data_7HF0
# 
_entry.id   7HF0 
# 
_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   7HF0         pdb_00007hf0 10.2210/pdb7hf0/pdb 
WWPDB D_1001407390 ?            ?                   
# 
_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                        7HF0 
_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 '(3R)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-3-ol' 204.228   1   ?                      ? ? ? 
4 water       nat water                                                     18.015    434 ?                      ? ? ? 
# 
_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 '(3R)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-3-ol' A1BAK 
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 
A1BAK non-polymer         . '(3R)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-3-ol' ? 'C10 H12 N4 O'   204.228 
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 A1BAK 1   202 201  A1BAK LA1 A . 
E 4 HOH   1   301 292  HOH   HOH A . 
E 4 HOH   2   302 20   HOH   HOH A . 
E 4 HOH   3   303 1309 HOH   HOH A . 
E 4 HOH   4   304 153  HOH   HOH A . 
E 4 HOH   5   305 16   HOH   HOH A . 
E 4 HOH   6   306 229  HOH   HOH A . 
E 4 HOH   7   307 3    HOH   HOH A . 
E 4 HOH   8   308 196  HOH   HOH A . 
E 4 HOH   9   309 625  HOH   HOH A . 
E 4 HOH   10  310 493  HOH   HOH A . 
E 4 HOH   11  311 209  HOH   HOH A . 
E 4 HOH   12  312 1301 HOH   HOH A . 
E 4 HOH   13  313 952  HOH   HOH A . 
E 4 HOH   14  314 109  HOH   HOH A . 
E 4 HOH   15  315 13   HOH   HOH A . 
E 4 HOH   16  316 281  HOH   HOH A . 
E 4 HOH   17  317 1    HOH   HOH A . 
E 4 HOH   18  318 21   HOH   HOH A . 
E 4 HOH   19  319 964  HOH   HOH A . 
E 4 HOH   20  320 661  HOH   HOH A . 
E 4 HOH   21  321 19   HOH   HOH A . 
E 4 HOH   22  322 1283 HOH   HOH A . 
E 4 HOH   23  323 76   HOH   HOH A . 
E 4 HOH   24  324 136  HOH   HOH A . 
E 4 HOH   25  325 124  HOH   HOH A . 
E 4 HOH   26  326 1290 HOH   HOH A . 
E 4 HOH   27  327 405  HOH   HOH A . 
E 4 HOH   28  328 236  HOH   HOH A . 
E 4 HOH   29  329 192  HOH   HOH A . 
E 4 HOH   30  330 247  HOH   HOH A . 
E 4 HOH   31  331 57   HOH   HOH A . 
E 4 HOH   32  332 86   HOH   HOH A . 
E 4 HOH   33  333 151  HOH   HOH A . 
E 4 HOH   34  334 1295 HOH   HOH A . 
E 4 HOH   35  335 155  HOH   HOH A . 
E 4 HOH   36  336 1275 HOH   HOH A . 
E 4 HOH   37  337 15   HOH   HOH A . 
E 4 HOH   38  338 630  HOH   HOH A . 
E 4 HOH   39  339 225  HOH   HOH A . 
E 4 HOH   40  340 164  HOH   HOH A . 
E 4 HOH   41  341 662  HOH   HOH A . 
E 4 HOH   42  342 8    HOH   HOH A . 
E 4 HOH   43  343 241  HOH   HOH A . 
E 4 HOH   44  344 140  HOH   HOH A . 
E 4 HOH   45  345 469  HOH   HOH A . 
E 4 HOH   46  346 337  HOH   HOH A . 
E 4 HOH   47  347 165  HOH   HOH A . 
E 4 HOH   48  348 115  HOH   HOH A . 
E 4 HOH   49  349 1300 HOH   HOH A . 
E 4 HOH   50  350 320  HOH   HOH A . 
E 4 HOH   51  351 42   HOH   HOH A . 
E 4 HOH   52  352 93   HOH   HOH A . 
E 4 HOH   53  353 393  HOH   HOH A . 
E 4 HOH   54  354 26   HOH   HOH A . 
E 4 HOH   55  355 33   HOH   HOH A . 
E 4 HOH   56  356 354  HOH   HOH A . 
E 4 HOH   57  357 92   HOH   HOH A . 
E 4 HOH   58  358 66   HOH   HOH A . 
E 4 HOH   59  359 139  HOH   HOH A . 
E 4 HOH   60  360 2    HOH   HOH A . 
E 4 HOH   61  361 17   HOH   HOH A . 
E 4 HOH   62  362 5    HOH   HOH A . 
E 4 HOH   63  363 138  HOH   HOH A . 
E 4 HOH   64  364 102  HOH   HOH A . 
E 4 HOH   65  365 19   HOH   HOH A . 
E 4 HOH   66  366 24   HOH   HOH A . 
E 4 HOH   67  367 45   HOH   HOH A . 
E 4 HOH   68  368 169  HOH   HOH A . 
E 4 HOH   69  369 162  HOH   HOH A . 
E 4 HOH   70  370 461  HOH   HOH A . 
E 4 HOH   71  371 159  HOH   HOH A . 
E 4 HOH   72  372 333  HOH   HOH A . 
E 4 HOH   73  373 81   HOH   HOH A . 
E 4 HOH   74  374 27   HOH   HOH A . 
E 4 HOH   75  375 49   HOH   HOH A . 
E 4 HOH   76  376 409  HOH   HOH A . 
E 4 HOH   77  377 140  HOH   HOH A . 
E 4 HOH   78  378 18   HOH   HOH A . 
E 4 HOH   79  379 186  HOH   HOH A . 
E 4 HOH   80  380 34   HOH   HOH A . 
E 4 HOH   81  381 56   HOH   HOH A . 
E 4 HOH   82  382 396  HOH   HOH A . 
E 4 HOH   83  383 39   HOH   HOH A . 
E 4 HOH   84  384 36   HOH   HOH A . 
E 4 HOH   85  385 939  HOH   HOH A . 
E 4 HOH   86  386 134  HOH   HOH A . 
E 4 HOH   87  387 218  HOH   HOH A . 
E 4 HOH   88  388 105  HOH   HOH A . 
E 4 HOH   89  389 85   HOH   HOH A . 
E 4 HOH   90  390 351  HOH   HOH A . 
E 4 HOH   91  391 35   HOH   HOH A . 
E 4 HOH   92  392 46   HOH   HOH A . 
E 4 HOH   93  393 12   HOH   HOH A . 
E 4 HOH   94  394 122  HOH   HOH A . 
E 4 HOH   95  395 62   HOH   HOH A . 
E 4 HOH   96  396 148  HOH   HOH A . 
E 4 HOH   97  397 83   HOH   HOH A . 
E 4 HOH   98  398 58   HOH   HOH A . 
E 4 HOH   99  399 154  HOH   HOH A . 
E 4 HOH   100 400 132  HOH   HOH A . 
E 4 HOH   101 401 78   HOH   HOH A . 
E 4 HOH   102 402 74   HOH   HOH A . 
E 4 HOH   103 403 296  HOH   HOH A . 
E 4 HOH   104 404 116  HOH   HOH A . 
E 4 HOH   105 405 366  HOH   HOH A . 
E 4 HOH   106 406 199  HOH   HOH A . 
E 4 HOH   107 407 14   HOH   HOH A . 
E 4 HOH   108 408 1068 HOH   HOH A . 
E 4 HOH   109 409 12   HOH   HOH A . 
E 4 HOH   110 410 195  HOH   HOH A . 
E 4 HOH   111 411 67   HOH   HOH A . 
E 4 HOH   112 412 1308 HOH   HOH A . 
E 4 HOH   113 413 123  HOH   HOH A . 
E 4 HOH   114 414 4    HOH   HOH A . 
E 4 HOH   115 415 121  HOH   HOH A . 
E 4 HOH   116 416 1315 HOH   HOH A . 
E 4 HOH   117 417 9    HOH   HOH A . 
E 4 HOH   118 418 25   HOH   HOH A . 
E 4 HOH   119 419 1094 HOH   HOH A . 
E 4 HOH   120 420 303  HOH   HOH A . 
E 4 HOH   121 421 68   HOH   HOH A . 
E 4 HOH   122 422 18   HOH   HOH A . 
E 4 HOH   123 423 6    HOH   HOH A . 
E 4 HOH   124 424 125  HOH   HOH A . 
E 4 HOH   125 425 10   HOH   HOH A . 
E 4 HOH   126 426 53   HOH   HOH A . 
E 4 HOH   127 427 3    HOH   HOH A . 
E 4 HOH   128 428 96   HOH   HOH A . 
E 4 HOH   129 429 8    HOH   HOH A . 
E 4 HOH   130 430 278  HOH   HOH A . 
E 4 HOH   131 431 397  HOH   HOH A . 
E 4 HOH   132 432 51   HOH   HOH A . 
E 4 HOH   133 433 95   HOH   HOH A . 
E 4 HOH   134 434 70   HOH   HOH A . 
E 4 HOH   135 435 156  HOH   HOH A . 
E 4 HOH   136 436 381  HOH   HOH A . 
E 4 HOH   137 437 5    HOH   HOH A . 
E 4 HOH   138 438 1279 HOH   HOH A . 
E 4 HOH   139 439 1313 HOH   HOH A . 
E 4 HOH   140 440 582  HOH   HOH A . 
E 4 HOH   141 441 1310 HOH   HOH A . 
E 4 HOH   142 442 1222 HOH   HOH A . 
E 4 HOH   143 443 1289 HOH   HOH A . 
E 4 HOH   144 444 1238 HOH   HOH A . 
E 4 HOH   145 445 1296 HOH   HOH A . 
E 4 HOH   146 446 7    HOH   HOH A . 
E 4 HOH   147 447 944  HOH   HOH A . 
E 4 HOH   148 448 212  HOH   HOH A . 
E 4 HOH   149 449 16   HOH   HOH A . 
E 4 HOH   150 450 80   HOH   HOH A . 
E 4 HOH   151 451 71   HOH   HOH A . 
E 4 HOH   152 452 40   HOH   HOH A . 
E 4 HOH   153 453 73   HOH   HOH A . 
E 4 HOH   154 454 1134 HOH   HOH A . 
E 4 HOH   155 455 1189 HOH   HOH A . 
E 4 HOH   156 456 94   HOH   HOH A . 
E 4 HOH   157 457 1286 HOH   HOH A . 
E 4 HOH   158 458 79   HOH   HOH A . 
E 4 HOH   159 459 97   HOH   HOH A . 
E 4 HOH   160 460 104  HOH   HOH A . 
E 4 HOH   161 461 576  HOH   HOH A . 
E 4 HOH   162 462 188  HOH   HOH A . 
E 4 HOH   163 463 330  HOH   HOH A . 
E 4 HOH   164 464 22   HOH   HOH A . 
E 4 HOH   165 465 2    HOH   HOH A . 
E 4 HOH   166 466 1119 HOH   HOH A . 
E 4 HOH   167 467 509  HOH   HOH A . 
E 4 HOH   168 468 107  HOH   HOH A . 
E 4 HOH   169 469 11   HOH   HOH A . 
E 4 HOH   170 470 726  HOH   HOH A . 
E 4 HOH   171 471 163  HOH   HOH A . 
E 4 HOH   172 472 756  HOH   HOH A . 
E 4 HOH   173 473 408  HOH   HOH A . 
E 4 HOH   174 474 280  HOH   HOH A . 
E 4 HOH   175 475 4    HOH   HOH A . 
E 4 HOH   176 476 319  HOH   HOH A . 
E 4 HOH   177 477 63   HOH   HOH A . 
E 4 HOH   178 478 556  HOH   HOH A . 
E 4 HOH   179 479 126  HOH   HOH A . 
E 4 HOH   180 480 1276 HOH   HOH A . 
E 4 HOH   181 481 361  HOH   HOH A . 
E 4 HOH   182 482 801  HOH   HOH A . 
E 4 HOH   183 483 1307 HOH   HOH A . 
E 4 HOH   184 484 342  HOH   HOH A . 
E 4 HOH   185 485 370  HOH   HOH A . 
E 4 HOH   186 486 250  HOH   HOH A . 
E 4 HOH   187 487 521  HOH   HOH A . 
E 4 HOH   188 488 17   HOH   HOH A . 
E 4 HOH   189 489 267  HOH   HOH A . 
E 4 HOH   190 490 1306 HOH   HOH A . 
E 4 HOH   191 491 224  HOH   HOH A . 
E 4 HOH   192 492 202  HOH   HOH A . 
E 4 HOH   193 493 326  HOH   HOH A . 
E 4 HOH   194 494 25   HOH   HOH A . 
E 4 HOH   195 495 1287 HOH   HOH A . 
E 4 HOH   196 496 695  HOH   HOH A . 
E 4 HOH   197 497 1314 HOH   HOH A . 
E 4 HOH   198 498 674  HOH   HOH A . 
E 4 HOH   199 499 919  HOH   HOH A . 
E 4 HOH   200 500 135  HOH   HOH A . 
E 4 HOH   201 501 315  HOH   HOH A . 
E 4 HOH   202 502 318  HOH   HOH A . 
E 4 HOH   203 503 309  HOH   HOH A . 
E 4 HOH   204 504 1299 HOH   HOH A . 
E 4 HOH   205 505 331  HOH   HOH A . 
E 4 HOH   206 506 941  HOH   HOH A . 
E 4 HOH   207 507 711  HOH   HOH A . 
E 4 HOH   208 508 208  HOH   HOH A . 
E 4 HOH   209 509 805  HOH   HOH A . 
E 4 HOH   210 510 263  HOH   HOH A . 
E 4 HOH   211 511 152  HOH   HOH A . 
E 4 HOH   212 512 23   HOH   HOH A . 
E 4 HOH   213 513 356  HOH   HOH A . 
E 4 HOH   214 514 7    HOH   HOH A . 
E 4 HOH   215 515 1284 HOH   HOH A . 
E 4 HOH   216 516 350  HOH   HOH A . 
E 4 HOH   217 517 180  HOH   HOH A . 
E 4 HOH   218 518 1071 HOH   HOH A . 
E 4 HOH   219 519 363  HOH   HOH A . 
E 4 HOH   220 520 15   HOH   HOH A . 
E 4 HOH   221 521 313  HOH   HOH A . 
E 4 HOH   222 522 371  HOH   HOH A . 
E 4 HOH   223 523 6    HOH   HOH A . 
E 4 HOH   224 524 185  HOH   HOH A . 
E 4 HOH   225 525 429  HOH   HOH A . 
E 4 HOH   226 526 21   HOH   HOH A . 
E 4 HOH   227 527 24   HOH   HOH A . 
E 4 HOH   228 528 772  HOH   HOH A . 
E 4 HOH   229 529 70   HOH   HOH A . 
E 4 HOH   230 530 376  HOH   HOH A . 
E 4 HOH   231 531 1074 HOH   HOH A . 
E 4 HOH   232 532 346  HOH   HOH A . 
E 4 HOH   233 533 1292 HOH   HOH A . 
E 4 HOH   234 534 1078 HOH   HOH A . 
F 4 HOH   1   201 64   HOH   HOH B . 
F 4 HOH   2   202 549  HOH   HOH B . 
F 4 HOH   3   203 358  HOH   HOH B . 
F 4 HOH   4   204 531  HOH   HOH B . 
F 4 HOH   5   205 900  HOH   HOH B . 
F 4 HOH   6   206 240  HOH   HOH B . 
F 4 HOH   7   207 364  HOH   HOH B . 
F 4 HOH   8   208 353  HOH   HOH B . 
F 4 HOH   9   209 1249 HOH   HOH B . 
F 4 HOH   10  210 654  HOH   HOH B . 
F 4 HOH   11  211 758  HOH   HOH B . 
F 4 HOH   12  212 264  HOH   HOH B . 
F 4 HOH   13  213 120  HOH   HOH B . 
F 4 HOH   14  214 743  HOH   HOH B . 
F 4 HOH   15  215 398  HOH   HOH B . 
F 4 HOH   16  216 232  HOH   HOH B . 
F 4 HOH   17  217 452  HOH   HOH B . 
F 4 HOH   18  218 50   HOH   HOH B . 
F 4 HOH   19  219 1278 HOH   HOH B . 
F 4 HOH   20  220 1140 HOH   HOH B . 
F 4 HOH   21  221 332  HOH   HOH B . 
F 4 HOH   22  222 282  HOH   HOH B . 
F 4 HOH   23  223 205  HOH   HOH B . 
F 4 HOH   24  224 252  HOH   HOH B . 
F 4 HOH   25  225 75   HOH   HOH B . 
F 4 HOH   26  226 131  HOH   HOH B . 
F 4 HOH   27  227 54   HOH   HOH B . 
F 4 HOH   28  228 444  HOH   HOH B . 
F 4 HOH   29  229 82   HOH   HOH B . 
F 4 HOH   30  230 276  HOH   HOH B . 
F 4 HOH   31  231 166  HOH   HOH B . 
F 4 HOH   32  232 343  HOH   HOH B . 
F 4 HOH   33  233 60   HOH   HOH B . 
F 4 HOH   34  234 272  HOH   HOH B . 
F 4 HOH   35  235 1    HOH   HOH B . 
F 4 HOH   36  236 325  HOH   HOH B . 
F 4 HOH   37  237 110  HOH   HOH B . 
F 4 HOH   38  238 300  HOH   HOH B . 
F 4 HOH   39  239 133  HOH   HOH B . 
F 4 HOH   40  240 9    HOH   HOH B . 
F 4 HOH   41  241 52   HOH   HOH B . 
F 4 HOH   42  242 181  HOH   HOH B . 
F 4 HOH   43  243 723  HOH   HOH B . 
F 4 HOH   44  244 144  HOH   HOH B . 
F 4 HOH   45  245 231  HOH   HOH B . 
F 4 HOH   46  246 14   HOH   HOH B . 
F 4 HOH   47  247 127  HOH   HOH B . 
F 4 HOH   48  248 69   HOH   HOH B . 
F 4 HOH   49  249 30   HOH   HOH B . 
F 4 HOH   50  250 129  HOH   HOH B . 
F 4 HOH   51  251 391  HOH   HOH B . 
F 4 HOH   52  252 41   HOH   HOH B . 
F 4 HOH   53  253 172  HOH   HOH B . 
F 4 HOH   54  254 103  HOH   HOH B . 
F 4 HOH   55  255 128  HOH   HOH B . 
F 4 HOH   56  256 143  HOH   HOH B . 
F 4 HOH   57  257 271  HOH   HOH B . 
F 4 HOH   58  258 31   HOH   HOH B . 
F 4 HOH   59  259 72   HOH   HOH B . 
F 4 HOH   60  260 1312 HOH   HOH B . 
F 4 HOH   61  261 117  HOH   HOH B . 
F 4 HOH   62  262 47   HOH   HOH B . 
F 4 HOH   63  263 10   HOH   HOH B . 
F 4 HOH   64  264 150  HOH   HOH B . 
F 4 HOH   65  265 302  HOH   HOH B . 
F 4 HOH   66  266 175  HOH   HOH B . 
F 4 HOH   67  267 61   HOH   HOH B . 
F 4 HOH   68  268 59   HOH   HOH B . 
F 4 HOH   69  269 147  HOH   HOH B . 
F 4 HOH   70  270 77   HOH   HOH B . 
F 4 HOH   71  271 287  HOH   HOH B . 
F 4 HOH   72  272 114  HOH   HOH B . 
F 4 HOH   73  273 1277 HOH   HOH B . 
F 4 HOH   74  274 221  HOH   HOH B . 
F 4 HOH   75  275 242  HOH   HOH B . 
F 4 HOH   76  276 84   HOH   HOH B . 
F 4 HOH   77  277 20   HOH   HOH B . 
F 4 HOH   78  278 347  HOH   HOH B . 
F 4 HOH   79  279 243  HOH   HOH B . 
F 4 HOH   80  280 11   HOH   HOH B . 
F 4 HOH   81  281 220  HOH   HOH B . 
F 4 HOH   82  282 43   HOH   HOH B . 
F 4 HOH   83  283 22   HOH   HOH B . 
F 4 HOH   84  284 88   HOH   HOH B . 
F 4 HOH   85  285 235  HOH   HOH B . 
F 4 HOH   86  286 89   HOH   HOH B . 
F 4 HOH   87  287 13   HOH   HOH B . 
F 4 HOH   88  288 387  HOH   HOH B . 
F 4 HOH   89  289 137  HOH   HOH B . 
F 4 HOH   90  290 1305 HOH   HOH B . 
F 4 HOH   91  291 106  HOH   HOH B . 
F 4 HOH   92  292 316  HOH   HOH B . 
F 4 HOH   93  293 1066 HOH   HOH B . 
F 4 HOH   94  294 1285 HOH   HOH B . 
F 4 HOH   95  295 216  HOH   HOH B . 
F 4 HOH   96  296 299  HOH   HOH B . 
F 4 HOH   97  297 160  HOH   HOH B . 
F 4 HOH   98  298 311  HOH   HOH B . 
F 4 HOH   99  299 99   HOH   HOH B . 
F 4 HOH   100 300 112  HOH   HOH B . 
F 4 HOH   101 301 1106 HOH   HOH B . 
F 4 HOH   102 302 297  HOH   HOH B . 
F 4 HOH   103 303 142  HOH   HOH B . 
F 4 HOH   104 304 32   HOH   HOH B . 
F 4 HOH   105 305 215  HOH   HOH B . 
F 4 HOH   106 306 101  HOH   HOH B . 
F 4 HOH   107 307 341  HOH   HOH B . 
F 4 HOH   108 308 37   HOH   HOH B . 
F 4 HOH   109 309 38   HOH   HOH B . 
F 4 HOH   110 310 635  HOH   HOH B . 
F 4 HOH   111 311 48   HOH   HOH B . 
F 4 HOH   112 312 197  HOH   HOH B . 
F 4 HOH   113 313 118  HOH   HOH B . 
F 4 HOH   114 314 416  HOH   HOH B . 
F 4 HOH   115 315 170  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 1274 HOH   HOH B . 
F 4 HOH   119 319 1126 HOH   HOH B . 
F 4 HOH   120 320 23   HOH   HOH B . 
F 4 HOH   121 321 177  HOH   HOH B . 
F 4 HOH   122 322 182  HOH   HOH B . 
F 4 HOH   123 323 44   HOH   HOH B . 
F 4 HOH   124 324 28   HOH   HOH B . 
F 4 HOH   125 325 141  HOH   HOH B . 
F 4 HOH   126 326 100  HOH   HOH B . 
F 4 HOH   127 327 1294 HOH   HOH B . 
F 4 HOH   128 328 1291 HOH   HOH B . 
F 4 HOH   129 329 29   HOH   HOH B . 
F 4 HOH   130 330 334  HOH   HOH B . 
F 4 HOH   131 331 98   HOH   HOH B . 
F 4 HOH   132 332 207  HOH   HOH B . 
F 4 HOH   133 333 161  HOH   HOH B . 
F 4 HOH   134 334 717  HOH   HOH B . 
F 4 HOH   135 335 55   HOH   HOH B . 
F 4 HOH   136 336 65   HOH   HOH B . 
F 4 HOH   137 337 445  HOH   HOH B . 
F 4 HOH   138 338 234  HOH   HOH B . 
F 4 HOH   139 339 619  HOH   HOH B . 
F 4 HOH   140 340 1293 HOH   HOH B . 
F 4 HOH   141 341 339  HOH   HOH B . 
F 4 HOH   142 342 362  HOH   HOH B . 
F 4 HOH   143 343 178  HOH   HOH B . 
F 4 HOH   144 344 90   HOH   HOH B . 
F 4 HOH   145 345 960  HOH   HOH B . 
F 4 HOH   146 346 87   HOH   HOH B . 
F 4 HOH   147 347 463  HOH   HOH B . 
F 4 HOH   148 348 1304 HOH   HOH B . 
F 4 HOH   149 349 191  HOH   HOH B . 
F 4 HOH   150 350 1046 HOH   HOH B . 
F 4 HOH   151 351 623  HOH   HOH B . 
F 4 HOH   152 352 335  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   160 360 718  HOH   HOH B . 
F 4 HOH   161 361 389  HOH   HOH B . 
F 4 HOH   162 362 283  HOH   HOH B . 
F 4 HOH   163 363 1072 HOH   HOH B . 
F 4 HOH   164 364 898  HOH   HOH B . 
F 4 HOH   165 365 1316 HOH   HOH B . 
F 4 HOH   166 366 291  HOH   HOH B . 
F 4 HOH   167 367 615  HOH   HOH B . 
F 4 HOH   168 368 373  HOH   HOH B . 
F 4 HOH   169 369 340  HOH   HOH B . 
F 4 HOH   170 370 667  HOH   HOH B . 
F 4 HOH   171 371 1303 HOH   HOH B . 
F 4 HOH   172 372 310  HOH   HOH B . 
F 4 HOH   173 373 190  HOH   HOH B . 
F 4 HOH   174 374 1173 HOH   HOH B . 
F 4 HOH   175 375 431  HOH   HOH B . 
F 4 HOH   176 376 149  HOH   HOH B . 
F 4 HOH   177 377 183  HOH   HOH B . 
F 4 HOH   178 378 1000 HOH   HOH B . 
F 4 HOH   179 379 418  HOH   HOH B . 
F 4 HOH   180 380 1163 HOH   HOH B . 
F 4 HOH   181 381 1311 HOH   HOH B . 
F 4 HOH   182 382 176  HOH   HOH B . 
F 4 HOH   183 383 424  HOH   HOH B . 
F 4 HOH   184 384 491  HOH   HOH B . 
F 4 HOH   185 385 981  HOH   HOH B . 
F 4 HOH   186 386 470  HOH   HOH B . 
F 4 HOH   187 387 1298 HOH   HOH B . 
F 4 HOH   188 388 248  HOH   HOH B . 
F 4 HOH   189 389 265  HOH   HOH B . 
F 4 HOH   190 390 184  HOH   HOH B . 
F 4 HOH   191 391 360  HOH   HOH B . 
F 4 HOH   192 392 410  HOH   HOH B . 
F 4 HOH   193 393 355  HOH   HOH B . 
F 4 HOH   194 394 566  HOH   HOH B . 
F 4 HOH   195 395 274  HOH   HOH B . 
F 4 HOH   196 396 314  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           7HF0 
_cell.length_a           88.692 
_cell.length_b           88.692 
_cell.length_c           39.539 
_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                         7HF0 
_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          7HF0 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.59 
_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   2023-05-28 
_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                     7HF0 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.350 
_reflns.d_resolution_high            1.000 
_reflns.number_obs                   165246 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.600 
_reflns.pdbx_Rmerge_I_obs            0.045 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        14.900 
_reflns.B_iso_Wilson_estimate        12.220 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.049 
_reflns.pdbx_Rpim_I_all              0.019 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1055445 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.000 1.020  ? 34034 7616 ? 1.564 ? ? ? 4.500 ? 0.800  ? ? ? ? ? ? 93.400 1.771 0.811 0.545 
1 2 5.480 44.350 ? 7499  1094 ? 0.028 ? ? ? 6.900 ? 59.100 ? ? ? ? ? ? 99.800 0.030 0.011 0.999 
# 
_refine.entry_id                                 7HF0 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0000 
_refine.ls_d_res_low                             39.6600 
_refine.pdbx_ls_sigma_F                          1.350 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.5400 
_refine.ls_number_reflns_obs                     165113 
_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                          0.1502 
_refine.ls_R_factor_R_work                       0.1495 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1633 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7962 
_refine.ls_number_reflns_R_work                  157151 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               19.5757 
_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                            0.1000 
_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                                68.970 
_refine.B_iso_min                                9.390 
_refine.pdbx_overall_phase_error                 20.4300 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0000 
_refine_hist.d_res_low                        39.6600 
_refine_hist.pdbx_number_atoms_ligand         34 
_refine_hist.number_atoms_solvent             434 
_refine_hist.number_atoms_total               3010 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           15.54 
_refine_hist.pdbx_B_iso_mean_solvent          30.82 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.0000 1.0100  30 91.0000  4822 . 0.4468 0.3983 . 252 0.0000 5074 . 'X-RAY DIFFRACTION' 
1.0100 1.0200  30 97.0000  5045 . 0.3814 0.3729 . 224 0.0000 5269 . 'X-RAY DIFFRACTION' 
1.0200 1.0400  30 100.0000 5267 . 0.3277 0.3164 . 259 0.0000 5526 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5186 . 0.2938 0.2863 . 267 0.0000 5453 . 'X-RAY DIFFRACTION' 
1.0500 1.0600  30 100.0000 5200 . 0.2681 0.2924 . 325 0.0000 5525 . 'X-RAY DIFFRACTION' 
1.0600 1.0800  30 100.0000 5253 . 0.2463 0.2571 . 252 0.0000 5505 . 'X-RAY DIFFRACTION' 
1.0800 1.0900  30 100.0000 5208 . 0.2251 0.2452 . 266 0.0000 5474 . 'X-RAY DIFFRACTION' 
1.0900 1.1100  30 100.0000 5241 . 0.2055 0.2203 . 239 0.0000 5480 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5225 . 0.1932 0.1926 . 284 0.0000 5509 . 'X-RAY DIFFRACTION' 
1.1300 1.1400  30 100.0000 5239 . 0.1787 0.1823 . 237 0.0000 5476 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5292 . 0.1646 0.1979 . 265 0.0000 5557 . 'X-RAY DIFFRACTION' 
1.1600 1.1900  30 100.0000 5240 . 0.1485 0.1832 . 264 0.0000 5504 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 5166 . 0.1416 0.1741 . 293 0.0000 5459 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5319 . 0.1326 0.1591 . 231 0.0000 5550 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 5194 . 0.1352 0.1515 . 258 0.0000 5452 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 5271 . 0.1326 0.1497 . 278 0.0000 5549 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 5235 . 0.1296 0.1537 . 285 0.0000 5520 . 'X-RAY DIFFRACTION' 
1.3200 1.3600  30 100.0000 5218 . 0.1331 0.1434 . 280 0.0000 5498 . 'X-RAY DIFFRACTION' 
1.3600 1.4000  30 100.0000 5281 . 0.1353 0.1659 . 240 0.0000 5521 . 'X-RAY DIFFRACTION' 
1.4000 1.4400  30 100.0000 5236 . 0.1336 0.1593 . 272 0.0000 5508 . 'X-RAY DIFFRACTION' 
1.4400 1.4900  30 100.0000 5300 . 0.1282 0.1395 . 251 0.0000 5551 . 'X-RAY DIFFRACTION' 
1.4900 1.5500  30 100.0000 5201 . 0.1223 0.1419 . 276 0.0000 5477 . 'X-RAY DIFFRACTION' 
1.5500 1.6200  30 100.0000 5282 . 0.1198 0.1369 . 267 0.0000 5549 . 'X-RAY DIFFRACTION' 
1.6200 1.7100  30 100.0000 5296 . 0.1285 0.1397 . 262 0.0000 5558 . 'X-RAY DIFFRACTION' 
1.7100 1.8200  30 100.0000 5281 . 0.1374 0.1394 . 252 0.0000 5533 . 'X-RAY DIFFRACTION' 
1.8200 1.9600  30 100.0000 5276 . 0.1349 0.1406 . 279 0.0000 5555 . 'X-RAY DIFFRACTION' 
1.9600 2.1500  30 100.0000 5283 . 0.1385 0.1418 . 289 0.0000 5572 . 'X-RAY DIFFRACTION' 
2.1500 2.4700  30 100.0000 5285 . 0.1380 0.1409 . 288 0.0000 5573 . 'X-RAY DIFFRACTION' 
2.4700 3.1100  30 100.0000 5330 . 0.1485 0.1693 . 258 0.0000 5588 . 'X-RAY DIFFRACTION' 
3.1100 39.6600 30 100.0000 5479 . 0.1489 0.1704 . 269 0.0000 5748 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HF0 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003661' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HF0 
_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 7HF0 A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HF0 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 7HF0 SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HF0 MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HF0 SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HF0 MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E 
2 1 B,F     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N TYR A 17  ? N TYR A 17  O LEU A 153 ? O LEU A 153 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O VAL B 95  ? O VAL B 95  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HF0 
_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   O 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    204 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    312 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.19 
# 
_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  ? ? 55.62 -132.78 
2 1 SER A 128 ? B 73.46 -7.93   
3 1 HIS B 86  ? ? 58.11 -128.00 
# 
_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 532 ? 5.89 . 
2 1 O ? A HOH 533 ? 5.93 . 
3 1 O ? A HOH 534 ? 7.61 . 
4 1 O ? B HOH 400 ? 6.25 . 
# 
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 
A1BAK N2   N Y N 1   
A1BAK C3   C N N 2   
A1BAK C6   C Y N 3   
A1BAK C9   C Y N 4   
A1BAK C1   C N R 5   
A1BAK C10  C N N 6   
A1BAK C2   C N N 7   
A1BAK C4   C Y N 8   
A1BAK C5   C Y N 9   
A1BAK C7   C Y N 10  
A1BAK C8   C Y N 11  
A1BAK N1   N N N 12  
A1BAK N3   N Y N 13  
A1BAK N4   N Y N 14  
A1BAK O1   O N N 15  
A1BAK H6   H N N 16  
A1BAK H5   H N N 17  
A1BAK H9   H N N 18  
A1BAK H1   H N N 19  
A1BAK H11  H N N 20  
A1BAK H12  H N N 21  
A1BAK H3   H N N 22  
A1BAK H4   H N N 23  
A1BAK H7   H N N 24  
A1BAK H8   H N N 25  
A1BAK H10  H N N 26  
A1BAK H2   H N N 27  
ALA   N    N N N 28  
ALA   CA   C N S 29  
ALA   C    C N N 30  
ALA   O    O N N 31  
ALA   CB   C N N 32  
ALA   OXT  O N N 33  
ALA   H    H N N 34  
ALA   H2   H N N 35  
ALA   HA   H N N 36  
ALA   HB1  H N N 37  
ALA   HB2  H N N 38  
ALA   HB3  H N N 39  
ALA   HXT  H N N 40  
ARG   N    N N N 41  
ARG   CA   C N S 42  
ARG   C    C N N 43  
ARG   O    O N N 44  
ARG   CB   C N N 45  
ARG   CG   C N N 46  
ARG   CD   C N N 47  
ARG   NE   N N N 48  
ARG   CZ   C N N 49  
ARG   NH1  N N N 50  
ARG   NH2  N N N 51  
ARG   OXT  O N N 52  
ARG   H    H N N 53  
ARG   H2   H N N 54  
ARG   HA   H N N 55  
ARG   HB2  H N N 56  
ARG   HB3  H N N 57  
ARG   HG2  H N N 58  
ARG   HG3  H N N 59  
ARG   HD2  H N N 60  
ARG   HD3  H N N 61  
ARG   HE   H N N 62  
ARG   HH11 H N N 63  
ARG   HH12 H N N 64  
ARG   HH21 H N N 65  
ARG   HH22 H N N 66  
ARG   HXT  H N N 67  
ASN   N    N N N 68  
ASN   CA   C N S 69  
ASN   C    C N N 70  
ASN   O    O N N 71  
ASN   CB   C N N 72  
ASN   CG   C N N 73  
ASN   OD1  O N N 74  
ASN   ND2  N N N 75  
ASN   OXT  O N N 76  
ASN   H    H N N 77  
ASN   H2   H N N 78  
ASN   HA   H N N 79  
ASN   HB2  H N N 80  
ASN   HB3  H N N 81  
ASN   HD21 H N N 82  
ASN   HD22 H N N 83  
ASN   HXT  H N N 84  
ASP   N    N N N 85  
ASP   CA   C N S 86  
ASP   C    C N N 87  
ASP   O    O N N 88  
ASP   CB   C N N 89  
ASP   CG   C N N 90  
ASP   OD1  O N N 91  
ASP   OD2  O N N 92  
ASP   OXT  O N N 93  
ASP   H    H N N 94  
ASP   H2   H N N 95  
ASP   HA   H N N 96  
ASP   HB2  H N N 97  
ASP   HB3  H N N 98  
ASP   HD2  H N N 99  
ASP   HXT  H N N 100 
CYS   N    N N N 101 
CYS   CA   C N R 102 
CYS   C    C N N 103 
CYS   O    O N N 104 
CYS   CB   C N N 105 
CYS   SG   S N N 106 
CYS   OXT  O N N 107 
CYS   H    H N N 108 
CYS   H2   H N N 109 
CYS   HA   H N N 110 
CYS   HB2  H N N 111 
CYS   HB3  H N N 112 
CYS   HG   H N N 113 
CYS   HXT  H N N 114 
GLN   N    N N N 115 
GLN   CA   C N S 116 
GLN   C    C N N 117 
GLN   O    O N N 118 
GLN   CB   C N N 119 
GLN   CG   C N N 120 
GLN   CD   C N N 121 
GLN   OE1  O N N 122 
GLN   NE2  N N N 123 
GLN   OXT  O N N 124 
GLN   H    H N N 125 
GLN   H2   H N N 126 
GLN   HA   H N N 127 
GLN   HB2  H N N 128 
GLN   HB3  H N N 129 
GLN   HG2  H N N 130 
GLN   HG3  H N N 131 
GLN   HE21 H N N 132 
GLN   HE22 H N N 133 
GLN   HXT  H N N 134 
GLU   N    N N N 135 
GLU   CA   C N S 136 
GLU   C    C N N 137 
GLU   O    O N N 138 
GLU   CB   C N N 139 
GLU   CG   C N N 140 
GLU   CD   C N N 141 
GLU   OE1  O N N 142 
GLU   OE2  O N N 143 
GLU   OXT  O N N 144 
GLU   H    H N N 145 
GLU   H2   H N N 146 
GLU   HA   H N N 147 
GLU   HB2  H N N 148 
GLU   HB3  H N N 149 
GLU   HG2  H N N 150 
GLU   HG3  H N N 151 
GLU   HE2  H N N 152 
GLU   HXT  H N N 153 
GLY   N    N N N 154 
GLY   CA   C N N 155 
GLY   C    C N N 156 
GLY   O    O N N 157 
GLY   OXT  O N N 158 
GLY   H    H N N 159 
GLY   H2   H N N 160 
GLY   HA2  H N N 161 
GLY   HA3  H N N 162 
GLY   HXT  H N N 163 
HIS   N    N N N 164 
HIS   CA   C N S 165 
HIS   C    C N N 166 
HIS   O    O N N 167 
HIS   CB   C N N 168 
HIS   CG   C Y N 169 
HIS   ND1  N Y N 170 
HIS   CD2  C Y N 171 
HIS   CE1  C Y N 172 
HIS   NE2  N Y N 173 
HIS   OXT  O N N 174 
HIS   H    H N N 175 
HIS   H2   H N N 176 
HIS   HA   H N N 177 
HIS   HB2  H N N 178 
HIS   HB3  H N N 179 
HIS   HD1  H N N 180 
HIS   HD2  H N N 181 
HIS   HE1  H N N 182 
HIS   HE2  H N N 183 
HIS   HXT  H N N 184 
HOH   O    O N N 185 
HOH   H1   H N N 186 
HOH   H2   H N N 187 
ILE   N    N N N 188 
ILE   CA   C N S 189 
ILE   C    C N N 190 
ILE   O    O N N 191 
ILE   CB   C N S 192 
ILE   CG1  C N N 193 
ILE   CG2  C N N 194 
ILE   CD1  C N N 195 
ILE   OXT  O N N 196 
ILE   H    H N N 197 
ILE   H2   H N N 198 
ILE   HA   H N N 199 
ILE   HB   H N N 200 
ILE   HG12 H N N 201 
ILE   HG13 H N N 202 
ILE   HG21 H N N 203 
ILE   HG22 H N N 204 
ILE   HG23 H N N 205 
ILE   HD11 H N N 206 
ILE   HD12 H N N 207 
ILE   HD13 H N N 208 
ILE   HXT  H N N 209 
LEU   N    N N N 210 
LEU   CA   C N S 211 
LEU   C    C N N 212 
LEU   O    O N N 213 
LEU   CB   C N N 214 
LEU   CG   C N N 215 
LEU   CD1  C N N 216 
LEU   CD2  C N N 217 
LEU   OXT  O N N 218 
LEU   H    H N N 219 
LEU   H2   H N N 220 
LEU   HA   H N N 221 
LEU   HB2  H N N 222 
LEU   HB3  H N N 223 
LEU   HG   H N N 224 
LEU   HD11 H N N 225 
LEU   HD12 H N N 226 
LEU   HD13 H N N 227 
LEU   HD21 H N N 228 
LEU   HD22 H N N 229 
LEU   HD23 H N N 230 
LEU   HXT  H N N 231 
LYS   N    N N N 232 
LYS   CA   C N S 233 
LYS   C    C N N 234 
LYS   O    O N N 235 
LYS   CB   C N N 236 
LYS   CG   C N N 237 
LYS   CD   C N N 238 
LYS   CE   C N N 239 
LYS   NZ   N N N 240 
LYS   OXT  O N N 241 
LYS   H    H N N 242 
LYS   H2   H N N 243 
LYS   HA   H N N 244 
LYS   HB2  H N N 245 
LYS   HB3  H N N 246 
LYS   HG2  H N N 247 
LYS   HG3  H N N 248 
LYS   HD2  H N N 249 
LYS   HD3  H N N 250 
LYS   HE2  H N N 251 
LYS   HE3  H N N 252 
LYS   HZ1  H N N 253 
LYS   HZ2  H N N 254 
LYS   HZ3  H N N 255 
LYS   HXT  H N N 256 
MET   N    N N N 257 
MET   CA   C N S 258 
MET   C    C N N 259 
MET   O    O N N 260 
MET   CB   C N N 261 
MET   CG   C N N 262 
MET   SD   S N N 263 
MET   CE   C N N 264 
MET   OXT  O N N 265 
MET   H    H N N 266 
MET   H2   H N N 267 
MET   HA   H N N 268 
MET   HB2  H N N 269 
MET   HB3  H N N 270 
MET   HG2  H N N 271 
MET   HG3  H N N 272 
MET   HE1  H N N 273 
MET   HE2  H N N 274 
MET   HE3  H N N 275 
MET   HXT  H N N 276 
PHE   N    N N N 277 
PHE   CA   C N S 278 
PHE   C    C N N 279 
PHE   O    O N N 280 
PHE   CB   C N N 281 
PHE   CG   C Y N 282 
PHE   CD1  C Y N 283 
PHE   CD2  C Y N 284 
PHE   CE1  C Y N 285 
PHE   CE2  C Y N 286 
PHE   CZ   C Y N 287 
PHE   OXT  O N N 288 
PHE   H    H N N 289 
PHE   H2   H N N 290 
PHE   HA   H N N 291 
PHE   HB2  H N N 292 
PHE   HB3  H N N 293 
PHE   HD1  H N N 294 
PHE   HD2  H N N 295 
PHE   HE1  H N N 296 
PHE   HE2  H N N 297 
PHE   HZ   H N N 298 
PHE   HXT  H N N 299 
PRO   N    N N N 300 
PRO   CA   C N S 301 
PRO   C    C N N 302 
PRO   O    O N N 303 
PRO   CB   C N N 304 
PRO   CG   C N N 305 
PRO   CD   C N N 306 
PRO   OXT  O N N 307 
PRO   H    H N N 308 
PRO   HA   H N N 309 
PRO   HB2  H N N 310 
PRO   HB3  H N N 311 
PRO   HG2  H N N 312 
PRO   HG3  H N N 313 
PRO   HD2  H N N 314 
PRO   HD3  H N N 315 
PRO   HXT  H N N 316 
SER   N    N N N 317 
SER   CA   C N S 318 
SER   C    C N N 319 
SER   O    O N N 320 
SER   CB   C N N 321 
SER   OG   O N N 322 
SER   OXT  O N N 323 
SER   H    H N N 324 
SER   H2   H N N 325 
SER   HA   H N N 326 
SER   HB2  H N N 327 
SER   HB3  H N N 328 
SER   HG   H N N 329 
SER   HXT  H N N 330 
TFA   C1   C N N 331 
TFA   C2   C N N 332 
TFA   O    O N N 333 
TFA   F1   F N N 334 
TFA   F2   F N N 335 
TFA   F3   F N N 336 
TFA   OXT  O N N 337 
TFA   HXT  H N N 338 
THR   N    N N N 339 
THR   CA   C N S 340 
THR   C    C N N 341 
THR   O    O N N 342 
THR   CB   C N R 343 
THR   OG1  O N N 344 
THR   CG2  C N N 345 
THR   OXT  O N N 346 
THR   H    H N N 347 
THR   H2   H N N 348 
THR   HA   H N N 349 
THR   HB   H N N 350 
THR   HG1  H N N 351 
THR   HG21 H N N 352 
THR   HG22 H N N 353 
THR   HG23 H N N 354 
THR   HXT  H N N 355 
TYR   N    N N N 356 
TYR   CA   C N S 357 
TYR   C    C N N 358 
TYR   O    O N N 359 
TYR   CB   C N N 360 
TYR   CG   C Y N 361 
TYR   CD1  C Y N 362 
TYR   CD2  C Y N 363 
TYR   CE1  C Y N 364 
TYR   CE2  C Y N 365 
TYR   CZ   C Y N 366 
TYR   OH   O N N 367 
TYR   OXT  O N N 368 
TYR   H    H N N 369 
TYR   H2   H N N 370 
TYR   HA   H N N 371 
TYR   HB2  H N N 372 
TYR   HB3  H N N 373 
TYR   HD1  H N N 374 
TYR   HD2  H N N 375 
TYR   HE1  H N N 376 
TYR   HE2  H N N 377 
TYR   HH   H N N 378 
TYR   HXT  H N N 379 
VAL   N    N N N 380 
VAL   CA   C N S 381 
VAL   C    C N N 382 
VAL   O    O N N 383 
VAL   CB   C N N 384 
VAL   CG1  C N N 385 
VAL   CG2  C N N 386 
VAL   OXT  O N N 387 
VAL   H    H N N 388 
VAL   H2   H N N 389 
VAL   HA   H N N 390 
VAL   HB   H N N 391 
VAL   HG11 H N N 392 
VAL   HG12 H N N 393 
VAL   HG13 H N N 394 
VAL   HG21 H N N 395 
VAL   HG22 H N N 396 
VAL   HG23 H N N 397 
VAL   HXT  H N N 398 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1BAK O1  C1   sing N N 1   
A1BAK C1  C2   sing N N 2   
A1BAK C1  C10  sing N N 3   
A1BAK C2  C3   sing N N 4   
A1BAK C3  N1   sing N N 5   
A1BAK C10 N1   sing N N 6   
A1BAK N1  C4   sing N N 7   
A1BAK C4  N2   doub Y N 8   
A1BAK C4  C7   sing Y N 9   
A1BAK C8  C7   sing Y N 10  
A1BAK C8  C9   doub Y N 11  
A1BAK N2  C5   sing Y N 12  
A1BAK C7  C6   doub Y N 13  
A1BAK C9  N4   sing Y N 14  
A1BAK C5  N3   doub Y N 15  
A1BAK C6  N4   sing Y N 16  
A1BAK C6  N3   sing Y N 17  
A1BAK C3  H6   sing N N 18  
A1BAK C3  H5   sing N N 19  
A1BAK C9  H9   sing N N 20  
A1BAK C1  H1   sing N N 21  
A1BAK C10 H11  sing N N 22  
A1BAK C10 H12  sing N N 23  
A1BAK C2  H3   sing N N 24  
A1BAK C2  H4   sing N N 25  
A1BAK C5  H7   sing N N 26  
A1BAK C8  H8   sing N N 27  
A1BAK N4  H10  sing N N 28  
A1BAK O1  H2   sing N N 29  
ALA   N   CA   sing N N 30  
ALA   N   H    sing N N 31  
ALA   N   H2   sing N N 32  
ALA   CA  C    sing N N 33  
ALA   CA  CB   sing N N 34  
ALA   CA  HA   sing N N 35  
ALA   C   O    doub N N 36  
ALA   C   OXT  sing N N 37  
ALA   CB  HB1  sing N N 38  
ALA   CB  HB2  sing N N 39  
ALA   CB  HB3  sing N N 40  
ALA   OXT HXT  sing N N 41  
ARG   N   CA   sing N N 42  
ARG   N   H    sing N N 43  
ARG   N   H2   sing N N 44  
ARG   CA  C    sing N N 45  
ARG   CA  CB   sing N N 46  
ARG   CA  HA   sing N N 47  
ARG   C   O    doub N N 48  
ARG   C   OXT  sing N N 49  
ARG   CB  CG   sing N N 50  
ARG   CB  HB2  sing N N 51  
ARG   CB  HB3  sing N N 52  
ARG   CG  CD   sing N N 53  
ARG   CG  HG2  sing N N 54  
ARG   CG  HG3  sing N N 55  
ARG   CD  NE   sing N N 56  
ARG   CD  HD2  sing N N 57  
ARG   CD  HD3  sing N N 58  
ARG   NE  CZ   sing N N 59  
ARG   NE  HE   sing N N 60  
ARG   CZ  NH1  sing N N 61  
ARG   CZ  NH2  doub N N 62  
ARG   NH1 HH11 sing N N 63  
ARG   NH1 HH12 sing N N 64  
ARG   NH2 HH21 sing N N 65  
ARG   NH2 HH22 sing N N 66  
ARG   OXT HXT  sing N N 67  
ASN   N   CA   sing N N 68  
ASN   N   H    sing N N 69  
ASN   N   H2   sing N N 70  
ASN   CA  C    sing N N 71  
ASN   CA  CB   sing N N 72  
ASN   CA  HA   sing N N 73  
ASN   C   O    doub N N 74  
ASN   C   OXT  sing N N 75  
ASN   CB  CG   sing N N 76  
ASN   CB  HB2  sing N N 77  
ASN   CB  HB3  sing N N 78  
ASN   CG  OD1  doub N N 79  
ASN   CG  ND2  sing N N 80  
ASN   ND2 HD21 sing N N 81  
ASN   ND2 HD22 sing N N 82  
ASN   OXT HXT  sing N N 83  
ASP   N   CA   sing N N 84  
ASP   N   H    sing N N 85  
ASP   N   H2   sing N N 86  
ASP   CA  C    sing N N 87  
ASP   CA  CB   sing N N 88  
ASP   CA  HA   sing N N 89  
ASP   C   O    doub N N 90  
ASP   C   OXT  sing N N 91  
ASP   CB  CG   sing N N 92  
ASP   CB  HB2  sing N N 93  
ASP   CB  HB3  sing N N 94  
ASP   CG  OD1  doub N N 95  
ASP   CG  OD2  sing N N 96  
ASP   OD2 HD2  sing N N 97  
ASP   OXT HXT  sing N N 98  
CYS   N   CA   sing N N 99  
CYS   N   H    sing N N 100 
CYS   N   H2   sing N N 101 
CYS   CA  C    sing N N 102 
CYS   CA  CB   sing N N 103 
CYS   CA  HA   sing N N 104 
CYS   C   O    doub N N 105 
CYS   C   OXT  sing N N 106 
CYS   CB  SG   sing N N 107 
CYS   CB  HB2  sing N N 108 
CYS   CB  HB3  sing N N 109 
CYS   SG  HG   sing N N 110 
CYS   OXT HXT  sing N N 111 
GLN   N   CA   sing N N 112 
GLN   N   H    sing N N 113 
GLN   N   H2   sing N N 114 
GLN   CA  C    sing N N 115 
GLN   CA  CB   sing N N 116 
GLN   CA  HA   sing N N 117 
GLN   C   O    doub N N 118 
GLN   C   OXT  sing N N 119 
GLN   CB  CG   sing N N 120 
GLN   CB  HB2  sing N N 121 
GLN   CB  HB3  sing N N 122 
GLN   CG  CD   sing N N 123 
GLN   CG  HG2  sing N N 124 
GLN   CG  HG3  sing N N 125 
GLN   CD  OE1  doub N N 126 
GLN   CD  NE2  sing N N 127 
GLN   NE2 HE21 sing N N 128 
GLN   NE2 HE22 sing N N 129 
GLN   OXT HXT  sing N N 130 
GLU   N   CA   sing N N 131 
GLU   N   H    sing N N 132 
GLU   N   H2   sing N N 133 
GLU   CA  C    sing N N 134 
GLU   CA  CB   sing N N 135 
GLU   CA  HA   sing N N 136 
GLU   C   O    doub N N 137 
GLU   C   OXT  sing N N 138 
GLU   CB  CG   sing N N 139 
GLU   CB  HB2  sing N N 140 
GLU   CB  HB3  sing N N 141 
GLU   CG  CD   sing N N 142 
GLU   CG  HG2  sing N N 143 
GLU   CG  HG3  sing N N 144 
GLU   CD  OE1  doub N N 145 
GLU   CD  OE2  sing N N 146 
GLU   OE2 HE2  sing N N 147 
GLU   OXT HXT  sing N N 148 
GLY   N   CA   sing N N 149 
GLY   N   H    sing N N 150 
GLY   N   H2   sing N N 151 
GLY   CA  C    sing N N 152 
GLY   CA  HA2  sing N N 153 
GLY   CA  HA3  sing N N 154 
GLY   C   O    doub N N 155 
GLY   C   OXT  sing N N 156 
GLY   OXT HXT  sing N N 157 
HIS   N   CA   sing N N 158 
HIS   N   H    sing N N 159 
HIS   N   H2   sing N N 160 
HIS   CA  C    sing N N 161 
HIS   CA  CB   sing N N 162 
HIS   CA  HA   sing N N 163 
HIS   C   O    doub N N 164 
HIS   C   OXT  sing N N 165 
HIS   CB  CG   sing N N 166 
HIS   CB  HB2  sing N N 167 
HIS   CB  HB3  sing N N 168 
HIS   CG  ND1  sing Y N 169 
HIS   CG  CD2  doub Y N 170 
HIS   ND1 CE1  doub Y N 171 
HIS   ND1 HD1  sing N N 172 
HIS   CD2 NE2  sing Y N 173 
HIS   CD2 HD2  sing N N 174 
HIS   CE1 NE2  sing Y N 175 
HIS   CE1 HE1  sing N N 176 
HIS   NE2 HE2  sing N N 177 
HIS   OXT HXT  sing N N 178 
HOH   O   H1   sing N N 179 
HOH   O   H2   sing N N 180 
ILE   N   CA   sing N N 181 
ILE   N   H    sing N N 182 
ILE   N   H2   sing N N 183 
ILE   CA  C    sing N N 184 
ILE   CA  CB   sing N N 185 
ILE   CA  HA   sing N N 186 
ILE   C   O    doub N N 187 
ILE   C   OXT  sing N N 188 
ILE   CB  CG1  sing N N 189 
ILE   CB  CG2  sing N N 190 
ILE   CB  HB   sing N N 191 
ILE   CG1 CD1  sing N N 192 
ILE   CG1 HG12 sing N N 193 
ILE   CG1 HG13 sing N N 194 
ILE   CG2 HG21 sing N N 195 
ILE   CG2 HG22 sing N N 196 
ILE   CG2 HG23 sing N N 197 
ILE   CD1 HD11 sing N N 198 
ILE   CD1 HD12 sing N N 199 
ILE   CD1 HD13 sing N N 200 
ILE   OXT HXT  sing N N 201 
LEU   N   CA   sing N N 202 
LEU   N   H    sing N N 203 
LEU   N   H2   sing N N 204 
LEU   CA  C    sing N N 205 
LEU   CA  CB   sing N N 206 
LEU   CA  HA   sing N N 207 
LEU   C   O    doub N N 208 
LEU   C   OXT  sing N N 209 
LEU   CB  CG   sing N N 210 
LEU   CB  HB2  sing N N 211 
LEU   CB  HB3  sing N N 212 
LEU   CG  CD1  sing N N 213 
LEU   CG  CD2  sing N N 214 
LEU   CG  HG   sing N N 215 
LEU   CD1 HD11 sing N N 216 
LEU   CD1 HD12 sing N N 217 
LEU   CD1 HD13 sing N N 218 
LEU   CD2 HD21 sing N N 219 
LEU   CD2 HD22 sing N N 220 
LEU   CD2 HD23 sing N N 221 
LEU   OXT HXT  sing N N 222 
LYS   N   CA   sing N N 223 
LYS   N   H    sing N N 224 
LYS   N   H2   sing N N 225 
LYS   CA  C    sing N N 226 
LYS   CA  CB   sing N N 227 
LYS   CA  HA   sing N N 228 
LYS   C   O    doub N N 229 
LYS   C   OXT  sing N N 230 
LYS   CB  CG   sing N N 231 
LYS   CB  HB2  sing N N 232 
LYS   CB  HB3  sing N N 233 
LYS   CG  CD   sing N N 234 
LYS   CG  HG2  sing N N 235 
LYS   CG  HG3  sing N N 236 
LYS   CD  CE   sing N N 237 
LYS   CD  HD2  sing N N 238 
LYS   CD  HD3  sing N N 239 
LYS   CE  NZ   sing N N 240 
LYS   CE  HE2  sing N N 241 
LYS   CE  HE3  sing N N 242 
LYS   NZ  HZ1  sing N N 243 
LYS   NZ  HZ2  sing N N 244 
LYS   NZ  HZ3  sing N N 245 
LYS   OXT HXT  sing N N 246 
MET   N   CA   sing N N 247 
MET   N   H    sing N N 248 
MET   N   H2   sing N N 249 
MET   CA  C    sing N N 250 
MET   CA  CB   sing N N 251 
MET   CA  HA   sing N N 252 
MET   C   O    doub N N 253 
MET   C   OXT  sing N N 254 
MET   CB  CG   sing N N 255 
MET   CB  HB2  sing N N 256 
MET   CB  HB3  sing N N 257 
MET   CG  SD   sing N N 258 
MET   CG  HG2  sing N N 259 
MET   CG  HG3  sing N N 260 
MET   SD  CE   sing N N 261 
MET   CE  HE1  sing N N 262 
MET   CE  HE2  sing N N 263 
MET   CE  HE3  sing N N 264 
MET   OXT HXT  sing N N 265 
PHE   N   CA   sing N N 266 
PHE   N   H    sing N N 267 
PHE   N   H2   sing N N 268 
PHE   CA  C    sing N N 269 
PHE   CA  CB   sing N N 270 
PHE   CA  HA   sing N N 271 
PHE   C   O    doub N N 272 
PHE   C   OXT  sing N N 273 
PHE   CB  CG   sing N N 274 
PHE   CB  HB2  sing N N 275 
PHE   CB  HB3  sing N N 276 
PHE   CG  CD1  doub Y N 277 
PHE   CG  CD2  sing Y N 278 
PHE   CD1 CE1  sing Y N 279 
PHE   CD1 HD1  sing N N 280 
PHE   CD2 CE2  doub Y N 281 
PHE   CD2 HD2  sing N N 282 
PHE   CE1 CZ   doub Y N 283 
PHE   CE1 HE1  sing N N 284 
PHE   CE2 CZ   sing Y N 285 
PHE   CE2 HE2  sing N N 286 
PHE   CZ  HZ   sing N N 287 
PHE   OXT HXT  sing N N 288 
PRO   N   CA   sing N N 289 
PRO   N   CD   sing N N 290 
PRO   N   H    sing N N 291 
PRO   CA  C    sing N N 292 
PRO   CA  CB   sing N N 293 
PRO   CA  HA   sing N N 294 
PRO   C   O    doub N N 295 
PRO   C   OXT  sing N N 296 
PRO   CB  CG   sing N N 297 
PRO   CB  HB2  sing N N 298 
PRO   CB  HB3  sing N N 299 
PRO   CG  CD   sing N N 300 
PRO   CG  HG2  sing N N 301 
PRO   CG  HG3  sing N N 302 
PRO   CD  HD2  sing N N 303 
PRO   CD  HD3  sing N N 304 
PRO   OXT HXT  sing N N 305 
SER   N   CA   sing N N 306 
SER   N   H    sing N N 307 
SER   N   H2   sing N N 308 
SER   CA  C    sing N N 309 
SER   CA  CB   sing N N 310 
SER   CA  HA   sing N N 311 
SER   C   O    doub N N 312 
SER   C   OXT  sing N N 313 
SER   CB  OG   sing N N 314 
SER   CB  HB2  sing N N 315 
SER   CB  HB3  sing N N 316 
SER   OG  HG   sing N N 317 
SER   OXT HXT  sing N N 318 
TFA   C1  C2   sing N N 319 
TFA   C1  O    doub N N 320 
TFA   C1  OXT  sing N N 321 
TFA   C2  F1   sing N N 322 
TFA   C2  F2   sing N N 323 
TFA   C2  F3   sing N N 324 
TFA   OXT HXT  sing N N 325 
THR   N   CA   sing N N 326 
THR   N   H    sing N N 327 
THR   N   H2   sing N N 328 
THR   CA  C    sing N N 329 
THR   CA  CB   sing N N 330 
THR   CA  HA   sing N N 331 
THR   C   O    doub N N 332 
THR   C   OXT  sing N N 333 
THR   CB  OG1  sing N N 334 
THR   CB  CG2  sing N N 335 
THR   CB  HB   sing N N 336 
THR   OG1 HG1  sing N N 337 
THR   CG2 HG21 sing N N 338 
THR   CG2 HG22 sing N N 339 
THR   CG2 HG23 sing N N 340 
THR   OXT HXT  sing N N 341 
TYR   N   CA   sing N N 342 
TYR   N   H    sing N N 343 
TYR   N   H2   sing N N 344 
TYR   CA  C    sing N N 345 
TYR   CA  CB   sing N N 346 
TYR   CA  HA   sing N N 347 
TYR   C   O    doub N N 348 
TYR   C   OXT  sing N N 349 
TYR   CB  CG   sing N N 350 
TYR   CB  HB2  sing N N 351 
TYR   CB  HB3  sing N N 352 
TYR   CG  CD1  doub Y N 353 
TYR   CG  CD2  sing Y N 354 
TYR   CD1 CE1  sing Y N 355 
TYR   CD1 HD1  sing N N 356 
TYR   CD2 CE2  doub Y N 357 
TYR   CD2 HD2  sing N N 358 
TYR   CE1 CZ   doub Y N 359 
TYR   CE1 HE1  sing N N 360 
TYR   CE2 CZ   sing Y N 361 
TYR   CE2 HE2  sing N N 362 
TYR   CZ  OH   sing N N 363 
TYR   OH  HH   sing N N 364 
TYR   OXT HXT  sing N N 365 
VAL   N   CA   sing N N 366 
VAL   N   H    sing N N 367 
VAL   N   H2   sing N N 368 
VAL   CA  C    sing N N 369 
VAL   CA  CB   sing N N 370 
VAL   CA  HA   sing N N 371 
VAL   C   O    doub N N 372 
VAL   C   OXT  sing N N 373 
VAL   CB  CG1  sing N N 374 
VAL   CB  CG2  sing N N 375 
VAL   CB  HB   sing N N 376 
VAL   CG1 HG11 sing N N 377 
VAL   CG1 HG12 sing N N 378 
VAL   CG1 HG13 sing N N 379 
VAL   CG2 HG21 sing N N 380 
VAL   CG2 HG22 sing N N 381 
VAL   CG2 HG23 sing N N 382 
VAL   OXT HXT  sing N N 383 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171110 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_title         
'PanDDA analysis group deposition of SARS-CoV-2 NSP3 macrodomain ligand screen - FrankenROCS hits and analogues of AVI-313' 
_pdbx_deposit_group.group_description   
'SARS-CoV-2 NSP3 macrodomain in complex with ligands identified by X-ray diffraction using ALS 8.3.1,  SSRL 9-2, and SSRL 12-2' 
_pdbx_deposit_group.group_type          'changed state' 
_pdbx_deposit_group.group_id            G_1002304 
# 
_atom_sites.entry_id                    7HF0 
_atom_sites.fract_transf_matrix[1][1]   0.011275 
_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]   0.011275 
_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]   0.025291 
_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   ? 19.647 -16.185 22.261  0.60 54.37 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.586 -16.166 22.342  0.40 53.77 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.664 -15.120 22.423  0.60 53.99 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.639 -15.073 22.520  0.40 53.46 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.304 -13.765 22.140  0.60 52.91 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.295 -13.743 22.171  0.40 52.59 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.413 -13.484 22.595  0.60 53.44 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.412 -13.459 22.606  0.40 53.04 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.021 -15.161 23.823  0.60 54.41 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.072 -15.051 23.953  0.40 53.79 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 16.980 -14.058 23.966  0.60 54.48 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 17.050 -13.931 24.104  0.40 53.83 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.395 -16.525 24.080  0.60 54.48 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.451 -16.396 24.299  0.40 53.84 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 17.955 -15.247 21.776  0.60 64.78 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.894 -15.199 21.916  0.40 64.15 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.706 -15.016 24.494  0.60 65.29 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.794 -14.885 24.578  0.40 64.54 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.473 -14.207 24.779  0.60 65.37 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.586 -14.041 24.949  0.40 64.60 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.430 -13.200 24.011  0.60 65.37 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.510 -13.077 24.089  0.40 64.60 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.387 -14.083 23.199  0.60 65.37 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.417 -13.981 23.371  0.40 64.60 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 16.930 -16.504 24.931  0.60 65.37 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 17.030 -16.334 25.171  0.40 64.60 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.769 -16.724 23.366  0.60 65.37 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.788 -16.619 23.627  0.40 64.60 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.095 -17.196 24.102  0.60 65.37 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.147 -17.072 24.315  0.40 64.60 ?  3   VAL   A HG23 1 
ATOM   31   N N    . ASN   A 1 4   ? 18.599 -12.932 21.377  1.00 50.98 ?  4   ASN   A N    1 
ATOM   32   C CA   . ASN   A 1 4   ? 19.045 -11.586 21.039  1.00 47.03 ?  4   ASN   A CA   1 
ATOM   33   C C    . ASN   A 1 4   ? 17.902 -10.607 21.291  1.00 43.96 ?  4   ASN   A C    1 
ATOM   34   O O    . ASN   A 1 4   ? 16.798 -10.995 21.685  1.00 43.73 ?  4   ASN   A O    1 
ATOM   35   C CB   . ASN   A 1 4   ? 19.580 -11.498 19.601  1.00 45.92 ?  4   ASN   A CB   1 
ATOM   36   C CG   . ASN   A 1 4   ? 18.554 -11.901 18.565  1.00 44.73 ?  4   ASN   A CG   1 
ATOM   37   O OD1  . ASN   A 1 4   ? 17.429 -11.402 18.560  1.00 44.30 ?  4   ASN   A OD1  1 
ATOM   38   N ND2  . ASN   A 1 4   ? 18.942 -12.809 17.674  1.00 44.40 ?  4   ASN   A ND2  1 
ATOM   39   H H    A ASN   A 1 4   ? 17.834 -13.133 21.037  0.60 61.16 ?  4   ASN   A H    1 
ATOM   40   H H    B ASN   A 1 4   ? 17.846 -13.146 21.019  0.40 61.16 ?  4   ASN   A H    1 
ATOM   41   H HA   . ASN   A 1 4   ? 19.774 -11.348 21.627  1.00 56.43 ?  4   ASN   A HA   1 
ATOM   42   H HB2  . ASN   A 1 4   ? 19.845 -10.581 19.419  1.00 55.10 ?  4   ASN   A HB2  1 
ATOM   43   H HB3  . ASN   A 1 4   ? 20.344 -12.086 19.512  1.00 55.10 ?  4   ASN   A HB3  1 
ATOM   44   H HD21 . ASN   A 1 4   ? 18.400 -13.073 17.061  1.00 53.28 ?  4   ASN   A HD21 1 
ATOM   45   H HD22 . ASN   A 1 4   ? 19.738 -13.135 17.712  1.00 53.28 ?  4   ASN   A HD22 1 
ATOM   46   N N    . SER   A 1 5   ? 18.171 -9.323  21.056  1.00 40.97 ?  5   SER   A N    1 
ATOM   47   C CA   . SER   A 1 5   ? 17.261 -8.251  21.438  1.00 37.89 ?  5   SER   A CA   1 
ATOM   48   C C    . SER   A 1 5   ? 16.371 -7.771  20.292  1.00 33.43 ?  5   SER   A C    1 
ATOM   49   O O    . SER   A 1 5   ? 15.652 -6.781  20.459  1.00 33.44 ?  5   SER   A O    1 
ATOM   50   C CB   . SER   A 1 5   ? 18.040 -7.077  22.037  1.00 39.53 ?  5   SER   A CB   1 
ATOM   51   O OG   . SER   A 1 5   ? 18.959 -6.541  21.102  1.00 40.27 ?  5   SER   A OG   1 
ATOM   52   H H    . SER   A 1 5   ? 18.888 -9.048  20.666  1.00 49.16 ?  5   SER   A H    1 
ATOM   53   H HA   . SER   A 1 5   ? 16.678 -8.584  22.134  1.00 45.46 ?  5   SER   A HA   1 
ATOM   54   H HB2  . SER   A 1 5   ? 17.414 -6.383  22.298  1.00 47.43 ?  5   SER   A HB2  1 
ATOM   55   H HB3  . SER   A 1 5   ? 18.529 -7.387  22.818  1.00 47.43 ?  5   SER   A HB3  1 
ATOM   56   H HG   . SER   A 1 5   ? 19.378 -5.898  21.449  1.00 48.32 ?  5   SER   A HG   1 
ATOM   57   N N    . PHE   A 1 6   ? 16.394 -8.441  19.144  1.00 28.43 ?  6   PHE   A N    1 
ATOM   58   C CA   . PHE   A 1 6   ? 15.476 -8.089  18.067  1.00 24.05 ?  6   PHE   A CA   1 
ATOM   59   C C    . PHE   A 1 6   ? 14.054 -8.475  18.459  1.00 23.78 ?  6   PHE   A C    1 
ATOM   60   O O    . PHE   A 1 6   ? 13.813 -9.582  18.944  1.00 25.18 ?  6   PHE   A O    1 
ATOM   61   C CB   . PHE   A 1 6   ? 15.879 -8.802  16.781  1.00 21.32 ?  6   PHE   A CB   1 
ATOM   62   C CG   . PHE   A 1 6   ? 17.165 -8.295  16.186  1.00 19.45 ?  6   PHE   A CG   1 
ATOM   63   C CD1  . PHE   A 1 6   ? 17.192 -7.106  15.483  1.00 18.70 ?  6   PHE   A CD1  1 
ATOM   64   C CD2  . PHE   A 1 6   ? 18.340 -9.012  16.328  1.00 19.87 ?  6   PHE   A CD2  1 
ATOM   65   C CE1  . PHE   A 1 6   ? 18.370 -6.634  14.934  1.00 18.68 ?  6   PHE   A CE1  1 
ATOM   66   C CE2  . PHE   A 1 6   ? 19.518 -8.552  15.779  1.00 19.93 ?  6   PHE   A CE2  1 
ATOM   67   C CZ   . PHE   A 1 6   ? 19.535 -7.357  15.082  1.00 19.44 ?  6   PHE   A CZ   1 
ATOM   68   H H    . PHE   A 1 6   ? 16.922 -9.099  18.968  1.00 34.11 ?  6   PHE   A H    1 
ATOM   69   H HA   . PHE   A 1 6   ? 15.504 -7.137  17.919  1.00 28.85 ?  6   PHE   A HA   1 
ATOM   70   H HB2  . PHE   A 1 6   ? 15.986 -9.750  16.971  1.00 25.58 ?  6   PHE   A HB2  1 
ATOM   71   H HB3  . PHE   A 1 6   ? 15.174 -8.681  16.126  1.00 25.58 ?  6   PHE   A HB3  1 
ATOM   72   H HD1  . PHE   A 1 6   ? 16.407 -6.617  15.382  1.00 22.43 ?  6   PHE   A HD1  1 
ATOM   73   H HD2  . PHE   A 1 6   ? 18.331 -9.816  16.802  1.00 23.84 ?  6   PHE   A HD2  1 
ATOM   74   H HE1  . PHE   A 1 6   ? 18.377 -5.831  14.462  1.00 22.40 ?  6   PHE   A HE1  1 
ATOM   75   H HE2  . PHE   A 1 6   ? 20.304 -9.040  15.886  1.00 23.91 ?  6   PHE   A HE2  1 
ATOM   76   H HZ   . PHE   A 1 6   ? 20.328 -7.042  14.713  1.00 23.32 ?  6   PHE   A HZ   1 
ATOM   77   N N    A SER   A 1 7   ? 13.102 -7.578  18.185  0.60 22.71 ?  7   SER   A N    1 
ATOM   78   N N    B SER   A 1 7   ? 13.116 -7.545  18.300  0.40 23.29 ?  7   SER   A N    1 
ATOM   79   C CA   A SER   A 1 7   ? 11.717 -7.732  18.618  0.60 22.56 ?  7   SER   A CA   1 
ATOM   80   C CA   B SER   A 1 7   ? 11.774 -7.707  18.844  0.40 23.37 ?  7   SER   A CA   1 
ATOM   81   C C    A SER   A 1 7   ? 10.752 -7.506  17.458  0.60 20.14 ?  7   SER   A C    1 
ATOM   82   C C    B SER   A 1 7   ? 10.735 -7.380  17.785  0.40 21.68 ?  7   SER   A C    1 
ATOM   83   O O    A SER   A 1 7   ? 10.960 -6.618  16.628  0.60 20.03 ?  7   SER   A O    1 
ATOM   84   O O    B SER   A 1 7   ? 10.937 -6.491  16.954  0.40 21.67 ?  7   SER   A O    1 
ATOM   85   C CB   A SER   A 1 7   ? 11.400 -6.728  19.738  0.60 24.61 ?  7   SER   A CB   1 
ATOM   86   C CB   B SER   A 1 7   ? 11.568 -6.796  20.062  0.40 24.89 ?  7   SER   A CB   1 
ATOM   87   O OG   A SER   A 1 7   ? 10.020 -6.727  20.053  0.60 26.05 ?  7   SER   A OG   1 
ATOM   88   O OG   B SER   A 1 7   ? 10.334 -7.070  20.701  0.40 26.06 ?  7   SER   A OG   1 
ATOM   89   H H    A SER   A 1 7   ? 13.243 -6.862  17.734  0.60 27.24 ?  7   SER   A H    1 
ATOM   90   H H    B SER   A 1 7   ? 13.234 -6.809  17.872  0.40 27.94 ?  7   SER   A H    1 
ATOM   91   H HA   A SER   A 1 7   ? 11.580 -8.627  18.964  0.60 27.07 ?  7   SER   A HA   1 
ATOM   92   H HA   B SER   A 1 7   ? 11.643 -8.625  19.126  0.40 28.03 ?  7   SER   A HA   1 
ATOM   93   H HB2  A SER   A 1 7   ? 11.908 -6.969  20.531  0.60 29.52 ?  7   SER   A HB2  1 
ATOM   94   H HB2  B SER   A 1 7   ? 12.286 -6.949  20.695  0.40 29.86 ?  7   SER   A HB2  1 
ATOM   95   H HB3  A SER   A 1 7   ? 11.654 -5.838  19.446  0.60 29.52 ?  7   SER   A HB3  1 
ATOM   96   H HB3  B SER   A 1 7   ? 11.575 -5.871  19.769  0.40 29.86 ?  7   SER   A HB3  1 
ATOM   97   H HG   A SER   A 1 7   ? 9.867  -6.178  20.671  0.60 31.25 ?  7   SER   A HG   1 
ATOM   98   H HG   B SER   A 1 7   ? 10.231 -6.560  21.361  0.40 31.26 ?  7   SER   A HG   1 
ATOM   99   N N    A GLY   A 1 8   ? 9.687  -8.308  17.414  0.60 18.16 ?  8   GLY   A N    1 
ATOM   100  N N    B GLY   A 1 8   ? 9.619  -8.105  17.819  0.40 20.05 ?  8   GLY   A N    1 
ATOM   101  C CA   A GLY   A 1 8   ? 8.596  -8.075  16.487  0.60 16.99 ?  8   GLY   A CA   1 
ATOM   102  C CA   B GLY   A 1 8   ? 8.538  -7.851  16.895  0.40 18.49 ?  8   GLY   A CA   1 
ATOM   103  C C    A GLY   A 1 8   ? 8.798  -8.588  15.080  0.60 15.89 ?  8   GLY   A C    1 
ATOM   104  C C    B GLY   A 1 8   ? 8.766  -8.350  15.492  0.40 16.80 ?  8   GLY   A C    1 
ATOM   105  O O    A GLY   A 1 8   ? 8.044  -8.191  14.183  0.60 16.50 ?  8   GLY   A O    1 
ATOM   106  O O    B GLY   A 1 8   ? 8.027  -7.950  14.585  0.40 17.13 ?  8   GLY   A O    1 
ATOM   107  H H    A GLY   A 1 8   ? 9.577  -8.995  17.920  0.60 21.79 ?  8   GLY   A H    1 
ATOM   108  H H    B GLY   A 1 8   ? 9.471  -8.754  18.367  0.40 24.06 ?  8   GLY   A H    1 
ATOM   109  H HA2  A GLY   A 1 8   ? 7.792  -8.486  16.846  0.60 20.38 ?  8   GLY   A HA2  1 
ATOM   110  H HA2  B GLY   A 1 8   ? 7.732  -8.272  17.222  0.40 22.18 ?  8   GLY   A HA2  1 
ATOM   111  H HA3  A GLY   A 1 8   ? 8.438  -7.121  16.426  0.60 20.38 ?  8   GLY   A HA3  1 
ATOM   112  H HA3  B GLY   A 1 8   ? 8.384  -6.895  16.847  0.40 22.18 ?  8   GLY   A HA3  1 
ATOM   113  N N    A TYR   A 1 9   ? 9.781  -9.458  14.852  0.60 14.34 ?  9   TYR   A N    1 
ATOM   114  N N    B TYR   A 1 9   ? 9.759  -9.209  15.277  0.40 15.49 ?  9   TYR   A N    1 
ATOM   115  C CA   A TYR   A 1 9   ? 10.046 -9.988  13.523  0.60 13.06 ?  9   TYR   A CA   1 
ATOM   116  C CA   B TYR   A 1 9   ? 10.043 -9.726  13.947  0.40 14.26 ?  9   TYR   A CA   1 
ATOM   117  C C    A TYR   A 1 9   ? 9.198  -11.222 13.244  0.60 12.57 ?  9   TYR   A C    1 
ATOM   118  C C    B TYR   A 1 9   ? 9.168  -10.934 13.643  0.40 13.47 ?  9   TYR   A C    1 
ATOM   119  O O    A TYR   A 1 9   ? 8.951  -12.048 14.130  0.60 13.85 ?  9   TYR   A O    1 
ATOM   120  O O    B TYR   A 1 9   ? 8.889  -11.758 14.519  0.40 14.43 ?  9   TYR   A O    1 
ATOM   121  C CB   A TYR   A 1 9   ? 11.525 -10.355 13.359  0.60 13.19 ?  9   TYR   A CB   1 
ATOM   122  C CB   B TYR   A 1 9   ? 11.518 -10.115 13.820  0.40 14.94 ?  9   TYR   A CB   1 
ATOM   123  C CG   A TYR   A 1 9   ? 12.435 -9.151  13.258  0.60 14.00 ?  9   TYR   A CG   1 
ATOM   124  C CG   B TYR   A 1 9   ? 12.419 -8.939  13.536  0.40 15.34 ?  9   TYR   A CG   1 
ATOM   125  C CD1  A TYR   A 1 9   ? 12.797 -8.441  14.393  0.60 14.64 ?  9   TYR   A CD1  1 
ATOM   126  C CD1  B TYR   A 1 9   ? 12.685 -7.997  14.517  0.40 15.76 ?  9   TYR   A CD1  1 
ATOM   127  C CD2  A TYR   A 1 9   ? 12.913 -8.715  12.027  0.60 14.32 ?  9   TYR   A CD2  1 
ATOM   128  C CD2  B TYR   A 1 9   ? 12.989 -8.763  12.283  0.40 15.12 ?  9   TYR   A CD2  1 
ATOM   129  C CE1  A TYR   A 1 9   ? 13.609 -7.330  14.312  0.60 15.69 ?  9   TYR   A CE1  1 
ATOM   130  C CE1  B TYR   A 1 9   ? 13.496 -6.915  14.262  0.40 15.87 ?  9   TYR   A CE1  1 
ATOM   131  C CE2  A TYR   A 1 9   ? 13.731 -7.602  11.935  0.60 15.10 ?  9   TYR   A CE2  1 
ATOM   132  C CE2  B TYR   A 1 9   ? 13.800 -7.683  12.017  0.40 15.34 ?  9   TYR   A CE2  1 
ATOM   133  C CZ   A TYR   A 1 9   ? 14.070 -6.915  13.080  0.60 16.09 ?  9   TYR   A CZ   1 
ATOM   134  C CZ   B TYR   A 1 9   ? 14.049 -6.762  13.007  0.40 15.75 ?  9   TYR   A CZ   1 
ATOM   135  O OH   A TYR   A 1 9   ? 14.877 -5.812  12.988  0.60 17.46 ?  9   TYR   A OH   1 
ATOM   136  O OH   B TYR   A 1 9   ? 14.854 -5.685  12.738  0.40 16.22 ?  9   TYR   A OH   1 
ATOM   137  H H    A TYR   A 1 9   ? 10.302 -9.765  15.457  0.60 17.20 ?  9   TYR   A H    1 
ATOM   138  H H    B TYR   A 1 9   ? 10.288 -9.509  15.892  0.40 18.59 ?  9   TYR   A H    1 
ATOM   139  H HA   A TYR   A 1 9   ? 9.823  -9.322  12.858  0.60 15.66 ?  9   TYR   A HA   1 
ATOM   140  H HA   B TYR   A 1 9   ? 9.855  -9.035  13.290  0.40 17.11 ?  9   TYR   A HA   1 
ATOM   141  H HB2  A TYR   A 1 9   ? 11.807 -10.893 14.117  0.60 15.82 ?  9   TYR   A HB2  1 
ATOM   142  H HB2  B TYR   A 1 9   ? 11.813 -10.524 14.646  0.40 17.92 ?  9   TYR   A HB2  1 
ATOM   143  H HB3  A TYR   A 1 9   ? 11.612 -10.868 12.540  0.60 15.82 ?  9   TYR   A HB3  1 
ATOM   144  H HB3  B TYR   A 1 9   ? 11.613 -10.742 13.088  0.40 17.92 ?  9   TYR   A HB3  1 
ATOM   145  H HD1  A TYR   A 1 9   ? 12.476 -8.720  15.224  0.60 17.56 ?  9   TYR   A HD1  1 
ATOM   146  H HD1  B TYR   A 1 9   ? 12.305 -8.099  15.362  0.40 18.91 ?  9   TYR   A HD1  1 
ATOM   147  H HD2  A TYR   A 1 9   ? 12.679 -9.177  11.253  0.60 17.18 ?  9   TYR   A HD2  1 
ATOM   148  H HD2  B TYR   A 1 9   ? 12.823 -9.384  11.612  0.40 18.13 ?  9   TYR   A HD2  1 
ATOM   149  H HE1  A TYR   A 1 9   ? 13.845 -6.866  15.082  0.60 18.82 ?  9   TYR   A HE1  1 
ATOM   150  H HE1  B TYR   A 1 9   ? 13.665 -6.292  14.930  0.40 19.04 ?  9   TYR   A HE1  1 
ATOM   151  H HE2  A TYR   A 1 9   ? 14.052 -7.319  11.107  0.60 18.11 ?  9   TYR   A HE2  1 
ATOM   152  H HE2  B TYR   A 1 9   ? 14.183 -7.579  11.176  0.40 18.41 ?  9   TYR   A HE2  1 
ATOM   153  H HH   A TYR   A 1 9   ? 15.026 -5.493  13.752  0.60 20.95 ?  9   TYR   A HH   1 
ATOM   154  H HH   B TYR   A 1 9   ? 14.933 -5.215  13.429  0.40 19.46 ?  9   TYR   A HH   1 
ATOM   155  N N    A LEU   A 1 10  ? 8.788  -11.353 11.988  0.60 12.05 ?  10  LEU   A N    1 
ATOM   156  N N    B LEU   A 1 10  ? 8.715  -11.009 12.394  0.40 12.87 ?  10  LEU   A N    1 
ATOM   157  C CA   A LEU   A 1 10  ? 8.210  -12.585 11.479  0.60 12.31 ?  10  LEU   A CA   1 
ATOM   158  C CA   B LEU   A 1 10  ? 8.089  -12.210 11.866  0.40 12.64 ?  10  LEU   A CA   1 
ATOM   159  C C    A LEU   A 1 10  ? 9.347  -13.512 11.059  0.60 11.71 ?  10  LEU   A C    1 
ATOM   160  C C    B LEU   A 1 10  ? 9.192  -13.160 11.416  0.40 12.20 ?  10  LEU   A C    1 
ATOM   161  O O    A LEU   A 1 10  ? 10.315 -13.080 10.426  0.60 12.03 ?  10  LEU   A O    1 
ATOM   162  O O    B LEU   A 1 10  ? 10.150 -12.746 10.755  0.40 11.91 ?  10  LEU   A O    1 
ATOM   163  C CB   A LEU   A 1 10  ? 7.338  -12.262 10.267  0.60 13.55 ?  10  LEU   A CB   1 
ATOM   164  C CB   B LEU   A 1 10  ? 7.202  -11.833 10.681  0.40 13.43 ?  10  LEU   A CB   1 
ATOM   165  C CG   A LEU   A 1 10  ? 6.630  -13.437 9.590   0.60 15.65 ?  10  LEU   A CG   1 
ATOM   166  C CG   B LEU   A 1 10  ? 6.616  -12.938 9.798   0.40 15.33 ?  10  LEU   A CG   1 
ATOM   167  C CD1  A LEU   A 1 10  ? 5.542  -14.006 10.485  0.60 17.17 ?  10  LEU   A CD1  1 
ATOM   168  C CD1  B LEU   A 1 10  ? 5.428  -13.592 10.460  0.40 16.93 ?  10  LEU   A CD1  1 
ATOM   169  C CD2  A LEU   A 1 10  ? 6.069  -13.018 8.243   0.60 16.85 ?  10  LEU   A CD2  1 
ATOM   170  C CD2  B LEU   A 1 10  ? 6.228  -12.350 8.450   0.40 15.99 ?  10  LEU   A CD2  1 
ATOM   171  H H    A LEU   A 1 10  ? 8.853  -10.737 11.392  0.60 14.45 ?  10  LEU   A H    1 
ATOM   172  H H    B LEU   A 1 10  ? 8.754  -10.359 11.825  0.40 15.44 ?  10  LEU   A H    1 
ATOM   173  H HA   A LEU   A 1 10  ? 7.671  -13.021 12.158  0.60 14.76 ?  10  LEU   A HA   1 
ATOM   174  H HA   B LEU   A 1 10  ? 7.548  -12.637 12.551  0.40 15.17 ?  10  LEU   A HA   1 
ATOM   175  H HB2  A LEU   A 1 10  ? 6.649  -11.642 10.543  0.60 16.25 ?  10  LEU   A HB2  1 
ATOM   176  H HB2  B LEU   A 1 10  ? 6.445  -11.329 11.028  0.40 16.10 ?  10  LEU   A HB2  1 
ATOM   177  H HB3  A LEU   A 1 10  ? 7.896  -11.846 9.592   0.60 16.25 ?  10  LEU   A HB3  1 
ATOM   178  H HB3  B LEU   A 1 10  ? 7.718  -11.255 10.100  0.40 16.10 ?  10  LEU   A HB3  1 
ATOM   179  H HG   A LEU   A 1 10  ? 7.274  -14.144 9.429   0.60 18.77 ?  10  LEU   A HG   1 
ATOM   180  H HG   B LEU   A 1 10  ? 7.289  -13.618 9.643   0.40 18.39 ?  10  LEU   A HG   1 
ATOM   181  H HD11 A LEU   A 1 10  ? 5.104  -14.738 10.026  0.60 20.60 ?  10  LEU   A HD11 1 
ATOM   182  H HD11 B LEU   A 1 10  ? 5.086  -14.285 9.874   0.40 20.31 ?  10  LEU   A HD11 1 
ATOM   183  H HD12 A LEU   A 1 10  ? 5.943  -14.320 11.309  0.60 20.60 ?  10  LEU   A HD12 1 
ATOM   184  H HD12 B LEU   A 1 10  ? 5.711  -13.978 11.302  0.40 20.31 ?  10  LEU   A HD12 1 
ATOM   185  H HD13 A LEU   A 1 10  ? 4.897  -13.304 10.678  0.60 20.60 ?  10  LEU   A HD13 1 
ATOM   186  H HD13 B LEU   A 1 10  ? 4.746  -12.920 10.613  0.40 20.31 ?  10  LEU   A HD13 1 
ATOM   187  H HD21 A LEU   A 1 10  ? 5.622  -13.779 7.840   0.60 20.21 ?  10  LEU   A HD21 1 
ATOM   188  H HD21 B LEU   A 1 10  ? 5.830  -13.045 7.907   0.40 19.18 ?  10  LEU   A HD21 1 
ATOM   189  H HD22 A LEU   A 1 10  ? 5.439  -12.295 8.378   0.60 20.21 ?  10  LEU   A HD22 1 
ATOM   190  H HD22 B LEU   A 1 10  ? 5.592  -11.632 8.592   0.40 19.18 ?  10  LEU   A HD22 1 
ATOM   191  H HD23 A LEU   A 1 10  ? 6.799  -12.724 7.678   0.60 20.21 ?  10  LEU   A HD23 1 
ATOM   192  H HD23 B LEU   A 1 10  ? 7.026  -12.004 8.016   0.40 19.18 ?  10  LEU   A HD23 1 
ATOM   193  N N    A LYS   A 1 11  ? 9.243  -14.785 11.431  0.60 11.83 ?  11  LYS   A N    1 
ATOM   194  N N    B LYS   A 1 11  ? 9.068  -14.428 11.785  0.40 12.19 ?  11  LYS   A N    1 
ATOM   195  C CA   A LYS   A 1 11  ? 10.258 -15.779 11.101  0.60 12.36 ?  11  LYS   A CA   1 
ATOM   196  C CA   B LYS   A 1 11  ? 10.052 -15.437 11.424  0.40 12.02 ?  11  LYS   A CA   1 
ATOM   197  C C    A LYS   A 1 11  ? 9.918  -16.381 9.745   0.60 12.64 ?  11  LYS   A C    1 
ATOM   198  C C    B LYS   A 1 11  ? 9.707  -15.981 10.042  0.40 11.68 ?  11  LYS   A C    1 
ATOM   199  O O    A LYS   A 1 11  ? 8.861  -16.995 9.589   0.60 14.27 ?  11  LYS   A O    1 
ATOM   200  O O    B LYS   A 1 11  ? 8.593  -16.467 9.823   0.40 12.11 ?  11  LYS   A O    1 
ATOM   201  C CB   A LYS   A 1 11  ? 10.305 -16.853 12.190  0.60 12.72 ?  11  LYS   A CB   1 
ATOM   202  C CB   B LYS   A 1 11  ? 10.069 -16.544 12.478  0.40 12.03 ?  11  LYS   A CB   1 
ATOM   203  C CG   A LYS   A 1 11  ? 11.343 -17.958 11.993  0.60 13.28 ?  11  LYS   A CG   1 
ATOM   204  C CG   B LYS   A 1 11  ? 11.084 -17.637 12.253  0.40 11.95 ?  11  LYS   A CG   1 
ATOM   205  C CD   A LYS   A 1 11  ? 11.454 -18.791 13.273  0.60 14.26 ?  11  LYS   A CD   1 
ATOM   206  C CD   B LYS   A 1 11  ? 11.104 -18.568 13.450  0.40 12.33 ?  11  LYS   A CD   1 
ATOM   207  C CE   A LYS   A 1 11  ? 12.461 -19.929 13.173  0.60 14.49 ?  11  LYS   A CE   1 
ATOM   208  C CE   B LYS   A 1 11  ? 12.089 -19.708 13.266  0.40 12.33 ?  11  LYS   A CE   1 
ATOM   209  N NZ   A LYS   A 1 11  ? 13.821 -19.445 12.842  0.60 14.34 ?  11  LYS   A NZ   1 
ATOM   210  N NZ   B LYS   A 1 11  ? 13.500 -19.232 13.163  0.40 12.21 ?  11  LYS   A NZ   1 
ATOM   211  H H    A LYS   A 1 11  ? 8.577  -15.106 11.871  0.60 14.19 ?  11  LYS   A H    1 
ATOM   212  H H    B LYS   A 1 11  ? 8.405  -14.732 12.243  0.40 14.62 ?  11  LYS   A H    1 
ATOM   213  H HA   A LYS   A 1 11  ? 11.125 -15.353 11.041  0.60 14.83 ?  11  LYS   A HA   1 
ATOM   214  H HA   B LYS   A 1 11  ? 10.928 -15.030 11.383  0.40 14.42 ?  11  LYS   A HA   1 
ATOM   215  H HB2  A LYS   A 1 11  ? 10.506 -16.417 13.033  0.60 15.26 ?  11  LYS   A HB2  1 
ATOM   216  H HB2  B LYS   A 1 11  ? 10.261 -16.138 13.340  0.40 14.43 ?  11  LYS   A HB2  1 
ATOM   217  H HB3  A LYS   A 1 11  ? 9.437  -17.276 12.242  0.60 15.26 ?  11  LYS   A HB3  1 
ATOM   218  H HB3  B LYS   A 1 11  ? 9.202  -16.964 12.502  0.40 14.43 ?  11  LYS   A HB3  1 
ATOM   219  H HG2  A LYS   A 1 11  ? 11.065 -18.540 11.267  0.60 15.93 ?  11  LYS   A HG2  1 
ATOM   220  H HG2  B LYS   A 1 11  ? 10.841 -18.150 11.466  0.40 14.33 ?  11  LYS   A HG2  1 
ATOM   221  H HG3  A LYS   A 1 11  ? 12.209 -17.565 11.802  0.60 15.93 ?  11  LYS   A HG3  1 
ATOM   222  H HG3  B LYS   A 1 11  ? 11.967 -17.249 12.149  0.40 14.33 ?  11  LYS   A HG3  1 
ATOM   223  H HD2  A LYS   A 1 11  ? 11.729 -18.214 14.000  0.60 17.10 ?  11  LYS   A HD2  1 
ATOM   224  H HD2  B LYS   A 1 11  ? 11.366 -18.067 14.237  0.40 14.79 ?  11  LYS   A HD2  1 
ATOM   225  H HD3  A LYS   A 1 11  ? 10.587 -19.181 13.469  0.60 17.10 ?  11  LYS   A HD3  1 
ATOM   226  H HD3  B LYS   A 1 11  ? 10.218 -18.947 13.574  0.40 14.79 ?  11  LYS   A HD3  1 
ATOM   227  H HE2  A LYS   A 1 11  ? 12.504 -20.392 14.026  0.60 17.38 ?  11  LYS   A HE2  1 
ATOM   228  H HE2  B LYS   A 1 11  ? 12.029 -20.306 14.026  0.40 14.79 ?  11  LYS   A HE2  1 
ATOM   229  H HE3  A LYS   A 1 11  ? 12.181 -20.541 12.476  0.60 17.38 ?  11  LYS   A HE3  1 
ATOM   230  H HE3  B LYS   A 1 11  ? 11.874 -20.184 12.448  0.40 14.79 ?  11  LYS   A HE3  1 
ATOM   231  H HZ1  A LYS   A 1 11  ? 14.385 -20.134 12.799  0.60 17.20 ?  11  LYS   A HZ1  1 
ATOM   232  H HZ1  B LYS   A 1 11  ? 14.048 -19.925 13.064  0.40 14.64 ?  11  LYS   A HZ1  1 
ATOM   233  H HZ2  A LYS   A 1 11  ? 13.812 -19.029 12.057  0.60 17.20 ?  11  LYS   A HZ2  1 
ATOM   234  H HZ2  B LYS   A 1 11  ? 13.588 -18.690 12.462  0.40 14.64 ?  11  LYS   A HZ2  1 
ATOM   235  H HZ3  A LYS   A 1 11  ? 14.103 -18.881 13.469  0.60 17.20 ?  11  LYS   A HZ3  1 
ATOM   236  H HZ3  B LYS   A 1 11  ? 13.725 -18.788 13.901  0.40 14.64 ?  11  LYS   A HZ3  1 
ATOM   237  N N    A LEU   A 1 12  ? 10.802 -16.204 8.761   0.60 11.83 ?  12  LEU   A N    1 
ATOM   238  N N    B LEU   A 1 12  ? 10.640 -15.856 9.098   0.40 11.90 ?  12  LEU   A N    1 
ATOM   239  C CA   A LEU   A 1 12  ? 10.560 -16.798 7.448   0.60 12.31 ?  12  LEU   A CA   1 
ATOM   240  C CA   B LEU   A 1 12  ? 10.417 -16.378 7.755   0.40 12.33 ?  12  LEU   A CA   1 
ATOM   241  C C    A LEU   A 1 12  ? 11.153 -18.195 7.314   0.60 11.95 ?  12  LEU   A C    1 
ATOM   242  C C    B LEU   A 1 12  ? 10.961 -17.794 7.601   0.40 12.11 ?  12  LEU   A C    1 
ATOM   243  O O    A LEU   A 1 12  ? 10.532 -19.072 6.705   0.60 12.23 ?  12  LEU   A O    1 
ATOM   244  O O    B LEU   A 1 12  ? 10.289 -18.668 7.043   0.40 12.27 ?  12  LEU   A O    1 
ATOM   245  C CB   A LEU   A 1 12  ? 11.119 -15.907 6.334   0.60 13.21 ?  12  LEU   A CB   1 
ATOM   246  C CB   B LEU   A 1 12  ? 11.065 -15.465 6.711   0.40 13.31 ?  12  LEU   A CB   1 
ATOM   247  C CG   A LEU   A 1 12  ? 10.470 -14.534 6.180   0.60 15.01 ?  12  LEU   A CG   1 
ATOM   248  C CG   B LEU   A 1 12  ? 10.361 -14.155 6.357   0.40 14.07 ?  12  LEU   A CG   1 
ATOM   249  C CD1  A LEU   A 1 12  ? 11.222 -13.719 5.142   0.60 16.31 ?  12  LEU   A CD1  1 
ATOM   250  C CD1  B LEU   A 1 12  ? 11.073 -13.494 5.184   0.40 14.80 ?  12  LEU   A CD1  1 
ATOM   251  C CD2  A LEU   A 1 12  ? 9.002  -14.684 5.804   0.60 15.94 ?  12  LEU   A CD2  1 
ATOM   252  C CD2  B LEU   A 1 12  ? 8.893  -14.381 6.033   0.40 14.66 ?  12  LEU   A CD2  1 
ATOM   253  H H    A LEU   A 1 12  ? 11.535 -15.749 8.823   0.60 14.19 ?  12  LEU   A H    1 
ATOM   254  H H    B LEU   A 1 12  ? 11.399 -15.456 9.207   0.40 14.27 ?  12  LEU   A H    1 
ATOM   255  H HA   A LEU   A 1 12  ? 9.605  -16.874 7.316   0.60 14.76 ?  12  LEU   A HA   1 
ATOM   256  H HA   B LEU   A 1 12  ? 9.464  -16.403 7.584   0.40 14.79 ?  12  LEU   A HA   1 
ATOM   257  H HB2  A LEU   A 1 12  ? 12.063 -15.767 6.500   0.60 15.84 ?  12  LEU   A HB2  1 
ATOM   258  H HB2  B LEU   A 1 12  ? 11.950 -15.226 7.030   0.40 15.97 ?  12  LEU   A HB2  1 
ATOM   259  H HB3  A LEU   A 1 12  ? 11.011 -16.377 5.489   0.60 15.84 ?  12  LEU   A HB3  1 
ATOM   260  H HB3  B LEU   A 1 12  ? 11.150 -15.967 5.888   0.40 15.97 ?  12  LEU   A HB3  1 
ATOM   261  H HG   A LEU   A 1 12  ? 10.519 -14.069 7.025   0.60 18.00 ?  12  LEU   A HG   1 
ATOM   262  H HG   B LEU   A 1 12  ? 10.411 -13.550 7.114   0.40 16.88 ?  12  LEU   A HG   1 
ATOM   263  H HD11 A LEU   A 1 12  ? 10.799 -12.852 5.054   0.60 19.57 ?  12  LEU   A HD11 1 
ATOM   264  H HD11 B LEU   A 1 12  ? 10.629 -12.662 4.966   0.40 17.76 ?  12  LEU   A HD11 1 
ATOM   265  H HD12 A LEU   A 1 12  ? 12.143 -13.609 5.433   0.60 19.57 ?  12  LEU   A HD12 1 
ATOM   266  H HD12 B LEU   A 1 12  ? 11.997 -13.322 5.430   0.40 17.76 ?  12  LEU   A HD12 1 
ATOM   267  H HD13 A LEU   A 1 12  ? 11.201 -14.187 4.292   0.60 19.57 ?  12  LEU   A HD13 1 
ATOM   268  H HD13 B LEU   A 1 12  ? 11.046 -14.093 4.418   0.40 17.76 ?  12  LEU   A HD13 1 
ATOM   269  H HD21 A LEU   A 1 12  ? 8.621  -13.805 5.666   0.60 19.12 ?  12  LEU   A HD21 1 
ATOM   270  H HD21 B LEU   A 1 12  ? 8.537  -13.588 5.605   0.40 17.59 ?  12  LEU   A HD21 1 
ATOM   271  H HD22 A LEU   A 1 12  ? 8.937  -15.201 4.987   0.60 19.12 ?  12  LEU   A HD22 1 
ATOM   272  H HD22 B LEU   A 1 12  ? 8.817  -15.142 5.435   0.40 17.59 ?  12  LEU   A HD22 1 
ATOM   273  H HD23 A LEU   A 1 12  ? 8.530  -15.139 6.520   0.60 19.12 ?  12  LEU   A HD23 1 
ATOM   274  H HD23 B LEU   A 1 12  ? 8.411  -14.558 6.856   0.40 17.59 ?  12  LEU   A HD23 1 
ATOM   275  N N    A THR   A 1 13  ? 12.356 -18.402 7.843   0.60 12.17 ?  13  THR   A N    1 
ATOM   276  N N    B THR   A 1 13  ? 12.184 -18.023 8.067   0.40 12.09 ?  13  THR   A N    1 
ATOM   277  C CA   A THR   A 1 13  ? 13.057 -19.678 7.768   0.60 12.76 ?  13  THR   A CA   1 
ATOM   278  C CA   B THR   A 1 13  ? 12.830 -19.322 7.980   0.40 12.28 ?  13  THR   A CA   1 
ATOM   279  C C    A THR   A 1 13  ? 13.834 -19.871 9.065   0.60 13.01 ?  13  THR   A C    1 
ATOM   280  C C    B THR   A 1 13  ? 13.584 -19.563 9.278   0.40 12.83 ?  13  THR   A C    1 
ATOM   281  O O    A THR   A 1 13  ? 13.733 -19.071 10.002  0.60 13.06 ?  13  THR   A O    1 
ATOM   282  O O    B THR   A 1 13  ? 13.490 -18.789 10.237  0.40 13.13 ?  13  THR   A O    1 
ATOM   283  C CB   A THR   A 1 13  ? 14.039 -19.730 6.588   0.60 13.76 ?  13  THR   A CB   1 
ATOM   284  C CB   B THR   A 1 13  ? 13.796 -19.386 6.789   0.40 12.56 ?  13  THR   A CB   1 
ATOM   285  O OG1  A THR   A 1 13  ? 15.108 -18.810 6.827   0.60 13.73 ?  13  THR   A OG1  1 
ATOM   286  O OG1  B THR   A 1 13  ? 14.865 -18.460 7.004   0.40 12.89 ?  13  THR   A OG1  1 
ATOM   287  C CG2  A THR   A 1 13  ? 13.371 -19.391 5.271   0.60 14.71 ?  13  THR   A CG2  1 
ATOM   288  C CG2  B THR   A 1 13  ? 13.090 -19.057 5.480   0.40 12.92 ?  13  THR   A CG2  1 
ATOM   289  H H    A THR   A 1 13  ? 12.797 -17.799 8.260   0.60 14.60 ?  13  THR   A H    1 
ATOM   290  H H    B THR   A 1 13  ? 12.670 -17.418 8.440   0.40 14.50 ?  13  THR   A H    1 
ATOM   291  H HA   A THR   A 1 13  ? 12.416 -20.405 7.670   0.60 15.30 ?  13  THR   A HA   1 
ATOM   292  H HA   B THR   A 1 13  ? 12.159 -20.012 7.876   0.40 14.72 ?  13  THR   A HA   1 
ATOM   293  H HB   A THR   A 1 13  ? 14.407 -20.625 6.516   0.60 16.50 ?  13  THR   A HB   1 
ATOM   294  H HB   B THR   A 1 13  ? 14.162 -20.281 6.724   0.40 15.07 ?  13  THR   A HB   1 
ATOM   295  H HG1  A THR   A 1 13  ? 15.646 -18.823 6.181   0.60 16.47 ?  13  THR   A HG1  1 
ATOM   296  H HG1  B THR   A 1 13  ? 15.403 -18.484 6.360   0.40 15.47 ?  13  THR   A HG1  1 
ATOM   297  H HG21 A THR   A 1 13  ? 13.981 -19.570 4.537   0.60 17.64 ?  13  THR   A HG21 1 
ATOM   298  H HG21 B THR   A 1 13  ? 13.704 -19.172 4.736   0.40 15.49 ?  13  THR   A HG21 1 
ATOM   299  H HG22 A THR   A 1 13  ? 12.576 -19.936 5.156   0.60 17.64 ?  13  THR   A HG22 1 
ATOM   300  H HG22 B THR   A 1 13  ? 12.334 -19.653 5.355   0.40 15.49 ?  13  THR   A HG22 1 
ATOM   301  H HG23 A THR   A 1 13  ? 13.120 -18.457 5.256   0.60 17.64 ?  13  THR   A HG23 1 
ATOM   302  H HG23 B THR   A 1 13  ? 12.774 -18.143 5.491   0.40 15.49 ?  13  THR   A HG23 1 
ATOM   303  N N    A ASP   A 1 14  ? 14.655 -20.924 9.099   0.60 13.76 ?  14  ASP   A N    1 
ATOM   304  N N    B ASP   A 1 14  ? 14.352 -20.649 9.291   0.40 13.35 ?  14  ASP   A N    1 
ATOM   305  C CA   A ASP   A 1 14  ? 15.481 -21.183 10.272  0.60 14.70 ?  14  ASP   A CA   1 
ATOM   306  C CA   B ASP   A 1 14  ? 15.210 -20.941 10.427  0.40 14.43 ?  14  ASP   A CA   1 
ATOM   307  C C    A ASP   A 1 14  ? 16.292 -19.962 10.699  0.60 14.38 ?  14  ASP   A C    1 
ATOM   308  C C    B ASP   A 1 14  ? 16.094 -19.752 10.768  0.40 14.08 ?  14  ASP   A C    1 
ATOM   309  O O    A ASP   A 1 14  ? 16.573 -19.792 11.891  0.60 14.99 ?  14  ASP   A O    1 
ATOM   310  O O    B ASP   A 1 14  ? 16.257 -19.412 11.946  0.40 14.05 ?  14  ASP   A O    1 
ATOM   311  C CB   A ASP   A 1 14  ? 16.428 -22.353 9.993   0.60 17.54 ?  14  ASP   A CB   1 
ATOM   312  C CB   B ASP   A 1 14  ? 16.083 -22.149 10.108  0.40 16.77 ?  14  ASP   A CB   1 
ATOM   313  C CG   A ASP   A 1 14  ? 17.377 -22.610 11.142  0.60 21.40 ?  14  ASP   A CG   1 
ATOM   314  C CG   B ASP   A 1 14  ? 16.974 -22.527 11.259  0.40 19.34 ?  14  ASP   A CG   1 
ATOM   315  O OD1  A ASP   A 1 14  ? 16.895 -22.815 12.275  0.60 22.56 ?  14  ASP   A OD1  1 
ATOM   316  O OD1  B ASP   A 1 14  ? 16.474 -23.134 12.229  0.40 19.87 ?  14  ASP   A OD1  1 
ATOM   317  O OD2  A ASP   A 1 14  ? 18.602 -22.607 10.913  0.60 23.74 -1 14  ASP   A OD2  1 
ATOM   318  O OD2  B ASP   A 1 14  ? 18.173 -22.194 11.201  0.40 20.85 -1 14  ASP   A OD2  1 
ATOM   319  H H    A ASP   A 1 14  ? 14.759 -21.498 8.457   0.60 16.51 ?  14  ASP   A H    1 
ATOM   320  H H    B ASP   A 1 14  ? 14.396 -21.215 8.659   0.40 16.01 ?  14  ASP   A H    1 
ATOM   321  H HA   A ASP   A 1 14  ? 14.913 -21.437 11.011  0.60 17.63 ?  14  ASP   A HA   1 
ATOM   322  H HA   B ASP   A 1 14  ? 14.663 -21.147 11.204  0.40 17.31 ?  14  ASP   A HA   1 
ATOM   323  H HB2  A ASP   A 1 14  ? 15.901 -23.163 9.835   0.60 21.04 ?  14  ASP   A HB2  1 
ATOM   324  H HB2  B ASP   A 1 14  ? 15.508 -22.896 9.871   0.40 20.11 ?  14  ASP   A HB2  1 
ATOM   325  H HB3  A ASP   A 1 14  ? 16.968 -22.161 9.213   0.60 21.04 ?  14  ASP   A HB3  1 
ATOM   326  H HB3  B ASP   A 1 14  ? 16.665 -21.930 9.365   0.40 20.11 ?  14  ASP   A HB3  1 
ATOM   327  N N    . ASN   A 1 15  ? 16.672 -19.100 9.752   1.00 14.00 ?  15  ASN   A N    1 
ATOM   328  C CA   . ASN   A 1 15  ? 17.662 -18.056 9.998   1.00 14.69 ?  15  ASN   A CA   1 
ATOM   329  C C    . ASN   A 1 15  ? 17.293 -16.666 9.493   1.00 14.79 ?  15  ASN   A C    1 
ATOM   330  O O    . ASN   A 1 15  ? 18.061 -15.735 9.735   1.00 16.11 ?  15  ASN   A O    1 
ATOM   331  C CB   . ASN   A 1 15  ? 19.033 -18.455 9.416   1.00 13.88 ?  15  ASN   A CB   1 
ATOM   332  C CG   . ASN   A 1 15  ? 19.021 -18.541 7.906   1.00 14.40 ?  15  ASN   A CG   1 
ATOM   333  O OD1  . ASN   A 1 15  ? 18.307 -19.365 7.328   1.00 15.64 ?  15  ASN   A OD1  1 
ATOM   334  N ND2  . ASN   A 1 15  ? 19.811 -17.687 7.254   1.00 14.76 ?  15  ASN   A ND2  1 
ATOM   335  H H    A ASN   A 1 15  ? 16.361 -19.098 8.955   0.60 16.80 ?  15  ASN   A H    1 
ATOM   336  H H    B ASN   A 1 15  ? 16.513 -19.251 8.924   0.40 16.80 ?  15  ASN   A H    1 
ATOM   337  H HA   . ASN   A 1 15  ? 17.792 -17.975 10.954  1.00 17.62 ?  15  ASN   A HA   1 
ATOM   338  H HB2  . ASN   A 1 15  ? 19.698 -17.788 9.676   1.00 16.65 ?  15  ASN   A HB2  1 
ATOM   339  H HB3  . ASN   A 1 15  ? 19.293 -19.323 9.765   1.00 16.65 ?  15  ASN   A HB3  1 
ATOM   340  H HD21 . ASN   A 1 15  ? 19.838 -17.694 6.394   1.00 17.71 ?  15  ASN   A HD21 1 
ATOM   341  H HD22 . ASN   A 1 15  ? 20.299 -17.121 7.689   1.00 17.71 ?  15  ASN   A HD22 1 
ATOM   342  N N    A VAL   A 1 16  ? 16.168 -16.493 8.799   0.60 13.95 ?  16  VAL   A N    1 
ATOM   343  N N    B VAL   A 1 16  ? 16.146 -16.489 8.839   0.40 14.19 ?  16  VAL   A N    1 
ATOM   344  C CA   A VAL   A 1 16  ? 15.784 -15.209 8.222   0.60 13.52 ?  16  VAL   A CA   1 
ATOM   345  C CA   B VAL   A 1 16  ? 15.749 -15.206 8.266   0.40 13.82 ?  16  VAL   A CA   1 
ATOM   346  C C    A VAL   A 1 16  ? 14.493 -14.725 8.865   0.60 13.11 ?  16  VAL   A C    1 
ATOM   347  C C    B VAL   A 1 16  ? 14.508 -14.694 8.986   0.40 13.58 ?  16  VAL   A C    1 
ATOM   348  O O    A VAL   A 1 16  ? 13.496 -15.455 8.916   0.60 13.43 ?  16  VAL   A O    1 
ATOM   349  O O    B VAL   A 1 16  ? 13.514 -15.418 9.127   0.40 14.01 ?  16  VAL   A O    1 
ATOM   350  C CB   A VAL   A 1 16  ? 15.641 -15.275 6.692   0.60 13.99 ?  16  VAL   A CB   1 
ATOM   351  C CB   B VAL   A 1 16  ? 15.518 -15.310 6.748   0.40 13.96 ?  16  VAL   A CB   1 
ATOM   352  C CG1  A VAL   A 1 16  ? 15.224 -13.912 6.140   0.60 14.69 ?  16  VAL   A CG1  1 
ATOM   353  C CG1  B VAL   A 1 16  ? 15.064 -13.972 6.176   0.40 14.35 ?  16  VAL   A CG1  1 
ATOM   354  C CG2  A VAL   A 1 16  ? 16.938 -15.746 6.055   0.60 14.97 ?  16  VAL   A CG2  1 
ATOM   355  C CG2  B VAL   A 1 16  ? 16.782 -15.795 6.046   0.40 14.46 ?  16  VAL   A CG2  1 
ATOM   356  H H    A VAL   A 1 16  ? 15.601 -17.122 8.653   0.60 16.73 ?  16  VAL   A H    1 
ATOM   357  H H    B VAL   A 1 16  ? 15.569 -17.115 8.720   0.40 17.02 ?  16  VAL   A H    1 
ATOM   358  H HA   A VAL   A 1 16  ? 16.475 -14.559 8.423   0.60 16.22 ?  16  VAL   A HA   1 
ATOM   359  H HA   B VAL   A 1 16  ? 16.459 -14.566 8.415   0.40 16.58 ?  16  VAL   A HA   1 
ATOM   360  H HB   A VAL   A 1 16  ? 14.949 -15.916 6.470   0.60 16.79 ?  16  VAL   A HB   1 
ATOM   361  H HB   B VAL   A 1 16  ? 14.819 -15.959 6.582   0.40 16.74 ?  16  VAL   A HB   1 
ATOM   362  H HG11 A VAL   A 1 16  ? 15.340 -13.919 5.179   0.60 17.62 ?  16  VAL   A HG11 1 
ATOM   363  H HG11 B VAL   A 1 16  ? 15.107 -14.017 5.208   0.40 17.22 ?  16  VAL   A HG11 1 
ATOM   364  H HG12 A VAL   A 1 16  ? 14.293 -13.755 6.360   0.60 17.62 ?  16  VAL   A HG12 1 
ATOM   365  H HG12 B VAL   A 1 16  ? 14.154 -13.800 6.458   0.40 17.22 ?  16  VAL   A HG12 1 
ATOM   366  H HG13 A VAL   A 1 16  ? 15.782 -13.229 6.539   0.60 17.62 ?  16  VAL   A HG13 1 
ATOM   367  H HG13 B VAL   A 1 16  ? 15.653 -13.275 6.501   0.40 17.22 ?  16  VAL   A HG13 1 
ATOM   368  H HG21 A VAL   A 1 16  ? 16.854 -15.686 5.091   0.60 17.96 ?  16  VAL   A HG21 1 
ATOM   369  H HG21 B VAL   A 1 16  ? 16.628 -15.804 5.089   0.40 17.35 ?  16  VAL   A HG21 1 
ATOM   370  H HG22 A VAL   A 1 16  ? 17.664 -15.181 6.361   0.60 17.96 ?  16  VAL   A HG22 1 
ATOM   371  H HG22 B VAL   A 1 16  ? 17.513 -15.192 6.257   0.40 17.35 ?  16  VAL   A HG22 1 
ATOM   372  H HG23 A VAL   A 1 16  ? 17.103 -16.665 6.318   0.60 17.96 ?  16  VAL   A HG23 1 
ATOM   373  H HG23 B VAL   A 1 16  ? 16.995 -16.690 6.356   0.40 17.35 ?  16  VAL   A HG23 1 
ATOM   374  N N    A TYR   A 1 17  ? 14.513 -13.469 9.299   0.60 13.21 ?  17  TYR   A N    1 
ATOM   375  N N    B TYR   A 1 17  ? 14.571 -13.438 9.425   0.40 13.43 ?  17  TYR   A N    1 
ATOM   376  C CA   A TYR   A 1 17  ? 13.427 -12.797 9.992   0.60 13.13 ?  17  TYR   A CA   1 
ATOM   377  C CA   B TYR   A 1 17  ? 13.490 -12.750 10.118  0.40 12.89 ?  17  TYR   A CA   1 
ATOM   378  C C    A TYR   A 1 17  ? 13.172 -11.466 9.301   0.60 13.09 ?  17  TYR   A C    1 
ATOM   379  C C    B TYR   A 1 17  ? 13.207 -11.437 9.391   0.40 12.47 ?  17  TYR   A C    1 
ATOM   380  O O    A TYR   A 1 17  ? 14.111 -10.830 8.815   0.60 13.53 ?  17  TYR   A O    1 
ATOM   381  O O    B TYR   A 1 17  ? 14.026 -10.972 8.594   0.40 12.57 ?  17  TYR   A O    1 
ATOM   382  C CB   A TYR   A 1 17  ? 13.852 -12.532 11.435  0.60 13.81 ?  17  TYR   A CB   1 
ATOM   383  C CB   B TYR   A 1 17  ? 13.885 -12.491 11.583  0.40 13.58 ?  17  TYR   A CB   1 
ATOM   384  C CG   A TYR   A 1 17  ? 14.017 -13.787 12.250  0.60 14.79 ?  17  TYR   A CG   1 
ATOM   385  C CG   B TYR   A 1 17  ? 14.161 -13.762 12.376  0.40 14.41 ?  17  TYR   A CG   1 
ATOM   386  C CD1  A TYR   A 1 17  ? 15.179 -14.548 12.182  0.60 15.50 ?  17  TYR   A CD1  1 
ATOM   387  C CD1  B TYR   A 1 17  ? 15.373 -14.441 12.262  0.40 15.19 ?  17  TYR   A CD1  1 
ATOM   388  C CD2  A TYR   A 1 17  ? 13.001 -14.221 13.084  0.60 14.98 ?  17  TYR   A CD2  1 
ATOM   389  C CD2  B TYR   A 1 17  ? 13.203 -14.284 13.239  0.40 14.76 ?  17  TYR   A CD2  1 
ATOM   390  C CE1  A TYR   A 1 17  ? 15.319 -15.714 12.927  0.60 15.55 ?  17  TYR   A CE1  1 
ATOM   391  C CE1  B TYR   A 1 17  ? 15.617 -15.608 12.983  0.40 15.93 ?  17  TYR   A CE1  1 
ATOM   392  C CE2  A TYR   A 1 17  ? 13.127 -15.382 13.830  0.60 15.26 ?  17  TYR   A CE2  1 
ATOM   393  C CE2  B TYR   A 1 17  ? 13.440 -15.447 13.963  0.40 15.47 ?  17  TYR   A CE2  1 
ATOM   394  C CZ   A TYR   A 1 17  ? 14.287 -16.124 13.752  0.60 15.20 ?  17  TYR   A CZ   1 
ATOM   395  C CZ   B TYR   A 1 17  ? 14.646 -16.102 13.831  0.40 16.09 ?  17  TYR   A CZ   1 
ATOM   396  O OH   A TYR   A 1 17  ? 14.414 -17.273 14.501  0.60 15.50 ?  17  TYR   A OH   1 
ATOM   397  O OH   B TYR   A 1 17  ? 14.881 -17.254 14.553  0.40 16.57 ?  17  TYR   A OH   1 
ATOM   398  H H    A TYR   A 1 17  ? 15.189 -12.949 9.180   0.60 15.84 ?  17  TYR   A H    1 
ATOM   399  H H    B TYR   A 1 17  ? 15.267 -12.941 9.320   0.40 16.11 ?  17  TYR   A H    1 
ATOM   400  H HA   A TYR   A 1 17  ? 12.621 -13.339 9.980   0.60 15.75 ?  17  TYR   A HA   1 
ATOM   401  H HA   B TYR   A 1 17  ? 12.692 -13.300 10.098  0.40 15.46 ?  17  TYR   A HA   1 
ATOM   402  H HB2  A TYR   A 1 17  ? 14.701 -12.070 11.431  0.60 16.56 ?  17  TYR   A HB2  1 
ATOM   403  H HB2  B TYR   A 1 17  ? 14.688 -11.949 11.597  0.40 16.30 ?  17  TYR   A HB2  1 
ATOM   404  H HB3  A TYR   A 1 17  ? 13.181 -11.990 11.866  0.60 16.56 ?  17  TYR   A HB3  1 
ATOM   405  H HB3  B TYR   A 1 17  ? 13.159 -12.017 12.020  0.40 16.30 ?  17  TYR   A HB3  1 
ATOM   406  H HD1  A TYR   A 1 17  ? 15.874 -14.277 11.625  0.60 18.60 ?  17  TYR   A HD1  1 
ATOM   407  H HD1  B TYR   A 1 17  ? 16.028 -14.118 11.691  0.40 18.22 ?  17  TYR   A HD1  1 
ATOM   408  H HD2  A TYR   A 1 17  ? 12.212 -13.731 13.138  0.60 17.97 ?  17  TYR   A HD2  1 
ATOM   409  H HD2  B TYR   A 1 17  ? 12.386 -13.850 13.332  0.40 17.70 ?  17  TYR   A HD2  1 
ATOM   410  H HE1  A TYR   A 1 17  ? 16.105 -16.216 12.875  0.60 18.66 ?  17  TYR   A HE1  1 
ATOM   411  H HE1  B TYR   A 1 17  ? 16.431 -16.057 12.900  0.40 19.10 ?  17  TYR   A HE1  1 
ATOM   412  H HE2  A TYR   A 1 17  ? 12.434 -15.657 14.385  0.60 18.30 ?  17  TYR   A HE2  1 
ATOM   413  H HE2  B TYR   A 1 17  ? 12.787 -15.784 14.538  0.40 18.56 ?  17  TYR   A HE2  1 
ATOM   414  H HH   A TYR   A 1 17  ? 13.671 -17.484 14.829  0.60 18.59 ?  17  TYR   A HH   1 
ATOM   415  H HH   B TYR   A 1 17  ? 15.622 -17.591 14.340  0.40 19.88 ?  17  TYR   A HH   1 
ATOM   416  N N    A ILE   A 1 18  ? 11.905 -11.033 9.256   0.60 12.21 ?  18  ILE   A N    1 
ATOM   417  N N    B ILE   A 1 18  ? 12.049 -10.824 9.669   0.40 11.77 ?  18  ILE   A N    1 
ATOM   418  C CA   A ILE   A 1 18  ? 11.533 -9.844  8.493   0.60 12.17 ?  18  ILE   A CA   1 
ATOM   419  C CA   B ILE   A 1 18  ? 11.622 -9.632  8.934   0.40 11.38 ?  18  ILE   A CA   1 
ATOM   420  C C    A ILE   A 1 18  ? 10.545 -8.983  9.274   0.60 12.41 ?  18  ILE   A C    1 
ATOM   421  C C    B ILE   A 1 18  ? 10.675 -8.788  9.781   0.40 11.03 ?  18  ILE   A C    1 
ATOM   422  O O    A ILE   A 1 18  ? 9.711  -9.493  10.027  0.60 12.55 ?  18  ILE   A O    1 
ATOM   423  O O    B ILE   A 1 18  ? 9.853  -9.309  10.542  0.40 11.65 ?  18  ILE   A O    1 
ATOM   424  C CB   A ILE   A 1 18  ? 10.997 -10.255 7.103   0.60 12.09 ?  18  ILE   A CB   1 
ATOM   425  C CB   B ILE   A 1 18  ? 10.993 -9.997  7.569   0.40 11.21 ?  18  ILE   A CB   1 
ATOM   426  C CG1  A ILE   A 1 18  ? 10.959 -9.061  6.151   0.60 12.13 ?  18  ILE   A CG1  1 
ATOM   427  C CG1  B ILE   A 1 18  ? 10.907 -8.762  6.671   0.40 12.12 ?  18  ILE   A CG1  1 
ATOM   428  C CG2  A ILE   A 1 18  ? 9.645  -10.953 7.228   0.60 12.20 ?  18  ILE   A CG2  1 
ATOM   429  C CG2  B ILE   A 1 18  ? 9.626  -10.660 7.755   0.40 11.92 ?  18  ILE   A CG2  1 
ATOM   430  C CD1  A ILE   A 1 18  ? 10.803 -9.472  4.708   0.60 13.50 ?  18  ILE   A CD1  1 
ATOM   431  C CD1  B ILE   A 1 18  ? 10.621 -9.091  5.227   0.40 12.88 ?  18  ILE   A CD1  1 
ATOM   432  H H    A ILE   A 1 18  ? 11.245 -11.435 9.644   0.60 14.64 ?  18  ILE   A H    1 
ATOM   433  H H    B ILE   A 1 18  ? 11.512 -11.072 10.285  0.40 14.12 ?  18  ILE   A H    1 
ATOM   434  H HA   A ILE   A 1 18  ? 12.336 -9.320  8.351   0.60 14.59 ?  18  ILE   A HA   1 
ATOM   435  H HA   B ILE   A 1 18  ? 12.407 -9.091  8.752   0.40 13.65 ?  18  ILE   A HA   1 
ATOM   436  H HB   A ILE   A 1 18  ? 11.618 -10.901 6.728   0.60 14.50 ?  18  ILE   A HB   1 
ATOM   437  H HB   B ILE   A 1 18  ? 11.576 -10.633 7.136   0.40 13.44 ?  18  ILE   A HB   1 
ATOM   438  H HG12 A ILE   A 1 18  ? 10.214 -8.492  6.384   0.60 14.55 ?  18  ILE   A HG12 1 
ATOM   439  H HG12 B ILE   A 1 18  ? 10.197 -8.183  6.989   0.40 14.53 ?  18  ILE   A HG12 1 
ATOM   440  H HG13 A ILE   A 1 18  ? 11.794 -8.568  6.230   0.60 14.55 ?  18  ILE   A HG13 1 
ATOM   441  H HG13 B ILE   A 1 18  ? 11.756 -8.287  6.703   0.40 14.53 ?  18  ILE   A HG13 1 
ATOM   442  H HG21 A ILE   A 1 18  ? 9.412  -11.347 6.371   0.60 14.64 ?  18  ILE   A HG21 1 
ATOM   443  H HG21 B ILE   A 1 18  ? 9.343  -11.039 6.907   0.40 14.30 ?  18  ILE   A HG21 1 
ATOM   444  H HG22 A ILE   A 1 18  ? 9.708  -11.647 7.902   0.60 14.64 ?  18  ILE   A HG22 1 
ATOM   445  H HG22 B ILE   A 1 18  ? 9.705  -11.359 8.421   0.40 14.30 ?  18  ILE   A HG22 1 
ATOM   446  H HG23 A ILE   A 1 18  ? 8.973  -10.302 7.485   0.60 14.64 ?  18  ILE   A HG23 1 
ATOM   447  H HG23 B ILE   A 1 18  ? 8.983  -9.994  8.048   0.40 14.30 ?  18  ILE   A HG23 1 
ATOM   448  H HD11 A ILE   A 1 18  ? 10.825 -8.678  4.150   0.60 16.19 ?  18  ILE   A HD11 1 
ATOM   449  H HD11 B ILE   A 1 18  ? 10.610 -8.270  4.709   0.40 15.45 ?  18  ILE   A HD11 1 
ATOM   450  H HD12 A ILE   A 1 18  ? 11.530 -10.066 4.467   0.60 16.19 ?  18  ILE   A HD12 1 
ATOM   451  H HD12 B ILE   A 1 18  ? 11.317 -9.681  4.893   0.40 15.45 ?  18  ILE   A HD12 1 
ATOM   452  H HD13 A ILE   A 1 18  ? 9.953  -9.927  4.602   0.60 16.19 ?  18  ILE   A HD13 1 
ATOM   453  H HD13 B ILE   A 1 18  ? 9.759  -9.531  5.168   0.40 15.45 ?  18  ILE   A HD13 1 
ATOM   454  N N    A LYS   A 1 19  ? 10.631 -7.666  9.077   0.60 12.36 ?  19  LYS   A N    1 
ATOM   455  N N    B LYS   A 1 19  ? 10.777 -7.467  9.612   0.40 11.40 ?  19  LYS   A N    1 
ATOM   456  C CA   A LYS   A 1 19  ? 9.802  -6.717  9.811   0.60 13.06 ?  19  LYS   A CA   1 
ATOM   457  C CA   B LYS   A 1 19  ? 9.982  -6.518  10.377  0.40 12.86 ?  19  LYS   A CA   1 
ATOM   458  C C    A LYS   A 1 19  ? 9.644  -5.443  8.990   0.60 13.19 ?  19  LYS   A C    1 
ATOM   459  C C    B LYS   A 1 19  ? 9.775  -5.272  9.533   0.40 13.57 ?  19  LYS   A C    1 
ATOM   460  O O    A LYS   A 1 19  ? 10.554 -5.050  8.256   0.60 12.65 ?  19  LYS   A O    1 
ATOM   461  O O    B LYS   A 1 19  ? 10.685 -4.846  8.820   0.40 13.81 ?  19  LYS   A O    1 
ATOM   462  C CB   A LYS   A 1 19  ? 10.464 -6.388  11.158  0.60 14.48 ?  19  LYS   A CB   1 
ATOM   463  C CB   B LYS   A 1 19  ? 10.712 -6.141  11.673  0.40 13.68 ?  19  LYS   A CB   1 
ATOM   464  C CG   A LYS   A 1 19  ? 9.725  -5.395  12.050  0.60 16.30 ?  19  LYS   A CG   1 
ATOM   465  C CG   B LYS   A 1 19  ? 9.961  -5.211  12.613  0.40 14.87 ?  19  LYS   A CG   1 
ATOM   466  C CD   A LYS   A 1 19  ? 10.550 -5.129  13.308  0.60 17.92 ?  19  LYS   A CD   1 
ATOM   467  C CD   B LYS   A 1 19  ? 10.877 -4.791  13.755  0.40 15.95 ?  19  LYS   A CD   1 
ATOM   468  C CE   A LYS   A 1 19  ? 9.885  -4.142  14.251  0.60 18.93 ?  19  LYS   A CE   1 
ATOM   469  C CE   B LYS   A 1 19  ? 10.136 -4.068  14.861  0.40 16.93 ?  19  LYS   A CE   1 
ATOM   470  N NZ   A LYS   A 1 19  ? 10.761 -3.843  15.423  0.60 19.41 ?  19  LYS   A NZ   1 
ATOM   471  N NZ   B LYS   A 1 19  ? 11.041 -3.786  16.013  0.40 17.52 ?  19  LYS   A NZ   1 
ATOM   472  H H    A LYS   A 1 19  ? 11.170 -7.310  8.519   0.60 14.83 ?  19  LYS   A H    1 
ATOM   473  H H    B LYS   A 1 19  ? 11.312 -7.082  9.047   0.40 13.67 ?  19  LYS   A H    1 
ATOM   474  H HA   A LYS   A 1 19  ? 8.926  -7.115  9.977   0.60 15.67 ?  19  LYS   A HA   1 
ATOM   475  H HA   B LYS   A 1 19  ? 9.119  -6.897  10.596  0.40 15.43 ?  19  LYS   A HA   1 
ATOM   476  H HB2  A LYS   A 1 19  ? 10.553 -7.215  11.664  0.60 17.37 ?  19  LYS   A HB2  1 
ATOM   477  H HB2  B LYS   A 1 19  ? 10.896 -6.956  12.167  0.40 16.41 ?  19  LYS   A HB2  1 
ATOM   478  H HB3  A LYS   A 1 19  ? 11.341 -6.025  10.981  0.60 17.37 ?  19  LYS   A HB3  1 
ATOM   479  H HB3  B LYS   A 1 19  ? 11.548 -5.706  11.445  0.40 16.41 ?  19  LYS   A HB3  1 
ATOM   480  H HG2  A LYS   A 1 19  ? 9.605  -4.556  11.577  0.60 19.55 ?  19  LYS   A HG2  1 
ATOM   481  H HG2  B LYS   A 1 19  ? 9.681  -4.416  12.136  0.40 17.84 ?  19  LYS   A HG2  1 
ATOM   482  H HG3  A LYS   A 1 19  ? 8.867  -5.763  12.315  0.60 19.55 ?  19  LYS   A HG3  1 
ATOM   483  H HG3  B LYS   A 1 19  ? 9.195  -5.674  12.988  0.40 17.84 ?  19  LYS   A HG3  1 
ATOM   484  H HD2  A LYS   A 1 19  ? 10.675 -5.962  13.789  0.60 21.50 ?  19  LYS   A HD2  1 
ATOM   485  H HD2  B LYS   A 1 19  ? 11.272 -5.585  14.141  0.40 19.13 ?  19  LYS   A HD2  1 
ATOM   486  H HD3  A LYS   A 1 19  ? 11.412 -4.763  13.051  0.60 21.50 ?  19  LYS   A HD3  1 
ATOM   487  H HD3  B LYS   A 1 19  ? 11.570 -4.204  13.412  0.40 19.13 ?  19  LYS   A HD3  1 
ATOM   488  H HE2  A LYS   A 1 19  ? 9.715  -3.310  13.781  0.60 22.71 ?  19  LYS   A HE2  1 
ATOM   489  H HE2  B LYS   A 1 19  ? 9.798  -3.225  14.524  0.40 20.31 ?  19  LYS   A HE2  1 
ATOM   490  H HE3  A LYS   A 1 19  ? 9.055  -4.518  14.581  0.60 22.71 ?  19  LYS   A HE3  1 
ATOM   491  H HE3  B LYS   A 1 19  ? 9.406  -4.625  15.175  0.40 20.31 ?  19  LYS   A HE3  1 
ATOM   492  H HZ1  A LYS   A 1 19  ? 10.360 -3.261  15.964  0.60 23.28 ?  19  LYS   A HZ1  1 
ATOM   493  H HZ1  B LYS   A 1 19  ? 10.591 -3.362  16.654  0.40 21.02 ?  19  LYS   A HZ1  1 
ATOM   494  H HZ2  A LYS   A 1 19  ? 10.928 -4.591  15.877  0.60 23.28 ?  19  LYS   A HZ2  1 
ATOM   495  H HZ2  B LYS   A 1 19  ? 11.362 -4.548  16.341  0.40 21.02 ?  19  LYS   A HZ2  1 
ATOM   496  H HZ3  A LYS   A 1 19  ? 11.533 -3.496  15.146  0.60 23.28 ?  19  LYS   A HZ3  1 
ATOM   497  H HZ3  B LYS   A 1 19  ? 11.719 -3.275  15.749  0.40 21.02 ?  19  LYS   A HZ3  1 
ATOM   498  N N    A ASN   A 1 20  ? 8.477  -4.808  9.107   0.60 14.12 ?  20  ASN   A N    1 
ATOM   499  N N    B ASN   A 1 20  ? 8.575  -4.706  9.598   0.40 14.72 ?  20  ASN   A N    1 
ATOM   500  C CA   A ASN   A 1 20  ? 8.258  -3.477  8.538   0.60 15.10 ?  20  ASN   A CA   1 
ATOM   501  C CA   B ASN   A 1 20  ? 8.329  -3.391  9.018   0.40 16.45 ?  20  ASN   A CA   1 
ATOM   502  C C    A ASN   A 1 20  ? 8.863  -2.465  9.504   0.60 16.33 ?  20  ASN   A C    1 
ATOM   503  C C    B ASN   A 1 20  ? 8.974  -2.368  9.938   0.40 16.92 ?  20  ASN   A C    1 
ATOM   504  O O    A ASN   A 1 20  ? 8.300  -2.199  10.568  0.60 17.97 ?  20  ASN   A O    1 
ATOM   505  O O    B ASN   A 1 20  ? 8.466  -2.080  11.024  0.40 17.59 ?  20  ASN   A O    1 
ATOM   506  C CB   A ASN   A 1 20  ? 6.765  -3.229  8.339   0.60 15.51 ?  20  ASN   A CB   1 
ATOM   507  C CB   B ASN   A 1 20  ? 6.830  -3.150  8.885   0.40 18.22 ?  20  ASN   A CB   1 
ATOM   508  C CG   A ASN   A 1 20  ? 6.443  -1.795  7.948   0.60 16.52 ?  20  ASN   A CG   1 
ATOM   509  C CG   B ASN   A 1 20  ? 6.499  -1.724  8.498   0.40 20.07 ?  20  ASN   A CG   1 
ATOM   510  O OD1  A ASN   A 1 20  ? 5.390  -1.265  8.317   0.60 17.94 ?  20  ASN   A OD1  1 
ATOM   511  O OD1  B ASN   A 1 20  ? 5.859  -0.996  9.258   0.40 20.90 ?  20  ASN   A OD1  1 
ATOM   512  N ND2  A ASN   A 1 20  ? 7.340  -1.163  7.190   0.60 17.00 ?  20  ASN   A ND2  1 
ATOM   513  N ND2  B ASN   A 1 20  ? 6.936  -1.314  7.313   0.40 20.86 ?  20  ASN   A ND2  1 
ATOM   514  H H    A ASN   A 1 20  ? 7.783  -5.144  9.503   0.60 16.93 ?  20  ASN   A H    1 
ATOM   515  H H    B ASN   A 1 20  ? 7.887  -5.061  9.965   0.40 17.66 ?  20  ASN   A H    1 
ATOM   516  H HA   A ASN   A 1 20  ? 8.707  -3.422  7.681   0.60 18.12 ?  20  ASN   A HA   1 
ATOM   517  H HA   B ASN   A 1 20  ? 8.740  -3.331  8.138   0.40 19.74 ?  20  ASN   A HA   1 
ATOM   518  H HB2  A ASN   A 1 20  ? 6.431  -3.794  7.635   0.60 18.60 ?  20  ASN   A HB2  1 
ATOM   519  H HB2  B ASN   A 1 20  ? 6.476  -3.737  8.200   0.40 21.86 ?  20  ASN   A HB2  1 
ATOM   520  H HB3  A ASN   A 1 20  ? 6.300  -3.435  9.166   0.60 18.60 ?  20  ASN   A HB3  1 
ATOM   521  H HB3  B ASN   A 1 20  ? 6.406  -3.336  9.736   0.40 21.86 ?  20  ASN   A HB3  1 
ATOM   522  H HD21 A ASN   A 1 20  ? 7.196  -0.352  6.953   0.60 20.39 ?  20  ASN   A HD21 1 
ATOM   523  H HD21 B ASN   A 1 20  ? 6.771  -0.514  7.047   0.40 25.03 ?  20  ASN   A HD21 1 
ATOM   524  H HD22 A ASN   A 1 20  ? 8.057  -1.565  6.940   0.60 20.39 ?  20  ASN   A HD22 1 
ATOM   525  H HD22 B ASN   A 1 20  ? 7.385  -1.850  6.811   0.40 25.03 ?  20  ASN   A HD22 1 
ATOM   526  N N    A ALA   A 1 21  ? 10.021 -1.905  9.151   0.60 16.31 ?  21  ALA   A N    1 
ATOM   527  N N    B ALA   A 1 21  ? 10.123 -1.842  9.528   0.40 16.89 ?  21  ALA   A N    1 
ATOM   528  C CA   A ALA   A 1 21  ? 10.710 -1.015  10.077  0.60 16.91 ?  21  ALA   A CA   1 
ATOM   529  C CA   B ALA   A 1 21  ? 10.816 -0.868  10.353  0.40 16.97 ?  21  ALA   A CA   1 
ATOM   530  C C    A ALA   A 1 21  ? 11.682 -0.113  9.333   0.60 16.36 ?  21  ALA   A C    1 
ATOM   531  C C    B ALA   A 1 21  ? 11.847 -0.146  9.508   0.40 16.33 ?  21  ALA   A C    1 
ATOM   532  O O    A ALA   A 1 21  ? 12.130 -0.426  8.227   0.60 16.27 ?  21  ALA   A O    1 
ATOM   533  O O    B ALA   A 1 21  ? 12.363 -0.692  8.529   0.40 16.40 ?  21  ALA   A O    1 
ATOM   534  C CB   A ALA   A 1 21  ? 11.459 -1.802  11.157  0.60 17.84 ?  21  ALA   A CB   1 
ATOM   535  C CB   B ALA   A 1 21  ? 11.493 -1.533  11.555  0.40 17.97 ?  21  ALA   A CB   1 
ATOM   536  H H    A ALA   A 1 21  ? 10.416 -2.030  8.397   0.60 19.57 ?  21  ALA   A H    1 
ATOM   537  H H    B ALA   A 1 21  ? 10.523 -2.036  8.788   0.40 20.26 ?  21  ALA   A H    1 
ATOM   538  H HA   A ALA   A 1 21  ? 10.046 -0.458  10.515  0.60 20.29 ?  21  ALA   A HA   1 
ATOM   539  H HA   B ALA   A 1 21  ? 10.178 -0.217  10.683  0.40 20.35 ?  21  ALA   A HA   1 
ATOM   540  H HB1  A ALA   A 1 21  ? 11.893 -1.173  11.752  0.60 21.40 ?  21  ALA   A HB1  1 
ATOM   541  H HB1  B ALA   A 1 21  ? 11.919 -0.850  12.093  0.40 21.56 ?  21  ALA   A HB1  1 
ATOM   542  H HB2  A ALA   A 1 21  ? 10.819 -2.339  11.655  0.60 21.40 ?  21  ALA   A HB2  1 
ATOM   543  H HB2  B ALA   A 1 21  ? 10.818 -1.995  12.080  0.40 21.56 ?  21  ALA   A HB2  1 
ATOM   544  H HB3  A ALA   A 1 21  ? 12.113 -2.373  10.734  0.60 21.40 ?  21  ALA   A HB3  1 
ATOM   545  H HB3  B ALA   A 1 21  ? 12.152 -2.167  11.235  0.40 21.56 ?  21  ALA   A HB3  1 
ATOM   546  N N    A ASP   A 1 22  ? 11.990 1.019   9.976   0.60 16.34 ?  22  ASP   A N    1 
ATOM   547  N N    B ASP   A 1 22  ? 12.107 1.101   9.886   0.40 16.04 ?  22  ASP   A N    1 
ATOM   548  C CA   A ASP   A 1 22  ? 13.009 1.965   9.527   0.60 16.27 ?  22  ASP   A CA   1 
ATOM   549  C CA   B ASP   A 1 22  ? 13.248 1.840   9.367   0.40 15.90 ?  22  ASP   A CA   1 
ATOM   550  C C    A ASP   A 1 22  ? 14.343 1.516   10.114  0.60 15.30 ?  22  ASP   A C    1 
ATOM   551  C C    B ASP   A 1 22  ? 14.515 1.240   9.966   0.40 14.41 ?  22  ASP   A C    1 
ATOM   552  O O    A ASP   A 1 22  ? 14.531 1.541   11.335  0.60 15.64 ?  22  ASP   A O    1 
ATOM   553  O O    B ASP   A 1 22  ? 14.649 1.165   11.191  0.40 14.50 ?  22  ASP   A O    1 
ATOM   554  C CB   A ASP   A 1 22  ? 12.641 3.370   10.004  0.60 17.23 ?  22  ASP   A CB   1 
ATOM   555  C CB   B ASP   A 1 22  ? 13.107 3.300   9.789   0.40 17.04 ?  22  ASP   A CB   1 
ATOM   556  C CG   A ASP   A 1 22  ? 13.687 4.419   9.644   0.60 18.49 ?  22  ASP   A CG   1 
ATOM   557  C CG   B ASP   A 1 22  ? 14.075 4.222   9.078   0.40 17.85 ?  22  ASP   A CG   1 
ATOM   558  O OD1  A ASP   A 1 22  ? 14.802 4.073   9.201   0.60 18.73 ?  22  ASP   A OD1  1 
ATOM   559  O OD1  B ASP   A 1 22  ? 15.171 3.764   8.694   0.40 17.57 ?  22  ASP   A OD1  1 
ATOM   560  O OD2  A ASP   A 1 22  ? 13.382 5.618   9.815   0.60 19.85 -1 22  ASP   A OD2  1 
ATOM   561  O OD2  B ASP   A 1 22  ? 13.742 5.415   8.911   0.40 19.15 -1 22  ASP   A OD2  1 
ATOM   562  H H    A ASP   A 1 22  ? 11.598 1.263   10.703  0.60 19.60 ?  22  ASP   A H    1 
ATOM   563  H H    B ASP   A 1 22  ? 11.621 1.543   10.445  0.40 19.24 ?  22  ASP   A H    1 
ATOM   564  H HA   A ASP   A 1 22  ? 13.064 1.960   8.559   0.60 19.52 ?  22  ASP   A HA   1 
ATOM   565  H HA   B ASP   A 1 22  ? 13.273 1.769   8.398   0.40 19.08 ?  22  ASP   A HA   1 
ATOM   566  H HB2  A ASP   A 1 22  ? 11.796 3.632   9.601   0.60 20.67 ?  22  ASP   A HB2  1 
ATOM   567  H HB2  B ASP   A 1 22  ? 12.209 3.596   9.591   0.40 20.44 ?  22  ASP   A HB2  1 
ATOM   568  H HB3  A ASP   A 1 22  ? 12.552 3.362   10.971  0.60 20.67 ?  22  ASP   A HB3  1 
ATOM   569  H HB3  B ASP   A 1 22  ? 13.280 3.359   10.740  0.40 20.44 ?  22  ASP   A HB3  1 
ATOM   570  N N    A ILE   A 1 23  ? 15.270 1.110   9.243   0.60 14.96 ?  23  ILE   A N    1 
ATOM   571  N N    B ILE   A 1 23  ? 15.438 0.794   9.108   0.40 13.64 ?  23  ILE   A N    1 
ATOM   572  C CA   A ILE   A 1 23  ? 16.527 0.516   9.694   0.60 14.28 ?  23  ILE   A CA   1 
ATOM   573  C CA   B ILE   A 1 23  ? 16.671 0.187   9.601   0.40 13.26 ?  23  ILE   A CA   1 
ATOM   574  C C    A ILE   A 1 23  ? 17.320 1.475   10.573  0.60 14.21 ?  23  ILE   A C    1 
ATOM   575  C C    B ILE   A 1 23  ? 17.419 1.153   10.506  0.40 13.76 ?  23  ILE   A C    1 
ATOM   576  O O    A ILE   A 1 23  ? 18.055 1.038   11.467  0.60 14.81 ?  23  ILE   A O    1 
ATOM   577  O O    B ILE   A 1 23  ? 18.087 0.733   11.459  0.40 13.72 ?  23  ILE   A O    1 
ATOM   578  C CB   A ILE   A 1 23  ? 17.339 0.011   8.483   0.60 13.44 ?  23  ILE   A CB   1 
ATOM   579  C CB   B ILE   A 1 23  ? 17.553 -0.333  8.444   0.40 12.73 ?  23  ILE   A CB   1 
ATOM   580  C CG1  A ILE   A 1 23  ? 18.486 -0.893  8.941   0.60 13.54 ?  23  ILE   A CG1  1 
ATOM   581  C CG1  B ILE   A 1 23  ? 18.618 -1.281  9.002   0.40 12.71 ?  23  ILE   A CG1  1 
ATOM   582  C CG2  A ILE   A 1 23  ? 17.836 1.180   7.639   0.60 13.42 ?  23  ILE   A CG2  1 
ATOM   583  C CG2  B ILE   A 1 23  ? 18.199 0.820   7.674   0.40 12.66 ?  23  ILE   A CG2  1 
ATOM   584  C CD1  A ILE   A 1 23  ? 19.139 -1.657  7.807   0.60 13.69 ?  23  ILE   A CD1  1 
ATOM   585  C CD1  B ILE   A 1 23  ? 19.557 -1.831  7.968   0.40 12.97 ?  23  ILE   A CD1  1 
ATOM   586  H H    A ILE   A 1 23  ? 15.187 1.165   8.393   0.60 17.94 ?  23  ILE   A H    1 
ATOM   587  H H    B ILE   A 1 23  ? 15.373 0.831   8.263   0.40 16.36 ?  23  ILE   A H    1 
ATOM   588  H HA   A ILE   A 1 23  ? 16.313 -0.255  10.240  0.60 17.13 ?  23  ILE   A HA   1 
ATOM   589  H HA   B ILE   A 1 23  ? 16.431 -0.583  10.136  0.40 15.91 ?  23  ILE   A HA   1 
ATOM   590  H HB   A ILE   A 1 23  ? 16.745 -0.520  7.935   0.60 16.12 ?  23  ILE   A HB   1 
ATOM   591  H HB   B ILE   A 1 23  ? 16.994 -0.836  7.829   0.40 15.27 ?  23  ILE   A HB   1 
ATOM   592  H HG12 A ILE   A 1 23  ? 19.169 -0.347  9.364   0.60 16.24 ?  23  ILE   A HG12 1 
ATOM   593  H HG12 B ILE   A 1 23  ? 19.150 -0.804  9.657   0.40 15.24 ?  23  ILE   A HG12 1 
ATOM   594  H HG13 A ILE   A 1 23  ? 18.143 -1.540  9.579   0.60 16.24 ?  23  ILE   A HG13 1 
ATOM   595  H HG13 B ILE   A 1 23  ? 18.175 -2.034  9.426   0.40 15.24 ?  23  ILE   A HG13 1 
ATOM   596  H HG21 A ILE   A 1 23  ? 18.205 0.836   6.811   0.60 16.10 ?  23  ILE   A HG21 1 
ATOM   597  H HG21 B ILE   A 1 23  ? 18.555 0.480   6.834   0.40 15.18 ?  23  ILE   A HG21 1 
ATOM   598  H HG22 A ILE   A 1 23  ? 17.087 1.770   7.445   0.60 16.10 ?  23  ILE   A HG22 1 
ATOM   599  H HG22 B ILE   A 1 23  ? 17.530 1.496   7.498   0.40 15.18 ?  23  ILE   A HG22 1 
ATOM   600  H HG23 A ILE   A 1 23  ? 18.516 1.665   8.130   0.60 16.10 ?  23  ILE   A HG23 1 
ATOM   601  H HG23 B ILE   A 1 23  ? 18.919 1.194   8.207   0.40 15.18 ?  23  ILE   A HG23 1 
ATOM   602  H HD11 A ILE   A 1 23  ? 19.820 -2.241  8.172   0.60 16.42 ?  23  ILE   A HD11 1 
ATOM   603  H HD11 B ILE   A 1 23  ? 20.101 -2.525  8.374   0.40 15.56 ?  23  ILE   A HD11 1 
ATOM   604  H HD12 A ILE   A 1 23  ? 18.460 -2.182  7.353   0.60 16.42 ?  23  ILE   A HD12 1 
ATOM   605  H HD12 B ILE   A 1 23  ? 19.033 -2.201  7.243   0.40 15.56 ?  23  ILE   A HD12 1 
ATOM   606  H HD13 A ILE   A 1 23  ? 19.536 -1.025  7.190   0.60 16.42 ?  23  ILE   A HD13 1 
ATOM   607  H HD13 B ILE   A 1 23  ? 20.123 -1.115  7.641   0.40 15.56 ?  23  ILE   A HD13 1 
ATOM   608  N N    A VAL   A 1 24  ? 17.190 2.784   10.347  0.60 14.52 ?  24  VAL   A N    1 
ATOM   609  N N    B VAL   A 1 24  ? 17.305 2.457   10.240  0.40 14.60 ?  24  VAL   A N    1 
ATOM   610  C CA   A VAL   A 1 24  ? 17.870 3.751   11.208  0.60 15.62 ?  24  VAL   A CA   1 
ATOM   611  C CA   B VAL   A 1 24  ? 17.927 3.456   11.104  0.40 15.95 ?  24  VAL   A CA   1 
ATOM   612  C C    A VAL   A 1 24  ? 17.350 3.644   12.635  0.60 16.09 ?  24  VAL   A C    1 
ATOM   613  C C    B VAL   A 1 24  ? 17.323 3.397   12.501  0.40 16.62 ?  24  VAL   A C    1 
ATOM   614  O O    A VAL   A 1 24  ? 18.122 3.497   13.592  0.60 17.02 ?  24  VAL   A O    1 
ATOM   615  O O    B VAL   A 1 24  ? 18.033 3.506   13.509  0.40 17.51 ?  24  VAL   A O    1 
ATOM   616  C CB   A VAL   A 1 24  ? 17.711 5.178   10.652  0.60 16.46 ?  24  VAL   A CB   1 
ATOM   617  C CB   B VAL   A 1 24  ? 17.791 4.854   10.473  0.40 16.71 ?  24  VAL   A CB   1 
ATOM   618  C CG1  A VAL   A 1 24  ? 18.210 6.207   11.666  0.60 17.14 ?  24  VAL   A CG1  1 
ATOM   619  C CG1  B VAL   A 1 24  ? 18.432 5.905   11.362  0.40 17.93 ?  24  VAL   A CG1  1 
ATOM   620  C CG2  A VAL   A 1 24  ? 18.448 5.318   9.333   0.60 17.17 ?  24  VAL   A CG2  1 
ATOM   621  C CG2  B VAL   A 1 24  ? 18.405 4.867   9.077   0.40 16.70 ?  24  VAL   A CG2  1 
ATOM   622  H H    A VAL   A 1 24  ? 16.725 3.132   9.713   0.60 17.42 ?  24  VAL   A H    1 
ATOM   623  H H    B VAL   A 1 24  ? 16.874 2.782   9.571   0.40 17.52 ?  24  VAL   A H    1 
ATOM   624  H HA   A VAL   A 1 24  ? 18.815 3.548   11.222  0.60 18.74 ?  24  VAL   A HA   1 
ATOM   625  H HA   B VAL   A 1 24  ? 18.870 3.255   11.181  0.40 19.13 ?  24  VAL   A HA   1 
ATOM   626  H HB   A VAL   A 1 24  ? 16.771 5.355   10.486  0.60 19.75 ?  24  VAL   A HB   1 
ATOM   627  H HB   B VAL   A 1 24  ? 16.849 5.069   10.385  0.40 20.04 ?  24  VAL   A HB   1 
ATOM   628  H HG11 A VAL   A 1 24  ? 18.384 7.043   11.206  0.60 20.56 ?  24  VAL   A HG11 1 
ATOM   629  H HG11 B VAL   A 1 24  ? 18.490 6.738   10.869  0.40 21.51 ?  24  VAL   A HG11 1 
ATOM   630  H HG12 A VAL   A 1 24  ? 17.532 6.337   12.344  0.60 20.56 ?  24  VAL   A HG12 1 
ATOM   631  H HG12 B VAL   A 1 24  ? 17.883 6.027   12.152  0.40 21.51 ?  24  VAL   A HG12 1 
ATOM   632  H HG13 A VAL   A 1 24  ? 19.030 5.877   12.069  0.60 20.56 ?  24  VAL   A HG13 1 
ATOM   633  H HG13 B VAL   A 1 24  ? 19.318 5.606   11.614  0.40 21.51 ?  24  VAL   A HG13 1 
ATOM   634  H HG21 A VAL   A 1 24  ? 18.205 6.163   8.921   0.60 20.60 ?  24  VAL   A HG21 1 
ATOM   635  H HG21 B VAL   A 1 24  ? 18.411 5.777   8.744   0.40 20.03 ?  24  VAL   A HG21 1 
ATOM   636  H HG22 A VAL   A 1 24  ? 19.403 5.298   9.501   0.60 20.60 ?  24  VAL   A HG22 1 
ATOM   637  H HG22 B VAL   A 1 24  ? 19.312 4.527   9.129   0.40 20.03 ?  24  VAL   A HG22 1 
ATOM   638  H HG23 A VAL   A 1 24  ? 18.198 4.584   8.749   0.60 20.60 ?  24  VAL   A HG23 1 
ATOM   639  H HG23 B VAL   A 1 24  ? 17.875 4.304   8.491   0.40 20.03 ?  24  VAL   A HG23 1 
ATOM   640  N N    A GLU   A 1 25  ? 16.027 3.719   12.797  0.60 16.52 ?  25  GLU   A N    1 
ATOM   641  N N    B GLU   A 1 25  ? 16.002 3.217   12.584  0.40 16.85 ?  25  GLU   A N    1 
ATOM   642  C CA   A GLU   A 1 25  ? 15.440 3.656   14.131  0.60 17.41 ?  25  GLU   A CA   1 
ATOM   643  C CA   B GLU   A 1 25  ? 15.347 3.119   13.885  0.40 17.77 ?  25  GLU   A CA   1 
ATOM   644  C C    A GLU   A 1 25  ? 15.670 2.296   14.775  0.60 16.41 ?  25  GLU   A C    1 
ATOM   645  C C    B GLU   A 1 25  ? 15.640 1.780   14.555  0.40 17.25 ?  25  GLU   A C    1 
ATOM   646  O O    A GLU   A 1 25  ? 15.879 2.207   15.990  0.60 17.14 ?  25  GLU   A O    1 
ATOM   647  O O    B GLU   A 1 25  ? 15.889 1.731   15.765  0.40 17.74 ?  25  GLU   A O    1 
ATOM   648  C CB   A GLU   A 1 25  ? 13.950 3.999   14.063  0.60 20.14 ?  25  GLU   A CB   1 
ATOM   649  C CB   B GLU   A 1 25  ? 13.842 3.352   13.736  0.40 19.12 ?  25  GLU   A CB   1 
ATOM   650  C CG   A GLU   A 1 25  ? 13.686 5.455   13.701  0.60 23.18 ?  25  GLU   A CG   1 
ATOM   651  C CG   B GLU   A 1 25  ? 13.494 4.727   13.186  0.40 21.74 ?  25  GLU   A CG   1 
ATOM   652  C CD   A GLU   A 1 25  ? 14.503 6.427   14.536  0.60 25.78 ?  25  GLU   A CD   1 
ATOM   653  C CD   B GLU   A 1 25  ? 13.986 5.852   14.078  0.40 23.89 ?  25  GLU   A CD   1 
ATOM   654  O OE1  A GLU   A 1 25  ? 14.549 6.263   15.774  0.60 26.59 ?  25  GLU   A OE1  1 
ATOM   655  O OE1  B GLU   A 1 25  ? 13.974 5.678   15.316  0.40 24.81 ?  25  GLU   A OE1  1 
ATOM   656  O OE2  A GLU   A 1 25  ? 15.119 7.342   13.949  0.60 27.06 -1 25  GLU   A OE2  1 
ATOM   657  O OE2  B GLU   A 1 25  ? 14.389 6.905   13.541  0.40 24.70 -1 25  GLU   A OE2  1 
ATOM   658  H H    A GLU   A 1 25  ? 15.456 3.817   12.158  0.60 19.82 ?  25  GLU   A H    1 
ATOM   659  H H    B GLU   A 1 25  ? 15.472 3.151   11.909  0.40 20.22 ?  25  GLU   A H    1 
ATOM   660  H HA   A GLU   A 1 25  ? 15.874 4.313   14.695  0.60 20.88 ?  25  GLU   A HA   1 
ATOM   661  H HA   B GLU   A 1 25  ? 15.698 3.812   14.460  0.40 21.32 ?  25  GLU   A HA   1 
ATOM   662  H HB2  A GLU   A 1 25  ? 13.524 3.449   13.383  0.60 24.16 ?  25  GLU   A HB2  1 
ATOM   663  H HB2  B GLU   A 1 25  ? 13.477 2.688   13.130  0.40 22.93 ?  25  GLU   A HB2  1 
ATOM   664  H HB3  A GLU   A 1 25  ? 13.540 3.831   14.925  0.60 24.16 ?  25  GLU   A HB3  1 
ATOM   665  H HB3  B GLU   A 1 25  ? 13.424 3.267   14.607  0.40 22.93 ?  25  GLU   A HB3  1 
ATOM   666  H HG2  A GLU   A 1 25  ? 13.924 5.599   12.774  0.60 27.81 ?  25  GLU   A HG2  1 
ATOM   667  H HG2  B GLU   A 1 25  ? 13.903 4.829   12.311  0.40 26.08 ?  25  GLU   A HG2  1 
ATOM   668  H HG3  A GLU   A 1 25  ? 12.746 5.652   13.840  0.60 27.81 ?  25  GLU   A HG3  1 
ATOM   669  H HG3  B GLU   A 1 25  ? 12.531 4.805   13.114  0.40 26.08 ?  25  GLU   A HG3  1 
ATOM   670  N N    A GLU   A 1 26  ? 15.650 1.227   13.976  0.60 16.50 ?  26  GLU   A N    1 
ATOM   671  N N    B GLU   A 1 26  ? 15.623 0.684   13.789  0.40 16.82 ?  26  GLU   A N    1 
ATOM   672  C CA   A GLU   A 1 26  ? 15.926 -0.104  14.508  0.60 16.77 ?  26  GLU   A CA   1 
ATOM   673  C CA   B GLU   A 1 26  ? 16.037 -0.600  14.347  0.40 16.73 ?  26  GLU   A CA   1 
ATOM   674  C C    A GLU   A 1 26  ? 17.354 -0.199  15.036  0.60 16.12 ?  26  GLU   A C    1 
ATOM   675  C C    B GLU   A 1 26  ? 17.448 -0.516  14.904  0.40 15.93 ?  26  GLU   A C    1 
ATOM   676  O O    A GLU   A 1 26  ? 17.585 -0.661  16.161  0.60 16.21 ?  26  GLU   A O    1 
ATOM   677  O O    B GLU   A 1 26  ? 17.749 -1.105  15.948  0.40 15.36 ?  26  GLU   A O    1 
ATOM   678  C CB   A GLU   A 1 26  ? 15.679 -1.153  13.424  0.60 18.29 ?  26  GLU   A CB   1 
ATOM   679  C CB   B GLU   A 1 26  ? 15.972 -1.701  13.285  0.40 17.99 ?  26  GLU   A CB   1 
ATOM   680  C CG   A GLU   A 1 26  ? 14.239 -1.608  13.306  0.60 21.55 ?  26  GLU   A CG   1 
ATOM   681  C CG   B GLU   A 1 26  ? 14.585 -2.187  12.955  0.40 18.60 ?  26  GLU   A CG   1 
ATOM   682  C CD   A GLU   A 1 26  ? 13.770 -2.375  14.525  0.60 23.67 ?  26  GLU   A CD   1 
ATOM   683  C CD   B GLU   A 1 26  ? 13.920 -2.857  14.138  0.40 18.87 ?  26  GLU   A CD   1 
ATOM   684  O OE1  A GLU   A 1 26  ? 14.412 -3.384  14.883  0.60 23.75 ?  26  GLU   A OE1  1 
ATOM   685  O OE1  B GLU   A 1 26  ? 14.316 -3.986  14.517  0.40 19.07 ?  26  GLU   A OE1  1 
ATOM   686  O OE2  A GLU   A 1 26  ? 12.767 -1.949  15.134  0.60 25.72 -1 26  GLU   A OE2  1 
ATOM   687  O OE2  B GLU   A 1 26  ? 13.005 -2.239  14.703  0.40 18.71 -1 26  GLU   A OE2  1 
ATOM   688  H H    A GLU   A 1 26  ? 15.479 1.253   13.133  0.60 19.79 ?  26  GLU   A H    1 
ATOM   689  H H    B GLU   A 1 26  ? 15.387 0.655   12.966  0.40 20.18 ?  26  GLU   A H    1 
ATOM   690  H HA   A GLU   A 1 26  ? 15.319 -0.276  15.241  0.60 20.11 ?  26  GLU   A HA   1 
ATOM   691  H HA   B GLU   A 1 26  ? 15.447 -0.844  15.076  0.40 20.07 ?  26  GLU   A HA   1 
ATOM   692  H HB2  A GLU   A 1 26  ? 15.939 -0.779  12.564  0.60 21.94 ?  26  GLU   A HB2  1 
ATOM   693  H HB2  B GLU   A 1 26  ? 16.365 -1.370  12.467  0.40 21.58 ?  26  GLU   A HB2  1 
ATOM   694  H HB3  A GLU   A 1 26  ? 16.222 -1.929  13.619  0.60 21.94 ?  26  GLU   A HB3  1 
ATOM   695  H HB3  B GLU   A 1 26  ? 16.477 -2.471  13.602  0.40 21.58 ?  26  GLU   A HB3  1 
ATOM   696  H HG2  A GLU   A 1 26  ? 13.664 -0.834  13.235  0.60 25.85 ?  26  GLU   A HG2  1 
ATOM   697  H HG2  B GLU   A 1 26  ? 14.045 -1.430  12.670  0.40 22.32 ?  26  GLU   A HG2  1 
ATOM   698  H HG3  A GLU   A 1 26  ? 14.149 -2.164  12.512  0.60 25.85 ?  26  GLU   A HG3  1 
ATOM   699  H HG3  B GLU   A 1 26  ? 14.634 -2.842  12.242  0.40 22.32 ?  26  GLU   A HG3  1 
ATOM   700  N N    . ALA   A 1 27  ? 18.330 0.219   14.226  1.00 15.74 ?  27  ALA   A N    1 
ATOM   701  C CA   . ALA   A 1 27  ? 19.719 0.226   14.664  1.00 16.01 ?  27  ALA   A CA   1 
ATOM   702  C C    . ALA   A 1 27  ? 19.889 1.028   15.949  1.00 17.98 ?  27  ALA   A C    1 
ATOM   703  O O    . ALA   A 1 27  ? 20.562 0.582   16.885  1.00 17.90 ?  27  ALA   A O    1 
ATOM   704  C CB   . ALA   A 1 27  ? 20.627 0.763   13.556  1.00 15.46 ?  27  ALA   A CB   1 
ATOM   705  H H    A ALA   A 1 27  ? 18.210 0.497   13.421  0.60 18.88 ?  27  ALA   A H    1 
ATOM   706  H H    B ALA   A 1 27  ? 18.151 0.710   13.542  0.40 18.88 ?  27  ALA   A H    1 
ATOM   707  H HA   . ALA   A 1 27  ? 19.991 -0.684  14.846  1.00 19.21 ?  27  ALA   A HA   1 
ATOM   708  H HB1  . ALA   A 1 27  ? 21.548 0.758   13.869  1.00 18.54 ?  27  ALA   A HB1  1 
ATOM   709  H HB2  . ALA   A 1 27  ? 20.547 0.193   12.773  1.00 18.54 ?  27  ALA   A HB2  1 
ATOM   710  H HB3  . ALA   A 1 27  ? 20.361 1.668   13.332  1.00 18.54 ?  27  ALA   A HB3  1 
ATOM   711  N N    A LYS   A 1 28  ? 19.284 2.216   16.016  0.60 19.94 ?  28  LYS   A N    1 
ATOM   712  N N    B LYS   A 1 28  ? 19.273 2.211   16.021  0.40 20.36 ?  28  LYS   A N    1 
ATOM   713  C CA   A LYS   A 1 28  ? 19.431 3.037   17.213  0.60 22.99 ?  28  LYS   A CA   1 
ATOM   714  C CA   B LYS   A 1 28  ? 19.391 3.027   17.225  0.40 23.39 ?  28  LYS   A CA   1 
ATOM   715  C C    A LYS   A 1 28  ? 18.877 2.337   18.446  0.60 24.02 ?  28  LYS   A C    1 
ATOM   716  C C    B LYS   A 1 28  ? 18.829 2.314   18.448  0.40 24.69 ?  28  LYS   A C    1 
ATOM   717  O O    A LYS   A 1 28  ? 19.418 2.499   19.545  0.60 25.24 ?  28  LYS   A O    1 
ATOM   718  O O    B LYS   A 1 28  ? 19.346 2.488   19.558  0.40 25.49 ?  28  LYS   A O    1 
ATOM   719  C CB   A LYS   A 1 28  ? 18.781 4.407   17.009  0.60 25.45 ?  28  LYS   A CB   1 
ATOM   720  C CB   B LYS   A 1 28  ? 18.704 4.380   17.020  0.40 25.38 ?  28  LYS   A CB   1 
ATOM   721  C CG   A LYS   A 1 28  ? 19.626 5.344   16.161  0.60 28.08 ?  28  LYS   A CG   1 
ATOM   722  C CG   B LYS   A 1 28  ? 19.455 5.301   16.072  0.40 27.48 ?  28  LYS   A CG   1 
ATOM   723  C CD   A LYS   A 1 28  ? 19.137 6.778   16.229  0.60 30.92 ?  28  LYS   A CD   1 
ATOM   724  C CD   B LYS   A 1 28  ? 18.975 6.741   16.166  0.40 29.81 ?  28  LYS   A CD   1 
ATOM   725  C CE   A LYS   A 1 28  ? 17.871 6.969   15.421  0.60 32.94 ?  28  LYS   A CE   1 
ATOM   726  C CE   B LYS   A 1 28  ? 17.718 6.968   15.350  0.40 31.50 ?  28  LYS   A CE   1 
ATOM   727  N NZ   A LYS   A 1 28  ? 17.479 8.403   15.364  0.60 34.17 ?  28  LYS   A NZ   1 
ATOM   728  N NZ   B LYS   A 1 28  ? 17.404 8.420   15.230  0.40 32.51 ?  28  LYS   A NZ   1 
ATOM   729  H H    A LYS   A 1 28  ? 18.798 2.560   15.398  0.60 23.92 ?  28  LYS   A H    1 
ATOM   730  H H    B LYS   A 1 28  ? 18.794 2.556   15.397  0.40 24.42 ?  28  LYS   A H    1 
ATOM   731  H HA   A LYS   A 1 28  ? 20.374 3.185   17.373  0.60 27.58 ?  28  LYS   A HA   1 
ATOM   732  H HA   B LYS   A 1 28  ? 20.328 3.199   17.395  0.40 28.07 ?  28  LYS   A HA   1 
ATOM   733  H HB2  A LYS   A 1 28  ? 17.929 4.292   16.563  0.60 30.54 ?  28  LYS   A HB2  1 
ATOM   734  H HB2  B LYS   A 1 28  ? 17.820 4.233   16.650  0.40 30.45 ?  28  LYS   A HB2  1 
ATOM   735  H HB3  A LYS   A 1 28  ? 18.650 4.828   17.873  0.60 30.54 ?  28  LYS   A HB3  1 
ATOM   736  H HB3  B LYS   A 1 28  ? 18.633 4.830   17.876  0.40 30.45 ?  28  LYS   A HB3  1 
ATOM   737  H HG2  A LYS   A 1 28  ? 20.542 5.324   16.479  0.60 33.69 ?  28  LYS   A HG2  1 
ATOM   738  H HG2  B LYS   A 1 28  ? 20.399 5.285   16.294  0.40 32.97 ?  28  LYS   A HG2  1 
ATOM   739  H HG3  A LYS   A 1 28  ? 19.588 5.057   15.236  0.60 33.69 ?  28  LYS   A HG3  1 
ATOM   740  H HG3  B LYS   A 1 28  ? 19.321 4.997   15.161  0.40 32.97 ?  28  LYS   A HG3  1 
ATOM   741  H HD2  A LYS   A 1 28  ? 18.947 7.010   17.152  0.60 37.10 ?  28  LYS   A HD2  1 
ATOM   742  H HD2  B LYS   A 1 28  ? 18.778 6.954   17.092  0.40 35.76 ?  28  LYS   A HD2  1 
ATOM   743  H HD3  A LYS   A 1 28  ? 19.819 7.367   15.869  0.60 37.10 ?  28  LYS   A HD3  1 
ATOM   744  H HD3  B LYS   A 1 28  ? 19.667 7.330   15.827  0.40 35.76 ?  28  LYS   A HD3  1 
ATOM   745  H HE2  A LYS   A 1 28  ? 18.021 6.656   14.515  0.60 39.52 ?  28  LYS   A HE2  1 
ATOM   746  H HE2  B LYS   A 1 28  ? 17.845 6.610   14.458  0.40 37.80 ?  28  LYS   A HE2  1 
ATOM   747  H HE3  A LYS   A 1 28  ? 17.149 6.470   15.834  0.60 39.52 ?  28  LYS   A HE3  1 
ATOM   748  H HE3  B LYS   A 1 28  ? 16.970 6.530   15.785  0.40 37.80 ?  28  LYS   A HE3  1 
ATOM   749  H HZ1  A LYS   A 1 28  ? 16.735 8.496   14.886  0.60 41.00 ?  28  LYS   A HZ1  1 
ATOM   750  H HZ1  B LYS   A 1 28  ? 16.665 8.533   14.748  0.40 39.00 ?  28  LYS   A HZ1  1 
ATOM   751  H HZ2  A LYS   A 1 28  ? 17.336 8.712   16.186  0.60 41.00 ?  28  LYS   A HZ2  1 
ATOM   752  H HZ2  B LYS   A 1 28  ? 17.281 8.772   16.038  0.40 39.00 ?  28  LYS   A HZ2  1 
ATOM   753  H HZ3  A LYS   A 1 28  ? 18.129 8.880   14.985  0.60 41.00 ?  28  LYS   A HZ3  1 
ATOM   754  H HZ3  B LYS   A 1 28  ? 18.078 8.844   14.830  0.40 39.00 ?  28  LYS   A HZ3  1 
ATOM   755  N N    A LYS   A 1 29  ? 17.817 1.543   18.284  0.60 24.49 ?  29  LYS   A N    1 
ATOM   756  N N    B LYS   A 1 29  ? 17.786 1.502   18.269  0.40 25.57 ?  29  LYS   A N    1 
ATOM   757  C CA   A LYS   A 1 29  ? 17.228 0.837   19.418  0.60 26.47 ?  29  LYS   A CA   1 
ATOM   758  C CA   B LYS   A 1 29  ? 17.174 0.809   19.399  0.40 27.10 ?  29  LYS   A CA   1 
ATOM   759  C C    A LYS   A 1 29  ? 18.053 -0.388  19.802  0.60 26.18 ?  29  LYS   A C    1 
ATOM   760  C C    B LYS   A 1 29  ? 17.976 -0.424  19.801  0.40 26.35 ?  29  LYS   A C    1 
ATOM   761  O O    A LYS   A 1 29  ? 18.388 -0.577  20.977  0.60 27.23 ?  29  LYS   A O    1 
ATOM   762  O O    B LYS   A 1 29  ? 18.216 -0.657  20.992  0.40 26.98 ?  29  LYS   A O    1 
ATOM   763  C CB   A LYS   A 1 29  ? 15.794 0.423   19.081  0.60 29.13 ?  29  LYS   A CB   1 
ATOM   764  C CB   B LYS   A 1 29  ? 15.741 0.406   19.044  0.40 29.43 ?  29  LYS   A CB   1 
ATOM   765  C CG   A LYS   A 1 29  ? 15.059 -0.286  20.212  0.60 32.19 ?  29  LYS   A CG   1 
ATOM   766  C CG   B LYS   A 1 29  ? 14.963 -0.228  20.190  0.40 31.90 ?  29  LYS   A CG   1 
ATOM   767  C CD   A LYS   A 1 29  ? 14.694 0.678   21.329  0.60 34.93 ?  29  LYS   A CD   1 
ATOM   768  C CD   B LYS   A 1 29  ? 14.627 0.791   21.265  0.40 34.06 ?  29  LYS   A CD   1 
ATOM   769  C CE   A LYS   A 1 29  ? 13.815 0.007   22.374  0.60 36.70 ?  29  LYS   A CE   1 
ATOM   770  C CE   B LYS   A 1 29  ? 13.766 0.180   22.359  0.40 35.49 ?  29  LYS   A CE   1 
ATOM   771  N NZ   A LYS   A 1 29  ? 13.364 0.966   23.419  0.60 37.77 ?  29  LYS   A NZ   1 
ATOM   772  N NZ   B LYS   A 1 29  ? 13.388 1.180   23.395  0.40 36.33 ?  29  LYS   A NZ   1 
ATOM   773  H H    A LYS   A 1 29  ? 17.424 1.398   17.533  0.60 29.39 ?  29  LYS   A H    1 
ATOM   774  H H    B LYS   A 1 29  ? 17.416 1.341   17.510  0.40 30.68 ?  29  LYS   A H    1 
ATOM   775  H HA   A LYS   A 1 29  ? 17.196 1.432   20.182  0.60 31.76 ?  29  LYS   A HA   1 
ATOM   776  H HA   B LYS   A 1 29  ? 17.139 1.410   20.160  0.40 32.52 ?  29  LYS   A HA   1 
ATOM   777  H HB2  A LYS   A 1 29  ? 15.284 1.218   18.856  0.60 34.95 ?  29  LYS   A HB2  1 
ATOM   778  H HB2  B LYS   A 1 29  ? 15.257 1.196   18.762  0.40 35.31 ?  29  LYS   A HB2  1 
ATOM   779  H HB3  A LYS   A 1 29  ? 15.813 -0.179  18.322  0.60 34.95 ?  29  LYS   A HB3  1 
ATOM   780  H HB3  B LYS   A 1 29  ? 15.771 -0.237  18.318  0.40 35.31 ?  29  LYS   A HB3  1 
ATOM   781  H HG2  A LYS   A 1 29  ? 14.239 -0.670  19.866  0.60 38.62 ?  29  LYS   A HG2  1 
ATOM   782  H HG2  B LYS   A 1 29  ? 14.132 -0.592  19.847  0.40 38.28 ?  29  LYS   A HG2  1 
ATOM   783  H HG3  A LYS   A 1 29  ? 15.622 -0.984  20.583  0.60 38.62 ?  29  LYS   A HG3  1 
ATOM   784  H HG3  B LYS   A 1 29  ? 15.493 -0.934  20.594  0.40 38.28 ?  29  LYS   A HG3  1 
ATOM   785  H HD2  A LYS   A 1 29  ? 15.504 0.986   21.765  0.60 41.90 ?  29  LYS   A HD2  1 
ATOM   786  H HD2  B LYS   A 1 29  ? 15.447 1.115   21.670  0.40 40.87 ?  29  LYS   A HD2  1 
ATOM   787  H HD3  A LYS   A 1 29  ? 14.205 1.429   20.957  0.60 41.90 ?  29  LYS   A HD3  1 
ATOM   788  H HD3  B LYS   A 1 29  ? 14.136 1.527   20.866  0.40 40.87 ?  29  LYS   A HD3  1 
ATOM   789  H HE2  A LYS   A 1 29  ? 13.029 -0.362  21.941  0.60 44.04 ?  29  LYS   A HE2  1 
ATOM   790  H HE2  B LYS   A 1 29  ? 12.952 -0.171  21.965  0.40 42.58 ?  29  LYS   A HE2  1 
ATOM   791  H HE3  A LYS   A 1 29  ? 14.319 -0.700  22.808  0.60 44.04 ?  29  LYS   A HE3  1 
ATOM   792  H HE3  B LYS   A 1 29  ? 14.261 -0.533  22.793  0.40 42.58 ?  29  LYS   A HE3  1 
ATOM   793  H HZ1  A LYS   A 1 29  ? 12.853 0.548   24.016  0.60 45.32 ?  29  LYS   A HZ1  1 
ATOM   794  H HZ1  B LYS   A 1 29  ? 12.886 0.795   24.021  0.40 43.58 ?  29  LYS   A HZ1  1 
ATOM   795  H HZ2  A LYS   A 1 29  ? 14.069 1.315   23.836  0.60 45.32 ?  29  LYS   A HZ2  1 
ATOM   796  H HZ2  B LYS   A 1 29  ? 14.120 1.514   23.776  0.40 43.58 ?  29  LYS   A HZ2  1 
ATOM   797  H HZ3  A LYS   A 1 29  ? 12.894 1.623   23.046  0.60 45.32 ?  29  LYS   A HZ3  1 
ATOM   798  H HZ3  B LYS   A 1 29  ? 12.927 1.844   23.022  0.40 43.58 ?  29  LYS   A HZ3  1 
ATOM   799  N N    . VAL   A 1 30  ? 18.386 -1.231  18.825  1.00 24.82 ?  30  VAL   A N    1 
ATOM   800  C CA   . VAL   A 1 30  ? 19.037 -2.501  19.126  1.00 23.12 ?  30  VAL   A CA   1 
ATOM   801  C C    . VAL   A 1 30  ? 20.538 -2.341  19.352  1.00 21.95 ?  30  VAL   A C    1 
ATOM   802  O O    . VAL   A 1 30  ? 21.124 -3.067  20.163  1.00 22.75 ?  30  VAL   A O    1 
ATOM   803  C CB   . VAL   A 1 30  ? 18.744 -3.501  17.992  1.00 23.58 ?  30  VAL   A CB   1 
ATOM   804  C CG1  . VAL   A 1 30  ? 19.503 -4.803  18.206  1.00 24.09 ?  30  VAL   A CG1  1 
ATOM   805  C CG2  . VAL   A 1 30  ? 17.245 -3.761  17.883  1.00 23.99 ?  30  VAL   A CG2  1 
ATOM   806  H H    A VAL   A 1 30  ? 18.249 -1.092  17.989  0.60 29.77 ?  30  VAL   A H    1 
ATOM   807  H H    B VAL   A 1 30  ? 18.295 -1.070  17.986  0.40 29.77 ?  30  VAL   A H    1 
ATOM   808  H HA   . VAL   A 1 30  ? 18.643 -2.865  19.938  1.00 27.73 ?  30  VAL   A HA   1 
ATOM   809  H HB   . VAL   A 1 30  ? 19.043 -3.120  17.150  1.00 28.29 ?  30  VAL   A HB   1 
ATOM   810  H HG11 . VAL   A 1 30  ? 19.136 -5.482  17.615  1.00 28.90 ?  30  VAL   A HG11 1 
ATOM   811  H HG12 . VAL   A 1 30  ? 20.440 -4.663  18.003  1.00 28.90 ?  30  VAL   A HG12 1 
ATOM   812  H HG13 . VAL   A 1 30  ? 19.398 -5.080  19.129  1.00 28.90 ?  30  VAL   A HG13 1 
ATOM   813  H HG21 . VAL   A 1 30  ? 17.088 -4.430  17.197  1.00 28.78 ?  30  VAL   A HG21 1 
ATOM   814  H HG22 . VAL   A 1 30  ? 16.919 -4.083  18.738  1.00 28.78 ?  30  VAL   A HG22 1 
ATOM   815  H HG23 . VAL   A 1 30  ? 16.797 -2.934  17.647  1.00 28.78 ?  30  VAL   A HG23 1 
ATOM   816  N N    . LYS   A 1 31  ? 21.174 -1.403  18.661  1.00 20.88 ?  31  LYS   A N    1 
ATOM   817  C CA   . LYS   A 1 31  ? 22.627 -1.291  18.621  1.00 21.85 ?  31  LYS   A CA   1 
ATOM   818  C C    . LYS   A 1 31  ? 23.240 -2.653  18.282  1.00 18.95 ?  31  LYS   A C    1 
ATOM   819  O O    . LYS   A 1 31  ? 24.009 -3.211  19.072  1.00 20.09 ?  31  LYS   A O    1 
ATOM   820  C CB   . LYS   A 1 31  ? 23.193 -0.742  19.922  1.00 27.91 ?  31  LYS   A CB   1 
ATOM   821  C CG   . LYS   A 1 31  ? 22.518 0.529   20.410  1.00 34.25 ?  31  LYS   A CG   1 
ATOM   822  C CD   . LYS   A 1 31  ? 23.526 1.648   20.612  1.00 39.03 ?  31  LYS   A CD   1 
ATOM   823  C CE   . LYS   A 1 31  ? 22.982 2.736   21.523  1.00 42.33 ?  31  LYS   A CE   1 
ATOM   824  N NZ   . LYS   A 1 31  ? 21.681 3.281   21.052  1.00 43.98 ?  31  LYS   A NZ   1 
ATOM   825  H H    . LYS   A 1 31  ? 20.772 -0.807  18.195  1.00 25.05 ?  31  LYS   A H    1 
ATOM   826  H HA   . LYS   A 1 31  ? 22.857 -0.670  17.917  1.00 26.22 ?  31  LYS   A HA   1 
ATOM   827  H HB2  . LYS   A 1 31  ? 23.080 -1.411  20.607  1.00 33.48 ?  31  LYS   A HB2  1 
ATOM   828  H HB3  . LYS   A 1 31  ? 24.139 -0.551  19.798  1.00 33.48 ?  31  LYS   A HB3  1 
ATOM   829  H HG2  . LYS   A 1 31  ? 21.868 0.821   19.752  1.00 41.10 ?  31  LYS   A HG2  1 
ATOM   830  H HG3  . LYS   A 1 31  ? 22.081 0.355   21.260  1.00 41.10 ?  31  LYS   A HG3  1 
ATOM   831  H HD2  . LYS   A 1 31  ? 24.329 1.287   21.020  1.00 46.83 ?  31  LYS   A HD2  1 
ATOM   832  H HD3  . LYS   A 1 31  ? 23.736 2.046   19.753  1.00 46.83 ?  31  LYS   A HD3  1 
ATOM   833  H HE2  . LYS   A 1 31  ? 22.851 2.368   22.410  1.00 50.79 ?  31  LYS   A HE2  1 
ATOM   834  H HE3  . LYS   A 1 31  ? 23.620 3.466   21.557  1.00 50.79 ?  31  LYS   A HE3  1 
ATOM   835  H HZ1  . LYS   A 1 31  ? 21.408 3.929   21.598  1.00 52.77 ?  31  LYS   A HZ1  1 
ATOM   836  H HZ2  . LYS   A 1 31  ? 21.770 3.613   20.231  1.00 52.77 ?  31  LYS   A HZ2  1 
ATOM   837  H HZ3  . LYS   A 1 31  ? 21.068 2.636   21.039  1.00 52.77 ?  31  LYS   A HZ3  1 
ATOM   838  N N    . PRO   A 1 32  ? 22.916 -3.207  17.118  1.00 16.69 ?  32  PRO   A N    1 
ATOM   839  C CA   . PRO   A 1 32  ? 23.389 -4.548  16.782  1.00 16.85 ?  32  PRO   A CA   1 
ATOM   840  C C    . PRO   A 1 32  ? 24.890 -4.560  16.569  1.00 17.06 ?  32  PRO   A C    1 
ATOM   841  O O    . PRO   A 1 32  ? 25.531 -3.528  16.359  1.00 17.23 ?  32  PRO   A O    1 
ATOM   842  C CB   . PRO   A 1 32  ? 22.663 -4.849  15.468  1.00 17.12 ?  32  PRO   A CB   1 
ATOM   843  C CG   . PRO   A 1 32  ? 22.502 -3.499  14.840  1.00 15.69 ?  32  PRO   A CG   1 
ATOM   844  C CD   . PRO   A 1 32  ? 22.189 -2.592  15.996  1.00 15.63 ?  32  PRO   A CD   1 
ATOM   845  H HA   . PRO   A 1 32  ? 23.134 -5.193  17.464  1.00 20.22 ?  32  PRO   A HA   1 
ATOM   846  H HB2  . PRO   A 1 32  ? 23.212 -5.432  14.916  1.00 20.54 ?  32  PRO   A HB2  1 
ATOM   847  H HB3  . PRO   A 1 32  ? 21.801 -5.259  15.650  1.00 20.54 ?  32  PRO   A HB3  1 
ATOM   848  H HG2  . PRO   A 1 32  ? 23.330 -3.245  14.408  1.00 18.83 ?  32  PRO   A HG2  1 
ATOM   849  H HG3  . PRO   A 1 32  ? 21.771 -3.526  14.205  1.00 18.83 ?  32  PRO   A HG3  1 
ATOM   850  H HD2  . PRO   A 1 32  ? 22.529 -1.700  15.815  1.00 18.75 ?  32  PRO   A HD2  1 
ATOM   851  H HD3  . PRO   A 1 32  ? 21.235 -2.583  16.165  1.00 18.75 ?  32  PRO   A HD3  1 
ATOM   852  N N    . THR   A 1 33  ? 25.446 -5.768  16.598  1.00 16.76 ?  33  THR   A N    1 
ATOM   853  C CA   . THR   A 1 33  ? 26.858 -5.927  16.281  1.00 17.07 ?  33  THR   A CA   1 
ATOM   854  C C    . THR   A 1 33  ? 27.153 -5.462  14.859  1.00 15.92 ?  33  THR   A C    1 
ATOM   855  O O    . THR   A 1 33  ? 28.182 -4.816  14.609  1.00 16.19 ?  33  THR   A O    1 
ATOM   856  C CB   . THR   A 1 33  ? 27.255 -7.389  16.477  1.00 18.86 ?  33  THR   A CB   1 
ATOM   857  O OG1  . THR   A 1 33  ? 26.963 -7.782  17.821  1.00 20.69 ?  33  THR   A OG1  1 
ATOM   858  C CG2  . THR   A 1 33  ? 28.734 -7.593  16.216  1.00 19.67 ?  33  THR   A CG2  1 
ATOM   859  H H    . THR   A 1 33  ? 25.033 -6.493  16.791  1.00 20.11 ?  33  THR   A H    1 
ATOM   860  H HA   . THR   A 1 33  ? 27.384 -5.385  16.893  1.00 20.47 ?  33  THR   A HA   1 
ATOM   861  H HB   . THR   A 1 33  ? 26.747 -7.945  15.863  1.00 22.63 ?  33  THR   A HB   1 
ATOM   862  H HG1  . THR   A 1 33  ? 27.381 -7.294  18.364  1.00 24.82 ?  33  THR   A HG1  1 
ATOM   863  H HG21 . THR   A 1 33  ? 28.993 -8.486  16.490  1.00 23.60 ?  33  THR   A HG21 1 
ATOM   864  H HG22 . THR   A 1 33  ? 28.921 -7.484  15.272  1.00 23.60 ?  33  THR   A HG22 1 
ATOM   865  H HG23 . THR   A 1 33  ? 29.248 -6.946  16.721  1.00 23.60 ?  33  THR   A HG23 1 
ATOM   866  N N    . VAL   A 1 34  ? 26.262 -5.779  13.918  1.00 14.10 ?  34  VAL   A N    1 
ATOM   867  C CA   . VAL   A 1 34  ? 26.456 -5.450  12.509  1.00 13.10 ?  34  VAL   A CA   1 
ATOM   868  C C    . VAL   A 1 34  ? 25.159 -4.892  11.937  1.00 12.59 ?  34  VAL   A C    1 
ATOM   869  O O    . VAL   A 1 34  ? 24.118 -5.559  11.983  1.00 13.38 ?  34  VAL   A O    1 
ATOM   870  C CB   . VAL   A 1 34  ? 26.903 -6.665  11.674  1.00 13.82 ?  34  VAL   A CB   1 
ATOM   871  C CG1  . VAL   A 1 34  ? 27.084 -6.264  10.217  1.00 13.96 ?  34  VAL   A CG1  1 
ATOM   872  C CG2  . VAL   A 1 34  ? 28.182 -7.291  12.242  1.00 15.43 ?  34  VAL   A CG2  1 
ATOM   873  H H    . VAL   A 1 34  ? 25.522 -6.195  14.077  1.00 16.91 ?  34  VAL   A H    1 
ATOM   874  H HA   . VAL   A 1 34  ? 27.136 -4.760  12.434  1.00 15.71 ?  34  VAL   A HA   1 
ATOM   875  H HB   . VAL   A 1 34  ? 26.204 -7.336  11.715  1.00 16.58 ?  34  VAL   A HB   1 
ATOM   876  H HG11 . VAL   A 1 34  ? 27.578 -6.961  9.761   1.00 16.74 ?  34  VAL   A HG11 1 
ATOM   877  H HG12 . VAL   A 1 34  ? 26.213 -6.153  9.806   1.00 16.74 ?  34  VAL   A HG12 1 
ATOM   878  H HG13 . VAL   A 1 34  ? 27.579 -5.430  10.178  1.00 16.74 ?  34  VAL   A HG13 1 
ATOM   879  H HG21 . VAL   A 1 34  ? 28.451 -8.028  11.669  1.00 18.51 ?  34  VAL   A HG21 1 
ATOM   880  H HG22 . VAL   A 1 34  ? 28.880 -6.620  12.268  1.00 18.51 ?  34  VAL   A HG22 1 
ATOM   881  H HG23 . VAL   A 1 34  ? 28.005 -7.620  13.139  1.00 18.51 ?  34  VAL   A HG23 1 
ATOM   882  N N    . VAL   A 1 35  ? 25.223 -3.680  11.385  1.00 11.73 ?  35  VAL   A N    1 
ATOM   883  C CA   . VAL   A 1 35  ? 24.195 -3.167  10.491  1.00 11.47 ?  35  VAL   A CA   1 
ATOM   884  C C    . VAL   A 1 35  ? 24.750 -3.170  9.073   1.00 10.72 ?  35  VAL   A C    1 
ATOM   885  O O    . VAL   A 1 35  ? 25.899 -2.768  8.847   1.00 11.55 ?  35  VAL   A O    1 
ATOM   886  C CB   . VAL   A 1 35  ? 23.670 -1.774  10.903  1.00 12.37 ?  35  VAL   A CB   1 
ATOM   887  C CG1  . VAL   A 1 35  ? 24.739 -0.684  10.769  1.00 12.75 ?  35  VAL   A CG1  1 
ATOM   888  C CG2  . VAL   A 1 35  ? 22.436 -1.423  10.076  1.00 12.85 ?  35  VAL   A CG2  1 
ATOM   889  H H    . VAL   A 1 35  ? 25.864 -3.125  11.513  1.00 14.07 ?  35  VAL   A H    1 
ATOM   890  H HA   . VAL   A 1 35  ? 23.437 -3.777  10.509  1.00 13.76 ?  35  VAL   A HA   1 
ATOM   891  H HB   . VAL   A 1 35  ? 23.389 -1.807  11.829  1.00 14.84 ?  35  VAL   A HB   1 
ATOM   892  H HG11 . VAL   A 1 35  ? 24.395 0.145   11.143  1.00 15.29 ?  35  VAL   A HG11 1 
ATOM   893  H HG12 . VAL   A 1 35  ? 25.530 -0.961  11.254  1.00 15.29 ?  35  VAL   A HG12 1 
ATOM   894  H HG13 . VAL   A 1 35  ? 24.952 -0.557  9.831   1.00 15.29 ?  35  VAL   A HG13 1 
ATOM   895  H HG21 . VAL   A 1 35  ? 22.074 -0.583  10.389  1.00 15.42 ?  35  VAL   A HG21 1 
ATOM   896  H HG22 . VAL   A 1 35  ? 22.694 -1.347  9.142   1.00 15.42 ?  35  VAL   A HG22 1 
ATOM   897  H HG23 . VAL   A 1 35  ? 21.777 -2.129  10.178  1.00 15.42 ?  35  VAL   A HG23 1 
ATOM   898  N N    . VAL   A 1 36  ? 23.936 -3.626  8.124   1.00 10.38 ?  36  VAL   A N    1 
ATOM   899  C CA   . VAL   A 1 36  ? 24.304 -3.637  6.718   1.00 10.19 ?  36  VAL   A CA   1 
ATOM   900  C C    . VAL   A 1 36  ? 23.847 -2.345  6.059   1.00 10.40 ?  36  VAL   A C    1 
ATOM   901  O O    . VAL   A 1 36  ? 22.686 -1.942  6.196   1.00 11.14 ?  36  VAL   A O    1 
ATOM   902  C CB   . VAL   A 1 36  ? 23.696 -4.848  5.997   1.00 10.37 ?  36  VAL   A CB   1 
ATOM   903  C CG1  . VAL   A 1 36  ? 23.960 -4.769  4.519   1.00 10.86 ?  36  VAL   A CG1  1 
ATOM   904  C CG2  . VAL   A 1 36  ? 24.245 -6.140  6.572   1.00 11.19 ?  36  VAL   A CG2  1 
ATOM   905  H H    . VAL   A 1 36  ? 23.145 -3.939  8.276   1.00 12.45 ?  36  VAL   A H    1 
ATOM   906  H HA   . VAL   A 1 36  ? 25.275 -3.700  6.643   1.00 12.22 ?  36  VAL   A HA   1 
ATOM   907  H HB   . VAL   A 1 36  ? 22.732 -4.841  6.133   1.00 12.44 ?  36  VAL   A HB   1 
ATOM   908  H HG11 . VAL   A 1 36  ? 23.828 -5.645  4.128   1.00 13.03 ?  36  VAL   A HG11 1 
ATOM   909  H HG12 . VAL   A 1 36  ? 23.344 -4.134  4.116   1.00 13.03 ?  36  VAL   A HG12 1 
ATOM   910  H HG13 . VAL   A 1 36  ? 24.874 -4.478  4.378   1.00 13.03 ?  36  VAL   A HG13 1 
ATOM   911  H HG21 . VAL   A 1 36  ? 23.849 -6.894  6.098   1.00 13.42 ?  36  VAL   A HG21 1 
ATOM   912  H HG22 . VAL   A 1 36  ? 25.208 -6.155  6.462   1.00 13.42 ?  36  VAL   A HG22 1 
