A C    1 
ATOM   2553 O O    A LEU   A 1 127 ? 18.497 -6.289  -3.010  0.68 11.35 ?  127 LEU   A O    1 
ATOM   2554 O O    B LEU   A 1 127 ? 18.329 -6.171  -2.968  0.32 11.76 ?  127 LEU   A O    1 
ATOM   2555 C CB   A LEU   A 1 127 ? 21.124 -6.596  -1.278  0.68 12.28 ?  127 LEU   A CB   1 
ATOM   2556 C CB   B LEU   A 1 127 ? 20.982 -6.632  -1.223  0.32 12.28 ?  127 LEU   A CB   1 
ATOM   2557 C CG   A LEU   A 1 127 ? 21.911 -6.873  -0.004  0.68 13.53 ?  127 LEU   A CG   1 
ATOM   2558 C CG   B LEU   A 1 127 ? 21.764 -6.842  0.074   0.32 12.91 ?  127 LEU   A CG   1 
ATOM   2559 C CD1  A LEU   A 1 127 ? 22.979 -7.917  -0.281  0.68 14.36 ?  127 LEU   A CD1  1 
ATOM   2560 C CD1  B LEU   A 1 127 ? 23.016 -7.661  -0.187  0.32 13.33 ?  127 LEU   A CD1  1 
ATOM   2561 C CD2  A LEU   A 1 127 ? 22.547 -5.604  0.509   0.68 14.06 ?  127 LEU   A CD2  1 
ATOM   2562 C CD2  B LEU   A 1 127 ? 22.125 -5.515  0.709   0.32 13.04 ?  127 LEU   A CD2  1 
ATOM   2563 H H    A LEU   A 1 127 ? 19.137 -6.975  0.066   0.68 14.25 ?  127 LEU   A H    1 
ATOM   2564 H H    B LEU   A 1 127 ? 18.904 -6.926  0.049   0.32 14.13 ?  127 LEU   A H    1 
ATOM   2565 H HA   A LEU   A 1 127 ? 20.232 -4.793  -0.857  0.68 13.80 ?  127 LEU   A HA   1 
ATOM   2566 H HA   B LEU   A 1 127 ? 20.168 -4.784  -0.836  0.32 14.05 ?  127 LEU   A HA   1 
ATOM   2567 H HB2  A LEU   A 1 127 ? 20.810 -7.447  -1.612  0.68 14.72 ?  127 LEU   A HB2  1 
ATOM   2568 H HB2  B LEU   A 1 127 ? 20.630 -7.493  -1.494  0.32 14.71 ?  127 LEU   A HB2  1 
ATOM   2569 H HB3  A LEU   A 1 127 ? 21.746 -6.210  -1.915  0.68 14.72 ?  127 LEU   A HB3  1 
ATOM   2570 H HB3  B LEU   A 1 127 ? 21.610 -6.312  -1.890  0.32 14.71 ?  127 LEU   A HB3  1 
ATOM   2571 H HG   A LEU   A 1 127 ? 21.310 -7.219  0.679   0.68 16.21 ?  127 LEU   A HG   1 
ATOM   2572 H HG   B LEU   A 1 127 ? 21.209 -7.335  0.700   0.32 15.47 ?  127 LEU   A HG   1 
ATOM   2573 H HD11 A LEU   A 1 127 ? 23.459 -8.108  0.542   0.68 17.21 ?  127 LEU   A HD11 1 
ATOM   2574 H HD11 B LEU   A 1 127 ? 23.492 -7.785  0.650   0.32 15.97 ?  127 LEU   A HD11 1 
ATOM   2575 H HD12 A LEU   A 1 127 ? 22.556 -8.728  -0.609  0.68 17.21 ?  127 LEU   A HD12 1 
ATOM   2576 H HD12 B LEU   A 1 127 ? 22.760 -8.523  -0.551  0.32 15.97 ?  127 LEU   A HD12 1 
ATOM   2577 H HD13 A LEU   A 1 127 ? 23.592 -7.573  -0.948  0.68 17.21 ?  127 LEU   A HD13 1 
ATOM   2578 H HD13 B LEU   A 1 127 ? 23.577 -7.187  -0.819  0.32 15.97 ?  127 LEU   A HD13 1 
ATOM   2579 H HD21 A LEU   A 1 127 ? 23.104 -5.818  1.273   0.68 16.85 ?  127 LEU   A HD21 1 
ATOM   2580 H HD21 B LEU   A 1 127 ? 22.797 -5.666  1.392   0.32 15.62 ?  127 LEU   A HD21 1 
ATOM   2581 H HD22 A LEU   A 1 127 ? 23.088 -5.218  -0.198  0.68 16.85 ?  127 LEU   A HD22 1 
ATOM   2582 H HD22 B LEU   A 1 127 ? 22.475 -4.925  0.025   0.32 15.62 ?  127 LEU   A HD22 1 
ATOM   2583 H HD23 A LEU   A 1 127 ? 21.850 -4.983  0.769   0.68 16.85 ?  127 LEU   A HD23 1 
ATOM   2584 H HD23 B LEU   A 1 127 ? 21.330 -5.128  1.106   0.32 15.62 ?  127 LEU   A HD23 1 
ATOM   2585 N N    . SER   A 1 128 ? 19.724 -4.414  -3.219  1.00 11.45 ?  128 SER   A N    1 
ATOM   2586 C CA   . SER   A 1 128 ? 19.321 -4.054  -4.567  1.00 11.44 ?  128 SER   A CA   1 
ATOM   2587 C C    . SER   A 1 128 ? 17.872 -3.593  -4.687  1.00 11.72 ?  128 SER   A C    1 
ATOM   2588 O O    . SER   A 1 128 ? 17.437 -3.288  -5.798  1.00 13.40 ?  128 SER   A O    1 
ATOM   2589 C CB   . SER   A 1 128 ? 19.670 -5.119  -5.612  1.00 11.32 ?  128 SER   A CB   1 
ATOM   2590 O OG   . SER   A 1 128 ? 21.078 -5.316  -5.672  1.00 11.92 ?  128 SER   A OG   1 
ATOM   2591 H H    A SER   A 1 128 ? 20.291 -3.858  -2.887  0.68 13.72 ?  128 SER   A H    1 
ATOM   2592 H H    B SER   A 1 128 ? 20.354 -3.912  -2.914  0.32 13.72 ?  128 SER   A H    1 
ATOM   2593 H HA   . SER   A 1 128 ? 19.855 -3.289  -4.798  1.00 13.71 ?  128 SER   A HA   1 
ATOM   2594 H HB2  . SER   A 1 128 ? 19.231 -5.950  -5.382  1.00 13.56 ?  128 SER   A HB2  1 
ATOM   2595 H HB3  . SER   A 1 128 ? 19.351 -4.811  -6.485  1.00 13.56 ?  128 SER   A HB3  1 
ATOM   2596 H HG   . SER   A 1 128 ? 21.453 -4.589  -5.867  1.00 14.28 ?  128 SER   A HG   1 
ATOM   2597 N N    A ALA   A 1 129 ? 17.123 -3.511  -3.588  0.68 12.60 ?  129 ALA   A N    1 
ATOM   2598 N N    B ALA   A 1 129 ? 17.155 -3.496  -3.566  0.32 12.29 ?  129 ALA   A N    1 
ATOM   2599 C CA   A ALA   A 1 129 ? 15.748 -3.034  -3.628  0.68 12.90 ?  129 ALA   A CA   1 
ATOM   2600 C CA   B ALA   A 1 129 ? 15.814 -2.933  -3.548  0.32 12.59 ?  129 ALA   A CA   1 
ATOM   2601 C C    A ALA   A 1 129 ? 15.729 -1.505  -3.549  0.68 12.68 ?  129 ALA   A C    1 
ATOM   2602 C C    B ALA   A 1 129 ? 15.890 -1.409  -3.629  0.32 12.32 ?  129 ALA   A C    1 
ATOM   2603 O O    A ALA   A 1 129 ? 16.766 -0.837  -3.618  0.68 12.61 ?  129 ALA   A O    1 
ATOM   2604 O O    B ALA   A 1 129 ? 16.967 -0.812  -3.710  0.32 12.38 ?  129 ALA   A O    1 
ATOM   2605 C CB   A ALA   A 1 129 ? 14.921 -3.712  -2.531  0.68 14.13 ?  129 ALA   A CB   1 
ATOM   2606 C CB   B ALA   A 1 129 ? 15.067 -3.385  -2.292  0.32 13.47 ?  129 ALA   A CB   1 
ATOM   2607 H H    A ALA   A 1 129 ? 17.397 -3.729  -2.797  0.68 15.09 ?  129 ALA   A H    1 
ATOM   2608 H H    B ALA   A 1 129 ? 17.429 -3.748  -2.789  0.32 14.72 ?  129 ALA   A H    1 
ATOM   2609 H HA   A ALA   A 1 129 ? 15.362 -3.287  -4.475  0.68 15.45 ?  129 ALA   A HA   1 
ATOM   2610 H HA   B ALA   A 1 129 ? 15.325 -3.247  -4.320  0.32 15.09 ?  129 ALA   A HA   1 
ATOM   2611 H HB1  A ALA   A 1 129 ? 14.008 -3.389  -2.578  0.68 16.94 ?  129 ALA   A HB1  1 
ATOM   2612 H HB1  B ALA   A 1 129 ? 14.173 -3.006  -2.300  0.32 16.14 ?  129 ALA   A HB1  1 
ATOM   2613 H HB2  A ALA   A 1 129 ? 14.940 -4.672  -2.669  0.68 16.94 ?  129 ALA   A HB2  1 
ATOM   2614 H HB2  B ALA   A 1 129 ? 15.012 -4.355  -2.288  0.32 16.14 ?  129 ALA   A HB2  1 
ATOM   2615 H HB3  A ALA   A 1 129 ? 15.303 -3.496  -1.664  0.68 16.94 ?  129 ALA   A HB3  1 
ATOM   2616 H HB3  B ALA   A 1 129 ? 15.547 -3.079  -1.506  0.32 16.14 ?  129 ALA   A HB3  1 
ATOM   2617 N N    A GLY   A 1 130 ? 14.536 -0.932  -3.422  0.68 12.81 ?  130 GLY   A N    1 
ATOM   2618 N N    B GLY   A 1 130 ? 14.726 -0.768  -3.619  0.32 12.28 ?  130 GLY   A N    1 
ATOM   2619 C CA   A GLY   A 1 130 ? 14.422 0.516   -3.364  0.68 12.94 ?  130 GLY   A CA   1 
ATOM   2620 C CA   B GLY   A 1 130 ? 14.701 0.685   -3.634  0.32 12.56 ?  130 GLY   A CA   1 
ATOM   2621 C C    A GLY   A 1 130 ? 15.029 1.161   -4.594  0.68 12.01 ?  130 GLY   A C    1 
ATOM   2622 C C    B GLY   A 1 130 ? 15.352 1.235   -4.888  0.32 12.38 ?  130 GLY   A C    1 
ATOM   2623 O O    A GLY   A 1 130 ? 14.795 0.726   -5.726  0.68 12.47 ?  130 GLY   A O    1 
ATOM   2624 O O    B GLY   A 1 130 ? 15.106 0.763   -6.004  0.32 13.05 ?  130 GLY   A O    1 
ATOM   2625 H H    A GLY   A 1 130 ? 13.785 -1.354  -3.371  0.68 15.35 ?  130 GLY   A H    1 
ATOM   2626 H H    B GLY   A 1 130 ? 13.952 -1.143  -3.606  0.32 14.72 ?  130 GLY   A H    1 
ATOM   2627 H HA2  A GLY   A 1 130 ? 13.482 0.769   -3.307  0.68 15.50 ?  130 GLY   A HA2  1 
ATOM   2628 H HA2  B GLY   A 1 130 ? 13.782 0.996   -3.600  0.32 15.05 ?  130 GLY   A HA2  1 
ATOM   2629 H HA3  A GLY   A 1 130 ? 14.880 0.852   -2.584  0.68 15.50 ?  130 GLY   A HA3  1 
ATOM   2630 H HA3  B GLY   A 1 130 ? 15.173 1.030   -2.859  0.32 15.05 ?  130 GLY   A HA3  1 
ATOM   2631 N N    A ILE   A 1 131 ? 15.820 2.219   -4.373  0.68 11.82 ?  131 ILE   A N    1 
ATOM   2632 N N    B ILE   A 1 131 ? 16.212 2.241   -4.701  0.32 12.22 ?  131 ILE   A N    1 
ATOM   2633 C CA   A ILE   A 1 131 ? 16.383 2.996   -5.474  0.68 11.70 ?  131 ILE   A CA   1 
ATOM   2634 C CA   B ILE   A 1 131 ? 16.813 2.951   -5.828  0.32 12.36 ?  131 ILE   A CA   1 
ATOM   2635 C C    A ILE   A 1 131 ? 17.427 2.235   -6.280  0.68 11.23 ?  131 ILE   A C    1 
ATOM   2636 C C    B ILE   A 1 131 ? 17.766 2.095   -6.649  0.32 12.73 ?  131 ILE   A C    1 
ATOM   2637 O O    A ILE   A 1 131 ? 17.854 2.731   -7.328  0.68 12.19 ?  131 ILE   A O    1 
ATOM   2638 O O    B ILE   A 1 131 ? 18.177 2.520   -7.736  0.32 13.46 ?  131 ILE   A O    1 
ATOM   2639 C CB   A ILE   A 1 131 ? 16.931 4.368   -5.019  0.68 13.34 ?  131 ILE   A CB   1 
ATOM   2640 C CB   B ILE   A 1 131 ? 17.488 4.265   -5.375  0.32 12.58 ?  131 ILE   A CB   1 
ATOM   2641 C CG1  A ILE   A 1 131 ? 18.151 4.210   -4.105  0.68 14.91 ?  131 ILE   A CG1  1 
ATOM   2642 C CG1  B ILE   A 1 131 ? 18.681 3.989   -4.457  0.32 13.19 ?  131 ILE   A CG1  1 
ATOM   2643 C CG2  A ILE   A 1 131 ? 15.840 5.180   -4.328  0.68 14.01 ?  131 ILE   A CG2  1 
ATOM   2644 C CG2  B ILE   A 1 131 ? 16.478 5.168   -4.671  0.32 12.45 ?  131 ILE   A CG2  1 
ATOM   2645 C CD1  A ILE   A 1 131 ? 18.785 5.539   -3.703  0.68 16.12 ?  131 ILE   A CD1  1 
ATOM   2646 C CD1  B ILE   A 1 131 ? 19.384 5.254   -3.971  0.32 13.71 ?  131 ILE   A CD1  1 
ATOM   2647 H H    A ILE   A 1 131 ? 16.020 2.514   -3.591  0.68 14.16 ?  131 ILE   A H    1 
ATOM   2648 H H    B ILE   A 1 131 ? 16.460 2.529   -3.928  0.32 14.64 ?  131 ILE   A H    1 
ATOM   2649 H HA   A ILE   A 1 131 ? 15.659 3.191   -6.085  0.68 14.02 ?  131 ILE   A HA   1 
ATOM   2650 H HA   B ILE   A 1 131 ? 16.100 3.200   -6.423  0.32 14.81 ?  131 ILE   A HA   1 
ATOM   2651 H HB   A ILE   A 1 131 ? 17.206 4.854   -5.810  0.68 15.99 ?  131 ILE   A HB   1 
ATOM   2652 H HB   B ILE   A 1 131 ? 17.808 4.731   -6.164  0.32 15.08 ?  131 ILE   A HB   1 
ATOM   2653 H HG12 A ILE   A 1 131 ? 17.880 3.751   -3.295  0.68 17.87 ?  131 ILE   A HG12 1 
ATOM   2654 H HG12 B ILE   A 1 131 ? 18.374 3.503   -3.678  0.32 15.80 ?  131 ILE   A HG12 1 
ATOM   2655 H HG13 A ILE   A 1 131 ? 18.828 3.691   -4.568  0.68 17.87 ?  131 ILE   A HG13 1 
ATOM   2656 H HG13 B ILE   A 1 131 ? 19.334 3.463   -4.941  0.32 15.80 ?  131 ILE   A HG13 1 
ATOM   2657 H HG21 A ILE   A 1 131 ? 16.148 6.090   -4.211  0.68 16.79 ?  131 ILE   A HG21 1 
ATOM   2658 H HG21 B ILE   A 1 131 ? 16.861 6.053   -4.564  0.32 14.92 ?  131 ILE   A HG21 1 
ATOM   2659 H HG22 A ILE   A 1 131 ? 15.043 5.168   -4.881  0.68 16.79 ?  131 ILE   A HG22 1 
ATOM   2660 H HG22 B ILE   A 1 131 ? 15.675 5.222   -5.212  0.32 14.92 ?  131 ILE   A HG22 1 
ATOM   2661 H HG23 A ILE   A 1 131 ? 15.649 4.778   -3.465  0.68 16.79 ?  131 ILE   A HG23 1 
ATOM   2662 H HG23 B ILE   A 1 131 ? 16.266 4.791   -3.804  0.32 14.92 ?  131 ILE   A HG23 1 
ATOM   2663 H HD11 A ILE   A 1 131 ? 19.620 5.364   -3.239  0.68 19.32 ?  131 ILE   A HD11 1 
ATOM   2664 H HD11 B ILE   A 1 131 ? 20.215 5.007   -3.536  0.32 16.43 ?  131 ILE   A HD11 1 
ATOM   2665 H HD12 A ILE   A 1 131 ? 18.956 6.064   -4.501  0.68 19.32 ?  131 ILE   A HD12 1 
ATOM   2666 H HD12 B ILE   A 1 131 ? 19.567 5.828   -4.732  0.32 16.43 ?  131 ILE   A HD12 1 
ATOM   2667 H HD13 A ILE   A 1 131 ? 18.177 6.018   -3.117  0.68 19.32 ?  131 ILE   A HD13 1 
ATOM   2668 H HD13 B ILE   A 1 131 ? 18.808 5.718   -3.341  0.32 16.43 ?  131 ILE   A HD13 1 
ATOM   2669 N N    A PHE   A 1 132 ? 17.848 1.043   -5.831  0.68 11.53 ?  132 PHE   A N    1 
ATOM   2670 N N    B PHE   A 1 132 ? 18.129 0.902   -6.172  0.32 12.40 ?  132 PHE   A N    1 
ATOM   2671 C CA   A PHE   A 1 132 ? 18.705 0.188   -6.647  0.68 11.40 ?  132 PHE   A CA   1 
ATOM   2672 C CA   B PHE   A 1 132 ? 18.997 0.027   -6.952  0.32 12.79 ?  132 PHE   A CA   1 
ATOM   2673 C C    A PHE   A 1 132 ? 17.929 -0.574  -7.725  0.68 11.98 ?  132 PHE   A C    1 
ATOM   2674 C C    B PHE   A 1 132 ? 18.255 -0.713  -8.063  0.32 13.14 ?  132 PHE   A C    1 
ATOM   2675 O O    A PHE   A 1 132 ? 18.548 -1.214  -8.582  0.68 13.05 ?  132 PHE   A O    1 
ATOM   2676 O O    B PHE   A 1 132 ? 18.904 -1.334  -8.912  0.32 14.14 ?  132 PHE   A O    1 
ATOM   2677 C CB   A PHE   A 1 132 ? 19.503 -0.783  -5.766  0.68 11.40 ?  132 PHE   A CB   1 
ATOM   2678 C CB   B PHE   A 1 132 ? 19.737 -0.962  -6.043  0.32 12.19 ?  132 PHE   A CB   1 
ATOM   2679 C CG   A PHE   A 1 132 ? 20.759 -0.191  -5.149  0.68 11.75 ?  132 PHE   A CG   1 
ATOM   2680 C CG   B PHE   A 1 132 ? 20.836 -0.340  -5.208  0.32 12.28 ?  132 PHE   A CG   1 
ATOM   2681 C CD1  A PHE   A 1 132 ? 20.696 0.891   -4.285  0.68 12.77 ?  132 PHE   A CD1  1 
ATOM   2682 C CD1  B PHE   A 1 132 ? 20.536 0.487   -4.137  0.32 12.52 ?  132 PHE   A CD1  1 
ATOM   2683 C CD2  A PHE   A 1 132 ? 21.997 -0.769  -5.399  0.68 12.63 ?  132 PHE   A CD2  1 
ATOM   2684 C CD2  B PHE   A 1 132 ? 22.168 -0.618  -5.476  0.32 12.20 ?  132 PHE   A CD2  1 
ATOM   2685 C CE1  A PHE   A 1 132 ? 21.852 1.405   -3.710  0.68 12.82 ?  132 PHE   A CE1  1 
ATOM   2686 C CE1  B PHE   A 1 132 ? 21.547 1.044   -3.365  0.32 12.16 ?  132 PHE   A CE1  1 
ATOM   2687 C CE2  A PHE   A 1 132 ? 23.154 -0.262  -4.826  0.68 13.35 ?  132 PHE   A CE2  1 
ATOM   2688 C CE2  B PHE   A 1 132 ? 23.182 -0.064  -4.707  0.32 12.07 ?  132 PHE   A CE2  1 
ATOM   2689 C CZ   A PHE   A 1 132 ? 23.079 0.830   -3.982  0.68 13.20 ?  132 PHE   A CZ   1 
ATOM   2690 C CZ   B PHE   A 1 132 ? 22.868 0.769   -3.652  0.32 11.96 ?  132 PHE   A CZ   1 
ATOM   2691 H H    A PHE   A 1 132 ? 17.647 0.712   -5.058  0.68 13.82 ?  132 PHE   A H    1 
ATOM   2692 H H    B PHE   A 1 132 ? 17.887 0.581   -5.409  0.32 14.86 ?  132 PHE   A H    1 
ATOM   2693 H HA   A PHE   A 1 132 ? 19.345 0.755   -7.098  0.68 13.65 ?  132 PHE   A HA   1 
ATOM   2694 H HA   B PHE   A 1 132 ? 19.671 0.576   -7.375  0.32 15.33 ?  132 PHE   A HA   1 
ATOM   2695 H HB2  A PHE   A 1 132 ? 18.934 -1.082  -5.037  0.68 13.66 ?  132 PHE   A HB2  1 
ATOM   2696 H HB2  B PHE   A 1 132 ? 19.100 -1.353  -5.429  0.32 14.61 ?  132 PHE   A HB2  1 
ATOM   2697 H HB3  A PHE   A 1 132 ? 19.768 -1.544  -6.305  0.68 13.66 ?  132 PHE   A HB3  1 
ATOM   2698 H HB3  B PHE   A 1 132 ? 20.140 -1.658  -6.590  0.32 14.61 ?  132 PHE   A HB3  1 
ATOM   2699 H HD1  A PHE   A 1 132 ? 19.877 1.281   -4.097  0.68 15.30 ?  132 PHE   A HD1  1 
ATOM   2700 H HD1  B PHE   A 1 132 ? 19.650 0.679   -3.938  0.32 15.00 ?  132 PHE   A HD1  1 
ATOM   2701 H HD2  A PHE   A 1 132 ? 22.056 -1.505  -5.972  0.68 15.13 ?  132 PHE   A HD2  1 
ATOM   2702 H HD2  B PHE   A 1 132 ? 22.387 -1.178  -6.188  0.32 14.62 ?  132 PHE   A HD2  1 
ATOM   2703 H HE1  A PHE   A 1 132 ? 21.802 2.138   -3.139  0.68 15.36 ?  132 PHE   A HE1  1 
ATOM   2704 H HE1  B PHE   A 1 132 ? 21.333 1.605   -2.653  0.32 14.57 ?  132 PHE   A HE1  1 
ATOM   2705 H HE2  A PHE   A 1 132 ? 23.979 -0.651  -5.016  0.68 16.00 ?  132 PHE   A HE2  1 
ATOM   2706 H HE2  B PHE   A 1 132 ? 24.070 -0.254  -4.905  0.32 14.46 ?  132 PHE   A HE2  1 
ATOM   2707 H HZ   A PHE   A 1 132 ? 23.852 1.178   -3.596  0.68 15.81 ?  132 PHE   A HZ   1 
ATOM   2708 H HZ   B PHE   A 1 132 ? 23.544 1.142   -3.135  0.32 14.33 ?  132 PHE   A HZ   1 
ATOM   2709 N N    A GLY   A 1 133 ? 16.597 -0.533  -7.704  0.68 12.06 ?  133 GLY   A N    1 
ATOM   2710 N N    B GLY   A 1 133 ? 16.921 -0.672  -8.077  0.32 13.01 ?  133 GLY   A N    1 
ATOM   2711 C CA   A GLY   A 1 133 ? 15.804 -0.900  -8.864  0.68 12.84 ?  133 GLY   A CA   1 
ATOM   2712 C CA   B GLY   A 1 133 ? 16.138 -1.057  -9.229  0.32 13.22 ?  133 GLY   A CA   1 
ATOM   2713 C C    A GLY   A 1 133 ? 15.542 -2.372  -9.108  0.68 13.73 ?  133 GLY   A C    1 
ATOM   2714 C C    B GLY   A 1 133 ? 15.530 -2.448  -9.190  0.32 13.51 ?  133 GLY   A C    1 
ATOM   2715 O O    A GLY   A 1 133 ? 14.998 -2.704  -10.168 0.68 15.13 ?  133 GLY   A O    1 
ATOM   2716 O O    B GLY   A 1 133 ? 14.554 -2.693  -9.910  0.32 13.91 ?  133 GLY   A O    1 
ATOM   2717 H H    A GLY   A 1 133 ? 16.127 -0.292  -7.025  0.68 14.45 ?  133 GLY   A H    1 
ATOM   2718 H H    B GLY   A 1 133 ? 16.442 -0.415  -7.411  0.32 15.59 ?  133 GLY   A H    1 
ATOM   2719 H HA2  A GLY   A 1 133 ? 14.938 -0.471  -8.794  0.68 15.38 ?  133 GLY   A HA2  1 
ATOM   2720 H HA2  B GLY   A 1 133 ? 15.407 -0.439  -9.310  0.32 15.84 ?  133 GLY   A HA2  1 
ATOM   2721 H HA3  A GLY   A 1 133 ? 16.239 -0.555  -9.658  0.68 15.38 ?  133 GLY   A HA3  1 
ATOM   2722 H HA3  B GLY   A 1 133 ? 16.682 -0.963  -10.025 0.32 15.84 ?  133 GLY   A HA3  1 
ATOM   2723 N N    A ALA   A 1 134 ? 15.901 -3.269  -8.190  0.68 13.70 ?  134 ALA   A N    1 
ATOM   2724 N N    B ALA   A 1 134 ? 16.062 -3.359  -8.380  0.32 13.46 ?  134 ALA   A N    1 
ATOM   2725 C CA   A ALA   A 1 134 ? 15.587 -4.676  -8.384  0.68 14.59 ?  134 ALA   A CA   1 
ATOM   2726 C CA   B ALA   A 1 134 ? 15.591 -4.736  -8.418  0.32 13.68 ?  134 ALA   A CA   1 
ATOM   2727 C C    A ALA   A 1 134 ? 14.223 -5.006  -7.778  0.68 15.19 ?  134 ALA   A C    1 
ATOM   2728 C C    B ALA   A 1 134 ? 14.270 -4.895  -7.666  0.32 13.80 ?  134 ALA   A C    1 
ATOM   2729 O O    A ALA   A 1 134 ? 13.643 -4.226  -7.021  0.68 15.97 ?  134 ALA   A O    1 
ATOM   2730 O O    B ALA   A 1 134 ? 13.903 -4.085  -6.809  0.32 13.95 ?  134 ALA   A O    1 
ATOM   2731 C CB   A ALA   A 1 134 ? 16.681 -5.569  -7.796  0.68 15.49 ?  134 ALA   A CB   1 
ATOM   2732 C CB   B ALA   A 1 134 ? 16.637 -5.681  -7.830  0.32 14.06 ?  134 ALA   A CB   1 
ATOM   2733 H H    A ALA   A 1 134 ? 16.330 -3.086  -7.462  0.68 16.42 ?  134 ALA   A H    1 
ATOM   2734 H H    B ALA   A 1 134 ? 16.691 -3.208  -7.812  0.32 16.13 ?  134 ALA   A H    1 
ATOM   2735 H HA   A ALA   A 1 134 ? 15.541 -4.859  -9.335  0.68 17.49 ?  134 ALA   A HA   1 
ATOM   2736 H HA   B ALA   A 1 134 ? 15.444 -4.988  -9.342  0.32 16.39 ?  134 ALA   A HA   1 
ATOM   2737 H HB1  A ALA   A 1 134 ? 16.453 -6.497  -7.964  0.68 18.56 ?  134 ALA   A HB1  1 
ATOM   2738 H HB1  B ALA   A 1 134 ? 16.301 -6.589  -7.876  0.32 16.85 ?  134 ALA   A HB1  1 
ATOM   2739 H HB2  A ALA   A 1 134 ? 17.528 -5.356  -8.225  0.68 18.56 ?  134 ALA   A HB2  1 
ATOM   2740 H HB2  B ALA   A 1 134 ? 17.455 -5.604  -8.346  0.32 16.85 ?  134 ALA   A HB2  1 
ATOM   2741 H HB3  A ALA   A 1 134 ? 16.744 -5.409  -6.844  0.68 18.56 ?  134 ALA   A HB3  1 
ATOM   2742 H HB3  B ALA   A 1 134 ? 16.803 -5.434  -6.908  0.32 16.85 ?  134 ALA   A HB3  1 
ATOM   2743 N N    A ASP   A 1 135 ? 13.715 -6.184  -8.126  0.68 15.53 ?  135 ASP   A N    1 
ATOM   2744 N N    B ASP   A 1 135 ? 13.564 -5.975  -7.993  0.32 14.25 ?  135 ASP   A N    1 
ATOM   2745 C CA   A ASP   A 1 135 ? 12.456 -6.675  -7.568  0.68 16.22 ?  135 ASP   A CA   1 
ATOM   2746 C CA   B ASP   A 1 135 ? 12.304 -6.309  -7.337  0.32 14.60 ?  135 ASP   A CA   1 
ATOM   2747 C C    A ASP   A 1 135 ? 12.691 -7.111  -6.127  0.68 15.47 ?  135 ASP   A C    1 
ATOM   2748 C C    B ASP   A 1 135 ? 12.596 -6.833  -5.937  0.32 13.97 ?  135 ASP   A C    1 
ATOM   2749 O O    A ASP   A 1 135 ? 13.488 -8.028  -5.894  0.68 15.16 ?  135 ASP   A O    1 
ATOM   2750 O O    B ASP   A 1 135 ? 13.273 -7.861  -5.801  0.32 13.75 ?  135 ASP   A O    1 
ATOM   2751 C CB   A ASP   A 1 135 ? 11.991 -7.868  -8.403  0.68 18.06 ?  135 ASP   A CB   1 
ATOM   2752 C CB   B ASP   A 1 135 ? 11.589 -7.381  -8.156  0.32 15.35 ?  135 ASP   A CB   1 
ATOM   2753 C CG   A ASP   A 1 135 ? 10.694 -8.495  -7.897  0.68 19.90 ?  135 ASP   A CG   1 
ATOM   2754 C CG   B ASP   A 1 135 ? 10.225 -7.749  -7.591  0.32 16.31 ?  135 ASP   A CG   1 
ATOM   2755 O OD1  A ASP   A 1 135 ? 10.129 -8.032  -6.886  0.68 19.63 ?  135 ASP   A OD1  1 
ATOM   2756 O OD1  B ASP   A 1 135 ? 9.898  -7.325  -6.461  0.32 16.29 ?  135 ASP   A OD1  1 
ATOM   2757 O OD2  A ASP   A 1 135 ? 10.242 -9.471  -8.529  0.68 22.62 -1 135 ASP   A OD2  1 
ATOM   2758 O OD2  B ASP   A 1 135 ? 9.476  -8.469  -8.286  0.32 17.13 -1 135 ASP   A OD2  1 
ATOM   2759 H H    A ASP   A 1 135 ? 14.079 -6.720  -8.691  0.68 18.62 ?  135 ASP   A H    1 
ATOM   2760 H H    B ASP   A 1 135 ? 13.795 -6.540  -8.595  0.32 17.07 ?  135 ASP   A H    1 
ATOM   2761 H HA   A ASP   A 1 135 ? 11.783 -5.976  -7.607  0.68 19.44 ?  135 ASP   A HA   1 
ATOM   2762 H HA   B ASP   A 1 135 ? 11.734 -5.524  -7.293  0.32 17.49 ?  135 ASP   A HA   1 
ATOM   2763 H HB2  A ASP   A 1 135 ? 11.844 -7.576  -9.315  0.68 21.65 ?  135 ASP   A HB2  1 
ATOM   2764 H HB2  B ASP   A 1 135 ? 11.470 -7.056  -9.062  0.32 18.40 ?  135 ASP   A HB2  1 
ATOM   2765 H HB3  A ASP   A 1 135 ? 12.676 -8.552  -8.379  0.68 21.65 ?  135 ASP   A HB3  1 
ATOM   2766 H HB3  B ASP   A 1 135 ? 12.126 -8.186  -8.159  0.32 18.40 ?  135 ASP   A HB3  1 
ATOM   2767 N N    A PRO   A 1 136 ? 12.045 -6.491  -5.135  0.68 14.86 ?  136 PRO   A N    1 
ATOM   2768 N N    B PRO   A 1 136 ? 12.123 -6.172  -4.879  0.32 13.67 ?  136 PRO   A N    1 
ATOM   2769 C CA   A PRO   A 1 136 ? 12.279 -6.917  -3.744  0.68 14.98 ?  136 PRO   A CA   1 
ATOM   2770 C CA   B PRO   A 1 136 ? 12.428 -6.649  -3.518  0.32 13.78 ?  136 PRO   A CA   1 
ATOM   2771 C C    A PRO   A 1 136 ? 11.874 -8.353  -3.463  0.68 14.15 ?  136 PRO   A C    1 
ATOM   2772 C C    B PRO   A 1 136 ? 11.915 -8.050  -3.214  0.32 13.03 ?  136 PRO   A C    1 
ATOM   2773 O O    A PRO   A 1 136 ? 12.499 -9.001  -2.615  0.68 13.99 ?  136 PRO   A O    1 
ATOM   2774 O O    B PRO   A 1 136 ? 12.455 -8.705  -2.314  0.32 12.40 ?  136 PRO   A O    1 
ATOM   2775 C CB   A PRO   A 1 136 ? 11.466 -5.907  -2.920  0.68 15.61 ?  136 PRO   A CB   1 
ATOM   2776 C CB   B PRO   A 1 136 ? 11.803 -5.578  -2.610  0.32 14.39 ?  136 PRO   A CB   1 
ATOM   2777 C CG   A PRO   A 1 136 ? 10.459 -5.351  -3.867  0.68 16.28 ?  136 PRO   A CG   1 
ATOM   2778 C CG   B PRO   A 1 136 ? 10.906 -4.772  -3.498  0.32 14.92 ?  136 PRO   A CG   1 
ATOM   2779 C CD   A PRO   A 1 136 ? 11.089 -5.374  -5.222  0.68 15.22 ?  136 PRO   A CD   1 
ATOM   2780 C CD   B PRO   A 1 136 ? 11.426 -4.876  -4.876  0.32 14.19 ?  136 PRO   A CD   1 
ATOM   2781 H HA   A PRO   A 1 136 ? 13.220 -6.817  -3.521  0.68 17.95 ?  136 PRO   A HA   1 
ATOM   2782 H HA   B PRO   A 1 136 ? 13.383 -6.641  -3.375  0.32 16.51 ?  136 PRO   A HA   1 
ATOM   2783 H HB2  A PRO   A 1 136 ? 11.031 -6.366  -2.183  0.68 18.71 ?  136 PRO   A HB2  1 
ATOM   2784 H HB2  B PRO   A 1 136 ? 11.295 -5.999  -1.902  0.32 17.25 ?  136 PRO   A HB2  1 
ATOM   2785 H HB3  A PRO   A 1 136 ? 12.055 -5.211  -2.590  0.68 18.71 ?  136 PRO   A HB3  1 
ATOM   2786 H HB3  B PRO   A 1 136 ? 12.502 -5.013  -2.236  0.32 17.25 ?  136 PRO   A HB3  1 
ATOM   2787 H HG2  A PRO   A 1 136 ? 9.666  -5.907  -3.853  0.68 19.51 ?  136 PRO   A HG2  1 
ATOM   2788 H HG2  B PRO   A 1 136 ? 10.012 -5.133  -3.466  0.32 17.88 ?  136 PRO   A HG2  1 
ATOM   2789 H HG3  A PRO   A 1 136 ? 10.247 -4.444  -3.610  0.68 19.51 ?  136 PRO   A HG3  1 
ATOM   2790 H HG3  B PRO   A 1 136 ? 10.910 -3.843  -3.214  0.32 17.88 ?  136 PRO   A HG3  1 
ATOM   2791 H HD2  A PRO   A 1 136 ? 10.419 -5.563  -5.900  0.68 18.24 ?  136 PRO   A HD2  1 
ATOM   2792 H HD2  B PRO   A 1 136 ? 10.690 -4.882  -5.511  0.32 17.01 ?  136 PRO   A HD2  1 
ATOM   2793 H HD3  A PRO   A 1 136 ? 11.552 -4.543  -5.400  0.68 18.24 ?  136 PRO   A HD3  1 
ATOM   2794 H HD3  B PRO   A 1 136 ? 12.050 -4.156  -5.065  0.32 17.01 ?  136 PRO   A HD3  1 
ATOM   2795 N N    A ILE   A 1 137 ? 10.834 -8.867  -4.127  0.68 14.22 ?  137 ILE   A N    1 
ATOM   2796 N N    B ILE   A 1 137 ? 10.898 -8.535  -3.932  0.32 13.41 ?  137 ILE   A N    1 
ATOM   2797 C CA   A ILE   A 1 137 ? 10.473 -10.272 -3.949  0.68 14.66 ?  137 ILE   A CA   1 
ATOM   2798 C CA   B ILE   A 1 137 ? 10.459 -9.919  -3.753  0.32 13.71 ?  137 ILE   A CA   1 
ATOM   2799 C C    A ILE   A 1 137 ? 11.635 -11.165 -4.358  0.68 14.22 ?  137 ILE   A C    1 
ATOM   2800 C C    B ILE   A 1 137 ? 11.580 -10.877 -4.141  0.32 13.56 ?  137 ILE   A C    1 
ATOM   2801 O O    A ILE   A 1 137 ? 11.940 -12.162 -3.692  0.68 14.63 ?  137 ILE   A O    1 
ATOM   2802 O O    B ILE   A 1 137 ? 11.874 -11.846 -3.430  0.32 13.57 ?  137 ILE   A O    1 
ATOM   2803 C CB   A ILE   A 1 137 ? 9.183  -10.605 -4.723  0.68 16.23 ?  137 ILE   A CB   1 
ATOM   2804 C CB   B ILE   A 1 137 ? 9.179  -10.188 -4.566  0.32 14.36 ?  137 ILE   A CB   1 
ATOM   2805 C CG1  A ILE   A 1 137 ? 7.999  -9.788  -4.187  0.68 18.14 ?  137 ILE   A CG1  1 
ATOM   2806 C CG1  B ILE   A 1 137 ? 8.059  -9.219  -4.167  0.32 15.59 ?  137 ILE   A CG1  1 
ATOM   2807 C CG2  A ILE   A 1 137 ? 8.880  -12.100 -4.637  0.68 16.79 ?  137 ILE   A CG2  1 
ATOM   2808 C CG2  B ILE   A 1 137 ? 8.733  -11.640 -4.397  0.32 14.44 ?  137 ILE   A CG2  1 
ATOM   2809 C CD1  A ILE   A 1 137 ? 6.704  -9.988  -4.950  0.68 19.49 ?  137 ILE   A CD1  1 
ATOM   2810 C CD1  B ILE   A 1 137 ? 6.819  -9.350  -5.022  0.32 16.21 ?  137 ILE   A CD1  1 
ATOM   2811 H H    A ILE   A 1 137 ? 10.337 -8.438  -4.677  0.68 17.04 ?  137 ILE   A H    1 
ATOM   2812 H H    B ILE   A 1 137 ? 10.453 -8.086  -4.516  0.32 16.07 ?  137 ILE   A H    1 
ATOM   2813 H HA   A ILE   A 1 137 ? 10.307 -10.440 -3.013  0.68 17.56 ?  137 ILE   A HA   1 
ATOM   2814 H HA   B ILE   A 1 137 ? 10.252 -10.064 -2.817  0.32 16.43 ?  137 ILE   A HA   1 
ATOM   2815 H HB   A ILE   A 1 137 ? 9.311  -10.379 -5.655  0.68 19.45 ?  137 ILE   A HB   1 
ATOM   2816 H HB   B ILE   A 1 137 ? 9.379  -10.041 -5.501  0.32 17.21 ?  137 ILE   A HB   1 
ATOM   2817 H HG12 A ILE   A 1 137 ? 7.844  -10.033 -3.262  0.68 21.75 ?  137 ILE   A HG12 1 
ATOM   2818 H HG12 B ILE   A 1 137 ? 7.806  -9.389  -3.247  0.32 18.69 ?  137 ILE   A HG12 1 
ATOM   2819 H HG13 A ILE   A 1 137 ? 8.231  -8.844  -4.238  0.68 21.75 ?  137 ILE   A HG13 1 
ATOM   2820 H HG13 B ILE   A 1 137 ? 8.379  -8.307  -4.257  0.32 18.69 ?  137 ILE   A HG13 1 
ATOM   2821 H HG21 A ILE   A 1 137 ? 7.994  -12.280 -4.993  0.68 20.13 ?  137 ILE   A HG21 1 
ATOM   2822 H HG21 B ILE   A 1 137 ? 7.874  -11.764 -4.831  0.32 17.31 ?  137 ILE   A HG21 1 
ATOM   2823 H HG22 A ILE   A 1 137 ? 9.537  -12.586 -5.155  0.68 20.13 ?  137 ILE   A HG22 1 
ATOM   2824 H HG22 B ILE   A 1 137 ? 9.391  -12.222 -4.804  0.32 17.31 ?  137 ILE   A HG22 1 
ATOM   2825 H HG23 A ILE   A 1 137 ? 8.917  -12.374 -3.709  0.68 20.13 ?  137 ILE   A HG23 1 
ATOM   2826 H HG23 B ILE   A 1 137 ? 8.655  -11.836 -3.451  0.32 17.31 ?  137 ILE   A HG23 1 
ATOM   2827 H HD11 A ILE   A 1 137 ? 6.021  -10.297 -4.336  0.68 23.37 ?  137 ILE   A HD11 1 
ATOM   2828 H HD11 B ILE   A 1 137 ? 6.521  -8.470  -5.291  0.32 19.43 ?  137 ILE   A HD11 1 
ATOM   2829 H HD12 A ILE   A 1 137 ? 6.449  -9.140  -5.339  0.68 23.37 ?  137 ILE   A HD12 1 
ATOM   2830 H HD12 B ILE   A 1 137 ? 7.035  -9.876  -5.807  0.32 19.43 ?  137 ILE   A HD12 1 
ATOM   2831 H HD13 A ILE   A 1 137 ? 6.841  -10.637 -5.655  0.68 23.37 ?  137 ILE   A HD13 1 
ATOM   2832 H HD13 B ILE   A 1 137 ? 6.128  -9.798  -4.508  0.32 19.43 ?  137 ILE   A HD13 1 
ATOM   2833 N N    A HIS   A 1 138 ? 12.295 -10.823 -5.465  0.68 14.31 ?  138 HIS   A N    1 
ATOM   2834 N N    B HIS   A 1 138 ? 12.217 -10.619 -5.286  0.32 13.87 ?  138 HIS   A N    1 
ATOM   2835 C CA   A HIS   A 1 138 ? 13.492 -11.552 -5.864  0.68 14.46 ?  138 HIS   A CA   1 
ATOM   2836 C CA   B HIS   A 1 138 ? 13.318 -11.461 -5.746  0.32 13.92 ?  138 HIS   A CA   1 
ATOM   2837 C C    A HIS   A 1 138 ? 14.612 -11.391 -4.840  0.68 13.75 ?  138 HIS   A C    1 
ATOM   2838 C C    B HIS   A 1 138 ? 14.507 -11.379 -4.798  0.32 13.77 ?  138 HIS   A C    1 
ATOM   2839 O O    A HIS   A 1 138 ? 15.289 -12.368 -4.494  0.68 14.10 ?  138 HIS   A O    1 
ATOM   2840 O O    B HIS   A 1 138 ? 15.139 -12.396 -4.485  0.32 14.10 ?  138 HIS   A O    1 
ATOM   2841 C CB   A HIS   A 1 138 ? 13.936 -11.102 -7.254  0.68 15.53 ?  138 HIS   A CB   1 
ATOM   2842 C CB   B HIS   A 1 138 ? 13.718 -11.032 -7.159  0.32 14.07 ?  138 HIS   A CB   1 
ATOM   2843 C CG   A HIS   A 1 138 ? 15.192 -11.768 -7.719  0.68 16.76 ?  138 HIS   A CG   1 
ATOM   2844 C CG   B HIS   A 1 138 ? 15.006 -11.630 -7.633  0.32 14.86 ?  138 HIS   A CG   1 
ATOM   2845 N ND1  A HIS   A 1 138 ? 15.279 -13.127 -7.934  0.68 17.93 ?  138 HIS   A ND1  1 
ATOM   2846 N ND1  B HIS   A 1 138 ? 15.143 -12.970 -7.923  0.32 15.71 ?  138 HIS   A ND1  1 
ATOM   2847 C CD2  A HIS   A 1 138 ? 16.417 -11.263 -7.991  0.68 17.00 ?  138 HIS   A CD2  1 
ATOM   2848 C CD2  B HIS   A 1 138 ? 16.214 -11.067 -7.871  0.32 15.00 ?  138 HIS   A CD2  1 
ATOM   2849 C CE1  A HIS   A 1 138 ? 16.503 -13.429 -8.327  0.68 18.38 ?  138 HIS   A CE1  1 
ATOM   2850 C CE1  B HIS   A 1 138 ? 16.382 -13.207 -8.317  0.32 15.91 ?  138 HIS   A CE1  1 
ATOM   2851 N NE2  A HIS   A 1 138 ? 17.213 -12.317 -8.369  0.68 17.83 ?  138 HIS   A NE2  1 
ATOM   2852 N NE2  B HIS   A 1 138 ? 17.053 -12.069 -8.294  0.32 15.54 ?  138 HIS   A NE2  1 
ATOM   2853 H H    A HIS   A 1 138 ? 12.068 -10.183 -6.001  0.68 17.14 ?  138 HIS   A H    1 
ATOM   2854 H H    B HIS   A 1 138 ? 12.029 -9.960  -5.808  0.32 16.62 ?  138 HIS   A H    1 
ATOM   2855 H HA   A HIS   A 1 138 ? 13.274 -12.492 -5.925  0.68 17.33 ?  138 HIS   A HA   1 
ATOM   2856 H HA   B HIS   A 1 138 ? 13.019 -12.380 -5.781  0.32 16.68 ?  138 HIS   A HA   1 
ATOM   2857 H HB2  A HIS   A 1 138 ? 13.231 -11.310 -7.895  0.68 18.61 ?  138 HIS   A HB2  1 
ATOM   2858 H HB2  B HIS   A 1 138 ? 13.019 -11.303 -7.777  0.32 16.86 ?  138 HIS   A HB2  1 
ATOM   2859 H HB3  A HIS   A 1 138 ? 14.091 -10.144 -7.244  0.68 18.61 ?  138 HIS   A HB3  1 
ATOM   2860 H HB3  B HIS   A 1 138 ? 13.814 -10.066 -7.179  0.32 16.86 ?  138 HIS   A HB3  1 
ATOM   2861 H HD1  B HIS   A 1 138 ? 14.519 -13.559 -7.856  0.32 18.82 ?  138 HIS   A HD1  1 
ATOM   2862 H HD2  A HIS   A 1 138 ? 16.666 -10.370 -7.934  0.68 20.38 ?  138 HIS   A HD2  1 
ATOM   2863 H HD2  B HIS   A 1 138 ? 16.433 -10.170 -7.767  0.32 17.97 ?  138 HIS   A HD2  1 
ATOM   2864 H HE1  A HIS   A 1 138 ? 16.806 -14.280 -8.538  0.68 22.04 ?  138 HIS   A HE1  1 
ATOM   2865 H HE1  B HIS   A 1 138 ? 16.722 -14.036 -8.568  0.32 19.07 ?  138 HIS   A HE1  1 
ATOM   2866 H HE2  A HIS   A 1 138 ? 18.036 -12.260 -8.596  0.68 21.37 ?  138 HIS   A HE2  1 
ATOM   2867 N N    . SER   A 1 139 ? 14.825 -10.172 -4.335  1.00 13.53 ?  139 SER   A N    1 
ATOM   2868 C CA   . SER   A 1 139 ? 15.899 -9.990  -3.367  1.00 13.23 ?  139 SER   A CA   1 
ATOM   2869 C C    . SER   A 1 139 ? 15.679 -10.841 -2.121  1.00 12.90 ?  139 SER   A C    1 
ATOM   2870 O O    . SER   A 1 139 ? 16.626 -11.440 -1.597  1.00 12.97 ?  139 SER   A O    1 
ATOM   2871 C CB   . SER   A 1 139 ? 16.029 -8.512  -3.006  1.00 13.29 ?  139 SER   A CB   1 
ATOM   2872 O OG   . SER   A 1 139 ? 17.108 -8.350  -2.105  1.00 13.43 ?  139 SER   A OG   1 
ATOM   2873 H H    A SER   A 1 139 ? 14.379 -9.461  -4.528  0.68 16.21 ?  139 SER   A H    1 
ATOM   2874 H H    B SER   A 1 139 ? 14.428 -9.443  -4.562  0.32 16.21 ?  139 SER   A H    1 
ATOM   2875 H HA   . SER   A 1 139 ? 16.737 -10.265 -3.770  1.00 15.85 ?  139 SER   A HA   1 
ATOM   2876 H HB2  . SER   A 1 139 ? 16.198 -7.991  -3.808  1.00 15.92 ?  139 SER   A HB2  1 
ATOM   2877 H HB3  . SER   A 1 139 ? 15.208 -8.207  -2.579  1.00 15.92 ?  139 SER   A HB3  1 
ATOM   2878 H HG   . SER   A 1 139 ? 17.195 -7.540  -1.893  1.00 16.09 ?  139 SER   A HG   1 
ATOM   2879 N N    . LEU   A 1 140 ? 14.442 -10.907 -1.628  1.00 12.90 ?  140 LEU   A N    1 
ATOM   2880 C CA   . LEU   A 1 140 ? 14.174 -11.733 -0.453  1.00 12.72 ?  140 LEU   A CA   1 
ATOM   2881 C C    . LEU   A 1 140 ? 14.432 -13.209 -0.743  1.00 13.05 ?  140 LEU   A C    1 
ATOM   2882 O O    . LEU   A 1 140 ? 14.975 -13.937 0.102   1.00 13.65 ?  140 LEU   A O    1 
ATOM   2883 C CB   . LEU   A 1 140 ? 12.733 -11.512 0.008   1.00 13.38 ?  140 LEU   A CB   1 
ATOM   2884 C CG   . LEU   A 1 140 ? 12.264 -12.363 1.189   1.00 14.13 ?  140 LEU   A CG   1 
ATOM   2885 C CD1  . LEU   A 1 140 ? 13.164 -12.177 2.409   1.00 14.61 ?  140 LEU   A CD1  1 
ATOM   2886 C CD2  . LEU   A 1 140 ? 10.804 -12.051 1.531   1.00 14.91 ?  140 LEU   A CD2  1 
ATOM   2887 H H    . LEU   A 1 140 ? 13.757 -10.496 -1.948  1.00 15.46 ?  140 LEU   A H    1 
ATOM   2888 H HA   . LEU   A 1 140 ? 14.762 -11.461 0.265   1.00 15.24 ?  140 LEU   A HA   1 
ATOM   2889 H HB2  . LEU   A 1 140 ? 12.633 -10.588 0.266   1.00 16.03 ?  140 LEU   A HB2  1 
ATOM   2890 H HB3  . LEU   A 1 140 ? 12.143 -11.709 -0.736  1.00 16.03 ?  140 LEU   A HB3  1 
ATOM   2891 H HG   . LEU   A 1 140 ? 12.300 -13.300 0.937   1.00 16.93 ?  140 LEU   A HG   1 
ATOM   2892 H HD11 . LEU   A 1 140 ? 12.785 -12.666 3.158   1.00 17.51 ?  140 LEU   A HD11 1 
ATOM   2893 H HD12 . LEU   A 1 140 ? 14.045 -12.527 2.202   1.00 17.51 ?  140 LEU   A HD12 1 
ATOM   2894 H HD13 . LEU   A 1 140 ? 13.218 -11.236 2.620   1.00 17.51 ?  140 LEU   A HD13 1 
ATOM   2895 H HD21 . LEU   A 1 140 ? 10.523 -12.611 2.277   1.00 17.87 ?  140 LEU   A HD21 1 
ATOM   2896 H HD22 . LEU   A 1 140 ? 10.727 -11.116 1.778   1.00 17.87 ?  140 LEU   A HD22 1 
ATOM   2897 H HD23 . LEU   A 1 140 ? 10.246 -12.236 0.758   1.00 17.87 ?  140 LEU   A HD23 1 
ATOM   2898 N N    . ARG   A 1 141 ? 14.040 -13.672 -1.933  1.00 13.54 ?  141 ARG   A N    1 
ATOM   2899 C CA   . ARG   A 1 141 ? 14.287 -15.059 -2.308  1.00 14.66 ?  141 ARG   A CA   1 
ATOM   2900 C C    . ARG   A 1 141 ? 15.782 -15.361 -2.315  1.00 13.86 ?  141 ARG   A C    1 
ATOM   2901 O O    . ARG   A 1 141 ? 16.228 -16.377 -1.767  1.00 13.97 ?  141 ARG   A O    1 
ATOM   2902 C CB   . ARG   A 1 141 ? 13.678 -15.308 -3.690  1.00 16.61 ?  141 ARG   A CB   1 
ATOM   2903 C CG   . ARG   A 1 141 ? 13.689 -16.750 -4.155  1.00 19.68 ?  141 ARG   A CG   1 
ATOM   2904 C CD   . ARG   A 1 141 ? 12.658 -17.550 -3.415  1.00 22.25 ?  141 ARG   A CD   1 
ATOM   2905 N NE   . ARG   A 1 141 ? 13.263 -18.329 -2.347  1.00 22.94 ?  141 ARG   A NE   1 
ATOM   2906 C CZ   . ARG   A 1 141 ? 12.573 -18.898 -1.367  1.00 23.36 ?  141 ARG   A CZ   1 
ATOM   2907 N NH1  . ARG   A 1 141 ? 11.277 -18.681 -1.217  1.00 23.11 ?  141 ARG   A NH1  1 
ATOM   2908 N NH2  . ARG   A 1 141 ? 13.203 -19.693 -0.507  1.00 24.07 ?  141 ARG   A NH2  1 
ATOM   2909 H H    . ARG   A 1 141 ? 13.637 -13.206 -2.533  1.00 16.23 ?  141 ARG   A H    1 
ATOM   2910 H HA   . ARG   A 1 141 ? 13.861 -15.648 -1.672  1.00 17.57 ?  141 ARG   A HA   1 
ATOM   2911 H HB2  . ARG   A 1 141 ? 12.757 -15.008 -3.680  1.00 19.91 ?  141 ARG   A HB2  1 
ATOM   2912 H HB3  . ARG   A 1 141 ? 14.178 -14.791 -4.341  1.00 19.91 ?  141 ARG   A HB3  1 
ATOM   2913 H HG2  . ARG   A 1 141 ? 13.485 -16.785 -5.105  1.00 23.59 ?  141 ARG   A HG2  1 
ATOM   2914 H HG3  . ARG   A 1 141 ? 14.563 -17.142 -3.988  1.00 23.59 ?  141 ARG   A HG3  1 
ATOM   2915 H HD2  . ARG   A 1 141 ? 12.011 -16.950 -3.013  1.00 26.67 ?  141 ARG   A HD2  1 
ATOM   2916 H HD3  . ARG   A 1 141 ? 12.213 -18.152 -4.035  1.00 26.67 ?  141 ARG   A HD3  1 
ATOM   2917 H HE   . ARG   A 1 141 ? 14.092 -18.541 -2.425  1.00 27.50 ?  141 ARG   A HE   1 
ATOM   2918 H HH11 . ARG   A 1 141 ? 10.852 -18.182 -1.773  1.00 27.71 ?  141 ARG   A HH11 1 
ATOM   2919 H HH12 . ARG   A 1 141 ? 10.849 -19.057 -0.569  1.00 27.71 ?  141 ARG   A HH12 1 
ATOM   2920 H HH21 . ARG   A 1 141 ? 14.046 -19.840 -0.596  1.00 28.87 ?  141 ARG   A HH21 1 
ATOM   2921 H HH22 . ARG   A 1 141 ? 12.770 -20.057 0.142   1.00 28.87 ?  141 ARG   A HH22 1 
ATOM   2922 N N    . VAL   A 1 142 ? 16.576 -14.492 -2.944  1.00 12.87 ?  142 VAL   A N    1 
ATOM   2923 C CA   . VAL   A 1 142 ? 18.021 -14.704 -2.972  1.00 13.13 ?  142 VAL   A CA   1 
ATOM   2924 C C    . VAL   A 1 142 ? 18.589 -14.690 -1.560  1.00 12.54 ?  142 VAL   A C    1 
ATOM   2925 O O    . VAL   A 1 142 ? 19.448 -15.508 -1.213  1.00 12.66 ?  142 VAL   A O    1 
ATOM   2926 C CB   . VAL   A 1 142 ? 18.719 -13.677 -3.885  1.00 13.36 ?  142 VAL   A CB   1 
ATOM   2927 C CG1  . VAL   A 1 142 ? 20.224 -13.880 -3.841  1.00 13.54 ?  142 VAL   A CG1  1 
ATOM   2928 C CG2  . VAL   A 1 142 ? 18.221 -13.803 -5.313  1.00 14.74 ?  142 VAL   A CG2  1 
ATOM   2929 H H    . VAL   A 1 142 ? 16.308 -13.778 -3.359  1.00 15.42 ?  142 VAL   A H    1 
ATOM   2930 H HA   . VAL   A 1 142 ? 18.194 -15.575 -3.348  1.00 15.73 ?  142 VAL   A HA   1 
ATOM   2931 H HB   . VAL   A 1 142 ? 18.529 -12.775 -3.574  1.00 16.01 ?  142 VAL   A HB   1 
ATOM   2932 H HG11 . VAL   A 1 142 ? 20.636 -13.388 -4.571  1.00 16.22 ?  142 VAL   A HG11 1 
ATOM   2933 H HG12 . VAL   A 1 142 ? 20.570 -13.549 -2.993  1.00 16.22 ?  142 VAL   A HG12 1 
ATOM   2934 H HG13 . VAL   A 1 142 ? 20.421 -14.825 -3.930  1.00 16.22 ?  142 VAL   A HG13 1 
ATOM   2935 H HG21 . VAL   A 1 142 ? 18.696 -13.164 -5.870  1.00 17.66 ?  142 VAL   A HG21 1 
ATOM   2936 H HG22 . VAL   A 1 142 ? 18.398 -14.705 -5.623  1.00 17.66 ?  142 VAL   A HG22 1 
ATOM   2937 H HG23 . VAL   A 1 142 ? 17.273 -13.622 -5.331  1.00 17.66 ?  142 VAL   A HG23 1 
ATOM   2938 N N    . CYS   A 1 143 ? 18.117 -13.769 -0.722  1.00 12.33 ?  143 CYS   A N    1 
ATOM   2939 C CA   . CYS   A 1 143 ? 18.581 -13.723 0.661   1.00 12.84 ?  143 CYS   A CA   1 
ATOM   2940 C C    . CYS   A 1 143 ? 18.358 -15.065 1.351   1.00 12.69 ?  143 CYS   A C    1 
ATOM   2941 O O    . CYS   A 1 143 ? 19.280 -15.650 1.928   1.00 12.35 ?  143 CYS   A O    1 
ATOM   2942 C CB   . CYS   A 1 143 ? 17.842 -12.613 1.405   1.00 13.40 ?  143 CYS   A CB   1 
ATOM   2943 S SG   . CYS   A 1 143 ? 18.325 -12.432 3.132   1.00 13.28 ?  143 CYS   A SG   1 
ATOM   2944 H H    . CYS   A 1 143 ? 17.536 -13.173 -0.925  1.00 14.77 ?  143 CYS   A H    1 
ATOM   2945 H HA   . CYS   A 1 143 ? 19.530 -13.525 0.677   1.00 15.38 ?  143 CYS   A HA   1 
ATOM   2946 H HB2  . CYS   A 1 143 ? 18.011 -11.769 0.958   1.00 16.06 ?  143 CYS   A HB2  1 
ATOM   2947 H HB3  . CYS   A 1 143 ? 16.893 -12.805 1.381   1.00 16.06 ?  143 CYS   A HB3  1 
ATOM   2948 H HG   . CYS   A 1 143 ? 17.740 -11.491 3.590   1.00 15.92 ?  143 CYS   A HG   1 
ATOM   2949 N N    . VAL   A 1 144 ? 17.130 -15.574 1.289   1.00 13.29 ?  144 VAL   A N    1 
ATOM   2950 C CA   . VAL   A 1 144 ? 16.794 -16.809 1.989   1.00 14.68 ?  144 VAL   A CA   1 
ATOM   2951 C C    . VAL   A 1 144 ? 17.606 -17.976 1.450   1.00 14.66 ?  144 VAL   A C    1 
ATOM   2952 O O    . VAL   A 1 144 ? 17.976 -18.889 2.200   1.00 15.43 ?  144 VAL   A O    1 
ATOM   2953 C CB   . VAL   A 1 144 ? 15.276 -17.051 1.887   1.00 17.45 ?  144 VAL   A CB   1 
ATOM   2954 C CG1  . VAL   A 1 144 ? 14.919 -18.486 2.225   1.00 19.56 ?  144 VAL   A CG1  1 
ATOM   2955 C CG2  . VAL   A 1 144 ? 14.535 -16.050 2.780   1.00 17.31 ?  144 VAL   A CG2  1 
ATOM   2956 H H    . VAL   A 1 144 ? 16.476 -15.217 0.854   1.00 15.93 ?  144 VAL   A H    1 
ATOM   2957 H HA   . VAL   A 1 144 ? 17.009 -16.704 2.925   1.00 17.59 ?  144 VAL   A HA   1 
ATOM   2958 H HB   . VAL   A 1 144 ? 14.993 -16.882 0.972   1.00 20.91 ?  144 VAL   A HB   1 
ATOM   2959 H HG11 . VAL   A 1 144 ? 13.969 -18.536 2.421   1.00 23.44 ?  144 VAL   A HG11 1 
ATOM   2960 H HG12 . VAL   A 1 144 ? 15.126 -19.051 1.465   1.00 23.44 ?  144 VAL   A HG12 1 
ATOM   2961 H HG13 . VAL   A 1 144 ? 15.430 -18.763 2.999   1.00 23.44 ?  144 VAL   A HG13 1 
ATOM   2962 H HG21 . VAL   A 1 144 ? 13.580 -16.166 2.666   1.00 20.75 ?  144 VAL   A HG21 1 
ATOM   2963 H HG22 . VAL   A 1 144 ? 14.781 -16.207 3.704   1.00 20.75 ?  144 VAL   A HG22 1 
ATOM   2964 H HG23 . VAL   A 1 144 ? 14.788 -15.145 2.522   1.00 20.75 ?  144 VAL   A HG23 1 
ATOM   2965 N N    . ASP   A 1 145 ? 17.865 -17.990 0.145   1.00 15.02 ?  145 ASP   A N    1 
ATOM   2966 C CA   . ASP   A 1 145 ? 18.585 -19.087 -0.491  1.00 15.75 ?  145 ASP   A CA   1 
ATOM   2967 C C    . ASP   A 1 145 ? 20.104 -18.934 -0.437  1.00 14.92 ?  145 ASP   A C    1 
ATOM   2968 O O    . ASP   A 1 145 ? 20.813 -19.820 -0.923  1.00 16.89 ?  145 ASP   A O    1 
ATOM   2969 C CB   . ASP   A 1 145 ? 18.143 -19.227 -1.951  1.00 17.09 ?  145 ASP   A CB   1 
ATOM   2970 C CG   . ASP   A 1 145 ? 16.694 -19.663 -2.085  1.00 19.29 ?  145 ASP   A CG   1 
ATOM   2971 O OD1  . ASP   A 1 145 ? 16.134 -20.218 -1.116  1.00 19.90 ?  145 ASP   A OD1  1 
ATOM   2972 O OD2  . ASP   A 1 145 ? 16.109 -19.436 -3.164  1.00 20.79 -1 145 ASP   A OD2  1 
ATOM   2973 H H    . ASP   A 1 145 ? 17.608 -17.376 -0.405  1.00 18.00 ?  145 ASP   A H    1 
ATOM   2974 H HA   . ASP   A 1 145 ? 18.354 -19.912 -0.039  1.00 18.88 ?  145 ASP   A HA   1 
ATOM   2975 H HB2  . ASP   A 1 145 ? 18.248 -18.370 -2.397  1.00 20.49 ?  145 ASP   A HB2  1 
ATOM   2976 H HB3  . ASP   A 1 145 ? 18.695 -19.895 -2.385  1.00 20.49 ?  145 ASP   A HB3  1 
ATOM   2977 N N    . THR   A 1 146 ? 20.624 -17.843 0.127   1.00 13.34 ?  146 THR   A N    1 
ATOM   2978 C CA   . THR   A 1 146 ? 22.064 -17.586 0.151   1.00 12.60 ?  146 THR   A CA   1 
ATOM   2979 C C    . THR   A 1 146 ? 22.619 -17.404 1.550   1.00 12.37 ?  146 THR   A C    1 
ATOM   2980 O O    . THR   A 1 146 ? 23.696 -17.934 1.860   1.00 13.20 ?  146 THR   A O    1 
ATOM   2981 C CB   . THR   A 1 146 ? 22.392 -16.334 -0.686  1.00 12.55 ?  146 THR   A CB   1 
ATOM   2982 O OG1  . THR   A 1 146 ? 21.866 -16.498 -2.007  1.00 13.20 ?  146 THR   A OG1  1 
ATOM   2983 C CG2  . THR   A 1 146 ? 23.890 -16.107 -0.767  1.00 12.76 ?  146 THR   A CG2  1 
ATOM   2984 H H    . THR   A 1 146 ? 20.157 -17.217 0.496   1.00 15.99 ?  146 THR   A H    1 
ATOM   2985 H HA   . THR   A 1 146 ? 22.523 -18.334 -0.250  1.00 15.10 ?  146 THR   A HA   1 
ATOM   2986 H HB   . THR   A 1 146 ? 21.992 -15.553 -0.269  1.00 15.03 ?  146 THR   A HB   1 
ATOM   2987 H HG1  . THR   A 1 146 ? 21.028 -16.568 -1.969  1.00 15.81 ?  146 THR   A HG1  1 
ATOM   2988 H HG21 . THR   A 1 146 ? 24.088 -15.443 -1.444  1.00 15.28 ?  146 THR   A HG21 1 
ATOM   2989 H HG22 . THR   A 1 146 ? 24.229 -15.793 0.088   1.00 15.28 ?  146 THR   A HG22 1 
ATOM   2990 H HG23 . THR   A 1 146 ? 24.338 -16.936 -0.998  1.00 15.28 ?  146 THR   A HG23 1 
ATOM   2991 N N    . VAL   A 1 147 ? 21.936 -16.631 2.388   1.00 12.09 ?  147 VAL   A N    1 
ATOM   2992 C CA   . VAL   A 1 147 ? 22.422 -16.331 3.725   1.00 12.31 ?  147 VAL   A CA   1 
ATOM   2993 C C    . VAL   A 1 147 ? 22.108 -17.503 4.645   1.00 12.75 ?  147 VAL   A C    1 
ATOM   2994 O O    . VAL   A 1 147 ? 20.969 -17.984 4.696   1.00 13.32 ?  147 VAL   A O    1 
ATOM   2995 C CB   . VAL   A 1 147 ? 21.802 -15.026 4.243   1.00 12.64 ?  147 VAL   A CB   1 
ATOM   2996 C CG1  . VAL   A 1 147 ? 22.329 -14.724 5.625   1.00 13.32 ?  147 VAL   A CG1  1 
ATOM   2997 C CG2  . VAL   A 1 147 ? 22.072 -13.879 3.273   1.00 12.73 ?  147 VAL   A CG2  1 
ATOM   2998 H H    . VAL   A 1 147 ? 21.175 -16.271 2.206   1.00 14.49 ?  147 VAL   A H    1 
ATOM   2999 H HA   . VAL   A 1 147 ? 23.382 -16.221 3.697   1.00 14.75 ?  147 VAL   A HA   1 
ATOM   3000 H HB   . VAL   A 1 147 ? 20.842 -15.142 4.316   1.00 15.15 ?  147 VAL   A HB   1 
ATOM   3001 H HG11 . VAL   A 1 147 ? 22.096 -13.816 5.859   1.00 15.96 ?  147 VAL   A HG11 1 
ATOM   3002 H HG12 . VAL   A 1 147 ? 21.927 -15.343 6.260   1.00 15.96 ?  147 VAL   A HG12 1 
ATOM   3003 H HG13 . VAL   A 1 147 ? 23.292 -14.834 5.626   1.00 15.96 ?  147 VAL   A HG13 1 
ATOM   3004 H HG21 . VAL   A 1 147 ? 21.743 -13.054 3.665   1.00 15.25 ?  147 VAL   A HG21 1 
ATOM   3005 H HG22 . VAL   A 1 147 ? 23.024 -13.817 3.116   1.00 15.25 ?  147 VAL   A HG22 1 
ATOM   3006 H HG23 . VAL   A 1 147 ? 21.606 -14.057 2.441   1.00 15.25 ?  147 VAL   A HG23 1 
ATOM   3007 N N    . ARG   A 1 148 ? 23.131 -17.977 5.356   1.00 12.90 ?  148 ARG   A N    1 
ATOM   3008 C CA   . ARG   A 1 148 ? 23.000 -19.055 6.322   1.00 12.98 ?  148 ARG   A CA   1 
ATOM   3009 C C    . ARG   A 1 148 ? 23.124 -18.579 7.758   1.00 13.40 ?  148 ARG   A C    1 
ATOM   3010 O O    . ARG   A 1 148 ? 22.725 -19.310 8.675   1.00 15.59 ?  148 ARG   A O    1 
ATOM   3011 C CB   . ARG   A 1 148 ? 24.039 -20.154 6.045   1.00 13.62 ?  148 ARG   A CB   1 
ATOM   3012 C CG   . ARG   A 1 148 ? 23.875 -20.784 4.672   1.00 14.85 ?  148 ARG   A CG   1 
ATOM   3013 C CD   . ARG   A 1 148 ? 24.954 -21.817 4.358   1.00 15.81 ?  148 ARG   A CD   1 
ATOM   3014 N NE   . ARG   A 1 148 ? 26.295 -21.249 4.393   1.00 16.21 ?  148 ARG   A NE   1 
ATOM   3015 C CZ   . ARG   A 1 148 ? 26.811 -20.501 3.426   1.00 15.11 ?  148 ARG   A CZ   1 
ATOM   3016 N NH1  . ARG   A 1 148 ? 26.141 -20.257 2.311   1.00 15.59 ?  148 ARG   A NH1  1 
ATOM   3017 N NH2  . ARG   A 1 148 ? 28.027 -19.975 3.586   1.00 15.45 ?  148 ARG   A NH2  1 
ATOM   3018 H H    . ARG   A 1 148 ? 23.938 -17.677 5.283   1.00 15.46 ?  148 ARG   A H    1 
ATOM   3019 H HA   . ARG   A 1 148 ? 22.126 -19.449 6.226   1.00 15.56 ?  148 ARG   A HA   1 
ATOM   3020 H HB2  . ARG   A 1 148 ? 24.927 -19.781 6.098   1.00 16.32 ?  148 ARG   A HB2  1 
ATOM   3021 H HB3  . ARG   A 1 148 ? 23.933 -20.861 6.706   1.00 16.32 ?  148 ARG   A HB3  1 
ATOM   3022 H HG2  . ARG   A 1 148 ? 23.010 -21.221 4.631   1.00 17.80 ?  148 ARG   A HG2  1 
ATOM   3023 H HG3  . ARG   A 1 148 ? 23.921 -20.081 4.004   1.00 17.80 ?  148 ARG   A HG3  1 
ATOM   3024 H HD2  . ARG   A 1 148 ? 24.912 -22.528 5.015   1.00 18.95 ?  148 ARG   A HD2  1 
ATOM   3025 H HD3  . ARG   A 1 148 ? 24.797 -22.176 3.469   1.00 18.95 ?  148 ARG   A HD3  1 
ATOM   3026 H HE   . ARG   A 1 148 ? 26.782 -21.406 5.081   1.00 19.42 ?  148 ARG   A HE   1 
ATOM   3027 H HH11 . ARG   A 1 148 ? 25.354 -20.579 2.198   1.00 18.68 ?  148 ARG   A HH11 1 
ATOM   3028 H HH12 . ARG   A 1 148 ? 26.492 -19.758 1.699   1.00 18.68 ?  148 ARG   A HH12 1 
ATOM   3029 H HH21 . ARG   A 1 148 ? 28.466 -20.118 4.308   1.00 18.52 ?  148 ARG   A HH21 1 
ATOM   3030 H HH22 . ARG   A 1 148 ? 28.367 -19.478 2.967   1.00 18.52 ?  148 ARG   A HH22 1 
ATOM   3031 N N    . THR   A 1 149 ? 23.673 -17.384 7.969   1.00 13.51 ?  149 THR   A N    1 
ATOM   3032 C CA   . THR   A 1 149 ? 23.754 -16.783 9.287   1.00 13.70 ?  149 THR   A CA   1 
ATOM   3033 C C    . THR   A 1 149 ? 22.428 -16.091 9.598   1.00 13.23 ?  149 THR   A C    1 
ATOM   3034 O O    . THR   A 1 149 ? 21.492 -16.089 8.789   1.00 14.03 ?  149 THR   A O    1 
ATOM   3035 C CB   . THR   A 1 149 ? 24.955 -15.844 9.344   1.00 14.20 ?  149 THR   A CB   1 
ATOM   3036 O OG1  . THR   A 1 149 ? 24.826 -14.908 8.272   1.00 14.32 ?  149 THR   A OG1  1 
ATOM   3037 C CG2  . THR   A 1 149 ? 26.263 -16.639 9.211   1.00 14.73 ?  149 THR   A CG2  1 
ATOM   3038 H H    . THR   A 1 149 ? 24.023 -16.893 7.348   1.00 16.19 ?  149 THR   A H    1 
ATOM   3039 H HA   . THR   A 1 149 ? 23.887 -17.485 9.942   1.00 16.42 ?  149 THR   A HA   1 
ATOM   3040 H HB   . THR   A 1 149 ? 24.955 -15.377 10.192  1.00 17.01 ?  149 THR   A HB   1 
ATOM   3041 H HG1  . THR   A 1 149 ? 25.476 -14.373 8.279   1.00 17.16 ?  149 THR   A HG1  1 
ATOM   3042 H HG21 . THR   A 1 149 ? 27.022 -16.040 9.269   1.00 17.66 ?  149 THR   A HG21 1 
ATOM   3043 H HG22 . THR   A 1 149 ? 26.327 -17.300 9.919   1.00 17.66 ?  149 THR   A HG22 1 
ATOM   3044 H HG23 . THR   A 1 149 ? 26.290 -17.098 8.353   1.00 17.66 ?  149 THR   A HG23 1 
ATOM   3045 N N    . ASN   A 1 150 ? 22.305 -15.551 10.803  1.00 13.26 ?  150 ASN   A N    1 
ATOM   3046 C CA   . ASN   A 1 150 ? 21.021 -15.042 11.284  1.00 14.37 ?  150 ASN   A CA   1 
ATOM   3047 C C    . ASN   A 1 150 ? 20.842 -13.602 10.821  1.00 13.72 ?  150 ASN   A C    1 
ATOM   3048 O O    . ASN   A 1 150 ? 21.588 -12.706 11.241  1.00 15.28 ?  150 ASN   A O    1 
ATOM   3049 C CB   . ASN   A 1 150 ? 20.956 -15.152 12.802  1.00 17.02 ?  150 ASN   A CB   1 
ATOM   3050 C CG   . ASN   A 1 150 ? 20.848 -16.580 13.266  1.00 21.00 ?  150 ASN   A CG   1 
ATOM   3051 O OD1  . ASN   A 1 150 ? 20.219 -17.403 12.602  1.00 22.67 ?  150 ASN   A OD1  1 
ATOM   3052 N ND2  . ASN   A 1 150 ? 21.470 -16.891 14.399  1.00 23.29 ?  150 ASN   A ND2  1 
ATOM   3053 H H    . ASN   A 1 150 ? 22.951 -15.468 11.364  1.00 15.89 ?  150 ASN   A H    1 
ATOM   3054 H HA   . ASN   A 1 150 ? 20.302 -15.583 10.910  1.00 17.22 ?  150 ASN   A HA   1 
ATOM   3055 H HB2  . ASN   A 1 150 ? 21.761 -14.773 13.183  1.00 20.40 ?  150 ASN   A HB2  1 
ATOM   3056 H HB3  . ASN   A 1 150 ? 20.174 -14.678 13.122  1.00 20.40 ?  150 ASN   A HB3  1 
ATOM   3057 H HD21 . ASN   A 1 150 ? 21.442 -17.698 14.709  1.00 27.92 ?  150 ASN   A HD21 1 
ATOM   3058 H HD22 . ASN   A 1 150 ? 21.902 -16.287 14.836  1.00 27.92 ?  150 ASN   A HD22 1 
ATOM   3059 N N    . VAL   A 1 151 ? 19.855 -13.374 9.960   1.00 13.37 ?  151 VAL   A N    1 
ATOM   3060 C CA   . VAL   A 1 151 ? 19.646 -12.066 9.357   1.00 13.36 ?  151 VAL   A CA   1 
ATOM   3061 C C    . VAL   A 1 151 ? 18.262 -11.547 9.725   1.00 13.33 ?  151 VAL   A C    1 
ATOM   3062 O O    . VAL   A 1 151 ? 17.253 -12.255 9.576   1.00 14.50 ?  151 VAL   A O    1 
ATOM   3063 C CB   . VAL   A 1 151 ? 19.931 -12.065 7.839   1.00 14.76 ?  151 VAL   A CB   1 
ATOM   3064 C CG1  . VAL   A 1 151 ? 19.099 -13.097 7.096   1.00 15.87 ?  151 VAL   A CG1  1 
ATOM   3065 C CG2  . VAL   A 1 151 ? 19.748 -10.661 7.259   1.00 15.02 ?  151 VAL   A CG2  1 
ATOM   3066 H H    . VAL   A 1 151 ? 19.291 -13.974 9.705   1.00 16.03 ?  151 VAL   A H    1 
ATOM   3067 H HA   . VAL   A 1 151 ? 20.289 -11.456 9.750   1.00 16.01 ?  151 VAL   A HA   1 
ATOM   3068 H HB   . VAL   A 1 151 ? 20.863 -12.307 7.705   1.00 17.69 ?  151 VAL   A HB   1 
ATOM   3069 H HG11 . VAL   A 1 151 ? 19.298 -13.048 6.146   1.00 19.02 ?  151 VAL   A HG11 1 
ATOM   3070 H HG12 . VAL   A 1 151 ? 19.323 -13.987 7.428   1.00 19.02 ?  151 VAL   A HG12 1 
ATOM   3071 H HG13 . VAL   A 1 151 ? 18.159 -12.921 7.246   1.00 19.02 ?  151 VAL   A HG13 1 
ATOM   3072 H HG21 . VAL   A 1 151 ? 20.060 -10.658 6.336   1.00 18.00 ?  151 VAL   A HG21 1 
ATOM   3073 H HG22 . VAL   A 1 151 ? 18.809 -10.424 7.286   1.00 18.00 ?  151 VAL   A HG22 1 
ATOM   3074 H HG23 . VAL   A 1 151 ? 20.268 -10.032 7.781   1.00 18.00 ?  151 VAL   A HG23 1 
ATOM   3075 N N    . TYR   A 1 152 ? 18.245 -10.308 10.223  1.00 13.18 ?  152 TYR   A N    1 
ATOM   3076 C CA   . TYR   A 1 152 ? 17.049 -9.574  10.609  1.00 12.66 ?  152 TYR   A CA   1 
ATOM   3077 C C    . TYR   A 1 152 ? 16.852 -8.470  9.586   1.00 12.41 ?  152 TYR   A C    1 
ATOM   3078 O O    . TYR   A 1 152 ? 17.624 -7.504  9.550   1.00 12.67 ?  152 TYR   A O    1 
ATOM   3079 C CB   . TYR   A 1 152 ? 17.222 -9.034  12.027  1.00 13.72 ?  152 TYR   A CB   1 
ATOM   3080 C CG   . TYR   A 1 152 ? 17.182 -10.160 13.028  1.00 14.78 ?  152 TYR   A CG   1 
ATOM   3081 C CD1  . TYR   A 1 152 ? 18.311 -10.923 13.298  1.00 16.33 ?  152 TYR   A CD1  1 
ATOM   3082 C CD2  . TYR   A 1 152 ? 16.001 -10.500 13.667  1.00 15.12 ?  152 TYR   A CD2  1 
ATOM   3083 C CE1  . TYR   A 1 152 ? 18.275 -11.977 14.188  1.00 17.59 ?  152 TYR   A CE1  1 
ATOM   3084 C CE2  . TYR   A 1 152 ? 15.950 -11.566 14.565  1.00 16.47 ?  152 TYR   A CE2  1 
ATOM   3085 C CZ   . TYR   A 1 152 ? 17.093 -12.298 14.823  1.00 17.69 ?  152 TYR   A CZ   1 
ATOM   3086 O OH   . TYR   A 1 152 ? 17.052 -13.359 15.710  1.00 19.88 ?  152 TYR   A OH   1 
ATOM   3087 H H    . TYR   A 1 152 ? 18.965 -9.845  10.332  1.00 15.79 ?  152 TYR   A H    1 
ATOM   3088 H HA   . TYR   A 1 152 ? 16.283 -10.167 10.586  1.00 15.17 ?  152 TYR   A HA   1 
ATOM   3089 H HB2  . TYR   A 1 152 ? 18.084 -8.598  12.096  1.00 16.45 ?  152 TYR   A HB2  1 
ATOM   3090 H HB3  . TYR   A 1 152 ? 16.512 -8.413  12.225  1.00 16.45 ?  152 TYR   A HB3  1 
ATOM   3091 H HD1  . TYR   A 1 152 ? 19.110 -10.713 12.867  1.00 19.57 ?  152 TYR   A HD1  1 
ATOM   3092 H HD2  . TYR   A 1 152 ? 15.225 -10.011 13.493  1.00 18.13 ?  152 TYR   A HD2  1 
ATOM   3093 H HE1  . TYR   A 1 152 ? 19.044 -12.466 14.361  1.00 21.09 ?  152 TYR   A HE1  1 
ATOM   3094 H HE2  . TYR   A 1 152 ? 15.151 -11.773 14.996  1.00 19.74 ?  152 TYR   A HE2  1 
ATOM   3095 H HH   . TYR   A 1 152 ? 16.278 -13.424 16.028  1.00 23.84 ?  152 TYR   A HH   1 
ATOM   3096 N N    A LEU   A 1 153 ? 15.842 -8.642  8.732   0.68 12.77 ?  153 LEU   A N    1 
ATOM   3097 N N    B LEU   A 1 153 ? 15.822 -8.605  8.763   0.32 12.38 ?  153 LEU   A N    1 
ATOM   3098 C CA   A LEU   A 1 153 ? 15.584 -7.769  7.593   0.68 12.61 ?  153 LEU   A CA   1 
ATOM   3099 C CA   B LEU   A 1 153 ? 15.540 -7.630  7.723   0.32 12.17 ?  153 LEU   A CA   1 
ATOM   3100 C C    A LEU   A 1 153 ? 14.567 -6.691  7.951   0.68 12.62 ?  153 LEU   A C    1 
ATOM   3101 C C    B LEU   A 1 153 ? 14.592 -6.561  8.249   0.32 12.29 ?  153 LEU   A C    1 
ATOM   3102 O O    A LEU   A 1 153 ? 13.466 -6.995  8.422   0.68 13.60 ?  153 LEU   A O    1 
ATOM   3103 O O    B LEU   A 1 153 ? 13.526 -6.874  8.790   0.32 12.71 ?  153 LEU   A O    1 
ATOM   3104 C CB   A LEU   A 1 153 ? 15.036 -8.585  6.419   0.68 12.42 ?  153 LEU   A CB   1 
ATOM   3105 C CB   B LEU   A 1 153 ? 14.922 -8.317  6.509   0.32 11.81 ?  153 LEU   A CB   1 
ATOM   3106 C CG   A LEU   A 1 153 ? 15.995 -9.588  5.772   0.68 12.54 ?  153 LEU   A CG   1 
ATOM   3107 C CG   B LEU   A 1 153 ? 15.808 -9.356  5.823   0.32 11.90 ?  153 LEU   A CG   1 
ATOM   3108 C CD1  A LEU   A 1 153 ? 15.241 -10.497 4.812   0.68 12.63 ?  153 LEU   A CD1  1 
ATOM   3109 C CD1  B LEU   A 1 153 ? 14.991 -10.160 4.828   0.32 12.06 ?  153 LEU   A CD1  1 
ATOM   3110 C CD2  A LEU   A 1 153 ? 17.112 -8.862  5.041   0.68 13.06 ?  153 LEU   A CD2  1 
ATOM   3111 C CD2  B LEU   A 1 153 ? 16.989 -8.689  5.136   0.32 12.40 ?  153 LEU   A CD2  1 
ATOM   3112 H H    A LEU   A 1 153 ? 15.266 -9.285  8.801   0.68 15.31 ?  153 LEU   A H    1 
ATOM   3113 H H    B LEU   A 1 153 ? 15.261 -9.261  8.787   0.32 14.84 ?  153 LEU   A H    1 
ATOM   3114 H HA   A LEU   A 1 153 ? 16.409 -7.347  7.317   0.68 15.11 ?  153 LEU   A HA   1 
ATOM   3115 H HA   B LEU   A 1 153 ? 16.365 -7.206  7.452   0.32 14.58 ?  153 LEU   A HA   1 
ATOM   3116 H HB2  A LEU   A 1 153 ? 14.266 -9.087  6.727   0.68 14.88 ?  153 LEU   A HB2  1 
ATOM   3117 H HB2  B LEU   A 1 153 ? 14.112 -8.767  6.793   0.32 14.15 ?  153 LEU   A HB2  1 
ATOM   3118 H HB3  A LEU   A 1 153 ? 14.760 -7.970  5.721   0.68 14.88 ?  153 LEU   A HB3  1 
ATOM   3119 H HB3  B LEU   A 1 153 ? 14.703 -7.637  5.852   0.32 14.15 ?  153 LEU   A HB3  1 
ATOM   3120 H HG   A LEU   A 1 153 ? 16.396 -10.142 6.463   0.68 15.02 ?  153 LEU   A HG   1 
ATOM   3121 H HG   B LEU   A 1 153 ? 16.156 -9.966  6.492   0.32 14.26 ?  153 LEU   A HG   1 
ATOM   3122 H HD11 A LEU   A 1 153 ? 15.797 -11.264 4.601   0.68 15.14 ?  153 LEU   A HD11 1 
ATOM   3123 H HD11 B LEU   A 1 153 ? 15.568 -10.809 4.399   0.32 14.45 ?  153 LEU   A HD11 1 
ATOM   3124 H HD12 A LEU   A 1 153 ? 14.422 -10.788 5.233   0.68 15.14 ?  153 LEU   A HD12 1 
ATOM   3125 H HD12 B LEU   A 1 153 ? 14.275 -10.611 5.300   0.32 14.45 ?  153 LEU   A HD12 1 
ATOM   3126 H HD13 A LEU   A 1 153 ? 15.043 -10.000 4.002   0.68 15.14 ?  153 LEU   A HD13 1 
ATOM   3127 H HD13 B LEU   A 1 153 ? 14.621 -9.555  4.165   0.32 14.45 ?  153 LEU   A HD13 1 
ATOM   3128 H HD21 A LEU   A 1 153 ? 17.697 -9.515  4.630   0.68 15.65 ?  153 LEU   A HD21 1 
ATOM   3129 H HD21 B LEU   A 1 153 ? 17.494 -9.364  4.656   0.32 14.86 ?  153 LEU   A HD21 1 
ATOM   3130 H HD22 A LEU   A 1 153 ? 16.720 -8.291  4.363   0.68 15.65 ?  153 LEU   A HD22 1 
ATOM   3131 H HD22 B LEU   A 1 153 ? 16.658 -8.020  4.518   0.32 14.86 ?  153 LEU   A HD22 1 
ATOM   3132 H HD23 A LEU   A 1 153 ? 17.609 -8.328  5.679   0.68 15.65 ?  153 LEU   A HD23 1 
ATOM   3133 H HD23 B LEU   A 1 153 ? 17.551 -8.272  5.808   0.32 14.86 ?  153 LEU   A HD23 1 
ATOM   3134 N N    A ALA   A 1 154 ? 14.927 -5.438  7.693   0.68 12.19 ?  154 ALA   A N    1 
ATOM   3135 N N    B ALA   A 1 154 ? 14.987 -5.302  8.089   0.32 11.80 ?  154 ALA   A N    1 
ATOM   3136 C CA   A ALA   A 1 154 ? 14.055 -4.291  7.914   0.68 12.48 ?  154 ALA   A CA   1 
ATOM   3137 C CA   B ALA   A 1 154 ? 14.138 -4.160  8.395   0.32 12.68 ?  154 ALA   A CA   1 
ATOM   3138 C C    A ALA   A 1 154 ? 13.575 -3.773  6.565   0.68 11.99 ?  154 ALA   A C    1 
ATOM   3139 C C    B ALA   A 1 154 ? 13.632 -3.591  7.076   0.32 12.44 ?  154 ALA   A C    1 
ATOM   3140 O O    A ALA   A 1 154 ? 14.387 -3.394  5.717   0.68 12.47 ?  154 ALA   A O    1 
ATOM   3141 O O    B ALA   A 1 154 ? 14.427 -3.158  6.235   0.32 12.07 ?  154 ALA   A O    1 
ATOM   3142 C CB   A ALA   A 1 154 ? 14.804 -3.190  8.662   0.68 13.05 ?  154 ALA   A CB   1 
ATOM   3143 C CB   B ALA   A 1 154 ? 14.912 -3.101  9.181   0.32 13.23 ?  154 ALA   A CB   1 
ATOM   3144 H H    A ALA   A 1 154 ? 15.698 -5.225  7.380   0.68 14.60 ?  154 ALA   A H    1 
ATOM   3145 H H    B ALA   A 1 154 ? 15.763 -5.076  7.789   0.32 14.14 ?  154 ALA   A H    1 
ATOM   3146 H HA   A ALA   A 1 154 ? 13.284 -4.559  8.443   0.68 14.96 ?  154 ALA   A HA   1 
ATOM   3147 H HA   B ALA   A 1 154 ? 13.377 -4.442  8.924   0.32 15.20 ?  154 ALA   A HA   1 
ATOM   3148 H HB1  A ALA   A 1 154 ? 14.208 -2.439  8.799   0.68 15.64 ?  154 ALA   A HB1  1 
ATOM   3149 H HB1  B ALA   A 1 154 ? 14.324 -2.353  9.373   0.32 15.86 ?  154 ALA   A HB1  1 
ATOM   3150 H HB2  A ALA   A 1 154 ? 15.106 -3.535  9.518   0.68 15.64 ?  154 ALA   A HB2  1 
ATOM   3151 H HB2  B ALA   A 1 154 ? 15.229 -3.493  10.011  0.32 15.86 ?  154 ALA   A HB2  1 
ATOM   3152 H HB3  A ALA   A 1 154 ? 15.569 -2.914  8.130   0.68 15.64 ?  154 ALA   A HB3  1 
ATOM   3153 H HB3  B ALA   A 1 154 ? 15.666 -2.800  8.650   0.32 15.86 ?  154 ALA   A HB3  1 
ATOM   3154 N N    A VAL   A 1 155 ? 12.259 -3.757  6.374   0.48 10.92 ?  155 VAL   A N    1 
ATOM   3155 N N    B VAL   A 1 155 ? 12.317 -3.621  6.887   0.32 12.88 ?  155 VAL   A N    1 
ATOM   3156 C CA   A VAL   A 1 155 ? 11.621 -3.294  5.145   0.48 12.76 ?  155 VAL   A CA   1 
ATOM   3157 C CA   B VAL   A 1 155 ? 11.665 -3.092  5.693   0.32 14.25 ?  155 VAL   A CA   1 
ATOM   3158 C CA   T VAL   A 1 155 ? 11.606 -3.296  5.301   0.20 13.99 ?  155 VAL   A CA   1 
ATOM   3159 C C    A VAL   A 1 155 ? 10.880 -2.005  5.481   0.48 14.27 ?  155 VAL   A C    1 
ATOM   3160 C C    B VAL   A 1 155 ? 10.804 -1.914  6.125   0.32 16.02 ?  155 VAL   A C    1 
ATOM   3161 C C    T VAL   A 1 155 ? 10.984 -1.934  5.615   0.20 14.11 ?  155 VAL   A C    1 
ATOM   3162 O O    A VAL   A 1 155 ? 9.901  -2.027  6.235   0.48 15.03 ?  155 VAL   A O    1 
ATOM   3163 O O    B VAL   A 1 155 ? 9.901  -2.069  6.956   0.32 15.84 ?  155 VAL   A O    1 
ATOM   3164 O O    T VAL   A 1 155 ? 10.150 -1.808  6.511   0.20 14.04 ?  155 VAL   A O    1 
ATOM   3165 C CB   A VAL   A 1 155 ? 10.664 -4.356  4.582   0.48 13.06 ?  155 VAL   A CB   1 
ATOM   3166 C CB   B VAL   A 1 155 ? 10.828 -4.168  4.986   0.32 14.33 ?  155 VAL   A CB   1 
ATOM   3167 C CB   T VAL   A 1 155 ? 10.582 -4.307  4.738   0.20 14.06 ?  155 VAL   A CB   1 
ATOM   3168 C CG1  A VAL   A 1 155 ? 9.997  -3.866  3.305   0.48 13.33 ?  155 VAL   A CG1  1 
ATOM   3169 C CG1  B VAL   A 1 155 ? 10.050 -3.561  3.823   0.32 14.39 ?  155 VAL   A CG1  1 
ATOM   3170 C CG1  T VAL   A 1 155 ? 9.897  -3.749  3.500   0.20 14.03 ?  155 VAL   A CG1  1 
ATOM   3171 C CG2  A VAL   A 1 155 ? 11.402 -5.671  4.332   0.48 14.07 ?  155 VAL   A CG2  1 
ATOM   3172 C CG2  B VAL   A 1 155 ? 11.729 -5.301  4.502   0.32 14.50 ?  155 VAL   A CG2  1 
ATOM   3173 C CG2  T VAL   A 1 155 ? 11.262 -5.636  4.417   0.20 14.40 ?  155 VAL   A CG2  1 
ATOM   3174 H H    A VAL   A 1 155 ? 11.696 -4.040  6.961   0.48 13.08 ?  155 VAL   A H    1 
ATOM   3175 H H    B VAL   A 1 155 ? 11.766 -3.950  7.455   0.32 15.43 ?  155 VAL   A H    1 
ATOM   3176 H HA   A VAL   A 1 155 ? 12.299 -3.106  4.476   0.48 15.29 ?  155 VAL   A HA   1 
ATOM   3177 H HA   B VAL   A 1 155 ? 12.336 -2.766  5.072   0.32 17.08 ?  155 VAL   A HA   1 
ATOM   3178 H HB   A VAL   A 1 155 ? 9.965  -4.532  5.235   0.48 15.65 ?  155 VAL   A HB   1 
ATOM   3179 H HB   B VAL   A 1 155 ? 10.190 -4.536  5.617   0.32 17.18 ?  155 VAL   A HB   1 
ATOM   3180 H HB   T VAL   A 1 155 ? 9.902  -4.476  5.408   0.20 16.85 ?  155 VAL   A HB   1 
ATOM   3181 H HG11 A VAL   A 1 155 ? 9.458  -4.585  2.934   0.48 15.97 ?  155 VAL   A HG11 1 
ATOM   3182 H HG11 B VAL   A 1 155 ? 9.706  -4.278  3.268   0.32 17.24 ?  155 VAL   A HG11 1 
ATOM   3183 H HG11 T VAL   A 1 155 ? 9.388  -4.458  3.074   0.20 16.82 ?  155 VAL   A HG11 1 
ATOM   3184 H HG12 A VAL   A 1 155 ? 9.430  -3.108  3.513   0.48 15.97 ?  155 VAL   A HG12 1 
ATOM   3185 H HG12 B VAL   A 1 155 ? 9.313  -3.033  4.172   0.32 17.24 ?  155 VAL   A HG12 1 
ATOM   3186 H HG12 T VAL   A 1 155 ? 9.302  -3.031  3.764   0.20 16.82 ?  155 VAL   A HG12 1 
ATOM   3187 H HG13 A VAL   A 1 155 ? 10.681 -3.607  2.671   0.48 15.97 ?  155 VAL   A HG13 1 
ATOM   3188 H HG13 B VAL   A 1 155 ? 10.645 -2.998  3.304   0.32 17.24 ?  155 VAL   A HG13 1 
ATOM   3189 H HG13 T VAL   A 1 155 ? 10.572 -3.416  2.889   0.20 16.82 ?  155 VAL   A HG13 1 
ATOM   3190 H HG21 A VAL   A 1 155 ? 10.797 -6.301  3.909   0.48 16.86 ?  155 VAL   A HG21 1 
ATOM   3191 H HG21 B VAL   A 1 155 ? 11.186 -5.960  4.043   0.32 17.37 ?  155 VAL   A HG21 1 
ATOM   3192 H HG21 T VAL   A 1 155 ? 10.601 -6.258  4.071   0.20 17.26 ?  155 VAL   A HG21 1 
ATOM   3193 H HG22 A VAL   A 1 155 ? 12.161 -5.501  3.753   0.48 16.86 ?  155 VAL   A HG22 1 
ATOM   3194 H HG22 B VAL   A 1 155 ? 12.395 -4.939  3.897   0.32 17.37 ?  155 VAL   A HG22 1 
ATOM   3195 H HG22 T VAL   A 1 155 ? 11.953 -5.486  3.751   0.20 17.26 ?  155 VAL   A HG22 1 
ATOM   3196 H HG23 A VAL   A 1 155 ? 11.709 -6.029  5.181   0.48 16.86 ?  155 VAL   A HG23 1 
ATOM   3197 H HG23 B VAL   A 1 155 ? 12.164 -5.707  5.269   0.32 17.37 ?  155 VAL   A HG23 1 
ATOM   3198 H HG23 T VAL   A 1 155 ? 11.658 -5.993  5.228   0.20 17.26 ?  155 VAL   A HG23 1 
ATOM   3199 N N    A PHE   A 1 156 ? 11.335 -0.880  4.914   0.48 15.93 ?  156 PHE   A N    1 
ATOM   3200 N N    B PHE   A 1 156 ? 11.084 -0.738  5.560   0.32 17.53 ?  156 PHE   A N    1 
ATOM   3201 N N    T PHE   A 1 156 ? 11.411 -0.913  4.868   0.20 14.50 ?  156 PHE   A N    1 
ATOM   3202 C CA   A PHE   A 1 156 ? 10.805 0.430   5.305   0.48 17.14 ?  156 PHE   A CA   1 
ATOM   3203 C CA   B PHE   A 1 156 ? 10.444 0.490   6.025   0.32 19.45 ?  156 PHE   A CA   1 
ATOM   3204 C CA   T PHE   A 1 156 ? 10.968 0.453   5.139   0.20 14.51 ?  156 PHE   A CA   1 
ATOM   3205 C C    A PHE   A 1 156 ? 9.342  0.600   4.907   0.48 16.93 ?  156 PHE   A C    1 
ATOM   3206 C C    B PHE   A 1 156 ? 8.956  0.510   5.695   0.32 20.53 ?  156 PHE   A C    1 
ATOM   3207 C C    T PHE   A 1 156 ? 9.510  0.660   4.748   0.20 15.43 ?  156 PHE   A C    1 
ATOM   3208 O O    A PHE   A 1 156 ? 8.534  1.132   5.683   0.48 17.81 ?  156 PHE   A O    1 
ATOM   3209 O O    B PHE   A 1 156 ? 8.118  0.724   6.579   0.32 21.09 ?  156 PHE   A O    1 
ATOM   3210 O O    T PHE   A 1 156 ? 8.747  1.296   5.486   0.20 16.14 ?  156 PHE   A O    1 
ATOM   3211 C CB   A PHE   A 1 156 ? 11.660 1.541   4.689   0.48 18.41 ?  156 PHE   A CB   1 
ATOM   3212 C CB   B PHE   A 1 156 ? 11.143 1.699   5.398   0.32 20.77 ?  156 PHE   A CB   1 
ATOM   3213 C CB   T PHE   A 1 156 ? 11.865 1.430   4.379   0.20 13.53 ?  156 PHE   A CB   1 
ATOM   3214 C CG   A PHE   A 1 156 ? 11.173 2.930   5.016   0.48 19.84 ?  156 PHE   A CG   1 
ATOM   3215 C CG   B PHE   A 1 156 ? 10.850 3.008   6.084   0.32 21.77 ?  156 PHE   A CG   1 
ATOM   3216 C CG   T PHE   A 1 156 ? 11.513 2.878   4.586   0.20 12.97 ?  156 PHE   A CG   1 
ATOM   3217 C CD1  A PHE   A 1 156 ? 11.168 3.378   6.327   0.48 20.90 ?  156 PHE   A CD1  1 
ATOM   3218 C CD1  B PHE   A 1 156 ? 9.569  3.536   6.098   0.32 22.32 ?  156 PHE   A CD1  1 
ATOM   3219 C CD1  T PHE   A 1 156 ? 11.889 3.535   5.748   0.20 13.10 ?  156 PHE   A CD1  1 
ATOM   3220 C CD2  A PHE   A 1 156 ? 10.725 3.785   4.017   0.48 20.77 ?  156 PHE   A CD2  1 
ATOM   3221 C CD2  B PHE   A 1 156 ? 11.867 3.725   6.690   0.32 22.05 ?  156 PHE   A CD2  1 
ATOM   3222 C CD2  T PHE   A 1 156 ? 10.827 3.588   3.612   0.20 13.11 ?  156 PHE   A CD2  1 
ATOM   3223 C CE1  A PHE   A 1 156 ? 10.720 4.648   6.640   0.48 21.52 ?  156 PHE   A CE1  1 
ATOM   3224 C CE1  B PHE   A 1 156 ? 9.307  4.742   6.721   0.32 22.58 ?  156 PHE   A CE1  1 
ATOM   3225 C CE1  T PHE   A 1 156 ? 11.575 4.867   5.941   0.20 13.52 ?  156 PHE   A CE1  1 
ATOM   3226 C CE2  A PHE   A 1 156 ? 10.276 5.060   4.325   0.48 21.59 ?  156 PHE   A CE2  1 
ATOM   3227 C CE2  B PHE   A 1 156 ? 11.609 4.932   7.313   0.32 22.27 ?  156 PHE   A CE2  1 
ATOM   3228 C CE2  T PHE   A 1 156 ? 10.513 4.922   3.799   0.20 13.46 ?  156 PHE   A CE2  1 
ATOM   3229 C CZ   A PHE   A 1 156 ? 10.278 5.491   5.637   0.48 21.78 ?  156 PHE   A CZ   1 
ATOM   3230 C CZ   B PHE   A 1 156 ? 10.327 5.440   7.327   0.32 22.47 ?  156 PHE   A CZ   1 
ATOM   3231 C CZ   T PHE   A 1 156 ? 10.889 5.562   4.966   0.20 13.51 ?  156 PHE   A CZ   1 
ATOM   3232 H H    A PHE   A 1 156 ? 11.956 -0.855  4.314   0.48 19.10 ?  156 PHE   A H    1 
ATOM   3233 H H    B PHE   A 1 156 ? 11.641 -0.621  4.914   0.32 21.01 ?  156 PHE   A H    1 
ATOM   3234 H H    T PHE   A 1 156 ? 11.964 -0.985  4.213   0.20 17.38 ?  156 PHE   A H    1 
ATOM   3235 H HA   A PHE   A 1 156 ? 10.871 0.513   6.269   0.48 20.55 ?  156 PHE   A HA   1 
ATOM   3236 H HA   B PHE   A 1 156 ? 10.534 0.551   6.987   0.32 23.32 ?  156 PHE   A HA   1 
ATOM   3237 H HA   T PHE   A 1 156 ? 11.059 0.632   6.089   0.20 17.39 ?  156 PHE   A HA   1 
ATOM   3238 H HB2  A PHE   A 1 156 ? 12.573 1.461   5.020   0.48 22.07 ?  156 PHE   A HB2  1 
ATOM   3239 H HB2  B PHE   A 1 156 ? 12.100 1.557   5.434   0.32 24.91 ?  156 PHE   A HB2  1 
ATOM   3240 H HB2  T PHE   A 1 156 ? 12.781 1.302   4.672   0.20 16.21 ?  156 PHE   A HB2  1 
ATOM   3241 H HB3  A PHE   A 1 156 ? 11.657 1.444   3.724   0.48 22.07 ?  156 PHE   A HB3  1 
ATOM   3242 H HB3  B PHE   A 1 156 ? 10.856 1.783   4.475   0.32 24.91 ?  156 PHE   A HB3  1 
ATOM   3243 H HB3  T PHE   A 1 156 ? 11.795 1.241   3.431   0.20 16.21 ?  156 PHE   A HB3  1 
ATOM   3244 H HD1  A PHE   A 1 156 ? 11.467 2.816   7.007   0.48 25.06 ?  156 PHE   A HD1  1 
ATOM   3245 H HD1  B PHE   A 1 156 ? 8.874  3.072   5.695   0.32 26.76 ?  156 PHE   A HD1  1 
ATOM   3246 H HD1  T PHE   A 1 156 ? 12.349 3.068   6.411   0.20 15.70 ?  156 PHE   A HD1  1 
ATOM   3247 H HD2  A PHE   A 1 156 ? 10.726 3.497   3.133   0.48 24.90 ?  156 PHE   A HD2  1 
ATOM   3248 H HD2  B PHE   A 1 156 ? 12.733 3.387   6.685   0.32 26.44 ?  156 PHE   A HD2  1 
ATOM   3249 H HD2  T PHE   A 1 156 ? 10.574 3.159   2.828   0.20 15.70 ?  156 PHE   A HD2  1 
ATOM   3250 H HE1  A PHE   A 1 156 ? 10.722 4.938   7.525   0.48 25.81 ?  156 PHE   A HE1  1 
ATOM   3251 H HE1  B PHE   A 1 156 ? 8.441  5.083   6.728   0.32 27.08 ?  156 PHE   A HE1  1 
ATOM   3252 H HE1  T PHE   A 1 156 ? 11.826 5.292   6.730   0.20 16.21 ?  156 PHE   A HE1  1 
ATOM   3253 H HE2  A PHE   A 1 156 ? 9.980  5.623   3.649   0.48 25.89 ?  156 PHE   A HE2  1 
ATOM   3254 H HE2  B PHE   A 1 156 ? 12.299 5.403   7.720   0.32 26.71 ?  156 PHE   A HE2  1 
ATOM   3255 H HE2  T PHE   A 1 156 ? 10.048 5.384   3.143   0.20 16.12 ?  156 PHE   A HE2  1 
ATOM   3256 H HZ   A PHE   A 1 156 ? 9.977  6.346   5.848   0.48 26.11 ?  156 PHE   A HZ   1 
ATOM   3257 H HZ   B PHE   A 1 156 ? 10.152 6.252   7.744   0.32 26.95 ?  156 PHE   A HZ   1 
ATOM   3258 H HZ   T PHE   A 1 156 ? 10.674 6.455   5.098   0.20 16.19 ?  156 PHE   A HZ   1 
ATOM   3259 N N    A ASP   A 1 157 ? 8.990  0.179   3.698   0.48 16.80 ?  157 ASP   A N    1 
ATOM   3260 N N    B ASP   A 1 157 ? 8.608  0.319   4.426   0.32 21.10 ?  157 ASP   A N    1 
ATOM   3261 N N    T ASP   A 1 157 ? 9.112  0.149   3.589   0.20 15.86 ?  157 ASP   A N    1 
ATOM   3262 C CA   A ASP   A 1 157 ? 7.661  0.424   3.148   0.48 17.84 ?  157 ASP   A CA   1 
ATOM   3263 C CA   B ASP   A 1 157 ? 7.258  0.603   3.959   0.32 22.09 ?  157 ASP   A CA   1 
ATOM   3264 C CA   T ASP   A 1 157 ? 7.791  0.404   3.034   0.20 16.46 ?  157 ASP   A CA   1 
ATOM   3265 C C    A ASP   A 1 157 ? 6.688  -0.613  3.697   0.48 18.30 ?  157 ASP   A C    1 
ATOM   3266 C C    B ASP   A 1 157 ? 6.358  -0.629  4.028   0.32 22.17 ?  157 ASP   A C    1 
ATOM   3267 C C    T ASP   A 1 157 ? 6.790  -0.589  3.616   0.20 17.30 ?  157 ASP   A C    1 
ATOM   3268 O O    A ASP   A 1 157 ? 6.825  -1.812  3.418   0.48 17.87 ?  157 ASP   A O    1 
ATOM   3269 O O    B ASP   A 1 157 ? 6.816  -1.773  3.952   0.32 22.33 ?  157 ASP   A O    1 
ATOM   3270 O O    T ASP   A 1 157 ? 6.930  -1.803  3.426   0.20 17.20 ?  157 ASP   A O    1 
ATOM   3271 C CB   A ASP   A 1 157 ? 7.732  0.356   1.629   0.48 19.26 ?  157 ASP   A CB   1 
ATOM   3272 C CB   B ASP   A 1 157 ? 7.303  1.187   2.546   0.32 23.00 ?  157 ASP   A CB   1 
ATOM   3273 C CB   T ASP   A 1 157 ? 7.861  0.263   1.517   0.20 16.46 ?  157 ASP   A CB   1 
ATOM   3274 C CG   A ASP   A 1 157 ? 6.465  0.846   0.964   0.48 20.83 ?  157 ASP   A CG   1 
ATOM   3275 C CG   B ASP   A 1 157 ? 5.925  1.370   1.942   0.32 23.47 ?  157 ASP   A CG   1 
ATOM   3276 C CG   T ASP   A 1 157 ? 6.706  0.925   0.817   0.20 16.14 ?  157 ASP   A CG   1 
ATOM   3277 O OD1  A ASP   A 1 157 ? 6.185  2.061   1.021   0.48 22.13 ?  157 ASP   A OD1  1 
ATOM   3278 O OD1  B ASP   A 1 157 ? 5.283  0.349   1.617   0.32 23.48 ?  157 ASP   A OD1  1 
ATOM   3279 O OD1  T ASP   A 1 157 ? 5.583  0.392   0.907   0.20 16.26 ?  157 ASP   A OD1  1 
ATOM   3280 O OD2  A ASP   A 1 157 ? 5.744  0.006   0.385   0.48 20.80 -1 157 ASP   A OD2  1 
ATOM   3281 O OD2  B ASP   A 1 157 ? 5.482  2.527   1.803   0.32 23.77 -1 157 ASP   A OD2  1 
ATOM   3282 O OD2  T ASP   A 1 157 ? 6.919  1.979   0.184   0.20 15.15 -1 157 ASP   A OD2  1 
ATOM   3283 H H    A ASP   A 1 157 ? 9.519  -0.256  3.169   0.48 20.14 ?  157 ASP   A H    1 
ATOM   3284 H H    B ASP   A 1 157 ? 9.136  0.037   3.811   0.32 25.30 ?  157 ASP   A H    1 
ATOM   3285 H H    T ASP   A 1 157 ? 9.608  -0.349  3.089   0.20 19.01 ?  157 ASP   A H    1 
ATOM   3286 H HA   A ASP   A 1 157 ? 7.366  1.305   3.416   0.48 21.39 ?  157 ASP   A HA   1 
ATOM   3287 H HA   B ASP   A 1 157 ? 6.869  1.273   4.535   0.32 26.49 ?  157 ASP   A HA   1 
ATOM   3288 H HA   T ASP   A 1 157 ? 7.509  1.307   3.257   0.20 19.73 ?  157 ASP   A HA   1 
ATOM   3289 H HB2  A ASP   A 1 157 ? 8.501  0.875   1.334   0.48 23.09 ?  157 ASP   A HB2  1 
ATOM   3290 H HB2  B ASP   A 1 157 ? 7.758  2.050   2.574   0.32 27.58 ?  157 ASP   A HB2  1 
ATOM   3291 H HB2  T ASP   A 1 157 ? 8.676  0.670   1.201   0.20 19.73 ?  157 ASP   A HB2  1 
ATOM   3292 H HB3  A ASP   A 1 157 ? 7.848  -0.568  1.364   0.48 23.09 ?  157 ASP   A HB3  1 
ATOM   3293 H HB3  B ASP   A 1 157 ? 7.789  0.583   1.978   0.32 27.58 ?  157 ASP   A HB3  1 
ATOM   3294 H HB3  T ASP   A 1 157 ? 7.854  -0.680  1.295   0.20 19.73 ?  157 ASP   A HB3  1 
ATOM   3295 N N    A LYS   A 1 158 ? 5.704  -0.152  4.483   0.48 19.52 ?  158 LYS   A N    1 
ATOM   3296 N N    B LYS   A 1 158 ? 5.053  -0.369  4.162   0.32 21.66 ?  158 LYS   A N    1 
ATOM   3297 N N    T LYS   A 1 158 ? 5.776  -0.070  4.318   0.20 18.41 ?  158 LYS   A N    1 
ATOM   3298 C CA   A LYS   A 1 158 ? 4.733  -1.071  5.076   0.48 20.01 ?  158 LYS   A CA   1 
ATOM   3299 C CA   B LYS   A 1 158 ? 4.087  -1.401  4.531   0.32 21.26 ?  158 LYS   A CA   1 
ATOM   3300 C CA   T LYS   A 1 158 ? 4.792  -0.946  4.949   0.20 19.61 ?  158 LYS   A CA   1 
ATOM   3301 C C    A LYS   A 1 158 ? 3.967  -1.821  3.999   0.48 19.59 ?  158 LYS   A C    1 
ATOM   3302 C C    B LYS   A 1 158 ? 3.658  -2.247  3.333   0.32 19.27 ?  158 LYS   A C    1 
ATOM   3303 C C    T LYS   A 1 158 ? 4.021  -1.749  3.910   0.20 19.82 ?  158 LYS   A C    1 
ATOM   3304 O O    A LYS   A 1 158 ? 3.744  -3.031  4.112   0.48 19.45 ?  158 LYS   A O    1 
ATOM   3305 O O    B LYS   A 1 158 ? 3.655  -3.481  3.406   0.32 18.37 ?  158 LYS   A O    1 
ATOM   3306 O O    T LYS   A 1 158 ? 3.779  -2.947  4.096   0.20 19.76 ?  158 LYS   A O    1 
ATOM   3307 C CB   A LYS   A 1 158 ? 3.764  -0.315  5.992   0.48 21.74 ?  158 LYS   A CB   1 
ATOM   3308 C CB   B LYS   A 1 158 ? 2.869  -0.740  5.187   0.32 22.75 ?  158 LYS   A CB   1 
ATOM   3309 C CB   T LYS   A 1 158 ? 3.835  -0.130  5.822   0.20 20.89 ?  158 LYS   A CB   1 
ATOM   3310 C CG   A LYS   A 1 158 ? 2.527  -1.118  6.433   0.48 23.64 ?  158 LYS   A CG   1 
ATOM   3311 C CG   B LYS   A 1 158 ? 1.793  -1.709  5.659   0.32 24.05 ?  158 LYS   A CG   1 
ATOM   3312 C CG   T LYS   A 1 158 ? 2.612  -0.905  6.312   0.20 22.13 ?  158 LYS   A CG   1 
ATOM   3313 C CD   A LYS   A 1 158 ? 2.877  -2.412  7.178   0.48 25.19 ?  158 LYS   A CD   1 
ATOM   3314 C CD   B LYS   A 1 158 ? 2.201  -2.406  6.943   0.32 25.09 ?  158 LYS   A CD   1 
ATOM   3315 C CD   T LYS   A 1 158 ? 2.999  -2.111  7.157   0.20 23.28 ?  158 LYS   A CD   1 
ATOM   3316 C CE   A LYS   A 1 158 ? 1.621  -3.093  7.725   0.48 26.08 ?  158 LYS   A CE   1 
ATOM   3317 C CE   B LYS   A 1 158 ? 1.150  -3.407  7.392   0.32 25.69 ?  158 LYS   A CE   1 
ATOM   3318 C CE   T LYS   A 1 158 ? 1.773  -2.923  7.552   0.20 24.12 ?  158 LYS   A CE   1 
ATOM   3319 N NZ   A LYS   A 1 158 ? 1.883  -4.468  8.250   0.48 26.36 ?  158 LYS   A NZ   1 
ATOM   3320 N NZ   B LYS   A 1 158 ? 1.514  -4.032  8.693   0.32 26.08 ?  158 LYS   A NZ   1 
ATOM   3321 N NZ   T LYS   A 1 158 ? 2.130  -4.148  8.321   0.20 24.57 ?  158 LYS   A NZ   1 
ATOM   3322 H H    A LYS   A 1 158 ? 5.588  0.673   4.687   0.48 23.40 ?  158 LYS   A H    1 
ATOM   3323 H H    B LYS   A 1 158 ? 4.699  0.406   4.043   0.32 25.96 ?  158 LYS   A H    1 
ATOM   3324 H H    T LYS   A 1 158 ? 5.639  0.770   4.440   0.20 22.07 ?  158 LYS   A H    1 
ATOM   3325 H HA   A LYS   A 1 158 ? 5.201  -1.723  5.619   0.48 23.99 ?  158 LYS   A HA   1 
ATOM   3326 H HA   B LYS   A 1 158 ? 4.489  -1.990  5.186   0.32 25.49 ?  158 LYS   A HA   1 
ATOM   3327 H HA   T LYS   A 1 158 ? 5.254  -1.572  5.526   0.20 23.51 ?  158 LYS   A HA   1 
ATOM   3328 H HB2  A LYS   A 1 158 ? 4.237  -0.041  6.795   0.48 26.07 ?  158 LYS   A HB2  1 
ATOM   3329 H HB2  B LYS   A 1 158 ? 3.166  -0.237  5.966   0.32 27.28 ?  158 LYS   A HB2  1 
ATOM   3330 H HB2  T LYS   A 1 158 ? 4.316  0.180   6.607   0.20 25.05 ?  158 LYS   A HB2  1 
ATOM   3331 H HB3  A LYS   A 1 158 ? 3.446  0.473   5.524   0.48 26.07 ?  158 LYS   A HB3  1 
ATOM   3332 H HB3  B LYS   A 1 158 ? 2.458  -0.135  4.551   0.32 27.28 ?  158 LYS   A HB3  1 
ATOM   3333 H HB3  T LYS   A 1 158 ? 3.516  0.630   5.313   0.20 25.05 ?  158 LYS   A HB3  1 
ATOM   3334 H HG2  A LYS   A 1 158 ? 1.997  -0.570  7.031   0.48 28.34 ?  158 LYS   A HG2  1 
ATOM   3335 H HG2  B LYS   A 1 158 ? 0.975  -1.217  5.830   0.32 28.84 ?  158 LYS   A HG2  1 
ATOM   3336 H HG2  T LYS   A 1 158 ? 2.069  -0.320  6.862   0.20 26.53 ?  158 LYS   A HG2  1 
ATOM   3337 H HG3  A LYS   A 1 158 ? 1.997  -1.352  5.654   0.48 28.34 ?  158 LYS   A HG3  1 
ATOM   3338 H HG3  B LYS   A 1 158 ? 1.637  -2.385  4.981   0.32 28.84 ?  158 LYS   A HG3  1 
ATOM   3339 H HG3  T LYS   A 1 158 ? 2.091  -1.216  5.554   0.20 26.53 ?  158 LYS   A HG3  1 
ATOM   3340 H HD2  A LYS   A 1 158 ? 3.318  -3.027  6.572   0.48 30.20 ?  158 LYS   A HD2  1 
ATOM   3341 H HD2  B LYS   A 1 158 ? 3.034  -2.882  6.798   0.32 30.08 ?  158 LYS   A HD2  1 
ATOM   3342 H HD2  T LYS   A 1 158 ? 3.592  -2.688  6.650   0.20 27.91 ?  158 LYS   A HD2  1 
ATOM   3343 H HD3  A LYS   A 1 158 ? 3.453  -2.205  7.928   0.48 30.20 ?  158 LYS   A HD3  1 
ATOM   3344 H HD3  B LYS   A 1 158 ? 2.311  -1.744  7.645   0.32 30.08 ?  158 LYS   A HD3  1 
ATOM   3345 H HD3  T LYS   A 1 158 ? 3.437  -1.808  7.968   0.20 27.91 ?  158 LYS   A HD3  1 
ATOM   3346 H HE2  A LYS   A 1 158 ? 1.260  -2.559  8.450   0.48 31.27 ?  158 LYS   A HE2  1 
ATOM   3347 H HE2  B LYS   A 1 158 ? 0.300  -2.953  7.498   0.32 30.80 ?  158 LYS   A HE2  1 
ATOM   3348 H HE2  T LYS   A 1 158 ? 1.191  -2.378  8.104   0.20 28.92 ?  158 LYS   A HE2  1 
ATOM   3349 H HE3  A LYS   A 1 158 ? 0.969  -3.166  7.014   0.48 31.27 ?  158 LYS   A HE3  1 
ATOM   3350 H HE3  B LYS   A 1 158 ? 1.075  -4.111  6.729   0.32 30.80 ?  158 LYS   A HE3  1 
ATOM   3351 H HE3  T LYS   A 1 158 ? 1.304  -3.200  6.749   0.20 28.92 ?  158 LYS   A HE3  1 
ATOM   3352 H HZ1  A LYS   A 1 158 ? 1.128  -4.828  8.554   0.48 31.61 ?  158 LYS   A HZ1  1 
ATOM   3353 H HZ1  B LYS   A 1 158 ? 0.888  -4.614  8.937   0.32 31.27 ?  158 LYS   A HZ1  1 
ATOM   3354 H HZ1  T LYS   A 1 158 ? 1.393  -4.600  8.535   0.20 29.47 ?  158 LYS   A HZ1  1 
ATOM   3355 H HZ2  A LYS   A 1 158 ? 2.208  -4.984  7.601   0.48 31.61 ?  158 LYS   A HZ2  1 
ATOM   3356 H HZ2  B LYS   A 1 158 ? 2.292  -4.459  8.618   0.32 31.27 ?  158 LYS   A HZ2  1 
ATOM   3357 H HZ2  T LYS   A 1 158 ? 2.657  -4.672  7.831   0.20 29.47 ?  158 LYS   A HZ2  1 
ATOM   3358 H HZ3  A LYS   A 1 158 ? 2.475  -4.434  8.914   0.48 31.61 ?  158 LYS   A HZ3  1 
ATOM   3359 H HZ3  B LYS   A 1 158 ? 1.588  -3.406  9.321   0.32 31.27 ?  158 LYS   A HZ3  1 
ATOM   3360 H HZ3  T LYS   A 1 158 ? 2.559  -3.925  9.068   0.20 29.47 ?  158 LYS   A HZ3  1 
ATOM   3361 N N    A ASN   A 1 159 ? 3.542  -1.118  2.951   0.48 19.60 ?  159 ASN   A N    1 
ATOM   3362 N N    B ASN   A 1 159 ? 3.274  -1.602  2.228   0.32 18.78 ?  159 ASN   A N    1 
ATOM   3363 N N    T ASN   A 1 159 ? 3.614  -1.109  2.820   0.20 20.19 ?  159 ASN   A N    1 
ATOM   3364 C CA   A ASN   A 1 159 ? 2.866  -1.804  1.859   0.48 19.59 ?  159 ASN   A CA   1 
ATOM   3365 C CA   B ASN   A 1 159 ? 2.725  -2.336  1.090   0.32 18.46 ?  159 ASN   A CA   1 
ATOM   3366 C CA   T ASN   A 1 159 ? 2.874  -1.802  1.772   0.20 20.53 ?  159 ASN   A CA   1 
ATOM   3367 C C    A ASN   A 1 159 ? 3.765  -2.876  1.258   0.48 18.40 ?  159 ASN   A C    1 
ATOM   3368 C C    B ASN   A 1 159 ? 3.691  -3.418  0.616   0.32 17.59 ?  159 ASN   A C    1 
ATOM   3369 C C    T ASN   A 1 159 ? 3.712  -2.907  1.140   0.20 20.37 ?  159 ASN   A C    1 
ATOM   3370 O O    A ASN   A 1 159 ? 3.307  -3.987  0.968   0.48 17.55 ?  159 ASN   A O    1 
ATOM   3371 O O    B ASN   A 1 159 ? 3.310  -4.583  0.443   0.32 17.67 ?  159 ASN   A O    1 
ATOM   3372 O O    T ASN   A 1 159 ? 3.184  -3.947  0.755   0.20 20.33 ?  159 ASN   A O    1 
ATOM   3373 C CB   A ASN   A 1 159 ? 2.394  -0.796  0.811   0.48 21.09 ?  159 ASN   A CB   1 
ATOM   3374 C CB   B ASN   A 1 159 ? 2.389  -1.363  -0.045  0.32 19.53 ?  159 ASN   A CB   1 
ATOM   3375 C CB   T ASN   A 1 159 ? 2.392  -0.815  0.706   0.20 21.18 ?  159 ASN   A CB   1 
ATOM   3376 C CG   A ASN   A 1 159 ? 1.184  0.001   1.276   0.48 22.81 ?  159 ASN   A CG   1 
ATOM   3377 C CG   B ASN   A 1 159 ? 0.924  -0.969  -0.061  0.32 20.81 ?  159 ASN   A CG   1 
ATOM   3378 C CG   T ASN   A 1 159 ? 1.201  0.005   1.168   0.20 21.91 ?  159 ASN   A CG   1 
ATOM   3379 O OD1  A ASN   A 1 159 ? 0.353  -0.502  2.031   0.48 23.61 ?  159 ASN   A OD1  1 
ATOM   3380 O OD1  B ASN   A 1 159 ? 0.300  -0.810  0.988   0.32 21.45 ?  159 ASN   A OD1  1 
ATOM   3381 O OD1  T ASN   A 1 159 ? 0.383  -0.461  1.961   0.20 22.28 ?  159 ASN   A OD1  1 
ATOM   3382 N ND2  A ASN   A 1 159 ? 1.080  1.244   0.827   0.48 23.79 ?  159 ASN   A ND2  1 
ATOM   3383 N ND2  B ASN   A 1 159 ? 0.363  -0.823  -1.258  0.32 21.18 ?  159 ASN   A ND2  1 
ATOM   3384 N ND2  T ASN   A 1 159 ? 1.097  1.232   0.675   0.20 22.31 ?  159 ASN   A ND2  1 
ATOM   3385 H H    A ASN   A 1 159 ? 3.632  -0.272  2.852   0.48 23.49 ?  159 ASN   A H    1 
ATOM   3386 H H    B ASN   A 1 159 ? 3.332  -0.752  2.116   0.32 22.52 ?  159 ASN   A H    1 
ATOM   3387 H H    T ASN   A 1 159 ? 3.748  -0.276  2.666   0.20 24.21 ?  159 ASN   A H    1 
ATOM   3388 H HA   A ASN   A 1 159 ? 2.083  -2.254  2.209   0.48 23.49 ?  159 ASN   A HA   1 
ATOM   3389 H HA   B ASN   A 1 159 ? 1.900  -2.764  1.360   0.32 22.13 ?  159 ASN   A HA   1 
ATOM   3390 H HA   T ASN   A 1 159 ? 2.094  -2.220  2.164   0.20 24.61 ?  159 ASN   A HA   1 
ATOM   3391 H HB2  A ASN   A 1 159 ? 3.109  -0.171  0.626   0.48 25.29 ?  159 ASN   A HB2  1 
ATOM   3392 H HB2  B ASN   A 1 159 ? 2.915  -0.548  0.063   0.32 23.41 ?  159 ASN   A HB2  1 
ATOM   3393 H HB2  T ASN   A 1 159 ? 3.112  -0.204  0.490   0.20 25.40 ?  159 ASN   A HB2  1 
ATOM   3394 H HB3  A ASN   A 1 159 ? 2.149  -1.273  0.001   0.48 25.29 ?  159 ASN   A HB3  1 
ATOM   3395 H HB3  B ASN   A 1 159 ? 2.594  -1.774  -0.895  0.32 23.41 ?  159 ASN   A HB3  1 
ATOM   3396 H HB3  T ASN   A 1 159 ? 2.129  -1.312  -0.087  0.20 25.40 ?  159 ASN   A HB3  1 
ATOM   3397 H HD21 A ASN   A 1 159 ? 0.412  1.728   1.063   0.48 28.52 ?  159 ASN   A HD21 1 
ATOM   3398 H HD21 B ASN   A 1 159 ? -0.464 -0.599  -1.325  0.32 25.39 ?  159 ASN   A HD21 1 
ATOM   3399 H HD21 T ASN   A 1 159 ? 0.438  1.731   0.907   0.20 26.75 ?  159 ASN   A HD21 1 
ATOM   3400 H HD22 A ASN   A 1 159 ? 1.682  1.561   0.306   0.48 28.52 ?  159 ASN   A HD22 1 
ATOM   3401 H HD22 B ASN   A 1 159 ? 0.831  -0.952  -1.970  0.32 25.39 ?  159 ASN   A HD22 1 
ATOM   3402 H HD22 T ASN   A 1 159 ? 1.688  1.524   0.126   0.20 26.75 ?  159 ASN   A HD22 1 
ATOM   3403 N N    A LEU   A 1 160 ? 5.057  -2.583  1.101   0.48 17.71 ?  160 LEU   A N    1 
ATOM   3404 N N    B LEU   A 1 160 ? 4.955  -3.046  0.409   0.32 16.59 ?  160 LEU   A N    1 
ATOM   3405 N N    T LEU   A 1 160 ? 5.018  -2.684  1.039   0.20 20.15 ?  160 LEU   A N    1 
ATOM   3406 C CA   A LEU   A 1 160 ? 5.963  -3.597  0.574   0.48 17.34 ?  160 LEU   A CA   1 
ATOM   3407 C CA   B LEU   A 1 160 ? 5.965  -4.014  -0.004  0.32 16.31 ?  160 LEU   A CA   1 
ATOM   3408 C CA   T LEU   A 1 160 ? 5.914  -3.693  0.486   0.20 20.10 ?  160 LEU   A CA   1 
ATOM   3409 C C    A LEU   A 1 160 ? 6.161  -4.732  1.570   0.48 15.82 ?  160 LEU   A C    1 
ATOM   3410 C C    B LEU   A 1 160 ? 6.115  -5.121  1.032   0.32 15.55 ?  160 LEU   A C    1 
ATOM   3411 O O    A LEU   A 1 160 ? 6.174  -5.906  1.182   0.48 15.57 ?  160 LEU   A O    1 
ATOM   3412 O O    B LEU   A 1 160 ? 6.180  -6.308  0.690   0.32 15.31 ?  160 LEU   A O    1 
ATOM   3413 C CB   A LEU   A 1 160 ? 7.303  -2.981  0.178   0.48 18.39 ?  160 LEU   A CB   1 
ATOM   3414 C CB   B LEU   A 1 160 ? 7.293  -3.285  -0.199  0.32 17.12 ?  160 LEU   A CB   1 
ATOM   3415 C CB   T LEU   A 1 160 ? 7.282  -3.090  0.170   0.20 20.06 ?  160 LEU   A CB   1 
ATOM   3416 C CG   A LEU   A 1 160 ? 8.310  -4.014  -0.334  0.48 19.36 ?  160 LEU   A CG   1 
ATOM   3417 C CG   B LEU   A 1 160 ? 8.545  -4.150  -0.083  0.32 18.12 ?  160 LEU   A CG   1 
ATOM   3418 C CG   T LEU   A 1 160 ? 8.336  -4.087  -0.309  0.20 20.12 ?  160 LEU   A CG   1 
ATOM   3419 C CD1  A LEU   A 1 160 ? 7.773  -4.742  -1.553  0.48 19.42 ?  160 LEU   A CD1  1 
ATOM   3420 C CD1  B LEU   A 1 160 ? 8.524  -5.184  -1.183  0.32 18.39 ?  160 LEU   A CD1  1 
ATOM   3421 C CD1  T LEU   A 1 160 ? 7.869  -4.804  -1.562  0.20 20.01 ?  160 LEU   A CD1  1 
ATOM   3422 C CD2  A LEU   A 1 160 ? 9.642  -3.362  -0.647  0.48 19.94 ?  160 LEU   A CD2  1 
ATOM   3423 C CD2  B LEU   A 1 160 ? 9.808  -3.305  -0.139  0.32 18.39 ?  160 LEU   A CD2  1 
ATOM   3424 C CD2  T LEU   A 1 160 ? 9.661  -3.387  -0.555  0.20 20.21 ?  160 LEU   A CD2  1 
ATOM   3425 H H    A LEU   A 1 160 ? 5.425  -1.827  1.293   0.48 21.22 ?  160 LEU   A H    1 
ATOM   3426 H H    B LEU   A 1 160 ? 5.248  -2.243  0.505   0.32 19.89 ?  160 LEU   A H    1 
ATOM   3427 H H    T LEU   A 1 160 ? 5.411  -1.957  1.282   0.20 24.15 ?  160 LEU   A H    1 
ATOM   3428 H HA   A LEU   A 1 160 ? 5.568  -3.971  -0.225  0.48 20.78 ?  160 LEU   A HA   1 
ATOM   3429 H HA   B LEU   A 1 160 ? 5.706  -4.412  -0.849  0.32 19.55 ?  160 LEU   A HA   1 
ATOM   3430 H HB2  A LEU   A 1 160 ? 7.164  -2.315  -0.520  0.48 22.05 ?  160 LEU   A HB2  1 
ATOM   3431 H HB2  B LEU   A 1 160 ? 7.297  -2.889  -1.085  0.32 20.52 ?  160 LEU   A HB2  1 
ATOM   3432 H HB2  T LEU   A 1 160 ? 7.175  -2.409  -0.517  0.20 24.05 ?  160 LEU   A HB2  1 
ATOM   3433 H HB3  A LEU   A 1 160 ? 7.696  -2.568  0.959   0.48 22.05 ?  160 LEU   A HB3  1 
ATOM   3434 H HB3  B LEU   A 1 160 ? 7.360  -2.583  0.467   0.32 20.52 ?  160 LEU   A HB3  1 
ATOM   3435 H HB3  T LEU   A 1 160 ? 7.630  -2.688  0.979   0.20 24.05 ?  160 LEU   A HB3  1 
ATOM   3436 H HG   A LEU   A 1 160 ? 8.470  -4.672  0.359   0.48 23.21 ?  160 LEU   A HG   1 
ATOM   3437 H HG   B LEU   A 1 160 ? 8.552  -4.611  0.770   0.32 21.72 ?  160 LEU   A HG   1 
ATOM   3438 H HG   T LEU   A 1 160 ? 8.476  -4.752  0.384   0.20 24.12 ?  160 LEU   A HG   1 
ATOM   3439 H HD11 A LEU   A 1 160 ? 8.485  -5.273  -1.941  0.48 23.28 ?  160 LEU   A HD11 1 
ATOM   3440 H HD11 B LEU   A 1 160 ? 9.340  -5.701  -1.142  0.32 22.05 ?  160 LEU   A HD11 1 
ATOM   3441 H HD11 T LEU   A 1 160 ? 8.592  -5.355  -1.897  0.20 23.99 ?  160 LEU   A HD11 1 
ATOM   3442 H HD12 A LEU   A 1 160 ? 7.042  -5.320  -1.281  0.48 23.28 ?  160 LEU   A HD12 1 
ATOM   3443 H HD12 B LEU   A 1 160 ? 7.759  -5.767  -1.058  0.32 22.05 ?  160 LEU   A HD12 1 
ATOM   3444 H HD12 T LEU   A 1 160 ? 7.104  -5.358  -1.342  0.20 23.99 ?  160 LEU   A HD12 1 
ATOM   3445 H HD13 A LEU   A 1 160 ? 7.457  -4.089  -2.198  0.48 23.28 ?  160 LEU   A HD13 1 
ATOM   3446 H HD13 B LEU   A 1 160 ? 8.454  -4.728  -2.035  0.32 22.05 ?  160 LEU   A HD13 1 
ATOM   3447 H HD13 T LEU   A 1 160 ? 7.621  -4.143  -2.227  0.20 23.99 ?  160 LEU   A HD13 1 
ATOM   3448 H HD21 A LEU   A 1 160 ? 10.261 -4.041  -0.962  0.48 23.91 ?  160 LEU   A HD21 1 
ATOM   3449 H HD21 B LEU   A 1 160 ? 10.581 -3.887  -0.060  0.32 22.04 ?  160 LEU   A HD21 1 
ATOM   3450 H HD21 T LEU   A 1 160 ? 10.312 -4.041  -0.855  0.20 24.23 ?  160 LEU   A HD21 1 
ATOM   3451 H HD22 A LEU   A 1 160 ? 9.513  -2.690  -1.334  0.48 23.91 ?  160 LEU   A HD22 1 
ATOM   3452 H HD22 B LEU   A 1 160 ? 9.836  -2.831  -0.984  0.32 22.04 ?  160 LEU   A HD22 1 
ATOM   3453 H HD22 T LEU   A 1 160 ? 9.536  -2.707  -1.236  0.20 24.23 ?  160 LEU   A HD22 1 
ATOM   3454 H HD23 A LEU   A 1 160 ? 9.990  -2.948  0.159   0.48 23.91 ?  160 LEU   A HD23 1 
ATOM   3455 H HD23 B LEU   A 1 160 ? 9.799  -2.670  0.596   0.32 22.04 ?  160 LEU   A HD23 1 
ATOM   3456 H HD23 T LEU   A 1 160 ? 9.960  -2.977  0.272   0.20 24.23 ?  160 LEU   A HD23 1 
ATOM   3457 N N    A TYR   A 1 161 ? 6.316  -4.409  2.855   0.68 16.13 ?  161 TYR   A N    1 
ATOM   3458 N N    B TYR   A 1 161 ? 6.197  -4.740  2.307   0.32 15.62 ?  161 TYR   A N    1 
ATOM   3459 C CA   A TYR   A 1 161 ? 6.431  -5.461  3.859   0.68 16.48 ?  161 TYR   A CA   1 
ATOM   3460 C CA   B TYR   A 1 161 ? 6.354  -5.707  3.387   0.32 15.99 ?  161 TYR   A CA   1 
ATOM   3461 C C    A TYR   A 1 161 ? 5.260  -6.428  3.772   0.68 17.30 ?  161 TYR   A C    1 
ATOM   3462 C C    B TYR   A 1 161 ? 5.257  -6.763  3.350   0.32 16.04 ?  161 TYR   A C    1 
ATOM   3463 O O    A TYR   A 1 161 ? 5.445  -7.649  3.739   0.68 17.60 ?  161 TYR   A O    1 
ATOM   3464 O O    B TYR   A 1 161 ? 5.522  -7.954  3.549   0.32 16.28 ?  161 TYR   A O    1 
ATOM   3465 C CB   A TYR   A 1 161 ? 6.523  -4.866  5.263   0.68 16.82 ?  161 TYR   A CB   1 
ATOM   3466 C CB   B TYR   A 1 161 ? 6.364  -4.945  4.716   0.32 16.62 ?  161 TYR   A CB   1 
ATOM   3467 C CG   A TYR   A 1 161 ? 6.429  -5.930  6.325   0.68 16.57 ?  161 TYR   A CG   1 
ATOM   3468 C CG   B TYR   A 1 161 ? 6.319  -5.795  5.962   0.32 17.44 ?  161 TYR   A CG   1 
ATOM   3469 C CD1  A TYR   A 1 161 ? 7.548  -6.662  6.695   0.68 16.14 ?  161 TYR   A CD1  1 
ATOM   3470 C CD1  B TYR   A 1 161 ? 7.480  -6.333  6.502   0.32 17.80 ?  161 TYR   A CD1  1 
ATOM   3471 C CD2  A TYR   A 1 161 ? 5.221  -6.215  6.946   0.68 16.91 ?  161 TYR   A CD2  1 
ATOM   3472 C CD2  B TYR   A 1 161 ? 5.119  -6.033  6.616   0.32 17.95 ?  161 TYR   A CD2  1 
ATOM   3473 C CE1  A TYR   A 1 161 ? 7.468  -7.642  7.651   0.68 15.73 ?  161 TYR   A CE1  1 
ATOM   3474 C CE1  B TYR   A 1 161 ? 7.444  -7.105  7.647   0.32 18.09 ?  161 TYR   A CE1  1 
ATOM   3475 C CE2  A TYR   A 1 161 ? 5.133  -7.192  7.902   0.68 16.74 ?  161 TYR   A CE2  1 
ATOM   3476 C CE2  B TYR   A 1 161 ? 5.072  -6.804  7.762   0.32 18.07 ?  161 TYR   A CE2  1 
ATOM   3477 C CZ   A TYR   A 1 161 ? 6.258  -7.899  8.250   0.68 16.35 ?  161 TYR   A CZ   1 
ATOM   3478 C CZ   B TYR   A 1 161 ? 6.237  -7.337  8.275   0.32 18.50 ?  161 TYR   A CZ   1 
ATOM   3479 O OH   A TYR   A 1 161 ? 6.178  -8.870  9.208   0.68 16.72 ?  161 TYR   A OH   1 
ATOM   3480 O OH   B TYR   A 1 161 ? 6.194  -8.105  9.417   0.32 19.54 ?  161 TYR   A OH   1 
ATOM   3481 H H    A TYR   A 1 161 ? 6.354  -3.605  3.162   0.68 19.33 ?  161 TYR   A H    1 
ATOM   3482 H H    B TYR   A 1 161 ? 6.162  -3.926  2.572   0.32 18.72 ?  161 TYR   A H    1 
ATOM   3483 H HA   A TYR   A 1 161 ? 7.240  -5.962  3.696   0.68 19.76 ?  161 TYR   A HA   1 
ATOM   3484 H HA   B TYR   A 1 161 ? 7.204  -6.161  3.294   0.32 19.16 ?  161 TYR   A HA   1 
ATOM   3485 H HB2  A TYR   A 1 161 ? 7.377  -4.412  5.363   0.68 20.16 ?  161 TYR   A HB2  1 
ATOM   3486 H HB2  B TYR   A 1 161 ? 7.178  -4.415  4.755   0.32 19.92 ?  161 TYR   A HB2  1 
ATOM   3487 H HB3  A TYR   A 1 161 ? 5.795  -4.237  5.397   0.68 20.16 ?  161 TYR   A HB3  1 
ATOM   3488 H HB3  B TYR   A 1 161 ? 5.596  -4.355  4.737   0.32 19.92 ?  161 TYR   A HB3  1 
ATOM   3489 H HD1  A TYR   A 1 161 ? 8.365  -6.486  6.290   0.68 19.35 ?  161 TYR   A HD1  1 
ATOM   3490 H HD1  B TYR   A 1 161 ? 8.295  -6.176  6.080   0.32 21.33 ?  161 TYR   A HD1  1 
ATOM   3491 H HD2  A TYR   A 1 161 ? 4.456  -5.738  6.711   0.68 20.27 ?  161 TYR   A HD2  1 
ATOM   3492 H HD2  B TYR   A 1 161 ? 4.331  -5.674  6.272   0.32 21.52 ?  161 TYR   A HD2  1 
ATOM   3493 H HE1  A TYR   A 1 161 ? 8.223  -8.129  7.893   0.68 18.85 ?  161 TYR   A HE1  1 
ATOM   3494 H HE1  B TYR   A 1 161 ? 8.229  -7.459  7.996   0.32 21.69 ?  161 TYR   A HE1  1 
ATOM   3495 H HE2  A TYR   A 1 161 ? 4.311  -7.379  8.313   0.68 20.06 ?  161 TYR   A HE2  1 
ATOM   3496 H HE2  B TYR   A 1 161 ? 4.259  -6.955  8.187   0.32 21.66 ?  161 TYR   A HE2  1 
ATOM   3497 H HH   A TYR   A 1 161 ? 6.921  -9.240  9.327   0.68 20.04 ?  161 TYR   A HH   1 
ATOM   3498 H HH   B TYR   A 1 161 ? 6.966  -8.357  9.620   0.32 23.42 ?  161 TYR   A HH   1 
ATOM   3499 N N    A ASP   A 1 162 ? 4.038  -5.895  3.730   0.68 17.05 ?  162 ASP   A N    1 
ATOM   3500 N N    B ASP   A 1 162 ? 4.019  -6.350  3.072   0.32 15.78 ?  162 ASP   A N    1 
ATOM   3501 C CA   A ASP   A 1 162 ? 2.867  -6.763  3.665   0.68 17.55 ?  162 ASP   A CA   1 
ATOM   3502 C CA   B ASP   A 1 162 ? 2.918  -7.305  3.015   0.32 15.93 ?  162 ASP   A CA   1 
ATOM   3503 C C    A ASP   A 1 162 ? 2.901  -7.644  2.423   0.68 17.47 ?  162 ASP   A C    1 
ATOM   3504 C C    B ASP   A 1 162 ? 2.971  -8.155  1.749   0.32 15.55 ?  162 ASP   A C    1 
ATOM   3505 O O    A ASP   A 1 162 ? 2.542  -8.827  2.482   0.68 17.40 ?  162 ASP   A O    1 
ATOM   3506 O O    B ASP   A 1 162 ? 2.585  -9.330  1.779   0.32 14.96 ?  162 ASP   A O    1 
ATOM   3507 C CB   A ASP   A 1 162 ? 1.583  -5.931  3.693   0.68 18.92 ?  162 ASP   A CB   1 
ATOM   3508 C CB   B ASP   A 1 162 ? 1.581  -6.570  3.136   0.32 17.13 ?  162 ASP   A CB   1 
ATOM   3509 C CG   A ASP   A 1 162 ? 1.262  -5.382  5.068   0.68 20.50 ?  162 ASP   A CG   1 
ATOM   3510 C CG   B ASP   A 1 162 ? 1.391  -5.908  4.488   0.32 18.51 ?  162 ASP   A CG   1 
ATOM   3511 O OD1  A ASP   A 1 162 ? 1.904  -5.777  6.058   0.68 20.89 ?  162 ASP   A OD1  1 
ATOM   3512 O OD1  B ASP   A 1 162 ? 1.893  -6.444  5.498   0.32 19.19 ?  162 ASP   A OD1  1 
ATOM   3513 O OD2  A ASP   A 1 162 ? 0.336  -4.549  5.153   0.68 21.58 -1 162 ASP   A OD2  1 
ATOM   3514 O OD2  B ASP   A 1 162 ? 0.726  -4.850  4.539   0.32 19.28 -1 162 ASP   A OD2  1 
ATOM   3515 H H    A ASP   A 1 162 ? 3.861  -5.049  3.731   0.68 20.44 ?  162 ASP   A H    1 
ATOM   3516 H H    B ASP   A 1 162 ? 3.796  -5.538  2.914   0.32 18.91 ?  162 ASP   A H    1 
ATOM   3517 H HA   A ASP   A 1 162 ? 2.862  -7.345  4.433   0.68 21.04 ?  162 ASP   A HA   1 
ATOM   3518 H HA   B ASP   A 1 162 ? 2.986  -7.910  3.765   0.32 19.10 ?  162 ASP   A HA   1 
ATOM   3519 H HB2  A ASP   A 1 162 ? 1.677  -5.172  3.102   0.68 22.69 ?  162 ASP   A HB2  1 
ATOM   3520 H HB2  B ASP   A 1 162 ? 1.535  -5.870  2.472   0.32 20.53 ?  162 ASP   A HB2  1 
ATOM   3521 H HB3  A ASP   A 1 162 ? 0.838  -6.486  3.411   0.68 22.69 ?  162 ASP   A HB3  1 
ATOM   3522 H HB3  B ASP   A 1 162 ? 0.859  -7.203  3.012   0.32 20.53 ?  162 ASP   A HB3  1 
ATOM   3523 N N    A LYS   A 1 163 ? 3.307  -7.081  1.281   0.68 18.11 ?  163 LYS   A N    1 
ATOM   3524 N N    B LYS   A 1 163 ? 3.449  -7.592  0.635   0.32 16.06 ?  163 LYS   A N    1 
ATOM   3525 C CA   A LYS   A 1 163 ? 3.386  -7.880  0.061   0.68 18.77 ?  163 LYS   A CA   1 
ATOM   3526 C CA   B LYS   A 1 163 ? 3.620  -8.390  -0.576  0.32 16.86 ?  163 LYS   A CA   1 
ATOM   3527 C C    A LYS   A 1 163 ? 4.483  -8.930  0.165   0.68 18.31 ?  163 LYS   A C    1 
ATOM   3528 C C    B LYS   A 1 163 ? 4.689  -9.462  -0.379  0.32 14.98 ?  163 LYS   A C    1 
ATOM   3529 O O    A LYS   A 1 163 ? 4.325  -10.054 -0.321  0.68 18.41 ?  163 LYS   A O    1 
ATOM   3530 O O    B LYS   A 1 163 ? 4.537  -10.594 -0.855  0.32 14.63 ?  163 LYS   A O    1 