ATOM   913  H HG23 . VAL   A 1 36  ? 24.019 -6.196  7.515   1.00 13.42 ?  36  VAL   A HG23 1 
ATOM   914  N N    . ASN   A 1 37  ? 24.765 -1.714  5.325   1.00 10.06 ?  37  ASN   A N    1 
ATOM   915  C CA   . ASN   A 1 37  ? 24.439 -0.598  4.457   1.00 9.73  ?  37  ASN   A CA   1 
ATOM   916  C C    . ASN   A 1 37  ? 24.311 -1.067  3.017   1.00 9.48  ?  37  ASN   A C    1 
ATOM   917  O O    . ASN   A 1 37  ? 25.098 -1.895  2.543   1.00 10.51 ?  37  ASN   A O    1 
ATOM   918  C CB   . ASN   A 1 37  ? 25.518 0.481   4.535   1.00 10.33 ?  37  ASN   A CB   1 
ATOM   919  C CG   . ASN   A 1 37  ? 25.193 1.680   3.681   1.00 10.45 ?  37  ASN   A CG   1 
ATOM   920  O OD1  . ASN   A 1 37  ? 24.018 2.009   3.496   1.00 11.14 ?  37  ASN   A OD1  1 
ATOM   921  N ND2  . ASN   A 1 37  ? 26.225 2.335   3.149   1.00 10.62 ?  37  ASN   A ND2  1 
ATOM   922  H H    . ASN   A 1 37  ? 25.605 -1.915  5.325   1.00 12.07 ?  37  ASN   A H    1 
ATOM   923  H HA   . ASN   A 1 37  ? 23.602 -0.205  4.735   1.00 11.68 ?  37  ASN   A HA   1 
ATOM   924  H HB2  . ASN   A 1 37  ? 25.602 0.782   5.456   1.00 12.39 ?  37  ASN   A HB2  1 
ATOM   925  H HB3  . ASN   A 1 37  ? 26.365 0.110   4.233   1.00 12.39 ?  37  ASN   A HB3  1 
ATOM   926  H HD21 . ASN   A 1 37  ? 26.086 3.022   2.648   1.00 12.74 ?  37  ASN   A HD21 1 
ATOM   927  H HD22 . ASN   A 1 37  ? 27.026 2.076   3.296   1.00 12.74 ?  37  ASN   A HD22 1 
ATOM   928  N N    A ALA   A 1 38  ? 23.297 -0.525  2.337   0.60 10.07 ?  38  ALA   A N    1 
ATOM   929  N N    B ALA   A 1 38  ? 23.287 -0.565  2.324   0.40 10.23 ?  38  ALA   A N    1 
ATOM   930  C CA   A ALA   A 1 38  ? 23.110 -0.645  0.893   0.60 9.86  ?  38  ALA   A CA   1 
ATOM   931  C CA   B ALA   A 1 38  ? 23.126 -0.832  0.895   0.40 10.77 ?  38  ALA   A CA   1 
ATOM   932  C C    A ALA   A 1 38  ? 24.038 0.350   0.195   0.60 10.15 ?  38  ALA   A C    1 
ATOM   933  C C    B ALA   A 1 38  ? 23.930 0.215   0.130   0.40 10.82 ?  38  ALA   A C    1 
ATOM   934  O O    A ALA   A 1 38  ? 23.644 1.449   -0.202  0.60 9.99  ?  38  ALA   A O    1 
ATOM   935  O O    B ALA   A 1 38  ? 23.421 1.244   -0.321  0.40 10.69 ?  38  ALA   A O    1 
ATOM   936  C CB   A ALA   A 1 38  ? 21.651 -0.381  0.541   0.60 10.27 ?  38  ALA   A CB   1 
ATOM   937  C CB   B ALA   A 1 38  ? 21.655 -0.835  0.505   0.40 11.34 ?  38  ALA   A CB   1 
ATOM   938  H H    A ALA   A 1 38  ? 22.685 -0.053  2.715   0.60 12.08 ?  38  ALA   A H    1 
ATOM   939  H H    B ALA   A 1 38  ? 22.675 -0.056  2.659   0.40 12.27 ?  38  ALA   A H    1 
ATOM   940  H HA   A ALA   A 1 38  ? 23.342 -1.541  0.608   0.60 11.82 ?  38  ALA   A HA   1 
ATOM   941  H HA   B ALA   A 1 38  ? 23.494 -1.709  0.693   0.40 12.92 ?  38  ALA   A HA   1 
ATOM   942  H HB1  A ALA   A 1 38  ? 21.535 -0.465  -0.418  0.60 12.31 ?  38  ALA   A HB1  1 
ATOM   943  H HB1  B ALA   A 1 38  ? 21.587 -0.952  -0.456  0.40 13.61 ?  38  ALA   A HB1  1 
ATOM   944  H HB2  A ALA   A 1 38  ? 21.091 -1.029  1.000   0.60 12.31 ?  38  ALA   A HB2  1 
ATOM   945  H HB2  B ALA   A 1 38  ? 21.206 -1.566  0.958   0.40 13.61 ?  38  ALA   A HB2  1 
ATOM   946  H HB3  A ALA   A 1 38  ? 21.413 0.517   0.825   0.60 12.31 ?  38  ALA   A HB3  1 
ATOM   947  H HB3  B ALA   A 1 38  ? 21.259 0.010   0.761   0.40 13.61 ?  38  ALA   A HB3  1 
ATOM   948  N N    A ALA   A 1 39  ? 25.297 -0.053  0.042   0.60 9.94  ?  39  ALA   A N    1 
ATOM   949  N N    B ALA   A 1 39  ? 25.221 -0.061  -0.005  0.40 11.08 ?  39  ALA   A N    1 
ATOM   950  C CA   A ALA   A 1 39  ? 26.364 0.816   -0.429  0.60 9.56  ?  39  ALA   A CA   1 
ATOM   951  C CA   B ALA   A 1 39  ? 26.179 0.900   -0.519  0.40 11.01 ?  39  ALA   A CA   1 
ATOM   952  C C    A ALA   A 1 39  ? 26.497 0.781   -1.947  0.60 9.83  ?  39  ALA   A C    1 
ATOM   953  C C    B ALA   A 1 39  ? 26.321 0.784   -2.032  0.40 10.69 ?  39  ALA   A C    1 
ATOM   954  O O    A ALA   A 1 39  ? 25.999 -0.123  -2.622  0.60 10.50 ?  39  ALA   A O    1 
ATOM   955  O O    B ALA   A 1 39  ? 25.892 -0.189  -2.657  0.40 11.34 ?  39  ALA   A O    1 
ATOM   956  C CB   A ALA   A 1 39  ? 27.689 0.394   0.216   0.60 10.17 ?  39  ALA   A CB   1 
ATOM   957  C CB   B ALA   A 1 39  ? 27.535 0.676   0.149   0.40 12.01 ?  39  ALA   A CB   1 
ATOM   958  H H    A ALA   A 1 39  ? 25.562 -0.857  0.213   0.60 11.93 ?  39  ALA   A H    1 
ATOM   959  H H    B ALA   A 1 39  ? 25.569 -0.822  0.199   0.40 13.29 ?  39  ALA   A H    1 
ATOM   960  H HA   A ALA   A 1 39  ? 26.174 1.726   -0.165  0.60 11.47 ?  39  ALA   A HA   1 
ATOM   961  H HA   B ALA   A 1 39  ? 25.875 1.794   -0.304  0.40 13.20 ?  39  ALA   A HA   1 
ATOM   962  H HB1  A ALA   A 1 39  ? 28.394 0.982   -0.103  0.60 12.20 ?  39  ALA   A HB1  1 
ATOM   963  H HB1  B ALA   A 1 39  ? 28.166 1.322   -0.199  0.40 14.40 ?  39  ALA   A HB1  1 
ATOM   964  H HB2  A ALA   A 1 39  ? 27.609 0.477   1.182   0.60 12.20 ?  39  ALA   A HB2  1 
ATOM   965  H HB2  B ALA   A 1 39  ? 27.435 0.791   1.108   0.40 14.40 ?  39  ALA   A HB2  1 
ATOM   966  H HB3  A ALA   A 1 39  ? 27.885 -0.521  -0.023  0.60 12.20 ?  39  ALA   A HB3  1 
ATOM   967  H HB3  B ALA   A 1 39  ? 27.837 -0.225  -0.046  0.40 14.40 ?  39  ALA   A HB3  1 
ATOM   968  N N    A ASN   A 1 40  ? 27.212 1.776   -2.477  0.60 10.08 ?  40  ASN   A N    1 
ATOM   969  N N    B ASN   A 1 40  ? 26.933 1.807   -2.622  0.40 10.58 ?  40  ASN   A N    1 
ATOM   970  C CA   A ASN   A 1 40  ? 27.758 1.734   -3.828  0.60 10.10 ?  40  ASN   A CA   1 
ATOM   971  C CA   B ASN   A 1 40  ? 27.442 1.751   -3.983  0.40 10.43 ?  40  ASN   A CA   1 
ATOM   972  C C    A ASN   A 1 40  ? 29.280 1.613   -3.757  0.60 9.61  ?  40  ASN   A C    1 
ATOM   973  C C    B ASN   A 1 40  ? 28.964 1.640   -3.940  0.40 10.11 ?  40  ASN   A C    1 
ATOM   974  O O    A ASN   A 1 40  ? 29.878 1.698   -2.679  0.60 9.79  ?  40  ASN   A O    1 
ATOM   975  O O    B ASN   A 1 40  ? 29.586 1.749   -2.880  0.40 10.54 ?  40  ASN   A O    1 
ATOM   976  C CB   A ASN   A 1 40  ? 27.289 2.921   -4.693  0.60 11.11 ?  40  ASN   A CB   1 
ATOM   977  C CB   B ASN   A 1 40  ? 26.983 2.966   -4.802  0.40 11.04 ?  40  ASN   A CB   1 
ATOM   978  C CG   A ASN   A 1 40  ? 27.656 4.274   -4.113  0.60 12.27 ?  40  ASN   A CG   1 
ATOM   979  C CG   B ASN   A 1 40  ? 27.373 4.284   -4.167  0.40 11.56 ?  40  ASN   A CG   1 
ATOM   980  O OD1  A ASN   A 1 40  ? 28.809 4.514   -3.745  0.60 12.62 ?  40  ASN   A OD1  1 
ATOM   981  O OD1  B ASN   A 1 40  ? 28.557 4.575   -3.994  0.40 12.26 ?  40  ASN   A OD1  1 
ATOM   982  N ND2  A ASN   A 1 40  ? 26.670 5.175   -4.044  0.60 13.49 ?  40  ASN   A ND2  1 
ATOM   983  N ND2  B ASN   A 1 40  ? 26.376 5.099   -3.832  0.40 11.95 ?  40  ASN   A ND2  1 
ATOM   984  H H    A ASN   A 1 40  ? 27.401 2.502   -2.060  0.60 12.09 ?  40  ASN   A H    1 
ATOM   985  H H    B ASN   A 1 40  ? 27.062 2.566   -2.239  0.40 12.68 ?  40  ASN   A H    1 
ATOM   986  H HA   A ASN   A 1 40  ? 27.437 0.932   -4.260  0.60 12.11 ?  40  ASN   A HA   1 
ATOM   987  H HA   B ASN   A 1 40  ? 27.093 0.951   -4.415  0.40 12.51 ?  40  ASN   A HA   1 
ATOM   988  H HB2  A ASN   A 1 40  ? 27.696 2.848   -5.578  0.60 13.32 ?  40  ASN   A HB2  1 
ATOM   989  H HB2  B ASN   A 1 40  ? 27.388 2.921   -5.680  0.40 13.25 ?  40  ASN   A HB2  1 
ATOM   990  H HB3  A ASN   A 1 40  ? 26.324 2.884   -4.780  0.60 13.32 ?  40  ASN   A HB3  1 
ATOM   991  H HB3  B ASN   A 1 40  ? 26.015 2.936   -4.886  0.40 13.25 ?  40  ASN   A HB3  1 
ATOM   992  H HD21 A ASN   A 1 40  ? 26.824 5.966   -3.738  0.60 16.18 ?  40  ASN   A HD21 1 
ATOM   993  H HD21 B ASN   A 1 40  ? 26.550 5.858   -3.468  0.40 14.33 ?  40  ASN   A HD21 1 
ATOM   994  H HD22 A ASN   A 1 40  ? 25.876 4.968   -4.306  0.60 16.18 ?  40  ASN   A HD22 1 
ATOM   995  H HD22 B ASN   A 1 40  ? 25.560 4.867   -3.976  0.40 14.33 ?  40  ASN   A HD22 1 
ATOM   996  N N    A VAL   A 1 41  ? 29.902 1.373   -4.917  0.60 10.15 ?  41  VAL   A N    1 
ATOM   997  N N    B VAL   A 1 41  ? 29.565 1.404   -5.109  0.40 10.10 ?  41  VAL   A N    1 
ATOM   998  C CA   A VAL   A 1 41  ? 31.329 1.046   -4.932  0.60 10.68 ?  41  VAL   A CA   1 
ATOM   999  C CA   B VAL   A 1 41  ? 30.994 1.100   -5.168  0.40 10.72 ?  41  VAL   A CA   1 
ATOM   1000 C C    A VAL   A 1 41  ? 32.180 2.202   -4.438  0.60 10.79 ?  41  VAL   A C    1 
ATOM   1001 C C    B VAL   A 1 41  ? 31.871 2.236   -4.658  0.40 11.02 ?  41  VAL   A C    1 
ATOM   1002 O O    A VAL   A 1 41  ? 33.308 1.993   -3.976  0.60 10.84 ?  41  VAL   A O    1 
ATOM   1003 O O    B VAL   A 1 41  ? 33.032 2.004   -4.302  0.40 10.94 ?  41  VAL   A O    1 
ATOM   1004 C CB   A VAL   A 1 41  ? 31.818 0.547   -6.313  0.60 10.71 ?  41  VAL   A CB   1 
ATOM   1005 C CB   B VAL   A 1 41  ? 31.427 0.682   -6.592  0.40 11.94 ?  41  VAL   A CB   1 
ATOM   1006 C CG1  A VAL   A 1 41  ? 31.116 -0.741  -6.701  0.60 11.29 ?  41  VAL   A CG1  1 
ATOM   1007 C CG1  B VAL   A 1 41  ? 30.778 -0.636  -6.985  0.40 12.88 ?  41  VAL   A CG1  1 
ATOM   1008 C CG2  A VAL   A 1 41  ? 31.671 1.611   -7.400  0.60 10.40 ?  41  VAL   A CG2  1 
ATOM   1009 C CG2  B VAL   A 1 41  ? 31.105 1.775   -7.608  0.40 12.38 ?  41  VAL   A CG2  1 
ATOM   1010 H H    A VAL   A 1 41  ? 29.534 1.388   -5.691  0.60 12.18 ?  41  VAL   A H    1 
ATOM   1011 H H    B VAL   A 1 41  ? 29.163 1.404   -5.869  0.40 12.11 ?  41  VAL   A H    1 
ATOM   1012 H HA   A VAL   A 1 41  ? 31.478 0.321   -4.313  0.60 12.81 ?  41  VAL   A HA   1 
ATOM   1013 H HA   B VAL   A 1 41  ? 31.156 0.337   -4.592  0.40 12.85 ?  41  VAL   A HA   1 
ATOM   1014 H HB   A VAL   A 1 41  ? 32.767 0.345   -6.247  0.60 12.84 ?  41  VAL   A HB   1 
ATOM   1015 H HB   B VAL   A 1 41  ? 32.388 0.547   -6.596  0.40 14.32 ?  41  VAL   A HB   1 
ATOM   1016 H HG11 A VAL   A 1 41  ? 31.452 -1.045  -7.557  0.60 13.55 ?  41  VAL   A HG11 1 
ATOM   1017 H HG11 B VAL   A 1 41  ? 31.047 -0.862  -7.889  0.40 15.44 ?  41  VAL   A HG11 1 
ATOM   1018 H HG12 A VAL   A 1 41  ? 31.285 -1.410  -6.020  0.60 13.55 ?  41  VAL   A HG12 1 
ATOM   1019 H HG12 B VAL   A 1 41  ? 31.071 -1.329  -6.371  0.40 15.44 ?  41  VAL   A HG12 1 
ATOM   1020 H HG13 A VAL   A 1 41  ? 30.160 -0.570  -6.764  0.60 13.55 ?  41  VAL   A HG13 1 
ATOM   1021 H HG13 B VAL   A 1 41  ? 29.815 -0.542  -6.940  0.40 15.44 ?  41  VAL   A HG13 1 
ATOM   1022 H HG21 A VAL   A 1 41  ? 31.922 1.223   -8.257  0.60 12.48 ?  41  VAL   A HG21 1 
ATOM   1023 H HG21 B VAL   A 1 41  ? 31.421 1.495   -8.481  0.40 14.85 ?  41  VAL   A HG21 1 
ATOM   1024 H HG22 A VAL   A 1 41  ? 30.752 1.907   -7.428  0.60 12.48 ?  41  VAL   A HG22 1 
ATOM   1025 H HG22 B VAL   A 1 41  ? 30.144 1.911   -7.634  0.40 14.85 ?  41  VAL   A HG22 1 
ATOM   1026 H HG23 A VAL   A 1 41  ? 32.259 2.356   -7.195  0.60 12.48 ?  41  VAL   A HG23 1 
ATOM   1027 H HG23 B VAL   A 1 41  ? 31.549 2.594   -7.343  0.40 14.85 ?  41  VAL   A HG23 1 
ATOM   1028 N N    A TYR   A 1 42  ? 31.685 3.432   -4.560  0.60 10.75 ?  42  TYR   A N    1 
ATOM   1029 N N    B TYR   A 1 42  ? 31.360 3.468   -4.641  0.40 11.02 ?  42  TYR   A N    1 
ATOM   1030 C CA   A TYR   A 1 42  ? 32.407 4.619   -4.121  0.60 11.17 ?  42  TYR   A CA   1 
ATOM   1031 C CA   B TYR   A 1 42  ? 32.138 4.641   -4.252  0.40 10.84 ?  42  TYR   A CA   1 
ATOM   1032 C C    A TYR   A 1 42  ? 32.087 4.988   -2.685  0.60 11.00 ?  42  TYR   A C    1 
ATOM   1033 C C    B TYR   A 1 42  ? 31.971 5.016   -2.785  0.40 11.07 ?  42  TYR   A C    1 
ATOM   1034 O O    A TYR   A 1 42  ? 32.647 5.964   -2.166  0.60 11.59 ?  42  TYR   A O    1 
ATOM   1035 O O    B TYR   A 1 42  ? 32.543 6.020   -2.344  0.40 11.52 ?  42  TYR   A O    1 
ATOM   1036 C CB   A TYR   A 1 42  ? 32.107 5.808   -5.053  0.60 11.62 ?  42  TYR   A CB   1 
ATOM   1037 C CB   B TYR   A 1 42  ? 31.749 5.840   -5.124  0.40 10.76 ?  42  TYR   A CB   1 
ATOM   1038 C CG   A TYR   A 1 42  ? 32.306 5.479   -6.517  0.60 11.76 ?  42  TYR   A CG   1 
ATOM   1039 C CG   B TYR   A 1 42  ? 31.898 5.561   -6.599  0.40 11.08 ?  42  TYR   A CG   1 
ATOM   1040 C CD1  A TYR   A 1 42  ? 33.578 5.274   -7.033  0.60 12.24 ?  42  TYR   A CD1  1 
ATOM   1041 C CD1  B TYR   A 1 42  ? 33.153 5.373   -7.162  0.40 11.30 ?  42  TYR   A CD1  1 
ATOM   1042 C CD2  A TYR   A 1 42  ? 31.222 5.333   -7.374  0.60 12.87 ?  42  TYR   A CD2  1 
ATOM   1043 C CD2  B TYR   A 1 42  ? 30.785 5.457   -7.426  0.40 12.24 ?  42  TYR   A CD2  1 
ATOM   1044 C CE1  A TYR   A 1 42  ? 33.767 4.954   -8.369  0.60 12.69 ?  42  TYR   A CE1  1 
ATOM   1045 C CE1  B TYR   A 1 42  ? 33.300 5.104   -8.509  0.40 11.73 ?  42  TYR   A CE1  1 
ATOM   1046 C CE2  A TYR   A 1 42  ? 31.402 5.016   -8.712  0.60 13.33 ?  42  TYR   A CE2  1 
ATOM   1047 C CE2  B TYR   A 1 42  ? 30.923 5.195   -8.778  0.40 12.86 ?  42  TYR   A CE2  1 
ATOM   1048 C CZ   A TYR   A 1 42  ? 32.677 4.827   -9.203  0.60 13.45 ?  42  TYR   A CZ   1 
ATOM   1049 C CZ   B TYR   A 1 42  ? 32.183 5.015   -9.311  0.40 12.81 ?  42  TYR   A CZ   1 
ATOM   1050 O OH   A TYR   A 1 42  ? 32.870 4.503   -10.528 0.60 14.49 ?  42  TYR   A OH   1 
ATOM   1051 O OH   B TYR   A 1 42  ? 32.332 4.754   -10.654 0.40 13.77 ?  42  TYR   A OH   1 
ATOM   1052 H H    A TYR   A 1 42  ? 30.914 3.608   -4.892  0.60 12.89 ?  42  TYR   A H    1 
ATOM   1053 H H    B TYR   A 1 42  ? 30.548 3.651   -4.865  0.40 13.22 ?  42  TYR   A H    1 
ATOM   1054 H HA   A TYR   A 1 42  ? 33.360 4.448   -4.164  0.60 13.40 ?  42  TYR   A HA   1 
ATOM   1055 H HA   B TYR   A 1 42  ? 33.073 4.454   -4.418  0.40 13.01 ?  42  TYR   A HA   1 
ATOM   1056 H HB2  A TYR   A 1 42  ? 31.186 6.082   -4.933  0.60 13.94 ?  42  TYR   A HB2  1 
ATOM   1057 H HB2  B TYR   A 1 42  ? 30.821 6.071   -4.953  0.40 12.90 ?  42  TYR   A HB2  1 
ATOM   1058 H HB3  A TYR   A 1 42  ? 32.703 6.544   -4.831  0.60 13.94 ?  42  TYR   A HB3  1 
ATOM   1059 H HB3  B TYR   A 1 42  ? 32.321 6.593   -4.899  0.40 12.90 ?  42  TYR   A HB3  1 
ATOM   1060 H HD1  A TYR   A 1 42  ? 34.323 5.362   -6.475  0.60 14.69 ?  42  TYR   A HD1  1 
ATOM   1061 H HD1  B TYR   A 1 42  ? 33.908 5.432   -6.624  0.40 13.55 ?  42  TYR   A HD1  1 
ATOM   1062 H HD2  A TYR   A 1 42  ? 30.363 5.462   -7.046  0.60 15.43 ?  42  TYR   A HD2  1 
ATOM   1063 H HD2  B TYR   A 1 42  ? 29.933 5.580   -7.069  0.40 14.68 ?  42  TYR   A HD2  1 
ATOM   1064 H HE1  A TYR   A 1 42  ? 34.630 4.828   -8.703  0.60 15.22 ?  42  TYR   A HE1  1 
ATOM   1065 H HE1  B TYR   A 1 42  ? 34.145 4.982   -8.875  0.40 14.07 ?  42  TYR   A HE1  1 
ATOM   1066 H HE2  A TYR   A 1 42  ? 30.667 4.929   -9.274  0.60 15.99 ?  42  TYR   A HE2  1 
ATOM   1067 H HE2  B TYR   A 1 42  ? 30.168 5.130   -9.321  0.40 15.43 ?  42  TYR   A HE2  1 
ATOM   1068 H HH   A TYR   A 1 42  ? 33.682 4.333   -10.665 0.60 17.38 ?  42  TYR   A HH   1 
ATOM   1069 H HH   B TYR   A 1 42  ? 31.581 4.721   -11.029 0.40 16.51 ?  42  TYR   A HH   1 
ATOM   1070 N N    . LEU   A 1 43  ? 31.187 4.242   -2.037  1.00 10.91 ?  43  LEU   A N    1 
ATOM   1071 C CA   . LEU   A 1 43  ? 30.749 4.584   -0.686  1.00 10.63 ?  43  LEU   A CA   1 
ATOM   1072 C C    . LEU   A 1 43  ? 30.264 6.029   -0.594  1.00 10.77 ?  43  LEU   A C    1 
ATOM   1073 O O    . LEU   A 1 43  ? 30.515 6.727   0.389   1.00 11.84 ?  43  LEU   A O    1 
ATOM   1074 C CB   . LEU   A 1 43  ? 31.795 4.273   0.380   1.00 11.40 ?  43  LEU   A CB   1 
ATOM   1075 C CG   . LEU   A 1 43  ? 32.289 2.826   0.461   1.00 11.41 ?  43  LEU   A CG   1 
ATOM   1076 C CD1  . LEU   A 1 43  ? 33.324 2.710   1.563   1.00 12.28 ?  43  LEU   A CD1  1 
ATOM   1077 C CD2  . LEU   A 1 43  ? 31.146 1.842   0.690   1.00 12.29 ?  43  LEU   A CD2  1 
ATOM   1078 H H    A LEU   A 1 43  ? 30.832 3.518   -2.348  0.60 13.09 ?  43  LEU   A H    1 
ATOM   1079 H H    B LEU   A 1 43  ? 30.868 3.484   -2.305  0.40 13.09 ?  43  LEU   A H    1 
ATOM   1080 H HA   . LEU   A 1 43  ? 29.981 4.025   -0.479  1.00 12.75 ?  43  LEU   A HA   1 
ATOM   1081 H HB2  . LEU   A 1 43  ? 32.569 4.836   0.224   1.00 13.67 ?  43  LEU   A HB2  1 
ATOM   1082 H HB3  . LEU   A 1 43  ? 31.415 4.491   1.250   1.00 13.67 ?  43  LEU   A HB3  1 
ATOM   1083 H HG   . LEU   A 1 43  ? 32.721 2.596   -0.376  1.00 13.69 ?  43  LEU   A HG   1 
ATOM   1084 H HD11 . LEU   A 1 43  ? 33.636 1.794   1.609   1.00 14.73 ?  43  LEU   A HD11 1 
ATOM   1085 H HD12 . LEU   A 1 43  ? 34.066 3.304   1.364   1.00 14.73 ?  43  LEU   A HD12 1 
ATOM   1086 H HD13 . LEU   A 1 43  ? 32.916 2.964   2.407   1.00 14.73 ?  43  LEU   A HD13 1 
ATOM   1087 H HD21 . LEU   A 1 43  ? 31.517 0.960   0.834   1.00 14.74 ?  43  LEU   A HD21 1 
ATOM   1088 H HD22 . LEU   A 1 43  ? 30.641 2.125   1.466   1.00 14.74 ?  43  LEU   A HD22 1 
ATOM   1089 H HD23 . LEU   A 1 43  ? 30.576 1.840   -0.095  1.00 14.74 ?  43  LEU   A HD23 1 
ATOM   1090 N N    A LYS   A 1 44  ? 29.535 6.471   -1.621  0.60 10.87 ?  44  LYS   A N    1 
ATOM   1091 N N    B LYS   A 1 44  ? 29.553 6.470   -1.633  0.40 11.22 ?  44  LYS   A N    1 
ATOM   1092 C CA   A LYS   A 1 44  ? 28.904 7.791   -1.616  0.60 11.34 ?  44  LYS   A CA   1 
ATOM   1093 C CA   B LYS   A 1 44  ? 28.887 7.767   -1.640  0.40 11.96 ?  44  LYS   A CA   1 
ATOM   1094 C C    A LYS   A 1 44  ? 27.472 7.615   -1.132  0.60 10.81 ?  44  LYS   A C    1 
ATOM   1095 C C    B LYS   A 1 44  ? 27.475 7.554   -1.112  0.40 11.01 ?  44  LYS   A C    1 
ATOM   1096 O O    A LYS   A 1 44  ? 26.601 7.142   -1.867  0.60 12.26 ?  44  LYS   A O    1 
ATOM   1097 O O    B LYS   A 1 44  ? 26.622 6.984   -1.801  0.40 11.24 ?  44  LYS   A O    1 
ATOM   1098 C CB   A LYS   A 1 44  ? 28.978 8.431   -2.995  0.60 13.49 ?  44  LYS   A CB   1 
ATOM   1099 C CB   B LYS   A 1 44  ? 28.871 8.352   -3.050  0.40 14.40 ?  44  LYS   A CB   1 
ATOM   1100 C CG   A LYS   A 1 44  ? 30.378 8.866   -3.392  0.60 16.86 ?  44  LYS   A CG   1 
ATOM   1101 C CG   B LYS   A 1 44  ? 30.219 8.852   -3.533  0.40 17.67 ?  44  LYS   A CG   1 
ATOM   1102 C CD   A LYS   A 1 44  ? 31.001 9.833   -2.384  0.60 21.61 ?  44  LYS   A CD   1 
ATOM   1103 C CD   B LYS   A 1 44  ? 30.938 9.646   -2.454  0.40 21.47 ?  44  LYS   A CD   1 
ATOM   1104 C CE   A LYS   A 1 44  ? 32.375 10.297  -2.841  0.60 24.51 ?  44  LYS   A CE   1 
ATOM   1105 C CE   B LYS   A 1 44  ? 32.045 10.501  -3.037  0.40 23.69 ?  44  LYS   A CE   1 
ATOM   1106 N NZ   A LYS   A 1 44  ? 33.167 10.888  -1.731  0.60 26.08 ?  44  LYS   A NZ   1 
ATOM   1107 N NZ   B LYS   A 1 44  ? 32.905 11.085  -1.975  0.40 25.20 ?  44  LYS   A NZ   1 
ATOM   1108 H H    A LYS   A 1 44  ? 29.395 6.016   -2.339  0.60 13.03 ?  44  LYS   A H    1 
ATOM   1109 H H    B LYS   A 1 44  ? 29.434 6.018   -2.356  0.40 13.46 ?  44  LYS   A H    1 
ATOM   1110 H HA   A LYS   A 1 44  ? 29.356 8.357   -0.977  0.60 13.60 ?  44  LYS   A HA   1 
ATOM   1111 H HA   B LYS   A 1 44  ? 29.338 8.375   -1.034  0.40 14.34 ?  44  LYS   A HA   1 
ATOM   1112 H HB2  A LYS   A 1 44  ? 28.666 7.796   -3.656  0.60 16.18 ?  44  LYS   A HB2  1 
ATOM   1113 H HB2  B LYS   A 1 44  ? 28.576 7.667   -3.670  0.40 17.28 ?  44  LYS   A HB2  1 
ATOM   1114 H HB3  A LYS   A 1 44  ? 28.410 9.219   -3.002  0.60 16.18 ?  44  LYS   A HB3  1 
ATOM   1115 H HB3  B LYS   A 1 44  ? 28.257 9.102   -3.074  0.40 17.28 ?  44  LYS   A HB3  1 
ATOM   1116 H HG2  A LYS   A 1 44  ? 30.949 8.084   -3.449  0.60 20.23 ?  44  LYS   A HG2  1 
ATOM   1117 H HG2  B LYS   A 1 44  ? 30.774 8.096   -3.777  0.40 21.20 ?  44  LYS   A HG2  1 
ATOM   1118 H HG3  A LYS   A 1 44  ? 30.341 9.315   -4.252  0.60 20.23 ?  44  LYS   A HG3  1 
ATOM   1119 H HG3  B LYS   A 1 44  ? 30.090 9.435   -4.301  0.40 21.20 ?  44  LYS   A HG3  1 
ATOM   1120 H HD2  A LYS   A 1 44  ? 30.425 10.608  -2.287  0.60 25.93 ?  44  LYS   A HD2  1 
ATOM   1121 H HD2  B LYS   A 1 44  ? 30.300 10.225  -2.006  0.40 25.76 ?  44  LYS   A HD2  1 
ATOM   1122 H HD3  A LYS   A 1 44  ? 31.109 9.385   -1.530  0.60 25.93 ?  44  LYS   A HD3  1 
ATOM   1123 H HD3  B LYS   A 1 44  ? 31.333 9.026   -1.816  0.40 25.76 ?  44  LYS   A HD3  1 
ATOM   1124 H HE2  A LYS   A 1 44  ? 32.866 9.537   -3.190  0.60 29.40 ?  44  LYS   A HE2  1 
ATOM   1125 H HE2  B LYS   A 1 44  ? 32.601 9.952   -3.612  0.40 28.42 ?  44  LYS   A HE2  1 
ATOM   1126 H HE3  A LYS   A 1 44  ? 32.268 10.970  -3.530  0.60 29.40 ?  44  LYS   A HE3  1 
ATOM   1127 H HE3  B LYS   A 1 44  ? 31.652 11.227  -3.544  0.40 28.42 ?  44  LYS   A HE3  1 
ATOM   1128 H HZ1  A LYS   A 1 44  ? 33.962 11.151  -2.031  0.60 31.29 ?  44  LYS   A HZ1  1 
ATOM   1129 H HZ1  B LYS   A 1 44  ? 33.545 11.581  -2.342  0.40 30.24 ?  44  LYS   A HZ1  1 
ATOM   1130 H HZ2  A LYS   A 1 44  ? 32.738 11.595  -1.396  0.60 31.29 ?  44  LYS   A HZ2  1 
ATOM   1131 H HZ2  B LYS   A 1 44  ? 32.416 11.595  -1.435  0.40 30.24 ?  44  LYS   A HZ2  1 
ATOM   1132 H HZ3  A LYS   A 1 44  ? 33.283 10.289  -1.085  0.60 31.29 ?  44  LYS   A HZ3  1 
ATOM   1133 H HZ3  B LYS   A 1 44  ? 33.281 10.435  -1.497  0.40 30.24 ?  44  LYS   A HZ3  1 
ATOM   1134 N N    . HIS   A 1 45  ? 27.240 7.975   0.126   1.00 10.68 ?  45  HIS   A N    1 
ATOM   1135 C CA   . HIS   A 1 45  ? 26.002 7.637   0.822   1.00 10.61 ?  45  HIS   A CA   1 
ATOM   1136 C C    . HIS   A 1 45  ? 24.971 8.754   0.649   1.00 11.92 ?  45  HIS   A C    1 
ATOM   1137 O O    . HIS   A 1 45  ? 24.678 9.526   1.563   1.00 13.77 ?  45  HIS   A O    1 
ATOM   1138 C CB   . HIS   A 1 45  ? 26.293 7.389   2.288   1.00 10.62 ?  45  HIS   A CB   1 
ATOM   1139 C CG   . HIS   A 1 45  ? 27.400 6.421   2.521   1.00 10.29 ?  45  HIS   A CG   1 
ATOM   1140 N ND1  . HIS   A 1 45  ? 27.396 5.134   2.021   1.00 10.95 ?  45  HIS   A ND1  1 
ATOM   1141 C CD2  . HIS   A 1 45  ? 28.563 6.573   3.195   1.00 10.39 ?  45  HIS   A CD2  1 
ATOM   1142 C CE1  . HIS   A 1 45  ? 28.517 4.538   2.390   1.00 10.64 ?  45  HIS   A CE1  1 
ATOM   1143 N NE2  . HIS   A 1 45  ? 29.240 5.386   3.105   1.00 10.90 ?  45  HIS   A NE2  1 
ATOM   1144 H H    A HIS   A 1 45  ? 27.787 8.438   0.601   0.60 12.81 ?  45  HIS   A H    1 
ATOM   1145 H H    B HIS   A 1 45  ? 27.779 8.461   0.587   0.40 12.81 ?  45  HIS   A H    1 
ATOM   1146 H HA   . HIS   A 1 45  ? 25.630 6.822   0.441   1.00 12.73 ?  45  HIS   A HA   1 
ATOM   1147 H HB2  . HIS   A 1 45  ? 26.534 8.230   2.702   1.00 12.73 ?  45  HIS   A HB2  1 
ATOM   1148 H HB3  . HIS   A 1 45  ? 25.490 7.035   2.709   1.00 12.73 ?  45  HIS   A HB3  1 
ATOM   1149 H HD2  . HIS   A 1 45  ? 28.849 7.342   3.635   1.00 12.46 ?  45  HIS   A HD2  1 
ATOM   1150 H HE1  . HIS   A 1 45  ? 28.748 3.660   2.197   1.00 12.76 ?  45  HIS   A HE1  1 
ATOM   1151 H HE2  . HIS   A 1 45  ? 30.007 5.219   3.453   1.00 13.07 ?  45  HIS   A HE2  1 
ATOM   1152 N N    . GLY   A 1 46  ? 24.404 8.822   -0.551  1.00 12.66 ?  46  GLY   A N    1 
ATOM   1153 C CA   . GLY   A 1 46  ? 23.580 9.963   -0.910  1.00 13.59 ?  46  GLY   A CA   1 
ATOM   1154 C C    . GLY   A 1 46  ? 22.099 9.840   -0.611  1.00 13.46 ?  46  GLY   A C    1 
ATOM   1155 O O    . GLY   A 1 46  ? 21.449 10.832  -0.262  1.00 14.99 ?  46  GLY   A O    1 
ATOM   1156 H H    . GLY   A 1 46  ? 24.467 8.224   -1.164  1.00 15.19 ?  46  GLY   A H    1 
ATOM   1157 H HA2  . GLY   A 1 46  ? 23.907 10.747  -0.438  1.00 16.30 ?  46  GLY   A HA2  1 
ATOM   1158 H HA3  . GLY   A 1 46  ? 23.675 10.131  -1.860  1.00 16.30 ?  46  GLY   A HA3  1 
ATOM   1159 N N    A GLY   A 1 47  ? 21.564 8.644   -0.796  0.60 13.19 ?  47  GLY   A N    1 
ATOM   1160 N N    B GLY   A 1 47  ? 21.548 8.629   -0.695  0.40 13.06 ?  47  GLY   A N    1 
ATOM   1161 C CA   A GLY   A 1 47  ? 20.133 8.439   -0.753  0.60 13.15 ?  47  GLY   A CA   1 
ATOM   1162 C CA   B GLY   A 1 47  ? 20.122 8.441   -0.480  0.40 12.81 ?  47  GLY   A CA   1 
ATOM   1163 C C    A GLY   A 1 47  ? 19.833 7.000   -0.405  0.60 12.64 ?  47  GLY   A C    1 
ATOM   1164 C C    B GLY   A 1 47  ? 19.773 7.027   -0.060  0.40 11.74 ?  47  GLY   A C    1 
ATOM   1165 O O    A GLY   A 1 47  ? 20.733 6.187   -0.183  0.60 13.19 ?  47  GLY   A O    1 
ATOM   1166 O O    B GLY   A 1 47  ? 20.645 6.177   0.139   0.40 11.64 ?  47  GLY   A O    1 
ATOM   1167 H H    A GLY   A 1 47  ? 22.023 7.932   -0.939  0.60 15.82 ?  47  GLY   A H    1 
ATOM   1168 H H    B GLY   A 1 47  ? 21.978 7.907   -0.869  0.40 15.66 ?  47  GLY   A H    1 
ATOM   1169 H HA2  A GLY   A 1 47  ? 19.735 9.021   -0.088  0.60 15.77 ?  47  GLY   A HA2  1 
ATOM   1170 H HA2  B GLY   A 1 47  ? 19.812 9.042   0.214   0.40 15.37 ?  47  GLY   A HA2  1 
ATOM   1171 H HA3  A GLY   A 1 47  ? 19.750 8.644   -1.621  0.60 15.77 ?  47  GLY   A HA3  1 
ATOM   1172 H HA3  B GLY   A 1 47  ? 19.641 8.640   -1.297  0.40 15.37 ?  47  GLY   A HA3  1 
ATOM   1173 N N    A GLY   A 1 48  ? 18.546 6.682   -0.380  0.60 12.05 ?  48  GLY   A N    1 
ATOM   1174 N N    B GLY   A 1 48  ? 18.467 6.785   0.078   0.40 11.85 ?  48  GLY   A N    1 
ATOM   1175 C CA   A GLY   A 1 48  ? 18.158 5.355   0.025   0.60 12.04 ?  48  GLY   A CA   1 
ATOM   1176 C CA   B GLY   A 1 48  ? 17.995 5.465   0.475   0.40 11.70 ?  48  GLY   A CA   1 
ATOM   1177 C C    A GLY   A 1 48  ? 18.588 5.079   1.451   0.60 11.56 ?  48  GLY   A C    1 
ATOM   1178 C C    B GLY   A 1 48  ? 18.566 5.053   1.817   0.40 11.18 ?  48  GLY   A C    1 
ATOM   1179 O O    A GLY   A 1 48  ? 18.745 5.990   2.277   0.60 11.77 ?  48  GLY   A O    1 
ATOM   1180 O O    B GLY   A 1 48  ? 18.703 5.864   2.743   0.40 11.43 ?  48  GLY   A O    1 
ATOM   1181 H H    A GLY   A 1 48  ? 17.896 7.200   -0.583  0.60 14.45 ?  48  GLY   A H    1 
ATOM   1182 H H    B GLY   A 1 48  ? 17.833 7.360   -0.047  0.40 14.21 ?  48  GLY   A H    1 
ATOM   1183 H HA2  A GLY   A 1 48  ? 17.199 5.257   -0.033  0.60 14.44 ?  48  GLY   A HA2  1 
ATOM   1184 H HA2  B GLY   A 1 48  ? 17.019 5.460   0.521   0.40 14.03 ?  48  GLY   A HA2  1 
ATOM   1185 H HA3  A GLY   A 1 48  ? 18.579 4.697   -0.551  0.60 14.44 ?  48  GLY   A HA3  1 
ATOM   1186 H HA3  B GLY   A 1 48  ? 18.266 4.806   -0.185  0.40 14.03 ?  48  GLY   A HA3  1 
ATOM   1187 N N    A VAL   A 1 49  ? 18.779 3.791   1.744   0.60 11.67 ?  49  VAL   A N    1 
ATOM   1188 N N    B VAL   A 1 49  ? 18.906 3.766   1.925   0.40 11.05 ?  49  VAL   A N    1 
ATOM   1189 C CA   A VAL   A 1 49  ? 19.262 3.383   3.058   0.60 11.66 ?  49  VAL   A CA   1 
ATOM   1190 C CA   B VAL   A 1 49  ? 19.485 3.237   3.157   0.40 10.95 ?  49  VAL   A CA   1 
ATOM   1191 C C    A VAL   A 1 49  ? 20.574 4.080   3.389   0.60 10.76 ?  49  VAL   A C    1 
ATOM   1192 C C    B VAL   A 1 49  ? 20.760 3.991   3.516   0.40 10.16 ?  49  VAL   A C    1 
ATOM   1193 O O    A VAL   A 1 49  ? 20.776 4.530   4.520   0.60 10.87 ?  49  VAL   A O    1 
ATOM   1194 O O    B VAL   A 1 49  ? 20.961 4.380   4.672   0.40 10.24 ?  49  VAL   A O    1 
ATOM   1195 C CB   A VAL   A 1 49  ? 19.401 1.847   3.119   0.60 12.42 ?  49  VAL   A CB   1 
ATOM   1196 C CB   B VAL   A 1 49  ? 19.754 1.727   3.018   0.40 10.73 ?  49  VAL   A CB   1 
ATOM   1197 C CG1  A VAL   A 1 49  ? 20.170 1.418   4.366   0.60 12.49 ?  49  VAL   A CG1  1 
ATOM   1198 C CG1  B VAL   A 1 49  ? 20.603 1.242   4.185   0.40 10.57 ?  49  VAL   A CG1  1 
ATOM   1199 C CG2  A VAL   A 1 49  ? 18.031 1.195   3.094   0.60 13.90 ?  49  VAL   A CG2  1 
ATOM   1200 C CG2  B VAL   A 1 49  ? 18.449 0.945   2.924   0.40 11.60 ?  49  VAL   A CG2  1 
ATOM   1201 H H    A VAL   A 1 49  ? 18.637 3.139   1.206   0.60 14.00 ?  49  VAL   A H    1 
ATOM   1202 H H    B VAL   A 1 49  ? 18.814 3.183   1.302   0.40 13.26 ?  49  VAL   A H    1 
ATOM   1203 H HA   A VAL   A 1 49  ? 18.615 3.641   3.732   0.60 13.99 ?  49  VAL   A HA   1 
ATOM   1204 H HA   B VAL   A 1 49  ? 18.856 3.358   3.885   0.40 13.13 ?  49  VAL   A HA   1 
ATOM   1205 H HB   A VAL   A 1 49  ? 19.900 1.540   2.344   0.60 14.89 ?  49  VAL   A HB   1 
ATOM   1206 H HB   B VAL   A 1 49  ? 20.255 1.569   2.203   0.40 12.87 ?  49  VAL   A HB   1 
ATOM   1207 H HG11 A VAL   A 1 49  ? 20.008 0.475   4.526   0.60 14.98 ?  49  VAL   A HG11 1 
ATOM   1208 H HG11 B VAL   A 1 49  ? 20.504 0.283   4.272   0.40 12.68 ?  49  VAL   A HG11 1 
ATOM   1209 H HG12 A VAL   A 1 49  ? 21.118 1.570   4.228   0.60 14.98 ?  49  VAL   A HG12 1 
ATOM   1210 H HG12 B VAL   A 1 49  ? 21.534 1.461   4.016   0.40 12.68 ?  49  VAL   A HG12 1 
ATOM   1211 H HG13 A VAL   A 1 49  ? 19.856 1.938   5.123   0.60 14.98 ?  49  VAL   A HG13 1 
ATOM   1212 H HG13 B VAL   A 1 49  ? 20.301 1.677   4.998   0.40 12.68 ?  49  VAL   A HG13 1 
ATOM   1213 H HG21 A VAL   A 1 49  ? 18.141 0.233   3.127   0.60 16.67 ?  49  VAL   A HG21 1 
ATOM   1214 H HG21 B VAL   A 1 49  ? 18.650 0.004   2.813   0.40 13.91 ?  49  VAL   A HG21 1 
ATOM   1215 H HG22 A VAL   A 1 49  ? 17.528 1.500   3.864   0.60 16.67 ?  49  VAL   A HG22 1 
ATOM   1216 H HG22 B VAL   A 1 49  ? 17.940 1.082   3.739   0.40 13.91 ?  49  VAL   A HG22 1 
ATOM   1217 H HG23 A VAL   A 1 49  ? 17.581 1.453   2.277   0.60 16.67 ?  49  VAL   A HG23 1 
ATOM   1218 H HG23 B VAL   A 1 49  ? 17.944 1.268   2.161   0.40 13.91 ?  49  VAL   A HG23 1 
ATOM   1219 N N    A ALA   A 1 50  ? 21.497 4.142   2.424   0.60 10.21 ?  50  ALA   A N    1 
ATOM   1220 N N    B ALA   A 1 50  ? 21.662 4.158   2.545   0.40 9.91  ?  50  ALA   A N    1 
ATOM   1221 C CA   A ALA   A 1 50  ? 22.825 4.684   2.693   0.60 10.10 ?  50  ALA   A CA   1 
ATOM   1222 C CA   B ALA   A 1 50  ? 22.960 4.756   2.843   0.40 10.11 ?  50  ALA   A CA   1 
ATOM   1223 C C    A ALA   A 1 50  ? 22.745 6.134   3.143   0.60 10.24 ?  50  ALA   A C    1 
ATOM   1224 C C    B ALA   A 1 50  ? 22.813 6.215   3.243   0.40 10.03 ?  50  ALA   A C    1 
ATOM   1225 O O    A ALA   A 1 50  ? 23.392 6.530   4.118   0.60 10.40 ?  50  ALA   A O    1 
ATOM   1226 O O    B ALA   A 1 50  ? 23.408 6.663   4.231   0.40 9.97  ?  50  ALA   A O    1 
ATOM   1227 C CB   A ALA   A 1 50  ? 23.695 4.571   1.443   0.60 9.87  ?  50  ALA   A CB   1 
ATOM   1228 C CB   B ALA   A 1 50  ? 23.891 4.626   1.639   0.40 9.99  ?  50  ALA   A CB   1 
ATOM   1229 H H    A ALA   A 1 50  ? 21.380 3.872   1.617   0.60 12.24 ?  50  ALA   A H    1 
ATOM   1230 H H    B ALA   A 1 50  ? 21.547 3.931   1.722   0.40 11.89 ?  50  ALA   A H    1 
ATOM   1231 H HA   A ALA   A 1 50  ? 23.246 4.178   3.405   0.60 12.11 ?  50  ALA   A HA   1 
ATOM   1232 H HA   B ALA   A 1 50  ? 23.362 4.286   3.585   0.40 12.13 ?  50  ALA   A HA   1 
ATOM   1233 H HB1  A ALA   A 1 50  ? 24.572 4.941   1.634   0.60 11.84 ?  50  ALA   A HB1  1 
ATOM   1234 H HB1  B ALA   A 1 50  ? 24.748 5.027   1.860   0.40 11.98 ?  50  ALA   A HB1  1 
ATOM   1235 H HB2  A ALA   A 1 50  ? 23.774 3.639   1.196   0.60 11.84 ?  50  ALA   A HB2  1 
ATOM   1236 H HB2  B ALA   A 1 50  ? 24.008 3.689   1.428   0.40 11.98 ?  50  ALA   A HB2  1 
ATOM   1237 H HB3  A ALA   A 1 50  ? 23.277 5.073   0.724   0.60 11.84 ?  50  ALA   A HB3  1 
ATOM   1238 H HB3  B ALA   A 1 50  ? 23.498 5.091   0.882   0.40 11.98 ?  50  ALA   A HB3  1 
ATOM   1239 N N    A GLY   A 1 51  ? 21.956 6.945   2.439   0.60 10.42 ?  51  GLY   A N    1 
ATOM   1240 N N    B GLY   A 1 51  ? 22.024 6.977   2.485   0.40 10.38 ?  51  GLY   A N    1 
ATOM   1241 C CA   A GLY   A 1 51  ? 21.818 8.335   2.834   0.60 10.87 ?  51  GLY   A CA   1 
ATOM   1242 C CA   B GLY   A 1 51  ? 21.808 8.367   2.840   0.40 10.86 ?  51  GLY   A CA   1 
ATOM   1243 C C    A GLY   A 1 51  ? 21.223 8.477   4.221   0.60 10.97 ?  51  GLY   A C    1 
ATOM   1244 C C    B GLY   A 1 51  ? 21.187 8.512   4.213   0.40 11.07 ?  51  GLY   A C    1 
ATOM   1245 O O    A GLY   A 1 51  ? 21.630 9.347   4.998   0.60 11.66 ?  51  GLY   A O    1 
ATOM   1246 O O    B GLY   A 1 51  ? 21.543 9.416   4.975   0.40 11.46 ?  51  GLY   A O    1 
ATOM   1247 H H    A GLY   A 1 51  ? 21.500 6.717   1.744   0.60 12.50 ?  51  GLY   A H    1 
ATOM   1248 H H    B GLY   A 1 51  ? 21.611 6.716   1.775   0.40 12.45 ?  51  GLY   A H    1 
ATOM   1249 H HA2  A GLY   A 1 51  ? 22.684 8.763   2.826   0.60 13.04 ?  51  GLY   A HA2  1 
ATOM   1250 H HA2  B GLY   A 1 51  ? 22.652 8.838   2.833   0.40 13.03 ?  51  GLY   A HA2  1 
ATOM   1251 H HA3  A GLY   A 1 51  ? 21.238 8.795   2.202   0.60 13.04 ?  51  GLY   A HA3  1 
ATOM   1252 H HA3  B GLY   A 1 51  ? 21.214 8.780   2.193   0.40 13.03 ?  51  GLY   A HA3  1 
ATOM   1253 N N    . ALA   A 1 52  ? 20.250 7.622   4.549   1.00 11.16 ?  52  ALA   A N    1 
ATOM   1254 C CA   . ALA   A 1 52  ? 19.604 7.686   5.855   1.00 11.77 ?  52  ALA   A CA   1 
ATOM   1255 C C    . ALA   A 1 52  ? 20.556 7.266   6.974   1.00 11.09 ?  52  ALA   A C    1 
ATOM   1256 O O    . ALA   A 1 52  ? 20.626 7.923   8.017   1.00 12.22 ?  52  ALA   A O    1 
ATOM   1257 C CB   . ALA   A 1 52  ? 18.335 6.828   5.853   1.00 13.09 ?  52  ALA   A CB   1 
ATOM   1258 H H    A ALA   A 1 52  ? 19.956 6.991   4.038   0.60 13.39 ?  52  ALA   A H    1 
ATOM   1259 H H    B ALA   A 1 52  ? 19.980 6.974   4.046   0.40 13.39 ?  52  ALA   A H    1 
ATOM   1260 H HA   . ALA   A 1 52  ? 19.336 8.595   6.024   1.00 14.12 ?  52  ALA   A HA   1 
ATOM   1261 H HB1  . ALA   A 1 52  ? 17.906 6.887   6.726   1.00 15.70 ?  52  ALA   A HB1  1 
ATOM   1262 H HB2  . ALA   A 1 52  ? 17.726 7.158   5.171   1.00 15.70 ?  52  ALA   A HB2  1 
ATOM   1263 H HB3  . ALA   A 1 52  ? 18.566 5.904   5.667   1.00 15.70 ?  52  ALA   A HB3  1 
ATOM   1264 N N    A LEU   A 1 53  ? 21.299 6.175   6.786   0.60 10.64 ?  53  LEU   A N    1 
ATOM   1265 N N    B LEU   A 1 53  ? 21.273 6.151   6.785   0.40 11.00 ?  53  LEU   A N    1 
ATOM   1266 C CA   A LEU   A 1 53  ? 22.269 5.782   7.806   0.60 10.71 ?  53  LEU   A CA   1 
ATOM   1267 C CA   B LEU   A 1 53  ? 22.242 5.711   7.787   0.40 11.18 ?  53  LEU   A CA   1 
ATOM   1268 C C    A LEU   A 1 53  ? 23.319 6.868   7.991   0.60 9.98  ?  53  LEU   A C    1 
ATOM   1269 C C    B LEU   A 1 53  ? 23.289 6.784   8.018   0.40 11.26 ?  53  LEU   A C    1 
ATOM   1270 O O    A LEU   A 1 53  ? 23.622 7.272   9.117   0.60 10.90 ?  53  LEU   A O    1 
ATOM   1271 O O    B LEU   A 1 53  ? 23.642 7.090   9.161   0.40 12.12 ?  53  LEU   A O    1 
ATOM   1272 C CB   A LEU   A 1 53  ? 22.920 4.441   7.452   0.60 11.30 ?  53  LEU   A CB   1 
ATOM   1273 C CB   B LEU   A 1 53  ? 22.930 4.416   7.336   0.40 11.12 ?  53  LEU   A CB   1 
ATOM   1274 C CG   A LEU   A 1 53  ? 21.973 3.232   7.459   0.60 11.89 ?  53  LEU   A CG   1 
ATOM   1275 C CG   B LEU   A 1 53  ? 22.231 3.062   7.487   0.40 10.61 ?  53  LEU   A CG   1 
ATOM   1276 C CD1  A LEU   A 1 53  ? 22.668 2.006   6.888   0.60 12.27 ?  53  LEU   A CD1  1 
ATOM   1277 C CD1  B LEU   A 1 53  ? 23.104 1.979   6.859   0.40 10.80 ?  53  LEU   A CD1  1 
ATOM   1278 C CD2  A LEU   A 1 53  ? 21.461 2.945   8.859   0.60 13.03 ?  53  LEU   A CD2  1 
ATOM   1279 C CD2  B LEU   A 1 53  ? 21.945 2.733   8.945   0.40 10.18 ?  53  LEU   A CD2  1 
ATOM   1280 H H    A LEU   A 1 53  ? 21.253 5.653   6.098   0.60 12.76 ?  53  LEU   A H    1 
ATOM   1281 H H    B LEU   A 1 53  ? 21.226 5.646   6.090   0.40 13.19 ?  53  LEU   A H    1 
ATOM   1282 H HA   A LEU   A 1 53  ? 21.803 5.673   8.646   0.60 12.84 ?  53  LEU   A HA   1 
ATOM   1283 H HA   B LEU   A 1 53  ? 21.792 5.539   8.626   0.40 13.41 ?  53  LEU   A HA   1 
ATOM   1284 H HB2  A LEU   A 1 53  ? 23.302 4.508   6.561   0.60 13.56 ?  53  LEU   A HB2  1 
ATOM   1285 H HB2  B LEU   A 1 53  ? 23.130 4.508   6.392   0.40 13.34 ?  53  LEU   A HB2  1 
ATOM   1286 H HB3  A LEU   A 1 53  ? 23.624 4.263   8.094   0.60 13.56 ?  53  LEU   A HB3  1 
ATOM   1287 H HB3  B LEU   A 1 53  ? 23.762 4.340   7.824   0.40 13.34 ?  53  LEU   A HB3  1 
ATOM   1288 H HG   A LEU   A 1 53  ? 21.208 3.431   6.893   0.60 14.26 ?  53  LEU   A HG   1 
ATOM   1289 H HG   B LEU   A 1 53  ? 21.389 3.077   7.006   0.40 12.72 ?  53  LEU   A HG   1 
ATOM   1290 H HD11 A LEU   A 1 53  ? 22.048 1.260   6.903   0.60 14.72 ?  53  LEU   A HD11 1 
ATOM   1291 H HD11 B LEU   A 1 53  ? 22.663 1.120   6.957   0.40 12.95 ?  53  LEU   A HD11 1 
ATOM   1292 H HD12 A LEU   A 1 53  ? 22.942 2.193   5.977   0.60 14.72 ?  53  LEU   A HD12 1 
ATOM   1293 H HD12 B LEU   A 1 53  ? 23.229 2.180   5.917   0.40 12.95 ?  53  LEU   A HD12 1 
ATOM   1294 H HD13 A LEU   A 1 53  ? 23.443 1.804   7.434   0.60 14.72 ?  53  LEU   A HD13 1 
ATOM   1295 H HD13 B LEU   A 1 53  ? 23.962 1.964   7.311   0.40 12.95 ?  53  LEU   A HD13 1 
ATOM   1296 H HD21 A LEU   A 1 53  ? 20.946 2.125   8.843   0.60 15.63 ?  53  LEU   A HD21 1 
ATOM   1297 H HD21 B LEU   A 1 53  ? 21.536 1.855   8.999   0.40 12.21 ?  53  LEU   A HD21 1 
ATOM   1298 H HD22 A LEU   A 1 53  ? 22.217 2.853   9.457   0.60 15.63 ?  53  LEU   A HD22 1 
ATOM   1299 H HD22 B LEU   A 1 53  ? 22.779 2.740   9.439   0.40 12.21 ?  53  LEU   A HD22 1 
ATOM   1300 H HD23 A LEU   A 1 53  ? 20.899 3.682   9.148   0.60 15.63 ?  53  LEU   A HD23 1 
ATOM   1301 H HD23 B LEU   A 1 53  ? 21.341 3.402   9.304   0.40 12.21 ?  53  LEU   A HD23 1 
ATOM   1302 N N    A ASN   A 1 54  ? 23.866 7.373   6.889   0.60 10.02 ?  54  ASN   A N    1 
ATOM   1303 N N    B ASN   A 1 54  ? 23.792 7.374   6.938   0.40 10.95 ?  54  ASN   A N    1 
ATOM   1304 C CA   A ASN   A 1 54  ? 24.900 8.389   7.015   0.60 10.21 ?  54  ASN   A CA   1 
ATOM   1305 C CA   B ASN   A 1 54  ? 24.866 8.342   7.083   0.40 10.73 ?  54  ASN   A CA   1 
ATOM   1306 C C    A ASN   A 1 54  ? 24.376 9.616   7.754   0.60 10.82 ?  54  ASN   A C    1 
ATOM   1307 C C    B ASN   A 1 54  ? 24.372 9.615   7.762   0.40 11.00 ?  54  ASN   A C    1 
ATOM   1308 O O    A ASN   A 1 54  ? 25.052 10.155  8.640   0.60 11.42 ?  54  ASN   A O    1 
ATOM   1309 O O    B ASN   A 1 54  ? 25.076 10.194  8.597   0.40 11.37 ?  54  ASN   A O    1 
ATOM   1310 C CB   A ASN   A 1 54  ? 25.437 8.786   5.649   0.60 10.40 ?  54  ASN   A CB   1 
ATOM   1311 C CB   B ASN   A 1 54  ? 25.470 8.656   5.723   0.40 10.72 ?  54  ASN   A CB   1 
ATOM   1312 C CG   A ASN   A 1 54  ? 26.425 9.921   5.756   0.60 10.56 ?  54  ASN   A CG   1 
ATOM   1313 C CG   B ASN   A 1 54  ? 26.537 9.716   5.816   0.40 10.55 ?  54  ASN   A CG   1 
ATOM   1314 O OD1  A ASN   A 1 54  ? 27.452 9.790   6.426   0.60 10.92 ?  54  ASN   A OD1  1 
ATOM   1315 O OD1  B ASN   A 1 54  ? 27.519 9.558   6.543   0.40 10.39 ?  54  ASN   A OD1  1 
ATOM   1316 N ND2  A ASN   A 1 54  ? 26.119 11.049  5.134   0.60 11.19 ?  54  ASN   A ND2  1 
ATOM   1317 N ND2  B ASN   A 1 54  ? 26.352 10.808  5.097   0.40 10.58 ?  54  ASN   A ND2  1 
ATOM   1318 H H    A ASN   A 1 54  ? 23.659 7.155   6.084   0.60 12.02 ?  54  ASN   A H    1 
ATOM   1319 H H    B ASN   A 1 54  ? 23.525 7.237   6.131   0.40 13.14 ?  54  ASN   A H    1 
ATOM   1320 H HA   A ASN   A 1 54  ? 25.632 8.027   7.531   0.60 12.24 ?  54  ASN   A HA   1 
ATOM   1321 H HA   B ASN   A 1 54  ? 25.562 7.957   7.635   0.40 12.87 ?  54  ASN   A HA   1 
ATOM   1322 H HB2  A ASN   A 1 54  ? 25.889 8.021   5.251   0.60 12.47 ?  54  ASN   A HB2  1 
ATOM   1323 H HB2  B ASN   A 1 54  ? 25.868 7.846   5.359   0.40 12.85 ?  54  ASN   A HB2  1 
ATOM   1324 H HB3  A ASN   A 1 54  ? 24.706 9.072   5.083   0.60 12.47 ?  54  ASN   A HB3  1 
ATOM   1325 H HB3  B ASN   A 1 54  ? 24.771 8.975   5.130   0.40 12.85 ?  54  ASN   A HB3  1 
ATOM   1326 H HD21 A ASN   A 1 54  ? 26.654 11.720  5.177   0.60 13.42 ?  54  ASN   A HD21 1 
ATOM   1327 H HD21 B ASN   A 1 54  ? 26.935 11.434  5.123   0.40 12.68 ?  54  ASN   A HD21 1 
ATOM   1328 H HD22 A ASN   A 1 54  ? 25.390 11.104  4.684   0.60 13.42 ?  54  ASN   A HD22 1 
ATOM   1329 H HD22 B ASN   A 1 54  ? 25.652 10.884  4.604   0.40 12.68 ?  54  ASN   A HD22 1 
ATOM   1330 N N    . LYS   A 1 55  ? 23.162 10.064  7.415   1.00 11.38 ?  55  LYS   A N    1 
ATOM   1331 C CA   . LYS   A 1 55  ? 22.585 11.228  8.082   1.00 12.09 ?  55  LYS   A CA   1 
ATOM   1332 C C    . LYS   A 1 55  ? 22.489 10.997  9.583   1.00 11.94 ?  55  LYS   A C    1 
ATOM   1333 O O    . LYS   A 1 55  ? 22.780 11.895  10.382  1.00 12.95 ?  55  LYS   A O    1 
ATOM   1334 C CB   . LYS   A 1 55  ? 21.212 11.531  7.477   1.00 13.06 ?  55  LYS   A CB   1 
ATOM   1335 C CG   . LYS   A 1 55  ? 20.469 12.702  8.096   1.00 15.03 ?  55  LYS   A CG   1 
ATOM   1336 C CD   . LYS   A 1 55  ? 19.149 12.942  7.354   1.00 16.71 ?  55  LYS   A CD   1 
ATOM   1337 C CE   . LYS   A 1 55  ? 18.290 13.998  8.028   1.00 19.09 ?  55  LYS   A CE   1 
ATOM   1338 N NZ   . LYS   A 1 55  ? 16.967 14.151  7.358   1.00 19.76 ?  55  LYS   A NZ   1 
ATOM   1339 H H    A LYS   A 1 55  ? 22.653 9.706   6.819   0.60 13.65 ?  55  LYS   A H    1 
ATOM   1340 H H    B LYS   A 1 55  ? 22.663 9.720   6.803   0.40 13.65 ?  55  LYS   A H    1 
ATOM   1341 H HA   . LYS   A 1 55  ? 23.156 11.997  7.933   1.00 14.50 ?  55  LYS   A HA   1 
ATOM   1342 H HB2  . LYS   A 1 55  ? 21.327 11.728  6.535   1.00 15.66 ?  55  LYS   A HB2  1 
ATOM   1343 H HB3  . LYS   A 1 55  ? 20.650 10.746  7.578   1.00 15.66 ?  55  LYS   A HB3  1 
ATOM   1344 H HG2  . LYS   A 1 55  ? 20.262 12.505  9.024   1.00 18.02 ?  55  LYS   A HG2  1 
ATOM   1345 H HG3  . LYS   A 1 55  ? 21.008 13.504  8.031   1.00 18.02 ?  55  LYS   A HG3  1 
ATOM   1346 H HD2  . LYS   A 1 55  ? 19.348 13.241  6.451   1.00 20.04 ?  55  LYS   A HD2  1 
ATOM   1347 H HD3  . LYS   A 1 55  ? 18.648 12.112  7.325   1.00 20.04 ?  55  LYS   A HD3  1 
ATOM   1348 H HE2  . LYS   A 1 55  ? 18.135 13.741  8.950   1.00 22.90 ?  55  LYS   A HE2  1 
ATOM   1349 H HE3  . LYS   A 1 55  ? 18.748 14.852  7.992   1.00 22.90 ?  55  LYS   A HE3  1 
ATOM   1350 H HZ1  . LYS   A 1 55  ? 16.419 14.638  7.868   1.00 23.70 ?  55  LYS   A HZ1  1 
ATOM   1351 H HZ2  . LYS   A 1 55  ? 17.063 14.560  6.573   1.00 23.70 ?  55  LYS   A HZ2  1 
ATOM   1352 H HZ3  . LYS   A 1 55  ? 16.594 13.353  7.224   1.00 23.70 ?  55  LYS   A HZ3  1 
ATOM   1353 N N    . ALA   A 1 56  ? 22.095 9.787   9.987   1.00 12.45 ?  56  ALA   A N    1 
ATOM   1354 C CA   . ALA   A 1 56  ? 21.972 9.467   11.401  1.00 13.03 ?  56  ALA   A CA   1 
ATOM   1355 C C    . ALA   A 1 56  ? 23.310 9.489   12.125  1.00 13.00 ?  56  ALA   A C    1 
ATOM   1356 O O    . ALA   A 1 56  ? 23.328 9.667   13.343  1.00 14.21 ?  56  ALA   A O    1 
ATOM   1357 C CB   . ALA   A 1 56  ? 21.279 8.112   11.585  1.00 14.01 ?  56  ALA   A CB   1 
ATOM   1358 H H    . ALA   A 1 56  ? 21.894 9.142   9.458   1.00 14.93 ?  56  ALA   A H    1 
ATOM   1359 H HA   . ALA   A 1 56  ? 21.412 10.129  11.822  1.00 15.63 ?  56  ALA   A HA   1 
ATOM   1360 H HB1  . ALA   A 1 56  ? 21.205 7.919   12.536  1.00 16.81 ?  56  ALA   A HB1  1 
ATOM   1361 H HB2  . ALA   A 1 56  ? 20.392 8.156   11.193  1.00 16.81 ?  56  ALA   A HB2  1 
ATOM   1362 H HB3  . ALA   A 1 56  ? 21.799 7.421   11.149  1.00 16.81 ?  56  ALA   A HB3  1 
ATOM   1363 N N    . THR   A 1 57  ? 24.425 9.298   11.413  1.00 12.15 ?  57  THR   A N    1 
ATOM   1364 C CA   . THR   A 1 57  ? 25.766 9.428   11.992  1.00 12.17 ?  57  THR   A CA   1 
ATOM   1365 C C    . THR   A 1 57  ? 26.318 10.847  11.912  1.00 12.45 ?  57  THR   A C    1 
ATOM   1366 O O    . THR   A 1 57  ? 27.504 11.053  12.201  1.00 13.11 ?  57  THR   A O    1 
ATOM   1367 C CB   . THR   A 1 57  ? 26.782 8.478   11.328  1.00 11.51 ?  57  THR   A CB   1 
ATOM   1368 O OG1  . THR   A 1 57  ? 27.158 8.970   10.031  1.00 11.80 ?  57  THR   A OG1  1 
ATOM   1369 C CG2  . THR   A 1 57  ? 26.251 7.054   11.215  1.00 11.99 ?  57  THR   A CG2  1 
ATOM   1370 H H    . THR   A 1 57  ? 24.431 9.062   10.585  1.00 14.57 ?  57  THR   A H    1 
ATOM   1371 H HA   . THR   A 1 57  ? 25.721 9.174   12.931  1.00 14.60 ?  57  THR   A HA   1 
ATOM   1372 H HB   . THR   A 1 57  ? 27.581 8.438   11.884  1.00 13.80 ?  57  THR   A HB   1 
ATOM   1373 H HG1  . THR   A 1 57  ? 26.481 9.031   9.541   1.00 14.16 ?  57  THR   A HG1  1 
ATOM   1374 H HG21 . THR   A 1 57  ? 26.906 6.478   10.783  1.00 14.38 ?  57  THR   A HG21 1 
ATOM   1375 H HG22 . THR   A 1 57  ? 26.056 6.693   12.096  1.00 14.38 ?  57  THR   A HG22 1 
ATOM   1376 H HG23 . THR   A 1 57  ? 25.436 7.038   10.689  1.00 14.38 ?  57  THR   A HG23 1 
ATOM   1377 N N    . ASN   A 1 58  ? 25.507 11.821  11.506  1.00 13.16 ?  58  ASN   A N    1 
ATOM   1378 C CA   . ASN   A 1 58  ? 25.970 13.203  11.412  1.00 14.10 ?  58  ASN   A CA   1 
ATOM   1379 C C    . ASN   A 1 58  ? 27.120 13.331  10.409  1.00 13.09 ?  58  ASN   A C    1 
ATOM   1380 O O    . ASN   A 1 58  ? 28.018 14.164  10.567  1.00 13.65 ?  58  ASN   A O    1 
ATOM   1381 C CB   . ASN   A 1 58  ? 26.345 13.738  12.807  1.00 17.20 ?  58  ASN   A CB   1 
ATOM   1382 C CG   . ASN   A 1 58  ? 26.753 15.194  12.804  1.00 21.22 ?  58  ASN   A CG   1 
ATOM   1383 O OD1  . ASN   A 1 58  ? 26.122 16.016  12.152  1.00 22.82 ?  58  ASN   A OD1  1 
ATOM   1384 N ND2  . ASN   A 1 58  ? 27.810 15.523  13.553  1.00 22.47 ?  58  ASN   A ND2  1 
ATOM   1385 H H    . ASN   A 1 58  ? 24.685 11.700  11.270  1.00 15.79 ?  58  ASN   A H    1 
ATOM   1386 H HA   . ASN   A 1 58  ? 25.237 13.740  11.085  1.00 16.92 ?  58  ASN   A HA   1 
ATOM   1387 H HB2  . ASN   A 1 58  ? 25.574 13.643  13.399  1.00 20.63 ?  58  ASN   A HB2  1 
ATOM   1388 H HB3  . ASN   A 1 58  ? 27.087 13.231  13.160  1.00 20.63 ?  58  ASN   A HB3  1 
ATOM   1389 H HD21 . ASN   A 1 58  ? 28.075 16.344  13.591  1.00 26.95 ?  58  ASN   A HD21 1 
ATOM   1390 H HD22 . ASN   A 1 58  ? 28.222 14.919  13.998  1.00 26.95 ?  58  ASN   A HD22 1 
ATOM   1391 N N    . ASN   A 1 59  ? 27.094 12.514  9.353   1.00 12.04 ?  59  ASN   A N    1 
ATOM   1392 C CA   . ASN   A 1 59  ? 28.079 12.484  8.262   1.00 11.77 ?  59  ASN   A CA   1 
ATOM   1393 C C    . ASN   A 1 59  ? 29.391 11.798  8.653   1.00 11.40 ?  59  ASN   A C    1 
ATOM   1394 O O    . ASN   A 1 59  ? 30.310 11.756  7.831   1.00 11.46 ?  59  ASN   A O    1 
ATOM   1395 C CB   . ASN   A 1 59  ? 28.379 13.870  7.658   1.00 11.73 ?  59  ASN   A CB   1 
ATOM   1396 C CG   . ASN   A 1 59  ? 28.733 13.801  6.187   1.00 12.19 ?  59  ASN   A CG   1 
ATOM   1397 O OD1  . ASN   A 1 59  ? 28.024 13.178  5.395   1.00 12.51 ?  59  ASN   A OD1  1 
ATOM   1398 N ND2  . ASN   A 1 59  ? 29.830 14.456  5.807   1.00 12.88 ?  59  ASN   A ND2  1 
ATOM   1399 H H    . ASN   A 1 59  ? 26.472 11.930  9.235   1.00 14.44 ?  59  ASN   A H    1 
ATOM   1400 H HA   . ASN   A 1 59  ? 27.699 11.959  7.548   1.00 14.12 ?  59  ASN   A HA   1 
ATOM   1401 H HB2  . ASN   A 1 59  ? 27.599 14.438  7.744   1.00 14.07 ?  59  ASN   A HB2  1 
ATOM   1402 H HB3  . ASN   A 1 59  ? 29.134 14.270  8.121   1.00 14.07 ?  59  ASN   A HB3  1 
ATOM   1403 H HD21 . ASN   A 1 59  ? 30.075 14.446  4.980   1.00 15.45 ?  59  ASN   A HD21 1 
ATOM   1404 H HD22 . ASN   A 1 59  ? 30.305 14.881  6.386   1.00 15.45 ?  59  ASN   A HD22 1 
ATOM   1405 N N    . ALA   A 1 60  ? 29.514 11.255  9.862   1.00 11.45 ?  60  ALA   A N    1 
ATOM   1406 C CA   . ALA   A 1 60  ? 30.752 10.570  10.218  1.00 11.44 ?  60  ALA   A CA   1 
ATOM   1407 C C    . ALA   A 1 60  ? 30.977 9.332   9.353   1.00 11.53 ?  60  ALA   A C    1 
ATOM   1408 O O    . ALA   A 1 60  ? 32.121 9.009   9.021   1.00 12.05 ?  60  ALA   A O    1 
ATOM   1409 C CB   . ALA   A 1 60  ? 30.742 10.214  11.701  1.00 12.29 ?  60  ALA   A CB   1 
ATOM   1410 H H    . ALA   A 1 60  ? 28.915 11.265  10.476  1.00 13.74 ?  60  ALA   A H    1 
ATOM   1411 H HA   . ALA   A 1 60  ? 31.497 11.176  10.063  1.00 13.72 ?  60  ALA   A HA   1 
ATOM   1412 H HB1  . ALA   A 1 60  ? 31.569 9.766   11.926  1.00 14.74 ?  60  ALA   A HB1  1 
ATOM   1413 H HB2  . ALA   A 1 60  ? 30.660 11.036  12.219  1.00 14.74 ?  60  ALA   A HB2  1 
ATOM   1414 H HB3  . ALA   A 1 60  ? 29.986 9.637   11.881  1.00 14.74 ?  60  ALA   A HB3  1 
ATOM   1415 N N    . MET   A 1 61  ? 29.906 8.635   8.971   1.00 11.06 ?  61  MET   A N    1 
ATOM   1416 C CA   . MET   A 1 61  ? 30.044 7.500   8.061   1.00 11.03 ?  61  MET   A CA   1 
ATOM   1417 C C    . MET   A 1 61  ? 30.675 7.929   6.736   1.00 10.89 ?  61  MET   A C    1 
ATOM   1418 O O    . MET   A 1 61  ? 31.571 7.251   6.220   1.00 11.36 ?  61  MET   A O    1 
ATOM   1419 C CB   . MET   A 1 61  ? 28.682 6.840   7.847   1.00 11.06 ?  61  MET   A CB   1 
ATOM   1420 C CG   . MET   A 1 61  ? 28.697 5.678   6.873   1.00 11.70 ?  61  MET   A CG   1 
ATOM   1421 S SD   . MET   A 1 61  ? 27.072 4.934   6.664   1.00 12.54 ?  61  MET   A SD   1 
ATOM   1422 C CE   . MET   A 1 61  ? 26.951 4.034   8.211   1.00 13.69 ?  61  MET   A CE   1 
ATOM   1423 H H    . MET   A 1 61  ? 29.100 8.795   9.221   1.00 13.26 ?  61  MET   A H    1 
ATOM   1424 H HA   . MET   A 1 61  ? 30.622 6.839   8.476   1.00 13.23 ?  61  MET   A HA   1 
ATOM   1425 H HB2  . MET   A 1 61  ? 28.360 6.505   8.698   1.00 13.27 ?  61  MET   A HB2  1 
ATOM   1426 H HB3  . MET   A 1 61  ? 28.060 7.501   7.503   1.00 13.27 ?  61  MET   A HB3  1 
ATOM   1427 H HG2  . MET   A 1 61  ? 28.988 5.984   6.002   1.00 14.03 ?  61  MET   A HG2  1 
ATOM   1428 H HG3  . MET   A 1 61  ? 29.294 4.989   7.203   1.00 14.03 ?  61  MET   A HG3  1 
ATOM   1429 H HE1  . MET   A 1 61  ? 26.115 3.544   8.225   1.00 16.42 ?  61  MET   A HE1  1 
ATOM   1430 H HE2  . MET   A 1 61  ? 27.698 3.419   8.276   1.00 16.42 ?  61  MET   A HE2  1 
ATOM   1431 H HE3  . MET   A 1 61  ? 26.977 4.666   8.948   1.00 16.42 ?  61  MET   A HE3  1 
ATOM   1432 N N    . GLN   A 1 62  ? 30.238 9.064   6.181   1.00 11.08 ?  62  GLN   A N    1 
ATOM   1433 C CA   . GLN   A 1 62  ? 30.802 9.535   4.919   1.00 10.78 ?  62  GLN   A CA   1 
ATOM   1434 C C    . GLN   A 1 62  ? 32.270 9.914   5.069   1.00 11.07 ?  62  GLN   A C    1 
ATOM   1435 O O    . GLN   A 1 62  ? 33.083 9.602   4.193   1.00 11.26 ?  62  GLN   A O    1 
ATOM   1436 C CB   . GLN   A 1 62  ? 30.001 10.718  4.386   1.00 11.31 ?  62  GLN   A CB   1 
ATOM   1437 C CG   . GLN   A 1 62  ? 30.378 11.079  2.964   1.00 10.89 ?  62  GLN   A CG   1 
ATOM   1438 C CD   . GLN   A 1 62  ? 30.052 9.953   2.016   1.00 11.38 ?  62  GLN   A CD   1 
ATOM   1439 O OE1  . GLN   A 1 62  ? 28.872 9.659   1.792   1.00 12.18 ?  62  GLN   A OE1  1 
ATOM   1440 N NE2  . GLN   A 1 62  ? 31.075 9.277   1.497   1.00 11.88 ?  62  GLN   A NE2  1 
ATOM   1441 H H    . GLN   A 1 62  ? 29.616 9.558   6.508   1.00 13.29 ?  62  GLN   A H    1 
ATOM   1442 H HA   . GLN   A 1 62  ? 30.748 8.814   4.271   1.00 12.93 ?  62  GLN   A HA   1 
ATOM   1443 H HB2  . GLN   A 1 62  ? 29.056 10.497  4.400   1.00 13.57 ?  62  GLN   A HB2  1 
ATOM   1444 H HB3  . GLN   A 1 62  ? 30.169 11.493  4.946   1.00 13.57 ?  62  GLN   A HB3  1 
ATOM   1445 H HG2  . GLN   A 1 62  ? 29.875 11.859  2.686   1.00 13.06 ?  62  GLN   A HG2  1 
ATOM   1446 H HG3  . GLN   A 1 62  ? 31.329 11.255  2.914   1.00 13.06 ?  62  GLN   A HG3  1 
ATOM   1447 H HE21 . GLN   A 1 62  ? 31.884 9.502   1.692   1.00 14.25 ?  62  GLN   A HE21 1 
ATOM   1448 H HE22 . GLN   A 1 62  ? 30.932 8.621   0.959   1.00 14.25 ?  62  GLN   A HE22 1 
ATOM   1449 N N    . VAL   A 1 63  ? 32.628 10.600  6.159   1.00 11.33 ?  63  VAL   A N    1 
ATOM   1450 C CA   . VAL   A 1 63  ? 34.021 10.987  6.379   1.00 12.29 ?  63  VAL   A CA   1 
ATOM   1451 C C    . VAL   A 1 63  ? 34.912 9.748   6.435   1.00 11.80 ?  63  VAL   A C    1 
ATOM   1452 O O    . VAL   A 1 63  ? 35.966 9.681   5.787   1.00 12.21 ?  63  VAL   A O    1 
ATOM   1453 C CB   . VAL   A 1 63  ? 34.136 11.852  7.649   1.00 13.94 ?  63  VAL   A CB   1 
ATOM   1454 C CG1  . VAL   A 1 63  ? 35.583 12.106  7.992   1.00 15.55 ?  63  VAL   A CG1  1 
ATOM   1455 C CG2  . VAL   A 1 63  ? 33.401 13.182  7.456   1.00 14.23 ?  63  VAL   A CG2  1 
ATOM   1456 H H    . VAL   A 1 63  ? 32.080 10.854  6.781   1.00 13.59 ?  63  VAL   A H    1 
ATOM   1457 H HA   . VAL   A 1 63  ? 34.310 11.526  5.632   1.00 14.75 ?  63  VAL   A HA   1 
ATOM   1458 H HB   . VAL   A 1 63  ? 33.726 11.383  8.395   1.00 16.72 ?  63  VAL   A HB   1 
ATOM   1459 H HG11 . VAL   A 1 63  ? 35.629 12.839  8.625   1.00 18.66 ?  63  VAL   A HG11 1 
ATOM   1460 H HG12 . VAL   A 1 63  ? 35.963 11.306  8.383   1.00 18.66 ?  63  VAL   A HG12 1 
ATOM   1461 H HG13 . VAL   A 1 63  ? 36.059 12.341  7.180   1.00 18.66 ?  63  VAL   A HG13 1 
ATOM   1462 H HG21 . VAL   A 1 63  ? 33.492 13.711  8.265   1.00 17.07 ?  63  VAL   A HG21 1 
ATOM   1463 H HG22 . VAL   A 1 63  ? 33.791 13.651  6.705   1.00 17.07 ?  63  VAL   A HG22 1 
ATOM   1464 H HG23 . VAL   A 1 63  ? 32.463 13.000  7.285   1.00 17.07 ?  63  VAL   A HG23 1 
ATOM   1465 N N    . GLU   A 1 64  ? 34.493 8.739   7.201   1.00 11.69 ?  64  GLU   A N    1 
ATOM   1466 C CA   . GLU   A 1 64  ? 35.257 7.502   7.295   1.00 11.37 ?  64  GLU   A CA   1 
ATOM   1467 C C    . GLU   A 1 64  ? 35.346 6.815   5.939   1.00 11.30 ?  64  GLU   A C    1 
ATOM   1468 O O    . GLU   A 1 64  ? 36.395 6.270   5.563   1.00 11.92 ?  64  GLU   A O    1 
ATOM   1469 C CB   . GLU   A 1 64  ? 34.571 6.594   8.316   1.00 12.30 ?  64  GLU   A CB   1 
ATOM   1470 C CG   . GLU   A 1 64  ? 35.211 5.236   8.452   1.00 13.11 ?  64  GLU   A CG   1 
ATOM   1471 C CD   . GLU   A 1 64  ? 34.330 4.250   9.191   1.00 13.40 ?  64  GLU   A CD   1 
ATOM   1472 O OE1  . GLU   A 1 64  ? 33.092 4.347   9.061   1.00 14.53 ?  64  GLU   A OE1  1 
ATOM   1473 O OE2  . GLU   A 1 64  ? 34.879 3.361   9.881   1.00 13.69 -1 64  GLU   A OE2  1 
ATOM   1474 H H    . GLU   A 1 64  ? 33.765 8.743   7.664   1.00 14.02 ?  64  GLU   A H    1 
ATOM   1475 H HA   . GLU   A 1 64  ? 36.155 7.703   7.609   1.00 13.64 ?  64  GLU   A HA   1 
ATOM   1476 H HB2  . GLU   A 1 64  ? 34.606 7.027   9.190   1.00 14.75 ?  64  GLU   A HB2  1 
ATOM   1477 H HB3  . GLU   A 1 64  ? 33.647 6.475   8.051   1.00 14.75 ?  64  GLU   A HB3  1 
ATOM   1478 H HG2  . GLU   A 1 64  ? 35.384 4.866   7.567   1.00 15.73 ?  64  GLU   A HG2  1 
ATOM   1479 H HG3  . GLU   A 1 64  ? 36.041 5.323   8.938   1.00 15.73 ?  64  GLU   A HG3  1 
ATOM   1480 N N    . SER   A 1 65  ? 34.228 6.803   5.210   1.00 11.10 ?  65  SER   A N    1 
ATOM   1481 C CA   . SER   A 1 65  ? 34.178 6.152   3.908   1.00 10.94 ?  65  SER   A CA   1 
ATOM   1482 C C    . SER   A 1 65  ? 35.106 6.822   2.903   1.00 11.08 ?  65  SER   A C    1 
ATOM   1483 O O    . SER   A 1 65  ? 35.742 6.144   2.088   1.00 12.14 ?  65  SER   A O    1 
ATOM   1484 C CB   . SER   A 1 65  ? 32.744 6.166   3.377   1.00 11.08 ?  65  SER   A CB   1 
ATOM   1485 O OG   . SER   A 1 65  ? 31.888 5.351   4.167   1.00 11.65 ?  65  SER   A OG   1 
ATOM   1486 H H    . SER   A 1 65  ? 33.492 7.178   5.447   1.00 13.31 ?  65  SER   A H    1 
ATOM   1487 H HA   . SER   A 1 65  ? 34.461 5.231   4.005   1.00 13.12 ?  65  SER   A HA   1 
ATOM   1488 H HB2  . SER   A 1 65  ? 32.411 7.073   3.394   1.00 13.29 ?  65  SER   A HB2  1 
ATOM   1489 H HB3  . SER   A 1 65  ? 32.747 5.827   2.469   1.00 13.29 ?  65  SER   A HB3  1 
ATOM   1490 H HG   . SER   A 1 65  ? 31.886 5.627   4.965   1.00 13.98 ?  65  SER   A HG   1 
ATOM   1491 N N    . ASP   A 1 66  ? 35.174 8.154   2.922   1.00 11.33 ?  66  ASP   A N    1 
ATOM   1492 C CA   . ASP   A 1 66  ? 36.033 8.851   1.972   1.00 12.45 ?  66  ASP   A CA   1 
ATOM   1493 C C    . ASP   A 1 66  ? 37.495 8.497   2.206   1.00 12.17 ?  66  ASP   A C    1 
ATOM   1494 O O    . ASP   A 1 66  ? 38.266 8.321   1.253   1.00 13.03 ?  66  ASP   A O    1 
ATOM   1495 C CB   . ASP   A 1 66  ? 35.819 10.357  2.085   1.00 13.56 ?  66  ASP   A CB   1 
ATOM   1496 C CG   . ASP   A 1 66  ? 34.485 10.821  1.492   1.00 15.52 ?  66  ASP   A CG   1 
ATOM   1497 O OD1  . ASP   A 1 66  ? 33.774 10.026  0.838   1.00 15.74 ?  66  ASP   A OD1  1 
ATOM   1498 O OD2  . ASP   A 1 66  ? 34.177 12.017  1.656   1.00 18.52 -1 66  ASP   A OD2  1 
ATOM   1499 H H    . ASP   A 1 66  ? 34.740 8.669   3.463   1.00 13.60 ?  66  ASP   A H    1 
ATOM   1500 H HA   . ASP   A 1 66  ? 35.792 8.579   1.072   1.00 14.94 ?  66  ASP   A HA   1 
ATOM   1501 H HB2  . ASP   A 1 66  ? 35.836 10.610  3.021   1.00 16.26 ?  66  ASP   A HB2  1 
ATOM   1502 H HB3  . ASP   A 1 66  ? 36.536 10.812  1.609   1.00 16.26 ?  66  ASP   A HB3  1 
ATOM   1503 N N    . ASP   A 1 67  ? 37.890 8.370   3.471   1.00 12.26 ?  67  ASP   A N    1 
ATOM   1504 C CA   . ASP   A 1 67  ? 39.245 7.926   3.771   1.00 12.99 ?  67  ASP   A CA   1 
ATOM   1505 C C    . ASP   A 1 67  ? 39.469 6.491   3.307   1.00 13.11 ?  67  ASP   A C    1 
ATOM   1506 O O    . ASP   A 1 67  ? 40.529 6.168   2.762   1.00 13.74 ?  67  ASP   A O    1 
ATOM   1507 C CB   . ASP   A 1 67  ? 39.510 8.059   5.267   1.00 14.32 ?  67  ASP   A CB   1 
ATOM   1508 C CG   . ASP   A 1 67  ? 40.805 7.398   5.686   1.00 15.71 ?  67  ASP   A CG   1 
ATOM   1509 O OD1  . ASP   A 1 67  ? 41.879 8.027   5.541   1.00 18.42 ?  67  ASP   A OD1  1 
ATOM   1510 O OD2  . ASP   A 1 67  ? 40.749 6.233   6.144   1.00 15.46 -1 67  ASP   A OD2  1 
ATOM   1511 H H    . ASP   A 1 67  ? 37.406 8.536   4.156   1.00 14.70 ?  67  ASP   A H    1 
ATOM   1512 H HA   . ASP   A 1 67  ? 39.877 8.494   3.299   1.00 15.58 ?  67  ASP   A HA   1 
ATOM   1513 H HB2  . ASP   A 1 67  ? 39.567 8.996   5.493   1.00 17.18 ?  67  ASP   A HB2  1 
ATOM   1514 H HB3  . ASP   A 1 67  ? 38.787 7.635   5.752   1.00 17.18 ?  67  ASP   A HB3  1 
ATOM   1515 N N    . TYR   A 1 68  ? 38.479 5.613   3.502   1.00 13.01 ?  68  TYR   A N    1 
ATOM   1516 C CA   . TYR   A 1 68  ? 38.601 4.235   3.028   1.00 12.92 ?  68  TYR   A CA   1 
ATOM   1517 C C    . TYR   A 1 68  ? 38.842 4.191   1.520   1.00 12.63 ?  68  TYR   A C    1 
ATOM   1518 O O    . TYR   A 1 68  ? 39.714 3.454   1.043   1.00 13.24 ?  68  TYR   A O    1 
ATOM   1519 C CB   . TYR   A 1 68  ? 37.350 3.416   3.403   1.00 12.93 ?  68  TYR   A CB   1 
ATOM   1520 C CG   . TYR   A 1 68  ? 37.380 2.031   2.777   1.00 14.72 ?  68  TYR   A CG   1 
ATOM   1521 C CD1  . TYR   A 1 68  ? 36.924 1.833   1.478   1.00 16.17 ?  68  TYR   A CD1  1 
ATOM   1522 C CD2  . TYR   A 1 68  ? 37.926 0.950   3.449   1.00 16.84 ?  68  TYR   A CD2  1 
ATOM   1523 C CE1  . TYR   A 1 68  ? 36.994 0.614   0.869   1.00 17.70 ?  68  TYR   A CE1  1 
ATOM   1524 C CE2  . TYR   A 1 68  ? 37.991 -0.312  2.842   1.00 17.62 ?  68  TYR   A CE2  1 
ATOM   1525 C CZ   . TYR   A 1 68  ? 37.531 -0.456  1.550   1.00 18.11 ?  68  TYR   A CZ   1 
ATOM   1526 O OH   . TYR   A 1 68  ? 37.614 -1.673  0.924   1.00 19.48 ?  68  TYR   A OH   1 
ATOM   1527 H H    . TYR   A 1 68  ? 37.736 5.789   3.898   1.00 15.61 ?  68  TYR   A H    1 
ATOM   1528 H HA   . TYR   A 1 68  ? 39.362 3.821   3.459   1.00 15.50 ?  68  TYR   A HA   1 
ATOM   1529 H HB2  . TYR   A 1 68  ? 37.312 3.311   4.365   1.00 15.51 ?  68  TYR   A HB2  1 
ATOM   1530 H HB3  . TYR   A 1 68  ? 36.556 3.876   3.082   1.00 15.51 ?  68  TYR   A HB3  1 
ATOM   1531 H HD1  . TYR   A 1 68  ? 36.570 2.555   1.007   1.00 19.40 ?  68  TYR   A HD1  1 
ATOM   1532 H HD2  . TYR   A 1 68  ? 38.254 1.061   4.309   1.00 20.20 ?  68  TYR   A HD2  1 
ATOM   1533 H HE1  . TYR   A 1 68  ? 36.675 0.508   0.002   1.00 21.24 ?  68  TYR   A HE1  1 
ATOM   1534 H HE2  . TYR   A 1 68  ? 38.363 -1.038  3.286   1.00 21.14 ?  68  TYR   A HE2  1 
ATOM   1535 H HH   . TYR   A 1 68  ? 37.949 -2.239  1.443   1.00 23.37 ?  68  TYR   A HH   1 
ATOM   1536 N N    . ILE   A 1 69  ? 38.054 4.948   0.748   1.00 11.95 ?  69  ILE   A N    1 
ATOM   1537 C CA   . ILE   A 1 69  ? 38.189 4.934   -0.707  1.00 11.89 ?  69  ILE   A CA   1 
ATOM   1538 C C    . ILE   A 1 69  ? 39.518 5.543   -1.135  1.00 12.02 ?  69  ILE   A C    1 
ATOM   1539 O O    . ILE   A 1 69  ? 40.161 5.062   -2.073  1.00 12.67 ?  69  ILE   A O    1 
ATOM   1540 C CB   . ILE   A 1 69  ? 36.989 5.639   -1.370  1.00 12.74 ?  69  ILE   A CB   1 
ATOM   1541 C CG1  . ILE   A 1 69  ? 35.679 4.900   -1.085  1.00 13.57 ?  69  ILE   A CG1  1 
ATOM   1542 C CG2  . ILE   A 1 69  ? 37.212 5.819   -2.881  1.00 14.25 ?  69  ILE   A CG2  1 
ATOM   1543 C CD1  . ILE   A 1 69  ? 35.510 3.620   -1.874  1.00 14.37 ?  69  ILE   A CD1  1 
ATOM   1544 H H    . ILE   A 1 69  ? 37.445 5.476   1.043   1.00 14.33 ?  69  ILE   A H    1 
ATOM   1545 H HA   . ILE   A 1 69  ? 38.187 4.013   -1.007  1.00 14.26 ?  69  ILE   A HA   1 
ATOM   1546 H HB   . ILE   A 1 69  ? 36.912 6.519   -0.981  1.00 15.28 ?  69  ILE   A HB   1 
ATOM   1547 H HG12 . ILE   A 1 69  ? 35.651 4.668   -0.142  1.00 16.27 ?  69  ILE   A HG12 1 
ATOM   1548 H HG13 . ILE   A 1 69  ? 34.937 5.481   -1.301  1.00 16.27 ?  69  ILE   A HG13 1 
ATOM   1549 H HG21 . ILE   A 1 69  ? 36.362 6.035   -3.304  1.00 17.10 ?  69  ILE   A HG21 1 
ATOM   1550 H HG22 . ILE   A 1 69  ? 37.838 6.551   -3.024  1.00 17.10 ?  69  ILE   A HG22 1 
ATOM   1551 H HG23 . ILE   A 1 69  ? 37.566 5.001   -3.255  1.00 17.10 ?  69  ILE   A HG23 1 
ATOM   1552 H HD11 . ILE   A 1 69  ? 34.738 3.144   -1.532  1.00 17.23 ?  69  ILE   A HD11 1 
ATOM   1553 H HD12 . ILE   A 1 69  ? 35.371 3.844   -2.808  1.00 17.23 ?  69  ILE   A HD12 1 
ATOM   1554 H HD13 . ILE   A 1 69  ? 36.305 3.078   -1.775  1.00 17.23 ?  69  ILE   A HD13 1 
ATOM   1555 N N    . ALA   A 1 70  ? 39.932 6.629   -0.486  1.00 12.67 ?  70  ALA   A N    1 
ATOM   1556 C CA   . ALA   A 1 70  ? 41.213 7.235   -0.834  1.00 13.66 ?  70  ALA   A CA   1 
ATOM   1557 C C    . ALA   A 1 70  ? 42.362 6.248   -0.663  1.00 13.98 ?  70  ALA   A C    1 
ATOM   1558 O O    . ALA   A 1 70  ? 43.333 6.288   -1.421  1.00 15.69 ?  70  ALA   A O    1 
ATOM   1559 C CB   . ALA   A 1 70  ? 41.450 8.487   0.012   1.00 14.10 ?  70  ALA   A CB   1 
ATOM   1560 H H    . ALA   A 1 70  ? 39.497 7.030   0.136   1.00 15.19 ?  70  ALA   A H    1 
ATOM   1561 H HA   . ALA   A 1 70  ? 41.189 7.513   -1.767  1.00 16.39 ?  70  ALA   A HA   1 
ATOM   1562 H HB1  . ALA   A 1 70  ? 42.311 8.874   -0.232  1.00 16.91 ?  70  ALA   A HB1  1 
ATOM   1563 H HB2  . ALA   A 1 70  ? 40.744 9.126   -0.155  1.00 16.91 ?  70  ALA   A HB2  1 
ATOM   1564 H HB3  . ALA   A 1 70  ? 41.461 8.236   0.949   1.00 16.91 ?  70  ALA   A HB3  1 
ATOM   1565 N N    . THR   A 1 71  ? 42.262 5.352   0.315   1.00 13.12 ?  71  THR   A N    1 
ATOM   1566 C CA   . THR   A 1 71  ? 43.317 4.378   0.569   1.00 14.93 ?  71  THR   A CA   1 
ATOM   1567 C C    . THR   A 1 71  ? 43.201 3.152   -0.326  1.00 15.07 ?  71  THR   A C    1 
ATOM   1568 O O    . THR   A 1 71  ? 44.215 2.638   -0.816  1.00 17.25 ?  71  THR   A O    1 
ATOM   1569 C CB   . THR   A 1 71  ? 43.250 3.934   2.026   1.00 17.11 ?  71  THR   A CB   1 
ATOM   1570 O OG1  . THR   A 1 71  ? 43.481 5.062   2.878   1.00 18.68 ?  71  THR   A OG1  1 
ATOM   1571 C CG2  . THR   A 1 71  ? 44.274 2.839   2.315   1.00 18.45 ?  71  THR   A CG2  1 
ATOM   1572 H H    . THR   A 1 71  ? 41.586 5.284   0.840   1.00 15.74 ?  71  THR   A H    1 
ATOM   1573 H HA   . THR   A 1 71  ? 44.179 4.788   0.408   1.00 17.91 ?  71  THR   A HA   1 
ATOM   1574 H HB   . THR   A 1 71  ? 42.367 3.565   2.203   1.00 20.52 ?  71  THR   A HB   1 
ATOM   1575 H HG1  . THR   A 1 71  ? 43.443 4.810   3.680   1.00 22.41 ?  71  THR   A HG1  1 
ATOM   1576 H HG21 . THR   A 1 71  ? 44.407 2.758   3.272   1.00 22.14 ?  71  THR   A HG21 1 
ATOM   1577 H HG22 . THR   A 1 71  ? 43.969 1.986   1.967   1.00 22.14 ?  71  THR   A HG22 1 
ATOM   1578 H HG23 . THR   A 1 71  ? 45.124 3.063   1.899   1.00 22.14 ?  71  THR   A HG23 1 
ATOM   1579 N N    . ASN   A 1 72  ? 41.976 2.654   -0.527  1.00 14.18 ?  72  ASN   A N    1 
ATOM   1580 C CA   . ASN   A 1 72  ? 41.757 1.327   -1.087  1.00 14.04 ?  72  ASN   A CA   1 
ATOM   1581 C C    . ASN   A 1 72  ? 41.140 1.314   -2.472  1.00 14.30 ?  72  ASN   A C    1 
ATOM   1582 O O    . ASN   A 1 72  ? 41.147 0.258   -3.117  1.00 15.55 ?  72  ASN   A O    1 
ATOM   1583 C CB   . ASN   A 1 72  ? 40.860 0.514   -0.150  1.00 14.97 ?  72  ASN   A CB   1 
ATOM   1584 C CG   . ASN   A 1 72  ? 41.474 0.348   1.211   1.00 16.23 ?  72  ASN   A CG   1 
ATOM   1585 O OD1  . ASN   A 1 72  ? 41.028 0.941   2.187   1.00 17.93 ?  72  ASN   A OD1  1 
ATOM   1586 N ND2  . ASN   A 1 72  ? 42.527 -0.435  1.277   1.00 16.74 ?  72  ASN   A ND2  1 
ATOM   1587 H H    . ASN   A 1 72  ? 41.244 3.075   -0.347  1.00 17.01 ?  72  ASN   A H    1 
ATOM   1588 H HA   . ASN   A 1 72  ? 42.608 0.873   -1.150  1.00 16.84 ?  72  ASN   A HA   1 
ATOM   1589 H HB2  . ASN   A 1 72  ? 40.010 0.968   -0.048  1.00 17.96 ?  72  ASN   A HB2  1 
ATOM   1590 H HB3  . ASN   A 1 72  ? 40.723 -0.370  -0.531  1.00 17.96 ?  72  ASN   A HB3  1 
ATOM   1591 H HD21 . ASN   A 1 72  ? 42.923 -0.556  2.032   1.00 20.08 ?  72  ASN   A HD21 1 
ATOM   1592 H HD22 . ASN   A 1 72  ? 42.826 -0.819  0.569   1.00 20.08 ?  72  ASN   A HD22 1 
ATOM   1593 N N    . GLY   A 1 73  ? 40.583 2.426   -2.930  1.00 13.76 ?  73  GLY   A N    1 
ATOM   1594 C CA   . GLY   A 1 73  ? 39.854 2.436   -4.171  1.00 13.67 ?  73  GLY   A CA   1 
ATOM   1595 C C    . GLY   A 1 73  ? 38.463 1.857   -4.003  1.00 12.86 ?  73  GLY   A C    1 
ATOM   1596 O O    . GLY   A 1 73  ? 38.073 1.402   -2.921  1.00 13.24 ?  73  GLY   A O    1 
ATOM   1597 H H    . GLY   A 1 73  ? 40.616 3.196   -2.537  1.00 16.50 ?  73  GLY   A H    1 
ATOM   1598 H HA2  . GLY   A 1 73  ? 39.777 3.351   -4.494  1.00 16.40 ?  73  GLY   A HA2  1 
ATOM   1599 H HA3  . GLY   A 1 73  ? 40.330 1.914   -4.834  1.00 16.40 ?  73  GLY   A HA3  1 
ATOM   1600 N N    . PRO   A 1 74  ? 37.686 1.879   -5.083  1.00 13.35 ?  74  PRO   A N    1 
ATOM   1601 C CA   . PRO   A 1 74  ? 36.288 1.447   -5.001  1.00 13.43 ?  74  PRO   A CA   1 
ATOM   1602 C C    . PRO   A 1 74  ? 36.145 -0.033  -4.685  1.00 12.79 ?  74  PRO   A C    1 
ATOM   1603 O O    . PRO   A 1 74  ? 37.015 -0.858  -4.978  1.00 13.78 ?  74  PRO   A O    1 
ATOM   1604 C CB   . PRO   A 1 74  ? 35.742 1.747   -6.405  1.00 15.47 ?  74  PRO   A CB   1 
ATOM   1605 C CG   . PRO   A 1 74  ? 36.690 2.725   -7.008  1.00 17.92 ?  74  PRO   A CG   1 
ATOM   1606 C CD   . PRO   A 1 74  ? 38.029 2.399   -6.417  1.00 15.43 ?  74  PRO   A CD   1 
ATOM   1607 H HA   . PRO   A 1 74  ? 35.802 1.973   -4.344  1.00 16.12 ?  74  PRO   A HA   1 
ATOM   1608 H HB2  . PRO   A 1 74  ? 35.716 0.927   -6.924  1.00 18.56 ?  74  PRO   A HB2  1 
ATOM   1609 H HB3  . PRO   A 1 74  ? 34.853 2.132   -6.333  1.00 18.56 ?  74  PRO   A HB3  1 
ATOM   1610 H HG2  . PRO   A 1 74  ? 36.709 2.614   -7.971  1.00 21.50 ?  74  PRO   A HG2  1 
ATOM   1611 H HG3  . PRO   A 1 74  ? 36.426 3.627   -6.772  1.00 21.50 ?  74  PRO   A HG3  1 
ATOM   1612 H HD2  . PRO   A 1 74  ? 38.478 1.716   -6.942  1.00 18.51 ?  74  PRO   A HD2  1 
ATOM   1613 H HD3  . PRO   A 1 74  ? 38.569 3.205   -6.350  1.00 18.51 ?  74  PRO   A HD3  1 
ATOM   1614 N N    . LEU   A 1 75  ? 35.003 -0.361  -4.091  1.00 12.07 ?  75  LEU   A N    1 
ATOM   1615 C CA   . LEU   A 1 75  ? 34.603 -1.751  -3.947  1.00 11.83 ?  75  LEU   A CA   1 
ATOM   1616 C C    . LEU   A 1 75  ? 34.225 -2.332  -5.307  1.00 12.20 ?  75  LEU   A C    1 
ATOM   1617 O O    . LEU   A 1 75  ? 34.094 -1.621  -6.307  1.00 13.84 ?  75  LEU   A O    1 
ATOM   1618 C CB   . LEU   A 1 75  ? 33.412 -1.877  -2.996  1.00 11.87 ?  75  LEU   A CB   1 
ATOM   1619 C CG   . LEU   A 1 75  ? 33.622 -1.446  -1.548  1.00 13.35 ?  75  LEU   A CG   1 
ATOM   1620 C CD1  . LEU   A 1 75  ? 32.329 -1.617  -0.760  1.00 15.84 ?  75  LEU   A CD1  1 
ATOM   1621 C CD2  . LEU   A 1 75  ? 34.760 -2.156  -0.866  1.00 16.77 ?  75  LEU   A CD2  1 
ATOM   1622 H H    . LEU   A 1 75  ? 34.444 0.207   -3.765  1.00 14.47 ?  75  LEU   A H    1 
ATOM   1623 H HA   . LEU   A 1 75  ? 35.340 -2.261  -3.589  1.00 14.19 ?  75  LEU   A HA   1 
ATOM   1624 H HB2  . LEU   A 1 75  ? 32.683 -1.344  -3.347  1.00 14.23 ?  75  LEU   A HB2  1 
ATOM   1625 H HB3  . LEU   A 1 75  ? 33.143 -2.810  -2.975  1.00 14.23 ?  75  LEU   A HB3  1 
ATOM   1626 H HG   . LEU   A 1 75  ? 33.839 -0.498  -1.545  1.00 16.02 ?  75  LEU   A HG   1 
ATOM   1627 H HD11 . LEU   A 1 75  ? 32.477 -1.334  0.157   1.00 19.00 ?  75  LEU   A HD11 1 
ATOM   1628 H HD12 . LEU   A 1 75  ? 31.640 -1.066  -1.166  1.00 19.00 ?  75  LEU   A HD12 1 
ATOM   1629 H HD13 . LEU   A 1 75  ? 32.066 -2.547  -0.783  1.00 19.00 ?  75  LEU   A HD13 1 
ATOM   1630 H HD21 . LEU   A 1 75  ? 34.813 -1.857  0.056   1.00 20.12 ?  75  LEU   A HD21 1 
ATOM   1631 H HD22 . LEU   A 1 75  ? 34.603 -3.110  -0.898  1.00 20.12 ?  75  LEU   A HD22 1 
ATOM   1632 H HD23 . LEU   A 1 75  ? 35.591 -1.941  -1.327  1.00 20.12 ?  75  LEU   A HD23 1 
ATOM   1633 N N    . LYS   A 1 76  ? 34.049 -3.651  -5.327  1.00 12.44 ?  76  LYS   A N    1 
ATOM   1634 C CA   . LYS   A 1 76  ? 33.456 -4.365  -6.451  1.00 13.20 ?  76  LYS   A CA   1 
ATOM   1635 C C    . LYS   A 1 76  ? 31.945 -4.446  -6.260  1.00 11.76 ?  76  LYS   A C    1 
ATOM   1636 O O    . LYS   A 1 76  ? 31.460 -4.559  -5.135  1.00 12.24 ?  76  LYS   A O    1 
ATOM   1637 C CB   . LYS   A 1 76  ? 33.994 -5.803  -6.505  1.00 14.92 ?  76  LYS   A CB   1 
ATOM   1638 C CG   . LYS   A 1 76  ? 35.503 -5.911  -6.698  1.00 16.34 ?  76  LYS   A CG   1 
ATOM   1639 C CD   . LYS   A 1 76  ? 36.017 -7.322  -6.509  1.00 17.68 ?  76  LYS   A CD   1 
ATOM   1640 C CE   . LYS   A 1 76  ? 37.524 -7.375  -6.654  1.00 20.41 ?  76  LYS   A CE   1 
ATOM   1641 N NZ   . LYS   A 1 76  ? 38.053 -8.740  -6.490  1.00 21.17 ?  76  LYS   A NZ   1 
ATOM   1642 H H    . LYS   A 1 76  ? 34.268 -4.170  -4.675  1.00 14.92 ?  76  LYS   A H    1 
ATOM   1643 H HA   . LYS   A 1 76  ? 33.656 -3.909  -7.285  1.00 15.84 ?  76  LYS   A HA   1 
ATOM   1644 H HB2  . LYS   A 1 76  ? 33.771 -6.244  -5.672  1.00 17.90 ?  76  LYS   A HB2  1 
ATOM   1645 H HB3  . LYS   A 1 76  ? 33.569 -6.261  -7.245  1.00 17.90 ?  76  LYS   A HB3  1 
ATOM   1646 H HG2  . LYS   A 1 76  ? 35.728 -5.626  -7.598  1.00 19.61 ?  76  LYS   A HG2  1 
ATOM   1647 H HG3  . LYS   A 1 76  ? 35.948 -5.341  -6.050  1.00 19.61 ?  76  LYS   A HG3  1 
ATOM   1648 H HD2  . LYS   A 1 76  ? 35.780 -7.636  -5.622  1.00 21.21 ?  76  LYS   A HD2  1 
ATOM   1649 H HD3  . LYS   A 1 76  ? 35.623 -7.900  -7.185  1.00 21.21 ?  76  LYS   A HD3  1 
ATOM   1650 H HE2  . LYS   A 1 76  ? 37.767 -7.058  -7.536  1.00 24.48 ?  76  LYS   A HE2  1 
ATOM   1651 H HE3  . LYS   A 1 76  ? 37.924 -6.813  -5.973  1.00 24.48 ?  76  LYS   A HE3  1 
ATOM   1652 H HZ1  . LYS   A 1 76  ? 38.938 -8.741  -6.581  1.00 25.40 ?  76  LYS   A HZ1  1 
ATOM   1653 H HZ2  . LYS   A 1 76  ? 37.846 -9.059  -5.684  1.00 25.40 ?  76  LYS   A HZ2  1 
ATOM   1654 H HZ3  . LYS   A 1 76  ? 37.703 -9.283  -7.108  1.00 25.40 ?  76  LYS   A HZ3  1 
ATOM   1655 N N    . VAL   A 1 77  ? 31.199 -4.408  -7.369  1.00 12.44 ?  77  VAL   A N    1 
ATOM   1656 C CA   . VAL   A 1 77  ? 29.791 -4.794  -7.292  1.00 12.35 ?  77  VAL   A CA   1 
ATOM   1657 C C    . VAL   A 1 77  ? 29.727 -6.247  -6.846  1.00 12.22 ?  77  VAL   A C    1 
ATOM   1658 O O    . VAL   A 1 77  ? 30.395 -7.118  -7.418  1.00 12.70 ?  77  VAL   A O    1 
ATOM   1659 C CB   . VAL   A 1 77  ? 29.079 -4.583  -8.635  1.00 13.59 ?  77  VAL   A CB   1 
ATOM   1660 C CG1  . VAL   A 1 77  ? 27.615 -5.011  -8.529  1.00 14.51 ?  77  VAL   A CG1  1 
ATOM   1661 C CG2  . VAL   A 1 77  ? 29.169 -3.134  -9.068  1.00 15.06 ?  77  VAL   A CG2  1 
ATOM   1662 H H    . VAL   A 1 77  ? 31.476 -4.166  -8.149  1.00 14.92 ?  77  VAL   A H    1 
ATOM   1663 H HA   . VAL   A 1 77  ? 29.350 -4.249  -6.623  1.00 14.81 ?  77  VAL   A HA   1 
ATOM   1664 H HB   . VAL   A 1 77  ? 29.507 -5.126  -9.312  1.00 16.30 ?  77  VAL   A HB   1 
ATOM   1665 H HG11 . VAL   A 1 77  ? 27.143 -4.716  -9.321  1.00 17.41 ?  77  VAL   A HG11 1 
ATOM   1666 H HG12 . VAL   A 1 77  ? 27.572 -5.977  -8.457  1.00 17.41 ?  77  VAL   A HG12 1 
ATOM   1667 H HG13 . VAL   A 1 77  ? 27.224 -4.603  -7.739  1.00 17.41 ?  77  VAL   A HG13 1 
ATOM   1668 H HG21 . VAL   A 1 77  ? 28.675 -3.021  -9.896  1.00 18.06 ?  77  VAL   A HG21 1 
ATOM   1669 H HG22 . VAL   A 1 77  ? 28.786 -2.571  -8.377  1.00 18.06 ?  77  VAL   A HG22 1 
ATOM   1670 H HG23 . VAL   A 1 77  ? 30.100 -2.899  -9.207  1.00 18.06 ?  77  VAL   A HG23 1 
ATOM   1671 N N    . GLY   A 1 78  ? 28.937 -6.512  -5.802  1.00 11.65 ?  78  GLY   A N    1 
ATOM   1672 C CA   . GLY   A 1 78  ? 28.909 -7.801  -5.148  1.00 12.07 ?  78  GLY   A CA   1 
ATOM   1673 C C    . GLY   A 1 78  ? 29.822 -7.897  -3.949  1.00 11.71 ?  78  GLY   A C    1 
ATOM   1674 O O    . GLY   A 1 78  ? 29.764 -8.903  -3.222  1.00 12.53 ?  78  GLY   A O    1 
ATOM   1675 H H    . GLY   A 1 78  ? 28.394 -5.936  -5.460  1.00 13.98 ?  78  GLY   A H    1 
ATOM   1676 H HA2  . GLY   A 1 78  ? 28.003 -7.985  -4.857  1.00 14.48 ?  78  GLY   A HA2  1 
ATOM   1677 H HA3  . GLY   A 1 78  ? 29.167 -8.483  -5.787  1.00 14.48 ?  78  GLY   A HA3  1 
ATOM   1678 N N    . GLY   A 1 79  ? 30.666 -6.889  -3.718  1.00 11.57 ?  79  GLY   A N    1 
ATOM   1679 C CA   . GLY   A 1 79  ? 31.631 -6.914  -2.642  1.00 11.77 ?  79  GLY   A CA   1 
ATOM   1680 C C    . GLY   A 1 79  ? 31.183 -6.119  -1.428  1.00 11.26 ?  79  GLY   A C    1 
ATOM   1681 O O    . GLY   A 1 79  ? 30.064 -5.609  -1.355  1.00 11.97 ?  79  GLY   A O    1 
ATOM   1682 H H    . GLY   A 1 79  ? 30.699 -6.166  -4.189  1.00 13.88 ?  79  GLY   A H    1 
ATOM   1683 H HA2  . GLY   A 1 79  ? 31.784 -7.839  -2.374  1.00 14.12 ?  79  GLY   A HA2  1 
ATOM   1684 H HA3  . GLY   A 1 79  ? 32.473 -6.550  -2.956  1.00 14.12 ?  79  GLY   A HA3  1 
ATOM   1685 N N    . SER   A 1 80  ? 32.086 -6.026  -0.453  1.00 11.89 ?  80  SER   A N    1 
ATOM   1686 C CA   . SER   A 1 80  ? 31.760 -5.397  0.816   1.00 11.22 ?  80  SER   A CA   1 
ATOM   1687 C C    . SER   A 1 80  ? 33.029 -4.944  1.517   1.00 11.62 ?  80  SER   A C    1 
ATOM   1688 O O    . SER   A 1 80  ? 34.142 -5.369  1.188   1.00 12.88 ?  80  SER   A O    1 
ATOM   1689 C CB   . SER   A 1 80  ? 30.995 -6.356  1.735   1.00 12.13 ?  80  SER   A CB   1 
ATOM   1690 O OG   . SER   A 1 80  ? 31.824 -7.401  2.221   1.00 13.92 ?  80  SER   A OG   1 
ATOM   1691 H H    . SER   A 1 80  ? 32.897 -6.312  -0.510  1.00 14.26 ?  80  SER   A H    1 
ATOM   1692 H HA   . SER   A 1 80  ? 31.205 -4.622  0.637   1.00 13.46 ?  80  SER   A HA   1 
ATOM   1693 H HB2  . SER   A 1 80  ? 30.652 -5.854  2.489   1.00 14.55 ?  80  SER   A HB2  1 
ATOM   1694 H HB3  . SER   A 1 80  ? 30.262 -6.747  1.236   1.00 14.55 ?  80  SER   A HB3  1 
ATOM   1695 H HG   . SER   A 1 80  ? 32.131 -7.845  1.575   1.00 16.70 ?  80  SER   A HG   1 
ATOM   1696 N N    . CYS   A 1 81  ? 32.837 -4.096  2.523   1.00 11.17 ?  81  CYS   A N    1 
ATOM   1697 C CA   . CYS   A 1 81  ? 33.884 -3.816  3.489   1.00 11.44 ?  81  CYS   A CA   1 
ATOM   1698 C C    . CYS   A 1 81  ? 33.239 -3.579  4.846   1.00 11.28 ?  81  CYS   A C    1 
ATOM   1699 O O    . CYS   A 1 81  ? 32.076 -3.174  4.933   1.00 12.49 ?  81  CYS   A O    1 
ATOM   1700 C CB   . CYS   A 1 81  ? 34.754 -2.625  3.067   1.00 12.15 ?  81  CYS   A CB   1 
ATOM   1701 S SG   . CYS   A 1 81  ? 33.862 -1.046  3.087   1.00 12.20 ?  81  CYS   A SG   1 
ATOM   1702 H H    . CYS   A 1 81  ? 32.097 -3.676  2.678   1.00 13.39 ?  81  CYS   A H    1 
ATOM   1703 H HA   . CYS   A 1 81  ? 34.460 -4.593  3.565   1.00 13.73 ?  81  CYS   A HA   1 
ATOM   1704 H HB2  . CYS   A 1 81  ? 35.511 -2.556  3.676   1.00 14.58 ?  81  CYS   A HB2  1 
ATOM   1705 H HB3  . CYS   A 1 81  ? 35.080 -2.780  2.163   1.00 14.58 ?  81  CYS   A HB3  1 
ATOM   1706 H HG   . CYS   A 1 81  ? 34.610 -0.170  2.745   1.00 14.63 ?  81  CYS   A HG   1 
ATOM   1707 N N    . VAL   A 1 82  ? 34.005 -3.839  5.902   1.00 11.46 ?  82  VAL   A N    1 
ATOM   1708 C CA   . VAL   A 1 82  ? 33.578 -3.600  7.273   1.00 11.82 ?  82  VAL   A CA   1 
ATOM   1709 C C    . VAL   A 1 82  ? 34.178 -2.287  7.744   1.00 12.06 ?  82  VAL   A C    1 
ATOM   1710 O O    . VAL   A 1 82  ? 35.401 -2.114  7.727   1.00 12.98 ?  82  VAL   A O    1 
ATOM   1711 C CB   . VAL   A 1 82  ? 34.000 -4.742  8.208   1.00 13.49 ?  82  VAL   A CB   1 
ATOM   1712 C CG1  . VAL   A 1 82  ? 33.535 -4.456  9.626   1.00 14.84 ?  82  VAL   A CG1  1 
ATOM   1713 C CG2  . VAL   A 1 82  ? 33.457 -6.071  7.718   1.00 14.82 ?  82  VAL   A CG2  1 
ATOM   1714 H H    . VAL   A 1 82  ? 34.803 -4.174  5.849   1.00 13.74 ?  82  VAL   A H    1 
ATOM   1715 H HA   . VAL   A 1 82  ? 32.611 -3.521  7.298   1.00 14.18 ?  82  VAL   A HA   1 
ATOM   1716 H HB   . VAL   A 1 82  ? 34.965 -4.795  8.221   1.00 16.18 ?  82  VAL   A HB   1 
ATOM   1717 H HG11 . VAL   A 1 82  ? 33.625 -5.262  10.156  1.00 17.80 ?  82  VAL   A HG11 1 
ATOM   1718 H HG12 . VAL   A 1 82  ? 34.078 -3.748  10.006  1.00 17.80 ?  82  VAL   A HG12 1 
ATOM   1719 H HG13 . VAL   A 1 82  ? 32.602 -4.180  9.604   1.00 17.80 ?  82  VAL   A HG13 1 
ATOM   1720 H HG21 . VAL   A 1 82  ? 33.697 -6.762  8.356   1.00 17.78 ?  82  VAL   A HG21 1 
ATOM   1721 H HG22 . VAL   A 1 82  ? 32.491 -6.010  7.646   1.00 17.78 ?  82  VAL   A HG22 1 
ATOM   1722 H HG23 . VAL   A 1 82  ? 33.843 -6.269  6.853   1.00 17.78 ?  82  VAL   A HG23 1 
ATOM   1723 N N    . LEU   A 1 83  ? 33.323 -1.367  8.168   1.00 11.62 ?  83  LEU   A N    1 
ATOM   1724 C CA   . LEU   A 1 83  ? 33.746 -0.103  8.746   1.00 11.63 ?  83  LEU   A CA   1 
ATOM   1725 C C    . LEU   A 1 83  ? 33.029 0.076   10.077  1.00 11.72 ?  83  LEU   A C    1 
ATOM   1726 O O    . LEU   A 1 83  ? 32.303 -0.811  10.538  1.00 12.33 ?  83  LEU   A O    1 
ATOM   1727 C CB   . LEU   A 1 83  ? 33.493 1.058   7.770   1.00 12.33 ?  83  LEU   A CB   1 
ATOM   1728 C CG   . LEU   A 1 83  ? 34.399 1.053   6.531   1.00 13.01 ?  83  LEU   A CG   1 
ATOM   1729 C CD1  . LEU   A 1 83  ? 33.967 2.098   5.518   1.00 13.28 ?  83  LEU   A CD1  1 
ATOM   1730 C CD2  . LEU   A 1 83  ? 35.870 1.266   6.918   1.00 13.49 ?  83  LEU   A CD2  1 
ATOM   1731 H H    . LEU   A 1 83  ? 32.466 -1.452  8.125   1.00 13.94 ?  83  LEU   A H    1 
ATOM   1732 H HA   . LEU   A 1 83  ? 34.697 -0.132  8.921   1.00 13.94 ?  83  LEU   A HA   1 
ATOM   1733 H HB2  . LEU   A 1 83  ? 32.574 1.015   7.456   1.00 14.78 ?  83  LEU   A HB2  1 
ATOM   1734 H HB3  . LEU   A 1 83  ? 33.636 1.900   8.232   1.00 14.78 ?  83  LEU   A HB3  1 
ATOM   1735 H HG   . LEU   A 1 83  ? 34.335 0.183   6.106   1.00 15.61 ?  83  LEU   A HG   1 
ATOM   1736 H HD11 . LEU   A 1 83  ? 34.562 2.058   4.751   1.00 15.93 ?  83  LEU   A HD11 1 
ATOM   1737 H HD12 . LEU   A 1 83  ? 33.058 1.910   5.243   1.00 15.93 ?  83  LEU   A HD12 1 
ATOM   1738 H HD13 . LEU   A 1 83  ? 34.017 2.974   5.929   1.00 15.93 ?  83  LEU   A HD13 1 
ATOM   1739 H HD21 . LEU   A 1 83  ? 36.393 1.424   6.114   1.00 16.18 ?  83  LEU   A HD21 1 
ATOM   1740 H HD22 . LEU   A 1 83  ? 35.938 2.034   7.509   1.00 16.18 ?  83  LEU   A HD22 1 
ATOM   1741 H HD23 . LEU   A 1 83  ? 36.203 0.473   7.372   1.00 16.18 ?  83  LEU   A HD23 1 
ATOM   1742 N N    . SER   A 1 84  ? 33.238 1.228   10.707  1.00 12.44 ?  84  SER   A N    1 
ATOM   1743 C CA   . SER   A 1 84  ? 32.592 1.485   11.983  1.00 12.34 ?  84  SER   A CA   1 
ATOM   1744 C C    . SER   A 1 84  ? 31.074 1.567   11.832  1.00 12.06 ?  84  SER   A C    1 
ATOM   1745 O O    . SER   A 1 84  ? 30.550 2.033   10.820  1.00 12.34 ?  84  SER   A O    1 
ATOM   1746 C CB   . SER   A 1 84  ? 33.080 2.810   12.552  1.00 13.56 ?  84  SER   A CB   1 
ATOM   1747 O OG   . SER   A 1 84  ? 32.466 3.074   13.796  1.00 14.52 ?  84  SER   A OG   1 
ATOM   1748 H H    . SER   A 1 84  ? 33.741 1.869   10.417  1.00 14.92 ?  84  SER   A H    1 
ATOM   1749 H HA   . SER   A 1 84  ? 32.814 0.775   12.605  1.00 14.80 ?  84  SER   A HA   1 
ATOM   1750 H HB2  . SER   A 1 84  ? 34.044 2.773   12.667  1.00 16.26 ?  84  SER   A HB2  1 
ATOM   1751 H HB3  . SER   A 1 84  ? 32.852 3.524   11.932  1.00 16.26 ?  84  SER   A HB3  1 
ATOM   1752 H HG   . SER   A 1 84  ? 32.747 3.803   14.105  1.00 17.42 ?  84  SER   A HG   1 
ATOM   1753 N N    . GLY   A 1 85  ? 30.367 1.150   12.881  1.00 13.19 ?  85  GLY   A N    1 
ATOM   1754 C CA   . GLY   A 1 85  ? 28.944 1.387   12.971  1.00 13.76 ?  85  GLY   A CA   1 
ATOM   1755 C C    . GLY   A 1 85  ? 28.577 2.701   13.616  1.00 13.56 ?  85  GLY   A C    1 
ATOM   1756 O O    . GLY   A 1 85  ? 27.386 3.011   13.728  1.00 14.19 ?  85  GLY   A O    1 
ATOM   1757 H H    . GLY   A 1 85  ? 30.699 0.719   13.552  1.00 15.82 ?  85  GLY   A H    1 
ATOM   1758 H HA2  . GLY   A 1 85  ? 28.567 1.372   12.078  1.00 16.50 ?  85  GLY   A HA2  1 
ATOM   1759 H HA3  . GLY   A 1 85  ? 28.536 0.676   13.483  1.00 16.50 ?  85  GLY   A HA3  1 
ATOM   1760 N N    . HIS   A 1 86  ? 29.566 3.477   14.057  1.00 13.51 ?  86  HIS   A N    1 
ATOM   1761 C CA   . HIS   A 1 86  ? 29.344 4.816   14.621  1.00 13.61 ?  86  HIS   A CA   1 
ATOM   1762 C C    . HIS   A 1 86  ? 28.357 4.694   15.775  1.00 14.59 ?  86  HIS   A C    1 
ATOM   1763 O O    . HIS   A 1 86  ? 28.536 3.815   16.632  1.00 16.11 ?  86  HIS   A O    1 
ATOM   1764 C CB   . HIS   A 1 86  ? 28.969 5.793   13.517  1.00 13.73 ?  86  HIS   A CB   1 
ATOM   1765 C CG   . HIS   A 1 86  ? 30.025 5.891   12.475  1.00 13.85 ?  86  HIS   A CG   1 
ATOM   1766 N ND1  . HIS   A 1 86  ? 31.117 6.723   12.604  1.00 14.68 ?  86  HIS   A ND1  1 
ATOM   1767 C CD2  . HIS   A 1 86  ? 30.201 5.204   11.325  1.00 13.52 ?  86  HIS   A CD2  1 
ATOM   1768 C CE1  . HIS   A 1 86  ? 31.905 6.562   11.557  1.00 14.46 ?  86  HIS   A CE1  1 
ATOM   1769 N NE2  . HIS   A 1 86  ? 31.383 5.635   10.776  1.00 13.90 ?  86  HIS   A NE2  1 
ATOM   1770 H H    . HIS   A 1 86  ? 30.391 3.252   14.046  1.00 16.21 ?  86  HIS   A H    1 
ATOM   1771 H HA   . HIS   A 1 86  ? 30.182 5.129   14.994  1.00 16.33 ?  86  HIS   A HA   1 
ATOM   1772 H HB2  . HIS   A 1 86  ? 28.147 5.504   13.092  1.00 16.47 ?  86  HIS   A HB2  1 
ATOM   1773 H HB3  . HIS   A 1 86  ? 28.847 6.682   13.898  1.00 16.47 ?  86  HIS   A HB3  1 
ATOM   1774 H HD2  . HIS   A 1 86  ? 29.637 4.543   10.976  1.00 16.22 ?  86  HIS   A HD2  1 
ATOM   1775 H HE1  . HIS   A 1 86  ? 32.697 7.018   11.389  1.00 17.35 ?  86  HIS   A HE1  1 
ATOM   1776 H HE2  . HIS   A 1 86  ? 31.714 5.360   10.022  1.00 16.67 ?  86  HIS   A HE2  1 
ATOM   1777 N N    . ASN   A 1 87  ? 27.338 5.540   15.842  1.00 15.75 ?  87  ASN   A N    1 
ATOM   1778 C CA   . ASN   A 1 87  ? 26.359 5.523   16.914  1.00 16.54 ?  87  ASN   A CA   1 
ATOM   1779 C C    . ASN   A 1 87  ? 25.235 4.528   16.675  1.00 17.98 ?  87  ASN   A C    1 
ATOM   1780 O O    . ASN   A 1 87  ? 24.319 4.461   17.495  1.00 20.30 ?  87  ASN   A O    1 
ATOM   1781 C CB   . ASN   A 1 87  ? 25.762 6.928   17.081  1.00 17.64 ?  87  ASN   A CB   1 
ATOM   1782 C CG   . ASN   A 1 87  ? 25.265 7.514   15.766  1.00 18.42 ?  87  ASN   A CG   1 
ATOM   1783 O OD1  . ASN   A 1 87  ? 25.911 7.390   14.731  1.00 19.05 ?  87  ASN   A OD1  1 
ATOM   1784 N ND2  . ASN   A 1 87  ? 24.113 8.162   15.808  1.00 19.70 ?  87  ASN   A ND2  1 
ATOM   1785 H H    . ASN   A 1 87  ? 27.190 6.150   15.261  1.00 18.89 ?  87  ASN   A H    1 
ATOM   1786 H HA   . ASN   A 1 87  ? 26.792 5.283   17.748  1.00 19.84 ?  87  ASN   A HA   1 
ATOM   1787 H HB2  . ASN   A 1 87  ? 25.010 6.883   17.697  1.00 21.17 ?  87  ASN   A HB2  1 
ATOM   1788 H HB3  . ASN   A 1 87  ? 26.443 7.519   17.438  1.00 21.17 ?  87  ASN   A HB3  1 
ATOM   1789 H HD21 . ASN   A 1 87  ? 23.793 8.508   15.090  1.00 23.64 ?  87  ASN   A HD21 1 
ATOM   1790 H HD22 . ASN   A 1 87  ? 23.687 8.238   16.551  1.00 23.64 ?  87  ASN   A HD22 1 
ATOM   1791 N N    . LEU   A 1 88  ? 25.284 3.754   15.595  1.00 16.43 ?  88  LEU   A N    1 
ATOM   1792 C CA   . LEU   A 1 88  ? 24.172 2.893   15.204  1.00 16.37 ?  88  LEU   A CA   1 
ATOM   1793 C C    . LEU   A 1 88  ? 24.391 1.418   15.504  1.00 16.01 ?  88  LEU   A C    1 
ATOM   1794 O O    . LEU   A 1 88  ? 23.414 0.689   15.693  1.00 17.02 ?  88  LEU   A O    1 
ATOM   1795 C CB   . LEU   A 1 88  ? 23.923 3.041   13.703  1.00 16.92 ?  88  LEU   A CB   1 
ATOM   1796 C CG   . LEU   A 1 88  ? 23.639 4.462   13.222  1.00 18.68 ?  88  LEU   A CG   1 
ATOM   1797 C CD1  . LEU   A 1 88  ? 23.469 4.458   11.719  1.00 19.27 ?  88  LEU   A CD1  1 
ATOM   1798 C CD2  . LEU   A 1 88  ? 22.408 5.037   13.911  1.00 20.15 ?  88  LEU   A CD2  1 
ATOM   1799 H H    . LEU   A 1 88  ? 25.962 3.710   15.070  1.00 19.71 ?  88  LEU   A H    1 
ATOM   1800 H HA   . LEU   A 1 88  ? 23.371 3.182   15.669  1.00 19.63 ?  88  LEU   A HA   1 
ATOM   1801 H HB2  . LEU   A 1 88  ? 24.704 2.729   13.226  1.00 20.30 ?  88  LEU   A HB2  1 
ATOM   1802 H HB3  . LEU   A 1 88  ? 23.154 2.500   13.463  1.00 20.30 ?  88  LEU   A HB3  1 
ATOM   1803 H HG   . LEU   A 1 88  ? 24.395 5.031   13.436  1.00 22.41 ?  88  LEU   A HG   1 
ATOM   1804 H HD11 . LEU   A 1 88  ? 23.307 5.365   11.415  1.00 23.11 ?  88  LEU   A HD11 1 
ATOM   1805 H HD12 . LEU   A 1 88  ? 24.279 4.112   11.313  1.00 23.11 ?  88  LEU   A HD12 1 
ATOM   1806 H HD13 . LEU   A 1 88  ? 22.715 3.892   11.489  1.00 23.11 ?  88  LEU   A HD13 1 
ATOM   1807 H HD21 . LEU   A 1 88  ? 22.176 5.880   13.491  1.00 24.18 ?  88  LEU   A HD21 1 
ATOM   1808 H HD22 . LEU   A 1 88  ? 21.676 4.409   13.820  1.00 24.18 ?  88  LEU   A HD22 1 
ATOM   1809 H HD23 . LEU   A 1 88  ? 22.610 5.178   14.848  1.00 24.18 ?  88  LEU   A HD23 1 
ATOM   1810 N N    . ALA   A 1 89  ? 25.639 0.967   15.520  1.00 15.35 ?  89  ALA   A N    1 
ATOM   1811 C CA   . ALA   A 1 89  ? 25.985 -0.442  15.635  1.00 14.78 ?  89  ALA   A CA   1 
ATOM   1812 C C    . ALA   A 1 89  ? 27.467 -0.497  15.958  1.00 15.02 ?  89  ALA   A C    1 
ATOM   1813 O O    . ALA   A 1 89  ? 28.176 0.503   15.837  1.00 15.99 ?  89  ALA   A O    1 
ATOM   1814 C CB   . ALA   A 1 89  ? 25.727 -1.173  14.318  1.00 14.24 ?  89  ALA   A CB   1 
ATOM   1815 H H    . ALA   A 1 89  ? 26.323 1.481   15.446  1.00 18.41 ?  89  ALA   A H    1 
ATOM   1816 H HA   . ALA   A 1 89  ? 25.470 -0.855  16.349  1.00 17.73 ?  89  ALA   A HA   1 
ATOM   1817 H HB1  . ALA   A 1 89  ? 25.982 -2.104  14.424  1.00 17.08 ?  89  ALA   A HB1  1 
ATOM   1818 H HB2  . ALA   A 1 89  ? 24.786 -1.110  14.096  1.00 17.08 ?  89  ALA   A HB2  1 
ATOM   1819 H HB3  . ALA   A 1 89  ? 26.262 -0.763  13.622  1.00 17.08 ?  89  ALA   A HB3  1 
ATOM   1820 N N    . LYS   A 1 90  ? 27.947 -1.672  16.355  1.00 15.72 ?  90  LYS   A N    1 
ATOM   1821 C CA   . LYS   A 1 90  ? 29.391 -1.821  16.503  1.00 16.72 ?  90  LYS   A CA   1 
ATOM   1822 C C    . LYS   A 1 90  ? 30.090 -1.640  15.159  1.00 15.54 ?  90  LYS   A C    1 
ATOM   1823 O O    . LYS   A 1 90  ? 31.037 -0.846  15.031  1.00 16.74 ?  90  LYS   A O    1 
ATOM   1824 C CB   . LYS   A 1 90  ? 29.725 -3.180  17.119  1.00 19.99 ?  90  LYS   A CB   1 
ATOM   1825 C CG   . LYS   A 1 90  ? 31.196 -3.328  17.474  1.00 24.87 ?  90  LYS   A CG   1 
ATOM   1826 C CD   . LYS   A 1 90  ? 31.438 -4.559  18.334  1.00 29.94 ?  90  LYS   A CD   1 
ATOM   1827 C CE   . LYS   A 1 90  ? 32.848 -4.579  18.906  1.00 34.24 ?  90  LYS   A CE   1 
ATOM   1828 N NZ   . LYS   A 1 90  ? 33.883 -4.848  17.871  1.00 36.67 ?  90  LYS   A NZ   1 
ATOM   1829 H H    . LYS   A 1 90  ? 27.473 -2.359  16.549  1.00 18.86 ?  90  LYS   A H    1 
ATOM   1830 H HA   . LYS   A 1 90  ? 29.717 -1.132  17.103  1.00 20.05 ?  90  LYS   A HA   1 
ATOM   1831 H HB2  . LYS   A 1 90  ? 29.205 -3.291  17.932  1.00 23.98 ?  90  LYS   A HB2  1 
ATOM   1832 H HB3  . LYS   A 1 90  ? 29.495 -3.875  16.484  1.00 23.98 ?  90  LYS   A HB3  1 
ATOM   1833 H HG2  . LYS   A 1 90  ? 31.714 -3.418  16.659  1.00 29.84 ?  90  LYS   A HG2  1 
ATOM   1834 H HG3  . LYS   A 1 90  ? 31.485 -2.547  17.972  1.00 29.84 ?  90  LYS   A HG3  1 
ATOM   1835 H HD2  . LYS   A 1 90  ? 30.809 -4.560  19.074  1.00 35.92 ?  90  LYS   A HD2  1 
ATOM   1836 H HD3  . LYS   A 1 90  ? 31.317 -5.355  17.793  1.00 35.92 ?  90  LYS   A HD3  1 
ATOM   1837 H HE2  . LYS   A 1 90  ? 33.040 -3.715  19.304  1.00 41.08 ?  90  LYS   A HE2  1 
ATOM   1838 H HE3  . LYS   A 1 90  ? 32.907 -5.274  19.579  1.00 41.08 ?  90  LYS   A HE3  1 
ATOM   1839 H HZ1  . LYS   A 1 90  ? 34.692 -4.854  18.245  1.00 43.99 ?  90  LYS   A HZ1  1 
ATOM   1840 H HZ2  . LYS   A 1 90  ? 33.735 -5.639  17.492  1.00 43.99 ?  90  LYS   A HZ2  1 
ATOM   1841 H HZ3  . LYS   A 1 90  ? 33.860 -4.217  17.245  1.00 43.99 ?  90  LYS   A HZ3  1 
ATOM   1842 N N    . HIS   A 1 91  ? 29.618 -2.356  14.140  1.00 13.75 ?  91  HIS   A N    1 
ATOM   1843 C CA   . HIS   A 1 91  ? 30.195 -2.345  12.810  1.00 13.03 ?  91  HIS   A CA   1 
ATOM   1844 C C    . HIS   A 1 91  ? 29.112 -2.066  11.783  1.00 11.77 ?  91  HIS   A C    1 
ATOM   1845 O O    . HIS   A 1 91  ? 27.947 -2.423  11.972  1.00 12.79 ?  91  HIS   A O    1 
ATOM   1846 C CB   . HIS   A 1 91  ? 30.792 -3.714  12.463  1.00 15.52 ?  91  HIS   A CB   1 
ATOM   1847 C CG   . HIS   A 1 91  ? 31.791 -4.211  13.458  1.00 19.80 ?  91  HIS   A CG   1 
ATOM   1848 N ND1  . HIS   A 1 91  ? 33.065 -3.694  13.557  1.00 22.10 ?  91  HIS   A ND1  1 
ATOM   1849 C CD2  . HIS   A 1 91  ? 31.709 -5.188  14.392  1.00 21.78 ?  91  HIS   A CD2  1 
ATOM   1850 C CE1  . HIS   A 1 91  ? 33.723 -4.328  14.511  1.00 23.05 ?  91  HIS   A CE1  1 
ATOM   1851 N NE2  . HIS   A 1 91  ? 32.923 -5.241  15.033  1.00 23.08 ?  91  HIS   A NE2  1 
ATOM   1852 H H    . HIS   A 1 91  ? 28.931 -2.887  14.206  1.00 16.49 ?  91  HIS   A H    1 
ATOM   1853 H HA   . HIS   A 1 91  ? 30.884 -1.674  12.748  1.00 15.63 ?  91  HIS   A HA   1 
ATOM   1854 H HB2  . HIS   A 1 91  ? 30.075 -4.370  12.416  1.00 18.61 ?  91  HIS   A HB2  1 
ATOM   1855 H HB3  . HIS   A 1 91  ? 31.235 -3.654  11.603  1.00 18.61 ?  91  HIS   A HB3  1 
ATOM   1856 H HD1  . HIS   A 1 91  ? 33.381 -3.057  13.069  1.00 26.52 ?  91  HIS   A HD1  1 
ATOM   1857 H HD2  . HIS   A 1 91  ? 30.974 -5.724  14.570  1.00 26.13 ?  91  HIS   A HD2  1 
ATOM   1858 H HE1  . HIS   A 1 91  ? 34.603 -4.154  14.768  1.00 27.65 ?  91  HIS   A HE1  1 
ATOM   1859 N N    . CYS   A 1 92  ? 29.517 -1.465  10.671  1.00 11.38 ?  92  CYS   A N    1 
ATOM   1860 C CA   . CYS   A 1 92  ? 28.688 -1.389  9.477   1.00 11.51 ?  92  CYS   A CA   1 
ATOM   1861 C C    . CYS   A 1 92  ? 29.339 -2.204  8.368   1.00 11.18 ?  92  CYS   A C    1 
ATOM   1862 O O    . CYS   A 1 92  ? 30.500 -1.959  8.009   1.00 11.96 ?  92  CYS   A O    1 
ATOM   1863 C CB   . CYS   A 1 92  ? 28.479 0.054   9.015   1.00 11.75 ?  92  CYS   A CB   1 
ATOM   1864 S SG   . CYS   A 1 92  ? 27.468 0.156   7.507   1.00 11.45 ?  92  CYS   A SG   1 
ATOM   1865 H H    . CYS   A 1 92  ? 30.287 -1.085  10.584  1.00 13.65 ?  92  CYS   A H    1 
ATOM   1866 H HA   . CYS   A 1 92  ? 27.821 -1.773  9.670   1.00 13.81 ?  92  CYS   A HA   1 
ATOM   1867 H HB2  . CYS   A 1 92  ? 28.025 0.550   9.718   1.00 14.09 ?  92  CYS   A HB2  1 
ATOM   1868 H HB3  . CYS   A 1 92  ? 29.341 0.458   8.829   1.00 14.09 ?  92  CYS   A HB3  1 
ATOM   1869 H HG   . CYS   A 1 92  ? 27.332 1.313   7.213   1.00 13.73 ?  92  CYS   A HG   1 
ATOM   1870 N N    . LEU   A 1 93  ? 28.603 -3.188  7.859   1.00 11.03 ?  93  LEU   A N    1 
ATOM   1871 C CA   . LEU   A 1 93  ? 29.009 -3.947  6.684   1.00 10.46 ?  93  LEU   A CA   1 
ATOM   1872 C C    . LEU   A 1 93  ? 28.414 -3.260  5.460   1.00 10.26 ?  93  LEU   A C    1 
ATOM   1873 O O    . LEU   A 1 93  ? 27.200 -3.314  5.238   1.00 10.65 ?  93  LEU   A O    1 
ATOM   1874 C CB   . LEU   A 1 93  ? 28.520 -5.393  6.789   1.00 11.22 ?  93  LEU   A CB   1 
ATOM   1875 C CG   . LEU   A 1 93  ? 28.912 -6.295  5.618   1.00 11.49 ?  93  LEU   A CG   1 
ATOM   1876 C CD1  . LEU   A 1 93  ? 30.421 -6.542  5.606   1.00 12.23 ?  93  LEU   A CD1  1 
ATOM   1877 C CD2  . LEU   A 1 93  ? 28.142 -7.620  5.651   1.00 12.17 ?  93  LEU   A CD2  1 
ATOM   1878 H H    . LEU   A 1 93  ? 27.843 -3.437  8.189   1.00 13.23 ?  93  LEU   A H    1 
ATOM   1879 H HA   . LEU   A 1 93  ? 29.972 -3.942  6.614   1.00 12.55 ?  93  LEU   A HA   1 
ATOM   1880 H HB2  . LEU   A 1 93  ? 28.889 -5.781  7.599   1.00 13.46 ?  93  LEU   A HB2  1 
ATOM   1881 H HB3  . LEU   A 1 93  ? 27.552 -5.388  6.845   1.00 13.46 ?  93  LEU   A HB3  1 
ATOM   1882 H HG   . LEU   A 1 93  ? 28.688 -5.851  4.792   1.00 13.78 ?  93  LEU   A HG   1 
ATOM   1883 H HD11 . LEU   A 1 93  ? 30.641 -7.160  4.891   1.00 14.67 ?  93  LEU   A HD11 1 
ATOM   1884 H HD12 . LEU   A 1 93  ? 30.884 -5.700  5.467   1.00 14.67 ?  93  LEU   A HD12 1 
ATOM   1885 H HD13 . LEU   A 1 93  ? 30.692 -6.925  6.461   1.00 14.67 ?  93  LEU   A HD13 1 
ATOM   1886 H HD21 . LEU   A 1 93  ? 28.421 -8.165  4.895   1.00 14.60 ?  93  LEU   A HD21 1 
ATOM   1887 H HD22 . LEU   A 1 93  ? 28.338 -8.083  6.480   1.00 14.60 ?  93  LEU   A HD22 1 
ATOM   1888 H HD23 . LEU   A 1 93  ? 27.193 -7.435  5.590   1.00 14.60 ?  93  LEU   A HD23 1 
ATOM   1889 N N    . HIS   A 1 94  ? 29.265 -2.566  4.699   1.00 10.28 ?  94  HIS   A N    1 
ATOM   1890 C CA   . HIS   A 1 94  ? 28.847 -1.892  3.472   1.00 10.56 ?  94  HIS   A CA   1 
ATOM   1891 C C    . HIS   A 1 94  ? 28.859 -2.925  2.363   1.00 10.28 ?  94  HIS   A C    1 
ATOM   1892 O O    . HIS   A 1 94  ? 29.923 -3.441  2.019   1.00 11.77 ?  94  HIS   A O    1 
ATOM   1893 C CB   . HIS   A 1 94  ? 29.799 -0.741  3.143   1.00 10.50 ?  94  HIS   A CB   1 
ATOM   1894 C CG   . HIS   A 1 94  ? 29.789 0.342   4.164   1.00 10.50 ?  94  HIS   A CG   1 
ATOM   1895 N ND1  . HIS   A 1 94  ? 28.918 1.407   4.107   1.00 10.46 ?  94  HIS   A ND1  1 
ATOM   1896 C CD2  . HIS   A 1 94  ? 30.526 0.505   5.285   1.00 11.12 ?  94  HIS   A CD2  1 
ATOM   1897 C CE1  . HIS   A 1 94  ? 29.130 2.183   5.152   1.00 10.67 ?  94  HIS   A CE1  1 
ATOM   1898 N NE2  . HIS   A 1 94  ? 30.102 1.662   5.879   1.00 11.10 ?  94  HIS   A NE2  1 
ATOM   1899 H H    . HIS   A 1 94  ? 30.103 -2.471  4.876   1.00 12.33 ?  94  HIS   A H    1 
ATOM   1900 H HA   . HIS   A 1 94  ? 27.946 -1.545  3.574   1.00 12.67 ?  94  HIS   A HA   1 
ATOM   1901 H HB2  . HIS   A 1 94  ? 30.699 -1.087  3.086   1.00 12.60 ?  94  HIS   A HB2  1 
ATOM   1902 H HB3  . HIS   A 1 94  ? 29.533 -0.352  2.295   1.00 12.60 ?  94  HIS   A HB3  1 
ATOM   1903 H HD2  . HIS   A 1 94  ? 31.197 -0.053  5.592   1.00 13.34 ?  94  HIS   A HD2  1 
ATOM   1904 H HE1  . HIS   A 1 94  ? 28.664 2.970   5.338   1.00 12.80 ?  94  HIS   A HE1  1 
ATOM   1905 H HE2  . HIS   A 1 94  ? 30.410 2.003   6.605   1.00 13.32 ?  94  HIS   A HE2  1 
ATOM   1906 N N    . VAL   A 1 95  ? 27.688 -3.246  1.816   1.00 9.85  ?  95  VAL   A N    1 
ATOM   1907 C CA   . VAL   A 1 95  ? 27.551 -4.279  0.795   1.00 9.79  ?  95  VAL   A CA   1 
ATOM   1908 C C    . VAL   A 1 95  ? 27.007 -3.643  -0.471  1.00 9.39  ?  95  VAL   A C    1 
ATOM   1909 O O    . VAL   A 1 95  ? 26.003 -2.918  -0.422  1.00 10.60 ?  95  VAL   A O    1 
ATOM   1910 C CB   . VAL   A 1 95  ? 26.621 -5.418  1.245   1.00 10.59 ?  95  VAL   A CB   1 
ATOM   1911 C CG1  . VAL   A 1 95  ? 26.522 -6.460  0.140   1.00 11.73 ?  95  VAL   A CG1  1 
ATOM   1912 C CG2  . VAL   A 1 95  ? 27.108 -6.037  2.537   1.00 10.85 ?  95  VAL   A CG2  1 
ATOM   1913 H H    . VAL   A 1 95  ? 26.941 -2.880  2.031   1.00 11.81 ?  95  VAL   A H    1 
ATOM   1914 H HA   . VAL   A 1 95  ? 28.420 -4.658  0.597   1.00 11.75 ?  95  VAL   A HA   1 
ATOM   1915 H HB   . VAL   A 1 95  ? 25.734 -5.065  1.397   1.00 12.70 ?  95  VAL   A HB   1 
ATOM   1916 H HG11 . VAL   A 1 95  ? 26.142 -7.277  0.504   1.00 14.07 ?  95  VAL   A HG11 1 
ATOM   1917 H HG12 . VAL   A 1 95  ? 25.958 -6.125  -0.573  1.00 14.07 ?  95  VAL   A HG12 1 
ATOM   1918 H HG13 . VAL   A 1 95  ? 27.414 -6.646  -0.205  1.00 14.07 ?  95  VAL   A HG13 1 
ATOM   1919 H HG21 . VAL   A 1 95  ? 26.537 -6.795  2.754   1.00 13.01 ?  95  VAL   A HG21 1 
ATOM   1920 H HG22 . VAL   A 1 95  ? 28.021 -6.335  2.421   1.00 13.01 ?  95  VAL   A HG22 1 
ATOM   1921 H HG23 . VAL   A 1 95  ? 27.056 -5.374  3.239   1.00 13.01 ?  95  VAL   A HG23 1 
ATOM   1922 N N    . VAL   A 1 96  ? 27.639 -3.936  -1.606  1.00 9.54  ?  96  VAL   A N    1 
ATOM   1923 C CA   . VAL   A 1 96  ? 27.233 -3.383  -2.890  1.00 10.24 ?  96  VAL   A CA   1 
ATOM   1924 C C    . VAL   A 1 96  ? 26.436 -4.429  -3.659  1.00 10.76 ?  96  VAL   A C    1 
ATOM   1925 O O    . VAL   A 1 96  ? 26.999 -5.375  -4.215  1.00 11.79 ?  96  VAL   A O    1 
ATOM   1926 C CB   . VAL   A 1 96  ? 28.430 -2.901  -3.715  1.00 10.88 ?  96  VAL   A CB   1 
ATOM   1927 C CG1  . VAL   A 1 96  ? 27.927 -2.270  -5.001  1.00 11.10 ?  96  VAL   A CG1  1 
ATOM   1928 C CG2  . VAL   A 1 96  ? 29.279 -1.920  -2.926  1.00 11.30 ?  96  VAL   A CG2  1 
ATOM   1929 H H    . VAL   A 1 96  ? 28.330 -4.458  -1.656  1.00 11.45 ?  96  VAL   A H    1 
ATOM   1930 H HA   . VAL   A 1 96  ? 26.656 -2.623  -2.735  1.00 12.28 ?  96  VAL   A HA   1 
ATOM   1931 H HB   . VAL   A 1 96  ? 28.984 -3.656  -3.952  1.00 13.05 ?  96  VAL   A HB   1 
ATOM   1932 H HG11 . VAL   A 1 96  ? 28.655 -1.780  -5.417  1.00 13.31 ?  96  VAL   A HG11 1 
ATOM   1933 H HG12 . VAL   A 1 96  ? 27.616 -2.966  -5.599  1.00 13.31 ?  96  VAL   A HG12 1 
ATOM   1934 H HG13 . VAL   A 1 96  ? 27.200 -1.660  -4.794  1.00 13.31 ?  96  VAL   A HG13 1 
ATOM   1935 H HG21 . VAL   A 1 96  ? 29.986 -1.577  -3.495  1.00 13.56 ?  96  VAL   A HG21 1 
ATOM   1936 H HG22 . VAL   A 1 96  ? 28.718 -1.184  -2.622  1.00 13.56 ?  96  VAL   A HG22 1 
ATOM   1937 H HG23 . VAL   A 1 96  ? 29.662 -2.376  -2.161  1.00 13.56 ?  96  VAL   A HG23 1 
ATOM   1938 N N    A GLY   A 1 97  ? 25.118 -4.280  -3.665  0.60 10.98 ?  97  GLY   A N    1 
ATOM   1939 N N    B GLY   A 1 97  ? 25.123 -4.249  -3.744  0.40 11.08 ?  97  GLY   A N    1 
ATOM   1940 C CA   A GLY   A 1 97  ? 24.288 -5.018  -4.580  0.60 11.34 ?  97  GLY   A CA   1 
ATOM   1941 C CA   B GLY   A 1 97  ? 24.324 -5.040  -4.648  0.40 11.35 ?  97  GLY   A CA   1 
ATOM   1942 C C    A GLY   A 1 97  ? 24.268 -4.317  -5.922  0.60 11.28 ?  97  GLY   A C    1 
ATOM   1943 C C    B GLY   A 1 97  ? 24.393 -4.487  -6.060  0.40 11.54 ?  97  GLY   A C    1 
ATOM   1944 O O    A GLY   A 1 97  ? 24.519 -3.110  -6.014  0.60 11.47 ?  97  GLY   A O    1 
ATOM   1945 O O    B GLY   A 1 97  ? 24.736 -3.318  -6.272  0.40 12.19 ?  97  GLY   A O    1 
ATOM   1946 H H    A GLY   A 1 97  ? 24.684 -3.745  -3.144  0.60 13.17 ?  97  GLY   A H    1 
ATOM   1947 H H    B GLY   A 1 97  ? 24.675 -3.673  -3.285  0.40 13.29 ?  97  GLY   A H    1 
ATOM   1948 H HA2  A GLY   A 1 97  ? 24.644 -5.910  -4.692  0.60 13.60 ?  97  GLY   A HA2  1 
ATOM   1949 H HA2  B GLY   A 1 97  ? 24.651 -5.953  -4.649  0.40 13.62 ?  97  GLY   A HA2  1 
ATOM   1950 H HA3  A GLY   A 1 97  ? 23.383 -5.077  -4.233  0.60 13.60 ?  97  GLY   A HA3  1 
ATOM   1951 H HA3  B GLY   A 1 97  ? 23.399 -5.041  -4.356  0.40 13.62 ?  97  GLY   A HA3  1 
ATOM   1952 N N    A PRO   A 1 98  ? 23.961 -5.049  -6.990  0.60 10.82 ?  98  PRO   A N    1 
ATOM   1953 N N    B PRO   A 1 98  ? 24.070 -5.312  -7.056  0.40 11.79 ?  98  PRO   A N    1 
ATOM   1954 C CA   A PRO   A 1 98  ? 23.852 -4.412  -8.306  0.60 11.64 ?  98  PRO   A CA   1 
ATOM   1955 C CA   B PRO   A 1 98  ? 24.039 -4.815  -8.437  0.40 12.71 ?  98  PRO   A CA   1 
ATOM   1956 C C    A PRO   A 1 98  ? 22.734 -3.380  -8.331  0.60 11.80 ?  98  PRO   A C    1 
ATOM   1957 C C    B PRO   A 1 98  ? 22.936 -3.787  -8.644  0.40 13.34 ?  98  PRO   A C    1 
ATOM   1958 O O    A PRO   A 1 98  ? 21.666 -3.572  -7.746  0.60 11.52 ?  98  PRO   A O    1 
ATOM   1959 O O    B PRO   A 1 98  ? 21.829 -3.908  -8.113  0.40 13.60 ?  98  PRO   A O    1 
ATOM   1960 C CB   A PRO   A 1 98  ? 23.548 -5.587  -9.243  0.60 11.76 ?  98  PRO   A CB   1 
ATOM   1961 C CB   B PRO   A 1 98  ? 23.783 -6.081  -9.267  0.40 12.56 ?  98  PRO   A CB   1 
ATOM   1962 C CG   A PRO   A 1 98  ? 22.909 -6.617  -8.362  0.60 12.19 ?  98  PRO   A CG   1 
ATOM   1963 C CG   B PRO   A 1 98  ? 23.136 -7.039  -8.313  0.40 12.63 ?  98  PRO   A CG   1 
ATOM   1964 C CD   A PRO   A 1 98  ? 23.633 -6.485  -7.043  0.60 11.47 ?  98  PRO   A CD   1 
ATOM   1965 C CD   B PRO   A 1 98  ? 23.780 -6.755  -6.983  0.40 11.92 ?  98  PRO   A CD   1 
ATOM   1966 H HA   A PRO   A 1 98  ? 24.692 -3.998  -8.550  0.60 13.97 ?  98  PRO   A HA   1 
ATOM   1967 H HA   B PRO   A 1 98  ? 24.897 -4.433  -8.684  0.40 15.25 ?  98  PRO   A HA   1 
ATOM   1968 H HB2  A PRO   A 1 98  ? 22.935 -5.301  -9.935  0.60 14.11 ?  98  PRO   A HB2  1 
ATOM   1969 H HB2  B PRO   A 1 98  ? 23.187 -5.873  -10.004 0.40 15.07 ?  98  PRO   A HB2  1 
ATOM   1970 H HB3  A PRO   A 1 98  ? 24.372 -5.924  -9.622  0.60 14.11 ?  98  PRO   A HB3  1 
ATOM   1971 H HB3  B PRO   A 1 98  ? 24.624 -6.436  -9.594  0.40 15.07 ?  98  PRO   A HB3  1 
ATOM   1972 H HG2  A PRO   A 1 98  ? 21.964 -6.423  -8.256  0.60 14.62 ?  98  PRO   A HG2  1 
ATOM   1973 H HG2  B PRO   A 1 98  ? 22.181 -6.870  -8.275  0.40 15.15 ?  98  PRO   A HG2  1 
ATOM   1974 H HG3  A PRO   A 1 98  ? 23.041 -7.501  -8.738  0.60 14.62 ?  98  PRO   A HG3  1 
ATOM   1975 H HG3  B PRO   A 1 98  ? 23.312 -7.951  -8.594  0.40 15.15 ?  98  PRO   A HG3  1 
ATOM   1976 H HD2  A PRO   A 1 98  ? 23.048 -6.736  -6.306  0.60 13.76 ?  98  PRO   A HD2  1 
ATOM   1977 H HD2  B PRO   A 1 98  ? 23.162 -6.944  -6.259  0.40 14.30 ?  98  PRO   A HD2  1 
ATOM   1978 H HD3  A PRO   A 1 98  ? 24.447 -7.013  -7.042  0.60 13.76 ?  98  PRO   A HD3  1 
ATOM   1979 H HD3  B PRO   A 1 98  ? 24.602 -7.265  -6.889  0.40 14.30 ?  98  PRO   A HD3  1 
ATOM   1980 N N    A ASN   A 1 99  ? 22.995 -2.274  -9.022  0.60 12.14 ?  99  ASN   A N    1 
ATOM   1981 N N    B ASN   A 1 99  ? 23.253 -2.763  -9.430  0.40 14.00 ?  99  ASN   A N    1 
ATOM   1982 C CA   A ASN   A 1 99  ? 22.014 -1.217  -9.235  0.60 12.58 ?  99  ASN   A CA   1 
ATOM   1983 C CA   B ASN   A 1 99  ? 22.312 -1.711  -9.798  0.40 15.45 ?  99  ASN   A CA   1 
ATOM   1984 C C    A ASN   A 1 99  ? 21.455 -1.374  -10.644 0.60 13.71 ?  99  ASN   A C    1 
ATOM   1985 C C    B ASN   A 1 99  ? 21.807 -2.024  -11.202 0.40 16.13 ?  99  ASN   A C    1 
ATOM   1986 O O    A ASN   A 1 99  ? 22.132 -1.058  -11.629 0.60 14.99 ?  99  ASN   A O    1 
ATOM   1987 O O    B ASN   A 1 99  ? 22.533 -1.840  -12.183 0.40 15.67 ?  99  ASN   A O    1 
ATOM   1988 C CB   A ASN   A 1 99  ? 22.662 0.153   -9.054  0.60 13.06 ?  99  ASN   A CB   1 
ATOM   1989 C CB   B ASN   A 1 99  ? 23.019 -0.358  -9.769  0.40 16.34 ?  99  ASN   A CB   1 
ATOM   1990 C CG   A ASN   A 1 99  ? 21.649 1.295   -9.053  0.60 13.98 ?  99  ASN   A CG   1 
ATOM   1991 C CG   B ASN   A 1 99  ? 22.095 0.798   -10.091 0.40 17.54 ?  99  ASN   A CG   1 
ATOM   1992 O OD1  A ASN   A 1 99  ? 20.655 1.264   -9.777  0.60 14.58 ?  99  ASN   A OD1  1 
ATOM   1993 O OD1  B ASN   A 1 99  ? 21.005 0.611   -10.629 0.40 17.52 ?  99  ASN   A OD1  1 
ATOM   1994 N ND2  A ASN   A 1 99  ? 21.902 2.303   -8.233  0.60 14.46 ?  99  ASN   A ND2  1 
ATOM   1995 N ND2  B ASN   A 1 99  ? 22.538 2.010   -9.773  0.40 18.80 ?  99  ASN   A ND2  1 
ATOM   1996 H H    A ASN   A 1 99  ? 23.761 -2.108  -9.371  0.60 14.57 ?  99  ASN   A H    1 
ATOM   1997 H H    B ASN   A 1 99  ? 24.034 -2.653  -9.771  0.40 16.79 ?  99  ASN   A H    1 
ATOM   1998 H HA   A ASN   A 1 99  ? 21.288 -1.312  -8.593  0.60 15.09 ?  99  ASN   A HA   1 
ATOM   1999 H HA   B ASN   A 1 99  ? 21.560 -1.701  -9.182  0.40 18.54 ?  99  ASN   A HA   1 
ATOM   2000 H HB2  A ASN   A 1 99  ? 23.139 0.169   -8.210  0.60 15.67 ?  99  ASN   A HB2  1 
ATOM   2001 H HB2  B ASN   A 1 99  ? 23.385 -0.216  -8.884  0.40 19.60 ?  99  ASN   A HB2  1 
ATOM   2002 H HB3  A ASN   A 1 99  ? 23.279 0.304   -9.788  0.60 15.67 ?  99  ASN   A HB3  1 
ATOM   2003 H HB3  B ASN   A 1 99  ? 23.730 -0.365  -10.428 0.40 19.60 ?  99  ASN   A HB3  1 
ATOM   2004 H HD21 A ASN   A 1 99  ? 21.360 2.967   -8.192  0.60 17.34 ?  99  ASN   A HD21 1 
ATOM   2005 H HD21 B ASN   A 1 99  ? 22.055 2.702   -9.934  0.40 22.56 ?  99  ASN   A HD21 1 
ATOM   2006 H HD22 A ASN   A 1 99  ? 22.609 2.291   -7.742  0.60 17.34 ?  99  ASN   A HD22 1 
ATOM   2007 H HD22 B ASN   A 1 99  ? 23.311 2.101   -9.405  0.40 22.56 ?  99  ASN   A HD22 1 
ATOM   2008 N N    A VAL   A 1 100 ? 20.212 -1.862  -10.733 0.60 14.57 ?  100 VAL   A N    1 
ATOM   2009 N N    B VAL   A 1 100 ? 20.563 -2.500  -11.300 0.40 18.23 ?  100 VAL   A N    1 
ATOM   2010 C CA   A VAL   A 1 100 ? 19.583 -2.097  -12.030 0.60 16.73 ?  100 VAL   A CA   1 
ATOM   2011 C CA   B VAL   A 1 100 ? 20.039 -2.910  -12.598 0.40 20.40 ?  100 VAL   A CA   1 
ATOM   2012 C C    A VAL   A 1 100 ? 19.464 -0.800  -12.814 0.60 17.28 ?  100 VAL   A C    1 
ATOM   2013 C C    B VAL   A 1 100 ? 19.840 -1.726  -13.537 0.40 20.94 ?  100 VAL   A C    1 
ATOM   2014 O O    A VAL   A 1 100 ? 19.535 -0.802  -14.049 0.60 18.18 ?  100 VAL   A O    1 
ATOM   2015 O O    B VAL   A 1 100 ? 19.740 -1.922  -14.753 0.40 20.94 ?  100 VAL   A O    1 
ATOM   2016 C CB   A VAL   A 1 100 ? 18.220 -2.802  -11.845 0.60 18.23 ?  100 VAL   A CB   1 
ATOM   2017 C CB   B VAL   A 1 100 ? 18.749 -3.739  -12.449 0.40 22.47 ?  100 VAL   A CB   1 
ATOM   2018 C CG1  A VAL   A 1 100 ? 17.548 -3.057  -13.193 0.60 19.26 ?  100 VAL   A CG1  1 
ATOM   2019 C CG1  B VAL   A 1 100 ? 17.525 -2.835  -12.458 0.40 23.26 ?  100 VAL   A CG1  1 
ATOM   2020 C CG2  A VAL   A 1 100 ? 18.402 -4.111  -11.092 0.60 18.98 ?  100 VAL   A CG2  1 
ATOM   2021 C CG2  B VAL   A 1 100 ? 18.666 -4.787  -13.550 0.40 23.23 ?  100 VAL   A CG2  1 
ATOM   2022 H H    A VAL   A 1 100 ? 19.712 -2.063  -10.057 0.60 17.48 ?  100 VAL   A H    1 
ATOM   2023 H H    B VAL   A 1 100 ? 20.016 -2.598  -10.643 0.40 21.86 ?  100 VAL   A H    1 
ATOM   2024 H HA   A VAL   A 1 100 ? 20.144 -2.694  -12.543 0.60 20.07 ?  100 VAL   A HA   1 
ATOM   2025 H HA   B VAL   A 1 100 ? 20.693 -3.486  -13.013 0.40 24.47 ?  100 VAL   A HA   1 
ATOM   2026 H HB   A VAL   A 1 100 ? 17.633 -2.235  -11.322 0.60 21.87 ?  100 VAL   A HB   1 
ATOM   2027 H HB   B VAL   A 1 100 ? 18.772 -4.201  -11.599 0.40 26.95 ?  100 VAL   A HB   1 
ATOM   2028 H HG11 A VAL   A 1 100 ? 16.780 -3.636  -13.058 0.60 23.11 ?  100 VAL   A HG11 1 
ATOM   2029 H HG11 B VAL   A 1 100 ? 16.778 -3.313  -12.063 0.40 27.91 ?  100 VAL   A HG11 1 
ATOM   2030 H HG12 A VAL   A 1 100 ? 17.260 -2.211  -13.570 0.60 23.11 ?  100 VAL   A HG12 1 
ATOM   2031 H HG12 B VAL   A 1 100 ? 17.718 -2.038  -11.942 0.40 27.91 ?  100 VAL   A HG12 1 
ATOM   2032 H HG13 A VAL   A 1 100 ? 18.183 -3.487  -13.786 0.60 23.11 ?  100 VAL   A HG13 1 
ATOM   2033 H HG13 B VAL   A 1 100 ? 17.314 -2.593  -13.374 0.40 27.91 ?  100 VAL   A HG13 1 
ATOM   2034 H HG21 A VAL   A 1 100 ? 17.558 -4.588  -11.076 0.60 22.77 ?  100 VAL   A HG21 1 
ATOM   2035 H HG21 B VAL   A 1 100 ? 17.838 -5.283  -13.451 0.40 27.87 ?  100 VAL   A HG21 1 
ATOM   2036 H HG22 A VAL   A 1 100 ? 19.075 -4.644  -11.543 0.60 22.77 ?  100 VAL   A HG22 1 
ATOM   2037 H HG22 B VAL   A 1 100 ? 18.686 -4.344  -14.412 0.40 27.87 ?  100 VAL   A HG22 1 
ATOM   2038 H HG23 A VAL   A 1 100 ? 18.687 -3.916  -10.185 0.60 22.77 ?  100 VAL   A HG23 1 
ATOM   2039 H HG23 B VAL   A 1 100 ? 19.423 -5.390  -13.470 0.40 27.87 ?  100 VAL   A HG23 1 
ATOM   2040 N N    A ASN   A 1 101 ? 19.288 0.324   -12.124 0.60 18.02 ?  101 ASN   A N    1 
ATOM   2041 N N    B ASN   A 1 101 ? 19.773 -0.499  -13.012 0.40 21.68 ?  101 ASN   A N    1 
ATOM   2042 C CA   A ASN   A 1 101 ? 19.209 1.603   -12.816 0.60 19.23 ?  101 ASN   A CA   1 
ATOM   2043 C CA   B ASN   A 1 101 ? 19.692 0.668   -13.883 0.40 22.70 ?  101 ASN   A CA   1 
ATOM   2044 C C    A ASN   A 1 101 ? 20.559 2.063   -13.365 0.60 21.58 ?  101 ASN   A C    1 
ATOM   2045 C C    B ASN   A 1 101 ? 21.020 0.964   -14.567 0.40 23.94 ?  101 ASN   A C    1 
ATOM   2046 O O    A ASN   A 1 101 ? 20.613 3.115   -14.014 0.60 23.27 ?  101 ASN   A O    1 
ATOM   2047 O O    B ASN   A 1 101 ? 21.030 1.616   -15.617 0.40 24.38 ?  101 ASN   A O    1 
ATOM   2048 C CB   A ASN   A 1 101 ? 18.568 2.643   -11.896 0.60 18.99 ?  101 ASN   A CB   1 
ATOM   2049 C CB   B ASN   A 1 101 ? 19.228 1.892   -13.092 0.40 23.03 ?  101 ASN   A CB   1 
ATOM   2050 C CG   A ASN   A 1 101 ? 17.196 2.201   -11.399 0.60 18.81 ?  101 ASN   A CG   1 
ATOM   2051 C CG   B ASN   A 1 101 ? 17.883 1.676   -12.431 0.40 23.50 ?  101 ASN   A CG   1 
ATOM   2052 O OD1  A ASN   A 1 101 ? 16.391 1.659   -12.162 0.60 18.32 ?  101 ASN   A OD1  1 
ATOM   2053 O OD1  B ASN   A 1 101 ? 17.069 0.876   -12.895 0.40 24.01 ?  101 ASN   A OD1  1 
ATOM   2054 N ND2  A ASN   A 1 101 ? 16.933 2.410   -10.113 0.60 18.59 ?  101 ASN   A ND2  1 
ATOM   2055 N ND2  B ASN   A 1 101 ? 17.643 2.387   -11.340 0.40 23.68 ?  101 ASN   A ND2  1 
ATOM   2056 H H    A ASN   A 1 101 ? 19.205 0.371   -11.271 0.60 21.62 ?  101 ASN   A H    1 
ATOM   2057 H H    B ASN   A 1 101 ? 19.768 -0.318  -12.171 0.40 26.01 ?  101 ASN   A H    1 
ATOM   2058 H HA   A ASN   A 1 101 ? 18.621 1.497   -13.576 0.60 23.07 ?  101 ASN   A HA   1 
ATOM   2059 H HA   B ASN   A 1 101 ? 19.032 0.497   -14.573 0.40 27.23 ?  101 ASN   A HA   1 
ATOM   2060 H HB2  A ASN   A 1 101 ? 19.136 2.788   -11.126 0.60 22.78 ?  101 ASN   A HB2  1 
ATOM   2061 H HB2  B ASN   A 1 101 ? 19.878 2.087   -12.400 0.40 27.63 ?  101 ASN   A HB2  1 
ATOM   2062 H HB3  A ASN   A 1 101 ? 18.456 3.477   -12.388 0.60 22.78 ?  101 ASN   A HB3  1 
ATOM   2063 H HB3  B ASN   A 1 101 ? 19.150 2.649   -13.697 0.40 27.63 ?  101 ASN   A HB3  1 
ATOM   2064 H HD21 A ASN   A 1 101 ? 16.171 2.178   -9.786  0.60 22.30 ?  101 ASN   A HD21 1 
ATOM   2065 H HD21 B ASN   A 1 101 ? 16.892 2.303   -10.931 0.40 28.41 ?  101 ASN   A HD21 1 
ATOM   2066 H HD22 A ASN   A 1 101 ? 17.519 2.786   -9.609  0.60 22.30 ?  101 ASN   A HD22 1 
ATOM   2067 H HD22 B ASN   A 1 101 ? 18.234 2.939   -11.047 0.40 28.41 ?  101 ASN   A HD22 1 
ATOM   2068 N N    A LYS   A 1 102 ? 21.630 1.295   -13.140 0.60 22.55 ?  102 LYS   A N    1 
ATOM   2069 N N    B LYS   A 1 102 ? 22.133 0.513   -13.993 0.40 24.65 ?  102 LYS   A N    1 
ATOM   2070 C CA   A LYS   A 1 102 ? 22.914 1.494   -13.801 0.60 23.53 ?  102 LYS   A CA   1 
ATOM   2071 C CA   B LYS   A 1 102 ? 23.448 0.624   -14.613 0.40 25.09 ?  102 LYS   A CA   1 
ATOM   2072 C C    A LYS   A 1 102 ? 23.230 0.400   -14.812 0.60 24.53 ?  102 LYS   A C    1 
ATOM   2073 C C    B LYS   A 1 102 ? 23.786 -0.568  -15.502 0.40 24.18 ?  102 LYS   A C    1 
ATOM   2074 O O    A LYS   A 1 102 ? 24.300 0.439   -15.427 0.60 25.23 ?  102 LYS   A O    1 
ATOM   2075 O O    B LYS   A 1 102 ? 24.921 -0.668  -15.979 0.40 24.27 ?  102 LYS   A O    1 
ATOM   2076 C CB   A LYS   A 1 102 ? 24.051 1.555   -12.772 0.60 23.93 ?  102 LYS   A CB   1 
ATOM   2077 C CB   B LYS   A 1 102 ? 24.536 0.760   -13.543 0.40 26.51 ?  102 LYS   A CB   1 
ATOM   2078 C CG   A LYS   A 1 102 ? 23.936 2.670   -11.756 0.60 24.35 ?  102 LYS   A CG   1 
ATOM   2079 C CG   B LYS   A 1 102 ? 24.774 2.172   -13.045 0.40 28.04 ?  102 LYS   A CG   1 
ATOM   2080 C CD   A LYS   A 1 102 ? 25.117 2.643   -10.793 0.60 25.32 ?  102 LYS   A CD   1 
ATOM   2081 C CD   B LYS   A 1 102 ? 26.163 2.291   -12.435 0.40 29.56 ?  102 LYS   A CD   1 
ATOM   2082 C CE   A LYS   A 1 102 ? 25.003 3.724   -9.732  0.60 26.17 ?  102 LYS   A CE   1 
ATOM   2083 C CE   B LYS   A 1 102 ? 26.388 3.657   -11.815 0.40 30.70 ?  102 LYS   A CE   1 
ATOM   2084 N NZ   A LYS   A 1 102 ? 26.103 3.633   -8.728  0.60 26.71 ?  102 LYS   A NZ   1 
ATOM   2085 N NZ   B LYS   A 1 102 ? 27.271 3.569   -10.619 0.40 31.38 ?  102 LYS   A NZ   1 
ATOM   2086 H H    A LYS   A 1 102 ? 21.634 0.626   -12.596 0.60 27.05 ?  102 LYS   A H    1 
ATOM   2087 H H    B LYS   A 1 102 ? 22.148 0.139   -13.219 0.40 29.57 ?  102 LYS   A H    1 
ATOM   2088 H HA   A LYS   A 1 102 ? 22.899 2.333   -14.277 0.60 28.23 ?  102 LYS   A HA   1 
ATOM   2089 H HA   B LYS   A 1 102 ? 23.466 1.428   -15.155 0.40 30.10 ?  102 LYS   A HA   1 
ATOM   2090 H HB2  A LYS   A 1 102 ? 24.073 0.716   -12.286 0.60 28.71 ?  102 LYS   A HB2  1 
ATOM   2091 H HB2  B LYS   A 1 102 ? 24.288 0.218   -12.778 0.40 31.81 ?  102 LYS   A HB2  1 
ATOM   2092 H HB3  A LYS   A 1 102 ? 24.889 1.676   -13.247 0.60 28.71 ?  102 LYS   A HB3  1 
ATOM   2093 H HB3  B LYS   A 1 102 ? 25.374 0.437   -13.910 0.40 31.81 ?  102 LYS   A HB3  1 
ATOM   2094 H HG2  A LYS   A 1 102 ? 23.933 3.525   -12.215 0.60 29.21 ?  102 LYS   A HG2  1 
ATOM   2095 H HG2  B LYS   A 1 102 ? 24.709 2.794   -13.786 0.40 33.64 ?  102 LYS   A HG2  1 
ATOM   2096 H HG3  A LYS   A 1 102 ? 23.120 2.557   -11.245 0.60 29.21 ?  102 LYS   A HG3  1 
ATOM   2097 H HG3  B LYS   A 1 102 ? 24.120 2.388   -12.361 0.40 33.64 ?  102 LYS   A HG3  1 
ATOM   2098 H HD2  A LYS   A 1 102 ? 25.146 1.781   -10.347 0.60 30.38 ?  102 LYS   A HD2  1 
ATOM   2099 H HD2  B LYS   A 1 102 ? 26.269 1.622   -11.742 0.40 35.47 ?  102 LYS   A HD2  1 
ATOM   2100 H HD3  A LYS   A 1 102 ? 25.938 2.789   -11.290 0.60 30.38 ?  102 LYS   A HD3  1 
ATOM   2101 H HD3  B LYS   A 1 102 ? 26.830 2.160   -13.130 0.40 35.47 ?  102 LYS   A HD3  1 
ATOM   2102 H HE2  A LYS   A 1 102 ? 25.053 4.595   -10.158 0.60 31.40 ?  102 LYS   A HE2  1 
ATOM   2103 H HE2  B LYS   A 1 102 ? 26.814 4.238   -12.465 0.40 36.83 ?  102 LYS   A HE2  1 
ATOM   2104 H HE3  A LYS   A 1 102 ? 24.158 3.628   -9.267  0.60 31.40 ?  102 LYS   A HE3  1 
ATOM   2105 H HE3  B LYS   A 1 102 ? 25.535 4.028   -11.540 0.40 36.83 ?  102 LYS   A HE3  1 
ATOM   2106 H HZ1  A LYS   A 1 102 ? 26.014 4.275   -8.119  0.60 32.05 ?  102 LYS   A HZ1  1 
ATOM   2107 H HZ1  B LYS   A 1 102 ? 27.390 4.377   -10.268 0.40 37.65 ?  102 LYS   A HZ1  1 
ATOM   2108 H HZ2  A LYS   A 1 102 ? 26.076 2.842   -8.320  0.60 32.05 ?  102 LYS   A HZ2  1 
ATOM   2109 H HZ2  B LYS   A 1 102 ? 26.898 3.040   -10.006 0.40 37.65 ?  102 LYS   A HZ2  1 
ATOM   2110 H HZ3  A LYS   A 1 102 ? 26.891 3.723   -9.131  0.60 32.05 ?  102 LYS   A HZ3  1 
ATOM   2111 H HZ3  B LYS   A 1 102 ? 28.062 3.232   -10.848 0.40 37.65 ?  102 LYS   A HZ3  1 
ATOM   2112 N N    A GLY   A 1 103 ? 22.341 -0.577  -14.991 0.60 25.52 ?  103 GLY   A N    1 
ATOM   2113 N N    B GLY   A 1 103 ? 22.840 -1.475  -15.728 0.40 23.44 ?  103 GLY   A N    1 
ATOM   2114 C CA   A GLY   A 1 103 ? 22.581 -1.664  -15.920 0.60 26.30 ?  103 GLY   A CA   1 
ATOM   2115 C CA   B GLY   A 1 103 ? 23.117 -2.672  -16.495 0.40 22.75 ?  103 GLY   A CA   1 
ATOM   2116 C C    A GLY   A 1 103 ? 23.443 -2.782  -15.381 0.60 26.93 ?  103 GLY   A C    1 
ATOM   2117 C C    B GLY   A 1 103 ? 23.870 -3.747  -15.747 0.40 21.70 ?  103 GLY   A C    1 
ATOM   2118 O O    A GLY   A 1 103 ? 24.007 -3.547  -16.169 0.60 27.95 ?  103 GLY   A O    1 
ATOM   2119 O O    B GLY   A 1 103 ? 24.334 -4.706  -16.375 0.40 22.07 ?  103 GLY   A O    1 
ATOM   2120 H H    A GLY   A 1 103 ? 21.590 -0.637  -14.581 0.60 30.62 ?  103 GLY   A H    1 
ATOM   2121 H H    B GLY   A 1 103 ? 22.030 -1.410  -15.452 0.40 28.12 ?  103 GLY   A H    1 
ATOM   2122 H HA2  A GLY   A 1 103 ? 21.728 -2.040  -16.200 0.60 31.55 ?  103 GLY   A HA2  1 
ATOM   2123 H HA2  B GLY   A 1 103 ? 22.282 -3.051  -16.804 0.40 27.30 ?  103 GLY   A HA2  1 
ATOM   2124 H HA3  A GLY   A 1 103 ? 23.025 -1.317  -16.708 0.60 31.55 ?  103 GLY   A HA3  1 
ATOM   2125 H HA3  B GLY   A 1 103 ? 23.646 -2.427  -17.271 0.40 27.30 ?  103 GLY   A HA3  1 
ATOM   2126 N N    A GLU   A 1 104 ? 23.562 -2.904  -14.063 0.60 25.74 ?  104 GLU   A N    1 
ATOM   2127 N N    B GLU   A 1 104 ? 23.999 -3.628  -14.429 0.40 20.06 ?  104 GLU   A N    1 
ATOM   2128 C CA   A GLU   A 1 104 ? 24.444 -3.893  -13.464 0.60 24.80 ?  104 GLU   A CA   1 
ATOM   2129 C CA   B GLU   A 1 104 ? 24.810 -4.561  -13.662 0.40 18.47 ?  104 GLU   A CA   1 
ATOM   2130 C C    A GLU   A 1 104 ? 23.763 -5.257  -13.367 0.60 25.46 ?  104 GLU   A C    1 
ATOM   2131 C C    B GLU   A 1 104 ? 24.077 -5.889  -13.492 0.40 18.67 ?  104 GLU   A C    1 
ATOM   2132 O O    A GLU   A 1 104 ? 22.540 -5.363  -13.225 0.60 25.50 ?  104 GLU   A O    1 
ATOM   2133 O O    B GLU   A 1 104 ? 22.862 -5.926  -13.273 0.40 19.00 ?  104 GLU   A O    1 
ATOM   2134 C CB   A GLU   A 1 104 ? 24.931 -3.396  -12.099 0.60 23.41 ?  104 GLU   A CB   1 
ATOM   2135 C CB   B GLU   A 1 104 ? 25.185 -3.944  -12.311 0.40 17.56 ?  104 GLU   A CB   1 
ATOM   2136 C CG   A GLU   A 1 104 ? 25.799 -2.137  -12.244 0.60 22.36 ?  104 GLU   A CG   1 
ATOM   2137 C CG   B GLU   A 1 104 ? 26.063 -2.703  -12.479 0.40 17.63 ?  104 GLU   A CG   1 
ATOM   2138 C CD   A GLU   A 1 104 ? 26.151 -1.426  -10.943 0.60 20.93 ?  104 GLU   A CD   1 
ATOM   2139 C CD   B GLU   A 1 104 ? 26.398 -1.971  -11.192 0.40 17.93 ?  104 GLU   A CD   1 
ATOM   2140 O OE1  A GLU   A 1 104 ? 25.617 -1.783  -9.875  0.60 19.19 ?  104 GLU   A OE1  1 
ATOM   2141 O OE1  B GLU   A 1 104 ? 25.793 -2.262  -10.142 0.40 17.99 ?  104 GLU   A OE1  1 
ATOM   2142 O OE2  A GLU   A 1 104 ? 26.970 -0.480  -11.009 0.60 21.55 -1 104 GLU   A OE2  1 
ATOM   2143 O OE2  B GLU   A 1 104 ? 27.272 -1.074  -11.249 0.40 18.50 -1 104 GLU   A OE2  1 
ATOM   2144 H H    A GLU   A 1 104 ? 23.144 -2.418  -13.494 0.60 30.88 ?  104 GLU   A H    1 
ATOM   2145 H H    B GLU   A 1 104 ? 23.619 -3.016  -13.960 0.40 24.06 ?  104 GLU   A H    1 
ATOM   2146 H HA   A GLU   A 1 104 ? 25.220 -3.997  -14.033 0.60 29.76 ?  104 GLU   A HA   1 
ATOM   2147 H HA   B GLU   A 1 104 ? 25.632 -4.731  -14.148 0.40 22.15 ?  104 GLU   A HA   1 
ATOM   2148 H HB2  A GLU   A 1 104 ? 24.163 -3.183  -11.547 0.60 28.08 ?  104 GLU   A HB2  1 
ATOM   2149 H HB2  B GLU   A 1 104 ? 24.378 -3.684  -11.845 0.40 21.07 ?  104 GLU   A HB2  1 
ATOM   2150 H HB3  A GLU   A 1 104 ? 25.462 -4.093  -11.680 0.60 28.08 ?  104 GLU   A HB3  1 
ATOM   2151 H HB3  B GLU   A 1 104 ? 25.681 -4.597  -11.794 0.40 21.07 ?  104 GLU   A HB3  1 
ATOM   2152 H HG2  A GLU   A 1 104 ? 26.627 -2.390  -12.676 0.60 26.83 ?  104 GLU   A HG2  1 
ATOM   2153 H HG2  B GLU   A 1 104 ? 26.896 -2.967  -12.895 0.40 21.15 ?  104 GLU   A HG2  1 
ATOM   2154 H HG3  A GLU   A 1 104 ? 25.320 -1.500  -12.792 0.60 26.83 ?  104 GLU   A HG3  1 
ATOM   2155 H HG3  B GLU   A 1 104 ? 25.597 -2.067  -13.039 0.40 21.15 ?  104 GLU   A HG3  1 
ATOM   2156 N N    A ASP   A 1 105 ? 24.580 -6.306  -13.458 0.60 26.36 ?  105 ASP   A N    1 
ATOM   2157 N N    B ASP   A 1 105 ? 24.835 -6.979  -13.609 0.40 19.68 ?  105 ASP   A N    1 
ATOM   2158 C CA   A ASP   A 1 105 ? 24.085 -7.672  -13.573 0.60 27.66 ?  105 ASP   A CA   1 
ATOM   2159 C CA   B ASP   A 1 105 ? 24.272 -8.323  -13.664 0.40 20.75 ?  105 ASP   A CA   1 
ATOM   2160 C C    A ASP   A 1 105 ? 23.398 -8.107  -12.282 0.60 26.17 ?  105 ASP   A C    1 
ATOM   2161 C C    B ASP   A 1 105 ? 23.532 -8.656  -12.374 0.40 19.18 ?  105 ASP   A C    1 
ATOM   2162 O O    A ASP   A 1 105 ? 23.990 -8.045  -11.202 0.60 25.24 ?  105 ASP   A O    1 
ATOM   2163 O O    B ASP   A 1 105 ? 24.126 -8.673  -11.291 0.40 16.28 ?  105 ASP   A O    1 
ATOM   2164 C CB   A ASP   A 1 105 ? 25.264 -8.599  -13.871 0.60 30.25 ?  105 ASP   A CB   1 
ATOM   2165 C CB   B ASP   A 1 105 ? 25.416 -9.311  -13.894 0.40 23.32 ?  105 ASP   A CB   1 
ATOM   2166 C CG   A ASP   A 1 105 ? 24.829 -10.000 -14.229 0.60 32.45 ?  105 ASP   A CG   1 
ATOM   2167 C CG   B ASP   A 1 105 ? 24.976 -10.758 -13.823 0.40 25.41 ?  105 ASP   A CG   1 
ATOM   2168 O OD1  A ASP   A 1 105 ? 23.607 -10.234 -14.327 0.60 32.93 ?  105 ASP   A OD1  1 
ATOM   2169 O OD1  B ASP   A 1 105 ? 23.761 -11.027 -13.911 0.40 25.66 ?  105 ASP   A OD1  1 
ATOM   2170 O OD2  A ASP   A 1 105 ? 25.713 -10.864 -14.419 0.60 33.54 -1 105 ASP   A OD2  1 
ATOM   2171 O OD2  B ASP   A 1 105 ? 25.862 -11.629 -13.679 0.40 26.67 -1 105 ASP   A OD2  1 
ATOM   2172 H H    A ASP   A 1 105 ? 25.438 -6.253  -13.455 0.60 31.63 ?  105 ASP   A H    1 
ATOM   2173 H H    B ASP   A 1 105 ? 25.692 -6.964  -13.660 0.40 23.61 ?  105 ASP   A H    1 
ATOM   2174 H HA   A ASP   A 1 105 ? 23.452 -7.742  -14.306 0.60 33.19 ?  105 ASP   A HA   1 
ATOM   2175 H HA   B ASP   A 1 105 ? 23.648 -8.387  -14.406 0.40 24.89 ?  105 ASP   A HA   1 
ATOM   2176 H HB2  A ASP   A 1 105 ? 25.763 -8.252  -14.628 0.60 36.29 ?  105 ASP   A HB2  1 
ATOM   2177 H HB2  B ASP   A 1 105 ? 25.790 -9.160  -14.777 0.40 27.98 ?  105 ASP   A HB2  1 
ATOM   2178 H HB3  A ASP   A 1 105 ? 25.841 -8.645  -13.090 0.60 36.29 ?  105 ASP   A HB3  1 
ATOM   2179 H HB3  B ASP   A 1 105 ? 26.095 -9.170  -13.217 0.40 27.98 ?  105 ASP   A HB3  1 
ATOM   2180 N N    A ILE   A 1 106 ? 22.149 -8.571  -12.400 0.60 25.58 ?  106 ILE   A N    1 
ATOM   2181 N N    B ILE   A 1 106 ? 22.229 -8.930  -12.491 0.40 20.70 ?  106 ILE   A N    1 
ATOM   2182 C CA   A ILE   A 1 106 ? 21.385 -8.966  -11.221 0.60 24.77 ?  106 ILE   A CA   1 
ATOM   2183 C CA   B ILE   A 1 106 ? 21.437 -9.265  -11.315 0.40 21.88 ?  106 ILE   A CA   1 
ATOM   2184 C C    A ILE   A 1 106 ? 21.898 -10.266 -10.617 0.60 23.56 ?  106 ILE   A C    1 
ATOM   2185 C C    B ILE   A 1 106 ? 21.962 -10.516 -10.631 0.40 22.18 ?  106 ILE   A C    1 
ATOM   2186 O O    A ILE   A 1 106 ? 21.654 -10.527 -9.435  0.60 22.45 ?  106 ILE   A O    1 
ATOM   2187 O O    B ILE   A 1 106 ? 21.748 -10.694 -9.427  0.40 21.95 ?  106 ILE   A O    1 
ATOM   2188 C CB   A ILE   A 1 106 ? 19.877 -9.034  -11.543 0.60 26.01 ?  106 ILE   A CB   1 
ATOM   2189 C CB   B ILE   A 1 106 ? 19.936 -9.377  -11.665 0.40 23.22 ?  106 ILE   A CB   1 
ATOM   2190 C CG1  A ILE   A 1 106 ? 19.042 -9.112  -10.259 0.60 26.72 ?  106 ILE   A CG1  1 
ATOM   2191 C CG1  B ILE   A 1 106 ? 19.082 -9.298  -10.397 0.40 24.00 ?  106 ILE   A CG1  1 
ATOM   2192 C CG2  A ILE   A 1 106 ? 19.575 -10.227 -12.435 0.60 26.40 ?  106 ILE   A CG2  1 
ATOM   2193 C CG2  B ILE   A 1 106 ? 19.650 -10.675 -12.389 0.40 23.41 ?  106 ILE   A CG2  1 
ATOM   2194 C CD1  A ILE   A 1 106 ? 19.177 -7.900  -9.357  0.60 27.21 ?  106 ILE   A CD1  1 
ATOM   2195 C CD1  B ILE   A 1 106 ? 19.229 -7.994  -9.640  0.40 24.57 ?  106 ILE   A CD1  1 
ATOM   2196 H H    A ILE   A 1 106 ? 21.730 -8.668  -13.142 0.60 30.69 ?  106 ILE   A H    1 
ATOM   2197 H H    B ILE   A 1 106 ? 21.790 -8.920  -13.229 0.40 24.83 ?  106 ILE   A H    1 
ATOM   2198 H HA   A ILE   A 1 106 ? 21.508 -8.283  -10.549 0.60 29.72 ?  106 ILE   A HA   1 
ATOM   2199 H HA   B ILE   A 1 106 ? 21.538 -8.545  -10.681 0.40 26.25 ?  106 ILE   A HA   1 
ATOM   2200 H HB   A ILE   A 1 106 ? 19.633 -8.227  -12.017 0.60 31.21 ?  106 ILE   A HB   1 
ATOM   2201 H HB   B ILE   A 1 106 ? 19.696 -8.637  -12.245 0.40 27.86 ?  106 ILE   A HB   1 
ATOM   2202 H HG12 A ILE   A 1 106 ? 18.107 -9.192  -10.503 0.60 32.06 ?  106 ILE   A HG12 1 
ATOM   2203 H HG12 B ILE   A 1 106 ? 18.148 -9.392  -10.641 0.40 28.80 ?  106 ILE   A HG12 1 
ATOM   2204 H HG13 A ILE   A 1 106 ? 19.315 -9.891  -9.751  0.60 32.06 ?  106 ILE   A HG13 1 
ATOM   2205 H HG13 B ILE   A 1 106 ? 19.340 -10.017 -9.800  0.40 28.80 ?  106 ILE   A HG13 1 
ATOM   2206 H HG21 A ILE   A 1 106 ? 18.671 -10.141 -12.776 0.60 31.67 ?  106 ILE   A HG21 1 
ATOM   2207 H HG21 B ILE   A 1 106 ? 18.782 -10.611 -12.816 0.40 28.09 ?  106 ILE   A HG21 1 
ATOM   2208 H HG22 A ILE   A 1 106 ? 20.207 -10.237 -13.170 0.60 31.67 ?  106 ILE   A HG22 1 
ATOM   2209 H HG22 B ILE   A 1 106 ? 20.339 -10.819 -13.054 0.40 28.09 ?  106 ILE   A HG22 1 
ATOM   2210 H HG23 A ILE   A 1 106 ? 19.656 -11.042 -11.915 0.60 31.67 ?  106 ILE   A HG23 1 
ATOM   2211 H HG23 B ILE   A 1 106 ? 19.651 -11.401 -11.746 0.40 28.09 ?  106 ILE   A HG23 1 
ATOM   2212 H HD11 A ILE   A 1 106 ? 18.462 -7.914  -8.703  0.60 32.64 ?  106 ILE   A HD11 1 
ATOM   2213 H HD11 B ILE   A 1 106 ? 18.468 -7.884  -9.052  0.40 29.48 ?  106 ILE   A HD11 1 
ATOM   2214 H HD12 A ILE   A 1 106 ? 20.036 -7.934  -8.907  0.60 32.64 ?  106 ILE   A HD12 1 
ATOM   2215 H HD12 B ILE   A 1 106 ? 20.048 -8.020  -9.118  0.40 29.48 ?  106 ILE   A HD12 1 
ATOM   2216 H HD13 A ILE   A 1 106 ? 19.116 -7.096  -9.896  0.60 32.64 ?  106 ILE   A HD13 1 
ATOM   2217 H HD13 B ILE   A 1 106 ? 19.265 -7.262  -10.276 0.40 29.48 ?  106 ILE   A HD13 1 
ATOM   2218 N N    A GLN   A 1 107 ? 22.629 -11.078 -11.391 0.60 24.44 ?  107 GLN   A N    1 
ATOM   2219 N N    B GLN   A 1 107 ? 22.664 -11.385 -11.366 0.40 22.92 ?  107 GLN   A N    1 
ATOM   2220 C CA   A GLN   A 1 107 ? 23.195 -12.314 -10.855 0.60 26.35 ?  107 GLN   A CA   1 
ATOM   2221 C CA   B GLN   A 1 107 ? 23.304 -12.530 -10.733 0.40 24.72 ?  107 GLN   A CA   1 
ATOM   2222 C C    A GLN   A 1 107 ? 24.162 -12.031 -9.711  0.60 23.85 ?  107 GLN   A C    1 
ATOM   2223 C C    B GLN   A 1 107 ? 24.324 -12.106 -9.686  0.40 22.93 ?  107 GLN   A C    1 
ATOM   2224 O O    A GLN   A 1 107 ? 24.332 -12.864 -8.814  0.60 24.64 ?  107 GLN   A O    1 
ATOM   2225 O O    B GLN   A 1 107 ? 24.694 -12.919 -8.832  0.40 23.60 ?  107 GLN   A O    1 
ATOM   2226 C CB   A GLN   A 1 107 ? 23.893 -13.091 -11.976 0.60 30.77 ?  107 GLN   A CB   1 
ATOM   2227 C CB   B GLN   A 1 107 ? 23.959 -13.431 -11.785 0.40 28.16 ?  107 GLN   A CB   1 
ATOM   2228 C CG   A GLN   A 1 107 ? 23.046 -13.251 -13.235 0.60 35.07 ?  107 GLN   A CG   1 
ATOM   2229 C CG   B GLN   A 1 107 ? 22.982 -13.974 -12.816 0.40 31.40 ?  107 GLN   A CG   1 
ATOM   2230 C CD   A GLN   A 1 107 ? 21.786 -14.059 -12.994 0.60 38.69 ?  107 GLN   A CD   1 
ATOM   2231 C CD   B GLN   A 1 107 ? 21.701 -14.487 -12.187 0.40 34.28 ?  107 GLN   A CD   1 
ATOM   2232 O OE1  A GLN   A 1 107 ? 21.831 -15.138 -12.401 0.60 40.03 ?  107 GLN   A OE1  1 
ATOM   2233 O OE1  B GLN   A 1 107 ? 21.730 -15.327 -11.287 0.40 35.16 ?  107 GLN   A OE1  1 
ATOM   2234 N NE2  A GLN   A 1 107 ? 20.651 -13.539 -13.449 0.60 39.90 ?  107 GLN   A NE2  1 
ATOM   2235 N NE2  B GLN   A 1 107 ? 20.569 -13.965 -12.644 0.40 35.26 ?  107 GLN   A NE2  1 
ATOM   2236 H H    A GLN   A 1 107 ? 22.827 -10.924 -12.213 0.60 29.32 ?  107 GLN   A H    1 
ATOM   2237 H H    B GLN   A 1 107 ? 22.780 -11.333 -12.218 0.40 27.50 ?  107 GLN   A H    1 
ATOM   2238 H HA   A GLN   A 1 107 ? 22.484 -12.870 -10.510 0.60 31.62 ?  107 GLN   A HA   1 
ATOM   2239 H HA   B GLN   A 1 107 ? 22.628 -13.052 -10.280 0.40 29.65 ?  107 GLN   A HA   1 
ATOM   2240 H HB2  A GLN   A 1 107 ? 24.708 -12.628 -12.228 0.60 36.92 ?  107 GLN   A HB2  1 
ATOM   2241 H HB2  B GLN   A 1 107 ? 24.640 -12.927 -12.256 0.40 33.78 ?  107 GLN   A HB2  1 
ATOM   2242 H HB3  A GLN   A 1 107 ? 24.111 -13.984 -11.659 0.60 36.92 ?  107 GLN   A HB3  1 
ATOM   2243 H HB3  B GLN   A 1 107 ? 24.367 -14.190 -11.339 0.40 33.78 ?  107 GLN   A HB3  1 
ATOM   2244 H HG2  A GLN   A 1 107 ? 22.786 -12.376 -13.564 0.60 42.08 ?  107 GLN   A HG2  1 
ATOM   2245 H HG2  B GLN   A 1 107 ? 22.753 -13.267 -13.438 0.40 37.68 ?  107 GLN   A HG2  1 
ATOM   2246 H HG3  A GLN   A 1 107 ? 23.570 -13.710 -13.908 0.60 42.08 ?  107 GLN   A HG3  1 
ATOM   2247 H HG3  B GLN   A 1 107 ? 23.398 -14.712 -13.288 0.40 37.68 ?  107 GLN   A HG3  1 
ATOM   2248 H HE21 A GLN   A 1 107 ? 20.657 -12.784 -13.858 0.60 47.87 ?  107 GLN   A HE21 1 
ATOM   2249 H HE21 B GLN   A 1 107 ? 20.590 -13.377 -13.271 0.40 42.30 ?  107 GLN   A HE21 1 
ATOM   2250 H HE22 A GLN   A 1 107 ? 19.910 -13.961 -13.335 0.60 47.87 ?  107 GLN   A HE22 1 
ATOM   2251 H HE22 B GLN   A 1 107 ? 19.816 -14.216 -12.315 0.40 42.30 ?  107 GLN   A HE22 1 
ATOM   2252 N N    . LEU   A 1 108 ? 24.780 -10.851 -9.716  1.00 20.51 ?  108 LEU   A N    1 
ATOM   2253 C CA   . LEU   A 1 108 ? 25.684 -10.408 -8.667  1.00 17.07 ?  108 LEU   A CA   1 
ATOM   2254 C C    . LEU   A 1 108 ? 24.977 -10.221 -7.335  1.00 14.49 ?  108 LEU   A C    1 
ATOM   2255 O O    . LEU   A 1 108 ? 25.655 -10.050 -6.319  1.00 14.93 ?  108 LEU   A O    1 
ATOM   2256 C CB   . LEU   A 1 108 ? 26.393 -9.115  -9.089  1.00 17.00 ?  108 LEU   A CB   1 
ATOM   2257 C CG   . LEU   A 1 108 ? 27.419 -9.315  -10.208 1.00 18.52 ?  108 LEU   A CG   1 
ATOM   2258 C CD1  . LEU   A 1 108 ? 27.915 -7.983  -10.749 1.00 19.42 ?  108 LEU   A CD1  1 
ATOM   2259 C CD2  . LEU   A 1 108 ? 28.597 -10.151 -9.721  1.00 20.15 ?  108 LEU   A CD2  1 
ATOM   2260 H H    A LEU   A 1 108 ? 24.683 -10.275 -10.338 0.60 24.60 ?  108 LEU   A H    1 
ATOM   2261 H H    B LEU   A 1 108 ? 24.600 -10.272 -10.316 0.40 24.60 ?  108 LEU   A H    1 
ATOM   2262 H HA   . LEU   A 1 108 ? 26.362 -11.086 -8.531  1.00 20.48 ?  108 LEU   A HA   1 
ATOM   2263 H HB2  . LEU   A 1 108 ? 25.728 -8.484  -9.410  1.00 20.40 ?  108 LEU   A HB2  1 
ATOM   2264 H HB3  . LEU   A 1 108 ? 26.857 -8.745  -8.325  1.00 20.40 ?  108 LEU   A HB3  1 
ATOM   2265 H HG   . LEU   A 1 108 ? 26.998 -9.796  -10.939 1.00 22.21 ?  108 LEU   A HG   1 
ATOM   2266 H HD11 . LEU   A 1 108 ? 28.538 -8.150  -11.478 1.00 23.30 ?  108 LEU   A HD11 1 
ATOM   2267 H HD12 . LEU   A 1 108 ? 27.159 -7.471  -11.074 1.00 23.30 ?  108 LEU   A HD12 1 
ATOM   2268 H HD13 . LEU   A 1 108 ? 28.364 -7.500  -10.038 1.00 23.30 ?  108 LEU   A HD13 1 
ATOM   2269 H HD21 . LEU   A 1 108 ? 29.312 -10.094 -10.367 1.00 24.17 ?  108 LEU   A HD21 1 
ATOM   2270 H HD22 . LEU   A 1 108 ? 28.891 -9.804  -8.864  1.00 24.17 ?  108 LEU   A HD22 1 
ATOM   2271 H HD23 . LEU   A 1 108 ? 28.309 -11.073 -9.621  1.00 24.17 ?  108 LEU   A HD23 1 
ATOM   2272 N N    . LEU   A 1 109 ? 23.645 -10.275 -7.305  1.00 13.84 ?  109 LEU   A N    1 
ATOM   2273 C CA   . LEU   A 1 109 ? 22.944 -10.147 -6.036  1.00 12.95 ?  109 LEU   A CA   1 
ATOM   2274 C C    . LEU   A 1 109 ? 23.283 -11.301 -5.099  1.00 12.04 ?  109 LEU   A C    1 
ATOM   2275 O O    . LEU   A 1 109 ? 23.417 -11.106 -3.887  1.00 12.58 ?  109 LEU   A O    1 
ATOM   2276 C CB   . LEU   A 1 109 ? 21.441 -10.057 -6.293  1.00 13.64 ?  109 LEU   A CB   1 
ATOM   2277 C CG   . LEU   A 1 109 ? 20.544 -9.779  -5.090  1.00 13.97 ?  109 LEU   A CG   1 
ATOM   2278 C CD1  . LEU   A 1 109 ? 21.004 -8.521  -4.374  1.00 14.26 ?  109 LEU   A CD1  1 
ATOM   2279 C CD2  . LEU   A 1 109 ? 19.086 -9.642  -5.525  1.00 15.35 ?  109 LEU   A CD2  1 
ATOM   2280 H H    . LEU   A 1 109 ? 23.132 -10.383 -7.990  1.00 16.60 ?  109 LEU   A H    1 
ATOM   2281 H HA   . LEU   A 1 109 ? 23.225 -9.323  -5.608  1.00 15.53 ?  109 LEU   A HA   1 
ATOM   2282 H HB2  . LEU   A 1 109 ? 21.285 -9.343  -6.931  1.00 16.36 ?  109 LEU   A HB2  1 
ATOM   2283 H HB3  . LEU   A 1 109 ? 21.147 -10.897 -6.673  1.00 16.36 ?  109 LEU   A HB3  1 
ATOM   2284 H HG   . LEU   A 1 109 ? 20.602 -10.517 -4.466  1.00 16.76 ?  109 LEU   A HG   1 
ATOM   2285 H HD11 . LEU   A 1 109 ? 20.316 -8.227  -3.761  1.00 17.11 ?  109 LEU   A HD11 1 
ATOM   2286 H HD12 . LEU   A 1 109 ? 21.823 -8.712  -3.889  1.00 17.11 ?  109 LEU   A HD12 1 
ATOM   2287 H HD13 . LEU   A 1 109 ? 21.173 -7.825  -5.036  1.00 17.11 ?  109 LEU   A HD13 1 
ATOM   2288 H HD21 . LEU   A 1 109 ? 18.552 -9.344  -4.770  1.00 18.41 ?  109 LEU   A HD21 1 
ATOM   2289 H HD22 . LEU   A 1 109 ? 19.026 -8.992  -6.244  1.00 18.41 ?  109 LEU   A HD22 1 
ATOM   2290 H HD23 . LEU   A 1 109 ? 18.763 -10.505 -5.835  1.00 18.41 ?  109 LEU   A HD23 1 
ATOM   2291 N N    . LYS   A 1 110 ? 23.417 -12.516 -5.634  1.00 12.21 ?  110 LYS   A N    1 
ATOM   2292 C CA   . LYS   A 1 110 ? 23.793 -13.634 -4.774  1.00 12.29 ?  110 LYS   A CA   1 
ATOM   2293 C C    . LYS   A 1 110 ? 25.173 -13.413 -4.166  1.00 11.69 ?  110 LYS   A C    1 
ATOM   2294 O O    . LYS   A 1 110 ? 25.365 -13.612 -2.962  1.00 12.01 ?  110 LYS   A O    1 
ATOM   2295 C CB   . LYS   A 1 110 ? 23.721 -14.957 -5.536  1.00 13.45 ?  110 LYS   A CB   1 
ATOM   2296 C CG   . LYS   A 1 110 ? 23.906 -16.172 -4.628  1.00 13.84 ?  110 LYS   A CG   1 
ATOM   2297 C CD   . LYS   A 1 110 ? 23.686 -17.489 -5.354  1.00 14.20 ?  110 LYS   A CD   1 
ATOM   2298 C CE   . LYS   A 1 110 ? 23.787 -18.679 -4.409  1.00 14.75 ?  110 LYS   A CE   1 
ATOM   2299 N NZ   . LYS   A 1 110 ? 22.611 -18.799 -3.514  1.00 15.42 ?  110 LYS   A NZ   1 
ATOM   2300 H H    . LYS   A 1 110 ? 23.298 -12.714 -6.461  1.00 14.65 ?  110 LYS   A H    1 
ATOM   2301 H HA   . LYS   A 1 110 ? 23.153 -13.687 -4.043  1.00 14.74 ?  110 LYS   A HA   1 
ATOM   2302 H HB2  . LYS   A 1 110 ? 22.855 -15.033 -5.961  1.00 16.14 ?  110 LYS   A HB2  1 
ATOM   2303 H HB3  . LYS   A 1 110 ? 24.425 -14.976 -6.202  1.00 16.14 ?  110 LYS   A HB3  1 
ATOM   2304 H HG2  . LYS   A 1 110 ? 24.809 -16.173 -4.274  1.00 16.60 ?  110 LYS   A HG2  1 
ATOM   2305 H HG3  . LYS   A 1 110 ? 23.266 -16.123 -3.899  1.00 16.60 ?  110 LYS   A HG3  1 
ATOM   2306 H HD2  . LYS   A 1 110 ? 22.802 -17.492 -5.749  1.00 17.03 ?  110 LYS   A HD2  1 
ATOM   2307 H HD3  . LYS   A 1 110 ? 24.363 -17.589 -6.042  1.00 17.03 ?  110 LYS   A HD3  1 
ATOM   2308 H HE2  . LYS   A 1 110 ? 23.854 -19.494 -4.931  1.00 17.69 ?  110 LYS   A HE2  1 
ATOM   2309 H HE3  . LYS   A 1 110 ? 24.579 -18.576 -3.854  1.00 17.69 ?  110 LYS   A HE3  1 
ATOM   2310 H HZ1  . LYS   A 1 110 ? 22.702 -19.500 -2.979  1.00 18.50 ?  110 LYS   A HZ1  1 
ATOM   2311 H HZ2  . LYS   A 1 110 ? 22.530 -18.062 -3.018  1.00 18.50 ?  110 LYS   A HZ2  1 
ATOM   2312 H HZ3  . LYS   A 1 110 ? 21.870 -18.898 -4.000  1.00 18.50 ?  110 LYS   A HZ3  1 
ATOM   2313 N N    . SER   A 1 111 ? 26.137 -12.971 -4.978  1.00 12.26 ?  111 SER   A N    1 
ATOM   2314 C CA   . SER   A 1 111 ? 27.464 -12.661 -4.459  1.00 12.09 ?  111 SER   A CA   1 
ATOM   2315 C C    . SER   A 1 111 ? 27.394 -11.612 -3.354  1.00 12.00 ?  111 SER   A C    1 
ATOM   2316 O O    . SER   A 1 111 ? 28.087 -11.716 -2.336  1.00 12.59 ?  111 SER   A O    1 
ATOM   2317 C CB   . SER   A 1 111 ? 28.355 -12.167 -5.599  1.00 13.57 ?  111 SER   A CB   1 
ATOM   2318 O OG   . SER   A 1 111 ? 28.463 -13.153 -6.616  1.00 15.20 ?  111 SER   A OG   1 
ATOM   2319 H H    . SER   A 1 111 ? 26.035 -12.842 -5.820  1.00 14.71 ?  111 SER   A H    1 
ATOM   2320 H HA   . SER   A 1 111 ? 27.856 -13.469 -4.091  1.00 14.50 ?  111 SER   A HA   1 
ATOM   2321 H HB2  . SER   A 1 111 ? 27.960 -11.372 -5.985  1.00 16.28 ?  111 SER   A HB2  1 
ATOM   2322 H HB3  . SER   A 1 111 ? 29.233 -11.966 -5.244  1.00 16.28 ?  111 SER   A HB3  1 
ATOM   2323 H HG   . SER   A 1 111 ? 28.977 -12.872 -7.230  1.00 18.24 ?  111 SER   A HG   1 
ATOM   2324 N N    . ALA   A 1 112 ? 26.550 -10.593 -3.535  1.00 12.21 ?  112 ALA   A N    1 
ATOM   2325 C CA   . ALA   A 1 112 ? 26.405 -9.556  -2.515  1.00 11.84 ?  112 ALA   A CA   1 
ATOM   2326 C C    . ALA   A 1 112 ? 25.920 -10.154 -1.198  1.00 11.78 ?  112 ALA   A C    1 
ATOM   2327 O O    . ALA   A 1 112 ? 26.470 -9.868  -0.128  1.00 12.10 ?  112 ALA   A O    1 
ATOM   2328 C CB   . ALA   A 1 112 ? 25.449 -8.466  -3.011  1.00 12.17 ?  112 ALA   A CB   1 
ATOM   2329 H H    . ALA   A 1 112 ? 26.061 -10.480 -4.232  1.00 14.64 ?  112 ALA   A H    1 
ATOM   2330 H HA   . ALA   A 1 112 ? 27.268 -9.142  -2.357  1.00 14.20 ?  112 ALA   A HA   1 
ATOM   2331 H HB1  . ALA   A 1 112 ? 25.380 -7.770  -2.331  1.00 14.60 ?  112 ALA   A HB1  1 
ATOM   2332 H HB2  . ALA   A 1 112 ? 25.799 -8.081  -3.831  1.00 14.60 ?  112 ALA   A HB2  1 
ATOM   2333 H HB3  . ALA   A 1 112 ? 24.576 -8.852  -3.173  1.00 14.60 ?  112 ALA   A HB3  1 
ATOM   2334 N N    . TYR   A 1 113 ? 24.883 -10.997 -1.254  1.00 11.78 ?  113 TYR   A N    1 
ATOM   2335 C CA   . TYR   A 1 113 ? 24.370 -11.602 -0.030  1.00 11.62 ?  113 TYR   A CA   1 
ATOM   2336 C C    . TYR   A 1 113 ? 25.370 -12.556 0.617   1.00 11.17 ?  113 TYR   A C    1 
ATOM   2337 O O    . TYR   A 1 113 ? 25.325 -12.748 1.836   1.00 11.76 ?  113 TYR   A O    1 
ATOM   2338 C CB   . TYR   A 1 113 ? 23.054 -12.330 -0.305  1.00 12.15 ?  113 TYR   A CB   1 
ATOM   2339 C CG   . TYR   A 1 113 ? 21.837 -11.432 -0.233  1.00 11.95 ?  113 TYR   A CG   1 
ATOM   2340 C CD1  . TYR   A 1 113 ? 21.471 -10.824 0.963   1.00 12.47 ?  113 TYR   A CD1  1 
ATOM   2341 C CD2  . TYR   A 1 113 ? 21.038 -11.216 -1.346  1.00 12.12 ?  113 TYR   A CD2  1 
ATOM   2342 C CE1  . TYR   A 1 113 ? 20.349 -10.021 1.044   1.00 12.53 ?  113 TYR   A CE1  1 
ATOM   2343 C CE2  . TYR   A 1 113 ? 19.892 -10.412 -1.272  1.00 12.21 ?  113 TYR   A CE2  1 
ATOM   2344 C CZ   . TYR   A 1 113 ? 19.563 -9.824  -0.074  1.00 12.26 ?  113 TYR   A CZ   1 
ATOM   2345 O OH   . TYR   A 1 113 ? 18.441 -9.029  0.026   1.00 13.05 ?  113 TYR   A OH   1 
ATOM   2346 H H    . TYR   A 1 113 ? 24.476 -11.231 -1.977  1.00 14.13 ?  113 TYR   A H    1 
ATOM   2347 H HA   . TYR   A 1 113 ? 24.193 -10.899 0.608   1.00 13.93 ?  113 TYR   A HA   1 
ATOM   2348 H HB2  . TYR   A 1 113 ? 23.081 -12.709 -1.195  1.00 14.57 ?  113 TYR   A HB2  1 
ATOM   2349 H HB3  . TYR   A 1 113 ? 22.940 -13.033 0.352   1.00 14.57 ?  113 TYR   A HB3  1 
ATOM   2350 H HD1  . TYR   A 1 113 ? 21.995 -10.964 1.722   1.00 14.95 ?  113 TYR   A HD1  1 
ATOM   2351 H HD2  . TYR   A 1 113 ? 21.256 -11.622 -2.149  1.00 14.54 ?  113 TYR   A HD2  1 
ATOM   2352 H HE1  . TYR   A 1 113 ? 20.122 -9.626  1.854   1.00 15.03 ?  113 TYR   A HE1  1 
ATOM   2353 H HE2  . TYR   A 1 113 ? 19.359 -10.270 -2.021  1.00 14.65 ?  113 TYR   A HE2  1 
ATOM   2354 H HH   . TYR   A 1 113 ? 18.057 -8.995  -0.725  1.00 15.65 ?  113 TYR   A HH   1 
ATOM   2355 N N    . GLU   A 1 114 ? 26.275 -13.166 -0.164  1.00 11.60 ?  114 GLU   A N    1 
ATOM   2356 C CA   . GLU   A 1 114 ? 27.261 -14.066 0.435   1.00 11.83 ?  114 GLU   A CA   1 
ATOM   2357 C C    . GLU   A 1 114 ? 28.110 -13.356 1.485   1.00 11.55 ?  114 GLU   A C    1 
ATOM   2358 O O    . GLU   A 1 114 ? 28.590 -13.996 2.430   1.00 11.88 ?  114 GLU   A O    1 
ATOM   2359 C CB   . GLU   A 1 114 ? 28.136 -14.711 -0.648  1.00 11.98 ?  114 GLU   A CB   1 
ATOM   2360 C CG   . GLU   A 1 114 ? 27.376 -15.763 -1.432  1.00 12.62 ?  114 GLU   A CG   1 
ATOM   2361 C CD   . GLU   A 1 114 ? 28.082 -16.288 -2.669  1.00 12.76 ?  114 GLU   A CD   1 
ATOM   2362 O OE1  . GLU   A 1 114 ? 29.040 -15.657 -3.161  1.00 13.01 ?  114 GLU   A OE1  1 
ATOM   2363 O OE2  . GLU   A 1 114 ? 27.642 -17.354 -3.159  1.00 14.00 -1 114 GLU   A OE2  1 
ATOM   2364 H H    . GLU   A 1 114 ? 26.338 -13.072 -1.024  1.00 13.92 ?  114 GLU   A H    1 
ATOM   2365 H HA   . GLU   A 1 114 ? 26.788 -14.776 0.881   1.00 14.19 ?  114 GLU   A HA   1 
ATOM   2366 H HB2  . GLU   A 1 114 ? 28.433 -14.029 -1.274  1.00 14.38 ?  114 GLU   A HB2  1 
ATOM   2367 H HB3  . GLU   A 1 114 ? 28.899 -15.137 -0.233  1.00 14.38 ?  114 GLU   A HB3  1 
ATOM   2368 H HG2  . GLU   A 1 114 ? 27.213 -16.523 -0.851  1.00 15.13 ?  114 GLU   A HG2  1 
ATOM   2369 H HG3  . GLU   A 1 114 ? 26.528 -15.388 -1.717  1.00 15.13 ?  114 GLU   A HG3  1 
ATOM   2370 N N    . ASN   A 1 115 ? 28.294 -12.040 1.356   1.00 11.46 ?  115 ASN   A N    1 
ATOM   2371 C CA   . ASN   A 1 115 ? 29.061 -11.312 2.363   1.00 11.54 ?  115 ASN   A CA   1 
ATOM   2372 C C    . ASN   A 1 115 ? 28.439 -11.445 3.747   1.00 11.55 ?  115 ASN   A C    1 
ATOM   2373 O O    . ASN   A 1 115 ? 29.147 -11.364 4.757   1.00 12.09 ?  115 ASN   A O    1 
ATOM   2374 C CB   . ASN   A 1 115 ? 29.162 -9.837  1.984   1.00 12.12 ?  115 ASN   A CB   1 
ATOM   2375 C CG   . ASN   A 1 115 ? 29.970 -9.617  0.726   1.00 12.74 ?  115 ASN   A CG   1 
ATOM   2376 O OD1  . ASN   A 1 115 ? 31.190 -9.720  0.749   1.00 15.81 ?  115 ASN   A OD1  1 
ATOM   2377 N ND2  . ASN   A 1 115 ? 29.300 -9.318  -0.373  1.00 12.27 ?  115 ASN   A ND2  1 
ATOM   2378 H H    . ASN   A 1 115 ? 27.990 -11.551 0.713   1.00 13.74 ?  115 ASN   A H    1 
ATOM   2379 H HA   . ASN   A 1 115 ? 29.958 -11.679 2.402   1.00 13.84 ?  115 ASN   A HA   1 
ATOM   2380 H HB2  . ASN   A 1 115 ? 28.268 -9.486  1.845   1.00 14.53 ?  115 ASN   A HB2  1 
ATOM   2381 H HB3  . ASN   A 1 115 ? 29.594 -9.356  2.712   1.00 14.53 ?  115 ASN   A HB3  1 
ATOM   2382 H HD21 . ASN   A 1 115 ? 29.721 -9.178  -1.109  1.00 14.72 ?  115 ASN   A HD21 1 
ATOM   2383 H HD22 . ASN   A 1 115 ? 28.440 -9.270  -0.355  1.00 14.72 ?  115 ASN   A HD22 1 
ATOM   2384 N N    . PHE   A 1 116 ? 27.111 -11.611 3.821   1.00 11.55 ?  116 PHE   A N    1 
ATOM   2385 C CA   . PHE   A 1 116 ? 26.459 -11.706 5.124   1.00 11.52 ?  116 PHE   A CA   1 
ATOM   2386 C C    . PHE   A 1 116 ? 26.934 -12.935 5.896   1.00 11.48 ?  116 PHE   A C    1 
ATOM   2387 O O    . PHE   A 1 116 ? 26.858 -12.959 7.128   1.00 12.16 ?  116 PHE   A O    1 
ATOM   2388 C CB   . PHE   A 1 116 ? 24.933 -11.839 4.984   1.00 11.82 ?  116 PHE   A CB   1 
ATOM   2389 C CG   . PHE   A 1 116 ? 24.178 -10.596 4.517   1.00 11.45 ?  116 PHE   A CG   1 
ATOM   2390 C CD1  . PHE   A 1 116 ? 24.748 -9.577  3.762   1.00 11.59 ?  116 PHE   A CD1  1 
ATOM   2391 C CD2  . PHE   A 1 116 ? 22.827 -10.491 4.834   1.00 12.00 ?  116 PHE   A CD2  1 
ATOM   2392 C CE1  . PHE   A 1 116 ? 23.980 -8.495  3.341   1.00 11.92 ?  116 PHE   A CE1  1 
ATOM   2393 C CE2  . PHE   A 1 116 ? 22.060 -9.415  4.421   1.00 12.02 ?  116 PHE   A CE2  1 
ATOM   2394 C CZ   . PHE   A 1 116 ? 22.630 -8.420  3.672   1.00 11.74 ?  116 PHE   A CZ   1 
ATOM   2395 H H    . PHE   A 1 116 ? 26.578 -11.661 3.145   1.00 13.86 ?  116 PHE   A H    1 
ATOM   2396 H HA   . PHE   A 1 116 ? 26.652 -10.913 5.647   1.00 13.81 ?  116 PHE   A HA   1 
ATOM   2397 H HB2  . PHE   A 1 116 ? 24.747 -12.546 4.345   1.00 14.18 ?  116 PHE   A HB2  1 
ATOM   2398 H HB3  . PHE   A 1 116 ? 24.571 -12.088 5.849   1.00 14.18 ?  116 PHE   A HB3  1 
ATOM   2399 H HD1  . PHE   A 1 116 ? 25.643 -9.634  3.528   1.00 13.90 ?  116 PHE   A HD1  1 
ATOM   2400 H HD2  . PHE   A 1 116 ? 22.424 -11.174 5.332   1.00 14.40 ?  116 PHE   A HD2  1 
ATOM   2401 H HE1  . PHE   A 1 116 ? 24.371 -7.818  2.841   1.00 14.30 ?  116 PHE   A HE1  1 
ATOM   2402 H HE2  . PHE   A 1 116 ? 21.157 -9.375  4.653   1.00 14.42 ?  116 PHE   A HE2  1 
ATOM   2403 H HZ   . PHE   A 1 116 ? 22.121 -7.689  3.406   1.00 14.08 ?  116 PHE   A HZ   1 
ATOM   2404 N N    . ASN   A 1 117 ? 27.377 -13.984 5.192   1.00 12.08 ?  117 ASN   A N    1 
ATOM   2405 C CA   . ASN   A 1 117 ? 27.745 -15.230 5.859   1.00 12.43 ?  117 ASN   A CA   1 
ATOM   2406 C C    . ASN   A 1 117 ? 29.004 -15.117 6.693   1.00 13.04 ?  117 ASN   A C    1 
ATOM   2407 O O    . ASN   A 1 117 ? 29.302 -16.041 7.457   1.00 13.74 ?  117 ASN   A O    1 
ATOM   2408 C CB   . ASN   A 1 117 ? 27.864 -16.355 4.840   1.00 12.23 ?  117 ASN   A CB   1 
ATOM   2409 C CG   . ASN   A 1 117 ? 26.515 -16.744 4.300   1.00 12.18 ?  117 ASN   A CG   1 
ATOM   2410 O OD1  . ASN   A 1 117 ? 25.535 -16.773 5.046   1.00 13.26 ?  117 ASN   A OD1  1 
ATOM   2411 N ND2  . ASN   A 1 117 ? 26.433 -16.992 3.007   1.00 12.21 ?  117 ASN   A ND2  1 
ATOM   2412 H H    . ASN   A 1 117 ? 27.453 -13.999 4.332   1.00 14.48 ?  117 ASN   A H    1 
ATOM   2413 H HA   . ASN   A 1 117 ? 27.019 -15.467 6.460   1.00 14.91 ?  117 ASN   A HA   1 
ATOM   2414 H HB2  . ASN   A 1 117 ? 28.413 -16.058 4.098   1.00 14.67 ?  117 ASN   A HB2  1 
ATOM   2415 H HB3  . ASN   A 1 117 ? 28.257 -17.128 5.266   1.00 14.67 ?  117 ASN   A HB3  1 
ATOM   2416 H HD21 . ASN   A 1 117 ? 25.676 -17.209 2.665   1.00 14.65 ?  117 ASN   A HD21 1 
ATOM   2417 H HD22 . ASN   A 1 117 ? 27.134 -16.944 2.517   1.00 14.65 ?  117 ASN   A HD22 1 
ATOM   2418 N N    . GLN   A 1 118 ? 29.728 -14.006 6.586   1.00 12.85 ?  118 GLN   A N    1 
ATOM   2419 C CA   . GLN   A 1 118 ? 30.906 -13.772 7.407   1.00 13.55 ?  118 GLN   A CA   1 
ATOM   2420 C C    . GLN   A 1 118 ? 30.565 -13.199 8.776   1.00 13.28 ?  118 GLN   A C    1 
ATOM   2421 O O    . GLN   A 1 118 ? 31.479 -12.907 9.556   1.00 14.89 ?  118 GLN   A O    1 
ATOM   2422 C CB   . GLN   A 1 118 ? 31.898 -12.866 6.671   1.00 13.64 ?  118 GLN   A CB   1 
ATOM   2423 C CG   . GLN   A 1 118 ? 32.372 -13.441 5.353   1.00 13.51 ?  118 GLN   A CG   1 
ATOM   2424 C CD   . GLN   A 1 118 ? 33.206 -14.698 5.530   1.00 14.02 ?  118 GLN   A CD   1 
ATOM   2425 O OE1  . GLN   A 1 118 ? 34.072 -14.759 6.412   1.00 14.76 ?  118 GLN   A OE1  1 
ATOM   2426 N NE2  . GLN   A 1 118 ? 32.957 -15.701 4.688   1.00 14.21 ?  118 GLN   A NE2  1 
ATOM   2427 H H    . GLN   A 1 118 ? 29.547 -13.359 6.039   1.00 15.42 ?  118 GLN   A H    1 
ATOM   2428 H HA   . GLN   A 1 118 ? 31.336 -14.626 7.554   1.00 16.25 ?  118 GLN   A HA   1 
ATOM   2429 H HB2  . GLN   A 1 118 ? 31.470 -12.016 6.493   1.00 16.36 ?  118 GLN   A HB2  1 
ATOM   2430 H HB3  . GLN   A 1 118 ? 32.673 -12.737 7.239   1.00 16.36 ?  118 GLN   A HB3  1 
ATOM   2431 H HG2  . GLN   A 1 118 ? 31.602 -13.662 4.804   1.00 16.21 ?  118 GLN   A HG2  1 
ATOM   2432 H HG3  . GLN   A 1 118 ? 32.920 -12.780 4.900   1.00 16.21 ?  118 GLN   A HG3  1 
ATOM   2433 H HE21 . GLN   A 1 118 ? 32.338 -15.618 4.089   1.00 17.04 ?  118 GLN   A HE21 1 
ATOM   2434 H HE22 . GLN   A 1 118 ? 33.395 -16.437 4.745   1.00 17.04 ?  118 GLN   A HE22 1 
ATOM   2435 N N    . HIS   A 1 119 ? 29.276 -13.042 9.086   1.00 12.91 ?  119 HIS   A N    1 
ATOM   2436 C CA   . HIS   A 1 119 ? 28.825 -12.436 10.332  1.00 13.28 ?  119 HIS   A CA   1 
ATOM   2437 C C    . HIS   A 1 119 ? 27.687 -13.262 10.906  1.00 13.53 ?  119 HIS   A C    1 
ATOM   2438 O O    . HIS   A 1 119 ? 26.737 -13.593 10.192  1.00 13.81 ?  119 HIS   A O    1 
ATOM   2439 C CB   . HIS   A 1 119 ? 28.365 -11.004 10.058  1.00 13.80 ?  119 HIS   A CB   1 
ATOM   2440 C CG   . HIS   A 1 119 ? 29.444 -10.190 9.444   1.00 15.18 ?  119 HIS   A CG   1 
ATOM   2441 N ND1  . HIS   A 1 119 ? 30.419 -9.582  10.199  1.00 17.51 ?  119 HIS   A ND1  1 
ATOM   2442 C CD2  . HIS   A 1 119 ? 29.788 -10.002 8.150   1.00 16.14 ?  119 HIS   A CD2  1 
ATOM   2443 C CE1  . HIS   A 1 119 ? 31.286 -8.996  9.394   1.00 17.71 ?  119 HIS   A CE1  1 
ATOM   2444 N NE2  . HIS   A 1 119 ? 30.935 -9.246  8.145   1.00 17.47 ?  119 HIS   A NE2  1 
ATOM   2445 H H    . HIS   A 1 119 ? 28.620 -13.293 8.579   1.00 15.48 ?  119 HIS   A H    1 
ATOM   2446 H HA   . HIS   A 1 119 ? 29.555 -12.419 10.972  1.00 15.93 ?  119 HIS   A HA   1 
ATOM   2447 H HB2  . HIS   A 1 119 ? 27.612 -11.029 9.446   1.00 16.56 ?  119 HIS   A HB2  1 
ATOM   2448 H HB3  . HIS   A 1 119 ? 28.108 -10.590 10.893  1.00 16.56 ?  119 HIS   A HB3  1 
ATOM   2449 H HD2  . HIS   A 1 119 ? 29.333 -10.320 7.400   1.00 19.36 ?  119 HIS   A HD2  1 
ATOM   2450 H HE1  . HIS   A 1 119 ? 32.025 -8.498  9.658   1.00 21.25 ?  119 HIS   A HE1  1 
ATOM   2451 H HE2  . HIS   A 1 119 ? 31.345 -8.961  7.441   1.00 20.96 ?  119 HIS   A HE2  1 
ATOM   2452 N N    . GLU   A 1 120 ? 27.775 -13.568 12.200  1.00 14.45 ?  120 GLU   A N    1 
ATOM   2453 C CA   . GLU   A 1 120 ? 26.822 -14.501 12.797  1.00 16.67 ?  120 GLU   A CA   1 
ATOM   2454 C C    . GLU   A 1 120 ? 25.404 -13.939 12.857  1.00 15.14 ?  120 GLU   A C    1 
ATOM   2455 O O    . GLU   A 1 120 ? 24.434 -14.702 12.730  1.00 15.39 ?  120 GLU   A O    1 
ATOM   2456 C CB   . GLU   A 1 120 ? 27.294 -14.912 14.194  1.00 21.49 ?  120 GLU   A CB   1 
ATOM   2457 C CG   . GLU   A 1 120 ? 28.470 -15.875 14.191  1.00 29.20 ?  120 GLU   A CG   1 
ATOM   2458 C CD   . GLU   A 1 120 ? 28.590 -16.642 15.490  1.00 36.83 ?  120 GLU   A CD   1 
ATOM   2459 O OE1  . GLU   A 1 120 ? 28.372 -16.035 16.560  1.00 38.79 ?  120 GLU   A OE1  1 
ATOM   2460 O OE2  . GLU   A 1 120 ? 28.894 -17.854 15.440  1.00 39.83 -1 120 GLU   A OE2  1 
ATOM   2461 H H    . GLU   A 1 120 ? 28.370 -13.261 12.746  1.00 17.33 ?  120 GLU   A H    1 
ATOM   2462 H HA   . GLU   A 1 120 ? 26.798 -15.304 12.260  1.00 20.00 ?  120 GLU   A HA   1 
ATOM   2463 H HB2  . GLU   A 1 120 ? 27.568 -14.124 14.687  1.00 25.78 ?  120 GLU   A HB2  1 
ATOM   2464 H HB3  . GLU   A 1 120 ? 26.563 -15.351 14.661  1.00 25.78 ?  120 GLU   A HB3  1 
ATOM   2465 H HG2  . GLU   A 1 120 ? 28.362 -16.513 13.470  1.00 35.03 ?  120 GLU   A HG2  1 
ATOM   2466 H HG3  . GLU   A 1 120 ? 29.294 -15.378 14.079  1.00 35.03 ?  120 GLU   A HG3  1 
ATOM   2467 N N    . VAL   A 1 121 ? 25.266 -12.631 13.075  1.00 14.61 ?  121 VAL   A N    1 
ATOM   2468 C CA   . VAL   A 1 121 ? 23.969 -11.971 13.195  1.00 14.72 ?  121 VAL   A CA   1 
ATOM   2469 C C    . VAL   A 1 121 ? 24.080 -10.591 12.555  1.00 13.78 ?  121 VAL   A C    1 
ATOM   2470 O O    . VAL   A 1 121 ? 25.049 -9.865  12.801  1.00 14.21 ?  121 VAL   A O    1 
ATOM   2471 C CB   . VAL   A 1 121 ? 23.536 -11.816 14.671  1.00 17.36 ?  121 VAL   A CB   1 
ATOM   2472 C CG1  . VAL   A 1 121 ? 22.138 -11.206 14.766  1.00 17.87 ?  121 VAL   A CG1  1 
ATOM   2473 C CG2  . VAL   A 1 121 ? 23.583 -13.141 15.413  1.00 19.40 ?  121 VAL   A CG2  1 
ATOM   2474 H H    . VAL   A 1 121 ? 25.931 -12.089 13.160  1.00 17.53 ?  121 VAL   A H    1 
ATOM   2475 H HA   . VAL   A 1 121 ? 23.296 -12.487 12.728  1.00 17.66 ?  121 VAL   A HA   1 
ATOM   2476 H HB   . VAL   A 1 121 ? 24.148 -11.213 15.116  1.00 20.82 ?  121 VAL   A HB   1 
ATOM   2477 H HG11 . VAL   A 1 121 ? 21.833 -11.250 15.688  1.00 21.44 ?  121 VAL   A HG11 1 
ATOM   2478 H HG12 . VAL   A 1 121 ? 22.173 -10.281 14.476  1.00 21.44 ?  121 VAL   A HG12 1 
ATOM   2479 H HG13 . VAL   A 1 121 ? 21.532 -11.709 14.198  1.00 21.44 ?  121 VAL   A HG13 1 
ATOM   2480 H HG21 . VAL   A 1 121 ? 23.231 -13.015 16.314  1.00 23.27 ?  121 VAL   A HG21 1 
ATOM   2481 H HG22 . VAL   A 1 121 ? 23.036 -13.792 14.942  1.00 23.27 ?  121 VAL   A HG22 1 
ATOM   2482 H HG23 . VAL   A 1 121 ? 24.498 -13.451 15.461  1.00 23.27 ?  121 VAL   A HG23 1 
ATOM   2483 N N    . LEU   A 1 122 ? 23.075 -10.208 11.763  1.00 12.80 ?  122 LEU   A N    1 
ATOM   2484 C CA   . LEU   A 1 122 ? 23.075 -8.910  11.096  1.00 12.31 ?  122 LEU   A CA   1 
ATOM   2485 C C    . LEU   A 1 122 ? 21.678 -8.318  11.061  1.00 12.23 ?  122 LEU   A C    1 
ATOM   2486 O O    . LEU   A 1 122 ? 20.690 -9.040  10.929  1.00 13.31 ?  122 LEU   A O    1 
ATOM   2487 C CB   . LEU   A 1 122 ? 23.497 -9.008  9.628   1.00 13.77 ?  122 LEU   A CB   1 
ATOM   2488 C CG   . LEU   A 1 122 ? 24.710 -9.853  9.273   1.00 13.72 ?  122 LEU   A CG   1 
ATOM   2489 C CD1  . LEU   A 1 122 ? 24.310 -11.303 9.054   1.00 14.56 ?  122 LEU   A CD1  1 
ATOM   2490 C CD2  . LEU   A 1 122 ? 25.387 -9.284  8.038   1.00 13.42 ?  122 LEU   A CD2  1 
ATOM   2491 H H    . LEU   A 1 122 ? 22.370 -10.682 11.601  1.00 15.35 ?  122 LEU   A H    1 
ATOM   2492 H HA   . LEU   A 1 122 ? 23.669 -8.296  11.556  1.00 14.76 ?  122 LEU   A HA   1 
ATOM   2493 H HB2  . LEU   A 1 122 ? 22.757 -9.371  9.126   1.00 16.51 ?  122 LEU   A HB2  1 
ATOM   2494 H HB3  . LEU   A 1 122 ? 23.690 -8.113  9.312   1.00 16.51 ?  122 LEU   A HB3  1 
ATOM   2495 H HG   . LEU   A 1 122 ? 25.355 -9.829  10.000  1.00 16.46 ?  122 LEU   A HG   1 
ATOM   2496 H HD11 . LEU   A 1 122 ? 25.087 -11.815 8.778   1.00 17.47 ?  122 LEU   A HD11 1 
ATOM   2497 H HD12 . LEU   A 1 122 ? 23.958 -11.664 9.884   1.00 17.47 ?  122 LEU   A HD12 1 
ATOM   2498 H HD13 . LEU   A 1 122 ? 23.629 -11.343 8.363   1.00 17.47 ?  122 LEU   A HD13 1 
ATOM   2499 H HD21 . LEU   A 1 122 ? 26.133 -9.858  7.787   1.00 16.10 ?  122 LEU   A HD21 1 
ATOM   2500 H HD22 . LEU   A 1 122 ? 24.745 -9.247  7.313   1.00 16.10 ?  122 LEU   A HD22 1 
ATOM   2501 H HD23 . LEU   A 1 122 ? 25.714 -8.393  8.238   1.00 16.10 ?  122 LEU   A HD23 1 
ATOM   2502 N N    A LEU   A 1 123 ? 21.613 -6.992  11.152  0.60 11.81 ?  123 LEU   A N    1 
ATOM   2503 N N    B LEU   A 1 123 ? 21.615 -6.992  11.199  0.40 12.05 ?  123 LEU   A N    1 
ATOM   2504 C CA   A LEU   A 1 123 ? 20.452 -6.204  10.751  0.60 11.41 ?  123 LEU   A CA   1 
ATOM   2505 C CA   B LEU   A 1 123 ? 20.434 -6.192  10.894  0.40 12.11 ?  123 LEU   A CA   1 
ATOM   2506 C C    A LEU   A 1 123 ? 20.701 -5.709  9.331   0.60 11.14 ?  123 LEU   A C    1 
ATOM   2507 C C    B LEU   A 1 123 ? 20.670 -5.585  9.520   0.40 11.52 ?  123 LEU   A C    1 
ATOM   2508 O O    A LEU   A 1 123 ? 21.773 -5.164  9.054   0.60 11.47 ?  123 LEU   A O    1 
ATOM   2509 O O    B LEU   A 1 123 ? 21.673 -4.893  9.319   0.40 11.37 ?  123 LEU   A O    1 
ATOM   2510 C CB   A LEU   A 1 123 ? 20.311 -5.005  11.689  0.60 11.50 ?  123 LEU   A CB   1 
ATOM   2511 C CB   B LEU   A 1 123 ? 20.261 -5.078  11.929  0.40 12.64 ?  123 LEU   A CB   1 
ATOM   2512 C CG   A LEU   A 1 123 ? 19.221 -3.989  11.359  0.60 12.57 ?  123 LEU   A CG   1 
ATOM   2513 C CG   B LEU   A 1 123 ? 19.311 -3.942  11.528  0.40 13.20 ?  123 LEU   A CG   1 
ATOM   2514 C CD1  A LEU   A 1 123 ? 17.850 -4.645  11.398  0.60 13.39 ?  123 LEU   A CD1  1 
ATOM   2515 C CD1  B LEU   A 1 123 ? 17.867 -4.429  11.426  0.40 13.71 ?  123 LEU   A CD1  1 
ATOM   2516 C CD2  A LEU   A 1 123 ? 19.291 -2.808  12.322  0.60 13.07 ?  123 LEU   A CD2  1 
ATOM   2517 C CD2  B LEU   A 1 123 ? 19.429 -2.776  12.495  0.40 13.69 ?  123 LEU   A CD2  1 
ATOM   2518 H H    A LEU   A 1 123 ? 22.258 -6.508  11.457  0.60 14.17 ?  123 LEU   A H    1 
ATOM   2519 H H    B LEU   A 1 123 ? 22.280 -6.508  11.454  0.40 14.46 ?  123 LEU   A H    1 
ATOM   2520 H HA   A LEU   A 1 123 ? 19.647 -6.748  10.778  0.60 13.69 ?  123 LEU   A HA   1 
ATOM   2521 H HA   B LEU   A 1 123 ? 19.637 -6.737  10.870  0.40 14.53 ?  123 LEU   A HA   1 
ATOM   2522 H HB2  A LEU   A 1 123 ? 20.123 -5.340  12.579  0.60 13.80 ?  123 LEU   A HB2  1 
ATOM   2523 H HB2  B LEU   A 1 123 ? 19.911 -5.469  12.747  0.40 15.16 ?  123 LEU   A HB2  1 
ATOM   2524 H HB3  A LEU   A 1 123 ? 21.151 -4.528  11.694  0.60 13.80 ?  123 LEU   A HB3  1 
ATOM   2525 H HB3  B LEU   A 1 123 ? 21.127 -4.678  12.108  0.40 15.16 ?  123 LEU   A HB3  1 
ATOM   2526 H HG   A LEU   A 1 123 ? 19.362 -3.644  10.462  0.60 15.07 ?  123 LEU   A HG   1 
ATOM   2527 H HG   B LEU   A 1 123 ? 19.560 -3.599  10.656  0.40 15.83 ?  123 LEU   A HG   1 
ATOM   2528 H HD11 A LEU   A 1 123 ? 17.170 -3.967  11.261  0.60 16.06 ?  123 LEU   A HD11 1 
ATOM   2529 H HD11 B LEU   A 1 123 ? 17.296 -3.683  11.178  0.40 16.44 ?  123 LEU   A HD11 1 
ATOM   2530 H HD12 A LEU   A 1 123 ? 17.800 -5.310  10.694  0.60 16.06 ?  123 LEU   A HD12 1 
ATOM   2531 H HD12 B LEU   A 1 123 ? 17.813 -5.123  10.749  0.40 16.44 ?  123 LEU   A HD12 1 
ATOM   2532 H HD13 A LEU   A 1 123 ? 17.728 -5.067  12.263  0.60 16.06 ?  123 LEU   A HD13 1 
ATOM   2533 H HD13 B LEU   A 1 123 ? 17.591 -4.784  12.285  0.40 16.44 ?  123 LEU   A HD13 1 
ATOM   2534 H HD21 A LEU   A 1 123 ? 18.593 -2.173  12.099  0.60 15.68 ?  123 LEU   A HD21 1 
ATOM   2535 H HD21 B LEU   A 1 123 ? 18.819 -2.075  12.219  0.40 16.43 ?  123 LEU   A HD21 1 
ATOM   2536 H HD22 A LEU   A 1 123 ? 19.163 -3.134  13.229  0.60 15.68 ?  123 LEU   A HD22 1 
ATOM   2537 H HD22 B LEU   A 1 123 ? 19.202 -3.083  13.385  0.40 16.43 ?  123 LEU   A HD22 1 
ATOM   2538 H HD23 A LEU   A 1 123 ? 20.161 -2.387  12.243  0.60 15.68 ?  123 LEU   A HD23 1 
ATOM   2539 H HD23 B LEU   A 1 123 ? 20.341 -2.448  12.478  0.40 16.43 ?  123 LEU   A HD23 1 
ATOM   2540 N N    A ALA   A 1 124 ? 19.728 -5.885  8.434   0.60 10.78 ?  124 ALA   A N    1 
ATOM   2541 N N    B ALA   A 1 124 ? 19.765 -5.835  8.583   0.40 11.07 ?  124 ALA   A N    1 
ATOM   2542 C CA   A ALA   A 1 124 ? 20.015 -5.636  7.027   0.60 10.88 ?  124 ALA   A CA   1 
ATOM   2543 C CA   B ALA   A 1 124 ? 20.013 -5.487  7.195   0.40 10.50 ?  124 ALA   A CA   1 
ATOM   2544 C C    A ALA   A 1 124 ? 18.790 -5.196  6.237   0.60 10.23 ?  124 ALA   A C    1 
ATOM   2545 C C    B ALA   A 1 124 ? 18.751 -4.991  6.512   0.40 10.40 ?  124 ALA   A C    1 
ATOM   2546 O O    A ALA   A 1 124 ? 17.658 -5.566  6.574   0.60 10.62 ?  124 ALA   A O    1 
ATOM   2547 O O    B ALA   A 1 124 ? 17.633 -5.307  6.934   0.40 10.62 ?  124 ALA   A O    1 
ATOM   2548 C CB   A ALA   A 1 124 ? 20.623 -6.879  6.359   0.60 11.71 ?  124 ALA   A CB   1 
ATOM   2549 C CB   B ALA   A 1 124 ? 20.540 -6.695  6.411   0.40 10.62 ?  124 ALA   A CB   1 
ATOM   2550 H H    A ALA   A 1 124 ? 18.929 -6.144  8.611   0.60 12.92 ?  124 ALA   A H    1 
ATOM   2551 H H    B ALA   A 1 124 ? 19.003 -6.208  8.720   0.40 13.28 ?  124 ALA   A H    1 
ATOM   2552 H HA   A ALA   A 1 124 ? 20.675 -4.934  6.983   0.60 13.05 ?  124 ALA   A HA   1 
ATOM   2553 H HA   B ALA   A 1 124 ? 20.684 -4.783  7.160   0.40 12.59 ?  124 ALA   A HA   1 
ATOM   2554 H HB1  A ALA   A 1 124 ? 20.805 -6.684  5.426   0.60 14.04 ?  124 ALA   A HB1  1 
ATOM   2555 H HB1  B ALA   A 1 124 ? 20.697 -6.430  5.490   0.40 12.74 ?  124 ALA   A HB1  1 
ATOM   2556 H HB2  A ALA   A 1 124 ? 21.455 -7.110  6.812   0.60 14.04 ?  124 ALA   A HB2  1 
ATOM   2557 H HB2  B ALA   A 1 124 ? 21.368 -6.992  6.817   0.40 12.74 ?  124 ALA   A HB2  1 
ATOM   2558 H HB3  A ALA   A 1 124 ? 20.000 -7.619  6.428   0.60 14.04 ?  124 ALA   A HB3  1 
ATOM   2559 H HB3  B ALA   A 1 124 ? 19.878 -7.401  6.445   0.40 12.74 ?  124 ALA   A HB3  1 
ATOM   2560 N N    A PRO   A 1 125 ? 18.993 -4.437  5.165   0.60 9.98  ?  125 PRO   A N    1 
ATOM   2561 N N    B PRO   A 1 125 ? 18.905 -4.202  5.453   0.40 10.39 ?  125 PRO   A N    1 
ATOM   2562 C CA   A PRO   A 1 125 ? 17.935 -4.172  4.193   0.60 10.39 ?  125 PRO   A CA   1 
ATOM   2563 C CA   B PRO   A 1 125 ? 17.810 -3.965  4.516   0.40 11.14 ?  125 PRO   A CA   1 
ATOM   2564 C C    A PRO   A 1 125 ? 17.971 -5.239  3.104   0.60 10.40 ?  125 PRO   A C    1 
ATOM   2565 C C    B PRO   A 1 125 ? 17.844 -5.027  3.432   0.40 11.48 ?  125 PRO   A C    1 
ATOM   2566 O O    A PRO   A 1 125 ? 18.934 -5.995  2.976   0.60 10.73 ?  125 PRO   A O    1 
ATOM   2567 O O    B PRO   A 1 125 ? 18.766 -5.851  3.379   0.40 10.90 ?  125 PRO   A O    1 
ATOM   2568 C CB   A PRO   A 1 125 ? 18.387 -2.831  3.608   0.60 9.99  ?  125 PRO   A CB   1 
ATOM   2569 C CB   B PRO   A 1 125 ? 18.184 -2.600  3.930   0.40 11.13 ?  125 PRO   A CB   1 
ATOM   2570 C CG   A PRO   A 1 125 ? 19.898 -2.980  3.552   0.60 9.60  ?  125 PRO   A CG   1 
ATOM   2571 C CG   B PRO   A 1 125 ? 19.684 -2.690  3.825   0.40 11.29 ?  125 PRO   A CG   1 
ATOM   2572 C CD   A PRO   A 1 125 ? 20.274 -3.828  4.755   0.60 9.64  ?  125 PRO   A CD   1 
ATOM   2573 C CD   B PRO   A 1 125 ? 20.132 -3.503  5.026   0.40 11.06 ?  125 PRO   A CD   1 
ATOM   2574 H HA   A PRO   A 1 125 ? 17.060 -4.118  4.605   0.60 12.47 ?  125 PRO   A HA   1 
ATOM   2575 H HA   B PRO   A 1 125 ? 16.937 -3.936  4.950   0.40 13.36 ?  125 PRO   A HA   1 
ATOM   2576 H HB2  A PRO   A 1 125 ? 18.009 -2.718  2.721   0.60 11.98 ?  125 PRO   A HB2  1 
ATOM   2577 H HB2  B PRO   A 1 125 ? 17.783 -2.480  3.055   0.40 13.35 ?  125 PRO   A HB2  1 
ATOM   2578 H HB3  A PRO   A 1 125 ? 18.120 -2.115  4.199   0.60 11.98 ?  125 PRO   A HB3  1 
ATOM   2579 H HB3  B PRO   A 1 125 ? 17.923 -1.887  4.536   0.40 13.35 ?  125 PRO   A HB3  1 
ATOM   2580 H HG2  A PRO   A 1 125 ? 20.156 -3.424  2.728   0.60 11.51 ?  125 PRO   A HG2  1 
ATOM   2581 H HG2  B PRO   A 1 125 ? 19.926 -3.140  2.999   0.40 13.54 ?  125 PRO   A HG2  1 
ATOM   2582 H HG3  A PRO   A 1 125 ? 20.312 -2.103  3.610   0.60 11.51 ?  125 PRO   A HG3  1 
ATOM   2583 H HG3  B PRO   A 1 125 ? 20.071 -1.801  3.851   0.40 13.54 ?  125 PRO   A HG3  1 
ATOM   2584 H HD2  A PRO   A 1 125 ? 20.919 -4.512  4.504   0.60 11.56 ?  125 PRO   A HD2  1 
ATOM   2585 H HD2  B PRO   A 1 125 ? 20.813 -4.141  4.761   0.40 13.27 ?  125 PRO   A HD2  1 
ATOM   2586 H HD3  A PRO   A 1 125 ? 20.619 -3.268  5.471   0.60 11.56 ?  125 PRO   A HD3  1 
ATOM   2587 H HD3  B PRO   A 1 125 ? 20.452 -2.917  5.727   0.40 13.27 ?  125 PRO   A HD3  1 
ATOM   2588 N N    A LEU   A 1 126 ? 16.912 -5.270  2.301   0.60 10.85 ?  126 LEU   A N    1 
ATOM   2589 N N    B LEU   A 1 126 ? 16.852 -5.001  2.552   0.40 12.44 ?  126 LEU   A N    1 
ATOM   2590 C CA   A LEU   A 1 126 ? 16.933 -6.077  1.091   0.60 11.00 ?  126 LEU   A CA   1 
ATOM   2591 C CA   B LEU   A 1 126 ? 16.892 -5.800  1.337   0.40 13.30 ?  126 LEU   A CA   1 
ATOM   2592 C C    A LEU   A 1 126 ? 17.861 -5.443  0.064   0.60 11.12 ?  126 LEU   A C    1 
ATOM   2593 C C    B LEU   A 1 126 ? 17.858 -5.144  0.355   0.40 12.91 ?  126 LEU   A C    1 
ATOM   2594 O O    A LEU   A 1 126 ? 17.611 -4.334  -0.426  0.60 11.47 ?  126 LEU   A O    1 
ATOM   2595 O O    B LEU   A 1 126 ? 17.857 -3.924  0.196   0.40 13.74 ?  126 LEU   A O    1 
ATOM   2596 C CB   A LEU   A 1 126 ? 15.531 -6.212  0.519   0.60 11.14 ?  126 LEU   A CB   1 
ATOM   2597 C CB   B LEU   A 1 126 ? 15.485 -5.849  0.739   0.40 15.93 ?  126 LEU   A CB   1 
ATOM   2598 C CG   A LEU   A 1 126 ? 14.606 -7.090  1.356   0.60 11.14 ?  126 LEU   A CG   1 
ATOM   2599 C CG   B LEU   A 1 126 ? 14.871 -7.124  0.152   0.40 18.30 ?  126 LEU   A CG   1 
ATOM   2600 C CD1  A LEU   A 1 126 ? 13.172 -6.945  0.876   0.60 12.35 ?  126 LEU   A CD1  1 
ATOM   2601 C CD1  B LEU   A 1 126 ? 15.133 -8.349  1.011   0.40 18.88 ?  126 LEU   A CD1  1 
ATOM   2602 C CD2  A LEU   A 1 126 ? 15.048 -8.554  1.289   0.60 12.17 ?  126 LEU   A CD2  1 
ATOM   2603 C CD2  B LEU   A 1 126 ? 13.365 -6.922  -0.032  0.40 18.82 ?  126 LEU   A CD2  1 
ATOM   2604 H H    A LEU   A 1 126 ? 16.185 -4.836  2.429   0.60 13.02 ?  126 LEU   A H    1 
ATOM   2605 H H    B LEU   A 1 126 ? 16.145 -4.514  2.642   0.40 14.92 ?  126 LEU   A H    1 
ATOM   2606 H HA   A LEU   A 1 126 ? 17.264 -6.968  1.294   0.60 13.20 ?  126 LEU   A HA   1 
ATOM   2607 H HA   B LEU   A 1 126 ? 17.200 -6.693  1.539   0.40 15.95 ?  126 LEU   A HA   1 
ATOM   2608 H HB2  A LEU   A 1 126 ? 15.124 -5.333  0.463   0.60 13.36 ?  126 LEU   A HB2  1 
ATOM   2609 H HB2  B LEU   A 1 126 ? 14.875 -5.565  1.437   0.40 19.11 ?  126 LEU   A HB2  1 
ATOM   2610 H HB3  A LEU   A 1 126 ? 15.579 -6.608  -0.366  0.60 13.36 ?  126 LEU   A HB3  1 
ATOM   2611 H HB3  B LEU   A 1 126 ? 15.461 -5.193  0.028   0.40 19.11 ?  126 LEU   A HB3  1 
ATOM   2612 H HG   A LEU   A 1 126 ? 14.636 -6.804  2.284   0.60 13.36 ?  126 LEU   A HG   1 
ATOM   2613 H HG   B LEU   A 1 126 ? 15.257 -7.279  -0.722  0.40 21.95 ?  126 LEU   A HG   1 
ATOM   2614 H HD11 A LEU   A 1 126 ? 12.599 -7.529  1.402   0.60 14.81 ?  126 LEU   A HD11 1 
ATOM   2615 H HD11 B LEU   A 1 126 ? 14.602 -9.089  0.674   0.40 22.65 ?  126 LEU   A HD11 1 
ATOM   2616 H HD12 A LEU   A 1 126 ? 12.891 -6.024  0.983   0.60 14.81 ?  126 LEU   A HD12 1 
ATOM   2617 H HD12 B LEU   A 1 126 ? 16.075 -8.570  0.964   0.40 22.65 ?  126 LEU   A HD12 1 
ATOM   2618 H HD13 A LEU   A 1 126 ? 13.126 -7.199  -0.061  0.60 14.81 ?  126 LEU   A HD13 1 
ATOM   2619 H HD13 B LEU   A 1 126 ? 14.881 -8.152  1.926   0.40 22.65 ?  126 LEU   A HD13 1 
ATOM   2620 H HD21 A LEU   A 1 126 ? 14.361 -9.115  1.683   0.60 14.60 ?  126 LEU   A HD21 1 
ATOM   2621 H HD21 B LEU   A 1 126 ? 12.975 -7.739  -0.382  0.40 22.58 ?  126 LEU   A HD21 1 
ATOM   2622 H HD22 A LEU   A 1 126 ? 15.182 -8.800  0.360   0.60 14.60 ?  126 LEU   A HD22 1 
ATOM   2623 H HD22 B LEU   A 1 126 ? 12.966 -6.711  0.828   0.40 22.58 ?  126 LEU   A HD22 1 
ATOM   2624 H HD23 A LEU   A 1 126 ? 15.878 -8.655  1.781   0.60 14.60 ?  126 LEU   A HD23 1 
ATOM   2625 H HD23 B LEU   A 1 126 ? 13.214 -6.192  -0.653  0.40 22.58 ?  126 LEU   A HD23 1 
ATOM   2626 N N    A LEU   A 1 127 ? 18.930 -6.161  -0.266  0.60 11.18 ?  127 LEU   A N    1 
ATOM   2627 N N    B LEU   A 1 127 ? 18.706 -5.944  -0.290  0.40 12.35 ?  127 LEU   A N    1 
ATOM   2628 C CA   A LEU   A 1 127 ? 19.913 -5.665  -1.212  0.60 11.08 ?  127 LEU   A CA   1 
ATOM   2629 C CA   B LEU   A 1 127 ? 19.704 -5.386  -1.197  0.40 12.44 ?  127 LEU   A CA   1 
ATOM   2630 C C    A LEU   A 1 127 ? 19.286 -5.450  -2.579  0.60 10.78 ?  127 LEU   A C    1 
ATOM   2631 C C    B LEU   A 1 127 ? 19.172 -5.305  -2.626  0.40 12.75 ?  127 LEU   A C    1 
ATOM   2632 O O    A LEU   A 1 127 ? 18.456 -6.239  -3.042  0.60 11.16 ?  127 LEU   A O    1 
ATOM   2633 O O    B LEU   A 1 127 ? 18.327 -6.100  -3.050  0.40 13.21 ?  127 LEU   A O    1 
ATOM   2634 C CB   A LEU   A 1 127 ? 21.070 -6.658  -1.316  0.60 11.70 ?  127 LEU   A CB   1 
ATOM   2635 C CB   B LEU   A 1 127 ? 21.004 -6.203  -1.178  0.40 12.95 ?  127 LEU   A CB   1 
ATOM   2636 C CG   A LEU   A 1 127 ? 21.862 -6.876  -0.029  0.60 11.78 ?  127 LEU   A CG   1 
ATOM   2637 C CG   B LEU   A 1 127 ? 21.828 -6.192  0.119   0.40 13.53 ?  127 LEU   A CG   1 
ATOM   2638 C CD1  A LEU   A 1 127 ? 22.973 -7.867  -0.288  0.60 12.16 ?  127 LEU   A CD1  1 
ATOM   2639 C CD1  B LEU   A 1 127 ? 23.005 -7.164  0.047   0.40 14.00 ?  127 LEU   A CD1  1 
ATOM   2640 C CD2  A LEU   A 1 127 ? 22.437 -5.575  0.475   0.60 12.44 ?  127 LEU   A CD2  1 
ATOM   2641 C CD2  B LEU   A 1 127 ? 22.327 -4.786  0.460   0.40 13.89 ?  127 LEU   A CD2  1 
ATOM   2642 H H    A LEU   A 1 127 ? 19.102 -6.943  0.052   0.60 13.41 ?  127 LEU   A H    1 
ATOM   2643 H H    B LEU   A 1 127 ? 18.729 -6.804  -0.214  0.40 14.82 ?  127 LEU   A H    1 
ATOM   2644 H HA   A LEU   A 1 127 ? 20.262 -4.821  -0.900  0.60 13.29 ?  127 LEU   A HA   1 
ATOM   2645 H HA   B LEU   A 1 127 ? 19.922 -4.489  -0.899  0.40 14.92 ?  127 LEU   A HA   1 
ATOM   2646 H HB2  A LEU   A 1 127 ? 20.714 -7.521  -1.585  0.60 14.04 ?  127 LEU   A HB2  1 
ATOM   2647 H HB2  B LEU   A 1 127 ? 20.782 -7.126  -1.371  0.40 15.54 ?  127 LEU   A HB2  1 
ATOM   2648 H HB3  A LEU   A 1 127 ? 21.691 -6.340  -1.987  0.60 14.04 ?  127 LEU   A HB3  1 
ATOM   2649 H HB3  B LEU   A 1 127 ? 21.579 -5.861  -1.885  0.40 15.54 ?  127 LEU   A HB3  1 
ATOM   2650 H HG   A LEU   A 1 127 ? 21.276 -7.242  0.656   0.60 14.13 ?  127 LEU   A HG   1 
ATOM   2651 H HG   B LEU   A 1 127 ? 21.259 -6.484  0.844   0.40 16.23 ?  127 LEU   A HG   1 
ATOM   2652 H HD11 A LEU   A 1 127 ? 23.450 -8.030  0.541   0.60 14.59 ?  127 LEU   A HD11 1 
ATOM   2653 H HD11 B LEU   A 1 127 ? 23.507 -7.113  0.878   0.40 16.79 ?  127 LEU   A HD11 1 
ATOM   2654 H HD12 A LEU   A 1 127 ? 22.591 -8.693  -0.619  0.60 14.59 ?  127 LEU   A HD12 1 
ATOM   2655 H HD12 B LEU   A 1 127 ? 22.665 -8.064  -0.076  0.40 16.79 ?  127 LEU   A HD12 1 
ATOM   2656 H HD13 A LEU   A 1 127 ? 23.577 -7.493  -0.949  0.60 14.59 ?  127 LEU   A HD13 1 
ATOM   2657 H HD13 B LEU   A 1 127 ? 23.575 -6.920  -0.697  0.40 16.79 ?  127 LEU   A HD13 1 
ATOM   2658 H HD21 A LEU   A 1 127 ? 23.081 -5.761  1.172   0.60 14.92 ?  127 LEU   A HD21 1 
ATOM   2659 H HD21 B LEU   A 1 127 ? 22.912 -4.839  1.234   0.40 16.66 ?  127 LEU   A HD21 1 
ATOM   2660 H HD22 A LEU   A 1 127 ? 22.872 -5.118  -0.266  0.60 14.92 ?  127 LEU   A HD22 1 
ATOM   2661 H HD22 B LEU   A 1 127 ? 22.817 -4.431  -0.298  0.40 16.66 ?  127 LEU   A HD22 1 
ATOM   2662 H HD23 A LEU   A 1 127 ? 21.718 -5.023  0.822   0.60 14.92 ?  127 LEU   A HD23 1 
ATOM   2663 H HD23 B LEU   A 1 127 ? 21.566 -4.222  0.659   0.40 16.66 ?  127 LEU   A HD23 1 
ATOM   2664 N N    A SER   A 1 128 ? 19.701 -4.365  -3.221  0.60 11.01 ?  128 SER   A N    1 
ATOM   2665 N N    B SER   A 1 128 ? 19.677 -4.313  -3.362  0.40 12.80 ?  128 SER   A N    1 
ATOM   2666 C CA   A SER   A 1 128 ? 19.291 -3.963  -4.559  0.60 10.43 ?  128 SER   A CA   1 
ATOM   2667 C CA   B SER   A 1 128 ? 19.439 -4.144  -4.794  0.40 12.53 ?  128 SER   A CA   1 
ATOM   2668 C C    A SER   A 1 128 ? 17.832 -3.530  -4.645  0.60 10.43 ?  128 SER   A C    1 
ATOM   2669 C C    B SER   A 1 128 ? 18.044 -3.653  -5.173  0.40 13.23 ?  128 SER   A C    1 
ATOM   2670 O O    A SER   A 1 128 ? 17.357 -3.236  -5.743  0.60 11.23 ?  128 SER   A O    1 
ATOM   2671 O O    B SER   A 1 128 ? 17.803 -3.335  -6.342  0.40 13.98 ?  128 SER   A O    1 
ATOM   2672 C CB   A SER   A 1 128 ? 19.633 -5.003  -5.632  0.60 10.47 ?  128 SER   A CB   1 
ATOM   2673 C CB   B SER   A 1 128 ? 19.802 -5.408  -5.578  0.40 12.44 ?  128 SER   A CB   1 
ATOM   2674 O OG   A SER   A 1 128 ? 21.037 -5.190  -5.707  0.60 11.20 ?  128 SER   A OG   1 
ATOM   2675 O OG   B SER   A 1 128 ? 21.208 -5.513  -5.718  0.40 12.53 ?  128 SER   A OG   1 
ATOM   2676 H H    A SER   A 1 128 ? 20.264 -3.809  -2.871  0.60 13.21 ?  128 SER   A H    1 
ATOM   2677 H H    B SER   A 1 128 ? 20.199 -3.704  -3.037  0.40 15.35 ?  128 SER   A H    1 
ATOM   2678 H HA   A SER   A 1 128 ? 19.808 -3.177  -4.775  0.60 12.51 ?  128 SER   A HA   1 
ATOM   2679 H HA   B SER   A 1 128 ? 20.042 -3.459  -5.095  0.40 15.03 ?  128 SER   A HA   1 
ATOM   2680 H HB2  A SER   A 1 128 ? 19.202 -5.840  -5.406  0.60 12.56 ?  128 SER   A HB2  1 
ATOM   2681 H HB2  B SER   A 1 128 ? 19.464 -6.190  -5.116  0.40 14.92 ?  128 SER   A HB2  1 
ATOM   2682 H HB3  A SER   A 1 128 ? 19.304 -4.680  -6.489  0.60 12.56 ?  128 SER   A HB3  1 
ATOM   2683 H HB3  B SER   A 1 128 ? 19.403 -5.348  -6.463  0.40 14.92 ?  128 SER   A HB3  1 
ATOM   2684 H HG   A SER   A 1 128 ? 21.409 -4.462  -5.894  0.60 13.44 ?  128 SER   A HG   1 
ATOM   2685 H HG   B SER   A 1 128 ? 21.498 -4.827  -6.108  0.40 15.03 ?  128 SER   A HG   1 
ATOM   2686 N N    A ALA   A 1 129 ? 17.122 -3.451  -3.518  0.60 10.73 ?  129 ALA   A N    1 
ATOM   2687 N N    B ALA   A 1 129 ? 17.124 -3.574  -4.222  0.40 13.59 ?  129 ALA   A N    1 
ATOM   2688 C CA   A ALA   A 1 129 ? 15.747 -2.973  -3.510  0.60 10.89 ?  129 ALA   A CA   1 
ATOM   2689 C CA   B ALA   A 1 129 ? 15.817 -3.004  -4.520  0.40 14.45 ?  129 ALA   A CA   1 
ATOM   2690 C C    A ALA   A 1 129 ? 15.729 -1.444  -3.495  0.60 10.68 ?  129 ALA   A C    1 
ATOM   2691 C C    B ALA   A 1 129 ? 15.869 -1.492  -4.275  0.40 14.89 ?  129 ALA   A C    1 
ATOM   2692 O O    A ALA   A 1 129 ? 16.768 -0.779  -3.555  0.60 11.05 ?  129 ALA   A O    1 
ATOM   2693 O O    B ALA   A 1 129 ? 16.950 -0.900  -4.222  0.40 14.78 ?  129 ALA   A O    1 
ATOM   2694 C CB   A ALA   A 1 129 ? 14.981 -3.569  -2.326  0.60 12.23 ?  129 ALA   A CB   1 
ATOM   2695 C CB   B ALA   A 1 129 ? 14.718 -3.780  -3.786  0.40 15.90 ?  129 ALA   A CB   1 
ATOM   2696 H H    A ALA   A 1 129 ? 17.420 -3.668  -2.738  0.60 12.87 ?  129 ALA   A H    1 
ATOM   2697 H H    B ALA   A 1 129 ? 17.225 -3.847  -3.408  0.40 16.31 ?  129 ALA   A H    1 
ATOM   2698 H HA   A ALA   A 1 129 ? 15.311 -3.263  -4.319  0.60 13.06 ?  129 ALA   A HA   1 
ATOM   2699 H HA   B ALA   A 1 129 ? 15.649 -3.119  -5.465  0.40 17.33 ?  129 ALA   A HA   1 
ATOM   2700 H HB1  A ALA   A 1 129 ? 14.066 -3.243  -2.345  0.60 14.66 ?  129 ALA   A HB1  1 
ATOM   2701 H HB1  B ALA   A 1 129 ? 13.878 -3.301  -3.878  0.40 19.08 ?  129 ALA   A HB1  1 
ATOM   2702 H HB2  A ALA   A 1 129 ? 14.990 -4.534  -2.396  0.60 14.66 ?  129 ALA   A HB2  1 
ATOM   2703 H HB2  B ALA   A 1 129 ? 14.635 -4.663  -4.187  0.40 19.08 ?  129 ALA   A HB2  1 
ATOM   2704 H HB3  A ALA   A 1 129 ? 15.409 -3.293  -1.497  0.60 14.66 ?  129 ALA   A HB3  1 
ATOM   2705 H HB3  B ALA   A 1 129 ? 14.957 -3.861  -2.856  0.40 19.08 ?  129 ALA   A HB3  1 
ATOM   2706 N N    A GLY   A 1 130 ? 14.530 -0.879  -3.419  0.60 11.34 ?  130 GLY   A N    1 
ATOM   2707 N N    B GLY   A 1 130 ? 14.716 -0.846  -4.146  0.40 15.56 ?  130 GLY   A N    1 
ATOM   2708 C CA   A GLY   A 1 130 ? 14.414 0.569   -3.383  0.60 11.72 ?  130 GLY   A CA   1 
ATOM   2709 C CA   B GLY   A 1 130 ? 14.729 0.605   -4.056  0.40 16.48 ?  130 GLY   A CA   1 
ATOM   2710 C C    A GLY   A 1 130 ? 15.033 1.197   -4.619  0.60 11.29 ?  130 GLY   A C    1 
ATOM   2711 C C    B GLY   A 1 130 ? 15.340 1.217   -5.300  0.40 17.43 ?  130 GLY   A C    1 
ATOM   2712 O O    A GLY   A 1 130 ? 14.803 0.752   -5.750  0.60 11.54 ?  130 GLY   A O    1 
ATOM   2713 O O    B GLY   A 1 130 ? 15.068 0.788   -6.429  0.40 17.62 ?  130 GLY   A O    1 
ATOM   2714 H H    A GLY   A 1 130 ? 13.779 -1.305  -3.392  0.60 13.61 ?  130 GLY   A H    1 
ATOM   2715 H H    B GLY   A 1 130 ? 13.938 -1.212  -4.112  0.40 18.66 ?  130 GLY   A H    1 
ATOM   2716 H HA2  A GLY   A 1 130 ? 13.470 0.820   -3.330  0.60 14.06 ?  130 GLY   A HA2  1 
ATOM   2717 H HA2  B GLY   A 1 130 ? 13.822 0.935   -3.963  0.40 19.78 ?  130 GLY   A HA2  1 
ATOM   2718 H HA3  A GLY   A 1 130 ? 14.864 0.916   -2.600  0.60 14.06 ?  130 GLY   A HA3  1 
ATOM   2719 H HA3  B GLY   A 1 130 ? 15.245 0.886   -3.285  0.40 19.78 ?  130 GLY   A HA3  1 
ATOM   2720 N N    A ILE   A 1 131 ? 15.814 2.262   -4.408  0.60 11.31 ?  131 ILE   A N    1 
ATOM   2721 N N    B ILE   A 1 131 ? 16.195 2.227   -5.101  0.40 18.29 ?  131 ILE   A N    1 
ATOM   2722 C CA   A ILE   A 1 131 ? 16.380 3.027   -5.519  0.60 11.20 ?  131 ILE   A CA   1 
ATOM   2723 C CA   B ILE   A 1 131 ? 16.799 2.927   -6.233  0.40 19.03 ?  131 ILE   A CA   1 
ATOM   2724 C C    A ILE   A 1 131 ? 17.422 2.259   -6.320  0.60 10.89 ?  131 ILE   A C    1 
ATOM   2725 C C    B ILE   A 1 131 ? 17.785 2.076   -7.010  0.40 18.57 ?  131 ILE   A C    1 
ATOM   2726 O O    A ILE   A 1 131 ? 17.861 2.757   -7.363  0.60 11.44 ?  131 ILE   A O    1 
ATOM   2727 O O    B ILE   A 1 131 ? 18.195 2.478   -8.105  0.40 19.00 ?  131 ILE   A O    1 
ATOM   2728 C CB   A ILE   A 1 131 ? 16.941 4.391   -5.062  0.60 12.62 ?  131 ILE   A CB   1 
ATOM   2729 C CB   B ILE   A 1 131 ? 17.461 4.284   -5.899  0.40 20.55 ?  131 ILE   A CB   1 
ATOM   2730 C CG1  A ILE   A 1 131 ? 18.175 4.223   -4.175  0.60 14.16 ?  131 ILE   A CG1  1 
ATOM   2731 C CG1  B ILE   A 1 131 ? 18.466 4.150   -4.744  0.40 21.09 ?  131 ILE   A CG1  1 
ATOM   2732 C CG2  A ILE   A 1 131 ? 15.874 5.177   -4.321  0.60 13.46 ?  131 ILE   A CG2  1 
ATOM   2733 C CG2  B ILE   A 1 131 ? 16.392 5.347   -5.687  0.40 21.35 ?  131 ILE   A CG2  1 
ATOM   2734 C CD1  A ILE   A 1 131 ? 18.792 5.544   -3.741  0.60 15.44 ?  131 ILE   A CD1  1 
ATOM   2735 C CD1  B ILE   A 1 131 ? 19.295 5.399   -4.487  0.40 21.25 ?  131 ILE   A CD1  1 
ATOM   2736 H H    A ILE   A 1 131 ? 16.004 2.567   -3.625  0.60 13.56 ?  131 ILE   A H    1 
ATOM   2737 H H    B ILE   A 1 131 ? 16.435 2.517   -4.329  0.40 21.94 ?  131 ILE   A H    1 
ATOM   2738 H HA   A ILE   A 1 131 ? 15.647 3.224   -6.126  0.60 13.43 ?  131 ILE   A HA   1 
ATOM   2739 H HA   B ILE   A 1 131 ? 16.096 3.118   -6.856  0.40 22.83 ?  131 ILE   A HA   1 
ATOM   2740 H HB   A ILE   A 1 131 ? 17.187 4.894   -5.851  0.60 15.14 ?  131 ILE   A HB   1 
ATOM   2741 H HB   B ILE   A 1 131 ? 17.963 4.552   -6.677  0.40 24.66 ?  131 ILE   A HB   1 
ATOM   2742 H HG12 A ILE   A 1 131 ? 17.919 3.731   -3.378  0.60 16.99 ?  131 ILE   A HG12 1 
ATOM   2743 H HG12 B ILE   A 1 131 ? 17.996 3.950   -3.929  0.40 25.30 ?  131 ILE   A HG12 1 
ATOM   2744 H HG13 A ILE   A 1 131 ? 18.847 3.728   -4.667  0.60 16.99 ?  131 ILE   A HG13 1 
ATOM   2745 H HG13 B ILE   A 1 131 ? 19.082 3.430   -4.948  0.40 25.30 ?  131 ILE   A HG13 1 
ATOM   2746 H HG21 A ILE   A 1 131 ? 16.164 6.098   -4.227  0.60 16.15 ?  131 ILE   A HG21 1 
ATOM   2747 H HG21 B ILE   A 1 131 ? 16.822 6.199   -5.517  0.40 25.61 ?  131 ILE   A HG21 1 
ATOM   2748 H HG22 A ILE   A 1 131 ? 15.045 5.142   -4.824  0.60 16.15 ?  131 ILE   A HG22 1 
ATOM   2749 H HG22 B ILE   A 1 131 ? 15.853 5.410   -6.497  0.40 25.61 ?  131 ILE   A HG22 1 
ATOM   2750 H HG23 A ILE   A 1 131 ? 15.743 4.781   -3.443  0.60 16.15 ?  131 ILE   A HG23 1 
ATOM   2751 H HG23 B ILE   A 1 131 ? 15.835 5.096   -4.940  0.40 25.61 ?  131 ILE   A HG23 1 
ATOM   2752 H HD11 A ILE   A 1 131 ? 19.647 5.367   -3.320  0.60 18.52 ?  131 ILE   A HD11 1 
ATOM   2753 H HD11 B ILE   A 1 131 ? 19.941 5.211   -3.786  0.40 25.49 ?  131 ILE   A HD11 1 
ATOM   2754 H HD12 A ILE   A 1 131 ? 18.916 6.105   -4.522  0.60 18.52 ?  131 ILE   A HD12 1 
ATOM   2755 H HD12 B ILE   A 1 131 ? 19.754 5.644   -5.303  0.40 25.49 ?  131 ILE   A HD12 1 
ATOM   2756 H HD13 A ILE   A 1 131 ? 18.197 5.981   -3.111  0.60 18.52 ?  131 ILE   A HD13 1 
ATOM   2757 H HD13 B ILE   A 1 131 ? 18.709 6.120   -4.210  0.40 25.49 ?  131 ILE   A HD13 1 
ATOM   2758 N N    A PHE   A 1 132 ? 17.829 1.062   -5.875  0.60 10.60 ?  132 PHE   A N    1 
ATOM   2759 N N    B PHE   A 1 132 ? 18.177 0.917   -6.486  0.40 17.49 ?  132 PHE   A N    1 
ATOM   2760 C CA   A PHE   A 1 132 ? 18.702 0.218   -6.685  0.60 11.10 ?  132 PHE   A CA   1 
ATOM   2761 C CA   B PHE   A 1 132 ? 19.055 0.038   -7.245  0.40 16.87 ?  132 PHE   A CA   1 
ATOM   2762 C C    A PHE   A 1 132 ? 17.938 -0.544  -7.769  0.60 11.60 ?  132 PHE   A C    1 
ATOM   2763 C C    B PHE   A 1 132 ? 18.313 -0.713  -8.347  0.40 17.26 ?  132 PHE   A C    1 
ATOM   2764 O O    A PHE   A 1 132 ? 18.563 -1.173  -8.628  0.60 13.12 ?  132 PHE   A O    1 
ATOM   2765 O O    B PHE   A 1 132 ? 18.959 -1.354  -9.184  0.40 17.95 ?  132 PHE   A O    1 
ATOM   2766 C CB   A PHE   A 1 132 ? 19.490 -0.754  -5.797  0.60 10.86 ?  132 PHE   A CB   1 
ATOM   2767 C CB   B PHE   A 1 132 ? 19.801 -0.920  -6.308  0.40 15.66 ?  132 PHE   A CB   1 
ATOM   2768 C CG   A PHE   A 1 132 ? 20.713 -0.154  -5.122  0.60 10.51 ?  132 PHE   A CG   1 
ATOM   2769 C CG   B PHE   A 1 132 ? 21.007 -0.306  -5.632  0.40 15.31 ?  132 PHE   A CG   1 
ATOM   2770 C CD1  A PHE   A 1 132 ? 20.587 0.880   -4.210  0.60 10.99 ?  132 PHE   A CD1  1 
ATOM   2771 C CD1  B PHE   A 1 132 ? 20.877 0.781   -4.780  0.40 15.53 ?  132 PHE   A CD1  1 
ATOM   2772 C CD2  A PHE   A 1 132 ? 21.975 -0.677  -5.361  0.60 11.04 ?  132 PHE   A CD2  1 
ATOM   2773 C CD2  B PHE   A 1 132 ? 22.270 -0.841  -5.836  0.40 15.78 ?  132 PHE   A CD2  1 
ATOM   2774 C CE1  A PHE   A 1 132 ? 21.705 1.406   -3.576  0.60 11.44 ?  132 PHE   A CE1  1 
ATOM   2775 C CE1  B PHE   A 1 132 ? 21.991 1.331   -4.158  0.40 15.76 ?  132 PHE   A CE1  1 
ATOM   2776 C CE2  A PHE   A 1 132 ? 23.094 -0.163  -4.730  0.60 11.43 ?  132 PHE   A CE2  1 
ATOM   2777 C CE2  B PHE   A 1 132 ? 23.384 -0.297  -5.218  0.40 15.99 ?  132 PHE   A CE2  1 
ATOM   2778 C CZ   A PHE   A 1 132 ? 22.958 0.883   -3.835  0.60 11.17 ?  132 PHE   A CZ   1 
ATOM   2779 C CZ   B PHE   A 1 132 ? 23.244 0.789   -4.378  0.40 16.03 ?  132 PHE   A CZ   1 
ATOM   2780 H H    A PHE   A 1 132 ? 17.610 0.724   -5.107  0.60 12.71 ?  132 PHE   A H    1 
ATOM   2781 H H    B PHE   A 1 132 ? 17.948 0.617   -5.711  0.40 20.98 ?  132 PHE   A H    1 
ATOM   2782 H HA   A PHE   A 1 132 ? 19.341 0.795   -7.124  0.60 13.31 ?  132 PHE   A HA   1 
ATOM   2783 H HA   B PHE   A 1 132 ? 19.728 0.586   -7.673  0.40 20.23 ?  132 PHE   A HA   1 
ATOM   2784 H HB2  A PHE   A 1 132 ? 18.895 -1.075  -5.095  0.60 13.02 ?  132 PHE   A HB2  1 
ATOM   2785 H HB2  B PHE   A 1 132 ? 19.198 -1.213  -5.609  0.40 18.79 ?  132 PHE   A HB2  1 
ATOM   2786 H HB3  A PHE   A 1 132 ? 19.783 -1.494  -6.341  0.60 13.02 ?  132 PHE   A HB3  1 
ATOM   2787 H HB3  B PHE   A 1 132 ? 20.112 -1.683  -6.819  0.40 18.79 ?  132 PHE   A HB3  1 
ATOM   2788 H HD1  A PHE   A 1 132 ? 19.745 1.241   -4.026  0.60 13.18 ?  132 PHE   A HD1  1 
ATOM   2789 H HD1  B PHE   A 1 132 ? 20.040 1.152   -4.627  0.40 18.63 ?  132 PHE   A HD1  1 
ATOM   2790 H HD2  A PHE   A 1 132 ? 22.065 -1.380  -5.961  0.60 13.24 ?  132 PHE   A HD2  1 
ATOM   2791 H HD2  B PHE   A 1 132 ? 22.373 -1.572  -6.400  0.40 18.93 ?  132 PHE   A HD2  1 
ATOM   2792 H HE1  A PHE   A 1 132 ? 21.610 2.114   -2.971  0.60 13.72 ?  132 PHE   A HE1  1 
ATOM   2793 H HE1  B PHE   A 1 132 ? 21.897 2.064   -3.591  0.40 18.90 ?  132 PHE   A HE1  1 
ATOM   2794 H HE2  A PHE   A 1 132 ? 23.931 -0.517  -4.912  0.60 13.71 ?  132 PHE   A HE2  1 
ATOM   2795 H HE2  B PHE   A 1 132 ? 24.226 -0.665  -5.368  0.40 19.19 ?  132 PHE   A HE2  1 
ATOM   2796 H HZ   A PHE   A 1 132 ? 23.706 1.239   -3.413  0.60 13.39 ?  132 PHE   A HZ   1 
ATOM   2797 H HZ   B PHE   A 1 132 ? 23.993 1.156   -3.962  0.40 19.23 ?  132 PHE   A HZ   1 
ATOM   2798 N N    A GLY   A 1 133 ? 16.607 -0.509  -7.747  0.60 11.54 ?  133 GLY   A N    1 
ATOM   2799 N N    B GLY   A 1 133 ? 16.980 -0.651  -8.368  0.40 17.11 ?  133 GLY   A N    1 
ATOM   2800 C CA   A GLY   A 1 133 ? 15.810 -0.886  -8.899  0.60 12.74 ?  133 GLY   A CA   1 
ATOM   2801 C CA   B GLY   A 1 133 ? 16.198 -1.005  -9.530  0.40 17.21 ?  133 GLY   A CA   1 
ATOM   2802 C C    A GLY   A 1 133 ? 15.523 -2.357  -9.097  0.60 13.84 ?  133 GLY   A C    1 
ATOM   2803 C C    B GLY   A 1 133 ? 15.558 -2.380  -9.500  0.40 17.34 ?  133 GLY   A C    1 
ATOM   2804 O O    A GLY   A 1 133 ? 14.957 -2.708  -10.138 0.60 15.43 ?  133 GLY   A O    1 
ATOM   2805 O O    B GLY   A 1 133 ? 14.564 -2.592  -10.206 0.40 17.73 ?  133 GLY   A O    1 
ATOM   2806 H H    A GLY   A 1 133 ? 16.134 -0.261  -7.071  0.60 13.85 ?  133 GLY   A H    1 
ATOM   2807 H H    B GLY   A 1 133 ? 16.506 -0.402  -7.700  0.40 20.53 ?  133 GLY   A H    1 
ATOM   2808 H HA2  A GLY   A 1 133 ? 14.950 -0.442  -8.842  0.60 15.28 ?  133 GLY   A HA2  1 
ATOM   2809 H HA2  B GLY   A 1 133 ? 15.491 -0.350  -9.633  0.40 20.65 ?  133 GLY   A HA2  1 
ATOM   2810 H HA3  A GLY   A 1 133 ? 16.252 -0.572  -9.702  0.60 15.28 ?  133 GLY   A HA3  1 
ATOM   2811 H HA3  B GLY   A 1 133 ? 16.767 -0.952  -10.314 0.40 20.65 ?  133 GLY   A HA3  1 
ATOM   2812 N N    A ALA   A 1 134 ? 15.885 -3.232  -8.160  0.60 13.26 ?  134 ALA   A N    1 
ATOM   2813 N N    B ALA   A 1 134 ? 16.084 -3.313  -8.709  0.40 16.74 ?  134 ALA   A N    1 
ATOM   2814 C CA   A ALA   A 1 134 ? 15.567 -4.643  -8.327  0.60 13.98 ?  134 ALA   A CA   1 
ATOM   2815 C CA   B ALA   A 1 134 ? 15.639 -4.697  -8.795  0.40 16.81 ?  134 ALA   A CA   1 
ATOM   2816 C C    A ALA   A 1 134 ? 14.195 -4.968  -7.737  0.60 14.77 ?  134 ALA   A C    1 
ATOM   2817 C C    B ALA   A 1 134 ? 14.330 -4.909  -8.030  0.40 17.02 ?  134 ALA   A C    1 
ATOM   2818 O O    A ALA   A 1 134 ? 13.607 -4.190  -6.983  0.60 15.72 ?  134 ALA   A O    1 
ATOM   2819 O O    B ALA   A 1 134 ? 13.905 -4.081  -7.221  0.40 17.44 ?  134 ALA   A O    1 
ATOM   2820 C CB   A ALA   A 1 134 ? 16.640 -5.540  -7.710  0.60 14.48 ?  134 ALA   A CB   1 
ATOM   2821 C CB   B ALA   A 1 134 ? 16.721 -5.643  -8.278  0.40 16.82 ?  134 ALA   A CB   1 
ATOM   2822 H H    A ALA   A 1 134 ? 16.304 -3.034  -7.428  0.60 15.91 ?  134 ALA   A H    1 
ATOM   2823 H H    B ALA   A 1 134 ? 16.698 -3.167  -8.120  0.40 20.08 ?  134 ALA   A H    1 
ATOM   2824 H HA   A ALA   A 1 134 ? 15.530 -4.838  -9.272  0.60 16.77 ?  134 ALA   A HA   1 
ATOM   2825 H HA   B ALA   A 1 134 ? 15.482 -4.910  -9.727  0.40 20.17 ?  134 ALA   A HA   1 
ATOM   2826 H HB1  A ALA   A 1 134 ? 16.402 -6.466  -7.872  0.60 17.37 ?  134 ALA   A HB1  1 
ATOM   2827 H HB1  B ALA   A 1 134 ? 16.400 -6.555  -8.351  0.40 20.17 ?  134 ALA   A HB1  1 
ATOM   2828 H HB2  A ALA   A 1 134 ? 17.492 -5.339  -8.130  0.60 17.37 ?  134 ALA   A HB2  1 
ATOM   2829 H HB2  B ALA   A 1 134 ? 17.521 -5.531  -8.817  0.40 20.17 ?  134 ALA   A HB2  1 
ATOM   2830 H HB3  A ALA   A 1 134 ? 16.689 -5.369  -6.760  0.60 17.37 ?  134 ALA   A HB3  1 
ATOM   2831 H HB3  B ALA   A 1 134 ? 16.911 -5.431  -7.353  0.40 20.17 ?  134 ALA   A HB3  1 
ATOM   2832 N N    A ASP   A 1 135 ? 13.690 -6.143  -8.104  0.60 15.63 ?  135 ASP   A N    1 
ATOM   2833 N N    B ASP   A 1 135 ? 13.694 -6.051  -8.296  0.40 17.41 ?  135 ASP   A N    1 
ATOM   2834 C CA   A ASP   A 1 135 ? 12.438 -6.659  -7.563  0.60 16.29 ?  135 ASP   A CA   1 
ATOM   2835 C CA   B ASP   A 1 135 ? 12.421 -6.382  -7.662  0.40 17.69 ?  135 ASP   A CA   1 
ATOM   2836 C C    A ASP   A 1 135 ? 12.667 -7.090  -6.120  0.60 15.50 ?  135 ASP   A C    1 
ATOM   2837 C C    B ASP   A 1 135 ? 12.669 -6.890  -6.246  0.40 16.82 ?  135 ASP   A C    1 
ATOM   2838 O O    A ASP   A 1 135 ? 13.473 -7.997  -5.879  0.60 15.40 ?  135 ASP   A O    1 
ATOM   2839 O O    B ASP   A 1 135 ? 13.348 -7.909  -6.076  0.40 16.55 ?  135 ASP   A O    1 
ATOM   2840 C CB   A ASP   A 1 135 ? 12.007 -7.861  -8.399  0.60 18.22 ?  135 ASP   A CB   1 
ATOM   2841 C CB   B ASP   A 1 135 ? 11.695 -7.450  -8.472  0.40 19.05 ?  135 ASP   A CB   1 
ATOM   2842 C CG   A ASP   A 1 135 ? 10.716 -8.499  -7.906  0.60 19.82 ?  135 ASP   A CG   1 
ATOM   2843 C CG   B ASP   A 1 135 ? 10.312 -7.772  -7.923  0.40 20.54 ?  135 ASP   A CG   1 
ATOM   2844 O OD1  A ASP   A 1 135 ? 10.112 -7.993  -6.937  0.60 19.64 ?  135 ASP   A OD1  1 
ATOM   2845 O OD1  B ASP   A 1 135 ? 9.946  -7.247  -6.850  0.40 21.32 ?  135 ASP   A OD1  1 
ATOM   2846 O OD2  A ASP   A 1 135 ? 10.311 -9.523  -8.494  0.60 22.23 -1 135 ASP   A OD2  1 
ATOM   2847 O OD2  B ASP   A 1 135 ? 9.589  -8.560  -8.569  0.40 21.18 -1 135 ASP   A OD2  1 
ATOM   2848 H H    A ASP   A 1 135 ? 14.060 -6.668  -8.673  0.60 18.74 ?  135 ASP   A H    1 
ATOM   2849 H H    B ASP   A 1 135 ? 13.978 -6.652  -8.841  0.40 20.88 ?  135 ASP   A H    1 
ATOM   2850 H HA   A ASP   A 1 135 ? 11.746 -5.979  -7.611  0.60 19.54 ?  135 ASP   A HA   1 
ATOM   2851 H HA   B ASP   A 1 135 ? 11.862 -5.592  -7.640  0.40 21.22 ?  135 ASP   A HA   1 
ATOM   2852 H HB2  A ASP   A 1 135 ? 11.881 -7.581  -9.320  0.60 21.86 ?  135 ASP   A HB2  1 
ATOM   2853 H HB2  B ASP   A 1 135 ? 11.607 -7.143  -9.389  0.40 22.86 ?  135 ASP   A HB2  1 
ATOM   2854 H HB3  A ASP   A 1 135 ? 12.693 -8.544  -8.352  0.60 21.86 ?  135 ASP   A HB3  1 
ATOM   2855 H HB3  B ASP   A 1 135 ? 12.203 -8.272  -8.444  0.40 22.86 ?  135 ASP   A HB3  1 
ATOM   2856 N N    A PRO   A 1 136 ? 12.007 -6.475  -5.137  0.60 15.10 ?  136 PRO   A N    1 
ATOM   2857 N N    B PRO   A 1 136 ? 12.147 -6.222  -5.215  0.40 16.50 ?  136 PRO   A N    1 
ATOM   2858 C CA   A PRO   A 1 136 ? 12.245 -6.880  -3.741  0.60 14.98 ?  136 PRO   A CA   1 
ATOM   2859 C CA   B PRO   A 1 136 ? 12.399 -6.679  -3.836  0.40 16.51 ?  136 PRO   A CA   1 
ATOM   2860 C C    A PRO   A 1 136 ? 11.848 -8.311  -3.434  0.60 14.49 ?  136 PRO   A C    1 
ATOM   2861 C C    B PRO   A 1 136 ? 11.884 -8.077  -3.535  0.40 16.13 ?  136 PRO   A C    1 
ATOM   2862 O O    A PRO   A 1 136 ? 12.463 -8.937  -2.562  0.60 14.37 ?  136 PRO   A O    1 
ATOM   2863 O O    B PRO   A 1 136 ? 12.422 -8.739  -2.639  0.40 15.82 ?  136 PRO   A O    1 
ATOM   2864 C CB   A PRO   A 1 136 ? 11.421 -5.869  -2.933  0.60 15.54 ?  136 PRO   A CB   1 
ATOM   2865 C CB   B PRO   A 1 136 ? 11.722 -5.601  -2.975  0.40 16.62 ?  136 PRO   A CB   1 
ATOM   2866 C CG   A PRO   A 1 136 ? 10.400 -5.348  -3.892  0.60 15.85 ?  136 PRO   A CG   1 
ATOM   2867 C CG   B PRO   A 1 136 ? 10.815 -4.865  -3.908  0.40 16.97 ?  136 PRO   A CG   1 
ATOM   2868 C CD   A PRO   A 1 136 ? 11.044 -5.366  -5.242  0.60 15.19 ?  136 PRO   A CD   1 
ATOM   2869 C CD   B PRO   A 1 136 ? 11.427 -4.941  -5.251  0.40 16.79 ?  136 PRO   A CD   1 
ATOM   2870 H HA   A PRO   A 1 136 ? 13.185 -6.771  -3.523  0.60 17.97 ?  136 PRO   A HA   1 
ATOM   2871 H HA   B PRO   A 1 136 ? 13.349 -6.663  -3.650  0.40 19.81 ?  136 PRO   A HA   1 
ATOM   2872 H HB2  A PRO   A 1 136 ? 10.997 -6.324  -2.186  0.60 18.65 ?  136 PRO   A HB2  1 
ATOM   2873 H HB2  B PRO   A 1 136 ? 11.213 -6.015  -2.262  0.40 19.93 ?  136 PRO   A HB2  1 
ATOM   2874 H HB3  A PRO   A 1 136 ? 12.002 -5.162  -2.619  0.60 18.65 ?  136 PRO   A HB3  1 
ATOM   2875 H HB3  B PRO   A 1 136 ? 12.393 -4.999  -2.611  0.40 19.93 ?  136 PRO   A HB3  1 
ATOM   2876 H HG2  A PRO   A 1 136 ? 9.620  -5.923  -3.881  0.60 19.02 ?  136 PRO   A HG2  1 
ATOM   2877 H HG2  B PRO   A 1 136 ? 9.946  -5.291  -3.918  0.40 20.35 ?  136 PRO   A HG2  1 
ATOM   2878 H HG3  A PRO   A 1 136 ? 10.162 -4.442  -3.646  0.60 19.02 ?  136 PRO   A HG3  1 
ATOM   2879 H HG3  B PRO   A 1 136 ? 10.739 -3.941  -3.630  0.40 20.35 ?  136 PRO   A HG3  1 
ATOM   2880 H HD2  A PRO   A 1 136 ? 10.382 -5.560  -5.928  0.60 18.22 ?  136 PRO   A HD2  1 
ATOM   2881 H HD2  B PRO   A 1 136 ? 10.739 -4.955  -5.935  0.40 20.14 ?  136 PRO   A HD2  1 
ATOM   2882 H HD3  A PRO   A 1 136 ? 11.505 -4.533  -5.417  0.60 18.22 ?  136 PRO   A HD3  1 
ATOM   2883 H HD3  B PRO   A 1 136 ? 12.053 -4.210  -5.390  0.40 20.14 ?  136 PRO   A HD3  1 
ATOM   2884 N N    A ILE   A 1 137 ? 10.820 -8.843  -4.098  0.60 14.67 ?  137 ILE   A N    1 
ATOM   2885 N N    B ILE   A 1 137 ? 10.853 -8.547  -4.240  0.40 16.35 ?  137 ILE   A N    1 
ATOM   2886 C CA   A ILE   A 1 137 ? 10.466 -10.247 -3.905  0.60 14.74 ?  137 ILE   A CA   1 
ATOM   2887 C CA   B ILE   A 1 137 ? 10.414 -9.932  -4.078  0.40 16.68 ?  137 ILE   A CA   1 
ATOM   2888 C C    A ILE   A 1 137 ? 11.626 -11.140 -4.323  0.60 14.46 ?  137 ILE   A C    1 
ATOM   2889 C C    B ILE   A 1 137 ? 11.564 -10.878 -4.389  0.40 16.77 ?  137 ILE   A C    1 
ATOM   2890 O O    A ILE   A 1 137 ? 11.956 -12.119 -3.642  0.60 14.29 ?  137 ILE   A O    1 
ATOM   2891 O O    B ILE   A 1 137 ? 11.824 -11.845 -3.661  0.40 17.01 ?  137 ILE   A O    1 
ATOM   2892 C CB   A ILE   A 1 137 ? 9.162  -10.587 -4.654  0.60 15.54 ?  137 ILE   A CB   1 
ATOM   2893 C CB   B ILE   A 1 137 ? 9.197  -10.210 -4.980  0.40 17.21 ?  137 ILE   A CB   1 
ATOM   2894 C CG1  A ILE   A 1 137 ? 8.002  -9.723  -4.139  0.60 17.04 ?  137 ILE   A CG1  1 
ATOM   2895 C CG1  B ILE   A 1 137 ? 8.034  -9.282  -4.608  0.40 18.07 ?  137 ILE   A CG1  1 
ATOM   2896 C CG2  A ILE   A 1 137 ? 8.824  -12.072 -4.502  0.60 15.72 ?  137 ILE   A CG2  1 
ATOM   2897 C CG2  B ILE   A 1 137 ? 8.799  -11.684 -4.904  0.40 17.32 ?  137 ILE   A CG2  1 
ATOM   2898 C CD1  A ILE   A 1 137 ? 6.695  -9.933  -4.879  0.60 18.18 ?  137 ILE   A CD1  1 
ATOM   2899 C CD1  B ILE   A 1 137 ? 6.819  -9.426  -5.500  0.40 18.56 ?  137 ILE   A CD1  1 
ATOM   2900 H H    A ILE   A 1 137 ? 10.319 -8.430  -4.657  0.60 17.60 ?  137 ILE   A H    1 
ATOM   2901 H H    B ILE   A 1 137 ? 10.400 -8.089  -4.812  0.40 19.61 ?  137 ILE   A H    1 
ATOM   2902 H HA   A ILE   A 1 137 ? 10.313 -10.413 -2.966  0.60 17.68 ?  137 ILE   A HA   1 
ATOM   2903 H HA   B ILE   A 1 137 ? 10.144 -10.077 -3.160  0.40 20.01 ?  137 ILE   A HA   1 
ATOM   2904 H HB   A ILE   A 1 137 ? 9.285  -10.404 -5.596  0.60 18.64 ?  137 ILE   A HB   1 
ATOM   2905 H HB   B ILE   A 1 137 ? 9.454  -10.014 -5.894  0.40 20.64 ?  137 ILE   A HB   1 
ATOM   2906 H HG12 A ILE   A 1 137 ? 7.853  -9.925  -3.203  0.60 20.44 ?  137 ILE   A HG12 1 
ATOM   2907 H HG12 B ILE   A 1 137 ? 7.761  -9.476  -3.699  0.40 21.68 ?  137 ILE   A HG12 1 
ATOM   2908 H HG13 A ILE   A 1 137 ? 8.249  -8.787  -4.237  0.60 20.44 ?  137 ILE   A HG13 1 
ATOM   2909 H HG13 B ILE   A 1 137 ? 8.334  -8.360  -4.669  0.40 21.68 ?  137 ILE   A HG13 1 
ATOM   2910 H HG21 A ILE   A 1 137 ? 7.977  -12.265 -4.939  0.60 18.86 ?  137 ILE   A HG21 1 
ATOM   2911 H HG21 B ILE   A 1 137 ? 7.977  -11.818 -5.399  0.40 20.77 ?  137 ILE   A HG21 1 
ATOM   2912 H HG22 A ILE   A 1 137 ? 9.520  -12.601 -4.915  0.60 18.86 ?  137 ILE   A HG22 1 
ATOM   2913 H HG22 B ILE   A 1 137 ? 9.504  -12.224 -5.294  0.40 20.77 ?  137 ILE   A HG22 1 
ATOM   2914 H HG23 A ILE   A 1 137 ? 8.758  -12.283 -3.560  0.60 18.86 ?  137 ILE   A HG23 1 
ATOM   2915 H HG23 B ILE   A 1 137 ? 8.670  -11.927 -3.975  0.40 20.77 ?  137 ILE   A HG23 1 
ATOM   2916 H HD11 A ILE   A 1 137 ? 6.004  -10.162 -4.239  0.60 21.80 ?  137 ILE   A HD11 1 
ATOM   2917 H HD11 B ILE   A 1 137 ? 6.221  -8.681  -5.339  0.40 22.27 ?  137 ILE   A HD11 1 
ATOM   2918 H HD12 A ILE   A 1 137 ? 6.473  -9.112  -5.337  0.60 21.80 ?  137 ILE   A HD12 1 
ATOM   2919 H HD12 B ILE   A 1 137 ? 7.107  -9.427  -6.426  0.40 22.27 ?  137 ILE   A HD12 1 
ATOM   2920 H HD13 A ILE   A 1 137 ? 6.798  -10.645 -5.529  0.60 21.80 ?  137 ILE   A HD13 1 
ATOM   2921 H HD13 B ILE   A 1 137 ? 6.372  -10.261 -5.291  0.40 22.27 ?  137 ILE   A HD13 1 
ATOM   2922 N N    A HIS   A 1 138 ? 12.257 -10.821 -5.455  0.60 14.85 ?  138 HIS   A N    1 
ATOM   2923 N N    B HIS   A 1 138 ? 12.263 -10.609 -5.488  0.40 16.60 ?  138 HIS   A N    1 
ATOM   2924 C CA   A HIS   A 1 138 ? 13.448 -11.556 -5.864  0.60 15.07 ?  138 HIS   A CA   1 
ATOM   2925 C CA   B HIS   A 1 138 ? 13.388 -11.440 -5.897  0.40 15.89 ?  138 HIS   A CA   1 
ATOM   2926 C C    A HIS   A 1 138 ? 14.579 -11.379 -4.858  0.60 14.30 ?  138 HIS   A C    1 
ATOM   2927 C C    B HIS   A 1 138 ? 14.541 -11.350 -4.902  0.40 14.90 ?  138 HIS   A C    1 
ATOM   2928 O O    A HIS   A 1 138 ? 15.249 -12.354 -4.492  0.60 14.42 ?  138 HIS   A O    1 
ATOM   2929 O O    B HIS   A 1 138 ? 15.185 -12.360 -4.590  0.40 15.11 ?  138 HIS   A O    1 
ATOM   2930 C CB   A HIS   A 1 138 ? 13.882 -11.132 -7.266  0.60 16.01 ?  138 HIS   A CB   1 
ATOM   2931 C CB   B HIS   A 1 138 ? 13.819 -11.003 -7.295  0.40 16.19 ?  138 HIS   A CB   1 
ATOM   2932 C CG   A HIS   A 1 138 ? 15.130 -11.813 -7.734  0.60 17.09 ?  138 HIS   A CG   1 
ATOM   2933 C CG   B HIS   A 1 138 ? 15.125 -11.577 -7.734  0.40 16.79 ?  138 HIS   A CG   1 
ATOM   2934 N ND1  A HIS   A 1 138 ? 15.211 -13.178 -7.918  0.60 18.21 ?  138 HIS   A ND1  1 
ATOM   2935 N ND1  B HIS   A 1 138 ? 15.280 -12.901 -8.082  0.40 17.41 ?  138 HIS   A ND1  1 
ATOM   2936 C CD2  A HIS   A 1 138 ? 16.354 -11.321 -8.035  0.60 17.28 ?  138 HIS   A CD2  1 
ATOM   2937 C CD2  B HIS   A 1 138 ? 16.342 -11.003 -7.882  0.40 16.77 ?  138 HIS   A CD2  1 
ATOM   2938 C CE1  A HIS   A 1 138 ? 16.427 -13.494 -8.324  0.60 18.39 ?  138 HIS   A CE1  1 
ATOM   2939 C CE1  B HIS   A 1 138 ? 16.535 -13.119 -8.427  0.40 17.37 ?  138 HIS   A CE1  1 
ATOM   2940 N NE2  A HIS   A 1 138 ? 17.141 -12.385 -8.402  0.60 17.82 ?  138 HIS   A NE2  1 
ATOM   2941 N NE2  B HIS   A 1 138 ? 17.201 -11.983 -8.314  0.40 16.99 ?  138 HIS   A NE2  1 
ATOM   2942 H H    A HIS   A 1 138 ? 12.022 -10.191 -5.996  0.60 17.81 ?  138 HIS   A H    1 
ATOM   2943 H H    B HIS   A 1 138 ? 12.099 -9.950  -6.016  0.40 19.91 ?  138 HIS   A H    1 
ATOM   2944 H HA   A HIS   A 1 138 ? 13.236 -12.499 -5.904  0.60 18.08 ?  138 HIS   A HA   1 
ATOM   2945 H HA   B HIS   A 1 138 ? 13.100 -12.361 -5.943  0.40 19.06 ?  138 HIS   A HA   1 
ATOM   2946 H HB2  A HIS   A 1 138 ? 13.173 -11.349 -7.897  0.60 19.21 ?  138 HIS   A HB2  1 
ATOM   2947 H HB2  B HIS   A 1 138 ? 13.139 -11.283 -7.932  0.40 19.42 ?  138 HIS   A HB2  1 
ATOM   2948 H HB3  A HIS   A 1 138 ? 14.046 -10.177 -7.275  0.60 19.21 ?  138 HIS   A HB3  1 
ATOM   2949 H HB3  B HIS   A 1 138 ? 13.897 -10.035 -7.311  0.40 19.42 ?  138 HIS   A HB3  1 
ATOM   2950 H HD1  A HIS   A 1 138 ? 14.566 -13.735 -7.796  0.60 21.84 ?  138 HIS   A HD1  1 
ATOM   2951 H HD2  A HIS   A 1 138 ? 16.611 -10.428 -8.004  0.60 20.73 ?  138 HIS   A HD2  1 
ATOM   2952 H HD2  B HIS   A 1 138 ? 16.552 -10.112 -7.722  0.40 20.12 ?  138 HIS   A HD2  1 
ATOM   2953 H HE1  A HIS   A 1 138 ? 16.731 -14.351 -8.518  0.60 22.07 ?  138 HIS   A HE1  1 
ATOM   2954 H HE1  B HIS   A 1 138 ? 16.886 -13.934 -8.701  0.40 20.83 ?  138 HIS   A HE1  1 
ATOM   2955 H HE2  B HIS   A 1 138 ? 18.033 -11.875 -8.483  0.40 20.38 ?  138 HIS   A HE2  1 
ATOM   2956 N N    . SER   A 1 139 ? 14.810 -10.149 -4.392  1.00 13.91 ?  139 SER   A N    1 
ATOM   2957 C CA   . SER   A 1 139 ? 15.881 -9.957  -3.424  1.00 13.82 ?  139 SER   A CA   1 
ATOM   2958 C C    . SER   A 1 139 ? 15.663 -10.798 -2.173  1.00 13.32 ?  139 SER   A C    1 
ATOM   2959 O O    . SER   A 1 139 ? 16.611 -11.388 -1.643  1.00 13.49 ?  139 SER   A O    1 
ATOM   2960 C CB   . SER   A 1 139 ? 16.005 -8.477  -3.068  1.00 13.96 ?  139 SER   A CB   1 
ATOM   2961 O OG   . SER   A 1 139 ? 17.093 -8.301  -2.177  1.00 14.22 ?  139 SER   A OG   1 
ATOM   2962 H H    A SER   A 1 139 ? 14.376 -9.438  -4.608  0.60 16.69 ?  139 SER   A H    1 
ATOM   2963 H H    B SER   A 1 139 ? 14.382 -9.428  -4.590  0.40 16.69 ?  139 SER   A H    1 
ATOM   2964 H HA   . SER   A 1 139 ? 16.721 -10.229 -3.822  1.00 16.58 ?  139 SER   A HA   1 
ATOM   2965 H HB2  . SER   A 1 139 ? 16.170 -7.959  -3.869  1.00 16.75 ?  139 SER   A HB2  1 
ATOM   2966 H HB3  . SER   A 1 139 ? 15.182 -8.178  -2.643  1.00 16.75 ?  139 SER   A HB3  1 
ATOM   2967 H HG   . SER   A 1 139 ? 17.173 -7.487  -1.961  1.00 17.06 ?  139 SER   A HG   1 
ATOM   2968 N N    . LEU   A 1 140 ? 14.424 -10.861 -1.682  1.00 13.16 ?  140 LEU   A N    1 
ATOM   2969 C CA   . LEU   A 1 140 ? 14.148 -11.673 -0.501  1.00 13.13 ?  140 LEU   A CA   1 
ATOM   2970 C C    . LEU   A 1 140 ? 14.414 -13.148 -0.779  1.00 13.19 ?  140 LEU   A C    1 
ATOM   2971 O O    . LEU   A 1 140 ? 14.971 -13.861 0.067   1.00 14.07 ?  140 LEU   A O    1 
ATOM   2972 C CB   . LEU   A 1 140 ? 12.705 -11.462 -0.055  1.00 13.76 ?  140 LEU   A CB   1 
ATOM   2973 C CG   . LEU   A 1 140 ? 12.244 -12.301 1.134   1.00 14.38 ?  140 LEU   A CG   1 
ATOM   2974 C CD1  . LEU   A 1 140 ? 13.141 -12.093 2.344   1.00 14.73 ?  140 LEU   A CD1  1 
ATOM   2975 C CD2  . LEU   A 1 140 ? 10.787 -11.982 1.468   1.00 15.31 ?  140 LEU   A CD2  1 
ATOM   2976 H H    . LEU   A 1 140 ? 13.739 -10.452 -2.005  1.00 15.79 ?  140 LEU   A H    1 
ATOM   2977 H HA   . LEU   A 1 140 ? 14.730 -11.393 0.220   1.00 15.75 ?  140 LEU   A HA   1 
ATOM   2978 H HB2  . LEU   A 1 140 ? 12.591 -10.536 0.189   1.00 16.50 ?  140 LEU   A HB2  1 
ATOM   2979 H HB3  . LEU   A 1 140 ? 12.122 -11.678 -0.801  1.00 16.50 ?  140 LEU   A HB3  1 
ATOM   2980 H HG   . LEU   A 1 140 ? 12.282 -13.242 0.891   1.00 17.25 ?  140 LEU   A HG   1 
ATOM   2981 H HD11 . LEU   A 1 140 ? 12.754 -12.552 3.105   1.00 17.66 ?  140 LEU   A HD11 1 
ATOM   2982 H HD12 . LEU   A 1 140 ? 14.018 -12.462 2.148   1.00 17.66 ?  140 LEU   A HD12 1 
ATOM   2983 H HD13 . LEU   A 1 140 ? 13.210 -11.146 2.523   1.00 17.66 ?  140 LEU   A HD13 1 
ATOM   2984 H HD21 . LEU   A 1 140 ? 10.505 -12.528 2.223   1.00 18.37 ?  140 LEU   A HD21 1 
ATOM   2985 H HD22 . LEU   A 1 140 ? 10.710 -11.044 1.696   1.00 18.37 ?  140 LEU   A HD22 1 
ATOM   2986 H HD23 . LEU   A 1 140 ? 10.229 -12.182 0.697   1.00 18.37 ?  140 LEU   A HD23 1 
ATOM   2987 N N    . ARG   A 1 141 ? 14.026 -13.620 -1.965  1.00 14.13 ?  141 ARG   A N    1 
ATOM   2988 C CA   . ARG   A 1 141 ? 14.266 -15.010 -2.334  1.00 15.14 ?  141 ARG   A CA   1 
ATOM   2989 C C    . ARG   A 1 141 ? 15.761 -15.318 -2.340  1.00 14.23 ?  141 ARG   A C    1 
ATOM   2990 O O    . ARG   A 1 141 ? 16.206 -16.330 -1.782  1.00 14.47 ?  141 ARG   A O    1 
ATOM   2991 C CB   . ARG   A 1 141 ? 13.652 -15.263 -3.712  1.00 17.17 ?  141 ARG   A CB   1 
ATOM   2992 C CG   . ARG   A 1 141 ? 13.662 -16.703 -4.165  1.00 19.74 ?  141 ARG   A CG   1 
ATOM   2993 C CD   . ARG   A 1 141 ? 12.642 -17.495 -3.402  1.00 22.05 ?  141 ARG   A CD   1 
ATOM   2994 N NE   . ARG   A 1 141 ? 13.251 -18.238 -2.311  1.00 22.88 ?  141 ARG   A NE   1 
ATOM   2995 C CZ   . ARG   A 1 141 ? 12.560 -18.834 -1.347  1.00 23.95 ?  141 ARG   A CZ   1 
ATOM   2996 N NH1  . ARG   A 1 141 ? 11.255 -18.659 -1.223  1.00 23.94 ?  141 ARG   A NH1  1 
ATOM   2997 N NH2  . ARG   A 1 141 ? 13.198 -19.610 -0.476  1.00 24.81 ?  141 ARG   A NH2  1 
ATOM   2998 H H    . ARG   A 1 141 ? 13.625 -13.157 -2.570  1.00 16.95 ?  141 ARG   A H    1 
ATOM   2999 H HA   . ARG   A 1 141 ? 13.836 -15.595 -1.694  1.00 18.16 ?  141 ARG   A HA   1 
ATOM   3000 H HB2  . ARG   A 1 141 ? 12.729 -14.961 -3.702  1.00 20.59 ?  141 ARG   A HB2  1 
ATOM   3001 H HB3  . ARG   A 1 141 ? 14.149 -14.750 -4.368  1.00 20.59 ?  141 ARG   A HB3  1 
ATOM   3002 H HG2  . ARG   A 1 141 ? 13.443 -16.750 -5.111  1.00 23.69 ?  141 ARG   A HG2  1 
ATOM   3003 H HG3  . ARG   A 1 141 ? 14.537 -17.094 -4.004  1.00 23.69 ?  141 ARG   A HG3  1 
ATOM   3004 H HD2  . ARG   A 1 141 ? 11.983 -16.892 -3.020  1.00 26.45 ?  141 ARG   A HD2  1 
ATOM   3005 H HD3  . ARG   A 1 141 ? 12.205 -18.122 -4.003  1.00 26.45 ?  141 ARG   A HD3  1 
ATOM   3006 H HE   . ARG   A 1 141 ? 14.092 -18.398 -2.357  1.00 27.45 ?  141 ARG   A HE   1 
ATOM   3007 H HH11 . ARG   A 1 141 ? 10.825 -18.173 -1.787  1.00 28.72 ?  141 ARG   A HH11 1 
ATOM   3008 H HH12 . ARG   A 1 141 ? 10.826 -19.054 -0.587  1.00 28.72 ?  141 ARG   A HH12 1 
ATOM   3009 H HH21 . ARG   A 1 141 ? 14.048 -19.724 -0.544  1.00 29.77 ?  141 ARG   A HH21 1 
ATOM   3010 H HH22 . ARG   A 1 141 ? 12.764 -19.989 0.163   1.00 29.77 ?  141 ARG   A HH22 1 
ATOM   3011 N N    . VAL   A 1 142 ? 16.558 -14.456 -2.977  1.00 13.66 ?  142 VAL   A N    1 
ATOM   3012 C CA   . VAL   A 1 142 ? 18.002 -14.672 -2.999  1.00 13.41 ?  142 VAL   A CA   1 
ATOM   3013 C C    . VAL   A 1 142 ? 18.563 -14.642 -1.583  1.00 12.94 ?  142 VAL   A C    1 
ATOM   3014 O O    . VAL   A 1 142 ? 19.428 -15.450 -1.229  1.00 13.48 ?  142 VAL   A O    1 
ATOM   3015 C CB   . VAL   A 1 142 ? 18.701 -13.656 -3.922  1.00 13.86 ?  142 VAL   A CB   1 
ATOM   3016 C CG1  . VAL   A 1 142 ? 20.213 -13.856 -3.880  1.00 13.55 ?  142 VAL   A CG1  1 
ATOM   3017 C CG2  . VAL   A 1 142 ? 18.205 -13.793 -5.350  1.00 15.15 ?  142 VAL   A CG2  1 
ATOM   3018 H H    . VAL   A 1 142 ? 16.293 -13.745 -3.397  1.00 16.38 ?  142 VAL   A H    1 
ATOM   3019 H HA   . VAL   A 1 142 ? 18.174 -15.548 -3.362  1.00 16.09 ?  142 VAL   A HA   1 
ATOM   3020 H HB   . VAL   A 1 142 ? 18.510 -12.751 -3.622  1.00 16.63 ?  142 VAL   A HB   1 
ATOM   3021 H HG11 . VAL   A 1 142 ? 20.622 -13.363 -4.611  1.00 16.25 ?  142 VAL   A HG11 1 
ATOM   3022 H HG12 . VAL   A 1 142 ? 20.557 -13.524 -3.033  1.00 16.25 ?  142 VAL   A HG12 1 
ATOM   3023 H HG13 . VAL   A 1 142 ? 20.411 -14.800 -3.970  1.00 16.25 ?  142 VAL   A HG13 1 
ATOM   3024 H HG21 . VAL   A 1 142 ? 18.682 -13.161 -5.912  1.00 18.17 ?  142 VAL   A HG21 1 
ATOM   3025 H HG22 . VAL   A 1 142 ? 18.381 -14.699 -5.653  1.00 18.17 ?  142 VAL   A HG22 1 
ATOM   3026 H HG23 . VAL   A 1 142 ? 17.258 -13.611 -5.372  1.00 18.17 ?  142 VAL   A HG23 1 
ATOM   3027 N N    . CYS   A 1 143 ? 18.093 -13.709 -0.755  1.00 12.70 ?  143 CYS   A N    1 
ATOM   3028 C CA   . CYS   A 1 143 ? 18.549 -13.657 0.631   1.00 13.09 ?  143 CYS   A CA   1 
ATOM   3029 C C    . CYS   A 1 143 ? 18.328 -14.995 1.328   1.00 12.90 ?  143 CYS   A C    1 
ATOM   3030 O O    . CYS   A 1 143 ? 19.251 -15.570 1.909   1.00 12.97 ?  143 CYS   A O    1 
ATOM   3031 C CB   . CYS   A 1 143 ? 17.821 -12.539 1.373   1.00 13.24 ?  143 CYS   A CB   1 
ATOM   3032 S SG   . CYS   A 1 143 ? 18.312 -12.359 3.087   1.00 14.16 ?  143 CYS   A SG   1 
ATOM   3033 H H    . CYS   A 1 143 ? 17.520 -13.109 -0.966  1.00 15.23 ?  143 CYS   A H    1 
ATOM   3034 H HA   . CYS   A 1 143 ? 19.499 -13.468 0.649   1.00 15.71 ?  143 CYS   A HA   1 
ATOM   3035 H HB2  . CYS   A 1 143 ? 17.993 -11.699 0.921   1.00 15.88 ?  143 CYS   A HB2  1 
ATOM   3036 H HB3  . CYS   A 1 143 ? 16.870 -12.724 1.359   1.00 15.88 ?  143 CYS   A HB3  1 
ATOM   3037 H HG   . CYS   A 1 143 ? 17.760 -11.394 3.542   1.00 16.98 ?  143 CYS   A HG   1 
ATOM   3038 N N    . VAL   A 1 144 ? 17.100 -15.504 1.277   1.00 13.76 ?  144 VAL   A N    1 
ATOM   3039 C CA   . VAL   A 1 144 ? 16.767 -16.733 1.986   1.00 15.13 ?  144 VAL   A CA   1 
ATOM   3040 C C    . VAL   A 1 144 ? 17.586 -17.903 1.463   1.00 14.82 ?  144 VAL   A C    1 
ATOM   3041 O O    . VAL   A 1 144 ? 17.961 -18.805 2.222   1.00 15.49 ?  144 VAL   A O    1 
ATOM   3042 C CB   . VAL   A 1 144 ? 15.251 -16.977 1.868   1.00 17.85 ?  144 VAL   A CB   1 
ATOM   3043 C CG1  . VAL   A 1 144 ? 14.895 -18.409 2.210   1.00 19.53 ?  144 VAL   A CG1  1 
ATOM   3044 C CG2  . VAL   A 1 144 ? 14.502 -15.973 2.749   1.00 17.81 ?  144 VAL   A CG2  1 
ATOM   3045 H H    . VAL   A 1 144 ? 16.441 -15.155 0.840   1.00 16.50 ?  144 VAL   A H    1 
ATOM   3046 H HA   . VAL   A 1 144 ? 16.968 -16.619 2.923   1.00 18.15 ?  144 VAL   A HA   1 
ATOM   3047 H HB   . VAL   A 1 144 ? 14.973 -16.815 0.949   1.00 21.42 ?  144 VAL   A HB   1 
ATOM   3048 H HG11 . VAL   A 1 144 ? 13.943 -18.460 2.404   1.00 23.43 ?  144 VAL   A HG11 1 
ATOM   3049 H HG12 . VAL   A 1 144 ? 15.104 -18.977 1.453   1.00 23.43 ?  144 VAL   A HG12 1 
ATOM   3050 H HG13 . VAL   A 1 144 ? 15.404 -18.681 2.986   1.00 23.43 ?  144 VAL   A HG13 1 
ATOM   3051 H HG21 . VAL   A 1 144 ? 13.544 -16.126 2.672   1.00 21.37 ?  144 VAL   A HG21 1 
ATOM   3052 H HG22 . VAL   A 1 144 ? 14.779 -16.088 3.671   1.00 21.37 ?  144 VAL   A HG22 1 
ATOM   3053 H HG23 . VAL   A 1 144 ? 14.710 -15.069 2.453   1.00 21.37 ?  144 VAL   A HG23 1 
ATOM   3054 N N    . ASP   A 1 145 ? 17.848 -17.926 0.161   1.00 14.94 ?  145 ASP   A N    1 
ATOM   3055 C CA   . ASP   A 1 145 ? 18.557 -19.035 -0.469  1.00 15.51 ?  145 ASP   A CA   1 
ATOM   3056 C C    . ASP   A 1 145 ? 20.077 -18.889 -0.423  1.00 15.14 ?  145 ASP   A C    1 
ATOM   3057 O O    . ASP   A 1 145 ? 20.783 -19.782 -0.906  1.00 16.99 ?  145 ASP   A O    1 
ATOM   3058 C CB   . ASP   A 1 145 ? 18.110 -19.171 -1.926  1.00 17.13 ?  145 ASP   A CB   1 
ATOM   3059 C CG   . ASP   A 1 145 ? 16.664 -19.607 -2.054  1.00 19.54 ?  145 ASP   A CG   1 
ATOM   3060 O OD1  . ASP   A 1 145 ? 16.100 -20.137 -1.071  1.00 20.01 ?  145 ASP   A OD1  1 
ATOM   3061 O OD2  . ASP   A 1 145 ? 16.095 -19.411 -3.144  1.00 21.13 -1 145 ASP   A OD2  1 
ATOM   3062 H H    . ASP   A 1 145 ? 17.602 -17.312 -0.388  1.00 17.92 ?  145 ASP   A H    1 
ATOM   3063 H HA   . ASP   A 1 145 ? 18.317 -19.856 -0.012  1.00 18.61 ?  145 ASP   A HA   1 
ATOM   3064 H HB2  . ASP   A 1 145 ? 18.213 -18.313 -2.371  1.00 20.55 ?  145 ASP   A HB2  1 
ATOM   3065 H HB3  . ASP   A 1 145 ? 18.655 -19.840 -2.363  1.00 20.55 ?  145 ASP   A HB3  1 
ATOM   3066 N N    . THR   A 1 146 ? 20.599 -17.795 0.128   1.00 13.30 ?  146 THR   A N    1 
ATOM   3067 C CA   . THR   A 1 146 ? 22.038 -17.541 0.152   1.00 12.76 ?  146 THR   A CA   1 
ATOM   3068 C C    . THR   A 1 146 ? 22.587 -17.354 1.551   1.00 12.89 ?  146 THR   A C    1 
ATOM   3069 O O    . THR   A 1 146 ? 23.664 -17.879 1.864   1.00 13.96 ?  146 THR   A O    1 
ATOM   3070 C CB   . THR   A 1 146 ? 22.362 -16.288 -0.680  1.00 13.02 ?  146 THR   A CB   1 
ATOM   3071 O OG1  . THR   A 1 146 ? 21.847 -16.454 -2.002  1.00 13.65 ?  146 THR   A OG1  1 
ATOM   3072 C CG2  . THR   A 1 146 ? 23.862 -16.060 -0.758  1.00 13.27 ?  146 THR   A CG2  1 
ATOM   3073 H H    . THR   A 1 146 ? 20.129 -17.166 0.494   1.00 15.96 ?  146 THR   A H    1 
ATOM   3074 H HA   . THR   A 1 146 ? 22.497 -18.288 -0.249  1.00 15.31 ?  146 THR   A HA   1 
ATOM   3075 H HB   . THR   A 1 146 ? 21.958 -15.507 -0.267  1.00 15.61 ?  146 THR   A HB   1 
ATOM   3076 H HG1  . THR   A 1 146 ? 21.009 -16.534 -1.971  1.00 16.38 ?  146 THR   A HG1  1 
ATOM   3077 H HG21 . THR   A 1 146 ? 24.061 -15.404 -1.444  1.00 15.92 ?  146 THR   A HG21 1 
ATOM   3078 H HG22 . THR   A 1 146 ? 24.197 -15.737 0.093   1.00 15.92 ?  146 THR   A HG22 1 
ATOM   3079 H HG23 . THR   A 1 146 ? 24.311 -16.892 -0.980  1.00 15.92 ?  146 THR   A HG23 1 
ATOM   3080 N N    . VAL   A 1 147 ? 21.904 -16.577 2.382   1.00 12.71 ?  147 VAL   A N    1 
ATOM   3081 C CA   . VAL   A 1 147 ? 22.384 -16.284 3.722   1.00 12.91 ?  147 VAL   A CA   1 
ATOM   3082 C C    . VAL   A 1 147 ? 22.064 -17.455 4.637   1.00 13.32 ?  147 VAL   A C    1 
ATOM   3083 O O    . VAL   A 1 147 ? 20.923 -17.933 4.684   1.00 13.86 ?  147 VAL   A O    1 
ATOM   3084 C CB   . VAL   A 1 147 ? 21.760 -14.981 4.240   1.00 12.97 ?  147 VAL   A CB   1 
ATOM   3085 C CG1  . VAL   A 1 147 ? 22.294 -14.669 5.619   1.00 14.08 ?  147 VAL   A CG1  1 
ATOM   3086 C CG2  . VAL   A 1 147 ? 22.023 -13.840 3.265   1.00 13.35 ?  147 VAL   A CG2  1 
ATOM   3087 H H    . VAL   A 1 147 ? 21.149 -16.209 2.195   1.00 15.25 ?  147 VAL   A H    1 
ATOM   3088 H HA   . VAL   A 1 147 ? 23.345 -16.172 3.700   1.00 15.49 ?  147 VAL   A HA   1 
ATOM   3089 H HB   . VAL   A 1 147 ? 20.802 -15.097 4.315   1.00 15.55 ?  147 VAL   A HB   1 
ATOM   3090 H HG11 . VAL   A 1 147 ? 22.050 -13.764 5.854   1.00 16.89 ?  147 VAL   A HG11 1 
ATOM   3091 H HG12 . VAL   A 1 147 ? 21.904 -15.292 6.257   1.00 16.89 ?  147 VAL   A HG12 1 
ATOM   3092 H HG13 . VAL   A 1 147 ? 23.259 -14.765 5.613   1.00 16.89 ?  147 VAL   A HG13 1 
ATOM   3093 H HG21 . VAL   A 1 147 ? 21.707 -13.011 3.661   1.00 16.02 ?  147 VAL   A HG21 1 
ATOM   3094 H HG22 . VAL   A 1 147 ? 22.972 -13.785 3.092   1.00 16.02 ?  147 VAL   A HG22 1 
ATOM   3095 H HG23 . VAL   A 1 147 ? 21.541 -14.015 2.442   1.00 16.02 ?  147 VAL   A HG23 1 
ATOM   3096 N N    . ARG   A 1 148 ? 23.081 -17.915 5.361   1.00 13.20 ?  148 ARG   A N    1 
ATOM   3097 C CA   . ARG   A 1 148 ? 22.954 -18.997 6.325   1.00 13.68 ?  148 ARG   A CA   1 
ATOM   3098 C C    . ARG   A 1 148 ? 23.082 -18.530 7.763   1.00 13.83 ?  148 ARG   A C    1 
ATOM   3099 O O    . ARG   A 1 148 ? 22.673 -19.257 8.678   1.00 15.48 ?  148 ARG   A O    1 
ATOM   3100 C CB   . ARG   A 1 148 ? 23.995 -20.093 6.044   1.00 13.94 ?  148 ARG   A CB   1 
ATOM   3101 C CG   . ARG   A 1 148 ? 23.833 -20.731 4.674   1.00 15.12 ?  148 ARG   A CG   1 
ATOM   3102 C CD   . ARG   A 1 148 ? 24.918 -21.765 4.389   1.00 16.01 ?  148 ARG   A CD   1 
ATOM   3103 N NE   . ARG   A 1 148 ? 26.257 -21.188 4.414   1.00 16.24 ?  148 ARG   A NE   1 
ATOM   3104 C CZ   . ARG   A 1 148 ? 26.768 -20.450 3.437   1.00 15.48 ?  148 ARG   A CZ   1 
ATOM   3105 N NH1  . ARG   A 1 148 ? 26.093 -20.211 2.324   1.00 15.82 ?  148 ARG   A NH1  1 
ATOM   3106 N NH2  . ARG   A 1 148 ? 27.985 -19.922 3.586   1.00 15.65 ?  148 ARG   A NH2  1 
ATOM   3107 H H    . ARG   A 1 148 ? 23.883 -17.605 5.298   1.00 15.83 ?  148 ARG   A H    1 
ATOM   3108 H HA   . ARG   A 1 148 ? 22.081 -19.395 6.228   1.00 16.41 ?  148 ARG   A HA   1 
ATOM   3109 H HB2  . ARG   A 1 148 ? 24.883 -19.716 6.092   1.00 16.72 ?  148 ARG   A HB2  1 
ATOM   3110 H HB3  . ARG   A 1 148 ? 23.897 -20.799 6.705   1.00 16.72 ?  148 ARG   A HB3  1 
ATOM   3111 H HG2  . ARG   A 1 148 ? 22.971 -21.169 4.629   1.00 18.13 ?  148 ARG   A HG2  1 
ATOM   3112 H HG3  . ARG   A 1 148 ? 23.890 -20.034 3.999   1.00 18.13 ?  148 ARG   A HG3  1 
ATOM   3113 H HD2  . ARG   A 1 148 ? 24.879 -22.460 5.062   1.00 19.20 ?  148 ARG   A HD2  1 
ATOM   3114 H HD3  . ARG   A 1 148 ? 24.769 -22.145 3.507   1.00 19.20 ?  148 ARG   A HD3  1 
ATOM   3115 H HE   . ARG   A 1 148 ? 26.745 -21.331 5.104   1.00 19.48 ?  148 ARG   A HE   1 
ATOM   3116 H HH11 . ARG   A 1 148 ? 25.306 -20.530 2.218   1.00 18.97 ?  148 ARG   A HH11 1 
ATOM   3117 H HH12 . ARG   A 1 148 ? 26.443 -19.717 1.708   1.00 18.97 ?  148 ARG   A HH12 1 
ATOM   3118 H HH21 . ARG   A 1 148 ? 28.431 -20.063 4.305   1.00 18.77 ?  148 ARG   A HH21 1 
ATOM   3119 H HH22 . ARG   A 1 148 ? 28.324 -19.434 2.960   1.00 18.77 ?  148 ARG   A HH22 1 
ATOM   3120 N N    . THR   A 1 149 ? 23.633 -17.336 7.977   1.00 13.78 ?  149 THR   A N    1 
ATOM   3121 C CA   . THR   A 1 149 ? 23.714 -16.740 9.296   1.00 14.00 ?  149 THR   A CA   1 
ATOM   3122 C C    . THR   A 1 149 ? 22.387 -16.045 9.602   1.00 13.63 ?  149 THR   A C    1 
ATOM   3123 O O    . THR   A 1 149 ? 21.452 -16.042 8.790   1.00 14.31 ?  149 THR   A O    1 
ATOM   3124 C CB   . THR   A 1 149 ? 24.913 -15.798 9.354   1.00 14.42 ?  149 THR   A CB   1 
ATOM   3125 O OG1  . THR   A 1 149 ? 24.783 -14.864 8.281   1.00 14.50 ?  149 THR   A OG1  1 
ATOM   3126 C CG2  . THR   A 1 149 ? 26.225 -16.587 9.226   1.00 14.97 ?  149 THR   A CG2  1 
ATOM   3127 H H    . THR   A 1 149 ? 23.980 -16.843 7.357   1.00 16.53 ?  149 THR   A H    1 
ATOM   3128 H HA   . THR   A 1 149 ? 23.845 -17.444 9.950   1.00 16.79 ?  149 THR   A HA   1 
ATOM   3129 H HB   . THR   A 1 149 ? 24.905 -15.331 10.204  1.00 17.30 ?  149 THR   A HB   1 
ATOM   3130 H HG1  . THR   A 1 149 ? 25.428 -14.328 8.290   1.00 17.39 ?  149 THR   A HG1  1 
ATOM   3131 H HG21 . THR   A 1 149 ? 26.980 -15.983 9.284   1.00 17.95 ?  149 THR   A HG21 1 
ATOM   3132 H HG22 . THR   A 1 149 ? 26.292 -17.245 9.939   1.00 17.95 ?  149 THR   A HG22 1 
ATOM   3133 H HG23 . THR   A 1 149 ? 26.255 -17.049 8.372   1.00 17.95 ?  149 THR   A HG23 1 
ATOM   3134 N N    . ASN   A 1 150 ? 22.261 -15.514 10.812  1.00 13.85 ?  150 ASN   A N    1 
ATOM   3135 C CA   . ASN   A 1 150 ? 20.975 -15.002 11.292  1.00 14.52 ?  150 ASN   A CA   1 
ATOM   3136 C C    . ASN   A 1 150 ? 20.798 -13.563 10.832  1.00 13.73 ?  150 ASN   A C    1 
ATOM   3137 O O    . ASN   A 1 150 ? 21.540 -12.670 11.258  1.00 15.05 ?  150 ASN   A O    1 
ATOM   3138 C CB   . ASN   A 1 150 ? 20.911 -15.111 12.810  1.00 16.97 ?  150 ASN   A CB   1 
ATOM   3139 C CG   . ASN   A 1 150 ? 20.821 -16.543 13.273  1.00 20.78 ?  150 ASN   A CG   1 
ATOM   3140 O OD1  . ASN   A 1 150 ? 20.242 -17.381 12.587  1.00 22.14 ?  150 ASN   A OD1  1 
ATOM   3141 N ND2  . ASN   A 1 150 ? 21.405 -16.839 14.431  1.00 23.35 ?  150 ASN   A ND2  1 
ATOM   3142 H H    . ASN   A 1 150 ? 22.900 -15.441 11.378  1.00 16.62 ?  150 ASN   A H    1 
ATOM   3143 H HA   . ASN   A 1 150 ? 20.252 -15.541 10.919  1.00 17.41 ?  150 ASN   A HA   1 
ATOM   3144 H HB2  . ASN   A 1 150 ? 21.710 -14.720 13.192  1.00 20.35 ?  150 ASN   A HB2  1 
ATOM   3145 H HB3  . ASN   A 1 150 ? 20.122 -14.642 13.130  1.00 20.35 ?  150 ASN   A HB3  1 
ATOM   3146 H HD21 . ASN   A 1 150 ? 21.384 -17.645 14.739  1.00 28.01 ?  150 ASN   A HD21 1 
ATOM   3147 H HD22 . ASN   A 1 150 ? 21.807 -16.224 14.882  1.00 28.01 ?  150 ASN   A HD22 1 
ATOM   3148 N N    . VAL   A 1 151 ? 19.819 -13.332 9.964   1.00 13.42 ?  151 VAL   A N    1 
ATOM   3149 C CA   . VAL   A 1 151 ? 19.608 -12.021 9.370   1.00 13.48 ?  151 VAL   A CA   1 
ATOM   3150 C C    . VAL   A 1 151 ? 18.217 -11.513 9.725   1.00 13.33 ?  151 VAL   A C    1 
ATOM   3151 O O    . VAL   A 1 151 ? 17.213 -12.226 9.571   1.00 14.60 ?  151 VAL   A O    1 
ATOM   3152 C CB   . VAL   A 1 151 ? 19.907 -12.012 7.855   1.00 14.51 ?  151 VAL   A CB   1 
ATOM   3153 C CG1  . VAL   A 1 151 ? 19.096 -13.042 7.100   1.00 15.66 ?  151 VAL   A CG1  1 
ATOM   3154 C CG2  . VAL   A 1 151 ? 19.714 -10.610 7.277   1.00 14.83 ?  151 VAL   A CG2  1 
ATOM   3155 H H    . VAL   A 1 151 ? 19.257 -13.929 9.698   1.00 16.09 ?  151 VAL   A H    1 
ATOM   3156 H HA   . VAL   A 1 151 ? 20.246 -11.408 9.772   1.00 16.17 ?  151 VAL   A HA   1 
ATOM   3157 H HB   . VAL   A 1 151 ? 20.843 -12.240 7.728   1.00 17.40 ?  151 VAL   A HB   1 
ATOM   3158 H HG11 . VAL   A 1 151 ? 19.301 -12.981 6.152   1.00 18.79 ?  151 VAL   A HG11 1 
ATOM   3159 H HG12 . VAL   A 1 151 ? 19.330 -13.931 7.425   1.00 18.79 ?  151 VAL   A HG12 1 
ATOM   3160 H HG13 . VAL   A 1 151 ? 18.153 -12.878 7.246   1.00 18.79 ?  151 VAL   A HG13 1 
ATOM   3161 H HG21 . VAL   A 1 151 ? 20.038 -10.600 6.359   1.00 17.79 ?  151 VAL   A HG21 1 
ATOM   3162 H HG22 . VAL   A 1 151 ? 18.771 -10.386 7.293   1.00 17.79 ?  151 VAL   A HG22 1 
ATOM   3163 H HG23 . VAL   A 1 151 ? 20.218 -9.976  7.809   1.00 17.79 ?  151 VAL   A HG23 1 
ATOM   3164 N N    . TYR   A 1 152 ? 18.190 -10.277 10.222  1.00 13.17 ?  152 TYR   A N    1 
ATOM   3165 C CA   . TYR   A 1 152 ? 16.990 -9.547  10.594  1.00 12.80 ?  152 TYR   A CA   1 
ATOM   3166 C C    . TYR   A 1 152 ? 16.801 -8.450  9.562   1.00 12.67 ?  152 TYR   A C    1 
ATOM   3167 O O    . TYR   A 1 152 ? 17.574 -7.483  9.523   1.00 12.90 ?  152 TYR   A O    1 
ATOM   3168 C CB   . TYR   A 1 152 ? 17.151 -8.991  12.006  1.00 13.70 ?  152 TYR   A CB   1 
ATOM   3169 C CG   . TYR   A 1 152 ? 17.112 -10.112 13.007  1.00 14.54 ?  152 TYR   A CG   1 
ATOM   3170 C CD1  . TYR   A 1 152 ? 18.246 -10.860 13.289  1.00 16.26 ?  152 TYR   A CD1  1 
ATOM   3171 C CD2  . TYR   A 1 152 ? 15.927 -10.466 13.631  1.00 14.65 ?  152 TYR   A CD2  1 
ATOM   3172 C CE1  . TYR   A 1 152 ? 18.211 -11.915 14.181  1.00 17.52 ?  152 TYR   A CE1  1 
ATOM   3173 C CE2  . TYR   A 1 152 ? 15.876 -11.529 14.529  1.00 16.28 ?  152 TYR   A CE2  1 
ATOM   3174 C CZ   . TYR   A 1 152 ? 17.026 -12.249 14.800  1.00 17.45 ?  152 TYR   A CZ   1 
ATOM   3175 O OH   . TYR   A 1 152 ? 16.993 -13.311 15.686  1.00 19.72 ?  152 TYR   A OH   1 
ATOM   3176 H H    . TYR   A 1 152 ? 18.910 -9.808  10.344  1.00 15.79 ?  152 TYR   A H    1 
ATOM   3177 H HA   . TYR   A 1 152 ? 16.227 -10.142 10.570  1.00 15.36 ?  152 TYR   A HA   1 
ATOM   3178 H HB2  . TYR   A 1 152 ? 18.008 -8.546  12.079  1.00 16.44 ?  152 TYR   A HB2  1 
ATOM   3179 H HB3  . TYR   A 1 152 ? 16.429 -8.378  12.196  1.00 16.44 ?  152 TYR   A HB3  1 
ATOM   3180 H HD1  . TYR   A 1 152 ? 19.046 -10.639 12.869  1.00 19.51 ?  152 TYR   A HD1  1 
ATOM   3181 H HD2  . TYR   A 1 152 ? 15.146 -9.985  13.444  1.00 17.57 ?  152 TYR   A HD2  1 
ATOM   3182 H HE1  . TYR   A 1 152 ? 18.982 -12.392 14.361  1.00 21.01 ?  152 TYR   A HE1  1 
ATOM   3183 H HE2  . TYR   A 1 152 ? 15.073 -11.746 14.946  1.00 19.53 ?  152 TYR   A HE2  1 
ATOM   3184 H HH   . TYR   A 1 152 ? 16.218 -13.390 15.995  1.00 23.66 ?  152 TYR   A HH   1 
ATOM   3185 N N    A LEU   A 1 153 ? 15.807 -8.645  8.691   0.60 12.65 ?  153 LEU   A N    1 
ATOM   3186 N N    B LEU   A 1 153 ? 15.757 -8.566  8.754   0.40 12.56 ?  153 LEU   A N    1 
ATOM   3187 C CA   A LEU   A 1 153 ? 15.544 -7.779  7.548   0.60 12.50 ?  153 LEU   A CA   1 
ATOM   3188 C CA   B LEU   A 1 153 ? 15.513 -7.608  7.687   0.40 12.23 ?  153 LEU   A CA   1 
ATOM   3189 C C    A LEU   A 1 153 ? 14.533 -6.703  7.913   0.60 12.35 ?  153 LEU   A C    1 
ATOM   3190 C C    B LEU   A 1 153 ? 14.550 -6.529  8.164   0.40 12.28 ?  153 LEU   A C    1 
ATOM   3191 O O    A LEU   A 1 153 ? 13.439 -7.008  8.400   0.60 13.30 ?  153 LEU   A O    1 
ATOM   3192 O O    B LEU   A 1 153 ? 13.433 -6.831  8.603   0.40 13.16 ?  153 LEU   A O    1 
ATOM   3193 C CB   A LEU   A 1 153 ? 14.989 -8.602  6.382   0.60 12.06 ?  153 LEU   A CB   1 
ATOM   3194 C CB   B LEU   A 1 153 ? 14.956 -8.317  6.458   0.40 12.23 ?  153 LEU   A CB   1 
ATOM   3195 C CG   A LEU   A 1 153 ? 15.957 -9.557  5.680   0.60 12.38 ?  153 LEU   A CG   1 
ATOM   3196 C CG   B LEU   A 1 153 ? 15.869 -9.404  5.893   0.40 12.63 ?  153 LEU   A CG   1 
ATOM   3197 C CD1  A LEU   A 1 153 ? 15.196 -10.499 4.753   0.60 12.70 ?  153 LEU   A CD1  1 
ATOM   3198 C CD1  B LEU   A 1 153 ? 15.118 -10.191 4.826   0.40 12.78 ?  153 LEU   A CD1  1 
ATOM   3199 C CD2  A LEU   A 1 153 ? 16.977 -8.758  4.896   0.60 11.80 ?  153 LEU   A CD2  1 
ATOM   3200 C CD2  B LEU   A 1 153 ? 17.175 -8.819  5.344   0.40 12.97 ?  153 LEU   A CD2  1 
ATOM   3201 H H    A LEU   A 1 153 ? 15.253 -9.309  8.747   0.60 15.17 ?  153 LEU   A H    1 
ATOM   3202 H H    B LEU   A 1 153 ? 15.166 -9.194  8.806   0.40 15.07 ?  153 LEU   A H    1 
ATOM   3203 H HA   A LEU   A 1 153 ? 16.365 -7.361  7.266   0.60 14.99 ?  153 LEU   A HA   1 
ATOM   3204 H HA   B LEU   A 1 153 ? 16.345 -7.182  7.449   0.40 14.67 ?  153 LEU   A HA   1 
ATOM   3205 H HB2  A LEU   A 1 153 ? 14.248 -9.139  6.708   0.60 14.47 ?  153 LEU   A HB2  1 
ATOM   3206 H HB2  B LEU   A 1 153 ? 14.112 -8.730  6.697   0.40 14.67 ?  153 LEU   A HB2  1 
ATOM   3207 H HB3  A LEU   A 1 153 ? 14.661 -7.989  5.704   0.60 14.47 ?  153 LEU   A HB3  1 
ATOM   3208 H HB3  B LEU   A 1 153 ? 14.812 -7.654  5.765   0.40 14.67 ?  153 LEU   A HB3  1 
ATOM   3209 H HG   A LEU   A 1 153 ? 16.426 -10.092 6.344   0.60 14.86 ?  153 LEU   A HG   1 
ATOM   3210 H HG   B LEU   A 1 153 ? 16.101 -10.015 6.609   0.40 15.15 ?  153 LEU   A HG   1 
ATOM   3211 H HD11 A LEU   A 1 153 ? 15.784 -11.226 4.489   0.60 15.23 ?  153 LEU   A HD11 1 
ATOM   3212 H HD11 B LEU   A 1 153 ? 15.698 -10.889 4.485   0.40 15.33 ?  153 LEU   A HD11 1 
ATOM   3213 H HD12 A LEU   A 1 153 ? 14.427 -10.850 5.221   0.60 15.23 ?  153 LEU   A HD12 1 
ATOM   3214 H HD12 B LEU   A 1 153 ? 14.326 -10.582 5.225   0.40 15.33 ?  153 LEU   A HD12 1 
ATOM   3215 H HD13 A LEU   A 1 153 ? 14.913 -10.002 3.969   0.60 15.23 ?  153 LEU   A HD13 1 
ATOM   3216 H HD13 B LEU   A 1 153 ? 14.866 -9.589  4.109   0.40 15.33 ?  153 LEU   A HD13 1 
ATOM   3217 H HD21 A LEU   A 1 153 ? 17.562 -9.367  4.431   0.60 14.15 ?  153 LEU   A HD21 1 
ATOM   3218 H HD21 B LEU   A 1 153 ? 17.691 -9.529  4.934   0.40 15.56 ?  153 LEU   A HD21 1 
ATOM   3219 H HD22 A LEU   A 1 153 ? 16.504 -8.195  4.264   0.60 14.15 ?  153 LEU   A HD22 1 
ATOM   3220 H HD22 B LEU   A 1 153 ? 16.966 -8.138  4.686   0.40 15.56 ?  153 LEU   A HD22 1 
ATOM   3221 H HD23 A LEU   A 1 153 ? 17.483 -8.211  5.514   0.60 14.15 ?  153 LEU   A HD23 1 
ATOM   3222 H HD23 B LEU   A 1 153 ? 17.681 -8.425  6.075   0.40 15.56 ?  153 LEU   A HD23 1 
ATOM   3223 N N    A ALA   A 1 154 ? 14.887 -5.452  7.639   0.60 11.67 ?  154 ALA   A N    1 
ATOM   3224 N N    B ALA   A 1 154 ? 14.984 -5.276  8.071   0.40 11.33 ?  154 ALA   A N    1 
ATOM   3225 C CA   A ALA   A 1 154 ? 14.008 -4.307  7.841   0.60 11.63 ?  154 ALA   A CA   1 
ATOM   3226 C CA   B ALA   A 1 154 ? 14.139 -4.122  8.340   0.40 11.15 ?  154 ALA   A CA   1 
ATOM   3227 C C    A ALA   A 1 154 ? 13.534 -3.815  6.479   0.60 11.27 ?  154 ALA   A C    1 
ATOM   3228 C C    B ALA   A 1 154 ? 13.641 -3.588  7.004   0.40 10.85 ?  154 ALA   A C    1 
ATOM   3229 O O    A ALA   A 1 154 ? 14.350 -3.438  5.630   0.60 11.87 ?  154 ALA   A O    1 
ATOM   3230 O O    B ALA   A 1 154 ? 14.442 -3.170  6.160   0.40 11.02 ?  154 ALA   A O    1 
ATOM   3231 C CB   A ALA   A 1 154 ? 14.742 -3.192  8.583   0.60 12.08 ?  154 ALA   A CB   1 
ATOM   3232 C CB   B ALA   A 1 154 ? 14.921 -3.040  9.086   0.40 11.68 ?  154 ALA   A CB   1 
ATOM   3233 H H    A ALA   A 1 154 ? 15.654 -5.245  7.318   0.60 13.99 ?  154 ALA   A H    1 
ATOM   3234 H H    B ALA   A 1 154 ? 15.787 -5.060  7.839   0.40 13.59 ?  154 ALA   A H    1 
ATOM   3235 H HA   A ALA   A 1 154 ? 13.234 -4.577  8.364   0.60 13.95 ?  154 ALA   A HA   1 
ATOM   3236 H HA   B ALA   A 1 154 ? 13.376 -4.383  8.876   0.40 13.38 ?  154 ALA   A HA   1 
ATOM   3237 H HB1  A ALA   A 1 154 ? 14.136 -2.447  8.705   0.60 14.49 ?  154 ALA   A HB1  1 
ATOM   3238 H HB1  B ALA   A 1 154 ? 14.336 -2.283  9.253   0.40 14.01 ?  154 ALA   A HB1  1 
ATOM   3239 H HB2  A ALA   A 1 154 ? 15.035 -3.528  9.445   0.60 14.49 ?  154 ALA   A HB2  1 
ATOM   3240 H HB2  B ALA   A 1 154 ? 15.237 -3.404  9.928   0.40 14.01 ?  154 ALA   A HB2  1 
ATOM   3241 H HB3  A ALA   A 1 154 ? 15.508 -2.918  8.057   0.60 14.49 ?  154 ALA   A HB3  1 
ATOM   3242 H HB3  B ALA   A 1 154 ? 15.675 -2.761  8.543   0.40 14.01 ?  154 ALA   A HB3  1 
ATOM   3243 N N    A VAL   A 1 155 ? 12.220 -3.837  6.274   0.40 10.38 ?  155 VAL   A N    1 
ATOM   3244 N N    B VAL   A 1 155 ? 12.326 -3.617  6.811   0.40 11.06 ?  155 VAL   A N    1 
ATOM   3245 C CA   A VAL   A 1 155 ? 11.578 -3.385  5.043   0.40 12.03 ?  155 VAL   A CA   1 
ATOM   3246 C CA   B VAL   A 1 155 ? 11.687 -3.138  5.592   0.40 12.68 ?  155 VAL   A CA   1 
ATOM   3247 C CA   T VAL   A 1 155 ? 11.571 -3.371  5.210   0.20 12.89 ?  155 VAL   A CA   1 
ATOM   3248 C C    A VAL   A 1 155 ? 10.828 -2.100  5.382   0.40 13.16 ?  155 VAL   A C    1 
ATOM   3249 C C    B VAL   A 1 155 ? 11.011 -1.810  5.908   0.40 14.32 ?  155 VAL   A C    1 
ATOM   3250 C C    T VAL   A 1 155 ? 10.944 -2.013  5.527   0.20 12.77 ?  155 VAL   A C    1 
ATOM   3251 O O    A VAL   A 1 155 ? 9.831  -2.132  6.111   0.40 12.83 ?  155 VAL   A O    1 
ATOM   3252 O O    B VAL   A 1 155 ? 10.084 -1.754  6.726   0.40 14.39 ?  155 VAL   A O    1 
ATOM   3253 O O    T VAL   A 1 155 ? 10.083 -1.903  6.398   0.20 12.40 ?  155 VAL   A O    1 
ATOM   3254 C CB   A VAL   A 1 155 ? 10.643 -4.467  4.478   0.40 12.08 ?  155 VAL   A CB   1 
ATOM   3255 C CB   B VAL   A 1 155 ? 10.690 -4.168  5.043   0.40 12.84 ?  155 VAL   A CB   1 
ATOM   3256 C CB   T VAL   A 1 155 ? 10.546 -4.379  4.650   0.20 12.92 ?  155 VAL   A CB   1 
ATOM   3257 C CG1  A VAL   A 1 155 ? 9.969  -4.004  3.193   0.40 12.32 ?  155 VAL   A CG1  1 
ATOM   3258 C CG1  B VAL   A 1 155 ? 9.922  -3.590  3.867   0.40 13.11 ?  155 VAL   A CG1  1 
ATOM   3259 C CG1  T VAL   A 1 155 ? 9.865  -3.817  3.413   0.20 13.04 ?  155 VAL   A CG1  1 
ATOM   3260 C CG2  A VAL   A 1 155 ? 11.422 -5.766  4.235   0.40 13.07 ?  155 VAL   A CG2  1 
ATOM   3261 C CG2  B VAL   A 1 155 ? 11.428 -5.437  4.636   0.40 13.64 ?  155 VAL   A CG2  1 
ATOM   3262 C CG2  T VAL   A 1 155 ? 11.224 -5.708  4.331   0.20 13.28 ?  155 VAL   A CG2  1 
ATOM   3263 H H    A VAL   A 1 155 ? 11.659 -4.142  6.853   0.40 12.44 ?  155 VAL   A H    1 
ATOM   3264 H H    B VAL   A 1 155 ? 11.768 -3.916  7.390   0.40 13.27 ?  155 VAL   A H    1 
ATOM   3265 H HA   A VAL   A 1 155 ? 12.250 -3.191  4.374   0.40 14.43 ?  155 VAL   A HA   1 
ATOM   3266 H HA   B VAL   A 1 155 ? 12.364 -2.981  4.913   0.40 15.20 ?  155 VAL   A HA   1 
ATOM   3267 H HB   A VAL   A 1 155 ? 9.946  -4.662  5.127   0.40 14.49 ?  155 VAL   A HB   1 
ATOM   3268 H HB   B VAL   A 1 155 ? 10.055 -4.397  5.741   0.40 15.40 ?  155 VAL   A HB   1 
ATOM   3269 H HB   T VAL   A 1 155 ? 9.866  -4.545  5.322   0.20 15.50 ?  155 VAL   A HB   1 
ATOM   3270 H HG11 A VAL   A 1 155 ? 9.276  -4.640  2.953   0.40 14.78 ?  155 VAL   A HG11 1 
ATOM   3271 H HG11 B VAL   A 1 155 ? 9.396  -4.294  3.460   0.40 15.73 ?  155 VAL   A HG11 1 
ATOM   3272 H HG11 T VAL   A 1 155 ? 9.354  -4.523  2.988   0.20 15.64 ?  155 VAL   A HG11 1 
ATOM   3273 H HG12 A VAL   A 1 155 ? 9.572  -3.134  3.335   0.40 14.78 ?  155 VAL   A HG12 1 
ATOM   3274 H HG12 B VAL   A 1 155 ? 9.339  -2.885  4.186   0.40 15.73 ?  155 VAL   A HG12 1 
ATOM   3275 H HG12 T VAL   A 1 155 ? 9.276  -3.095  3.676   0.20 15.64 ?  155 VAL   A HG12 1 
ATOM   3276 H HG13 A VAL   A 1 155 ? 10.633 -3.957  2.488   0.40 14.78 ?  155 VAL   A HG13 1 
ATOM   3277 H HG13 B VAL   A 1 155 ? 10.553 -3.232  3.225   0.40 15.73 ?  155 VAL   A HG13 1 
ATOM   3278 H HG13 T VAL   A 1 155 ? 10.544 -3.489  2.803   0.20 15.64 ?  155 VAL   A HG13 1 
ATOM   3279 H HG21 A VAL   A 1 155 ? 10.842 -6.413  3.804   0.40 15.68 ?  155 VAL   A HG21 1 
ATOM   3280 H HG21 B VAL   A 1 155 ? 10.801 -6.048  4.219   0.40 16.36 ?  155 VAL   A HG21 1 
ATOM   3281 H HG21 T VAL   A 1 155 ? 10.563 -6.327  3.984   0.20 15.93 ?  155 VAL   A HG21 1 
ATOM   3282 H HG22 A VAL   A 1 155 ? 12.185 -5.576  3.666   0.40 15.68 ?  155 VAL   A HG22 1 
ATOM   3283 H HG22 B VAL   A 1 155 ? 12.132 -5.206  4.008   0.40 16.36 ?  155 VAL   A HG22 1 
ATOM   3284 H HG22 T VAL   A 1 155 ? 11.917 -5.558  3.667   0.20 15.93 ?  155 VAL   A HG22 1 
ATOM   3285 H HG23 A VAL   A 1 155 ? 11.729 -6.118  5.088   0.40 15.68 ?  155 VAL   A HG23 1 
ATOM   3286 H HG23 B VAL   A 1 155 ? 11.816 -5.848  5.426   0.40 16.36 ?  155 VAL   A HG23 1 
ATOM   3287 H HG23 T VAL   A 1 155 ? 11.619 -6.066  5.143   0.20 15.93 ?  155 VAL   A HG23 1 
ATOM   3288 N N    A PHE   A 1 156 ? 11.300 -0.964  4.858   0.40 14.84 ?  156 PHE   A N    1 
ATOM   3289 N N    B PHE   A 1 156 ? 11.475 -0.746  5.247   0.40 16.21 ?  156 PHE   A N    1 
ATOM   3290 N N    T PHE   A 1 156 ? 11.387 -0.984  4.801   0.20 13.21 ?  156 PHE   A N    1 
ATOM   3291 C CA   A PHE   A 1 156 ? 10.765 0.333   5.284   0.40 16.39 ?  156 PHE   A CA   1 
ATOM   3292 C CA   B PHE   A 1 156 ? 11.012 0.605   5.554   0.40 18.83 ?  156 PHE   A CA   1 
ATOM   3293 C CA   T PHE   A 1 156 ? 10.960 0.384   5.091   0.20 13.41 ?  156 PHE   A CA   1 
ATOM   3294 C C    A PHE   A 1 156 ? 9.319  0.525   4.849   0.40 16.44 ?  156 PHE   A C    1 
ATOM   3295 C C    B PHE   A 1 156 ? 9.526  0.772   5.246   0.40 20.14 ?  156 PHE   A C    1 
ATOM   3296 C C    T PHE   A 1 156 ? 9.513  0.620   4.683   0.20 13.90 ?  156 PHE   A C    1 
ATOM   3297 O O    A PHE   A 1 156 ? 8.492  1.034   5.619   0.40 17.26 ?  156 PHE   A O    1 
ATOM   3298 O O    B PHE   A 1 156 ? 8.785  1.376   6.032   0.40 20.46 ?  156 PHE   A O    1 
ATOM   3299 O O    T PHE   A 1 156 ? 8.749  1.261   5.416   0.20 14.37 ?  156 PHE   A O    1 
ATOM   3300 C CB   A PHE   A 1 156 ? 11.634 1.465   4.734   0.40 17.73 ?  156 PHE   A CB   1 
ATOM   3301 C CB   B PHE   A 1 156 ? 11.856 1.602   4.755   0.40 19.92 ?  156 PHE   A CB   1 
ATOM   3302 C CB   T PHE   A 1 156 ? 11.877 1.362   4.358   0.20 12.83 ?  156 PHE   A CB   1 
ATOM   3303 C CG   A PHE   A 1 156 ? 11.109 2.849   5.046   0.40 18.95 ?  156 PHE   A CG   1 
ATOM   3304 C CG   B PHE   A 1 156 ? 11.605 3.044   5.101   0.40 20.53 ?  156 PHE   A CG   1 
ATOM   3305 C CG   T PHE   A 1 156 ? 11.509 2.812   4.547   0.20 12.43 ?  156 PHE   A CG   1 
ATOM   3306 C CD1  A PHE   A 1 156 ? 11.051 3.301   6.355   0.40 19.40 ?  156 PHE   A CD1  1 
ATOM   3307 C CD1  B PHE   A 1 156 ? 11.734 3.493   6.406   0.40 21.13 ?  156 PHE   A CD1  1 
ATOM   3308 C CD1  T PHE   A 1 156 ? 11.851 3.480   5.713   0.20 12.75 ?  156 PHE   A CD1  1 
ATOM   3309 C CD2  A PHE   A 1 156 ? 10.689 3.697   4.031   0.40 20.00 ?  156 PHE   A CD2  1 
ATOM   3310 C CD2  B PHE   A 1 156 ? 11.270 3.956   4.113   0.40 20.60 ?  156 PHE   A CD2  1 
ATOM   3311 C CD2  T PHE   A 1 156 ? 10.839 3.509   3.554   0.20 12.82 ?  156 PHE   A CD2  1 
ATOM   3312 C CE1  A PHE   A 1 156 ? 10.578 4.572   6.648   0.40 20.14 ?  156 PHE   A CE1  1 
ATOM   3313 C CE1  B PHE   A 1 156 ? 11.510 4.817   6.722   0.40 21.33 ?  156 PHE   A CE1  1 
ATOM   3314 C CE1  T PHE   A 1 156 ? 11.522 4.810   5.891   0.20 13.10 ?  156 PHE   A CE1  1 
ATOM   3315 C CE2  A PHE   A 1 156 ? 10.213 4.968   4.317   0.40 20.59 ?  156 PHE   A CE2  1 
ATOM   3316 C CE2  B PHE   A 1 156 ? 11.048 5.285   4.423   0.40 20.72 ?  156 PHE   A CE2  1 
ATOM   3317 C CE2  T PHE   A 1 156 ? 10.509 4.842   3.725   0.20 13.21 ?  156 PHE   A CE2  1 
ATOM   3318 C CZ   A PHE   A 1 156 ? 10.160 5.406   5.628   0.40 20.69 ?  156 PHE   A CZ   1 
ATOM   3319 C CZ   B PHE   A 1 156 ? 11.167 5.715   5.729   0.40 20.95 ?  156 PHE   A CZ   1 
ATOM   3320 C CZ   T PHE   A 1 156 ? 10.851 5.493   4.897   0.20 13.33 ?  156 PHE   A CZ   1 
ATOM   3321 H H    A PHE   A 1 156 ? 11.921 -0.928  4.266   0.40 17.80 ?  156 PHE   A H    1 
ATOM   3322 H H    B PHE   A 1 156 ? 12.061 -0.785  4.619   0.40 19.45 ?  156 PHE   A H    1 
ATOM   3323 H H    T PHE   A 1 156 ? 11.935 -1.060  4.144   0.20 15.85 ?  156 PHE   A H    1 
ATOM   3324 H HA   A PHE   A 1 156 ? 10.791 0.373   6.249   0.40 19.67 ?  156 PHE   A HA   1 
ATOM   3325 H HA   B PHE   A 1 156 ? 11.152 0.781   6.497   0.40 22.59 ?  156 PHE   A HA   1 
ATOM   3326 H HA   T PHE   A 1 156 ? 11.038 0.541   6.044   0.20 16.08 ?  156 PHE   A HA   1 
ATOM   3327 H HB2  A PHE   A 1 156 ? 12.522 1.388   5.121   0.40 21.27 ?  156 PHE   A HB2  1 
ATOM   3328 H HB2  B PHE   A 1 156 ? 12.793 1.418   4.924   0.40 23.90 ?  156 PHE   A HB2  1 
ATOM   3329 H HB2  T PHE   A 1 156 ? 12.782 1.238   4.683   0.20 15.39 ?  156 PHE   A HB2  1 
ATOM   3330 H HB3  A PHE   A 1 156 ? 11.689 1.376   3.770   0.40 21.27 ?  156 PHE   A HB3  1 
ATOM   3331 H HB3  B PHE   A 1 156 ? 11.669 1.489   3.811   0.40 23.90 ?  156 PHE   A HB3  1 
ATOM   3332 H HB3  T PHE   A 1 156 ? 11.840 1.167   3.409   0.20 15.39 ?  156 PHE   A HB3  1 
ATOM   3333 H HD1  A PHE   A 1 156 ? 11.332 2.743   7.047   0.40 23.27 ?  156 PHE   A HD1  1 
ATOM   3334 H HD1  B PHE   A 1 156 ? 11.963 2.890   7.078   0.40 25.35 ?  156 PHE   A HD1  1 
ATOM   3335 H HD1  T PHE   A 1 156 ? 12.300 3.020   6.390   0.20 15.29 ?  156 PHE   A HD1  1 
ATOM   3336 H HD2  A PHE   A 1 156 ? 10.724 3.407   3.149   0.40 24.00 ?  156 PHE   A HD2  1 
ATOM   3337 H HD2  B PHE   A 1 156 ? 11.188 3.667   3.233   0.40 24.71 ?  156 PHE   A HD2  1 
ATOM   3338 H HD2  T PHE   A 1 156 ? 10.605 3.073   2.768   0.20 15.37 ?  156 PHE   A HD2  1 
ATOM   3339 H HE1  A PHE   A 1 156 ? 10.544 4.863   7.532   0.40 24.16 ?  156 PHE   A HE1  1 
ATOM   3340 H HE1  B PHE   A 1 156 ? 11.592 5.104   7.603   0.40 25.58 ?  156 PHE   A HE1  1 
ATOM   3341 H HE1  T PHE   A 1 156 ? 11.753 5.241   6.683   0.20 15.71 ?  156 PHE   A HE1  1 
ATOM   3342 H HE2  A PHE   A 1 156 ? 9.935  5.527   3.629   0.40 24.70 ?  156 PHE   A HE2  1 
ATOM   3343 H HE2  B PHE   A 1 156 ? 10.816 5.885   3.754   0.40 24.85 ?  156 PHE   A HE2  1 
ATOM   3344 H HE2  T PHE   A 1 156 ? 10.054 5.298   3.058   0.20 15.84 ?  156 PHE   A HE2  1 
ATOM   3345 H HZ   A PHE   A 1 156 ? 9.844  6.259   5.824   0.40 24.82 ?  156 PHE   A HZ   1 
ATOM   3346 H HZ   B PHE   A 1 156 ? 11.017 6.606   5.942   0.40 25.13 ?  156 PHE   A HZ   1 
ATOM   3347 H HZ   T PHE   A 1 156 ? 10.628 6.386   5.018   0.20 15.99 ?  156 PHE   A HZ   1 
ATOM   3348 N N    A ASP   A 1 157 ? 9.000  0.155   3.618   0.40 16.42 ?  157 ASP   A N    1 
ATOM   3349 N N    B ASP   A 1 157 ? 9.075  0.242   4.116   0.40 20.91 ?  157 ASP   A N    1 
ATOM   3350 N N    T ASP   A 1 157 ? 9.124  0.125   3.516   0.20 14.01 ?  157 ASP   A N    1 
ATOM   3351 C CA   A ASP   A 1 157 ? 7.677  0.420   3.070   0.40 17.15 ?  157 ASP   A CA   1 
ATOM   3352 C CA   B ASP   A 1 157 ? 7.718  0.440   3.623   0.40 22.73 ?  157 ASP   A CA   1 
ATOM   3353 C CA   T ASP   A 1 157 ? 7.809  0.408   2.964   0.20 14.40 ?  157 ASP   A CA   1 
ATOM   3354 C C    A ASP   A 1 157 ? 6.697  -0.584  3.668   0.40 17.03 ?  157 ASP   A C    1 
ATOM   3355 C C    B ASP   A 1 157 ? 6.823  -0.748  3.982   0.40 23.63 ?  157 ASP   A C    1 
ATOM   3356 C C    T ASP   A 1 157 ? 6.791  -0.554  3.567   0.20 15.06 ?  157 ASP   A C    1 
ATOM   3357 O O    A ASP   A 1 157 ? 6.825  -1.793  3.437   0.40 16.39 ?  157 ASP   A O    1 
ATOM   3358 O O    B ASP   A 1 157 ? 7.299  -1.829  4.333   0.40 24.96 ?  157 ASP   A O    1 
ATOM   3359 O O    T ASP   A 1 157 ? 6.907  -1.773  3.393   0.20 14.44 ?  157 ASP   A O    1 
ATOM   3360 C CB   A ASP   A 1 157 ? 7.739  0.320   1.550   0.40 18.36 ?  157 ASP   A CB   1 
ATOM   3361 C CB   B ASP   A 1 157 ? 7.758  0.636   2.107   0.40 23.58 ?  157 ASP   A CB   1 
ATOM   3362 C CB   T ASP   A 1 157 ? 7.879  0.242   1.450   0.20 14.15 ?  157 ASP   A CB   1 
ATOM   3363 C CG   A ASP   A 1 157 ? 6.459  0.789   0.882   0.40 19.67 ?  157 ASP   A CG   1 
ATOM   3364 C CG   B ASP   A 1 157 ? 6.475  1.203   1.559   0.40 24.57 ?  157 ASP   A CG   1 
ATOM   3365 C CG   T ASP   A 1 157 ? 6.762  0.939   0.736   0.20 13.61 ?  157 ASP   A CG   1 
ATOM   3366 O OD1  A ASP   A 1 157 ? 6.110  1.979   1.014   0.40 21.00 ?  157 ASP   A OD1  1 
ATOM   3367 O OD1  B ASP   A 1 157 ? 5.500  0.433   1.448   0.40 24.28 ?  157 ASP   A OD1  1 
ATOM   3368 O OD1  T ASP   A 1 157 ? 5.650  0.381   0.722   0.20 13.00 ?  157 ASP   A OD1  1 
ATOM   3369 O OD2  A ASP   A 1 157 ? 5.793  -0.038  0.227   0.40 19.37 -1 157 ASP   A OD2  1 
ATOM   3370 O OD2  B ASP   A 1 157 ? 6.439  2.412   1.249   0.40 25.80 -1 157 ASP   A OD2  1 
ATOM   3371 O OD2  T ASP   A 1 157 ? 6.991  2.040   0.197   0.20 12.75 -1 157 ASP   A OD2  1 
ATOM   3372 H H    A ASP   A 1 157 ? 9.529  -0.258  3.076   0.40 19.69 ?  157 ASP   A H    1 
ATOM   3373 H H    B ASP   A 1 157 ? 9.563  -0.237  3.597   0.40 25.09 ?  157 ASP   A H    1 
ATOM   3374 H H    T ASP   A 1 157 ? 9.610  -0.381  3.013   0.20 16.80 ?  157 ASP   A H    1 
ATOM   3375 H HA   A ASP   A 1 157 ? 7.396  1.314   3.309   0.40 20.58 ?  157 ASP   A HA   1 
ATOM   3376 H HA   B ASP   A 1 157 ? 7.349  1.241   4.027   0.40 27.27 ?  157 ASP   A HA   1 
ATOM   3377 H HA   T ASP   A 1 157 ? 7.549  1.318   3.171   0.20 17.27 ?  157 ASP   A HA   1 
ATOM   3378 H HB2  A ASP   A 1 157 ? 8.513  0.824   1.242   0.40 22.03 ?  157 ASP   A HB2  1 
ATOM   3379 H HB2  B ASP   A 1 157 ? 8.493  1.231   1.888   0.40 28.28 ?  157 ASP   A HB2  1 
ATOM   3380 H HB2  T ASP   A 1 157 ? 8.708  0.607   1.129   0.20 16.97 ?  157 ASP   A HB2  1 
ATOM   3381 H HB3  A ASP   A 1 157 ? 7.859  -0.600  1.297   0.40 22.03 ?  157 ASP   A HB3  1 
ATOM   3382 H HB3  B ASP   A 1 157 ? 7.885  -0.224  1.685   0.40 28.28 ?  157 ASP   A HB3  1 
ATOM   3383 H HB3  T ASP   A 1 157 ? 7.831  -0.701  1.240   0.20 16.97 ?  157 ASP   A HB3  1 
ATOM   3384 N N    A LYS   A 1 158 ? 5.743  -0.092  4.473   0.40 18.29 ?  158 LYS   A N    1 
ATOM   3385 N N    B LYS   A 1 158 ? 5.507  -0.537  3.881   0.40 22.93 ?  158 LYS   A N    1 
ATOM   3386 N N    T LYS   A 1 158 ? 5.800  -0.010  4.286   0.20 16.67 ?  158 LYS   A N    1 
ATOM   3387 C CA   A LYS   A 1 158 ? 4.743  -0.982  5.063   0.40 19.20 ?  158 LYS   A CA   1 
ATOM   3388 C CA   B LYS   A 1 158 ? 4.520  -1.511  4.352   0.40 22.27 ?  158 LYS   A CA   1 
ATOM   3389 C CA   T LYS   A 1 158 ? 4.801  -0.867  4.922   0.20 18.16 ?  158 LYS   A CA   1 
ATOM   3390 C C    A LYS   A 1 158 ? 3.986  -1.726  3.978   0.40 18.01 ?  158 LYS   A C    1 
ATOM   3391 C C    B LYS   A 1 158 ? 3.855  -2.296  3.224   0.40 20.02 ?  158 LYS   A C    1 
ATOM   3392 C C    T LYS   A 1 158 ? 4.029  -1.674  3.888   0.20 18.05 ?  158 LYS   A C    1 
ATOM   3393 O O    A LYS   A 1 158 ? 3.788  -2.943  4.063   0.40 17.63 ?  158 LYS   A O    1 
ATOM   3394 O O    B LYS   A 1 158 ? 3.706  -3.518  3.327   0.40 18.91 ?  158 LYS   A O    1 
ATOM   3395 O O    T LYS   A 1 158 ? 3.797  -2.874  4.074   0.20 17.89 ?  158 LYS   A O    1 
ATOM   3396 C CB   A LYS   A 1 158 ? 3.769  -0.203  5.952   0.40 21.24 ?  158 LYS   A CB   1 
ATOM   3397 C CB   B LYS   A 1 158 ? 3.456  -0.814  5.214   0.40 23.88 ?  158 LYS   A CB   1 
ATOM   3398 C CB   T LYS   A 1 158 ? 3.843  -0.042  5.786   0.20 19.77 ?  158 LYS   A CB   1 
ATOM   3399 C CG   A LYS   A 1 158 ? 2.508  -0.996  6.369   0.40 23.44 ?  158 LYS   A CG   1 
ATOM   3400 C CG   B LYS   A 1 158 ? 2.281  -1.704  5.632   0.40 25.45 ?  158 LYS   A CG   1 
ATOM   3401 C CG   T LYS   A 1 158 ? 2.608  -0.814  6.266   0.20 21.36 ?  158 LYS   A CG   1 
ATOM   3402 C CD   A LYS   A 1 158 ? 2.830  -2.317  7.087   0.40 25.35 ?  158 LYS   A CD   1 
ATOM   3403 C CD   B LYS   A 1 158 ? 2.667  -2.722  6.702   0.40 26.82 ?  158 LYS   A CD   1 
ATOM   3404 C CD   T LYS   A 1 158 ? 2.978  -2.023  7.120   0.20 22.84 ?  158 LYS   A CD   1 
ATOM   3405 C CE   A LYS   A 1 158 ? 1.573  -2.993  7.636   0.40 26.43 ?  158 LYS   A CE   1 
ATOM   3406 C CE   B LYS   A 1 158 ? 1.432  -3.443  7.236   0.40 27.61 ?  158 LYS   A CE   1 
ATOM   3407 C CE   T LYS   A 1 158 ? 1.740  -2.820  7.516   0.20 23.87 ?  158 LYS   A CE   1 
ATOM   3408 N NZ   A LYS   A 1 158 ? 1.850  -4.343  8.219   0.40 27.10 ?  158 LYS   A NZ   1 
ATOM   3409 N NZ   B LYS   A 1 158 ? 1.735  -4.332  8.393   0.40 28.27 ?  158 LYS   A NZ   1 
ATOM   3410 N NZ   T LYS   A 1 158 ? 2.078  -4.050  8.286   0.20 24.47 ?  158 LYS   A NZ   1 
ATOM   3411 H H    A LYS   A 1 158 ? 5.666  0.734   4.694   0.40 21.94 ?  158 LYS   A H    1 
ATOM   3412 H H    B LYS   A 1 158 ? 5.160  0.168   3.534   0.40 27.51 ?  158 LYS   A H    1 
ATOM   3413 H H    T LYS   A 1 158 ? 5.689  0.834   4.421   0.20 19.99 ?  158 LYS   A H    1 
ATOM   3414 H HA   A LYS   A 1 158 ? 5.189  -1.639  5.615   0.40 23.03 ?  158 LYS   A HA   1 
ATOM   3415 H HA   B LYS   A 1 158 ? 4.970  -2.150  4.922   0.40 26.72 ?  158 LYS   A HA   1 
ATOM   3416 H HA   T LYS   A 1 158 ? 5.253  -1.492  5.509   0.20 21.78 ?  158 LYS   A HA   1 
ATOM   3417 H HB2  A LYS   A 1 158 ? 4.228  0.068   6.763   0.40 25.48 ?  158 LYS   A HB2  1 
ATOM   3418 H HB2  B LYS   A 1 158 ? 3.877  -0.491  6.030   0.40 28.65 ?  158 LYS   A HB2  1 
ATOM   3419 H HB2  T LYS   A 1 158 ? 4.317  0.266   6.578   0.20 23.71 ?  158 LYS   A HB2  1 
ATOM   3420 H HB3  A LYS   A 1 158 ? 3.470  0.585   5.471   0.40 25.48 ?  158 LYS   A HB3  1 
ATOM   3421 H HB3  B LYS   A 1 158 ? 3.093  -0.064  4.720   0.40 28.65 ?  158 LYS   A HB3  1 
ATOM   3422 H HB3  T LYS   A 1 158 ? 3.531  0.720   5.276   0.20 23.71 ?  158 LYS   A HB3  1 
ATOM   3423 H HG2  A LYS   A 1 158 ? 1.985  -0.453  6.977   0.40 28.12 ?  158 LYS   A HG2  1 
ATOM   3424 H HG2  B LYS   A 1 158 ? 1.587  -1.141  6.001   0.40 30.54 ?  158 LYS   A HG2  1 
ATOM   3425 H HG2  T LYS   A 1 158 ? 2.062  -0.227  6.809   0.20 25.62 ?  158 LYS   A HG2  1 
ATOM   3426 H HG3  A LYS   A 1 158 ? 1.979  -1.203  5.581   0.40 28.12 ?  158 LYS   A HG3  1 
ATOM   3427 H HG3  B LYS   A 1 158 ? 1.933  -2.186  4.865   0.40 30.54 ?  158 LYS   A HG3  1 
ATOM   3428 H HG3  T LYS   A 1 158 ? 2.093  -1.124  5.503   0.20 25.62 ?  158 LYS   A HG3  1 
ATOM   3429 H HD2  A LYS   A 1 158 ? 3.258  -2.928  6.467   0.40 30.41 ?  158 LYS   A HD2  1 
ATOM   3430 H HD2  B LYS   A 1 158 ? 3.267  -3.382  6.320   0.40 32.17 ?  158 LYS   A HD2  1 
ATOM   3431 H HD2  T LYS   A 1 158 ? 3.566  -2.610  6.619   0.20 27.41 ?  158 LYS   A HD2  1 
ATOM   3432 H HD3  A LYS   A 1 158 ? 3.411  -2.140  7.838   0.40 30.41 ?  158 LYS   A HD3  1 
ATOM   3433 H HD3  B LYS   A 1 158 ? 3.097  -2.262  7.441   0.40 32.17 ?  158 LYS   A HD3  1 
ATOM   3434 H HD3  T LYS   A 1 158 ? 3.417  -1.722  7.932   0.20 27.41 ?  158 LYS   A HD3  1 
ATOM   3435 H HE2  A LYS   A 1 158 ? 1.196  -2.438  8.337   0.40 31.70 ?  158 LYS   A HE2  1 
ATOM   3436 H HE2  B LYS   A 1 158 ? 0.782  -2.783  7.525   0.40 33.12 ?  158 LYS   A HE2  1 
ATOM   3437 H HE2  T LYS   A 1 158 ? 1.166  -2.267  8.068   0.20 28.63 ?  158 LYS   A HE2  1 
ATOM   3438 H HE3  A LYS   A 1 158 ? 0.931  -3.101  6.919   0.40 31.70 ?  158 LYS   A HE3  1 
ATOM   3439 H HE3  B LYS   A 1 158 ? 1.056  -3.989  6.528   0.40 33.12 ?  158 LYS   A HE3  1 
ATOM   3440 H HE3  T LYS   A 1 158 ? 1.267  -3.090  6.713   0.20 28.63 ?  158 LYS   A HE3  1 
ATOM   3441 H HZ1  A LYS   A 1 158 ? 1.096  -4.703  8.527   0.40 32.52 ?  158 LYS   A HZ1  1 
ATOM   3442 H HZ1  B LYS   A 1 158 ? 0.989  -4.730  8.673   0.40 33.92 ?  158 LYS   A HZ1  1 
ATOM   3443 H HZ1  T LYS   A 1 158 ? 1.334  -4.490  8.500   0.20 29.36 ?  158 LYS   A HZ1  1 
ATOM   3444 H HZ2  A LYS   A 1 158 ? 2.193  -4.879  7.597   0.40 32.52 ?  158 LYS   A HZ2  1 
ATOM   3445 H HZ2  B LYS   A 1 158 ? 2.324  -4.953  8.154   0.40 33.92 ?  158 LYS   A HZ2  1 
ATOM   3446 H HZ2  T LYS   A 1 158 ? 2.597  -4.582  7.796   0.20 29.36 ?  158 LYS   A HZ2  1 
ATOM   3447 H HZ3  A LYS   A 1 158 ? 2.430  -4.272  8.891   0.40 32.52 ?  158 LYS   A HZ3  1 
ATOM   3448 H HZ3  B LYS   A 1 158 ? 2.074  -3.853  9.063   0.40 33.92 ?  158 LYS   A HZ3  1 
ATOM   3449 H HZ3  T LYS   A 1 158 ? 2.510  -3.833  9.033   0.20 29.36 ?  158 LYS   A HZ3  1 
ATOM   3450 N N    A ASN   A 1 159 ? 3.544  -1.007  2.949   0.40 17.55 ?  159 ASN   A N    1 
ATOM   3451 N N    B ASN   A 1 159 ? 3.423  -1.616  2.159   0.40 19.76 ?  159 ASN   A N    1 
ATOM   3452 N N    T ASN   A 1 159 ? 3.610  -1.036  2.800   0.20 18.23 ?  159 ASN   A N    1 
ATOM   3453 C CA   A ASN   A 1 159 ? 2.887  -1.680  1.839   0.40 17.21 ?  159 ASN   A CA   1 
ATOM   3454 C CA   B ASN   A 1 159 ? 2.819  -2.311  1.026   0.40 19.99 ?  159 ASN   A CA   1 
ATOM   3455 C CA   T ASN   A 1 159 ? 2.865  -1.735  1.760   0.20 18.60 ?  159 ASN   A CA   1 
ATOM   3456 C C    A ASN   A 1 159 ? 3.806  -2.728  1.225   0.40 15.81 ?  159 ASN   A C    1 
ATOM   3457 C C    B ASN   A 1 159 ? 3.729  -3.434  0.542   0.40 18.02 ?  159 ASN   A C    1 
ATOM   3458 C C    T ASN   A 1 159 ? 3.702  -2.841  1.131   0.20 18.41 ?  159 ASN   A C    1 
ATOM   3459 O O    A ASN   A 1 159 ? 3.366  -3.838  0.913   0.40 14.73 ?  159 ASN   A O    1 
ATOM   3460 O O    B ASN   A 1 159 ? 3.296  -4.579  0.358   0.40 17.85 ?  159 ASN   A O    1 
ATOM   3461 O O    T ASN   A 1 159 ? 3.176  -3.888  0.761   0.20 18.43 ?  159 ASN   A O    1 
ATOM   3462 C CB   A ASN   A 1 159 ? 2.403  -0.660  0.808   0.40 18.73 ?  159 ASN   A CB   1 
ATOM   3463 C CB   B ASN   A 1 159 ? 2.554  -1.307  -0.100  0.40 22.43 ?  159 ASN   A CB   1 
ATOM   3464 C CB   T ASN   A 1 159 ? 2.374  -0.755  0.691   0.20 19.42 ?  159 ASN   A CB   1 
ATOM   3465 C CG   A ASN   A 1 159 ? 1.143  0.061   1.255   0.40 20.97 ?  159 ASN   A CG   1 
ATOM   3466 C CG   B ASN   A 1 159 ? 1.455  -0.321  0.242   0.40 24.69 ?  159 ASN   A CG   1 
ATOM   3467 C CG   T ASN   A 1 159 ? 1.167  0.045   1.146   0.20 20.47 ?  159 ASN   A CG   1 
ATOM   3468 O OD1  A ASN   A 1 159 ? 0.337  -0.494  1.996   0.40 22.24 ?  159 ASN   A OD1  1 
ATOM   3469 O OD1  B ASN   A 1 159 ? 1.656  0.599   1.033   0.40 25.68 ?  159 ASN   A OD1  1 
ATOM   3470 O OD1  T ASN   A 1 159 ? 0.358  -0.434  1.938   0.20 21.06 ?  159 ASN   A OD1  1 
ATOM   3471 N ND2  A ASN   A 1 159 ? 0.972  1.299   0.810   0.40 21.56 ?  159 ASN   A ND2  1 
ATOM   3472 N ND2  B ASN   A 1 159 ? 0.287  -0.503  -0.365  0.40 25.18 ?  159 ASN   A ND2  1 
ATOM   3473 N ND2  T ASN   A 1 159 ? 1.041  1.267   0.646   0.20 20.74 ?  159 ASN   A ND2  1 
ATOM   3474 H H    A ASN   A 1 159 ? 3.604  -0.153  2.875   0.40 21.06 ?  159 ASN   A H    1 
ATOM   3475 H H    B ASN   A 1 159 ? 3.476  -0.764  2.068   0.40 23.71 ?  159 ASN   A H    1 
ATOM   3476 H H    T ASN   A 1 159 ? 3.737  -0.201  2.645   0.20 21.87 ?  159 ASN   A H    1 
ATOM   3477 H HA   A ASN   A 1 159 ? 2.106  -2.147  2.175   0.40 20.65 ?  159 ASN   A HA   1 
ATOM   3478 H HA   B ASN   A 1 159 ? 1.968  -2.693  1.293   0.40 23.98 ?  159 ASN   A HA   1 
ATOM   3479 H HA   T ASN   A 1 159 ? 2.087  -2.154  2.157   0.20 22.31 ?  159 ASN   A HA   1 
ATOM   3480 H HB2  A ASN   A 1 159 ? 3.088  0.006   0.669   0.40 22.47 ?  159 ASN   A HB2  1 
ATOM   3481 H HB2  B ASN   A 1 159 ? 3.363  -0.795  -0.271  0.40 26.91 ?  159 ASN   A HB2  1 
ATOM   3482 H HB2  T ASN   A 1 159 ? 3.084  -0.131  0.482   0.20 23.29 ?  159 ASN   A HB2  1 
ATOM   3483 H HB3  A ASN   A 1 159 ? 2.205  -1.119  -0.025  0.40 22.47 ?  159 ASN   A HB3  1 
ATOM   3484 H HB3  B ASN   A 1 159 ? 2.285  -1.779  -0.900  0.40 26.91 ?  159 ASN   A HB3  1 
ATOM   3485 H HB3  T ASN   A 1 159 ? 2.124  -1.254  -0.105  0.20 23.29 ?  159 ASN   A HB3  1 
ATOM   3486 H HD21 A ASN   A 1 159 ? 0.269  1.744   1.033   0.40 25.87 ?  159 ASN   A HD21 1 
ATOM   3487 H HD21 B ASN   A 1 159 ? -0.370 0.032   -0.210  0.40 30.21 ?  159 ASN   A HD21 1 
ATOM   3488 H HD21 T ASN   A 1 159 ? 0.370  1.754   0.874   0.20 24.89 ?  159 ASN   A HD21 1 
ATOM   3489 H HD22 A ASN   A 1 159 ? 1.560  1.653   0.297   0.40 25.87 ?  159 ASN   A HD22 1 
ATOM   3490 H HD22 B ASN   A 1 159 ? 0.187  -1.157  -0.913  0.40 30.21 ?  159 ASN   A HD22 1 
ATOM   3491 H HD22 T ASN   A 1 159 ? 1.627  1.568   0.097   0.20 24.89 ?  159 ASN   A HD22 1 
ATOM   3492 N N    A LEU   A 1 160 ? 5.094  -2.418  1.082   0.40 15.17 ?  160 LEU   A N    1 
ATOM   3493 N N    B LEU   A 1 160 ? 5.011  -3.120  0.354   0.40 16.52 ?  160 LEU   A N    1 
ATOM   3494 N N    T LEU   A 1 160 ? 5.006  -2.615  1.020   0.20 18.08 ?  160 LEU   A N    1 
ATOM   3495 C CA   A LEU   A 1 160 ? 6.003  -3.430  0.555   0.40 14.74 ?  160 LEU   A CA   1 
ATOM   3496 C CA   B LEU   A 1 160 ? 5.968  -4.120  -0.102  0.40 15.85 ?  160 LEU   A CA   1 
ATOM   3497 C CA   T LEU   A 1 160 ? 5.894  -3.624  0.456   0.20 17.93 ?  160 LEU   A CA   1 
ATOM   3498 C C    A LEU   A 1 160 ? 6.167  -4.591  1.533   0.40 13.07 ?  160 LEU   A C    1 
ATOM   3499 C C    B LEU   A 1 160 ? 6.116  -5.240  0.921   0.40 15.07 ?  160 LEU   A C    1 
ATOM   3500 O O    A LEU   A 1 160 ? 6.184  -5.758  1.123   0.40 12.34 ?  160 LEU   A O    1 
ATOM   3501 O O    B LEU   A 1 160 ? 6.126  -6.423  0.567   0.40 15.05 ?  160 LEU   A O    1 
ATOM   3502 C CB   A LEU   A 1 160 ? 7.354  -2.815  0.204   0.40 15.74 ?  160 LEU   A CB   1 
ATOM   3503 C CB   B LEU   A 1 160 ? 7.317  -3.452  -0.362  0.40 16.51 ?  160 LEU   A CB   1 
ATOM   3504 C CB   T LEU   A 1 160 ? 7.251  -3.017  0.111   0.20 17.83 ?  160 LEU   A CB   1 
ATOM   3505 C CG   A LEU   A 1 160 ? 8.371  -3.831  -0.305  0.40 16.73 ?  160 LEU   A CG   1 
ATOM   3506 C CG   B LEU   A 1 160 ? 8.508  -4.406  -0.430  0.40 17.57 ?  160 LEU   A CG   1 
ATOM   3507 C CG   T LEU   A 1 160 ? 8.311  -4.015  -0.348  0.20 17.84 ?  160 LEU   A CG   1 
ATOM   3508 C CD1  A LEU   A 1 160 ? 7.829  -4.594  -1.499  0.40 16.92 ?  160 LEU   A CD1  1 
ATOM   3509 C CD1  B LEU   A 1 160 ? 8.338  -5.356  -1.598  0.40 18.08 ?  160 LEU   A CD1  1 
ATOM   3510 C CD1  T LEU   A 1 160 ? 7.854  -4.758  -1.588  0.20 17.79 ?  160 LEU   A CD1  1 
ATOM   3511 C CD2  A LEU   A 1 160 ? 9.669  -3.139  -0.651  0.40 17.21 ?  160 LEU   A CD2  1 
ATOM   3512 C CD2  B LEU   A 1 160 ? 9.814  -3.636  -0.527  0.40 17.91 ?  160 LEU   A CD2  1 
ATOM   3513 C CD2  T LEU   A 1 160 ? 9.630  -3.307  -0.597  0.20 17.87 ?  160 LEU   A CD2  1 
ATOM   3514 H H    A LEU   A 1 160 ? 5.453  -1.656  1.280   0.40 18.19 ?  160 LEU   A H    1 
ATOM   3515 H H    B LEU   A 1 160 ? 5.346  -2.340  0.491   0.40 19.82 ?  160 LEU   A H    1 
ATOM   3516 H H    T LEU   A 1 160 ? 5.399  -1.887  1.266   0.20 21.69 ?  160 LEU   A H    1 
ATOM   3517 H HA   A LEU   A 1 160 ? 5.622  -3.776  -0.260  0.40 17.68 ?  160 LEU   A HA   1 
ATOM   3518 H HA   B LEU   A 1 160 ? 5.654  -4.504  -0.937  0.40 19.01 ?  160 LEU   A HA   1 
ATOM   3519 H HB2  A LEU   A 1 160 ? 7.248  -2.102  -0.464  0.40 18.88 ?  160 LEU   A HB2  1 
ATOM   3520 H HB2  B LEU   A 1 160 ? 7.271  -2.982  -1.212  0.40 19.81 ?  160 LEU   A HB2  1 
ATOM   3521 H HB2  T LEU   A 1 160 ? 7.131  -2.345  -0.586  0.20 21.39 ?  160 LEU   A HB2  1 
ATOM   3522 H HB3  A LEU   A 1 160 ? 7.732  -2.463  1.016   0.40 18.88 ?  160 LEU   A HB3  1 
ATOM   3523 H HB3  B LEU   A 1 160 ? 7.489  -2.815  0.349   0.40 19.81 ?  160 LEU   A HB3  1 
ATOM   3524 H HB3  T LEU   A 1 160 ? 7.605  -2.606  0.911   0.20 21.39 ?  160 LEU   A HB3  1 
ATOM   3525 H HG   A LEU   A 1 160 ? 8.558  -4.466  0.405   0.40 20.06 ?  160 LEU   A HG   1 
ATOM   3526 H HG   B LEU   A 1 160 ? 8.551  -4.933  0.383   0.40 21.08 ?  160 LEU   A HG   1 
ATOM   3527 H HG   T LEU   A 1 160 ? 8.452  -4.664  0.361   0.20 21.40 ?  160 LEU   A HG   1 
ATOM   3528 H HD11 A LEU   A 1 160 ? 8.548  -5.106  -1.895  0.40 20.30 ?  160 LEU   A HD11 1 
ATOM   3529 H HD11 B LEU   A 1 160 ? 9.099  -5.955  -1.624  0.40 21.69 ?  160 LEU   A HD11 1 
ATOM   3530 H HD11 T LEU   A 1 160 ? 8.577  -5.324  -1.898  0.20 21.34 ?  160 LEU   A HD11 1 
ATOM   3531 H HD12 A LEU   A 1 160 ? 7.124  -5.191  -1.201  0.40 20.30 ?  160 LEU   A HD12 1 
ATOM   3532 H HD12 B LEU   A 1 160 ? 7.522  -5.863  -1.478  0.40 21.69 ?  160 LEU   A HD12 1 
ATOM   3533 H HD12 T LEU   A 1 160 ? 7.081  -5.299  -1.365  0.20 21.34 ?  160 LEU   A HD12 1 
ATOM   3534 H HD13 A LEU   A 1 160 ? 7.477  -3.960  -2.144  0.40 20.30 ?  160 LEU   A HD13 1 
ATOM   3535 H HD13 B LEU   A 1 160 ? 8.292  -4.839  -2.416  0.40 21.69 ?  160 LEU   A HD13 1 
ATOM   3536 H HD13 T LEU   A 1 160 ? 7.621  -4.112  -2.273  0.20 21.34 ?  160 LEU   A HD13 1 
ATOM   3537 H HD21 A LEU   A 1 160 ? 10.305 -3.802  -0.961  0.40 20.64 ?  160 LEU   A HD21 1 
ATOM   3538 H HD21 B LEU   A 1 160 ? 10.550 -4.267  -0.564  0.40 21.49 ?  160 LEU   A HD21 1 
ATOM   3539 H HD21 T LEU   A 1 160 ? 10.287 -3.960  -0.884  0.20 21.44 ?  160 LEU   A HD21 1 
ATOM   3540 H HD22 A LEU   A 1 160 ? 9.502  -2.488  -1.349  0.40 20.64 ?  160 LEU   A HD22 1 
ATOM   3541 H HD22 B LEU   A 1 160 ? 9.803  -3.091  -1.328  0.40 21.49 ?  160 LEU   A HD22 1 
ATOM   3542 H HD22 T LEU   A 1 160 ? 9.503  -2.638  -1.287  0.20 21.44 ?  160 LEU   A HD22 1 
ATOM   3543 H HD23 A LEU   A 1 160 ? 10.013 -2.695  0.141   0.40 20.64 ?  160 LEU   A HD23 1 
ATOM   3544 H HD23 B LEU   A 1 160 ? 9.906  -3.068  0.257   0.40 21.49 ?  160 LEU   A HD23 1 
ATOM   3545 H HD23 T LEU   A 1 160 ? 9.923  -2.883  0.226   0.20 21.44 ?  160 LEU   A HD23 1 
ATOM   3546 N N    A TYR   A 1 161 ? 6.293  -4.295  2.827   0.60 13.61 ?  161 TYR   A N    1 
ATOM   3547 N N    B TYR   A 1 161 ? 6.261  -4.882  2.199   0.40 14.51 ?  161 TYR   A N    1 
ATOM   3548 C CA   A TYR   A 1 161 ? 6.420  -5.358  3.817   0.60 13.85 ?  161 TYR   A CA   1 
ATOM   3549 C CA   B TYR   A 1 161 ? 6.369  -5.892  3.247   0.40 14.97 ?  161 TYR   A CA   1 
ATOM   3550 C C    A TYR   A 1 161 ? 5.256  -6.332  3.727   0.60 14.54 ?  161 TYR   A C    1 
ATOM   3551 C C    B TYR   A 1 161 ? 5.207  -6.876  3.176   0.40 15.46 ?  161 TYR   A C    1 
ATOM   3552 O O    A TYR   A 1 161 ? 5.451  -7.552  3.726   0.60 14.64 ?  161 TYR   A O    1 
ATOM   3553 O O    B TYR   A 1 161 ? 5.402  -8.089  3.307   0.40 15.34 ?  161 TYR   A O    1 
ATOM   3554 C CB   A TYR   A 1 161 ? 6.501  -4.779  5.227   0.60 14.67 ?  161 TYR   A CB   1 
ATOM   3555 C CB   B TYR   A 1 161 ? 6.439  -5.194  4.610   0.40 15.29 ?  161 TYR   A CB   1 
ATOM   3556 C CG   A TYR   A 1 161 ? 6.392  -5.860  6.273   0.60 14.90 ?  161 TYR   A CG   1 
ATOM   3557 C CG   B TYR   A 1 161 ? 6.348  -6.080  5.837   0.40 16.17 ?  161 TYR   A CG   1 
ATOM   3558 C CD1  A TYR   A 1 161 ? 7.468  -6.687  6.543   0.60 15.53 ?  161 TYR   A CD1  1 
ATOM   3559 C CD1  B TYR   A 1 161 ? 5.113  -6.441  6.364   0.40 16.87 ?  161 TYR   A CD1  1 
ATOM   3560 C CD2  A TYR   A 1 161 ? 5.209  -6.064  6.979   0.60 15.33 ?  161 TYR   A CD2  1 
ATOM   3561 C CD2  B TYR   A 1 161 ? 7.492  -6.513  6.499   0.40 16.79 ?  161 TYR   A CD2  1 
ATOM   3562 C CE1  A TYR   A 1 161 ? 7.382  -7.690  7.484   0.60 15.31 ?  161 TYR   A CE1  1 
ATOM   3563 C CE1  B TYR   A 1 161 ? 5.019  -7.233  7.491   0.40 17.17 ?  161 TYR   A CE1  1 
ATOM   3564 C CE2  A TYR   A 1 161 ? 5.113  -7.066  7.932   0.60 15.57 ?  161 TYR   A CE2  1 
ATOM   3565 C CE2  B TYR   A 1 161 ? 7.407  -7.311  7.632   0.40 17.09 ?  161 TYR   A CE2  1 
ATOM   3566 C CZ   A TYR   A 1 161 ? 6.205  -7.877  8.178   0.60 15.84 ?  161 TYR   A CZ   1 
ATOM   3567 C CZ   B TYR   A 1 161 ? 6.166  -7.663  8.123   0.40 17.64 ?  161 TYR   A CZ   1 
ATOM   3568 O OH   A TYR   A 1 161 ? 6.136  -8.882  9.117   0.60 16.31 ?  161 TYR   A OH   1 
ATOM   3569 O OH   B TYR   A 1 161 ? 6.063  -8.453  9.245   0.40 18.59 ?  161 TYR   A OH   1 
ATOM   3570 H H    A TYR   A 1 161 ? 6.303  -3.499  3.150   0.60 16.32 ?  161 TYR   A H    1 
ATOM   3571 H H    B TYR   A 1 161 ? 6.299  -4.071  2.478   0.40 17.41 ?  161 TYR   A H    1 
ATOM   3572 H HA   A TYR   A 1 161 ? 7.231  -5.853  3.647   0.60 16.61 ?  161 TYR   A HA   1 
ATOM   3573 H HA   B TYR   A 1 161 ? 7.190  -6.392  3.120   0.40 17.96 ?  161 TYR   A HA   1 
ATOM   3574 H HB2  A TYR   A 1 161 ? 7.351  -4.327  5.338   0.60 17.59 ?  161 TYR   A HB2  1 
ATOM   3575 H HB2  B TYR   A 1 161 ? 7.286  -4.724  4.661   0.40 18.35 ?  161 TYR   A HB2  1 
ATOM   3576 H HB3  A TYR   A 1 161 ? 5.770  -4.148  5.357   0.60 17.59 ?  161 TYR   A HB3  1 
ATOM   3577 H HB3  B TYR   A 1 161 ? 5.713  -4.558  4.662   0.40 18.35 ?  161 TYR   A HB3  1 
ATOM   3578 H HD1  A TYR   A 1 161 ? 8.261  -6.564  6.075   0.60 18.63 ?  161 TYR   A HD1  1 
ATOM   3579 H HD1  B TYR   A 1 161 ? 4.334  -6.158  5.943   0.40 20.24 ?  161 TYR   A HD1  1 
ATOM   3580 H HD2  A TYR   A 1 161 ? 4.469  -5.516  6.818   0.60 18.39 ?  161 TYR   A HD2  1 
ATOM   3581 H HD2  B TYR   A 1 161 ? 8.329  -6.279  6.169   0.40 20.14 ?  161 TYR   A HD2  1 
ATOM   3582 H HE1  A TYR   A 1 161 ? 8.115  -8.238  7.648   0.60 18.36 ?  161 TYR   A HE1  1 
ATOM   3583 H HE1  B TYR   A 1 161 ? 4.183  -7.469  7.827   0.40 20.60 ?  161 TYR   A HE1  1 
ATOM   3584 H HE2  A TYR   A 1 161 ? 4.315  -7.195  8.401   0.60 18.67 ?  161 TYR   A HE2  1 
ATOM   3585 H HE2  B TYR   A 1 161 ? 8.181  -7.598  8.064   0.40 20.50 ?  161 TYR   A HE2  1 
ATOM   3586 H HH   A TYR   A 1 161 ? 5.365  -8.900  9.466   0.60 19.57 ?  161 TYR   A HH   1 
ATOM   3587 H HH   B TYR   A 1 161 ? 6.822  -8.641  9.544   0.40 22.30 ?  161 TYR   A HH   1 
ATOM   3588 N N    A ASP   A 1 162 ? 4.028  -5.811  3.664   0.60 15.25 ?  162 ASP   A N    1 
ATOM   3589 N N    B ASP   A 1 162 ? 3.992  -6.371  2.941   0.40 16.11 ?  162 ASP   A N    1 
ATOM   3590 C CA   A ASP   A 1 162 ? 2.869  -6.697  3.610   0.60 16.15 ?  162 ASP   A CA   1 
ATOM   3591 C CA   B ASP   A 1 162 ? 2.827  -7.242  2.804   0.40 17.33 ?  162 ASP   A CA   1 
ATOM   3592 C C    A ASP   A 1 162 ? 2.892  -7.555  2.354   0.60 16.06 ?  162 ASP   A C    1 
ATOM   3593 C C    B ASP   A 1 162 ? 2.927  -8.110  1.554   0.40 17.40 ?  162 ASP   A C    1 
ATOM   3594 O O    A ASP   A 1 162 ? 2.536  -8.741  2.392   0.60 16.02 ?  162 ASP   A O    1 
ATOM   3595 O O    B ASP   A 1 162 ? 2.583  -9.298  1.587   0.40 17.40 ?  162 ASP   A O    1 
ATOM   3596 C CB   A ASP   A 1 162 ? 1.574  -5.890  3.694   0.60 17.75 ?  162 ASP   A CB   1 
ATOM   3597 C CB   B ASP   A 1 162 ? 1.554  -6.395  2.747   0.40 19.26 ?  162 ASP   A CB   1 
ATOM   3598 C CG   A ASP   A 1 162 ? 1.281  -5.402  5.086   0.60 19.00 ?  162 ASP   A CG   1 
ATOM   3599 C CG   B ASP   A 1 162 ? 1.317  -5.603  4.021   0.40 21.27 ?  162 ASP   A CG   1 
ATOM   3600 O OD1  A ASP   A 1 162 ? 1.937  -5.855  6.046   0.60 19.52 ?  162 ASP   A OD1  1 
ATOM   3601 O OD1  B ASP   A 1 162 ? 1.769  -6.050  5.095   0.40 21.65 ?  162 ASP   A OD1  1 
ATOM   3602 O OD2  A ASP   A 1 162 ? 0.375  -4.561  5.214   0.60 20.22 -1 162 ASP   A OD2  1 
ATOM   3603 O OD2  B ASP   A 1 162 ? 0.654  -4.545  3.952   0.40 22.39 -1 162 ASP   A OD2  1 
ATOM   3604 H H    A ASP   A 1 162 ? 3.843  -4.961  3.642   0.60 18.29 ?  162 ASP   A H    1 
ATOM   3605 H H    B ASP   A 1 162 ? 3.820  -5.538  2.857   0.40 19.32 ?  162 ASP   A H    1 
ATOM   3606 H HA   A ASP   A 1 162 ? 2.899  -7.287  4.369   0.60 19.38 ?  162 ASP   A HA   1 
ATOM   3607 H HA   B ASP   A 1 162 ? 2.764  -7.828  3.573   0.40 20.79 ?  162 ASP   A HA   1 
ATOM   3608 H HB2  A ASP   A 1 162 ? 1.636  -5.104  3.134   0.60 21.29 ?  162 ASP   A HB2  1 
ATOM   3609 H HB2  B ASP   A 1 162 ? 1.615  -5.789  1.987   0.40 23.10 ?  162 ASP   A HB2  1 
ATOM   3610 H HB3  A ASP   A 1 162 ? 0.829  -6.444  3.419   0.60 21.29 ?  162 ASP   A HB3  1 
ATOM   3611 H HB3  B ASP   A 1 162 ? 0.791  -6.974  2.641   0.40 23.10 ?  162 ASP   A HB3  1 
ATOM   3612 N N    A LYS   A 1 163 ? 3.304  -6.975  1.226   0.60 16.46 ?  163 LYS   A N    1 
ATOM   3613 N N    B LYS   A 1 163 ? 3.375  -7.523  0.439   0.40 17.79 ?  163 LYS   A N    1 
ATOM   3614 C CA   A LYS   A 1 163 ? 3.386  -7.767  0.005   0.60 17.52 ?  163 LYS   A CA   1 
ATOM   3615 C CA   B LYS   A 1 163 ? 3.564  -8.282  -0.796  0.40 18.86 ?  163 LYS   A CA   1 
ATOM   3616 C C    A LYS   A 1 163 ? 4.472  -8.828  0.112   0.60 16.66 ?  163 LYS   A C    1 
ATOM   3617 C C    B LYS   A 1 163 ? 4.591  -9.393  -0.601  0.40 17.28 ?  163 LYS   A C    1 
ATOM   3618 O O    A LYS   A 1 163 ? 4.296  -9.949  -0.374  0.60 16.61 ?  163 LYS   A O    1 
ATOM   3619 O O    B LYS   A 1 163 ? 4.387  -10.529 -1.051  0.40 17.19 ?  163 LYS   A O    1 
ATOM   3620 C CB   A LYS   A 1 163 ? 3.624  -6.864  -1.206  0.60 20.30 ?  163 LYS   A CB   1 
ATOM   3621 C CB   B LYS   A 1 163 ? 4.006  -7.321  -1.909  0.40 21.86 ?  163 LYS   A CB   1 
ATOM   3622 C CG   A LYS   A 1 163 ? 3.680  -7.624  -2.521  0.60 23.61 ?  163 LYS   A CG   1 
ATOM   3623 C CG   B LYS   A 1 163 ? 4.193  -7.947  -3.293  0.40 24.88 ?  163 LYS   A CG   1 
ATOM   3624 C CD   A LYS   A 1 163 ? 4.104  -6.726  -3.665  0.60 26.83 ?  163 LYS   A CD   1 
ATOM   3625 C CD   B LYS   A 1 163 ? 3.304  -7.283  -4.350  0.40 27.55 ?  163 LYS   A CD   1 
ATOM   3626 C CE   A LYS   A 1 163 ? 4.079  -7.476  -4.984  0.60 29.37 ?  163 LYS   A CE   1 
ATOM   3627 C CE   B LYS   A 1 163 ? 3.950  -6.050  -4.984  0.40 29.48 ?  163 LYS   A CE   1 
ATOM   3628 N NZ   A LYS   A 1 163 ? 4.668  -6.681  -6.095  0.60 30.92 ?  163 LYS   A NZ   1 
ATOM   3629 N NZ   B LYS   A 1 163 ? 4.956  -6.400  -6.030  0.40 30.75 ?  163 LYS   A NZ   1 
ATOM   3630 H H    A LYS   A 1 163 ? 3.529  -6.143  1.142   0.60 19.75 ?  163 LYS   A H    1 
ATOM   3631 H H    B LYS   A 1 163 ? 3.566  -6.687  0.372   0.40 21.34 ?  163 LYS   A H    1 
ATOM   3632 H HA   A LYS   A 1 163 ? 2.537  -8.219  -0.129  0.60 21.02 ?  163 LYS   A HA   1 
ATOM   3633 H HA   B LYS   A 1 163 ? 2.721  -8.681  -1.062  0.40 22.63 ?  163 LYS   A HA   1 
ATOM   3634 H HB2  A LYS   A 1 163 ? 2.895  -6.220  -1.269  0.60 24.35 ?  163 LYS   A HB2  1 
ATOM   3635 H HB2  B LYS   A 1 163 ? 3.344  -6.617  -1.993  0.40 26.23 ?  163 LYS   A HB2  1 
ATOM   3636 H HB3  A LYS   A 1 163 ? 4.463  -6.398  -1.093  0.60 24.35 ?  163 LYS   A HB3  1 
ATOM   3637 H HB3  B LYS   A 1 163 ? 4.857  -6.930  -1.656  0.40 26.23 ?  163 LYS   A HB3  1 
ATOM   3638 H HG2  A LYS   A 1 163 ? 4.326  -8.344  -2.452  0.60 28.32 ?  163 LYS   A HG2  1 
ATOM   3639 H HG2  B LYS   A 1 163 ? 5.120  -7.839  -3.569  0.40 29.85 ?  163 LYS   A HG2  1 
ATOM   3640 H HG3  A LYS   A 1 163 ? 2.801  -7.982  -2.723  0.60 28.32 ?  163 LYS   A HG3  1 
ATOM   3641 H HG3  B LYS   A 1 163 ? 3.966  -8.887  -3.256  0.40 29.85 ?  163 LYS   A HG3  1 
ATOM   3642 H HD2  A LYS   A 1 163 ? 3.491  -5.977  -3.728  0.60 32.19 ?  163 LYS   A HD2  1 
ATOM   3643 H HD2  B LYS   A 1 163 ? 3.128  -7.920  -5.058  0.40 33.06 ?  163 LYS   A HD2  1 
ATOM   3644 H HD3  A LYS   A 1 163 ? 5.008  -6.411  -3.508  0.60 32.19 ?  163 LYS   A HD3  1 
ATOM   3645 H HD3  B LYS   A 1 163 ? 2.470  -7.005  -3.942  0.40 33.06 ?  163 LYS   A HD3  1 
ATOM   3646 H HE2  A LYS   A 1 163 ? 4.581  -8.300  -4.891  0.60 35.23 ?  163 LYS   A HE2  1 
ATOM   3647 H HE2  B LYS   A 1 163 ? 3.261  -5.509  -5.404  0.40 35.37 ?  163 LYS   A HE2  1 
ATOM   3648 H HE3  A LYS   A 1 163 ? 3.160  -7.677  -5.215  0.60 35.23 ?  163 LYS   A HE3  1 
ATOM   3649 H HE3  B LYS   A 1 163 ? 4.402  -5.536  -4.298  0.40 35.37 ?  163 LYS   A HE3  1 
ATOM   3650 H HZ1  A LYS   A 1 163 ? 4.640  -7.148  -6.852  0.60 37.10 ?  163 LYS   A HZ1  1 
ATOM   3651 H HZ1  B LYS   A 1 163 ? 5.160  -5.678  -6.511  0.40 36.89 ?  163 LYS   A HZ1  1 
ATOM   3652 H HZ2  A LYS   A 1 163 ? 4.209  -5.926  -6.203  0.60 37.10 ?  163 LYS   A HZ2  1 
ATOM   3653 H HZ2  B LYS   A 1 163 ? 5.697  -6.710  -5.649  0.40 36.89 ?  163 LYS   A HZ2  1 
ATOM   3654 H HZ3  A LYS   A 1 163 ? 5.515  -6.480  -5.910  0.60 37.10 ?  163 LYS   A HZ3  1 
ATOM   3655 H HZ3  B LYS   A 1 163 ? 4.625  -7.023  -6.575  0.40 36.89 ?  163 LYS   A HZ3  1 
ATOM   3656 N N    A LEU   A 1 164 ? 5.601  -8.497  0.741   0.60 15.05 ?  164 LEU   A N    1 
ATOM   3657 N N    B LEU   A 1 164 ? 5.699  -9.082  0.078   0.40 16.27 ?  164 LEU   A N    1 
ATOM   3658 C CA   A LEU   A 1 164 ? 6.682  -9.472  0.875   0.60 14.56 ?  164 LEU   A CA   1 
ATOM   3659 C CA   B LEU   A 1 164 ? 6.769  -10.057 0.274   0.40 16.28 ?  164 LEU   A CA   1 
ATOM   3660 C C    A LEU   A 1 164 ? 6.248  -10.666 1.717   0.60 14.83 ?  164 LEU   A C    1 
ATOM   3661 C C    B LEU   A 1 164 ? 6.278  -11.261 1.060   0.40 17.35 ?  164 LEU   A C    1 
ATOM   3662 O O    A LEU   A 1 164 ? 6.549  -11.819 1.385   0.60 14.46 ?  164 LEU   A O    1 
ATOM   3663 O O    B LEU   A 1 164 ? 6.531  -12.410 0.684   0.40 17.97 ?  164 LEU   A O    1 
ATOM   3664 C CB   A LEU   A 1 164 ? 7.900  -8.795  1.497   0.60 14.05 ?  164 LEU   A CB   1 
ATOM   3665 C CB   B LEU   A 1 164 ? 7.940  -9.401  1.009   0.40 15.81 ?  164 LEU   A CB   1 
ATOM   3666 C CG   A LEU   A 1 164 ? 8.673  -7.858  0.569   0.60 14.47 ?  164 LEU   A CG   1 
ATOM   3667 C CG   B LEU   A 1 164 ? 8.803  -8.424  0.219   0.40 15.98 ?  164 LEU   A CG   1 
ATOM   3668 C CD1  A LEU   A 1 164 ? 9.615  -7.001  1.378   0.60 14.37 ?  164 LEU   A CD1  1 
ATOM   3669 C CD1  B LEU   A 1 164 ? 9.680  -7.599  1.149   0.40 15.77 ?  164 LEU   A CD1  1 
ATOM   3670 C CD2  A LEU   A 1 164 ? 9.456  -8.643  -0.480  0.60 14.71 ?  164 LEU   A CD2  1 
ATOM   3671 C CD2  B LEU   A 1 164 ? 9.660  -9.189  -0.753  0.40 16.44 ?  164 LEU   A CD2  1 
ATOM   3672 H H    A LEU   A 1 164 ? 5.764  -7.715  1.089   0.60 18.06 ?  164 LEU   A H    1 
ATOM   3673 H H    B LEU   A 1 164 ? 5.852  -8.320  0.431   0.40 19.51 ?  164 LEU   A H    1 
ATOM   3674 H HA   A LEU   A 1 164 ? 6.932  -9.780  -0.009  0.60 17.47 ?  164 LEU   A HA   1 
ATOM   3675 H HA   B LEU   A 1 164 ? 7.080  -10.373 -0.588  0.40 19.53 ?  164 LEU   A HA   1 
ATOM   3676 H HB2  A LEU   A 1 164 ? 7.610  -8.263  2.256   0.60 16.86 ?  164 LEU   A HB2  1 
ATOM   3677 H HB2  B LEU   A 1 164 ? 7.584  -8.920  1.769   0.40 18.97 ?  164 LEU   A HB2  1 
ATOM   3678 H HB3  A LEU   A 1 164 ? 8.517  -9.476  1.790   0.60 16.86 ?  164 LEU   A HB3  1 
ATOM   3679 H HB3  B LEU   A 1 164 ? 8.528  -10.107 1.325   0.40 18.97 ?  164 LEU   A HB3  1 