ATOM   3531 C CB   A LYS   A 1 163 ? 3.626  -6.977  -1.150  0.68 21.50 ?  163 LYS   A CB   1 
ATOM   3532 C CB   B LYS   A 1 163 ? 3.971  -7.478  -1.756  0.32 19.68 ?  163 LYS   A CB   1 
ATOM   3533 C CG   A LYS   A 1 163 ? 3.717  -7.730  -2.470  0.68 24.55 ?  163 LYS   A CG   1 
ATOM   3534 C CG   B LYS   A 1 163 ? 3.879  -8.156  -3.122  0.32 22.45 ?  163 LYS   A CG   1 
ATOM   3535 C CD   A LYS   A 1 163 ? 4.141  -6.817  -3.605  0.68 27.59 ?  163 LYS   A CD   1 
ATOM   3536 C CD   B LYS   A 1 163 ? 3.569  -7.163  -4.246  0.32 25.10 ?  163 LYS   A CD   1 
ATOM   3537 C CE   A LYS   A 1 163 ? 4.063  -7.531  -4.946  0.68 29.85 ?  163 LYS   A CE   1 
ATOM   3538 C CE   B LYS   A 1 163 ? 4.803  -6.402  -4.711  0.32 26.93 ?  163 LYS   A CE   1 
ATOM   3539 N NZ   A LYS   A 1 163 ? 4.666  -6.730  -6.046  0.68 31.02 ?  163 LYS   A NZ   1 
ATOM   3540 N NZ   B LYS   A 1 163 ? 4.927  -6.414  -6.201  0.32 27.81 ?  163 LYS   A NZ   1 
ATOM   3541 H H    A LYS   A 1 163 ? 3.530  -6.252  1.185   0.68 21.71 ?  163 LYS   A H    1 
ATOM   3542 H H    B LYS   A 1 163 ? 3.669  -6.763  0.555   0.32 19.25 ?  163 LYS   A H    1 
ATOM   3543 H HA   A LYS   A 1 163 ? 2.537  -8.335  -0.075  0.68 22.50 ?  163 LYS   A HA   1 
ATOM   3544 H HA   B LYS   A 1 163 ? 2.781  -8.830  -0.783  0.32 20.21 ?  163 LYS   A HA   1 
ATOM   3545 H HB2  A LYS   A 1 163 ? 2.888  -6.345  -1.226  0.68 25.77 ?  163 LYS   A HB2  1 
ATOM   3546 H HB2  B LYS   A 1 163 ? 3.364  -6.724  -1.760  0.32 23.60 ?  163 LYS   A HB2  1 
ATOM   3547 H HB3  A LYS   A 1 163 ? 4.455  -6.497  -1.025  0.68 25.77 ?  163 LYS   A HB3  1 
ATOM   3548 H HB3  B LYS   A 1 163 ? 4.883  -7.164  -1.647  0.32 23.60 ?  163 LYS   A HB3  1 
ATOM   3549 H HG2  A LYS   A 1 163 ? 4.375  -8.439  -2.396  0.68 29.44 ?  163 LYS   A HG2  1 
ATOM   3550 H HG2  B LYS   A 1 163 ? 4.727  -8.583  -3.322  0.32 26.91 ?  163 LYS   A HG2  1 
ATOM   3551 H HG3  A LYS   A 1 163 ? 2.847  -8.103  -2.688  0.68 29.44 ?  163 LYS   A HG3  1 
ATOM   3552 H HG3  B LYS   A 1 163 ? 3.171  -8.816  -3.104  0.32 26.91 ?  163 LYS   A HG3  1 
ATOM   3553 H HD2  A LYS   A 1 163 ? 3.551  -6.048  -3.636  0.68 33.08 ?  163 LYS   A HD2  1 
ATOM   3554 H HD2  B LYS   A 1 163 ? 3.211  -7.645  -5.008  0.32 30.09 ?  163 LYS   A HD2  1 
ATOM   3555 H HD3  A LYS   A 1 163 ? 5.057  -6.533  -3.463  0.68 33.08 ?  163 LYS   A HD3  1 
ATOM   3556 H HD3  B LYS   A 1 163 ? 2.920  -6.513  -3.932  0.32 30.09 ?  163 LYS   A HD3  1 
ATOM   3557 H HE2  A LYS   A 1 163 ? 4.532  -8.377  -4.885  0.68 35.80 ?  163 LYS   A HE2  1 
ATOM   3558 H HE2  B LYS   A 1 163 ? 4.733  -5.478  -4.429  0.32 32.29 ?  163 LYS   A HE2  1 
ATOM   3559 H HE3  A LYS   A 1 163 ? 3.133  -7.687  -5.166  0.68 35.80 ?  163 LYS   A HE3  1 
ATOM   3560 H HE3  B LYS   A 1 163 ? 5.599  -6.804  -4.332  0.32 32.29 ?  163 LYS   A HE3  1 
ATOM   3561 H HZ1  A LYS   A 1 163 ? 4.606  -7.174  -6.815  0.68 37.20 ?  163 LYS   A HZ1  1 
ATOM   3562 H HZ1  B LYS   A 1 163 ? 5.655  -5.967  -6.451  0.32 33.35 ?  163 LYS   A HZ1  1 
ATOM   3563 H HZ2  A LYS   A 1 163 ? 4.237  -5.954  -6.127  0.68 37.20 ?  163 LYS   A HZ2  1 
ATOM   3564 H HZ2  B LYS   A 1 163 ? 4.989  -7.253  -6.495  0.32 33.35 ?  163 LYS   A HZ2  1 
ATOM   3565 H HZ3  A LYS   A 1 163 ? 5.524  -6.568  -5.872  0.68 37.20 ?  163 LYS   A HZ3  1 
ATOM   3566 H HZ3  B LYS   A 1 163 ? 4.212  -6.032  -6.569  0.32 33.35 ?  163 LYS   A HZ3  1 
ATOM   3567 N N    A LEU   A 1 164 ? 5.609  -8.576  0.784   0.68 16.73 ?  164 LEU   A N    1 
ATOM   3568 N N    B LEU   A 1 164 ? 5.774  -9.119  0.323   0.32 14.00 ?  164 LEU   A N    1 
ATOM   3569 C CA   A LEU   A 1 164 ? 6.703  -9.531  0.928   0.68 16.33 ?  164 LEU   A CA   1 
ATOM   3570 C CA   B LEU   A 1 164 ? 6.857  -10.071 0.564   0.32 13.61 ?  164 LEU   A CA   1 
ATOM   3571 C C    A LEU   A 1 164 ? 6.290  -10.710 1.796   0.68 16.21 ?  164 LEU   A C    1 
ATOM   3572 C C    B LEU   A 1 164 ? 6.369  -11.271 1.364   0.32 14.11 ?  164 LEU   A C    1 
ATOM   3573 O O    A LEU   A 1 164 ? 6.625  -11.865 1.498   0.68 16.38 ?  164 LEU   A O    1 
ATOM   3574 O O    B LEU   A 1 164 ? 6.576  -12.422 0.965   0.32 14.04 ?  164 LEU   A O    1 
ATOM   3575 C CB   A LEU   A 1 164 ? 7.909  -8.819  1.528   0.68 16.22 ?  164 LEU   A CB   1 
ATOM   3576 C CB   B LEU   A 1 164 ? 8.003  -9.391  1.319   0.32 13.59 ?  164 LEU   A CB   1 
ATOM   3577 C CG   A LEU   A 1 164 ? 8.662  -7.929  0.541   0.68 17.02 ?  164 LEU   A CG   1 
ATOM   3578 C CG   B LEU   A 1 164 ? 8.815  -8.272  0.669   0.32 14.08 ?  164 LEU   A CG   1 
ATOM   3579 C CD1  A LEU   A 1 164 ? 9.649  -7.067  1.287   0.68 16.08 ?  164 LEU   A CD1  1 
ATOM   3580 C CD1  B LEU   A 1 164 ? 9.583  -7.482  1.729   0.32 14.38 ?  164 LEU   A CD1  1 
ATOM   3581 C CD2  A LEU   A 1 164 ? 9.374  -8.759  -0.516  0.68 17.55 ?  164 LEU   A CD2  1 
ATOM   3582 C CD2  B LEU   A 1 164 ? 9.774  -8.844  -0.353  0.32 14.16 ?  164 LEU   A CD2  1 
ATOM   3583 H H    A LEU   A 1 164 ? 5.760  -7.789  1.117   0.68 20.05 ?  164 LEU   A H    1 
ATOM   3584 H H    B LEU   A 1 164 ? 5.905  -8.351  0.667   0.32 16.78 ?  164 LEU   A H    1 
ATOM   3585 H HA   A LEU   A 1 164 ? 6.946  -9.862  0.053   0.68 19.57 ?  164 LEU   A HA   1 
ATOM   3586 H HA   B LEU   A 1 164 ? 7.192  -10.402 -0.282  0.32 16.30 ?  164 LEU   A HA   1 
ATOM   3587 H HB2  A LEU   A 1 164 ? 7.607  -8.253  2.260   0.68 19.44 ?  164 LEU   A HB2  1 
ATOM   3588 H HB2  B LEU   A 1 164 ? 7.629  -9.025  2.130   0.32 16.29 ?  164 LEU   A HB2  1 
ATOM   3589 H HB3  A LEU   A 1 164 ? 8.527  -9.482  1.858   0.68 19.44 ?  164 LEU   A HB3  1 
ATOM   3590 H HB3  B LEU   A 1 164 ? 8.637  -10.087 1.555   0.32 16.29 ?  164 LEU   A HB3  1 
ATOM   3591 H HG   A LEU   A 1 164 ? 8.031  -7.343  0.090   0.68 20.40 ?  164 LEU   A HG   1 
ATOM   3592 H HG   B LEU   A 1 164 ? 8.214  -7.665  0.215   0.32 16.87 ?  164 LEU   A HG   1 
ATOM   3593 H HD11 A LEU   A 1 164 ? 10.067 -6.451  0.665   0.68 19.27 ?  164 LEU   A HD11 1 
ATOM   3594 H HD11 B LEU   A 1 164 ? 10.036 -6.738  1.304   0.32 17.23 ?  164 LEU   A HD11 1 
ATOM   3595 H HD12 A LEU   A 1 164 ? 9.178  -6.574  1.976   0.68 19.27 ?  164 LEU   A HD12 1 
ATOM   3596 H HD12 B LEU   A 1 164 ? 8.957  -7.152  2.395   0.32 17.23 ?  164 LEU   A HD12 1 
ATOM   3597 H HD13 A LEU   A 1 164 ? 10.322 -7.638  1.691   0.68 19.27 ?  164 LEU   A HD13 1 
ATOM   3598 H HD13 B LEU   A 1 164 ? 10.232 -8.067  2.153   0.32 17.23 ?  164 LEU   A HD13 1 
ATOM   3599 H HD21 A LEU   A 1 164 ? 9.972  -8.184  -1.020  0.68 21.03 ?  164 LEU   A HD21 1 
ATOM   3600 H HD21 B LEU   A 1 164 ? 10.220 -8.112  -0.809  0.32 16.97 ?  164 LEU   A HD21 1 
ATOM   3601 H HD22 A LEU   A 1 164 ? 9.881  -9.459  -0.077  0.68 21.03 ?  164 LEU   A HD22 1 
ATOM   3602 H HD22 B LEU   A 1 164 ? 10.427 -9.400  0.101   0.32 16.97 ?  164 LEU   A HD22 1 
ATOM   3603 H HD23 A LEU   A 1 164 ? 8.715  -9.151  -1.111  0.68 21.03 ?  164 LEU   A HD23 1 
ATOM   3604 H HD23 B LEU   A 1 164 ? 9.269  -9.373  -0.988  0.32 16.97 ?  164 LEU   A HD23 1 
ATOM   3605 N N    A VAL   A 1 165 ? 5.558  -10.436 2.874   0.68 15.67 ?  165 VAL   A N    1 
ATOM   3606 N N    B VAL   A 1 165 ? 5.748  -11.023 2.519   0.32 14.65 ?  165 VAL   A N    1 
ATOM   3607 C CA   A VAL   A 1 165 ? 5.078  -11.512 3.733   0.68 15.98 ?  165 VAL   A CA   1 
ATOM   3608 C CA   B VAL   A 1 165 ? 5.312  -12.121 3.378   0.32 14.84 ?  165 VAL   A CA   1 
ATOM   3609 C C    A VAL   A 1 165 ? 4.062  -12.372 2.995   0.68 16.51 ?  165 VAL   A C    1 
ATOM   3610 C C    B VAL   A 1 165 ? 4.192  -12.908 2.708   0.32 14.88 ?  165 VAL   A C    1 
ATOM   3611 O O    A VAL   A 1 165 ? 4.164  -13.604 2.976   0.68 16.39 ?  165 VAL   A O    1 
ATOM   3612 O O    B VAL   A 1 165 ? 4.236  -14.141 2.628   0.32 14.32 ?  165 VAL   A O    1 
ATOM   3613 C CB   A VAL   A 1 165 ? 4.499  -10.940 5.038   0.68 16.54 ?  165 VAL   A CB   1 
ATOM   3614 C CB   B VAL   A 1 165 ? 4.901  -11.593 4.767   0.32 15.53 ?  165 VAL   A CB   1 
ATOM   3615 C CG1  A VAL   A 1 165 ? 3.756  -12.023 5.808   0.68 16.65 ?  165 VAL   A CG1  1 
ATOM   3616 C CG1  B VAL   A 1 165 ? 4.310  -12.716 5.617   0.32 15.80 ?  165 VAL   A CG1  1 
ATOM   3617 C CG2  A VAL   A 1 165 ? 5.605  -10.324 5.880   0.68 16.61 ?  165 VAL   A CG2  1 
ATOM   3618 C CG2  B VAL   A 1 165 ? 6.094  -10.965 5.473   0.32 15.92 ?  165 VAL   A CG2  1 
ATOM   3619 H H    A VAL   A 1 165 ? 5.315  -9.645  3.120   0.68 18.78 ?  165 VAL   A H    1 
ATOM   3620 H H    B VAL   A 1 165 ? 5.562  -10.245 2.825   0.32 17.55 ?  165 VAL   A H    1 
ATOM   3621 H HA   A VAL   A 1 165 ? 5.823  -12.079 3.965   0.68 19.15 ?  165 VAL   A HA   1 
ATOM   3622 H HA   B VAL   A 1 165 ? 6.054  -12.732 3.515   0.32 17.78 ?  165 VAL   A HA   1 
ATOM   3623 H HB   A VAL   A 1 165 ? 3.863  -10.238 4.824   0.68 19.82 ?  165 VAL   A HB   1 
ATOM   3624 H HB   B VAL   A 1 165 ? 4.221  -10.911 4.665   0.32 18.61 ?  165 VAL   A HB   1 
ATOM   3625 H HG11 A VAL   A 1 165 ? 3.654  -11.741 6.731   0.68 19.96 ?  165 VAL   A HG11 1 
ATOM   3626 H HG11 B VAL   A 1 165 ? 4.283  -12.431 6.545   0.32 18.93 ?  165 VAL   A HG11 1 
ATOM   3627 H HG12 A VAL   A 1 165 ? 2.879  -12.154 5.409   0.68 19.96 ?  165 VAL   A HG12 1 
ATOM   3628 H HG12 B VAL   A 1 165 ? 3.412  -12.912 5.309   0.32 18.93 ?  165 VAL   A HG12 1 
ATOM   3629 H HG13 A VAL   A 1 165 ? 4.265  -12.846 5.769   0.68 19.96 ?  165 VAL   A HG13 1 
ATOM   3630 H HG13 B VAL   A 1 165 ? 4.870  -13.504 5.534   0.32 18.93 ?  165 VAL   A HG13 1 
ATOM   3631 H HG21 A VAL   A 1 165 ? 5.229  -10.011 6.718   0.68 19.91 ?  165 VAL   A HG21 1 
ATOM   3632 H HG21 B VAL   A 1 165 ? 5.821  -10.658 6.353   0.32 19.08 ?  165 VAL   A HG21 1 
ATOM   3633 H HG22 A VAL   A 1 165 ? 6.284  -10.995 6.051   0.68 19.91 ?  165 VAL   A HG22 1 
ATOM   3634 H HG22 B VAL   A 1 165 ? 6.797  -11.630 5.561   0.32 19.08 ?  165 VAL   A HG22 1 
ATOM   3635 H HG23 A VAL   A 1 165 ? 5.994  -9.578  5.394   0.68 19.91 ?  165 VAL   A HG23 1 
ATOM   3636 H HG23 B VAL   A 1 165 ? 6.413  -10.216 4.947   0.32 19.08 ?  165 VAL   A HG23 1 
ATOM   3637 N N    A SER   A 1 166 ? 3.067  -11.735 2.371   0.68 17.43 ?  166 SER   A N    1 
ATOM   3638 N N    B SER   A 1 166 ? 3.181  -12.204 2.196   0.32 15.38 ?  166 SER   A N    1 
ATOM   3639 C CA   A SER   A 1 166 ? 1.961  -12.495 1.794   0.68 18.71 ?  166 SER   A CA   1 
ATOM   3640 C CA   B SER   A 1 166 ? 2.007  -12.870 1.647   0.32 16.17 ?  166 SER   A CA   1 
ATOM   3641 C C    A SER   A 1 166 ? 2.418  -13.390 0.651   0.68 19.13 ?  166 SER   A C    1 
ATOM   3642 C C    B SER   A 1 166 ? 2.313  -13.636 0.370   0.32 17.28 ?  166 SER   A C    1 
ATOM   3643 O O    A SER   A 1 166 ? 1.813  -14.446 0.414   0.68 20.76 ?  166 SER   A O    1 
ATOM   3644 O O    B SER   A 1 166 ? 1.549  -14.538 0.008   0.32 17.79 ?  166 SER   A O    1 
ATOM   3645 C CB   A SER   A 1 166 ? 0.848  -11.553 1.321   0.68 20.22 ?  166 SER   A CB   1 
ATOM   3646 C CB   B SER   A 1 166 ? 0.883  -11.857 1.403   0.32 16.06 ?  166 SER   A CB   1 
ATOM   3647 O OG   A SER   A 1 166 ? 0.206  -10.924 2.416   0.68 21.83 ?  166 SER   A OG   1 
ATOM   3648 O OG   B SER   A 1 166 ? 1.187  -10.986 0.327   0.32 15.86 ?  166 SER   A OG   1 
ATOM   3649 H H    A SER   A 1 166 ? 3.001  -10.881 2.278   0.68 20.90 ?  166 SER   A H    1 
ATOM   3650 H H    B SER   A 1 166 ? 3.155  -11.354 2.159   0.32 18.43 ?  166 SER   A H    1 
ATOM   3651 H HA   A SER   A 1 166 ? 1.579  -13.067 2.478   0.68 22.43 ?  166 SER   A HA   1 
ATOM   3652 H HA   B SER   A 1 166 ? 1.679  -13.515 2.293   0.32 19.38 ?  166 SER   A HA   1 
ATOM   3653 H HB2  A SER   A 1 166 ? 1.228  -10.881 0.734   0.68 24.24 ?  166 SER   A HB2  1 
ATOM   3654 H HB2  B SER   A 1 166 ? 0.064  -12.336 1.195   0.32 19.24 ?  166 SER   A HB2  1 
ATOM   3655 H HB3  A SER   A 1 166 ? 0.175  -12.066 0.846   0.68 24.24 ?  166 SER   A HB3  1 
ATOM   3656 H HB3  B SER   A 1 166 ? 0.757  -11.330 2.209   0.32 19.24 ?  166 SER   A HB3  1 
ATOM   3657 H HG   A SER   A 1 166 ? -0.380 -10.386 2.140   0.68 26.17 ?  166 SER   A HG   1 
ATOM   3658 H HG   B SER   A 1 166 ? 1.891  -10.555 0.494   0.32 19.01 ?  166 SER   A HG   1 
ATOM   3659 N N    A SER   A 1 167 ? 3.472  -12.995 -0.065  0.68 18.47 ?  167 SER   A N    1 
ATOM   3660 N N    B SER   A 1 167 ? 3.408  -13.314 -0.314  0.32 17.81 ?  167 SER   A N    1 
ATOM   3661 C CA   A SER   A 1 167 ? 3.930  -13.728 -1.237  0.68 18.96 ?  167 SER   A CA   1 
ATOM   3662 C CA   B SER   A 1 167 ? 3.795  -14.031 -1.519  0.32 18.76 ?  167 SER   A CA   1 
ATOM   3663 C C    A SER   A 1 167 ? 5.075  -14.689 -0.939  0.68 18.97 ?  167 SER   A C    1 
ATOM   3664 C C    B SER   A 1 167 ? 5.021  -14.903 -1.312  0.32 19.84 ?  167 SER   A C    1 
ATOM   3665 O O    A SER   A 1 167 ? 5.589  -15.321 -1.866  0.68 19.83 ?  167 SER   A O    1 
ATOM   3666 O O    B SER   A 1 167 ? 5.498  -15.515 -2.274  0.32 20.20 ?  167 SER   A O    1 
ATOM   3667 C CB   A SER   A 1 167 ? 4.357  -12.751 -2.343  0.68 19.42 ?  167 SER   A CB   1 
ATOM   3668 C CB   B SER   A 1 167 ? 4.034  -13.055 -2.678  0.32 18.35 ?  167 SER   A CB   1 
ATOM   3669 O OG   A SER   A 1 167 ? 5.393  -11.890 -1.890  0.68 19.58 ?  167 SER   A OG   1 
ATOM   3670 O OG   B SER   A 1 167 ? 5.291  -12.416 -2.553  0.32 17.77 ?  167 SER   A OG   1 
ATOM   3671 H H    A SER   A 1 167 ? 3.934  -12.287 0.109   0.68 22.14 ?  167 SER   A H    1 
ATOM   3672 H H    B SER   A 1 167 ? 3.953  -12.683 -0.092  0.32 21.34 ?  167 SER   A H    1 
ATOM   3673 H HA   A SER   A 1 167 ? 3.185  -14.243 -1.583  0.68 22.73 ?  167 SER   A HA   1 
ATOM   3674 H HA   B SER   A 1 167 ? 3.073  -14.614 -1.782  0.32 22.49 ?  167 SER   A HA   1 
ATOM   3675 H HB2  A SER   A 1 167 ? 4.681  -13.260 -3.103  0.68 23.29 ?  167 SER   A HB2  1 
ATOM   3676 H HB2  B SER   A 1 167 ? 4.008  -13.548 -3.515  0.32 21.99 ?  167 SER   A HB2  1 
ATOM   3677 H HB3  A SER   A 1 167 ? 3.585  -12.220 -2.613  0.68 23.29 ?  167 SER   A HB3  1 
ATOM   3678 H HB3  B SER   A 1 167 ? 3.331  -12.383 -2.673  0.32 21.99 ?  167 SER   A HB3  1 
ATOM   3679 H HG   A SER   A 1 167 ? 5.105  -11.415 -1.254  0.68 23.47 ?  167 SER   A HG   1 
ATOM   3680 H HG   B SER   A 1 167 ? 5.321  -11.983 -1.836  0.32 21.30 ?  167 SER   A HG   1 
ATOM   3681 N N    A PHE   A 1 168 ? 5.481  -14.829 0.320   0.68 18.18 ?  168 PHE   A N    1 
ATOM   3682 N N    B PHE   A 1 168 ? 5.535  -14.993 -0.087  0.32 20.74 ?  168 PHE   A N    1 
ATOM   3683 C CA   A PHE   A 1 168 ? 6.668  -15.620 0.622   0.68 18.66 ?  168 PHE   A CA   1 
ATOM   3684 C CA   B PHE   A 1 168 ? 6.741  -15.776 0.152   0.32 21.95 ?  168 PHE   A CA   1 
ATOM   3685 C C    A PHE   A 1 168 ? 6.373  -17.107 0.496   0.68 20.34 ?  168 PHE   A C    1 
ATOM   3686 C C    B PHE   A 1 168 ? 6.426  -17.259 0.031   0.32 24.82 ?  168 PHE   A C    1 
ATOM   3687 O O    A PHE   A 1 168 ? 5.372  -17.602 1.025   0.68 22.17 ?  168 PHE   A O    1 
ATOM   3688 O O    B PHE   A 1 168 ? 5.664  -17.811 0.832   0.32 25.27 ?  168 PHE   A O    1 
ATOM   3689 C CB   A PHE   A 1 168 ? 7.173  -15.322 2.031   0.68 17.96 ?  168 PHE   A CB   1 
ATOM   3690 C CB   B PHE   A 1 168 ? 7.327  -15.475 1.527   0.32 20.70 ?  168 PHE   A CB   1 
ATOM   3691 C CG   A PHE   A 1 168 ? 8.448  -16.039 2.366   0.68 17.30 ?  168 PHE   A CG   1 
ATOM   3692 C CG   B PHE   A 1 168 ? 8.572  -16.261 1.826   0.32 19.33 ?  168 PHE   A CG   1 
ATOM   3693 C CD1  A PHE   A 1 168 ? 9.639  -15.645 1.786   0.68 16.94 ?  168 PHE   A CD1  1 
ATOM   3694 C CD1  B PHE   A 1 168 ? 9.724  -16.061 1.082   0.32 18.93 ?  168 PHE   A CD1  1 
ATOM   3695 C CD2  A PHE   A 1 168 ? 8.457  -17.120 3.233   0.68 17.14 ?  168 PHE   A CD2  1 
ATOM   3696 C CD2  B PHE   A 1 168 ? 8.587  -17.210 2.835   0.32 18.55 ?  168 PHE   A CD2  1 
ATOM   3697 C CE1  A PHE   A 1 168 ? 10.813 -16.303 2.073   0.68 16.20 ?  168 PHE   A CE1  1 
ATOM   3698 C CE1  B PHE   A 1 168 ? 10.870 -16.783 1.345   0.32 18.43 ?  168 PHE   A CE1  1 
ATOM   3699 C CE2  A PHE   A 1 168 ? 9.635  -17.778 3.526   0.68 17.12 ?  168 PHE   A CE2  1 
ATOM   3700 C CE2  B PHE   A 1 168 ? 9.732  -17.936 3.102   0.32 18.20 ?  168 PHE   A CE2  1 
ATOM   3701 C CZ   A PHE   A 1 168 ? 10.812 -17.369 2.944   0.68 16.56 ?  168 PHE   A CZ   1 
ATOM   3702 C CZ   B PHE   A 1 168 ? 10.875 -17.722 2.355   0.32 18.18 ?  168 PHE   A CZ   1 
ATOM   3703 H H    A PHE   A 1 168 ? 5.097  -14.474 1.003   0.68 21.79 ?  168 PHE   A H    1 
ATOM   3704 H H    B PHE   A 1 168 ? 5.206  -14.615 0.614   0.32 24.86 ?  168 PHE   A H    1 
ATOM   3705 H HA   A PHE   A 1 168 ? 7.368  -15.393 -0.009  0.68 22.37 ?  168 PHE   A HA   1 
ATOM   3706 H HA   B PHE   A 1 168 ? 7.402  -15.550 -0.518  0.32 26.31 ?  168 PHE   A HA   1 
ATOM   3707 H HB2  A PHE   A 1 168 ? 7.334  -14.368 2.110   0.68 21.52 ?  168 PHE   A HB2  1 
ATOM   3708 H HB2  B PHE   A 1 168 ? 7.554  -14.534 1.575   0.32 24.82 ?  168 PHE   A HB2  1 
ATOM   3709 H HB3  A PHE   A 1 168 ? 6.495  -15.596 2.669   0.68 21.52 ?  168 PHE   A HB3  1 
ATOM   3710 H HB3  B PHE   A 1 168 ? 6.667  -15.690 2.205   0.32 24.82 ?  168 PHE   A HB3  1 
ATOM   3711 H HD1  A PHE   A 1 168 ? 9.648  -14.926 1.197   0.68 20.31 ?  168 PHE   A HD1  1 
ATOM   3712 H HD1  B PHE   A 1 168 ? 9.725  -15.431 0.398   0.32 22.69 ?  168 PHE   A HD1  1 
ATOM   3713 H HD2  A PHE   A 1 168 ? 7.662  -17.399 3.627   0.68 20.55 ?  168 PHE   A HD2  1 
ATOM   3714 H HD2  B PHE   A 1 168 ? 7.820  -17.356 3.340   0.32 22.24 ?  168 PHE   A HD2  1 
ATOM   3715 H HE1  A PHE   A 1 168 ? 11.613 -16.026 1.683   0.68 19.41 ?  168 PHE   A HE1  1 
ATOM   3716 H HE1  B PHE   A 1 168 ? 11.637 -16.640 0.839   0.32 22.09 ?  168 PHE   A HE1  1 
ATOM   3717 H HE2  A PHE   A 1 168 ? 9.630  -18.500 4.114   0.68 20.52 ?  168 PHE   A HE2  1 
ATOM   3718 H HE2  B PHE   A 1 168 ? 9.733  -18.569 3.784   0.32 21.82 ?  168 PHE   A HE2  1 
ATOM   3719 H HZ   A PHE   A 1 168 ? 11.609 -17.812 3.141   0.68 19.84 ?  168 PHE   A HZ   1 
ATOM   3720 H HZ   B PHE   A 1 168 ? 11.646 -18.211 2.533   0.32 21.79 ?  168 PHE   A HZ   1 
ATOM   3721 N N    A LEU   A 1 169 ? 7.267  -17.825 -0.180  0.68 22.45 ?  169 LEU   A N    1 
ATOM   3722 N N    B LEU   A 1 169 ? 7.021  -17.903 -0.964  0.32 27.46 ?  169 LEU   A N    1 
ATOM   3723 C CA   A LEU   A 1 169 ? 7.103  -19.258 -0.353  0.68 27.20 ?  169 LEU   A CA   1 
ATOM   3724 C CA   B LEU   A 1 169 ? 6.813  -19.323 -1.182  0.32 29.97 ?  169 LEU   A CA   1 
ATOM   3725 C C    A LEU   A 1 169 ? 8.009  -19.988 0.626   0.68 28.84 ?  169 LEU   A C    1 
ATOM   3726 C C    B LEU   A 1 169 ? 7.589  -20.128 -0.145  0.32 30.75 ?  169 LEU   A C    1 
ATOM   3727 O O    A LEU   A 1 169 ? 7.550  -20.421 1.685   0.68 29.55 ?  169 LEU   A O    1 
ATOM   3728 O O    B LEU   A 1 169 ? 7.014  -20.656 0.808   0.32 30.98 ?  169 LEU   A O    1 
ATOM   3729 C CB   A LEU   A 1 169 ? 7.408  -19.669 -1.798  0.68 29.59 ?  169 LEU   A CB   1 
ATOM   3730 C CB   B LEU   A 1 169 ? 7.271  -19.706 -2.589  0.32 31.34 ?  169 LEU   A CB   1 
ATOM   3731 C CG   A LEU   A 1 169 ? 7.092  -21.124 -2.162  0.68 31.41 ?  169 LEU   A CG   1 
ATOM   3732 C CG   B LEU   A 1 169 ? 6.870  -21.097 -3.077  0.32 32.46 ?  169 LEU   A CG   1 
ATOM   3733 C CD1  A LEU   A 1 169 ? 5.668  -21.484 -1.766  0.68 32.05 ?  169 LEU   A CD1  1 
ATOM   3734 C CD1  B LEU   A 1 169 ? 5.361  -21.265 -3.017  0.32 32.79 ?  169 LEU   A CD1  1 
ATOM   3735 C CD2  A LEU   A 1 169 ? 7.308  -21.370 -3.650  0.68 31.93 ?  169 LEU   A CD2  1 
ATOM   3736 C CD2  B LEU   A 1 169 ? 7.382  -21.326 -4.489  0.32 32.82 ?  169 LEU   A CD2  1 
ATOM   3737 O OXT  A LEU   A 1 169 ? 9.208  -20.143 0.395   0.68 28.86 -1 169 LEU   A OXT  1 
ATOM   3738 O OXT  B LEU   A 1 169 ? 8.811  -20.258 -0.231  0.32 31.05 -1 169 LEU   A OXT  1 
ATOM   3739 H H    A LEU   A 1 169 ? 7.977  -17.504 -0.545  0.68 26.91 ?  169 LEU   A H    1 
ATOM   3740 H H    B LEU   A 1 169 ? 7.549  -17.531 -1.531  0.32 32.93 ?  169 LEU   A H    1 
ATOM   3741 H HA   A LEU   A 1 169 ? 6.189  -19.500 -0.152  0.68 32.62 ?  169 LEU   A HA   1 
ATOM   3742 H HA   B LEU   A 1 169 ? 5.867  -19.522 -1.091  0.32 35.94 ?  169 LEU   A HA   1 
ATOM   3743 H HB2  A LEU   A 1 169 ? 6.885  -19.107 -2.392  0.68 35.48 ?  169 LEU   A HB2  1 
ATOM   3744 H HB2  B LEU   A 1 169 ? 6.904  -19.064 -3.215  0.32 37.59 ?  169 LEU   A HB2  1 
ATOM   3745 H HB3  A LEU   A 1 169 ? 8.351  -19.530 -1.968  0.68 35.48 ?  169 LEU   A HB3  1 
ATOM   3746 H HB3  B LEU   A 1 169 ? 8.240  -19.660 -2.613  0.32 37.59 ?  169 LEU   A HB3  1 
ATOM   3747 H HG   A LEU   A 1 169 ? 7.694  -21.710 -1.676  0.68 37.67 ?  169 LEU   A HG   1 
ATOM   3748 H HG   B LEU   A 1 169 ? 7.272  -21.764 -2.499  0.32 38.93 ?  169 LEU   A HG   1 
ATOM   3749 H HD11 A LEU   A 1 169 ? 5.420  -22.316 -2.198  0.68 38.43 ?  169 LEU   A HD11 1 
ATOM   3750 H HD11 B LEU   A 1 169 ? 5.112  -22.048 -3.530  0.32 39.32 ?  169 LEU   A HD11 1 
ATOM   3751 H HD12 A LEU   A 1 169 ? 5.624  -21.587 -0.803  0.68 38.43 ?  169 LEU   A HD12 1 
ATOM   3752 H HD12 B LEU   A 1 169 ? 5.092  -21.377 -2.091  0.32 39.32 ?  169 LEU   A HD12 1 
ATOM   3753 H HD13 A LEU   A 1 169 ? 5.073  -20.774 -2.053  0.68 38.43 ?  169 LEU   A HD13 1 
ATOM   3754 H HD13 B LEU   A 1 169 ? 4.941  -20.475 -3.392  0.32 39.32 ?  169 LEU   A HD13 1 
ATOM   3755 H HD21 A LEU   A 1 169 ? 7.109  -22.299 -3.850  0.68 38.29 ?  169 LEU   A HD21 1 
ATOM   3756 H HD21 B LEU   A 1 169 ? 7.123  -22.214 -4.778  0.32 39.36 ?  169 LEU   A HD21 1 
ATOM   3757 H HD22 A LEU   A 1 169 ? 6.715  -20.791 -4.155  0.68 38.29 ?  169 LEU   A HD22 1 
ATOM   3758 H HD22 B LEU   A 1 169 ? 6.993  -20.659 -5.077  0.32 39.36 ?  169 LEU   A HD22 1 
ATOM   3759 H HD23 A LEU   A 1 169 ? 8.231  -21.174 -3.872  0.68 38.29 ?  169 LEU   A HD23 1 
ATOM   3760 H HD23 B LEU   A 1 169 ? 8.349  -21.245 -4.491  0.32 39.36 ?  169 LEU   A HD23 1 
ATOM   3761 N N    A SER   B 1 1   ? 50.796 -9.237  -23.758 0.68 28.35 ?  1   SER   B N    1 
ATOM   3762 N N    B SER   B 1 1   ? 50.684 -9.266  -23.740 0.32 26.83 ?  1   SER   B N    1 
ATOM   3763 C CA   A SER   B 1 1   ? 51.289 -10.287 -22.845 0.68 28.30 ?  1   SER   B CA   1 
ATOM   3764 C CA   B SER   B 1 1   ? 51.189 -10.271 -22.781 0.32 26.66 ?  1   SER   B CA   1 
ATOM   3765 C C    A SER   B 1 1   ? 50.212 -11.330 -22.578 0.68 27.15 ?  1   SER   B C    1 
ATOM   3766 C C    B SER   B 1 1   ? 50.136 -11.343 -22.532 0.32 25.91 ?  1   SER   B C    1 
ATOM   3767 O O    A SER   B 1 1   ? 49.016 -11.118 -22.834 0.68 26.85 ?  1   SER   B O    1 
ATOM   3768 O O    B SER   B 1 1   ? 48.959 -11.178 -22.871 0.32 25.46 ?  1   SER   B O    1 
ATOM   3769 C CB   A SER   B 1 1   ? 51.762 -9.683  -21.526 0.68 29.03 ?  1   SER   B CB   1 
ATOM   3770 C CB   B SER   B 1 1   ? 51.569 -9.609  -21.461 0.32 27.00 ?  1   SER   B CB   1 
ATOM   3771 O OG   A SER   B 1 1   ? 50.666 -9.390  -20.682 0.68 30.80 ?  1   SER   B OG   1 
ATOM   3772 O OG   B SER   B 1 1   ? 50.443 -9.510  -20.608 0.32 27.82 ?  1   SER   B OG   1 
ATOM   3773 H H1   A SER   B 1 1   ? 50.688 -9.585  -24.567 0.68 34.00 ?  1   SER   B H1   1 
ATOM   3774 H H1   B SER   B 1 1   ? 51.375 -8.885  -24.148 0.32 32.17 ?  1   SER   B H1   1 
ATOM   3775 H H2   A SER   B 1 1   ? 50.023 -8.929  -23.454 0.68 34.00 ?  1   SER   B H2   1 
ATOM   3776 H H2   B SER   B 1 1   ? 50.168 -9.670  -24.338 0.32 32.17 ?  1   SER   B H2   1 
ATOM   3777 H H3   A SER   B 1 1   ? 51.394 -8.581  -23.788 0.68 34.00 ?  1   SER   B H3   1 
ATOM   3778 H H3   B SER   B 1 1   ? 50.218 -8.655  -23.299 0.32 32.17 ?  1   SER   B H3   1 
ATOM   3779 H HA   A SER   B 1 1   ? 52.040 -10.723 -23.267 0.68 33.93 ?  1   SER   B HA   1 
ATOM   3780 H HA   B SER   B 1 1   ? 51.977 -10.683 -23.160 0.32 31.97 ?  1   SER   B HA   1 
ATOM   3781 H HB2  A SER   B 1 1   ? 52.342 -10.322 -21.085 0.68 34.81 ?  1   SER   B HB2  1 
ATOM   3782 H HB2  B SER   B 1 1   ? 52.253 -10.146 -21.034 0.32 32.38 ?  1   SER   B HB2  1 
ATOM   3783 H HB3  A SER   B 1 1   ? 52.247 -8.863  -21.708 0.68 34.81 ?  1   SER   B HB3  1 
ATOM   3784 H HB3  B SER   B 1 1   ? 51.907 -8.718  -21.637 0.32 32.38 ?  1   SER   B HB3  1 
ATOM   3785 H HG   A SER   B 1 1   ? 50.928 -8.930  -20.028 0.68 36.94 ?  1   SER   B HG   1 
ATOM   3786 H HG   B SER   B 1 1   ? 50.615 -8.986  -19.975 0.32 33.36 ?  1   SER   B HG   1 
ATOM   3787 N N    A MET   B 1 2   ? 50.658 -12.459 -22.046 0.68 26.50 ?  2   MET   B N    1 
ATOM   3788 N N    B MET   B 1 2   ? 50.573 -12.438 -21.923 0.32 25.61 ?  2   MET   B N    1 
ATOM   3789 C CA   A MET   B 1 2   ? 49.835 -13.648 -21.875 0.68 26.49 ?  2   MET   B CA   1 
ATOM   3790 C CA   B MET   B 1 2   ? 49.761 -13.638 -21.754 0.32 25.32 ?  2   MET   B CA   1 
ATOM   3791 C C    A MET   B 1 2   ? 49.603 -13.851 -20.384 0.68 24.07 ?  2   MET   B C    1 
ATOM   3792 C C    B MET   B 1 2   ? 49.511 -13.849 -20.266 0.32 23.83 ?  2   MET   B C    1 
ATOM   3793 O O    A MET   B 1 2   ? 50.548 -14.114 -19.635 0.68 24.06 ?  2   MET   B O    1 
ATOM   3794 O O    B MET   B 1 2   ? 50.402 -14.284 -19.531 0.32 24.22 ?  2   MET   B O    1 
ATOM   3795 C CB   A MET   B 1 2   ? 50.555 -14.842 -22.490 0.68 30.36 ?  2   MET   B CB   1 
ATOM   3796 C CB   B MET   B 1 2   ? 50.504 -14.818 -22.355 0.32 27.04 ?  2   MET   B CB   1 
ATOM   3797 C CG   A MET   B 1 2   ? 49.710 -16.093 -22.647 0.68 34.00 ?  2   MET   B CG   1 
ATOM   3798 C CG   B MET   B 1 2   ? 49.625 -15.963 -22.833 0.32 28.41 ?  2   MET   B CG   1 
ATOM   3799 S SD   A MET   B 1 2   ? 50.558 -17.325 -23.656 0.68 37.48 ?  2   MET   B SD   1 
ATOM   3800 S SD   B MET   B 1 2   ? 50.528 -17.053 -23.941 0.32 29.71 ?  2   MET   B SD   1 
ATOM   3801 C CE   A MET   B 1 2   ? 51.087 -16.290 -25.016 0.68 37.47 ?  2   MET   B CE   1 
ATOM   3802 C CE   B MET   B 1 2   ? 51.542 -15.861 -24.793 0.32 29.94 ?  2   MET   B CE   1 
ATOM   3803 H H    A MET   B 1 2   ? 51.466 -12.569 -21.764 0.68 31.78 ?  2   MET   B H    1 
ATOM   3804 H H    B MET   B 1 2   ? 51.367 -12.517 -21.601 0.32 30.71 ?  2   MET   B H    1 
ATOM   3805 H HA   A MET   B 1 2   ? 48.988 -13.538 -22.329 0.68 31.76 ?  2   MET   B HA   1 
ATOM   3806 H HA   B MET   B 1 2   ? 48.925 -13.540 -22.234 0.32 30.36 ?  2   MET   B HA   1 
ATOM   3807 H HB2  A MET   B 1 2   ? 50.865 -14.558 -23.360 0.68 36.41 ?  2   MET   B HB2  1 
ATOM   3808 H HB2  B MET   B 1 2   ? 50.995 -14.437 -23.091 0.32 32.42 ?  2   MET   B HB2  1 
ATOM   3809 H HB3  A MET   B 1 2   ? 51.314 -15.084 -21.939 0.68 36.41 ?  2   MET   B HB3  1 
ATOM   3810 H HB3  B MET   B 1 2   ? 51.123 -15.193 -21.714 0.32 32.42 ?  2   MET   B HB3  1 
ATOM   3811 H HG2  A MET   B 1 2   ? 49.540 -16.475 -21.769 0.68 40.78 ?  2   MET   B HG2  1 
ATOM   3812 H HG2  B MET   B 1 2   ? 49.328 -16.484 -22.066 0.32 34.07 ?  2   MET   B HG2  1 
ATOM   3813 H HG3  A MET   B 1 2   ? 48.875 -15.869 -23.086 0.68 40.78 ?  2   MET   B HG3  1 
ATOM   3814 H HG3  B MET   B 1 2   ? 48.862 -15.621 -23.317 0.32 34.07 ?  2   MET   B HG3  1 
ATOM   3815 H HE1  A MET   B 1 2   ? 51.243 -16.846 -25.782 0.68 44.94 ?  2   MET   B HE1  1 
ATOM   3816 H HE1  B MET   B 1 2   ? 51.881 -16.291 -25.563 0.32 35.90 ?  2   MET   B HE1  1 
ATOM   3817 H HE2  A MET   B 1 2   ? 50.383 -15.645 -25.205 0.68 44.94 ?  2   MET   B HE2  1 
ATOM   3818 H HE2  B MET   B 1 2   ? 50.993 -15.095 -25.049 0.32 35.90 ?  2   MET   B HE2  1 
ATOM   3819 H HE3  A MET   B 1 2   ? 51.903 -15.818 -24.769 0.68 44.94 ?  2   MET   B HE3  1 
ATOM   3820 H HE3  B MET   B 1 2   ? 52.279 -15.575 -24.219 0.32 35.90 ?  2   MET   B HE3  1 
ATOM   3821 N N    A VAL   B 1 3   ? 48.354 -13.693 -19.954 0.68 21.72 ?  3   VAL   B N    1 
ATOM   3822 N N    B VAL   B 1 3   ? 48.298 -13.534 -19.827 0.32 21.95 ?  3   VAL   B N    1 
ATOM   3823 C CA   A VAL   B 1 3   ? 47.952 -13.934 -18.576 0.68 20.42 ?  3   VAL   B CA   1 
ATOM   3824 C CA   B VAL   B 1 3   ? 47.873 -13.790 -18.458 0.32 20.37 ?  3   VAL   B CA   1 
ATOM   3825 C C    A VAL   B 1 3   ? 46.711 -14.816 -18.589 0.68 18.76 ?  3   VAL   B C    1 
ATOM   3826 C C    B VAL   B 1 3   ? 46.614 -14.644 -18.484 0.32 18.49 ?  3   VAL   B C    1 
ATOM   3827 O O    A VAL   B 1 3   ? 45.985 -14.897 -19.582 0.68 18.95 ?  3   VAL   B O    1 
ATOM   3828 O O    B VAL   B 1 3   ? 45.779 -14.531 -19.387 0.32 18.22 ?  3   VAL   B O    1 
ATOM   3829 C CB   A VAL   B 1 3   ? 47.681 -12.623 -17.802 0.68 22.06 ?  3   VAL   B CB   1 
ATOM   3830 C CB   B VAL   B 1 3   ? 47.630 -12.495 -17.654 0.32 20.93 ?  3   VAL   B CB   1 
ATOM   3831 C CG1  A VAL   B 1 3   ? 48.951 -11.776 -17.709 0.68 22.37 ?  3   VAL   B CG1  1 
ATOM   3832 C CG1  B VAL   B 1 3   ? 48.905 -11.669 -17.564 0.32 21.08 ?  3   VAL   B CG1  1 
ATOM   3833 C CG2  A VAL   B 1 3   ? 46.550 -11.838 -18.458 0.68 22.57 ?  3   VAL   B CG2  1 
ATOM   3834 C CG2  B VAL   B 1 3   ? 46.496 -11.690 -18.270 0.32 21.00 ?  3   VAL   B CG2  1 
ATOM   3835 H H    A VAL   B 1 3   ? 47.708 -13.437 -20.460 0.68 26.05 ?  3   VAL   B H    1 
ATOM   3836 H H    B VAL   B 1 3   ? 47.702 -13.161 -20.320 0.32 26.32 ?  3   VAL   B H    1 
ATOM   3837 H HA   A VAL   B 1 3   ? 48.655 -14.416 -18.115 0.68 24.49 ?  3   VAL   B HA   1 
ATOM   3838 H HA   B VAL   B 1 3   ? 48.570 -14.292 -18.011 0.32 24.42 ?  3   VAL   B HA   1 
ATOM   3839 H HB   A VAL   B 1 3   ? 47.408 -12.845 -16.897 0.68 26.45 ?  3   VAL   B HB   1 
ATOM   3840 H HB   B VAL   B 1 3   ? 47.368 -12.740 -16.754 0.32 25.10 ?  3   VAL   B HB   1 
ATOM   3841 H HG11 A VAL   B 1 3   ? 48.754 -10.969 -17.210 0.68 26.82 ?  3   VAL   B HG11 1 
ATOM   3842 H HG11 B VAL   B 1 3   ? 48.726 -10.875 -17.038 0.32 25.27 ?  3   VAL   B HG11 1 
ATOM   3843 H HG12 A VAL   B 1 3   ? 49.638 -12.288 -17.255 0.68 26.82 ?  3   VAL   B HG12 1 
ATOM   3844 H HG12 B VAL   B 1 3   ? 49.595 -12.201 -17.138 0.32 25.27 ?  3   VAL   B HG12 1 
ATOM   3845 H HG13 A VAL   B 1 3   ? 49.243 -11.550 -18.605 0.68 26.82 ?  3   VAL   B HG13 1 
ATOM   3846 H HG13 B VAL   B 1 3   ? 49.183 -11.420 -18.459 0.32 25.27 ?  3   VAL   B HG13 1 
ATOM   3847 H HG21 A VAL   B 1 3   ? 46.501 -10.959 -18.054 0.68 27.06 ?  3   VAL   B HG21 1 
ATOM   3848 H HG21 B VAL   B 1 3   ? 46.463 -10.821 -17.844 0.32 25.18 ?  3   VAL   B HG21 1 
ATOM   3849 H HG22 A VAL   B 1 3   ? 46.729 -11.759 -19.407 0.68 27.06 ?  3   VAL   B HG22 1 
ATOM   3850 H HG22 B VAL   B 1 3   ? 46.660 -11.589 -19.220 0.32 25.18 ?  3   VAL   B HG22 1 
ATOM   3851 H HG23 A VAL   B 1 3   ? 45.713 -12.312 -18.318 0.68 27.06 ?  3   VAL   B HG23 1 
ATOM   3852 H HG23 B VAL   B 1 3   ? 45.659 -12.160 -18.127 0.32 25.18 ?  3   VAL   B HG23 1 
ATOM   3853 N N    . ASN   B 1 4   ? 46.476 -15.492 -17.466 1.00 17.19 ?  4   ASN   B N    1 
ATOM   3854 C CA   . ASN   B 1 4   ? 45.338 -16.406 -17.351 1.00 16.02 ?  4   ASN   B CA   1 
ATOM   3855 C C    . ASN   B 1 4   ? 45.281 -17.373 -18.532 1.00 16.63 ?  4   ASN   B C    1 
ATOM   3856 O O    . ASN   B 1 4   ? 44.216 -17.643 -19.086 1.00 17.36 ?  4   ASN   B O    1 
ATOM   3857 C CB   . ASN   B 1 4   ? 44.014 -15.651 -17.190 1.00 15.44 ?  4   ASN   B CB   1 
ATOM   3858 C CG   . ASN   B 1 4   ? 43.971 -14.827 -15.918 1.00 14.83 ?  4   ASN   B CG   1 
ATOM   3859 O OD1  . ASN   B 1 4   ? 44.253 -15.332 -14.832 1.00 14.54 ?  4   ASN   B OD1  1 
ATOM   3860 N ND2  . ASN   B 1 4   ? 43.636 -13.549 -16.049 1.00 15.82 ?  4   ASN   B ND2  1 
ATOM   3861 H H    A ASN   B 1 4   ? 46.971 -15.452 -16.764 0.68 20.61 ?  4   ASN   B H    1 
ATOM   3862 H H    B ASN   B 1 4   ? 47.036 -15.552 -16.816 0.32 20.61 ?  4   ASN   B H    1 
ATOM   3863 H HA   . ASN   B 1 4   ? 45.465 -16.939 -16.551 1.00 19.20 ?  4   ASN   B HA   1 
ATOM   3864 H HB2  . ASN   B 1 4   ? 43.895 -15.051 -17.942 1.00 18.51 ?  4   ASN   B HB2  1 
ATOM   3865 H HB3  . ASN   B 1 4   ? 43.287 -16.293 -17.159 1.00 18.51 ?  4   ASN   B HB3  1 
ATOM   3866 H HD21 . ASN   B 1 4   ? 43.600 -13.040 -15.356 1.00 18.97 ?  4   ASN   B HD21 1 
ATOM   3867 H HD22 . ASN   B 1 4   ? 43.450 -13.228 -16.826 1.00 18.97 ?  4   ASN   B HD22 1 
ATOM   3868 N N    . SER   B 1 5   ? 46.441 -17.899 -18.922 1.00 18.00 ?  5   SER   B N    1 
ATOM   3869 C CA   . SER   B 1 5   ? 46.532 -18.813 -20.060 1.00 20.31 ?  5   SER   B CA   1 
ATOM   3870 C C    . SER   B 1 5   ? 46.521 -20.250 -19.549 1.00 21.69 ?  5   SER   B C    1 
ATOM   3871 O O    . SER   B 1 5   ? 47.527 -20.952 -19.542 1.00 24.03 ?  5   SER   B O    1 
ATOM   3872 C CB   . SER   B 1 5   ? 47.780 -18.517 -20.887 1.00 21.92 ?  5   SER   B CB   1 
ATOM   3873 O OG   . SER   B 1 5   ? 48.957 -18.691 -20.114 1.00 24.50 ?  5   SER   B OG   1 
ATOM   3874 H H    . SER   B 1 5   ? 47.199 -17.744 -18.540 1.00 21.58 ?  5   SER   B H    1 
ATOM   3875 H HA   . SER   B 1 5   ? 45.759 -18.695 -20.628 1.00 24.35 ?  5   SER   B HA   1 
ATOM   3876 H HB2  . SER   B 1 5   ? 47.804 -19.117 -21.652 1.00 26.28 ?  5   SER   B HB2  1 
ATOM   3877 H HB3  . SER   B 1 5   ? 47.729 -17.599 -21.193 1.00 26.28 ?  5   SER   B HB3  1 
ATOM   3878 H HG   . SER   B 1 5   ? 49.018 -19.492 -19.868 1.00 29.37 ?  5   SER   B HG   1 
ATOM   3879 N N    . PHE   B 1 6   ? 45.343 -20.665 -19.100 1.00 21.92 ?  6   PHE   B N    1 
ATOM   3880 C CA   . PHE   B 1 6   ? 45.155 -22.011 -18.582 1.00 21.26 ?  6   PHE   B CA   1 
ATOM   3881 C C    . PHE   B 1 6   ? 45.090 -22.997 -19.739 1.00 25.02 ?  6   PHE   B C    1 
ATOM   3882 O O    . PHE   B 1 6   ? 44.442 -22.736 -20.754 1.00 26.88 ?  6   PHE   B O    1 
ATOM   3883 C CB   . PHE   B 1 6   ? 43.864 -22.073 -17.767 1.00 18.64 ?  6   PHE   B CB   1 
ATOM   3884 C CG   . PHE   B 1 6   ? 43.885 -21.217 -16.533 1.00 16.78 ?  6   PHE   B CG   1 
ATOM   3885 C CD1  . PHE   B 1 6   ? 44.403 -21.704 -15.348 1.00 16.18 ?  6   PHE   B CD1  1 
ATOM   3886 C CD2  . PHE   B 1 6   ? 43.403 -19.916 -16.566 1.00 16.43 ?  6   PHE   B CD2  1 
ATOM   3887 C CE1  . PHE   B 1 6   ? 44.422 -20.918 -14.207 1.00 15.55 ?  6   PHE   B CE1  1 
ATOM   3888 C CE2  . PHE   B 1 6   ? 43.428 -19.119 -15.435 1.00 16.80 ?  6   PHE   B CE2  1 
ATOM   3889 C CZ   . PHE   B 1 6   ? 43.943 -19.613 -14.257 1.00 16.08 ?  6   PHE   B CZ   1 
ATOM   3890 H H    . PHE   B 1 6   ? 44.629 -20.190 -19.100 1.00 26.28 ?  6   PHE   B H    1 
ATOM   3891 H HA   . PHE   B 1 6   ? 45.895 -22.253 -18.008 1.00 25.49 ?  6   PHE   B HA   1 
ATOM   3892 H HB2  . PHE   B 1 6   ? 43.125 -21.773 -18.320 1.00 22.35 ?  6   PHE   B HB2  1 
ATOM   3893 H HB3  . PHE   B 1 6   ? 43.710 -22.989 -17.483 1.00 22.35 ?  6   PHE   B HB3  1 
ATOM   3894 H HD1  . PHE   B 1 6   ? 44.735 -22.572 -15.310 1.00 19.39 ?  6   PHE   B HD1  1 
ATOM   3895 H HD2  . PHE   B 1 6   ? 43.055 -19.579 -17.359 1.00 19.70 ?  6   PHE   B HD2  1 
ATOM   3896 H HE1  . PHE   B 1 6   ? 44.780 -21.250 -13.413 1.00 18.63 ?  6   PHE   B HE1  1 
ATOM   3897 H HE2  . PHE   B 1 6   ? 43.096 -18.250 -15.470 1.00 20.13 ?  6   PHE   B HE2  1 
ATOM   3898 H HZ   . PHE   B 1 6   ? 43.958 -19.084 -13.492 1.00 19.27 ?  6   PHE   B HZ   1 
ATOM   3899 N N    . SER   B 1 7   ? 45.790 -24.123 -19.591 1.00 26.13 ?  7   SER   B N    1 
ATOM   3900 C CA   . SER   B 1 7   ? 45.893 -25.113 -20.652 1.00 29.34 ?  7   SER   B CA   1 
ATOM   3901 C C    . SER   B 1 7   ? 45.824 -26.514 -20.064 1.00 28.24 ?  7   SER   B C    1 
ATOM   3902 O O    . SER   B 1 7   ? 46.401 -26.785 -19.007 1.00 29.04 ?  7   SER   B O    1 
ATOM   3903 C CB   . SER   B 1 7   ? 47.204 -24.947 -21.433 1.00 32.68 ?  7   SER   B CB   1 
ATOM   3904 O OG   . SER   B 1 7   ? 47.271 -25.858 -22.516 1.00 34.63 ?  7   SER   B OG   1 
ATOM   3905 H H    . SER   B 1 7   ? 46.228 -24.334 -18.877 1.00 31.34 ?  7   SER   B H    1 
ATOM   3906 H HA   . SER   B 1 7   ? 45.155 -25.009 -21.269 1.00 35.18 ?  7   SER   B HA   1 
ATOM   3907 H HB2  . SER   B 1 7   ? 47.249 -24.042 -21.782 1.00 39.19 ?  7   SER   B HB2  1 
ATOM   3908 H HB3  . SER   B 1 7   ? 47.952 -25.107 -20.835 1.00 39.19 ?  7   SER   B HB3  1 
ATOM   3909 H HG   . SER   B 1 7   ? 47.995 -25.758 -22.932 1.00 41.53 ?  7   SER   B HG   1 
ATOM   3910 N N    . GLY   B 1 8   ? 45.114 -27.401 -20.758 1.00 27.85 ?  8   GLY   B N    1 
ATOM   3911 C CA   . GLY   B 1 8   ? 45.074 -28.797 -20.379 1.00 26.86 ?  8   GLY   B CA   1 
ATOM   3912 C C    . GLY   B 1 8   ? 44.114 -29.133 -19.266 1.00 25.01 ?  8   GLY   B C    1 
ATOM   3913 O O    . GLY   B 1 8   ? 44.241 -30.206 -18.660 1.00 26.56 ?  8   GLY   B O    1 
ATOM   3914 H H    . GLY   B 1 8   ? 44.650 -27.209 -21.453 1.00 33.40 ?  8   GLY   B H    1 
ATOM   3915 H HA2  . GLY   B 1 8   ? 44.819 -29.323 -21.151 1.00 32.21 ?  8   GLY   B HA2  1 
ATOM   3916 H HA3  . GLY   B 1 8   ? 45.958 -29.076 -20.102 1.00 32.21 ?  8   GLY   B HA3  1 
ATOM   3917 N N    . TYR   B 1 9   ? 43.134 -28.275 -18.993 1.00 22.68 ?  9   TYR   B N    1 
ATOM   3918 C CA   . TYR   B 1 9   ? 42.179 -28.544 -17.930 1.00 20.37 ?  9   TYR   B CA   1 
ATOM   3919 C C    . TYR   B 1 9   ? 40.990 -29.331 -18.447 1.00 19.88 ?  9   TYR   B C    1 
ATOM   3920 O O    . TYR   B 1 9   ? 40.567 -29.184 -19.598 1.00 21.85 ?  9   TYR   B O    1 
ATOM   3921 C CB   . TYR   B 1 9   ? 41.675 -27.256 -17.288 1.00 19.60 ?  9   TYR   B CB   1 
ATOM   3922 C CG   . TYR   B 1 9   ? 42.693 -26.641 -16.365 1.00 18.67 ?  9   TYR   B CG   1 
ATOM   3923 C CD1  . TYR   B 1 9   ? 43.802 -25.981 -16.875 1.00 19.58 ?  9   TYR   B CD1  1 
ATOM   3924 C CD2  . TYR   B 1 9   ? 42.563 -26.732 -14.990 1.00 17.63 ?  9   TYR   B CD2  1 
ATOM   3925 C CE1  . TYR   B 1 9   ? 44.751 -25.430 -16.042 1.00 19.65 ?  9   TYR   B CE1  1 
ATOM   3926 C CE2  . TYR   B 1 9   ? 43.506 -26.180 -14.145 1.00 18.29 ?  9   TYR   B CE2  1 
ATOM   3927 C CZ   . TYR   B 1 9   ? 44.601 -25.525 -14.680 1.00 19.39 ?  9   TYR   B CZ   1 
ATOM   3928 O OH   . TYR   B 1 9   ? 45.551 -24.973 -13.854 1.00 20.08 ?  9   TYR   B OH   1 
ATOM   3929 H H    . TYR   B 1 9   ? 42.983 -27.546 -19.424 1.00 27.19 ?  9   TYR   B H    1 
ATOM   3930 H HA   . TYR   B 1 9   ? 42.606 -29.071 -17.243 1.00 24.42 ?  9   TYR   B HA   1 
ATOM   3931 H HB2  . TYR   B 1 9   ? 41.459 -26.608 -17.979 1.00 23.49 ?  9   TYR   B HB2  1 
ATOM   3932 H HB3  . TYR   B 1 9   ? 40.888 -27.460 -16.764 1.00 23.49 ?  9   TYR   B HB3  1 
ATOM   3933 H HD1  . TYR   B 1 9   ? 43.910 -25.915 -17.797 1.00 23.47 ?  9   TYR   B HD1  1 
ATOM   3934 H HD2  . TYR   B 1 9   ? 41.825 -27.172 -14.627 1.00 21.13 ?  9   TYR   B HD2  1 
ATOM   3935 H HE1  . TYR   B 1 9   ? 45.485 -24.990 -16.400 1.00 23.56 ?  9   TYR   B HE1  1 
ATOM   3936 H HE2  . TYR   B 1 9   ? 43.400 -26.247 -13.221 1.00 21.92 ?  9   TYR   B HE2  1 
ATOM   3937 H HH   . TYR   B 1 9   ? 46.147 -24.609 -14.313 1.00 24.07 ?  9   TYR   B HH   1 
ATOM   3938 N N    . LEU   B 1 10  ? 40.450 -30.166 -17.570 1.00 18.20 ?  10  LEU   B N    1 
ATOM   3939 C CA   . LEU   B 1 10  ? 39.248 -30.933 -17.840 1.00 17.97 ?  10  LEU   B CA   1 
ATOM   3940 C C    . LEU   B 1 10  ? 38.059 -30.165 -17.280 1.00 17.40 ?  10  LEU   B C    1 
ATOM   3941 O O    . LEU   B 1 10  ? 38.075 -29.746 -16.118 1.00 17.22 ?  10  LEU   B O    1 
ATOM   3942 C CB   . LEU   B 1 10  ? 39.357 -32.304 -17.176 1.00 18.96 ?  10  LEU   B CB   1 
ATOM   3943 C CG   . LEU   B 1 10  ? 38.204 -33.252 -17.485 1.00 20.48 ?  10  LEU   B CG   1 
ATOM   3944 C CD1  . LEU   B 1 10  ? 38.305 -33.758 -18.917 1.00 21.86 ?  10  LEU   B CD1  1 
ATOM   3945 C CD2  . LEU   B 1 10  ? 38.173 -34.399 -16.496 1.00 21.58 ?  10  LEU   B CD2  1 
ATOM   3946 H H    . LEU   B 1 10  ? 40.766 -30.304 -16.773 1.00 21.82 ?  10  LEU   B H    1 
ATOM   3947 H HA   . LEU   B 1 10  ? 39.132 -31.050 -18.792 1.00 21.54 ?  10  LEU   B HA   1 
ATOM   3948 H HB2  . LEU   B 1 10  ? 40.178 -32.729 -17.478 1.00 22.72 ?  10  LEU   B HB2  1 
ATOM   3949 H HB3  . LEU   B 1 10  ? 39.391 -32.183 -16.213 1.00 22.72 ?  10  LEU   B HB3  1 
ATOM   3950 H HG   . LEU   B 1 10  ? 37.369 -32.767 -17.401 1.00 24.55 ?  10  LEU   B HG   1 
ATOM   3951 H HD11 . LEU   B 1 10  ? 37.596 -34.400 -19.072 1.00 26.20 ?  10  LEU   B HD11 1 
ATOM   3952 H HD12 . LEU   B 1 10  ? 38.209 -33.006 -19.524 1.00 26.20 ?  10  LEU   B HD12 1 
ATOM   3953 H HD13 . LEU   B 1 10  ? 39.168 -34.178 -19.042 1.00 26.20 ?  10  LEU   B HD13 1 
ATOM   3954 H HD21 . LEU   B 1 10  ? 37.434 -34.984 -16.721 1.00 25.88 ?  10  LEU   B HD21 1 
ATOM   3955 H HD22 . LEU   B 1 10  ? 39.010 -34.880 -16.548 1.00 25.88 ?  10  LEU   B HD22 1 
ATOM   3956 H HD23 . LEU   B 1 10  ? 38.051 -34.037 -15.604 1.00 25.88 ?  10  LEU   B HD23 1 
ATOM   3957 N N    . LYS   B 1 11  ? 37.042 -29.974 -18.108 1.00 18.25 ?  11  LYS   B N    1 
ATOM   3958 C CA   . LYS   B 1 11  ? 35.842 -29.262 -17.697 1.00 20.17 ?  11  LYS   B CA   1 
ATOM   3959 C C    . LYS   B 1 11  ? 34.961 -30.190 -16.866 1.00 19.60 ?  11  LYS   B C    1 
ATOM   3960 O O    . LYS   B 1 11  ? 34.576 -31.269 -17.329 1.00 21.53 ?  11  LYS   B O    1 
ATOM   3961 C CB   . LYS   B 1 11  ? 35.100 -28.785 -18.945 1.00 24.12 ?  11  LYS   B CB   1 
ATOM   3962 C CG   . LYS   B 1 11  ? 33.947 -27.835 -18.688 1.00 27.61 ?  11  LYS   B CG   1 
ATOM   3963 C CD   . LYS   B 1 11  ? 33.195 -27.552 -19.984 1.00 30.57 ?  11  LYS   B CD   1 
ATOM   3964 C CE   . LYS   B 1 11  ? 32.172 -26.442 -19.816 1.00 32.72 ?  11  LYS   B CE   1 
ATOM   3965 N NZ   . LYS   B 1 11  ? 32.822 -25.115 -19.651 1.00 33.93 ?  11  LYS   B NZ   1 
ATOM   3966 H H    . LYS   B 1 11  ? 37.019 -30.257 -18.921 1.00 21.87 ?  11  LYS   B H    1 
ATOM   3967 H HA   . LYS   B 1 11  ? 36.084 -28.494 -17.160 1.00 24.18 ?  11  LYS   B HA   1 
ATOM   3968 H HB2  . LYS   B 1 11  ? 35.733 -28.324 -19.521 1.00 28.92 ?  11  LYS   B HB2  1 
ATOM   3969 H HB3  . LYS   B 1 11  ? 34.745 -29.557 -19.409 1.00 28.92 ?  11  LYS   B HB3  1 
ATOM   3970 H HG2  . LYS   B 1 11  ? 33.329 -28.236 -18.058 1.00 33.11 ?  11  LYS   B HG2  1 
ATOM   3971 H HG3  . LYS   B 1 11  ? 34.287 -26.995 -18.344 1.00 33.11 ?  11  LYS   B HG3  1 
ATOM   3972 H HD2  . LYS   B 1 11  ? 33.828 -27.280 -20.668 1.00 36.66 ?  11  LYS   B HD2  1 
ATOM   3973 H HD3  . LYS   B 1 11  ? 32.727 -28.356 -20.263 1.00 36.66 ?  11  LYS   B HD3  1 
ATOM   3974 H HE2  . LYS   B 1 11  ? 31.606 -26.408 -20.603 1.00 39.25 ?  11  LYS   B HE2  1 
ATOM   3975 H HE3  . LYS   B 1 11  ? 31.638 -26.623 -19.027 1.00 39.25 ?  11  LYS   B HE3  1 
ATOM   3976 H HZ1  . LYS   B 1 11  ? 32.202 -24.482 -19.563 1.00 40.70 ?  11  LYS   B HZ1  1 
ATOM   3977 H HZ2  . LYS   B 1 11  ? 33.339 -25.117 -18.928 1.00 40.70 ?  11  LYS   B HZ2  1 
ATOM   3978 H HZ3  . LYS   B 1 11  ? 33.323 -24.932 -20.365 1.00 40.70 ?  11  LYS   B HZ3  1 
ATOM   3979 N N    . LEU   B 1 12  ? 34.638 -29.775 -15.642 1.00 18.00 ?  12  LEU   B N    1 
ATOM   3980 C CA   . LEU   B 1 12  ? 33.673 -30.477 -14.802 1.00 17.58 ?  12  LEU   B CA   1 
ATOM   3981 C C    . LEU   B 1 12  ? 32.284 -29.864 -14.891 1.00 17.56 ?  12  LEU   B C    1 
ATOM   3982 O O    . LEU   B 1 12  ? 31.298 -30.583 -15.061 1.00 18.42 ?  12  LEU   B O    1 
ATOM   3983 C CB   . LEU   B 1 12  ? 34.133 -30.493 -13.341 1.00 16.77 ?  12  LEU   B CB   1 
ATOM   3984 C CG   . LEU   B 1 12  ? 35.469 -31.175 -13.059 1.00 16.74 ?  12  LEU   B CG   1 
ATOM   3985 C CD1  . LEU   B 1 12  ? 35.794 -31.105 -11.582 1.00 17.00 ?  12  LEU   B CD1  1 
ATOM   3986 C CD2  . LEU   B 1 12  ? 35.455 -32.618 -13.542 1.00 17.61 ?  12  LEU   B CD2  1 
ATOM   3987 H H    . LEU   B 1 12  ? 34.973 -29.077 -15.271 1.00 21.58 ?  12  LEU   B H    1 
ATOM   3988 H HA   . LEU   B 1 12  ? 33.599 -31.393 -15.106 1.00 21.07 ?  12  LEU   B HA   1 
ATOM   3989 H HB2  . LEU   B 1 12  ? 34.206 -29.576 -13.037 1.00 20.10 ?  12  LEU   B HB2  1 
ATOM   3990 H HB3  . LEU   B 1 12  ? 33.457 -30.952 -12.817 1.00 20.10 ?  12  LEU   B HB3  1 
ATOM   3991 H HG   . LEU   B 1 12  ? 36.166 -30.705 -13.540 1.00 20.06 ?  12  LEU   B HG   1 
ATOM   3992 H HD11 . LEU   B 1 12  ? 36.647 -31.542 -11.425 1.00 20.38 ?  12  LEU   B HD11 1 
ATOM   3993 H HD12 . LEU   B 1 12  ? 35.846 -30.176 -11.310 1.00 20.38 ?  12  LEU   B HD12 1 
ATOM   3994 H HD13 . LEU   B 1 12  ? 35.096 -31.558 -11.080 1.00 20.38 ?  12  LEU   B HD13 1 
ATOM   3995 H HD21 . LEU   B 1 12  ? 36.259 -33.060 -13.229 1.00 21.11 ?  12  LEU   B HD21 1 
ATOM   3996 H HD22 . LEU   B 1 12  ? 34.671 -33.061 -13.185 1.00 21.11 ?  12  LEU   B HD22 1 
ATOM   3997 H HD23 . LEU   B 1 12  ? 35.428 -32.625 -14.511 1.00 21.11 ?  12  LEU   B HD23 1 
ATOM   3998 N N    . THR   B 1 13  ? 32.196 -28.544 -14.768 1.00 17.50 ?  13  THR   B N    1 
ATOM   3999 C CA   . THR   B 1 13  ? 30.971 -27.792 -14.979 1.00 17.42 ?  13  THR   B CA   1 
ATOM   4000 C C    . THR   B 1 13  ? 31.305 -26.593 -15.861 1.00 19.57 ?  13  THR   B C    1 
ATOM   4001 O O    . THR   B 1 13  ? 32.452 -26.399 -16.280 1.00 20.78 ?  13  THR   B O    1 
ATOM   4002 C CB   . THR   B 1 13  ? 30.370 -27.311 -13.654 1.00 17.34 ?  13  THR   B CB   1 
ATOM   4003 O OG1  . THR   B 1 13  ? 31.213 -26.284 -13.111 1.00 17.06 ?  13  THR   B OG1  1 
ATOM   4004 C CG2  . THR   B 1 13  ? 30.256 -28.457 -12.654 1.00 17.79 ?  13  THR   B CG2  1 
ATOM   4005 H H    . THR   B 1 13  ? 32.862 -28.041 -14.549 1.00 20.98 ?  13  THR   B H    1 
ATOM   4006 H HA   . THR   B 1 13  ? 30.318 -28.347 -15.431 1.00 20.88 ?  13  THR   B HA   1 
ATOM   4007 H HB   . THR   B 1 13  ? 29.477 -26.952 -13.813 1.00 20.78 ?  13  THR   B HB   1 
ATOM   4008 H HG1  . THR   B 1 13  ? 30.885 -25.524 -13.285 1.00 20.45 ?  13  THR   B HG1  1 
ATOM   4009 H HG21 . THR   B 1 13  ? 29.727 -28.181 -11.890 1.00 21.32 ?  13  THR   B HG21 1 
ATOM   4010 H HG22 . THR   B 1 13  ? 29.827 -29.221 -13.073 1.00 21.32 ?  13  THR   B HG22 1 
ATOM   4011 H HG23 . THR   B 1 13  ? 31.138 -28.720 -12.350 1.00 21.32 ?  13  THR   B HG23 1 
ATOM   4012 N N    A ASP   B 1 14  ? 30.291 -25.770 -16.129 0.68 20.80 ?  14  ASP   B N    1 
ATOM   4013 N N    B ASP   B 1 14  ? 30.294 -25.761 -16.124 0.32 20.50 ?  14  ASP   B N    1 
ATOM   4014 C CA   A ASP   B 1 14  ? 30.506 -24.606 -16.981 0.68 22.09 ?  14  ASP   B CA   1 
ATOM   4015 C CA   B ASP   B 1 14  ? 30.499 -24.601 -16.985 0.32 21.37 ?  14  ASP   B CA   1 
ATOM   4016 C C    A ASP   B 1 14  ? 31.607 -23.701 -16.442 0.68 20.24 ?  14  ASP   B C    1 
ATOM   4017 C C    B ASP   B 1 14  ? 31.522 -23.623 -16.424 0.32 19.66 ?  14  ASP   B C    1 
ATOM   4018 O O    A ASP   B 1 14  ? 32.278 -23.016 -17.223 0.68 21.68 ?  14  ASP   B O    1 
ATOM   4019 O O    B ASP   B 1 14  ? 32.030 -22.784 -17.177 0.32 20.19 ?  14  ASP   B O    1 
ATOM   4020 C CB   A ASP   B 1 14  ? 29.202 -23.826 -17.146 0.68 25.54 ?  14  ASP   B CB   1 
ATOM   4021 C CB   B ASP   B 1 14  ? 29.181 -23.863 -17.216 0.32 24.01 ?  14  ASP   B CB   1 
ATOM   4022 C CG   A ASP   B 1 14  ? 28.240 -24.487 -18.111 0.68 29.17 ?  14  ASP   B CG   1 
ATOM   4023 C CG   B ASP   B 1 14  ? 28.298 -24.554 -18.237 0.32 26.49 ?  14  ASP   B CG   1 
ATOM   4024 O OD1  A ASP   B 1 14  ? 28.625 -25.469 -18.787 0.68 30.38 ?  14  ASP   B OD1  1 
ATOM   4025 O OD1  B ASP   B 1 14  ? 28.843 -25.226 -19.139 0.32 27.32 ?  14  ASP   B OD1  1 
ATOM   4026 O OD2  A ASP   B 1 14  ? 27.084 -24.022 -18.187 0.68 30.65 -1 14  ASP   B OD2  1 
ATOM   4027 O OD2  B ASP   B 1 14  ? 27.059 -24.431 -18.138 0.32 27.44 -1 14  ASP   B OD2  1 
ATOM   4028 H H    A ASP   B 1 14  ? 29.491 -25.851 -15.823 0.68 24.94 ?  14  ASP   B H    1 
ATOM   4029 H H    B ASP   B 1 14  ? 29.494 -25.841 -15.817 0.32 24.58 ?  14  ASP   B H    1 
ATOM   4030 H HA   A ASP   B 1 14  ? 30.785 -24.904 -17.856 0.68 26.49 ?  14  ASP   B HA   1 
ATOM   4031 H HA   B ASP   B 1 14  ? 30.823 -24.906 -17.845 0.32 25.62 ?  14  ASP   B HA   1 
ATOM   4032 H HB2  A ASP   B 1 14  ? 28.749 -23.767 -16.292 0.68 30.62 ?  14  ASP   B HB2  1 
ATOM   4033 H HB2  B ASP   B 1 14  ? 28.693 -23.818 -16.379 0.32 28.79 ?  14  ASP   B HB2  1 
ATOM   4034 H HB3  A ASP   B 1 14  ? 29.398 -22.937 -17.482 0.68 30.62 ?  14  ASP   B HB3  1 
ATOM   4035 H HB3  B ASP   B 1 14  ? 29.377 -22.963 -17.532 0.32 28.79 ?  14  ASP   B HB3  1 
ATOM   4036 N N    . ASN   B 1 15  ? 31.818 -23.687 -15.124 1.00 17.66 ?  15  ASN   B N    1 
ATOM   4037 C CA   . ASN   B 1 15  ? 32.778 -22.768 -14.518 1.00 15.37 ?  15  ASN   B CA   1 
ATOM   4038 C C    . ASN   B 1 15  ? 33.873 -23.423 -13.684 1.00 14.31 ?  15  ASN   B C    1 
ATOM   4039 O O    . ASN   B 1 15  ? 34.729 -22.700 -13.163 1.00 15.04 ?  15  ASN   B O    1 
ATOM   4040 C CB   . ASN   B 1 15  ? 32.064 -21.715 -13.657 1.00 15.56 ?  15  ASN   B CB   1 
ATOM   4041 C CG   . ASN   B 1 15  ? 31.438 -22.315 -12.422 1.00 14.98 ?  15  ASN   B CG   1 
ATOM   4042 O OD1  . ASN   B 1 15  ? 30.492 -23.111 -12.513 1.00 17.04 ?  15  ASN   B OD1  1 
ATOM   4043 N ND2  . ASN   B 1 15  ? 31.960 -21.966 -11.263 1.00 14.26 ?  15  ASN   B ND2  1 
ATOM   4044 H H    A ASN   B 1 15  ? 31.414 -24.199 -14.561 0.68 21.17 ?  15  ASN   B H    1 
ATOM   4045 H H    B ASN   B 1 15  ? 31.452 -24.233 -14.569 0.32 21.17 ?  15  ASN   B H    1 
ATOM   4046 H HA   . ASN   B 1 15  ? 33.223 -22.282 -15.224 1.00 18.42 ?  15  ASN   B HA   1 
ATOM   4047 H HB2  . ASN   B 1 15  ? 32.713 -21.039 -13.377 1.00 18.65 ?  15  ASN   B HB2  1 
ATOM   4048 H HB3  . ASN   B 1 15  ? 31.363 -21.287 -14.180 1.00 18.65 ?  15  ASN   B HB3  1 
ATOM   4049 H HD21 . ASN   B 1 15  ? 31.632 -22.277 -10.531 1.00 17.09 ?  15  ASN   B HD21 1 
ATOM   4050 H HD22 . ASN   B 1 15  ? 32.627 -21.416 -11.228 1.00 17.09 ?  15  ASN   B HD22 1 
ATOM   4051 N N    . VAL   B 1 16  ? 33.878 -24.746 -13.533 1.00 13.97 ?  16  VAL   B N    1 
ATOM   4052 C CA   . VAL   B 1 16  ? 34.877 -25.442 -12.728 1.00 13.71 ?  16  VAL   B CA   1 
ATOM   4053 C C    . VAL   B 1 16  ? 35.673 -26.377 -13.626 1.00 13.96 ?  16  VAL   B C    1 
ATOM   4054 O O    . VAL   B 1 16  ? 35.098 -27.248 -14.298 1.00 15.21 ?  16  VAL   B O    1 
ATOM   4055 C CB   . VAL   B 1 16  ? 34.250 -26.205 -11.546 1.00 14.14 ?  16  VAL   B CB   1 
ATOM   4056 C CG1  . VAL   B 1 16  ? 35.334 -26.938 -10.748 1.00 14.31 ?  16  VAL   B CG1  1 
ATOM   4057 C CG2  . VAL   B 1 16  ? 33.450 -25.254 -10.657 1.00 14.91 ?  16  VAL   B CG2  1 
ATOM   4058 H H    . VAL   B 1 16  ? 33.290 -25.272 -13.885 1.00 16.74 ?  16  VAL   B H    1 
ATOM   4059 H HA   . VAL   B 1 16  ? 35.490 -24.785 -12.359 1.00 16.43 ?  16  VAL   B HA   1 
ATOM   4060 H HB   . VAL   B 1 16  ? 33.637 -26.871 -11.895 1.00 16.95 ?  16  VAL   B HB   1 
ATOM   4061 H HG11 . VAL   B 1 16  ? 34.951 -27.247 -9.911  1.00 17.14 ?  16  VAL   B HG11 1 
ATOM   4062 H HG12 . VAL   B 1 16  ? 35.654 -27.692 -11.263 1.00 17.14 ?  16  VAL   B HG12 1 
ATOM   4063 H HG13 . VAL   B 1 16  ? 36.062 -26.321 -10.568 1.00 17.14 ?  16  VAL   B HG13 1 
ATOM   4064 H HG21 . VAL   B 1 16  ? 33.119 -25.744 -9.887  1.00 17.87 ?  16  VAL   B HG21 1 
ATOM   4065 H HG22 . VAL   B 1 16  ? 34.025 -24.531 -10.367 1.00 17.87 ?  16  VAL   B HG22 1 
ATOM   4066 H HG23 . VAL   B 1 16  ? 32.703 -24.898 -11.166 1.00 17.87 ?  16  VAL   B HG23 1 
ATOM   4067 N N    . TYR   B 1 17  ? 36.997 -26.213 -13.600 1.00 14.33 ?  17  TYR   B N    1 
ATOM   4068 C CA   . TYR   B 1 17  ? 37.941 -26.964 -14.412 1.00 14.90 ?  17  TYR   B CA   1 
ATOM   4069 C C    . TYR   B 1 17  ? 38.991 -27.580 -13.497 1.00 13.97 ?  17  TYR   B C    1 
ATOM   4070 O O    . TYR   B 1 17  ? 39.269 -27.053 -12.417 1.00 14.49 ?  17  TYR   B O    1 
ATOM   4071 C CB   . TYR   B 1 17  ? 38.654 -26.033 -15.400 1.00 17.38 ?  17  TYR   B CB   1 
ATOM   4072 C CG   . TYR   B 1 17  ? 37.734 -25.256 -16.304 1.00 20.57 ?  17  TYR   B CG   1 
ATOM   4073 C CD1  . TYR   B 1 17  ? 37.184 -24.046 -15.902 1.00 21.98 ?  17  TYR   B CD1  1 
ATOM   4074 C CD2  . TYR   B 1 17  ? 37.422 -25.728 -17.570 1.00 22.61 ?  17  TYR   B CD2  1 
ATOM   4075 C CE1  . TYR   B 1 17  ? 36.340 -23.329 -16.736 1.00 23.82 ?  17  TYR   B CE1  1 
ATOM   4076 C CE2  . TYR   B 1 17  ? 36.583 -25.021 -18.411 1.00 24.35 ?  17  TYR   B CE2  1 
ATOM   4077 C CZ   . TYR   B 1 17  ? 36.046 -23.823 -17.989 1.00 25.02 ?  17  TYR   B CZ   1 
ATOM   4078 O OH   . TYR   B 1 17  ? 35.212 -23.117 -18.823 1.00 26.39 ?  17  TYR   B OH   1 
ATOM   4079 H H    . TYR   B 1 17  ? 37.391 -25.635 -13.090 1.00 17.17 ?  17  TYR   B H    1 
ATOM   4080 H HA   . TYR   B 1 17  ? 37.477 -27.666 -14.901 1.00 17.86 ?  17  TYR   B HA   1 
ATOM   4081 H HB2  . TYR   B 1 17  ? 39.186 -25.398 -14.901 1.00 20.83 ?  17  TYR   B HB2  1 
ATOM   4082 H HB3  . TYR   B 1 17  ? 39.221 -26.570 -15.966 1.00 20.83 ?  17  TYR   B HB3  1 
ATOM   4083 H HD1  . TYR   B 1 17  ? 37.381 -23.710 -15.059 1.00 26.35 ?  17  TYR   B HD1  1 
ATOM   4084 H HD2  . TYR   B 1 17  ? 37.775 -26.535 -17.860 1.00 27.11 ?  17  TYR   B HD2  1 
ATOM   4085 H HE1  . TYR   B 1 17  ? 35.976 -22.518 -16.455 1.00 28.57 ?  17  TYR   B HE1  1 
ATOM   4086 H HE2  . TYR   B 1 17  ? 36.375 -25.352 -19.258 1.00 29.20 ?  17  TYR   B HE2  1 
ATOM   4087 H HH   . TYR   B 1 17  ? 35.110 -23.524 -19.551 1.00 31.65 ?  17  TYR   B HH   1 
ATOM   4088 N N    . ILE   B 1 18  ? 39.603 -28.685 -13.931 1.00 13.73 ?  18  ILE   B N    1 
ATOM   4089 C CA   . ILE   B 1 18  ? 40.534 -29.408 -13.070 1.00 13.58 ?  18  ILE   B CA   1 
ATOM   4090 C C    . ILE   B 1 18  ? 41.697 -29.961 -13.885 1.00 14.30 ?  18  ILE   B C    1 
ATOM   4091 O O    . ILE   B 1 18  ? 41.539 -30.355 -15.045 1.00 15.64 ?  18  ILE   B O    1 
ATOM   4092 C CB   . ILE   B 1 18  ? 39.781 -30.510 -12.277 1.00 14.33 ?  18  ILE   B CB   1 
ATOM   4093 C CG1  . ILE   B 1 18  ? 40.634 -31.060 -11.131 1.00 14.81 ?  18  ILE   B CG1  1 
ATOM   4094 C CG2  . ILE   B 1 18  ? 39.278 -31.626 -13.204 1.00 14.79 ?  18  ILE   B CG2  1 
ATOM   4095 C CD1  . ILE   B 1 18  ? 39.830 -31.877 -10.126 1.00 15.84 ?  18  ILE   B CD1  1 
ATOM   4096 H H    . ILE   B 1 18  ? 39.497 -29.031 -14.710 1.00 16.46 ?  18  ILE   B H    1 
ATOM   4097 H HA   . ILE   B 1 18  ? 40.896 -28.788 -12.418 1.00 16.28 ?  18  ILE   B HA   1 
ATOM   4098 H HB   . ILE   B 1 18  ? 38.998 -30.102 -11.874 1.00 17.18 ?  18  ILE   B HB   1 
ATOM   4099 H HG12 . ILE   B 1 18  ? 41.327 -31.626 -11.494 1.00 17.75 ?  18  ILE   B HG12 1 
ATOM   4100 H HG13 . ILE   B 1 18  ? 41.032 -30.311 -10.652 1.00 17.75 ?  18  ILE   B HG13 1 
ATOM   4101 H HG21 . ILE   B 1 18  ? 38.692 -32.215 -12.701 1.00 17.72 ?  18  ILE   B HG21 1 
ATOM   4102 H HG22 . ILE   B 1 18  ? 38.790 -31.223 -13.938 1.00 17.72 ?  18  ILE   B HG22 1 
ATOM   4103 H HG23 . ILE   B 1 18  ? 40.037 -32.123 -13.542 1.00 17.72 ?  18  ILE   B HG23 1 
ATOM   4104 H HD11 . ILE   B 1 18  ? 40.413 -32.150 -9.400  1.00 18.99 ?  18  ILE   B HD11 1 
ATOM   4105 H HD12 . ILE   B 1 18  ? 39.104 -31.333 -9.780  1.00 18.99 ?  18  ILE   B HD12 1 
ATOM   4106 H HD13 . ILE   B 1 18  ? 39.471 -32.661 -10.572 1.00 18.99 ?  18  ILE   B HD13 1 
ATOM   4107 N N    . LYS   B 1 19  ? 42.873 -30.004 -13.257 1.00 14.76 ?  19  LYS   B N    1 
ATOM   4108 C CA   . LYS   B 1 19  ? 44.085 -30.475 -13.911 1.00 15.13 ?  19  LYS   B CA   1 
ATOM   4109 C C    . LYS   B 1 19  ? 44.981 -31.153 -12.885 1.00 14.97 ?  19  LYS   B C    1 
ATOM   4110 O O    . LYS   B 1 19  ? 45.067 -30.714 -11.738 1.00 14.50 ?  19  LYS   B O    1 
ATOM   4111 C CB   . LYS   B 1 19  ? 44.850 -29.305 -14.551 1.00 16.99 ?  19  LYS   B CB   1 
ATOM   4112 C CG   . LYS   B 1 19  ? 46.047 -29.721 -15.394 1.00 18.80 ?  19  LYS   B CG   1 
ATOM   4113 C CD   . LYS   B 1 19  ? 46.826 -28.503 -15.878 1.00 20.84 ?  19  LYS   B CD   1 
ATOM   4114 C CE   . LYS   B 1 19  ? 47.946 -28.886 -16.826 1.00 22.98 ?  19  LYS   B CE   1 
ATOM   4115 N NZ   . LYS   B 1 19  ? 48.741 -27.706 -17.260 1.00 24.07 ?  19  LYS   B NZ   1 
ATOM   4116 H H    . LYS   B 1 19  ? 42.986 -29.753 -12.439 1.00 17.68 ?  19  LYS   B H    1 
ATOM   4117 H HA   . LYS   B 1 19  ? 43.850 -31.113 -14.600 1.00 18.14 ?  19  LYS   B HA   1 
ATOM   4118 H HB2  . LYS   B 1 19  ? 44.240 -28.818 -15.128 1.00 20.37 ?  19  LYS   B HB2  1 
ATOM   4119 H HB3  . LYS   B 1 19  ? 45.168 -28.718 -13.845 1.00 20.37 ?  19  LYS   B HB3  1 
ATOM   4120 H HG2  . LYS   B 1 19  ? 46.636 -30.274 -14.860 1.00 22.54 ?  19  LYS   B HG2  1 
ATOM   4121 H HG3  . LYS   B 1 19  ? 45.730 -30.214 -16.169 1.00 22.54 ?  19  LYS   B HG3  1 
ATOM   4122 H HD2  . LYS   B 1 19  ? 46.221 -27.903 -16.344 1.00 24.98 ?  19  LYS   B HD2  1 
ATOM   4123 H HD3  . LYS   B 1 19  ? 47.216 -28.052 -15.111 1.00 24.98 ?  19  LYS   B HD3  1 
ATOM   4124 H HE2  . LYS   B 1 19  ? 48.540 -29.508 -16.378 1.00 27.55 ?  19  LYS   B HE2  1 
ATOM   4125 H HE3  . LYS   B 1 19  ? 47.562 -29.303 -17.615 1.00 27.55 ?  19  LYS   B HE3  1 
ATOM   4126 H HZ1  . LYS   B 1 19  ? 49.374 -27.960 -17.833 1.00 28.86 ?  19  LYS   B HZ1  1 
ATOM   4127 H HZ2  . LYS   B 1 19  ? 48.213 -27.111 -17.660 1.00 28.86 ?  19  LYS   B HZ2  1 
ATOM   4128 H HZ3  . LYS   B 1 19  ? 49.127 -27.322 -16.556 1.00 28.86 ?  19  LYS   B HZ3  1 
ATOM   4129 N N    . ASN   B 1 20  ? 45.667 -32.209 -13.315 1.00 16.34 ?  20  ASN   B N    1 
ATOM   4130 C CA   . ASN   B 1 20  ? 46.697 -32.847 -12.498 1.00 17.36 ?  20  ASN   B CA   1 
ATOM   4131 C C    . ASN   B 1 20  ? 47.972 -32.034 -12.684 1.00 18.08 ?  20  ASN   B C    1 
ATOM   4132 O O    . ASN   B 1 20  ? 48.632 -32.126 -13.723 1.00 19.80 ?  20  ASN   B O    1 
ATOM   4133 C CB   . ASN   B 1 20  ? 46.870 -34.300 -12.934 1.00 19.06 ?  20  ASN   B CB   1 
ATOM   4134 C CG   . ASN   B 1 20  ? 48.035 -35.005 -12.249 1.00 20.42 ?  20  ASN   B CG   1 
ATOM   4135 O OD1  . ASN   B 1 20  ? 48.705 -35.847 -12.857 1.00 22.62 ?  20  ASN   B OD1  1 
ATOM   4136 N ND2  . ASN   B 1 20  ? 48.268 -34.690 -10.985 1.00 19.61 ?  20  ASN   B ND2  1 
ATOM   4137 H H    . ASN   B 1 20  ? 45.549 -32.573 -14.083 1.00 19.59 ?  20  ASN   B H    1 
ATOM   4138 H HA   . ASN   B 1 20  ? 46.423 -32.823 -11.564 1.00 20.80 ?  20  ASN   B HA   1 
ATOM   4139 H HB2  . ASN   B 1 20  ? 46.057 -34.787 -12.722 1.00 22.85 ?  20  ASN   B HB2  1 
ATOM   4140 H HB3  . ASN   B 1 20  ? 47.024 -34.316 -13.890 1.00 22.85 ?  20  ASN   B HB3  1 
ATOM   4141 H HD21 . ASN   B 1 20  ? 48.917 -35.060 -10.565 1.00 23.50 ?  20  ASN   B HD21 1 
ATOM   4142 H HD22 . ASN   B 1 20  ? 47.775 -34.105 -10.583 1.00 23.50 ?  20  ASN   B HD22 1 
ATOM   4143 N N    . ALA   B 1 21  ? 48.311 -31.210 -11.689 1.00 17.41 ?  21  ALA   B N    1 
ATOM   4144 C CA   . ALA   B 1 21  ? 49.420 -30.278 -11.840 1.00 18.20 ?  21  ALA   B CA   1 
ATOM   4145 C C    . ALA   B 1 21  ? 49.888 -29.791 -10.477 1.00 17.19 ?  21  ALA   B C    1 
ATOM   4146 O O    . ALA   B 1 21  ? 49.148 -29.818 -9.490  1.00 17.05 ?  21  ALA   B O    1 
ATOM   4147 C CB   . ALA   B 1 21  ? 49.023 -29.089 -12.715 1.00 19.55 ?  21  ALA   B CB   1 
ATOM   4148 H H    . ALA   B 1 21  ? 47.911 -31.172 -10.920 1.00 20.87 ?  21  ALA   B H    1 
ATOM   4149 H HA   . ALA   B 1 21  ? 50.157 -30.740 -12.263 1.00 21.82 ?  21  ALA   B HA   1 
ATOM   4150 H HB1  . ALA   B 1 21  ? 49.807 -28.544 -12.861 1.00 23.44 ?  21  ALA   B HB1  1 
ATOM   4151 H HB2  . ALA   B 1 21  ? 48.687 -29.427 -13.559 1.00 23.44 ?  21  ALA   B HB2  1 
ATOM   4152 H HB3  . ALA   B 1 21  ? 48.334 -28.581 -12.262 1.00 23.44 ?  21  ALA   B HB3  1 
ATOM   4153 N N    . ASP   B 1 22  ? 51.144 -29.347 -10.456 1.00 16.53 ?  22  ASP   B N    1 
ATOM   4154 C CA   . ASP   B 1 22  ? 51.753 -28.655 -9.326  1.00 16.04 ?  22  ASP   B CA   1 
ATOM   4155 C C    . ASP   B 1 22  ? 51.344 -27.184 -9.399  1.00 14.71 ?  22  ASP   B C    1 
ATOM   4156 O O    . ASP   B 1 22  ? 51.656 -26.503 -10.380 1.00 14.80 ?  22  ASP   B O    1 
ATOM   4157 C CB   . ASP   B 1 22  ? 53.270 -28.831 -9.480  1.00 17.10 ?  22  ASP   B CB   1 
ATOM   4158 C CG   . ASP   B 1 22  ? 54.095 -28.072 -8.452  1.00 18.65 ?  22  ASP   B CG   1 
ATOM   4159 O OD1  . ASP   B 1 22  ? 53.732 -26.958 -8.044  1.00 18.94 ?  22  ASP   B OD1  1 
ATOM   4160 O OD2  . ASP   B 1 22  ? 55.174 -28.590 -8.084  1.00 20.87 -1 22  ASP   B OD2  1 
ATOM   4161 H H    . ASP   B 1 22  ? 51.684 -29.435 -11.121 1.00 19.82 ?  22  ASP   B H    1 
ATOM   4162 H HA   . ASP   B 1 22  ? 51.462 -29.044 -8.482  1.00 19.23 ?  22  ASP   B HA   1 
ATOM   4163 H HB2  . ASP   B 1 22  ? 53.493 -29.768 -9.396  1.00 20.49 ?  22  ASP   B HB2  1 
ATOM   4164 H HB3  . ASP   B 1 22  ? 53.534 -28.505 -10.355 1.00 20.49 ?  22  ASP   B HB3  1 
ATOM   4165 N N    . ILE   B 1 23  ? 50.633 -26.696 -8.375  1.00 13.84 ?  23  ILE   B N    1 
ATOM   4166 C CA   . ILE   B 1 23  ? 50.047 -25.354 -8.443  1.00 13.36 ?  23  ILE   B CA   1 
ATOM   4167 C C    . ILE   B 1 23  ? 51.105 -24.265 -8.583  1.00 13.00 ?  23  ILE   B C    1 
ATOM   4168 O O    . ILE   B 1 23  ? 50.842 -23.222 -9.192  1.00 12.67 ?  23  ILE   B O    1 
ATOM   4169 C CB   . ILE   B 1 23  ? 49.112 -25.109 -7.243  1.00 13.65 ?  23  ILE   B CB   1 
ATOM   4170 C CG1  . ILE   B 1 23  ? 48.293 -23.835 -7.446  1.00 14.42 ?  23  ILE   B CG1  1 
ATOM   4171 C CG2  . ILE   B 1 23  ? 49.882 -25.064 -5.945  1.00 14.72 ?  23  ILE   B CG2  1 
ATOM   4172 C CD1  . ILE   B 1 23  ? 47.165 -23.679 -6.442  1.00 15.11 ?  23  ILE   B CD1  1 
ATOM   4173 H H    . ILE   B 1 23  ? 50.479 -27.115 -7.641  1.00 16.58 ?  23  ILE   B H    1 
ATOM   4174 H HA   . ILE   B 1 23  ? 49.497 -25.311 -9.238  1.00 16.01 ?  23  ILE   B HA   1 
ATOM   4175 H HB   . ILE   B 1 23  ? 48.491 -25.851 -7.196  1.00 16.35 ?  23  ILE   B HB   1 
ATOM   4176 H HG12 . ILE   B 1 23  ? 48.881 -23.064 -7.354  1.00 17.28 ?  23  ILE   B HG12 1 
ATOM   4177 H HG13 . ILE   B 1 23  ? 47.906 -23.844 -8.336  1.00 17.28 ?  23  ILE   B HG13 1 
ATOM   4178 H HG21 . ILE   B 1 23  ? 49.257 -25.069 -5.206  1.00 17.64 ?  23  ILE   B HG21 1 
ATOM   4179 H HG22 . ILE   B 1 23  ? 50.459 -25.843 -5.896  1.00 17.64 ?  23  ILE   B HG22 1 
ATOM   4180 H HG23 . ILE   B 1 23  ? 50.418 -24.255 -5.923  1.00 17.64 ?  23  ILE   B HG23 1 
ATOM   4181 H HD11 . ILE   B 1 23  ? 46.639 -22.901 -6.676  1.00 18.11 ?  23  ILE   B HD11 1 
ATOM   4182 H HD12 . ILE   B 1 23  ? 46.609 -24.477 -6.475  1.00 18.11 ?  23  ILE   B HD12 1 
ATOM   4183 H HD13 . ILE   B 1 23  ? 47.542 -23.576 -5.557  1.00 18.11 ?  23  ILE   B HD13 1 
ATOM   4184 N N    . VAL   B 1 24  ? 52.301 -24.472 -8.024  1.00 13.46 ?  24  VAL   B N    1 
ATOM   4185 C CA   . VAL   B 1 24  ? 53.378 -23.492 -8.184  1.00 13.93 ?  24  VAL   B CA   1 
ATOM   4186 C C    . VAL   B 1 24  ? 53.836 -23.442 -9.635  1.00 14.44 ?  24  VAL   B C    1 
ATOM   4187 O O    . VAL   B 1 24  ? 53.985 -22.364 -10.226 1.00 14.68 ?  24  VAL   B O    1 
ATOM   4188 C CB   . VAL   B 1 24  ? 54.552 -23.812 -7.237  1.00 14.97 ?  24  VAL   B CB   1 
ATOM   4189 C CG1  . VAL   B 1 24  ? 55.759 -22.923 -7.550  1.00 15.64 ?  24  VAL   B CG1  1 
ATOM   4190 C CG2  . VAL   B 1 24  ? 54.130 -23.638 -5.799  1.00 15.68 ?  24  VAL   B CG2  1 
ATOM   4191 H H    . VAL   B 1 24  ? 52.510 -25.160 -7.555  1.00 16.13 ?  24  VAL   B H    1 
ATOM   4192 H HA   . VAL   B 1 24  ? 53.040 -22.615 -7.949  1.00 16.69 ?  24  VAL   B HA   1 
ATOM   4193 H HB   . VAL   B 1 24  ? 54.819 -24.736 -7.359  1.00 17.94 ?  24  VAL   B HB   1 
ATOM   4194 H HG11 . VAL   B 1 24  ? 56.350 -22.911 -6.780  1.00 18.74 ?  24  VAL   B HG11 1 
ATOM   4195 H HG12 . VAL   B 1 24  ? 56.226 -23.285 -8.317  1.00 18.74 ?  24  VAL   B HG12 1 
ATOM   4196 H HG13 . VAL   B 1 24  ? 55.449 -22.023 -7.739  1.00 18.74 ?  24  VAL   B HG13 1 
ATOM   4197 H HG21 . VAL   B 1 24  ? 54.852 -23.923 -5.220  1.00 18.79 ?  24  VAL   B HG21 1 
ATOM   4198 H HG22 . VAL   B 1 24  ? 53.929 -22.701 -5.642  1.00 18.79 ?  24  VAL   B HG22 1 
ATOM   4199 H HG23 . VAL   B 1 24  ? 53.339 -24.177 -5.633  1.00 18.79 ?  24  VAL   B HG23 1 
ATOM   4200 N N    . GLU   B 1 25  ? 54.088 -24.612 -10.228 1.00 15.01 ?  25  GLU   B N    1 
ATOM   4201 C CA   . GLU   B 1 25  ? 54.487 -24.641 -11.628 1.00 16.57 ?  25  GLU   B CA   1 
ATOM   4202 C C    . GLU   B 1 25  ? 53.382 -24.096 -12.519 1.00 15.55 ?  25  GLU   B C    1 
ATOM   4203 O O    . GLU   B 1 25  ? 53.653 -23.387 -13.497 1.00 16.40 ?  25  GLU   B O    1 
ATOM   4204 C CB   . GLU   B 1 25  ? 54.881 -26.061 -12.030 1.00 20.44 ?  25  GLU   B CB   1 
ATOM   4205 C CG   . GLU   B 1 25  ? 56.174 -26.520 -11.374 1.00 25.90 ?  25  GLU   B CG   1 
ATOM   4206 C CD   . GLU   B 1 25  ? 57.294 -25.492 -11.466 1.00 30.76 ?  25  GLU   B CD   1 
ATOM   4207 O OE1  . GLU   B 1 25  ? 57.667 -25.109 -12.595 1.00 32.53 ?  25  GLU   B OE1  1 
ATOM   4208 O OE2  . GLU   B 1 25  ? 57.791 -25.050 -10.403 1.00 32.44 -1 25  GLU   B OE2  1 
ATOM   4209 H H    . GLU   B 1 25  ? 54.032 -25.381 -9.848  1.00 17.99 ?  25  GLU   B H    1 
ATOM   4210 H HA   . GLU   B 1 25  ? 55.245 -24.056 -11.747 1.00 19.86 ?  25  GLU   B HA   1 
ATOM   4211 H HB2  . GLU   B 1 25  ? 54.176 -26.674 -11.760 1.00 24.50 ?  25  GLU   B HB2  1 
ATOM   4212 H HB3  . GLU   B 1 25  ? 54.997 -26.096 -12.992 1.00 24.50 ?  25  GLU   B HB3  1 
ATOM   4213 H HG2  . GLU   B 1 25  ? 56.015 -26.677 -10.437 1.00 31.06 ?  25  GLU   B HG2  1 
ATOM   4214 H HG3  . GLU   B 1 25  ? 56.478 -27.328 -11.812 1.00 31.06 ?  25  GLU   B HG3  1 
ATOM   4215 N N    . GLU   B 1 26  ? 52.127 -24.412 -12.191 1.00 14.39 ?  26  GLU   B N    1 
ATOM   4216 C CA   . GLU   B 1 26  ? 51.003 -23.875 -12.951 1.00 15.11 ?  26  GLU   B CA   1 
ATOM   4217 C C    . GLU   B 1 26  ? 50.958 -22.357 -12.864 1.00 13.85 ?  26  GLU   B C    1 
ATOM   4218 O O    . GLU   B 1 26  ? 50.767 -21.677 -13.876 1.00 15.50 ?  26  GLU   B O    1 
ATOM   4219 C CB   . GLU   B 1 26  ? 49.689 -24.462 -12.438 1.00 17.13 ?  26  GLU   B CB   1 
ATOM   4220 C CG   . GLU   B 1 26  ? 49.245 -25.738 -13.124 1.00 20.70 ?  26  GLU   B CG   1 
ATOM   4221 C CD   . GLU   B 1 26  ? 49.005 -25.574 -14.622 1.00 22.31 ?  26  GLU   B CD   1 
ATOM   4222 O OE1  . GLU   B 1 26  ? 48.032 -24.908 -15.040 1.00 22.72 ?  26  GLU   B OE1  1 
ATOM   4223 O OE2  . GLU   B 1 26  ? 49.799 -26.139 -15.384 1.00 24.58 -1 26  GLU   B OE2  1 
ATOM   4224 H H    . GLU   B 1 26  ? 51.900 -24.938 -11.542 1.00 17.24 ?  26  GLU   B H    1 
ATOM   4225 H HA   . GLU   B 1 26  ? 51.102 -24.121 -13.880 1.00 18.11 ?  26  GLU   B HA   1 
ATOM   4226 H HB2  . GLU   B 1 26  ? 49.782 -24.660 -11.491 1.00 20.53 ?  26  GLU   B HB2  1 
ATOM   4227 H HB3  . GLU   B 1 26  ? 48.986 -23.804 -12.561 1.00 20.53 ?  26  GLU   B HB3  1 
ATOM   4228 H HG2  . GLU   B 1 26  ? 49.939 -26.398 -13.018 1.00 24.82 ?  26  GLU   B HG2  1 
ATOM   4229 H HG3  . GLU   B 1 26  ? 48.420 -26.044 -12.715 1.00 24.82 ?  26  GLU   B HG3  1 
ATOM   4230 N N    . ALA   B 1 27  ? 51.107 -21.811 -11.654 1.00 13.00 ?  27  ALA   B N    1 
ATOM   4231 C CA   . ALA   B 1 27  ? 51.078 -20.360 -11.506 1.00 13.56 ?  27  ALA   B CA   1 
ATOM   4232 C C    . ALA   B 1 27  ? 52.153 -19.699 -12.360 1.00 14.44 ?  27  ALA   B C    1 
ATOM   4233 O O    . ALA   B 1 27  ? 51.896 -18.692 -13.037 1.00 15.26 ?  27  ALA   B O    1 
ATOM   4234 C CB   . ALA   B 1 27  ? 51.225 -19.975 -10.033 1.00 13.84 ?  27  ALA   B CB   1 
ATOM   4235 H H    . ALA   B 1 27  ? 51.217 -22.249 -10.919 1.00 15.58 ?  27  ALA   B H    1 
ATOM   4236 H HA   . ALA   B 1 27  ? 50.220 -20.030 -11.807 1.00 16.25 ?  27  ALA   B HA   1 
ATOM   4237 H HB1  . ALA   B 1 27  ? 51.196 -19.008 -9.952  1.00 16.59 ?  27  ALA   B HB1  1 
ATOM   4238 H HB2  . ALA   B 1 27  ? 50.488 -20.366 -9.530  1.00 16.59 ?  27  ALA   B HB2  1 
ATOM   4239 H HB3  . ALA   B 1 27  ? 52.067 -20.311 -9.696  1.00 16.59 ?  27  ALA   B HB3  1 
ATOM   4240 N N    . LYS   B 1 28  ? 53.363 -20.258 -12.357 1.00 16.28 ?  28  LYS   B N    1 
ATOM   4241 C CA   . LYS   B 1 28  ? 54.441 -19.645 -13.121 1.00 17.78 ?  28  LYS   B CA   1 
ATOM   4242 C C    . LYS   B 1 28  ? 54.190 -19.722 -14.621 1.00 18.67 ?  28  LYS   B C    1 
ATOM   4243 O O    . LYS   B 1 28  ? 54.605 -18.820 -15.359 1.00 20.03 ?  28  LYS   B O    1 
ATOM   4244 C CB   . LYS   B 1 28  ? 55.790 -20.256 -12.732 1.00 20.71 ?  28  LYS   B CB   1 
ATOM   4245 C CG   . LYS   B 1 28  ? 56.191 -19.927 -11.295 1.00 24.10 ?  28  LYS   B CG   1 
ATOM   4246 C CD   . LYS   B 1 28  ? 57.623 -20.323 -10.969 1.00 28.34 ?  28  LYS   B CD   1 
ATOM   4247 C CE   . LYS   B 1 28  ? 57.728 -21.777 -10.587 1.00 31.50 ?  28  LYS   B CE   1 
ATOM   4248 N NZ   . LYS   B 1 28  ? 59.084 -22.100 -10.057 1.00 32.94 ?  28  LYS   B NZ   1 
ATOM   4249 H H    . LYS   B 1 28  ? 53.582 -20.971 -11.931 1.00 19.51 ?  28  LYS   B H    1 
ATOM   4250 H HA   . LYS   B 1 28  ? 54.481 -18.704 -12.896 1.00 21.31 ?  28  LYS   B HA   1 
ATOM   4251 H HB2  . LYS   B 1 28  ? 55.742 -21.219 -12.815 1.00 24.83 ?  28  LYS   B HB2  1 
ATOM   4252 H HB3  . LYS   B 1 28  ? 56.481 -19.906 -13.320 1.00 24.83 ?  28  LYS   B HB3  1 
ATOM   4253 H HG2  . LYS   B 1 28  ? 56.103 -18.969 -11.157 1.00 28.90 ?  28  LYS   B HG2  1 
ATOM   4254 H HG3  . LYS   B 1 28  ? 55.601 -20.402 -10.690 1.00 28.90 ?  28  LYS   B HG3  1 
ATOM   4255 H HD2  . LYS   B 1 28  ? 58.179 -20.168 -11.749 1.00 33.99 ?  28  LYS   B HD2  1 
ATOM   4256 H HD3  . LYS   B 1 28  ? 57.937 -19.786 -10.224 1.00 33.99 ?  28  LYS   B HD3  1 
ATOM   4257 H HE2  . LYS   B 1 28  ? 57.076 -21.976 -9.897  1.00 37.78 ?  28  LYS   B HE2  1 
ATOM   4258 H HE3  . LYS   B 1 28  ? 57.568 -22.328 -11.370 1.00 37.78 ?  28  LYS   B HE3  1 
ATOM   4259 H HZ1  . LYS   B 1 28  ? 59.128 -22.961 -9.837  1.00 39.51 ?  28  LYS   B HZ1  1 
ATOM   4260 H HZ2  . LYS   B 1 28  ? 59.701 -21.927 -10.675 1.00 39.51 ?  28  LYS   B HZ2  1 
ATOM   4261 H HZ3  . LYS   B 1 28  ? 59.253 -21.608 -9.335  1.00 39.51 ?  28  LYS   B HZ3  1 
ATOM   4262 N N    . LYS   B 1 29  ? 53.485 -20.754 -15.086 1.00 19.88 ?  29  LYS   B N    1 
ATOM   4263 C CA   . LYS   B 1 29  ? 53.196 -20.895 -16.509 1.00 22.71 ?  29  LYS   B CA   1 
ATOM   4264 C C    . LYS   B 1 29  ? 51.955 -20.120 -16.942 1.00 21.43 ?  29  LYS   B C    1 
ATOM   4265 O O    . LYS   B 1 29  ? 51.964 -19.487 -18.003 1.00 22.91 ?  29  LYS   B O    1 
ATOM   4266 C CB   . LYS   B 1 29  ? 53.025 -22.375 -16.862 1.00 27.22 ?  29  LYS   B CB   1 
ATOM   4267 C CG   . LYS   B 1 29  ? 52.870 -22.640 -18.352 1.00 31.49 ?  29  LYS   B CG   1 
ATOM   4268 C CD   . LYS   B 1 29  ? 53.149 -24.098 -18.696 1.00 35.03 ?  29  LYS   B CD   1 
ATOM   4269 C CE   . LYS   B 1 29  ? 52.104 -25.030 -18.105 1.00 37.39 ?  29  LYS   B CE   1 
ATOM   4270 N NZ   . LYS   B 1 29  ? 52.384 -26.458 -18.437 1.00 38.48 ?  29  LYS   B NZ   1 
ATOM   4271 H H    . LYS   B 1 29  ? 53.159 -21.385 -14.594 1.00 23.83 ?  29  LYS   B H    1 
ATOM   4272 H HA   . LYS   B 1 29  ? 53.948 -20.554 -17.013 1.00 27.23 ?  29  LYS   B HA   1 
ATOM   4273 H HB2  . LYS   B 1 29  ? 53.808 -22.859 -16.556 1.00 32.64 ?  29  LYS   B HB2  1 
ATOM   4274 H HB3  . LYS   B 1 29  ? 52.234 -22.713 -16.419 1.00 32.64 ?  29  LYS   B HB3  1 
ATOM   4275 H HG2  . LYS   B 1 29  ? 51.962 -22.433 -18.620 1.00 37.77 ?  29  LYS   B HG2  1 
ATOM   4276 H HG3  . LYS   B 1 29  ? 53.499 -22.087 -18.842 1.00 37.77 ?  29  LYS   B HG3  1 
ATOM   4277 H HD2  . LYS   B 1 29  ? 53.141 -24.206 -19.660 1.00 42.02 ?  29  LYS   B HD2  1 
ATOM   4278 H HD3  . LYS   B 1 29  ? 54.016 -24.351 -18.339 1.00 42.02 ?  29  LYS   B HD3  1 
ATOM   4279 H HE2  . LYS   B 1 29  ? 52.102 -24.939 -17.140 1.00 44.85 ?  29  LYS   B HE2  1 
ATOM   4280 H HE3  . LYS   B 1 29  ? 51.233 -24.801 -18.466 1.00 44.85 ?  29  LYS   B HE3  1 
ATOM   4281 H HZ1  . LYS   B 1 29  ? 51.758 -26.981 -18.081 1.00 46.15 ?  29  LYS   B HZ1  1 
ATOM   4282 H HZ2  . LYS   B 1 29  ? 52.387 -26.570 -19.320 1.00 46.15 ?  29  LYS   B HZ2  1 
ATOM   4283 H HZ3  . LYS   B 1 29  ? 53.178 -26.695 -18.113 1.00 46.15 ?  29  LYS   B HZ3  1 
ATOM   4284 N N    . VAL   B 1 30  ? 50.888 -20.167 -16.140 1.00 19.97 ?  30  VAL   B N    1 
ATOM   4285 C CA   . VAL   B 1 30  ? 49.601 -19.576 -16.518 1.00 20.23 ?  30  VAL   B CA   1 
ATOM   4286 C C    . VAL   B 1 30  ? 49.593 -18.062 -16.343 1.00 19.30 ?  30  VAL   B C    1 
ATOM   4287 O O    . VAL   B 1 30  ? 48.844 -17.351 -17.032 1.00 20.18 ?  30  VAL   B O    1 
ATOM   4288 C CB   . VAL   B 1 30  ? 48.485 -20.224 -15.674 1.00 21.90 ?  30  VAL   B CB   1 
ATOM   4289 C CG1  . VAL   B 1 30  ? 47.188 -19.435 -15.775 1.00 22.58 ?  30  VAL   B CG1  1 
ATOM   4290 C CG2  . VAL   B 1 30  ? 48.275 -21.679 -16.087 1.00 22.76 ?  30  VAL   B CG2  1 
ATOM   4291 H H    . VAL   B 1 30  ? 50.876 -20.560 -15.367 1.00 23.95 ?  30  VAL   B H    1 
ATOM   4292 H HA   . VAL   B 1 30  ? 49.421 -19.790 -17.446 1.00 24.26 ?  30  VAL   B HA   1 
ATOM   4293 H HB   . VAL   B 1 30  ? 48.754 -20.227 -14.741 1.00 26.26 ?  30  VAL   B HB   1 
ATOM   4294 H HG11 . VAL   B 1 30  ? 46.447 -20.036 -15.591 1.00 27.07 ?  30  VAL   B HG11 1 
ATOM   4295 H HG12 . VAL   B 1 30  ? 47.197 -18.720 -15.123 1.00 27.07 ?  30  VAL   B HG12 1 
ATOM   4296 H HG13 . VAL   B 1 30  ? 47.098 -19.083 -16.669 1.00 27.07 ?  30  VAL   B HG13 1 
ATOM   4297 H HG21 . VAL   B 1 30  ? 47.576 -22.070 -15.534 1.00 27.29 ?  30  VAL   B HG21 1 
ATOM   4298 H HG22 . VAL   B 1 30  ? 48.006 -21.707 -17.020 1.00 27.29 ?  30  VAL   B HG22 1 
ATOM   4299 H HG23 . VAL   B 1 30  ? 49.102 -22.167 -15.965 1.00 27.29 ?  30  VAL   B HG23 1 
ATOM   4300 N N    . LYS   B 1 31  ? 50.378 -17.558 -15.404 1.00 18.93 ?  31  LYS   B N    1 
ATOM   4301 C CA   . LYS   B 1 31  ? 50.400 -16.148 -15.044 1.00 19.11 ?  31  LYS   B CA   1 
ATOM   4302 C C    . LYS   B 1 31  ? 48.997 -15.680 -14.662 1.00 16.94 ?  31  LYS   B C    1 
ATOM   4303 O O    . LYS   B 1 31  ? 48.456 -14.760 -15.285 1.00 17.88 ?  31  LYS   B O    1 
ATOM   4304 C CB   . LYS   B 1 31  ? 51.029 -15.324 -16.174 1.00 22.16 ?  31  LYS   B CB   1 
ATOM   4305 C CG   . LYS   B 1 31  ? 52.451 -15.780 -16.517 1.00 25.56 ?  31  LYS   B CG   1 
ATOM   4306 C CD   . LYS   B 1 31  ? 53.010 -15.044 -17.716 1.00 28.94 ?  31  LYS   B CD   1 
ATOM   4307 C CE   . LYS   B 1 31  ? 54.498 -15.283 -17.853 1.00 31.41 ?  31  LYS   B CE   1 
ATOM   4308 N NZ   . LYS   B 1 31  ? 55.233 -14.818 -16.642 1.00 32.61 ?  31  LYS   B NZ   1 
ATOM   4309 H H    . LYS   B 1 31  ? 50.929 -18.035 -14.955 1.00 22.70 ?  31  LYS   B H    1 
ATOM   4310 H HA   . LYS   B 1 31  ? 50.957 -16.054 -14.268 1.00 22.91 ?  31  LYS   B HA   1 
ATOM   4311 H HB2  . LYS   B 1 31  ? 50.485 -15.407 -16.974 1.00 26.57 ?  31  LYS   B HB2  1 
ATOM   4312 H HB3  . LYS   B 1 31  ? 51.070 -14.397 -15.895 1.00 26.57 ?  31  LYS   B HB3  1 
ATOM   4313 H HG2  . LYS   B 1 31  ? 53.025 -15.614 -15.754 1.00 30.64 ?  31  LYS   B HG2  1 
ATOM   4314 H HG3  . LYS   B 1 31  ? 52.440 -16.730 -16.723 1.00 30.64 ?  31  LYS   B HG3  1 
ATOM   4315 H HD2  . LYS   B 1 31  ? 52.569 -15.368 -18.518 1.00 34.70 ?  31  LYS   B HD2  1 
ATOM   4316 H HD3  . LYS   B 1 31  ? 52.856 -14.096 -17.604 1.00 34.70 ?  31  LYS   B HD3  1 
ATOM   4317 H HE2  . LYS   B 1 31  ? 54.664 -16.233 -17.964 1.00 37.67 ?  31  LYS   B HE2  1 
ATOM   4318 H HE3  . LYS   B 1 31  ? 54.831 -14.791 -18.620 1.00 37.67 ?  31  LYS   B HE3  1 
ATOM   4319 H HZ1  . LYS   B 1 31  ? 56.107 -14.809 -16.801 1.00 39.11 ?  31  LYS   B HZ1  1 
ATOM   4320 H HZ2  . LYS   B 1 31  ? 54.970 -13.996 -16.425 1.00 39.11 ?  31  LYS   B HZ2  1 
ATOM   4321 H HZ3  . LYS   B 1 31  ? 55.069 -15.363 -15.957 1.00 39.11 ?  31  LYS   B HZ3  1 
ATOM   4322 N N    . PRO   B 1 32  ? 48.387 -16.283 -13.634 1.00 14.65 ?  32  PRO   B N    1 
ATOM   4323 C CA   . PRO   B 1 32  ? 47.006 -15.931 -13.279 1.00 13.78 ?  32  PRO   B CA   1 
ATOM   4324 C C    . PRO   B 1 32  ? 46.926 -14.584 -12.579 1.00 13.94 ?  32  PRO   B C    1 
ATOM   4325 O O    . PRO   B 1 32  ? 47.845 -14.165 -11.871 1.00 15.22 ?  32  PRO   B O    1 
ATOM   4326 C CB   . PRO   B 1 32  ? 46.611 -17.048 -12.308 1.00 14.02 ?  32  PRO   B CB   1 
ATOM   4327 C CG   . PRO   B 1 32  ? 47.914 -17.381 -11.630 1.00 14.41 ?  32  PRO   B CG   1 
ATOM   4328 C CD   . PRO   B 1 32  ? 48.956 -17.283 -12.710 1.00 14.66 ?  32  PRO   B CD   1 
ATOM   4329 H HA   . PRO   B 1 32  ? 46.422 -15.947 -14.059 1.00 16.51 ?  32  PRO   B HA   1 
ATOM   4330 H HB2  . PRO   B 1 32  ? 45.960 -16.719 -11.667 1.00 16.80 ?  32  PRO   B HB2  1 
ATOM   4331 H HB3  . PRO   B 1 32  ? 46.269 -17.814 -12.793 1.00 16.80 ?  32  PRO   B HB3  1 
ATOM   4332 H HG2  . PRO   B 1 32  ? 48.092 -16.735 -10.924 1.00 17.26 ?  32  PRO   B HG2  1 
ATOM   4333 H HG3  . PRO   B 1 32  ? 47.879 -18.280 -11.266 1.00 17.26 ?  32  PRO   B HG3  1 
ATOM   4334 H HD2  . PRO   B 1 32  ? 49.791 -16.964 -12.345 1.00 17.57 ?  32  PRO   B HD2  1 
ATOM   4335 H HD3  . PRO   B 1 32  ? 49.056 -18.139 -13.152 1.00 17.57 ?  32  PRO   B HD3  1 
ATOM   4336 N N    . THR   B 1 33  ? 45.778 -13.927 -12.747 1.00 13.20 ?  33  THR   B N    1 
ATOM   4337 C CA   . THR   B 1 33  ? 45.489 -12.750 -11.939 1.00 13.51 ?  33  THR   B CA   1 
ATOM   4338 C C    . THR   B 1 33  ? 45.440 -13.101 -10.457 1.00 13.12 ?  33  THR   B C    1 
ATOM   4339 O O    . THR   B 1 33  ? 45.915 -12.323 -9.614  1.00 14.07 ?  33  THR   B O    1 
ATOM   4340 C CB   . THR   B 1 33  ? 44.168 -12.117 -12.387 1.00 14.46 ?  33  THR   B CB   1 
ATOM   4341 O OG1  . THR   B 1 33  ? 44.202 -11.865 -13.797 1.00 14.50 ?  33  THR   B OG1  1 
ATOM   4342 C CG2  . THR   B 1 33  ? 43.929 -10.811 -11.646 1.00 15.90 ?  33  THR   B CG2  1 
ATOM   4343 H H    . THR   B 1 33  ? 45.159 -14.148 -13.308 1.00 15.81 ?  33  THR   B H    1 
ATOM   4344 H HA   . THR   B 1 33  ? 46.191 -12.100 -12.074 1.00 16.19 ?  33  THR   B HA   1 
ATOM   4345 H HB   . THR   B 1 33  ? 43.433 -12.724 -12.185 1.00 17.33 ?  33  THR   B HB   1 
ATOM   4346 H HG1  . THR   B 1 33  ? 43.476 -11.510 -14.044 1.00 17.38 ?  33  THR   B HG1  1 
ATOM   4347 H HG21 . THR   B 1 33  ? 43.176 -10.344 -12.033 1.00 19.05 ?  33  THR   B HG21 1 
ATOM   4348 H HG22 . THR   B 1 33  ? 43.747 -10.988 -10.710 1.00 19.05 ?  33  THR   B HG22 1 
ATOM   4349 H HG23 . THR   B 1 33  ? 44.719 -10.249 -11.713 1.00 19.05 ?  33  THR   B HG23 1 
ATOM   4350 N N    . VAL   B 1 34  ? 44.881 -14.271 -10.119 1.00 12.25 ?  34  VAL   B N    1 
ATOM   4351 C CA   . VAL   B 1 34  ? 44.687 -14.671 -8.729  1.00 11.64 ?  34  VAL   B CA   1 
ATOM   4352 C C    . VAL   B 1 34  ? 45.112 -16.120 -8.561  1.00 10.86 ?  34  VAL   B C    1 
ATOM   4353 O O    . VAL   B 1 34  ? 44.595 -17.008 -9.251  1.00 11.67 ?  34  VAL   B O    1 
ATOM   4354 C CB   . VAL   B 1 34  ? 43.217 -14.527 -8.286  1.00 12.92 ?  34  VAL   B CB   1 
ATOM   4355 C CG1  . VAL   B 1 34  ? 43.056 -14.957 -6.839  1.00 13.09 ?  34  VAL   B CG1  1 
ATOM   4356 C CG2  . VAL   B 1 34  ? 42.706 -13.104 -8.503  1.00 13.86 ?  34  VAL   B CG2  1 
ATOM   4357 H H    . VAL   B 1 34  ? 44.610 -14.862 -10.687 1.00 14.68 ?  34  VAL   B H    1 
ATOM   4358 H HA   . VAL   B 1 34  ? 45.240 -14.119 -8.153  1.00 13.95 ?  34  VAL   B HA   1 
ATOM   4359 H HB   . VAL   B 1 34  ? 42.677 -15.117 -8.831  1.00 15.48 ?  34  VAL   B HB   1 
ATOM   4360 H HG11 . VAL   B 1 34  ? 42.194 -14.644 -6.514  1.00 15.68 ?  34  VAL   B HG11 1 
ATOM   4361 H HG12 . VAL   B 1 34  ? 43.092 -15.925 -6.786  1.00 15.68 ?  34  VAL   B HG12 1 
ATOM   4362 H HG13 . VAL   B 1 34  ? 43.766 -14.566 -6.308  1.00 15.68 ?  34  VAL   B HG13 1 
ATOM   4363 H HG21 . VAL   B 1 34  ? 41.789 -13.047 -8.189  1.00 16.61 ?  34  VAL   B HG21 1 
ATOM   4364 H HG22 . VAL   B 1 34  ? 43.264 -12.485 -8.011  1.00 16.61 ?  34  VAL   B HG22 1 
ATOM   4365 H HG23 . VAL   B 1 34  ? 42.739 -12.896 -9.453  1.00 16.61 ?  34  VAL   B HG23 1 
ATOM   4366 N N    . VAL   B 1 35  ? 46.018 -16.370 -7.619  1.00 10.29 ?  35  VAL   B N    1 
ATOM   4367 C CA   . VAL   B 1 35  ? 46.259 -17.713 -7.106  1.00 10.09 ?  35  VAL   B CA   1 
ATOM   4368 C C    . VAL   B 1 35  ? 45.716 -17.769 -5.689  1.00 9.79  ?  35  VAL   B C    1 
ATOM   4369 O O    . VAL   B 1 35  ? 45.929 -16.846 -4.895  1.00 10.32 ?  35  VAL   B O    1 
ATOM   4370 C CB   . VAL   B 1 35  ? 47.744 -18.132 -7.180  1.00 11.19 ?  35  VAL   B CB   1 
ATOM   4371 C CG1  . VAL   B 1 35  ? 48.637 -17.291 -6.254  1.00 12.02 ?  35  VAL   B CG1  1 
ATOM   4372 C CG2  . VAL   B 1 35  ? 47.885 -19.631 -6.866  1.00 11.95 ?  35  VAL   B CG2  1 
ATOM   4373 H H    . VAL   B 1 35  ? 46.518 -15.767 -7.258  1.00 12.32 ?  35  VAL   B H    1 
ATOM   4374 H HA   . VAL   B 1 35  ? 45.748 -18.345 -7.632  1.00 12.08 ?  35  VAL   B HA   1 
ATOM   4375 H HB   . VAL   B 1 35  ? 48.051 -18.000 -8.091  1.00 13.41 ?  35  VAL   B HB   1 
ATOM   4376 H HG11 . VAL   B 1 35  ? 49.563 -17.516 -6.431  1.00 14.40 ?  35  VAL   B HG11 1 
ATOM   4377 H HG12 . VAL   B 1 35  ? 48.475 -16.358 -6.428  1.00 14.40 ?  35  VAL   B HG12 1 
ATOM   4378 H HG13 . VAL   B 1 35  ? 48.416 -17.506 -5.332  1.00 14.40 ?  35  VAL   B HG13 1 
ATOM   4379 H HG21 . VAL   B 1 35  ? 48.809 -19.895 -6.970  1.00 14.32 ?  35  VAL   B HG21 1 
ATOM   4380 H HG22 . VAL   B 1 35  ? 47.594 -19.794 -5.952  1.00 14.32 ?  35  VAL   B HG22 1 
ATOM   4381 H HG23 . VAL   B 1 35  ? 47.325 -20.142 -7.479  1.00 14.32 ?  35  VAL   B HG23 1 
ATOM   4382 N N    . VAL   B 1 36  ? 44.998 -18.851 -5.374  1.00 9.94  ?  36  VAL   B N    1 
ATOM   4383 C CA   . VAL   B 1 36  ? 44.450 -19.056 -4.045  1.00 9.78  ?  36  VAL   B CA   1 
ATOM   4384 C C    . VAL   B 1 36  ? 45.452 -19.823 -3.193  1.00 9.57  ?  36  VAL   B C    1 
ATOM   4385 O O    . VAL   B 1 36  ? 45.996 -20.850 -3.621  1.00 10.73 ?  36  VAL   B O    1 
ATOM   4386 C CB   . VAL   B 1 36  ? 43.113 -19.816 -4.122  1.00 10.07 ?  36  VAL   B CB   1 
ATOM   4387 C CG1  . VAL   B 1 36  ? 42.610 -20.185 -2.731  1.00 11.25 ?  36  VAL   B CG1  1 
ATOM   4388 C CG2  . VAL   B 1 36  ? 42.077 -18.984 -4.862  1.00 10.50 ?  36  VAL   B CG2  1 
ATOM   4389 H H    . VAL   B 1 36  ? 44.829 -19.491 -5.923  1.00 11.90 ?  36  VAL   B H    1 
ATOM   4390 H HA   . VAL   B 1 36  ? 44.286 -18.197 -3.627  1.00 11.72 ?  36  VAL   B HA   1 
ATOM   4391 H HB   . VAL   B 1 36  ? 43.245 -20.640 -4.619  1.00 12.06 ?  36  VAL   B HB   1 
ATOM   4392 H HG11 . VAL   B 1 36  ? 41.670 -20.425 -2.788  1.00 13.48 ?  36  VAL   B HG11 1 
ATOM   4393 H HG12 . VAL   B 1 36  ? 43.120 -20.935 -2.392  1.00 13.48 ?  36  VAL   B HG12 1 
ATOM   4394 H HG13 . VAL   B 1 36  ? 42.715 -19.418 -2.144  1.00 13.48 ?  36  VAL   B HG13 1 
ATOM   4395 H HG21 . VAL   B 1 36  ? 41.239 -19.469 -4.889  1.00 12.58 ?  36  VAL   B HG21 1 
ATOM   4396 H HG22 . VAL   B 1 36  ? 41.959 -18.141 -4.397  1.00 12.58 ?  36  VAL   B HG22 1 
ATOM   4397 H HG23 . VAL   B 1 36  ? 42.393 -18.819 -5.767  1.00 12.58 ?  36  VAL   B HG23 1 
ATOM   4398 N N    . ASN   B 1 37  ? 45.669 -19.333 -1.975  1.00 9.99  ?  37  ASN   B N    1 
ATOM   4399 C CA   . ASN   B 1 37  ? 46.423 -20.051 -0.961  1.00 10.12 ?  37  ASN   B CA   1 
ATOM   4400 C C    . ASN   B 1 37  ? 45.474 -20.722 0.025   1.00 10.07 ?  37  ASN   B C    1 
ATOM   4401 O O    . ASN   B 1 37  ? 44.459 -20.147 0.431   1.00 10.83 ?  37  ASN   B O    1 
ATOM   4402 C CB   . ASN   B 1 37  ? 47.356 -19.101 -0.212  1.00 10.42 ?  37  ASN   B CB   1 
ATOM   4403 C CG   . ASN   B 1 37  ? 48.207 -19.816 0.810   1.00 10.44 ?  37  ASN   B CG   1 
ATOM   4404 O OD1  . ASN   B 1 37  ? 48.541 -20.993 0.640   1.00 11.42 ?  37  ASN   B OD1  1 
ATOM   4405 N ND2  . ASN   B 1 37  ? 48.560 -19.116 1.882   1.00 10.64 ?  37  ASN   B ND2  1 
ATOM   4406 H H    . ASN   B 1 37  ? 45.386 -18.562 -1.706  1.00 11.96 ?  37  ASN   B H    1 
ATOM   4407 H HA   . ASN   B 1 37  ? 46.957 -20.740 -1.377  1.00 12.12 ?  37  ASN   B HA   1 
ATOM   4408 H HB2  . ASN   B 1 37  ? 47.956 -18.679 -0.848  1.00 12.48 ?  37  ASN   B HB2  1 
ATOM   4409 H HB3  . ASN   B 1 37  ? 46.838 -18.433 0.256   1.00 12.48 ?  37  ASN   B HB3  1 
ATOM   4410 H HD21 . ASN   B 1 37  ? 49.051 -19.483 2.493   1.00 12.75 ?  37  ASN   B HD21 1 
ATOM   4411 H HD22 . ASN   B 1 37  ? 48.317 -18.306 1.968   1.00 12.75 ?  37  ASN   B HD22 1 
ATOM   4412 N N    . ALA   B 1 38  ? 45.826 -21.951 0.402   1.00 10.31 ?  38  ALA   B N    1 
ATOM   4413 C CA   . ALA   B 1 38  ? 45.173 -22.693 1.483   1.00 10.81 ?  38  ALA   B CA   1 
ATOM   4414 C C    . ALA   B 1 38  ? 45.754 -22.210 2.810   1.00 10.59 ?  38  ALA   B C    1 
ATOM   4415 O O    . ALA   B 1 38  ? 46.659 -22.816 3.395   1.00 11.59 ?  38  ALA   B O    1 
ATOM   4416 C CB   . ALA   B 1 38  ? 45.392 -24.189 1.296   1.00 12.12 ?  38  ALA   B CB   1 
ATOM   4417 H H    . ALA   B 1 38  ? 46.471 -22.388 0.043   1.00 12.35 ?  38  ALA   B H    1 
ATOM   4418 H HA   . ALA   B 1 38  ? 44.222 -22.515 1.480   1.00 12.95 ?  38  ALA   B HA   1 
ATOM   4419 H HB1  . ALA   B 1 38  ? 44.948 -24.669 2.022   1.00 14.52 ?  38  ALA   B HB1  1 
ATOM   4420 H HB2  . ALA   B 1 38  ? 45.006 -24.462 0.448   1.00 14.52 ?  38  ALA   B HB2  1 
ATOM   4421 H HB3  . ALA   B 1 38  ? 46.339 -24.383 1.310   1.00 14.52 ?  38  ALA   B HB3  1 
ATOM   4422 N N    . ALA   B 1 39  ? 45.232 -21.070 3.271   1.00 10.50 ?  39  ALA   B N    1 
ATOM   4423 C CA   . ALA   B 1 39  ? 45.780 -20.340 4.404   1.00 10.40 ?  39  ALA   B CA   1 
ATOM   4424 C C    . ALA   B 1 39  ? 45.161 -20.785 5.725   1.00 10.18 ?  39  ALA   B C    1 
ATOM   4425 O O    . ALA   B 1 39  ? 44.131 -21.458 5.769   1.00 11.84 ?  39  ALA   B O    1 
ATOM   4426 C CB   . ALA   B 1 39  ? 45.550 -18.837 4.212   1.00 11.33 ?  39  ALA   B CB   1 
ATOM   4427 H H    . ALA   B 1 39  ? 44.538 -20.698 2.928   1.00 12.58 ?  39  ALA   B H    1 
ATOM   4428 H HA   . ALA   B 1 39  ? 46.736 -20.494 4.449   1.00 12.46 ?  39  ALA   B HA   1 
ATOM   4429 H HB1  . ALA   B 1 39  ? 45.920 -18.361 4.973   1.00 13.58 ?  39  ALA   B HB1  1 
ATOM   4430 H HB2  . ALA   B 1 39  ? 45.991 -18.549 3.397   1.00 13.58 ?  39  ALA   B HB2  1 
ATOM   4431 H HB3  . ALA   B 1 39  ? 44.597 -18.667 4.149   1.00 13.58 ?  39  ALA   B HB3  1 
ATOM   4432 N N    . ASN   B 1 40  ? 45.802 -20.370 6.812   1.00 11.18 ?  40  ASN   B N    1 
ATOM   4433 C CA   . ASN   B 1 40  ? 45.238 -20.412 8.151   1.00 12.30 ?  40  ASN   B CA   1 
ATOM   4434 C C    . ASN   B 1 40  ? 45.063 -18.983 8.668   1.00 11.98 ?  40  ASN   B C    1 
ATOM   4435 O O    . ASN   B 1 40  ? 45.481 -18.008 8.037   1.00 11.87 ?  40  ASN   B O    1 
ATOM   4436 C CB   . ASN   B 1 40  ? 46.091 -21.277 9.097   1.00 13.11 ?  40  ASN   B CB   1 
ATOM   4437 C CG   . ASN   B 1 40  ? 47.549 -20.878 9.111   1.00 14.26 ?  40  ASN   B CG   1 
ATOM   4438 O OD1  . ASN   B 1 40  ? 47.869 -19.699 9.174   1.00 16.17 ?  40  ASN   B OD1  1 
ATOM   4439 N ND2  . ASN   B 1 40  ? 48.441 -21.855 9.059   1.00 14.53 ?  40  ASN   B ND2  1 
ATOM   4440 H H    . ASN   B 1 40  ? 46.601 -20.049 6.794   1.00 13.39 ?  40  ASN   B H    1 
ATOM   4441 H HA   . ASN   B 1 40  ? 44.354 -20.808 8.107   1.00 14.74 ?  40  ASN   B HA   1 
ATOM   4442 H HB2  . ASN   B 1 40  ? 45.747 -21.190 10.000  1.00 15.71 ?  40  ASN   B HB2  1 
ATOM   4443 H HB3  . ASN   B 1 40  ? 46.037 -22.201 8.809   1.00 15.71 ?  40  ASN   B HB3  1 
ATOM   4444 H HD21 . ASN   B 1 40  ? 49.283 -21.672 9.067   1.00 17.42 ?  40  ASN   B HD21 1 
ATOM   4445 H HD22 . ASN   B 1 40  ? 48.179 -22.672 9.020   1.00 17.42 ?  40  ASN   B HD22 1 
ATOM   4446 N N    . VAL   B 1 41  ? 44.402 -18.853 9.820   1.00 12.56 ?  41  VAL   B N    1 
ATOM   4447 C CA   . VAL   B 1 41  ? 43.947 -17.532 10.266  1.00 13.53 ?  41  VAL   B CA   1 
ATOM   4448 C C    . VAL   B 1 41  ? 45.101 -16.586 10.571  1.00 13.33 ?  41  VAL   B C    1 
ATOM   4449 O O    . VAL   B 1 41  ? 44.925 -15.364 10.500  1.00 13.65 ?  41  VAL   B O    1 
ATOM   4450 C CB   . VAL   B 1 41  ? 42.968 -17.612 11.453  1.00 14.70 ?  41  VAL   B CB   1 
ATOM   4451 C CG1  . VAL   B 1 41  ? 41.666 -18.288 11.039  1.00 14.87 ?  41  VAL   B CG1  1 
ATOM   4452 C CG2  . VAL   B 1 41  ? 43.608 -18.305 12.643  1.00 16.03 ?  41  VAL   B CG2  1 
ATOM   4453 H H    . VAL   B 1 41  ? 44.207 -19.496 10.347  1.00 15.05 ?  41  VAL   B H    1 
ATOM   4454 H HA   . VAL   B 1 41  ? 43.455 -17.131 9.533   1.00 16.21 ?  41  VAL   B HA   1 
ATOM   4455 H HB   . VAL   B 1 41  ? 42.748 -16.710 11.732  1.00 17.62 ?  41  VAL   B HB   1 
ATOM   4456 H HG11 . VAL   B 1 41  ? 41.056 -18.288 11.795  1.00 17.82 ?  41  VAL   B HG11 1 
ATOM   4457 H HG12 . VAL   B 1 41  ? 41.277 -17.800 10.299  1.00 17.82 ?  41  VAL   B HG12 1 
ATOM   4458 H HG13 . VAL   B 1 41  ? 41.857 -19.202 10.772  1.00 17.82 ?  41  VAL   B HG13 1 
ATOM   4459 H HG21 . VAL   B 1 41  ? 42.973 -18.334 13.372  1.00 19.21 ?  41  VAL   B HG21 1 
ATOM   4460 H HG22 . VAL   B 1 41  ? 43.857 -19.209 12.386  1.00 19.21 ?  41  VAL   B HG22 1 
ATOM   4461 H HG23 . VAL   B 1 41  ? 44.399 -17.811 12.910  1.00 19.21 ?  41  VAL   B HG23 1 
ATOM   4462 N N    . TYR   B 1 42  ? 46.268 -17.106 10.945  1.00 13.58 ?  42  TYR   B N    1 
ATOM   4463 C CA   . TYR   B 1 42  ? 47.423 -16.259 11.214  1.00 14.12 ?  42  TYR   B CA   1 
ATOM   4464 C C    . TYR   B 1 42  ? 48.387 -16.181 10.033  1.00 13.08 ?  42  TYR   B C    1 
ATOM   4465 O O    . TYR   B 1 42  ? 49.478 -15.611 10.169  1.00 14.24 ?  42  TYR   B O    1 
ATOM   4466 C CB   . TYR   B 1 42  ? 48.121 -16.669 12.518  1.00 15.75 ?  42  TYR   B CB   1 
ATOM   4467 C CG   . TYR   B 1 42  ? 47.516 -15.995 13.745  1.00 16.81 ?  42  TYR   B CG   1 
ATOM   4468 C CD1  . TYR   B 1 42  ? 47.728 -14.641 13.989  1.00 16.29 ?  42  TYR   B CD1  1 
ATOM   4469 C CD2  . TYR   B 1 42  ? 46.727 -16.700 14.641  1.00 18.67 ?  42  TYR   B CD2  1 
ATOM   4470 C CE1  . TYR   B 1 42  ? 47.180 -14.011 15.091  1.00 17.55 ?  42  TYR   B CE1  1 
ATOM   4471 C CE2  . TYR   B 1 42  ? 46.174 -16.077 15.751  1.00 19.07 ?  42  TYR   B CE2  1 
ATOM   4472 C CZ   . TYR   B 1 42  ? 46.402 -14.729 15.969  1.00 19.54 ?  42  TYR   B CZ   1 
ATOM   4473 O OH   . TYR   B 1 42  ? 45.860 -14.095 17.070  1.00 22.40 ?  42  TYR   B OH   1 
ATOM   4474 H H    . TYR   B 1 42  ? 46.415 -17.953 11.038  1.00 16.27 ?  42  TYR   B H    1 
ATOM   4475 H HA   . TYR   B 1 42  ? 47.094 -15.362 11.353  1.00 16.92 ?  42  TYR   B HA   1 
ATOM   4476 H HB2  . TYR   B 1 42  ? 48.043 -17.628 12.633  1.00 18.88 ?  42  TYR   B HB2  1 
ATOM   4477 H HB3  . TYR   B 1 42  ? 49.056 -16.415 12.466  1.00 18.88 ?  42  TYR   B HB3  1 
ATOM   4478 H HD1  . TYR   B 1 42  ? 48.255 -14.148 13.392  1.00 19.52 ?  42  TYR   B HD1  1 
ATOM   4479 H HD2  . TYR   B 1 42  ? 46.566 -17.606 14.495  1.00 22.39 ?  42  TYR   B HD2  1 
ATOM   4480 H HE1  . TYR   B 1 42  ? 47.338 -13.105 15.234  1.00 21.04 ?  42  TYR   B HE1  1 
ATOM   4481 H HE2  . TYR   B 1 42  ? 45.646 -16.564 16.343  1.00 22.87 ?  42  TYR   B HE2  1 
ATOM   4482 H HH   . TYR   B 1 42  ? 46.085 -13.288 17.067  1.00 26.85 ?  42  TYR   B HH   1 
ATOM   4483 N N    . LEU   B 1 43  ? 47.990 -16.696 8.870   1.00 12.03 ?  43  LEU   B N    1 
ATOM   4484 C CA   . LEU   B 1 43  ? 48.807 -16.632 7.660   1.00 11.75 ?  43  LEU   B CA   1 
ATOM   4485 C C    . LEU   B 1 43  ? 50.220 -17.136 7.923   1.00 12.21 ?  43  LEU   B C    1 
ATOM   4486 O O    . LEU   B 1 43  ? 51.205 -16.545 7.478   1.00 13.14 ?  43  LEU   B O    1 
ATOM   4487 C CB   . LEU   B 1 43  ? 48.827 -15.231 7.049   1.00 12.03 ?  43  LEU   B CB   1 
ATOM   4488 C CG   . LEU   B 1 43  ? 47.469 -14.615 6.687   1.00 12.43 ?  43  LEU   B CG   1 
ATOM   4489 C CD1  . LEU   B 1 43  ? 47.681 -13.211 6.123   1.00 13.50 ?  43  LEU   B CD1  1 
ATOM   4490 C CD2  . LEU   B 1 43  ? 46.707 -15.495 5.707   1.00 12.59 ?  43  LEU   B CD2  1 
ATOM   4491 H H    . LEU   B 1 43  ? 47.247 -17.112 8.759   1.00 14.42 ?  43  LEU   B H    1 
ATOM   4492 H HA   . LEU   B 1 43  ? 48.410 -17.225 7.000   1.00 14.08 ?  43  LEU   B HA   1 
ATOM   4493 H HB2  . LEU   B 1 43  ? 49.259 -14.634 7.678   1.00 14.41 ?  43  LEU   B HB2  1 
ATOM   4494 H HB3  . LEU   B 1 43  ? 49.349 -15.270 6.232   1.00 14.41 ?  43  LEU   B HB3  1 
ATOM   4495 H HG   . LEU   B 1 43  ? 46.940 -14.530 7.493   1.00 14.89 ?  43  LEU   B HG   1 
ATOM   4496 H HD11 . LEU   B 1 43  ? 46.819 -12.825 5.899   1.00 16.17 ?  43  LEU   B HD11 1 
ATOM   4497 H HD12 . LEU   B 1 43  ? 48.122 -12.661 6.793   1.00 16.17 ?  43  LEU   B HD12 1 
ATOM   4498 H HD13 . LEU   B 1 43  ? 48.235 -13.265 5.328   1.00 16.17 ?  43  LEU   B HD13 1 
ATOM   4499 H HD21 . LEU   B 1 43  ? 45.903 -15.031 5.423   1.00 15.09 ?  43  LEU   B HD21 1 
ATOM   4500 H HD22 . LEU   B 1 43  ? 47.270 -15.679 4.938   1.00 15.09 ?  43  LEU   B HD22 1 
ATOM   4501 H HD23 . LEU   B 1 43  ? 46.470 -16.326 6.148   1.00 15.09 ?  43  LEU   B HD23 1 
ATOM   4502 N N    . LYS   B 1 44  ? 50.317 -18.254 8.642   1.00 12.40 ?  44  LYS   B N    1 
ATOM   4503 C CA   . LYS   B 1 44  ? 51.583 -18.932 8.886   1.00 12.85 ?  44  LYS   B CA   1 
ATOM   4504 C C    . LYS   B 1 44  ? 51.705 -20.051 7.858   1.00 12.60 ?  44  LYS   B C    1 
ATOM   4505 O O    . LYS   B 1 44  ? 51.006 -21.066 7.942   1.00 13.82 ?  44  LYS   B O    1 
ATOM   4506 C CB   . LYS   B 1 44  ? 51.628 -19.449 10.322  1.00 14.52 ?  44  LYS   B CB   1 
ATOM   4507 C CG   . LYS   B 1 44  ? 51.819 -18.346 11.351  1.00 17.22 ?  44  LYS   B CG   1 