ATOM   3680 H HG   A LEU   A 1 164 ? 8.056  -7.268  0.106   0.60 17.36 ?  164 LEU   A HG   1 
ATOM   3681 H HG   B LEU   A 1 164 ? 8.233  -7.821  -0.282  0.40 19.17 ?  164 LEU   A HG   1 
ATOM   3682 H HD11 A LEU   A 1 164 ? 9.972  -6.297  0.814   0.60 17.24 ?  164 LEU   A HD11 1 
ATOM   3683 H HD11 B LEU   A 1 164 ? 10.218 -6.992  0.618   0.40 18.92 ?  164 LEU   A HD11 1 
ATOM   3684 H HD12 A LEU   A 1 164 ? 9.122  -6.617  2.118   0.60 17.24 ?  164 LEU   A HD12 1 
ATOM   3685 H HD12 B LEU   A 1 164 ? 9.114  -7.098  1.756   0.40 18.92 ?  164 LEU   A HD12 1 
ATOM   3686 H HD13 A LEU   A 1 164 ? 10.334 -7.557  1.712   0.60 17.24 ?  164 LEU   A HD13 1 
ATOM   3687 H HD13 B LEU   A 1 164 ? 10.257 -8.198  1.651   0.40 18.92 ?  164 LEU   A HD13 1 
ATOM   3688 H HD21 A LEU   A 1 164 ? 9.997  -8.029  -1.003  0.60 17.64 ?  164 LEU   A HD21 1 
ATOM   3689 H HD21 B LEU   A 1 164 ? 10.120 -8.562  -1.329  0.40 19.73 ?  164 LEU   A HD21 1 
ATOM   3690 H HD22 A LEU   A 1 164 ? 10.030 -9.284  -0.030  0.60 17.64 ?  164 LEU   A HD22 1 
ATOM   3691 H HD22 B LEU   A 1 164 ? 10.305 -9.718  -0.255  0.40 19.73 ?  164 LEU   A HD22 1 
ATOM   3692 H HD23 A LEU   A 1 164 ? 8.832  -9.107  -1.059  0.60 17.64 ?  164 LEU   A HD23 1 
ATOM   3693 H HD23 B LEU   A 1 164 ? 9.092  -9.772  -1.279  0.40 19.73 ?  164 LEU   A HD23 1 
ATOM   3694 N N    A VAL   A 1 165 ? 5.544  -10.407 2.814   0.60 14.07 ?  165 VAL   A N    1 
ATOM   3695 N N    B VAL   A 1 165 ? 5.593  -11.018 2.177   0.40 17.96 ?  165 VAL   A N    1 
ATOM   3696 C CA   A VAL   A 1 165 ? 5.081  -11.494 3.670   0.60 14.29 ?  165 VAL   A CA   1 
ATOM   3697 C CA   B VAL   A 1 165 ? 5.087  -12.125 2.979   0.40 18.91 ?  165 VAL   A CA   1 
ATOM   3698 C C    A VAL   A 1 165 ? 4.061  -12.359 2.940   0.60 14.50 ?  165 VAL   A C    1 
ATOM   3699 C C    B VAL   A 1 165 ? 4.047  -12.917 2.196   0.40 20.07 ?  165 VAL   A C    1 
ATOM   3700 O O    A VAL   A 1 165 ? 4.168  -13.591 2.922   0.60 14.57 ?  165 VAL   A O    1 
ATOM   3701 O O    B VAL   A 1 165 ? 3.997  -14.149 2.273   0.40 19.87 ?  165 VAL   A O    1 
ATOM   3702 C CB   A VAL   A 1 165 ? 4.513  -10.929 4.983   0.60 14.48 ?  165 VAL   A CB   1 
ATOM   3703 C CB   B VAL   A 1 165 ? 4.539  -11.603 4.320   0.40 19.59 ?  165 VAL   A CB   1 
ATOM   3704 C CG1  A VAL   A 1 165 ? 3.744  -12.008 5.741   0.60 15.11 ?  165 VAL   A CG1  1 
ATOM   3705 C CG1  B VAL   A 1 165 ? 4.040  -12.757 5.172   0.40 19.92 ?  165 VAL   A CG1  1 
ATOM   3706 C CG2  A VAL   A 1 165 ? 5.630  -10.337 5.832   0.60 14.96 ?  165 VAL   A CG2  1 
ATOM   3707 C CG2  B VAL   A 1 165 ? 5.612  -10.818 5.056   0.40 19.51 ?  165 VAL   A CG2  1 
ATOM   3708 H H    A VAL   A 1 165 ? 5.320  -9.613  3.078   0.60 16.87 ?  165 VAL   A H    1 
ATOM   3709 H H    B VAL   A 1 165 ? 5.410  -10.240 2.486   0.40 21.54 ?  165 VAL   A H    1 
ATOM   3710 H HA   A VAL   A 1 165 ? 5.837  -12.050 3.889   0.60 17.14 ?  165 VAL   A HA   1 
ATOM   3711 H HA   B VAL   A 1 165 ? 5.823  -12.728 3.181   0.40 22.68 ?  165 VAL   A HA   1 
ATOM   3712 H HB   A VAL   A 1 165 ? 3.892  -10.211 4.776   0.60 17.37 ?  165 VAL   A HB   1 
ATOM   3713 H HB   B VAL   A 1 165 ? 3.790  -11.012 4.148   0.40 23.50 ?  165 VAL   A HB   1 
ATOM   3714 H HG11 A VAL   A 1 165 ? 3.645  -11.734 6.665   0.60 18.12 ?  165 VAL   A HG11 1 
ATOM   3715 H HG11 B VAL   A 1 165 ? 3.853  -12.430 6.065   0.40 23.89 ?  165 VAL   A HG11 1 
ATOM   3716 H HG12 A VAL   A 1 165 ? 2.867  -12.115 5.335   0.60 18.12 ?  165 VAL   A HG12 1 
ATOM   3717 H HG12 B VAL   A 1 165 ? 3.231  -13.120 4.778   0.40 23.89 ?  165 VAL   A HG12 1 
ATOM   3718 H HG13 A VAL   A 1 165 ? 4.237  -12.840 5.692   0.60 18.12 ?  165 VAL   A HG13 1 
ATOM   3719 H HG13 B VAL   A 1 165 ? 4.727  -13.442 5.209   0.40 23.89 ?  165 VAL   A HG13 1 
ATOM   3720 H HG21 A VAL   A 1 165 ? 5.261  -10.040 6.678   0.60 17.95 ?  165 VAL   A HG21 1 
ATOM   3721 H HG21 B VAL   A 1 165 ? 5.253  -10.507 5.899   0.40 23.41 ?  165 VAL   A HG21 1 
ATOM   3722 H HG22 A VAL   A 1 165 ? 6.305  -11.016 5.985   0.60 17.95 ?  165 VAL   A HG22 1 
ATOM   3723 H HG22 B VAL   A 1 165 ? 6.373  -11.399 5.213   0.40 23.41 ?  165 VAL   A HG22 1 
ATOM   3724 H HG23 A VAL   A 1 165 ? 6.021  -9.583  5.360   0.60 17.95 ?  165 VAL   A HG23 1 
ATOM   3725 H HG23 B VAL   A 1 165 ? 5.884  -10.062 4.514   0.40 23.41 ?  165 VAL   A HG23 1 
ATOM   3726 N N    A SER   A 1 166 ? 3.055  -11.730 2.328   0.60 14.92 ?  166 SER   A N    1 
ATOM   3727 N N    B SER   A 1 166 ? 3.219  -12.223 1.409   0.40 21.82 ?  166 SER   A N    1 
ATOM   3728 C CA   A SER   A 1 166 ? 1.946  -12.493 1.761   0.60 16.06 ?  166 SER   A CA   1 
ATOM   3729 C CA   B SER   A 1 166 ? 2.145  -12.876 0.664   0.40 23.83 ?  166 SER   A CA   1 
ATOM   3730 C C    A SER   A 1 166 ? 2.365  -13.329 0.562   0.60 17.24 ?  166 SER   A C    1 
ATOM   3731 C C    B SER   A 1 166 ? 2.673  -13.637 -0.546  0.40 25.57 ?  166 SER   A C    1 
ATOM   3732 O O    A SER   A 1 166 ? 1.681  -14.307 0.236   0.60 19.28 ?  166 SER   A O    1 
ATOM   3733 O O    B SER   A 1 166 ? 2.134  -14.693 -0.898  0.40 26.37 ?  166 SER   A O    1 
ATOM   3734 C CB   A SER   A 1 166 ? 0.805  -11.563 1.339   0.60 17.28 ?  166 SER   A CB   1 
ATOM   3735 C CB   B SER   A 1 166 ? 1.123  -11.833 0.206   0.40 24.22 ?  166 SER   A CB   1 
ATOM   3736 O OG   A SER   A 1 166 ? 0.218  -10.914 2.452   0.60 19.29 ?  166 SER   A OG   1 
ATOM   3737 O OG   B SER   A 1 166 ? 1.003  -10.786 1.150   0.40 24.69 ?  166 SER   A OG   1 
ATOM   3738 H H    A SER   A 1 166 ? 2.987  -10.873 2.229   0.60 17.89 ?  166 SER   A H    1 
ATOM   3739 H H    B SER   A 1 166 ? 3.261  -11.377 1.291   0.40 26.17 ?  166 SER   A H    1 
ATOM   3740 H HA   A SER   A 1 166 ? 1.597  -13.090 2.443   0.60 19.26 ?  166 SER   A HA   1 
ATOM   3741 H HA   B SER   A 1 166 ? 1.692  -13.513 1.234   0.40 28.60 ?  166 SER   A HA   1 
ATOM   3742 H HB2  A SER   A 1 166 ? 1.152  -10.892 0.731   0.60 20.72 ?  166 SER   A HB2  1 
ATOM   3743 H HB2  B SER   A 1 166 ? 1.405  -11.463 -0.646  0.40 29.05 ?  166 SER   A HB2  1 
ATOM   3744 H HB3  A SER   A 1 166 ? 0.118  -12.087 0.893   0.60 20.72 ?  166 SER   A HB3  1 
ATOM   3745 H HB3  B SER   A 1 166 ? 0.257  -12.259 0.110   0.40 29.05 ?  166 SER   A HB3  1 
ATOM   3746 H HG   A SER   A 1 166 ? -0.401 -10.406 2.198   0.60 23.14 ?  166 SER   A HG   1 
ATOM   3747 H HG   B SER   A 1 166 ? 0.447  -10.218 0.878   0.40 29.62 ?  166 SER   A HG   1 
ATOM   3748 N N    A SER   A 1 167 ? 3.454  -12.961 -0.108  0.60 16.27 ?  167 SER   A N    1 
ATOM   3749 N N    B SER   A 1 167 ? 3.711  -13.118 -1.196  0.40 26.29 ?  167 SER   A N    1 
ATOM   3750 C CA   A SER   A 1 167 ? 3.913  -13.678 -1.286  0.60 17.15 ?  167 SER   A CA   1 
ATOM   3751 C CA   B SER   A 1 167 ? 4.251  -13.712 -2.411  0.40 26.89 ?  167 SER   A CA   1 
ATOM   3752 C C    A SER   A 1 167 ? 5.061  -14.635 -0.991  0.60 17.15 ?  167 SER   A C    1 
ATOM   3753 C C    B SER   A 1 167 ? 5.425  -14.642 -2.142  0.40 27.84 ?  167 SER   A C    1 
ATOM   3754 O O    A SER   A 1 167 ? 5.555  -15.289 -1.915  0.60 17.88 ?  167 SER   A O    1 
ATOM   3755 O O    B SER   A 1 167 ? 5.978  -15.211 -3.089  0.40 28.39 ?  167 SER   A O    1 
ATOM   3756 C CB   A SER   A 1 167 ? 4.335  -12.683 -2.377  0.60 17.77 ?  167 SER   A CB   1 
ATOM   3757 C CB   B SER   A 1 167 ? 4.671  -12.613 -3.396  0.40 26.54 ?  167 SER   A CB   1 
ATOM   3758 O OG   A SER   A 1 167 ? 5.388  -11.842 -1.925  0.60 18.70 ?  167 SER   A OG   1 
ATOM   3759 O OG   B SER   A 1 167 ? 5.473  -11.636 -2.757  0.40 26.25 ?  167 SER   A OG   1 
ATOM   3760 H H    A SER   A 1 167 ? 3.941  -12.278 0.103   0.60 19.52 ?  167 SER   A H    1 
ATOM   3761 H H    B SER   A 1 167 ? 4.139  -12.416 -0.938  0.40 31.55 ?  167 SER   A H    1 
ATOM   3762 H HA   A SER   A 1 167 ? 3.175  -14.198 -1.632  0.60 20.57 ?  167 SER   A HA   1 
ATOM   3763 H HA   B SER   A 1 167 ? 3.560  -14.231 -2.841  0.40 32.26 ?  167 SER   A HA   1 
ATOM   3764 H HB2  A SER   A 1 167 ? 4.639  -13.182 -3.151  0.60 21.32 ?  167 SER   A HB2  1 
ATOM   3765 H HB2  B SER   A 1 167 ? 5.179  -13.010 -4.123  0.40 31.84 ?  167 SER   A HB2  1 
ATOM   3766 H HB3  A SER   A 1 167 ? 3.564  -12.141 -2.620  0.60 21.32 ?  167 SER   A HB3  1 
ATOM   3767 H HB3  B SER   A 1 167 ? 3.874  -12.182 -3.752  0.40 31.84 ?  167 SER   A HB3  1 
ATOM   3768 H HG   A SER   A 1 167 ? 5.117  -11.388 -1.267  0.60 22.43 ?  167 SER   A HG   1 
ATOM   3769 H HG   B SER   A 1 167 ? 4.990  -11.004 -2.484  0.40 31.49 ?  167 SER   A HG   1 
ATOM   3770 N N    A PHE   A 1 168 ? 5.492  -14.741 0.265   0.60 16.75 ?  168 PHE   A N    1 
ATOM   3771 N N    B PHE   A 1 168 ? 5.809  -14.819 -0.881  0.40 28.03 ?  168 PHE   A N    1 
ATOM   3772 C CA   A PHE   A 1 168 ? 6.666  -15.548 0.575   0.60 16.88 ?  168 PHE   A CA   1 
ATOM   3773 C CA   B PHE   A 1 168 ? 6.976  -15.628 -0.559  0.40 27.93 ?  168 PHE   A CA   1 
ATOM   3774 C C    A PHE   A 1 168 ? 6.351  -17.030 0.455   0.60 17.92 ?  168 PHE   A C    1 
ATOM   3775 C C    B PHE   A 1 168 ? 6.702  -17.094 -0.859  0.40 29.63 ?  168 PHE   A C    1 
ATOM   3776 O O    A PHE   A 1 168 ? 5.365  -17.513 1.017   0.60 19.78 ?  168 PHE   A O    1 
ATOM   3777 O O    B PHE   A 1 168 ? 5.676  -17.645 -0.447  0.40 30.12 ?  168 PHE   A O    1 
ATOM   3778 C CB   A PHE   A 1 168 ? 7.166  -15.263 1.989   0.60 16.27 ?  168 PHE   A CB   1 
ATOM   3779 C CB   B PHE   A 1 168 ? 7.338  -15.461 0.913   0.40 26.13 ?  168 PHE   A CB   1 
ATOM   3780 C CG   A PHE   A 1 168 ? 8.439  -15.995 2.322   0.60 15.42 ?  168 PHE   A CG   1 
ATOM   3781 C CG   B PHE   A 1 168 ? 8.586  -16.191 1.313   0.40 24.56 ?  168 PHE   A CG   1 
ATOM   3782 C CD1  A PHE   A 1 168 ? 9.624  -15.624 1.720   0.60 15.47 ?  168 PHE   A CD1  1 
ATOM   3783 C CD1  B PHE   A 1 168 ? 9.804  -15.869 0.738   0.40 23.90 ?  168 PHE   A CD1  1 
ATOM   3784 C CD2  A PHE   A 1 168 ? 8.450  -17.065 3.207   0.60 15.03 ?  168 PHE   A CD2  1 
ATOM   3785 C CD2  B PHE   A 1 168 ? 8.544  -17.192 2.268   0.40 23.73 ?  168 PHE   A CD2  1 
ATOM   3786 C CE1  A PHE   A 1 168 ? 10.796 -16.291 2.001   0.60 15.12 ?  168 PHE   A CE1  1 
ATOM   3787 C CE1  B PHE   A 1 168 ? 10.956 -16.538 1.104   0.40 23.42 ?  168 PHE   A CE1  1 
ATOM   3788 C CE2  A PHE   A 1 168 ? 9.633  -17.731 3.497   0.60 15.16 ?  168 PHE   A CE2  1 
ATOM   3789 C CE2  B PHE   A 1 168 ? 9.692  -17.864 2.639   0.40 23.35 ?  168 PHE   A CE2  1 
ATOM   3790 C CZ   A PHE   A 1 168 ? 10.802 -17.342 2.890   0.60 15.40 ?  168 PHE   A CZ   1 
ATOM   3791 C CZ   B PHE   A 1 168 ? 10.899 -17.536 2.056   0.40 23.23 ?  168 PHE   A CZ   1 
ATOM   3792 H H    A PHE   A 1 168 ? 5.132  -14.351 0.946   0.60 20.09 ?  168 PHE   A H    1 
ATOM   3793 H H    B PHE   A 1 168 ? 5.412  -14.478 -0.200  0.40 33.63 ?  168 PHE   A H    1 
ATOM   3794 H HA   A PHE   A 1 168 ? 7.374  -15.333 -0.048  0.60 20.25 ?  168 PHE   A HA   1 
ATOM   3795 H HA   B PHE   A 1 168 ? 7.726  -15.338 -1.099  0.40 33.50 ?  168 PHE   A HA   1 
ATOM   3796 H HB2  A PHE   A 1 168 ? 7.334  -14.312 2.080   0.60 19.51 ?  168 PHE   A HB2  1 
ATOM   3797 H HB2  B PHE   A 1 168 ? 7.475  -14.522 1.097   0.40 31.35 ?  168 PHE   A HB2  1 
ATOM   3798 H HB3  A PHE   A 1 168 ? 6.485  -15.539 2.625   0.60 19.51 ?  168 PHE   A HB3  1 
ATOM   3799 H HB3  B PHE   A 1 168 ? 6.608  -15.802 1.453   0.40 31.35 ?  168 PHE   A HB3  1 
ATOM   3800 H HD1  A PHE   A 1 168 ? 9.632  -14.915 1.120   0.60 18.55 ?  168 PHE   A HD1  1 
ATOM   3801 H HD1  B PHE   A 1 168 ? 9.847  -15.197 0.092   0.40 28.67 ?  168 PHE   A HD1  1 
ATOM   3802 H HD2  A PHE   A 1 168 ? 7.657  -17.327 3.623   0.60 18.03 ?  168 PHE   A HD2  1 
ATOM   3803 H HD2  B PHE   A 1 168 ? 7.731  -17.416 2.660   0.40 28.47 ?  168 PHE   A HD2  1 
ATOM   3804 H HE1  A PHE   A 1 168 ? 11.593 -16.028 1.597   0.60 18.14 ?  168 PHE   A HE1  1 
ATOM   3805 H HE1  B PHE   A 1 168 ? 11.769 -16.316 0.710   0.40 28.10 ?  168 PHE   A HE1  1 
ATOM   3806 H HE2  A PHE   A 1 168 ? 9.628  -18.441 4.098   0.60 18.19 ?  168 PHE   A HE2  1 
ATOM   3807 H HE2  B PHE   A 1 168 ? 9.652  -18.536 3.280   0.40 28.02 ?  168 PHE   A HE2  1 
ATOM   3808 H HZ   A PHE   A 1 168 ? 11.596 -17.788 3.082   0.60 18.47 ?  168 PHE   A HZ   1 
ATOM   3809 H HZ   B PHE   A 1 168 ? 11.674 -17.986 2.304   0.40 27.87 ?  168 PHE   A HZ   1 
ATOM   3810 N N    A LEU   A 1 169 ? 7.212  -17.762 -0.241  0.60 19.29 ?  169 LEU   A N    1 
ATOM   3811 N N    B LEU   A 1 169 ? 7.633  -17.728 -1.565  0.40 30.66 ?  169 LEU   A N    1 
ATOM   3812 C CA   A LEU   A 1 169 ? 7.004  -19.189 -0.404  0.60 22.19 ?  169 LEU   A CA   1 
ATOM   3813 C CA   B LEU   A 1 169 ? 7.469  -19.108 -1.983  0.40 31.41 ?  169 LEU   A CA   1 
ATOM   3814 C C    A LEU   A 1 169 ? 7.845  -19.942 0.614   0.60 22.12 ?  169 LEU   A C    1 
ATOM   3815 C C    B LEU   A 1 169 ? 8.348  -20.041 -1.154  0.40 31.97 ?  169 LEU   A C    1 
ATOM   3816 O O    A LEU   A 1 169 ? 7.293  -20.464 1.582   0.60 22.36 ?  169 LEU   A O    1 
ATOM   3817 O O    B LEU   A 1 169 ? 8.250  -21.265 -1.258  0.40 32.22 ?  169 LEU   A O    1 
ATOM   3818 C CB   A LEU   A 1 169 ? 7.336  -19.631 -1.831  0.60 24.34 ?  169 LEU   A CB   1 
ATOM   3819 C CB   B LEU   A 1 169 ? 7.839  -19.256 -3.466  0.40 31.74 ?  169 LEU   A CB   1 
ATOM   3820 C CG   A LEU   A 1 169 ? 6.997  -21.083 -2.186  0.60 26.33 ?  169 LEU   A CG   1 
ATOM   3821 C CG   B LEU   A 1 169 ? 6.956  -20.134 -4.361  0.40 31.93 ?  169 LEU   A CG   1 
ATOM   3822 C CD1  A LEU   A 1 169 ? 5.553  -21.411 -1.835  0.60 26.98 ?  169 LEU   A CD1  1 
ATOM   3823 C CD1  B LEU   A 1 169 ? 5.751  -20.687 -3.611  0.40 31.93 ?  169 LEU   A CD1  1 
ATOM   3824 C CD2  A LEU   A 1 169 ? 7.255  -21.346 -3.663  0.60 26.89 ?  169 LEU   A CD2  1 
ATOM   3825 C CD2  B LEU   A 1 169 ? 6.507  -19.341 -5.582  0.40 31.95 ?  169 LEU   A CD2  1 
ATOM   3826 O OXT  A LEU   A 1 169 ? 9.072  -20.027 0.508   0.60 21.76 -1 169 LEU   A OXT  1 
ATOM   3827 O OXT  B LEU   A 1 169 ? 9.191  -19.598 -0.374  0.40 32.17 -1 169 LEU   A OXT  1 
ATOM   3828 H H    A LEU   A 1 169 ? 7.916  -17.457 -0.618  0.60 23.14 ?  169 LEU   A H    1 
ATOM   3829 H H    B LEU   A 1 169 ? 8.371  -17.376 -1.817  0.40 36.79 ?  169 LEU   A H    1 
ATOM   3830 H HA   A LEU   A 1 169 ? 6.072  -19.395 -0.230  0.60 26.62 ?  169 LEU   A HA   1 
ATOM   3831 H HA   B LEU   A 1 169 ? 6.536  -19.332 -1.839  0.40 37.68 ?  169 LEU   A HA   1 
ATOM   3832 H HB2  A LEU   A 1 169 ? 6.845  -19.064 -2.444  0.60 29.20 ?  169 LEU   A HB2  1 
ATOM   3833 H HB2  B LEU   A 1 169 ? 7.853  -18.373 -3.864  0.40 38.09 ?  169 LEU   A HB2  1 
ATOM   3834 H HB3  A LEU   A 1 169 ? 8.286  -19.517 -1.972  0.60 29.20 ?  169 LEU   A HB3  1 
ATOM   3835 H HB3  B LEU   A 1 169 ? 8.736  -19.632 -3.509  0.40 38.09 ?  169 LEU   A HB3  1 
ATOM   3836 H HG   A LEU   A 1 169 ? 7.569  -21.677 -1.676  0.60 31.59 ?  169 LEU   A HG   1 
ATOM   3837 H HG   B LEU   A 1 169 ? 7.480  -20.887 -4.677  0.40 38.31 ?  169 LEU   A HG   1 
ATOM   3838 H HD11 A LEU   A 1 169 ? 5.310  -22.254 -2.249  0.60 32.37 ?  169 LEU   A HD11 1 
ATOM   3839 H HD11 B LEU   A 1 169 ? 5.260  -21.265 -4.200  0.40 38.31 ?  169 LEU   A HD11 1 
ATOM   3840 H HD12 A LEU   A 1 169 ? 5.469  -21.481 -0.871  0.60 32.37 ?  169 LEU   A HD12 1 
ATOM   3841 H HD12 B LEU   A 1 169 ? 6.061  -21.189 -2.837  0.40 38.31 ?  169 LEU   A HD12 1 
ATOM   3842 H HD13 A LEU   A 1 169 ? 4.978  -20.703 -2.168  0.60 32.37 ?  169 LEU   A HD13 1 
ATOM   3843 H HD13 B LEU   A 1 169 ? 5.187  -19.947 -3.327  0.40 38.31 ?  169 LEU   A HD13 1 
ATOM   3844 H HD21 A LEU   A 1 169 ? 7.040  -22.271 -3.863  0.60 32.26 ?  169 LEU   A HD21 1 
ATOM   3845 H HD21 B LEU   A 1 169 ? 5.958  -19.911 -6.143  0.40 38.34 ?  169 LEU   A HD21 1 
ATOM   3846 H HD22 A LEU   A 1 169 ? 6.695  -20.755 -4.192  0.60 32.26 ?  169 LEU   A HD22 1 
ATOM   3847 H HD22 B LEU   A 1 169 ? 5.993  -18.573 -5.288  0.40 38.34 ?  169 LEU   A HD22 1 
ATOM   3848 H HD23 A LEU   A 1 169 ? 8.190  -21.174 -3.855  0.60 32.26 ?  169 LEU   A HD23 1 
ATOM   3849 H HD23 B LEU   A 1 169 ? 7.289  -19.047 -6.075  0.40 38.34 ?  169 LEU   A HD23 1 
ATOM   3850 N N    A SER   B 1 1   ? 50.792 -9.223  -23.727 0.60 29.30 ?  1   SER   B N    1 
ATOM   3851 N N    B SER   B 1 1   ? 50.695 -9.276  -23.692 0.40 27.43 ?  1   SER   B N    1 
ATOM   3852 C CA   A SER   B 1 1   ? 51.288 -10.283 -22.827 0.60 29.45 ?  1   SER   B CA   1 
ATOM   3853 C CA   B SER   B 1 1   ? 51.174 -10.285 -22.724 0.40 27.40 ?  1   SER   B CA   1 
ATOM   3854 C C    A SER   B 1 1   ? 50.220 -11.338 -22.585 0.60 28.38 ?  1   SER   B C    1 
ATOM   3855 C C    B SER   B 1 1   ? 50.108 -11.348 -22.482 0.40 26.54 ?  1   SER   B C    1 
ATOM   3856 O O    A SER   B 1 1   ? 49.029 -11.132 -22.849 0.60 28.43 ?  1   SER   B O    1 
ATOM   3857 O O    B SER   B 1 1   ? 48.933 -11.172 -22.825 0.40 26.12 ?  1   SER   B O    1 
ATOM   3858 C CB   A SER   B 1 1   ? 51.744 -9.692  -21.495 0.60 30.09 ?  1   SER   B CB   1 
ATOM   3859 C CB   B SER   B 1 1   ? 51.552 -9.625  -21.402 0.40 27.81 ?  1   SER   B CB   1 
ATOM   3860 O OG   A SER   B 1 1   ? 50.633 -9.335  -20.696 0.60 31.53 ?  1   SER   B OG   1 
ATOM   3861 O OG   B SER   B 1 1   ? 50.422 -9.514  -20.558 0.40 28.81 ?  1   SER   B OG   1 
ATOM   3862 H H1   A SER   B 1 1   ? 50.718 -9.554  -24.547 0.60 35.15 ?  1   SER   B H1   1 
ATOM   3863 H H1   B SER   B 1 1   ? 51.397 -8.885  -24.073 0.40 32.91 ?  1   SER   B H1   1 
ATOM   3864 H H2   A SER   B 1 1   ? 50.002 -8.945  -23.438 0.60 35.15 ?  1   SER   B H2   1 
ATOM   3865 H H2   B SER   B 1 1   ? 50.202 -9.679  -24.310 0.40 32.91 ?  1   SER   B H2   1 
ATOM   3866 H H3   A SER   B 1 1   ? 51.372 -8.551  -23.723 0.60 35.15 ?  1   SER   B H3   1 
ATOM   3867 H H3   B SER   B 1 1   ? 50.210 -8.671  -23.263 0.40 32.91 ?  1   SER   B H3   1 
ATOM   3868 H HA   A SER   B 1 1   ? 52.047 -10.707 -23.248 0.60 35.33 ?  1   SER   B HA   1 
ATOM   3869 H HA   B SER   B 1 1   ? 51.962 -10.707 -23.095 0.40 32.87 ?  1   SER   B HA   1 
ATOM   3870 H HB2  A SER   B 1 1   ? 52.274 -10.356 -21.029 0.60 36.10 ?  1   SER   B HB2  1 
ATOM   3871 H HB2  B SER   B 1 1   ? 52.226 -10.168 -20.968 0.40 33.37 ?  1   SER   B HB2  1 
ATOM   3872 H HB3  A SER   B 1 1   ? 52.275 -8.900  -21.665 0.60 36.10 ?  1   SER   B HB3  1 
ATOM   3873 H HB3  B SER   B 1 1   ? 51.903 -8.737  -21.578 0.40 33.37 ?  1   SER   B HB3  1 
ATOM   3874 H HG   A SER   B 1 1   ? 50.894 -8.890  -20.032 0.60 37.83 ?  1   SER   B HG   1 
ATOM   3875 H HG   B SER   B 1 1   ? 50.549 -8.905  -19.994 0.40 34.57 ?  1   SER   B HG   1 
ATOM   3876 N N    A MET   B 1 2   ? 50.669 -12.471 -22.064 0.60 27.31 ?  2   MET   B N    1 
ATOM   3877 N N    B MET   B 1 2   ? 50.531 -12.447 -21.873 0.40 26.19 ?  2   MET   B N    1 
ATOM   3878 C CA   A MET   B 1 2   ? 49.840 -13.651 -21.879 0.60 26.98 ?  2   MET   B CA   1 
ATOM   3879 C CA   B MET   B 1 2   ? 49.710 -13.645 -21.724 0.40 26.00 ?  2   MET   B CA   1 
ATOM   3880 C C    A MET   B 1 2   ? 49.600 -13.833 -20.388 0.60 23.91 ?  2   MET   B C    1 
ATOM   3881 C C    B MET   B 1 2   ? 49.435 -13.884 -20.244 0.40 24.14 ?  2   MET   B C    1 
ATOM   3882 O O    A MET   B 1 2   ? 50.548 -14.028 -19.622 0.60 23.57 ?  2   MET   B O    1 
ATOM   3883 O O    B MET   B 1 2   ? 50.284 -14.417 -19.523 0.40 24.53 ?  2   MET   B O    1 
ATOM   3884 C CB   A MET   B 1 2   ? 50.551 -14.865 -22.468 0.60 30.73 ?  2   MET   B CB   1 
ATOM   3885 C CB   B MET   B 1 2   ? 50.451 -14.823 -22.331 0.40 28.17 ?  2   MET   B CB   1 
ATOM   3886 C CG   A MET   B 1 2   ? 49.688 -16.107 -22.598 0.60 34.06 ?  2   MET   B CG   1 
ATOM   3887 C CG   B MET   B 1 2   ? 49.570 -15.979 -22.774 0.40 29.93 ?  2   MET   B CG   1 
ATOM   3888 S SD   A MET   B 1 2   ? 50.510 -17.361 -23.598 0.60 37.19 ?  2   MET   B SD   1 
ATOM   3889 S SD   B MET   B 1 2   ? 50.453 -17.070 -23.896 0.40 31.58 ?  2   MET   B SD   1 
ATOM   3890 C CE   A MET   B 1 2   ? 51.023 -16.352 -24.985 0.60 37.58 ?  2   MET   B CE   1 
ATOM   3891 C CE   B MET   B 1 2   ? 51.362 -15.866 -24.848 0.40 31.91 ?  2   MET   B CE   1 
ATOM   3892 H H    A MET   B 1 2   ? 51.480 -12.587 -21.795 0.60 32.76 ?  2   MET   B H    1 
ATOM   3893 H H    B MET   B 1 2   ? 51.323 -12.531 -21.546 0.40 31.42 ?  2   MET   B H    1 
ATOM   3894 H HA   A MET   B 1 2   ? 48.996 -13.546 -22.340 0.60 32.37 ?  2   MET   B HA   1 
ATOM   3895 H HA   B MET   B 1 2   ? 48.878 -13.533 -22.209 0.40 31.20 ?  2   MET   B HA   1 
ATOM   3896 H HB2  A MET   B 1 2   ? 50.864 -14.602 -23.345 0.60 36.87 ?  2   MET   B HB2  1 
ATOM   3897 H HB2  B MET   B 1 2   ? 50.935 -14.456 -23.079 0.40 33.80 ?  2   MET   B HB2  1 
ATOM   3898 H HB3  A MET   B 1 2   ? 51.306 -15.103 -21.913 0.60 36.87 ?  2   MET   B HB3  1 
ATOM   3899 H HB3  B MET   B 1 2   ? 51.078 -15.186 -21.693 0.40 33.80 ?  2   MET   B HB3  1 
ATOM   3900 H HG2  A MET   B 1 2   ? 49.525 -16.477 -21.713 0.60 40.87 ?  2   MET   B HG2  1 
ATOM   3901 H HG2  B MET   B 1 2   ? 49.302 -16.496 -21.993 0.40 35.91 ?  2   MET   B HG2  1 
ATOM   3902 H HG3  A MET   B 1 2   ? 48.849 -15.881 -23.029 0.60 40.87 ?  2   MET   B HG3  1 
ATOM   3903 H HG3  B MET   B 1 2   ? 48.788 -15.647 -23.235 0.40 35.91 ?  2   MET   B HG3  1 
ATOM   3904 H HE1  A MET   B 1 2   ? 51.157 -16.920 -25.747 0.60 45.09 ?  2   MET   B HE1  1 
ATOM   3905 H HE1  B MET   B 1 2   ? 51.609 -16.285 -25.661 0.40 38.29 ?  2   MET   B HE1  1 
ATOM   3906 H HE2  A MET   B 1 2   ? 50.323 -15.700 -25.168 0.60 45.09 ?  2   MET   B HE2  1 
ATOM   3907 H HE2  B MET   B 1 2   ? 50.789 -15.098 -25.030 0.40 38.29 ?  2   MET   B HE2  1 
ATOM   3908 H HE3  A MET   B 1 2   ? 51.850 -15.888 -24.761 0.60 45.09 ?  2   MET   B HE3  1 
ATOM   3909 H HE3  B MET   B 1 2   ? 52.156 -15.584 -24.353 0.40 38.29 ?  2   MET   B HE3  1 
ATOM   3910 N N    A VAL   B 1 3   ? 48.338 -13.737 -19.980 0.60 21.17 ?  3   VAL   B N    1 
ATOM   3911 N N    B VAL   B 1 3   ? 48.244 -13.502 -19.800 0.40 21.96 ?  3   VAL   B N    1 
ATOM   3912 C CA   A VAL   B 1 3   ? 47.931 -13.978 -18.604 0.60 20.03 ?  3   VAL   B CA   1 
ATOM   3913 C CA   B VAL   B 1 3   ? 47.801 -13.762 -18.438 0.40 20.48 ?  3   VAL   B CA   1 
ATOM   3914 C C    A VAL   B 1 3   ? 46.694 -14.864 -18.624 0.60 18.42 ?  3   VAL   B C    1 
ATOM   3915 C C    B VAL   B 1 3   ? 46.551 -14.627 -18.483 0.40 18.67 ?  3   VAL   B C    1 
ATOM   3916 O O    A VAL   B 1 3   ? 46.000 -14.981 -19.636 0.60 18.53 ?  3   VAL   B O    1 
ATOM   3917 O O    B VAL   B 1 3   ? 45.723 -14.516 -19.392 0.40 18.59 ?  3   VAL   B O    1 
ATOM   3918 C CB   A VAL   B 1 3   ? 47.649 -12.667 -17.836 0.60 21.52 ?  3   VAL   B CB   1 
ATOM   3919 C CB   B VAL   B 1 3   ? 47.539 -12.471 -17.630 0.40 21.14 ?  3   VAL   B CB   1 
ATOM   3920 C CG1  A VAL   B 1 3   ? 48.915 -11.810 -17.743 0.60 22.00 ?  3   VAL   B CG1  1 
ATOM   3921 C CG1  B VAL   B 1 3   ? 48.813 -11.644 -17.510 0.40 21.33 ?  3   VAL   B CG1  1 
ATOM   3922 C CG2  A VAL   B 1 3   ? 46.518 -11.895 -18.499 0.60 21.95 ?  3   VAL   B CG2  1 
ATOM   3923 C CG2  B VAL   B 1 3   ? 46.418 -11.663 -18.262 0.40 21.27 ?  3   VAL   B CG2  1 
ATOM   3924 H H    A VAL   B 1 3   ? 47.685 -13.528 -20.499 0.60 25.40 ?  3   VAL   B H    1 
ATOM   3925 H H    B VAL   B 1 3   ? 47.666 -13.092 -20.288 0.40 26.34 ?  3   VAL   B H    1 
ATOM   3926 H HA   A VAL   B 1 3   ? 48.640 -14.456 -18.141 0.60 24.03 ?  3   VAL   B HA   1 
ATOM   3927 H HA   B VAL   B 1 3   ? 48.490 -14.263 -17.980 0.40 24.57 ?  3   VAL   B HA   1 
ATOM   3928 H HB   A VAL   B 1 3   ? 47.374 -12.889 -16.932 0.60 25.82 ?  3   VAL   B HB   1 
ATOM   3929 H HB   B VAL   B 1 3   ? 47.262 -12.720 -16.736 0.40 25.37 ?  3   VAL   B HB   1 
ATOM   3930 H HG11 A VAL   B 1 3   ? 48.709 -11.003 -17.247 0.60 26.39 ?  3   VAL   B HG11 1 
ATOM   3931 H HG11 B VAL   B 1 3   ? 48.623 -10.851 -16.985 0.40 25.59 ?  3   VAL   B HG11 1 
ATOM   3932 H HG12 A VAL   B 1 3   ? 49.604 -12.316 -17.285 0.60 26.39 ?  3   VAL   B HG12 1 
ATOM   3933 H HG12 B VAL   B 1 3   ? 49.494 -12.177 -17.071 0.40 25.59 ?  3   VAL   B HG12 1 
ATOM   3934 H HG13 A VAL   B 1 3   ? 49.207 -11.586 -18.639 0.60 26.39 ?  3   VAL   B HG13 1 
ATOM   3935 H HG13 B VAL   B 1 3   ? 49.109 -11.392 -18.398 0.40 25.59 ?  3   VAL   B HG13 1 
ATOM   3936 H HG21 A VAL   B 1 3   ? 46.456 -11.019 -18.090 0.60 26.33 ?  3   VAL   B HG21 1 
ATOM   3937 H HG21 B VAL   B 1 3   ? 46.377 -10.797 -17.832 0.40 25.52 ?  3   VAL   B HG21 1 
ATOM   3938 H HG22 A VAL   B 1 3   ? 46.708 -11.807 -19.445 0.60 26.33 ?  3   VAL   B HG22 1 
ATOM   3939 H HG22 B VAL   B 1 3   ? 46.598 -11.559 -19.208 0.40 25.52 ?  3   VAL   B HG22 1 
ATOM   3940 H HG23 A VAL   B 1 3   ? 45.687 -12.380 -18.371 0.60 26.33 ?  3   VAL   B HG23 1 
ATOM   3941 H HG23 B VAL   B 1 3   ? 45.579 -12.135 -18.135 0.40 25.52 ?  3   VAL   B HG23 1 
ATOM   3942 N N    . ASN   B 1 4   ? 46.421 -15.491 -17.481 1.00 17.30 ?  4   ASN   B N    1 
ATOM   3943 C CA   . ASN   B 1 4   ? 45.281 -16.398 -17.358 1.00 16.55 ?  4   ASN   B CA   1 
ATOM   3944 C C    . ASN   B 1 4   ? 45.220 -17.368 -18.535 1.00 17.17 ?  4   ASN   B C    1 
ATOM   3945 O O    . ASN   B 1 4   ? 44.157 -17.622 -19.095 1.00 17.62 ?  4   ASN   B O    1 
ATOM   3946 C CB   . ASN   B 1 4   ? 43.962 -15.635 -17.195 1.00 15.86 ?  4   ASN   B CB   1 
ATOM   3947 C CG   . ASN   B 1 4   ? 43.922 -14.823 -15.916 1.00 15.25 ?  4   ASN   B CG   1 
ATOM   3948 O OD1  . ASN   B 1 4   ? 44.215 -15.329 -14.837 1.00 14.68 ?  4   ASN   B OD1  1 
ATOM   3949 N ND2  . ASN   B 1 4   ? 43.582 -13.545 -16.037 1.00 16.17 ?  4   ASN   B ND2  1 
ATOM   3950 H H    A ASN   B 1 4   ? 46.882 -15.409 -16.762 0.60 20.75 ?  4   ASN   B H    1 
ATOM   3951 H H    B ASN   B 1 4   ? 46.995 -15.575 -16.848 0.40 20.75 ?  4   ASN   B H    1 
ATOM   3952 H HA   . ASN   B 1 4   ? 45.406 -16.928 -16.557 1.00 19.85 ?  4   ASN   B HA   1 
ATOM   3953 H HB2  . ASN   B 1 4   ? 43.846 -15.028 -17.943 1.00 19.02 ?  4   ASN   B HB2  1 
ATOM   3954 H HB3  . ASN   B 1 4   ? 43.229 -16.273 -17.172 1.00 19.02 ?  4   ASN   B HB3  1 
ATOM   3955 H HD21 . ASN   B 1 4   ? 43.548 -13.040 -15.338 1.00 19.39 ?  4   ASN   B HD21 1 
ATOM   3956 H HD22 . ASN   B 1 4   ? 43.388 -13.216 -16.808 1.00 19.39 ?  4   ASN   B HD22 1 
ATOM   3957 N N    . SER   B 1 5   ? 46.378 -17.912 -18.916 1.00 18.28 ?  5   SER   B N    1 
ATOM   3958 C CA   . SER   B 1 5   ? 46.476 -18.832 -20.049 1.00 21.02 ?  5   SER   B CA   1 
ATOM   3959 C C    . SER   B 1 5   ? 46.470 -20.250 -19.492 1.00 22.39 ?  5   SER   B C    1 
ATOM   3960 O O    . SER   B 1 5   ? 47.500 -20.915 -19.391 1.00 23.96 ?  5   SER   B O    1 
ATOM   3961 C CB   . SER   B 1 5   ? 47.731 -18.550 -20.870 1.00 23.07 ?  5   SER   B CB   1 
ATOM   3962 O OG   . SER   B 1 5   ? 48.907 -18.776 -20.110 1.00 25.76 ?  5   SER   B OG   1 
ATOM   3963 H H    . SER   B 1 5   ? 47.133 -17.763 -18.529 1.00 21.93 ?  5   SER   B H    1 
ATOM   3964 H HA   . SER   B 1 5   ? 45.705 -18.725 -20.625 1.00 25.22 ?  5   SER   B HA   1 
ATOM   3965 H HB2  . SER   B 1 5   ? 47.738 -19.130 -21.650 1.00 27.68 ?  5   SER   B HB2  1 
ATOM   3966 H HB3  . SER   B 1 5   ? 47.706 -17.623 -21.152 1.00 27.68 ?  5   SER   B HB3  1 
ATOM   3967 H HG   . SER   B 1 5   ? 48.958 -19.588 -19.897 1.00 30.91 ?  5   SER   B HG   1 
ATOM   3968 N N    . PHE   B 1 6   ? 45.280 -20.702 -19.108 1.00 22.81 ?  6   PHE   B N    1 
ATOM   3969 C CA   . PHE   B 1 6   ? 45.102 -22.042 -18.571 1.00 22.32 ?  6   PHE   B CA   1 
ATOM   3970 C C    . PHE   B 1 6   ? 45.041 -23.038 -19.721 1.00 25.94 ?  6   PHE   B C    1 
ATOM   3971 O O    . PHE   B 1 6   ? 44.362 -22.796 -20.722 1.00 27.94 ?  6   PHE   B O    1 
ATOM   3972 C CB   . PHE   B 1 6   ? 43.815 -22.103 -17.749 1.00 19.91 ?  6   PHE   B CB   1 
ATOM   3973 C CG   . PHE   B 1 6   ? 43.833 -21.229 -16.524 1.00 17.75 ?  6   PHE   B CG   1 
ATOM   3974 C CD1  . PHE   B 1 6   ? 44.354 -21.700 -15.334 1.00 16.76 ?  6   PHE   B CD1  1 
ATOM   3975 C CD2  . PHE   B 1 6   ? 43.334 -19.934 -16.567 1.00 17.08 ?  6   PHE   B CD2  1 
ATOM   3976 C CE1  . PHE   B 1 6   ? 44.362 -20.904 -14.200 1.00 16.46 ?  6   PHE   B CE1  1 
ATOM   3977 C CE2  . PHE   B 1 6   ? 43.352 -19.129 -15.445 1.00 17.45 ?  6   PHE   B CE2  1 
ATOM   3978 C CZ   . PHE   B 1 6   ? 43.871 -19.606 -14.263 1.00 16.87 ?  6   PHE   B CZ   1 
ATOM   3979 H H    . PHE   B 1 6   ? 44.550 -20.248 -19.158 1.00 27.36 ?  6   PHE   B H    1 
ATOM   3980 H HA   . PHE   B 1 6   ? 45.849 -22.273 -18.001 1.00 26.78 ?  6   PHE   B HA   1 
ATOM   3981 H HB2  . PHE   B 1 6   ? 43.072 -21.820 -18.305 1.00 23.88 ?  6   PHE   B HB2  1 
ATOM   3982 H HB3  . PHE   B 1 6   ? 43.673 -23.019 -17.456 1.00 23.88 ?  6   PHE   B HB3  1 
ATOM   3983 H HD1  . PHE   B 1 6   ? 44.694 -22.566 -15.289 1.00 20.11 ?  6   PHE   B HD1  1 
ATOM   3984 H HD2  . PHE   B 1 6   ? 42.982 -19.608 -17.362 1.00 20.49 ?  6   PHE   B HD2  1 
ATOM   3985 H HE1  . PHE   B 1 6   ? 44.727 -21.225 -13.405 1.00 19.75 ?  6   PHE   B HE1  1 
ATOM   3986 H HE2  . PHE   B 1 6   ? 43.011 -18.264 -15.488 1.00 20.93 ?  6   PHE   B HE2  1 
ATOM   3987 H HZ   . PHE   B 1 6   ? 43.882 -19.068 -13.505 1.00 20.24 ?  6   PHE   B HZ   1 
ATOM   3988 N N    A SER   B 1 7   ? 45.754 -24.155 -19.580 0.60 26.66 ?  7   SER   B N    1 
ATOM   3989 N N    B SER   B 1 7   ? 45.765 -24.149 -19.579 0.40 26.92 ?  7   SER   B N    1 
ATOM   3990 C CA   A SER   B 1 7   ? 45.828 -25.153 -20.638 0.60 28.16 ?  7   SER   B CA   1 
ATOM   3991 C CA   B SER   B 1 7   ? 45.872 -25.150 -20.630 0.40 28.29 ?  7   SER   B CA   1 
ATOM   3992 C C    A SER   B 1 7   ? 45.790 -26.553 -20.044 0.60 27.10 ?  7   SER   B C    1 
ATOM   3993 C C    B SER   B 1 7   ? 45.811 -26.543 -20.024 0.40 27.57 ?  7   SER   B C    1 
ATOM   3994 O O    A SER   B 1 7   ? 46.389 -26.812 -18.997 0.60 27.41 ?  7   SER   B O    1 
ATOM   3995 O O    B SER   B 1 7   ? 46.383 -26.793 -18.959 0.40 27.78 ?  7   SER   B O    1 
ATOM   3996 C CB   A SER   B 1 7   ? 47.106 -24.976 -21.471 0.60 30.31 ?  7   SER   B CB   1 
ATOM   3997 C CB   B SER   B 1 7   ? 47.187 -24.989 -21.407 0.40 29.96 ?  7   SER   B CB   1 
ATOM   3998 O OG   A SER   B 1 7   ? 47.075 -25.785 -22.633 0.60 32.00 ?  7   SER   B OG   1 
ATOM   3999 O OG   B SER   B 1 7   ? 47.313 -25.980 -22.411 0.40 31.27 ?  7   SER   B OG   1 
ATOM   4000 H H    A SER   B 1 7   ? 46.214 -24.353 -18.879 0.60 31.99 ?  7   SER   B H    1 
ATOM   4001 H H    B SER   B 1 7   ? 46.215 -24.343 -18.872 0.40 32.30 ?  7   SER   B H    1 
ATOM   4002 H HA   A SER   B 1 7   ? 45.068 -25.055 -21.228 0.60 33.78 ?  7   SER   B HA   1 
ATOM   4003 H HA   B SER   B 1 7   ? 45.135 -25.054 -21.250 0.40 33.94 ?  7   SER   B HA   1 
ATOM   4004 H HB2  A SER   B 1 7   ? 47.180 -24.048 -21.744 0.60 36.36 ?  7   SER   B HB2  1 
ATOM   4005 H HB2  B SER   B 1 7   ? 47.200 -24.112 -21.824 0.40 35.95 ?  7   SER   B HB2  1 
ATOM   4006 H HB3  A SER   B 1 7   ? 47.874 -25.223 -20.931 0.60 36.36 ?  7   SER   B HB3  1 
ATOM   4007 H HB3  B SER   B 1 7   ? 47.931 -25.071 -20.790 0.40 35.95 ?  7   SER   B HB3  1 
ATOM   4008 H HG   A SER   B 1 7   ? 47.784 -25.685 -23.074 0.60 38.40 ?  7   SER   B HG   1 
ATOM   4009 H HG   B SER   B 1 7   ? 48.034 -25.876 -22.829 0.40 37.52 ?  7   SER   B HG   1 
ATOM   4010 N N    A GLY   B 1 8   ? 45.080 -27.452 -20.724 0.60 26.64 ?  8   GLY   B N    1 
ATOM   4011 N N    B GLY   B 1 8   ? 45.115 -27.446 -20.711 0.40 27.08 ?  8   GLY   B N    1 
ATOM   4012 C CA   A GLY   B 1 8   ? 45.042 -28.842 -20.322 0.60 25.96 ?  8   GLY   B CA   1 
ATOM   4013 C CA   B GLY   B 1 8   ? 45.065 -28.832 -20.297 0.40 26.31 ?  8   GLY   B CA   1 
ATOM   4014 C C    A GLY   B 1 8   ? 44.071 -29.167 -19.215 0.60 24.99 ?  8   GLY   B C    1 
ATOM   4015 C C    B GLY   B 1 8   ? 44.115 -29.132 -19.164 0.40 25.25 ?  8   GLY   B C    1 
ATOM   4016 O O    A GLY   B 1 8   ? 44.174 -30.244 -18.617 0.60 25.76 ?  8   GLY   B O    1 
ATOM   4017 O O    B GLY   B 1 8   ? 44.284 -30.154 -18.489 0.40 25.95 ?  8   GLY   B O    1 
ATOM   4018 H H    A GLY   B 1 8   ? 44.614 -27.273 -21.423 0.60 31.96 ?  8   GLY   B H    1 
ATOM   4019 H H    B GLY   B 1 8   ? 44.664 -27.275 -21.422 0.40 32.49 ?  8   GLY   B H    1 
ATOM   4020 H HA2  A GLY   B 1 8   ? 44.804 -29.384 -21.089 0.60 31.14 ?  8   GLY   B HA2  1 
ATOM   4021 H HA2  B GLY   B 1 8   ? 44.807 -29.378 -21.056 0.40 31.56 ?  8   GLY   B HA2  1 
ATOM   4022 H HA3  A GLY   B 1 8   ? 45.925 -29.109 -20.027 0.60 31.14 ?  8   GLY   B HA3  1 
ATOM   4023 H HA3  B GLY   B 1 8   ? 45.948 -29.110 -20.014 0.40 31.56 ?  8   GLY   B HA3  1 
ATOM   4024 N N    . TYR   B 1 9   ? 43.113 -28.287 -18.934 1.00 23.83 ?  9   TYR   B N    1 
ATOM   4025 C CA   . TYR   B 1 9   ? 42.145 -28.536 -17.879 1.00 21.21 ?  9   TYR   B CA   1 
ATOM   4026 C C    . TYR   B 1 9   ? 40.956 -29.319 -18.403 1.00 20.61 ?  9   TYR   B C    1 
ATOM   4027 O O    . TYR   B 1 9   ? 40.547 -29.180 -19.559 1.00 22.45 ?  9   TYR   B O    1 
ATOM   4028 C CB   . TYR   B 1 9   ? 41.648 -27.239 -17.247 1.00 20.78 ?  9   TYR   B CB   1 
ATOM   4029 C CG   . TYR   B 1 9   ? 42.666 -26.623 -16.323 1.00 19.83 ?  9   TYR   B CG   1 
ATOM   4030 C CD1  . TYR   B 1 9   ? 43.775 -25.968 -16.833 1.00 20.41 ?  9   TYR   B CD1  1 
ATOM   4031 C CD2  . TYR   B 1 9   ? 42.534 -26.711 -14.945 1.00 18.96 ?  9   TYR   B CD2  1 
ATOM   4032 C CE1  . TYR   B 1 9   ? 44.724 -25.413 -16.001 1.00 20.44 ?  9   TYR   B CE1  1 
ATOM   4033 C CE2  . TYR   B 1 9   ? 43.478 -26.155 -14.100 1.00 19.53 ?  9   TYR   B CE2  1 
ATOM   4034 C CZ   . TYR   B 1 9   ? 44.572 -25.507 -14.638 1.00 20.54 ?  9   TYR   B CZ   1 
ATOM   4035 O OH   . TYR   B 1 9   ? 45.520 -24.957 -13.814 1.00 21.15 ?  9   TYR   B OH   1 
ATOM   4036 H H    A TYR   B 1 9   ? 42.990 -27.547 -19.355 0.60 28.59 ?  9   TYR   B H    1 
ATOM   4037 H H    B TYR   B 1 9   ? 42.965 -27.568 -19.384 0.40 28.59 ?  9   TYR   B H    1 
ATOM   4038 H HA   . TYR   B 1 9   ? 42.557 -29.063 -17.184 1.00 25.44 ?  9   TYR   B HA   1 
ATOM   4039 H HB2  . TYR   B 1 9   ? 41.439 -26.593 -17.941 1.00 24.93 ?  9   TYR   B HB2  1 
ATOM   4040 H HB3  . TYR   B 1 9   ? 40.858 -27.435 -16.724 1.00 24.93 ?  9   TYR   B HB3  1 
ATOM   4041 H HD1  . TYR   B 1 9   ? 43.883 -25.901 -17.754 1.00 24.49 ?  9   TYR   B HD1  1 
ATOM   4042 H HD2  . TYR   B 1 9   ? 41.796 -27.152 -14.583 1.00 22.75 ?  9   TYR   B HD2  1 
ATOM   4043 H HE1  . TYR   B 1 9   ? 45.459 -24.975 -16.358 1.00 24.52 ?  9   TYR   B HE1  1 
ATOM   4044 H HE2  . TYR   B 1 9   ? 43.372 -26.225 -13.176 1.00 23.43 ?  9   TYR   B HE2  1 
ATOM   4045 H HH   . TYR   B 1 9   ? 46.120 -24.595 -14.273 1.00 25.37 ?  9   TYR   B HH   1 
ATOM   4046 N N    . LEU   B 1 10  ? 40.413 -30.157 -17.530 1.00 19.10 ?  10  LEU   B N    1 
ATOM   4047 C CA   . LEU   B 1 10  ? 39.210 -30.920 -17.805 1.00 19.02 ?  10  LEU   B CA   1 
ATOM   4048 C C    . LEU   B 1 10  ? 38.022 -30.151 -17.246 1.00 18.60 ?  10  LEU   B C    1 
ATOM   4049 O O    . LEU   B 1 10  ? 38.037 -29.736 -16.083 1.00 18.15 ?  10  LEU   B O    1 
ATOM   4050 C CB   . LEU   B 1 10  ? 39.318 -32.291 -17.138 1.00 20.17 ?  10  LEU   B CB   1 
ATOM   4051 C CG   . LEU   B 1 10  ? 38.183 -33.253 -17.463 1.00 21.48 ?  10  LEU   B CG   1 
ATOM   4052 C CD1  . LEU   B 1 10  ? 38.307 -33.767 -18.892 1.00 22.86 ?  10  LEU   B CD1  1 
ATOM   4053 C CD2  . LEU   B 1 10  ? 38.147 -34.399 -16.468 1.00 22.57 ?  10  LEU   B CD2  1 
ATOM   4054 H H    . LEU   B 1 10  ? 40.728 -30.299 -16.737 1.00 22.91 ?  10  LEU   B H    1 
ATOM   4055 H HA   . LEU   B 1 10  ? 39.093 -31.035 -18.758 1.00 22.81 ?  10  LEU   B HA   1 
ATOM   4056 H HB2  . LEU   B 1 10  ? 40.147 -32.708 -17.426 1.00 24.20 ?  10  LEU   B HB2  1 
ATOM   4057 H HB3  . LEU   B 1 10  ? 39.333 -32.171 -16.176 1.00 24.20 ?  10  LEU   B HB3  1 
ATOM   4058 H HG   . LEU   B 1 10  ? 37.341 -32.780 -17.394 1.00 25.77 ?  10  LEU   B HG   1 
ATOM   4059 H HD11 . LEU   B 1 10  ? 37.603 -34.412 -19.056 1.00 27.42 ?  10  LEU   B HD11 1 
ATOM   4060 H HD12 . LEU   B 1 10  ? 38.219 -33.017 -19.503 1.00 27.42 ?  10  LEU   B HD12 1 
ATOM   4061 H HD13 . LEU   B 1 10  ? 39.174 -34.185 -19.002 1.00 27.42 ?  10  LEU   B HD13 1 
ATOM   4062 H HD21 . LEU   B 1 10  ? 37.420 -34.994 -16.705 1.00 27.08 ?  10  LEU   B HD21 1 
ATOM   4063 H HD22 . LEU   B 1 10  ? 38.991 -34.870 -16.503 1.00 27.08 ?  10  LEU   B HD22 1 
ATOM   4064 H HD23 . LEU   B 1 10  ? 38.003 -34.034 -15.581 1.00 27.08 ?  10  LEU   B HD23 1 
ATOM   4065 N N    . LYS   B 1 11  ? 37.001 -29.963 -18.073 1.00 20.04 ?  11  LYS   B N    1 
ATOM   4066 C CA   . LYS   B 1 11  ? 35.804 -29.247 -17.660 1.00 22.46 ?  11  LYS   B CA   1 
ATOM   4067 C C    . LYS   B 1 11  ? 34.926 -30.174 -16.826 1.00 21.16 ?  11  LYS   B C    1 
ATOM   4068 O O    . LYS   B 1 11  ? 34.559 -31.264 -17.280 1.00 22.68 ?  11  LYS   B O    1 
ATOM   4069 C CB   . LYS   B 1 11  ? 35.059 -28.771 -18.907 1.00 26.75 ?  11  LYS   B CB   1 
ATOM   4070 C CG   . LYS   B 1 11  ? 33.907 -27.816 -18.654 1.00 30.64 ?  11  LYS   B CG   1 
ATOM   4071 C CD   . LYS   B 1 11  ? 33.153 -27.538 -19.951 1.00 33.77 ?  11  LYS   B CD   1 
ATOM   4072 C CE   . LYS   B 1 11  ? 32.136 -26.423 -19.788 1.00 36.00 ?  11  LYS   B CE   1 
ATOM   4073 N NZ   . LYS   B 1 11  ? 32.789 -25.097 -19.628 1.00 37.20 ?  11  LYS   B NZ   1 
ATOM   4074 H H    . LYS   B 1 11  ? 36.971 -30.252 -18.883 1.00 24.04 ?  11  LYS   B H    1 
ATOM   4075 H HA   . LYS   B 1 11  ? 36.045 -28.477 -17.125 1.00 26.95 ?  11  LYS   B HA   1 
ATOM   4076 H HB2  . LYS   B 1 11  ? 35.691 -28.314 -19.486 1.00 32.09 ?  11  LYS   B HB2  1 
ATOM   4077 H HB3  . LYS   B 1 11  ? 34.699 -29.544 -19.368 1.00 32.09 ?  11  LYS   B HB3  1 
ATOM   4078 H HG2  . LYS   B 1 11  ? 33.289 -28.214 -18.022 1.00 36.76 ?  11  LYS   B HG2  1 
ATOM   4079 H HG3  . LYS   B 1 11  ? 34.250 -26.976 -18.314 1.00 36.76 ?  11  LYS   B HG3  1 
ATOM   4080 H HD2  . LYS   B 1 11  ? 33.787 -27.272 -20.636 1.00 40.51 ?  11  LYS   B HD2  1 
ATOM   4081 H HD3  . LYS   B 1 11  ? 32.683 -28.341 -20.225 1.00 40.51 ?  11  LYS   B HD3  1 
ATOM   4082 H HE2  . LYS   B 1 11  ? 31.570 -26.390 -20.576 1.00 43.19 ?  11  LYS   B HE2  1 
ATOM   4083 H HE3  . LYS   B 1 11  ? 31.600 -26.600 -18.999 1.00 43.19 ?  11  LYS   B HE3  1 
ATOM   4084 H HZ1  . LYS   B 1 11  ? 32.171 -24.462 -19.543 1.00 44.63 ?  11  LYS   B HZ1  1 
ATOM   4085 H HZ2  . LYS   B 1 11  ? 33.306 -25.098 -18.904 1.00 44.63 ?  11  LYS   B HZ2  1 
ATOM   4086 H HZ3  . LYS   B 1 11  ? 33.291 -24.918 -20.342 1.00 44.63 ?  11  LYS   B HZ3  1 
ATOM   4087 N N    . LEU   B 1 12  ? 34.595 -29.749 -15.605 1.00 19.18 ?  12  LEU   B N    1 
ATOM   4088 C CA   . LEU   B 1 12  ? 33.639 -30.458 -14.760 1.00 18.37 ?  12  LEU   B CA   1 
ATOM   4089 C C    . LEU   B 1 12  ? 32.248 -29.855 -14.851 1.00 18.17 ?  12  LEU   B C    1 
ATOM   4090 O O    . LEU   B 1 12  ? 31.263 -30.573 -15.027 1.00 18.61 ?  12  LEU   B O    1 
ATOM   4091 C CB   . LEU   B 1 12  ? 34.096 -30.463 -13.297 1.00 17.56 ?  12  LEU   B CB   1 
ATOM   4092 C CG   . LEU   B 1 12  ? 35.432 -31.147 -13.013 1.00 17.37 ?  12  LEU   B CG   1 
ATOM   4093 C CD1  . LEU   B 1 12  ? 35.769 -31.089 -11.532 1.00 17.55 ?  12  LEU   B CD1  1 
ATOM   4094 C CD2  . LEU   B 1 12  ? 35.424 -32.586 -13.508 1.00 17.86 ?  12  LEU   B CD2  1 
ATOM   4095 H H    . LEU   B 1 12  ? 34.909 -29.038 -15.240 1.00 23.01 ?  12  LEU   B H    1 
ATOM   4096 H HA   . LEU   B 1 12  ? 33.571 -31.377 -15.061 1.00 22.04 ?  12  LEU   B HA   1 
ATOM   4097 H HB2  . LEU   B 1 12  ? 34.168 -29.546 -12.997 1.00 21.06 ?  12  LEU   B HB2  1 
ATOM   4098 H HB3  . LEU   B 1 12  ? 33.418 -30.921 -12.769 1.00 21.06 ?  12  LEU   B HB3  1 
ATOM   4099 H HG   . LEU   B 1 12  ? 36.125 -30.673 -13.493 1.00 20.83 ?  12  LEU   B HG   1 
ATOM   4100 H HD11 . LEU   B 1 12  ? 36.625 -31.527 -11.387 1.00 21.06 ?  12  LEU   B HD11 1 
ATOM   4101 H HD12 . LEU   B 1 12  ? 35.824 -30.162 -11.254 1.00 21.06 ?  12  LEU   B HD12 1 
ATOM   4102 H HD13 . LEU   B 1 12  ? 35.077 -31.546 -11.028 1.00 21.06 ?  12  LEU   B HD13 1 
ATOM   4103 H HD21 . LEU   B 1 12  ? 36.217 -33.035 -13.183 1.00 21.43 ?  12  LEU   B HD21 1 
ATOM   4104 H HD22 . LEU   B 1 12  ? 34.629 -33.032 -13.170 1.00 21.43 ?  12  LEU   B HD22 1 
ATOM   4105 H HD23 . LEU   B 1 12  ? 35.413 -32.587 -14.478 1.00 21.43 ?  12  LEU   B HD23 1 
ATOM   4106 N N    . THR   B 1 13  ? 32.156 -28.540 -14.723 1.00 18.24 ?  13  THR   B N    1 
ATOM   4107 C CA   . THR   B 1 13  ? 30.933 -27.793 -14.938 1.00 18.27 ?  13  THR   B CA   1 
ATOM   4108 C C    . THR   B 1 13  ? 31.273 -26.599 -15.822 1.00 20.13 ?  13  THR   B C    1 
ATOM   4109 O O    . THR   B 1 13  ? 32.418 -26.413 -16.248 1.00 21.03 ?  13  THR   B O    1 
ATOM   4110 C CB   . THR   B 1 13  ? 30.331 -27.310 -13.614 1.00 18.03 ?  13  THR   B CB   1 
ATOM   4111 O OG1  . THR   B 1 13  ? 31.173 -26.286 -13.067 1.00 17.93 ?  13  THR   B OG1  1 
ATOM   4112 C CG2  . THR   B 1 13  ? 30.208 -28.460 -12.621 1.00 18.68 ?  13  THR   B CG2  1 
ATOM   4113 H H    . THR   B 1 13  ? 32.821 -28.040 -14.503 1.00 21.89 ?  13  THR   B H    1 
ATOM   4114 H HA   . THR   B 1 13  ? 30.282 -28.350 -15.390 1.00 21.92 ?  13  THR   B HA   1 
ATOM   4115 H HB   . THR   B 1 13  ? 29.441 -26.950 -13.774 1.00 21.63 ?  13  THR   B HB   1 
ATOM   4116 H HG1  . THR   B 1 13  ? 30.862 -25.526 -13.263 1.00 21.51 ?  13  THR   B HG1  1 
ATOM   4117 H HG21 . THR   B 1 13  ? 29.683 -28.184 -11.854 1.00 22.41 ?  13  THR   B HG21 1 
ATOM   4118 H HG22 . THR   B 1 13  ? 29.770 -29.217 -13.044 1.00 22.41 ?  13  THR   B HG22 1 
ATOM   4119 H HG23 . THR   B 1 13  ? 31.088 -28.734 -12.320 1.00 22.41 ?  13  THR   B HG23 1 
ATOM   4120 N N    A ASP   B 1 14  ? 30.263 -25.775 -16.091 0.60 21.03 ?  14  ASP   B N    1 
ATOM   4121 N N    B ASP   B 1 14  ? 30.266 -25.766 -16.088 0.40 20.96 ?  14  ASP   B N    1 
ATOM   4122 C CA   A ASP   B 1 14  ? 30.478 -24.615 -16.947 0.60 22.35 ?  14  ASP   B CA   1 
ATOM   4123 C CA   B ASP   B 1 14  ? 30.470 -24.608 -16.951 0.40 21.96 ?  14  ASP   B CA   1 
ATOM   4124 C C    A ASP   B 1 14  ? 31.580 -23.709 -16.411 0.60 20.71 ?  14  ASP   B C    1 
ATOM   4125 C C    B ASP   B 1 14  ? 31.483 -23.620 -16.391 0.40 20.38 ?  14  ASP   B C    1 
ATOM   4126 O O    A ASP   B 1 14  ? 32.267 -23.043 -17.196 0.60 21.88 ?  14  ASP   B O    1 
ATOM   4127 O O    B ASP   B 1 14  ? 31.977 -22.771 -17.143 0.40 21.06 ?  14  ASP   B O    1 
ATOM   4128 C CB   A ASP   B 1 14  ? 29.172 -23.839 -17.119 0.60 25.68 ?  14  ASP   B CB   1 
ATOM   4129 C CB   B ASP   B 1 14  ? 29.149 -23.877 -17.187 0.40 24.72 ?  14  ASP   B CB   1 
ATOM   4130 C CG   A ASP   B 1 14  ? 28.214 -24.510 -18.081 0.60 29.04 ?  14  ASP   B CG   1 
ATOM   4131 C CG   B ASP   B 1 14  ? 28.262 -24.589 -18.189 0.40 27.41 ?  14  ASP   B CG   1 
ATOM   4132 O OD1  A ASP   B 1 14  ? 28.577 -25.544 -18.686 0.60 30.29 ?  14  ASP   B OD1  1 
ATOM   4133 O OD1  B ASP   B 1 14  ? 28.803 -25.195 -19.138 0.40 28.42 ?  14  ASP   B OD1  1 
ATOM   4134 O OD2  A ASP   B 1 14  ? 27.084 -23.998 -18.226 0.60 30.23 -1 14  ASP   B OD2  1 
ATOM   4135 O OD2  B ASP   B 1 14  ? 27.024 -24.548 -18.027 0.40 28.21 -1 14  ASP   B OD2  1 
ATOM   4136 H H    A ASP   B 1 14  ? 29.463 -25.858 -15.787 0.60 25.23 ?  14  ASP   B H    1 
ATOM   4137 H H    B ASP   B 1 14  ? 29.466 -25.851 -15.785 0.40 25.14 ?  14  ASP   B H    1 
ATOM   4138 H HA   A ASP   B 1 14  ? 30.761 -24.916 -17.820 0.60 26.82 ?  14  ASP   B HA   1 
ATOM   4139 H HA   B ASP   B 1 14  ? 30.795 -24.915 -17.811 0.40 26.35 ?  14  ASP   B HA   1 
ATOM   4140 H HB2  A ASP   B 1 14  ? 28.718 -23.781 -16.266 0.60 30.81 ?  14  ASP   B HB2  1 
ATOM   4141 H HB2  B ASP   B 1 14  ? 28.669 -23.816 -16.346 0.40 29.66 ?  14  ASP   B HB2  1 
ATOM   4142 H HB3  A ASP   B 1 14  ? 29.367 -22.952 -17.457 0.60 30.81 ?  14  ASP   B HB3  1 
ATOM   4143 H HB3  B ASP   B 1 14  ? 29.343 -22.983 -17.521 0.40 29.66 ?  14  ASP   B HB3  1 
ATOM   4144 N N    . ASN   B 1 15  ? 31.782 -23.681 -15.090 1.00 18.53 ?  15  ASN   B N    1 
ATOM   4145 C CA   . ASN   B 1 15  ? 32.746 -22.762 -14.488 1.00 16.19 ?  15  ASN   B CA   1 
ATOM   4146 C C    . ASN   B 1 15  ? 33.838 -23.417 -13.653 1.00 15.23 ?  15  ASN   B C    1 
ATOM   4147 O O    . ASN   B 1 15  ? 34.687 -22.693 -13.122 1.00 15.43 ?  15  ASN   B O    1 
ATOM   4148 C CB   . ASN   B 1 15  ? 32.032 -21.708 -13.628 1.00 16.50 ?  15  ASN   B CB   1 
ATOM   4149 C CG   . ASN   B 1 15  ? 31.405 -22.311 -12.393 1.00 16.02 ?  15  ASN   B CG   1 
ATOM   4150 O OD1  . ASN   B 1 15  ? 30.463 -23.108 -12.489 1.00 17.80 ?  15  ASN   B OD1  1 
ATOM   4151 N ND2  . ASN   B 1 15  ? 31.927 -21.966 -11.230 1.00 15.24 ?  15  ASN   B ND2  1 
ATOM   4152 H H    A ASN   B 1 15  ? 31.374 -24.186 -14.523 0.60 22.23 ?  15  ASN   B H    1 
ATOM   4153 H H    B ASN   B 1 15  ? 31.412 -24.221 -14.530 0.40 22.23 ?  15  ASN   B H    1 
ATOM   4154 H HA   . ASN   B 1 15  ? 33.192 -22.280 -15.193 1.00 19.42 ?  15  ASN   B HA   1 
ATOM   4155 H HB2  . ASN   B 1 15  ? 32.679 -21.033 -13.345 1.00 19.79 ?  15  ASN   B HB2  1 
ATOM   4156 H HB3  . ASN   B 1 15  ? 31.330 -21.280 -14.150 1.00 19.79 ?  15  ASN   B HB3  1 
ATOM   4157 H HD21 . ASN   B 1 15  ? 31.599 -22.279 -10.497 1.00 18.28 ?  15  ASN   B HD21 1 
ATOM   4158 H HD22 . ASN   B 1 15  ? 32.593 -21.416 -11.193 1.00 18.28 ?  15  ASN   B HD22 1 
ATOM   4159 N N    . VAL   B 1 16  ? 33.851 -24.742 -13.513 1.00 14.78 ?  16  VAL   B N    1 
ATOM   4160 C CA   . VAL   B 1 16  ? 34.850 -25.436 -12.704 1.00 14.50 ?  16  VAL   B CA   1 
ATOM   4161 C C    . VAL   B 1 16  ? 35.641 -26.376 -13.597 1.00 14.72 ?  16  VAL   B C    1 
ATOM   4162 O O    . VAL   B 1 16  ? 35.062 -27.250 -14.259 1.00 15.82 ?  16  VAL   B O    1 
ATOM   4163 C CB   . VAL   B 1 16  ? 34.218 -26.201 -11.528 1.00 14.86 ?  16  VAL   B CB   1 
ATOM   4164 C CG1  . VAL   B 1 16  ? 35.300 -26.925 -10.730 1.00 14.65 ?  16  VAL   B CG1  1 
ATOM   4165 C CG2  . VAL   B 1 16  ? 33.421 -25.243 -10.638 1.00 15.46 ?  16  VAL   B CG2  1 
ATOM   4166 H H    . VAL   B 1 16  ? 33.272 -25.270 -13.877 1.00 17.73 ?  16  VAL   B H    1 
ATOM   4167 H HA   . VAL   B 1 16  ? 35.462 -24.782 -12.335 1.00 17.39 ?  16  VAL   B HA   1 
ATOM   4168 H HB   . VAL   B 1 16  ? 33.605 -26.866 -11.875 1.00 17.83 ?  16  VAL   B HB   1 
ATOM   4169 H HG11 . VAL   B 1 16  ? 34.921 -27.225 -9.888  1.00 17.57 ?  16  VAL   B HG11 1 
ATOM   4170 H HG12 . VAL   B 1 16  ? 35.614 -27.687 -11.240 1.00 17.57 ?  16  VAL   B HG12 1 
ATOM   4171 H HG13 . VAL   B 1 16  ? 36.032 -26.312 -10.561 1.00 17.57 ?  16  VAL   B HG13 1 
ATOM   4172 H HG21 . VAL   B 1 16  ? 33.084 -25.733 -9.869  1.00 18.54 ?  16  VAL   B HG21 1 
ATOM   4173 H HG22 . VAL   B 1 16  ? 33.997 -24.524 -10.347 1.00 18.54 ?  16  VAL   B HG22 1 
ATOM   4174 H HG23 . VAL   B 1 16  ? 32.675 -24.885 -11.149 1.00 18.54 ?  16  VAL   B HG23 1 
ATOM   4175 N N    . TYR   B 1 17  ? 36.965 -26.218 -13.565 1.00 14.96 ?  17  TYR   B N    1 
ATOM   4176 C CA   . TYR   B 1 17  ? 37.912 -26.963 -14.378 1.00 15.42 ?  17  TYR   B CA   1 
ATOM   4177 C C    . TYR   B 1 17  ? 38.960 -27.571 -13.458 1.00 14.43 ?  17  TYR   B C    1 
ATOM   4178 O O    . TYR   B 1 17  ? 39.221 -27.049 -12.371 1.00 14.82 ?  17  TYR   B O    1 
ATOM   4179 C CB   . TYR   B 1 17  ? 38.614 -26.027 -15.371 1.00 18.29 ?  17  TYR   B CB   1 
ATOM   4180 C CG   . TYR   B 1 17  ? 37.681 -25.263 -16.279 1.00 21.52 ?  17  TYR   B CG   1 
ATOM   4181 C CD1  . TYR   B 1 17  ? 37.098 -24.069 -15.872 1.00 23.22 ?  17  TYR   B CD1  1 
ATOM   4182 C CD2  . TYR   B 1 17  ? 37.385 -25.737 -17.548 1.00 23.83 ?  17  TYR   B CD2  1 
ATOM   4183 C CE1  . TYR   B 1 17  ? 36.241 -23.369 -16.707 1.00 24.90 ?  17  TYR   B CE1  1 
ATOM   4184 C CE2  . TYR   B 1 17  ? 36.533 -25.045 -18.389 1.00 25.51 ?  17  TYR   B CE2  1 
ATOM   4185 C CZ   . TYR   B 1 17  ? 35.964 -23.863 -17.963 1.00 26.18 ?  17  TYR   B CZ   1 
ATOM   4186 O OH   . TYR   B 1 17  ? 35.119 -23.173 -18.799 1.00 27.37 ?  17  TYR   B OH   1 
ATOM   4187 H H    . TYR   B 1 17  ? 37.358 -25.647 -13.047 1.00 17.95 ?  17  TYR   B H    1 
ATOM   4188 H HA   . TYR   B 1 17  ? 37.452 -27.667 -14.864 1.00 18.50 ?  17  TYR   B HA   1 
ATOM   4189 H HB2  . TYR   B 1 17  ? 39.140 -25.381 -14.876 1.00 21.95 ?  17  TYR   B HB2  1 
ATOM   4190 H HB3  . TYR   B 1 17  ? 39.188 -26.558 -15.936 1.00 21.95 ?  17  TYR   B HB3  1 
ATOM   4191 H HD1  . TYR   B 1 17  ? 37.283 -23.734 -15.026 1.00 27.86 ?  17  TYR   B HD1  1 
ATOM   4192 H HD2  . TYR   B 1 17  ? 37.762 -26.533 -17.840 1.00 28.58 ?  17  TYR   B HD2  1 
ATOM   4193 H HE1  . TYR   B 1 17  ? 35.856 -22.569 -16.423 1.00 29.87 ?  17  TYR   B HE1  1 
ATOM   4194 H HE2  . TYR   B 1 17  ? 36.340 -25.377 -19.238 1.00 30.61 ?  17  TYR   B HE2  1 
ATOM   4195 H HH   . TYR   B 1 17  ? 35.032 -23.579 -19.529 1.00 32.83 ?  17  TYR   B HH   1 
ATOM   4196 N N    . ILE   B 1 18  ? 39.575 -28.672 -13.889 1.00 14.60 ?  18  ILE   B N    1 
ATOM   4197 C CA   . ILE   B 1 18  ? 40.500 -29.393 -13.022 1.00 14.91 ?  18  ILE   B CA   1 
ATOM   4198 C C    . ILE   B 1 18  ? 41.660 -29.949 -13.837 1.00 15.17 ?  18  ILE   B C    1 
ATOM   4199 O O    . ILE   B 1 18  ? 41.503 -30.340 -14.998 1.00 16.65 ?  18  ILE   B O    1 
ATOM   4200 C CB   . ILE   B 1 18  ? 39.752 -30.497 -12.228 1.00 15.14 ?  18  ILE   B CB   1 
ATOM   4201 C CG1  . ILE   B 1 18  ? 40.606 -31.034 -11.077 1.00 15.57 ?  18  ILE   B CG1  1 
ATOM   4202 C CG2  . ILE   B 1 18  ? 39.273 -31.624 -13.161 1.00 15.58 ?  18  ILE   B CG2  1 
ATOM   4203 C CD1  . ILE   B 1 18  ? 39.803 -31.854 -10.069 1.00 16.61 ?  18  ILE   B CD1  1 
ATOM   4204 H H    . ILE   B 1 18  ? 39.471 -29.022 -14.666 1.00 17.51 ?  18  ILE   B H    1 
ATOM   4205 H HA   . ILE   B 1 18  ? 40.860 -28.772 -12.369 1.00 17.88 ?  18  ILE   B HA   1 
ATOM   4206 H HB   . ILE   B 1 18  ? 38.961 -30.099 -11.833 1.00 18.16 ?  18  ILE   B HB   1 
ATOM   4207 H HG12 . ILE   B 1 18  ? 41.302 -31.602 -11.435 1.00 18.68 ?  18  ILE   B HG12 1 
ATOM   4208 H HG13 . ILE   B 1 18  ? 40.998 -30.284 -10.602 1.00 18.68 ?  18  ILE   B HG13 1 
ATOM   4209 H HG21 . ILE   B 1 18  ? 38.678 -32.212 -12.668 1.00 18.69 ?  18  ILE   B HG21 1 
ATOM   4210 H HG22 . ILE   B 1 18  ? 38.797 -31.226 -13.908 1.00 18.69 ?  18  ILE   B HG22 1 
ATOM   4211 H HG23 . ILE   B 1 18  ? 40.040 -32.119 -13.481 1.00 18.69 ?  18  ILE   B HG23 1 
ATOM   4212 H HD11 . ILE   B 1 18  ? 40.391 -32.131 -9.347  1.00 19.92 ?  18  ILE   B HD11 1 
ATOM   4213 H HD12 . ILE   B 1 18  ? 39.083 -31.308 -9.716  1.00 19.92 ?  18  ILE   B HD12 1 
ATOM   4214 H HD13 . ILE   B 1 18  ? 39.438 -32.635 -10.514 1.00 19.92 ?  18  ILE   B HD13 1 
ATOM   4215 N N    . LYS   B 1 19  ? 42.837 -29.982 -13.211 1.00 15.44 ?  19  LYS   B N    1 
ATOM   4216 C CA   . LYS   B 1 19  ? 44.047 -30.456 -13.864 1.00 16.02 ?  19  LYS   B CA   1 
ATOM   4217 C C    . LYS   B 1 19  ? 44.943 -31.133 -12.839 1.00 15.95 ?  19  LYS   B C    1 
ATOM   4218 O O    . LYS   B 1 19  ? 45.021 -30.703 -11.687 1.00 15.29 ?  19  LYS   B O    1 
ATOM   4219 C CB   . LYS   B 1 19  ? 44.822 -29.290 -14.493 1.00 17.64 ?  19  LYS   B CB   1 
ATOM   4220 C CG   . LYS   B 1 19  ? 45.998 -29.705 -15.356 1.00 19.51 ?  19  LYS   B CG   1 
ATOM   4221 C CD   . LYS   B 1 19  ? 46.743 -28.476 -15.862 1.00 21.29 ?  19  LYS   B CD   1 
ATOM   4222 C CE   . LYS   B 1 19  ? 47.898 -28.851 -16.771 1.00 23.10 ?  19  LYS   B CE   1 
ATOM   4223 N NZ   . LYS   B 1 19  ? 48.677 -27.662 -17.206 1.00 23.79 ?  19  LYS   B NZ   1 
ATOM   4224 H H    . LYS   B 1 19  ? 42.950 -29.720 -12.398 1.00 18.53 ?  19  LYS   B H    1 
ATOM   4225 H HA   . LYS   B 1 19  ? 43.810 -31.090 -14.559 1.00 19.21 ?  19  LYS   B HA   1 
ATOM   4226 H HB2  . LYS   B 1 19  ? 44.215 -28.782 -15.053 1.00 21.16 ?  19  LYS   B HB2  1 
ATOM   4227 H HB3  . LYS   B 1 19  ? 45.159 -28.723 -13.780 1.00 21.16 ?  19  LYS   B HB3  1 
ATOM   4228 H HG2  . LYS   B 1 19  ? 46.606 -30.247 -14.831 1.00 23.40 ?  19  LYS   B HG2  1 
ATOM   4229 H HG3  . LYS   B 1 19  ? 45.669 -30.209 -16.120 1.00 23.40 ?  19  LYS   B HG3  1 
ATOM   4230 H HD2  . LYS   B 1 19  ? 46.128 -27.917 -16.363 1.00 25.54 ?  19  LYS   B HD2  1 
ATOM   4231 H HD3  . LYS   B 1 19  ? 47.098 -27.988 -15.103 1.00 25.54 ?  19  LYS   B HD3  1 
ATOM   4232 H HE2  . LYS   B 1 19  ? 48.494 -29.450 -16.294 1.00 27.71 ?  19  LYS   B HE2  1 
ATOM   4233 H HE3  . LYS   B 1 19  ? 47.546 -29.293 -17.562 1.00 27.71 ?  19  LYS   B HE3  1 
ATOM   4234 H HZ1  . LYS   B 1 19  ? 49.265 -27.898 -17.831 1.00 28.54 ?  19  LYS   B HZ1  1 
ATOM   4235 H HZ2  . LYS   B 1 19  ? 48.129 -27.047 -17.542 1.00 28.54 ?  19  LYS   B HZ2  1 
ATOM   4236 H HZ3  . LYS   B 1 19  ? 49.112 -27.316 -16.513 1.00 28.54 ?  19  LYS   B HZ3  1 
ATOM   4237 N N    . ASN   B 1 20  ? 45.630 -32.185 -13.269 1.00 17.04 ?  20  ASN   B N    1 
ATOM   4238 C CA   . ASN   B 1 20  ? 46.650 -32.820 -12.439 1.00 18.23 ?  20  ASN   B CA   1 
ATOM   4239 C C    . ASN   B 1 20  ? 47.929 -32.008 -12.619 1.00 18.54 ?  20  ASN   B C    1 
ATOM   4240 O O    . ASN   B 1 20  ? 48.589 -32.093 -13.658 1.00 20.62 ?  20  ASN   B O    1 
ATOM   4241 C CB   . ASN   B 1 20  ? 46.815 -34.278 -12.861 1.00 19.95 ?  20  ASN   B CB   1 
ATOM   4242 C CG   . ASN   B 1 20  ? 47.978 -34.982 -12.175 1.00 21.30 ?  20  ASN   B CG   1 
ATOM   4243 O OD1  . ASN   B 1 20  ? 48.644 -35.832 -12.783 1.00 23.47 ?  20  ASN   B OD1  1 
ATOM   4244 N ND2  . ASN   B 1 20  ? 48.216 -34.662 -10.913 1.00 20.68 ?  20  ASN   B ND2  1 
ATOM   4245 H H    . ASN   B 1 20  ? 45.525 -32.545 -14.041 1.00 20.44 ?  20  ASN   B H    1 
ATOM   4246 H HA   . ASN   B 1 20  ? 46.367 -32.788 -11.509 1.00 21.87 ?  20  ASN   B HA   1 
ATOM   4247 H HB2  . ASN   B 1 20  ? 46.000 -34.761 -12.640 1.00 23.93 ?  20  ASN   B HB2  1 
ATOM   4248 H HB3  . ASN   B 1 20  ? 46.964 -34.308 -13.817 1.00 23.93 ?  20  ASN   B HB3  1 
ATOM   4249 H HD21 . ASN   B 1 20  ? 48.865 -35.031 -10.491 1.00 24.81 ?  20  ASN   B HD21 1 
ATOM   4250 H HD22 . ASN   B 1 20  ? 47.729 -34.069 -10.513 1.00 24.81 ?  20  ASN   B HD22 1 
ATOM   4251 N N    . ALA   B 1 21  ? 48.269 -31.190 -11.620 1.00 17.84 ?  21  ALA   B N    1 
ATOM   4252 C CA   . ALA   B 1 21  ? 49.400 -30.291 -11.771 1.00 18.66 ?  21  ALA   B CA   1 
ATOM   4253 C C    . ALA   B 1 21  ? 49.855 -29.777 -10.415 1.00 17.56 ?  21  ALA   B C    1 
ATOM   4254 O O    . ALA   B 1 21  ? 49.111 -29.803 -9.430  1.00 17.37 ?  21  ALA   B O    1 
ATOM   4255 C CB   . ALA   B 1 21  ? 49.054 -29.131 -12.703 1.00 20.42 ?  21  ALA   B CB   1 
ATOM   4256 H H    . ALA   B 1 21  ? 47.860 -31.141 -10.856 1.00 21.40 ?  21  ALA   B H    1 
ATOM   4257 H HA   . ALA   B 1 21  ? 50.134 -30.789 -12.161 1.00 22.39 ?  21  ALA   B HA   1 
ATOM   4258 H HB1  . ALA   B 1 21  ? 49.855 -28.616 -12.852 1.00 24.49 ?  21  ALA   B HB1  1 
ATOM   4259 H HB2  . ALA   B 1 21  ? 48.730 -29.500 -13.539 1.00 24.49 ?  21  ALA   B HB2  1 
ATOM   4260 H HB3  . ALA   B 1 21  ? 48.367 -28.593 -12.287 1.00 24.49 ?  21  ALA   B HB3  1 
ATOM   4261 N N    . ASP   B 1 22  ? 51.110 -29.327 -10.396 1.00 16.81 ?  22  ASP   B N    1 
ATOM   4262 C CA   . ASP   B 1 22  ? 51.722 -28.629 -9.272  1.00 16.26 ?  22  ASP   B CA   1 
ATOM   4263 C C    . ASP   B 1 22  ? 51.314 -27.160 -9.363  1.00 15.00 ?  22  ASP   B C    1 
ATOM   4264 O O    . ASP   B 1 22  ? 51.622 -26.493 -10.355 1.00 15.31 ?  22  ASP   B O    1 
ATOM   4265 C CB   . ASP   B 1 22  ? 53.239 -28.801 -9.428  1.00 18.07 ?  22  ASP   B CB   1 
ATOM   4266 C CG   . ASP   B 1 22  ? 54.063 -28.047 -8.394  1.00 19.85 ?  22  ASP   B CG   1 
ATOM   4267 O OD1  . ASP   B 1 22  ? 53.706 -26.926 -8.001  1.00 19.75 ?  22  ASP   B OD1  1 
ATOM   4268 O OD2  . ASP   B 1 22  ? 55.127 -28.573 -8.001  1.00 22.00 -1 22  ASP   B OD2  1 
ATOM   4269 H H    . ASP   B 1 22  ? 51.648 -29.421 -11.061 1.00 20.16 ?  22  ASP   B H    1 
ATOM   4270 H HA   . ASP   B 1 22  ? 51.430 -29.009 -8.426  1.00 19.50 ?  22  ASP   B HA   1 
ATOM   4271 H HB2  . ASP   B 1 22  ? 53.461 -29.738 -9.354  1.00 21.67 ?  22  ASP   B HB2  1 
ATOM   4272 H HB3  . ASP   B 1 22  ? 53.500 -28.465 -10.300 1.00 21.67 ?  22  ASP   B HB3  1 
ATOM   4273 N N    . ILE   B 1 23  ? 50.598 -26.666 -8.347  1.00 14.36 ?  23  ILE   B N    1 
ATOM   4274 C CA   . ILE   B 1 23  ? 50.005 -25.329 -8.423  1.00 13.62 ?  23  ILE   B CA   1 
ATOM   4275 C C    . ILE   B 1 23  ? 51.060 -24.241 -8.560  1.00 13.35 ?  23  ILE   B C    1 
ATOM   4276 O O    . ILE   B 1 23  ? 50.796 -23.201 -9.168  1.00 13.15 ?  23  ILE   B O    1 
ATOM   4277 C CB   . ILE   B 1 23  ? 49.065 -25.084 -7.227  1.00 14.05 ?  23  ILE   B CB   1 
ATOM   4278 C CG1  . ILE   B 1 23  ? 48.236 -23.815 -7.435  1.00 14.84 ?  23  ILE   B CG1  1 
ATOM   4279 C CG2  . ILE   B 1 23  ? 49.828 -25.044 -5.920  1.00 15.19 ?  23  ILE   B CG2  1 
ATOM   4280 C CD1  . ILE   B 1 23  ? 47.124 -23.643 -6.416  1.00 15.37 ?  23  ILE   B CD1  1 
ATOM   4281 H H    . ILE   B 1 23  ? 50.443 -27.084 -7.612  1.00 17.22 ?  23  ILE   B H    1 
ATOM   4282 H HA   . ILE   B 1 23  ? 49.458 -25.292 -9.223  1.00 16.34 ?  23  ILE   B HA   1 
ATOM   4283 H HB   . ILE   B 1 23  ? 48.446 -25.830 -7.186  1.00 16.86 ?  23  ILE   B HB   1 
ATOM   4284 H HG12 . ILE   B 1 23  ? 48.825 -23.042 -7.368  1.00 17.80 ?  23  ILE   B HG12 1 
ATOM   4285 H HG13 . ILE   B 1 23  ? 47.834 -23.840 -8.319  1.00 17.80 ?  23  ILE   B HG13 1 
ATOM   4286 H HG21 . ILE   B 1 23  ? 49.196 -25.045 -5.187  1.00 18.22 ?  23  ILE   B HG21 1 
ATOM   4287 H HG22 . ILE   B 1 23  ? 50.399 -25.827 -5.867  1.00 18.22 ?  23  ILE   B HG22 1 
ATOM   4288 H HG23 . ILE   B 1 23  ? 50.368 -24.240 -5.896  1.00 18.22 ?  23  ILE   B HG23 1 
ATOM   4289 H HD11 . ILE   B 1 23  ? 46.591 -22.871 -6.659  1.00 18.44 ?  23  ILE   B HD11 1 
ATOM   4290 H HD12 . ILE   B 1 23  ? 46.573 -24.442 -6.420  1.00 18.44 ?  23  ILE   B HD12 1 
ATOM   4291 H HD13 . ILE   B 1 23  ? 47.516 -23.515 -5.540  1.00 18.44 ?  23  ILE   B HD13 1 
ATOM   4292 N N    . VAL   B 1 24  ? 52.255 -24.447 -8.001  1.00 13.64 ?  24  VAL   B N    1 
ATOM   4293 C CA   . VAL   B 1 24  ? 53.332 -23.473 -8.170  1.00 14.40 ?  24  VAL   B CA   1 
ATOM   4294 C C    . VAL   B 1 24  ? 53.787 -23.433 -9.622  1.00 14.68 ?  24  VAL   B C    1 
ATOM   4295 O O    . VAL   B 1 24  ? 53.930 -22.357 -10.220 1.00 14.94 ?  24  VAL   B O    1 
ATOM   4296 C CB   . VAL   B 1 24  ? 54.506 -23.790 -7.222  1.00 15.25 ?  24  VAL   B CB   1 
ATOM   4297 C CG1  . VAL   B 1 24  ? 55.717 -22.911 -7.548  1.00 16.16 ?  24  VAL   B CG1  1 
ATOM   4298 C CG2  . VAL   B 1 24  ? 54.088 -23.607 -5.783  1.00 16.14 ?  24  VAL   B CG2  1 
ATOM   4299 H H    . VAL   B 1 24  ? 52.464 -25.131 -7.525  1.00 16.36 ?  24  VAL   B H    1 
ATOM   4300 H HA   . VAL   B 1 24  ? 53.001 -22.594 -7.940  1.00 17.27 ?  24  VAL   B HA   1 
ATOM   4301 H HB   . VAL   B 1 24  ? 54.770 -24.717 -7.337  1.00 18.29 ?  24  VAL   B HB   1 
ATOM   4302 H HG11 . VAL   B 1 24  ? 56.305 -22.885 -6.776  1.00 19.39 ?  24  VAL   B HG11 1 
ATOM   4303 H HG12 . VAL   B 1 24  ? 56.186 -23.291 -8.305  1.00 19.39 ?  24  VAL   B HG12 1 
ATOM   4304 H HG13 . VAL   B 1 24  ? 55.409 -22.016 -7.758  1.00 19.39 ?  24  VAL   B HG13 1 
ATOM   4305 H HG21 . VAL   B 1 24  ? 54.818 -23.873 -5.204  1.00 19.36 ?  24  VAL   B HG21 1 
ATOM   4306 H HG22 . VAL   B 1 24  ? 53.871 -22.673 -5.636  1.00 19.36 ?  24  VAL   B HG22 1 
ATOM   4307 H HG23 . VAL   B 1 24  ? 53.309 -24.159 -5.608  1.00 19.36 ?  24  VAL   B HG23 1 
ATOM   4308 N N    . GLU   B 1 25  ? 54.050 -24.606 -10.204 1.00 15.91 ?  25  GLU   B N    1 
ATOM   4309 C CA   . GLU   B 1 25  ? 54.439 -24.640 -11.608 1.00 17.13 ?  25  GLU   B CA   1 
ATOM   4310 C C    . GLU   B 1 25  ? 53.332 -24.090 -12.490 1.00 15.42 ?  25  GLU   B C    1 
ATOM   4311 O O    . GLU   B 1 25  ? 53.599 -23.372 -13.463 1.00 16.41 ?  25  GLU   B O    1 
ATOM   4312 C CB   . GLU   B 1 25  ? 54.827 -26.061 -12.012 1.00 21.08 ?  25  GLU   B CB   1 
ATOM   4313 C CG   . GLU   B 1 25  ? 56.131 -26.510 -11.372 1.00 26.75 ?  25  GLU   B CG   1 
ATOM   4314 C CD   . GLU   B 1 25  ? 57.245 -25.476 -11.483 1.00 31.70 ?  25  GLU   B CD   1 
ATOM   4315 O OE1  . GLU   B 1 25  ? 57.601 -25.103 -12.621 1.00 33.94 ?  25  GLU   B OE1  1 
ATOM   4316 O OE2  . GLU   B 1 25  ? 57.752 -25.018 -10.431 1.00 33.56 -1 25  GLU   B OE2  1 
ATOM   4317 H H    . GLU   B 1 25  ? 54.010 -25.375 -9.817  1.00 19.09 ?  25  GLU   B H    1 
ATOM   4318 H HA   . GLU   B 1 25  ? 55.199 -24.058 -11.733 1.00 20.55 ?  25  GLU   B HA   1 
ATOM   4319 H HB2  . GLU   B 1 25  ? 54.128 -26.675 -11.728 1.00 25.29 ?  25  GLU   B HB2  1 
ATOM   4320 H HB3  . GLU   B 1 25  ? 54.930 -26.101 -12.976 1.00 25.29 ?  25  GLU   B HB3  1 
ATOM   4321 H HG2  . GLU   B 1 25  ? 55.983 -26.671 -10.433 1.00 32.09 ?  25  GLU   B HG2  1 
ATOM   4322 H HG3  . GLU   B 1 25  ? 56.438 -27.313 -11.815 1.00 32.09 ?  25  GLU   B HG3  1 
ATOM   4323 N N    A GLU   B 1 26  ? 52.079 -24.407 -12.161 0.60 14.77 ?  26  GLU   B N    1 
ATOM   4324 N N    B GLU   B 1 26  ? 52.078 -24.411 -12.163 0.40 14.95 ?  26  GLU   B N    1 
ATOM   4325 C CA   A GLU   B 1 26  ? 50.955 -23.879 -12.927 0.60 15.53 ?  26  GLU   B CA   1 
ATOM   4326 C CA   B GLU   B 1 26  ? 50.950 -23.884 -12.923 0.40 15.44 ?  26  GLU   B CA   1 
ATOM   4327 C C    A GLU   B 1 26  ? 50.906 -22.360 -12.851 0.60 14.70 ?  26  GLU   B C    1 
ATOM   4328 C C    B GLU   B 1 26  ? 50.904 -22.364 -12.850 0.40 14.63 ?  26  GLU   B C    1 
ATOM   4329 O O    A GLU   B 1 26  ? 50.712 -21.683 -13.865 0.60 16.07 ?  26  GLU   B O    1 
ATOM   4330 O O    B GLU   B 1 26  ? 50.717 -21.688 -13.867 0.40 15.52 ?  26  GLU   B O    1 
ATOM   4331 C CB   A GLU   B 1 26  ? 49.646 -24.472 -12.411 0.60 16.95 ?  26  GLU   B CB   1 
ATOM   4332 C CB   B GLU   B 1 26  ? 49.641 -24.476 -12.396 0.40 16.69 ?  26  GLU   B CB   1 
ATOM   4333 C CG   A GLU   B 1 26  ? 49.314 -25.823 -12.995 0.60 19.32 ?  26  GLU   B CG   1 
ATOM   4334 C CG   B GLU   B 1 26  ? 49.181 -25.722 -13.123 0.40 18.66 ?  26  GLU   B CG   1 
ATOM   4335 C CD   A GLU   B 1 26  ? 49.133 -25.796 -14.503 0.60 20.06 ?  26  GLU   B CD   1 
ATOM   4336 C CD   B GLU   B 1 26  ? 48.834 -25.446 -14.582 0.40 19.11 ?  26  GLU   B CD   1 
ATOM   4337 O OE1  A GLU   B 1 26  ? 48.333 -24.977 -15.002 0.60 20.11 ?  26  GLU   B OE1  1 
ATOM   4338 O OE1  B GLU   B 1 26  ? 47.740 -24.905 -14.860 0.40 19.67 ?  26  GLU   B OE1  1 
ATOM   4339 O OE2  A GLU   B 1 26  ? 49.796 -26.600 -15.188 0.60 21.23 -1 26  GLU   B OE2  1 
ATOM   4340 O OE2  B GLU   B 1 26  ? 49.663 -25.760 -15.451 0.40 18.91 -1 26  GLU   B OE2  1 
ATOM   4341 H H    A GLU   B 1 26  ? 51.855 -24.926 -11.509 0.60 17.71 ?  26  GLU   B H    1 
ATOM   4342 H H    B GLU   B 1 26  ? 51.858 -24.932 -11.512 0.40 17.94 ?  26  GLU   B H    1 
ATOM   4343 H HA   A GLU   B 1 26  ? 51.059 -24.131 -13.856 0.60 18.62 ?  26  GLU   B HA   1 
ATOM   4344 H HA   B GLU   B 1 26  ? 51.049 -24.138 -13.852 0.40 18.52 ?  26  GLU   B HA   1 
ATOM   4345 H HB2  A GLU   B 1 26  ? 49.706 -24.574 -11.445 0.60 20.34 ?  26  GLU   B HB2  1 
ATOM   4346 H HB2  B GLU   B 1 26  ? 49.753 -24.704 -11.461 0.40 20.02 ?  26  GLU   B HB2  1 
ATOM   4347 H HB3  A GLU   B 1 26  ? 48.920 -23.864 -12.627 0.60 20.34 ?  26  GLU   B HB3  1 
ATOM   4348 H HB3  B GLU   B 1 26  ? 48.940 -23.812 -12.489 0.40 20.02 ?  26  GLU   B HB3  1 
ATOM   4349 H HG2  A GLU   B 1 26  ? 50.045 -26.421 -12.811 0.60 23.18 ?  26  GLU   B HG2  1 
ATOM   4350 H HG2  B GLU   B 1 26  ? 49.886 -26.392 -13.060 0.40 22.39 ?  26  GLU   B HG2  1 
ATOM   4351 H HG3  A GLU   B 1 26  ? 48.496 -26.144 -12.586 0.60 23.18 ?  26  GLU   B HG3  1 
ATOM   4352 H HG3  B GLU   B 1 26  ? 48.374 -26.052 -12.706 0.40 22.39 ?  26  GLU   B HG3  1 
ATOM   4353 N N    . ALA   B 1 27  ? 51.058 -21.808 -11.647 1.00 13.95 ?  27  ALA   B N    1 
ATOM   4354 C CA   . ALA   B 1 27  ? 51.021 -20.359 -11.500 1.00 13.91 ?  27  ALA   B CA   1 
ATOM   4355 C C    . ALA   B 1 27  ? 52.095 -19.697 -12.353 1.00 14.99 ?  27  ALA   B C    1 
ATOM   4356 O O    . ALA   B 1 27  ? 51.835 -18.694 -13.033 1.00 15.85 ?  27  ALA   B O    1 
ATOM   4357 C CB   . ALA   B 1 27  ? 51.165 -19.984 -10.026 1.00 14.43 ?  27  ALA   B CB   1 
ATOM   4358 H H    A ALA   B 1 27  ? 51.175 -22.245 -10.914 0.60 16.74 ?  27  ALA   B H    1 
ATOM   4359 H H    B ALA   B 1 27  ? 51.179 -22.244 -10.914 0.40 16.74 ?  27  ALA   B H    1 
ATOM   4360 H HA   . ALA   B 1 27  ? 50.163 -20.035 -11.804 1.00 16.68 ?  27  ALA   B HA   1 
ATOM   4361 H HB1  . ALA   B 1 27  ? 51.132 -19.019 -9.940  1.00 17.31 ?  27  ALA   B HB1  1 
ATOM   4362 H HB2  . ALA   B 1 27  ? 50.428 -20.382 -9.528  1.00 17.31 ?  27  ALA   B HB2  1 
ATOM   4363 H HB3  . ALA   B 1 27  ? 52.008 -20.322 -9.691  1.00 17.31 ?  27  ALA   B HB3  1 
ATOM   4364 N N    . LYS   B 1 28  ? 53.306 -20.259 -12.352 1.00 16.23 ?  28  LYS   B N    1 
ATOM   4365 C CA   . LYS   B 1 28  ? 54.383 -19.651 -13.124 1.00 18.65 ?  28  LYS   B CA   1 
ATOM   4366 C C    . LYS   B 1 28  ? 54.123 -19.738 -14.621 1.00 19.17 ?  28  LYS   B C    1 
ATOM   4367 O O    . LYS   B 1 28  ? 54.530 -18.839 -15.369 1.00 20.27 ?  28  LYS   B O    1 
ATOM   4368 C CB   . LYS   B 1 28  ? 55.734 -20.256 -12.733 1.00 21.98 ?  28  LYS   B CB   1 
ATOM   4369 C CG   . LYS   B 1 28  ? 56.136 -19.895 -11.307 1.00 25.76 ?  28  LYS   B CG   1 
ATOM   4370 C CD   . LYS   B 1 28  ? 57.556 -20.317 -10.959 1.00 31.10 ?  28  LYS   B CD   1 
ATOM   4371 C CE   . LYS   B 1 28  ? 57.634 -21.782 -10.594 1.00 35.95 ?  28  LYS   B CE   1 
ATOM   4372 N NZ   . LYS   B 1 28  ? 58.986 -22.148 -10.076 1.00 38.37 ?  28  LYS   B NZ   1 
ATOM   4373 H H    . LYS   B 1 28  ? 53.526 -20.973 -11.925 1.00 19.47 ?  28  LYS   B H    1 
ATOM   4374 H HA   . LYS   B 1 28  ? 54.420 -18.710 -12.908 1.00 22.38 ?  28  LYS   B HA   1 
ATOM   4375 H HB2  . LYS   B 1 28  ? 55.683 -21.222 -12.796 1.00 26.37 ?  28  LYS   B HB2  1 
ATOM   4376 H HB3  . LYS   B 1 28  ? 56.420 -19.919 -13.334 1.00 26.37 ?  28  LYS   B HB3  1 
ATOM   4377 H HG2  . LYS   B 1 28  ? 56.073 -18.931 -11.201 1.00 30.91 ?  28  LYS   B HG2  1 
ATOM   4378 H HG3  . LYS   B 1 28  ? 55.530 -20.334 -10.692 1.00 30.91 ?  28  LYS   B HG3  1 
ATOM   4379 H HD2  . LYS   B 1 28  ? 58.130 -20.162 -11.726 1.00 37.32 ?  28  LYS   B HD2  1 
ATOM   4380 H HD3  . LYS   B 1 28  ? 57.862 -19.795 -10.201 1.00 37.32 ?  28  LYS   B HD3  1 
ATOM   4381 H HE2  . LYS   B 1 28  ? 56.982 -21.973 -9.902  1.00 43.13 ?  28  LYS   B HE2  1 
ATOM   4382 H HE3  . LYS   B 1 28  ? 57.454 -22.319 -11.381 1.00 43.13 ?  28  LYS   B HE3  1 
ATOM   4383 H HZ1  . LYS   B 1 28  ? 59.008 -23.013 -9.868  1.00 46.03 ?  28  LYS   B HZ1  1 
ATOM   4384 H HZ2  . LYS   B 1 28  ? 59.603 -21.984 -10.696 1.00 46.03 ?  28  LYS   B HZ2  1 
ATOM   4385 H HZ3  . LYS   B 1 28  ? 59.173 -21.671 -9.348  1.00 46.03 ?  28  LYS   B HZ3  1 
ATOM   4386 N N    . LYS   B 1 29  ? 53.418 -20.774 -15.075 1.00 20.53 ?  29  LYS   B N    1 
ATOM   4387 C CA   . LYS   B 1 29  ? 53.136 -20.918 -16.499 1.00 23.37 ?  29  LYS   B CA   1 
ATOM   4388 C C    . LYS   B 1 29  ? 51.888 -20.156 -16.936 1.00 22.23 ?  29  LYS   B C    1 
ATOM   4389 O O    . LYS   B 1 29  ? 51.890 -19.529 -18.002 1.00 23.52 ?  29  LYS   B O    1 
ATOM   4390 C CB   . LYS   B 1 29  ? 53.001 -22.400 -16.857 1.00 28.38 ?  29  LYS   B CB   1 
ATOM   4391 C CG   . LYS   B 1 29  ? 52.786 -22.663 -18.336 1.00 33.04 ?  29  LYS   B CG   1 
ATOM   4392 C CD   . LYS   B 1 29  ? 53.024 -24.126 -18.679 1.00 36.79 ?  29  LYS   B CD   1 
ATOM   4393 C CE   . LYS   B 1 29  ? 51.966 -25.030 -18.069 1.00 39.51 ?  29  LYS   B CE   1 
ATOM   4394 N NZ   . LYS   B 1 29  ? 52.223 -26.468 -18.373 1.00 40.90 ?  29  LYS   B NZ   1 
ATOM   4395 H H    . LYS   B 1 29  ? 53.087 -21.405 -14.580 1.00 24.63 ?  29  LYS   B H    1 
ATOM   4396 H HA   . LYS   B 1 29  ? 53.886 -20.564 -16.997 1.00 28.03 ?  29  LYS   B HA   1 
ATOM   4397 H HB2  . LYS   B 1 29  ? 53.816 -22.858 -16.593 1.00 34.05 ?  29  LYS   B HB2  1 
ATOM   4398 H HB3  . LYS   B 1 29  ? 52.246 -22.770 -16.379 1.00 34.05 ?  29  LYS   B HB3  1 
ATOM   4399 H HG2  . LYS   B 1 29  ? 51.871 -22.440 -18.570 1.00 39.65 ?  29  LYS   B HG2  1 
ATOM   4400 H HG3  . LYS   B 1 29  ? 53.406 -22.123 -18.852 1.00 39.65 ?  29  LYS   B HG3  1 
ATOM   4401 H HD2  . LYS   B 1 29  ? 52.999 -24.235 -19.642 1.00 44.14 ?  29  LYS   B HD2  1 
ATOM   4402 H HD3  . LYS   B 1 29  ? 53.890 -24.397 -18.335 1.00 44.14 ?  29  LYS   B HD3  1 
ATOM   4403 H HE2  . LYS   B 1 29  ? 51.966 -24.922 -17.105 1.00 47.40 ?  29  LYS   B HE2  1 
ATOM   4404 H HE3  . LYS   B 1 29  ? 51.097 -24.794 -18.432 1.00 47.40 ?  29  LYS   B HE3  1 
ATOM   4405 H HZ1  . LYS   B 1 29  ? 51.590 -26.975 -18.006 1.00 49.08 ?  29  LYS   B HZ1  1 
ATOM   4406 H HZ2  . LYS   B 1 29  ? 52.222 -26.597 -19.254 1.00 49.08 ?  29  LYS   B HZ2  1 
ATOM   4407 H HZ3  . LYS   B 1 29  ? 53.014 -26.711 -18.046 1.00 49.08 ?  29  LYS   B HZ3  1 
ATOM   4408 N N    . VAL   B 1 30  ? 50.819 -20.207 -16.136 1.00 20.59 ?  30  VAL   B N    1 
ATOM   4409 C CA   . VAL   B 1 30  ? 49.534 -19.608 -16.506 1.00 20.49 ?  30  VAL   B CA   1 
ATOM   4410 C C    . VAL   B 1 30  ? 49.542 -18.092 -16.345 1.00 19.47 ?  30  VAL   B C    1 
ATOM   4411 O O    . VAL   B 1 30  ? 48.820 -17.379 -17.060 1.00 20.53 ?  30  VAL   B O    1 
ATOM   4412 C CB   . VAL   B 1 30  ? 48.425 -20.227 -15.634 1.00 21.84 ?  30  VAL   B CB   1 
ATOM   4413 C CG1  . VAL   B 1 30  ? 47.148 -19.398 -15.701 1.00 22.35 ?  30  VAL   B CG1  1 
ATOM   4414 C CG2  . VAL   B 1 30  ? 48.166 -21.673 -16.039 1.00 22.71 ?  30  VAL   B CG2  1 
ATOM   4415 H H    . VAL   B 1 30  ? 50.803 -20.616 -15.370 1.00 24.70 ?  30  VAL   B H    1 
ATOM   4416 H HA   . VAL   B 1 30  ? 49.338 -19.832 -17.430 1.00 24.58 ?  30  VAL   B HA   1 
ATOM   4417 H HB   . VAL   B 1 30  ? 48.718 -20.239 -14.709 1.00 26.20 ?  30  VAL   B HB   1 
ATOM   4418 H HG11 . VAL   B 1 30  ? 46.397 -19.971 -15.481 1.00 26.81 ?  30  VAL   B HG11 1 
ATOM   4419 H HG12 . VAL   B 1 30  ? 47.204 -18.674 -15.059 1.00 26.81 ?  30  VAL   B HG12 1 
ATOM   4420 H HG13 . VAL   B 1 30  ? 47.037 -19.055 -16.596 1.00 26.81 ?  30  VAL   B HG13 1 
ATOM   4421 H HG21 . VAL   B 1 30  ? 47.463 -22.044 -15.474 1.00 27.25 ?  30  VAL   B HG21 1 
ATOM   4422 H HG22 . VAL   B 1 30  ? 47.881 -21.697 -16.967 1.00 27.25 ?  30  VAL   B HG22 1 
ATOM   4423 H HG23 . VAL   B 1 30  ? 48.979 -22.187 -15.928 1.00 27.25 ?  30  VAL   B HG23 1 
ATOM   4424 N N    A LYS   B 1 31  ? 50.324 -17.580 -15.404 0.60 18.65 ?  31  LYS   B N    1 
ATOM   4425 N N    B LYS   B 1 31  ? 50.324 -17.585 -15.403 0.40 19.04 ?  31  LYS   B N    1 
ATOM   4426 C CA   A LYS   B 1 31  ? 50.349 -16.166 -15.048 0.60 18.90 ?  31  LYS   B CA   1 
ATOM   4427 C CA   B LYS   B 1 31  ? 50.349 -16.175 -15.047 0.40 19.29 ?  31  LYS   B CA   1 
ATOM   4428 C C    A LYS   B 1 31  ? 48.954 -15.682 -14.662 0.60 17.05 ?  31  LYS   B C    1 
ATOM   4429 C C    B LYS   B 1 31  ? 48.944 -15.707 -14.681 0.40 17.27 ?  31  LYS   B C    1 
ATOM   4430 O O    A LYS   B 1 31  ? 48.421 -14.747 -15.275 0.60 17.63 ?  31  LYS   B O    1 
ATOM   4431 O O    B LYS   B 1 31  ? 48.388 -14.818 -15.340 0.40 17.58 ?  31  LYS   B O    1 
ATOM   4432 C CB   A LYS   B 1 31  ? 50.971 -15.336 -16.177 0.60 21.67 ?  31  LYS   B CB   1 
ATOM   4433 C CB   B LYS   B 1 31  ? 50.969 -15.352 -16.178 0.40 21.81 ?  31  LYS   B CB   1 
ATOM   4434 C CG   A LYS   B 1 31  ? 52.419 -15.716 -16.475 0.60 24.49 ?  31  LYS   B CG   1 
ATOM   4435 C CG   B LYS   B 1 31  ? 52.370 -15.826 -16.549 0.40 24.24 ?  31  LYS   B CG   1 
ATOM   4436 C CD   A LYS   B 1 31  ? 52.983 -14.914 -17.635 0.60 27.42 ?  31  LYS   B CD   1 
ATOM   4437 C CD   B LYS   B 1 31  ? 52.936 -15.071 -17.735 0.40 26.51 ?  31  LYS   B CD   1 
ATOM   4438 C CE   A LYS   B 1 31  ? 54.459 -15.198 -17.832 0.60 29.92 ?  31  LYS   B CE   1 
ATOM   4439 C CE   B LYS   B 1 31  ? 54.420 -15.342 -17.897 0.40 28.31 ?  31  LYS   B CE   1 
ATOM   4440 N NZ   A LYS   B 1 31  ? 55.250 -14.835 -16.624 0.60 31.31 ?  31  LYS   B NZ   1 
ATOM   4441 N NZ   B LYS   B 1 31  ? 55.174 -14.981 -16.663 0.40 29.27 ?  31  LYS   B NZ   1 
ATOM   4442 H H    A LYS   B 1 31  ? 50.872 -18.059 -14.948 0.60 22.38 ?  31  LYS   B H    1 
ATOM   4443 H H    B LYS   B 1 31  ? 50.871 -18.063 -14.948 0.40 22.84 ?  31  LYS   B H    1 
ATOM   4444 H HA   A LYS   B 1 31  ? 50.911 -16.071 -14.272 0.60 22.68 ?  31  LYS   B HA   1 
ATOM   4445 H HA   B LYS   B 1 31  ? 50.908 -16.074 -14.267 0.40 23.15 ?  31  LYS   B HA   1 
ATOM   4446 H HB2  A LYS   B 1 31  ? 50.456 -15.465 -16.989 0.60 25.99 ?  31  LYS   B HB2  1 
ATOM   4447 H HB2  B LYS   B 1 31  ? 50.413 -15.417 -16.968 0.40 26.17 ?  31  LYS   B HB2  1 
ATOM   4448 H HB3  A LYS   B 1 31  ? 50.955 -14.402 -15.918 0.60 25.99 ?  31  LYS   B HB3  1 
ATOM   4449 H HB3  B LYS   B 1 31  ? 51.035 -14.426 -15.892 0.40 26.17 ?  31  LYS   B HB3  1 
ATOM   4450 H HG2  A LYS   B 1 31  ? 52.960 -15.540 -15.689 0.60 29.38 ?  31  LYS   B HG2  1 
ATOM   4451 H HG2  B LYS   B 1 31  ? 52.958 -15.692 -15.789 0.40 29.08 ?  31  LYS   B HG2  1 
ATOM   4452 H HG3  A LYS   B 1 31  ? 52.462 -16.658 -16.706 0.60 29.38 ?  31  LYS   B HG3  1 
ATOM   4453 H HG3  B LYS   B 1 31  ? 52.340 -16.768 -16.781 0.40 29.08 ?  31  LYS   B HG3  1 
ATOM   4454 H HD2  A LYS   B 1 31  ? 52.512 -15.158 -18.448 0.60 32.90 ?  31  LYS   B HD2  1 
ATOM   4455 H HD2  B LYS   B 1 31  ? 52.483 -15.360 -18.543 0.40 31.80 ?  31  LYS   B HD2  1 
ATOM   4456 H HD3  A LYS   B 1 31  ? 52.873 -13.969 -17.452 0.60 32.90 ?  31  LYS   B HD3  1 
ATOM   4457 H HD3  B LYS   B 1 31  ? 52.812 -14.121 -17.599 0.40 31.80 ?  31  LYS   B HD3  1 
ATOM   4458 H HE2  A LYS   B 1 31  ? 54.585 -16.145 -18.005 0.60 35.90 ?  31  LYS   B HE2  1 
ATOM   4459 H HE2  B LYS   B 1 31  ? 54.558 -16.287 -18.072 0.40 33.96 ?  31  LYS   B HE2  1 
ATOM   4460 H HE3  A LYS   B 1 31  ? 54.789 -14.675 -18.580 0.60 35.90 ?  31  LYS   B HE3  1 
ATOM   4461 H HE3  B LYS   B 1 31  ? 54.766 -14.811 -18.631 0.40 33.96 ?  31  LYS   B HE3  1 
ATOM   4462 H HZ1  A LYS   B 1 31  ? 56.120 -14.917 -16.793 0.60 37.56 ?  31  LYS   B HZ1  1 
ATOM   4463 H HZ1  B LYS   B 1 31  ? 56.047 -14.971 -16.831 0.40 35.12 ?  31  LYS   B HZ1  1 
ATOM   4464 H HZ2  A LYS   B 1 31  ? 55.079 -13.993 -16.392 0.60 37.56 ?  31  LYS   B HZ2  1 
ATOM   4465 H HZ2  B LYS   B 1 31  ? 54.924 -14.174 -16.380 0.40 35.12 ?  31  LYS   B HZ2  1 
ATOM   4466 H HZ3  A LYS   B 1 31  ? 55.035 -15.371 -15.947 0.60 37.56 ?  31  LYS   B HZ3  1 
ATOM   4467 H HZ3  B LYS   B 1 31  ? 55.009 -15.575 -16.020 0.40 35.12 ?  31  LYS   B HZ3  1 
ATOM   4468 N N    . PRO   B 1 32  ? 48.345 -16.277 -13.636 1.00 15.34 ?  32  PRO   B N    1 
ATOM   4469 C CA   . PRO   B 1 32  ? 46.971 -15.916 -13.278 1.00 14.41 ?  32  PRO   B CA   1 
ATOM   4470 C C    . PRO   B 1 32  ? 46.886 -14.573 -12.575 1.00 14.23 ?  32  PRO   B C    1 
ATOM   4471 O O    . PRO   B 1 32  ? 47.803 -14.152 -11.867 1.00 15.33 ?  32  PRO   B O    1 
ATOM   4472 C CB   . PRO   B 1 32  ? 46.571 -17.030 -12.303 1.00 14.65 ?  32  PRO   B CB   1 
ATOM   4473 C CG   . PRO   B 1 32  ? 47.869 -17.366 -11.619 1.00 15.14 ?  32  PRO   B CG   1 
ATOM   4474 C CD   . PRO   B 1 32  ? 48.920 -17.258 -12.691 1.00 15.15 ?  32  PRO   B CD   1 
ATOM   4475 H HA   . PRO   B 1 32  ? 46.387 -15.935 -14.058 1.00 17.28 ?  32  PRO   B HA   1 
ATOM   4476 H HB2  . PRO   B 1 32  ? 45.916 -16.698 -11.667 1.00 17.57 ?  32  PRO   B HB2  1 
ATOM   4477 H HB3  . PRO   B 1 32  ? 46.226 -17.798 -12.787 1.00 17.57 ?  32  PRO   B HB3  1 
ATOM   4478 H HG2  . PRO   B 1 32  ? 48.040 -16.725 -10.905 1.00 18.16 ?  32  PRO   B HG2  1 
ATOM   4479 H HG3  . PRO   B 1 32  ? 47.834 -18.268 -11.261 1.00 18.16 ?  32  PRO   B HG3  1 
ATOM   4480 H HD2  . PRO   B 1 32  ? 49.746 -16.919 -12.313 1.00 18.17 ?  32  PRO   B HD2  1 
ATOM   4481 H HD3  . PRO   B 1 32  ? 49.045 -18.117 -13.116 1.00 18.17 ?  32  PRO   B HD3  1 
ATOM   4482 N N    . THR   B 1 33  ? 45.737 -13.921 -12.747 1.00 13.88 ?  33  THR   B N    1 
ATOM   4483 C CA   . THR   B 1 33  ? 45.443 -12.744 -11.942 1.00 14.16 ?  33  THR   B CA   1 
ATOM   4484 C C    . THR   B 1 33  ? 45.392 -13.091 -10.461 1.00 13.75 ?  33  THR   B C    1 
ATOM   4485 O O    . THR   B 1 33  ? 45.863 -12.311 -9.619  1.00 14.76 ?  33  THR   B O    1 
ATOM   4486 C CB   . THR   B 1 33  ? 44.126 -12.112 -12.392 1.00 14.64 ?  33  THR   B CB   1 
ATOM   4487 O OG1  . THR   B 1 33  ? 44.171 -11.873 -13.801 1.00 14.38 ?  33  THR   B OG1  1 
ATOM   4488 C CG2  . THR   B 1 33  ? 43.884 -10.808 -11.654 1.00 15.65 ?  33  THR   B CG2  1 
ATOM   4489 H H    . THR   B 1 33  ? 45.124 -14.140 -13.310 1.00 16.65 ?  33  THR   B H    1 
ATOM   4490 H HA   . THR   B 1 33  ? 46.147 -12.093 -12.071 1.00 16.98 ?  33  THR   B HA   1 
ATOM   4491 H HB   . THR   B 1 33  ? 43.392 -12.720 -12.191 1.00 17.57 ?  33  THR   B HB   1 
ATOM   4492 H HG1  . THR   B 1 33  ? 43.457 -11.506 -14.053 1.00 17.25 ?  33  THR   B HG1  1 
ATOM   4493 H HG21 . THR   B 1 33  ? 43.132 -10.343 -12.041 1.00 18.78 ?  33  THR   B HG21 1 
ATOM   4494 H HG22 . THR   B 1 33  ? 43.702 -10.983 -10.716 1.00 18.78 ?  33  THR   B HG22 1 
ATOM   4495 H HG23 . THR   B 1 33  ? 44.674 -10.244 -11.719 1.00 18.78 ?  33  THR   B HG23 1 
ATOM   4496 N N    . VAL   B 1 34  ? 44.850 -14.265 -10.121 1.00 12.78 ?  34  VAL   B N    1 
ATOM   4497 C CA   . VAL   B 1 34  ? 44.655 -14.659 -8.730  1.00 12.28 ?  34  VAL   B CA   1 
ATOM   4498 C C    . VAL   B 1 34  ? 45.077 -16.109 -8.562  1.00 11.69 ?  34  VAL   B C    1 
ATOM   4499 O O    . VAL   B 1 34  ? 44.554 -16.996 -9.246  1.00 12.21 ?  34  VAL   B O    1 
ATOM   4500 C CB   . VAL   B 1 34  ? 43.185 -14.514 -8.290  1.00 13.26 ?  34  VAL   B CB   1 
ATOM   4501 C CG1  . VAL   B 1 34  ? 43.020 -14.953 -6.840  1.00 13.61 ?  34  VAL   B CG1  1 
ATOM   4502 C CG2  . VAL   B 1 34  ? 42.689 -13.088 -8.494  1.00 14.38 ?  34  VAL   B CG2  1 
ATOM   4503 H H    . VAL   B 1 34  ? 44.594 -14.863 -10.685 1.00 15.33 ?  34  VAL   B H    1 
ATOM   4504 H HA   . VAL   B 1 34  ? 45.210 -14.109 -8.152  1.00 14.73 ?  34  VAL   B HA   1 
ATOM   4505 H HB   . VAL   B 1 34  ? 42.639 -15.095 -8.840  1.00 15.91 ?  34  VAL   B HB   1 
ATOM   4506 H HG11 . VAL   B 1 34  ? 42.162 -14.635 -6.510  1.00 16.32 ?  34  VAL   B HG11 1 
ATOM   4507 H HG12 . VAL   B 1 34  ? 43.048 -15.921 -6.793  1.00 16.32 ?  34  VAL   B HG12 1 
ATOM   4508 H HG13 . VAL   B 1 34  ? 43.736 -14.572 -6.308  1.00 16.32 ?  34  VAL   B HG13 1 
ATOM   4509 H HG21 . VAL   B 1 34  ? 41.773 -13.021 -8.181  1.00 17.25 ?  34  VAL   B HG21 1 
ATOM   4510 H HG22 . VAL   B 1 34  ? 43.254 -12.477 -7.995  1.00 17.25 ?  34  VAL   B HG22 1 
ATOM   4511 H HG23 . VAL   B 1 34  ? 42.727 -12.869 -9.442  1.00 17.25 ?  34  VAL   B HG23 1 
ATOM   4512 N N    . VAL   B 1 35  ? 45.980 -16.361 -7.619  1.00 11.12 ?  35  VAL   B N    1 
ATOM   4513 C CA   . VAL   B 1 35  ? 46.211 -17.703 -7.097  1.00 10.84 ?  35  VAL   B CA   1 
ATOM   4514 C C    . VAL   B 1 35  ? 45.672 -17.755 -5.676  1.00 10.67 ?  35  VAL   B C    1 
ATOM   4515 O O    . VAL   B 1 35  ? 45.888 -16.829 -4.885  1.00 11.01 ?  35  VAL   B O    1 
ATOM   4516 C CB   . VAL   B 1 35  ? 47.694 -18.128 -7.171  1.00 11.50 ?  35  VAL   B CB   1 
ATOM   4517 C CG1  . VAL   B 1 35  ? 48.589 -17.285 -6.250  1.00 12.37 ?  35  VAL   B CG1  1 
ATOM   4518 C CG2  . VAL   B 1 35  ? 47.835 -19.616 -6.835  1.00 12.11 ?  35  VAL   B CG2  1 
ATOM   4519 H H    . VAL   B 1 35  ? 46.481 -15.760 -7.258  1.00 13.34 ?  35  VAL   B H    1 
ATOM   4520 H HA   . VAL   B 1 35  ? 45.699 -18.335 -7.625  1.00 13.00 ?  35  VAL   B HA   1 
ATOM   4521 H HB   . VAL   B 1 35  ? 48.008 -18.012 -8.080  1.00 13.79 ?  35  VAL   B HB   1 
ATOM   4522 H HG11 . VAL   B 1 35  ? 49.515 -17.508 -6.425  1.00 14.83 ?  35  VAL   B HG11 1 
ATOM   4523 H HG12 . VAL   B 1 35  ? 48.426 -16.352 -6.432  1.00 14.83 ?  35  VAL   B HG12 1 
ATOM   4524 H HG13 . VAL   B 1 35  ? 48.368 -17.490 -5.326  1.00 14.83 ?  35  VAL   B HG13 1 
ATOM   4525 H HG21 . VAL   B 1 35  ? 48.759 -19.888 -6.945  1.00 14.52 ?  35  VAL   B HG21 1 
ATOM   4526 H HG22 . VAL   B 1 35  ? 47.556 -19.768 -5.914  1.00 14.52 ?  35  VAL   B HG22 1 
ATOM   4527 H HG23 . VAL   B 1 35  ? 47.268 -20.138 -7.433  1.00 14.52 ?  35  VAL   B HG23 1 
ATOM   4528 N N    . VAL   B 1 36  ? 44.947 -18.829 -5.361  1.00 10.54 ?  36  VAL   B N    1 
ATOM   4529 C CA   . VAL   B 1 36  ? 44.403 -19.033 -4.026  1.00 9.83  ?  36  VAL   B CA   1 
ATOM   4530 C C    . VAL   B 1 36  ? 45.412 -19.792 -3.175  1.00 9.69  ?  36  VAL   B C    1 
ATOM   4531 O O    . VAL   B 1 36  ? 45.947 -20.829 -3.593  1.00 11.12 ?  36  VAL   B O    1 
ATOM   4532 C CB   . VAL   B 1 36  ? 43.066 -19.795 -4.096  1.00 10.82 ?  36  VAL   B CB   1 
ATOM   4533 C CG1  . VAL   B 1 36  ? 42.564 -20.145 -2.702  1.00 11.44 ?  36  VAL   B CG1  1 
ATOM   4534 C CG2  . VAL   B 1 36  ? 42.039 -18.966 -4.844  1.00 11.40 ?  36  VAL   B CG2  1 
ATOM   4535 H H    . VAL   B 1 36  ? 44.762 -19.464 -5.912  1.00 12.65 ?  36  VAL   B H    1 
ATOM   4536 H HA   . VAL   B 1 36  ? 44.238 -18.172 -3.613  1.00 11.79 ?  36  VAL   B HA   1 
ATOM   4537 H HB   . VAL   B 1 36  ? 43.194 -20.621 -4.586  1.00 12.98 ?  36  VAL   B HB   1 
ATOM   4538 H HG11 . VAL   B 1 36  ? 41.623 -20.380 -2.755  1.00 13.72 ?  36  VAL   B HG11 1 
ATOM   4539 H HG12 . VAL   B 1 36  ? 43.072 -20.888 -2.355  1.00 13.72 ?  36  VAL   B HG12 1 
ATOM   4540 H HG13 . VAL   B 1 36  ? 42.670 -19.367 -2.126  1.00 13.72 ?  36  VAL   B HG13 1 
ATOM   4541 H HG21 . VAL   B 1 36  ? 41.196 -19.445 -4.858  1.00 13.67 ?  36  VAL   B HG21 1 
ATOM   4542 H HG22 . VAL   B 1 36  ? 41.931 -18.115 -4.392  1.00 13.67 ?  36  VAL   B HG22 1 
ATOM   4543 H HG23 . VAL   B 1 36  ? 42.352 -18.820 -5.752  1.00 13.67 ?  36  VAL   B HG23 1 
ATOM   4544 N N    . ASN   B 1 37  ? 45.622 -19.306 -1.957  1.00 10.21 ?  37  ASN   B N    1 
ATOM   4545 C CA   . ASN   B 1 37  ? 46.379 -20.024 -0.948  1.00 10.76 ?  37  ASN   B CA   1 
ATOM   4546 C C    . ASN   B 1 37  ? 45.431 -20.692 0.036   1.00 10.84 ?  37  ASN   B C    1 
ATOM   4547 O O    . ASN   B 1 37  ? 44.417 -20.115 0.438   1.00 11.50 ?  37  ASN   B O    1 
ATOM   4548 C CB   . ASN   B 1 37  ? 47.305 -19.075 -0.190  1.00 10.63 ?  37  ASN   B CB   1 
ATOM   4549 C CG   . ASN   B 1 37  ? 48.153 -19.794 0.823   1.00 11.07 ?  37  ASN   B CG   1 
ATOM   4550 O OD1  . ASN   B 1 37  ? 48.484 -20.971 0.647   1.00 12.02 ?  37  ASN   B OD1  1 
ATOM   4551 N ND2  . ASN   B 1 37  ? 48.500 -19.104 1.901   1.00 11.20 ?  37  ASN   B ND2  1 
ATOM   4552 H H    . ASN   B 1 37  ? 45.337 -18.535 -1.686  1.00 12.25 ?  37  ASN   B H    1 
ATOM   4553 H HA   . ASN   B 1 37  ? 46.915 -20.713 -1.367  1.00 12.90 ?  37  ASN   B HA   1 
ATOM   4554 H HB2  . ASN   B 1 37  ? 47.901 -18.648 -0.821  1.00 12.75 ?  37  ASN   B HB2  1 
ATOM   4555 H HB3  . ASN   B 1 37  ? 46.776 -18.415 0.278   1.00 12.75 ?  37  ASN   B HB3  1 
ATOM   4556 H HD21 . ASN   B 1 37  ? 48.993 -19.468 2.505   1.00 13.43 ?  37  ASN   B HD21 1 
ATOM   4557 H HD22 . ASN   B 1 37  ? 48.258 -18.288 1.987   1.00 13.43 ?  37  ASN   B HD22 1 
ATOM   4558 N N    . ALA   B 1 38  ? 45.776 -21.927 0.408   1.00 11.02 ?  38  ALA   B N    1 
ATOM   4559 C CA   . ALA   B 1 38  ? 45.117 -22.672 1.483   1.00 11.51 ?  38  ALA   B CA   1 
ATOM   4560 C C    . ALA   B 1 38  ? 45.700 -22.186 2.806   1.00 11.36 ?  38  ALA   B C    1 
ATOM   4561 O O    . ALA   B 1 38  ? 46.597 -22.794 3.396   1.00 12.41 ?  38  ALA   B O    1 
ATOM   4562 C CB   . ALA   B 1 38  ? 45.340 -24.166 1.296   1.00 12.80 ?  38  ALA   B CB   1 
ATOM   4563 H H    . ALA   B 1 38  ? 46.421 -22.367 0.048   1.00 13.22 ?  38  ALA   B H    1 
ATOM   4564 H HA   . ALA   B 1 38  ? 44.165 -22.492 1.477   1.00 13.81 ?  38  ALA   B HA   1 
ATOM   4565 H HB1  . ALA   B 1 38  ? 44.891 -24.647 2.018   1.00 15.35 ?  38  ALA   B HB1  1 
ATOM   4566 H HB2  . ALA   B 1 38  ? 44.960 -24.439 0.444   1.00 15.35 ?  38  ALA   B HB2  1 
ATOM   4567 H HB3  . ALA   B 1 38  ? 46.286 -24.356 1.316   1.00 15.35 ?  38  ALA   B HB3  1 
ATOM   4568 N N    . ALA   B 1 39  ? 45.182 -21.049 3.261   1.00 11.01 ?  39  ALA   B N    1 
ATOM   4569 C CA   . ALA   B 1 39  ? 45.732 -20.318 4.391   1.00 11.55 ?  39  ALA   B CA   1 
ATOM   4570 C C    . ALA   B 1 39  ? 45.111 -20.758 5.717   1.00 11.47 ?  39  ALA   B C    1 
ATOM   4571 O O    . ALA   B 1 39  ? 44.080 -21.428 5.768   1.00 12.48 ?  39  ALA   B O    1 
ATOM   4572 C CB   . ALA   B 1 39  ? 45.499 -18.817 4.191   1.00 12.00 ?  39  ALA   B CB   1 
ATOM   4573 H H    . ALA   B 1 39  ? 44.488 -20.678 2.918   1.00 13.21 ?  39  ALA   B H    1 
ATOM   4574 H HA   . ALA   B 1 39  ? 46.685 -20.474 4.436   1.00 13.86 ?  39  ALA   B HA   1 
ATOM   4575 H HB1  . ALA   B 1 39  ? 45.867 -18.338 4.947   1.00 14.40 ?  39  ALA   B HB1  1 
ATOM   4576 H HB2  . ALA   B 1 39  ? 45.939 -18.536 3.372   1.00 14.40 ?  39  ALA   B HB2  1 
ATOM   4577 H HB3  . ALA   B 1 39  ? 44.545 -18.651 4.125   1.00 14.40 ?  39  ALA   B HB3  1 
ATOM   4578 N N    . ASN   B 1 40  ? 45.754 -20.337 6.804   1.00 12.14 ?  40  ASN   B N    1 
ATOM   4579 C CA   . ASN   B 1 40  ? 45.195 -20.383 8.145   1.00 12.59 ?  40  ASN   B CA   1 
ATOM   4580 C C    . ASN   B 1 40  ? 45.015 -18.956 8.667   1.00 12.50 ?  40  ASN   B C    1 
ATOM   4581 O O    . ASN   B 1 40  ? 45.424 -17.976 8.035   1.00 12.57 ?  40  ASN   B O    1 
ATOM   4582 C CB   . ASN   B 1 40  ? 46.042 -21.259 9.085   1.00 13.17 ?  40  ASN   B CB   1 
ATOM   4583 C CG   . ASN   B 1 40  ? 47.495 -20.852 9.119   1.00 14.73 ?  40  ASN   B CG   1 
ATOM   4584 O OD1  . ASN   B 1 40  ? 47.817 -19.670 9.181   1.00 16.68 ?  40  ASN   B OD1  1 
ATOM   4585 N ND2  . ASN   B 1 40  ? 48.386 -21.830 9.086   1.00 14.66 ?  40  ASN   B ND2  1 
ATOM   4586 H H    . ASN   B 1 40  ? 46.553 -20.024 6.779   1.00 14.56 ?  40  ASN   B H    1 
ATOM   4587 H HA   . ASN   B 1 40  ? 44.311 -20.776 8.095   1.00 15.10 ?  40  ASN   B HA   1 
ATOM   4588 H HB2  . ASN   B 1 40  ? 45.682 -21.185 9.983   1.00 15.80 ?  40  ASN   B HB2  1 
ATOM   4589 H HB3  . ASN   B 1 40  ? 45.991 -22.176 8.780   1.00 15.80 ?  40  ASN   B HB3  1 
ATOM   4590 H HD21 . ASN   B 1 40  ? 49.226 -21.650 9.110   1.00 17.59 ?  40  ASN   B HD21 1 
ATOM   4591 H HD22 . ASN   B 1 40  ? 48.122 -22.648 9.043   1.00 17.59 ?  40  ASN   B HD22 1 
ATOM   4592 N N    . VAL   B 1 41  ? 44.361 -18.830 9.824   1.00 13.15 ?  41  VAL   B N    1 
ATOM   4593 C CA   . VAL   B 1 41  ? 43.906 -17.509 10.272  1.00 13.57 ?  41  VAL   B CA   1 
ATOM   4594 C C    . VAL   B 1 41  ? 45.056 -16.556 10.566  1.00 13.60 ?  41  VAL   B C    1 
ATOM   4595 O O    . VAL   B 1 41  ? 44.876 -15.335 10.487  1.00 13.95 ?  41  VAL   B O    1 
ATOM   4596 C CB   . VAL   B 1 41  ? 42.939 -17.591 11.470  1.00 15.19 ?  41  VAL   B CB   1 
ATOM   4597 C CG1  . VAL   B 1 41  ? 41.627 -18.257 11.068  1.00 15.63 ?  41  VAL   B CG1  1 
ATOM   4598 C CG2  . VAL   B 1 41  ? 43.595 -18.293 12.650  1.00 16.26 ?  41  VAL   B CG2  1 
ATOM   4599 H H    . VAL   B 1 41  ? 44.167 -19.474 10.346  1.00 15.77 ?  41  VAL   B H    1 
ATOM   4600 H HA   . VAL   B 1 41  ? 43.405 -17.109 9.547   1.00 16.27 ?  41  VAL   B HA   1 
ATOM   4601 H HB   . VAL   B 1 41  ? 42.729 -16.687 11.756  1.00 18.22 ?  41  VAL   B HB   1 
ATOM   4602 H HG11 . VAL   B 1 41  ? 41.031 -18.266 11.834  1.00 18.75 ?  41  VAL   B HG11 1 
ATOM   4603 H HG12 . VAL   B 1 41  ? 41.227 -17.752 10.344  1.00 18.75 ?  41  VAL   B HG12 1 
ATOM   4604 H HG13 . VAL   B 1 41  ? 41.810 -19.164 10.780  1.00 18.75 ?  41  VAL   B HG13 1 
ATOM   4605 H HG21 . VAL   B 1 41  ? 42.970 -18.317 13.389  1.00 19.51 ?  41  VAL   B HG21 1 
ATOM   4606 H HG22 . VAL   B 1 41  ? 43.831 -19.198 12.387  1.00 19.51 ?  41  VAL   B HG22 1 
ATOM   4607 H HG23 . VAL   B 1 41  ? 44.394 -17.806 12.905  1.00 19.51 ?  41  VAL   B HG23 1 
ATOM   4608 N N    . TYR   B 1 42  ? 46.224 -17.073 10.952  1.00 13.98 ?  42  TYR   B N    1 
ATOM   4609 C CA   . TYR   B 1 42  ? 47.381 -16.228 11.223  1.00 14.12 ?  42  TYR   B CA   1 
ATOM   4610 C C    . TYR   B 1 42  ? 48.344 -16.156 10.042  1.00 13.54 ?  42  TYR   B C    1 
ATOM   4611 O O    . TYR   B 1 42  ? 49.435 -15.592 10.178  1.00 14.70 ?  42  TYR   B O    1 
ATOM   4612 C CB   . TYR   B 1 42  ? 48.074 -16.638 12.528  1.00 16.22 ?  42  TYR   B CB   1 
ATOM   4613 C CG   . TYR   B 1 42  ? 47.468 -15.955 13.751  1.00 16.84 ?  42  TYR   B CG   1 
ATOM   4614 C CD1  . TYR   B 1 42  ? 47.688 -14.601 13.986  1.00 16.54 ?  42  TYR   B CD1  1 
ATOM   4615 C CD2  . TYR   B 1 42  ? 46.679 -16.651 14.655  1.00 18.66 ?  42  TYR   B CD2  1 
ATOM   4616 C CE1  . TYR   B 1 42  ? 47.143 -13.961 15.085  1.00 17.51 ?  42  TYR   B CE1  1 
ATOM   4617 C CE2  . TYR   B 1 42  ? 46.130 -16.018 15.763  1.00 18.82 ?  42  TYR   B CE2  1 
ATOM   4618 C CZ   . TYR   B 1 42  ? 46.366 -14.670 15.972  1.00 19.51 ?  42  TYR   B CZ   1 
ATOM   4619 O OH   . TYR   B 1 42  ? 45.825 -14.027 17.069  1.00 22.39 ?  42  TYR   B OH   1 
ATOM   4620 H H    . TYR   B 1 42  ? 46.372 -17.920 11.056  1.00 16.77 ?  42  TYR   B H    1 
ATOM   4621 H HA   . TYR   B 1 42  ? 47.054 -15.330 11.361  1.00 16.94 ?  42  TYR   B HA   1 
ATOM   4622 H HB2  . TYR   B 1 42  ? 47.991 -17.596 12.648  1.00 19.46 ?  42  TYR   B HB2  1 
ATOM   4623 H HB3  . TYR   B 1 42  ? 49.011 -16.389 12.479  1.00 19.46 ?  42  TYR   B HB3  1 
ATOM   4624 H HD1  . TYR   B 1 42  ? 48.215 -14.116 13.388  1.00 19.84 ?  42  TYR   B HD1  1 
ATOM   4625 H HD2  . TYR   B 1 42  ? 46.516 -17.559 14.518  1.00 22.39 ?  42  TYR   B HD2  1 
ATOM   4626 H HE1  . TYR   B 1 42  ? 47.308 -13.056 15.221  1.00 21.01 ?  42  TYR   B HE1  1 
ATOM   4627 H HE2  . TYR   B 1 42  ? 45.603 -16.499 16.359  1.00 22.57 ?  42  TYR   B HE2  1 
ATOM   4628 H HH   . TYR   B 1 42  ? 46.053 -13.222 17.063  1.00 26.86 ?  42  TYR   B HH   1 
ATOM   4629 N N    . LEU   B 1 43  ? 47.944 -16.666 8.879   1.00 12.48 ?  43  LEU   B N    1 
ATOM   4630 C CA   . LEU   B 1 43  ? 48.754 -16.604 7.667   1.00 12.25 ?  43  LEU   B CA   1 
ATOM   4631 C C    . LEU   B 1 43  ? 50.165 -17.115 7.925   1.00 12.56 ?  43  LEU   B C    1 
ATOM   4632 O O    . LEU   B 1 43  ? 51.149 -16.518 7.487   1.00 13.27 ?  43  LEU   B O    1 
ATOM   4633 C CB   . LEU   B 1 43  ? 48.777 -15.200 7.058   1.00 12.57 ?  43  LEU   B CB   1 
ATOM   4634 C CG   . LEU   B 1 43  ? 47.424 -14.579 6.690   1.00 13.19 ?  43  LEU   B CG   1 
ATOM   4635 C CD1  . LEU   B 1 43  ? 47.648 -13.193 6.080   1.00 14.18 ?  43  LEU   B CD1  1 
ATOM   4636 C CD2  . LEU   B 1 43  ? 46.645 -15.481 5.742   1.00 13.36 ?  43  LEU   B CD2  1 
ATOM   4637 H H    . LEU   B 1 43  ? 47.192 -17.067 8.769   1.00 14.97 ?  43  LEU   B H    1 
ATOM   4638 H HA   . LEU   B 1 43  ? 48.354 -17.196 7.010   1.00 14.69 ?  43  LEU   B HA   1 
ATOM   4639 H HB2  . LEU   B 1 43  ? 49.206 -14.606 7.690   1.00 15.08 ?  43  LEU   B HB2  1 
ATOM   4640 H HB3  . LEU   B 1 43  ? 49.304 -15.239 6.244   1.00 15.08 ?  43  LEU   B HB3  1 
ATOM   4641 H HG   . LEU   B 1 43  ? 46.901 -14.466 7.497   1.00 15.82 ?  43  LEU   B HG   1 
ATOM   4642 H HD11 . LEU   B 1 43  ? 46.789 -12.804 5.851   1.00 17.01 ?  43  LEU   B HD11 1 
ATOM   4643 H HD12 . LEU   B 1 43  ? 48.101 -12.629 6.730   1.00 17.01 ?  43  LEU   B HD12 1 
ATOM   4644 H HD13 . LEU   B 1 43  ? 48.194 -13.280 5.283   1.00 17.01 ?  43  LEU   B HD13 1 
ATOM   4645 H HD21 . LEU   B 1 43  ? 45.847 -15.014 5.444   1.00 16.02 ?  43  LEU   B HD21 1 
ATOM   4646 H HD22 . LEU   B 1 43  ? 47.202 -15.704 4.982   1.00 16.02 ?  43  LEU   B HD22 1 
ATOM   4647 H HD23 . LEU   B 1 43  ? 46.391 -16.292 6.215   1.00 16.02 ?  43  LEU   B HD23 1 
ATOM   4648 N N    . LYS   B 1 44  ? 50.261 -18.237 8.644   1.00 12.69 ?  44  LYS   B N    1 
ATOM   4649 C CA   . LYS   B 1 44  ? 51.527 -18.916 8.896   1.00 13.71 ?  44  LYS   B CA   1 
ATOM   4650 C C    . LYS   B 1 44  ? 51.642 -20.033 7.868   1.00 13.30 ?  44  LYS   B C    1 
ATOM   4651 O O    . LYS   B 1 44  ? 50.949 -21.048 7.952   1.00 14.16 ?  44  LYS   B O    1 
ATOM   4652 C CB   . LYS   B 1 44  ? 51.571 -19.424 10.333  1.00 15.27 ?  44  LYS   B CB   1 
ATOM   4653 C CG   . LYS   B 1 44  ? 51.765 -18.313 11.356  1.00 18.28 ?  44  LYS   B CG   1 
ATOM   4654 C CD   . LYS   B 1 44  ? 52.949 -17.436 10.944  1.00 21.23 ?  44  LYS   B CD   1 
ATOM   4655 C CE   . LYS   B 1 44  ? 53.480 -16.593 12.073  1.00 24.30 ?  44  LYS   B CE   1 
ATOM   4656 N NZ   . LYS   B 1 44  ? 54.652 -15.775 11.673  1.00 25.37 ?  44  LYS   B NZ   1 
ATOM   4657 H H    . LYS   B 1 44  ? 49.583 -18.624 9.009   1.00 15.23 ?  44  LYS   B H    1 
ATOM   4658 H HA   . LYS   B 1 44  ? 52.258 -18.302 8.737   1.00 16.44 ?  44  LYS   B HA   1 
ATOM   4659 H HB2  . LYS   B 1 44  ? 50.728 -19.867 10.539  1.00 18.31 ?  44  LYS   B HB2  1 
ATOM   4660 H HB3  . LYS   B 1 44  ? 52.302 -20.047 10.429  1.00 18.31 ?  44  LYS   B HB3  1 
ATOM   4661 H HG2  . LYS   B 1 44  ? 50.968 -17.764 11.398  1.00 21.92 ?  44  LYS   B HG2  1 
ATOM   4662 H HG3  . LYS   B 1 44  ? 51.958 -18.704 12.225  1.00 21.92 ?  44  LYS   B HG3  1 
ATOM   4663 H HD2  . LYS   B 1 44  ? 53.663 -18.011 10.614  1.00 25.47 ?  44  LYS   B HD2  1 
ATOM   4664 H HD3  . LYS   B 1 44  ? 52.659 -16.835 10.238  1.00 25.47 ?  44  LYS   B HD3  1 
ATOM   4665 H HE2  . LYS   B 1 44  ? 52.791 -15.974 12.329  1.00 29.16 ?  44  LYS   B HE2  1 
ATOM   4666 H HE3  . LYS   B 1 44  ? 53.732 -17.165 12.818  1.00 29.16 ?  44  LYS   B HE3  1 
ATOM   4667 H HZ1  . LYS   B 1 44  ? 54.932 -15.288 12.364  1.00 30.44 ?  44  LYS   B HZ1  1 
ATOM   4668 H HZ2  . LYS   B 1 44  ? 55.315 -16.299 11.399  1.00 30.44 ?  44  LYS   B HZ2  1 
ATOM   4669 H HZ3  . LYS   B 1 44  ? 54.424 -15.226 11.008  1.00 30.44 ?  44  LYS   B HZ3  1 
ATOM   4670 N N    . HIS   B 1 45  ? 52.494 -19.814 6.870   1.00 12.89 ?  45  HIS   B N    1 
ATOM   4671 C CA   . HIS   B 1 45  ? 52.518 -20.640 5.663   1.00 12.92 ?  45  HIS   B CA   1 
ATOM   4672 C C    . HIS   B 1 45  ? 53.534 -21.764 5.826   1.00 15.22 ?  45  HIS   B C    1 
ATOM   4673 O O    . HIS   B 1 45  ? 54.593 -21.786 5.206   1.00 17.32 ?  45  HIS   B O    1 
ATOM   4674 C CB   . HIS   B 1 45  ? 52.841 -19.785 4.452   1.00 12.77 ?  45  HIS   B CB   1 
ATOM   4675 C CG   . HIS   B 1 45  ? 51.972 -18.582 4.335   1.00 12.41 ?  45  HIS   B CG   1 
ATOM   4676 N ND1  . HIS   B 1 45  ? 50.594 -18.659 4.291   1.00 12.71 ?  45  HIS   B ND1  1 
ATOM   4677 C CD2  . HIS   B 1 45  ? 52.290 -17.268 4.262   1.00 12.99 ?  45  HIS   B CD2  1 
ATOM   4678 C CE1  . HIS   B 1 45  ? 50.109 -17.434 4.178   1.00 12.36 ?  45  HIS   B CE1  1 
ATOM   4679 N NE2  . HIS   B 1 45  ? 51.114 -16.574 4.160   1.00 12.87 ?  45  HIS   B NE2  1 
ATOM   4680 H H    . HIS   B 1 45  ? 53.061 -19.169 6.861   1.00 15.46 ?  45  HIS   B H    1 
ATOM   4681 H HA   . HIS   B 1 45  ? 51.638 -21.033 5.530   1.00 15.49 ?  45  HIS   B HA   1 
ATOM   4682 H HB2  . HIS   B 1 45  ? 53.759 -19.487 4.512   1.00 15.32 ?  45  HIS   B HB2  1 
ATOM   4683 H HB3  . HIS   B 1 45  ? 52.719 -20.322 3.649   1.00 15.32 ?  45  HIS   B HB3  1 
ATOM   4684 H HD2  . HIS   B 1 45  ? 53.146 -16.904 4.275   1.00 15.59 ?  45  HIS   B HD2  1 
ATOM   4685 H HE1  . HIS   B 1 45  ? 49.206 -17.211 4.118   1.00 14.82 ?  45  HIS   B HE1  1 
ATOM   4686 H HE2  . HIS   B 1 45  ? 51.038 -15.717 4.104   1.00 15.43 ?  45  HIS   B HE2  1 
ATOM   4687 N N    A GLY   B 1 46  ? 53.165 -22.732 6.660   0.60 16.55 ?  46  GLY   B N    1 
ATOM   4688 N N    B GLY   B 1 46  ? 53.180 -22.714 6.682   0.40 16.26 ?  46  GLY   B N    1 
ATOM   4689 C CA   A GLY   B 1 46  ? 54.092 -23.778 7.051   0.60 18.16 ?  46  GLY   B CA   1 
ATOM   4690 C CA   B GLY   B 1 46  ? 54.103 -23.777 7.019   0.40 17.45 ?  46  GLY   B CA   1 
ATOM   4691 C C    A GLY   B 1 46  ? 54.139 -25.013 6.173   0.60 19.59 ?  46  GLY   B C    1 
ATOM   4692 C C    B GLY   B 1 46  ? 54.125 -24.923 6.029   0.40 18.69 ?  46  GLY   B C    1 
ATOM   4693 O O    A GLY   B 1 46  ? 55.222 -25.482 5.811   0.60 22.21 ?  46  GLY   B O    1 
ATOM   4694 O O    B GLY   B 1 46  ? 55.159 -25.213 5.418   0.40 20.00 ?  46  GLY   B O    1 
ATOM   4695 H H    A GLY   B 1 46  ? 52.384 -22.791 7.026   0.60 19.85 ?  46  GLY   B H    1 
ATOM   4696 H H    B GLY   B 1 46  ? 52.415 -22.758 7.083   0.40 19.50 ?  46  GLY   B H    1 
ATOM   4697 H HA2  A GLY   B 1 46  ? 54.983 -23.400 7.082   0.60 21.78 ?  46  GLY   B HA2  1 
ATOM   4698 H HA2  B GLY   B 1 46  ? 54.997 -23.409 7.074   0.40 20.93 ?  46  GLY   B HA2  1 
ATOM   4699 H HA3  A GLY   B 1 46  ? 53.861 -24.073 7.944   0.60 21.78 ?  46  GLY   B HA3  1 
ATOM   4700 H HA3  B GLY   B 1 46  ? 53.868 -24.130 7.892   0.40 20.93 ?  46  GLY   B HA3  1 
ATOM   4701 N N    . GLY   B 1 47  ? 52.978 -25.575 5.842   1.00 18.88 ?  47  GLY   B N    1 
ATOM   4702 C CA   . GLY   B 1 47  ? 52.914 -26.847 5.154   1.00 16.74 ?  47  GLY   B CA   1 
ATOM   4703 C C    . GLY   B 1 47  ? 52.017 -26.825 3.932   1.00 14.85 ?  47  GLY   B C    1 
ATOM   4704 O O    . GLY   B 1 47  ? 51.369 -25.824 3.629   1.00 14.55 ?  47  GLY   B O    1 
ATOM   4705 H H    A GLY   B 1 47  ? 52.206 -25.238 6.026   0.60 22.65 ?  47  GLY   B H    1 
ATOM   4706 H H    B GLY   B 1 47  ? 52.211 -25.285 6.109   0.40 22.65 ?  47  GLY   B H    1 
ATOM   4707 H HA2  . GLY   B 1 47  ? 53.799 -27.112 4.868   1.00 20.09 ?  47  GLY   B HA2  1 
ATOM   4708 H HA3  . GLY   B 1 47  ? 52.577 -27.521 5.765   1.00 20.09 ?  47  GLY   B HA3  1 
ATOM   4709 N N    . GLY   B 1 48  ? 51.976 -27.966 3.248   1.00 13.97 ?  48  GLY   B N    1 
ATOM   4710 C CA   . GLY   B 1 48  ? 51.058 -28.116 2.137   1.00 13.76 ?  48  GLY   B CA   1 
ATOM   4711 C C    . GLY   B 1 48  ? 51.197 -27.005 1.124   1.00 12.96 ?  48  GLY   B C    1 
ATOM   4712 O O    . GLY   B 1 48  ? 52.302 -26.548 0.807   1.00 13.49 ?  48  GLY   B O    1 
ATOM   4713 H H    . GLY   B 1 48  ? 52.470 -28.647 3.401   1.00 16.76 ?  48  GLY   B H    1 
ATOM   4714 H HA2  . GLY   B 1 48  ? 51.224 -28.964 1.691   1.00 16.51 ?  48  GLY   B HA2  1 
ATOM   4715 H HA3  . GLY   B 1 48  ? 50.145 -28.117 2.464   1.00 16.51 ?  48  GLY   B HA3  1 
ATOM   4716 N N    . VAL   B 1 49  ? 50.051 -26.571 0.595   1.00 12.99 ?  49  VAL   B N    1 
ATOM   4717 C CA   . VAL   B 1 49  ? 50.033 -25.554 -0.452  1.00 13.02 ?  49  VAL   B CA   1 
ATOM   4718 C C    . VAL   B 1 49  ? 50.694 -24.269 0.031   1.00 12.25 ?  49  VAL   B C    1 
ATOM   4719 O O    . VAL   B 1 49  ? 51.489 -23.652 -0.687  1.00 13.08 ?  49  VAL   B O    1 
ATOM   4720 C CB   . VAL   B 1 49  ? 48.588 -25.303 -0.925  1.00 14.01 ?  49  VAL   B CB   1 
ATOM   4721 C CG1  . VAL   B 1 49  ? 48.510 -24.059 -1.798  1.00 14.31 ?  49  VAL   B CG1  1 
ATOM   4722 C CG2  . VAL   B 1 49  ? 48.050 -26.521 -1.673  1.00 15.74 ?  49  VAL   B CG2  1 
ATOM   4723 H H    . VAL   B 1 49  ? 49.265 -26.846 0.826   1.00 15.59 ?  49  VAL   B H    1 
ATOM   4724 H HA   . VAL   B 1 49  ? 50.535 -25.878 -1.216  1.00 15.61 ?  49  VAL   B HA   1 
ATOM   4725 H HB   . VAL   B 1 49  ? 48.021 -25.158 -0.152  1.00 16.81 ?  49  VAL   B HB   1 
ATOM   4726 H HG11 . VAL   B 1 49  ? 47.676 -24.077 -2.298  1.00 17.16 ?  49  VAL   B HG11 1 
ATOM   4727 H HG12 . VAL   B 1 49  ? 48.532 -23.271 -1.232  1.00 17.16 ?  49  VAL   B HG12 1 
ATOM   4728 H HG13 . VAL   B 1 49  ? 49.260 -24.054 -2.410  1.00 17.16 ?  49  VAL   B HG13 1 
ATOM   4729 H HG21 . VAL   B 1 49  ? 47.139 -26.341 -1.958  1.00 18.88 ?  49  VAL   B HG21 1 
ATOM   4730 H HG22 . VAL   B 1 49  ? 48.610 -26.687 -2.448  1.00 18.88 ?  49  VAL   B HG22 1 
ATOM   4731 H HG23 . VAL   B 1 49  ? 48.067 -27.287 -1.081  1.00 18.88 ?  49  VAL   B HG23 1 
ATOM   4732 N N    . ALA   B 1 50  ? 50.348 -23.824 1.239   1.00 11.91 ?  50  ALA   B N    1 
ATOM   4733 C CA   . ALA   B 1 50  ? 50.873 -22.549 1.721   1.00 11.52 ?  50  ALA   B CA   1 
ATOM   4734 C C    . ALA   B 1 50  ? 52.390 -22.581 1.832   1.00 11.78 ?  50  ALA   B C    1 
ATOM   4735 O O    . ALA   B 1 50  ? 53.072 -21.613 1.473   1.00 12.22 ?  50  ALA   B O    1 
ATOM   4736 C CB   . ALA   B 1 50  ? 50.249 -22.193 3.066   1.00 12.00 ?  50  ALA   B CB   1 
ATOM   4737 H H    . ALA   B 1 50  ? 49.822 -24.225 1.784   1.00 14.28 ?  50  ALA   B H    1 
ATOM   4738 H HA   . ALA   B 1 50  ? 50.643 -21.850 1.091   1.00 13.81 ?  50  ALA   B HA   1 
ATOM   4739 H HB1  . ALA   B 1 50  ? 50.612 -21.343 3.368   1.00 14.39 ?  50  ALA   B HB1  1 
ATOM   4740 H HB2  . ALA   B 1 50  ? 49.289 -22.121 2.959   1.00 14.39 ?  50  ALA   B HB2  1 
ATOM   4741 H HB3  . ALA   B 1 50  ? 50.462 -22.888 3.708   1.00 14.39 ?  50  ALA   B HB3  1 
ATOM   4742 N N    . GLY   B 1 51  ? 52.938 -23.676 2.346   1.00 12.40 ?  51  GLY   B N    1 
ATOM   4743 C CA   . GLY   B 1 51  ? 54.382 -23.780 2.417   1.00 13.32 ?  51  GLY   B CA   1 
ATOM   4744 C C    . GLY   B 1 51  ? 55.027 -23.729 1.048   1.00 12.90 ?  51  GLY   B C    1 
ATOM   4745 O O    . GLY   B 1 51  ? 56.069 -23.093 0.866   1.00 13.94 ?  51  GLY   B O    1 
ATOM   4746 H H    . GLY   B 1 51  ? 52.512 -24.359 2.645   1.00 14.87 ?  51  GLY   B H    1 
ATOM   4747 H HA2  . GLY   B 1 51  ? 54.736 -23.046 2.945   1.00 15.97 ?  51  GLY   B HA2  1 
ATOM   4748 H HA3  . GLY   B 1 51  ? 54.632 -24.614 2.842   1.00 15.97 ?  51  GLY   B HA3  1 
ATOM   4749 N N    . ALA   B 1 52  ? 54.426 -24.398 0.067   1.00 12.76 ?  52  ALA   B N    1 
ATOM   4750 C CA   . ALA   B 1 52  ? 54.986 -24.402 -1.278  1.00 13.03 ?  52  ALA   B CA   1 
ATOM   4751 C C    . ALA   B 1 52  ? 54.910 -23.023 -1.922  1.00 12.46 ?  52  ALA   B C    1 
ATOM   4752 O O    . ALA   B 1 52  ? 55.879 -22.574 -2.552  1.00 13.27 ?  52  ALA   B O    1 
ATOM   4753 C CB   . ALA   B 1 52  ? 54.270 -25.433 -2.142  1.00 13.58 ?  52  ALA   B CB   1 
ATOM   4754 H H    . ALA   B 1 52  ? 53.697 -24.847 0.152   1.00 15.30 ?  52  ALA   B H    1 
ATOM   4755 H HA   . ALA   B 1 52  ? 55.919 -24.649 -1.226  1.00 15.63 ?  52  ALA   B HA   1 
ATOM   4756 H HB1  . ALA   B 1 52  ? 54.659 -25.423 -3.033  1.00 16.29 ?  52  ALA   B HB1  1 
ATOM   4757 H HB2  . ALA   B 1 52  ? 54.390 -26.312 -1.744  1.00 16.29 ?  52  ALA   B HB2  1 
ATOM   4758 H HB3  . ALA   B 1 52  ? 53.329 -25.216 -2.188  1.00 16.29 ?  52  ALA   B HB3  1 
ATOM   4759 N N    . LEU   B 1 53  ? 53.766 -22.343 -1.800  1.00 12.21 ?  53  LEU   B N    1 
ATOM   4760 C CA   . LEU   B 1 53  ? 53.656 -21.004 -2.374  1.00 12.19 ?  53  LEU   B CA   1 
ATOM   4761 C C    . LEU   B 1 53  ? 54.661 -20.062 -1.726  1.00 11.65 ?  53  LEU   B C    1 
ATOM   4762 O O    . LEU   B 1 53  ? 55.364 -19.311 -2.415  1.00 12.72 ?  53  LEU   B O    1 
ATOM   4763 C CB   . LEU   B 1 53  ? 52.233 -20.463 -2.208  1.00 12.76 ?  53  LEU   B CB   1 
ATOM   4764 C CG   . LEU   B 1 53  ? 51.096 -21.186 -2.934  1.00 13.12 ?  53  LEU   B CG   1 
ATOM   4765 C CD1  . LEU   B 1 53  ? 49.756 -20.568 -2.574  1.00 14.64 ?  53  LEU   B CD1  1 
ATOM   4766 C CD2  . LEU   B 1 53  ? 51.292 -21.187 -4.444  1.00 14.79 ?  53  LEU   B CD2  1 
ATOM   4767 H H    . LEU   B 1 53  ? 53.059 -22.622 -1.399  1.00 14.65 ?  53  LEU   B H    1 
ATOM   4768 H HA   . LEU   B 1 53  ? 53.856 -21.049 -3.324  1.00 14.62 ?  53  LEU   B HA   1 
ATOM   4769 H HB2  . LEU   B 1 53  ? 52.018 -20.479 -1.265  1.00 15.31 ?  53  LEU   B HB2  1 
ATOM   4770 H HB3  . LEU   B 1 53  ? 52.225 -19.546 -2.522  1.00 15.31 ?  53  LEU   B HB3  1 
ATOM   4771 H HG   . LEU   B 1 53  ? 51.076 -22.110 -2.641  1.00 15.74 ?  53  LEU   B HG   1 
ATOM   4772 H HD11 . LEU   B 1 53  ? 49.050 -21.046 -3.041  1.00 17.56 ?  53  LEU   B HD11 1 
ATOM   4773 H HD12 . LEU   B 1 53  ? 49.621 -20.644 -1.614  1.00 17.56 ?  53  LEU   B HD12 1 
ATOM   4774 H HD13 . LEU   B 1 53  ? 49.754 -19.636 -2.835  1.00 17.56 ?  53  LEU   B HD13 1 
ATOM   4775 H HD21 . LEU   B 1 53  ? 50.588 -21.715 -4.855  1.00 17.74 ?  53  LEU   B HD21 1 
ATOM   4776 H HD22 . LEU   B 1 53  ? 51.251 -20.276 -4.770  1.00 17.74 ?  53  LEU   B HD22 1 
ATOM   4777 H HD23 . LEU   B 1 53  ? 52.155 -21.577 -4.653  1.00 17.74 ?  53  LEU   B HD23 1 
ATOM   4778 N N    . ASN   B 1 54  ? 54.747 -20.089 -0.398  1.00 11.34 ?  54  ASN   B N    1 
ATOM   4779 C CA   . ASN   B 1 54  ? 55.665 -19.183 0.274   1.00 12.20 ?  54  ASN   B CA   1 
ATOM   4780 C C    . ASN   B 1 54  ? 57.110 -19.468 -0.122  1.00 13.06 ?  54  ASN   B C    1 
ATOM   4781 O O    . ASN   B 1 54  ? 57.891 -18.536 -0.361  1.00 13.30 ?  54  ASN   B O    1 
ATOM   4782 C CB   . ASN   B 1 54  ? 55.500 -19.261 1.783   1.00 12.97 ?  54  ASN   B CB   1 
ATOM   4783 C CG   . ASN   B 1 54  ? 56.474 -18.351 2.496   1.00 13.34 ?  54  ASN   B CG   1 
ATOM   4784 O OD1  . ASN   B 1 54  ? 56.500 -17.139 2.253   1.00 13.61 ?  54  ASN   B OD1  1 
ATOM   4785 N ND2  . ASN   B 1 54  ? 57.310 -18.930 3.352   1.00 15.19 ?  54  ASN   B ND2  1 
ATOM   4786 H H    . ASN   B 1 54  ? 54.299 -20.609 0.118   1.00 13.61 ?  54  ASN   B H    1 
ATOM   4787 H HA   . ASN   B 1 54  ? 55.456 -18.275 0.002   1.00 14.64 ?  54  ASN   B HA   1 
ATOM   4788 H HB2  . ASN   B 1 54  ? 54.599 -18.985 2.022   1.00 15.55 ?  54  ASN   B HB2  1 
ATOM   4789 H HB3  . ASN   B 1 54  ? 55.660 -20.170 2.077   1.00 15.55 ?  54  ASN   B HB3  1 
ATOM   4790 H HD21 . ASN   B 1 54  ? 57.890 -18.457 3.778   1.00 18.22 ?  54  ASN   B HD21 1 
ATOM   4791 H HD22 . ASN   B 1 54  ? 57.273 -19.780 3.485   1.00 18.22 ?  54  ASN   B HD22 1 
ATOM   4792 N N    . LYS   B 1 55  ? 57.493 -20.747 -0.186  1.00 13.65 ?  55  LYS   B N    1 
ATOM   4793 C CA   . LYS   B 1 55  ? 58.847 -21.089 -0.605  1.00 14.51 ?  55  LYS   B CA   1 
ATOM   4794 C C    . LYS   B 1 55  ? 59.140 -20.544 -1.996  1.00 14.39 ?  55  LYS   B C    1 
ATOM   4795 O O    . LYS   B 1 55  ? 60.240 -20.040 -2.252  1.00 15.06 ?  55  LYS   B O    1 
ATOM   4796 C CB   . LYS   B 1 55  ? 59.038 -22.605 -0.558  1.00 16.38 ?  55  LYS   B CB   1 
ATOM   4797 C CG   . LYS   B 1 55  ? 60.415 -23.072 -0.991  1.00 20.66 ?  55  LYS   B CG   1 
ATOM   4798 C CD   . LYS   B 1 55  ? 60.580 -24.571 -0.807  1.00 24.16 ?  55  LYS   B CD   1 
ATOM   4799 C CE   . LYS   B 1 55  ? 60.654 -24.964 0.668   1.00 27.27 ?  55  LYS   B CE   1 
ATOM   4800 N NZ   . LYS   B 1 55  ? 60.998 -26.398 0.846   1.00 28.78 ?  55  LYS   B NZ   1 
ATOM   4801 H H    . LYS   B 1 55  ? 56.984 -21.418 -0.004  1.00 16.37 ?  55  LYS   B H    1 
ATOM   4802 H HA   . LYS   B 1 55  ? 59.473 -20.685 0.011   1.00 17.40 ?  55  LYS   B HA   1 
ATOM   4803 H HB2  . LYS   B 1 55  ? 58.895 -22.901 0.356   1.00 19.64 ?  55  LYS   B HB2  1 
ATOM   4804 H HB3  . LYS   B 1 55  ? 58.387 -23.021 -1.142  1.00 19.64 ?  55  LYS   B HB3  1 
ATOM   4805 H HG2  . LYS   B 1 55  ? 60.543 -22.866 -1.931  1.00 24.79 ?  55  LYS   B HG2  1 
ATOM   4806 H HG3  . LYS   B 1 55  ? 61.089 -22.622 -0.456  1.00 24.79 ?  55  LYS   B HG3  1 
ATOM   4807 H HD2  . LYS   B 1 55  ? 59.821 -25.030 -1.201  1.00 28.99 ?  55  LYS   B HD2  1 
ATOM   4808 H HD3  . LYS   B 1 55  ? 61.403 -24.860 -1.234  1.00 28.99 ?  55  LYS   B HD3  1 
ATOM   4809 H HE2  . LYS   B 1 55  ? 61.337 -24.426 1.104   1.00 32.72 ?  55  LYS   B HE2  1 
ATOM   4810 H HE3  . LYS   B 1 55  ? 59.791 -24.801 1.083   1.00 32.72 ?  55  LYS   B HE3  1 
ATOM   4811 H HZ1  . LYS   B 1 55  ? 60.994 -26.604 1.712   1.00 34.53 ?  55  LYS   B HZ1  1 
ATOM   4812 H HZ2  . LYS   B 1 55  ? 60.400 -26.904 0.425   1.00 34.53 ?  55  LYS   B HZ2  1 
ATOM   4813 H HZ3  . LYS   B 1 55  ? 61.804 -26.560 0.512   1.00 34.53 ?  55  LYS   B HZ3  1 
ATOM   4814 N N    . ALA   B 1 56  ? 58.167 -20.628 -2.909  1.00 13.78 ?  56  ALA   B N    1 
ATOM   4815 C CA   . ALA   B 1 56  ? 58.390 -20.126 -4.259  1.00 14.69 ?  56  ALA   B CA   1 
ATOM   4816 C C    . ALA   B 1 56  ? 58.668 -18.629 -4.259  1.00 14.42 ?  56  ALA   B C    1 
ATOM   4817 O O    . ALA   B 1 56  ? 59.408 -18.136 -5.120  1.00 15.40 ?  56  ALA   B O    1 
ATOM   4818 C CB   . ALA   B 1 56  ? 57.194 -20.455 -5.151  1.00 15.63 ?  56  ALA   B CB   1 
ATOM   4819 H H    . ALA   B 1 56  ? 57.381 -20.954 -2.771  1.00 16.53 ?  56  ALA   B H    1 
ATOM   4820 H HA   . ALA   B 1 56  ? 59.166 -20.562 -4.630  1.00 17.62 ?  56  ALA   B HA   1 
ATOM   4821 H HB1  . ALA   B 1 56  ? 57.364 -20.119 -6.047  1.00 18.75 ?  56  ALA   B HB1  1 
ATOM   4822 H HB2  . ALA   B 1 56  ? 57.077 -21.417 -5.177  1.00 18.75 ?  56  ALA   B HB2  1 
ATOM   4823 H HB3  . ALA   B 1 56  ? 56.399 -20.034 -4.788  1.00 18.75 ?  56  ALA   B HB3  1 
ATOM   4824 N N    . THR   B 1 57  ? 58.103 -17.894 -3.300  1.00 14.12 ?  57  THR   B N    1 
ATOM   4825 C CA   . THR   B 1 57  ? 58.346 -16.460 -3.186  1.00 14.00 ?  57  THR   B CA   1 
ATOM   4826 C C    . THR   B 1 57  ? 59.593 -16.134 -2.373  1.00 14.84 ?  57  THR   B C    1 
ATOM   4827 O O    . THR   B 1 57  ? 59.830 -14.959 -2.064  1.00 15.16 ?  57  THR   B O    1 
ATOM   4828 C CB   . THR   B 1 57  ? 57.150 -15.731 -2.552  1.00 13.20 ?  57  THR   B CB   1 
ATOM   4829 O OG1  . THR   B 1 57  ? 57.131 -15.950 -1.135  1.00 13.61 ?  57  THR   B OG1  1 
ATOM   4830 C CG2  . THR   B 1 57  ? 55.826 -16.151 -3.184  1.00 13.66 ?  57  THR   B CG2  1 
ATOM   4831 H H    . THR   B 1 57  ? 57.560 -18.201 -2.705  1.00 16.94 ?  57  THR   B H    1 
ATOM   4832 H HA   . THR   B 1 57  ? 58.465 -16.095 -4.078  1.00 16.79 ?  57  THR   B HA   1 
ATOM   4833 H HB   . THR   B 1 57  ? 57.253 -14.779 -2.716  1.00 15.84 ?  57  THR   B HB   1 
ATOM   4834 H HG1  . THR   B 1 57  ? 57.061 -16.771 -0.976  1.00 16.33 ?  57  THR   B HG1  1 
ATOM   4835 H HG21 . THR   B 1 57  ? 55.104 -15.601 -2.842  1.00 16.38 ?  57  THR   B HG21 1 
ATOM   4836 H HG22 . THR   B 1 57  ? 55.869 -16.050 -4.149  1.00 16.38 ?  57  THR   B HG22 1 
ATOM   4837 H HG23 . THR   B 1 57  ? 55.638 -17.079 -2.976  1.00 16.38 ?  57  THR   B HG23 1 
ATOM   4838 N N    . ASN   B 1 58  ? 60.383 -17.140 -2.008  1.00 15.90 ?  58  ASN   B N    1 
ATOM   4839 C CA   . ASN   B 1 58  ? 61.583 -16.926 -1.202  1.00 18.72 ?  58  ASN   B CA   1 
ATOM   4840 C C    . ASN   B 1 58  ? 61.246 -16.218 0.111   1.00 16.10 ?  58  ASN   B C    1 
ATOM   4841 O O    . ASN   B 1 58  ? 61.983 -15.346 0.581   1.00 17.09 ?  58  ASN   B O    1 
ATOM   4842 C CB   . ASN   B 1 58  ? 62.669 -16.178 -1.982  1.00 27.94 ?  58  ASN   B CB   1 
ATOM   4843 C CG   . ASN   B 1 58  ? 64.038 -16.309 -1.342  1.00 38.29 ?  58  ASN   B CG   1 
ATOM   4844 O OD1  . ASN   B 1 58  ? 64.336 -17.307 -0.687  1.00 40.42 ?  58  ASN   B OD1  1 
ATOM   4845 N ND2  . ASN   B 1 58  ? 64.878 -15.296 -1.528  1.00 43.73 ?  58  ASN   B ND2  1 
ATOM   4846 H H    . ASN   B 1 58  ? 60.245 -17.966 -2.219  1.00 19.08 ?  58  ASN   B H    1 
ATOM   4847 H HA   . ASN   B 1 58  ? 61.946 -17.800 -0.982  1.00 22.46 ?  58  ASN   B HA   1 
ATOM   4848 H HB2  . ASN   B 1 58  ? 62.724 -16.540 -2.884  1.00 33.52 ?  58  ASN   B HB2  1 
ATOM   4849 H HB3  . ASN   B 1 58  ? 62.446 -15.237 -2.018  1.00 33.52 ?  58  ASN   B HB3  1 
ATOM   4850 H HD21 . ASN   B 1 58  ? 65.667 -15.323 -1.186  1.00 52.47 ?  58  ASN   B HD21 1 
ATOM   4851 H HD22 . ASN   B 1 58  ? 64.632 -14.614 -1.990  1.00 52.47 ?  58  ASN   B HD22 1 
ATOM   4852 N N    . ASN   B 1 59  ? 60.121 -16.604 0.713   1.00 15.05 ?  59  ASN   B N    1 
ATOM   4853 C CA   . ASN   B 1 59  ? 59.644 -16.127 2.012   1.00 14.84 ?  59  ASN   B CA   1 
ATOM   4854 C C    . ASN   B 1 59  ? 59.052 -14.717 1.953   1.00 14.44 ?  59  ASN   B C    1 
ATOM   4855 O O    . ASN   B 1 59  ? 58.621 -14.212 2.993   1.00 14.74 ?  59  ASN   B O    1 
ATOM   4856 C CB   . ASN   B 1 59  ? 60.715 -16.193 3.117   1.00 16.04 ?  59  ASN   B CB   1 
ATOM   4857 C CG   . ASN   B 1 59  ? 60.124 -16.364 4.497   1.00 17.23 ?  59  ASN   B CG   1 
ATOM   4858 O OD1  . ASN   B 1 59  ? 59.298 -17.251 4.724   1.00 17.39 ?  59  ASN   B OD1  1 
ATOM   4859 N ND2  . ASN   B 1 59  ? 60.543 -15.519 5.432   1.00 18.36 ?  59  ASN   B ND2  1 
ATOM   4860 H H    . ASN   B 1 59  ? 59.586 -17.189 0.367   1.00 18.05 ?  59  ASN   B H    1 
ATOM   4861 H HA   . ASN   B 1 59  ? 58.932 -16.722 2.292   1.00 17.80 ?  59  ASN   B HA   1 
ATOM   4862 H HB2  . ASN   B 1 59  ? 61.300 -16.951 2.957   1.00 19.24 ?  59  ASN   B HB2  1 
ATOM   4863 H HB3  . ASN   B 1 59  ? 61.225 -15.372 3.119   1.00 19.24 ?  59  ASN   B HB3  1 
ATOM   4864 H HD21 . ASN   B 1 59  ? 60.234 -15.571 6.235   1.00 22.03 ?  59  ASN   B HD21 1 
ATOM   4865 H HD22 . ASN   B 1 59  ? 61.117 -14.911 5.233   1.00 22.03 ?  59  ASN   B HD22 1 
ATOM   4866 N N    . ALA   B 1 60  ? 58.992 -14.076 0.783   1.00 14.06 ?  60  ALA   B N    1 
ATOM   4867 C CA   . ALA   B 1 60  ? 58.396 -12.743 0.706   1.00 14.09 ?  60  ALA   B CA   1 
ATOM   4868 C C    . ALA   B 1 60  ? 56.928 -12.767 1.112   1.00 13.49 ?  60  ALA   B C    1 
ATOM   4869 O O    . ALA   B 1 60  ? 56.426 -11.816 1.726   1.00 14.07 ?  60  ALA   B O    1 
ATOM   4870 C CB   . ALA   B 1 60  ? 58.546 -12.180 -0.706  1.00 15.23 ?  60  ALA   B CB   1 
ATOM   4871 H H    . ALA   B 1 60  ? 59.292 -14.388 0.039   1.00 16.86 ?  60  ALA   B H    1 
ATOM   4872 H HA   . ALA   B 1 60  ? 58.866 -12.158 1.317   1.00 16.90 ?  60  ALA   B HA   1 
ATOM   4873 H HB1  . ALA   B 1 60  ? 58.146 -11.301 -0.735  1.00 18.27 ?  60  ALA   B HB1  1 
ATOM   4874 H HB2  . ALA   B 1 60  ? 59.491 -12.125 -0.925  1.00 18.27 ?  60  ALA   B HB2  1 
ATOM   4875 H HB3  . ALA   B 1 60  ? 58.098 -12.773 -1.331  1.00 18.27 ?  60  ALA   B HB3  1 
ATOM   4876 N N    . MET   B 1 61  ? 56.218 -13.843 0.768   1.00 12.98 ?  61  MET   B N    1 
ATOM   4877 C CA   . MET   B 1 61  ? 54.823 -13.966 1.161   1.00 12.41 ?  61  MET   B CA   1 
ATOM   4878 C C    . MET   B 1 61  ? 54.684 -13.970 2.682   1.00 12.69 ?  61  MET   B C    1 
ATOM   4879 O O    . MET   B 1 61  ? 53.781 -13.329 3.233   1.00 12.69 ?  61  MET   B O    1 
ATOM   4880 C CB   . MET   B 1 61  ? 54.242 -15.236 0.534   1.00 12.73 ?  61  MET   B CB   1 
ATOM   4881 C CG   . MET   B 1 61  ? 52.805 -15.525 0.940   1.00 12.44 ?  61  MET   B CG   1 
ATOM   4882 S SD   . MET   B 1 61  ? 52.163 -17.031 0.181   1.00 13.25 ?  61  MET   B SD   1 
ATOM   4883 C CE   . MET   B 1 61  ? 51.903 -16.450 -1.494  1.00 14.19 ?  61  MET   B CE   1 
ATOM   4884 H H    . MET   B 1 61  ? 56.520 -14.513 0.309   1.00 15.57 ?  61  MET   B H    1 
ATOM   4885 H HA   . MET   B 1 61  ? 54.329 -13.214 0.802   1.00 14.88 ?  61  MET   B HA   1 
ATOM   4886 H HB2  . MET   B 1 61  ? 54.260 -15.148 -0.434  1.00 15.28 ?  61  MET   B HB2  1 
ATOM   4887 H HB3  . MET   B 1 61  ? 54.781 -15.997 0.801   1.00 15.28 ?  61  MET   B HB3  1 
ATOM   4888 H HG2  . MET   B 1 61  ? 52.758 -15.642 1.902   1.00 14.92 ?  61  MET   B HG2  1 
ATOM   4889 H HG3  . MET   B 1 61  ? 52.240 -14.786 0.667   1.00 14.92 ?  61  MET   B HG3  1 
ATOM   4890 H HE1  . MET   B 1 61  ? 51.522 -17.167 -2.024  1.00 17.02 ?  61  MET   B HE1  1 
ATOM   4891 H HE2  . MET   B 1 61  ? 51.295 -15.692 -1.478  1.00 17.02 ?  61  MET   B HE2  1 
ATOM   4892 H HE3  . MET   B 1 61  ? 52.756 -16.178 -1.871  1.00 17.02 ?  61  MET   B HE3  1 
ATOM   4893 N N    . GLN   B 1 62  ? 55.563 -14.690 3.382   1.00 12.54 ?  62  GLN   B N    1 
ATOM   4894 C CA   . GLN   B 1 62  ? 55.451 -14.752 4.836   1.00 13.07 ?  62  GLN   B CA   1 
ATOM   4895 C C    . GLN   B 1 62  ? 55.735 -13.400 5.473   1.00 13.26 ?  62  GLN   B C    1 
ATOM   4896 O O    . GLN   B 1 62  ? 55.048 -12.996 6.420   1.00 13.86 ?  62  GLN   B O    1 
ATOM   4897 C CB   . GLN   B 1 62  ? 56.402 -15.808 5.397   1.00 13.37 ?  62  GLN   B CB   1 
ATOM   4898 C CG   . GLN   B 1 62  ? 56.181 -16.075 6.872   1.00 13.57 ?  62  GLN   B CG   1 
ATOM   4899 C CD   . GLN   B 1 62  ? 54.806 -16.668 7.118   1.00 13.10 ?  62  GLN   B CD   1 
ATOM   4900 O OE1  . GLN   B 1 62  ? 54.551 -17.819 6.770   1.00 13.58 ?  62  GLN   B OE1  1 
ATOM   4901 N NE2  . GLN   B 1 62  ? 53.900 -15.878 7.682   1.00 13.61 ?  62  GLN   B NE2  1 
ATOM   4902 H H    . GLN   B 1 62  ? 56.212 -15.144 3.044   1.00 15.04 ?  62  GLN   B H    1 
ATOM   4903 H HA   . GLN   B 1 62  ? 54.544 -15.010 5.066   1.00 15.67 ?  62  GLN   B HA   1 
ATOM   4904 H HB2  . GLN   B 1 62  ? 56.271 -16.643 4.918   1.00 16.03 ?  62  GLN   B HB2  1 
ATOM   4905 H HB3  . GLN   B 1 62  ? 57.317 -15.503 5.281   1.00 16.03 ?  62  GLN   B HB3  1 
ATOM   4906 H HG2  . GLN   B 1 62  ? 56.846 -16.709 7.186   1.00 16.27 ?  62  GLN   B HG2  1 
ATOM   4907 H HG3  . GLN   B 1 62  ? 56.249 -15.245 7.366   1.00 16.27 ?  62  GLN   B HG3  1 
ATOM   4908 H HE21 . GLN   B 1 62  ? 54.110 -15.076 7.905   1.00 16.32 ?  62  GLN   B HE21 1 
ATOM   4909 H HE22 . GLN   B 1 62  ? 53.107 -16.175 7.835   1.00 16.32 ?  62  GLN   B HE22 1 
ATOM   4910 N N    . VAL   B 1 63  ? 56.755 -12.692 4.984   1.00 13.81 ?  63  VAL   B N    1 
ATOM   4911 C CA   . VAL   B 1 63  ? 57.063 -11.374 5.535   1.00 14.65 ?  63  VAL   B CA   1 
ATOM   4912 C C    . VAL   B 1 63  ? 55.872 -10.439 5.352   1.00 13.82 ?  63  VAL   B C    1 
ATOM   4913 O O    . VAL   B 1 63  ? 55.457 -9.737  6.284   1.00 14.21 ?  63  VAL   B O    1 
ATOM   4914 C CB   . VAL   B 1 63  ? 58.357 -10.820 4.911   1.00 16.08 ?  63  VAL   B CB   1 
ATOM   4915 C CG1  . VAL   B 1 63  ? 58.582 -9.382  5.346   1.00 17.05 ?  63  VAL   B CG1  1 
ATOM   4916 C CG2  . VAL   B 1 63  ? 59.541 -11.695 5.319   1.00 16.60 ?  63  VAL   B CG2  1 
ATOM   4917 H H    . VAL   B 1 63  ? 57.266 -12.946 4.338   1.00 16.56 ?  63  VAL   B H    1 
ATOM   4918 H HA   . VAL   B 1 63  ? 57.218 -11.472 6.482   1.00 17.57 ?  63  VAL   B HA   1 
ATOM   4919 H HB   . VAL   B 1 63  ? 58.291 -10.846 3.943   1.00 19.29 ?  63  VAL   B HB   1 
ATOM   4920 H HG11 . VAL   B 1 63  ? 59.502 -9.139  5.160   1.00 20.45 ?  63  VAL   B HG11 1 
ATOM   4921 H HG12 . VAL   B 1 63  ? 57.981 -8.808  4.852   1.00 20.45 ?  63  VAL   B HG12 1 
ATOM   4922 H HG13 . VAL   B 1 63  ? 58.408 -9.314  6.297   1.00 20.45 ?  63  VAL   B HG13 1 
ATOM   4923 H HG21 . VAL   B 1 63  ? 60.356 -11.330 4.937   1.00 19.91 ?  63  VAL   B HG21 1 
ATOM   4924 H HG22 . VAL   B 1 63  ? 59.610 -11.702 6.290   1.00 19.91 ?  63  VAL   B HG22 1 
ATOM   4925 H HG23 . VAL   B 1 63  ? 59.403 -12.599 4.995   1.00 19.91 ?  63  VAL   B HG23 1 
ATOM   4926 N N    . GLU   B 1 64  ? 55.305 -10.419 4.145   1.00 13.41 ?  64  GLU   B N    1 
ATOM   4927 C CA   . GLU   B 1 64  ? 54.134 -9.588  3.873   1.00 13.38 ?  64  GLU   B CA   1 
ATOM   4928 C C    . GLU   B 1 64  ? 52.955 -9.990  4.753   1.00 12.85 ?  64  GLU   B C    1 
ATOM   4929 O O    . GLU   B 1 64  ? 52.211 -9.131  5.259   1.00 13.30 ?  64  GLU   B O    1 
ATOM   4930 C CB   . GLU   B 1 64  ? 53.774 -9.740  2.396   1.00 13.23 ?  64  GLU   B CB   1 
ATOM   4931 C CG   . GLU   B 1 64  ? 52.516 -8.996  1.962   1.00 13.71 ?  64  GLU   B CG   1 
ATOM   4932 C CD   . GLU   B 1 64  ? 51.981 -9.497  0.628   1.00 14.19 ?  64  GLU   B CD   1 
ATOM   4933 O OE1  . GLU   B 1 64  ? 52.164 -10.704 0.308   1.00 15.09 ?  64  GLU   B OE1  1 
ATOM   4934 O OE2  . GLU   B 1 64  ? 51.348 -8.687  -0.094  1.00 14.91 -1 64  GLU   B OE2  1 
ATOM   4935 H H    . GLU   B 1 64  ? 55.583 -10.873 3.465   1.00 16.08 ?  64  GLU   B H    1 
ATOM   4936 H HA   . GLU   B 1 64  ? 54.346 -8.657  4.046   1.00 16.06 ?  64  GLU   B HA   1 
ATOM   4937 H HB2  . GLU   B 1 64  ? 54.508 -9.392  1.857   1.00 15.87 ?  64  GLU   B HB2  1 
ATOM   4938 H HB3  . GLU   B 1 64  ? 53.642 -10.675 2.201   1.00 15.87 ?  64  GLU   B HB3  1 
ATOM   4939 H HG2  . GLU   B 1 64  ? 51.816 -9.117  2.626   1.00 16.44 ?  64  GLU   B HG2  1 
ATOM   4940 H HG3  . GLU   B 1 64  ? 52.718 -8.051  1.869   1.00 16.44 ?  64  GLU   B HG3  1 
ATOM   4941 N N    . SER   B 1 65  ? 52.775 -11.296 4.941   1.00 12.51 ?  65  SER   B N    1 
ATOM   4942 C CA   . SER   B 1 65  ? 51.663 -11.803 5.736   1.00 12.53 ?  65  SER   B CA   1 
ATOM   4943 C C    . SER   B 1 65  ? 51.794 -11.403 7.199   1.00 12.99 ?  65  SER   B C    1 
ATOM   4944 O O    . SER   B 1 65  ? 50.794 -11.036 7.833   1.00 13.16 ?  65  SER   B O    1 
ATOM   4945 C CB   . SER   B 1 65  ? 51.577 -13.325 5.603   1.00 12.59 ?  65  SER   B CB   1 
ATOM   4946 O OG   . SER   B 1 65  ? 51.232 -13.714 4.281   1.00 13.00 ?  65  SER   B OG   1 
ATOM   4947 H H    . SER   B 1 65  ? 53.285 -11.915 4.621   1.00 15.00 ?  65  SER   B H    1 
ATOM   4948 H HA   . SER   B 1 65  ? 50.834 -11.428 5.400   1.00 15.03 ?  65  SER   B HA   1 
ATOM   4949 H HB2  . SER   B 1 65  ? 52.434 -13.712 5.829   1.00 15.11 ?  65  SER   B HB2  1 
ATOM   4950 H HB3  . SER   B 1 65  ? 50.895 -13.655 6.214   1.00 15.11 ?  65  SER   B HB3  1 
ATOM   4951 H HG   . SER   B 1 65  ? 51.810 -13.423 3.739   1.00 15.60 ?  65  SER   B HG   1 
ATOM   4952 N N    . ASP   B 1 66  ? 53.002 -11.502 7.766   1.00 13.22 ?  66  ASP   B N    1 
ATOM   4953 C CA   . ASP   B 1 66  ? 53.188 -11.117 9.161   1.00 13.41 ?  66  ASP   B CA   1 
ATOM   4954 C C    . ASP   B 1 66  ? 52.875 -9.639  9.364   1.00 13.58 ?  66  ASP   B C    1 
ATOM   4955 O O    . ASP   B 1 66  ? 52.299 -9.248  10.387  1.00 13.99 ?  66  ASP   B O    1 
ATOM   4956 C CB   . ASP   B 1 66  ? 54.620 -11.428 9.603   1.00 14.77 ?  66  ASP   B CB   1 
ATOM   4957 C CG   . ASP   B 1 66  ? 54.882 -12.919 9.770   1.00 16.61 ?  66  ASP   B CG   1 
ATOM   4958 O OD1  . ASP   B 1 66  ? 53.925 -13.723 9.702   1.00 17.42 ?  66  ASP   B OD1  1 
ATOM   4959 O OD2  . ASP   B 1 66  ? 56.059 -13.291 9.980   1.00 19.32 -1 66  ASP   B OD2  1 
ATOM   4960 H H    . ASP   B 1 66  ? 53.707 -11.795 7.373   1.00 15.86 ?  66  ASP   B H    1 
ATOM   4961 H HA   . ASP   B 1 66  ? 52.585 -11.630 9.721   1.00 16.08 ?  66  ASP   B HA   1 
ATOM   4962 H HB2  . ASP   B 1 66  ? 55.239 -11.093 8.936   1.00 17.71 ?  66  ASP   B HB2  1 
ATOM   4963 H HB3  . ASP   B 1 66  ? 54.790 -10.997 10.457  1.00 17.71 ?  66  ASP   B HB3  1 
ATOM   4964 N N    . ASP   B 1 67  ? 53.256 -8.796  8.404   1.00 13.22 ?  67  ASP   B N    1 
ATOM   4965 C CA   . ASP   B 1 67  ? 52.909 -7.385  8.489   1.00 13.78 ?  67  ASP   B CA   1 
ATOM   4966 C C    . ASP   B 1 67  ? 51.398 -7.176  8.399   1.00 14.01 ?  67  ASP   B C    1 
ATOM   4967 O O    . ASP   B 1 67  ? 50.835 -6.362  9.141   1.00 14.70 ?  67  ASP   B O    1 
ATOM   4968 C CB   . ASP   B 1 67  ? 53.630 -6.617  7.391   1.00 15.25 ?  67  ASP   B CB   1 
ATOM   4969 C CG   . ASP   B 1 67  ? 53.204 -5.176  7.343   1.00 16.87 ?  67  ASP   B CG   1 
ATOM   4970 O OD1  . ASP   B 1 67  ? 53.683 -4.369  8.171   1.00 18.09 ?  67  ASP   B OD1  1 
ATOM   4971 O OD2  . ASP   B 1 67  ? 52.355 -4.869  6.496   1.00 17.79 -1 67  ASP   B OD2  1 
ATOM   4972 H H    . ASP   B 1 67  ? 53.712 -9.018  7.708   1.00 15.86 ?  67  ASP   B H    1 
ATOM   4973 H HA   . ASP   B 1 67  ? 53.209 -7.039  9.342   1.00 16.53 ?  67  ASP   B HA   1 
ATOM   4974 H HB2  . ASP   B 1 67  ? 54.588 -6.649  7.556   1.00 18.29 ?  67  ASP   B HB2  1 
ATOM   4975 H HB3  . ASP   B 1 67  ? 53.433 -7.029  6.531   1.00 18.29 ?  67  ASP   B HB3  1 
ATOM   4976 N N    . TYR   B 1 68  ? 50.721 -7.904  7.503   1.00 13.95 ?  68  TYR   B N    1 
ATOM   4977 C CA   . TYR   B 1 68  ? 49.264 -7.823  7.432   1.00 14.44 ?  68  TYR   B CA   1 
ATOM   4978 C C    . TYR   B 1 68  ? 48.629 -8.168  8.775   1.00 14.20 ?  68  TYR   B C    1 
ATOM   4979 O O    . TYR   B 1 68  ? 47.694 -7.493  9.223   1.00 15.00 ?  68  TYR   B O    1 
ATOM   4980 C CB   . TYR   B 1 68  ? 48.726 -8.755  6.338   1.00 15.16 ?  68  TYR   B CB   1 
ATOM   4981 C CG   . TYR   B 1 68  ? 47.222 -8.903  6.398   1.00 16.50 ?  68  TYR   B CG   1 
ATOM   4982 C CD1  . TYR   B 1 68  ? 46.631 -9.855  7.224   1.00 17.35 ?  68  TYR   B CD1  1 
ATOM   4983 C CD2  . TYR   B 1 68  ? 46.394 -8.077  5.660   1.00 17.82 ?  68  TYR   B CD2  1 
ATOM   4984 C CE1  . TYR   B 1 68  ? 45.269 -9.981  7.310   1.00 18.82 ?  68  TYR   B CE1  1 
ATOM   4985 C CE2  . TYR   B 1 68  ? 45.013 -8.202  5.735   1.00 18.55 ?  68  TYR   B CE2  1 
ATOM   4986 C CZ   . TYR   B 1 68  ? 44.471 -9.153  6.564   1.00 18.94 ?  68  TYR   B CZ   1 
ATOM   4987 O OH   . TYR   B 1 68  ? 43.103 -9.276  6.653   1.00 20.47 ?  68  TYR   B OH   1 
ATOM   4988 H H    . TYR   B 1 68  ? 51.081 -8.450  6.934   1.00 16.74 ?  68  TYR   B H    1 
ATOM   4989 H HA   . TYR   B 1 68  ? 49.014 -6.917  7.203   1.00 17.33 ?  68  TYR   B HA   1 
ATOM   4990 H HB2  . TYR   B 1 68  ? 48.954 -8.392  5.468   1.00 18.18 ?  68  TYR   B HB2  1 
ATOM   4991 H HB3  . TYR   B 1 68  ? 49.119 -9.635  6.444   1.00 18.18 ?  68  TYR   B HB3  1 
ATOM   4992 H HD1  . TYR   B 1 68  ? 47.169 -10.420 7.732   1.00 20.81 ?  68  TYR   B HD1  1 
ATOM   4993 H HD2  . TYR   B 1 68  ? 46.765 -7.430  5.111   1.00 21.37 ?  68  TYR   B HD2  1 
ATOM   4994 H HE1  . TYR   B 1 68  ? 44.886 -10.631 7.862   1.00 22.58 ?  68  TYR   B HE1  1 
ATOM   4995 H HE2  . TYR   B 1 68  ? 44.455 -7.643  5.241   1.00 22.25 ?  68  TYR   B HE2  1 
ATOM   4996 H HH   . TYR   B 1 68  ? 42.712 -8.722  6.147   1.00 24.56 ?  68  TYR   B HH   1 
ATOM   4997 N N    . ILE   B 1 69  ? 49.107 -9.236  9.419   1.00 13.95 ?  69  ILE   B N    1 
ATOM   4998 C CA   . ILE   B 1 69  ? 48.547 -9.668  10.697  1.00 14.54 ?  69  ILE   B CA   1 
ATOM   4999 C C    . ILE   B 1 69  ? 48.801 -8.629  11.782  1.00 14.33 ?  69  ILE   B C    1 
ATOM   5000 O O    . ILE   B 1 69  ? 47.931 -8.358  12.617  1.00 14.67 ?  69  ILE   B O    1 
ATOM   5001 C CB   . ILE   B 1 69  ? 49.124 -11.042 11.084  1.00 15.51 ?  69  ILE   B CB   1 
ATOM   5002 C CG1  . ILE   B 1 69  ? 48.590 -12.144 10.160  1.00 15.56 ?  69  ILE   B CG1  1 
ATOM   5003 C CG2  . ILE   B 1 69  ? 48.838 -11.355 12.547  1.00 16.41 ?  69  ILE   B CG2  1 
ATOM   5004 C CD1  . ILE   B 1 69  ? 47.113 -12.455 10.320  1.00 15.89 ?  69  ILE   B CD1  1 
ATOM   5005 H H    . ILE   B 1 69  ? 49.757 -9.723  9.138   1.00 16.74 ?  69  ILE   B H    1 
ATOM   5006 H HA   . ILE   B 1 69  ? 47.590 -9.765  10.599  1.00 17.45 ?  69  ILE   B HA   1 
ATOM   5007 H HB   . ILE   B 1 69  ? 50.089 -11.003 10.973  1.00 18.60 ?  69  ILE   B HB   1 
ATOM   5008 H HG12 . ILE   B 1 69  ? 48.736 -11.868 9.241   1.00 18.67 ?  69  ILE   B HG12 1 
ATOM   5009 H HG13 . ILE   B 1 69  ? 49.086 -12.959 10.336  1.00 18.67 ?  69  ILE   B HG13 1 
ATOM   5010 H HG21 . ILE   B 1 69  ? 48.966 -12.306 12.693  1.00 19.68 ?  69  ILE   B HG21 1 
ATOM   5011 H HG22 . ILE   B 1 69  ? 49.453 -10.854 13.107  1.00 19.68 ?  69  ILE   B HG22 1 
ATOM   5012 H HG23 . ILE   B 1 69  ? 47.924 -11.110 12.750  1.00 19.68 ?  69  ILE   B HG23 1 
ATOM   5013 H HD11 . ILE   B 1 69  ? 46.880 -13.171 9.709   1.00 19.07 ?  69  ILE   B HD11 1 
ATOM   5014 H HD12 . ILE   B 1 69  ? 46.946 -12.734 11.233  1.00 19.07 ?  69  ILE   B HD12 1 
ATOM   5015 H HD13 . ILE   B 1 69  ? 46.597 -11.663 10.113  1.00 19.07 ?  69  ILE   B HD13 1 
ATOM   5016 N N    . ALA   B 1 70  ? 49.997 -8.045  11.808  1.00 14.43 ?  70  ALA   B N    1 
ATOM   5017 C CA   . ALA   B 1 70  ? 50.276 -7.006  12.794  1.00 13.92 ?  70  ALA   B CA   1 
ATOM   5018 C C    . ALA   B 1 70  ? 49.275 -5.863  12.683  1.00 14.53 ?  70  ALA   B C    1 
ATOM   5019 O O    . ALA   B 1 70  ? 48.820 -5.323  13.696  1.00 15.02 ?  70  ALA   B O    1 
ATOM   5020 C CB   . ALA   B 1 70  ? 51.702 -6.490  12.613  1.00 14.42 ?  70  ALA   B CB   1 
ATOM   5021 H H    . ALA   B 1 70  ? 50.644 -8.229  11.282  1.00 17.31 ?  70  ALA   B H    1 
ATOM   5022 H HA   . ALA   B 1 70  ? 50.206 -7.384  13.686  1.00 16.69 ?  70  ALA   B HA   1 
ATOM   5023 H HB1  . ALA   B 1 70  ? 51.891 -5.828  13.298  1.00 17.30 ?  70  ALA   B HB1  1 
ATOM   5024 H HB2  . ALA   B 1 70  ? 52.322 -7.232  12.693  1.00 17.30 ?  70  ALA   B HB2  1 
ATOM   5025 H HB3  . ALA   B 1 70  ? 51.785 -6.086  11.733  1.00 17.30 ?  70  ALA   B HB3  1 
ATOM   5026 N N    . THR   B 1 71  ? 48.912 -5.489  11.460  1.00 14.78 ?  71  THR   B N    1 
ATOM   5027 C CA   . THR   B 1 71  ? 48.018 -4.354  11.258  1.00 15.61 ?  71  THR   B CA   1 
ATOM   5028 C C    . THR   B 1 71  ? 46.551 -4.728  11.455  1.00 16.24 ?  71  THR   B C    1 
ATOM   5029 O O    . THR   B 1 71  ? 45.766 -3.922  11.975  1.00 17.83 ?  71  THR   B O    1 
ATOM   5030 C CB   . THR   B 1 71  ? 48.237 -3.780  9.858   1.00 17.49 ?  71  THR   B CB   1 
ATOM   5031 O OG1  . THR   B 1 71  ? 49.564 -3.249  9.763   1.00 19.35 ?  71  THR   B OG1  1 
ATOM   5032 C CG2  . THR   B 1 71  ? 47.224 -2.687  9.548   1.00 18.48 ?  71  THR   B CG2  1 
ATOM   5033 H H    . THR   B 1 71  ? 49.167 -5.877  10.737  1.00 17.73 ?  71  THR   B H    1 
ATOM   5034 H HA   . THR   B 1 71  ? 48.240 -3.663  11.900  1.00 18.73 ?  71  THR   B HA   1 
ATOM   5035 H HB   . THR   B 1 71  ? 48.141 -4.480  9.198   1.00 20.99 ?  71  THR   B HB   1 
ATOM   5036 H HG1  . THR   B 1 71  ? 49.693 -2.910  9.002   1.00 23.21 ?  71  THR   B HG1  1 
ATOM   5037 H HG21 . THR   B 1 71  ? 47.529 -2.153  8.795   1.00 22.17 ?  71  THR   B HG21 1 
ATOM   5038 H HG22 . THR   B 1 71  ? 46.367 -3.079  9.327   1.00 22.17 ?  71  THR   B HG22 1 
ATOM   5039 H HG23 . THR   B 1 71  ? 47.118 -2.103  10.318  1.00 22.17 ?  71  THR   B HG23 1 
ATOM   5040 N N    . ASN   B 1 72  ? 46.160 -5.938  11.051  1.00 15.81 ?  72  ASN   B N    1 
ATOM   5041 C CA   . ASN   B 1 72  ? 44.756 -6.295  10.924  1.00 16.30 ?  72  ASN   B CA   1 
ATOM   5042 C C    . ASN   B 1 72  ? 44.287 -7.389  11.873  1.00 16.86 ?  72  ASN   B C    1 
ATOM   5043 O O    . ASN   B 1 72  ? 43.072 -7.542  12.047  1.00 18.17 ?  72  ASN   B O    1 
ATOM   5044 C CB   . ASN   B 1 72  ? 44.450 -6.723  9.480   1.00 17.16 ?  72  ASN   B CB   1 
ATOM   5045 C CG   . ASN   B 1 72  ? 44.733 -5.622  8.481   1.00 18.22 ?  72  ASN   B CG   1 
ATOM   5046 O OD1  . ASN   B 1 72  ? 45.751 -5.636  7.785   1.00 19.34 ?  72  ASN   B OD1  1 
ATOM   5047 N ND2  . ASN   B 1 72  ? 43.854 -4.642  8.433   1.00 19.65 ?  72  ASN   B ND2  1 
ATOM   5048 H H    . ASN   B 1 72  ? 46.705 -6.577  10.839  1.00 18.97 ?  72  ASN   B H    1 
ATOM   5049 H HA   . ASN   B 1 72  ? 44.228 -5.507  11.107  1.00 19.55 ?  72  ASN   B HA   1 
ATOM   5050 H HB2  . ASN   B 1 72  ? 45.007 -7.487  9.249   1.00 20.59 ?  72  ASN   B HB2  1 
ATOM   5051 H HB3  . ASN   B 1 72  ? 43.516 -6.958  9.409   1.00 20.59 ?  72  ASN   B HB3  1 
ATOM   5052 H HD21 . ASN   B 1 72  ? 43.967 -3.990  7.882   1.00 23.57 ?  72  ASN   B HD21 1 
ATOM   5053 H HD22 . ASN   B 1 72  ? 43.157 -4.665  8.935   1.00 23.57 ?  72  ASN   B HD22 1 
ATOM   5054 N N    . GLY   B 1 73  ? 45.190 -8.144  12.491  1.00 16.23 ?  73  GLY   B N    1 
ATOM   5055 C CA   . GLY   B 1 73  ? 44.788 -9.277  13.288  1.00 15.72 ?  73  GLY   B CA   1 
ATOM   5056 C C    . GLY   B 1 73  ? 44.422 -10.462 12.420  1.00 14.48 ?  73  GLY   B C    1 
ATOM   5057 O O    . GLY   B 1 73  ? 44.408 -10.379 11.190  1.00 14.34 ?  73  GLY   B O    1 
ATOM   5058 H H    . GLY   B 1 73  ? 46.043 -8.016  12.459  1.00 19.48 ?  73  GLY   B H    1 
ATOM   5059 H HA2  . GLY   B 1 73  ? 45.515 -9.532  13.879  1.00 18.86 ?  73  GLY   B HA2  1 
ATOM   5060 H HA3  . GLY   B 1 73  ? 44.020 -9.036  13.831  1.00 18.86 ?  73  GLY   B HA3  1 
ATOM   5061 N N    . PRO   B 1 74  ? 44.110 -11.588 13.057  1.00 14.59 ?  74  PRO   B N    1 
ATOM   5062 C CA   . PRO   B 1 74  ? 43.860 -12.821 12.307  1.00 14.52 ?  74  PRO   B CA   1 