ATOM   4508 C CD   . LYS   B 1 44  ? 53.015 -17.476 10.962  1.00 20.25 ?  44  LYS   B CD   1 
ATOM   4509 C CE   . LYS   B 1 44  ? 53.509 -16.616 12.089  1.00 23.05 ?  44  LYS   B CE   1 
ATOM   4510 N NZ   . LYS   B 1 44  ? 54.668 -15.781 11.702  1.00 24.53 ?  44  LYS   B NZ   1 
ATOM   4511 H H    . LYS   B 1 44  ? 49.641 -18.641 9.012   1.00 14.86 ?  44  LYS   B H    1 
ATOM   4512 H HA   . LYS   B 1 44  ? 52.314 -18.319 8.731   1.00 15.39 ?  44  LYS   B HA   1 
ATOM   4513 H HB2  . LYS   B 1 44  ? 50.784 -19.897 10.520  1.00 17.40 ?  44  LYS   B HB2  1 
ATOM   4514 H HB3  . LYS   B 1 44  ? 52.359 -20.075 10.410  1.00 17.40 ?  44  LYS   B HB3  1 
ATOM   4515 H HG2  . LYS   B 1 44  ? 51.026 -17.792 11.388  1.00 20.64 ?  44  LYS   B HG2  1 
ATOM   4516 H HG3  . LYS   B 1 44  ? 51.998 -18.746 12.221  1.00 20.64 ?  44  LYS   B HG3  1 
ATOM   4517 H HD2  . LYS   B 1 44  ? 53.738 -18.058 10.662  1.00 24.27 ?  44  LYS   B HD2  1 
ATOM   4518 H HD3  . LYS   B 1 44  ? 52.745 -16.889 10.237  1.00 24.27 ?  44  LYS   B HD3  1 
ATOM   4519 H HE2  . LYS   B 1 44  ? 52.800 -16.010 12.320  1.00 27.64 ?  44  LYS   B HE2  1 
ATOM   4520 H HE3  . LYS   B 1 44  ? 53.756 -17.175 12.846  1.00 27.64 ?  44  LYS   B HE3  1 
ATOM   4521 H HZ1  . LYS   B 1 44  ? 54.928 -15.282 12.392  1.00 29.41 ?  44  LYS   B HZ1  1 
ATOM   4522 H HZ2  . LYS   B 1 44  ? 55.347 -16.291 11.441  1.00 29.41 ?  44  LYS   B HZ2  1 
ATOM   4523 H HZ3  . LYS   B 1 44  ? 54.440 -15.239 11.029  1.00 29.41 ?  44  LYS   B HZ3  1 
ATOM   4524 N N    . HIS   B 1 45  ? 52.558 -19.834 6.860   1.00 12.12 ?  45  HIS   B N    1 
ATOM   4525 C CA   . HIS   B 1 45  ? 52.587 -20.668 5.659   1.00 12.42 ?  45  HIS   B CA   1 
ATOM   4526 C C    . HIS   B 1 45  ? 53.606 -21.790 5.827   1.00 14.52 ?  45  HIS   B C    1 
ATOM   4527 O O    . HIS   B 1 45  ? 54.673 -21.798 5.224   1.00 17.06 ?  45  HIS   B O    1 
ATOM   4528 C CB   . HIS   B 1 45  ? 52.904 -19.819 4.438   1.00 12.13 ?  45  HIS   B CB   1 
ATOM   4529 C CG   . HIS   B 1 45  ? 52.035 -18.612 4.321   1.00 12.13 ?  45  HIS   B CG   1 
ATOM   4530 N ND1  . HIS   B 1 45  ? 50.657 -18.687 4.279   1.00 12.39 ?  45  HIS   B ND1  1 
ATOM   4531 C CD2  . HIS   B 1 45  ? 52.350 -17.297 4.257   1.00 12.91 ?  45  HIS   B CD2  1 
ATOM   4532 C CE1  . HIS   B 1 45  ? 50.170 -17.464 4.178   1.00 11.88 ?  45  HIS   B CE1  1 
ATOM   4533 N NE2  . HIS   B 1 45  ? 51.172 -16.603 4.161   1.00 12.75 ?  45  HIS   B NE2  1 
ATOM   4534 H H    . HIS   B 1 45  ? 53.130 -19.188 6.849   1.00 14.52 ?  45  HIS   B H    1 
ATOM   4535 H HA   . HIS   B 1 45  ? 51.709 -21.064 5.529   1.00 14.88 ?  45  HIS   B HA   1 
ATOM   4536 H HB2  . HIS   B 1 45  ? 53.824 -19.525 4.488   1.00 14.54 ?  45  HIS   B HB2  1 
ATOM   4537 H HB3  . HIS   B 1 45  ? 52.775 -20.363 3.639   1.00 14.54 ?  45  HIS   B HB3  1 
ATOM   4538 H HD2  . HIS   B 1 45  ? 53.206 -16.933 4.271   1.00 15.47 ?  45  HIS   B HD2  1 
ATOM   4539 H HE1  . HIS   B 1 45  ? 49.266 -17.250 4.118   1.00 14.24 ?  45  HIS   B HE1  1 
ATOM   4540 H HE2  . HIS   B 1 45  ? 51.094 -15.750 4.109   1.00 15.28 ?  45  HIS   B HE2  1 
ATOM   4541 N N    A GLY   B 1 46  ? 53.233 -22.766 6.650   0.68 15.46 ?  46  GLY   B N    1 
ATOM   4542 N N    B GLY   B 1 46  ? 53.244 -22.752 6.668   0.32 15.57 ?  46  GLY   B N    1 
ATOM   4543 C CA   A GLY   B 1 46  ? 54.158 -23.820 7.025   0.68 17.45 ?  46  GLY   B CA   1 
ATOM   4544 C CA   B GLY   B 1 46  ? 54.165 -23.817 7.006   0.32 16.97 ?  46  GLY   B CA   1 
ATOM   4545 C C    A GLY   B 1 46  ? 54.208 -25.031 6.115   0.68 19.34 ?  46  GLY   B C    1 
ATOM   4546 C C    B GLY   B 1 46  ? 54.190 -24.963 6.016   0.32 18.38 ?  46  GLY   B C    1 
ATOM   4547 O O    A GLY   B 1 46  ? 55.286 -25.442 5.673   0.68 22.11 ?  46  GLY   B O    1 
ATOM   4548 O O    B GLY   B 1 46  ? 55.222 -25.236 5.394   0.32 19.38 ?  46  GLY   B O    1 
ATOM   4549 H H    A GLY   B 1 46  ? 52.455 -22.822 7.021   0.68 18.53 ?  46  GLY   B H    1 
ATOM   4550 H H    B GLY   B 1 46  ? 52.475 -22.801 7.059   0.32 18.66 ?  46  GLY   B H    1 
ATOM   4551 H HA2  A GLY   B 1 46  ? 55.051 -23.444 7.073   0.68 20.91 ?  46  GLY   B HA2  1 
ATOM   4552 H HA2  B GLY   B 1 46  ? 55.060 -23.448 7.062   0.32 20.34 ?  46  GLY   B HA2  1 
ATOM   4553 H HA3  A GLY   B 1 46  ? 53.922 -24.137 7.910   0.68 20.91 ?  46  GLY   B HA3  1 
ATOM   4554 H HA3  B GLY   B 1 46  ? 53.930 -24.167 7.879   0.32 20.34 ?  46  GLY   B HA3  1 
ATOM   4555 N N    . GLY   B 1 47  ? 53.052 -25.634 5.844   1.00 18.82 ?  47  GLY   B N    1 
ATOM   4556 C CA   . GLY   B 1 47  ? 52.995 -26.894 5.134   1.00 16.43 ?  47  GLY   B CA   1 
ATOM   4557 C C    . GLY   B 1 47  ? 52.080 -26.862 3.926   1.00 14.09 ?  47  GLY   B C    1 
ATOM   4558 O O    . GLY   B 1 47  ? 51.435 -25.854 3.633   1.00 14.34 ?  47  GLY   B O    1 
ATOM   4559 H H    A GLY   B 1 47  ? 52.280 -25.337 6.091   0.68 22.56 ?  47  GLY   B H    1 
ATOM   4560 H H    B GLY   B 1 47  ? 52.286 -25.367 6.140   0.32 22.56 ?  47  GLY   B H    1 
ATOM   4561 H HA2  . GLY   B 1 47  ? 53.883 -27.139 4.833   1.00 19.70 ?  47  GLY   B HA2  1 
ATOM   4562 H HA3  . GLY   B 1 47  ? 52.679 -27.584 5.738   1.00 19.70 ?  47  GLY   B HA3  1 
ATOM   4563 N N    . GLY   B 1 48  ? 52.028 -28.001 3.236   1.00 13.07 ?  48  GLY   B N    1 
ATOM   4564 C CA   . GLY   B 1 48  ? 51.093 -28.147 2.139   1.00 12.84 ?  48  GLY   B CA   1 
ATOM   4565 C C    . GLY   B 1 48  ? 51.243 -27.043 1.116   1.00 12.08 ?  48  GLY   B C    1 
ATOM   4566 O O    . GLY   B 1 48  ? 52.352 -26.588 0.808   1.00 12.89 ?  48  GLY   B O    1 
ATOM   4567 H H    . GLY   B 1 48  ? 52.530 -28.682 3.375   1.00 15.66 ?  48  GLY   B H    1 
ATOM   4568 H HA2  . GLY   B 1 48  ? 51.233 -28.999 1.700   1.00 15.39 ?  48  GLY   B HA2  1 
ATOM   4569 H HA3  . GLY   B 1 48  ? 50.184 -28.124 2.483   1.00 15.39 ?  48  GLY   B HA3  1 
ATOM   4570 N N    . VAL   B 1 49  ? 50.100 -26.605 0.580   1.00 12.36 ?  49  VAL   B N    1 
ATOM   4571 C CA   . VAL   B 1 49  ? 50.085 -25.583 -0.466  1.00 12.09 ?  49  VAL   B CA   1 
ATOM   4572 C C    . VAL   B 1 49  ? 50.745 -24.296 0.019   1.00 11.59 ?  49  VAL   B C    1 
ATOM   4573 O O    . VAL   B 1 49  ? 51.535 -23.678 -0.703  1.00 12.25 ?  49  VAL   B O    1 
ATOM   4574 C CB   . VAL   B 1 49  ? 48.643 -25.329 -0.946  1.00 13.51 ?  49  VAL   B CB   1 
ATOM   4575 C CG1  . VAL   B 1 49  ? 48.574 -24.074 -1.813  1.00 13.53 ?  49  VAL   B CG1  1 
ATOM   4576 C CG2  . VAL   B 1 49  ? 48.109 -26.530 -1.703  1.00 15.30 ?  49  VAL   B CG2  1 
ATOM   4577 H H    . VAL   B 1 49  ? 49.312 -26.876 0.809   1.00 14.80 ?  49  VAL   B H    1 
ATOM   4578 H HA   . VAL   B 1 49  ? 50.593 -25.905 -1.226  1.00 14.48 ?  49  VAL   B HA   1 
ATOM   4579 H HB   . VAL   B 1 49  ? 48.075 -25.182 -0.175  1.00 16.19 ?  49  VAL   B HB   1 
ATOM   4580 H HG11 . VAL   B 1 49  ? 47.747 -24.090 -2.320  1.00 16.22 ?  49  VAL   B HG11 1 
ATOM   4581 H HG12 . VAL   B 1 49  ? 48.595 -23.289 -1.243  1.00 16.22 ?  49  VAL   B HG12 1 
ATOM   4582 H HG13 . VAL   B 1 49  ? 49.332 -24.067 -2.419  1.00 16.22 ?  49  VAL   B HG13 1 
ATOM   4583 H HG21 . VAL   B 1 49  ? 47.201 -26.348 -1.990  1.00 18.34 ?  49  VAL   B HG21 1 
ATOM   4584 H HG22 . VAL   B 1 49  ? 48.673 -26.690 -2.480  1.00 18.34 ?  49  VAL   B HG22 1 
ATOM   4585 H HG23 . VAL   B 1 49  ? 48.125 -27.303 -1.120  1.00 18.34 ?  49  VAL   B HG23 1 
ATOM   4586 N N    . ALA   B 1 50  ? 50.402 -23.850 1.229   1.00 11.27 ?  50  ALA   B N    1 
ATOM   4587 C CA   . ALA   B 1 50  ? 50.925 -22.574 1.706   1.00 11.00 ?  50  ALA   B CA   1 
ATOM   4588 C C    . ALA   B 1 50  ? 52.443 -22.610 1.819   1.00 11.46 ?  50  ALA   B C    1 
ATOM   4589 O O    . ALA   B 1 50  ? 53.125 -21.647 1.456   1.00 11.74 ?  50  ALA   B O    1 
ATOM   4590 C CB   . ALA   B 1 50  ? 50.297 -22.209 3.052   1.00 11.92 ?  50  ALA   B CB   1 
ATOM   4591 H H    . ALA   B 1 50  ? 49.884 -24.258 1.780   1.00 13.50 ?  50  ALA   B H    1 
ATOM   4592 H HA   . ALA   B 1 50  ? 50.699 -21.880 1.072   1.00 13.18 ?  50  ALA   B HA   1 
ATOM   4593 H HB1  . ALA   B 1 50  ? 50.659 -21.355 3.350   1.00 14.28 ?  50  ALA   B HB1  1 
ATOM   4594 H HB2  . ALA   B 1 50  ? 49.338 -22.138 2.943   1.00 14.28 ?  50  ALA   B HB2  1 
ATOM   4595 H HB3  . ALA   B 1 50  ? 50.510 -22.898 3.700   1.00 14.28 ?  50  ALA   B HB3  1 
ATOM   4596 N N    . GLY   B 1 51  ? 52.992 -23.702 2.338   1.00 11.97 ?  51  GLY   B N    1 
ATOM   4597 C CA   . GLY   B 1 51  ? 54.437 -23.807 2.406   1.00 12.62 ?  51  GLY   B CA   1 
ATOM   4598 C C    . GLY   B 1 51  ? 55.080 -23.759 1.036   1.00 12.33 ?  51  GLY   B C    1 
ATOM   4599 O O    . GLY   B 1 51  ? 56.121 -23.123 0.849   1.00 13.66 ?  51  GLY   B O    1 
ATOM   4600 H H    . GLY   B 1 51  ? 52.567 -24.382 2.647   1.00 14.34 ?  51  GLY   B H    1 
ATOM   4601 H HA2  . GLY   B 1 51  ? 54.793 -23.074 2.934   1.00 15.12 ?  51  GLY   B HA2  1 
ATOM   4602 H HA3  . GLY   B 1 51  ? 54.687 -24.642 2.829   1.00 15.12 ?  51  GLY   B HA3  1 
ATOM   4603 N N    . ALA   B 1 52  ? 54.472 -24.424 0.056   1.00 12.13 ?  52  ALA   B N    1 
ATOM   4604 C CA   . ALA   B 1 52  ? 55.040 -24.432 -1.286  1.00 12.77 ?  52  ALA   B CA   1 
ATOM   4605 C C    . ALA   B 1 52  ? 54.959 -23.053 -1.932  1.00 12.17 ?  52  ALA   B C    1 
ATOM   4606 O O    . ALA   B 1 52  ? 55.932 -22.600 -2.557  1.00 13.05 ?  52  ALA   B O    1 
ATOM   4607 C CB   . ALA   B 1 52  ? 54.339 -25.477 -2.145  1.00 13.29 ?  52  ALA   B CB   1 
ATOM   4608 H H    . ALA   B 1 52  ? 53.736 -24.862 0.138   1.00 14.54 ?  52  ALA   B H    1 
ATOM   4609 H HA   . ALA   B 1 52  ? 55.975 -24.673 -1.225  1.00 15.30 ?  52  ALA   B HA   1 
ATOM   4610 H HB1  . ALA   B 1 52  ? 54.734 -25.471 -3.033  1.00 15.93 ?  52  ALA   B HB1  1 
ATOM   4611 H HB2  . ALA   B 1 52  ? 54.462 -26.351 -1.738  1.00 15.93 ?  52  ALA   B HB2  1 
ATOM   4612 H HB3  . ALA   B 1 52  ? 53.397 -25.266 -2.200  1.00 15.93 ?  52  ALA   B HB3  1 
ATOM   4613 N N    . LEU   B 1 53  ? 53.812 -22.373 -1.813  1.00 11.69 ?  53  LEU   B N    1 
ATOM   4614 C CA   . LEU   B 1 53  ? 53.703 -21.034 -2.388  1.00 11.66 ?  53  LEU   B CA   1 
ATOM   4615 C C    . LEU   B 1 53  ? 54.711 -20.091 -1.743  1.00 11.60 ?  53  LEU   B C    1 
ATOM   4616 O O    . LEU   B 1 53  ? 55.419 -19.343 -2.433  1.00 12.45 ?  53  LEU   B O    1 
ATOM   4617 C CB   . LEU   B 1 53  ? 52.278 -20.497 -2.225  1.00 12.54 ?  53  LEU   B CB   1 
ATOM   4618 C CG   . LEU   B 1 53  ? 51.151 -21.221 -2.965  1.00 12.55 ?  53  LEU   B CG   1 
ATOM   4619 C CD1  . LEU   B 1 53  ? 49.820 -20.593 -2.605  1.00 14.40 ?  53  LEU   B CD1  1 
ATOM   4620 C CD2  . LEU   B 1 53  ? 51.359 -21.201 -4.472  1.00 14.38 ?  53  LEU   B CD2  1 
ATOM   4621 H H    . LEU   B 1 53  ? 53.106 -22.656 -1.410  1.00 14.00 ?  53  LEU   B H    1 
ATOM   4622 H HA   . LEU   B 1 53  ? 53.902 -21.086 -3.341  1.00 13.97 ?  53  LEU   B HA   1 
ATOM   4623 H HB2  . LEU   B 1 53  ? 52.059 -20.525 -1.285  1.00 15.03 ?  53  LEU   B HB2  1 
ATOM   4624 H HB3  . LEU   B 1 53  ? 52.271 -19.582 -2.534  1.00 15.03 ?  53  LEU   B HB3  1 
ATOM   4625 H HG   . LEU   B 1 53  ? 51.124 -22.147 -2.678  1.00 15.03 ?  53  LEU   B HG   1 
ATOM   4626 H HD11 . LEU   B 1 53  ? 49.109 -21.060 -3.076  1.00 17.25 ?  53  LEU   B HD11 1 
ATOM   4627 H HD12 . LEU   B 1 53  ? 49.681 -20.671 -1.646  1.00 17.25 ?  53  LEU   B HD12 1 
ATOM   4628 H HD13 . LEU   B 1 53  ? 49.827 -19.659 -2.861  1.00 17.25 ?  53  LEU   B HD13 1 
ATOM   4629 H HD21 . LEU   B 1 53  ? 50.639 -21.694 -4.899  1.00 17.23 ?  53  LEU   B HD21 1 
ATOM   4630 H HD22 . LEU   B 1 53  ? 51.355 -20.283 -4.781  1.00 17.23 ?  53  LEU   B HD22 1 
ATOM   4631 H HD23 . LEU   B 1 53  ? 52.209 -21.619 -4.680  1.00 17.23 ?  53  LEU   B HD23 1 
ATOM   4632 N N    . ASN   B 1 54  ? 54.804 -20.120 -0.417  1.00 11.27 ?  54  ASN   B N    1 
ATOM   4633 C CA   . ASN   B 1 54  ? 55.719 -19.207 0.254   1.00 11.83 ?  54  ASN   B CA   1 
ATOM   4634 C C    . ASN   B 1 54  ? 57.163 -19.487 -0.137  1.00 12.74 ?  54  ASN   B C    1 
ATOM   4635 O O    . ASN   B 1 54  ? 57.938 -18.551 -0.375  1.00 12.94 ?  54  ASN   B O    1 
ATOM   4636 C CB   . ASN   B 1 54  ? 55.551 -19.279 1.763   1.00 13.04 ?  54  ASN   B CB   1 
ATOM   4637 C CG   . ASN   B 1 54  ? 56.532 -18.368 2.476   1.00 13.00 ?  54  ASN   B CG   1 
ATOM   4638 O OD1  . ASN   B 1 54  ? 56.550 -17.156 2.241   1.00 13.27 ?  54  ASN   B OD1  1 
ATOM   4639 N ND2  . ASN   B 1 54  ? 57.383 -18.947 3.316   1.00 14.53 ?  54  ASN   B ND2  1 
ATOM   4640 H H    . ASN   B 1 54  ? 54.359 -20.644 0.101   1.00 13.50 ?  54  ASN   B H    1 
ATOM   4641 H HA   . ASN   B 1 54  ? 55.504 -18.301 -0.023  1.00 14.18 ?  54  ASN   B HA   1 
ATOM   4642 H HB2  . ASN   B 1 54  ? 54.650 -19.001 2.000   1.00 15.62 ?  54  ASN   B HB2  1 
ATOM   4643 H HB3  . ASN   B 1 54  ? 55.709 -20.187 2.060   1.00 15.62 ?  54  ASN   B HB3  1 
ATOM   4644 H HD21 . ASN   B 1 54  ? 57.965 -18.470 3.736   1.00 17.41 ?  54  ASN   B HD21 1 
ATOM   4645 H HD22 . ASN   B 1 54  ? 57.355 -19.797 3.442   1.00 17.41 ?  54  ASN   B HD22 1 
ATOM   4646 N N    . LYS   B 1 55  ? 57.547 -20.765 -0.196  1.00 12.94 ?  55  LYS   B N    1 
ATOM   4647 C CA   . LYS   B 1 55  ? 58.900 -21.110 -0.616  1.00 14.15 ?  55  LYS   B CA   1 
ATOM   4648 C C    . LYS   B 1 55  ? 59.193 -20.567 -2.009  1.00 13.99 ?  55  LYS   B C    1 
ATOM   4649 O O    . LYS   B 1 55  ? 60.291 -20.062 -2.266  1.00 14.72 ?  55  LYS   B O    1 
ATOM   4650 C CB   . LYS   B 1 55  ? 59.095 -22.627 -0.567  1.00 15.87 ?  55  LYS   B CB   1 
ATOM   4651 C CG   . LYS   B 1 55  ? 60.483 -23.083 -0.982  1.00 19.88 ?  55  LYS   B CG   1 
ATOM   4652 C CD   . LYS   B 1 55  ? 60.659 -24.581 -0.803  1.00 23.38 ?  55  LYS   B CD   1 
ATOM   4653 C CE   . LYS   B 1 55  ? 60.672 -24.982 0.671   1.00 26.17 ?  55  LYS   B CE   1 
ATOM   4654 N NZ   . LYS   B 1 55  ? 61.040 -26.409 0.859   1.00 27.60 ?  55  LYS   B NZ   1 
ATOM   4655 H H    . LYS   B 1 55  ? 57.041 -21.436 -0.009  1.00 15.50 ?  55  LYS   B H    1 
ATOM   4656 H HA   . LYS   B 1 55  ? 59.528 -20.706 -0.001  1.00 16.96 ?  55  LYS   B HA   1 
ATOM   4657 H HB2  . LYS   B 1 55  ? 58.939 -22.924 0.343   1.00 19.02 ?  55  LYS   B HB2  1 
ATOM   4658 H HB3  . LYS   B 1 55  ? 58.454 -23.043 -1.163  1.00 19.02 ?  55  LYS   B HB3  1 
ATOM   4659 H HG2  . LYS   B 1 55  ? 60.622 -22.872 -1.919  1.00 23.84 ?  55  LYS   B HG2  1 
ATOM   4660 H HG3  . LYS   B 1 55  ? 61.144 -22.629 -0.435  1.00 23.84 ?  55  LYS   B HG3  1 
ATOM   4661 H HD2  . LYS   B 1 55  ? 59.925 -25.047 -1.234  1.00 28.03 ?  55  LYS   B HD2  1 
ATOM   4662 H HD3  . LYS   B 1 55  ? 61.505 -24.855 -1.194  1.00 28.03 ?  55  LYS   B HD3  1 
ATOM   4663 H HE2  . LYS   B 1 55  ? 61.319 -24.430 1.141   1.00 31.38 ?  55  LYS   B HE2  1 
ATOM   4664 H HE3  . LYS   B 1 55  ? 59.785 -24.841 1.044   1.00 31.38 ?  55  LYS   B HE3  1 
ATOM   4665 H HZ1  . LYS   B 1 55  ? 61.005 -26.616 1.724   1.00 33.10 ?  55  LYS   B HZ1  1 
ATOM   4666 H HZ2  . LYS   B 1 55  ? 60.469 -26.926 0.414   1.00 33.10 ?  55  LYS   B HZ2  1 
ATOM   4667 H HZ3  . LYS   B 1 55  ? 61.861 -26.551 0.557   1.00 33.10 ?  55  LYS   B HZ3  1 
ATOM   4668 N N    . ALA   B 1 56  ? 58.220 -20.651 -2.922  1.00 13.33 ?  56  ALA   B N    1 
ATOM   4669 C CA   . ALA   B 1 56  ? 58.444 -20.148 -4.272  1.00 14.44 ?  56  ALA   B CA   1 
ATOM   4670 C C    . ALA   B 1 56  ? 58.718 -18.650 -4.273  1.00 14.03 ?  56  ALA   B C    1 
ATOM   4671 O O    . ALA   B 1 56  ? 59.453 -18.154 -5.139  1.00 15.16 ?  56  ALA   B O    1 
ATOM   4672 C CB   . ALA   B 1 56  ? 57.258 -20.487 -5.172  1.00 15.41 ?  56  ALA   B CB   1 
ATOM   4673 H H    . ALA   B 1 56  ? 57.432 -20.973 -2.784  1.00 15.97 ?  56  ALA   B H    1 
ATOM   4674 H HA   . ALA   B 1 56  ? 59.226 -20.581 -4.638  1.00 17.30 ?  56  ALA   B HA   1 
ATOM   4675 H HB1  . ALA   B 1 56  ? 57.435 -20.152 -6.068  1.00 18.46 ?  56  ALA   B HB1  1 
ATOM   4676 H HB2  . ALA   B 1 56  ? 57.151 -21.451 -5.197  1.00 18.46 ?  56  ALA   B HB2  1 
ATOM   4677 H HB3  . ALA   B 1 56  ? 56.458 -20.073 -4.817  1.00 18.46 ?  56  ALA   B HB3  1 
ATOM   4678 N N    . THR   B 1 57  ? 58.157 -17.917 -3.311  1.00 13.59 ?  57  THR   B N    1 
ATOM   4679 C CA   . THR   B 1 57  ? 58.396 -16.482 -3.192  1.00 13.81 ?  57  THR   B CA   1 
ATOM   4680 C C    . THR   B 1 57  ? 59.646 -16.156 -2.382  1.00 14.53 ?  57  THR   B C    1 
ATOM   4681 O O    . THR   B 1 57  ? 59.874 -14.983 -2.062  1.00 14.84 ?  57  THR   B O    1 
ATOM   4682 C CB   . THR   B 1 57  ? 57.192 -15.756 -2.558  1.00 13.35 ?  57  THR   B CB   1 
ATOM   4683 O OG1  . THR   B 1 57  ? 57.166 -15.970 -1.140  1.00 13.56 ?  57  THR   B OG1  1 
ATOM   4684 C CG2  . THR   B 1 57  ? 55.868 -16.174 -3.201  1.00 13.14 ?  57  THR   B CG2  1 
ATOM   4685 H H    . THR   B 1 57  ? 57.615 -18.225 -2.718  1.00 16.28 ?  57  THR   B H    1 
ATOM   4686 H HA   . THR   B 1 57  ? 58.515 -16.114 -4.084  1.00 16.55 ?  57  THR   B HA   1 
ATOM   4687 H HB   . THR   B 1 57  ? 57.294 -14.804 -2.722  1.00 16.00 ?  57  THR   B HB   1 
ATOM   4688 H HG1  . THR   B 1 57  ? 57.101 -16.790 -0.977  1.00 16.24 ?  57  THR   B HG1  1 
ATOM   4689 H HG21 . THR   B 1 57  ? 55.141 -15.642 -2.842  1.00 15.74 ?  57  THR   B HG21 1 
ATOM   4690 H HG22 . THR   B 1 57  ? 55.908 -16.047 -4.162  1.00 15.74 ?  57  THR   B HG22 1 
ATOM   4691 H HG23 . THR   B 1 57  ? 55.691 -17.110 -3.017  1.00 15.74 ?  57  THR   B HG23 1 
ATOM   4692 N N    . ASN   B 1 58  ? 60.446 -17.157 -2.028  1.00 15.29 ?  58  ASN   B N    1 
ATOM   4693 C CA   . ASN   B 1 58  ? 61.640 -16.937 -1.218  1.00 18.04 ?  58  ASN   B CA   1 
ATOM   4694 C C    . ASN   B 1 58  ? 61.299 -16.226 0.093   1.00 15.80 ?  58  ASN   B C    1 
ATOM   4695 O O    . ASN   B 1 58  ? 62.038 -15.355 0.562   1.00 16.67 ?  58  ASN   B O    1 
ATOM   4696 C CB   . ASN   B 1 58  ? 62.724 -16.185 -1.997  1.00 25.32 ?  58  ASN   B CB   1 
ATOM   4697 C CG   . ASN   B 1 58  ? 64.095 -16.318 -1.361  1.00 33.50 ?  58  ASN   B CG   1 
ATOM   4698 O OD1  . ASN   B 1 58  ? 64.401 -17.327 -0.727  1.00 36.33 ?  58  ASN   B OD1  1 
ATOM   4699 N ND2  . ASN   B 1 58  ? 64.928 -15.295 -1.525  1.00 38.08 ?  58  ASN   B ND2  1 
ATOM   4700 H H    . ASN   B 1 58  ? 60.316 -17.984 -2.244  1.00 18.32 ?  58  ASN   B H    1 
ATOM   4701 H HA   . ASN   B 1 58  ? 62.008 -17.808 -0.993  1.00 21.62 ?  58  ASN   B HA   1 
ATOM   4702 H HB2  . ASN   B 1 58  ? 62.776 -16.544 -2.900  1.00 30.36 ?  58  ASN   B HB2  1 
ATOM   4703 H HB3  . ASN   B 1 58  ? 62.500 -15.244 -2.027  1.00 30.36 ?  58  ASN   B HB3  1 
ATOM   4704 H HD21 . ASN   B 1 58  ? 65.718 -15.323 -1.184  1.00 45.67 ?  58  ASN   B HD21 1 
ATOM   4705 H HD22 . ASN   B 1 58  ? 64.678 -14.604 -1.972  1.00 45.67 ?  58  ASN   B HD22 1 
ATOM   4706 N N    . ASN   B 1 59  ? 60.175 -16.614 0.699   1.00 14.64 ?  59  ASN   B N    1 
ATOM   4707 C CA   . ASN   B 1 59  ? 59.702 -16.148 2.005   1.00 14.61 ?  59  ASN   B CA   1 
ATOM   4708 C C    . ASN   B 1 59  ? 59.100 -14.745 1.950   1.00 14.05 ?  59  ASN   B C    1 
ATOM   4709 O O    . ASN   B 1 59  ? 58.665 -14.241 2.994   1.00 14.33 ?  59  ASN   B O    1 
ATOM   4710 C CB   . ASN   B 1 59  ? 60.773 -16.210 3.109   1.00 15.67 ?  59  ASN   B CB   1 
ATOM   4711 C CG   . ASN   B 1 59  ? 60.181 -16.378 4.488   1.00 17.18 ?  59  ASN   B CG   1 
ATOM   4712 O OD1  . ASN   B 1 59  ? 59.348 -17.256 4.714   1.00 17.24 ?  59  ASN   B OD1  1 
ATOM   4713 N ND2  . ASN   B 1 59  ? 60.604 -15.537 5.421   1.00 17.89 ?  59  ASN   B ND2  1 
ATOM   4714 H H    . ASN   B 1 59  ? 59.636 -17.190 0.350   1.00 17.54 ?  59  ASN   B H    1 
ATOM   4715 H HA   . ASN   B 1 59  ? 58.994 -16.748 2.283   1.00 17.51 ?  59  ASN   B HA   1 
ATOM   4716 H HB2  . ASN   B 1 59  ? 61.360 -16.966 2.950   1.00 18.78 ?  59  ASN   B HB2  1 
ATOM   4717 H HB3  . ASN   B 1 59  ? 61.283 -15.387 3.108   1.00 18.78 ?  59  ASN   B HB3  1 
ATOM   4718 H HD21 . ASN   B 1 59  ? 60.298 -15.592 6.226   1.00 21.45 ?  59  ASN   B HD21 1 
ATOM   4719 H HD22 . ASN   B 1 59  ? 61.190 -14.938 5.228   1.00 21.45 ?  59  ASN   B HD22 1 
ATOM   4720 N N    . ALA   B 1 60  ? 59.045 -14.099 0.783   1.00 14.04 ?  60  ALA   B N    1 
ATOM   4721 C CA   . ALA   B 1 60  ? 58.451 -12.767 0.709   1.00 13.90 ?  60  ALA   B CA   1 
ATOM   4722 C C    . ALA   B 1 60  ? 56.981 -12.792 1.105   1.00 13.06 ?  60  ALA   B C    1 
ATOM   4723 O O    . ALA   B 1 60  ? 56.477 -11.840 1.716   1.00 13.73 ?  60  ALA   B O    1 
ATOM   4724 C CB   . ALA   B 1 60  ? 58.612 -12.199 -0.700  1.00 15.29 ?  60  ALA   B CB   1 
ATOM   4725 H H    . ALA   B 1 60  ? 59.347 -14.407 0.039   1.00 16.83 ?  60  ALA   B H    1 
ATOM   4726 H HA   . ALA   B 1 60  ? 58.917 -12.184 1.327   1.00 16.66 ?  60  ALA   B HA   1 
ATOM   4727 H HB1  . ALA   B 1 60  ? 58.214 -11.317 -0.728  1.00 18.33 ?  60  ALA   B HB1  1 
ATOM   4728 H HB2  . ALA   B 1 60  ? 59.560 -12.142 -0.910  1.00 18.33 ?  60  ALA   B HB2  1 
ATOM   4729 H HB3  . ALA   B 1 60  ? 58.170 -12.787 -1.330  1.00 18.33 ?  60  ALA   B HB3  1 
ATOM   4730 N N    . MET   B 1 61  ? 56.272 -13.871 0.759   1.00 12.64 ?  61  MET   B N    1 
ATOM   4731 C CA   . MET   B 1 61  ? 54.874 -13.993 1.151   1.00 12.14 ?  61  MET   B CA   1 
ATOM   4732 C C    . MET   B 1 61  ? 54.732 -14.006 2.670   1.00 12.19 ?  61  MET   B C    1 
ATOM   4733 O O    . MET   B 1 61  ? 53.827 -13.363 3.222   1.00 12.10 ?  61  MET   B O    1 
ATOM   4734 C CB   . MET   B 1 61  ? 54.293 -15.262 0.525   1.00 12.30 ?  61  MET   B CB   1 
ATOM   4735 C CG   . MET   B 1 61  ? 52.852 -15.556 0.940   1.00 12.20 ?  61  MET   B CG   1 
ATOM   4736 S SD   . MET   B 1 61  ? 52.205 -17.058 0.176   1.00 12.75 ?  61  MET   B SD   1 
ATOM   4737 C CE   . MET   B 1 61  ? 51.965 -16.465 -1.494  1.00 13.78 ?  61  MET   B CE   1 
ATOM   4738 H H    . MET   B 1 61  ? 56.577 -14.541 0.304   1.00 15.14 ?  61  MET   B H    1 
ATOM   4739 H HA   . MET   B 1 61  ? 54.383 -13.239 0.789   1.00 14.55 ?  61  MET   B HA   1 
ATOM   4740 H HB2  . MET   B 1 61  ? 54.307 -15.173 -0.444  1.00 14.74 ?  61  MET   B HB2  1 
ATOM   4741 H HB3  . MET   B 1 61  ? 54.839 -16.022 0.787   1.00 14.74 ?  61  MET   B HB3  1 
ATOM   4742 H HG2  . MET   B 1 61  ? 52.815 -15.678 1.903   1.00 14.62 ?  61  MET   B HG2  1 
ATOM   4743 H HG3  . MET   B 1 61  ? 52.286 -14.816 0.676   1.00 14.62 ?  61  MET   B HG3  1 
ATOM   4744 H HE1  . MET   B 1 61  ? 51.569 -17.169 -2.023  1.00 16.51 ?  61  MET   B HE1  1 
ATOM   4745 H HE2  . MET   B 1 61  ? 51.378 -15.691 -1.472  1.00 16.51 ?  61  MET   B HE2  1 
ATOM   4746 H HE3  . MET   B 1 61  ? 52.826 -16.210 -1.867  1.00 16.51 ?  61  MET   B HE3  1 
ATOM   4747 N N    . GLN   B 1 62  ? 55.618 -14.722 3.369   1.00 12.34 ?  62  GLN   B N    1 
ATOM   4748 C CA   . GLN   B 1 62  ? 55.510 -14.780 4.823   1.00 12.76 ?  62  GLN   B CA   1 
ATOM   4749 C C    . GLN   B 1 62  ? 55.788 -13.422 5.457   1.00 12.92 ?  62  GLN   B C    1 
ATOM   4750 O O    . GLN   B 1 62  ? 55.103 -13.022 6.407   1.00 13.43 ?  62  GLN   B O    1 
ATOM   4751 C CB   . GLN   B 1 62  ? 56.465 -15.830 5.388   1.00 13.10 ?  62  GLN   B CB   1 
ATOM   4752 C CG   . GLN   B 1 62  ? 56.234 -16.102 6.866   1.00 13.54 ?  62  GLN   B CG   1 
ATOM   4753 C CD   . GLN   B 1 62  ? 54.859 -16.696 7.108   1.00 13.22 ?  62  GLN   B CD   1 
ATOM   4754 O OE1  . GLN   B 1 62  ? 54.601 -17.849 6.764   1.00 13.34 ?  62  GLN   B OE1  1 
ATOM   4755 N NE2  . GLN   B 1 62  ? 53.953 -15.896 7.664   1.00 13.57 ?  62  GLN   B NE2  1 
ATOM   4756 H H    . GLN   B 1 62  ? 56.269 -15.174 3.029   1.00 14.78 ?  62  GLN   B H    1 
ATOM   4757 H HA   . GLN   B 1 62  ? 54.606 -15.038 5.054   1.00 15.29 ?  62  GLN   B HA   1 
ATOM   4758 H HB2  . GLN   B 1 62  ? 56.344 -16.663 4.908   1.00 15.70 ?  62  GLN   B HB2  1 
ATOM   4759 H HB3  . GLN   B 1 62  ? 57.379 -15.517 5.281   1.00 15.70 ?  62  GLN   B HB3  1 
ATOM   4760 H HG2  . GLN   B 1 62  ? 56.899 -16.737 7.178   1.00 16.22 ?  62  GLN   B HG2  1 
ATOM   4761 H HG3  . GLN   B 1 62  ? 56.304 -15.273 7.361   1.00 16.22 ?  62  GLN   B HG3  1 
ATOM   4762 H HE21 . GLN   B 1 62  ? 54.162 -15.090 7.877   1.00 16.26 ?  62  GLN   B HE21 1 
ATOM   4763 H HE22 . GLN   B 1 62  ? 53.158 -16.188 7.809   1.00 16.26 ?  62  GLN   B HE22 1 
ATOM   4764 N N    . VAL   B 1 63  ? 56.807 -12.709 4.970   1.00 13.27 ?  63  VAL   B N    1 
ATOM   4765 C CA   . VAL   B 1 63  ? 57.109 -11.389 5.522   1.00 14.22 ?  63  VAL   B CA   1 
ATOM   4766 C C    . VAL   B 1 63  ? 55.915 -10.457 5.340   1.00 13.53 ?  63  VAL   B C    1 
ATOM   4767 O O    . VAL   B 1 63  ? 55.496 -9.756  6.272   1.00 14.47 ?  63  VAL   B O    1 
ATOM   4768 C CB   . VAL   B 1 63  ? 58.399 -10.826 4.899   1.00 15.78 ?  63  VAL   B CB   1 
ATOM   4769 C CG1  . VAL   B 1 63  ? 58.630 -9.381  5.353   1.00 16.53 ?  63  VAL   B CG1  1 
ATOM   4770 C CG2  . VAL   B 1 63  ? 59.587 -11.706 5.278   1.00 16.53 ?  63  VAL   B CG2  1 
ATOM   4771 H H    . VAL   B 1 63  ? 57.324 -12.962 4.328   1.00 15.90 ?  63  VAL   B H    1 
ATOM   4772 H HA   . VAL   B 1 63  ? 57.264 -11.487 6.472   1.00 17.04 ?  63  VAL   B HA   1 
ATOM   4773 H HB   . VAL   B 1 63  ? 58.321 -10.836 3.933   1.00 18.92 ?  63  VAL   B HB   1 
ATOM   4774 H HG11 . VAL   B 1 63  ? 59.543 -9.131  5.151   1.00 19.81 ?  63  VAL   B HG11 1 
ATOM   4775 H HG12 . VAL   B 1 63  ? 58.013 -8.802  4.882   1.00 19.81 ?  63  VAL   B HG12 1 
ATOM   4776 H HG13 . VAL   B 1 63  ? 58.476 -9.326  6.310   1.00 19.81 ?  63  VAL   B HG13 1 
ATOM   4777 H HG21 . VAL   B 1 63  ? 60.397 -11.325 4.902   1.00 19.81 ?  63  VAL   B HG21 1 
ATOM   4778 H HG22 . VAL   B 1 63  ? 59.661 -11.737 6.248   1.00 19.81 ?  63  VAL   B HG22 1 
ATOM   4779 H HG23 . VAL   B 1 63  ? 59.449 -12.599 4.930   1.00 19.81 ?  63  VAL   B HG23 1 
ATOM   4780 N N    . GLU   B 1 64  ? 55.351 -10.435 4.132   1.00 13.22 ?  64  GLU   B N    1 
ATOM   4781 C CA   . GLU   B 1 64  ? 54.183 -9.599  3.862   1.00 12.91 ?  64  GLU   B CA   1 
ATOM   4782 C C    . GLU   B 1 64  ? 53.001 -10.002 4.739   1.00 12.37 ?  64  GLU   B C    1 
ATOM   4783 O O    . GLU   B 1 64  ? 52.254 -9.142  5.237   1.00 13.43 ?  64  GLU   B O    1 
ATOM   4784 C CB   . GLU   B 1 64  ? 53.821 -9.737  2.382   1.00 13.15 ?  64  GLU   B CB   1 
ATOM   4785 C CG   . GLU   B 1 64  ? 52.564 -8.995  1.952   1.00 13.18 ?  64  GLU   B CG   1 
ATOM   4786 C CD   . GLU   B 1 64  ? 52.017 -9.493  0.620   1.00 13.98 ?  64  GLU   B CD   1 
ATOM   4787 O OE1  . GLU   B 1 64  ? 52.197 -10.697 0.299   1.00 15.06 ?  64  GLU   B OE1  1 
ATOM   4788 O OE2  . GLU   B 1 64  ? 51.385 -8.680  -0.099  1.00 14.96 -1 64  GLU   B OE2  1 
ATOM   4789 H H    . GLU   B 1 64  ? 55.627 -10.895 3.452   1.00 15.84 ?  64  GLU   B H    1 
ATOM   4790 H HA   . GLU   B 1 64  ? 54.400 -8.675  4.041   1.00 15.47 ?  64  GLU   B HA   1 
ATOM   4791 H HB2  . GLU   B 1 64  ? 54.557 -9.383  1.848   1.00 15.76 ?  64  GLU   B HB2  1 
ATOM   4792 H HB3  . GLU   B 1 64  ? 53.696 -10.672 2.176   1.00 15.76 ?  64  GLU   B HB3  1 
ATOM   4793 H HG2  . GLU   B 1 64  ? 51.868 -9.115  2.619   1.00 15.80 ?  64  GLU   B HG2  1 
ATOM   4794 H HG3  . GLU   B 1 64  ? 52.768 -8.050  1.859   1.00 15.80 ?  64  GLU   B HG3  1 
ATOM   4795 N N    . SER   B 1 65  ? 52.814 -11.312 4.926   1.00 12.18 ?  65  SER   B N    1 
ATOM   4796 C CA   . SER   B 1 65  ? 51.706 -11.819 5.727   1.00 12.34 ?  65  SER   B CA   1 
ATOM   4797 C C    . SER   B 1 65  ? 51.838 -11.424 7.193   1.00 12.70 ?  65  SER   B C    1 
ATOM   4798 O O    . SER   B 1 65  ? 50.837 -11.065 7.833   1.00 13.02 ?  65  SER   B O    1 
ATOM   4799 C CB   . SER   B 1 65  ? 51.617 -13.341 5.591   1.00 12.54 ?  65  SER   B CB   1 
ATOM   4800 O OG   . SER   B 1 65  ? 51.279 -13.734 4.270   1.00 12.76 ?  65  SER   B OG   1 
ATOM   4801 H H    . SER   B 1 65  ? 53.324 -11.936 4.604   1.00 14.59 ?  65  SER   B H    1 
ATOM   4802 H HA   . SER   B 1 65  ? 50.879 -11.442 5.391   1.00 14.78 ?  65  SER   B HA   1 
ATOM   4803 H HB2  . SER   B 1 65  ? 52.471 -13.728 5.824   1.00 15.02 ?  65  SER   B HB2  1 
ATOM   4804 H HB3  . SER   B 1 65  ? 50.929 -13.667 6.196   1.00 15.02 ?  65  SER   B HB3  1 
ATOM   4805 H HG   . SER   B 1 65  ? 51.865 -13.445 3.729   1.00 15.29 ?  65  SER   B HG   1 
ATOM   4806 N N    . ASP   B 1 66  ? 53.046 -11.524 7.759   1.00 12.75 ?  66  ASP   B N    1 
ATOM   4807 C CA   . ASP   B 1 66  ? 53.229 -11.141 9.156   1.00 13.11 ?  66  ASP   B CA   1 
ATOM   4808 C C    . ASP   B 1 66  ? 52.920 -9.661  9.360   1.00 13.48 ?  66  ASP   B C    1 
ATOM   4809 O O    . ASP   B 1 66  ? 52.350 -9.269  10.387  1.00 14.04 ?  66  ASP   B O    1 
ATOM   4810 C CB   . ASP   B 1 66  ? 54.655 -11.454 9.616   1.00 14.70 ?  66  ASP   B CB   1 
ATOM   4811 C CG   . ASP   B 1 66  ? 54.921 -12.948 9.769   1.00 16.44 ?  66  ASP   B CG   1 
ATOM   4812 O OD1  . ASP   B 1 66  ? 53.970 -13.763 9.705   1.00 17.15 ?  66  ASP   B OD1  1 
ATOM   4813 O OD2  . ASP   B 1 66  ? 56.103 -13.312 9.968   1.00 19.26 -1 66  ASP   B OD2  1 
ATOM   4814 H H    . ASP   B 1 66  ? 53.754 -11.816 7.367   1.00 15.28 ?  66  ASP   B H    1 
ATOM   4815 H HA   . ASP   B 1 66  ? 52.620 -11.649 9.712   1.00 15.70 ?  66  ASP   B HA   1 
ATOM   4816 H HB2  . ASP   B 1 66  ? 55.282 -11.107 8.963   1.00 17.62 ?  66  ASP   B HB2  1 
ATOM   4817 H HB3  . ASP   B 1 66  ? 54.810 -11.030 10.478  1.00 17.62 ?  66  ASP   B HB3  1 
ATOM   4818 N N    . ASP   B 1 67  ? 53.303 -8.820  8.399   1.00 13.26 ?  67  ASP   B N    1 
ATOM   4819 C CA   . ASP   B 1 67  ? 52.960 -7.407  8.486   1.00 13.84 ?  67  ASP   B CA   1 
ATOM   4820 C C    . ASP   B 1 67  ? 51.449 -7.199  8.406   1.00 13.94 ?  67  ASP   B C    1 
ATOM   4821 O O    . ASP   B 1 67  ? 50.887 -6.387  9.153   1.00 14.38 ?  67  ASP   B O    1 
ATOM   4822 C CB   . ASP   B 1 67  ? 53.669 -6.637  7.380   1.00 15.23 ?  67  ASP   B CB   1 
ATOM   4823 C CG   . ASP   B 1 67  ? 53.256 -5.188  7.347   1.00 16.95 ?  67  ASP   B CG   1 
ATOM   4824 O OD1  . ASP   B 1 67  ? 53.751 -4.388  8.177   1.00 18.35 ?  67  ASP   B OD1  1 
ATOM   4825 O OD2  . ASP   B 1 67  ? 52.401 -4.868  6.508   1.00 18.27 -1 67  ASP   B OD2  1 
ATOM   4826 H H    . ASP   B 1 67  ? 53.765 -9.039  7.703   1.00 15.89 ?  67  ASP   B H    1 
ATOM   4827 H HA   . ASP   B 1 67  ? 53.269 -7.058  9.336   1.00 16.58 ?  67  ASP   B HA   1 
ATOM   4828 H HB2  . ASP   B 1 67  ? 54.629 -6.675  7.524   1.00 18.25 ?  67  ASP   B HB2  1 
ATOM   4829 H HB3  . ASP   B 1 67  ? 53.452 -7.041  6.520   1.00 18.25 ?  67  ASP   B HB3  1 
ATOM   4830 N N    . TYR   B 1 68  ? 50.771 -7.928  7.510   1.00 13.75 ?  68  TYR   B N    1 
ATOM   4831 C CA   . TYR   B 1 68  ? 49.313 -7.852  7.437   1.00 14.29 ?  68  TYR   B CA   1 
ATOM   4832 C C    . TYR   B 1 68  ? 48.675 -8.197  8.778   1.00 13.71 ?  68  TYR   B C    1 
ATOM   4833 O O    . TYR   B 1 68  ? 47.741 -7.517  9.227   1.00 14.53 ?  68  TYR   B O    1 
ATOM   4834 C CB   . TYR   B 1 68  ? 48.779 -8.783  6.342   1.00 15.09 ?  68  TYR   B CB   1 
ATOM   4835 C CG   . TYR   B 1 68  ? 47.269 -8.926  6.397   1.00 16.51 ?  68  TYR   B CG   1 
ATOM   4836 C CD1  . TYR   B 1 68  ? 46.671 -9.880  7.215   1.00 16.95 ?  68  TYR   B CD1  1 
ATOM   4837 C CD2  . TYR   B 1 68  ? 46.445 -8.087  5.667   1.00 17.60 ?  68  TYR   B CD2  1 
ATOM   4838 C CE1  . TYR   B 1 68  ? 45.308 -9.998  7.299   1.00 18.20 ?  68  TYR   B CE1  1 
ATOM   4839 C CE2  . TYR   B 1 68  ? 45.059 -8.208  5.738   1.00 18.02 ?  68  TYR   B CE2  1 
ATOM   4840 C CZ   . TYR   B 1 68  ? 44.513 -9.164  6.560   1.00 18.11 ?  68  TYR   B CZ   1 
ATOM   4841 O OH   . TYR   B 1 68  ? 43.147 -9.291  6.656   1.00 19.52 ?  68  TYR   B OH   1 
ATOM   4842 H H    . TYR   B 1 68  ? 51.131 -8.473  6.942   1.00 16.48 ?  68  TYR   B H    1 
ATOM   4843 H HA   . TYR   B 1 68  ? 49.062 -6.946  7.212   1.00 17.13 ?  68  TYR   B HA   1 
ATOM   4844 H HB2  . TYR   B 1 68  ? 49.014 -8.420  5.476   1.00 18.08 ?  68  TYR   B HB2  1 
ATOM   4845 H HB3  . TYR   B 1 68  ? 49.169 -9.664  6.454   1.00 18.08 ?  68  TYR   B HB3  1 
ATOM   4846 H HD1  . TYR   B 1 68  ? 47.206 -10.454 7.719   1.00 20.32 ?  68  TYR   B HD1  1 
ATOM   4847 H HD2  . TYR   B 1 68  ? 46.822 -7.436  5.127   1.00 21.10 ?  68  TYR   B HD2  1 
ATOM   4848 H HE1  . TYR   B 1 68  ? 44.923 -10.653 7.840   1.00 21.82 ?  68  TYR   B HE1  1 
ATOM   4849 H HE2  . TYR   B 1 68  ? 44.509 -7.639  5.249   1.00 21.60 ?  68  TYR   B HE2  1 
ATOM   4850 H HH   . TYR   B 1 68  ? 42.757 -8.734  6.152   1.00 23.40 ?  68  TYR   B HH   1 
ATOM   4851 N N    . ILE   B 1 69  ? 49.155 -9.263  9.423   1.00 13.59 ?  69  ILE   B N    1 
ATOM   4852 C CA   . ILE   B 1 69  ? 48.596 -9.696  10.700  1.00 14.09 ?  69  ILE   B CA   1 
ATOM   4853 C C    . ILE   B 1 69  ? 48.851 -8.656  11.783  1.00 14.19 ?  69  ILE   B C    1 
ATOM   4854 O O    . ILE   B 1 69  ? 47.979 -8.380  12.613  1.00 14.38 ?  69  ILE   B O    1 
ATOM   4855 C CB   . ILE   B 1 69  ? 49.166 -11.077 11.081  1.00 15.37 ?  69  ILE   B CB   1 
ATOM   4856 C CG1  . ILE   B 1 69  ? 48.642 -12.175 10.143  1.00 15.69 ?  69  ILE   B CG1  1 
ATOM   4857 C CG2  . ILE   B 1 69  ? 48.875 -11.406 12.539  1.00 16.53 ?  69  ILE   B CG2  1 
ATOM   4858 C CD1  . ILE   B 1 69  ? 47.160 -12.480 10.286  1.00 16.16 ?  69  ILE   B CD1  1 
ATOM   4859 H H    . ILE   B 1 69  ? 49.801 -9.754  9.141   1.00 16.29 ?  69  ILE   B H    1 
ATOM   4860 H HA   . ILE   B 1 69  ? 47.637 -9.791  10.605  1.00 16.88 ?  69  ILE   B HA   1 
ATOM   4861 H HB   . ILE   B 1 69  ? 50.131 -11.037 10.980  1.00 18.42 ?  69  ILE   B HB   1 
ATOM   4862 H HG12 . ILE   B 1 69  ? 48.801 -11.894 9.227   1.00 18.81 ?  69  ILE   B HG12 1 
ATOM   4863 H HG13 . ILE   B 1 69  ? 49.134 -12.992 10.321  1.00 18.81 ?  69  ILE   B HG13 1 
ATOM   4864 H HG21 . ILE   B 1 69  ? 49.016 -12.356 12.680  1.00 19.81 ?  69  ILE   B HG21 1 
ATOM   4865 H HG22 . ILE   B 1 69  ? 49.477 -10.900 13.108  1.00 19.81 ?  69  ILE   B HG22 1 
ATOM   4866 H HG23 . ILE   B 1 69  ? 47.955 -11.176 12.737  1.00 19.81 ?  69  ILE   B HG23 1 
ATOM   4867 H HD11 . ILE   B 1 69  ? 46.931 -13.193 9.670   1.00 19.37 ?  69  ILE   B HD11 1 
ATOM   4868 H HD12 . ILE   B 1 69  ? 46.982 -12.762 11.196  1.00 19.37 ?  69  ILE   B HD12 1 
ATOM   4869 H HD13 . ILE   B 1 69  ? 46.650 -11.685 10.076  1.00 19.37 ?  69  ILE   B HD13 1 
ATOM   4870 N N    . ALA   B 1 70  ? 50.047 -8.070  11.808  1.00 14.09 ?  70  ALA   B N    1 
ATOM   4871 C CA   . ALA   B 1 70  ? 50.325 -7.032  12.796  1.00 13.98 ?  70  ALA   B CA   1 
ATOM   4872 C C    . ALA   B 1 70  ? 49.328 -5.889  12.685  1.00 14.33 ?  70  ALA   B C    1 
ATOM   4873 O O    . ALA   B 1 70  ? 48.882 -5.347  13.700  1.00 14.72 ?  70  ALA   B O    1 
ATOM   4874 C CB   . ALA   B 1 70  ? 51.750 -6.510  12.628  1.00 14.83 ?  70  ALA   B CB   1 
ATOM   4875 H H    . ALA   B 1 70  ? 50.695 -8.251  11.279  1.00 16.88 ?  70  ALA   B H    1 
ATOM   4876 H HA   . ALA   B 1 70  ? 50.251 -7.409  13.687  1.00 16.76 ?  70  ALA   B HA   1 
ATOM   4877 H HB1  . ALA   B 1 70  ? 51.933 -5.852  13.318  1.00 17.77 ?  70  ALA   B HB1  1 
ATOM   4878 H HB2  . ALA   B 1 70  ? 52.373 -7.251  12.708  1.00 17.77 ?  70  ALA   B HB2  1 
ATOM   4879 H HB3  . ALA   B 1 70  ? 51.839 -6.101  11.751  1.00 17.77 ?  70  ALA   B HB3  1 
ATOM   4880 N N    . THR   B 1 71  ? 48.968 -5.510  11.459  1.00 14.68 ?  71  THR   B N    1 
ATOM   4881 C CA   . THR   B 1 71  ? 48.072 -4.377  11.251  1.00 15.74 ?  71  THR   B CA   1 
ATOM   4882 C C    . THR   B 1 71  ? 46.605 -4.745  11.455  1.00 16.34 ?  71  THR   B C    1 
ATOM   4883 O O    . THR   B 1 71  ? 45.826 -3.932  11.969  1.00 17.47 ?  71  THR   B O    1 
ATOM   4884 C CB   . THR   B 1 71  ? 48.294 -3.802  9.850   1.00 17.71 ?  71  THR   B CB   1 
ATOM   4885 O OG1  . THR   B 1 71  ? 49.622 -3.275  9.761   1.00 19.62 ?  71  THR   B OG1  1 
ATOM   4886 C CG2  . THR   B 1 71  ? 47.278 -2.709  9.530   1.00 18.72 ?  71  THR   B CG2  1 
ATOM   4887 H H    . THR   B 1 71  ? 49.230 -5.892  10.736  1.00 17.59 ?  71  THR   B H    1 
ATOM   4888 H HA   . THR   B 1 71  ? 48.294 -3.682  11.889  1.00 18.86 ?  71  THR   B HA   1 
ATOM   4889 H HB   . THR   B 1 71  ? 48.201 -4.506  9.190   1.00 21.23 ?  71  THR   B HB   1 
ATOM   4890 H HG1  . THR   B 1 71  ? 49.755 -2.937  9.000   1.00 23.52 ?  71  THR   B HG1  1 
ATOM   4891 H HG21 . THR   B 1 71  ? 47.583 -2.186  8.771   1.00 22.44 ?  71  THR   B HG21 1 
ATOM   4892 H HG22 . THR   B 1 71  ? 46.421 -3.105  9.315   1.00 22.44 ?  71  THR   B HG22 1 
ATOM   4893 H HG23 . THR   B 1 71  ? 47.175 -2.121  10.294  1.00 22.44 ?  71  THR   B HG23 1 
ATOM   4894 N N    . ASN   B 1 72  ? 46.209 -5.956  11.061  1.00 16.01 ?  72  ASN   B N    1 
ATOM   4895 C CA   . ASN   B 1 72  ? 44.804 -6.309  10.940  1.00 16.16 ?  72  ASN   B CA   1 
ATOM   4896 C C    . ASN   B 1 72  ? 44.331 -7.404  11.885  1.00 16.64 ?  72  ASN   B C    1 
ATOM   4897 O O    . ASN   B 1 72  ? 43.115 -7.556  12.054  1.00 17.97 ?  72  ASN   B O    1 
ATOM   4898 C CB   . ASN   B 1 72  ? 44.492 -6.738  9.498   1.00 17.20 ?  72  ASN   B CB   1 
ATOM   4899 C CG   . ASN   B 1 72  ? 44.770 -5.641  8.505   1.00 18.05 ?  72  ASN   B CG   1 
ATOM   4900 O OD1  . ASN   B 1 72  ? 45.784 -5.655  7.802   1.00 19.03 ?  72  ASN   B OD1  1 
ATOM   4901 N ND2  . ASN   B 1 72  ? 43.891 -4.658  8.465   1.00 19.11 ?  72  ASN   B ND2  1 
ATOM   4902 H H    . ASN   B 1 72  ? 46.750 -6.598  10.853  1.00 19.18 ?  72  ASN   B H    1 
ATOM   4903 H HA   . ASN   B 1 72  ? 44.278 -5.519  11.125  1.00 19.37 ?  72  ASN   B HA   1 
ATOM   4904 H HB2  . ASN   B 1 72  ? 45.049 -7.501  9.266   1.00 20.62 ?  72  ASN   B HB2  1 
ATOM   4905 H HB3  . ASN   B 1 72  ? 43.557 -6.974  9.434   1.00 20.62 ?  72  ASN   B HB3  1 
ATOM   4906 H HD21 . ASN   B 1 72  ? 43.995 -4.006  7.914   1.00 22.91 ?  72  ASN   B HD21 1 
ATOM   4907 H HD22 . ASN   B 1 72  ? 43.194 -4.683  8.971   1.00 22.91 ?  72  ASN   B HD22 1 
ATOM   4908 N N    . GLY   B 1 73  ? 45.233 -8.162  12.502  1.00 15.84 ?  73  GLY   B N    1 
ATOM   4909 C CA   . GLY   B 1 73  ? 44.835 -9.302  13.293  1.00 15.26 ?  73  GLY   B CA   1 
ATOM   4910 C C    . GLY   B 1 73  ? 44.474 -10.489 12.426  1.00 13.80 ?  73  GLY   B C    1 
ATOM   4911 O O    . GLY   B 1 73  ? 44.461 -10.404 11.200  1.00 13.88 ?  73  GLY   B O    1 
ATOM   4912 H H    . GLY   B 1 73  ? 46.085 -8.030  12.477  1.00 18.98 ?  73  GLY   B H    1 
ATOM   4913 H HA2  . GLY   B 1 73  ? 45.563 -9.556  13.884  1.00 18.29 ?  73  GLY   B HA2  1 
ATOM   4914 H HA3  . GLY   B 1 73  ? 44.066 -9.067  13.837  1.00 18.29 ?  73  GLY   B HA3  1 
ATOM   4915 N N    . PRO   B 1 74  ? 44.166 -11.614 13.064  1.00 14.38 ?  74  PRO   B N    1 
ATOM   4916 C CA   . PRO   B 1 74  ? 43.911 -12.846 12.316  1.00 13.60 ?  74  PRO   B CA   1 
ATOM   4917 C C    . PRO   B 1 74  ? 42.613 -12.789 11.522  1.00 13.08 ?  74  PRO   B C    1 
ATOM   4918 O O    . PRO   B 1 74  ? 41.677 -12.049 11.846  1.00 14.59 ?  74  PRO   B O    1 
ATOM   4919 C CB   . PRO   B 1 74  ? 43.832 -13.910 13.417  1.00 14.85 ?  74  PRO   B CB   1 
ATOM   4920 C CG   . PRO   B 1 74  ? 43.387 -13.162 14.626  1.00 17.03 ?  74  PRO   B CG   1 
ATOM   4921 C CD   . PRO   B 1 74  ? 44.045 -11.815 14.517  1.00 16.19 ?  74  PRO   B CD   1 
ATOM   4922 H HA   . PRO   B 1 74  ? 44.656 -13.040 11.719  1.00 16.30 ?  74  PRO   B HA   1 
ATOM   4923 H HB2  . PRO   B 1 74  ? 43.183 -14.586 13.166  1.00 17.80 ?  74  PRO   B HB2  1 
ATOM   4924 H HB3  . PRO   B 1 74  ? 44.707 -14.304 13.553  1.00 17.80 ?  74  PRO   B HB3  1 
ATOM   4925 H HG2  . PRO   B 1 74  ? 42.420 -13.075 14.617  1.00 20.41 ?  74  PRO   B HG2  1 
ATOM   4926 H HG3  . PRO   B 1 74  ? 43.684 -13.626 15.422  1.00 20.41 ?  74  PRO   B HG3  1 
ATOM   4927 H HD2  . PRO   B 1 74  ? 43.481 -11.128 14.913  1.00 19.40 ?  74  PRO   B HD2  1 
ATOM   4928 H HD3  . PRO   B 1 74  ? 44.924 -11.829 14.923  1.00 19.40 ?  74  PRO   B HD3  1 
ATOM   4929 N N    . LEU   B 1 75  ? 42.576 -13.594 10.464  1.00 12.80 ?  75  LEU   B N    1 
ATOM   4930 C CA   . LEU   B 1 75  ? 41.363 -13.806 9.695   1.00 12.63 ?  75  LEU   B CA   1 
ATOM   4931 C C    . LEU   B 1 75  ? 40.387 -14.664 10.496  1.00 13.16 ?  75  LEU   B C    1 
ATOM   4932 O O    . LEU   B 1 75  ? 40.729 -15.229 11.535  1.00 14.19 ?  75  LEU   B O    1 
ATOM   4933 C CB   . LEU   B 1 75  ? 41.689 -14.519 8.383   1.00 12.64 ?  75  LEU   B CB   1 
ATOM   4934 C CG   . LEU   B 1 75  ? 42.537 -13.771 7.349   1.00 15.04 ?  75  LEU   B CG   1 
ATOM   4935 C CD1  . LEU   B 1 75  ? 42.717 -14.600 6.078   1.00 16.35 ?  75  LEU   B CD1  1 
ATOM   4936 C CD2  . LEU   B 1 75  ? 41.953 -12.428 7.019   1.00 18.47 ?  75  LEU   B CD2  1 
ATOM   4937 H H    . LEU   B 1 75  ? 43.254 -14.039 10.167  1.00 15.34 ?  75  LEU   B H    1 
ATOM   4938 H HA   . LEU   B 1 75  ? 40.943 -12.957 9.495   1.00 15.13 ?  75  LEU   B HA   1 
ATOM   4939 H HB2  . LEU   B 1 75  ? 42.164 -15.340 8.595   1.00 15.15 ?  75  LEU   B HB2  1 
ATOM   4940 H HB3  . LEU   B 1 75  ? 40.852 -14.747 7.946   1.00 15.15 ?  75  LEU   B HB3  1 
ATOM   4941 H HG   . LEU   B 1 75  ? 43.420 -13.627 7.722   1.00 18.03 ?  75  LEU   B HG   1 
ATOM   4942 H HD11 . LEU   B 1 75  ? 43.265 -14.100 5.447   1.00 19.60 ?  75  LEU   B HD11 1 
ATOM   4943 H HD12 . LEU   B 1 75  ? 43.158 -15.436 6.299   1.00 19.60 ?  75  LEU   B HD12 1 
ATOM   4944 H HD13 . LEU   B 1 75  ? 41.849 -14.778 5.686   1.00 19.60 ?  75  LEU   B HD13 1 
ATOM   4945 H HD21 . LEU   B 1 75  ? 42.454 -12.036 6.288   1.00 22.14 ?  75  LEU   B HD21 1 
ATOM   4946 H HD22 . LEU   B 1 75  ? 41.026 -12.544 6.765   1.00 22.14 ?  75  LEU   B HD22 1 
ATOM   4947 H HD23 . LEU   B 1 75  ? 42.014 -11.861 7.804   1.00 22.14 ?  75  LEU   B HD23 1 
ATOM   4948 N N    . LYS   B 1 76  ? 39.156 -14.758 9.993   1.00 14.64 ?  76  LYS   B N    1 
ATOM   4949 C CA   . LYS   B 1 76  ? 38.176 -15.728 10.470  1.00 15.83 ?  76  LYS   B CA   1 
ATOM   4950 C C    . LYS   B 1 76  ? 38.264 -16.996 9.624   1.00 14.36 ?  76  LYS   B C    1 
ATOM   4951 O O    . LYS   B 1 76  ? 38.537 -16.935 8.426   1.00 14.05 ?  76  LYS   B O    1 
ATOM   4952 C CB   . LYS   B 1 76  ? 36.752 -15.170 10.311  1.00 18.02 ?  76  LYS   B CB   1 
ATOM   4953 C CG   . LYS   B 1 76  ? 36.489 -13.766 10.884  1.00 20.30 ?  76  LYS   B CG   1 
ATOM   4954 C CD   . LYS   B 1 76  ? 35.074 -13.254 10.543  1.00 21.53 ?  76  LYS   B CD   1 
ATOM   4955 C CE   . LYS   B 1 76  ? 34.831 -11.857 11.094  1.00 23.59 ?  76  LYS   B CE   1 
ATOM   4956 N NZ   . LYS   B 1 76  ? 33.510 -11.295 10.694  1.00 24.15 ?  76  LYS   B NZ   1 
ATOM   4957 H H    . LYS   B 1 76  ? 38.863 -14.262 9.358   1.00 17.54 ?  76  LYS   B H    1 
ATOM   4958 H HA   . LYS   B 1 76  ? 38.337 -15.951 11.402  1.00 18.97 ?  76  LYS   B HA   1 
ATOM   4959 H HB2  . LYS   B 1 76  ? 36.545 -15.137 9.364   1.00 21.60 ?  76  LYS   B HB2  1 
ATOM   4960 H HB3  . LYS   B 1 76  ? 36.137 -15.778 10.752  1.00 21.60 ?  76  LYS   B HB3  1 
ATOM   4961 H HG2  . LYS   B 1 76  ? 36.580 -13.797 11.849  1.00 24.34 ?  76  LYS   B HG2  1 
ATOM   4962 H HG3  . LYS   B 1 76  ? 37.137 -13.147 10.508  1.00 24.34 ?  76  LYS   B HG3  1 
ATOM   4963 H HD2  . LYS   B 1 76  ? 34.969 -13.222 9.578   1.00 25.81 ?  76  LYS   B HD2  1 
ATOM   4964 H HD3  . LYS   B 1 76  ? 34.416 -13.851 10.931  1.00 25.81 ?  76  LYS   B HD3  1 
ATOM   4965 H HE2  . LYS   B 1 76  ? 34.863 -11.891 12.062  1.00 28.28 ?  76  LYS   B HE2  1 
ATOM   4966 H HE3  . LYS   B 1 76  ? 35.523 -11.263 10.760  1.00 28.28 ?  76  LYS   B HE3  1 
ATOM   4967 H HZ1  . LYS   B 1 76  ? 33.455 -11.242 9.807   1.00 28.96 ?  76  LYS   B HZ1  1 
ATOM   4968 H HZ2  . LYS   B 1 76  ? 32.853 -11.815 10.994  1.00 28.96 ?  76  LYS   B HZ2  1 
ATOM   4969 H HZ3  . LYS   B 1 76  ? 33.410 -10.478 11.037  1.00 28.96 ?  76  LYS   B HZ3  1 
ATOM   4970 N N    . VAL   B 1 77  ? 38.016 -18.155 10.247  1.00 15.03 ?  77  VAL   B N    1 
ATOM   4971 C CA   . VAL   B 1 77  ? 37.810 -19.365 9.457   1.00 15.00 ?  77  VAL   B CA   1 
ATOM   4972 C C    . VAL   B 1 77  ? 36.621 -19.130 8.539   1.00 13.79 ?  77  VAL   B C    1 
ATOM   4973 O O    . VAL   B 1 77  ? 35.553 -18.687 8.984   1.00 13.50 ?  77  VAL   B O    1 
ATOM   4974 C CB   . VAL   B 1 77  ? 37.610 -20.592 10.360  1.00 16.20 ?  77  VAL   B CB   1 
ATOM   4975 C CG1  . VAL   B 1 77  ? 37.311 -21.819 9.504   1.00 16.98 ?  77  VAL   B CG1  1 
ATOM   4976 C CG2  . VAL   B 1 77  ? 38.843 -20.831 11.230  1.00 17.52 ?  77  VAL   B CG2  1 
ATOM   4977 H H    . VAL   B 1 77  ? 37.973 -18.260 11.097  1.00 18.01 ?  77  VAL   B H    1 
ATOM   4978 H HA   . VAL   B 1 77  ? 38.589 -19.520 8.902   1.00 17.98 ?  77  VAL   B HA   1 
ATOM   4979 H HB   . VAL   B 1 77  ? 36.849 -20.435 10.943  1.00 19.42 ?  77  VAL   B HB   1 
ATOM   4980 H HG11 . VAL   B 1 77  ? 37.368 -22.611 10.061  1.00 20.35 ?  77  VAL   B HG11 1 
ATOM   4981 H HG12 . VAL   B 1 77  ? 36.413 -21.743 9.137   1.00 20.35 ?  77  VAL   B HG12 1 
ATOM   4982 H HG13 . VAL   B 1 77  ? 37.958 -21.871 8.787   1.00 20.35 ?  77  VAL   B HG13 1 
ATOM   4983 H HG21 . VAL   B 1 77  ? 38.697 -21.628 11.762  1.00 21.00 ?  77  VAL   B HG21 1 
ATOM   4984 H HG22 . VAL   B 1 77  ? 39.612 -20.950 10.654  1.00 21.00 ?  77  VAL   B HG22 1 
ATOM   4985 H HG23 . VAL   B 1 77  ? 38.972 -20.064 11.807  1.00 21.00 ?  77  VAL   B HG23 1 
ATOM   4986 N N    . GLY   B 1 78  ? 36.805 -19.407 7.251   1.00 13.12 ?  78  GLY   B N    1 
ATOM   4987 C CA   . GLY   B 1 78  ? 35.830 -19.088 6.235   1.00 12.75 ?  78  GLY   B CA   1 
ATOM   4988 C C    . GLY   B 1 78  ? 36.073 -17.773 5.533   1.00 12.34 ?  78  GLY   B C    1 
ATOM   4989 O O    . GLY   B 1 78  ? 35.393 -17.489 4.540   1.00 12.99 ?  78  GLY   B O    1 
ATOM   4990 H H    . GLY   B 1 78  ? 37.509 -19.795 6.941   1.00 15.73 ?  78  GLY   B H    1 
ATOM   4991 H HA2  . GLY   B 1 78  ? 35.826 -19.785 5.569   1.00 15.27 ?  78  GLY   B HA2  1 
ATOM   4992 H HA3  . GLY   B 1 78  ? 34.951 -19.048 6.643   1.00 15.27 ?  78  GLY   B HA3  1 
ATOM   4993 N N    . GLY   B 1 79  ? 37.020 -16.965 6.017   1.00 12.48 ?  79  GLY   B N    1 
ATOM   4994 C CA   . GLY   B 1 79  ? 37.314 -15.674 5.434   1.00 12.05 ?  79  GLY   B CA   1 
ATOM   4995 C C    . GLY   B 1 79  ? 38.555 -15.692 4.554   1.00 11.71 ?  79  GLY   B C    1 
ATOM   4996 O O    . GLY   B 1 79  ? 39.178 -16.724 4.310   1.00 12.26 ?  79  GLY   B O    1 
ATOM   4997 H H    . GLY   B 1 79  ? 37.521 -17.154 6.690   1.00 14.96 ?  79  GLY   B H    1 
ATOM   4998 H HA2  . GLY   B 1 79  ? 36.562 -15.383 4.893   1.00 14.44 ?  79  GLY   B HA2  1 
ATOM   4999 H HA3  . GLY   B 1 79  ? 37.449 -15.024 6.142   1.00 14.44 ?  79  GLY   B HA3  1 
ATOM   5000 N N    . SER   B 1 80  ? 38.920 -14.498 4.085   1.00 11.77 ?  80  SER   B N    1 
ATOM   5001 C CA   . SER   B 1 80  ? 40.028 -14.363 3.154   1.00 11.56 ?  80  SER   B CA   1 
ATOM   5002 C C    . SER   B 1 80  ? 40.609 -12.957 3.215   1.00 11.60 ?  80  SER   B C    1 
ATOM   5003 O O    . SER   B 1 80  ? 39.999 -12.026 3.743   1.00 12.97 ?  80  SER   B O    1 
ATOM   5004 C CB   . SER   B 1 80  ? 39.583 -14.656 1.718   1.00 11.94 ?  80  SER   B CB   1 
ATOM   5005 O OG   . SER   B 1 80  ? 38.752 -13.627 1.217   1.00 13.08 ?  80  SER   B OG   1 
ATOM   5006 H H    . SER   B 1 80  ? 38.546 -13.752 4.294   1.00 14.10 ?  80  SER   B H    1 
ATOM   5007 H HA   . SER   B 1 80  ? 40.719 -14.995 3.396   1.00 13.85 ?  80  SER   B HA   1 
ATOM   5008 H HB2  . SER   B 1 80  ? 40.365 -14.728 1.150   1.00 14.30 ?  80  SER   B HB2  1 
ATOM   5009 H HB3  . SER   B 1 80  ? 39.089 -15.493 1.705   1.00 14.30 ?  80  SER   B HB3  1 
ATOM   5010 H HG   . SER   B 1 80  ? 38.062 -13.554 1.699   1.00 15.67 ?  80  SER   B HG   1 
ATOM   5011 N N    . CYS   B 1 81  ? 41.794 -12.813 2.626   1.00 11.38 ?  81  CYS   B N    1 
ATOM   5012 C CA   . CYS   B 1 81  ? 42.340 -11.498 2.324   1.00 11.38 ?  81  CYS   B CA   1 
ATOM   5013 C C    . CYS   B 1 81  ? 43.117 -11.583 1.020   1.00 10.86 ?  81  CYS   B C    1 
ATOM   5014 O O    . CYS   B 1 81  ? 43.628 -12.644 0.648   1.00 12.15 ?  81  CYS   B O    1 
ATOM   5015 C CB   . CYS   B 1 81  ? 43.235 -10.948 3.447   1.00 12.37 ?  81  CYS   B CB   1 
ATOM   5016 S SG   . CYS   B 1 81  ? 44.757 -11.886 3.703   1.00 12.67 ?  81  CYS   B SG   1 
ATOM   5017 H H    . CYS   B 1 81  ? 42.300 -13.467 2.381   1.00 13.64 ?  81  CYS   B H    1 
ATOM   5018 H HA   . CYS   B 1 81  ? 41.611 -10.875 2.198   1.00 13.64 ?  81  CYS   B HA   1 
ATOM   5019 H HB2  . CYS   B 1 81  ? 43.488 -10.038 3.230   1.00 14.82 ?  81  CYS   B HB2  1 
ATOM   5020 H HB3  . CYS   B 1 81  ? 42.734 -10.957 4.280   1.00 14.82 ?  81  CYS   B HB3  1 
ATOM   5021 H HG   . CYS   B 1 81  ? 45.381 -11.386 4.606   1.00 15.18 ?  81  CYS   B HG   1 
ATOM   5022 N N    . VAL   B 1 82  ? 43.217 -10.443 0.343   1.00 11.08 ?  82  VAL   B N    1 
ATOM   5023 C CA   . VAL   B 1 82  ? 43.982 -10.307 -0.894  1.00 11.63 ?  82  VAL   B CA   1 
ATOM   5024 C C    . VAL   B 1 82  ? 45.324 -9.664  -0.573  1.00 11.97 ?  82  VAL   B C    1 
ATOM   5025 O O    . VAL   B 1 82  ? 45.371 -8.541  -0.050  1.00 12.80 ?  82  VAL   B O    1 
ATOM   5026 C CB   . VAL   B 1 82  ? 43.227 -9.464  -1.934  1.00 12.85 ?  82  VAL   B CB   1 
ATOM   5027 C CG1  . VAL   B 1 82  ? 44.066 -9.309  -3.198  1.00 14.25 ?  82  VAL   B CG1  1 
ATOM   5028 C CG2  . VAL   B 1 82  ? 41.864 -10.067 -2.243  1.00 13.80 ?  82  VAL   B CG2  1 
ATOM   5029 H H    . VAL   B 1 82  ? 42.830 -9.705  0.583   1.00 13.27 ?  82  VAL   B H    1 
ATOM   5030 H HA   . VAL   B 1 82  ? 44.145 -11.183 -1.269  1.00 13.93 ?  82  VAL   B HA   1 
ATOM   5031 H HB   . VAL   B 1 82  ? 43.082 -8.579  -1.573  1.00 15.40 ?  82  VAL   B HB   1 
ATOM   5032 H HG11 . VAL   B 1 82  ? 43.500 -8.984  -3.915  1.00 17.07 ?  82  VAL   B HG11 1 
ATOM   5033 H HG12 . VAL   B 1 82  ? 44.780 -8.672  -3.029  1.00 17.07 ?  82  VAL   B HG12 1 
ATOM   5034 H HG13 . VAL   B 1 82  ? 44.442 -10.170 -3.438  1.00 17.07 ?  82  VAL   B HG13 1 
ATOM   5035 H HG21 . VAL   B 1 82  ? 41.433 -9.539  -2.935  1.00 16.53 ?  82  VAL   B HG21 1 
ATOM   5036 H HG22 . VAL   B 1 82  ? 41.981 -10.980 -2.550  1.00 16.53 ?  82  VAL   B HG22 1 
ATOM   5037 H HG23 . VAL   B 1 82  ? 41.324 -10.056 -1.437  1.00 16.53 ?  82  VAL   B HG23 1 
ATOM   5038 N N    . LEU   B 1 83  ? 46.408 -10.346 -0.937  1.00 11.38 ?  83  LEU   B N    1 
ATOM   5039 C CA   . LEU   B 1 83  ? 47.763 -9.831  -0.810  1.00 11.08 ?  83  LEU   B CA   1 
ATOM   5040 C C    . LEU   B 1 83  ? 48.465 -9.976  -2.159  1.00 11.00 ?  83  LEU   B C    1 
ATOM   5041 O O    . LEU   B 1 83  ? 47.863 -10.398 -3.148  1.00 11.32 ?  83  LEU   B O    1 
ATOM   5042 C CB   . LEU   B 1 83  ? 48.506 -10.522 0.340   1.00 12.09 ?  83  LEU   B CB   1 
ATOM   5043 C CG   . LEU   B 1 83  ? 47.996 -10.161 1.739   1.00 12.88 ?  83  LEU   B CG   1 
ATOM   5044 C CD1  . LEU   B 1 83  ? 48.624 -11.031 2.803   1.00 13.34 ?  83  LEU   B CD1  1 
ATOM   5045 C CD2  . LEU   B 1 83  ? 48.209 -8.678  2.066   1.00 13.96 ?  83  LEU   B CD2  1 
ATOM   5046 H H    . LEU   B 1 83  ? 46.374 -11.140 -1.275  1.00 13.64 ?  83  LEU   B H    1 
ATOM   5047 H HA   . LEU   B 1 83  ? 47.714 -8.886  -0.612  1.00 13.27 ?  83  LEU   B HA   1 
ATOM   5048 H HB2  . LEU   B 1 83  ? 48.422 -11.480 0.233   1.00 14.49 ?  83  LEU   B HB2  1 
ATOM   5049 H HB3  . LEU   B 1 83  ? 49.443 -10.269 0.291   1.00 14.49 ?  83  LEU   B HB3  1 
ATOM   5050 H HG   . LEU   B 1 83  ? 47.044 -10.321 1.761   1.00 15.43 ?  83  LEU   B HG   1 
ATOM   5051 H HD11 . LEU   B 1 83  ? 48.271 -10.779 3.672   1.00 15.98 ?  83  LEU   B HD11 1 
ATOM   5052 H HD12 . LEU   B 1 83  ? 48.406 -11.963 2.620   1.00 15.98 ?  83  LEU   B HD12 1 
ATOM   5053 H HD13 . LEU   B 1 83  ? 49.587 -10.914 2.792   1.00 15.98 ?  83  LEU   B HD13 1 
ATOM   5054 H HD21 . LEU   B 1 83  ? 48.007 -8.530  3.003   1.00 16.73 ?  83  LEU   B HD21 1 
ATOM   5055 H HD22 . LEU   B 1 83  ? 49.134 -8.443  1.887   1.00 16.73 ?  83  LEU   B HD22 1 
ATOM   5056 H HD23 . LEU   B 1 83  ? 47.620 -8.143  1.512   1.00 16.73 ?  83  LEU   B HD23 1 
ATOM   5057 N N    . SER   B 1 84  ? 49.743 -9.602  -2.213  1.00 12.54 ?  84  SER   B N    1 
ATOM   5058 C CA   . SER   B 1 84  ? 50.476 -9.717  -3.464  1.00 12.54 ?  84  SER   B CA   1 
ATOM   5059 C C    . SER   B 1 84  ? 50.638 -11.178 -3.873  1.00 11.62 ?  84  SER   B C    1 
ATOM   5060 O O    . SER   B 1 84  ? 50.741 -12.077 -3.038  1.00 11.48 ?  84  SER   B O    1 
ATOM   5061 C CB   . SER   B 1 84  ? 51.866 -9.100  -3.322  1.00 14.84 ?  84  SER   B CB   1 
ATOM   5062 O OG   . SER   B 1 84  ? 52.614 -9.322  -4.502  1.00 16.30 ?  84  SER   B OG   1 
ATOM   5063 H H    . SER   B 1 84  ? 50.184 -9.268  -1.558  1.00 15.03 ?  84  SER   B H    1 
ATOM   5064 H HA   . SER   B 1 84  ? 50.000 -9.253  -4.168  1.00 15.03 ?  84  SER   B HA   1 
ATOM   5065 H HB2  . SER   B 1 84  ? 51.775 -8.143  -3.174  1.00 17.78 ?  84  SER   B HB2  1 
ATOM   5066 H HB3  . SER   B 1 84  ? 52.325 -9.509  -2.575  1.00 17.78 ?  84  SER   B HB3  1 
ATOM   5067 H HG   . SER   B 1 84  ? 53.381 -8.973  -4.428  1.00 19.53 ?  84  SER   B HG   1 
ATOM   5068 N N    . GLY   B 1 85  ? 50.697 -11.401 -5.180  1.00 12.32 ?  85  GLY   B N    1 
ATOM   5069 C CA   . GLY   B 1 85  ? 51.051 -12.693 -5.717  1.00 13.18 ?  85  GLY   B CA   1 
ATOM   5070 C C    . GLY   B 1 85  ? 52.521 -12.879 -6.021  1.00 12.32 ?  85  GLY   B C    1 
ATOM   5071 O O    . GLY   B 1 85  ? 52.895 -13.955 -6.485  1.00 13.29 ?  85  GLY   B O    1 
ATOM   5072 H H    . GLY   B 1 85  ? 50.549 -10.813 -5.778  1.00 14.76 ?  85  GLY   B H    1 
ATOM   5073 H HA2  . GLY   B 1 85  ? 50.789 -13.386 -5.084  1.00 15.79 ?  85  GLY   B HA2  1 
ATOM   5074 H HA3  . GLY   B 1 85  ? 50.561 -12.842 -6.536  1.00 15.79 ?  85  GLY   B HA3  1 
ATOM   5075 N N    . HIS   B 1 86  ? 53.374 -11.880 -5.794  1.00 12.55 ?  86  HIS   B N    1 
ATOM   5076 C CA   . HIS   B 1 86  ? 54.834 -12.045 -5.884  1.00 12.38 ?  86  HIS   B CA   1 
ATOM   5077 C C    . HIS   B 1 86  ? 55.199 -12.554 -7.276  1.00 12.72 ?  86  HIS   B C    1 
ATOM   5078 O O    . HIS   B 1 86  ? 54.807 -11.935 -8.277  1.00 13.42 ?  86  HIS   B O    1 
ATOM   5079 C CB   . HIS   B 1 86  ? 55.328 -12.889 -4.712  1.00 12.91 ?  86  HIS   B CB   1 
ATOM   5080 C CG   . HIS   B 1 86  ? 55.009 -12.286 -3.387  1.00 13.03 ?  86  HIS   B CG   1 
ATOM   5081 N ND1  . HIS   B 1 86  ? 55.827 -11.359 -2.775  1.00 14.62 ?  86  HIS   B ND1  1 
ATOM   5082 C CD2  . HIS   B 1 86  ? 53.939 -12.446 -2.572  1.00 13.37 ?  86  HIS   B CD2  1 
ATOM   5083 C CE1  . HIS   B 1 86  ? 55.268 -10.972 -1.641  1.00 14.55 ?  86  HIS   B CE1  1 
ATOM   5084 N NE2  . HIS   B 1 86  ? 54.120 -11.612 -1.497  1.00 14.07 ?  86  HIS   B NE2  1 
ATOM   5085 H H    . HIS   B 1 86  ? 53.130 -11.087 -5.584  1.00 15.04 ?  86  HIS   B H    1 
ATOM   5086 H HA   . HIS   B 1 86  ? 55.240 -11.173 -5.785  1.00 14.84 ?  86  HIS   B HA   1 
ATOM   5087 H HB2  . HIS   B 1 86  ? 54.917 -13.767 -4.751  1.00 15.47 ?  86  HIS   B HB2  1 
ATOM   5088 H HB3  . HIS   B 1 86  ? 56.296 -12.979 -4.769  1.00 15.47 ?  86  HIS   B HB3  1 
ATOM   5089 H HD2  . HIS   B 1 86  ? 53.205 -13.001 -2.722  1.00 16.02 ?  86  HIS   B HD2  1 
ATOM   5090 H HE1  . HIS   B 1 86  ? 55.631 -10.368 -1.035  1.00 17.43 ?  86  HIS   B HE1  1 
ATOM   5091 H HE2  . HIS   B 1 86  ? 53.584 -11.540 -0.825  1.00 16.86 ?  86  HIS   B HE2  1 
ATOM   5092 N N    . ASN   B 1 87  ? 55.963 -13.639 -7.389  1.00 13.15 ?  87  ASN   B N    1 
ATOM   5093 C CA   . ASN   B 1 87  ? 56.357 -14.213 -8.666  1.00 14.08 ?  87  ASN   B CA   1 
ATOM   5094 C C    . ASN   B 1 87  ? 55.374 -15.258 -9.163  1.00 13.72 ?  87  ASN   B C    1 
ATOM   5095 O O    . ASN   B 1 87  ? 55.680 -15.957 -10.133 1.00 15.37 ?  87  ASN   B O    1 
ATOM   5096 C CB   . ASN   B 1 87  ? 57.750 -14.845 -8.551  1.00 16.11 ?  87  ASN   B CB   1 
ATOM   5097 C CG   . ASN   B 1 87  ? 57.811 -15.954 -7.507  1.00 16.80 ?  87  ASN   B CG   1 
ATOM   5098 O OD1  . ASN   B 1 87  ? 57.178 -15.875 -6.450  1.00 16.06 ?  87  ASN   B OD1  1 
ATOM   5099 N ND2  . ASN   B 1 87  ? 58.574 -17.007 -7.811  1.00 19.27 ?  87  ASN   B ND2  1 
ATOM   5100 H H    . ASN   B 1 87  ? 56.271 -14.075 -6.715  1.00 15.75 ?  87  ASN   B H    1 
ATOM   5101 H HA   . ASN   B 1 87  ? 56.402 -13.507 -9.327  1.00 16.87 ?  87  ASN   B HA   1 
ATOM   5102 H HB2  . ASN   B 1 87  ? 57.996 -15.224 -9.413  1.00 19.31 ?  87  ASN   B HB2  1 
ATOM   5103 H HB3  . ASN   B 1 87  ? 58.388 -14.161 -8.299  1.00 19.31 ?  87  ASN   B HB3  1 
ATOM   5104 H HD21 . ASN   B 1 87  ? 58.647 -17.660 -7.259  1.00 23.10 ?  87  ASN   B HD21 1 
ATOM   5105 H HD22 . ASN   B 1 87  ? 59.003 -17.029 -8.560  1.00 23.10 ?  87  ASN   B HD22 1 
ATOM   5106 N N    . LEU   B 1 88  ? 54.201 -15.365 -8.540  1.00 12.52 ?  88  LEU   B N    1 
ATOM   5107 C CA   . LEU   B 1 88  ? 53.227 -16.397 -8.871  1.00 13.03 ?  88  LEU   B CA   1 
ATOM   5108 C C    . LEU   B 1 88  ? 51.994 -15.879 -9.592  1.00 12.90 ?  88  LEU   B C    1 
ATOM   5109 O O    . LEU   B 1 88  ? 51.395 -16.624 -10.380 1.00 14.58 ?  88  LEU   B O    1 
ATOM   5110 C CB   . LEU   B 1 88  ? 52.759 -17.092 -7.589  1.00 14.08 ?  88  LEU   B CB   1 
ATOM   5111 C CG   . LEU   B 1 88  ? 53.878 -17.755 -6.798  1.00 16.56 ?  88  LEU   B CG   1 
ATOM   5112 C CD1  . LEU   B 1 88  ? 53.388 -18.108 -5.407  1.00 18.22 ?  88  LEU   B CD1  1 
ATOM   5113 C CD2  . LEU   B 1 88  ? 54.353 -18.987 -7.537  1.00 19.67 ?  88  LEU   B CD2  1 
ATOM   5114 H H    . LEU   B 1 88  ? 53.946 -14.848 -7.898  1.00 15.00 ?  88  LEU   B H    1 
ATOM   5115 H HA   . LEU   B 1 88  ? 53.642 -17.057 -9.437  1.00 15.61 ?  88  LEU   B HA   1 
ATOM   5116 H HB2  . LEU   B 1 88  ? 52.336 -16.440 -7.010  1.00 16.88 ?  88  LEU   B HB2  1 
ATOM   5117 H HB3  . LEU   B 1 88  ? 52.117 -17.783 -7.826  1.00 16.88 ?  88  LEU   B HB3  1 
ATOM   5118 H HG   . LEU   B 1 88  ? 54.623 -17.140 -6.714  1.00 19.84 ?  88  LEU   B HG   1 
ATOM   5119 H HD11 . LEU   B 1 88  ? 54.039 -18.687 -4.981  1.00 21.84 ?  88  LEU   B HD11 1 
ATOM   5120 H HD12 . LEU   B 1 88  ? 53.281 -17.293 -4.894  1.00 21.84 ?  88  LEU   B HD12 1 
ATOM   5121 H HD13 . LEU   B 1 88  ? 52.537 -18.567 -5.483  1.00 21.84 ?  88  LEU   B HD13 1 
ATOM   5122 H HD21 . LEU   B 1 88  ? 55.009 -19.447 -6.990  1.00 23.58 ?  88  LEU   B HD21 1 
ATOM   5123 H HD22 . LEU   B 1 88  ? 53.595 -19.567 -7.704  1.00 23.58 ?  88  LEU   B HD22 1 
ATOM   5124 H HD23 . LEU   B 1 88  ? 54.756 -18.716 -8.377  1.00 23.58 ?  88  LEU   B HD23 1 
ATOM   5125 N N    . ALA   B 1 89  ? 51.586 -14.645 -9.323  1.00 12.07 ?  89  ALA   B N    1 
ATOM   5126 C CA   . ALA   B 1 89  ? 50.300 -14.145 -9.784  1.00 11.51 ?  89  ALA   B CA   1 
ATOM   5127 C C    . ALA   B 1 89  ? 50.271 -12.656 -9.493  1.00 12.10 ?  89  ALA   B C    1 
ATOM   5128 O O    . ALA   B 1 89  ? 51.110 -12.142 -8.753  1.00 12.96 ?  89  ALA   B O    1 
ATOM   5129 C CB   . ALA   B 1 89  ? 49.150 -14.819 -9.046  1.00 11.95 ?  89  ALA   B CB   1 
ATOM   5130 H H    . ALA   B 1 89  ? 52.032 -14.062 -8.866  1.00 14.46 ?  89  ALA   B H    1 
ATOM   5131 H HA   . ALA   B 1 89  ? 50.199 -14.284 -10.742 1.00 13.79 ?  89  ALA   B HA   1 
ATOM   5132 H HB1  . ALA   B 1 89  ? 48.306 -14.488 -9.402  1.00 14.32 ?  89  ALA   B HB1  1 
ATOM   5133 H HB2  . ALA   B 1 89  ? 49.210 -15.778 -9.189  1.00 14.32 ?  89  ALA   B HB2  1 
ATOM   5134 H HB3  . ALA   B 1 89  ? 49.217 -14.617 -8.106  1.00 14.32 ?  89  ALA   B HB3  1 
ATOM   5135 N N    . LYS   B 1 90  ? 49.277 -11.965 -10.050 1.00 13.08 ?  90  LYS   B N    1 
ATOM   5136 C CA   . LYS   B 1 90  ? 49.090 -10.576 -9.652  1.00 13.31 ?  90  LYS   B CA   1 
ATOM   5137 C C    . LYS   B 1 90  ? 48.765 -10.495 -8.166  1.00 12.79 ?  90  LYS   B C    1 
ATOM   5138 O O    . LYS   B 1 90  ? 49.402 -9.740  -7.416  1.00 14.02 ?  90  LYS   B O    1 
ATOM   5139 C CB   . LYS   B 1 90  ? 48.016 -9.916  -10.517 1.00 14.74 ?  90  LYS   B CB   1 
ATOM   5140 C CG   . LYS   B 1 90  ? 47.715 -8.477  -10.138 1.00 15.38 ?  90  LYS   B CG   1 
ATOM   5141 C CD   . LYS   B 1 90  ? 48.914 -7.564  -10.241 1.00 18.31 ?  90  LYS   B CD   1 
ATOM   5142 C CE   . LYS   B 1 90  ? 48.466 -6.142  -9.990  1.00 20.67 ?  90  LYS   B CE   1 
ATOM   5143 N NZ   . LYS   B 1 90  ? 49.610 -5.206  -9.904  1.00 20.64 ?  90  LYS   B NZ   1 
ATOM   5144 H H    . LYS   B 1 90  ? 48.720 -12.265 -10.635 1.00 15.67 ?  90  LYS   B H    1 
ATOM   5145 H HA   . LYS   B 1 90  ? 49.918 -10.099 -9.799  1.00 15.95 ?  90  LYS   B HA   1 
ATOM   5146 H HB2  . LYS   B 1 90  ? 48.316 -9.917  -11.443 1.00 17.67 ?  90  LYS   B HB2  1 
ATOM   5147 H HB3  . LYS   B 1 90  ? 47.193 -10.422 -10.443 1.00 17.67 ?  90  LYS   B HB3  1 
ATOM   5148 H HG2  . LYS   B 1 90  ? 47.027 -8.133  -10.731 1.00 18.43 ?  90  LYS   B HG2  1 
ATOM   5149 H HG3  . LYS   B 1 90  ? 47.392 -8.450  -9.221  1.00 18.43 ?  90  LYS   B HG3  1 
ATOM   5150 H HD2  . LYS   B 1 90  ? 49.572 -7.804  -9.569  1.00 21.95 ?  90  LYS   B HD2  1 
ATOM   5151 H HD3  . LYS   B 1 90  ? 49.295 -7.618  -11.131 1.00 21.95 ?  90  LYS   B HD3  1 
ATOM   5152 H HE2  . LYS   B 1 90  ? 47.897 -5.847  -10.720 1.00 24.78 ?  90  LYS   B HE2  1 
ATOM   5153 H HE3  . LYS   B 1 90  ? 47.983 -6.096  -9.151  1.00 24.78 ?  90  LYS   B HE3  1 
ATOM   5154 H HZ1  . LYS   B 1 90  ? 49.322 -4.374  -9.758  1.00 24.74 ?  90  LYS   B HZ1  1 
ATOM   5155 H HZ2  . LYS   B 1 90  ? 50.152 -5.442  -9.238  1.00 24.74 ?  90  LYS   B HZ2  1 
ATOM   5156 H HZ3  . LYS   B 1 90  ? 50.074 -5.215  -10.667 1.00 24.74 ?  90  LYS   B HZ3  1 
ATOM   5157 N N    . HIS   B 1 91  ? 47.809 -11.315 -7.719  1.00 11.17 ?  91  HIS   B N    1 
ATOM   5158 C CA   . HIS   B 1 91  ? 47.341 -11.341 -6.347  1.00 11.35 ?  91  HIS   B CA   1 
ATOM   5159 C C    . HIS   B 1 91  ? 47.345 -12.770 -5.832  1.00 10.65 ?  91  HIS   B C    1 
ATOM   5160 O O    . HIS   B 1 91  ? 47.116 -13.723 -6.588  1.00 11.22 ?  91  HIS   B O    1 
ATOM   5161 C CB   . HIS   B 1 91  ? 45.889 -10.858 -6.231  1.00 12.57 ?  91  HIS   B CB   1 
ATOM   5162 C CG   . HIS   B 1 91  ? 45.682 -9.450  -6.673  1.00 16.23 ?  91  HIS   B CG   1 
ATOM   5163 N ND1  . HIS   B 1 91  ? 46.302 -8.376  -6.070  1.00 19.01 ?  91  HIS   B ND1  1 
ATOM   5164 C CD2  . HIS   B 1 91  ? 44.893 -8.934  -7.642  1.00 18.77 ?  91  HIS   B CD2  1 
ATOM   5165 C CE1  . HIS   B 1 91  ? 45.918 -7.259  -6.662  1.00 19.85 ?  91  HIS   B CE1  1 
ATOM   5166 N NE2  . HIS   B 1 91  ? 45.061 -7.571  -7.619  1.00 20.23 ?  91  HIS   B NE2  1 
ATOM   5167 H H    . HIS   B 1 91  ? 47.404 -11.889 -8.218  1.00 13.38 ?  91  HIS   B H    1 
ATOM   5168 H HA   . HIS   B 1 91  ? 47.910 -10.787 -5.783  1.00 13.60 ?  91  HIS   B HA   1 
ATOM   5169 H HB2  . HIS   B 1 91  ? 45.325 -11.424 -6.778  1.00 15.06 ?  91  HIS   B HB2  1 
ATOM   5170 H HB3  . HIS   B 1 91  ? 45.611 -10.919 -5.301  1.00 15.06 ?  91  HIS   B HB3  1 
ATOM   5171 H HD1  . HIS   B 1 91  ? 46.855 -8.426  -5.412  1.00 22.78 ?  91  HIS   B HD1  1 
ATOM   5172 H HD2  . HIS   B 1 91  ? 44.349 -9.407  -8.227  1.00 22.50 ?  91  HIS   B HD2  1 
ATOM   5173 H HE1  . HIS   B 1 91  ? 46.201 -6.399  -6.439  1.00 23.79 ?  91  HIS   B HE1  1 
ATOM   5174 N N    . CYS   B 1 92  ? 47.539 -12.903 -4.531  1.00 10.44 ?  92  CYS   B N    1 
ATOM   5175 C CA   . CYS   B 1 92  ? 47.239 -14.135 -3.817  1.00 10.34 ?  92  CYS   B CA   1 
ATOM   5176 C C    . CYS   B 1 92  ? 46.014 -13.903 -2.940  1.00 9.95  ?  92  CYS   B C    1 
ATOM   5177 O O    . CYS   B 1 92  ? 46.010 -13.003 -2.089  1.00 10.90 ?  92  CYS   B O    1 
ATOM   5178 C CB   . CYS   B 1 92  ? 48.414 -14.588 -2.955  1.00 11.12 ?  92  CYS   B CB   1 
ATOM   5179 S SG   . CYS   B 1 92  ? 48.057 -16.135 -2.070  1.00 11.25 ?  92  CYS   B SG   1 
ATOM   5180 H H    . CYS   B 1 92  ? 47.871 -12.284 -4.025  1.00 12.50 ?  92  CYS   B H    1 
ATOM   5181 H HA   . CYS   B 1 92  ? 47.047 -14.837 -4.457  1.00 12.38 ?  92  CYS   B HA   1 
ATOM   5182 H HB2  . CYS   B 1 92  ? 49.189 -14.730 -3.517  1.00 13.32 ?  92  CYS   B HB2  1 
ATOM   5183 H HB3  . CYS   B 1 92  ? 48.602 -13.901 -2.293  1.00 13.32 ?  92  CYS   B HB3  1 
ATOM   5184 H HG   . CYS   B 1 92  ? 49.026 -16.447 -1.437  1.00 13.48 ?  92  CYS   B HG   1 
ATOM   5185 N N    . LEU   B 1 93  ? 44.979 -14.714 -3.155  1.00 10.14 ?  93  LEU   B N    1 
ATOM   5186 C CA   . LEU   B 1 93  ? 43.803 -14.736 -2.294  1.00 10.03 ?  93  LEU   B CA   1 
ATOM   5187 C C    . LEU   B 1 93  ? 44.024 -15.797 -1.223  1.00 9.62  ?  93  LEU   B C    1 
ATOM   5188 O O    . LEU   B 1 93  ? 43.985 -17.001 -1.510  1.00 10.45 ?  93  LEU   B O    1 
ATOM   5189 C CB   . LEU   B 1 93  ? 42.544 -15.032 -3.105  1.00 10.59 ?  93  LEU   B CB   1 
ATOM   5190 C CG   . LEU   B 1 93  ? 41.243 -15.045 -2.304  1.00 11.46 ?  93  LEU   B CG   1 
ATOM   5191 C CD1  . LEU   B 1 93  ? 40.878 -13.658 -1.811  1.00 12.08 ?  93  LEU   B CD1  1 
ATOM   5192 C CD2  . LEU   B 1 93  ? 40.123 -15.633 -3.141  1.00 11.59 ?  93  LEU   B CD2  1 
ATOM   5193 H H    . LEU   B 1 93  ? 44.942 -15.287 -3.809  1.00 12.14 ?  93  LEU   B H    1 
ATOM   5194 H HA   . LEU   B 1 93  ? 43.703 -13.875 -1.870  1.00 12.01 ?  93  LEU   B HA   1 
ATOM   5195 H HB2  . LEU   B 1 93  ? 42.453 -14.350 -3.795  1.00 12.69 ?  93  LEU   B HB2  1 
ATOM   5196 H HB3  . LEU   B 1 93  ? 42.638 -15.900 -3.524  1.00 12.69 ?  93  LEU   B HB3  1 
ATOM   5197 H HG   . LEU   B 1 93  ? 41.358 -15.611 -1.530  1.00 13.73 ?  93  LEU   B HG   1 
ATOM   5198 H HD11 . LEU   B 1 93  ? 40.024 -13.698 -1.357  1.00 14.48 ?  93  LEU   B HD11 1 
ATOM   5199 H HD12 . LEU   B 1 93  ? 41.566 -13.348 -1.203  1.00 14.48 ?  93  LEU   B HD12 1 
ATOM   5200 H HD13 . LEU   B 1 93  ? 40.818 -13.057 -2.574  1.00 14.48 ?  93  LEU   B HD13 1 
ATOM   5201 H HD21 . LEU   B 1 93  ? 39.301 -15.630 -2.622  1.00 13.88 ?  93  LEU   B HD21 1 
ATOM   5202 H HD22 . LEU   B 1 93  ? 40.005 -15.098 -3.944  1.00 13.88 ?  93  LEU   B HD22 1 
ATOM   5203 H HD23 . LEU   B 1 93  ? 40.351 -16.545 -3.386  1.00 13.88 ?  93  LEU   B HD23 1 
ATOM   5204 N N    . HIS   B 1 94  ? 44.304 -15.360 -0.002  1.00 9.54  ?  94  HIS   B N    1 
ATOM   5205 C CA   . HIS   B 1 94  ? 44.518 -16.267 1.116   1.00 9.75  ?  94  HIS   B CA   1 
ATOM   5206 C C    . HIS   B 1 94  ? 43.156 -16.620 1.692   1.00 10.49 ?  94  HIS   B C    1 
ATOM   5207 O O    . HIS   B 1 94  ? 42.486 -15.751 2.252   1.00 11.98 ?  94  HIS   B O    1 
ATOM   5208 C CB   . HIS   B 1 94  ? 45.387 -15.591 2.172   1.00 10.26 ?  94  HIS   B CB   1 
ATOM   5209 C CG   . HIS   B 1 94  ? 46.771 -15.289 1.704   1.00 10.43 ?  94  HIS   B CG   1 
ATOM   5210 N ND1  . HIS   B 1 94  ? 47.799 -16.202 1.786   1.00 10.92 ?  94  HIS   B ND1  1 
ATOM   5211 C CD2  . HIS   B 1 94  ? 47.280 -14.180 1.110   1.00 10.56 ?  94  HIS   B CD2  1 
ATOM   5212 C CE1  . HIS   B 1 94  ? 48.890 -15.648 1.285   1.00 10.43 ?  94  HIS   B CE1  1 
ATOM   5213 N NE2  . HIS   B 1 94  ? 48.604 -14.425 0.867   1.00 10.98 ?  94  HIS   B NE2  1 
ATOM   5214 H H    . HIS   B 1 94  ? 44.380 -14.522 0.200   1.00 11.42 ?  94  HIS   B H    1 
ATOM   5215 H HA   . HIS   B 1 94  ? 44.955 -17.073 0.805   1.00 11.68 ?  94  HIS   B HA   1 
ATOM   5216 H HB2  . HIS   B 1 94  ? 44.973 -14.757 2.430   1.00 12.29 ?  94  HIS   B HB2  1 
ATOM   5217 H HB3  . HIS   B 1 94  ? 45.458 -16.181 2.935   1.00 12.29 ?  94  HIS   B HB3  1 
ATOM   5218 H HD2  . HIS   B 1 94  ? 46.823 -13.396 0.912   1.00 12.64 ?  94  HIS   B HD2  1 
ATOM   5219 H HE1  . HIS   B 1 94  ? 49.724 -16.063 1.225   1.00 12.49 ?  94  HIS   B HE1  1 
ATOM   5220 H HE2  . HIS   B 1 94  ? 49.161 -13.884 0.497   1.00 13.16 ?  94  HIS   B HE2  1 
ATOM   5221 N N    . VAL   B 1 95  ? 42.725 -17.879 1.541   1.00 10.37 ?  95  VAL   B N    1 
ATOM   5222 C CA   . VAL   B 1 95  ? 41.396 -18.318 1.972   1.00 10.35 ?  95  VAL   B CA   1 
ATOM   5223 C C    . VAL   B 1 95  ? 41.563 -19.353 3.069   1.00 10.37 ?  95  VAL   B C    1 
ATOM   5224 O O    . VAL   B 1 95  ? 42.335 -20.306 2.912   1.00 11.29 ?  95  VAL   B O    1 
ATOM   5225 C CB   . VAL   B 1 95  ? 40.578 -18.921 0.813   1.00 10.78 ?  95  VAL   B CB   1 
ATOM   5226 C CG1  . VAL   B 1 95  ? 39.196 -19.372 1.299   1.00 11.89 ?  95  VAL   B CG1  1 
ATOM   5227 C CG2  . VAL   B 1 95  ? 40.452 -17.935 -0.323  1.00 10.90 ?  95  VAL   B CG2  1 
ATOM   5228 H H    . VAL   B 1 95  ? 43.195 -18.509 1.183   1.00 12.42 ?  95  VAL   B H    1 
ATOM   5229 H HA   . VAL   B 1 95  ? 40.904 -17.563 2.331   1.00 12.40 ?  95  VAL   B HA   1 
ATOM   5230 H HB   . VAL   B 1 95  ? 41.038 -19.703 0.475   1.00 12.91 ?  95  VAL   B HB   1 
ATOM   5231 H HG11 . VAL   B 1 95  ? 38.636 -19.570 0.527   1.00 14.25 ?  95  VAL   B HG11 1 
ATOM   5232 H HG12 . VAL   B 1 95  ? 39.290 -20.168 1.844   1.00 14.25 ?  95  VAL   B HG12 1 
ATOM   5233 H HG13 . VAL   B 1 95  ? 38.791 -18.659 1.819   1.00 14.25 ?  95  VAL   B HG13 1 
ATOM   5234 H HG21 . VAL   B 1 95  ? 39.877 -18.317 -1.005  1.00 13.05 ?  95  VAL   B HG21 1 
ATOM   5235 H HG22 . VAL   B 1 95  ? 40.063 -17.116 0.017   1.00 13.05 ?  95  VAL   B HG22 1 
ATOM   5236 H HG23 . VAL   B 1 95  ? 41.332 -17.766 -0.684  1.00 13.05 ?  95  VAL   B HG23 1 
ATOM   5237 N N    . VAL   B 1 96  ? 40.832 -19.183 4.165   1.00 10.55 ?  96  VAL   B N    1 
ATOM   5238 C CA   . VAL   B 1 96  ? 40.908 -20.095 5.306   1.00 11.04 ?  96  VAL   B CA   1 
ATOM   5239 C C    . VAL   B 1 96  ? 39.719 -21.059 5.261   1.00 11.80 ?  96  VAL   B C    1 
ATOM   5240 O O    . VAL   B 1 96  ? 38.597 -20.704 5.634   1.00 12.41 ?  96  VAL   B O    1 
ATOM   5241 C CB   . VAL   B 1 96  ? 40.961 -19.346 6.640   1.00 11.51 ?  96  VAL   B CB   1 
ATOM   5242 C CG1  . VAL   B 1 96  ? 41.140 -20.322 7.788   1.00 12.53 ?  96  VAL   B CG1  1 
ATOM   5243 C CG2  . VAL   B 1 96  ? 42.071 -18.308 6.638   1.00 12.47 ?  96  VAL   B CG2  1 
ATOM   5244 H H    . VAL   B 1 96  ? 40.268 -18.541 4.273   1.00 12.64 ?  96  VAL   B H    1 
ATOM   5245 H HA   . VAL   B 1 96  ? 41.722 -20.622 5.233   1.00 13.23 ?  96  VAL   B HA   1 
ATOM   5246 H HB   . VAL   B 1 96  ? 40.119 -18.882 6.773   1.00 13.79 ?  96  VAL   B HB   1 
ATOM   5247 H HG11 . VAL   B 1 96  ? 41.318 -19.823 8.605   1.00 15.02 ?  96  VAL   B HG11 1 
ATOM   5248 H HG12 . VAL   B 1 96  ? 40.333 -20.846 7.895   1.00 15.02 ?  96  VAL   B HG12 1 
ATOM   5249 H HG13 . VAL   B 1 96  ? 41.893 -20.906 7.595   1.00 15.02 ?  96  VAL   B HG13 1 
ATOM   5250 H HG21 . VAL   B 1 96  ? 42.124 -17.898 7.518   1.00 14.94 ?  96  VAL   B HG21 1 
ATOM   5251 H HG22 . VAL   B 1 96  ? 42.909 -18.735 6.420   1.00 14.94 ?  96  VAL   B HG22 1 
ATOM   5252 H HG23 . VAL   B 1 96  ? 41.864 -17.624 5.975   1.00 14.94 ?  96  VAL   B HG23 1 
ATOM   5253 N N    . GLY   B 1 97  ? 39.958 -22.290 4.825   1.00 11.90 ?  97  GLY   B N    1 
ATOM   5254 C CA   . GLY   B 1 97  ? 38.982 -23.347 4.980   1.00 12.42 ?  97  GLY   B CA   1 
ATOM   5255 C C    . GLY   B 1 97  ? 39.099 -23.949 6.362   1.00 13.23 ?  97  GLY   B C    1 
ATOM   5256 O O    . GLY   B 1 97  ? 40.132 -23.816 7.028   1.00 13.86 ?  97  GLY   B O    1 
ATOM   5257 H H    . GLY   B 1 97  ? 40.691 -22.535 4.437   1.00 14.25 ?  97  GLY   B H    1 
ATOM   5258 H HA2  . GLY   B 1 97  ? 38.090 -22.978 4.857   1.00 14.88 ?  97  GLY   B HA2  1 
ATOM   5259 H HA3  . GLY   B 1 97  ? 39.132 -24.033 4.312   1.00 14.88 ?  97  GLY   B HA3  1 
ATOM   5260 N N    . PRO   B 1 98  ? 38.051 -24.631 6.822   1.00 13.87 ?  98  PRO   B N    1 
ATOM   5261 C CA   . PRO   B 1 98  ? 38.144 -25.323 8.111   1.00 14.68 ?  98  PRO   B CA   1 
ATOM   5262 C C    . PRO   B 1 98  ? 39.172 -26.444 8.068   1.00 14.31 ?  98  PRO   B C    1 
ATOM   5263 O O    . PRO   B 1 98  ? 39.283 -27.178 7.086   1.00 14.82 ?  98  PRO   B O    1 
ATOM   5264 C CB   . PRO   B 1 98  ? 36.729 -25.870 8.318   1.00 14.91 ?  98  PRO   B CB   1 
ATOM   5265 C CG   . PRO   B 1 98  ? 36.170 -26.009 6.937   1.00 14.60 ?  98  PRO   B CG   1 
ATOM   5266 C CD   . PRO   B 1 98  ? 36.738 -24.835 6.181   1.00 13.90 ?  98  PRO   B CD   1 
ATOM   5267 H HA   . PRO   B 1 98  ? 38.368 -24.699 8.816   1.00 17.60 ?  98  PRO   B HA   1 
ATOM   5268 H HB2  . PRO   B 1 98  ? 36.777 -26.737 8.759   1.00 17.87 ?  98  PRO   B HB2  1 
ATOM   5269 H HB3  . PRO   B 1 98  ? 36.210 -25.245 8.839   1.00 17.87 ?  98  PRO   B HB3  1 
ATOM   5270 H HG2  . PRO   B 1 98  ? 36.467 -26.849 6.547   1.00 17.50 ?  98  PRO   B HG2  1 
ATOM   5271 H HG3  . PRO   B 1 98  ? 35.205 -25.968 6.970   1.00 17.50 ?  98  PRO   B HG3  1 
ATOM   5272 H HD2  . PRO   B 1 98  ? 36.844 -25.058 5.239   1.00 16.66 ?  98  PRO   B HD2  1 
ATOM   5273 H HD3  . PRO   B 1 98  ? 36.181 -24.052 6.299   1.00 16.66 ?  98  PRO   B HD3  1 
ATOM   5274 N N    . ASN   B 1 99  ? 39.926 -26.567 9.152   1.00 15.04 ?  99  ASN   B N    1 
ATOM   5275 C CA   . ASN   B 1 99  ? 40.902 -27.644 9.320   1.00 15.85 ?  99  ASN   B CA   1 
ATOM   5276 C C    . ASN   B 1 99  ? 40.264 -28.729 10.189  1.00 18.31 ?  99  ASN   B C    1 
ATOM   5277 O O    . ASN   B 1 99  ? 40.184 -28.592 11.411  1.00 19.05 ?  99  ASN   B O    1 
ATOM   5278 C CB   . ASN   B 1 99  ? 42.173 -27.091 9.951   1.00 16.56 ?  99  ASN   B CB   1 
ATOM   5279 C CG   . ASN   B 1 99  ? 43.301 -28.096 9.961   1.00 17.57 ?  99  ASN   B CG   1 
ATOM   5280 O OD1  . ASN   B 1 99  ? 43.071 -29.286 10.131  1.00 18.47 ?  99  ASN   B OD1  1 
ATOM   5281 N ND2  . ASN   B 1 99  ? 44.523 -27.623 9.772   1.00 17.71 ?  99  ASN   B ND2  1 
ATOM   5282 H H    . ASN   B 1 99  ? 39.892 -26.029 9.819   1.00 18.03 ?  99  ASN   B H    1 
ATOM   5283 H HA   . ASN   B 1 99  ? 41.121 -28.031 8.459   1.00 18.99 ?  99  ASN   B HA   1 
ATOM   5284 H HB2  . ASN   B 1 99  ? 42.460 -26.317 9.453   1.00 19.85 ?  99  ASN   B HB2  1 
ATOM   5285 H HB3  . ASN   B 1 99  ? 41.980 -26.844 10.873  1.00 19.85 ?  99  ASN   B HB3  1 
ATOM   5286 H HD21 . ASN   B 1 99  ? 45.194 -28.158 9.770   1.00 21.23 ?  99  ASN   B HD21 1 
ATOM   5287 H HD22 . ASN   B 1 99  ? 44.639 -26.780 9.658   1.00 21.23 ?  99  ASN   B HD22 1 
ATOM   5288 N N    A VAL   B 1 100 ? 39.798 -29.805 9.547   0.68 20.00 ?  100 VAL   B N    1 
ATOM   5289 N N    B VAL   B 1 100 ? 39.808 -29.807 9.545   0.32 20.15 ?  100 VAL   B N    1 
ATOM   5290 C CA   A VAL   B 1 100 ? 39.179 -30.908 10.280  0.68 22.79 ?  100 VAL   B CA   1 
ATOM   5291 C CA   B VAL   B 1 100 ? 39.183 -30.910 10.271  0.32 22.45 ?  100 VAL   B CA   1 
ATOM   5292 C C    A VAL   B 1 100 ? 40.180 -31.576 11.214  0.68 23.16 ?  100 VAL   B C    1 
ATOM   5293 C C    B VAL   B 1 100 ? 40.179 -31.579 11.209  0.32 23.07 ?  100 VAL   B C    1 
ATOM   5294 O O    A VAL   B 1 100 ? 39.805 -32.082 12.279  0.68 23.85 ?  100 VAL   B O    1 
ATOM   5295 O O    B VAL   B 1 100 ? 39.800 -32.082 12.274  0.32 23.44 ?  100 VAL   B O    1 
ATOM   5296 C CB   A VAL   B 1 100 ? 38.537 -31.914 9.301   0.68 25.14 ?  100 VAL   B CB   1 
ATOM   5297 C CB   B VAL   B 1 100 ? 38.551 -31.912 9.282   0.32 24.01 ?  100 VAL   B CB   1 
ATOM   5298 C CG1  A VAL   B 1 100 ? 38.056 -33.155 10.038  0.68 26.32 ?  100 VAL   B CG1  1 
ATOM   5299 C CG1  B VAL   B 1 100 ? 38.024 -33.137 10.016  0.32 24.73 ?  100 VAL   B CG1  1 
ATOM   5300 C CG2  A VAL   B 1 100 ? 37.386 -31.263 8.551   0.68 25.69 ?  100 VAL   B CG2  1 
ATOM   5301 C CG2  B VAL   B 1 100 ? 37.437 -31.243 8.495   0.32 24.42 ?  100 VAL   B CG2  1 
ATOM   5302 H H    A VAL   B 1 100 ? 39.817 -29.910 8.693   0.68 23.97 ?  100 VAL   B H    1 
ATOM   5303 H H    B VAL   B 1 100 ? 39.843 -29.919 8.693   0.32 24.16 ?  100 VAL   B H    1 
ATOM   5304 H HA   A VAL   B 1 100 ? 38.462 -30.550 10.824  0.68 27.32 ?  100 VAL   B HA   1 
ATOM   5305 H HA   B VAL   B 1 100 ? 38.465 -30.553 10.815  0.32 26.92 ?  100 VAL   B HA   1 
ATOM   5306 H HB   A VAL   B 1 100 ? 39.201 -32.191 8.654   0.68 30.15 ?  100 VAL   B HB   1 
ATOM   5307 H HB   B VAL   B 1 100 ? 39.227 -32.209 8.654   0.32 28.79 ?  100 VAL   B HB   1 
ATOM   5308 H HG11 A VAL   B 1 100 ? 37.467 -33.658 9.452   0.68 31.56 ?  100 VAL   B HG11 1 
ATOM   5309 H HG11 B VAL   B 1 100 ? 37.449 -33.639 9.415   0.32 29.66 ?  100 VAL   B HG11 1 
ATOM   5310 H HG12 A VAL   B 1 100 ? 38.820 -33.700 10.281  0.68 31.56 ?  100 VAL   B HG12 1 
ATOM   5311 H HG12 B VAL   B 1 100 ? 38.771 -33.690 10.293  0.32 29.66 ?  100 VAL   B HG12 1 
ATOM   5312 H HG13 A VAL   B 1 100 ? 37.573 -32.884 10.835  0.68 31.56 ?  100 VAL   B HG13 1 
ATOM   5313 H HG13 B VAL   B 1 100 ? 37.517 -32.848 10.790  0.32 29.66 ?  100 VAL   B HG13 1 
ATOM   5314 H HG21 A VAL   B 1 100 ? 36.998 -31.914 7.945   0.68 30.81 ?  100 VAL   B HG21 1 
ATOM   5315 H HG21 B VAL   B 1 100 ? 37.035 -31.894 7.900   0.32 29.28 ?  100 VAL   B HG21 1 
ATOM   5316 H HG22 A VAL   B 1 100 ? 36.718 -30.969 9.191   0.68 30.81 ?  100 VAL   B HG22 1 
ATOM   5317 H HG22 B VAL   B 1 100 ? 36.770 -30.908 9.116   0.32 29.28 ?  100 VAL   B HG22 1 
ATOM   5318 H HG23 A VAL   B 1 100 ? 37.723 -30.505 8.052   0.68 30.81 ?  100 VAL   B HG23 1 
ATOM   5319 H HG23 B VAL   B 1 100 ? 37.809 -30.510 7.982   0.32 29.28 ?  100 VAL   B HG23 1 
ATOM   5320 N N    . ASN   B 1 101 ? 41.459 -31.609 10.833  1.00 23.48 ?  101 ASN   B N    1 
ATOM   5321 C CA   . ASN   B 1 101 ? 42.491 -32.149 11.717  1.00 25.44 ?  101 ASN   B CA   1 
ATOM   5322 C C    . ASN   B 1 101 ? 42.682 -31.314 12.978  1.00 27.84 ?  101 ASN   B C    1 
ATOM   5323 O O    . ASN   B 1 101 ? 43.347 -31.777 13.912  1.00 29.19 ?  101 ASN   B O    1 
ATOM   5324 C CB   . ASN   B 1 101 ? 43.821 -32.274 10.971  1.00 25.67 ?  101 ASN   B CB   1 
ATOM   5325 C CG   . ASN   B 1 101 ? 43.822 -33.416 9.975   1.00 25.44 ?  101 ASN   B CG   1 
ATOM   5326 O OD1  . ASN   B 1 101 ? 43.163 -34.427 10.185  1.00 26.30 ?  101 ASN   B OD1  1 
ATOM   5327 N ND2  . ASN   B 1 101 ? 44.560 -33.256 8.884   1.00 25.02 ?  101 ASN   B ND2  1 
ATOM   5328 H H    A ASN   B 1 101 ? 41.746 -31.343 10.067  0.68 28.16 ?  101 ASN   B H    1 
ATOM   5329 H H    B ASN   B 1 101 ? 41.748 -31.334 10.071  0.32 28.16 ?  101 ASN   B H    1 
ATOM   5330 H HA   . ASN   B 1 101 ? 42.226 -33.037 11.993  1.00 30.51 ?  101 ASN   B HA   1 
ATOM   5331 H HB2  . ASN   B 1 101 ? 43.998 -31.455 10.485  1.00 30.78 ?  101 ASN   B HB2  1 
ATOM   5332 H HB3  . ASN   B 1 101 ? 44.530 -32.436 11.615  1.00 30.78 ?  101 ASN   B HB3  1 
ATOM   5333 H HD21 . ASN   B 1 101 ? 44.594 -33.880 8.291   1.00 30.01 ?  101 ASN   B HD21 1 
ATOM   5334 H HD22 . ASN   B 1 101 ? 45.006 -32.531 8.769   1.00 30.01 ?  101 ASN   B HD22 1 
ATOM   5335 N N    . LYS   B 1 102 ? 42.132 -30.098 13.016  1.00 29.85 ?  102 LYS   B N    1 
ATOM   5336 C CA   . LYS   B 1 102 ? 42.103 -29.265 14.212  1.00 32.26 ?  102 LYS   B CA   1 
ATOM   5337 C C    . LYS   B 1 102 ? 40.717 -29.210 14.841  1.00 31.63 ?  102 LYS   B C    1 
ATOM   5338 O O    . LYS   B 1 102 ? 40.487 -28.392 15.738  1.00 32.26 ?  102 LYS   B O    1 
ATOM   5339 C CB   . LYS   B 1 102 ? 42.550 -27.840 13.882  1.00 35.78 ?  102 LYS   B CB   1 
ATOM   5340 C CG   . LYS   B 1 102 ? 44.004 -27.693 13.474  1.00 39.24 ?  102 LYS   B CG   1 
ATOM   5341 C CD   . LYS   B 1 102 ? 44.272 -26.263 13.027  1.00 42.38 ?  102 LYS   B CD   1 
ATOM   5342 C CE   . LYS   B 1 102 ? 45.748 -25.995 12.796  1.00 44.78 ?  102 LYS   B CE   1 
ATOM   5343 N NZ   . LYS   B 1 102 ? 45.975 -24.586 12.360  1.00 46.18 ?  102 LYS   B NZ   1 
ATOM   5344 H H    . LYS   B 1 102 ? 41.756 -29.724 12.340  1.00 35.79 ?  102 LYS   B H    1 
ATOM   5345 H HA   . LYS   B 1 102 ? 42.721 -29.627 14.865  1.00 38.69 ?  102 LYS   B HA   1 
ATOM   5346 H HB2  . LYS   B 1 102 ? 42.005 -27.510 13.150  1.00 42.92 ?  102 LYS   B HB2  1 
ATOM   5347 H HB3  . LYS   B 1 102 ? 42.409 -27.284 14.666  1.00 42.92 ?  102 LYS   B HB3  1 
ATOM   5348 H HG2  . LYS   B 1 102 ? 44.577 -27.893 14.231  1.00 47.06 ?  102 LYS   B HG2  1 
ATOM   5349 H HG3  . LYS   B 1 102 ? 44.196 -28.290 12.734  1.00 47.06 ?  102 LYS   B HG3  1 
ATOM   5350 H HD2  . LYS   B 1 102 ? 43.801 -26.098 12.194  1.00 50.84 ?  102 LYS   B HD2  1 
ATOM   5351 H HD3  . LYS   B 1 102 ? 43.958 -25.653 13.713  1.00 50.84 ?  102 LYS   B HD3  1 
ATOM   5352 H HE2  . LYS   B 1 102 ? 46.236 -26.141 13.622  1.00 53.72 ?  102 LYS   B HE2  1 
ATOM   5353 H HE3  . LYS   B 1 102 ? 46.079 -26.586 12.101  1.00 53.72 ?  102 LYS   B HE3  1 
ATOM   5354 H HZ1  . LYS   B 1 102 ? 46.843 -24.444 12.229  1.00 55.40 ?  102 LYS   B HZ1  1 
ATOM   5355 H HZ2  . LYS   B 1 102 ? 45.537 -24.429 11.601  1.00 55.40 ?  102 LYS   B HZ2  1 
ATOM   5356 H HZ3  . LYS   B 1 102 ? 45.680 -24.024 12.984  1.00 55.40 ?  102 LYS   B HZ3  1 
ATOM   5357 N N    . GLY   B 1 103 ? 39.782 -30.035 14.378  1.00 30.60 ?  103 GLY   B N    1 
ATOM   5358 C CA   . GLY   B 1 103 ? 38.449 -30.070 14.943  1.00 29.91 ?  103 GLY   B CA   1 
ATOM   5359 C C    . GLY   B 1 103 ? 37.525 -28.964 14.489  1.00 28.70 ?  103 GLY   B C    1 
ATOM   5360 O O    . GLY   B 1 103 ? 36.447 -28.804 15.073  1.00 29.29 ?  103 GLY   B O    1 
ATOM   5361 H H    . GLY   B 1 103 ? 39.898 -30.586 13.730  1.00 36.69 ?  103 GLY   B H    1 
ATOM   5362 H HA2  . GLY   B 1 103 ? 38.032 -30.916 14.713  1.00 35.87 ?  103 GLY   B HA2  1 
ATOM   5363 H HA3  . GLY   B 1 103 ? 38.514 -30.024 15.911  1.00 35.87 ?  103 GLY   B HA3  1 
ATOM   5364 N N    A GLU   B 1 104 ? 37.908 -28.196 13.473  0.68 26.99 ?  104 GLU   B N    1 
ATOM   5365 N N    B GLU   B 1 104 ? 37.899 -28.199 13.470  0.32 28.04 ?  104 GLU   B N    1 
ATOM   5366 C CA   A GLU   B 1 104 ? 37.075 -27.102 13.001  0.68 25.32 ?  104 GLU   B CA   1 
ATOM   5367 C CA   B GLU   B 1 104 ? 37.063 -27.101 13.011  0.32 27.24 ?  104 GLU   B CA   1 
ATOM   5368 C C    A GLU   B 1 104 ? 35.910 -27.633 12.172  0.68 26.09 ?  104 GLU   B C    1 
ATOM   5369 C C    B GLU   B 1 104 ? 35.898 -27.622 12.175  0.32 27.53 ?  104 GLU   B C    1 
ATOM   5370 O O    A GLU   B 1 104 ? 35.972 -28.721 11.590  0.68 26.85 ?  104 GLU   B O    1 
ATOM   5371 O O    B GLU   B 1 104 ? 35.981 -28.677 11.539  0.32 27.88 ?  104 GLU   B O    1 
ATOM   5372 C CB   A GLU   B 1 104 ? 37.918 -26.099 12.209  0.68 23.43 ?  104 GLU   B CB   1 
ATOM   5373 C CB   B GLU   B 1 104 ? 37.898 -26.094 12.222  0.32 26.30 ?  104 GLU   B CB   1 
ATOM   5374 C CG   A GLU   B 1 104 ? 39.018 -25.483 13.066  0.68 22.00 ?  104 GLU   B CG   1 
ATOM   5375 C CG   B GLU   B 1 104 ? 38.996 -25.463 13.069  0.32 25.55 ?  104 GLU   B CG   1 
ATOM   5376 C CD   A GLU   B 1 104 ? 39.968 -24.578 12.309  0.68 20.57 ?  104 GLU   B CD   1 
ATOM   5377 C CD   B GLU   B 1 104 ? 39.937 -24.577 12.278  0.32 24.93 ?  104 GLU   B CD   1 
ATOM   5378 O OE1  A GLU   B 1 104 ? 39.993 -24.600 11.058  0.68 18.68 ?  104 GLU   B OE1  1 
ATOM   5379 O OE1  B GLU   B 1 104 ? 39.888 -24.599 11.029  0.32 24.35 ?  104 GLU   B OE1  1 
ATOM   5380 O OE2  A GLU   B 1 104 ? 40.700 -23.833 12.992  0.68 21.42 -1 104 GLU   B OE2  1 
ATOM   5381 O OE2  B GLU   B 1 104 ? 40.732 -23.856 12.915  0.32 25.16 -1 104 GLU   B OE2  1 
ATOM   5382 H H    A GLU   B 1 104 ? 38.652 -28.284 13.049  0.68 32.36 ?  104 GLU   B H    1 
ATOM   5383 H H    B GLU   B 1 104 ? 38.634 -28.292 13.033  0.32 33.63 ?  104 GLU   B H    1 
ATOM   5384 H HA   A GLU   B 1 104 ? 36.709 -26.637 13.769  0.68 30.36 ?  104 GLU   B HA   1 
ATOM   5385 H HA   B GLU   B 1 104 ? 36.697 -26.643 13.784  0.32 32.67 ?  104 GLU   B HA   1 
ATOM   5386 H HB2  A GLU   B 1 104 ? 38.334 -26.551 11.461  0.68 28.09 ?  104 GLU   B HB2  1 
ATOM   5387 H HB2  B GLU   B 1 104 ? 38.317 -26.545 11.473  0.32 31.54 ?  104 GLU   B HB2  1 
ATOM   5388 H HB3  A GLU   B 1 104 ? 37.345 -25.383 11.893  0.68 28.09 ?  104 GLU   B HB3  1 
ATOM   5389 H HB3  B GLU   B 1 104 ? 37.319 -25.384 11.901  0.32 31.54 ?  104 GLU   B HB3  1 
ATOM   5390 H HG2  A GLU   B 1 104 ? 38.611 -24.951 13.768  0.68 26.38 ?  104 GLU   B HG2  1 
ATOM   5391 H HG2  B GLU   B 1 104 ? 38.585 -24.921 13.762  0.32 30.63 ?  104 GLU   B HG2  1 
ATOM   5392 H HG3  A GLU   B 1 104 ? 39.549 -26.192 13.459  0.68 26.38 ?  104 GLU   B HG3  1 
ATOM   5393 H HG3  B GLU   B 1 104 ? 39.525 -26.167 13.474  0.32 30.63 ?  104 GLU   B HG3  1 
ATOM   5394 N N    A ASP   B 1 105 ? 34.832 -26.852 12.138  0.68 25.99 ?  105 ASP   B N    1 
ATOM   5395 N N    B ASP   B 1 105 ? 34.801 -26.867 12.189  0.32 27.37 ?  105 ASP   B N    1 
ATOM   5396 C CA   A ASP   B 1 105 ? 33.556 -27.312 11.605  0.68 27.06 ?  105 ASP   B CA   1 
ATOM   5397 C CA   B ASP   B 1 105 ? 33.544 -27.337 11.619  0.32 27.56 ?  105 ASP   B CA   1 
ATOM   5398 C C    A ASP   B 1 105 ? 33.607 -27.352 10.083  0.68 25.40 ?  105 ASP   B C    1 
ATOM   5399 C C    B ASP   B 1 105 ? 33.627 -27.361 10.096  0.32 26.32 ?  105 ASP   B C    1 
ATOM   5400 O O    A ASP   B 1 105 ? 33.752 -26.311 9.433   0.68 24.30 ?  105 ASP   B O    1 
ATOM   5401 O O    B ASP   B 1 105 ? 33.826 -26.321 9.459   0.32 26.00 ?  105 ASP   B O    1 
ATOM   5402 C CB   A ASP   B 1 105 ? 32.441 -26.378 12.072  0.68 29.95 ?  105 ASP   B CB   1 
ATOM   5403 C CB   B ASP   B 1 105 ? 32.401 -26.433 12.078  0.32 28.86 ?  105 ASP   B CB   1 
ATOM   5404 C CG   A ASP   B 1 105 ? 31.065 -26.839 11.628  0.68 32.44 ?  105 ASP   B CG   1 
ATOM   5405 C CG   B ASP   B 1 105 ? 31.034 -27.004 11.739  0.32 29.97 ?  105 ASP   B CG   1 
ATOM   5406 O OD1  A ASP   B 1 105 ? 30.963 -27.929 11.026  0.68 32.46 ?  105 ASP   B OD1  1 
ATOM   5407 O OD1  B ASP   B 1 105 ? 30.974 -28.005 10.994  0.32 30.20 ?  105 ASP   B OD1  1 
ATOM   5408 O OD2  A ASP   B 1 105 ? 30.082 -26.108 11.881  0.68 34.12 -1 105 ASP   B OD2  1 
ATOM   5409 O OD2  B ASP   B 1 105 ? 30.020 -26.461 12.228  0.32 30.28 -1 105 ASP   B OD2  1 
ATOM   5410 H H    A ASP   B 1 105 ? 34.820 -26.040 12.418  0.68 31.16 ?  105 ASP   B H    1 
ATOM   5411 H H    B ASP   B 1 105 ? 34.759 -26.077 12.524  0.32 32.82 ?  105 ASP   B H    1 
ATOM   5412 H HA   A ASP   B 1 105 ? 33.368 -28.205 11.931  0.68 32.45 ?  105 ASP   B HA   1 
ATOM   5413 H HA   B ASP   B 1 105 ? 33.361 -28.237 11.931  0.32 33.05 ?  105 ASP   B HA   1 
ATOM   5414 H HB2  A ASP   B 1 105 ? 32.458 -26.327 13.043  0.68 35.91 ?  105 ASP   B HB2  1 
ATOM   5415 H HB2  B ASP   B 1 105 ? 32.447 -26.326 13.042  0.32 34.61 ?  105 ASP   B HB2  1 
ATOM   5416 H HB3  A ASP   B 1 105 ? 32.586 -25.497 11.693  0.68 35.91 ?  105 ASP   B HB3  1 
ATOM   5417 H HB3  B ASP   B 1 105 ? 32.489 -25.566 11.647  0.32 34.61 ?  105 ASP   B HB3  1 
ATOM   5418 N N    . ILE   B 1 106 ? 33.463 -28.553 9.516   1.00 25.46 ?  106 ILE   B N    1 
ATOM   5419 C CA   . ILE   B 1 106 ? 33.467 -28.714 8.066   1.00 23.79 ?  106 ILE   B CA   1 
ATOM   5420 C C    . ILE   B 1 106 ? 32.373 -27.888 7.394   1.00 22.52 ?  106 ILE   B C    1 
ATOM   5421 O O    . ILE   B 1 106 ? 32.473 -27.576 6.202   1.00 21.46 ?  106 ILE   B O    1 
ATOM   5422 C CB   . ILE   B 1 106 ? 33.369 -30.219 7.718   1.00 24.60 ?  106 ILE   B CB   1 
ATOM   5423 C CG1  . ILE   B 1 106 ? 33.613 -30.453 6.229   1.00 24.78 ?  106 ILE   B CG1  1 
ATOM   5424 C CG2  . ILE   B 1 106 ? 32.016 -30.784 8.134   1.00 25.59 ?  106 ILE   B CG2  1 
ATOM   5425 C CD1  . ILE   B 1 106 ? 34.973 -29.990 5.769   1.00 24.71 ?  106 ILE   B CD1  1 
ATOM   5426 H H    A ILE   B 1 106 ? 33.364 -29.286 9.952   0.68 30.53 ?  106 ILE   B H    1 
ATOM   5427 H H    B ILE   B 1 106 ? 33.352 -29.287 9.948   0.32 30.53 ?  106 ILE   B H    1 
ATOM   5428 H HA   . ILE   B 1 106 ? 34.316 -28.389 7.734   1.00 28.52 ?  106 ILE   B HA   1 
ATOM   5429 H HB   . ILE   B 1 106 ? 34.058 -30.689 8.214   1.00 29.49 ?  106 ILE   B HB   1 
ATOM   5430 H HG12 . ILE   B 1 106 ? 33.552 -31.406 6.047   1.00 29.72 ?  106 ILE   B HG12 1 
ATOM   5431 H HG13 . ILE   B 1 106 ? 32.947 -29.976 5.715   1.00 29.72 ?  106 ILE   B HG13 1 
ATOM   5432 H HG21 . ILE   B 1 106 ? 32.028 -31.746 8.013   1.00 30.68 ?  106 ILE   B HG21 1 
ATOM   5433 H HG22 . ILE   B 1 106 ? 31.859 -30.570 9.067   1.00 30.68 ?  106 ILE   B HG22 1 
ATOM   5434 H HG23 . ILE   B 1 106 ? 31.325 -30.389 7.582   1.00 30.68 ?  106 ILE   B HG23 1 
ATOM   5435 H HD11 . ILE   B 1 106 ? 35.170 -30.388 4.907   1.00 29.63 ?  106 ILE   B HD11 1 
ATOM   5436 H HD12 . ILE   B 1 106 ? 34.971 -29.022 5.691   1.00 29.63 ?  106 ILE   B HD12 1 
ATOM   5437 H HD13 . ILE   B 1 106 ? 35.641 -30.268 6.418   1.00 29.63 ?  106 ILE   B HD13 1 
ATOM   5438 N N    A GLN   B 1 107 ? 31.327 -27.516 8.135   0.68 23.49 ?  107 GLN   B N    1 
ATOM   5439 N N    B GLN   B 1 107 ? 31.327 -27.514 8.135   0.32 23.25 ?  107 GLN   B N    1 
ATOM   5440 C CA   A GLN   B 1 107 ? 30.254 -26.715 7.558   0.68 24.10 ?  107 GLN   B CA   1 
ATOM   5441 C CA   B GLN   B 1 107 ? 30.251 -26.714 7.561   0.32 23.86 ?  107 GLN   B CA   1 
ATOM   5442 C C    A GLN   B 1 107 ? 30.747 -25.363 7.058   0.68 22.34 ?  107 GLN   B C    1 
ATOM   5443 C C    B GLN   B 1 107 ? 30.734 -25.351 7.077   0.32 22.19 ?  107 GLN   B C    1 
ATOM   5444 O O    A GLN   B 1 107 ? 30.116 -24.777 6.174   0.68 23.16 ?  107 GLN   B O    1 
ATOM   5445 O O    B GLN   B 1 107 ? 30.074 -24.740 6.231   0.32 22.72 ?  107 GLN   B O    1 
ATOM   5446 C CB   A GLN   B 1 107 ? 29.140 -26.527 8.592   0.68 27.77 ?  107 GLN   B CB   1 
ATOM   5447 C CB   B GLN   B 1 107 ? 29.129 -26.547 8.590   0.32 26.62 ?  107 GLN   B CB   1 
ATOM   5448 C CG   A GLN   B 1 107 ? 27.820 -26.015 8.027   0.68 31.54 ?  107 GLN   B CG   1 
ATOM   5449 C CG   B GLN   B 1 107 ? 27.807 -26.046 8.020   0.32 29.22 ?  107 GLN   B CG   1 
ATOM   5450 C CD   A GLN   B 1 107 ? 27.761 -24.500 7.940   0.68 34.28 ?  107 GLN   B CD   1 
ATOM   5451 C CD   B GLN   B 1 107 ? 27.702 -24.531 8.012   0.32 31.22 ?  107 GLN   B CD   1 
ATOM   5452 O OE1  A GLN   B 1 107 ? 28.596 -23.798 8.515   0.68 35.29 ?  107 GLN   B OE1  1 
ATOM   5453 O OE1  B GLN   B 1 107 ? 28.529 -23.834 8.603   0.32 31.93 ?  107 GLN   B OE1  1 
ATOM   5454 N NE2  A GLN   B 1 107 ? 26.767 -23.987 7.219   0.68 35.26 ?  107 GLN   B NE2  1 
ATOM   5455 N NE2  B GLN   B 1 107 ? 26.677 -24.014 7.343   0.32 31.97 ?  107 GLN   B NE2  1 
ATOM   5456 H H    A GLN   B 1 107 ? 31.225 -27.702 8.964   0.68 28.17 ?  107 GLN   B H    1 
ATOM   5457 H H    B GLN   B 1 107 ? 31.221 -27.712 8.961   0.32 27.87 ?  107 GLN   B H    1 
ATOM   5458 H HA   A GLN   B 1 107 ? 29.877 -27.196 6.803   0.68 28.89 ?  107 GLN   B HA   1 
ATOM   5459 H HA   B GLN   B 1 107 ? 29.883 -27.188 6.798   0.32 28.61 ?  107 GLN   B HA   1 
ATOM   5460 H HB2  A GLN   B 1 107 ? 28.964 -27.381 9.011   0.68 33.31 ?  107 GLN   B HB2  1 
ATOM   5461 H HB2  B GLN   B 1 107 ? 28.959 -27.407 9.001   0.32 31.92 ?  107 GLN   B HB2  1 
ATOM   5462 H HB3  A GLN   B 1 107 ? 29.442 -25.893 9.260   0.68 33.31 ?  107 GLN   B HB3  1 
ATOM   5463 H HB3  B GLN   B 1 107 ? 29.420 -25.915 9.266   0.32 31.92 ?  107 GLN   B HB3  1 
ATOM   5464 H HG2  A GLN   B 1 107 ? 27.697 -26.367 7.133   0.68 37.82 ?  107 GLN   B HG2  1 
ATOM   5465 H HG2  B GLN   B 1 107 ? 27.717 -26.355 7.106   0.32 35.04 ?  107 GLN   B HG2  1 
ATOM   5466 H HG3  A GLN   B 1 107 ? 27.094 -26.313 8.602   0.68 37.82 ?  107 GLN   B HG3  1 
ATOM   5467 H HG3  B GLN   B 1 107 ? 27.078 -26.396 8.560   0.32 35.04 ?  107 GLN   B HG3  1 
ATOM   5468 H HE21 A GLN   B 1 107 ? 26.203 -24.509 6.830   0.68 42.28 ?  107 GLN   B HE21 1 
ATOM   5469 H HE21 B GLN   B 1 107 ? 26.119 -24.532 6.941   0.32 38.34 ?  107 GLN   B HE21 1 
ATOM   5470 H HE22 A GLN   B 1 107 ? 26.686 -23.134 7.142   0.68 42.28 ?  107 GLN   B HE22 1 
ATOM   5471 H HE22 B GLN   B 1 107 ? 26.570 -23.161 7.311   0.32 38.34 ?  107 GLN   B HE22 1 
ATOM   5472 N N    . LEU   B 1 108 ? 31.868 -24.865 7.587   1.00 20.26 ?  108 LEU   B N    1 
ATOM   5473 C CA   . LEU   B 1 108 ? 32.417 -23.570 7.175   1.00 18.10 ?  108 LEU   B CA   1 
ATOM   5474 C C    . LEU   B 1 108 ? 33.059 -23.596 5.796   1.00 15.77 ?  108 LEU   B C    1 
ATOM   5475 O O    . LEU   B 1 108 ? 33.489 -22.540 5.307   1.00 15.52 ?  108 LEU   B O    1 
ATOM   5476 C CB   . LEU   B 1 108 ? 33.425 -23.081 8.214   1.00 18.88 ?  108 LEU   B CB   1 
ATOM   5477 C CG   . LEU   B 1 108 ? 32.799 -22.608 9.525   1.00 20.25 ?  108 LEU   B CG   1 
ATOM   5478 C CD1  . LEU   B 1 108 ? 33.825 -22.562 10.643  1.00 20.54 ?  108 LEU   B CD1  1 
ATOM   5479 C CD2  . LEU   B 1 108 ? 32.181 -21.234 9.325   1.00 21.43 ?  108 LEU   B CD2  1 
ATOM   5480 H H    A LEU   B 1 108 ? 32.322 -25.261 8.199   0.68 24.29 ?  108 LEU   B H    1 
ATOM   5481 H H    B LEU   B 1 108 ? 32.334 -25.270 8.184   0.32 24.29 ?  108 LEU   B H    1 
ATOM   5482 H HA   . LEU   B 1 108 ? 31.692 -22.931 7.146   1.00 21.69 ?  108 LEU   B HA   1 
ATOM   5483 H HB2  . LEU   B 1 108 ? 34.031 -23.805 8.429   1.00 22.64 ?  108 LEU   B HB2  1 
ATOM   5484 H HB3  . LEU   B 1 108 ? 33.917 -22.336 7.842   1.00 22.64 ?  108 LEU   B HB3  1 
ATOM   5485 H HG   . LEU   B 1 108 ? 32.090 -23.220 9.787   1.00 24.28 ?  108 LEU   B HG   1 