ATOM   5063 C C    . PRO   B 1 74  ? 42.566 -12.768 11.509  1.00 14.03 ?  74  PRO   B C    1 
ATOM   5064 O O    . PRO   B 1 74  ? 41.621 -12.035 11.831  1.00 15.01 ?  74  PRO   B O    1 
ATOM   5065 C CB   . PRO   B 1 74  ? 43.781 -13.888 13.405  1.00 15.85 ?  74  PRO   B CB   1 
ATOM   5066 C CG   . PRO   B 1 74  ? 43.334 -13.142 14.619  1.00 16.89 ?  74  PRO   B CG   1 
ATOM   5067 C CD   . PRO   B 1 74  ? 43.979 -11.788 14.510  1.00 16.14 ?  74  PRO   B CD   1 
ATOM   5068 H HA   . PRO   B 1 74  ? 44.606 -13.010 11.714  1.00 17.42 ?  74  PRO   B HA   1 
ATOM   5069 H HB2  . PRO   B 1 74  ? 43.133 -14.565 13.154  1.00 19.01 ?  74  PRO   B HB2  1 
ATOM   5070 H HB3  . PRO   B 1 74  ? 44.656 -14.281 13.542  1.00 19.01 ?  74  PRO   B HB3  1 
ATOM   5071 H HG2  . PRO   B 1 74  ? 42.366 -13.064 14.615  1.00 20.26 ?  74  PRO   B HG2  1 
ATOM   5072 H HG3  . PRO   B 1 74  ? 43.637 -13.604 15.415  1.00 20.26 ?  74  PRO   B HG3  1 
ATOM   5073 H HD2  . PRO   B 1 74  ? 43.403 -11.109 14.903  1.00 19.36 ?  74  PRO   B HD2  1 
ATOM   5074 H HD3  . PRO   B 1 74  ? 44.853 -11.795 14.927  1.00 19.36 ?  74  PRO   B HD3  1 
ATOM   5075 N N    . LEU   B 1 75  ? 42.539 -13.572 10.449  1.00 13.19 ?  75  LEU   B N    1 
ATOM   5076 C CA   . LEU   B 1 75  ? 41.325 -13.785 9.682   1.00 13.03 ?  75  LEU   B CA   1 
ATOM   5077 C C    . LEU   B 1 75  ? 40.347 -14.639 10.486  1.00 13.51 ?  75  LEU   B C    1 
ATOM   5078 O O    . LEU   B 1 75  ? 40.687 -15.197 11.530  1.00 14.57 ?  75  LEU   B O    1 
ATOM   5079 C CB   . LEU   B 1 75  ? 41.647 -14.506 8.372   1.00 13.14 ?  75  LEU   B CB   1 
ATOM   5080 C CG   . LEU   B 1 75  ? 42.489 -13.750 7.338   1.00 15.28 ?  75  LEU   B CG   1 
ATOM   5081 C CD1  . LEU   B 1 75  ? 42.688 -14.570 6.063   1.00 16.67 ?  75  LEU   B CD1  1 
ATOM   5082 C CD2  . LEU   B 1 75  ? 41.889 -12.411 7.008   1.00 18.44 ?  75  LEU   B CD2  1 
ATOM   5083 H H    . LEU   B 1 75  ? 43.219 -14.015 10.154  1.00 15.82 ?  75  LEU   B H    1 
ATOM   5084 H HA   . LEU   B 1 75  ? 40.907 -12.936 9.481   1.00 15.63 ?  75  LEU   B HA   1 
ATOM   5085 H HB2  . LEU   B 1 75  ? 42.127 -15.323 8.584   1.00 15.76 ?  75  LEU   B HB2  1 
ATOM   5086 H HB3  . LEU   B 1 75  ? 40.809 -14.735 7.937   1.00 15.76 ?  75  LEU   B HB3  1 
ATOM   5087 H HG   . LEU   B 1 75  ? 43.368 -13.592 7.715   1.00 18.33 ?  75  LEU   B HG   1 
ATOM   5088 H HD11 . LEU   B 1 75  ? 43.235 -14.060 5.438   1.00 20.00 ?  75  LEU   B HD11 1 
ATOM   5089 H HD12 . LEU   B 1 75  ? 43.140 -15.401 6.284   1.00 20.00 ?  75  LEU   B HD12 1 
ATOM   5090 H HD13 . LEU   B 1 75  ? 41.826 -14.759 5.665   1.00 20.00 ?  75  LEU   B HD13 1 
ATOM   5091 H HD21 . LEU   B 1 75  ? 42.378 -12.018 6.269   1.00 22.12 ?  75  LEU   B HD21 1 
ATOM   5092 H HD22 . LEU   B 1 75  ? 40.960 -12.535 6.764   1.00 22.12 ?  75  LEU   B HD22 1 
ATOM   5093 H HD23 . LEU   B 1 75  ? 41.954 -11.838 7.789   1.00 22.12 ?  75  LEU   B HD23 1 
ATOM   5094 N N    . LYS   B 1 76  ? 39.113 -14.727 9.986   1.00 15.03 ?  76  LYS   B N    1 
ATOM   5095 C CA   . LYS   B 1 76  ? 38.131 -15.694 10.461  1.00 16.39 ?  76  LYS   B CA   1 
ATOM   5096 C C    . LYS   B 1 76  ? 38.226 -16.963 9.620   1.00 14.56 ?  76  LYS   B C    1 
ATOM   5097 O O    . LYS   B 1 76  ? 38.494 -16.904 8.420   1.00 14.19 ?  76  LYS   B O    1 
ATOM   5098 C CB   . LYS   B 1 76  ? 36.708 -15.135 10.293  1.00 18.73 ?  76  LYS   B CB   1 
ATOM   5099 C CG   . LYS   B 1 76  ? 36.438 -13.740 10.888  1.00 20.81 ?  76  LYS   B CG   1 
ATOM   5100 C CD   . LYS   B 1 76  ? 35.029 -13.221 10.545  1.00 22.06 ?  76  LYS   B CD   1 
ATOM   5101 C CE   . LYS   B 1 76  ? 34.786 -11.821 11.095  1.00 24.12 ?  76  LYS   B CE   1 
ATOM   5102 N NZ   . LYS   B 1 76  ? 33.475 -11.254 10.672  1.00 24.63 ?  76  LYS   B NZ   1 
ATOM   5103 H H    . LYS   B 1 76  ? 38.819 -14.228 9.351   1.00 18.03 ?  76  LYS   B H    1 
ATOM   5104 H HA   . LYS   B 1 76  ? 38.287 -15.913 11.393  1.00 19.67 ?  76  LYS   B HA   1 
ATOM   5105 H HB2  . LYS   B 1 76  ? 36.510 -15.084 9.345   1.00 22.47 ?  76  LYS   B HB2  1 
ATOM   5106 H HB3  . LYS   B 1 76  ? 36.087 -15.749 10.717  1.00 22.47 ?  76  LYS   B HB3  1 
ATOM   5107 H HG2  . LYS   B 1 76  ? 36.521 -13.786 11.854  1.00 24.96 ?  76  LYS   B HG2  1 
ATOM   5108 H HG3  . LYS   B 1 76  ? 37.091 -13.113 10.530  1.00 24.96 ?  76  LYS   B HG3  1 
ATOM   5109 H HD2  . LYS   B 1 76  ? 34.928 -13.188 9.580   1.00 26.47 ?  76  LYS   B HD2  1 
ATOM   5110 H HD3  . LYS   B 1 76  ? 34.369 -13.815 10.930  1.00 26.47 ?  76  LYS   B HD3  1 
ATOM   5111 H HE2  . LYS   B 1 76  ? 34.803 -11.856 12.063  1.00 28.94 ?  76  LYS   B HE2  1 
ATOM   5112 H HE3  . LYS   B 1 76  ? 35.487 -11.230 10.773  1.00 28.94 ?  76  LYS   B HE3  1 
ATOM   5113 H HZ1  . LYS   B 1 76  ? 33.434 -11.201 9.784   1.00 29.55 ?  76  LYS   B HZ1  1 
ATOM   5114 H HZ2  . LYS   B 1 76  ? 32.810 -11.771 10.961  1.00 29.55 ?  76  LYS   B HZ2  1 
ATOM   5115 H HZ3  . LYS   B 1 76  ? 33.370 -10.436 11.013  1.00 29.55 ?  76  LYS   B HZ3  1 
ATOM   5116 N N    . VAL   B 1 77  ? 37.974 -18.119 10.246  1.00 15.51 ?  77  VAL   B N    1 
ATOM   5117 C CA   . VAL   B 1 77  ? 37.768 -19.331 9.459   1.00 15.58 ?  77  VAL   B CA   1 
ATOM   5118 C C    . VAL   B 1 77  ? 36.578 -19.096 8.544   1.00 14.14 ?  77  VAL   B C    1 
ATOM   5119 O O    . VAL   B 1 77  ? 35.515 -18.649 8.992   1.00 14.20 ?  77  VAL   B O    1 
ATOM   5120 C CB   . VAL   B 1 77  ? 37.562 -20.556 10.363  1.00 17.24 ?  77  VAL   B CB   1 
ATOM   5121 C CG1  . VAL   B 1 77  ? 37.278 -21.792 9.511   1.00 17.81 ?  77  VAL   B CG1  1 
ATOM   5122 C CG2  . VAL   B 1 77  ? 38.791 -20.786 11.243  1.00 18.52 ?  77  VAL   B CG2  1 
ATOM   5123 H H    . VAL   B 1 77  ? 37.918 -18.223 11.095  1.00 18.60 ?  77  VAL   B H    1 
ATOM   5124 H HA   . VAL   B 1 77  ? 38.541 -19.489 8.903   1.00 18.69 ?  77  VAL   B HA   1 
ATOM   5125 H HB   . VAL   B 1 77  ? 36.794 -20.404 10.939  1.00 20.68 ?  77  VAL   B HB   1 
ATOM   5126 H HG11 . VAL   B 1 77  ? 37.333 -22.581 10.073  1.00 21.37 ?  77  VAL   B HG11 1 
ATOM   5127 H HG12 . VAL   B 1 77  ? 36.385 -21.723 9.132   1.00 21.37 ?  77  VAL   B HG12 1 
ATOM   5128 H HG13 . VAL   B 1 77  ? 37.934 -21.845 8.801   1.00 21.37 ?  77  VAL   B HG13 1 
ATOM   5129 H HG21 . VAL   B 1 77  ? 38.648 -21.584 11.774  1.00 22.21 ?  77  VAL   B HG21 1 
ATOM   5130 H HG22 . VAL   B 1 77  ? 39.565 -20.895 10.674  1.00 22.21 ?  77  VAL   B HG22 1 
ATOM   5131 H HG23 . VAL   B 1 77  ? 38.906 -20.018 11.823  1.00 22.21 ?  77  VAL   B HG23 1 
ATOM   5132 N N    . GLY   B 1 78  ? 36.757 -19.369 7.254   1.00 13.57 ?  78  GLY   B N    1 
ATOM   5133 C CA   . GLY   B 1 78  ? 35.780 -19.050 6.241   1.00 13.39 ?  78  GLY   B CA   1 
ATOM   5134 C C    . GLY   B 1 78  ? 36.023 -17.730 5.544   1.00 12.96 ?  78  GLY   B C    1 
ATOM   5135 O O    . GLY   B 1 78  ? 35.350 -17.448 4.549   1.00 13.11 ?  78  GLY   B O    1 
ATOM   5136 H H    . GLY   B 1 78  ? 37.460 -19.756 6.939   1.00 16.28 ?  78  GLY   B H    1 
ATOM   5137 H HA2  . GLY   B 1 78  ? 35.775 -19.744 5.571   1.00 16.06 ?  78  GLY   B HA2  1 
ATOM   5138 H HA3  . GLY   B 1 78  ? 34.901 -19.009 6.649   1.00 16.06 ?  78  GLY   B HA3  1 
ATOM   5139 N N    . GLY   B 1 79  ? 36.971 -16.925 6.033   1.00 13.24 ?  79  GLY   B N    1 
ATOM   5140 C CA   . GLY   B 1 79  ? 37.275 -15.633 5.455   1.00 13.14 ?  79  GLY   B CA   1 
ATOM   5141 C C    . GLY   B 1 79  ? 38.511 -15.663 4.563   1.00 12.41 ?  79  GLY   B C    1 
ATOM   5142 O O    . GLY   B 1 79  ? 39.128 -16.699 4.322   1.00 12.80 ?  79  GLY   B O    1 
ATOM   5143 H H    . GLY   B 1 79  ? 37.463 -17.116 6.710   1.00 15.88 ?  79  GLY   B H    1 
ATOM   5144 H HA2  . GLY   B 1 79  ? 36.522 -15.328 4.923   1.00 15.76 ?  79  GLY   B HA2  1 
ATOM   5145 H HA3  . GLY   B 1 79  ? 37.429 -14.989 6.164   1.00 15.76 ?  79  GLY   B HA3  1 
ATOM   5146 N N    . SER   B 1 80  ? 38.879 -14.472 4.085   1.00 12.53 ?  80  SER   B N    1 
ATOM   5147 C CA   . SER   B 1 80  ? 39.989 -14.339 3.152   1.00 11.94 ?  80  SER   B CA   1 
ATOM   5148 C C    . SER   B 1 80  ? 40.567 -12.932 3.212   1.00 12.28 ?  80  SER   B C    1 
ATOM   5149 O O    . SER   B 1 80  ? 39.953 -11.999 3.737   1.00 13.48 ?  80  SER   B O    1 
ATOM   5150 C CB   . SER   B 1 80  ? 39.548 -14.631 1.714   1.00 12.48 ?  80  SER   B CB   1 
ATOM   5151 O OG   . SER   B 1 80  ? 38.712 -13.602 1.216   1.00 13.63 ?  80  SER   B OG   1 
ATOM   5152 H H    . SER   B 1 80  ? 38.506 -13.727 4.294   1.00 15.03 ?  80  SER   B H    1 
ATOM   5153 H HA   . SER   B 1 80  ? 40.680 -14.968 3.398   1.00 14.32 ?  80  SER   B HA   1 
ATOM   5154 H HB2  . SER   B 1 80  ? 40.330 -14.691 1.145   1.00 14.97 ?  80  SER   B HB2  1 
ATOM   5155 H HB3  . SER   B 1 80  ? 39.057 -15.466 1.694   1.00 14.97 ?  80  SER   B HB3  1 
ATOM   5156 H HG   . SER   B 1 80  ? 38.021 -13.530 1.702   1.00 16.35 ?  80  SER   B HG   1 
ATOM   5157 N N    . CYS   B 1 81  ? 41.754 -12.787 2.628   1.00 12.10 ?  81  CYS   B N    1 
ATOM   5158 C CA   . CYS   B 1 81  ? 42.306 -11.474 2.322   1.00 12.18 ?  81  CYS   B CA   1 
ATOM   5159 C C    . CYS   B 1 81  ? 43.084 -11.558 1.018   1.00 11.35 ?  81  CYS   B C    1 
ATOM   5160 O O    . CYS   B 1 81  ? 43.591 -12.622 0.644   1.00 12.51 ?  81  CYS   B O    1 
ATOM   5161 C CB   . CYS   B 1 81  ? 43.191 -10.922 3.451   1.00 12.73 ?  81  CYS   B CB   1 
ATOM   5162 S SG   . CYS   B 1 81  ? 44.710 -11.860 3.699   1.00 13.41 ?  81  CYS   B SG   1 
ATOM   5163 H H    . CYS   B 1 81  ? 42.263 -13.443 2.391   1.00 14.51 ?  81  CYS   B H    1 
ATOM   5164 H HA   . CYS   B 1 81  ? 41.575 -10.852 2.191   1.00 14.61 ?  81  CYS   B HA   1 
ATOM   5165 H HB2  . CYS   B 1 81  ? 43.438 -10.007 3.242   1.00 15.27 ?  81  CYS   B HB2  1 
ATOM   5166 H HB3  . CYS   B 1 81  ? 42.686 -10.939 4.284   1.00 15.27 ?  81  CYS   B HB3  1 
ATOM   5167 H HG   . CYS   B 1 81  ? 45.335 -11.365 4.605   1.00 16.08 ?  81  CYS   B HG   1 
ATOM   5168 N N    . VAL   B 1 82  ? 43.188 -10.416 0.343   1.00 11.72 ?  82  VAL   B N    1 
ATOM   5169 C CA   . VAL   B 1 82  ? 43.951 -10.293 -0.895  1.00 12.04 ?  82  VAL   B CA   1 
ATOM   5170 C C    . VAL   B 1 82  ? 45.291 -9.652  -0.573  1.00 12.26 ?  82  VAL   B C    1 
ATOM   5171 O O    . VAL   B 1 82  ? 45.340 -8.534  -0.042  1.00 13.19 ?  82  VAL   B O    1 
ATOM   5172 C CB   . VAL   B 1 82  ? 43.206 -9.450  -1.941  1.00 13.11 ?  82  VAL   B CB   1 
ATOM   5173 C CG1  . VAL   B 1 82  ? 44.058 -9.289  -3.194  1.00 14.19 ?  82  VAL   B CG1  1 
ATOM   5174 C CG2  . VAL   B 1 82  ? 41.853 -10.054 -2.270  1.00 13.90 ?  82  VAL   B CG2  1 
ATOM   5175 H H    . VAL   B 1 82  ? 42.809 -9.678  0.584   1.00 14.06 ?  82  VAL   B H    1 
ATOM   5176 H HA   . VAL   B 1 82  ? 44.110 -11.172 -1.267  1.00 14.44 ?  82  VAL   B HA   1 
ATOM   5177 H HB   . VAL   B 1 82  ? 43.051 -8.565  -1.578  1.00 15.73 ?  82  VAL   B HB   1 
ATOM   5178 H HG11 . VAL   B 1 82  ? 43.496 -8.975  -3.920  1.00 17.02 ?  82  VAL   B HG11 1 
ATOM   5179 H HG12 . VAL   B 1 82  ? 44.759 -8.638  -3.020  1.00 17.02 ?  82  VAL   B HG12 1 
ATOM   5180 H HG13 . VAL   B 1 82  ? 44.449 -10.144 -3.424  1.00 17.02 ?  82  VAL   B HG13 1 
ATOM   5181 H HG21 . VAL   B 1 82  ? 41.421 -9.517  -2.956  1.00 16.67 ?  82  VAL   B HG21 1 
ATOM   5182 H HG22 . VAL   B 1 82  ? 41.977 -10.961 -2.595  1.00 16.67 ?  82  VAL   B HG22 1 
ATOM   5183 H HG23 . VAL   B 1 82  ? 41.305 -10.064 -1.469  1.00 16.67 ?  82  VAL   B HG23 1 
ATOM   5184 N N    . LEU   B 1 83  ? 46.370 -10.335 -0.936  1.00 11.67 ?  83  LEU   B N    1 
ATOM   5185 C CA   . LEU   B 1 83  ? 47.726 -9.821  -0.816  1.00 11.66 ?  83  LEU   B CA   1 
ATOM   5186 C C    . LEU   B 1 83  ? 48.423 -9.967  -2.166  1.00 11.51 ?  83  LEU   B C    1 
ATOM   5187 O O    . LEU   B 1 83  ? 47.824 -10.384 -3.159  1.00 11.71 ?  83  LEU   B O    1 
ATOM   5188 C CB   . LEU   B 1 83  ? 48.474 -10.501 0.338   1.00 12.28 ?  83  LEU   B CB   1 
ATOM   5189 C CG   . LEU   B 1 83  ? 47.951 -10.141 1.734   1.00 13.32 ?  83  LEU   B CG   1 
ATOM   5190 C CD1  . LEU   B 1 83  ? 48.568 -11.004 2.819   1.00 14.45 ?  83  LEU   B CD1  1 
ATOM   5191 C CD2  . LEU   B 1 83  ? 48.153 -8.655  2.051   1.00 14.32 ?  83  LEU   B CD2  1 
ATOM   5192 H H    . LEU   B 1 83  ? 46.335 -11.131 -1.271  1.00 13.99 ?  83  LEU   B H    1 
ATOM   5193 H HA   . LEU   B 1 83  ? 47.675 -8.873  -0.621  1.00 13.98 ?  83  LEU   B HA   1 
ATOM   5194 H HB2  . LEU   B 1 83  ? 48.400 -11.459 0.232   1.00 14.73 ?  83  LEU   B HB2  1 
ATOM   5195 H HB3  . LEU   B 1 83  ? 49.406 -10.236 0.294   1.00 14.73 ?  83  LEU   B HB3  1 
ATOM   5196 H HG   . LEU   B 1 83  ? 46.998 -10.305 1.742   1.00 15.98 ?  83  LEU   B HG   1 
ATOM   5197 H HD11 . LEU   B 1 83  ? 48.195 -10.743 3.676   1.00 17.33 ?  83  LEU   B HD11 1 
ATOM   5198 H HD12 . LEU   B 1 83  ? 48.356 -11.935 2.638   1.00 17.33 ?  83  LEU   B HD12 1 
ATOM   5199 H HD13 . LEU   B 1 83  ? 49.527 -10.877 2.821   1.00 17.33 ?  83  LEU   B HD13 1 
ATOM   5200 H HD21 . LEU   B 1 83  ? 47.951 -8.505  2.988   1.00 17.18 ?  83  LEU   B HD21 1 
ATOM   5201 H HD22 . LEU   B 1 83  ? 49.073 -8.412  1.867   1.00 17.18 ?  83  LEU   B HD22 1 
ATOM   5202 H HD23 . LEU   B 1 83  ? 47.555 -8.127  1.497   1.00 17.18 ?  83  LEU   B HD23 1 
ATOM   5203 N N    . SER   B 1 84  ? 49.699 -9.601  -2.216  1.00 12.45 ?  84  SER   B N    1 
ATOM   5204 C CA   . SER   B 1 84  ? 50.429 -9.713  -3.468  1.00 12.62 ?  84  SER   B CA   1 
ATOM   5205 C C    . SER   B 1 84  ? 50.589 -11.173 -3.878  1.00 12.26 ?  84  SER   B C    1 
ATOM   5206 O O    . SER   B 1 84  ? 50.701 -12.071 -3.043  1.00 11.97 ?  84  SER   B O    1 
ATOM   5207 C CB   . SER   B 1 84  ? 51.817 -9.096  -3.323  1.00 14.48 ?  84  SER   B CB   1 
ATOM   5208 O OG   . SER   B 1 84  ? 52.566 -9.314  -4.502  1.00 16.14 ?  84  SER   B OG   1 
ATOM   5209 H H    . SER   B 1 84  ? 50.149 -9.271  -1.560  1.00 14.93 ?  84  SER   B H    1 
ATOM   5210 H HA   . SER   B 1 84  ? 49.954 -9.245  -4.172  1.00 15.14 ?  84  SER   B HA   1 
ATOM   5211 H HB2  . SER   B 1 84  ? 51.727 -8.137  -3.169  1.00 17.37 ?  84  SER   B HB2  1 
ATOM   5212 H HB3  . SER   B 1 84  ? 52.279 -9.507  -2.579  1.00 17.37 ?  84  SER   B HB3  1 
ATOM   5213 H HG   . SER   B 1 84  ? 53.330 -8.956  -4.427  1.00 19.36 ?  84  SER   B HG   1 
ATOM   5214 N N    . GLY   B 1 85  ? 50.647 -11.399 -5.185  1.00 13.29 ?  85  GLY   B N    1 
ATOM   5215 C CA   . GLY   B 1 85  ? 50.998 -12.689 -5.725  1.00 13.84 ?  85  GLY   B CA   1 
ATOM   5216 C C    . GLY   B 1 85  ? 52.469 -12.877 -6.021  1.00 13.09 ?  85  GLY   B C    1 
ATOM   5217 O O    . GLY   B 1 85  ? 52.853 -13.956 -6.475  1.00 13.80 ?  85  GLY   B O    1 
ATOM   5218 H H    . GLY   B 1 85  ? 50.489 -10.809 -5.783  1.00 15.94 ?  85  GLY   B H    1 
ATOM   5219 H HA2  . GLY   B 1 85  ? 50.733 -13.381 -5.095  1.00 16.60 ?  85  GLY   B HA2  1 
ATOM   5220 H HA3  . GLY   B 1 85  ? 50.508 -12.833 -6.547  1.00 16.60 ?  85  GLY   B HA3  1 
ATOM   5221 N N    . HIS   B 1 86  ? 53.315 -11.872 -5.799  1.00 13.04 ?  86  HIS   B N    1 
ATOM   5222 C CA   . HIS   B 1 86  ? 54.776 -12.042 -5.874  1.00 12.56 ?  86  HIS   B CA   1 
ATOM   5223 C C    . HIS   B 1 86  ? 55.156 -12.549 -7.263  1.00 12.75 ?  86  HIS   B C    1 
ATOM   5224 O O    . HIS   B 1 86  ? 54.767 -11.937 -8.270  1.00 13.89 ?  86  HIS   B O    1 
ATOM   5225 C CB   . HIS   B 1 86  ? 55.259 -12.885 -4.698  1.00 12.85 ?  86  HIS   B CB   1 
ATOM   5226 C CG   . HIS   B 1 86  ? 54.948 -12.275 -3.374  1.00 13.22 ?  86  HIS   B CG   1 
ATOM   5227 N ND1  . HIS   B 1 86  ? 55.777 -11.359 -2.763  1.00 14.78 ?  86  HIS   B ND1  1 
ATOM   5228 C CD2  . HIS   B 1 86  ? 53.876 -12.417 -2.560  1.00 13.76 ?  86  HIS   B CD2  1 
ATOM   5229 C CE1  . HIS   B 1 86  ? 55.231 -10.972 -1.624  1.00 14.47 ?  86  HIS   B CE1  1 
ATOM   5230 N NE2  . HIS   B 1 86  ? 54.074 -11.594 -1.480  1.00 13.98 ?  86  HIS   B NE2  1 
ATOM   5231 H H    . HIS   B 1 86  ? 53.073 -11.074 -5.604  1.00 15.64 ?  86  HIS   B H    1 
ATOM   5232 H HA   . HIS   B 1 86  ? 55.187 -11.172 -5.775  1.00 15.06 ?  86  HIS   B HA   1 
ATOM   5233 H HB2  . HIS   B 1 86  ? 54.837 -13.757 -4.733  1.00 15.41 ?  86  HIS   B HB2  1 
ATOM   5234 H HB3  . HIS   B 1 86  ? 56.226 -12.987 -4.753  1.00 15.41 ?  86  HIS   B HB3  1 
ATOM   5235 H HD2  . HIS   B 1 86  ? 53.134 -12.963 -2.709  1.00 16.50 ?  86  HIS   B HD2  1 
ATOM   5236 H HE1  . HIS   B 1 86  ? 55.601 -10.370 -1.019  1.00 17.35 ?  86  HIS   B HE1  1 
ATOM   5237 H HE2  . HIS   B 1 86  ? 53.538 -11.510 -0.808  1.00 16.77 ?  86  HIS   B HE2  1 
ATOM   5238 N N    . ASN   B 1 87  ? 55.923 -13.634 -7.371  1.00 13.73 ?  87  ASN   B N    1 
ATOM   5239 C CA   . ASN   B 1 87  ? 56.323 -14.207 -8.648  1.00 14.29 ?  87  ASN   B CA   1 
ATOM   5240 C C    . ASN   B 1 87  ? 55.340 -15.251 -9.153  1.00 14.10 ?  87  ASN   B C    1 
ATOM   5241 O O    . ASN   B 1 87  ? 55.655 -15.956 -10.116 1.00 15.78 ?  87  ASN   B O    1 
ATOM   5242 C CB   . ASN   B 1 87  ? 57.718 -14.833 -8.529  1.00 16.38 ?  87  ASN   B CB   1 
ATOM   5243 C CG   . ASN   B 1 87  ? 57.774 -15.937 -7.486  1.00 17.18 ?  87  ASN   B CG   1 
ATOM   5244 O OD1  . ASN   B 1 87  ? 57.133 -15.850 -6.437  1.00 16.14 ?  87  ASN   B OD1  1 
ATOM   5245 N ND2  . ASN   B 1 87  ? 58.523 -17.002 -7.784  1.00 19.64 ?  87  ASN   B ND2  1 
ATOM   5246 H H    . ASN   B 1 87  ? 56.227 -14.072 -6.695  1.00 16.47 ?  87  ASN   B H    1 
ATOM   5247 H HA   . ASN   B 1 87  ? 56.370 -13.502 -9.306  1.00 17.14 ?  87  ASN   B HA   1 
ATOM   5248 H HB2  . ASN   B 1 87  ? 57.967 -15.219 -9.387  1.00 19.65 ?  87  ASN   B HB2  1 
ATOM   5249 H HB3  . ASN   B 1 87  ? 58.352 -14.150 -8.275  1.00 19.65 ?  87  ASN   B HB3  1 
ATOM   5250 H HD21 . ASN   B 1 87  ? 58.591 -17.652 -7.227  1.00 23.57 ?  87  ASN   B HD21 1 
ATOM   5251 H HD22 . ASN   B 1 87  ? 58.953 -17.031 -8.531  1.00 23.57 ?  87  ASN   B HD22 1 
ATOM   5252 N N    . LEU   B 1 88  ? 54.162 -15.358 -8.535  1.00 13.07 ?  88  LEU   B N    1 
ATOM   5253 C CA   . LEU   B 1 88  ? 53.182 -16.386 -8.870  1.00 13.48 ?  88  LEU   B CA   1 
ATOM   5254 C C    . LEU   B 1 88  ? 51.953 -15.867 -9.594  1.00 13.27 ?  88  LEU   B C    1 
ATOM   5255 O O    . LEU   B 1 88  ? 51.353 -16.614 -10.379 1.00 15.05 ?  88  LEU   B O    1 
ATOM   5256 C CB   . LEU   B 1 88  ? 52.699 -17.068 -7.590  1.00 14.41 ?  88  LEU   B CB   1 
ATOM   5257 C CG   . LEU   B 1 88  ? 53.818 -17.723 -6.792  1.00 16.94 ?  88  LEU   B CG   1 
ATOM   5258 C CD1  . LEU   B 1 88  ? 53.317 -18.112 -5.413  1.00 18.46 ?  88  LEU   B CD1  1 
ATOM   5259 C CD2  . LEU   B 1 88  ? 54.346 -18.930 -7.540  1.00 20.03 ?  88  LEU   B CD2  1 
ATOM   5260 H H    . LEU   B 1 88  ? 53.906 -14.842 -7.892  1.00 15.68 ?  88  LEU   B H    1 
ATOM   5261 H HA   . LEU   B 1 88  ? 53.593 -17.052 -9.429  1.00 16.17 ?  88  LEU   B HA   1 
ATOM   5262 H HB2  . LEU   B 1 88  ? 52.270 -16.411 -7.017  1.00 17.29 ?  88  LEU   B HB2  1 
ATOM   5263 H HB3  . LEU   B 1 88  ? 52.057 -17.762 -7.824  1.00 17.29 ?  88  LEU   B HB3  1 
ATOM   5264 H HG   . LEU   B 1 88  ? 54.542 -17.091 -6.681  1.00 20.32 ?  88  LEU   B HG   1 
ATOM   5265 H HD11 . LEU   B 1 88  ? 53.993 -18.646 -4.969  1.00 22.14 ?  88  LEU   B HD11 1 
ATOM   5266 H HD12 . LEU   B 1 88  ? 53.141 -17.306 -4.901  1.00 22.14 ?  88  LEU   B HD12 1 
ATOM   5267 H HD13 . LEU   B 1 88  ? 52.499 -18.626 -5.509  1.00 22.14 ?  88  LEU   B HD13 1 
ATOM   5268 H HD21 . LEU   B 1 88  ? 54.974 -19.403 -6.971  1.00 24.03 ?  88  LEU   B HD21 1 
ATOM   5269 H HD22 . LEU   B 1 88  ? 53.604 -19.511 -7.768  1.00 24.03 ?  88  LEU   B HD22 1 
ATOM   5270 H HD23 . LEU   B 1 88  ? 54.792 -18.631 -8.348  1.00 24.03 ?  88  LEU   B HD23 1 
ATOM   5271 N N    . ALA   B 1 89  ? 51.548 -14.630 -9.329  1.00 12.55 ?  89  ALA   B N    1 
ATOM   5272 C CA   . ALA   B 1 89  ? 50.253 -14.139 -9.769  1.00 12.37 ?  89  ALA   B CA   1 
ATOM   5273 C C    . ALA   B 1 89  ? 50.227 -12.649 -9.488  1.00 12.91 ?  89  ALA   B C    1 
ATOM   5274 O O    . ALA   B 1 89  ? 51.063 -12.126 -8.747  1.00 13.43 ?  89  ALA   B O    1 
ATOM   5275 C CB   . ALA   B 1 89  ? 49.120 -14.816 -9.002  1.00 12.41 ?  89  ALA   B CB   1 
ATOM   5276 H H    . ALA   B 1 89  ? 52.003 -14.045 -8.886  1.00 15.05 ?  89  ALA   B H    1 
ATOM   5277 H HA   . ALA   B 1 89  ? 50.134 -14.292 -10.722 1.00 14.84 ?  89  ALA   B HA   1 
ATOM   5278 H HB1  . ALA   B 1 89  ? 48.270 -14.483 -9.335  1.00 14.88 ?  89  ALA   B HB1  1 
ATOM   5279 H HB2  . ALA   B 1 89  ? 49.175 -15.774 -9.144  1.00 14.88 ?  89  ALA   B HB2  1 
ATOM   5280 H HB3  . ALA   B 1 89  ? 49.212 -14.612 -8.062  1.00 14.88 ?  89  ALA   B HB3  1 
ATOM   5281 N N    . LYS   B 1 90  ? 49.241 -11.960 -10.059 1.00 13.59 ?  90  LYS   B N    1 
ATOM   5282 C CA   . LYS   B 1 90  ? 49.051 -10.574 -9.657  1.00 13.48 ?  90  LYS   B CA   1 
ATOM   5283 C C    . LYS   B 1 90  ? 48.727 -10.498 -8.170  1.00 13.17 ?  90  LYS   B C    1 
ATOM   5284 O O    . LYS   B 1 90  ? 49.362 -9.741  -7.420  1.00 14.69 ?  90  LYS   B O    1 
ATOM   5285 C CB   . LYS   B 1 90  ? 47.980 -9.909  -10.518 1.00 15.15 ?  90  LYS   B CB   1 
ATOM   5286 C CG   . LYS   B 1 90  ? 47.679 -8.474  -10.122 1.00 16.25 ?  90  LYS   B CG   1 
ATOM   5287 C CD   . LYS   B 1 90  ? 48.885 -7.575  -10.207 1.00 19.16 ?  90  LYS   B CD   1 
ATOM   5288 C CE   . LYS   B 1 90  ? 48.445 -6.160  -9.922  1.00 21.86 ?  90  LYS   B CE   1 
ATOM   5289 N NZ   . LYS   B 1 90  ? 49.593 -5.226  -9.846  1.00 22.09 ?  90  LYS   B NZ   1 
ATOM   5290 H H    . LYS   B 1 90  ? 48.692 -12.263 -10.653 1.00 16.30 ?  90  LYS   B H    1 
ATOM   5291 H HA   . LYS   B 1 90  ? 49.879 -10.100 -9.803  1.00 16.18 ?  90  LYS   B HA   1 
ATOM   5292 H HB2  . LYS   B 1 90  ? 48.282 -9.903  -11.445 1.00 18.17 ?  90  LYS   B HB2  1 
ATOM   5293 H HB3  . LYS   B 1 90  ? 47.157 -10.419 -10.451 1.00 18.17 ?  90  LYS   B HB3  1 
ATOM   5294 H HG2  . LYS   B 1 90  ? 47.000 -8.122  -10.718 1.00 19.49 ?  90  LYS   B HG2  1 
ATOM   5295 H HG3  . LYS   B 1 90  ? 47.351 -8.460  -9.208  1.00 19.49 ?  90  LYS   B HG3  1 
ATOM   5296 H HD2  . LYS   B 1 90  ? 49.542 -7.837  -9.541  1.00 22.99 ?  90  LYS   B HD2  1 
ATOM   5297 H HD3  . LYS   B 1 90  ? 49.265 -7.614  -11.098 1.00 22.99 ?  90  LYS   B HD3  1 
ATOM   5298 H HE2  . LYS   B 1 90  ? 47.859 -5.855  -10.634 1.00 26.23 ?  90  LYS   B HE2  1 
ATOM   5299 H HE3  . LYS   B 1 90  ? 47.980 -6.130  -9.072  1.00 26.23 ?  90  LYS   B HE3  1 
ATOM   5300 H HZ1  . LYS   B 1 90  ? 49.307 -4.399  -9.679  1.00 26.50 ?  90  LYS   B HZ1  1 
ATOM   5301 H HZ2  . LYS   B 1 90  ? 50.148 -5.475  -9.196  1.00 26.50 ?  90  LYS   B HZ2  1 
ATOM   5302 H HZ3  . LYS   B 1 90  ? 50.038 -5.225  -10.619 1.00 26.50 ?  90  LYS   B HZ3  1 
ATOM   5303 N N    . HIS   B 1 91  ? 47.765 -11.311 -7.725  1.00 11.70 ?  91  HIS   B N    1 
ATOM   5304 C CA   . HIS   B 1 91  ? 47.305 -11.333 -6.349  1.00 11.88 ?  91  HIS   B CA   1 
ATOM   5305 C C    . HIS   B 1 91  ? 47.303 -12.758 -5.829  1.00 11.26 ?  91  HIS   B C    1 
ATOM   5306 O O    . HIS   B 1 91  ? 47.080 -13.713 -6.583  1.00 11.91 ?  91  HIS   B O    1 
ATOM   5307 C CB   . HIS   B 1 91  ? 45.851 -10.857 -6.234  1.00 13.34 ?  91  HIS   B CB   1 
ATOM   5308 C CG   . HIS   B 1 91  ? 45.636 -9.446  -6.661  1.00 16.88 ?  91  HIS   B CG   1 
ATOM   5309 N ND1  . HIS   B 1 91  ? 46.250 -8.377  -6.045  1.00 19.26 ?  91  HIS   B ND1  1 
ATOM   5310 C CD2  . HIS   B 1 91  ? 44.846 -8.923  -7.625  1.00 19.15 ?  91  HIS   B CD2  1 
ATOM   5311 C CE1  . HIS   B 1 91  ? 45.865 -7.254  -6.626  1.00 20.26 ?  91  HIS   B CE1  1 
ATOM   5312 N NE2  . HIS   B 1 91  ? 45.007 -7.558  -7.585  1.00 20.36 ?  91  HIS   B NE2  1 
ATOM   5313 H H    . HIS   B 1 91  ? 47.352 -11.882 -8.224  1.00 14.04 ?  91  HIS   B H    1 
ATOM   5314 H HA   . HIS   B 1 91  ? 47.875 -10.776 -5.791  1.00 14.25 ?  91  HIS   B HA   1 
ATOM   5315 H HB2  . HIS   B 1 91  ? 45.292 -11.419 -6.790  1.00 16.00 ?  91  HIS   B HB2  1 
ATOM   5316 H HB3  . HIS   B 1 91  ? 45.570 -10.930 -5.306  1.00 16.00 ?  91  HIS   B HB3  1 
ATOM   5317 H HD1  . HIS   B 1 91  ? 46.807 -8.431  -5.388  1.00 23.10 ?  91  HIS   B HD1  1 
ATOM   5318 H HD2  . HIS   B 1 91  ? 44.301 -9.388  -8.212  1.00 22.97 ?  91  HIS   B HD2  1 
ATOM   5319 H HE1  . HIS   B 1 91  ? 46.145 -6.395  -6.391  1.00 24.30 ?  91  HIS   B HE1  1 
ATOM   5320 N N    . CYS   B 1 92  ? 47.495 -12.890 -4.523  1.00 11.03 ?  92  CYS   B N    1 
ATOM   5321 C CA   . CYS   B 1 92  ? 47.191 -14.127 -3.815  1.00 11.24 ?  92  CYS   B CA   1 
ATOM   5322 C C    . CYS   B 1 92  ? 45.971 -13.890 -2.936  1.00 10.49 ?  92  CYS   B C    1 
ATOM   5323 O O    . CYS   B 1 92  ? 45.971 -12.986 -2.088  1.00 11.48 ?  92  CYS   B O    1 
ATOM   5324 C CB   . CYS   B 1 92  ? 48.368 -14.590 -2.960  1.00 11.73 ?  92  CYS   B CB   1 
ATOM   5325 S SG   . CYS   B 1 92  ? 48.010 -16.118 -2.063  1.00 11.53 ?  92  CYS   B SG   1 
ATOM   5326 H H    . CYS   B 1 92  ? 47.823 -12.271 -4.016  1.00 13.23 ?  92  CYS   B H    1 
ATOM   5327 H HA   . CYS   B 1 92  ? 46.991 -14.823 -4.460  1.00 13.48 ?  92  CYS   B HA   1 
ATOM   5328 H HB2  . CYS   B 1 92  ? 49.133 -14.745 -3.528  1.00 14.06 ?  92  CYS   B HB2  1 
ATOM   5329 H HB3  . CYS   B 1 92  ? 48.568 -13.900 -2.306  1.00 14.06 ?  92  CYS   B HB3  1 
ATOM   5330 H HG   . CYS   B 1 92  ? 48.982 -16.427 -1.431  1.00 13.83 ?  92  CYS   B HG   1 
ATOM   5331 N N    . LEU   B 1 93  ? 44.933 -14.694 -3.149  1.00 10.69 ?  93  LEU   B N    1 
ATOM   5332 C CA   . LEU   B 1 93  ? 43.760 -14.704 -2.287  1.00 10.81 ?  93  LEU   B CA   1 
ATOM   5333 C C    . LEU   B 1 93  ? 43.984 -15.768 -1.219  1.00 10.23 ?  93  LEU   B C    1 
ATOM   5334 O O    . LEU   B 1 93  ? 43.937 -16.968 -1.507  1.00 11.17 ?  93  LEU   B O    1 
ATOM   5335 C CB   . LEU   B 1 93  ? 42.500 -14.996 -3.095  1.00 11.36 ?  93  LEU   B CB   1 
ATOM   5336 C CG   . LEU   B 1 93  ? 41.201 -15.021 -2.287  1.00 11.78 ?  93  LEU   B CG   1 
ATOM   5337 C CD1  . LEU   B 1 93  ? 40.848 -13.639 -1.792  1.00 12.39 ?  93  LEU   B CD1  1 
ATOM   5338 C CD2  . LEU   B 1 93  ? 40.074 -15.613 -3.117  1.00 12.24 ?  93  LEU   B CD2  1 
ATOM   5339 H H    . LEU   B 1 93  ? 44.893 -15.266 -3.801  1.00 12.82 ?  93  LEU   B H    1 
ATOM   5340 H HA   . LEU   B 1 93  ? 43.672 -13.841 -1.859  1.00 12.97 ?  93  LEU   B HA   1 
ATOM   5341 H HB2  . LEU   B 1 93  ? 42.406 -14.305 -3.773  1.00 13.63 ?  93  LEU   B HB2  1 
ATOM   5342 H HB3  . LEU   B 1 93  ? 42.598 -15.857 -3.520  1.00 13.63 ?  93  LEU   B HB3  1 
ATOM   5343 H HG   . LEU   B 1 93  ? 41.327 -15.587 -1.511  1.00 14.13 ?  93  LEU   B HG   1 
ATOM   5344 H HD11 . LEU   B 1 93  ? 39.994 -13.675 -1.338  1.00 14.86 ?  93  LEU   B HD11 1 
ATOM   5345 H HD12 . LEU   B 1 93  ? 41.538 -13.334 -1.181  1.00 14.86 ?  93  LEU   B HD12 1 
ATOM   5346 H HD13 . LEU   B 1 93  ? 40.794 -13.036 -2.554  1.00 14.86 ?  93  LEU   B HD13 1 
ATOM   5347 H HD21 . LEU   B 1 93  ? 39.261 -15.614 -2.590  1.00 14.68 ?  93  LEU   B HD21 1 
ATOM   5348 H HD22 . LEU   B 1 93  ? 39.952 -15.073 -3.914  1.00 14.68 ?  93  LEU   B HD22 1 
ATOM   5349 H HD23 . LEU   B 1 93  ? 40.310 -16.521 -3.366  1.00 14.68 ?  93  LEU   B HD23 1 
ATOM   5350 N N    . HIS   B 1 94  ? 44.253 -15.339 0.008   1.00 10.31 ?  94  HIS   B N    1 
ATOM   5351 C CA   . HIS   B 1 94  ? 44.471 -16.247 1.125   1.00 10.25 ?  94  HIS   B CA   1 
ATOM   5352 C C    . HIS   B 1 94  ? 43.109 -16.598 1.703   1.00 11.01 ?  94  HIS   B C    1 
ATOM   5353 O O    . HIS   B 1 94  ? 42.445 -15.726 2.268   1.00 12.33 ?  94  HIS   B O    1 
ATOM   5354 C CB   . HIS   B 1 94  ? 45.344 -15.575 2.181   1.00 11.01 ?  94  HIS   B CB   1 
ATOM   5355 C CG   . HIS   B 1 94  ? 46.725 -15.269 1.710   1.00 11.20 ?  94  HIS   B CG   1 
ATOM   5356 N ND1  . HIS   B 1 94  ? 47.753 -16.183 1.797   1.00 11.18 ?  94  HIS   B ND1  1 
ATOM   5357 C CD2  . HIS   B 1 94  ? 47.233 -14.160 1.120   1.00 11.29 ?  94  HIS   B CD2  1 
ATOM   5358 C CE1  . HIS   B 1 94  ? 48.843 -15.628 1.294   1.00 11.59 ?  94  HIS   B CE1  1 
ATOM   5359 N NE2  . HIS   B 1 94  ? 48.558 -14.403 0.880   1.00 11.53 ?  94  HIS   B NE2  1 
ATOM   5360 H H    . HIS   B 1 94  ? 44.314 -14.506 0.217   1.00 12.37 ?  94  HIS   B H    1 
ATOM   5361 H HA   . HIS   B 1 94  ? 44.905 -17.058 0.811   1.00 12.30 ?  94  HIS   B HA   1 
ATOM   5362 H HB2  . HIS   B 1 94  ? 44.927 -14.746 2.443   1.00 13.21 ?  94  HIS   B HB2  1 
ATOM   5363 H HB3  . HIS   B 1 94  ? 45.414 -16.172 2.942   1.00 13.21 ?  94  HIS   B HB3  1 
ATOM   5364 H HD2  . HIS   B 1 94  ? 46.776 -13.380 0.927   1.00 13.54 ?  94  HIS   B HD2  1 
ATOM   5365 H HE1  . HIS   B 1 94  ? 49.678 -16.042 1.243   1.00 13.90 ?  94  HIS   B HE1  1 
ATOM   5366 H HE2  . HIS   B 1 94  ? 49.116 -13.862 0.517   1.00 13.83 ?  94  HIS   B HE2  1 
ATOM   5367 N N    . VAL   B 1 95  ? 42.680 -17.853 1.551   1.00 10.99 ?  95  VAL   B N    1 
ATOM   5368 C CA   . VAL   B 1 95  ? 41.352 -18.290 1.980   1.00 11.20 ?  95  VAL   B CA   1 
ATOM   5369 C C    . VAL   B 1 95  ? 41.517 -19.327 3.076   1.00 11.32 ?  95  VAL   B C    1 
ATOM   5370 O O    . VAL   B 1 95  ? 42.289 -20.279 2.920   1.00 11.83 ?  95  VAL   B O    1 
ATOM   5371 C CB   . VAL   B 1 95  ? 40.531 -18.889 0.820   1.00 11.29 ?  95  VAL   B CB   1 
ATOM   5372 C CG1  . VAL   B 1 95  ? 39.157 -19.351 1.304   1.00 12.33 ?  95  VAL   B CG1  1 
ATOM   5373 C CG2  . VAL   B 1 95  ? 40.401 -17.901 -0.318  1.00 11.56 ?  95  VAL   B CG2  1 
ATOM   5374 H H    . VAL   B 1 95  ? 43.148 -18.485 1.192   1.00 13.19 ?  95  VAL   B H    1 
ATOM   5375 H HA   . VAL   B 1 95  ? 40.862 -17.532 2.339   1.00 13.43 ?  95  VAL   B HA   1 
ATOM   5376 H HB   . VAL   B 1 95  ? 40.994 -19.664 0.478   1.00 13.54 ?  95  VAL   B HB   1 
ATOM   5377 H HG11 . VAL   B 1 95  ? 38.594 -19.542 0.531   1.00 14.79 ?  95  VAL   B HG11 1 
ATOM   5378 H HG12 . VAL   B 1 95  ? 39.256 -20.154 1.837   1.00 14.79 ?  95  VAL   B HG12 1 
ATOM   5379 H HG13 . VAL   B 1 95  ? 38.749 -18.648 1.834   1.00 14.79 ?  95  VAL   B HG13 1 
ATOM   5380 H HG21 . VAL   B 1 95  ? 39.823 -18.282 -0.999  1.00 13.86 ?  95  VAL   B HG21 1 
ATOM   5381 H HG22 . VAL   B 1 95  ? 40.013 -17.080 0.022   1.00 13.86 ?  95  VAL   B HG22 1 
ATOM   5382 H HG23 . VAL   B 1 95  ? 41.279 -17.730 -0.684  1.00 13.86 ?  95  VAL   B HG23 1 
ATOM   5383 N N    . VAL   B 1 96  ? 40.782 -19.157 4.170   1.00 11.85 ?  96  VAL   B N    1 
ATOM   5384 C CA   . VAL   B 1 96  ? 40.868 -20.068 5.309   1.00 12.15 ?  96  VAL   B CA   1 
ATOM   5385 C C    . VAL   B 1 96  ? 39.676 -21.020 5.260   1.00 12.70 ?  96  VAL   B C    1 
ATOM   5386 O O    . VAL   B 1 96  ? 38.559 -20.661 5.638   1.00 13.17 ?  96  VAL   B O    1 
ATOM   5387 C CB   . VAL   B 1 96  ? 40.917 -19.318 6.642   1.00 12.86 ?  96  VAL   B CB   1 
ATOM   5388 C CG1  . VAL   B 1 96  ? 41.096 -20.310 7.789   1.00 13.73 ?  96  VAL   B CG1  1 
ATOM   5389 C CG2  . VAL   B 1 96  ? 42.027 -18.277 6.643   1.00 13.49 ?  96  VAL   B CG2  1 
ATOM   5390 H H    . VAL   B 1 96  ? 40.216 -18.518 4.280   1.00 14.21 ?  96  VAL   B H    1 
ATOM   5391 H HA   . VAL   B 1 96  ? 41.678 -20.597 5.231   1.00 14.57 ?  96  VAL   B HA   1 
ATOM   5392 H HB   . VAL   B 1 96  ? 40.075 -18.858 6.774   1.00 15.42 ?  96  VAL   B HB   1 
ATOM   5393 H HG11 . VAL   B 1 96  ? 41.281 -19.818 8.605   1.00 16.47 ?  96  VAL   B HG11 1 
ATOM   5394 H HG12 . VAL   B 1 96  ? 40.283 -20.828 7.894   1.00 16.47 ?  96  VAL   B HG12 1 
ATOM   5395 H HG13 . VAL   B 1 96  ? 41.841 -20.899 7.586   1.00 16.47 ?  96  VAL   B HG13 1 
ATOM   5396 H HG21 . VAL   B 1 96  ? 42.079 -17.870 7.522   1.00 16.19 ?  96  VAL   B HG21 1 
ATOM   5397 H HG22 . VAL   B 1 96  ? 42.868 -18.707 6.427   1.00 16.19 ?  96  VAL   B HG22 1 
ATOM   5398 H HG23 . VAL   B 1 96  ? 41.824 -17.596 5.978   1.00 16.19 ?  96  VAL   B HG23 1 
ATOM   5399 N N    . GLY   B 1 97  ? 39.910 -22.254 4.822   1.00 12.54 ?  97  GLY   B N    1 
ATOM   5400 C CA   . GLY   B 1 97  ? 38.935 -23.307 4.981   1.00 13.08 ?  97  GLY   B CA   1 
ATOM   5401 C C    . GLY   B 1 97  ? 39.055 -23.910 6.362   1.00 14.16 ?  97  GLY   B C    1 
ATOM   5402 O O    . GLY   B 1 97  ? 40.096 -23.788 7.021   1.00 14.42 ?  97  GLY   B O    1 
ATOM   5403 H H    . GLY   B 1 97  ? 40.637 -22.500 4.423   1.00 15.05 ?  97  GLY   B H    1 
ATOM   5404 H HA2  . GLY   B 1 97  ? 38.043 -22.942 4.859   1.00 15.69 ?  97  GLY   B HA2  1 
ATOM   5405 H HA3  . GLY   B 1 97  ? 39.082 -23.997 4.311   1.00 15.69 ?  97  GLY   B HA3  1 
ATOM   5406 N N    . PRO   B 1 98  ? 38.007 -24.591 6.822   1.00 14.64 ?  98  PRO   B N    1 
ATOM   5407 C CA   . PRO   B 1 98  ? 38.098 -25.288 8.108   1.00 15.59 ?  98  PRO   B CA   1 
ATOM   5408 C C    . PRO   B 1 98  ? 39.123 -26.411 8.069   1.00 15.22 ?  98  PRO   B C    1 
ATOM   5409 O O    . PRO   B 1 98  ? 39.233 -27.150 7.090   1.00 15.31 ?  98  PRO   B O    1 
ATOM   5410 C CB   . PRO   B 1 98  ? 36.678 -25.829 8.313   1.00 15.79 ?  98  PRO   B CB   1 
ATOM   5411 C CG   . PRO   B 1 98  ? 36.129 -25.974 6.934   1.00 15.38 ?  98  PRO   B CG   1 
ATOM   5412 C CD   . PRO   B 1 98  ? 36.698 -24.799 6.177   1.00 14.60 ?  98  PRO   B CD   1 
ATOM   5413 H HA   . PRO   B 1 98  ? 38.322 -24.665 8.814   1.00 18.70 ?  98  PRO   B HA   1 
ATOM   5414 H HB2  . PRO   B 1 98  ? 36.719 -26.688 8.764   1.00 18.94 ?  98  PRO   B HB2  1 
ATOM   5415 H HB3  . PRO   B 1 98  ? 36.158 -25.193 8.825   1.00 18.94 ?  98  PRO   B HB3  1 
ATOM   5416 H HG2  . PRO   B 1 98  ? 36.434 -26.816 6.549   1.00 18.45 ?  98  PRO   B HG2  1 
ATOM   5417 H HG3  . PRO   B 1 98  ? 35.163 -25.940 6.961   1.00 18.45 ?  98  PRO   B HG3  1 
ATOM   5418 H HD2  . PRO   B 1 98  ? 36.805 -25.024 5.236   1.00 17.51 ?  98  PRO   B HD2  1 
ATOM   5419 H HD3  . PRO   B 1 98  ? 36.138 -24.018 6.295   1.00 17.51 ?  98  PRO   B HD3  1 
ATOM   5420 N N    . ASN   B 1 99  ? 39.870 -26.541 9.159   1.00 16.34 ?  99  ASN   B N    1 
ATOM   5421 C CA   . ASN   B 1 99  ? 40.850 -27.613 9.323   1.00 17.21 ?  99  ASN   B CA   1 
ATOM   5422 C C    . ASN   B 1 99  ? 40.221 -28.700 10.193  1.00 19.99 ?  99  ASN   B C    1 
ATOM   5423 O O    . ASN   B 1 99  ? 40.146 -28.565 11.416  1.00 20.66 ?  99  ASN   B O    1 
ATOM   5424 C CB   . ASN   B 1 99  ? 42.121 -27.060 9.954   1.00 17.56 ?  99  ASN   B CB   1 
ATOM   5425 C CG   . ASN   B 1 99  ? 43.251 -28.062 9.949   1.00 18.39 ?  99  ASN   B CG   1 
ATOM   5426 O OD1  . ASN   B 1 99  ? 43.025 -29.258 10.089  1.00 19.21 ?  99  ASN   B OD1  1 
ATOM   5427 N ND2  . ASN   B 1 99  ? 44.471 -27.582 9.783   1.00 18.74 ?  99  ASN   B ND2  1 
ATOM   5428 H H    . ASN   B 1 99  ? 39.832 -26.005 9.826   1.00 19.60 ?  99  ASN   B H    1 
ATOM   5429 H HA   . ASN   B 1 99  ? 41.070 -27.998 8.460   1.00 20.65 ?  99  ASN   B HA   1 
ATOM   5430 H HB2  . ASN   B 1 99  ? 42.406 -26.282 9.463   1.00 21.06 ?  99  ASN   B HB2  1 
ATOM   5431 H HB3  . ASN   B 1 99  ? 41.932 -26.824 10.879  1.00 21.06 ?  99  ASN   B HB3  1 
ATOM   5432 H HD21 . ASN   B 1 99  ? 45.146 -28.113 9.771   1.00 22.48 ?  99  ASN   B HD21 1 
ATOM   5433 H HD22 . ASN   B 1 99  ? 44.584 -26.736 9.687   1.00 22.48 ?  99  ASN   B HD22 1 
ATOM   5434 N N    A VAL   B 1 100 ? 39.755 -29.777 9.552   0.60 21.83 ?  100 VAL   B N    1 
ATOM   5435 N N    B VAL   B 1 100 ? 39.768 -29.780 9.550   0.40 21.97 ?  100 VAL   B N    1 
ATOM   5436 C CA   A VAL   B 1 100 ? 39.138 -30.876 10.293  0.60 24.47 ?  100 VAL   B CA   1 
ATOM   5437 C CA   B VAL   B 1 100 ? 39.145 -30.885 10.276  0.40 24.36 ?  100 VAL   B CA   1 
ATOM   5438 C C    A VAL   B 1 100 ? 40.142 -31.542 11.226  0.60 24.92 ?  100 VAL   B C    1 
ATOM   5439 C C    B VAL   B 1 100 ? 40.141 -31.546 11.217  0.40 24.92 ?  100 VAL   B C    1 
ATOM   5440 O O    A VAL   B 1 100 ? 39.766 -32.060 12.284  0.60 25.40 ?  100 VAL   B O    1 
ATOM   5441 O O    B VAL   B 1 100 ? 39.760 -32.059 12.277  0.40 25.25 ?  100 VAL   B O    1 
ATOM   5442 C CB   A VAL   B 1 100 ? 38.490 -31.886 9.324   0.60 26.92 ?  100 VAL   B CB   1 
ATOM   5443 C CB   B VAL   B 1 100 ? 38.531 -31.893 9.283   0.40 26.29 ?  100 VAL   B CB   1 
ATOM   5444 C CG1  A VAL   B 1 100 ? 38.009 -33.121 10.076  0.60 27.94 ?  100 VAL   B CG1  1 
ATOM   5445 C CG1  B VAL   B 1 100 ? 38.015 -33.125 10.015  0.40 27.08 ?  100 VAL   B CG1  1 
ATOM   5446 C CG2  A VAL   B 1 100 ? 37.335 -31.237 8.576   0.60 27.52 ?  100 VAL   B CG2  1 
ATOM   5447 C CG2  B VAL   B 1 100 ? 37.416 -31.235 8.490   0.40 26.82 ?  100 VAL   B CG2  1 
ATOM   5448 H H    A VAL   B 1 100 ? 39.771 -29.885 8.698   0.60 26.19 ?  100 VAL   B H    1 
ATOM   5449 H H    B VAL   B 1 100 ? 39.807 -29.892 8.698   0.40 26.36 ?  100 VAL   B H    1 
ATOM   5450 H HA   A VAL   B 1 100 ? 38.425 -30.511 10.839  0.60 29.36 ?  100 VAL   B HA   1 
ATOM   5451 H HA   B VAL   B 1 100 ? 38.421 -30.531 10.815  0.40 29.22 ?  100 VAL   B HA   1 
ATOM   5452 H HB   A VAL   B 1 100 ? 39.151 -32.170 8.675   0.60 32.29 ?  100 VAL   B HB   1 
ATOM   5453 H HB   B VAL   B 1 100 ? 39.216 -32.181 8.660   0.40 31.54 ?  100 VAL   B HB   1 
ATOM   5454 H HG11 A VAL   B 1 100 ? 37.421 -33.632 9.495   0.60 33.52 ?  100 VAL   B HG11 1 
ATOM   5455 H HG11 B VAL   B 1 100 ? 37.451 -33.635 9.411   0.40 32.49 ?  100 VAL   B HG11 1 
ATOM   5456 H HG12 A VAL   B 1 100 ? 38.774 -33.662 10.327  0.60 33.52 ?  100 VAL   B HG12 1 
ATOM   5457 H HG12 B VAL   B 1 100 ? 38.767 -33.668 10.299  0.40 32.49 ?  100 VAL   B HG12 1 
ATOM   5458 H HG13 A VAL   B 1 100 ? 37.524 -32.841 10.869  0.60 33.52 ?  100 VAL   B HG13 1 
ATOM   5459 H HG13 B VAL   B 1 100 ? 37.498 -32.842 10.786  0.40 32.49 ?  100 VAL   B HG13 1 
ATOM   5460 H HG21 A VAL   B 1 100 ? 36.942 -31.891 7.976   0.60 33.01 ?  100 VAL   B HG21 1 
ATOM   5461 H HG21 B VAL   B 1 100 ? 37.024 -31.891 7.893   0.40 32.17 ?  100 VAL   B HG21 1 
ATOM   5462 H HG22 A VAL   B 1 100 ? 36.671 -30.937 9.217   0.60 33.01 ?  100 VAL   B HG22 1 
ATOM   5463 H HG22 B VAL   B 1 100 ? 36.743 -30.905 9.107   0.40 32.17 ?  100 VAL   B HG22 1 
ATOM   5464 H HG23 A VAL   B 1 100 ? 37.671 -30.483 8.069   0.60 33.01 ?  100 VAL   B HG23 1 
ATOM   5465 H HG23 B VAL   B 1 100 ? 37.785 -30.499 7.978   0.40 32.17 ?  100 VAL   B HG23 1 
ATOM   5466 N N    . ASN   B 1 101 ? 41.423 -31.564 10.848  1.00 25.44 ?  101 ASN   B N    1 
ATOM   5467 C CA   . ASN   B 1 101 ? 42.455 -32.100 11.732  1.00 27.35 ?  101 ASN   B CA   1 
ATOM   5468 C C    . ASN   B 1 101 ? 42.643 -31.265 12.992  1.00 29.94 ?  101 ASN   B C    1 
ATOM   5469 O O    . ASN   B 1 101 ? 43.285 -31.738 13.937  1.00 31.32 ?  101 ASN   B O    1 
ATOM   5470 C CB   . ASN   B 1 101 ? 43.786 -32.230 10.987  1.00 27.43 ?  101 ASN   B CB   1 
ATOM   5471 C CG   . ASN   B 1 101 ? 43.787 -33.378 9.997   1.00 27.22 ?  101 ASN   B CG   1 
ATOM   5472 O OD1  . ASN   B 1 101 ? 43.134 -34.390 10.214  1.00 27.58 ?  101 ASN   B OD1  1 
ATOM   5473 N ND2  . ASN   B 1 101 ? 44.517 -33.221 8.901   1.00 26.90 ?  101 ASN   B ND2  1 
ATOM   5474 H H    A ASN   B 1 101 ? 41.710 -31.296 10.083  0.60 30.52 ?  101 ASN   B H    1 
ATOM   5475 H H    B ASN   B 1 101 ? 41.714 -31.284 10.089  0.40 30.52 ?  101 ASN   B H    1 
ATOM   5476 H HA   . ASN   B 1 101 ? 42.190 -32.986 12.011  1.00 32.81 ?  101 ASN   B HA   1 
ATOM   5477 H HB2  . ASN   B 1 101 ? 43.963 -31.415 10.496  1.00 32.90 ?  101 ASN   B HB2  1 
ATOM   5478 H HB3  . ASN   B 1 101 ? 44.495 -32.388 11.633  1.00 32.90 ?  101 ASN   B HB3  1 
ATOM   5479 H HD21 . ASN   B 1 101 ? 44.547 -33.848 8.313   1.00 32.27 ?  101 ASN   B HD21 1 
ATOM   5480 H HD22 . ASN   B 1 101 ? 44.955 -32.493 8.779   1.00 32.27 ?  101 ASN   B HD22 1 
ATOM   5481 N N    . LYS   B 1 102 ? 42.112 -30.041 13.020  1.00 32.27 ?  102 LYS   B N    1 
ATOM   5482 C CA   . LYS   B 1 102 ? 42.076 -29.206 14.214  1.00 35.06 ?  102 LYS   B CA   1 
ATOM   5483 C C    . LYS   B 1 102 ? 40.692 -29.161 14.847  1.00 34.59 ?  102 LYS   B C    1 
ATOM   5484 O O    . LYS   B 1 102 ? 40.462 -28.352 15.751  1.00 35.33 ?  102 LYS   B O    1 
ATOM   5485 C CB   . LYS   B 1 102 ? 42.515 -27.780 13.880  1.00 38.51 ?  102 LYS   B CB   1 
ATOM   5486 C CG   . LYS   B 1 102 ? 43.976 -27.622 13.503  1.00 41.80 ?  102 LYS   B CG   1 
ATOM   5487 C CD   . LYS   B 1 102 ? 44.248 -26.194 13.056  1.00 44.91 ?  102 LYS   B CD   1 
ATOM   5488 C CE   . LYS   B 1 102 ? 45.723 -25.944 12.801  1.00 47.21 ?  102 LYS   B CE   1 
ATOM   5489 N NZ   . LYS   B 1 102 ? 45.962 -24.548 12.328  1.00 48.60 ?  102 LYS   B NZ   1 
ATOM   5490 H H    . LYS   B 1 102 ? 41.752 -29.664 12.338  1.00 38.72 ?  102 LYS   B H    1 
ATOM   5491 H HA   . LYS   B 1 102 ? 42.698 -29.561 14.867  1.00 42.07 ?  102 LYS   B HA   1 
ATOM   5492 H HB2  . LYS   B 1 102 ? 41.984 -27.461 13.134  1.00 46.20 ?  102 LYS   B HB2  1 
ATOM   5493 H HB3  . LYS   B 1 102 ? 42.352 -27.218 14.655  1.00 46.20 ?  102 LYS   B HB3  1 
ATOM   5494 H HG2  . LYS   B 1 102 ? 44.533 -27.816 14.273  1.00 50.16 ?  102 LYS   B HG2  1 
ATOM   5495 H HG3  . LYS   B 1 102 ? 44.188 -28.221 12.770  1.00 50.16 ?  102 LYS   B HG3  1 
ATOM   5496 H HD2  . LYS   B 1 102 ? 43.766 -26.022 12.232  1.00 53.89 ?  102 LYS   B HD2  1 
ATOM   5497 H HD3  . LYS   B 1 102 ? 43.952 -25.582 13.749  1.00 53.89 ?  102 LYS   B HD3  1 
ATOM   5498 H HE2  . LYS   B 1 102 ? 46.218 -26.075 13.626  1.00 56.65 ?  102 LYS   B HE2  1 
ATOM   5499 H HE3  . LYS   B 1 102 ? 46.040 -26.556 12.119  1.00 56.65 ?  102 LYS   B HE3  1 
ATOM   5500 H HZ1  . LYS   B 1 102 ? 46.831 -24.420 12.185  1.00 58.32 ?  102 LYS   B HZ1  1 
ATOM   5501 H HZ2  . LYS   B 1 102 ? 45.519 -24.405 11.569  1.00 58.32 ?  102 LYS   B HZ2  1 
ATOM   5502 H HZ3  . LYS   B 1 102 ? 45.681 -23.967 12.941  1.00 58.32 ?  102 LYS   B HZ3  1 
ATOM   5503 N N    . GLY   B 1 103 ? 39.760 -29.988 14.379  1.00 33.68 ?  103 GLY   B N    1 
ATOM   5504 C CA   . GLY   B 1 103 ? 38.429 -30.034 14.947  1.00 33.09 ?  103 GLY   B CA   1 
ATOM   5505 C C    . GLY   B 1 103 ? 37.496 -28.933 14.496  1.00 32.05 ?  103 GLY   B C    1 
ATOM   5506 O O    . GLY   B 1 103 ? 36.415 -28.785 15.077  1.00 32.60 ?  103 GLY   B O    1 
ATOM   5507 H H    . GLY   B 1 103 ? 39.879 -30.533 13.726  1.00 40.41 ?  103 GLY   B H    1 
ATOM   5508 H HA2  . GLY   B 1 103 ? 38.020 -30.882 14.718  1.00 39.70 ?  103 GLY   B HA2  1 
ATOM   5509 H HA3  . GLY   B 1 103 ? 38.498 -29.986 15.913  1.00 39.70 ?  103 GLY   B HA3  1 
ATOM   5510 N N    A GLU   B 1 104 ? 37.881 -28.151 13.491  0.60 31.03 ?  104 GLU   B N    1 
ATOM   5511 N N    B GLU   B 1 104 ? 37.864 -28.166 13.475  0.40 31.14 ?  104 GLU   B N    1 
ATOM   5512 C CA   A GLU   B 1 104 ? 37.052 -27.051 13.027  0.60 29.92 ?  104 GLU   B CA   1 
ATOM   5513 C CA   B GLU   B 1 104 ? 37.014 -27.084 13.004  0.40 30.09 ?  104 GLU   B CA   1 
ATOM   5514 C C    A GLU   B 1 104 ? 35.870 -27.575 12.211  0.60 30.33 ?  104 GLU   B C    1 
ATOM   5515 C C    B GLU   B 1 104 ? 35.859 -27.627 12.167  0.40 30.24 ?  104 GLU   B C    1 
ATOM   5516 O O    A GLU   B 1 104 ? 35.909 -28.665 11.633  0.60 30.77 ?  104 GLU   B O    1 
ATOM   5517 O O    B GLU   B 1 104 ? 35.943 -28.707 11.575  0.40 30.53 ?  104 GLU   B O    1 
ATOM   5518 C CB   A GLU   B 1 104 ? 37.896 -26.056 12.227  0.60 28.62 ?  104 GLU   B CB   1 
ATOM   5519 C CB   B GLU   B 1 104 ? 37.842 -26.069 12.215  0.40 29.01 ?  104 GLU   B CB   1 
ATOM   5520 C CG   A GLU   B 1 104 ? 38.999 -25.422 13.071  0.60 27.25 ?  104 GLU   B CG   1 
ATOM   5521 C CG   B GLU   B 1 104 ? 38.917 -25.413 13.073  0.40 27.98 ?  104 GLU   B CG   1 
ATOM   5522 C CD   A GLU   B 1 104 ? 39.936 -24.529 12.284  0.60 25.91 ?  104 GLU   B CD   1 
ATOM   5523 C CD   B GLU   B 1 104 ? 39.883 -24.554 12.283  0.40 27.07 ?  104 GLU   B CD   1 
ATOM   5524 O OE1  A GLU   B 1 104 ? 39.920 -24.570 11.036  0.60 24.18 ?  104 GLU   B OE1  1 
ATOM   5525 O OE1  B GLU   B 1 104 ? 39.841 -24.581 11.035  0.40 26.21 ?  104 GLU   B OE1  1 
ATOM   5526 O OE2  A GLU   B 1 104 ? 40.698 -23.780 12.929  0.60 25.84 -1 104 GLU   B OE2  1 
ATOM   5527 O OE2  B GLU   B 1 104 ? 40.693 -23.849 12.920  0.40 26.90 -1 104 GLU   B OE2  1 
ATOM   5528 H H    A GLU   B 1 104 ? 38.626 -28.235 13.068  0.60 37.23 ?  104 GLU   B H    1 
ATOM   5529 H H    B GLU   B 1 104 ? 38.603 -28.249 13.044  0.40 37.36 ?  104 GLU   B H    1 
ATOM   5530 H HA   A GLU   B 1 104 ? 36.699 -26.581 13.799  0.60 35.90 ?  104 GLU   B HA   1 
ATOM   5531 H HA   B GLU   B 1 104 ? 36.638 -26.627 13.770  0.40 36.10 ?  104 GLU   B HA   1 
ATOM   5532 H HB2  A GLU   B 1 104 ? 38.313 -26.517 11.483  0.60 34.33 ?  104 GLU   B HB2  1 
ATOM   5533 H HB2  B GLU   B 1 104 ? 38.278 -26.518 11.475  0.40 34.81 ?  104 GLU   B HB2  1 
ATOM   5534 H HB3  A GLU   B 1 104 ? 37.323 -25.344 11.899  0.60 34.33 ?  104 GLU   B HB3  1 
ATOM   5535 H HB3  B GLU   B 1 104 ? 37.254 -25.371 11.882  0.40 34.81 ?  104 GLU   B HB3  1 
ATOM   5536 H HG2  A GLU   B 1 104 ? 38.595 -24.880 13.767  0.60 32.70 ?  104 GLU   B HG2  1 
ATOM   5537 H HG2  B GLU   B 1 104 ? 38.488 -24.848 13.736  0.40 33.57 ?  104 GLU   B HG2  1 
ATOM   5538 H HG3  A GLU   B 1 104 ? 39.535 -26.124 13.473  0.60 32.70 ?  104 GLU   B HG3  1 
ATOM   5539 H HG3  B GLU   B 1 104 ? 39.431 -26.105 13.518  0.40 33.57 ?  104 GLU   B HG3  1 
ATOM   5540 N N    A ASP   B 1 105 ? 34.805 -26.775 12.176  0.60 29.96 ?  105 ASP   B N    1 
ATOM   5541 N N    B ASP   B 1 105 ? 34.771 -26.860 12.129  0.40 29.81 ?  105 ASP   B N    1 
ATOM   5542 C CA   A ASP   B 1 105 ? 33.528 -27.225 11.635  0.60 30.35 ?  105 ASP   B CA   1 
ATOM   5543 C CA   B ASP   B 1 105 ? 33.508 -27.336 11.575  0.40 29.87 ?  105 ASP   B CA   1 
ATOM   5544 C C    A ASP   B 1 105 ? 33.581 -27.277 10.112  0.60 27.97 ?  105 ASP   B C    1 
ATOM   5545 C C    B ASP   B 1 105 ? 33.574 -27.349 10.052  0.40 28.42 ?  105 ASP   B C    1 
ATOM   5546 O O    A ASP   B 1 105 ? 33.733 -26.245 9.450   0.60 26.83 ?  105 ASP   B O    1 
ATOM   5547 O O    B ASP   B 1 105 ? 33.765 -26.304 9.420   0.40 27.77 ?  105 ASP   B O    1 
ATOM   5548 C CB   A ASP   B 1 105 ? 32.414 -26.287 12.097  0.60 33.19 ?  105 ASP   B CB   1 
ATOM   5549 C CB   B ASP   B 1 105 ? 32.361 -26.448 12.056  0.40 31.34 ?  105 ASP   B CB   1 
ATOM   5550 C CG   A ASP   B 1 105 ? 31.038 -26.759 11.669  0.60 35.76 ?  105 ASP   B CG   1 
ATOM   5551 C CG   B ASP   B 1 105 ? 30.997 -27.030 11.727  0.40 32.71 ?  105 ASP   B CG   1 
ATOM   5552 O OD1  A ASP   B 1 105 ? 30.931 -27.873 11.116  0.60 36.13 ?  105 ASP   B OD1  1 
ATOM   5553 O OD1  B ASP   B 1 105 ? 30.940 -28.035 10.987  0.40 32.93 ?  105 ASP   B OD1  1 
ATOM   5554 O OD2  A ASP   B 1 105 ? 30.062 -26.007 11.880  0.60 37.12 -1 105 ASP   B OD2  1 
ATOM   5555 O OD2  B ASP   B 1 105 ? 29.982 -26.491 12.217  0.40 33.20 -1 105 ASP   B OD2  1 
ATOM   5556 H H    A ASP   B 1 105 ? 34.800 -25.965 12.459  0.60 35.95 ?  105 ASP   B H    1 
ATOM   5557 H H    B ASP   B 1 105 ? 34.741 -26.052 12.416  0.40 35.76 ?  105 ASP   B H    1 
ATOM   5558 H HA   A ASP   B 1 105 ? 33.333 -28.116 11.966  0.60 36.41 ?  105 ASP   B HA   1 
ATOM   5559 H HA   B ASP   B 1 105 ? 33.337 -28.240 11.881  0.40 35.84 ?  105 ASP   B HA   1 
ATOM   5560 H HB2  A ASP   B 1 105 ? 32.436 -26.221 13.067  0.60 39.82 ?  105 ASP   B HB2  1 
ATOM   5561 H HB2  B ASP   B 1 105 ? 32.419 -26.350 13.021  0.40 37.60 ?  105 ASP   B HB2  1 
ATOM   5562 H HB3  A ASP   B 1 105 ? 32.549 -25.413 11.703  0.60 39.82 ?  105 ASP   B HB3  1 
ATOM   5563 H HB3  B ASP   B 1 105 ? 32.435 -25.576 11.632  0.40 37.60 ?  105 ASP   B HB3  1 
ATOM   5564 N N    A ILE   B 1 106 ? 33.436 -28.484 9.559   0.60 27.08 ?  106 ILE   B N    1 
ATOM   5565 N N    B ILE   B 1 106 ? 33.400 -28.537 9.465   0.40 27.67 ?  106 ILE   B N    1 
ATOM   5566 C CA   A ILE   B 1 106 ? 33.434 -28.669 8.112   0.60 25.99 ?  106 ILE   B CA   1 
ATOM   5567 C CA   B ILE   B 1 106 ? 33.409 -28.684 8.015   0.40 26.99 ?  106 ILE   B CA   1 
ATOM   5568 C C    A ILE   B 1 106 ? 32.340 -27.850 7.436   0.60 24.60 ?  106 ILE   B C    1 
ATOM   5569 C C    B ILE   B 1 106 ? 32.313 -27.856 7.355   0.40 26.07 ?  106 ILE   B C    1 
ATOM   5570 O O    A ILE   B 1 106 ? 32.449 -27.536 6.245   0.60 23.79 ?  106 ILE   B O    1 
ATOM   5571 O O    B ILE   B 1 106 ? 32.408 -27.542 6.163   0.40 25.57 ?  106 ILE   B O    1 
ATOM   5572 C CB   A ILE   B 1 106 ? 33.326 -30.177 7.783   0.60 26.79 ?  106 ILE   B CB   1 
ATOM   5573 C CB   B ILE   B 1 106 ? 33.309 -30.182 7.643   0.40 27.49 ?  106 ILE   B CB   1 
ATOM   5574 C CG1  A ILE   B 1 106 ? 33.588 -30.435 6.299   0.60 27.07 ?  106 ILE   B CG1  1 
ATOM   5575 C CG1  B ILE   B 1 106 ? 33.618 -30.401 6.160   0.40 27.63 ?  106 ILE   B CG1  1 
ATOM   5576 C CG2  A ILE   B 1 106 ? 31.959 -30.719 8.183   0.60 27.51 ?  106 ILE   B CG2  1 
ATOM   5577 C CG2  B ILE   B 1 106 ? 31.930 -30.730 7.982   0.40 27.95 ?  106 ILE   B CG2  1 
ATOM   5578 C CD1  A ILE   B 1 106 ? 34.954 -29.985 5.840   0.60 27.00 ?  106 ILE   B CD1  1 
ATOM   5579 C CD1  B ILE   B 1 106 ? 34.993 -29.929 5.751   0.40 27.65 ?  106 ILE   B CD1  1 
ATOM   5580 H H    A ILE   B 1 106 ? 33.346 -29.210 10.006  0.60 32.49 ?  106 ILE   B H    1 
ATOM   5581 H H    B ILE   B 1 106 ? 33.285 -29.273 9.890   0.40 33.19 ?  106 ILE   B H    1 
ATOM   5582 H HA   A ILE   B 1 106 ? 34.282 -28.353 7.771   0.60 31.18 ?  106 ILE   B HA   1 
ATOM   5583 H HA   B ILE   B 1 106 ? 34.255 -28.352 7.686   0.40 32.39 ?  106 ILE   B HA   1 
ATOM   5584 H HB   A ILE   B 1 106 ? 33.999 -30.649 8.297   0.60 32.14 ?  106 ILE   B HB   1 
ATOM   5585 H HB   B ILE   B 1 106 ? 33.965 -30.670 8.164   0.40 32.98 ?  106 ILE   B HB   1 
ATOM   5586 H HG12 A ILE   B 1 106 ? 33.522 -31.389 6.131   0.60 32.48 ?  106 ILE   B HG12 1 
ATOM   5587 H HG12 B ILE   B 1 106 ? 33.565 -31.352 5.967   0.40 33.15 ?  106 ILE   B HG12 1 
ATOM   5588 H HG13 A ILE   B 1 106 ? 32.927 -29.962 5.773   0.60 32.48 ?  106 ILE   B HG13 1 
ATOM   5589 H HG13 B ILE   B 1 106 ? 32.967 -29.922 5.627   0.40 33.15 ?  106 ILE   B HG13 1 
ATOM   5590 H HG21 A ILE   B 1 106 ? 31.969 -31.686 8.105   0.60 33.00 ?  106 ILE   B HG21 1 
ATOM   5591 H HG21 B ILE   B 1 106 ? 31.948 -31.698 7.908   0.40 33.54 ?  106 ILE   B HG21 1 
ATOM   5592 H HG22 A ILE   B 1 106 ? 31.774 -30.463 9.100   0.60 33.00 ?  106 ILE   B HG22 1 
ATOM   5593 H HG22 B ILE   B 1 106 ? 31.704 -30.473 8.889   0.40 33.54 ?  106 ILE   B HG22 1 
ATOM   5594 H HG23 A ILE   B 1 106 ? 31.285 -30.347 7.593   0.60 33.00 ?  106 ILE   B HG23 1 
ATOM   5595 H HG23 B ILE   B 1 106 ? 31.280 -30.364 7.362   0.40 33.54 ?  106 ILE   B HG23 1 
ATOM   5596 H HD11 A ILE   B 1 106 ? 35.153 -30.400 4.987   0.60 32.40 ?  106 ILE   B HD11 1 
ATOM   5597 H HD11 B ILE   B 1 106 ? 35.224 -30.333 4.902   0.40 33.18 ?  106 ILE   B HD11 1 
ATOM   5598 H HD12 A ILE   B 1 106 ? 34.955 -29.019 5.745   0.60 32.40 ?  106 ILE   B HD12 1 
ATOM   5599 H HD12 B ILE   B 1 106 ? 34.982 -28.962 5.665   0.40 33.18 ?  106 ILE   B HD12 1 
ATOM   5600 H HD13 A ILE   B 1 106 ? 35.614 -30.254 6.500   0.60 32.40 ?  106 ILE   B HD13 1 
ATOM   5601 H HD13 B ILE   B 1 106 ? 35.633 -30.195 6.430   0.40 33.18 ?  106 ILE   B HD13 1 
ATOM   5602 N N    A GLN   B 1 107 ? 31.288 -27.479 8.170   0.60 25.04 ?  107 GLN   B N    1 
ATOM   5603 N N    B GLN   B 1 107 ? 31.270 -27.488 8.103   0.40 26.18 ?  107 GLN   B N    1 
ATOM   5604 C CA   A GLN   B 1 107 ? 30.209 -26.693 7.582   0.60 25.93 ?  107 GLN   B CA   1 
ATOM   5605 C CA   B GLN   B 1 107 ? 30.192 -26.681 7.540   0.40 26.51 ?  107 GLN   B CA   1 
ATOM   5606 C C    A GLN   B 1 107 ? 30.691 -25.343 7.063   0.60 23.61 ?  107 GLN   B C    1 
ATOM   5607 C C    B GLN   B 1 107 ? 30.674 -25.313 7.073   0.40 23.99 ?  107 GLN   B C    1 
ATOM   5608 O O    A GLN   B 1 107 ? 30.054 -24.773 6.172   0.60 23.86 ?  107 GLN   B O    1 
ATOM   5609 O O    B GLN   B 1 107 ? 30.015 -24.694 6.232   0.40 24.31 ?  107 GLN   B O    1 
ATOM   5610 C CB   A GLN   B 1 107 ? 29.093 -26.492 8.612   0.60 30.04 ?  107 GLN   B CB   1 
ATOM   5611 C CB   B GLN   B 1 107 ? 29.069 -26.526 8.570   0.40 29.79 ?  107 GLN   B CB   1 
ATOM   5612 C CG   A GLN   B 1 107 ? 27.774 -25.975 8.040   0.60 33.91 ?  107 GLN   B CG   1 
ATOM   5613 C CG   B GLN   B 1 107 ? 27.742 -26.036 7.999   0.40 32.83 ?  107 GLN   B CG   1 
ATOM   5614 C CD   A GLN   B 1 107 ? 27.719 -24.460 7.947   0.60 36.94 ?  107 GLN   B CD   1 
ATOM   5615 C CD   B GLN   B 1 107 ? 27.616 -24.523 8.007   0.40 35.24 ?  107 GLN   B CD   1 
ATOM   5616 O OE1  A GLN   B 1 107 ? 28.556 -23.759 8.518   0.60 38.10 ?  107 GLN   B OE1  1 
ATOM   5617 O OE1  B GLN   B 1 107 ? 28.445 -23.821 8.587   0.40 36.15 ?  107 GLN   B OE1  1 
ATOM   5618 N NE2  A GLN   B 1 107 ? 26.725 -23.947 7.226   0.60 37.91 ?  107 GLN   B NE2  1 
ATOM   5619 N NE2  B GLN   B 1 107 ? 26.570 -24.014 7.364   0.40 36.03 ?  107 GLN   B NE2  1 
ATOM   5620 H H    A GLN   B 1 107 ? 31.184 -27.660 9.001   0.60 30.04 ?  107 GLN   B H    1 
ATOM   5621 H H    B GLN   B 1 107 ? 31.161 -27.694 8.928   0.40 31.41 ?  107 GLN   B H    1 
ATOM   5622 H HA   A GLN   B 1 107 ? 29.835 -27.186 6.834   0.60 31.11 ?  107 GLN   B HA   1 
ATOM   5623 H HA   B GLN   B 1 107 ? 29.824 -27.145 6.772   0.40 31.81 ?  107 GLN   B HA   1 
ATOM   5624 H HB2  A GLN   B 1 107 ? 28.912 -27.343 9.035   0.60 36.05 ?  107 GLN   B HB2  1 
ATOM   5625 H HB2  B GLN   B 1 107 ? 28.906 -27.388 8.979   0.40 35.74 ?  107 GLN   B HB2  1 
ATOM   5626 H HB3  A GLN   B 1 107 ? 29.396 -25.855 9.277   0.60 36.05 ?  107 GLN   B HB3  1 
ATOM   5627 H HB3  B GLN   B 1 107 ? 29.351 -25.893 9.248   0.40 35.74 ?  107 GLN   B HB3  1 
ATOM   5628 H HG2  A GLN   B 1 107 ? 27.653 -26.332 7.147   0.60 40.69 ?  107 GLN   B HG2  1 
ATOM   5629 H HG2  B GLN   B 1 107 ? 27.660 -26.337 7.081   0.40 39.39 ?  107 GLN   B HG2  1 
ATOM   5630 H HG3  A GLN   B 1 107 ? 27.045 -26.270 8.613   0.60 40.69 ?  107 GLN   B HG3  1 
ATOM   5631 H HG3  B GLN   B 1 107 ? 27.015 -26.403 8.531   0.40 39.39 ?  107 GLN   B HG3  1 
ATOM   5632 H HE21 A GLN   B 1 107 ? 26.158 -24.467 6.839   0.60 45.49 ?  107 GLN   B HE21 1 
ATOM   5633 H HE21 B GLN   B 1 107 ? 26.011 -24.535 6.969   0.40 43.23 ?  107 GLN   B HE21 1 
ATOM   5634 H HE22 A GLN   B 1 107 ? 26.646 -23.093 7.146   0.60 45.49 ?  107 GLN   B HE22 1 
ATOM   5635 H HE22 B GLN   B 1 107 ? 26.452 -23.162 7.343   0.40 43.23 ?  107 GLN   B HE22 1 
ATOM   5636 N N    . LEU   B 1 108 ? 31.809 -24.830 7.584   1.00 21.61 ?  108 LEU   B N    1 
ATOM   5637 C CA   . LEU   B 1 108 ? 32.349 -23.533 7.176   1.00 19.13 ?  108 LEU   B CA   1 
ATOM   5638 C C    . LEU   B 1 108 ? 33.005 -23.555 5.804   1.00 16.92 ?  108 LEU   B C    1 
ATOM   5639 O O    . LEU   B 1 108 ? 33.434 -22.496 5.317   1.00 16.37 ?  108 LEU   B O    1 
ATOM   5640 C CB   . LEU   B 1 108 ? 33.349 -23.036 8.219   1.00 19.73 ?  108 LEU   B CB   1 
ATOM   5641 C CG   . LEU   B 1 108 ? 32.720 -22.538 9.518   1.00 21.22 ?  108 LEU   B CG   1 
ATOM   5642 C CD1  . LEU   B 1 108 ? 33.734 -22.498 10.645  1.00 21.56 ?  108 LEU   B CD1  1 
ATOM   5643 C CD2  . LEU   B 1 108 ? 32.126 -21.157 9.301   1.00 22.39 ?  108 LEU   B CD2  1 
ATOM   5644 H H    A LEU   B 1 108 ? 32.269 -25.219 8.195   0.60 25.92 ?  108 LEU   B H    1 
ATOM   5645 H H    B LEU   B 1 108 ? 32.279 -25.235 8.176   0.40 25.92 ?  108 LEU   B H    1 
ATOM   5646 H HA   . LEU   B 1 108 ? 31.620 -22.896 7.138   1.00 22.95 ?  108 LEU   B HA   1 
ATOM   5647 H HB2  . LEU   B 1 108 ? 33.946 -23.762 8.446   1.00 23.66 ?  108 LEU   B HB2  1 
ATOM   5648 H HB3  . LEU   B 1 108 ? 33.852 -22.301 7.838   1.00 23.66 ?  108 LEU   B HB3  1 
ATOM   5649 H HG   . LEU   B 1 108 ? 31.999 -23.136 9.778   1.00 25.45 ?  108 LEU   B HG   1 
ATOM   5650 H HD11 . LEU   B 1 108 ? 33.294 -22.195 11.457  1.00 25.87 ?  108 LEU   B HD11 1 
ATOM   5651 H HD12 . LEU   B 1 108 ? 34.093 -23.388 10.778  1.00 25.87 ?  108 LEU   B HD12 1 
ATOM   5652 H HD13 . LEU   B 1 108 ? 34.445 -21.883 10.408  1.00 25.87 ?  108 LEU   B HD13 1 
ATOM   5653 H HD21 . LEU   B 1 108 ? 31.768 -20.831 10.142  1.00 26.86 ?  108 LEU   B HD21 1 
ATOM   5654 H HD22 . LEU   B 1 108 ? 32.822 -20.561 8.984   1.00 26.86 ?  108 LEU   B HD22 1 
ATOM   5655 H HD23 . LEU   B 1 108 ? 31.416 -21.217 8.642   1.00 26.86 ?  108 LEU   B HD23 1 
ATOM   5656 N N    . LEU   B 1 109 ? 33.077 -24.722 5.170   1.00 15.94 ?  109 LEU   B N    1 
ATOM   5657 C CA   . LEU   B 1 109 ? 33.713 -24.828 3.865   1.00 14.90 ?  109 LEU   B CA   1 
ATOM   5658 C C    . LEU   B 1 109 ? 32.951 -24.044 2.806   1.00 14.17 ?  109 LEU   B C    1 
ATOM   5659 O O    . LEU   B 1 109 ? 33.566 -23.458 1.905   1.00 13.71 ?  109 LEU   B O    1 
ATOM   5660 C CB   . LEU   B 1 109 ? 33.820 -26.302 3.482   1.00 15.14 ?  109 LEU   B CB   1 
ATOM   5661 C CG   . LEU   B 1 109 ? 34.614 -26.644 2.227   1.00 14.85 ?  109 LEU   B CG   1 
ATOM   5662 C CD1  . LEU   B 1 109 ? 35.994 -25.995 2.251   1.00 14.66 ?  109 LEU   B CD1  1 
ATOM   5663 C CD2  . LEU   B 1 109 ? 34.746 -28.155 2.099   1.00 15.65 ?  109 LEU   B CD2  1 
ATOM   5664 H H    . LEU   B 1 109 ? 32.772 -25.465 5.471   1.00 19.12 ?  109 LEU   B H    1 
ATOM   5665 H HA   . LEU   B 1 109 ? 34.609 -24.465 3.917   1.00 17.88 ?  109 LEU   B HA   1 
ATOM   5666 H HB2  . LEU   B 1 109 ? 34.238 -26.776 4.218   1.00 18.16 ?  109 LEU   B HB2  1 
ATOM   5667 H HB3  . LEU   B 1 109 ? 32.922 -26.649 3.352   1.00 18.16 ?  109 LEU   B HB3  1 
ATOM   5668 H HG   . LEU   B 1 109 ? 34.136 -26.325 1.444   1.00 17.82 ?  109 LEU   B HG   1 
ATOM   5669 H HD11 . LEU   B 1 109 ? 36.532 -26.367 1.534   1.00 17.59 ?  109 LEU   B HD11 1 
ATOM   5670 H HD12 . LEU   B 1 109 ? 35.892 -25.040 2.128   1.00 17.59 ?  109 LEU   B HD12 1 
ATOM   5671 H HD13 . LEU   B 1 109 ? 36.412 -26.180 3.106   1.00 17.59 ?  109 LEU   B HD13 1 
ATOM   5672 H HD21 . LEU   B 1 109 ? 35.318 -28.361 1.342   1.00 18.77 ?  109 LEU   B HD21 1 
ATOM   5673 H HD22 . LEU   B 1 109 ? 35.133 -28.510 2.913   1.00 18.77 ?  109 LEU   B HD22 1 
ATOM   5674 H HD23 . LEU   B 1 109 ? 33.864 -28.542 1.958   1.00 18.77 ?  109 LEU   B HD23 1 
ATOM   5675 N N    . LYS   B 1 110 ? 31.617 -24.014 2.886   1.00 13.94 ?  110 LYS   B N    1 
ATOM   5676 C CA   . LYS   B 1 110 ? 30.861 -23.252 1.896   1.00 13.87 ?  110 LYS   B CA   1 
ATOM   5677 C C    . LYS   B 1 110 ? 31.200 -21.765 1.980   1.00 13.64 ?  110 LYS   B C    1 
ATOM   5678 O O    . LYS   B 1 110 ? 31.456 -21.117 0.960   1.00 13.41 ?  110 LYS   B O    1 
ATOM   5679 C CB   . LYS   B 1 110 ? 29.354 -23.496 2.040   1.00 14.52 ?  110 LYS   B CB   1 
ATOM   5680 C CG   . LYS   B 1 110 ? 28.555 -22.876 0.896   1.00 14.92 ?  110 LYS   B CG   1 
ATOM   5681 C CD   . LYS   B 1 110 ? 27.090 -23.304 0.908   1.00 14.90 ?  110 LYS   B CD   1 
ATOM   5682 C CE   . LYS   B 1 110 ? 26.333 -22.770 -0.308  1.00 15.78 ?  110 LYS   B CE   1 
ATOM   5683 N NZ   . LYS   B 1 110 ? 26.659 -23.502 -1.564  1.00 15.99 ?  110 LYS   B NZ   1 
ATOM   5684 H H    . LYS   B 1 110 ? 31.146 -24.418 3.476   1.00 16.73 ?  110 LYS   B H    1 
ATOM   5685 H HA   . LYS   B 1 110 ? 31.117 -23.555 1.011   1.00 16.64 ?  110 LYS   B HA   1 
ATOM   5686 H HB2  . LYS   B 1 110 ? 29.186 -24.455 2.036   1.00 17.42 ?  110 LYS   B HB2  1 
ATOM   5687 H HB3  . LYS   B 1 110 ? 29.043 -23.109 2.871   1.00 17.42 ?  110 LYS   B HB3  1 
ATOM   5688 H HG2  . LYS   B 1 110 ? 28.580 -21.909 0.977   1.00 17.89 ?  110 LYS   B HG2  1 
ATOM   5689 H HG3  . LYS   B 1 110 ? 28.938 -23.149 0.050   1.00 17.89 ?  110 LYS   B HG3  1 
ATOM   5690 H HD2  . LYS   B 1 110 ? 27.041 -24.276 0.892   1.00 17.88 ?  110 LYS   B HD2  1 
ATOM   5691 H HD3  . LYS   B 1 110 ? 26.661 -22.963 1.708   1.00 17.88 ?  110 LYS   B HD3  1 
ATOM   5692 H HE2  . LYS   B 1 110 ? 25.383 -22.850 -0.152  1.00 18.93 ?  110 LYS   B HE2  1 
ATOM   5693 H HE3  . LYS   B 1 110 ? 26.573 -21.836 -0.438  1.00 18.93 ?  110 LYS   B HE3  1 
ATOM   5694 H HZ1  . LYS   B 1 110 ? 26.203 -23.157 -2.244  1.00 19.18 ?  110 LYS   B HZ1  1 
ATOM   5695 H HZ2  . LYS   B 1 110 ? 27.531 -23.437 -1.737  1.00 19.18 ?  110 LYS   B HZ2  1 
ATOM   5696 H HZ3  . LYS   B 1 110 ? 26.447 -24.361 -1.476  1.00 19.18 ?  110 LYS   B HZ3  1 
ATOM   5697 N N    . SER   B 1 111 ? 31.227 -21.214 3.198   1.00 13.89 ?  111 SER   B N    1 
ATOM   5698 C CA   . SER   B 1 111 ? 31.615 -19.816 3.376   1.00 13.64 ?  111 SER   B CA   1 
ATOM   5699 C C    . SER   B 1 111 ? 32.998 -19.556 2.793   1.00 13.34 ?  111 SER   B C    1 
ATOM   5700 O O    . SER   B 1 111 ? 33.227 -18.526 2.144   1.00 13.74 ?  111 SER   B O    1 
ATOM   5701 C CB   . SER   B 1 111 ? 31.601 -19.465 4.862   1.00 14.83 ?  111 SER   B CB   1 
ATOM   5702 O OG   . SER   B 1 111 ? 30.291 -19.468 5.387   1.00 16.46 ?  111 SER   B OG   1 
ATOM   5703 H H    . SER   B 1 111 ? 31.034 -21.631 3.926   1.00 16.66 ?  111 SER   B H    1 
ATOM   5704 H HA   . SER   B 1 111 ? 30.980 -19.248 2.919   1.00 16.36 ?  111 SER   B HA   1 
ATOM   5705 H HB2  . SER   B 1 111 ? 32.126 -20.121 5.348   1.00 17.79 ?  111 SER   B HB2  1 
ATOM   5706 H HB3  . SER   B 1 111 ? 31.981 -18.584 4.981   1.00 17.79 ?  111 SER   B HB3  1 
ATOM   5707 H HG   . SER   B 1 111 ? 30.303 -19.269 6.208   1.00 19.74 ?  111 SER   B HG   1 
ATOM   5708 N N    . ALA   B 1 112 ? 33.936 -20.475 3.023   1.00 13.37 ?  112 ALA   B N    1 
ATOM   5709 C CA   . ALA   B 1 112 ? 35.280 -20.308 2.481   1.00 12.71 ?  112 ALA   B CA   1 
ATOM   5710 C C    . ALA   B 1 112 ? 35.249 -20.216 0.958   1.00 12.21 ?  112 ALA   B C    1 
ATOM   5711 O O    . ALA   B 1 112 ? 35.875 -19.330 0.360   1.00 12.64 ?  112 ALA   B O    1 
ATOM   5712 C CB   . ALA   B 1 112 ? 36.177 -21.453 2.962   1.00 13.56 ?  112 ALA   B CB   1 
ATOM   5713 H H    . ALA   B 1 112 ? 33.823 -21.196 3.494   1.00 16.04 ?  112 ALA   B H    1 
ATOM   5714 H HA   . ALA   B 1 112 ? 35.648 -19.481 2.825   1.00 15.24 ?  112 ALA   B HA   1 
ATOM   5715 H HB1  . ALA   B 1 112 ? 37.070 -21.321 2.598   1.00 16.27 ?  112 ALA   B HB1  1 
ATOM   5716 H HB2  . ALA   B 1 112 ? 36.218 -21.436 3.934   1.00 16.27 ?  112 ALA   B HB2  1 
ATOM   5717 H HB3  . ALA   B 1 112 ? 35.814 -22.293 2.658   1.00 16.27 ?  112 ALA   B HB3  1 
ATOM   5718 N N    . TYR   B 1 113 ? 34.514 -21.121 0.307   1.00 12.41 ?  113 TYR   B N    1 
ATOM   5719 C CA   . TYR   B 1 113 ? 34.443 -21.074 -1.150  1.00 12.15 ?  113 TYR   B CA   1 
ATOM   5720 C C    . TYR   B 1 113 ? 33.737 -19.823 -1.670  1.00 11.89 ?  113 TYR   B C    1 
ATOM   5721 O O    . TYR   B 1 113 ? 34.012 -19.391 -2.796  1.00 11.85 ?  113 TYR   B O    1 
ATOM   5722 C CB   . TYR   B 1 113 ? 33.776 -22.335 -1.700  1.00 12.46 ?  113 TYR   B CB   1 
ATOM   5723 C CG   . TYR   B 1 113 ? 34.736 -23.485 -1.959  1.00 12.92 ?  113 TYR   B CG   1 
ATOM   5724 C CD1  . TYR   B 1 113 ? 35.728 -23.378 -2.924  1.00 13.48 ?  113 TYR   B CD1  1 
ATOM   5725 C CD2  . TYR   B 1 113 ? 34.625 -24.677 -1.264  1.00 13.06 ?  113 TYR   B CD2  1 
ATOM   5726 C CE1  . TYR   B 1 113 ? 36.605 -24.406 -3.171  1.00 13.32 ?  113 TYR   B CE1  1 
ATOM   5727 C CE2  . TYR   B 1 113 ? 35.500 -25.725 -1.505  1.00 13.56 ?  113 TYR   B CE2  1 
ATOM   5728 C CZ   . TYR   B 1 113 ? 36.481 -25.588 -2.464  1.00 13.43 ?  113 TYR   B CZ   1 
ATOM   5729 O OH   . TYR   B 1 113 ? 37.362 -26.608 -2.735  1.00 14.34 ?  113 TYR   B OH   1 
ATOM   5730 H H    . TYR   B 1 113 ? 34.049 -21.751 0.679   1.00 14.88 ?  113 TYR   B H    1 
ATOM   5731 H HA   . TYR   B 1 113 ? 35.345 -21.055 -1.483  1.00 14.57 ?  113 TYR   B HA   1 
ATOM   5732 H HB2  . TYR   B 1 113 ? 33.113 -22.649 -1.060  1.00 14.94 ?  113 TYR   B HB2  1 
ATOM   5733 H HB3  . TYR   B 1 113 ? 33.340 -22.117 -2.537  1.00 14.94 ?  113 TYR   B HB3  1 
ATOM   5734 H HD1  . TYR   B 1 113 ? 35.817 -22.581 -3.402  1.00 16.17 ?  113 TYR   B HD1  1 
ATOM   5735 H HD2  . TYR   B 1 113 ? 33.963 -24.772 -0.623  1.00 15.66 ?  113 TYR   B HD2  1 
ATOM   5736 H HE1  . TYR   B 1 113 ? 37.268 -24.315 -3.823  1.00 15.98 ?  113 TYR   B HE1  1 
ATOM   5737 H HE2  . TYR   B 1 113 ? 35.416 -26.523 -1.038  1.00 16.26 ?  113 TYR   B HE2  1 
ATOM   5738 H HH   . TYR   B 1 113 ? 37.181 -27.274 -2.258  1.00 17.21 ?  113 TYR   B HH   1 
ATOM   5739 N N    . GLU   B 1 114 ? 32.808 -19.249 -0.896  1.00 12.02 ?  114 GLU   B N    1 
ATOM   5740 C CA   . GLU   B 1 114 ? 32.133 -18.039 -1.356  1.00 12.18 ?  114 GLU   B CA   1 
ATOM   5741 C C    . GLU   B 1 114 ? 33.120 -16.918 -1.658  1.00 12.05 ?  114 GLU   B C    1 
ATOM   5742 O O    . GLU   B 1 114 ? 32.840 -16.058 -2.498  1.00 12.36 ?  114 GLU   B O    1 
ATOM   5743 C CB   . GLU   B 1 114 ? 31.076 -17.607 -0.339  1.00 12.87 ?  114 GLU   B CB   1 
ATOM   5744 C CG   . GLU   B 1 114 ? 29.859 -18.526 -0.413  1.00 13.22 ?  114 GLU   B CG   1 
ATOM   5745 C CD   . GLU   B 1 114 ? 28.833 -18.343 0.699   1.00 13.29 ?  114 GLU   B CD   1 
ATOM   5746 O OE1  . GLU   B 1 114 ? 29.120 -17.719 1.743   1.00 13.27 ?  114 GLU   B OE1  1 
ATOM   5747 O OE2  . GLU   B 1 114 ? 27.708 -18.876 0.534   1.00 14.06 -1 114 GLU   B OE2  1 
ATOM   5748 H H    . GLU   B 1 114 ? 32.547 -19.542 -0.128  1.00 14.42 ?  114 GLU   B H    1 
ATOM   5749 H HA   . GLU   B 1 114 ? 31.672 -18.240 -2.180  1.00 14.61 ?  114 GLU   B HA   1 
ATOM   5750 H HB2  . GLU   B 1 114 ? 31.445 -17.661 0.558   1.00 15.43 ?  114 GLU   B HB2  1 
ATOM   5751 H HB3  . GLU   B 1 114 ? 30.788 -16.703 -0.533  1.00 15.43 ?  114 GLU   B HB3  1 
ATOM   5752 H HG2  . GLU   B 1 114 ? 29.407 -18.368 -1.254  1.00 15.86 ?  114 GLU   B HG2  1 
ATOM   5753 H HG3  . GLU   B 1 114 ? 30.167 -19.446 -0.375  1.00 15.86 ?  114 GLU   B HG3  1 
ATOM   5754 N N    . ASN   B 1 115 ? 34.284 -16.910 -1.004  1.00 11.70 ?  115 ASN   B N    1 
ATOM   5755 C CA   . ASN   B 1 115 ? 35.277 -15.883 -1.303  1.00 11.68 ?  115 ASN   B CA   1 
ATOM   5756 C C    . ASN   B 1 115 ? 35.688 -15.906 -2.767  1.00 11.45 ?  115 ASN   B C    1 
ATOM   5757 O O    . ASN   B 1 115 ? 36.073 -14.868 -3.322  1.00 12.08 ?  115 ASN   B O    1 
ATOM   5758 C CB   . ASN   B 1 115 ? 36.514 -16.058 -0.420  1.00 12.38 ?  115 ASN   B CB   1 
ATOM   5759 C CG   . ASN   B 1 115 ? 36.238 -15.795 1.042   1.00 12.68 ?  115 ASN   B CG   1 
ATOM   5760 O OD1  . ASN   B 1 115 ? 36.239 -14.649 1.486   1.00 14.80 ?  115 ASN   B OD1  1 
ATOM   5761 N ND2  . ASN   B 1 115 ? 36.067 -16.858 1.813   1.00 12.74 ?  115 ASN   B ND2  1 
ATOM   5762 H H    . ASN   B 1 115 ? 34.517 -17.472 -0.388  1.00 14.04 ?  115 ASN   B H    1 
ATOM   5763 H HA   . ASN   B 1 115 ? 34.898 -15.012 -1.115  1.00 14.00 ?  115 ASN   B HA   1 
ATOM   5764 H HB2  . ASN   B 1 115 ? 36.842 -16.965 -0.509  1.00 14.85 ?  115 ASN   B HB2  1 
ATOM   5765 H HB3  . ASN   B 1 115 ? 37.198 -15.430 -0.710  1.00 14.85 ?  115 ASN   B HB3  1 
ATOM   5766 H HD21 . ASN   B 1 115 ? 35.921 -16.759 2.656   1.00 15.28 ?  115 ASN   B HD21 1 
ATOM   5767 H HD22 . ASN   B 1 115 ? 36.089 -17.649 1.473   1.00 15.28 ?  115 ASN   B HD22 1 
ATOM   5768 N N    . PHE   B 1 116 ? 35.665 -17.084 -3.399  1.00 11.43 ?  116 PHE   B N    1 
ATOM   5769 C CA   . PHE   B 1 116 ? 36.095 -17.174 -4.790  1.00 11.46 ?  116 PHE   B CA   1 
ATOM   5770 C C    . PHE   B 1 116 ? 35.198 -16.348 -5.701  1.00 11.32 ?  116 PHE   B C    1 
ATOM   5771 O O    . PHE   B 1 116 ? 35.631 -15.923 -6.776  1.00 11.84 ?  116 PHE   B O    1 
ATOM   5772 C CB   . PHE   B 1 116 ? 36.058 -18.619 -5.311  1.00 11.40 ?  116 PHE   B CB   1 
ATOM   5773 C CG   . PHE   B 1 116 ? 37.127 -19.577 -4.758  1.00 11.47 ?  116 PHE   B CG   1 
ATOM   5774 C CD1  . PHE   B 1 116 ? 37.770 -19.394 -3.545  1.00 12.02 ?  116 PHE   B CD1  1 
ATOM   5775 C CD2  . PHE   B 1 116 ? 37.435 -20.713 -5.491  1.00 11.63 ?  116 PHE   B CD2  1 
ATOM   5776 C CE1  . PHE   B 1 116 ? 38.706 -20.329 -3.087  1.00 12.39 ?  116 PHE   B CE1  1 
ATOM   5777 C CE2  . PHE   B 1 116 ? 38.363 -21.650 -5.040  1.00 12.06 ?  116 PHE   B CE2  1 
ATOM   5778 C CZ   . PHE   B 1 116 ? 38.987 -21.463 -3.840  1.00 12.12 ?  116 PHE   B CZ   1 
ATOM   5779 H H    . PHE   B 1 116 ? 35.403 -17.832 -3.054  1.00 13.71 ?  116 PHE   B H    1 
ATOM   5780 H HA   . PHE   B 1 116 ? 37.001 -16.848 -4.871  1.00 13.75 ?  116 PHE   B HA   1 
ATOM   5781 H HB2  . PHE   B 1 116 ? 35.186 -18.998 -5.094  1.00 13.68 ?  116 PHE   B HB2  1 
ATOM   5782 H HB3  . PHE   B 1 116 ? 36.158 -18.598 -6.277  1.00 13.68 ?  116 PHE   B HB3  1 
ATOM   5783 H HD1  . PHE   B 1 116 ? 37.569 -18.646 -3.029  1.00 14.42 ?  116 PHE   B HD1  1 
ATOM   5784 H HD2  . PHE   B 1 116 ? 37.002 -20.863 -6.302  1.00 13.95 ?  116 PHE   B HD2  1 
ATOM   5785 H HE1  . PHE   B 1 116 ? 39.133 -20.193 -2.274  1.00 14.86 ?  116 PHE   B HE1  1 
ATOM   5786 H HE2  . PHE   B 1 116 ? 38.557 -22.402 -5.553  1.00 14.46 ?  116 PHE   B HE2  1 
ATOM   5787 H HZ   . PHE   B 1 116 ? 39.623 -22.071 -3.541  1.00 14.54 ?  116 PHE   B HZ   1 
ATOM   5788 N N    . ASN   B 1 117 ? 33.930 -16.155 -5.322  1.00 11.68 ?  117 ASN   B N    1 
ATOM   5789 C CA   . ASN   B 1 117 ? 32.981 -15.451 -6.183  1.00 12.12 ?  117 ASN   B CA   1 
ATOM   5790 C C    . ASN   B 1 117 ? 33.293 -13.970 -6.331  1.00 12.84 ?  117 ASN   B C    1 
ATOM   5791 O O    . ASN   B 1 117 ? 32.697 -13.315 -7.189  1.00 13.60 ?  117 ASN   B O    1 
ATOM   5792 C CB   . ASN   B 1 117 ? 31.561 -15.669 -5.684  1.00 12.32 ?  117 ASN   B CB   1 
ATOM   5793 C CG   . ASN   B 1 117 ? 31.100 -17.078 -5.939  1.00 12.28 ?  117 ASN   B CG   1 
ATOM   5794 O OD1  . ASN   B 1 117 ? 31.455 -17.668 -6.960  1.00 13.54 ?  117 ASN   B OD1  1 
ATOM   5795 N ND2  . ASN   B 1 117 ? 30.364 -17.648 -5.000  1.00 12.79 ?  117 ASN   B ND2  1 
ATOM   5796 H H    . ASN   B 1 117 ? 33.602 -16.418 -4.569  1.00 14.01 ?  117 ASN   B H    1 
ATOM   5797 H HA   . ASN   B 1 117 ? 33.038 -15.846 -7.064  1.00 14.54 ?  117 ASN   B HA   1 
ATOM   5798 H HB2  . ASN   B 1 117 ? 31.528 -15.506 -4.725  1.00 14.78 ?  117 ASN   B HB2  1 
ATOM   5799 H HB3  . ASN   B 1 117 ? 30.964 -15.057 -6.144  1.00 14.78 ?  117 ASN   B HB3  1 
ATOM   5800 H HD21 . ASN   B 1 117 ? 30.078 -18.451 -5.105  1.00 15.34 ?  117 ASN   B HD21 1 
ATOM   5801 H HD22 . ASN   B 1 117 ? 30.146 -17.203 -4.295  1.00 15.34 ?  117 ASN   B HD22 1 
ATOM   5802 N N    . GLN   B 1 118 ? 34.233 -13.447 -5.554  1.00 12.33 ?  118 GLN   B N    1 
ATOM   5803 C CA   . GLN   B 1 118 ? 34.659 -12.060 -5.692  1.00 12.64 ?  118 GLN   B CA   1 
ATOM   5804 C C    . GLN   B 1 118 ? 35.725 -11.869 -6.766  1.00 12.85 ?  118 GLN   B C    1 
ATOM   5805 O O    . GLN   B 1 118 ? 36.194 -10.741 -6.956  1.00 14.38 ?  118 GLN   B O    1 
ATOM   5806 C CB   . GLN   B 1 118 ? 35.139 -11.526 -4.339  1.00 13.12 ?  118 GLN   B CB   1 
ATOM   5807 C CG   . GLN   B 1 118 ? 34.058 -11.569 -3.270  1.00 13.41 ?  118 GLN   B CG   1 
ATOM   5808 C CD   . GLN   B 1 118 ? 32.883 -10.662 -3.603  1.00 13.34 ?  118 GLN   B CD   1 
ATOM   5809 O OE1  . GLN   B 1 118 ? 33.073 -9.520  -4.028  1.00 14.24 ?  118 GLN   B OE1  1 
ATOM   5810 N NE2  . GLN   B 1 118 ? 31.665 -11.155 -3.407  1.00 13.57 ?  118 GLN   B NE2  1 
ATOM   5811 H H    . GLN   B 1 118 ? 34.655 -13.873 -4.933  1.00 14.79 ?  118 GLN   B H    1 
ATOM   5812 H HA   . GLN   B 1 118 ? 33.892 -11.529 -5.960  1.00 15.16 ?  118 GLN   B HA   1 
ATOM   5813 H HB2  . GLN   B 1 118 ? 35.888 -12.052 -4.032  1.00 15.74 ?  118 GLN   B HB2  1 
ATOM   5814 H HB3  . GLN   B 1 118 ? 35.413 -10.593 -4.444  1.00 15.74 ?  118 GLN   B HB3  1 
ATOM   5815 H HG2  . GLN   B 1 118 ? 33.729 -12.474 -3.188  1.00 16.09 ?  118 GLN   B HG2  1 
ATOM   5816 H HG3  . GLN   B 1 118 ? 34.436 -11.272 -2.424  1.00 16.09 ?  118 GLN   B HG3  1 
ATOM   5817 H HE21 . GLN   B 1 118 ? 31.570 -11.955 -3.104  1.00 16.27 ?  118 GLN   B HE21 1 
ATOM   5818 H HE22 . GLN   B 1 118 ? 30.977 -10.677 -3.586  1.00 16.27 ?  118 GLN   B HE22 1 
ATOM   5819 N N    . HIS   B 1 119 ? 36.085 -12.928 -7.491  1.00 12.37 ?  119 HIS   B N    1 
ATOM   5820 C CA   . HIS   B 1 119 ? 37.125 -12.880 -8.510  1.00 12.46 ?  119 HIS   B CA   1 
ATOM   5821 C C    . HIS   B 1 119 ? 36.645 -13.617 -9.746  1.00 12.39 ?  119 HIS   B C    1 
ATOM   5822 O O    . HIS   B 1 119 ? 36.140 -14.733 -9.640  1.00 13.16 ?  119 HIS   B O    1 
ATOM   5823 C CB   . HIS   B 1 119 ? 38.406 -13.509 -7.959  1.00 13.19 ?  119 HIS   B CB   1 
ATOM   5824 C CG   . HIS   B 1 119 ? 38.886 -12.810 -6.735  1.00 14.01 ?  119 HIS   B CG   1 
ATOM   5825 N ND1  . HIS   B 1 119 ? 39.689 -11.690 -6.791  1.00 15.61 ?  119 HIS   B ND1  1 
ATOM   5826 C CD2  . HIS   B 1 119 ? 38.599 -13.005 -5.427  1.00 15.11 ?  119 HIS   B CD2  1 
ATOM   5827 C CE1  . HIS   B 1 119 ? 39.904 -11.249 -5.565  1.00 16.73 ?  119 HIS   B CE1  1 
ATOM   5828 N NE2  . HIS   B 1 119 ? 39.247 -12.023 -4.720  1.00 16.71 ?  119 HIS   B NE2  1 
ATOM   5829 H H    . HIS   B 1 119 ? 35.723 -13.708 -7.413  1.00 14.84 ?  119 HIS   B H    1 
ATOM   5830 H HA   . HIS   B 1 119 ? 37.306 -11.954 -8.749  1.00 14.94 ?  119 HIS   B HA   1 
ATOM   5831 H HB2  . HIS   B 1 119 ? 38.234 -14.435 -7.734  1.00 15.82 ?  119 HIS   B HB2  1 
ATOM   5832 H HB3  . HIS   B 1 119 ? 39.102 -13.453 -8.635  1.00 15.82 ?  119 HIS   B HB3  1 
ATOM   5833 H HD2  . HIS   B 1 119 ? 38.070 -13.683 -5.074  1.00 18.12 ?  119 HIS   B HD2  1 
ATOM   5834 H HE1  . HIS   B 1 119 ? 40.436 -10.521 -5.331  1.00 20.06 ?  119 HIS   B HE1  1 
ATOM   5835 H HE2  . HIS   B 1 119 ? 39.256 -11.947 -3.862  1.00 20.04 ?  119 HIS   B HE2  1 
ATOM   5836 N N    . GLU   B 1 120 ? 36.799 -13.002 -10.917 1.00 12.81 ?  120 GLU   B N    1 
ATOM   5837 C CA   . GLU   B 1 120 ? 36.202 -13.588 -12.112 1.00 14.48 ?  120 GLU   B CA   1 
ATOM   5838 C C    . GLU   B 1 120 ? 36.884 -14.884 -12.530 1.00 13.37 ?  120 GLU   B C    1 
ATOM   5839 O O    . GLU   B 1 120 ? 36.228 -15.760 -13.102 1.00 13.92 ?  120 GLU   B O    1 
ATOM   5840 C CB   . GLU   B 1 120 ? 36.194 -12.581 -13.262 1.00 19.47 ?  120 GLU   B CB   1 
ATOM   5841 C CG   . GLU   B 1 120 ? 35.245 -11.419 -13.032 1.00 25.93 ?  120 GLU   B CG   1 
ATOM   5842 C CD   . GLU   B 1 120 ? 35.095 -10.527 -14.246 1.00 32.54 ?  120 GLU   B CD   1 
ATOM   5843 O OE1  . GLU   B 1 120 ? 36.090 -10.338 -14.977 1.00 35.03 ?  120 GLU   B OE1  1 
ATOM   5844 O OE2  . GLU   B 1 120 ? 33.977 -10.015 -14.465 1.00 35.19 -1 120 GLU   B OE2  1 
ATOM   5845 H H    . GLU   B 1 120 ? 37.223 -12.261 -11.045 1.00 15.37 ?  120 GLU   B H    1 
ATOM   5846 H HA   . GLU   B 1 120 ? 35.280 -13.806 -11.915 1.00 17.37 ?  120 GLU   B HA   1 
ATOM   5847 H HB2  . GLU   B 1 120 ? 37.083 -12.221 -13.373 1.00 23.36 ?  120 GLU   B HB2  1 
ATOM   5848 H HB3  . GLU   B 1 120 ? 35.914 -13.036 -14.074 1.00 23.36 ?  120 GLU   B HB3  1 
ATOM   5849 H HG2  . GLU   B 1 120 ? 34.364 -11.765 -12.812 1.00 31.11 ?  120 GLU   B HG2  1 
ATOM   5850 H HG3  . GLU   B 1 120 ? 35.579 -10.875 -12.304 1.00 31.11 ?  120 GLU   B HG3  1 
ATOM   5851 N N    . VAL   B 1 121 ? 38.184 -15.024 -12.267 1.00 12.82 ?  121 VAL   B N    1 
ATOM   5852 C CA   . VAL   B 1 121 ? 38.929 -16.233 -12.613 1.00 12.62 ?  121 VAL   B CA   1 
ATOM   5853 C C    . VAL   B 1 121 ? 40.039 -16.436 -11.593 1.00 12.26 ?  121 VAL   B C    1 
ATOM   5854 O O    . VAL   B 1 121 ? 40.709 -15.478 -11.193 1.00 13.13 ?  121 VAL   B O    1 
ATOM   5855 C CB   . VAL   B 1 121 ? 39.448 -16.199 -14.070 1.00 14.35 ?  121 VAL   B CB   1 
ATOM   5856 C CG1  . VAL   B 1 121 ? 40.315 -14.971 -14.328 1.00 16.03 ?  121 VAL   B CG1  1 
ATOM   5857 C CG2  . VAL   B 1 121 ? 40.190 -17.490 -14.412 1.00 15.84 ?  121 VAL   B CG2  1 
ATOM   5858 H H    . VAL   B 1 121 ? 38.670 -14.418 -11.890 1.00 15.38 ?  121 VAL   B H    1 
ATOM   5859 H HA   . VAL   B 1 121 ? 38.325 -16.984 -12.544 1.00 15.14 ?  121 VAL   B HA   1 
ATOM   5860 H HB   . VAL   B 1 121 ? 38.681 -16.144 -14.666 1.00 17.21 ?  121 VAL   B HB   1 
ATOM   5861 H HG11 . VAL   B 1 121 ? 40.624 -14.990 -15.248 1.00 19.23 ?  121 VAL   B HG11 1 
ATOM   5862 H HG12 . VAL   B 1 121 ? 39.786 -14.173 -14.174 1.00 19.23 ?  121 VAL   B HG12 1 
ATOM   5863 H HG13 . VAL   B 1 121 ? 41.074 -14.988 -13.725 1.00 19.23 ?  121 VAL   B HG13 1 
ATOM   5864 H HG21 . VAL   B 1 121 ? 40.389 -17.498 -15.363 1.00 19.00 ?  121 VAL   B HG21 1 
ATOM   5865 H HG22 . VAL   B 1 121 ? 41.017 -17.523 -13.905 1.00 19.00 ?  121 VAL   B HG22 1 
ATOM   5866 H HG23 . VAL   B 1 121 ? 39.631 -18.248 -14.186 1.00 19.00 ?  121 VAL   B HG23 1 
ATOM   5867 N N    . LEU   B 1 122 ? 40.224 -17.691 -11.165 1.00 11.83 ?  122 LEU   B N    1 
ATOM   5868 C CA   . LEU   B 1 122 ? 41.203 -18.037 -10.138 1.00 11.61 ?  122 LEU   B CA   1 
ATOM   5869 C C    . LEU   B 1 122 ? 41.860 -19.368 -10.460 1.00 11.46 ?  122 LEU   B C    1 
ATOM   5870 O O    . LEU   B 1 122 ? 41.199 -20.287 -10.963 1.00 12.60 ?  122 LEU   B O    1 
ATOM   5871 C CB   . LEU   B 1 122 ? 40.549 -18.268 -8.765  1.00 13.38 ?  122 LEU   B CB   1 
ATOM   5872 C CG   . LEU   B 1 122 ? 39.520 -17.242 -8.281  1.00 13.59 ?  122 LEU   B CG   1 
ATOM   5873 C CD1  . LEU   B 1 122 ? 38.121 -17.588 -8.766  1.00 14.26 ?  122 LEU   B CD1  1 
ATOM   5874 C CD2  . LEU   B 1 122 ? 39.558 -17.130 -6.769  1.00 12.91 ?  122 LEU   B CD2  1 
ATOM   5875 H H    . LEU   B 1 122 ? 39.788 -18.372 -11.462 1.00 14.18 ?  122 LEU   B H    1 
ATOM   5876 H HA   . LEU   B 1 122 ? 41.880 -17.346 -10.061 1.00 13.93 ?  122 LEU   B HA   1 
ATOM   5877 H HB2  . LEU   B 1 122 ? 40.099 -19.125 -8.788  1.00 16.04 ?  122 LEU   B HB2  1 
ATOM   5878 H HB3  . LEU   B 1 122 ? 41.252 -18.295 -8.098  1.00 16.04 ?  122 LEU   B HB3  1 
ATOM   5879 H HG   . LEU   B 1 122 ? 39.752 -16.373 -8.643  1.00 16.30 ?  122 LEU   B HG   1 
ATOM   5880 H HD11 . LEU   B 1 122 ? 37.493 -16.943 -8.397  1.00 17.11 ?  122 LEU   B HD11 1 
ATOM   5881 H HD12 . LEU   B 1 122 ? 38.103 -17.540 -9.736  1.00 17.11 ?  122 LEU   B HD12 1 
ATOM   5882 H HD13 . LEU   B 1 122 ? 37.893 -18.478 -8.471  1.00 17.11 ?  122 LEU   B HD13 1 
ATOM   5883 H HD21 . LEU   B 1 122 ? 38.883 -16.497 -6.477  1.00 15.48 ?  122 LEU   B HD21 1 
ATOM   5884 H HD22 . LEU   B 1 122 ? 39.387 -18.001 -6.379  1.00 15.48 ?  122 LEU   B HD22 1 
ATOM   5885 H HD23 . LEU   B 1 122 ? 40.439 -16.816 -6.496  1.00 15.48 ?  122 LEU   B HD23 1 
ATOM   5886 N N    . LEU   B 1 123 ? 43.147 -19.478 -10.110 1.00 11.05 ?  123 LEU   B N    1 
ATOM   5887 C CA   . LEU   B 1 123 ? 43.854 -20.749 -9.978  1.00 11.49 ?  123 LEU   B CA   1 
ATOM   5888 C C    . LEU   B 1 123 ? 43.824 -21.138 -8.504  1.00 11.18 ?  123 LEU   B C    1 
ATOM   5889 O O    . LEU   B 1 123 ? 44.178 -20.312 -7.650  1.00 11.79 ?  123 LEU   B O    1 
ATOM   5890 C CB   . LEU   B 1 123 ? 45.304 -20.565 -10.433 1.00 12.25 ?  123 LEU   B CB   1 
ATOM   5891 C CG   . LEU   B 1 123 ? 46.245 -21.750 -10.187 1.00 12.62 ?  123 LEU   B CG   1 
ATOM   5892 C CD1  . LEU   B 1 123 ? 45.812 -22.999 -10.960 1.00 12.85 ?  123 LEU   B CD1  1 
ATOM   5893 C CD2  . LEU   B 1 123 ? 47.665 -21.353 -10.559 1.00 13.11 ?  123 LEU   B CD2  1 
ATOM   5894 H H    . LEU   B 1 123 ? 43.648 -18.800 -9.923  1.00 13.25 ?  123 LEU   B H    1 
ATOM   5895 H HA   . LEU   B 1 123 ? 43.423 -21.439 -10.507 1.00 13.79 ?  123 LEU   B HA   1 
ATOM   5896 H HB2  . LEU   B 1 123 ? 45.300 -20.391 -11.387 1.00 14.69 ?  123 LEU   B HB2  1 
ATOM   5897 H HB3  . LEU   B 1 123 ? 45.674 -19.801 -9.967  1.00 14.69 ?  123 LEU   B HB3  1 
ATOM   5898 H HG   . LEU   B 1 123 ? 46.239 -21.972 -9.244  1.00 15.14 ?  123 LEU   B HG   1 
ATOM   5899 H HD11 . LEU   B 1 123 ? 46.448 -23.710 -10.792 1.00 15.42 ?  123 LEU   B HD11 1 
ATOM   5900 H HD12 . LEU   B 1 123 ? 44.929 -23.266 -10.659 1.00 15.42 ?  123 LEU   B HD12 1 
ATOM   5901 H HD13 . LEU   B 1 123 ? 45.789 -22.790 -11.907 1.00 15.42 ?  123 LEU   B HD13 1 
ATOM   5902 H HD21 . LEU   B 1 123 ? 48.254 -22.107 -10.404 1.00 15.73 ?  123 LEU   B HD21 1 
ATOM   5903 H HD22 . LEU   B 1 123 ? 47.686 -21.103 -11.497 1.00 15.73 ?  123 LEU   B HD22 1 
ATOM   5904 H HD23 . LEU   B 1 123 ? 47.935 -20.601 -10.010 1.00 15.73 ?  123 LEU   B HD23 1 
ATOM   5905 N N    . ALA   B 1 124 ? 43.393 -22.367 -8.192  1.00 11.13 ?  124 ALA   B N    1 
ATOM   5906 C CA   . ALA   B 1 124 ? 43.132 -22.676 -6.793  1.00 11.15 ?  124 ALA   B CA   1 
ATOM   5907 C C    . ALA   B 1 124 ? 43.406 -24.137 -6.468  1.00 11.05 ?  124 ALA   B C    1 
ATOM   5908 O O    . ALA   B 1 124 ? 43.263 -25.017 -7.329  1.00 11.83 ?  124 ALA   B O    1 
ATOM   5909 C CB   . ALA   B 1 124 ? 41.677 -22.365 -6.428  1.00 11.64 ?  124 ALA   B CB   1 
ATOM   5910 H H    . ALA   B 1 124 ? 43.231 -23.006 -8.754  1.00 13.35 ?  124 ALA   B H    1 
ATOM   5911 H HA   . ALA   B 1 124 ? 43.709 -22.130 -6.248  1.00 13.37 ?  124 ALA   B HA   1 
ATOM   5912 H HB1  . ALA   B 1 124 ? 41.526 -22.582 -5.495  1.00 13.96 ?  124 ALA   B HB1  1 
ATOM   5913 H HB2  . ALA   B 1 124 ? 41.511 -21.420 -6.579  1.00 13.96 ?  124 ALA   B HB2  1 
ATOM   5914 H HB3  . ALA   B 1 124 ? 41.085 -22.895 -6.989  1.00 13.96 ?  124 ALA   B HB3  1 
ATOM   5915 N N    . PRO   B 1 125 ? 43.697 -24.431 -5.205  1.00 11.34 ?  125 PRO   B N    1 
ATOM   5916 C CA   . PRO   B 1 125 ? 43.631 -25.797 -4.686  1.00 11.95 ?  125 PRO   B CA   1 
ATOM   5917 C C    . PRO   B 1 125 ? 42.229 -26.069 -4.144  1.00 12.06 ?  125 PRO   B C    1 
ATOM   5918 O O    . PRO   B 1 125 ? 41.440 -25.151 -3.928  1.00 12.74 ?  125 PRO   B O    1 
ATOM   5919 C CB   . PRO   B 1 125 ? 44.611 -25.726 -3.510  1.00 13.09 ?  125 PRO   B CB   1 
ATOM   5920 C CG   . PRO   B 1 125 ? 44.372 -24.341 -2.940  1.00 12.82 ?  125 PRO   B CG   1 
ATOM   5921 C CD   . PRO   B 1 125 ? 44.029 -23.466 -4.140  1.00 11.81 ?  125 PRO   B CD   1 
ATOM   5922 H HA   . PRO   B 1 125 ? 43.909 -26.465 -5.330  1.00 14.33 ?  125 PRO   B HA   1 
ATOM   5923 H HB2  . PRO   B 1 125 ? 44.398 -26.407 -2.849  1.00 15.70 ?  125 PRO   B HB2  1 
ATOM   5924 H HB3  . PRO   B 1 125 ? 45.523 -25.816 -3.820  1.00 15.70 ?  125 PRO   B HB3  1 
ATOM   5925 H HG2  . PRO   B 1 125 ? 43.628 -24.361 -2.312  1.00 15.38 ?  125 PRO   B HG2  1 
ATOM   5926 H HG3  . PRO   B 1 125 ? 45.176 -24.018 -2.496  1.00 15.38 ?  125 PRO   B HG3  1 
ATOM   5927 H HD2  . PRO   B 1 125 ? 43.268 -22.899 -3.947  1.00 14.16 ?  125 PRO   B HD2  1 
ATOM   5928 H HD3  . PRO   B 1 125 ? 44.805 -22.933 -4.399  1.00 14.16 ?  125 PRO   B HD3  1 
ATOM   5929 N N    . LEU   B 1 126 ? 41.957 -27.346 -3.869  1.00 12.77 ?  126 LEU   B N    1 
ATOM   5930 C CA   . LEU   B 1 126 ? 40.738 -27.708 -3.154  1.00 13.20 ?  126 LEU   B CA   1 
ATOM   5931 C C    . LEU   B 1 126 ? 40.854 -27.307 -1.692  1.00 13.23 ?  126 LEU   B C    1 
ATOM   5932 O O    . LEU   B 1 126 ? 41.746 -27.767 -0.975  1.00 15.15 ?  126 LEU   B O    1 
ATOM   5933 C CB   . LEU   B 1 126 ? 40.479 -29.204 -3.267  1.00 14.54 ?  126 LEU   B CB   1 
ATOM   5934 C CG   . LEU   B 1 126 ? 39.947 -29.696 -4.614  1.00 15.60 ?  126 LEU   B CG   1 
ATOM   5935 C CD1  . LEU   B 1 126 ? 39.997 -31.209 -4.679  1.00 17.34 ?  126 LEU   B CD1  1 
ATOM   5936 C CD2  . LEU   B 1 126 ? 38.535 -29.199 -4.871  1.00 15.87 ?  126 LEU   B CD2  1 
ATOM   5937 H H    . LEU   B 1 126 ? 42.460 -28.012 -4.077  1.00 15.32 ?  126 LEU   B H    1 
ATOM   5938 H HA   . LEU   B 1 126 ? 39.988 -27.234 -3.543  1.00 15.83 ?  126 LEU   B HA   1 
ATOM   5939 H HB2  . LEU   B 1 126 ? 41.309 -29.670 -3.095  1.00 17.44 ?  126 LEU   B HB2  1 
ATOM   5940 H HB3  . LEU   B 1 126 ? 39.823 -29.448 -2.595  1.00 17.44 ?  126 LEU   B HB3  1 
ATOM   5941 H HG   . LEU   B 1 126 ? 40.520 -29.352 -5.320  1.00 18.71 ?  126 LEU   B HG   1 
ATOM   5942 H HD11 . LEU   B 1 126 ? 39.655 -31.499 -5.538  1.00 20.80 ?  126 LEU   B HD11 1 
ATOM   5943 H HD12 . LEU   B 1 126 ? 40.913 -31.502 -4.567  1.00 20.80 ?  126 LEU   B HD12 1 
ATOM   5944 H HD13 . LEU   B 1 126 ? 39.445 -31.571 -3.965  1.00 20.80 ?  126 LEU   B HD13 1 
ATOM   5945 H HD21 . LEU   B 1 126 ? 38.197 -29.613 -5.680  1.00 19.03 ?  126 LEU   B HD21 1 
ATOM   5946 H HD22 . LEU   B 1 126 ? 37.974 -29.439 -4.117  1.00 19.03 ?  126 LEU   B HD22 1 
ATOM   5947 H HD23 . LEU   B 1 126 ? 38.552 -28.234 -4.976  1.00 19.03 ?  126 LEU   B HD23 1 
ATOM   5948 N N    . LEU   B 1 127 ? 39.927 -26.474 -1.237  1.00 13.43 ?  127 LEU   B N    1 
ATOM   5949 C CA   . LEU   B 1 127 ? 39.979 -25.986 0.127   1.00 13.60 ?  127 LEU   B CA   1 
ATOM   5950 C C    . LEU   B 1 127 ? 39.700 -27.107 1.120   1.00 13.66 ?  127 LEU   B C    1 
ATOM   5951 O O    . LEU   B 1 127 ? 38.884 -28.002 0.885   1.00 13.81 ?  127 LEU   B O    1 
ATOM   5952 C CB   . LEU   B 1 127 ? 38.958 -24.867 0.336   1.00 14.16 ?  127 LEU   B CB   1 
ATOM   5953 C CG   . LEU   B 1 127 ? 39.139 -23.606 -0.509  1.00 14.53 ?  127 LEU   B CG   1 
ATOM   5954 C CD1  . LEU   B 1 127 ? 38.025 -22.631 -0.176  1.00 14.77 ?  127 LEU   B CD1  1 
ATOM   5955 C CD2  . LEU   B 1 127 ? 40.505 -22.970 -0.276  1.00 15.12 ?  127 LEU   B CD2  1 
ATOM   5956 H H    . LEU   B 1 127 ? 39.260 -26.172 -1.698  1.00 16.11 ?  127 LEU   B H    1 
ATOM   5957 H HA   . LEU   B 1 127 ? 40.863 -25.626 0.306   1.00 16.32 ?  127 LEU   B HA   1 
ATOM   5958 H HB2  . LEU   B 1 127 ? 38.075 -25.220 0.140   1.00 16.99 ?  127 LEU   B HB2  1 
ATOM   5959 H HB3  . LEU   B 1 127 ? 38.991 -24.593 1.267   1.00 16.99 ?  127 LEU   B HB3  1 
ATOM   5960 H HG   . LEU   B 1 127 ? 39.058 -23.833 -1.448  1.00 17.43 ?  127 LEU   B HG   1 
ATOM   5961 H HD11 . LEU   B 1 127 ? 38.141 -21.821 -0.705  1.00 17.72 ?  127 LEU   B HD11 1 
ATOM   5962 H HD12 . LEU   B 1 127 ? 37.169 -23.034 -0.377  1.00 17.72 ?  127 LEU   B HD12 1 
ATOM   5963 H HD13 . LEU   B 1 127 ? 38.071 -22.406 0.770   1.00 17.72 ?  127 LEU   B HD13 1 
ATOM   5964 H HD21 . LEU   B 1 127 ? 40.543 -22.116 -0.736  1.00 18.14 ?  127 LEU   B HD21 1 
ATOM   5965 H HD22 . LEU   B 1 127 ? 40.636 -22.838 0.676   1.00 18.14 ?  127 LEU   B HD22 1 
ATOM   5966 H HD23 . LEU   B 1 127 ? 41.191 -23.562 -0.624  1.00 18.14 ?  127 LEU   B HD23 1 
ATOM   5967 N N    . SER   B 1 128 ? 40.383 -27.025 2.253   1.00 13.79 ?  128 SER   B N    1 
ATOM   5968 C CA   . SER   B 1 128 ? 40.269 -27.939 3.378   1.00 14.00 ?  128 SER   B CA   1 
ATOM   5969 C C    . SER   B 1 128 ? 40.760 -29.346 3.057   1.00 15.17 ?  128 SER   B C    1 
ATOM   5970 O O    . SER   B 1 128 ? 40.659 -30.224 3.908   1.00 16.56 ?  128 SER   B O    1 
ATOM   5971 C CB   . SER   B 1 128 ? 38.868 -27.948 4.006   1.00 14.23 ?  128 SER   B CB   1 
ATOM   5972 O OG   . SER   B 1 128 ? 38.554 -26.663 4.540   1.00 14.62 ?  128 SER   B OG   1 
ATOM   5973 H H    . SER   B 1 128 ? 40.957 -26.404 2.402   1.00 16.54 ?  128 SER   B H    1 
ATOM   5974 H HA   . SER   B 1 128 ? 40.854 -27.607 4.066   1.00 16.80 ?  128 SER   B HA   1 
ATOM   5975 H HB2  . SER   B 1 128 ? 38.207 -28.189 3.334   1.00 17.07 ?  128 SER   B HB2  1 
ATOM   5976 H HB3  . SER   B 1 128 ? 38.845 -28.607 4.731   1.00 17.07 ?  128 SER   B HB3  1 
ATOM   5977 H HG   . SER   B 1 128 ? 39.121 -26.454 5.121   1.00 17.53 ?  128 SER   B HG   1 
ATOM   5978 N N    . ALA   B 1 129 ? 41.336 -29.571 1.873   1.00 16.30 ?  129 ALA   B N    1 
ATOM   5979 C CA   . ALA   B 1 129 ? 41.886 -30.869 1.519   1.00 17.07 ?  129 ALA   B CA   1 
ATOM   5980 C C    . ALA   B 1 129 ? 43.275 -31.045 2.119   1.00 16.24 ?  129 ALA   B C    1 
ATOM   5981 O O    . ALA   B 1 129 ? 43.833 -30.147 2.763   1.00 16.13 ?  129 ALA   B O    1 
ATOM   5982 C CB   . ALA   B 1 129 ? 41.943 -31.027 0.001   1.00 19.14 ?  129 ALA   B CB   1 
ATOM   5983 H H    . ALA   B 1 129 ? 41.407 -28.982 1.246   1.00 19.56 ?  129 ALA   B H    1 
ATOM   5984 H HA   . ALA   B 1 129 ? 41.313 -31.564 1.870   1.00 20.48 ?  129 ALA   B HA   1 
ATOM   5985 H HB1  . ALA   B 1 129 ? 42.307 -31.904 -0.212  1.00 22.96 ?  129 ALA   B HB1  1 
ATOM   5986 H HB2  . ALA   B 1 129 ? 41.048 -30.946 -0.359  1.00 22.96 ?  129 ALA   B HB2  1 
ATOM   5987 H HB3  . ALA   B 1 129 ? 42.515 -30.336 -0.370  1.00 22.96 ?  129 ALA   B HB3  1 
ATOM   5988 N N    . GLY   B 1 130 ? 43.837 -32.228 1.893   1.00 16.27 ?  130 GLY   B N    1 
ATOM   5989 C CA   . GLY   B 1 130 ? 45.221 -32.466 2.252   1.00 16.87 ?  130 GLY   B CA   1 
ATOM   5990 C C    . GLY   B 1 130 ? 45.426 -32.363 3.743   1.00 17.03 ?  130 GLY   B C    1 
ATOM   5991 O O    . GLY   B 1 130 ? 44.727 -33.005 4.539   1.00 17.96 ?  130 GLY   B O    1 
ATOM   5992 H H    . GLY   B 1 130 ? 43.442 -32.897 1.530   1.00 19.52 ?  130 GLY   B H    1 
ATOM   5993 H HA2  . GLY   B 1 130 ? 45.482 -33.355 1.965   1.00 20.23 ?  130 GLY   B HA2  1 
ATOM   5994 H HA3  . GLY   B 1 130 ? 45.790 -31.817 1.814   1.00 20.23 ?  130 GLY   B HA3  1 
ATOM   5995 N N    . ILE   B 1 131 ? 46.407 -31.542 4.130   1.00 17.33 ?  131 ILE   B N    1 
ATOM   5996 C CA   . ILE   B 1 131 ? 46.768 -31.405 5.530   1.00 18.09 ?  131 ILE   B CA   1 
ATOM   5997 C C    . ILE   B 1 131 ? 45.650 -30.807 6.364   1.00 17.05 ?  131 ILE   B C    1 
ATOM   5998 O O    . ILE   B 1 131 ? 45.719 -30.867 7.592   1.00 18.91 ?  131 ILE   B O    1 
ATOM   5999 C CB   . ILE   B 1 131 ? 48.090 -30.618 5.713   1.00 20.20 ?  131 ILE   B CB   1 
ATOM   6000 C CG1  . ILE   B 1 131 ? 47.913 -29.136 5.353   1.00 21.94 ?  131 ILE   B CG1  1 
ATOM   6001 C CG2  . ILE   B 1 131 ? 49.206 -31.245 4.882   1.00 21.34 ?  131 ILE   B CG2  1 
ATOM   6002 C CD1  . ILE   B 1 131 ? 49.143 -28.283 5.639   1.00 23.24 ?  131 ILE   B CD1  1 
ATOM   6003 H H    . ILE   B 1 131 ? 46.878 -31.058 3.598   1.00 20.79 ?  131 ILE   B H    1 
ATOM   6004 H HA   . ILE   B 1 131 ? 46.923 -32.291 5.884   1.00 21.70 ?  131 ILE   B HA   1 
ATOM   6005 H HB   . ILE   B 1 131 ? 48.341 -30.670 6.648   1.00 24.23 ?  131 ILE   B HB   1 
ATOM   6006 H HG12 . ILE   B 1 131 ? 47.713 -29.067 4.407   1.00 26.32 ?  131 ILE   B HG12 1 
ATOM   6007 H HG13 . ILE   B 1 131 ? 47.177 -28.766 5.869   1.00 26.32 ?  131 ILE   B HG13 1 
ATOM   6008 H HG21 . ILE   B 1 131 ? 50.049 -30.846 5.142   1.00 25.60 ?  131 ILE   B HG21 1 
ATOM   6009 H HG22 . ILE   B 1 131 ? 49.219 -32.197 5.047   1.00 25.60 ?  131 ILE   B HG22 1 
ATOM   6010 H HG23 . ILE   B 1 131 ? 49.029 -31.071 3.944   1.00 25.60 ?  131 ILE   B HG23 1 
ATOM   6011 H HD11 . ILE   B 1 131 ? 48.919 -27.351 5.493   1.00 27.88 ?  131 ILE   B HD11 1 
ATOM   6012 H HD12 . ILE   B 1 131 ? 49.412 -28.420 6.561   1.00 27.88 ?  131 ILE   B HD12 1 
ATOM   6013 H HD13 . ILE   B 1 131 ? 49.857 -28.551 5.041   1.00 27.88 ?  131 ILE   B HD13 1 
ATOM   6014 N N    . PHE   B 1 132 ? 44.624 -30.227 5.731   1.00 15.73 ?  132 PHE   B N    1 
ATOM   6015 C CA   . PHE   B 1 132 ? 43.461 -29.723 6.454   1.00 16.29 ?  132 PHE   B CA   1 
ATOM   6016 C C    . PHE   B 1 132 ? 42.438 -30.814 6.773   1.00 17.46 ?  132 PHE   B C    1 
ATOM   6017 O O    . PHE   B 1 132 ? 41.524 -30.563 7.564   1.00 19.08 ?  132 PHE   B O    1 
ATOM   6018 C CB   . PHE   B 1 132 ? 42.786 -28.594 5.666   1.00 15.70 ?  132 PHE   B CB   1 
ATOM   6019 C CG   . PHE   B 1 132 ? 43.481 -27.249 5.777   1.00 15.54 ?  132 PHE   B CG   1 
ATOM   6020 C CD1  . PHE   B 1 132 ? 44.778 -27.069 5.320   1.00 16.45 ?  132 PHE   B CD1  1 
ATOM   6021 C CD2  . PHE   B 1 132 ? 42.806 -26.152 6.296   1.00 15.21 ?  132 PHE   B CD2  1 
ATOM   6022 C CE1  . PHE   B 1 132 ? 45.396 -25.828 5.414   1.00 17.16 ?  132 PHE   B CE1  1 
ATOM   6023 C CE2  . PHE   B 1 132 ? 43.413 -24.909 6.385   1.00 15.71 ?  132 PHE   B CE2  1 
ATOM   6024 C CZ   . PHE   B 1 132 ? 44.706 -24.750 5.945   1.00 16.71 ?  132 PHE   B CZ   1 
ATOM   6025 H H    . PHE   B 1 132 ? 44.581 -30.112 4.879   1.00 18.88 ?  132 PHE   B H    1 
ATOM   6026 H HA   . PHE   B 1 132 ? 43.760 -29.350 7.295   1.00 19.54 ?  132 PHE   B HA   1 
ATOM   6027 H HB2  . PHE   B 1 132 ? 42.773 -28.835 4.729   1.00 18.83 ?  132 PHE   B HB2  1 
ATOM   6028 H HB3  . PHE   B 1 132 ? 41.878 -28.483 5.992   1.00 18.83 ?  132 PHE   B HB3  1 
ATOM   6029 H HD1  . PHE   B 1 132 ? 45.248 -27.792 4.967   1.00 19.73 ?  132 PHE   B HD1  1 
ATOM   6030 H HD2  . PHE   B 1 132 ? 41.932 -26.256 6.595   1.00 18.24 ?  132 PHE   B HD2  1 
ATOM   6031 H HE1  . PHE   B 1 132 ? 46.271 -25.717 5.118   1.00 20.58 ?  132 PHE   B HE1  1 
ATOM   6032 H HE2  . PHE   B 1 132 ? 42.949 -24.185 6.746   1.00 18.85 ?  132 PHE   B HE2  1 
ATOM   6033 H HZ   . PHE   B 1 132 ? 45.116 -23.915 6.010   1.00 20.05 ?  132 PHE   B HZ   1 
ATOM   6034 N N    . GLY   B 1 133 ? 42.549 -32.004 6.170   1.00 17.36 ?  133 GLY   B N    1 
ATOM   6035 C CA   . GLY   B 1 133 ? 41.839 -33.175 6.653   1.00 18.37 ?  133 GLY   B CA   1 
ATOM   6036 C C    . GLY   B 1 133 ? 40.436 -33.424 6.128   1.00 18.84 ?  133 GLY   B C    1 
ATOM   6037 O O    . GLY   B 1 133 ? 39.844 -34.440 6.498   1.00 20.75 ?  133 GLY   B O    1 
ATOM   6038 H H    . GLY   B 1 133 ? 43.042 -32.150 5.479   1.00 20.82 ?  133 GLY   B H    1 
ATOM   6039 H HA2  . GLY   B 1 133 ? 42.373 -33.956 6.447   1.00 22.04 ?  133 GLY   B HA2  1 
ATOM   6040 H HA3  . GLY   B 1 133 ? 41.773 -33.110 7.618   1.00 22.04 ?  133 GLY   B HA3  1 
ATOM   6041 N N    . ALA   B 1 134 ? 39.875 -32.555 5.297   1.00 17.75 ?  134 ALA   B N    1 
ATOM   6042 C CA   . ALA   B 1 134 ? 38.549 -32.837 4.769   1.00 17.57 ?  134 ALA   B CA   1 
ATOM   6043 C C    . ALA   B 1 134 ? 38.630 -33.839 3.621   1.00 17.60 ?  134 ALA   B C    1 
ATOM   6044 O O    . ALA   B 1 134 ? 39.683 -34.043 3.009   1.00 18.61 ?  134 ALA   B O    1 
ATOM   6045 C CB   . ALA   B 1 134 ? 37.877 -31.556 4.282   1.00 18.07 ?  134 ALA   B CB   1 
ATOM   6046 H H    . ALA   B 1 134 ? 40.227 -31.812 5.036   1.00 21.29 ?  134 ALA   B H    1 
ATOM   6047 H HA   . ALA   B 1 134 ? 38.000 -33.219 5.472   1.00 21.08 ?  134 ALA   B HA   1 
ATOM   6048 H HB1  . ALA   B 1 134 ? 36.989 -31.771 3.954   1.00 21.68 ?  134 ALA   B HB1  1 
ATOM   6049 H HB2  . ALA   B 1 134 ? 37.814 -30.931 5.021   1.00 21.68 ?  134 ALA   B HB2  1 
ATOM   6050 H HB3  . ALA   B 1 134 ? 38.408 -31.172 3.567   1.00 21.68 ?  134 ALA   B HB3  1 
ATOM   6051 N N    . ASP   B 1 135 ? 37.491 -34.457 3.332   1.00 17.73 ?  135 ASP   B N    1 
ATOM   6052 C CA   . ASP   B 1 135 ? 37.387 -35.350 2.190   1.00 18.55 ?  135 ASP   B CA   1 
ATOM   6053 C C    . ASP   B 1 135 ? 37.493 -34.513 0.922   1.00 17.39 ?  135 ASP   B C    1 
ATOM   6054 O O    . ASP   B 1 135 ? 36.643 -33.639 0.697   1.00 17.22 ?  135 ASP   B O    1 
ATOM   6055 C CB   . ASP   B 1 135 ? 36.044 -36.076 2.243   1.00 20.72 ?  135 ASP   B CB   1 
ATOM   6056 C CG   . ASP   B 1 135 ? 35.868 -37.078 1.119   1.00 22.64 ?  135 ASP   B CG   1 
ATOM   6057 O OD1  . ASP   B 1 135 ? 36.723 -37.129 0.209   1.00 22.13 ?  135 ASP   B OD1  1 
ATOM   6058 O OD2  . ASP   B 1 135 ? 34.872 -37.835 1.159   1.00 25.38 -1 135 ASP   B OD2  1 
ATOM   6059 H H    . ASP   B 1 135 ? 36.763 -34.375 3.784   1.00 21.27 ?  135 ASP   B H    1 
ATOM   6060 H HA   . ASP   B 1 135 ? 38.100 -36.008 2.221   1.00 22.25 ?  135 ASP   B HA   1 
ATOM   6061 H HB2  . ASP   B 1 135 ? 35.980 -36.555 3.083   1.00 24.85 ?  135 ASP   B HB2  1 
ATOM   6062 H HB3  . ASP   B 1 135 ? 35.333 -35.424 2.174   1.00 24.85 ?  135 ASP   B HB3  1 
ATOM   6063 N N    . PRO   B 1 136 ? 38.505 -34.724 0.079   1.00 17.49 ?  136 PRO   B N    1 
ATOM   6064 C CA   . PRO   B 1 136 ? 38.608 -33.905 -1.140  1.00 16.66 ?  136 PRO   B CA   1 
ATOM   6065 C C    . PRO   B 1 136 ? 37.416 -34.056 -2.068  1.00 15.93 ?  136 PRO   B C    1 
ATOM   6066 O O    . PRO   B 1 136 ? 37.095 -33.112 -2.798  1.00 15.16 ?  136 PRO   B O    1 
ATOM   6067 C CB   . PRO   B 1 136 ? 39.921 -34.384 -1.779  1.00 17.48 ?  136 PRO   B CB   1 
ATOM   6068 C CG   . PRO   B 1 136 ? 40.119 -35.773 -1.231  1.00 18.73 ?  136 PRO   B CG   1 
ATOM   6069 C CD   . PRO   B 1 136 ? 39.580 -35.728 0.167   1.00 18.39 ?  136 PRO   B CD   1 
ATOM   6070 H HA   . PRO   B 1 136 ? 38.700 -32.970 -0.907  1.00 19.98 ?  136 PRO   B HA   1 
ATOM   6071 H HB2  . PRO   B 1 136 ? 39.832 -34.407 -2.747  1.00 20.97 ?  136 PRO   B HB2  1 
ATOM   6072 H HB3  . PRO   B 1 136 ? 40.649 -33.800 -1.516  1.00 20.97 ?  136 PRO   B HB3  1 
ATOM   6073 H HG2  . PRO   B 1 136 ? 39.626 -36.416 -1.764  1.00 22.47 ?  136 PRO   B HG2  1 
ATOM   6074 H HG3  . PRO   B 1 136 ? 41.066 -35.994 -1.221  1.00 22.47 ?  136 PRO   B HG3  1 
ATOM   6075 H HD2  . PRO   B 1 136 ? 39.217 -36.591 0.422   1.00 22.06 ?  136 PRO   B HD2  1 
ATOM   6076 H HD3  . PRO   B 1 136 ? 40.264 -35.431 0.792   1.00 22.06 ?  136 PRO   B HD3  1 
ATOM   6077 N N    . ILE   B 1 137 ? 36.761 -35.223 -2.072  1.00 16.48 ?  137 ILE   B N    1 
ATOM   6078 C CA   . ILE   B 1 137 ? 35.547 -35.392 -2.866  1.00 17.38 ?  137 ILE   B CA   1 
ATOM   6079 C C    . ILE   B 1 137 ? 34.472 -34.421 -2.395  1.00 16.74 ?  137 ILE   B C    1 
ATOM   6080 O O    . ILE   B 1 137 ? 33.760 -33.808 -3.203  1.00 16.30 ?  137 ILE   B O    1 
ATOM   6081 C CB   . ILE   B 1 137 ? 35.072 -36.860 -2.804  1.00 19.60 ?  137 ILE   B CB   1 
ATOM   6082 C CG1  . ILE   B 1 137 ? 36.077 -37.769 -3.519  1.00 22.20 ?  137 ILE   B CG1  1 
ATOM   6083 C CG2  . ILE   B 1 137 ? 33.673 -36.998 -3.397  1.00 19.99 ?  137 ILE   B CG2  1 
ATOM   6084 C CD1  . ILE   B 1 137 ? 35.789 -39.249 -3.371  1.00 24.56 ?  137 ILE   B CD1  1 
ATOM   6085 H H    . ILE   B 1 137 ? 36.997 -35.925 -1.633  1.00 19.77 ?  137 ILE   B H    1 
ATOM   6086 H HA   . ILE   B 1 137 ? 35.746 -35.189 -3.795  1.00 20.85 ?  137 ILE   B HA   1 
ATOM   6087 H HB   . ILE   B 1 137 ? 35.031 -37.124 -1.876  1.00 23.51 ?  137 ILE   B HB   1 
ATOM   6088 H HG12 . ILE   B 1 137 ? 36.070 -37.564 -4.466  1.00 26.63 ?  137 ILE   B HG12 1 
ATOM   6089 H HG13 . ILE   B 1 137 ? 36.960 -37.606 -3.154  1.00 26.63 ?  137 ILE   B HG13 1 
ATOM   6090 H HG21 . ILE   B 1 137 ? 33.465 -37.940 -3.515  1.00 23.98 ?  137 ILE   B HG21 1 
ATOM   6091 H HG22 . ILE   B 1 137 ? 33.027 -36.602 -2.792  1.00 23.98 ?  137 ILE   B HG22 1 
ATOM   6092 H HG23 . ILE   B 1 137 ? 33.644 -36.549 -4.256  1.00 23.98 ?  137 ILE   B HG23 1 
ATOM   6093 H HD11 . ILE   B 1 137 ? 36.544 -39.748 -3.718  1.00 29.46 ?  137 ILE   B HD11 1 
ATOM   6094 H HD12 . ILE   B 1 137 ? 35.660 -39.456 -2.432  1.00 29.46 ?  137 ILE   B HD12 1 
ATOM   6095 H HD13 . ILE   B 1 137 ? 34.990 -39.473 -3.873  1.00 29.46 ?  137 ILE   B HD13 1 
ATOM   6096 N N    . HIS   B 1 138 ? 34.341 -34.268 -1.080  1.00 16.79 ?  138 HIS   B N    1 
ATOM   6097 C CA   . HIS   B 1 138 ? 33.390 -33.304 -0.546  1.00 16.76 ?  138 HIS   B CA   1 
ATOM   6098 C C    . HIS   B 1 138 ? 33.810 -31.877 -0.866  1.00 16.03 ?  138 HIS   B C    1 
ATOM   6099 O O    . HIS   B 1 138 ? 32.966 -31.032 -1.178  1.00 16.50 ?  138 HIS   B O    1 
ATOM   6100 C CB   . HIS   B 1 138 ? 33.271 -33.478 0.960   1.00 17.90 ?  138 HIS   B CB   1 
ATOM   6101 C CG   . HIS   B 1 138 ? 32.341 -32.496 1.593   1.00 19.03 ?  138 HIS   B CG   1 
ATOM   6102 N ND1  . HIS   B 1 138 ? 31.002 -32.425 1.269   1.00 20.45 ?  138 HIS   B ND1  1 
ATOM   6103 C CD2  . HIS   B 1 138 ? 32.559 -31.518 2.503   1.00 19.63 ?  138 HIS   B CD2  1 
ATOM   6104 C CE1  . HIS   B 1 138 ? 30.434 -31.455 1.963   1.00 20.35 ?  138 HIS   B CE1  1 
ATOM   6105 N NE2  . HIS   B 1 138 ? 31.357 -30.892 2.723   1.00 19.86 ?  138 HIS   B NE2  1 
ATOM   6106 H H    . HIS   B 1 138 ? 34.783 -34.705 -0.489  1.00 20.14 ?  138 HIS   B H    1 
ATOM   6107 H HA   . HIS   B 1 138 ? 32.517 -33.463 -0.941  1.00 20.11 ?  138 HIS   B HA   1 
ATOM   6108 H HB2  . HIS   B 1 138 ? 32.933 -34.366 1.149   1.00 21.47 ?  138 HIS   B HB2  1 
ATOM   6109 H HB3  . HIS   B 1 138 ? 34.143 -33.360 1.361   1.00 21.47 ?  138 HIS   B HB3  1 
ATOM   6110 H HD1  . HIS   B 1 138 ? 30.598 -32.935 0.704   1.00 24.53 ?  138 HIS   B HD1  1 
ATOM   6111 H HD2  . HIS   B 1 138 ? 33.363 -31.311 2.915   1.00 23.55 ?  138 HIS   B HD2  1 
ATOM   6112 H HE1  . HIS   B 1 138 ? 29.530 -31.219 1.929   1.00 24.41 ?  138 HIS   B HE1  1 
ATOM   6113 N N    . SER   B 1 139 ? 35.104 -31.578 -0.780  1.00 15.41 ?  139 SER   B N    1 
ATOM   6114 C CA   . SER   B 1 139 ? 35.551 -30.229 -1.104  1.00 14.79 ?  139 SER   B CA   1 
ATOM   6115 C C    . SER   B 1 139 ? 35.221 -29.878 -2.546  1.00 13.94 ?  139 SER   B C    1 
ATOM   6116 O O    . SER   B 1 139 ? 34.772 -28.762 -2.831  1.00 14.10 ?  139 SER   B O    1 
ATOM   6117 C CB   . SER   B 1 139 ? 37.046 -30.103 -0.842  1.00 15.18 ?  139 SER   B CB   1 
ATOM   6118 O OG   . SER   B 1 139 ? 37.465 -28.769 -1.074  1.00 15.16 ?  139 SER   B OG   1 
ATOM   6119 H H    . SER   B 1 139 ? 35.720 -32.123 -0.552  1.00 18.49 ?  139 SER   B H    1 
ATOM   6120 H HA   . SER   B 1 139 ? 35.088 -29.598 -0.536  1.00 17.74 ?  139 SER   B HA   1 
ATOM   6121 H HB2  . SER   B 1 139 ? 37.228 -30.343 0.080   1.00 18.21 ?  139 SER   B HB2  1 
ATOM   6122 H HB3  . SER   B 1 139 ? 37.529 -30.695 -1.441  1.00 18.21 ?  139 SER   B HB3  1 
ATOM   6123 H HG   . SER   B 1 139 ? 38.294 -28.700 -0.920  1.00 18.19 ?  139 SER   B HG   1 
ATOM   6124 N N    . LEU   B 1 140 ? 35.400 -30.829 -3.467  1.00 13.58 ?  140 LEU   B N    1 
ATOM   6125 C CA   . LEU   B 1 140 ? 35.046 -30.581 -4.859  1.00 13.86 ?  140 LEU   B CA   1 
ATOM   6126 C C    . LEU   B 1 140 ? 33.545 -30.348 -5.001  1.00 14.22 ?  140 LEU   B C    1 
ATOM   6127 O O    . LEU   B 1 140 ? 33.115 -29.457 -5.740  1.00 14.41 ?  140 LEU   B O    1 
ATOM   6128 C CB   . LEU   B 1 140 ? 35.518 -31.742 -5.737  1.00 13.75 ?  140 LEU   B CB   1 
ATOM   6129 C CG   . LEU   B 1 140 ? 35.164 -31.642 -7.213  1.00 14.12 ?  140 LEU   B CG   1 
ATOM   6130 C CD1  . LEU   B 1 140 ? 35.735 -30.361 -7.810  1.00 15.12 ?  140 LEU   B CD1  1 
ATOM   6131 C CD2  . LEU   B 1 140 ? 35.661 -32.864 -7.949  1.00 15.47 ?  140 LEU   B CD2  1 
ATOM   6132 H H    . LEU   B 1 140 ? 35.714 -31.615 -3.315  1.00 16.29 ?  140 LEU   B H    1 
ATOM   6133 H HA   . LEU   B 1 140 ? 35.504 -29.780 -5.160  1.00 16.62 ?  140 LEU   B HA   1 
ATOM   6134 H HB2  . LEU   B 1 140 ? 36.486 -31.800 -5.680  1.00 16.50 ?  140 LEU   B HB2  1 
ATOM   6135 H HB3  . LEU   B 1 140 ? 35.125 -32.562 -5.406  1.00 16.50 ?  140 LEU   B HB3  1 
ATOM   6136 H HG   . LEU   B 1 140 ? 34.200 -31.604 -7.305  1.00 16.94 ?  140 LEU   B HG   1 
ATOM   6137 H HD11 . LEU   B 1 140 ? 35.620 -30.386 -8.772  1.00 18.14 ?  140 LEU   B HD11 1 
ATOM   6138 H HD12 . LEU   B 1 140 ? 35.260 -29.599 -7.440  1.00 18.14 ?  140 LEU   B HD12 1 
ATOM   6139 H HD13 . LEU   B 1 140 ? 36.677 -30.304 -7.590  1.00 18.14 ?  140 LEU   B HD13 1 
ATOM   6140 H HD21 . LEU   B 1 140 ? 35.422 -32.780 -8.886  1.00 18.55 ?  140 LEU   B HD21 1 
ATOM   6141 H HD22 . LEU   B 1 140 ? 36.619 -32.921 -7.851  1.00 18.55 ?  140 LEU   B HD22 1 
ATOM   6142 H HD23 . LEU   B 1 140 ? 35.234 -33.646 -7.568  1.00 18.55 ?  140 LEU   B HD23 1 
ATOM   6143 N N    . ARG   B 1 141 ? 32.737 -31.136 -4.289  1.00 14.56 ?  141 ARG   B N    1 
ATOM   6144 C CA   . ARG   B 1 141 ? 31.290 -30.956 -4.276  1.00 15.49 ?  141 ARG   B CA   1 
ATOM   6145 C C    . ARG   B 1 141 ? 30.912 -29.549 -3.845  1.00 15.14 ?  141 ARG   B C    1 
ATOM   6146 O O    . ARG   B 1 141 ? 30.113 -28.872 -4.505  1.00 15.19 ?  141 ARG   B O    1 
ATOM   6147 C CB   . ARG   B 1 141 ? 30.698 -31.988 -3.307  1.00 16.65 ?  141 ARG   B CB   1 
ATOM   6148 C CG   . ARG   B 1 141 ? 29.231 -31.872 -2.988  1.00 18.82 ?  141 ARG   B CG   1 
ATOM   6149 C CD   . ARG   B 1 141 ? 28.436 -32.510 -4.055  1.00 20.86 ?  141 ARG   B CD   1 
ATOM   6150 N NE   . ARG   B 1 141 ? 28.178 -31.599 -5.158  1.00 21.43 ?  141 ARG   B NE   1 
ATOM   6151 C CZ   . ARG   B 1 141 ? 28.168 -31.950 -6.436  1.00 21.12 ?  141 ARG   B CZ   1 
ATOM   6152 N NH1  . ARG   B 1 141 ? 28.589 -33.141 -6.830  1.00 20.88 ?  141 ARG   B NH1  1 
ATOM   6153 N NH2  . ARG   B 1 141 ? 27.722 -31.085 -7.341  1.00 22.04 ?  141 ARG   B NH2  1 
ATOM   6154 H H    . ARG   B 1 141 ? 33.013 -31.787 -3.805  1.00 17.47 ?  141 ARG   B H    1 
ATOM   6155 H HA   . ARG   B 1 141 ? 30.930 -31.114 -5.160  1.00 18.58 ?  141 ARG   B HA   1 
ATOM   6156 H HB2  . ARG   B 1 141 ? 30.851 -32.873 -3.682  1.00 19.97 ?  141 ARG   B HB2  1 
ATOM   6157 H HB3  . ARG   B 1 141 ? 31.176 -31.921 -2.468  1.00 19.97 ?  141 ARG   B HB3  1 
ATOM   6158 H HG2  . ARG   B 1 141 ? 29.051 -32.323 -2.150  1.00 22.57 ?  141 ARG   B HG2  1 
ATOM   6159 H HG3  . ARG   B 1 141 ? 28.975 -30.935 -2.926  1.00 22.57 ?  141 ARG   B HG3  1 
ATOM   6160 H HD2  . ARG   B 1 141 ? 28.915 -33.288 -4.390  1.00 25.02 ?  141 ARG   B HD2  1 
ATOM   6161 H HD3  . ARG   B 1 141 ? 27.590 -32.789 -3.683  1.00 25.02 ?  141 ARG   B HD3  1 
ATOM   6162 H HE   . ARG   B 1 141 ? 28.006 -30.779 -4.965  1.00 25.70 ?  141 ARG   B HE   1 
ATOM   6163 H HH11 . ARG   B 1 141 ? 28.866 -33.720 -6.258  1.00 25.05 ?  141 ARG   B HH11 1 
ATOM   6164 H HH12 . ARG   B 1 141 ? 28.576 -33.344 -7.664  1.00 25.05 ?  141 ARG   B HH12 1 
ATOM   6165 H HH21 . ARG   B 1 141 ? 27.453 -30.304 -7.096  1.00 26.45 ?  141 ARG   B HH21 1 
ATOM   6166 H HH22 . ARG   B 1 141 ? 27.727 -31.292 -8.176  1.00 26.45 ?  141 ARG   B HH22 1 
ATOM   6167 N N    . VAL   B 1 142 ? 31.454 -29.105 -2.713  1.00 14.94 ?  142 VAL   B N    1 
ATOM   6168 C CA   . VAL   B 1 142 ? 31.119 -27.773 -2.229  1.00 14.50 ?  142 VAL   B CA   1 
ATOM   6169 C C    . VAL   B 1 142 ? 31.598 -26.715 -3.216  1.00 14.40 ?  142 VAL   B C    1 
ATOM   6170 O O    . VAL   B 1 142 ? 30.899 -25.730 -3.481  1.00 14.83 ?  142 VAL   B O    1 
ATOM   6171 C CB   . VAL   B 1 142 ? 31.661 -27.548 -0.804  1.00 15.03 ?  142 VAL   B CB   1 
ATOM   6172 C CG1  . VAL   B 1 142 ? 31.349 -26.128 -0.334  1.00 14.94 ?  142 VAL   B CG1  1 
ATOM   6173 C CG2  . VAL   B 1 142 ? 31.068 -28.567 0.157   1.00 15.90 ?  142 VAL   B CG2  1 
ATOM   6174 H H    . VAL   B 1 142 ? 32.006 -29.546 -2.219  1.00 17.92 ?  142 VAL   B H    1 
ATOM   6175 H HA   . VAL   B 1 142 ? 30.159 -27.703 -2.179  1.00 17.40 ?  142 VAL   B HA   1 
ATOM   6176 H HB   . VAL   B 1 142 ? 32.623 -27.662 -0.803  1.00 18.02 ?  142 VAL   B HB   1 
ATOM   6177 H HG11 . VAL   B 1 142 ? 31.521 -26.067 0.617   1.00 17.92 ?  142 VAL   B HG11 1 
ATOM   6178 H HG12 . VAL   B 1 142 ? 31.917 -25.505 -0.814  1.00 17.92 ?  142 VAL   B HG12 1 
ATOM   6179 H HG13 . VAL   B 1 142 ? 30.416 -25.935 -0.516  1.00 17.92 ?  142 VAL   B HG13 1 
ATOM   6180 H HG21 . VAL   B 1 142 ? 31.387 -28.383 1.053   1.00 19.07 ?  142 VAL   B HG21 1 
ATOM   6181 H HG22 . VAL   B 1 142 ? 30.098 -28.497 0.132   1.00 19.07 ?  142 VAL   B HG22 1 
ATOM   6182 H HG23 . VAL   B 1 142 ? 31.339 -29.457 -0.116  1.00 19.07 ?  142 VAL   B HG23 1 
ATOM   6183 N N    . CYS   B 1 143 ? 32.783 -26.912 -3.792  1.00 13.79 ?  143 CYS   B N    1 
ATOM   6184 C CA   . CYS   B 1 143 ? 33.279 -25.978 -4.798  1.00 13.84 ?  143 CYS   B CA   1 
ATOM   6185 C C    . CYS   B 1 143 ? 32.281 -25.833 -5.941  1.00 13.67 ?  143 CYS   B C    1 
ATOM   6186 O O    . CYS   B 1 143 ? 31.885 -24.719 -6.304  1.00 13.79 ?  143 CYS   B O    1 
ATOM   6187 C CB   . CYS   B 1 143 ? 34.638 -26.460 -5.316  1.00 14.16 ?  143 CYS   B CB   1 
ATOM   6188 S SG   . CYS   B 1 143 ? 35.391 -25.366 -6.547  1.00 14.72 ?  143 CYS   B SG   1 
ATOM   6189 H H    . CYS   B 1 143 ? 33.312 -27.565 -3.621  1.00 16.54 ?  143 CYS   B H    1 
ATOM   6190 H HA   . CYS   B 1 143 ? 33.403 -25.105 -4.396  1.00 16.60 ?  143 CYS   B HA   1 
ATOM   6191 H HB2  . CYS   B 1 143 ? 35.257 -26.531 -4.570  1.00 16.99 ?  143 CYS   B HB2  1 
ATOM   6192 H HB3  . CYS   B 1 143 ? 34.528 -27.328 -5.725  1.00 16.99 ?  143 CYS   B HB3  1 
ATOM   6193 H HG   . CYS   B 1 143 ? 36.467 -25.800 -6.856  1.00 17.66 ?  143 CYS   B HG   1 
ATOM   6194 N N    . VAL   B 1 144 ? 31.879 -26.955 -6.534  1.00 14.15 ?  144 VAL   B N    1 
ATOM   6195 C CA   . VAL   B 1 144 ? 30.977 -26.894 -7.678  1.00 15.36 ?  144 VAL   B CA   1 
ATOM   6196 C C    . VAL   B 1 144 ? 29.633 -26.283 -7.306  1.00 15.48 ?  144 VAL   B C    1 
ATOM   6197 O O    . VAL   B 1 144 ? 29.018 -25.585 -8.121  1.00 16.66 ?  144 VAL   B O    1 
ATOM   6198 C CB   . VAL   B 1 144 ? 30.826 -28.303 -8.269  1.00 17.85 ?  144 VAL   B CB   1 
ATOM   6199 C CG1  . VAL   B 1 144 ? 29.554 -28.420 -9.109  1.00 20.54 ?  144 VAL   B CG1  1 
ATOM   6200 C CG2  . VAL   B 1 144 ? 32.079 -28.694 -9.057  1.00 17.87 ?  144 VAL   B CG2  1 
ATOM   6201 H H    . VAL   B 1 144 ? 32.115 -27.752 -6.303  1.00 16.97 ?  144 VAL   B H    1 
ATOM   6202 H HA   . VAL   B 1 144 ? 31.370 -26.335 -8.362  1.00 18.42 ?  144 VAL   B HA   1 
ATOM   6203 H HB   . VAL   B 1 144 ? 30.742 -28.937 -7.540  1.00 21.42 ?  144 VAL   B HB   1 
ATOM   6204 H HG11 . VAL   B 1 144 ? 29.631 -29.200 -9.686  1.00 24.64 ?  144 VAL   B HG11 1 
ATOM   6205 H HG12 . VAL   B 1 144 ? 28.794 -28.529 -8.517  1.00 24.64 ?  144 VAL   B HG12 1 
ATOM   6206 H HG13 . VAL   B 1 144 ? 29.454 -27.624 -9.647  1.00 24.64 ?  144 VAL   B HG13 1 
ATOM   6207 H HG21 . VAL   B 1 144 ? 31.964 -29.588 -9.419  1.00 21.44 ?  144 VAL   B HG21 1 
ATOM   6208 H HG22 . VAL   B 1 144 ? 32.205 -28.060 -9.783  1.00 21.44 ?  144 VAL   B HG22 1 
ATOM   6209 H HG23 . VAL   B 1 144 ? 32.844 -28.673 -8.464  1.00 21.44 ?  144 VAL   B HG23 1 
ATOM   6210 N N    . ASP   B 1 145 ? 29.164 -26.518 -6.084  1.00 15.74 ?  145 ASP   B N    1 
ATOM   6211 C CA   . ASP   B 1 145 ? 27.853 -26.046 -5.662  1.00 16.47 ?  145 ASP   B CA   1 
ATOM   6212 C C    . ASP   B 1 145 ? 27.884 -24.625 -5.116  1.00 15.83 ?  145 ASP   B C    1 
ATOM   6213 O O    . ASP   B 1 145 ? 26.822 -24.087 -4.785  1.00 17.70 ?  145 ASP   B O    1 
ATOM   6214 C CB   . ASP   B 1 145 ? 27.259 -26.964 -4.582  1.00 18.03 ?  145 ASP   B CB   1 
ATOM   6215 C CG   . ASP   B 1 145 ? 26.905 -28.347 -5.091  1.00 19.49 ?  145 ASP   B CG   1 
ATOM   6216 O OD1  . ASP   B 1 145 ? 26.814 -28.546 -6.319  1.00 20.00 ?  145 ASP   B OD1  1 
ATOM   6217 O OD2  . ASP   B 1 145 ? 26.704 -29.231 -4.236  1.00 21.49 -1 145 ASP   B OD2  1 
ATOM   6218 H H    . ASP   B 1 145 ? 29.598 -26.940 -5.474  1.00 18.88 ?  145 ASP   B H    1 
ATOM   6219 H HA   . ASP   B 1 145 ? 27.263 -26.037 -6.428  1.00 19.75 ?  145 ASP   B HA   1 
ATOM   6220 H HB2  . ASP   B 1 145 ? 27.898 -27.068 -3.872  1.00 21.64 ?  145 ASP   B HB2  1 
ATOM   6221 H HB3  . ASP   B 1 145 ? 26.444 -26.549 -4.244  1.00 21.64 ?  145 ASP   B HB3  1 
ATOM   6222 N N    . THR   B 1 146 ? 29.064 -24.017 -4.994  1.00 14.23 ?  146 THR   B N    1 
ATOM   6223 C CA   . THR   B 1 146 ? 29.200 -22.696 -4.388  1.00 13.82 ?  146 THR   B CA   1 
ATOM   6224 C C    . THR   B 1 146 ? 29.833 -21.669 -5.312  1.00 13.56 ?  146 THR   B C    1 
ATOM   6225 O O    . THR   B 1 146 ? 29.380 -20.510 -5.367  1.00 14.01 ?  146 THR   B O    1 
ATOM   6226 C CB   . THR   B 1 146 ? 30.025 -22.803 -3.100  1.00 13.86 ?  146 THR   B CB   1 
ATOM   6227 O OG1  . THR   B 1 146 ? 29.448 -23.791 -2.241  1.00 14.35 ?  146 THR   B OG1  1 
ATOM   6228 C CG2  . THR   B 1 146 ? 30.100 -21.463 -2.386  1.00 14.36 ?  146 THR   B CG2  1 
ATOM   6229 H H    . THR   B 1 146 ? 29.814 -24.350 -5.259  1.00 17.07 ?  146 THR   B H    1 
ATOM   6230 H HA   . THR   B 1 146 ? 28.326 -22.366 -4.144  1.00 16.57 ?  146 THR   B HA   1 
ATOM   6231 H HB   . THR   B 1 146 ? 30.933 -23.065 -3.321  1.00 16.63 ?  146 THR   B HB   1 
ATOM   6232 H HG1  . THR   B 1 146 ? 29.478 -24.548 -2.614  1.00 17.21 ?  146 THR   B HG1  1 
ATOM   6233 H HG21 . THR   B 1 146 ? 30.440 -21.584 -1.486  1.00 17.23 ?  146 THR   B HG21 1 
ATOM   6234 H HG22 . THR   B 1 146 ? 30.697 -20.863 -2.866  1.00 17.23 ?  146 THR   B HG22 1 
ATOM   6235 H HG23 . THR   B 1 146 ? 29.220 -21.062 -2.340  1.00 17.23 ?  146 THR   B HG23 1 
ATOM   6236 N N    . VAL   B 1 147 ? 30.900 -22.043 -6.008  1.00 13.56 ?  147 VAL   B N    1 
ATOM   6237 C CA   . VAL   B 1 147 ? 31.623 -21.103 -6.854  1.00 13.36 ?  147 VAL   B CA   1 
ATOM   6238 C C    . VAL   B 1 147 ? 30.890 -20.967 -8.177  1.00 13.23 ?  147 VAL   B C    1 
ATOM   6239 O O    . VAL   B 1 147 ? 30.520 -21.969 -8.803  1.00 14.01 ?  147 VAL   B O    1 
ATOM   6240 C CB   . VAL   B 1 147 ? 33.077 -21.558 -7.058  1.00 13.26 ?  147 VAL   B CB   1 
ATOM   6241 C CG1  . VAL   B 1 147 ? 33.832 -20.529 -7.871  1.00 13.26 ?  147 VAL   B CG1  1 
ATOM   6242 C CG2  . VAL   B 1 147 ? 33.755 -21.772 -5.716  1.00 13.51 ?  147 VAL   B CG2  1 
ATOM   6243 H H    . VAL   B 1 147 ? 31.227 -22.841 -6.013  1.00 16.26 ?  147 VAL   B H    1 
ATOM   6244 H HA   . VAL   B 1 147 ? 31.640 -20.233 -6.427  1.00 16.03 ?  147 VAL   B HA   1 
ATOM   6245 H HB   . VAL   B 1 147 ? 33.087 -22.402 -7.545  1.00 15.91 ?  147 VAL   B HB   1 
ATOM   6246 H HG11 . VAL   B 1 147 ? 34.777 -20.748 -7.858  1.00 15.90 ?  147 VAL   B HG11 1 
ATOM   6247 H HG12 . VAL   B 1 147 ? 33.504 -20.539 -8.784  1.00 15.90 ?  147 VAL   B HG12 1 
ATOM   6248 H HG13 . VAL   B 1 147 ? 33.691 -19.654 -7.477  1.00 15.90 ?  147 VAL   B HG13 1 
ATOM   6249 H HG21 . VAL   B 1 147 ? 34.695 -21.962 -5.865  1.00 16.21 ?  147 VAL   B HG21 1 
ATOM   6250 H HG22 . VAL   B 1 147 ? 33.662 -20.964 -5.188  1.00 16.21 ?  147 VAL   B HG22 1 
ATOM   6251 H HG23 . VAL   B 1 147 ? 33.335 -22.516 -5.261  1.00 16.21 ?  147 VAL   B HG23 1 
ATOM   6252 N N    . ARG   B 1 148 ? 30.682 -19.721 -8.597  1.00 13.20 ?  148 ARG   B N    1 
ATOM   6253 C CA   . ARG   B 1 148 ? 30.059 -19.403 -9.873  1.00 13.53 ?  148 ARG   B CA   1 
ATOM   6254 C C    . ARG   B 1 148 ? 31.016 -18.734 -10.846 1.00 13.50 ?  148 ARG   B C    1 
ATOM   6255 O O    . ARG   B 1 148 ? 30.739 -18.723 -12.048 1.00 15.36 ?  148 ARG   B O    1 
ATOM   6256 C CB   . ARG   B 1 148 ? 28.826 -18.511 -9.659  1.00 13.82 ?  148 ARG   B CB   1 
ATOM   6257 C CG   . ARG   B 1 148 ? 27.744 -19.219 -8.852  1.00 14.68 ?  148 ARG   B CG   1 
ATOM   6258 C CD   . ARG   B 1 148 ? 26.545 -18.325 -8.542  1.00 15.40 ?  148 ARG   B CD   1 
ATOM   6259 N NE   . ARG   B 1 148 ? 26.934 -17.127 -7.807  1.00 15.16 ?  148 ARG   B NE   1 
ATOM   6260 C CZ   . ARG   B 1 148 ? 27.232 -17.099 -6.514  1.00 14.41 ?  148 ARG   B CZ   1 
ATOM   6261 N NH1  . ARG   B 1 148 ? 27.157 -18.185 -5.759  1.00 14.86 ?  148 ARG   B NH1  1 
ATOM   6262 N NH2  . ARG   B 1 148 ? 27.635 -15.954 -5.967  1.00 14.33 ?  148 ARG   B NH2  1 
ATOM   6263 H H    . ARG   B 1 148 ? 30.901 -19.018 -8.144  1.00 15.83 ?  148 ARG   B H    1 
ATOM   6264 H HA   . ARG   B 1 148 ? 29.754 -20.224 -10.282 1.00 16.23 ?  148 ARG   B HA   1 
ATOM   6265 H HB2  . ARG   B 1 148 ? 29.087 -17.711 -9.176  1.00 16.58 ?  148 ARG   B HB2  1 
ATOM   6266 H HB3  . ARG   B 1 148 ? 28.450 -18.271 -10.522 1.00 16.58 ?  148 ARG   B HB3  1 
ATOM   6267 H HG2  . ARG   B 1 148 ? 27.423 -19.982 -9.360  1.00 17.61 ?  148 ARG   B HG2  1 
ATOM   6268 H HG3  . ARG   B 1 148 ? 28.121 -19.516 -8.011  1.00 17.61 ?  148 ARG   B HG3  1 
ATOM   6269 H HD2  . ARG   B 1 148 ? 26.131 -18.045 -9.373  1.00 18.48 ?  148 ARG   B HD2  1 
ATOM   6270 H HD3  . ARG   B 1 148 ? 25.908 -18.820 -8.002  1.00 18.48 ?  148 ARG   B HD3  1 
ATOM   6271 H HE   . ARG   B 1 148 ? 26.988 -16.389 -8.240  1.00 18.19 ?  148 ARG   B HE   1 
ATOM   6272 H HH11 . ARG   B 1 148 ? 26.895 -18.933 -6.097  1.00 17.83 ?  148 ARG   B HH11 1 
ATOM   6273 H HH12 . ARG   B 1 148 ? 27.349 -18.144 -4.919  1.00 17.83 ?  148 ARG   B HH12 1 
ATOM   6274 H HH21 . ARG   B 1 148 ? 27.696 -15.246 -6.447  1.00 17.19 ?  148 ARG   B HH21 1 
ATOM   6275 H HH22 . ARG   B 1 148 ? 27.832 -15.922 -5.129  1.00 17.19 ?  148 ARG   B HH22 1 
ATOM   6276 N N    . THR   B 1 149 ? 32.119 -18.179 -10.357 1.00 13.32 ?  149 THR   B N    1 
ATOM   6277 C CA   . THR   B 1 149 ? 33.160 -17.622 -11.205 1.00 13.62 ?  149 THR   B CA   1 
ATOM   6278 C C    . THR   B 1 149 ? 34.046 -18.763 -11.709 1.00 13.12 ?  149 THR   B C    1 
ATOM   6279 O O    . THR   B 1 149 ? 33.854 -19.930 -11.365 1.00 13.48 ?  149 THR   B O    1 
ATOM   6280 C CB   . THR   B 1 149 ? 33.929 -16.566 -10.423 1.00 13.55 ?  149 THR   B CB   1 
ATOM   6281 O OG1  . THR   B 1 149 ? 34.395 -17.166 -9.212  1.00 13.57 ?  149 THR   B OG1  1 
ATOM   6282 C CG2  . THR   B 1 149 ? 33.027 -15.368 -10.114 1.00 14.27 ?  149 THR   B CG2  1 
ATOM   6283 H H    . THR   B 1 149 ? 32.277 -18.102 -9.516  1.00 15.98 ?  149 THR   B H    1 
ATOM   6284 H HA   . THR   B 1 149 ? 32.751 -17.193 -11.971 1.00 16.34 ?  149 THR   B HA   1 
ATOM   6285 H HB   . THR   B 1 149 ? 34.681 -16.263 -10.944 1.00 16.26 ?  149 THR   B HB   1 
ATOM   6286 H HG1  . THR   B 1 149 ? 34.817 -16.597 -8.752  1.00 16.28 ?  149 THR   B HG1  1 
ATOM   6287 H HG21 . THR   B 1 149 ? 33.529 -14.690 -9.634  1.00 17.12 ?  149 THR   B HG21 1 
ATOM   6288 H HG22 . THR   B 1 149 ? 32.690 -14.983 -10.939 1.00 17.12 ?  149 THR   B HG22 1 
ATOM   6289 H HG23 . THR   B 1 149 ? 32.273 -15.645 -9.567  1.00 17.12 ?  149 THR   B HG23 1 
ATOM   6290 N N    . ASN   B 1 150 ? 35.015 -18.444 -12.554 1.00 13.31 ?  150 ASN   B N    1 
ATOM   6291 C CA   . ASN   B 1 150 ? 35.781 -19.470 -13.251 1.00 13.84 ?  150 ASN   B CA   1 
ATOM   6292 C C    . ASN   B 1 150 ? 36.942 -19.920 -12.375 1.00 13.55 ?  150 ASN   B C    1 
ATOM   6293 O O    . ASN   B 1 150 ? 37.878 -19.152 -12.129 1.00 13.77 ?  150 ASN   B O    1 
ATOM   6294 C CB   . ASN   B 1 150 ? 36.251 -18.936 -14.597 1.00 15.70 ?  150 ASN   B CB   1 
ATOM   6295 C CG   . ASN   B 1 150 ? 35.105 -18.734 -15.548 1.00 18.26 ?  150 ASN   B CG   1 
ATOM   6296 O OD1  . ASN   B 1 150 ? 34.214 -19.571 -15.627 1.00 19.19 ?  150 ASN   B OD1  1 
ATOM   6297 N ND2  . ASN   B 1 150 ? 35.092 -17.610 -16.245 1.00 19.63 ?  150 ASN   B ND2  1 
ATOM   6298 H H    . ASN   B 1 150 ? 35.257 -17.638 -12.737 1.00 15.97 ?  150 ASN   B H    1 
ATOM   6299 H HA   . ASN   B 1 150 ? 35.207 -20.238 -13.414 1.00 16.60 ?  150 ASN   B HA   1 
ATOM   6300 H HB2  . ASN   B 1 150 ? 36.688 -18.079 -14.462 1.00 18.84 ?  150 ASN   B HB2  1 
ATOM   6301 H HB3  . ASN   B 1 150 ? 36.865 -19.568 -14.995 1.00 18.84 ?  150 ASN   B HB3  1 
ATOM   6302 H HD21 . ASN   B 1 150 ? 34.453 -17.450 -16.800 1.00 23.55 ?  150 ASN   B HD21 1 
ATOM   6303 H HD22 . ASN   B 1 150 ? 35.732 -17.040 -16.157 1.00 23.55 ?  150 ASN   B HD22 1 
ATOM   6304 N N    . VAL   B 1 151 ? 36.893 -21.164 -11.911 1.00 12.95 ?  151 VAL   B N    1 
ATOM   6305 C CA   . VAL   B 1 151 ? 37.911 -21.698 -11.019 1.00 13.07 ?  151 VAL   B CA   1 
ATOM   6306 C C    . VAL   B 1 151 ? 38.617 -22.866 -11.695 1.00 12.56 ?  151 VAL   B C    1 
ATOM   6307 O O    . VAL   B 1 151 ? 37.976 -23.799 -12.199 1.00 13.87 ?  151 VAL   B O    1 
ATOM   6308 C CB   . VAL   B 1 151 ? 37.353 -22.038 -9.621  1.00 14.35 ?  151 VAL   B CB   1 
ATOM   6309 C CG1  . VAL   B 1 151 ? 36.187 -23.033 -9.697  1.00 15.41 ?  151 VAL   B CG1  1 
ATOM   6310 C CG2  . VAL   B 1 151 ? 38.465 -22.529 -8.696  1.00 14.82 ?  151 VAL   B CG2  1 
ATOM   6311 H H    . VAL   B 1 151 ? 36.267 -21.727 -12.103 1.00 15.54 ?  151 VAL   B H    1 
ATOM   6312 H HA   . VAL   B 1 151 ? 38.579 -21.008 -10.884 1.00 15.68 ?  151 VAL   B HA   1 
ATOM   6313 H HB   . VAL   B 1 151 ? 37.001 -21.221 -9.230  1.00 17.21 ?  151 VAL   B HB   1 
ATOM   6314 H HG11 . VAL   B 1 151 ? 35.870 -23.223 -8.799  1.00 18.48 ?  151 VAL   B HG11 1 
ATOM   6315 H HG12 . VAL   B 1 151 ? 35.470 -22.645 -10.223 1.00 18.48 ?  151 VAL   B HG12 1 
ATOM   6316 H HG13 . VAL   B 1 151 ? 36.496 -23.854 -10.116 1.00 18.48 ?  151 VAL   B HG13 1 
ATOM   6317 H HG21 . VAL   B 1 151 ? 38.109 -22.619 -7.795  1.00 17.78 ?  151 VAL   B HG21 1 
ATOM   6318 H HG22 . VAL   B 1 151 ? 38.786 -23.387 -9.009  1.00 17.78 ?  151 VAL   B HG22 1 
ATOM   6319 H HG23 . VAL   B 1 151 ? 39.188 -21.881 -8.698  1.00 17.78 ?  151 VAL   B HG23 1 
ATOM   6320 N N    . TYR   B 1 152 ? 39.944 -22.778 -11.726 1.00 12.14 ?  152 TYR   B N    1 
ATOM   6321 C CA   . TYR   B 1 152 ? 40.845 -23.764 -12.305 1.00 12.20 ?  152 TYR   B CA   1 
ATOM   6322 C C    . TYR   B 1 152 ? 41.565 -24.434 -11.142 1.00 11.92 ?  152 TYR   B C    1 
ATOM   6323 O O    . TYR   B 1 152 ? 42.414 -23.815 -10.492 1.00 12.57 ?  152 TYR   B O    1 
ATOM   6324 C CB   . TYR   B 1 152 ? 41.819 -23.057 -13.249 1.00 12.97 ?  152 TYR   B CB   1 
ATOM   6325 C CG   . TYR   B 1 152 ? 41.145 -22.591 -14.515 1.00 13.57 ?  152 TYR   B CG   1 
ATOM   6326 C CD1  . TYR   B 1 152 ? 40.472 -21.372 -14.576 1.00 14.14 ?  152 TYR   B CD1  1 
ATOM   6327 C CD2  . TYR   B 1 152 ? 41.148 -23.395 -15.643 1.00 14.86 ?  152 TYR   B CD2  1 
ATOM   6328 C CE1  . TYR   B 1 152 ? 39.830 -20.971 -15.735 1.00 15.47 ?  152 TYR   B CE1  1 
ATOM   6329 C CE2  . TYR   B 1 152 ? 40.514 -23.005 -16.803 1.00 15.98 ?  152 TYR   B CE2  1 
ATOM   6330 C CZ   . TYR   B 1 152 ? 39.860 -21.791 -16.847 1.00 16.28 ?  152 TYR   B CZ   1 
ATOM   6331 O OH   . TYR   B 1 152 ? 39.231 -21.415 -18.008 1.00 18.95 ?  152 TYR   B OH   1 
ATOM   6332 H H    . TYR   B 1 152 ? 40.375 -22.111 -11.385 1.00 14.56 ?  152 TYR   B H    1 
ATOM   6333 H HA   . TYR   B 1 152 ? 40.340 -24.431 -12.801 1.00 14.64 ?  152 TYR   B HA   1 
ATOM   6334 H HB2  . TYR   B 1 152 ? 42.184 -22.279 -12.799 1.00 15.55 ?  152 TYR   B HB2  1 
ATOM   6335 H HB3  . TYR   B 1 152 ? 42.531 -23.667 -13.491 1.00 15.55 ?  152 TYR   B HB3  1 
ATOM   6336 H HD1  . TYR   B 1 152 ? 40.448 -20.825 -13.826 1.00 16.97 ?  152 TYR   B HD1  1 
ATOM   6337 H HD2  . TYR   B 1 152 ? 41.588 -24.216 -15.619 1.00 17.83 ?  152 TYR   B HD2  1 
ATOM   6338 H HE1  . TYR   B 1 152 ? 39.387 -20.154 -15.770 1.00 18.55 ?  152 TYR   B HE1  1 
ATOM   6339 H HE2  . TYR   B 1 152 ? 40.536 -23.554 -17.555 1.00 19.17 ?  152 TYR   B HE2  1 
ATOM   6340 H HH   . TYR   B 1 152 ? 38.870 -20.659 -17.906 1.00 22.74 ?  152 TYR   B HH   1 
ATOM   6341 N N    . LEU   B 1 153 ? 41.204 -25.690 -10.868 1.00 12.11 ?  153 LEU   B N    1 
ATOM   6342 C CA   . LEU   B 1 153 ? 41.711 -26.430 -9.722  1.00 12.10 ?  153 LEU   B CA   1 
ATOM   6343 C C    . LEU   B 1 153 ? 42.944 -27.230 -10.116 1.00 12.26 ?  153 LEU   B C    1 
ATOM   6344 O O    . LEU   B 1 153 ? 42.929 -27.965 -11.108 1.00 13.27 ?  153 LEU   B O    1 
ATOM   6345 C CB   . LEU   B 1 153 ? 40.633 -27.386 -9.203  1.00 12.49 ?  153 LEU   B CB   1 
ATOM   6346 C CG   . LEU   B 1 153 ? 39.372 -26.734 -8.637  1.00 13.41 ?  153 LEU   B CG   1 
ATOM   6347 C CD1  . LEU   B 1 153 ? 38.280 -27.776 -8.482  1.00 14.23 ?  153 LEU   B CD1  1 
ATOM   6348 C CD2  . LEU   B 1 153 ? 39.663 -26.059 -7.300  1.00 13.68 ?  153 LEU   B CD2  1 
ATOM   6349 H H    . LEU   B 1 153 ? 40.638 -26.145 -11.344 1.00 14.52 ?  153 LEU   B H    1 
ATOM   6350 H HA   . LEU   B 1 153 ? 41.937 -25.809 -9.016  1.00 14.51 ?  153 LEU   B HA   1 
ATOM   6351 H HB2  . LEU   B 1 153 ? 40.353 -27.963 -9.927  1.00 14.98 ?  153 LEU   B HB2  1 
ATOM   6352 H HB3  . LEU   B 1 153 ? 41.016 -27.922 -8.489  1.00 14.98 ?  153 LEU   B HB3  1 
ATOM   6353 H HG   . LEU   B 1 153 ? 39.053 -26.050 -9.254  1.00 16.09 ?  153 LEU   B HG   1 
ATOM   6354 H HD11 . LEU   B 1 153 ? 37.473 -27.340 -8.158  1.00 17.06 ?  153 LEU   B HD11 1 
ATOM   6355 H HD12 . LEU   B 1 153 ? 38.113 -28.182 -9.342  1.00 17.06 ?  153 LEU   B HD12 1 
ATOM   6356 H HD13 . LEU   B 1 153 ? 38.575 -28.440 -7.844  1.00 17.06 ?  153 LEU   B HD13 1 
ATOM   6357 H HD21 . LEU   B 1 153 ? 38.842 -25.681 -6.945  1.00 16.40 ?  153 LEU   B HD21 1 
ATOM   6358 H HD22 . LEU   B 1 153 ? 40.012 -26.723 -6.684  1.00 16.40 ?  153 LEU   B HD22 1 
ATOM   6359 H HD23 . LEU   B 1 153 ? 40.318 -25.357 -7.435  1.00 16.40 ?  153 LEU   B HD23 1 
ATOM   6360 N N    . ALA   B 1 154 ? 43.991 -27.115 -9.311  1.00 12.68 ?  154 ALA   B N    1 
ATOM   6361 C CA   . ALA   B 1 154 ? 45.218 -27.880 -9.494  1.00 13.75 ?  154 ALA   B CA   1 
ATOM   6362 C C    . ALA   B 1 154 ? 45.280 -28.960 -8.422  1.00 13.98 ?  154 ALA   B C    1 
ATOM   6363 O O    . ALA   B 1 154 ? 45.212 -28.660 -7.222  1.00 15.45 ?  154 ALA   B O    1 
ATOM   6364 C CB   . ALA   B 1 154 ? 46.446 -26.974 -9.429  1.00 14.89 ?  154 ALA   B CB   1 
ATOM   6365 H H    . ALA   B 1 154 ? 44.011 -26.584 -8.629  1.00 15.22 ?  154 ALA   B H    1 
ATOM   6366 H HA   . ALA   B 1 154 ? 45.201 -28.309 -10.360 1.00 16.49 ?  154 ALA   B HA   1 
ATOM   6367 H HB1  . ALA   B 1 154 ? 47.243 -27.512 -9.554  1.00 17.86 ?  154 ALA   B HB1  1 
ATOM   6368 H HB2  . ALA   B 1 154 ? 46.385 -26.307 -10.132 1.00 17.86 ?  154 ALA   B HB2  1 
ATOM   6369 H HB3  . ALA   B 1 154 ? 46.475 -26.537 -8.563  1.00 17.86 ?  154 ALA   B HB3  1 
ATOM   6370 N N    . VAL   B 1 155 ? 45.399 -30.208 -8.855  1.00 13.40 ?  155 VAL   B N    1 
ATOM   6371 C CA   . VAL   B 1 155 ? 45.504 -31.355 -7.962  1.00 14.03 ?  155 VAL   B CA   1 
ATOM   6372 C C    . VAL   B 1 155 ? 46.843 -32.028 -8.234  1.00 13.42 ?  155 VAL   B C    1 
ATOM   6373 O O    . VAL   B 1 155 ? 47.081 -32.522 -9.342  1.00 15.21 ?  155 VAL   B O    1 
ATOM   6374 C CB   . VAL   B 1 155 ? 44.344 -32.346 -8.161  1.00 15.42 ?  155 VAL   B CB   1 
ATOM   6375 C CG1  . VAL   B 1 155 ? 44.526 -33.546 -7.250  1.00 15.14 ?  155 VAL   B CG1  1 
ATOM   6376 C CG2  . VAL   B 1 155 ? 43.006 -31.656 -7.903  1.00 16.15 ?  155 VAL   B CG2  1 
ATOM   6377 H H    . VAL   B 1 155 ? 45.431 -30.423 -9.690  1.00 16.08 ?  155 VAL   B H    1 
ATOM   6378 H HA   . VAL   B 1 155 ? 45.491 -31.054 -7.042  1.00 16.83 ?  155 VAL   B HA   1 
ATOM   6379 H HB   . VAL   B 1 155 ? 44.346 -32.659 -9.080  1.00 18.50 ?  155 VAL   B HB   1 
ATOM   6380 H HG11 . VAL   B 1 155 ? 43.694 -34.047 -7.215  1.00 18.16 ?  155 VAL   B HG11 1 
ATOM   6381 H HG12 . VAL   B 1 155 ? 45.233 -34.112 -7.602  1.00 18.16 ?  155 VAL   B HG12 1 
ATOM   6382 H HG13 . VAL   B 1 155 ? 44.760 -33.238 -6.360  1.00 18.16 ?  155 VAL   B HG13 1 
ATOM   6383 H HG21 . VAL   B 1 155 ? 42.292 -32.309 -7.988  1.00 19.37 ?  155 VAL   B HG21 1 
ATOM   6384 H HG22 . VAL   B 1 155 ? 43.010 -31.286 -7.006  1.00 19.37 ?  155 VAL   B HG22 1 
ATOM   6385 H HG23 . VAL   B 1 155 ? 42.884 -30.947 -8.553  1.00 19.37 ?  155 VAL   B HG23 1 
ATOM   6386 N N    . PHE   B 1 156 ? 47.705 -32.061 -7.216  1.00 13.89 ?  156 PHE   B N    1 
ATOM   6387 C CA   . PHE   B 1 156 ? 49.083 -32.518 -7.406  1.00 15.25 ?  156 PHE   B CA   1 
ATOM   6388 C C    . PHE   B 1 156 ? 49.177 -34.018 -7.690  1.00 15.99 ?  156 PHE   B C    1 
ATOM   6389 O O    . PHE   B 1 156 ? 49.903 -34.444 -8.598  1.00 17.84 ?  156 PHE   B O    1 
ATOM   6390 C CB   . PHE   B 1 156 ? 49.914 -32.145 -6.178  1.00 15.43 ?  156 PHE   B CB   1 
ATOM   6391 C CG   . PHE   B 1 156 ? 51.337 -32.611 -6.236  1.00 16.17 ?  156 PHE   B CG   1 
ATOM   6392 C CD1  . PHE   B 1 156 ? 52.222 -32.063 -7.142  1.00 17.65 ?  156 PHE   B CD1  1 
ATOM   6393 C CD2  . PHE   B 1 156 ? 51.792 -33.583 -5.368  1.00 16.60 ?  156 PHE   B CD2  1 
ATOM   6394 C CE1  . PHE   B 1 156 ? 53.542 -32.479 -7.188  1.00 18.33 ?  156 PHE   B CE1  1 
ATOM   6395 C CE2  . PHE   B 1 156 ? 53.110 -34.009 -5.410  1.00 18.03 ?  156 PHE   B CE2  1 
ATOM   6396 C CZ   . PHE   B 1 156 ? 53.978 -33.455 -6.324  1.00 18.31 ?  156 PHE   B CZ   1 
ATOM   6397 H H    . PHE   B 1 156 ? 47.516 -31.829 -6.407  1.00 16.66 ?  156 PHE   B H    1 
ATOM   6398 H HA   . PHE   B 1 156 ? 49.457 -32.054 -8.165  1.00 18.30 ?  156 PHE   B HA   1 
ATOM   6399 H HB2  . PHE   B 1 156 ? 49.925 -31.177 -6.095  1.00 18.51 ?  156 PHE   B HB2  1 
ATOM   6400 H HB3  . PHE   B 1 156 ? 49.509 -32.536 -5.390  1.00 18.51 ?  156 PHE   B HB3  1 
ATOM   6401 H HD1  . PHE   B 1 156 ? 51.936 -31.397 -7.728  1.00 21.17 ?  156 PHE   B HD1  1 
ATOM   6402 H HD2  . PHE   B 1 156 ? 51.201 -33.961 -4.754  1.00 19.91 ?  156 PHE   B HD2  1 
ATOM   6403 H HE1  . PHE   B 1 156 ? 54.134 -32.105 -7.804  1.00 21.99 ?  156 PHE   B HE1  1 
ATOM   6404 H HE2  . PHE   B 1 156 ? 53.401 -34.673 -4.826  1.00 21.63 ?  156 PHE   B HE2  1 
ATOM   6405 H HZ   . PHE   B 1 156 ? 54.865 -33.743 -6.353  1.00 21.97 ?  156 PHE   B HZ   1 
ATOM   6406 N N    . ASP   B 1 157 ? 48.510 -34.839 -6.888  1.00 16.42 ?  157 ASP   B N    1 
ATOM   6407 C CA   . ASP   B 1 157 ? 48.657 -36.288 -6.983  1.00 17.63 ?  157 ASP   B CA   1 
ATOM   6408 C C    . ASP   B 1 157 ? 47.742 -36.832 -8.075  1.00 17.86 ?  157 ASP   B C    1 
ATOM   6409 O O    . ASP   B 1 157 ? 46.517 -36.708 -7.975  1.00 17.31 ?  157 ASP   B O    1 
ATOM   6410 C CB   . ASP   B 1 157 ? 48.290 -36.901 -5.638  1.00 19.32 ?  157 ASP   B CB   1 
ATOM   6411 C CG   . ASP   B 1 157 ? 48.428 -38.411 -5.620  1.00 21.35 ?  157 ASP   B CG   1 
ATOM   6412 O OD1  . ASP   B 1 157 ? 48.751 -39.017 -6.669  1.00 21.72 ?  157 ASP   B OD1  1 
ATOM   6413 O OD2  . ASP   B 1 157 ? 48.220 -38.996 -4.539  1.00 23.39 -1 157 ASP   B OD2  1 
ATOM   6414 H H    . ASP   B 1 157 ? 47.967 -34.585 -6.275  1.00 19.70 ?  157 ASP   B H    1 
ATOM   6415 H HA   . ASP   B 1 157 ? 49.577 -36.521 -7.195  1.00 21.15 ?  157 ASP   B HA   1 
ATOM   6416 H HB2  . ASP   B 1 157 ? 48.864 -36.527 -4.955  1.00 23.17 ?  157 ASP   B HB2  1 
ATOM   6417 H HB3  . ASP   B 1 157 ? 47.362 -36.687 -5.441  1.00 23.17 ?  157 ASP   B HB3  1 
ATOM   6418 N N    . LYS   B 1 158 ? 48.336 -37.449 -9.105  1.00 18.92 ?  158 LYS   B N    1 
ATOM   6419 C CA   . LYS   B 1 158 ? 47.561 -38.068 -10.183 1.00 20.27 ?  158 LYS   B CA   1 
ATOM   6420 C C    . LYS   B 1 158 ? 46.503 -39.030 -9.649  1.00 20.11 ?  158 LYS   B C    1 
ATOM   6421 O O    . LYS   B 1 158 ? 45.396 -39.116 -10.197 1.00 20.09 ?  158 LYS   B O    1 
ATOM   6422 C CB   . LYS   B 1 158 ? 48.508 -38.795 -11.144 1.00 22.20 ?  158 LYS   B CB   1 
ATOM   6423 C CG   . LYS   B 1 158 ? 47.823 -39.689 -12.169 1.00 24.65 ?  158 LYS   B CG   1 
ATOM   6424 C CD   . LYS   B 1 158 ? 46.983 -38.895 -13.148 1.00 27.16 ?  158 LYS   B CD   1 
ATOM   6425 C CE   . LYS   B 1 158 ? 46.393 -39.803 -14.214 1.00 28.69 ?  158 LYS   B CE   1 
ATOM   6426 N NZ   . LYS   B 1 158 ? 45.327 -39.121 -15.002 1.00 29.27 ?  158 LYS   B NZ   1 
ATOM   6427 H H    . LYS   B 1 158 ? 49.192 -37.515 -9.206  1.00 22.70 ?  158 LYS   B H    1 
ATOM   6428 H HA   . LYS   B 1 158 ? 47.112 -37.371 -10.690 1.00 24.32 ?  158 LYS   B HA   1 
ATOM   6429 H HB2  . LYS   B 1 158 ? 49.024 -38.135 -11.640 1.00 26.63 ?  158 LYS   B HB2  1 
ATOM   6430 H HB3  . LYS   B 1 158 ? 49.111 -39.352 -10.628 1.00 26.63 ?  158 LYS   B HB3  1 
ATOM   6431 H HG2  . LYS   B 1 158 ? 48.502 -40.161 -12.677 1.00 29.58 ?  158 LYS   B HG2  1 
ATOM   6432 H HG3  . LYS   B 1 158 ? 47.249 -40.334 -11.722 1.00 29.58 ?  158 LYS   B HG3  1 
ATOM   6433 H HD2  . LYS   B 1 158 ? 46.255 -38.464 -12.675 1.00 32.59 ?  158 LYS   B HD2  1 
ATOM   6434 H HD3  . LYS   B 1 158 ? 47.541 -38.233 -13.587 1.00 32.59 ?  158 LYS   B HD3  1 
ATOM   6435 H HE2  . LYS   B 1 158 ? 47.093 -40.075 -14.826 1.00 34.42 ?  158 LYS   B HE2  1 
ATOM   6436 H HE3  . LYS   B 1 158 ? 46.000 -40.582 -13.788 1.00 34.42 ?  158 LYS   B HE3  1 
ATOM   6437 H HZ1  . LYS   B 1 158 ? 45.000 -39.675 -15.616 1.00 35.12 ?  158 LYS   B HZ1  1 
ATOM   6438 H HZ2  . LYS   B 1 158 ? 44.667 -38.863 -14.463 1.00 35.12 ?  158 LYS   B HZ2  1 
ATOM   6439 H HZ3  . LYS   B 1 158 ? 45.663 -38.404 -15.409 1.00 35.12 ?  158 LYS   B HZ3  1 
ATOM   6440 N N    . ASN   B 1 159 ? 46.824 -39.782 -8.596  1.00 20.36 ?  159 ASN   B N    1 
ATOM   6441 C CA   . ASN   B 1 159 ? 45.867 -40.763 -8.090  1.00 20.92 ?  159 ASN   B CA   1 
ATOM   6442 C C    . ASN   B 1 159 ? 44.669 -40.088 -7.422  1.00 19.64 ?  159 ASN   B C    1 
ATOM   6443 O O    . ASN   B 1 159 ? 43.535 -40.578 -7.525  1.00 20.34 ?  159 ASN   B O    1 
ATOM   6444 C CB   . ASN   B 1 159 ? 46.569 -41.736 -7.150  1.00 22.54 ?  159 ASN   B CB   1 
ATOM   6445 C CG   . ASN   B 1 159 ? 47.591 -42.586 -7.865  1.00 24.63 ?  159 ASN   B CG   1 
ATOM   6446 O OD1  . ASN   B 1 159 ? 47.338 -43.087 -8.968  1.00 25.20 ?  159 ASN   B OD1  1 
ATOM   6447 N ND2  . ASN   B 1 159 ? 48.757 -42.755 -7.247  1.00 25.33 ?  159 ASN   B ND2  1 
ATOM   6448 H H    . ASN   B 1 159 ? 47.570 -39.739 -8.175  1.00 24.43 ?  159 ASN   B H    1 
ATOM   6449 H HA   . ASN   B 1 159 ? 45.535 -41.274 -8.847  1.00 25.10 ?  159 ASN   B HA   1 
ATOM   6450 H HB2  . ASN   B 1 159 ? 47.024 -41.237 -6.456  1.00 27.04 ?  159 ASN   B HB2  1 
ATOM   6451 H HB3  . ASN   B 1 159 ? 45.910 -42.330 -6.764  1.00 27.04 ?  159 ASN   B HB3  1 
ATOM   6452 H HD21 . ASN   B 1 159 ? 49.379 -43.232 -7.610  1.00 30.39 ?  159 ASN   B HD21 1 
ATOM   6453 H HD22 . ASN   B 1 159 ? 48.893 -42.401 -6.473  1.00 30.39 ?  159 ASN   B HD22 1 
ATOM   6454 N N    . LEU   B 1 160 ? 44.887 -38.959 -6.742  1.00 18.70 ?  160 LEU   B N    1 
ATOM   6455 C CA   . LEU   B 1 160 ? 43.754 -38.222 -6.200  1.00 17.81 ?  160 LEU   B CA   1 
ATOM   6456 C C    . LEU   B 1 160 ? 42.964 -37.558 -7.315  1.00 17.09 ?  160 LEU   B C    1 
ATOM   6457 O O    . LEU   B 1 160 ? 41.728 -37.563 -7.296  1.00 16.89 ?  160 LEU   B O    1 
ATOM   6458 C CB   . LEU   B 1 160 ? 44.224 -37.188 -5.178  1.00 17.67 ?  160 LEU   B CB   1 
ATOM   6459 C CG   . LEU   B 1 160 ? 43.097 -36.292 -4.648  1.00 17.49 ?  160 LEU   B CG   1 
ATOM   6460 C CD1  . LEU   B 1 160 ? 41.967 -37.129 -4.050  1.00 18.20 ?  160 LEU   B CD1  1 
ATOM   6461 C CD2  . LEU   B 1 160 ? 43.633 -35.298 -3.628  1.00 17.59 ?  160 LEU   B CD2  1 
ATOM   6462 H H    . LEU   B 1 160 ? 45.662 -38.609 -6.593  1.00 22.43 ?  160 LEU   B H    1 
ATOM   6463 H HA   . LEU   B 1 160 ? 43.169 -38.848 -5.752  1.00 21.36 ?  160 LEU   B HA   1 
ATOM   6464 H HB2  . LEU   B 1 160 ? 44.621 -37.659 -4.424  1.00 21.20 ?  160 LEU   B HB2  1 
ATOM   6465 H HB3  . LEU   B 1 160 ? 44.894 -36.620 -5.594  1.00 21.20 ?  160 LEU   B HB3  1 
ATOM   6466 H HG   . LEU   B 1 160 ? 42.732 -35.786 -5.387  1.00 20.98 ?  160 LEU   B HG   1 
ATOM   6467 H HD11 . LEU   B 1 160 ? 41.348 -36.540 -3.597  1.00 21.83 ?  160 LEU   B HD11 1 
ATOM   6468 H HD12 . LEU   B 1 160 ? 41.509 -37.606 -4.762  1.00 21.83 ?  160 LEU   B HD12 1 
ATOM   6469 H HD13 . LEU   B 1 160 ? 42.342 -37.765 -3.417  1.00 21.83 ?  160 LEU   B HD13 1 
ATOM   6470 H HD21 . LEU   B 1 160 ? 42.906 -34.727 -3.342  1.00 21.10 ?  160 LEU   B HD21 1 
ATOM   6471 H HD22 . LEU   B 1 160 ? 43.992 -35.787 -2.871  1.00 21.10 ?  160 LEU   B HD22 1 
ATOM   6472 H HD23 . LEU   B 1 160 ? 44.331 -34.769 -4.043  1.00 21.10 ?  160 LEU   B HD23 1 
ATOM   6473 N N    . TYR   B 1 161 ? 43.662 -36.984 -8.298  1.00 17.22 ?  161 TYR   B N    1 
ATOM   6474 C CA   . TYR   B 1 161 ? 42.995 -36.420 -9.466  1.00 17.24 ?  161 TYR   B CA   1 
ATOM   6475 C C    . TYR   B 1 161 ? 42.050 -37.440 -10.090 1.00 17.28 ?  161 TYR   B C    1 
ATOM   6476 O O    . TYR   B 1 161 ? 40.878 -37.146 -10.342 1.00 17.11 ?  161 TYR   B O    1 
ATOM   6477 C CB   . TYR   B 1 161 ? 44.045 -35.945 -10.479 1.00 17.69 ?  161 TYR   B CB   1 
ATOM   6478 C CG   . TYR   B 1 161 ? 43.472 -35.478 -11.792 1.00 18.13 ?  161 TYR   B CG   1 
ATOM   6479 C CD1  . TYR   B 1 161 ? 43.083 -34.156 -11.964 1.00 18.26 ?  161 TYR   B CD1  1 
ATOM   6480 C CD2  . TYR   B 1 161 ? 43.300 -36.359 -12.856 1.00 18.64 ?  161 TYR   B CD2  1 
ATOM   6481 C CE1  . TYR   B 1 161 ? 42.553 -33.723 -13.151 1.00 19.25 ?  161 TYR   B CE1  1 
ATOM   6482 C CE2  . TYR   B 1 161 ? 42.769 -35.932 -14.051 1.00 19.68 ?  161 TYR   B CE2  1 
ATOM   6483 C CZ   . TYR   B 1 161 ? 42.399 -34.611 -14.193 1.00 19.66 ?  161 TYR   B CZ   1 
ATOM   6484 O OH   . TYR   B 1 161 ? 41.864 -34.175 -15.380 1.00 21.51 ?  161 TYR   B OH   1 
ATOM   6485 H H    . TYR   B 1 161 ? 44.515 -36.922 -8.319  1.00 20.65 ?  161 TYR   B H    1 
ATOM   6486 H HA   . TYR   B 1 161 ? 42.468 -35.653 -9.195  1.00 20.68 ?  161 TYR   B HA   1 
ATOM   6487 H HB2  . TYR   B 1 161 ? 44.532 -35.198 -10.094 1.00 21.23 ?  161 TYR   B HB2  1 
ATOM   6488 H HB3  . TYR   B 1 161 ? 44.653 -36.672 -10.668 1.00 21.23 ?  161 TYR   B HB3  1 
ATOM   6489 H HD1  . TYR   B 1 161 ? 43.190 -33.550 -11.266 1.00 21.91 ?  161 TYR   B HD1  1 
ATOM   6490 H HD2  . TYR   B 1 161 ? 43.547 -37.249 -12.763 1.00 22.36 ?  161 TYR   B HD2  1 
ATOM   6491 H HE1  . TYR   B 1 161 ? 42.305 -32.829 -13.251 1.00 23.09 ?  161 TYR   B HE1  1 
ATOM   6492 H HE2  . TYR   B 1 161 ? 42.658 -36.527 -14.758 1.00 23.61 ?  161 TYR   B HE2  1 
ATOM   6493 H HH   . TYR   B 1 161 ? 41.816 -34.815 -15.924 1.00 25.81 ?  161 TYR   B HH   1 
ATOM   6494 N N    . ASP   B 1 162 ? 42.542 -38.660 -10.318 1.00 17.87 ?  162 ASP   B N    1 
ATOM   6495 C CA   . ASP   B 1 162 ? 41.712 -39.693 -10.935 1.00 18.26 ?  162 ASP   B CA   1 
ATOM   6496 C C    . ASP   B 1 162 ? 40.509 -40.037 -10.065 1.00 17.88 ?  162 ASP   B C    1 
ATOM   6497 O O    . ASP   B 1 162 ? 39.405 -40.250 -10.579 1.00 18.07 ?  162 ASP   B O    1 
ATOM   6498 C CB   . ASP   B 1 162 ? 42.537 -40.957 -11.190 1.00 19.64 ?  162 ASP   B CB   1 
ATOM   6499 C CG   . ASP   B 1 162 ? 43.547 -40.793 -12.309 1.00 21.11 ?  162 ASP   B CG   1 
ATOM   6500 O OD1  . ASP   B 1 162 ? 43.421 -39.849 -13.111 1.00 21.51 ?  162 ASP   B OD1  1 
ATOM   6501 O OD2  . ASP   B 1 162 ? 44.452 -41.648 -12.406 1.00 22.57 -1 162 ASP   B OD2  1 
ATOM   6502 H H    . ASP   B 1 162 ? 43.339 -38.909 -10.131 1.00 21.44 ?  162 ASP   B H    1 
ATOM   6503 H HA   . ASP   B 1 162 ? 41.382 -39.370 -11.787 1.00 21.91 ?  162 ASP   B HA   1 
ATOM   6504 H HB2  . ASP   B 1 162 ? 43.024 -41.184 -10.385 1.00 23.56 ?  162 ASP   B HB2  1 
ATOM   6505 H HB3  . ASP   B 1 162 ? 41.941 -41.678 -11.437 1.00 23.56 ?  162 ASP   B HB3  1 
ATOM   6506 N N    . LYS   B 1 163 ? 40.701 -40.109 -8.746  1.00 17.11 ?  163 LYS   B N    1 
ATOM   6507 C CA   . LYS   B 1 163 ? 39.577 -40.385 -7.858  1.00 17.94 ?  163 LYS   B CA   1 
ATOM   6508 C C    . LYS   B 1 163 ? 38.534 -39.276 -7.921  1.00 16.57 ?  163 LYS   B C    1 
ATOM   6509 O O    . LYS   B 1 163 ? 37.325 -39.547 -7.915  1.00 17.50 ?  163 LYS   B O    1 
ATOM   6510 C CB   . LYS   B 1 163 ? 40.066 -40.562 -6.424  1.00 21.13 ?  163 LYS   B CB   1 
ATOM   6511 C CG   . LYS   B 1 163 ? 38.974 -41.041 -5.490  1.00 27.09 ?  163 LYS   B CG   1 
ATOM   6512 C CD   . LYS   B 1 163 ? 39.470 -41.282 -4.077  1.00 32.86 ?  163 LYS   B CD   1 
ATOM   6513 C CE   . LYS   B 1 163 ? 38.386 -41.955 -3.242  1.00 37.22 ?  163 LYS   B CE   1 
ATOM   6514 N NZ   . LYS   B 1 163 ? 38.499 -41.618 -1.796  1.00 39.86 ?  163 LYS   B NZ   1 
ATOM   6515 H H    . LYS   B 1 163 ? 41.458 -39.999 -8.352  1.00 20.52 ?  163 LYS   B H    1 
ATOM   6516 H HA   . LYS   B 1 163 ? 39.153 -41.210 -8.137  1.00 21.52 ?  163 LYS   B HA   1 
ATOM   6517 H HB2  . LYS   B 1 163 ? 40.781 -41.221 -6.415  1.00 25.35 ?  163 LYS   B HB2  1 
ATOM   6518 H HB3  . LYS   B 1 163 ? 40.394 -39.713 -6.094  1.00 25.35 ?  163 LYS   B HB3  1 
ATOM   6519 H HG2  . LYS   B 1 163 ? 38.275 -40.373 -5.451  1.00 32.50 ?  163 LYS   B HG2  1 
ATOM   6520 H HG3  . LYS   B 1 163 ? 38.615 -41.878 -5.829  1.00 32.50 ?  163 LYS   B HG3  1 
ATOM   6521 H HD2  . LYS   B 1 163 ? 40.246 -41.867 -4.101  1.00 39.43 ?  163 LYS   B HD2  1 
ATOM   6522 H HD3  . LYS   B 1 163 ? 39.697 -40.436 -3.665  1.00 39.43 ?  163 LYS   B HD3  1 
ATOM   6523 H HE2  . LYS   B 1 163 ? 37.514 -41.669 -3.558  1.00 44.65 ?  163 LYS   B HE2  1 
ATOM   6524 H HE3  . LYS   B 1 163 ? 38.469 -42.917 -3.334  1.00 44.65 ?  163 LYS   B HE3  1 
ATOM   6525 H HZ1  . LYS   B 1 163 ? 37.852 -42.024 -1.338  1.00 47.83 ?  163 LYS   B HZ1  1 
ATOM   6526 H HZ2  . LYS   B 1 163 ? 39.287 -41.886 -1.482  1.00 47.83 ?  163 LYS   B HZ2  1 
ATOM   6527 H HZ3  . LYS   B 1 163 ? 38.425 -40.738 -1.682  1.00 47.83 ?  163 LYS   B HZ3  1 
ATOM   6528 N N    . LEU   B 1 164 ? 38.986 -38.021 -7.965  1.00 15.34 ?  164 LEU   B N    1 
ATOM   6529 C CA   . LEU   B 1 164 ? 38.075 -36.882 -8.025  1.00 15.19 ?  164 LEU   B CA   1 
ATOM   6530 C C    . LEU   B 1 164 ? 37.299 -36.863 -9.336  1.00 15.39 ?  164 LEU   B C    1 
ATOM   6531 O O    . LEU   B 1 164 ? 36.075 -36.665 -9.347  1.00 16.35 ?  164 LEU   B O    1 
ATOM   6532 C CB   . LEU   B 1 164 ? 38.878 -35.591 -7.862  1.00 14.72 ?  164 LEU   B CB   1 
ATOM   6533 C CG   . LEU   B 1 164 ? 39.403 -35.301 -6.458  1.00 15.78 ?  164 LEU   B CG   1 
ATOM   6534 C CD1  . LEU   B 1 164 ? 40.501 -34.243 -6.512  1.00 15.84 ?  164 LEU   B CD1  1 
ATOM   6535 C CD2  . LEU   B 1 164 ? 38.279 -34.859 -5.533  1.00 17.71 ?  164 LEU   B CD2  1 
ATOM   6536 H H    . LEU   B 1 164 ? 39.826 -37.805 -7.958  1.00 18.40 ?  164 LEU   B H    1 
ATOM   6537 H HA   . LEU   B 1 164 ? 37.447 -36.940 -7.298  1.00 18.23 ?  164 LEU   B HA   1 
ATOM   6538 H HB2  . LEU   B 1 164 ? 39.652 -35.630 -8.451  1.00 17.66 ?  164 LEU   B HB2  1 
ATOM   6539 H HB3  . LEU   B 1 164 ? 38.318 -34.846 -8.119  1.00 17.66 ?  164 LEU   B HB3  1 
ATOM   6540 H HG   . LEU   B 1 164 ? 39.793 -36.106 -6.091  1.00 18.93 ?  164 LEU   B HG   1 
ATOM   6541 H HD11 . LEU   B 1 164 ? 40.818 -34.060 -5.611  1.00 19.00 ?  164 LEU   B HD11 1 
ATOM   6542 H HD12 . LEU   B 1 164 ? 41.238 -34.572 -7.055  1.00 19.00 ?  164 LEU   B HD12 1 
ATOM   6543 H HD13 . LEU   B 1 164 ? 40.146 -33.428 -6.904  1.00 19.00 ?  164 LEU   B HD13 1 
ATOM   6544 H HD21 . LEU   B 1 164 ? 38.647 -34.633 -4.665  1.00 21.25 ?  164 LEU   B HD21 1 
ATOM   6545 H HD22 . LEU   B 1 164 ? 37.836 -34.085 -5.916  1.00 21.25 ?  164 LEU   B HD22 1 
ATOM   6546 H HD23 . LEU   B 1 164 ? 37.643 -35.588 -5.441  1.00 21.25 ?  164 LEU   B HD23 1 
ATOM   6547 N N    . VAL   B 1 165 ? 37.998 -37.039 -10.456 1.00 16.79 ?  165 VAL   B N    1 
ATOM   6548 C CA   . VAL   B 1 165 ? 37.349 -36.980 -11.758 1.00 17.96 ?  165 VAL   B CA   1 
ATOM   6549 C C    . VAL   B 1 165 ? 36.427 -38.179 -11.942 1.00 19.76 ?  165 VAL   B C    1 
ATOM   6550 O O    . VAL   B 1 165 ? 35.268 -38.039 -12.349 1.00 20.83 ?  165 VAL   B O    1 
ATOM   6551 C CB   . VAL   B 1 165 ? 38.402 -36.896 -12.878 1.00 18.97 ?  165 VAL   B CB   1 
ATOM   6552 C CG1  . VAL   B 1 165 ? 37.746 -36.996 -14.233 1.00 20.45 ?  165 VAL   B CG1  1 
ATOM   6553 C CG2  . VAL   B 1 165 ? 39.192 -35.605 -12.761 1.00 18.54 ?  165 VAL   B CG2  1 
ATOM   6554 H H    . VAL   B 1 165 ? 38.851 -37.184 -10.488 1.00 20.14 ?  165 VAL   B H    1 
ATOM   6555 H HA   . VAL   B 1 165 ? 36.808 -36.183 -11.804 1.00 21.54 ?  165 VAL   B HA   1 
ATOM   6556 H HB   . VAL   B 1 165 ? 39.029 -37.632 -12.788 1.00 22.76 ?  165 VAL   B HB   1 
ATOM   6557 H HG11 . VAL   B 1 165 ? 38.373 -36.702 -14.909 1.00 24.54 ?  165 VAL   B HG11 1 
ATOM   6558 H HG12 . VAL   B 1 165 ? 37.502 -37.923 -14.394 1.00 24.54 ?  165 VAL   B HG12 1 
ATOM   6559 H HG13 . VAL   B 1 165 ? 36.956 -36.438 -14.242 1.00 24.54 ?  165 VAL   B HG13 1 
ATOM   6560 H HG21 . VAL   B 1 165 ? 39.832 -35.553 -13.490 1.00 22.24 ?  165 VAL   B HG21 1 
ATOM   6561 H HG22 . VAL   B 1 165 ? 38.579 -34.851 -12.810 1.00 22.24 ?  165 VAL   B HG22 1 
ATOM   6562 H HG23 . VAL   B 1 165 ? 39.661 -35.589 -11.911 1.00 22.24 ?  165 VAL   B HG23 1 
ATOM   6563 N N    . SER   B 1 166 ? 36.934 -39.379 -11.640 1.00 20.74 ?  166 SER   B N    1 
ATOM   6564 C CA   . SER   B 1 166 ? 36.175 -40.589 -11.922 1.00 21.99 ?  166 SER   B CA   1 
ATOM   6565 C C    . SER   B 1 166 ? 34.916 -40.672 -11.075 1.00 22.49 ?  166 SER   B C    1 
ATOM   6566 O O    . SER   B 1 166 ? 33.942 -41.290 -11.500 1.00 23.97 ?  166 SER   B O    1 
ATOM   6567 C CB   . SER   B 1 166 ? 37.041 -41.844 -11.756 1.00 22.66 ?  166 SER   B CB   1 
ATOM   6568 O OG   . SER   B 1 166 ? 37.411 -42.051 -10.403 1.00 22.68 ?  166 SER   B OG   1 
ATOM   6569 H H    . SER   B 1 166 ? 37.709 -39.518 -11.281 1.00 24.88 ?  166 SER   B H    1 
ATOM   6570 H HA   . SER   B 1 166 ? 35.897 -40.563 -12.848 1.00 26.38 ?  166 SER   B HA   1 
ATOM   6571 H HB2  . SER   B 1 166 ? 36.540 -42.616 -12.064 1.00 27.18 ?  166 SER   B HB2  1 
ATOM   6572 H HB3  . SER   B 1 166 ? 37.844 -41.744 -12.299 1.00 27.18 ?  166 SER   B HB3  1 
ATOM   6573 H HG   . SER   B 1 166 ? 37.873 -41.403 -10.132 1.00 27.21 ?  166 SER   B HG   1 
ATOM   6574 N N    . SER   B 1 167 ? 34.900 -40.066 -9.890  1.00 20.96 ?  167 SER   B N    1 
ATOM   6575 C CA   . SER   B 1 167 ? 33.740 -40.115 -9.008  1.00 20.46 ?  167 SER   B CA   1 
ATOM   6576 C C    . SER   B 1 167 ? 32.830 -38.892 -9.116  1.00 19.70 ?  167 SER   B C    1 
ATOM   6577 O O    . SER   B 1 167 ? 31.749 -38.891 -8.516  1.00 19.72 ?  167 SER   B O    1 
ATOM   6578 C CB   . SER   B 1 167 ? 34.179 -40.289 -7.548  1.00 20.41 ?  167 SER   B CB   1 
ATOM   6579 O OG   . SER   B 1 167 ? 34.847 -39.127 -7.079  1.00 20.39 ?  167 SER   B OG   1 
ATOM   6580 H H    . SER   B 1 167 ? 35.554 -39.621 -9.573  1.00 25.15 ?  167 SER   B H    1 
ATOM   6581 H HA   . SER   B 1 167 ? 33.207 -40.895 -9.240  1.00 24.54 ?  167 SER   B HA   1 
ATOM   6582 H HB2  . SER   B 1 167 ? 33.394 -40.449 -6.998  1.00 24.49 ?  167 SER   B HB2  1 
ATOM   6583 H HB3  . SER   B 1 167 ? 34.778 -41.055 -7.490  1.00 24.49 ?  167 SER   B HB3  1 
ATOM   6584 H HG   . SER   B 1 167 ? 35.533 -38.992 -7.545  1.00 24.46 ?  167 SER   B HG   1 
ATOM   6585 N N    . PHE   B 1 168 ? 33.214 -37.862 -9.870  1.00 19.33 ?  168 PHE   B N    1 
ATOM   6586 C CA   . PHE   B 1 168 ? 32.385 -36.657 -9.936  1.00 18.88 ?  168 PHE   B CA   1 
ATOM   6587 C C    . PHE   B 1 168 ? 31.068 -36.915 -10.663 1.00 16.88 ?  168 PHE   B C    1 
ATOM   6588 O O    . PHE   B 1 168 ? 30.029 -36.318 -10.319 1.00 17.30 ?  168 PHE   B O    1 
ATOM   6589 C CB   . PHE   B 1 168 ? 33.147 -35.519 -10.611 1.00 19.22 ?  168 PHE   B CB   1 
ATOM   6590 C CG   . PHE   B 1 168 ? 32.338 -34.272 -10.752 1.00 19.01 ?  168 PHE   B CG   1 
ATOM   6591 C CD1  . PHE   B 1 168 ? 31.990 -33.534 -9.629  1.00 20.28 ?  168 PHE   B CD1  1 
ATOM   6592 C CD2  . PHE   B 1 168 ? 31.892 -33.851 -11.990 1.00 18.59 ?  168 PHE   B CD2  1 
ATOM   6593 C CE1  . PHE   B 1 168 ? 31.221 -32.390 -9.738  1.00 20.77 ?  168 PHE   B CE1  1 
ATOM   6594 C CE2  . PHE   B 1 168 ? 31.141 -32.689 -12.111 1.00 19.68 ?  168 PHE   B CE2  1 
ATOM   6595 C CZ   . PHE   B 1 168 ? 30.794 -31.962 -10.981 1.00 20.16 ?  168 PHE   B CZ   1 
ATOM   6596 H H    . PHE   B 1 168 ? 33.932 -37.835 -10.340 1.00 23.19 ?  168 PHE   B H    1 
ATOM   6597 H HA   . PHE   B 1 168 ? 32.168 -36.380 -9.036  1.00 22.65 ?  168 PHE   B HA   1 
ATOM   6598 H HB2  . PHE   B 1 168 ? 33.928 -35.310 -10.078 1.00 23.06 ?  168 PHE   B HB2  1 
ATOM   6599 H HB3  . PHE   B 1 168 ? 33.414 -35.801 -11.498 1.00 23.06 ?  168 PHE   B HB3  1 
ATOM   6600 H HD1  . PHE   B 1 168 ? 32.268 -33.823 -8.790  1.00 24.33 ?  168 PHE   B HD1  1 
ATOM   6601 H HD2  . PHE   B 1 168 ? 32.122 -34.326 -12.752 1.00 22.30 ?  168 PHE   B HD2  1 
ATOM   6602 H HE1  . PHE   B 1 168 ? 30.995 -31.906 -8.976  1.00 24.92 ?  168 PHE   B HE1  1 
ATOM   6603 H HE2  . PHE   B 1 168 ? 30.847 -32.408 -12.949 1.00 23.61 ?  168 PHE   B HE2  1 
ATOM   6604 H HZ   . PHE   B 1 168 ? 30.279 -31.190 -11.061 1.00 24.18 ?  168 PHE   B HZ   1 
ATOM   6605 N N    . LEU   B 1 169 ? 31.096 -37.786 -11.669 1.00 17.22 ?  169 LEU   B N    1 
ATOM   6606 C CA   . LEU   B 1 169 ? 29.914 -38.098 -12.462 1.00 19.28 ?  169 LEU   B CA   1 
ATOM   6607 C C    . LEU   B 1 169 ? 29.909 -39.540 -12.956 1.00 22.11 ?  169 LEU   B C    1 
ATOM   6608 O O    . LEU   B 1 169 ? 28.991 -39.965 -13.660 1.00 24.33 ?  169 LEU   B O    1 
ATOM   6609 C CB   . LEU   B 1 169 ? 29.833 -37.163 -13.667 1.00 20.98 ?  169 LEU   B CB   1 
ATOM   6610 C CG   . LEU   B 1 169 ? 28.570 -36.310 -13.774 1.00 23.99 ?  169 LEU   B CG   1 
ATOM   6611 C CD1  . LEU   B 1 169 ? 28.521 -35.648 -15.131 1.00 25.03 ?  169 LEU   B CD1  1 
ATOM   6612 C CD2  . LEU   B 1 169 ? 27.321 -37.136 -13.532 1.00 23.96 ?  169 LEU   B CD2  1 
ATOM   6613 O OXT  . LEU   B 1 169 ? 30.832 -40.303 -12.678 1.00 23.18 -1 169 LEU   B OXT  1 
ATOM   6614 H H    . LEU   B 1 169 ? 31.800 -38.209 -11.926 1.00 20.66 ?  169 LEU   B H    1 
ATOM   6615 H HA   . LEU   B 1 169 ? 29.130 -37.955 -11.912 1.00 23.13 ?  169 LEU   B HA   1 
ATOM   6616 H HB2  . LEU   B 1 169 ? 30.588 -36.554 -13.637 1.00 25.17 ?  169 LEU   B HB2  1 
ATOM   6617 H HB3  . LEU   B 1 169 ? 29.883 -37.697 -14.477 1.00 25.17 ?  169 LEU   B HB3  1 
ATOM   6618 H HG   . LEU   B 1 169 ? 28.603 -35.610 -13.102 1.00 28.79 ?  169 LEU   B HG   1 
ATOM   6619 H HD11 . LEU   B 1 169 ? 27.732 -35.087 -15.178 1.00 30.03 ?  169 LEU   B HD11 1 
ATOM   6620 H HD12 . LEU   B 1 169 ? 29.319 -35.110 -15.246 1.00 30.03 ?  169 LEU   B HD12 1 
ATOM   6621 H HD13 . LEU   B 1 169 ? 28.482 -36.336 -15.813 1.00 30.03 ?  169 LEU   B HD13 1 
ATOM   6622 H HD21 . LEU   B 1 169 ? 26.567 -36.702 -13.954 1.00 28.75 ?  169 LEU   B HD21 1 
ATOM   6623 H HD22 . LEU   B 1 169 ? 27.451 -38.020 -13.913 1.00 28.75 ?  169 LEU   B HD22 1 
ATOM   6624 H HD23 . LEU   B 1 169 ? 27.173 -37.208 -12.577 1.00 28.75 ?  169 LEU   B HD23 1 
HETATM 6625 C C1   T TFA   C 2 .   ? 12.141 -1.304  1.449   0.20 10.61 ?  201 TFA   A C1   1 
HETATM 6626 C C2   T TFA   C 2 .   ? 12.755 -1.754  0.099   0.20 12.93 ?  201 TFA   A C2   1 
HETATM 6627 O O    T TFA   C 2 .   ? 12.853 -1.562  2.426   0.20 9.95  ?  201 TFA   A O    1 
HETATM 6628 F F1   T TFA   C 2 .   ? 12.780 -3.098  0.018   0.20 13.91 ?  201 TFA   A F1   1 
HETATM 6629 F F2   T TFA   C 2 .   ? 12.054 -1.314  -0.959  0.20 13.39 ?  201 TFA   A F2   1 
HETATM 6630 F F3   T TFA   C 2 .   ? 14.006 -1.314  -0.078  0.20 14.02 ?  201 TFA   A F3   1 
HETATM 6631 O OXT  T TFA   C 2 .   ? 11.043 -0.752  1.364   0.20 9.95  ?  201 TFA   A OXT  1 
HETATM 6632 N N2   B A1BAK D 3 .   ? 15.016 -0.093  4.083   0.40 13.61 ?  202 A1BAK A N2   1 
HETATM 6633 C C3   B A1BAK D 3 .   ? 14.648 2.171   1.071   0.40 14.49 ?  202 A1BAK A C3   1 
HETATM 6634 C C6   B A1BAK D 3 .   ? 15.291 2.149   5.565   0.40 12.42 ?  202 A1BAK A C6   1 
HETATM 6635 C C9   B A1BAK D 3 .   ? 15.524 4.352   5.160   0.40 12.52 ?  202 A1BAK A C9   1 
HETATM 6636 C C1   B A1BAK D 3 .   ? 14.635 0.150   -0.332  0.40 17.33 ?  202 A1BAK A C1   1 
HETATM 6637 C C10  B A1BAK D 3 .   ? 15.038 -0.219  1.152   0.40 15.41 ?  202 A1BAK A C10  1 
HETATM 6638 C C2   B A1BAK D 3 .   ? 14.228 1.624   -0.313  0.40 16.50 ?  202 A1BAK A C2   1 
HETATM 6639 C C4   B A1BAK D 3 .   ? 15.113 1.073   3.377   0.40 13.27 ?  202 A1BAK A C4   1 
HETATM 6640 C C5   B A1BAK D 3 .   ? 15.046 -0.098  5.472   0.40 13.91 ?  202 A1BAK A C5   1 
HETATM 6641 C C7   B A1BAK D 3 .   ? 15.266 2.297   4.124   0.40 12.60 ?  202 A1BAK A C7   1 
HETATM 6642 C C8   B A1BAK D 3 .   ? 15.424 3.738   3.916   0.40 13.14 ?  202 A1BAK A C8   1 
HETATM 6643 N N1   B A1BAK D 3 .   ? 15.066 1.033   1.950   0.40 14.01 ?  202 A1BAK A N1   1 
HETATM 6644 N N3   B A1BAK D 3 .   ? 15.176 0.973   6.238   0.40 13.51 ?  202 A1BAK A N3   1 
HETATM 6645 N N4   B A1BAK D 3 .   ? 15.438 3.373   6.091   0.40 12.12 ?  202 A1BAK A N4   1 
HETATM 6646 O O1   B A1BAK D 3 .   ? 15.756 0.004   -1.157  0.40 19.42 ?  202 A1BAK A O1   1 
HETATM 6647 H H6   B A1BAK D 3 .   ? 13.818 2.757   1.517   0.40 17.38 ?  202 A1BAK A H6   1 
HETATM 6648 H H5   B A1BAK D 3 .   ? 15.454 2.921   0.898   0.40 17.38 ?  202 A1BAK A H5   1 
HETATM 6649 H H9   B A1BAK D 3 .   ? 15.636 5.371   5.511   0.40 15.02 ?  202 A1BAK A H9   1 
HETATM 6650 H H1   B A1BAK D 3 .   ? 13.794 -0.507  -0.683  0.40 20.79 ?  202 A1BAK A H1   1 
HETATM 6651 H H11  B A1BAK D 3 .   ? 16.012 -0.759  1.129   0.40 18.48 ?  202 A1BAK A H11  1 
HETATM 6652 H H12  B A1BAK D 3 .   ? 14.300 -0.949  1.557   0.40 18.48 ?  202 A1BAK A H12  1 
HETATM 6653 H H3   B A1BAK D 3 .   ? 13.137 1.754   -0.533  0.40 19.79 ?  202 A1BAK A H3   1 
HETATM 6654 H H4   B A1BAK D 3 .   ? 14.698 2.189   -1.150  0.40 19.79 ?  202 A1BAK A H4   1 
HETATM 6655 H H7   B A1BAK D 3 .   ? 14.946 -1.049  6.052   0.40 16.68 ?  202 A1BAK A H7   1 
HETATM 6656 H H8   B A1BAK D 3 .   ? 15.455 4.288   3.006   0.40 15.76 ?  202 A1BAK A H8   1 
HETATM 6657 H H10  B A1BAK D 3 .   ? 15.480 3.572   7.122   0.40 14.54 ?  202 A1BAK A H10  1 
HETATM 6658 H H2   B A1BAK D 3 .   ? 15.624 -0.690  -1.810  0.40 23.30 ?  202 A1BAK A H2   1 
HETATM 6659 O O    . HOH   E 4 .   ? 14.686 -4.676  20.505  1.00 45.65 ?  301 HOH   A O    1 
HETATM 6660 O O    B HOH   E 4 .   ? 5.308  3.993   -0.037  0.40 31.86 ?  302 HOH   A O    1 
HETATM 6661 O O    . HOH   E 4 .   ? 10.426 -22.192 -1.220  1.00 51.38 ?  303 HOH   A O    1 
HETATM 6662 O O    . HOH   E 4 .   ? 17.125 -18.032 14.946  1.00 28.11 ?  304 HOH   A O    1 
HETATM 6663 O O    B HOH   E 4 .   ? 14.801 7.036   7.467   0.40 19.33 ?  305 HOH   A O    1 
HETATM 6664 O O    . HOH   E 4 .   ? 11.957 0.309   14.708  1.00 33.15 ?  306 HOH   A O    1 
HETATM 6665 O O    B HOH   E 4 .   ? 16.533 -2.591  -1.407  0.40 35.68 ?  307 HOH   A O    1 
HETATM 6666 O O    A HOH   E 4 .   ? 4.656  3.940   0.588   0.60 20.08 ?  308 HOH   A O    1 
HETATM 6667 O O    . HOH   E 4 .   ? 34.334 -1.812  12.521  1.00 38.45 ?  309 HOH   A O    1 
HETATM 6668 O O    . HOH   E 4 .   ? 7.626  -6.301  -6.656  1.00 42.20 ?  310 HOH   A O    1 
HETATM 6669 O O    . HOH   E 4 .   ? 15.048 -12.211 18.671  1.00 38.57 ?  311 HOH   A O    1 
HETATM 6670 O O    . HOH   E 4 .   ? 11.771 -10.847 -10.098 1.00 46.23 ?  312 HOH   A O    1 
HETATM 6671 O O    . HOH   E 4 .   ? 9.527  -16.277 -2.461  1.00 45.85 ?  313 HOH   A O    1 
HETATM 6672 O O    . HOH   E 4 .   ? 28.946 0.464   -9.704  1.00 22.32 ?  314 HOH   A O    1 
HETATM 6673 O O    B HOH   E 4 .   ? 21.627 3.032   0.008   0.40 19.98 ?  315 HOH   A O    1 
HETATM 6674 O O    . HOH   E 4 .   ? 30.953 6.176   -12.268 1.00 29.60 ?  316 HOH   A O    1 
HETATM 6675 O O    B HOH   E 4 .   ? 18.729 -0.525  -2.420  0.40 23.49 ?  317 HOH   A O    1 
HETATM 6676 O O    A HOH   E 4 .   ? 14.594 -3.634  3.080   0.60 16.99 ?  318 HOH   A O    1 
HETATM 6677 O O    . HOH   E 4 .   ? 28.367 -0.171  -13.404 1.00 36.73 ?  319 HOH   A O    1 
HETATM 6678 O O    . HOH   E 4 .   ? 9.067  -10.145 19.302  1.00 39.27 ?  320 HOH   A O    1 
HETATM 6679 O O    B HOH   E 4 .   ? 8.498  3.963   1.408   0.40 28.92 ?  321 HOH   A O    1 
HETATM 6680 O O    . HOH   E 4 .   ? 15.033 3.957   17.706  1.00 42.69 ?  322 HOH   A O    1 
HETATM 6681 O O    . HOH   E 4 .   ? 42.383 10.544  5.168   1.00 20.69 ?  323 HOH   A O    1 
HETATM 6682 O O    . HOH   E 4 .   ? 14.655 -13.900 16.669  1.00 25.63 ?  324 HOH   A O    1 
HETATM 6683 O O    . HOH   E 4 .   ? 30.237 -13.298 -8.519  1.00 23.06 ?  325 HOH   A O    1 
HETATM 6684 O O    . HOH   E 4 .   ? -0.710 -8.496  2.152   1.00 43.41 ?  326 HOH   A O    1 
HETATM 6685 O O    . HOH   E 4 .   ? 8.795  -12.071 17.107  1.00 40.28 ?  327 HOH   A O    1 
HETATM 6686 O O    . HOH   E 4 .   ? 36.091 -5.060  -0.522  1.00 29.84 ?  328 HOH   A O    1 
HETATM 6687 O O    . HOH   E 4 .   ? 14.137 -4.516  -11.930 1.00 34.50 ?  329 HOH   A O    1 
HETATM 6688 O O    . HOH   E 4 .   ? 0.693  -4.401  0.104   1.00 33.74 ?  330 HOH   A O    1 
HETATM 6689 O O    . HOH   E 4 .   ? 9.872  -21.377 5.644   1.00 20.92 ?  331 HOH   A O    1 
HETATM 6690 O O    A HOH   E 4 .   ? 6.895  -8.144  11.818  0.60 17.02 ?  332 HOH   A O    1 
HETATM 6691 O O    . HOH   E 4 .   ? 19.920 -12.515 -8.881  1.00 26.18 ?  333 HOH   A O    1 
HETATM 6692 O O    . HOH   E 4 .   ? 28.124 -6.269  19.647  1.00 43.60 ?  334 HOH   A O    1 
HETATM 6693 O O    . HOH   E 4 .   ? 13.543 -15.194 -7.538  1.00 27.47 ?  335 HOH   A O    1 
HETATM 6694 O O    . HOH   E 4 .   ? 14.388 -24.650 11.583  1.00 40.96 ?  336 HOH   A O    1 
HETATM 6695 O O    . HOH   E 4 .   ? 26.466 -19.308 -1.793  1.00 14.97 ?  337 HOH   A O    1 
HETATM 6696 O O    . HOH   E 4 .   ? 18.620 -19.356 13.538  1.00 40.19 ?  338 HOH   A O    1 
HETATM 6697 O O    . HOH   E 4 .   ? 33.975 -0.955  -8.890  1.00 28.59 ?  339 HOH   A O    1 
HETATM 6698 O O    . HOH   E 4 .   ? 37.476 2.788   10.179  1.00 29.16 ?  340 HOH   A O    1 
HETATM 6699 O O    . HOH   E 4 .   ? 7.952  -21.455 3.983   1.00 48.57 ?  341 HOH   A O    1 
HETATM 6700 O O    . HOH   E 4 .   ? 27.907 0.842   -7.146  1.00 14.74 ?  342 HOH   A O    1 
HETATM 6701 O O    . HOH   E 4 .   ? 27.329 13.776  2.870   1.00 30.85 ?  343 HOH   A O    1 
HETATM 6702 O O    . HOH   E 4 .   ? 30.985 -18.111 7.790   1.00 20.54 ?  344 HOH   A O    1 
HETATM 6703 O O    . HOH   E 4 .   ? 38.218 10.127  7.197   1.00 40.95 ?  345 HOH   A O    1 
HETATM 6704 O O    . HOH   E 4 .   ? 18.876 -21.977 6.990   1.00 33.72 ?  346 HOH   A O    1 
HETATM 6705 O O    . HOH   E 4 .   ? 44.241 7.113   6.468   1.00 26.51 ?  347 HOH   A O    1 
HETATM 6706 O O    A HOH   E 4 .   ? 11.027 -0.359  1.913   0.40 17.56 ?  348 HOH   A O    1 
HETATM 6707 O O    . HOH   E 4 .   ? 22.226 5.420   18.903  1.00 43.10 ?  349 HOH   A O    1 
HETATM 6708 O O    . HOH   E 4 .   ? 20.615 -19.692 -5.102  1.00 27.88 ?  350 HOH   A O    1 
HETATM 6709 O O    . HOH   E 4 .   ? 38.508 4.966   6.976   1.00 16.10 ?  351 HOH   A O    1 
HETATM 6710 O O    . HOH   E 4 .   ? 26.799 11.401  1.674   1.00 17.51 ?  352 HOH   A O    1 
HETATM 6711 O O    A HOH   E 4 .   ? 3.548  -9.445  9.695   0.60 22.00 ?  353 HOH   A O    1 
HETATM 6712 O O    . HOH   E 4 .   ? 25.708 -0.781  -7.353  1.00 17.37 ?  354 HOH   A O    1 
HETATM 6713 O O    A HOH   E 4 .   ? 14.229 0.592   6.784   0.60 19.49 ?  355 HOH   A O    1 
HETATM 6714 O O    . HOH   E 4 .   ? 42.480 4.275   5.384   1.00 30.68 ?  356 HOH   A O    1 
HETATM 6715 O O    . HOH   E 4 .   ? 39.731 -1.026  -5.146  1.00 21.81 ?  357 HOH   A O    1 
HETATM 6716 O O    . HOH   E 4 .   ? 35.739 -12.641 6.851   1.00 16.56 ?  358 HOH   A O    1 
HETATM 6717 O O    . HOH   E 4 .   ? 17.148 -17.788 -5.072  1.00 27.83 ?  359 HOH   A O    1 
HETATM 6718 O O    . HOH   E 4 .   ? 24.002 -2.092  -2.111  1.00 11.49 ?  360 HOH   A O    1 
HETATM 6719 O O    . HOH   E 4 .   ? 21.238 -2.260  -2.384  1.00 16.60 ?  361 HOH   A O    1 
HETATM 6720 O O    . HOH   E 4 .   ? 30.748 3.077   8.290   1.00 12.32 ?  362 HOH   A O    1 
HETATM 6721 O O    . HOH   E 4 .   ? 21.838 -21.859 8.408   1.00 30.41 ?  363 HOH   A O    1 
HETATM 6722 O O    . HOH   E 4 .   ? 31.649 8.183   14.877  1.00 24.99 ?  364 HOH   A O    1 
HETATM 6723 O O    . HOH   E 4 .   ? 31.062 -13.917 -2.474  1.00 14.64 ?  365 HOH   A O    1 
HETATM 6724 O O    . HOH   E 4 .   ? 6.383  -5.549  11.038  1.00 19.37 ?  366 HOH   A O    1 
HETATM 6725 O O    . HOH   E 4 .   ? 33.602 -7.145  4.310   1.00 17.05 ?  367 HOH   A O    1 
HETATM 6726 O O    . HOH   E 4 .   ? 14.352 -21.222 -4.273  1.00 30.55 ?  368 HOH   A O    1 
HETATM 6727 O O    . HOH   E 4 .   ? 37.235 11.984  4.958   1.00 30.59 ?  369 HOH   A O    1 
HETATM 6728 O O    . HOH   E 4 .   ? 22.528 -11.879 21.808  1.00 50.07 ?  370 HOH   A O    1 
HETATM 6729 O O    . HOH   E 4 .   ? 43.896 8.465   -3.023  1.00 27.08 ?  371 HOH   A O    1 
HETATM 6730 O O    . HOH   E 4 .   ? 21.789 -13.735 -8.180  1.00 43.96 ?  372 HOH   A O    1 
HETATM 6731 O O    . HOH   E 4 .   ? 31.897 -9.309  -6.656  1.00 23.41 ?  373 HOH   A O    1 
HETATM 6732 O O    . HOH   E 4 .   ? 24.360 3.590   -1.797  1.00 15.92 ?  374 HOH   A O    1 
HETATM 6733 O O    . HOH   E 4 .   ? 16.995 -19.269 4.857   1.00 15.86 ?  375 HOH   A O    1 
HETATM 6734 O O    A HOH   E 4 .   ? -0.519 -3.069  3.062   0.60 28.59 ?  376 HOH   A O    1 
HETATM 6735 O O    T HOH   E 4 .   ? 15.367 -0.401  2.371   0.20 10.57 ?  377 HOH   A O    1 
HETATM 6736 O O    . HOH   E 4 .   ? 22.698 12.477  1.584   1.00 15.88 ?  378 HOH   A O    1 
HETATM 6737 O O    . HOH   E 4 .   ? 16.491 -22.020 0.924   1.00 30.62 ?  379 HOH   A O    1 
HETATM 6738 O O    . HOH   E 4 .   ? 14.021 -23.048 7.435   1.00 18.71 ?  380 HOH   A O    1 
HETATM 6739 O O    . HOH   E 4 .   ? 18.564 9.500   8.989   1.00 22.92 ?  381 HOH   A O    1 
HETATM 6740 O O    . HOH   E 4 .   ? 22.135 -19.280 11.399  1.00 34.96 ?  382 HOH   A O    1 
HETATM 6741 O O    . HOH   E 4 .   ? 13.234 -1.425  -6.749  1.00 19.06 ?  383 HOH   A O    1 
HETATM 6742 O O    A HOH   E 4 .   ? 17.458 -1.692  0.429   0.60 17.43 ?  384 HOH   A O    1 
HETATM 6743 O O    . HOH   E 4 .   ? 37.234 -2.910  9.668   1.00 43.24 ?  385 HOH   A O    1 
HETATM 6744 O O    . HOH   E 4 .   ? 31.799 -7.310  -9.819  1.00 21.82 ?  386 HOH   A O    1 
HETATM 6745 O O    . HOH   E 4 .   ? 43.291 7.845   2.727   1.00 29.38 ?  387 HOH   A O    1 
HETATM 6746 O O    A HOH   E 4 .   ? 7.959  -12.574 -0.912  0.60 17.97 ?  388 HOH   A O    1 
HETATM 6747 O O    . HOH   E 4 .   ? 24.580 2.005   -7.024  1.00 21.57 ?  389 HOH   A O    1 
HETATM 6748 O O    . HOH   E 4 .   ? 6.639  -3.300  12.770  1.00 30.17 ?  390 HOH   A O    1 
HETATM 6749 O O    . HOH   E 4 .   ? 24.172 -7.747  14.424  1.00 17.14 ?  391 HOH   A O    1 
HETATM 6750 O O    . HOH   E 4 .   ? 27.425 -10.621 14.098  1.00 18.33 ?  392 HOH   A O    1 
HETATM 6751 O O    B HOH   E 4 .   ? 22.608 5.685   -1.812  0.40 24.89 ?  393 HOH   A O    1 
HETATM 6752 O O    . HOH   E 4 .   ? 23.996 3.943   -4.795  1.00 24.93 ?  394 HOH   A O    1 
HETATM 6753 O O    . HOH   E 4 .   ? 33.454 -16.956 8.064   1.00 19.62 ?  395 HOH   A O    1 
HETATM 6754 O O    . HOH   E 4 .   ? 13.868 -4.977  17.395  1.00 27.44 ?  396 HOH   A O    1 
HETATM 6755 O O    . HOH   E 4 .   ? 30.606 1.890   16.705  1.00 21.30 ?  397 HOH   A O    1 
HETATM 6756 O O    . HOH   E 4 .   ? 32.736 -9.214  5.965   1.00 20.56 ?  398 HOH   A O    1 
HETATM 6757 O O    . HOH   E 4 .   ? 24.689 -17.523 12.686  1.00 24.01 ?  399 HOH   A O    1 
HETATM 6758 O O    . HOH   E 4 .   ? 10.912 1.650   12.522  1.00 23.46 ?  400 HOH   A O    1 
HETATM 6759 O O    . HOH   E 4 .   ? 20.088 4.535   -7.608  1.00 22.92 ?  401 HOH   A O    1 
HETATM 6760 O O    . HOH   E 4 .   ? 15.189 -21.527 14.208  1.00 18.84 ?  402 HOH   A O    1 
HETATM 6761 O O    . HOH   E 4 .   ? 15.447 11.817  7.923   1.00 42.19 ?  403 HOH   A O    1 
HETATM 6762 O O    . HOH   E 4 .   ? 37.495 -2.055  5.803   1.00 27.06 ?  404 HOH   A O    1 
HETATM 6763 O O    . HOH   E 4 .   ? 21.152 10.275  15.071  1.00 36.44 ?  405 HOH   A O    1 
HETATM 6764 O O    . HOH   E 4 .   ? 23.956 -15.661 -9.179  1.00 36.66 ?  406 HOH   A O    1 
HETATM 6765 O O    B HOH   E 4 .   ? 16.130 7.088   2.735   0.40 29.22 ?  407 HOH   A O    1 
HETATM 6766 O O    . HOH   E 4 .   ? 40.862 -8.279  -6.734  1.00 36.34 ?  408 HOH   A O    1 
HETATM 6767 O O    . HOH   E 4 .   ? 23.438 11.375  4.086   1.00 13.12 ?  409 HOH   A O    1 
HETATM 6768 O O    . HOH   E 4 .   ? 14.525 -0.517  -12.268 1.00 27.78 ?  410 HOH   A O    1 
HETATM 6769 O O    . HOH   E 4 .   ? 20.558 -19.998 2.726   1.00 18.50 ?  411 HOH   A O    1 
HETATM 6770 O O    . HOH   E 4 .   ? 27.576 -6.206  -14.060 1.00 39.98 ?  412 HOH   A O    1 
HETATM 6771 O O    . HOH   E 4 .   ? 30.279 -12.912 13.476  1.00 19.93 ?  413 HOH   A O    1 
HETATM 6772 O O    A HOH   E 4 .   ? 18.924 -0.647  -1.636  0.60 11.94 ?  414 HOH   A O    1 
HETATM 6773 O O    . HOH   E 4 .   ? 30.003 -10.082 13.019  1.00 22.76 ?  415 HOH   A O    1 
HETATM 6774 O O    . HOH   E 4 .   ? 27.213 2.310   18.722  1.00 30.03 ?  416 HOH   A O    1 
HETATM 6775 O O    B HOH   E 4 .   ? 14.886 -2.855  3.217   0.40 14.11 ?  417 HOH   A O    1 
HETATM 6776 O O    . HOH   E 4 .   ? 23.906 -20.250 -1.365  1.00 17.53 ?  418 HOH   A O    1 
HETATM 6777 O O    . HOH   E 4 .   ? -1.449 -5.022  7.422   1.00 42.21 ?  419 HOH   A O    1 
HETATM 6778 O O    A HOH   E 4 .   ? 15.756 -0.926  5.256   0.60 19.42 ?  420 HOH   A O    1 
HETATM 6779 O O    . HOH   E 4 .   ? 38.075 -1.325  -1.921  1.00 19.11 ?  421 HOH   A O    1 
HETATM 6780 O O    B HOH   E 4 .   ? 11.206 6.379   9.944   0.40 24.18 ?  422 HOH   A O    1 
HETATM 6781 O O    A HOH   E 4 .   ? 21.312 3.177   -0.354  0.60 11.29 ?  423 HOH   A O    1 
HETATM 6782 O O    . HOH   E 4 .   ? 32.687 -4.309  -9.864  1.00 29.53 ?  424 HOH   A O    1 
HETATM 6783 O O    B HOH   E 4 .   ? 16.566 3.406   -2.469  0.40 30.05 ?  425 HOH   A O    1 
HETATM 6784 O O    . HOH   E 4 .   ? 35.060 -5.211  -3.090  1.00 17.98 ?  426 HOH   A O    1 
HETATM 6785 O O    . HOH   E 4 .   ? 26.893 4.165   -0.677  1.00 13.19 ?  427 HOH   A O    1 
HETATM 6786 O O    . HOH   E 4 .   ? 15.141 -8.048  -9.842  1.00 23.76 ?  428 HOH   A O    1 
HETATM 6787 O O    B HOH   E 4 .   ? 11.323 -0.548  2.346   0.40 19.42 ?  429 HOH   A O    1 
HETATM 6788 O O    . HOH   E 4 .   ? 16.232 16.713  8.543   1.00 37.65 ?  430 HOH   A O    1 
HETATM 6789 O O    . HOH   E 4 .   ? 41.523 1.545   5.000   1.00 35.58 ?  431 HOH   A O    1 
HETATM 6790 O O    . HOH   E 4 .   ? 10.379 -13.704 -1.755  1.00 18.36 ?  432 HOH   A O    1 
HETATM 6791 O O    . HOH   E 4 .   ? 36.683 -4.930  5.414   1.00 25.45 ?  433 HOH   A O    1 
HETATM 6792 O O    . HOH   E 4 .   ? 11.617 -10.738 16.960  1.00 24.53 ?  434 HOH   A O    1 
HETATM 6793 O O    . HOH   E 4 .   ? 32.500 -10.611 3.223   1.00 31.86 ?  435 HOH   A O    1 
HETATM 6794 O O    . HOH   E 4 .   ? 5.345  2.831   4.910   1.00 35.47 ?  436 HOH   A O    1 
HETATM 6795 O O    B HOH   E 4 .   ? 12.162 -1.632  -2.889  0.40 19.52 ?  437 HOH   A O    1 
HETATM 6796 O O    . HOH   E 4 .   ? 44.915 -0.653  3.018   1.00 41.14 ?  438 HOH   A O    1 
HETATM 6797 O O    . HOH   E 4 .   ? 15.831 2.149   24.771  1.00 45.25 ?  439 HOH   A O    1 
HETATM 6798 O O    . HOH   E 4 .   ? 16.178 -14.143 20.163  1.00 52.58 ?  440 HOH   A O    1 
HETATM 6799 O O    . HOH   E 4 .   ? 28.657 -10.664 -13.976 1.00 42.33 ?  441 HOH   A O    1 
HETATM 6800 O O    . HOH   E 4 .   ? 22.557 8.144   18.354  1.00 46.76 ?  442 HOH   A O    1 
HETATM 6801 O O    A HOH   E 4 .   ? 18.558 -2.434  -16.350 0.60 31.14 ?  443 HOH   A O    1 
HETATM 6802 O O    A HOH   E 4 .   ? 18.419 4.871   -15.036 0.60 33.54 ?  444 HOH   A O    1 
HETATM 6803 O O    . HOH   E 4 .   ? 19.371 -11.018 24.049  1.00 68.97 ?  445 HOH   A O    1 
HETATM 6804 O O    A HOH   E 4 .   ? 15.977 6.975   2.979   0.60 13.10 ?  446 HOH   A O    1 
HETATM 6805 O O    . HOH   E 4 .   ? 18.380 -15.946 16.298  1.00 37.07 ?  447 HOH   A O    1 
HETATM 6806 O O    . HOH   E 4 .   ? 27.034 -3.256  19.386  1.00 37.20 ?  448 HOH   A O    1 
HETATM 6807 O O    A HOH   E 4 .   ? 18.827 2.055   -0.760  0.60 12.07 ?  449 HOH   A O    1 
HETATM 6808 O O    . HOH   E 4 .   ? 23.307 -20.910 1.303   1.00 18.76 ?  450 HOH   A O    1 
HETATM 6809 O O    . HOH   E 4 .   ? 23.493 -8.062  17.082  1.00 22.22 ?  451 HOH   A O    1 
HETATM 6810 O O    A HOH   E 4 .   ? 16.224 2.970   -1.453  0.60 13.61 ?  452 HOH   A O    1 
HETATM 6811 O O    . HOH   E 4 .   ? 37.710 -8.825  -3.443  1.00 25.44 ?  453 HOH   A O    1 
HETATM 6812 O O    . HOH   E 4 .   ? 29.821 -1.944  -12.733 1.00 46.11 ?  454 HOH   A O    1 
HETATM 6813 O O    . HOH   E 4 .   ? 20.507 -17.719 24.842  1.00 52.50 ?  455 HOH   A O    1 
HETATM 6814 O O    . HOH   E 4 .   ? 34.422 -8.039  -0.555  1.00 31.56 ?  456 HOH   A O    1 
HETATM 6815 O O    . HOH   E 4 .   ? 21.259 -9.189  21.276  1.00 53.75 ?  457 HOH   A O    1 
HETATM 6816 O O    A HOH   E 4 .   ? 13.986 -0.318  3.445   0.40 28.69 ?  458 HOH   A O    1 
HETATM 6817 O O    . HOH   E 4 .   ? 30.550 14.770  2.776   1.00 19.63 ?  459 HOH   A O    1 
HETATM 6818 O O    . HOH   E 4 .   ? 31.298 -12.766 0.006   1.00 20.36 ?  460 HOH   A O    1 
HETATM 6819 O O    . HOH   E 4 .   ? 21.418 -14.740 17.907  1.00 51.54 ?  461 HOH   A O    1 
HETATM 6820 O O    . HOH   E 4 .   ? 23.197 7.533   -3.285  1.00 31.74 ?  462 HOH   A O    1 
HETATM 6821 O O    . HOH   E 4 .   ? 29.733 -15.997 10.692  1.00 38.56 ?  463 HOH   A O    1 
HETATM 6822 O O    B HOH   E 4 .   ? 7.490  3.697   4.121   0.40 25.41 ?  464 HOH   A O    1 
HETATM 6823 O O    B HOH   E 4 .   ? 18.423 2.116   -0.876  0.40 18.24 ?  465 HOH   A O    1 
HETATM 6824 O O    . HOH   E 4 .   ? 27.829 7.113   -6.453  1.00 38.48 ?  466 HOH   A O    1 
HETATM 6825 O O    . HOH   E 4 .   ? 32.430 -15.846 10.849  1.00 34.57 ?  467 HOH   A O    1 
HETATM 6826 O O    . HOH   E 4 .   ? 25.359 8.225   -4.798  1.00 33.38 ?  468 HOH   A O    1 
HETATM 6827 O O    B HOH   E 4 .   ? 16.781 6.067   -2.833  0.40 38.65 ?  469 HOH   A O    1 
HETATM 6828 O O    . HOH   E 4 .   ? 24.804 5.607   20.711  1.00 54.64 ?  470 HOH   A O    1 
HETATM 6829 O O    . HOH   E 4 .   ? 19.868 -17.323 -5.118  1.00 25.72 ?  471 HOH   A O    1 
HETATM 6830 O O    . HOH   E 4 .   ? 24.587 14.582  7.813   1.00 36.22 ?  472 HOH   A O    1 
HETATM 6831 O O    . HOH   E 4 .   ? 23.132 -22.361 -3.347  1.00 35.69 ?  473 HOH   A O    1 
HETATM 6832 O O    . HOH   E 4 .   ? 22.000 5.197   -6.049  1.00 33.73 ?  474 HOH   A O    1 
HETATM 6833 O O    B HOH   E 4 .   ? 13.790 -3.108  -1.020  0.40 29.35 ?  475 HOH   A O    1 
HETATM 6834 O O    . HOH   E 4 .   ? 18.772 10.836  11.338  1.00 32.77 ?  476 HOH   A O    1 
HETATM 6835 O O    . HOH   E 4 .   ? 23.450 13.703  5.485   1.00 18.95 ?  477 HOH   A O    1 
HETATM 6836 O O    . HOH   E 4 .   ? 39.610 -7.024  -3.474  1.00 44.70 ?  478 HOH   A O    1 
HETATM 6837 O O    . HOH   E 4 .   ? 15.762 -21.550 3.698   1.00 24.36 ?  479 HOH   A O    1 
HETATM 6838 O O    . HOH   E 4 .   ? 11.903 -13.409 16.218  1.00 52.08 ?  480 HOH   A O    1 
HETATM 6839 O O    . HOH   E 4 .   ? 26.901 11.609  -1.386  1.00 30.83 ?  481 HOH   A O    1 
HETATM 6840 O O    . HOH   E 4 .   ? 27.361 -11.398 16.587  1.00 38.43 ?  482 HOH   A O    1 
HETATM 6841 O O    . HOH   E 4 .   ? 12.278 1.525   17.329  1.00 40.53 ?  483 HOH   A O    1 
HETATM 6842 O O    . HOH   E 4 .   ? 11.077 -15.023 -6.143  1.00 35.68 ?  484 HOH   A O    1 
HETATM 6843 O O    . HOH   E 4 .   ? 18.107 -16.210 -8.883  1.00 43.50 ?  485 HOH   A O    1 
HETATM 6844 O O    . HOH   E 4 .   ? 25.817 10.762  -3.774  1.00 25.66 ?  486 HOH   A O    1 
HETATM 6845 O O    . HOH   E 4 .   ? 28.646 -4.714  -12.265 1.00 41.31 ?  487 HOH   A O    1 
HETATM 6846 O O    B HOH   E 4 .   ? 16.767 10.323  6.075   0.40 18.77 ?  488 HOH   A O    1 
HETATM 6847 O O    . HOH   E 4 .   ? 13.956 -10.354 -10.947 1.00 33.67 ?  489 HOH   A O    1 
HETATM 6848 O O    . HOH   E 4 .   ? 35.132 7.420   12.258  1.00 43.09 ?  490 HOH   A O    1 
HETATM 6849 O O    . HOH   E 4 .   ? 15.741 -17.134 -7.025  1.00 32.38 ?  491 HOH   A O    1 
HETATM 6850 O O    . HOH   E 4 .   ? 16.848 -20.515 16.115  1.00 29.69 ?  492 HOH   A O    1 
HETATM 6851 O O    . HOH   E 4 .   ? 20.544 -16.071 -7.411  1.00 29.61 ?  493 HOH   A O    1 
HETATM 6852 O O    B HOH   E 4 .   ? 10.823 -1.525  -5.443  0.40 20.07 ?  494 HOH   A O    1 
HETATM 6853 O O    . HOH   E 4 .   ? 28.707 9.095   17.540  1.00 37.07 ?  495 HOH   A O    1 
HETATM 6854 O O    . HOH   E 4 .   ? 17.344 -18.653 19.779  1.00 53.76 ?  496 HOH   A O    1 
HETATM 6855 O O    . HOH   E 4 .   ? 28.673 -8.016  -15.288 1.00 49.51 ?  497 HOH   A O    1 
HETATM 6856 O O    . HOH   E 4 .   ? 40.967 -3.995  -0.329  1.00 37.95 ?  498 HOH   A O    1 
HETATM 6857 O O    . HOH   E 4 .   ? 30.808 0.705   19.155  1.00 40.96 ?  499 HOH   A O    1 
HETATM 6858 O O    . HOH   E 4 .   ? 23.130 11.819  -4.086  1.00 20.45 ?  500 HOH   A O    1 
HETATM 6859 O O    . HOH   E 4 .   ? 31.478 -0.611  -10.511 1.00 28.38 ?  501 HOH   A O    1 
HETATM 6860 O O    . HOH   E 4 .   ? 44.473 10.461  -1.549  1.00 33.06 ?  502 HOH   A O    1 
HETATM 6861 O O    . HOH   E 4 .   ? 41.661 9.298   -4.068  1.00 31.94 ?  503 HOH   A O    1 
HETATM 6862 O O    . HOH   E 4 .   ? 23.224 -12.875 19.340  1.00 42.83 ?  504 HOH   A O    1 
HETATM 6863 O O    . HOH   E 4 .   ? 39.111 2.415   7.483   1.00 32.61 ?  505 HOH   A O    1 
HETATM 6864 O O    . HOH   E 4 .   ? 13.938 -25.251 8.895   1.00 33.21 ?  506 HOH   A O    1 
HETATM 6865 O O    . HOH   E 4 .   ? 16.059 -6.776  -11.937 1.00 43.02 ?  507 HOH   A O    1 
HETATM 6866 O O    . HOH   E 4 .   ? 16.157 -23.377 5.740   1.00 30.21 ?  508 HOH   A O    1 
HETATM 6867 O O    . HOH   E 4 .   ? 18.355 -23.197 1.865   1.00 44.81 ?  509 HOH   A O    1 
HETATM 6868 O O    . HOH   E 4 .   ? 40.532 -0.247  -7.754  1.00 34.43 ?  510 HOH   A O    1 
HETATM 6869 O O    . HOH   E 4 .   ? 20.031 -22.300 4.119   1.00 29.22 ?  511 HOH   A O    1 
HETATM 6870 O O    B HOH   E 4 .   ? 7.489  5.651   5.547   0.40 35.61 ?  512 HOH   A O    1 
HETATM 6871 O O    . HOH   E 4 .   ? 30.630 5.837   -14.724 1.00 37.24 ?  513 HOH   A O    1 
HETATM 6872 O O    B HOH   E 4 .   ? 12.784 -3.130  1.524   0.40 16.47 ?  514 HOH   A O    1 
HETATM 6873 O O    . HOH   E 4 .   ? 8.161  -3.107  -5.790  1.00 46.68 ?  515 HOH   A O    1 
HETATM 6874 O O    . HOH   E 4 .   ? 23.172 -23.770 1.634   1.00 30.59 ?  516 HOH   A O    1 
HETATM 6875 O O    . HOH   E 4 .   ? 37.356 -6.616  7.572   1.00 27.62 ?  517 HOH   A O    1 
HETATM 6876 O O    . HOH   E 4 .   ? 30.724 -5.774  -11.903 1.00 49.16 ?  518 HOH   A O    1 
HETATM 6877 O O    . HOH   E 4 .   ? 39.496 -0.004  6.659   1.00 30.75 ?  519 HOH   A O    1 
HETATM 6878 O O    B HOH   E 4 .   ? 14.803 7.960   4.968   0.40 20.19 ?  520 HOH   A O    1 
HETATM 6879 O O    . HOH   E 4 .   ? 37.953 13.895  6.814   1.00 49.01 ?  521 HOH   A O    1 
HETATM 6880 O O    . HOH   E 4 .   ? 28.946 14.413  0.869   1.00 47.39 ?  522 HOH   A O    1 
HETATM 6881 O O    B HOH   E 4 .   ? 10.845 -0.151  -1.110  0.40 26.00 ?  523 HOH   A O    1 
HETATM 6882 O O    . HOH   E 4 .   ? 22.001 -23.991 4.503   1.00 28.39 ?  524 HOH   A O    1 
HETATM 6883 O O    . HOH   E 4 .   ? 36.436 -6.489  10.185  1.00 44.84 ?  525 HOH   A O    1 
HETATM 6884 O O    B HOH   E 4 .   ? 8.514  7.078   1.866   0.40 32.86 ?  526 HOH   A O    1 
HETATM 6885 O O    B HOH   E 4 .   ? 9.958  1.068   -5.598  0.40 23.42 ?  527 HOH   A O    1 
HETATM 6886 O O    A HOH   E 4 .   ? 17.466 -6.491  -14.194 0.60 30.61 ?  528 HOH   A O    1 
HETATM 6887 O O    T HOH   E 4 .   ? 11.890 -2.125  -3.675  0.20 10.91 ?  529 HOH   A O    1 
HETATM 6888 O O    A HOH   E 4 .   ? 14.807 8.670   4.877   0.60 42.43 ?  530 HOH   A O    1 
HETATM 6889 O O    . HOH   E 4 .   ? 24.063 8.931   -7.194  1.00 38.39 ?  531 HOH   A O    1 
HETATM 6890 O O    . HOH   E 4 .   ? 16.315 -21.157 18.724  1.00 42.27 ?  532 HOH   A O    1 
HETATM 6891 O O    . HOH   E 4 .   ? 15.851 -12.219 27.409  1.00 42.89 ?  533 HOH   A O    1 
HETATM 6892 O O    . HOH   E 4 .   ? 14.676 -22.689 19.875  1.00 38.15 ?  534 HOH   A O    1 
HETATM 6893 O O    . HOH   F 4 .   ? 29.806 -22.397 5.439   1.00 21.39 ?  201 HOH   B O    1 
HETATM 6894 O O    . HOH   F 4 .   ? 41.810 -35.957 -17.143 1.00 30.43 ?  202 HOH   B O    1 
HETATM 6895 O O    . HOH   F 4 .   ? 48.065 -6.865  15.557  1.00 32.75 ?  203 HOH   B O    1 
HETATM 6896 O O    . HOH   F 4 .   ? 52.899 -13.454 -20.402 1.00 37.31 ?  204 HOH   B O    1 
HETATM 6897 O O    . HOH   F 4 .   ? 49.356 -22.630 -19.761 1.00 50.97 ?  205 HOH   B O    1 
HETATM 6898 O O    . HOH   F 4 .   ? 27.675 -29.156 -1.869  1.00 34.94 ?  206 HOH   B O    1 
HETATM 6899 O O    . HOH   F 4 .   ? 59.114 -18.656 6.862   1.00 36.94 ?  207 HOH   B O    1 
HETATM 6900 O O    . HOH   F 4 .   ? 50.202 -3.313  7.246   1.00 36.21 ?  208 HOH   B O    1 
HETATM 6901 O O    . HOH   F 4 .   ? 37.897 -39.417 -0.186  1.00 38.85 ?  209 HOH   B O    1 
HETATM 6902 O O    . HOH   F 4 .   ? 47.405 -7.412  -3.906  1.00 38.64 ?  210 HOH   B O    1 
HETATM 6903 O O    . HOH   F 4 .   ? 41.315 -7.801  5.436   1.00 40.90 ?  211 HOH   B O    1 
HETATM 6904 O O    . HOH   F 4 .   ? 58.155 -12.932 8.449   1.00 31.89 ?  212 HOH   B O    1 
HETATM 6905 O O    . HOH   F 4 .   ? 54.456 -9.372  -8.751  1.00 19.84 ?  213 HOH   B O    1 
HETATM 6906 O O    . HOH   F 4 .   ? 56.304 -19.682 7.394   1.00 34.63 ?  214 HOH   B O    1 
HETATM 6907 O O    . HOH   F 4 .   ? 27.809 -41.800 -15.137 1.00 35.23 ?  215 HOH   B O    1 
HETATM 6908 O O    . HOH   F 4 .   ? 29.866 -26.272 4.008   1.00 30.00 ?  216 HOH   B O    1 
HETATM 6909 O O    . HOH   F 4 .   ? 57.672 -24.481 5.049   1.00 35.29 ?  217 HOH   B O    1 
HETATM 6910 O O    . HOH   F 4 .   ? 30.186 -40.982 -8.101  1.00 17.36 ?  218 HOH   B O    1 
HETATM 6911 O O    . HOH   F 4 .   ? 37.151 -19.783 -18.113 1.00 38.42 ?  219 HOH   B O    1 
HETATM 6912 O O    . HOH   F 4 .   ? 57.122 -26.875 -7.603  1.00 41.56 ?  220 HOH   B O    1 
HETATM 6913 O O    . HOH   F 4 .   ? 56.623 -30.756 -7.715  1.00 32.44 ?  221 HOH   B O    1 
HETATM 6914 O O    . HOH   F 4 .   ? 35.923 -43.206 -8.507  1.00 33.08 ?  222 HOH   B O    1 
HETATM 6915 O O    . HOH   F 4 .   ? 30.857 -28.718 4.325   1.00 27.24 ?  223 HOH   B O    1 
HETATM 6916 O O    . HOH   F 4 .   ? 48.091 -24.574 -17.651 1.00 30.44 ?  224 HOH   B O    1 
HETATM 6917 O O    . HOH   F 4 .   ? 34.511 -36.340 -7.175  1.00 18.10 ?  225 HOH   B O    1 
HETATM 6918 O O    . HOH   F 4 .   ? 50.696 -6.088  0.216   1.00 26.12 ?  226 HOH   B O    1 
HETATM 6919 O O    . HOH   F 4 .   ? 57.377 -16.253 -12.182 1.00 19.40 ?  227 HOH   B O    1 
HETATM 6920 O O    . HOH   F 4 .   ? 44.424 -7.214  2.136   1.00 34.09 ?  228 HOH   B O    1 
HETATM 6921 O O    . HOH   F 4 .   ? 41.476 -39.143 -14.862 1.00 22.88 ?  229 HOH   B O    1 
HETATM 6922 O O    . HOH   F 4 .   ? 29.754 -34.156 -0.406  1.00 35.99 ?  230 HOH   B O    1 
HETATM 6923 O O    . HOH   F 4 .   ? 44.881 -43.543 -10.502 1.00 28.36 ?  231 HOH   B O    1 
HETATM 6924 O O    . HOH   F 4 .   ? 55.405 -16.498 -14.284 1.00 36.44 ?  232 HOH   B O    1 
HETATM 6925 O O    . HOH   F 4 .   ? 51.646 -6.484  4.413   1.00 20.93 ?  233 HOH   B O    1 
HETATM 6926 O O    . HOH   F 4 .   ? 39.261 -10.905 6.141   1.00 26.28 ?  234 HOH   B O    1 
HETATM 6927 O O    . HOH   F 4 .   ? 50.708 -12.965 -0.463  1.00 12.43 ?  235 HOH   B O    1 
HETATM 6928 O O    . HOH   F 4 .   ? 46.353 -1.579  13.260  1.00 28.36 ?  236 HOH   B O    1 
HETATM 6929 O O    . HOH   F 4 .   ? 35.099 -7.991  -3.003  1.00 18.91 ?  237 HOH   B O    1 
HETATM 6930 O O    . HOH   F 4 .   ? 25.362 -25.909 -1.331  1.00 33.34 ?  238 HOH   B O    1 
HETATM 6931 O O    . HOH   F 4 .   ? 44.476 -27.759 -0.695  1.00 23.33 ?  239 HOH   B O    1 
HETATM 6932 O O    . HOH   F 4 .   ? 42.595 -22.843 3.861   1.00 12.38 ?  240 HOH   B O    1 
HETATM 6933 O O    . HOH   F 4 .   ? 57.566 -24.360 -3.790  1.00 22.60 ?  241 HOH   B O    1 
HETATM 6934 O O    . HOH   F 4 .   ? 28.390 -19.702 -13.094 1.00 25.12 ?  242 HOH   B O    1 
HETATM 6935 O O    . HOH   F 4 .   ? 45.099 -34.880 6.784   1.00 42.62 ?  243 HOH   B O    1 
HETATM 6936 O O    . HOH   F 4 .   ? 34.191 -18.441 11.396  1.00 24.60 ?  244 HOH   B O    1 
HETATM 6937 O O    . HOH   F 4 .   ? 51.494 -13.831 10.991  1.00 28.12 ?  245 HOH   B O    1 
HETATM 6938 O O    . HOH   F 4 .   ? 42.523 -25.334 2.639   1.00 16.05 ?  246 HOH   B O    1 
HETATM 6939 O O    . HOH   F 4 .   ? 41.350 -9.601  13.101  1.00 23.10 ?  247 HOH   B O    1 
HETATM 6940 O O    . HOH   F 4 .   ? 32.775 -43.781 -11.279 1.00 20.36 ?  248 HOH   B O    1 
HETATM 6941 O O    . HOH   F 4 .   ? 39.460 -11.093 0.343   1.00 17.59 ?  249 HOH   B O    1 
HETATM 6942 O O    . HOH   F 4 .   ? 43.037 -43.209 -8.196  1.00 30.43 ?  250 HOH   B O    1 
HETATM 6943 O O    . HOH   F 4 .   ? 50.918 -39.945 -8.111  1.00 35.19 ?  251 HOH   B O    1 
HETATM 6944 O O    . HOH   F 4 .   ? 38.469 -11.042 -2.255  1.00 19.64 ?  252 HOH   B O    1 
HETATM 6945 O O    . HOH   F 4 .   ? 34.857 -24.586 13.868  1.00 33.16 ?  253 HOH   B O    1 
HETATM 6946 O O    . HOH   F 4 .   ? 27.123 -31.806 -9.945  1.00 21.48 ?  254 HOH   B O    1 
HETATM 6947 O O    . HOH   F 4 .   ? 40.623 -16.005 14.177  1.00 25.86 ?  255 HOH   B O    1 
HETATM 6948 O O    . HOH   F 4 .   ? 43.175 -32.369 -17.022 1.00 24.04 ?  256 HOH   B O    1 
HETATM 6949 O O    . HOH   F 4 .   ? 31.800 -17.923 -14.486 1.00 30.05 ?  257 HOH   B O    1 
HETATM 6950 O O    . HOH   F 4 .   ? 40.314 -12.746 -11.498 1.00 15.86 ?  258 HOH   B O    1 
HETATM 6951 O O    . HOH   F 4 .   ? 41.818 -23.504 9.301   1.00 17.94 ?  259 HOH   B O    1 
HETATM 6952 O O    . HOH   F 4 .   ? 48.506 -36.454 -15.493 1.00 43.73 ?  260 HOH   B O    1 
HETATM 6953 O O    . HOH   F 4 .   ? 42.309 -9.906  9.418   1.00 21.29 ?  261 HOH   B O    1 
HETATM 6954 O O    . HOH   F 4 .   ? 29.715 -25.208 -10.805 1.00 17.47 ?  262 HOH   B O    1 
HETATM 6955 O O    . HOH   F 4 .   ? 30.831 -15.704 2.662   1.00 14.33 ?  263 HOH   B O    1 
HETATM 6956 O O    . HOH   F 4 .   ? 58.143 -10.615 -4.060  1.00 20.71 ?  264 HOH   B O    1 
HETATM 6957 O O    . HOH   F 4 .   ? 49.706 -0.498  10.262  1.00 30.95 ?  265 HOH   B O    1 
HETATM 6958 O O    . HOH   F 4 .   ? 34.460 -12.778 2.590   1.00 24.60 ?  266 HOH   B O    1 
HETATM 6959 O O    . HOH   F 4 .   ? 57.465 -9.215  1.455   1.00 20.66 ?  267 HOH   B O    1 
HETATM 6960 O O    . HOH   F 4 .   ? 47.954 -22.745 5.863   1.00 17.76 ?  268 HOH   B O    1 
HETATM 6961 O O    . HOH   F 4 .   ? 42.315 -34.668 3.792   1.00 26.05 ?  269 HOH   B O    1 
HETATM 6962 O O    . HOH   F 4 .   ? 28.235 -34.334 -9.433  1.00 20.03 ?  270 HOH   B O    1 
HETATM 6963 O O    . HOH   F 4 .   ? 46.810 -29.536 9.827   1.00 32.46 ?  271 HOH   B O    1 
HETATM 6964 O O    . HOH   F 4 .   ? 46.576 -31.237 -4.762  1.00 22.28 ?  272 HOH   B O    1 
HETATM 6965 O O    . HOH   F 4 .   ? 34.929 -33.371 -19.124 1.00 31.91 ?  273 HOH   B O    1 
HETATM 6966 O O    . HOH   F 4 .   ? 30.546 -42.198 -10.603 1.00 29.31 ?  274 HOH   B O    1 
HETATM 6967 O O    . HOH   F 4 .   ? 56.144 -23.538 -14.679 1.00 26.57 ?  275 HOH   B O    1 
HETATM 6968 O O    . HOH   F 4 .   ? 56.888 -8.627  8.457   1.00 19.28 ?  276 HOH   B O    1 
HETATM 6969 O O    . HOH   F 4 .   ? 49.268 -28.674 -6.841  1.00 16.11 ?  277 HOH   B O    1 
HETATM 6970 O O    . HOH   F 4 .   ? 38.863 -11.949 12.458  1.00 36.23 ?  278 HOH   B O    1 
HETATM 6971 O O    . HOH   F 4 .   ? 28.466 -30.909 -14.667 1.00 32.26 ?  279 HOH   B O    1 
HETATM 6972 O O    . HOH   F 4 .   ? 43.360 -15.792 -12.165 1.00 15.01 ?  280 HOH   B O    1 
HETATM 6973 O O    . HOH   F 4 .   ? 49.998 -24.586 5.792   1.00 33.81 ?  281 HOH   B O    1 
HETATM 6974 O O    . HOH   F 4 .   ? 27.937 -22.865 -8.016  1.00 18.50 ?  282 HOH   B O    1 
HETATM 6975 O O    . HOH   F 4 .   ? 48.370 -25.023 3.118   1.00 14.23 ?  283 HOH   B O    1 
HETATM 6976 O O    . HOH   F 4 .   ? 52.468 -10.386 13.012  1.00 21.99 ?  284 HOH   B O    1 
HETATM 6977 O O    . HOH   F 4 .   ? 27.584 -26.696 -15.653 1.00 31.85 ?  285 HOH   B O    1 
HETATM 6978 O O    . HOH   F 4 .   ? 47.037 -33.955 -4.591  1.00 18.04 ?  286 HOH   B O    1 
HETATM 6979 O O    . HOH   F 4 .   ? 48.668 -20.005 5.950   1.00 14.52 ?  287 HOH   B O    1 
HETATM 6980 O O    . HOH   F 4 .   ? 42.261 -10.009 -14.888 1.00 40.98 ?  288 HOH   B O    1 
HETATM 6981 O O    . HOH   F 4 .   ? 51.186 -37.587 -9.513  1.00 27.43 ?  289 HOH   B O    1 
HETATM 6982 O O    . HOH   F 4 .   ? 41.089 -5.486  11.605  1.00 46.09 ?  290 HOH   B O    1 
HETATM 6983 O O    . HOH   F 4 .   ? 33.508 -15.306 -13.970 1.00 21.43 ?  291 HOH   B O    1 
HETATM 6984 O O    . HOH   F 4 .   ? 52.538 -35.640 -8.562  1.00 28.99 ?  292 HOH   B O    1 
HETATM 6985 O O    . HOH   F 4 .   ? 36.775 -12.742 -1.484  1.00 26.18 ?  293 HOH   B O    1 
HETATM 6986 O O    . HOH   F 4 .   ? 51.644 -6.003  -7.947  1.00 46.11 ?  294 HOH   B O    1 
HETATM 6987 O O    . HOH   F 4 .   ? 59.720 -15.205 8.198   1.00 30.76 ?  295 HOH   B O    1 
HETATM 6988 O O    . HOH   F 4 .   ? 45.867 -40.376 -3.546  1.00 29.91 ?  296 HOH   B O    1 
HETATM 6989 O O    . HOH   F 4 .   ? 42.681 -12.278 -18.494 1.00 29.05 ?  297 HOH   B O    1 
HETATM 6990 O O    . HOH   F 4 .   ? 37.517 -18.095 13.118  1.00 30.33 ?  298 HOH   B O    1 
HETATM 6991 O O    . HOH   F 4 .   ? 45.362 -33.386 -15.905 1.00 24.33 ?  299 HOH   B O    1 
HETATM 6992 O O    . HOH   F 4 .   ? 44.583 -27.436 2.015   1.00 16.24 ?  300 HOH   B O    1 
HETATM 6993 O O    . HOH   F 4 .   ? 57.060 -12.066 12.429  1.00 38.53 ?  301 HOH   B O    1 
HETATM 6994 O O    . HOH   F 4 .   ? 35.010 -33.500 4.548   1.00 30.00 ?  302 HOH   B O    1 
HETATM 6995 O O    . HOH   F 4 .   ? 44.012 -29.321 -4.638  1.00 23.57 ?  303 HOH   B O    1 
HETATM 6996 O O    . HOH   F 4 .   ? 40.244 -10.831 -9.534  1.00 17.71 ?  304 HOH   B O    1 
HETATM 6997 O O    . HOH   F 4 .   ? 53.071 -16.056 -12.701 1.00 28.11 ?  305 HOH   B O    1 
HETATM 6998 O O    . HOH   F 4 .   ? 53.428 -30.170 4.532   1.00 19.47 ?  306 HOH   B O    1 
HETATM 6999 O O    . HOH   F 4 .   ? 43.498 -15.409 18.210  1.00 32.66 ?  307 HOH   B O    1 
HETATM 7000 O O    . HOH   F 4 .   ? 37.839 -10.257 -10.766 1.00 17.74 ?  308 HOH   B O    1 
HETATM 7001 O O    . HOH   F 4 .   ? 25.934 -21.448 -3.542  1.00 17.48 ?  309 HOH   B O    1 
HETATM 7002 O O    . HOH   F 4 .   ? 37.249 -35.643 7.209   1.00 34.59 ?  310 HOH   B O    1 
HETATM 7003 O O    . HOH   F 4 .   ? 32.772 -34.572 -5.874  1.00 17.53 ?  311 HOH   B O    1 
HETATM 7004 O O    . HOH   F 4 .   ? 53.612 -12.522 -22.256 1.00 35.78 ?  312 HOH   B O    1 
HETATM 7005 O O    . HOH   F 4 .   ? 52.510 -29.236 -12.995 1.00 25.99 ?  313 HOH   B O    1 
HETATM 7006 O O    . HOH   F 4 .   ? 42.872 -20.245 -20.794 1.00 37.50 ?  314 HOH   B O    1 
HETATM 7007 O O    . HOH   F 4 .   ? 62.657 -13.558 4.759   1.00 28.02 ?  315 HOH   B O    1 
HETATM 7008 O O    . HOH   F 4 .   ? 41.725 -8.060  1.386   1.00 25.51 ?  316 HOH   B O    1 
HETATM 7009 O O    . HOH   F 4 .   ? 62.801 -20.246 -0.772  1.00 36.70 ?  317 HOH   B O    1 
HETATM 7010 O O    . HOH   F 4 .   ? 51.359 -32.925 -10.688 1.00 38.80 ?  318 HOH   B O    1 
HETATM 7011 O O    . HOH   F 4 .   ? 41.206 -24.482 15.772  1.00 44.85 ?  319 HOH   B O    1 
HETATM 7012 O O    . HOH   F 4 .   ? 43.156 -21.399 10.688  1.00 16.82 ?  320 HOH   B O    1 
HETATM 7013 O O    . HOH   F 4 .   ? 37.093 -30.565 -20.987 1.00 32.67 ?  321 HOH   B O    1 
HETATM 7014 O O    . HOH   F 4 .   ? 38.346 -9.402  -13.270 1.00 27.48 ?  322 HOH   B O    1 
HETATM 7015 O O    . HOH   F 4 .   ? 38.305 -12.715 7.941   1.00 18.77 ?  323 HOH   B O    1 
HETATM 7016 O O    . HOH   F 4 .   ? 26.328 -21.009 -6.229  1.00 17.59 ?  324 HOH   B O    1 
HETATM 7017 O O    . HOH   F 4 .   ? 57.590 -22.055 3.229   1.00 29.14 ?  325 HOH   B O    1 
HETATM 7018 O O    . HOH   F 4 .   ? 44.526 -24.584 9.610   1.00 20.78 ?  326 HOH   B O    1 
HETATM 7019 O O    . HOH   F 4 .   ? 44.103 -1.745  7.674   1.00 46.80 ?  327 HOH   B O    1 
HETATM 7020 O O    . HOH   F 4 .   ? 48.037 -32.683 -16.559 1.00 44.95 ?  328 HOH   B O    1 
HETATM 7021 O O    . HOH   F 4 .   ? 36.691 -12.391 4.307   1.00 18.25 ?  329 HOH   B O    1 
HETATM 7022 O O    . HOH   F 4 .   ? 27.923 -14.752 -9.412  1.00 35.27 ?  330 HOH   B O    1 
HETATM 7023 O O    . HOH   F 4 .   ? 47.092 -24.442 8.212   1.00 28.42 ?  331 HOH   B O    1 
HETATM 7024 O O    . HOH   F 4 .   ? 48.596 -11.964 -14.045 1.00 26.75 ?  332 HOH   B O    1 
HETATM 7025 O O    . HOH   F 4 .   ? 59.928 -17.146 -10.505 1.00 33.67 ?  333 HOH   B O    1 
HETATM 7026 O O    . HOH   F 4 .   ? 33.571 -31.175 11.037  1.00 34.05 ?  334 HOH   B O    1 
HETATM 7027 O O    . HOH   F 4 .   ? 43.063 -34.637 0.135   1.00 20.23 ?  335 HOH   B O    1 
HETATM 7028 O O    . HOH   F 4 .   ? 47.434 -27.416 2.033   1.00 15.78 ?  336 HOH   B O    1 
HETATM 7029 O O    . HOH   F 4 .   ? 45.708 -36.219 -16.061 1.00 34.39 ?  337 HOH   B O    1 
HETATM 7030 O O    . HOH   F 4 .   ? 42.819 -43.482 -14.322 1.00 43.75 ?  338 HOH   B O    1 
HETATM 7031 O O    . HOH   F 4 .   ? 46.797 -19.863 12.265  1.00 31.02 ?  339 HOH   B O    1 
HETATM 7032 O O    . HOH   F 4 .   ? 37.006 -15.124 -16.491 1.00 40.94 ?  340 HOH   B O    1 
HETATM 7033 O O    . HOH   F 4 .   ? 39.447 -23.493 -20.367 1.00 36.33 ?  341 HOH   B O    1 
HETATM 7034 O O    . HOH   F 4 .   ? 28.860 -42.889 -12.355 1.00 39.09 ?  342 HOH   B O    1 
HETATM 7035 O O    . HOH   F 4 .   ? 37.055 -45.196 -9.751  1.00 37.39 ?  343 HOH   B O    1 
HETATM 7036 O O    . HOH   F 4 .   ? 32.979 -14.663 1.056   1.00 20.75 ?  344 HOH   B O    1 
HETATM 7037 O O    . HOH   F 4 .   ? 38.422 -12.283 -16.245 1.00 44.89 ?  345 HOH   B O    1 
HETATM 7038 O O    . HOH   F 4 .   ? 34.500 -10.316 7.672   1.00 23.23 ?  346 HOH   B O    1 
HETATM 7039 O O    . HOH   F 4 .   ? 39.780 -44.297 -11.194 1.00 40.86 ?  347 HOH   B O    1 
HETATM 7040 O O    . HOH   F 4 .   ? 38.525 -22.317 15.033  1.00 40.30 ?  348 HOH   B O    1 
HETATM 7041 O O    . HOH   F 4 .   ? 40.374 -43.443 -9.118  1.00 26.31 ?  349 HOH   B O    1 
HETATM 7042 O O    . HOH   F 4 .   ? 62.581 -20.113 -4.708  1.00 46.56 ?  350 HOH   B O    1 
HETATM 7043 O O    . HOH   F 4 .   ? 33.796 -9.178  -8.805  1.00 34.18 ?  351 HOH   B O    1 
HETATM 7044 O O    . HOH   F 4 .   ? 27.751 -26.595 -0.576  1.00 30.34 ?  352 HOH   B O    1 
HETATM 7045 O O    . HOH   F 4 .   ? 55.621 -8.258  10.835  1.00 26.41 ?  353 HOH   B O    1 
HETATM 7046 O O    . HOH   F 4 .   ? 23.190 -23.644 6.802   1.00 36.76 ?  354 HOH   B O    1 
HETATM 7047 O O    . HOH   F 4 .   ? 44.152 -37.338 -17.724 1.00 33.29 ?  355 HOH   B O    1 
HETATM 7048 O O    . HOH   F 4 .   ? 36.127 -8.547  -9.677  1.00 32.54 ?  356 HOH   B O    1 
HETATM 7049 O O    . HOH   F 4 .   ? 56.537 -7.286  3.123   1.00 27.79 ?  357 HOH   B O    1 
HETATM 7050 O O    . HOH   F 4 .   ? 34.033 -7.767  11.462  1.00 39.91 ?  358 HOH   B O    1 
HETATM 7051 O O    . HOH   F 4 .   ? 43.099 -12.700 -21.242 1.00 40.89 ?  359 HOH   B O    1 
HETATM 7052 O O    . HOH   F 4 .   ? 56.852 -21.560 -16.348 1.00 40.40 ?  360 HOH   B O    1 
HETATM 7053 O O    . HOH   F 4 .   ? 61.458 -19.943 1.756   1.00 36.36 ?  361 HOH   B O    1 
HETATM 7054 O O    . HOH   F 4 .   ? 40.226 -8.806  9.903   1.00 39.52 ?  362 HOH   B O    1 
HETATM 7055 O O    . HOH   F 4 .   ? 27.125 -25.940 -11.422 1.00 34.30 ?  363 HOH   B O    1 
HETATM 7056 O O    . HOH   F 4 .   ? 32.484 -23.646 14.092  1.00 39.42 ?  364 HOH   B O    1 
HETATM 7057 O O    . HOH   F 4 .   ? 54.194 -5.747  2.971   1.00 35.31 ?  365 HOH   B O    1 
HETATM 7058 O O    . HOH   F 4 .   ? 40.098 -11.344 -13.958 1.00 33.43 ?  366 HOH   B O    1 
HETATM 7059 O O    . HOH   F 4 .   ? 48.325 -26.486 8.850   1.00 40.43 ?  367 HOH   B O    1 
HETATM 7060 O O    . HOH   F 4 .   ? 58.907 -10.400 9.269   1.00 39.24 ?  368 HOH   B O    1 
HETATM 7061 O O    . HOH   F 4 .   ? 36.181 -8.633  8.981   1.00 39.05 ?  369 HOH   B O    1 
HETATM 7062 O O    . HOH   F 4 .   ? 39.859 -6.994  7.832   1.00 40.88 ?  370 HOH   B O    1 
HETATM 7063 O O    . HOH   F 4 .   ? 41.825 -10.041 -17.432 1.00 57.55 ?  371 HOH   B O    1 
HETATM 7064 O O    . HOH   F 4 .   ? 52.030 -12.941 13.363  1.00 32.44 ?  372 HOH   B O    1 
HETATM 7065 O O    . HOH   F 4 .   ? 56.018 -7.766  -0.577  1.00 33.44 ?  373 HOH   B O    1 
HETATM 7066 O O    . HOH   F 4 .   ? 41.824 -6.758  -4.878  1.00 46.48 ?  374 HOH   B O    1 
HETATM 7067 O O    . HOH   F 4 .   ? 62.956 -12.364 6.977   1.00 37.71 ?  375 HOH   B O    1 
HETATM 7068 O O    . HOH   F 4 .   ? 38.000 -10.540 10.064  1.00 30.43 ?  376 HOH   B O    1 
HETATM 7069 O O    . HOH   F 4 .   ? 36.505 -22.797 13.305  1.00 27.72 ?  377 HOH   B O    1 
HETATM 7070 O O    . HOH   F 4 .   ? 42.620 -17.064 -23.181 1.00 44.34 ?  378 HOH   B O    1 
HETATM 7071 O O    . HOH   F 4 .   ? 40.088 -7.626  3.241   1.00 38.13 ?  379 HOH   B O    1 
HETATM 7072 O O    . HOH   F 4 .   ? 44.014 -5.584  -3.456  1.00 40.33 ?  380 HOH   B O    1 
HETATM 7073 O O    . HOH   F 4 .   ? 39.596 -13.991 15.702  1.00 50.96 ?  381 HOH   B O    1 
HETATM 7074 O O    . HOH   F 4 .   ? 52.797 -29.860 7.229   1.00 23.90 ?  382 HOH   B O    1 
HETATM 7075 O O    . HOH   F 4 .   ? 60.460 -22.253 2.860   1.00 46.29 ?  383 HOH   B O    1 
HETATM 7076 O O    . HOH   F 4 .   ? 46.666 -5.405  2.940   1.00 41.43 ?  384 HOH   B O    1 
HETATM 7077 O O    . HOH   F 4 .   ? 25.801 -18.853 -11.880 1.00 40.50 ?  385 HOH   B O    1 
HETATM 7078 O O    . HOH   F 4 .   ? 35.365 -33.720 7.313   1.00 42.97 ?  386 HOH   B O    1 
HETATM 7079 O O    . HOH   F 4 .   ? 40.939 -9.800  15.846  1.00 45.40 ?  387 HOH   B O    1 
HETATM 7080 O O    . HOH   F 4 .   ? 23.933 -20.843 -7.680  1.00 28.47 ?  388 HOH   B O    1 
HETATM 7081 O O    . HOH   F 4 .   ? 35.303 -20.302 13.330  1.00 33.37 ?  389 HOH   B O    1 
HETATM 7082 O O    . HOH   F 4 .   ? 40.670 -6.628  -0.841  1.00 25.52 ?  390 HOH   B O    1 
HETATM 7083 O O    . HOH   F 4 .   ? 44.023 -31.708 -3.731  1.00 36.26 ?  391 HOH   B O    1 
HETATM 7084 O O    . HOH   F 4 .   ? 27.900 -27.045 2.213   1.00 30.94 ?  392 HOH   B O    1 
HETATM 7085 O O    . HOH   F 4 .   ? 26.604 -27.979 -13.449 1.00 34.19 ?  393 HOH   B O    1 
HETATM 7086 O O    . HOH   F 4 .   ? 34.358 -33.424 9.649   1.00 34.67 ?  394 HOH   B O    1 
HETATM 7087 O O    . HOH   F 4 .   ? 24.611 -20.624 -10.510 1.00 41.44 ?  395 HOH   B O    1 
HETATM 7088 O O    . HOH   F 4 .   ? 50.608 -30.770 8.719   1.00 29.22 ?  396 HOH   B O    1 
HETATM 7089 O O    . HOH   F 4 .   ? 26.827 -30.654 -12.636 1.00 30.17 ?  397 HOH   B O    1 
HETATM 7090 O O    . HOH   F 4 .   ? 45.673 -20.246 15.210  1.00 53.05 ?  398 HOH   B O    1 
HETATM 7091 O O    . HOH   F 4 .   ? 57.642 -6.499  -2.365  1.00 33.78 ?  399 HOH   B O    1 
HETATM 7092 O O    . HOH   F 4 .   ? 40.946 -11.729 -22.307 1.00 40.55 ?  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   ? 0.6613 0.6741 0.7303 -0.0047 -0.0297 0.0700  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.6601 0.6710 0.7119 -0.0072 -0.0266 0.0604  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.6598 0.6725 0.7191 -0.0064 -0.0284 0.0706  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.6585 0.6696 0.7033 -0.0086 -0.0261 0.0617  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.6487 0.6639 0.6979 -0.0137 -0.0330 0.0785  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.6481 0.6622 0.6878 -0.0148 -0.0312 0.0731  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.6510 0.6659 0.7135 -0.0123 -0.0354 0.0810  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.6504 0.6640 0.7009 -0.0135 -0.0329 0.0747  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.6670 0.6781 0.7223 -0.0025 -0.0226 0.0639  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.6651 0.6742 0.7044 -0.0051 -0.0208 0.0530  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.6696 0.6796 0.7207 -0.0006 -0.0208 0.0614  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.6674 0.6753 0.7028 -0.0036 -0.0191 0.0498  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.6689 0.6800 0.7211 -0.0016 -0.0207 0.0620  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.6670 0.6758 0.7027 -0.0041 -0.0191 0.0503  3   VAL   A CG2 
31   N N   . ASN   A 4   ? 0.6331 0.6514 0.6523 -0.0229 -0.0341 0.0820  4   ASN   A N   
32   C CA  . ASN   A 4   ? 0.6003 0.6264 0.5603 -0.0413 -0.0363 0.0908  4   ASN   A CA  
33   C C   . ASN   A 4   ? 0.5576 0.6009 0.5118 -0.0582 -0.0237 0.0707  4   ASN   A C   
34   O O   . ASN   A 4   ? 0.5577 0.6020 0.5017 -0.0598 -0.0222 0.0753  4   ASN   A O   
35   C CB  . ASN   A 4   ? 0.6062 0.6245 0.5141 -0.0430 -0.0498 0.1178  4   ASN   A CB  
36   C CG  . ASN   A 4   ? 0.6092 0.6213 0.4689 -0.0455 -0.0633 0.1432  4   ASN   A CG  
37   O OD1 . ASN   A 4   ? 0.6125 0.6201 0.4505 -0.0470 -0.0675 0.1516  4   ASN   A OD1 
38   N ND2 . ASN   A 4   ? 0.6084 0.6200 0.4587 -0.0450 -0.0696 0.1554  4   ASN   A ND2 
46   N N   . SER   A 5   ? 0.5116 0.5697 0.4754 -0.0751 -0.0134 0.0446  5   SER   A N   
47   C CA  . SER   A 5   ? 0.4625 0.5353 0.4417 -0.0913 0.0010  0.0177  5   SER   A CA  
48   C C   . SER   A 5   ? 0.4069 0.4883 0.3748 -0.1031 0.0207  0.0029  5   SER   A C   
49   O O   . SER   A 5   ? 0.4109 0.4947 0.3650 -0.0994 0.0209  -0.0078 5   SER   A O   
50   C CB  . SER   A 5   ? 0.4703 0.5462 0.4855 -0.0948 -0.0049 0.0058  5   SER   A CB  
51   O OG  . SER   A 5   ? 0.4740 0.5500 0.5060 -0.0978 -0.0086 -0.0016 5   SER   A OG  
57   N N   . PHE   A 6   ? 0.3452 0.4327 0.3022 -0.1158 0.0392  0.0058  6   PHE   A N   
58   C CA  . PHE   A 6   ? 0.2897 0.3756 0.2485 -0.1171 0.0472  0.0196  6   PHE   A CA  
59   C C   . PHE   A 6   ? 0.2830 0.3669 0.2535 -0.1123 0.0634  0.0163  6   PHE   A C   
60   O O   . PHE   A 6   ? 0.2943 0.3735 0.2888 -0.1179 0.0634  0.0335  6   PHE   A O   
61   C CB  . PHE   A 6   ? 0.2660 0.3316 0.2124 -0.1012 0.0278  0.0333  6   PHE   A CB  
62   C CG  . PHE   A 6   ? 0.2465 0.2958 0.1968 -0.0832 0.0151  0.0311  6   PHE   A CG  
63   C CD1 . PHE   A 6   ? 0.2364 0.2791 0.1949 -0.0727 0.0081  0.0285  6   PHE   A CD1 
64   C CD2 . PHE   A 6   ? 0.2528 0.2854 0.2167 -0.0608 0.0199  0.0297  6   PHE   A CD2 
65   C CE1 . PHE   A 6   ? 0.2352 0.2710 0.2034 -0.0673 0.0158  0.0322  6   PHE   A CE1 
66   C CE2 . PHE   A 6   ? 0.2477 0.2768 0.2326 -0.0537 0.0202  0.0265  6   PHE   A CE2 
67   C CZ  . PHE   A 6   ? 0.2437 0.2713 0.2236 -0.0558 0.0107  0.0261  6   PHE   A CZ  
77   N N   A SER   A 7   ? 0.2731 0.3568 0.2330 -0.1099 0.0712  0.0077  7   SER   A N   
78   N N   B SER   A 7   ? 0.2755 0.3553 0.2540 -0.0987 0.0677  0.0074  7   SER   A N   
79   C CA  A SER   A 7   ? 0.2718 0.3476 0.2379 -0.0982 0.0650  -0.0092 7   SER   A CA  
80   C CA  B SER   A 7   ? 0.2738 0.3449 0.2692 -0.0792 0.0637  -0.0026 7   SER   A CA  
81   C C   A SER   A 7   ? 0.2549 0.3090 0.2012 -0.0914 0.0697  -0.0121 7   SER   A C   
82   C C   B SER   A 7   ? 0.2619 0.3173 0.2447 -0.0680 0.0705  0.0015  7   SER   A C   
83   O O   A SER   A 7   ? 0.2679 0.2997 0.1934 -0.0913 0.0755  -0.0118 7   SER   A O   
84   O O   B SER   A 7   ? 0.2685 0.3135 0.2413 -0.0697 0.0730  0.0024  7   SER   A O   
85   C CB  A SER   A 7   ? 0.2918 0.3734 0.2698 -0.0862 0.0612  -0.0117 7   SER   A CB  
86   C CB  B SER   A 7   ? 0.2847 0.3600 0.3010 -0.0687 0.0539  -0.0074 7   SER   A CB  
87   O OG  A SER   A 7   ? 0.3090 0.3878 0.2928 -0.0772 0.0538  -0.0161 7   SER   A OG  
88   O OG  B SER   A 7   ? 0.2933 0.3683 0.3285 -0.0613 0.0434  -0.0070 7   SER   A OG  
99   N N   A GLY   A 8   ? 0.2305 0.2791 0.1806 -0.0819 0.0642  -0.0248 8   GLY   A N   
100  N N   B GLY   A 8   ? 0.2441 0.2929 0.2250 -0.0563 0.0706  -0.0004 8   GLY   A N   
101  C CA  A GLY   A 8   ? 0.2105 0.2532 0.1819 -0.0601 0.0643  -0.0217 8   GLY   A CA  
102  C CA  B GLY   A 8   ? 0.2263 0.2671 0.2091 -0.0446 0.0642  0.0034  8   GLY   A CA  
103  C C   A GLY   A 8   ? 0.1898 0.2325 0.1815 -0.0383 0.0492  -0.0185 8   GLY   A C   
104  C C   B GLY   A 8   ? 0.2045 0.2443 0.1894 -0.0314 0.0561  0.0051  8   GLY   A C   
105  O O   A GLY   A 8   ? 0.1925 0.2372 0.1972 -0.0190 0.0483  -0.0327 8   GLY   A O   
106  O O   B GLY   A 8   ? 0.2061 0.2470 0.1979 -0.0218 0.0554  -0.0050 8   GLY   A O   
113  N N   A TYR   A 9   ? 0.1693 0.2064 0.1692 -0.0311 0.0423  -0.0047 9   TYR   A N   
114  N N   B TYR   A 9   ? 0.1848 0.2205 0.1834 -0.0258 0.0387  0.0144  9   TYR   A N   
115  C CA  A TYR   A 9   ? 0.1562 0.1900 0.1500 -0.0241 0.0308  0.0044  9   TYR   A CA  
116  C CA  B TYR   A 9   ? 0.1701 0.2001 0.1717 -0.0224 0.0358  0.0192  9   TYR   A CA  
117  C C   A TYR   A 9   ? 0.1596 0.1696 0.1485 -0.0072 0.0318  0.0147  9   TYR   A C   
118  C C   B TYR   A 9   ? 0.1706 0.1792 0.1619 -0.0110 0.0366  0.0194  9   TYR   A C   
119  O O   A TYR   A 9   ? 0.1784 0.1835 0.1644 -0.0119 0.0203  0.0085  9   TYR   A O   
120  O O   B TYR   A 9   ? 0.1839 0.1940 0.1705 -0.0142 0.0314  0.0223  9   TYR   A O   
121  C CB  A TYR   A 9   ? 0.1506 0.1977 0.1530 -0.0236 0.0296  -0.0044 9   TYR   A CB  
122  C CB  B TYR   A 9   ? 0.1683 0.2130 0.1863 -0.0198 0.0278  0.0172  9   TYR   A CB  
123  C CG  A TYR   A 9   ? 0.1527 0.2055 0.1738 -0.0118 0.0392  -0.0073 9   TYR   A CG  
124  C CG  B TYR   A 9   ? 0.1716 0.2179 0.1934 -0.0169 0.0234  0.0224  9   TYR   A CG  
125  C CD1 A TYR   A 9   ? 0.1513 0.2051 0.1998 -0.0209 0.0451  -0.0110 9   TYR   A CD1 
126  C CD1 B TYR   A 9   ? 0.1727 0.2190 0.2071 -0.0253 0.0270  0.0222  9   TYR   A CD1 
127  C CD2 A TYR   A 9   ? 0.1527 0.2101 0.1815 -0.0056 0.0335  0.0086  9   TYR   A CD2 
128  C CD2 B TYR   A 9   ? 0.1701 0.2154 0.1888 -0.0153 0.0203  0.0327  9   TYR   A CD2 
129  C CE1 A TYR   A 9   ? 0.1613 0.2135 0.2213 -0.0238 0.0474  -0.0059 9   TYR   A CE1 
130  C CE1 B TYR   A 9   ? 0.1754 0.2186 0.2091 -0.0305 0.0335  0.0233  9   TYR   A CE1 
131  C CE2 A TYR   A 9   ? 0.1555 0.2176 0.2005 -0.0082 0.0411  0.0062  9   TYR   A CE2 
132  C CE2 B TYR   A 9   ? 0.1708 0.2180 0.1942 -0.0204 0.0289  0.0304  9   TYR   A CE2 
133  C CZ  A TYR   A 9   ? 0.1580 0.2238 0.2295 -0.0244 0.0584  -0.0020 9   TYR   A CZ  
134  C CZ  B TYR   A 9   ? 0.1709 0.2199 0.2076 -0.0319 0.0417  0.0280  9   TYR   A CZ  
135  O OH  A TYR   A 9   ? 0.1698 0.2384 0.2552 -0.0407 0.0647  -0.0034 9   TYR   A OH  
136  O OH  B TYR   A 9   ? 0.1732 0.2260 0.2172 -0.0452 0.0442  0.0241  9   TYR   A OH  
155  N N   A LEU   A 10  ? 0.1534 0.1464 0.1579 -0.0089 0.0302  0.0125  10  LEU   A N   
156  N N   B LEU   A 10  ? 0.1670 0.1601 0.1621 -0.0067 0.0275  0.0085  10  LEU   A N   
157  C CA  A LEU   A 10  ? 0.1466 0.1387 0.1823 -0.0204 0.0223  0.0248  10  LEU   A CA  
158  C CA  B LEU   A 10  ? 0.1598 0.1518 0.1689 -0.0051 0.0226  0.0083  10  LEU   A CA  
159  C C   A LEU   A 10  ? 0.1365 0.1331 0.1754 -0.0138 0.0283  0.0282  10  LEU   A C   
160  C C   B LEU   A 10  ? 0.1525 0.1450 0.1661 -0.0047 0.0183  0.0117  10  LEU   A C   
161  O O   A LEU   A 10  ? 0.1438 0.1317 0.1815 -0.0112 0.0435  0.0209  10  LEU   A O   
162  O O   B LEU   A 10  ? 0.1543 0.1373 0.1610 -0.0066 0.0365  0.0065  10  LEU   A O   
163  C CB  A LEU   A 10  ? 0.1477 0.1418 0.2254 -0.0233 0.0104  0.0370  10  LEU   A CB  
164  C CB  B LEU   A 10  ? 0.1640 0.1527 0.1934 -0.0095 0.0107  0.0232  10  LEU   A CB  
165  C CG  A LEU   A 10  ? 0.1730 0.1479 0.2738 -0.0214 -0.0327 0.0544  10  LEU   A CG  
166  C CG  B LEU   A 10  ? 0.1833 0.1663 0.2328 -0.0049 0.0002  0.0410  10  LEU   A CG  
167  C CD1 A LEU   A 10  ? 0.1909 0.1571 0.3044 -0.0182 -0.0278 0.0634  10  LEU   A CD1 
168  C CD1 B LEU   A 10  ? 0.2002 0.1803 0.2626 -0.0071 0.0030  0.0482  10  LEU   A CD1 
169  C CD2 A LEU   A 10  ? 0.1904 0.1585 0.2912 -0.0271 -0.0324 0.0431  10  LEU   A CD2 
170  C CD2 B LEU   A 10  ? 0.1936 0.1727 0.2413 -0.0147 0.0099  0.0522  10  LEU   A CD2 
193  N N   A LYS   A 11  ? 0.1351 0.1331 0.1813 -0.0076 0.0267  0.0254  11  LYS   A N   
194  N N   B LYS   A 11  ? 0.1546 0.1432 0.1654 -0.0053 0.0041  0.0216  11  LYS   A N   
195  C CA  A LYS   A 11  ? 0.1430 0.1319 0.1948 -0.0122 0.0258  0.0266  11  LYS   A CA  
196  C CA  B LYS   A 11  ? 0.1553 0.1399 0.1615 -0.0115 0.0092  0.0247  11  LYS   A CA  
197  C C   A LYS   A 11  ? 0.1392 0.1389 0.2022 -0.0139 0.0318  0.0125  11  LYS   A C   
198  C C   B LYS   A 11  ? 0.1444 0.1319 0.1673 -0.0167 0.0140  0.0161  11  LYS   A C   
199  O O   A LYS   A 11  ? 0.1431 0.1552 0.2439 -0.0398 0.0464  -0.0046 11  LYS   A O   
200  O O   B LYS   A 11  ? 0.1406 0.1320 0.1876 -0.0162 0.0050  -0.0006 11  LYS   A O   
201  C CB  A LYS   A 11  ? 0.1460 0.1352 0.2022 -0.0112 0.0213  0.0184  11  LYS   A CB  
202  C CB  B LYS   A 11  ? 0.1664 0.1362 0.1545 -0.0106 0.0050  0.0213  11  LYS   A CB  
203  C CG  A LYS   A 11  ? 0.1536 0.1411 0.2099 -0.0144 0.0234  0.0215  11  LYS   A CG  
204  C CG  B LYS   A 11  ? 0.1757 0.1399 0.1384 -0.0068 0.0127  0.0338  11  LYS   A CG  
205  C CD  A LYS   A 11  ? 0.1666 0.1572 0.2179 -0.0066 0.0207  0.0239  11  LYS   A CD  
206  C CD  B LYS   A 11  ? 0.1827 0.1470 0.1389 -0.0015 0.0225  0.0389  11  LYS   A CD  
207  C CE  A LYS   A 11  ? 0.1732 0.1578 0.2197 -0.0004 0.0276  0.0290  11  LYS   A CE  
208  C CE  B LYS   A 11  ? 0.1844 0.1490 0.1350 -0.0063 0.0233  0.0401  11  LYS   A CE  
209  N NZ  A LYS   A 11  ? 0.1683 0.1528 0.2238 0.0123  0.0304  0.0232  11  LYS   A NZ  
210  N NZ  B LYS   A 11  ? 0.1831 0.1518 0.1288 -0.0048 0.0200  0.0346  11  LYS   A NZ  
237  N N   A LEU   A 12  ? 0.1374 0.1325 0.1794 -0.0158 0.0288  0.0129  12  LEU   A N   
238  N N   B LEU   A 12  ? 0.1405 0.1386 0.1730 -0.0063 0.0154  0.0085  12  LEU   A N   
239  C CA  A LEU   A 12  ? 0.1459 0.1421 0.1797 -0.0144 0.0201  0.0207  12  LEU   A CA  
240  C CA  B LEU   A 12  ? 0.1438 0.1489 0.1759 -0.0032 0.0134  0.0176  12  LEU   A CA  
241  C C   A LEU   A 12  ? 0.1440 0.1334 0.1768 -0.0192 0.0185  0.0192  12  LEU   A C   
242  C C   B LEU   A 12  ? 0.1421 0.1507 0.1675 -0.0072 0.0217  0.0128  12  LEU   A C   
243  O O   A LEU   A 12  ? 0.1446 0.1301 0.1898 -0.0129 0.0255  0.0069  12  LEU   A O   
244  O O   B LEU   A 12  ? 0.1488 0.1532 0.1644 -0.0032 0.0143  0.0011  12  LEU   A O   
245  C CB  A LEU   A 12  ? 0.1567 0.1419 0.2032 -0.0125 0.0111  0.0288  12  LEU   A CB  
246  C CB  B LEU   A 12  ? 0.1482 0.1591 0.1986 -0.0018 0.0166  0.0301  12  LEU   A CB  
247  C CG  A LEU   A 12  ? 0.1698 0.1590 0.2415 -0.0054 0.0117  0.0376  12  LEU   A CG  
248  C CG  B LEU   A 12  ? 0.1509 0.1655 0.2183 -0.0039 0.0266  0.0398  12  LEU   A CG  
249  C CD1 A LEU   A 12  ? 0.1863 0.1744 0.2591 0.0033  0.0152  0.0503  12  LEU   A CD1 
250  C CD1 B LEU   A 12  ? 0.1596 0.1768 0.2260 -0.0017 0.0342  0.0466  12  LEU   A CD1 
251  C CD2 A LEU   A 12  ? 0.1711 0.1654 0.2690 -0.0030 0.0058  0.0292  12  LEU   A CD2 
252  C CD2 B LEU   A 12  ? 0.1492 0.1712 0.2368 -0.0044 0.0249  0.0373  12  LEU   A CD2 
275  N N   A THR   A 13  ? 0.1398 0.1315 0.1913 -0.0172 0.0071  0.0170  13  THR   A N   
276  N N   B THR   A 13  ? 0.1402 0.1462 0.1731 -0.0053 0.0157  0.0066  13  THR   A N   
277  C CA  A THR   A 13  ? 0.1430 0.1402 0.2014 -0.0113 0.0228  0.0162  13  THR   A CA  
278  C CA  B THR   A 13  ? 0.1432 0.1493 0.1739 -0.0058 0.0195  0.0102  13  THR   A CA  
279  C C   A THR   A 13  ? 0.1393 0.1402 0.2147 -0.0113 0.0157  0.0273  13  THR   A C   
280  C C   B THR   A 13  ? 0.1457 0.1576 0.1843 -0.0105 0.0208  0.0193  13  THR   A C   
281  O O   A THR   A 13  ? 0.1366 0.1450 0.2148 -0.0066 0.0111  0.0234  13  THR   A O   
282  O O   B THR   A 13  ? 0.1513 0.1634 0.1842 -0.0119 0.0123  0.0191  13  THR   A O   
283  C CB  A THR   A 13  ? 0.1491 0.1531 0.2206 -0.0093 0.0190  0.0170  13  THR   A CB  
284  C CB  B THR   A 13  ? 0.1423 0.1542 0.1808 -0.0004 0.0200  0.0155  13  THR   A CB  
285  O OG1 A THR   A 13  ? 0.1508 0.1451 0.2257 -0.0124 0.0075  0.0262  13  THR   A OG1 
286  O OG1 B THR   A 13  ? 0.1297 0.1596 0.2006 -0.0031 0.0319  0.0182  13  THR   A OG1 
287  C CG2 A THR   A 13  ? 0.1612 0.1654 0.2321 -0.0079 0.0262  0.0052  13  THR   A CG2 
288  C CG2 B THR   A 13  ? 0.1510 0.1612 0.1785 0.0046  0.0137  0.0071  13  THR   A CG2 
303  N N   A ASP   A 14  ? 0.1424 0.1432 0.2373 -0.0158 0.0152  0.0338  14  ASP   A N   
304  N N   B ASP   A 14  ? 0.1434 0.1571 0.2066 -0.0182 0.0200  0.0378  14  ASP   A N   
305  C CA  A ASP   A 14  ? 0.1433 0.1605 0.2546 -0.0125 0.0030  0.0496  14  ASP   A CA  
306  C CA  B ASP   A 14  ? 0.1517 0.1597 0.2368 -0.0154 0.0049  0.0594  14  ASP   A CA  
307  C C   A ASP   A 14  ? 0.1480 0.1621 0.2363 -0.0132 -0.0076 0.0530  14  ASP   A C   
308  C C   B ASP   A 14  ? 0.1479 0.1546 0.2323 -0.0179 -0.0095 0.0626  14  ASP   A C   
309  O O   A ASP   A 14  ? 0.1606 0.1664 0.2426 -0.0132 -0.0180 0.0595  14  ASP   A O   
310  O O   B ASP   A 14  ? 0.1493 0.1456 0.2390 -0.0218 -0.0181 0.0709  14  ASP   A O   
311  C CB  A ASP   A 14  ? 0.1576 0.1958 0.3130 -0.0124 0.0085  0.0584  14  ASP   A CB  
312  C CB  B ASP   A 14  ? 0.1668 0.1804 0.2898 -0.0115 -0.0007 0.0717  14  ASP   A CB  
313  C CG  A ASP   A 14  ? 0.1831 0.2469 0.3832 -0.0107 0.0049  0.0558  14  ASP   A CG  
314  C CG  B ASP   A 14  ? 0.1758 0.2172 0.3417 -0.0104 0.0036  0.0683  14  ASP   A CG  
315  O OD1 A ASP   A 14  ? 0.1923 0.2621 0.4028 -0.0101 -0.0154 0.0615  14  ASP   A OD1 
316  O OD1 B ASP   A 14  ? 0.1766 0.2237 0.3546 -0.0286 0.0100  0.0772  14  ASP   A OD1 
317  O OD2 A ASP   A 14  ? 0.2006 0.2781 0.4233 0.0100  0.0063  0.0383  14  ASP   A OD2 
318  O OD2 B ASP   A 14  ? 0.1823 0.2368 0.3731 0.0062  -0.0062 0.0528  14  ASP   A OD2 
327  N N   . ASN   A 15  ? 0.1430 0.1561 0.2329 -0.0227 -0.0084 0.0537  15  ASN   A N   
328  C CA  . ASN   A 15  ? 0.1481 0.1613 0.2487 -0.0246 -0.0091 0.0443  15  ASN   A CA  
329  C C   . ASN   A 15  ? 0.1466 0.1555 0.2600 -0.0269 0.0000  0.0433  15  ASN   A C   
330  O O   . ASN   A 15  ? 0.1508 0.1567 0.3046 -0.0208 -0.0146 0.0443  15  ASN   A O   
331  C CB  . ASN   A 15  ? 0.1389 0.1577 0.2308 -0.0184 -0.0001 0.0452  15  ASN   A CB  
332  C CG  . ASN   A 15  ? 0.1405 0.1677 0.2388 -0.0115 0.0040  0.0349  15  ASN   A CG  
333  O OD1 . ASN   A 15  ? 0.1566 0.1720 0.2656 -0.0311 -0.0012 0.0370  15  ASN   A OD1 
334  N ND2 . ASN   A 15  ? 0.1483 0.1812 0.2314 -0.0165 0.0130  0.0285  15  ASN   A ND2 
342  N N   A VAL   A 16  ? 0.1425 0.1500 0.2373 -0.0226 0.0018  0.0442  16  VAL   A N   
343  N N   B VAL   A 16  ? 0.1461 0.1589 0.2341 -0.0185 0.0034  0.0448  16  VAL   A N   
344  C CA  A VAL   A 16  ? 0.1364 0.1518 0.2254 -0.0235 0.0008  0.0455  16  VAL   A CA  
345  C CA  B VAL   A 16  ? 0.1451 0.1651 0.2150 -0.0136 0.0080  0.0479  16  VAL   A CA  
346  C C   A VAL   A 16  ? 0.1286 0.1522 0.2172 -0.0287 -0.0047 0.0463  16  VAL   A C   
347  C C   B VAL   A 16  ? 0.1440 0.1705 0.2017 -0.0157 0.0071  0.0529  16  VAL   A C   
348  O O   A VAL   A 16  ? 0.1282 0.1491 0.2328 -0.0257 0.0024  0.0371  16  VAL   A O   
349  O O   B VAL   A 16  ? 0.1447 0.1720 0.2158 -0.0115 0.0089  0.0483  16  VAL   A O   
350  C CB  A VAL   A 16  ? 0.1463 0.1664 0.2190 -0.0050 0.0171  0.0540  16  VAL   A CB  
351  C CB  B VAL   A 16  ? 0.1494 0.1732 0.2077 0.0009  0.0250  0.0498  16  VAL   A CB  
352  C CG1 A VAL   A 16  ? 0.1581 0.1803 0.2196 0.0056  0.0234  0.0513  16  VAL   A CG1 
353  C CG1 B VAL   A 16  ? 0.1566 0.1814 0.2074 0.0086  0.0294  0.0479  16  VAL   A CG1 
354  C CG2 A VAL   A 16  ? 0.1583 0.1771 0.2334 0.0005  0.0248  0.0464  16  VAL   A CG2 
355  C CG2 B VAL   A 16  ? 0.1533 0.1778 0.2184 -0.0009 0.0308  0.0418  16  VAL   A CG2 
374  N N   A TYR   A 17  ? 0.1325 0.1494 0.2200 -0.0264 0.0021  0.0557  17  TYR   A N   
375  N N   B TYR   A 17  ? 0.1465 0.1694 0.1945 -0.0153 0.0119  0.0499  17  TYR   A N   
376  C CA  A TYR   A 17  ? 0.1370 0.1518 0.2100 -0.0251 0.0035  0.0499  17  TYR   A CA  
377  C CA  B TYR   A 17  ? 0.1456 0.1675 0.1768 -0.0164 0.0174  0.0400  17  TYR   A CA  
378  C C   A TYR   A 17  ? 0.1356 0.1488 0.2129 -0.0218 0.0014  0.0404  17  TYR   A C   
379  C C   B TYR   A 17  ? 0.1444 0.1595 0.1697 -0.0186 0.0182  0.0287  17  TYR   A C   
380  O O   A TYR   A 17  ? 0.1316 0.1552 0.2272 -0.0286 -0.0049 0.0537  17  TYR   A O   
381  O O   B TYR   A 17  ? 0.1429 0.1552 0.1795 -0.0205 0.0217  0.0249  17  TYR   A O   
382  C CB  A TYR   A 17  ? 0.1612 0.1522 0.2113 -0.0320 -0.0090 0.0478  17  TYR   A CB  
383  C CB  B TYR   A 17  ? 0.1557 0.1746 0.1859 -0.0141 0.0102  0.0327  17  TYR   A CB  
384  C CG  A TYR   A 17  ? 0.1848 0.1671 0.2101 -0.0388 -0.0302 0.0452  17  TYR   A CG  
385  C CG  B TYR   A 17  ? 0.1665 0.1897 0.1914 -0.0133 0.0019  0.0289  17  TYR   A CG  
386  C CD1 A TYR   A 17  ? 0.1956 0.1771 0.2164 -0.0292 -0.0433 0.0451  17  TYR   A CD1 
387  C CD1 B TYR   A 17  ? 0.1770 0.1975 0.2026 -0.0033 -0.0048 0.0298  17  TYR   A CD1 
388  C CD2 A TYR   A 17  ? 0.1944 0.1776 0.1973 -0.0503 -0.0389 0.0514  17  TYR   A CD2 
389  C CD2 B TYR   A 17  ? 0.1713 0.2013 0.1882 -0.0140 -0.0023 0.0318  17  TYR   A CD2 
390  C CE1 A TYR   A 17  ? 0.1959 0.1771 0.2179 -0.0348 -0.0494 0.0510  17  TYR   A CE1 
391  C CE1 B TYR   A 17  ? 0.1846 0.2060 0.2145 -0.0031 -0.0084 0.0355  17  TYR   A CE1 
392  C CE2 A TYR   A 17  ? 0.2015 0.1765 0.2017 -0.0495 -0.0523 0.0426  17  TYR   A CE2 
393  C CE2 B TYR   A 17  ? 0.1830 0.2072 0.1977 -0.0092 -0.0060 0.0311  17  TYR   A CE2 
394  C CZ  A TYR   A 17  ? 0.2007 0.1717 0.2053 -0.0482 -0.0561 0.0495  17  TYR   A CZ  
395  C CZ  B TYR   A 17  ? 0.1886 0.2109 0.2118 -0.0049 -0.0128 0.0346  17  TYR   A CZ  
396  O OH  A TYR   A 17  ? 0.2097 0.1664 0.2128 -0.0484 -0.0566 0.0457  17  TYR   A OH  
397  O OH  B TYR   A 17  ? 0.1907 0.2163 0.2228 -0.0003 -0.0212 0.0318  17  TYR   A OH  
416  N N   A ILE   A 18  ? 0.1371 0.1449 0.1817 -0.0234 -0.0049 0.0338  18  ILE   A N   
417  N N   B ILE   A 18  ? 0.1422 0.1587 0.1466 -0.0275 0.0130  0.0316  18  ILE   A N   
418  C CA  A ILE   A 18  ? 0.1493 0.1513 0.1617 -0.0155 0.0066  0.0340  18  ILE   A CA  
419  C CA  B ILE   A 18  ? 0.1414 0.1610 0.1301 -0.0204 0.0102  0.0231  18  ILE   A CA  
420  C C   A ILE   A 18  ? 0.1521 0.1522 0.1673 -0.0259 0.0112  0.0297  18  ILE   A C   
421  C C   B ILE   A 18  ? 0.1326 0.1734 0.1129 -0.0227 0.0033  0.0209  18  ILE   A C   
422  O O   A ILE   A 18  ? 0.1517 0.1564 0.1688 -0.0353 0.0073  0.0358  18  ILE   A O   
423  O O   B ILE   A 18  ? 0.1305 0.1829 0.1291 -0.0273 0.0086  0.0248  18  ILE   A O   
424  C CB  A ILE   A 18  ? 0.1599 0.1542 0.1454 -0.0030 0.0098  0.0321  18  ILE   A CB  
425  C CB  B ILE   A 18  ? 0.1491 0.1560 0.1206 -0.0169 0.0107  0.0243  18  ILE   A CB  
426  C CG1 A ILE   A 18  ? 0.1645 0.1573 0.1389 0.0089  0.0053  0.0218  18  ILE   A CG1 
427  C CG1 B ILE   A 18  ? 0.1646 0.1601 0.1356 -0.0133 0.0194  0.0261  18  ILE   A CG1 
428  C CG2 A ILE   A 18  ? 0.1617 0.1534 0.1485 -0.0074 0.0116  0.0154  18  ILE   A CG2 
429  C CG2 B ILE   A 18  ? 0.1547 0.1649 0.1333 -0.0224 0.0040  0.0221  18  ILE   A CG2 
430  C CD1 A ILE   A 18  ? 0.1824 0.1720 0.1584 0.0163  0.0083  0.0214  18  ILE   A CD1 
431  C CD1 B ILE   A 18  ? 0.1809 0.1645 0.1439 -0.0072 0.0226  0.0221  18  ILE   A CD1 
454  N N   A LYS   A 19  ? 0.1528 0.1539 0.1629 -0.0152 0.0233  0.0321  19  LYS   A N   
455  N N   B LYS   A 19  ? 0.1368 0.1775 0.1187 -0.0106 0.0165  0.0187  19  LYS   A N   
456  C CA  A LYS   A 19  ? 0.1600 0.1641 0.1722 -0.0115 0.0199  0.0316  19  LYS   A CA  
457  C CA  B LYS   A 19  ? 0.1547 0.1922 0.1418 -0.0012 0.0310  0.0132  19  LYS   A CA  
458  C C   A LYS   A 19  ? 0.1460 0.1604 0.1946 -0.0069 0.0283  0.0408  19  LYS   A C   
459  C C   B LYS   A 19  ? 0.1654 0.1960 0.1543 0.0050  0.0359  0.0154  19  LYS   A C   
460  O O   A LYS   A 19  ? 0.1398 0.1540 0.1869 -0.0086 0.0224  0.0365  19  LYS   A O   
461  O O   B LYS   A 19  ? 0.1658 0.1958 0.1629 -0.0011 0.0319  0.0240  19  LYS   A O   
462  C CB  A LYS   A 19  ? 0.1840 0.1820 0.1842 -0.0133 0.0121  0.0231  19  LYS   A CB  
463  C CB  B LYS   A 19  ? 0.1565 0.2052 0.1580 -0.0034 0.0333  0.0035  19  LYS   A CB  
464  C CG  A LYS   A 19  ? 0.2115 0.2027 0.2051 -0.0141 0.0052  0.0142  19  LYS   A CG  
465  C CG  B LYS   A 19  ? 0.1821 0.2200 0.1628 -0.0028 0.0364  0.0010  19  LYS   A CG  
466  C CD  A LYS   A 19  ? 0.2374 0.2241 0.2196 -0.0213 0.0040  0.0060  19  LYS   A CD  
467  C CD  B LYS   A 19  ? 0.2033 0.2343 0.1684 -0.0085 0.0380  0.0070  19  LYS   A CD  
468  C CE  A LYS   A 19  ? 0.2589 0.2379 0.2226 -0.0323 0.0054  0.0068  19  LYS   A CE  
469  C CE  B LYS   A 19  ? 0.2180 0.2462 0.1790 -0.0144 0.0363  0.0072  19  LYS   A CE  
470  N NZ  A LYS   A 19  ? 0.2687 0.2513 0.2174 -0.0421 0.0123  0.0041  19  LYS   A NZ  
471  N NZ  B LYS   A 19  ? 0.2272 0.2556 0.1829 -0.0226 0.0423  0.0050  19  LYS   A NZ  
498  N N   A ASN   A 20  ? 0.1464 0.1593 0.2307 -0.0084 0.0359  0.0603  20  ASN   A N   
499  N N   B ASN   A 20  ? 0.1806 0.2031 0.1757 0.0082  0.0349  0.0079  20  ASN   A N   
500  C CA  A ASN   A 20  ? 0.1523 0.1795 0.2421 0.0087  0.0499  0.0571  20  ASN   A CA  
501  C CA  B ASN   A 20  ? 0.1980 0.2189 0.2083 0.0135  0.0330  -0.0006 20  ASN   A CA  
502  C C   A ASN   A 20  ? 0.1766 0.1922 0.2517 -0.0011 0.0727  0.0408  20  ASN   A C   
503  C C   B ASN   A 20  ? 0.2066 0.2141 0.2221 0.0010  0.0414  -0.0099 20  ASN   A C   
504  O O   A ASN   A 20  ? 0.2097 0.2110 0.2621 -0.0229 0.0790  0.0221  20  ASN   A O   
505  O O   B ASN   A 20  ? 0.2209 0.2231 0.2242 -0.0161 0.0395  -0.0146 20  ASN   A O   
506  C CB  A ASN   A 20  ? 0.1504 0.1898 0.2490 0.0175  0.0509  0.0702  20  ASN   A CB  
507  C CB  B ASN   A 20  ? 0.2161 0.2391 0.2371 0.0259  0.0246  0.0035  20  ASN   A CB  
508  C CG  A ASN   A 20  ? 0.1559 0.1953 0.2767 0.0300  0.0569  0.0801  20  ASN   A CG  
509  C CG  B ASN   A 20  ? 0.2369 0.2565 0.2691 0.0359  0.0185  0.0093  20  ASN   A CG  
510  O OD1 A ASN   A 20  ? 0.1782 0.1970 0.3065 0.0445  0.0670  0.0687  20  ASN   A OD1 
511  O OD1 B ASN   A 20  ? 0.2484 0.2629 0.2828 0.0357  0.0067  0.0063  20  ASN   A OD1 
512  N ND2 A ASN   A 20  ? 0.1521 0.1940 0.2998 0.0299  0.0459  0.0954  20  ASN   A ND2 
513  N ND2 B ASN   A 20  ? 0.2441 0.2622 0.2864 0.0417  0.0135  0.0160  20  ASN   A ND2 
526  N N   A ALA   A 21  ? 0.1737 0.1917 0.2543 0.0043  0.0668  0.0343  21  ALA   A N   
527  N N   B ALA   A 21  ? 0.2053 0.2045 0.2320 0.0012  0.0405  -0.0102 21  ALA   A N   
528  C CA  A ALA   A 21  ? 0.1871 0.1949 0.2606 -0.0022 0.0572  0.0419  21  ALA   A CA  
529  C CA  B ALA   A 21  ? 0.2089 0.1983 0.2374 -0.0072 0.0404  0.0004  21  ALA   A CA  
530  C C   A ALA   A 21  ? 0.1699 0.1911 0.2607 -0.0063 0.0461  0.0486  21  ALA   A C   
531  C C   B ALA   A 21  ? 0.1976 0.1896 0.2332 -0.0068 0.0516  0.0155  21  ALA   A C   
532  O O   A ALA   A 21  ? 0.1583 0.1970 0.2628 0.0043  0.0305  0.0625  21  ALA   A O   
533  O O   B ALA   A 21  ? 0.1970 0.1859 0.2400 0.0031  0.0546  0.0217  21  ALA   A O   
534  C CB  A ALA   A 21  ? 0.2112 0.2044 0.2622 -0.0077 0.0483  0.0439  21  ALA   A CB  
535  C CB  B ALA   A 21  ? 0.2230 0.2042 0.2557 -0.0157 0.0276  0.0000  21  ALA   A CB  
546  N N   A ASP   A 22  ? 0.1678 0.1860 0.2669 -0.0081 0.0476  0.0428  22  ASP   A N   
547  N N   B ASP   A 22  ? 0.1925 0.1873 0.2297 -0.0111 0.0606  0.0278  22  ASP   A N   
548  C CA  A ASP   A 22  ? 0.1724 0.1873 0.2585 -0.0048 0.0370  0.0395  22  ASP   A CA  
549  C CA  B ASP   A 22  ? 0.1889 0.1898 0.2254 -0.0072 0.0617  0.0314  22  ASP   A CA  
550  C C   A ASP   A 22  ? 0.1711 0.1866 0.2235 0.0012  0.0354  0.0416  22  ASP   A C   
551  C C   B ASP   A 22  ? 0.1724 0.1852 0.1898 -0.0161 0.0583  0.0319  22  ASP   A C   
552  O O   A ASP   A 22  ? 0.1776 0.1900 0.2268 0.0012  0.0357  0.0387  22  ASP   A O   
553  O O   B ASP   A 22  ? 0.1735 0.1917 0.1855 -0.0183 0.0582  0.0288  22  ASP   A O   
554  C CB  A ASP   A 22  ? 0.1829 0.1892 0.2825 -0.0083 0.0362  0.0308  22  ASP   A CB  
555  C CB  B ASP   A 22  ? 0.2032 0.1949 0.2494 0.0052  0.0757  0.0289  22  ASP   A CB  
556  C CG  A ASP   A 22  ? 0.2007 0.1991 0.3026 -0.0095 0.0292  0.0343  22  ASP   A CG  
557  C CG  B ASP   A 22  ? 0.2157 0.1977 0.2650 0.0106  0.0890  0.0314  22  ASP   A CG  
558  O OD1 A ASP   A 22  ? 0.1934 0.1945 0.3237 -0.0195 0.0157  0.0485  22  ASP   A OD1 
559  O OD1 B ASP   A 22  ? 0.2151 0.1964 0.2559 0.0049  0.0896  0.0352  22  ASP   A OD1 
560  O OD2 A ASP   A 22  ? 0.2287 0.2115 0.3140 -0.0015 0.0400  0.0160  22  ASP   A OD2 
561  O OD2 B ASP   A 22  ? 0.2314 0.2080 0.2881 0.0106  0.0984  0.0344  22  ASP   A OD2 
570  N N   A ILE   A 23  ? 0.1769 0.1843 0.2071 0.0003  0.0351  0.0348  23  ILE   A N   
571  N N   B ILE   A 23  ? 0.1652 0.1750 0.1780 -0.0187 0.0459  0.0240  23  ILE   A N   
572  C CA  A ILE   A 23  ? 0.1767 0.1736 0.1921 0.0014  0.0366  0.0272  23  ILE   A CA  
573  C CA  B ILE   A 23  ? 0.1602 0.1754 0.1682 -0.0169 0.0334  0.0235  23  ILE   A CA  
574  C C   A ILE   A 23  ? 0.1764 0.1798 0.1837 0.0061  0.0479  0.0207  23  ILE   A C   
575  C C   B ILE   A 23  ? 0.1680 0.1856 0.1691 -0.0283 0.0426  0.0118  23  ILE   A C   
576  O O   A ILE   A 23  ? 0.1859 0.1907 0.1862 0.0115  0.0327  0.0124  23  ILE   A O   
577  O O   B ILE   A 23  ? 0.1700 0.1831 0.1683 -0.0261 0.0371  0.0139  23  ILE   A O   
578  C CB  A ILE   A 23  ? 0.1848 0.1658 0.1600 0.0071  0.0288  0.0211  23  ILE   A CB  
579  C CB  B ILE   A 23  ? 0.1608 0.1696 0.1533 -0.0018 0.0187  0.0276  23  ILE   A CB  
580  C CG1 A ILE   A 23  ? 0.1857 0.1658 0.1629 0.0046  0.0219  0.0117  23  ILE   A CG1 
581  C CG1 B ILE   A 23  ? 0.1653 0.1683 0.1493 -0.0043 0.0053  0.0217  23  ILE   A CG1 
582  C CG2 A ILE   A 23  ? 0.1879 0.1664 0.1557 0.0123  0.0307  0.0299  23  ILE   A CG2 
583  C CG2 B ILE   A 23  ? 0.1588 0.1646 0.1574 0.0125  0.0156  0.0303  23  ILE   A CG2 
584  C CD1 A ILE   A 23  ? 0.1831 0.1730 0.1638 0.0002  0.0063  -0.0024 23  ILE   A CD1 
585  C CD1 B ILE   A 23  ? 0.1633 0.1693 0.1603 -0.0033 -0.0095 0.0135  23  ILE   A CD1 
608  N N   A VAL   A 24  ? 0.1816 0.1841 0.1860 0.0007  0.0466  0.0131  24  VAL   A N   
609  N N   B VAL   A 24  ? 0.1777 0.1950 0.1821 -0.0358 0.0444  -0.0008 24  VAL   A N   
610  C CA  A VAL   A 24  ? 0.2010 0.1977 0.1947 -0.0071 0.0417  -0.0025 24  VAL   A CA  
611  C CA  B VAL   A 24  ? 0.2002 0.2033 0.2026 -0.0391 0.0427  -0.0028 24  VAL   A CA  
612  C C   A VAL   A 24  ? 0.2064 0.2130 0.1919 -0.0184 0.0278  0.0004  24  VAL   A C   
613  C C   B VAL   A 24  ? 0.2094 0.2214 0.2005 -0.0420 0.0478  -0.0098 24  VAL   A C   
614  O O   A VAL   A 24  ? 0.2152 0.2241 0.2075 -0.0162 0.0307  0.0003  24  VAL   A O   
615  O O   B VAL   A 24  ? 0.2188 0.2298 0.2169 -0.0385 0.0492  -0.0067 24  VAL   A O   
616  C CB  A VAL   A 24  ? 0.2100 0.2036 0.2118 -0.0084 0.0516  -0.0074 24  VAL   A CB  
617  C CB  B VAL   A 24  ? 0.2072 0.2011 0.2264 -0.0428 0.0421  0.0082  24  VAL   A CB  
618  C CG1 A VAL   A 24  ? 0.2169 0.2141 0.2202 -0.0039 0.0590  -0.0197 24  VAL   A CG1 
619  C CG1 B VAL   A 24  ? 0.2202 0.2119 0.2491 -0.0373 0.0336  0.0074  24  VAL   A CG1 
620  C CG2 A VAL   A 24  ? 0.2196 0.2101 0.2228 -0.0068 0.0559  0.0032  24  VAL   A CG2 
621  C CG2 B VAL   A 24  ? 0.2095 0.1935 0.2315 -0.0497 0.0460  0.0124  24  VAL   A CG2 
640  N N   A GLU   A 25  ? 0.2093 0.2223 0.1961 -0.0245 0.0328  -0.0084 25  GLU   A N   
641  N N   B GLU   A 25  ? 0.2108 0.2357 0.1939 -0.0432 0.0655  -0.0174 25  GLU   A N   
642  C CA  A GLU   A 25  ? 0.2216 0.2408 0.1991 -0.0187 0.0434  -0.0124 25  GLU   A CA  
643  C CA  B GLU   A 25  ? 0.2207 0.2502 0.2045 -0.0502 0.0732  -0.0195 25  GLU   A CA  
644  C C   A GLU   A 25  ? 0.2108 0.2416 0.1712 -0.0266 0.0609  -0.0131 25  GLU   A C   
645  C C   B GLU   A 25  ? 0.2190 0.2501 0.1863 -0.0522 0.0789  -0.0243 25  GLU   A C   
646  O O   A GLU   A 25  ? 0.2193 0.2460 0.1862 -0.0263 0.0602  -0.0162 25  GLU   A O   
647  O O   B GLU   A 25  ? 0.2270 0.2545 0.1924 -0.0514 0.0736  -0.0356 25  GLU   A O   
648  C CB  A GLU   A 25  ? 0.2484 0.2706 0.2463 -0.0124 0.0337  -0.0119 25  GLU   A CB  
649  C CB  B GLU   A 25  ? 0.2333 0.2595 0.2336 -0.0549 0.0752  -0.0173 25  GLU   A CB  
650  C CG  A GLU   A 25  ? 0.2745 0.2949 0.3115 -0.0178 0.0147  -0.0208 25  GLU   A CG  
651  C CG  B GLU   A 25  ? 0.2562 0.2766 0.2932 -0.0538 0.0631  -0.0156 25  GLU   A CG  
652  C CD  A GLU   A 25  ? 0.2948 0.3156 0.3692 -0.0235 -0.0010 -0.0201 25  GLU   A CD  
653  C CD  B GLU   A 25  ? 0.2710 0.2907 0.3462 -0.0547 0.0510  -0.0142 25  GLU   A CD  
654  O OE1 A GLU   A 25  ? 0.3056 0.3261 0.3788 -0.0211 -0.0129 -0.0265 25  GLU   A OE1 
655  O OE1 B GLU   A 25  ? 0.2794 0.2955 0.3677 -0.0539 0.0445  -0.0155 25  GLU   A OE1 
656  O OE2 A GLU   A 25  ? 0.2989 0.3232 0.4061 -0.0300 -0.0036 -0.0206 25  GLU   A OE2 
657  O OE2 B GLU   A 25  ? 0.2741 0.2965 0.3678 -0.0539 0.0489  -0.0111 25  GLU   A OE2 
670  N N   A GLU   A 26  ? 0.2016 0.2437 0.1815 -0.0415 0.0627  -0.0172 26  GLU   A N   
671  N N   B GLU   A 26  ? 0.2138 0.2411 0.1842 -0.0552 0.0861  -0.0254 26  GLU   A N   
672  C CA  A GLU   A 26  ? 0.2118 0.2532 0.1720 -0.0519 0.0495  -0.0137 26  GLU   A CA  
673  C CA  B GLU   A 26  ? 0.2218 0.2336 0.1802 -0.0543 0.0831  -0.0212 26  GLU   A CA  
674  C C   A GLU   A 26  ? 0.2092 0.2442 0.1592 -0.0479 0.0451  -0.0057 26  GLU   A C   
675  C C   B GLU   A 26  ? 0.2152 0.2304 0.1595 -0.0502 0.0654  -0.0082 26  GLU   A C   
676  O O   A GLU   A 26  ? 0.2153 0.2433 0.1571 -0.0512 0.0376  -0.0078 26  GLU   A O   
677  O O   B GLU   A 26  ? 0.2205 0.2222 0.1408 -0.0510 0.0658  -0.0058 26  GLU   A O   
678  C CB  A GLU   A 26  ? 0.2314 0.2701 0.1934 -0.0558 0.0486  -0.0155 26  GLU   A CB  
679  C CB  B GLU   A 26  ? 0.2392 0.2305 0.2140 -0.0586 0.0806  -0.0322 26  GLU   A CB  
680  C CG  A GLU   A 26  ? 0.2578 0.2976 0.2634 -0.0568 0.0481  -0.0205 26  GLU   A CG  
681  C CG  B GLU   A 26  ? 0.2518 0.2191 0.2359 -0.0697 0.0986  -0.0433 26  GLU   A CG  
682  C CD  A GLU   A 26  ? 0.2730 0.3184 0.3077 -0.0617 0.0565  -0.0194 26  GLU   A CD  
683  C CD  B GLU   A 26  ? 0.2624 0.2056 0.2489 -0.0855 0.1174  -0.0574 26  GLU   A CD  
684  O OE1 A GLU   A 26  ? 0.2731 0.3288 0.3005 -0.0640 0.0595  -0.0278 26  GLU   A OE1 
685  O OE1 B GLU   A 26  ? 0.2595 0.1989 0.2660 -0.0947 0.1226  -0.0816 26  GLU   A OE1 
686  O OE2 A GLU   A 26  ? 0.2968 0.3315 0.3489 -0.0565 0.0558  -0.0124 26  GLU   A OE2 
687  O OE2 B GLU   A 26  ? 0.2749 0.2060 0.2298 -0.0793 0.1393  -0.0478 26  GLU   A OE2 
700  N N   . ALA   A 27  ? 0.1985 0.2334 0.1662 -0.0471 0.0492  0.0025  27  ALA   A N   
701  C CA  . ALA   A 27  ? 0.2066 0.2473 0.1546 -0.0406 0.0409  0.0020  27  ALA   A CA  
702  C C   . ALA   A 27  ? 0.2419 0.2726 0.1688 -0.0509 0.0499  -0.0140 27  ALA   A C   
703  O O   . ALA   A 27  ? 0.2414 0.2608 0.1780 -0.0637 0.0329  -0.0087 27  ALA   A O   
704  C CB  . ALA   A 27  ? 0.1876 0.2393 0.1604 -0.0451 0.0332  0.0071  27  ALA   A CB  
711  N N   A LYS   A 28  ? 0.2728 0.2966 0.1883 -0.0445 0.0487  -0.0382 28  LYS   A N   
712  N N   B LYS   A 28  ? 0.2743 0.2987 0.2005 -0.0442 0.0431  -0.0278 28  LYS   A N   
713  C CA  A LYS   A 28  ? 0.3091 0.3327 0.2315 -0.0322 0.0496  -0.0505 28  LYS   A CA  
714  C CA  B LYS   A 28  ? 0.3100 0.3320 0.2468 -0.0340 0.0371  -0.0344 28  LYS   A CA  
715  C C   A LYS   A 28  ? 0.3279 0.3592 0.2255 -0.0383 0.0692  -0.0348 28  LYS   A C   
716  C C   B LYS   A 28  ? 0.3313 0.3553 0.2517 -0.0372 0.0467  -0.0241 28  LYS   A C   
717  O O   A LYS   A 28  ? 0.3350 0.3674 0.2565 -0.0376 0.0576  -0.0350 28  LYS   A O   
718  O O   B LYS   A 28  ? 0.3377 0.3611 0.2699 -0.0357 0.0393  -0.0250 28  LYS   A O   
719  C CB  A LYS   A 28  ? 0.3280 0.3462 0.2930 -0.0150 0.0385  -0.0667 28  LYS   A CB  
720  C CB  B LYS   A 28  ? 0.3255 0.3440 0.2948 -0.0221 0.0263  -0.0442 28  LYS   A CB  
721  C CG  A LYS   A 28  ? 0.3472 0.3583 0.3614 -0.0014 0.0299  -0.0718 28  LYS   A CG  
722  C CG  B LYS   A 28  ? 0.3415 0.3547 0.3481 -0.0122 0.0173  -0.0480 28  LYS   A CG  
723  C CD  A LYS   A 28  ? 0.3649 0.3740 0.4359 0.0079  0.0179  -0.0715 28  LYS   A CD  
724  C CD  B LYS   A 28  ? 0.3573 0.3677 0.4075 -0.0049 0.0077  -0.0491 28  LYS   A CD  
725  C CE  A LYS   A 28  ? 0.3771 0.3852 0.4892 0.0131  0.0083  -0.0764 28  LYS   A CE  
726  C CE  B LYS   A 28  ? 0.3685 0.3768 0.4517 -0.0014 0.0004  -0.0528 28  LYS   A CE  
727  N NZ  A LYS   A 28  ? 0.3853 0.3910 0.5222 0.0172  0.0052  -0.0832 28  LYS   A NZ  
728  N NZ  B LYS   A 28  ? 0.3757 0.3817 0.4778 0.0016  -0.0034 -0.0580 28  LYS   A NZ  
755  N N   A LYS   A 29  ? 0.3377 0.3783 0.2147 -0.0481 0.0989  -0.0144 29  LYS   A N   
756  N N   B LYS   A 29  ? 0.3440 0.3728 0.2547 -0.0442 0.0649  -0.0105 29  LYS   A N   
757  C CA  A LYS   A 29  ? 0.3559 0.4022 0.2476 -0.0543 0.1108  -0.0016 29  LYS   A CA  
758  C CA  B LYS   A 29  ? 0.3598 0.3924 0.2776 -0.0501 0.0771  -0.0009 29  LYS   A CA  
759  C C   A LYS   A 29  ? 0.3578 0.3988 0.2381 -0.0668 0.0961  0.0081  29  LYS   A C   
760  C C   B LYS   A 29  ? 0.3583 0.3915 0.2515 -0.0650 0.0790  0.0083  29  LYS   A C   
761  O O   A LYS   A 29  ? 0.3677 0.4094 0.2574 -0.0623 0.0902  0.0029  29  LYS   A O   
762  O O   B LYS   A 29  ? 0.3648 0.3969 0.2633 -0.0632 0.0753  0.0062  29  LYS   A O   
763  C CB  A LYS   A 29  ? 0.3725 0.4280 0.3065 -0.0466 0.1230  0.0017  29  LYS   A CB  
764  C CB  B LYS   A 29  ? 0.3763 0.4116 0.3304 -0.0409 0.0808  0.0001  29  LYS   A CB  
765  C CG  A LYS   A 29  ? 0.3927 0.4523 0.3779 -0.0386 0.1219  0.0052  29  LYS   A CG  
766  C CG  B LYS   A 29  ? 0.3939 0.4293 0.3889 -0.0327 0.0793  0.0023  29  LYS   A CG  
767  C CD  A LYS   A 29  ? 0.4105 0.4725 0.4441 -0.0315 0.1196  0.0054  29  LYS   A CD  
768  C CD  B LYS   A 29  ? 0.4086 0.4438 0.4418 -0.0260 0.0779  0.0034  29  LYS   A CD  
769  C CE  A LYS   A 29  ? 0.4222 0.4859 0.4864 -0.0262 0.1207  0.0034  29  LYS   A CE  
770  C CE  B LYS   A 29  ? 0.4181 0.4533 0.4772 -0.0212 0.0786  0.0023  29  LYS   A CE  
771  N NZ  A LYS   A 29  ? 0.4282 0.4929 0.5141 -0.0223 0.1190  0.0018  29  LYS   A NZ  
772  N NZ  B LYS   A 29  ? 0.4229 0.4581 0.4992 -0.0182 0.0773  0.0022  29  LYS   A NZ  
799  N N   . VAL   A 30  ? 0.3485 0.3830 0.2115 -0.0811 0.0865  0.0190  30  VAL   A N   
800  C CA  . VAL   A 30  ? 0.3417 0.3618 0.1748 -0.1032 0.0599  0.0359  30  VAL   A CA  
801  C C   . VAL   A 30  ? 0.3442 0.3480 0.1419 -0.1082 0.0444  0.0388  30  VAL   A C   
802  O O   . VAL   A 30  ? 0.3576 0.3551 0.1515 -0.1060 0.0361  0.0411  30  VAL   A O   
803  C CB  . VAL   A 30  ? 0.3381 0.3532 0.2046 -0.1144 0.0363  0.0422  30  VAL   A CB  
804  C CG1 . VAL   A 30  ? 0.3420 0.3484 0.2247 -0.1146 0.0241  0.0457  30  VAL   A CG1 
805  C CG2 . VAL   A 30  ? 0.3370 0.3554 0.2192 -0.1224 0.0326  0.0417  30  VAL   A CG2 
816  N N   . LYS   A 31  ? 0.3343 0.3278 0.1313 -0.1142 0.0203  0.0277  31  LYS   A N   
817  C CA  . LYS   A 31  ? 0.3429 0.3298 0.1575 -0.0948 -0.0070 0.0272  31  LYS   A CA  
818  C C   . LYS   A 31  ? 0.3080 0.3003 0.1120 -0.0652 -0.0110 0.0586  31  LYS   A C   
819  O O   . LYS   A 31  ? 0.3130 0.3199 0.1303 -0.0630 -0.0326 0.0656  31  LYS   A O   
820  C CB  . LYS   A 31  ? 0.3963 0.3696 0.2945 -0.0982 -0.0271 0.0037  31  LYS   A CB  
821  C CG  . LYS   A 31  ? 0.4501 0.4077 0.4437 -0.0933 -0.0437 -0.0127 31  LYS   A CG  
822  C CD  . LYS   A 31  ? 0.4909 0.4373 0.5548 -0.0871 -0.0586 -0.0250 31  LYS   A CD  
823  C CE  . LYS   A 31  ? 0.5211 0.4647 0.6226 -0.0801 -0.0697 -0.0358 31  LYS   A CE  
824  N NZ  . LYS   A 31  ? 0.5358 0.4741 0.6610 -0.0744 -0.0759 -0.0423 31  LYS   A NZ  
838  N N   . PRO   A 32  ? 0.2728 0.2681 0.0932 -0.0643 -0.0039 0.0377  32  PRO   A N   
839  C CA  . PRO   A 32  ? 0.2616 0.2496 0.1291 -0.0574 -0.0128 0.0536  32  PRO   A CA  
840  C C   . PRO   A 32  ? 0.2607 0.2443 0.1432 -0.0479 -0.0157 0.0626  32  PRO   A C   
841  O O   . PRO   A 32  ? 0.2589 0.2371 0.1587 -0.0495 -0.0276 0.0519  32  PRO   A O   
842  C CB  . PRO   A 32  ? 0.2524 0.2526 0.1456 -0.0584 -0.0128 0.0410  32  PRO   A CB  
843  C CG  . PRO   A 32  ? 0.2488 0.2570 0.0905 -0.0530 -0.0255 0.0242  32  PRO   A CG  
844  C CD  . PRO   A 32  ? 0.2516 0.2595 0.0828 -0.0564 -0.0087 0.0262  32  PRO   A CD  
852  N N   . THR   A 33  ? 0.2607 0.2423 0.1340 -0.0429 -0.0116 0.0575  33  THR   A N   
853  C CA  . THR   A 33  ? 0.2569 0.2474 0.1441 -0.0361 -0.0330 0.0536  33  THR   A CA  
854  C C   . THR   A 33  ? 0.2312 0.2316 0.1421 -0.0403 -0.0324 0.0389  33  THR   A C   
855  O O   . THR   A 33  ? 0.2259 0.2371 0.1522 -0.0467 -0.0468 0.0461  33  THR   A O   
856  C CB  . THR   A 33  ? 0.2823 0.2694 0.1649 -0.0262 -0.0379 0.0726  33  THR   A CB  
857  O OG1 . THR   A 33  ? 0.3121 0.2803 0.1939 -0.0100 -0.0267 0.0836  33  THR   A OG1 
858  C CG2 . THR   A 33  ? 0.2873 0.2826 0.1774 -0.0210 -0.0402 0.0701  33  THR   A CG2 
866  N N   . VAL   A 34  ? 0.2045 0.2071 0.1241 -0.0415 -0.0210 0.0372  34  VAL   A N   
867  C CA  . VAL   A 34  ? 0.1841 0.1918 0.1216 -0.0337 -0.0172 0.0297  34  VAL   A CA  
868  C C   . VAL   A 34  ? 0.1746 0.1792 0.1244 -0.0293 -0.0036 0.0223  34  VAL   A C   
869  O O   . VAL   A 34  ? 0.1739 0.1822 0.1524 -0.0371 -0.0067 0.0355  34  VAL   A O   
870  C CB  . VAL   A 34  ? 0.1912 0.1906 0.1433 -0.0286 -0.0046 0.0173  34  VAL   A CB  
871  C CG1 . VAL   A 34  ? 0.1959 0.1890 0.1454 -0.0273 0.0076  0.0116  34  VAL   A CG1 
872  C CG2 . VAL   A 34  ? 0.1987 0.2057 0.1820 -0.0233 -0.0121 0.0207  34  VAL   A CG2 
882  N N   . VAL   A 35  ? 0.1633 0.1634 0.1189 -0.0299 -0.0093 0.0262  35  VAL   A N   
883  C CA  . VAL   A 35  ? 0.1563 0.1642 0.1154 -0.0224 -0.0084 0.0236  35  VAL   A CA  
884  C C   . VAL   A 35  ? 0.1497 0.1507 0.1067 -0.0162 -0.0022 0.0173  35  VAL   A C   
885  O O   . VAL   A 35  ? 0.1332 0.1596 0.1459 -0.0224 0.0119  0.0152  35  VAL   A O   
886  C CB  . VAL   A 35  ? 0.1575 0.1719 0.1405 -0.0130 0.0096  0.0133  35  VAL   A CB  
887  C CG1 . VAL   A 35  ? 0.1711 0.1791 0.1342 -0.0083 0.0015  0.0086  35  VAL   A CG1 
888  C CG2 . VAL   A 35  ? 0.1554 0.1679 0.1650 -0.0145 0.0122  0.0056  35  VAL   A CG2 
898  N N   . VAL   A 36  ? 0.1377 0.1467 0.1100 -0.0169 0.0017  0.0203  36  VAL   A N   
899  C CA  . VAL   A 36  ? 0.1307 0.1368 0.1195 -0.0118 0.0030  0.0131  36  VAL   A CA  
900  C C   . VAL   A 36  ? 0.1282 0.1398 0.1271 -0.0179 0.0063  0.0131  36  VAL   A C   
901  O O   . VAL   A 36  ? 0.1312 0.1377 0.1542 -0.0087 0.0172  0.0152  36  VAL   A O   
902  C CB  . VAL   A 36  ? 0.1326 0.1284 0.1332 -0.0094 -0.0007 0.0119  36  VAL   A CB  
903  C CG1 . VAL   A 36  ? 0.1384 0.1322 0.1422 -0.0131 0.0054  0.0001  36  VAL   A CG1 
904  C CG2 . VAL   A 36  ? 0.1412 0.1395 0.1444 -0.0121 -0.0022 0.0212  36  VAL   A CG2 
914  N N   . ASN   A 37  ? 0.1247 0.1315 0.1260 -0.0078 0.0066  0.0134  37  ASN   A N   
915  C CA  . ASN   A 37  ? 0.1217 0.1241 0.1241 0.0005  0.0035  0.0205  37  ASN   A CA  
916  C C   . ASN   A 37  ? 0.1200 0.1241 0.1163 -0.0026 0.0079  0.0281  37  ASN   A C   
917  O O   . ASN   A 37  ? 0.1332 0.1384 0.1279 0.0048  0.0106  0.0131  37  ASN   A O   
918  C CB  . ASN   A 37  ? 0.1279 0.1270 0.1378 0.0001  0.0046  0.0153  37  ASN   A CB  
919  C CG  . ASN   A 37  ? 0.1265 0.1291 0.1415 -0.0002 0.0055  0.0079  37  ASN   A CG  
920  O OD1 . ASN   A 37  ? 0.1256 0.1312 0.1663 0.0001  0.0070  0.0152  37  ASN   A OD1 
921  N ND2 . ASN   A 37  ? 0.1265 0.1302 0.1468 -0.0028 0.0016  0.0240  37  ASN   A ND2 
928  N N   A ALA   A 38  ? 0.1195 0.1353 0.1280 0.0004  0.0132  0.0127  38  ALA   A N   
929  N N   B ALA   A 38  ? 0.1237 0.1374 0.1278 -0.0024 0.0029  0.0202  38  ALA   A N   
930  C CA  A ALA   A 38  ? 0.1248 0.1345 0.1153 -0.0026 0.0112  0.0020  38  ALA   A CA  
931  C CA  B ALA   A 38  ? 0.1318 0.1458 0.1316 -0.0046 -0.0074 0.0257  38  ALA   A CA  
932  C C   A ALA   A 38  ? 0.1256 0.1340 0.1259 -0.0004 0.0033  0.0026  38  ALA   A C   
933  C C   B ALA   A 38  ? 0.1315 0.1442 0.1354 -0.0017 -0.0089 0.0157  38  ALA   A C   
934  O O   A ALA   A 38  ? 0.1214 0.1237 0.1346 -0.0033 -0.0123 -0.0011 38  ALA   A O   
935  O O   B ALA   A 38  ? 0.1237 0.1354 0.1471 -0.0053 -0.0156 0.0159  38  ALA   A O   
936  C CB  A ALA   A 38  ? 0.1253 0.1488 0.1159 -0.0156 0.0041  -0.0016 38  ALA   A CB  
937  C CB  B ALA   A 38  ? 0.1378 0.1500 0.1432 -0.0130 -0.0123 0.0190  38  ALA   A CB  
948  N N   A ALA   A 39  ? 0.1253 0.1258 0.1268 -0.0008 0.0075  0.0078  39  ALA   A N   
949  N N   B ALA   A 39  ? 0.1368 0.1457 0.1385 -0.0001 -0.0059 0.0183  39  ALA   A N   
950  C CA  A ALA   A 39  ? 0.1191 0.1201 0.1241 0.0024  0.0088  0.0056  39  ALA   A CA  
951  C CA  B ALA   A 39  ? 0.1378 0.1462 0.1343 -0.0033 -0.0141 0.0154  39  ALA   A CA  
952  C C   A ALA   A 39  ? 0.1221 0.1246 0.1270 0.0002  0.0002  0.0041  39  ALA   A C   
953  C C   B ALA   A 39  ? 0.1350 0.1380 0.1333 -0.0022 -0.0088 0.0118  39  ALA   A C   
954  O O   A ALA   A 39  ? 0.1354 0.1304 0.1329 -0.0094 0.0152  0.0099  39  ALA   A O   
955  O O   B ALA   A 39  ? 0.1504 0.1386 0.1418 -0.0058 -0.0061 0.0055  39  ALA   A O   
956  C CB  A ALA   A 39  ? 0.1200 0.1248 0.1418 0.0100  0.0004  -0.0082 39  ALA   A CB  
957  C CB  B ALA   A 39  ? 0.1499 0.1580 0.1484 -0.0029 -0.0172 0.0122  39  ALA   A CB  
968  N N   A ASN   A 40  ? 0.1250 0.1285 0.1295 -0.0068 0.0028  0.0070  40  ASN   A N   
969  N N   B ASN   A 40  ? 0.1384 0.1353 0.1281 -0.0036 0.0022  0.0122  40  ASN   A N   
970  C CA  A ASN   A 40  ? 0.1282 0.1290 0.1264 -0.0012 -0.0003 0.0031  40  ASN   A CA  
971  C CA  B ASN   A 40  ? 0.1379 0.1301 0.1283 -0.0015 -0.0079 0.0124  40  ASN   A CA  
972  C C   A ASN   A 40  ? 0.1300 0.1207 0.1145 -0.0045 0.0040  0.0113  40  ASN   A C   
973  C C   B ASN   A 40  ? 0.1336 0.1255 0.1252 -0.0055 0.0048  0.0178  40  ASN   A C   
974  O O   A ASN   A 40  ? 0.1271 0.1175 0.1271 -0.0030 0.0072  0.0112  40  ASN   A O   
975  O O   B ASN   A 40  ? 0.1281 0.1300 0.1424 -0.0053 0.0072  0.0224  40  ASN   A O   
976  C CB  A ASN   A 40  ? 0.1348 0.1359 0.1514 -0.0008 -0.0018 0.0072  40  ASN   A CB  
977  C CB  B ASN   A 40  ? 0.1427 0.1300 0.1469 0.0043  -0.0118 0.0176  40  ASN   A CB  
978  C CG  A ASN   A 40  ? 0.1440 0.1411 0.1814 -0.0004 0.0000  0.0118  40  ASN   A CG  
979  C CG  B ASN   A 40  ? 0.1471 0.1352 0.1569 0.0031  -0.0181 0.0177  40  ASN   A CG  
980  O OD1 A ASN   A 40  ? 0.1536 0.1376 0.1884 0.0035  -0.0087 0.0175  40  ASN   A OD1 
981  O OD1 B ASN   A 40  ? 0.1532 0.1399 0.1725 0.0007  -0.0232 0.0042  40  ASN   A OD1 
982  N ND2 A ASN   A 40  ? 0.1505 0.1553 0.2068 -0.0001 0.0116  -0.0028 40  ASN   A ND2 
983  N ND2 B ASN   A 40  ? 0.1480 0.1414 0.1647 -0.0026 0.0022  0.0087  40  ASN   A ND2 
996  N N   A VAL   A 41  ? 0.1309 0.1333 0.1215 -0.0005 0.0079  0.0189  41  VAL   A N   
997  N N   B VAL   A 41  ? 0.1361 0.1265 0.1212 -0.0025 0.0092  0.0203  41  VAL   A N   
998  C CA  A VAL   A 41  ? 0.1328 0.1364 0.1365 -0.0040 0.0109  0.0146  41  VAL   A CA  
999  C CA  B VAL   A 41  ? 0.1377 0.1333 0.1362 -0.0017 0.0189  0.0163  41  VAL   A CA  
1000 C C   A VAL   A 41  ? 0.1298 0.1312 0.1488 0.0082  0.0094  0.0153  41  VAL   A C   
1001 C C   B VAL   A 41  ? 0.1397 0.1378 0.1413 -0.0040 0.0202  0.0156  41  VAL   A C   
1002 O O   A VAL   A 41  ? 0.1315 0.1278 0.1523 0.0084  0.0022  0.0098  41  VAL   A O   
1003 O O   B VAL   A 41  ? 0.1448 0.1351 0.1359 -0.0060 -0.0020 0.0059  41  VAL   A O   
1004 C CB  A VAL   A 41  ? 0.1371 0.1406 0.1292 -0.0056 0.0142  0.0157  41  VAL   A CB  
1005 C CB  B VAL   A 41  ? 0.1517 0.1444 0.1575 0.0011  0.0224  0.0141  41  VAL   A CB  
1006 C CG1 A VAL   A 41  ? 0.1466 0.1499 0.1326 -0.0023 0.0062  0.0131  41  VAL   A CG1 
1007 C CG1 B VAL   A 41  ? 0.1705 0.1507 0.1680 -0.0050 0.0292  0.0039  41  VAL   A CG1 
1008 C CG2 A VAL   A 41  ? 0.1373 0.1406 0.1174 -0.0055 0.0281  0.0105  41  VAL   A CG2 
1009 C CG2 B VAL   A 41  ? 0.1512 0.1513 0.1679 0.0035  0.0164  0.0151  41  VAL   A CG2 
1028 N N   A TYR   A 42  ? 0.1202 0.1246 0.1635 0.0024  0.0216  0.0262  42  TYR   A N   
1029 N N   B TYR   A 42  ? 0.1317 0.1374 0.1496 0.0006  0.0323  0.0238  42  TYR   A N   
1030 C CA  A TYR   A 42  ? 0.1327 0.1250 0.1669 -0.0052 0.0150  0.0236  42  TYR   A CA  
1031 C CA  B TYR   A 42  ? 0.1317 0.1315 0.1488 0.0037  0.0334  0.0264  42  TYR   A CA  
1032 C C   A TYR   A 42  ? 0.1329 0.1246 0.1605 -0.0037 0.0142  0.0230  42  TYR   A C   
1033 C C   B TYR   A 42  ? 0.1405 0.1312 0.1488 -0.0021 0.0208  0.0280  42  TYR   A C   
1034 O O   A TYR   A 42  ? 0.1355 0.1324 0.1723 -0.0145 0.0144  0.0044  42  TYR   A O   
1035 O O   B TYR   A 42  ? 0.1421 0.1354 0.1601 -0.0094 0.0215  0.0228  42  TYR   A O   
1036 C CB  A TYR   A 42  ? 0.1413 0.1364 0.1639 0.0009  0.0225  0.0215  42  TYR   A CB  
1037 C CB  B TYR   A 42  ? 0.1333 0.1317 0.1436 0.0013  0.0252  0.0374  42  TYR   A CB  
1038 C CG  A TYR   A 42  ? 0.1446 0.1480 0.1544 0.0034  0.0130  0.0309  42  TYR   A CG  
1039 C CG  B TYR   A 42  ? 0.1394 0.1424 0.1393 0.0061  0.0067  0.0421  42  TYR   A CG  
1040 C CD1 A TYR   A 42  ? 0.1459 0.1562 0.1631 -0.0013 0.0168  0.0251  42  TYR   A CD1 
1041 C CD1 B TYR   A 42  ? 0.1397 0.1481 0.1414 -0.0006 0.0112  0.0455  42  TYR   A CD1 
1042 C CD2 A TYR   A 42  ? 0.1477 0.1645 0.1766 0.0126  0.0088  0.0228  42  TYR   A CD2 
1043 C CD2 B TYR   A 42  ? 0.1476 0.1593 0.1582 0.0130  0.0054  0.0340  42  TYR   A CD2 
1044 C CE1 A TYR   A 42  ? 0.1510 0.1660 0.1651 0.0008  0.0205  0.0168  42  TYR   A CE1 
1045 C CE1 B TYR   A 42  ? 0.1410 0.1585 0.1461 0.0030  0.0121  0.0437  42  TYR   A CE1 
1046 C CE2 A TYR   A 42  ? 0.1507 0.1721 0.1838 0.0027  0.0079  0.0184  42  TYR   A CE2 
1047 C CE2 B TYR   A 42  ? 0.1514 0.1711 0.1662 0.0139  0.0086  0.0339  42  TYR   A CE2 
1048 C CZ  A TYR   A 42  ? 0.1602 0.1757 0.1751 0.0003  0.0132  0.0187  42  TYR   A CZ  
1049 C CZ  B TYR   A 42  ? 0.1489 0.1730 0.1648 0.0090  0.0146  0.0329  42  TYR   A CZ  
1050 O OH  A TYR   A 42  ? 0.1693 0.1895 0.1918 -0.0038 0.0073  0.0135  42  TYR   A OH  
1051 O OH  B TYR   A 42  ? 0.1508 0.1909 0.1814 0.0046  0.0194  0.0241  42  TYR   A OH  
1070 N N   . LEU   A 43  ? 0.1391 0.1248 0.1507 -0.0064 0.0143  0.0062  43  LEU   A N   
1071 C CA  . LEU   A 43  ? 0.1334 0.1257 0.1447 -0.0098 0.0064  0.0052  43  LEU   A CA  
1072 C C   . LEU   A 43  ? 0.1319 0.1339 0.1432 -0.0037 0.0067  0.0056  43  LEU   A C   
1073 O O   . LEU   A 43  ? 0.1509 0.1364 0.1626 -0.0005 -0.0001 0.0093  43  LEU   A O   
1074 C CB  . LEU   A 43  ? 0.1382 0.1264 0.1684 -0.0102 0.0128  0.0087  43  LEU   A CB  
1075 C CG  . LEU   A 43  ? 0.1399 0.1300 0.1637 -0.0070 0.0091  0.0088  43  LEU   A CG  
1076 C CD1 . LEU   A 43  ? 0.1476 0.1382 0.1809 -0.0029 0.0003  0.0152  43  LEU   A CD1 
1077 C CD2 . LEU   A 43  ? 0.1574 0.1323 0.1771 -0.0030 0.0037  0.0147  43  LEU   A CD2 
1090 N N   A LYS   A 44  ? 0.1391 0.1287 0.1451 -0.0019 0.0046  0.0106  44  LYS   A N   
1091 N N   B LYS   A 44  ? 0.1433 0.1350 0.1480 -0.0027 0.0074  0.0101  44  LYS   A N   
1092 C CA  A LYS   A 44  ? 0.1490 0.1318 0.1499 -0.0039 0.0058  0.0154  44  LYS   A CA  
1093 C CA  B LYS   A 44  ? 0.1542 0.1414 0.1587 -0.0035 0.0091  0.0136  44  LYS   A CA  
1094 C C   A LYS   A 44  ? 0.1412 0.1325 0.1369 0.0044  -0.0011 0.0132  44  LYS   A C   
1095 C C   B LYS   A 44  ? 0.1403 0.1368 0.1413 -0.0027 0.0049  0.0117  44  LYS   A C   
1096 O O   A LYS   A 44  ? 0.1558 0.1468 0.1633 0.0097  -0.0027 0.0015  44  LYS   A O   
1097 O O   B LYS   A 44  ? 0.1429 0.1414 0.1427 -0.0083 0.0086  0.0110  44  LYS   A O   
1098 C CB  A LYS   A 44  ? 0.1723 0.1505 0.1898 -0.0045 0.0162  0.0250  44  LYS   A CB  
1099 C CB  B LYS   A 44  ? 0.1818 0.1623 0.2031 0.0006  0.0181  0.0190  44  LYS   A CB  
1100 C CG  A LYS   A 44  ? 0.2040 0.1750 0.2616 -0.0153 0.0339  0.0286  44  LYS   A CG  
1101 C CG  B LYS   A 44  ? 0.2088 0.1921 0.2704 -0.0002 0.0268  0.0239  44  LYS   A CG  
1102 C CD  A LYS   A 44  ? 0.2438 0.2210 0.3564 -0.0211 0.0332  0.0237  44  LYS   A CD  
1103 C CD  B LYS   A 44  ? 0.2397 0.2320 0.3441 -0.0063 0.0204  0.0255  44  LYS   A CD  
1104 C CE  A LYS   A 44  ? 0.2650 0.2522 0.4140 -0.0197 0.0331  0.0233  44  LYS   A CE  
1105 C CE  B LYS   A 44  ? 0.2535 0.2569 0.3898 -0.0121 0.0171  0.0297  44  LYS   A CE  
1106 N NZ  A LYS   A 44  ? 0.2748 0.2737 0.4423 -0.0202 0.0294  0.0245  44  LYS   A NZ  
1107 N NZ  B LYS   A 44  ? 0.2648 0.2748 0.4180 -0.0195 0.0148  0.0309  44  LYS   A NZ  
1134 N N   . HIS   A 45  ? 0.1277 0.1302 0.1478 0.0008  0.0045  0.0132  45  HIS   A N   
1135 C CA  . HIS   A 45  ? 0.1303 0.1266 0.1463 0.0023  -0.0017 0.0128  45  HIS   A CA  
1136 C C   . HIS   A 45  ? 0.1433 0.1417 0.1678 0.0006  0.0002  0.0120  45  HIS   A C   
1137 O O   . HIS   A 45  ? 0.1610 0.1550 0.2070 0.0202  -0.0063 -0.0015 45  HIS   A O   
1138 C CB  . HIS   A 45  ? 0.1322 0.1293 0.1420 -0.0039 0.0060  0.0054  45  HIS   A CB  
1139 C CG  . HIS   A 45  ? 0.1271 0.1262 0.1376 -0.0076 0.0053  0.0125  45  HIS   A CG  
1140 N ND1 . HIS   A 45  ? 0.1227 0.1356 0.1576 -0.0075 0.0027  0.0138  45  HIS   A ND1 
1141 C CD2 . HIS   A 45  ? 0.1288 0.1334 0.1326 -0.0114 -0.0065 0.0175  45  HIS   A CD2 
1142 C CE1 . HIS   A 45  ? 0.1258 0.1397 0.1388 -0.0062 -0.0016 0.0134  45  HIS   A CE1 
1143 N NE2 . HIS   A 45  ? 0.1307 0.1445 0.1389 -0.0057 -0.0012 0.0204  45  HIS   A NE2 
1152 N N   . GLY   A 46  ? 0.1570 0.1477 0.1765 0.0139  -0.0146 0.0228  46  GLY   A N   
1153 C CA  . GLY   A 46  ? 0.1565 0.1679 0.1918 0.0178  -0.0161 0.0228  46  GLY   A CA  
1154 C C   . GLY   A 46  ? 0.1602 0.1585 0.1926 0.0262  -0.0190 0.0300  46  GLY   A C   
1155 O O   . GLY   A 46  ? 0.1600 0.1655 0.2443 0.0253  -0.0306 0.0137  46  GLY   A O   
1159 N N   A GLY   A 47  ? 0.1675 0.1550 0.1786 0.0243  -0.0139 0.0262  47  GLY   A N   
1160 N N   B GLY   A 47  ? 0.1590 0.1603 0.1767 0.0192  -0.0135 0.0228  47  GLY   A N   
1161 C CA  A GLY   A 47  ? 0.1697 0.1559 0.1740 0.0317  -0.0317 0.0102  47  GLY   A CA  
1162 C CA  B GLY   A 47  ? 0.1552 0.1625 0.1692 0.0171  -0.0255 0.0108  47  GLY   A CA  
1163 C C   A GLY   A 47  ? 0.1670 0.1505 0.1629 0.0323  -0.0396 -0.0010 47  GLY   A C   
1164 C C   B GLY   A 47  ? 0.1478 0.1539 0.1445 0.0163  -0.0238 -0.0038 47  GLY   A C   
1165 O O   A GLY   A 47  ? 0.1699 0.1438 0.1874 0.0364  -0.0346 0.0128  47  GLY   A O   
1166 O O   B GLY   A 47  ? 0.1439 0.1523 0.1459 0.0203  -0.0110 0.0100  47  GLY   A O   
1173 N N   A GLY   A 48  ? 0.1593 0.1520 0.1464 0.0311  -0.0427 -0.0107 48  GLY   A N   
1174 N N   B GLY   A 48  ? 0.1481 0.1514 0.1508 0.0134  -0.0193 -0.0110 48  GLY   A N   
1175 C CA  A GLY   A 48  ? 0.1552 0.1435 0.1586 0.0184  -0.0311 -0.0248 48  GLY   A CA  
1176 C CA  B GLY   A 48  ? 0.1458 0.1442 0.1545 0.0090  -0.0078 -0.0110 48  GLY   A CA  
1177 C C   A GLY   A 48  ? 0.1457 0.1385 0.1551 0.0091  -0.0143 -0.0118 48  GLY   A C   
1178 C C   B GLY   A 48  ? 0.1350 0.1423 0.1473 0.0009  0.0082  -0.0060 48  GLY   A C   
1179 O O   A GLY   A 48  ? 0.1575 0.1366 0.1531 0.0153  -0.0149 0.0019  48  GLY   A O   
1180 O O   B GLY   A 48  ? 0.1418 0.1466 0.1459 0.0000  0.0109  -0.0062 48  GLY   A O   
1187 N N   A VAL   A 49  ? 0.1334 0.1369 0.1731 0.0014  -0.0139 -0.0052 49  VAL   A N   
1188 N N   B VAL   A 49  ? 0.1244 0.1389 0.1566 -0.0049 0.0025  -0.0080 49  VAL   A N   
1189 C CA  A VAL   A 49  ? 0.1366 0.1348 0.1717 -0.0062 0.0095  0.0009  49  VAL   A CA  
1190 C CA  B VAL   A 49  ? 0.1202 0.1406 0.1552 -0.0056 0.0114  0.0029  49  VAL   A CA  
1191 C C   A VAL   A 49  ? 0.1363 0.1241 0.1485 -0.0001 0.0092  0.0102  49  VAL   A C   
1192 C C   B VAL   A 49  ? 0.1242 0.1284 0.1336 0.0018  0.0101  -0.0010 49  VAL   A C   
1193 O O   A VAL   A 49  ? 0.1360 0.1320 0.1449 -0.0061 0.0115  0.0062  49  VAL   A O   
1194 O O   B VAL   A 49  ? 0.1292 0.1241 0.1356 0.0053  0.0133  0.0072  49  VAL   A O   
1195 C CB  A VAL   A 49  ? 0.1493 0.1360 0.1865 -0.0076 0.0138  -0.0042 49  VAL   A CB  
1196 C CB  B VAL   A 49  ? 0.1093 0.1388 0.1596 0.0007  0.0137  0.0053  49  VAL   A CB  
1197 C CG1 A VAL   A 49  ? 0.1563 0.1261 0.1920 0.0024  0.0229  -0.0021 49  VAL   A CG1 
1198 C CG1 B VAL   A 49  ? 0.1011 0.1356 0.1650 0.0123  0.0149  0.0192  49  VAL   A CG1 
1199 C CG2 A VAL   A 49  ? 0.1576 0.1448 0.2256 -0.0209 0.0147  -0.0014 49  VAL   A CG2 
1200 C CG2 B VAL   A 49  ? 0.1133 0.1442 0.1831 -0.0052 0.0195  0.0095  49  VAL   A CG2 
1219 N N   A ALA   A 50  ? 0.1273 0.1236 0.1368 -0.0055 -0.0117 0.0134  50  ALA   A N   
1220 N N   B ALA   A 50  ? 0.1229 0.1243 0.1295 0.0044  0.0028  -0.0001 50  ALA   A N   
1221 C CA  A ALA   A 50  ? 0.1208 0.1265 0.1364 -0.0099 -0.0046 0.0116  50  ALA   A CA  
1222 C CA  B ALA   A 50  ? 0.1246 0.1262 0.1336 0.0006  -0.0026 0.0009  50  ALA   A CA  
1223 C C   A ALA   A 50  ? 0.1229 0.1298 0.1365 -0.0063 -0.0034 0.0105  50  ALA   A C   
1224 C C   B ALA   A 50  ? 0.1287 0.1297 0.1228 0.0004  -0.0073 -0.0025 50  ALA   A C   
1225 O O   A ALA   A 50  ? 0.1240 0.1315 0.1397 -0.0009 -0.0022 0.0078  50  ALA   A O   
1226 O O   B ALA   A 50  ? 0.1294 0.1305 0.1189 0.0009  -0.0003 -0.0056 50  ALA   A O   
1227 C CB  A ALA   A 50  ? 0.1202 0.1328 0.1220 -0.0108 -0.0048 -0.0024 50  ALA   A CB  
1228 C CB  B ALA   A 50  ? 0.1237 0.1219 0.1339 0.0092  0.0017  -0.0008 50  ALA   A CB  
1239 N N   A GLY   A 51  ? 0.1251 0.1232 0.1476 -0.0018 -0.0068 0.0123  51  GLY   A N   
1240 N N   B GLY   A 51  ? 0.1316 0.1292 0.1337 0.0009  -0.0131 -0.0022 51  GLY   A N   
1241 C CA  A GLY   A 51  ? 0.1420 0.1209 0.1502 0.0018  -0.0184 0.0133  51  GLY   A CA  
1242 C CA  B GLY   A 51  ? 0.1432 0.1293 0.1402 0.0002  -0.0167 -0.0030 51  GLY   A CA  
1243 C C   A GLY   A 51  ? 0.1286 0.1304 0.1577 0.0025  -0.0098 0.0018  51  GLY   A C   
1244 C C   B GLY   A 51  ? 0.1333 0.1360 0.1511 -0.0004 -0.0080 -0.0080 51  GLY   A C   
1245 O O   A GLY   A 51  ? 0.1305 0.1411 0.1712 0.0008  -0.0061 -0.0029 51  GLY   A O   
1246 O O   B GLY   A 51  ? 0.1342 0.1420 0.1592 -0.0006 -0.0041 -0.0156 51  GLY   A O   
1253 N N   . ALA   A 52  ? 0.1267 0.1407 0.1566 -0.0015 -0.0033 -0.0143 52  ALA   A N   
1254 C CA  . ALA   A 52  ? 0.1305 0.1524 0.1643 -0.0046 0.0053  -0.0169 52  ALA   A CA  
1255 C C   . ALA   A 52  ? 0.1270 0.1514 0.1430 -0.0108 0.0028  -0.0057 52  ALA   A C   
1256 O O   . ALA   A 52  ? 0.1351 0.1616 0.1675 -0.0070 0.0068  -0.0130 52  ALA   A O   
1257 C CB  . ALA   A 52  ? 0.1348 0.1812 0.1814 -0.0113 0.0003  -0.0059 52  ALA   A CB  
1264 N N   A LEU   A 53  ? 0.1245 0.1455 0.1342 -0.0081 0.0042  0.0014  53  LEU   A N   
1265 N N   B LEU   A 53  ? 0.1278 0.1491 0.1410 -0.0067 0.0010  -0.0000 53  LEU   A N   
1266 C CA  A LEU   A 53  ? 0.1384 0.1480 0.1204 -0.0066 0.0066  0.0062  53  LEU   A CA  
1267 C CA  B LEU   A 53  ? 0.1393 0.1487 0.1369 -0.0063 -0.0011 0.0017  53  LEU   A CA  
1268 C C   A LEU   A 53  ? 0.1381 0.1528 0.0885 0.0057  0.0121  0.0056  53  LEU   A C   
1269 C C   B LEU   A 53  ? 0.1446 0.1514 0.1318 -0.0005 -0.0022 -0.0036 53  LEU   A C   
1270 O O   A LEU   A 53  ? 0.1477 0.1578 0.1088 -0.0088 0.0101  0.0085  53  LEU   A O   
1271 O O   B LEU   A 53  ? 0.1555 0.1558 0.1491 -0.0109 -0.0026 -0.0084 53  LEU   A O   
1272 C CB  A LEU   A 53  ? 0.1455 0.1493 0.1347 -0.0042 0.0006  0.0123  53  LEU   A CB  
1273 C CB  B LEU   A 53  ? 0.1395 0.1439 0.1392 -0.0056 -0.0025 0.0059  53  LEU   A CB  
1274 C CG  A LEU   A 53  ? 0.1496 0.1510 0.1511 -0.0009 -0.0005 0.0135  53  LEU   A CG  
1275 C CG  B LEU   A 53  ? 0.1360 0.1388 0.1283 -0.0061 -0.0105 0.0090  53  LEU   A CG  
1276 C CD1 A LEU   A 53  ? 0.1479 0.1605 0.1578 0.0063  -0.0057 0.0234  53  LEU   A CD1 
1277 C CD1 B LEU   A 53  ? 0.1356 0.1428 0.1318 -0.0052 -0.0004 0.0031  53  LEU   A CD1 
1278 C CD2 A LEU   A 53  ? 0.1608 0.1707 0.1636 0.0015  -0.0004 0.0178  53  LEU   A CD2 
1279 C CD2 B LEU   A 53  ? 0.1297 0.1407 0.1164 0.0001  -0.0023 0.0046  53  LEU   A CD2 
1302 N N   A ASN   A 54  ? 0.1291 0.1469 0.1047 -0.0012 0.0080  0.0080  54  ASN   A N   
1303 N N   B ASN   A 54  ? 0.1371 0.1418 0.1373 -0.0054 -0.0055 -0.0004 54  ASN   A N   
1304 C CA  A ASN   A 54  ? 0.1168 0.1434 0.1276 -0.0006 -0.0016 0.0014  54  ASN   A CA  
1305 C CA  B ASN   A 54  ? 0.1296 0.1347 0.1435 -0.0091 -0.0133 -0.0006 54  ASN   A CA  
1306 C C   A ASN   A 54  ? 0.1300 0.1449 0.1362 -0.0055 0.0006  -0.0022 54  ASN   A C   
1307 C C   B ASN   A 54  ? 0.1355 0.1393 0.1431 -0.0096 -0.0072 -0.0047 54  ASN   A C   
1308 O O   A ASN   A 54  ? 0.1341 0.1540 0.1458 -0.0001 0.0002  -0.0115 54  ASN   A O   
1309 O O   B ASN   A 54  ? 0.1392 0.1440 0.1486 -0.0080 -0.0091 -0.0118 54  ASN   A O   
1310 C CB  A ASN   A 54  ? 0.1171 0.1424 0.1355 0.0033  -0.0003 0.0025  54  ASN   A CB  
1311 C CB  B ASN   A 54  ? 0.1309 0.1292 0.1471 -0.0120 -0.0152 0.0036  54  ASN   A CB  
1312 C CG  A ASN   A 54  ? 0.1137 0.1368 0.1506 0.0104  0.0072  -0.0016 54  ASN   A CG  
1313 C CG  B ASN   A 54  ? 0.1287 0.1221 0.1499 -0.0131 -0.0149 0.0128  54  ASN   A CG  
1314 O OD1 A ASN   A 54  ? 0.1133 0.1426 0.1588 0.0078  0.0026  -0.0010 54  ASN   A OD1 
1315 O OD1 B ASN   A 54  ? 0.1294 0.1187 0.1469 -0.0109 -0.0214 0.0280  54  ASN   A OD1 
1316 N ND2 A ASN   A 54  ? 0.1220 0.1365 0.1666 0.0092  -0.0014 0.0054  54  ASN   A ND2 
1317 N ND2 B ASN   A 54  ? 0.1216 0.1257 0.1545 -0.0098 -0.0209 0.0169  54  ASN   A ND2 
1330 N N   . LYS   A 55  ? 0.1346 0.1451 0.1528 -0.0018 -0.0033 -0.0109 55  LYS   A N   
1331 C CA  . LYS   A 55  ? 0.1450 0.1556 0.1589 0.0045  -0.0070 -0.0162 55  LYS   A CA  
1332 C C   . LYS   A 55  ? 0.1362 0.1621 0.1554 -0.0017 -0.0059 -0.0205 55  LYS   A C   
1333 O O   . LYS   A 55  ? 0.1500 0.1756 0.1663 -0.0020 -0.0009 -0.0241 55  LYS   A O   
1334 C CB  . LYS   A 55  ? 0.1522 0.1586 0.1854 0.0177  -0.0082 -0.0227 55  LYS   A CB  
1335 C CG  . LYS   A 55  ? 0.1728 0.1947 0.2035 0.0314  -0.0236 -0.0338 55  LYS   A CG  
1336 C CD  . LYS   A 55  ? 0.1847 0.2328 0.2173 0.0475  -0.0200 -0.0337 55  LYS   A CD  
1337 C CE  . LYS   A 55  ? 0.2042 0.2776 0.2435 0.0603  -0.0327 -0.0481 55  LYS   A CE  
1338 N NZ  . LYS   A 55  ? 0.2111 0.2938 0.2458 0.0750  -0.0420 -0.0562 55  LYS   A NZ  
1353 N N   . ALA   A 56  ? 0.1405 0.1701 0.1625 -0.0114 0.0018  -0.0244 56  ALA   A N   
1354 C CA  . ALA   A 56  ? 0.1515 0.1950 0.1485 -0.0134 0.0158  -0.0217 56  ALA   A CA  
1355 C C   . ALA   A 56  ? 0.1556 0.2020 0.1361 -0.0115 0.0178  -0.0267 56  ALA   A C   
1356 O O   . ALA   A 56  ? 0.1614 0.2304 0.1482 0.0031  0.0206  -0.0164 56  ALA   A O   
1357 C CB  . ALA   A 56  ? 0.1609 0.2146 0.1569 -0.0199 0.0144  -0.0086 56  ALA   A CB  
1363 N N   . THR   A 57  ? 0.1432 0.1794 0.1391 -0.0148 0.0121  -0.0158 57  THR   A N   
1364 C CA  . THR   A 57  ? 0.1538 0.1761 0.1325 -0.0096 0.0022  -0.0110 57  THR   A CA  
1365 C C   . THR   A 57  ? 0.1515 0.1794 0.1420 -0.0070 0.0012  -0.0166 57  THR   A C   
1366 O O   . THR   A 57  ? 0.1486 0.1843 0.1653 -0.0126 -0.0093 -0.0291 57  THR   A O   
1367 C CB  . THR   A 57  ? 0.1489 0.1746 0.1138 -0.0075 0.0010  -0.0180 57  THR   A CB  
1368 O OG1 . THR   A 57  ? 0.1366 0.1697 0.1422 -0.0054 0.0020  -0.0141 57  THR   A OG1 
1369 C CG2 . THR   A 57  ? 0.1502 0.1784 0.1270 -0.0055 0.0056  -0.0027 57  THR   A CG2 
1377 N N   . ASN   A 58  ? 0.1568 0.1700 0.1733 -0.0059 0.0047  -0.0292 58  ASN   A N   
1378 C CA  . ASN   A 58  ? 0.1734 0.1677 0.1948 -0.0101 0.0127  -0.0379 58  ASN   A CA  
1379 C C   . ASN   A 58  ? 0.1518 0.1607 0.1851 -0.0009 0.0073  -0.0225 58  ASN   A C   
1380 O O   . ASN   A 58  ? 0.1520 0.1692 0.1975 -0.0164 -0.0042 -0.0270 58  ASN   A O   
1381 C CB  . ASN   A 58  ? 0.2220 0.1887 0.2429 -0.0209 0.0397  -0.0507 58  ASN   A CB  
1382 C CG  . ASN   A 58  ? 0.2659 0.2171 0.3233 -0.0191 0.0498  -0.0352 58  ASN   A CG  
1383 O OD1 . ASN   A 58  ? 0.2927 0.2091 0.3652 0.0154  0.0905  -0.0258 58  ASN   A OD1 
1384 N ND2 . ASN   A 58  ? 0.2763 0.2358 0.3415 -0.0210 0.0344  -0.0443 58  ASN   A ND2 
1391 N N   . ASN   A 59  ? 0.1350 0.1515 0.1710 -0.0073 -0.0032 -0.0169 59  ASN   A N   
1392 C CA  . ASN   A 59  ? 0.1386 0.1412 0.1676 0.0003  -0.0064 -0.0113 59  ASN   A CA  
1393 C C   . ASN   A 59  ? 0.1371 0.1464 0.1498 -0.0071 0.0017  -0.0063 59  ASN   A C   
1394 O O   . ASN   A 59  ? 0.1372 0.1455 0.1526 -0.0088 -0.0016 0.0005  59  ASN   A O   
1395 C CB  . ASN   A 59  ? 0.1434 0.1353 0.1671 0.0029  -0.0115 -0.0207 59  ASN   A CB  
1396 C CG  . ASN   A 59  ? 0.1462 0.1427 0.1741 0.0024  -0.0238 -0.0029 59  ASN   A CG  
1397 O OD1 . ASN   A 59  ? 0.1588 0.1511 0.1656 -0.0127 -0.0188 0.0052  59  ASN   A OD1 
1398 N ND2 . ASN   A 59  ? 0.1505 0.1452 0.1938 -0.0150 -0.0108 -0.0017 59  ASN   A ND2 
1405 N N   . ALA   A 60  ? 0.1328 0.1539 0.1484 -0.0063 0.0031  -0.0069 60  ALA   A N   
1406 C CA  . ALA   A 60  ? 0.1312 0.1484 0.1551 -0.0058 -0.0090 -0.0064 60  ALA   A CA  
1407 C C   . ALA   A 60  ? 0.1326 0.1411 0.1644 -0.0021 -0.0037 -0.0009 60  ALA   A C   
1408 O O   . ALA   A 60  ? 0.1305 0.1427 0.1848 -0.0024 -0.0090 -0.0071 60  ALA   A O   
1409 C CB  . ALA   A 60  ? 0.1455 0.1667 0.1547 -0.0094 -0.0156 -0.0251 60  ALA   A CB  
1415 N N   . MET   A 61  ? 0.1297 0.1388 0.1516 -0.0041 0.0008  -0.0033 61  MET   A N   
1416 C CA  . MET   A 61  ? 0.1312 0.1333 0.1547 -0.0043 0.0033  -0.0002 61  MET   A CA  
1417 C C   . MET   A 61  ? 0.1294 0.1291 0.1552 -0.0062 0.0000  -0.0011 61  MET   A C   
1418 O O   . MET   A 61  ? 0.1318 0.1342 0.1656 -0.0064 0.0049  0.0039  61  MET   A O   
1419 C CB  . MET   A 61  ? 0.1358 0.1407 0.1438 -0.0083 0.0070  -0.0016 61  MET   A CB  
1420 C CG  . MET   A 61  ? 0.1321 0.1427 0.1696 -0.0071 -0.0009 0.0043  61  MET   A CG  
1421 S SD  . MET   A 61  ? 0.1361 0.1424 0.1979 -0.0118 0.0013  -0.0159 61  MET   A SD  
1422 C CE  . MET   A 61  ? 0.1578 0.1566 0.2058 -0.0130 0.0155  -0.0088 61  MET   A CE  
1432 N N   . GLN   A 62  ? 0.1267 0.1317 0.1625 -0.0066 0.0025  -0.0022 62  GLN   A N   
1433 C CA  . GLN   A 62  ? 0.1287 0.1274 0.1536 -0.0053 0.0030  0.0021  62  GLN   A CA  
1434 C C   . GLN   A 62  ? 0.1362 0.1194 0.1652 0.0003  0.0084  -0.0001 62  GLN   A C   
1435 O O   . GLN   A 62  ? 0.1345 0.1370 0.1562 -0.0014 0.0066  0.0027  62  GLN   A O   
1436 C CB  . GLN   A 62  ? 0.1346 0.1318 0.1634 -0.0016 0.0013  0.0023  62  GLN   A CB  
1437 C CG  . GLN   A 62  ? 0.1376 0.1255 0.1507 -0.0015 0.0005  0.0121  62  GLN   A CG  
1438 C CD  . GLN   A 62  ? 0.1467 0.1302 0.1556 -0.0019 0.0086  0.0134  62  GLN   A CD  
1439 O OE1 . GLN   A 62  ? 0.1504 0.1438 0.1686 -0.0030 0.0042  0.0033  62  GLN   A OE1 
1440 N NE2 . GLN   A 62  ? 0.1493 0.1390 0.1630 0.0001  -0.0037 -0.0044 62  GLN   A NE2 
1449 N N   . VAL   A 63  ? 0.1300 0.1259 0.1746 -0.0016 0.0081  -0.0193 63  VAL   A N   
1450 C CA  . VAL   A 63  ? 0.1311 0.1377 0.1984 -0.0110 0.0019  -0.0112 63  VAL   A CA  
1451 C C   . VAL   A 63  ? 0.1228 0.1420 0.1836 -0.0115 -0.0060 -0.0118 63  VAL   A C   
1452 O O   . VAL   A 63  ? 0.1220 0.1414 0.2006 -0.0124 -0.0007 -0.0093 63  VAL   A O   
1453 C CB  . VAL   A 63  ? 0.1424 0.1586 0.2287 -0.0134 0.0007  -0.0342 63  VAL   A CB  
1454 C CG1 . VAL   A 63  ? 0.1574 0.1802 0.2534 -0.0150 -0.0025 -0.0521 63  VAL   A CG1 
1455 C CG2 . VAL   A 63  ? 0.1503 0.1503 0.2399 -0.0130 0.0167  -0.0288 63  VAL   A CG2 
1465 N N   . GLU   A 64  ? 0.1258 0.1475 0.1707 -0.0066 -0.0051 -0.0041 64  GLU   A N   
1466 C CA  . GLU   A 64  ? 0.1197 0.1494 0.1631 -0.0066 -0.0104 0.0027  64  GLU   A CA  
1467 C C   . GLU   A 64  ? 0.1201 0.1416 0.1678 -0.0069 0.0020  0.0053  64  GLU   A C   
1468 O O   . GLU   A 64  ? 0.1277 0.1442 0.1809 -0.0043 0.0023  -0.0036 64  GLU   A O   
1469 C CB  . GLU   A 64  ? 0.1360 0.1561 0.1752 -0.0051 0.0057  0.0061  64  GLU   A CB  
1470 C CG  . GLU   A 64  ? 0.1484 0.1615 0.1883 -0.0131 0.0031  0.0035  64  GLU   A CG  
1471 C CD  . GLU   A 64  ? 0.1542 0.1669 0.1882 -0.0164 0.0062  0.0050  64  GLU   A CD  
1472 O OE1 . GLU   A 64  ? 0.1532 0.1774 0.2216 -0.0215 0.0135  0.0060  64  GLU   A OE1 
1473 O OE2 . GLU   A 64  ? 0.1721 0.1683 0.1799 -0.0242 -0.0114 0.0072  64  GLU   A OE2 
1480 N N   . SER   A 65  ? 0.1182 0.1385 0.1650 -0.0008 0.0037  0.0031  65  SER   A N   
1481 C CA  . SER   A 65  ? 0.1264 0.1343 0.1549 -0.0049 -0.0007 -0.0026 65  SER   A CA  
1482 C C   . SER   A 65  ? 0.1276 0.1390 0.1546 -0.0090 -0.0061 -0.0044 65  SER   A C   
1483 O O   . SER   A 65  ? 0.1342 0.1467 0.1802 0.0006  0.0139  -0.0067 65  SER   A O   
1484 C CB  . SER   A 65  ? 0.1282 0.1334 0.1593 -0.0095 0.0007  0.0097  65  SER   A CB  
1485 O OG  . SER   A 65  ? 0.1294 0.1458 0.1675 -0.0119 -0.0072 0.0089  65  SER   A OG  
1491 N N   . ASP   A 66  ? 0.1296 0.1372 0.1638 -0.0073 0.0113  0.0042  66  ASP   A N   
1492 C CA  . ASP   A 66  ? 0.1395 0.1444 0.1893 -0.0010 0.0070  0.0177  66  ASP   A CA  
1493 C C   . ASP   A 66  ? 0.1388 0.1402 0.1833 -0.0096 0.0144  0.0185  66  ASP   A C   
1494 O O   . ASP   A 66  ? 0.1456 0.1507 0.1986 -0.0042 0.0249  0.0276  66  ASP   A O   
1495 C CB  . ASP   A 66  ? 0.1479 0.1586 0.2087 0.0040  0.0129  0.0328  66  ASP   A CB  
1496 C CG  . ASP   A 66  ? 0.1710 0.1706 0.2480 -0.0020 0.0052  0.0521  66  ASP   A CG  
1497 O OD1 . ASP   A 66  ? 0.1733 0.2015 0.2233 -0.0097 -0.0032 0.0532  66  ASP   A OD1 
1498 O OD2 . ASP   A 66  ? 0.1892 0.1794 0.3351 0.0171  -0.0143 0.0343  66  ASP   A OD2 
1503 N N   . ASP   A 67  ? 0.1290 0.1464 0.1904 -0.0082 0.0084  0.0179  67  ASP   A N   
1504 C CA  . ASP   A 67  ? 0.1301 0.1641 0.1993 -0.0051 0.0022  0.0251  67  ASP   A CA  
1505 C C   . ASP   A 67  ? 0.1350 0.1652 0.1980 0.0011  0.0087  0.0241  67  ASP   A C   
1506 O O   . ASP   A 67  ? 0.1319 0.1685 0.2217 -0.0006 0.0245  0.0289  67  ASP   A O   
1507 C CB  . ASP   A 67  ? 0.1401 0.1707 0.2332 -0.0090 -0.0174 0.0312  67  ASP   A CB  
1508 C CG  . ASP   A 67  ? 0.1370 0.1803 0.2796 -0.0146 -0.0250 0.0360  67  ASP   A CG  
1509 O OD1 . ASP   A 67  ? 0.1424 0.2002 0.3575 -0.0149 -0.0374 0.0504  67  ASP   A OD1 
1510 O OD2 . ASP   A 67  ? 0.1429 0.1829 0.2618 0.0032  -0.0120 0.0290  67  ASP   A OD2 
1515 N N   . TYR   A 68  ? 0.1407 0.1509 0.2029 0.0023  0.0160  0.0278  68  TYR   A N   
1516 C CA  . TYR   A 68  ? 0.1448 0.1463 0.1998 0.0030  0.0213  0.0250  68  TYR   A CA  
1517 C C   . TYR   A 68  ? 0.1380 0.1426 0.1994 0.0020  0.0248  0.0169  68  TYR   A C   
1518 O O   . TYR   A 68  ? 0.1419 0.1511 0.2099 0.0094  0.0306  0.0162  68  TYR   A O   
1519 C CB  . TYR   A 68  ? 0.1464 0.1375 0.2073 0.0049  0.0352  0.0268  68  TYR   A CB  
1520 C CG  . TYR   A 68  ? 0.1547 0.1589 0.2457 0.0009  0.0455  0.0248  68  TYR   A CG  
1521 C CD1 . TYR   A 68  ? 0.1582 0.1675 0.2888 -0.0217 0.0321  -0.0087 68  TYR   A CD1 
1522 C CD2 . TYR   A 68  ? 0.1792 0.1657 0.2950 0.0091  0.0554  0.0282  68  TYR   A CD2 
1523 C CE1 . TYR   A 68  ? 0.1663 0.1745 0.3319 -0.0158 0.0467  -0.0188 68  TYR   A CE1 
1524 C CE2 . TYR   A 68  ? 0.1765 0.1688 0.3243 -0.0003 0.0720  0.0060  68  TYR   A CE2 
1525 C CZ  . TYR   A 68  ? 0.1726 0.1676 0.3478 -0.0203 0.0541  -0.0193 68  TYR   A CZ  
1526 O OH  . TYR   A 68  ? 0.2004 0.1695 0.3702 -0.0140 0.0303  -0.0411 68  TYR   A OH  
1536 N N   . ILE   A 69  ? 0.1301 0.1386 0.1852 -0.0015 0.0189  0.0137  69  ILE   A N   
1537 C CA  . ILE   A 69  ? 0.1391 0.1417 0.1710 0.0042  0.0111  0.0021  69  ILE   A CA  
1538 C C   . ILE   A 69  ? 0.1482 0.1441 0.1644 0.0025  0.0199  0.0173  69  ILE   A C   
1539 O O   . ILE   A 69  ? 0.1545 0.1535 0.1733 -0.0026 0.0240  0.0190  69  ILE   A O   
1540 C CB  . ILE   A 69  ? 0.1438 0.1659 0.1742 0.0051  0.0092  -0.0077 69  ILE   A CB  
1541 C CG1 . ILE   A 69  ? 0.1449 0.1749 0.1956 0.0082  0.0083  -0.0228 69  ILE   A CG1 
1542 C CG2 . ILE   A 69  ? 0.1613 0.1888 0.1914 0.0165  -0.0057 -0.0161 69  ILE   A CG2 
1543 C CD1 . ILE   A 69  ? 0.1420 0.1860 0.2179 -0.0022 0.0093  -0.0218 69  ILE   A CD1 
1555 N N   . ALA   A 70  ? 0.1487 0.1452 0.1874 -0.0058 0.0213  0.0133  70  ALA   A N   
1556 C CA  . ALA   A 70  ? 0.1555 0.1585 0.2052 -0.0162 0.0278  0.0185  70  ALA   A CA  
1557 C C   . ALA   A 70  ? 0.1538 0.1727 0.2046 -0.0142 0.0298  0.0207  70  ALA   A C   
1558 O O   . ALA   A 70  ? 0.1678 0.2045 0.2237 0.0047  0.0466  0.0369  70  ALA   A O   
1559 C CB  . ALA   A 70  ? 0.1578 0.1534 0.2245 -0.0227 0.0238  0.0128  70  ALA   A CB  
1565 N N   . THR   A 71  ? 0.1397 0.1655 0.1934 -0.0064 0.0204  0.0121  71  THR   A N   
1566 C CA  . THR   A 71  ? 0.1507 0.1894 0.2274 0.0095  0.0144  0.0154  71  THR   A CA  
1567 C C   . THR   A 71  ? 0.1411 0.1798 0.2517 0.0133  0.0317  0.0200  71  THR   A C   
1568 O O   . THR   A 71  ? 0.1487 0.2048 0.3017 0.0081  0.0415  -0.0065 71  THR   A O   
1569 C CB  . THR   A 71  ? 0.1813 0.2153 0.2533 0.0129  -0.0159 0.0284  71  THR   A CB  