ATOM   5486 H HD11 . LEU   B 1 108 ? 33.384 -22.299 11.468  1.00 24.63 ?  108 LEU   B HD11 1 
ATOM   5487 H HD12 . LEU   B 1 108 ? 34.219 -23.441 10.745  1.00 24.63 ?  108 LEU   B HD12 1 
ATOM   5488 H HD13 . LEU   B 1 108 ? 34.510 -21.915 10.415  1.00 24.63 ?  108 LEU   B HD13 1 
ATOM   5489 H HD21 . LEU   B 1 108 ? 31.839 -20.913 10.173  1.00 25.69 ?  108 LEU   B HD21 1 
ATOM   5490 H HD22 . LEU   B 1 108 ? 32.863 -20.629 8.993   1.00 25.69 ?  108 LEU   B HD22 1 
ATOM   5491 H HD23 . LEU   B 1 108 ? 31.458 -21.302 8.681   1.00 25.69 ?  108 LEU   B HD23 1 
ATOM   5492 N N    . LEU   B 1 109 ? 33.128 -24.765 5.164   1.00 14.72 ?  109 LEU   B N    1 
ATOM   5493 C CA   . LEU   B 1 109 ? 33.760 -24.874 3.856   1.00 14.09 ?  109 LEU   B CA   1 
ATOM   5494 C C    . LEU   B 1 109 ? 32.997 -24.086 2.795   1.00 13.31 ?  109 LEU   B C    1 
ATOM   5495 O O    . LEU   B 1 109 ? 33.613 -23.500 1.898   1.00 13.02 ?  109 LEU   B O    1 
ATOM   5496 C CB   . LEU   B 1 109 ? 33.887 -26.351 3.472   1.00 14.48 ?  109 LEU   B CB   1 
ATOM   5497 C CG   . LEU   B 1 109 ? 34.669 -26.688 2.203   1.00 14.09 ?  109 LEU   B CG   1 
ATOM   5498 C CD1  . LEU   B 1 109 ? 36.047 -26.036 2.221   1.00 13.80 ?  109 LEU   B CD1  1 
ATOM   5499 C CD2  . LEU   B 1 109 ? 34.788 -28.197 2.049   1.00 14.58 ?  109 LEU   B CD2  1 
ATOM   5500 H H    . LEU   B 1 109 ? 32.826 -25.508 5.468   1.00 17.64 ?  109 LEU   B H    1 
ATOM   5501 H HA   . LEU   B 1 109 ? 34.654 -24.505 3.907   1.00 16.89 ?  109 LEU   B HA   1 
ATOM   5502 H HB2  . LEU   B 1 109 ? 34.331 -26.814 4.201   1.00 17.35 ?  109 LEU   B HB2  1 
ATOM   5503 H HB3  . LEU   B 1 109 ? 32.997 -26.714 3.359   1.00 17.35 ?  109 LEU   B HB3  1 
ATOM   5504 H HG   . LEU   B 1 109 ? 34.184 -26.351 1.431   1.00 16.89 ?  109 LEU   B HG   1 
ATOM   5505 H HD11 . LEU   B 1 109 ? 36.576 -26.392 1.489   1.00 16.54 ?  109 LEU   B HD11 1 
ATOM   5506 H HD12 . LEU   B 1 109 ? 35.945 -25.078 2.119   1.00 16.54 ?  109 LEU   B HD12 1 
ATOM   5507 H HD13 . LEU   B 1 109 ? 36.479 -26.237 3.067   1.00 16.54 ?  109 LEU   B HD13 1 
ATOM   5508 H HD21 . LEU   B 1 109 ? 35.364 -28.393 1.291   1.00 17.47 ?  109 LEU   B HD21 1 
ATOM   5509 H HD22 . LEU   B 1 109 ? 35.171 -28.567 2.858   1.00 17.47 ?  109 LEU   B HD22 1 
ATOM   5510 H HD23 . LEU   B 1 109 ? 33.905 -28.572 1.898   1.00 17.47 ?  109 LEU   B HD23 1 
ATOM   5511 N N    . LYS   B 1 110 ? 31.662 -24.052 2.872   1.00 12.95 ?  110 LYS   B N    1 
ATOM   5512 C CA   . LYS   B 1 110 ? 30.908 -23.294 1.878   1.00 12.90 ?  110 LYS   B CA   1 
ATOM   5513 C C    . LYS   B 1 110 ? 31.242 -21.804 1.966   1.00 12.72 ?  110 LYS   B C    1 
ATOM   5514 O O    . LYS   B 1 110 ? 31.492 -21.153 0.947   1.00 12.43 ?  110 LYS   B O    1 
ATOM   5515 C CB   . LYS   B 1 110 ? 29.404 -23.545 2.024   1.00 13.82 ?  110 LYS   B CB   1 
ATOM   5516 C CG   . LYS   B 1 110 ? 28.596 -22.927 0.889   1.00 14.07 ?  110 LYS   B CG   1 
ATOM   5517 C CD   . LYS   B 1 110 ? 27.132 -23.357 0.917   1.00 14.45 ?  110 LYS   B CD   1 
ATOM   5518 C CE   . LYS   B 1 110 ? 26.368 -22.838 -0.300  1.00 15.48 ?  110 LYS   B CE   1 
ATOM   5519 N NZ   . LYS   B 1 110 ? 26.703 -23.550 -1.560  1.00 15.49 ?  110 LYS   B NZ   1 
ATOM   5520 H H    . LYS   B 1 110 ? 31.189 -24.458 3.463   1.00 15.52 ?  110 LYS   B H    1 
ATOM   5521 H HA   . LYS   B 1 110 ? 31.170 -23.600 0.994   1.00 15.46 ?  110 LYS   B HA   1 
ATOM   5522 H HB2  . LYS   B 1 110 ? 29.243 -24.505 2.019   1.00 16.56 ?  110 LYS   B HB2  1 
ATOM   5523 H HB3  . LYS   B 1 110 ? 29.099 -23.164 2.859   1.00 16.56 ?  110 LYS   B HB3  1 
ATOM   5524 H HG2  . LYS   B 1 110 ? 28.620 -21.960 0.969   1.00 16.86 ?  110 LYS   B HG2  1 
ATOM   5525 H HG3  . LYS   B 1 110 ? 28.970 -23.200 0.039   1.00 16.86 ?  110 LYS   B HG3  1 
ATOM   5526 H HD2  . LYS   B 1 110 ? 27.083 -24.329 0.916   1.00 17.32 ?  110 LYS   B HD2  1 
ATOM   5527 H HD3  . LYS   B 1 110 ? 26.706 -23.005 1.715   1.00 17.32 ?  110 LYS   B HD3  1 
ATOM   5528 H HE2  . LYS   B 1 110 ? 25.418 -22.945 -0.146  1.00 18.55 ?  110 LYS   B HE2  1 
ATOM   5529 H HE3  . LYS   B 1 110 ? 26.582 -21.902 -0.426  1.00 18.55 ?  110 LYS   B HE3  1 
ATOM   5530 H HZ1  . LYS   B 1 110 ? 26.238 -23.211 -2.237  1.00 18.56 ?  110 LYS   B HZ1  1 
ATOM   5531 H HZ2  . LYS   B 1 110 ? 27.574 -23.465 -1.737  1.00 18.56 ?  110 LYS   B HZ2  1 
ATOM   5532 H HZ3  . LYS   B 1 110 ? 26.512 -24.417 -1.482  1.00 18.56 ?  110 LYS   B HZ3  1 
ATOM   5533 N N    . SER   B 1 111 ? 31.269 -21.255 3.185   1.00 13.47 ?  111 SER   B N    1 
ATOM   5534 C CA   . SER   B 1 111 ? 31.654 -19.855 3.360   1.00 13.04 ?  111 SER   B CA   1 
ATOM   5535 C C    . SER   B 1 111 ? 33.036 -19.592 2.776   1.00 12.82 ?  111 SER   B C    1 
ATOM   5536 O O    . SER   B 1 111 ? 33.261 -18.563 2.126   1.00 12.80 ?  111 SER   B O    1 
ATOM   5537 C CB   . SER   B 1 111 ? 31.642 -19.489 4.842   1.00 14.49 ?  111 SER   B CB   1 
ATOM   5538 O OG   . SER   B 1 111 ? 30.339 -19.522 5.383   1.00 16.36 ?  111 SER   B OG   1 
ATOM   5539 H H    . SER   B 1 111 ? 31.077 -21.669 3.914   1.00 16.15 ?  111 SER   B H    1 
ATOM   5540 H HA   . SER   B 1 111 ? 31.020 -19.289 2.897   1.00 15.62 ?  111 SER   B HA   1 
ATOM   5541 H HB2  . SER   B 1 111 ? 32.193 -20.122 5.328   1.00 17.37 ?  111 SER   B HB2  1 
ATOM   5542 H HB3  . SER   B 1 111 ? 31.995 -18.594 4.948   1.00 17.37 ?  111 SER   B HB3  1 
ATOM   5543 H HG   . SER   B 1 111 ? 30.048 -20.314 5.397   1.00 19.61 ?  111 SER   B HG   1 
ATOM   5544 N N    . ALA   B 1 112 ? 33.975 -20.515 2.993   1.00 12.79 ?  112 ALA   B N    1 
ATOM   5545 C CA   . ALA   B 1 112 ? 35.321 -20.344 2.453   1.00 12.55 ?  112 ALA   B CA   1 
ATOM   5546 C C    . ALA   B 1 112 ? 35.293 -20.247 0.930   1.00 11.96 ?  112 ALA   B C    1 
ATOM   5547 O O    . ALA   B 1 112 ? 35.922 -19.358 0.335   1.00 12.18 ?  112 ALA   B O    1 
ATOM   5548 C CB   . ALA   B 1 112 ? 36.233 -21.482 2.926   1.00 13.37 ?  112 ALA   B CB   1 
ATOM   5549 H H    . ALA   B 1 112 ? 33.861 -21.243 3.449   1.00 15.33 ?  112 ALA   B H    1 
ATOM   5550 H HA   . ALA   B 1 112 ? 35.686 -19.512 2.798   1.00 15.04 ?  112 ALA   B HA   1 
ATOM   5551 H HB1  . ALA   B 1 112 ? 37.124 -21.339 2.563   1.00 16.02 ?  112 ALA   B HB1  1 
ATOM   5552 H HB2  . ALA   B 1 112 ? 36.273 -21.472 3.898   1.00 16.02 ?  112 ALA   B HB2  1 
ATOM   5553 H HB3  . ALA   B 1 112 ? 35.877 -22.323 2.616   1.00 16.02 ?  112 ALA   B HB3  1 
ATOM   5554 N N    . TYR   B 1 113 ? 34.562 -21.154 0.277   1.00 11.88 ?  113 TYR   B N    1 
ATOM   5555 C CA   . TYR   B 1 113 ? 34.488 -21.106 -1.176  1.00 11.67 ?  113 TYR   B CA   1 
ATOM   5556 C C    . TYR   B 1 113 ? 33.779 -19.853 -1.690  1.00 11.09 ?  113 TYR   B C    1 
ATOM   5557 O O    . TYR   B 1 113 ? 34.047 -19.422 -2.815  1.00 11.18 ?  113 TYR   B O    1 
ATOM   5558 C CB   . TYR   B 1 113 ? 33.816 -22.368 -1.722  1.00 11.56 ?  113 TYR   B CB   1 
ATOM   5559 C CG   . TYR   B 1 113 ? 34.777 -23.518 -1.982  1.00 11.96 ?  113 TYR   B CG   1 
ATOM   5560 C CD1  . TYR   B 1 113 ? 35.771 -23.411 -2.947  1.00 12.63 ?  113 TYR   B CD1  1 
ATOM   5561 C CD2  . TYR   B 1 113 ? 34.679 -24.707 -1.277  1.00 12.33 ?  113 TYR   B CD2  1 
ATOM   5562 C CE1  . TYR   B 1 113 ? 36.647 -24.443 -3.195  1.00 12.62 ?  113 TYR   B CE1  1 
ATOM   5563 C CE2  . TYR   B 1 113 ? 35.548 -25.758 -1.524  1.00 12.74 ?  113 TYR   B CE2  1 
ATOM   5564 C CZ   . TYR   B 1 113 ? 36.530 -25.622 -2.487  1.00 12.72 ?  113 TYR   B CZ   1 
ATOM   5565 O OH   . TYR   B 1 113 ? 37.414 -26.638 -2.766  1.00 13.42 ?  113 TYR   B OH   1 
ATOM   5566 H H    . TYR   B 1 113 ? 34.106 -21.787 0.652   1.00 14.24 ?  113 TYR   B H    1 
ATOM   5567 H HA   . TYR   B 1 113 ? 35.389 -21.087 -1.513  1.00 13.98 ?  113 TYR   B HA   1 
ATOM   5568 H HB2  . TYR   B 1 113 ? 33.155 -22.679 -1.079  1.00 13.85 ?  113 TYR   B HB2  1 
ATOM   5569 H HB3  . TYR   B 1 113 ? 33.378 -22.148 -2.558  1.00 13.85 ?  113 TYR   B HB3  1 
ATOM   5570 H HD1  . TYR   B 1 113 ? 35.852 -22.617 -3.432  1.00 15.14 ?  113 TYR   B HD1  1 
ATOM   5571 H HD2  . TYR   B 1 113 ? 34.017 -24.803 -0.638  1.00 14.77 ?  113 TYR   B HD2  1 
ATOM   5572 H HE1  . TYR   B 1 113 ? 37.306 -24.350 -3.852  1.00 15.12 ?  113 TYR   B HE1  1 
ATOM   5573 H HE2  . TYR   B 1 113 ? 35.472 -26.556 -1.050  1.00 15.26 ?  113 TYR   B HE2  1 
ATOM   5574 H HH   . TYR   B 1 113 ? 37.245 -27.305 -2.289  1.00 16.08 ?  113 TYR   B HH   1 
ATOM   5575 N N    . GLU   B 1 114 ? 32.856 -19.272 -0.910  1.00 11.53 ?  114 GLU   B N    1 
ATOM   5576 C CA   . GLU   B 1 114 ? 32.170 -18.067 -1.369  1.00 11.54 ?  114 GLU   B CA   1 
ATOM   5577 C C    . GLU   B 1 114 ? 33.152 -16.941 -1.662  1.00 11.11 ?  114 GLU   B C    1 
ATOM   5578 O O    . GLU   B 1 114 ? 32.878 -16.088 -2.507  1.00 11.60 ?  114 GLU   B O    1 
ATOM   5579 C CB   . GLU   B 1 114 ? 31.106 -17.641 -0.357  1.00 12.24 ?  114 GLU   B CB   1 
ATOM   5580 C CG   . GLU   B 1 114 ? 29.899 -18.562 -0.426  1.00 12.01 ?  114 GLU   B CG   1 
ATOM   5581 C CD   . GLU   B 1 114 ? 28.876 -18.374 0.683   1.00 12.37 ?  114 GLU   B CD   1 
ATOM   5582 O OE1  . GLU   B 1 114 ? 29.168 -17.753 1.725   1.00 12.80 ?  114 GLU   B OE1  1 
ATOM   5583 O OE2  . GLU   B 1 114 ? 27.753 -18.913 0.526   1.00 13.25 -1 114 GLU   B OE2  1 
ATOM   5584 H H    . GLU   B 1 114 ? 32.609 -19.559 -0.131  1.00 13.81 ?  114 GLU   B H    1 
ATOM   5585 H HA   . GLU   B 1 114 ? 31.719 -18.271 -2.196  1.00 13.83 ?  114 GLU   B HA   1 
ATOM   5586 H HB2  . GLU   B 1 114 ? 31.474 -17.683 0.540   1.00 14.66 ?  114 GLU   B HB2  1 
ATOM   5587 H HB3  . GLU   B 1 114 ? 30.812 -16.739 -0.561  1.00 14.66 ?  114 GLU   B HB3  1 
ATOM   5588 H HG2  . GLU   B 1 114 ? 29.447 -18.417 -1.269  1.00 14.38 ?  114 GLU   B HG2  1 
ATOM   5589 H HG3  . GLU   B 1 114 ? 30.214 -19.482 -0.380  1.00 14.38 ?  114 GLU   B HG3  1 
ATOM   5590 N N    . ASN   B 1 115 ? 34.318 -16.937 -1.012  1.00 11.02 ?  115 ASN   B N    1 
ATOM   5591 C CA   . ASN   B 1 115 ? 35.307 -15.903 -1.307  1.00 10.94 ?  115 ASN   B CA   1 
ATOM   5592 C C    . ASN   B 1 115 ? 35.724 -15.925 -2.770  1.00 10.96 ?  115 ASN   B C    1 
ATOM   5593 O O    . ASN   B 1 115 ? 36.109 -14.881 -3.322  1.00 11.75 ?  115 ASN   B O    1 
ATOM   5594 C CB   . ASN   B 1 115 ? 36.546 -16.082 -0.423  1.00 11.91 ?  115 ASN   B CB   1 
ATOM   5595 C CG   . ASN   B 1 115 ? 36.271 -15.820 1.037   1.00 12.20 ?  115 ASN   B CG   1 
ATOM   5596 O OD1  . ASN   B 1 115 ? 36.260 -14.675 1.475   1.00 14.13 ?  115 ASN   B OD1  1 
ATOM   5597 N ND2  . ASN   B 1 115 ? 36.110 -16.885 1.816   1.00 12.58 ?  115 ASN   B ND2  1 
ATOM   5598 H H    . ASN   B 1 115 ? 34.557 -17.506 -0.406  1.00 13.20 ?  115 ASN   B H    1 
ATOM   5599 H HA   . ASN   B 1 115 ? 34.927 -15.033 -1.116  1.00 13.11 ?  115 ASN   B HA   1 
ATOM   5600 H HB2  . ASN   B 1 115 ? 36.870 -16.992 -0.509  1.00 14.26 ?  115 ASN   B HB2  1 
ATOM   5601 H HB3  . ASN   B 1 115 ? 37.232 -15.458 -0.706  1.00 14.26 ?  115 ASN   B HB3  1 
ATOM   5602 H HD21 . ASN   B 1 115 ? 35.959 -16.785 2.659   1.00 15.07 ?  115 ASN   B HD21 1 
ATOM   5603 H HD22 . ASN   B 1 115 ? 36.137 -17.677 1.480   1.00 15.07 ?  115 ASN   B HD22 1 
ATOM   5604 N N    . PHE   B 1 116 ? 35.695 -17.102 -3.406  1.00 10.67 ?  116 PHE   B N    1 
ATOM   5605 C CA   . PHE   B 1 116 ? 36.125 -17.194 -4.795  1.00 11.16 ?  116 PHE   B CA   1 
ATOM   5606 C C    . PHE   B 1 116 ? 35.230 -16.358 -5.707  1.00 10.61 ?  116 PHE   B C    1 
ATOM   5607 O O    . PHE   B 1 116 ? 35.668 -15.923 -6.776  1.00 11.31 ?  116 PHE   B O    1 
ATOM   5608 C CB   . PHE   B 1 116 ? 36.089 -18.640 -5.315  1.00 10.46 ?  116 PHE   B CB   1 
ATOM   5609 C CG   . PHE   B 1 116 ? 37.163 -19.598 -4.770  1.00 10.56 ?  116 PHE   B CG   1 
ATOM   5610 C CD1  . PHE   B 1 116 ? 37.817 -19.412 -3.566  1.00 11.55 ?  116 PHE   B CD1  1 
ATOM   5611 C CD2  . PHE   B 1 116 ? 37.467 -20.733 -5.507  1.00 10.86 ?  116 PHE   B CD2  1 
ATOM   5612 C CE1  . PHE   B 1 116 ? 38.753 -20.349 -3.114  1.00 11.42 ?  116 PHE   B CE1  1 
ATOM   5613 C CE2  . PHE   B 1 116 ? 38.396 -21.670 -5.060  1.00 11.17 ?  116 PHE   B CE2  1 
ATOM   5614 C CZ   . PHE   B 1 116 ? 39.036 -21.474 -3.867  1.00 11.18 ?  116 PHE   B CZ   1 
ATOM   5615 H H    . PHE   B 1 116 ? 35.426 -17.846 -3.062  1.00 12.79 ?  116 PHE   B H    1 
ATOM   5616 H HA   . PHE   B 1 116 ? 37.034 -16.869 -4.873  1.00 13.37 ?  116 PHE   B HA   1 
ATOM   5617 H HB2  . PHE   B 1 116 ? 35.220 -19.022 -5.092  1.00 12.53 ?  116 PHE   B HB2  1 
ATOM   5618 H HB3  . PHE   B 1 116 ? 36.182 -18.620 -6.282  1.00 12.53 ?  116 PHE   B HB3  1 
ATOM   5619 H HD1  . PHE   B 1 116 ? 37.619 -18.665 -3.047  1.00 13.84 ?  116 PHE   B HD1  1 
ATOM   5620 H HD2  . PHE   B 1 116 ? 37.025 -20.887 -6.314  1.00 13.01 ?  116 PHE   B HD2  1 
ATOM   5621 H HE1  . PHE   B 1 116 ? 39.191 -20.213 -2.305  1.00 13.68 ?  116 PHE   B HE1  1 
ATOM   5622 H HE2  . PHE   B 1 116 ? 38.587 -22.420 -5.574  1.00 13.38 ?  116 PHE   B HE2  1 
ATOM   5623 H HZ   . PHE   B 1 116 ? 39.670 -22.085 -3.570  1.00 13.40 ?  116 PHE   B HZ   1 
ATOM   5624 N N    . ASN   B 1 117 ? 33.958 -16.168 -5.331  1.00 11.27 ?  117 ASN   B N    1 
ATOM   5625 C CA   . ASN   B 1 117 ? 33.013 -15.462 -6.195  1.00 11.56 ?  117 ASN   B CA   1 
ATOM   5626 C C    . ASN   B 1 117 ? 33.333 -13.985 -6.345  1.00 11.88 ?  117 ASN   B C    1 
ATOM   5627 O O    . ASN   B 1 117 ? 32.733 -13.328 -7.200  1.00 13.10 ?  117 ASN   B O    1 
ATOM   5628 C CB   . ASN   B 1 117 ? 31.588 -15.680 -5.706  1.00 11.71 ?  117 ASN   B CB   1 
ATOM   5629 C CG   . ASN   B 1 117 ? 31.137 -17.090 -5.953  1.00 11.63 ?  117 ASN   B CG   1 
ATOM   5630 O OD1  . ASN   B 1 117 ? 31.489 -17.683 -6.978  1.00 12.77 ?  117 ASN   B OD1  1 
ATOM   5631 N ND2  . ASN   B 1 117 ? 30.404 -17.662 -5.005  1.00 11.94 ?  117 ASN   B ND2  1 
ATOM   5632 H H    . ASN   B 1 117 ? 33.629 -16.431 -4.575  1.00 13.50 ?  117 ASN   B H    1 
ATOM   5633 H HA   . ASN   B 1 117 ? 33.071 -15.859 -7.072  1.00 13.85 ?  117 ASN   B HA   1 
ATOM   5634 H HB2  . ASN   B 1 117 ? 31.541 -15.506 -4.746  1.00 14.02 ?  117 ASN   B HB2  1 
ATOM   5635 H HB3  . ASN   B 1 117 ? 30.990 -15.074 -6.176  1.00 14.02 ?  117 ASN   B HB3  1 
ATOM   5636 H HD21 . ASN   B 1 117 ? 30.127 -18.471 -5.102  1.00 14.30 ?  117 ASN   B HD21 1 
ATOM   5637 H HD22 . ASN   B 1 117 ? 30.186 -17.220 -4.295  1.00 14.30 ?  117 ASN   B HD22 1 
ATOM   5638 N N    . GLN   B 1 118 ? 34.262 -13.457 -5.559  1.00 11.39 ?  118 GLN   B N    1 
ATOM   5639 C CA   . GLN   B 1 118 ? 34.693 -12.071 -5.696  1.00 11.88 ?  118 GLN   B CA   1 
ATOM   5640 C C    . GLN   B 1 118 ? 35.763 -11.881 -6.765  1.00 12.26 ?  118 GLN   B C    1 
ATOM   5641 O O    . GLN   B 1 118 ? 36.226 -10.751 -6.951  1.00 13.74 ?  118 GLN   B O    1 
ATOM   5642 C CB   . GLN   B 1 118 ? 35.163 -11.537 -4.339  1.00 12.76 ?  118 GLN   B CB   1 
ATOM   5643 C CG   . GLN   B 1 118 ? 34.073 -11.586 -3.276  1.00 12.88 ?  118 GLN   B CG   1 
ATOM   5644 C CD   . GLN   B 1 118 ? 32.906 -10.672 -3.603  1.00 12.69 ?  118 GLN   B CD   1 
ATOM   5645 O OE1  . GLN   B 1 118 ? 33.094 -9.529  -4.040  1.00 13.23 ?  118 GLN   B OE1  1 
ATOM   5646 N NE2  . GLN   B 1 118 ? 31.695 -11.159 -3.393  1.00 13.41 ?  118 GLN   B NE2  1 
ATOM   5647 H H    . GLN   B 1 118 ? 34.677 -13.885 -4.931  1.00 13.64 ?  118 GLN   B H    1 
ATOM   5648 H HA   . GLN   B 1 118 ? 33.925 -11.543 -5.965  1.00 14.23 ?  118 GLN   B HA   1 
ATOM   5649 H HB2  . GLN   B 1 118 ? 35.906 -12.064 -4.025  1.00 15.29 ?  118 GLN   B HB2  1 
ATOM   5650 H HB3  . GLN   B 1 118 ? 35.428 -10.606 -4.437  1.00 15.29 ?  118 GLN   B HB3  1 
ATOM   5651 H HG2  . GLN   B 1 118 ? 33.736 -12.495 -3.208  1.00 15.43 ?  118 GLN   B HG2  1 
ATOM   5652 H HG3  . GLN   B 1 118 ? 34.447 -11.309 -2.424  1.00 15.43 ?  118 GLN   B HG3  1 
ATOM   5653 H HE21 . GLN   B 1 118 ? 31.603 -11.959 -3.085  1.00 16.07 ?  118 GLN   B HE21 1 
ATOM   5654 H HE22 . GLN   B 1 118 ? 31.007 -10.681 -3.565  1.00 16.07 ?  118 GLN   B HE22 1 
ATOM   5655 N N    . HIS   B 1 119 ? 36.123 -12.934 -7.498  1.00 11.78 ?  119 HIS   B N    1 
ATOM   5656 C CA   . HIS   B 1 119 ? 37.162 -12.880 -8.518  1.00 12.00 ?  119 HIS   B CA   1 
ATOM   5657 C C    . HIS   B 1 119 ? 36.683 -13.615 -9.756  1.00 11.94 ?  119 HIS   B C    1 
ATOM   5658 O O    . HIS   B 1 119 ? 36.178 -14.734 -9.656  1.00 12.57 ?  119 HIS   B O    1 
ATOM   5659 C CB   . HIS   B 1 119 ? 38.446 -13.507 -7.980  1.00 12.66 ?  119 HIS   B CB   1 
ATOM   5660 C CG   . HIS   B 1 119 ? 38.928 -12.816 -6.751  1.00 13.73 ?  119 HIS   B CG   1 
ATOM   5661 N ND1  . HIS   B 1 119 ? 39.731 -11.695 -6.797  1.00 15.42 ?  119 HIS   B ND1  1 
ATOM   5662 C CD2  . HIS   B 1 119 ? 38.632 -13.018 -5.448  1.00 14.66 ?  119 HIS   B CD2  1 
ATOM   5663 C CE1  . HIS   B 1 119 ? 39.942 -11.265 -5.567  1.00 16.54 ?  119 HIS   B CE1  1 
ATOM   5664 N NE2  . HIS   B 1 119 ? 39.281 -12.043 -4.731  1.00 16.40 ?  119 HIS   B NE2  1 
ATOM   5665 H H    . HIS   B 1 119 ? 35.763 -13.716 -7.421  1.00 14.11 ?  119 HIS   B H    1 
ATOM   5666 H HA   . HIS   B 1 119 ? 37.338 -11.955 -8.755  1.00 14.37 ?  119 HIS   B HA   1 
ATOM   5667 H HB2  . HIS   B 1 119 ? 38.280 -14.437 -7.765  1.00 15.17 ?  119 HIS   B HB2  1 
ATOM   5668 H HB3  . HIS   B 1 119 ? 39.138 -13.441 -8.660  1.00 15.17 ?  119 HIS   B HB3  1 
ATOM   5669 H HD2  . HIS   B 1 119 ? 38.100 -13.697 -5.103  1.00 17.57 ?  119 HIS   B HD2  1 
ATOM   5670 H HE1  . HIS   B 1 119 ? 40.479 -10.544 -5.331  1.00 19.82 ?  119 HIS   B HE1  1 
ATOM   5671 H HE2  . HIS   B 1 119 ? 39.286 -11.974 -3.874  1.00 19.66 ?  119 HIS   B HE2  1 
ATOM   5672 N N    . GLU   B 1 120 ? 36.838 -12.998 -10.924 1.00 12.51 ?  120 GLU   B N    1 
ATOM   5673 C CA   . GLU   B 1 120 ? 36.257 -13.581 -12.127 1.00 14.02 ?  120 GLU   B CA   1 
ATOM   5674 C C    . GLU   B 1 120 ? 36.932 -14.884 -12.535 1.00 13.05 ?  120 GLU   B C    1 
ATOM   5675 O O    . GLU   B 1 120 ? 36.272 -15.753 -13.117 1.00 13.39 ?  120 GLU   B O    1 
ATOM   5676 C CB   . GLU   B 1 120 ? 36.278 -12.572 -13.273 1.00 18.90 ?  120 GLU   B CB   1 
ATOM   5677 C CG   . GLU   B 1 120 ? 35.312 -11.419 -13.072 1.00 25.49 ?  120 GLU   B CG   1 
ATOM   5678 C CD   . GLU   B 1 120 ? 35.197 -10.524 -14.289 1.00 31.25 ?  120 GLU   B CD   1 
ATOM   5679 O OE1  . GLU   B 1 120 ? 36.186 -10.411 -15.045 1.00 33.33 ?  120 GLU   B OE1  1 
ATOM   5680 O OE2  . GLU   B 1 120 ? 34.115 -9.933  -14.487 1.00 33.82 -1 120 GLU   B OE2  1 
ATOM   5681 H H    . GLU   B 1 120 ? 37.264 -12.257 -11.047 1.00 14.98 ?  120 GLU   B H    1 
ATOM   5682 H HA   . GLU   B 1 120 ? 35.332 -13.790 -11.942 1.00 16.80 ?  120 GLU   B HA   1 
ATOM   5683 H HB2  . GLU   B 1 120 ? 37.167 -12.202 -13.356 1.00 22.66 ?  120 GLU   B HB2  1 
ATOM   5684 H HB3  . GLU   B 1 120 ? 36.028 -13.026 -14.095 1.00 22.66 ?  120 GLU   B HB3  1 
ATOM   5685 H HG2  . GLU   B 1 120 ? 34.428 -11.773 -12.878 1.00 30.56 ?  120 GLU   B HG2  1 
ATOM   5686 H HG3  . GLU   B 1 120 ? 35.618 -10.873 -12.333 1.00 30.56 ?  120 GLU   B HG3  1 
ATOM   5687 N N    . VAL   B 1 121 ? 38.232 -15.027 -12.267 1.00 12.41 ?  121 VAL   B N    1 
ATOM   5688 C CA   . VAL   B 1 121 ? 38.978 -16.236 -12.614 1.00 12.31 ?  121 VAL   B CA   1 
ATOM   5689 C C    . VAL   B 1 121 ? 40.088 -16.443 -11.593 1.00 12.11 ?  121 VAL   B C    1 
ATOM   5690 O O    . VAL   B 1 121 ? 40.766 -15.487 -11.198 1.00 12.64 ?  121 VAL   B O    1 
ATOM   5691 C CB   . VAL   B 1 121 ? 39.497 -16.186 -14.069 1.00 14.15 ?  121 VAL   B CB   1 
ATOM   5692 C CG1  . VAL   B 1 121 ? 40.361 -14.957 -14.311 1.00 16.07 ?  121 VAL   B CG1  1 
ATOM   5693 C CG2  . VAL   B 1 121 ? 40.238 -17.467 -14.426 1.00 15.58 ?  121 VAL   B CG2  1 
ATOM   5694 H H    . VAL   B 1 121 ? 38.716 -14.422 -11.889 1.00 14.87 ?  121 VAL   B H    1 
ATOM   5695 H HA   . VAL   B 1 121 ? 38.371 -16.987 -12.551 1.00 14.74 ?  121 VAL   B HA   1 
ATOM   5696 H HB   . VAL   B 1 121 ? 38.732 -16.125 -14.666 1.00 16.96 ?  121 VAL   B HB   1 
ATOM   5697 H HG11 . VAL   B 1 121 ? 40.676 -14.970 -15.229 1.00 19.26 ?  121 VAL   B HG11 1 
ATOM   5698 H HG12 . VAL   B 1 121 ? 39.826 -14.162 -14.157 1.00 19.26 ?  121 VAL   B HG12 1 
ATOM   5699 H HG13 . VAL   B 1 121 ? 41.113 -14.976 -13.702 1.00 19.26 ?  121 VAL   B HG13 1 
ATOM   5700 H HG21 . VAL   B 1 121 ? 40.441 -17.461 -15.375 1.00 18.68 ?  121 VAL   B HG21 1 
ATOM   5701 H HG22 . VAL   B 1 121 ? 41.063 -17.508 -13.914 1.00 18.68 ?  121 VAL   B HG22 1 
ATOM   5702 H HG23 . VAL   B 1 121 ? 39.678 -18.228 -14.212 1.00 18.68 ?  121 VAL   B HG23 1 
ATOM   5703 N N    . LEU   B 1 122 ? 40.269 -17.699 -11.168 1.00 11.56 ?  122 LEU   B N    1 
ATOM   5704 C CA   . LEU   B 1 122 ? 41.246 -18.055 -10.141 1.00 11.04 ?  122 LEU   B CA   1 
ATOM   5705 C C    . LEU   B 1 122 ? 41.905 -19.382 -10.468 1.00 10.95 ?  122 LEU   B C    1 
ATOM   5706 O O    . LEU   B 1 122 ? 41.245 -20.300 -10.971 1.00 12.34 ?  122 LEU   B O    1 
ATOM   5707 C CB   . LEU   B 1 122 ? 40.593 -18.282 -8.764  1.00 12.66 ?  122 LEU   B CB   1 
ATOM   5708 C CG   . LEU   B 1 122 ? 39.557 -17.263 -8.281  1.00 12.86 ?  122 LEU   B CG   1 
ATOM   5709 C CD1  . LEU   B 1 122 ? 38.157 -17.607 -8.769  1.00 14.00 ?  122 LEU   B CD1  1 
ATOM   5710 C CD2  . LEU   B 1 122 ? 39.586 -17.148 -6.772  1.00 12.54 ?  122 LEU   B CD2  1 
ATOM   5711 H H    . LEU   B 1 122 ? 39.833 -18.378 -11.469 1.00 13.85 ?  122 LEU   B H    1 
ATOM   5712 H HA   . LEU   B 1 122 ? 41.922 -17.364 -10.061 1.00 13.22 ?  122 LEU   B HA   1 
ATOM   5713 H HB2  . LEU   B 1 122 ? 40.146 -19.141 -8.783  1.00 15.16 ?  122 LEU   B HB2  1 
ATOM   5714 H HB3  . LEU   B 1 122 ? 41.294 -18.300 -8.098  1.00 15.16 ?  122 LEU   B HB3  1 
ATOM   5715 H HG   . LEU   B 1 122 ? 39.784 -16.392 -8.642  1.00 15.41 ?  122 LEU   B HG   1 
ATOM   5716 H HD11 . LEU   B 1 122 ? 37.527 -16.965 -8.401  1.00 16.78 ?  122 LEU   B HD11 1 
ATOM   5717 H HD12 . LEU   B 1 122 ? 38.140 -17.557 -9.740  1.00 16.78 ?  122 LEU   B HD12 1 
ATOM   5718 H HD13 . LEU   B 1 122 ? 37.929 -18.499 -8.479  1.00 16.78 ?  122 LEU   B HD13 1 
ATOM   5719 H HD21 . LEU   B 1 122 ? 38.903 -16.518 -6.488  1.00 15.02 ?  122 LEU   B HD21 1 
ATOM   5720 H HD22 . LEU   B 1 122 ? 39.414 -18.019 -6.384  1.00 15.02 ?  122 LEU   B HD22 1 
ATOM   5721 H HD23 . LEU   B 1 122 ? 40.461 -16.829 -6.498  1.00 15.02 ?  122 LEU   B HD23 1 
ATOM   5722 N N    . LEU   B 1 123 ? 43.191 -19.492 -10.113 1.00 10.56 ?  123 LEU   B N    1 
ATOM   5723 C CA   . LEU   B 1 123 ? 43.904 -20.761 -9.987  1.00 11.01 ?  123 LEU   B CA   1 
ATOM   5724 C C    . LEU   B 1 123 ? 43.871 -21.158 -8.518  1.00 10.51 ?  123 LEU   B C    1 
ATOM   5725 O O    . LEU   B 1 123 ? 44.224 -20.338 -7.662  1.00 10.98 ?  123 LEU   B O    1 
ATOM   5726 C CB   . LEU   B 1 123 ? 45.355 -20.581 -10.438 1.00 11.86 ?  123 LEU   B CB   1 
ATOM   5727 C CG   . LEU   B 1 123 ? 46.295 -21.766 -10.200 1.00 11.86 ?  123 LEU   B CG   1 
ATOM   5728 C CD1  . LEU   B 1 123 ? 45.868 -23.013 -10.974 1.00 12.53 ?  123 LEU   B CD1  1 
ATOM   5729 C CD2  . LEU   B 1 123 ? 47.716 -21.367 -10.574 1.00 12.73 ?  123 LEU   B CD2  1 
ATOM   5730 H H    . LEU   B 1 123 ? 43.687 -18.812 -9.921  1.00 12.65 ?  123 LEU   B H    1 
ATOM   5731 H HA   . LEU   B 1 123 ? 43.471 -21.447 -10.521 1.00 13.19 ?  123 LEU   B HA   1 
ATOM   5732 H HB2  . LEU   B 1 123 ? 45.352 -20.404 -11.391 1.00 14.20 ?  123 LEU   B HB2  1 
ATOM   5733 H HB3  . LEU   B 1 123 ? 45.725 -19.821 -9.968  1.00 14.20 ?  123 LEU   B HB3  1 
ATOM   5734 H HG   . LEU   B 1 123 ? 46.294 -21.990 -9.256  1.00 14.20 ?  123 LEU   B HG   1 
ATOM   5735 H HD11 . LEU   B 1 123 ? 46.504 -23.722 -10.802 1.00 15.01 ?  123 LEU   B HD11 1 
ATOM   5736 H HD12 . LEU   B 1 123 ? 44.984 -23.278 -10.674 1.00 15.01 ?  123 LEU   B HD12 1 
ATOM   5737 H HD13 . LEU   B 1 123 ? 45.848 -22.802 -11.919 1.00 15.01 ?  123 LEU   B HD13 1 
ATOM   5738 H HD21 . LEU   B 1 123 ? 48.307 -22.121 -10.424 1.00 15.25 ?  123 LEU   B HD21 1 
ATOM   5739 H HD22 . LEU   B 1 123 ? 47.735 -21.115 -11.512 1.00 15.25 ?  123 LEU   B HD22 1 
ATOM   5740 H HD23 . LEU   B 1 123 ? 47.988 -20.616 -10.025 1.00 15.25 ?  123 LEU   B HD23 1 
ATOM   5741 N N    . ALA   B 1 124 ? 43.433 -22.390 -8.214  1.00 10.58 ?  124 ALA   B N    1 
ATOM   5742 C CA   . ALA   B 1 124 ? 43.175 -22.711 -6.820  1.00 10.43 ?  124 ALA   B CA   1 
ATOM   5743 C C    . ALA   B 1 124 ? 43.445 -24.170 -6.487  1.00 9.94  ?  124 ALA   B C    1 
ATOM   5744 O O    . ALA   B 1 124 ? 43.323 -25.046 -7.355  1.00 10.96 ?  124 ALA   B O    1 
ATOM   5745 C CB   . ALA   B 1 124 ? 41.718 -22.398 -6.450  1.00 11.25 ?  124 ALA   B CB   1 
ATOM   5746 H H    . ALA   B 1 124 ? 43.275 -23.027 -8.777  1.00 12.68 ?  124 ALA   B H    1 
ATOM   5747 H HA   . ALA   B 1 124 ? 43.745 -22.159 -6.270  1.00 12.50 ?  124 ALA   B HA   1 
ATOM   5748 H HB1  . ALA   B 1 124 ? 41.566 -22.618 -5.517  1.00 13.47 ?  124 ALA   B HB1  1 
ATOM   5749 H HB2  . ALA   B 1 124 ? 41.551 -21.451 -6.595  1.00 13.47 ?  124 ALA   B HB2  1 
ATOM   5750 H HB3  . ALA   B 1 124 ? 41.125 -22.923 -7.013  1.00 13.47 ?  124 ALA   B HB3  1 
ATOM   5751 N N    . PRO   B 1 125 ? 43.745 -24.462 -5.226  1.00 10.54 ?  125 PRO   B N    1 
ATOM   5752 C CA   . PRO   B 1 125 ? 43.686 -25.829 -4.709  1.00 11.31 ?  125 PRO   B CA   1 
ATOM   5753 C C    . PRO   B 1 125 ? 42.285 -26.106 -4.163  1.00 11.65 ?  125 PRO   B C    1 
ATOM   5754 O O    . PRO   B 1 125 ? 41.485 -25.193 -3.954  1.00 12.11 ?  125 PRO   B O    1 
ATOM   5755 C CB   . PRO   B 1 125 ? 44.670 -25.754 -3.539  1.00 12.53 ?  125 PRO   B CB   1 
ATOM   5756 C CG   . PRO   B 1 125 ? 44.426 -24.363 -2.969  1.00 12.63 ?  125 PRO   B CG   1 
ATOM   5757 C CD   . PRO   B 1 125 ? 44.070 -23.493 -4.164  1.00 11.45 ?  125 PRO   B CD   1 
ATOM   5758 H HA   . PRO   B 1 125 ? 43.962 -26.498 -5.358  1.00 13.55 ?  125 PRO   B HA   1 
ATOM   5759 H HB2  . PRO   B 1 125 ? 44.465 -26.435 -2.877  1.00 15.02 ?  125 PRO   B HB2  1 
ATOM   5760 H HB3  . PRO   B 1 125 ? 45.582 -25.840 -3.856  1.00 15.02 ?  125 PRO   B HB3  1 
ATOM   5761 H HG2  . PRO   B 1 125 ? 43.688 -24.386 -2.337  1.00 15.13 ?  125 PRO   B HG2  1 
ATOM   5762 H HG3  . PRO   B 1 125 ? 45.232 -24.034 -2.533  1.00 15.13 ?  125 PRO   B HG3  1 
ATOM   5763 H HD2  . PRO   B 1 125 ? 43.302 -22.935 -3.970  1.00 13.71 ?  125 PRO   B HD2  1 
ATOM   5764 H HD3  . PRO   B 1 125 ? 44.839 -22.949 -4.426  1.00 13.71 ?  125 PRO   B HD3  1 
ATOM   5765 N N    . LEU   B 1 126 ? 42.017 -27.382 -3.880  1.00 12.16 ?  126 LEU   B N    1 
ATOM   5766 C CA   . LEU   B 1 126 ? 40.795 -27.746 -3.168  1.00 12.37 ?  126 LEU   B CA   1 
ATOM   5767 C C    . LEU   B 1 126 ? 40.910 -27.344 -1.703  1.00 12.71 ?  126 LEU   B C    1 
ATOM   5768 O O    . LEU   B 1 126 ? 41.800 -27.808 -0.981  1.00 14.73 ?  126 LEU   B O    1 
ATOM   5769 C CB   . LEU   B 1 126 ? 40.530 -29.244 -3.280  1.00 13.76 ?  126 LEU   B CB   1 
ATOM   5770 C CG   . LEU   B 1 126 ? 40.003 -29.732 -4.629  1.00 14.76 ?  126 LEU   B CG   1 
ATOM   5771 C CD1  . LEU   B 1 126 ? 40.040 -31.241 -4.702  1.00 16.01 ?  126 LEU   B CD1  1 
ATOM   5772 C CD2  . LEU   B 1 126 ? 38.587 -29.231 -4.885  1.00 15.13 ?  126 LEU   B CD2  1 
ATOM   5773 H H    . LEU   B 1 126 ? 42.525 -28.048 -4.076  1.00 14.57 ?  126 LEU   B H    1 
ATOM   5774 H HA   . LEU   B 1 126 ? 40.046 -27.268 -3.557  1.00 14.83 ?  126 LEU   B HA   1 
ATOM   5775 H HB2  . LEU   B 1 126 ? 41.354 -29.715 -3.105  1.00 16.48 ?  126 LEU   B HB2  1 
ATOM   5776 H HB3  . LEU   B 1 126 ? 39.867 -29.486 -2.610  1.00 16.48 ?  126 LEU   B HB3  1 
ATOM   5777 H HG   . LEU   B 1 126 ? 40.572 -29.378 -5.333  1.00 17.69 ?  126 LEU   B HG   1 
ATOM   5778 H HD11 . LEU   B 1 126 ? 39.700 -31.522 -5.565  1.00 19.19 ?  126 LEU   B HD11 1 
ATOM   5779 H HD12 . LEU   B 1 126 ? 40.953 -31.538 -4.588  1.00 19.19 ?  126 LEU   B HD12 1 
ATOM   5780 H HD13 . LEU   B 1 126 ? 39.481 -31.601 -3.994  1.00 19.19 ?  126 LEU   B HD13 1 
ATOM   5781 H HD21 . LEU   B 1 126 ? 38.248 -29.635 -5.699  1.00 18.13 ?  126 LEU   B HD21 1 
ATOM   5782 H HD22 . LEU   B 1 126 ? 38.022 -29.478 -4.135  1.00 18.13 ?  126 LEU   B HD22 1 
ATOM   5783 H HD23 . LEU   B 1 126 ? 38.598 -28.263 -4.980  1.00 18.13 ?  126 LEU   B HD23 1 
ATOM   5784 N N    . LEU   B 1 127 ? 39.980 -26.510 -1.249  1.00 12.83 ?  127 LEU   B N    1 
ATOM   5785 C CA   . LEU   B 1 127 ? 40.032 -26.020 0.114   1.00 12.82 ?  127 LEU   B CA   1 
ATOM   5786 C C    . LEU   B 1 127 ? 39.750 -27.142 1.106   1.00 12.57 ?  127 LEU   B C    1 
ATOM   5787 O O    . LEU   B 1 127 ? 38.931 -28.040 0.873   1.00 13.17 ?  127 LEU   B O    1 
ATOM   5788 C CB   . LEU   B 1 127 ? 39.021 -24.891 0.323   1.00 13.32 ?  127 LEU   B CB   1 
ATOM   5789 C CG   . LEU   B 1 127 ? 39.193 -23.633 -0.525  1.00 13.78 ?  127 LEU   B CG   1 
ATOM   5790 C CD1  . LEU   B 1 127 ? 38.077 -22.648 -0.207  1.00 14.15 ?  127 LEU   B CD1  1 
ATOM   5791 C CD2  . LEU   B 1 127 ? 40.555 -22.990 -0.300  1.00 14.33 ?  127 LEU   B CD2  1 
ATOM   5792 H H    . LEU   B 1 127 ? 39.311 -26.209 -1.708  1.00 15.38 ?  127 LEU   B H    1 
ATOM   5793 H HA   . LEU   B 1 127 ? 40.920 -25.666 0.290   1.00 15.36 ?  127 LEU   B HA   1 
ATOM   5794 H HB2  . LEU   B 1 127 ? 38.136 -25.240 0.134   1.00 15.96 ?  127 LEU   B HB2  1 
ATOM   5795 H HB3  . LEU   B 1 127 ? 39.063 -24.615 1.252   1.00 15.96 ?  127 LEU   B HB3  1 
ATOM   5796 H HG   . LEU   B 1 127 ? 39.119 -23.864 -1.462  1.00 16.52 ?  127 LEU   B HG   1 
ATOM   5797 H HD11 . LEU   B 1 127 ? 38.197 -21.842 -0.740  1.00 16.95 ?  127 LEU   B HD11 1 
ATOM   5798 H HD12 . LEU   B 1 127 ? 37.220 -23.051 -0.414  1.00 16.95 ?  127 LEU   B HD12 1 
ATOM   5799 H HD13 . LEU   B 1 127 ? 38.112 -22.417 0.738   1.00 16.95 ?  127 LEU   B HD13 1 
ATOM   5800 H HD21 . LEU   B 1 127 ? 40.595 -22.145 -0.777  1.00 17.17 ?  127 LEU   B HD21 1 
ATOM   5801 H HD22 . LEU   B 1 127 ? 40.682 -22.835 0.651   1.00 17.17 ?  127 LEU   B HD22 1 
ATOM   5802 H HD23 . LEU   B 1 127 ? 41.245 -23.587 -0.631  1.00 17.17 ?  127 LEU   B HD23 1 
ATOM   5803 N N    . SER   B 1 128 ? 40.429 -27.054 2.241   1.00 12.62 ?  128 SER   B N    1 
ATOM   5804 C CA   . SER   B 1 128 ? 40.320 -27.970 3.365   1.00 12.98 ?  128 SER   B CA   1 
ATOM   5805 C C    . SER   B 1 128 ? 40.813 -29.378 3.045   1.00 14.05 ?  128 SER   B C    1 
ATOM   5806 O O    . SER   B 1 128 ? 40.718 -30.258 3.901   1.00 15.61 ?  128 SER   B O    1 
ATOM   5807 C CB   . SER   B 1 128 ? 38.919 -27.975 3.995   1.00 13.52 ?  128 SER   B CB   1 
ATOM   5808 O OG   . SER   B 1 128 ? 38.603 -26.696 4.532   1.00 14.17 ?  128 SER   B OG   1 
ATOM   5809 H H    . SER   B 1 128 ? 40.999 -26.424 2.391   1.00 15.12 ?  128 SER   B H    1 
ATOM   5810 H HA   . SER   B 1 128 ? 40.905 -27.636 4.053   1.00 15.55 ?  128 SER   B HA   1 
ATOM   5811 H HB2  . SER   B 1 128 ? 38.261 -28.219 3.324   1.00 16.20 ?  128 SER   B HB2  1 
ATOM   5812 H HB3  . SER   B 1 128 ? 38.900 -28.640 4.718   1.00 16.20 ?  128 SER   B HB3  1 
ATOM   5813 H HG   . SER   B 1 128 ? 39.164 -26.490 5.121   1.00 16.98 ?  128 SER   B HG   1 
ATOM   5814 N N    . ALA   B 1 129 ? 41.383 -29.602 1.859   1.00 15.14 ?  129 ALA   B N    1 
ATOM   5815 C CA   . ALA   B 1 129 ? 41.930 -30.901 1.500   1.00 16.30 ?  129 ALA   B CA   1 
ATOM   5816 C C    . ALA   B 1 129 ? 43.321 -31.079 2.100   1.00 15.49 ?  129 ALA   B C    1 
ATOM   5817 O O    . ALA   B 1 129 ? 43.875 -30.178 2.745   1.00 15.30 ?  129 ALA   B O    1 
ATOM   5818 C CB   . ALA   B 1 129 ? 41.983 -31.055 -0.018  1.00 18.38 ?  129 ALA   B CB   1 
ATOM   5819 H H    . ALA   B 1 129 ? 41.461 -29.011 1.234   1.00 18.14 ?  129 ALA   B H    1 
ATOM   5820 H HA   . ALA   B 1 129 ? 41.358 -31.599 1.852   1.00 19.54 ?  129 ALA   B HA   1 
ATOM   5821 H HB1  . ALA   B 1 129 ? 42.344 -31.931 -0.236  1.00 22.03 ?  129 ALA   B HB1  1 
ATOM   5822 H HB2  . ALA   B 1 129 ? 41.088 -30.969 -0.376  1.00 22.03 ?  129 ALA   B HB2  1 
ATOM   5823 H HB3  . ALA   B 1 129 ? 42.557 -30.363 -0.386  1.00 22.03 ?  129 ALA   B HB3  1 
ATOM   5824 N N    . GLY   B 1 130 ? 43.886 -32.265 1.876   1.00 15.38 ?  130 GLY   B N    1 
ATOM   5825 C CA   . GLY   B 1 130 ? 45.272 -32.502 2.231   1.00 15.75 ?  130 GLY   B CA   1 
ATOM   5826 C C    . GLY   B 1 130 ? 45.489 -32.401 3.722   1.00 15.62 ?  130 GLY   B C    1 
ATOM   5827 O O    . GLY   B 1 130 ? 44.792 -33.043 4.521   1.00 16.49 ?  130 GLY   B O    1 
ATOM   5828 H H    . GLY   B 1 130 ? 43.492 -32.937 1.509   1.00 18.43 ?  130 GLY   B H    1 
ATOM   5829 H HA2  . GLY   B 1 130 ? 45.535 -33.391 1.938   1.00 18.88 ?  130 GLY   B HA2  1 
ATOM   5830 H HA3  . GLY   B 1 130 ? 45.840 -31.853 1.788   1.00 18.88 ?  130 GLY   B HA3  1 
ATOM   5831 N N    . ILE   B 1 131 ? 46.463 -31.572 4.108   1.00 16.03 ?  131 ILE   B N    1 
ATOM   5832 C CA   . ILE   B 1 131 ? 46.822 -31.433 5.510   1.00 16.97 ?  131 ILE   B CA   1 
ATOM   5833 C C    . ILE   B 1 131 ? 45.702 -30.836 6.346   1.00 16.29 ?  131 ILE   B C    1 
ATOM   5834 O O    . ILE   B 1 131 ? 45.774 -30.893 7.575   1.00 17.84 ?  131 ILE   B O    1 
ATOM   5835 C CB   . ILE   B 1 131 ? 48.140 -30.643 5.701   1.00 19.21 ?  131 ILE   B CB   1 
ATOM   5836 C CG1  . ILE   B 1 131 ? 47.964 -29.161 5.332   1.00 20.19 ?  131 ILE   B CG1  1 
ATOM   5837 C CG2  . ILE   B 1 131 ? 49.266 -31.272 4.885   1.00 20.19 ?  131 ILE   B CG2  1 
ATOM   5838 C CD1  . ILE   B 1 131 ? 49.159 -28.290 5.679   1.00 21.21 ?  131 ILE   B CD1  1 
ATOM   5839 H H    . ILE   B 1 131 ? 46.926 -31.081 3.572   1.00 19.22 ?  131 ILE   B H    1 
ATOM   5840 H HA   . ILE   B 1 131 ? 46.977 -32.320 5.861   1.00 20.34 ?  131 ILE   B HA   1 
ATOM   5841 H HB   . ILE   B 1 131 ? 48.378 -30.691 6.641   1.00 23.03 ?  131 ILE   B HB   1 
ATOM   5842 H HG12 . ILE   B 1 131 ? 47.810 -29.099 4.376   1.00 24.20 ?  131 ILE   B HG12 1 
ATOM   5843 H HG13 . ILE   B 1 131 ? 47.193 -28.801 5.807   1.00 24.20 ?  131 ILE   B HG13 1 
ATOM   5844 H HG21 . ILE   B 1 131 ? 50.101 -30.855 5.137   1.00 24.20 ?  131 ILE   B HG21 1 
ATOM   5845 H HG22 . ILE   B 1 131 ? 49.293 -32.220 5.073   1.00 24.20 ?  131 ILE   B HG22 1 
ATOM   5846 H HG23 . ILE   B 1 131 ? 49.087 -31.123 3.944   1.00 24.20 ?  131 ILE   B HG23 1 
ATOM   5847 H HD11 . ILE   B 1 131 ? 48.934 -27.364 5.498   1.00 25.43 ?  131 ILE   B HD11 1 
ATOM   5848 H HD12 . ILE   B 1 131 ? 49.367 -28.403 6.619   1.00 25.43 ?  131 ILE   B HD12 1 
ATOM   5849 H HD13 . ILE   B 1 131 ? 49.912 -28.562 5.136   1.00 25.43 ?  131 ILE   B HD13 1 
ATOM   5850 N N    . PHE   B 1 132 ? 44.671 -30.259 5.715   1.00 14.95 ?  132 PHE   B N    1 
ATOM   5851 C CA   . PHE   B 1 132 ? 43.508 -29.759 6.440   1.00 15.68 ?  132 PHE   B CA   1 
ATOM   5852 C C    . PHE   B 1 132 ? 42.485 -30.850 6.761   1.00 16.99 ?  132 PHE   B C    1 
ATOM   5853 O O    . PHE   B 1 132 ? 41.575 -30.598 7.556   1.00 18.58 ?  132 PHE   B O    1 
ATOM   5854 C CB   . PHE   B 1 132 ? 42.830 -28.627 5.658   1.00 14.58 ?  132 PHE   B CB   1 
ATOM   5855 C CG   . PHE   B 1 132 ? 43.526 -27.283 5.771   1.00 14.79 ?  132 PHE   B CG   1 
ATOM   5856 C CD1  . PHE   B 1 132 ? 44.815 -27.095 5.293   1.00 15.95 ?  132 PHE   B CD1  1 
ATOM   5857 C CD2  . PHE   B 1 132 ? 42.851 -26.189 6.299   1.00 14.34 ?  132 PHE   B CD2  1 
ATOM   5858 C CE1  . PHE   B 1 132 ? 45.434 -25.856 5.385   1.00 16.39 ?  132 PHE   B CE1  1 
ATOM   5859 C CE2  . PHE   B 1 132 ? 43.459 -24.944 6.385   1.00 14.76 ?  132 PHE   B CE2  1 
ATOM   5860 C CZ   . PHE   B 1 132 ? 44.752 -24.781 5.928   1.00 15.92 ?  132 PHE   B CZ   1 
ATOM   5861 H H    . PHE   B 1 132 ? 44.629 -30.138 4.863   1.00 17.92 ?  132 PHE   B H    1 
ATOM   5862 H HA   . PHE   B 1 132 ? 43.813 -29.385 7.280   1.00 18.79 ?  132 PHE   B HA   1 
ATOM   5863 H HB2  . PHE   B 1 132 ? 42.814 -28.867 4.721   1.00 17.47 ?  132 PHE   B HB2  1 
ATOM   5864 H HB3  . PHE   B 1 132 ? 41.924 -28.520 5.988   1.00 17.47 ?  132 PHE   B HB3  1 
ATOM   5865 H HD1  . PHE   B 1 132 ? 45.279 -27.817 4.934   1.00 19.12 ?  132 PHE   B HD1  1 
ATOM   5866 H HD2  . PHE   B 1 132 ? 41.979 -26.296 6.610   1.00 17.18 ?  132 PHE   B HD2  1 
ATOM   5867 H HE1  . PHE   B 1 132 ? 46.304 -25.747 5.078   1.00 19.64 ?  132 PHE   B HE1  1 
ATOM   5868 H HE2  . PHE   B 1 132 ? 42.998 -24.221 6.756   1.00 17.69 ?  132 PHE   B HE2  1 
ATOM   5869 H HZ   . PHE   B 1 132 ? 45.163 -23.946 5.992   1.00 19.09 ?  132 PHE   B HZ   1 
ATOM   5870 N N    . GLY   B 1 133 ? 42.593 -32.042 6.161   1.00 16.36 ?  133 GLY   B N    1 
ATOM   5871 C CA   . GLY   B 1 133 ? 41.881 -33.208 6.649   1.00 17.29 ?  133 GLY   B CA   1 
ATOM   5872 C C    . GLY   B 1 133 ? 40.482 -33.460 6.118   1.00 17.16 ?  133 GLY   B C    1 
ATOM   5873 O O    . GLY   B 1 133 ? 39.893 -34.479 6.484   1.00 19.50 ?  133 GLY   B O    1 
ATOM   5874 H H    . GLY   B 1 133 ? 43.083 -32.191 5.468   1.00 19.61 ?  133 GLY   B H    1 
ATOM   5875 H HA2  . GLY   B 1 133 ? 42.414 -33.993 6.448   1.00 20.72 ?  133 GLY   B HA2  1 
ATOM   5876 H HA3  . GLY   B 1 133 ? 41.818 -33.140 7.615   1.00 20.72 ?  133 GLY   B HA3  1 
ATOM   5877 N N    . ALA   B 1 134 ? 39.921 -32.592 5.286   1.00 16.40 ?  134 ALA   B N    1 
ATOM   5878 C CA   . ALA   B 1 134 ? 38.596 -32.873 4.753   1.00 16.75 ?  134 ALA   B CA   1 
ATOM   5879 C C    . ALA   B 1 134 ? 38.681 -33.866 3.599   1.00 16.55 ?  134 ALA   B C    1 
ATOM   5880 O O    . ALA   B 1 134 ? 39.734 -34.061 2.988   1.00 17.64 ?  134 ALA   B O    1 
ATOM   5881 C CB   . ALA   B 1 134 ? 37.916 -31.587 4.285   1.00 17.42 ?  134 ALA   B CB   1 
ATOM   5882 H H    . ALA   B 1 134 ? 40.275 -31.849 5.027   1.00 19.66 ?  134 ALA   B H    1 
ATOM   5883 H HA   . ALA   B 1 134 ? 38.050 -33.262 5.454   1.00 20.08 ?  134 ALA   B HA   1 
ATOM   5884 H HB1  . ALA   B 1 134 ? 37.031 -31.804 3.952   1.00 20.88 ?  134 ALA   B HB1  1 
ATOM   5885 H HB2  . ALA   B 1 134 ? 37.847 -30.974 5.034   1.00 20.88 ?  134 ALA   B HB2  1 
ATOM   5886 H HB3  . ALA   B 1 134 ? 38.447 -31.188 3.578   1.00 20.88 ?  134 ALA   B HB3  1 
ATOM   5887 N N    . ASP   B 1 135 ? 37.548 -34.491 3.304   1.00 16.98 ?  135 ASP   B N    1 
ATOM   5888 C CA   . ASP   B 1 135 ? 37.458 -35.393 2.164   1.00 17.88 ?  135 ASP   B CA   1 
ATOM   5889 C C    . ASP   B 1 135 ? 37.557 -34.561 0.891   1.00 16.49 ?  135 ASP   B C    1 
ATOM   5890 O O    . ASP   B 1 135 ? 36.707 -33.686 0.666   1.00 16.65 ?  135 ASP   B O    1 
ATOM   5891 C CB   . ASP   B 1 135 ? 36.126 -36.142 2.214   1.00 19.85 ?  135 ASP   B CB   1 
ATOM   5892 C CG   . ASP   B 1 135 ? 35.962 -37.136 1.075   1.00 21.70 ?  135 ASP   B CG   1 
ATOM   5893 O OD1  . ASP   B 1 135 ? 36.830 -37.179 0.174   1.00 21.13 ?  135 ASP   B OD1  1 
ATOM   5894 O OD2  . ASP   B 1 135 ? 34.966 -37.899 1.099   1.00 24.84 -1 135 ASP   B OD2  1 
ATOM   5895 H H    . ASP   B 1 135 ? 36.817 -34.408 3.746   1.00 20.35 ?  135 ASP   B H    1 
ATOM   5896 H HA   . ASP   B 1 135 ? 38.183 -36.038 2.201   1.00 21.43 ?  135 ASP   B HA   1 
ATOM   5897 H HB2  . ASP   B 1 135 ? 36.078 -36.635 3.048   1.00 23.80 ?  135 ASP   B HB2  1 
ATOM   5898 H HB3  . ASP   B 1 135 ? 35.405 -35.498 2.165   1.00 23.80 ?  135 ASP   B HB3  1 
ATOM   5899 N N    . PRO   B 1 136 ? 38.564 -34.776 0.042   1.00 16.59 ?  136 PRO   B N    1 
ATOM   5900 C CA   . PRO   B 1 136 ? 38.669 -33.955 -1.175  1.00 15.68 ?  136 PRO   B CA   1 
ATOM   5901 C C    . PRO   B 1 136 ? 37.478 -34.103 -2.102  1.00 15.32 ?  136 PRO   B C    1 
ATOM   5902 O O    . PRO   B 1 136 ? 37.159 -33.157 -2.831  1.00 14.86 ?  136 PRO   B O    1 
ATOM   5903 C CB   . PRO   B 1 136 ? 39.980 -34.436 -1.817  1.00 16.50 ?  136 PRO   B CB   1 
ATOM   5904 C CG   . PRO   B 1 136 ? 40.183 -35.821 -1.271  1.00 18.01 ?  136 PRO   B CG   1 
ATOM   5905 C CD   . PRO   B 1 136 ? 39.634 -35.782 0.126   1.00 17.69 ?  136 PRO   B CD   1 
ATOM   5906 H HA   . PRO   B 1 136 ? 38.763 -33.020 -0.939  1.00 18.79 ?  136 PRO   B HA   1 
ATOM   5907 H HB2  . PRO   B 1 136 ? 39.885 -34.460 -2.786  1.00 19.78 ?  136 PRO   B HB2  1 
ATOM   5908 H HB3  . PRO   B 1 136 ? 40.707 -33.852 -1.559  1.00 19.78 ?  136 PRO   B HB3  1 
ATOM   5909 H HG2  . PRO   B 1 136 ? 39.696 -36.465 -1.810  1.00 21.59 ?  136 PRO   B HG2  1 
ATOM   5910 H HG3  . PRO   B 1 136 ? 41.130 -36.035 -1.257  1.00 21.59 ?  136 PRO   B HG3  1 
ATOM   5911 H HD2  . PRO   B 1 136 ? 39.267 -36.647 0.373   1.00 21.21 ?  136 PRO   B HD2  1 
ATOM   5912 H HD3  . PRO   B 1 136 ? 40.314 -35.493 0.756   1.00 21.21 ?  136 PRO   B HD3  1 
ATOM   5913 N N    . ILE   B 1 137 ? 36.821 -35.270 -2.105  1.00 15.60 ?  137 ILE   B N    1 
ATOM   5914 C CA   . ILE   B 1 137 ? 35.605 -35.440 -2.899  1.00 16.23 ?  137 ILE   B CA   1 
ATOM   5915 C C    . ILE   B 1 137 ? 34.523 -34.476 -2.427  1.00 15.99 ?  137 ILE   B C    1 
ATOM   5916 O O    . ILE   B 1 137 ? 33.814 -33.859 -3.235  1.00 15.46 ?  137 ILE   B O    1 
ATOM   5917 C CB   . ILE   B 1 137 ? 35.141 -36.910 -2.837  1.00 18.07 ?  137 ILE   B CB   1 
ATOM   5918 C CG1  . ILE   B 1 137 ? 36.144 -37.813 -3.564  1.00 20.16 ?  137 ILE   B CG1  1 
ATOM   5919 C CG2  . ILE   B 1 137 ? 33.746 -37.058 -3.425  1.00 18.58 ?  137 ILE   B CG2  1 
ATOM   5920 C CD1  . ILE   B 1 137 ? 35.830 -39.298 -3.454  1.00 22.70 ?  137 ILE   B CD1  1 
ATOM   5921 H H    . ILE   B 1 137 ? 37.056 -35.969 -1.664  1.00 18.70 ?  137 ILE   B H    1 
ATOM   5922 H HA   . ILE   B 1 137 ? 35.805 -35.234 -3.828  1.00 19.46 ?  137 ILE   B HA   1 
ATOM   5923 H HB   . ILE   B 1 137 ? 35.108 -37.179 -1.909  1.00 21.66 ?  137 ILE   B HB   1 
ATOM   5924 H HG12 . ILE   B 1 137 ? 36.150 -37.583 -4.507  1.00 24.16 ?  137 ILE   B HG12 1 
ATOM   5925 H HG13 . ILE   B 1 137 ? 37.025 -37.671 -3.186  1.00 24.16 ?  137 ILE   B HG13 1 
ATOM   5926 H HG21 . ILE   B 1 137 ? 33.543 -38.001 -3.536  1.00 22.27 ?  137 ILE   B HG21 1 
ATOM   5927 H HG22 . ILE   B 1 137 ? 33.104 -36.660 -2.821  1.00 22.27 ?  137 ILE   B HG22 1 
ATOM   5928 H HG23 . ILE   B 1 137 ? 33.718 -36.613 -4.285  1.00 22.27 ?  137 ILE   B HG23 1 
ATOM   5929 H HD11 . ILE   B 1 137 ? 36.614 -39.804 -3.712  1.00 27.22 ?  137 ILE   B HD11 1 
ATOM   5930 H HD12 . ILE   B 1 137 ? 35.590 -39.501 -2.536  1.00 27.22 ?  137 ILE   B HD12 1 
ATOM   5931 H HD13 . ILE   B 1 137 ? 35.089 -39.510 -4.044  1.00 27.22 ?  137 ILE   B HD13 1 
ATOM   5932 N N    . HIS   B 1 138 ? 34.390 -34.320 -1.114  1.00 15.77 ?  138 HIS   B N    1 
ATOM   5933 C CA   . HIS   B 1 138 ? 33.444 -33.350 -0.580  1.00 16.27 ?  138 HIS   B CA   1 
ATOM   5934 C C    . HIS   B 1 138 ? 33.864 -31.922 -0.903  1.00 15.32 ?  138 HIS   B C    1 
ATOM   5935 O O    . HIS   B 1 138 ? 33.020 -31.073 -1.210  1.00 15.83 ?  138 HIS   B O    1 
ATOM   5936 C CB   . HIS   B 1 138 ? 33.331 -33.524 0.927   1.00 17.44 ?  138 HIS   B CB   1 
ATOM   5937 C CG   . HIS   B 1 138 ? 32.397 -32.548 1.561   1.00 18.45 ?  138 HIS   B CG   1 
ATOM   5938 N ND1  . HIS   B 1 138 ? 31.060 -32.481 1.232   1.00 19.92 ?  138 HIS   B ND1  1 
ATOM   5939 C CD2  . HIS   B 1 138 ? 32.609 -31.573 2.477   1.00 18.86 ?  138 HIS   B CD2  1 
ATOM   5940 C CE1  . HIS   B 1 138 ? 30.485 -31.518 1.930   1.00 19.86 ?  138 HIS   B CE1  1 
ATOM   5941 N NE2  . HIS   B 1 138 ? 31.403 -30.952 2.693   1.00 19.14 ?  138 HIS   B NE2  1 
ATOM   5942 H H    . HIS   B 1 138 ? 34.838 -34.755 -0.522  1.00 18.90 ?  138 HIS   B H    1 
ATOM   5943 H HA   . HIS   B 1 138 ? 32.573 -33.511 -0.972  1.00 19.50 ?  138 HIS   B HA   1 
ATOM   5944 H HB2  . HIS   B 1 138 ? 32.999 -34.416 1.116   1.00 20.90 ?  138 HIS   B HB2  1 
ATOM   5945 H HB3  . HIS   B 1 138 ? 34.205 -33.403 1.326   1.00 20.90 ?  138 HIS   B HB3  1 
ATOM   5946 H HD1  . HIS   B 1 138 ? 30.661 -32.991 0.663   1.00 23.88 ?  138 HIS   B HD1  1 
ATOM   5947 H HD2  . HIS   B 1 138 ? 33.410 -31.366 2.893   1.00 22.61 ?  138 HIS   B HD2  1 
ATOM   5948 H HE1  . HIS   B 1 138 ? 29.581 -31.287 1.891   1.00 23.81 ?  138 HIS   B HE1  1 
ATOM   5949 N N    . SER   B 1 139 ? 35.158 -31.624 -0.818  1.00 14.50 ?  139 SER   B N    1 
ATOM   5950 C CA   . SER   B 1 139 ? 35.598 -30.275 -1.138  1.00 13.81 ?  139 SER   B CA   1 
ATOM   5951 C C    . SER   B 1 139 ? 35.261 -29.920 -2.578  1.00 13.37 ?  139 SER   B C    1 
ATOM   5952 O O    . SER   B 1 139 ? 34.812 -28.803 -2.855  1.00 13.49 ?  139 SER   B O    1 
ATOM   5953 C CB   . SER   B 1 139 ? 37.091 -30.135 -0.871  1.00 14.47 ?  139 SER   B CB   1 
ATOM   5954 O OG   . SER   B 1 139 ? 37.502 -28.797 -1.121  1.00 14.57 ?  139 SER   B OG   1 
ATOM   5955 H H    . SER   B 1 139 ? 35.778 -32.170 -0.592  1.00 17.38 ?  139 SER   B H    1 
ATOM   5956 H HA   . SER   B 1 139 ? 35.130 -29.649 -0.570  1.00 16.54 ?  139 SER   B HA   1 
ATOM   5957 H HB2  . SER   B 1 139 ? 37.268 -30.362 0.057   1.00 17.34 ?  139 SER   B HB2  1 
ATOM   5958 H HB3  . SER   B 1 139 ? 37.580 -30.736 -1.458  1.00 17.34 ?  139 SER   B HB3  1 
ATOM   5959 H HG   . SER   B 1 139 ? 38.328 -28.722 -0.965  1.00 17.46 ?  139 SER   B HG   1 
ATOM   5960 N N    . LEU   B 1 140 ? 35.447 -30.864 -3.505  1.00 13.24 ?  140 LEU   B N    1 
ATOM   5961 C CA   . LEU   B 1 140 ? 35.084 -30.611 -4.894  1.00 13.01 ?  140 LEU   B CA   1 
ATOM   5962 C C    . LEU   B 1 140 ? 33.582 -30.380 -5.028  1.00 13.41 ?  140 LEU   B C    1 
ATOM   5963 O O    . LEU   B 1 140 ? 33.147 -29.498 -5.773  1.00 13.78 ?  140 LEU   B O    1 
ATOM   5964 C CB   . LEU   B 1 140 ? 35.556 -31.769 -5.779  1.00 13.30 ?  140 LEU   B CB   1 
ATOM   5965 C CG   . LEU   B 1 140 ? 35.202 -31.662 -7.257  1.00 13.69 ?  140 LEU   B CG   1 
ATOM   5966 C CD1  . LEU   B 1 140 ? 35.764 -30.379 -7.850  1.00 14.68 ?  140 LEU   B CD1  1 
ATOM   5967 C CD2  . LEU   B 1 140 ? 35.697 -32.887 -8.004  1.00 14.58 ?  140 LEU   B CD2  1 
ATOM   5968 H H    . LEU   B 1 140 ? 35.772 -31.647 -3.360  1.00 15.86 ?  140 LEU   B H    1 
ATOM   5969 H HA   . LEU   B 1 140 ? 35.540 -29.808 -5.196  1.00 15.59 ?  140 LEU   B HA   1 
ATOM   5970 H HB2  . LEU   B 1 140 ? 36.522 -31.833 -5.722  1.00 15.94 ?  140 LEU   B HB2  1 
ATOM   5971 H HB3  . LEU   B 1 140 ? 35.158 -32.591 -5.452  1.00 15.94 ?  140 LEU   B HB3  1 
ATOM   5972 H HG   . LEU   B 1 140 ? 34.236 -31.625 -7.348  1.00 16.41 ?  140 LEU   B HG   1 
ATOM   5973 H HD11 . LEU   B 1 140 ? 35.646 -30.398 -8.812  1.00 17.59 ?  140 LEU   B HD11 1 
ATOM   5974 H HD12 . LEU   B 1 140 ? 35.287 -29.619 -7.475  1.00 17.59 ?  140 LEU   B HD12 1 
ATOM   5975 H HD13 . LEU   B 1 140 ? 36.707 -30.317 -7.632  1.00 17.59 ?  140 LEU   B HD13 1 
ATOM   5976 H HD21 . LEU   B 1 140 ? 35.459 -32.794 -8.941  1.00 17.47 ?  140 LEU   B HD21 1 
ATOM   5977 H HD22 . LEU   B 1 140 ? 36.656 -32.944 -7.907  1.00 17.47 ?  140 LEU   B HD22 1 
ATOM   5978 H HD23 . LEU   B 1 140 ? 35.270 -33.669 -7.629  1.00 17.47 ?  140 LEU   B HD23 1 
ATOM   5979 N N    . ARG   B 1 141 ? 32.778 -31.169 -4.310  1.00 13.60 ?  141 ARG   B N    1 
ATOM   5980 C CA   . ARG   B 1 141 ? 31.326 -30.998 -4.292  1.00 14.75 ?  141 ARG   B CA   1 
ATOM   5981 C C    . ARG   B 1 141 ? 30.947 -29.587 -3.862  1.00 14.24 ?  141 ARG   B C    1 
ATOM   5982 O O    . ARG   B 1 141 ? 30.141 -28.914 -4.520  1.00 14.42 ?  141 ARG   B O    1 
ATOM   5983 C CB   . ARG   B 1 141 ? 30.739 -32.029 -3.316  1.00 16.31 ?  141 ARG   B CB   1 
ATOM   5984 C CG   . ARG   B 1 141 ? 29.269 -31.910 -2.988  1.00 18.67 ?  141 ARG   B CG   1 
ATOM   5985 C CD   . ARG   B 1 141 ? 28.468 -32.542 -4.052  1.00 20.71 ?  141 ARG   B CD   1 
ATOM   5986 N NE   . ARG   B 1 141 ? 28.212 -31.635 -5.159  1.00 21.34 ?  141 ARG   B NE   1 
ATOM   5987 C CZ   . ARG   B 1 141 ? 28.227 -31.986 -6.438  1.00 20.62 ?  141 ARG   B CZ   1 
ATOM   5988 N NH1  . ARG   B 1 141 ? 28.687 -33.164 -6.830  1.00 20.49 ?  141 ARG   B NH1  1 
ATOM   5989 N NH2  . ARG   B 1 141 ? 27.763 -31.132 -7.347  1.00 21.32 ?  141 ARG   B NH2  1 
ATOM   5990 H H    . ARG   B 1 141 ? 33.060 -31.817 -3.821  1.00 16.30 ?  141 ARG   B H    1 
ATOM   5991 H HA   . ARG   B 1 141 ? 30.967 -31.157 -5.174  1.00 17.67 ?  141 ARG   B HA   1 
ATOM   5992 H HB2  . ARG   B 1 141 ? 30.892 -32.912 -3.689  1.00 19.55 ?  141 ARG   B HB2  1 
ATOM   5993 H HB3  . ARG   B 1 141 ? 31.225 -31.958 -2.479  1.00 19.55 ?  141 ARG   B HB3  1 
ATOM   5994 H HG2  . ARG   B 1 141 ? 29.096 -32.360 -2.149  1.00 22.38 ?  141 ARG   B HG2  1 
ATOM   5995 H HG3  . ARG   B 1 141 ? 29.018 -30.971 -2.921  1.00 22.38 ?  141 ARG   B HG3  1 
ATOM   5996 H HD2  . ARG   B 1 141 ? 28.944 -33.323 -4.386  1.00 24.83 ?  141 ARG   B HD2  1 
ATOM   5997 H HD3  . ARG   B 1 141 ? 27.621 -32.820 -3.678  1.00 24.83 ?  141 ARG   B HD3  1 
ATOM   5998 H HE   . ARG   B 1 141 ? 28.007 -30.822 -4.966  1.00 25.59 ?  141 ARG   B HE   1 
ATOM   5999 H HH11 . ARG   B 1 141 ? 28.974 -33.735 -6.253  1.00 24.56 ?  141 ARG   B HH11 1 
ATOM   6000 H HH12 . ARG   B 1 141 ? 28.694 -33.363 -7.663  1.00 24.56 ?  141 ARG   B HH12 1 
ATOM   6001 H HH21 . ARG   B 1 141 ? 27.470 -30.359 -7.104  1.00 25.56 ?  141 ARG   B HH21 1 
ATOM   6002 H HH22 . ARG   B 1 141 ? 27.790 -31.335 -8.182  1.00 25.56 ?  141 ARG   B HH22 1 
ATOM   6003 N N    . VAL   B 1 142 ? 31.500 -29.140 -2.735  1.00 13.67 ?  142 VAL   B N    1 
ATOM   6004 C CA   . VAL   B 1 142 ? 31.170 -27.805 -2.250  1.00 13.52 ?  142 VAL   B CA   1 
ATOM   6005 C C    . VAL   B 1 142 ? 31.642 -26.750 -3.243  1.00 13.22 ?  142 VAL   B C    1 
ATOM   6006 O O    . VAL   B 1 142 ? 30.940 -25.768 -3.506  1.00 13.99 ?  142 VAL   B O    1 
ATOM   6007 C CB   . VAL   B 1 142 ? 31.717 -27.577 -0.827  1.00 14.54 ?  142 VAL   B CB   1 
ATOM   6008 C CG1  . VAL   B 1 142 ? 31.403 -26.153 -0.348  1.00 14.21 ?  142 VAL   B CG1  1 
ATOM   6009 C CG2  . VAL   B 1 142 ? 31.129 -28.601 0.135   1.00 15.12 ?  142 VAL   B CG2  1 
ATOM   6010 H H    . VAL   B 1 142 ? 32.060 -29.577 -2.242  1.00 16.38 ?  142 VAL   B H    1 
ATOM   6011 H HA   . VAL   B 1 142 ? 30.211 -27.733 -2.194  1.00 16.20 ?  142 VAL   B HA   1 
ATOM   6012 H HB   . VAL   B 1 142 ? 32.682 -27.688 -0.828  1.00 17.43 ?  142 VAL   B HB   1 
ATOM   6013 H HG11 . VAL   B 1 142 ? 31.596 -26.089 0.600   1.00 17.03 ?  142 VAL   B HG11 1 
ATOM   6014 H HG12 . VAL   B 1 142 ? 31.958 -25.525 -0.840  1.00 17.03 ?  142 VAL   B HG12 1 
ATOM   6015 H HG13 . VAL   B 1 142 ? 30.467 -25.966 -0.510  1.00 17.03 ?  142 VAL   B HG13 1 
ATOM   6016 H HG21 . VAL   B 1 142 ? 31.445 -28.414 1.032   1.00 18.12 ?  142 VAL   B HG21 1 
ATOM   6017 H HG22 . VAL   B 1 142 ? 30.161 -28.542 0.106   1.00 18.12 ?  142 VAL   B HG22 1 
ATOM   6018 H HG23 . VAL   B 1 142 ? 31.413 -29.490 -0.137  1.00 18.12 ?  142 VAL   B HG23 1 
ATOM   6019 N N    . CYS   B 1 143 ? 32.824 -26.948 -3.828  1.00 12.74 ?  143 CYS   B N    1 
ATOM   6020 C CA   . CYS   B 1 143 ? 33.322 -26.008 -4.829  1.00 12.80 ?  143 CYS   B CA   1 
ATOM   6021 C C    . CYS   B 1 143 ? 32.325 -25.861 -5.974  1.00 12.89 ?  143 CYS   B C    1 
ATOM   6022 O O    . CYS   B 1 143 ? 31.915 -24.749 -6.325  1.00 13.25 ?  143 CYS   B O    1 
ATOM   6023 C CB   . CYS   B 1 143 ? 34.680 -26.490 -5.352  1.00 13.29 ?  143 CYS   B CB   1 
ATOM   6024 S SG   . CYS   B 1 143 ? 35.430 -25.392 -6.577  1.00 13.48 ?  143 CYS   B SG   1 
ATOM   6025 H H    . CYS   B 1 143 ? 33.356 -27.605 -3.661  1.00 15.27 ?  143 CYS   B H    1 
ATOM   6026 H HA   . CYS   B 1 143 ? 33.446 -25.136 -4.423  1.00 15.34 ?  143 CYS   B HA   1 
ATOM   6027 H HB2  . CYS   B 1 143 ? 35.299 -26.565 -4.606  1.00 15.92 ?  143 CYS   B HB2  1 
ATOM   6028 H HB3  . CYS   B 1 143 ? 34.567 -27.356 -5.764  1.00 15.92 ?  143 CYS   B HB3  1 
ATOM   6029 H HG   . CYS   B 1 143 ? 36.506 -25.823 -6.895  1.00 16.15 ?  143 CYS   B HG   1 
ATOM   6030 N N    . VAL   B 1 144 ? 31.925 -26.984 -6.571  1.00 13.39 ?  144 VAL   B N    1 
ATOM   6031 C CA   . VAL   B 1 144 ? 31.016 -26.923 -7.713  1.00 14.29 ?  144 VAL   B CA   1 
ATOM   6032 C C    . VAL   B 1 144 ? 29.670 -26.313 -7.336  1.00 14.51 ?  144 VAL   B C    1 
ATOM   6033 O O    . VAL   B 1 144 ? 29.051 -25.607 -8.146  1.00 15.63 ?  144 VAL   B O    1 
ATOM   6034 C CB   . VAL   B 1 144 ? 30.863 -28.326 -8.312  1.00 17.25 ?  144 VAL   B CB   1 
ATOM   6035 C CG1  . VAL   B 1 144 ? 29.596 -28.437 -9.153  1.00 20.34 ?  144 VAL   B CG1  1 
ATOM   6036 C CG2  . VAL   B 1 144 ? 32.112 -28.704 -9.108  1.00 17.64 ?  144 VAL   B CG2  1 
ATOM   6037 H H    . VAL   B 1 144 ? 32.166 -27.779 -6.342  1.00 16.04 ?  144 VAL   B H    1 
ATOM   6038 H HA   . VAL   B 1 144 ? 31.409 -26.361 -8.393  1.00 17.13 ?  144 VAL   B HA   1 
ATOM   6039 H HB   . VAL   B 1 144 ? 30.784 -28.968 -7.588  1.00 20.68 ?  144 VAL   B HB   1 
ATOM   6040 H HG11 . VAL   B 1 144 ? 29.674 -29.215 -9.734  1.00 24.39 ?  144 VAL   B HG11 1 
ATOM   6041 H HG12 . VAL   B 1 144 ? 28.835 -28.549 -8.563  1.00 24.39 ?  144 VAL   B HG12 1 
ATOM   6042 H HG13 . VAL   B 1 144 ? 29.498 -27.638 -9.687  1.00 24.39 ?  144 VAL   B HG13 1 
ATOM   6043 H HG21 . VAL   B 1 144 ? 31.999 -29.597 -9.474  1.00 21.14 ?  144 VAL   B HG21 1 
ATOM   6044 H HG22 . VAL   B 1 144 ? 32.230 -28.066 -9.832  1.00 21.14 ?  144 VAL   B HG22 1 
ATOM   6045 H HG23 . VAL   B 1 144 ? 32.881 -28.683 -8.520  1.00 21.14 ?  144 VAL   B HG23 1 
ATOM   6046 N N    . ASP   B 1 145 ? 29.202 -26.555 -6.115  1.00 14.62 ?  145 ASP   B N    1 
ATOM   6047 C CA   . ASP   B 1 145 ? 27.892 -26.084 -5.687  1.00 15.15 ?  145 ASP   B CA   1 
ATOM   6048 C C    . ASP   B 1 145 ? 27.924 -24.664 -5.140  1.00 14.70 ?  145 ASP   B C    1 
ATOM   6049 O O    . ASP   B 1 145 ? 26.861 -24.121 -4.805  1.00 16.05 ?  145 ASP   B O    1 
ATOM   6050 C CB   . ASP   B 1 145 ? 27.309 -26.999 -4.603  1.00 17.07 ?  145 ASP   B CB   1 
ATOM   6051 C CG   . ASP   B 1 145 ? 26.941 -28.376 -5.111  1.00 18.62 ?  145 ASP   B CG   1 
ATOM   6052 O OD1  . ASP   B 1 145 ? 26.838 -28.570 -6.339  1.00 18.59 ?  145 ASP   B OD1  1 
ATOM   6053 O OD2  . ASP   B 1 145 ? 26.748 -29.260 -4.256  1.00 20.74 -1 145 ASP   B OD2  1 
ATOM   6054 H H    . ASP   B 1 145 ? 29.634 -26.984 -5.508  1.00 17.52 ?  145 ASP   B H    1 
ATOM   6055 H HA   . ASP   B 1 145 ? 27.297 -26.078 -6.450  1.00 18.16 ?  145 ASP   B HA   1 
ATOM   6056 H HB2  . ASP   B 1 145 ? 27.960 -27.103 -3.902  1.00 20.46 ?  145 ASP   B HB2  1 
ATOM   6057 H HB3  . ASP   B 1 145 ? 26.504 -26.576 -4.252  1.00 20.46 ?  145 ASP   B HB3  1 
ATOM   6058 N N    . THR   B 1 146 ? 29.104 -24.052 -5.026  1.00 12.99 ?  146 THR   B N    1 
ATOM   6059 C CA   . THR   B 1 146 ? 29.242 -22.729 -4.422  1.00 12.85 ?  146 THR   B CA   1 
ATOM   6060 C C    . THR   B 1 146 ? 29.875 -21.696 -5.340  1.00 12.55 ?  146 THR   B C    1 
ATOM   6061 O O    . THR   B 1 146 ? 29.423 -20.539 -5.385  1.00 13.24 ?  146 THR   B O    1 
ATOM   6062 C CB   . THR   B 1 146 ? 30.065 -22.832 -3.130  1.00 13.46 ?  146 THR   B CB   1 
ATOM   6063 O OG1  . THR   B 1 146 ? 29.488 -23.821 -2.263  1.00 13.69 ?  146 THR   B OG1  1 
ATOM   6064 C CG2  . THR   B 1 146 ? 30.150 -21.487 -2.426  1.00 13.90 ?  146 THR   B CG2  1 
ATOM   6065 H H    . THR   B 1 146 ? 29.856 -24.384 -5.293  1.00 15.56 ?  146 THR   B H    1 
ATOM   6066 H HA   . THR   B 1 146 ? 28.365 -22.402 -4.182  1.00 15.39 ?  146 THR   B HA   1 
ATOM   6067 H HB   . THR   B 1 146 ? 30.970 -23.098 -3.353  1.00 16.13 ?  146 THR   B HB   1 
ATOM   6068 H HG1  . THR   B 1 146 ? 29.517 -24.577 -2.634  1.00 16.41 ?  146 THR   B HG1  1 
ATOM   6069 H HG21 . THR   B 1 146 ? 30.476 -21.604 -1.522  1.00 16.66 ?  146 THR   B HG21 1 
ATOM   6070 H HG22 . THR   B 1 146 ? 30.761 -20.898 -2.904  1.00 16.66 ?  146 THR   B HG22 1 
ATOM   6071 H HG23 . THR   B 1 146 ? 29.275 -21.071 -2.395  1.00 16.66 ?  146 THR   B HG23 1 
ATOM   6072 N N    . VAL   B 1 147 ? 30.939 -22.068 -6.038  1.00 12.51 ?  147 VAL   B N    1 
ATOM   6073 C CA   . VAL   B 1 147 ? 31.663 -21.121 -6.872  1.00 12.27 ?  147 VAL   B CA   1 
ATOM   6074 C C    . VAL   B 1 147 ? 30.928 -20.983 -8.193  1.00 12.61 ?  147 VAL   B C    1 
ATOM   6075 O O    . VAL   B 1 147 ? 30.559 -21.986 -8.822  1.00 13.72 ?  147 VAL   B O    1 
ATOM   6076 C CB   . VAL   B 1 147 ? 33.115 -21.583 -7.080  1.00 12.62 ?  147 VAL   B CB   1 
ATOM   6077 C CG1  . VAL   B 1 147 ? 33.876 -20.554 -7.897  1.00 12.74 ?  147 VAL   B CG1  1 
ATOM   6078 C CG2  . VAL   B 1 147 ? 33.800 -21.793 -5.739  1.00 12.72 ?  147 VAL   B CG2  1 
ATOM   6079 H H    . VAL   B 1 147 ? 31.263 -22.867 -6.049  1.00 14.99 ?  147 VAL   B H    1 
ATOM   6080 H HA   . VAL   B 1 147 ? 31.683 -20.256 -6.438  1.00 14.70 ?  147 VAL   B HA   1 
ATOM   6081 H HB   . VAL   B 1 147 ? 33.122 -22.427 -7.565  1.00 15.12 ?  147 VAL   B HB   1 
ATOM   6082 H HG11 . VAL   B 1 147 ? 34.819 -20.778 -7.890  1.00 15.27 ?  147 VAL   B HG11 1 
ATOM   6083 H HG12 . VAL   B 1 147 ? 33.542 -20.557 -8.808  1.00 15.27 ?  147 VAL   B HG12 1 
ATOM   6084 H HG13 . VAL   B 1 147 ? 33.744 -19.677 -7.499  1.00 15.27 ?  147 VAL   B HG13 1 
ATOM   6085 H HG21 . VAL   B 1 147 ? 34.739 -21.998 -5.891  1.00 15.24 ?  147 VAL   B HG21 1 
ATOM   6086 H HG22 . VAL   B 1 147 ? 33.722 -20.983 -5.213  1.00 15.24 ?  147 VAL   B HG22 1 
ATOM   6087 H HG23 . VAL   B 1 147 ? 33.376 -22.532 -5.275  1.00 15.24 ?  147 VAL   B HG23 1 
ATOM   6088 N N    . ARG   B 1 148 ? 30.715 -19.732 -8.608  1.00 12.71 ?  148 ARG   B N    1 
ATOM   6089 C CA   . ARG   B 1 148 ? 30.095 -19.415 -9.884  1.00 12.88 ?  148 ARG   B CA   1 
ATOM   6090 C C    . ARG   B 1 148 ? 31.054 -18.743 -10.856 1.00 12.83 ?  148 ARG   B C    1 
ATOM   6091 O O    . ARG   B 1 148 ? 30.770 -18.719 -12.054 1.00 14.19 ?  148 ARG   B O    1 
ATOM   6092 C CB   . ARG   B 1 148 ? 28.852 -18.531 -9.676  1.00 13.11 ?  148 ARG   B CB   1 
ATOM   6093 C CG   . ARG   B 1 148 ? 27.787 -19.233 -8.842  1.00 13.91 ?  148 ARG   B CG   1 
ATOM   6094 C CD   . ARG   B 1 148 ? 26.578 -18.358 -8.546  1.00 14.89 ?  148 ARG   B CD   1 
ATOM   6095 N NE   . ARG   B 1 148 ? 26.950 -17.156 -7.812  1.00 14.72 ?  148 ARG   B NE   1 
ATOM   6096 C CZ   . ARG   B 1 148 ? 27.257 -17.125 -6.522  1.00 14.00 ?  148 ARG   B CZ   1 
ATOM   6097 N NH1  . ARG   B 1 148 ? 27.195 -18.212 -5.767  1.00 14.27 ?  148 ARG   B NH1  1 
ATOM   6098 N NH2  . ARG   B 1 148 ? 27.645 -15.975 -5.978  1.00 13.94 ?  148 ARG   B NH2  1 
ATOM   6099 H H    . ARG   B 1 148 ? 30.938 -19.031 -8.152  1.00 15.23 ?  148 ARG   B H    1 
ATOM   6100 H HA   . ARG   B 1 148 ? 29.801 -20.242 -10.293 1.00 15.43 ?  148 ARG   B HA   1 
ATOM   6101 H HB2  . ARG   B 1 148 ? 29.113 -17.721 -9.214  1.00 15.71 ?  148 ARG   B HB2  1 
ATOM   6102 H HB3  . ARG   B 1 148 ? 28.468 -18.319 -10.539 1.00 15.71 ?  148 ARG   B HB3  1 
ATOM   6103 H HG2  . ARG   B 1 148 ? 27.477 -20.016 -9.323  1.00 16.67 ?  148 ARG   B HG2  1 
ATOM   6104 H HG3  . ARG   B 1 148 ? 28.175 -19.499 -7.994  1.00 16.67 ?  148 ARG   B HG3  1 
ATOM   6105 H HD2  . ARG   B 1 148 ? 26.167 -18.087 -9.382  1.00 17.84 ?  148 ARG   B HD2  1 
ATOM   6106 H HD3  . ARG   B 1 148 ? 25.943 -18.860 -8.009  1.00 17.84 ?  148 ARG   B HD3  1 
ATOM   6107 H HE   . ARG   B 1 148 ? 26.983 -16.417 -8.245  1.00 17.64 ?  148 ARG   B HE   1 
ATOM   6108 H HH11 . ARG   B 1 148 ? 26.943 -18.962 -6.103  1.00 17.10 ?  148 ARG   B HH11 1 
ATOM   6109 H HH12 . ARG   B 1 148 ? 27.394 -18.167 -4.928  1.00 17.10 ?  148 ARG   B HH12 1 
ATOM   6110 H HH21 . ARG   B 1 148 ? 27.694 -15.266 -6.462  1.00 16.70 ?  148 ARG   B HH21 1 
ATOM   6111 H HH22 . ARG   B 1 148 ? 27.847 -15.939 -5.143  1.00 16.70 ?  148 ARG   B HH22 1 
ATOM   6112 N N    . THR   B 1 149 ? 32.166 -18.194 -10.371 1.00 12.85 ?  149 THR   B N    1 
ATOM   6113 C CA   . THR   B 1 149 ? 33.200 -17.627 -11.223 1.00 13.01 ?  149 THR   B CA   1 
ATOM   6114 C C    . THR   B 1 149 ? 34.088 -18.764 -11.731 1.00 12.78 ?  149 THR   B C    1 
ATOM   6115 O O    . THR   B 1 149 ? 33.888 -19.933 -11.397 1.00 13.18 ?  149 THR   B O    1 
ATOM   6116 C CB   . THR   B 1 149 ? 33.973 -16.576 -10.441 1.00 13.08 ?  149 THR   B CB   1 
ATOM   6117 O OG1  . THR   B 1 149 ? 34.437 -17.180 -9.232  1.00 12.86 ?  149 THR   B OG1  1 
ATOM   6118 C CG2  . THR   B 1 149 ? 33.075 -15.378 -10.138 1.00 13.47 ?  149 THR   B CG2  1 
ATOM   6119 H H    . THR   B 1 149 ? 32.335 -18.127 -9.533  1.00 15.40 ?  149 THR   B H    1 
ATOM   6120 H HA   . THR   B 1 149 ? 32.787 -17.198 -11.989 1.00 15.59 ?  149 THR   B HA   1 
ATOM   6121 H HB   . THR   B 1 149 ? 34.730 -16.277 -10.964 1.00 15.67 ?  149 THR   B HB   1 
ATOM   6122 H HG1  . THR   B 1 149 ? 34.863 -16.616 -8.772  1.00 15.41 ?  149 THR   B HG1  1 
ATOM   6123 H HG21 . THR   B 1 149 ? 33.577 -14.701 -9.657  1.00 16.14 ?  149 THR   B HG21 1 
ATOM   6124 H HG22 . THR   B 1 149 ? 32.742 -14.994 -10.965 1.00 16.14 ?  149 THR   B HG22 1 
ATOM   6125 H HG23 . THR   B 1 149 ? 32.320 -15.654 -9.595  1.00 16.14 ?  149 THR   B HG23 1 
ATOM   6126 N N    . ASN   B 1 150 ? 35.060 -18.445 -12.572 1.00 12.58 ?  150 ASN   B N    1 
ATOM   6127 C CA   . ASN   B 1 150 ? 35.824 -19.470 -13.273 1.00 13.19 ?  150 ASN   B CA   1 
ATOM   6128 C C    . ASN   B 1 150 ? 36.988 -19.924 -12.402 1.00 12.90 ?  150 ASN   B C    1 
ATOM   6129 O O    . ASN   B 1 150 ? 37.914 -19.153 -12.140 1.00 13.64 ?  150 ASN   B O    1 
ATOM   6130 C CB   . ASN   B 1 150 ? 36.302 -18.929 -14.612 1.00 15.27 ?  150 ASN   B CB   1 
ATOM   6131 C CG   . ASN   B 1 150 ? 35.163 -18.713 -15.565 1.00 17.81 ?  150 ASN   B CG   1 
ATOM   6132 O OD1  . ASN   B 1 150 ? 34.286 -19.560 -15.681 1.00 18.68 ?  150 ASN   B OD1  1 
ATOM   6133 N ND2  . ASN   B 1 150 ? 35.135 -17.561 -16.216 1.00 19.55 ?  150 ASN   B ND2  1 
ATOM   6134 H H    . ASN   B 1 150 ? 35.302 -17.639 -12.753 1.00 15.08 ?  150 ASN   B H    1 
ATOM   6135 H HA   . ASN   B 1 150 ? 35.246 -20.237 -13.444 1.00 15.81 ?  150 ASN   B HA   1 
ATOM   6136 H HB2  . ASN   B 1 150 ? 36.744 -18.076 -14.467 1.00 18.30 ?  150 ASN   B HB2  1 
ATOM   6137 H HB3  . ASN   B 1 150 ? 36.918 -19.561 -15.010 1.00 18.30 ?  150 ASN   B HB3  1 
ATOM   6138 H HD21 . ASN   B 1 150 ? 34.498 -17.394 -16.773 1.00 23.44 ?  150 ASN   B HD21 1 
ATOM   6139 H HD22 . ASN   B 1 150 ? 35.760 -16.980 -16.098 1.00 23.44 ?  150 ASN   B HD22 1 
ATOM   6140 N N    . VAL   B 1 151 ? 36.944 -21.173 -11.950 1.00 12.35 ?  151 VAL   B N    1 
ATOM   6141 C CA   . VAL   B 1 151 ? 37.958 -21.704 -11.054 1.00 12.48 ?  151 VAL   B CA   1 
ATOM   6142 C C    . VAL   B 1 151 ? 38.669 -22.873 -11.727 1.00 12.38 ?  151 VAL   B C    1 
ATOM   6143 O O    . VAL   B 1 151 ? 38.030 -23.810 -12.229 1.00 13.29 ?  151 VAL   B O    1 
ATOM   6144 C CB   . VAL   B 1 151 ? 37.388 -22.050 -9.664  1.00 13.72 ?  151 VAL   B CB   1 
ATOM   6145 C CG1  . VAL   B 1 151 ? 36.221 -23.037 -9.758  1.00 15.03 ?  151 VAL   B CG1  1 
ATOM   6146 C CG2  . VAL   B 1 151 ? 38.492 -22.565 -8.748  1.00 14.57 ?  151 VAL   B CG2  1 
ATOM   6147 H H    . VAL   B 1 151 ? 36.323 -21.740 -12.154 1.00 14.79 ?  151 VAL   B H    1 
ATOM   6148 H HA   . VAL   B 1 151 ? 38.621 -21.013 -10.915 1.00 14.95 ?  151 VAL   B HA   1 
ATOM   6149 H HB   . VAL   B 1 151 ? 37.042 -21.235 -9.264  1.00 16.44 ?  151 VAL   B HB   1 
ATOM   6150 H HG11 . VAL   B 1 151 ? 35.892 -23.235 -8.865  1.00 18.01 ?  151 VAL   B HG11 1 
ATOM   6151 H HG12 . VAL   B 1 151 ? 35.505 -22.641 -10.286 1.00 18.01 ?  151 VAL   B HG12 1 
ATOM   6152 H HG13 . VAL   B 1 151 ? 36.524 -23.856 -10.184 1.00 18.01 ?  151 VAL   B HG13 1 
ATOM   6153 H HG21 . VAL   B 1 151 ? 38.143 -22.635 -7.844  1.00 17.46 ?  151 VAL   B HG21 1 
ATOM   6154 H HG22 . VAL   B 1 151 ? 38.779 -23.439 -9.057  1.00 17.46 ?  151 VAL   B HG22 1 
ATOM   6155 H HG23 . VAL   B 1 151 ? 39.235 -21.944 -8.767  1.00 17.46 ?  151 VAL   B HG23 1 
ATOM   6156 N N    . TYR   B 1 152 ? 39.994 -22.785 -11.747 1.00 11.86 ?  152 TYR   B N    1 
ATOM   6157 C CA   . TYR   B 1 152 ? 40.899 -23.768 -12.324 1.00 12.13 ?  152 TYR   B CA   1 
ATOM   6158 C C    . TYR   B 1 152 ? 41.612 -24.450 -11.162 1.00 11.38 ?  152 TYR   B C    1 
ATOM   6159 O O    . TYR   B 1 152 ? 42.458 -23.840 -10.501 1.00 11.93 ?  152 TYR   B O    1 
ATOM   6160 C CB   . TYR   B 1 152 ? 41.872 -23.059 -13.268 1.00 12.83 ?  152 TYR   B CB   1 
ATOM   6161 C CG   . TYR   B 1 152 ? 41.190 -22.600 -14.535 1.00 13.31 ?  152 TYR   B CG   1 
ATOM   6162 C CD1  . TYR   B 1 152 ? 40.517 -21.378 -14.596 1.00 13.46 ?  152 TYR   B CD1  1 
ATOM   6163 C CD2  . TYR   B 1 152 ? 41.197 -23.403 -15.665 1.00 14.58 ?  152 TYR   B CD2  1 
ATOM   6164 C CE1  . TYR   B 1 152 ? 39.882 -20.978 -15.748 1.00 14.70 ?  152 TYR   B CE1  1 
ATOM   6165 C CE2  . TYR   B 1 152 ? 40.559 -23.017 -16.819 1.00 15.21 ?  152 TYR   B CE2  1 
ATOM   6166 C CZ   . TYR   B 1 152 ? 39.909 -21.796 -16.860 1.00 15.28 ?  152 TYR   B CZ   1 
ATOM   6167 O OH   . TYR   B 1 152 ? 39.277 -21.421 -18.017 1.00 18.13 ?  152 TYR   B OH   1 
ATOM   6168 H H    . TYR   B 1 152 ? 40.421 -22.117 -11.402 1.00 14.21 ?  152 TYR   B H    1 
ATOM   6169 H HA   . TYR   B 1 152 ? 40.392 -24.429 -12.825 1.00 14.53 ?  152 TYR   B HA   1 
ATOM   6170 H HB2  . TYR   B 1 152 ? 42.238 -22.279 -12.815 1.00 15.37 ?  152 TYR   B HB2  1 
ATOM   6171 H HB3  . TYR   B 1 152 ? 42.586 -23.668 -13.507 1.00 15.37 ?  152 TYR   B HB3  1 
ATOM   6172 H HD1  . TYR   B 1 152 ? 40.498 -20.827 -13.844 1.00 16.12 ?  152 TYR   B HD1  1 
ATOM   6173 H HD2  . TYR   B 1 152 ? 41.637 -24.224 -15.636 1.00 17.48 ?  152 TYR   B HD2  1 
ATOM   6174 H HE1  . TYR   B 1 152 ? 39.436 -20.163 -15.784 1.00 17.62 ?  152 TYR   B HE1  1 
ATOM   6175 H HE2  . TYR   B 1 152 ? 40.580 -23.565 -17.571 1.00 18.22 ?  152 TYR   B HE2  1 
ATOM   6176 H HH   . TYR   B 1 152 ? 39.378 -22.011 -18.609 1.00 21.73 ?  152 TYR   B HH   1 
ATOM   6177 N N    . LEU   B 1 153 ? 41.241 -25.704 -10.896 1.00 11.56 ?  153 LEU   B N    1 
ATOM   6178 C CA   . LEU   B 1 153 ? 41.751 -26.456 -9.760  1.00 11.35 ?  153 LEU   B CA   1 
ATOM   6179 C C    . LEU   B 1 153 ? 42.983 -27.258 -10.156 1.00 11.66 ?  153 LEU   B C    1 
ATOM   6180 O O    . LEU   B 1 153 ? 42.966 -27.986 -11.149 1.00 12.74 ?  153 LEU   B O    1 
ATOM   6181 C CB   . LEU   B 1 153 ? 40.676 -27.418 -9.246  1.00 11.65 ?  153 LEU   B CB   1 
ATOM   6182 C CG   . LEU   B 1 153 ? 39.422 -26.750 -8.682  1.00 12.48 ?  153 LEU   B CG   1 
ATOM   6183 C CD1  . LEU   B 1 153 ? 38.317 -27.792 -8.539  1.00 13.44 ?  153 LEU   B CD1  1 
ATOM   6184 C CD2  . LEU   B 1 153 ? 39.710 -26.087 -7.343  1.00 12.84 ?  153 LEU   B CD2  1 
ATOM   6185 H H    . LEU   B 1 153 ? 40.672 -26.148 -11.376 1.00 13.85 ?  153 LEU   B H    1 
ATOM   6186 H HA   . LEU   B 1 153 ? 41.977 -25.842 -9.047  1.00 13.59 ?  153 LEU   B HA   1 
ATOM   6187 H HB2  . LEU   B 1 153 ? 40.392 -27.991 -9.974  1.00 13.96 ?  153 LEU   B HB2  1 
ATOM   6188 H HB3  . LEU   B 1 153 ? 41.055 -27.958 -8.534  1.00 13.96 ?  153 LEU   B HB3  1 
ATOM   6189 H HG   . LEU   B 1 153 ? 39.114 -26.062 -9.297  1.00 14.95 ?  153 LEU   B HG   1 
ATOM   6190 H HD11 . LEU   B 1 153 ? 37.512 -27.355 -8.212  1.00 16.11 ?  153 LEU   B HD11 1 
ATOM   6191 H HD12 . LEU   B 1 153 ? 38.147 -28.187 -9.406  1.00 16.11 ?  153 LEU   B HD12 1 
ATOM   6192 H HD13 . LEU   B 1 153 ? 38.604 -28.468 -7.911  1.00 16.11 ?  153 LEU   B HD13 1 
ATOM   6193 H HD21 . LEU   B 1 153 ? 38.891 -25.711 -6.987  1.00 15.39 ?  153 LEU   B HD21 1 
ATOM   6194 H HD22 . LEU   B 1 153 ? 40.059 -26.757 -6.731  1.00 15.39 ?  153 LEU   B HD22 1 
ATOM   6195 H HD23 . LEU   B 1 153 ? 40.369 -25.386 -7.471  1.00 15.39 ?  153 LEU   B HD23 1 
ATOM   6196 N N    . ALA   B 1 154 ? 44.031 -27.149 -9.350  1.00 11.94 ?  154 ALA   B N    1 
ATOM   6197 C CA   . ALA   B 1 154 ? 45.260 -27.909 -9.534  1.00 13.10 ?  154 ALA   B CA   1 
ATOM   6198 C C    . ALA   B 1 154 ? 45.330 -28.983 -8.458  1.00 13.71 ?  154 ALA   B C    1 
ATOM   6199 O O    . ALA   B 1 154 ? 45.265 -28.681 -7.259  1.00 15.18 ?  154 ALA   B O    1 
ATOM   6200 C CB   . ALA   B 1 154 ? 46.482 -26.996 -9.473  1.00 14.25 ?  154 ALA   B CB   1 
ATOM   6201 H H    . ALA   B 1 154 ? 44.048 -26.620 -8.667  1.00 14.31 ?  154 ALA   B H    1 
ATOM   6202 H HA   . ALA   B 1 154 ? 45.242 -28.340 -10.399 1.00 15.70 ?  154 ALA   B HA   1 
ATOM   6203 H HB1  . ALA   B 1 154 ? 47.280 -27.527 -9.598  1.00 17.08 ?  154 ALA   B HB1  1 
ATOM   6204 H HB2  . ALA   B 1 154 ? 46.413 -26.328 -10.177 1.00 17.08 ?  154 ALA   B HB2  1 
ATOM   6205 H HB3  . ALA   B 1 154 ? 46.507 -26.555 -8.607  1.00 17.08 ?  154 ALA   B HB3  1 
ATOM   6206 N N    . VAL   B 1 155 ? 45.445 -30.233 -8.891  1.00 12.66 ?  155 VAL   B N    1 
ATOM   6207 C CA   . VAL   B 1 155 ? 45.552 -31.384 -8.003  1.00 13.20 ?  155 VAL   B CA   1 
ATOM   6208 C C    . VAL   B 1 155 ? 46.893 -32.057 -8.277  1.00 12.69 ?  155 VAL   B C    1 
ATOM   6209 O O    . VAL   B 1 155 ? 47.135 -32.543 -9.387  1.00 14.46 ?  155 VAL   B O    1 
ATOM   6210 C CB   . VAL   B 1 155 ? 44.387 -32.373 -8.197  1.00 14.65 ?  155 VAL   B CB   1 
ATOM   6211 C CG1  . VAL   B 1 155 ? 44.563 -33.575 -7.283  1.00 14.67 ?  155 VAL   B CG1  1 
ATOM   6212 C CG2  . VAL   B 1 155 ? 43.050 -31.674 -7.936  1.00 15.57 ?  155 VAL   B CG2  1 
ATOM   6213 H H    . VAL   B 1 155 ? 45.474 -30.446 -9.724  1.00 15.17 ?  155 VAL   B H    1 
ATOM   6214 H HA   . VAL   B 1 155 ? 45.543 -31.085 -7.083  1.00 15.82 ?  155 VAL   B HA   1 
ATOM   6215 H HB   . VAL   B 1 155 ? 44.385 -32.687 -9.117  1.00 17.56 ?  155 VAL   B HB   1 
ATOM   6216 H HG11 . VAL   B 1 155 ? 43.735 -34.080 -7.260  1.00 17.58 ?  155 VAL   B HG11 1 
ATOM   6217 H HG12 . VAL   B 1 155 ? 45.280 -34.134 -7.624  1.00 17.58 ?  155 VAL   B HG12 1 
ATOM   6218 H HG13 . VAL   B 1 155 ? 44.783 -33.263 -6.390  1.00 17.58 ?  155 VAL   B HG13 1 
ATOM   6219 H HG21 . VAL   B 1 155 ? 42.334 -32.323 -8.023  1.00 18.66 ?  155 VAL   B HG21 1 
ATOM   6220 H HG22 . VAL   B 1 155 ? 43.058 -31.309 -7.038  1.00 18.66 ?  155 VAL   B HG22 1 
ATOM   6221 H HG23 . VAL   B 1 155 ? 42.932 -30.962 -8.583  1.00 18.66 ?  155 VAL   B HG23 1 
ATOM   6222 N N    . PHE   B 1 156 ? 47.760 -32.087 -7.262  1.00 13.52 ?  156 PHE   B N    1 
ATOM   6223 C CA   . PHE   B 1 156 ? 49.136 -32.550 -7.461  1.00 14.67 ?  156 PHE   B CA   1 
ATOM   6224 C C    . PHE   B 1 156 ? 49.224 -34.051 -7.738  1.00 15.55 ?  156 PHE   B C    1 
ATOM   6225 O O    . PHE   B 1 156 ? 49.947 -34.487 -8.645  1.00 17.34 ?  156 PHE   B O    1 
ATOM   6226 C CB   . PHE   B 1 156 ? 49.968 -32.182 -6.236  1.00 14.88 ?  156 PHE   B CB   1 
ATOM   6227 C CG   . PHE   B 1 156 ? 51.388 -32.651 -6.297  1.00 15.24 ?  156 PHE   B CG   1 
ATOM   6228 C CD1  . PHE   B 1 156 ? 52.267 -32.115 -7.218  1.00 17.04 ?  156 PHE   B CD1  1 
ATOM   6229 C CD2  . PHE   B 1 156 ? 51.853 -33.600 -5.408  1.00 15.62 ?  156 PHE   B CD2  1 
ATOM   6230 C CE1  . PHE   B 1 156 ? 53.585 -32.530 -7.266  1.00 17.72 ?  156 PHE   B CE1  1 
ATOM   6231 C CE2  . PHE   B 1 156 ? 53.169 -34.025 -5.455  1.00 16.97 ?  156 PHE   B CE2  1 
ATOM   6232 C CZ   . PHE   B 1 156 ? 54.030 -33.485 -6.386  1.00 17.53 ?  156 PHE   B CZ   1 
ATOM   6233 H H    . PHE   B 1 156 ? 47.576 -31.847 -6.457  1.00 16.20 ?  156 PHE   B H    1 
ATOM   6234 H HA   . PHE   B 1 156 ? 49.512 -32.087 -8.222  1.00 17.58 ?  156 PHE   B HA   1 
ATOM   6235 H HB2  . PHE   B 1 156 ? 49.979 -31.216 -6.148  1.00 17.84 ?  156 PHE   B HB2  1 
ATOM   6236 H HB3  . PHE   B 1 156 ? 49.562 -32.578 -5.449  1.00 17.84 ?  156 PHE   B HB3  1 
ATOM   6237 H HD1  . PHE   B 1 156 ? 51.970 -31.462 -7.815  1.00 20.42 ?  156 PHE   B HD1  1 
ATOM   6238 H HD2  . PHE   B 1 156 ? 51.269 -33.970 -4.784  1.00 18.73 ?  156 PHE   B HD2  1 
ATOM   6239 H HE1  . PHE   B 1 156 ? 54.170 -32.162 -7.896  1.00 21.24 ?  156 PHE   B HE1  1 
ATOM   6240 H HE2  . PHE   B 1 156 ? 53.468 -34.674 -4.861  1.00 20.34 ?  156 PHE   B HE2  1 
ATOM   6241 H HZ   . PHE   B 1 156 ? 54.916 -33.770 -6.418  1.00 21.01 ?  156 PHE   B HZ   1 
ATOM   6242 N N    . ASP   B 1 157 ? 48.556 -34.864 -6.933  1.00 15.84 ?  157 ASP   B N    1 
ATOM   6243 C CA   . ASP   B 1 157 ? 48.697 -36.314 -7.029  1.00 17.25 ?  157 ASP   B CA   1 
ATOM   6244 C C    . ASP   B 1 157 ? 47.783 -36.858 -8.123  1.00 17.37 ?  157 ASP   B C    1 
ATOM   6245 O O    . ASP   B 1 157 ? 46.556 -36.749 -8.021  1.00 16.83 ?  157 ASP   B O    1 
ATOM   6246 C CB   . ASP   B 1 157 ? 48.339 -36.927 -5.681  1.00 18.78 ?  157 ASP   B CB   1 
ATOM   6247 C CG   . ASP   B 1 157 ? 48.477 -38.434 -5.664  1.00 21.02 ?  157 ASP   B CG   1 
ATOM   6248 O OD1  . ASP   B 1 157 ? 48.796 -39.039 -6.715  1.00 21.62 ?  157 ASP   B OD1  1 
ATOM   6249 O OD2  . ASP   B 1 157 ? 48.280 -39.013 -4.579  1.00 23.16 -1 157 ASP   B OD2  1 
ATOM   6250 H H    . ASP   B 1 157 ? 48.018 -34.608 -6.316  1.00 18.98 ?  157 ASP   B H    1 
ATOM   6251 H HA   . ASP   B 1 157 ? 49.618 -36.549 -7.240  1.00 20.67 ?  157 ASP   B HA   1 
ATOM   6252 H HB2  . ASP   B 1 157 ? 48.915 -36.551 -4.998  1.00 22.51 ?  157 ASP   B HB2  1 
ATOM   6253 H HB3  . ASP   B 1 157 ? 47.413 -36.717 -5.478  1.00 22.51 ?  157 ASP   B HB3  1 
ATOM   6254 N N    . LYS   B 1 158 ? 48.379 -37.469 -9.154  1.00 18.67 ?  158 LYS   B N    1 
ATOM   6255 C CA   . LYS   B 1 158 ? 47.605 -38.088 -10.233 1.00 19.60 ?  158 LYS   B CA   1 
ATOM   6256 C C    . LYS   B 1 158 ? 46.548 -39.057 -9.702  1.00 19.22 ?  158 LYS   B C    1 
ATOM   6257 O O    . LYS   B 1 158 ? 45.441 -39.145 -10.249 1.00 19.32 ?  158 LYS   B O    1 
ATOM   6258 C CB   . LYS   B 1 158 ? 48.558 -38.808 -11.198 1.00 21.43 ?  158 LYS   B CB   1 
ATOM   6259 C CG   . LYS   B 1 158 ? 47.889 -39.715 -12.224 1.00 23.72 ?  158 LYS   B CG   1 
ATOM   6260 C CD   . LYS   B 1 158 ? 47.025 -38.937 -13.195 1.00 26.02 ?  158 LYS   B CD   1 
ATOM   6261 C CE   . LYS   B 1 158 ? 46.427 -39.855 -14.249 1.00 27.55 ?  158 LYS   B CE   1 
ATOM   6262 N NZ   . LYS   B 1 158 ? 45.361 -39.172 -15.040 1.00 27.85 ?  158 LYS   B NZ   1 
ATOM   6263 H H    . LYS   B 1 158 ? 49.233 -37.537 -9.250  1.00 22.38 ?  158 LYS   B H    1 
ATOM   6264 H HA   . LYS   B 1 158 ? 47.153 -37.391 -10.736 1.00 23.49 ?  158 LYS   B HA   1 
ATOM   6265 H HB2  . LYS   B 1 158 ? 49.064 -38.139 -11.694 1.00 25.69 ?  158 LYS   B HB2  1 
ATOM   6266 H HB3  . LYS   B 1 158 ? 49.170 -39.353 -10.681 1.00 25.69 ?  158 LYS   B HB3  1 
ATOM   6267 H HG2  . LYS   B 1 158 ? 48.577 -40.168 -12.737 1.00 28.44 ?  158 LYS   B HG2  1 
ATOM   6268 H HG3  . LYS   B 1 158 ? 47.334 -40.373 -11.775 1.00 28.44 ?  158 LYS   B HG3  1 
ATOM   6269 H HD2  . LYS   B 1 158 ? 46.299 -38.510 -12.712 1.00 31.20 ?  158 LYS   B HD2  1 
ATOM   6270 H HD3  . LYS   B 1 158 ? 47.567 -38.270 -13.646 1.00 31.20 ?  158 LYS   B HD3  1 
ATOM   6271 H HE2  . LYS   B 1 158 ? 47.121 -40.138 -14.861 1.00 33.04 ?  158 LYS   B HE2  1 
ATOM   6272 H HE3  . LYS   B 1 158 ? 46.030 -40.627 -13.814 1.00 33.04 ?  158 LYS   B HE3  1 
ATOM   6273 H HZ1  . LYS   B 1 158 ? 45.026 -39.729 -15.647 1.00 33.39 ?  158 LYS   B HZ1  1 
ATOM   6274 H HZ2  . LYS   B 1 158 ? 44.704 -38.904 -14.501 1.00 33.39 ?  158 LYS   B HZ2  1 
ATOM   6275 H HZ3  . LYS   B 1 158 ? 45.700 -38.461 -15.456 1.00 33.39 ?  158 LYS   B HZ3  1 
ATOM   6276 N N    . ASN   B 1 159 ? 46.874 -39.818 -8.656  1.00 19.37 ?  159 ASN   B N    1 
ATOM   6277 C CA   . ASN   B 1 159 ? 45.917 -40.800 -8.154  1.00 20.19 ?  159 ASN   B CA   1 
ATOM   6278 C C    . ASN   B 1 159 ? 44.718 -40.125 -7.484  1.00 18.98 ?  159 ASN   B C    1 
ATOM   6279 O O    . ASN   B 1 159 ? 43.585 -40.609 -7.600  1.00 19.30 ?  159 ASN   B O    1 
ATOM   6280 C CB   . ASN   B 1 159 ? 46.616 -41.787 -7.225  1.00 21.65 ?  159 ASN   B CB   1 
ATOM   6281 C CG   . ASN   B 1 159 ? 47.656 -42.622 -7.947  1.00 23.69 ?  159 ASN   B CG   1 
ATOM   6282 O OD1  . ASN   B 1 159 ? 47.411 -43.124 -9.052  1.00 24.44 ?  159 ASN   B OD1  1 
ATOM   6283 N ND2  . ASN   B 1 159 ? 48.824 -42.778 -7.329  1.00 24.25 ?  159 ASN   B ND2  1 
ATOM   6284 H H    . ASN   B 1 159 ? 47.622 -39.778 -8.236  1.00 23.22 ?  159 ASN   B H    1 
ATOM   6285 H HA   . ASN   B 1 159 ? 45.583 -41.301 -8.915  1.00 24.20 ?  159 ASN   B HA   1 
ATOM   6286 H HB2  . ASN   B 1 159 ? 47.061 -41.299 -6.518  1.00 25.96 ?  159 ASN   B HB2  1 
ATOM   6287 H HB3  . ASN   B 1 159 ? 45.957 -42.392 -6.858  1.00 25.96 ?  159 ASN   B HB3  1 
ATOM   6288 H HD21 . ASN   B 1 159 ? 49.451 -43.244 -7.697  1.00 29.08 ?  159 ASN   B HD21 1 
ATOM   6289 H HD22 . ASN   B 1 159 ? 48.954 -42.427 -6.554  1.00 29.08 ?  159 ASN   B HD22 1 
ATOM   6290 N N    . LEU   B 1 160 ? 44.933 -39.001 -6.794  1.00 18.16 ?  160 LEU   B N    1 
ATOM   6291 C CA   . LEU   B 1 160 ? 43.797 -38.265 -6.251  1.00 17.31 ?  160 LEU   B CA   1 
ATOM   6292 C C    . LEU   B 1 160 ? 43.009 -37.593 -7.364  1.00 16.34 ?  160 LEU   B C    1 
ATOM   6293 O O    . LEU   B 1 160 ? 41.770 -37.593 -7.346  1.00 15.66 ?  160 LEU   B O    1 
ATOM   6294 C CB   . LEU   B 1 160 ? 44.261 -37.237 -5.223  1.00 16.89 ?  160 LEU   B CB   1 
ATOM   6295 C CG   . LEU   B 1 160 ? 43.134 -36.336 -4.695  1.00 16.64 ?  160 LEU   B CG   1 
ATOM   6296 C CD1  . LEU   B 1 160 ? 42.009 -37.170 -4.090  1.00 17.35 ?  160 LEU   B CD1  1 
ATOM   6297 C CD2  . LEU   B 1 160 ? 43.670 -35.335 -3.680  1.00 16.57 ?  160 LEU   B CD2  1 
ATOM   6298 H H    . LEU   B 1 160 ? 45.705 -38.652 -6.638  1.00 21.77 ?  160 LEU   B H    1 
ATOM   6299 H HA   . LEU   B 1 160 ? 43.207 -38.891 -5.811  1.00 20.75 ?  160 LEU   B HA   1 
ATOM   6300 H HB2  . LEU   B 1 160 ? 44.652 -37.710 -4.470  1.00 20.25 ?  160 LEU   B HB2  1 
ATOM   6301 H HB3  . LEU   B 1 160 ? 44.936 -36.668 -5.634  1.00 20.25 ?  160 LEU   B HB3  1 
ATOM   6302 H HG   . LEU   B 1 160 ? 42.766 -35.834 -5.435  1.00 19.94 ?  160 LEU   B HG   1 
ATOM   6303 H HD11 . LEU   B 1 160 ? 41.385 -36.579 -3.647  1.00 20.80 ?  160 LEU   B HD11 1 
ATOM   6304 H HD12 . LEU   B 1 160 ? 41.556 -37.659 -4.798  1.00 20.80 ?  160 LEU   B HD12 1 
ATOM   6305 H HD13 . LEU   B 1 160 ? 42.385 -37.796 -3.449  1.00 20.80 ?  160 LEU   B HD13 1 
ATOM   6306 H HD21 . LEU   B 1 160 ? 42.939 -34.769 -3.388  1.00 19.86 ?  160 LEU   B HD21 1 
ATOM   6307 H HD22 . LEU   B 1 160 ? 44.038 -35.818 -2.924  1.00 19.86 ?  160 LEU   B HD22 1 
ATOM   6308 H HD23 . LEU   B 1 160 ? 44.359 -34.798 -4.100  1.00 19.86 ?  160 LEU   B HD23 1 
ATOM   6309 N N    . TYR   B 1 161 ? 43.711 -37.025 -8.349  1.00 16.45 ?  161 TYR   B N    1 
ATOM   6310 C CA   . TYR   B 1 161 ? 43.040 -36.457 -9.514  1.00 16.30 ?  161 TYR   B CA   1 
ATOM   6311 C C    . TYR   B 1 161 ? 42.094 -37.477 -10.139 1.00 16.17 ?  161 TYR   B C    1 
ATOM   6312 O O    . TYR   B 1 161 ? 40.923 -37.182 -10.398 1.00 15.83 ?  161 TYR   B O    1 
ATOM   6313 C CB   . TYR   B 1 161 ? 44.085 -35.973 -10.530 1.00 16.87 ?  161 TYR   B CB   1 
ATOM   6314 C CG   . TYR   B 1 161 ? 43.510 -35.505 -11.845 1.00 17.60 ?  161 TYR   B CG   1 
ATOM   6315 C CD1  . TYR   B 1 161 ? 43.113 -34.185 -12.013 1.00 17.73 ?  161 TYR   B CD1  1 
ATOM   6316 C CD2  . TYR   B 1 161 ? 43.337 -36.384 -12.908 1.00 18.17 ?  161 TYR   B CD2  1 
ATOM   6317 C CE1  . TYR   B 1 161 ? 42.580 -33.749 -13.200 1.00 18.85 ?  161 TYR   B CE1  1 
ATOM   6318 C CE2  . TYR   B 1 161 ? 42.796 -35.959 -14.099 1.00 19.33 ?  161 TYR   B CE2  1 
ATOM   6319 C CZ   . TYR   B 1 161 ? 42.421 -34.637 -14.240 1.00 19.30 ?  161 TYR   B CZ   1 
ATOM   6320 O OH   . TYR   B 1 161 ? 41.881 -34.199 -15.424 1.00 21.34 ?  161 TYR   B OH   1 
ATOM   6321 H H    . TYR   B 1 161 ? 44.567 -36.966 -8.374  1.00 19.71 ?  161 TYR   B H    1 
ATOM   6322 H HA   . TYR   B 1 161 ? 42.515 -35.690 -9.237  1.00 19.54 ?  161 TYR   B HA   1 
ATOM   6323 H HB2  . TYR   B 1 161 ? 44.571 -35.224 -10.146 1.00 20.22 ?  161 TYR   B HB2  1 
ATOM   6324 H HB3  . TYR   B 1 161 ? 44.696 -36.696 -10.724 1.00 20.22 ?  161 TYR   B HB3  1 
ATOM   6325 H HD1  . TYR   B 1 161 ? 43.221 -33.575 -11.317 1.00 21.26 ?  161 TYR   B HD1  1 
ATOM   6326 H HD2  . TYR   B 1 161 ? 43.583 -37.274 -12.815 1.00 21.78 ?  161 TYR   B HD2  1 
ATOM   6327 H HE1  . TYR   B 1 161 ? 42.325 -32.857 -13.300 1.00 22.59 ?  161 TYR   B HE1  1 
ATOM   6328 H HE2  . TYR   B 1 161 ? 42.684 -36.557 -14.805 1.00 23.18 ?  161 TYR   B HE2  1 
ATOM   6329 H HH   . TYR   B 1 161 ? 41.833 -34.838 -15.972 1.00 25.59 ?  161 TYR   B HH   1 
ATOM   6330 N N    . ASP   B 1 162 ? 42.588 -38.695 -10.366 1.00 16.74 ?  162 ASP   B N    1 
ATOM   6331 C CA   . ASP   B 1 162 ? 41.758 -39.729 -10.977 1.00 17.11 ?  162 ASP   B CA   1 
ATOM   6332 C C    . ASP   B 1 162 ? 40.553 -40.067 -10.106 1.00 16.48 ?  162 ASP   B C    1 
ATOM   6333 O O    . ASP   B 1 162 ? 39.448 -40.279 -10.620 1.00 16.79 ?  162 ASP   B O    1 
ATOM   6334 C CB   . ASP   B 1 162 ? 42.583 -40.993 -11.239 1.00 18.53 ?  162 ASP   B CB   1 
ATOM   6335 C CG   . ASP   B 1 162 ? 43.593 -40.821 -12.363 1.00 19.99 ?  162 ASP   B CG   1 
ATOM   6336 O OD1  . ASP   B 1 162 ? 43.465 -39.875 -13.164 1.00 20.07 ?  162 ASP   B OD1  1 
ATOM   6337 O OD2  . ASP   B 1 162 ? 44.503 -41.670 -12.464 1.00 22.30 -1 162 ASP   B OD2  1 
ATOM   6338 H H    . ASP   B 1 162 ? 43.389 -38.942 -10.184 1.00 20.06 ?  162 ASP   B H    1 
ATOM   6339 H HA   . ASP   B 1 162 ? 41.422 -39.407 -11.826 1.00 20.51 ?  162 ASP   B HA   1 
ATOM   6340 H HB2  . ASP   B 1 162 ? 43.067 -41.226 -10.434 1.00 22.21 ?  162 ASP   B HB2  1 
ATOM   6341 H HB3  . ASP   B 1 162 ? 41.982 -41.714 -11.487 1.00 22.21 ?  162 ASP   B HB3  1 
ATOM   6342 N N    . LYS   B 1 163 ? 40.746 -40.136 -8.787  1.00 16.06 ?  163 LYS   B N    1 
ATOM   6343 C CA   . LYS   B 1 163 ? 39.621 -40.412 -7.898  1.00 16.58 ?  163 LYS   B CA   1 
ATOM   6344 C C    . LYS   B 1 163 ? 38.578 -39.301 -7.967  1.00 15.45 ?  163 LYS   B C    1 
ATOM   6345 O O    . LYS   B 1 163 ? 37.368 -39.568 -7.979  1.00 16.37 ?  163 LYS   B O    1 
ATOM   6346 C CB   . LYS   B 1 163 ? 40.108 -40.596 -6.463  1.00 20.11 ?  163 LYS   B CB   1 
ATOM   6347 C CG   . LYS   B 1 163 ? 39.018 -41.084 -5.534  1.00 26.11 ?  163 LYS   B CG   1 
ATOM   6348 C CD   . LYS   B 1 163 ? 39.517 -41.351 -4.127  1.00 31.59 ?  163 LYS   B CD   1 
ATOM   6349 C CE   . LYS   B 1 163 ? 38.435 -42.045 -3.307  1.00 35.53 ?  163 LYS   B CE   1 
ATOM   6350 N NZ   . LYS   B 1 163 ? 38.441 -41.622 -1.880  1.00 37.94 ?  163 LYS   B NZ   1 
ATOM   6351 H H    . LYS   B 1 163 ? 41.505 -40.030 -8.390  1.00 19.24 ?  163 LYS   B H    1 
ATOM   6352 H HA   . LYS   B 1 163 ? 39.199 -41.237 -8.176  1.00 19.87 ?  163 LYS   B HA   1 
ATOM   6353 H HB2  . LYS   B 1 163 ? 40.825 -41.252 -6.450  1.00 24.11 ?  163 LYS   B HB2  1 
ATOM   6354 H HB3  . LYS   B 1 163 ? 40.430 -39.748 -6.122  1.00 24.11 ?  163 LYS   B HB3  1 
ATOM   6355 H HG2  . LYS   B 1 163 ? 38.321 -40.412 -5.480  1.00 31.31 ?  163 LYS   B HG2  1 
ATOM   6356 H HG3  . LYS   B 1 163 ? 38.652 -41.913 -5.885  1.00 31.31 ?  163 LYS   B HG3  1 
ATOM   6357 H HD2  . LYS   B 1 163 ? 40.294 -41.932 -4.163  1.00 37.88 ?  163 LYS   B HD2  1 
ATOM   6358 H HD3  . LYS   B 1 163 ? 39.739 -40.513 -3.696  1.00 37.88 ?  163 LYS   B HD3  1 
ATOM   6359 H HE2  . LYS   B 1 163 ? 37.566 -41.833 -3.683  1.00 42.61 ?  163 LYS   B HE2  1 
ATOM   6360 H HE3  . LYS   B 1 163 ? 38.582 -43.004 -3.336  1.00 42.61 ?  163 LYS   B HE3  1 
ATOM   6361 H HZ1  . LYS   B 1 163 ? 37.797 -42.046 -1.435  1.00 45.50 ?  163 LYS   B HZ1  1 
ATOM   6362 H HZ2  . LYS   B 1 163 ? 39.225 -41.816 -1.510  1.00 45.50 ?  163 LYS   B HZ2  1 
ATOM   6363 H HZ3  . LYS   B 1 163 ? 38.302 -40.745 -1.824  1.00 45.50 ?  163 LYS   B HZ3  1 
ATOM   6364 N N    . LEU   B 1 164 ? 39.032 -38.047 -8.013  1.00 14.62 ?  164 LEU   B N    1 
ATOM   6365 C CA   . LEU   B 1 164 ? 38.118 -36.911 -8.071  1.00 14.27 ?  164 LEU   B CA   1 
ATOM   6366 C C    . LEU   B 1 164 ? 37.335 -36.895 -9.379  1.00 14.47 ?  164 LEU   B C    1 
ATOM   6367 O O    . LEU   B 1 164 ? 36.112 -36.692 -9.381  1.00 15.39 ?  164 LEU   B O    1 
ATOM   6368 C CB   . LEU   B 1 164 ? 38.916 -35.617 -7.906  1.00 13.55 ?  164 LEU   B CB   1 
ATOM   6369 C CG   . LEU   B 1 164 ? 39.461 -35.349 -6.505  1.00 14.67 ?  164 LEU   B CG   1 
ATOM   6370 C CD1  . LEU   B 1 164 ? 40.543 -34.274 -6.559  1.00 14.83 ?  164 LEU   B CD1  1 
ATOM   6371 C CD2  . LEU   B 1 164 ? 38.351 -34.941 -5.553  1.00 16.54 ?  164 LEU   B CD2  1 
ATOM   6372 H H    . LEU   B 1 164 ? 39.870 -37.829 -8.011  1.00 17.52 ?  164 LEU   B H    1 
ATOM   6373 H HA   . LEU   B 1 164 ? 37.489 -36.971 -7.343  1.00 17.10 ?  164 LEU   B HA   1 
ATOM   6374 H HB2  . LEU   B 1 164 ? 39.681 -35.645 -8.511  1.00 16.24 ?  164 LEU   B HB2  1 
ATOM   6375 H HB3  . LEU   B 1 164 ? 38.350 -34.871 -8.143  1.00 16.24 ?  164 LEU   B HB3  1 
ATOM   6376 H HG   . LEU   B 1 164 ? 39.872 -36.157 -6.167  1.00 17.58 ?  164 LEU   B HG   1 
ATOM   6377 H HD11 . LEU   B 1 164 ? 40.876 -34.107 -5.662  1.00 17.78 ?  164 LEU   B HD11 1 
ATOM   6378 H HD12 . LEU   B 1 164 ? 41.275 -34.581 -7.125  1.00 17.78 ?  164 LEU   B HD12 1 
ATOM   6379 H HD13 . LEU   B 1 164 ? 40.170 -33.457 -6.928  1.00 17.78 ?  164 LEU   B HD13 1 
ATOM   6380 H HD21 . LEU   B 1 164 ? 38.737 -34.715 -4.693  1.00 19.82 ?  164 LEU   B HD21 1 
ATOM   6381 H HD22 . LEU   B 1 164 ? 37.881 -34.178 -5.918  1.00 19.82 ?  164 LEU   B HD22 1 
ATOM   6382 H HD23 . LEU   B 1 164 ? 37.738 -35.689 -5.452  1.00 19.82 ?  164 LEU   B HD23 1 
ATOM   6383 N N    . VAL   B 1 165 ? 38.025 -37.071 -10.508 1.00 16.20 ?  165 VAL   B N    1 
ATOM   6384 C CA   . VAL   B 1 165 ? 37.363 -37.001 -11.807 1.00 17.22 ?  165 VAL   B CA   1 
ATOM   6385 C C    . VAL   B 1 165 ? 36.437 -38.194 -11.989 1.00 18.93 ?  165 VAL   B C    1 
ATOM   6386 O O    . VAL   B 1 165 ? 35.278 -38.051 -12.400 1.00 20.46 ?  165 VAL   B O    1 
ATOM   6387 C CB   . VAL   B 1 165 ? 38.401 -36.918 -12.941 1.00 18.27 ?  165 VAL   B CB   1 
ATOM   6388 C CG1  . VAL   B 1 165 ? 37.722 -37.008 -14.289 1.00 19.88 ?  165 VAL   B CG1  1 
ATOM   6389 C CG2  . VAL   B 1 165 ? 39.202 -35.634 -12.835 1.00 18.23 ?  165 VAL   B CG2  1 
ATOM   6390 H H    . VAL   B 1 165 ? 38.878 -37.217 -10.549 1.00 19.42 ?  165 VAL   B H    1 
ATOM   6391 H HA   . VAL   B 1 165 ? 36.826 -36.199 -11.843 1.00 20.64 ?  165 VAL   B HA   1 
ATOM   6392 H HB   . VAL   B 1 165 ? 39.024 -37.657 -12.864 1.00 21.90 ?  165 VAL   B HB   1 
ATOM   6393 H HG11 . VAL   B 1 165 ? 38.337 -36.707 -14.973 1.00 23.83 ?  165 VAL   B HG11 1 
ATOM   6394 H HG12 . VAL   B 1 165 ? 37.477 -37.932 -14.452 1.00 23.83 ?  165 VAL   B HG12 1 
ATOM   6395 H HG13 . VAL   B 1 165 ? 36.932 -36.450 -14.281 1.00 23.83 ?  165 VAL   B HG13 1 
ATOM   6396 H HG21 . VAL   B 1 165 ? 39.832 -35.585 -13.575 1.00 21.85 ?  165 VAL   B HG21 1 
ATOM   6397 H HG22 . VAL   B 1 165 ? 38.595 -34.874 -12.874 1.00 21.85 ?  165 VAL   B HG22 1 
ATOM   6398 H HG23 . VAL   B 1 165 ? 39.685 -35.623 -11.993 1.00 21.85 ?  165 VAL   B HG23 1 
ATOM   6399 N N    . SER   B 1 166 ? 36.946 -39.394 -11.690 1.00 19.68 ?  166 SER   B N    1 
ATOM   6400 C CA   . SER   B 1 166 ? 36.192 -40.608 -11.965 1.00 21.17 ?  166 SER   B CA   1 
ATOM   6401 C C    . SER   B 1 166 ? 34.937 -40.695 -11.113 1.00 21.34 ?  166 SER   B C    1 
ATOM   6402 O O    . SER   B 1 166 ? 33.968 -41.325 -11.532 1.00 22.81 ?  166 SER   B O    1 
ATOM   6403 C CB   . SER   B 1 166 ? 37.060 -41.862 -11.789 1.00 22.19 ?  166 SER   B CB   1 
ATOM   6404 O OG   . SER   B 1 166 ? 37.427 -42.059 -10.433 1.00 22.22 ?  166 SER   B OG   1 
ATOM   6405 H H    . SER   B 1 166 ? 37.730 -39.529 -11.344 1.00 23.59 ?  166 SER   B H    1 
ATOM   6406 H HA   . SER   B 1 166 ? 35.918 -40.592 -12.894 1.00 25.38 ?  166 SER   B HA   1 
ATOM   6407 H HB2  . SER   B 1 166 ? 36.559 -42.636 -12.091 1.00 26.61 ?  166 SER   B HB2  1 
ATOM   6408 H HB3  . SER   B 1 166 ? 37.864 -41.767 -12.331 1.00 26.61 ?  166 SER   B HB3  1 
ATOM   6409 H HG   . SER   B 1 166 ? 37.893 -41.411 -10.167 1.00 26.64 ?  166 SER   B HG   1 
ATOM   6410 N N    . SER   B 1 167 ? 34.920 -40.084 -9.932  1.00 19.72 ?  167 SER   B N    1 
ATOM   6411 C CA   . SER   B 1 167 ? 33.765 -40.137 -9.044  1.00 19.76 ?  167 SER   B CA   1 
ATOM   6412 C C    . SER   B 1 167 ? 32.856 -38.911 -9.142  1.00 19.57 ?  167 SER   B C    1 
ATOM   6413 O O    . SER   B 1 167 ? 31.783 -38.904 -8.529  1.00 19.72 ?  167 SER   B O    1 
ATOM   6414 C CB   . SER   B 1 167 ? 34.216 -40.319 -7.590  1.00 19.69 ?  167 SER   B CB   1 
ATOM   6415 O OG   . SER   B 1 167 ? 34.891 -39.160 -7.122  1.00 19.51 ?  167 SER   B OG   1 
ATOM   6416 H H    . SER   B 1 167 ? 35.576 -39.634 -9.622  1.00 23.65 ?  167 SER   B H    1 
ATOM   6417 H HA   . SER   B 1 167 ? 33.231 -40.912 -9.281  1.00 23.69 ?  167 SER   B HA   1 
ATOM   6418 H HB2  . SER   B 1 167 ? 33.434 -40.478 -7.037  1.00 23.60 ?  167 SER   B HB2  1 
ATOM   6419 H HB3  . SER   B 1 167 ? 34.812 -41.088 -7.541  1.00 23.60 ?  167 SER   B HB3  1 
ATOM   6420 H HG   . SER   B 1 167 ? 35.577 -39.028 -7.591  1.00 23.39 ?  167 SER   B HG   1 
ATOM   6421 N N    . PHE   B 1 168 ? 33.241 -37.879 -9.895  1.00 19.16 ?  168 PHE   B N    1 
ATOM   6422 C CA   . PHE   B 1 168 ? 32.410 -36.677 -9.970  1.00 18.40 ?  168 PHE   B CA   1 
ATOM   6423 C C    . PHE   B 1 168 ? 31.099 -36.941 -10.706 1.00 16.43 ?  168 PHE   B C    1 
ATOM   6424 O O    . PHE   B 1 168 ? 30.058 -36.346 -10.372 1.00 17.18 ?  168 PHE   B O    1 
ATOM   6425 C CB   . PHE   B 1 168 ? 33.173 -35.542 -10.653 1.00 19.32 ?  168 PHE   B CB   1 
ATOM   6426 C CG   . PHE   B 1 168 ? 32.367 -34.295 -10.795 1.00 19.41 ?  168 PHE   B CG   1 
ATOM   6427 C CD1  . PHE   B 1 168 ? 32.026 -33.556 -9.674  1.00 20.67 ?  168 PHE   B CD1  1 
ATOM   6428 C CD2  . PHE   B 1 168 ? 31.925 -33.869 -12.034 1.00 18.62 ?  168 PHE   B CD2  1 
ATOM   6429 C CE1  . PHE   B 1 168 ? 31.260 -32.411 -9.781  1.00 20.91 ?  168 PHE   B CE1  1 
ATOM   6430 C CE2  . PHE   B 1 168 ? 31.167 -32.713 -12.156 1.00 19.87 ?  168 PHE   B CE2  1 
ATOM   6431 C CZ   . PHE   B 1 168 ? 30.837 -31.977 -11.024 1.00 20.16 ?  168 PHE   B CZ   1 
ATOM   6432 H H    . PHE   B 1 168 ? 33.967 -37.848 -10.356 1.00 22.96 ?  168 PHE   B H    1 
ATOM   6433 H HA   . PHE   B 1 168 ? 32.192 -36.388 -9.074  1.00 22.05 ?  168 PHE   B HA   1 
ATOM   6434 H HB2  . PHE   B 1 168 ? 33.957 -35.328 -10.124 1.00 23.16 ?  168 PHE   B HB2  1 
ATOM   6435 H HB3  . PHE   B 1 168 ? 33.437 -35.826 -11.540 1.00 23.16 ?  168 PHE   B HB3  1 
ATOM   6436 H HD1  . PHE   B 1 168 ? 32.308 -33.845 -8.837  1.00 24.78 ?  168 PHE   B HD1  1 
ATOM   6437 H HD2  . PHE   B 1 168 ? 32.148 -34.353 -12.795 1.00 22.32 ?  168 PHE   B HD2  1 
ATOM   6438 H HE1  . PHE   B 1 168 ? 31.041 -31.926 -9.019  1.00 25.07 ?  168 PHE   B HE1  1 
ATOM   6439 H HE2  . PHE   B 1 168 ? 30.876 -32.429 -12.995 1.00 23.83 ?  168 PHE   B HE2  1 
ATOM   6440 H HZ   . PHE   B 1 168 ? 30.318 -31.208 -11.104 1.00 24.17 ?  168 PHE   B HZ   1 
ATOM   6441 N N    . LEU   B 1 169 ? 31.140 -37.807 -11.715 1.00 16.67 ?  169 LEU   B N    1 
ATOM   6442 C CA   . LEU   B 1 169 ? 29.962 -38.127 -12.513 1.00 18.70 ?  169 LEU   B CA   1 
ATOM   6443 C C    . LEU   B 1 169 ? 29.943 -39.570 -12.996 1.00 21.75 ?  169 LEU   B C    1 
ATOM   6444 O O    . LEU   B 1 169 ? 29.044 -39.979 -13.735 1.00 24.64 ?  169 LEU   B O    1 
ATOM   6445 C CB   . LEU   B 1 169 ? 29.886 -37.207 -13.729 1.00 20.52 ?  169 LEU   B CB   1 
ATOM   6446 C CG   . LEU   B 1 169 ? 28.631 -36.344 -13.846 1.00 23.69 ?  169 LEU   B CG   1 
ATOM   6447 C CD1  . LEU   B 1 169 ? 28.578 -35.721 -15.221 1.00 24.40 ?  169 LEU   B CD1  1 
ATOM   6448 C CD2  . LEU   B 1 169 ? 27.366 -37.137 -13.570 1.00 23.97 ?  169 LEU   B CD2  1 
ATOM   6449 O OXT  . LEU   B 1 169 ? 30.832 -40.352 -12.680 1.00 22.50 -1 169 LEU   B OXT  1 
ATOM   6450 H H    . LEU   B 1 169 ? 31.852 -38.217 -11.972 1.00 19.99 ?  169 LEU   B H    1 
ATOM   6451 H HA   . LEU   B 1 169 ? 29.178 -37.980 -11.969 1.00 22.42 ?  169 LEU   B HA   1 
ATOM   6452 H HB2  . LEU   B 1 169 ? 30.646 -36.604 -13.710 1.00 24.60 ?  169 LEU   B HB2  1 
ATOM   6453 H HB3  . LEU   B 1 169 ? 29.929 -37.751 -14.532 1.00 24.60 ?  169 LEU   B HB3  1 
ATOM   6454 H HG   . LEU   B 1 169 ? 28.680 -35.624 -13.196 1.00 28.40 ?  169 LEU   B HG   1 
ATOM   6455 H HD11 . LEU   B 1 169 ? 27.798 -35.147 -15.277 1.00 29.26 ?  169 LEU   B HD11 1 
ATOM   6456 H HD12 . LEU   B 1 169 ? 29.384 -35.200 -15.360 1.00 29.26 ?  169 LEU   B HD12 1 
ATOM   6457 H HD13 . LEU   B 1 169 ? 28.520 -36.427 -15.882 1.00 29.26 ?  169 LEU   B HD13 1 
ATOM   6458 H HD21 . LEU   B 1 169 ? 26.616 -36.699 -13.997 1.00 28.74 ?  169 LEU   B HD21 1 
ATOM   6459 H HD22 . LEU   B 1 169 ? 27.474 -38.034 -13.929 1.00 28.74 ?  169 LEU   B HD22 1 
ATOM   6460 H HD23 . LEU   B 1 169 ? 27.224 -37.181 -12.612 1.00 28.74 ?  169 LEU   B HD23 1 
HETATM 6461 C C1   T TFA   C 2 .   ? 12.097 -1.287  1.470   0.20 11.59 ?  201 TFA   A C1   1 
HETATM 6462 C C2   T TFA   C 2 .   ? 12.752 -1.751  0.141   0.20 13.16 ?  201 TFA   A C2   1 