1570 O OG1 . THR   A 71  ? 0.2114 0.2357 0.2628 0.0068  -0.0315 0.0201  71  THR   A OG1 
1571 C CG2 . THR   A 71  ? 0.1931 0.2311 0.2769 0.0213  -0.0349 0.0461  71  THR   A CG2 
1579 N N   . ASN   A 72  ? 0.1447 0.1646 0.2294 0.0100  0.0282  0.0232  72  ASN   A N   
1580 C CA  . ASN   A 72  ? 0.1517 0.1611 0.2204 0.0125  0.0379  0.0205  72  ASN   A CA  
1581 C C   . ASN   A 72  ? 0.1676 0.1591 0.2168 0.0072  0.0506  0.0091  72  ASN   A C   
1582 O O   . ASN   A 72  ? 0.1795 0.1609 0.2504 0.0129  0.0453  0.0016  72  ASN   A O   
1583 C CB  . ASN   A 72  ? 0.1774 0.1681 0.2233 0.0097  0.0344  0.0208  72  ASN   A CB  
1584 C CG  . ASN   A 72  ? 0.2076 0.1873 0.2219 0.0182  0.0345  0.0305  72  ASN   A CG  
1585 O OD1 . ASN   A 72  ? 0.2258 0.2195 0.2359 0.0154  0.0379  0.0298  72  ASN   A OD1 
1586 N ND2 . ASN   A 72  ? 0.2195 0.1854 0.2312 0.0547  0.0213  0.0262  72  ASN   A ND2 
1593 N N   . GLY   A 73  ? 0.1711 0.1552 0.1964 0.0034  0.0443  0.0028  73  GLY   A N   
1594 C CA  . GLY   A 73  ? 0.1748 0.1536 0.1910 -0.0092 0.0362  0.0059  73  GLY   A CA  
1595 C C   . GLY   A 73  ? 0.1714 0.1436 0.1736 0.0007  0.0438  0.0238  73  GLY   A C   
1596 O O   . GLY   A 73  ? 0.1679 0.1503 0.1849 0.0114  0.0350  0.0259  73  GLY   A O   
1600 N N   . PRO   A 74  ? 0.1772 0.1510 0.1792 -0.0110 0.0400  0.0157  74  PRO   A N   
1601 C CA  . PRO   A 74  ? 0.1723 0.1493 0.1889 -0.0065 0.0448  0.0130  74  PRO   A CA  
1602 C C   . PRO   A 74  ? 0.1622 0.1343 0.1894 -0.0026 0.0288  0.0029  74  PRO   A C   
1603 O O   . PRO   A 74  ? 0.1687 0.1420 0.2128 -0.0005 0.0281  -0.0050 74  PRO   A O   
1604 C CB  . PRO   A 74  ? 0.1939 0.1786 0.2154 -0.0022 0.0411  0.0276  74  PRO   A CB  
1605 C CG  . PRO   A 74  ? 0.2171 0.2151 0.2488 -0.0185 0.0322  0.0202  74  PRO   A CG  
1606 C CD  . PRO   A 74  ? 0.1997 0.1910 0.1956 -0.0193 0.0274  0.0094  74  PRO   A CD  
1614 N N   . LEU   A 75  ? 0.1633 0.1256 0.1696 -0.0010 0.0195  0.0048  75  LEU   A N   
1615 C CA  . LEU   A 75  ? 0.1688 0.1341 0.1467 0.0023  0.0096  0.0129  75  LEU   A CA  
1616 C C   . LEU   A 75  ? 0.1785 0.1496 0.1354 0.0087  0.0135  0.0131  75  LEU   A C   
1617 O O   . LEU   A 75  ? 0.2079 0.1657 0.1522 0.0133  0.0079  0.0108  75  LEU   A O   
1618 C CB  . LEU   A 75  ? 0.1696 0.1379 0.1434 -0.0055 0.0085  0.0202  75  LEU   A CB  
1619 C CG  . LEU   A 75  ? 0.1814 0.1733 0.1527 -0.0317 0.0099  0.0070  75  LEU   A CG  
1620 C CD1 . LEU   A 75  ? 0.1914 0.2253 0.1851 -0.0311 0.0011  -0.0085 75  LEU   A CD1 
1621 C CD2 . LEU   A 75  ? 0.2106 0.2162 0.2104 -0.0089 0.0073  0.0070  75  LEU   A CD2 
1633 N N   . LYS   A 76  ? 0.1787 0.1406 0.1534 -0.0001 0.0075  -0.0001 76  LYS   A N   
1634 C CA  . LYS   A 76  ? 0.1757 0.1597 0.1663 -0.0057 0.0060  -0.0133 76  LYS   A CA  
1635 C C   . LYS   A 76  ? 0.1702 0.1415 0.1350 -0.0007 0.0047  0.0043  76  LYS   A C   
1636 O O   . LYS   A 76  ? 0.1719 0.1367 0.1563 -0.0035 0.0136  0.0164  76  LYS   A O   
1637 C CB  . LYS   A 76  ? 0.1719 0.1799 0.2150 0.0022  0.0186  -0.0307 76  LYS   A CB  
1638 C CG  . LYS   A 76  ? 0.1789 0.1763 0.2658 0.0041  0.0018  -0.0310 76  LYS   A CG  
1639 C CD  . LYS   A 76  ? 0.1883 0.1711 0.3125 0.0048  -0.0101 -0.0297 76  LYS   A CD  
1640 C CE  . LYS   A 76  ? 0.2077 0.1981 0.3695 0.0014  -0.0018 -0.0404 76  LYS   A CE  
1641 N NZ  . LYS   A 76  ? 0.2105 0.1889 0.4050 -0.0096 -0.0031 -0.0522 76  LYS   A NZ  
1655 N N   . VAL   A 77  ? 0.1826 0.1526 0.1375 -0.0039 0.0179  0.0127  77  VAL   A N   
1656 C CA  . VAL   A 77  ? 0.1785 0.1533 0.1373 0.0010  0.0178  0.0034  77  VAL   A CA  
1657 C C   . VAL   A 77  ? 0.1763 0.1461 0.1419 0.0085  0.0120  0.0006  77  VAL   A C   
1658 O O   . VAL   A 77  ? 0.1813 0.1540 0.1472 0.0080  0.0267  -0.0028 77  VAL   A O   
1659 C CB  . VAL   A 77  ? 0.1956 0.1723 0.1486 -0.0054 0.0095  0.0133  77  VAL   A CB  
1660 C CG1 . VAL   A 77  ? 0.1954 0.1904 0.1656 0.0060  0.0011  0.0039  77  VAL   A CG1 
1661 C CG2 . VAL   A 77  ? 0.2177 0.1833 0.1711 -0.0108 0.0011  0.0272  77  VAL   A CG2 
1671 N N   . GLY   A 78  ? 0.1650 0.1388 0.1390 0.0042  0.0212  0.0032  78  GLY   A N   
1672 C CA  . GLY   A 78  ? 0.1631 0.1374 0.1581 0.0002  0.0245  0.0093  78  GLY   A CA  
1673 C C   . GLY   A 78  ? 0.1490 0.1344 0.1615 0.0019  0.0176  0.0135  78  GLY   A C   
1674 O O   . GLY   A 78  ? 0.1466 0.1418 0.1875 -0.0022 0.0156  0.0243  78  GLY   A O   
1678 N N   . GLY   A 79  ? 0.1559 0.1327 0.1512 0.0024  0.0136  0.0120  79  GLY   A N   
1679 C CA  . GLY   A 79  ? 0.1523 0.1364 0.1587 0.0008  0.0149  0.0130  79  GLY   A CA  
1680 C C   . GLY   A 79  ? 0.1411 0.1311 0.1558 0.0021  0.0112  0.0063  79  GLY   A C   
1681 O O   . GLY   A 79  ? 0.1429 0.1401 0.1718 0.0176  0.0090  0.0057  79  GLY   A O   
1685 N N   . SER   A 80  ? 0.1343 0.1445 0.1728 -0.0024 0.0132  -0.0020 80  SER   A N   
1686 C CA  . SER   A 80  ? 0.1294 0.1371 0.1597 -0.0038 0.0070  0.0063  80  SER   A CA  
1687 C C   . SER   A 80  ? 0.1274 0.1396 0.1743 -0.0062 0.0071  0.0117  80  SER   A C   
1688 O O   . SER   A 80  ? 0.1310 0.1625 0.1960 0.0082  0.0113  -0.0007 80  SER   A O   
1689 C CB  . SER   A 80  ? 0.1436 0.1416 0.1758 -0.0075 0.0108  -0.0023 80  SER   A CB  
1690 O OG  . SER   A 80  ? 0.1693 0.1434 0.2162 0.0050  -0.0021 0.0224  80  SER   A OG  
1696 N N   . CYS   A 81  ? 0.1268 0.1344 0.1630 -0.0016 -0.0070 0.0116  81  CYS   A N   
1697 C CA  . CYS   A 81  ? 0.1274 0.1420 0.1654 -0.0084 -0.0049 0.0201  81  CYS   A CA  
1698 C C   . CYS   A 81  ? 0.1300 0.1413 0.1573 -0.0120 -0.0007 0.0272  81  CYS   A C   
1699 O O   . CYS   A 81  ? 0.1234 0.1687 0.1825 0.0028  0.0032  0.0341  81  CYS   A O   
1700 C CB  . CYS   A 81  ? 0.1330 0.1464 0.1824 -0.0091 -0.0034 0.0194  81  CYS   A CB  
1701 S SG  . CYS   A 81  ? 0.1480 0.1377 0.1777 -0.0129 0.0017  0.0130  81  CYS   A SG  
1707 N N   . VAL   A 82  ? 0.1325 0.1458 0.1571 -0.0035 -0.0111 0.0187  82  VAL   A N   
1708 C CA  . VAL   A 82  ? 0.1460 0.1522 0.1511 -0.0016 -0.0109 0.0241  82  VAL   A CA  
1709 C C   . VAL   A 82  ? 0.1423 0.1593 0.1564 -0.0010 -0.0066 0.0230  82  VAL   A C   
1710 O O   . VAL   A 82  ? 0.1346 0.1639 0.1945 -0.0016 -0.0073 0.0010  82  VAL   A O   
1711 C CB  . VAL   A 82  ? 0.1720 0.1677 0.1729 -0.0009 -0.0055 0.0359  82  VAL   A CB  
1712 C CG1 . VAL   A 82  ? 0.1943 0.1823 0.1872 0.0013  -0.0031 0.0315  82  VAL   A CG1 
1713 C CG2 . VAL   A 82  ? 0.1741 0.1748 0.2144 -0.0055 -0.0036 0.0314  82  VAL   A CG2 
1723 N N   . LEU   A 83  ? 0.1362 0.1544 0.1509 -0.0086 -0.0079 0.0128  83  LEU   A N   
1724 C CA  . LEU   A 83  ? 0.1399 0.1564 0.1454 -0.0131 -0.0063 0.0117  83  LEU   A CA  
1725 C C   . LEU   A 83  ? 0.1429 0.1583 0.1440 -0.0128 -0.0156 0.0142  83  LEU   A C   
1726 O O   . LEU   A 83  ? 0.1506 0.1641 0.1537 -0.0196 -0.0053 0.0211  83  LEU   A O   
1727 C CB  . LEU   A 83  ? 0.1464 0.1653 0.1566 -0.0153 -0.0132 0.0158  83  LEU   A CB  
1728 C CG  . LEU   A 83  ? 0.1596 0.1744 0.1604 -0.0149 0.0024  0.0080  83  LEU   A CG  
1729 C CD1 . LEU   A 83  ? 0.1731 0.1707 0.1609 -0.0284 0.0013  0.0210  83  LEU   A CD1 
1730 C CD2 . LEU   A 83  ? 0.1524 0.1884 0.1718 -0.0147 0.0161  0.0100  83  LEU   A CD2 
1742 N N   . SER   A 84  ? 0.1605 0.1649 0.1473 -0.0174 -0.0155 0.0172  84  SER   A N   
1743 C CA  . SER   A 84  ? 0.1739 0.1722 0.1226 -0.0152 -0.0099 0.0112  84  SER   A CA  
1744 C C   . SER   A 84  ? 0.1784 0.1684 0.1112 -0.0235 0.0031  0.0106  84  SER   A C   
1745 O O   . SER   A 84  ? 0.1731 0.1787 0.1173 -0.0201 -0.0075 0.0151  84  SER   A O   
1746 C CB  . SER   A 84  ? 0.1811 0.1926 0.1414 -0.0089 -0.0122 0.0020  84  SER   A CB  
1747 O OG  . SER   A 84  ? 0.1842 0.2145 0.1531 -0.0102 -0.0185 -0.0129 84  SER   A OG  
1753 N N   . GLY   A 85  ? 0.1862 0.1848 0.1302 -0.0236 0.0015  0.0122  85  GLY   A N   
1754 C CA  . GLY   A 85  ? 0.1816 0.1925 0.1485 -0.0237 0.0089  0.0048  85  GLY   A CA  
1755 C C   . GLY   A 85  ? 0.1837 0.1977 0.1337 -0.0255 0.0023  0.0072  85  GLY   A C   
1756 O O   . GLY   A 85  ? 0.1842 0.2040 0.1511 -0.0337 0.0112  -0.0071 85  GLY   A O   
1760 N N   . HIS   A 86  ? 0.1859 0.1900 0.1375 -0.0203 -0.0020 0.0080  86  HIS   A N   
1761 C CA  . HIS   A 86  ? 0.1998 0.1971 0.1203 -0.0227 -0.0028 0.0063  86  HIS   A CA  
1762 C C   . HIS   A 86  ? 0.2251 0.2138 0.1153 -0.0251 -0.0061 0.0014  86  HIS   A C   
1763 O O   . HIS   A 86  ? 0.2370 0.2383 0.1369 -0.0260 0.0039  0.0066  86  HIS   A O   
1764 C CB  . HIS   A 86  ? 0.2015 0.1893 0.1310 -0.0164 0.0002  0.0094  86  HIS   A CB  
1765 C CG  . HIS   A 86  ? 0.1966 0.1905 0.1393 -0.0142 0.0032  0.0086  86  HIS   A CG  
1766 N ND1 . HIS   A 86  ? 0.2012 0.1842 0.1723 -0.0257 -0.0002 0.0056  86  HIS   A ND1 
1767 C CD2 . HIS   A 86  ? 0.1932 0.1851 0.1354 0.0006  0.0064  0.0128  86  HIS   A CD2 
1768 C CE1 . HIS   A 86  ? 0.1926 0.1814 0.1754 -0.0139 0.0187  0.0113  86  HIS   A CE1 
1769 N NE2 . HIS   A 86  ? 0.1913 0.1799 0.1570 0.0029  0.0139  0.0225  86  HIS   A NE2 
1777 N N   . ASN   A 87  ? 0.2438 0.2233 0.1312 -0.0160 0.0188  -0.0096 87  ASN   A N   
1778 C CA  . ASN   A 87  ? 0.2641 0.2325 0.1318 -0.0138 0.0425  -0.0155 87  ASN   A CA  
1779 C C   . ASN   A 87  ? 0.2635 0.2511 0.1684 -0.0233 0.0633  -0.0048 87  ASN   A C   
1780 O O   . ASN   A 87  ? 0.2870 0.2702 0.2140 -0.0411 0.0960  -0.0102 87  ASN   A O   
1781 C CB  . ASN   A 87  ? 0.2833 0.2410 0.1461 -0.0062 0.0467  -0.0122 87  ASN   A CB  
1782 C CG  . ASN   A 87  ? 0.2987 0.2525 0.1485 -0.0001 0.0564  -0.0006 87  ASN   A CG  
1783 O OD1 . ASN   A 87  ? 0.3203 0.2539 0.1494 0.0164  0.0488  0.0059  87  ASN   A OD1 
1784 N ND2 . ASN   A 87  ? 0.3013 0.2747 0.1726 0.0018  0.0524  0.0061  87  ASN   A ND2 
1791 N N   . LEU   A 88  ? 0.2287 0.2385 0.1570 -0.0278 0.0349  0.0038  88  LEU   A N   
1792 C CA  . LEU   A 88  ? 0.2057 0.2322 0.1839 -0.0319 0.0321  0.0127  88  LEU   A CA  
1793 C C   . LEU   A 88  ? 0.1987 0.2354 0.1743 -0.0297 0.0309  0.0273  88  LEU   A C   
1794 O O   . LEU   A 88  ? 0.1988 0.2398 0.2083 -0.0247 0.0316  0.0425  88  LEU   A O   
1795 C CB  . LEU   A 88  ? 0.2057 0.2389 0.1983 -0.0370 0.0001  0.0210  88  LEU   A CB  
1796 C CG  . LEU   A 88  ? 0.2295 0.2534 0.2268 -0.0357 -0.0135 0.0242  88  LEU   A CG  
1797 C CD1 . LEU   A 88  ? 0.2424 0.2630 0.2267 -0.0327 -0.0176 0.0126  88  LEU   A CD1 
1798 C CD2 . LEU   A 88  ? 0.2421 0.2599 0.2637 -0.0345 -0.0104 0.0249  88  LEU   A CD2 
1810 N N   . ALA   A 89  ? 0.1981 0.2301 0.1548 -0.0281 0.0177  0.0084  89  ALA   A N   
1811 C CA  . ALA   A 89  ? 0.2036 0.2329 0.1252 -0.0237 0.0099  0.0191  89  ALA   A CA  
1812 C C   . ALA   A 89  ? 0.2097 0.2303 0.1306 -0.0221 0.0011  0.0191  89  ALA   A C   
1813 O O   . ALA   A 89  ? 0.2033 0.2267 0.1775 -0.0331 -0.0077 -0.0037 89  ALA   A O   
1814 C CB  . ALA   A 89  ? 0.2018 0.2357 0.1035 -0.0209 0.0072  0.0194  89  ALA   A CB  
1820 N N   . LYS   A 90  ? 0.2221 0.2450 0.1302 -0.0288 -0.0116 0.0249  90  LYS   A N   
1821 C CA  . LYS   A 90  ? 0.2310 0.2616 0.1425 -0.0241 -0.0334 0.0305  90  LYS   A CA  
1822 C C   . LYS   A 90  ? 0.2102 0.2456 0.1347 -0.0280 -0.0339 0.0209  90  LYS   A C   
1823 O O   . LYS   A 90  ? 0.2034 0.2615 0.1712 -0.0344 -0.0348 0.0056  90  LYS   A O   
1824 C CB  . LYS   A 90  ? 0.2611 0.2986 0.1997 -0.0283 -0.0396 0.0525  90  LYS   A CB  
1825 C CG  . LYS   A 90  ? 0.3045 0.3364 0.3041 -0.0305 -0.0384 0.0562  90  LYS   A CG  
1826 C CD  . LYS   A 90  ? 0.3530 0.3740 0.4106 -0.0373 -0.0245 0.0546  90  LYS   A CD  
1827 C CE  . LYS   A 90  ? 0.3972 0.4119 0.4918 -0.0401 -0.0132 0.0499  90  LYS   A CE  
1828 N NZ  . LYS   A 90  ? 0.4199 0.4274 0.5459 -0.0413 -0.0068 0.0493  90  LYS   A NZ  
1842 N N   . HIS   A 91  ? 0.1989 0.2144 0.1091 -0.0253 -0.0326 0.0199  91  HIS   A N   
1843 C CA  . HIS   A 91  ? 0.1866 0.1884 0.1200 -0.0165 -0.0272 0.0204  91  HIS   A CA  
1844 C C   . HIS   A 91  ? 0.1650 0.1785 0.1037 -0.0136 -0.0132 0.0192  91  HIS   A C   
1845 O O   . HIS   A 91  ? 0.1546 0.1919 0.1392 -0.0231 -0.0053 0.0217  91  HIS   A O   
1846 C CB  . HIS   A 91  ? 0.2003 0.2180 0.1713 0.0062  -0.0335 0.0271  91  HIS   A CB  
1847 C CG  . HIS   A 91  ? 0.2397 0.2728 0.2399 0.0166  -0.0609 0.0140  91  HIS   A CG  
1848 N ND1 . HIS   A 91  ? 0.2501 0.3025 0.2872 0.0213  -0.0712 -0.0049 91  HIS   A ND1 
1849 C CD2 . HIS   A 91  ? 0.2689 0.2955 0.2630 0.0223  -0.0762 0.0207  91  HIS   A CD2 
1850 C CE1 . HIS   A 91  ? 0.2682 0.3131 0.2944 0.0238  -0.0720 0.0054  91  HIS   A CE1 
1851 N NE2 . HIS   A 91  ? 0.2804 0.3117 0.2848 0.0290  -0.0814 0.0127  91  HIS   A NE2 
1859 N N   . CYS   A 92  ? 0.1543 0.1658 0.1123 -0.0162 -0.0064 0.0168  92  CYS   A N   
1860 C CA  . CYS   A 92  ? 0.1500 0.1609 0.1266 -0.0147 -0.0004 0.0124  92  CYS   A CA  
1861 C C   . CYS   A 92  ? 0.1406 0.1553 0.1290 -0.0180 -0.0016 0.0140  92  CYS   A C   
1862 O O   . CYS   A 92  ? 0.1380 0.1595 0.1567 -0.0186 -0.0077 0.0128  92  CYS   A O   
1863 C CB  . CYS   A 92  ? 0.1479 0.1623 0.1362 -0.0107 -0.0017 0.0095  92  CYS   A CB  
1864 S SG  . CYS   A 92  ? 0.1435 0.1467 0.1447 -0.0132 -0.0036 0.0140  92  CYS   A SG  
1870 N N   . LEU   A 93  ? 0.1387 0.1404 0.1400 -0.0144 0.0023  0.0106  93  LEU   A N   
1871 C CA  . LEU   A 93  ? 0.1304 0.1370 0.1300 -0.0102 -0.0086 0.0147  93  LEU   A CA  
1872 C C   . LEU   A 93  ? 0.1271 0.1269 0.1358 -0.0022 0.0031  0.0148  93  LEU   A C   
1873 O O   . LEU   A 93  ? 0.1221 0.1365 0.1463 -0.0007 -0.0001 0.0144  93  LEU   A O   
1874 C CB  . LEU   A 93  ? 0.1378 0.1368 0.1518 -0.0040 -0.0081 0.0200  93  LEU   A CB  
1875 C CG  . LEU   A 93  ? 0.1418 0.1413 0.1533 -0.0052 -0.0018 0.0220  93  LEU   A CG  
1876 C CD1 . LEU   A 93  ? 0.1498 0.1439 0.1708 0.0004  0.0030  0.0099  93  LEU   A CD1 
1877 C CD2 . LEU   A 93  ? 0.1585 0.1366 0.1674 -0.0075 -0.0051 0.0202  93  LEU   A CD2 
1889 N N   . HIS   A 94  ? 0.1214 0.1245 0.1448 -0.0034 0.0060  0.0206  94  HIS   A N   
1890 C CA  . HIS   A 94  ? 0.1215 0.1276 0.1523 -0.0041 -0.0019 0.0227  94  HIS   A CA  
1891 C C   . HIS   A 94  ? 0.1211 0.1189 0.1505 -0.0052 0.0027  0.0149  94  HIS   A C   
1892 O O   . HIS   A 94  ? 0.1258 0.1436 0.1779 -0.0006 0.0002  -0.0013 94  HIS   A O   
1893 C CB  . HIS   A 94  ? 0.1182 0.1195 0.1613 -0.0040 0.0006  0.0183  94  HIS   A CB  
1894 C CG  . HIS   A 94  ? 0.1300 0.1241 0.1447 -0.0033 -0.0057 0.0205  94  HIS   A CG  
1895 N ND1 . HIS   A 94  ? 0.1276 0.1245 0.1453 -0.0040 -0.0006 0.0185  94  HIS   A ND1 
1896 C CD2 . HIS   A 94  ? 0.1328 0.1324 0.1574 -0.0094 -0.0060 0.0095  94  HIS   A CD2 
1897 C CE1 . HIS   A 94  ? 0.1298 0.1291 0.1467 -0.0076 -0.0132 0.0046  94  HIS   A CE1 
1898 N NE2 . HIS   A 94  ? 0.1398 0.1346 0.1474 -0.0126 -0.0070 0.0064  94  HIS   A NE2 
1906 N N   . VAL   A 95  ? 0.1207 0.1234 0.1300 0.0000  0.0070  0.0140  95  VAL   A N   
1907 C CA  . VAL   A 95  ? 0.1314 0.1281 0.1126 -0.0048 0.0110  0.0113  95  VAL   A CA  
1908 C C   . VAL   A 95  ? 0.1334 0.1277 0.0956 -0.0139 0.0059  0.0086  95  VAL   A C   
1909 O O   . VAL   A 95  ? 0.1292 0.1344 0.1392 0.0075  0.0036  0.0083  95  VAL   A O   
1910 C CB  . VAL   A 95  ? 0.1292 0.1299 0.1431 -0.0124 0.0085  0.0096  95  VAL   A CB  
1911 C CG1 . VAL   A 95  ? 0.1487 0.1316 0.1655 -0.0214 0.0028  0.0020  95  VAL   A CG1 
1912 C CG2 . VAL   A 95  ? 0.1291 0.1350 0.1481 -0.0128 0.0104  0.0230  95  VAL   A CG2 
1922 N N   . VAL   A 96  ? 0.1319 0.1273 0.1034 -0.0067 -0.0023 0.0177  96  VAL   A N   
1923 C CA  . VAL   A 96  ? 0.1400 0.1318 0.1172 -0.0019 0.0072  0.0143  96  VAL   A CA  
1924 C C   . VAL   A 96  ? 0.1415 0.1373 0.1302 -0.0041 0.0039  0.0154  96  VAL   A C   
1925 O O   . VAL   A 96  ? 0.1485 0.1446 0.1549 -0.0059 0.0105  0.0016  96  VAL   A O   
1926 C CB  . VAL   A 96  ? 0.1388 0.1421 0.1324 -0.0055 0.0146  0.0166  96  VAL   A CB  
1927 C CG1 . VAL   A 96  ? 0.1434 0.1545 0.1239 -0.0063 0.0156  0.0089  96  VAL   A CG1 
1928 C CG2 . VAL   A 96  ? 0.1372 0.1457 0.1465 -0.0167 0.0131  0.0109  96  VAL   A CG2 
1938 N N   A GLY   A 97  ? 0.1406 0.1416 0.1352 -0.0085 0.0019  0.0171  97  GLY   A N   
1939 N N   B GLY   A 97  ? 0.1426 0.1439 0.1344 -0.0039 0.0040  0.0148  97  GLY   A N   
1940 C CA  A GLY   A 97  ? 0.1452 0.1528 0.1329 -0.0114 -0.0052 0.0133  97  GLY   A CA  
1941 C CA  B GLY   A 97  ? 0.1470 0.1510 0.1332 -0.0017 0.0048  0.0149  97  GLY   A CA  
1942 C C   A GLY   A 97  ? 0.1500 0.1623 0.1163 -0.0083 0.0004  0.0032  97  GLY   A C   
1943 C C   B GLY   A 97  ? 0.1522 0.1557 0.1304 0.0044  0.0131  0.0118  97  GLY   A C   
1944 O O   A GLY   A 97  ? 0.1559 0.1551 0.1246 -0.0059 0.0011  -0.0021 97  GLY   A O   
1945 O O   B GLY   A 97  ? 0.1585 0.1554 0.1492 0.0017  0.0254  0.0150  97  GLY   A O   
1952 N N   A PRO   A 98  ? 0.1530 0.1590 0.0992 -0.0008 -0.0052 0.0058  98  PRO   A N   
1953 N N   B PRO   A 98  ? 0.1606 0.1552 0.1320 0.0071  0.0077  0.0144  98  PRO   A N   
1954 C CA  A PRO   A 98  ? 0.1595 0.1725 0.1104 0.0014  0.0010  -0.0008 98  PRO   A CA  
1955 C CA  B PRO   A 98  ? 0.1709 0.1599 0.1522 0.0062  0.0013  0.0037  98  PRO   A CA  
1956 C C   A PRO   A 98  ? 0.1596 0.1806 0.1082 -0.0072 -0.0012 0.0037  98  PRO   A C   
1957 C C   B PRO   A 98  ? 0.1886 0.1591 0.1593 0.0010  0.0015  0.0117  98  PRO   A C   
1958 O O   A PRO   A 98  ? 0.1530 0.1617 0.1231 -0.0040 0.0014  -0.0005 98  PRO   A O   
1959 O O   B PRO   A 98  ? 0.1861 0.1537 0.1770 0.0007  0.0139  0.0066  98  PRO   A O   
1960 C CB  A PRO   A 98  ? 0.1695 0.1763 0.1012 0.0120  -0.0023 -0.0132 98  PRO   A CB  
1961 C CB  B PRO   A 98  ? 0.1741 0.1531 0.1501 0.0138  -0.0014 0.0050  98  PRO   A CB  
1962 C CG  A PRO   A 98  ? 0.1684 0.1676 0.1272 0.0192  -0.0057 -0.0106 98  PRO   A CG  
1963 C CG  B PRO   A 98  ? 0.1785 0.1532 0.1481 0.0154  0.0005  0.0111  98  PRO   A CG  
1964 C CD  A PRO   A 98  ? 0.1609 0.1568 0.1181 0.0104  -0.0089 0.0033  98  PRO   A CD  
1965 C CD  B PRO   A 98  ? 0.1675 0.1518 0.1337 0.0121  0.0037  0.0155  98  PRO   A CD  
1980 N N   A ASN   A 99  ? 0.1646 0.2023 0.0946 -0.0073 0.0078  0.0164  99  ASN   A N   
1981 N N   B ASN   A 99  ? 0.2168 0.1663 0.1488 0.0023  -0.0043 0.0230  99  ASN   A N   
1982 C CA  A ASN   A 99  ? 0.1861 0.2148 0.0772 -0.0080 0.0079  0.0294  99  ASN   A CA  
1983 C CA  B ASN   A 99  ? 0.2456 0.1744 0.1671 0.0056  -0.0072 0.0390  99  ASN   A CA  
1984 C C   A ASN   A 99  ? 0.2030 0.2455 0.0725 -0.0121 0.0180  0.0329  99  ASN   A C   
1985 C C   B ASN   A 99  ? 0.2598 0.1830 0.1700 0.0126  -0.0181 0.0452  99  ASN   A C   
1986 O O   A ASN   A 99  ? 0.2164 0.2687 0.0845 -0.0060 0.0081  0.0195  99  ASN   A O   
1987 O O   B ASN   A 99  ? 0.2607 0.1759 0.1589 0.0176  -0.0235 0.0450  99  ASN   A O   
1988 C CB  A ASN   A 99  ? 0.1824 0.2058 0.1082 -0.0107 0.0001  0.0359  99  ASN   A CB  
1989 C CB  B ASN   A 99  ? 0.2570 0.1732 0.1907 0.0066  -0.0143 0.0446  99  ASN   A CB  
1990 C CG  A ASN   A 99  ? 0.1812 0.2021 0.1480 -0.0016 -0.0144 0.0274  99  ASN   A CG  
1991 C CG  B ASN   A 99  ? 0.2716 0.1840 0.2108 0.0001  -0.0185 0.0454  99  ASN   A CG  
1992 O OD1 A ASN   A 99  ? 0.1918 0.2095 0.1527 0.0079  -0.0113 0.0200  99  ASN   A OD1 
1993 O OD1 B ASN   A 99  ? 0.2722 0.1890 0.2043 0.0083  -0.0241 0.0553  99  ASN   A OD1 
1994 N ND2 A ASN   A 99  ? 0.1799 0.1939 0.1755 -0.0075 -0.0185 0.0383  99  ASN   A ND2 
1995 N ND2 B ASN   A 99  ? 0.2807 0.1884 0.2453 -0.0042 -0.0269 0.0269  99  ASN   A ND2 
2008 N N   A VAL   A 100 ? 0.2126 0.2547 0.0863 -0.0245 -0.0118 0.0275  100 VAL   A N   
2009 N N   B VAL   A 100 ? 0.2778 0.2100 0.2048 0.0140  -0.0155 0.0428  100 VAL   A N   
2010 C CA  A VAL   A 100 ? 0.2315 0.2747 0.1296 -0.0299 -0.0283 0.0344  100 VAL   A CA  
2011 C CA  B VAL   A 100 ? 0.2986 0.2322 0.2444 0.0160  -0.0125 0.0314  100 VAL   A CA  
2012 C C   A VAL   A 100 ? 0.2378 0.2873 0.1314 -0.0432 -0.0276 0.0566  100 VAL   A C   
2013 C C   B VAL   A 100 ? 0.3101 0.2355 0.2500 0.0250  -0.0194 0.0252  100 VAL   A C   
2014 O O   A VAL   A 100 ? 0.2499 0.2952 0.1456 -0.0403 -0.0119 0.0536  100 VAL   A O   
2015 O O   B VAL   A 100 ? 0.3126 0.2376 0.2455 0.0234  -0.0282 0.0231  100 VAL   A O   
2016 C CB  A VAL   A 100 ? 0.2448 0.2798 0.1681 -0.0351 -0.0407 0.0230  100 VAL   A CB  
2017 C CB  B VAL   A 100 ? 0.3075 0.2547 0.2914 0.0091  0.0024  0.0223  100 VAL   A CB  
2018 C CG1 A VAL   A 100 ? 0.2473 0.2894 0.1950 -0.0426 -0.0303 0.0134  100 VAL   A CG1 
2019 C CG1 B VAL   A 100 ? 0.3096 0.2636 0.3106 0.0056  0.0092  0.0148  100 VAL   A CG1 
2020 C CG2 A VAL   A 100 ? 0.2558 0.2817 0.1837 -0.0372 -0.0369 0.0250  100 VAL   A CG2 
2021 C CG2 B VAL   A 100 ? 0.3103 0.2641 0.3083 0.0096  0.0049  0.0185  100 VAL   A CG2 
2040 N N   A ASN   A 101 ? 0.2392 0.2950 0.1504 -0.0507 -0.0324 0.0806  101 ASN   A N   
2041 N N   B ASN   A 101 ? 0.3236 0.2443 0.2558 0.0322  -0.0187 0.0187  101 ASN   A N   
2042 C CA  A ASN   A 101 ? 0.2556 0.3054 0.1695 -0.0605 -0.0229 0.0945  101 ASN   A CA  
2043 C CA  B ASN   A 101 ? 0.3367 0.2580 0.2677 0.0429  -0.0147 0.0192  101 ASN   A CA  
2044 C C   A ASN   A 101 ? 0.2771 0.3335 0.2093 -0.0629 0.0006  0.1084  101 ASN   A C   
2045 C C   B ASN   A 101 ? 0.3493 0.2752 0.2851 0.0409  -0.0083 0.0191  101 ASN   A C   
2046 O O   A ASN   A 101 ? 0.2962 0.3402 0.2476 -0.0619 0.0009  0.0994  101 ASN   A O   
2047 O O   B ASN   A 101 ? 0.3538 0.2774 0.2950 0.0421  -0.0091 0.0242  101 ASN   A O   
2048 C CB  A ASN   A 101 ? 0.2552 0.2908 0.1754 -0.0632 -0.0324 0.0754  101 ASN   A CB  
2049 C CB  B ASN   A 101 ? 0.3410 0.2609 0.2732 0.0471  -0.0140 0.0126  101 ASN   A CB  
2050 C CG  A ASN   A 101 ? 0.2577 0.2759 0.1811 -0.0647 -0.0341 0.0433  101 ASN   A CG  
2051 C CG  B ASN   A 101 ? 0.3459 0.2675 0.2795 0.0490  -0.0110 0.0045  101 ASN   A CG  
2052 O OD1 A ASN   A 101 ? 0.2522 0.2719 0.1719 -0.0491 -0.0303 0.0148  101 ASN   A OD1 
2053 O OD1 B ASN   A 101 ? 0.3503 0.2727 0.2892 0.0503  -0.0085 0.0052  101 ASN   A OD1 
2054 N ND2 A ASN   A 101 ? 0.2643 0.2681 0.1737 -0.0718 -0.0419 0.0394  101 ASN   A ND2 
2055 N ND2 B ASN   A 101 ? 0.3478 0.2714 0.2805 0.0470  -0.0052 -0.0019 101 ASN   A ND2 
2068 N N   A LYS   A 102 ? 0.2755 0.3572 0.2242 -0.0657 0.0169  0.1098  102 LYS   A N   
2069 N N   B LYS   A 102 ? 0.3560 0.2871 0.2934 0.0410  -0.0039 0.0175  102 LYS   A N   
2070 C CA  A LYS   A 102 ? 0.2829 0.3810 0.2301 -0.0622 0.0242  0.0964  102 LYS   A CA  
2071 C CA  B LYS   A 102 ? 0.3621 0.3021 0.2891 0.0347  0.0021  0.0168  102 LYS   A CA  
2072 C C   A LYS   A 102 ? 0.2964 0.4032 0.2326 -0.0491 0.0236  0.0805  102 LYS   A C   
2073 C C   B LYS   A 102 ? 0.3559 0.2976 0.2654 0.0331  0.0061  0.0325  102 LYS   A C   
2074 O O   A LYS   A 102 ? 0.2994 0.4162 0.2431 -0.0443 0.0252  0.0672  102 LYS   A O   
2075 O O   B LYS   A 102 ? 0.3575 0.2965 0.2680 0.0341  0.0121  0.0380  102 LYS   A O   
2076 C CB  A LYS   A 102 ? 0.2822 0.3824 0.2445 -0.0683 0.0293  0.0895  102 LYS   A CB  
2077 C CB  B LYS   A 102 ? 0.3733 0.3194 0.3147 0.0317  0.0001  0.0049  102 LYS   A CB  
2078 C CG  A LYS   A 102 ? 0.2844 0.3829 0.2580 -0.0719 0.0262  0.0789  102 LYS   A CG  
2079 C CG  B LYS   A 102 ? 0.3841 0.3362 0.3450 0.0275  -0.0055 -0.0025 102 LYS   A CG  
2080 C CD  A LYS   A 102 ? 0.2929 0.3859 0.2832 -0.0691 0.0220  0.0573  102 LYS   A CD  
2081 C CD  B LYS   A 102 ? 0.3939 0.3522 0.3771 0.0237  -0.0111 -0.0082 102 LYS   A CD  
2082 C CE  A LYS   A 102 ? 0.3018 0.3884 0.3042 -0.0633 0.0195  0.0383  102 LYS   A CE  
2083 C CE  B LYS   A 102 ? 0.4005 0.3630 0.4029 0.0217  -0.0154 -0.0113 102 LYS   A CE  
2084 N NZ  A LYS   A 102 ? 0.3078 0.3891 0.3182 -0.0614 0.0185  0.0228  102 LYS   A NZ  
2085 N NZ  B LYS   A 102 ? 0.4039 0.3696 0.4189 0.0199  -0.0150 -0.0134 102 LYS   A NZ  
2112 N N   A GLY   A 103 ? 0.3068 0.4138 0.2490 -0.0364 0.0154  0.0583  103 GLY   A N   
2113 N N   B GLY   A 103 ? 0.3467 0.2979 0.2461 0.0327  -0.0013 0.0325  103 GLY   A N   
2114 C CA  A GLY   A 103 ? 0.3187 0.4212 0.2595 -0.0240 0.0170  0.0405  103 GLY   A CA  
2115 C CA  B GLY   A 103 ? 0.3336 0.2931 0.2378 0.0347  -0.0097 0.0452  103 GLY   A CA  
2116 C C   A GLY   A 103 ? 0.3244 0.4280 0.2708 -0.0153 0.0221  0.0277  103 GLY   A C   
2117 C C   B GLY   A 103 ? 0.3171 0.2858 0.2217 0.0322  -0.0173 0.0547  103 GLY   A C   
2118 O O   A GLY   A 103 ? 0.3332 0.4333 0.2956 -0.0068 0.0196  0.0233  103 GLY   A O   
2119 O O   B GLY   A 103 ? 0.3244 0.2859 0.2280 0.0306  -0.0178 0.0560  103 GLY   A O   
2126 N N   A GLU   A 104 ? 0.3178 0.4256 0.2345 -0.0197 0.0358  0.0189  104 GLU   A N   
2127 N N   B GLU   A 104 ? 0.2910 0.2770 0.1941 0.0266  -0.0272 0.0589  104 GLU   A N   
2128 C CA  A GLU   A 104 ? 0.3088 0.4204 0.2131 -0.0265 0.0371  0.0141  104 GLU   A CA  
2129 C CA  B GLU   A 104 ? 0.2702 0.2674 0.1640 0.0121  -0.0296 0.0586  104 GLU   A CA  
2130 C C   A GLU   A 104 ? 0.3209 0.4310 0.2156 -0.0291 0.0323  -0.0033 104 GLU   A C   
2131 C C   B GLU   A 104 ? 0.2666 0.2725 0.1701 0.0110  -0.0263 0.0427  104 GLU   A C   
2132 O O   A GLU   A 104 ? 0.3196 0.4348 0.2144 -0.0290 0.0228  -0.0100 104 GLU   A O   
2133 O O   B GLU   A 104 ? 0.2668 0.2674 0.1875 0.0133  -0.0260 0.0432  104 GLU   A O   
2134 C CB  A GLU   A 104 ? 0.2837 0.4047 0.2010 -0.0313 0.0419  0.0288  104 GLU   A CB  
2135 C CB  B GLU   A 104 ? 0.2589 0.2540 0.1545 -0.0038 -0.0240 0.0674  104 GLU   A CB  
2136 C CG  A GLU   A 104 ? 0.2632 0.3880 0.1985 -0.0316 0.0383  0.0364  104 GLU   A CG  
2137 C CG  B GLU   A 104 ? 0.2535 0.2501 0.1664 -0.0167 -0.0252 0.0689  104 GLU   A CG  
2138 C CD  A GLU   A 104 ? 0.2424 0.3696 0.1832 -0.0335 0.0379  0.0527  104 GLU   A CD  
2139 C CD  B GLU   A 104 ? 0.2527 0.2503 0.1781 -0.0245 -0.0293 0.0678  104 GLU   A CD  
2140 O OE1 A GLU   A 104 ? 0.2230 0.3576 0.1487 -0.0376 0.0302  0.0586  104 GLU   A OE1 
2141 O OE1 B GLU   A 104 ? 0.2515 0.2547 0.1774 -0.0239 -0.0360 0.0646  104 GLU   A OE1 
2142 O OE2 A GLU   A 104 ? 0.2527 0.3665 0.1996 -0.0309 0.0377  0.0665  104 GLU   A OE2 
2143 O OE2 B GLU   A 104 ? 0.2558 0.2481 0.1991 -0.0295 -0.0182 0.0659  104 GLU   A OE2 
2156 N N   A ASP   A 105 ? 0.3345 0.4373 0.2299 -0.0290 0.0370  -0.0214 105 ASP   A N   
2157 N N   B ASP   A 105 ? 0.2731 0.2815 0.1932 0.0028  -0.0249 0.0251  105 ASP   A N   
2158 C CA  A ASP   A 105 ? 0.3416 0.4438 0.2656 -0.0300 0.0408  -0.0392 105 ASP   A CA  
2159 C CA  B ASP   A 105 ? 0.2776 0.2875 0.2232 -0.0017 -0.0153 -0.0056 105 ASP   A CA  
2160 C C   A ASP   A 105 ? 0.3176 0.4359 0.2406 -0.0425 0.0301  -0.0583 105 ASP   A C   
2161 C C   B ASP   A 105 ? 0.2657 0.2810 0.1823 -0.0151 -0.0139 -0.0257 105 ASP   A C   
2162 O O   A ASP   A 105 ? 0.3107 0.4359 0.2125 -0.0418 0.0341  -0.0764 105 ASP   A O   
2163 O O   B ASP   A 105 ? 0.2485 0.2671 0.1030 -0.0149 -0.0161 -0.0396 105 ASP   A O   
2164 C CB  A ASP   A 105 ? 0.3678 0.4562 0.3254 -0.0186 0.0502  -0.0403 105 ASP   A CB  
2165 C CB  B ASP   A 105 ? 0.2953 0.3006 0.2903 0.0068  -0.0054 -0.0206 105 ASP   A CB  
2166 C CG  A ASP   A 105 ? 0.3884 0.4675 0.3770 -0.0104 0.0523  -0.0421 105 ASP   A CG  
2167 C CG  B ASP   A 105 ? 0.3102 0.3114 0.3440 0.0171  -0.0000 -0.0340 105 ASP   A CG  
2168 O OD1 A ASP   A 105 ? 0.3926 0.4721 0.3863 -0.0088 0.0511  -0.0477 105 ASP   A OD1 
2169 O OD1 B ASP   A 105 ? 0.3137 0.3131 0.3480 0.0171  -0.0036 -0.0393 105 ASP   A OD1 
2170 O OD2 A ASP   A 105 ? 0.3983 0.4720 0.4039 -0.0088 0.0569  -0.0360 105 ASP   A OD2 
2171 O OD2 B ASP   A 105 ? 0.3196 0.3181 0.3758 0.0226  -0.0015 -0.0371 105 ASP   A OD2 
2180 N N   A ILE   A 106 ? 0.2986 0.4242 0.2490 -0.0574 0.0028  -0.0645 106 ILE   A N   
2181 N N   B ILE   A 106 ? 0.2699 0.2937 0.2227 -0.0269 -0.0188 -0.0285 106 ILE   A N   
2182 C CA  A ILE   A 106 ? 0.2716 0.4071 0.2624 -0.0750 -0.0219 -0.0757 106 ILE   A CA  
2183 C CA  B ILE   A 106 ? 0.2705 0.3050 0.2558 -0.0432 -0.0247 -0.0381 106 ILE   A CA  
2184 C C   A ILE   A 106 ? 0.2504 0.3815 0.2631 -0.0982 -0.0190 -0.0931 106 ILE   A C   
2185 C C   B ILE   A 106 ? 0.2728 0.3067 0.2633 -0.0573 -0.0133 -0.0440 106 ILE   A C   
2186 O O   A ILE   A 106 ? 0.2247 0.3726 0.2556 -0.1059 -0.0104 -0.0966 106 ILE   A O   
2187 O O   B ILE   A 106 ? 0.2662 0.3074 0.2604 -0.0598 -0.0077 -0.0434 106 ILE   A O   
2188 C CB  A ILE   A 106 ? 0.2740 0.4154 0.2988 -0.0620 -0.0374 -0.0497 106 ILE   A CB  
2189 C CB  B ILE   A 106 ? 0.2736 0.3174 0.2915 -0.0403 -0.0357 -0.0251 106 ILE   A CB  
2190 C CG1 A ILE   A 106 ? 0.2689 0.4155 0.3308 -0.0507 -0.0440 -0.0298 106 ILE   A CG1 
2191 C CG1 B ILE   A 106 ? 0.2709 0.3248 0.3163 -0.0345 -0.0412 -0.0139 106 ILE   A CG1 
2192 C CG2 A ILE   A 106 ? 0.2792 0.4182 0.3055 -0.0600 -0.0418 -0.0453 106 ILE   A CG2 
2193 C CG2 B ILE   A 106 ? 0.2763 0.3192 0.2941 -0.0415 -0.0374 -0.0220 106 ILE   A CG2 
2194 C CD1 A ILE   A 106 ? 0.2704 0.4140 0.3494 -0.0390 -0.0395 -0.0173 106 ILE   A CD1 
2195 C CD1 B ILE   A 106 ? 0.2723 0.3270 0.3344 -0.0270 -0.0387 -0.0068 106 ILE   A CD1 
2218 N N   A GLN   A 107 ? 0.2705 0.3681 0.2901 -0.0960 -0.0037 -0.1027 107 GLN   A N   
2219 N N   B GLN   A 107 ? 0.2866 0.3054 0.2791 -0.0622 0.0004  -0.0519 107 GLN   A N   
2220 C CA  A GLN   A 107 ? 0.2940 0.3540 0.3533 -0.0809 0.0229  -0.0944 107 GLN   A CA  
2221 C CA  B GLN   A 107 ? 0.3024 0.3090 0.3277 -0.0624 0.0173  -0.0528 107 GLN   A CA  
2222 C C   A GLN   A 107 ? 0.2644 0.3043 0.3376 -0.0696 0.0518  -0.0791 107 GLN   A C   
2223 C C   B GLN   A 107 ? 0.2728 0.2822 0.3163 -0.0665 0.0396  -0.0603 107 GLN   A C   
2224 O O   A GLN   A 107 ? 0.2612 0.2964 0.3785 -0.0625 0.0727  -0.0856 107 GLN   A O   
2225 O O   B GLN   A 107 ? 0.2760 0.2772 0.3436 -0.0758 0.0410  -0.0675 107 GLN   A O   
2226 C CB  A GLN   A 107 ? 0.3399 0.3876 0.4417 -0.0800 0.0160  -0.0867 107 GLN   A CB  
2227 C CB  B GLN   A 107 ? 0.3415 0.3391 0.3893 -0.0617 0.0084  -0.0429 107 GLN   A CB  
2228 C CG  A GLN   A 107 ? 0.3817 0.4190 0.5319 -0.0753 0.0088  -0.0724 107 GLN   A CG  
2229 C CG  B GLN   A 107 ? 0.3753 0.3652 0.4527 -0.0598 -0.0008 -0.0295 107 GLN   A CG  
2230 C CD  A GLN   A 107 ? 0.4158 0.4429 0.6114 -0.0705 0.0039  -0.0575 107 GLN   A CD  
2231 C CD  B GLN   A 107 ? 0.4036 0.3882 0.5106 -0.0565 -0.0064 -0.0151 107 GLN   A CD  
2232 O OE1 A GLN   A 107 ? 0.4274 0.4501 0.6436 -0.0711 0.0021  -0.0534 107 GLN   A OE1 
2233 O OE1 B GLN   A 107 ? 0.4142 0.3962 0.5255 -0.0579 -0.0063 -0.0069 107 GLN   A OE1 
2234 N NE2 A GLN   A 107 ? 0.4281 0.4506 0.6372 -0.0668 0.0017  -0.0530 107 GLN   A NE2 
2235 N NE2 B GLN   A 107 ? 0.4114 0.3973 0.5310 -0.0540 -0.0112 -0.0125 107 GLN   A NE2 
2252 N N   . LEU   A 108 ? 0.2407 0.2596 0.2789 -0.0623 0.0491  -0.0669 108 LEU   A N   
2253 C CA  . LEU   A 108 ? 0.2077 0.2043 0.2367 -0.0298 0.0427  -0.0297 108 LEU   A CA  
2254 C C   . LEU   A 108 ? 0.1827 0.1550 0.2129 -0.0092 0.0316  -0.0031 108 LEU   A C   
2255 O O   . LEU   A 108 ? 0.1800 0.1585 0.2287 -0.0017 0.0326  0.0040  108 LEU   A O   
2256 C CB  . LEU   A 108 ? 0.2133 0.2159 0.2169 -0.0287 0.0451  -0.0288 108 LEU   A CB  
2257 C CG  . LEU   A 108 ? 0.2281 0.2405 0.2349 -0.0220 0.0572  -0.0304 108 LEU   A CG  
2258 C CD1 . LEU   A 108 ? 0.2481 0.2463 0.2435 -0.0298 0.0645  -0.0202 108 LEU   A CD1 
2259 C CD2 . LEU   A 108 ? 0.2270 0.2643 0.2742 -0.0142 0.0553  -0.0223 108 LEU   A CD2 
2272 N N   . LEU   A 109 ? 0.1675 0.1513 0.2069 0.0027  0.0232  0.0138  109 LEU   A N   
2273 C CA  . LEU   A 109 ? 0.1629 0.1447 0.1843 0.0009  0.0078  0.0158  109 LEU   A CA  
2274 C C   . LEU   A 109 ? 0.1473 0.1398 0.1705 -0.0097 0.0109  0.0075  109 LEU   A C   
2275 O O   . LEU   A 109 ? 0.1526 0.1348 0.1906 -0.0048 0.0018  0.0036  109 LEU   A O   
2276 C CB  . LEU   A 109 ? 0.1675 0.1496 0.2012 0.0063  0.0040  0.0211  109 LEU   A CB  
2277 C CG  . LEU   A 109 ? 0.1557 0.1602 0.2150 0.0033  0.0063  0.0308  109 LEU   A CG  
2278 C CD1 . LEU   A 109 ? 0.1611 0.1544 0.2265 0.0012  0.0179  0.0063  109 LEU   A CD1 
2279 C CD2 . LEU   A 109 ? 0.1534 0.1872 0.2426 -0.0020 0.0002  0.0307  109 LEU   A CD2 
2291 N N   . LYS   A 110 ? 0.1493 0.1402 0.1746 -0.0064 -0.0065 0.0008  110 LYS   A N   
2292 C CA  . LYS   A 110 ? 0.1436 0.1325 0.1910 -0.0091 -0.0043 0.0103  110 LYS   A CA  
2293 C C   . LYS   A 110 ? 0.1436 0.1290 0.1714 -0.0051 0.0034  -0.0020 110 LYS   A C   
2294 O O   . LYS   A 110 ? 0.1426 0.1357 0.1779 -0.0094 0.0043  -0.0051 110 LYS   A O   
2295 C CB  . LYS   A 110 ? 0.1549 0.1423 0.2140 -0.0105 -0.0095 0.0005  110 LYS   A CB  
2296 C CG  . LYS   A 110 ? 0.1598 0.1374 0.2288 -0.0050 -0.0194 -0.0054 110 LYS   A CG  
2297 C CD  . LYS   A 110 ? 0.1604 0.1407 0.2384 -0.0112 -0.0144 -0.0100 110 LYS   A CD  
2298 C CE  . LYS   A 110 ? 0.1636 0.1487 0.2480 -0.0115 0.0029  -0.0097 110 LYS   A CE  
2299 N NZ  . LYS   A 110 ? 0.1654 0.1568 0.2638 -0.0213 0.0151  -0.0064 110 LYS   A NZ  
2313 N N   . SER   A 111 ? 0.1472 0.1348 0.1839 -0.0016 0.0026  0.0029  111 SER   A N   
2314 C CA  . SER   A 111 ? 0.1389 0.1384 0.1821 -0.0024 0.0054  0.0035  111 SER   A CA  
2315 C C   . SER   A 111 ? 0.1345 0.1329 0.1886 -0.0074 0.0079  0.0072  111 SER   A C   
2316 O O   . SER   A 111 ? 0.1458 0.1276 0.2049 -0.0055 0.0110  0.0054  111 SER   A O   
2317 C CB  . SER   A 111 ? 0.1579 0.1606 0.1971 -0.0065 0.0108  -0.0103 111 SER   A CB  
2318 O OG  . SER   A 111 ? 0.2003 0.1773 0.2001 0.0014  0.0167  -0.0170 111 SER   A OG  
2324 N N   . ALA   A 112 ? 0.1422 0.1261 0.1956 -0.0026 0.0108  0.0087  112 ALA   A N   
2325 C CA  . ALA   A 112 ? 0.1425 0.1224 0.1849 -0.0052 0.0170  0.0044  112 ALA   A CA  
2326 C C   . ALA   A 112 ? 0.1369 0.1238 0.1871 -0.0031 0.0120  0.0061  112 ALA   A C   
2327 O O   . ALA   A 112 ? 0.1384 0.1252 0.1962 -0.0112 0.0156  0.0087  112 ALA   A O   
2328 C CB  . ALA   A 112 ? 0.1552 0.1291 0.1781 -0.0054 0.0129  0.0033  112 ALA   A CB  
2334 N N   . TYR   A 113 ? 0.1270 0.1282 0.1925 -0.0071 0.0096  0.0124  113 TYR   A N   
2335 C CA  . TYR   A 113 ? 0.1268 0.1253 0.1893 -0.0029 0.0108  0.0115  113 TYR   A CA  
2336 C C   . TYR   A 113 ? 0.1249 0.1236 0.1758 -0.0127 0.0113  0.0067  113 TYR   A C   
2337 O O   . TYR   A 113 ? 0.1293 0.1325 0.1851 -0.0077 0.0200  0.0061  113 TYR   A O   
2338 C CB  . TYR   A 113 ? 0.1260 0.1378 0.1977 -0.0036 0.0033  0.0151  113 TYR   A CB  
2339 C CG  . TYR   A 113 ? 0.1302 0.1386 0.1852 -0.0134 0.0133  0.0179  113 TYR   A CG  
2340 C CD1 . TYR   A 113 ? 0.1299 0.1533 0.1905 -0.0064 0.0109  0.0212  113 TYR   A CD1 
2341 C CD2 . TYR   A 113 ? 0.1383 0.1397 0.1824 -0.0093 0.0124  0.0223  113 TYR   A CD2 
2342 C CE1 . TYR   A 113 ? 0.1354 0.1582 0.1827 -0.0031 0.0055  0.0185  113 TYR   A CE1 
2343 C CE2 . TYR   A 113 ? 0.1340 0.1511 0.1789 -0.0114 -0.0008 0.0241  113 TYR   A CE2 
2344 C CZ  . TYR   A 113 ? 0.1337 0.1562 0.1760 -0.0006 0.0059  0.0228  113 TYR   A CZ  
2345 O OH  . TYR   A 113 ? 0.1324 0.1629 0.2006 0.0073  0.0063  0.0211  113 TYR   A OH  
2355 N N   . GLU   A 114 ? 0.1277 0.1254 0.1878 -0.0076 0.0093  0.0141  114 GLU   A N   
2356 C CA  . GLU   A 114 ? 0.1324 0.1207 0.1965 0.0005  0.0071  0.0147  114 GLU   A CA  
2357 C C   . GLU   A 114 ? 0.1269 0.1283 0.1837 -0.0019 0.0171  0.0121  114 GLU   A C   
2358 O O   . GLU   A 114 ? 0.1370 0.1290 0.1852 -0.0005 0.0040  0.0113  114 GLU   A O   
2359 C CB  . GLU   A 114 ? 0.1319 0.1257 0.1978 -0.0034 0.0050  0.0126  114 GLU   A CB  
2360 C CG  . GLU   A 114 ? 0.1402 0.1267 0.2125 -0.0033 0.0127  0.0008  114 GLU   A CG  
2361 C CD  . GLU   A 114 ? 0.1480 0.1236 0.2132 -0.0070 0.0070  0.0059  114 GLU   A CD  
2362 O OE1 . GLU   A 114 ? 0.1535 0.1275 0.2132 -0.0078 0.0129  -0.0082 114 GLU   A OE1 
2363 O OE2 . GLU   A 114 ? 0.1694 0.1369 0.2257 -0.0113 0.0087  -0.0082 114 GLU   A OE2 
2370 N N   . ASN   A 115 ? 0.1308 0.1271 0.1775 -0.0094 0.0089  0.0104  115 ASN   A N   
2371 C CA  . ASN   A 115 ? 0.1309 0.1271 0.1804 -0.0104 0.0167  0.0122  115 ASN   A CA  
2372 C C   . ASN   A 115 ? 0.1297 0.1263 0.1830 -0.0127 0.0029  0.0065  115 ASN   A C   
2373 O O   . ASN   A 115 ? 0.1312 0.1380 0.1901 -0.0081 0.0113  0.0118  115 ASN   A O   
2374 C CB  . ASN   A 115 ? 0.1432 0.1387 0.1785 -0.0148 0.0104  0.0052  115 ASN   A CB  
2375 C CG  . ASN   A 115 ? 0.1423 0.1570 0.1846 -0.0188 0.0170  0.0040  115 ASN   A CG  
2376 O OD1 . ASN   A 115 ? 0.1406 0.2534 0.2068 -0.0117 0.0241  0.0197  115 ASN   A OD1 
2377 N ND2 . ASN   A 115 ? 0.1451 0.1386 0.1826 -0.0134 0.0262  0.0104  115 ASN   A ND2 
2384 N N   . PHE   A 116 ? 0.1279 0.1269 0.1841 -0.0051 0.0120  0.0234  116 PHE   A N   
2385 C CA  . PHE   A 116 ? 0.1308 0.1350 0.1718 -0.0042 0.0085  0.0163  116 PHE   A CA  
2386 C C   . PHE   A 116 ? 0.1263 0.1403 0.1697 -0.0098 0.0089  0.0223  116 PHE   A C   
2387 O O   . PHE   A 116 ? 0.1324 0.1492 0.1804 0.0023  0.0141  0.0288  116 PHE   A O   
2388 C CB  . PHE   A 116 ? 0.1307 0.1274 0.1909 -0.0065 0.0187  0.0234  116 PHE   A CB  
2389 C CG  . PHE   A 116 ? 0.1293 0.1280 0.1777 -0.0097 0.0124  0.0153  116 PHE   A CG  
2390 C CD1 . PHE   A 116 ? 0.1308 0.1331 0.1763 -0.0065 0.0105  0.0129  116 PHE   A CD1 
2391 C CD2 . PHE   A 116 ? 0.1362 0.1365 0.1834 -0.0081 0.0155  0.0171  116 PHE   A CD2 
2392 C CE1 . PHE   A 116 ? 0.1381 0.1319 0.1829 -0.0130 0.0016  0.0075  116 PHE   A CE1 
2393 C CE2 . PHE   A 116 ? 0.1327 0.1304 0.1936 -0.0095 0.0159  0.0153  116 PHE   A CE2 
2394 C CZ  . PHE   A 116 ? 0.1393 0.1224 0.1843 -0.0027 0.0025  0.0149  116 PHE   A CZ  
2404 N N   . ASN   A 117 ? 0.1290 0.1350 0.1948 -0.0056 0.0145  0.0223  117 ASN   A N   
2405 C CA  . ASN   A 117 ? 0.1322 0.1345 0.2055 -0.0043 0.0122  0.0289  117 ASN   A CA  
2406 C C   . ASN   A 117 ? 0.1365 0.1448 0.2140 -0.0022 0.0141  0.0275  117 ASN   A C   
2407 O O   . ASN   A 117 ? 0.1410 0.1531 0.2280 -0.0071 -0.0096 0.0374  117 ASN   A O   
2408 C CB  . ASN   A 117 ? 0.1341 0.1331 0.1975 -0.0054 0.0082  0.0333  117 ASN   A CB  
2409 C CG  . ASN   A 117 ? 0.1318 0.1347 0.1961 -0.0012 0.0107  0.0261  117 ASN   A CG  
2410 O OD1 . ASN   A 117 ? 0.1345 0.1605 0.2089 -0.0072 0.0122  0.0172  117 ASN   A OD1 
2411 N ND2 . ASN   A 117 ? 0.1300 0.1410 0.1930 -0.0028 0.0068  0.0250  117 ASN   A ND2 
2418 N N   . GLN   A 118 ? 0.1327 0.1425 0.2132 -0.0047 0.0013  0.0257  118 GLN   A N   
2419 C CA  . GLN   A 118 ? 0.1377 0.1611 0.2159 -0.0080 -0.0067 0.0255  118 GLN   A CA  
2420 C C   . GLN   A 118 ? 0.1417 0.1646 0.1985 -0.0094 -0.0007 0.0300  118 GLN   A C   
2421 O O   . GLN   A 118 ? 0.1453 0.1921 0.2282 0.0006  -0.0086 0.0072  118 GLN   A O   
2422 C CB  . GLN   A 118 ? 0.1357 0.1607 0.2219 -0.0078 0.0100  0.0297  118 GLN   A CB  
2423 C CG  . GLN   A 118 ? 0.1331 0.1599 0.2204 -0.0033 0.0096  0.0297  118 GLN   A CG  
2424 C CD  . GLN   A 118 ? 0.1303 0.1647 0.2375 -0.0058 0.0042  0.0208  118 GLN   A CD  
2425 O OE1 . GLN   A 118 ? 0.1345 0.1757 0.2505 0.0070  0.0008  0.0150  118 GLN   A OE1 
2426 N NE2 . GLN   A 118 ? 0.1386 0.1585 0.2427 0.0008  -0.0041 0.0243  118 GLN   A NE2 
2435 N N   . HIS   A 119 ? 0.1494 0.1590 0.1821 -0.0075 0.0050  0.0299  119 HIS   A N   
2436 C CA  . HIS   A 119 ? 0.1550 0.1667 0.1830 -0.0086 -0.0008 0.0336  119 HIS   A CA  
2437 C C   . HIS   A 119 ? 0.1620 0.1742 0.1778 -0.0084 0.0031  0.0395  119 HIS   A C   
2438 O O   . HIS   A 119 ? 0.1667 0.1811 0.1768 -0.0213 -0.0024 0.0378  119 HIS   A O   
2439 C CB  . HIS   A 119 ? 0.1582 0.1569 0.2093 -0.0073 0.0203  0.0331  119 HIS   A CB  
2440 C CG  . HIS   A 119 ? 0.1576 0.1621 0.2573 0.0024  0.0093  0.0395  119 HIS   A CG  
2441 N ND1 . HIS   A 119 ? 0.1708 0.1816 0.3129 -0.0102 0.0133  0.0271  119 HIS   A ND1 
2442 C CD2 . HIS   A 119 ? 0.1691 0.1721 0.2722 0.0160  0.0307  0.0585  119 HIS   A CD2 
2443 C CE1 . HIS   A 119 ? 0.1702 0.1832 0.3196 -0.0137 0.0309  0.0516  119 HIS   A CE1 
2444 N NE2 . HIS   A 119 ? 0.1783 0.1781 0.3074 0.0027  0.0442  0.0647  119 HIS   A NE2 
2452 N N   . GLU   A 120 ? 0.1676 0.1954 0.1859 -0.0064 -0.0015 0.0603  120 GLU   A N   
2453 C CA  . GLU   A 120 ? 0.1910 0.2251 0.2174 0.0016  0.0012  0.0974  120 GLU   A CA  
2454 C C   . GLU   A 120 ? 0.1692 0.2135 0.1925 -0.0109 0.0013  0.0869  120 GLU   A C   
2455 O O   . GLU   A 120 ? 0.1716 0.2003 0.2127 -0.0108 0.0050  0.0807  120 GLU   A O   
2456 C CB  . GLU   A 120 ? 0.2539 0.2866 0.2758 0.0210  -0.0019 0.1474  120 GLU   A CB  
2457 C CG  . GLU   A 120 ? 0.3501 0.3572 0.4021 0.0373  -0.0091 0.1447  120 GLU   A CG  
2458 C CD  . GLU   A 120 ? 0.4433 0.4271 0.5290 0.0483  -0.0071 0.1220  120 GLU   A CD  
2459 O OE1 . GLU   A 120 ? 0.4728 0.4376 0.5633 0.0504  -0.0079 0.1139  120 GLU   A OE1 
2460 O OE2 . GLU   A 120 ? 0.4757 0.4596 0.5781 0.0502  -0.0063 0.1123  120 GLU   A OE2 
2467 N N   . VAL   A 121 ? 0.1665 0.2169 0.1719 -0.0130 0.0016  0.0659  121 VAL   A N   
2468 C CA  . VAL   A 121 ? 0.1768 0.2206 0.1621 -0.0196 0.0085  0.0665  121 VAL   A CA  
2469 C C   . VAL   A 121 ? 0.1674 0.2049 0.1515 -0.0252 0.0121  0.0485  121 VAL   A C   
2470 O O   . VAL   A 121 ? 0.1674 0.2043 0.1683 -0.0306 -0.0003 0.0365  121 VAL   A O   
2471 C CB  . VAL   A 121 ? 0.2146 0.2551 0.1896 -0.0071 0.0200  0.0771  121 VAL   A CB  
2472 C CG1 . VAL   A 121 ? 0.2161 0.2688 0.1942 0.0027  0.0222  0.0809  121 VAL   A CG1 
2473 C CG2 . VAL   A 121 ? 0.2373 0.2728 0.2268 -0.0156 0.0215  0.0577  121 VAL   A CG2 
2483 N N   . LEU   A 122 ? 0.1541 0.1766 0.1557 -0.0237 0.0077  0.0418  122 LEU   A N   
2484 C CA  . LEU   A 122 ? 0.1593 0.1582 0.1502 -0.0224 0.0188  0.0428  122 LEU   A CA  
2485 C C   . LEU   A 122 ? 0.1511 0.1587 0.1547 -0.0269 0.0093  0.0278  122 LEU   A C   
2486 O O   . LEU   A 122 ? 0.1527 0.1689 0.1843 -0.0277 0.0054  0.0362  122 LEU   A O   
2487 C CB  . LEU   A 122 ? 0.1807 0.1641 0.1782 -0.0111 0.0129  0.0446  122 LEU   A CB  
2488 C CG  . LEU   A 122 ? 0.1782 0.1700 0.1732 -0.0097 0.0189  0.0344  122 LEU   A CG  
2489 C CD1 . LEU   A 122 ? 0.1965 0.1688 0.1880 -0.0232 0.0223  0.0312  122 LEU   A CD1 
2490 C CD2 . LEU   A 122 ? 0.1722 0.1709 0.1669 -0.0042 0.0306  0.0243  122 LEU   A CD2 
2502 N N   A LEU   A 123 ? 0.1484 0.1552 0.1453 -0.0225 0.0020  0.0277  123 LEU   A N   
2503 N N   B LEU   A 123 ? 0.1493 0.1582 0.1505 -0.0213 0.0022  0.0276  123 LEU   A N   
2504 C CA  A LEU   A 123 ? 0.1472 0.1601 0.1263 -0.0210 0.0068  0.0320  123 LEU   A CA  
2505 C CA  B LEU   A 123 ? 0.1493 0.1629 0.1479 -0.0164 0.0009  0.0254  123 LEU   A CA  
2506 C C   A LEU   A 123 ? 0.1444 0.1516 0.1274 -0.0159 0.0035  0.0286  123 LEU   A C   
2507 C C   B LEU   A 123 ? 0.1459 0.1580 0.1341 -0.0125 0.0043  0.0218  123 LEU   A C   
2508 O O   A LEU   A 123 ? 0.1334 0.1494 0.1531 -0.0216 0.0098  0.0230  123 LEU   A O   
2509 O O   B LEU   A 123 ? 0.1389 0.1541 0.1390 -0.0191 0.0110  0.0226  123 LEU   A O   
2510 C CB  A LEU   A 123 ? 0.1546 0.1696 0.1129 -0.0276 0.0267  0.0265  123 LEU   A CB  
2511 C CB  B LEU   A 123 ? 0.1567 0.1721 0.1515 -0.0196 -0.0034 0.0245  123 LEU   A CB  
2512 C CG  A LEU   A 123 ? 0.1630 0.1850 0.1295 -0.0164 0.0212  0.0043  123 LEU   A CG  
2513 C CG  B LEU   A 123 ? 0.1612 0.1801 0.1602 -0.0207 -0.0061 0.0223  123 LEU   A CG  
2514 C CD1 A LEU   A 123 ? 0.1626 0.1855 0.1607 -0.0069 0.0267  -0.0063 123 LEU   A CD1 
2515 C CD1 B LEU   A 123 ? 0.1647 0.1819 0.1742 -0.0204 -0.0024 0.0177  123 LEU   A CD1 
2516 C CD2 A LEU   A 123 ? 0.1728 0.1942 0.1296 -0.0113 0.0102  0.0118  123 LEU   A CD2 
2517 C CD2 B LEU   A 123 ? 0.1679 0.1841 0.1682 -0.0174 -0.0088 0.0261  123 LEU   A CD2 
2540 N N   A ALA   A 124 ? 0.1449 0.1448 0.1197 -0.0188 0.0034  0.0276  124 ALA   A N   
2541 N N   B ALA   A 124 ? 0.1446 0.1501 0.1259 -0.0079 0.0009  0.0176  124 ALA   A N   
2542 C CA  A ALA   A 124 ? 0.1396 0.1361 0.1377 -0.0210 0.0003  0.0178  124 ALA   A CA  
2543 C CA  B ALA   A 124 ? 0.1383 0.1435 0.1172 0.0029  0.0020  0.0154  124 ALA   A CA  
2544 C C   A ALA   A 124 ? 0.1289 0.1235 0.1365 -0.0150 0.0134  0.0125  124 ALA   A C   
2545 C C   B ALA   A 124 ? 0.1355 0.1447 0.1151 0.0028  0.0159  0.0065  124 ALA   A C   
2546 O O   A ALA   A 124 ? 0.1226 0.1283 0.1527 -0.0184 0.0245  0.0112  124 ALA   A O   
2547 O O   B ALA   A 124 ? 0.1354 0.1474 0.1207 0.0022  0.0215  0.0094  124 ALA   A O   
2548 C CB  A ALA   A 124 ? 0.1415 0.1303 0.1731 -0.0160 0.0027  0.0216  124 ALA   A CB  
2549 C CB  B ALA   A 124 ? 0.1312 0.1350 0.1373 0.0155  -0.0029 0.0252  124 ALA   A CB  
2560 N N   A PRO   A 125 ? 0.1206 0.1182 0.1403 -0.0087 0.0094  0.0142  125 PRO   A N   
2561 N N   B PRO   A 125 ? 0.1352 0.1399 0.1195 0.0010  0.0176  0.0075  125 PRO   A N   
2562 C CA  A PRO   A 125 ? 0.1269 0.1231 0.1450 0.0003  0.0114  0.0149  125 PRO   A CA  
2563 C CA  B PRO   A 125 ? 0.1471 0.1449 0.1312 0.0067  0.0153  -0.0053 125 PRO   A CA  
2564 C C   A PRO   A 125 ? 0.1167 0.1296 0.1490 -0.0080 0.0064  0.0217  125 PRO   A C   
2565 C C   B PRO   A 125 ? 0.1505 0.1509 0.1349 0.0048  0.0113  -0.0027 125 PRO   A C   
2566 O O   A PRO   A 125 ? 0.1253 0.1368 0.1454 0.0027  0.0119  0.0113  125 PRO   A O   
2567 O O   B PRO   A 125 ? 0.1506 0.1467 0.1168 0.0078  0.0208  0.0066  125 PRO   A O   
2568 C CB  A PRO   A 125 ? 0.1316 0.1161 0.1319 -0.0020 0.0211  0.0174  125 PRO   A CB  
2569 C CB  B PRO   A 125 ? 0.1487 0.1469 0.1272 0.0082  0.0293  -0.0068 125 PRO   A CB  
2570 C CG  A PRO   A 125 ? 0.1273 0.1107 0.1267 -0.0013 0.0200  0.0100  125 PRO   A CG  
2571 C CG  B PRO   A 125 ? 0.1519 0.1480 0.1290 0.0057  0.0300  -0.0005 125 PRO   A CG  
2572 C CD  A PRO   A 125 ? 0.1199 0.1113 0.1349 -0.0055 0.0165  0.0068  125 PRO   A CD  
2573 C CD  B PRO   A 125 ? 0.1424 0.1461 0.1319 -0.0008 0.0273  0.0025  125 PRO   A CD  
2588 N N   A LEU   A 126 ? 0.1115 0.1405 0.1604 -0.0002 0.0057  0.0178  126 LEU   A N   
2589 N N   B LEU   A 126 ? 0.1644 0.1617 0.1464 -0.0018 0.0024  -0.0073 126 LEU   A N   
2590 C CA  A LEU   A 126 ? 0.1186 0.1459 0.1536 -0.0035 0.0087  0.0190  126 LEU   A CA  
2591 C CA  B LEU   A 126 ? 0.1728 0.1662 0.1663 -0.0001 0.0019  -0.0033 126 LEU   A CA  
2592 C C   A LEU   A 126 ? 0.1347 0.1379 0.1498 -0.0029 0.0074  0.0107  126 LEU   A C   
2593 C C   B LEU   A 126 ? 0.1701 0.1564 0.1643 0.0138  0.0148  0.0091  126 LEU   A C   
2594 O O   A LEU   A 126 ? 0.1526 0.1275 0.1556 -0.0040 0.0094  -0.0011 126 LEU   A O   
2595 O O   B LEU   A 126 ? 0.1834 0.1472 0.1915 0.0106  0.0263  0.0089  126 LEU   A O   
2596 C CB  A LEU   A 126 ? 0.1222 0.1509 0.1501 -0.0117 0.0020  0.0190  126 LEU   A CB  
2597 C CB  B LEU   A 126 ? 0.1918 0.1886 0.2250 -0.0154 -0.0074 0.0002  126 LEU   A CB  
2598 C CG  A LEU   A 126 ? 0.1130 0.1718 0.1385 -0.0166 0.0061  0.0172  126 LEU   A CG  
2599 C CG  B LEU   A 126 ? 0.2069 0.2087 0.2798 -0.0193 -0.0147 0.0090  126 LEU   A CG  
2600 C CD1 A LEU   A 126 ? 0.1219 0.1893 0.1580 -0.0156 0.0075  0.0125  126 LEU   A CD1 
2601 C CD1 B LEU   A 126 ? 0.2116 0.2128 0.2930 -0.0258 -0.0140 0.0122  126 LEU   A CD1 
2602 C CD2 A LEU   A 126 ? 0.1316 0.1759 0.1548 -0.0281 -0.0021 0.0277  126 LEU   A CD2 
2603 C CD2 B LEU   A 126 ? 0.2099 0.2144 0.2908 -0.0189 -0.0144 0.0120  126 LEU   A CD2 
2626 N N   A LEU   A 127 ? 0.1344 0.1505 0.1399 -0.0053 0.0117  0.0263  127 LEU   A N   
2627 N N   B LEU   A 127 ? 0.1625 0.1576 0.1492 0.0172  0.0095  0.0186  127 LEU   A N   
2628 C CA  A LEU   A 127 ? 0.1327 0.1516 0.1367 -0.0075 0.0027  0.0174  127 LEU   A CA  
2629 C CA  B LEU   A 127 ? 0.1588 0.1647 0.1492 0.0102  0.0019  0.0213  127 LEU   A CA  
2630 C C   A LEU   A 127 ? 0.1364 0.1408 0.1324 -0.0036 -0.0013 0.0144  127 LEU   A C   
2631 C C   B LEU   A 127 ? 0.1564 0.1634 0.1646 0.0004  -0.0050 0.0075  127 LEU   A C   
2632 O O   A LEU   A 127 ? 0.1377 0.1367 0.1495 -0.0155 -0.0034 0.0188  127 LEU   A O   
2633 O O   B LEU   A 127 ? 0.1611 0.1656 0.1753 -0.0151 -0.0016 0.0102  127 LEU   A O   
2634 C CB  A LEU   A 127 ? 0.1416 0.1555 0.1475 0.0051  0.0086  0.0144  127 LEU   A CB  
2635 C CB  B LEU   A 127 ? 0.1621 0.1811 0.1489 0.0097  0.0027  0.0175  127 LEU   A CB  
2636 C CG  A LEU   A 127 ? 0.1452 0.1527 0.1497 0.0077  -0.0012 0.0214  127 LEU   A CG  
2637 C CG  B LEU   A 127 ? 0.1667 0.1944 0.1530 0.0084  0.0034  0.0239  127 LEU   A CG  
2638 C CD1 A LEU   A 127 ? 0.1517 0.1498 0.1606 0.0086  0.0043  0.0246  127 LEU   A CD1 
2639 C CD1 B LEU   A 127 ? 0.1629 0.1984 0.1705 0.0139  0.0150  0.0216  127 LEU   A CD1 
2640 C CD2 A LEU   A 127 ? 0.1533 0.1545 0.1649 0.0113  -0.0126 0.0232  127 LEU   A CD2 
2641 C CD2 B LEU   A 127 ? 0.1755 0.2017 0.1504 0.0035  -0.0011 0.0174  127 LEU   A CD2 
2664 N N   A SER   A 128 ? 0.1457 0.1433 0.1293 -0.0101 -0.0028 0.0144  128 SER   A N   
2665 N N   B SER   A 128 ? 0.1542 0.1641 0.1680 -0.0083 -0.0074 -0.0001 128 SER   A N   
2666 C CA  A SER   A 128 ? 0.1511 0.1342 0.1111 -0.0040 0.0033  0.0171  128 SER   A CA  
2667 C CA  B SER   A 128 ? 0.1559 0.1594 0.1609 -0.0081 0.0021  -0.0066 128 SER   A CA  
2668 C C   A SER   A 128 ? 0.1483 0.1391 0.1087 0.0010  0.0007  0.0156  128 SER   A C   
2669 C C   B SER   A 128 ? 0.1633 0.1688 0.1704 -0.0072 -0.0076 0.0001  128 SER   A C   
2670 O O   A SER   A 128 ? 0.1515 0.1527 0.1226 0.0024  0.0065  0.0064  128 SER   A O   
2671 O O   B SER   A 128 ? 0.1654 0.1749 0.1908 -0.0027 -0.0045 0.0018  128 SER   A O   
2672 C CB  A SER   A 128 ? 0.1498 0.1311 0.1171 0.0007  -0.0083 0.0206  128 SER   A CB  
2673 C CB  B SER   A 128 ? 0.1542 0.1582 0.1602 -0.0061 0.0007  -0.0021 128 SER   A CB  
2674 O OG  A SER   A 128 ? 0.1509 0.1423 0.1324 0.0059  -0.0058 0.0159  128 SER   A OG  
2675 O OG  B SER   A 128 ? 0.1518 0.1623 0.1619 -0.0056 0.0117  0.0110  128 SER   A OG  
2686 N N   A ALA   A 129 ? 0.1425 0.1461 0.1191 -0.0001 -0.0079 0.0239  129 ALA   A N   
2687 N N   B ALA   A 129 ? 0.1685 0.1759 0.1722 -0.0054 -0.0112 0.0019  129 ALA   A N   
2688 C CA  A ALA   A 129 ? 0.1359 0.1487 0.1293 0.0014  -0.0018 0.0272  129 ALA   A CA  
2689 C CA  B ALA   A 129 ? 0.1803 0.1865 0.1822 -0.0028 -0.0025 -0.0008 129 ALA   A CA  
2690 C C   A ALA   A 129 ? 0.1423 0.1451 0.1183 0.0017  0.0030  0.0026  129 ALA   A C   
2691 C C   B ALA   A 129 ? 0.1936 0.1929 0.1792 -0.0050 0.0009  0.0030  129 ALA   A C   
2692 O O   A ALA   A 129 ? 0.1509 0.1511 0.1178 0.0018  0.0126  0.0033  129 ALA   A O   
2693 O O   B ALA   A 129 ? 0.1925 0.1941 0.1749 -0.0045 0.0042  -0.0045 129 ALA   A O   
2694 C CB  A ALA   A 129 ? 0.1395 0.1631 0.1620 0.0055  0.0038  0.0394  129 ALA   A CB  
2695 C CB  B ALA   A 129 ? 0.1872 0.1989 0.2181 -0.0057 0.0070  -0.0100 129 ALA   A CB  
2706 N N   A GLY   A 130 ? 0.1441 0.1381 0.1488 0.0029  0.0071  0.0004  130 GLY   A N   
2707 N N   B GLY   A 130 ? 0.2093 0.2000 0.1818 -0.0054 0.0015  0.0066  130 GLY   A N   
2708 C CA  A GLY   A 130 ? 0.1583 0.1378 0.1493 0.0056  0.0048  0.0054  130 GLY   A CA  
2709 C CA  B GLY   A 130 ? 0.2217 0.2056 0.1991 -0.0037 0.0017  0.0068  130 GLY   A CA  
2710 C C   A GLY   A 130 ? 0.1591 0.1359 0.1338 0.0066  -0.0022 0.0086  130 GLY   A C   
2711 C C   B GLY   A 130 ? 0.2328 0.2136 0.2156 -0.0050 -0.0060 0.0086  130 GLY   A C   
2712 O O   A GLY   A 130 ? 0.1618 0.1385 0.1382 0.0019  -0.0109 0.0111  130 GLY   A O   
2713 O O   B GLY   A 130 ? 0.2354 0.2121 0.2221 -0.0060 -0.0129 0.0111  130 GLY   A O   
2720 N N   A ILE   A 131 ? 0.1706 0.1295 0.1296 -0.0052 -0.0009 0.0030  131 ILE   A N   
2721 N N   B ILE   A 131 ? 0.2405 0.2205 0.2338 -0.0061 -0.0077 0.0123  131 ILE   A N   
2722 C CA  A ILE   A 131 ? 0.1880 0.1290 0.1085 -0.0126 -0.0115 0.0008  131 ILE   A CA  
2723 C CA  B ILE   A 131 ? 0.2479 0.2272 0.2478 -0.0024 -0.0066 0.0119  131 ILE   A CA  
2724 C C   A ILE   A 131 ? 0.1729 0.1335 0.1072 -0.0060 -0.0103 0.0068  131 ILE   A C   
2725 C C   B ILE   A 131 ? 0.2376 0.2270 0.2409 0.0068  -0.0012 0.0226  131 ILE   A C   
2726 O O   A ILE   A 131 ? 0.1791 0.1310 0.1245 0.0018  -0.0064 0.0022  131 ILE   A O   
2727 O O   B ILE   A 131 ? 0.2438 0.2345 0.2437 0.0121  0.0055  0.0301  131 ILE   A O   
2728 C CB  A ILE   A 131 ? 0.2177 0.1466 0.1152 -0.0232 -0.0129 -0.0043 131 ILE   A CB  
2729 C CB  B ILE   A 131 ? 0.2652 0.2400 0.2756 -0.0067 -0.0093 0.0030  131 ILE   A CB  
2730 C CG1 A ILE   A 131 ? 0.2279 0.1820 0.1283 -0.0339 -0.0134 -0.0136 131 ILE   A CG1 
2731 C CG1 B ILE   A 131 ? 0.2729 0.2479 0.2805 -0.0142 -0.0096 -0.0041 131 ILE   A CG1 
2732 C CG2 A ILE   A 131 ? 0.2326 0.1313 0.1476 -0.0145 -0.0089 -0.0104 131 ILE   A CG2 
2733 C CG2 B ILE   A 131 ? 0.2733 0.2455 0.2923 -0.0039 -0.0110 0.0030  131 ILE   A CG2 
2734 C CD1 A ILE   A 131 ? 0.2322 0.1952 0.1590 -0.0406 -0.0129 -0.0227 131 ILE   A CD1 
2735 C CD1 B ILE   A 131 ? 0.2778 0.2491 0.2805 -0.0153 -0.0057 -0.0060 131 ILE   A CD1 
2758 N N   A PHE   A 132 ? 0.1630 0.1342 0.1054 -0.0116 0.0023  0.0077  132 PHE   A N   
2759 N N   B PHE   A 132 ? 0.2214 0.2161 0.2270 0.0092  -0.0060 0.0203  132 PHE   A N   
2760 C CA  A PHE   A 132 ? 0.1659 0.1423 0.1136 -0.0096 0.0049  0.0010  132 PHE   A CA  
2761 C CA  B PHE   A 132 ? 0.2110 0.2096 0.2202 0.0132  -0.0137 0.0178  132 PHE   A CA  
2762 C C   A PHE   A 132 ? 0.1658 0.1651 0.1099 -0.0092 -0.0044 -0.0020 132 PHE   A C   
2763 C C   B PHE   A 132 ? 0.2133 0.2153 0.2272 0.0202  -0.0151 0.0138  132 PHE   A C   
2764 O O   A PHE   A 132 ? 0.1765 0.1828 0.1394 -0.0118 0.0037  -0.0076 132 PHE   A O   
2765 O O   B PHE   A 132 ? 0.2234 0.2204 0.2383 0.0226  0.0015  0.0094  132 PHE   A O   
2766 C CB  A PHE   A 132 ? 0.1679 0.1344 0.1103 -0.0047 0.0056  0.0024  132 PHE   A CB  
2767 C CB  B PHE   A 132 ? 0.1984 0.2008 0.1959 0.0120  -0.0159 0.0300  132 PHE   A CB  
2768 C CG  A PHE   A 132 ? 0.1616 0.1347 0.1032 -0.0014 0.0013  -0.0026 132 PHE   A CG  
2769 C CG  B PHE   A 132 ? 0.1952 0.1995 0.1870 0.0152  -0.0184 0.0250  132 PHE   A CG  
2770 C CD1 A PHE   A 132 ? 0.1610 0.1509 0.1057 0.0028  0.0048  -0.0103 132 PHE   A CD1 
2771 C CD1 B PHE   A 132 ? 0.1959 0.2043 0.1898 0.0187  -0.0156 0.0165  132 PHE   A CD1 
2772 C CD2 A PHE   A 132 ? 0.1587 0.1438 0.1170 0.0033  0.0094  -0.0053 132 PHE   A CD2 
2773 C CD2 B PHE   A 132 ? 0.1941 0.2074 0.1981 0.0176  -0.0215 0.0222  132 PHE   A CD2 
2774 C CE1 A PHE   A 132 ? 0.1596 0.1566 0.1183 0.0010  -0.0007 -0.0047 132 PHE   A CE1 
2775 C CE1 B PHE   A 132 ? 0.1966 0.2059 0.1962 0.0196  -0.0254 0.0114  132 PHE   A CE1 
2776 C CE2 A PHE   A 132 ? 0.1551 0.1480 0.1313 0.0094  0.0030  0.0002  132 PHE   A CE2 
2777 C CE2 B PHE   A 132 ? 0.1923 0.2094 0.2060 0.0180  -0.0265 0.0126  132 PHE   A CE2 
2778 C CZ  A PHE   A 132 ? 0.1503 0.1505 0.1236 0.0015  0.0016  0.0003  132 PHE   A CZ  
2779 C CZ  B PHE   A 132 ? 0.1946 0.2083 0.2063 0.0166  -0.0335 0.0111  132 PHE   A CZ  
2798 N N   A GLY   A 133 ? 0.1660 0.1671 0.1055 -0.0054 -0.0115 0.0136  133 GLY   A N   
2799 N N   B GLY   A 133 ? 0.2125 0.2154 0.2224 0.0192  -0.0244 0.0152  133 GLY   A N   
2800 C CA  A GLY   A 133 ? 0.1809 0.1784 0.1247 -0.0060 -0.0215 0.0004  133 GLY   A CA  
2801 C CA  B GLY   A 133 ? 0.2133 0.2179 0.2227 0.0098  -0.0323 0.0021  133 GLY   A CA  
2802 C C   A GLY   A 133 ? 0.1876 0.1932 0.1450 -0.0139 -0.0414 -0.0091 133 GLY   A C   
2803 C C   B GLY   A 133 ? 0.2119 0.2207 0.2263 0.0033  -0.0450 -0.0059 133 GLY   A C   
2804 O O   A GLY   A 133 ? 0.1992 0.2138 0.1734 -0.0139 -0.0506 -0.0228 133 GLY   A O   
2805 O O   B GLY   A 133 ? 0.2117 0.2298 0.2323 0.0082  -0.0571 -0.0111 133 GLY   A O   
2812 N N   A ALA   A 134 ? 0.1849 0.1796 0.1394 -0.0206 -0.0286 -0.0023 134 ALA   A N   
2813 N N   B ALA   A 134 ? 0.2105 0.2112 0.2141 -0.0046 -0.0339 -0.0076 134 ALA   A N   
2814 C CA  A ALA   A 134 ? 0.1866 0.1811 0.1635 -0.0207 -0.0315 -0.0035 134 ALA   A CA  
2815 C CA  B ALA   A 134 ? 0.2135 0.2095 0.2158 -0.0133 -0.0348 -0.0075 134 ALA   A CA  
2816 C C   A ALA   A 134 ? 0.1879 0.1869 0.1863 -0.0212 -0.0225 0.0082  134 ALA   A C   
2817 C C   B ALA   A 134 ? 0.2124 0.2089 0.2254 -0.0189 -0.0340 0.0144  134 ALA   A C   
2818 O O   A ALA   A 134 ? 0.1956 0.1933 0.2083 -0.0131 0.0041  0.0152  134 ALA   A O   
2819 O O   B ALA   A 134 ? 0.2120 0.2118 0.2388 -0.0268 -0.0238 0.0303  134 ALA   A O   
2820 C CB  A ALA   A 134 ? 0.1938 0.1779 0.1785 -0.0160 -0.0343 -0.0121 134 ALA   A CB  
2821 C CB  B ALA   A 134 ? 0.2187 0.2063 0.2140 -0.0120 -0.0351 -0.0276 134 ALA   A CB  
2832 N N   A ASP   A 135 ? 0.1956 0.1927 0.2053 -0.0292 -0.0357 0.0268  135 ASP   A N   
2833 N N   B ASP   A 135 ? 0.2195 0.2091 0.2327 -0.0138 -0.0377 0.0204  135 ASP   A N   
2834 C CA  A ASP   A 135 ? 0.1926 0.1988 0.2274 -0.0359 -0.0536 0.0372  135 ASP   A CA  
2835 C CA  B ASP   A 135 ? 0.2200 0.2102 0.2418 -0.0093 -0.0387 0.0228  135 ASP   A CA  
2836 C C   A ASP   A 135 ? 0.1752 0.1842 0.2296 -0.0267 -0.0422 0.0476  135 ASP   A C   
2837 C C   B ASP   A 135 ? 0.2050 0.2013 0.2329 -0.0025 -0.0328 0.0356  135 ASP   A C   
2838 O O   A ASP   A 135 ? 0.1717 0.1765 0.2370 -0.0244 -0.0443 0.0508  135 ASP   A O   
2839 O O   B ASP   A 135 ? 0.2019 0.1937 0.2330 0.0022  -0.0364 0.0414  135 ASP   A O   
2840 C CB  A ASP   A 135 ? 0.2090 0.2214 0.2619 -0.0494 -0.0718 0.0312  135 ASP   A CB  
2841 C CB  B ASP   A 135 ? 0.2337 0.2222 0.2680 -0.0140 -0.0424 0.0151  135 ASP   A CB  
2842 C CG  A ASP   A 135 ? 0.2259 0.2366 0.2907 -0.0629 -0.0735 0.0312  135 ASP   A CG  
2843 C CG  B ASP   A 135 ? 0.2464 0.2357 0.2982 -0.0175 -0.0410 0.0057  135 ASP   A CG  
2844 O OD1 A ASP   A 135 ? 0.2208 0.2390 0.2864 -0.0720 -0.0840 0.0533  135 ASP   A OD1 
2845 O OD1 B ASP   A 135 ? 0.2538 0.2391 0.3170 -0.0167 -0.0361 0.0001  135 ASP   A OD1 
2846 O OD2 A ASP   A 135 ? 0.2552 0.2535 0.3357 -0.0593 -0.0472 0.0209  135 ASP   A OD2 
2847 O OD2 B ASP   A 135 ? 0.2480 0.2427 0.3140 -0.0183 -0.0487 0.0064  135 ASP   A OD2 
2856 N N   A PRO   A 136 ? 0.1555 0.1765 0.2416 -0.0179 -0.0244 0.0555  136 PRO   A N   
2857 N N   B PRO   A 136 ? 0.1908 0.1986 0.2375 -0.0021 -0.0193 0.0444  136 PRO   A N   
2858 C CA  A PRO   A 136 ? 0.1455 0.1730 0.2506 -0.0161 -0.0138 0.0428  136 PRO   A CA  
2859 C CA  B PRO   A 136 ? 0.1861 0.2021 0.2393 -0.0066 -0.0113 0.0395  136 PRO   A CA  
2860 C C   A PRO   A 136 ? 0.1282 0.1709 0.2514 -0.0084 -0.0093 0.0348  136 PRO   A C   
2861 C C   B PRO   A 136 ? 0.1775 0.2038 0.2317 0.0001  -0.0152 0.0380  136 PRO   A C   
2862 O O   A PRO   A 136 ? 0.1232 0.1769 0.2457 -0.0086 0.0007  0.0384  136 PRO   A O   
2863 O O   B PRO   A 136 ? 0.1776 0.1989 0.2247 0.0052  -0.0155 0.0363  136 PRO   A O   
2864 C CB  A PRO   A 136 ? 0.1613 0.1707 0.2586 -0.0181 -0.0083 0.0471  136 PRO   A CB  
2865 C CB  B PRO   A 136 ? 0.1894 0.1985 0.2435 -0.0102 -0.0065 0.0442  136 PRO   A CB  
2866 C CG  A PRO   A 136 ? 0.1684 0.1738 0.2601 -0.0198 -0.0132 0.0505  136 PRO   A CG  
2867 C CG  B PRO   A 136 ? 0.1955 0.1984 0.2507 -0.0068 -0.0102 0.0477  136 PRO   A CG  
2868 C CD  A PRO   A 136 ? 0.1607 0.1689 0.2476 -0.0196 -0.0185 0.0517  136 PRO   A CD  
2869 C CD  B PRO   A 136 ? 0.1900 0.1975 0.2504 -0.0016 -0.0102 0.0503  136 PRO   A CD  
2884 N N   A ILE   A 137 ? 0.1302 0.1681 0.2592 -0.0103 -0.0172 0.0357  137 ILE   A N   
2885 N N   B ILE   A 137 ? 0.1782 0.2058 0.2371 -0.0048 -0.0170 0.0364  137 ILE   A N   
2886 C CA  A ILE   A 137 ? 0.1341 0.1736 0.2524 -0.0137 -0.0326 0.0497  137 ILE   A CA  
2887 C CA  B ILE   A 137 ? 0.1831 0.2145 0.2361 -0.0041 -0.0227 0.0387  137 ILE   A CA  
2888 C C   A ILE   A 137 ? 0.1425 0.1766 0.2303 -0.0160 -0.0306 0.0517  137 ILE   A C   
2889 C C   B ILE   A 137 ? 0.1806 0.2174 0.2390 -0.0077 -0.0130 0.0266  137 ILE   A C   
2890 O O   A ILE   A 137 ? 0.1407 0.1662 0.2362 -0.0202 -0.0210 0.0417  137 ILE   A O   
2891 O O   B ILE   A 137 ? 0.1769 0.2208 0.2484 -0.0091 -0.0095 0.0236  137 ILE   A O   
2892 C CB  A ILE   A 137 ? 0.1419 0.1906 0.2578 -0.0175 -0.0415 0.0663  137 ILE   A CB  
2893 C CB  B ILE   A 137 ? 0.1952 0.2208 0.2377 -0.0058 -0.0362 0.0529  137 ILE   A CB  
2894 C CG1 A ILE   A 137 ? 0.1560 0.2169 0.2744 -0.0085 -0.0381 0.0825  137 ILE   A CG1 
2895 C CG1 B ILE   A 137 ? 0.2080 0.2281 0.2506 0.0033  -0.0404 0.0664  137 ILE   A CG1 
2896 C CG2 A ILE   A 137 ? 0.1465 0.1932 0.2577 -0.0293 -0.0479 0.0626  137 ILE   A CG2 
2897 C CG2 B ILE   A 137 ? 0.2001 0.2198 0.2381 -0.0085 -0.0392 0.0574  137 ILE   A CG2 
2898 C CD1 A ILE   A 137 ? 0.1716 0.2341 0.2849 -0.0056 -0.0295 0.0839  137 ILE   A CD1 
2899 C CD1 B ILE   A 137 ? 0.2164 0.2292 0.2597 0.0064  -0.0417 0.0769  137 ILE   A CD1 
2922 N N   A HIS   A 138 ? 0.1466 0.1943 0.2231 -0.0183 -0.0198 0.0410  138 HIS   A N   
2923 N N   B HIS   A 138 ? 0.1778 0.2218 0.2310 -0.0096 -0.0045 0.0117  138 HIS   A N   
2924 C CA  A HIS   A 138 ? 0.1563 0.2086 0.2078 -0.0162 -0.0169 0.0325  138 HIS   A CA  
2925 C CA  B HIS   A 138 ? 0.1742 0.2162 0.2132 -0.0103 -0.0049 0.0099  138 HIS   A CA  
2926 C C   A HIS   A 138 ? 0.1492 0.1925 0.2016 -0.0073 -0.0140 0.0321  138 HIS   A C   
2927 C C   B HIS   A 138 ? 0.1617 0.1993 0.2052 -0.0056 -0.0057 0.0210  138 HIS   A C   
2928 O O   A HIS   A 138 ? 0.1568 0.1899 0.2012 -0.0125 -0.0071 0.0253  138 HIS   A O   
2929 O O   B HIS   A 138 ? 0.1696 0.1989 0.2055 -0.0092 0.0001  0.0171  138 HIS   A O   
2930 C CB  A HIS   A 138 ? 0.1740 0.2309 0.2034 -0.0215 -0.0234 0.0240  138 HIS   A CB  
2931 C CB  B HIS   A 138 ? 0.1804 0.2247 0.2101 -0.0113 -0.0116 -0.0064 138 HIS   A CB  
2932 C CG  A HIS   A 138 ? 0.1927 0.2421 0.2144 -0.0293 -0.0202 0.0214  138 HIS   A CG  
2933 C CG  B HIS   A 138 ? 0.1894 0.2285 0.2201 -0.0145 -0.0142 -0.0219 138 HIS   A CG  
2934 N ND1 A HIS   A 138 ? 0.2066 0.2518 0.2334 -0.0300 -0.0160 0.0127  138 HIS   A ND1 
2935 N ND1 B HIS   A 138 ? 0.1974 0.2324 0.2319 -0.0143 -0.0103 -0.0317 138 HIS   A ND1 
2936 C CD2 A HIS   A 138 ? 0.1972 0.2498 0.2097 -0.0267 -0.0201 0.0251  138 HIS   A CD2 
2937 C CD2 B HIS   A 138 ? 0.1903 0.2280 0.2191 -0.0087 -0.0190 -0.0269 138 HIS   A CD2 
2938 C CE1 A HIS   A 138 ? 0.2102 0.2552 0.2335 -0.0271 -0.0155 0.0114  138 HIS   A CE1 
2939 C CE1 B HIS   A 138 ? 0.1981 0.2312 0.2305 -0.0113 -0.0152 -0.0375 138 HIS   A CE1 
2940 N NE2 A HIS   A 138 ? 0.2050 0.2562 0.2159 -0.0255 -0.0147 0.0171  138 HIS   A NE2 
2941 N NE2 B HIS   A 138 ? 0.1938 0.2289 0.2228 -0.0080 -0.0195 -0.0380 138 HIS   A NE2 
2956 N N   . SER   A 139 ? 0.1449 0.1879 0.1958 -0.0060 -0.0108 0.0316  139 SER   A N   
2957 C CA  . SER   A 139 ? 0.1394 0.1836 0.2022 -0.0089 -0.0031 0.0404  139 SER   A CA  
2958 C C   . SER   A 139 ? 0.1319 0.1739 0.2001 -0.0100 -0.0063 0.0271  139 SER   A C   
2959 O O   . SER   A 139 ? 0.1308 0.1714 0.2104 -0.0109 -0.0029 0.0325  139 SER   A O   
2960 C CB  . SER   A 139 ? 0.1366 0.1803 0.2135 -0.0116 -0.0008 0.0408  139 SER   A CB  
2961 O OG  . SER   A 139 ? 0.1431 0.1732 0.2241 -0.0177 -0.0149 0.0422  139 SER   A OG  
2968 N N   . LEU   A 140 ? 0.1314 0.1820 0.1867 -0.0062 -0.0045 0.0414  140 LEU   A N   
2969 C CA  . LEU   A 140 ? 0.1291 0.1756 0.1942 -0.0104 -0.0003 0.0299  140 LEU   A CA  
2970 C C   . LEU   A 140 ? 0.1247 0.1803 0.1959 -0.0134 -0.0052 0.0361  140 LEU   A C   
2971 O O   . LEU   A 140 ? 0.1328 0.1781 0.2235 -0.0066 -0.0042 0.0350  140 LEU   A O   
2972 C CB  . LEU   A 140 ? 0.1336 0.1860 0.2031 -0.0133 0.0050  0.0279  140 LEU   A CB  
2973 C CG  . LEU   A 140 ? 0.1350 0.2030 0.2085 -0.0223 0.0064  0.0461  140 LEU   A CG  
2974 C CD1 . LEU   A 140 ? 0.1467 0.2016 0.2112 -0.0167 0.0013  0.0439  140 LEU   A CD1 
2975 C CD2 . LEU   A 140 ? 0.1401 0.2223 0.2193 -0.0218 0.0098  0.0494  140 LEU   A CD2 
2987 N N   . ARG   A 141 ? 0.1400 0.1863 0.2107 -0.0161 -0.0101 0.0304  141 ARG   A N   
2988 C CA  . ARG   A 141 ? 0.1555 0.1956 0.2243 -0.0270 -0.0087 0.0131  141 ARG   A CA  
2989 C C   . ARG   A 141 ? 0.1535 0.1739 0.2132 -0.0248 -0.0092 0.0216  141 ARG   A C   
2990 O O   . ARG   A 141 ? 0.1548 0.1704 0.2248 -0.0248 -0.0007 0.0159  141 ARG   A O   
2991 C CB  . ARG   A 141 ? 0.1736 0.2219 0.2566 -0.0293 -0.0139 -0.0077 141 ARG   A CB  
2992 C CG  . ARG   A 141 ? 0.2057 0.2551 0.2894 -0.0391 -0.0135 -0.0123 141 ARG   A CG  
2993 C CD  . ARG   A 141 ? 0.2342 0.2809 0.3226 -0.0536 -0.0187 -0.0136 141 ARG   A CD  
2994 N NE  . ARG   A 141 ? 0.2234 0.3016 0.3443 -0.0645 -0.0281 -0.0033 141 ARG   A NE  
2995 C CZ  . ARG   A 141 ? 0.2244 0.3279 0.3578 -0.0762 -0.0206 0.0114  141 ARG   A CZ  
2996 N NH1 . ARG   A 141 ? 0.2149 0.3386 0.3559 -0.0786 -0.0054 0.0028  141 ARG   A NH1 
2997 N NH2 . ARG   A 141 ? 0.2318 0.3349 0.3761 -0.0691 -0.0248 0.0211  141 ARG   A NH2 
3011 N N   . VAL   A 142 ? 0.1460 0.1707 0.2022 -0.0175 -0.0070 0.0202  142 VAL   A N   
3012 C CA  . VAL   A 142 ? 0.1441 0.1639 0.2016 -0.0111 0.0102  0.0119  142 VAL   A CA  
3013 C C   . VAL   A 142 ? 0.1320 0.1560 0.2034 -0.0127 0.0005  0.0137  142 VAL   A C   
3014 O O   . VAL   A 142 ? 0.1355 0.1576 0.2190 -0.0003 0.0096  0.0136  142 VAL   A O   
3015 C CB  . VAL   A 142 ? 0.1546 0.1771 0.1950 -0.0143 0.0050  0.0135  142 VAL   A CB  
3016 C CG1 . VAL   A 142 ? 0.1554 0.1691 0.1902 -0.0215 0.0085  0.0150  142 VAL   A CG1 
3017 C CG2 . VAL   A 142 ? 0.1711 0.1880 0.2165 -0.0098 0.0053  0.0192  142 VAL   A CG2 
3027 N N   . CYS   A 143 ? 0.1382 0.1535 0.1908 -0.0179 0.0041  0.0140  143 CYS   A N   
3028 C CA  . CYS   A 143 ? 0.1359 0.1553 0.2062 -0.0133 0.0045  0.0234  143 CYS   A CA  
3029 C C   . CYS   A 143 ? 0.1317 0.1510 0.2074 -0.0071 -0.0012 0.0285  143 CYS   A C   
3030 O O   . CYS   A 143 ? 0.1323 0.1544 0.2062 -0.0041 0.0030  0.0233  143 CYS   A O   
3031 C CB  . CYS   A 143 ? 0.1419 0.1533 0.2079 -0.0040 0.0076  0.0302  143 CYS   A CB  
3032 S SG  . CYS   A 143 ? 0.1563 0.1676 0.2140 0.0024  0.0098  0.0203  143 CYS   A SG  
3038 N N   . VAL   A 144 ? 0.1299 0.1574 0.2354 -0.0139 0.0091  0.0379  144 VAL   A N   
3039 C CA  . VAL   A 144 ? 0.1358 0.1668 0.2722 -0.0130 0.0147  0.0437  144 VAL   A CA  
3040 C C   . VAL   A 144 ? 0.1397 0.1636 0.2597 -0.0190 -0.0132 0.0344  144 VAL   A C   
3041 O O   . VAL   A 144 ? 0.1534 0.1637 0.2716 -0.0102 -0.0088 0.0350  144 VAL   A O   
3042 C CB  . VAL   A 144 ? 0.1624 0.1966 0.3194 -0.0099 0.0269  0.0532  144 VAL   A CB  
3043 C CG1 . VAL   A 144 ? 0.1766 0.2144 0.3510 -0.0244 0.0147  0.0546  144 VAL   A CG1 
3044 C CG2 . VAL   A 144 ? 0.1456 0.2059 0.3252 -0.0032 0.0369  0.0567  144 VAL   A CG2 
3054 N N   . ASP   A 145 ? 0.1455 0.1560 0.2661 -0.0200 -0.0038 0.0172  145 ASP   A N   
3055 C CA  . ASP   A 145 ? 0.1612 0.1619 0.2663 -0.0237 -0.0123 0.0015  145 ASP   A CA  
3056 C C   . ASP   A 145 ? 0.1608 0.1516 0.2629 -0.0164 -0.0063 -0.0010 145 ASP   A C   
3057 O O   . ASP   A 145 ? 0.1717 0.1613 0.3126 -0.0189 -0.0085 -0.0336 145 ASP   A O   
3058 C CB  . ASP   A 145 ? 0.1744 0.1907 0.2857 -0.0302 -0.0202 0.0010  145 ASP   A CB  
3059 C CG  . ASP   A 145 ? 0.1936 0.2313 0.3176 -0.0527 -0.0298 0.0189  145 ASP   A CG  
3060 O OD1 . ASP   A 145 ? 0.1852 0.2475 0.3277 -0.0639 -0.0187 0.0269  145 ASP   A OD1 
3061 O OD2 . ASP   A 145 ? 0.2201 0.2523 0.3307 -0.0649 -0.0536 0.0160  145 ASP   A OD2 
3066 N N   . THR   A 146 ? 0.1460 0.1458 0.2137 -0.0145 0.0023  0.0136  146 THR   A N   
3067 C CA  . THR   A 146 ? 0.1414 0.1382 0.2053 -0.0058 0.0012  0.0102  146 THR   A CA  
3068 C C   . THR   A 146 ? 0.1375 0.1392 0.2130 -0.0033 0.0042  0.0164  146 THR   A C   
3069 O O   . THR   A 146 ? 0.1452 0.1501 0.2351 0.0023  -0.0024 0.0109  146 THR   A O   
3070 C CB  . THR   A 146 ? 0.1423 0.1438 0.2084 -0.0048 0.0020  0.0130  146 THR   A CB  
3071 O OG1 . THR   A 146 ? 0.1416 0.1611 0.2159 -0.0007 -0.0023 0.0082  146 THR   A OG1 
3072 C CG2 . THR   A 146 ? 0.1366 0.1439 0.2238 -0.0061 0.0069  0.0181  146 THR   A CG2 
3080 N N   . VAL   A 147 ? 0.1352 0.1424 0.2054 -0.0016 0.0050  0.0158  147 VAL   A N   
3081 C CA  . VAL   A 147 ? 0.1357 0.1451 0.2097 -0.0125 0.0216  0.0256  147 VAL   A CA  
3082 C C   . VAL   A 147 ? 0.1364 0.1445 0.2254 -0.0121 0.0164  0.0306  147 VAL   A C   
3083 O O   . VAL   A 147 ? 0.1381 0.1514 0.2372 -0.0165 0.0094  0.0338  147 VAL   A O   
3084 C CB  . VAL   A 147 ? 0.1462 0.1440 0.2024 -0.0098 0.0187  0.0249  147 VAL   A CB  
3085 C CG1 . VAL   A 147 ? 0.1813 0.1529 0.2008 -0.0050 0.0229  0.0214  147 VAL   A CG1 
3086 C CG2 . VAL   A 147 ? 0.1490 0.1433 0.2151 -0.0090 0.0093  0.0158  147 VAL   A CG2 
3096 N N   . ARG   A 148 ? 0.1342 0.1454 0.2220 -0.0152 0.0171  0.0439  148 ARG   A N   
3097 C CA  . ARG   A 148 ? 0.1456 0.1524 0.2217 -0.0109 0.0145  0.0449  148 ARG   A CA  
3098 C C   . ARG   A 148 ? 0.1566 0.1519 0.2169 -0.0125 0.0141  0.0595  148 ARG   A C   
3099 O O   . ARG   A 148 ? 0.1856 0.1631 0.2395 -0.0223 0.0180  0.0531  148 ARG   A O   
3100 C CB  . ARG   A 148 ? 0.1540 0.1537 0.2219 -0.0041 0.0232  0.0391  148 ARG   A CB  
3101 C CG  . ARG   A 148 ? 0.1700 0.1506 0.2537 -0.0073 0.0336  0.0299  148 ARG   A CG  
3102 C CD  . ARG   A 148 ? 0.1801 0.1518 0.2763 -0.0027 0.0400  0.0466  148 ARG   A CD  
3103 N NE  . ARG   A 148 ? 0.1793 0.1588 0.2788 0.0064  0.0436  0.0488  148 ARG   A NE  
3104 C CZ  . ARG   A 148 ? 0.1763 0.1481 0.2638 0.0015  0.0415  0.0373  148 ARG   A CZ  
3105 N NH1 . ARG   A 148 ? 0.1837 0.1469 0.2703 -0.0081 0.0422  0.0133  148 ARG   A NH1 
3106 N NH2 . ARG   A 148 ? 0.1654 0.1676 0.2615 0.0110  0.0409  0.0406  148 ARG   A NH2 
3120 N N   . THR   A 149 ? 0.1528 0.1608 0.2100 -0.0132 -0.0002 0.0493  149 THR   A N   
3121 C CA  . THR   A 149 ? 0.1523 0.1656 0.2138 -0.0132 0.0019  0.0500  149 THR   A CA  
3122 C C   . THR   A 149 ? 0.1486 0.1627 0.2065 -0.0194 0.0064  0.0534  149 THR   A C   
3123 O O   . THR   A 149 ? 0.1478 0.1704 0.2256 -0.0214 0.0107  0.0450  149 THR   A O   
3124 C CB  . THR   A 149 ? 0.1519 0.1768 0.2194 -0.0177 0.0072  0.0425  149 THR   A CB  
3125 O OG1 . THR   A 149 ? 0.1591 0.1628 0.2289 -0.0236 0.0055  0.0356  149 THR   A OG1 
3126 C CG2 . THR   A 149 ? 0.1515 0.1928 0.2243 -0.0134 -0.0025 0.0349  149 THR   A CG2 
3134 N N   . ASN   A 150 ? 0.1519 0.1686 0.2058 -0.0131 0.0018  0.0608  150 ASN   A N   
3135 C CA  . ASN   A 150 ? 0.1680 0.1778 0.2057 -0.0171 0.0057  0.0478  150 ASN   A CA  
3136 C C   . ASN   A 150 ? 0.1488 0.1627 0.2103 -0.0193 0.0046  0.0457  150 ASN   A C   
3137 O O   . ASN   A 150 ? 0.1589 0.1744 0.2384 -0.0158 -0.0065 0.0422  150 ASN   A O   
3138 C CB  . ASN   A 150 ? 0.2145 0.2052 0.2250 -0.0225 0.0303  0.0633  150 ASN   A CB  
3139 C CG  . ASN   A 150 ? 0.2675 0.2386 0.2834 -0.0173 0.0134  0.0685  150 ASN   A CG  
3140 O OD1 . ASN   A 150 ? 0.2885 0.2496 0.3031 -0.0227 0.0165  0.0805  150 ASN   A OD1 
3141 N ND2 . ASN   A 150 ? 0.2961 0.2608 0.3302 -0.0112 -0.0056 0.0679  150 ASN   A ND2 
3148 N N   . VAL   A 151 ? 0.1495 0.1504 0.2098 -0.0181 0.0006  0.0440  151 VAL   A N   
3149 C CA  . VAL   A 151 ? 0.1520 0.1547 0.2054 -0.0261 0.0040  0.0480  151 VAL   A CA  
3150 C C   . VAL   A 151 ? 0.1402 0.1570 0.2091 -0.0279 0.0062  0.0512  151 VAL   A C   
3151 O O   . VAL   A 151 ? 0.1477 0.1639 0.2433 -0.0197 0.0051  0.0450  151 VAL   A O   
3152 C CB  . VAL   A 151 ? 0.1763 0.1757 0.1993 -0.0147 0.0119  0.0478  151 VAL   A CB  
3153 C CG1 . VAL   A 151 ? 0.1795 0.1957 0.2200 -0.0159 0.0105  0.0427  151 VAL   A CG1 
3154 C CG2 . VAL   A 151 ? 0.1879 0.1754 0.2003 -0.0046 0.0276  0.0433  151 VAL   A CG2 
3164 N N   . TYR   A 152 ? 0.1401 0.1578 0.2023 -0.0256 0.0058  0.0458  152 TYR   A N   
3165 C CA  . TYR   A 152 ? 0.1410 0.1664 0.1791 -0.0185 0.0118  0.0432  152 TYR   A CA  
3166 C C   . TYR   A 152 ? 0.1383 0.1582 0.1848 -0.0196 0.0160  0.0387  152 TYR   A C   
3167 O O   . TYR   A 152 ? 0.1488 0.1559 0.1854 -0.0244 0.0148  0.0321  152 TYR   A O   
3168 C CB  . TYR   A 152 ? 0.1620 0.1726 0.1860 -0.0161 0.0196  0.0432  152 TYR   A CB  
3169 C CG  . TYR   A 152 ? 0.1709 0.1957 0.1860 -0.0215 0.0220  0.0434  152 TYR   A CG  
3170 C CD1 . TYR   A 152 ? 0.1898 0.2200 0.2080 -0.0091 0.0364  0.0487  152 TYR   A CD1 
3171 C CD2 . TYR   A 152 ? 0.1758 0.2028 0.1781 -0.0356 0.0172  0.0403  152 TYR   A CD2 
3172 C CE1 . TYR   A 152 ? 0.2202 0.2306 0.2147 -0.0121 0.0206  0.0625  152 TYR   A CE1 
3173 C CE2 . TYR   A 152 ? 0.2101 0.2192 0.1894 -0.0337 0.0188  0.0507  152 TYR   A CE2 
3174 C CZ  . TYR   A 152 ? 0.2374 0.2278 0.1979 -0.0263 0.0137  0.0729  152 TYR   A CZ  
3175 O OH  . TYR   A 152 ? 0.2719 0.2505 0.2270 -0.0171 0.0117  0.0921  152 TYR   A OH  
3185 N N   A LEU   A 153 ? 0.1378 0.1502 0.1925 -0.0152 0.0175  0.0406  153 LEU   A N   
3186 N N   B LEU   A 153 ? 0.1388 0.1599 0.1786 -0.0170 0.0157  0.0404  153 LEU   A N   
3187 C CA  A LEU   A 153 ? 0.1350 0.1429 0.1970 -0.0066 0.0130  0.0399  153 LEU   A CA  
3188 C CA  B LEU   A 153 ? 0.1362 0.1591 0.1692 -0.0073 0.0154  0.0408  153 LEU   A CA  
3189 C C   A LEU   A 153 ? 0.1348 0.1386 0.1960 -0.0074 0.0237  0.0255  153 LEU   A C   
3190 C C   B LEU   A 153 ? 0.1396 0.1625 0.1645 -0.0099 0.0199  0.0392  153 LEU   A C   
3191 O O   A LEU   A 153 ? 0.1356 0.1459 0.2240 -0.0079 0.0311  0.0221  153 LEU   A O   
3192 O O   B LEU   A 153 ? 0.1424 0.1692 0.1885 -0.0174 0.0354  0.0476  153 LEU   A O   
3193 C CB  A LEU   A 153 ? 0.1316 0.1343 0.1925 -0.0109 0.0060  0.0393  153 LEU   A CB  
3194 C CB  B LEU   A 153 ? 0.1339 0.1573 0.1733 0.0029  0.0104  0.0399  153 LEU   A CB  
3195 C CG  A LEU   A 153 ? 0.1348 0.1464 0.1893 -0.0182 0.0141  0.0259  153 LEU   A CG  
3196 C CG  B LEU   A 153 ? 0.1423 0.1634 0.1744 0.0025  0.0043  0.0385  153 LEU   A CG  
3197 C CD1 A LEU   A 153 ? 0.1492 0.1392 0.1942 -0.0219 0.0088  0.0236  153 LEU   A CD1 
3198 C CD1 B LEU   A 153 ? 0.1505 0.1597 0.1755 0.0116  -0.0006 0.0397  153 LEU   A CD1 
3199 C CD2 A LEU   A 153 ? 0.1373 0.1512 0.1599 -0.0153 0.0183  0.0119  153 LEU   A CD2 
3200 C CD2 B LEU   A 153 ? 0.1465 0.1687 0.1777 -0.0035 0.0031  0.0369  153 LEU   A CD2 
3223 N N   A ALA   A 154 ? 0.1364 0.1358 0.1710 -0.0127 0.0228  0.0196  154 ALA   A N   
3224 N N   B ALA   A 154 ? 0.1419 0.1588 0.1298 -0.0085 0.0134  0.0270  154 ALA   A N   
3225 C CA  A ALA   A 154 ? 0.1444 0.1423 0.1551 -0.0123 0.0229  0.0168  154 ALA   A CA  
3226 C CA  B ALA   A 154 ? 0.1517 0.1582 0.1138 -0.0096 0.0019  0.0168  154 ALA   A CA  
3227 C C   A ALA   A 154 ? 0.1375 0.1361 0.1547 -0.0075 0.0234  0.0134  154 ALA   A C   
3228 C C   B ALA   A 154 ? 0.1500 0.1598 0.1026 -0.0130 0.0064  0.0162  154 ALA   A C   
3229 O O   A ALA   A 154 ? 0.1404 0.1445 0.1661 -0.0048 0.0158  0.0086  154 ALA   A O   
3230 O O   B ALA   A 154 ? 0.1576 0.1645 0.0965 -0.0141 0.0147  0.0133  154 ALA   A O   
3231 C CB  A ALA   A 154 ? 0.1513 0.1520 0.1557 -0.0062 0.0186  0.0029  154 ALA   A CB  
3232 C CB  B ALA   A 154 ? 0.1586 0.1611 0.1242 -0.0062 -0.0224 0.0073  154 ALA   A CB  
3243 N N   A VAL   A 155 ? 0.1302 0.1281 0.1359 -0.0084 0.0230  0.0346  155 VAL   A N   
3244 N N   B VAL   A 155 ? 0.1482 0.1548 0.1173 -0.0085 0.0070  0.0200  155 VAL   A N   
3245 C CA  A VAL   A 155 ? 0.1429 0.1441 0.1701 -0.0074 0.0169  0.0419  155 VAL   A CA  
3246 C CA  B VAL   A 155 ? 0.1652 0.1675 0.1489 -0.0066 0.0042  0.0156  155 VAL   A CA  
3247 C CA  T VAL   A 155 ? 0.1578 0.1653 0.1665 -0.0113 0.0146  0.0322  155 VAL   A CA  
3248 C C   A VAL   A 155 ? 0.1489 0.1475 0.2036 0.0036  0.0150  0.0455  155 VAL   A C   
3249 C C   B VAL   A 155 ? 0.1751 0.1780 0.1909 0.0049  -0.0094 0.0290  155 VAL   A C   
3250 C C   T VAL   A 155 ? 0.1542 0.1615 0.1693 -0.0068 0.0159  0.0334  155 VAL   A C   
3251 O O   A VAL   A 155 ? 0.1398 0.1364 0.2113 0.0093  0.0277  0.0223  155 VAL   A O   
3252 O O   B VAL   A 155 ? 0.1663 0.1834 0.1973 0.0083  -0.0156 0.0133  155 VAL   A O   
3253 O O   T VAL   A 155 ? 0.1454 0.1615 0.1642 -0.0085 0.0143  0.0216  155 VAL   A O   
3254 C CB  A VAL   A 155 ? 0.1459 0.1508 0.1622 -0.0017 0.0128  0.0321  155 VAL   A CB  
3255 C CB  B VAL   A 155 ? 0.1729 0.1686 0.1462 0.0033  0.0009  -0.0038 155 VAL   A CB  
3256 C CB  T VAL   A 155 ? 0.1601 0.1664 0.1643 -0.0078 0.0094  0.0259  155 VAL   A CB  
3257 C CG1 A VAL   A 155 ? 0.1508 0.1606 0.1567 0.0045  0.0127  0.0193  155 VAL   A CG1 
3258 C CG1 B VAL   A 155 ? 0.1804 0.1708 0.1469 0.0082  -0.0008 -0.0064 155 VAL   A CG1 
3259 C CG1 T VAL   A 155 ? 0.1644 0.1686 0.1624 -0.0053 0.0063  0.0206  155 VAL   A CG1 
3260 C CG2 A VAL   A 155 ? 0.1600 0.1546 0.1821 0.0051  -0.0037 0.0284  155 VAL   A CG2 
3261 C CG2 B VAL   A 155 ? 0.1836 0.1720 0.1626 0.0064  -0.0068 -0.0159 155 VAL   A CG2 
3262 C CG2 T VAL   A 155 ? 0.1638 0.1686 0.1723 -0.0056 0.0023  0.0251  155 VAL   A CG2 
3288 N N   A PHE   A 156 ? 0.1620 0.1601 0.2417 0.0090  0.0203  0.0629  156 PHE   A N   
3289 N N   B PHE   A 156 ? 0.1957 0.1909 0.2294 0.0057  -0.0115 0.0472  156 PHE   A N   
3290 N N   T PHE   A 156 ? 0.1622 0.1585 0.1814 -0.0008 0.0285  0.0461  156 PHE   A N   
3291 C CA  A PHE   A 156 ? 0.1793 0.1713 0.2724 0.0137  0.0108  0.0702  156 PHE   A CA  
3292 C CA  B PHE   A 156 ? 0.2276 0.2085 0.2793 0.0053  -0.0090 0.0535  156 PHE   A CA  
3293 C CA  T PHE   A 156 ? 0.1730 0.1538 0.1825 0.0039  0.0367  0.0581  156 PHE   A CA  
3294 C C   A PHE   A 156 ? 0.1764 0.1741 0.2741 0.0296  0.0287  0.0761  156 PHE   A C   
3295 C C   B PHE   A 156 ? 0.2410 0.2262 0.2979 0.0072  -0.0109 0.0543  156 PHE   A C   
3296 C C   T PHE   A 156 ? 0.1714 0.1659 0.1908 0.0141  0.0522  0.0586  156 PHE   A C   
3297 O O   A PHE   A 156 ? 0.1805 0.1762 0.2991 0.0158  0.0443  0.0605  156 PHE   A O   
3298 O O   B PHE   A 156 ? 0.2432 0.2254 0.3088 0.0098  -0.0099 0.0412  156 PHE   A O   
3299 O O   T PHE   A 156 ? 0.1786 0.1684 0.1990 0.0129  0.0673  0.0481  156 PHE   A O   
3300 C CB  A PHE   A 156 ? 0.1990 0.1834 0.2913 0.0005  -0.0093 0.0711  156 PHE   A CB  
3301 C CB  B PHE   A 156 ? 0.2400 0.2165 0.3003 -0.0017 -0.0066 0.0594  156 PHE   A CB  
3302 C CB  T PHE   A 156 ? 0.1804 0.1392 0.1679 0.0020  0.0285  0.0639  156 PHE   A CB  
3303 C CG  A PHE   A 156 ? 0.2196 0.1967 0.3038 -0.0038 -0.0331 0.0593  156 PHE   A CG  
3304 C CG  B PHE   A 156 ? 0.2513 0.2224 0.3065 -0.0088 -0.0114 0.0532  156 PHE   A CG  
3305 C CG  T PHE   A 156 ? 0.1904 0.1296 0.1523 0.0067  0.0132  0.0672  156 PHE   A CG  
3306 C CD1 A PHE   A 156 ? 0.2260 0.2044 0.3067 -0.0007 -0.0332 0.0525  156 PHE   A CD1 
3307 C CD1 B PHE   A 156 ? 0.2590 0.2286 0.3154 -0.0113 -0.0197 0.0432  156 PHE   A CD1 
3308 C CD1 T PHE   A 156 ? 0.1963 0.1304 0.1578 0.0137  0.0035  0.0591  156 PHE   A CD1 
3309 C CD2 A PHE   A 156 ? 0.2335 0.2108 0.3158 -0.0030 -0.0427 0.0483  156 PHE   A CD2 
3310 C CD2 B PHE   A 156 ? 0.2528 0.2222 0.3076 -0.0204 -0.0089 0.0536  156 PHE   A CD2 
3311 C CD2 T PHE   A 156 ? 0.1991 0.1291 0.1589 0.0064  0.0073  0.0569  156 PHE   A CD2 
3312 C CE1 A PHE   A 156 ? 0.2350 0.2128 0.3174 -0.0009 -0.0301 0.0415  156 PHE   A CE1 
3313 C CE1 B PHE   A 156 ? 0.2610 0.2304 0.3189 -0.0192 -0.0298 0.0382  156 PHE   A CE1 
3314 C CE1 T PHE   A 156 ? 0.2024 0.1329 0.1625 0.0146  -0.0011 0.0452  156 PHE   A CE1 
3315 C CE2 A PHE   A 156 ? 0.2421 0.2195 0.3208 -0.0034 -0.0423 0.0357  156 PHE   A CE2 
3316 C CE2 B PHE   A 156 ? 0.2534 0.2236 0.3100 -0.0256 -0.0131 0.0482  156 PHE   A CE2 
3317 C CE2 T PHE   A 156 ? 0.2050 0.1310 0.1658 0.0068  -0.0020 0.0466  156 PHE   A CE2 
3318 C CZ  A PHE   A 156 ? 0.2416 0.2213 0.3230 -0.0007 -0.0337 0.0320  156 PHE   A CZ  
3319 C CZ  B PHE   A 156 ? 0.2574 0.2268 0.3116 -0.0282 -0.0271 0.0406  156 PHE   A CZ  
3320 C CZ  T PHE   A 156 ? 0.2056 0.1312 0.1698 0.0076  -0.0026 0.0428  156 PHE   A CZ  
3348 N N   A ASP   A 157 ? 0.1796 0.1870 0.2571 0.0444  0.0275  0.0924  157 ASP   A N   
3349 N N   B ASP   A 157 ? 0.2505 0.2439 0.3002 0.0046  -0.0197 0.0644  157 ASP   A N   
3350 N N   T ASP   A 157 ? 0.1622 0.1795 0.1905 0.0214  0.0464  0.0715  157 ASP   A N   
3351 C CA  A ASP   A 157 ? 0.1934 0.2085 0.2499 0.0551  0.0217  0.0930  157 ASP   A CA  
3352 C CA  B ASP   A 157 ? 0.2707 0.2698 0.3230 0.0013  -0.0195 0.0689  157 ASP   A CA  
3353 C CA  T ASP   A 157 ? 0.1614 0.1955 0.1901 0.0306  0.0362  0.0738  157 ASP   A CA  
3354 C C   A ASP   A 157 ? 0.1743 0.2271 0.2457 0.0572  0.0219  0.0973  157 ASP   A C   
3355 C C   B ASP   A 157 ? 0.2738 0.2818 0.3423 -0.0005 -0.0061 0.0662  157 ASP   A C   
3356 C C   T ASP   A 157 ? 0.1606 0.2140 0.1977 0.0352  0.0331  0.0740  157 ASP   A C   
3357 O O   A ASP   A 157 ? 0.1587 0.2255 0.2385 0.0557  0.0206  0.1077  157 ASP   A O   
3358 O O   B ASP   A 157 ? 0.2852 0.2917 0.3714 0.0036  0.0051  0.0651  157 ASP   A O   
3359 O O   T ASP   A 157 ? 0.1442 0.2143 0.1904 0.0382  0.0370  0.0805  157 ASP   A O   
3360 C CB  A ASP   A 157 ? 0.2202 0.2133 0.2642 0.0663  0.0194  0.0725  157 ASP   A CB  
3361 C CB  B ASP   A 157 ? 0.2857 0.2806 0.3294 -0.0005 -0.0358 0.0712  157 ASP   A CB  
3362 C CB  T ASP   A 157 ? 0.1595 0.1931 0.1849 0.0364  0.0319  0.0670  157 ASP   A CB  
3363 C CG  A ASP   A 157 ? 0.2423 0.2184 0.2868 0.0754  0.0121  0.0605  157 ASP   A CG  
3364 C CG  B ASP   A 157 ? 0.3012 0.2923 0.3400 -0.0009 -0.0499 0.0744  157 ASP   A CG  
3365 C CG  T ASP   A 157 ? 0.1543 0.1864 0.1762 0.0419  0.0278  0.0655  157 ASP   A CG  
3366 O OD1 A ASP   A 157 ? 0.2663 0.2215 0.3100 0.0681  -0.0024 0.0506  157 ASP   A OD1 
3367 O OD1 B ASP   A 157 ? 0.3001 0.2887 0.3338 -0.0019 -0.0561 0.0819  157 ASP   A OD1 
3368 O OD1 T ASP   A 157 ? 0.1503 0.1734 0.1702 0.0459  0.0418  0.0566  157 ASP   A OD1 
3369 O OD2 A ASP   A 157 ? 0.2327 0.2121 0.2912 0.0827  0.0227  0.0696  157 ASP   A OD2 
3370 O OD2 B ASP   A 157 ? 0.3141 0.3028 0.3635 -0.0045 -0.0529 0.0646  157 ASP   A OD2 
3371 O OD2 T ASP   A 157 ? 0.1411 0.1849 0.1582 0.0422  0.0198  0.0782  157 ASP   A OD2 
3384 N N   A LYS   A 158 ? 0.1855 0.2502 0.2592 0.0528  0.0283  0.0664  158 LYS   A N   
3385 N N   B LYS   A 158 ? 0.2664 0.2796 0.3252 -0.0074 -0.0051 0.0582  158 LYS   A N   
3386 N N   T LYS   A 158 ? 0.1830 0.2320 0.2183 0.0348  0.0276  0.0525  158 LYS   A N   
3387 C CA  A LYS   A 158 ? 0.1854 0.2697 0.2744 0.0540  0.0375  0.0385  158 LYS   A CA  
3388 C CA  B LYS   A 158 ? 0.2610 0.2779 0.3072 -0.0096 0.0061  0.0462  158 LYS   A CA  
3389 C CA  T LYS   A 158 ? 0.2008 0.2491 0.2400 0.0351  0.0238  0.0324  158 LYS   A CA  
3390 C C   A LYS   A 158 ? 0.1648 0.2678 0.2517 0.0546  0.0259  0.0361  158 LYS   A C   
3391 C C   B LYS   A 158 ? 0.2352 0.2598 0.2657 -0.0053 -0.0048 0.0194  158 LYS   A C   
3392 C C   T LYS   A 158 ? 0.2017 0.2511 0.2331 0.0361  0.0157  0.0273  158 LYS   A C   
3393 O O   A LYS   A 158 ? 0.1504 0.2771 0.2425 0.0495  0.0409  0.0373  158 LYS   A O   
3394 O O   B LYS   A 158 ? 0.2204 0.2552 0.2429 -0.0126 -0.0049 0.0110  158 LYS   A O   
3395 O O   T LYS   A 158 ? 0.1978 0.2532 0.2289 0.0344  0.0171  0.0262  158 LYS   A O   
3396 C CB  A LYS   A 158 ? 0.2100 0.2829 0.3140 0.0501  0.0572  0.0293  158 LYS   A CB  
3397 C CB  B LYS   A 158 ? 0.2802 0.2957 0.3315 -0.0101 0.0216  0.0662  158 LYS   A CB  
3398 C CB  T LYS   A 158 ? 0.2195 0.2601 0.2714 0.0308  0.0304  0.0237  158 LYS   A CB  
3399 C CG  A LYS   A 158 ? 0.2362 0.2962 0.3583 0.0460  0.0649  0.0319  158 LYS   A CG  
3400 C CG  B LYS   A 158 ? 0.2971 0.3119 0.3581 -0.0095 0.0336  0.0861  158 LYS   A CG  
3401 C CG  T LYS   A 158 ? 0.2370 0.2697 0.3047 0.0275  0.0326  0.0219  158 LYS   A CG  
3402 C CD  A LYS   A 158 ? 0.2561 0.3084 0.3986 0.0422  0.0756  0.0396  158 LYS   A CD  
3403 C CD  B LYS   A 158 ? 0.3079 0.3267 0.3843 -0.0085 0.0488  0.1033  158 LYS   A CD  
3404 C CD  T LYS   A 158 ? 0.2525 0.2788 0.3367 0.0256  0.0347  0.0232  158 LYS   A CD  
3405 C CE  A LYS   A 158 ? 0.2677 0.3154 0.4210 0.0386  0.0860  0.0524  158 LYS   A CE  
3406 C CE  B LYS   A 158 ? 0.3149 0.3355 0.3985 -0.0074 0.0582  0.1226  158 LYS   A CE  
3407 C CE  T LYS   A 158 ? 0.2627 0.2854 0.3587 0.0243  0.0369  0.0273  158 LYS   A CE  
3408 N NZ  A LYS   A 158 ? 0.2731 0.3206 0.4360 0.0350  0.0912  0.0592  158 LYS   A NZ  
3409 N NZ  B LYS   A 158 ? 0.3181 0.3431 0.4131 -0.0075 0.0633  0.1302  158 LYS   A NZ  
3410 N NZ  T LYS   A 158 ? 0.2688 0.2895 0.3715 0.0231  0.0382  0.0303  158 LYS   A NZ  
3450 N N   A ASN   A 159 ? 0.1644 0.2481 0.2545 0.0506  0.0029  0.0334  159 ASN   A N   
3451 N N   B ASN   A 159 ? 0.2311 0.2557 0.2640 0.0071  -0.0131 0.0052  159 ASN   A N   
3452 N N   T ASN   A 159 ? 0.2080 0.2468 0.2381 0.0345  0.0107  0.0250  159 ASN   A N   
3453 C CA  A ASN   A 159 ? 0.1651 0.2350 0.2538 0.0389  -0.0153 0.0315  159 ASN   A CA  
3454 C CA  B ASN   A 159 ? 0.2302 0.2532 0.2761 0.0188  -0.0230 -0.0014 159 ASN   A CA  
3455 C CA  T ASN   A 159 ? 0.2163 0.2452 0.2452 0.0301  0.0051  0.0242  159 ASN   A CA  
3456 C C   A ASN   A 159 ? 0.1507 0.2179 0.2322 0.0264  -0.0041 0.0147  159 ASN   A C   
3457 C C   B ASN   A 159 ? 0.2022 0.2338 0.2488 0.0100  -0.0233 -0.0053 159 ASN   A C   
3458 C C   T ASN   A 159 ? 0.2189 0.2431 0.2374 0.0266  0.0131  0.0170  159 ASN   A C   
3459 O O   A ASN   A 159 ? 0.1332 0.2026 0.2239 0.0218  -0.0140 -0.0083 159 ASN   A O   
3460 O O   B ASN   A 159 ? 0.1916 0.2370 0.2498 0.0143  -0.0335 -0.0047 159 ASN   A O   
3461 O O   T ASN   A 159 ? 0.2210 0.2419 0.2372 0.0247  0.0144  0.0098  159 ASN   A O   
3462 C CB  A ASN   A 159 ? 0.1766 0.2430 0.2919 0.0391  -0.0275 0.0465  159 ASN   A CB  
3463 C CB  B ASN   A 159 ? 0.2558 0.2715 0.3249 0.0290  -0.0250 -0.0070 159 ASN   A CB  
3464 C CB  T ASN   A 159 ? 0.2208 0.2478 0.2692 0.0292  -0.0023 0.0316  159 ASN   A CB  
3465 C CG  A ASN   A 159 ? 0.1965 0.2569 0.3435 0.0364  -0.0249 0.0542  159 ASN   A CG  
3466 C CG  B ASN   A 159 ? 0.2753 0.2897 0.3732 0.0284  -0.0294 -0.0178 159 ASN   A CG  
3467 C CG  T ASN   A 159 ? 0.2278 0.2518 0.2981 0.0264  -0.0042 0.0348  159 ASN   A CG  
3468 O OD1 A ASN   A 159 ? 0.2041 0.2723 0.3685 0.0292  -0.0105 0.0528  159 ASN   A OD1 
3469 O OD1 B ASN   A 159 ? 0.2842 0.2969 0.3946 0.0279  -0.0356 -0.0205 159 ASN   A OD1 
3470 O OD1 T ASN   A 159 ? 0.2297 0.2583 0.3121 0.0232  0.0027  0.0341  159 ASN   A OD1 
3471 N ND2 A ASN   A 159 ? 0.2022 0.2583 0.3588 0.0439  -0.0356 0.0592  159 ASN   A ND2 
3472 N ND2 B ASN   A 159 ? 0.2770 0.2946 0.3853 0.0245  -0.0322 -0.0222 159 ASN   A ND2 
3473 N ND2 T ASN   A 159 ? 0.2298 0.2517 0.3067 0.0294  -0.0103 0.0377  159 ASN   A ND2 
3492 N N   A LEU   A 160 ? 0.1535 0.2079 0.2148 0.0231  -0.0017 0.0220  160 LEU   A N   
3493 N N   B LEU   A 160 ? 0.1862 0.2160 0.2257 -0.0026 -0.0187 0.0014  160 LEU   A N   
3494 N N   T LEU   A 160 ? 0.2177 0.2386 0.2307 0.0252  0.0131  0.0194  160 LEU   A N   
3495 C CA  A LEU   A 160 ? 0.1576 0.2009 0.2016 0.0134  0.0135  0.0333  160 LEU   A CA  
3496 C CA  B LEU   A 160 ? 0.1797 0.2048 0.2176 -0.0127 -0.0020 0.0173  160 LEU   A CA  
3497 C CA  T LEU   A 160 ? 0.2180 0.2345 0.2286 0.0214  0.0184  0.0257  160 LEU   A CA  
3498 C C   A LEU   A 160 ? 0.1353 0.1937 0.1675 0.0084  0.0173  0.0307  160 LEU   A C   
3499 C C   B LEU   A 160 ? 0.1621 0.2020 0.2084 -0.0152 -0.0006 0.0155  160 LEU   A C   
3500 O O   A LEU   A 160 ? 0.1266 0.1893 0.1529 0.0025  0.0083  0.0235  160 LEU   A O   
3501 O O   B LEU   A 160 ? 0.1591 0.1949 0.2180 -0.0200 -0.0032 0.0067  160 LEU   A O   
3502 C CB  A LEU   A 160 ? 0.1728 0.2041 0.2211 0.0091  0.0256  0.0436  160 LEU   A CB  
3503 C CB  B LEU   A 160 ? 0.1952 0.2037 0.2285 -0.0163 0.0138  0.0335  160 LEU   A CB  
3504 C CB  T LEU   A 160 ? 0.2162 0.2329 0.2284 0.0189  0.0230  0.0311  160 LEU   A CB  
3505 C CG  A LEU   A 160 ? 0.1812 0.2070 0.2472 0.0092  0.0274  0.0448  160 LEU   A CG  
3506 C CG  B LEU   A 160 ? 0.2070 0.2088 0.2519 -0.0133 0.0254  0.0479  160 LEU   A CG  
3507 C CG  T LEU   A 160 ? 0.2131 0.2316 0.2329 0.0188  0.0247  0.0340  160 LEU   A CG  
3508 C CD1 A LEU   A 160 ? 0.1803 0.2102 0.2524 0.0120  0.0319  0.0371  160 LEU   A CD1 
3509 C CD1 B LEU   A 160 ? 0.2131 0.2114 0.2625 -0.0100 0.0348  0.0586  160 LEU   A CD1 
3510 C CD1 T LEU   A 160 ? 0.2103 0.2313 0.2341 0.0224  0.0267  0.0316  160 LEU   A CD1 
3511 C CD2 A LEU   A 160 ? 0.1855 0.2092 0.2590 0.0089  0.0311  0.0481  160 LEU   A CD2 
3512 C CD2 B LEU   A 160 ? 0.2130 0.2080 0.2596 -0.0170 0.0266  0.0534  160 LEU   A CD2 
3513 C CD2 T LEU   A 160 ? 0.2134 0.2315 0.2342 0.0170  0.0278  0.0364  160 LEU   A CD2 
3546 N N   A TYR   A 161 ? 0.1382 0.1954 0.1835 0.0043  0.0161  0.0384  161 TYR   A N   
3547 N N   B TYR   A 161 ? 0.1541 0.2044 0.1929 -0.0114 0.0210  0.0241  161 TYR   A N   
3548 C CA  A TYR   A 161 ? 0.1376 0.2045 0.1840 -0.0003 0.0122  0.0307  161 TYR   A CA  
3549 C CA  B TYR   A 161 ? 0.1579 0.2079 0.2031 -0.0128 0.0192  0.0322  161 TYR   A CA  
3550 C C   A TYR   A 161 ? 0.1367 0.2235 0.1921 -0.0049 0.0125  0.0267  161 TYR   A C   
3551 C C   B TYR   A 161 ? 0.1590 0.2165 0.2117 -0.0114 0.0167  0.0230  161 TYR   A C   
3552 O O   A TYR   A 161 ? 0.1365 0.2188 0.2009 -0.0114 0.0096  0.0296  161 TYR   A O   
3553 O O   B TYR   A 161 ? 0.1603 0.2147 0.2080 -0.0127 0.0176  0.0290  161 TYR   A O   
3554 C CB  A TYR   A 161 ? 0.1455 0.2043 0.2074 -0.0010 0.0154  0.0261  161 TYR   A CB  
3555 C CB  B TYR   A 161 ? 0.1628 0.2094 0.2088 -0.0116 0.0158  0.0417  161 TYR   A CB  
3556 C CG  A TYR   A 161 ? 0.1428 0.2014 0.2220 0.0044  0.0086  0.0342  161 TYR   A CG  
3557 C CG  B TYR   A 161 ? 0.1691 0.2181 0.2272 -0.0109 0.0050  0.0435  161 TYR   A CG  
3558 C CD1 A TYR   A 161 ? 0.1415 0.1954 0.2532 0.0030  0.0155  0.0397  161 TYR   A CD1 
3559 C CD1 B TYR   A 161 ? 0.1767 0.2279 0.2365 -0.0084 -0.0022 0.0338  161 TYR   A CD1 
3560 C CD2 A TYR   A 161 ? 0.1491 0.2037 0.2297 0.0095  0.0013  0.0271  161 TYR   A CD2 
3561 C CD2 B TYR   A 161 ? 0.1726 0.2194 0.2460 -0.0071 0.0010  0.0482  161 TYR   A CD2 
3562 C CE1 A TYR   A 161 ? 0.1460 0.1823 0.2533 0.0016  0.0068  0.0451  161 TYR   A CE1 
3563 C CE1 B TYR   A 161 ? 0.1819 0.2312 0.2393 -0.0075 -0.0068 0.0408  161 TYR   A CE1 
3564 C CE2 A TYR   A 161 ? 0.1543 0.1998 0.2373 -0.0004 0.0029  0.0446  161 TYR   A CE2 
3565 C CE2 B TYR   A 161 ? 0.1768 0.2253 0.2472 -0.0047 -0.0054 0.0496  161 TYR   A CE2 
3566 C CZ  A TYR   A 161 ? 0.1629 0.1883 0.2506 -0.0067 -0.0008 0.0583  161 TYR   A CZ  
3567 C CZ  B TYR   A 161 ? 0.1886 0.2305 0.2512 -0.0067 -0.0065 0.0522  161 TYR   A CZ  
3568 O OH  A TYR   A 161 ? 0.1809 0.1778 0.2611 -0.0152 -0.0030 0.0671  161 TYR   A OH  
3569 O OH  B TYR   A 161 ? 0.2030 0.2349 0.2684 -0.0075 -0.0025 0.0538  161 TYR   A OH  
3588 N N   A ASP   A 162 ? 0.1393 0.2532 0.1870 -0.0013 0.0190  0.0279  162 ASP   A N   
3589 N N   B ASP   A 162 ? 0.1616 0.2263 0.2241 -0.0115 0.0155  0.0156  162 ASP   A N   
3590 C CA  A ASP   A 162 ? 0.1418 0.2867 0.1852 -0.0001 0.0201  0.0225  162 ASP   A CA  
3591 C CA  B ASP   A 162 ? 0.1720 0.2443 0.2420 -0.0149 0.0118  0.0047  162 ASP   A CA  
3592 C C   A ASP   A 162 ? 0.1397 0.2902 0.1805 -0.0003 0.0242  0.0197  162 ASP   A C   
3593 C C   B ASP   A 162 ? 0.1711 0.2513 0.2387 -0.0158 0.0097  -0.0028 162 ASP   A C   
3594 O O   A ASP   A 162 ? 0.1411 0.2915 0.1762 0.0078  0.0252  0.0030  162 ASP   A O   
3595 O O   B ASP   A 162 ? 0.1706 0.2477 0.2429 -0.0185 0.0102  -0.0067 162 ASP   A O   
3596 C CB  A ASP   A 162 ? 0.1519 0.3179 0.2046 0.0103  0.0227  0.0183  162 ASP   A CB  
3597 C CB  B ASP   A 162 ? 0.1903 0.2631 0.2783 -0.0088 0.0084  -0.0025 162 ASP   A CB  
3598 C CG  A ASP   A 162 ? 0.1605 0.3444 0.2169 0.0124  0.0382  0.0246  162 ASP   A CG  
3599 C CG  B ASP   A 162 ? 0.2102 0.2801 0.3177 0.0010  0.0029  -0.0076 162 ASP   A CG  
3600 O OD1 A ASP   A 162 ? 0.1742 0.3562 0.2115 0.0005  0.0384  0.0299  162 ASP   A OD1 
3601 O OD1 B ASP   A 162 ? 0.2166 0.2829 0.3231 0.0006  -0.0008 -0.0119 162 ASP   A OD1 
3602 O OD2 A ASP   A 162 ? 0.1639 0.3564 0.2479 0.0243  0.0535  0.0267  162 ASP   A OD2 
3603 O OD2 B ASP   A 162 ? 0.2243 0.2879 0.3387 0.0057  0.0035  -0.0084 162 ASP   A OD2 
3612 N N   A LYS   A 163 ? 0.1505 0.2972 0.1778 0.0011  0.0183  0.0160  163 LYS   A N   
3613 N N   B LYS   A 163 ? 0.1760 0.2627 0.2373 -0.0182 0.0077  -0.0096 163 LYS   A N   
3614 C CA  A LYS   A 163 ? 0.1650 0.3082 0.1925 0.0026  0.0124  0.0133  163 LYS   A CA  
3615 C CA  B LYS   A 163 ? 0.1886 0.2763 0.2519 -0.0133 0.0089  -0.0157 163 LYS   A CA  
3616 C C   A LYS   A 163 ? 0.1575 0.2924 0.1831 -0.0025 0.0198  0.0054  163 LYS   A C   
3617 C C   B LYS   A 163 ? 0.1767 0.2611 0.2189 -0.0173 0.0113  -0.0258 163 LYS   A C   
3618 O O   A LYS   A 163 ? 0.1533 0.2933 0.1847 -0.0061 0.0232  -0.0196 163 LYS   A O   
3619 O O   B LYS   A 163 ? 0.1747 0.2709 0.2078 -0.0117 0.0160  -0.0343 163 LYS   A O   
3620 C CB  A LYS   A 163 ? 0.1996 0.3332 0.2385 0.0166  0.0048  0.0196  163 LYS   A CB  
3621 C CB  B LYS   A 163 ? 0.2199 0.3050 0.3058 -0.0068 0.0083  -0.0021 163 LYS   A CB  
3622 C CG  A LYS   A 163 ? 0.2333 0.3572 0.3065 0.0212  0.0099  0.0223  163 LYS   A CG  
3623 C CG  B LYS   A 163 ? 0.2528 0.3292 0.3635 -0.0046 0.0095  0.0086  163 LYS   A CG  
3624 C CD  A LYS   A 163 ? 0.2670 0.3766 0.3759 0.0232  0.0095  0.0230  163 LYS   A CD  
3625 C CD  B LYS   A 163 ? 0.2793 0.3481 0.4195 -0.0064 0.0095  0.0164  163 LYS   A CD  
3626 C CE  A LYS   A 163 ? 0.2950 0.3905 0.4303 0.0235  0.0139  0.0260  163 LYS   A CE  
3627 C CE  B LYS   A 163 ? 0.2989 0.3613 0.4600 -0.0060 0.0119  0.0235  163 LYS   A CE  
3628 N NZ  A LYS   A 163 ? 0.3106 0.3997 0.4645 0.0215  0.0158  0.0285  163 LYS   A NZ  
3629 N NZ  B LYS   A 163 ? 0.3111 0.3694 0.4880 -0.0057 0.0108  0.0261  163 LYS   A NZ  
3656 N N   A LEU   A 164 ? 0.1393 0.2653 0.1674 -0.0082 0.0181  0.0151  164 LEU   A N   
3657 N N   B LEU   A 164 ? 0.1683 0.2424 0.2074 -0.0258 0.0058  -0.0199 164 LEU   A N   
3658 C CA  A LEU   A 164 ? 0.1427 0.2458 0.1648 -0.0158 0.0232  0.0159  164 LEU   A CA  
3659 C CA  B LEU   A 164 ? 0.1766 0.2288 0.2133 -0.0232 0.0147  -0.0121 164 LEU   A CA  
3660 C C   A LEU   A 164 ? 0.1532 0.2458 0.1646 -0.0233 0.0201  0.0138  164 LEU   A C   
3661 C C   B LEU   A 164 ? 0.1961 0.2346 0.2285 -0.0226 0.0116  -0.0127 164 LEU   A C   
3662 O O   A LEU   A 164 ? 0.1513 0.2459 0.1521 -0.0364 0.0290  0.0204  164 LEU   A O   
3663 O O   B LEU   A 164 ? 0.2040 0.2375 0.2414 -0.0231 0.0158  -0.0241 164 LEU   A O   
3664 C CB  A LEU   A 164 ? 0.1422 0.2234 0.1685 -0.0147 0.0270  0.0207  164 LEU   A CB  
3665 C CB  B LEU   A 164 ? 0.1764 0.2159 0.2085 -0.0202 0.0191  0.0004  164 LEU   A CB  
3666 C CG  A LEU   A 164 ? 0.1485 0.2099 0.1914 -0.0080 0.0242  0.0211  164 LEU   A CG  
3667 C CG  B LEU   A 164 ? 0.1773 0.2120 0.2178 -0.0108 0.0214  -0.0033 164 LEU   A CG  
3668 C CD1 A LEU   A 164 ? 0.1411 0.2011 0.2038 -0.0048 0.0156  0.0313  164 LEU   A CD1 
3669 C CD1 B LEU   A 164 ? 0.1699 0.2102 0.2191 -0.0135 0.0145  -0.0059 164 LEU   A CD1 
3670 C CD2 A LEU   A 164 ? 0.1561 0.2024 0.2003 -0.0054 0.0456  0.0139  164 LEU   A CD2 
3671 C CD2 B LEU   A 164 ? 0.1838 0.2158 0.2252 0.0010  0.0248  -0.0106 164 LEU   A CD2 
3694 N N   A VAL   A 165 ? 0.1390 0.2423 0.1532 -0.0234 0.0200  0.0219  165 VAL   A N   
3695 N N   B VAL   A 165 ? 0.2121 0.2403 0.2299 -0.0203 0.0059  -0.0009 165 VAL   A N   
3696 C CA  A VAL   A 165 ? 0.1491 0.2477 0.1462 -0.0365 0.0184  0.0361  165 VAL   A CA  
3697 C CA  B VAL   A 165 ? 0.2273 0.2512 0.2398 -0.0201 -0.0015 0.0096  165 VAL   A CA  
3698 C C   A VAL   A 165 ? 0.1381 0.2674 0.1453 -0.0321 0.0194  0.0367  165 VAL   A C   
3699 C C   B VAL   A 165 ? 0.2362 0.2669 0.2594 -0.0215 -0.0192 -0.0027 165 VAL   A C   
3700 O O   A VAL   A 165 ? 0.1325 0.2708 0.1503 -0.0375 0.0089  0.0330  165 VAL   A O   
3701 O O   B VAL   A 165 ? 0.2340 0.2643 0.2566 -0.0252 -0.0142 -0.0037 165 VAL   A O   
3702 C CB  A VAL   A 165 ? 0.1674 0.2401 0.1425 -0.0404 0.0258  0.0288  165 VAL   A CB  
3703 C CB  B VAL   A 165 ? 0.2389 0.2546 0.2510 -0.0140 -0.0005 0.0265  165 VAL   A CB  
3704 C CG1 A VAL   A 165 ? 0.1728 0.2420 0.1593 -0.0353 0.0322  0.0220  165 VAL   A CG1 
3705 C CG1 B VAL   A 165 ? 0.2437 0.2551 0.2580 -0.0167 0.0006  0.0263  165 VAL   A CG1 
3706 C CG2 A VAL   A 165 ? 0.1805 0.2417 0.1463 -0.0349 0.0251  0.0314  165 VAL   A CG2 
3707 C CG2 B VAL   A 165 ? 0.2448 0.2551 0.2416 -0.0080 0.0000  0.0320  165 VAL   A CG2 
3726 N N   A SER   A 166 ? 0.1258 0.2830 0.1580 -0.0253 0.0227  0.0368  166 SER   A N   
3727 N N   B SER   A 166 ? 0.2502 0.2864 0.2923 -0.0171 -0.0360 -0.0116 166 SER   A N   
3728 C CA  A SER   A 166 ? 0.1312 0.2999 0.1791 -0.0262 0.0232  0.0413  166 SER   A CA  
3729 C CA  B SER   A 166 ? 0.2670 0.3073 0.3313 -0.0134 -0.0469 -0.0278 166 SER   A CA  
3730 C C   A SER   A 166 ? 0.1368 0.3225 0.1956 -0.0184 0.0057  0.0327  166 SER   A C   
3731 C C   B SER   A 166 ? 0.2920 0.3235 0.3560 -0.0136 -0.0447 -0.0394 166 SER   A C   
3732 O O   A SER   A 166 ? 0.1603 0.3388 0.2335 -0.0260 0.0142  0.0138  166 SER   A O   
3733 O O   B SER   A 166 ? 0.2963 0.3300 0.3758 -0.0144 -0.0462 -0.0438 166 SER   A O   
3734 C CB  A SER   A 166 ? 0.1507 0.2960 0.2097 -0.0258 0.0166  0.0454  166 SER   A CB  
3735 C CB  B SER   A 166 ? 0.2605 0.3163 0.3434 -0.0090 -0.0569 -0.0273 166 SER   A CB  
3736 O OG  A SER   A 166 ? 0.1796 0.3029 0.2505 -0.0183 0.0167  0.0543  166 SER   A OG  
3737 O OG  B SER   A 166 ? 0.2585 0.3210 0.3585 -0.0032 -0.0570 -0.0212 166 SER   A OG  
3748 N N   A SER   A 167 ? 0.1346 0.3257 0.1580 -0.0047 -0.0046 0.0407  167 SER   A N   
3749 N N   B SER   A 167 ? 0.3070 0.3322 0.3598 -0.0133 -0.0391 -0.0418 167 SER   A N   
3750 C CA  A SER   A 167 ? 0.1604 0.3306 0.1606 0.0037  -0.0129 0.0340  167 SER   A CA  
3751 C CA  B SER   A 167 ? 0.3217 0.3393 0.3608 -0.0140 -0.0293 -0.0404 167 SER   A CA  
3752 C C   A SER   A 167 ? 0.1635 0.3313 0.1568 0.0100  0.0116  0.0303  167 SER   A C   
3753 C C   B SER   A 167 ? 0.3315 0.3437 0.3827 -0.0125 -0.0253 -0.0406 167 SER   A C   
3754 O O   A SER   A 167 ? 0.1820 0.3333 0.1642 0.0113  0.0015  0.0377  167 SER   A O   
3755 O O   B SER   A 167 ? 0.3357 0.3448 0.3984 -0.0132 -0.0266 -0.0451 167 SER   A O   
3756 C CB  A SER   A 167 ? 0.1750 0.3353 0.1649 0.0059  0.0013  0.0441  167 SER   A CB  
3757 C CB  B SER   A 167 ? 0.3252 0.3423 0.3409 -0.0146 -0.0216 -0.0346 167 SER   A CB  
3758 O OG  A SER   A 167 ? 0.1859 0.3410 0.1835 0.0054  0.0032  0.0524  167 SER   A OG  
3759 O OG  B SER   A 167 ? 0.3256 0.3450 0.3268 -0.0158 -0.0178 -0.0296 167 SER   A OG  
3770 N N   A PHE   A 168 ? 0.1562 0.3285 0.1515 0.0171  0.0144  0.0190  168 PHE   A N   
3771 N N   B PHE   A 168 ? 0.3340 0.3469 0.3842 -0.0098 -0.0197 -0.0349 168 PHE   A N   
3772 C CA  A PHE   A 168 ? 0.1562 0.3271 0.1581 0.0137  0.0204  0.0180  168 PHE   A CA  
3773 C CA  B PHE   A 168 ? 0.3334 0.3483 0.3794 -0.0091 -0.0121 -0.0331 168 PHE   A CA  
3774 C C   A PHE   A 168 ? 0.1646 0.3398 0.1765 0.0042  0.0410  0.0115  168 PHE   A C   
3775 C C   B PHE   A 168 ? 0.3490 0.3639 0.4130 -0.0035 -0.0088 -0.0380 168 PHE   A C   
3776 O O   A PHE   A 168 ? 0.1737 0.3490 0.2288 -0.0088 0.0512  0.0224  168 PHE   A O   
3777 O O   B PHE   A 168 ? 0.3523 0.3666 0.4255 -0.0019 -0.0006 -0.0371 168 PHE   A O   
3778 C CB  A PHE   A 168 ? 0.1542 0.3136 0.1502 0.0086  0.0085  0.0149  168 PHE   A CB  
3779 C CB  B PHE   A 168 ? 0.3185 0.3350 0.3394 -0.0161 -0.0078 -0.0262 168 PHE   A CB  
3780 C CG  A PHE   A 168 ? 0.1481 0.3038 0.1341 -0.0018 0.0064  0.0206  168 PHE   A CG  
3781 C CG  B PHE   A 168 ? 0.3064 0.3236 0.3031 -0.0234 -0.0055 -0.0206 168 PHE   A CG  
3782 C CD1 A PHE   A 168 ? 0.1514 0.3025 0.1337 -0.0061 -0.0006 0.0303  168 PHE   A CD1 
3783 C CD1 B PHE   A 168 ? 0.3011 0.3201 0.2868 -0.0277 -0.0076 -0.0180 168 PHE   A CD1 
3784 C CD2 A PHE   A 168 ? 0.1435 0.3008 0.1268 -0.0073 0.0136  0.0216  168 PHE   A CD2 
3785 C CD2 B PHE   A 168 ? 0.3001 0.3180 0.2837 -0.0261 -0.0027 -0.0197 168 PHE   A CD2 
3786 C CE1 A PHE   A 168 ? 0.1471 0.2986 0.1289 -0.0093 0.0022  0.0350  168 PHE   A CE1 
3787 C CE1 B PHE   A 168 ? 0.2968 0.3168 0.2763 -0.0309 -0.0107 -0.0161 168 PHE   A CE1 
3788 C CE2 A PHE   A 168 ? 0.1524 0.2939 0.1298 -0.0089 0.0101  0.0357  168 PHE   A CE2 
3789 C CE2 B PHE   A 168 ? 0.2967 0.3146 0.2761 -0.0304 -0.0040 -0.0165 168 PHE   A CE2 
3790 C CZ  A PHE   A 168 ? 0.1512 0.2955 0.1383 -0.0131 0.0070  0.0378  168 PHE   A CZ  
3791 C CZ  B PHE   A 168 ? 0.2950 0.3156 0.2722 -0.0317 -0.0082 -0.0162 168 PHE   A CZ  
3810 N N   A LEU   A 169 ? 0.1946 0.3408 0.1974 -0.0074 0.0413  0.0044  169 LEU   A N   
3811 N N   B LEU   A 169 ? 0.3609 0.3754 0.4287 0.0027  -0.0125 -0.0425 169 LEU   A N   
3812 C CA  A LEU   A 169 ? 0.2353 0.3476 0.2603 -0.0061 0.0202  0.0124  169 LEU   A CA  
3813 C CA  B LEU   A 169 ? 0.3715 0.3866 0.4352 0.0086  -0.0131 -0.0429 169 LEU   A CA  
3814 C C   A LEU   A 169 ? 0.2295 0.3413 0.2698 -0.0080 0.0310  0.0341  169 LEU   A C   
3815 C C   B LEU   A 169 ? 0.3738 0.3915 0.4493 0.0108  -0.0148 -0.0500 169 LEU   A C   
3816 O O   A LEU   A 169 ? 0.2318 0.3369 0.2808 -0.0074 0.0313  0.0384  169 LEU   A O   
3817 O O   B LEU   A 169 ? 0.3763 0.3938 0.4541 0.0142  -0.0142 -0.0526 169 LEU   A O   
3818 C CB  A LEU   A 169 ? 0.2654 0.3582 0.3012 -0.0102 -0.0045 0.0015  169 LEU   A CB  
3819 C CB  B LEU   A 169 ? 0.3799 0.3944 0.4318 0.0114  -0.0141 -0.0353 169 LEU   A CB  
3820 C CG  A LEU   A 169 ? 0.2926 0.3676 0.3401 -0.0155 -0.0284 -0.0136 169 LEU   A CG  
3821 C CG  B LEU   A 169 ? 0.3868 0.3999 0.4264 0.0147  -0.0153 -0.0282 169 LEU   A CG  
3822 C CD1 A LEU   A 169 ? 0.3012 0.3690 0.3548 -0.0178 -0.0386 -0.0186 169 LEU   A CD1 
3823 C CD1 B LEU   A 169 ? 0.3884 0.4017 0.4231 0.0160  -0.0147 -0.0263 169 LEU   A CD1 
3824 C CD2 A LEU   A 169 ? 0.3012 0.3727 0.3479 -0.0180 -0.0346 -0.0174 169 LEU   A CD2 
3825 C CD2 B LEU   A 169 ? 0.3892 0.4021 0.4227 0.0156  -0.0166 -0.0251 169 LEU   A CD2 
3826 O OXT A LEU   A 169 ? 0.2211 0.3426 0.2632 -0.0131 0.0435  0.0469  169 LEU   A OXT 
3827 O OXT B LEU   A 169 ? 0.3720 0.3940 0.4563 0.0105  -0.0140 -0.0510 169 LEU   A OXT 
3850 N N   A SER   B 1   ? 0.3793 0.3539 0.3800 -0.1071 -0.0750 0.0376  1   SER   B N   
3851 N N   B SER   B 1   ? 0.3498 0.3314 0.3611 -0.0848 -0.0568 0.0134  1   SER   B N   
3852 C CA  A SER   B 1   ? 0.3733 0.3554 0.3901 -0.1121 -0.0730 0.0392  1   SER   B CA  
3853 C CA  B SER   B 1   ? 0.3438 0.3347 0.3625 -0.0873 -0.0558 0.0123  1   SER   B CA  
3854 C C   A SER   B 1   ? 0.3506 0.3527 0.3750 -0.1141 -0.0755 0.0594  1   SER   B C   
3855 C C   B SER   B 1   ? 0.3261 0.3386 0.3438 -0.0841 -0.0597 0.0297  1   SER   B C   
3856 O O   A SER   B 1   ? 0.3619 0.3560 0.3622 -0.1059 -0.0726 0.0595  1   SER   B O   
3857 O O   B SER   B 1   ? 0.3276 0.3382 0.3265 -0.0833 -0.0606 0.0294  1   SER   B O   
3858 C CB  A SER   B 1   ? 0.3846 0.3556 0.4031 -0.1131 -0.0672 0.0250  1   SER   B CB  
3859 C CB  B SER   B 1   ? 0.3516 0.3310 0.3741 -0.0902 -0.0503 -0.0051 1   SER   B CB  
3860 O OG  A SER   B 1   ? 0.3957 0.3634 0.4390 -0.1120 -0.0611 0.0218  1   SER   B OG  
3861 O OG  B SER   B 1   ? 0.3593 0.3341 0.4013 -0.0915 -0.0473 -0.0126 1   SER   B OG  
3876 N N   A MET   B 2   ? 0.3222 0.3441 0.3713 -0.1189 -0.0717 0.0938  2   MET   B N   
3877 N N   B MET   B 2   ? 0.3119 0.3417 0.3415 -0.0770 -0.0575 0.0563  2   MET   B N   
3878 C CA  A MET   B 2   ? 0.3021 0.3439 0.3792 -0.1039 -0.0726 0.1099  2   MET   B CA  
3879 C CA  B MET   B 2   ? 0.3011 0.3452 0.3417 -0.0609 -0.0559 0.0747  2   MET   B CA  
3880 C C   A MET   B 2   ? 0.2594 0.3180 0.3311 -0.0938 -0.0874 0.1367  2   MET   B C   
3881 C C   B MET   B 2   ? 0.2783 0.3299 0.3089 -0.0545 -0.0552 0.0891  2   MET   B C   
3882 O O   A MET   B 2   ? 0.2462 0.3250 0.3243 -0.0897 -0.1027 0.1416  2   MET   B O   
3883 O O   B MET   B 2   ? 0.2789 0.3380 0.3154 -0.0522 -0.0530 0.0892  2   MET   B O   
3884 C CB  A MET   B 2   ? 0.3330 0.3767 0.4580 -0.0842 -0.0529 0.0823  2   MET   B CB  
3885 C CB  B MET   B 2   ? 0.3177 0.3658 0.3868 -0.0456 -0.0516 0.0725  2   MET   B CB  
3886 C CG  A MET   B 2   ? 0.3611 0.4055 0.5277 -0.0638 -0.0344 0.0641  2   MET   B CG  
3887 C CG  B MET   B 2   ? 0.3312 0.3841 0.4219 -0.0319 -0.0479 0.0785  2   MET   B CG  
3888 S SD  A MET   B 2   ? 0.3860 0.4313 0.5959 -0.0455 -0.0223 0.0512  2   MET   B SD  
3889 S SD  B MET   B 2   ? 0.3433 0.4025 0.4543 -0.0202 -0.0492 0.0836  2   MET   B SD  
3890 C CE  A MET   B 2   ? 0.3906 0.4376 0.5996 -0.0433 -0.0155 0.0510  2   MET   B CE  
3891 C CE  B MET   B 2   ? 0.3444 0.4068 0.4613 -0.0196 -0.0464 0.0766  2   MET   B CE  
3910 N N   A VAL   B 3   ? 0.2302 0.2803 0.2939 -0.0947 -0.0864 0.1455  3   VAL   B N   
3911 N N   B VAL   B 3   ? 0.2545 0.3029 0.2770 -0.0540 -0.0576 0.0962  3   VAL   B N   
3912 C CA  A VAL   B 3   ? 0.2247 0.2516 0.2849 -0.0784 -0.0838 0.1222  3   VAL   B CA  
3913 C CA  B VAL   B 3   ? 0.2387 0.2769 0.2626 -0.0463 -0.0573 0.0838  3   VAL   B CA  
3914 C C   A VAL   B 3   ? 0.2069 0.2401 0.2529 -0.0666 -0.0732 0.1027  3   VAL   B C   
3915 C C   B VAL   B 3   ? 0.2159 0.2581 0.2355 -0.0447 -0.0572 0.0838  3   VAL   B C   
3916 O O   A VAL   B 3   ? 0.2044 0.2366 0.2630 -0.0682 -0.0681 0.1072  3   VAL   B O   
3917 O O   B VAL   B 3   ? 0.2122 0.2621 0.2321 -0.0326 -0.0601 0.0840  3   VAL   B O   
3918 C CB  A VAL   B 3   ? 0.2420 0.2464 0.3294 -0.0804 -0.0724 0.1028  3   VAL   B CB  
3919 C CB  B VAL   B 3   ? 0.2480 0.2706 0.2847 -0.0452 -0.0484 0.0718  3   VAL   B CB  
3920 C CG1 A VAL   B 3   ? 0.2508 0.2424 0.3426 -0.0823 -0.0723 0.1019  3   VAL   B CG1 
3921 C CG1 B VAL   B 3   ? 0.2527 0.2654 0.2924 -0.0476 -0.0478 0.0685  3   VAL   B CG1 
3922 C CG2 A VAL   B 3   ? 0.2436 0.2498 0.3404 -0.0785 -0.0595 0.1064  3   VAL   B CG2 
3923 C CG2 B VAL   B 3   ? 0.2495 0.2711 0.2877 -0.0421 -0.0437 0.0740  3   VAL   B CG2 
3942 N N   . ASN   B 4   ? 0.1984 0.2303 0.2286 -0.0576 -0.0599 0.0810  4   ASN   B N   
3943 C CA  . ASN   B 4   ? 0.2002 0.2254 0.2032 -0.0569 -0.0491 0.0492  4   ASN   B CA  
3944 C C   . ASN   B 4   ? 0.2101 0.2396 0.2025 -0.0604 -0.0342 0.0317  4   ASN   B C   
3945 O O   . ASN   B 4   ? 0.2102 0.2434 0.2157 -0.0588 -0.0319 0.0142  4   ASN   B O   
3946 C CB  . ASN   B 4   ? 0.1997 0.2179 0.1850 -0.0490 -0.0551 0.0526  4   ASN   B CB  
3947 C CG  . ASN   B 4   ? 0.2001 0.2033 0.1760 -0.0501 -0.0526 0.0353  4   ASN   B CG  
3948 O OD1 . ASN   B 4   ? 0.2016 0.1772 0.1790 -0.0483 -0.0509 0.0268  4   ASN   B OD1 
3949 N ND2 . ASN   B 4   ? 0.2152 0.2098 0.1892 -0.0310 -0.0415 0.0247  4   ASN   B ND2 
3957 N N   . SER   B 5   ? 0.2234 0.2566 0.2146 -0.0618 -0.0222 0.0325  5   SER   B N   
3958 C CA  . SER   B 5   ? 0.2501 0.2925 0.2562 -0.0532 0.0022  0.0305  5   SER   B CA  
3959 C C   . SER   B 5   ? 0.2733 0.2982 0.2794 -0.0684 0.0310  0.0318  5   SER   B C   
3960 O O   . SER   B 5   ? 0.2907 0.2951 0.3248 -0.0651 0.0612  0.0323  5   SER   B O   
3961 C CB  . SER   B 5   ? 0.2610 0.3150 0.3007 -0.0413 0.0132  0.0371  5   SER   B CB  
3962 O OG  . SER   B 5   ? 0.2844 0.3368 0.3576 -0.0275 0.0197  0.0416  5   SER   B OG  
3968 N N   . PHE   B 6   ? 0.2903 0.3133 0.2629 -0.0735 0.0431  0.0417  6   PHE   B N   
3969 C CA  . PHE   B 6   ? 0.2996 0.3153 0.2332 -0.0881 0.0459  0.0262  6   PHE   B CA  
3970 C C   . PHE   B 6   ? 0.3571 0.3511 0.2775 -0.0918 0.0691  -0.0059 6   PHE   B C   
3971 O O   . PHE   B 6   ? 0.3662 0.3845 0.3107 -0.0890 0.0494  -0.0217 6   PHE   B O   
3972 C CB  . PHE   B 6   ? 0.2646 0.2892 0.2026 -0.0832 0.0202  0.0205  6   PHE   B CB  
3973 C CG  . PHE   B 6   ? 0.2293 0.2567 0.1884 -0.0801 -0.0008 0.0173  6   PHE   B CG  
3974 C CD1 . PHE   B 6   ? 0.2303 0.2323 0.1744 -0.0715 -0.0135 0.0137  6   PHE   B CD1 
3975 C CD2 . PHE   B 6   ? 0.2042 0.2562 0.1886 -0.0675 -0.0094 0.0367  6   PHE   B CD2 
3976 C CE1 . PHE   B 6   ? 0.2266 0.2125 0.1864 -0.0614 -0.0180 0.0102  6   PHE   B CE1 
3977 C CE2 . PHE   B 6   ? 0.2097 0.2398 0.2135 -0.0546 -0.0034 0.0356  6   PHE   B CE2 
3978 C CZ  . PHE   B 6   ? 0.2180 0.2196 0.2033 -0.0545 -0.0122 0.0166  6   PHE   B CZ  
3988 N N   A SER   B 7   ? 0.3832 0.3401 0.2898 -0.1039 0.0922  -0.0238 7   SER   B N   
3989 N N   B SER   B 7   ? 0.3778 0.3464 0.2987 -0.0961 0.0814  -0.0149 7   SER   B N   
3990 C CA  A SER   B 7   ? 0.4061 0.3409 0.3229 -0.1046 0.1106  -0.0354 7   SER   B CA  
3991 C CA  B SER   B 7   ? 0.3957 0.3478 0.3312 -0.0933 0.0890  -0.0214 7   SER   B CA  
3992 C C   A SER   B 7   ? 0.4051 0.3258 0.2986 -0.1126 0.1193  -0.0444 7   SER   B C   
3993 C C   B SER   B 7   ? 0.3969 0.3350 0.3156 -0.0982 0.0915  -0.0292 7   SER   B C   
3994 O O   A SER   B 7   ? 0.4074 0.3225 0.3114 -0.1178 0.1162  -0.0437 7   SER   B O   
3995 O O   B SER   B 7   ? 0.3987 0.3344 0.3225 -0.1005 0.0895  -0.0274 7   SER   B O   
3996 C CB  A SER   B 7   ? 0.4216 0.3526 0.3774 -0.0993 0.1209  -0.0313 7   SER   B CB  
3997 C CB  B SER   B 7   ? 0.4067 0.3584 0.3734 -0.0869 0.0943  -0.0173 7   SER   B CB  
3998 O OG  A SER   B 7   ? 0.4317 0.3639 0.4204 -0.0965 0.1230  -0.0219 7   SER   B OG  
3999 O OG  B SER   B 7   ? 0.4139 0.3678 0.4065 -0.0826 0.0948  -0.0108 7   SER   B OG  
4010 N N   A GLY   B 8   ? 0.4049 0.3164 0.2909 -0.1057 0.1233  -0.0541 8   GLY   B N   
4011 N N   B GLY   B 8   ? 0.3972 0.3233 0.3085 -0.0954 0.0939  -0.0391 8   GLY   B N   
4012 C CA  A GLY   B 8   ? 0.3972 0.3025 0.2866 -0.1004 0.1219  -0.0630 8   GLY   B CA  
4013 C CA  B GLY   B 8   ? 0.3919 0.3080 0.2997 -0.0935 0.0949  -0.0502 8   GLY   B CA  
4014 C C   A GLY   B 8   ? 0.3842 0.2824 0.2830 -0.0963 0.1187  -0.0618 8   GLY   B C   
4015 C C   B GLY   B 8   ? 0.3824 0.2878 0.2890 -0.0921 0.0968  -0.0560 8   GLY   B C   
4016 O O   A GLY   B 8   ? 0.3900 0.2834 0.3053 -0.0928 0.1212  -0.0698 8   GLY   B O   
4017 O O   B GLY   B 8   ? 0.3878 0.2934 0.3049 -0.0866 0.0947  -0.0597 8   GLY   B O   
4024 N N   . TYR   B 9   ? 0.3714 0.2650 0.2692 -0.0899 0.0946  -0.0661 9   TYR   B N   
4025 C CA  . TYR   B 9   ? 0.3487 0.2288 0.2283 -0.0753 0.0737  -0.0516 9   TYR   B CA  
4026 C C   . TYR   B 9   ? 0.3448 0.2260 0.2122 -0.0701 0.0446  -0.0377 9   TYR   B C   
4027 O O   . TYR   B 9   ? 0.3607 0.2466 0.2458 -0.0730 0.0439  -0.0232 9   TYR   B O   
4028 C CB  . TYR   B 9   ? 0.3393 0.2034 0.2468 -0.0644 0.0705  -0.0447 9   TYR   B CB  
4029 C CG  . TYR   B 9   ? 0.3259 0.1817 0.2461 -0.0721 0.0651  -0.0500 9   TYR   B CG  
4030 C CD1 . TYR   B 9   ? 0.3282 0.1835 0.2638 -0.0872 0.0688  -0.0440 9   TYR   B CD1 
4031 C CD2 . TYR   B 9   ? 0.3089 0.1777 0.2338 -0.0681 0.0631  -0.0516 9   TYR   B CD2 
4032 C CE1 . TYR   B 9   ? 0.3220 0.1946 0.2599 -0.0939 0.0748  -0.0561 9   TYR   B CE1 
4033 C CE2 . TYR   B 9   ? 0.3107 0.1825 0.2490 -0.0703 0.0601  -0.0505 9   TYR   B CE2 
4034 C CZ  . TYR   B 9   ? 0.3141 0.2019 0.2645 -0.0839 0.0690  -0.0660 9   TYR   B CZ  
4035 O OH  . TYR   B 9   ? 0.3062 0.2170 0.2803 -0.0983 0.0734  -0.0834 9   TYR   B OH  
4046 N N   . LEU   B 10  ? 0.3258 0.2019 0.1980 -0.0643 0.0251  -0.0387 10  LEU   B N   
4047 C CA  . LEU   B 10  ? 0.3190 0.1972 0.2063 -0.0722 -0.0050 -0.0378 10  LEU   B CA  
4048 C C   . LEU   B 10  ? 0.3005 0.1967 0.2095 -0.0694 -0.0198 -0.0335 10  LEU   B C   
4049 O O   . LEU   B 10  ? 0.2856 0.1976 0.2063 -0.0506 -0.0090 -0.0262 10  LEU   B O   
4050 C CB  . LEU   B 10  ? 0.3356 0.1954 0.2353 -0.0732 -0.0261 -0.0217 10  LEU   B CB  
4051 C CG  . LEU   B 10  ? 0.3531 0.2008 0.2623 -0.0704 -0.0502 -0.0119 10  LEU   B CG  
4052 C CD1 . LEU   B 10  ? 0.3664 0.2154 0.2866 -0.0671 -0.0466 -0.0084 10  LEU   B CD1 
4053 C CD2 . LEU   B 10  ? 0.3600 0.2062 0.2914 -0.0721 -0.0479 0.0116  10  LEU   B CD2 
4065 N N   . LYS   B 11  ? 0.3134 0.2241 0.2240 -0.0644 -0.0346 -0.0271 11  LYS   B N   
4066 C CA  . LYS   B 11  ? 0.3289 0.2532 0.2714 -0.0537 -0.0514 -0.0357 11  LYS   B CA  
4067 C C   . LYS   B 11  ? 0.3066 0.2283 0.2693 -0.0748 -0.0473 -0.0467 11  LYS   B C   
4068 O O   . LYS   B 11  ? 0.3193 0.2461 0.2965 -0.0902 -0.0401 -0.0760 11  LYS   B O   
4069 C CB  . LYS   B 11  ? 0.3657 0.3070 0.3436 -0.0281 -0.0590 -0.0453 11  LYS   B CB  
4070 C CG  . LYS   B 11  ? 0.3974 0.3445 0.4222 -0.0133 -0.0572 -0.0540 11  LYS   B CG  
4071 C CD  . LYS   B 11  ? 0.4231 0.3712 0.4887 -0.0046 -0.0537 -0.0621 11  LYS   B CD  
4072 C CE  . LYS   B 11  ? 0.4410 0.3889 0.5377 -0.0035 -0.0539 -0.0689 11  LYS   B CE  
4073 N NZ  . LYS   B 11  ? 0.4508 0.3990 0.5634 -0.0039 -0.0559 -0.0692 11  LYS   B NZ  
4087 N N   . LEU   B 12  ? 0.2700 0.1998 0.2590 -0.0669 -0.0477 -0.0390 12  LEU   B N   
4088 C CA  . LEU   B 12  ? 0.2500 0.1805 0.2675 -0.0568 -0.0376 -0.0273 12  LEU   B CA  
4089 C C   . LEU   B 12  ? 0.2354 0.1815 0.2732 -0.0529 -0.0511 -0.0226 12  LEU   B C   
4090 O O   . LEU   B 12  ? 0.2311 0.1820 0.2939 -0.0592 -0.0587 -0.0148 12  LEU   B O   
4091 C CB  . LEU   B 12  ? 0.2472 0.1625 0.2574 -0.0430 -0.0275 -0.0291 12  LEU   B CB  
4092 C CG  . LEU   B 12  ? 0.2438 0.1641 0.2520 -0.0385 -0.0152 -0.0138 12  LEU   B CG  
4093 C CD1 . LEU   B 12  ? 0.2525 0.1686 0.2459 -0.0295 -0.0219 0.0032  12  LEU   B CD1 
4094 C CD2 . LEU   B 12  ? 0.2481 0.1667 0.2639 -0.0407 -0.0049 -0.0236 12  LEU   B CD2 
4106 N N   . THR   B 13  ? 0.2251 0.1886 0.2795 -0.0521 -0.0521 -0.0318 13  THR   B N   
4107 C CA  . THR   B 13  ? 0.2253 0.1979 0.2709 -0.0632 -0.0687 -0.0177 13  THR   B CA  
4108 C C   . THR   B 13  ? 0.2638 0.2155 0.2857 -0.0715 -0.0797 -0.0122 13  THR   B C   
4109 O O   . THR   B 13  ? 0.2808 0.2156 0.3027 -0.0718 -0.0470 -0.0178 13  THR   B O   
4110 C CB  . THR   B 13  ? 0.2092 0.2020 0.2740 -0.0567 -0.0591 -0.0092 13  THR   B CB  
4111 O OG1 . THR   B 13  ? 0.1961 0.1977 0.2874 -0.0510 -0.0478 -0.0111 13  THR   B OG1 
4112 C CG2 . THR   B 13  ? 0.2207 0.2063 0.2828 -0.0448 -0.0438 0.0021  13  THR   B CG2 
4120 N N   A ASP   B 14  ? 0.2746 0.2288 0.2957 -0.0778 -0.1055 -0.0052 14  ASP   B N   
4121 N N   B ASP   B 14  ? 0.2744 0.2280 0.2940 -0.0703 -0.0921 -0.0015 14  ASP   B N   
4122 C CA  A ASP   B 14  ? 0.2865 0.2437 0.3191 -0.0795 -0.1086 0.0120  14  ASP   B CA  
4123 C CA  B ASP   B 14  ? 0.2848 0.2409 0.3088 -0.0673 -0.0918 0.0140  14  ASP   B CA  
4124 C C   A ASP   B 14  ? 0.2758 0.2277 0.2832 -0.0802 -0.0935 0.0179  14  ASP   B C   
4125 C C   B ASP   B 14  ? 0.2716 0.2249 0.2779 -0.0697 -0.0882 0.0157  14  ASP   B C   
4126 O O   A ASP   B 14  ? 0.2980 0.2435 0.2897 -0.0797 -0.0853 0.0287  14  ASP   B O   
4127 O O   B ASP   B 14  ? 0.2871 0.2318 0.2811 -0.0669 -0.0861 0.0203  14  ASP   B O   
4128 C CB  A ASP   B 14  ? 0.3087 0.2769 0.3902 -0.0775 -0.1147 0.0132  14  ASP   B CB  
4129 C CB  B ASP   B 14  ? 0.3069 0.2707 0.3616 -0.0605 -0.0886 0.0216  14  ASP   B CB  
4130 C CG  A ASP   B 14  ? 0.3354 0.3080 0.4601 -0.0695 -0.1065 0.0050  14  ASP   B CG  
4131 C CG  B ASP   B 14  ? 0.3301 0.2984 0.4128 -0.0511 -0.0790 0.0226  14  ASP   B CG  
4132 O OD1 A ASP   B 14  ? 0.3511 0.3174 0.4825 -0.0704 -0.1004 -0.0008 14  ASP   B OD1 
4133 O OD1 B ASP   B 14  ? 0.3415 0.3120 0.4261 -0.0471 -0.0690 0.0219  14  ASP   B OD1 
4134 O OD2 A ASP   B 14  ? 0.3386 0.3211 0.4888 -0.0668 -0.1026 0.0081  14  ASP   B OD2 
4135 O OD2 B ASP   B 14  ? 0.3342 0.3051 0.4325 -0.0522 -0.0800 0.0282  14  ASP   B OD2 
4144 N N   . ASN   B 15  ? 0.2423 0.2040 0.2578 -0.0630 -0.0874 0.0198  15  ASN   B N   
4145 C CA  . ASN   B 15  ? 0.1966 0.1745 0.2439 -0.0415 -0.0631 0.0073  15  ASN   B CA  
4146 C C   . ASN   B 15  ? 0.1813 0.1598 0.2377 -0.0266 -0.0467 -0.0011 15  ASN   B C   
4147 O O   . ASN   B 15  ? 0.1807 0.1546 0.2510 -0.0289 -0.0532 -0.0100 15  ASN   B O   
4148 C CB  . ASN   B 15  ? 0.1923 0.1722 0.2623 -0.0179 -0.0621 0.0098  15  ASN   B CB  
4149 C CG  . ASN   B 15  ? 0.1781 0.1656 0.2650 -0.0192 -0.0336 0.0108  15  ASN   B CG  
4150 O OD1 . ASN   B 15  ? 0.1790 0.1935 0.3037 -0.0415 -0.0356 0.0231  15  ASN   B OD1 
4151 N ND2 . ASN   B 15  ? 0.1759 0.1454 0.2577 -0.0123 -0.0073 -0.0109 15  ASN   B ND2 
4159 N N   . VAL   B 16  ? 0.1810 0.1544 0.2263 -0.0348 -0.0509 -0.0043 16  VAL   B N   
4160 C CA  . VAL   B 16  ? 0.1836 0.1586 0.2087 -0.0300 -0.0360 -0.0227 16  VAL   B CA  
4161 C C   . VAL   B 16  ? 0.1831 0.1691 0.2073 -0.0384 -0.0370 -0.0120 16  VAL   B C   
4162 O O   . VAL   B 16  ? 0.1856 0.1816 0.2340 -0.0378 -0.0314 -0.0220 16  VAL   B O   
4163 C CB  . VAL   B 16  ? 0.1886 0.1549 0.2212 -0.0129 -0.0272 -0.0182 16  VAL   B CB  
4164 C CG1 . VAL   B 16  ? 0.1937 0.1455 0.2173 0.0019  -0.0248 -0.0174 16  VAL   B CG1 
4165 C CG2 . VAL   B 16  ? 0.1861 0.1608 0.2404 -0.0116 -0.0248 -0.0182 16  VAL   B CG2 
4175 N N   . TYR   B 17  ? 0.1897 0.1738 0.2050 -0.0367 -0.0329 -0.0185 17  TYR   B N   
4176 C CA  . TYR   B 17  ? 0.1999 0.1819 0.2040 -0.0441 -0.0312 0.0009  17  TYR   B CA  
4177 C C   . TYR   B 17  ? 0.1941 0.1551 0.1990 -0.0474 -0.0242 -0.0092 17  TYR   B C   
4178 O O   . TYR   B 17  ? 0.1893 0.1620 0.2118 -0.0356 -0.0271 -0.0318 17  TYR   B O   
4179 C CB  . TYR   B 17  ? 0.2334 0.2287 0.2331 -0.0286 -0.0404 0.0287  17  TYR   B CB  
4180 C CG  . TYR   B 17  ? 0.2615 0.2835 0.2727 -0.0201 -0.0577 0.0457  17  TYR   B CG  
4181 C CD1 . TYR   B 17  ? 0.2800 0.3014 0.3009 -0.0165 -0.0657 0.0592  17  TYR   B CD1 
4182 C CD2 . TYR   B 17  ? 0.2854 0.3139 0.3060 -0.0100 -0.0667 0.0480  17  TYR   B CD2 
4183 C CE1 . TYR   B 17  ? 0.2987 0.3253 0.3220 -0.0069 -0.0745 0.0582  17  TYR   B CE1 
4184 C CE2 . TYR   B 17  ? 0.3031 0.3338 0.3325 0.0032  -0.0787 0.0557  17  TYR   B CE2 
4185 C CZ  . TYR   B 17  ? 0.3113 0.3438 0.3398 0.0047  -0.0837 0.0606  17  TYR   B CZ  
4186 O OH  . TYR   B 17  ? 0.3257 0.3582 0.3560 0.0144  -0.0959 0.0616  17  TYR   B OH  
4196 N N   . ILE   B 18  ? 0.2073 0.1566 0.1908 -0.0394 -0.0126 -0.0130 18  ILE   B N   
4197 C CA  . ILE   B 18  ? 0.2131 0.1555 0.1979 -0.0396 -0.0122 -0.0213 18  ILE   B CA  
4198 C C   . ILE   B 18  ? 0.2242 0.1617 0.1904 -0.0476 -0.0068 -0.0335 18  ILE   B C   
4199 O O   . ILE   B 18  ? 0.2437 0.1807 0.2085 -0.0483 0.0010  -0.0306 18  ILE   B O   
4200 C CB  . ILE   B 18  ? 0.2160 0.1566 0.2025 -0.0474 -0.0167 -0.0140 18  ILE   B CB  
4201 C CG1 . ILE   B 18  ? 0.2120 0.1651 0.2146 -0.0471 -0.0175 -0.0135 18  ILE   B CG1 
4202 C CG2 . ILE   B 18  ? 0.2215 0.1628 0.2077 -0.0488 -0.0196 -0.0073 18  ILE   B CG2 
4203 C CD1 . ILE   B 18  ? 0.2175 0.1926 0.2210 -0.0429 -0.0208 0.0143  18  ILE   B CD1 
4215 N N   . LYS   B 19  ? 0.2228 0.1611 0.2028 -0.0270 0.0251  -0.0368 19  LYS   B N   
4216 C CA  . LYS   B 19  ? 0.2308 0.1662 0.2115 -0.0342 0.0297  -0.0390 19  LYS   B CA  
4217 C C   . LYS   B 19  ? 0.2115 0.1639 0.2305 -0.0256 0.0337  -0.0427 19  LYS   B C   
4218 O O   . LYS   B 19  ? 0.2000 0.1663 0.2145 -0.0150 0.0203  -0.0287 19  LYS   B O   
4219 C CB  . LYS   B 19  ? 0.2547 0.1898 0.2257 -0.0402 0.0310  -0.0323 19  LYS   B CB  
4220 C CG  . LYS   B 19  ? 0.2797 0.2111 0.2504 -0.0467 0.0383  -0.0300 19  LYS   B CG  
4221 C CD  . LYS   B 19  ? 0.3080 0.2398 0.2611 -0.0538 0.0471  -0.0252 19  LYS   B CD  
4222 C CE  . LYS   B 19  ? 0.3337 0.2627 0.2812 -0.0537 0.0455  -0.0269 19  LYS   B CE  
4223 N NZ  . LYS   B 19  ? 0.3472 0.2772 0.2796 -0.0563 0.0448  -0.0212 19  LYS   B NZ  
4237 N N   . ASN   B 20  ? 0.2082 0.1735 0.2657 -0.0236 0.0368  -0.0568 20  ASN   B N   
4238 C CA  . ASN   B 20  ? 0.2079 0.1923 0.2926 -0.0193 0.0438  -0.0723 20  ASN   B CA  
4239 C C   . ASN   B 20  ? 0.2028 0.2106 0.2910 -0.0244 0.0590  -0.0822 20  ASN   B C   
4240 O O   . ASN   B 20  ? 0.2268 0.2456 0.3111 -0.0438 0.0582  -0.0844 20  ASN   B O   
4241 C CB  . ASN   B 20  ? 0.2361 0.1979 0.3240 0.0061  0.0311  -0.0785 20  ASN   B CB  
4242 C CG  . ASN   B 20  ? 0.2589 0.2024 0.3479 0.0360  0.0316  -0.0891 20  ASN   B CG  
4243 O OD1 . ASN   B 20  ? 0.2905 0.2270 0.3744 0.0499  0.0295  -0.0937 20  ASN   B OD1 
4244 N ND2 . ASN   B 20  ? 0.2443 0.1996 0.3417 0.0345  0.0214  -0.0853 20  ASN   B ND2 
4251 N N   . ALA   B 21  ? 0.1982 0.1962 0.2833 -0.0317 0.0530  -0.0627 21  ALA   B N   
4252 C CA  . ALA   B 21  ? 0.2070 0.2045 0.2976 -0.0309 0.0411  -0.0487 21  ALA   B CA  
4253 C C   . ALA   B 21  ? 0.2085 0.1763 0.2823 -0.0170 0.0364  -0.0353 21  ALA   B C   
4254 O O   . ALA   B 21  ? 0.2114 0.1620 0.2864 -0.0301 0.0289  -0.0285 21  ALA   B O   
4255 C CB  . ALA   B 21  ? 0.2227 0.2384 0.3146 -0.0411 0.0467  -0.0374 21  ALA   B CB  
4261 N N   . ASP   B 22  ? 0.1966 0.1690 0.2730 -0.0187 0.0231  -0.0283 22  ASP   B N   
4262 C CA  . ASP   B 22  ? 0.1935 0.1640 0.2602 -0.0108 0.0156  -0.0234 22  ASP   B CA  
4263 C C   . ASP   B 22  ? 0.1876 0.1580 0.2242 -0.0199 0.0071  -0.0116 22  ASP   B C   
4264 O O   . ASP   B 22  ? 0.1884 0.1629 0.2304 -0.0140 0.0107  -0.0085 22  ASP   B O   
4265 C CB  . ASP   B 22  ? 0.2028 0.1747 0.3090 -0.0054 0.0147  -0.0105 22  ASP   B CB  
4266 C CG  . ASP   B 22  ? 0.2054 0.1934 0.3554 -0.0020 -0.0081 -0.0051 22  ASP   B CG  
4267 O OD1 . ASP   B 22  ? 0.2113 0.1833 0.3557 0.0018  -0.0199 -0.0024 22  ASP   B OD1 
4268 O OD2 . ASP   B 22  ? 0.2143 0.2220 0.3995 0.0090  -0.0301 -0.0180 22  ASP   B OD2 
4273 N N   . ILE   B 23  ? 0.1911 0.1490 0.2055 -0.0143 -0.0011 0.0122  23  ILE   B N   
4274 C CA  . ILE   B 23  ? 0.1803 0.1477 0.1895 -0.0113 -0.0019 0.0037  23  ILE   B CA  
4275 C C   . ILE   B 23  ? 0.1698 0.1492 0.1881 -0.0076 -0.0064 0.0048  23  ILE   B C   
4276 O O   . ILE   B 23  ? 0.1607 0.1537 0.1854 -0.0083 -0.0049 0.0093  23  ILE   B O   
4277 C CB  . ILE   B 23  ? 0.1744 0.1552 0.2044 -0.0193 -0.0006 0.0079  23  ILE   B CB  
4278 C CG1 . ILE   B 23  ? 0.1753 0.1657 0.2229 -0.0115 0.0057  0.0238  23  ILE   B CG1 
4279 C CG2 . ILE   B 23  ? 0.1873 0.1713 0.2185 -0.0225 0.0015  0.0092  23  ILE   B CG2 
4280 C CD1 . ILE   B 23  ? 0.1827 0.1751 0.2264 -0.0102 0.0044  0.0258  23  ILE   B CD1 
4292 N N   . VAL   B 24  ? 0.1724 0.1491 0.1967 -0.0113 -0.0075 -0.0042 24  VAL   B N   
4293 C CA  . VAL   B 24  ? 0.1694 0.1566 0.2210 -0.0076 -0.0176 0.0000  24  VAL   B CA  
4294 C C   . VAL   B 24  ? 0.1675 0.1582 0.2322 -0.0105 -0.0108 0.0110  24  VAL   B C   
4295 O O   . VAL   B 24  ? 0.1584 0.1697 0.2395 -0.0165 -0.0046 0.0167  24  VAL   B O   
4296 C CB  . VAL   B 24  ? 0.1830 0.1751 0.2214 -0.0034 -0.0228 0.0040  24  VAL   B CB  
4297 C CG1 . VAL   B 24  ? 0.1826 0.1784 0.2530 -0.0159 -0.0206 0.0058  24  VAL   B CG1 
4298 C CG2 . VAL   B 24  ? 0.1934 0.2015 0.2184 0.0055  -0.0234 -0.0020 24  VAL   B CG2 
4308 N N   . GLU   B 25  ? 0.1902 0.1658 0.2485 -0.0130 0.0026  0.0076  25  GLU   B N   
4309 C CA  . GLU   B 25  ? 0.1997 0.1927 0.2585 -0.0013 0.0143  -0.0009 25  GLU   B CA  
4310 C C   . GLU   B 25  ? 0.1933 0.1860 0.2067 -0.0132 0.0109  -0.0006 25  GLU   B C   
4311 O O   . GLU   B 25  ? 0.1993 0.2047 0.2193 -0.0187 0.0153  0.0010  25  GLU   B O   
4312 C CB  . GLU   B 25  ? 0.2367 0.2378 0.3264 0.0235  0.0172  -0.0015 25  GLU   B CB  
4313 C CG  . GLU   B 25  ? 0.2853 0.2983 0.4327 0.0324  0.0120  -0.0085 25  GLU   B CG  
4314 C CD  . GLU   B 25  ? 0.3221 0.3610 0.5215 0.0273  0.0054  -0.0133 25  GLU   B CD  
4315 O OE1 . GLU   B 25  ? 0.3530 0.3880 0.5486 0.0321  0.0074  -0.0125 25  GLU   B OE1 
4316 O OE2 . GLU   B 25  ? 0.3456 0.3794 0.5501 0.0238  -0.0008 -0.0200 25  GLU   B OE2 
4323 N N   A GLU   B 26  ? 0.1925 0.1821 0.1865 -0.0298 0.0096  -0.0035 26  GLU   B N   
4324 N N   B GLU   B 26  ? 0.1905 0.1829 0.1948 -0.0239 0.0098  0.0024  26  GLU   B N   
4325 C CA  A GLU   B 26  ? 0.1963 0.1953 0.1983 -0.0358 0.0043  0.0081  26  GLU   B CA  
4326 C CA  B GLU   B 26  ? 0.1895 0.1911 0.2060 -0.0281 0.0056  0.0129  26  GLU   B CA  
4327 C C   A GLU   B 26  ? 0.1791 0.1975 0.1820 -0.0272 0.0078  0.0176  26  GLU   B C   
4328 C C   B GLU   B 26  ? 0.1766 0.1928 0.1863 -0.0242 0.0080  0.0196  26  GLU   B C   
4329 O O   A GLU   B 26  ? 0.1945 0.2155 0.2005 -0.0277 0.0036  0.0191  26  GLU   B O   
4330 O O   B GLU   B 26  ? 0.1876 0.2053 0.1966 -0.0240 0.0052  0.0209  26  GLU   B O   
4331 C CB  A GLU   B 26  ? 0.2286 0.2082 0.2073 -0.0445 0.0107  0.0192  26  GLU   B CB  
4332 C CB  B GLU   B 26  ? 0.2088 0.1995 0.2258 -0.0322 0.0083  0.0214  26  GLU   B CB  
4333 C CG  A GLU   B 26  ? 0.2664 0.2305 0.2374 -0.0491 0.0203  0.0116  26  GLU   B CG  
4334 C CG  B GLU   B 26  ? 0.2322 0.2149 0.2619 -0.0346 0.0158  0.0134  26  GLU   B CG  
4335 C CD  A GLU   B 26  ? 0.2869 0.2418 0.2335 -0.0654 0.0396  -0.0053 26  GLU   B CD  
4336 C CD  B GLU   B 26  ? 0.2401 0.2189 0.2673 -0.0492 0.0264  -0.0052 26  GLU   B CD  
4337 O OE1 A GLU   B 26  ? 0.2936 0.2347 0.2359 -0.0701 0.0683  0.0005  26  GLU   B OE1 
4338 O OE1 B GLU   B 26  ? 0.2366 0.2219 0.2888 -0.0598 0.0485  -0.0255 26  GLU   B OE1 
4339 O OE2 A GLU   B 26  ? 0.2936 0.2586 0.2543 -0.0714 0.0426  0.0049  26  GLU   B OE2 
4340 O OE2 B GLU   B 26  ? 0.2416 0.2180 0.2588 -0.0498 0.0306  -0.0068 26  GLU   B OE2 
4353 N N   . ALA   B 27  ? 0.1652 0.1820 0.1830 -0.0254 0.0079  0.0234  27  ALA   B N   
4354 C CA  . ALA   B 27  ? 0.1631 0.1754 0.1899 -0.0166 -0.0036 0.0328  27  ALA   B CA  
4355 C C   . ALA   B 27  ? 0.1670 0.1860 0.2167 -0.0149 0.0110  0.0427  27  ALA   B C   
4356 O O   . ALA   B 27  ? 0.1769 0.1922 0.2330 -0.0024 0.0088  0.0441  27  ALA   B O   
4357 C CB  . ALA   B 27  ? 0.1844 0.1609 0.2032 -0.0138 0.0036  0.0273  27  ALA   B CB  
4364 N N   . LYS   B 28  ? 0.1581 0.2068 0.2517 -0.0212 0.0136  0.0587  28  LYS   B N   
4365 C CA  . LYS   B 28  ? 0.1810 0.2462 0.2814 -0.0059 0.0486  0.0865  28  LYS   B CA  
4366 C C   . LYS   B 28  ? 0.2050 0.2578 0.2657 -0.0041 0.0655  0.0738  28  LYS   B C   
4367 O O   . LYS   B 28  ? 0.2271 0.2626 0.2804 -0.0060 0.0596  0.0631  28  LYS   B O   
4368 C CB  . LYS   B 28  ? 0.2072 0.2886 0.3394 0.0103  0.0805  0.1159  28  LYS   B CB  
4369 C CG  . LYS   B 28  ? 0.2491 0.3465 0.3834 0.0215  0.1001  0.1340  28  LYS   B CG  
4370 C CD  . LYS   B 28  ? 0.3199 0.4135 0.4483 0.0262  0.1123  0.1424  28  LYS   B CD  
4371 C CE  . LYS   B 28  ? 0.3844 0.4730 0.5084 0.0332  0.1093  0.1463  28  LYS   B CE  
4372 N NZ  . LYS   B 28  ? 0.4230 0.4997 0.5351 0.0374  0.1054  0.1518  28  LYS   B NZ  
4386 N N   . LYS   B 29  ? 0.2213 0.2824 0.2765 0.0154  0.0624  0.0597  29  LYS   B N   
4387 C CA  . LYS   B 29  ? 0.2683 0.3177 0.3018 0.0124  0.0558  0.0605  29  LYS   B CA  
4388 C C   . LYS   B 29  ? 0.2590 0.3152 0.2705 0.0087  0.0407  0.0727  29  LYS   B C   
4389 O O   . LYS   B 29  ? 0.2756 0.3360 0.2822 0.0164  0.0405  0.0760  29  LYS   B O   
4390 C CB  . LYS   B 29  ? 0.3330 0.3608 0.3844 0.0115  0.0500  0.0474  29  LYS   B CB  
4391 C CG  . LYS   B 29  ? 0.3863 0.3978 0.4714 0.0094  0.0486  0.0396  29  LYS   B CG  
4392 C CD  . LYS   B 29  ? 0.4311 0.4243 0.5423 0.0035  0.0570  0.0312  29  LYS   B CD  
4393 C CE  . LYS   B 29  ? 0.4708 0.4422 0.5880 -0.0016 0.0680  0.0251  29  LYS   B CE  
4394 N NZ  . LYS   B 29  ? 0.4867 0.4512 0.6162 -0.0042 0.0718  0.0224  29  LYS   B NZ  
4408 N N   . VAL   B 30  ? 0.2305 0.2931 0.2586 -0.0044 0.0249  0.0742  30  VAL   B N   
4409 C CA  . VAL   B 30  ? 0.2171 0.2825 0.2790 -0.0148 0.0009  0.0746  30  VAL   B CA  
4410 C C   . VAL   B 30  ? 0.1947 0.2724 0.2727 -0.0154 0.0020  0.0880  30  VAL   B C   
4411 O O   . VAL   B 30  ? 0.2112 0.2931 0.2759 -0.0058 0.0052  0.1065  30  VAL   B O   
4412 C CB  . VAL   B 30  ? 0.2253 0.2798 0.3246 -0.0304 -0.0174 0.0720  30  VAL   B CB  
4413 C CG1 . VAL   B 30  ? 0.2333 0.2846 0.3312 -0.0322 -0.0066 0.0660  30  VAL   B CG1 
4414 C CG2 . VAL   B 30  ? 0.2388 0.2823 0.3419 -0.0341 -0.0276 0.0655  30  VAL   B CG2 
4424 N N   A LYS   B 31  ? 0.1791 0.2438 0.2859 -0.0270 0.0062  0.0967  31  LYS   B N   
4425 N N   B LYS   B 31  ? 0.1937 0.2526 0.2770 -0.0220 -0.0021 0.0841  31  LYS   B N   
4426 C CA  A LYS   B 31  ? 0.1651 0.2375 0.3156 -0.0354 0.0030  0.1017  31  LYS   B CA  
4427 C CA  B LYS   B 31  ? 0.1941 0.2447 0.2943 -0.0266 -0.0097 0.0779  31  LYS   B CA  
4428 C C   A LYS   B 31  ? 0.1611 0.2026 0.2839 -0.0307 -0.0161 0.0871  31  LYS   B C   
4429 C C   B LYS   B 31  ? 0.1824 0.2076 0.2663 -0.0273 -0.0253 0.0679  31  LYS   B C   
4430 O O   A LYS   B 31  ? 0.1591 0.2113 0.2994 -0.0264 -0.0057 0.1014  31  LYS   B O   
4431 O O   B LYS   B 31  ? 0.1838 0.2126 0.2714 -0.0273 -0.0252 0.0715  31  LYS   B O   
4432 C CB  A LYS   B 31  ? 0.1763 0.2820 0.3649 -0.0325 0.0203  0.1142  31  LYS   B CB  
4433 C CB  B LYS   B 31  ? 0.2145 0.2807 0.3336 -0.0230 -0.0022 0.0770  31  LYS   B CB  
4434 C CG  A LYS   B 31  ? 0.1987 0.3233 0.4083 -0.0317 0.0340  0.1162  31  LYS   B CG  
4435 C CG  B LYS   B 31  ? 0.2377 0.3128 0.3705 -0.0225 0.0039  0.0687  31  LYS   B CG  
4436 C CD  A LYS   B 31  ? 0.2259 0.3655 0.4505 -0.0241 0.0299  0.1040  31  LYS   B CD  
4437 C CD  B LYS   B 31  ? 0.2588 0.3414 0.4070 -0.0214 0.0024  0.0566  31  LYS   B CD  
4438 C CE  A LYS   B 31  ? 0.2496 0.3987 0.4887 -0.0175 0.0165  0.0916  31  LYS   B CE  
4439 C CE  B LYS   B 31  ? 0.2746 0.3613 0.4396 -0.0201 -0.0029 0.0472  31  LYS   B CE  
4440 N NZ  A LYS   B 31  ? 0.2652 0.4171 0.5073 -0.0100 0.0029  0.0826  31  LYS   B NZ  
4441 N NZ  B LYS   B 31  ? 0.2843 0.3728 0.4551 -0.0168 -0.0107 0.0405  31  LYS   B NZ  
4468 N N   . PRO   B 32  ? 0.1778 0.1691 0.2359 -0.0299 -0.0345 0.0541  32  PRO   B N   
4469 C CA  . PRO   B 32  ? 0.1911 0.1584 0.1979 -0.0363 -0.0373 0.0321  32  PRO   B CA  
4470 C C   . PRO   B 32  ? 0.2001 0.1481 0.1923 -0.0382 -0.0525 0.0375  32  PRO   B C   
4471 O O   . PRO   B 32  ? 0.2099 0.1530 0.2195 -0.0405 -0.0695 0.0325  32  PRO   B O   
4472 C CB  . PRO   B 32  ? 0.2028 0.1504 0.2034 -0.0399 -0.0288 0.0153  32  PRO   B CB  
4473 C CG  . PRO   B 32  ? 0.2174 0.1449 0.2127 -0.0324 -0.0471 0.0266  32  PRO   B CG  
4474 C CD  . PRO   B 32  ? 0.2035 0.1492 0.2228 -0.0239 -0.0555 0.0302  32  PRO   B CD  
4482 N N   . THR   B 33  ? 0.2035 0.1413 0.1826 -0.0327 -0.0482 0.0281  33  THR   B N   
4483 C CA  . THR   B 33  ? 0.2093 0.1507 0.1779 -0.0384 -0.0463 0.0244  33  THR   B CA  
4484 C C   . THR   B 33  ? 0.2100 0.1389 0.1736 -0.0389 -0.0501 0.0209  33  THR   B C   
4485 O O   . THR   B 33  ? 0.2381 0.1461 0.1766 -0.0484 -0.0518 0.0222  33  THR   B O   
4486 C CB  . THR   B 33  ? 0.2141 0.1659 0.1763 -0.0233 -0.0535 0.0269  33  THR   B CB  
4487 O OG1 . THR   B 33  ? 0.1987 0.1657 0.1819 -0.0206 -0.0450 0.0341  33  THR   B OG1 
4488 C CG2 . THR   B 33  ? 0.2395 0.1701 0.1851 -0.0165 -0.0454 0.0231  33  THR   B CG2 
4496 N N   . VAL   B 34  ? 0.1900 0.1368 0.1587 -0.0355 -0.0416 0.0153  34  VAL   B N   
4497 C CA  . VAL   B 34  ? 0.1759 0.1391 0.1516 -0.0288 -0.0311 0.0053  34  VAL   B CA  
4498 C C   . VAL   B 34  ? 0.1641 0.1329 0.1471 -0.0282 -0.0217 0.0014  34  VAL   B C   
4499 O O   . VAL   B 34  ? 0.1797 0.1355 0.1486 -0.0262 -0.0328 0.0063  34  VAL   B O   
4500 C CB  . VAL   B 34  ? 0.1846 0.1448 0.1744 -0.0102 -0.0339 -0.0003 34  VAL   B CB  
4501 C CG1 . VAL   B 34  ? 0.1812 0.1611 0.1747 -0.0018 -0.0197 -0.0026 34  VAL   B CG1 
4502 C CG2 . VAL   B 34  ? 0.1935 0.1499 0.2029 -0.0120 -0.0341 0.0072  34  VAL   B CG2 
4512 N N   . VAL   B 35  ? 0.1553 0.1281 0.1390 -0.0270 -0.0189 0.0059  35  VAL   B N   
4513 C CA  . VAL   B 35  ? 0.1503 0.1252 0.1364 -0.0206 -0.0127 -0.0012 35  VAL   B CA  
4514 C C   . VAL   B 35  ? 0.1445 0.1218 0.1392 -0.0194 -0.0149 0.0039  35  VAL   B C   
4515 O O   . VAL   B 35  ? 0.1439 0.1303 0.1442 -0.0210 -0.0052 -0.0077 35  VAL   B O   
4516 C CB  . VAL   B 35  ? 0.1457 0.1488 0.1423 -0.0193 -0.0009 0.0068  35  VAL   B CB  
4517 C CG1 . VAL   B 35  ? 0.1414 0.1600 0.1685 -0.0192 0.0039  0.0053  35  VAL   B CG1 
4518 C CG2 . VAL   B 35  ? 0.1487 0.1425 0.1688 -0.0145 -0.0055 0.0043  35  VAL   B CG2 