HETATM 6463 O O    T TFA   C 2 .   ? 12.813 -1.512  2.456   0.20 10.50 ?  201 TFA   A O    1 
HETATM 6464 F F1   T TFA   C 2 .   ? 12.804 -3.093  0.093   0.20 13.66 ?  201 TFA   A F1   1 
HETATM 6465 F F2   T TFA   C 2 .   ? 12.069 -1.353  -0.943  0.20 13.08 ?  201 TFA   A F2   1 
HETATM 6466 F F3   T TFA   C 2 .   ? 14.007 -1.320  -0.026  0.20 14.64 ?  201 TFA   A F3   1 
HETATM 6467 O OXT  T TFA   C 2 .   ? 10.981 -0.762  1.373   0.20 12.28 ?  201 TFA   A OXT  1 
HETATM 6468 N N2   B A1A8K D 3 .   ? 14.587 -0.021  4.362   0.32 15.84 ?  202 A1A8K A N2   1 
HETATM 6469 C C3   B A1A8K D 3 .   ? 14.055 -0.697  0.545   0.32 22.74 ?  202 A1A8K A C3   1 
HETATM 6470 C C6   B A1A8K D 3 .   ? 14.681 1.116   3.623   0.32 16.67 ?  202 A1A8K A C6   1 
HETATM 6471 C C9   B A1A8K D 3 .   ? 14.990 2.328   4.306   0.32 14.74 ?  202 A1A8K A C9   1 
HETATM 6472 C C1   B A1A8K D 3 .   ? 12.121 0.282   1.888   0.32 23.60 ?  202 A1A8K A C1   1 
HETATM 6473 C C10  B A1A8K D 3 .   ? 15.188 3.720   3.994   0.32 14.49 ?  202 A1A8K A C10  1 
HETATM 6474 C C11  B A1A8K D 3 .   ? 15.475 4.362   5.173   0.32 14.07 ?  202 A1A8K A C11  1 
HETATM 6475 C C2   B A1A8K D 3 .   ? 13.596 -0.139  1.898   0.32 22.20 ?  202 A1A8K A C2   1 
HETATM 6476 C C4   B A1A8K D 3 .   ? 15.145 0.250   0.057   0.32 22.92 ?  202 A1A8K A C4   1 
HETATM 6477 C C5   B A1A8K D 3 .   ? 15.594 0.991   1.319   0.32 21.79 ?  202 A1A8K A C5   1 
HETATM 6478 C C7   B A1A8K D 3 .   ? 14.771 -0.003  5.671   0.32 14.88 ?  202 A1A8K A C7   1 
HETATM 6479 C C8   B A1A8K D 3 .   ? 15.158 2.187   5.708   0.32 14.01 ?  202 A1A8K A C8   1 
HETATM 6480 N N1   B A1A8K D 3 .   ? 14.457 1.004   2.234   0.32 20.22 ?  202 A1A8K A N1   1 
HETATM 6481 N N3   B A1A8K D 3 .   ? 15.059 1.042   6.428   0.32 14.38 ?  202 A1A8K A N3   1 
HETATM 6482 N N4   B A1A8K D 3 .   ? 15.456 3.436   6.202   0.32 13.92 ?  202 A1A8K A N4   1 
HETATM 6483 O O1   B A1A8K D 3 .   ? 11.440 -0.054  2.880   0.32 23.81 ?  202 A1A8K A O1   1 
HETATM 6484 O O2   B A1A8K D 3 .   ? 16.208 -0.406  -0.600  0.32 24.09 ?  202 A1A8K A O2   1 
HETATM 6485 O O3   B A1A8K D 3 .   ? 11.696 0.938   0.910   0.32 24.49 ?  202 A1A8K A O3   1 
HETATM 6486 H H3   B A1A8K D 3 .   ? 14.473 -1.685  0.716   0.32 27.26 ?  202 A1A8K A H3   1 
HETATM 6487 H H4   B A1A8K D 3 .   ? 13.238 -0.803  -0.166  0.32 27.26 ?  202 A1A8K A H4   1 
HETATM 6488 H H9   B A1A8K D 3 .   ? 15.126 4.160   3.012   0.32 17.36 ?  202 A1A8K A H9   1 
HETATM 6489 H H10  B A1A8K D 3 .   ? 15.681 5.403   5.364   0.32 16.86 ?  202 A1A8K A H10  1 
HETATM 6490 H H1   B A1A8K D 3 .   ? 13.726 -0.964  2.602   0.32 26.62 ?  202 A1A8K A H1   1 
HETATM 6491 H H2   B A1A8K D 3 .   ? 14.710 0.922   -0.658  0.32 27.48 ?  202 A1A8K A H2   1 
HETATM 6492 H H6   B A1A8K D 3 .   ? 15.927 2.004   1.065   0.32 26.13 ?  202 A1A8K A H6   1 
HETATM 6493 H H7   B A1A8K D 3 .   ? 16.425 0.468   1.776   0.32 26.13 ?  202 A1A8K A H7   1 
HETATM 6494 H H8   B A1A8K D 3 .   ? 14.666 -0.952  6.175   0.32 17.84 ?  202 A1A8K A H8   1 
HETATM 6495 H H11  B A1A8K D 3 .   ? 15.632 3.677   7.169   0.32 16.68 ?  202 A1A8K A H11  1 
HETATM 6496 H H5   B A1A8K D 3 .   ? 16.341 0.039   -1.427  0.32 28.88 ?  202 A1A8K A H5   1 
HETATM 6497 O O    . HOH   E 4 .   ? 17.384 -1.789  0.428   1.00 23.59 ?  301 HOH   A O    1 
HETATM 6498 O O    . HOH   E 4 .   ? 14.744 -4.750  20.518  1.00 43.60 ?  302 HOH   A O    1 
HETATM 6499 O O    . HOH   E 4 .   ? 12.090 0.277   14.840  1.00 34.44 ?  303 HOH   A O    1 
HETATM 6500 O O    A HOH   E 4 .   ? 4.689  3.906   0.614   0.68 23.65 ?  304 HOH   A O    1 
HETATM 6501 O O    . HOH   E 4 .   ? 34.390 -1.856  12.510  1.00 39.85 ?  305 HOH   A O    1 
HETATM 6502 O O    . HOH   E 4 .   ? 15.197 -12.263 18.711  1.00 38.11 ?  306 HOH   A O    1 
HETATM 6503 O O    . HOH   E 4 .   ? 9.235  -10.244 19.479  1.00 43.13 ?  307 HOH   A O    1 
HETATM 6504 O O    . HOH   E 4 .   ? 7.616  -6.293  -6.592  1.00 39.63 ?  308 HOH   A O    1 
HETATM 6505 O O    . HOH   E 4 .   ? 11.634 -10.859 -10.102 1.00 42.16 ?  309 HOH   A O    1 
HETATM 6506 O O    . HOH   E 4 .   ? 6.939  -8.105  11.828  1.00 22.95 ?  310 HOH   A O    1 
HETATM 6507 O O    . HOH   E 4 .   ? -0.649 -8.573  2.053   1.00 43.83 ?  311 HOH   A O    1 
HETATM 6508 O O    . HOH   E 4 .   ? 26.836 11.409  1.678   1.00 17.27 ?  312 HOH   A O    1 
HETATM 6509 O O    . HOH   E 4 .   ? 8.782  -12.062 17.191  1.00 42.19 ?  313 HOH   A O    1 
HETATM 6510 O O    . HOH   E 4 .   ? 7.977  -21.500 3.958   1.00 48.72 ?  314 HOH   A O    1 
HETATM 6511 O O    . HOH   E 4 .   ? 15.014 3.824   17.730  1.00 39.87 ?  315 HOH   A O    1 
HETATM 6512 O O    B HOH   E 4 .   ? 10.590 -0.266  -1.072  0.32 24.05 ?  316 HOH   A O    1 
HETATM 6513 O O    . HOH   E 4 .   ? 15.194 -21.569 14.232  1.00 20.16 ?  317 HOH   A O    1 
HETATM 6514 O O    . HOH   E 4 .   ? 18.602 -2.360  -16.403 1.00 45.62 ?  318 HOH   A O    1 
HETATM 6515 O O    . HOH   E 4 .   ? 42.412 10.546  5.206   1.00 19.61 ?  319 HOH   A O    1 
HETATM 6516 O O    . HOH   E 4 .   ? 36.124 -5.062  -0.520  1.00 30.75 ?  320 HOH   A O    1 
HETATM 6517 O O    . HOH   E 4 .   ? 0.713  -4.542  0.107   1.00 32.61 ?  321 HOH   A O    1 
HETATM 6518 O O    . HOH   E 4 .   ? 30.241 -13.317 -8.568  1.00 21.46 ?  322 HOH   A O    1 
HETATM 6519 O O    . HOH   E 4 .   ? 28.945 0.501   -9.678  1.00 20.71 ?  323 HOH   A O    1 
HETATM 6520 O O    . HOH   E 4 .   ? 14.707 -13.947 16.750  1.00 26.76 ?  324 HOH   A O    1 
HETATM 6521 O O    . HOH   E 4 .   ? 28.128 -6.352  19.670  1.00 39.12 ?  325 HOH   A O    1 
HETATM 6522 O O    . HOH   E 4 .   ? 14.162 -4.565  -11.850 1.00 28.96 ?  326 HOH   A O    1 
HETATM 6523 O O    A HOH   E 4 .   ? 14.631 -3.666  3.094   0.68 15.48 ?  327 HOH   A O    1 
HETATM 6524 O O    . HOH   E 4 .   ? 33.982 -1.014  -8.893  1.00 27.00 ?  328 HOH   A O    1 
HETATM 6525 O O    . HOH   E 4 .   ? 19.909 -12.499 -8.946  1.00 25.34 ?  329 HOH   A O    1 
HETATM 6526 O O    . HOH   E 4 .   ? 9.841  -21.380 5.672   1.00 20.58 ?  330 HOH   A O    1 
HETATM 6527 O O    . HOH   E 4 .   ? 38.250 10.112  7.190   1.00 36.96 ?  331 HOH   A O    1 
HETATM 6528 O O    . HOH   E 4 .   ? 18.938 -21.975 6.943   1.00 35.25 ?  332 HOH   A O    1 
HETATM 6529 O O    . HOH   E 4 .   ? 26.502 -19.345 -1.799  1.00 14.49 ?  333 HOH   A O    1 
HETATM 6530 O O    . HOH   E 4 .   ? 31.022 -18.137 7.791   1.00 19.84 ?  334 HOH   A O    1 
HETATM 6531 O O    . HOH   E 4 .   ? 6.435  -5.579  11.162  1.00 23.37 ?  335 HOH   A O    1 
HETATM 6532 O O    . HOH   E 4 .   ? 37.530 2.763   10.211  1.00 28.06 ?  336 HOH   A O    1 
HETATM 6533 O O    . HOH   E 4 .   ? 20.648 -19.754 -5.090  1.00 27.98 ?  337 HOH   A O    1 
HETATM 6534 O O    . HOH   E 4 .   ? 27.367 13.799  2.896   1.00 29.49 ?  338 HOH   A O    1 
HETATM 6535 O O    . HOH   E 4 .   ? 18.703 -19.436 13.541  1.00 41.18 ?  339 HOH   A O    1 
HETATM 6536 O O    . HOH   E 4 .   ? 6.694  -3.392  12.940  1.00 33.09 ?  340 HOH   A O    1 
HETATM 6537 O O    . HOH   E 4 .   ? 28.396 -0.195  -13.371 1.00 30.79 ?  341 HOH   A O    1 
HETATM 6538 O O    . HOH   E 4 .   ? 44.317 7.159   6.444   1.00 26.94 ?  342 HOH   A O    1 
HETATM 6539 O O    . HOH   E 4 .   ? 22.314 5.325   18.989  1.00 39.95 ?  343 HOH   A O    1 
HETATM 6540 O O    A HOH   E 4 .   ? 14.266 0.556   6.802   0.68 25.09 ?  344 HOH   A O    1 
HETATM 6541 O O    . HOH   E 4 .   ? 22.723 12.494  1.649   1.00 16.44 ?  345 HOH   A O    1 
HETATM 6542 O O    . HOH   E 4 .   ? 38.552 4.966   7.011   1.00 15.90 ?  346 HOH   A O    1 
HETATM 6543 O O    A HOH   E 4 .   ? 17.099 -18.127 15.043  0.68 23.67 ?  347 HOH   A O    1 
HETATM 6544 O O    . HOH   E 4 .   ? -0.440 -2.965  2.973   1.00 40.05 ?  348 HOH   A O    1 
HETATM 6545 O O    . HOH   E 4 .   ? 10.407 -22.210 -1.244  1.00 47.54 ?  349 HOH   A O    1 
HETATM 6546 O O    . HOH   E 4 .   ? 39.752 -1.008  -5.168  1.00 20.20 ?  350 HOH   A O    1 
HETATM 6547 O O    . HOH   E 4 .   ? 22.223 -19.329 11.350  1.00 34.47 ?  351 HOH   A O    1 
HETATM 6548 O O    . HOH   E 4 .   ? 13.271 -1.441  -6.657  1.00 16.79 ?  352 HOH   A O    1 
HETATM 6549 O O    . HOH   E 4 .   ? 17.172 -17.807 -5.077  1.00 27.43 ?  353 HOH   A O    1 
HETATM 6550 O O    . HOH   E 4 .   ? 24.023 -2.123  -2.069  1.00 11.17 ?  354 HOH   A O    1 
HETATM 6551 O O    . HOH   E 4 .   ? 42.554 4.293   5.414   1.00 31.43 ?  355 HOH   A O    1 
HETATM 6552 O O    . HOH   E 4 .   ? 35.774 -12.684 6.828   1.00 15.91 ?  356 HOH   A O    1 
HETATM 6553 O O    . HOH   E 4 .   ? 31.089 -13.949 -2.492  1.00 14.15 ?  357 HOH   A O    1 
HETATM 6554 O O    . HOH   E 4 .   ? 14.415 -24.671 11.614  1.00 40.34 ?  358 HOH   A O    1 
HETATM 6555 O O    . HOH   E 4 .   ? 21.266 -2.346  -2.278  1.00 16.36 ?  359 HOH   A O    1 
HETATM 6556 O O    . HOH   E 4 .   ? 13.552 -15.227 -7.547  1.00 27.50 ?  360 HOH   A O    1 
HETATM 6557 O O    . HOH   E 4 .   ? 14.367 -21.202 -4.351  1.00 30.15 ?  361 HOH   A O    1 
HETATM 6558 O O    . HOH   E 4 .   ? 31.673 8.172   14.904  1.00 23.90 ?  362 HOH   A O    1 
HETATM 6559 O O    . HOH   E 4 .   ? 3.530  -9.330  9.799   1.00 32.50 ?  363 HOH   A O    1 
HETATM 6560 O O    . HOH   E 4 .   ? 37.284 11.961  4.975   1.00 30.62 ?  364 HOH   A O    1 
HETATM 6561 O O    . HOH   E 4 .   ? 37.202 -2.855  9.739   1.00 41.64 ?  365 HOH   A O    1 
HETATM 6562 O O    . HOH   E 4 .   ? 30.799 3.070   8.294   1.00 12.55 ?  366 HOH   A O    1 
HETATM 6563 O O    . HOH   E 4 .   ? 13.973 -5.049  17.503  1.00 25.08 ?  367 HOH   A O    1 
HETATM 6564 O O    . HOH   E 4 .   ? 21.831 -21.903 8.359   1.00 28.63 ?  368 HOH   A O    1 
HETATM 6565 O O    . HOH   E 4 .   ? 18.564 9.461   9.012   1.00 22.95 ?  369 HOH   A O    1 
HETATM 6566 O O    . HOH   E 4 .   ? 43.334 7.826   2.745   1.00 26.48 ?  370 HOH   A O    1 
HETATM 6567 O O    . HOH   E 4 .   ? 43.951 8.472   -3.031  1.00 26.64 ?  371 HOH   A O    1 
HETATM 6568 O O    . HOH   E 4 .   ? 33.642 -7.160  4.306   1.00 16.58 ?  372 HOH   A O    1 
HETATM 6569 O O    . HOH   E 4 .   ? 24.728 -17.521 12.729  1.00 24.84 ?  373 HOH   A O    1 
HETATM 6570 O O    . HOH   E 4 .   ? 22.627 -11.949 21.868  1.00 44.29 ?  374 HOH   A O    1 
HETATM 6571 O O    . HOH   E 4 .   ? 20.110 4.512   -7.631  1.00 20.54 ?  375 HOH   A O    1 
HETATM 6572 O O    . HOH   E 4 .   ? 31.823 -9.362  -6.648  1.00 22.58 ?  376 HOH   A O    1 
HETATM 6573 O O    . HOH   E 4 .   ? 27.485 -10.622 14.050  1.00 17.91 ?  377 HOH   A O    1 
HETATM 6574 O O    A HOH   E 4 .   ? 11.063 -0.391  1.931   0.48 28.65 ?  378 HOH   A O    1 
HETATM 6575 O O    . HOH   E 4 .   ? 15.462 11.900  7.909   1.00 40.20 ?  379 HOH   A O    1 
HETATM 6576 O O    . HOH   E 4 .   ? 17.029 -19.338 4.868   1.00 16.09 ?  380 HOH   A O    1 
HETATM 6577 O O    . HOH   E 4 .   ? 31.812 -7.267  -9.826  1.00 21.65 ?  381 HOH   A O    1 
HETATM 6578 O O    . HOH   E 4 .   ? 25.703 -0.801  -7.350  1.00 15.68 ?  382 HOH   A O    1 
HETATM 6579 O O    . HOH   E 4 .   ? 24.374 3.594   -1.769  1.00 16.93 ?  383 HOH   A O    1 
HETATM 6580 O O    T HOH   E 4 .   ? 15.402 -0.432  2.388   0.20 11.91 ?  384 HOH   A O    1 
HETATM 6581 O O    . HOH   E 4 .   ? 27.373 -6.048  -13.959 1.00 35.33 ?  385 HOH   A O    1 
HETATM 6582 O O    . HOH   E 4 .   ? 18.849 -0.689  -1.627  1.00 15.87 ?  386 HOH   A O    1 
HETATM 6583 O O    . HOH   E 4 .   ? 33.504 -17.003 8.040   1.00 18.92 ?  387 HOH   A O    1 
HETATM 6584 O O    . HOH   E 4 .   ? 14.050 -23.064 7.422   1.00 19.47 ?  388 HOH   A O    1 
HETATM 6585 O O    . HOH   E 4 .   ? 24.241 -7.803  14.442  1.00 17.38 ?  389 HOH   A O    1 
HETATM 6586 O O    B HOH   E 4 .   ? 14.823 -2.942  3.455   0.32 18.69 ?  390 HOH   A O    1 
HETATM 6587 O O    . HOH   E 4 .   ? 16.484 -22.070 0.978   1.00 29.43 ?  391 HOH   A O    1 
HETATM 6588 O O    . HOH   E 4 .   ? 21.207 10.283  15.092  1.00 33.42 ?  392 HOH   A O    1 
HETATM 6589 O O    . HOH   E 4 .   ? 27.927 0.828   -7.114  1.00 13.75 ?  393 HOH   A O    1 
HETATM 6590 O O    . HOH   E 4 .   ? 30.079 -10.146 12.965  1.00 21.71 ?  394 HOH   A O    1 
HETATM 6591 O O    . HOH   E 4 .   ? 37.537 -2.043  5.812   1.00 28.35 ?  395 HOH   A O    1 
HETATM 6592 O O    . HOH   E 4 .   ? 11.702 -10.823 17.061  1.00 26.93 ?  396 HOH   A O    1 
HETATM 6593 O O    . HOH   E 4 .   ? 23.451 11.363  4.134   1.00 13.28 ?  397 HOH   A O    1 
HETATM 6594 O O    A HOH   E 4 .   ? 15.793 -0.960  5.272   0.68 21.63 ?  398 HOH   A O    1 
HETATM 6595 O O    . HOH   E 4 .   ? 14.538 -0.528  -12.162 1.00 26.97 ?  399 HOH   A O    1 
HETATM 6596 O O    . HOH   E 4 .   ? 21.286 3.081   -0.247  1.00 14.10 ?  400 HOH   A O    1 
HETATM 6597 O O    . HOH   E 4 .   ? 30.697 1.836   16.710  1.00 21.74 ?  401 HOH   A O    1 
HETATM 6598 O O    . HOH   E 4 .   ? 32.786 -9.262  5.950   1.00 20.06 ?  402 HOH   A O    1 
HETATM 6599 O O    . HOH   E 4 .   ? 26.905 4.175   -0.633  1.00 13.15 ?  403 HOH   A O    1 
HETATM 6600 O O    . HOH   E 4 .   ? 24.548 1.985   -6.985  1.00 19.21 ?  404 HOH   A O    1 
HETATM 6601 O O    A HOH   E 4 .   ? 7.998  -12.605 -0.903  0.68 18.46 ?  405 HOH   A O    1 
HETATM 6602 O O    . HOH   E 4 .   ? 28.632 -10.693 -14.049 1.00 40.94 ?  406 HOH   A O    1 
HETATM 6603 O O    . HOH   E 4 .   ? 20.560 -20.047 2.741   1.00 18.59 ?  407 HOH   A O    1 
HETATM 6604 O O    . HOH   E 4 .   ? 15.155 -8.101  -9.708  1.00 23.18 ?  408 HOH   A O    1 
HETATM 6605 O O    . HOH   E 4 .   ? 15.991 6.946   2.971   1.00 18.11 ?  409 HOH   A O    1 
HETATM 6606 O O    . HOH   E 4 .   ? 24.005 3.911   -4.809  1.00 20.68 ?  410 HOH   A O    1 
HETATM 6607 O O    . HOH   E 4 .   ? 40.895 -8.256  -6.748  1.00 35.87 ?  411 HOH   A O    1 
HETATM 6608 O O    . HOH   E 4 .   ? 27.320 2.282   18.753  1.00 29.89 ?  412 HOH   A O    1 
HETATM 6609 O O    . HOH   E 4 .   ? 16.298 -14.158 20.249  1.00 53.16 ?  413 HOH   A O    1 
HETATM 6610 O O    . HOH   E 4 .   ? 10.962 1.640   12.693  1.00 24.96 ?  414 HOH   A O    1 
HETATM 6611 O O    . HOH   E 4 .   ? 21.796 -13.801 -8.201  1.00 38.51 ?  415 HOH   A O    1 
HETATM 6612 O O    . HOH   E 4 .   ? 23.954 -20.290 -1.400  1.00 16.71 ?  416 HOH   A O    1 
HETATM 6613 O O    . HOH   E 4 .   ? 23.930 -15.714 -9.142  1.00 34.34 ?  417 HOH   A O    1 
HETATM 6614 O O    . HOH   E 4 .   ? 41.569 1.546   4.979   1.00 37.23 ?  418 HOH   A O    1 
HETATM 6615 O O    . HOH   E 4 .   ? 38.075 -1.322  -1.931  1.00 19.81 ?  419 HOH   A O    1 
HETATM 6616 O O    . HOH   E 4 .   ? 32.523 -10.629 3.190   1.00 31.15 ?  420 HOH   A O    1 
HETATM 6617 O O    . HOH   E 4 .   ? 30.332 -12.946 13.484  1.00 20.48 ?  421 HOH   A O    1 
HETATM 6618 O O    . HOH   E 4 .   ? 16.294 16.767  8.576   1.00 38.29 ?  422 HOH   A O    1 
HETATM 6619 O O    . HOH   E 4 .   ? 30.920 6.208   -12.292 1.00 28.30 ?  423 HOH   A O    1 
HETATM 6620 O O    . HOH   E 4 .   ? 35.084 -5.209  -3.076  1.00 17.91 ?  424 HOH   A O    1 
HETATM 6621 O O    . HOH   E 4 .   ? 36.721 -4.971  5.379   1.00 23.40 ?  425 HOH   A O    1 
HETATM 6622 O O    B HOH   E 4 .   ? 16.680 3.284   -1.990  0.32 23.90 ?  426 HOH   A O    1 
HETATM 6623 O O    B HOH   E 4 .   ? 7.642  0.087   -0.126  0.32 34.00 ?  427 HOH   A O    1 
HETATM 6624 O O    . HOH   E 4 .   ? 32.687 -4.264  -9.910  1.00 28.20 ?  428 HOH   A O    1 
HETATM 6625 O O    . HOH   E 4 .   ? 22.643 8.136   18.404  1.00 43.85 ?  429 HOH   A O    1 
HETATM 6626 O O    . HOH   E 4 .   ? 44.999 -0.576  2.980   1.00 41.56 ?  430 HOH   A O    1 
HETATM 6627 O O    . HOH   E 4 .   ? 15.837 2.114   24.774  1.00 45.03 ?  431 HOH   A O    1 
HETATM 6628 O O    . HOH   E 4 .   ? 10.384 -13.774 -1.729  1.00 17.97 ?  432 HOH   A O    1 
HETATM 6629 O O    B HOH   E 4 .   ? 11.944 -1.508  -2.842  0.32 15.28 ?  433 HOH   A O    1 
HETATM 6630 O O    . HOH   E 4 .   ? 5.184  2.766   5.057   1.00 30.91 ?  434 HOH   A O    1 
HETATM 6631 O O    . HOH   E 4 .   ? 27.130 -3.337  19.340  1.00 36.42 ?  435 HOH   A O    1 
HETATM 6632 O O    . HOH   E 4 .   ? 21.310 -9.258  21.342  1.00 46.99 ?  436 HOH   A O    1 
HETATM 6633 O O    . HOH   E 4 .   ? 20.580 -17.725 24.791  1.00 54.04 ?  437 HOH   A O    1 
HETATM 6634 O O    . HOH   E 4 .   ? 19.394 -11.114 24.084  1.00 69.84 ?  438 HOH   A O    1 
HETATM 6635 O O    . HOH   E 4 .   ? 18.793 1.992   -0.635  1.00 14.78 ?  439 HOH   A O    1 
HETATM 6636 O O    . HOH   E 4 .   ? 23.528 -8.066  17.080  1.00 22.18 ?  440 HOH   A O    1 
HETATM 6637 O O    A HOH   E 4 .   ? 16.256 2.942   -1.433  0.68 14.76 ?  441 HOH   A O    1 
HETATM 6638 O O    . HOH   E 4 .   ? 23.343 -20.959 1.282   1.00 18.86 ?  442 HOH   A O    1 
HETATM 6639 O O    . HOH   E 4 .   ? 18.429 -16.038 16.281  1.00 37.38 ?  443 HOH   A O    1 
HETATM 6640 O O    . HOH   E 4 .   ? 23.146 7.505   -3.241  1.00 32.68 ?  444 HOH   A O    1 
HETATM 6641 O O    A HOH   E 4 .   ? -1.438 -4.966  7.624   0.68 36.27 ?  445 HOH   A O    1 
HETATM 6642 O O    . HOH   E 4 .   ? 34.377 -8.109  -0.538  1.00 28.05 ?  446 HOH   A O    1 
HETATM 6643 O O    . HOH   E 4 .   ? 9.473  -16.338 -2.087  1.00 41.67 ?  447 HOH   A O    1 
HETATM 6644 O O    . HOH   E 4 .   ? 37.717 -8.804  -3.420  1.00 23.86 ?  448 HOH   A O    1 
HETATM 6645 O O    A HOH   E 4 .   ? 14.021 -0.351  3.462   0.48 41.54 ?  449 HOH   A O    1 
HETATM 6646 O O    . HOH   E 4 .   ? 18.494 4.917   -15.078 1.00 48.06 ?  450 HOH   A O    1 
HETATM 6647 O O    . HOH   E 4 .   ? 21.556 -14.706 17.936  1.00 48.87 ?  451 HOH   A O    1 
HETATM 6648 O O    . HOH   E 4 .   ? 31.353 -12.793 -0.013  1.00 19.86 ?  452 HOH   A O    1 
HETATM 6649 O O    . HOH   E 4 .   ? 30.558 14.767  2.812   1.00 19.94 ?  453 HOH   A O    1 
HETATM 6650 O O    B HOH   E 4 .   ? 11.424 1.867   -2.148  0.32 31.84 ?  454 HOH   A O    1 
HETATM 6651 O O    B HOH   E 4 .   ? 13.828 2.632   -0.936  0.32 18.45 ?  455 HOH   A O    1 
HETATM 6652 O O    . HOH   E 4 .   ? 29.838 -16.109 10.731  1.00 35.41 ?  456 HOH   A O    1 
HETATM 6653 O O    . HOH   E 4 .   ? 27.825 7.072   -6.495  1.00 39.00 ?  457 HOH   A O    1 
HETATM 6654 O O    . HOH   E 4 .   ? 25.404 8.193   -4.816  1.00 31.60 ?  458 HOH   A O    1 
HETATM 6655 O O    . HOH   E 4 .   ? 32.486 -15.956 10.822  1.00 35.54 ?  459 HOH   A O    1 
HETATM 6656 O O    . HOH   E 4 .   ? 24.876 5.621   20.722  1.00 53.21 ?  460 HOH   A O    1 
HETATM 6657 O O    . HOH   E 4 .   ? 19.940 -17.367 -5.088  1.00 24.37 ?  461 HOH   A O    1 
HETATM 6658 O O    . HOH   E 4 .   ? 29.831 -1.945  -12.757 1.00 47.71 ?  462 HOH   A O    1 
HETATM 6659 O O    . HOH   E 4 .   ? 23.186 -22.335 -3.412  1.00 36.61 ?  463 HOH   A O    1 
HETATM 6660 O O    . HOH   E 4 .   ? 24.620 14.640  7.864   1.00 37.96 ?  464 HOH   A O    1 
HETATM 6661 O O    . HOH   E 4 .   ? 21.967 5.209   -5.967  1.00 31.93 ?  465 HOH   A O    1 
HETATM 6662 O O    . HOH   E 4 .   ? 27.514 -11.363 16.603  1.00 37.97 ?  466 HOH   A O    1 
HETATM 6663 O O    . HOH   E 4 .   ? 18.781 10.910  11.344  1.00 33.27 ?  467 HOH   A O    1 
HETATM 6664 O O    . HOH   E 4 .   ? 26.925 11.570  -1.345  1.00 32.73 ?  468 HOH   A O    1 
HETATM 6665 O O    . HOH   E 4 .   ? 12.397 1.551   17.373  1.00 40.50 ?  469 HOH   A O    1 
HETATM 6666 O O    . HOH   E 4 .   ? 15.778 -21.606 3.740   1.00 25.83 ?  470 HOH   A O    1 
HETATM 6667 O O    . HOH   E 4 .   ? 39.620 -6.977  -3.433  1.00 42.18 ?  471 HOH   A O    1 
HETATM 6668 O O    . HOH   E 4 .   ? 10.993 -15.077 -6.072  1.00 36.11 ?  472 HOH   A O    1 
HETATM 6669 O O    . HOH   E 4 .   ? 11.976 -13.503 16.305  1.00 49.34 ?  473 HOH   A O    1 
HETATM 6670 O O    . HOH   E 4 .   ? 23.482 13.732  5.521   1.00 21.31 ?  474 HOH   A O    1 
HETATM 6671 O O    . HOH   E 4 .   ? 25.795 10.776  -3.720  1.00 27.29 ?  475 HOH   A O    1 
HETATM 6672 O O    . HOH   E 4 .   ? 16.852 -20.536 16.136  1.00 31.74 ?  476 HOH   A O    1 
HETATM 6673 O O    . HOH   E 4 .   ? 18.139 -16.227 -8.823  1.00 43.28 ?  477 HOH   A O    1 
HETATM 6674 O O    . HOH   E 4 .   ? 35.135 7.417   12.282  1.00 47.55 ?  478 HOH   A O    1 
HETATM 6675 O O    . HOH   E 4 .   ? 28.796 9.028   17.515  1.00 36.33 ?  479 HOH   A O    1 
HETATM 6676 O O    . HOH   E 4 .   ? 13.981 -10.372 -10.921 1.00 32.47 ?  480 HOH   A O    1 
HETATM 6677 O O    . HOH   E 4 .   ? 17.431 -18.737 19.775  1.00 53.49 ?  481 HOH   A O    1 
HETATM 6678 O O    . HOH   E 4 .   ? 15.787 -17.175 -7.006  1.00 33.41 ?  482 HOH   A O    1 
HETATM 6679 O O    B HOH   E 4 .   ? 6.903  -1.475  -2.952  0.32 32.02 ?  483 HOH   A O    1 
HETATM 6680 O O    . HOH   E 4 .   ? 30.837 0.685   19.203  1.00 39.79 ?  484 HOH   A O    1 
HETATM 6681 O O    . HOH   E 4 .   ? 40.942 -3.992  -0.366  1.00 36.69 ?  485 HOH   A O    1 
HETATM 6682 O O    . HOH   E 4 .   ? 20.558 -16.035 -7.417  1.00 30.26 ?  486 HOH   A O    1 
HETATM 6683 O O    . HOH   E 4 .   ? 18.427 -23.160 1.955   1.00 44.39 ?  487 HOH   A O    1 
HETATM 6684 O O    B HOH   E 4 .   ? 10.844 -1.408  -5.391  0.32 17.25 ?  488 HOH   A O    1 
HETATM 6685 O O    . HOH   E 4 .   ? 41.707 9.304   -4.056  1.00 29.85 ?  489 HOH   A O    1 
HETATM 6686 O O    . HOH   E 4 .   ? 23.140 11.806  -4.069  1.00 20.33 ?  490 HOH   A O    1 
HETATM 6687 O O    . HOH   E 4 .   ? 39.178 2.392   7.500   1.00 31.96 ?  491 HOH   A O    1 
HETATM 6688 O O    . HOH   E 4 .   ? 23.298 -12.972 19.320  1.00 48.12 ?  492 HOH   A O    1 
HETATM 6689 O O    . HOH   E 4 .   ? 44.502 10.530  -1.527  1.00 32.39 ?  493 HOH   A O    1 
HETATM 6690 O O    . HOH   E 4 .   ? 16.163 -23.373 5.828   1.00 30.40 ?  494 HOH   A O    1 
HETATM 6691 O O    . HOH   E 4 .   ? 31.453 -0.568  -10.539 1.00 26.47 ?  495 HOH   A O    1 
HETATM 6692 O O    . HOH   E 4 .   ? 28.635 -4.683  -12.250 1.00 37.86 ?  496 HOH   A O    1 
HETATM 6693 O O    . HOH   E 4 .   ? 13.962 -25.311 8.889   1.00 34.92 ?  497 HOH   A O    1 
HETATM 6694 O O    . HOH   E 4 .   ? 40.508 -0.235  -7.810  1.00 33.75 ?  498 HOH   A O    1 
HETATM 6695 O O    . HOH   E 4 .   ? 16.030 -6.813  -11.895 1.00 41.25 ?  499 HOH   A O    1 
HETATM 6696 O O    . HOH   E 4 .   ? 28.759 -7.871  -15.281 1.00 46.05 ?  500 HOH   A O    1 
HETATM 6697 O O    . HOH   E 4 .   ? 20.051 -22.351 4.160   1.00 28.11 ?  501 HOH   A O    1 
HETATM 6698 O O    . HOH   E 4 .   ? 37.396 -6.648  7.528   1.00 23.74 ?  502 HOH   A O    1 
HETATM 6699 O O    . HOH   E 4 .   ? 30.781 -5.796  -11.882 1.00 46.85 ?  503 HOH   A O    1 
HETATM 6700 O O    . HOH   E 4 .   ? 8.153  -3.051  -5.710  1.00 48.29 ?  504 HOH   A O    1 
HETATM 6701 O O    . HOH   E 4 .   ? 23.146 -23.798 1.611   1.00 31.19 ?  505 HOH   A O    1 
HETATM 6702 O O    . HOH   E 4 .   ? 30.726 5.843   -14.717 1.00 36.75 ?  506 HOH   A O    1 
HETATM 6703 O O    . HOH   E 4 .   ? 39.550 0.016   6.627   1.00 29.90 ?  507 HOH   A O    1 
HETATM 6704 O O    . HOH   E 4 .   ? 37.982 13.905  6.781   1.00 41.78 ?  508 HOH   A O    1 
HETATM 6705 O O    . HOH   E 4 .   ? 28.984 14.392  0.860   1.00 47.39 ?  509 HOH   A O    1 
HETATM 6706 O O    . HOH   E 4 .   ? 14.807 8.230   5.065   1.00 39.76 ?  510 HOH   A O    1 
HETATM 6707 O O    . HOH   E 4 .   ? 22.037 -24.052 4.479   1.00 26.94 ?  511 HOH   A O    1 
HETATM 6708 O O    . HOH   E 4 .   ? 36.492 -6.561  10.140  1.00 44.79 ?  512 HOH   A O    1 
HETATM 6709 O O    T HOH   E 4 .   ? 11.923 -2.152  -3.658  0.20 11.11 ?  513 HOH   A O    1 
HETATM 6710 O O    . HOH   E 4 .   ? 17.402 -6.587  -14.200 1.00 40.09 ?  514 HOH   A O    1 
HETATM 6711 O O    . HOH   E 4 .   ? 24.068 8.991   -7.227  1.00 35.60 ?  515 HOH   A O    1 
HETATM 6712 O O    . HOH   E 4 .   ? 16.227 -21.183 18.732  1.00 42.49 ?  516 HOH   A O    1 
HETATM 6713 O O    . HOH   E 4 .   ? 15.879 -12.323 27.540  1.00 43.63 ?  517 HOH   A O    1 
HETATM 6714 O O    . HOH   E 4 .   ? 14.685 -22.729 19.867  1.00 40.65 ?  518 HOH   A O    1 
HETATM 6715 O O    . HOH   F 4 .   ? 29.830 -22.408 5.476   1.00 21.24 ?  201 HOH   B O    1 
HETATM 6716 O O    . HOH   F 4 .   ? 48.144 -6.899  15.574  1.00 31.49 ?  202 HOH   B O    1 
HETATM 6717 O O    . HOH   F 4 .   ? 41.801 -35.964 -17.268 1.00 30.97 ?  203 HOH   B O    1 
HETATM 6718 O O    . HOH   F 4 .   ? 27.745 -29.154 -1.906  1.00 37.08 ?  204 HOH   B O    1 
HETATM 6719 O O    . HOH   F 4 .   ? 27.893 -41.730 -15.204 1.00 36.78 ?  205 HOH   B O    1 
HETATM 6720 O O    . HOH   F 4 .   ? 59.151 -18.702 6.834   1.00 36.15 ?  206 HOH   B O    1 
HETATM 6721 O O    . HOH   F 4 .   ? 49.431 -22.692 -19.722 1.00 47.15 ?  207 HOH   B O    1 
HETATM 6722 O O    . HOH   F 4 .   ? 38.015 -39.479 -0.146  1.00 39.95 ?  208 HOH   B O    1 
HETATM 6723 O O    . HOH   F 4 .   ? 41.338 -7.796  5.518   1.00 39.53 ?  209 HOH   B O    1 
HETATM 6724 O O    . HOH   F 4 .   ? 47.388 -7.417  -3.901  1.00 38.43 ?  210 HOH   B O    1 
HETATM 6725 O O    . HOH   F 4 .   ? 54.493 -9.373  -8.728  1.00 19.51 ?  211 HOH   B O    1 
HETATM 6726 O O    . HOH   F 4 .   ? 52.983 -13.432 -20.335 1.00 38.58 ?  212 HOH   B O    1 
HETATM 6727 O O    . HOH   F 4 .   ? 56.370 -19.731 7.227   1.00 33.22 ?  213 HOH   B O    1 
HETATM 6728 O O    . HOH   F 4 .   ? 30.222 -40.994 -8.119  1.00 16.80 ?  214 HOH   B O    1 
HETATM 6729 O O    . HOH   F 4 .   ? 57.722 -24.481 4.996   1.00 36.66 ?  215 HOH   B O    1 
HETATM 6730 O O    . HOH   F 4 .   ? 58.222 -12.954 8.430   1.00 31.38 ?  216 HOH   B O    1 
HETATM 6731 O O    . HOH   F 4 .   ? 55.396 -16.503 -14.327 1.00 33.63 ?  217 HOH   B O    1 
HETATM 6732 O O    . HOH   F 4 .   ? 44.435 -7.241  2.081   1.00 35.68 ?  218 HOH   B O    1 
HETATM 6733 O O    . HOH   F 4 .   ? 56.669 -30.773 -7.747  1.00 31.25 ?  219 HOH   B O    1 
HETATM 6734 O O    . HOH   F 4 .   ? 50.241 -3.369  7.168   1.00 34.44 ?  220 HOH   B O    1 
HETATM 6735 O O    . HOH   F 4 .   ? 57.168 -26.858 -7.628  1.00 38.23 ?  221 HOH   B O    1 
HETATM 6736 O O    . HOH   F 4 .   ? 50.717 -6.102  0.233   1.00 27.66 ?  222 HOH   B O    1 
HETATM 6737 O O    . HOH   F 4 .   ? 57.422 -16.252 -12.160 1.00 18.89 ?  223 HOH   B O    1 
HETATM 6738 O O    . HOH   F 4 .   ? 29.790 -34.180 -0.426  1.00 34.25 ?  224 HOH   B O    1 
HETATM 6739 O O    . HOH   F 4 .   ? 35.983 -43.282 -8.513  1.00 31.20 ?  225 HOH   B O    1 
HETATM 6740 O O    . HOH   F 4 .   ? 34.558 -36.382 -7.190  1.00 18.04 ?  226 HOH   B O    1 
HETATM 6741 O O    . HOH   F 4 .   ? 29.895 -26.324 3.967   1.00 28.34 ?  227 HOH   B O    1 
HETATM 6742 O O    . HOH   F 4 .   ? 48.101 -24.572 -17.725 1.00 30.09 ?  228 HOH   B O    1 
HETATM 6743 O O    . HOH   F 4 .   ? 41.521 -39.188 -14.931 1.00 21.62 ?  229 HOH   B O    1 
HETATM 6744 O O    . HOH   F 4 .   ? 37.202 -19.672 -18.116 1.00 40.90 ?  230 HOH   B O    1 
HETATM 6745 O O    . HOH   F 4 .   ? 39.327 -10.923 6.132   1.00 25.06 ?  231 HOH   B O    1 
HETATM 6746 O O    . HOH   F 4 .   ? 25.397 -25.930 -1.388  1.00 31.68 ?  232 HOH   B O    1 
HETATM 6747 O O    . HOH   F 4 .   ? 30.922 -28.781 4.317   1.00 26.79 ?  233 HOH   B O    1 
HETATM 6748 O O    . HOH   F 4 .   ? 35.116 -7.983  -3.044  1.00 18.22 ?  234 HOH   B O    1 
HETATM 6749 O O    . HOH   F 4 .   ? 41.392 -9.632  13.090  1.00 22.68 ?  235 HOH   B O    1 
HETATM 6750 O O    . HOH   F 4 .   ? 32.814 -43.799 -11.341 1.00 20.87 ?  236 HOH   B O    1 
HETATM 6751 O O    . HOH   F 4 .   ? 45.165 -34.957 6.827   1.00 37.79 ?  237 HOH   B O    1 
HETATM 6752 O O    . HOH   F 4 .   ? 50.758 -12.981 -0.451  1.00 12.57 ?  238 HOH   B O    1 
HETATM 6753 O O    . HOH   F 4 .   ? 51.680 -6.492  4.421   1.00 20.77 ?  239 HOH   B O    1 
HETATM 6754 O O    . HOH   F 4 .   ? 28.434 -19.667 -13.134 1.00 24.40 ?  240 HOH   B O    1 
HETATM 6755 O O    . HOH   F 4 .   ? 48.598 -36.468 -15.527 1.00 40.14 ?  241 HOH   B O    1 
HETATM 6756 O O    . HOH   F 4 .   ? 40.601 -16.099 14.136  1.00 25.29 ?  242 HOH   B O    1 
HETATM 6757 O O    . HOH   F 4 .   ? 42.567 -25.373 2.652   1.00 14.77 ?  243 HOH   B O    1 
HETATM 6758 O O    . HOH   F 4 .   ? 44.540 -27.818 -0.740  1.00 21.69 ?  244 HOH   B O    1 
HETATM 6759 O O    . HOH   F 4 .   ? 34.250 -18.503 11.401  1.00 24.00 ?  245 HOH   B O    1 
HETATM 6760 O O    . HOH   F 4 .   ? 44.968 -43.545 -10.502 1.00 28.19 ?  246 HOH   B O    1 
HETATM 6761 O O    . HOH   F 4 .   ? 42.642 -22.876 3.859   1.00 11.81 ?  247 HOH   B O    1 
HETATM 6762 O O    . HOH   F 4 .   ? 39.491 -11.122 0.324   1.00 16.91 ?  248 HOH   B O    1 
HETATM 6763 O O    . HOH   F 4 .   ? 43.112 -43.259 -8.223  1.00 28.81 ?  249 HOH   B O    1 
HETATM 6764 O O    . HOH   F 4 .   ? 58.160 -10.619 -4.064  1.00 21.00 ?  250 HOH   B O    1 
HETATM 6765 O O    . HOH   F 4 .   ? 57.652 -24.371 -3.812  1.00 21.42 ?  251 HOH   B O    1 
HETATM 6766 O O    . HOH   F 4 .   ? 46.415 -1.571  13.299  1.00 29.93 ?  252 HOH   B O    1 
HETATM 6767 O O    . HOH   F 4 .   ? 43.198 -32.404 -17.081 1.00 24.23 ?  253 HOH   B O    1 
HETATM 6768 O O    . HOH   F 4 .   ? 29.740 -25.201 -10.808 1.00 16.47 ?  254 HOH   B O    1 
HETATM 6769 O O    . HOH   F 4 .   ? 40.360 -12.755 -11.515 1.00 15.62 ?  255 HOH   B O    1 
HETATM 6770 O O    . HOH   F 4 .   ? 49.338 -28.720 -6.938  1.00 15.59 ?  256 HOH   B O    1 
HETATM 6771 O O    . HOH   F 4 .   ? 38.474 -11.056 -2.248  1.00 19.50 ?  257 HOH   B O    1 
HETATM 6772 O O    . HOH   F 4 .   ? 30.867 -15.744 2.660   1.00 13.98 ?  258 HOH   B O    1 
HETATM 6773 O O    . HOH   F 4 .   ? 41.883 -23.512 9.314   1.00 17.13 ?  259 HOH   B O    1 
HETATM 6774 O O    . HOH   F 4 .   ? 27.163 -31.802 -9.996  1.00 21.03 ?  260 HOH   B O    1 
HETATM 6775 O O    . HOH   F 4 .   ? 51.506 -13.848 11.028  1.00 26.73 ?  261 HOH   B O    1 
HETATM 6776 O O    . HOH   F 4 .   ? 30.550 -42.257 -10.648 1.00 28.56 ?  262 HOH   B O    1 
HETATM 6777 O O    . HOH   F 4 .   ? 50.956 -39.984 -8.225  1.00 31.40 ?  263 HOH   B O    1 
HETATM 6778 O O    . HOH   F 4 .   ? 49.818 -0.522  10.254  1.00 31.37 ?  264 HOH   B O    1 
HETATM 6779 O O    . HOH   F 4 .   ? 34.503 -12.809 2.615   1.00 24.97 ?  265 HOH   B O    1 
HETATM 6780 O O    . HOH   F 4 .   ? 46.631 -31.255 -4.832  1.00 21.59 ?  266 HOH   B O    1 
HETATM 6781 O O    . HOH   F 4 .   ? 31.827 -17.898 -14.520 1.00 30.39 ?  267 HOH   B O    1 
HETATM 6782 O O    . HOH   F 4 .   ? 34.951 -33.330 -19.207 1.00 28.56 ?  268 HOH   B O    1 
HETATM 6783 O O    . HOH   F 4 .   ? 57.522 -9.238  1.455   1.00 20.26 ?  269 HOH   B O    1 
HETATM 6784 O O    . HOH   F 4 .   ? 43.401 -15.786 -12.169 1.00 14.66 ?  270 HOH   B O    1 
HETATM 6785 O O    . HOH   F 4 .   ? 46.862 -29.578 9.826   1.00 30.69 ?  271 HOH   B O    1 
HETATM 6786 O O    . HOH   F 4 .   ? 56.213 -23.527 -14.686 1.00 26.68 ?  272 HOH   B O    1 
HETATM 6787 O O    . HOH   F 4 .   ? 38.903 -12.015 12.387  1.00 35.21 ?  273 HOH   B O    1 
HETATM 6788 O O    . HOH   F 4 .   ? 42.374 -34.702 3.779   1.00 24.89 ?  274 HOH   B O    1 
HETATM 6789 O O    . HOH   F 4 .   ? 48.031 -22.777 5.870   1.00 17.80 ?  275 HOH   B O    1 
HETATM 6790 O O    . HOH   F 4 .   ? 28.271 -34.348 -9.463  1.00 19.69 ?  276 HOH   B O    1 
HETATM 6791 O O    . HOH   F 4 .   ? 34.878 -24.585 13.862  1.00 28.86 ?  277 HOH   B O    1 
HETATM 6792 O O    . HOH   F 4 .   ? 42.340 -9.900  9.394   1.00 21.40 ?  278 HOH   B O    1 
HETATM 6793 O O    . HOH   F 4 .   ? 28.496 -30.855 -14.761 1.00 30.36 ?  279 HOH   B O    1 
HETATM 6794 O O    . HOH   F 4 .   ? 56.948 -8.662  8.447   1.00 19.51 ?  280 HOH   B O    1 
HETATM 6795 O O    . HOH   F 4 .   ? 27.987 -22.890 -8.019  1.00 17.80 ?  281 HOH   B O    1 
HETATM 6796 O O    . HOH   F 4 .   ? 42.919 -20.322 -20.800 1.00 37.83 ?  282 HOH   B O    1 
HETATM 6797 O O    . HOH   F 4 .   ? 36.819 -12.777 -1.512  1.00 26.38 ?  283 HOH   B O    1 
HETATM 6798 O O    . HOH   F 4 .   ? 48.419 -25.064 3.126   1.00 13.47 ?  284 HOH   B O    1 
HETATM 6799 O O    . HOH   F 4 .   ? 41.119 -5.559  11.538  1.00 43.48 ?  285 HOH   B O    1 
HETATM 6800 O O    . HOH   F 4 .   ? 43.577 -15.405 18.228  1.00 32.07 ?  286 HOH   B O    1 
HETATM 6801 O O    . HOH   F 4 .   ? 57.121 -12.159 12.403  1.00 38.09 ?  287 HOH   B O    1 
HETATM 6802 O O    . HOH   F 4 .   ? 33.562 -15.280 -13.974 1.00 21.12 ?  288 HOH   B O    1 
HETATM 6803 O O    . HOH   F 4 .   ? 27.590 -26.668 -15.648 1.00 32.59 ?  289 HOH   B O    1 
HETATM 6804 O O    . HOH   F 4 .   ? 52.536 -10.422 13.027  1.00 22.59 ?  290 HOH   B O    1 
HETATM 6805 O O    . HOH   F 4 .   ? 49.994 -24.640 5.823   1.00 32.86 ?  291 HOH   B O    1 
HETATM 6806 O O    . HOH   F 4 .   ? 48.720 -20.031 5.954   1.00 14.20 ?  292 HOH   B O    1 
HETATM 6807 O O    . HOH   F 4 .   ? 47.089 -33.982 -4.599  1.00 17.72 ?  293 HOH   B O    1 
HETATM 6808 O O    . HOH   F 4 .   ? 35.081 -33.613 4.540   1.00 28.65 ?  294 HOH   B O    1 
HETATM 6809 O O    . HOH   F 4 .   ? 45.413 -33.382 -15.953 1.00 23.84 ?  295 HOH   B O    1 
HETATM 6810 O O    . HOH   F 4 .   ? 51.244 -37.600 -9.592  1.00 25.82 ?  296 HOH   B O    1 
HETATM 6811 O O    . HOH   F 4 .   ? 59.752 -15.273 8.184   1.00 30.81 ?  297 HOH   B O    1 
HETATM 6812 O O    . HOH   F 4 .   ? 37.551 -18.170 13.118  1.00 29.58 ?  298 HOH   B O    1 
HETATM 6813 O O    . HOH   F 4 .   ? 44.628 -27.468 2.001   1.00 15.70 ?  299 HOH   B O    1 
HETATM 6814 O O    . HOH   F 4 .   ? 40.275 -10.830 -9.522  1.00 17.44 ?  300 HOH   B O    1 
HETATM 6815 O O    . HOH   F 4 .   ? 42.371 -9.886  -14.898 1.00 36.99 ?  301 HOH   B O    1 
HETATM 6816 O O    . HOH   F 4 .   ? 42.715 -12.262 -18.499 1.00 29.28 ?  302 HOH   B O    1 
HETATM 6817 O O    . HOH   F 4 .   ? 44.049 -29.365 -4.697  1.00 23.72 ?  303 HOH   B O    1 
HETATM 6818 O O    . HOH   F 4 .   ? 45.921 -40.423 -3.599  1.00 28.94 ?  304 HOH   B O    1 
HETATM 6819 O O    . HOH   F 4 .   ? 37.341 -35.684 7.242   1.00 34.44 ?  305 HOH   B O    1 
HETATM 6820 O O    . HOH   F 4 .   ? 52.630 -35.668 -8.644  1.00 29.21 ?  306 HOH   B O    1 
HETATM 6821 O O    . HOH   F 4 .   ? 41.277 -24.505 15.791  1.00 42.98 ?  307 HOH   B O    1 
HETATM 6822 O O    . HOH   F 4 .   ? 52.549 -29.256 -13.034 1.00 24.75 ?  308 HOH   B O    1 
HETATM 6823 O O    . HOH   F 4 .   ? 53.256 -16.108 -12.695 1.00 28.20 ?  309 HOH   B O    1 
HETATM 6824 O O    . HOH   F 4 .   ? 53.446 -30.217 4.550   1.00 19.28 ?  310 HOH   B O    1 
HETATM 6825 O O    . HOH   F 4 .   ? 62.699 -13.573 4.756   1.00 26.64 ?  311 HOH   B O    1 
HETATM 6826 O O    . HOH   F 4 .   ? 37.866 -10.231 -10.753 1.00 17.46 ?  312 HOH   B O    1 
HETATM 6827 O O    . HOH   F 4 .   ? 48.124 -32.594 -16.601 1.00 44.92 ?  313 HOH   B O    1 
HETATM 6828 O O    . HOH   F 4 .   ? 38.351 -12.775 7.945   1.00 18.01 ?  314 HOH   B O    1 
HETATM 6829 O O    . HOH   F 4 .   ? 32.828 -34.615 -5.926  1.00 16.78 ?  315 HOH   B O    1 
HETATM 6830 O O    . HOH   F 4 .   ? 41.753 -8.074  1.377   1.00 24.57 ?  316 HOH   B O    1 
HETATM 6831 O O    . HOH   F 4 .   ? 62.864 -20.273 -0.793  1.00 38.36 ?  317 HOH   B O    1 
HETATM 6832 O O    . HOH   F 4 .   ? 57.651 -22.085 3.179   1.00 28.05 ?  318 HOH   B O    1 
HETATM 6833 O O    . HOH   F 4 .   ? 43.187 -21.431 10.679  1.00 16.00 ?  319 HOH   B O    1 
HETATM 6834 O O    . HOH   F 4 .   ? 37.147 -30.544 -21.028 1.00 32.60 ?  320 HOH   B O    1 
HETATM 6835 O O    . HOH   F 4 .   ? 25.967 -21.473 -3.569  1.00 17.03 ?  321 HOH   B O    1 
HETATM 6836 O O    . HOH   F 4 .   ? 44.142 -1.804  7.622   1.00 43.18 ?  322 HOH   B O    1 
HETATM 6837 O O    . HOH   F 4 .   ? 26.352 -21.035 -6.270  1.00 16.24 ?  323 HOH   B O    1 
HETATM 6838 O O    . HOH   F 4 .   ? 51.701 -5.959  -7.898  1.00 44.27 ?  324 HOH   B O    1 
HETATM 6839 O O    . HOH   F 4 .   ? 44.598 -24.629 9.602   1.00 19.75 ?  325 HOH   B O    1 
HETATM 6840 O O    . HOH   F 4 .   ? 53.649 -12.564 -22.269 1.00 33.57 ?  326 HOH   B O    1 
HETATM 6841 O O    . HOH   F 4 .   ? 38.386 -9.339  -13.291 1.00 27.83 ?  327 HOH   B O    1 
HETATM 6842 O O    . HOH   F 4 .   ? 36.716 -12.428 4.286   1.00 18.56 ?  328 HOH   B O    1 
HETATM 6843 O O    . HOH   F 4 .   ? 51.391 -32.925 -10.818 1.00 39.29 ?  329 HOH   B O    1 
HETATM 6844 O O    . HOH   F 4 .   ? 59.939 -17.209 -10.521 1.00 34.15 ?  330 HOH   B O    1 
HETATM 6845 O O    . HOH   F 4 .   ? 47.142 -24.472 8.195   1.00 25.02 ?  331 HOH   B O    1 
HETATM 6846 O O    . HOH   F 4 .   ? 27.862 -14.745 -9.437  1.00 35.29 ?  332 HOH   B O    1 
HETATM 6847 O O    . HOH   F 4 .   ? 33.622 -31.195 11.051  1.00 35.06 ?  333 HOH   B O    1 
HETATM 6848 O O    . HOH   F 4 .   ? 39.474 -23.468 -20.322 1.00 36.68 ?  334 HOH   B O    1 
HETATM 6849 O O    . HOH   F 4 .   ? 43.115 -34.681 0.099   1.00 19.97 ?  335 HOH   B O    1 
HETATM 6850 O O    . HOH   F 4 .   ? 47.487 -27.444 2.024   1.00 14.99 ?  336 HOH   B O    1 
HETATM 6851 O O    . HOH   F 4 .   ? 37.042 -15.116 -16.501 1.00 39.29 ?  337 HOH   B O    1 
HETATM 6852 O O    . HOH   F 4 .   ? 38.429 -12.207 -16.269 1.00 40.23 ?  338 HOH   B O    1 
HETATM 6853 O O    . HOH   F 4 .   ? 48.624 -11.937 -13.943 1.00 26.75 ?  339 HOH   B O    1 
HETATM 6854 O O    . HOH   F 4 .   ? 45.734 -36.244 -16.122 1.00 34.59 ?  340 HOH   B O    1 
HETATM 6855 O O    . HOH   F 4 .   ? 42.856 -43.530 -14.398 1.00 42.80 ?  341 HOH   B O    1 
HETATM 6856 O O    . HOH   F 4 .   ? 46.808 -19.903 12.317  1.00 32.69 ?  342 HOH   B O    1 
HETATM 6857 O O    . HOH   F 4 .   ? 28.864 -42.864 -12.382 1.00 37.45 ?  343 HOH   B O    1 
HETATM 6858 O O    . HOH   F 4 .   ? 37.101 -45.232 -9.748  1.00 38.10 ?  344 HOH   B O    1 
HETATM 6859 O O    . HOH   F 4 .   ? 32.999 -14.692 1.053   1.00 18.78 ?  345 HOH   B O    1 
HETATM 6860 O O    . HOH   F 4 .   ? 38.517 -22.334 15.033  1.00 42.11 ?  346 HOH   B O    1 
HETATM 6861 O O    . HOH   F 4 .   ? 39.844 -44.310 -11.218 1.00 39.50 ?  347 HOH   B O    1 
HETATM 6862 O O    . HOH   F 4 .   ? 40.406 -43.497 -9.134  1.00 26.48 ?  348 HOH   B O    1 
HETATM 6863 O O    . HOH   F 4 .   ? 33.745 -9.386  -8.831  1.00 32.10 ?  349 HOH   B O    1 
HETATM 6864 O O    . HOH   F 4 .   ? 27.759 -26.646 -0.620  1.00 30.73 ?  350 HOH   B O    1 
HETATM 6865 O O    . HOH   F 4 .   ? 34.589 -10.331 7.587   1.00 23.88 ?  351 HOH   B O    1 
HETATM 6866 O O    . HOH   F 4 .   ? 62.636 -20.148 -4.770  1.00 45.73 ?  352 HOH   B O    1 
HETATM 6867 O O    . HOH   F 4 .   ? 55.643 -8.253  10.859  1.00 25.20 ?  353 HOH   B O    1 
HETATM 6868 O O    . HOH   F 4 .   ? 23.275 -23.695 6.800   1.00 36.00 ?  354 HOH   B O    1 
HETATM 6869 O O    . HOH   F 4 .   ? 44.177 -37.357 -17.757 1.00 34.21 ?  355 HOH   B O    1 
HETATM 6870 O O    . HOH   F 4 .   ? 36.164 -8.537  -9.656  1.00 34.78 ?  356 HOH   B O    1 
HETATM 6871 O O    . HOH   F 4 .   ? 56.618 -7.302  3.112   1.00 28.66 ?  357 HOH   B O    1 
HETATM 6872 O O    . HOH   F 4 .   ? 34.060 -7.833  11.462  1.00 40.34 ?  358 HOH   B O    1 
HETATM 6873 O O    . HOH   F 4 .   ? 43.200 -12.705 -21.284 1.00 40.69 ?  359 HOH   B O    1 
HETATM 6874 O O    . HOH   F 4 .   ? 61.512 -19.926 1.723   1.00 37.67 ?  360 HOH   B O    1 
HETATM 6875 O O    . HOH   F 4 .   ? 56.978 -21.549 -16.364 1.00 41.11 ?  361 HOH   B O    1 
HETATM 6876 O O    . HOH   F 4 .   ? 40.253 -8.824  9.969   1.00 34.10 ?  362 HOH   B O    1 
HETATM 6877 O O    . HOH   F 4 .   ? 27.181 -25.948 -11.415 1.00 33.00 ?  363 HOH   B O    1 
HETATM 6878 O O    . HOH   F 4 .   ? 54.206 -5.755  3.034   1.00 36.36 ?  364 HOH   B O    1 
HETATM 6879 O O    . HOH   F 4 .   ? 40.203 -11.327 -13.921 1.00 33.62 ?  365 HOH   B O    1 
HETATM 6880 O O    . HOH   F 4 .   ? 36.224 -8.745  8.989   1.00 39.06 ?  366 HOH   B O    1 
HETATM 6881 O O    . HOH   F 4 .   ? 48.365 -26.519 8.840   1.00 41.05 ?  367 HOH   B O    1 
HETATM 6882 O O    . HOH   F 4 .   ? 58.996 -10.464 9.185   1.00 38.13 ?  368 HOH   B O    1 
HETATM 6883 O O    . HOH   F 4 .   ? 39.886 -6.980  7.868   1.00 39.57 ?  369 HOH   B O    1 
HETATM 6884 O O    . HOH   F 4 .   ? 56.059 -7.786  -0.575  1.00 35.56 ?  370 HOH   B O    1 
HETATM 6885 O O    . HOH   F 4 .   ? 32.580 -23.576 14.122  1.00 39.00 ?  371 HOH   B O    1 
HETATM 6886 O O    . HOH   F 4 .   ? 52.069 -12.906 13.356  1.00 30.50 ?  372 HOH   B O    1 
HETATM 6887 O O    . HOH   F 4 .   ? 41.797 -9.992  -17.408 1.00 54.78 ?  373 HOH   B O    1 
HETATM 6888 O O    . HOH   F 4 .   ? 63.007 -12.386 6.899   1.00 38.08 ?  374 HOH   B O    1 
HETATM 6889 O O    . HOH   F 4 .   ? 36.558 -22.817 13.287  1.00 26.00 ?  375 HOH   B O    1 
HETATM 6890 O O    . HOH   F 4 .   ? 38.048 -10.583 10.068  1.00 29.81 ?  376 HOH   B O    1 
HETATM 6891 O O    . HOH   F 4 .   ? 41.835 -6.781  -4.850  1.00 46.34 ?  377 HOH   B O    1 
HETATM 6892 O O    . HOH   F 4 .   ? 44.074 -5.589  -3.502  1.00 41.57 ?  378 HOH   B O    1 
HETATM 6893 O O    . HOH   F 4 .   ? 40.122 -7.639  3.260   1.00 33.81 ?  379 HOH   B O    1 
HETATM 6894 O O    . HOH   F 4 .   ? 42.632 -17.086 -23.185 1.00 44.95 ?  380 HOH   B O    1 
HETATM 6895 O O    . HOH   F 4 .   ? 39.678 -14.100 15.711  1.00 52.05 ?  381 HOH   B O    1 
HETATM 6896 O O    . HOH   F 4 .   ? 60.508 -22.292 2.839   1.00 47.66 ?  382 HOH   B O    1 
HETATM 6897 O O    . HOH   F 4 .   ? 52.879 -29.940 7.230   1.00 23.22 ?  383 HOH   B O    1 
HETATM 6898 O O    . HOH   F 4 .   ? 25.807 -18.888 -11.929 1.00 38.83 ?  384 HOH   B O    1 
HETATM 6899 O O    . HOH   F 4 .   ? 46.788 -5.333  2.945   1.00 40.33 ?  385 HOH   B O    1 
HETATM 6900 O O    . HOH   F 4 .   ? 23.926 -20.852 -7.688  1.00 27.68 ?  386 HOH   B O    1 
HETATM 6901 O O    . HOH   F 4 .   ? 35.405 -33.752 7.334   1.00 42.57 ?  387 HOH   B O    1 
HETATM 6902 O O    . HOH   F 4 .   ? 40.903 -9.838  15.866  1.00 45.62 ?  388 HOH   B O    1 
HETATM 6903 O O    . HOH   F 4 .   ? 35.309 -20.340 13.354  1.00 31.41 ?  389 HOH   B O    1 
HETATM 6904 O O    . HOH   F 4 .   ? 40.695 -6.609  -0.857  1.00 26.27 ?  390 HOH   B O    1 
HETATM 6905 O O    . HOH   F 4 .   ? 44.100 -31.831 -3.841  1.00 34.25 ?  391 HOH   B O    1 
HETATM 6906 O O    . HOH   F 4 .   ? 26.671 -27.988 -13.524 1.00 35.09 ?  392 HOH   B O    1 
HETATM 6907 O O    . HOH   F 4 .   ? 27.916 -27.090 2.168   1.00 31.16 ?  393 HOH   B O    1 
HETATM 6908 O O    . HOH   F 4 .   ? 24.611 -20.685 -10.474 1.00 38.60 ?  394 HOH   B O    1 
HETATM 6909 O O    . HOH   F 4 .   ? 50.651 -30.835 8.724   1.00 29.37 ?  395 HOH   B O    1 
HETATM 6910 O O    . HOH   F 4 .   ? 34.412 -33.477 9.598   1.00 33.18 ?  396 HOH   B O    1 
HETATM 6911 O O    . HOH   F 4 .   ? 26.846 -30.638 -12.699 1.00 29.83 ?  397 HOH   B O    1 
HETATM 6912 O O    . HOH   F 4 .   ? 45.736 -20.256 15.173  1.00 50.47 ?  398 HOH   B O    1 
HETATM 6913 O O    . HOH   F 4 .   ? 57.597 -6.436  -2.348  1.00 33.54 ?  399 HOH   B O    1 
HETATM 6914 O O    . HOH   F 4 .   ? 40.925 -11.826 -22.356 1.00 42.01 ?  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   ? 0.6637 0.6575 0.7334 0.0011  -0.0155 0.0699  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.6602 0.6546 0.7072 -0.0023 -0.0151 0.0539  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.6610 0.6546 0.7228 -0.0005 -0.0151 0.0700  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.6576 0.6520 0.6997 -0.0033 -0.0151 0.0551  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.6455 0.6426 0.6894 -0.0061 -0.0184 0.0717  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.6440 0.6412 0.6756 -0.0076 -0.0181 0.0628  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.6477 0.6450 0.7009 -0.0050 -0.0191 0.0742  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.6467 0.6434 0.6847 -0.0068 -0.0186 0.0633  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.6710 0.6619 0.7368 0.0024  -0.0116 0.0694  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.6658 0.6586 0.7102 -0.0009 -0.0121 0.0499  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.6747 0.6641 0.7401 0.0034  -0.0107 0.0688  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.6687 0.6607 0.7130 -0.0002 -0.0111 0.0478  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.6743 0.6644 0.7406 0.0033  -0.0101 0.0704  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.6685 0.6609 0.7131 -0.0000 -0.0109 0.0487  3   VAL   A CG2 
31   N N   . ASN   A 4   ? 0.6252 0.6259 0.6355 -0.0131 -0.0202 0.0703  4   ASN   A N   
32   C CA  . ASN   A 4   ? 0.5834 0.5915 0.5353 -0.0264 -0.0225 0.0738  4   ASN   A CA  
33   C C   . ASN   A 4   ? 0.5330 0.5540 0.4783 -0.0387 -0.0120 0.0543  4   ASN   A C   
34   O O   . ASN   A 4   ? 0.5350 0.5570 0.4650 -0.0397 -0.0133 0.0568  4   ASN   A O   
35   C CB  . ASN   A 4   ? 0.5900 0.5918 0.4873 -0.0282 -0.0349 0.0955  4   ASN   A CB  
36   C CG  . ASN   A 4   ? 0.5946 0.5906 0.4449 -0.0307 -0.0464 0.1164  4   ASN   A CG  
37   O OD1 . ASN   A 4   ? 0.5980 0.5901 0.4294 -0.0318 -0.0535 0.1242  4   ASN   A OD1 
38   N ND2 . ASN   A 4   ? 0.5946 0.5893 0.4340 -0.0312 -0.0468 0.1265  4   ASN   A ND2 
46   N N   . SER   A 5   ? 0.4789 0.5115 0.4319 -0.0512 -0.0018 0.0324  5   SER   A N   
47   C CA  . SER   A 5   ? 0.4232 0.4726 0.3905 -0.0621 0.0146  0.0096  5   SER   A CA  
48   C C   . SER   A 5   ? 0.3636 0.4224 0.3341 -0.0681 0.0313  -0.0053 5   SER   A C   
49   O O   . SER   A 5   ? 0.3690 0.4330 0.3448 -0.0564 0.0289  -0.0155 5   SER   A O   
50   C CB  . SER   A 5   ? 0.4293 0.4827 0.4117 -0.0685 0.0142  0.0017  5   SER   A CB  
51   O OG  . SER   A 5   ? 0.4329 0.4857 0.4245 -0.0726 0.0168  -0.0035 5   SER   A OG  
57   N N   A PHE   A 6   ? 0.3196 0.3883 0.2919 -0.0863 0.0508  -0.0016 6   PHE   A N   
58   N N   B PHE   A 6   ? 0.3346 0.3897 0.3015 -0.0684 0.0347  -0.0041 6   PHE   A N   
59   C CA  A PHE   A 6   ? 0.2823 0.3554 0.2430 -0.0989 0.0629  0.0156  6   PHE   A CA  
60   C CA  B PHE   A 6   ? 0.3082 0.3579 0.2646 -0.0676 0.0367  0.0039  6   PHE   A CA  
61   C C   A PHE   A 6   ? 0.2787 0.3545 0.2449 -0.1073 0.0789  0.0110  6   PHE   A C   
62   C C   B PHE   A 6   ? 0.2993 0.3470 0.2567 -0.0698 0.0432  0.0047  6   PHE   A C   
63   O O   A PHE   A 6   ? 0.2851 0.3594 0.2821 -0.1077 0.0775  0.0145  6   PHE   A O   
64   O O   B PHE   A 6   ? 0.2989 0.3456 0.2494 -0.0752 0.0433  0.0049  6   PHE   A O   
65   C CB  A PHE   A 6   ? 0.2598 0.3271 0.2160 -0.0913 0.0515  0.0289  6   PHE   A CB  
66   C CB  B PHE   A 6   ? 0.2952 0.3388 0.2438 -0.0610 0.0304  0.0088  6   PHE   A CB  
67   C CG  A PHE   A 6   ? 0.2374 0.3027 0.1982 -0.0858 0.0356  0.0303  6   PHE   A CG  
68   C CG  B PHE   A 6   ? 0.2821 0.3212 0.2277 -0.0574 0.0223  0.0131  6   PHE   A CG  
69   C CD1 A PHE   A 6   ? 0.2228 0.2913 0.1897 -0.0776 0.0251  0.0276  6   PHE   A CD1 
70   C CD1 B PHE   A 6   ? 0.2757 0.3138 0.2209 -0.0531 0.0164  0.0141  6   PHE   A CD1 
71   C CD2 A PHE   A 6   ? 0.2413 0.2957 0.2142 -0.0748 0.0325  0.0253  6   PHE   A CD2 
72   C CD2 B PHE   A 6   ? 0.2803 0.3139 0.2275 -0.0529 0.0217  0.0151  6   PHE   A CD2 
73   C CE1 A PHE   A 6   ? 0.2208 0.2850 0.1970 -0.0751 0.0285  0.0291  6   PHE   A CE1 
74   C CE1 B PHE   A 6   ? 0.2735 0.3092 0.2222 -0.0516 0.0164  0.0168  6   PHE   A CE1 
75   C CE2 A PHE   A 6   ? 0.2372 0.2907 0.2290 -0.0699 0.0293  0.0222  6   PHE   A CE2 
76   C CE2 B PHE   A 6   ? 0.2776 0.3104 0.2320 -0.0501 0.0194  0.0161  6   PHE   A CE2 
77   C CZ  A PHE   A 6   ? 0.2296 0.2866 0.2118 -0.0719 0.0291  0.0212  6   PHE   A CZ  
78   C CZ  B PHE   A 6   ? 0.2753 0.3087 0.2262 -0.0502 0.0160  0.0158  6   PHE   A CZ  
97   N N   A SER   A 7   ? 0.2645 0.3476 0.2256 -0.1109 0.0855  -0.0021 7   SER   A N   
98   N N   B SER   A 7   ? 0.2893 0.3372 0.2610 -0.0651 0.0446  0.0048  7   SER   A N   
99   C CA  A SER   A 7   ? 0.2656 0.3488 0.2290 -0.0956 0.0825  -0.0169 7   SER   A CA  
100  C CA  B SER   A 7   ? 0.2850 0.3307 0.2738 -0.0574 0.0411  0.0048  7   SER   A CA  
101  C C   A SER   A 7   ? 0.2445 0.3209 0.1988 -0.0997 0.0808  -0.0230 7   SER   A C   
102  C C   B SER   A 7   ? 0.2723 0.3151 0.2602 -0.0566 0.0434  0.0020  7   SER   A C   
103  O O   A SER   A 7   ? 0.2548 0.3121 0.1949 -0.1044 0.0779  -0.0166 7   SER   A O   
104  O O   B SER   A 7   ? 0.2729 0.3148 0.2560 -0.0575 0.0416  0.0006  7   SER   A O   
105  C CB  A SER   A 7   ? 0.2877 0.3710 0.2547 -0.0792 0.0810  -0.0139 7   SER   A CB  
106  C CB  B SER   A 7   ? 0.2923 0.3376 0.2940 -0.0528 0.0370  0.0111  7   SER   A CB  
107  O OG  A SER   A 7   ? 0.3074 0.3845 0.2759 -0.0649 0.0727  -0.0150 7   SER   A OG  
108  O OG  B SER   A 7   ? 0.2976 0.3414 0.3156 -0.0492 0.0322  0.0194  7   SER   A OG  
119  N N   A GLY   A 8   ? 0.2203 0.3014 0.1940 -0.0942 0.0747  -0.0328 8   GLY   A N   
120  N N   B GLY   A 8   ? 0.2614 0.3017 0.2449 -0.0541 0.0517  -0.0009 8   GLY   A N   
121  C CA  A GLY   A 8   ? 0.2068 0.2777 0.2032 -0.0788 0.0740  -0.0313 8   GLY   A CA  
122  C CA  B GLY   A 8   ? 0.2515 0.2837 0.2284 -0.0503 0.0509  -0.0033 8   GLY   A CA  
123  C C   A GLY   A 8   ? 0.1900 0.2597 0.2036 -0.0636 0.0624  -0.0390 8   GLY   A C   
124  C C   B GLY   A 8   ? 0.2388 0.2670 0.2110 -0.0472 0.0521  -0.0037 8   GLY   A C   
125  O O   A GLY   A 8   ? 0.1900 0.2629 0.2146 -0.0496 0.0575  -0.0567 8   GLY   A O   
126  O O   B GLY   A 8   ? 0.2390 0.2640 0.2107 -0.0481 0.0585  -0.0084 8   GLY   A O   
133  N N   A TYR   A 9   ? 0.1720 0.2393 0.1891 -0.0589 0.0542  -0.0234 9   TYR   A N   
134  N N   B TYR   A 9   ? 0.2241 0.2535 0.2116 -0.0398 0.0393  0.0002  9   TYR   A N   
135  C CA  A TYR   A 9   ? 0.1614 0.2180 0.1689 -0.0550 0.0423  -0.0155 9   TYR   A CA  
136  C CA  B TYR   A 9   ? 0.2103 0.2383 0.2053 -0.0308 0.0418  0.0045  9   TYR   A CA  
137  C C   A TYR   A 9   ? 0.1632 0.1958 0.1715 -0.0495 0.0495  0.0020  9   TYR   A C   
138  C C   B TYR   A 9   ? 0.2060 0.2183 0.1927 -0.0212 0.0477  0.0062  9   TYR   A C   
139  O O   A TYR   A 9   ? 0.1881 0.2088 0.1888 -0.0387 0.0488  -0.0035 9   TYR   A O   
140  O O   B TYR   A 9   ? 0.2138 0.2216 0.1945 -0.0181 0.0549  0.0094  9   TYR   A O   
141  C CB  A TYR   A 9   ? 0.1536 0.2269 0.1605 -0.0444 0.0409  -0.0145 9   TYR   A CB  
142  C CB  B TYR   A 9   ? 0.2040 0.2445 0.2152 -0.0273 0.0318  0.0027  9   TYR   A CB  
143  C CG  A TYR   A 9   ? 0.1543 0.2353 0.1724 -0.0322 0.0542  -0.0182 9   TYR   A CG  
144  C CG  B TYR   A 9   ? 0.2004 0.2468 0.2131 -0.0254 0.0235  0.0026  9   TYR   A CG  
145  C CD1 A TYR   A 9   ? 0.1546 0.2426 0.1871 -0.0408 0.0571  -0.0268 9   TYR   A CD1 
146  C CD1 B TYR   A 9   ? 0.2014 0.2507 0.2191 -0.0270 0.0203  -0.0007 9   TYR   A CD1 
147  C CD2 A TYR   A 9   ? 0.1535 0.2310 0.1749 -0.0305 0.0415  0.0045  9   TYR   A CD2 
148  C CD2 B TYR   A 9   ? 0.1954 0.2421 0.2022 -0.0262 0.0167  0.0033  9   TYR   A CD2 
149  C CE1 A TYR   A 9   ? 0.1582 0.2441 0.2062 -0.0385 0.0486  -0.0267 9   TYR   A CE1 
150  C CE1 B TYR   A 9   ? 0.2002 0.2502 0.2206 -0.0286 0.0191  -0.0052 9   TYR   A CE1 
151  C CE2 A TYR   A 9   ? 0.1527 0.2340 0.1806 -0.0288 0.0392  0.0032  9   TYR   A CE2 
152  C CE2 B TYR   A 9   ? 0.1948 0.2434 0.2060 -0.0277 0.0190  -0.0007 9   TYR   A CE2 
153  C CZ  A TYR   A 9   ? 0.1478 0.2397 0.2123 -0.0448 0.0570  -0.0064 9   TYR   A CZ  
154  C CZ  B TYR   A 9   ? 0.1981 0.2471 0.2199 -0.0323 0.0243  -0.0034 9   TYR   A CZ  
155  O OH  A TYR   A 9   ? 0.1525 0.2453 0.2465 -0.0607 0.0589  -0.0059 9   TYR   A OH  
156  O OH  B TYR   A 9   ? 0.2074 0.2498 0.2359 -0.0371 0.0308  -0.0019 9   TYR   A OH  
175  N N   A LEU   A 10  ? 0.1565 0.1736 0.1792 -0.0427 0.0356  0.0144  10  LEU   A N   
176  N N   B LEU   A 10  ? 0.1982 0.2015 0.1827 -0.0141 0.0404  0.0011  10  LEU   A N   
177  C CA  A LEU   A 10  ? 0.1439 0.1624 0.1893 -0.0338 0.0318  0.0360  10  LEU   A CA  
178  C CA  B LEU   A 10  ? 0.1962 0.1998 0.1875 -0.0055 0.0305  -0.0020 10  LEU   A CA  
179  C C   A LEU   A 10  ? 0.1352 0.1504 0.2062 -0.0288 0.0301  0.0364  10  LEU   A C   
180  C C   B LEU   A 10  ? 0.1873 0.1784 0.1845 -0.0050 0.0226  0.0054  10  LEU   A C   
181  O O   A LEU   A 10  ? 0.1365 0.1436 0.2193 -0.0250 0.0477  0.0339  10  LEU   A O   
182  O O   B LEU   A 10  ? 0.1884 0.1740 0.1878 -0.0066 0.0313  0.0117  10  LEU   A O   
183  C CB  A LEU   A 10  ? 0.1399 0.1666 0.2040 -0.0285 0.0215  0.0537  10  LEU   A CB  
184  C CB  B LEU   A 10  ? 0.2051 0.2180 0.2046 -0.0023 0.0225  -0.0076 10  LEU   A CB  
185  C CG  A LEU   A 10  ? 0.1552 0.1748 0.2623 -0.0148 -0.0049 0.0629  10  LEU   A CG  
186  C CG  B LEU   A 10  ? 0.2176 0.2439 0.2341 0.0001  0.0166  -0.0161 10  LEU   A CG  
187  C CD1 A LEU   A 10  ? 0.1649 0.1821 0.3012 -0.0220 -0.0124 0.0610  10  LEU   A CD1 
188  C CD1 B LEU   A 10  ? 0.2206 0.2549 0.2425 0.0024  0.0116  -0.0180 10  LEU   A CD1 
189  C CD2 A LEU   A 10  ? 0.1756 0.2018 0.2675 -0.0095 -0.0011 0.0480  10  LEU   A CD2 
190  C CD2 B LEU   A 10  ? 0.2238 0.2520 0.2450 -0.0001 0.0201  -0.0112 10  LEU   A CD2 
213  N N   A LYS   A 11  ? 0.1319 0.1491 0.2090 -0.0221 0.0379  0.0409  11  LYS   A N   
214  N N   B LYS   A 11  ? 0.1826 0.1677 0.1793 -0.0055 0.0168  0.0155  11  LYS   A N   
215  C CA  A LYS   A 11  ? 0.1375 0.1444 0.2204 -0.0315 0.0329  0.0455  11  LYS   A CA  
216  C CA  B LYS   A 11  ? 0.1770 0.1604 0.1734 -0.0069 0.0140  0.0208  11  LYS   A CA  
217  C C   A LYS   A 11  ? 0.1306 0.1520 0.2136 -0.0264 0.0278  0.0273  11  LYS   A C   
218  C C   B LYS   A 11  ? 0.1631 0.1516 0.1725 -0.0111 0.0112  0.0178  11  LYS   A C   
219  O O   A LYS   A 11  ? 0.1338 0.1788 0.2621 -0.0467 0.0360  0.0134  11  LYS   A O   
220  O O   B LYS   A 11  ? 0.1577 0.1470 0.1843 -0.0108 0.0053  0.0042  11  LYS   A O   
221  C CB  A LYS   A 11  ? 0.1437 0.1440 0.2279 -0.0286 0.0263  0.0369  11  LYS   A CB  
222  C CB  B LYS   A 11  ? 0.1863 0.1570 0.1773 -0.0076 0.0111  0.0187  11  LYS   A CB  
223  C CG  A LYS   A 11  ? 0.1563 0.1488 0.2305 -0.0282 0.0221  0.0352  11  LYS   A CG  
224  C CG  B LYS   A 11  ? 0.1901 0.1614 0.1846 -0.0044 0.0155  0.0313  11  LYS   A CG  
225  C CD  A LYS   A 11  ? 0.1604 0.1573 0.2196 -0.0298 0.0122  0.0359  11  LYS   A CD  
226  C CD  B LYS   A 11  ? 0.1942 0.1704 0.1920 -0.0023 0.0209  0.0369  11  LYS   A CD  
227  C CE  A LYS   A 11  ? 0.1712 0.1603 0.2152 -0.0190 0.0095  0.0413  11  LYS   A CE  
228  C CE  B LYS   A 11  ? 0.1963 0.1729 0.1930 -0.0054 0.0268  0.0413  11  LYS   A CE  
229  N NZ  A LYS   A 11  ? 0.1717 0.1519 0.2152 0.0046  0.0117  0.0219  11  LYS   A NZ  
230  N NZ  B LYS   A 11  ? 0.1971 0.1744 0.1948 -0.0076 0.0328  0.0345  11  LYS   A NZ  
257  N N   A LEU   A 12  ? 0.1294 0.1393 0.1933 -0.0254 0.0268  0.0223  12  LEU   A N   
258  N N   B LEU   A 12  ? 0.1589 0.1603 0.1839 0.0030  0.0126  0.0116  12  LEU   A N   
259  C CA  A LEU   A 12  ? 0.1374 0.1461 0.1858 -0.0243 0.0170  0.0348  12  LEU   A CA  
260  C CA  B LEU   A 12  ? 0.1533 0.1666 0.1867 0.0079  0.0198  0.0187  12  LEU   A CA  
261  C C   A LEU   A 12  ? 0.1383 0.1405 0.1857 -0.0294 0.0148  0.0316  12  LEU   A C   
262  C C   B LEU   A 12  ? 0.1455 0.1644 0.1831 0.0063  0.0313  0.0154  12  LEU   A C   
263  O O   A LEU   A 12  ? 0.1385 0.1430 0.1892 -0.0218 0.0220  0.0068  12  LEU   A O   
264  O O   B LEU   A 12  ? 0.1529 0.1658 0.1869 0.0112  0.0240  0.0099  12  LEU   A O   
265  C CB  A LEU   A 12  ? 0.1488 0.1440 0.2015 -0.0230 0.0040  0.0353  12  LEU   A CB  
266  C CB  B LEU   A 12  ? 0.1620 0.1754 0.2119 0.0097  0.0263  0.0243  12  LEU   A CB  
267  C CG  A LEU   A 12  ? 0.1553 0.1583 0.2264 -0.0133 0.0155  0.0516  12  LEU   A CG  
268  C CG  B LEU   A 12  ? 0.1618 0.1794 0.2347 0.0064  0.0363  0.0298  12  LEU   A CG  
269  C CD1 A LEU   A 12  ? 0.1733 0.1617 0.2353 0.0027  0.0291  0.0534  12  LEU   A CD1 
270  C CD1 B LEU   A 12  ? 0.1673 0.1827 0.2400 0.0026  0.0412  0.0228  12  LEU   A CD1 
271  C CD2 A LEU   A 12  ? 0.1602 0.1802 0.2503 -0.0138 0.0023  0.0581  12  LEU   A CD2 
272  C CD2 B LEU   A 12  ? 0.1632 0.1871 0.2523 0.0028  0.0332  0.0368  12  LEU   A CD2 
295  N N   A THR   A 13  ? 0.1385 0.1341 0.2103 -0.0271 0.0053  0.0190  13  THR   A N   
296  N N   B THR   A 13  ? 0.1410 0.1584 0.1884 0.0017  0.0265  0.0150  13  THR   A N   
297  C CA  A THR   A 13  ? 0.1410 0.1411 0.2176 -0.0206 0.0158  0.0170  13  THR   A CA  
298  C CA  B THR   A 13  ? 0.1442 0.1596 0.1943 -0.0089 0.0242  0.0210  13  THR   A CA  
299  C C   A THR   A 13  ? 0.1400 0.1387 0.2258 -0.0269 0.0110  0.0243  13  THR   A C   
300  C C   B THR   A 13  ? 0.1484 0.1687 0.2069 -0.0204 0.0195  0.0250  13  THR   A C   
301  O O   A THR   A 13  ? 0.1412 0.1372 0.2373 -0.0167 0.0124  0.0334  13  THR   A O   
302  O O   B THR   A 13  ? 0.1541 0.1751 0.2172 -0.0233 0.0104  0.0294  13  THR   A O   
303  C CB  A THR   A 13  ? 0.1407 0.1593 0.2402 -0.0159 0.0090  0.0294  13  THR   A CB  
304  C CB  B THR   A 13  ? 0.1392 0.1641 0.1994 -0.0051 0.0277  0.0197  13  THR   A CB  
305  O OG1 A THR   A 13  ? 0.1481 0.1571 0.2580 -0.0194 0.0014  0.0388  13  THR   A OG1 
306  O OG1 B THR   A 13  ? 0.1308 0.1678 0.2031 -0.0112 0.0382  0.0283  13  THR   A OG1 
307  C CG2 A THR   A 13  ? 0.1450 0.1768 0.2477 -0.0169 0.0135  0.0145  13  THR   A CG2 
308  C CG2 B THR   A 13  ? 0.1414 0.1662 0.2022 0.0065  0.0287  0.0145  13  THR   A CG2 
323  N N   A ASP   A 14  ? 0.1493 0.1439 0.2347 -0.0273 0.0047  0.0312  14  ASP   A N   
324  N N   B ASP   A 14  ? 0.1529 0.1746 0.2228 -0.0215 0.0118  0.0276  14  ASP   A N   
325  C CA  A ASP   A 14  ? 0.1550 0.1638 0.2459 -0.0228 -0.0035 0.0565  14  ASP   A CA  
326  C CA  B ASP   A 14  ? 0.1623 0.1788 0.2378 -0.0218 0.0069  0.0420  14  ASP   A CA  
327  C C   A ASP   A 14  ? 0.1580 0.1676 0.2160 -0.0253 -0.0141 0.0608  14  ASP   A C   
328  C C   B ASP   A 14  ? 0.1554 0.1671 0.2252 -0.0242 -0.0016 0.0569  14  ASP   A C   
329  O O   A ASP   A 14  ? 0.1698 0.1829 0.2166 -0.0285 -0.0129 0.0522  14  ASP   A O   
330  O O   B ASP   A 14  ? 0.1533 0.1643 0.2279 -0.0235 -0.0063 0.0698  14  ASP   A O   
331  C CB  A ASP   A 14  ? 0.1742 0.1962 0.3054 -0.0222 -0.0003 0.0787  14  ASP   A CB  
332  C CB  B ASP   A 14  ? 0.1811 0.1965 0.2693 -0.0170 0.0057  0.0458  14  ASP   A CB  
333  C CG  A ASP   A 14  ? 0.1927 0.2444 0.3729 -0.0251 -0.0065 0.0837  14  ASP   A CG  
334  C CG  B ASP   A 14  ? 0.1912 0.2237 0.2982 -0.0154 0.0132  0.0482  14  ASP   A CG  
335  O OD1 A ASP   A 14  ? 0.1995 0.2669 0.3923 -0.0042 -0.0345 0.0910  14  ASP   A OD1 
336  O OD1 B ASP   A 14  ? 0.1946 0.2353 0.3133 -0.0116 0.0172  0.0532  14  ASP   A OD1 
337  O OD2 A ASP   A 14  ? 0.2055 0.2656 0.4011 -0.0359 -0.0083 0.0699  14  ASP   A OD2 
338  O OD2 B ASP   A 14  ? 0.1945 0.2319 0.3169 -0.0199 0.0102  0.0452  14  ASP   A OD2 
347  N N   . ASN   A 15  ? 0.1516 0.1568 0.2233 -0.0322 -0.0012 0.0574  15  ASN   A N   
348  C CA  . ASN   A 15  ? 0.1506 0.1676 0.2388 -0.0241 -0.0143 0.0442  15  ASN   A CA  
349  C C   . ASN   A 15  ? 0.1459 0.1650 0.2506 -0.0283 -0.0019 0.0499  15  ASN   A C   
350  O O   . ASN   A 15  ? 0.1477 0.1655 0.2997 -0.0260 -0.0207 0.0573  15  ASN   A O   
351  C CB  . ASN   A 15  ? 0.1483 0.1705 0.2340 -0.0197 -0.0087 0.0385  15  ASN   A CB  
352  C CG  . ASN   A 15  ? 0.1458 0.1701 0.2388 -0.0161 -0.0019 0.0330  15  ASN   A CG  
353  O OD1 . ASN   A 15  ? 0.1555 0.1775 0.2609 -0.0316 -0.0022 0.0375  15  ASN   A OD1 
354  N ND2 . ASN   A 15  ? 0.1438 0.1760 0.2307 -0.0220 0.0062  0.0325  15  ASN   A ND2 
362  N N   A VAL   A 16  ? 0.1420 0.1612 0.2379 -0.0221 0.0003  0.0549  16  VAL   A N   
363  N N   B VAL   A 16  ? 0.1501 0.1657 0.2228 -0.0231 0.0046  0.0459  16  VAL   A N   
364  C CA  A VAL   A 16  ? 0.1350 0.1594 0.2380 -0.0192 -0.0009 0.0503  16  VAL   A CA  
365  C CA  B VAL   A 16  ? 0.1529 0.1672 0.2064 -0.0200 0.0081  0.0381  16  VAL   A CA  
366  C C   A VAL   A 16  ? 0.1241 0.1597 0.2459 -0.0275 -0.0091 0.0452  16  VAL   A C   
367  C C   B VAL   A 16  ? 0.1530 0.1670 0.1960 -0.0183 0.0060  0.0372  16  VAL   A C   
368  O O   A VAL   A 16  ? 0.1187 0.1611 0.2650 -0.0331 0.0051  0.0390  16  VAL   A O   
369  O O   B VAL   A 16  ? 0.1535 0.1673 0.2011 -0.0156 0.0121  0.0408  16  VAL   A O   
370  C CB  A VAL   A 16  ? 0.1460 0.1689 0.2302 -0.0018 0.0158  0.0546  16  VAL   A CB  
371  C CB  B VAL   A 16  ? 0.1588 0.1742 0.2062 -0.0153 0.0177  0.0387  16  VAL   A CB  
372  C CG1 A VAL   A 16  ? 0.1598 0.1803 0.2298 0.0034  0.0174  0.0518  16  VAL   A CG1 
373  C CG1 B VAL   A 16  ? 0.1638 0.1795 0.2082 -0.0158 0.0168  0.0342  16  VAL   A CG1 
374  C CG2 A VAL   A 16  ? 0.1538 0.1800 0.2442 0.0036  0.0274  0.0521  16  VAL   A CG2 
375  C CG2 B VAL   A 16  ? 0.1596 0.1782 0.2126 -0.0170 0.0237  0.0329  16  VAL   A CG2 
394  N N   A TYR   A 17  ? 0.1245 0.1570 0.2323 -0.0264 0.0010  0.0516  17  TYR   A N   
395  N N   B TYR   A 17  ? 0.1520 0.1666 0.1843 -0.0176 0.0112  0.0333  17  TYR   A N   
396  C CA  A TYR   A 17  ? 0.1335 0.1678 0.2131 -0.0306 0.0055  0.0559  17  TYR   A CA  
397  C CA  B TYR   A 17  ? 0.1547 0.1745 0.1741 -0.0238 0.0161  0.0293  17  TYR   A CA  
398  C C   A TYR   A 17  ? 0.1341 0.1659 0.2211 -0.0240 0.0044  0.0521  17  TYR   A C   
399  C C   B TYR   A 17  ? 0.1551 0.1666 0.1731 -0.0293 0.0166  0.0165  17  TYR   A C   
400  O O   A TYR   A 17  ? 0.1284 0.1603 0.2122 -0.0267 0.0037  0.0615  17  TYR   A O   
401  O O   B TYR   A 17  ? 0.1503 0.1454 0.1830 -0.0382 0.0170  0.0149  17  TYR   A O   
402  C CB  A TYR   A 17  ? 0.1542 0.1691 0.2221 -0.0424 -0.0093 0.0469  17  TYR   A CB  
403  C CB  B TYR   A 17  ? 0.1629 0.1888 0.1915 -0.0181 0.0084  0.0278  17  TYR   A CB  
404  C CG  A TYR   A 17  ? 0.1696 0.1748 0.2203 -0.0518 -0.0240 0.0396  17  TYR   A CG  
405  C CG  B TYR   A 17  ? 0.1712 0.2061 0.2088 -0.0139 0.0040  0.0278  17  TYR   A CG  
406  C CD1 A TYR   A 17  ? 0.1798 0.1806 0.2317 -0.0446 -0.0282 0.0360  17  TYR   A CD1 
407  C CD1 B TYR   A 17  ? 0.1801 0.2159 0.2249 -0.0058 -0.0014 0.0280  17  TYR   A CD1 
408  C CD2 A TYR   A 17  ? 0.1811 0.1763 0.2076 -0.0617 -0.0253 0.0506  17  TYR   A CD2 
409  C CD2 B TYR   A 17  ? 0.1767 0.2171 0.2169 -0.0138 0.0024  0.0331  17  TYR   A CD2 
410  C CE1 A TYR   A 17  ? 0.1855 0.1808 0.2191 -0.0456 -0.0297 0.0406  17  TYR   A CE1 
411  C CE1 B TYR   A 17  ? 0.1880 0.2248 0.2347 -0.0025 -0.0018 0.0320  17  TYR   A CE1 
412  C CE2 A TYR   A 17  ? 0.1879 0.1786 0.2040 -0.0559 -0.0358 0.0383  17  TYR   A CE2 
413  C CE2 B TYR   A 17  ? 0.1847 0.2263 0.2292 -0.0073 0.0061  0.0328  17  TYR   A CE2 
414  C CZ  A TYR   A 17  ? 0.1900 0.1765 0.2047 -0.0476 -0.0367 0.0474  17  TYR   A CZ  
415  C CZ  B TYR   A 17  ? 0.1903 0.2305 0.2408 -0.0030 -0.0005 0.0328  17  TYR   A CZ  
416  O OH  A TYR   A 17  ? 0.1959 0.1728 0.2071 -0.0433 -0.0401 0.0412  17  TYR   A OH  
417  O OH  B TYR   A 17  ? 0.1971 0.2369 0.2556 -0.0016 -0.0060 0.0313  17  TYR   A OH  
436  N N   A ILE   A 18  ? 0.1315 0.1592 0.2057 -0.0339 -0.0025 0.0508  18  ILE   A N   
437  N N   B ILE   A 18  ? 0.1542 0.1747 0.1544 -0.0386 0.0144  0.0111  18  ILE   A N   
438  C CA  A ILE   A 18  ? 0.1382 0.1557 0.1985 -0.0277 0.0149  0.0398  18  ILE   A CA  
439  C CA  B ILE   A 18  ? 0.1537 0.1830 0.1411 -0.0290 0.0158  0.0051  18  ILE   A CA  
440  C C   A ILE   A 18  ? 0.1367 0.1661 0.1925 -0.0326 0.0118  0.0410  18  ILE   A C   
441  C C   B ILE   A 18  ? 0.1511 0.2048 0.1198 -0.0271 -0.0044 0.0058  18  ILE   A C   
442  O O   A ILE   A 18  ? 0.1269 0.1813 0.1925 -0.0385 0.0130  0.0469  18  ILE   A O   
443  O O   B ILE   A 18  ? 0.1514 0.2157 0.1326 -0.0331 -0.0077 0.0116  18  ILE   A O   
444  C CB  A ILE   A 18  ? 0.1477 0.1504 0.1925 -0.0112 0.0231  0.0428  18  ILE   A CB  
445  C CB  B ILE   A 18  ? 0.1520 0.1690 0.1302 -0.0220 0.0235  0.0075  18  ILE   A CB  
446  C CG1 A ILE   A 18  ? 0.1621 0.1541 0.1889 0.0053  0.0048  0.0482  18  ILE   A CG1 
447  C CG1 B ILE   A 18  ? 0.1589 0.1648 0.1292 -0.0237 0.0247  0.0055  18  ILE   A CG1 
448  C CG2 A ILE   A 18  ? 0.1467 0.1460 0.1968 -0.0088 0.0247  0.0200  18  ILE   A CG2 
449  C CG2 B ILE   A 18  ? 0.1553 0.1732 0.1424 -0.0247 0.0156  0.0077  18  ILE   A CG2 
450  C CD1 A ILE   A 18  ? 0.1854 0.1675 0.1936 0.0215  0.0019  0.0532  18  ILE   A CD1 
451  C CD1 B ILE   A 18  ? 0.1654 0.1685 0.1397 -0.0219 0.0299  -0.0047 18  ILE   A CD1 
474  N N   A LYS   A 19  ? 0.1358 0.1650 0.1783 -0.0268 0.0292  0.0328  19  LYS   A N   
475  N N   B LYS   A 19  ? 0.1557 0.2158 0.1219 -0.0195 -0.0025 -0.0040 19  LYS   A N   
476  C CA  A LYS   A 19  ? 0.1485 0.1821 0.1860 -0.0268 0.0373  0.0316  19  LYS   A CA  
477  C CA  B LYS   A 19  ? 0.1662 0.2297 0.1377 -0.0110 0.0014  -0.0087 19  LYS   A CA  
478  C C   A LYS   A 19  ? 0.1366 0.1736 0.1984 -0.0105 0.0378  0.0414  19  LYS   A C   
479  C C   B LYS   A 19  ? 0.1699 0.2319 0.1413 0.0002  0.0124  -0.0057 19  LYS   A C   
480  O O   A LYS   A 19  ? 0.1295 0.1674 0.2027 -0.0116 0.0324  0.0439  19  LYS   A O   
481  O O   B LYS   A 19  ? 0.1694 0.2249 0.1296 -0.0042 0.0140  0.0014  19  LYS   A O   
482  C CB  A LYS   A 19  ? 0.1656 0.2006 0.1880 -0.0364 0.0392  0.0230  19  LYS   A CB  
483  C CB  B LYS   A 19  ? 0.1693 0.2380 0.1556 -0.0108 0.0051  -0.0150 19  LYS   A CB  
484  C CG  A LYS   A 19  ? 0.1926 0.2265 0.2009 -0.0354 0.0310  0.0022  19  LYS   A CG  
485  C CG  B LYS   A 19  ? 0.1814 0.2478 0.1704 -0.0076 0.0060  -0.0165 19  LYS   A CG  
486  C CD  A LYS   A 19  ? 0.2192 0.2479 0.2174 -0.0364 0.0217  -0.0084 19  LYS   A CD  
487  C CD  B LYS   A 19  ? 0.1937 0.2570 0.1830 -0.0077 0.0062  -0.0153 19  LYS   A CD  
488  C CE  A LYS   A 19  ? 0.2436 0.2628 0.2281 -0.0395 0.0182  -0.0084 19  LYS   A CE  
489  C CE  B LYS   A 19  ? 0.2011 0.2625 0.1942 -0.0096 0.0007  -0.0131 19  LYS   A CE  
490  N NZ  A LYS   A 19  ? 0.2534 0.2693 0.2265 -0.0513 0.0232  -0.0140 19  LYS   A NZ  
491  N NZ  B LYS   A 19  ? 0.2075 0.2654 0.1944 -0.0136 0.0031  -0.0118 19  LYS   A NZ  
518  N N   A ASN   A 20  ? 0.1391 0.1835 0.2306 -0.0127 0.0417  0.0558  20  ASN   A N   
519  N N   B ASN   A 20  ? 0.1860 0.2436 0.1656 0.0106  0.0219  -0.0135 20  ASN   A N   
520  C CA  A ASN   A 20  ? 0.1553 0.2075 0.2546 0.0141  0.0544  0.0443  20  ASN   A CA  
521  C CA  B ASN   A 20  ? 0.2008 0.2573 0.1927 0.0180  0.0312  -0.0169 20  ASN   A CA  
522  C C   A ASN   A 20  ? 0.1773 0.2131 0.2605 0.0068  0.0729  0.0269  20  ASN   A C   
523  C C   B ASN   A 20  ? 0.2081 0.2504 0.2032 0.0162  0.0326  -0.0249 20  ASN   A C   
524  O O   A ASN   A 20  ? 0.2073 0.2324 0.2774 -0.0167 0.0808  0.0115  20  ASN   A O   
525  O O   B ASN   A 20  ? 0.2192 0.2566 0.2013 0.0052  0.0345  -0.0289 20  ASN   A O   
526  C CB  A ASN   A 20  ? 0.1609 0.2246 0.2702 0.0248  0.0552  0.0633  20  ASN   A CB  
527  C CB  B ASN   A 20  ? 0.2113 0.2734 0.2119 0.0234  0.0395  -0.0088 20  ASN   A CB  
528  C CG  A ASN   A 20  ? 0.1691 0.2368 0.3014 0.0492  0.0602  0.0770  20  ASN   A CG  
529  C CG  B ASN   A 20  ? 0.2228 0.2867 0.2226 0.0328  0.0506  0.0024  20  ASN   A CG  
530  O OD1 A ASN   A 20  ? 0.1961 0.2418 0.3310 0.0642  0.0836  0.0733  20  ASN   A OD1 
531  O OD1 B ASN   A 20  ? 0.2343 0.2936 0.2312 0.0428  0.0476  0.0117  20  ASN   A OD1 
532  N ND2 A ASN   A 20  ? 0.1732 0.2379 0.3072 0.0511  0.0578  0.0898  20  ASN   A ND2 
533  N ND2 B ASN   A 20  ? 0.2280 0.2888 0.2275 0.0325  0.0548  0.0016  20  ASN   A ND2 
546  N N   A ALA   A 21  ? 0.1713 0.2055 0.2540 0.0078  0.0661  0.0112  21  ALA   A N   
547  N N   B ALA   A 21  ? 0.2087 0.2411 0.2187 0.0172  0.0261  -0.0263 21  ALA   A N   
548  C CA  A ALA   A 21  ? 0.1773 0.1996 0.2481 -0.0001 0.0570  0.0211  21  ALA   A CA  
549  C CA  B ALA   A 21  ? 0.2110 0.2337 0.2296 0.0148  0.0229  -0.0228 21  ALA   A CA  
550  C C   A ALA   A 21  ? 0.1664 0.1971 0.2553 -0.0054 0.0437  0.0314  21  ALA   A C   
551  C C   B ALA   A 21  ? 0.2032 0.2228 0.2270 0.0144  0.0361  -0.0164 21  ALA   A C   
552  O O   A ALA   A 21  ? 0.1659 0.1993 0.2565 -0.0007 0.0367  0.0398  21  ALA   A O   
553  O O   B ALA   A 21  ? 0.2011 0.2170 0.2101 0.0182  0.0531  -0.0109 21  ALA   A O   
554  C CB  A ALA   A 21  ? 0.1995 0.2081 0.2520 -0.0094 0.0526  0.0222  21  ALA   A CB  
555  C CB  B ALA   A 21  ? 0.2233 0.2382 0.2414 0.0127  0.0212  -0.0261 21  ALA   A CB  
566  N N   A ASP   A 22  ? 0.1712 0.1982 0.2786 -0.0102 0.0374  0.0283  22  ASP   A N   
567  N N   B ASP   A 22  ? 0.1985 0.2166 0.2397 0.0080  0.0334  -0.0124 22  ASP   A N   
568  C CA  A ASP   A 22  ? 0.1718 0.1925 0.2758 -0.0020 0.0387  0.0351  22  ASP   A CA  
569  C CA  B ASP   A 22  ? 0.1945 0.2117 0.2416 0.0036  0.0363  -0.0074 22  ASP   A CA  
570  C C   A ASP   A 22  ? 0.1640 0.1927 0.2464 -0.0007 0.0483  0.0379  22  ASP   A C   
571  C C   B ASP   A 22  ? 0.1784 0.1964 0.2159 -0.0097 0.0364  0.0018  22  ASP   A C   
572  O O   A ASP   A 22  ? 0.1705 0.1987 0.2532 -0.0008 0.0450  0.0444  22  ASP   A O   
573  O O   B ASP   A 22  ? 0.1745 0.1926 0.2101 -0.0155 0.0454  0.0008  22  ASP   A O   
574  C CB  A ASP   A 22  ? 0.1958 0.1979 0.3141 0.0068  0.0377  0.0188  22  ASP   A CB  
575  C CB  B ASP   A 22  ? 0.2073 0.2199 0.2696 0.0142  0.0468  -0.0105 22  ASP   A CB  
576  C CG  A ASP   A 22  ? 0.2123 0.2041 0.3472 0.0010  0.0278  0.0217  22  ASP   A CG  
577  C CG  B ASP   A 22  ? 0.2206 0.2221 0.2933 0.0164  0.0569  -0.0080 22  ASP   A CG  
578  O OD1 A ASP   A 22  ? 0.2025 0.2036 0.3695 -0.0169 0.0147  0.0397  22  ASP   A OD1 
579  O OD1 B ASP   A 22  ? 0.2218 0.2155 0.2913 0.0146  0.0611  -0.0084 22  ASP   A OD1 
580  O OD2 A ASP   A 22  ? 0.2402 0.2160 0.3693 0.0100  0.0358  -0.0083 22  ASP   A OD2 
581  O OD2 B ASP   A 22  ? 0.2294 0.2335 0.3118 0.0151  0.0623  -0.0047 22  ASP   A OD2 
590  N N   A ILE   A 23  ? 0.1631 0.1871 0.2275 -0.0008 0.0453  0.0301  23  ILE   A N   
591  N N   B ILE   A 23  ? 0.1712 0.1867 0.2006 -0.0099 0.0286  0.0053  23  ILE   A N   
592  C CA  A ILE   A 23  ? 0.1638 0.1769 0.2072 -0.0061 0.0345  0.0280  23  ILE   A CA  
593  C CA  B ILE   A 23  ? 0.1621 0.1829 0.1862 -0.0108 0.0217  0.0051  23  ILE   A CA  
594  C C   A ILE   A 23  ? 0.1628 0.1840 0.2036 -0.0042 0.0553  0.0236  23  ILE   A C   
595  C C   B ILE   A 23  ? 0.1595 0.1876 0.1897 -0.0222 0.0338  -0.0066 23  ILE   A C   
596  O O   A ILE   A 23  ? 0.1766 0.1848 0.2025 0.0010  0.0412  0.0166  23  ILE   A O   
597  O O   B ILE   A 23  ? 0.1584 0.1824 0.1815 -0.0251 0.0369  -0.0119 23  ILE   A O   
598  C CB  A ILE   A 23  ? 0.1691 0.1719 0.1763 0.0002  0.0240  0.0261  23  ILE   A CB  
599  C CB  B ILE   A 23  ? 0.1635 0.1716 0.1689 -0.0018 0.0177  0.0077  23  ILE   A CB  
600  C CG1 A ILE   A 23  ? 0.1765 0.1781 0.1662 -0.0020 0.0239  0.0173  23  ILE   A CG1 
601  C CG1 B ILE   A 23  ? 0.1595 0.1660 0.1571 0.0002  0.0116  0.0021  23  ILE   A CG1 
602  C CG2 A ILE   A 23  ? 0.1753 0.1683 0.1655 0.0089  0.0252  0.0241  23  ILE   A CG2 
603  C CG2 B ILE   A 23  ? 0.1684 0.1706 0.1776 0.0048  0.0131  0.0056  23  ILE   A CG2 
604  C CD1 A ILE   A 23  ? 0.1822 0.1809 0.1688 -0.0051 0.0137  0.0082  23  ILE   A CD1 
605  C CD1 B ILE   A 23  ? 0.1512 0.1645 0.1567 0.0058  -0.0017 -0.0085 23  ILE   A CD1 
628  N N   A VAL   A 24  ? 0.1679 0.1903 0.2178 -0.0064 0.0536  0.0132  24  VAL   A N   
629  N N   B VAL   A 24  ? 0.1683 0.1976 0.2084 -0.0285 0.0353  -0.0112 24  VAL   A N   
630  C CA  A VAL   A 24  ? 0.1857 0.2007 0.2401 -0.0134 0.0465  0.0049  24  VAL   A CA  
631  C CA  B VAL   A 24  ? 0.1831 0.2088 0.2262 -0.0297 0.0359  -0.0091 24  VAL   A CA  
632  C C   A VAL   A 24  ? 0.1960 0.2180 0.2409 -0.0216 0.0452  -0.0016 24  VAL   A C   
633  C C   B VAL   A 24  ? 0.1882 0.2229 0.2278 -0.0320 0.0508  -0.0213 24  VAL   A C   
634  O O   A VAL   A 24  ? 0.2102 0.2236 0.2405 -0.0205 0.0483  -0.0038 24  VAL   A O   
635  O O   B VAL   A 24  ? 0.1912 0.2264 0.2284 -0.0274 0.0559  -0.0249 24  VAL   A O   
636  C CB  A VAL   A 24  ? 0.1943 0.2009 0.2641 -0.0120 0.0500  0.0079  24  VAL   A CB  
637  C CB  B VAL   A 24  ? 0.1905 0.2102 0.2451 -0.0276 0.0287  0.0037  24  VAL   A CB  
638  C CG1 A VAL   A 24  ? 0.1945 0.2069 0.2743 -0.0035 0.0569  -0.0091 24  VAL   A CG1 
639  C CG1 B VAL   A 24  ? 0.1994 0.2145 0.2604 -0.0219 0.0217  0.0053  24  VAL   A CG1 
640  C CG2 A VAL   A 24  ? 0.2066 0.2053 0.2764 -0.0112 0.0650  0.0232  24  VAL   A CG2 
641  C CG2 B VAL   A 24  ? 0.1934 0.2086 0.2446 -0.0328 0.0296  0.0083  24  VAL   A CG2 
660  N N   A GLU   A 25  ? 0.2023 0.2388 0.2496 -0.0297 0.0532  -0.0129 25  GLU   A N   
661  N N   B GLU   A 25  ? 0.1908 0.2322 0.2275 -0.0364 0.0700  -0.0307 25  GLU   A N   
662  C CA  A GLU   A 25  ? 0.2247 0.2629 0.2519 -0.0262 0.0618  -0.0167 25  GLU   A CA  
663  C CA  B GLU   A 25  ? 0.2032 0.2439 0.2389 -0.0458 0.0806  -0.0302 25  GLU   A CA  
664  C C   A GLU   A 25  ? 0.2138 0.2690 0.2123 -0.0349 0.0675  -0.0207 25  GLU   A C   
665  C C   B GLU   A 25  ? 0.2000 0.2448 0.2174 -0.0475 0.0861  -0.0369 25  GLU   A C   
666  O O   A GLU   A 25  ? 0.2220 0.2764 0.2253 -0.0285 0.0661  -0.0281 25  GLU   A O   
667  O O   B GLU   A 25  ? 0.2020 0.2482 0.2194 -0.0441 0.0865  -0.0422 25  GLU   A O   
668  C CB  A GLU   A 25  ? 0.2526 0.2850 0.2869 -0.0260 0.0626  -0.0073 25  GLU   A CB  
669  C CB  B GLU   A 25  ? 0.2165 0.2511 0.2588 -0.0481 0.0868  -0.0209 25  GLU   A CB  
670  C CG  A GLU   A 25  ? 0.2843 0.3082 0.3458 -0.0279 0.0493  -0.0069 25  GLU   A CG  
671  C CG  B GLU   A 25  ? 0.2360 0.2591 0.2937 -0.0483 0.0798  -0.0122 25  GLU   A CG  
672  C CD  A GLU   A 25  ? 0.3058 0.3276 0.3985 -0.0312 0.0409  -0.0004 25  GLU   A CD  
673  C CD  B GLU   A 25  ? 0.2500 0.2644 0.3265 -0.0494 0.0685  -0.0019 25  GLU   A CD  
674  O OE1 A GLU   A 25  ? 0.3149 0.3352 0.4075 -0.0303 0.0290  -0.0025 25  GLU   A OE1 
675  O OE1 B GLU   A 25  ? 0.2551 0.2627 0.3320 -0.0487 0.0667  0.0015  25  GLU   A OE1 
676  O OE2 A GLU   A 25  ? 0.3089 0.3349 0.4296 -0.0363 0.0418  -0.0031 25  GLU   A OE2 
677  O OE2 B GLU   A 25  ? 0.2570 0.2694 0.3442 -0.0475 0.0693  0.0059  25  GLU   A OE2 
690  N N   A GLU   A 26  ? 0.2045 0.2697 0.2135 -0.0553 0.0683  -0.0265 26  GLU   A N   
691  N N   B GLU   A 26  ? 0.1986 0.2417 0.2156 -0.0528 0.0826  -0.0446 26  GLU   A N   
692  C CA  A GLU   A 26  ? 0.2087 0.2732 0.2026 -0.0700 0.0656  -0.0235 26  GLU   A CA  
693  C CA  B GLU   A 26  ? 0.2072 0.2395 0.2183 -0.0522 0.0825  -0.0419 26  GLU   A CA  
694  C C   A GLU   A 26  ? 0.2105 0.2659 0.1774 -0.0667 0.0600  -0.0264 26  GLU   A C   
695  C C   B GLU   A 26  ? 0.2049 0.2464 0.2018 -0.0562 0.0719  -0.0407 26  GLU   A C   
696  O O   A GLU   A 26  ? 0.2155 0.2662 0.1616 -0.0746 0.0594  -0.0267 26  GLU   A O   
697  O O   B GLU   A 26  ? 0.2031 0.2414 0.1995 -0.0514 0.0833  -0.0532 26  GLU   A O   
698  C CB  A GLU   A 26  ? 0.2247 0.2832 0.2333 -0.0746 0.0577  -0.0213 26  GLU   A CB  
699  C CB  B GLU   A 26  ? 0.2221 0.2308 0.2416 -0.0458 0.0733  -0.0482 26  GLU   A CB  
700  C CG  A GLU   A 26  ? 0.2463 0.3028 0.3050 -0.0762 0.0550  -0.0210 26  GLU   A CG  
701  C CG  B GLU   A 26  ? 0.2314 0.2105 0.2435 -0.0489 0.0884  -0.0432 26  GLU   A CG  
702  C CD  A GLU   A 26  ? 0.2561 0.3222 0.3553 -0.0796 0.0663  -0.0139 26  GLU   A CD  
703  C CD  B GLU   A 26  ? 0.2345 0.1890 0.2375 -0.0589 0.1100  -0.0422 26  GLU   A CD  
704  O OE1 A GLU   A 26  ? 0.2624 0.3352 0.3624 -0.0783 0.0698  -0.0242 26  GLU   A OE1 
705  O OE1 B GLU   A 26  ? 0.2332 0.1729 0.2436 -0.0707 0.1235  -0.0521 26  GLU   A OE1 
706  O OE2 A GLU   A 26  ? 0.2704 0.3332 0.3911 -0.0765 0.0625  -0.0071 26  GLU   A OE2 
707  O OE2 B GLU   A 26  ? 0.2387 0.1896 0.2164 -0.0472 0.1310  -0.0415 26  GLU   A OE2 
720  N N   . ALA   A 27  ? 0.1988 0.2567 0.1926 -0.0666 0.0570  -0.0223 27  ALA   A N   
721  C CA  . ALA   A 27  ? 0.2038 0.2657 0.1752 -0.0577 0.0526  -0.0243 27  ALA   A CA  
722  C C   . ALA   A 27  ? 0.2460 0.2936 0.1888 -0.0655 0.0561  -0.0341 27  ALA   A C   
723  O O   . ALA   A 27  ? 0.2458 0.2845 0.1917 -0.0709 0.0489  -0.0257 27  ALA   A O   
724  C CB  . ALA   A 27  ? 0.1811 0.2512 0.1909 -0.0608 0.0417  -0.0187 27  ALA   A CB  
731  N N   A LYS   A 28  ? 0.2749 0.3134 0.1982 -0.0611 0.0480  -0.0619 28  LYS   A N   
732  N N   B LYS   A 28  ? 0.2751 0.3188 0.2136 -0.0613 0.0535  -0.0416 28  LYS   A N   
733  C CA  A LYS   A 28  ? 0.3111 0.3439 0.2444 -0.0508 0.0415  -0.0753 28  LYS   A CA  
734  C CA  B LYS   A 28  ? 0.3067 0.3481 0.2544 -0.0547 0.0495  -0.0459 28  LYS   A CA  
735  C C   A LYS   A 28  ? 0.3262 0.3700 0.2391 -0.0586 0.0515  -0.0590 28  LYS   A C   
736  C C   B LYS   A 28  ? 0.3232 0.3701 0.2457 -0.0605 0.0597  -0.0420 28  LYS   A C   
737  O O   A LYS   A 28  ? 0.3306 0.3791 0.2772 -0.0624 0.0340  -0.0535 28  LYS   A O   
738  O O   B LYS   A 28  ? 0.3271 0.3751 0.2680 -0.0623 0.0500  -0.0388 28  LYS   A O   
739  C CB  A LYS   A 28  ? 0.3316 0.3560 0.2995 -0.0306 0.0346  -0.0894 28  LYS   A CB  
740  C CB  B LYS   A 28  ? 0.3210 0.3581 0.3013 -0.0415 0.0399  -0.0486 28  LYS   A CB  
741  C CG  A LYS   A 28  ? 0.3489 0.3668 0.3570 -0.0161 0.0287  -0.0927 28  LYS   A CG  
742  C CG  B LYS   A 28  ? 0.3336 0.3662 0.3464 -0.0308 0.0320  -0.0479 28  LYS   A CG  
743  C CD  A LYS   A 28  ? 0.3651 0.3816 0.4188 -0.0063 0.0201  -0.0876 28  LYS   A CD  
744  C CD  B LYS   A 28  ? 0.3452 0.3756 0.3906 -0.0225 0.0237  -0.0442 28  LYS   A CD  
745  C CE  A LYS   A 28  ? 0.3764 0.3906 0.4620 -0.0011 0.0135  -0.0877 28  LYS   A CE  
746  C CE  B LYS   A 28  ? 0.3535 0.3813 0.4220 -0.0180 0.0180  -0.0433 28  LYS   A CE  
747  N NZ  A LYS   A 28  ? 0.3836 0.3961 0.4917 0.0027  0.0121  -0.0874 28  LYS   A NZ  
748  N NZ  B LYS   A 28  ? 0.3584 0.3844 0.4421 -0.0148 0.0155  -0.0432 28  LYS   A NZ  
775  N N   . LYS   A 29  ? 0.3322 0.3846 0.2275 -0.0667 0.0811  -0.0368 29  LYS   A N   
776  C CA  . LYS   A 29  ? 0.3607 0.4156 0.2582 -0.0779 0.0978  -0.0232 29  LYS   A CA  
777  C C   . LYS   A 29  ? 0.3609 0.4153 0.2258 -0.0917 0.0953  -0.0158 29  LYS   A C   
778  O O   . LYS   A 29  ? 0.3758 0.4279 0.2482 -0.0818 0.0859  -0.0171 29  LYS   A O   
779  C CB  . LYS   A 29  ? 0.3839 0.4453 0.3396 -0.0702 0.1106  -0.0198 29  LYS   A CB  
780  C CG  . LYS   A 29  ? 0.4096 0.4699 0.4246 -0.0620 0.1117  -0.0158 29  LYS   A CG  
781  C CD  . LYS   A 29  ? 0.4309 0.4902 0.5014 -0.0560 0.1110  -0.0136 29  LYS   A CD  
782  C CE  . LYS   A 29  ? 0.4458 0.5045 0.5519 -0.0511 0.1130  -0.0132 29  LYS   A CE  
783  N NZ  . LYS   A 29  ? 0.4530 0.5134 0.5832 -0.0478 0.1112  -0.0139 29  LYS   A NZ  
798  N N   . VAL   A 30  ? 0.3473 0.3995 0.2004 -0.1134 0.0932  -0.0080 30  VAL   A N   
799  C CA  . VAL   A 30  ? 0.3432 0.3850 0.1902 -0.1283 0.0640  0.0146  30  VAL   A CA  
800  C C   . VAL   A 30  ? 0.3457 0.3742 0.1632 -0.1247 0.0461  0.0226  30  VAL   A C   
801  O O   . VAL   A 30  ? 0.3573 0.3783 0.1668 -0.1235 0.0404  0.0251  30  VAL   A O   
802  C CB  . VAL   A 30  ? 0.3417 0.3785 0.2340 -0.1428 0.0312  0.0152  30  VAL   A CB  
803  C CG1 . VAL   A 30  ? 0.3477 0.3773 0.2542 -0.1436 0.0160  0.0184  30  VAL   A CG1 
804  C CG2 . VAL   A 30  ? 0.3384 0.3766 0.2566 -0.1516 0.0266  0.0127  30  VAL   A CG2 
814  N N   . LYS   A 31  ? 0.3334 0.3561 0.1432 -0.1239 0.0250  0.0174  31  LYS   A N   
815  C CA  . LYS   A 31  ? 0.3505 0.3543 0.1544 -0.1105 -0.0010 0.0123  31  LYS   A CA  
816  C C   . LYS   A 31  ? 0.3167 0.3240 0.1188 -0.0914 -0.0098 0.0518  31  LYS   A C   
817  O O   . LYS   A 31  ? 0.3229 0.3381 0.1436 -0.0875 -0.0295 0.0653  31  LYS   A O   
818  C CB  . LYS   A 31  ? 0.3993 0.3817 0.2669 -0.1039 -0.0193 -0.0109 31  LYS   A CB  
819  C CG  . LYS   A 31  ? 0.4405 0.4117 0.4051 -0.0924 -0.0352 -0.0223 31  LYS   A CG  
820  C CD  . LYS   A 31  ? 0.4769 0.4426 0.5064 -0.0833 -0.0491 -0.0338 31  LYS   A CD  
821  C CE  . LYS   A 31  ? 0.5070 0.4636 0.5657 -0.0765 -0.0594 -0.0465 31  LYS   A CE  
822  N NZ  . LYS   A 31  ? 0.5199 0.4629 0.5974 -0.0722 -0.0636 -0.0557 31  LYS   A NZ  
836  N N   . PRO   A 32  ? 0.2816 0.2879 0.1027 -0.0915 -0.0101 0.0347  32  PRO   A N   
837  C CA  . PRO   A 32  ? 0.2706 0.2670 0.1525 -0.0822 -0.0192 0.0583  32  PRO   A CA  
838  C C   . PRO   A 32  ? 0.2613 0.2577 0.1480 -0.0726 -0.0237 0.0639  32  PRO   A C   
839  O O   . PRO   A 32  ? 0.2533 0.2532 0.1573 -0.0738 -0.0272 0.0555  32  PRO   A O   
840  C CB  . PRO   A 32  ? 0.2619 0.2665 0.1597 -0.0817 -0.0239 0.0442  32  PRO   A CB  
841  C CG  . PRO   A 32  ? 0.2599 0.2727 0.1054 -0.0796 -0.0357 0.0258  32  PRO   A CG  
842  C CD  . PRO   A 32  ? 0.2630 0.2742 0.0942 -0.0851 -0.0200 0.0241  32  PRO   A CD  
850  N N   . THR   A 33  ? 0.2705 0.2533 0.1514 -0.0636 -0.0218 0.0642  33  THR   A N   
851  C CA  . THR   A 33  ? 0.2678 0.2528 0.1577 -0.0484 -0.0393 0.0549  33  THR   A CA  
852  C C   . THR   A 33  ? 0.2282 0.2361 0.1485 -0.0481 -0.0421 0.0382  33  THR   A C   
853  O O   . THR   A 33  ? 0.2182 0.2383 0.1719 -0.0498 -0.0537 0.0485  33  THR   A O   
854  C CB  . THR   A 33  ? 0.2960 0.2724 0.1762 -0.0389 -0.0477 0.0715  33  THR   A CB  
855  O OG1 . THR   A 33  ? 0.3189 0.2860 0.2054 -0.0221 -0.0343 0.0901  33  THR   A OG1 
856  C CG2 . THR   A 33  ? 0.3018 0.2794 0.2001 -0.0348 -0.0539 0.0709  33  THR   A CG2 
864  N N   . VAL   A 34  ? 0.2037 0.2109 0.1286 -0.0478 -0.0306 0.0386  34  VAL   A N   
865  C CA  . VAL   A 34  ? 0.1881 0.1957 0.1128 -0.0369 -0.0221 0.0353  34  VAL   A CA  
866  C C   . VAL   A 34  ? 0.1716 0.1845 0.1212 -0.0332 -0.0106 0.0274  34  VAL   A C   
867  O O   . VAL   A 34  ? 0.1716 0.1817 0.1503 -0.0439 -0.0014 0.0342  34  VAL   A O   
868  C CB  . VAL   A 34  ? 0.1848 0.1908 0.1435 -0.0358 -0.0095 0.0119  34  VAL   A CB  
869  C CG1 . VAL   A 34  ? 0.1947 0.1862 0.1521 -0.0287 0.0093  0.0006  34  VAL   A CG1 
870  C CG2 . VAL   A 34  ? 0.1867 0.2032 0.1900 -0.0322 -0.0120 0.0204  34  VAL   A CG2 
880  N N   . VAL   A 35  ? 0.1531 0.1694 0.1255 -0.0346 -0.0085 0.0227  35  VAL   A N   
881  C CA  . VAL   A 35  ? 0.1439 0.1661 0.1265 -0.0309 -0.0072 0.0168  35  VAL   A CA  
882  C C   . VAL   A 35  ? 0.1404 0.1516 0.1139 -0.0197 0.0001  0.0198  35  VAL   A C   
883  O O   . VAL   A 35  ? 0.1317 0.1588 0.1433 -0.0261 0.0097  0.0113  35  VAL   A O   
884  C CB  . VAL   A 35  ? 0.1553 0.1732 0.1415 -0.0205 0.0055  0.0026  35  VAL   A CB  
885  C CG1 . VAL   A 35  ? 0.1607 0.1718 0.1421 -0.0163 0.0003  -0.0022 35  VAL   A CG1 
886  C CG2 . VAL   A 35  ? 0.1513 0.1780 0.1667 -0.0154 0.0131  -0.0061 35  VAL   A CG2 
896  N N   . VAL   A 36  ? 0.1267 0.1486 0.1036 -0.0216 0.0044  0.0196  36  VAL   A N   
897  C CA  . VAL   A 36  ? 0.1271 0.1406 0.1124 -0.0155 -0.0016 0.0094  36  VAL   A CA  
898  C C   . VAL   A 36  ? 0.1226 0.1461 0.1289 -0.0165 0.0113  0.0113  36  VAL   A C   
899  O O   . VAL   A 36  ? 0.1314 0.1390 0.1476 -0.0092 0.0231  0.0059  36  VAL   A O   
900  C CB  . VAL   A 36  ? 0.1247 0.1296 0.1301 -0.0117 -0.0010 0.0151  36  VAL   A CB  
901  C CG1 . VAL   A 36  ? 0.1360 0.1339 0.1315 -0.0157 0.0011  0.0034  36  VAL   A CG1 
902  C CG2 . VAL   A 36  ? 0.1326 0.1404 0.1434 -0.0122 0.0039  0.0231  36  VAL   A CG2 
912  N N   . ASN   A 37  ? 0.1136 0.1348 0.1171 -0.0061 0.0067  0.0198  37  ASN   A N   
913  C CA  . ASN   A 37  ? 0.1203 0.1274 0.1205 -0.0021 0.0091  0.0151  37  ASN   A CA  
914  C C   . ASN   A 37  ? 0.1240 0.1204 0.1282 -0.0069 0.0142  0.0227  37  ASN   A C   
915  O O   . ASN   A 37  ? 0.1357 0.1342 0.1204 0.0063  0.0145  0.0035  37  ASN   A O   
916  C CB  . ASN   A 37  ? 0.1193 0.1259 0.1259 0.0041  0.0069  0.0129  37  ASN   A CB  
917  C CG  . ASN   A 37  ? 0.1230 0.1339 0.1369 -0.0032 0.0069  0.0061  37  ASN   A CG  
918  O OD1 . ASN   A 37  ? 0.1193 0.1342 0.1599 -0.0027 0.0093  0.0129  37  ASN   A OD1 
919  N ND2 . ASN   A 37  ? 0.1214 0.1292 0.1526 -0.0024 0.0057  0.0196  37  ASN   A ND2 
926  N N   . ALA   A 38  ? 0.1213 0.1311 0.1390 0.0011  0.0120  0.0107  38  ALA   A N   
927  C CA  . ALA   A 38  ? 0.1253 0.1390 0.1276 -0.0032 0.0001  0.0070  38  ALA   A CA  
928  C C   . ALA   A 38  ? 0.1231 0.1349 0.1245 0.0014  -0.0032 0.0015  38  ALA   A C   
929  O O   . ALA   A 38  ? 0.1289 0.1308 0.1405 0.0051  -0.0087 0.0049  38  ALA   A O   
930  C CB  . ALA   A 38  ? 0.1294 0.1707 0.1431 -0.0168 -0.0057 0.0088  38  ALA   A CB  
936  N N   A ALA   A 39  ? 0.1162 0.1325 0.1432 0.0054  0.0035  0.0087  39  ALA   A N   
937  N N   B ALA   A 39  ? 0.1242 0.1353 0.1273 -0.0014 0.0020  0.0080  39  ALA   A N   
938  C CA  A ALA   A 39  ? 0.1258 0.1318 0.1393 0.0034  0.0021  0.0016  39  ALA   A CA  
939  C CA  B ALA   A 39  ? 0.1324 0.1388 0.1274 -0.0076 0.0045  0.0113  39  ALA   A CA  
940  C C   A ALA   A 39  ? 0.1285 0.1239 0.1398 0.0020  -0.0043 0.0032  39  ALA   A C   
941  C C   B ALA   A 39  ? 0.1278 0.1291 0.1188 -0.0095 0.0020  0.0152  39  ALA   A C   
942  O O   A ALA   A 39  ? 0.1380 0.1260 0.1478 0.0031  0.0001  0.0010  39  ALA   A O   
943  O O   B ALA   A 39  ? 0.1221 0.1245 0.1148 -0.0149 0.0061  0.0184  39  ALA   A O   
944  C CB  A ALA   A 39  ? 0.1261 0.1395 0.1451 0.0014  -0.0060 -0.0093 39  ALA   A CB  
945  C CB  B ALA   A 39  ? 0.1416 0.1489 0.1408 -0.0091 0.0048  0.0005  39  ALA   A CB  
956  N N   A ASN   A 40  ? 0.1384 0.1255 0.1455 -0.0090 0.0176  -0.0004 40  ASN   A N   
957  N N   B ASN   A 40  ? 0.1358 0.1276 0.1258 -0.0101 0.0132  0.0134  40  ASN   A N   
958  C CA  A ASN   A 40  ? 0.1420 0.1269 0.1342 -0.0018 0.0108  0.0013  40  ASN   A CA  
959  C CA  B ASN   A 40  ? 0.1405 0.1283 0.1308 -0.0057 0.0041  0.0156  40  ASN   A CA  
960  C C   A ASN   A 40  ? 0.1447 0.1191 0.1178 -0.0034 0.0229  0.0066  40  ASN   A C   
961  C C   B ASN   A 40  ? 0.1429 0.1221 0.1269 -0.0080 0.0138  0.0240  40  ASN   A C   
962  O O   A ASN   A 40  ? 0.1393 0.1200 0.1417 -0.0067 0.0192  0.0072  40  ASN   A O   
963  O O   B ASN   A 40  ? 0.1374 0.1214 0.1396 -0.0131 0.0094  0.0309  40  ASN   A O   
964  C CB  A ASN   A 40  ? 0.1554 0.1339 0.1519 0.0050  0.0000  0.0039  40  ASN   A CB  
965  C CB  B ASN   A 40  ? 0.1515 0.1346 0.1494 -0.0040 -0.0040 0.0069  40  ASN   A CB  
966  C CG  A ASN   A 40  ? 0.1629 0.1318 0.1836 0.0109  -0.0071 0.0142  40  ASN   A CG  
967  C CG  B ASN   A 40  ? 0.1555 0.1362 0.1725 -0.0049 -0.0030 0.0002  40  ASN   A CG  
968  O OD1 A ASN   A 40  ? 0.1686 0.1292 0.2031 0.0128  -0.0103 0.0130  40  ASN   A OD1 
969  O OD1 B ASN   A 40  ? 0.1618 0.1415 0.1842 -0.0013 -0.0049 -0.0067 40  ASN   A OD1 
970  N ND2 A ASN   A 40  ? 0.1637 0.1438 0.1861 0.0104  -0.0013 0.0045  40  ASN   A ND2 
971  N ND2 B ASN   A 40  ? 0.1500 0.1365 0.1859 -0.0166 0.0090  -0.0056 40  ASN   A ND2 
984  N N   A VAL   A 41  ? 0.1510 0.1259 0.1261 0.0022  0.0180  0.0126  41  VAL   A N   
985  N N   B VAL   A 41  ? 0.1498 0.1248 0.1244 -0.0009 0.0176  0.0241  41  VAL   A N   
986  C CA  A VAL   A 41  ? 0.1493 0.1271 0.1492 0.0009  0.0234  0.0088  41  VAL   A CA  
987  C CA  B VAL   A 41  ? 0.1523 0.1244 0.1318 -0.0004 0.0319  0.0208  41  VAL   A CA  
988  C C   A VAL   A 41  ? 0.1532 0.1275 0.1524 0.0024  0.0173  0.0126  41  VAL   A C   
989  C C   B VAL   A 41  ? 0.1499 0.1218 0.1353 0.0013  0.0362  0.0134  41  VAL   A C   
990  O O   A VAL   A 41  ? 0.1610 0.1223 0.1733 0.0002  0.0098  0.0031  41  VAL   A O   
991  O O   B VAL   A 41  ? 0.1505 0.1127 0.1354 0.0014  0.0487  0.0037  41  VAL   A O   
992  C CB  A VAL   A 41  ? 0.1538 0.1329 0.1572 -0.0021 0.0306  0.0018  41  VAL   A CB  
993  C CB  B VAL   A 41  ? 0.1585 0.1315 0.1494 -0.0001 0.0397  0.0182  41  VAL   A CB  
994  C CG1 A VAL   A 41  ? 0.1705 0.1420 0.1681 0.0007  0.0269  -0.0017 41  VAL   A CG1 
995  C CG1 B VAL   A 41  ? 0.1738 0.1391 0.1647 -0.0037 0.0462  0.0084  41  VAL   A CG1 
996  C CG2 A VAL   A 41  ? 0.1560 0.1355 0.1355 -0.0032 0.0373  0.0058  41  VAL   A CG2 
997  C CG2 B VAL   A 41  ? 0.1622 0.1401 0.1558 0.0004  0.0296  0.0184  41  VAL   A CG2 
1016 N N   . TYR   A 42  ? 0.1435 0.1229 0.1609 0.0014  0.0344  0.0191  42  TYR   A N   
1017 C CA  . TYR   A 42  ? 0.1449 0.1221 0.1669 -0.0025 0.0321  0.0167  42  TYR   A CA  
1018 C C   . TYR   A 42  ? 0.1373 0.1214 0.1641 0.0013  0.0231  0.0244  42  TYR   A C   
1019 O O   . TYR   A 42  ? 0.1442 0.1205 0.1817 -0.0124 0.0215  -0.0007 42  TYR   A O   
1020 C CB  . TYR   A 42  ? 0.1727 0.1276 0.1569 -0.0053 0.0343  0.0329  42  TYR   A CB  
1021 C CG  . TYR   A 42  ? 0.1838 0.1374 0.1640 0.0032  0.0272  0.0350  42  TYR   A CG  
1022 C CD1 . TYR   A 42  ? 0.1918 0.1484 0.1790 -0.0065 0.0289  0.0259  42  TYR   A CD1 
1023 C CD2 . TYR   A 42  ? 0.2011 0.1645 0.1846 0.0019  0.0168  0.0214  42  TYR   A CD2 
1024 C CE1 . TYR   A 42  ? 0.2034 0.1654 0.1780 -0.0147 0.0379  0.0207  42  TYR   A CE1 
1025 C CE2 . TYR   A 42  ? 0.2132 0.1780 0.1963 -0.0139 0.0224  0.0292  42  TYR   A CE2 
1026 C CZ  . TYR   A 42  ? 0.2223 0.1826 0.1839 -0.0187 0.0428  0.0274  42  TYR   A CZ  
1027 O OH  . TYR   A 42  ? 0.2351 0.2118 0.2115 -0.0330 0.0445  0.0130  42  TYR   A OH  
1038 N N   . LEU   A 43  ? 0.1360 0.1261 0.1502 -0.0014 0.0135  0.0081  43  LEU   A N   
1039 C CA  . LEU   A 43  ? 0.1220 0.1250 0.1562 -0.0019 0.0078  0.0055  43  LEU   A CA  
1040 C C   . LEU   A 43  ? 0.1271 0.1279 0.1458 -0.0052 0.0061  0.0033  43  LEU   A C   
1041 O O   . LEU   A 43  ? 0.1442 0.1314 0.1833 0.0028  -0.0016 0.0035  43  LEU   A O   
1042 C CB  . LEU   A 43  ? 0.1343 0.1254 0.1822 -0.0037 0.0157  0.0042  43  LEU   A CB  
1043 C CG  . LEU   A 43  ? 0.1346 0.1247 0.1690 0.0011  0.0067  0.0088  43  LEU   A CG  
1044 C CD1 . LEU   A 43  ? 0.1478 0.1313 0.1914 0.0009  -0.0061 0.0135  43  LEU   A CD1 
1045 C CD2 . LEU   A 43  ? 0.1527 0.1272 0.1656 -0.0007 0.0030  0.0165  43  LEU   A CD2 
1057 N N   A LYS   A 44  ? 0.1348 0.1222 0.1471 0.0024  0.0006  0.0052  44  LYS   A N   
1058 N N   B LYS   A 44  ? 0.1408 0.1350 0.1559 -0.0003 0.0063  -0.0009 44  LYS   A N   
1059 C CA  A LYS   A 44  ? 0.1448 0.1234 0.1493 0.0014  0.0046  0.0160  44  LYS   A CA  
1060 C CA  B LYS   A 44  ? 0.1570 0.1451 0.1695 0.0007  0.0093  -0.0023 44  LYS   A CA  
1061 C C   A LYS   A 44  ? 0.1282 0.1177 0.1359 0.0084  -0.0019 0.0107  44  LYS   A C   
1062 C C   B LYS   A 44  ? 0.1516 0.1444 0.1527 0.0016  0.0020  -0.0065 44  LYS   A C   
1063 O O   A LYS   A 44  ? 0.1413 0.1378 0.1602 0.0087  0.0027  0.0035  44  LYS   A O   
1064 O O   B LYS   A 44  ? 0.1550 0.1491 0.1558 -0.0039 0.0020  -0.0054 44  LYS   A O   
1065 C CB  A LYS   A 44  ? 0.1780 0.1357 0.1930 0.0016  0.0098  0.0250  44  LYS   A CB  
1066 C CB  B LYS   A 44  ? 0.1793 0.1589 0.2084 0.0050  0.0218  0.0028  44  LYS   A CB  
1067 C CG  A LYS   A 44  ? 0.2073 0.1747 0.2576 -0.0093 0.0230  0.0276  44  LYS   A CG  
1068 C CG  B LYS   A 44  ? 0.1973 0.1820 0.2586 0.0075  0.0304  0.0119  44  LYS   A CG  
1069 C CD  A LYS   A 44  ? 0.2427 0.2295 0.3451 -0.0122 0.0120  0.0280  44  LYS   A CD  
1070 C CD  B LYS   A 44  ? 0.2175 0.2114 0.3129 0.0048  0.0208  0.0135  44  LYS   A CD  
1071 C CE  A LYS   A 44  ? 0.2611 0.2597 0.3909 -0.0160 0.0053  0.0343  44  LYS   A CE  
1072 C CE  B LYS   A 44  ? 0.2292 0.2307 0.3488 0.0025  0.0168  0.0151  44  LYS   A CE  
1073 N NZ  A LYS   A 44  ? 0.2688 0.2849 0.4071 -0.0190 0.0044  0.0405  44  LYS   A NZ  
1074 N NZ  B LYS   A 44  ? 0.2392 0.2442 0.3718 -0.0040 0.0151  0.0103  44  LYS   A NZ  
1101 N N   A HIS   A 45  ? 0.1188 0.1176 0.1405 0.0071  0.0024  0.0207  45  HIS   A N   
1102 N N   B HIS   A 45  ? 0.1516 0.1448 0.1541 0.0046  -0.0040 -0.0039 45  HIS   A N   
1103 C CA  A HIS   A 45  ? 0.1175 0.1218 0.1485 0.0030  0.0063  0.0071  45  HIS   A CA  
1104 C CA  B HIS   A 45  ? 0.1532 0.1463 0.1551 0.0104  -0.0089 -0.0065 45  HIS   A CA  
1105 C C   A HIS   A 45  ? 0.1270 0.1332 0.1685 0.0038  0.0095  0.0124  45  HIS   A C   
1106 C C   B HIS   A 45  ? 0.1606 0.1526 0.1657 0.0195  -0.0095 0.0018  45  HIS   A C   
1107 O O   A HIS   A 45  ? 0.1406 0.1396 0.2050 0.0106  0.0040  -0.0024 45  HIS   A O   
1108 O O   B HIS   A 45  ? 0.1662 0.1524 0.1871 0.0268  -0.0090 -0.0016 45  HIS   A O   
1109 C CB  A HIS   A 45  ? 0.1218 0.1183 0.1503 -0.0041 0.0150  0.0008  45  HIS   A CB  
1110 C CB  B HIS   A 45  ? 0.1481 0.1421 0.1498 0.0081  -0.0112 -0.0126 45  HIS   A CB  
1111 C CG  A HIS   A 45  ? 0.1221 0.1149 0.1494 -0.0060 0.0039  0.0085  45  HIS   A CG  
1112 C CG  B HIS   A 45  ? 0.1368 0.1387 0.1289 0.0028  -0.0046 -0.0092 45  HIS   A CG  
1113 N ND1 A HIS   A 45  ? 0.1126 0.1270 0.1588 -0.0059 0.0053  0.0136  45  HIS   A ND1 
1114 N ND1 B HIS   A 45  ? 0.1310 0.1421 0.1423 0.0038  -0.0068 0.0021  45  HIS   A ND1 
1115 C CD2 A HIS   A 45  ? 0.1246 0.1175 0.1615 -0.0101 -0.0013 0.0284  45  HIS   A CD2 
1116 C CD2 B HIS   A 45  ? 0.1277 0.1320 0.1080 0.0022  -0.0032 -0.0125 45  HIS   A CD2 
1117 C CE1 A HIS   A 45  ? 0.1180 0.1334 0.1537 -0.0112 0.0004  0.0194  45  HIS   A CE1 
1118 C CE1 B HIS   A 45  ? 0.1271 0.1337 0.1111 -0.0012 -0.0114 -0.0108 45  HIS   A CE1 
1119 N NE2 A HIS   A 45  ? 0.1237 0.1293 0.1626 -0.0022 0.0091  0.0286  45  HIS   A NE2 
1120 N NE2 B HIS   A 45  ? 0.1261 0.1300 0.0994 0.0007  -0.0088 -0.0122 45  HIS   A NE2 
1135 N N   A GLY   A 46  ? 0.1477 0.1472 0.1889 0.0179  -0.0090 0.0218  46  GLY   A N   
1136 N N   B GLY   A 46  ? 0.1676 0.1570 0.1691 0.0265  -0.0162 0.0112  46  GLY   A N   
1137 C CA  A GLY   A 46  ? 0.1553 0.1582 0.2059 0.0166  -0.0072 0.0212  46  GLY   A CA  
1138 C CA  B GLY   A 46  ? 0.1661 0.1577 0.1732 0.0279  -0.0165 0.0163  46  GLY   A CA  
1139 C C   A GLY   A 46  ? 0.1653 0.1520 0.2127 0.0251  -0.0164 0.0264  46  GLY   A C   
1140 C C   B GLY   A 46  ? 0.1645 0.1501 0.1697 0.0344  -0.0223 0.0210  46  GLY   A C   
1141 O O   A GLY   A 46  ? 0.1704 0.1638 0.2489 0.0257  -0.0281 -0.0033 46  GLY   A O   
1142 O O   B GLY   A 46  ? 0.1682 0.1510 0.1909 0.0388  -0.0233 0.0148  46  GLY   A O   
1149 N N   A GLY   A 47  ? 0.1724 0.1451 0.1882 0.0219  -0.0188 0.0112  47  GLY   A N   
1150 N N   B GLY   A 47  ? 0.1582 0.1482 0.1538 0.0292  -0.0304 0.0105  47  GLY   A N   
1151 C CA  A GLY   A 47  ? 0.1695 0.1525 0.1707 0.0305  -0.0408 -0.0096 47  GLY   A CA  
1152 C CA  B GLY   A 47  ? 0.1526 0.1543 0.1422 0.0246  -0.0414 0.0024  47  GLY   A CA  
1153 C C   A GLY   A 47  ? 0.1709 0.1415 0.1563 0.0303  -0.0468 -0.0159 47  GLY   A C   
1154 C C   B GLY   A 47  ? 0.1508 0.1497 0.1317 0.0161  -0.0325 -0.0099 47  GLY   A C   
1155 O O   A GLY   A 47  ? 0.1692 0.1330 0.1614 0.0379  -0.0466 -0.0025 47  GLY   A O   
1156 O O   B GLY   A 47  ? 0.1505 0.1487 0.1182 0.0171  -0.0276 -0.0011 47  GLY   A O   
1163 N N   A GLY   A 48  ? 0.1651 0.1442 0.1668 0.0301  -0.0601 -0.0171 48  GLY   A N   
1164 N N   B GLY   A 48  ? 0.1481 0.1501 0.1574 0.0090  -0.0298 -0.0151 48  GLY   A N   
1165 C CA  A GLY   A 48  ? 0.1607 0.1406 0.1884 0.0205  -0.0493 -0.0194 48  GLY   A CA  
1166 C CA  B GLY   A 48  ? 0.1454 0.1413 0.1697 0.0098  -0.0203 -0.0232 48  GLY   A CA  
1167 C C   A GLY   A 48  ? 0.1424 0.1386 0.1695 0.0085  -0.0228 -0.0060 48  GLY   A C   
1168 C C   B GLY   A 48  ? 0.1353 0.1334 0.1741 0.0068  -0.0035 -0.0217 48  GLY   A C   
1169 O O   A GLY   A 48  ? 0.1512 0.1383 0.1655 0.0079  -0.0135 -0.0071 48  GLY   A O   
1170 O O   B GLY   A 48  ? 0.1394 0.1258 0.1784 0.0075  0.0078  -0.0253 48  GLY   A O   
1177 N N   A VAL   A 49  ? 0.1282 0.1324 0.1889 0.0029  -0.0243 -0.0023 49  VAL   A N   
1178 N N   B VAL   A 49  ? 0.1228 0.1303 0.1688 0.0015  -0.0080 -0.0264 49  VAL   A N   
1179 C CA  A VAL   A 49  ? 0.1368 0.1349 0.1757 -0.0048 -0.0012 0.0050  49  VAL   A CA  
1180 C CA  B VAL   A 49  ? 0.1159 0.1369 0.1579 0.0012  -0.0007 -0.0183 49  VAL   A CA  
1181 C C   A VAL   A 49  ? 0.1322 0.1254 0.1456 -0.0020 -0.0015 0.0082  49  VAL   A C   
1182 C C   B VAL   A 49  ? 0.1101 0.1271 0.1379 0.0046  0.0075  -0.0290 49  VAL   A C   
1183 O O   A VAL   A 49  ? 0.1356 0.1334 0.1459 -0.0036 -0.0037 0.0051  49  VAL   A O   
1184 O O   B VAL   A 49  ? 0.1053 0.1223 0.1435 0.0117  0.0159  -0.0148 49  VAL   A O   
1185 C CB  A VAL   A 49  ? 0.1492 0.1298 0.1839 -0.0085 -0.0075 0.0029  49  VAL   A CB  
1186 C CB  B VAL   A 49  ? 0.1231 0.1421 0.1661 0.0034  -0.0067 -0.0101 49  VAL   A CB  
1187 C CG1 A VAL   A 49  ? 0.1412 0.1269 0.1939 -0.0072 0.0135  0.0041  49  VAL   A CG1 
1188 C CG1 B VAL   A 49  ? 0.1086 0.1411 0.1679 0.0100  -0.0011 -0.0018 49  VAL   A CG1 
1189 C CG2 A VAL   A 49  ? 0.1658 0.1466 0.2112 -0.0265 -0.0254 0.0112  49  VAL   A CG2 
1190 C CG2 B VAL   A 49  ? 0.1396 0.1555 0.1879 0.0038  -0.0177 -0.0039 49  VAL   A CG2 
1209 N N   A ALA   A 50  ? 0.1281 0.1262 0.1561 0.0016  -0.0194 0.0175  50  ALA   A N   
1210 N N   B ALA   A 50  ? 0.1163 0.1299 0.1323 0.0019  0.0030  -0.0374 50  ALA   A N   
1211 C CA  A ALA   A 50  ? 0.1235 0.1223 0.1567 -0.0037 -0.0083 0.0297  50  ALA   A CA  
1212 C CA  B ALA   A 50  ? 0.1151 0.1308 0.1153 -0.0004 0.0060  -0.0423 50  ALA   A CA  
1213 C C   A ALA   A 50  ? 0.1160 0.1244 0.1551 -0.0009 -0.0042 0.0224  50  ALA   A C   
1214 C C   B ALA   A 50  ? 0.1142 0.1303 0.0981 -0.0009 -0.0025 -0.0427 50  ALA   A C   
1215 O O   A ALA   A 50  ? 0.1232 0.1267 0.1862 -0.0021 -0.0061 0.0208  50  ALA   A O   
1216 O O   B ALA   A 50  ? 0.1188 0.1330 0.0833 0.0001  -0.0018 -0.0425 50  ALA   A O   
1217 C CB  A ALA   A 50  ? 0.1200 0.1229 0.1715 -0.0032 -0.0090 0.0210  50  ALA   A CB  
1218 C CB  B ALA   A 50  ? 0.1144 0.1260 0.1150 0.0003  0.0157  -0.0584 50  ALA   A CB  
1229 N N   A GLY   A 51  ? 0.1237 0.1199 0.1663 0.0151  -0.0157 0.0087  51  GLY   A N   
1230 N N   B GLY   A 51  ? 0.1205 0.1320 0.1332 0.0019  -0.0164 -0.0374 51  GLY   A N   
1231 C CA  A GLY   A 51  ? 0.1416 0.1204 0.1624 0.0230  -0.0156 0.0099  51  GLY   A CA  
1232 C CA  B GLY   A 51  ? 0.1293 0.1337 0.1434 -0.0026 -0.0247 -0.0378 51  GLY   A CA  
1233 C C   A GLY   A 51  ? 0.1311 0.1331 0.1622 0.0197  0.0003  -0.0091 51  GLY   A C   
1234 C C   B GLY   A 51  ? 0.1226 0.1395 0.1583 -0.0063 -0.0198 -0.0409 51  GLY   A C   
1235 O O   A GLY   A 51  ? 0.1376 0.1486 0.1721 0.0181  -0.0088 -0.0143 51  GLY   A O   
1236 O O   B GLY   A 51  ? 0.1226 0.1408 0.1729 -0.0054 -0.0164 -0.0437 51  GLY   A O   
1243 N N   A ALA   A 52  ? 0.1273 0.1448 0.1660 0.0136  0.0030  -0.0132 52  ALA   A N   
1244 N N   B ALA   A 52  ? 0.1232 0.1434 0.1481 -0.0069 -0.0095 -0.0467 52  ALA   A N   
1245 C CA  A ALA   A 52  ? 0.1209 0.1586 0.1745 0.0053  -0.0020 -0.0173 52  ALA   A CA  
1246 C CA  B ALA   A 52  ? 0.1234 0.1516 0.1544 -0.0099 0.0009  -0.0403 52  ALA   A CA  
1247 C C   A ALA   A 52  ? 0.1236 0.1585 0.1603 -0.0053 0.0075  -0.0079 52  ALA   A C   
1248 C C   B ALA   A 52  ? 0.1230 0.1470 0.1450 -0.0150 0.0176  -0.0385 52  ALA   A C   
1249 O O   A ALA   A 52  ? 0.1322 0.1622 0.1778 -0.0008 0.0059  -0.0022 52  ALA   A O   
1250 O O   B ALA   A 52  ? 0.1287 0.1433 0.1540 -0.0136 0.0307  -0.0413 52  ALA   A O   
1251 C CB  A ALA   A 52  ? 0.1278 0.1823 0.1909 -0.0015 -0.0039 -0.0212 52  ALA   A CB  
1252 C CB  B ALA   A 52  ? 0.1281 0.1658 0.1632 -0.0094 0.0014  -0.0352 52  ALA   A CB  
1263 N N   A LEU   A 53  ? 0.1224 0.1508 0.1562 -0.0051 0.0012  -0.0106 53  LEU   A N   
1264 N N   B LEU   A 53  ? 0.1199 0.1445 0.1464 -0.0117 0.0107  -0.0313 53  LEU   A N   
1265 C CA  A LEU   A 53  ? 0.1356 0.1525 0.1444 -0.0082 0.0054  -0.0078 53  LEU   A CA  
1266 C CA  B LEU   A 53  ? 0.1232 0.1473 0.1471 -0.0099 0.0083  -0.0204 53  LEU   A CA  
1267 C C   A LEU   A 53  ? 0.1306 0.1438 0.1102 0.0025  0.0073  -0.0093 53  LEU   A C   
1268 C C   B LEU   A 53  ? 0.1253 0.1467 0.1332 -0.0018 0.0059  -0.0140 53  LEU   A C   
1269 O O   A LEU   A 53  ? 0.1411 0.1452 0.1383 -0.0062 0.0109  -0.0101 53  LEU   A O   
1270 O O   B LEU   A 53  ? 0.1300 0.1538 0.1497 -0.0039 0.0017  -0.0125 53  LEU   A O   
1271 C CB  A LEU   A 53  ? 0.1500 0.1552 0.1401 -0.0101 0.0037  0.0056  53  LEU   A CB  
1272 C CB  B LEU   A 53  ? 0.1226 0.1454 0.1438 -0.0109 0.0128  -0.0158 53  LEU   A CB  
1273 C CG  A LEU   A 53  ? 0.1655 0.1592 0.1674 -0.0090 0.0052  0.0082  53  LEU   A CG  
1274 C CG  B LEU   A 53  ? 0.1218 0.1431 0.1361 -0.0140 0.0052  -0.0173 53  LEU   A CG  
1275 C CD1 A LEU   A 53  ? 0.1756 0.1651 0.1574 0.0019  -0.0003 0.0143  53  LEU   A CD1 
1276 C CD1 B LEU   A 53  ? 0.1316 0.1500 0.1294 -0.0108 0.0027  -0.0171 53  LEU   A CD1 
1277 C CD2 A LEU   A 53  ? 0.1775 0.1795 0.1857 -0.0135 -0.0050 0.0068  53  LEU   A CD2 
1278 C CD2 B LEU   A 53  ? 0.1185 0.1449 0.1330 -0.0113 0.0031  -0.0224 53  LEU   A CD2 
1301 N N   . ASN   A 54  ? 0.1247 0.1405 0.1362 -0.0021 0.0016  -0.0012 54  ASN   A N   
1302 C CA  . ASN   A 54  ? 0.1102 0.1359 0.1443 -0.0013 -0.0047 -0.0147 54  ASN   A CA  
1303 C C   . ASN   A 54  ? 0.1248 0.1468 0.1508 -0.0061 -0.0025 -0.0127 54  ASN   A C   
1304 O O   . ASN   A 54  ? 0.1269 0.1588 0.1582 -0.0041 -0.0042 -0.0197 54  ASN   A O   
1305 C CB  . ASN   A 54  ? 0.1133 0.1363 0.1529 -0.0030 0.0015  -0.0078 54  ASN   A CB  
1306 C CG  . ASN   A 54  ? 0.1166 0.1419 0.1608 -0.0038 -0.0040 -0.0069 54  ASN   A CG  
1307 O OD1 . ASN   A 54  ? 0.1188 0.1444 0.1684 0.0031  -0.0057 -0.0097 54  ASN   A OD1 
1308 N ND2 . ASN   A 54  ? 0.1263 0.1472 0.1844 -0.0100 -0.0069 0.0134  54  ASN   A ND2 
1316 N N   . LYS   A 55  ? 0.1277 0.1472 0.1623 0.0004  -0.0035 -0.0226 55  LYS   A N   
1317 C CA  . LYS   A 55  ? 0.1440 0.1584 0.1748 0.0093  -0.0097 -0.0310 55  LYS   A CA  
1318 C C   . LYS   A 55  ? 0.1361 0.1626 0.1684 0.0002  -0.0008 -0.0387 55  LYS   A C   
1319 O O   . LYS   A 55  ? 0.1439 0.1762 0.1800 0.0074  -0.0004 -0.0379 55  LYS   A O   
1320 C CB  . LYS   A 55  ? 0.1582 0.1716 0.1915 0.0280  -0.0054 -0.0307 55  LYS   A CB  
1321 C CG  . LYS   A 55  ? 0.1774 0.2083 0.2157 0.0437  -0.0188 -0.0369 55  LYS   A CG  
1322 C CD  . LYS   A 55  ? 0.1980 0.2455 0.2283 0.0602  -0.0146 -0.0337 55  LYS   A CD  
1323 C CE  . LYS   A 55  ? 0.2205 0.2740 0.2471 0.0720  -0.0221 -0.0358 55  LYS   A CE  
1324 N NZ  . LYS   A 55  ? 0.2334 0.2848 0.2446 0.0795  -0.0262 -0.0302 55  LYS   A NZ  
1338 N N   . ALA   A 56  ? 0.1407 0.1792 0.1797 -0.0075 0.0027  -0.0386 56  ALA   A N   
1339 C CA  . ALA   A 56  ? 0.1502 0.1951 0.1678 -0.0157 0.0101  -0.0346 56  ALA   A CA  
1340 C C   . ALA   A 56  ? 0.1543 0.2060 0.1455 -0.0161 0.0141  -0.0397 56  ALA   A C   
1341 O O   . ALA   A 56  ? 0.1575 0.2399 0.1558 0.0017  0.0124  -0.0323 56  ALA   A O   
1342 C CB  . ALA   A 56  ? 0.1594 0.2138 0.1740 -0.0212 0.0081  -0.0115 56  ALA   A CB  
1348 N N   . THR   A 57  ? 0.1374 0.1784 0.1434 -0.0128 0.0136  -0.0302 57  THR   A N   
1349 C CA  . THR   A 57  ? 0.1450 0.1747 0.1523 -0.0124 0.0050  -0.0207 57  THR   A CA  
1350 C C   . THR   A 57  ? 0.1452 0.1799 0.1634 -0.0066 -0.0019 -0.0220 57  THR   A C   
1351 O O   . THR   A 57  ? 0.1380 0.1818 0.1871 -0.0108 -0.0043 -0.0374 57  THR   A O   
1352 C CB  . THR   A 57  ? 0.1453 0.1700 0.1390 -0.0109 0.0048  -0.0254 57  THR   A CB  
1353 O OG1 . THR   A 57  ? 0.1330 0.1673 0.1577 -0.0051 0.0104  -0.0180 57  THR   A OG1 
1354 C CG2 . THR   A 57  ? 0.1519 0.1719 0.1356 -0.0100 0.0040  -0.0128 57  THR   A CG2 
1362 N N   . ASN   A 58  ? 0.1508 0.1721 0.1868 -0.0068 0.0048  -0.0408 58  ASN   A N   
1363 C CA  . ASN   A 58  ? 0.1689 0.1650 0.2033 -0.0065 0.0146  -0.0496 58  ASN   A CA  
1364 C C   . ASN   A 58  ? 0.1450 0.1549 0.1900 0.0022  0.0051  -0.0362 58  ASN   A C   
1365 O O   . ASN   A 58  ? 0.1480 0.1690 0.1999 -0.0081 -0.0007 -0.0434 58  ASN   A O   
1366 C CB  . ASN   A 58  ? 0.2255 0.1807 0.2230 -0.0212 0.0384  -0.0667 58  ASN   A CB  
1367 C CG  . ASN   A 58  ? 0.2800 0.2087 0.3024 -0.0221 0.0428  -0.0490 58  ASN   A CG  
1368 O OD1 . ASN   A 58  ? 0.3073 0.2019 0.3559 0.0215  0.0750  -0.0390 58  ASN   A OD1 
1369 N ND2 . ASN   A 58  ? 0.2960 0.2239 0.3284 -0.0319 0.0338  -0.0500 58  ASN   A ND2 
1376 N N   . ASN   A 59  ? 0.1300 0.1483 0.1716 -0.0061 -0.0032 -0.0280 59  ASN   A N   
1377 C CA  . ASN   A 59  ? 0.1326 0.1377 0.1726 -0.0011 -0.0052 -0.0205 59  ASN   A CA  
1378 C C   . ASN   A 59  ? 0.1313 0.1396 0.1583 -0.0068 0.0030  -0.0110 59  ASN   A C   
1379 O O   . ASN   A 59  ? 0.1381 0.1416 0.1525 -0.0061 -0.0029 -0.0098 59  ASN   A O   
1380 C CB  . ASN   A 59  ? 0.1414 0.1314 0.1652 0.0023  -0.0141 -0.0199 59  ASN   A CB  
1381 C CG  . ASN   A 59  ? 0.1449 0.1360 0.1767 -0.0008 -0.0226 -0.0079 59  ASN   A CG  
1382 O OD1 . ASN   A 59  ? 0.1554 0.1438 0.1759 -0.0107 -0.0182 -0.0075 59  ASN   A OD1 
1383 N ND2 . ASN   A 59  ? 0.1556 0.1376 0.1965 -0.0095 -0.0221 0.0023  59  ASN   A ND2 
1390 N N   . ALA   A 60  ? 0.1214 0.1454 0.1598 -0.0028 -0.0001 -0.0072 60  ALA   A N   
1391 C CA  . ALA   A 60  ? 0.1256 0.1484 0.1590 -0.0034 -0.0123 -0.0092 60  ALA   A CA  
1392 C C   . ALA   A 60  ? 0.1276 0.1478 0.1624 -0.0032 -0.0075 -0.0071 60  ALA   A C   
1393 O O   . ALA   A 60  ? 0.1215 0.1450 0.1864 -0.0069 -0.0080 -0.0119 60  ALA   A O   
1394 C CB  . ALA   A 60  ? 0.1382 0.1557 0.1592 -0.0061 -0.0205 -0.0268 60  ALA   A CB  
1400 N N   . MET   A 61  ? 0.1218 0.1348 0.1571 -0.0030 -0.0009 -0.0141 61  MET   A N   
1401 C CA  . MET   A 61  ? 0.1197 0.1347 0.1539 -0.0046 0.0048  -0.0031 61  MET   A CA  
1402 C C   . MET   A 61  ? 0.1231 0.1261 0.1584 -0.0096 0.0071  -0.0142 61  MET   A C   
1403 O O   . MET   A 61  ? 0.1274 0.1306 0.1700 -0.0051 0.0115  -0.0076 61  MET   A O   
1404 C CB  . MET   A 61  ? 0.1317 0.1357 0.1425 -0.0011 0.0025  -0.0109 61  MET   A CB  
1405 C CG  . MET   A 61  ? 0.1365 0.1424 0.1584 0.0009  0.0070  -0.0002 61  MET   A CG  
1406 S SD  . MET   A 61  ? 0.1336 0.1436 0.1941 -0.0099 -0.0001 -0.0240 61  MET   A SD  
1407 C CE  . MET   A 61  ? 0.1534 0.1613 0.2099 -0.0195 0.0070  -0.0229 61  MET   A CE  
1417 N N   . GLN   A 62  ? 0.1228 0.1212 0.1691 -0.0073 0.0033  -0.0083 62  GLN   A N   
1418 C CA  . GLN   A 62  ? 0.1290 0.1208 0.1702 -0.0047 -0.0000 -0.0023 62  GLN   A CA  
1419 C C   . GLN   A 62  ? 0.1280 0.1172 0.1660 -0.0020 0.0095  0.0019  62  GLN   A C   
1420 O O   . GLN   A 62  ? 0.1317 0.1345 0.1687 -0.0020 0.0093  0.0038  62  GLN   A O   
1421 C CB  . GLN   A 62  ? 0.1281 0.1187 0.1810 0.0004  0.0012  0.0016  62  GLN   A CB  
1422 C CG  . GLN   A 62  ? 0.1333 0.1186 0.1746 0.0003  -0.0002 0.0086  62  GLN   A CG  
1423 C CD  . GLN   A 62  ? 0.1439 0.1243 0.1640 0.0000  0.0079  0.0023  62  GLN   A CD  
1424 O OE1 . GLN   A 62  ? 0.1435 0.1366 0.1808 0.0032  0.0053  -0.0004 62  GLN   A OE1 
1425 N NE2 . GLN   A 62  ? 0.1538 0.1318 0.1726 0.0044  0.0012  -0.0144 62  GLN   A NE2 
1434 N N   . VAL   A 63  ? 0.1227 0.1242 0.1863 -0.0058 0.0105  -0.0258 63  VAL   A N   
1435 C CA  . VAL   A 63  ? 0.1289 0.1348 0.2024 -0.0133 0.0048  -0.0241 63  VAL   A CA  
1436 C C   . VAL   A 63  ? 0.1193 0.1315 0.1893 -0.0163 -0.0076 -0.0202 63  VAL   A C   
1437 O O   . VAL   A 63  ? 0.1194 0.1371 0.2006 -0.0160 -0.0029 -0.0092 63  VAL   A O   
1438 C CB  . VAL   A 63  ? 0.1488 0.1526 0.2392 -0.0109 -0.0050 -0.0460 63  VAL   A CB  
1439 C CG1 . VAL   A 63  ? 0.1508 0.1730 0.2633 -0.0121 -0.0113 -0.0611 63  VAL   A CG1 
1440 C CG2 . VAL   A 63  ? 0.1556 0.1425 0.2500 -0.0149 0.0113  -0.0451 63  VAL   A CG2 
1450 N N   . GLU   A 64  ? 0.1247 0.1384 0.1780 -0.0089 -0.0028 -0.0152 64  GLU   A N   
1451 C CA  . GLU   A 64  ? 0.1212 0.1388 0.1597 -0.0152 -0.0084 -0.0064 64  GLU   A CA  
1452 C C   . GLU   A 64  ? 0.1186 0.1270 0.1715 -0.0116 0.0050  -0.0014 64  GLU   A C   
1453 O O   . GLU   A 64  ? 0.1237 0.1369 0.1901 -0.0033 0.0016  -0.0064 64  GLU   A O   
1454 C CB  . GLU   A 64  ? 0.1330 0.1537 0.1743 -0.0114 -0.0030 -0.0064 64  GLU   A CB  
1455 C CG  . GLU   A 64  ? 0.1443 0.1581 0.1964 -0.0144 0.0034  -0.0041 64  GLU   A CG  
1456 C CD  . GLU   A 64  ? 0.1507 0.1658 0.2004 -0.0211 0.0180  -0.0056 64  GLU   A CD  
1457 O OE1 . GLU   A 64  ? 0.1486 0.1727 0.2168 -0.0284 0.0239  -0.0053 64  GLU   A OE1 
1458 O OE2 . GLU   A 64  ? 0.1678 0.1692 0.1948 -0.0295 0.0003  0.0067  64  GLU   A OE2 
1465 N N   . SER   A 65  ? 0.1134 0.1319 0.1708 -0.0016 0.0029  -0.0016 65  SER   A N   
1466 C CA  . SER   A 65  ? 0.1219 0.1238 0.1630 0.0004  0.0027  -0.0128 65  SER   A CA  
1467 C C   . SER   A 65  ? 0.1228 0.1315 0.1643 0.0010  -0.0015 -0.0122 65  SER   A C   
1468 O O   . SER   A 65  ? 0.1331 0.1322 0.1816 0.0006  0.0084  -0.0106 65  SER   A O   
1469 C CB  . SER   A 65  ? 0.1222 0.1265 0.1634 -0.0079 0.0037  0.0030  65  SER   A CB  
1470 O OG  . SER   A 65  ? 0.1204 0.1397 0.1759 -0.0068 -0.0017 0.0043  65  SER   A OG  
1476 N N   . ASP   A 66  ? 0.1265 0.1284 0.1690 -0.0012 0.0130  0.0011  66  ASP   A N   
1477 C CA  . ASP   A 66  ? 0.1330 0.1424 0.1864 0.0021  0.0154  0.0118  66  ASP   A CA  
1478 C C   . ASP   A 66  ? 0.1293 0.1385 0.1845 -0.0063 0.0146  0.0149  66  ASP   A C   
1479 O O   . ASP   A 66  ? 0.1348 0.1516 0.2114 -0.0027 0.0247  0.0206  66  ASP   A O   
1480 C CB  . ASP   A 66  ? 0.1510 0.1517 0.2184 0.0100  0.0146  0.0291  66  ASP   A CB  
1481 C CG  . ASP   A 66  ? 0.1752 0.1640 0.2549 0.0064  0.0041  0.0453  66  ASP   A CG  
1482 O OD1 . ASP   A 66  ? 0.1717 0.1852 0.2489 -0.0029 -0.0063 0.0535  66  ASP   A OD1 
1483 O OD2 . ASP   A 66  ? 0.1937 0.1827 0.3354 0.0262  -0.0177 0.0243  66  ASP   A OD2 
1488 N N   . ASP   A 67  ? 0.1269 0.1391 0.1947 -0.0018 0.0145  0.0118  67  ASP   A N   
1489 C CA  . ASP   A 67  ? 0.1262 0.1600 0.2104 0.0005  0.0059  0.0232  67  ASP   A CA  
1490 C C   . ASP   A 67  ? 0.1243 0.1613 0.2002 0.0023  0.0181  0.0257  67  ASP   A C   
1491 O O   . ASP   A 67  ? 0.1239 0.1655 0.2235 0.0011  0.0279  0.0324  67  ASP   A O   
1492 C CB  . ASP   A 67  ? 0.1354 0.1697 0.2508 -0.0020 -0.0157 0.0267  67  ASP   A CB  
1493 C CG  . ASP   A 67  ? 0.1327 0.1838 0.2771 -0.0122 -0.0277 0.0403  67  ASP   A CG  
1494 O OD1 . ASP   A 67  ? 0.1427 0.2035 0.3600 -0.0189 -0.0389 0.0477  67  ASP   A OD1 
1495 O OD2 . ASP   A 67  ? 0.1360 0.1852 0.2604 -0.0002 -0.0160 0.0301  67  ASP   A OD2 
1500 N N   . TYR   A 68  ? 0.1231 0.1412 0.2031 0.0076  0.0168  0.0263  68  TYR   A N   
1501 C CA  . TYR   A 68  ? 0.1428 0.1417 0.1981 0.0073  0.0235  0.0276  68  TYR   A CA  
1502 C C   . TYR   A 68  ? 0.1383 0.1368 0.1903 0.0018  0.0263  0.0139  68  TYR   A C   
1503 O O   . TYR   A 68  ? 0.1433 0.1387 0.2044 0.0096  0.0305  0.0125  68  TYR   A O   
1504 C CB  . TYR   A 68  ? 0.1441 0.1392 0.2225 0.0067  0.0473  0.0330  68  TYR   A CB  
1505 C CG  . TYR   A 68  ? 0.1502 0.1524 0.2576 0.0082  0.0652  0.0347  68  TYR   A CG  
1506 C CD1 . TYR   A 68  ? 0.1609 0.1640 0.2901 -0.0189 0.0578  -0.0149 68  TYR   A CD1 
1507 C CD2 . TYR   A 68  ? 0.1711 0.1515 0.2957 0.0110  0.0668  0.0420  68  TYR   A CD2 
1508 C CE1 . TYR   A 68  ? 0.1726 0.1745 0.3243 -0.0221 0.0660  -0.0272 68  TYR   A CE1 
1509 C CE2 . TYR   A 68  ? 0.1729 0.1584 0.3173 -0.0028 0.0826  0.0110  68  TYR   A CE2 
1510 C CZ  . TYR   A 68  ? 0.1753 0.1652 0.3375 -0.0232 0.0681  -0.0228 68  TYR   A CZ  
1511 O OH  . TYR   A 68  ? 0.2076 0.1697 0.3645 -0.0190 0.0469  -0.0555 68  TYR   A OH  
1521 N N   . ILE   A 69  ? 0.1293 0.1324 0.1888 0.0035  0.0193  0.0154  69  ILE   A N   
1522 C CA  . ILE   A 69  ? 0.1371 0.1370 0.1887 0.0065  0.0097  -0.0045 69  ILE   A CA  
1523 C C   . ILE   A 69  ? 0.1410 0.1398 0.1778 0.0025  0.0178  0.0085  69  ILE   A C   
1524 O O   . ILE   A 69  ? 0.1473 0.1456 0.1729 -0.0006 0.0196  0.0190  69  ILE   A O   
1525 C CB  . ILE   A 69  ? 0.1426 0.1631 0.1924 0.0060  0.0106  -0.0146 69  ILE   A CB  
1526 C CG1 . ILE   A 69  ? 0.1455 0.1707 0.2024 0.0054  0.0180  -0.0295 69  ILE   A CG1 
1527 C CG2 . ILE   A 69  ? 0.1657 0.1844 0.2102 0.0129  -0.0022 -0.0252 69  ILE   A CG2 
1528 C CD1 . ILE   A 69  ? 0.1434 0.1821 0.2262 -0.0039 0.0217  -0.0296 69  ILE   A CD1 
1540 N N   . ALA   A 70  ? 0.1445 0.1416 0.1917 -0.0077 0.0265  0.0137  70  ALA   A N   
1541 C CA  . ALA   A 70  ? 0.1482 0.1489 0.2090 -0.0156 0.0340  0.0144  70  ALA   A CA  
1542 C C   . ALA   A 70  ? 0.1466 0.1611 0.2044 -0.0191 0.0336  0.0121  70  ALA   A C   
1543 O O   . ALA   A 70  ? 0.1679 0.1969 0.2233 0.0015  0.0454  0.0334  70  ALA   A O   
1544 C CB  . ALA   A 70  ? 0.1489 0.1482 0.2406 -0.0169 0.0248  0.0055  70  ALA   A CB  
1550 N N   . THR   A 71  ? 0.1374 0.1611 0.1974 -0.0094 0.0246  0.0223  71  THR   A N   
1551 C CA  . THR   A 71  ? 0.1472 0.1772 0.2133 0.0062  0.0276  0.0201  71  THR   A CA  
1552 C C   . THR   A 71  ? 0.1393 0.1727 0.2364 0.0117  0.0325  0.0165  71  THR   A C   
1553 O O   . THR   A 71  ? 0.1500 0.2005 0.2827 0.0106  0.0481  -0.0036 71  THR   A O   
1554 C CB  . THR   A 71  ? 0.1777 0.2043 0.2447 0.0148  -0.0058 0.0317  71  THR   A CB  
1555 O OG1 . THR   A 71  ? 0.2042 0.2258 0.2589 0.0104  -0.0299 0.0227  71  THR   A OG1 
1556 C CG2 . THR   A 71  ? 0.1920 0.2222 0.2690 0.0218  -0.0239 0.0464  71  THR   A CG2 
1564 N N   . ASN   A 72  ? 0.1396 0.1523 0.2186 0.0084  0.0239  0.0186  72  ASN   A N   
1565 C CA  . ASN   A 72  ? 0.1422 0.1553 0.2347 0.0152  0.0355  0.0234  72  ASN   A CA  
1566 C C   . ASN   A 72  ? 0.1562 0.1514 0.2230 0.0067  0.0501  0.0167  72  ASN   A C   
1567 O O   . ASN   A 72  ? 0.1760 0.1519 0.2466 0.0140  0.0431  0.0029  72  ASN   A O   
1568 C CB  . ASN   A 72  ? 0.1626 0.1654 0.2267 0.0200  0.0445  0.0197  72  ASN   A CB  
1569 C CG  . ASN   A 72  ? 0.1941 0.1832 0.2301 0.0282  0.0407  0.0201  72  ASN   A CG  
1570 O OD1 . ASN   A 72  ? 0.2087 0.2121 0.2498 0.0280  0.0491  0.0340  72  ASN   A OD1 
1571 N ND2 . ASN   A 72  ? 0.2143 0.1795 0.2216 0.0567  0.0196  0.0227  72  ASN   A ND2 
1578 N N   . GLY   A 73  ? 0.1595 0.1506 0.2046 0.0045  0.0437  0.0109  73  GLY   A N   
1579 C CA  . GLY   A 73  ? 0.1625 0.1500 0.1859 -0.0043 0.0440  0.0049  73  GLY   A CA  
1580 C C   . GLY   A 73  ? 0.1652 0.1431 0.1707 0.0008  0.0494  0.0252  73  GLY   A C   
1581 O O   . GLY   A 73  ? 0.1658 0.1486 0.1903 0.0100  0.0374  0.0275  73  GLY   A O   
1585 N N   . PRO   A 74  ? 0.1775 0.1436 0.1893 -0.0083 0.0437  0.0133  74  PRO   A N   
1586 C CA  . PRO   A 74  ? 0.1739 0.1430 0.1949 -0.0013 0.0495  0.0162  74  PRO   A CA  
1587 C C   . PRO   A 74  ? 0.1665 0.1256 0.1848 0.0012  0.0406  0.0081  74  PRO   A C   
1588 O O   . PRO   A 74  ? 0.1740 0.1300 0.2067 0.0023  0.0426  -0.0059 74  PRO   A O   
1589 C CB  . PRO   A 74  ? 0.1924 0.1752 0.2226 0.0008  0.0493  0.0280  74  PRO   A CB  
1590 C CG  . PRO   A 74  ? 0.2203 0.2063 0.2624 -0.0168 0.0339  0.0168  74  PRO   A CG  
1591 C CD  . PRO   A 74  ? 0.2021 0.1775 0.2059 -0.0170 0.0335  0.0114  74  PRO   A CD  
1599 N N   . LEU   A 75  ? 0.1615 0.1194 0.1662 0.0014  0.0294  0.0046  75  LEU   A N   
1600 C CA  . LEU   A 75  ? 0.1668 0.1189 0.1542 -0.0037 0.0163  0.0087  75  LEU   A CA  
1601 C C   . LEU   A 75  ? 0.1679 0.1352 0.1494 0.0087  0.0136  0.0152  75  LEU   A C   
1602 O O   . LEU   A 75  ? 0.2010 0.1550 0.1568 0.0165  0.0112  0.0077  75  LEU   A O   
1603 C CB  . LEU   A 75  ? 0.1679 0.1212 0.1611 -0.0091 0.0111  0.0160  75  LEU   A CB  
1604 C CG  . LEU   A 75  ? 0.1820 0.1598 0.1757 -0.0309 0.0162  0.0078  75  LEU   A CG  
1605 C CD1 . LEU   A 75  ? 0.1915 0.2122 0.1921 -0.0309 0.0152  -0.0038 75  LEU   A CD1 
1606 C CD2 . LEU   A 75  ? 0.2135 0.1996 0.2300 -0.0072 0.0168  0.0091  75  LEU   A CD2 
1618 N N   . LYS   A 76  ? 0.1649 0.1292 0.1600 -0.0033 0.0115  0.0039  76  LYS   A N   
1619 C CA  . LYS   A 76  ? 0.1647 0.1549 0.1630 -0.0069 0.0086  -0.0141 76  LYS   A CA  
1620 C C   . LYS   A 76  ? 0.1607 0.1367 0.1298 -0.0002 0.0088  0.0010  76  LYS   A C   
1621 O O   . LYS   A 76  ? 0.1647 0.1277 0.1506 0.0023  0.0155  0.0050  76  LYS   A O   
1622 C CB  . LYS   A 76  ? 0.1648 0.1777 0.2074 0.0062  0.0115  -0.0435 76  LYS   A CB  
1623 C CG  . LYS   A 76  ? 0.1713 0.1666 0.2602 0.0028  -0.0052 -0.0288 76  LYS   A CG  
1624 C CD  . LYS   A 76  ? 0.1845 0.1702 0.2965 0.0124  -0.0113 -0.0343 76  LYS   A CD  
1625 C CE  . LYS   A 76  ? 0.1982 0.1993 0.3504 0.0065  0.0062  -0.0406 76  LYS   A CE  
1626 N NZ  . LYS   A 76  ? 0.1972 0.1968 0.3923 -0.0062 -0.0001 -0.0500 76  LYS   A NZ  
1640 N N   . VAL   A 77  ? 0.1751 0.1454 0.1388 -0.0008 0.0227  0.0154  77  VAL   A N   
1641 C CA  . VAL   A 77  ? 0.1661 0.1469 0.1351 0.0107  0.0218  0.0141  77  VAL   A CA  
1642 C C   . VAL   A 77  ? 0.1622 0.1374 0.1519 0.0113  0.0123  0.0055  77  VAL   A C   
1643 O O   . VAL   A 77  ? 0.1709 0.1434 0.1487 0.0137  0.0300  -0.0052 77  VAL   A O   
1644 C CB  . VAL   A 77  ? 0.1810 0.1648 0.1528 0.0051  0.0153  0.0231  77  VAL   A CB  
1645 C CG1 . VAL   A 77  ? 0.1803 0.1818 0.1793 0.0124  0.0031  0.0085  77  VAL   A CG1 
1646 C CG2 . VAL   A 77  ? 0.2075 0.1733 0.1753 -0.0026 0.0051  0.0231  77  VAL   A CG2 
1656 N N   . GLY   A 78  ? 0.1582 0.1311 0.1433 0.0035  0.0203  0.0065  78  GLY   A N   
1657 C CA  . GLY   A 78  ? 0.1517 0.1342 0.1628 0.0031  0.0246  0.0087  78  GLY   A CA  
1658 C C   . GLY   A 78  ? 0.1426 0.1313 0.1491 0.0065  0.0170  0.0142  78  GLY   A C   
1659 O O   . GLY   A 78  ? 0.1436 0.1411 0.1702 0.0032  0.0153  0.0249  78  GLY   A O   
1663 N N   . GLY   A 79  ? 0.1449 0.1281 0.1462 0.0037  0.0163  0.0133  79  GLY   A N   
1664 C CA  . GLY   A 79  ? 0.1460 0.1299 0.1497 -0.0040 0.0098  0.0092  79  GLY   A CA  
1665 C C   . GLY   A 79  ? 0.1299 0.1290 0.1479 -0.0035 0.0088  0.0054  79  GLY   A C   
1666 O O   . GLY   A 79  ? 0.1335 0.1388 0.1707 0.0149  0.0096  0.0043  79  GLY   A O   
1670 N N   . SER   A 80  ? 0.1244 0.1385 0.1709 -0.0008 0.0150  -0.0080 80  SER   A N   
1671 C CA  . SER   A 80  ? 0.1266 0.1321 0.1501 0.0002  0.0135  -0.0000 80  SER   A CA  
1672 C C   . SER   A 80  ? 0.1281 0.1340 0.1478 -0.0052 0.0136  0.0124  80  SER   A C   
1673 O O   . SER   A 80  ? 0.1272 0.1543 0.1877 0.0061  0.0160  -0.0043 80  SER   A O   
1674 C CB  . SER   A 80  ? 0.1437 0.1328 0.1818 -0.0051 0.0073  0.0046  80  SER   A CB  
1675 O OG  . SER   A 80  ? 0.1657 0.1318 0.2236 0.0053  -0.0008 0.0239  80  SER   A OG  
1681 N N   . CYS   A 81  ? 0.1209 0.1293 0.1515 0.0049  -0.0067 0.0126  81  CYS   A N   
1682 C CA  . CYS   A 81  ? 0.1184 0.1393 0.1512 -0.0030 -0.0083 0.0258  81  CYS   A CA  
1683 C C   . CYS   A 81  ? 0.1178 0.1371 0.1501 -0.0140 -0.0046 0.0278  81  CYS   A C   
1684 O O   . CYS   A 81  ? 0.1170 0.1685 0.1699 -0.0018 -0.0024 0.0330  81  CYS   A O   
1685 C CB  . CYS   A 81  ? 0.1313 0.1492 0.1705 -0.0116 -0.0006 0.0262  81  CYS   A CB  
1686 S SG  . CYS   A 81  ? 0.1457 0.1367 0.1687 -0.0122 0.0014  0.0122  81  CYS   A SG  
1692 N N   . VAL   A 82  ? 0.1265 0.1427 0.1525 -0.0032 -0.0116 0.0195  82  VAL   A N   
1693 C CA  . VAL   A 82  ? 0.1406 0.1462 0.1531 -0.0032 -0.0112 0.0245  82  VAL   A CA  
1694 C C   . VAL   A 82  ? 0.1381 0.1534 0.1658 -0.0050 -0.0087 0.0183  82  VAL   A C   
1695 O O   . VAL   A 82  ? 0.1270 0.1628 0.1897 -0.0071 -0.0018 -0.0070 82  VAL   A O   
1696 C CB  . VAL   A 82  ? 0.1673 0.1637 0.1741 0.0010  0.0009  0.0253  82  VAL   A CB  
1697 C CG1 . VAL   A 82  ? 0.1846 0.1766 0.1974 0.0046  0.0067  0.0215  82  VAL   A CG1 
1698 C CG2 . VAL   A 82  ? 0.1766 0.1639 0.2080 -0.0022 -0.0036 0.0218  82  VAL   A CG2 
1708 N N   . LEU   A 83  ? 0.1299 0.1455 0.1585 -0.0110 -0.0054 0.0076  83  LEU   A N   
1709 C CA  . LEU   A 83  ? 0.1288 0.1528 0.1466 -0.0102 -0.0042 0.0031  83  LEU   A CA  
1710 C C   . LEU   A 83  ? 0.1348 0.1592 0.1450 -0.0123 -0.0133 0.0067  83  LEU   A C   
1711 O O   . LEU   A 83  ? 0.1444 0.1582 0.1708 -0.0171 -0.0024 0.0198  83  LEU   A O   
1712 C CB  . LEU   A 83  ? 0.1382 0.1599 0.1597 -0.0132 -0.0082 0.0111  83  LEU   A CB  
1713 C CG  . LEU   A 83  ? 0.1492 0.1685 0.1697 -0.0191 0.0018  0.0020  83  LEU   A CG  
1714 C CD1 . LEU   A 83  ? 0.1584 0.1656 0.1781 -0.0247 -0.0048 0.0277  83  LEU   A CD1 
1715 C CD2 . LEU   A 83  ? 0.1473 0.1900 0.1931 -0.0172 0.0217  0.0184  83  LEU   A CD2 
1727 N N   . SER   A 84  ? 0.1481 0.1670 0.1477 -0.0154 -0.0118 0.0072  84  SER   A N   
1728 C CA  . SER   A 84  ? 0.1644 0.1737 0.1350 -0.0160 -0.0115 0.0004  84  SER   A CA  
1729 C C   . SER   A 84  ? 0.1638 0.1721 0.1183 -0.0243 0.0096  0.0106  84  SER   A C   
1730 O O   . SER   A 84  ? 0.1664 0.1821 0.1202 -0.0151 -0.0036 0.0126  84  SER   A O   
1731 C CB  . SER   A 84  ? 0.1731 0.1879 0.1513 -0.0126 -0.0037 -0.0018 84  SER   A CB  
1732 O OG  . SER   A 84  ? 0.1762 0.2040 0.1604 -0.0106 -0.0140 -0.0223 84  SER   A OG  
1738 N N   . GLY   A 85  ? 0.1754 0.1861 0.1255 -0.0239 0.0056  -0.0002 85  GLY   A N   
1739 C CA  . GLY   A 85  ? 0.1774 0.1918 0.1502 -0.0269 0.0058  -0.0110 85  GLY   A CA  
1740 C C   . GLY   A 85  ? 0.1728 0.1999 0.1455 -0.0227 -0.0016 -0.0032 85  GLY   A C   
1741 O O   . GLY   A 85  ? 0.1721 0.2108 0.1577 -0.0277 0.0162  -0.0144 85  GLY   A O   
1745 N N   . HIS   A 86  ? 0.1724 0.1914 0.1424 -0.0246 -0.0066 0.0052  86  HIS   A N   
1746 C CA  . HIS   A 86  ? 0.1918 0.1994 0.1409 -0.0310 -0.0007 0.0026  86  HIS   A CA  
1747 C C   . HIS   A 86  ? 0.2149 0.2138 0.1436 -0.0303 0.0021  0.0004  86  HIS   A C   
1748 O O   . HIS   A 86  ? 0.2268 0.2372 0.1401 -0.0226 0.0146  -0.0048 86  HIS   A O   
1749 C CB  . HIS   A 86  ? 0.1907 0.1862 0.1448 -0.0264 0.0059  -0.0013 86  HIS   A CB  
1750 C CG  . HIS   A 86  ? 0.1828 0.1915 0.1490 -0.0165 0.0049  0.0043  86  HIS   A CG  
1751 N ND1 . HIS   A 86  ? 0.1864 0.1889 0.1857 -0.0212 0.0024  0.0043  86  HIS   A ND1 
1752 C CD2 . HIS   A 86  ? 0.1840 0.1837 0.1481 -0.0108 0.0032  0.0046  86  HIS   A CD2 
1753 C CE1 . HIS   A 86  ? 0.1869 0.1898 0.1777 -0.0157 0.0251  0.0201  86  HIS   A CE1 
1754 N NE2 . HIS   A 86  ? 0.1870 0.1867 0.1695 -0.0010 0.0154  0.0305  86  HIS   A NE2 
1762 N N   . ASN   A 87  ? 0.2289 0.2247 0.1582 -0.0241 0.0304  -0.0193 87  ASN   A N   
1763 C CA  . ASN   A 87  ? 0.2483 0.2374 0.1642 -0.0220 0.0483  -0.0278 87  ASN   A CA  
1764 C C   . ASN   A 87  ? 0.2443 0.2554 0.2023 -0.0294 0.0647  -0.0157 87  ASN   A C   
1765 O O   . ASN   A 87  ? 0.2664 0.2725 0.2453 -0.0439 0.0956  -0.0277 87  ASN   A O   
1766 C CB  . ASN   A 87  ? 0.2706 0.2445 0.1831 -0.0106 0.0486  -0.0255 87  ASN   A CB  
1767 C CG  . ASN   A 87  ? 0.2828 0.2545 0.1871 0.0016  0.0629  -0.0120 87  ASN   A CG  
1768 O OD1 . ASN   A 87  ? 0.2999 0.2543 0.1883 0.0179  0.0587  -0.0057 87  ASN   A OD1 
1769 N ND2 . ASN   A 87  ? 0.2839 0.2741 0.1932 0.0030  0.0639  -0.0070 87  ASN   A ND2 
1776 N N   . LEU   A 88  ? 0.2182 0.2445 0.1992 -0.0344 0.0367  -0.0031 88  LEU   A N   
1777 C CA  . LEU   A 88  ? 0.2004 0.2383 0.2017 -0.0404 0.0410  0.0033  88  LEU   A CA  
1778 C C   . LEU   A 88  ? 0.1941 0.2393 0.1923 -0.0426 0.0398  0.0195  88  LEU   A C   
1779 O O   . LEU   A 88  ? 0.1963 0.2457 0.2316 -0.0381 0.0407  0.0364  88  LEU   A O   
1780 C CB  . LEU   A 88  ? 0.1986 0.2445 0.2222 -0.0458 0.0100  0.0039  88  LEU   A CB  
1781 C CG  . LEU   A 88  ? 0.2143 0.2565 0.2544 -0.0422 0.0005  0.0086  88  LEU   A CG  
1782 C CD1 . LEU   A 88  ? 0.2281 0.2656 0.2488 -0.0405 -0.0016 -0.0016 88  LEU   A CD1 
1783 C CD2 . LEU   A 88  ? 0.2237 0.2639 0.2939 -0.0375 0.0023  0.0076  88  LEU   A CD2 
1795 N N   . ALA   A 89  ? 0.1979 0.2271 0.1614 -0.0361 0.0315  0.0024  89  ALA   A N   
1796 C CA  . ALA   A 89  ? 0.2017 0.2230 0.1433 -0.0301 0.0149  0.0124  89  ALA   A CA  
1797 C C   . ALA   A 89  ? 0.2094 0.2245 0.1466 -0.0292 -0.0005 0.0155  89  ALA   A C   
1798 O O   . ALA   A 89  ? 0.2072 0.2216 0.1873 -0.0365 -0.0080 -0.0059 89  ALA   A O   
1799 C CB  . ALA   A 89  ? 0.1912 0.2234 0.1204 -0.0314 0.0057  0.0093  89  ALA   A CB  
1805 N N   . LYS   A 90  ? 0.2166 0.2405 0.1558 -0.0430 -0.0255 0.0164  90  LYS   A N   
1806 C CA  . LYS   A 90  ? 0.2300 0.2567 0.1259 -0.0350 -0.0374 0.0099  90  LYS   A CA  
1807 C C   . LYS   A 90  ? 0.2128 0.2408 0.1151 -0.0318 -0.0326 -0.0017 90  LYS   A C   
1808 O O   . LYS   A 90  ? 0.2082 0.2580 0.1802 -0.0355 -0.0397 -0.0089 90  LYS   A O   
1809 C CB  . LYS   A 90  ? 0.2551 0.2917 0.1847 -0.0316 -0.0458 0.0393  90  LYS   A CB  
1810 C CG  . LYS   A 90  ? 0.2982 0.3270 0.2853 -0.0289 -0.0461 0.0494  90  LYS   A CG  
1811 C CD  . LYS   A 90  ? 0.3465 0.3671 0.3897 -0.0318 -0.0334 0.0578  90  LYS   A CD  
1812 C CE  . LYS   A 90  ? 0.3805 0.3987 0.4615 -0.0341 -0.0203 0.0568  90  LYS   A CE  
1813 N NZ  . LYS   A 90  ? 0.3958 0.4085 0.5096 -0.0349 -0.0130 0.0527  90  LYS   A NZ  
1827 N N   . HIS   A 91  ? 0.2019 0.2078 0.0862 -0.0224 -0.0393 0.0132  91  HIS   A N   
1828 C CA  . HIS   A 91  ? 0.1879 0.1843 0.1056 -0.0192 -0.0343 0.0183  91  HIS   A CA  
1829 C C   . HIS   A 91  ? 0.1654 0.1728 0.0879 -0.0169 -0.0186 0.0162  91  HIS   A C   
1830 O O   . HIS   A 91  ? 0.1524 0.1838 0.1299 -0.0270 -0.0035 0.0186  91  HIS   A O   
1831 C CB  . HIS   A 91  ? 0.1990 0.2088 0.1619 -0.0003 -0.0454 0.0192  91  HIS   A CB  
1832 C CG  . HIS   A 91  ? 0.2451 0.2602 0.2431 0.0104  -0.0722 0.0091  91  HIS   A CG  
1833 N ND1 . HIS   A 91  ? 0.2579 0.2911 0.2978 0.0149  -0.0851 -0.0155 91  HIS   A ND1 
1834 C CD2 . HIS   A 91  ? 0.2674 0.2820 0.2720 0.0182  -0.0850 0.0188  91  HIS   A CD2 
1835 C CE1 . HIS   A 91  ? 0.2700 0.2992 0.3110 0.0203  -0.0837 -0.0013 91  HIS   A CE1 
1836 N NE2 . HIS   A 91  ? 0.2787 0.2974 0.3007 0.0258  -0.0925 0.0069  91  HIS   A NE2 
1844 N N   . CYS   A 92  ? 0.1475 0.1662 0.1146 -0.0152 -0.0125 0.0184  92  CYS   A N   
1845 C CA  . CYS   A 92  ? 0.1365 0.1532 0.1293 -0.0128 0.0014  0.0133  92  CYS   A CA  
1846 C C   . CYS   A 92  ? 0.1282 0.1456 0.1314 -0.0150 0.0018  0.0099  92  CYS   A C   
1847 O O   . CYS   A 92  ? 0.1355 0.1555 0.1566 -0.0202 -0.0015 0.0095  92  CYS   A O   
1848 C CB  . CYS   A 92  ? 0.1397 0.1577 0.1563 -0.0073 0.0037  0.0092  92  CYS   A CB  
1849 S SG  . CYS   A 92  ? 0.1397 0.1440 0.1501 -0.0122 -0.0021 0.0079  92  CYS   A SG  
1855 N N   . LEU   A 93  ? 0.1265 0.1358 0.1439 -0.0107 0.0087  0.0103  93  LEU   A N   
1856 C CA  . LEU   A 93  ? 0.1213 0.1273 0.1248 -0.0071 -0.0007 0.0102  93  LEU   A CA  
1857 C C   . LEU   A 93  ? 0.1191 0.1226 0.1319 0.0002  0.0084  0.0038  93  LEU   A C   
1858 O O   . LEU   A 93  ? 0.1142 0.1361 0.1403 -0.0042 0.0037  0.0050  93  LEU   A O   
1859 C CB  . LEU   A 93  ? 0.1331 0.1265 0.1506 -0.0038 -0.0111 0.0157  93  LEU   A CB  
1860 C CG  . LEU   A 93  ? 0.1364 0.1293 0.1489 -0.0091 0.0035  0.0179  93  LEU   A CG  
1861 C CD1 . LEU   A 93  ? 0.1439 0.1359 0.1800 -0.0046 0.0166  0.0110  93  LEU   A CD1 
1862 C CD2 . LEU   A 93  ? 0.1472 0.1290 0.1762 -0.0084 0.0024  0.0113  93  LEU   A CD2 
1874 N N   . HIS   A 94  ? 0.1131 0.1215 0.1356 -0.0025 0.0114  0.0174  94  HIS   A N   
1875 C CA  . HIS   A 94  ? 0.1146 0.1261 0.1412 -0.0030 0.0058  0.0130  94  HIS   A CA  
1876 C C   . HIS   A 94  ? 0.1129 0.1217 0.1445 -0.0059 0.0054  0.0035  94  HIS   A C   
1877 O O   . HIS   A 94  ? 0.1219 0.1396 0.1762 -0.0020 0.0070  -0.0122 94  HIS   A O   
1878 C CB  . HIS   A 94  ? 0.1165 0.1199 0.1439 -0.0084 -0.0067 0.0076  94  HIS   A CB  
1879 C CG  . HIS   A 94  ? 0.1228 0.1204 0.1418 -0.0062 -0.0021 0.0090  94  HIS   A CG  
1880 N ND1 . HIS   A 94  ? 0.1214 0.1175 0.1448 -0.0026 0.0039  0.0115  94  HIS   A ND1 
1881 C CD2 . HIS   A 94  ? 0.1262 0.1305 0.1550 -0.0031 -0.0087 0.0048  94  HIS   A CD2 
1882 C CE1 . HIS   A 94  ? 0.1279 0.1236 0.1448 -0.0070 -0.0076 0.0081  94  HIS   A CE1 
1883 N NE2 . HIS   A 94  ? 0.1307 0.1304 0.1452 -0.0086 -0.0021 0.0011  94  HIS   A NE2 
1891 N N   . VAL   A 95  ? 0.1123 0.1157 0.1245 -0.0028 0.0087  0.0044  95  VAL   A N   
1892 C CA  . VAL   A 95  ? 0.1204 0.1244 0.1231 -0.0033 0.0126  0.0119  95  VAL   A CA  
1893 C C   . VAL   A 95  ? 0.1248 0.1193 0.1077 -0.0144 0.0060  0.0066  95  VAL   A C   
1894 O O   . VAL   A 95  ? 0.1262 0.1325 0.1358 0.0088  0.0066  0.0049  95  VAL   A O   
1895 C CB  . VAL   A 95  ? 0.1212 0.1230 0.1527 -0.0068 0.0039  0.0122  95  VAL   A CB  
1896 C CG1 . VAL   A 95  ? 0.1374 0.1248 0.1567 -0.0111 -0.0010 -0.0039 95  VAL   A CG1 
1897 C CG2 . VAL   A 95  ? 0.1310 0.1311 0.1478 -0.0126 0.0090  0.0252  95  VAL   A CG2 
1907 N N   . VAL   A 96  ? 0.1278 0.1249 0.0974 -0.0024 0.0067  0.0095  96  VAL   A N   
1908 C CA  . VAL   A 96  ? 0.1401 0.1239 0.1253 -0.0030 0.0092  0.0125  96  VAL   A CA  
1909 C C   . VAL   A 96  ? 0.1356 0.1294 0.1349 -0.0005 0.0104  0.0112  96  VAL   A C   
1910 O O   . VAL   A 96  ? 0.1440 0.1334 0.1569 -0.0061 0.0171  -0.0070 96  VAL   A O   
1911 C CB  . VAL   A 96  ? 0.1349 0.1219 0.1457 -0.0031 0.0192  0.0089  96  VAL   A CB  
1912 C CG1 . VAL   A 96  ? 0.1461 0.1282 0.1344 -0.0049 0.0115  0.0076  96  VAL   A CG1 
1913 C CG2 . VAL   A 96  ? 0.1324 0.1344 0.1622 -0.0101 0.0152  0.0071  96  VAL   A CG2 
1923 N N   . GLY   A 97  ? 0.1335 0.1344 0.1368 -0.0055 0.0031  0.0127  97  GLY   A N   
1924 C CA  . GLY   A 97  ? 0.1430 0.1423 0.1278 -0.0048 -0.0008 0.0084  97  GLY   A CA  
1925 C C   . GLY   A 97  ? 0.1452 0.1532 0.1260 -0.0025 0.0011  0.0074  97  GLY   A C   
1926 O O   . GLY   A 97  ? 0.1594 0.1531 0.1454 -0.0089 -0.0001 0.0170  97  GLY   A O   
1930 N N   . PRO   A 98  ? 0.1549 0.1524 0.1116 0.0041  -0.0090 0.0162  98  PRO   A N   
1931 C CA  . PRO   A 98  ? 0.1616 0.1809 0.1296 0.0009  -0.0062 -0.0004 98  PRO   A CA  
1932 C C   . PRO   A 98  ? 0.1702 0.1907 0.1288 -0.0144 -0.0047 0.0253  98  PRO   A C   
1933 O O   . PRO   A 98  ? 0.1630 0.1677 0.1589 -0.0080 -0.0012 0.0247  98  PRO   A O   
1934 C CB  . PRO   A 98  ? 0.1739 0.1937 0.1185 0.0117  -0.0059 -0.0018 98  PRO   A CB  
1935 C CG  . PRO   A 98  ? 0.1821 0.1765 0.1356 0.0111  0.0005  -0.0109 98  PRO   A CG  
1936 C CD  . PRO   A 98  ? 0.1670 0.1516 0.1171 0.0071  0.0005  0.0057  98  PRO   A CD  
1944 N N   A ASN   A 99  ? 0.1748 0.2107 0.1220 -0.0165 -0.0010 0.0437  99  ASN   A N   
1945 N N   B ASN   A 99  ? 0.1898 0.1977 0.1431 -0.0070 -0.0167 0.0462  99  ASN   A N   
1946 C CA  A ASN   A 99  ? 0.1961 0.2240 0.1161 -0.0262 -0.0052 0.0609  99  ASN   A CA  
1947 C CA  B ASN   A 99  ? 0.2162 0.2017 0.1586 -0.0029 -0.0287 0.0606  99  ASN   A CA  
1948 C C   A ASN   A 99  ? 0.2127 0.2641 0.1131 -0.0405 -0.0047 0.0763  99  ASN   A C   
1949 C C   B ASN   A 99  ? 0.2344 0.2138 0.1730 -0.0002 -0.0266 0.0549  99  ASN   A C   
1950 O O   A ASN   A 99  ? 0.2181 0.2778 0.1255 -0.0371 -0.0017 0.0659  99  ASN   A O   
1951 O O   B ASN   A 99  ? 0.2359 0.1956 0.1767 0.0065  -0.0334 0.0440  99  ASN   A O   
1952 C CB  A ASN   A 99  ? 0.1945 0.2102 0.1423 -0.0240 -0.0159 0.0610  99  ASN   A CB  
1953 C CB  B ASN   A 99  ? 0.2238 0.2014 0.1848 -0.0043 -0.0430 0.0788  99  ASN   A CB  
1954 C CG  A ASN   A 99  ? 0.1979 0.2122 0.1755 -0.0173 -0.0226 0.0444  99  ASN   A CG  
1955 C CG  B ASN   A 99  ? 0.2318 0.2061 0.2023 -0.0039 -0.0530 0.0974  99  ASN   A CG  
1956 O OD1 A ASN   A 99  ? 0.2102 0.2237 0.1883 -0.0090 -0.0253 0.0287  99  ASN   A OD1 
1957 O OD1 B ASN   A 99  ? 0.2427 0.2138 0.1971 -0.0108 -0.0559 0.1047  99  ASN   A OD1 
1958 N ND2 A ASN   A 99  ? 0.2012 0.2064 0.1951 -0.0111 -0.0131 0.0507  99  ASN   A ND2 
1959 N ND2 B ASN   A 99  ? 0.2328 0.2082 0.2148 0.0069  -0.0630 0.0895  99  ASN   A ND2 
1972 N N   A VAL   A 100 ? 0.2218 0.2847 0.1366 -0.0575 -0.0323 0.0681  100 VAL   A N   
1973 N N   B VAL   A 100 ? 0.2469 0.2428 0.1897 -0.0056 -0.0281 0.0494  100 VAL   A N   
1974 C CA  A VAL   A 100 ? 0.2477 0.3139 0.1677 -0.0602 -0.0406 0.0642  100 VAL   A CA  
1975 C CA  B VAL   A 100 ? 0.2615 0.2741 0.2188 -0.0079 -0.0256 0.0442  100 VAL   A CA  
1976 C C   A VAL   A 100 ? 0.2597 0.3311 0.1592 -0.0632 -0.0469 0.0848  100 VAL   A C   
1977 C C   B VAL   A 100 ? 0.2770 0.3010 0.2360 -0.0072 -0.0278 0.0581  100 VAL   A C   
1978 O O   A VAL   A 100 ? 0.2678 0.3411 0.1830 -0.0580 -0.0294 0.0812  100 VAL   A O   
1979 O O   B VAL   A 100 ? 0.2809 0.3110 0.2501 -0.0046 -0.0241 0.0552  100 VAL   A O   
1980 C CB  A VAL   A 100 ? 0.2651 0.3233 0.2053 -0.0593 -0.0490 0.0450  100 VAL   A CB  
1981 C CB  B VAL   A 100 ? 0.2613 0.2750 0.2343 -0.0089 -0.0239 0.0281  100 VAL   A CB  
1982 C CG1 A VAL   A 100 ? 0.2682 0.3295 0.2297 -0.0628 -0.0433 0.0428  100 VAL   A CG1 
1983 C CG1 B VAL   A 100 ? 0.2603 0.2750 0.2438 -0.0082 -0.0201 0.0249  100 VAL   A CG1 
1984 C CG2 A VAL   A 100 ? 0.2705 0.3256 0.2045 -0.0595 -0.0549 0.0360  100 VAL   A CG2 
1985 C CG2 B VAL   A 100 ? 0.2632 0.2766 0.2407 -0.0132 -0.0226 0.0205  100 VAL   A CG2 
2004 N N   A ASN   A 101 ? 0.2674 0.3336 0.1786 -0.0734 -0.0528 0.1200  101 ASN   A N   
2005 N N   B ASN   A 101 ? 0.2882 0.3117 0.2447 -0.0076 -0.0327 0.0777  101 ASN   A N   
2006 C CA  A ASN   A 101 ? 0.2923 0.3390 0.2023 -0.0758 -0.0510 0.1358  101 ASN   A CA  
2007 C CA  B ASN   A 101 ? 0.3011 0.3204 0.2535 -0.0054 -0.0335 0.0920  101 ASN   A CA  
2008 C C   A ASN   A 101 ? 0.3201 0.3619 0.2263 -0.0719 -0.0284 0.1536  101 ASN   A C   
2009 C C   B ASN   A 101 ? 0.3178 0.3322 0.2587 -0.0093 -0.0243 0.1156  101 ASN   A C   
2010 O O   A ASN   A 101 ? 0.3351 0.3674 0.2590 -0.0705 -0.0288 0.1386  101 ASN   A O   
2011 O O   B ASN   A 101 ? 0.3225 0.3248 0.2325 -0.0082 -0.0303 0.1417  101 ASN   A O   
2012 C CB  A ASN   A 101 ? 0.2894 0.3183 0.2086 -0.0787 -0.0717 0.1324  101 ASN   A CB  
2013 C CB  B ASN   A 101 ? 0.2964 0.3149 0.2557 0.0010  -0.0373 0.0770  101 ASN   A CB  
2014 C CG  A ASN   A 101 ? 0.2911 0.3041 0.2005 -0.0829 -0.0815 0.1109  101 ASN   A CG  
2015 C CG  B ASN   A 101 ? 0.2909 0.3085 0.2594 0.0081  -0.0360 0.0591  101 ASN   A CG  
2016 O OD1 A ASN   A 101 ? 0.2941 0.3132 0.2238 -0.0750 -0.0717 0.0801  101 ASN   A OD1 
2017 O OD1 B ASN   A 101 ? 0.2887 0.3080 0.2610 0.0166  -0.0306 0.0455  101 ASN   A OD1 
2018 N ND2 A ASN   A 101 ? 0.2958 0.2914 0.2004 -0.0871 -0.0825 0.1160  101 ASN   A ND2 
2019 N ND2 B ASN   A 101 ? 0.2888 0.3052 0.2652 0.0081  -0.0362 0.0536  101 ASN   A ND2 
2032 N N   A LYS   A 102 ? 0.3294 0.3908 0.2669 -0.0756 -0.0151 0.1504  102 LYS   A N   
2033 N N   B LYS   A 102 ? 0.3293 0.3513 0.2932 -0.0178 -0.0052 0.1083  102 LYS   A N   
2034 C CA  A LYS   A 102 ? 0.3437 0.4138 0.2869 -0.0752 -0.0178 0.1332  102 LYS   A CA  
2035 C CA  B LYS   A 102 ? 0.3424 0.3676 0.3081 -0.0250 0.0071  0.0982  102 LYS   A CA  
2036 C C   A LYS   A 102 ? 0.3563 0.4336 0.2824 -0.0647 -0.0182 0.1185  102 LYS   A C   
2037 C C   B LYS   A 102 ? 0.3497 0.3798 0.2919 -0.0254 0.0066  0.1043  102 LYS   A C   
2038 O O   A LYS   A 102 ? 0.3621 0.4465 0.2907 -0.0610 -0.0159 0.1095  102 LYS   A O   
2039 O O   B LYS   A 102 ? 0.3532 0.3781 0.2797 -0.0239 0.0117  0.1178  102 LYS   A O   
2040 C CB  A LYS   A 102 ? 0.3512 0.4168 0.3192 -0.0826 -0.0233 0.1232  102 LYS   A CB  
2041 C CB  B LYS   A 102 ? 0.3509 0.3727 0.3443 -0.0308 0.0137  0.0806  102 LYS   A CB  
2042 C CG  A LYS   A 102 ? 0.3590 0.4169 0.3469 -0.0878 -0.0329 0.1093  102 LYS   A CG  
2043 C CG  B LYS   A 102 ? 0.3590 0.3759 0.3796 -0.0350 0.0160  0.0642  102 LYS   A CG  
2044 C CD  A LYS   A 102 ? 0.3698 0.4193 0.3753 -0.0889 -0.0396 0.0915  102 LYS   A CD  
2045 C CD  B LYS   A 102 ? 0.3674 0.3806 0.4132 -0.0361 0.0152  0.0477  102 LYS   A CD  
2046 C CE  A LYS   A 102 ? 0.3791 0.4205 0.3950 -0.0870 -0.0466 0.0835  102 LYS   A CE  
2047 C CE  B LYS   A 102 ? 0.3733 0.3847 0.4378 -0.0364 0.0124  0.0353  102 LYS   A CE  
2048 N NZ  A LYS   A 102 ? 0.3841 0.4190 0.3993 -0.0898 -0.0458 0.0807  102 LYS   A NZ  
2049 N NZ  B LYS   A 102 ? 0.3765 0.3870 0.4503 -0.0365 0.0098  0.0289  102 LYS   A NZ  
2076 N N   A GLY   A 103 ? 0.3597 0.4400 0.2864 -0.0538 -0.0229 0.0990  103 GLY   A N   
2077 N N   B GLY   A 103 ? 0.3515 0.3945 0.2904 -0.0245 -0.0008 0.0914  103 GLY   A N   
2078 C CA  A GLY   A 103 ? 0.3625 0.4399 0.2735 -0.0428 -0.0207 0.0821  103 GLY   A CA  
2079 C CA  B GLY   A 103 ? 0.3524 0.4055 0.2805 -0.0250 -0.0034 0.0819  103 GLY   A CA  
2080 C C   A GLY   A 103 ? 0.3594 0.4386 0.2706 -0.0331 -0.0107 0.0629  103 GLY   A C   
2081 C C   B GLY   A 103 ? 0.3498 0.4152 0.2643 -0.0268 -0.0018 0.0706  103 GLY   A C   
2082 O O   A GLY   A 103 ? 0.3718 0.4506 0.2929 -0.0282 -0.0100 0.0473  103 GLY   A O   
2083 O O   B GLY   A 103 ? 0.3550 0.4186 0.2753 -0.0246 -0.0019 0.0685  103 GLY   A O   
2090 N N   . GLU   A 104 ? 0.3384 0.4180 0.2248 -0.0319 -0.0014 0.0655  104 GLU   A N   
2091 C CA  . GLU   A 104 ? 0.3044 0.3982 0.1867 -0.0421 0.0040  0.0488  104 GLU   A CA  
2092 C C   . GLU   A 104 ? 0.3024 0.4001 0.1916 -0.0456 0.0066  0.0142  104 GLU   A C   
2093 O O   . GLU   A 104 ? 0.2929 0.4009 0.2146 -0.0452 0.0031  0.0046  104 GLU   A O   
2094 C CB  . GLU   A 104 ? 0.2691 0.3786 0.1638 -0.0468 0.0168  0.0643  104 GLU   A CB  
2095 C CG  . GLU   A 104 ? 0.2523 0.3649 0.1762 -0.0446 -0.0012 0.0687  104 GLU   A CG  
2096 C CD  . GLU   A 104 ? 0.2328 0.3495 0.1804 -0.0444 -0.0006 0.0788  104 GLU   A CD  
2097 O OE1 . GLU   A 104 ? 0.2172 0.3336 0.1605 -0.0450 -0.0080 0.0763  104 GLU   A OE1 
2098 O OE2 . GLU   A 104 ? 0.2508 0.3486 0.2178 -0.0447 0.0041  0.0910  104 GLU   A OE2 
2106 N N   A ASP   A 105 ? 0.3075 0.4072 0.2019 -0.0479 0.0175  -0.0046 105 ASP   A N   
2107 N N   B ASP   A 105 ? 0.3143 0.3985 0.2289 -0.0414 0.0040  -0.0009 105 ASP   A N   
2108 C CA  A ASP   A 105 ? 0.3072 0.4119 0.2272 -0.0459 0.0295  -0.0314 105 ASP   A CA  
2109 C CA  B ASP   A 105 ? 0.3232 0.3964 0.2685 -0.0368 0.0024  -0.0185 105 ASP   A CA  
2110 C C   A ASP   A 105 ? 0.2748 0.3972 0.1827 -0.0541 0.0211  -0.0474 105 ASP   A C   
2111 C C   B ASP   A 105 ? 0.3149 0.3854 0.2636 -0.0390 -0.0006 -0.0231 105 ASP   A C   
2112 O O   A ASP   A 105 ? 0.2559 0.3846 0.1232 -0.0497 0.0258  -0.0668 105 ASP   A O   
2113 O O   B ASP   A 105 ? 0.3116 0.3859 0.2558 -0.0392 -0.0033 -0.0267 105 ASP   A O   
2114 C CB  A ASP   A 105 ? 0.3366 0.4328 0.2947 -0.0356 0.0452  -0.0421 105 ASP   A CB  
2115 C CB  B ASP   A 105 ? 0.3386 0.4034 0.3081 -0.0299 0.0021  -0.0318 105 ASP   A CB  
2116 C CG  A ASP   A 105 ? 0.3615 0.4490 0.3564 -0.0244 0.0508  -0.0554 105 ASP   A CG  
2117 C CG  B ASP   A 105 ? 0.3514 0.4086 0.3428 -0.0235 -0.0020 -0.0450 105 ASP   A CG  
2118 O OD1 A ASP   A 105 ? 0.3676 0.4562 0.3683 -0.0256 0.0490  -0.0682 105 ASP   A OD1 
2119 O OD1 B ASP   A 105 ? 0.3558 0.4103 0.3445 -0.0238 -0.0052 -0.0546 105 ASP   A OD1 
2120 O OD2 A ASP   A 105 ? 0.3755 0.4549 0.3893 -0.0204 0.0613  -0.0521 105 ASP   A OD2 
2121 O OD2 B ASP   A 105 ? 0.3579 0.4113 0.3657 -0.0220 -0.0051 -0.0460 105 ASP   A OD2 
2130 N N   A ILE   A 106 ? 0.2595 0.3899 0.2004 -0.0629 -0.0023 -0.0468 106 ILE   A N   
2131 N N   B ILE   A 106 ? 0.3091 0.3728 0.2670 -0.0404 -0.0045 -0.0241 106 ILE   A N   
2132 C CA  A ILE   A 106 ? 0.2377 0.3807 0.2147 -0.0754 -0.0286 -0.0607 106 ILE   A CA  
2133 C CA  B ILE   A 106 ? 0.3007 0.3582 0.2715 -0.0424 -0.0081 -0.0290 106 ILE   A CA  
2134 C C   A ILE   A 106 ? 0.2231 0.3571 0.2202 -0.0874 -0.0281 -0.0765 106 ILE   A C   
2135 C C   B ILE   A 106 ? 0.2928 0.3385 0.2722 -0.0461 -0.0030 -0.0371 106 ILE   A C   
2136 O O   A ILE   A 106 ? 0.1949 0.3453 0.2162 -0.0945 -0.0151 -0.0796 106 ILE   A O   
2137 O O   B ILE   A 106 ? 0.2874 0.3347 0.2669 -0.0446 -0.0020 -0.0407 106 ILE   A O   
2138 C CB  A ILE   A 106 ? 0.2412 0.3978 0.2526 -0.0632 -0.0498 -0.0355 106 ILE   A CB  
2139 C CB  B ILE   A 106 ? 0.3022 0.3642 0.2858 -0.0377 -0.0163 -0.0200 106 ILE   A CB  
2140 C CG1 A ILE   A 106 ? 0.2345 0.4034 0.2898 -0.0477 -0.0541 -0.0157 106 ILE   A CG1 
2141 C CG1 B ILE   A 106 ? 0.2991 0.3660 0.2997 -0.0329 -0.0199 -0.0118 106 ILE   A CG1 
2142 C CG2 A ILE   A 106 ? 0.2449 0.4032 0.2608 -0.0647 -0.0616 -0.0329 106 ILE   A CG2 
2143 C CG2 B ILE   A 106 ? 0.3041 0.3666 0.2892 -0.0378 -0.0201 -0.0193 106 ILE   A CG2 
2144 C CD1 A ILE   A 106 ? 0.2366 0.4040 0.3135 -0.0331 -0.0463 -0.0070 106 ILE   A CD1 
2145 C CD1 B ILE   A 106 ? 0.2983 0.3654 0.3080 -0.0282 -0.0188 -0.0082 106 ILE   A CD1 
2168 N N   A GLN   A 107 ? 0.2470 0.3421 0.2539 -0.0825 -0.0076 -0.0843 107 GLN   A N   
2169 N N   B GLN   A 107 ? 0.2917 0.3212 0.2872 -0.0498 0.0073  -0.0414 107 GLN   A N   
2170 C CA  A GLN   A 107 ? 0.2765 0.3291 0.3306 -0.0651 0.0130  -0.0812 107 GLN   A CA  
2171 C CA  B GLN   A 107 ? 0.2910 0.3043 0.3170 -0.0485 0.0168  -0.0459 107 GLN   A CA  
2172 C C   A GLN   A 107 ? 0.2534 0.2779 0.3092 -0.0560 0.0324  -0.0629 107 GLN   A C   
2173 C C   B GLN   A 107 ? 0.2605 0.2681 0.2904 -0.0488 0.0312  -0.0465 107 GLN   A C   
2174 O O   A GLN   A 107 ? 0.2564 0.2720 0.3566 -0.0491 0.0397  -0.0683 107 GLN   A O   
2175 O O   B GLN   A 107 ? 0.2631 0.2665 0.3163 -0.0458 0.0328  -0.0482 107 GLN   A O   
2176 C CB  A GLN   A 107 ? 0.3190 0.3611 0.4271 -0.0694 0.0029  -0.0833 107 GLN   A CB  
2177 C CB  B GLN   A 107 ? 0.3152 0.3202 0.3734 -0.0524 0.0067  -0.0408 107 GLN   A CB  
2178 C CG  A GLN   A 107 ? 0.3654 0.3970 0.5263 -0.0680 -0.0049 -0.0753 107 GLN   A CG  
2179 C CG  B GLN   A 107 ? 0.3372 0.3349 0.4323 -0.0552 -0.0018 -0.0312 107 GLN   A CG  
2180 C CD  A GLN   A 107 ? 0.3990 0.4207 0.6088 -0.0666 -0.0071 -0.0650 107 GLN   A CD  
2181 C CD  B GLN   A 107 ? 0.3572 0.3500 0.4820 -0.0540 -0.0071 -0.0205 107 GLN   A CD  
2182 O OE1 A GLN   A 107 ? 0.4103 0.4285 0.6415 -0.0667 -0.0061 -0.0621 107 GLN   A OE1 
2183 O OE1 B GLN   A 107 ? 0.3652 0.3560 0.4983 -0.0537 -0.0061 -0.0140 107 GLN   A OE1 
2184 N NE2 A GLN   A 107 ? 0.4100 0.4278 0.6363 -0.0675 -0.0102 -0.0644 107 GLN   A NE2 
2185 N NE2 B GLN   A 107 ? 0.3629 0.3554 0.4971 -0.0551 -0.0139 -0.0199 107 GLN   A NE2 
2202 N N   . LEU   A 108 ? 0.2251 0.2329 0.2448 -0.0514 0.0435  -0.0528 108 LEU   A N   
2203 C CA  . LEU   A 108 ? 0.1943 0.1843 0.2129 -0.0209 0.0348  -0.0187 108 LEU   A CA  
2204 C C   . LEU   A 108 ? 0.1630 0.1487 0.2019 -0.0066 0.0215  0.0031  108 LEU   A C   
2205 O O   . LEU   A 108 ? 0.1606 0.1506 0.2317 0.0017  0.0257  0.0018  108 LEU   A O   
2206 C CB  . LEU   A 108 ? 0.2014 0.1908 0.2004 -0.0245 0.0349  -0.0123 108 LEU   A CB  
2207 C CG  . LEU   A 108 ? 0.2137 0.2136 0.2378 -0.0221 0.0455  -0.0187 108 LEU   A CG  
2208 C CD1 . LEU   A 108 ? 0.2322 0.2196 0.2434 -0.0317 0.0577  -0.0135 108 LEU   A CD1 
2209 C CD2 . LEU   A 108 ? 0.2178 0.2417 0.2860 -0.0097 0.0433  -0.0120 108 LEU   A CD2 
2222 N N   . LEU   A 109 ? 0.1456 0.1469 0.1970 0.0023  0.0152  0.0115  109 LEU   A N   
2223 C CA  . LEU   A 109 ? 0.1476 0.1418 0.1722 0.0039  0.0070  0.0179  109 LEU   A CA  
2224 C C   . LEU   A 109 ? 0.1358 0.1344 0.1657 -0.0087 0.0124  0.0059  109 LEU   A C   
2225 O O   . LEU   A 109 ? 0.1491 0.1272 0.1826 0.0010  0.0024  0.0085  109 LEU   A O   
2226 C CB  . LEU   A 109 ? 0.1588 0.1485 0.1980 0.0122  -0.0004 0.0311  109 LEU   A CB  
2227 C CG  . LEU   A 109 ? 0.1525 0.1587 0.2098 0.0057  0.0071  0.0315  109 LEU   A CG  
2228 C CD1 . LEU   A 109 ? 0.1489 0.1459 0.2147 0.0065  0.0116  0.0115  109 LEU   A CD1 
2229 C CD2 . LEU   A 109 ? 0.1461 0.1738 0.2386 0.0048  0.0005  0.0338  109 LEU   A CD2 
2241 N N   . LYS   A 110 ? 0.1417 0.1302 0.1716 -0.0036 -0.0027 0.0064  110 LYS   A N   
2242 C CA  . LYS   A 110 ? 0.1390 0.1301 0.1791 -0.0038 -0.0049 0.0147  110 LYS   A CA  
2243 C C   . LYS   A 110 ? 0.1383 0.1226 0.1667 -0.0061 -0.0034 0.0039  110 LYS   A C   
2244 O O   . LYS   A 110 ? 0.1299 0.1267 0.1820 -0.0034 0.0000  -0.0006 110 LYS   A O   
2245 C CB  . LYS   A 110 ? 0.1451 0.1373 0.2043 -0.0042 -0.0138 -0.0032 110 LYS   A CB  
2246 C CG  . LYS   A 110 ? 0.1425 0.1348 0.2137 -0.0038 -0.0176 -0.0057 110 LYS   A CG  
2247 C CD  . LYS   A 110 ? 0.1516 0.1445 0.2330 -0.0135 -0.0128 -0.0068 110 LYS   A CD  
2248 C CE  . LYS   A 110 ? 0.1619 0.1498 0.2489 -0.0076 0.0084  -0.0002 110 LYS   A CE  
2249 N NZ  . LYS   A 110 ? 0.1589 0.1451 0.2634 -0.0163 0.0137  0.0022  110 LYS   A NZ  
2263 N N   . SER   A 111 ? 0.1391 0.1263 0.1688 -0.0006 -0.0078 -0.0005 111 SER   A N   
2264 C CA  . SER   A 111 ? 0.1309 0.1319 0.1730 0.0057  0.0065  0.0045  111 SER   A CA  
2265 C C   . SER   A 111 ? 0.1213 0.1279 0.1744 -0.0019 0.0053  0.0051  111 SER   A C   
2266 O O   . SER   A 111 ? 0.1360 0.1222 0.1965 0.0019  0.0034  0.0039  111 SER   A O   
2267 C CB  . SER   A 111 ? 0.1481 0.1495 0.1992 0.0030  0.0132  -0.0087 111 SER   A CB  
2268 O OG  . SER   A 111 ? 0.1990 0.1734 0.2075 0.0106  0.0199  -0.0137 111 SER   A OG  
2274 N N   . ALA   A 112 ? 0.1272 0.1236 0.1803 -0.0017 0.0134  0.0093  112 ALA   A N   
2275 C CA  . ALA   A 112 ? 0.1341 0.1183 0.1651 -0.0015 0.0163  0.0052  112 ALA   A CA  
2276 C C   . ALA   A 112 ? 0.1277 0.1152 0.1769 0.0005  0.0122  0.0000  112 ALA   A C   
2277 O O   . ALA   A 112 ? 0.1326 0.1172 0.1836 -0.0131 0.0115  0.0107  112 ALA   A O   
2278 C CB  . ALA   A 112 ? 0.1462 0.1230 0.1714 -0.0055 0.0053  0.0122  112 ALA   A CB  
2284 N N   . TYR   A 113 ? 0.1198 0.1222 0.1757 -0.0020 0.0086  0.0145  113 TYR   A N   
2285 C CA  . TYR   A 113 ? 0.1184 0.1216 0.1689 -0.0037 0.0080  0.0121  113 TYR   A CA  
2286 C C   . TYR   A 113 ? 0.1205 0.1240 0.1621 -0.0119 0.0052  0.0096  113 TYR   A C   
2287 O O   . TYR   A 113 ? 0.1244 0.1265 0.1790 -0.0066 0.0077  0.0036  113 TYR   A O   
2288 C CB  . TYR   A 113 ? 0.1239 0.1361 0.1744 -0.0034 -0.0006 0.0213  113 TYR   A CB  
2289 C CG  . TYR   A 113 ? 0.1207 0.1300 0.1654 -0.0097 0.0056  0.0257  113 TYR   A CG  
2290 C CD1 . TYR   A 113 ? 0.1222 0.1442 0.1663 -0.0015 0.0026  0.0300  113 TYR   A CD1 
2291 C CD2 . TYR   A 113 ? 0.1301 0.1391 0.1624 -0.0124 0.0029  0.0240  113 TYR   A CD2 
2292 C CE1 . TYR   A 113 ? 0.1261 0.1557 0.1690 -0.0026 0.0023  0.0293  113 TYR   A CE1 
2293 C CE2 . TYR   A 113 ? 0.1237 0.1488 0.1748 -0.0112 -0.0029 0.0297  113 TYR   A CE2 
2294 C CZ  . TYR   A 113 ? 0.1224 0.1499 0.1684 0.0037  0.0113  0.0283  113 TYR   A CZ  
2295 O OH  . TYR   A 113 ? 0.1277 0.1610 0.1921 0.0082  0.0130  0.0312  113 TYR   A OH  
2305 N N   . GLU   A 114 ? 0.1212 0.1216 0.1672 -0.0044 0.0097  0.0129  114 GLU   A N   
2306 C CA  . GLU   A 114 ? 0.1269 0.1153 0.1795 0.0018  0.0027  0.0187  114 GLU   A CA  
2307 C C   . GLU   A 114 ? 0.1218 0.1143 0.1728 0.0067  0.0097  0.0088  114 GLU   A C   
2308 O O   . GLU   A 114 ? 0.1300 0.1169 0.1859 0.0015  0.0023  0.0119  114 GLU   A O   
2309 C CB  . GLU   A 114 ? 0.1225 0.1172 0.1798 -0.0067 0.0039  0.0118  114 GLU   A CB  
2310 C CG  . GLU   A 114 ? 0.1297 0.1206 0.1914 0.0047  0.0112  0.0039  114 GLU   A CG  
2311 C CD  . GLU   A 114 ? 0.1378 0.1257 0.1995 -0.0031 -0.0041 0.0007  114 GLU   A CD  
2312 O OE1 . GLU   A 114 ? 0.1432 0.1252 0.2032 -0.0105 0.0111  -0.0103 114 GLU   A OE1 
2313 O OE2 . GLU   A 114 ? 0.1574 0.1321 0.2143 -0.0057 0.0024  -0.0148 114 GLU   A OE2 
2320 N N   . ASN   A 115 ? 0.1228 0.1221 0.1542 -0.0030 0.0013  0.0051  115 ASN   A N   
2321 C CA  . ASN   A 115 ? 0.1228 0.1284 0.1611 -0.0070 0.0109  0.0072  115 ASN   A CA  
2322 C C   . ASN   A 115 ? 0.1231 0.1193 0.1627 -0.0085 0.0035  0.0054  115 ASN   A C   
2323 O O   . ASN   A 115 ? 0.1277 0.1389 0.1752 -0.0103 0.0066  0.0111  115 ASN   A O   
2324 C CB  . ASN   A 115 ? 0.1276 0.1347 0.1544 -0.0111 0.0105  0.0045  115 ASN   A CB  
2325 C CG  . ASN   A 115 ? 0.1296 0.1557 0.1644 -0.0144 0.0165  0.0023  115 ASN   A CG  
2326 O OD1 . ASN   A 115 ? 0.1333 0.2506 0.2011 -0.0157 0.0253  0.0230  115 ASN   A OD1 
2327 N ND2 . ASN   A 115 ? 0.1345 0.1402 0.1717 -0.0156 0.0185  0.0154  115 ASN   A ND2 
2334 N N   . PHE   A 116 ? 0.1154 0.1284 0.1746 -0.0014 0.0059  0.0157  116 PHE   A N   
2335 C CA  . PHE   A 116 ? 0.1241 0.1343 0.1592 -0.0013 0.0096  0.0201  116 PHE   A CA  
2336 C C   . PHE   A 116 ? 0.1234 0.1384 0.1574 -0.0125 0.0178  0.0224  116 PHE   A C   
2337 O O   . PHE   A 116 ? 0.1341 0.1450 0.1696 -0.0043 0.0150  0.0263  116 PHE   A O   
2338 C CB  . PHE   A 116 ? 0.1210 0.1296 0.1811 -0.0083 0.0179  0.0239  116 PHE   A CB  
2339 C CG  . PHE   A 116 ? 0.1254 0.1251 0.1737 -0.0085 0.0100  0.0201  116 PHE   A CG  
2340 C CD1 . PHE   A 116 ? 0.1247 0.1217 0.1780 -0.0084 0.0108  0.0152  116 PHE   A CD1 
2341 C CD2 . PHE   A 116 ? 0.1271 0.1310 0.1836 -0.0113 0.0117  0.0210  116 PHE   A CD2 
2342 C CE1 . PHE   A 116 ? 0.1266 0.1211 0.1793 -0.0146 0.0085  0.0114  116 PHE   A CE1 
2343 C CE2 . PHE   A 116 ? 0.1332 0.1250 0.1909 -0.0055 0.0113  0.0086  116 PHE   A CE2 
2344 C CZ  . PHE   A 116 ? 0.1363 0.1133 0.1812 -0.0047 -0.0015 0.0088  116 PHE   A CZ  
2354 N N   . ASN   A 117 ? 0.1224 0.1322 0.1787 -0.0049 0.0116  0.0229  117 ASN   A N   
2355 C CA  . ASN   A 117 ? 0.1289 0.1250 0.1904 -0.0051 0.0098  0.0300  117 ASN   A CA  
2356 C C   . ASN   A 117 ? 0.1310 0.1340 0.2009 -0.0004 0.0114  0.0256  117 ASN   A C   
2357 O O   . ASN   A 117 ? 0.1410 0.1437 0.2390 -0.0064 -0.0144 0.0453  117 ASN   A O   
2358 C CB  . ASN   A 117 ? 0.1283 0.1296 0.2054 -0.0026 0.0104  0.0338  117 ASN   A CB  
2359 C CG  . ASN   A 117 ? 0.1253 0.1333 0.2044 -0.0061 0.0086  0.0322  117 ASN   A CG  
2360 O OD1 . ASN   A 117 ? 0.1253 0.1568 0.2024 -0.0153 0.0076  0.0236  117 ASN   A OD1 
2361 N ND2 . ASN   A 117 ? 0.1171 0.1377 0.1989 -0.0028 0.0058  0.0277  117 ASN   A ND2 
2368 N N   . GLN   A 118 ? 0.1253 0.1335 0.1961 -0.0085 -0.0111 0.0300  118 GLN   A N   
2369 C CA  . GLN   A 118 ? 0.1355 0.1522 0.1959 -0.0072 -0.0116 0.0287  118 GLN   A CA  
2370 C C   . GLN   A 118 ? 0.1359 0.1647 0.1850 -0.0105 -0.0142 0.0281  118 GLN   A C   
2371 O O   . GLN   A 118 ? 0.1368 0.1938 0.2050 -0.0057 -0.0128 0.0133  118 GLN   A O   
2372 C CB  . GLN   A 118 ? 0.1318 0.1512 0.2071 -0.0018 0.0025  0.0350  118 GLN   A CB  
2373 C CG  . GLN   A 118 ? 0.1322 0.1524 0.2159 -0.0039 0.0093  0.0292  118 GLN   A CG  
2374 C CD  . GLN   A 118 ? 0.1284 0.1545 0.2340 0.0003  0.0054  0.0154  118 GLN   A CD  
2375 O OE1 . GLN   A 118 ? 0.1313 0.1656 0.2480 0.0044  -0.0038 0.0118  118 GLN   A OE1 
2376 N NE2 . GLN   A 118 ? 0.1414 0.1476 0.2372 0.0022  -0.0009 0.0220  118 GLN   A NE2 
2385 N N   . HIS   A 119 ? 0.1378 0.1550 0.1718 -0.0052 -0.0061 0.0337  119 HIS   A N   
2386 C CA  . HIS   A 119 ? 0.1450 0.1729 0.1709 -0.0081 -0.0032 0.0361  119 HIS   A CA  
2387 C C   . HIS   A 119 ? 0.1552 0.1773 0.1771 -0.0141 -0.0058 0.0406  119 HIS   A C   
2388 O O   . HIS   A 119 ? 0.1590 0.1832 0.1929 -0.0310 -0.0145 0.0381  119 HIS   A O   
2389 C CB  . HIS   A 119 ? 0.1523 0.1652 0.1897 -0.0075 0.0138  0.0393  119 HIS   A CB  
2390 C CG  . HIS   A 119 ? 0.1547 0.1690 0.2376 0.0022  0.0092  0.0414  119 HIS   A CG  
2391 N ND1 . HIS   A 119 ? 0.1674 0.1907 0.2923 -0.0119 0.0093  0.0287  119 HIS   A ND1 
2392 C CD2 . HIS   A 119 ? 0.1689 0.1719 0.2529 0.0118  0.0302  0.0523  119 HIS   A CD2 
2393 C CE1 . HIS   A 119 ? 0.1658 0.1843 0.3021 -0.0154 0.0228  0.0546  119 HIS   A CE1 
2394 N NE2 . HIS   A 119 ? 0.1768 0.1757 0.2873 -0.0001 0.0458  0.0640  119 HIS   A NE2 
2402 N N   . GLU   A 120 ? 0.1603 0.2017 0.1824 -0.0113 -0.0068 0.0555  120 GLU   A N   
2403 C CA  . GLU   A 120 ? 0.1862 0.2320 0.2133 -0.0064 -0.0061 0.0937  120 GLU   A CA  
2404 C C   . GLU   A 120 ? 0.1646 0.2180 0.1899 -0.0183 -0.0003 0.0839  120 GLU   A C   
2405 O O   . GLU   A 120 ? 0.1627 0.2126 0.2024 -0.0155 -0.0027 0.0796  120 GLU   A O   
2406 C CB  . GLU   A 120 ? 0.2505 0.2932 0.2767 0.0077  0.0011  0.1463  120 GLU   A CB  
2407 C CG  . GLU   A 120 ? 0.3452 0.3619 0.3940 0.0206  -0.0006 0.1491  120 GLU   A CG  
2408 C CD  . GLU   A 120 ? 0.4184 0.4188 0.5035 0.0319  0.0062  0.1396  120 GLU   A CD  
2409 O OE1 . GLU   A 120 ? 0.4409 0.4419 0.5263 0.0338  0.0078  0.1323  120 GLU   A OE1 
2410 O OE2 . GLU   A 120 ? 0.4627 0.4627 0.5566 0.0349  0.0091  0.1367  120 GLU   A OE2 
2417 N N   . VAL   A 121 ? 0.1663 0.2163 0.1727 -0.0209 0.0040  0.0620  121 VAL   A N   
2418 C CA  . VAL   A 121 ? 0.1746 0.2177 0.1577 -0.0253 0.0183  0.0575  121 VAL   A CA  
2419 C C   . VAL   A 121 ? 0.1610 0.2001 0.1456 -0.0266 0.0140  0.0394  121 VAL   A C   
2420 O O   . VAL   A 121 ? 0.1630 0.2038 0.1798 -0.0370 -0.0017 0.0351  121 VAL   A O   
2421 C CB  . VAL   A 121 ? 0.2168 0.2514 0.2109 -0.0116 0.0349  0.0611  121 VAL   A CB  
2422 C CG1 . VAL   A 121 ? 0.2228 0.2659 0.2169 -0.0033 0.0475  0.0627  121 VAL   A CG1 
2423 C CG2 . VAL   A 121 ? 0.2393 0.2724 0.2538 -0.0176 0.0327  0.0438  121 VAL   A CG2 
2433 N N   . LEU   A 122 ? 0.1487 0.1817 0.1523 -0.0252 0.0082  0.0404  122 LEU   A N   
2434 C CA  . LEU   A 122 ? 0.1567 0.1671 0.1587 -0.0261 0.0202  0.0361  122 LEU   A CA  
2435 C C   . LEU   A 122 ? 0.1462 0.1671 0.1666 -0.0276 0.0107  0.0330  122 LEU   A C   
2436 O O   . LEU   A 122 ? 0.1437 0.1805 0.2063 -0.0306 0.0046  0.0336  122 LEU   A O   
2437 C CB  . LEU   A 122 ? 0.1741 0.1653 0.1990 -0.0178 0.0128  0.0500  122 LEU   A CB  
2438 C CG  . LEU   A 122 ? 0.1740 0.1697 0.1987 -0.0158 0.0231  0.0303  122 LEU   A CG  
2439 C CD1 . LEU   A 122 ? 0.2004 0.1679 0.2102 -0.0259 0.0277  0.0303  122 LEU   A CD1 
2440 C CD2 . LEU   A 122 ? 0.1677 0.1645 0.1847 -0.0133 0.0357  0.0188  122 LEU   A CD2 
2452 N N   . LEU   A 123 ? 0.1441 0.1681 0.1542 -0.0287 0.0001  0.0316  123 LEU   A N   
2453 C CA  . LEU   A 123 ? 0.1377 0.1692 0.1593 -0.0321 0.0069  0.0276  123 LEU   A CA  
2454 C C   . LEU   A 123 ? 0.1335 0.1585 0.1460 -0.0176 0.0043  0.0268  123 LEU   A C   
2455 O O   . LEU   A 123 ? 0.1314 0.1702 0.1665 -0.0300 0.0031  0.0299  123 LEU   A O   
2456 C CB  . LEU   A 123 ? 0.1500 0.1798 0.1398 -0.0314 0.0173  0.0225  123 LEU   A CB  
2457 C CG  . LEU   A 123 ? 0.1548 0.1869 0.1579 -0.0248 0.0154  0.0115  123 LEU   A CG  
2458 C CD1 . LEU   A 123 ? 0.1679 0.1935 0.1673 -0.0095 0.0147  0.0040  123 LEU   A CD1 
2459 C CD2 . LEU   A 123 ? 0.1708 0.1977 0.1745 -0.0238 0.0146  0.0125  123 LEU   A CD2 
2471 N N   . ALA   A 124 ? 0.1340 0.1429 0.1398 -0.0197 0.0064  0.0180  124 ALA   A N   
2472 C CA  . ALA   A 124 ? 0.1275 0.1426 0.1535 -0.0197 -0.0021 0.0197  124 ALA   A CA  
2473 C C   . ALA   A 124 ? 0.1260 0.1408 0.1537 -0.0170 0.0077  0.0192  124 ALA   A C   
2474 O O   . ALA   A 124 ? 0.1314 0.1461 0.1754 -0.0182 0.0176  0.0287  124 ALA   A O   
2475 C CB  . ALA   A 124 ? 0.1341 0.1402 0.1743 -0.0170 0.0023  0.0257  124 ALA   A CB  
2481 N N   A PRO   A 125 ? 0.1218 0.1290 0.1643 -0.0109 0.0061  0.0292  125 PRO   A N   
2482 N N   B PRO   A 125 ? 0.1295 0.1406 0.1406 -0.0127 0.0081  0.0225  125 PRO   A N   
2483 C CA  A PRO   A 125 ? 0.1265 0.1283 0.1699 -0.0078 0.0096  0.0215  125 PRO   A CA  
2484 C CA  B PRO   A 125 ? 0.1367 0.1425 0.1340 -0.0098 0.0050  0.0131  125 PRO   A CA  
2485 C C   A PRO   A 125 ? 0.1185 0.1331 0.1743 -0.0077 0.0137  0.0220  125 PRO   A C   
2486 C C   B PRO   A 125 ? 0.1381 0.1471 0.1313 -0.0029 0.0075  0.0137  125 PRO   A C   
2487 O O   A PRO   A 125 ? 0.1268 0.1274 0.1939 -0.0006 0.0047  0.0059  125 PRO   A O   
2488 O O   B PRO   A 125 ? 0.1408 0.1502 0.1387 0.0073  0.0041  0.0114  125 PRO   A O   
2489 C CB  A PRO   A 125 ? 0.1415 0.1230 0.1689 -0.0051 0.0167  0.0168  125 PRO   A CB  
2490 C CB  B PRO   A 125 ? 0.1429 0.1405 0.1389 -0.0104 0.0093  0.0156  125 PRO   A CB  
2491 C CG  A PRO   A 125 ? 0.1324 0.1119 0.1699 -0.0118 0.0227  0.0205  125 PRO   A CG  
2492 C CG  B PRO   A 125 ? 0.1436 0.1383 0.1415 -0.0172 0.0095  0.0220  125 PRO   A CG  
2493 C CD  A PRO   A 125 ? 0.1234 0.1240 0.1668 -0.0165 0.0154  0.0217  125 PRO   A CD  
2494 C CD  B PRO   A 125 ? 0.1321 0.1417 0.1399 -0.0166 0.0132  0.0198  125 PRO   A CD  
2509 N N   A LEU   A 126 ? 0.1121 0.1375 0.1762 -0.0049 0.0145  0.0163  126 LEU   A N   
2510 N N   B LEU   A 126 ? 0.1407 0.1530 0.1385 -0.0031 0.0071  0.0050  126 LEU   A N   
2511 C CA  A LEU   A 126 ? 0.1197 0.1369 0.1797 -0.0031 0.0132  0.0286  126 LEU   A CA  
2512 C CA  B LEU   A 126 ? 0.1377 0.1445 0.1395 -0.0027 0.0057  0.0054  126 LEU   A CA  
2513 C C   A LEU   A 126 ? 0.1291 0.1425 0.1814 -0.0060 0.0011  0.0238  126 LEU   A C   
2514 C C   B LEU   A 126 ? 0.1408 0.1391 0.1558 0.0016  0.0017  0.0060  126 LEU   A C   
2515 O O   A LEU   A 126 ? 0.1441 0.1360 0.1996 -0.0125 0.0128  0.0131  126 LEU   A O   
2516 O O   B LEU   A 126 ? 0.1518 0.1244 0.1868 -0.0010 0.0254  0.0050  126 LEU   A O   
2517 C CB  A LEU   A 126 ? 0.1375 0.1428 0.1873 -0.0079 -0.0010 0.0176  126 LEU   A CB  
2518 C CB  B LEU   A 126 ? 0.1391 0.1521 0.1483 -0.0140 0.0049  0.0051  126 LEU   A CB  
2519 C CG  A LEU   A 126 ? 0.1336 0.1529 0.2106 -0.0060 0.0051  0.0214  126 LEU   A CG  
2520 C CG  B LEU   A 126 ? 0.1313 0.1540 0.1552 -0.0056 0.0130  0.0108  126 LEU   A CG  
2521 C CD1 A LEU   A 126 ? 0.1462 0.1753 0.2283 -0.0125 -0.0009 0.0266  126 LEU   A CD1 
2522 C CD1 B LEU   A 126 ? 0.1301 0.1576 0.1644 -0.0088 0.0005  0.0220  126 LEU   A CD1 
2523 C CD2 A LEU   A 126 ? 0.1475 0.1380 0.2117 -0.0191 0.0116  0.0137  126 LEU   A CD2 
2524 C CD2 B LEU   A 126 ? 0.1342 0.1551 0.1584 -0.0054 0.0169  0.0085  126 LEU   A CD2 
2547 N N   A LEU   A 127 ? 0.1218 0.1581 0.1720 -0.0028 0.0045  0.0241  127 LEU   A N   
2548 N N   B LEU   A 127 ? 0.1365 0.1544 0.1573 0.0067  -0.0069 0.0108  127 LEU   A N   
2549 C CA  A LEU   A 127 ? 0.1179 0.1629 0.1569 -0.0053 -0.0013 0.0184  127 LEU   A CA  
2550 C CA  B LEU   A 127 ? 0.1315 0.1642 0.1500 0.0057  -0.0109 0.0127  127 LEU   A CA  
2551 C C   A LEU   A 127 ? 0.1216 0.1498 0.1537 0.0028  -0.0047 0.0127  127 LEU   A C   
2552 C C   B LEU   A 127 ? 0.1324 0.1538 0.1489 0.0008  -0.0107 0.0083  127 LEU   A C   
2553 O O   A LEU   A 127 ? 0.1298 0.1434 0.1581 -0.0012 -0.0060 0.0252  127 LEU   A O   
2554 O O   B LEU   A 127 ? 0.1418 0.1520 0.1529 -0.0097 -0.0076 0.0123  127 LEU   A O   
2555 C CB  A LEU   A 127 ? 0.1230 0.1796 0.1641 0.0066  0.0057  0.0209  127 LEU   A CB  
2556 C CB  B LEU   A 127 ? 0.1299 0.1839 0.1528 0.0152  -0.0069 0.0243  127 LEU   A CB  
2557 C CG  A LEU   A 127 ? 0.1391 0.1957 0.1793 0.0112  0.0035  0.0290  127 LEU   A CG  
2558 C CG  B LEU   A 127 ? 0.1268 0.2045 0.1592 0.0228  -0.0086 0.0363  127 LEU   A CG  
2559 C CD1 A LEU   A 127 ? 0.1502 0.1906 0.2048 0.0156  0.0025  0.0314  127 LEU   A CD1 
2560 C CD1 B LEU   A 127 ? 0.1291 0.2050 0.1722 0.0265  -0.0045 0.0477  127 LEU   A CD1 
2561 C CD2 A LEU   A 127 ? 0.1444 0.2006 0.1893 0.0246  0.0142  0.0263  127 LEU   A CD2 
2562 C CD2 B LEU   A 127 ? 0.1284 0.2169 0.1501 0.0278  -0.0090 0.0384  127 LEU   A CD2 
2585 N N   . SER   A 128 ? 0.1306 0.1463 0.1581 -0.0027 -0.0061 0.0167  128 SER   A N   
2586 C CA  . SER   A 128 ? 0.1418 0.1451 0.1479 0.0027  -0.0046 0.0204  128 SER   A CA  
2587 C C   . SER   A 128 ? 0.1455 0.1450 0.1548 0.0039  -0.0142 0.0227  128 SER   A C   
2588 O O   . SER   A 128 ? 0.1687 0.1572 0.1831 0.0057  -0.0226 0.0127  128 SER   A O   
2589 C CB  . SER   A 128 ? 0.1428 0.1477 0.1397 -0.0061 -0.0069 0.0201  128 SER   A CB  
2590 O OG  . SER   A 128 ? 0.1426 0.1565 0.1536 -0.0063 -0.0033 0.0186  128 SER   A OG  
2597 N N   A ALA   A 129 ? 0.1410 0.1482 0.1894 -0.0004 -0.0123 0.0288  129 ALA   A N   
2598 N N   B ALA   A 129 ? 0.1448 0.1495 0.1725 0.0047  -0.0150 0.0266  129 ALA   A N   
2599 C CA  A ALA   A 129 ? 0.1335 0.1455 0.2111 -0.0003 -0.0009 0.0310  129 ALA   A CA  
2600 C CA  B ALA   A 129 ? 0.1421 0.1508 0.1856 0.0080  -0.0132 0.0288  129 ALA   A CA  
2601 C C   A ALA   A 129 ? 0.1443 0.1484 0.1889 0.0016  0.0029  0.0147  129 ALA   A C   
2602 C C   B ALA   A 129 ? 0.1415 0.1528 0.1739 0.0058  -0.0206 0.0204  129 ALA   A C   
2603 O O   A ALA   A 129 ? 0.1442 0.1515 0.1833 0.0008  -0.0000 0.0191  129 ALA   A O   
2604 O O   B ALA   A 129 ? 0.1436 0.1520 0.1749 0.0035  -0.0187 0.0207  129 ALA   A O   
2605 C CB  A ALA   A 129 ? 0.1381 0.1524 0.2464 0.0022  0.0037  0.0442  129 ALA   A CB  
2606 C CB  B ALA   A 129 ? 0.1483 0.1539 0.2095 0.0159  -0.0075 0.0304  129 ALA   A CB  
2617 N N   A GLY   A 130 ? 0.1544 0.1396 0.1926 -0.0019 0.0074  0.0162  130 GLY   A N   
2618 N N   B GLY   A 130 ? 0.1428 0.1551 0.1688 0.0041  -0.0185 0.0197  130 GLY   A N   
2619 C CA  A GLY   A 130 ? 0.1688 0.1372 0.1855 0.0000  0.0142  0.0176  130 GLY   A CA  
2620 C CA  B GLY   A 130 ? 0.1487 0.1577 0.1709 0.0019  -0.0123 0.0142  130 GLY   A CA  
2621 C C   A GLY   A 130 ? 0.1617 0.1333 0.1615 0.0074  0.0092  0.0107  130 GLY   A C   
2622 C C   B GLY   A 130 ? 0.1475 0.1565 0.1664 0.0033  -0.0246 0.0161  130 GLY   A C   
2623 O O   A GLY   A 130 ? 0.1631 0.1340 0.1767 -0.0010 0.0043  0.0032  130 GLY   A O   
2624 O O   B GLY   A 130 ? 0.1528 0.1589 0.1841 0.0071  -0.0292 0.0224  130 GLY   A O   
2631 N N   A ILE   A 131 ? 0.1658 0.1319 0.1514 0.0053  0.0115  0.0161  131 ILE   A N   
2632 N N   B ILE   A 131 ? 0.1441 0.1541 0.1661 -0.0003 -0.0209 0.0217  131 ILE   A N   
2633 C CA  A ILE   A 131 ? 0.1746 0.1330 0.1369 -0.0030 -0.0018 0.0049  131 ILE   A CA  
2634 C CA  B ILE   A 131 ? 0.1497 0.1552 0.1647 0.0007  -0.0223 0.0184  131 ILE   A CA  
2635 C C   A ILE   A 131 ? 0.1678 0.1396 0.1192 -0.0059 -0.0016 0.0164  131 ILE   A C   
2636 C C   B ILE   A 131 ? 0.1580 0.1603 0.1653 0.0054  -0.0118 0.0260  131 ILE   A C   
2637 O O   A ILE   A 131 ? 0.1770 0.1428 0.1434 -0.0009 -0.0085 0.0179  131 ILE   A O   
2638 O O   B ILE   A 131 ? 0.1694 0.1657 0.1764 0.0095  -0.0054 0.0341  131 ILE   A O   
2639 C CB  A ILE   A 131 ? 0.1893 0.1512 0.1664 -0.0118 0.0034  -0.0120 131 ILE   A CB  
2640 C CB  B ILE   A 131 ? 0.1518 0.1601 0.1662 0.0036  -0.0298 0.0067  131 ILE   A CB  
2641 C CG1 A ILE   A 131 ? 0.1944 0.1882 0.1841 -0.0153 -0.0055 -0.0256 131 ILE   A CG1 
2642 C CG1 B ILE   A 131 ? 0.1535 0.1755 0.1722 0.0093  -0.0323 -0.0104 131 ILE   A CG1 
2643 C CG2 A ILE   A 131 ? 0.2054 0.1414 0.1854 -0.0104 0.0097  -0.0160 131 ILE   A CG2 
2644 C CG2 B ILE   A 131 ? 0.1491 0.1546 0.1694 0.0012  -0.0225 0.0061  131 ILE   A CG2 
2645 C CD1 A ILE   A 131 ? 0.1946 0.2046 0.2133 -0.0111 -0.0133 -0.0366 131 ILE   A CD1 
2646 C CD1 B ILE   A 131 ? 0.1615 0.1790 0.1804 0.0102  -0.0285 -0.0273 131 ILE   A CD1 
2669 N N   A PHE   A 132 ? 0.1596 0.1429 0.1357 -0.0014 -0.0011 0.0209  132 PHE   A N   
2670 N N   B PHE   A 132 ? 0.1550 0.1580 0.1582 0.0135  -0.0112 0.0170  132 PHE   A N   
2671 C CA  A PHE   A 132 ? 0.1592 0.1501 0.1237 -0.0042 0.0087  0.0127  132 PHE   A CA  
2672 C CA  B PHE   A 132 ? 0.1570 0.1602 0.1687 0.0141  -0.0125 0.0079  132 PHE   A CA  
2673 C C   A PHE   A 132 ? 0.1604 0.1672 0.1274 -0.0012 0.0067  0.0091  132 PHE   A C   
2674 C C   B PHE   A 132 ? 0.1599 0.1664 0.1729 0.0198  -0.0151 0.0085  132 PHE   A C   
2675 O O   A PHE   A 132 ? 0.1645 0.1843 0.1472 0.0013  0.0050  0.0055  132 PHE   A O   
2676 O O   B PHE   A 132 ? 0.1713 0.1768 0.1894 0.0184  -0.0011 0.0013  132 PHE   A O   
2677 C CB  A PHE   A 132 ? 0.1643 0.1383 0.1305 -0.0022 -0.0030 0.0107  132 PHE   A CB  
2678 C CB  B PHE   A 132 ? 0.1516 0.1574 0.1543 0.0146  -0.0151 0.0171  132 PHE   A CB  
2679 C CG  A PHE   A 132 ? 0.1694 0.1406 0.1363 -0.0030 -0.0131 0.0096  132 PHE   A CG  
2680 C CG  B PHE   A 132 ? 0.1567 0.1600 0.1499 0.0153  -0.0158 0.0051  132 PHE   A CG  
2681 C CD1 A PHE   A 132 ? 0.1662 0.1476 0.1712 0.0002  -0.0180 0.0030  132 PHE   A CD1 
2682 C CD1 B PHE   A 132 ? 0.1539 0.1632 0.1585 0.0160  -0.0089 -0.0027 132 PHE   A CD1 
2683 C CD2 A PHE   A 132 ? 0.1703 0.1535 0.1559 -0.0064 -0.0048 0.0151  132 PHE   A CD2 
2684 C CD2 B PHE   A 132 ? 0.1573 0.1631 0.1433 0.0135  -0.0170 -0.0035 132 PHE   A CD2 
2685 C CE1 A PHE   A 132 ? 0.1663 0.1511 0.1698 -0.0051 -0.0208 0.0020  132 PHE   A CE1 
2686 C CE1 B PHE   A 132 ? 0.1526 0.1628 0.1465 0.0208  -0.0071 -0.0104 132 PHE   A CE1 
2687 C CE2 A PHE   A 132 ? 0.1727 0.1541 0.1806 0.0019  -0.0145 0.0102  132 PHE   A CE2 
2688 C CE2 B PHE   A 132 ? 0.1550 0.1631 0.1404 0.0207  -0.0149 -0.0115 132 PHE   A CE2 
2689 C CZ  A PHE   A 132 ? 0.1699 0.1531 0.1784 -0.0001 -0.0233 0.0052  132 PHE   A CZ  
2690 C CZ  B PHE   A 132 ? 0.1532 0.1615 0.1397 0.0210  -0.0101 -0.0087 132 PHE   A CZ  
2709 N N   A GLY   A 133 ? 0.1606 0.1692 0.1285 -0.0012 -0.0030 0.0124  133 GLY   A N   
2710 N N   B GLY   A 133 ? 0.1596 0.1631 0.1716 0.0146  -0.0210 0.0123  133 GLY   A N   
2711 C CA  A GLY   A 133 ? 0.1732 0.1768 0.1377 -0.0035 -0.0141 0.0003  133 GLY   A CA  
2712 C CA  B GLY   A 133 ? 0.1622 0.1681 0.1718 0.0087  -0.0253 0.0082  133 GLY   A CA  
2713 C C   A GLY   A 133 ? 0.1822 0.1916 0.1479 -0.0201 -0.0406 0.0022  133 GLY   A C   
2714 C C   B GLY   A 133 ? 0.1640 0.1765 0.1729 0.0024  -0.0351 -0.0009 133 GLY   A C   
2715 O O   A GLY   A 133 ? 0.1919 0.2092 0.1736 -0.0227 -0.0390 -0.0118 133 GLY   A O   
2716 O O   B GLY   A 133 ? 0.1638 0.1899 0.1747 0.0021  -0.0297 -0.0156 133 GLY   A O   
2723 N N   A ALA   A 134 ? 0.1877 0.1794 0.1536 -0.0210 -0.0293 0.0026  134 ALA   A N   
2724 N N   B ALA   A 134 ? 0.1673 0.1647 0.1793 0.0042  -0.0307 -0.0009 134 ALA   A N   
2725 C CA  A ALA   A 134 ? 0.1924 0.1783 0.1837 -0.0189 -0.0327 -0.0025 134 ALA   A CA  
2726 C CA  B ALA   A 134 ? 0.1712 0.1612 0.1873 0.0003  -0.0269 -0.0027 134 ALA   A CA  
2727 C C   A ALA   A 134 ? 0.1925 0.1871 0.1977 -0.0189 -0.0400 0.0087  134 ALA   A C   
2728 C C   B ALA   A 134 ? 0.1730 0.1631 0.1883 -0.0022 -0.0256 -0.0018 134 ALA   A C   
2729 O O   A ALA   A 134 ? 0.1968 0.1905 0.2195 -0.0202 -0.0287 0.0161  134 ALA   A O   
2730 O O   B ALA   A 134 ? 0.1657 0.1626 0.2018 -0.0079 -0.0101 -0.0016 134 ALA   A O   
2731 C CB  A ALA   A 134 ? 0.1999 0.1731 0.2155 -0.0173 -0.0266 -0.0089 134 ALA   A CB  
2732 C CB  B ALA   A 134 ? 0.1751 0.1578 0.2013 0.0006  -0.0249 -0.0057 134 ALA   A CB  
2743 N N   A ASP   A 135 ? 0.1940 0.1863 0.2098 -0.0189 -0.0358 0.0190  135 ASP   A N   
2744 N N   B ASP   A 135 ? 0.1828 0.1678 0.1907 -0.0015 -0.0328 0.0055  135 ASP   A N   
2745 C CA  A ASP   A 135 ? 0.1910 0.1903 0.2351 -0.0280 -0.0440 0.0246  135 ASP   A CA  
2746 C CA  B ASP   A 135 ? 0.1815 0.1711 0.2020 0.0011  -0.0359 0.0008  135 ASP   A CA  
2747 C C   A ASP   A 135 ? 0.1719 0.1804 0.2354 -0.0211 -0.0334 0.0391  135 ASP   A C   
2748 C C   B ASP   A 135 ? 0.1685 0.1639 0.1983 0.0052  -0.0299 -0.0003 135 ASP   A C   
2749 O O   A ASP   A 135 ? 0.1627 0.1728 0.2405 -0.0176 -0.0274 0.0412  135 ASP   A O   
2750 O O   B ASP   A 135 ? 0.1662 0.1571 0.1992 0.0091  -0.0240 0.0069  135 ASP   A O   
2751 C CB  A ASP   A 135 ? 0.2071 0.2110 0.2683 -0.0478 -0.0563 0.0141  135 ASP   A CB  
2752 C CB  B ASP   A 135 ? 0.1904 0.1823 0.2107 -0.0020 -0.0389 -0.0056 135 ASP   A CB  
2753 C CG  A ASP   A 135 ? 0.2232 0.2345 0.2986 -0.0608 -0.0627 0.0101  135 ASP   A CG  
2754 C CG  B ASP   A 135 ? 0.2004 0.1940 0.2253 -0.0024 -0.0402 -0.0082 135 ASP   A CG  
2755 O OD1 A ASP   A 135 ? 0.2148 0.2413 0.2898 -0.0649 -0.0749 0.0276  135 ASP   A OD1 
2756 O OD1 B ASP   A 135 ? 0.2029 0.1910 0.2251 0.0006  -0.0415 -0.0078 135 ASP   A OD1 
2757 O OD2 A ASP   A 135 ? 0.2530 0.2568 0.3499 -0.0608 -0.0395 0.0003  135 ASP   A OD2 
2758 O OD2 B ASP   A 135 ? 0.2042 0.2046 0.2419 -0.0038 -0.0441 -0.0138 135 ASP   A OD2 
2767 N N   A PRO   A 136 ? 0.1583 0.1697 0.2366 -0.0159 -0.0312 0.0455  136 PRO   A N   
2768 N N   B PRO   A 136 ? 0.1601 0.1626 0.1969 0.0027  -0.0266 -0.0067 136 PRO   A N   
2769 C CA  A PRO   A 136 ? 0.1502 0.1693 0.2495 -0.0180 -0.0204 0.0307  136 PRO   A CA  
2770 C CA  B PRO   A 136 ? 0.1556 0.1714 0.1966 -0.0035 -0.0158 -0.0131 136 PRO   A CA  
2771 C C   A PRO   A 136 ? 0.1290 0.1629 0.2456 -0.0035 -0.0164 0.0243  136 PRO   A C   
2772 C C   B PRO   A 136 ? 0.1381 0.1735 0.1834 -0.0033 -0.0166 -0.0067 136 PRO   A C   
2773 O O   A PRO   A 136 ? 0.1300 0.1634 0.2381 -0.0079 -0.0050 0.0161  136 PRO   A O   
2774 O O   B PRO   A 136 ? 0.1359 0.1691 0.1661 0.0047  0.0017  -0.0088 136 PRO   A O   
2775 C CB  A PRO   A 136 ? 0.1623 0.1680 0.2630 -0.0244 -0.0269 0.0263  136 PRO   A CB  
2776 C CB  B PRO   A 136 ? 0.1687 0.1714 0.2067 -0.0042 -0.0140 -0.0173 136 PRO   A CB  
2777 C CG  A PRO   A 136 ? 0.1726 0.1729 0.2731 -0.0181 -0.0276 0.0325  136 PRO   A CG  
2778 C CG  B PRO   A 136 ? 0.1764 0.1720 0.2185 -0.0011 -0.0226 -0.0139 136 PRO   A CG  
2779 C CD  A PRO   A 136 ? 0.1656 0.1679 0.2449 -0.0182 -0.0300 0.0469  136 PRO   A CD  
2780 C CD  B PRO   A 136 ? 0.1647 0.1660 0.2085 0.0048  -0.0241 -0.0112 136 PRO   A CD  
2795 N N   A ILE   A 137 ? 0.1316 0.1595 0.2494 -0.0010 -0.0219 0.0242  137 ILE   A N   
2796 N N   B ILE   A 137 ? 0.1384 0.1737 0.1975 -0.0076 -0.0227 -0.0018 137 ILE   A N   
2797 C CA  A ILE   A 137 ? 0.1354 0.1644 0.2570 -0.0180 -0.0285 0.0307  137 ILE   A CA  
2798 C CA  B ILE   A 137 ? 0.1435 0.1785 0.1989 -0.0060 -0.0196 -0.0015 137 ILE   A CA  
2799 C C   A ILE   A 137 ? 0.1398 0.1630 0.2372 -0.0175 -0.0299 0.0315  137 ILE   A C   
2800 C C   B ILE   A 137 ? 0.1414 0.1847 0.1893 -0.0118 -0.0108 0.0047  137 ILE   A C   
2801 O O   A ILE   A 137 ? 0.1503 0.1579 0.2477 -0.0155 -0.0172 0.0263  137 ILE   A O   
2802 O O   B ILE   A 137 ? 0.1376 0.1851 0.1930 -0.0135 -0.0047 0.0057  137 ILE   A O   
2803 C CB  A ILE   A 137 ? 0.1454 0.1803 0.2908 -0.0195 -0.0435 0.0323  137 ILE   A CB  
2804 C CB  B ILE   A 137 ? 0.1552 0.1753 0.2152 -0.0017 -0.0302 -0.0002 137 ILE   A CB  
2805 C CG1 A ILE   A 137 ? 0.1598 0.2019 0.3277 -0.0196 -0.0356 0.0389  137 ILE   A CG1 
2806 C CG1 B ILE   A 137 ? 0.1657 0.1795 0.2473 0.0039  -0.0398 0.0079  137 ILE   A CG1 
2807 C CG2 A ILE   A 137 ? 0.1595 0.1794 0.2992 -0.0171 -0.0566 0.0133  137 ILE   A CG2 
2808 C CG2 B ILE   A 137 ? 0.1661 0.1709 0.2117 0.0083  -0.0326 -0.0040 137 ILE   A CG2 
2809 C CD1 A ILE   A 137 ? 0.1811 0.2142 0.3454 -0.0153 -0.0296 0.0440  137 ILE   A CD1 
2810 C CD1 B ILE   A 137 ? 0.1726 0.1774 0.2657 0.0045  -0.0433 0.0136  137 ILE   A CD1 
2833 N N   A HIS   A 138 ? 0.1414 0.1820 0.2201 -0.0088 -0.0209 0.0183  138 HIS   A N   
2834 N N   B HIS   A 138 ? 0.1430 0.1941 0.1899 -0.0113 0.0058  0.0052  138 HIS   A N   
2835 C CA  A HIS   A 138 ? 0.1463 0.1960 0.2072 -0.0089 -0.0147 0.0153  138 HIS   A CA  
2836 C CA  B HIS   A 138 ? 0.1465 0.1952 0.1873 -0.0125 0.0119  0.0116  138 HIS   A CA  
2837 C C   A HIS   A 138 ? 0.1354 0.1892 0.1980 -0.0021 -0.0217 0.0222  138 HIS   A C   
2838 C C   B HIS   A 138 ? 0.1412 0.1879 0.1939 -0.0087 0.0000  0.0229  138 HIS   A C   
2839 O O   A HIS   A 138 ? 0.1443 0.1859 0.2054 -0.0031 -0.0113 0.0197  138 HIS   A O   
2840 O O   B HIS   A 138 ? 0.1462 0.1879 0.2015 -0.0121 0.0063  0.0216  138 HIS   A O   
2841 C CB  A HIS   A 138 ? 0.1670 0.2144 0.2085 -0.0138 -0.0265 0.0096  138 HIS   A CB  
2842 C CB  B HIS   A 138 ? 0.1492 0.2027 0.1827 -0.0114 0.0149  0.0026  138 HIS   A CB  
2843 C CG  A HIS   A 138 ? 0.1865 0.2322 0.2179 -0.0182 -0.0229 0.0075  138 HIS   A CG  
2844 C CG  B HIS   A 138 ? 0.1606 0.2123 0.1917 -0.0115 0.0102  -0.0053 138 HIS   A CG  
2845 N ND1 A HIS   A 138 ? 0.1978 0.2464 0.2371 -0.0178 -0.0192 -0.0064 138 HIS   A ND1 
2846 N ND1 B HIS   A 138 ? 0.1682 0.2192 0.2093 -0.0089 0.0026  -0.0149 138 HIS   A ND1 
2847 C CD2 A HIS   A 138 ? 0.1896 0.2400 0.2164 -0.0140 -0.0251 0.0125  138 HIS   A CD2 
2848 C CD2 B HIS   A 138 ? 0.1609 0.2139 0.1949 -0.0080 0.0122  -0.0022 138 HIS   A CD2 
2849 C CE1 A HIS   A 138 ? 0.2040 0.2537 0.2408 -0.0107 -0.0227 0.0005  138 HIS   A CE1 
2850 C CE1 B HIS   A 138 ? 0.1705 0.2201 0.2138 -0.0048 0.0025  -0.0123 138 HIS   A CE1 
2851 N NE2 A HIS   A 138 ? 0.1984 0.2519 0.2270 -0.0090 -0.0189 0.0112  138 HIS   A NE2 
2852 N NE2 B HIS   A 138 ? 0.1663 0.2186 0.2056 -0.0047 0.0120  -0.0065 138 HIS   A NE2 
2867 N N   . SER   A 139 ? 0.1361 0.1792 0.1988 -0.0091 -0.0124 0.0339  139 SER   A N   
2868 C CA  . SER   A 139 ? 0.1309 0.1728 0.1990 -0.0141 -0.0058 0.0454  139 SER   A CA  
2869 C C   . SER   A 139 ? 0.1282 0.1655 0.1965 -0.0108 -0.0050 0.0270  139 SER   A C   
2870 O O   . SER   A 139 ? 0.1234 0.1645 0.2049 -0.0144 -0.0080 0.0348  139 SER   A O   
2871 C CB  . SER   A 139 ? 0.1303 0.1697 0.2049 -0.0211 -0.0093 0.0368  139 SER   A CB  
2872 O OG  . SER   A 139 ? 0.1391 0.1660 0.2051 -0.0242 -0.0141 0.0465  139 SER   A OG  
2879 N N   . LEU   A 140 ? 0.1246 0.1679 0.1977 -0.0133 -0.0039 0.0431  140 LEU   A N   
2880 C CA  . LEU   A 140 ? 0.1217 0.1624 0.1990 -0.0159 -0.0030 0.0403  140 LEU   A CA  
2881 C C   . LEU   A 140 ? 0.1217 0.1723 0.2020 -0.0208 0.0006  0.0414  140 LEU   A C   
2882 O O   . LEU   A 140 ? 0.1259 0.1745 0.2182 -0.0149 -0.0083 0.0409  140 LEU   A O   
2883 C CB  . LEU   A 140 ? 0.1303 0.1702 0.2079 -0.0141 0.0047  0.0405  140 LEU   A CB  
2884 C CG  . LEU   A 140 ? 0.1309 0.1840 0.2219 -0.0257 0.0046  0.0462  140 LEU   A CG  
2885 C CD1 . LEU   A 140 ? 0.1344 0.1870 0.2338 -0.0192 0.0041  0.0440  140 LEU   A CD1 
2886 C CD2 . LEU   A 140 ? 0.1329 0.2018 0.2318 -0.0202 0.0117  0.0405  140 LEU   A CD2 
2898 N N   . ARG   A 141 ? 0.1327 0.1707 0.2112 -0.0165 -0.0078 0.0273  141 ARG   A N   
2899 C CA  . ARG   A 141 ? 0.1446 0.1818 0.2305 -0.0253 -0.0231 0.0117  141 ARG   A CA  
2900 C C   . ARG   A 141 ? 0.1415 0.1694 0.2158 -0.0151 -0.0150 0.0139  141 ARG   A C   
2901 O O   . ARG   A 141 ? 0.1338 0.1647 0.2325 -0.0145 -0.0028 0.0149  141 ARG   A O   
2902 C CB  . ARG   A 141 ? 0.1575 0.2091 0.2646 -0.0315 -0.0260 -0.0111 141 ARG   A CB  
2903 C CG  . ARG   A 141 ? 0.1922 0.2471 0.3083 -0.0344 -0.0158 -0.0099 141 ARG   A CG  
2904 C CD  . ARG   A 141 ? 0.2227 0.2769 0.3456 -0.0391 -0.0128 -0.0102 141 ARG   A CD  
2905 N NE  . ARG   A 141 ? 0.2129 0.2960 0.3626 -0.0406 -0.0236 -0.0083 141 ARG   A NE  
2906 C CZ  . ARG   A 141 ? 0.2087 0.3125 0.3662 -0.0512 -0.0222 -0.0026 141 ARG   A CZ  
2907 N NH1 . ARG   A 141 ? 0.2018 0.3165 0.3597 -0.0513 -0.0093 -0.0167 141 ARG   A NH1 
2908 N NH2 . ARG   A 141 ? 0.2112 0.3210 0.3825 -0.0474 -0.0344 0.0077  141 ARG   A NH2 
2922 N N   . VAL   A 142 ? 0.1313 0.1686 0.1891 -0.0143 -0.0082 0.0160  142 VAL   A N   
2923 C CA  . VAL   A 142 ? 0.1367 0.1625 0.1996 -0.0092 0.0077  0.0106  142 VAL   A CA  
2924 C C   . VAL   A 142 ? 0.1234 0.1530 0.2000 -0.0114 0.0053  0.0205  142 VAL   A C   
2925 O O   . VAL   A 142 ? 0.1281 0.1497 0.2034 -0.0051 0.0033  0.0176  142 VAL   A O   
2926 C CB  . VAL   A 142 ? 0.1424 0.1702 0.1950 -0.0098 0.0067  0.0222  142 VAL   A CB  
2927 C CG1 . VAL   A 142 ? 0.1463 0.1662 0.2019 -0.0137 0.0060  0.0113  142 VAL   A CG1 
2928 C CG2 . VAL   A 142 ? 0.1596 0.1889 0.2116 0.0019  0.0041  0.0226  142 VAL   A CG2 
2938 N N   . CYS   A 143 ? 0.1234 0.1474 0.1977 -0.0157 -0.0006 0.0207  143 CYS   A N   
2939 C CA  . CYS   A 143 ? 0.1282 0.1545 0.2051 -0.0142 0.0041  0.0255  143 CYS   A CA  
2940 C C   . CYS   A 143 ? 0.1285 0.1508 0.2029 -0.0106 -0.0013 0.0335  143 CYS   A C   
2941 O O   . CYS   A 143 ? 0.1268 0.1423 0.2000 -0.0093 -0.0019 0.0295  143 CYS   A O   
2942 C CB  . CYS   A 143 ? 0.1371 0.1572 0.2148 -0.0104 0.0105  0.0310  143 CYS   A CB  
2943 S SG  . CYS   A 143 ? 0.1535 0.1650 0.1861 0.0012  0.0116  0.0236  143 CYS   A SG  
2949 N N   . VAL   A 144 ? 0.1253 0.1517 0.2281 -0.0076 0.0084  0.0390  144 VAL   A N   
2950 C CA  . VAL   A 144 ? 0.1337 0.1645 0.2596 -0.0151 0.0177  0.0393  144 VAL   A CA  
2951 C C   . VAL   A 144 ? 0.1395 0.1554 0.2620 -0.0223 -0.0090 0.0328  144 VAL   A C   
2952 O O   . VAL   A 144 ? 0.1521 0.1640 0.2701 -0.0101 -0.0125 0.0460  144 VAL   A O   
2953 C CB  . VAL   A 144 ? 0.1613 0.1888 0.3128 -0.0103 0.0283  0.0456  144 VAL   A CB  
2954 C CG1 . VAL   A 144 ? 0.1724 0.2123 0.3583 -0.0181 0.0062  0.0454  144 VAL   A CG1 
2955 C CG2 . VAL   A 144 ? 0.1517 0.1900 0.3160 -0.0087 0.0289  0.0545  144 VAL   A CG2 
2965 N N   . ASP   A 145 ? 0.1496 0.1484 0.2728 -0.0230 -0.0074 0.0193  145 ASP   A N   
2966 C CA  . ASP   A 145 ? 0.1625 0.1567 0.2794 -0.0208 -0.0137 0.0098  145 ASP   A CA  
2967 C C   . ASP   A 145 ? 0.1592 0.1443 0.2632 -0.0177 -0.0071 0.0003  145 ASP   A C   
2968 O O   . ASP   A 145 ? 0.1721 0.1555 0.3142 -0.0177 -0.0086 -0.0310 145 ASP   A O   
2969 C CB  . ASP   A 145 ? 0.1719 0.1829 0.2947 -0.0315 -0.0262 0.0076  145 ASP   A CB  
2970 C CG  . ASP   A 145 ? 0.1903 0.2197 0.3228 -0.0500 -0.0378 0.0156  145 ASP   A CG  
2971 O OD1 . ASP   A 145 ? 0.1862 0.2347 0.3353 -0.0651 -0.0230 0.0172  145 ASP   A OD1 
2972 O OD2 . ASP   A 145 ? 0.2144 0.2405 0.3352 -0.0577 -0.0626 0.0129  145 ASP   A OD2 
2977 N N   . THR   A 146 ? 0.1433 0.1387 0.2250 -0.0165 -0.0032 0.0120  146 THR   A N   
2978 C CA  . THR   A 146 ? 0.1336 0.1377 0.2074 -0.0093 -0.0027 0.0113  146 THR   A CA  
2979 C C   . THR   A 146 ? 0.1257 0.1411 0.2030 -0.0038 0.0031  0.0203  146 THR   A C   
2980 O O   . THR   A 146 ? 0.1408 0.1494 0.2113 0.0005  -0.0058 0.0117  146 THR   A O   
2981 C CB  . THR   A 146 ? 0.1321 0.1439 0.2008 -0.0052 -0.0016 0.0154  146 THR   A CB  
2982 O OG1 . THR   A 146 ? 0.1301 0.1603 0.2110 0.0015  -0.0071 0.0114  146 THR   A OG1 
2983 C CG2 . THR   A 146 ? 0.1298 0.1455 0.2093 -0.0084 -0.0022 0.0064  146 THR   A CG2 
2991 N N   . VAL   A 147 ? 0.1247 0.1428 0.1919 -0.0020 0.0039  0.0198  147 VAL   A N   
2992 C CA  . VAL   A 147 ? 0.1307 0.1462 0.1909 -0.0077 0.0170  0.0272  147 VAL   A CA  
2993 C C   . VAL   A 147 ? 0.1334 0.1447 0.2064 -0.0108 0.0108  0.0296  147 VAL   A C   
2994 O O   . VAL   A 147 ? 0.1340 0.1481 0.2241 -0.0152 0.0053  0.0295  147 VAL   A O   
2995 C CB  . VAL   A 147 ? 0.1471 0.1437 0.1895 -0.0129 0.0232  0.0247  147 VAL   A CB  
2996 C CG1 . VAL   A 147 ? 0.1765 0.1558 0.1736 -0.0027 0.0189  0.0271  147 VAL   A CG1 
2997 C CG2 . VAL   A 147 ? 0.1447 0.1435 0.1953 -0.0105 0.0067  0.0275  147 VAL   A CG2 
3007 N N   . ARG   A 148 ? 0.1347 0.1465 0.2089 -0.0130 0.0069  0.0442  148 ARG   A N   
3008 C CA  . ARG   A 148 ? 0.1417 0.1444 0.2073 -0.0136 0.0049  0.0531  148 ARG   A CA  
3009 C C   . ARG   A 148 ? 0.1542 0.1476 0.2072 -0.0215 0.0050  0.0688  148 ARG   A C   
3010 O O   . ARG   A 148 ? 0.1837 0.1636 0.2449 -0.0211 0.0122  0.0605  148 ARG   A O   
3011 C CB  . ARG   A 148 ? 0.1484 0.1457 0.2234 -0.0031 0.0174  0.0426  148 ARG   A CB  
3012 C CG  . ARG   A 148 ? 0.1575 0.1446 0.2622 -0.0115 0.0340  0.0311  148 ARG   A CG  
3013 C CD  . ARG   A 148 ? 0.1699 0.1495 0.2814 -0.0084 0.0382  0.0552  148 ARG   A CD  
3014 N NE  . ARG   A 148 ? 0.1729 0.1569 0.2860 0.0033  0.0327  0.0616  148 ARG   A NE  
3015 C CZ  . ARG   A 148 ? 0.1660 0.1420 0.2663 0.0005  0.0351  0.0513  148 ARG   A CZ  
3016 N NH1 . ARG   A 148 ? 0.1697 0.1437 0.2789 -0.0088 0.0331  0.0257  148 ARG   A NH1 
3017 N NH2 . ARG   A 148 ? 0.1599 0.1679 0.2594 0.0099  0.0378  0.0565  148 ARG   A NH2 
3031 N N   . THR   A 149 ? 0.1523 0.1588 0.2021 -0.0179 -0.0032 0.0488  149 THR   A N   
3032 C CA  . THR   A 149 ? 0.1505 0.1668 0.2034 -0.0172 0.0068  0.0495  149 THR   A CA  
3033 C C   . THR   A 149 ? 0.1477 0.1657 0.1894 -0.0250 0.0052  0.0550  149 THR   A C   
3034 O O   . THR   A 149 ? 0.1460 0.1768 0.2101 -0.0252 0.0010  0.0470  149 THR   A O   
3035 C CB  . THR   A 149 ? 0.1480 0.1790 0.2124 -0.0184 0.0081  0.0492  149 THR   A CB  
3036 O OG1 . THR   A 149 ? 0.1532 0.1621 0.2288 -0.0260 0.0052  0.0428  149 THR   A OG1 
3037 C CG2 . THR   A 149 ? 0.1513 0.1953 0.2132 -0.0126 -0.0004 0.0362  149 THR   A CG2 
3045 N N   . ASN   A 150 ? 0.1488 0.1733 0.1818 -0.0151 -0.0049 0.0582  150 ASN   A N   
3046 C CA  . ASN   A 150 ? 0.1636 0.1870 0.1955 -0.0176 0.0046  0.0507  150 ASN   A CA  
3047 C C   . ASN   A 150 ? 0.1415 0.1744 0.2055 -0.0254 -0.0004 0.0450  150 ASN   A C   
3048 O O   . ASN   A 150 ? 0.1537 0.1829 0.2440 -0.0195 -0.0068 0.0414  150 ASN   A O   
3049 C CB  . ASN   A 150 ? 0.2108 0.2085 0.2275 -0.0278 0.0214  0.0644  150 ASN   A CB  
3050 C CG  . ASN   A 150 ? 0.2707 0.2382 0.2892 -0.0279 0.0080  0.0736  150 ASN   A CG  
3051 O OD1 . ASN   A 150 ? 0.2987 0.2463 0.3163 -0.0359 0.0116  0.0907  150 ASN   A OD1 
3052 N ND2 . ASN   A 150 ? 0.3041 0.2600 0.3206 -0.0216 -0.0085 0.0711  150 ASN   A ND2 
3059 N N   . VAL   A 151 ? 0.1446 0.1602 0.2033 -0.0280 0.0043  0.0444  151 VAL   A N   
3060 C CA  . VAL   A 151 ? 0.1471 0.1621 0.1985 -0.0303 0.0111  0.0504  151 VAL   A CA  
3061 C C   . VAL   A 151 ? 0.1407 0.1605 0.2051 -0.0306 0.0130  0.0418  151 VAL   A C   
3062 O O   . VAL   A 151 ? 0.1484 0.1713 0.2312 -0.0228 0.0091  0.0370  151 VAL   A O   
3063 C CB  . VAL   A 151 ? 0.1758 0.1791 0.2059 -0.0157 0.0161  0.0474  151 VAL   A CB  
3064 C CG1 . VAL   A 151 ? 0.1727 0.2001 0.2302 -0.0175 0.0043  0.0342  151 VAL   A CG1 
3065 C CG2 . VAL   A 151 ? 0.1856 0.1744 0.2107 -0.0111 0.0218  0.0400  151 VAL   A CG2 
3075 N N   . TYR   A 152 ? 0.1433 0.1630 0.1944 -0.0261 0.0040  0.0391  152 TYR   A N   
3076 C CA  . TYR   A 152 ? 0.1429 0.1702 0.1680 -0.0292 0.0102  0.0386  152 TYR   A CA  
3077 C C   . TYR   A 152 ? 0.1404 0.1627 0.1685 -0.0260 0.0226  0.0398  152 TYR   A C   
3078 O O   . TYR   A 152 ? 0.1438 0.1555 0.1821 -0.0260 0.0216  0.0315  152 TYR   A O   
3079 C CB  . TYR   A 152 ? 0.1621 0.1782 0.1811 -0.0249 0.0195  0.0361  152 TYR   A CB  
3080 C CG  . TYR   A 152 ? 0.1799 0.2024 0.1792 -0.0354 0.0259  0.0431  152 TYR   A CG  
3081 C CD1 . TYR   A 152 ? 0.1945 0.2200 0.2059 -0.0259 0.0213  0.0540  152 TYR   A CD1 
3082 C CD2 . TYR   A 152 ? 0.1888 0.2152 0.1707 -0.0507 0.0189  0.0383  152 TYR   A CD2 
3083 C CE1 . TYR   A 152 ? 0.2247 0.2338 0.2099 -0.0216 0.0009  0.0634  152 TYR   A CE1 
3084 C CE2 . TYR   A 152 ? 0.2141 0.2278 0.1839 -0.0509 0.0177  0.0434  152 TYR   A CE2 
3085 C CZ  . TYR   A 152 ? 0.2417 0.2334 0.1969 -0.0376 0.0070  0.0650  152 TYR   A CZ  
3086 O OH  . TYR   A 152 ? 0.2739 0.2557 0.2260 -0.0287 0.0141  0.0749  152 TYR   A OH  
3096 N N   A LEU   A 153 ? 0.1387 0.1561 0.1906 -0.0321 0.0245  0.0427  153 LEU   A N   
3097 N N   B LEU   A 153 ? 0.1418 0.1685 0.1602 -0.0235 0.0114  0.0393  153 LEU   A N   
3098 C CA  A LEU   A 153 ? 0.1333 0.1446 0.2013 -0.0241 0.0299  0.0316  153 LEU   A CA  
3099 C CA  B LEU   A 153 ? 0.1405 0.1695 0.1526 -0.0109 0.0040  0.0352  153 LEU   A CA  
3100 C C   A LEU   A 153 ? 0.1337 0.1516 0.1942 -0.0197 0.0367  0.0192  153 LEU   A C   
3101 C C   B LEU   A 153 ? 0.1420 0.1798 0.1451 -0.0078 0.0012  0.0267  153 LEU   A C   
3102 O O   A LEU   A 153 ? 0.1412 0.1642 0.2113 -0.0239 0.0418  0.0084  153 LEU   A O   
3103 O O   B LEU   A 153 ? 0.1458 0.1867 0.1506 -0.0125 0.0089  0.0195  153 LEU   A O   
3104 C CB  A LEU   A 153 ? 0.1214 0.1392 0.2112 -0.0178 0.0275  0.0330  153 LEU   A CB  
3105 C CB  B LEU   A 153 ? 0.1302 0.1637 0.1550 0.0034  0.0000  0.0434  153 LEU   A CB  
3106 C CG  A LEU   A 153 ? 0.1247 0.1341 0.2176 -0.0180 0.0309  0.0146  153 LEU   A CG  
3107 C CG  B LEU   A 153 ? 0.1323 0.1598 0.1602 0.0066  0.0029  0.0421  153 LEU   A CG  
3108 C CD1 A LEU   A 153 ? 0.1348 0.1278 0.2175 -0.0078 0.0144  0.0174  153 LEU   A CD1 
3109 C CD1 B LEU   A 153 ? 0.1310 0.1572 0.1701 0.0105  0.0001  0.0434  153 LEU   A CD1 
3110 C CD2 A LEU   A 153 ? 0.1387 0.1451 0.2126 -0.0197 0.0381  -0.0081 153 LEU   A CD2 
3111 C CD2 B LEU   A 153 ? 0.1393 0.1667 0.1653 0.0061  0.0044  0.0343  153 LEU   A CD2 
3134 N N   A ALA   A 154 ? 0.1271 0.1421 0.1939 -0.0152 0.0341  0.0203  154 ALA   A N   
3135 N N   B ALA   A 154 ? 0.1406 0.1826 0.1251 -0.0080 0.0002  0.0231  154 ALA   A N   
3136 C CA  A ALA   A 154 ? 0.1380 0.1482 0.1882 -0.0122 0.0339  0.0156  154 ALA   A CA  
3137 C CA  B ALA   A 154 ? 0.1516 0.1876 0.1426 -0.0041 -0.0061 0.0164  154 ALA   A CA  
3138 C C   A ALA   A 154 ? 0.1292 0.1366 0.1898 -0.0030 0.0265  0.0200  154 ALA   A C   
3139 C C   B ALA   A 154 ? 0.1523 0.1861 0.1344 -0.0036 -0.0061 0.0063  154 ALA   A C   
3140 O O   A ALA   A 154 ? 0.1333 0.1469 0.1937 -0.0136 0.0228  0.0207  154 ALA   A O   
3141 O O   B ALA   A 154 ? 0.1555 0.1840 0.1189 -0.0060 -0.0013 0.0048  154 ALA   A O   
3142 C CB  A ALA   A 154 ? 0.1522 0.1642 0.1794 0.0014  0.0242  0.0074  154 ALA   A CB  
3143 C CB  B ALA   A 154 ? 0.1555 0.1905 0.1569 -0.0001 -0.0180 0.0108  154 ALA   A CB  
3154 N N   A VAL   A 155 ? 0.1202 0.1208 0.1737 0.0059  0.0321  0.0384  155 VAL   A N   
3155 N N   B VAL   A 155 ? 0.1558 0.1877 0.1458 -0.0016 -0.0076 0.0046  155 VAL   A N   
3156 C CA  A VAL   A 155 ? 0.1427 0.1346 0.2075 0.0072  0.0197  0.0399  155 VAL   A CA  
3157 C CA  B VAL   A 155 ? 0.1733 0.1999 0.1682 -0.0004 -0.0129 0.0064  155 VAL   A CA  
3158 C CA  T VAL   A 155 ? 0.1678 0.1751 0.1886 -0.0162 0.0203  0.0373  155 VAL   A CA  
3159 C C   A VAL   A 155 ? 0.1582 0.1507 0.2333 0.0346  0.0253  0.0453  155 VAL   A C   
3160 C C   B VAL   A 155 ? 0.1889 0.2203 0.1993 0.0199  -0.0188 0.0137  155 VAL   A C   
3161 C C   T VAL   A 155 ? 0.1699 0.1776 0.1886 -0.0095 0.0315  0.0465  155 VAL   A C   
3162 O O   A VAL   A 155 ? 0.1543 0.1681 0.2485 0.0423  0.0295  0.0401  155 VAL   A O   
3163 O O   B VAL   A 155 ? 0.1839 0.2256 0.1922 0.0301  -0.0254 0.0182  155 VAL   A O   
3164 O O   T VAL   A 155 ? 0.1627 0.1852 0.1857 -0.0090 0.0383  0.0512  155 VAL   A O   
3165 C CB  A VAL   A 155 ? 0.1510 0.1320 0.2133 0.0033  -0.0002 0.0335  155 VAL   A CB  
3166 C CB  B VAL   A 155 ? 0.1769 0.1969 0.1709 -0.0078 -0.0239 0.0005  155 VAL   A CB  
3167 C CB  T VAL   A 155 ? 0.1688 0.1740 0.1914 -0.0153 0.0060  0.0283  155 VAL   A CB  
3168 C CG1 A VAL   A 155 ? 0.1617 0.1395 0.2053 0.0091  -0.0023 0.0288  155 VAL   A CG1 
3169 C CG1 B VAL   A 155 ? 0.1793 0.1978 0.1695 -0.0077 -0.0289 0.0021  155 VAL   A CG1 
3170 C CG1 T VAL   A 155 ? 0.1733 0.1750 0.1849 -0.0117 0.0027  0.0257  155 VAL   A CG1 
3171 C CG2 A VAL   A 155 ? 0.1658 0.1374 0.2313 0.0064  -0.0262 0.0311  155 VAL   A CG2 
3172 C CG2 B VAL   A 155 ? 0.1858 0.1960 0.1691 -0.0112 -0.0309 -0.0032 155 VAL   A CG2 
3173 C CG2 T VAL   A 155 ? 0.1704 0.1765 0.2003 -0.0139 -0.0044 0.0245  155 VAL   A CG2 
3199 N N   A PHE   A 156 ? 0.1755 0.1573 0.2726 0.0408  0.0299  0.0515  156 PHE   A N   
3200 N N   B PHE   A 156 ? 0.2065 0.2328 0.2266 0.0277  -0.0131 0.0083  156 PHE   A N   
3201 N N   T PHE   A 156 ? 0.1793 0.1713 0.2005 -0.0081 0.0348  0.0522  156 PHE   A N   
3202 C CA  A PHE   A 156 ? 0.1952 0.1674 0.2888 0.0512  0.0313  0.0512  156 PHE   A CA  
3203 C CA  B PHE   A 156 ? 0.2240 0.2511 0.2640 0.0337  -0.0120 0.0001  156 PHE   A CA  
3204 C CA  T PHE   A 156 ? 0.1907 0.1656 0.1950 -0.0062 0.0404  0.0574  156 PHE   A CA  
3205 C C   A PHE   A 156 ? 0.1918 0.1752 0.2762 0.0568  0.0542  0.0708  156 PHE   A C   
3206 C C   B PHE   A 156 ? 0.2364 0.2636 0.2798 0.0344  -0.0077 0.0090  156 PHE   A C   
3207 C C   T PHE   A 156 ? 0.1970 0.1803 0.2089 -0.0006 0.0496  0.0575  156 PHE   A C   
3208 O O   A PHE   A 156 ? 0.2054 0.1848 0.2865 0.0439  0.0563  0.0642  156 PHE   A O   
3209 O O   B PHE   A 156 ? 0.2409 0.2684 0.2919 0.0334  0.0018  0.0057  156 PHE   A O   
3210 O O   T PHE   A 156 ? 0.2046 0.1847 0.2239 -0.0003 0.0465  0.0498  156 PHE   A O   
3211 C CB  A PHE   A 156 ? 0.2150 0.1807 0.3038 0.0474  0.0148  0.0445  156 PHE   A CB  
3212 C CB  B PHE   A 156 ? 0.2384 0.2613 0.2896 0.0321  -0.0195 -0.0109 156 PHE   A CB  
3213 C CB  T PHE   A 156 ? 0.1897 0.1482 0.1762 -0.0099 0.0323  0.0636  156 PHE   A CB  
3214 C CG  A PHE   A 156 ? 0.2434 0.1949 0.3155 0.0468  -0.0033 0.0351  156 PHE   A CG  
3215 C CG  B PHE   A 156 ? 0.2484 0.2696 0.3091 0.0306  -0.0290 -0.0238 156 PHE   A CG  
3216 C CG  T PHE   A 156 ? 0.1899 0.1378 0.1650 -0.0077 0.0231  0.0706  156 PHE   A CG  
3217 C CD1 A PHE   A 156 ? 0.2589 0.2113 0.3240 0.0456  -0.0052 0.0238  156 PHE   A CD1 
3218 C CD1 B PHE   A 156 ? 0.2557 0.2748 0.3176 0.0318  -0.0322 -0.0249 156 PHE   A CD1 
3219 C CD1 T PHE   A 156 ? 0.1874 0.1398 0.1707 -0.0099 0.0179  0.0619  156 PHE   A CD1 
3220 C CD2 A PHE   A 156 ? 0.2591 0.2025 0.3275 0.0509  -0.0098 0.0357  156 PHE   A CD2 
3221 C CD2 B PHE   A 156 ? 0.2503 0.2731 0.3144 0.0299  -0.0354 -0.0306 156 PHE   A CD2 
3222 C CD2 T PHE   A 156 ? 0.1943 0.1365 0.1672 -0.0046 0.0207  0.0731  156 PHE   A CD2 
3223 C CE1 A PHE   A 156 ? 0.2706 0.2167 0.3306 0.0464  -0.0036 0.0195  156 PHE   A CE1 
3224 C CE1 B PHE   A 156 ? 0.2592 0.2764 0.3225 0.0314  -0.0308 -0.0282 156 PHE   A CE1 
3225 C CE1 T PHE   A 156 ? 0.1877 0.1423 0.1838 -0.0089 0.0165  0.0481  156 PHE   A CE1 
3226 C CE2 A PHE   A 156 ? 0.2712 0.2133 0.3360 0.0505  -0.0130 0.0236  156 PHE   A CE2 
3227 C CE2 B PHE   A 156 ? 0.2531 0.2754 0.3178 0.0301  -0.0397 -0.0331 156 PHE   A CE2 
3228 C CE2 T PHE   A 156 ? 0.1966 0.1396 0.1751 -0.0055 0.0149  0.0594  156 PHE   A CE2 
3229 C CZ  A PHE   A 156 ? 0.2742 0.2168 0.3365 0.0505  -0.0029 0.0146  156 PHE   A CZ  
3230 C CZ  B PHE   A 156 ? 0.2578 0.2765 0.3196 0.0328  -0.0347 -0.0336 156 PHE   A CZ  
3231 C CZ  T PHE   A 156 ? 0.1908 0.1382 0.1842 -0.0105 0.0184  0.0482  156 PHE   A CZ  
3259 N N   A ASP   A 157 ? 0.1911 0.1852 0.2622 0.0614  0.0656  0.0899  157 ASP   A N   
3260 N N   B ASP   A 157 ? 0.2461 0.2729 0.2828 0.0344  -0.0133 0.0151  157 ASP   A N   
3261 N N   T ASP   A 157 ? 0.1956 0.1929 0.2143 0.0021  0.0541  0.0622  157 ASP   A N   
3262 C CA  A ASP   A 157 ? 0.2071 0.2099 0.2609 0.0650  0.0548  0.0967  157 ASP   A CA  
3263 C CA  B ASP   A 157 ? 0.2555 0.2862 0.2978 0.0316  -0.0169 0.0267  157 ASP   A CA  
3264 C CA  T ASP   A 157 ? 0.2002 0.2066 0.2185 0.0122  0.0515  0.0608  157 ASP   A CA  
3265 C C   A ASP   A 157 ? 0.1876 0.2335 0.2742 0.0627  0.0474  0.1019  157 ASP   A C   
3266 C C   B ASP   A 157 ? 0.2526 0.2854 0.3042 0.0291  -0.0242 0.0314  157 ASP   A C   
3267 C C   T ASP   A 157 ? 0.2051 0.2239 0.2282 0.0173  0.0472  0.0613  157 ASP   A C   
3268 O O   A ASP   A 157 ? 0.1739 0.2341 0.2709 0.0622  0.0411  0.1053  157 ASP   A O   
3269 O O   B ASP   A 157 ? 0.2540 0.2887 0.3056 0.0284  -0.0302 0.0364  157 ASP   A O   
3270 O O   T ASP   A 157 ? 0.1992 0.2253 0.2291 0.0193  0.0478  0.0581  157 ASP   A O   
3271 C CB  A ASP   A 157 ? 0.2376 0.2201 0.2741 0.0744  0.0521  0.0916  157 ASP   A CB  
3272 C CB  B ASP   A 157 ? 0.2677 0.2985 0.3078 0.0250  -0.0102 0.0294  157 ASP   A CB  
3273 C CB  T ASP   A 157 ? 0.1983 0.2060 0.2210 0.0187  0.0547  0.0592  157 ASP   A CB  
3274 C CG  A ASP   A 157 ? 0.2614 0.2334 0.2966 0.0844  0.0456  0.0893  157 ASP   A CG  
3275 C CG  B ASP   A 157 ? 0.2772 0.3057 0.3088 0.0222  -0.0029 0.0319  157 ASP   A CG  
3276 C CG  T ASP   A 157 ? 0.1908 0.2032 0.2193 0.0282  0.0536  0.0594  157 ASP   A CG  
3277 O OD1 A ASP   A 157 ? 0.2845 0.2433 0.3132 0.0808  0.0304  0.0803  157 ASP   A OD1 
3278 O OD1 B ASP   A 157 ? 0.2847 0.3046 0.3031 0.0214  -0.0012 0.0382  157 ASP   A OD1 
3279 O OD1 T ASP   A 157 ? 0.1914 0.1997 0.2268 0.0265  0.0590  0.0460  157 ASP   A OD1 
3280 O OD2 A ASP   A 157 ? 0.2545 0.2261 0.3098 0.0861  0.0609  0.0989  157 ASP   A OD2 
3281 O OD2 B ASP   A 157 ? 0.2747 0.3110 0.3174 0.0252  -0.0030 0.0301  157 ASP   A OD2 
3282 O OD2 T ASP   A 157 ? 0.1746 0.1985 0.2026 0.0348  0.0496  0.0705  157 ASP   A OD2 
3295 N N   A LYS   A 158 ? 0.1915 0.2590 0.2912 0.0551  0.0492  0.0846  158 LYS   A N   
3296 N N   B LYS   A 158 ? 0.2465 0.2789 0.2974 0.0235  -0.0309 0.0313  158 LYS   A N   
3297 N N   T LYS   A 158 ? 0.2187 0.2401 0.2408 0.0194  0.0401  0.0547  158 LYS   A N   
3298 C CA  A LYS   A 158 ? 0.1847 0.2788 0.2967 0.0593  0.0501  0.0714  158 LYS   A CA  
3299 C CA  B LYS   A 158 ? 0.2468 0.2746 0.2863 0.0139  -0.0221 0.0264  158 LYS   A CA  
3300 C CA  T LYS   A 158 ? 0.2303 0.2557 0.2589 0.0220  0.0301  0.0452  158 LYS   A CA  
3301 C C   A LYS   A 158 ? 0.1732 0.2856 0.2855 0.0616  0.0365  0.0661  158 LYS   A C   
3302 C C   B LYS   A 158 ? 0.2244 0.2575 0.2501 0.0121  -0.0258 0.0147  158 LYS   A C   
3303 C C   T LYS   A 158 ? 0.2334 0.2621 0.2578 0.0232  0.0197  0.0390  158 LYS   A C   
3304 O O   A LYS   A 158 ? 0.1636 0.2911 0.2843 0.0569  0.0464  0.0643  158 LYS   A O   
3305 O O   B LYS   A 158 ? 0.2136 0.2552 0.2293 0.0047  -0.0198 0.0146  158 LYS   A O   
3306 O O   T LYS   A 158 ? 0.2317 0.2638 0.2553 0.0225  0.0174  0.0386  158 LYS   A O   
3307 C CB  A LYS   A 158 ? 0.2044 0.2931 0.3286 0.0522  0.0731  0.0615  158 LYS   A CB  
3308 C CB  B LYS   A 158 ? 0.2655 0.2885 0.3105 0.0090  -0.0116 0.0345  158 LYS   A CB  
3309 C CB  T LYS   A 158 ? 0.2427 0.2648 0.2862 0.0210  0.0333  0.0386  158 LYS   A CB  
3310 C CG  A LYS   A 158 ? 0.2266 0.3066 0.3651 0.0469  0.0848  0.0613  158 LYS   A CG  
3311 C CG  B LYS   A 158 ? 0.2779 0.3008 0.3351 0.0034  -0.0006 0.0442  158 LYS   A CG  
3312 C CG  T LYS   A 158 ? 0.2542 0.2728 0.3138 0.0199  0.0342  0.0364  158 LYS   A CG  
3313 C CD  A LYS   A 158 ? 0.2435 0.3181 0.3955 0.0461  0.1003  0.0651  158 LYS   A CD  
3314 C CD  B LYS   A 158 ? 0.2868 0.3104 0.3560 -0.0026 0.0122  0.0561  158 LYS   A CD  
3315 C CD  T LYS   A 158 ? 0.2634 0.2796 0.3414 0.0207  0.0344  0.0365  158 LYS   A CD  
3316 C CE  A LYS   A 158 ? 0.2545 0.3240 0.4123 0.0409  0.1174  0.0740  158 LYS   A CE  
3317 C CE  B LYS   A 158 ? 0.2916 0.3158 0.3687 -0.0043 0.0218  0.0654  158 LYS   A CE  
3318 C CE  T LYS   A 158 ? 0.2712 0.2836 0.3618 0.0208  0.0349  0.0391  158 LYS   A CE  
3319 N NZ  A LYS   A 158 ? 0.2537 0.3268 0.4212 0.0378  0.1295  0.0801  158 LYS   A NZ  
3320 N NZ  B LYS   A 158 ? 0.2948 0.3178 0.3783 -0.0039 0.0265  0.0714  158 LYS   A NZ  
3321 N NZ  T LYS   A 158 ? 0.2753 0.2858 0.3726 0.0227  0.0350  0.0401  158 LYS   A NZ  
3361 N N   A ASN   A 159 ? 0.1738 0.2849 0.2859 0.0572  0.0165  0.0616  159 ASN   A N   
3362 N N   B ASN   A 159 ? 0.2186 0.2504 0.2446 0.0201  -0.0283 0.0056  159 ASN   A N   
3363 N N   T ASN   A 159 ? 0.2383 0.2643 0.2646 0.0211  0.0128  0.0334  159 ASN   A N   
3364 C CA  A ASN   A 159 ? 0.1758 0.2869 0.2817 0.0462  -0.0046 0.0577  159 ASN   A CA  
3365 C CA  B ASN   A 159 ? 0.2137 0.2450 0.2427 0.0288  -0.0242 0.0073  159 ASN   A CA  
3366 C CA  T ASN   A 159 ? 0.2442 0.2667 0.2692 0.0171  0.0053  0.0289  159 ASN   A CA  
3367 C C   A ASN   A 159 ? 0.1581 0.2828 0.2583 0.0320  0.0031  0.0477  159 ASN   A C   
3368 C C   B ASN   A 159 ? 0.1956 0.2329 0.2398 0.0270  -0.0169 0.0069  159 ASN   A C   
3369 C C   T ASN   A 159 ? 0.2439 0.2656 0.2646 0.0137  0.0097  0.0237  159 ASN   A C   
3370 O O   A ASN   A 159 ? 0.1358 0.2765 0.2544 0.0322  -0.0040 0.0354  159 ASN   A O   
3371 O O   B ASN   A 159 ? 0.1870 0.2370 0.2472 0.0301  -0.0220 -0.0015 159 ASN   A O   
3372 O O   T ASN   A 159 ? 0.2414 0.2635 0.2677 0.0135  0.0096  0.0196  159 ASN   A O   
3373 C CB  A ASN   A 159 ? 0.1971 0.2951 0.3092 0.0436  -0.0181 0.0639  159 ASN   A CB  
3374 C CB  B ASN   A 159 ? 0.2292 0.2545 0.2584 0.0339  -0.0225 0.0052  159 ASN   A CB  
3375 C CB  T ASN   A 159 ? 0.2509 0.2707 0.2833 0.0151  -0.0019 0.0306  159 ASN   A CB  
3376 C CG  A ASN   A 159 ? 0.2152 0.3079 0.3436 0.0383  -0.0233 0.0609  159 ASN   A CG  
3377 C CG  B ASN   A 159 ? 0.2405 0.2670 0.2832 0.0281  -0.0160 -0.0062 159 ASN   A CG  
3378 C CG  T ASN   A 159 ? 0.2567 0.2756 0.3000 0.0124  -0.0064 0.0297  159 ASN   A CG  
3379 O OD1 A ASN   A 159 ? 0.2227 0.3193 0.3550 0.0384  -0.0152 0.0588  159 ASN   A OD1 
3380 O OD1 B ASN   A 159 ? 0.2433 0.2771 0.2945 0.0242  -0.0123 -0.0157 159 ASN   A OD1 
3381 O OD1 T ASN   A 159 ? 0.2588 0.2806 0.3070 0.0125  -0.0024 0.0281  159 ASN   A OD1 
3382 N ND2 A ASN   A 159 ? 0.2247 0.3146 0.3646 0.0315  -0.0235 0.0531  159 ASN   A ND2 
3383 N ND2 B ASN   A 159 ? 0.2439 0.2701 0.2908 0.0277  -0.0173 -0.0017 159 ASN   A ND2 
3384 N ND2 T ASN   A 159 ? 0.2596 0.2785 0.3095 0.0102  -0.0097 0.0279  159 ASN   A ND2 
3403 N N   A LEU   A 160 ? 0.1547 0.2741 0.2439 0.0205  0.0009  0.0592  160 LEU   A N   
3404 N N   B LEU   A 160 ? 0.1871 0.2210 0.2223 0.0184  -0.0130 0.0277  160 LEU   A N   
3405 N N   T LEU   A 160 ? 0.2438 0.2626 0.2592 0.0102  0.0101  0.0271  160 LEU   A N   
3406 C CA  A LEU   A 160 ? 0.1534 0.2676 0.2376 0.0020  0.0158  0.0690  160 LEU   A CA  
3407 C CA  B LEU   A 160 ? 0.1855 0.2144 0.2198 0.0102  0.0038  0.0404  160 LEU   A CA  
3408 C CA  T LEU   A 160 ? 0.2456 0.2606 0.2574 0.0053  0.0142  0.0317  160 LEU   A CA  
3409 C C   A LEU   A 160 ? 0.1268 0.2617 0.2126 -0.0059 0.0180  0.0651  160 LEU   A C   
3410 C C   B LEU   A 160 ? 0.1730 0.2067 0.2113 0.0054  0.0047  0.0399  160 LEU   A C   
3411 O O   A LEU   A 160 ? 0.1145 0.2622 0.2149 -0.0122 0.0090  0.0631  160 LEU   A O   
3412 O O   B LEU   A 160 ? 0.1691 0.1950 0.2177 -0.0001 0.0035  0.0360  160 LEU   A O   
3413 C CB  A LEU   A 160 ? 0.1734 0.2695 0.2559 -0.0065 0.0213  0.0788  160 LEU   A CB  
3414 C CB  B LEU   A 160 ? 0.1989 0.2201 0.2315 0.0010  0.0133  0.0502  160 LEU   A CB  
3415 C CB  T LEU   A 160 ? 0.2465 0.2597 0.2559 0.0007  0.0163  0.0358  160 LEU   A CB  
3416 C CG  A LEU   A 160 ? 0.1853 0.2731 0.2772 -0.0115 0.0221  0.0786  160 LEU   A CG  
3417 C CG  B LEU   A 160 ? 0.2091 0.2302 0.2492 -0.0038 0.0196  0.0522  160 LEU   A CG  
3418 C CG  T LEU   A 160 ? 0.2469 0.2602 0.2574 -0.0025 0.0178  0.0368  160 LEU   A CG  
3419 C CD1 A LEU   A 160 ? 0.1851 0.2747 0.2779 -0.0097 0.0218  0.0741  160 LEU   A CD1 
3420 C CD1 B LEU   A 160 ? 0.2121 0.2327 0.2540 -0.0031 0.0206  0.0542  160 LEU   A CD1 
3421 C CD1 T LEU   A 160 ? 0.2455 0.2604 0.2544 -0.0017 0.0173  0.0361  160 LEU   A CD1 
3422 C CD2 A LEU   A 160 ? 0.1954 0.2756 0.2868 -0.0175 0.0269  0.0719  160 LEU   A CD2 
3423 C CD2 B LEU   A 160 ? 0.2140 0.2355 0.2490 -0.0065 0.0274  0.0468  160 LEU   A CD2 
3424 C CD2 T LEU   A 160 ? 0.2487 0.2606 0.2587 -0.0054 0.0211  0.0343  160 LEU   A CD2 
3457 N N   A TYR   A 161 ? 0.1345 0.2512 0.2271 -0.0004 0.0130  0.0681  161 TYR   A N   
3458 N N   B TYR   A 161 ? 0.1717 0.2132 0.2087 0.0043  0.0073  0.0451  161 TYR   A N   
3459 C CA  A TYR   A 161 ? 0.1384 0.2489 0.2389 0.0011  0.0209  0.0618  161 TYR   A CA  
3460 C CA  B TYR   A 161 ? 0.1747 0.2213 0.2114 -0.0002 0.0103  0.0507  161 TYR   A CA  
3461 C C   A TYR   A 161 ? 0.1381 0.2613 0.2578 -0.0046 0.0171  0.0515  161 TYR   A C   
3462 C C   B TYR   A 161 ? 0.1682 0.2234 0.2177 -0.0045 0.0168  0.0396  161 TYR   A C   
3463 O O   A TYR   A 161 ? 0.1318 0.2600 0.2769 -0.0120 0.0129  0.0623  161 TYR   A O   
3464 O O   B TYR   A 161 ? 0.1661 0.2269 0.2256 -0.0115 0.0139  0.0440  161 TYR   A O   
3465 C CB  A TYR   A 161 ? 0.1464 0.2396 0.2530 0.0015  0.0167  0.0638  161 TYR   A CB  
3466 C CB  B TYR   A 161 ? 0.1863 0.2286 0.2166 0.0010  0.0068  0.0597  161 TYR   A CB  
3467 C CG  A TYR   A 161 ? 0.1442 0.2284 0.2570 0.0002  0.0131  0.0601  161 TYR   A CG  
3468 C CG  B TYR   A 161 ? 0.1981 0.2343 0.2301 0.0037  0.0059  0.0701  161 TYR   A CG  
3469 C CD1 A TYR   A 161 ? 0.1415 0.2136 0.2581 -0.0033 0.0137  0.0590  161 TYR   A CD1 
3470 C CD1 B TYR   A 161 ? 0.2039 0.2357 0.2366 0.0054  0.0049  0.0715  161 TYR   A CD1 
3471 C CD2 A TYR   A 161 ? 0.1470 0.2319 0.2637 0.0093  0.0099  0.0614  161 TYR   A CD2 
3472 C CD2 B TYR   A 161 ? 0.2055 0.2376 0.2390 0.0068  0.0072  0.0797  161 TYR   A CD2 
3473 C CE1 A TYR   A 161 ? 0.1451 0.2008 0.2518 -0.0013 0.0136  0.0588  161 TYR   A CE1 
3474 C CE1 B TYR   A 161 ? 0.2091 0.2408 0.2376 0.0076  0.0054  0.0737  161 TYR   A CE1 
3475 C CE2 A TYR   A 161 ? 0.1496 0.2146 0.2717 0.0020  0.0161  0.0639  161 TYR   A CE2 
3476 C CE2 B TYR   A 161 ? 0.2087 0.2377 0.2401 0.0057  0.0073  0.0869  161 TYR   A CE2 
3477 C CZ  A TYR   A 161 ? 0.1589 0.2022 0.2600 -0.0034 0.0116  0.0670  161 TYR   A CZ  
3478 C CZ  B TYR   A 161 ? 0.2156 0.2417 0.2457 0.0086  0.0088  0.0819  161 TYR   A CZ  
3479 O OH  A TYR   A 161 ? 0.1718 0.1853 0.2782 -0.0169 0.0000  0.0690  161 TYR   A OH  
3480 O OH  B TYR   A 161 ? 0.2231 0.2497 0.2695 0.0105  0.0129  0.0811  161 TYR   A OH  
3499 N N   A ASP   A 162 ? 0.1341 0.2718 0.2421 -0.0052 0.0219  0.0376  162 ASP   A N   
3500 N N   B ASP   A 162 ? 0.1642 0.2213 0.2139 -0.0060 0.0233  0.0284  162 ASP   A N   
3501 C CA  A ASP   A 162 ? 0.1338 0.2907 0.2423 -0.0048 0.0225  0.0226  162 ASP   A CA  
3502 C CA  B ASP   A 162 ? 0.1644 0.2260 0.2151 -0.0111 0.0259  0.0129  162 ASP   A CA  
3503 C C   A ASP   A 162 ? 0.1362 0.2931 0.2344 -0.0050 0.0189  0.0148  162 ASP   A C   
3504 C C   B ASP   A 162 ? 0.1583 0.2247 0.2080 -0.0173 0.0256  0.0139  162 ASP   A C   
3505 O O   A ASP   A 162 ? 0.1437 0.2912 0.2263 -0.0102 0.0232  0.0005  162 ASP   A O   
3506 O O   B ASP   A 162 ? 0.1505 0.2223 0.1957 -0.0264 0.0225  0.0097  162 ASP   A O   
3507 C CB  A ASP   A 162 ? 0.1453 0.3090 0.2648 0.0033  0.0356  0.0116  162 ASP   A CB  
3508 C CB  B ASP   A 162 ? 0.1790 0.2350 0.2369 -0.0043 0.0272  -0.0011 162 ASP   A CB  
3509 C CG  A ASP   A 162 ? 0.1638 0.3247 0.2906 0.0112  0.0451  0.0016  162 ASP   A CG  
3510 C CG  B ASP   A 162 ? 0.1974 0.2444 0.2614 0.0093  0.0288  -0.0163 162 ASP   A CG  
3511 O OD1 A ASP   A 162 ? 0.1706 0.3265 0.2966 -0.0029 0.0488  -0.0028 162 ASP   A OD1 
3512 O OD1 B ASP   A 162 ? 0.2049 0.2534 0.2708 0.0073  0.0263  -0.0276 162 ASP   A OD1 
3513 O OD2 A ASP   A 162 ? 0.1739 0.3364 0.3097 0.0315  0.0645  -0.0061 162 ASP   A OD2 
3514 O OD2 B ASP   A 162 ? 0.2108 0.2469 0.2749 0.0186  0.0332  -0.0262 162 ASP   A OD2 
3523 N N   A LYS   A 163 ? 0.1469 0.3035 0.2377 0.0022  0.0120  0.0156  163 LYS   A N   
3524 N N   B LYS   A 163 ? 0.1655 0.2246 0.2200 -0.0188 0.0201  0.0139  163 LYS   A N   
3525 C CA  A LYS   A 163 ? 0.1585 0.3122 0.2425 0.0030  0.0059  0.0224  163 LYS   A CA  
3526 C CA  B LYS   A 163 ? 0.1781 0.2271 0.2353 -0.0180 0.0224  0.0117  163 LYS   A CA  
3527 C C   A LYS   A 163 ? 0.1541 0.2984 0.2430 -0.0063 0.0182  0.0285  163 LYS   A C   
3528 C C   B LYS   A 163 ? 0.1606 0.1998 0.2087 -0.0180 0.0308  0.0056  163 LYS   A C   
3529 O O   A LYS   A 163 ? 0.1457 0.3038 0.2498 -0.0122 0.0209  0.0151  163 LYS   A O   
3530 O O   B LYS   A 163 ? 0.1510 0.2002 0.2046 -0.0101 0.0337  -0.0014 163 LYS   A O   
3531 C CB  A LYS   A 163 ? 0.1940 0.3353 0.2875 0.0135  -0.0070 0.0247  163 LYS   A CB  
3532 C CB  B LYS   A 163 ? 0.2110 0.2546 0.2823 -0.0141 0.0148  0.0146  163 LYS   A CB  
3533 C CG  A LYS   A 163 ? 0.2341 0.3541 0.3447 0.0110  -0.0094 0.0273  163 LYS   A CG  
3534 C CG  B LYS   A 163 ? 0.2411 0.2778 0.3340 -0.0116 0.0151  0.0191  163 LYS   A CG  
3535 C CD  A LYS   A 163 ? 0.2728 0.3704 0.4050 0.0058  -0.0107 0.0258  163 LYS   A CD  
3536 C CD  B LYS   A 163 ? 0.2716 0.2981 0.3838 -0.0105 0.0125  0.0221  163 LYS   A CD  
3537 C CE  A LYS   A 163 ? 0.3002 0.3836 0.4506 0.0037  -0.0048 0.0261  163 LYS   A CE  
3538 C CE  B LYS   A 163 ? 0.2936 0.3127 0.4170 -0.0109 0.0139  0.0278  163 LYS   A CE  
3539 N NZ  A LYS   A 163 ? 0.3088 0.3917 0.4781 -0.0000 -0.0046 0.0272  163 LYS   A NZ  
3540 N NZ  B LYS   A 163 ? 0.2970 0.3179 0.4418 -0.0106 0.0138  0.0269  163 LYS   A NZ  
3567 N N   A LEU   A 164 ? 0.1373 0.2670 0.2314 -0.0141 0.0229  0.0335  164 LEU   A N   
3568 N N   B LEU   A 164 ? 0.1503 0.1785 0.2031 -0.0304 0.0198  0.0150  164 LEU   A N   
3569 C CA  A LEU   A 164 ? 0.1476 0.2438 0.2289 -0.0246 0.0248  0.0362  164 LEU   A CA  
3570 C CA  B LEU   A 164 ? 0.1504 0.1666 0.1999 -0.0335 0.0276  0.0266  164 LEU   A CA  
3571 C C   A LEU   A 164 ? 0.1549 0.2340 0.2271 -0.0256 0.0217  0.0261  164 LEU   A C   
3572 C C   B LEU   A 164 ? 0.1601 0.1688 0.2072 -0.0294 0.0228  0.0241  164 LEU   A C   
3573 O O   A LEU   A 164 ? 0.1597 0.2367 0.2261 -0.0408 0.0329  -0.0005 164 LEU   A O   
3574 O O   B LEU   A 164 ? 0.1645 0.1615 0.2074 -0.0305 0.0297  0.0113  164 LEU   A O   
3575 C CB  A LEU   A 164 ? 0.1500 0.2318 0.2345 -0.0244 0.0225  0.0528  164 LEU   A CB  
3576 C CB  B LEU   A 164 ? 0.1529 0.1634 0.2002 -0.0413 0.0335  0.0449  164 LEU   A CB  
3577 C CG  A LEU   A 164 ? 0.1615 0.2307 0.2544 -0.0178 0.0177  0.0664  164 LEU   A CG  
3578 C CG  B LEU   A 164 ? 0.1549 0.1659 0.2142 -0.0378 0.0281  0.0431  164 LEU   A CG  
3579 C CD1 A LEU   A 164 ? 0.1489 0.2205 0.2413 -0.0150 0.0286  0.0867  164 LEU   A CD1 
3580 C CD1 B LEU   A 164 ? 0.1579 0.1696 0.2189 -0.0378 0.0295  0.0427  164 LEU   A CD1 
3581 C CD2 A LEU   A 164 ? 0.1713 0.2372 0.2581 -0.0253 0.0188  0.0590  164 LEU   A CD2 
3582 C CD2 B LEU   A 164 ? 0.1514 0.1667 0.2200 -0.0350 0.0210  0.0325  164 LEU   A CD2 
3605 N N   A VAL   A 165 ? 0.1433 0.2302 0.2220 -0.0263 0.0214  0.0410  165 VAL   A N   
3606 N N   B VAL   A 165 ? 0.1656 0.1803 0.2106 -0.0263 0.0249  0.0266  165 VAL   A N   
3607 C CA  A VAL   A 165 ? 0.1523 0.2351 0.2197 -0.0291 0.0222  0.0565  165 VAL   A CA  
3608 C CA  B VAL   A 165 ? 0.1682 0.1908 0.2047 -0.0283 0.0248  0.0314  165 VAL   A CA  
3609 C C   A VAL   A 165 ? 0.1491 0.2542 0.2241 -0.0319 0.0280  0.0509  165 VAL   A C   
3610 C C   B VAL   A 165 ? 0.1624 0.1986 0.2043 -0.0265 0.0256  0.0384  165 VAL   A C   
3611 O O   A VAL   A 165 ? 0.1492 0.2530 0.2208 -0.0330 0.0258  0.0371  165 VAL   A O   
3612 O O   B VAL   A 165 ? 0.1632 0.1897 0.1913 -0.0244 0.0333  0.0476  165 VAL   A O   
3613 C CB  A VAL   A 165 ? 0.1691 0.2325 0.2268 -0.0232 0.0309  0.0622  165 VAL   A CB  
3614 C CB  B VAL   A 165 ? 0.1761 0.1951 0.2189 -0.0328 0.0215  0.0220  165 VAL   A CB  
3615 C CG1 A VAL   A 165 ? 0.1734 0.2367 0.2227 -0.0212 0.0315  0.0562  165 VAL   A CG1 
3616 C CG1 B VAL   A 165 ? 0.1775 0.1966 0.2261 -0.0336 0.0161  0.0228  165 VAL   A CG1 
3617 C CG2 A VAL   A 165 ? 0.1747 0.2294 0.2270 -0.0159 0.0317  0.0692  165 VAL   A CG2 
3618 C CG2 B VAL   A 165 ? 0.1827 0.1999 0.2221 -0.0311 0.0260  0.0151  165 VAL   A CG2 
3637 N N   A SER   A 166 ? 0.1390 0.2754 0.2480 -0.0283 0.0277  0.0535  166 SER   A N   
3638 N N   B SER   A 166 ? 0.1554 0.2135 0.2154 -0.0321 0.0173  0.0383  166 SER   A N   
3639 C CA  A SER   A 166 ? 0.1432 0.3054 0.2623 -0.0337 0.0247  0.0469  166 SER   A CA  
3640 C CA  B SER   A 166 ? 0.1525 0.2359 0.2261 -0.0359 0.0109  0.0324  166 SER   A CA  
3641 C C   A SER   A 166 ? 0.1357 0.3275 0.2637 -0.0343 0.0031  0.0344  166 SER   A C   
3642 C C   B SER   A 166 ? 0.1692 0.2593 0.2281 -0.0406 0.0094  0.0298  166 SER   A C   
3643 O O   A SER   A 166 ? 0.1549 0.3432 0.2907 -0.0427 0.0006  0.0129  166 SER   A O   
3644 O O   B SER   A 166 ? 0.1666 0.2711 0.2384 -0.0471 0.0043  0.0189  166 SER   A O   
3645 C CB  A SER   A 166 ? 0.1623 0.3191 0.2868 -0.0246 0.0123  0.0390  166 SER   A CB  
3646 C CB  B SER   A 166 ? 0.1374 0.2356 0.2370 -0.0320 0.0014  0.0291  166 SER   A CB  
3647 O OG  A SER   A 166 ? 0.1910 0.3305 0.3078 -0.0186 0.0097  0.0423  166 SER   A OG  
3648 O OG  B SER   A 166 ? 0.1266 0.2311 0.2450 -0.0257 -0.0006 0.0293  166 SER   A OG  
3659 N N   A SER   A 167 ? 0.1379 0.3333 0.2305 -0.0167 -0.0002 0.0426  167 SER   A N   
3660 N N   B SER   A 167 ? 0.1908 0.2675 0.2182 -0.0350 0.0117  0.0292  167 SER   A N   
3661 C CA  A SER   A 167 ? 0.1604 0.3401 0.2199 -0.0101 -0.0114 0.0291  167 SER   A CA  
3662 C CA  B SER   A 167 ? 0.2168 0.2770 0.2190 -0.0259 0.0128  0.0138  167 SER   A CA  
3663 C C   A SER   A 167 ? 0.1639 0.3409 0.2159 -0.0026 0.0002  0.0385  167 SER   A C   
3664 C C   B SER   A 167 ? 0.2372 0.2859 0.2306 -0.0219 0.0131  0.0083  167 SER   A C   
3665 O O   A SER   A 167 ? 0.1786 0.3434 0.2315 0.0015  -0.0138 0.0437  167 SER   A O   
3666 O O   B SER   A 167 ? 0.2466 0.2894 0.2313 -0.0227 0.0070  0.0078  167 SER   A O   
3667 C CB  A SER   A 167 ? 0.1721 0.3473 0.2187 -0.0116 -0.0110 0.0223  167 SER   A CB  
3668 C CB  B SER   A 167 ? 0.2194 0.2755 0.2022 -0.0223 0.0214  0.0054  167 SER   A CB  
3669 O OG  A SER   A 167 ? 0.1848 0.3514 0.2076 -0.0153 -0.0018 0.0212  167 SER   A OG  
3670 O OG  B SER   A 167 ? 0.2198 0.2722 0.1832 -0.0209 0.0430  -0.0012 167 SER   A OG  
3681 N N   A PHE   A 168 ? 0.1516 0.3388 0.2003 0.0078  0.0091  0.0440  168 PHE   A N   
3682 N N   B PHE   A 168 ? 0.2485 0.2922 0.2473 -0.0164 0.0089  0.0028  168 PHE   A N   
3683 C CA  A PHE   A 168 ? 0.1578 0.3390 0.2121 0.0037  0.0169  0.0373  168 PHE   A CA  
3684 C CA  B PHE   A 168 ? 0.2636 0.2983 0.2720 -0.0140 0.0110  -0.0027 168 PHE   A CA  
3685 C C   A PHE   A 168 ? 0.1712 0.3575 0.2442 -0.0102 0.0490  0.0178  168 PHE   A C   
3686 C C   B PHE   A 168 ? 0.2908 0.3234 0.3290 -0.0066 0.0157  -0.0024 168 PHE   A C   
3687 O O   A PHE   A 168 ? 0.1820 0.3621 0.2984 -0.0228 0.0658  0.0222  168 PHE   A O   
3688 O O   B PHE   A 168 ? 0.2913 0.3249 0.3440 -0.0051 0.0191  -0.0032 168 PHE   A O   
3689 C CB  A PHE   A 168 ? 0.1600 0.3216 0.2006 0.0003  0.0019  0.0395  168 PHE   A CB  
3690 C CB  B PHE   A 168 ? 0.2535 0.2824 0.2506 -0.0238 0.0062  -0.0023 168 PHE   A CB  
3691 C CG  A PHE   A 168 ? 0.1576 0.3051 0.1948 -0.0023 -0.0044 0.0454  168 PHE   A CG  
3692 C CG  B PHE   A 168 ? 0.2432 0.2683 0.2231 -0.0322 0.0037  -0.0008 168 PHE   A CG  
3693 C CD1 A PHE   A 168 ? 0.1576 0.3005 0.1857 -0.0070 -0.0082 0.0490  168 PHE   A CD1 
3694 C CD1 B PHE   A 168 ? 0.2389 0.2642 0.2163 -0.0348 0.0015  -0.0006 168 PHE   A CD1 
3695 C CD2 A PHE   A 168 ? 0.1572 0.2967 0.1976 -0.0007 0.0041  0.0454  168 PHE   A CD2 
3696 C CD2 B PHE   A 168 ? 0.2370 0.2615 0.2063 -0.0356 0.0083  0.0005  168 PHE   A CD2 
3697 C CE1 A PHE   A 168 ? 0.1446 0.2914 0.1793 -0.0101 -0.0125 0.0563  168 PHE   A CE1 
3698 C CE1 B PHE   A 168 ? 0.2320 0.2606 0.2075 -0.0392 0.0013  0.0044  168 PHE   A CE1 
3699 C CE2 A PHE   A 168 ? 0.1607 0.2866 0.2031 -0.0042 -0.0006 0.0577  168 PHE   A CE2 
3700 C CE2 B PHE   A 168 ? 0.2341 0.2566 0.2009 -0.0393 0.0108  0.0066  168 PHE   A CE2 
3701 C CZ  A PHE   A 168 ? 0.1510 0.2848 0.1932 -0.0086 -0.0050 0.0550  168 PHE   A CZ  
3702 C CZ  B PHE   A 168 ? 0.2307 0.2583 0.2018 -0.0397 0.0049  0.0087  168 PHE   A CZ  
3721 N N   A LEU   A 169 ? 0.2114 0.3723 0.2691 -0.0235 0.0331  -0.0032 169 LEU   A N   
3722 N N   B LEU   A 169 ? 0.3186 0.3463 0.3784 -0.0006 0.0162  -0.0020 169 LEU   A N   
3723 C CA  A LEU   A 169 ? 0.2841 0.3972 0.3521 -0.0267 -0.0073 -0.0195 169 LEU   A CA  
3724 C CA  B LEU   A 169 ? 0.3451 0.3695 0.4239 0.0051  0.0088  0.0010  169 LEU   A CA  
3725 C C   A LEU   A 169 ? 0.3061 0.4021 0.3874 -0.0327 -0.0205 -0.0140 169 LEU   A C   
3726 C C   B LEU   A 169 ? 0.3509 0.3758 0.4418 0.0064  0.0069  0.0068  169 LEU   A C   
3727 O O   A LEU   A 169 ? 0.3189 0.4041 0.3998 -0.0336 -0.0227 -0.0144 169 LEU   A O   
3728 O O   B LEU   A 169 ? 0.3515 0.3780 0.4474 0.0062  0.0048  0.0095  169 LEU   A O   
3729 C CB  A LEU   A 169 ? 0.3244 0.4133 0.3865 -0.0273 -0.0249 -0.0364 169 LEU   A CB  
3730 C CB  B LEU   A 169 ? 0.3613 0.3841 0.4455 0.0061  0.0052  -0.0025 169 LEU   A CB  
3731 C CG  A LEU   A 169 ? 0.3551 0.4249 0.4134 -0.0312 -0.0388 -0.0549 169 LEU   A CG  
3732 C CG  B LEU   A 169 ? 0.3740 0.3954 0.4639 0.0058  0.0031  -0.0090 169 LEU   A CG  
3733 C CD1 A LEU   A 169 ? 0.3657 0.4276 0.4244 -0.0315 -0.0449 -0.0591 169 LEU   A CD1 
3734 C CD1 B LEU   A 169 ? 0.3783 0.3990 0.4685 0.0053  0.0022  -0.0116 169 LEU   A CD1 
3735 C CD2 A LEU   A 169 ? 0.3648 0.4298 0.4186 -0.0331 -0.0386 -0.0622 169 LEU   A CD2 
3736 C CD2 B LEU   A 169 ? 0.3773 0.3987 0.4710 0.0058  0.0039  -0.0108 169 LEU   A CD2 
3737 O OXT A LEU   A 169 ? 0.2994 0.4043 0.3930 -0.0373 -0.0251 -0.0126 169 LEU   A OXT 
3738 O OXT B LEU   A 169 ? 0.3526 0.3783 0.4489 0.0074  0.0113  0.0078  169 LEU   A OXT 
3761 N N   A SER   B 1   ? 0.3710 0.3425 0.3638 -0.1107 -0.0861 0.0414  1   SER   B N   
3762 N N   B SER   B 1   ? 0.3419 0.3278 0.3496 -0.0708 -0.0560 0.0185  1   SER   B N   
3763 C CA  A SER   B 1   ? 0.3620 0.3457 0.3675 -0.1159 -0.0906 0.0385  1   SER   B CA  
3764 C CA  B SER   B 1   ? 0.3361 0.3298 0.3470 -0.0716 -0.0566 0.0172  1   SER   B CA  
3765 C C   A SER   B 1   ? 0.3337 0.3440 0.3536 -0.1150 -0.0953 0.0605  1   SER   B C   
3766 C C   B SER   B 1   ? 0.3192 0.3292 0.3361 -0.0680 -0.0626 0.0309  1   SER   B C   
3767 O O   A SER   B 1   ? 0.3455 0.3452 0.3295 -0.1036 -0.0872 0.0618  1   SER   B O   
3768 O O   B SER   B 1   ? 0.3201 0.3281 0.3193 -0.0665 -0.0640 0.0286  1   SER   B O   
3769 C CB  A SER   B 1   ? 0.3767 0.3481 0.3781 -0.1164 -0.0826 0.0184  1   SER   B CB  
3770 C CB  B SER   B 1   ? 0.3435 0.3300 0.3524 -0.0733 -0.0490 0.0024  1   SER   B CB  
3771 O OG  A SER   B 1   ? 0.3924 0.3588 0.4190 -0.1129 -0.0705 0.0104  1   SER   B OG  
3772 O OG  B SER   B 1   ? 0.3505 0.3339 0.3727 -0.0748 -0.0437 -0.0061 1   SER   B OG  
3787 N N   A MET   B 2   ? 0.3077 0.3414 0.3579 -0.1150 -0.0927 0.1007  2   MET   B N   
3788 N N   B MET   B 2   ? 0.3072 0.3301 0.3357 -0.0620 -0.0620 0.0550  2   MET   B N   
3789 C CA  A MET   B 2   ? 0.2899 0.3431 0.3735 -0.0931 -0.0962 0.1207  2   MET   B CA  
3790 C CA  B MET   B 2   ? 0.2957 0.3305 0.3359 -0.0492 -0.0621 0.0734  2   MET   B CA  
3791 C C   A MET   B 2   ? 0.2517 0.3239 0.3390 -0.0791 -0.1031 0.1446  2   MET   B C   
3792 C C   B MET   B 2   ? 0.2746 0.3178 0.3128 -0.0455 -0.0551 0.0829  2   MET   B C   
3793 O O   A MET   B 2   ? 0.2417 0.3343 0.3383 -0.0702 -0.1169 0.1500  2   MET   B O   
3794 O O   B MET   B 2   ? 0.2756 0.3254 0.3191 -0.0419 -0.0487 0.0842  2   MET   B O   
3795 C CB  A MET   B 2   ? 0.3221 0.3761 0.4552 -0.0705 -0.0787 0.0947  2   MET   B CB  
3796 C CB  B MET   B 2   ? 0.3093 0.3473 0.3707 -0.0360 -0.0644 0.0774  2   MET   B CB  
3797 C CG  A MET   B 2   ? 0.3516 0.4072 0.5329 -0.0495 -0.0581 0.0810  2   MET   B CG  
3798 C CG  B MET   B 2   ? 0.3206 0.3613 0.3976 -0.0249 -0.0651 0.0893  2   MET   B CG  
3799 S SD  A MET   B 2   ? 0.3817 0.4365 0.6059 -0.0313 -0.0408 0.0686  2   MET   B SD  
3800 S SD  B MET   B 2   ? 0.3332 0.3764 0.4193 -0.0147 -0.0683 0.1003  2   MET   B SD  
3801 C CE  A MET   B 2   ? 0.3832 0.4383 0.6022 -0.0304 -0.0328 0.0710  2   MET   B CE  
3802 C CE  B MET   B 2   ? 0.3334 0.3782 0.4259 -0.0148 -0.0648 0.0948  2   MET   B CE  
3821 N N   A VAL   B 3   ? 0.2247 0.2907 0.3100 -0.0783 -0.0921 0.1573  3   VAL   B N   
3822 N N   B VAL   B 3   ? 0.2523 0.2962 0.2855 -0.0470 -0.0536 0.0878  3   VAL   B N   
3823 C CA  A VAL   B 3   ? 0.2147 0.2630 0.2983 -0.0734 -0.0802 0.1356  3   VAL   B CA  
3824 C CA  B VAL   B 3   ? 0.2343 0.2745 0.2651 -0.0467 -0.0512 0.0837  3   VAL   B CA  
3825 C C   A VAL   B 3   ? 0.2042 0.2535 0.2552 -0.0645 -0.0731 0.1176  3   VAL   B C   
3826 C C   B VAL   B 3   ? 0.2125 0.2591 0.2308 -0.0471 -0.0550 0.0876  3   VAL   B C   
3827 O O   A VAL   B 3   ? 0.2031 0.2548 0.2622 -0.0679 -0.0725 0.1294  3   VAL   B O   
3828 O O   B VAL   B 3   ? 0.2080 0.2649 0.2195 -0.0376 -0.0529 0.0882  3   VAL   B O   
3829 C CB  A VAL   B 3   ? 0.2293 0.2596 0.3493 -0.0748 -0.0672 0.1133  3   VAL   B CB  
3830 C CB  B VAL   B 3   ? 0.2412 0.2712 0.2830 -0.0471 -0.0422 0.0735  3   VAL   B CB  
3831 C CG1 A VAL   B 3   ? 0.2329 0.2538 0.3633 -0.0809 -0.0665 0.1098  3   VAL   B CG1 
3832 C CG1 B VAL   B 3   ? 0.2426 0.2685 0.2898 -0.0499 -0.0408 0.0704  3   VAL   B CG1 
3833 C CG2 A VAL   B 3   ? 0.2337 0.2608 0.3632 -0.0708 -0.0587 0.1232  3   VAL   B CG2 
3834 C CG2 B VAL   B 3   ? 0.2435 0.2700 0.2845 -0.0450 -0.0403 0.0775  3   VAL   B CG2 
3853 N N   . ASN   B 4   ? 0.1957 0.2329 0.2245 -0.0583 -0.0617 0.0911  4   ASN   B N   
3854 C CA  . ASN   B 4   ? 0.1951 0.2234 0.1902 -0.0593 -0.0507 0.0532  4   ASN   B CA  
3855 C C   . ASN   B 4   ? 0.2067 0.2359 0.1895 -0.0615 -0.0440 0.0432  4   ASN   B C   
3856 O O   . ASN   B 4   ? 0.2099 0.2362 0.2134 -0.0608 -0.0345 0.0195  4   ASN   B O   
3857 C CB  . ASN   B 4   ? 0.1922 0.2108 0.1837 -0.0555 -0.0591 0.0426  4   ASN   B CB  
3858 C CG  . ASN   B 4   ? 0.1936 0.1891 0.1807 -0.0494 -0.0526 0.0366  4   ASN   B CG  
3859 O OD1 . ASN   B 4   ? 0.1946 0.1723 0.1857 -0.0489 -0.0499 0.0361  4   ASN   B OD1 
3860 N ND2 . ASN   B 4   ? 0.2149 0.2006 0.1858 -0.0309 -0.0332 0.0334  4   ASN   B ND2 
3868 N N   . SER   B 5   ? 0.2226 0.2566 0.2046 -0.0600 -0.0259 0.0366  5   SER   B N   
3869 C CA  . SER   B 5   ? 0.2480 0.2923 0.2315 -0.0503 -0.0017 0.0386  5   SER   B CA  
3870 C C   . SER   B 5   ? 0.2650 0.2971 0.2619 -0.0681 0.0282  0.0388  5   SER   B C   
3871 O O   . SER   B 5   ? 0.2809 0.2959 0.3361 -0.0607 0.0706  0.0383  5   SER   B O   
3872 C CB  . SER   B 5   ? 0.2567 0.3123 0.2637 -0.0369 0.0021  0.0471  5   SER   B CB  
3873 O OG  . SER   B 5   ? 0.2782 0.3369 0.3157 -0.0234 0.0117  0.0545  5   SER   B OG  
3879 N N   . PHE   B 6   ? 0.2818 0.3165 0.2345 -0.0745 0.0355  0.0385  6   PHE   B N   
3880 C CA  . PHE   B 6   ? 0.2899 0.3180 0.2000 -0.0952 0.0350  0.0205  6   PHE   B CA  
3881 C C   . PHE   B 6   ? 0.3433 0.3537 0.2538 -0.1040 0.0593  -0.0076 6   PHE   B C   
3882 O O   . PHE   B 6   ? 0.3560 0.3842 0.2811 -0.1014 0.0417  -0.0319 6   PHE   B O   
3883 C CB  . PHE   B 6   ? 0.2556 0.2889 0.1639 -0.0916 0.0061  0.0245  6   PHE   B CB  
3884 C CG  . PHE   B 6   ? 0.2236 0.2558 0.1582 -0.0842 -0.0107 0.0232  6   PHE   B CG  
3885 C CD1 . PHE   B 6   ? 0.2250 0.2319 0.1578 -0.0761 -0.0248 0.0182  6   PHE   B CD1 
3886 C CD2 . PHE   B 6   ? 0.2025 0.2521 0.1698 -0.0656 -0.0002 0.0442  6   PHE   B CD2 
3887 C CE1 . PHE   B 6   ? 0.2183 0.2114 0.1611 -0.0594 -0.0243 0.0107  6   PHE   B CE1 
3888 C CE2 . PHE   B 6   ? 0.2002 0.2402 0.1978 -0.0494 0.0035  0.0363  6   PHE   B CE2 
3889 C CZ  . PHE   B 6   ? 0.2073 0.2185 0.1850 -0.0537 -0.0107 0.0144  6   PHE   B CZ  
3899 N N   . SER   B 7   ? 0.3809 0.3479 0.2642 -0.1219 0.0967  -0.0296 7   SER   B N   
3900 C CA  . SER   B 7   ? 0.4218 0.3709 0.3220 -0.1179 0.1268  -0.0347 7   SER   B CA  
3901 C C   . SER   B 7   ? 0.4206 0.3452 0.3071 -0.1184 0.1416  -0.0475 7   SER   B C   
3902 O O   . SER   B 7   ? 0.4285 0.3393 0.3356 -0.1217 0.1416  -0.0504 7   SER   B O   
3903 C CB  . SER   B 7   ? 0.4460 0.4001 0.3954 -0.1151 0.1465  -0.0253 7   SER   B CB  
3904 O OG  . SER   B 7   ? 0.4532 0.4071 0.4555 -0.1140 0.1490  -0.0148 7   SER   B OG  
3910 N N   . GLY   B 8   ? 0.4181 0.3292 0.3110 -0.1018 0.1444  -0.0527 8   GLY   B N   
3911 C CA  . GLY   B 8   ? 0.4031 0.3068 0.3108 -0.0968 0.1446  -0.0610 8   GLY   B CA  
3912 C C   . GLY   B 8   ? 0.3803 0.2711 0.2988 -0.0999 0.1437  -0.0574 8   GLY   B C   
3913 O O   . GLY   B 8   ? 0.3956 0.2791 0.3345 -0.0922 0.1426  -0.0632 8   GLY   B O   
3917 N N   . TYR   B 9   ? 0.3544 0.2462 0.2611 -0.0870 0.1164  -0.0742 9   TYR   B N   
3918 C CA  . TYR   B 9   ? 0.3303 0.2176 0.2259 -0.0663 0.0790  -0.0581 9   TYR   B CA  
3919 C C   . TYR   B 9   ? 0.3231 0.2225 0.2096 -0.0548 0.0449  -0.0436 9   TYR   B C   
3920 O O   . TYR   B 9   ? 0.3365 0.2427 0.2511 -0.0546 0.0448  -0.0267 9   TYR   B O   
3921 C CB  . TYR   B 9   ? 0.3204 0.1925 0.2317 -0.0538 0.0714  -0.0525 9   TYR   B CB  
3922 C CG  . TYR   B 9   ? 0.3055 0.1714 0.2326 -0.0598 0.0623  -0.0580 9   TYR   B CG  
3923 C CD1 . TYR   B 9   ? 0.3065 0.1774 0.2601 -0.0715 0.0660  -0.0448 9   TYR   B CD1 
3924 C CD2 . TYR   B 9   ? 0.2848 0.1635 0.2215 -0.0588 0.0537  -0.0519 9   TYR   B CD2 
3925 C CE1 . TYR   B 9   ? 0.2972 0.1893 0.2602 -0.0781 0.0711  -0.0537 9   TYR   B CE1 
3926 C CE2 . TYR   B 9   ? 0.2857 0.1689 0.2403 -0.0582 0.0553  -0.0473 9   TYR   B CE2 
3927 C CZ  . TYR   B 9   ? 0.2897 0.1882 0.2589 -0.0714 0.0607  -0.0614 9   TYR   B CZ  
3928 O OH  . TYR   B 9   ? 0.2883 0.2045 0.2702 -0.0846 0.0630  -0.0647 9   TYR   B OH  
3938 N N   . LEU   B 10  ? 0.2991 0.2020 0.1905 -0.0570 0.0165  -0.0322 10  LEU   B N   
3939 C CA  . LEU   B 10  ? 0.2925 0.1939 0.1963 -0.0661 -0.0110 -0.0288 10  LEU   B CA  
3940 C C   . LEU   B 10  ? 0.2682 0.1946 0.1984 -0.0636 -0.0258 -0.0270 10  LEU   B C   
3941 O O   . LEU   B 10  ? 0.2493 0.1989 0.2062 -0.0469 -0.0221 -0.0211 10  LEU   B O   
3942 C CB  . LEU   B 10  ? 0.3094 0.1880 0.2228 -0.0743 -0.0291 -0.0085 10  LEU   B CB  
3943 C CG  . LEU   B 10  ? 0.3265 0.1959 0.2557 -0.0719 -0.0571 0.0042  10  LEU   B CG  
3944 C CD1 . LEU   B 10  ? 0.3400 0.2070 0.2833 -0.0682 -0.0517 0.0044  10  LEU   B CD1 
3945 C CD2 . LEU   B 10  ? 0.3331 0.2004 0.2866 -0.0756 -0.0500 0.0254  10  LEU   B CD2 
3957 N N   . LYS   B 11  ? 0.2824 0.2155 0.1954 -0.0564 -0.0303 -0.0282 11  LYS   B N   
3958 C CA  . LYS   B 11  ? 0.2985 0.2427 0.2253 -0.0464 -0.0442 -0.0326 11  LYS   B CA  
3959 C C   . LYS   B 11  ? 0.2821 0.2206 0.2419 -0.0664 -0.0401 -0.0385 11  LYS   B C   
3960 O O   . LYS   B 11  ? 0.2997 0.2388 0.2796 -0.0812 -0.0311 -0.0714 11  LYS   B O   
3961 C CB  . LYS   B 11  ? 0.3329 0.2943 0.2891 -0.0211 -0.0492 -0.0268 11  LYS   B CB  
3962 C CG  . LYS   B 11  ? 0.3654 0.3281 0.3557 -0.0068 -0.0531 -0.0290 11  LYS   B CG  
3963 C CD  . LYS   B 11  ? 0.3921 0.3507 0.4186 0.0008  -0.0512 -0.0335 11  LYS   B CD  
3964 C CE  . LYS   B 11  ? 0.4111 0.3660 0.4662 0.0009  -0.0485 -0.0351 11  LYS   B CE  
3965 N NZ  . LYS   B 11  ? 0.4213 0.3775 0.4905 -0.0005 -0.0465 -0.0312 11  LYS   B NZ  
3979 N N   . LEU   B 12  ? 0.2468 0.1977 0.2395 -0.0594 -0.0446 -0.0370 12  LEU   B N   
3980 C CA  . LEU   B 12  ? 0.2347 0.1814 0.2518 -0.0492 -0.0384 -0.0272 12  LEU   B CA  
3981 C C   . LEU   B 12  ? 0.2241 0.1814 0.2619 -0.0508 -0.0542 -0.0240 12  LEU   B C   
3982 O O   . LEU   B 12  ? 0.2251 0.1851 0.2898 -0.0597 -0.0644 -0.0259 12  LEU   B O   
3983 C CB  . LEU   B 12  ? 0.2352 0.1551 0.2467 -0.0367 -0.0246 -0.0356 12  LEU   B CB  
3984 C CG  . LEU   B 12  ? 0.2346 0.1526 0.2487 -0.0388 -0.0113 -0.0233 12  LEU   B CG  
3985 C CD1 . LEU   B 12  ? 0.2459 0.1565 0.2437 -0.0256 -0.0024 -0.0053 12  LEU   B CD1 
3986 C CD2 . LEU   B 12  ? 0.2391 0.1622 0.2678 -0.0427 -0.0128 -0.0307 12  LEU   B CD2 
3998 N N   . THR   B 13  ? 0.2170 0.1860 0.2620 -0.0493 -0.0582 -0.0268 13  THR   B N   
3999 C CA  . THR   B 13  ? 0.2187 0.1920 0.2512 -0.0601 -0.0699 -0.0164 13  THR   B CA  
4000 C C   . THR   B 13  ? 0.2596 0.2075 0.2765 -0.0709 -0.0779 -0.0152 13  THR   B C   
4001 O O   . THR   B 13  ? 0.2802 0.2063 0.3031 -0.0764 -0.0396 -0.0130 13  THR   B O   
4002 C CB  . THR   B 13  ? 0.1993 0.1987 0.2607 -0.0526 -0.0627 -0.0083 13  THR   B CB  
4003 O OG1 . THR   B 13  ? 0.1869 0.1886 0.2728 -0.0484 -0.0511 -0.0140 13  THR   B OG1 
4004 C CG2 . THR   B 13  ? 0.2073 0.2046 0.2640 -0.0469 -0.0485 0.0055  13  THR   B CG2 
4012 N N   A ASP   B 14  ? 0.2750 0.2225 0.2930 -0.0727 -0.1049 -0.0067 14  ASP   B N   
4013 N N   B ASP   B 14  ? 0.2701 0.2188 0.2899 -0.0675 -0.0838 -0.0076 14  ASP   B N   
4014 C CA  A ASP   B 14  ? 0.2843 0.2399 0.3152 -0.0697 -0.1128 0.0128  14  ASP   B CA  
4015 C CA  B ASP   B 14  ? 0.2759 0.2301 0.3058 -0.0632 -0.0827 0.0044  14  ASP   B CA  
4016 C C   A ASP   B 14  ? 0.2713 0.2219 0.2759 -0.0755 -0.0937 0.0140  14  ASP   B C   
4017 C C   B ASP   B 14  ? 0.2614 0.2130 0.2724 -0.0663 -0.0829 0.0063  14  ASP   B C   
4018 O O   A ASP   B 14  ? 0.2971 0.2405 0.2859 -0.0749 -0.0872 0.0289  14  ASP   B O   
4019 O O   B ASP   B 14  ? 0.2749 0.2175 0.2748 -0.0647 -0.0841 0.0091  14  ASP   B O   
4020 C CB  A ASP   B 14  ? 0.3058 0.2772 0.3873 -0.0615 -0.1271 0.0163  14  ASP   B CB  
4021 C CB  B ASP   B 14  ? 0.2950 0.2582 0.3590 -0.0554 -0.0764 0.0083  14  ASP   B CB  
4022 C CG  A ASP   B 14  ? 0.3328 0.3102 0.4653 -0.0530 -0.1192 0.0016  14  ASP   B CG  
4023 C CG  B ASP   B 14  ? 0.3145 0.2832 0.4088 -0.0469 -0.0646 0.0028  14  ASP   B CG  
4024 O OD1 A ASP   B 14  ? 0.3504 0.3192 0.4848 -0.0588 -0.1148 -0.0134 14  ASP   B OD1 
4025 O OD1 B ASP   B 14  ? 0.3239 0.2943 0.4197 -0.0455 -0.0571 -0.0010 14  ASP   B OD1 
4026 O OD2 A ASP   B 14  ? 0.3354 0.3260 0.5032 -0.0505 -0.1159 0.0030  14  ASP   B OD2 
4027 O OD2 B ASP   B 14  ? 0.3193 0.2920 0.4312 -0.0473 -0.0632 0.0034  14  ASP   B OD2 
4036 N N   . ASN   B 15  ? 0.2325 0.1918 0.2468 -0.0608 -0.0858 0.0122  15  ASN   B N   
4037 C CA  . ASN   B 15  ? 0.1894 0.1633 0.2312 -0.0386 -0.0535 0.0076  15  ASN   B CA  
4038 C C   . ASN   B 15  ? 0.1704 0.1536 0.2199 -0.0247 -0.0448 0.0025  15  ASN   B C   
4039 O O   . ASN   B 15  ? 0.1751 0.1513 0.2449 -0.0247 -0.0546 -0.0139 15  ASN   B O   
4040 C CB  . ASN   B 15  ? 0.1813 0.1661 0.2440 -0.0133 -0.0583 0.0014  15  ASN   B CB  
4041 C CG  . ASN   B 15  ? 0.1635 0.1607 0.2451 -0.0177 -0.0402 0.0032  15  ASN   B CG  
4042 O OD1 . ASN   B 15  ? 0.1718 0.1917 0.2839 -0.0403 -0.0363 0.0111  15  ASN   B OD1 
4043 N ND2 . ASN   B 15  ? 0.1618 0.1421 0.2379 -0.0147 -0.0096 -0.0118 15  ASN   B ND2 
4051 N N   . VAL   B 16  ? 0.1704 0.1455 0.2146 -0.0332 -0.0544 0.0061  16  VAL   B N   
4052 C CA  . VAL   B 16  ? 0.1725 0.1496 0.1989 -0.0275 -0.0383 -0.0224 16  VAL   B CA  
4053 C C   . VAL   B 16  ? 0.1724 0.1614 0.1966 -0.0367 -0.0420 -0.0147 16  VAL   B C   
4054 O O   . VAL   B 16  ? 0.1779 0.1711 0.2287 -0.0288 -0.0406 -0.0262 16  VAL   B O   
4055 C CB  . VAL   B 16  ? 0.1795 0.1466 0.2112 -0.0080 -0.0194 -0.0179 16  VAL   B CB  
4056 C CG1 . VAL   B 16  ? 0.1951 0.1416 0.2069 0.0027  -0.0174 -0.0082 16  VAL   B CG1 
4057 C CG2 . VAL   B 16  ? 0.1834 0.1515 0.2316 -0.0066 -0.0172 -0.0170 16  VAL   B CG2 
4067 N N   . TYR   B 17  ? 0.1802 0.1690 0.1954 -0.0317 -0.0315 -0.0201 17  TYR   B N   
4068 C CA  . TYR   B 17  ? 0.1876 0.1849 0.1937 -0.0361 -0.0317 -0.0033 17  TYR   B CA  
4069 C C   . TYR   B 17  ? 0.1797 0.1559 0.1950 -0.0400 -0.0226 -0.0139 17  TYR   B C   
4070 O O   . TYR   B 17  ? 0.1782 0.1613 0.2113 -0.0336 -0.0284 -0.0351 17  TYR   B O   
4071 C CB  . TYR   B 17  ? 0.2206 0.2269 0.2127 -0.0241 -0.0344 0.0456  17  TYR   B CB  
4072 C CG  . TYR   B 17  ? 0.2486 0.2740 0.2589 -0.0186 -0.0479 0.0527  17  TYR   B CG  
4073 C CD1 . TYR   B 17  ? 0.2662 0.2871 0.2817 -0.0165 -0.0576 0.0614  17  TYR   B CD1 
4074 C CD2 . TYR   B 17  ? 0.2723 0.3040 0.2830 -0.0114 -0.0629 0.0501  17  TYR   B CD2 
4075 C CE1 . TYR   B 17  ? 0.2852 0.3173 0.3027 -0.0055 -0.0684 0.0520  17  TYR   B CE1 
4076 C CE2 . TYR   B 17  ? 0.2898 0.3287 0.3068 0.0024  -0.0782 0.0531  17  TYR   B CE2 
4077 C CZ  . TYR   B 17  ? 0.2988 0.3355 0.3163 0.0050  -0.0814 0.0518  17  TYR   B CZ  
4078 O OH  . TYR   B 17  ? 0.3147 0.3542 0.3339 0.0146  -0.0916 0.0481  17  TYR   B OH  
4088 N N   . ILE   B 18  ? 0.1899 0.1641 0.1677 -0.0335 -0.0102 -0.0137 18  ILE   B N   
4089 C CA  . ILE   B 18  ? 0.1936 0.1550 0.1676 -0.0364 -0.0106 -0.0097 18  ILE   B CA  
4090 C C   . ILE   B 18  ? 0.2099 0.1582 0.1751 -0.0481 -0.0116 -0.0243 18  ILE   B C   
4091 O O   . ILE   B 18  ? 0.2303 0.1767 0.1871 -0.0419 -0.0009 -0.0380 18  ILE   B O   
4092 C CB  . ILE   B 18  ? 0.2022 0.1567 0.1857 -0.0423 -0.0111 -0.0197 18  ILE   B CB  
4093 C CG1 . ILE   B 18  ? 0.2067 0.1641 0.1919 -0.0440 -0.0134 -0.0096 18  ILE   B CG1 
4094 C CG2 . ILE   B 18  ? 0.2075 0.1622 0.1922 -0.0469 -0.0080 -0.0175 18  ILE   B CG2 
4095 C CD1 . ILE   B 18  ? 0.2139 0.1870 0.2010 -0.0433 -0.0273 0.0259  18  ILE   B CD1 
4107 N N   . LYS   B 19  ? 0.2087 0.1579 0.1941 -0.0301 0.0301  -0.0303 19  LYS   B N   
4108 C CA  . LYS   B 19  ? 0.2149 0.1598 0.2003 -0.0279 0.0335  -0.0395 19  LYS   B CA  
4109 C C   . LYS   B 19  ? 0.1990 0.1593 0.2104 -0.0296 0.0274  -0.0510 19  LYS   B C   
4110 O O   . LYS   B 19  ? 0.1903 0.1655 0.1952 -0.0167 0.0179  -0.0426 19  LYS   B O   
4111 C CB  . LYS   B 19  ? 0.2371 0.1841 0.2243 -0.0318 0.0356  -0.0247 19  LYS   B CB  
4112 C CG  . LYS   B 19  ? 0.2615 0.2044 0.2485 -0.0410 0.0458  -0.0237 19  LYS   B CG  
4113 C CD  . LYS   B 19  ? 0.2882 0.2344 0.2691 -0.0505 0.0596  -0.0148 19  LYS   B CD  
4114 C CE  . LYS   B 19  ? 0.3183 0.2618 0.2928 -0.0538 0.0589  -0.0155 19  LYS   B CE  
4115 N NZ  . LYS   B 19  ? 0.3375 0.2780 0.2991 -0.0565 0.0644  -0.0127 19  LYS   B NZ  
4129 N N   . ASN   B 20  ? 0.2005 0.1759 0.2446 -0.0199 0.0218  -0.0605 20  ASN   B N   
4130 C CA  . ASN   B 20  ? 0.2009 0.1855 0.2730 -0.0128 0.0368  -0.0744 20  ASN   B CA  
4131 C C   . ASN   B 20  ? 0.1988 0.2100 0.2783 -0.0201 0.0510  -0.0786 20  ASN   B C   
4132 O O   . ASN   B 20  ? 0.2163 0.2471 0.2888 -0.0319 0.0575  -0.0755 20  ASN   B O   
4133 C CB  . ASN   B 20  ? 0.2260 0.1853 0.3130 0.0077  0.0203  -0.0728 20  ASN   B CB  
4134 C CG  . ASN   B 20  ? 0.2521 0.1914 0.3322 0.0390  0.0222  -0.0827 20  ASN   B CG  
4135 O OD1 . ASN   B 20  ? 0.2841 0.2187 0.3567 0.0588  0.0197  -0.0835 20  ASN   B OD1 
4136 N ND2 . ASN   B 20  ? 0.2379 0.1890 0.3181 0.0348  0.0003  -0.0767 20  ASN   B ND2 
4143 N N   . ALA   B 21  ? 0.1987 0.1865 0.2764 -0.0277 0.0468  -0.0735 21  ALA   B N   
4144 C CA  . ALA   B 21  ? 0.2040 0.1934 0.2943 -0.0300 0.0348  -0.0559 21  ALA   B CA  
4145 C C   . ALA   B 21  ? 0.2029 0.1661 0.2842 -0.0236 0.0392  -0.0380 21  ALA   B C   
4146 O O   . ALA   B 21  ? 0.2043 0.1607 0.2829 -0.0345 0.0381  -0.0332 21  ALA   B O   
4147 C CB  . ALA   B 21  ? 0.2176 0.2245 0.3007 -0.0437 0.0366  -0.0364 21  ALA   B CB  
4153 N N   . ASP   B 22  ? 0.1950 0.1577 0.2755 -0.0250 0.0278  -0.0337 22  ASP   B N   
4154 C CA  . ASP   B 22  ? 0.1940 0.1524 0.2632 -0.0080 0.0199  -0.0247 22  ASP   B CA  
4155 C C   . ASP   B 22  ? 0.1883 0.1500 0.2205 -0.0162 0.0096  -0.0134 22  ASP   B C   
4156 O O   . ASP   B 22  ? 0.1912 0.1474 0.2239 -0.0110 0.0066  -0.0091 22  ASP   B O   
4157 C CB  . ASP   B 22  ? 0.1975 0.1593 0.2929 0.0001  0.0172  -0.0088 22  ASP   B CB  
4158 C CG  . ASP   B 22  ? 0.1990 0.1779 0.3317 0.0017  0.0011  -0.0118 22  ASP   B CG  
4159 O OD1 . ASP   B 22  ? 0.2150 0.1672 0.3373 0.0031  -0.0135 -0.0109 22  ASP   B OD1 
4160 O OD2 . ASP   B 22  ? 0.2055 0.2114 0.3762 0.0103  -0.0137 -0.0260 22  ASP   B OD2 
4165 N N   . ILE   B 23  ? 0.1824 0.1410 0.2024 -0.0116 0.0025  0.0107  23  ILE   B N   
4166 C CA  . ILE   B 23  ? 0.1736 0.1418 0.1921 -0.0094 -0.0020 0.0043  23  ILE   B CA  
4167 C C   . ILE   B 23  ? 0.1622 0.1430 0.1887 -0.0029 -0.0037 -0.0006 23  ILE   B C   
4168 O O   . ILE   B 23  ? 0.1555 0.1431 0.1827 -0.0083 -0.0047 0.0056  23  ILE   B O   
4169 C CB  . ILE   B 23  ? 0.1672 0.1476 0.2037 -0.0178 0.0042  0.0145  23  ILE   B CB  
4170 C CG1 . ILE   B 23  ? 0.1737 0.1539 0.2203 -0.0116 0.0090  0.0236  23  ILE   B CG1 
4171 C CG2 . ILE   B 23  ? 0.1765 0.1728 0.2100 -0.0159 0.0069  0.0041  23  ILE   B CG2 
4172 C CD1 . ILE   B 23  ? 0.1791 0.1714 0.2237 -0.0037 -0.0008 0.0180  23  ILE   B CD1 
4184 N N   . VAL   B 24  ? 0.1664 0.1468 0.1981 -0.0092 -0.0077 -0.0015 24  VAL   B N   
4185 C CA  . VAL   B 24  ? 0.1597 0.1530 0.2167 -0.0018 -0.0196 -0.0009 24  VAL   B CA  
4186 C C   . VAL   B 24  ? 0.1618 0.1561 0.2307 -0.0060 -0.0119 0.0045  24  VAL   B C   
4187 O O   . VAL   B 24  ? 0.1537 0.1658 0.2384 -0.0137 -0.0088 0.0141  24  VAL   B O   
4188 C CB  . VAL   B 24  ? 0.1714 0.1742 0.2230 0.0000  -0.0246 0.0013  24  VAL   B CB  
4189 C CG1 . VAL   B 24  ? 0.1669 0.1763 0.2509 -0.0096 -0.0224 0.0083  24  VAL   B CG1 
4190 C CG2 . VAL   B 24  ? 0.1809 0.2010 0.2138 0.0029  -0.0200 -0.0057 24  VAL   B CG2 
4200 N N   . GLU   B 25  ? 0.1811 0.1637 0.2256 -0.0100 -0.0005 0.0118  25  GLU   B N   
4201 C CA  . GLU   B 25  ? 0.1971 0.1910 0.2412 -0.0044 0.0111  -0.0001 25  GLU   B CA  
4202 C C   . GLU   B 25  ? 0.1922 0.1826 0.2161 -0.0115 0.0129  0.0020  25  GLU   B C   
4203 O O   . GLU   B 25  ? 0.1941 0.1959 0.2330 -0.0104 0.0186  0.0079  25  GLU   B O   
4204 C CB  . GLU   B 25  ? 0.2362 0.2377 0.3026 0.0149  0.0211  -0.0054 25  GLU   B CB  
4205 C CG  . GLU   B 25  ? 0.2735 0.3003 0.4104 0.0211  0.0212  -0.0107 25  GLU   B CG  
4206 C CD  . GLU   B 25  ? 0.3164 0.3566 0.4957 0.0163  0.0194  -0.0123 25  GLU   B CD  
4207 O OE1 . GLU   B 25  ? 0.3354 0.3777 0.5229 0.0210  0.0260  -0.0094 25  GLU   B OE1 
4208 O OE2 . GLU   B 25  ? 0.3299 0.3750 0.5276 0.0147  0.0107  -0.0210 25  GLU   B OE2 
4215 N N   . GLU   B 26  ? 0.1887 0.1720 0.1859 -0.0309 0.0050  0.0042  26  GLU   B N   
4216 C CA  . GLU   B 26  ? 0.1884 0.1867 0.1992 -0.0414 -0.0094 0.0063  26  GLU   B CA  
4217 C C   . GLU   B 26  ? 0.1694 0.1831 0.1736 -0.0267 0.0074  0.0200  26  GLU   B C   
4218 O O   . GLU   B 26  ? 0.1902 0.2067 0.1920 -0.0242 0.0061  0.0227  26  GLU   B O   
4219 C CB  . GLU   B 26  ? 0.2231 0.2070 0.2208 -0.0477 0.0050  0.0158  26  GLU   B CB  
4220 C CG  . GLU   B 26  ? 0.2642 0.2463 0.2760 -0.0521 0.0191  -0.0058 26  GLU   B CG  
4221 C CD  . GLU   B 26  ? 0.2899 0.2695 0.2884 -0.0700 0.0309  -0.0405 26  GLU   B CD  
4222 O OE1 . GLU   B 26  ? 0.3108 0.2525 0.2998 -0.0774 0.0695  -0.0394 26  GLU   B OE1 
4223 O OE2 . GLU   B 26  ? 0.2914 0.3114 0.3312 -0.0636 0.0236  -0.0325 26  GLU   B OE2 
4230 N N   . ALA   B 27  ? 0.1524 0.1659 0.1756 -0.0227 0.0110  0.0235  27  ALA   B N   
4231 C CA  . ALA   B 27  ? 0.1582 0.1659 0.1912 -0.0154 0.0077  0.0281  27  ALA   B CA  
4232 C C   . ALA   B 27  ? 0.1616 0.1807 0.2065 -0.0156 0.0163  0.0418  27  ALA   B C   
4233 O O   . ALA   B 27  ? 0.1680 0.1877 0.2241 -0.0000 0.0146  0.0507  27  ALA   B O   
4234 C CB  . ALA   B 27  ? 0.1828 0.1435 0.1997 -0.0205 0.0115  0.0179  27  ALA   B CB  
4240 N N   . LYS   B 28  ? 0.1578 0.1991 0.2615 -0.0228 0.0234  0.0586  28  LYS   B N   
4241 C CA  . LYS   B 28  ? 0.1677 0.2297 0.2781 -0.0133 0.0485  0.0866  28  LYS   B CA  
4242 C C   . LYS   B 28  ? 0.1928 0.2479 0.2686 -0.0083 0.0521  0.0766  28  LYS   B C   
4243 O O   . LYS   B 28  ? 0.2184 0.2598 0.2826 -0.0115 0.0543  0.0738  28  LYS   B O   
4244 C CB  . LYS   B 28  ? 0.1906 0.2616 0.3349 -0.0040 0.0696  0.1023  28  LYS   B CB  
4245 C CG  . LYS   B 28  ? 0.2185 0.3155 0.3818 0.0110  0.0613  0.1052  28  LYS   B CG  
4246 C CD  . LYS   B 28  ? 0.2681 0.3757 0.4330 0.0167  0.0759  0.1060  28  LYS   B CD  
4247 C CE  . LYS   B 28  ? 0.3037 0.4146 0.4787 0.0260  0.0807  0.1115  28  LYS   B CE  
4248 N NZ  . LYS   B 28  ? 0.3267 0.4266 0.4984 0.0367  0.0814  0.1192  28  LYS   B NZ  
4262 N N   . LYS   B 29  ? 0.2114 0.2709 0.2731 0.0122  0.0560  0.0615  29  LYS   B N   
4263 C CA  . LYS   B 29  ? 0.2565 0.3030 0.3034 0.0166  0.0575  0.0617  29  LYS   B CA  
4264 C C   . LYS   B 29  ? 0.2493 0.3060 0.2589 0.0167  0.0440  0.0723  29  LYS   B C   
4265 O O   . LYS   B 29  ? 0.2684 0.3295 0.2727 0.0239  0.0431  0.0770  29  LYS   B O   
4266 C CB  . LYS   B 29  ? 0.3123 0.3391 0.3830 0.0179  0.0614  0.0478  29  LYS   B CB  
4267 C CG  . LYS   B 29  ? 0.3611 0.3673 0.4682 0.0163  0.0650  0.0444  29  LYS   B CG  
4268 C CD  . LYS   B 29  ? 0.4052 0.3892 0.5367 0.0114  0.0760  0.0380  29  LYS   B CD  
4269 C CE  . LYS   B 29  ? 0.4348 0.4027 0.5833 0.0067  0.0892  0.0345  29  LYS   B CE  
4270 N NZ  . LYS   B 29  ? 0.4444 0.4064 0.6114 0.0046  0.0949  0.0327  29  LYS   B NZ  
4284 N N   . VAL   B 30  ? 0.2205 0.2896 0.2488 -0.0015 0.0316  0.0749  30  VAL   B N   
4285 C CA  . VAL   B 30  ? 0.2088 0.2800 0.2800 -0.0138 0.0001  0.0848  30  VAL   B CA  
4286 C C   . VAL   B 30  ? 0.1908 0.2752 0.2674 -0.0126 0.0055  0.1014  30  VAL   B C   
4287 O O   . VAL   B 30  ? 0.2052 0.2933 0.2684 -0.0050 0.0095  0.1195  30  VAL   B O   
4288 C CB  . VAL   B 30  ? 0.2201 0.2799 0.3323 -0.0312 -0.0313 0.0789  30  VAL   B CB  
4289 C CG1 . VAL   B 30  ? 0.2281 0.2939 0.3358 -0.0295 -0.0254 0.0670  30  VAL   B CG1 
4290 C CG2 . VAL   B 30  ? 0.2348 0.2777 0.3525 -0.0392 -0.0448 0.0700  30  VAL   B CG2 
4300 N N   . LYS   B 31  ? 0.1811 0.2396 0.2987 -0.0265 0.0064  0.1074  31  LYS   B N   
4301 C CA  . LYS   B 31  ? 0.1663 0.2332 0.3267 -0.0393 0.0032  0.1102  31  LYS   B CA  
4302 C C   . LYS   B 31  ? 0.1596 0.1983 0.2856 -0.0336 -0.0265 0.0952  31  LYS   B C   
4303 O O   . LYS   B 31  ? 0.1677 0.2136 0.2981 -0.0288 -0.0219 0.1110  31  LYS   B O   
4304 C CB  . LYS   B 31  ? 0.1815 0.2821 0.3784 -0.0333 0.0257  0.1259  31  LYS   B CB  
4305 C CG  . LYS   B 31  ? 0.2196 0.3315 0.4199 -0.0310 0.0396  0.1191  31  LYS   B CG  
4306 C CD  . LYS   B 31  ? 0.2603 0.3790 0.4603 -0.0235 0.0323  0.1034  31  LYS   B CD  
4307 C CE  . LYS   B 31  ? 0.2864 0.4062 0.5010 -0.0207 0.0223  0.0874  31  LYS   B CE  
4308 N NZ  . LYS   B 31  ? 0.3000 0.4237 0.5155 -0.0117 0.0100  0.0737  31  LYS   B NZ  
4322 N N   . PRO   B 32  ? 0.1709 0.1641 0.2215 -0.0319 -0.0456 0.0572  32  PRO   B N   
4323 C CA  . PRO   B 32  ? 0.1795 0.1556 0.1885 -0.0323 -0.0382 0.0377  32  PRO   B CA  
4324 C C   . PRO   B 32  ? 0.1910 0.1431 0.1955 -0.0392 -0.0550 0.0359  32  PRO   B C   
4325 O O   . PRO   B 32  ? 0.2049 0.1429 0.2305 -0.0430 -0.0722 0.0384  32  PRO   B O   
4326 C CB  . PRO   B 32  ? 0.1895 0.1529 0.1903 -0.0375 -0.0253 0.0147  32  PRO   B CB  
4327 C CG  . PRO   B 32  ? 0.2045 0.1466 0.1962 -0.0237 -0.0470 0.0196  32  PRO   B CG  
4328 C CD  . PRO   B 32  ? 0.1957 0.1468 0.2145 -0.0270 -0.0577 0.0291  32  PRO   B CD  
4336 N N   . THR   B 33  ? 0.1950 0.1373 0.1690 -0.0331 -0.0470 0.0255  33  THR   B N   
4337 C CA  . THR   B 33  ? 0.1990 0.1489 0.1656 -0.0355 -0.0509 0.0287  33  THR   B CA  
4338 C C   . THR   B 33  ? 0.2007 0.1345 0.1635 -0.0304 -0.0418 0.0239  33  THR   B C   
4339 O O   . THR   B 33  ? 0.2174 0.1338 0.1833 -0.0427 -0.0528 0.0205  33  THR   B O   
4340 C CB  . THR   B 33  ? 0.2088 0.1581 0.1827 -0.0225 -0.0547 0.0338  33  THR   B CB  
4341 O OG1 . THR   B 33  ? 0.1968 0.1669 0.1872 -0.0222 -0.0570 0.0360  33  THR   B OG1 
4342 C CG2 . THR   B 33  ? 0.2337 0.1595 0.2108 -0.0173 -0.0494 0.0298  33  THR   B CG2 
4350 N N   . VAL   B 34  ? 0.1782 0.1346 0.1526 -0.0280 -0.0410 0.0187  34  VAL   B N   
4351 C CA  . VAL   B 34  ? 0.1653 0.1331 0.1438 -0.0254 -0.0412 0.0152  34  VAL   B CA  
4352 C C   . VAL   B 34  ? 0.1531 0.1266 0.1329 -0.0261 -0.0234 0.0087  34  VAL   B C   
4353 O O   . VAL   B 34  ? 0.1684 0.1259 0.1490 -0.0193 -0.0327 0.0109  34  VAL   B O   
4354 C CB  . VAL   B 34  ? 0.1720 0.1405 0.1785 -0.0102 -0.0376 0.0075  34  VAL   B CB  
4355 C CG1 . VAL   B 34  ? 0.1691 0.1556 0.1725 -0.0075 -0.0146 -0.0034 34  VAL   B CG1 
4356 C CG2 . VAL   B 34  ? 0.1795 0.1478 0.1993 -0.0072 -0.0301 0.0126  34  VAL   B CG2 
4366 N N   . VAL   B 35  ? 0.1437 0.1241 0.1230 -0.0257 -0.0178 0.0101  35  VAL   B N   
4367 C CA  . VAL   B 35  ? 0.1423 0.1230 0.1180 -0.0167 -0.0141 0.0023  35  VAL   B CA  
4368 C C   . VAL   B 35  ? 0.1327 0.1146 0.1248 -0.0151 -0.0154 0.0087  35  VAL   B C   
4369 O O   . VAL   B 35  ? 0.1366 0.1246 0.1308 -0.0207 -0.0055 -0.0026 35  VAL   B O   
4370 C CB  . VAL   B 35  ? 0.1380 0.1430 0.1443 -0.0190 0.0004  0.0033  35  VAL   B CB  
4371 C CG1 . VAL   B 35  ? 0.1248 0.1521 0.1799 -0.0192 -0.0018 -0.0009 35  VAL   B CG1 
4372 C CG2 . VAL   B 35  ? 0.1439 0.1420 0.1683 -0.0092 -0.0040 -0.0001 35  VAL   B CG2 
4382 N N   . VAL   B 36  ? 0.1335 0.1161 0.1279 -0.0137 -0.0219 0.0146  36  VAL   B N   
4383 C CA  . VAL   B 36  ? 0.1301 0.1153 0.1262 -0.0120 -0.0126 0.0078  36  VAL   B CA  
4384 C C   . VAL   B 36  ? 0.1297 0.1160 0.1179 -0.0096 -0.0138 0.0036  36  VAL   B C   
4385 O O   . VAL   B 36  ? 0.1375 0.1218 0.1485 -0.0119 -0.0029 -0.0061 36  VAL   B O   
4386 C CB  . VAL   B 36  ? 0.1304 0.1196 0.1326 -0.0148 -0.0101 0.0089  36  VAL   B CB  
4387 C CG1 . VAL   B 36  ? 0.1313 0.1339 0.1622 -0.0222 -0.0131 0.0037  36  VAL   B CG1 
4388 C CG2 . VAL   B 36  ? 0.1338 0.1276 0.1376 -0.0136 -0.0172 0.0090  36  VAL   B CG2 
4398 N N   . ASN   B 37  ? 0.1346 0.1198 0.1250 -0.0008 -0.0089 0.0088  37  ASN   B N   
4399 C CA  . ASN   B 37  ? 0.1333 0.1232 0.1280 -0.0003 -0.0203 0.0044  37  ASN   B CA  
4400 C C   . ASN   B 37  ? 0.1285 0.1269 0.1272 0.0028  -0.0067 0.0040  37  ASN   B C   
4401 O O   . ASN   B 37  ? 0.1379 0.1312 0.1424 0.0003  -0.0024 0.0032  37  ASN   B O   
4402 C CB  . ASN   B 37  ? 0.1300 0.1323 0.1335 0.0023  -0.0225 0.0086  37  ASN   B CB  
4403 C CG  . ASN   B 37  ? 0.1344 0.1257 0.1366 -0.0057 -0.0127 0.0023  37  ASN   B CG  
4404 O OD1 . ASN   B 37  ? 0.1405 0.1283 0.1652 0.0034  -0.0144 0.0074  37  ASN   B OD1 
4405 N ND2 . ASN   B 37  ? 0.1364 0.1255 0.1425 -0.0009 -0.0171 0.0034  37  ASN   B ND2 
4412 N N   . ALA   B 38  ? 0.1355 0.1261 0.1301 0.0074  0.0022  0.0125  38  ALA   B N   
4413 C CA  . ALA   B 38  ? 0.1485 0.1287 0.1337 0.0029  0.0008  0.0154  38  ALA   B CA  
4414 C C   . ALA   B 38  ? 0.1421 0.1222 0.1379 -0.0007 0.0008  0.0101  38  ALA   B C   
4415 O O   . ALA   B 38  ? 0.1519 0.1336 0.1548 0.0061  -0.0060 0.0076  38  ALA   B O   
4416 C CB  . ALA   B 38  ? 0.1685 0.1384 0.1535 -0.0065 0.0104  0.0066  38  ALA   B CB  
4422 N N   . ALA   B 39  ? 0.1447 0.1291 0.1253 0.0092  -0.0033 0.0020  39  ALA   B N   
4423 C CA  . ALA   B 39  ? 0.1536 0.1339 0.1077 0.0066  -0.0065 0.0031  39  ALA   B CA  
4424 C C   . ALA   B 39  ? 0.1536 0.1398 0.0935 0.0107  -0.0085 -0.0038 39  ALA   B C   
4425 O O   . ALA   B 39  ? 0.1518 0.1504 0.1477 -0.0025 -0.0107 0.0118  39  ALA   B O   
4426 C CB  . ALA   B 39  ? 0.1510 0.1392 0.1405 -0.0021 -0.0035 0.0036  39  ALA   B CB  
4432 N N   . ASN   B 40  ? 0.1564 0.1642 0.1040 -0.0072 -0.0064 -0.0065 40  ASN   B N   
4433 C CA  . ASN   B 40  ? 0.1671 0.1668 0.1335 -0.0013 -0.0119 -0.0056 40  ASN   B CA  
4434 C C   . ASN   B 40  ? 0.1661 0.1638 0.1252 0.0047  -0.0142 0.0051  40  ASN   B C   
4435 O O   . ASN   B 40  ? 0.1657 0.1560 0.1294 0.0067  -0.0139 0.0092  40  ASN   B O   
4436 C CB  . ASN   B 40  ? 0.1812 0.1616 0.1553 0.0077  -0.0146 0.0083  40  ASN   B CB  
4437 C CG  . ASN   B 40  ? 0.1850 0.1663 0.1906 0.0038  -0.0290 0.0214  40  ASN   B CG  
4438 O OD1 . ASN   B 40  ? 0.1831 0.1598 0.2714 0.0031  -0.0370 0.0243  40  ASN   B OD1 
4439 N ND2 . ASN   B 40  ? 0.1823 0.1642 0.2057 0.0023  -0.0231 0.0206  40  ASN   B ND2 
4446 N N   . VAL   B 41  ? 0.1738 0.1717 0.1316 0.0103  0.0006  -0.0008 41  VAL   B N   
4447 C CA  . VAL   B 41  ? 0.1799 0.1831 0.1511 0.0089  -0.0019 -0.0061 41  VAL   B CA  
4448 C C   . VAL   B 41  ? 0.1745 0.1851 0.1467 0.0170  -0.0108 -0.0189 41  VAL   B C   
4449 O O   . VAL   B 41  ? 0.1734 0.1808 0.1643 0.0116  -0.0144 -0.0197 41  VAL   B O   
4450 C CB  . VAL   B 41  ? 0.1921 0.1959 0.1704 -0.0050 0.0175  -0.0158 41  VAL   B CB  
4451 C CG1 . VAL   B 41  ? 0.1923 0.1951 0.1776 -0.0150 0.0196  -0.0157 41  VAL   B CG1 
4452 C CG2 . VAL   B 41  ? 0.2031 0.2188 0.1871 -0.0116 0.0155  -0.0191 41  VAL   B CG2 
4462 N N   . TYR   B 42  ? 0.1803 0.1829 0.1527 0.0135  -0.0158 0.0016  42  TYR   B N   
4463 C CA  . TYR   B 42  ? 0.1888 0.1879 0.1599 0.0142  -0.0235 -0.0112 42  TYR   B CA  
4464 C C   . TYR   B 42  ? 0.1714 0.1657 0.1601 0.0151  -0.0226 -0.0154 42  TYR   B C   
4465 O O   . TYR   B 42  ? 0.1678 0.1754 0.1980 0.0095  -0.0290 -0.0202 42  TYR   B O   
4466 C CB  . TYR   B 42  ? 0.2153 0.2156 0.1676 0.0123  -0.0371 0.0038  42  TYR   B CB  
4467 C CG  . TYR   B 42  ? 0.2274 0.2444 0.1670 0.0061  -0.0315 0.0174  42  TYR   B CG  
4468 C CD1 . TYR   B 42  ? 0.2274 0.2455 0.1459 0.0072  -0.0181 0.0089  42  TYR   B CD1 
4469 C CD2 . TYR   B 42  ? 0.2428 0.2621 0.2046 0.0027  -0.0186 0.0221  42  TYR   B CD2 
4470 C CE1 . TYR   B 42  ? 0.2422 0.2651 0.1595 0.0110  -0.0114 0.0077  42  TYR   B CE1 
4471 C CE2 . TYR   B 42  ? 0.2516 0.2729 0.2002 0.0059  0.0111  0.0376  42  TYR   B CE2 
4472 C CZ  . TYR   B 42  ? 0.2625 0.2830 0.1970 0.0228  0.0140  0.0194  42  TYR   B CZ  
4473 O OH  . TYR   B 42  ? 0.2967 0.3091 0.2452 0.0356  0.0270  0.0351  42  TYR   B OH  
4483 N N   . LEU   B 43  ? 0.1585 0.1496 0.1492 0.0106  -0.0166 -0.0154 43  LEU   B N   
4484 C CA  . LEU   B 43  ? 0.1568 0.1571 0.1327 0.0041  -0.0125 0.0001  43  LEU   B CA  
4485 C C   . LEU   B 43  ? 0.1628 0.1558 0.1452 0.0003  -0.0162 0.0021  43  LEU   B C   
4486 O O   . LEU   B 43  ? 0.1583 0.1609 0.1800 0.0009  -0.0183 0.0093  43  LEU   B O   
4487 C CB  . LEU   B 43  ? 0.1537 0.1470 0.1562 -0.0047 -0.0193 -0.0038 43  LEU   B CB  
4488 C CG  . LEU   B 43  ? 0.1588 0.1484 0.1650 -0.0040 -0.0202 -0.0062 43  LEU   B CG  
4489 C CD1 . LEU   B 43  ? 0.1675 0.1564 0.1890 -0.0023 -0.0325 -0.0080 43  LEU   B CD1 
4490 C CD2 . LEU   B 43  ? 0.1577 0.1431 0.1777 -0.0101 -0.0167 -0.0027 43  LEU   B CD2 
4502 N N   . LYS   B 44  ? 0.1654 0.1487 0.1572 0.0050  -0.0100 -0.0029 44  LYS   B N   
4503 C CA  . LYS   B 44  ? 0.1704 0.1634 0.1543 0.0090  -0.0174 0.0094  44  LYS   B CA  
4504 C C   . LYS   B 44  ? 0.1601 0.1584 0.1604 0.0055  -0.0216 0.0045  44  LYS   B C   
4505 O O   . LYS   B 44  ? 0.1855 0.1548 0.1849 0.0011  -0.0089 0.0050  44  LYS   B O   
4506 C CB  . LYS   B 44  ? 0.1931 0.1834 0.1753 0.0202  -0.0254 0.0076  44  LYS   B CB  
4507 C CG  . LYS   B 44  ? 0.2315 0.2153 0.2076 0.0113  -0.0501 0.0072  44  LYS   B CG  
4508 C CD  . LYS   B 44  ? 0.2688 0.2387 0.2618 -0.0069 -0.0621 0.0013  44  LYS   B CD  
4509 C CE  . LYS   B 44  ? 0.3002 0.2652 0.3105 -0.0153 -0.0624 0.0071  44  LYS   B CE  
4510 N NZ  . LYS   B 44  ? 0.3090 0.2793 0.3436 -0.0151 -0.0715 0.0192  44  LYS   B NZ  
4524 N N   . HIS   B 45  ? 0.1560 0.1564 0.1481 0.0005  -0.0097 0.0116  45  HIS   B N   
4525 C CA  . HIS   B 45  ? 0.1616 0.1535 0.1567 0.0063  -0.0150 -0.0007 45  HIS   B CA  
4526 C C   . HIS   B 45  ? 0.1868 0.1744 0.1905 0.0156  -0.0197 -0.0015 45  HIS   B C   
4527 O O   . HIS   B 45  ? 0.2043 0.2032 0.2408 0.0410  0.0178  0.0018  45  HIS   B O   
4528 C CB  . HIS   B 45  ? 0.1530 0.1570 0.1509 -0.0033 -0.0105 -0.0081 45  HIS   B CB  
4529 C CG  . HIS   B 45  ? 0.1529 0.1522 0.1559 -0.0046 -0.0080 0.0019  45  HIS   B CG  
4530 N ND1 . HIS   B 45  ? 0.1586 0.1432 0.1691 -0.0027 -0.0176 -0.0011 45  HIS   B ND1 
4531 C CD2 . HIS   B 45  ? 0.1648 0.1550 0.1707 -0.0114 -0.0172 0.0023  45  HIS   B CD2 
4532 C CE1 . HIS   B 45  ? 0.1669 0.1326 0.1521 -0.0036 -0.0322 -0.0052 45  HIS   B CE1 
4533 N NE2 . HIS   B 45  ? 0.1762 0.1453 0.1629 -0.0016 -0.0224 -0.0063 45  HIS   B NE2 
4541 N N   A GLY   B 46  ? 0.1984 0.1740 0.2150 0.0211  -0.0459 0.0152  46  GLY   B N   
4542 N N   B GLY   B 46  ? 0.1981 0.1839 0.2097 0.0174  -0.0322 0.0110  46  GLY   B N   
4543 C CA  A GLY   B 46  ? 0.2147 0.1920 0.2561 0.0169  -0.0497 0.0186  46  GLY   B CA  
4544 C CA  B GLY   B 46  ? 0.2105 0.1993 0.2349 0.0146  -0.0363 0.0185  46  GLY   B CA  
4545 C C   A GLY   B 46  ? 0.2170 0.2114 0.3064 0.0232  -0.0486 0.0131  46  GLY   B C   
4546 C C   B GLY   B 46  ? 0.2160 0.2150 0.2674 0.0165  -0.0373 0.0218  46  GLY   B C   
4547 O O   A GLY   B 46  ? 0.2294 0.2216 0.3891 0.0255  -0.0268 -0.0170 46  GLY   B O   
4548 O O   B GLY   B 46  ? 0.2246 0.2240 0.2879 0.0185  -0.0296 0.0278  46  GLY   B O   
4555 N N   . GLY   B 47  ? 0.2154 0.2194 0.2801 0.0051  -0.0286 0.0080  47  GLY   B N   
4556 C CA  . GLY   B 47  ? 0.2050 0.1860 0.2333 0.0037  -0.0231 0.0142  47  GLY   B CA  
4557 C C   . GLY   B 47  ? 0.1834 0.1612 0.1909 0.0036  -0.0072 0.0105  47  GLY   B C   
4558 O O   . GLY   B 47  ? 0.1931 0.1479 0.2037 0.0035  -0.0083 0.0179  47  GLY   B O   
4563 N N   . GLY   B 48  ? 0.1560 0.1484 0.1922 0.0069  -0.0156 0.0150  48  GLY   B N   
4564 C CA  . GLY   B 48  ? 0.1491 0.1527 0.1862 0.0010  -0.0056 0.0121  48  GLY   B CA  
4565 C C   . GLY   B 48  ? 0.1422 0.1464 0.1704 0.0058  0.0045  0.0072  48  GLY   B C   
4566 O O   . GLY   B 48  ? 0.1428 0.1435 0.2033 0.0114  -0.0079 0.0060  48  GLY   B O   
4570 N N   . VAL   B 49  ? 0.1500 0.1465 0.1730 0.0125  0.0011  0.0107  49  VAL   B N   
4571 C CA  . VAL   B 49  ? 0.1523 0.1527 0.1542 0.0097  -0.0136 -0.0051 49  VAL   B CA  
4572 C C   . VAL   B 49  ? 0.1413 0.1489 0.1504 0.0085  -0.0105 0.0003  49  VAL   B C   
4573 O O   . VAL   B 49  ? 0.1467 0.1465 0.1721 0.0071  -0.0061 0.0034  49  VAL   B O   
4574 C CB  . VAL   B 49  ? 0.1520 0.1698 0.1916 0.0012  -0.0274 -0.0045 49  VAL   B CB  
4575 C CG1 . VAL   B 49  ? 0.1495 0.1807 0.1839 0.0076  -0.0391 0.0040  49  VAL   B CG1 
4576 C CG2 . VAL   B 49  ? 0.1675 0.1885 0.2253 -0.0064 -0.0375 0.0012  49  VAL   B CG2 
4586 N N   . ALA   B 50  ? 0.1409 0.1392 0.1479 0.0013  -0.0054 0.0106  50  ALA   B N   
4587 C CA  . ALA   B 50  ? 0.1358 0.1326 0.1496 0.0060  -0.0057 0.0111  50  ALA   B CA  
4588 C C   . ALA   B 50  ? 0.1433 0.1373 0.1547 0.0028  -0.0051 0.0120  50  ALA   B C   
4589 O O   . ALA   B 50  ? 0.1392 0.1409 0.1661 0.0042  -0.0050 0.0032  50  ALA   B O   
4590 C CB  . ALA   B 50  ? 0.1420 0.1422 0.1687 0.0050  -0.0041 0.0161  50  ALA   B CB  
4596 N N   . GLY   B 51  ? 0.1441 0.1432 0.1675 0.0070  -0.0122 0.0131  51  GLY   B N   
4597 C CA  . GLY   B 51  ? 0.1437 0.1528 0.1830 0.0134  -0.0125 0.0141  51  GLY   B CA  
4598 C C   . GLY   B 51  ? 0.1410 0.1449 0.1826 0.0204  -0.0120 0.0156  51  GLY   B C   
4599 O O   . GLY   B 51  ? 0.1449 0.1579 0.2161 0.0069  -0.0120 0.0027  51  GLY   B O   
4603 N N   . ALA   B 52  ? 0.1446 0.1380 0.1785 0.0175  -0.0110 0.0076  52  ALA   B N   
4604 C CA  . ALA   B 52  ? 0.1495 0.1511 0.1847 0.0166  0.0017  -0.0006 52  ALA   B CA  
4605 C C   . ALA   B 52  ? 0.1394 0.1520 0.1712 0.0123  0.0026  0.0010  52  ALA   B C   
4606 O O   . ALA   B 52  ? 0.1456 0.1577 0.1927 0.0090  -0.0039 0.0082  52  ALA   B O   
4607 C CB  . ALA   B 52  ? 0.1683 0.1533 0.1834 0.0134  0.0055  -0.0040 52  ALA   B CB  
4613 N N   . LEU   B 53  ? 0.1335 0.1482 0.1624 0.0192  -0.0002 0.0061  53  LEU   B N   
4614 C CA  . LEU   B 53  ? 0.1346 0.1608 0.1478 0.0108  -0.0056 0.0039  53  LEU   B CA  
4615 C C   . LEU   B 53  ? 0.1431 0.1492 0.1482 0.0078  -0.0044 0.0090  53  LEU   B C   
4616 O O   . LEU   B 53  ? 0.1529 0.1557 0.1645 -0.0009 0.0044  0.0184  53  LEU   B O   
4617 C CB  . LEU   B 53  ? 0.1364 0.1683 0.1719 0.0084  -0.0087 0.0166  53  LEU   B CB  
4618 C CG  . LEU   B 53  ? 0.1289 0.1754 0.1725 0.0006  -0.0069 0.0189  53  LEU   B CG  
4619 C CD1 . LEU   B 53  ? 0.1445 0.1965 0.2060 0.0150  -0.0065 0.0059  53  LEU   B CD1 
4620 C CD2 . LEU   B 53  ? 0.1447 0.2020 0.1997 -0.0046 -0.0148 -0.0091 53  LEU   B CD2 
4632 N N   . ASN   B 54  ? 0.1480 0.1352 0.1450 -0.0026 -0.0015 0.0087  54  ASN   B N   
4633 C CA  . ASN   B 54  ? 0.1464 0.1507 0.1525 -0.0020 -0.0116 -0.0020 54  ASN   B CA  
4634 C C   . ASN   B 54  ? 0.1443 0.1526 0.1871 0.0002  -0.0031 0.0031  54  ASN   B C   
4635 O O   . ASN   B 54  ? 0.1374 0.1574 0.1970 -0.0014 -0.0033 0.0029  54  ASN   B O   
4636 C CB  . ASN   B 54  ? 0.1500 0.1651 0.1803 0.0028  -0.0111 0.0009  54  ASN   B CB  
4637 C CG  . ASN   B 54  ? 0.1435 0.1715 0.1790 0.0077  -0.0108 -0.0016 54  ASN   B CG  
4638 O OD1 . ASN   B 54  ? 0.1418 0.1718 0.1908 0.0029  -0.0119 -0.0116 54  ASN   B OD1 
4639 N ND2 . ASN   B 54  ? 0.1606 0.1870 0.2044 0.0024  -0.0341 0.0161  54  ASN   B ND2 
4646 N N   . LYS   B 55  ? 0.1363 0.1573 0.1979 0.0102  -0.0006 0.0051  55  LYS   B N   
4647 C CA  . LYS   B 55  ? 0.1447 0.1755 0.2174 0.0186  -0.0034 0.0040  55  LYS   B CA  
4648 C C   . LYS   B 55  ? 0.1384 0.1725 0.2208 0.0126  0.0068  -0.0026 55  LYS   B C   
4649 O O   . LYS   B 55  ? 0.1350 0.1909 0.2333 0.0111  0.0068  -0.0011 55  LYS   B O   
4650 C CB  . LYS   B 55  ? 0.1623 0.1906 0.2501 0.0211  0.0118  0.0094  55  LYS   B CB  
4651 C CG  . LYS   B 55  ? 0.2040 0.2183 0.3332 0.0273  0.0222  0.0230  55  LYS   B CG  
4652 C CD  . LYS   B 55  ? 0.2451 0.2460 0.3971 0.0413  0.0450  0.0274  55  LYS   B CD  
4653 C CE  . LYS   B 55  ? 0.2708 0.2657 0.4578 0.0487  0.0605  0.0313  55  LYS   B CE  
4654 N NZ  . LYS   B 55  ? 0.2798 0.2800 0.4891 0.0493  0.0446  0.0401  55  LYS   B NZ  
4668 N N   . ALA   B 56  ? 0.1384 0.1742 0.1939 0.0110  0.0020  -0.0077 56  ALA   B N   
4669 C CA  . ALA   B 56  ? 0.1572 0.1941 0.1972 0.0023  0.0030  -0.0018 56  ALA   B CA  
4670 C C   . ALA   B 56  ? 0.1575 0.1867 0.1890 0.0040  0.0176  0.0027  56  ALA   B C   
4671 O O   . ALA   B 56  ? 0.1718 0.1969 0.2073 0.0085  0.0301  0.0043  56  ALA   B O   
4672 C CB  . ALA   B 56  ? 0.1701 0.2193 0.1960 -0.0162 -0.0104 -0.0120 56  ALA   B CB  
4678 N N   . THR   B 57  ? 0.1448 0.1750 0.1965 0.0060  0.0171  0.0095  57  THR   B N   
4679 C CA  . THR   B 57  ? 0.1543 0.1721 0.1981 -0.0038 0.0283  0.0137  57  THR   B CA  
4680 C C   . THR   B 57  ? 0.1546 0.1845 0.2129 -0.0005 0.0235  0.0109  57  THR   B C   
4681 O O   . THR   B 57  ? 0.1610 0.1877 0.2154 -0.0137 0.0054  0.0080  57  THR   B O   
4682 C CB  . THR   B 57  ? 0.1661 0.1636 0.1776 -0.0040 0.0181  0.0135  57  THR   B CB  
4683 O OG1 . THR   B 57  ? 0.1599 0.1557 0.1995 -0.0053 0.0140  0.0040  57  THR   B OG1 
4684 C CG2 . THR   B 57  ? 0.1571 0.1656 0.1764 -0.0037 0.0163  -0.0001 57  THR   B CG2 
4692 N N   . ASN   B 58  ? 0.1406 0.2023 0.2379 -0.0142 0.0034  -0.0089 58  ASN   B N   
4693 C CA  . ASN   B 58  ? 0.1634 0.2501 0.2719 -0.0269 0.0332  -0.0010 58  ASN   B CA  
4694 C C   . ASN   B 58  ? 0.1445 0.2278 0.2282 -0.0152 -0.0041 0.0058  58  ASN   B C   
4695 O O   . ASN   B 58  ? 0.1512 0.2380 0.2441 -0.0163 -0.0086 -0.0058 58  ASN   B O   
4696 C CB  . ASN   B 58  ? 0.2523 0.3264 0.3832 -0.0381 0.0687  0.0011  58  ASN   B CB  
4697 C CG  . ASN   B 58  ? 0.3548 0.3921 0.5258 -0.0389 0.0871  0.0216  58  ASN   B CG  
4698 O OD1 . ASN   B 58  ? 0.3829 0.4129 0.5847 -0.0379 0.0917  0.0301  58  ASN   B OD1 
4699 N ND2 . ASN   B 58  ? 0.4389 0.4389 0.5692 -0.0416 0.0942  0.0256  58  ASN   B ND2 
4706 N N   . ASN   B 59  ? 0.1443 0.2102 0.2017 -0.0082 -0.0059 0.0139  59  ASN   B N   
4707 C CA  . ASN   B 59  ? 0.1457 0.2107 0.1986 -0.0116 -0.0192 0.0224  59  ASN   B CA  
4708 C C   . ASN   B 59  ? 0.1425 0.1977 0.1937 -0.0157 -0.0198 0.0101  59  ASN   B C   
4709 O O   . ASN   B 59  ? 0.1500 0.2045 0.1900 -0.0174 -0.0105 0.0163  59  ASN   B O   
4710 C CB  . ASN   B 59  ? 0.1566 0.2321 0.2067 -0.0083 -0.0331 0.0192  59  ASN   B CB  
4711 C CG  . ASN   B 59  ? 0.1663 0.2534 0.2330 -0.0048 -0.0403 0.0151  59  ASN   B CG  
4712 O OD1 . ASN   B 59  ? 0.1687 0.2555 0.2310 -0.0032 -0.0266 0.0326  59  ASN   B OD1 
4713 N ND2 . ASN   B 59  ? 0.1732 0.2632 0.2434 -0.0175 -0.0452 0.0105  59  ASN   B ND2 
4720 N N   . ALA   B 60  ? 0.1446 0.1860 0.2028 -0.0143 -0.0028 0.0061  60  ALA   B N   
4721 C CA  . ALA   B 60  ? 0.1548 0.1737 0.1998 -0.0195 -0.0054 0.0081  60  ALA   B CA  
4722 C C   . ALA   B 60  ? 0.1528 0.1591 0.1844 -0.0093 -0.0038 0.0139  60  ALA   B C   
4723 O O   . ALA   B 60  ? 0.1548 0.1630 0.2040 -0.0175 -0.0002 0.0011  60  ALA   B O   
4724 C CB  . ALA   B 60  ? 0.1729 0.1757 0.2324 -0.0238 0.0073  0.0146  60  ALA   B CB  
4730 N N   . MET   B 61  ? 0.1412 0.1513 0.1876 -0.0072 0.0006  0.0109  61  MET   B N   
4731 C CA  . MET   B 61  ? 0.1384 0.1500 0.1730 -0.0050 -0.0118 0.0024  61  MET   B CA  
4732 C C   . MET   B 61  ? 0.1465 0.1462 0.1705 -0.0118 -0.0149 0.0069  61  MET   B C   
4733 O O   . MET   B 61  ? 0.1494 0.1467 0.1634 -0.0028 -0.0100 -0.0059 61  MET   B O   
4734 C CB  . MET   B 61  ? 0.1385 0.1540 0.1748 0.0010  -0.0101 0.0011  61  MET   B CB  
4735 C CG  . MET   B 61  ? 0.1381 0.1537 0.1719 -0.0005 -0.0128 0.0059  61  MET   B CG  
4736 S SD  . MET   B 61  ? 0.1413 0.1544 0.1890 -0.0049 -0.0074 -0.0066 61  MET   B SD  
4737 C CE  . MET   B 61  ? 0.1477 0.1717 0.2041 -0.0042 -0.0040 -0.0148 61  MET   B CE  
4747 N N   . GLN   B 62  ? 0.1453 0.1498 0.1736 -0.0094 -0.0223 0.0083  62  GLN   B N   
4748 C CA  . GLN   B 62  ? 0.1517 0.1561 0.1770 -0.0024 -0.0226 -0.0011 62  GLN   B CA  
4749 C C   . GLN   B 62  ? 0.1503 0.1646 0.1760 -0.0071 -0.0250 -0.0021 62  GLN   B C   
4750 O O   . GLN   B 62  ? 0.1641 0.1625 0.1838 -0.0070 -0.0337 -0.0095 62  GLN   B O   
4751 C CB  . GLN   B 62  ? 0.1545 0.1639 0.1794 -0.0029 -0.0189 0.0045  62  GLN   B CB  
4752 C CG  . GLN   B 62  ? 0.1558 0.1710 0.1875 0.0014  -0.0301 0.0011  62  GLN   B CG  
4753 C CD  . GLN   B 62  ? 0.1607 0.1646 0.1771 0.0096  -0.0304 0.0026  62  GLN   B CD  
4754 O OE1 . GLN   B 62  ? 0.1630 0.1602 0.1835 0.0015  -0.0304 -0.0094 62  GLN   B OE1 
4755 N NE2 . GLN   B 62  ? 0.1635 0.1695 0.1826 0.0026  -0.0250 -0.0093 62  GLN   B NE2 
4764 N N   . VAL   B 63  ? 0.1411 0.1685 0.1946 -0.0094 -0.0263 -0.0111 63  VAL   B N   
4765 C CA  . VAL   B 63  ? 0.1577 0.1729 0.2097 -0.0137 -0.0328 -0.0046 63  VAL   B CA  
4766 C C   . VAL   B 63  ? 0.1611 0.1572 0.1957 -0.0214 -0.0290 -0.0100 63  VAL   B C   
4767 O O   . VAL   B 63  ? 0.1797 0.1582 0.2119 -0.0159 -0.0408 -0.0100 63  VAL   B O   
4768 C CB  . VAL   B 63  ? 0.1637 0.1869 0.2491 -0.0199 -0.0328 -0.0081 63  VAL   B CB  
4769 C CG1 . VAL   B 63  ? 0.1730 0.1939 0.2613 -0.0324 -0.0272 -0.0073 63  VAL   B CG1 
4770 C CG2 . VAL   B 63  ? 0.1566 0.2078 0.2636 -0.0132 -0.0326 -0.0104 63  VAL   B CG2 
4780 N N   . GLU   B 64  ? 0.1574 0.1519 0.1929 -0.0161 -0.0283 -0.0054 64  GLU   B N   
4781 C CA  . GLU   B 64  ? 0.1578 0.1468 0.1859 -0.0119 -0.0342 -0.0040 64  GLU   B CA  
4782 C C   . GLU   B 64  ? 0.1542 0.1406 0.1752 -0.0052 -0.0283 -0.0186 64  GLU   B C   
4783 O O   . GLU   B 64  ? 0.1654 0.1510 0.1939 -0.0166 -0.0296 -0.0131 64  GLU   B O   
4784 C CB  . GLU   B 64  ? 0.1531 0.1589 0.1877 -0.0124 -0.0281 0.0059  64  GLU   B CB  
4785 C CG  . GLU   B 64  ? 0.1661 0.1582 0.1765 -0.0266 -0.0244 -0.0036 64  GLU   B CG  
4786 C CD  . GLU   B 64  ? 0.1732 0.1741 0.1838 -0.0333 -0.0282 -0.0118 64  GLU   B CD  
4787 O OE1 . GLU   B 64  ? 0.1783 0.1910 0.2029 -0.0384 -0.0175 -0.0301 64  GLU   B OE1 
4788 O OE2 . GLU   B 64  ? 0.1869 0.1898 0.1916 -0.0343 -0.0479 -0.0049 64  GLU   B OE2 
4795 N N   . SER   B 65  ? 0.1572 0.1400 0.1656 -0.0070 -0.0157 -0.0113 65  SER   B N   
4796 C CA  . SER   B 65  ? 0.1609 0.1403 0.1676 -0.0015 -0.0136 -0.0098 65  SER   B CA  
4797 C C   . SER   B 65  ? 0.1597 0.1462 0.1765 -0.0022 -0.0202 -0.0110 65  SER   B C   
4798 O O   . SER   B 65  ? 0.1619 0.1529 0.1799 -0.0020 -0.0237 -0.0179 65  SER   B O   
4799 C CB  . SER   B 65  ? 0.1623 0.1434 0.1707 -0.0083 -0.0142 -0.0076 65  SER   B CB  
4800 O OG  . SER   B 65  ? 0.1613 0.1461 0.1774 -0.0076 -0.0174 -0.0201 65  SER   B OG  
4806 N N   . ASP   B 66  ? 0.1648 0.1514 0.1683 -0.0039 -0.0276 -0.0186 66  ASP   B N   
4807 C CA  . ASP   B 66  ? 0.1726 0.1638 0.1615 0.0015  -0.0285 -0.0127 66  ASP   B CA  
4808 C C   . ASP   B 66  ? 0.1772 0.1691 0.1660 -0.0115 -0.0242 -0.0192 66  ASP   B C   
4809 O O   . ASP   B 66  ? 0.1825 0.1717 0.1790 0.0013  -0.0302 -0.0192 66  ASP   B O   
4810 C CB  . ASP   B 66  ? 0.1876 0.1743 0.1967 0.0106  -0.0433 -0.0107 66  ASP   B CB  
4811 C CG  . ASP   B 66  ? 0.2167 0.1892 0.2188 0.0166  -0.0532 0.0010  66  ASP   B CG  
4812 O OD1 . ASP   B 66  ? 0.2431 0.1867 0.2219 0.0084  -0.0537 0.0070  66  ASP   B OD1 
4813 O OD2 . ASP   B 66  ? 0.2377 0.2181 0.2760 0.0366  -0.0505 -0.0026 66  ASP   B OD2 
4818 N N   . ASP   B 67  ? 0.1710 0.1595 0.1733 -0.0145 -0.0279 -0.0227 67  ASP   B N   
4819 C CA  . ASP   B 67  ? 0.1887 0.1549 0.1821 -0.0171 -0.0303 -0.0163 67  ASP   B CA  
4820 C C   . ASP   B 67  ? 0.1837 0.1568 0.1892 -0.0033 -0.0290 -0.0189 67  ASP   B C   
4821 O O   . ASP   B 67  ? 0.1875 0.1612 0.1977 -0.0045 -0.0147 -0.0284 67  ASP   B O   
4822 C CB  . ASP   B 67  ? 0.2096 0.1643 0.2048 -0.0237 -0.0413 -0.0024 67  ASP   B CB  
4823 C CG  . ASP   B 67  ? 0.2536 0.1725 0.2181 -0.0117 -0.0659 -0.0118 67  ASP   B CG  
4824 O OD1 . ASP   B 67  ? 0.2787 0.1879 0.2305 -0.0109 -0.0628 -0.0148 67  ASP   B OD1 
4825 O OD2 . ASP   B 67  ? 0.2702 0.1785 0.2455 0.0098  -0.0719 -0.0130 67  ASP   B OD2 
4830 N N   . TYR   B 68  ? 0.1800 0.1575 0.1851 0.0032  -0.0458 -0.0337 68  TYR   B N   
4831 C CA  . TYR   B 68  ? 0.1759 0.1723 0.1949 0.0077  -0.0421 -0.0340 68  TYR   B CA  
4832 C C   . TYR   B 68  ? 0.1692 0.1684 0.1834 0.0023  -0.0328 -0.0370 68  TYR   B C   
4833 O O   . TYR   B 68  ? 0.1773 0.1751 0.1997 0.0051  -0.0310 -0.0544 68  TYR   B O   
4834 C CB  . TYR   B 68  ? 0.1800 0.1937 0.1995 0.0078  -0.0570 -0.0426 68  TYR   B CB  
4835 C CG  . TYR   B 68  ? 0.1932 0.2128 0.2212 0.0114  -0.0430 -0.0632 68  TYR   B CG  
4836 C CD1 . TYR   B 68  ? 0.1942 0.2139 0.2362 -0.0071 -0.0398 -0.0806 68  TYR   B CD1 
4837 C CD2 . TYR   B 68  ? 0.1972 0.2338 0.2376 0.0197  -0.0542 -0.0648 68  TYR   B CD2 
4838 C CE1 . TYR   B 68  ? 0.2011 0.2350 0.2556 -0.0006 -0.0376 -0.0825 68  TYR   B CE1 
4839 C CE2 . TYR   B 68  ? 0.1960 0.2379 0.2508 0.0187  -0.0484 -0.0739 68  TYR   B CE2 
4840 C CZ  . TYR   B 68  ? 0.1924 0.2418 0.2539 0.0051  -0.0459 -0.0834 68  TYR   B CZ  
4841 O OH  . TYR   B 68  ? 0.1879 0.2618 0.2921 -0.0028 -0.0338 -0.0546 68  TYR   B OH  
4851 N N   . ILE   B 69  ? 0.1672 0.1592 0.1900 0.0003  -0.0363 -0.0308 69  ILE   B N   
4852 C CA  . ILE   B 69  ? 0.1791 0.1629 0.1932 -0.0066 -0.0194 -0.0341 69  ILE   B CA  
4853 C C   . ILE   B 69  ? 0.1788 0.1664 0.1942 0.0010  -0.0332 -0.0247 69  ILE   B C   
4854 O O   . ILE   B 69  ? 0.1828 0.1762 0.1875 0.0023  -0.0242 -0.0251 69  ILE   B O   
4855 C CB  . ILE   B 69  ? 0.1891 0.1733 0.2215 -0.0084 0.0075  -0.0240 69  ILE   B CB  
4856 C CG1 . ILE   B 69  ? 0.1925 0.1774 0.2263 -0.0123 0.0189  -0.0335 69  ILE   B CG1 
4857 C CG2 . ILE   B 69  ? 0.2074 0.1843 0.2363 -0.0119 0.0051  -0.0203 69  ILE   B CG2 
4858 C CD1 . ILE   B 69  ? 0.1860 0.1822 0.2460 -0.0233 0.0250  -0.0383 69  ILE   B CD1 
4870 N N   . ALA   B 70  ? 0.1696 0.1636 0.2021 0.0036  -0.0420 -0.0283 70  ALA   B N   
4871 C CA  . ALA   B 70  ? 0.1761 0.1693 0.1860 0.0061  -0.0416 -0.0267 70  ALA   B CA  
4872 C C   . ALA   B 70  ? 0.1838 0.1683 0.1925 0.0008  -0.0466 -0.0348 70  ALA   B C   
4873 O O   . ALA   B 70  ? 0.2018 0.1703 0.1874 0.0071  -0.0473 -0.0354 70  ALA   B O   
4874 C CB  . ALA   B 70  ? 0.1818 0.1834 0.1983 -0.0022 -0.0513 -0.0217 70  ALA   B CB  
4880 N N   . THR   B 71  ? 0.1932 0.1680 0.1965 -0.0003 -0.0585 -0.0419 71  THR   B N   
4881 C CA  . THR   B 71  ? 0.2067 0.1721 0.2193 0.0071  -0.0627 -0.0406 71  THR   B CA  
4882 C C   . THR   B 71  ? 0.2010 0.1718 0.2483 0.0288  -0.0594 -0.0537 71  THR   B C   
4883 O O   . THR   B 71  ? 0.2059 0.1771 0.2808 0.0266  -0.0581 -0.0648 71  THR   B O   
4884 C CB  . THR   B 71  ? 0.2301 0.1964 0.2465 0.0000  -0.0697 -0.0140 71  THR   B CB  
4885 O OG1 . THR   B 71  ? 0.2448 0.2235 0.2772 -0.0222 -0.0692 0.0018  71  THR   B OG1 
4886 C CG2 . THR   B 71  ? 0.2484 0.1921 0.2707 0.0052  -0.0561 0.0075  71  THR   B CG2 
4894 N N   . ASN   B 72  ? 0.1891 0.1769 0.2422 0.0168  -0.0615 -0.0731 72  ASN   B N   
4895 C CA  . ASN   B 72  ? 0.1898 0.1885 0.2358 0.0150  -0.0465 -0.0767 72  ASN   B CA  
4896 C C   . ASN   B 72  ? 0.1904 0.1982 0.2437 -0.0000 -0.0225 -0.0701 72  ASN   B C   
4897 O O   . ASN   B 72  ? 0.1915 0.2166 0.2747 0.0028  -0.0013 -0.0752 72  ASN   B O   
4898 C CB  . ASN   B 72  ? 0.1997 0.2037 0.2502 0.0139  -0.0575 -0.0580 72  ASN   B CB  
4899 C CG  . ASN   B 72  ? 0.2160 0.2164 0.2535 0.0282  -0.0535 -0.0318 72  ASN   B CG  
4900 O OD1 . ASN   B 72  ? 0.2416 0.2340 0.2476 0.0106  -0.0375 -0.0423 72  ASN   B OD1 
4901 N ND2 . ASN   B 72  ? 0.2299 0.2203 0.2762 0.0440  -0.0397 0.0016  72  ASN   B ND2 
4908 N N   . GLY   B 73  ? 0.1943 0.1954 0.2120 -0.0025 -0.0326 -0.0643 73  GLY   B N   
4909 C CA  . GLY   B 73  ? 0.1881 0.2065 0.1852 -0.0026 -0.0252 -0.0460 73  GLY   B CA  
4910 C C   . GLY   B 73  ? 0.1822 0.2055 0.1368 0.0002  -0.0273 -0.0407 73  GLY   B C   
4911 O O   . GLY   B 73  ? 0.1817 0.1922 0.1533 0.0029  -0.0225 -0.0329 73  GLY   B O   
4915 N N   . PRO   B 74  ? 0.1879 0.2147 0.1440 0.0022  -0.0237 -0.0359 74  PRO   B N   
4916 C CA  . PRO   B 74  ? 0.1781 0.2144 0.1244 0.0112  -0.0221 -0.0278 74  PRO   B CA  
4917 C C   . PRO   B 74  ? 0.1603 0.1968 0.1400 0.0086  -0.0180 -0.0153 74  PRO   B C   
4918 O O   . PRO   B 74  ? 0.1633 0.1997 0.1912 0.0037  -0.0108 -0.0247 74  PRO   B O   
4919 C CB  . PRO   B 74  ? 0.1933 0.2330 0.1381 0.0037  -0.0248 -0.0223 74  PRO   B CB  
4920 C CG  . PRO   B 74  ? 0.2184 0.2415 0.1871 0.0031  -0.0204 -0.0194 74  PRO   B CG  
4921 C CD  . PRO   B 74  ? 0.2138 0.2307 0.1706 0.0028  -0.0143 -0.0342 74  PRO   B CD  
4929 N N   . LEU   B 75  ? 0.1566 0.1858 0.1440 0.0059  -0.0269 -0.0227 75  LEU   B N   
4930 C CA  . LEU   B 75  ? 0.1589 0.1849 0.1361 0.0053  -0.0172 -0.0028 75  LEU   B CA  
4931 C C   . LEU   B 75  ? 0.1647 0.1947 0.1407 0.0063  -0.0076 0.0015  75  LEU   B C   
4932 O O   . LEU   B 75  ? 0.1811 0.2086 0.1495 0.0005  -0.0074 0.0022  75  LEU   B O   
4933 C CB  . LEU   B 75  ? 0.1672 0.1912 0.1219 -0.0058 -0.0193 0.0050  75  LEU   B CB  
4934 C CG  . LEU   B 75  ? 0.2048 0.2096 0.1571 -0.0330 -0.0098 0.0007  75  LEU   B CG  
4935 C CD1 . LEU   B 75  ? 0.2405 0.2284 0.1525 -0.0450 0.0166  -0.0074 75  LEU   B CD1 
4936 C CD2 . LEU   B 75  ? 0.2409 0.2305 0.2304 -0.0213 0.0000  0.0109  75  LEU   B CD2 
4948 N N   . LYS   B 76  ? 0.1655 0.2218 0.1688 0.0001  -0.0046 0.0032  76  LYS   B N   
4949 C CA  . LYS   B 76  ? 0.1776 0.2265 0.1973 -0.0018 0.0184  -0.0027 76  LYS   B CA  
4950 C C   . LYS   B 76  ? 0.1733 0.2062 0.1663 0.0047  0.0000  0.0192  76  LYS   B C   
4951 O O   . LYS   B 76  ? 0.1665 0.1887 0.1784 -0.0022 -0.0028 0.0219  76  LYS   B O   
4952 C CB  . LYS   B 76  ? 0.1950 0.2309 0.2588 -0.0088 0.0418  -0.0420 76  LYS   B CB  
4953 C CG  . LYS   B 76  ? 0.2087 0.2531 0.3097 0.0019  0.0278  -0.0408 76  LYS   B CG  
4954 C CD  . LYS   B 76  ? 0.2089 0.2653 0.3436 0.0138  0.0168  -0.0476 76  LYS   B CD  
4955 C CE  . LYS   B 76  ? 0.2194 0.2839 0.3930 0.0158  0.0014  -0.0533 76  LYS   B CE  
4956 N NZ  . LYS   B 76  ? 0.2161 0.2898 0.4116 0.0136  -0.0177 -0.0684 76  LYS   B NZ  
4970 N N   . VAL   B 77  ? 0.1850 0.2196 0.1664 0.0128  0.0068  0.0183  77  VAL   B N   
4971 C CA  . VAL   B 77  ? 0.1848 0.2106 0.1746 0.0134  0.0109  0.0404  77  VAL   B CA  
4972 C C   . VAL   B 77  ? 0.1652 0.1847 0.1741 0.0154  0.0168  0.0252  77  VAL   B C   
4973 O O   . VAL   B 77  ? 0.1680 0.1808 0.1641 0.0221  0.0232  0.0189  77  VAL   B O   
4974 C CB  . VAL   B 77  ? 0.1931 0.2167 0.2059 0.0098  0.0212  0.0540  77  VAL   B CB  
4975 C CG1 . VAL   B 77  ? 0.1959 0.2063 0.2429 0.0007  0.0247  0.0733  77  VAL   B CG1 
4976 C CG2 . VAL   B 77  ? 0.2097 0.2310 0.2250 0.0019  0.0058  0.0573  77  VAL   B CG2 
4986 N N   . GLY   B 78  ? 0.1557 0.1680 0.1749 0.0101  0.0086  0.0226  78  GLY   B N   
4987 C CA  . GLY   B 78  ? 0.1551 0.1651 0.1641 0.0087  0.0179  0.0083  78  GLY   B CA  
4988 C C   . GLY   B 78  ? 0.1568 0.1608 0.1512 0.0090  0.0219  0.0119  78  GLY   B C   
4989 O O   . GLY   B 78  ? 0.1580 0.1576 0.1780 0.0185  0.0063  0.0244  78  GLY   B O   
4993 N N   . GLY   B 79  ? 0.1482 0.1606 0.1655 0.0048  0.0090  0.0070  79  GLY   B N   
4994 C CA  . GLY   B 79  ? 0.1498 0.1510 0.1570 0.0080  0.0039  0.0078  79  GLY   B CA  
4995 C C   . GLY   B 79  ? 0.1402 0.1441 0.1604 0.0138  0.0073  0.0067  79  GLY   B C   
4996 O O   . GLY   B 79  ? 0.1474 0.1410 0.1774 0.0099  0.0098  0.0200  79  GLY   B O   
5000 N N   . SER   B 80  ? 0.1441 0.1387 0.1645 0.0074  0.0186  0.0045  80  SER   B N   
5001 C CA  . SER   B 80  ? 0.1386 0.1364 0.1645 0.0001  0.0022  0.0026  80  SER   B CA  
5002 C C   . SER   B 80  ? 0.1407 0.1318 0.1682 0.0026  -0.0122 -0.0019 80  SER   B C   
5003 O O   . SER   B 80  ? 0.1518 0.1365 0.2046 0.0101  0.0017  -0.0103 80  SER   B O   
5004 C CB  . SER   B 80  ? 0.1434 0.1402 0.1699 -0.0053 -0.0048 0.0073  80  SER   B CB  
5005 O OG  . SER   B 80  ? 0.1533 0.1549 0.1887 -0.0021 -0.0188 0.0115  80  SER   B OG  
5011 N N   . CYS   B 81  ? 0.1417 0.1218 0.1691 -0.0016 -0.0066 -0.0054 81  CYS   B N   
5012 C CA  . CYS   B 81  ? 0.1420 0.1236 0.1669 0.0032  -0.0145 0.0048  81  CYS   B CA  
5013 C C   . CYS   B 81  ? 0.1412 0.1210 0.1505 0.0012  -0.0185 0.0056  81  CYS   B C   
5014 O O   . CYS   B 81  ? 0.1611 0.1234 0.1772 0.0073  -0.0060 -0.0085 81  CYS   B O   
5015 C CB  . CYS   B 81  ? 0.1561 0.1359 0.1780 -0.0017 -0.0094 0.0025  81  CYS   B CB  
5016 S SG  . CYS   B 81  ? 0.1585 0.1599 0.1629 -0.0040 -0.0267 -0.0096 81  CYS   B SG  
5022 N N   . VAL   B 82  ? 0.1398 0.1212 0.1600 -0.0003 -0.0172 -0.0068 82  VAL   B N   
5023 C CA  . VAL   B 82  ? 0.1470 0.1281 0.1666 -0.0038 -0.0122 0.0071  82  VAL   B CA  
5024 C C   . VAL   B 82  ? 0.1561 0.1218 0.1768 -0.0037 -0.0110 -0.0028 82  VAL   B C   
5025 O O   . VAL   B 82  ? 0.1644 0.1240 0.1980 -0.0022 -0.0112 -0.0182 82  VAL   B O   
5026 C CB  . VAL   B 82  ? 0.1586 0.1473 0.1824 -0.0040 -0.0190 0.0150  82  VAL   B CB  
5027 C CG1 . VAL   B 82  ? 0.1785 0.1634 0.1994 0.0054  -0.0162 0.0159  82  VAL   B CG1 
5028 C CG2 . VAL   B 82  ? 0.1723 0.1621 0.1898 -0.0101 -0.0288 0.0191  82  VAL   B CG2 
5038 N N   . LEU   B 83  ? 0.1435 0.1230 0.1660 -0.0144 -0.0201 -0.0082 83  LEU   B N   
5039 C CA  . LEU   B 83  ? 0.1476 0.1278 0.1456 -0.0105 -0.0214 -0.0019 83  LEU   B CA  
5040 C C   . LEU   B 83  ? 0.1446 0.1250 0.1483 -0.0176 -0.0282 -0.0003 83  LEU   B C   
5041 O O   . LEU   B 83  ? 0.1509 0.1333 0.1458 -0.0172 -0.0177 0.0074  83  LEU   B O   
5042 C CB  . LEU   B 83  ? 0.1552 0.1452 0.1591 -0.0123 -0.0264 -0.0089 83  LEU   B CB  
5043 C CG  . LEU   B 83  ? 0.1724 0.1570 0.1600 -0.0166 -0.0152 -0.0047 83  LEU   B CG  
5044 C CD1 . LEU   B 83  ? 0.1851 0.1602 0.1615 -0.0170 -0.0181 -0.0055 83  LEU   B CD1 
5045 C CD2 . LEU   B 83  ? 0.1916 0.1610 0.1777 -0.0082 -0.0200 -0.0231 83  LEU   B CD2 
5057 N N   . SER   B 84  ? 0.1524 0.1387 0.1855 -0.0229 -0.0241 0.0047  84  SER   B N   
5058 C CA  . SER   B 84  ? 0.1510 0.1581 0.1675 -0.0231 -0.0144 0.0196  84  SER   B CA  
5059 C C   . SER   B 84  ? 0.1448 0.1771 0.1194 -0.0165 -0.0194 0.0242  84  SER   B C   
5060 O O   . SER   B 84  ? 0.1529 0.1569 0.1263 -0.0158 -0.0171 0.0054  84  SER   B O   
5061 C CB  . SER   B 84  ? 0.1729 0.1639 0.2268 -0.0293 0.0093  0.0107  84  SER   B CB  
5062 O OG  . SER   B 84  ? 0.1688 0.1749 0.2755 -0.0367 0.0084  0.0252  84  SER   B OG  
5068 N N   . GLY   B 85  ? 0.1474 0.1925 0.1283 -0.0210 -0.0155 0.0259  85  GLY   B N   
5069 C CA  . GLY   B 85  ? 0.1499 0.2001 0.1507 -0.0308 0.0003  -0.0085 85  GLY   B CA  
5070 C C   . GLY   B 85  ? 0.1454 0.1819 0.1409 -0.0353 -0.0019 -0.0005 85  GLY   B C   
5071 O O   . GLY   B 85  ? 0.1566 0.1792 0.1691 -0.0547 0.0111  -0.0087 85  GLY   B O   
5075 N N   . HIS   B 86  ? 0.1443 0.1593 0.1733 -0.0252 -0.0176 0.0120  86  HIS   B N   
5076 C CA  . HIS   B 86  ? 0.1485 0.1597 0.1623 -0.0312 -0.0240 0.0206  86  HIS   B CA  
5077 C C   . HIS   B 86  ? 0.1524 0.1787 0.1522 -0.0402 -0.0142 0.0422  86  HIS   B C   
5078 O O   . HIS   B 86  ? 0.1645 0.1887 0.1566 -0.0309 -0.0009 0.0310  86  HIS   B O   
5079 C CB  . HIS   B 86  ? 0.1629 0.1651 0.1624 -0.0215 -0.0254 0.0067  86  HIS   B CB  
5080 C CG  . HIS   B 86  ? 0.1614 0.1712 0.1624 -0.0137 -0.0214 0.0192  86  HIS   B CG  
5081 N ND1 . HIS   B 86  ? 0.1710 0.1965 0.1881 -0.0236 -0.0331 0.0074  86  HIS   B ND1 
5082 C CD2 . HIS   B 86  ? 0.1590 0.1685 0.1805 -0.0080 -0.0223 0.0116  86  HIS   B CD2 
5083 C CE1 . HIS   B 86  ? 0.1790 0.1941 0.1796 -0.0142 -0.0189 -0.0199 86  HIS   B CE1 
5084 N NE2 . HIS   B 86  ? 0.1730 0.1844 0.1770 -0.0025 -0.0150 -0.0042 86  HIS   B NE2 
5092 N N   . ASN   B 87  ? 0.1540 0.1821 0.1635 -0.0294 -0.0117 0.0323  87  ASN   B N   
5093 C CA  . ASN   B 87  ? 0.1632 0.2015 0.1703 -0.0281 0.0169  0.0254  87  ASN   B CA  
5094 C C   . ASN   B 87  ? 0.1795 0.1890 0.1529 -0.0311 0.0262  0.0121  87  ASN   B C   
5095 O O   . ASN   B 87  ? 0.2061 0.1931 0.1846 -0.0220 0.0455  0.0050  87  ASN   B O   
5096 C CB  . ASN   B 87  ? 0.1625 0.2375 0.2121 -0.0277 0.0204  0.0216  87  ASN   B CB  
5097 C CG  . ASN   B 87  ? 0.1662 0.2552 0.2171 0.0044  0.0306  0.0334  87  ASN   B CG  
5098 O OD1 . ASN   B 87  ? 0.1637 0.2419 0.2047 0.0083  0.0435  0.0486  87  ASN   B OD1 
5099 N ND2 . ASN   B 87  ? 0.2029 0.2701 0.2593 0.0101  0.0469  0.0240  87  ASN   B ND2 
5106 N N   . LEU   B 88  ? 0.1564 0.1741 0.1451 -0.0319 0.0111  0.0118  88  LEU   B N   
5107 C CA  . LEU   B 88  ? 0.1715 0.1684 0.1551 -0.0290 -0.0031 -0.0025 88  LEU   B CA  
5108 C C   . LEU   B 88  ? 0.1692 0.1643 0.1566 -0.0295 -0.0022 0.0018  88  LEU   B C   
5109 O O   . LEU   B 88  ? 0.1930 0.1715 0.1896 -0.0177 -0.0304 -0.0100 88  LEU   B O   
5110 C CB  . LEU   B 88  ? 0.1860 0.1739 0.1752 -0.0372 -0.0077 0.0173  88  LEU   B CB  
5111 C CG  . LEU   B 88  ? 0.2245 0.2033 0.2013 -0.0299 -0.0282 0.0414  88  LEU   B CG  
5112 C CD1 . LEU   B 88  ? 0.2382 0.2346 0.2196 -0.0447 -0.0270 0.0526  88  LEU   B CD1 
5113 C CD2 . LEU   B 88  ? 0.2591 0.2271 0.2610 0.0098  -0.0524 0.0158  88  LEU   B CD2 
5125 N N   . ALA   B 89  ? 0.1539 0.1567 0.1478 -0.0308 0.0155  0.0039  89  ALA   B N   
5126 C CA  . ALA   B 89  ? 0.1543 0.1492 0.1338 -0.0332 0.0077  0.0136  89  ALA   B CA  
5127 C C   . ALA   B 89  ? 0.1624 0.1495 0.1480 -0.0360 0.0129  0.0088  89  ALA   B C   
5128 O O   . ALA   B 89  ? 0.1467 0.1616 0.1843 -0.0385 0.0109  -0.0214 89  ALA   B O   
5129 C CB  . ALA   B 89  ? 0.1487 0.1535 0.1519 -0.0340 0.0016  0.0159  89  ALA   B CB  
5135 N N   . LYS   B 90  ? 0.2015 0.1365 0.1590 -0.0437 -0.0074 0.0154  90  LYS   B N   
5136 C CA  . LYS   B 90  ? 0.2127 0.1409 0.1522 -0.0441 -0.0100 0.0116  90  LYS   B CA  
5137 C C   . LYS   B 90  ? 0.1917 0.1364 0.1579 -0.0400 -0.0124 0.0017  90  LYS   B C   
5138 O O   . LYS   B 90  ? 0.2011 0.1542 0.1774 -0.0567 -0.0012 0.0019  90  LYS   B O   
5139 C CB  . LYS   B 90  ? 0.2342 0.1446 0.1813 -0.0349 0.0019  0.0222  90  LYS   B CB  
5140 C CG  . LYS   B 90  ? 0.2358 0.1628 0.1859 -0.0220 0.0289  0.0218  90  LYS   B CG  
5141 C CD  . LYS   B 90  ? 0.2639 0.1908 0.2410 -0.0094 0.0440  -0.0009 90  LYS   B CD  
5142 C CE  . LYS   B 90  ? 0.2744 0.2135 0.2975 -0.0107 0.0482  -0.0095 90  LYS   B CE  
5143 N NZ  . LYS   B 90  ? 0.2838 0.2051 0.2952 -0.0277 0.0606  -0.0104 90  LYS   B NZ  
5157 N N   . HIS   B 91  ? 0.1648 0.1261 0.1336 -0.0310 -0.0134 0.0119  91  HIS   B N   
5158 C CA  . HIS   B 91  ? 0.1584 0.1288 0.1441 -0.0206 -0.0176 0.0034  91  HIS   B CA  
5159 C C   . HIS   B 91  ? 0.1525 0.1291 0.1232 -0.0236 -0.0039 0.0082  91  HIS   B C   
5160 O O   . HIS   B 91  ? 0.1627 0.1316 0.1320 -0.0237 -0.0179 0.0019  91  HIS   B O   
5161 C CB  . HIS   B 91  ? 0.1686 0.1287 0.1802 -0.0068 -0.0135 0.0159  91  HIS   B CB  
5162 C CG  . HIS   B 91  ? 0.2155 0.1464 0.2548 0.0116  0.0186  0.0236  91  HIS   B CG  
5163 N ND1 . HIS   B 91  ? 0.2506 0.1495 0.3220 0.0093  0.0275  0.0079  91  HIS   B ND1 
5164 C CD2 . HIS   B 91  ? 0.2317 0.1774 0.3041 0.0198  0.0094  0.0629  91  HIS   B CD2 
5165 C CE1 . HIS   B 91  ? 0.2529 0.1620 0.3392 0.0241  0.0260  0.0162  91  HIS   B CE1 
5166 N NE2 . HIS   B 91  ? 0.2434 0.1834 0.3417 0.0322  0.0257  0.0661  91  HIS   B NE2 
5174 N N   . CYS   B 92  ? 0.1438 0.1305 0.1222 -0.0264 -0.0128 0.0096  92  CYS   B N   
5175 C CA  . CYS   B 92  ? 0.1429 0.1263 0.1236 -0.0221 -0.0090 0.0016  92  CYS   B CA  
5176 C C   . CYS   B 92  ? 0.1342 0.1227 0.1211 -0.0123 -0.0067 0.0014  92  CYS   B C   
5177 O O   . CYS   B 92  ? 0.1397 0.1298 0.1447 -0.0132 -0.0061 -0.0001 92  CYS   B O   
5178 C CB  . CYS   B 92  ? 0.1438 0.1338 0.1450 -0.0175 -0.0076 0.0008  92  CYS   B CB  
5179 S SG  . CYS   B 92  ? 0.1412 0.1360 0.1502 -0.0117 -0.0145 0.0070  92  CYS   B SG  
5185 N N   . LEU   B 93  ? 0.1265 0.1249 0.1338 -0.0133 -0.0100 -0.0052 93  LEU   B N   
5186 C CA  . LEU   B 93  ? 0.1325 0.1227 0.1258 -0.0024 -0.0128 0.0054  93  LEU   B CA  
5187 C C   . LEU   B 93  ? 0.1280 0.1186 0.1190 -0.0014 -0.0072 0.0076  93  LEU   B C   
5188 O O   . LEU   B 93  ? 0.1329 0.1174 0.1467 -0.0022 -0.0109 -0.0021 93  LEU   B O   
5189 C CB  . LEU   B 93  ? 0.1329 0.1248 0.1449 -0.0028 -0.0063 0.0146  93  LEU   B CB  
5190 C CG  . LEU   B 93  ? 0.1294 0.1362 0.1697 -0.0053 -0.0103 0.0190  93  LEU   B CG  
5191 C CD1 . LEU   B 93  ? 0.1293 0.1482 0.1816 0.0057  -0.0050 -0.0020 93  LEU   B CD1 
5192 C CD2 . LEU   B 93  ? 0.1321 0.1397 0.1685 -0.0011 -0.0203 0.0074  93  LEU   B CD2 
5204 N N   . HIS   B 94  ? 0.1323 0.1189 0.1112 -0.0019 -0.0100 0.0044  94  HIS   B N   
5205 C CA  . HIS   B 94  ? 0.1327 0.1223 0.1155 0.0020  -0.0090 -0.0000 94  HIS   B CA  
5206 C C   . HIS   B 94  ? 0.1295 0.1224 0.1466 -0.0037 -0.0047 0.0042  94  HIS   B C   
5207 O O   . HIS   B 94  ? 0.1322 0.1279 0.1952 -0.0072 0.0066  -0.0121 94  HIS   B O   
5208 C CB  . HIS   B 94  ? 0.1291 0.1297 0.1311 -0.0001 -0.0070 0.0012  94  HIS   B CB  
5209 C CG  . HIS   B 94  ? 0.1363 0.1240 0.1361 -0.0064 -0.0268 0.0052  94  HIS   B CG  
5210 N ND1 . HIS   B 94  ? 0.1394 0.1297 0.1456 -0.0090 -0.0260 0.0038  94  HIS   B ND1 
5211 C CD2 . HIS   B 94  ? 0.1404 0.1241 0.1366 -0.0038 -0.0186 0.0085  94  HIS   B CD2 
5212 C CE1 . HIS   B 94  ? 0.1390 0.1297 0.1276 -0.0128 -0.0245 0.0030  94  HIS   B CE1 
5213 N NE2 . HIS   B 94  ? 0.1315 0.1336 0.1522 -0.0178 -0.0160 0.0012  94  HIS   B NE2 
5221 N N   . VAL   B 95  ? 0.1248 0.1183 0.1509 -0.0027 -0.0070 0.0016  95  VAL   B N   
5222 C CA  . VAL   B 95  ? 0.1230 0.1264 0.1439 -0.0007 -0.0039 0.0143  95  VAL   B CA  
5223 C C   . VAL   B 95  ? 0.1396 0.1242 0.1303 -0.0066 0.0049  0.0060  95  VAL   B C   
5224 O O   . VAL   B 95  ? 0.1368 0.1217 0.1704 0.0070  0.0038  0.0172  95  VAL   B O   
5225 C CB  . VAL   B 95  ? 0.1330 0.1267 0.1498 -0.0030 -0.0108 0.0032  95  VAL   B CB  
5226 C CG1 . VAL   B 95  ? 0.1402 0.1414 0.1702 -0.0062 -0.0083 0.0139  95  VAL   B CG1 
5227 C CG2 . VAL   B 95  ? 0.1402 0.1274 0.1464 0.0062  -0.0120 0.0015  95  VAL   B CG2 
5237 N N   . VAL   B 96  ? 0.1459 0.1350 0.1201 0.0059  0.0058  0.0073  96  VAL   B N   
5238 C CA  . VAL   B 96  ? 0.1457 0.1444 0.1295 0.0072  0.0017  0.0205  96  VAL   B CA  
5239 C C   . VAL   B 96  ? 0.1515 0.1462 0.1507 0.0084  0.0103  0.0259  96  VAL   B C   
5240 O O   . VAL   B 96  ? 0.1524 0.1485 0.1708 0.0009  0.0159  0.0117  96  VAL   B O   
5241 C CB  . VAL   B 96  ? 0.1499 0.1640 0.1234 0.0079  0.0016  0.0141  96  VAL   B CB  
5242 C CG1 . VAL   B 96  ? 0.1503 0.1782 0.1476 0.0157  0.0092  0.0019  96  VAL   B CG1 
5243 C CG2 . VAL   B 96  ? 0.1566 0.1654 0.1516 0.0049  0.0079  -0.0004 96  VAL   B CG2 
5253 N N   . GLY   B 97  ? 0.1575 0.1453 0.1491 0.0076  0.0057  0.0275  97  GLY   B N   
5254 C CA  . GLY   B 97  ? 0.1692 0.1469 0.1557 -0.0020 0.0037  0.0219  97  GLY   B CA  
5255 C C   . GLY   B 97  ? 0.1851 0.1489 0.1688 -0.0070 -0.0052 0.0074  97  GLY   B C   
5256 O O   . GLY   B 97  ? 0.1981 0.1613 0.1674 -0.0041 0.0022  0.0076  97  GLY   B O   
5260 N N   . PRO   B 98  ? 0.1942 0.1529 0.1800 -0.0014 0.0192  0.0281  98  PRO   B N   
5261 C CA  . PRO   B 98  ? 0.2082 0.1702 0.1795 0.0118  0.0321  0.0178  98  PRO   B CA  
5262 C C   . PRO   B 98  ? 0.2239 0.1758 0.1440 0.0262  0.0331  0.0382  98  PRO   B C   
5263 O O   . PRO   B 98  ? 0.2179 0.1713 0.1737 0.0191  0.0285  0.0363  98  PRO   B O   
5264 C CB  . PRO   B 98  ? 0.1961 0.1731 0.1973 0.0076  0.0444  0.0189  98  PRO   B CB  
5265 C CG  . PRO   B 98  ? 0.1930 0.1631 0.1988 0.0021  0.0347  0.0296  98  PRO   B CG  
5266 C CD  . PRO   B 98  ? 0.1787 0.1527 0.1970 0.0017  0.0253  0.0361  98  PRO   B CD  
5274 N N   . ASN   B 99  ? 0.2331 0.1890 0.1496 0.0399  0.0301  0.0241  99  ASN   B N   
5275 C CA  . ASN   B 99  ? 0.2490 0.1897 0.1634 0.0453  0.0239  0.0409  99  ASN   B CA  
5276 C C   . ASN   B 99  ? 0.2756 0.2246 0.1956 0.0433  0.0408  0.0622  99  ASN   B C   
5277 O O   . ASN   B 99  ? 0.2894 0.2327 0.2018 0.0488  0.0314  0.0642  99  ASN   B O   
5278 C CB  . ASN   B 99  ? 0.2583 0.1881 0.1829 0.0437  0.0128  0.0353  99  ASN   B CB  
5279 C CG  . ASN   B 99  ? 0.2590 0.2014 0.2072 0.0419  -0.0043 0.0303  99  ASN   B CG  
5280 O OD1 . ASN   B 99  ? 0.2598 0.2062 0.2356 0.0423  -0.0041 0.0388  99  ASN   B OD1 
5281 N ND2 . ASN   B 99  ? 0.2537 0.2044 0.2149 0.0492  -0.0215 0.0247  99  ASN   B ND2 
5288 N N   A VAL   B 100 ? 0.2896 0.2366 0.2336 0.0263  0.0525  0.0840  100 VAL   B N   
5289 N N   B VAL   B 100 ? 0.2933 0.2387 0.2337 0.0330  0.0397  0.0759  100 VAL   B N   
5290 C CA  A VAL   B 100 ? 0.3165 0.2574 0.2920 0.0163  0.0559  0.0940  100 VAL   B CA  
5291 C CA  B VAL   B 100 ? 0.3172 0.2561 0.2797 0.0257  0.0355  0.0831  100 VAL   B CA  
5292 C C   A VAL   B 100 ? 0.3373 0.2618 0.2808 0.0246  0.0532  0.1069  100 VAL   B C   
5293 C C   B VAL   B 100 ? 0.3359 0.2617 0.2791 0.0304  0.0349  0.0984  100 VAL   B C   
5294 O O   A VAL   B 100 ? 0.3457 0.2745 0.2861 0.0243  0.0642  0.0966  100 VAL   B O   
5295 O O   B VAL   B 100 ? 0.3402 0.2688 0.2816 0.0292  0.0382  0.0929  100 VAL   B O   
5296 C CB  A VAL   B 100 ? 0.3218 0.2740 0.3594 -0.0040 0.0546  0.1041  100 VAL   B CB  
5297 C CB  B VAL   B 100 ? 0.3217 0.2674 0.3232 0.0139  0.0296  0.0820  100 VAL   B CB  
5298 C CG1 A VAL   B 100 ? 0.3283 0.2823 0.3895 -0.0075 0.0558  0.1022  100 VAL   B CG1 
5299 C CG1 B VAL   B 100 ? 0.3256 0.2724 0.3417 0.0112  0.0291  0.0803  100 VAL   B CG1 
5300 C CG2 A VAL   B 100 ? 0.3208 0.2784 0.3769 -0.0105 0.0569  0.1125  100 VAL   B CG2 
5301 C CG2 B VAL   B 100 ? 0.3215 0.2704 0.3360 0.0103  0.0285  0.0832  100 VAL   B CG2 
5320 N N   . ASN   B 101 ? 0.3491 0.2644 0.2788 0.0390  0.0282  0.1120  101 ASN   B N   
5321 C CA  . ASN   B 101 ? 0.3866 0.2839 0.2962 0.0453  0.0103  0.1250  101 ASN   B CA  
5322 C C   . ASN   B 101 ? 0.4298 0.3255 0.3026 0.0464  0.0002  0.1274  101 ASN   B C   
5323 O O   . ASN   B 101 ? 0.4358 0.3441 0.3290 0.0531  0.0056  0.0951  101 ASN   B O   
5324 C CB  . ASN   B 101 ? 0.3848 0.2715 0.3191 0.0411  0.0115  0.1109  101 ASN   B CB  
5325 C CG  . ASN   B 101 ? 0.3836 0.2590 0.3239 0.0367  0.0129  0.1153  101 ASN   B CG  
5326 O OD1 . ASN   B 101 ? 0.3891 0.2557 0.3545 0.0280  0.0298  0.1092  101 ASN   B OD1 
5327 N ND2 . ASN   B 101 ? 0.3791 0.2575 0.3142 0.0361  0.0080  0.1086  101 ASN   B ND2 
5335 N N   . LYS   B 102 ? 0.4628 0.3556 0.3157 0.0350  0.0003  0.1270  102 LYS   B N   
5336 C CA  . LYS   B 102 ? 0.4941 0.3947 0.3371 0.0187  0.0098  0.1086  102 LYS   B CA  
5337 C C   . LYS   B 102 ? 0.4910 0.3949 0.3160 0.0185  0.0211  0.1080  102 LYS   B C   
5338 O O   . LYS   B 102 ? 0.5011 0.4008 0.3240 0.0194  0.0123  0.1001  102 LYS   B O   
5339 C CB  . LYS   B 102 ? 0.5238 0.4333 0.4025 0.0060  0.0198  0.0734  102 LYS   B CB  
5340 C CG  . LYS   B 102 ? 0.5478 0.4700 0.4732 -0.0031 0.0296  0.0370  102 LYS   B CG  
5341 C CD  . LYS   B 102 ? 0.5688 0.5005 0.5410 -0.0091 0.0396  0.0098  102 LYS   B CD  
5342 C CE  . LYS   B 102 ? 0.5851 0.5204 0.5961 -0.0140 0.0458  -0.0099 102 LYS   B CE  
5343 N NZ  . LYS   B 102 ? 0.5940 0.5324 0.6285 -0.0163 0.0476  -0.0212 102 LYS   B NZ  
5357 N N   . GLY   B 103 ? 0.4718 0.3849 0.3059 0.0172  0.0417  0.1051  103 GLY   B N   
5358 C CA  . GLY   B 103 ? 0.4496 0.3742 0.3126 0.0177  0.0628  0.0878  103 GLY   B CA  
5359 C C   . GLY   B 103 ? 0.4238 0.3591 0.3074 0.0143  0.0801  0.0671  103 GLY   B C   
5360 O O   . GLY   B 103 ? 0.4326 0.3696 0.3107 0.0131  0.0856  0.0666  103 GLY   B O   
5364 N N   A GLU   B 104 ? 0.3991 0.3386 0.2876 0.0128  0.0972  0.0516  104 GLU   B N   
5365 N N   B GLU   B 104 ? 0.4099 0.3498 0.3059 0.0098  0.0753  0.0529  104 GLU   B N   
5366 C CA  A GLU   B 104 ? 0.3723 0.3193 0.2703 0.0110  0.1057  0.0395  104 GLU   B CA  
5367 C CA  B GLU   B 104 ? 0.3944 0.3400 0.3008 0.0049  0.0689  0.0388  104 GLU   B CA  
5368 C C   A GLU   B 104 ? 0.3756 0.3260 0.2896 -0.0022 0.1267  0.0326  104 GLU   B C   
5369 C C   B GLU   B 104 ? 0.3920 0.3401 0.3138 -0.0043 0.0816  0.0314  104 GLU   B C   
5370 O O   A GLU   B 104 ? 0.3784 0.3289 0.3131 -0.0073 0.1210  0.0216  104 GLU   B O   
5371 O O   B GLU   B 104 ? 0.3932 0.3425 0.3236 -0.0066 0.0789  0.0256  104 GLU   B O   
5372 C CB  A GLU   B 104 ? 0.3481 0.2934 0.2486 0.0214  0.0823  0.0243  104 GLU   B CB  
5373 C CB  B GLU   B 104 ? 0.3832 0.3294 0.2869 0.0080  0.0495  0.0286  104 GLU   B CB  
5374 C CG  A GLU   B 104 ? 0.3299 0.2763 0.2297 0.0319  0.0471  0.0059  104 GLU   B CG  
5375 C CG  B GLU   B 104 ? 0.3745 0.3218 0.2744 0.0109  0.0289  0.0172  104 GLU   B CG  
5376 C CD  A GLU   B 104 ? 0.3143 0.2598 0.2075 0.0395  0.0195  0.0021  104 GLU   B CD  
5377 C CD  B GLU   B 104 ? 0.3685 0.3155 0.2633 0.0119  0.0127  0.0108  104 GLU   B CD  
5378 O OE1 A GLU   B 104 ? 0.2924 0.2410 0.1764 0.0453  0.0232  0.0076  104 GLU   B OE1 
5379 O OE1 B GLU   B 104 ? 0.3634 0.3102 0.2515 0.0112  0.0124  0.0119  104 GLU   B OE1 
5380 O OE2 A GLU   B 104 ? 0.3224 0.2721 0.2194 0.0380  -0.0111 -0.0077 104 GLU   B OE2 
5381 O OE2 B GLU   B 104 ? 0.3697 0.3185 0.2678 0.0130  -0.0011 0.0034  104 GLU   B OE2 
5394 N N   A ASP   B 105 ? 0.3708 0.3323 0.2843 -0.0119 0.1521  0.0404  105 ASP   B N   
5395 N N   B ASP   B 105 ? 0.3862 0.3383 0.3153 -0.0120 0.0974  0.0317  105 ASP   B N   
5396 C CA  A ASP   B 105 ? 0.3738 0.3406 0.3140 -0.0176 0.1666  0.0257  105 ASP   B CA  
5397 C CA  B ASP   B 105 ? 0.3831 0.3359 0.3281 -0.0187 0.1112  0.0244  105 ASP   B CA  
5398 C C   A ASP   B 105 ? 0.3584 0.3134 0.2933 -0.0235 0.1634  0.0234  105 ASP   B C   
5399 C C   B ASP   B 105 ? 0.3714 0.3165 0.3121 -0.0224 0.1264  0.0228  105 ASP   B C   
5400 O O   A ASP   B 105 ? 0.3421 0.3023 0.2789 -0.0255 0.1764  0.0262  105 ASP   B O   
5401 O O   B ASP   B 105 ? 0.3687 0.3148 0.3045 -0.0232 0.1276  0.0229  105 ASP   B O   
5402 C CB  A ASP   B 105 ? 0.3883 0.3710 0.3785 -0.0108 0.1755  0.0059  105 ASP   B CB  
5403 C CB  B ASP   B 105 ? 0.3883 0.3498 0.3585 -0.0185 0.1108  0.0169  105 ASP   B CB  
5404 C CG  A ASP   B 105 ? 0.3981 0.3929 0.4413 -0.0077 0.1876  -0.0073 105 ASP   B CG  
5405 C CG  B ASP   B 105 ? 0.3918 0.3583 0.3888 -0.0201 0.1122  0.0135  105 ASP   B CG  
5406 O OD1 A ASP   B 105 ? 0.3939 0.3983 0.4409 -0.0179 0.2092  0.0022  105 ASP   B OD1 
5407 O OD1 B ASP   B 105 ? 0.3914 0.3616 0.3946 -0.0249 0.1154  0.0169  105 ASP   B OD1 
5408 O OD2 A ASP   B 105 ? 0.4069 0.4048 0.4847 0.0014  0.1715  -0.0247 105 ASP   B OD2 
5409 O OD2 B ASP   B 105 ? 0.3914 0.3611 0.3979 -0.0208 0.1147  0.0116  105 ASP   B OD2 
5418 N N   . ILE   B 106 ? 0.3619 0.2972 0.3082 -0.0225 0.1337  0.0239  106 ILE   B N   
5419 C CA  . ILE   B 106 ? 0.3371 0.2574 0.3092 -0.0263 0.1392  0.0204  106 ILE   B CA  
5420 C C   . ILE   B 106 ? 0.2999 0.2540 0.3017 -0.0165 0.1339  -0.0050 106 ILE   B C   
5421 O O   . ILE   B 106 ? 0.2885 0.2260 0.3007 -0.0228 0.1227  -0.0066 106 ILE   B O   
5422 C CB  . ILE   B 106 ? 0.3604 0.2442 0.3300 -0.0302 0.1299  0.0317  106 ILE   B CB  
5423 C CG1 . ILE   B 106 ? 0.3686 0.2398 0.3332 -0.0109 0.1194  0.0284  106 ILE   B CG1 
5424 C CG2 . ILE   B 106 ? 0.3668 0.2487 0.3567 -0.0422 0.1329  0.0370  106 ILE   B CG2 
5425 C CD1 . ILE   B 106 ? 0.3721 0.2408 0.3259 0.0064  0.1138  0.0372  106 ILE   B CD1 
5438 N N   A GLN   B 107 ? 0.2908 0.2766 0.3253 -0.0182 0.1300  -0.0120 107 GLN   B N   
5439 N N   B GLN   B 107 ? 0.2949 0.2703 0.3181 -0.0151 0.1192  -0.0094 107 GLN   B N   
5440 C CA  A GLN   B 107 ? 0.2766 0.2941 0.3449 -0.0220 0.1234  -0.0087 107 GLN   B CA  
5441 C CA  B GLN   B 107 ? 0.2874 0.2841 0.3351 -0.0140 0.1018  -0.0086 107 GLN   B CA  
5442 C C   A GLN   B 107 ? 0.2534 0.2720 0.3235 -0.0108 0.0891  -0.0144 107 GLN   B C   
5443 C C   B GLN   B 107 ? 0.2629 0.2695 0.3106 -0.0060 0.0856  -0.0118 107 GLN   B C   
5444 O O   A GLN   B 107 ? 0.2429 0.2770 0.3601 -0.0067 0.0619  -0.0289 107 GLN   B O   
5445 O O   B GLN   B 107 ? 0.2616 0.2744 0.3275 -0.0048 0.0724  -0.0185 107 GLN   B O   
5446 C CB  A GLN   B 107 ? 0.3077 0.3396 0.4080 -0.0241 0.1139  -0.0055 107 GLN   B CB  
5447 C CB  B GLN   B 107 ? 0.3121 0.3137 0.3855 -0.0153 0.0867  -0.0062 107 GLN   B CB  
5448 C CG  A GLN   B 107 ? 0.3408 0.3841 0.4733 -0.0190 0.0870  -0.0030 107 GLN   B CG  
5449 C CG  B GLN   B 107 ? 0.3352 0.3397 0.4353 -0.0131 0.0657  -0.0037 107 GLN   B CG  
5450 C CD  A GLN   B 107 ? 0.3638 0.4136 0.5250 -0.0197 0.0661  0.0034  107 GLN   B CD  
5451 C CD  B GLN   B 107 ? 0.3521 0.3586 0.4755 -0.0137 0.0484  0.0009  107 GLN   B CD  
5452 O OE1 A GLN   B 107 ? 0.3735 0.4240 0.5433 -0.0182 0.0648  0.0019  107 GLN   B OE1 
5453 O OE1 B GLN   B 107 ? 0.3582 0.3659 0.4891 -0.0136 0.0458  0.0009  107 GLN   B OE1 
5454 N NE2 A GLN   B 107 ? 0.3728 0.4224 0.5443 -0.0176 0.0546  0.0115  107 GLN   B NE2 
5455 N NE2 B GLN   B 107 ? 0.3592 0.3649 0.4906 -0.0123 0.0410  0.0057  107 GLN   B NE2 
5472 N N   . LEU   B 108 ? 0.2372 0.2504 0.2822 0.0037  0.0807  -0.0097 108 LEU   B N   
5473 C CA  . LEU   B 108 ? 0.2231 0.2258 0.2387 0.0199  0.0552  0.0093  108 LEU   B CA  
5474 C C   . LEU   B 108 ? 0.1882 0.1878 0.2233 0.0192  0.0294  0.0230  108 LEU   B C   
5475 O O   . LEU   B 108 ? 0.1897 0.1769 0.2231 0.0173  0.0208  0.0142  108 LEU   B O   
5476 C CB  . LEU   B 108 ? 0.2421 0.2481 0.2273 0.0164  0.0600  0.0197  108 LEU   B CB  
5477 C CG  . LEU   B 108 ? 0.2587 0.2773 0.2334 0.0240  0.0486  -0.0033 108 LEU   B CG  
5478 C CD1 . LEU   B 108 ? 0.2670 0.2926 0.2209 0.0147  0.0493  -0.0008 108 LEU   B CD1 
5479 C CD2 . LEU   B 108 ? 0.2761 0.2902 0.2480 0.0337  0.0399  -0.0183 108 LEU   B CD2 
5492 N N   . LEU   B 109 ? 0.1746 0.1712 0.2135 0.0135  0.0316  0.0171  109 LEU   B N   
5493 C CA  . LEU   B 109 ? 0.1556 0.1477 0.2323 0.0069  0.0331  0.0325  109 LEU   B CA  
5494 C C   . LEU   B 109 ? 0.1480 0.1314 0.2262 0.0018  0.0291  0.0180  109 LEU   B C   
5495 O O   . LEU   B 109 ? 0.1446 0.1347 0.2155 0.0051  0.0274  0.0277  109 LEU   B O   
5496 C CB  . LEU   B 109 ? 0.1658 0.1391 0.2451 0.0113  0.0208  0.0374  109 LEU   B CB  
5497 C CG  . LEU   B 109 ? 0.1627 0.1366 0.2362 0.0073  0.0105  0.0227  109 LEU   B CG  
5498 C CD1 . LEU   B 109 ? 0.1566 0.1551 0.2128 0.0072  0.0112  0.0213  109 LEU   B CD1 
5499 C CD2 . LEU   B 109 ? 0.1756 0.1363 0.2421 0.0027  0.0076  0.0214  109 LEU   B CD2 
5511 N N   . LYS   B 110 ? 0.1468 0.1347 0.2106 -0.0060 0.0295  0.0242  110 LYS   B N   
5512 C CA  . LYS   B 110 ? 0.1444 0.1318 0.2139 0.0007  0.0200  0.0154  110 LYS   B CA  
5513 C C   . LYS   B 110 ? 0.1401 0.1359 0.2073 -0.0046 0.0223  0.0126  110 LYS   B C   
5514 O O   . LYS   B 110 ? 0.1384 0.1358 0.1980 -0.0050 0.0122  0.0101  110 LYS   B O   
5515 C CB  . LYS   B 110 ? 0.1474 0.1388 0.2390 -0.0030 0.0206  0.0106  110 LYS   B CB  
5516 C CG  . LYS   B 110 ? 0.1460 0.1387 0.2499 -0.0052 0.0038  0.0147  110 LYS   B CG  
5517 C CD  . LYS   B 110 ? 0.1520 0.1372 0.2599 -0.0085 0.0050  0.0167  110 LYS   B CD  
5518 C CE  . LYS   B 110 ? 0.1533 0.1567 0.2781 -0.0104 0.0024  0.0045  110 LYS   B CE  
5519 N NZ  . LYS   B 110 ? 0.1532 0.1629 0.2723 -0.0073 -0.0010 0.0012  110 LYS   B NZ  
5533 N N   . SER   B 111 ? 0.1462 0.1333 0.2325 -0.0088 0.0239  0.0113  111 SER   B N   
5534 C CA  . SER   B 111 ? 0.1474 0.1345 0.2134 0.0020  0.0174  0.0163  111 SER   B CA  
5535 C C   . SER   B 111 ? 0.1471 0.1296 0.2105 0.0040  0.0111  0.0065  111 SER   B C   
5536 O O   . SER   B 111 ? 0.1421 0.1358 0.2086 0.0025  0.0044  0.0117  111 SER   B O   
5537 C CB  . SER   B 111 ? 0.1604 0.1588 0.2314 0.0060  0.0309  0.0279  111 SER   B CB  
5538 O OG  . SER   B 111 ? 0.1798 0.1989 0.2428 0.0094  0.0391  0.0406  111 SER   B OG  
5544 N N   . ALA   B 112 ? 0.1421 0.1339 0.2101 0.0027  0.0175  0.0185  112 ALA   B N   
5545 C CA  . ALA   B 112 ? 0.1369 0.1424 0.1976 0.0001  -0.0025 0.0012  112 ALA   B CA  
5546 C C   . ALA   B 112 ? 0.1290 0.1368 0.1885 0.0016  -0.0028 0.0027  112 ALA   B C   
5547 O O   . ALA   B 112 ? 0.1299 0.1334 0.1994 -0.0055 0.0054  0.0013  112 ALA   B O   
5548 C CB  . ALA   B 112 ? 0.1382 0.1469 0.2229 0.0037  -0.0023 0.0179  112 ALA   B CB  
5554 N N   . TYR   B 113 ? 0.1250 0.1271 0.1995 0.0002  0.0004  0.0063  113 TYR   B N   
5555 C CA  . TYR   B 113 ? 0.1297 0.1242 0.1895 -0.0039 0.0030  0.0014  113 TYR   B CA  
5556 C C   . TYR   B 113 ? 0.1267 0.1216 0.1729 -0.0088 0.0076  0.0079  113 TYR   B C   
5557 O O   . TYR   B 113 ? 0.1271 0.1191 0.1786 -0.0027 -0.0047 -0.0015 113 TYR   B O   
5558 C CB  . TYR   B 113 ? 0.1302 0.1152 0.1939 -0.0033 0.0090  0.0096  113 TYR   B CB  
5559 C CG  . TYR   B 113 ? 0.1307 0.1134 0.2103 -0.0035 0.0014  0.0061  113 TYR   B CG  
5560 C CD1 . TYR   B 113 ? 0.1373 0.1157 0.2271 -0.0028 0.0087  0.0141  113 TYR   B CD1 
5561 C CD2 . TYR   B 113 ? 0.1391 0.1173 0.2119 -0.0022 0.0006  0.0047  113 TYR   B CD2 
5562 C CE1 . TYR   B 113 ? 0.1380 0.1258 0.2155 -0.0043 0.0105  0.0069  113 TYR   B CE1 
5563 C CE2 . TYR   B 113 ? 0.1403 0.1124 0.2313 -0.0013 0.0056  0.0075  113 TYR   B CE2 
5564 C CZ  . TYR   B 113 ? 0.1366 0.1186 0.2283 0.0069  0.0051  0.0080  113 TYR   B CZ  
5565 O OH  . TYR   B 113 ? 0.1461 0.1164 0.2475 0.0057  0.0189  0.0118  113 TYR   B OH  
5575 N N   . GLU   B 114 ? 0.1243 0.1173 0.1963 -0.0038 0.0043  0.0051  114 GLU   B N   
5576 C CA  . GLU   B 114 ? 0.1200 0.1178 0.2008 0.0025  -0.0001 0.0080  114 GLU   B CA  
5577 C C   . GLU   B 114 ? 0.1185 0.1112 0.1925 0.0012  0.0057  0.0023  114 GLU   B C   
5578 O O   . GLU   B 114 ? 0.1196 0.1188 0.2022 0.0043  -0.0068 0.0070  114 GLU   B O   
5579 C CB  . GLU   B 114 ? 0.1228 0.1250 0.2173 -0.0003 0.0146  0.0104  114 GLU   B CB  
5580 C CG  . GLU   B 114 ? 0.1270 0.1217 0.2075 -0.0019 0.0048  0.0121  114 GLU   B CG  
5581 C CD  . GLU   B 114 ? 0.1283 0.1292 0.2125 -0.0051 0.0066  0.0105  114 GLU   B CD  
5582 O OE1 . GLU   B 114 ? 0.1293 0.1458 0.2113 -0.0031 0.0152  0.0047  114 GLU   B OE1 
5583 O OE2 . GLU   B 114 ? 0.1286 0.1455 0.2292 -0.0164 0.0078  0.0084  114 GLU   B OE2 
5590 N N   . ASN   B 115 ? 0.1247 0.1082 0.1858 -0.0017 -0.0017 0.0077  115 ASN   B N   
5591 C CA  . ASN   B 115 ? 0.1284 0.1172 0.1702 -0.0054 -0.0008 0.0069  115 ASN   B CA  
5592 C C   . ASN   B 115 ? 0.1265 0.1182 0.1718 -0.0057 -0.0077 0.0058  115 ASN   B C   
5593 O O   . ASN   B 115 ? 0.1316 0.1248 0.1901 -0.0121 -0.0058 0.0020  115 ASN   B O   
5594 C CB  . ASN   B 115 ? 0.1398 0.1279 0.1847 -0.0081 -0.0004 0.0068  115 ASN   B CB  
5595 C CG  . ASN   B 115 ? 0.1433 0.1372 0.1831 0.0071  -0.0044 -0.0036 115 ASN   B CG  
5596 O OD1 . ASN   B 115 ? 0.1861 0.1463 0.2044 0.0032  0.0097  -0.0110 115 ASN   B OD1 
5597 N ND2 . ASN   B 115 ? 0.1426 0.1468 0.1885 -0.0005 0.0028  0.0061  115 ASN   B ND2 
5604 N N   . PHE   B 116 ? 0.1300 0.1193 0.1563 -0.0003 -0.0003 -0.0007 116 PHE   B N   
5605 C CA  . PHE   B 116 ? 0.1346 0.1220 0.1674 -0.0123 -0.0073 0.0022  116 PHE   B CA  
5606 C C   . PHE   B 116 ? 0.1331 0.1095 0.1606 -0.0101 -0.0128 0.0088  116 PHE   B C   
5607 O O   . PHE   B 116 ? 0.1355 0.1167 0.1773 -0.0020 -0.0104 0.0014  116 PHE   B O   
5608 C CB  . PHE   B 116 ? 0.1299 0.1146 0.1531 -0.0074 -0.0140 -0.0020 116 PHE   B CB  
5609 C CG  . PHE   B 116 ? 0.1214 0.1166 0.1632 -0.0001 -0.0128 0.0018  116 PHE   B CG  
5610 C CD1 . PHE   B 116 ? 0.1290 0.1232 0.1866 -0.0007 -0.0063 0.0013  116 PHE   B CD1 
5611 C CD2 . PHE   B 116 ? 0.1259 0.1259 0.1609 -0.0036 -0.0056 -0.0070 116 PHE   B CD2 
5612 C CE1 . PHE   B 116 ? 0.1308 0.1309 0.1722 -0.0020 -0.0242 -0.0003 116 PHE   B CE1 
5613 C CE2 . PHE   B 116 ? 0.1262 0.1219 0.1764 -0.0013 -0.0066 0.0031  116 PHE   B CE2 
5614 C CZ  . PHE   B 116 ? 0.1154 0.1327 0.1768 -0.0013 -0.0134 0.0063  116 PHE   B CZ  
5624 N N   . ASN   B 117 ? 0.1313 0.1184 0.1785 -0.0039 -0.0126 0.0067  117 ASN   B N   
5625 C CA  . ASN   B 117 ? 0.1378 0.1201 0.1814 -0.0010 -0.0116 0.0045  117 ASN   B CA  
5626 C C   . ASN   B 117 ? 0.1423 0.1145 0.1944 0.0035  -0.0084 0.0063  117 ASN   B C   
5627 O O   . ASN   B 117 ? 0.1491 0.1234 0.2253 -0.0036 -0.0335 0.0095  117 ASN   B O   
5628 C CB  . ASN   B 117 ? 0.1339 0.1228 0.1880 -0.0045 -0.0057 -0.0012 117 ASN   B CB  
5629 C CG  . ASN   B 117 ? 0.1302 0.1217 0.1901 0.0022  -0.0097 -0.0113 117 ASN   B CG  
5630 O OD1 . ASN   B 117 ? 0.1523 0.1207 0.2121 -0.0102 -0.0053 -0.0059 117 ASN   B OD1 
5631 N ND2 . ASN   B 117 ? 0.1359 0.1266 0.1912 -0.0016 -0.0062 -0.0035 117 ASN   B ND2 
5638 N N   . GLN   B 118 ? 0.1347 0.1147 0.1833 -0.0016 -0.0249 0.0030  118 GLN   B N   
5639 C CA  . GLN   B 118 ? 0.1367 0.1142 0.2004 -0.0006 -0.0142 0.0026  118 GLN   B CA  
5640 C C   . GLN   B 118 ? 0.1433 0.1185 0.2040 -0.0007 -0.0116 -0.0026 118 GLN   B C   
5641 O O   . GLN   B 118 ? 0.1618 0.1194 0.2407 -0.0040 0.0038  0.0043  118 GLN   B O   
5642 C CB  . GLN   B 118 ? 0.1465 0.1221 0.2163 0.0037  -0.0204 0.0059  118 GLN   B CB  
5643 C CG  . GLN   B 118 ? 0.1525 0.1273 0.2095 0.0083  -0.0091 -0.0086 118 GLN   B CG  
5644 C CD  . GLN   B 118 ? 0.1582 0.1243 0.1996 0.0086  -0.0086 -0.0144 118 GLN   B CD  
5645 O OE1 . GLN   B 118 ? 0.1666 0.1238 0.2121 0.0059  0.0030  0.0052  118 GLN   B OE1 
5646 N NE2 . GLN   B 118 ? 0.1635 0.1232 0.2230 0.0040  -0.0134 0.0001  118 GLN   B NE2 
5655 N N   . HIS   B 119 ? 0.1467 0.1205 0.1804 -0.0092 -0.0171 0.0019  119 HIS   B N   
5656 C CA  . HIS   B 119 ? 0.1547 0.1295 0.1716 -0.0023 -0.0194 0.0107  119 HIS   B CA  
5657 C C   . HIS   B 119 ? 0.1579 0.1288 0.1669 -0.0008 -0.0299 0.0118  119 HIS   B C   
5658 O O   . HIS   B 119 ? 0.1610 0.1271 0.1895 -0.0229 -0.0128 0.0099  119 HIS   B O   
5659 C CB  . HIS   B 119 ? 0.1607 0.1489 0.1714 -0.0039 -0.0189 0.0030  119 HIS   B CB  
5660 C CG  . HIS   B 119 ? 0.1640 0.1697 0.1881 0.0088  -0.0459 -0.0142 119 HIS   B CG  
5661 N ND1 . HIS   B 119 ? 0.1788 0.1808 0.2261 0.0003  -0.0519 -0.0256 119 HIS   B ND1 
5662 C CD2 . HIS   B 119 ? 0.1797 0.1894 0.1879 0.0370  -0.0509 -0.0273 119 HIS   B CD2 
5663 C CE1 . HIS   B 119 ? 0.1980 0.1969 0.2335 0.0167  -0.0504 -0.0375 119 HIS   B CE1 
5664 N NE2 . HIS   B 119 ? 0.2012 0.2111 0.2110 0.0338  -0.0474 -0.0379 119 HIS   B NE2 
5672 N N   . GLU   B 120 ? 0.1794 0.1288 0.1669 -0.0076 -0.0359 0.0184  120 GLU   B N   
5673 C CA  . GLU   B 120 ? 0.2065 0.1480 0.1782 -0.0031 -0.0451 0.0291  120 GLU   B CA  
5674 C C   . GLU   B 120 ? 0.1816 0.1429 0.1714 -0.0125 -0.0357 0.0194  120 GLU   B C   
5675 O O   . GLU   B 120 ? 0.1753 0.1585 0.1751 -0.0154 -0.0399 0.0118  120 GLU   B O   
5676 C CB  . GLU   B 120 ? 0.2803 0.1897 0.2483 0.0246  -0.0783 0.0453  120 GLU   B CB  
5677 C CG  . GLU   B 120 ? 0.3469 0.2664 0.3551 0.0352  -0.0968 0.0678  120 GLU   B CG  
5678 C CD  . GLU   B 120 ? 0.3949 0.3389 0.4536 0.0388  -0.1043 0.0821  120 GLU   B CD  
5679 O OE1 . GLU   B 120 ? 0.4146 0.3664 0.4854 0.0333  -0.1007 0.0973  120 GLU   B OE1 
5680 O OE2 . GLU   B 120 ? 0.4166 0.3663 0.5021 0.0410  -0.1051 0.0758  120 GLU   B OE2 
5687 N N   . VAL   B 121 ? 0.1668 0.1328 0.1720 -0.0218 -0.0235 0.0162  121 VAL   B N   
5688 C CA  . VAL   B 121 ? 0.1644 0.1417 0.1614 -0.0174 -0.0192 0.0073  121 VAL   B CA  
5689 C C   . VAL   B 121 ? 0.1573 0.1420 0.1608 -0.0249 -0.0199 0.0136  121 VAL   B C   
5690 O O   . VAL   B 121 ? 0.1675 0.1381 0.1748 -0.0373 -0.0250 0.0100  121 VAL   B O   
5691 C CB  . VAL   B 121 ? 0.1886 0.1795 0.1696 -0.0044 -0.0270 0.0170  121 VAL   B CB  
5692 C CG1 . VAL   B 121 ? 0.1978 0.1972 0.2155 -0.0127 -0.0155 0.0117  121 VAL   B CG1 
5693 C CG2 . VAL   B 121 ? 0.2146 0.2066 0.1710 0.0067  -0.0189 0.0084  121 VAL   B CG2 
5703 N N   . LEU   B 122 ? 0.1522 0.1349 0.1522 -0.0175 -0.0230 0.0119  122 LEU   B N   
5704 C CA  . LEU   B 122 ? 0.1379 0.1411 0.1404 -0.0240 -0.0202 0.0137  122 LEU   B CA  
5705 C C   . LEU   B 122 ? 0.1395 0.1315 0.1449 -0.0251 -0.0186 0.0090  122 LEU   B C   
5706 O O   . LEU   B 122 ? 0.1513 0.1330 0.1847 -0.0253 -0.0256 -0.0009 122 LEU   B O   
5707 C CB  . LEU   B 122 ? 0.1617 0.1494 0.1698 -0.0040 -0.0290 0.0116  122 LEU   B CB  
5708 C CG  . LEU   B 122 ? 0.1499 0.1595 0.1794 -0.0132 -0.0156 0.0057  122 LEU   B CG  
5709 C CD1 . LEU   B 122 ? 0.1544 0.1893 0.1884 -0.0229 -0.0160 0.0137  122 LEU   B CD1 
5710 C CD2 . LEU   B 122 ? 0.1530 0.1582 0.1651 -0.0120 -0.0107 -0.0056 122 LEU   B CD2 
5722 N N   . LEU   B 123 ? 0.1445 0.1183 0.1385 -0.0270 -0.0215 0.0117  123 LEU   B N   
5723 C CA  . LEU   B 123 ? 0.1513 0.1240 0.1433 -0.0241 -0.0303 0.0032  123 LEU   B CA  
5724 C C   . LEU   B 123 ? 0.1441 0.1230 0.1320 -0.0135 -0.0241 0.0007  123 LEU   B C   
5725 O O   . LEU   B 123 ? 0.1518 0.1297 0.1357 -0.0281 -0.0150 0.0041  123 LEU   B O   
5726 C CB  . LEU   B 123 ? 0.1597 0.1318 0.1590 -0.0220 -0.0131 -0.0032 123 LEU   B CB  
5727 C CG  . LEU   B 123 ? 0.1517 0.1342 0.1647 -0.0159 -0.0090 0.0030  123 LEU   B CG  
5728 C CD1 . LEU   B 123 ? 0.1617 0.1444 0.1699 -0.0173 -0.0019 -0.0105 123 LEU   B CD1 
5729 C CD2 . LEU   B 123 ? 0.1592 0.1363 0.1882 -0.0141 -0.0032 0.0120  123 LEU   B CD2 
5741 N N   . ALA   B 124 ? 0.1395 0.1181 0.1446 -0.0136 -0.0124 0.0026  124 ALA   B N   
5742 C CA  . ALA   B 124 ? 0.1283 0.1197 0.1485 -0.0167 -0.0118 -0.0046 124 ALA   B CA  
5743 C C   . ALA   B 124 ? 0.1279 0.1218 0.1280 -0.0172 -0.0031 -0.0033 124 ALA   B C   
5744 O O   . ALA   B 124 ? 0.1414 0.1255 0.1494 -0.0123 -0.0150 -0.0033 124 ALA   B O   
5745 C CB  . ALA   B 124 ? 0.1375 0.1276 0.1623 -0.0099 -0.0063 0.0004  124 ALA   B CB  
5751 N N   . PRO   B 125 ? 0.1394 0.1285 0.1326 -0.0171 -0.0170 0.0097  125 PRO   B N   
5752 C CA  . PRO   B 125 ? 0.1489 0.1258 0.1551 -0.0182 -0.0147 0.0195  125 PRO   B CA  
5753 C C   . PRO   B 125 ? 0.1451 0.1166 0.1811 -0.0158 -0.0049 0.0054  125 PRO   B C   
5754 O O   . PRO   B 125 ? 0.1478 0.1186 0.1938 -0.0100 -0.0035 0.0184  125 PRO   B O   
5755 C CB  . PRO   B 125 ? 0.1488 0.1505 0.1769 -0.0218 -0.0220 0.0352  125 PRO   B CB  
5756 C CG  . PRO   B 125 ? 0.1556 0.1528 0.1714 -0.0317 -0.0271 0.0189  125 PRO   B CG  
5757 C CD  . PRO   B 125 ? 0.1518 0.1341 0.1490 -0.0298 -0.0128 0.0034  125 PRO   B CD  
5765 N N   . LEU   B 126 ? 0.1450 0.1142 0.2030 -0.0132 0.0105  0.0119  126 LEU   B N   
5766 C CA  . LEU   B 126 ? 0.1494 0.1273 0.1934 -0.0120 0.0150  0.0213  126 LEU   B CA  
5767 C C   . LEU   B 126 ? 0.1456 0.1377 0.1996 -0.0005 0.0162  0.0189  126 LEU   B C   
5768 O O   . LEU   B 126 ? 0.1694 0.1677 0.2226 0.0159  -0.0110 -0.0098 126 LEU   B O   
5769 C CB  . LEU   B 126 ? 0.1673 0.1343 0.2211 -0.0165 0.0182  0.0124  126 LEU   B CB  
5770 C CG  . LEU   B 126 ? 0.1836 0.1475 0.2298 -0.0183 0.0181  -0.0111 126 LEU   B CG  
5771 C CD1 . LEU   B 126 ? 0.1928 0.1473 0.2682 -0.0209 0.0101  -0.0244 126 LEU   B CD1 
5772 C CD2 . LEU   B 126 ? 0.1818 0.1581 0.2350 -0.0300 0.0077  -0.0173 126 LEU   B CD2 
5784 N N   . LEU   B 127 ? 0.1474 0.1250 0.2152 0.0034  0.0198  0.0177  127 LEU   B N   
5785 C CA  . LEU   B 127 ? 0.1423 0.1335 0.2112 -0.0047 0.0237  0.0254  127 LEU   B CA  
5786 C C   . LEU   B 127 ? 0.1388 0.1304 0.2083 -0.0005 0.0131  0.0220  127 LEU   B C   
5787 O O   . LEU   B 127 ? 0.1446 0.1366 0.2191 -0.0171 0.0018  0.0189  127 LEU   B O   
5788 C CB  . LEU   B 127 ? 0.1546 0.1301 0.2214 -0.0023 0.0165  0.0224  127 LEU   B CB  
5789 C CG  . LEU   B 127 ? 0.1675 0.1294 0.2267 0.0012  0.0173  0.0207  127 LEU   B CG  
5790 C CD1 . LEU   B 127 ? 0.1762 0.1297 0.2317 0.0026  0.0054  0.0088  127 LEU   B CD1 
5791 C CD2 . LEU   B 127 ? 0.1675 0.1447 0.2323 -0.0109 0.0178  0.0304  127 LEU   B CD2 
5803 N N   . SER   B 128 ? 0.1444 0.1293 0.2058 -0.0000 -0.0079 0.0108  128 SER   B N   
5804 C CA  . SER   B 128 ? 0.1609 0.1383 0.1939 0.0081  -0.0108 0.0193  128 SER   B CA  
5805 C C   . SER   B 128 ? 0.1761 0.1408 0.2167 0.0083  -0.0283 0.0201  128 SER   B C   
5806 O O   . SER   B 128 ? 0.1903 0.1401 0.2627 0.0083  -0.0195 0.0360  128 SER   B O   
5807 C CB  . SER   B 128 ? 0.1692 0.1404 0.2041 0.0043  0.0013  0.0314  128 SER   B CB  
5808 O OG  . SER   B 128 ? 0.1734 0.1514 0.2135 0.0076  0.0055  0.0349  128 SER   B OG  
5814 N N   . ALA   B 129 ? 0.1820 0.1454 0.2479 0.0304  -0.0130 0.0068  129 ALA   B N   
5815 C CA  . ALA   B 129 ? 0.1996 0.1550 0.2649 0.0294  -0.0154 -0.0026 129 ALA   B CA  
5816 C C   . ALA   B 129 ? 0.1905 0.1495 0.2484 0.0233  0.0038  0.0006  129 ALA   B C   
5817 O O   . ALA   B 129 ? 0.1703 0.1561 0.2552 0.0206  -0.0066 0.0050  129 ALA   B O   
5818 C CB  . ALA   B 129 ? 0.2252 0.1742 0.2990 0.0315  -0.0029 -0.0058 129 ALA   B CB  
5824 N N   . GLY   B 130 ? 0.1889 0.1422 0.2532 0.0268  0.0107  -0.0048 130 GLY   B N   
5825 C CA  . GLY   B 130 ? 0.1907 0.1507 0.2571 0.0189  0.0281  -0.0026 130 GLY   B CA  
5826 C C   . GLY   B 130 ? 0.1919 0.1528 0.2490 0.0118  0.0158  0.0067  130 GLY   B C   
5827 O O   . GLY   B 130 ? 0.2084 0.1671 0.2511 0.0152  0.0054  0.0213  130 GLY   B O   
5831 N N   . ILE   B 131 ? 0.1822 0.1672 0.2598 0.0276  0.0108  0.0066  131 ILE   B N   
5832 C CA  . ILE   B 131 ? 0.2028 0.1783 0.2635 0.0285  -0.0023 0.0143  131 ILE   B CA  
5833 C C   . ILE   B 131 ? 0.2145 0.1736 0.2310 0.0177  -0.0032 0.0148  131 ILE   B C   
5834 O O   . ILE   B 131 ? 0.2443 0.1930 0.2403 0.0254  -0.0119 0.0207  131 ILE   B O   
5835 C CB  . ILE   B 131 ? 0.2046 0.2159 0.3095 0.0260  -0.0047 0.0193  131 ILE   B CB  
5836 C CG1 . ILE   B 131 ? 0.2041 0.2348 0.3281 0.0035  0.0004  0.0214  131 ILE   B CG1 
5837 C CG2 . ILE   B 131 ? 0.2047 0.2344 0.3279 0.0357  -0.0027 0.0169  131 ILE   B CG2 
5838 C CD1 . ILE   B 131 ? 0.2102 0.2544 0.3412 -0.0209 -0.0080 0.0324  131 ILE   B CD1 
5850 N N   . PHE   B 132 ? 0.2004 0.1527 0.2151 0.0121  0.0091  0.0192  132 PHE   B N   
5851 C CA  . PHE   B 132 ? 0.2095 0.1606 0.2257 0.0076  0.0276  0.0108  132 PHE   B CA  
5852 C C   . PHE   B 132 ? 0.2290 0.1768 0.2396 0.0066  0.0390  0.0148  132 PHE   B C   
5853 O O   . PHE   B 132 ? 0.2512 0.1943 0.2606 0.0018  0.0584  0.0187  132 PHE   B O   
5854 C CB  . PHE   B 132 ? 0.1890 0.1588 0.2062 0.0116  0.0257  0.0208  132 PHE   B CB  
5855 C CG  . PHE   B 132 ? 0.1898 0.1643 0.2077 0.0184  0.0178  0.0222  132 PHE   B CG  
5856 C CD1 . PHE   B 132 ? 0.2022 0.1596 0.2443 0.0113  0.0225  0.0239  132 PHE   B CD1 
5857 C CD2 . PHE   B 132 ? 0.1895 0.1666 0.1887 0.0237  0.0159  0.0252  132 PHE   B CD2 
5858 C CE1 . PHE   B 132 ? 0.2047 0.1673 0.2506 0.0040  0.0179  0.0245  132 PHE   B CE1 
5859 C CE2 . PHE   B 132 ? 0.1957 0.1734 0.1916 0.0202  0.0090  0.0159  132 PHE   B CE2 
5860 C CZ  . PHE   B 132 ? 0.2024 0.1711 0.2316 0.0102  -0.0008 0.0294  132 PHE   B CZ  
5870 N N   . GLY   B 133 ? 0.2222 0.1657 0.2338 0.0002  0.0263  0.0392  133 GLY   B N   
5871 C CA  . GLY   B 133 ? 0.2325 0.1770 0.2474 -0.0174 0.0239  0.0486  133 GLY   B CA  
5872 C C   . GLY   B 133 ? 0.2352 0.1827 0.2342 -0.0301 0.0335  0.0474  133 GLY   B C   
5873 O O   . GLY   B 133 ? 0.2611 0.1969 0.2829 -0.0445 0.0243  0.0588  133 GLY   B O   
5877 N N   . ALA   B 134 ? 0.2176 0.1863 0.2193 -0.0264 0.0351  0.0251  134 ALA   B N   
5878 C CA  . ALA   B 134 ? 0.2155 0.1821 0.2388 -0.0178 0.0408  0.0152  134 ALA   B CA  
5879 C C   . ALA   B 134 ? 0.2200 0.1694 0.2395 -0.0173 0.0388  0.0312  134 ALA   B C   
5880 O O   . ALA   B 134 ? 0.2257 0.1871 0.2574 -0.0015 0.0305  0.0231  134 ALA   B O   
5881 C CB  . ALA   B 134 ? 0.2185 0.1821 0.2611 -0.0138 0.0348  -0.0007 134 ALA   B CB  
5887 N N   . ASP   B 135 ? 0.2360 0.1618 0.2473 -0.0167 0.0228  0.0295  135 ASP   B N   
5888 C CA  . ASP   B 135 ? 0.2557 0.1556 0.2681 -0.0071 0.0041  0.0297  135 ASP   B CA  
5889 C C   . ASP   B 135 ? 0.2340 0.1464 0.2460 -0.0026 -0.0012 0.0198  135 ASP   B C   
5890 O O   . ASP   B 135 ? 0.2241 0.1429 0.2658 -0.0057 0.0110  0.0267  135 ASP   B O   
5891 C CB  . ASP   B 135 ? 0.2871 0.1704 0.2969 -0.0257 0.0066  0.0332  135 ASP   B CB  
5892 C CG  . ASP   B 135 ? 0.3145 0.1717 0.3383 -0.0499 0.0089  0.0338  135 ASP   B CG  
5893 O OD1 . ASP   B 135 ? 0.3221 0.1496 0.3312 -0.0216 -0.0054 0.0312  135 ASP   B OD1 
5894 O OD2 . ASP   B 135 ? 0.3395 0.2103 0.3939 -0.0714 0.0120  0.0185  135 ASP   B OD2 
5899 N N   . PRO   B 136 ? 0.2276 0.1468 0.2559 0.0178  -0.0137 0.0154  136 PRO   B N   
5900 C CA  . PRO   B 136 ? 0.2044 0.1355 0.2558 0.0153  -0.0154 0.0102  136 PRO   B CA  
5901 C C   . PRO   B 136 ? 0.1890 0.1279 0.2653 0.0145  -0.0093 0.0089  136 PRO   B C   
5902 O O   . PRO   B 136 ? 0.1681 0.1340 0.2626 0.0100  -0.0075 0.0123  136 PRO   B O   
5903 C CB  . PRO   B 136 ? 0.2031 0.1648 0.2592 0.0287  -0.0205 0.0004  136 PRO   B CB  
5904 C CG  . PRO   B 136 ? 0.2285 0.1733 0.2825 0.0309  -0.0133 0.0014  136 PRO   B CG  
5905 C CD  . PRO   B 136 ? 0.2354 0.1637 0.2731 0.0375  -0.0051 0.0119  136 PRO   B CD  
5913 N N   . ILE   B 137 ? 0.2020 0.1225 0.2682 0.0103  -0.0082 0.0082  137 ILE   B N   
5914 C CA  . ILE   B 137 ? 0.2073 0.1186 0.2909 -0.0048 -0.0067 0.0078  137 ILE   B CA  
5915 C C   . ILE   B 137 ? 0.1957 0.1315 0.2803 -0.0076 0.0064  0.0153  137 ILE   B C   
5916 O O   . ILE   B 137 ? 0.1844 0.1334 0.2696 -0.0092 -0.0025 0.0130  137 ILE   B O   
5917 C CB  . ILE   B 137 ? 0.2258 0.1338 0.3269 -0.0075 -0.0061 0.0106  137 ILE   B CB  
5918 C CG1 . ILE   B 137 ? 0.2472 0.1504 0.3682 0.0093  -0.0008 -0.0071 137 ILE   B CG1 
5919 C CG2 . ILE   B 137 ? 0.2309 0.1376 0.3374 -0.0307 -0.0075 0.0113  137 ILE   B CG2 
5920 C CD1 . ILE   B 137 ? 0.2731 0.1801 0.4095 0.0202  -0.0061 -0.0013 137 ILE   B CD1 
5932 N N   . HIS   B 138 ? 0.1991 0.1260 0.2739 -0.0081 0.0162  0.0140  138 HIS   B N   
5933 C CA  . HIS   B 138 ? 0.2073 0.1392 0.2716 -0.0053 0.0241  0.0090  138 HIS   B CA  
5934 C C   . HIS   B 138 ? 0.1886 0.1359 0.2575 -0.0031 0.0266  0.0212  138 HIS   B C   
5935 O O   . HIS   B 138 ? 0.1757 0.1379 0.2878 -0.0001 0.0275  0.0350  138 HIS   B O   
5936 C CB  . HIS   B 138 ? 0.2293 0.1578 0.2755 -0.0106 0.0418  -0.0024 138 HIS   B CB  
5937 C CG  . HIS   B 138 ? 0.2451 0.1762 0.2796 -0.0075 0.0599  0.0227  138 HIS   B CG  
5938 N ND1 . HIS   B 138 ? 0.2549 0.1927 0.3092 -0.0090 0.0708  0.0160  138 HIS   B ND1 
5939 C CD2 . HIS   B 138 ? 0.2581 0.1856 0.2731 -0.0101 0.0667  0.0199  138 HIS   B CD2 
5940 C CE1 . HIS   B 138 ? 0.2596 0.1950 0.3000 -0.0089 0.0711  0.0222  138 HIS   B CE1 
5941 N NE2 . HIS   B 138 ? 0.2651 0.1829 0.2790 -0.0048 0.0710  0.0196  138 HIS   B NE2 
5949 N N   . SER   B 139 ? 0.1839 0.1264 0.2407 0.0014  0.0197  0.0112  139 SER   B N   
5950 C CA  . SER   B 139 ? 0.1799 0.1179 0.2268 0.0025  0.0147  0.0092  139 SER   B CA  
5951 C C   . SER   B 139 ? 0.1561 0.1149 0.2372 -0.0013 0.0147  0.0077  139 SER   B C   
5952 O O   . SER   B 139 ? 0.1521 0.1192 0.2413 0.0007  0.0065  0.0052  139 SER   B O   
5953 C CB  . SER   B 139 ? 0.1874 0.1223 0.2399 0.0032  0.0005  0.0048  139 SER   B CB  
5954 O OG  . SER   B 139 ? 0.1874 0.1227 0.2436 -0.0005 -0.0127 0.0149  139 SER   B OG  
5960 N N   . LEU   B 140 ? 0.1567 0.1109 0.2354 -0.0026 0.0124  0.0006  140 LEU   B N   
5961 C CA  . LEU   B 140 ? 0.1509 0.1136 0.2300 -0.0018 0.0050  0.0072  140 LEU   B CA  
5962 C C   . LEU   B 140 ? 0.1400 0.1178 0.2519 -0.0046 -0.0016 0.0020  140 LEU   B C   
5963 O O   . LEU   B 140 ? 0.1427 0.1288 0.2521 -0.0029 0.0016  0.0083  140 LEU   B O   
5964 C CB  . LEU   B 140 ? 0.1460 0.1166 0.2428 -0.0124 0.0051  -0.0024 140 LEU   B CB  
5965 C CG  . LEU   B 140 ? 0.1614 0.1189 0.2399 -0.0146 -0.0042 0.0064  140 LEU   B CG  
5966 C CD1 . LEU   B 140 ? 0.1654 0.1320 0.2602 -0.0200 0.0097  0.0106  140 LEU   B CD1 
5967 C CD2 . LEU   B 140 ? 0.1767 0.1314 0.2458 -0.0085 0.0055  -0.0034 140 LEU   B CD2 
5979 N N   . ARG   B 141 ? 0.1356 0.1208 0.2604 -0.0088 0.0037  0.0043  141 ARG   B N   
5980 C CA  . ARG   B 141 ? 0.1449 0.1192 0.2962 -0.0162 0.0173  0.0043  141 ARG   B CA  
5981 C C   . ARG   B 141 ? 0.1391 0.1197 0.2823 -0.0153 0.0098  0.0026  141 ARG   B C   
5982 O O   . ARG   B 141 ? 0.1451 0.1260 0.2769 -0.0135 -0.0029 -0.0089 141 ARG   B O   
5983 C CB  . ARG   B 141 ? 0.1585 0.1354 0.3257 -0.0205 0.0311  -0.0049 141 ARG   B CB  
5984 C CG  . ARG   B 141 ? 0.1961 0.1554 0.3579 -0.0184 0.0308  0.0014  141 ARG   B CG  
5985 C CD  . ARG   B 141 ? 0.2412 0.1798 0.3660 -0.0092 0.0105  -0.0123 141 ARG   B CD  
5986 N NE  . ARG   B 141 ? 0.2694 0.1857 0.3559 -0.0273 0.0160  -0.0179 141 ARG   B NE  
5987 C CZ  . ARG   B 141 ? 0.2846 0.1675 0.3314 -0.0265 0.0254  -0.0321 141 ARG   B CZ  
5988 N NH1 . ARG   B 141 ? 0.2997 0.1582 0.3206 -0.0244 0.0235  -0.0315 141 ARG   B NH1 
5989 N NH2 . ARG   B 141 ? 0.2903 0.1761 0.3437 -0.0159 0.0137  -0.0132 141 ARG   B NH2 
6003 N N   . VAL   B 142 ? 0.1380 0.1209 0.2603 -0.0102 0.0079  -0.0029 142 VAL   B N   
6004 C CA  . VAL   B 142 ? 0.1420 0.1198 0.2519 -0.0067 0.0152  -0.0019 142 VAL   B CA  
6005 C C   . VAL   B 142 ? 0.1362 0.1188 0.2475 -0.0025 0.0083  -0.0057 142 VAL   B C   
6006 O O   . VAL   B 142 ? 0.1473 0.1192 0.2650 0.0014  0.0122  -0.0003 142 VAL   B O   
6007 C CB  . VAL   B 142 ? 0.1559 0.1351 0.2617 -0.0016 0.0136  0.0100  142 VAL   B CB  
6008 C CG1 . VAL   B 142 ? 0.1482 0.1325 0.2591 0.0010  0.0140  0.0058  142 VAL   B CG1 
6009 C CG2 . VAL   B 142 ? 0.1795 0.1349 0.2602 0.0033  0.0129  0.0183  142 VAL   B CG2 
6019 N N   . CYS   B 143 ? 0.1338 0.1186 0.2317 -0.0010 -0.0000 0.0055  143 CYS   B N   
6020 C CA  . CYS   B 143 ? 0.1316 0.1198 0.2350 -0.0066 0.0005  -0.0013 143 CYS   B CA  
6021 C C   . CYS   B 143 ? 0.1322 0.1264 0.2310 -0.0074 0.0006  -0.0079 143 CYS   B C   
6022 O O   . CYS   B 143 ? 0.1352 0.1286 0.2395 -0.0050 -0.0084 0.0030  143 CYS   B O   
6023 C CB  . CYS   B 143 ? 0.1380 0.1320 0.2349 -0.0053 0.0003  0.0011  143 CYS   B CB  
6024 S SG  . CYS   B 143 ? 0.1432 0.1441 0.2249 -0.0044 0.0038  0.0062  143 CYS   B SG  
6030 N N   . VAL   B 144 ? 0.1374 0.1264 0.2448 -0.0052 -0.0018 -0.0192 144 VAL   B N   
6031 C CA  . VAL   B 144 ? 0.1426 0.1337 0.2667 -0.0147 -0.0140 -0.0225 144 VAL   B CA  
6032 C C   . VAL   B 144 ? 0.1395 0.1351 0.2766 -0.0129 -0.0143 -0.0013 144 VAL   B C   
6033 O O   . VAL   B 144 ? 0.1478 0.1545 0.2915 0.0024  -0.0139 0.0176  144 VAL   B O   
6034 C CB  . VAL   B 144 ? 0.1645 0.1504 0.3406 -0.0093 -0.0276 -0.0374 144 VAL   B CB  
6035 C CG1 . VAL   B 144 ? 0.1975 0.1980 0.3774 -0.0074 -0.0278 -0.0347 144 VAL   B CG1 
6036 C CG2 . VAL   B 144 ? 0.1724 0.1530 0.3448 0.0058  -0.0367 -0.0460 144 VAL   B CG2 
6046 N N   . ASP   B 145 ? 0.1395 0.1312 0.2849 -0.0072 -0.0110 -0.0187 145 ASP   B N   
6047 C CA  . ASP   B 145 ? 0.1381 0.1324 0.3052 -0.0064 0.0049  -0.0024 145 ASP   B CA  
6048 C C   . ASP   B 145 ? 0.1335 0.1420 0.2830 -0.0064 0.0036  -0.0040 145 ASP   B C   
6049 O O   . ASP   B 145 ? 0.1327 0.1577 0.3195 -0.0132 0.0059  -0.0227 145 ASP   B O   
6050 C CB  . ASP   B 145 ? 0.1533 0.1458 0.3494 -0.0147 0.0172  0.0005  145 ASP   B CB  
6051 C CG  . ASP   B 145 ? 0.1719 0.1485 0.3872 -0.0209 0.0240  -0.0057 145 ASP   B CG  
6052 O OD1 . ASP   B 145 ? 0.1738 0.1445 0.3881 -0.0237 -0.0106 -0.0157 145 ASP   B OD1 
6053 O OD2 . ASP   B 145 ? 0.1989 0.1587 0.4304 -0.0228 0.0484  -0.0021 145 ASP   B OD2 
6058 N N   . THR   B 146 ? 0.1245 0.1282 0.2408 -0.0087 -0.0051 0.0055  146 THR   B N   
6059 C CA  . THR   B 146 ? 0.1347 0.1245 0.2289 -0.0046 0.0005  -0.0059 146 THR   B CA  
6060 C C   . THR   B 146 ? 0.1355 0.1235 0.2179 -0.0053 0.0004  0.0033  146 THR   B C   
6061 O O   . THR   B 146 ? 0.1400 0.1266 0.2363 -0.0048 -0.0120 0.0055  146 THR   B O   
6062 C CB  . THR   B 146 ? 0.1444 0.1289 0.2380 -0.0025 0.0080  0.0021  146 THR   B CB  
6063 O OG1 . THR   B 146 ? 0.1462 0.1264 0.2477 -0.0053 0.0110  0.0182  146 THR   B OG1 
6064 C CG2 . THR   B 146 ? 0.1522 0.1345 0.2416 0.0010  0.0083  -0.0008 146 THR   B CG2 
6072 N N   . VAL   B 147 ? 0.1428 0.1306 0.2018 -0.0039 0.0076  0.0058  147 VAL   B N   
6073 C CA  . VAL   B 147 ? 0.1406 0.1249 0.2006 -0.0103 -0.0065 0.0027  147 VAL   B CA  
6074 C C   . VAL   B 147 ? 0.1349 0.1227 0.2215 -0.0149 -0.0080 -0.0025 147 VAL   B C   
6075 O O   . VAL   B 147 ? 0.1527 0.1337 0.2348 -0.0181 -0.0321 -0.0111 147 VAL   B O   
6076 C CB  . VAL   B 147 ? 0.1391 0.1417 0.1987 -0.0049 -0.0104 0.0014  147 VAL   B CB  
6077 C CG1 . VAL   B 147 ? 0.1406 0.1533 0.1902 -0.0137 -0.0050 0.0036  147 VAL   B CG1 
6078 C CG2 . VAL   B 147 ? 0.1467 0.1373 0.1995 -0.0068 -0.0013 0.0027  147 VAL   B CG2 
6088 N N   . ARG   B 148 ? 0.1359 0.1217 0.2254 -0.0085 -0.0189 -0.0024 148 ARG   B N   
6089 C CA  . ARG   B 148 ? 0.1454 0.1328 0.2111 -0.0004 -0.0291 -0.0069 148 ARG   B CA  
6090 C C   . ARG   B 148 ? 0.1500 0.1443 0.1931 -0.0045 -0.0315 -0.0009 148 ARG   B C   
6091 O O   . ARG   B 148 ? 0.1700 0.1766 0.1927 -0.0245 -0.0407 0.0054  148 ARG   B O   
6092 C CB  . ARG   B 148 ? 0.1454 0.1420 0.2107 -0.0008 -0.0360 -0.0132 148 ARG   B CB  
6093 C CG  . ARG   B 148 ? 0.1431 0.1579 0.2276 -0.0086 -0.0331 -0.0244 148 ARG   B CG  
6094 C CD  . ARG   B 148 ? 0.1541 0.1776 0.2339 0.0042  -0.0263 -0.0248 148 ARG   B CD  
6095 N NE  . ARG   B 148 ? 0.1616 0.1716 0.2262 0.0185  -0.0373 -0.0221 148 ARG   B NE  
6096 C CZ  . ARG   B 148 ? 0.1474 0.1688 0.2158 0.0144  -0.0324 -0.0150 148 ARG   B CZ  
6097 N NH1 . ARG   B 148 ? 0.1391 0.1768 0.2261 0.0006  -0.0151 -0.0099 148 ARG   B NH1 
6098 N NH2 . ARG   B 148 ? 0.1702 0.1519 0.2074 0.0167  -0.0257 -0.0138 148 ARG   B NH2 
6112 N N   . THR   B 149 ? 0.1480 0.1358 0.2046 -0.0061 -0.0273 0.0022  149 THR   B N   
6113 C CA  . THR   B 149 ? 0.1537 0.1360 0.2047 -0.0139 -0.0308 0.0085  149 THR   B CA  
6114 C C   . THR   B 149 ? 0.1546 0.1313 0.1997 -0.0157 -0.0322 0.0020  149 THR   B C   
6115 O O   . THR   B 149 ? 0.1645 0.1381 0.1983 -0.0185 -0.0195 0.0002  149 THR   B O   
6116 C CB  . THR   B 149 ? 0.1558 0.1337 0.2074 -0.0109 -0.0352 0.0054  149 THR   B CB  
6117 O OG1 . THR   B 149 ? 0.1564 0.1390 0.1933 -0.0181 -0.0313 0.0021  149 THR   B OG1 
6118 C CG2 . THR   B 149 ? 0.1625 0.1407 0.2087 -0.0033 -0.0280 0.0048  149 THR   B CG2 
6126 N N   . ASN   B 150 ? 0.1605 0.1296 0.1880 -0.0169 -0.0398 -0.0039 150 ASN   B N   
6127 C CA  . ASN   B 150 ? 0.1700 0.1504 0.1808 -0.0225 -0.0336 -0.0047 150 ASN   B CA  
6128 C C   . ASN   B 150 ? 0.1535 0.1457 0.1909 -0.0144 -0.0297 -0.0020 150 ASN   B C   
6129 O O   . ASN   B 150 ? 0.1646 0.1455 0.2081 -0.0290 -0.0463 0.0039  150 ASN   B O   
6130 C CB  . ASN   B 150 ? 0.1940 0.1851 0.2010 -0.0237 -0.0405 0.0155  150 ASN   B CB  
6131 C CG  . ASN   B 150 ? 0.2154 0.2248 0.2366 -0.0240 -0.0394 0.0332  150 ASN   B CG  
6132 O OD1 . ASN   B 150 ? 0.2219 0.2381 0.2498 -0.0337 -0.0564 0.0304  150 ASN   B OD1 
6133 N ND2 . ASN   B 150 ? 0.2300 0.2474 0.2655 -0.0135 -0.0485 0.0703  150 ASN   B ND2 
6140 N N   . VAL   B 151 ? 0.1441 0.1453 0.1797 -0.0167 -0.0323 0.0060  151 VAL   B N   
6141 C CA  . VAL   B 151 ? 0.1480 0.1467 0.1795 -0.0249 -0.0262 0.0004  151 VAL   B CA  
6142 C C   . VAL   B 151 ? 0.1531 0.1384 0.1788 -0.0266 -0.0360 -0.0105 151 VAL   B C   
6143 O O   . VAL   B 151 ? 0.1630 0.1486 0.1934 -0.0243 -0.0246 -0.0193 151 VAL   B O   
6144 C CB  . VAL   B 151 ? 0.1704 0.1593 0.1915 -0.0097 -0.0281 0.0051  151 VAL   B CB  
6145 C CG1 . VAL   B 151 ? 0.1809 0.1613 0.2288 -0.0185 -0.0137 -0.0039 151 VAL   B CG1 
6146 C CG2 . VAL   B 151 ? 0.1944 0.1779 0.1814 0.0068  -0.0267 0.0213  151 VAL   B CG2 
6156 N N   . TYR   B 152 ? 0.1485 0.1216 0.1805 -0.0278 -0.0252 -0.0058 152 TYR   B N   
6157 C CA  . TYR   B 152 ? 0.1525 0.1401 0.1681 -0.0252 -0.0075 -0.0044 152 TYR   B CA  
6158 C C   . TYR   B 152 ? 0.1487 0.1298 0.1539 -0.0158 -0.0160 -0.0104 152 TYR   B C   
6159 O O   . TYR   B 152 ? 0.1559 0.1294 0.1681 -0.0213 -0.0099 -0.0019 152 TYR   B O   
6160 C CB  . TYR   B 152 ? 0.1672 0.1606 0.1597 -0.0262 -0.0152 0.0021  152 TYR   B CB  
6161 C CG  . TYR   B 152 ? 0.1800 0.1683 0.1576 -0.0404 -0.0206 -0.0014 152 TYR   B CG  
6162 C CD1 . TYR   B 152 ? 0.1913 0.1736 0.1464 -0.0281 -0.0323 -0.0014 152 TYR   B CD1 
6163 C CD2 . TYR   B 152 ? 0.2103 0.1859 0.1579 -0.0376 -0.0168 -0.0069 152 TYR   B CD2 
6164 C CE1 . TYR   B 152 ? 0.2092 0.1910 0.1584 -0.0242 -0.0394 0.0173  152 TYR   B CE1 
6165 C CE2 . TYR   B 152 ? 0.2211 0.2015 0.1552 -0.0329 -0.0221 -0.0105 152 TYR   B CE2 
6166 C CZ  . TYR   B 152 ? 0.2223 0.2107 0.1475 -0.0316 -0.0526 0.0130  152 TYR   B CZ  
6167 O OH  . TYR   B 152 ? 0.2454 0.2483 0.1950 -0.0194 -0.0466 0.0145  152 TYR   B OH  
6177 N N   . LEU   B 153 ? 0.1501 0.1226 0.1665 -0.0215 -0.0151 -0.0048 153 LEU   B N   
6178 C CA  . LEU   B 153 ? 0.1550 0.1194 0.1568 -0.0170 -0.0062 -0.0057 153 LEU   B CA  
6179 C C   . LEU   B 153 ? 0.1551 0.1209 0.1669 -0.0221 -0.0094 -0.0175 153 LEU   B C   
6180 O O   . LEU   B 153 ? 0.1655 0.1430 0.1756 -0.0109 -0.0140 -0.0330 153 LEU   B O   
6181 C CB  . LEU   B 153 ? 0.1558 0.1216 0.1653 -0.0156 -0.0013 -0.0054 153 LEU   B CB  
6182 C CG  . LEU   B 153 ? 0.1477 0.1333 0.1930 -0.0212 -0.0032 -0.0015 153 LEU   B CG  
6183 C CD1 . LEU   B 153 ? 0.1571 0.1484 0.2052 -0.0265 0.0054  0.0036  153 LEU   B CD1 
6184 C CD2 . LEU   B 153 ? 0.1522 0.1439 0.1918 -0.0208 0.0087  0.0028  153 LEU   B CD2 
6196 N N   . ALA   B 154 ? 0.1513 0.1215 0.1809 -0.0084 -0.0207 -0.0107 154 ALA   B N   
6197 C CA  . ALA   B 154 ? 0.1609 0.1353 0.2015 -0.0008 -0.0204 -0.0178 154 ALA   B CA  
6198 C C   . ALA   B 154 ? 0.1711 0.1411 0.2086 0.0080  -0.0273 -0.0273 154 ALA   B C   
6199 O O   . ALA   B 154 ? 0.2075 0.1420 0.2273 0.0101  -0.0148 -0.0124 154 ALA   B O   
6200 C CB  . ALA   B 154 ? 0.1600 0.1558 0.2255 -0.0032 -0.0124 -0.0235 154 ALA   B CB  
6206 N N   . VAL   B 155 ? 0.1381 0.1329 0.2099 -0.0014 -0.0069 -0.0139 155 VAL   B N   
6207 C CA  . VAL   B 155 ? 0.1405 0.1364 0.2247 -0.0019 -0.0132 -0.0039 155 VAL   B CA  
6208 C C   . VAL   B 155 ? 0.1395 0.1349 0.2077 0.0033  -0.0092 -0.0243 155 VAL   B C   
6209 O O   . VAL   B 155 ? 0.1599 0.1501 0.2395 0.0015  -0.0164 -0.0341 155 VAL   B O   
6210 C CB  . VAL   B 155 ? 0.1419 0.1532 0.2615 -0.0004 -0.0207 0.0033  155 VAL   B CB  
6211 C CG1 . VAL   B 155 ? 0.1453 0.1515 0.2607 -0.0017 -0.0147 0.0001  155 VAL   B CG1 
6212 C CG2 . VAL   B 155 ? 0.1436 0.1638 0.2841 -0.0102 -0.0172 0.0267  155 VAL   B CG2 
6222 N N   . PHE   B 156 ? 0.1316 0.1446 0.2375 0.0041  -0.0053 -0.0185 156 PHE   B N   
6223 C CA  . PHE   B 156 ? 0.1389 0.1563 0.2623 0.0080  -0.0088 -0.0149 156 PHE   B CA  
6224 C C   . PHE   B 156 ? 0.1384 0.1653 0.2872 0.0142  -0.0176 -0.0333 156 PHE   B C   
6225 O O   . PHE   B 156 ? 0.1611 0.1836 0.3142 0.0211  -0.0073 -0.0341 156 PHE   B O   
6226 C CB  . PHE   B 156 ? 0.1468 0.1531 0.2655 0.0025  -0.0107 -0.0133 156 PHE   B CB  
6227 C CG  . PHE   B 156 ? 0.1445 0.1586 0.2759 -0.0039 -0.0151 0.0092  156 PHE   B CG  
6228 C CD1 . PHE   B 156 ? 0.1489 0.1838 0.3146 0.0049  -0.0073 0.0410  156 PHE   B CD1 
6229 C CD2 . PHE   B 156 ? 0.1519 0.1667 0.2750 0.0034  -0.0214 0.0102  156 PHE   B CD2 
6230 C CE1 . PHE   B 156 ? 0.1517 0.1955 0.3259 0.0060  -0.0066 0.0395  156 PHE   B CE1 
6231 C CE2 . PHE   B 156 ? 0.1553 0.1886 0.3007 0.0106  -0.0148 0.0143  156 PHE   B CE2 
6232 C CZ  . PHE   B 156 ? 0.1487 0.1917 0.3256 0.0124  -0.0177 0.0240  156 PHE   B CZ  
6242 N N   . ASP   B 157 ? 0.1389 0.1515 0.3113 0.0158  -0.0317 -0.0116 157 ASP   B N   
6243 C CA  . ASP   B 157 ? 0.1587 0.1553 0.3412 0.0138  -0.0304 -0.0208 157 ASP   B CA  
6244 C C   . ASP   B 157 ? 0.1576 0.1533 0.3490 0.0085  -0.0286 -0.0453 157 ASP   B C   
6245 O O   . ASP   B 157 ? 0.1410 0.1498 0.3485 0.0069  -0.0292 -0.0314 157 ASP   B O   
6246 C CB  . ASP   B 157 ? 0.1882 0.1683 0.3569 0.0014  -0.0586 -0.0072 157 ASP   B CB  
6247 C CG  . ASP   B 157 ? 0.2301 0.1832 0.3853 -0.0004 -0.0537 -0.0077 157 ASP   B CG  
6248 O OD1 . ASP   B 157 ? 0.2374 0.1782 0.4058 0.0087  -0.0505 -0.0033 157 ASP   B OD1 
6249 O OD2 . ASP   B 157 ? 0.2644 0.2045 0.4110 -0.0031 -0.0343 -0.0064 157 ASP   B OD2 
6254 N N   . LYS   B 158 ? 0.1612 0.1829 0.3652 0.0024  -0.0034 -0.0681 158 LYS   B N   
6255 C CA  . LYS   B 158 ? 0.1772 0.1968 0.3706 0.0031  0.0007  -0.0840 158 LYS   B CA  
6256 C C   . LYS   B 158 ? 0.1738 0.1816 0.3748 0.0078  -0.0054 -0.0803 158 LYS   B C   
6257 O O   . LYS   B 158 ? 0.1763 0.1766 0.3813 -0.0095 -0.0040 -0.0872 158 LYS   B O   
6258 C CB  . LYS   B 158 ? 0.2060 0.2404 0.3677 0.0065  0.0088  -0.1059 158 LYS   B CB  
6259 C CG  . LYS   B 158 ? 0.2425 0.2795 0.3794 0.0130  0.0159  -0.1184 158 LYS   B CG  
6260 C CD  . LYS   B 158 ? 0.2645 0.3242 0.3998 0.0118  0.0243  -0.1093 158 LYS   B CD  
6261 C CE  . LYS   B 158 ? 0.2793 0.3551 0.4125 0.0143  0.0269  -0.1005 158 LYS   B CE  
6262 N NZ  . LYS   B 158 ? 0.2740 0.3714 0.4126 0.0112  0.0285  -0.0946 158 LYS   B NZ  
6276 N N   . ASN   B 159 ? 0.1738 0.1688 0.3935 0.0045  -0.0154 -0.0607 159 ASN   B N   
6277 C CA  . ASN   B 159 ? 0.1917 0.1631 0.4122 0.0165  -0.0257 -0.0468 159 ASN   B CA  
6278 C C   . ASN   B 159 ? 0.1707 0.1475 0.4031 0.0105  -0.0434 -0.0366 159 ASN   B C   
6279 O O   . ASN   B 159 ? 0.1731 0.1447 0.4154 -0.0021 -0.0429 -0.0328 159 ASN   B O   
6280 C CB  . ASN   B 159 ? 0.2102 0.1768 0.4357 0.0342  -0.0276 -0.0438 159 ASN   B CB  
6281 C CG  . ASN   B 159 ? 0.2369 0.2014 0.4616 0.0360  -0.0436 -0.0549 159 ASN   B CG  
6282 O OD1 . ASN   B 159 ? 0.2535 0.2102 0.4649 0.0451  -0.0431 -0.0658 159 ASN   B OD1 
6283 N ND2 . ASN   B 159 ? 0.2324 0.2126 0.4763 0.0380  -0.0569 -0.0451 159 ASN   B ND2 
6290 N N   . LEU   B 160 ? 0.1596 0.1462 0.3842 0.0074  -0.0407 -0.0339 160 LEU   B N   
6291 C CA  . LEU   B 160 ? 0.1605 0.1553 0.3418 0.0118  -0.0351 -0.0229 160 LEU   B CA  
6292 C C   . LEU   B 160 ? 0.1560 0.1445 0.3202 0.0005  -0.0269 -0.0264 160 LEU   B C   
6293 O O   . LEU   B 160 ? 0.1430 0.1485 0.3035 -0.0027 -0.0358 -0.0184 160 LEU   B O   
6294 C CB  . LEU   B 160 ? 0.1559 0.1582 0.3277 0.0065  -0.0379 -0.0137 160 LEU   B CB  
6295 C CG  . LEU   B 160 ? 0.1543 0.1713 0.3066 0.0059  -0.0340 -0.0051 160 LEU   B CG  
6296 C CD1 . LEU   B 160 ? 0.1644 0.1884 0.3066 -0.0067 -0.0215 -0.0036 160 LEU   B CD1 
6297 C CD2 . LEU   B 160 ? 0.1571 0.1766 0.2958 0.0240  -0.0307 -0.0100 160 LEU   B CD2 
6309 N N   . TYR   B 161 ? 0.1526 0.1506 0.3217 -0.0076 -0.0032 -0.0421 161 TYR   B N   
6310 C CA  . TYR   B 161 ? 0.1619 0.1489 0.3086 -0.0106 0.0143  -0.0474 161 TYR   B CA  
6311 C C   . TYR   B 161 ? 0.1663 0.1456 0.3023 -0.0106 0.0138  -0.0439 161 TYR   B C   
6312 O O   . TYR   B 161 ? 0.1684 0.1437 0.2895 -0.0156 0.0020  -0.0305 161 TYR   B O   
6313 C CB  . TYR   B 161 ? 0.1768 0.1596 0.3045 -0.0206 0.0354  -0.0551 161 TYR   B CB  
6314 C CG  . TYR   B 161 ? 0.2017 0.1631 0.3039 -0.0323 0.0426  -0.0609 161 TYR   B CG  
6315 C CD1 . TYR   B 161 ? 0.2120 0.1617 0.3001 -0.0434 0.0461  -0.0565 161 TYR   B CD1 
6316 C CD2 . TYR   B 161 ? 0.2246 0.1724 0.2934 -0.0313 0.0399  -0.0635 161 TYR   B CD2 
6317 C CE1 . TYR   B 161 ? 0.2332 0.1844 0.2985 -0.0444 0.0413  -0.0516 161 TYR   B CE1 
6318 C CE2 . TYR   B 161 ? 0.2468 0.1913 0.2965 -0.0399 0.0458  -0.0526 161 TYR   B CE2 
6319 C CZ  . TYR   B 161 ? 0.2476 0.1902 0.2953 -0.0512 0.0343  -0.0427 161 TYR   B CZ  
6320 O OH  . TYR   B 161 ? 0.2792 0.2140 0.3177 -0.0506 0.0298  -0.0416 161 TYR   B OH  
6330 N N   . ASP   B 162 ? 0.1680 0.1432 0.3247 -0.0104 -0.0005 -0.0528 162 ASP   B N   
6331 C CA  . ASP   B 162 ? 0.1766 0.1492 0.3244 -0.0032 -0.0024 -0.0496 162 ASP   B CA  
6332 C C   . ASP   B 162 ? 0.1693 0.1429 0.3141 -0.0104 -0.0076 -0.0430 162 ASP   B C   
6333 O O   . ASP   B 162 ? 0.1775 0.1478 0.3124 -0.0154 -0.0249 -0.0328 162 ASP   B O   
6334 C CB  . ASP   B 162 ? 0.2022 0.1666 0.3352 0.0050  -0.0107 -0.0668 162 ASP   B CB  
6335 C CG  . ASP   B 162 ? 0.2078 0.1913 0.3604 0.0127  -0.0067 -0.0807 162 ASP   B CG  
6336 O OD1 . ASP   B 162 ? 0.2020 0.2153 0.3454 0.0021  0.0029  -0.0705 162 ASP   B OD1 
6337 O OD2 . ASP   B 162 ? 0.2269 0.2196 0.4007 0.0275  0.0026  -0.0786 162 ASP   B OD2 
6342 N N   . LYS   B 163 ? 0.1701 0.1298 0.3101 -0.0103 -0.0267 -0.0289 163 LYS   B N   
6343 C CA  . LYS   B 163 ? 0.1822 0.1392 0.3084 -0.0190 -0.0226 -0.0075 163 LYS   B CA  
6344 C C   . LYS   B 163 ? 0.1539 0.1320 0.3010 -0.0220 -0.0181 -0.0077 163 LYS   B C   
6345 O O   . LYS   B 163 ? 0.1535 0.1473 0.3210 -0.0257 -0.0210 -0.0022 163 LYS   B O   
6346 C CB  . LYS   B 163 ? 0.2319 0.1874 0.3448 -0.0026 -0.0307 0.0134  163 LYS   B CB  
6347 C CG  . LYS   B 163 ? 0.3131 0.2691 0.4098 -0.0041 -0.0209 0.0188  163 LYS   B CG  
6348 C CD  . LYS   B 163 ? 0.3818 0.3368 0.4816 -0.0130 -0.0170 0.0121  163 LYS   B CD  
6349 C CE  . LYS   B 163 ? 0.4326 0.3902 0.5271 -0.0197 -0.0096 0.0098  163 LYS   B CE  
6350 N NZ  . LYS   B 163 ? 0.4652 0.4199 0.5564 -0.0236 -0.0061 0.0050  163 LYS   B NZ  
6364 N N   . LEU   B 164 ? 0.1423 0.1205 0.2926 -0.0149 -0.0160 -0.0087 164 LEU   B N   
6365 C CA  . LEU   B 164 ? 0.1441 0.1275 0.2705 -0.0103 -0.0272 -0.0063 164 LEU   B CA  
6366 C C   . LEU   B 164 ? 0.1487 0.1326 0.2686 -0.0173 -0.0306 0.0000  164 LEU   B C   
6367 O O   . LEU   B 164 ? 0.1523 0.1544 0.2781 -0.0124 -0.0276 -0.0026 164 LEU   B O   
6368 C CB  . LEU   B 164 ? 0.1351 0.1259 0.2538 -0.0049 -0.0214 -0.0035 164 LEU   B CB  
6369 C CG  . LEU   B 164 ? 0.1454 0.1466 0.2655 -0.0082 -0.0169 0.0045  164 LEU   B CG  
6370 C CD1 . LEU   B 164 ? 0.1551 0.1464 0.2621 -0.0159 -0.0211 -0.0009 164 LEU   B CD1 
6371 C CD2 . LEU   B 164 ? 0.1600 0.1858 0.2826 -0.0048 -0.0035 -0.0057 164 LEU   B CD2 
6383 N N   . VAL   B 165 ? 0.1834 0.1475 0.2848 -0.0233 -0.0346 -0.0074 165 VAL   B N   
6384 C CA  . VAL   B 165 ? 0.2147 0.1543 0.2851 -0.0262 -0.0573 -0.0073 165 VAL   B CA  
6385 C C   . VAL   B 165 ? 0.2432 0.1621 0.3138 -0.0368 -0.0854 -0.0128 165 VAL   B C   
6386 O O   . VAL   B 165 ? 0.2653 0.1789 0.3331 -0.0431 -0.0886 0.0096  165 VAL   B O   
6387 C CB  . VAL   B 165 ? 0.2436 0.1699 0.2808 -0.0145 -0.0311 -0.0172 165 VAL   B CB  
6388 C CG1 . VAL   B 165 ? 0.2592 0.1854 0.3109 -0.0184 -0.0170 -0.0131 165 VAL   B CG1 
6389 C CG2 . VAL   B 165 ? 0.2430 0.1778 0.2718 -0.0106 -0.0268 -0.0131 165 VAL   B CG2 
6399 N N   . SER   B 166 ? 0.2519 0.1517 0.3441 -0.0373 -0.0944 -0.0339 166 SER   B N   
6400 C CA  . SER   B 166 ? 0.2504 0.1581 0.3960 -0.0384 -0.0789 -0.0401 166 SER   B CA  
6401 C C   . SER   B 166 ? 0.2332 0.1684 0.4090 -0.0451 -0.0725 -0.0140 166 SER   B C   
6402 O O   . SER   B 166 ? 0.2339 0.1962 0.4366 -0.0521 -0.0933 -0.0361 166 SER   B O   
6403 C CB  . SER   B 166 ? 0.2519 0.1705 0.4208 -0.0309 -0.0715 -0.0507 166 SER   B CB  
6404 O OG  . SER   B 166 ? 0.2417 0.1691 0.4334 -0.0260 -0.0728 -0.0307 166 SER   B OG  
6410 N N   . SER   B 167 ? 0.2104 0.1619 0.3772 -0.0417 -0.0732 0.0342  167 SER   B N   
6411 C CA  . SER   B 167 ? 0.2048 0.1740 0.3721 -0.0341 -0.0543 0.0339  167 SER   B CA  
6412 C C   . SER   B 167 ? 0.1984 0.1848 0.3603 -0.0470 -0.0513 0.0526  167 SER   B C   
6413 O O   . SER   B 167 ? 0.1994 0.1971 0.3526 -0.0561 -0.0498 0.0525  167 SER   B O   
6414 C CB  . SER   B 167 ? 0.1969 0.1726 0.3785 -0.0331 -0.0286 0.0309  167 SER   B CB  
6415 O OG  . SER   B 167 ? 0.1904 0.1811 0.3699 -0.0213 -0.0152 0.0292  167 SER   B OG  
6421 N N   . PHE   B 168 ? 0.1955 0.1774 0.3548 -0.0413 -0.0348 0.0571  168 PHE   B N   
6422 C CA  . PHE   B 168 ? 0.2011 0.1692 0.3287 -0.0444 -0.0316 0.0367  168 PHE   B CA  
6423 C C   . PHE   B 168 ? 0.1767 0.1613 0.2861 -0.0266 -0.0134 0.0161  168 PHE   B C   
6424 O O   . PHE   B 168 ? 0.2135 0.1537 0.2856 -0.0024 -0.0129 0.0017  168 PHE   B O   
6425 C CB  . PHE   B 168 ? 0.2187 0.1798 0.3357 -0.0552 -0.0493 0.0503  168 PHE   B CB  
6426 C CG  . PHE   B 168 ? 0.2476 0.1678 0.3222 -0.0590 -0.0511 0.0282  168 PHE   B CG  
6427 C CD1 . PHE   B 168 ? 0.2800 0.1806 0.3247 -0.0511 -0.0625 0.0207  168 PHE   B CD1 
6428 C CD2 . PHE   B 168 ? 0.2307 0.1581 0.3185 -0.0588 -0.0459 0.0380  168 PHE   B CD2 
6429 C CE1 . PHE   B 168 ? 0.2913 0.1865 0.3166 -0.0401 -0.0516 0.0352  168 PHE   B CE1 
6430 C CE2 . PHE   B 168 ? 0.2623 0.1698 0.3230 -0.0382 -0.0536 0.0257  168 PHE   B CE2 
6431 C CZ  . PHE   B 168 ? 0.2802 0.1692 0.3167 -0.0271 -0.0602 0.0357  168 PHE   B CZ  
6441 N N   . LEU   B 169 ? 0.1825 0.1728 0.2782 -0.0004 0.0016  0.0024  169 LEU   B N   
6442 C CA  . LEU   B 169 ? 0.2088 0.1984 0.3034 -0.0115 0.0014  -0.0238 169 LEU   B CA  
6443 C C   . LEU   B 169 ? 0.2393 0.2301 0.3569 0.0050  -0.0093 -0.0494 169 LEU   B C   
6444 O O   . LEU   B 169 ? 0.2620 0.2542 0.4201 0.0050  -0.0115 -0.0656 169 LEU   B O   
6445 C CB  . LEU   B 169 ? 0.2331 0.2408 0.3056 -0.0196 -0.0077 -0.0001 169 LEU   B CB  
6446 C CG  . LEU   B 169 ? 0.2772 0.2815 0.3414 -0.0067 -0.0033 0.0060  169 LEU   B CG  
6447 C CD1 . LEU   B 169 ? 0.2894 0.2986 0.3392 -0.0084 -0.0045 0.0256  169 LEU   B CD1 
6448 C CD2 . LEU   B 169 ? 0.2768 0.2924 0.3416 0.0079  0.0119  -0.0075 169 LEU   B CD2 
6449 O OXT . LEU   B 169 ? 0.2584 0.2471 0.3495 0.0376  -0.0026 -0.0561 169 LEU   B OXT 
6461 C C1  T TFA   C .   ? 0.1520 0.1669 0.1214 -0.0219 0.0507  0.0075  201 TFA   A C1  
6462 C C2  T TFA   C .   ? 0.1691 0.1780 0.1529 -0.0283 0.0340  -0.0038 201 TFA   A C2  
6463 O O   T TFA   C .   ? 0.1248 0.1568 0.1173 -0.0224 0.0539  0.0152  201 TFA   A O   
6464 F F1  T TFA   C .   ? 0.1773 0.1766 0.1650 -0.0304 0.0219  -0.0023 201 TFA   A F1  
6465 F F2  T TFA   C .   ? 0.1736 0.1763 0.1473 -0.0286 0.0377  0.0092  201 TFA   A F2  
6466 F F3  T TFA   C .   ? 0.1800 0.1915 0.1847 -0.0320 0.0376  -0.0201 201 TFA   A F3  
6467 O OXT T TFA   C .   ? 0.1645 0.1741 0.1281 -0.0078 0.0550  0.0031  201 TFA   A OXT 
6468 N N2  B A1A8K D .   ? 0.2184 0.1880 0.1954 0.0222  -0.0213 -0.0058 202 A1A8K A N2  
6469 C C3  B A1A8K D .   ? 0.2840 0.2714 0.3086 0.0059  -0.0055 -0.0092 202 A1A8K A C3  
6470 C C6  B A1A8K D .   ? 0.2246 0.1984 0.2106 0.0189  -0.0223 -0.0048 202 A1A8K A C6  
6471 C C9  B A1A8K D .   ? 0.1988 0.1782 0.1830 0.0111  -0.0291 -0.0043 202 A1A8K A C9  
6472 C C1  B A1A8K D .   ? 0.2927 0.2843 0.3197 0.0111  -0.0021 -0.0121 202 A1A8K A C1  
6473 C C10 B A1A8K D .   ? 0.2004 0.1735 0.1766 -0.0047 -0.0379 -0.0003 202 A1A8K A C10 
6474 C C11 B A1A8K D .   ? 0.1910 0.1675 0.1761 0.0039  -0.0428 0.0087  202 A1A8K A C11 
6475 C C2  B A1A8K D .   ? 0.2800 0.2657 0.2978 0.0107  -0.0063 -0.0091 202 A1A8K A C2  
6476 C C4  B A1A8K D .   ? 0.2853 0.2718 0.3136 0.0065  -0.0088 -0.0050 202 A1A8K A C4  
6477 C C5  B A1A8K D .   ? 0.2750 0.2585 0.2944 0.0117  -0.0154 -0.0033 202 A1A8K A C5  
6478 C C7  B A1A8K D .   ? 0.2061 0.1834 0.1760 0.0226  -0.0154 -0.0085 202 A1A8K A C7  
6479 C C8  B A1A8K D .   ? 0.1897 0.1690 0.1736 0.0132  -0.0321 -0.0038 202 A1A8K A C8  
6480 N N1  B A1A8K D .   ? 0.2626 0.2390 0.2666 0.0175  -0.0150 -0.0045 202 A1A8K A N1  
6481 N N3  B A1A8K D .   ? 0.1997 0.1749 0.1718 0.0181  -0.0194 -0.0045 202 A1A8K A N3  
6482 N N4  B A1A8K D .   ? 0.1852 0.1636 0.1802 0.0081  -0.0487 0.0053  202 A1A8K A N4  
6483 O O1  B A1A8K D .   ? 0.2930 0.2883 0.3233 0.0157  0.0082  -0.0097 202 A1A8K A O1  
6484 O O2  B A1A8K D .   ? 0.2974 0.2850 0.3329 0.0028  -0.0042 -0.0056 202 A1A8K A O2  
6485 O O3  B A1A8K D .   ? 0.3004 0.2939 0.3363 0.0127  -0.0036 -0.0169 202 A1A8K A O3  
6497 O O   . HOH   E .   ? 0.4399 0.2196 0.2367 0.0633  -0.0114 0.0086  301 HOH   A O   
6498 O O   . HOH   E .   ? 0.4022 0.7533 0.5012 -0.1355 0.0265  0.0482  302 HOH   A O   
6499 O O   . HOH   E .   ? 0.4240 0.3607 0.5241 -0.0326 0.1609  -0.0558 303 HOH   A O   
6500 O O   A HOH   E .   ? 0.3461 0.2253 0.3273 -0.0297 -0.0310 0.0428  304 HOH   A O   
6501 O O   . HOH   E .   ? 0.6542 0.4797 0.3800 0.1799  -0.1210 0.0690  305 HOH   A O   
6502 O O   . HOH   E .   ? 0.5586 0.3546 0.5348 -0.0572 0.1593  0.0893  306 HOH   A O   
6503 O O   . HOH   E .   ? 0.6475 0.5401 0.4512 -0.1121 0.1708  0.1696  307 HOH   A O   
6504 O O   . HOH   E .   ? 0.3018 0.6455 0.5584 -0.0424 -0.0759 0.2038  308 HOH   A O   
6505 O O   . HOH   E .   ? 0.5206 0.6113 0.4700 -0.1494 -0.1131 -0.0877 309 HOH   A O   
6506 O O   . HOH   E .   ? 0.2499 0.3025 0.3197 -0.0508 0.0437  0.0834  310 HOH   A O   
6507 O O   . HOH   E .   ? 0.6353 0.4407 0.5893 0.0641  -0.1097 0.0116  311 HOH   A O   
6508 O O   . HOH   E .   ? 0.2247 0.1832 0.2484 0.0299  -0.0364 -0.0037 312 HOH   A O   
6509 O O   . HOH   E .   ? 0.6619 0.4287 0.5123 -0.1366 0.0303  0.1520  313 HOH   A O   
6510 O O   . HOH   E .   ? 0.8086 0.4344 0.6080 -0.0820 -0.1438 0.0526  314 HOH   A O   
6511 O O   . HOH   E .   ? 0.4401 0.6028 0.4718 0.1717  0.1024  -0.1109 315 HOH   A O   
6512 O O   B HOH   E .   ? 0.3020 0.3070 0.3047 -0.0575 0.0349  -0.0881 316 HOH   A O   
6513 O O   . HOH   E .   ? 0.2180 0.2471 0.3010 -0.0232 -0.0288 0.0822  317 HOH   A O   
6514 O O   . HOH   E .   ? 0.7341 0.5681 0.4313 -0.1144 0.0072  0.2116  318 HOH   A O   
6515 O O   . HOH   E .   ? 0.2116 0.1904 0.3429 -0.0393 0.0135  -0.0274 319 HOH   A O   
6516 O O   . HOH   E .   ? 0.4685 0.3161 0.3836 -0.0307 0.2022  0.0302  320 HOH   A O   
6517 O O   . HOH   E .   ? 0.2666 0.5331 0.4393 -0.0108 -0.0357 0.0980  321 HOH   A O   
6518 O O   . HOH   E .   ? 0.1951 0.3069 0.3132 0.0305  -0.0180 -0.0038 322 HOH   A O   
6519 O O   . HOH   E .   ? 0.3026 0.3056 0.1787 -0.0204 0.0518  0.0376  323 HOH   A O   
6520 O O   . HOH   E .   ? 0.3519 0.3616 0.3033 -0.1374 0.0220  0.0702  324 HOH   A O   
6521 O O   . HOH   E .   ? 0.6370 0.5078 0.3414 -0.0217 -0.0621 0.0705  325 HOH   A O   
6522 O O   . HOH   E .   ? 0.4257 0.3556 0.3191 -0.0705 -0.0774 -0.0032 326 HOH   A O   
6523 O O   A HOH   E .   ? 0.1443 0.2077 0.2360 0.0400  0.0380  0.0552  327 HOH   A O   
6524 O O   . HOH   E .   ? 0.3444 0.4482 0.2332 -0.0072 0.0511  0.0134  328 HOH   A O   
6525 O O   . HOH   E .   ? 0.1973 0.3449 0.4207 -0.0324 0.0267  -0.1023 329 HOH   A O   
6526 O O   . HOH   E .   ? 0.2882 0.2149 0.2788 -0.0302 0.0186  -0.0269 330 HOH   A O   
6527 O O   . HOH   E .   ? 0.4619 0.4875 0.4549 -0.0390 -0.1190 -0.1076 331 HOH   A O   
6528 O O   . HOH   E .   ? 0.6031 0.2180 0.5184 0.0730  -0.0313 -0.0025 332 HOH   A O   
6529 O O   . HOH   E .   ? 0.1544 0.1622 0.2341 -0.0199 0.0009  0.0103  333 HOH   A O   
6530 O O   . HOH   E .   ? 0.2427 0.2273 0.2836 0.0358  0.0208  0.0375  334 HOH   A O   
6531 O O   . HOH   E .   ? 0.1685 0.3614 0.3581 -0.0433 0.0664  0.0452  335 HOH   A O   
6532 O O   . HOH   E .   ? 0.2354 0.4355 0.3951 -0.0253 -0.0433 0.1453  336 HOH   A O   
6533 O O   . HOH   E .   ? 0.2733 0.3666 0.4231 -0.0641 -0.0688 -0.0658 337 HOH   A O   
6534 O O   . HOH   E .   ? 0.4533 0.2216 0.4457 0.0577  -0.0798 0.0496  338 HOH   A O   
6535 O O   . HOH   E .   ? 0.5705 0.5175 0.4766 -0.2089 -0.0846 0.2486  339 HOH   A O   
6536 O O   . HOH   E .   ? 0.3089 0.4436 0.5049 -0.0444 0.1432  -0.0287 340 HOH   A O   
6537 O O   . HOH   E .   ? 0.4349 0.4995 0.2356 -0.1568 0.0312  0.0654  341 HOH   A O   
6538 O O   . HOH   E .   ? 0.2363 0.4137 0.3738 0.1014  -0.0760 -0.0370 342 HOH   A O   
6539 O O   . HOH   E .   ? 0.5451 0.4753 0.4975 0.0616  0.2052  -0.0922 343 HOH   A O   
6540 O O   A HOH   E .   ? 0.2588 0.4571 0.2375 0.1294  -0.0003 -0.0300 344 HOH   A O   
6541 O O   . HOH   E .   ? 0.1939 0.1846 0.2462 0.0157  -0.0196 0.0256  345 HOH   A O   
6542 O O   . HOH   E .   ? 0.1490 0.2233 0.2317 0.0026  -0.0089 0.0501  346 HOH   A O   
6543 O O   A HOH   E .   ? 0.2684 0.2307 0.4003 -0.0201 -0.1038 0.0961  347 HOH   A O   
6544 O O   . HOH   E .   ? 0.3004 0.6002 0.6211 0.1044  0.0648  0.0799  348 HOH   A O   
6545 O O   . HOH   E .   ? 0.5689 0.6321 0.6051 -0.0516 0.1017  0.0141  349 HOH   A O   
6546 O O   . HOH   E .   ? 0.1897 0.2123 0.3656 0.0160  0.0836  -0.0142 350 HOH   A O   
6547 O O   . HOH   E .   ? 0.6224 0.3858 0.3014 -0.0204 0.0339  0.1089  351 HOH   A O   
6548 O O   . HOH   E .   ? 0.2090 0.1650 0.2641 0.0028  -0.0435 -0.0057 352 HOH   A O   
6549 O O   . HOH   E .   ? 0.2668 0.4199 0.3557 -0.0627 0.0340  -0.0052 353 HOH   A O   
6550 O O   . HOH   E .   ? 0.1378 0.1315 0.1552 -0.0056 0.0180  0.0046  354 HOH   A O   
6551 O O   . HOH   E .   ? 0.3891 0.4253 0.3798 0.1893  0.0837  0.0582  355 HOH   A O   
6552 O O   . HOH   E .   ? 0.1548 0.1942 0.2555 0.0116  -0.0169 0.0059  356 HOH   A O   
6553 O O   . HOH   E .   ? 0.1594 0.1329 0.2452 -0.0098 0.0224  -0.0118 357 HOH   A O   
6554 O O   . HOH   E .   ? 0.5456 0.4392 0.5479 0.0781  0.0953  -0.1355 358 HOH   A O   
6555 O O   . HOH   E .   ? 0.1651 0.1890 0.2675 0.0091  -0.0382 -0.0541 359 HOH   A O   
6556 O O   . HOH   E .   ? 0.3422 0.3049 0.3977 -0.0798 -0.0137 -0.0322 360 HOH   A O   
6557 O O   . HOH   E .   ? 0.3169 0.3434 0.4854 -0.0451 -0.1164 -0.0734 361 HOH   A O   
6558 O O   . HOH   E .   ? 0.3101 0.3547 0.2432 -0.0799 -0.0331 -0.0701 362 HOH   A O   
6559 O O   . HOH   E .   ? 0.2579 0.4787 0.4981 -0.0237 0.1118  0.1953  363 HOH   A O   
6560 O O   . HOH   E .   ? 0.5092 0.2525 0.4018 -0.1560 0.1681  -0.0528 364 HOH   A O   
6561 O O   . HOH   E .   ? 0.3623 0.7156 0.5042 -0.0470 -0.1597 0.0471  365 HOH   A O   
6562 O O   . HOH   E .   ? 0.1446 0.1669 0.1654 -0.0085 0.0016  -0.0092 366 HOH   A O   
6563 O O   . HOH   E .   ? 0.2719 0.3259 0.3549 -0.0941 0.0785  -0.0112 367 HOH   A O   
6564 O O   . HOH   E .   ? 0.3980 0.2358 0.4540 -0.1198 0.0806  0.0104  368 HOH   A O   
6565 O O   . HOH   E .   ? 0.1998 0.2783 0.3940 0.0183  0.0807  -0.0841 369 HOH   A O   
6566 O O   . HOH   E .   ? 0.2623 0.4180 0.3257 -0.0007 -0.0392 0.0600  370 HOH   A O   
6567 O O   . HOH   E .   ? 0.2728 0.4134 0.3260 0.0458  0.0852  0.1679  371 HOH   A O   
6568 O O   . HOH   E .   ? 0.1986 0.1951 0.2360 -0.0330 0.0061  0.0319  372 HOH   A O   
6569 O O   . HOH   E .   ? 0.3119 0.2941 0.3377 -0.0149 -0.0482 0.1025  373 HOH   A O   
6570 O O   . HOH   E .   ? 0.5264 0.5110 0.6454 -0.1235 -0.0637 0.1014  374 HOH   A O   
6571 O O   . HOH   E .   ? 0.2297 0.2275 0.3230 0.0079  -0.0057 0.0795  375 HOH   A O   
6572 O O   . HOH   E .   ? 0.3824 0.2125 0.2632 0.1043  0.0462  0.0207  376 HOH   A O   
6573 O O   . HOH   E .   ? 0.2150 0.2320 0.2335 -0.0370 -0.0447 0.0323  377 HOH   A O   
6574 O O   A HOH   E .   ? 0.5659 0.2559 0.2668 0.0828  0.0433  0.0826  378 HOH   A O   
6575 O O   . HOH   E .   ? 0.3939 0.5440 0.5896 0.1384  -0.0364 0.1199  379 HOH   A O   
6576 O O   . HOH   E .   ? 0.1846 0.1789 0.2478 -0.0281 0.0038  0.0382  380 HOH   A O   
6577 O O   . HOH   E .   ? 0.3135 0.3033 0.2059 0.0367  0.0621  0.0001  381 HOH   A O   
6578 O O   . HOH   E .   ? 0.1759 0.2125 0.2074 -0.0075 0.0065  0.0591  382 HOH   A O   
6579 O O   . HOH   E .   ? 0.2316 0.2115 0.2001 -0.0003 0.0209  0.0101  383 HOH   A O   
6580 O O   T HOH   E .   ? 0.1118 0.1258 0.2151 -0.0335 0.0103  0.0440  384 HOH   A O   
6581 O O   . HOH   E .   ? 0.3414 0.6146 0.3864 -0.0652 0.0381  0.0929  385 HOH   A O   
6582 O O   . HOH   E .   ? 0.1765 0.1721 0.2542 0.0046  -0.0410 0.0024  386 HOH   A O   
6583 O O   . HOH   E .   ? 0.1782 0.2749 0.2656 0.0362  0.0267  0.0852  387 HOH   A O   
6584 O O   . HOH   E .   ? 0.2539 0.1917 0.2942 -0.0178 0.0137  0.0285  388 HOH   A O   
6585 O O   . HOH   E .   ? 0.2644 0.2100 0.1858 -0.0697 0.0280  0.0211  389 HOH   A O   
6586 O O   B HOH   E .   ? 0.2343 0.2515 0.2242 0.0617  -0.0372 -0.0410 390 HOH   A O   
6587 O O   . HOH   E .   ? 0.3400 0.2586 0.5196 -0.0602 -0.0490 0.0019  391 HOH   A O   
6588 O O   . HOH   E .   ? 0.3041 0.6239 0.3417 0.0927  0.0634  -0.0811 392 HOH   A O   
6589 O O   . HOH   E .   ? 0.2009 0.1690 0.1527 0.0014  0.0175  0.0184  393 HOH   A O   
6590 O O   . HOH   E .   ? 0.1999 0.2757 0.3493 -0.0167 -0.0173 0.0060  394 HOH   A O   
6591 O O   . HOH   E .   ? 0.2602 0.3998 0.4170 -0.0498 0.1296  -0.0991 395 HOH   A O   
6592 O O   . HOH   E .   ? 0.4299 0.3299 0.2635 -0.0903 -0.0128 0.0151  396 HOH   A O   
6593 O O   . HOH   E .   ? 0.1459 0.1487 0.2098 0.0004  -0.0218 0.0029  397 HOH   A O   
6594 O O   A HOH   E .   ? 0.2335 0.2764 0.3118 -0.0460 0.0227  -0.0177 398 HOH   A O   
6595 O O   . HOH   E .   ? 0.3994 0.3757 0.2498 0.0270  -0.1113 0.0281  399 HOH   A O   
6596 O O   . HOH   E .   ? 0.1498 0.1811 0.2046 0.0274  -0.0436 -0.0424 400 HOH   A O   
6597 O O   . HOH   E .   ? 0.2847 0.3069 0.2343 -0.0699 -0.0706 0.0184  401 HOH   A O   
6598 O O   . HOH   E .   ? 0.1928 0.1795 0.3901 0.0307  0.1045  0.0849  402 HOH   A O   
6599 O O   . HOH   E .   ? 0.1805 0.1378 0.1812 -0.0209 0.0192  -0.0070 403 HOH   A O   
6600 O O   . HOH   E .   ? 0.2079 0.2103 0.3115 0.0065  -0.0399 0.0346  404 HOH   A O   
6601 O O   A HOH   E .   ? 0.1170 0.3241 0.2605 -0.0094 0.0190  0.0904  405 HOH   A O   
6602 O O   . HOH   E .   ? 0.5377 0.5947 0.4233 0.1699  -0.0280 -0.0204 406 HOH   A O   
6603 O O   . HOH   E .   ? 0.2196 0.1708 0.3159 0.0023  -0.0279 0.0136  407 HOH   A O   
6604 O O   . HOH   E .   ? 0.2550 0.2777 0.3481 -0.0047 -0.0176 -0.0498 408 HOH   A O   
6605 O O   . HOH   E .   ? 0.2007 0.2032 0.2842 0.0336  -0.0585 0.0317  409 HOH   A O   
6606 O O   . HOH   E .   ? 0.2246 0.2288 0.3322 0.0025  -0.0137 -0.0163 410 HOH   A O   
6607 O O   . HOH   E .   ? 0.2784 0.4011 0.6834 -0.0325 0.0919  -0.0481 411 HOH   A O   
6608 O O   . HOH   E .   ? 0.4696 0.4429 0.2232 -0.0301 0.0667  0.0792  412 HOH   A O   
6609 O O   . HOH   E .   ? 0.6506 0.6990 0.6703 -0.1269 -0.0240 -0.0777 413 HOH   A O   
6610 O O   . HOH   E .   ? 0.2683 0.3464 0.3335 -0.0403 0.0949  -0.0393 414 HOH   A O   
6611 O O   . HOH   E .   ? 0.4071 0.6103 0.4459 0.1362  0.0662  0.0921  415 HOH   A O   
6612 O O   . HOH   E .   ? 0.1568 0.1628 0.3154 0.0005  -0.0112 0.0236  416 HOH   A O   
6613 O O   . HOH   E .   ? 0.5302 0.3067 0.4679 0.0910  -0.0138 -0.0582 417 HOH   A O   
6614 O O   . HOH   E .   ? 0.5115 0.5744 0.3285 -0.0856 -0.0004 0.1091  418 HOH   A O   
6615 O O   . HOH   E .   ? 0.2432 0.2115 0.2981 -0.0534 -0.0069 0.0499  419 HOH   A O   
6616 O O   . HOH   E .   ? 0.4183 0.2322 0.5332 -0.0900 -0.2384 0.1098  420 HOH   A O   
6617 O O   . HOH   E .   ? 0.2234 0.3040 0.2507 -0.0079 -0.0522 0.0408  421 HOH   A O   
6618 O O   . HOH   E .   ? 0.4705 0.5753 0.4091 0.1622  -0.1257 -0.1708 422 HOH   A O   
6619 O O   . HOH   E .   ? 0.4952 0.3101 0.2699 -0.1149 0.0261  0.0453  423 HOH   A O   
6620 O O   . HOH   E .   ? 0.3303 0.1294 0.2207 0.0056  -0.0425 0.0084  424 HOH   A O   
6621 O O   . HOH   E .   ? 0.2281 0.3996 0.2615 0.1469  -0.0191 0.0100  425 HOH   A O   
6622 O O   B HOH   E .   ? 0.4178 0.3192 0.1710 0.0428  0.0288  -0.0100 426 HOH   A O   
6623 O O   B HOH   E .   ? 0.5102 0.2390 0.5428 0.0302  0.0487  0.0837  427 HOH   A O   
6624 O O   . HOH   E .   ? 0.2921 0.5957 0.1835 -0.0380 0.0433  0.0134  428 HOH   A O   
6625 O O   . HOH   E .   ? 0.5360 0.7151 0.4151 0.0358  0.2630  -0.0493 429 HOH   A O   
6626 O O   . HOH   E .   ? 0.6708 0.4144 0.4938 0.1940  -0.0951 0.1375  430 HOH   A O   
6627 O O   . HOH   E .   ? 0.5558 0.6478 0.5072 0.0338  0.0693  0.0300  431 HOH   A O   
6628 O O   . HOH   E .   ? 0.1640 0.2061 0.3126 -0.0231 -0.0152 0.0504  432 HOH   A O   
6629 O O   B HOH   E .   ? 0.1172 0.1502 0.3130 0.0040  0.0445  0.0484  433 HOH   A O   
6630 O O   . HOH   E .   ? 0.3957 0.3653 0.4133 0.1182  0.0168  0.0221  434 HOH   A O   
6631 O O   . HOH   E .   ? 0.5115 0.4933 0.3790 -0.0191 -0.1459 0.0321  435 HOH   A O   
6632 O O   . HOH   E .   ? 0.5314 0.6180 0.6360 -0.1526 -0.0663 -0.1239 436 HOH   A O   
6633 O O   . HOH   E .   ? 0.7079 0.6906 0.6546 0.0458  -0.0944 -0.0387 437 HOH   A O   
6634 O O   . HOH   E .   ? 0.9637 0.9478 0.7422 -0.0499 -0.0463 -0.1160 438 HOH   A O   
6635 O O   . HOH   E .   ? 0.1986 0.1528 0.2100 -0.0013 -0.0486 -0.0088 439 HOH   A O   
6636 O O   . HOH   E .   ? 0.3766 0.2795 0.1867 -0.0909 0.0239  0.0360  440 HOH   A O   
6637 O O   A HOH   E .   ? 0.2009 0.1506 0.2095 0.0104  -0.0319 -0.0169 441 HOH   A O   
6638 O O   . HOH   E .   ? 0.2335 0.1756 0.3076 0.0132  0.0098  0.0166  442 HOH   A O   
6639 O O   . HOH   E .   ? 0.4745 0.4439 0.5018 -0.0703 -0.1044 -0.1453 443 HOH   A O   
6640 O O   . HOH   E .   ? 0.3330 0.3423 0.5662 -0.0119 0.1391  -0.1516 444 HOH   A O   
6641 O O   A HOH   E .   ? 0.5461 0.4093 0.4228 -0.0894 0.0650  0.1564  445 HOH   A O   
6642 O O   . HOH   E .   ? 0.3856 0.3566 0.3235 0.2142  -0.0440 -0.0308 446 HOH   A O   
6643 O O   . HOH   E .   ? 0.5633 0.3611 0.6589 0.0524  0.0198  -0.0988 447 HOH   A O   
6644 O O   . HOH   E .   ? 0.1845 0.2118 0.5102 -0.0201 -0.0746 0.0675  448 HOH   A O   
6645 O O   A HOH   E .   ? 0.6833 0.4796 0.4153 0.1451  0.1335  0.1262  449 HOH   A O   
6646 O O   . HOH   E .   ? 0.6411 0.7651 0.4198 0.1865  -0.1191 0.1815  450 HOH   A O   
6647 O O   . HOH   E .   ? 0.6243 0.4812 0.7514 0.0991  -0.1299 0.1355  451 HOH   A O   
6648 O O   . HOH   E .   ? 0.2323 0.2788 0.2433 -0.0145 -0.0186 -0.0491 452 HOH   A O   
6649 O O   . HOH   E .   ? 0.2515 0.2013 0.3049 0.0226  0.0316  0.0215  453 HOH   A O   
6650 O O   B HOH   E .   ? 0.3787 0.4014 0.4297 -0.0369 0.0524  0.0208  454 HOH   A O   
6651 O O   B HOH   E .   ? 0.2290 0.1879 0.2842 -0.0048 0.0263  -0.0745 455 HOH   A O   
6652 O O   . HOH   E .   ? 0.5300 0.3672 0.4483 0.0262  0.0631  0.1100  456 HOH   A O   
6653 O O   . HOH   E .   ? 0.4229 0.5481 0.5107 0.0836  0.0463  0.0912  457 HOH   A O   
6654 O O   . HOH   E .   ? 0.3079 0.3823 0.5106 0.0945  -0.0640 0.1275  458 HOH   A O   
6655 O O   . HOH   E .   ? 0.5210 0.3392 0.4903 0.0433  0.0476  0.0493  459 HOH   A O   
6656 O O   . HOH   E .   ? 0.7303 0.7815 0.5099 0.0054  -0.0298 0.0089  460 HOH   A O   
6657 O O   . HOH   E .   ? 0.2728 0.2817 0.3716 -0.0406 0.0095  -0.0711 461 HOH   A O   
6658 O O   . HOH   E .   ? 0.6764 0.6551 0.4815 -0.0936 0.1352  0.0909  462 HOH   A O   
6659 O O   . HOH   E .   ? 0.3262 0.5102 0.5548 -0.1528 0.0999  -0.1607 463 HOH   A O   
6660 O O   . HOH   E .   ? 0.3272 0.5750 0.5400 0.0511  -0.0709 0.1710  464 HOH   A O   
6661 O O   . HOH   E .   ? 0.3123 0.2727 0.6283 0.0679  -0.1163 -0.0268 465 HOH   A O   
6662 O O   . HOH   E .   ? 0.3874 0.6500 0.4054 -0.0963 -0.0994 0.2310  466 HOH   A O   
6663 O O   . HOH   E .   ? 0.2744 0.4624 0.5272 0.0592  0.0093  -0.1928 467 HOH   A O   
6664 O O   . HOH   E .   ? 0.3582 0.4647 0.4205 -0.0602 -0.0120 -0.0113 468 HOH   A O   
6665 O O   . HOH   E .   ? 0.5478 0.5234 0.4675 -0.0082 0.1067  0.0433  469 HOH   A O   
6666 O O   . HOH   E .   ? 0.2845 0.2957 0.4013 -0.0988 0.0563  -0.0600 470 HOH   A O   
6667 O O   . HOH   E .   ? 0.6066 0.3222 0.6738 0.0512  -0.0034 0.2132  471 HOH   A O   
6668 O O   . HOH   E .   ? 0.4181 0.5536 0.4003 0.0437  -0.0470 -0.0631 472 HOH   A O   
6669 O O   . HOH   E .   ? 0.6820 0.6071 0.5855 0.1486  0.2520  0.1905  473 HOH   A O   
6670 O O   . HOH   E .   ? 0.3294 0.1957 0.2845 0.0441  -0.1017 -0.0405 474 HOH   A O   
6671 O O   . HOH   E .   ? 0.3180 0.3106 0.4084 0.0294  0.0669  -0.0008 475 HOH   A O   
6672 O O   . HOH   E .   ? 0.5087 0.3279 0.3693 -0.0648 -0.1249 0.0500  476 HOH   A O   
6673 O O   . HOH   E .   ? 0.5375 0.5883 0.5186 0.1393  -0.0628 -0.0979 477 HOH   A O   
6674 O O   . HOH   E .   ? 0.5302 0.6184 0.6581 -0.1738 -0.1402 0.0248  478 HOH   A O   
6675 O O   . HOH   E .   ? 0.4309 0.4288 0.5208 -0.1912 -0.0097 -0.0048 479 HOH   A O   
6676 O O   . HOH   E .   ? 0.4568 0.4186 0.3582 -0.0205 -0.0700 -0.0174 480 HOH   A O   
6677 O O   . HOH   E .   ? 0.6475 0.6437 0.7410 -0.0403 0.0300  -0.0974 481 HOH   A O   
6678 O O   . HOH   E .   ? 0.4647 0.5194 0.2851 0.0134  0.0243  0.0250  482 HOH   A O   
6679 O O   B HOH   E .   ? 0.3131 0.5064 0.3972 0.0888  0.1057  0.0363  483 HOH   A O   
6680 O O   . HOH   E .   ? 0.7672 0.4124 0.3322 -0.0172 -0.1101 0.0097  484 HOH   A O   
6681 O O   . HOH   E .   ? 0.5578 0.3959 0.4404 0.0291  0.0067  -0.1287 485 HOH   A O   
6682 O O   . HOH   E .   ? 0.3057 0.4752 0.3690 -0.0195 -0.0499 -0.0861 486 HOH   A O   
6683 O O   . HOH   E .   ? 0.5419 0.5971 0.5476 0.0299  -0.1123 0.0872  487 HOH   A O   
6684 O O   B HOH   E .   ? 0.1503 0.2034 0.3016 0.0367  -0.0313 0.0807  488 HOH   A O   
6685 O O   . HOH   E .   ? 0.2595 0.5347 0.3401 0.0893  0.0827  0.2186  489 HOH   A O   
6686 O O   . HOH   E .   ? 0.2511 0.2538 0.2674 0.0110  0.0047  -0.0012 490 HOH   A O   
6687 O O   . HOH   E .   ? 0.2697 0.2497 0.6949 -0.0183 -0.1613 0.0223  491 HOH   A O   
6688 O O   . HOH   E .   ? 0.6258 0.7106 0.4918 -0.0750 0.1228  0.1331  492 HOH   A O   
6689 O O   . HOH   E .   ? 0.2927 0.4424 0.4955 0.0285  0.1260  0.1139  493 HOH   A O   
6690 O O   . HOH   E .   ? 0.2657 0.3907 0.4986 -0.0145 0.1009  -0.0583 494 HOH   A O   
6691 O O   . HOH   E .   ? 0.3814 0.3452 0.2790 -0.0255 0.1117  -0.0394 495 HOH   A O   
6692 O O   . HOH   E .   ? 0.5806 0.4043 0.4535 -0.0250 0.1107  0.0123  496 HOH   A O   
6693 O O   . HOH   E .   ? 0.4444 0.3799 0.5026 -0.1280 0.0500  0.0377  497 HOH   A O   
6694 O O   . HOH   E .   ? 0.4701 0.3469 0.4654 -0.0447 0.2168  0.0251  498 HOH   A O   
6695 O O   . HOH   E .   ? 0.5766 0.5225 0.4681 -0.0862 -0.0738 -0.0700 499 HOH   A O   
6696 O O   . HOH   E .   ? 0.5341 0.5825 0.6329 0.0578  0.1459  -0.1192 500 HOH   A O   
6697 O O   . HOH   E .   ? 0.2913 0.2306 0.5460 0.0097  0.0262  0.1040  501 HOH   A O   
6698 O O   . HOH   E .   ? 0.2316 0.3116 0.3591 0.0234  -0.0439 0.0779  502 HOH   A O   
6699 O O   . HOH   E .   ? 0.3908 0.8467 0.5424 -0.1059 -0.0300 0.2272  503 HOH   A O   
6700 O O   . HOH   E .   ? 0.6561 0.6508 0.5277 0.2124  -0.1586 0.0759  504 HOH   A O   
6701 O O   . HOH   E .   ? 0.4685 0.2618 0.4548 -0.1442 0.0298  0.0284  505 HOH   A O   
6702 O O   . HOH   E .   ? 0.6464 0.2501 0.5000 -0.0758 0.0687  0.0704  506 HOH   A O   
6703 O O   . HOH   E .   ? 0.2875 0.4239 0.4247 0.0266  -0.0678 0.0059  507 HOH   A O   
6704 O O   . HOH   E .   ? 0.6238 0.3775 0.5862 0.0314  -0.0011 0.0907  508 HOH   A O   
6705 O O   . HOH   E .   ? 0.5770 0.7073 0.5162 0.1155  -0.0635 0.0455  509 HOH   A O   
6706 O O   . HOH   E .   ? 0.3561 0.7659 0.3885 0.1679  0.0936  0.0325  510 HOH   A O   
6707 O O   . HOH   E .   ? 0.3108 0.2469 0.4658 -0.0014 0.0187  0.0662  511 HOH   A O   
6708 O O   . HOH   E .   ? 0.5021 0.7021 0.4978 0.2790  0.0015  0.1675  512 HOH   A O   
6709 O O   T HOH   E .   ? 0.1440 0.1016 0.1765 -0.0380 -0.0273 0.0542  513 HOH   A O   
6710 O O   . HOH   E .   ? 0.5181 0.5471 0.4582 -0.0562 -0.0332 -0.1431 514 HOH   A O   
6711 O O   . HOH   E .   ? 0.2968 0.6424 0.4133 0.0534  0.0299  -0.0297 515 HOH   A O   
6712 O O   . HOH   E .   ? 0.5803 0.5033 0.5307 0.0249  0.1285  0.0731  516 HOH   A O   
6713 O O   . HOH   E .   ? 0.4988 0.6532 0.5055 -0.0465 -0.0756 0.0436  517 HOH   A O   
6714 O O   . HOH   E .   ? 0.4461 0.4619 0.6365 -0.1001 -0.0686 0.2267  518 HOH   A O   
6715 O O   . HOH   F .   ? 0.2347 0.2268 0.3453 0.0255  0.0747  0.0371  201 HOH   B O   
6716 O O   . HOH   F .   ? 0.5076 0.4168 0.2723 0.0249  -0.0479 -0.1290 202 HOH   B O   
6717 O O   . HOH   F .   ? 0.4418 0.3395 0.3955 -0.0536 0.0067  -0.1276 203 HOH   B O   
6718 O O   . HOH   F .   ? 0.3719 0.4436 0.5933 -0.0835 0.0624  -0.0729 204 HOH   B O   
6719 O O   . HOH   F .   ? 0.3014 0.5863 0.5100 0.0082  0.1719  -0.1565 205 HOH   B O   
6720 O O   . HOH   F .   ? 0.3087 0.6874 0.3773 0.0326  0.0198  0.2375  206 HOH   B O   
6721 O O   . HOH   F .   ? 0.6374 0.5545 0.5995 0.1972  0.0892  0.0154  207 HOH   B O   
6722 O O   . HOH   F .   ? 0.6908 0.3269 0.5002 0.0727  0.1355  -0.0157 208 HOH   B O   
6723 O O   . HOH   F .   ? 0.4949 0.5849 0.4222 0.2770  -0.1408 -0.0209 209 HOH   B O   
6724 O O   . HOH   F .   ? 0.4293 0.4049 0.6258 0.0218  -0.1090 0.2596  210 HOH   B O   
6725 O O   . HOH   F .   ? 0.1924 0.2231 0.3258 -0.0076 0.0172  -0.0150 211 HOH   B O   
6726 O O   . HOH   F .   ? 0.4443 0.4655 0.5562 -0.1156 -0.0221 -0.1399 212 HOH   B O   
6727 O O   . HOH   F .   ? 0.3090 0.3099 0.6433 0.0935  -0.1045 0.0510  213 HOH   B O   
6728 O O   . HOH   F .   ? 0.1704 0.1889 0.2790 -0.0175 -0.0057 0.0054  214 HOH   B O   
6729 O O   . HOH   F .   ? 0.4159 0.5025 0.4746 0.2023  0.0567  -0.0206 215 HOH   B O   
6730 O O   . HOH   F .   ? 0.4382 0.4080 0.3459 -0.0095 -0.1001 0.0757  216 HOH   B O   
6731 O O   . HOH   F .   ? 0.5718 0.3094 0.3967 -0.1778 0.0282  0.0016  217 HOH   B O   
6732 O O   . HOH   F .   ? 0.4379 0.5135 0.4044 0.0333  0.0666  -0.1667 218 HOH   B O   
6733 O O   . HOH   F .   ? 0.3230 0.3632 0.5010 0.0133  -0.0778 0.0145  219 HOH   B O   
6734 O O   . HOH   F .   ? 0.4483 0.5099 0.3505 0.2346  -0.0271 0.0593  220 HOH   B O   
6735 O O   . HOH   F .   ? 0.4101 0.4161 0.6262 -0.0192 -0.1811 -0.0912 221 HOH   B O   
6736 O O   . HOH   F .   ? 0.5164 0.2097 0.3247 0.0036  -0.0843 -0.0040 222 HOH   B O   
6737 O O   . HOH   F .   ? 0.2485 0.1862 0.2830 -0.0252 0.0926  0.0101  223 HOH   B O   
6738 O O   . HOH   F .   ? 0.3852 0.3987 0.5175 -0.1644 0.0196  0.0838  224 HOH   B O   
6739 O O   . HOH   F .   ? 0.3253 0.2931 0.5671 -0.0202 0.0497  -0.0034 225 HOH   B O   
6740 O O   . HOH   F .   ? 0.1695 0.2278 0.2881 -0.0143 0.0029  -0.0153 226 HOH   B O   
6741 O O   . HOH   F .   ? 0.3211 0.2005 0.5552 0.0074  0.1853  0.0643  227 HOH   B O   
6742 O O   . HOH   F .   ? 0.4792 0.3437 0.3205 -0.0748 0.0711  -0.0686 228 HOH   B O   
6743 O O   . HOH   F .   ? 0.2125 0.2196 0.3895 -0.0298 -0.0141 -0.0491 229 HOH   B O   
6744 O O   . HOH   F .   ? 0.4687 0.7534 0.3319 0.2882  0.0367  0.0319  230 HOH   B O   
6745 O O   . HOH   F .   ? 0.2748 0.3594 0.3179 -0.0847 0.0091  -0.0329 231 HOH   B O   
6746 O O   . HOH   F .   ? 0.4706 0.3170 0.4160 -0.2216 0.0220  0.0010  232 HOH   B O   
6747 O O   . HOH   F .   ? 0.2976 0.2320 0.4883 -0.0123 0.1593  0.0010  233 HOH   B O   
6748 O O   . HOH   F .   ? 0.2086 0.1370 0.3467 0.0071  -0.0548 -0.0149 234 HOH   B O   
6749 O O   . HOH   F .   ? 0.2688 0.2691 0.3238 0.0377  0.0198  -0.0917 235 HOH   B O   
6750 O O   . HOH   F .   ? 0.2215 0.2352 0.3365 -0.0535 -0.0011 -0.0379 236 HOH   B O   
6751 O O   . HOH   F .   ? 0.5210 0.6016 0.3133 0.0370  -0.0274 0.0589  237 HOH   B O   
6752 O O   . HOH   F .   ? 0.1503 0.1453 0.1820 -0.0156 -0.0089 0.0011  238 HOH   B O   
6753 O O   . HOH   F .   ? 0.3762 0.1873 0.2255 0.0134  -0.0823 -0.0106 239 HOH   B O   
6754 O O   . HOH   F .   ? 0.2397 0.3631 0.3244 -0.0387 -0.0723 -0.0545 240 HOH   B O   
6755 O O   . HOH   F .   ? 0.6398 0.4243 0.4609 0.1555  -0.0313 -0.1167 241 HOH   B O   
6756 O O   . HOH   F .   ? 0.3865 0.3282 0.2463 0.0301  0.0771  0.0638  242 HOH   B O   
6757 O O   . HOH   F .   ? 0.1576 0.1542 0.2494 -0.0070 0.0035  -0.0137 243 HOH   B O   
6758 O O   . HOH   F .   ? 0.2046 0.3489 0.2704 -0.0199 -0.0284 0.0777  244 HOH   B O   
6759 O O   . HOH   F .   ? 0.3348 0.3441 0.2330 0.0397  0.0715  0.0232  245 HOH   B O   
6760 O O   . HOH   F .   ? 0.3726 0.2635 0.4350 0.0919  -0.0550 -0.0754 246 HOH   B O   
6761 O O   . HOH   F .   ? 0.1447 0.1296 0.1743 -0.0052 -0.0090 0.0125  247 HOH   B O   
6762 O O   . HOH   F .   ? 0.2273 0.1975 0.2175 -0.0367 -0.0502 0.0072  248 HOH   B O   
6763 O O   . HOH   F .   ? 0.3124 0.1768 0.6053 -0.0065 -0.1251 -0.0361 249 HOH   B O   
6764 O O   . HOH   F .   ? 0.2306 0.3376 0.2296 -0.0578 0.0230  0.0391  250 HOH   B O   
6765 O O   . HOH   F .   ? 0.2765 0.2178 0.3194 0.0785  0.0638  0.0084  251 HOH   B O   
6766 O O   . HOH   F .   ? 0.3829 0.2655 0.4887 0.0566  -0.0969 -0.1418 252 HOH   B O   
6767 O O   . HOH   F .   ? 0.3367 0.2430 0.3410 -0.0431 0.0324  -0.0420 253 HOH   B O   
6768 O O   . HOH   F .   ? 0.1611 0.1692 0.2957 -0.0189 -0.0271 0.0132  254 HOH   B O   
6769 O O   . HOH   F .   ? 0.2128 0.1554 0.2251 -0.0295 -0.0438 0.0319  255 HOH   B O   
6770 O O   . HOH   F .   ? 0.2128 0.1503 0.2294 -0.0310 -0.0194 0.0196  256 HOH   B O   
6771 O O   . HOH   F .   ? 0.2424 0.2350 0.2636 0.0928  -0.0841 -0.0746 257 HOH   B O   
6772 O O   . HOH   F .   ? 0.1410 0.1724 0.2179 -0.0098 0.0075  0.0154  258 HOH   B O   
6773 O O   . HOH   F .   ? 0.2393 0.2129 0.1988 0.0021  -0.0116 0.0074  259 HOH   B O   
6774 O O   . HOH   F .   ? 0.2484 0.2016 0.3492 0.0022  -0.0617 -0.0396 260 HOH   B O   
6775 O O   . HOH   F .   ? 0.3084 0.3932 0.3139 -0.1064 -0.0372 -0.0378 261 HOH   B O   
6776 O O   . HOH   F .   ? 0.4478 0.3414 0.2959 0.0695  -0.0038 -0.0797 262 HOH   B O   
6777 O O   . HOH   F .   ? 0.2682 0.3899 0.5349 0.1091  -0.0583 -0.0449 263 HOH   B O   
6778 O O   . HOH   F .   ? 0.4233 0.2953 0.4731 -0.0198 -0.1056 -0.0548 264 HOH   B O   
6779 O O   . HOH   F .   ? 0.2339 0.3849 0.3298 -0.0446 0.0183  -0.1268 265 HOH   B O   
6780 O O   . HOH   F .   ? 0.2345 0.3478 0.2381 0.1127  -0.0146 0.0098  266 HOH   B O   
6781 O O   . HOH   F .   ? 0.3340 0.4648 0.3558 -0.0502 -0.1123 0.0852  267 HOH   B O   
6782 O O   . HOH   F .   ? 0.2959 0.2962 0.4931 -0.0304 -0.0062 -0.0955 268 HOH   B O   
6783 O O   . HOH   F .   ? 0.2602 0.1988 0.3109 -0.0655 0.0174  -0.0021 269 HOH   B O   
6784 O O   . HOH   F .   ? 0.1904 0.1830 0.1835 -0.0418 -0.0420 0.0132  270 HOH   B O   
6785 O O   . HOH   F .   ? 0.3563 0.3597 0.4502 0.1313  -0.1011 -0.1029 271 HOH   B O   
6786 O O   . HOH   F .   ? 0.2534 0.3825 0.3780 0.0375  0.1100  0.0302  272 HOH   B O   
6787 O O   . HOH   F .   ? 0.2752 0.4282 0.6343 0.0204  0.0257  -0.0958 273 HOH   B O   
6788 O O   . HOH   F .   ? 0.2790 0.2203 0.4465 0.0172  0.0432  0.0467  274 HOH   B O   
6789 O O   . HOH   F .   ? 0.2283 0.2258 0.2223 0.0082  -0.0078 0.0000  275 HOH   B O   
6790 O O   . HOH   F .   ? 0.1839 0.1457 0.4185 -0.0107 -0.0219 -0.0161 276 HOH   B O   
6791 O O   . HOH   F .   ? 0.5000 0.3051 0.2916 0.0512  0.0900  -0.0133 277 HOH   B O   
6792 O O   . HOH   F .   ? 0.2692 0.2911 0.2530 -0.0498 -0.0813 0.0277  278 HOH   B O   
6793 O O   . HOH   F .   ? 0.2432 0.4301 0.4803 -0.0660 -0.0259 -0.1261 279 HOH   B O   
6794 O O   . HOH   F .   ? 0.2423 0.2549 0.2442 -0.0503 -0.0580 -0.0268 280 HOH   B O   
6795 O O   . HOH   F .   ? 0.1670 0.1584 0.3509 -0.0148 0.0055  0.0062  281 HOH   B O   
6796 O O   . HOH   F .   ? 0.4816 0.6870 0.2689 0.0272  -0.0818 0.1119  282 HOH   B O   
6797 O O   . HOH   F .   ? 0.3671 0.2238 0.4114 -0.1073 -0.2039 0.0890  283 HOH   B O   
6798 O O   . HOH   F .   ? 0.1632 0.1513 0.1974 0.0057  0.0018  -0.0062 284 HOH   B O   
6799 O O   . HOH   F .   ? 0.2696 0.6841 0.6984 0.1419  -0.0463 -0.0584 285 HOH   B O   
6800 O O   . HOH   F .   ? 0.4884 0.4670 0.2632 0.1320  -0.0625 -0.0288 286 HOH   B O   
6801 O O   . HOH   F .   ? 0.4372 0.4717 0.5381 0.0061  -0.1724 0.0014  287 HOH   B O   
6802 O O   . HOH   F .   ? 0.2674 0.2458 0.2895 0.0170  -0.0779 0.0148  288 HOH   B O   
6803 O O   . HOH   F .   ? 0.2791 0.4857 0.4732 -0.1216 -0.1031 0.0673  289 HOH   B O   
6804 O O   . HOH   F .   ? 0.3776 0.2667 0.2140 -0.0004 -0.0806 0.0055  290 HOH   B O   
6805 O O   . HOH   F .   ? 0.5591 0.3711 0.3186 0.2528  0.1143  0.0796  291 HOH   B O   
6806 O O   . HOH   F .   ? 0.1645 0.2020 0.1731 -0.0191 -0.0248 0.0067  292 HOH   B O   
6807 O O   . HOH   F .   ? 0.1702 0.1998 0.3032 0.0196  -0.0067 0.0042  293 HOH   B O   
6808 O O   . HOH   F .   ? 0.3174 0.3795 0.3917 -0.1431 0.0996  -0.0445 294 HOH   B O   
6809 O O   . HOH   F .   ? 0.3409 0.2844 0.2807 -0.0348 0.0236  -0.1252 295 HOH   B O   
6810 O O   . HOH   F .   ? 0.1737 0.3475 0.4598 0.0289  0.0020  -0.1310 296 HOH   B O   
6811 O O   . HOH   F .   ? 0.2395 0.6759 0.2553 0.0416  -0.0361 -0.0481 297 HOH   B O   
6812 O O   . HOH   F .   ? 0.4525 0.4442 0.2273 -0.0112 0.0450  0.0647  298 HOH   B O   
6813 O O   . HOH   F .   ? 0.1831 0.1652 0.2483 0.0091  0.0036  0.0160  299 HOH   B O   
6814 O O   . HOH   F .   ? 0.2193 0.1655 0.2779 -0.0302 -0.0262 0.0011  300 HOH   B O   
6815 O O   . HOH   F .   ? 0.3492 0.6917 0.3646 0.1464  -0.0752 0.0743  301 HOH   B O   
6816 O O   . HOH   F .   ? 0.4873 0.3860 0.2393 0.1362  -0.0970 0.0334  302 HOH   B O   
6817 O O   . HOH   F .   ? 0.3648 0.1925 0.3440 0.0761  0.1212  0.0592  303 HOH   B O   
6818 O O   . HOH   F .   ? 0.3073 0.2807 0.5115 -0.0243 -0.0571 0.1008  304 HOH   B O   
6819 O O   . HOH   F .   ? 0.4509 0.3738 0.4840 -0.0932 -0.0049 0.1530  305 HOH   B O   
6820 O O   . HOH   F .   ? 0.2240 0.2818 0.6042 0.0633  -0.0210 -0.1024 306 HOH   B O   
6821 O O   . HOH   F .   ? 0.5865 0.5598 0.4867 -0.1131 -0.0379 0.1222  307 HOH   B O   
6822 O O   . HOH   F .   ? 0.2732 0.3012 0.3660 -0.0548 0.0931  -0.0942 308 HOH   B O   
6823 O O   . HOH   F .   ? 0.5242 0.2984 0.2487 -0.1827 0.0888  -0.0334 309 HOH   B O   
6824 O O   . HOH   F .   ? 0.2100 0.1668 0.3557 0.0378  -0.1007 -0.0050 310 HOH   B O   
6825 O O   . HOH   F .   ? 0.2332 0.3055 0.4737 -0.0362 -0.0499 0.0368  311 HOH   B O   
6826 O O   . HOH   F .   ? 0.2467 0.1516 0.2652 -0.0141 -0.0220 0.0268  312 HOH   B O   
6827 O O   . HOH   F .   ? 0.6526 0.4453 0.6090 0.1172  0.1125  -0.0059 313 HOH   B O   
6828 O O   . HOH   F .   ? 0.1682 0.2732 0.2429 -0.0077 -0.0185 0.0495  314 HOH   B O   
6829 O O   . HOH   F .   ? 0.1626 0.1915 0.2833 -0.0299 -0.0133 0.0150  315 HOH   B O   
6830 O O   . HOH   F .   ? 0.4143 0.2263 0.2930 0.1406  0.0925  0.0254  316 HOH   B O   
6831 O O   . HOH   F .   ? 0.4483 0.4042 0.6049 0.0470  0.0101  0.0690  317 HOH   B O   
6832 O O   . HOH   F .   ? 0.2798 0.3107 0.4753 -0.0517 -0.1478 0.1063  318 HOH   B O   
6833 O O   . HOH   F .   ? 0.2126 0.1944 0.2009 -0.0127 0.0039  0.0153  319 HOH   B O   
6834 O O   . HOH   F .   ? 0.4870 0.4838 0.2679 0.0834  -0.0729 -0.0705 320 HOH   B O   
6835 O O   . HOH   F .   ? 0.1632 0.1524 0.3314 0.0102  -0.0089 0.0026  321 HOH   B O   
6836 O O   . HOH   F .   ? 0.5443 0.4446 0.6517 0.0845  -0.1259 0.1931  322 HOH   B O   
6837 O O   . HOH   F .   ? 0.1618 0.1622 0.2929 -0.0084 -0.0175 -0.0176 323 HOH   B O   
6838 O O   . HOH   F .   ? 0.6092 0.5945 0.4784 0.2572  0.0043  0.0185  324 HOH   B O   
6839 O O   . HOH   F .   ? 0.2738 0.2136 0.2629 0.0068  -0.0250 0.0142  325 HOH   B O   
6840 O O   . HOH   F .   ? 0.2222 0.5579 0.4953 -0.0372 -0.0266 -0.0301 326 HOH   B O   
6841 O O   . HOH   F .   ? 0.4875 0.2583 0.3115 0.0349  0.0380  0.0848  327 HOH   B O   
6842 O O   . HOH   F .   ? 0.1917 0.1991 0.3146 0.0370  0.0476  0.0205  328 HOH   B O   
6843 O O   . HOH   F .   ? 0.3707 0.3956 0.7267 -0.0090 -0.0827 0.1924  329 HOH   B O   
6844 O O   . HOH   F .   ? 0.4291 0.3223 0.5462 0.1197  0.2114  0.1851  330 HOH   B O   
6845 O O   . HOH   F .   ? 0.2818 0.2044 0.4643 -0.0090 -0.0063 0.0293  331 HOH   B O   
6846 O O   . HOH   F .   ? 0.8286 0.2148 0.2973 0.0084  -0.0676 0.0176  332 HOH   B O   
6847 O O   . HOH   F .   ? 0.6238 0.3619 0.3465 -0.0150 0.1101  0.1218  333 HOH   B O   
6848 O O   . HOH   F .   ? 0.5208 0.5101 0.3627 0.0339  -0.0729 0.0256  334 HOH   B O   
6849 O O   . HOH   F .   ? 0.1721 0.2841 0.3028 0.0283  -0.0194 -0.0513 335 HOH   B O   
6850 O O   . HOH   F .   ? 0.1791 0.1467 0.2437 0.0067  -0.0267 0.0102  336 HOH   B O   
6851 O O   . HOH   F .   ? 0.4584 0.6571 0.3774 -0.0280 -0.0593 0.1708  337 HOH   B O   
6852 O O   . HOH   F .   ? 0.6397 0.5974 0.2916 -0.0069 -0.0321 0.0837  338 HOH   B O   
6853 O O   . HOH   F .   ? 0.2296 0.2376 0.5492 -0.0531 -0.0196 0.1480  339 HOH   B O   
6854 O O   . HOH   F .   ? 0.5134 0.3665 0.4342 0.0238  0.0723  -0.1757 340 HOH   B O   
6855 O O   . HOH   F .   ? 0.5749 0.4543 0.5968 -0.0653 -0.0717 -0.1385 341 HOH   B O   
6856 O O   . HOH   F .   ? 0.5347 0.3625 0.3449 0.0970  -0.1288 -0.0678 342 HOH   B O   
6857 O O   . HOH   F .   ? 0.2096 0.5330 0.6804 -0.0330 -0.0682 0.0125  343 HOH   B O   
6858 O O   . HOH   F .   ? 0.4096 0.6300 0.4079 -0.1297 -0.0978 -0.0730 344 HOH   B O   
6859 O O   . HOH   F .   ? 0.2152 0.2097 0.2887 -0.0002 0.0537  -0.0061 345 HOH   B O   
6860 O O   . HOH   F .   ? 0.5328 0.5839 0.4833 -0.1226 0.0797  0.0691  346 HOH   B O   
6861 O O   . HOH   F .   ? 0.4246 0.5535 0.5227 0.0141  -0.0757 0.0217  347 HOH   B O   
6862 O O   . HOH   F .   ? 0.2783 0.2411 0.4869 -0.0211 -0.1012 -0.0395 348 HOH   B O   
6863 O O   . HOH   F .   ? 0.2422 0.6161 0.3614 0.1592  -0.0593 -0.1216 349 HOH   B O   
6864 O O   . HOH   F .   ? 0.2444 0.3940 0.5292 0.0242  0.0249  0.0262  350 HOH   B O   
6865 O O   . HOH   F .   ? 0.3038 0.1825 0.4211 0.0436  -0.1214 -0.0467 351 HOH   B O   
6866 O O   . HOH   F .   ? 0.4589 0.6388 0.6398 0.0513  0.0109  -0.0162 352 HOH   B O   
6867 O O   . HOH   F .   ? 0.3832 0.2227 0.3516 -0.0551 0.0137  -0.0673 353 HOH   B O   
6868 O O   . HOH   F .   ? 0.5207 0.3028 0.5442 -0.1086 0.1515  0.0329  354 HOH   B O   
6869 O O   . HOH   F .   ? 0.3625 0.4735 0.4638 -0.1772 0.0242  -0.0132 355 HOH   B O   
6870 O O   . HOH   F .   ? 0.5033 0.3989 0.4192 0.0656  0.0907  -0.0462 356 HOH   B O   
6871 O O   . HOH   F .   ? 0.3896 0.2925 0.4067 -0.1011 -0.0130 -0.0568 357 HOH   B O   
6872 O O   . HOH   F .   ? 0.4560 0.5786 0.4983 0.1774  -0.1107 0.1512  358 HOH   B O   
6873 O O   . HOH   F .   ? 0.5054 0.4738 0.5667 0.0474  -0.0109 0.0616  359 HOH   B O   
6874 O O   . HOH   F .   ? 0.5337 0.3790 0.5188 -0.0146 -0.1665 -0.0475 360 HOH   B O   
6875 O O   . HOH   F .   ? 0.5345 0.3944 0.6332 0.0585  0.1258  0.1353  361 HOH   B O   
6876 O O   . HOH   F .   ? 0.3990 0.5961 0.3006 0.1425  -0.0032 0.0268  362 HOH   B O   
6877 O O   . HOH   F .   ? 0.2287 0.3824 0.6429 -0.0678 -0.1070 -0.0668 363 HOH   B O   
6878 O O   . HOH   F .   ? 0.4981 0.3060 0.5773 -0.1427 -0.0544 0.0456  364 HOH   B O   
6879 O O   . HOH   F .   ? 0.6491 0.2383 0.3898 -0.0174 -0.0221 0.0913  365 HOH   B O   
6880 O O   . HOH   F .   ? 0.5818 0.3612 0.5411 0.1235  -0.1438 0.0129  366 HOH   B O   
6881 O O   . HOH   F .   ? 0.5197 0.5881 0.4520 -0.0935 -0.0794 -0.1183 367 HOH   B O   
6882 O O   . HOH   F .   ? 0.5344 0.5902 0.3240 0.1305  -0.1466 0.0401  368 HOH   B O   
6883 O O   . HOH   F .   ? 0.4600 0.5175 0.5261 0.2404  0.0416  0.0912  369 HOH   B O   
6884 O O   . HOH   F .   ? 0.6362 0.4055 0.3096 -0.1037 -0.1184 -0.0462 370 HOH   B O   
6885 O O   . HOH   F .   ? 0.6079 0.4429 0.4310 0.0859  0.0789  0.0564  371 HOH   B O   
6886 O O   . HOH   F .   ? 0.4058 0.3308 0.4224 0.0418  -0.1412 -0.0223 372 HOH   B O   
6887 O O   . HOH   F .   ? 0.7722 0.7753 0.5340 0.2363  -0.1476 0.0777  373 HOH   B O   
6888 O O   . HOH   F .   ? 0.4677 0.4841 0.4952 -0.0731 -0.0658 0.0357  374 HOH   B O   
6889 O O   . HOH   F .   ? 0.3377 0.4019 0.2480 0.0628  0.0156  0.0267  375 HOH   B O   
6890 O O   . HOH   F .   ? 0.2346 0.4303 0.4679 0.0354  -0.0634 -0.0670 376 HOH   B O   
6891 O O   . HOH   F .   ? 0.4675 0.7198 0.5732 0.1426  0.0302  0.2575  377 HOH   B O   
6892 O O   . HOH   F .   ? 0.6599 0.3789 0.5408 -0.0460 -0.0228 -0.0204 378 HOH   B O   
6893 O O   . HOH   F .   ? 0.3362 0.5188 0.4295 0.1161  -0.0283 0.0179  379 HOH   B O   
6894 O O   . HOH   F .   ? 0.5794 0.7093 0.4193 -0.1387 0.0082  -0.1355 380 HOH   B O   
6895 O O   . HOH   F .   ? 0.5597 0.7360 0.6820 -0.0598 0.2223  0.0900  381 HOH   B O   
6896 O O   . HOH   F .   ? 0.4261 0.8017 0.5832 0.1127  0.2275  0.0801  382 HOH   B O   
6897 O O   . HOH   F .   ? 0.3128 0.2492 0.3203 0.0160  0.0226  0.0286  383 HOH   B O   
6898 O O   . HOH   F .   ? 0.5276 0.4566 0.4912 -0.0056 -0.0548 -0.0332 384 HOH   B O   
6899 O O   . HOH   F .   ? 0.6879 0.3890 0.4557 0.0631  0.0916  -0.0766 385 HOH   B O   
6900 O O   . HOH   F .   ? 0.2494 0.4065 0.3960 -0.0655 -0.1099 -0.0008 386 HOH   B O   
6901 O O   . HOH   F .   ? 0.5910 0.4701 0.5564 -0.0730 0.0288  -0.0343 387 HOH   B O   
6902 O O   . HOH   F .   ? 0.6667 0.5843 0.4822 0.1913  -0.0203 0.1023  388 HOH   B O   
6903 O O   . HOH   F .   ? 0.4690 0.3903 0.3343 0.0116  0.0627  -0.0047 389 HOH   B O   
6904 O O   . HOH   F .   ? 0.4482 0.2347 0.3153 0.0959  -0.0200 0.0230  390 HOH   B O   
6905 O O   . HOH   F .   ? 0.4716 0.3867 0.4429 0.0126  0.0262  0.0230  391 HOH   B O   
6906 O O   . HOH   F .   ? 0.2403 0.4399 0.6529 -0.1227 -0.0743 0.0037  392 HOH   B O   
6907 O O   . HOH   F .   ? 0.4253 0.2371 0.5216 -0.0625 0.0676  0.0322  393 HOH   B O   
6908 O O   . HOH   F .   ? 0.4704 0.5926 0.4037 0.1610  -0.0110 -0.0928 394 HOH   B O   
6909 O O   . HOH   F .   ? 0.3389 0.3919 0.3850 0.0480  0.0096  -0.0812 395 HOH   B O   
6910 O O   . HOH   F .   ? 0.3902 0.4653 0.4052 -0.0381 0.0520  0.0479  396 HOH   B O   
6911 O O   . HOH   F .   ? 0.2244 0.2918 0.6171 -0.0546 -0.0819 -0.0019 397 HOH   B O   
6912 O O   . HOH   F .   ? 0.5526 0.6540 0.7110 0.1299  -0.1153 0.2247  398 HOH   B O   
6913 O O   . HOH   F .   ? 0.5436 0.4251 0.3056 -0.2192 -0.0532 0.0941  399 HOH   B O   
6914 O O   . HOH   F .   ? 0.5832 0.6144 0.3985 0.1534  0.0311  -0.0521 400 HOH   B O   
# 