4528 N N   . VAL   B 36  ? 0.1464 0.1254 0.1289 -0.0124 -0.0185 0.0121  36  VAL   B N   
4529 C CA  . VAL   B 36  ? 0.1387 0.1213 0.1136 -0.0099 -0.0081 0.0054  36  VAL   B CA  
4530 C C   . VAL   B 36  ? 0.1354 0.1276 0.1051 -0.0117 -0.0059 0.0086  36  VAL   B C   
4531 O O   . VAL   B 36  ? 0.1382 0.1343 0.1500 -0.0122 -0.0082 -0.0051 36  VAL   B O   
4532 C CB  . VAL   B 36  ? 0.1368 0.1338 0.1404 -0.0104 -0.0052 0.0039  36  VAL   B CB  
4533 C CG1 . VAL   B 36  ? 0.1412 0.1458 0.1474 -0.0166 -0.0048 -0.0025 36  VAL   B CG1 
4534 C CG2 . VAL   B 36  ? 0.1403 0.1398 0.1531 -0.0124 -0.0089 0.0059  36  VAL   B CG2 
4544 N N   . ASN   B 37  ? 0.1390 0.1317 0.1172 -0.0036 -0.0095 0.0042  37  ASN   B N   
4545 C CA  . ASN   B 37  ? 0.1380 0.1355 0.1352 -0.0024 -0.0142 0.0058  37  ASN   B CA  
4546 C C   . ASN   B 37  ? 0.1370 0.1335 0.1415 0.0023  -0.0088 0.0021  37  ASN   B C   
4547 O O   . ASN   B 37  ? 0.1449 0.1424 0.1495 0.0012  0.0010  0.0056  37  ASN   B O   
4548 C CB  . ASN   B 37  ? 0.1386 0.1399 0.1252 -0.0035 -0.0148 0.0051  37  ASN   B CB  
4549 C CG  . ASN   B 37  ? 0.1400 0.1413 0.1393 -0.0029 -0.0108 0.0021  37  ASN   B CG  
4550 O OD1 . ASN   B 37  ? 0.1513 0.1427 0.1625 0.0075  -0.0135 0.0004  37  ASN   B OD1 
4551 N ND2 . ASN   B 37  ? 0.1460 0.1378 0.1416 0.0025  -0.0182 0.0077  37  ASN   B ND2 
4558 N N   . ALA   B 38  ? 0.1497 0.1312 0.1379 0.0074  0.0021  0.0065  38  ALA   B N   
4559 C CA  . ALA   B 38  ? 0.1613 0.1342 0.1418 0.0022  -0.0028 0.0128  38  ALA   B CA  
4560 C C   . ALA   B 38  ? 0.1538 0.1268 0.1511 0.0048  -0.0008 0.0121  38  ALA   B C   
4561 O O   . ALA   B 38  ? 0.1649 0.1371 0.1693 0.0045  -0.0053 0.0089  38  ALA   B O   
4562 C CB  . ALA   B 38  ? 0.1862 0.1445 0.1556 -0.0141 0.0064  0.0077  38  ALA   B CB  
4568 N N   . ALA   B 39  ? 0.1512 0.1325 0.1348 0.0049  -0.0048 0.0076  39  ALA   B N   
4569 C CA  . ALA   B 39  ? 0.1631 0.1414 0.1345 0.0061  -0.0049 0.0028  39  ALA   B CA  
4570 C C   . ALA   B 39  ? 0.1670 0.1470 0.1218 0.0100  -0.0077 0.0049  39  ALA   B C   
4571 O O   . ALA   B 39  ? 0.1669 0.1568 0.1505 -0.0065 -0.0043 0.0063  39  ALA   B O   
4572 C CB  . ALA   B 39  ? 0.1622 0.1474 0.1465 -0.0054 -0.0046 -0.0017 39  ALA   B CB  
4578 N N   . ASN   B 40  ? 0.1675 0.1672 0.1264 -0.0021 -0.0048 0.0004  40  ASN   B N   
4579 C CA  . ASN   B 40  ? 0.1782 0.1700 0.1301 -0.0009 -0.0087 -0.0031 40  ASN   B CA  
4580 C C   . ASN   B 40  ? 0.1820 0.1721 0.1211 0.0039  -0.0151 0.0049  40  ASN   B C   
4581 O O   . ASN   B 40  ? 0.1783 0.1646 0.1346 0.0090  -0.0107 0.0003  40  ASN   B O   
4582 C CB  . ASN   B 40  ? 0.1858 0.1693 0.1453 0.0066  -0.0157 0.0042  40  ASN   B CB  
4583 C CG  . ASN   B 40  ? 0.1906 0.1773 0.1919 0.0022  -0.0270 0.0061  40  ASN   B CG  
4584 O OD1 . ASN   B 40  ? 0.1923 0.1734 0.2682 0.0017  -0.0355 0.0182  40  ASN   B OD1 
4585 N ND2 . ASN   B 40  ? 0.1913 0.1775 0.1884 0.0030  -0.0183 0.0134  40  ASN   B ND2 
4592 N N   . VAL   B 41  ? 0.1908 0.1755 0.1333 0.0106  -0.0009 -0.0022 41  VAL   B N   
4593 C CA  . VAL   B 41  ? 0.1944 0.1872 0.1339 0.0083  -0.0052 -0.0070 41  VAL   B CA  
4594 C C   . VAL   B 41  ? 0.1923 0.1856 0.1388 0.0126  -0.0081 -0.0081 41  VAL   B C   
4595 O O   . VAL   B 41  ? 0.1924 0.1801 0.1576 0.0126  -0.0102 -0.0110 41  VAL   B O   
4596 C CB  . VAL   B 41  ? 0.2115 0.2104 0.1552 -0.0058 0.0174  -0.0178 41  VAL   B CB  
4597 C CG1 . VAL   B 41  ? 0.2095 0.2115 0.1731 -0.0101 0.0309  -0.0212 41  VAL   B CG1 
4598 C CG2 . VAL   B 41  ? 0.2235 0.2316 0.1627 -0.0170 0.0159  -0.0164 41  VAL   B CG2 
4608 N N   . TYR   B 42  ? 0.1988 0.1884 0.1439 0.0134  -0.0200 -0.0023 42  TYR   B N   
4609 C CA  . TYR   B 42  ? 0.2041 0.1935 0.1390 0.0181  -0.0260 -0.0130 42  TYR   B CA  
4610 C C   . TYR   B 42  ? 0.1868 0.1765 0.1513 0.0219  -0.0228 -0.0049 42  TYR   B C   
4611 O O   . TYR   B 42  ? 0.1828 0.1794 0.1964 0.0115  -0.0254 -0.0158 42  TYR   B O   
4612 C CB  . TYR   B 42  ? 0.2229 0.2215 0.1720 0.0108  -0.0291 -0.0039 42  TYR   B CB  
4613 C CG  . TYR   B 42  ? 0.2215 0.2401 0.1784 0.0027  -0.0230 0.0203  42  TYR   B CG  
4614 C CD1 . TYR   B 42  ? 0.2173 0.2414 0.1697 0.0019  -0.0085 0.0273  42  TYR   B CD1 
4615 C CD2 . TYR   B 42  ? 0.2325 0.2558 0.2207 0.0023  -0.0109 0.0261  42  TYR   B CD2 
4616 C CE1 . TYR   B 42  ? 0.2291 0.2544 0.1820 0.0040  -0.0011 0.0281  42  TYR   B CE1 
4617 C CE2 . TYR   B 42  ? 0.2376 0.2652 0.2121 0.0014  0.0213  0.0447  42  TYR   B CE2 
4618 C CZ  . TYR   B 42  ? 0.2526 0.2768 0.2119 0.0188  0.0251  0.0329  42  TYR   B CZ  
4619 O OH  . TYR   B 42  ? 0.2898 0.3081 0.2529 0.0363  0.0312  0.0395  42  TYR   B OH  
4629 N N   . LEU   B 43  ? 0.1772 0.1619 0.1350 0.0100  -0.0131 -0.0095 43  LEU   B N   
4630 C CA  . LEU   B 43  ? 0.1784 0.1600 0.1269 0.0008  -0.0165 -0.0077 43  LEU   B CA  
4631 C C   . LEU   B 43  ? 0.1773 0.1600 0.1400 0.0019  -0.0121 -0.0031 43  LEU   B C   
4632 O O   . LEU   B 43  ? 0.1669 0.1611 0.1760 0.0072  -0.0168 0.0045  43  LEU   B O   
4633 C CB  . LEU   B 43  ? 0.1710 0.1521 0.1547 -0.0067 -0.0279 -0.0050 43  LEU   B CB  
4634 C CG  . LEU   B 43  ? 0.1738 0.1523 0.1751 -0.0045 -0.0225 -0.0075 43  LEU   B CG  
4635 C CD1 . LEU   B 43  ? 0.1824 0.1528 0.2036 -0.0035 -0.0315 -0.0114 43  LEU   B CD1 
4636 C CD2 . LEU   B 43  ? 0.1740 0.1533 0.1802 -0.0100 -0.0256 -0.0093 43  LEU   B CD2 
4648 N N   . LYS   B 44  ? 0.1742 0.1556 0.1526 0.0050  -0.0020 -0.0067 44  LYS   B N   
4649 C CA  . LYS   B 44  ? 0.1884 0.1683 0.1641 0.0028  -0.0102 0.0062  44  LYS   B CA  
4650 C C   . LYS   B 44  ? 0.1752 0.1651 0.1649 0.0065  -0.0110 -0.0021 44  LYS   B C   
4651 O O   . LYS   B 44  ? 0.1900 0.1644 0.1836 0.0031  -0.0034 -0.0010 44  LYS   B O   
4652 C CB  . LYS   B 44  ? 0.2200 0.1868 0.1733 0.0072  -0.0270 0.0075  44  LYS   B CB  
4653 C CG  . LYS   B 44  ? 0.2594 0.2160 0.2190 -0.0009 -0.0556 0.0025  44  LYS   B CG  
4654 C CD  . LYS   B 44  ? 0.2908 0.2381 0.2777 -0.0151 -0.0730 0.0005  44  LYS   B CD  
4655 C CE  . LYS   B 44  ? 0.3209 0.2697 0.3328 -0.0233 -0.0778 0.0151  44  LYS   B CE  
4656 N NZ  . LYS   B 44  ? 0.3271 0.2806 0.3562 -0.0224 -0.0919 0.0334  44  LYS   B NZ  
4670 N N   . HIS   B 45  ? 0.1655 0.1661 0.1581 0.0027  -0.0117 0.0067  45  HIS   B N   
4671 C CA  . HIS   B 45  ? 0.1718 0.1608 0.1582 0.0103  -0.0044 0.0012  45  HIS   B CA  
4672 C C   . HIS   B 45  ? 0.1998 0.1808 0.1977 0.0179  -0.0191 -0.0010 45  HIS   B C   
4673 O O   . HIS   B 45  ? 0.2119 0.2121 0.2341 0.0431  0.0049  -0.0001 45  HIS   B O   
4674 C CB  . HIS   B 45  ? 0.1640 0.1648 0.1564 0.0033  -0.0165 -0.0026 45  HIS   B CB  
4675 C CG  . HIS   B 45  ? 0.1619 0.1586 0.1510 -0.0049 -0.0097 -0.0015 45  HIS   B CG  
4676 N ND1 . HIS   B 45  ? 0.1684 0.1531 0.1612 -0.0020 -0.0154 -0.0046 45  HIS   B ND1 
4677 C CD2 . HIS   B 45  ? 0.1713 0.1576 0.1649 -0.0110 -0.0178 -0.0007 45  HIS   B CD2 
4678 C CE1 . HIS   B 45  ? 0.1795 0.1424 0.1476 -0.0017 -0.0252 -0.0046 45  HIS   B CE1 
4679 N NE2 . HIS   B 45  ? 0.1842 0.1510 0.1538 -0.0021 -0.0201 -0.0033 45  HIS   B NE2 
4687 N N   A GLY   B 46  ? 0.2127 0.1778 0.2383 0.0187  -0.0372 0.0122  46  GLY   B N   
4688 N N   B GLY   B 46  ? 0.2096 0.1848 0.2233 0.0189  -0.0329 0.0100  46  GLY   B N   
4689 C CA  A GLY   B 46  ? 0.2241 0.1873 0.2785 0.0187  -0.0423 0.0092  46  GLY   B CA  
4690 C CA  B GLY   B 46  ? 0.2184 0.1964 0.2483 0.0197  -0.0396 0.0119  46  GLY   B CA  
4691 C C   A GLY   B 46  ? 0.2213 0.2022 0.3208 0.0218  -0.0387 0.0015  46  GLY   B C   
4692 C C   B GLY   B 46  ? 0.2184 0.2120 0.2800 0.0225  -0.0388 0.0129  46  GLY   B C   
4693 O O   A GLY   B 46  ? 0.2290 0.2111 0.4037 0.0275  -0.0247 -0.0216 46  GLY   B O   
4694 O O   B GLY   B 46  ? 0.2245 0.2263 0.3091 0.0282  -0.0348 0.0207  46  GLY   B O   
4701 N N   . GLY   B 47  ? 0.2166 0.2130 0.2877 0.0082  -0.0279 0.0021  47  GLY   B N   
4702 C CA  . GLY   B 47  ? 0.2055 0.1849 0.2458 -0.0040 -0.0286 0.0060  47  GLY   B CA  
4703 C C   . GLY   B 47  ? 0.1880 0.1654 0.2108 -0.0034 -0.0057 0.0162  47  GLY   B C   
4704 O O   . GLY   B 47  ? 0.1941 0.1489 0.2100 0.0017  -0.0095 0.0152  47  GLY   B O   
4709 N N   . GLY   B 48  ? 0.1673 0.1582 0.2053 0.0008  -0.0146 0.0191  48  GLY   B N   
4710 C CA  . GLY   B 48  ? 0.1656 0.1518 0.2055 -0.0063 -0.0064 0.0121  48  GLY   B CA  
4711 C C   . GLY   B 48  ? 0.1557 0.1501 0.1868 0.0027  0.0029  0.0008  48  GLY   B C   
4712 O O   . GLY   B 48  ? 0.1513 0.1508 0.2103 0.0055  -0.0089 0.0037  48  GLY   B O   
4716 N N   . VAL   B 49  ? 0.1607 0.1566 0.1765 0.0102  0.0026  0.0052  49  VAL   B N   
4717 C CA  . VAL   B 49  ? 0.1605 0.1619 0.1722 0.0108  -0.0120 -0.0051 49  VAL   B CA  
4718 C C   . VAL   B 49  ? 0.1519 0.1517 0.1618 0.0098  -0.0129 0.0080  49  VAL   B C   
4719 O O   . VAL   B 49  ? 0.1620 0.1568 0.1782 0.0038  -0.0019 0.0067  49  VAL   B O   
4720 C CB  . VAL   B 49  ? 0.1617 0.1766 0.1941 0.0000  -0.0232 -0.0060 49  VAL   B CB  
4721 C CG1 . VAL   B 49  ? 0.1655 0.1856 0.1926 0.0050  -0.0260 -0.0007 49  VAL   B CG1 
4722 C CG2 . VAL   B 49  ? 0.1802 0.1907 0.2272 -0.0096 -0.0374 -0.0058 49  VAL   B CG2 
4732 N N   . ALA   B 50  ? 0.1508 0.1459 0.1557 0.0011  -0.0041 0.0065  50  ALA   B N   
4733 C CA  . ALA   B 50  ? 0.1517 0.1395 0.1463 0.0056  -0.0050 0.0071  50  ALA   B CA  
4734 C C   . ALA   B 50  ? 0.1560 0.1435 0.1479 0.0056  -0.0010 0.0013  50  ALA   B C   
4735 O O   . ALA   B 50  ? 0.1567 0.1466 0.1611 0.0047  0.0009  -0.0055 50  ALA   B O   
4736 C CB  . ALA   B 50  ? 0.1601 0.1428 0.1529 -0.0055 -0.0099 0.0079  50  ALA   B CB  
4742 N N   . GLY   B 51  ? 0.1503 0.1572 0.1635 0.0135  -0.0127 0.0076  51  GLY   B N   
4743 C CA  . GLY   B 51  ? 0.1548 0.1646 0.1865 0.0180  -0.0213 0.0087  51  GLY   B CA  
4744 C C   . GLY   B 51  ? 0.1566 0.1598 0.1739 0.0217  -0.0084 0.0019  51  GLY   B C   
4745 O O   . GLY   B 51  ? 0.1548 0.1728 0.2019 0.0105  -0.0101 -0.0053 51  GLY   B O   
4749 N N   . ALA   B 52  ? 0.1591 0.1544 0.1713 0.0203  -0.0123 0.0048  52  ALA   B N   
4750 C CA  . ALA   B 52  ? 0.1605 0.1600 0.1745 0.0215  -0.0062 -0.0050 52  ALA   B CA  
4751 C C   . ALA   B 52  ? 0.1442 0.1577 0.1716 0.0123  -0.0016 -0.0035 52  ALA   B C   
4752 O O   . ALA   B 52  ? 0.1476 0.1646 0.1921 0.0082  -0.0044 0.0014  52  ALA   B O   
4753 C CB  . ALA   B 52  ? 0.1786 0.1628 0.1746 0.0133  0.0019  -0.0050 52  ALA   B CB  
4759 N N   . LEU   B 53  ? 0.1434 0.1530 0.1675 0.0132  0.0003  0.0007  53  LEU   B N   
4760 C CA  . LEU   B 53  ? 0.1446 0.1596 0.1589 0.0112  -0.0003 0.0042  53  LEU   B CA  
4761 C C   . LEU   B 53  ? 0.1511 0.1526 0.1391 0.0101  0.0013  0.0066  53  LEU   B C   
4762 O O   . LEU   B 53  ? 0.1564 0.1640 0.1628 0.0018  0.0006  0.0154  53  LEU   B O   
4763 C CB  . LEU   B 53  ? 0.1438 0.1685 0.1725 0.0067  -0.0016 0.0141  53  LEU   B CB  
4764 C CG  . LEU   B 53  ? 0.1417 0.1787 0.1780 0.0012  -0.0089 0.0211  53  LEU   B CG  
4765 C CD1 . LEU   B 53  ? 0.1517 0.2017 0.2029 0.0114  -0.0074 0.0064  53  LEU   B CD1 
4766 C CD2 . LEU   B 53  ? 0.1506 0.2074 0.2038 -0.0086 -0.0164 -0.0064 53  LEU   B CD2 
4778 N N   . ASN   B 54  ? 0.1486 0.1419 0.1405 0.0049  0.0003  0.0053  54  ASN   B N   
4779 C CA  . ASN   B 54  ? 0.1546 0.1569 0.1521 0.0025  -0.0046 -0.0037 54  ASN   B CA  
4780 C C   . ASN   B 54  ? 0.1497 0.1611 0.1853 0.0003  -0.0007 0.0029  54  ASN   B C   
4781 O O   . ASN   B 54  ? 0.1450 0.1691 0.1912 0.0018  -0.0039 0.0035  54  ASN   B O   
4782 C CB  . ASN   B 54  ? 0.1573 0.1677 0.1676 0.0038  -0.0029 0.0001  54  ASN   B CB  
4783 C CG  . ASN   B 54  ? 0.1567 0.1770 0.1733 0.0040  -0.0079 -0.0028 54  ASN   B CG  
4784 O OD1 . ASN   B 54  ? 0.1528 0.1747 0.1897 0.0017  -0.0148 -0.0138 54  ASN   B OD1 
4785 N ND2 . ASN   B 54  ? 0.1718 0.2002 0.2052 -0.0016 -0.0304 0.0096  54  ASN   B ND2 
4792 N N   . LYS   B 55  ? 0.1486 0.1640 0.2060 0.0058  -0.0034 0.0004  55  LYS   B N   
4793 C CA  . LYS   B 55  ? 0.1526 0.1817 0.2170 0.0143  -0.0072 -0.0024 55  LYS   B CA  
4794 C C   . LYS   B 55  ? 0.1502 0.1830 0.2135 0.0136  0.0005  -0.0085 55  LYS   B C   
4795 O O   . LYS   B 55  ? 0.1486 0.1973 0.2265 0.0113  0.0030  -0.0030 55  LYS   B O   
4796 C CB  . LYS   B 55  ? 0.1631 0.1927 0.2664 0.0225  0.0105  0.0126  55  LYS   B CB  
4797 C CG  . LYS   B 55  ? 0.2107 0.2187 0.3556 0.0298  0.0232  0.0328  55  LYS   B CG  
4798 C CD  . LYS   B 55  ? 0.2535 0.2434 0.4212 0.0402  0.0370  0.0519  55  LYS   B CD  
4799 C CE  . LYS   B 55  ? 0.2820 0.2679 0.4863 0.0407  0.0560  0.0584  55  LYS   B CE  
4800 N NZ  . LYS   B 55  ? 0.2873 0.2849 0.5214 0.0405  0.0432  0.0695  55  LYS   B NZ  
4814 N N   . ALA   B 56  ? 0.1524 0.1850 0.1863 0.0116  -0.0046 -0.0053 56  ALA   B N   
4815 C CA  . ALA   B 56  ? 0.1641 0.2050 0.1891 0.0030  0.0033  -0.0114 56  ALA   B CA  
4816 C C   . ALA   B 56  ? 0.1626 0.2007 0.1846 0.0025  0.0111  -0.0022 56  ALA   B C   
4817 O O   . ALA   B 56  ? 0.1669 0.2125 0.2058 0.0052  0.0266  0.0039  56  ALA   B O   
4818 C CB  . ALA   B 56  ? 0.1725 0.2220 0.1994 -0.0143 -0.0024 -0.0052 56  ALA   B CB  
4824 N N   . THR   B 57  ? 0.1583 0.1879 0.1903 -0.0003 0.0161  0.0002  57  THR   B N   
4825 C CA  . THR   B 57  ? 0.1629 0.1846 0.1843 0.0009  0.0224  0.0084  57  THR   B CA  
4826 C C   . THR   B 57  ? 0.1645 0.1910 0.2085 -0.0002 0.0204  0.0056  57  THR   B C   
4827 O O   . THR   B 57  ? 0.1709 0.1901 0.2152 -0.0172 0.0075  -0.0032 57  THR   B O   
4828 C CB  . THR   B 57  ? 0.1682 0.1681 0.1653 -0.0010 0.0068  0.0117  57  THR   B CB  
4829 O OG1 . THR   B 57  ? 0.1632 0.1624 0.1917 -0.0063 0.0103  0.0053  57  THR   B OG1 
4830 C CG2 . THR   B 57  ? 0.1683 0.1754 0.1753 0.0002  0.0058  0.0118  57  THR   B CG2 
4838 N N   . ASN   B 58  ? 0.1489 0.2160 0.2394 -0.0118 0.0102  -0.0062 58  ASN   B N   
4839 C CA  . ASN   B 58  ? 0.1710 0.2600 0.2803 -0.0321 0.0421  0.0040  58  ASN   B CA  
4840 C C   . ASN   B 58  ? 0.1540 0.2292 0.2286 -0.0253 -0.0011 0.0018  58  ASN   B C   
4841 O O   . ASN   B 58  ? 0.1666 0.2378 0.2448 -0.0234 -0.0069 -0.0052 58  ASN   B O   
4842 C CB  . ASN   B 58  ? 0.2823 0.3545 0.4249 -0.0438 0.0923  0.0170  58  ASN   B CB  
4843 C CG  . ASN   B 58  ? 0.4216 0.4535 0.5796 -0.0437 0.1231  0.0374  58  ASN   B CG  
4844 O OD1 . ASN   B 58  ? 0.4365 0.4663 0.6328 -0.0440 0.1324  0.0414  58  ASN   B OD1 
4845 N ND2 . ASN   B 58  ? 0.5149 0.5149 0.6320 -0.0444 0.1348  0.0428  58  ASN   B ND2 
4852 N N   . ASN   B 59  ? 0.1515 0.2141 0.2063 -0.0198 -0.0078 0.0084  59  ASN   B N   
4853 C CA  . ASN   B 59  ? 0.1561 0.2131 0.1944 -0.0202 -0.0157 0.0160  59  ASN   B CA  
4854 C C   . ASN   B 59  ? 0.1532 0.2051 0.1903 -0.0182 -0.0195 0.0039  59  ASN   B C   
4855 O O   . ASN   B 59  ? 0.1579 0.2050 0.1972 -0.0146 -0.0107 0.0034  59  ASN   B O   
4856 C CB  . ASN   B 59  ? 0.1652 0.2302 0.2139 -0.0059 -0.0237 0.0143  59  ASN   B CB  
4857 C CG  . ASN   B 59  ? 0.1786 0.2447 0.2315 0.0006  -0.0386 0.0070  59  ASN   B CG  
4858 O OD1 . ASN   B 59  ? 0.1832 0.2483 0.2295 0.0004  -0.0229 0.0203  59  ASN   B OD1 
4859 N ND2 . ASN   B 59  ? 0.1873 0.2543 0.2561 -0.0097 -0.0382 -0.0025 59  ASN   B ND2 
4866 N N   . ALA   B 60  ? 0.1512 0.1951 0.1879 -0.0102 -0.0074 0.0034  60  ALA   B N   
4867 C CA  . ALA   B 60  ? 0.1588 0.1833 0.1931 -0.0174 -0.0040 0.0116  60  ALA   B CA  
4868 C C   . ALA   B 60  ? 0.1620 0.1744 0.1762 -0.0130 -0.0094 0.0078  60  ALA   B C   
4869 O O   . ALA   B 60  ? 0.1674 0.1766 0.1905 -0.0152 0.0023  -0.0036 60  ALA   B O   
4870 C CB  . ALA   B 60  ? 0.1734 0.1800 0.2252 -0.0198 -0.0027 0.0136  60  ALA   B CB  
4876 N N   . MET   B 61  ? 0.1569 0.1634 0.1729 -0.0115 -0.0068 0.0100  61  MET   B N   
4877 C CA  . MET   B 61  ? 0.1467 0.1574 0.1674 -0.0068 -0.0056 0.0019  61  MET   B CA  
4878 C C   . MET   B 61  ? 0.1566 0.1551 0.1705 -0.0109 -0.0098 0.0013  61  MET   B C   
4879 O O   . MET   B 61  ? 0.1586 0.1558 0.1677 -0.0013 -0.0080 -0.0108 61  MET   B O   
4880 C CB  . MET   B 61  ? 0.1459 0.1598 0.1781 -0.0033 -0.0104 -0.0031 61  MET   B CB  
4881 C CG  . MET   B 61  ? 0.1470 0.1531 0.1725 0.0014  -0.0095 0.0019  61  MET   B CG  
4882 S SD  . MET   B 61  ? 0.1491 0.1556 0.1987 -0.0036 -0.0076 -0.0089 61  MET   B SD  
4883 C CE  . MET   B 61  ? 0.1579 0.1760 0.2050 -0.0038 -0.0012 -0.0197 61  MET   B CE  
4893 N N   . GLN   B 62  ? 0.1532 0.1615 0.1616 -0.0034 -0.0198 0.0051  62  GLN   B N   
4894 C CA  . GLN   B 62  ? 0.1598 0.1635 0.1730 0.0017  -0.0173 -0.0017 62  GLN   B CA  
4895 C C   . GLN   B 62  ? 0.1560 0.1697 0.1782 -0.0055 -0.0244 -0.0037 62  GLN   B C   
4896 O O   . GLN   B 62  ? 0.1726 0.1651 0.1890 -0.0045 -0.0297 -0.0054 62  GLN   B O   
4897 C CB  . GLN   B 62  ? 0.1599 0.1708 0.1771 0.0053  -0.0129 -0.0016 62  GLN   B CB  
4898 C CG  . GLN   B 62  ? 0.1633 0.1762 0.1760 0.0059  -0.0253 -0.0047 62  GLN   B CG  
4899 C CD  . GLN   B 62  ? 0.1670 0.1701 0.1606 0.0087  -0.0243 0.0034  62  GLN   B CD  
4900 O OE1 . GLN   B 62  ? 0.1702 0.1653 0.1805 0.0016  -0.0270 -0.0094 62  GLN   B OE1 
4901 N NE2 . GLN   B 62  ? 0.1698 0.1748 0.1724 0.0088  -0.0195 -0.0036 62  GLN   B NE2 
4910 N N   . VAL   B 63  ? 0.1588 0.1739 0.1919 -0.0077 -0.0239 -0.0065 63  VAL   B N   
4911 C CA  . VAL   B 63  ? 0.1723 0.1769 0.2073 -0.0128 -0.0254 -0.0052 63  VAL   B CA  
4912 C C   . VAL   B 63  ? 0.1755 0.1705 0.1792 -0.0190 -0.0276 -0.0165 63  VAL   B C   
4913 O O   . VAL   B 63  ? 0.1885 0.1688 0.1827 -0.0152 -0.0457 -0.0132 63  VAL   B O   
4914 C CB  . VAL   B 63  ? 0.1709 0.1912 0.2489 -0.0185 -0.0251 -0.0128 63  VAL   B CB  
4915 C CG1 . VAL   B 63  ? 0.1753 0.1964 0.2761 -0.0331 -0.0123 -0.0059 63  VAL   B CG1 
4916 C CG2 . VAL   B 63  ? 0.1667 0.2071 0.2568 -0.0144 -0.0276 -0.0153 63  VAL   B CG2 
4926 N N   . GLU   B 64  ? 0.1732 0.1555 0.1807 -0.0134 -0.0212 -0.0122 64  GLU   B N   
4927 C CA  . GLU   B 64  ? 0.1728 0.1536 0.1822 -0.0114 -0.0259 -0.0028 64  GLU   B CA  
4928 C C   . GLU   B 64  ? 0.1639 0.1492 0.1752 -0.0052 -0.0256 -0.0089 64  GLU   B C   
4929 O O   . GLU   B 64  ? 0.1747 0.1597 0.1710 -0.0140 -0.0269 -0.0108 64  GLU   B O   
4930 C CB  . GLU   B 64  ? 0.1700 0.1591 0.1736 -0.0179 -0.0177 0.0039  64  GLU   B CB  
4931 C CG  . GLU   B 64  ? 0.1810 0.1662 0.1736 -0.0189 -0.0228 -0.0116 64  GLU   B CG  
4932 C CD  . GLU   B 64  ? 0.1823 0.1777 0.1793 -0.0270 -0.0271 -0.0042 64  GLU   B CD  
4933 O OE1 . GLU   B 64  ? 0.1835 0.1913 0.1984 -0.0322 -0.0180 -0.0247 64  GLU   B OE1 
4934 O OE2 . GLU   B 64  ? 0.1912 0.1880 0.1872 -0.0355 -0.0393 -0.0073 64  GLU   B OE2 
4941 N N   . SER   B 65  ? 0.1671 0.1491 0.1591 -0.0067 -0.0132 -0.0140 65  SER   B N   
4942 C CA  . SER   B 65  ? 0.1651 0.1496 0.1613 0.0031  -0.0171 -0.0109 65  SER   B CA  
4943 C C   . SER   B 65  ? 0.1674 0.1531 0.1729 -0.0002 -0.0207 -0.0102 65  SER   B C   
4944 O O   . SER   B 65  ? 0.1693 0.1580 0.1728 -0.0001 -0.0197 -0.0157 65  SER   B O   
4945 C CB  . SER   B 65  ? 0.1642 0.1531 0.1612 -0.0079 -0.0083 -0.0040 65  SER   B CB  
4946 O OG  . SER   B 65  ? 0.1702 0.1519 0.1719 -0.0094 -0.0115 -0.0152 65  SER   B OG  
4952 N N   . ASP   B 66  ? 0.1775 0.1604 0.1646 0.0015  -0.0252 -0.0172 66  ASP   B N   
4953 C CA  . ASP   B 66  ? 0.1853 0.1690 0.1551 0.0037  -0.0268 -0.0105 66  ASP   B CA  
4954 C C   . ASP   B 66  ? 0.1888 0.1743 0.1529 -0.0084 -0.0220 -0.0152 66  ASP   B C   
4955 O O   . ASP   B 66  ? 0.1896 0.1728 0.1693 0.0013  -0.0239 -0.0166 66  ASP   B O   
4956 C CB  . ASP   B 66  ? 0.2019 0.1810 0.1781 0.0064  -0.0381 -0.0160 66  ASP   B CB  
4957 C CG  . ASP   B 66  ? 0.2290 0.1942 0.2079 0.0117  -0.0550 -0.0027 66  ASP   B CG  
4958 O OD1 . ASP   B 66  ? 0.2526 0.1875 0.2217 0.0062  -0.0572 0.0066  66  ASP   B OD1 
4959 O OD2 . ASP   B 66  ? 0.2449 0.2194 0.2699 0.0315  -0.0420 -0.0029 66  ASP   B OD2 
4964 N N   . ASP   B 67  ? 0.1817 0.1668 0.1539 -0.0111 -0.0245 -0.0150 67  ASP   B N   
4965 C CA  . ASP   B 67  ? 0.1961 0.1635 0.1639 -0.0087 -0.0301 -0.0107 67  ASP   B CA  
4966 C C   . ASP   B 67  ? 0.1921 0.1604 0.1799 0.0021  -0.0324 -0.0177 67  ASP   B C   
4967 O O   . ASP   B 67  ? 0.1967 0.1670 0.1949 0.0029  -0.0208 -0.0244 67  ASP   B O   
4968 C CB  . ASP   B 67  ? 0.2195 0.1718 0.1881 -0.0217 -0.0424 -0.0107 67  ASP   B CB  
4969 C CG  . ASP   B 67  ? 0.2559 0.1776 0.2076 -0.0172 -0.0671 -0.0131 67  ASP   B CG  
4970 O OD1 . ASP   B 67  ? 0.2768 0.1835 0.2270 -0.0153 -0.0646 -0.0101 67  ASP   B OD1 
4971 O OD2 . ASP   B 67  ? 0.2712 0.1853 0.2194 0.0006  -0.0728 -0.0105 67  ASP   B OD2 
4976 N N   . TYR   B 68  ? 0.1916 0.1583 0.1802 0.0052  -0.0378 -0.0228 68  TYR   B N   
4977 C CA  . TYR   B 68  ? 0.1847 0.1737 0.1904 0.0110  -0.0368 -0.0267 68  TYR   B CA  
4978 C C   . TYR   B 68  ? 0.1815 0.1724 0.1857 0.0067  -0.0316 -0.0364 68  TYR   B C   
4979 O O   . TYR   B 68  ? 0.1863 0.1853 0.1984 0.0101  -0.0326 -0.0518 68  TYR   B O   
4980 C CB  . TYR   B 68  ? 0.1864 0.1948 0.1946 0.0138  -0.0402 -0.0443 68  TYR   B CB  
4981 C CG  . TYR   B 68  ? 0.1955 0.2172 0.2143 0.0153  -0.0336 -0.0675 68  TYR   B CG  
4982 C CD1 . TYR   B 68  ? 0.1985 0.2197 0.2410 -0.0025 -0.0296 -0.0749 68  TYR   B CD1 
4983 C CD2 . TYR   B 68  ? 0.2007 0.2427 0.2336 0.0264  -0.0466 -0.0690 68  TYR   B CD2 
4984 C CE1 . TYR   B 68  ? 0.2022 0.2378 0.2751 0.0003  -0.0284 -0.0758 68  TYR   B CE1 
4985 C CE2 . TYR   B 68  ? 0.1994 0.2495 0.2559 0.0249  -0.0400 -0.0833 68  TYR   B CE2 
4986 C CZ  . TYR   B 68  ? 0.1942 0.2472 0.2783 0.0091  -0.0372 -0.0860 68  TYR   B CZ  
4987 O OH  . TYR   B 68  ? 0.1910 0.2714 0.3156 0.0027  -0.0314 -0.0665 68  TYR   B OH  
4997 N N   . ILE   B 69  ? 0.1810 0.1651 0.1840 0.0021  -0.0286 -0.0339 69  ILE   B N   
4998 C CA  . ILE   B 69  ? 0.1875 0.1728 0.1923 -0.0019 -0.0276 -0.0333 69  ILE   B CA  
4999 C C   . ILE   B 69  ? 0.1867 0.1698 0.1879 0.0041  -0.0318 -0.0283 69  ILE   B C   
5000 O O   . ILE   B 69  ? 0.1953 0.1792 0.1828 0.0040  -0.0195 -0.0297 69  ILE   B O   
5001 C CB  . ILE   B 69  ? 0.1937 0.1795 0.2159 -0.0042 -0.0025 -0.0287 69  ILE   B CB  
5002 C CG1 . ILE   B 69  ? 0.1942 0.1799 0.2173 -0.0078 0.0070  -0.0316 69  ILE   B CG1 
5003 C CG2 . ILE   B 69  ? 0.2063 0.1855 0.2317 -0.0030 -0.0040 -0.0231 69  ILE   B CG2 
5004 C CD1 . ILE   B 69  ? 0.1878 0.1809 0.2352 -0.0163 0.0155  -0.0319 69  ILE   B CD1 
5016 N N   . ALA   B 70  ? 0.1828 0.1725 0.1928 0.0053  -0.0355 -0.0242 70  ALA   B N   
5017 C CA  . ALA   B 70  ? 0.1849 0.1782 0.1657 -0.0015 -0.0365 -0.0253 70  ALA   B CA  
5018 C C   . ALA   B 70  ? 0.1960 0.1788 0.1774 -0.0062 -0.0390 -0.0305 70  ALA   B C   
5019 O O   . ALA   B 70  ? 0.2038 0.1755 0.1912 -0.0012 -0.0458 -0.0307 70  ALA   B O   
5020 C CB  . ALA   B 70  ? 0.1891 0.1888 0.1701 -0.0006 -0.0289 -0.0242 70  ALA   B CB  
5026 N N   . THR   B 71  ? 0.2007 0.1763 0.1845 0.0001  -0.0515 -0.0342 71  THR   B N   
5027 C CA  . THR   B 71  ? 0.2112 0.1748 0.2072 0.0098  -0.0596 -0.0317 71  THR   B CA  
5028 C C   . THR   B 71  ? 0.2072 0.1797 0.2303 0.0292  -0.0618 -0.0445 71  THR   B C   
5029 O O   . THR   B 71  ? 0.2198 0.1831 0.2747 0.0288  -0.0587 -0.0482 71  THR   B O   
5030 C CB  . THR   B 71  ? 0.2372 0.1950 0.2324 0.0016  -0.0653 -0.0079 71  THR   B CB  
5031 O OG1 . THR   B 71  ? 0.2529 0.2205 0.2617 -0.0197 -0.0637 0.0112  71  THR   B OG1 
5032 C CG2 . THR   B 71  ? 0.2563 0.1882 0.2576 0.0036  -0.0583 0.0031  71  THR   B CG2 
5040 N N   . ASN   B 72  ? 0.1921 0.1838 0.2248 0.0208  -0.0600 -0.0670 72  ASN   B N   
5041 C CA  . ASN   B 72  ? 0.1950 0.1975 0.2267 0.0215  -0.0493 -0.0750 72  ASN   B CA  
5042 C C   . ASN   B 72  ? 0.1967 0.2096 0.2342 0.0077  -0.0254 -0.0664 72  ASN   B C   
5043 O O   . ASN   B 72  ? 0.2006 0.2288 0.2611 0.0027  -0.0112 -0.0679 72  ASN   B O   
5044 C CB  . ASN   B 72  ? 0.2017 0.2114 0.2390 0.0174  -0.0572 -0.0621 72  ASN   B CB  
5045 C CG  . ASN   B 72  ? 0.2183 0.2223 0.2517 0.0291  -0.0516 -0.0402 72  ASN   B CG  
5046 O OD1 . ASN   B 72  ? 0.2403 0.2404 0.2541 0.0150  -0.0385 -0.0443 72  ASN   B OD1 
5047 N ND2 . ASN   B 72  ? 0.2254 0.2316 0.2895 0.0372  -0.0476 -0.0080 72  ASN   B ND2 
5054 N N   . GLY   B 73  ? 0.1977 0.2048 0.2143 0.0018  -0.0274 -0.0609 73  GLY   B N   
5055 C CA  . GLY   B 73  ? 0.1957 0.2108 0.1909 -0.0028 -0.0219 -0.0512 73  GLY   B CA  
5056 C C   . GLY   B 73  ? 0.1894 0.2114 0.1494 0.0043  -0.0230 -0.0432 73  GLY   B C   
5057 O O   . GLY   B 73  ? 0.1819 0.1991 0.1639 0.0071  -0.0246 -0.0344 73  GLY   B O   
5061 N N   . PRO   B 74  ? 0.1889 0.2178 0.1477 0.0020  -0.0216 -0.0322 74  PRO   B N   
5062 C CA  . PRO   B 74  ? 0.1860 0.2215 0.1443 0.0075  -0.0198 -0.0229 74  PRO   B CA  
5063 C C   . PRO   B 74  ? 0.1713 0.2055 0.1561 0.0100  -0.0143 -0.0167 74  PRO   B C   
5064 O O   . PRO   B 74  ? 0.1740 0.2063 0.1901 0.0050  -0.0060 -0.0346 74  PRO   B O   
5065 C CB  . PRO   B 74  ? 0.2005 0.2404 0.1613 0.0050  -0.0162 -0.0208 74  PRO   B CB  
5066 C CG  . PRO   B 74  ? 0.2190 0.2432 0.1793 0.0045  -0.0143 -0.0126 74  PRO   B CG  
5067 C CD  . PRO   B 74  ? 0.2136 0.2313 0.1682 0.0062  -0.0064 -0.0232 74  PRO   B CD  
5075 N N   . LEU   B 75  ? 0.1664 0.1919 0.1426 0.0064  -0.0187 -0.0140 75  LEU   B N   
5076 C CA  . LEU   B 75  ? 0.1658 0.1967 0.1326 -0.0002 -0.0182 -0.0010 75  LEU   B CA  
5077 C C   . LEU   B 75  ? 0.1782 0.2089 0.1262 0.0038  -0.0046 -0.0049 75  LEU   B C   
5078 O O   . LEU   B 75  ? 0.1967 0.2178 0.1393 -0.0024 -0.0083 0.0036  75  LEU   B O   
5079 C CB  . LEU   B 75  ? 0.1785 0.2013 0.1195 -0.0114 -0.0135 0.0131  75  LEU   B CB  
5080 C CG  . LEU   B 75  ? 0.2154 0.2216 0.1436 -0.0286 -0.0097 0.0033  75  LEU   B CG  
5081 C CD1 . LEU   B 75  ? 0.2468 0.2372 0.1494 -0.0331 0.0143  -0.0047 75  LEU   B CD1 
5082 C CD2 . LEU   B 75  ? 0.2486 0.2414 0.2107 -0.0207 -0.0000 0.0064  75  LEU   B CD2 
5094 N N   . LYS   B 76  ? 0.1760 0.2268 0.1683 0.0053  -0.0004 0.0022  76  LYS   B N   
5095 C CA  . LYS   B 76  ? 0.1856 0.2344 0.2029 -0.0027 0.0189  -0.0015 76  LYS   B CA  
5096 C C   . LYS   B 76  ? 0.1766 0.2143 0.1623 0.0029  0.0111  0.0128  76  LYS   B C   
5097 O O   . LYS   B 76  ? 0.1786 0.1975 0.1631 -0.0002 0.0024  0.0119  76  LYS   B O   
5098 C CB  . LYS   B 76  ? 0.2017 0.2454 0.2646 -0.0105 0.0356  -0.0360 76  LYS   B CB  
5099 C CG  . LYS   B 76  ? 0.2090 0.2671 0.3146 0.0015  0.0207  -0.0430 76  LYS   B CG  
5100 C CD  . LYS   B 76  ? 0.2108 0.2797 0.3479 0.0103  0.0088  -0.0603 76  LYS   B CD  
5101 C CE  . LYS   B 76  ? 0.2196 0.2968 0.4000 0.0123  -0.0075 -0.0693 76  LYS   B CE  
5102 N NZ  . LYS   B 76  ? 0.2208 0.3029 0.4121 0.0120  -0.0265 -0.0886 76  LYS   B NZ  
5116 N N   . VAL   B 77  ? 0.1850 0.2224 0.1818 0.0028  0.0136  0.0240  77  VAL   B N   
5117 C CA  . VAL   B 77  ? 0.1894 0.2128 0.1899 0.0121  0.0166  0.0432  77  VAL   B CA  
5118 C C   . VAL   B 77  ? 0.1733 0.1904 0.1737 0.0137  0.0212  0.0288  77  VAL   B C   
5119 O O   . VAL   B 77  ? 0.1763 0.1895 0.1739 0.0231  0.0235  0.0191  77  VAL   B O   
5120 C CB  . VAL   B 77  ? 0.2017 0.2213 0.2320 0.0140  0.0262  0.0567  77  VAL   B CB  
5121 C CG1 . VAL   B 77  ? 0.2066 0.2091 0.2611 0.0092  0.0361  0.0692  77  VAL   B CG1 
5122 C CG2 . VAL   B 77  ? 0.2144 0.2403 0.2487 0.0074  0.0116  0.0642  77  VAL   B CG2 
5132 N N   . GLY   B 78  ? 0.1664 0.1790 0.1701 0.0082  0.0116  0.0189  78  GLY   B N   
5133 C CA  . GLY   B 78  ? 0.1694 0.1732 0.1662 0.0097  0.0146  0.0121  78  GLY   B CA  
5134 C C   . GLY   B 78  ? 0.1646 0.1655 0.1622 0.0079  0.0133  0.0166  78  GLY   B C   
5135 O O   . GLY   B 78  ? 0.1629 0.1631 0.1721 0.0166  0.0109  0.0206  78  GLY   B O   
5139 N N   . GLY   B 79  ? 0.1594 0.1688 0.1747 0.0070  0.0127  0.0124  79  GLY   B N   
5140 C CA  . GLY   B 79  ? 0.1583 0.1583 0.1827 0.0115  0.0080  0.0069  79  GLY   B CA  
5141 C C   . GLY   B 79  ? 0.1503 0.1526 0.1688 0.0117  0.0029  0.0085  79  GLY   B C   
5142 O O   . GLY   B 79  ? 0.1574 0.1502 0.1788 0.0062  0.0098  0.0179  79  GLY   B O   
5146 N N   . SER   B 80  ? 0.1493 0.1523 0.1744 0.0098  0.0144  0.0066  80  SER   B N   
5147 C CA  . SER   B 80  ? 0.1423 0.1455 0.1659 0.0068  0.0069  0.0095  80  SER   B CA  
5148 C C   . SER   B 80  ? 0.1498 0.1408 0.1759 0.0119  -0.0042 -0.0023 80  SER   B C   
5149 O O   . SER   B 80  ? 0.1634 0.1417 0.2071 0.0137  -0.0035 -0.0018 80  SER   B O   
5150 C CB  . SER   B 80  ? 0.1564 0.1520 0.1659 -0.0011 -0.0020 0.0148  80  SER   B CB  
5151 O OG  . SER   B 80  ? 0.1611 0.1686 0.1883 -0.0027 -0.0055 0.0093  80  SER   B OG  
5157 N N   . CYS   B 81  ? 0.1483 0.1320 0.1796 0.0028  -0.0104 -0.0012 81  CYS   B N   
5158 C CA  . CYS   B 81  ? 0.1538 0.1290 0.1801 0.0066  -0.0138 0.0004  81  CYS   B CA  
5159 C C   . CYS   B 81  ? 0.1496 0.1258 0.1560 0.0043  -0.0179 -0.0044 81  CYS   B C   
5160 O O   . CYS   B 81  ? 0.1695 0.1331 0.1727 0.0057  -0.0014 -0.0092 81  CYS   B O   
5161 C CB  . CYS   B 81  ? 0.1648 0.1421 0.1768 -0.0009 -0.0154 -0.0009 81  CYS   B CB  
5162 S SG  . CYS   B 81  ? 0.1672 0.1601 0.1821 -0.0034 -0.0278 -0.0114 81  CYS   B SG  
5168 N N   . VAL   B 82  ? 0.1589 0.1267 0.1598 0.0002  -0.0129 -0.0070 82  VAL   B N   
5169 C CA  . VAL   B 82  ? 0.1663 0.1353 0.1557 -0.0035 -0.0123 0.0075  82  VAL   B CA  
5170 C C   . VAL   B 82  ? 0.1645 0.1267 0.1748 -0.0036 -0.0130 0.0077  82  VAL   B C   
5171 O O   . VAL   B 82  ? 0.1754 0.1272 0.1984 -0.0016 -0.0093 -0.0094 82  VAL   B O   
5172 C CB  . VAL   B 82  ? 0.1704 0.1555 0.1723 -0.0007 -0.0149 0.0069  82  VAL   B CB  
5173 C CG1 . VAL   B 82  ? 0.1887 0.1729 0.1776 0.0122  -0.0154 0.0203  82  VAL   B CG1 
5174 C CG2 . VAL   B 82  ? 0.1757 0.1667 0.1856 -0.0012 -0.0271 0.0071  82  VAL   B CG2 
5184 N N   . LEU   B 83  ? 0.1521 0.1277 0.1635 -0.0148 -0.0254 -0.0027 83  LEU   B N   
5185 C CA  . LEU   B 83  ? 0.1565 0.1357 0.1507 -0.0154 -0.0230 -0.0018 83  LEU   B CA  
5186 C C   . LEU   B 83  ? 0.1579 0.1327 0.1468 -0.0183 -0.0195 -0.0041 83  LEU   B C   
5187 O O   . LEU   B 83  ? 0.1551 0.1426 0.1471 -0.0198 -0.0108 0.0047  83  LEU   B O   
5188 C CB  . LEU   B 83  ? 0.1630 0.1490 0.1547 -0.0149 -0.0239 -0.0103 83  LEU   B CB  
5189 C CG  . LEU   B 83  ? 0.1794 0.1663 0.1603 -0.0236 -0.0155 -0.0058 83  LEU   B CG  
5190 C CD1 . LEU   B 83  ? 0.1930 0.1722 0.1836 -0.0181 -0.0195 -0.0023 83  LEU   B CD1 
5191 C CD2 . LEU   B 83  ? 0.2032 0.1654 0.1756 -0.0124 -0.0157 -0.0192 83  LEU   B CD2 
5203 N N   . SER   B 84  ? 0.1663 0.1408 0.1659 -0.0212 -0.0215 0.0055  84  SER   B N   
5204 C CA  . SER   B 84  ? 0.1635 0.1586 0.1574 -0.0289 -0.0163 0.0192  84  SER   B CA  
5205 C C   . SER   B 84  ? 0.1552 0.1832 0.1276 -0.0264 -0.0172 0.0273  84  SER   B C   
5206 O O   . SER   B 84  ? 0.1615 0.1617 0.1316 -0.0225 -0.0110 0.0075  84  SER   B O   
5207 C CB  . SER   B 84  ? 0.1787 0.1618 0.2096 -0.0309 0.0067  0.0139  84  SER   B CB  
5208 O OG  . SER   B 84  ? 0.1802 0.1807 0.2524 -0.0395 0.0083  0.0214  84  SER   B OG  
5214 N N   . GLY   B 85  ? 0.1550 0.2063 0.1437 -0.0268 -0.0188 0.0257  85  GLY   B N   
5215 C CA  . GLY   B 85  ? 0.1582 0.2118 0.1557 -0.0361 -0.0076 0.0015  85  GLY   B CA  
5216 C C   . GLY   B 85  ? 0.1561 0.1957 0.1455 -0.0447 -0.0125 0.0079  85  GLY   B C   
5217 O O   . GLY   B 85  ? 0.1673 0.1916 0.1655 -0.0551 0.0085  -0.0101 85  GLY   B O   
5221 N N   . HIS   B 86  ? 0.1562 0.1821 0.1572 -0.0347 -0.0163 0.0181  86  HIS   B N   
5222 C CA  . HIS   B 86  ? 0.1557 0.1801 0.1413 -0.0373 -0.0216 0.0206  86  HIS   B CA  
5223 C C   . HIS   B 86  ? 0.1594 0.1970 0.1280 -0.0514 -0.0077 0.0337  86  HIS   B C   
5224 O O   . HIS   B 86  ? 0.1767 0.2086 0.1424 -0.0377 0.0024  0.0222  86  HIS   B O   
5225 C CB  . HIS   B 86  ? 0.1682 0.1765 0.1436 -0.0314 -0.0203 0.0075  86  HIS   B CB  
5226 C CG  . HIS   B 86  ? 0.1758 0.1823 0.1443 -0.0237 -0.0184 0.0148  86  HIS   B CG  
5227 N ND1 . HIS   B 86  ? 0.1832 0.2054 0.1732 -0.0299 -0.0246 0.0022  86  HIS   B ND1 
5228 C CD2 . HIS   B 86  ? 0.1746 0.1818 0.1663 -0.0131 -0.0166 0.0129  86  HIS   B CD2 
5229 C CE1 . HIS   B 86  ? 0.1864 0.2003 0.1630 -0.0206 -0.0112 -0.0164 86  HIS   B CE1 
5230 N NE2 . HIS   B 86  ? 0.1816 0.1913 0.1583 0.0011  -0.0100 0.0008  86  HIS   B NE2 
5238 N N   . ASN   B 87  ? 0.1664 0.1966 0.1587 -0.0403 -0.0077 0.0212  87  ASN   B N   
5239 C CA  . ASN   B 87  ? 0.1742 0.2054 0.1634 -0.0357 0.0144  0.0219  87  ASN   B CA  
5240 C C   . ASN   B 87  ? 0.1857 0.1945 0.1556 -0.0349 0.0253  0.0088  87  ASN   B C   
5241 O O   . ASN   B 87  ? 0.2100 0.2049 0.1845 -0.0325 0.0377  -0.0001 87  ASN   B O   
5242 C CB  . ASN   B 87  ? 0.1753 0.2417 0.2054 -0.0265 0.0175  0.0090  87  ASN   B CB  
5243 C CG  . ASN   B 87  ? 0.1831 0.2587 0.2109 0.0080  0.0258  0.0293  87  ASN   B CG  
5244 O OD1 . ASN   B 87  ? 0.1775 0.2431 0.1924 0.0109  0.0383  0.0444  87  ASN   B OD1 
5245 N ND2 . ASN   B 87  ? 0.2143 0.2725 0.2596 0.0161  0.0390  0.0286  87  ASN   B ND2 
5252 N N   . LEU   B 88  ? 0.1742 0.1844 0.1379 -0.0359 0.0085  0.0103  88  LEU   B N   
5253 C CA  . LEU   B 88  ? 0.1834 0.1750 0.1538 -0.0361 0.0046  0.0045  88  LEU   B CA  
5254 C C   . LEU   B 88  ? 0.1839 0.1597 0.1607 -0.0420 -0.0030 0.0046  88  LEU   B C   
5255 O O   . LEU   B 88  ? 0.2124 0.1710 0.1883 -0.0258 -0.0283 -0.0057 88  LEU   B O   
5256 C CB  . LEU   B 88  ? 0.1963 0.1802 0.1711 -0.0376 -0.0106 0.0133  88  LEU   B CB  
5257 C CG  . LEU   B 88  ? 0.2388 0.2114 0.1934 -0.0297 -0.0227 0.0311  88  LEU   B CG  
5258 C CD1 . LEU   B 88  ? 0.2508 0.2416 0.2089 -0.0393 -0.0176 0.0474  88  LEU   B CD1 
5259 C CD2 . LEU   B 88  ? 0.2738 0.2354 0.2518 0.0047  -0.0487 0.0090  88  LEU   B CD2 
5271 N N   . ALA   B 89  ? 0.1650 0.1632 0.1486 -0.0399 0.0122  0.0010  89  ALA   B N   
5272 C CA  . ALA   B 89  ? 0.1614 0.1609 0.1477 -0.0388 0.0047  0.0075  89  ALA   B CA  
5273 C C   . ALA   B 89  ? 0.1764 0.1652 0.1488 -0.0407 0.0110  0.0033  89  ALA   B C   
5274 O O   . ALA   B 89  ? 0.1616 0.1706 0.1782 -0.0377 0.0105  -0.0215 89  ALA   B O   
5275 C CB  . ALA   B 89  ? 0.1580 0.1619 0.1515 -0.0417 0.0016  0.0124  89  ALA   B CB  
5281 N N   . LYS   B 90  ? 0.2128 0.1519 0.1515 -0.0455 -0.0094 0.0131  90  LYS   B N   
5282 C CA  . LYS   B 90  ? 0.2244 0.1467 0.1412 -0.0420 -0.0092 0.0082  90  LYS   B CA  
5283 C C   . LYS   B 90  ? 0.2085 0.1375 0.1544 -0.0427 -0.0122 -0.0023 90  LYS   B C   
5284 O O   . LYS   B 90  ? 0.2186 0.1599 0.1796 -0.0607 -0.0031 0.0005  90  LYS   B O   
5285 C CB  . LYS   B 90  ? 0.2409 0.1531 0.1815 -0.0383 0.0028  0.0152  90  LYS   B CB  
5286 C CG  . LYS   B 90  ? 0.2555 0.1657 0.1962 -0.0242 0.0333  0.0111  90  LYS   B CG  
5287 C CD  . LYS   B 90  ? 0.2867 0.1926 0.2487 -0.0215 0.0638  -0.0159 90  LYS   B CD  
5288 C CE  . LYS   B 90  ? 0.3053 0.2104 0.3150 -0.0266 0.0901  -0.0286 90  LYS   B CE  
5289 N NZ  . LYS   B 90  ? 0.3163 0.2033 0.3196 -0.0385 0.1142  -0.0330 90  LYS   B NZ  
5303 N N   . HIS   B 91  ? 0.1799 0.1295 0.1353 -0.0322 -0.0221 0.0111  91  HIS   B N   
5304 C CA  . HIS   B 91  ? 0.1719 0.1350 0.1444 -0.0249 -0.0212 0.0035  91  HIS   B CA  
5305 C C   . HIS   B 91  ? 0.1605 0.1366 0.1306 -0.0300 -0.0054 0.0064  91  HIS   B C   
5306 O O   . HIS   B 91  ? 0.1742 0.1392 0.1393 -0.0293 -0.0200 0.0051  91  HIS   B O   
5307 C CB  . HIS   B 91  ? 0.1866 0.1368 0.1835 -0.0104 -0.0094 0.0120  91  HIS   B CB  
5308 C CG  . HIS   B 91  ? 0.2270 0.1538 0.2605 0.0009  0.0217  0.0252  91  HIS   B CG  
5309 N ND1 . HIS   B 91  ? 0.2572 0.1554 0.3191 0.0023  0.0325  0.0101  91  HIS   B ND1 
5310 C CD2 . HIS   B 91  ? 0.2376 0.1861 0.3038 0.0141  0.0108  0.0524  91  HIS   B CD2 
5311 C CE1 . HIS   B 91  ? 0.2575 0.1757 0.3366 0.0180  0.0344  0.0152  91  HIS   B CE1 
5312 N NE2 . HIS   B 91  ? 0.2494 0.1923 0.3320 0.0270  0.0245  0.0543  91  HIS   B NE2 
5320 N N   . CYS   B 92  ? 0.1492 0.1363 0.1334 -0.0282 -0.0119 0.0005  92  CYS   B N   
5321 C CA  . CYS   B 92  ? 0.1514 0.1314 0.1443 -0.0199 -0.0074 0.0029  92  CYS   B CA  
5322 C C   . CYS   B 92  ? 0.1431 0.1209 0.1345 -0.0127 -0.0074 0.0050  92  CYS   B C   
5323 O O   . CYS   B 92  ? 0.1542 0.1303 0.1516 -0.0165 -0.0040 -0.0029 92  CYS   B O   
5324 C CB  . CYS   B 92  ? 0.1512 0.1433 0.1511 -0.0116 -0.0091 0.0020  92  CYS   B CB  
5325 S SG  . CYS   B 92  ? 0.1479 0.1418 0.1485 -0.0138 -0.0123 0.0050  92  CYS   B SG  
5331 N N   . LEU   B 93  ? 0.1356 0.1278 0.1428 -0.0133 -0.0058 0.0021  93  LEU   B N   
5332 C CA  . LEU   B 93  ? 0.1356 0.1328 0.1424 -0.0077 -0.0090 0.0036  93  LEU   B CA  
5333 C C   . LEU   B 93  ? 0.1328 0.1309 0.1249 -0.0011 -0.0041 0.0108  93  LEU   B C   
5334 O O   . LEU   B 93  ? 0.1421 0.1275 0.1549 -0.0110 -0.0093 -0.0014 93  LEU   B O   
5335 C CB  . LEU   B 93  ? 0.1413 0.1323 0.1580 0.0029  -0.0107 0.0105  93  LEU   B CB  
5336 C CG  . LEU   B 93  ? 0.1347 0.1409 0.1721 -0.0044 -0.0072 0.0090  93  LEU   B CG  
5337 C CD1 . LEU   B 93  ? 0.1394 0.1534 0.1780 0.0059  -0.0033 0.0001  93  LEU   B CD1 
5338 C CD2 . LEU   B 93  ? 0.1394 0.1423 0.1833 -0.0042 -0.0078 0.0081  93  LEU   B CD2 
5350 N N   . HIS   B 94  ? 0.1399 0.1297 0.1221 -0.0063 -0.0111 0.0053  94  HIS   B N   
5351 C CA  . HIS   B 94  ? 0.1404 0.1292 0.1200 0.0001  -0.0047 0.0018  94  HIS   B CA  
5352 C C   . HIS   B 94  ? 0.1369 0.1302 0.1511 -0.0025 -0.0019 0.0073  94  HIS   B C   
5353 O O   . HIS   B 94  ? 0.1392 0.1390 0.1903 -0.0062 0.0117  -0.0040 94  HIS   B O   
5354 C CB  . HIS   B 94  ? 0.1382 0.1330 0.1472 -0.0031 -0.0084 0.0019  94  HIS   B CB  
5355 C CG  . HIS   B 94  ? 0.1411 0.1317 0.1528 -0.0084 -0.0238 0.0004  94  HIS   B CG  
5356 N ND1 . HIS   B 94  ? 0.1392 0.1337 0.1518 -0.0069 -0.0228 0.0013  94  HIS   B ND1 
5357 C CD2 . HIS   B 94  ? 0.1469 0.1371 0.1449 -0.0028 -0.0188 0.0020  94  HIS   B CD2 
5358 C CE1 . HIS   B 94  ? 0.1490 0.1344 0.1569 -0.0125 -0.0211 -0.0003 94  HIS   B CE1 
5359 N NE2 . HIS   B 94  ? 0.1426 0.1365 0.1589 -0.0154 -0.0097 0.0087  94  HIS   B NE2 
5367 N N   . VAL   B 95  ? 0.1309 0.1265 0.1603 -0.0032 0.0026  0.0048  95  VAL   B N   
5368 C CA  . VAL   B 95  ? 0.1347 0.1346 0.1561 0.0009  0.0020  0.0135  95  VAL   B CA  
5369 C C   . VAL   B 95  ? 0.1441 0.1284 0.1576 -0.0068 0.0020  0.0078  95  VAL   B C   
5370 O O   . VAL   B 95  ? 0.1432 0.1301 0.1761 0.0041  0.0011  0.0111  95  VAL   B O   
5371 C CB  . VAL   B 95  ? 0.1407 0.1384 0.1500 -0.0020 -0.0113 0.0086  95  VAL   B CB  
5372 C CG1 . VAL   B 95  ? 0.1449 0.1519 0.1718 -0.0116 0.0001  0.0143  95  VAL   B CG1 
5373 C CG2 . VAL   B 95  ? 0.1529 0.1329 0.1533 -0.0000 -0.0091 0.0080  95  VAL   B CG2 
5383 N N   . VAL   B 96  ? 0.1511 0.1381 0.1610 0.0086  0.0074  0.0144  96  VAL   B N   
5384 C CA  . VAL   B 96  ? 0.1596 0.1546 0.1474 0.0049  0.0054  0.0173  96  VAL   B CA  
5385 C C   . VAL   B 96  ? 0.1640 0.1565 0.1621 0.0070  0.0125  0.0184  96  VAL   B C   
5386 O O   . VAL   B 96  ? 0.1640 0.1625 0.1739 0.0005  0.0128  0.0041  96  VAL   B O   
5387 C CB  . VAL   B 96  ? 0.1639 0.1723 0.1522 0.0070  0.0030  0.0129  96  VAL   B CB  
5388 C CG1 . VAL   B 96  ? 0.1613 0.1848 0.1755 0.0117  -0.0021 0.0072  96  VAL   B CG1 
5389 C CG2 . VAL   B 96  ? 0.1755 0.1759 0.1613 0.0031  0.0148  0.0038  96  VAL   B CG2 
5399 N N   . GLY   B 97  ? 0.1685 0.1549 0.1532 0.0029  0.0062  0.0233  97  GLY   B N   
5400 C CA  . GLY   B 97  ? 0.1806 0.1614 0.1551 -0.0027 0.0102  0.0163  97  GLY   B CA  
5401 C C   . GLY   B 97  ? 0.1971 0.1699 0.1711 0.0053  0.0036  0.0128  97  GLY   B C   
5402 O O   . GLY   B 97  ? 0.2062 0.1718 0.1698 0.0028  -0.0000 0.0130  97  GLY   B O   
5406 N N   . PRO   B 98  ? 0.2092 0.1697 0.1773 0.0060  0.0210  0.0269  98  PRO   B N   
5407 C CA  . PRO   B 98  ? 0.2223 0.1866 0.1835 0.0149  0.0284  0.0210  98  PRO   B CA  
5408 C C   . PRO   B 98  ? 0.2348 0.1886 0.1548 0.0294  0.0325  0.0330  98  PRO   B C   
5409 O O   . PRO   B 98  ? 0.2324 0.1874 0.1617 0.0223  0.0289  0.0331  98  PRO   B O   
5410 C CB  . PRO   B 98  ? 0.2120 0.1913 0.1967 0.0123  0.0372  0.0288  98  PRO   B CB  
5411 C CG  . PRO   B 98  ? 0.2035 0.1819 0.1990 0.0087  0.0325  0.0391  98  PRO   B CG  
5412 C CD  . PRO   B 98  ? 0.1930 0.1709 0.1907 0.0083  0.0212  0.0362  98  PRO   B CD  
5420 N N   . ASN   B 99  ? 0.2405 0.2059 0.1744 0.0409  0.0343  0.0191  99  ASN   B N   
5421 C CA  . ASN   B 99  ? 0.2595 0.2133 0.1812 0.0464  0.0267  0.0435  99  ASN   B CA  
5422 C C   . ASN   B 99  ? 0.2927 0.2511 0.2156 0.0397  0.0478  0.0801  99  ASN   B C   
5423 O O   . ASN   B 99  ? 0.3061 0.2581 0.2209 0.0435  0.0361  0.0792  99  ASN   B O   
5424 C CB  . ASN   B 99  ? 0.2684 0.2072 0.1914 0.0447  0.0107  0.0384  99  ASN   B CB  
5425 C CG  . ASN   B 99  ? 0.2720 0.2138 0.2128 0.0413  -0.0019 0.0302  99  ASN   B CG  
5426 O OD1 . ASN   B 99  ? 0.2764 0.2165 0.2371 0.0392  0.0064  0.0368  99  ASN   B OD1 
5427 N ND2 . ASN   B 99  ? 0.2718 0.2162 0.2239 0.0439  -0.0230 0.0264  99  ASN   B ND2 
5434 N N   A VAL   B 100 ? 0.3143 0.2640 0.2511 0.0318  0.0504  0.1025  100 VAL   B N   
5435 N N   B VAL   B 100 ? 0.3151 0.2657 0.2541 0.0318  0.0456  0.0953  100 VAL   B N   
5436 C CA  A VAL   B 100 ? 0.3436 0.2832 0.3031 0.0200  0.0498  0.1216  100 VAL   B CA  
5437 C CA  B VAL   B 100 ? 0.3427 0.2838 0.2989 0.0219  0.0412  0.1082  100 VAL   B CA  
5438 C C   A VAL   B 100 ? 0.3657 0.2896 0.2918 0.0259  0.0461  0.1315  100 VAL   B C   
5439 C C   B VAL   B 100 ? 0.3644 0.2904 0.2921 0.0274  0.0391  0.1234  100 VAL   B C   
5440 O O   A VAL   B 100 ? 0.3738 0.2993 0.2921 0.0232  0.0526  0.1208  100 VAL   B O   
5441 O O   B VAL   B 100 ? 0.3704 0.2975 0.2916 0.0249  0.0428  0.1153  100 VAL   B O   
5442 C CB  A VAL   B 100 ? 0.3537 0.2989 0.3701 0.0041  0.0495  0.1308  100 VAL   B CB  
5443 C CB  B VAL   B 100 ? 0.3503 0.2968 0.3517 0.0087  0.0380  0.1075  100 VAL   B CB  
5444 C CG1 A VAL   B 100 ? 0.3598 0.3052 0.3966 0.0018  0.0492  0.1305  100 VAL   B CG1 
5445 C CG1 B VAL   B 100 ? 0.3549 0.3017 0.3725 0.0063  0.0371  0.1055  100 VAL   B CG1 
5446 C CG2 A VAL   B 100 ? 0.3541 0.3020 0.3895 -0.0039 0.0532  0.1410  100 VAL   B CG2 
5447 C CG2 B VAL   B 100 ? 0.3510 0.3001 0.3677 0.0025  0.0388  0.1110  100 VAL   B CG2 
5466 N N   . ASN   B 101 ? 0.3795 0.2941 0.2930 0.0366  0.0315  0.1375  101 ASN   B N   
5467 C CA  . ASN   B 101 ? 0.4166 0.3132 0.3092 0.0477  0.0069  0.1434  101 ASN   B CA  
5468 C C   . ASN   B 101 ? 0.4600 0.3538 0.3239 0.0482  -0.0059 0.1587  101 ASN   B C   
5469 O O   . ASN   B 101 ? 0.4671 0.3689 0.3542 0.0532  -0.0036 0.1355  101 ASN   B O   
5470 C CB  . ASN   B 101 ? 0.4151 0.2972 0.3297 0.0459  0.0080  0.1159  101 ASN   B CB  
5471 C CG  . ASN   B 101 ? 0.4137 0.2798 0.3408 0.0492  0.0058  0.1058  101 ASN   B CG  
5472 O OD1 . ASN   B 101 ? 0.4162 0.2740 0.3578 0.0422  0.0203  0.0984  101 ASN   B OD1 
5473 N ND2 . ASN   B 101 ? 0.4104 0.2741 0.3375 0.0506  -0.0004 0.0981  101 ASN   B ND2 
5481 N N   . LYS   B 102 ? 0.4945 0.3890 0.3427 0.0361  -0.0027 0.1577  102 LYS   B N   
5482 C CA  . LYS   B 102 ? 0.5274 0.4324 0.3723 0.0190  0.0045  0.1277  102 LYS   B CA  
5483 C C   . LYS   B 102 ? 0.5230 0.4342 0.3569 0.0171  0.0092  0.1358  102 LYS   B C   
5484 O O   . LYS   B 102 ? 0.5325 0.4408 0.3689 0.0175  -0.0057 0.1318  102 LYS   B O   
5485 C CB  . LYS   B 102 ? 0.5600 0.4715 0.4315 0.0055  0.0155  0.0797  102 LYS   B CB  
5486 C CG  . LYS   B 102 ? 0.5871 0.5059 0.4953 -0.0055 0.0275  0.0337  102 LYS   B CG  
5487 C CD  . LYS   B 102 ? 0.6097 0.5339 0.5628 -0.0129 0.0409  -0.0049 102 LYS   B CD  
5488 C CE  . LYS   B 102 ? 0.6259 0.5528 0.6152 -0.0184 0.0505  -0.0333 102 LYS   B CE  
5489 N NZ  . LYS   B 102 ? 0.6347 0.5640 0.6480 -0.0203 0.0545  -0.0485 102 LYS   B NZ  
5503 N N   . GLY   B 103 ? 0.5049 0.4242 0.3507 0.0149  0.0273  0.1376  103 GLY   B N   
5504 C CA  . GLY   B 103 ? 0.4848 0.4140 0.3584 0.0149  0.0433  0.1182  103 GLY   B CA  
5505 C C   . GLY   B 103 ? 0.4608 0.3990 0.3580 0.0145  0.0559  0.0938  103 GLY   B C   
5506 O O   . GLY   B 103 ? 0.4670 0.4076 0.3641 0.0143  0.0565  0.0919  103 GLY   B O   
5510 N N   A GLU   B 104 ? 0.4446 0.3847 0.3496 0.0159  0.0664  0.0784  104 GLU   B N   
5511 N N   B GLU   B 104 ? 0.4432 0.3859 0.3538 0.0122  0.0543  0.0766  104 GLU   B N   
5512 C CA  A GLU   B 104 ? 0.4263 0.3704 0.3401 0.0199  0.0707  0.0594  104 GLU   B CA  
5513 C CA  B GLU   B 104 ? 0.4239 0.3724 0.3470 0.0113  0.0489  0.0560  104 GLU   B CA  
5514 C C   A GLU   B 104 ? 0.4273 0.3725 0.3527 0.0065  0.1051  0.0611  104 GLU   B C   
5515 C C   B GLU   B 104 ? 0.4195 0.3712 0.3582 0.0046  0.0678  0.0513  104 GLU   B C   
5516 O O   A GLU   B 104 ? 0.4281 0.3755 0.3655 0.0020  0.1086  0.0621  104 GLU   B O   
5517 O O   B GLU   B 104 ? 0.4201 0.3723 0.3674 0.0023  0.0695  0.0496  104 GLU   B O   
5518 C CB  A GLU   B 104 ? 0.4087 0.3517 0.3269 0.0369  0.0361  0.0305  104 GLU   B CB  
5519 C CB  B GLU   B 104 ? 0.4102 0.3581 0.3339 0.0165  0.0228  0.0349  104 GLU   B CB  
5520 C CG  A GLU   B 104 ? 0.3921 0.3359 0.3075 0.0529  0.0009  -0.0010 104 GLU   B CG  
5521 C CG  B GLU   B 104 ? 0.3984 0.3464 0.3183 0.0213  -0.0035 0.0124  104 GLU   B CG  
5522 C CD  A GLU   B 104 ? 0.3772 0.3200 0.2872 0.0676  -0.0303 -0.0241 104 GLU   B CD  
5523 C CD  B GLU   B 104 ? 0.3894 0.3353 0.3040 0.0244  -0.0256 -0.0038 104 GLU   B CD  
5524 O OE1 A GLU   B 104 ? 0.3631 0.3026 0.2532 0.0795  -0.0307 -0.0401 104 GLU   B OE1 
5525 O OE1 B GLU   B 104 ? 0.3828 0.3263 0.2868 0.0258  -0.0277 -0.0111 104 GLU   B OE1 
5526 O OE2 A GLU   B 104 ? 0.3762 0.3230 0.2826 0.0685  -0.0535 -0.0314 104 GLU   B OE2 
5527 O OE2 B GLU   B 104 ? 0.3879 0.3352 0.2990 0.0252  -0.0408 -0.0100 104 GLU   B OE2 
5540 N N   A ASP   B 105 ? 0.4246 0.3709 0.3429 -0.0021 0.1326  0.0594  105 ASP   B N   
5541 N N   B ASP   B 105 ? 0.4130 0.3684 0.3512 -0.0001 0.0828  0.0472  105 ASP   B N   
5542 C CA  A ASP   B 105 ? 0.4262 0.3711 0.3559 -0.0107 0.1512  0.0454  105 ASP   B CA  
5543 C CA  B ASP   B 105 ? 0.4097 0.3665 0.3587 -0.0052 0.0927  0.0364  105 ASP   B CA  
5544 C C   A ASP   B 105 ? 0.4077 0.3435 0.3117 -0.0255 0.1687  0.0422  105 ASP   B C   
5545 C C   B ASP   B 105 ? 0.3988 0.3518 0.3292 -0.0130 0.1001  0.0272  105 ASP   B C   
5546 O O   A ASP   B 105 ? 0.3991 0.3353 0.2850 -0.0284 0.1848  0.0461  105 ASP   B O   
5547 O O   B ASP   B 105 ? 0.3957 0.3476 0.3120 -0.0137 0.1065  0.0262  105 ASP   B O   
5548 C CB  A ASP   B 105 ? 0.4429 0.3957 0.4224 -0.0018 0.1489  0.0273  105 ASP   B CB  
5549 C CB  B ASP   B 105 ? 0.4152 0.3779 0.3976 -0.0011 0.0939  0.0316  105 ASP   B CB  
5550 C CG  A ASP   B 105 ? 0.4566 0.4151 0.4870 0.0024  0.1515  0.0160  105 ASP   B CG  
5551 C CG  B ASP   B 105 ? 0.4201 0.3863 0.4364 -0.0003 0.0979  0.0314  105 ASP   B CG  
5552 O OD1 A ASP   B 105 ? 0.4574 0.4193 0.4961 -0.0029 0.1609  0.0182  105 ASP   B OD1 
5553 O OD1 B ASP   B 105 ? 0.4195 0.3894 0.4421 -0.0050 0.1021  0.0336  105 ASP   B OD1 
5554 O OD2 A ASP   B 105 ? 0.4636 0.4252 0.5214 0.0088  0.1455  0.0054  105 ASP   B OD2 
5555 O OD2 B ASP   B 105 ? 0.4213 0.3894 0.4506 0.0018  0.1004  0.0312  105 ASP   B OD2 
5564 N N   A ILE   B 106 ? 0.3970 0.3207 0.3112 -0.0345 0.1613  0.0382  106 ILE   B N   
5565 N N   B ILE   B 106 ? 0.3898 0.3392 0.3223 -0.0175 0.0954  0.0214  106 ILE   B N   
5566 C CA  A ILE   B 106 ? 0.3755 0.2945 0.3173 -0.0479 0.1654  0.0330  106 ILE   B CA  
5567 C CA  B ILE   B 106 ? 0.3759 0.3267 0.3231 -0.0228 0.0959  0.0139  106 ILE   B CA  
5568 C C   A ILE   B 106 ? 0.3431 0.2874 0.3040 -0.0395 0.1681  0.0166  106 ILE   B C   
5569 C C   B ILE   B 106 ? 0.3539 0.3223 0.3144 -0.0183 0.0968  0.0014  106 ILE   B C   
5570 O O   A ILE   B 106 ? 0.3344 0.2672 0.3024 -0.0414 0.1674  0.0128  106 ILE   B O   
5571 O O   B ILE   B 106 ? 0.3492 0.3133 0.3088 -0.0205 0.0946  -0.0046 106 ILE   B O   
5572 C CB  A ILE   B 106 ? 0.3908 0.2827 0.3444 -0.0617 0.1584  0.0384  106 ILE   B CB  
5573 C CB  B ILE   B 106 ? 0.3852 0.3225 0.3368 -0.0298 0.0936  0.0160  106 ILE   B CB  
5574 C CG1 A ILE   B 106 ? 0.3984 0.2809 0.3493 -0.0538 0.1476  0.0308  106 ILE   B CG1 
5575 C CG1 B ILE   B 106 ? 0.3896 0.3206 0.3397 -0.0256 0.0876  0.0139  106 ILE   B CG1 
5576 C CG2 A ILE   B 106 ? 0.3955 0.2822 0.3675 -0.0728 0.1608  0.0442  106 ILE   B CG2 
5577 C CG2 B ILE   B 106 ? 0.3885 0.3241 0.3495 -0.0352 0.0955  0.0176  106 ILE   B CG2 
5578 C CD1 A ILE   B 106 ? 0.4020 0.2812 0.3429 -0.0489 0.1440  0.0322  106 ILE   B CD1 
5579 C CD1 B ILE   B 106 ? 0.3919 0.3198 0.3390 -0.0228 0.0840  0.0153  106 ILE   B CD1 
5602 N N   A GLN   B 107 ? 0.3278 0.3068 0.3167 -0.0303 0.1567  0.0130  107 GLN   B N   
5603 N N   B GLN   B 107 ? 0.3398 0.3304 0.3245 -0.0126 0.0945  -0.0012 107 GLN   B N   
5604 C CA  A GLN   B 107 ? 0.3159 0.3280 0.3413 -0.0187 0.1289  0.0118  107 GLN   B CA  
5605 C CA  B GLN   B 107 ? 0.3277 0.3382 0.3415 -0.0050 0.0855  0.0011  107 GLN   B CA  
5606 C C   A GLN   B 107 ? 0.2842 0.3071 0.3056 -0.0041 0.1022  -0.0003 107 GLN   B C   
5607 C C   B GLN   B 107 ? 0.2935 0.3146 0.3035 0.0029  0.0824  -0.0030 107 GLN   B C   
5608 O O   A GLN   B 107 ? 0.2727 0.3092 0.3246 0.0025  0.0878  -0.0201 107 GLN   B O   
5609 O O   B GLN   B 107 ? 0.2889 0.3197 0.3150 0.0055  0.0726  -0.0162 107 GLN   B O   
5610 C CB  A GLN   B 107 ? 0.3485 0.3703 0.4227 -0.0148 0.1017  0.0147  107 GLN   B CB  
5611 C CB  B GLN   B 107 ? 0.3546 0.3688 0.4085 -0.0025 0.0688  0.0040  107 GLN   B CB  
5612 C CG  A GLN   B 107 ? 0.3798 0.4076 0.5011 -0.0073 0.0690  0.0171  107 GLN   B CG  
5613 C CG  B GLN   B 107 ? 0.3791 0.3956 0.4727 0.0020  0.0487  0.0069  107 GLN   B CG  
5614 C CD  A GLN   B 107 ? 0.4024 0.4359 0.5652 -0.0049 0.0462  0.0217  107 GLN   B CD  
5615 C CD  B GLN   B 107 ? 0.3974 0.4159 0.5258 0.0035  0.0338  0.0105  107 GLN   B CD  
5616 O OE1 A GLN   B 107 ? 0.4114 0.4471 0.5893 -0.0052 0.0421  0.0210  107 GLN   B OE1 
5617 O OE1 B GLN   B 107 ? 0.4047 0.4240 0.5448 0.0027  0.0315  0.0108  107 GLN   B OE1 
5618 N NE2 A GLN   B 107 ? 0.4104 0.4441 0.5859 -0.0007 0.0371  0.0265  107 GLN   B NE2 
5619 N NE2 B GLN   B 107 ? 0.4039 0.4217 0.5434 0.0067  0.0286  0.0135  107 GLN   B NE2 
5636 N N   . LEU   B 108 ? 0.2633 0.2868 0.2708 0.0139  0.0877  0.0035  108 LEU   B N   
5637 C CA  . LEU   B 108 ? 0.2419 0.2517 0.2332 0.0287  0.0643  0.0160  108 LEU   B CA  
5638 C C   . LEU   B 108 ? 0.2041 0.2056 0.2333 0.0258  0.0381  0.0302  108 LEU   B C   
5639 O O   . LEU   B 108 ? 0.2010 0.1946 0.2263 0.0218  0.0362  0.0254  108 LEU   B O   
5640 C CB  . LEU   B 108 ? 0.2602 0.2712 0.2181 0.0249  0.0646  0.0231  108 LEU   B CB  
5641 C CG  . LEU   B 108 ? 0.2778 0.2999 0.2284 0.0261  0.0625  0.0049  108 LEU   B CG  
5642 C CD1 . LEU   B 108 ? 0.2843 0.3120 0.2229 0.0194  0.0659  0.0049  108 LEU   B CD1 
5643 C CD2 . LEU   B 108 ? 0.2937 0.3139 0.2430 0.0347  0.0498  -0.0111 108 LEU   B CD2 
5656 N N   . LEU   B 109 ? 0.1863 0.1840 0.2354 0.0142  0.0390  0.0208  109 LEU   B N   
5657 C CA  . LEU   B 109 ? 0.1663 0.1508 0.2491 0.0077  0.0338  0.0300  109 LEU   B CA  
5658 C C   . LEU   B 109 ? 0.1572 0.1366 0.2447 0.0053  0.0320  0.0210  109 LEU   B C   
5659 O O   . LEU   B 109 ? 0.1574 0.1346 0.2287 0.0050  0.0242  0.0251  109 LEU   B O   
5660 C CB  . LEU   B 109 ? 0.1729 0.1441 0.2581 0.0048  0.0212  0.0336  109 LEU   B CB  
5661 C CG  . LEU   B 109 ? 0.1708 0.1409 0.2527 0.0031  0.0247  0.0208  109 LEU   B CG  
5662 C CD1 . LEU   B 109 ? 0.1646 0.1561 0.2363 0.0106  0.0233  0.0291  109 LEU   B CD1 
5663 C CD2 . LEU   B 109 ? 0.1833 0.1467 0.2644 0.0060  0.0185  0.0208  109 LEU   B CD2 
5675 N N   . LYS   B 110 ? 0.1550 0.1434 0.2315 -0.0015 0.0340  0.0183  110 LYS   B N   
5676 C CA  . LYS   B 110 ? 0.1507 0.1369 0.2396 0.0037  0.0213  0.0180  110 LYS   B CA  
5677 C C   . LYS   B 110 ? 0.1483 0.1421 0.2277 0.0015  0.0253  0.0129  110 LYS   B C   
5678 O O   . LYS   B 110 ? 0.1395 0.1443 0.2258 -0.0052 0.0168  0.0106  110 LYS   B O   
5679 C CB  . LYS   B 110 ? 0.1491 0.1404 0.2624 0.0008  0.0308  0.0140  110 LYS   B CB  
5680 C CG  . LYS   B 110 ? 0.1502 0.1414 0.2752 -0.0052 0.0108  0.0174  110 LYS   B CG  
5681 C CD  . LYS   B 110 ? 0.1517 0.1387 0.2758 -0.0028 0.0146  0.0192  110 LYS   B CD  
5682 C CE  . LYS   B 110 ? 0.1487 0.1602 0.2906 -0.0021 0.0122  0.0078  110 LYS   B CE  
5683 N NZ  . LYS   B 110 ? 0.1547 0.1707 0.2821 0.0055  0.0106  0.0054  110 LYS   B NZ  
5697 N N   . SER   B 111 ? 0.1539 0.1395 0.2342 -0.0003 0.0219  0.0126  111 SER   B N   
5698 C CA  . SER   B 111 ? 0.1575 0.1417 0.2191 0.0007  0.0146  0.0135  111 SER   B CA  
5699 C C   . SER   B 111 ? 0.1522 0.1378 0.2169 0.0008  0.0108  0.0037  111 SER   B C   
5700 O O   . SER   B 111 ? 0.1488 0.1425 0.2306 0.0009  0.0137  0.0065  111 SER   B O   
5701 C CB  . SER   B 111 ? 0.1676 0.1669 0.2289 0.0020  0.0304  0.0224  111 SER   B CB  
5702 O OG  . SER   B 111 ? 0.1881 0.2039 0.2333 0.0080  0.0357  0.0291  111 SER   B OG  
5708 N N   . ALA   B 112 ? 0.1450 0.1418 0.2213 0.0081  0.0193  0.0156  112 ALA   B N   
5709 C CA  . ALA   B 112 ? 0.1412 0.1431 0.1985 0.0020  0.0118  0.0035  112 ALA   B CA  
5710 C C   . ALA   B 112 ? 0.1337 0.1387 0.1915 -0.0003 0.0065  0.0045  112 ALA   B C   
5711 O O   . ALA   B 112 ? 0.1334 0.1364 0.2106 -0.0052 0.0092  0.0004  112 ALA   B O   
5712 C CB  . ALA   B 112 ? 0.1436 0.1506 0.2210 0.0061  0.0034  0.0172  112 ALA   B CB  
5718 N N   . TYR   B 113 ? 0.1341 0.1282 0.2091 0.0011  0.0071  0.0048  113 TYR   B N   
5719 C CA  . TYR   B 113 ? 0.1353 0.1271 0.1993 -0.0061 0.0096  -0.0041 113 TYR   B CA  
5720 C C   . TYR   B 113 ? 0.1319 0.1244 0.1957 -0.0066 0.0086  0.0107  113 TYR   B C   
5721 O O   . TYR   B 113 ? 0.1356 0.1269 0.1878 -0.0052 0.0009  0.0019  113 TYR   B O   
5722 C CB  . TYR   B 113 ? 0.1374 0.1244 0.2116 -0.0022 0.0096  0.0011  113 TYR   B CB  
5723 C CG  . TYR   B 113 ? 0.1363 0.1244 0.2304 -0.0042 0.0065  0.0053  113 TYR   B CG  
5724 C CD1 . TYR   B 113 ? 0.1459 0.1280 0.2383 -0.0070 0.0116  0.0178  113 TYR   B CD1 
5725 C CD2 . TYR   B 113 ? 0.1476 0.1243 0.2242 -0.0044 0.0042  0.0132  113 TYR   B CD2 
5726 C CE1 . TYR   B 113 ? 0.1481 0.1336 0.2245 -0.0044 0.0154  0.0068  113 TYR   B CE1 
5727 C CE2 . TYR   B 113 ? 0.1592 0.1252 0.2308 -0.0009 0.0100  0.0160  113 TYR   B CE2 
5728 C CZ  . TYR   B 113 ? 0.1426 0.1279 0.2397 0.0050  0.0113  0.0075  113 TYR   B CZ  
5729 O OH  . TYR   B 113 ? 0.1513 0.1254 0.2682 0.0081  0.0183  0.0112  113 TYR   B OH  
5739 N N   . GLU   B 114 ? 0.1254 0.1187 0.2127 -0.0028 0.0065  0.0098  114 GLU   B N   
5740 C CA  . GLU   B 114 ? 0.1258 0.1205 0.2166 0.0005  0.0014  0.0020  114 GLU   B CA  
5741 C C   . GLU   B 114 ? 0.1309 0.1264 0.2004 0.0024  0.0037  0.0034  114 GLU   B C   
5742 O O   . GLU   B 114 ? 0.1299 0.1295 0.2102 0.0017  -0.0043 0.0122  114 GLU   B O   
5743 C CB  . GLU   B 114 ? 0.1330 0.1242 0.2317 -0.0019 0.0075  0.0030  114 GLU   B CB  
5744 C CG  . GLU   B 114 ? 0.1380 0.1260 0.2385 -0.0037 0.0081  0.0104  114 GLU   B CG  
5745 C CD  . GLU   B 114 ? 0.1345 0.1317 0.2390 -0.0068 0.0037  0.0042  114 GLU   B CD  
5746 O OE1 . GLU   B 114 ? 0.1320 0.1490 0.2232 -0.0082 0.0134  0.0059  114 GLU   B OE1 
5747 O OE2 . GLU   B 114 ? 0.1330 0.1512 0.2500 -0.0182 0.0092  0.0059  114 GLU   B OE2 
5754 N N   . ASN   B 115 ? 0.1349 0.1220 0.1879 -0.0038 -0.0054 0.0095  115 ASN   B N   
5755 C CA  . ASN   B 115 ? 0.1365 0.1257 0.1814 -0.0101 -0.0039 0.0067  115 ASN   B CA  
5756 C C   . ASN   B 115 ? 0.1334 0.1237 0.1781 -0.0100 -0.0089 -0.0003 115 ASN   B C   
5757 O O   . ASN   B 115 ? 0.1392 0.1275 0.1925 -0.0104 -0.0029 0.0002  115 ASN   B O   
5758 C CB  . ASN   B 115 ? 0.1442 0.1385 0.1876 -0.0064 -0.0044 0.0074  115 ASN   B CB  
5759 C CG  . ASN   B 115 ? 0.1548 0.1429 0.1840 0.0015  -0.0048 0.0008  115 ASN   B CG  
5760 O OD1 . ASN   B 115 ? 0.1937 0.1544 0.2142 0.0007  0.0080  -0.0088 115 ASN   B OD1 
5761 N ND2 . ASN   B 115 ? 0.1521 0.1555 0.1764 -0.0038 0.0036  0.0026  115 ASN   B ND2 
5768 N N   . PHE   B 116 ? 0.1333 0.1288 0.1722 -0.0080 0.0003  0.0019  116 PHE   B N   
5769 C CA  . PHE   B 116 ? 0.1387 0.1251 0.1717 -0.0099 -0.0014 0.0029  116 PHE   B CA  
5770 C C   . PHE   B 116 ? 0.1371 0.1180 0.1749 -0.0104 -0.0058 0.0097  116 PHE   B C   
5771 O O   . PHE   B 116 ? 0.1411 0.1285 0.1802 -0.0019 -0.0077 0.0072  116 PHE   B O   
5772 C CB  . PHE   B 116 ? 0.1351 0.1236 0.1746 -0.0048 -0.0130 0.0077  116 PHE   B CB  
5773 C CG  . PHE   B 116 ? 0.1320 0.1254 0.1783 -0.0088 -0.0058 0.0016  116 PHE   B CG  
5774 C CD1 . PHE   B 116 ? 0.1366 0.1281 0.1921 -0.0025 0.0005  0.0056  116 PHE   B CD1 
5775 C CD2 . PHE   B 116 ? 0.1342 0.1325 0.1750 -0.0073 -0.0029 -0.0043 116 PHE   B CD2 
5776 C CE1 . PHE   B 116 ? 0.1416 0.1323 0.1969 -0.0070 -0.0122 0.0076  116 PHE   B CE1 
5777 C CE2 . PHE   B 116 ? 0.1380 0.1342 0.1859 -0.0031 0.0033  0.0020  116 PHE   B CE2 
5778 C CZ  . PHE   B 116 ? 0.1323 0.1362 0.1920 -0.0058 -0.0095 0.0100  116 PHE   B CZ  
5788 N N   . ASN   B 117 ? 0.1334 0.1248 0.1856 -0.0055 -0.0104 0.0062  117 ASN   B N   
5789 C CA  . ASN   B 117 ? 0.1404 0.1265 0.1936 0.0009  -0.0085 0.0013  117 ASN   B CA  
5790 C C   . ASN   B 117 ? 0.1440 0.1273 0.2166 0.0016  -0.0128 0.0096  117 ASN   B C   
5791 O O   . ASN   B 117 ? 0.1531 0.1332 0.2302 -0.0024 -0.0350 0.0088  117 ASN   B O   
5792 C CB  . ASN   B 117 ? 0.1405 0.1334 0.1942 -0.0015 -0.0050 0.0019  117 ASN   B CB  
5793 C CG  . ASN   B 117 ? 0.1351 0.1311 0.2002 0.0028  -0.0082 -0.0032 117 ASN   B CG  
5794 O OD1 . ASN   B 117 ? 0.1579 0.1311 0.2252 -0.0136 0.0026  -0.0051 117 ASN   B OD1 
5795 N ND2 . ASN   B 117 ? 0.1416 0.1360 0.2084 -0.0046 -0.0017 -0.0019 117 ASN   B ND2 
5802 N N   . GLN   B 118 ? 0.1418 0.1175 0.2091 -0.0041 -0.0158 0.0025  118 GLN   B N   
5803 C CA  . GLN   B 118 ? 0.1455 0.1277 0.2071 0.0036  -0.0184 0.0030  118 GLN   B CA  
5804 C C   . GLN   B 118 ? 0.1473 0.1253 0.2156 -0.0013 -0.0131 -0.0064 118 GLN   B C   
5805 O O   . GLN   B 118 ? 0.1701 0.1268 0.2495 -0.0044 -0.0057 0.0057  118 GLN   B O   
5806 C CB  . GLN   B 118 ? 0.1531 0.1318 0.2136 0.0013  -0.0152 0.0027  118 GLN   B CB  
5807 C CG  . GLN   B 118 ? 0.1613 0.1373 0.2111 0.0063  -0.0034 -0.0114 118 GLN   B CG  
5808 C CD  . GLN   B 118 ? 0.1650 0.1289 0.2129 0.0057  -0.0149 -0.0159 118 GLN   B CD  
5809 O OE1 . GLN   B 118 ? 0.1740 0.1300 0.2373 0.0056  0.0015  0.0017  118 GLN   B OE1 
5810 N NE2 . GLN   B 118 ? 0.1686 0.1353 0.2115 0.0028  -0.0167 0.0048  118 GLN   B NE2 
5819 N N   . HIS   B 119 ? 0.1526 0.1336 0.1839 -0.0033 -0.0124 0.0041  119 HIS   B N   
5820 C CA  . HIS   B 119 ? 0.1608 0.1405 0.1720 0.0030  -0.0171 0.0068  119 HIS   B CA  
5821 C C   . HIS   B 119 ? 0.1692 0.1418 0.1598 0.0028  -0.0322 0.0043  119 HIS   B C   
5822 O O   . HIS   B 119 ? 0.1759 0.1341 0.1898 -0.0227 -0.0194 0.0091  119 HIS   B O   
5823 C CB  . HIS   B 119 ? 0.1672 0.1571 0.1768 0.0019  -0.0199 -0.0009 119 HIS   B CB  
5824 C CG  . HIS   B 119 ? 0.1699 0.1795 0.1830 0.0096  -0.0416 -0.0145 119 HIS   B CG  
5825 N ND1 . HIS   B 119 ? 0.1790 0.1951 0.2188 0.0006  -0.0488 -0.0309 119 HIS   B ND1 
5826 C CD2 . HIS   B 119 ? 0.1845 0.1956 0.1940 0.0399  -0.0426 -0.0155 119 HIS   B CD2 
5827 C CE1 . HIS   B 119 ? 0.1977 0.2141 0.2237 0.0144  -0.0518 -0.0394 119 HIS   B CE1 
5828 N NE2 . HIS   B 119 ? 0.1986 0.2194 0.2168 0.0339  -0.0419 -0.0392 119 HIS   B NE2 
5836 N N   . GLU   B 120 ? 0.1858 0.1463 0.1546 -0.0067 -0.0372 0.0142  120 GLU   B N   
5837 C CA  . GLU   B 120 ? 0.2172 0.1583 0.1747 -0.0023 -0.0501 0.0280  120 GLU   B CA  
5838 C C   . GLU   B 120 ? 0.1937 0.1460 0.1683 -0.0141 -0.0408 0.0310  120 GLU   B C   
5839 O O   . GLU   B 120 ? 0.1827 0.1591 0.1872 -0.0186 -0.0361 0.0106  120 GLU   B O   
5840 C CB  . GLU   B 120 ? 0.2870 0.1943 0.2584 0.0184  -0.0804 0.0467  120 GLU   B CB  
5841 C CG  . GLU   B 120 ? 0.3474 0.2754 0.3625 0.0303  -0.1010 0.0639  120 GLU   B CG  
5842 C CD  . GLU   B 120 ? 0.4020 0.3564 0.4780 0.0336  -0.1072 0.0752  120 GLU   B CD  
5843 O OE1 . GLU   B 120 ? 0.4269 0.3884 0.5159 0.0285  -0.1039 0.0862  120 GLU   B OE1 
5844 O OE2 . GLU   B 120 ? 0.4180 0.3862 0.5327 0.0339  -0.1080 0.0682  120 GLU   B OE2 
5851 N N   . VAL   B 121 ? 0.1805 0.1376 0.1691 -0.0212 -0.0294 0.0210  121 VAL   B N   
5852 C CA  . VAL   B 121 ? 0.1739 0.1538 0.1519 -0.0214 -0.0266 0.0163  121 VAL   B CA  
5853 C C   . VAL   B 121 ? 0.1663 0.1461 0.1533 -0.0260 -0.0149 0.0143  121 VAL   B C   
5854 O O   . VAL   B 121 ? 0.1747 0.1430 0.1812 -0.0259 -0.0235 0.0077  121 VAL   B O   
5855 C CB  . VAL   B 121 ? 0.1934 0.1931 0.1588 -0.0111 -0.0288 0.0181  121 VAL   B CB  
5856 C CG1 . VAL   B 121 ? 0.2063 0.2089 0.1939 -0.0168 -0.0161 0.0162  121 VAL   B CG1 
5857 C CG2 . VAL   B 121 ? 0.2161 0.2166 0.1689 0.0010  -0.0214 0.0118  121 VAL   B CG2 
5867 N N   . LEU   B 122 ? 0.1593 0.1405 0.1495 -0.0183 -0.0249 0.0124  122 LEU   B N   
5868 C CA  . LEU   B 122 ? 0.1541 0.1456 0.1415 -0.0234 -0.0260 0.0089  122 LEU   B CA  
5869 C C   . LEU   B 122 ? 0.1484 0.1327 0.1542 -0.0277 -0.0138 0.0126  122 LEU   B C   
5870 O O   . LEU   B 122 ? 0.1590 0.1348 0.1850 -0.0314 -0.0239 0.0007  122 LEU   B O   
5871 C CB  . LEU   B 122 ? 0.1783 0.1540 0.1759 -0.0064 -0.0335 0.0170  122 LEU   B CB  
5872 C CG  . LEU   B 122 ? 0.1622 0.1611 0.1930 -0.0185 -0.0160 0.0128  122 LEU   B CG  
5873 C CD1 . LEU   B 122 ? 0.1669 0.1817 0.1932 -0.0247 -0.0192 0.0105  122 LEU   B CD1 
5874 C CD2 . LEU   B 122 ? 0.1664 0.1606 0.1634 -0.0145 -0.0173 0.0013  122 LEU   B CD2 
5886 N N   . LEU   B 123 ? 0.1498 0.1282 0.1418 -0.0228 -0.0169 0.0067  123 LEU   B N   
5887 C CA  . LEU   B 123 ? 0.1547 0.1321 0.1500 -0.0220 -0.0188 -0.0031 123 LEU   B CA  
5888 C C   . LEU   B 123 ? 0.1446 0.1291 0.1512 -0.0225 -0.0211 -0.0026 123 LEU   B C   
5889 O O   . LEU   B 123 ? 0.1545 0.1337 0.1597 -0.0292 -0.0133 -0.0001 123 LEU   B O   
5890 C CB  . LEU   B 123 ? 0.1656 0.1352 0.1645 -0.0224 -0.0144 -0.0032 123 LEU   B CB  
5891 C CG  . LEU   B 123 ? 0.1632 0.1396 0.1769 -0.0145 -0.0068 0.0091  123 LEU   B CG  
5892 C CD1 . LEU   B 123 ? 0.1700 0.1402 0.1782 -0.0137 -0.0059 -0.0057 123 LEU   B CD1 
5893 C CD2 . LEU   B 123 ? 0.1653 0.1515 0.1815 -0.0139 -0.0022 0.0172  123 LEU   B CD2 
5905 N N   . ALA   B 124 ? 0.1435 0.1291 0.1505 -0.0171 -0.0060 -0.0045 124 ALA   B N   
5906 C CA  . ALA   B 124 ? 0.1382 0.1316 0.1537 -0.0156 -0.0076 -0.0085 124 ALA   B CA  
5907 C C   . ALA   B 124 ? 0.1366 0.1306 0.1526 -0.0208 -0.0072 -0.0067 124 ALA   B C   
5908 O O   . ALA   B 124 ? 0.1447 0.1358 0.1692 -0.0092 -0.0168 -0.0033 124 ALA   B O   
5909 C CB  . ALA   B 124 ? 0.1488 0.1347 0.1587 -0.0099 -0.0025 -0.0002 124 ALA   B CB  
5915 N N   . PRO   B 125 ? 0.1447 0.1330 0.1532 -0.0184 -0.0105 0.0068  125 PRO   B N   
5916 C CA  . PRO   B 125 ? 0.1547 0.1303 0.1688 -0.0139 -0.0202 0.0154  125 PRO   B CA  
5917 C C   . PRO   B 125 ? 0.1459 0.1231 0.1893 -0.0109 -0.0148 0.0106  125 PRO   B C   
5918 O O   . PRO   B 125 ? 0.1523 0.1258 0.2059 -0.0078 -0.0096 0.0135  125 PRO   B O   
5919 C CB  . PRO   B 125 ? 0.1577 0.1554 0.1844 -0.0197 -0.0166 0.0297  125 PRO   B CB  
5920 C CG  . PRO   B 125 ? 0.1652 0.1620 0.1599 -0.0289 -0.0188 0.0192  125 PRO   B CG  
5921 C CD  . PRO   B 125 ? 0.1549 0.1453 0.1484 -0.0306 -0.0075 0.0078  125 PRO   B CD  
5929 N N   . LEU   B 126 ? 0.1525 0.1244 0.2083 -0.0133 0.0022  0.0183  126 LEU   B N   
5930 C CA  . LEU   B 126 ? 0.1598 0.1358 0.2059 -0.0117 0.0083  0.0178  126 LEU   B CA  
5931 C C   . LEU   B 126 ? 0.1509 0.1441 0.2075 -0.0038 0.0170  0.0213  126 LEU   B C   
5932 O O   . LEU   B 126 ? 0.1726 0.1705 0.2324 0.0190  -0.0058 -0.0035 126 LEU   B O   
5933 C CB  . LEU   B 126 ? 0.1770 0.1401 0.2354 -0.0133 0.0194  0.0126  126 LEU   B CB  
5934 C CG  . LEU   B 126 ? 0.1926 0.1470 0.2530 -0.0226 0.0174  -0.0064 126 LEU   B CG  
5935 C CD1 . LEU   B 126 ? 0.2062 0.1548 0.2979 -0.0244 0.0085  -0.0185 126 LEU   B CD1 
5936 C CD2 . LEU   B 126 ? 0.1950 0.1559 0.2520 -0.0282 0.0052  -0.0128 126 LEU   B CD2 
5948 N N   . LEU   B 127 ? 0.1521 0.1328 0.2254 0.0025  0.0185  0.0130  127 LEU   B N   
5949 C CA  . LEU   B 127 ? 0.1497 0.1410 0.2262 -0.0050 0.0207  0.0197  127 LEU   B CA  
5950 C C   . LEU   B 127 ? 0.1471 0.1360 0.2359 0.0005  0.0127  0.0235  127 LEU   B C   
5951 O O   . LEU   B 127 ? 0.1502 0.1378 0.2366 -0.0132 0.0094  0.0173  127 LEU   B O   
5952 C CB  . LEU   B 127 ? 0.1642 0.1379 0.2358 -0.0028 0.0167  0.0204  127 LEU   B CB  
5953 C CG  . LEU   B 127 ? 0.1723 0.1370 0.2429 0.0026  0.0210  0.0151  127 LEU   B CG  
5954 C CD1 . LEU   B 127 ? 0.1799 0.1391 0.2422 0.0043  0.0109  0.0134  127 LEU   B CD1 
5955 C CD2 . LEU   B 127 ? 0.1721 0.1457 0.2568 -0.0089 0.0210  0.0238  127 LEU   B CD2 
5967 N N   . SER   B 128 ? 0.1534 0.1382 0.2324 -0.0023 0.0000  0.0204  128 SER   B N   
5968 C CA  . SER   B 128 ? 0.1614 0.1420 0.2287 0.0106  -0.0125 0.0256  128 SER   B CA  
5969 C C   . SER   B 128 ? 0.1734 0.1524 0.2507 0.0066  -0.0229 0.0230  128 SER   B C   
5970 O O   . SER   B 128 ? 0.1855 0.1561 0.2877 0.0053  -0.0216 0.0336  128 SER   B O   
5971 C CB  . SER   B 128 ? 0.1723 0.1437 0.2246 0.0072  0.0024  0.0357  128 SER   B CB  
5972 O OG  . SER   B 128 ? 0.1781 0.1598 0.2175 0.0085  0.0041  0.0352  128 SER   B OG  
5978 N N   . ALA   B 129 ? 0.1893 0.1558 0.2744 0.0295  -0.0076 0.0063  129 ALA   B N   
5979 C CA  . ALA   B 129 ? 0.2061 0.1623 0.2803 0.0310  -0.0080 -0.0028 129 ALA   B CA  
5980 C C   . ALA   B 129 ? 0.1913 0.1546 0.2711 0.0217  0.0042  0.0028  129 ALA   B C   
5981 O O   . ALA   B 129 ? 0.1784 0.1588 0.2755 0.0183  0.0000  0.0075  129 ALA   B O   
5982 C CB  . ALA   B 129 ? 0.2281 0.1877 0.3114 0.0356  0.0047  -0.0075 129 ALA   B CB  
5988 N N   . GLY   B 130 ? 0.1857 0.1538 0.2787 0.0244  0.0037  0.0013  130 GLY   B N   
5989 C CA  . GLY   B 130 ? 0.1910 0.1610 0.2888 0.0198  0.0183  0.0053  130 GLY   B CA  
5990 C C   . GLY   B 130 ? 0.1953 0.1691 0.2825 0.0170  0.0129  0.0103  130 GLY   B C   
5991 O O   . GLY   B 130 ? 0.2100 0.1824 0.2899 0.0193  0.0083  0.0159  130 GLY   B O   
5995 N N   . ILE   B 131 ? 0.1908 0.1822 0.2855 0.0312  0.0115  0.0085  131 ILE   B N   
5996 C CA  . ILE   B 131 ? 0.2118 0.1920 0.2834 0.0325  -0.0027 0.0207  131 ILE   B CA  
5997 C C   . ILE   B 131 ? 0.2237 0.1811 0.2431 0.0226  0.0020  0.0203  131 ILE   B C   
5998 O O   . ILE   B 131 ? 0.2536 0.2037 0.2612 0.0219  -0.0111 0.0249  131 ILE   B O   
5999 C CB  . ILE   B 131 ? 0.2115 0.2271 0.3289 0.0307  -0.0181 0.0274  131 ILE   B CB  
6000 C CG1 . ILE   B 131 ? 0.2188 0.2501 0.3648 0.0022  -0.0180 0.0220  131 ILE   B CG1 
6001 C CG2 . ILE   B 131 ? 0.2133 0.2488 0.3488 0.0395  -0.0177 0.0244  131 ILE   B CG2 
6002 C CD1 . ILE   B 131 ? 0.2263 0.2694 0.3872 -0.0141 -0.0214 0.0231  131 ILE   B CD1 
6014 N N   . PHE   B 132 ? 0.2071 0.1633 0.2274 0.0140  0.0153  0.0173  132 PHE   B N   
6015 C CA  . PHE   B 132 ? 0.2211 0.1666 0.2313 0.0075  0.0291  0.0142  132 PHE   B CA  
6016 C C   . PHE   B 132 ? 0.2381 0.1770 0.2482 0.0072  0.0333  0.0162  132 PHE   B C   
6017 O O   . PHE   B 132 ? 0.2546 0.2009 0.2694 0.0050  0.0473  0.0199  132 PHE   B O   
6018 C CB  . PHE   B 132 ? 0.2084 0.1682 0.2198 0.0089  0.0305  0.0214  132 PHE   B CB  
6019 C CG  . PHE   B 132 ? 0.2027 0.1701 0.2178 0.0139  0.0217  0.0235  132 PHE   B CG  
6020 C CD1 . PHE   B 132 ? 0.2068 0.1666 0.2514 0.0142  0.0237  0.0247  132 PHE   B CD1 
6021 C CD2 . PHE   B 132 ? 0.2021 0.1716 0.2041 0.0240  0.0160  0.0273  132 PHE   B CD2 
6022 C CE1 . PHE   B 132 ? 0.2171 0.1745 0.2604 0.0061  0.0188  0.0215  132 PHE   B CE1 
6023 C CE2 . PHE   B 132 ? 0.2074 0.1777 0.2120 0.0194  0.0079  0.0246  132 PHE   B CE2 
6024 C CZ  . PHE   B 132 ? 0.2144 0.1793 0.2413 0.0117  0.0032  0.0319  132 PHE   B CZ  
6034 N N   . GLY   B 133 ? 0.2343 0.1715 0.2537 -0.0009 0.0199  0.0362  133 GLY   B N   
6035 C CA  . GLY   B 133 ? 0.2449 0.1869 0.2663 -0.0226 0.0200  0.0459  133 GLY   B CA  
6036 C C   . GLY   B 133 ? 0.2507 0.1946 0.2704 -0.0328 0.0282  0.0516  133 GLY   B C   
6037 O O   . GLY   B 133 ? 0.2712 0.2060 0.3112 -0.0430 0.0266  0.0672  133 GLY   B O   
6041 N N   . ALA   B 134 ? 0.2305 0.1951 0.2487 -0.0308 0.0329  0.0386  134 ALA   B N   
6042 C CA  . ALA   B 134 ? 0.2261 0.1895 0.2519 -0.0223 0.0358  0.0215  134 ALA   B CA  
6043 C C   . ALA   B 134 ? 0.2358 0.1834 0.2497 -0.0140 0.0309  0.0261  134 ALA   B C   
6044 O O   . ALA   B 134 ? 0.2441 0.1997 0.2634 -0.0011 0.0246  0.0217  134 ALA   B O   
6045 C CB  . ALA   B 134 ? 0.2263 0.1891 0.2711 -0.0119 0.0303  0.0096  134 ALA   B CB  
6051 N N   . ASP   B 135 ? 0.2451 0.1755 0.2531 -0.0166 0.0181  0.0286  135 ASP   B N   
6052 C CA  . ASP   B 135 ? 0.2589 0.1698 0.2760 -0.0150 0.0097  0.0296  135 ASP   B CA  
6053 C C   . ASP   B 135 ? 0.2393 0.1595 0.2618 -0.0055 0.0037  0.0265  135 ASP   B C   
6054 O O   . ASP   B 135 ? 0.2293 0.1556 0.2694 -0.0057 0.0038  0.0266  135 ASP   B O   
6055 C CB  . ASP   B 135 ? 0.2898 0.1838 0.3135 -0.0375 0.0113  0.0325  135 ASP   B CB  
6056 C CG  . ASP   B 135 ? 0.3192 0.1835 0.3574 -0.0604 0.0138  0.0286  135 ASP   B CG  
6057 O OD1 . ASP   B 135 ? 0.3272 0.1647 0.3489 -0.0420 0.0051  0.0268  135 ASP   B OD1 
6058 O OD2 . ASP   B 135 ? 0.3404 0.2166 0.4071 -0.0786 0.0159  0.0075  135 ASP   B OD2 
6063 N N   . PRO   B 136 ? 0.2321 0.1592 0.2732 0.0139  -0.0124 0.0232  136 PRO   B N   
6064 C CA  . PRO   B 136 ? 0.2096 0.1519 0.2715 0.0142  -0.0118 0.0129  136 PRO   B CA  
6065 C C   . PRO   B 136 ? 0.1846 0.1361 0.2846 0.0162  -0.0061 0.0060  136 PRO   B C   
6066 O O   . PRO   B 136 ? 0.1678 0.1391 0.2693 0.0091  0.0052  0.0115  136 PRO   B O   
6067 C CB  . PRO   B 136 ? 0.2190 0.1699 0.2752 0.0280  -0.0104 0.0001  136 PRO   B CB  
6068 C CG  . PRO   B 136 ? 0.2416 0.1767 0.2933 0.0336  -0.0088 -0.0008 136 PRO   B CG  
6069 C CD  . PRO   B 136 ? 0.2429 0.1724 0.2833 0.0356  -0.0075 0.0061  136 PRO   B CD  
6077 N N   . ILE   B 137 ? 0.1940 0.1323 0.2999 0.0145  -0.0115 -0.0006 137 ILE   B N   
6078 C CA  . ILE   B 137 ? 0.2076 0.1310 0.3217 0.0026  -0.0074 -0.0037 137 ILE   B CA  
6079 C C   . ILE   B 137 ? 0.1958 0.1335 0.3068 -0.0054 0.0101  0.0075  137 ILE   B C   
6080 O O   . ILE   B 137 ? 0.1890 0.1358 0.2945 -0.0095 0.0085  0.0069  137 ILE   B O   
6081 C CB  . ILE   B 137 ? 0.2292 0.1358 0.3796 -0.0031 -0.0072 -0.0018 137 ILE   B CB  
6082 C CG1 . ILE   B 137 ? 0.2552 0.1578 0.4304 0.0055  -0.0000 -0.0137 137 ILE   B CG1 
6083 C CG2 . ILE   B 137 ? 0.2309 0.1362 0.3924 -0.0314 -0.0041 -0.0008 137 ILE   B CG2 
6084 C CD1 . ILE   B 137 ? 0.2761 0.1840 0.4730 0.0196  -0.0018 -0.0104 137 ILE   B CD1 
6096 N N   . HIS   B 138 ? 0.2029 0.1347 0.3003 -0.0042 0.0241  0.0149  138 HIS   B N   
6097 C CA  . HIS   B 138 ? 0.2067 0.1442 0.2860 -0.0043 0.0347  0.0158  138 HIS   B CA  
6098 C C   . HIS   B 138 ? 0.1892 0.1422 0.2775 -0.0051 0.0287  0.0188  138 HIS   B C   
6099 O O   . HIS   B 138 ? 0.1821 0.1493 0.2954 0.0018  0.0324  0.0281  138 HIS   B O   
6100 C CB  . HIS   B 138 ? 0.2298 0.1615 0.2889 -0.0092 0.0559  0.0079  138 HIS   B CB  
6101 C CG  . HIS   B 138 ? 0.2510 0.1829 0.2890 -0.0131 0.0648  0.0338  138 HIS   B CG  
6102 N ND1 . HIS   B 138 ? 0.2607 0.1996 0.3167 -0.0099 0.0738  0.0276  138 HIS   B ND1 
6103 C CD2 . HIS   B 138 ? 0.2669 0.1960 0.2828 -0.0100 0.0647  0.0303  138 HIS   B CD2 
6104 C CE1 . HIS   B 138 ? 0.2666 0.2014 0.3053 -0.0045 0.0798  0.0323  138 HIS   B CE1 
6105 N NE2 . HIS   B 138 ? 0.2737 0.1966 0.2842 -0.0007 0.0746  0.0238  138 HIS   B NE2 
6113 N N   . SER   B 139 ? 0.1833 0.1287 0.2735 0.0063  0.0200  0.0128  139 SER   B N   
6114 C CA  . SER   B 139 ? 0.1829 0.1283 0.2507 0.0009  0.0193  0.0068  139 SER   B CA  
6115 C C   . SER   B 139 ? 0.1603 0.1257 0.2437 -0.0035 0.0135  0.0081  139 SER   B C   
6116 O O   . SER   B 139 ? 0.1589 0.1251 0.2518 -0.0009 0.0049  0.0103  139 SER   B O   
6117 C CB  . SER   B 139 ? 0.1876 0.1287 0.2606 0.0022  0.0040  0.0074  139 SER   B CB  
6118 O OG  . SER   B 139 ? 0.1838 0.1300 0.2624 -0.0009 -0.0069 0.0165  139 SER   B OG  
6124 N N   . LEU   B 140 ? 0.1599 0.1221 0.2339 -0.0075 0.0141  -0.0013 140 LEU   B N   
6125 C CA  . LEU   B 140 ? 0.1553 0.1232 0.2481 -0.0042 0.0099  0.0019  140 LEU   B CA  
6126 C C   . LEU   B 140 ? 0.1552 0.1249 0.2602 -0.0071 0.0039  -0.0061 140 LEU   B C   
6127 O O   . LEU   B 140 ? 0.1539 0.1332 0.2605 -0.0031 0.0041  0.0093  140 LEU   B O   
6128 C CB  . LEU   B 140 ? 0.1534 0.1205 0.2486 -0.0112 0.0143  -0.0117 140 LEU   B CB  
6129 C CG  . LEU   B 140 ? 0.1655 0.1248 0.2461 -0.0116 0.0033  0.0001  140 LEU   B CG  
6130 C CD1 . LEU   B 140 ? 0.1785 0.1336 0.2625 -0.0096 0.0105  0.0066  140 LEU   B CD1 
6131 C CD2 . LEU   B 140 ? 0.1839 0.1331 0.2706 -0.0125 -0.0062 -0.0056 140 LEU   B CD2 
6143 N N   . ARG   B 141 ? 0.1471 0.1266 0.2797 -0.0104 0.0060  -0.0027 141 ARG   B N   
6144 C CA  . ARG   B 141 ? 0.1493 0.1283 0.3110 -0.0130 0.0227  0.0014  141 ARG   B CA  
6145 C C   . ARG   B 141 ? 0.1467 0.1287 0.2999 -0.0134 0.0119  -0.0063 141 ARG   B C   
6146 O O   . ARG   B 141 ? 0.1514 0.1278 0.2980 -0.0138 -0.0019 -0.0088 141 ARG   B O   
6147 C CB  . ARG   B 141 ? 0.1656 0.1375 0.3295 -0.0196 0.0343  -0.0001 141 ARG   B CB  
6148 C CG  . ARG   B 141 ? 0.1991 0.1687 0.3472 -0.0221 0.0430  0.0039  141 ARG   B CG  
6149 C CD  . ARG   B 141 ? 0.2446 0.1943 0.3535 -0.0175 0.0362  -0.0102 141 ARG   B CD  
6150 N NE  . ARG   B 141 ? 0.2697 0.1940 0.3504 -0.0350 0.0466  -0.0208 141 ARG   B NE  
6151 C CZ  . ARG   B 141 ? 0.2878 0.1809 0.3338 -0.0281 0.0552  -0.0327 141 ARG   B CZ  
6152 N NH1 . ARG   B 141 ? 0.2963 0.1663 0.3309 -0.0297 0.0492  -0.0355 141 ARG   B NH1 
6153 N NH2 . ARG   B 141 ? 0.2985 0.1928 0.3462 -0.0155 0.0455  -0.0172 141 ARG   B NH2 
6167 N N   . VAL   B 142 ? 0.1552 0.1280 0.2845 -0.0109 0.0113  -0.0080 142 VAL   B N   
6168 C CA  . VAL   B 142 ? 0.1527 0.1232 0.2750 -0.0077 0.0142  -0.0037 142 VAL   B CA  
6169 C C   . VAL   B 142 ? 0.1492 0.1252 0.2726 -0.0069 0.0043  -0.0022 142 VAL   B C   
6170 O O   . VAL   B 142 ? 0.1523 0.1251 0.2862 -0.0037 0.0122  0.0008  142 VAL   B O   
6171 C CB  . VAL   B 142 ? 0.1633 0.1356 0.2720 -0.0022 0.0195  0.0149  142 VAL   B CB  
6172 C CG1 . VAL   B 142 ? 0.1600 0.1375 0.2701 0.0077  0.0210  0.0049  142 VAL   B CG1 
6173 C CG2 . VAL   B 142 ? 0.1845 0.1397 0.2799 -0.0011 0.0157  0.0116  142 VAL   B CG2 
6183 N N   . CYS   B 143 ? 0.1426 0.1269 0.2543 0.0003  0.0027  0.0033  143 CYS   B N   
6184 C CA  . CYS   B 143 ? 0.1357 0.1287 0.2614 -0.0044 0.0017  -0.0006 143 CYS   B CA  
6185 C C   . CYS   B 143 ? 0.1345 0.1274 0.2577 -0.0091 0.0083  0.0033  143 CYS   B C   
6186 O O   . CYS   B 143 ? 0.1441 0.1312 0.2486 -0.0061 0.0014  0.0002  143 CYS   B O   
6187 C CB  . CYS   B 143 ? 0.1447 0.1350 0.2584 -0.0119 -0.0008 -0.0004 143 CYS   B CB  
6188 S SG  . CYS   B 143 ? 0.1480 0.1455 0.2657 -0.0047 0.0036  0.0048  143 CYS   B SG  
6194 N N   . VAL   B 144 ? 0.1404 0.1266 0.2706 -0.0096 0.0038  -0.0072 144 VAL   B N   
6195 C CA  . VAL   B 144 ? 0.1489 0.1399 0.2947 -0.0135 -0.0141 -0.0178 144 VAL   B CA  
6196 C C   . VAL   B 144 ? 0.1459 0.1442 0.2982 -0.0123 -0.0182 0.0012  144 VAL   B C   
6197 O O   . VAL   B 144 ? 0.1569 0.1651 0.3110 -0.0033 -0.0154 0.0190  144 VAL   B O   
6198 C CB  . VAL   B 144 ? 0.1733 0.1531 0.3519 -0.0098 -0.0227 -0.0311 144 VAL   B CB  
6199 C CG1 . VAL   B 144 ? 0.1987 0.1963 0.3854 -0.0066 -0.0270 -0.0282 144 VAL   B CG1 
6200 C CG2 . VAL   B 144 ? 0.1892 0.1517 0.3382 0.0051  -0.0332 -0.0422 144 VAL   B CG2 
6210 N N   . ASP   B 145 ? 0.1460 0.1359 0.3160 -0.0044 -0.0093 -0.0186 145 ASP   B N   
6211 C CA  . ASP   B 145 ? 0.1464 0.1425 0.3367 -0.0091 -0.0008 -0.0102 145 ASP   B CA  
6212 C C   . ASP   B 145 ? 0.1404 0.1416 0.3195 -0.0062 0.0006  -0.0041 145 ASP   B C   
6213 O O   . ASP   B 145 ? 0.1428 0.1559 0.3739 -0.0128 0.0080  -0.0192 145 ASP   B O   
6214 C CB  . ASP   B 145 ? 0.1521 0.1512 0.3820 -0.0208 0.0086  -0.0077 145 ASP   B CB  
6215 C CG  . ASP   B 145 ? 0.1674 0.1459 0.4274 -0.0297 0.0252  -0.0141 145 ASP   B CG  
6216 O OD1 . ASP   B 145 ? 0.1748 0.1523 0.4329 -0.0230 -0.0070 -0.0239 145 ASP   B OD1 
6217 O OD2 . ASP   B 145 ? 0.1964 0.1566 0.4637 -0.0312 0.0562  -0.0033 145 ASP   B OD2 
6222 N N   . THR   B 146 ? 0.1349 0.1337 0.2721 -0.0076 -0.0031 0.0059  146 THR   B N   
6223 C CA  . THR   B 146 ? 0.1431 0.1307 0.2512 -0.0052 0.0013  -0.0052 146 THR   B CA  
6224 C C   . THR   B 146 ? 0.1440 0.1265 0.2448 -0.0085 -0.0050 0.0029  146 THR   B C   
6225 O O   . THR   B 146 ? 0.1471 0.1299 0.2552 -0.0044 -0.0055 0.0024  146 THR   B O   
6226 C CB  . THR   B 146 ? 0.1501 0.1269 0.2498 -0.0044 0.0186  -0.0025 146 THR   B CB  
6227 O OG1 . THR   B 146 ? 0.1528 0.1282 0.2643 -0.0055 0.0194  0.0107  146 THR   B OG1 
6228 C CG2 . THR   B 146 ? 0.1545 0.1360 0.2551 -0.0038 0.0136  -0.0052 146 THR   B CG2 
6236 N N   . VAL   B 147 ? 0.1492 0.1307 0.2352 -0.0052 0.0052  0.0050  147 VAL   B N   
6237 C CA  . VAL   B 147 ? 0.1505 0.1268 0.2304 -0.0104 -0.0084 0.0037  147 VAL   B CA  
6238 C C   . VAL   B 147 ? 0.1447 0.1262 0.2318 -0.0185 -0.0056 -0.0042 147 VAL   B C   
6239 O O   . VAL   B 147 ? 0.1547 0.1388 0.2390 -0.0201 -0.0219 -0.0090 147 VAL   B O   
6240 C CB  . VAL   B 147 ? 0.1486 0.1398 0.2155 -0.0128 -0.0117 0.0040  147 VAL   B CB  
6241 C CG1 . VAL   B 147 ? 0.1457 0.1548 0.2032 -0.0108 -0.0105 0.0046  147 VAL   B CG1 
6242 C CG2 . VAL   B 147 ? 0.1525 0.1395 0.2214 -0.0131 -0.0013 0.0016  147 VAL   B CG2 
6252 N N   . ARG   B 148 ? 0.1448 0.1261 0.2305 -0.0142 -0.0194 -0.0071 148 ARG   B N   
6253 C CA  . ARG   B 148 ? 0.1506 0.1394 0.2240 -0.0078 -0.0290 -0.0101 148 ARG   B CA  
6254 C C   . ARG   B 148 ? 0.1536 0.1484 0.2110 -0.0112 -0.0322 -0.0037 148 ARG   B C   
6255 O O   . ARG   B 148 ? 0.1753 0.1829 0.2255 -0.0278 -0.0405 0.0032  148 ARG   B O   
6256 C CB  . ARG   B 148 ? 0.1526 0.1496 0.2229 0.0002  -0.0343 -0.0147 148 ARG   B CB  
6257 C CG  . ARG   B 148 ? 0.1569 0.1652 0.2356 -0.0069 -0.0272 -0.0270 148 ARG   B CG  
6258 C CD  . ARG   B 148 ? 0.1630 0.1790 0.2432 0.0079  -0.0332 -0.0311 148 ARG   B CD  
6259 N NE  . ARG   B 148 ? 0.1664 0.1778 0.2319 0.0211  -0.0356 -0.0266 148 ARG   B NE  
6260 C CZ  . ARG   B 148 ? 0.1567 0.1713 0.2195 0.0100  -0.0301 -0.0163 148 ARG   B CZ  
6261 N NH1 . ARG   B 148 ? 0.1524 0.1768 0.2355 -0.0027 -0.0086 -0.0169 148 ARG   B NH1 
6262 N NH2 . ARG   B 148 ? 0.1755 0.1525 0.2165 0.0144  -0.0207 -0.0098 148 ARG   B NH2 
6276 N N   . THR   B 149 ? 0.1566 0.1420 0.2075 -0.0110 -0.0285 -0.0034 149 THR   B N   
6277 C CA  . THR   B 149 ? 0.1660 0.1506 0.2009 -0.0177 -0.0299 0.0013  149 THR   B CA  
6278 C C   . THR   B 149 ? 0.1656 0.1438 0.1892 -0.0133 -0.0336 -0.0023 149 THR   B C   
6279 O O   . THR   B 149 ? 0.1702 0.1410 0.2010 -0.0179 -0.0172 -0.0008 149 THR   B O   
6280 C CB  . THR   B 149 ? 0.1689 0.1466 0.1994 -0.0170 -0.0279 0.0063  149 THR   B CB  
6281 O OG1 . THR   B 149 ? 0.1663 0.1513 0.1981 -0.0251 -0.0335 0.0024  149 THR   B OG1 
6282 C CG2 . THR   B 149 ? 0.1755 0.1431 0.2237 -0.0081 -0.0277 0.0057  149 THR   B CG2 
6290 N N   . ASN   B 150 ? 0.1724 0.1443 0.1892 -0.0159 -0.0361 -0.0008 150 ASN   B N   
6291 C CA  . ASN   B 150 ? 0.1804 0.1645 0.1810 -0.0190 -0.0369 -0.0035 150 ASN   B CA  
6292 C C   . ASN   B 150 ? 0.1724 0.1501 0.1924 -0.0211 -0.0270 -0.0003 150 ASN   B C   
6293 O O   . ASN   B 150 ? 0.1753 0.1422 0.2058 -0.0281 -0.0361 -0.0023 150 ASN   B O   
6294 C CB  . ASN   B 150 ? 0.2051 0.1997 0.1918 -0.0187 -0.0426 0.0080  150 ASN   B CB  
6295 C CG  . ASN   B 150 ? 0.2296 0.2357 0.2284 -0.0218 -0.0409 0.0265  150 ASN   B CG  
6296 O OD1 . ASN   B 150 ? 0.2327 0.2497 0.2468 -0.0299 -0.0559 0.0156  150 ASN   B OD1 
6297 N ND2 . ASN   B 150 ? 0.2355 0.2531 0.2572 -0.0117 -0.0426 0.0687  150 ASN   B ND2 
6304 N N   . VAL   B 151 ? 0.1603 0.1456 0.1861 -0.0190 -0.0316 0.0017  151 VAL   B N   
6305 C CA  . VAL   B 151 ? 0.1621 0.1493 0.1852 -0.0210 -0.0271 -0.0074 151 VAL   B CA  
6306 C C   . VAL   B 151 ? 0.1615 0.1422 0.1736 -0.0268 -0.0230 -0.0008 151 VAL   B C   
6307 O O   . VAL   B 151 ? 0.1732 0.1508 0.2028 -0.0284 -0.0173 -0.0073 151 VAL   B O   
6308 C CB  . VAL   B 151 ? 0.1821 0.1621 0.2010 -0.0081 -0.0203 -0.0038 151 VAL   B CB  
6309 C CG1 . VAL   B 151 ? 0.1921 0.1680 0.2253 -0.0161 -0.0042 -0.0091 151 VAL   B CG1 
6310 C CG2 . VAL   B 151 ? 0.1903 0.1811 0.1916 0.0068  -0.0225 0.0046  151 VAL   B CG2 
6320 N N   . TYR   B 152 ? 0.1552 0.1321 0.1740 -0.0221 -0.0237 -0.0005 152 TYR   B N   
6321 C CA  . TYR   B 152 ? 0.1607 0.1486 0.1543 -0.0275 -0.0170 -0.0078 152 TYR   B CA  
6322 C C   . TYR   B 152 ? 0.1593 0.1356 0.1581 -0.0210 -0.0163 -0.0106 152 TYR   B C   
6323 O O   . TYR   B 152 ? 0.1662 0.1353 0.1759 -0.0219 -0.0102 -0.0048 152 TYR   B O   
6324 C CB  . TYR   B 152 ? 0.1728 0.1627 0.1571 -0.0293 -0.0107 0.0059  152 TYR   B CB  
6325 C CG  . TYR   B 152 ? 0.1879 0.1728 0.1550 -0.0412 -0.0091 0.0063  152 TYR   B CG  
6326 C CD1 . TYR   B 152 ? 0.1980 0.1829 0.1565 -0.0344 -0.0223 0.0057  152 TYR   B CD1 
6327 C CD2 . TYR   B 152 ? 0.2126 0.1941 0.1580 -0.0394 -0.0102 -0.0065 152 TYR   B CD2 
6328 C CE1 . TYR   B 152 ? 0.2157 0.2034 0.1686 -0.0337 -0.0262 0.0158  152 TYR   B CE1 
6329 C CE2 . TYR   B 152 ? 0.2225 0.2141 0.1706 -0.0379 -0.0180 -0.0051 152 TYR   B CE2 
6330 C CZ  . TYR   B 152 ? 0.2270 0.2262 0.1652 -0.0355 -0.0424 0.0154  152 TYR   B CZ  
6331 O OH  . TYR   B 152 ? 0.2553 0.2622 0.2026 -0.0245 -0.0477 0.0278  152 TYR   B OH  
6341 N N   . LEU   B 153 ? 0.1632 0.1349 0.1618 -0.0245 -0.0179 -0.0027 153 LEU   B N   
6342 C CA  . LEU   B 153 ? 0.1642 0.1347 0.1608 -0.0189 -0.0142 -0.0076 153 LEU   B CA  
6343 C C   . LEU   B 153 ? 0.1630 0.1282 0.1747 -0.0253 -0.0112 -0.0154 153 LEU   B C   
6344 O O   . LEU   B 153 ? 0.1797 0.1469 0.1778 -0.0171 -0.0173 -0.0284 153 LEU   B O   
6345 C CB  . LEU   B 153 ? 0.1652 0.1325 0.1767 -0.0248 -0.0105 -0.0048 153 LEU   B CB  
6346 C CG  . LEU   B 153 ? 0.1623 0.1436 0.2038 -0.0240 -0.0028 -0.0031 153 LEU   B CG  
6347 C CD1 . LEU   B 153 ? 0.1637 0.1522 0.2246 -0.0279 -0.0019 0.0073  153 LEU   B CD1 
6348 C CD2 . LEU   B 153 ? 0.1631 0.1578 0.1987 -0.0268 0.0061  0.0058  153 LEU   B CD2 
6360 N N   . ALA   B 154 ? 0.1575 0.1320 0.1924 -0.0114 -0.0160 -0.0093 154 ALA   B N   
6361 C CA  . ALA   B 154 ? 0.1625 0.1467 0.2131 -0.0044 -0.0160 -0.0150 154 ALA   B CA  
6362 C C   . ALA   B 154 ? 0.1739 0.1489 0.2085 0.0008  -0.0225 -0.0243 154 ALA   B C   
6363 O O   . ALA   B 154 ? 0.2127 0.1485 0.2257 0.0053  -0.0131 -0.0110 154 ALA   B O   
6364 C CB  . ALA   B 154 ? 0.1604 0.1645 0.2407 -0.0086 -0.0050 -0.0227 154 ALA   B CB  
6370 N N   . VAL   B 155 ? 0.1478 0.1396 0.2219 0.0005  0.0024  -0.0184 155 VAL   B N   
6371 C CA  . VAL   B 155 ? 0.1455 0.1404 0.2472 -0.0007 -0.0074 -0.0096 155 VAL   B CA  
6372 C C   . VAL   B 155 ? 0.1473 0.1394 0.2231 -0.0045 -0.0147 -0.0196 155 VAL   B C   
6373 O O   . VAL   B 155 ? 0.1649 0.1593 0.2538 0.0037  -0.0098 -0.0305 155 VAL   B O   
6374 C CB  . VAL   B 155 ? 0.1497 0.1511 0.2851 -0.0048 -0.0141 0.0019  155 VAL   B CB  
6375 C CG1 . VAL   B 155 ? 0.1549 0.1435 0.2768 -0.0102 -0.0059 -0.0033 155 VAL   B CG1 
6376 C CG2 . VAL   B 155 ? 0.1450 0.1658 0.3027 -0.0116 -0.0174 0.0313  155 VAL   B CG2 
6386 N N   . PHE   B 156 ? 0.1389 0.1455 0.2434 0.0003  -0.0091 -0.0130 156 PHE   B N   
6387 C CA  . PHE   B 156 ? 0.1426 0.1561 0.2808 0.0043  -0.0081 -0.0158 156 PHE   B CA  
6388 C C   . PHE   B 156 ? 0.1388 0.1608 0.3080 0.0120  -0.0089 -0.0323 156 PHE   B C   
6389 O O   . PHE   B 156 ? 0.1637 0.1753 0.3390 0.0210  0.0005  -0.0333 156 PHE   B O   
6390 C CB  . PHE   B 156 ? 0.1485 0.1493 0.2885 -0.0021 -0.0119 -0.0067 156 PHE   B CB  
6391 C CG  . PHE   B 156 ? 0.1511 0.1619 0.3013 -0.0022 -0.0112 0.0103  156 PHE   B CG  
6392 C CD1 . PHE   B 156 ? 0.1527 0.1901 0.3278 -0.0005 -0.0052 0.0369  156 PHE   B CD1 
6393 C CD2 . PHE   B 156 ? 0.1550 0.1714 0.3043 0.0049  -0.0217 0.0146  156 PHE   B CD2 
6394 C CE1 . PHE   B 156 ? 0.1542 0.2013 0.3409 -0.0018 -0.0056 0.0360  156 PHE   B CE1 
6395 C CE2 . PHE   B 156 ? 0.1626 0.1999 0.3225 0.0061  -0.0255 0.0123  156 PHE   B CE2 
6396 C CZ  . PHE   B 156 ? 0.1518 0.2010 0.3429 0.0126  -0.0220 0.0222  156 PHE   B CZ  
6406 N N   . ASP   B 157 ? 0.1444 0.1531 0.3264 0.0104  -0.0269 -0.0148 157 ASP   B N   
6407 C CA  . ASP   B 157 ? 0.1585 0.1599 0.3515 0.0133  -0.0288 -0.0162 157 ASP   B CA  
6408 C C   . ASP   B 157 ? 0.1581 0.1584 0.3619 0.0094  -0.0220 -0.0366 157 ASP   B C   
6409 O O   . ASP   B 157 ? 0.1443 0.1547 0.3588 0.0037  -0.0269 -0.0309 157 ASP   B O   
6410 C CB  . ASP   B 157 ? 0.1899 0.1803 0.3637 0.0074  -0.0530 0.0001  157 ASP   B CB  
6411 C CG  . ASP   B 157 ? 0.2312 0.1904 0.3896 -0.0007 -0.0397 -0.0052 157 ASP   B CG  
6412 O OD1 . ASP   B 157 ? 0.2369 0.1847 0.4038 0.0047  -0.0324 -0.0027 157 ASP   B OD1 
6413 O OD2 . ASP   B 157 ? 0.2661 0.2082 0.4146 -0.0041 -0.0260 -0.0060 157 ASP   B OD2 
6418 N N   . LYS   B 158 ? 0.1594 0.1846 0.3749 0.0039  -0.0058 -0.0646 158 LYS   B N   
6419 C CA  . LYS   B 158 ? 0.1802 0.2001 0.3901 0.0039  0.0035  -0.0876 158 LYS   B CA  
6420 C C   . LYS   B 158 ? 0.1808 0.1847 0.3986 0.0011  -0.0073 -0.0775 158 LYS   B C   
6421 O O   . LYS   B 158 ? 0.1791 0.1808 0.4034 -0.0073 -0.0069 -0.0831 158 LYS   B O   
6422 C CB  . LYS   B 158 ? 0.2076 0.2426 0.3931 0.0043  0.0120  -0.1159 158 LYS   B CB  
6423 C CG  . LYS   B 158 ? 0.2439 0.2871 0.4056 0.0054  0.0184  -0.1237 158 LYS   B CG  
6424 C CD  . LYS   B 158 ? 0.2673 0.3424 0.4223 0.0042  0.0283  -0.1160 158 LYS   B CD  
6425 C CE  . LYS   B 158 ? 0.2836 0.3731 0.4334 0.0080  0.0307  -0.1103 158 LYS   B CE  
6426 N NZ  . LYS   B 158 ? 0.2845 0.3962 0.4315 0.0074  0.0316  -0.1076 158 LYS   B NZ  
6440 N N   . ASN   B 159 ? 0.1820 0.1764 0.4152 0.0039  -0.0178 -0.0636 159 ASN   B N   
6441 C CA  . ASN   B 159 ? 0.1918 0.1712 0.4320 0.0161  -0.0302 -0.0473 159 ASN   B CA  
6442 C C   . ASN   B 159 ? 0.1720 0.1542 0.4201 0.0117  -0.0432 -0.0382 159 ASN   B C   
6443 O O   . ASN   B 159 ? 0.1775 0.1473 0.4481 -0.0046 -0.0483 -0.0272 159 ASN   B O   
6444 C CB  . ASN   B 159 ? 0.2114 0.1863 0.4588 0.0270  -0.0410 -0.0387 159 ASN   B CB  
6445 C CG  . ASN   B 159 ? 0.2394 0.2074 0.4891 0.0296  -0.0478 -0.0538 159 ASN   B CG  
6446 O OD1 . ASN   B 159 ? 0.2506 0.2168 0.4901 0.0373  -0.0460 -0.0627 159 ASN   B OD1 
6447 N ND2 . ASN   B 159 ? 0.2426 0.2173 0.5025 0.0301  -0.0559 -0.0533 159 ASN   B ND2 
6454 N N   . LEU   B 160 ? 0.1600 0.1529 0.3975 0.0068  -0.0366 -0.0280 160 LEU   B N   
6455 C CA  . LEU   B 160 ? 0.1620 0.1571 0.3575 0.0044  -0.0336 -0.0160 160 LEU   B CA  
6456 C C   . LEU   B 160 ? 0.1581 0.1445 0.3468 -0.0018 -0.0266 -0.0245 160 LEU   B C   
6457 O O   . LEU   B 160 ? 0.1489 0.1498 0.3432 -0.0036 -0.0310 -0.0138 160 LEU   B O   
6458 C CB  . LEU   B 160 ? 0.1639 0.1667 0.3407 0.0055  -0.0308 -0.0099 160 LEU   B CB  
6459 C CG  . LEU   B 160 ? 0.1602 0.1811 0.3231 0.0101  -0.0298 -0.0016 160 LEU   B CG  
6460 C CD1 . LEU   B 160 ? 0.1755 0.1992 0.3166 -0.0003 -0.0122 0.0029  160 LEU   B CD1 
6461 C CD2 . LEU   B 160 ? 0.1653 0.1828 0.3202 0.0238  -0.0298 -0.0099 160 LEU   B CD2 
6473 N N   . TYR   B 161 ? 0.1551 0.1484 0.3507 -0.0075 -0.0007 -0.0381 161 TYR   B N   
6474 C CA  . TYR   B 161 ? 0.1669 0.1555 0.3326 -0.0134 0.0127  -0.0387 161 TYR   B CA  
6475 C C   . TYR   B 161 ? 0.1740 0.1501 0.3323 -0.0113 0.0124  -0.0354 161 TYR   B C   
6476 O O   . TYR   B 161 ? 0.1734 0.1511 0.3256 -0.0194 0.0086  -0.0330 161 TYR   B O   
6477 C CB  . TYR   B 161 ? 0.1825 0.1667 0.3231 -0.0247 0.0331  -0.0435 161 TYR   B CB  
6478 C CG  . TYR   B 161 ? 0.2076 0.1684 0.3131 -0.0315 0.0355  -0.0570 161 TYR   B CG  
6479 C CD1 . TYR   B 161 ? 0.2164 0.1676 0.3098 -0.0409 0.0403  -0.0508 161 TYR   B CD1 
6480 C CD2 . TYR   B 161 ? 0.2289 0.1770 0.3021 -0.0291 0.0269  -0.0616 161 TYR   B CD2 
6481 C CE1 . TYR   B 161 ? 0.2380 0.1878 0.3056 -0.0378 0.0394  -0.0527 161 TYR   B CE1 
6482 C CE2 . TYR   B 161 ? 0.2500 0.1958 0.3019 -0.0355 0.0308  -0.0601 161 TYR   B CE2 
6483 C CZ  . TYR   B 161 ? 0.2525 0.1981 0.2963 -0.0472 0.0288  -0.0493 161 TYR   B CZ  
6484 O OH  . TYR   B 161 ? 0.2844 0.2219 0.3110 -0.0497 0.0242  -0.0434 161 TYR   B OH  
6494 N N   . ASP   B 162 ? 0.1793 0.1488 0.3509 -0.0074 0.0023  -0.0487 162 ASP   B N   
6495 C CA  . ASP   B 162 ? 0.1852 0.1555 0.3531 -0.0054 -0.0079 -0.0511 162 ASP   B CA  
6496 C C   . ASP   B 162 ? 0.1784 0.1515 0.3495 -0.0097 -0.0070 -0.0402 162 ASP   B C   
6497 O O   . ASP   B 162 ? 0.1755 0.1563 0.3547 -0.0178 -0.0234 -0.0303 162 ASP   B O   
6498 C CB  . ASP   B 162 ? 0.2063 0.1734 0.3664 0.0001  -0.0123 -0.0670 162 ASP   B CB  
6499 C CG  . ASP   B 162 ? 0.2123 0.2010 0.3887 0.0067  -0.0061 -0.0792 162 ASP   B CG  
6500 O OD1 . ASP   B 162 ? 0.2111 0.2241 0.3822 0.0012  0.0085  -0.0787 162 ASP   B OD1 
6501 O OD2 . ASP   B 162 ? 0.2234 0.2218 0.4124 0.0210  -0.0059 -0.0711 162 ASP   B OD2 
6506 N N   . LYS   B 163 ? 0.1764 0.1366 0.3371 -0.0073 -0.0197 -0.0233 163 LYS   B N   
6507 C CA  . LYS   B 163 ? 0.1903 0.1464 0.3449 -0.0156 -0.0098 -0.0082 163 LYS   B CA  
6508 C C   . LYS   B 163 ? 0.1586 0.1428 0.3282 -0.0147 -0.0134 -0.0002 163 LYS   B C   
6509 O O   . LYS   B 163 ? 0.1560 0.1545 0.3545 -0.0224 -0.0136 0.0044  163 LYS   B O   
6510 C CB  . LYS   B 163 ? 0.2444 0.1835 0.3749 -0.0143 -0.0131 0.0038  163 LYS   B CB  
6511 C CG  . LYS   B 163 ? 0.3297 0.2655 0.4341 -0.0192 0.0017  0.0114  163 LYS   B CG  
6512 C CD  . LYS   B 163 ? 0.4004 0.3503 0.4978 -0.0319 0.0048  0.0084  163 LYS   B CD  
6513 C CE  . LYS   B 163 ? 0.4594 0.4122 0.5426 -0.0404 0.0114  0.0095  163 LYS   B CE  
6514 N NZ  . LYS   B 163 ? 0.4916 0.4521 0.5710 -0.0445 0.0127  0.0068  163 LYS   B NZ  
6528 N N   . LEU   B 164 ? 0.1465 0.1337 0.3027 -0.0118 -0.0216 -0.0042 164 LEU   B N   
6529 C CA  . LEU   B 164 ? 0.1480 0.1388 0.2904 -0.0122 -0.0249 -0.0028 164 LEU   B CA  
6530 C C   . LEU   B 164 ? 0.1570 0.1411 0.2865 -0.0152 -0.0319 0.0023  164 LEU   B C   
6531 O O   . LEU   B 164 ? 0.1604 0.1618 0.2991 -0.0167 -0.0339 0.0024  164 LEU   B O   
6532 C CB  . LEU   B 164 ? 0.1459 0.1350 0.2785 -0.0073 -0.0216 -0.0018 164 LEU   B CB  
6533 C CG  . LEU   B 164 ? 0.1571 0.1564 0.2860 -0.0091 -0.0143 0.0041  164 LEU   B CG  
6534 C CD1 . LEU   B 164 ? 0.1623 0.1547 0.2847 -0.0180 -0.0221 -0.0005 164 LEU   B CD1 
6535 C CD2 . LEU   B 164 ? 0.1706 0.1914 0.3110 -0.0097 0.0005  -0.0122 164 LEU   B CD2 
6547 N N   . VAL   B 165 ? 0.1882 0.1452 0.3046 -0.0191 -0.0423 -0.0068 165 VAL   B N   
6548 C CA  . VAL   B 165 ? 0.2218 0.1546 0.3058 -0.0266 -0.0612 -0.0090 165 VAL   B CA  
6549 C C   . VAL   B 165 ? 0.2484 0.1669 0.3355 -0.0347 -0.0843 -0.0119 165 VAL   B C   
6550 O O   . VAL   B 165 ? 0.2679 0.1833 0.3402 -0.0417 -0.0892 -0.0019 165 VAL   B O   
6551 C CB  . VAL   B 165 ? 0.2468 0.1720 0.3019 -0.0095 -0.0303 -0.0097 165 VAL   B CB  
6552 C CG1 . VAL   B 165 ? 0.2660 0.1868 0.3245 -0.0097 -0.0149 -0.0099 165 VAL   B CG1 
6553 C CG2 . VAL   B 165 ? 0.2440 0.1768 0.2834 -0.0056 -0.0213 -0.0074 165 VAL   B CG2 
6563 N N   . SER   B 166 ? 0.2567 0.1552 0.3761 -0.0319 -0.0890 -0.0375 166 SER   B N   
6564 C CA  . SER   B 166 ? 0.2514 0.1591 0.4250 -0.0332 -0.0803 -0.0384 166 SER   B CA  
6565 C C   . SER   B 166 ? 0.2353 0.1747 0.4445 -0.0389 -0.0845 -0.0118 166 SER   B C   
6566 O O   . SER   B 166 ? 0.2401 0.1951 0.4757 -0.0512 -0.0966 -0.0350 166 SER   B O   
6567 C CB  . SER   B 166 ? 0.2483 0.1684 0.4441 -0.0303 -0.0767 -0.0413 166 SER   B CB  
6568 O OG  . SER   B 166 ? 0.2353 0.1693 0.4571 -0.0186 -0.0720 -0.0163 166 SER   B OG  
6574 N N   . SER   B 167 ? 0.2148 0.1629 0.4188 -0.0435 -0.0869 0.0290  167 SER   B N   
6575 C CA  . SER   B 167 ? 0.2088 0.1719 0.3965 -0.0400 -0.0638 0.0273  167 SER   B CA  
6576 C C   . SER   B 167 ? 0.2007 0.1794 0.3685 -0.0480 -0.0557 0.0456  167 SER   B C   
6577 O O   . SER   B 167 ? 0.1973 0.1925 0.3595 -0.0474 -0.0511 0.0354  167 SER   B O   
6578 C CB  . SER   B 167 ? 0.1963 0.1778 0.4016 -0.0339 -0.0344 0.0208  167 SER   B CB  
6579 O OG  . SER   B 167 ? 0.1883 0.1862 0.4000 -0.0203 -0.0133 0.0154  167 SER   B OG  
6585 N N   . PHE   B 168 ? 0.2019 0.1826 0.3500 -0.0453 -0.0456 0.0503  168 PHE   B N   
6586 C CA  . PHE   B 168 ? 0.2089 0.1824 0.3261 -0.0463 -0.0408 0.0316  168 PHE   B CA  
6587 C C   . PHE   B 168 ? 0.1796 0.1706 0.2913 -0.0280 -0.0201 0.0090  168 PHE   B C   
6588 O O   . PHE   B 168 ? 0.2121 0.1589 0.2863 0.0015  -0.0151 -0.0014 168 PHE   B O   
6589 C CB  . PHE   B 168 ? 0.2238 0.1834 0.3231 -0.0584 -0.0514 0.0480  168 PHE   B CB  
6590 C CG  . PHE   B 168 ? 0.2538 0.1679 0.3007 -0.0543 -0.0498 0.0220  168 PHE   B CG  
6591 C CD1 . PHE   B 168 ? 0.2855 0.1723 0.3128 -0.0507 -0.0499 0.0169  168 PHE   B CD1 
6592 C CD2 . PHE   B 168 ? 0.2509 0.1652 0.2901 -0.0447 -0.0430 0.0194  168 PHE   B CD2 
6593 C CE1 . PHE   B 168 ? 0.2980 0.1816 0.3095 -0.0402 -0.0379 0.0187  168 PHE   B CE1 
6594 C CE2 . PHE   B 168 ? 0.2763 0.1717 0.2996 -0.0298 -0.0416 0.0142  168 PHE   B CE2 
6595 C CZ  . PHE   B 168 ? 0.2891 0.1696 0.3071 -0.0273 -0.0428 0.0218  168 PHE   B CZ  
6605 N N   . LEU   B 169 ? 0.1786 0.1839 0.2918 -0.0105 -0.0064 0.0001  169 LEU   B N   
6606 C CA  . LEU   B 169 ? 0.2022 0.2138 0.3167 -0.0109 -0.0057 -0.0287 169 LEU   B CA  
6607 C C   . LEU   B 169 ? 0.2301 0.2356 0.3742 0.0055  -0.0104 -0.0540 169 LEU   B C   
6608 O O   . LEU   B 169 ? 0.2495 0.2560 0.4188 0.0073  -0.0098 -0.0776 169 LEU   B O   
6609 C CB  . LEU   B 169 ? 0.2226 0.2581 0.3163 -0.0180 -0.0071 -0.0048 169 LEU   B CB  
6610 C CG  . LEU   B 169 ? 0.2642 0.3024 0.3450 -0.0046 -0.0031 -0.0020 169 LEU   B CG  
6611 C CD1 . LEU   B 169 ? 0.2796 0.3220 0.3493 -0.0033 -0.0039 0.0110  169 LEU   B CD1 
6612 C CD2 . LEU   B 169 ? 0.2583 0.3115 0.3405 0.0079  0.0110  -0.0184 169 LEU   B CD2 
6613 O OXT . LEU   B 169 ? 0.2506 0.2521 0.3778 0.0327  -0.0048 -0.0576 169 LEU   B OXT 
6625 C C1  T TFA   C .   ? 0.1471 0.1696 0.0865 -0.0158 0.0280  0.0158  201 TFA   A C1  
6626 C C2  T TFA   C .   ? 0.1648 0.1916 0.1349 -0.0223 0.0143  -0.0024 201 TFA   A C2  
6627 O O   T TFA   C .   ? 0.1279 0.1581 0.0921 -0.0098 0.0357  0.0248  201 TFA   A O   
6628 F F1  T TFA   C .   ? 0.1742 0.1961 0.1583 -0.0213 0.0034  -0.0092 201 TFA   A F1  
6629 F F2  T TFA   C .   ? 0.1702 0.2004 0.1380 -0.0231 0.0222  0.0006  201 TFA   A F2  
6630 F F3  T TFA   C .   ? 0.1728 0.2014 0.1585 -0.0287 0.0206  -0.0004 201 TFA   A F3  
6631 O OXT T TFA   C .   ? 0.1458 0.1646 0.0679 -0.0079 0.0403  0.0205  201 TFA   A OXT 
6632 N N2  B A1BAK D .   ? 0.1619 0.1638 0.1916 -0.0054 0.0107  0.0187  202 A1BAK A N2  
6633 C C3  B A1BAK D .   ? 0.1902 0.1482 0.2120 -0.0022 0.0105  0.0381  202 A1BAK A C3  
6634 C C6  B A1BAK D .   ? 0.1533 0.1537 0.1649 0.0081  -0.0035 0.0185  202 A1BAK A C6  
6635 C C9  B A1BAK D .   ? 0.1543 0.1527 0.1687 0.0023  0.0017  0.0175  202 A1BAK A C9  
6636 C C1  B A1BAK D .   ? 0.2151 0.1976 0.2457 -0.0021 -0.0012 0.0441  202 A1BAK A C1  
6637 C C10 B A1BAK D .   ? 0.1935 0.1756 0.2163 -0.0018 0.0033  0.0410  202 A1BAK A C10 
6638 C C2  B A1BAK D .   ? 0.2118 0.1809 0.2343 0.0033  0.0023  0.0443  202 A1BAK A C2  
6639 C C4  B A1BAK D .   ? 0.1629 0.1576 0.1837 -0.0046 0.0092  0.0262  202 A1BAK A C4  
6640 C C5  B A1BAK D .   ? 0.1643 0.1699 0.1943 0.0026  0.0010  0.0162  202 A1BAK A C5  
6641 C C7  B A1BAK D .   ? 0.1538 0.1563 0.1686 0.0052  0.0065  0.0242  202 A1BAK A C7  
6642 C C8  B A1BAK D .   ? 0.1633 0.1612 0.1748 -0.0018 0.0100  0.0193  202 A1BAK A C8  
6643 N N1  B A1BAK D .   ? 0.1781 0.1550 0.1990 -0.0071 0.0029  0.0371  202 A1BAK A N1  
6644 N N3  B A1BAK D .   ? 0.1644 0.1634 0.1855 0.0010  0.0034  0.0232  202 A1BAK A N3  
6645 N N4  B A1BAK D .   ? 0.1525 0.1460 0.1622 0.0105  -0.0110 0.0275  202 A1BAK A N4  
6646 O O1  B A1BAK D .   ? 0.2280 0.2249 0.2849 -0.0024 -0.0132 0.0421  202 A1BAK A O1  
6659 O O   . HOH   E .   ? 0.4535 0.7811 0.5000 -0.1125 0.0634  0.1355  301 HOH   A O   
6660 O O   B HOH   E .   ? 0.4654 0.3694 0.3757 0.1433  -0.0528 -0.0881 302 HOH   A O   
6661 O O   . HOH   E .   ? 0.6410 0.7141 0.5972 0.0221  0.0802  0.0185  303 HOH   A O   
6662 O O   . HOH   E .   ? 0.3079 0.2797 0.4805 -0.0295 -0.1514 0.1201  304 HOH   A O   
6663 O O   B HOH   E .   ? 0.3212 0.2485 0.1649 -0.1152 -0.0074 0.0293  305 HOH   A O   
6664 O O   . HOH   E .   ? 0.4418 0.3603 0.4575 -0.0033 0.1123  0.0108  306 HOH   A O   
6665 O O   B HOH   E .   ? 0.5345 0.3507 0.4704 0.1023  -0.0577 0.0297  307 HOH   A O   
6666 O O   A HOH   E .   ? 0.2155 0.2514 0.2959 -0.0402 -0.0331 0.0341  308 HOH   A O   
6667 O O   . HOH   E .   ? 0.6135 0.5017 0.3456 0.2177  -0.0996 0.0654  309 HOH   A O   
6668 O O   . HOH   E .   ? 0.3220 0.6994 0.5820 -0.0612 -0.0815 0.2184  310 HOH   A O   
6669 O O   . HOH   E .   ? 0.5745 0.3496 0.5414 -0.0687 0.1750  0.0972  311 HOH   A O   
6670 O O   . HOH   E .   ? 0.5845 0.6546 0.5174 -0.1165 -0.1197 -0.0949 312 HOH   A O   
6671 O O   . HOH   E .   ? 0.5821 0.4423 0.7178 0.1186  0.0554  -0.1194 313 HOH   A O   
6672 O O   . HOH   E .   ? 0.3182 0.3438 0.1860 -0.0263 0.0468  0.0499  314 HOH   A O   
6673 O O   B HOH   E .   ? 0.2779 0.2223 0.2588 0.0632  -0.0303 0.0948  315 HOH   A O   
6674 O O   . HOH   E .   ? 0.5190 0.2844 0.3212 -0.1309 0.0766  0.0124  316 HOH   A O   
6675 O O   B HOH   E .   ? 0.2700 0.2373 0.3851 -0.0452 -0.0832 -0.0144 317 HOH   A O   
6676 O O   A HOH   E .   ? 0.1624 0.2435 0.2399 0.0518  0.0457  0.0912  318 HOH   A O   
6677 O O   . HOH   E .   ? 0.5101 0.5456 0.3399 -0.1230 0.1468  0.0688  319 HOH   A O   
6678 O O   . HOH   E .   ? 0.5332 0.5103 0.4484 -0.0582 0.0936  0.2209  320 HOH   A O   
6679 O O   B HOH   E .   ? 0.4311 0.2656 0.4022 0.1142  -0.1015 0.0537  321 HOH   A O   
6680 O O   . HOH   E .   ? 0.4705 0.5713 0.5804 0.1852  0.1207  -0.0505 322 HOH   A O   
6681 O O   . HOH   E .   ? 0.2145 0.1958 0.3757 -0.0444 0.0096  -0.0259 323 HOH   A O   
6682 O O   . HOH   E .   ? 0.3312 0.3233 0.3194 -0.1025 0.0042  0.0810  324 HOH   A O   
6683 O O   . HOH   E .   ? 0.1863 0.3797 0.3101 0.0526  -0.0183 0.0069  325 HOH   A O   
6684 O O   . HOH   E .   ? 0.6340 0.4083 0.6071 0.0560  -0.0625 -0.0233 326 HOH   A O   
6685 O O   . HOH   E .   ? 0.5950 0.4923 0.4433 -0.1076 -0.0459 0.2029  327 HOH   A O   
6686 O O   . HOH   E .   ? 0.3386 0.3964 0.3986 -0.0632 0.1386  0.0604  328 HOH   A O   
6687 O O   . HOH   E .   ? 0.5621 0.3676 0.3813 -0.0945 -0.1065 0.0462  329 HOH   A O   
6688 O O   . HOH   E .   ? 0.2659 0.6121 0.4039 -0.0046 -0.0651 0.0821  330 HOH   A O   
6689 O O   . HOH   E .   ? 0.2924 0.2291 0.2735 -0.0464 0.0192  -0.0269 331 HOH   A O   
6690 O O   A HOH   E .   ? 0.2035 0.2159 0.2273 -0.0096 0.0476  0.0530  332 HOH   A O   
6691 O O   . HOH   E .   ? 0.2088 0.3689 0.4169 -0.0354 0.0460  -0.0915 333 HOH   A O   
6692 O O   . HOH   E .   ? 0.7285 0.5769 0.3510 -0.0439 -0.0759 0.1321  334 HOH   A O   
6693 O O   . HOH   E .   ? 0.4107 0.3095 0.3234 -0.1171 -0.0357 -0.0074 335 HOH   A O   
6694 O O   . HOH   E .   ? 0.5788 0.4138 0.5635 0.0703  0.1545  -0.1385 336 HOH   A O   
6695 O O   . HOH   E .   ? 0.1648 0.1639 0.2401 -0.0209 0.0043  0.0064  337 HOH   A O   
6696 O O   . HOH   E .   ? 0.6609 0.4306 0.4357 -0.1859 -0.1138 0.2084  338 HOH   A O   
6697 O O   . HOH   E .   ? 0.3299 0.4901 0.2661 -0.0160 0.0317  0.0305  339 HOH   A O   
6698 O O   . HOH   E .   ? 0.2183 0.4567 0.4331 -0.0233 -0.0702 0.1689  340 HOH   A O   
6699 O O   . HOH   E .   ? 0.8022 0.4521 0.5912 -0.0668 -0.1323 0.1129  341 HOH   A O   
6700 O O   . HOH   E .   ? 0.2213 0.1683 0.1704 -0.0069 0.0171  0.0171  342 HOH   A O   
6701 O O   . HOH   E .   ? 0.4458 0.2080 0.5185 0.0324  -0.1306 0.0485  343 HOH   A O   
6702 O O   . HOH   E .   ? 0.2429 0.2281 0.3094 0.0364  0.0420  0.0381  344 HOH   A O   
6703 O O   . HOH   E .   ? 0.5911 0.5434 0.4215 -0.0577 -0.1097 -0.1181 345 HOH   A O   
6704 O O   . HOH   E .   ? 0.4908 0.2088 0.5817 0.0719  -0.0296 -0.0081 346 HOH   A O   
6705 O O   . HOH   E .   ? 0.2379 0.4195 0.3500 0.0927  -0.0587 -0.0076 347 HOH   A O   
6706 O O   A HOH   E .   ? 0.2825 0.2229 0.1617 0.0462  -0.0066 0.0664  348 HOH   A O   
6707 O O   . HOH   E .   ? 0.6633 0.5052 0.4692 0.1307  0.1925  -0.0788 349 HOH   A O   
6708 O O   . HOH   E .   ? 0.2904 0.3678 0.4013 -0.0795 -0.0762 -0.0310 350 HOH   A O   
6709 O O   . HOH   E .   ? 0.1471 0.2370 0.2277 -0.0007 -0.0114 0.0510  351 HOH   A O   
6710 O O   . HOH   E .   ? 0.2193 0.1877 0.2583 0.0279  -0.0327 -0.0010 352 HOH   A O   
6711 O O   A HOH   E .   ? 0.2247 0.3024 0.3087 -0.0186 0.0851  0.0837  353 HOH   A O   
6712 O O   . HOH   E .   ? 0.1851 0.2510 0.2237 -0.0250 -0.0106 0.0796  354 HOH   A O   
6713 O O   A HOH   E .   ? 0.2025 0.3135 0.2247 0.0585  0.0190  0.0142  355 HOH   A O   
6714 O O   . HOH   E .   ? 0.3717 0.4638 0.3301 0.1830  0.0744  0.0816  356 HOH   A O   
6715 O O   . HOH   E .   ? 0.2094 0.2087 0.4106 0.0150  0.1004  -0.0130 357 HOH   A O   
6716 O O   . HOH   E .   ? 0.1506 0.2040 0.2747 0.0055  -0.0123 0.0014  358 HOH   A O   
6717 O O   . HOH   E .   ? 0.2686 0.4241 0.3649 -0.0551 0.0646  -0.0108 359 HOH   A O   
6718 O O   . HOH   E .   ? 0.1383 0.1379 0.1606 -0.0078 0.0128  0.0114  360 HOH   A O   
6719 O O   . HOH   E .   ? 0.1645 0.1904 0.2760 0.0073  -0.0296 -0.0484 361 HOH   A O   
6720 O O   . HOH   E .   ? 0.1515 0.1635 0.1531 -0.0085 -0.0113 0.0002  362 HOH   A O   
6721 O O   . HOH   E .   ? 0.4276 0.2604 0.4675 -0.1278 0.1180  0.0199  363 HOH   A O   
6722 O O   . HOH   E .   ? 0.3457 0.3892 0.2146 -0.1017 -0.0148 -0.0692 364 HOH   A O   
6723 O O   . HOH   E .   ? 0.1579 0.1413 0.2570 -0.0059 0.0195  -0.0097 365 HOH   A O   
6724 O O   . HOH   E .   ? 0.1705 0.2663 0.2992 -0.0095 0.0582  0.0747  366 HOH   A O   
6725 O O   . HOH   E .   ? 0.2003 0.2026 0.2448 -0.0369 0.0049  0.0388  367 HOH   A O   
6726 O O   . HOH   E .   ? 0.3078 0.3350 0.5179 -0.0697 -0.1049 -0.0796 368 HOH   A O   
6727 O O   . HOH   E .   ? 0.4657 0.2859 0.4107 -0.1804 0.1533  -0.0616 369 HOH   A O   
6728 O O   . HOH   E .   ? 0.5344 0.5683 0.7997 -0.1114 0.0171  0.2011  370 HOH   A O   
6729 O O   . HOH   E .   ? 0.2968 0.4376 0.2943 0.0561  0.0827  0.1706  371 HOH   A O   
6730 O O   . HOH   E .   ? 0.4308 0.6810 0.5585 0.1297  0.1970  0.0532  372 HOH   A O   
6731 O O   . HOH   E .   ? 0.4048 0.2166 0.2680 0.1107  0.0445  0.0268  373 HOH   A O   
6732 O O   . HOH   E .   ? 0.2050 0.2120 0.1878 0.0037  0.0145  0.0250  374 HOH   A O   
6733 O O   . HOH   E .   ? 0.1773 0.1827 0.2425 -0.0255 0.0085  0.0311  375 HOH   A O   
6734 O O   A HOH   E .   ? 0.2439 0.4392 0.4034 0.0594  0.0086  0.0558  376 HOH   A O   
6735 O O   T HOH   E .   ? 0.1057 0.1086 0.1872 -0.0191 0.0142  0.0420  377 HOH   A O   
6736 O O   . HOH   E .   ? 0.1853 0.1770 0.2412 0.0118  -0.0252 0.0328  378 HOH   A O   
6737 O O   . HOH   E .   ? 0.3709 0.2724 0.5202 -0.0933 -0.0303 0.0371  379 HOH   A O   
6738 O O   . HOH   E .   ? 0.2511 0.1946 0.2654 -0.0062 0.0087  0.0226  380 HOH   A O   
6739 O O   . HOH   E .   ? 0.2021 0.2488 0.4199 0.0157  0.0930  -0.0554 381 HOH   A O   
6740 O O   . HOH   E .   ? 0.6197 0.3683 0.3404 0.0545  -0.0169 0.0825  382 HOH   A O   
6741 O O   . HOH   E .   ? 0.2251 0.1848 0.3144 -0.0120 -0.0584 -0.0081 383 HOH   A O   
6742 O O   A HOH   E .   ? 0.3106 0.1599 0.1918 0.0194  0.0031  0.0042  384 HOH   A O   
6743 O O   . HOH   E .   ? 0.3848 0.6992 0.5591 -0.0577 -0.1407 0.0114  385 HOH   A O   
6744 O O   . HOH   E .   ? 0.3265 0.3007 0.2020 0.0250  0.0756  0.0073  386 HOH   A O   
6745 O O   . HOH   E .   ? 0.2890 0.4827 0.3445 -0.0042 -0.0368 0.1001  387 HOH   A O   
6746 O O   A HOH   E .   ? 0.1281 0.3283 0.2264 -0.0038 0.0078  0.0684  388 HOH   A O   
6747 O O   . HOH   E .   ? 0.2246 0.2186 0.3763 -0.0009 -0.0579 0.0467  389 HOH   A O   
6748 O O   . HOH   E .   ? 0.2966 0.4221 0.4278 -0.0461 0.1165  -0.0227 390 HOH   A O   
6749 O O   . HOH   E .   ? 0.2569 0.2100 0.1842 -0.0561 0.0059  0.0309  391 HOH   A O   
6750 O O   . HOH   E .   ? 0.2009 0.2457 0.2498 -0.0223 -0.0402 0.0496  392 HOH   A O   
6751 O O   B HOH   E .   ? 0.3207 0.4086 0.2164 0.2058  0.0369  0.0735  393 HOH   A O   
6752 O O   . HOH   E .   ? 0.2226 0.2531 0.4715 0.0026  -0.0503 -0.0627 394 HOH   A O   
6753 O O   . HOH   E .   ? 0.1943 0.2767 0.2744 0.0357  0.0361  0.0834  395 HOH   A O   
6754 O O   . HOH   E .   ? 0.3162 0.3551 0.3713 -0.1352 0.1018  -0.0019 396 HOH   A O   
6755 O O   . HOH   E .   ? 0.3074 0.2802 0.2215 -0.0659 -0.0770 0.0232  397 HOH   A O   
6756 O O   . HOH   E .   ? 0.1935 0.1991 0.3886 0.0322  0.1004  0.0969  398 HOH   A O   
6757 O O   . HOH   E .   ? 0.3112 0.2761 0.3248 -0.0215 -0.0278 0.1057  399 HOH   A O   
6758 O O   . HOH   E .   ? 0.2727 0.3232 0.2955 -0.0292 0.0985  -0.0262 400 HOH   A O   
6759 O O   . HOH   E .   ? 0.2607 0.2387 0.3713 -0.0060 -0.0333 0.0820  401 HOH   A O   
6760 O O   . HOH   E .   ? 0.2076 0.2231 0.2853 -0.0180 -0.0318 0.0773  402 HOH   A O   
6761 O O   . HOH   E .   ? 0.4103 0.5132 0.6794 0.1230  -0.0889 0.1010  403 HOH   A O   
6762 O O   . HOH   E .   ? 0.2614 0.3773 0.3894 -0.0399 0.1181  -0.0913 404 HOH   A O   
6763 O O   . HOH   E .   ? 0.3095 0.6557 0.4194 0.1262  0.0917  -0.0481 405 HOH   A O   
6764 O O   . HOH   E .   ? 0.5675 0.2853 0.5403 0.0830  -0.0473 -0.0023 406 HOH   A O   
6765 O O   B HOH   E .   ? 0.3285 0.4802 0.3015 0.0248  -0.0712 -0.0673 407 HOH   A O   
6766 O O   . HOH   E .   ? 0.2978 0.3664 0.7164 -0.0249 0.1250  -0.0429 408 HOH   A O   
6767 O O   . HOH   E .   ? 0.1402 0.1491 0.2092 -0.0020 -0.0108 0.0073  409 HOH   A O   
6768 O O   . HOH   E .   ? 0.3561 0.4795 0.2201 -0.0828 -0.0586 -0.0080 410 HOH   A O   
6769 O O   . HOH   E .   ? 0.2249 0.1819 0.2962 -0.0044 -0.0285 0.0102  411 HOH   A O   
6770 O O   . HOH   E .   ? 0.3689 0.7775 0.3728 -0.0821 0.0040  0.1091  412 HOH   A O   
6771 O O   . HOH   E .   ? 0.2196 0.2937 0.2438 -0.0092 -0.0501 0.0434  413 HOH   A O   
6772 O O   A HOH   E .   ? 0.1535 0.1486 0.1514 0.0090  -0.0200 0.0141  414 HOH   A O   
6773 O O   . HOH   E .   ? 0.1874 0.2683 0.4091 0.0018  -0.0196 0.0224  415 HOH   A O   
6774 O O   . HOH   E .   ? 0.5385 0.4153 0.1872 -0.0806 0.0513  0.0575  416 HOH   A O   
6775 O O   B HOH   E .   ? 0.1774 0.1634 0.1954 -0.0056 0.0108  0.0349  417 HOH   A O   
6776 O O   . HOH   E .   ? 0.1613 0.1769 0.3277 -0.0052 -0.0012 0.0225  418 HOH   A O   
6777 O O   . HOH   E .   ? 0.7074 0.4026 0.4936 -0.0073 0.1557  0.1489  419 HOH   A O   
6778 O O   A HOH   E .   ? 0.2085 0.2056 0.3239 -0.0247 0.0331  0.0010  420 HOH   A O   
6779 O O   . HOH   E .   ? 0.2477 0.2156 0.2627 -0.0560 0.0008  0.0542  421 HOH   A O   
6780 O O   B HOH   E .   ? 0.2797 0.2805 0.3587 0.0246  0.0587  -0.0331 422 HOH   A O   
6781 O O   A HOH   E .   ? 0.1167 0.1678 0.1444 0.0227  -0.0380 -0.0357 423 HOH   A O   
6782 O O   . HOH   E .   ? 0.2817 0.6666 0.1736 -0.0162 0.0265  0.0080  424 HOH   A O   
6783 O O   B HOH   E .   ? 0.4338 0.4274 0.2807 -0.0026 -0.0467 -0.1037 425 HOH   A O   
6784 O O   . HOH   E .   ? 0.3419 0.1387 0.2026 0.0030  -0.0493 0.0095  426 HOH   A O   
6785 O O   . HOH   E .   ? 0.1845 0.1441 0.1726 -0.0201 0.0154  0.0031  427 HOH   A O   
6786 O O   . HOH   E .   ? 0.3216 0.2818 0.2992 0.0010  -0.0403 -0.0375 428 HOH   A O   
6787 O O   B HOH   E .   ? 0.2280 0.2312 0.2789 0.0759  0.0352  0.1178  429 HOH   A O   
6788 O O   . HOH   E .   ? 0.4744 0.5262 0.4299 0.1590  -0.1242 -0.1556 430 HOH   A O   
6789 O O   . HOH   E .   ? 0.4073 0.6083 0.3361 -0.0515 0.0121  0.1203  431 HOH   A O   
6790 O O   . HOH   E .   ? 0.1719 0.2237 0.3021 -0.0172 -0.0086 0.0322  432 HOH   A O   
6791 O O   . HOH   E .   ? 0.2359 0.4519 0.2790 0.1676  0.0107  0.0487  433 HOH   A O   
6792 O O   . HOH   E .   ? 0.3747 0.3236 0.2336 -0.0269 -0.0425 0.0282  434 HOH   A O   
6793 O O   . HOH   E .   ? 0.4398 0.2230 0.5479 -0.0844 -0.2367 0.0973  435 HOH   A O   
6794 O O   . HOH   E .   ? 0.4243 0.5572 0.3663 0.2443  -0.0066 -0.0605 436 HOH   A O   
6795 O O   B HOH   E .   ? 0.1622 0.1690 0.4106 -0.0064 0.0057  0.0474  437 HOH   A O   
6796 O O   . HOH   E .   ? 0.6956 0.4164 0.4512 0.1956  -0.0844 0.1480  438 HOH   A O   
6797 O O   . HOH   E .   ? 0.5797 0.6051 0.5347 -0.0110 0.0807  0.1113  439 HOH   A O   
6798 O O   . HOH   E .   ? 0.6376 0.6909 0.6694 -0.1077 -0.0721 -0.0534 440 HOH   A O   
6799 O O   . HOH   E .   ? 0.5567 0.6255 0.4262 0.1790  -0.0633 -0.0245 441 HOH   A O   
6800 O O   . HOH   E .   ? 0.5650 0.7611 0.4506 0.0783  0.2851  -0.0308 442 HOH   A O   
6801 O O   A HOH   E .   ? 0.4936 0.3986 0.2909 -0.1203 -0.0206 0.1129  443 HOH   A O   
6802 O O   A HOH   E .   ? 0.4497 0.5139 0.3106 0.0601  -0.0945 0.1304  444 HOH   A O   
6803 O O   . HOH   E .   ? 0.9243 0.9926 0.7038 -0.0058 -0.0293 -0.0241 445 HOH   A O   
6804 O O   A HOH   E .   ? 0.1494 0.1388 0.2096 0.0270  -0.0390 0.0185  446 HOH   A O   
6805 O O   . HOH   E .   ? 0.4705 0.4708 0.4673 -0.0882 -0.1087 -0.1286 447 HOH   A O   
6806 O O   . HOH   E .   ? 0.5187 0.4945 0.4004 -0.0320 -0.1431 0.0423  448 HOH   A O   
6807 O O   A HOH   E .   ? 0.1687 0.1463 0.1438 0.0186  -0.0226 -0.0119 449 HOH   A O   
6808 O O   . HOH   E .   ? 0.2606 0.1672 0.2850 0.0011  0.0129  0.0043  450 HOH   A O   
6809 O O   . HOH   E .   ? 0.3672 0.2810 0.1959 -0.0530 0.0362  0.0542  451 HOH   A O   
6810 O O   A HOH   E .   ? 0.1896 0.1646 0.1628 0.0003  -0.0224 0.0036  452 HOH   A O   
6811 O O   . HOH   E .   ? 0.1912 0.2205 0.5547 -0.0242 -0.0952 0.0537  453 HOH   A O   
6812 O O   . HOH   E .   ? 0.6529 0.6316 0.4673 -0.0798 0.0688  0.1395  454 HOH   A O   
6813 O O   . HOH   E .   ? 0.6342 0.6954 0.6653 0.0809  -0.0788 -0.0028 455 HOH   A O   
6814 O O   . HOH   E .   ? 0.4506 0.3998 0.3488 0.2486  -0.0703 -0.0604 456 HOH   A O   
6815 O O   . HOH   E .   ? 0.6315 0.6906 0.7201 -0.1432 -0.0177 -0.1341 457 HOH   A O   
6816 O O   A HOH   E .   ? 0.5373 0.2498 0.3031 -0.0724 0.1137  0.0445  458 HOH   A O   
6817 O O   . HOH   E .   ? 0.2366 0.2047 0.3044 0.0197  0.0383  0.0253  459 HOH   A O   
6818 O O   . HOH   E .   ? 0.2191 0.2800 0.2745 -0.0072 -0.0081 -0.0497 460 HOH   A O   
6819 O O   . HOH   E .   ? 0.6914 0.5054 0.7616 0.1123  -0.0983 0.1421  461 HOH   A O   
6820 O O   . HOH   E .   ? 0.3106 0.3377 0.5578 -0.0022 0.1104  -0.1284 462 HOH   A O   
6821 O O   . HOH   E .   ? 0.5654 0.4567 0.4432 -0.0413 0.0905  0.0630  463 HOH   A O   
6822 O O   B HOH   E .   ? 0.4047 0.2139 0.3467 -0.1219 -0.0652 0.0436  464 HOH   A O   
6823 O O   B HOH   E .   ? 0.2624 0.1529 0.2777 -0.0648 0.0616  -0.0543 465 HOH   A O   
6824 O O   . HOH   E .   ? 0.4596 0.5774 0.4252 0.0814  0.0656  0.0822  466 HOH   A O   
6825 O O   . HOH   E .   ? 0.4904 0.3536 0.4694 0.0248  0.0868  0.0756  467 HOH   A O   
6826 O O   . HOH   E .   ? 0.3929 0.4476 0.4279 0.1888  -0.0426 0.1022  468 HOH   A O   
6827 O O   B HOH   E .   ? 0.5184 0.5293 0.4207 0.1400  -0.1010 0.0960  469 HOH   A O   
6828 O O   . HOH   E .   ? 0.7338 0.8292 0.5131 -0.0220 -0.0305 0.0370  470 HOH   A O   
6829 O O   . HOH   E .   ? 0.2916 0.2755 0.4102 -0.0563 0.0238  -0.0625 471 HOH   A O   
6830 O O   . HOH   E .   ? 0.3353 0.5500 0.4908 0.0606  -0.0543 0.0893  472 HOH   A O   
6831 O O   . HOH   E .   ? 0.3363 0.5504 0.4692 -0.1603 0.0526  -0.1177 473 HOH   A O   
6832 O O   . HOH   E .   ? 0.3364 0.2977 0.6476 0.0964  -0.1593 -0.0442 474 HOH   A O   
6833 O O   B HOH   E .   ? 0.2950 0.4291 0.3911 -0.1059 -0.0015 0.0428  475 HOH   A O   
6834 O O   . HOH   E .   ? 0.2602 0.4334 0.5517 0.0759  0.0063  -0.1687 476 HOH   A O   
6835 O O   . HOH   E .   ? 0.2786 0.1979 0.2434 0.0342  -0.0759 -0.0297 477 HOH   A O   
6836 O O   . HOH   E .   ? 0.6542 0.3163 0.7278 0.0137  -0.0035 0.2054  478 HOH   A O   
6837 O O   . HOH   E .   ? 0.2831 0.3097 0.3329 -0.1135 0.0413  -0.0356 479 HOH   A O   
6838 O O   . HOH   E .   ? 0.7132 0.5752 0.6904 0.1227  0.2508  0.2789  480 HOH   A O   
6839 O O   . HOH   E .   ? 0.3075 0.4549 0.4089 -0.0467 -0.0072 -0.0093 481 HOH   A O   
6840 O O   . HOH   E .   ? 0.4116 0.6482 0.4002 -0.1015 -0.0834 0.2205  482 HOH   A O   
6841 O O   . HOH   E .   ? 0.5360 0.5237 0.4804 0.0309  0.1142  0.0740  483 HOH   A O   
6842 O O   . HOH   E .   ? 0.4054 0.5349 0.4155 0.0356  -0.0718 -0.0697 484 HOH   A O   
6843 O O   . HOH   E .   ? 0.5630 0.5522 0.5378 0.1442  -0.0687 -0.0786 485 HOH   A O   
6844 O O   . HOH   E .   ? 0.3395 0.2839 0.3516 0.0462  0.0729  0.0101  486 HOH   A O   
6845 O O   . HOH   E .   ? 0.6970 0.3824 0.4902 -0.0412 0.0973  -0.0396 487 HOH   A O   
6846 O O   B HOH   E .   ? 0.2496 0.2504 0.2130 0.0062  0.0183  0.0034  488 HOH   A O   
6847 O O   . HOH   E .   ? 0.4273 0.5331 0.3191 -0.0177 -0.0427 -0.0135 489 HOH   A O   
6848 O O   . HOH   E .   ? 0.4838 0.4960 0.6573 -0.1826 -0.1283 -0.0152 490 HOH   A O   
6849 O O   . HOH   E .   ? 0.4268 0.5182 0.2853 -0.0180 -0.0100 0.0107  491 HOH   A O   
6850 O O   . HOH   E .   ? 0.4972 0.2932 0.3375 -0.0442 -0.1094 0.0576  492 HOH   A O   
6851 O O   . HOH   E .   ? 0.3132 0.4465 0.3655 -0.0337 -0.0222 -0.0936 493 HOH   A O   
6852 O O   B HOH   E .   ? 0.2074 0.2060 0.3491 0.0457  -0.0089 0.0726  494 HOH   A O   
6853 O O   . HOH   E .   ? 0.4601 0.4119 0.5365 -0.1633 -0.0515 -0.0152 495 HOH   A O   
6854 O O   . HOH   E .   ? 0.7217 0.5646 0.7563 -0.0735 0.0576  -0.1056 496 HOH   A O   
6855 O O   . HOH   E .   ? 0.6546 0.5879 0.6384 0.1256  0.1928  -0.1141 497 HOH   A O   
6856 O O   . HOH   E .   ? 0.5965 0.4053 0.4400 -0.0011 -0.0378 -0.1093 498 HOH   A O   
6857 O O   . HOH   E .   ? 0.8093 0.4013 0.3456 -0.0680 -0.1291 0.0338  499 HOH   A O   
6858 O O   . HOH   E .   ? 0.2677 0.2483 0.2610 0.0357  -0.0045 -0.0170 500 HOH   A O   
6859 O O   . HOH   E .   ? 0.4420 0.3657 0.2704 -0.0968 0.1432  -0.0464 501 HOH   A O   
6860 O O   . HOH   E .   ? 0.2999 0.4161 0.5403 0.0333  0.1533  0.1415  502 HOH   A O   
6861 O O   . HOH   E .   ? 0.2868 0.5575 0.3692 0.1371  0.0945  0.2474  503 HOH   A O   
6862 O O   . HOH   E .   ? 0.5805 0.6388 0.4080 -0.0950 0.1051  0.0909  504 HOH   A O   
6863 O O   . HOH   E .   ? 0.2653 0.2528 0.7211 -0.0161 -0.1457 0.0274  505 HOH   A O   
6864 O O   . HOH   E .   ? 0.4626 0.3591 0.4401 -0.1415 0.0322  0.0794  506 HOH   A O   
6865 O O   . HOH   E .   ? 0.5987 0.5045 0.5315 -0.1097 -0.1047 -0.0681 507 HOH   A O   
6866 O O   . HOH   E .   ? 0.2603 0.3862 0.5014 -0.0089 0.0724  -0.1028 508 HOH   A O   
6867 O O   . HOH   E .   ? 0.5588 0.5660 0.5778 0.1199  -0.0579 0.0810  509 HOH   A O   
6868 O O   . HOH   E .   ? 0.4969 0.3422 0.4690 -0.0131 0.2184  0.0612  510 HOH   A O   
6869 O O   . HOH   E .   ? 0.2999 0.2128 0.5977 0.0070  0.0350  0.1005  511 HOH   A O   
6870 O O   B HOH   E .   ? 0.4944 0.4844 0.3742 -0.1031 -0.0199 0.0411  512 HOH   A O   
6871 O O   . HOH   E .   ? 0.6989 0.2451 0.4709 -0.0676 0.0228  0.0503  513 HOH   A O   
6872 O O   B HOH   E .   ? 0.1669 0.2073 0.2515 -0.0116 0.0063  0.0181  514 HOH   A O   
6873 O O   . HOH   E .   ? 0.6732 0.5923 0.5082 0.1952  -0.1470 -0.0123 515 HOH   A O   
6874 O O   . HOH   E .   ? 0.4898 0.2673 0.4051 -0.1393 -0.0019 0.0208  516 HOH   A O   
6875 O O   . HOH   E .   ? 0.2771 0.4476 0.3247 0.1304  -0.0432 0.0450  517 HOH   A O   
6876 O O   . HOH   E .   ? 0.3981 0.8470 0.6226 -0.0719 -0.0759 0.1686  518 HOH   A O   
6877 O O   . HOH   E .   ? 0.2958 0.3845 0.4879 0.0623  -0.0711 0.0038  519 HOH   A O   
6878 O O   B HOH   E .   ? 0.1959 0.2766 0.2946 0.0278  0.0597  0.0181  520 HOH   A O   
6879 O O   . HOH   E .   ? 0.7370 0.4666 0.6585 0.0710  -0.0960 0.1074  521 HOH   A O   
6880 O O   . HOH   E .   ? 0.5793 0.7398 0.4816 0.0754  -0.0644 0.0794  522 HOH   A O   
6881 O O   B HOH   E .   ? 0.2829 0.3506 0.3544 -0.0174 -0.0053 -0.0860 523 HOH   A O   
6882 O O   . HOH   E .   ? 0.3097 0.2679 0.5010 0.0257  0.0496  0.1015  524 HOH   A O   
6883 O O   . HOH   E .   ? 0.4873 0.7119 0.5046 0.3019  -0.0213 0.1425  525 HOH   A O   
6884 O O   B HOH   E .   ? 0.4835 0.3892 0.3756 0.1703  -0.0708 0.0096  526 HOH   A O   
6885 O O   B HOH   E .   ? 0.3124 0.1832 0.3941 0.0287  -0.0792 0.0009  527 HOH   A O   
6886 O O   A HOH   E .   ? 0.4109 0.4116 0.3404 -0.0274 -0.0732 -0.1128 528 HOH   A O   
6887 O O   T HOH   E .   ? 0.1136 0.1235 0.1776 -0.0311 -0.0298 0.0431  529 HOH   A O   
6888 O O   A HOH   E .   ? 0.4320 0.7650 0.4150 0.1275  0.0396  -0.0935 530 HOH   A O   
6889 O O   . HOH   E .   ? 0.3157 0.7216 0.4214 0.0899  0.0235  -0.0875 531 HOH   A O   
6890 O O   . HOH   E .   ? 0.5741 0.5047 0.5272 0.1517  0.0189  0.1061  532 HOH   A O   
6891 O O   . HOH   E .   ? 0.4991 0.6582 0.4723 -0.0952 -0.0134 0.0146  533 HOH   A O   
6892 O O   . HOH   E .   ? 0.3445 0.4994 0.6057 -0.0340 -0.1139 0.3052  534 HOH   A O   
6893 O O   . HOH   F .   ? 0.2506 0.2259 0.3361 0.0159  0.0735  0.0343  201 HOH   B O   
6894 O O   . HOH   F .   ? 0.4518 0.3139 0.3908 -0.0424 0.0160  -0.1187 202 HOH   B O   
6895 O O   . HOH   F .   ? 0.4338 0.4599 0.3507 -0.0187 0.0033  -0.1315 203 HOH   B O   
6896 O O   . HOH   F .   ? 0.4066 0.4410 0.5702 -0.0818 -0.0109 -0.1238 204 HOH   B O   
6897 O O   . HOH   F .   ? 0.7060 0.5930 0.6376 0.2420  0.0216  -0.0422 205 HOH   B O   
6898 O O   . HOH   F .   ? 0.3529 0.3969 0.5777 -0.0777 0.0150  -0.0572 206 HOH   B O   
6899 O O   . HOH   F .   ? 0.3437 0.6750 0.3850 0.0460  0.0200  0.2398  207 HOH   B O   
6900 O O   . HOH   F .   ? 0.4419 0.5257 0.4081 0.2424  -0.0856 -0.0164 208 HOH   B O   
6901 O O   . HOH   F .   ? 0.7120 0.3499 0.4145 0.0422  0.0924  0.0145  209 HOH   B O   
6902 O O   . HOH   F .   ? 0.4474 0.3746 0.6460 0.0228  -0.1212 0.2377  210 HOH   B O   
6903 O O   . HOH   F .   ? 0.5120 0.6043 0.4377 0.3035  -0.1303 -0.0409 211 HOH   B O   
6904 O O   . HOH   F .   ? 0.4394 0.4277 0.3445 0.0176  -0.1022 0.0564  212 HOH   B O   
6905 O O   . HOH   F .   ? 0.1979 0.2397 0.3160 0.0028  0.0214  -0.0277 213 HOH   B O   
6906 O O   . HOH   F .   ? 0.3033 0.2909 0.7215 0.0686  -0.1366 0.0601  214 HOH   B O   
6907 O O   . HOH   F .   ? 0.2907 0.5689 0.4789 -0.0227 0.1396  -0.1891 215 HOH   B O   
6908 O O   . HOH   F .   ? 0.3218 0.2069 0.6111 0.0075  0.2046  0.0682  216 HOH   B O   
6909 O O   . HOH   F .   ? 0.3646 0.4980 0.4782 0.2116  0.0334  -0.0248 217 HOH   B O   
6910 O O   . HOH   F .   ? 0.1686 0.1987 0.2923 -0.0147 -0.0020 -0.0006 218 HOH   B O   
6911 O O   . HOH   F .   ? 0.4220 0.6704 0.3674 0.2106  0.0042  -0.0012 219 HOH   B O   
6912 O O   . HOH   F .   ? 0.4762 0.4694 0.6334 -0.0282 -0.1546 -0.0733 220 HOH   B O   
6913 O O   . HOH   F .   ? 0.3298 0.3541 0.5487 0.0517  -0.0029 -0.0194 221 HOH   B O   
6914 O O   . HOH   F .   ? 0.3156 0.3096 0.6316 -0.0022 0.0898  0.0101  222 HOH   B O   
6915 O O   . HOH   F .   ? 0.3206 0.2416 0.4727 -0.0166 0.1589  0.0019  223 HOH   B O   
6916 O O   . HOH   F .   ? 0.4797 0.3171 0.3597 -0.0722 -0.0227 -0.0511 224 HOH   B O   
6917 O O   . HOH   F .   ? 0.1830 0.2080 0.2965 -0.0190 0.0072  -0.0080 225 HOH   B O   
6918 O O   . HOH   F .   ? 0.4700 0.2085 0.3140 0.0043  -0.0929 0.0004  226 HOH   B O   
6919 O O   . HOH   F .   ? 0.2585 0.1913 0.2873 -0.0352 0.0954  -0.0123 227 HOH   B O   
6920 O O   . HOH   F .   ? 0.4350 0.4814 0.3790 0.0453  0.0606  -0.1504 228 HOH   B O   
6921 O O   . HOH   F .   ? 0.2278 0.2237 0.4177 -0.0360 -0.0011 -0.0659 229 HOH   B O   
6922 O O   . HOH   F .   ? 0.3800 0.4428 0.5447 -0.1743 0.0041  0.0788  230 HOH   B O   
6923 O O   . HOH   F .   ? 0.3792 0.2824 0.4159 0.0883  -0.0251 -0.0345 231 HOH   B O   
6924 O O   . HOH   F .   ? 0.5934 0.2983 0.4928 -0.1734 0.0028  0.0307  232 HOH   B O   
6925 O O   . HOH   F .   ? 0.3904 0.1849 0.2199 0.0226  -0.0868 -0.0093 233 HOH   B O   
6926 O O   . HOH   F .   ? 0.2979 0.3764 0.3243 -0.0655 0.0030  -0.0614 234 HOH   B O   
6927 O O   . HOH   F .   ? 0.1590 0.1494 0.1638 -0.0155 -0.0068 0.0001  235 HOH   B O   
6928 O O   . HOH   F .   ? 0.3745 0.2651 0.4377 0.0396  -0.0818 -0.1284 236 HOH   B O   
6929 O O   . HOH   F .   ? 0.2186 0.1348 0.3650 0.0083  -0.0511 -0.0158 237 HOH   B O   
6930 O O   . HOH   F .   ? 0.5395 0.3213 0.4061 -0.2325 -0.0048 0.0231  238 HOH   B O   
6931 O O   . HOH   F .   ? 0.2160 0.4153 0.2552 -0.0437 -0.0183 0.0487  239 HOH   B O   
6932 O O   . HOH   F .   ? 0.1532 0.1387 0.1786 -0.0006 -0.0041 0.0082  240 HOH   B O   
6933 O O   . HOH   F .   ? 0.2855 0.2369 0.3364 0.0789  0.0752  0.0077  241 HOH   B O   
6934 O O   . HOH   F .   ? 0.2310 0.4073 0.3162 -0.0584 -0.0624 -0.0436 242 HOH   B O   
6935 O O   . HOH   F .   ? 0.6636 0.6183 0.3375 0.1147  0.0222  0.0938  243 HOH   B O   
6936 O O   . HOH   F .   ? 0.3405 0.3770 0.2173 0.0286  0.0786  0.0178  244 HOH   B O   
6937 O O   . HOH   F .   ? 0.2978 0.4134 0.3572 -0.1069 -0.0204 -0.0646 245 HOH   B O   
6938 O O   . HOH   F .   ? 0.1644 0.1547 0.2909 -0.0104 -0.0030 -0.0064 246 HOH   B O   
6939 O O   . HOH   F .   ? 0.3081 0.2667 0.3030 0.0474  0.0154  -0.0873 247 HOH   B O   
6940 O O   . HOH   F .   ? 0.2202 0.2476 0.3057 -0.0573 0.0018  -0.0245 248 HOH   B O   
6941 O O   . HOH   F .   ? 0.2360 0.2045 0.2276 -0.0366 -0.0516 0.0209  249 HOH   B O   
6942 O O   . HOH   F .   ? 0.3265 0.1787 0.6508 -0.0193 -0.1120 -0.0214 250 HOH   B O   
6943 O O   . HOH   F .   ? 0.2400 0.5354 0.5617 0.1211  -0.0841 -0.1044 251 HOH   B O   
6944 O O   . HOH   F .   ? 0.2513 0.2283 0.2666 0.0745  -0.0795 -0.0626 252 HOH   B O   
6945 O O   . HOH   F .   ? 0.6289 0.3869 0.2442 -0.0185 0.0505  0.0102  253 HOH   B O   
6946 O O   . HOH   F .   ? 0.2374 0.1968 0.3820 -0.0051 -0.0627 -0.0339 254 HOH   B O   
6947 O O   . HOH   F .   ? 0.3832 0.3233 0.2759 0.0458  0.0921  0.0588  255 HOH   B O   
6948 O O   . HOH   F .   ? 0.3406 0.2625 0.3104 -0.0325 0.0195  -0.0629 256 HOH   B O   
6949 O O   . HOH   F .   ? 0.3459 0.4358 0.3602 -0.0148 -0.1227 0.0643  257 HOH   B O   
6950 O O   . HOH   F .   ? 0.2166 0.1606 0.2255 -0.0296 -0.0326 0.0264  258 HOH   B O   
6951 O O   . HOH   F .   ? 0.2574 0.2238 0.2006 0.0080  -0.0214 0.0013  259 HOH   B O   
6952 O O   . HOH   F .   ? 0.6940 0.5129 0.4548 0.2126  -0.0386 -0.1407 260 HOH   B O   
6953 O O   . HOH   F .   ? 0.2679 0.2963 0.2447 -0.0353 -0.0789 0.0167  261 HOH   B O   
6954 O O   . HOH   F .   ? 0.1731 0.1789 0.3119 -0.0248 -0.0162 0.0095  262 HOH   B O   
6955 O O   . HOH   F .   ? 0.1500 0.1697 0.2249 -0.0076 0.0078  0.0057  263 HOH   B O   
6956 O O   . HOH   F .   ? 0.2388 0.3333 0.2148 -0.0679 0.0106  0.0461  264 HOH   B O   
6957 O O   . HOH   F .   ? 0.4095 0.2933 0.4731 -0.0235 -0.0986 -0.0751 265 HOH   B O   
6958 O O   . HOH   F .   ? 0.2338 0.3792 0.3218 -0.0441 0.0284  -0.1281 266 HOH   B O   
6959 O O   . HOH   F .   ? 0.2740 0.2068 0.3043 -0.0706 0.0135  -0.0111 267 HOH   B O   
6960 O O   . HOH   F .   ? 0.2462 0.2093 0.2192 0.0175  -0.0038 -0.0094 268 HOH   B O   
6961 O O   . HOH   F .   ? 0.2856 0.2179 0.4863 0.0082  0.0373  0.0413  269 HOH   B O   
6962 O O   . HOH   F .   ? 0.1907 0.1392 0.4311 -0.0100 -0.0287 -0.0146 270 HOH   B O   
6963 O O   . HOH   F .   ? 0.3824 0.3598 0.4913 0.1307  -0.0868 -0.0867 271 HOH   B O   
6964 O O   . HOH   F .   ? 0.2457 0.3759 0.2250 0.1146  -0.0259 -0.0222 272 HOH   B O   
6965 O O   . HOH   F .   ? 0.3562 0.3392 0.5173 0.0414  0.0108  -0.0086 273 HOH   B O   
6966 O O   . HOH   F .   ? 0.4643 0.3708 0.2787 0.0497  -0.0165 -0.0947 274 HOH   B O   
6967 O O   . HOH   F .   ? 0.2557 0.3885 0.3655 0.0118  0.1079  0.0159  275 HOH   B O   
6968 O O   . HOH   F .   ? 0.2395 0.2626 0.2305 -0.0382 -0.0597 -0.0274 276 HOH   B O   
6969 O O   . HOH   F .   ? 0.2093 0.1604 0.2424 -0.0240 -0.0174 0.0170  277 HOH   B O   
6970 O O   . HOH   F .   ? 0.2771 0.4620 0.6374 0.0400  -0.0193 -0.0910 278 HOH   B O   
6971 O O   . HOH   F .   ? 0.2239 0.5058 0.4960 -0.0498 -0.0590 -0.1401 279 HOH   B O   
6972 O O   . HOH   F .   ? 0.1940 0.1891 0.1870 -0.0496 -0.0430 0.0073  280 HOH   B O   
6973 O O   . HOH   F .   ? 0.5818 0.3844 0.3183 0.2624  0.1199  0.0887  281 HOH   B O   
6974 O O   . HOH   F .   ? 0.1755 0.1663 0.3613 -0.0088 0.0018  -0.0056 282 HOH   B O   
6975 O O   . HOH   F .   ? 0.1778 0.1629 0.1999 -0.0000 0.0032  0.0066  283 HOH   B O   
6976 O O   . HOH   F .   ? 0.3470 0.2724 0.2160 0.0057  -0.0742 -0.0015 284 HOH   B O   
6977 O O   . HOH   F .   ? 0.2742 0.4883 0.4476 -0.1065 -0.1107 0.0763  285 HOH   B O   
6978 O O   . HOH   F .   ? 0.1735 0.2050 0.3068 0.0223  -0.0054 0.0093  286 HOH   B O   
6979 O O   . HOH   F .   ? 0.1712 0.2021 0.1786 -0.0157 -0.0164 0.0039  287 HOH   B O   
6980 O O   . HOH   F .   ? 0.4427 0.7522 0.3623 0.1961  -0.0789 0.0808  288 HOH   B O   
6981 O O   . HOH   F .   ? 0.1852 0.3286 0.5282 0.0278  0.0105  -0.1179 289 HOH   B O   
6982 O O   . HOH   F .   ? 0.2933 0.7478 0.7101 0.1105  -0.0689 -0.0826 290 HOH   B O   
6983 O O   . HOH   F .   ? 0.2527 0.2721 0.2893 0.0123  -0.0738 0.0203  291 HOH   B O   
6984 O O   . HOH   F .   ? 0.2131 0.2928 0.5957 0.0416  -0.0437 -0.1152 292 HOH   B O   
6985 O O   . HOH   F .   ? 0.3778 0.2276 0.3892 -0.0937 -0.1941 0.0848  293 HOH   B O   
6986 O O   . HOH   F .   ? 0.6174 0.6117 0.5227 0.2872  -0.0338 -0.0317 294 HOH   B O   
6987 O O   . HOH   F .   ? 0.2730 0.6579 0.2379 0.0651  -0.0308 -0.0385 295 HOH   B O   
6988 O O   . HOH   F .   ? 0.3420 0.2766 0.5180 -0.0237 -0.0650 0.1141  296 HOH   B O   
6989 O O   . HOH   F .   ? 0.4816 0.3871 0.2351 0.1159  -0.0986 0.0381  297 HOH   B O   
6990 O O   . HOH   F .   ? 0.4828 0.4448 0.2248 -0.0114 0.0916  0.0592  298 HOH   B O   
6991 O O   . HOH   F .   ? 0.3517 0.2952 0.2777 -0.0282 0.0145  -0.1181 299 HOH   B O   
6992 O O   . HOH   F .   ? 0.1844 0.1710 0.2617 0.0040  0.0075  0.0188  300 HOH   B O   
6993 O O   . HOH   F .   ? 0.4570 0.4956 0.5112 0.0363  -0.1399 0.0367  301 HOH   B O   
6994 O O   . HOH   F .   ? 0.3118 0.4152 0.4130 -0.1366 0.1200  -0.1030 302 HOH   B O   
6995 O O   . HOH   F .   ? 0.3384 0.2057 0.3515 0.0711  0.1243  0.0533  303 HOH   B O   
6996 O O   . HOH   F .   ? 0.2287 0.1681 0.2761 -0.0284 -0.0198 0.0017  304 HOH   B O   
6997 O O   . HOH   F .   ? 0.5060 0.3023 0.2598 -0.1750 0.0710  -0.0181 305 HOH   B O   
6998 O O   . HOH   F .   ? 0.2177 0.1689 0.3532 0.0339  -0.0925 -0.0058 306 HOH   B O   
6999 O O   . HOH   F .   ? 0.4841 0.4917 0.2650 0.1463  -0.0819 -0.0271 307 HOH   B O   
7000 O O   . HOH   F .   ? 0.2512 0.1581 0.2649 -0.0175 -0.0303 0.0268  308 HOH   B O   
7001 O O   . HOH   F .   ? 0.1675 0.1579 0.3387 0.0092  -0.0056 -0.0019 309 HOH   B O   
7002 O O   . HOH   F .   ? 0.4329 0.3719 0.5097 -0.0840 -0.0000 0.1728  310 HOH   B O   
7003 O O   . HOH   F .   ? 0.1625 0.1900 0.3135 -0.0266 -0.0012 0.0126  311 HOH   B O   
7004 O O   . HOH   F .   ? 0.2279 0.6097 0.5220 -0.0410 0.0139  0.0109  312 HOH   B O   
7005 O O   . HOH   F .   ? 0.3002 0.3108 0.3766 -0.0488 0.1119  -0.1008 313 HOH   B O   
7006 O O   . HOH   F .   ? 0.4560 0.7040 0.2647 -0.0345 -0.1119 0.0354  314 HOH   B O   
7007 O O   . HOH   F .   ? 0.2238 0.3373 0.5034 -0.0145 -0.0624 -0.0271 315 HOH   B O   
7008 O O   . HOH   F .   ? 0.4511 0.2432 0.2750 0.1674  0.1107  0.0438  316 HOH   B O   
7009 O O   . HOH   F .   ? 0.4236 0.4010 0.5697 0.0435  -0.0067 0.0520  317 HOH   B O   
7010 O O   . HOH   F .   ? 0.3628 0.3723 0.7392 0.0078  -0.0977 0.1764  318 HOH   B O   
7011 O O   . HOH   F .   ? 0.6110 0.5785 0.5147 -0.1192 -0.0702 0.1553  319 HOH   B O   
7012 O O   . HOH   F .   ? 0.2254 0.2069 0.2067 -0.0106 0.0103  0.0216  320 HOH   B O   
7013 O O   . HOH   F .   ? 0.5032 0.4406 0.2975 0.0325  -0.0641 -0.0841 321 HOH   B O   
7014 O O   . HOH   F .   ? 0.4591 0.2565 0.3286 0.0283  0.0176  0.0787  322 HOH   B O   
7015 O O   . HOH   F .   ? 0.1758 0.2953 0.2421 -0.0124 -0.0220 0.0678  323 HOH   B O   
7016 O O   . HOH   F .   ? 0.1651 0.1731 0.3303 -0.0116 -0.0145 -0.0111 324 HOH   B O   
7017 O O   . HOH   F .   ? 0.2863 0.3431 0.4777 -0.0589 -0.1374 0.1328  325 HOH   B O   
7018 O O   . HOH   F .   ? 0.3114 0.2323 0.2459 0.0158  -0.0184 0.0293  326 HOH   B O   
7019 O O   . HOH   F .   ? 0.6103 0.4686 0.6991 0.1222  -0.1087 0.1882  327 HOH   B O   
7020 O O   . HOH   F .   ? 0.6444 0.4700 0.5933 0.1545  0.1650  0.0255  328 HOH   B O   
7021 O O   . HOH   F .   ? 0.1968 0.2033 0.2932 0.0305  0.0371  0.0218  329 HOH   B O   
7022 O O   . HOH   F .   ? 0.8007 0.2249 0.3145 0.0435  -0.0996 0.0142  330 HOH   B O   
7023 O O   . HOH   F .   ? 0.2682 0.2097 0.6020 -0.0109 -0.0161 0.0282  331 HOH   B O   
7024 O O   . HOH   F .   ? 0.2241 0.2407 0.5516 -0.0555 0.0047  0.1346  332 HOH   B O   
7025 O O   . HOH   F .   ? 0.4305 0.3155 0.5334 0.0938  0.1964  0.1676  333 HOH   B O   
7026 O O   . HOH   F .   ? 0.5666 0.3539 0.3733 -0.0009 0.0931  0.1061  334 HOH   B O   
7027 O O   . HOH   F .   ? 0.1880 0.2753 0.3052 0.0225  -0.0142 -0.0533 335 HOH   B O   
7028 O O   . HOH   F .   ? 0.1815 0.1550 0.2631 0.0076  -0.0225 0.0069  336 HOH   B O   
7029 O O   . HOH   F .   ? 0.5231 0.3470 0.4364 0.0295  0.0511  -0.1477 337 HOH   B O   
7030 O O   . HOH   F .   ? 0.6121 0.4435 0.6067 -0.0982 -0.1117 -0.0899 338 HOH   B O   
7031 O O   . HOH   F .   ? 0.5515 0.3231 0.3039 0.0438  -0.1315 -0.0717 339 HOH   B O   
7032 O O   . HOH   F .   ? 0.4246 0.7506 0.3802 0.0076  -0.0557 0.1615  340 HOH   B O   
7033 O O   . HOH   F .   ? 0.5244 0.4753 0.3807 0.0032  -0.1254 0.0008  341 HOH   B O   
7034 O O   . HOH   F .   ? 0.2133 0.6077 0.6644 -0.0286 -0.0968 0.1040  342 HOH   B O   
7035 O O   . HOH   F .   ? 0.3850 0.6517 0.3841 -0.1285 -0.0778 -0.0750 343 HOH   B O   
7036 O O   . HOH   F .   ? 0.2200 0.1970 0.3713 -0.0174 0.0675  -0.0055 344 HOH   B O   
7037 O O   . HOH   F .   ? 0.7476 0.6361 0.3217 0.0514  -0.0440 0.1212  345 HOH   B O   
7038 O O   . HOH   F .   ? 0.2986 0.2009 0.3830 0.0367  -0.1030 -0.0569 346 HOH   B O   
7039 O O   . HOH   F .   ? 0.4154 0.5630 0.5741 -0.0034 -0.1137 0.1018  347 HOH   B O   
7040 O O   . HOH   F .   ? 0.4983 0.5739 0.4590 -0.1208 0.0311  0.1489  348 HOH   B O   
7041 O O   . HOH   F .   ? 0.2849 0.2322 0.4825 -0.0219 -0.0828 -0.0476 349 HOH   B O   
7042 O O   . HOH   F .   ? 0.4579 0.6122 0.6988 0.0272  0.0306  0.0218  350 HOH   B O   
7043 O O   . HOH   F .   ? 0.2464 0.6122 0.4400 0.1537  -0.0757 -0.1420 351 HOH   B O   
7044 O O   . HOH   F .   ? 0.2301 0.4147 0.5079 0.0200  0.0153  0.0300  352 HOH   B O   
7045 O O   . HOH   F .   ? 0.4216 0.2245 0.3574 -0.0823 0.0641  -0.0850 353 HOH   B O   
7046 O O   . HOH   F .   ? 0.5113 0.3705 0.5149 -0.1240 0.1185  0.1000  354 HOH   B O   
7047 O O   . HOH   F .   ? 0.3474 0.4278 0.4895 -0.1586 -0.0038 -0.0222 355 HOH   B O   
7048 O O   . HOH   F .   ? 0.4592 0.3751 0.4019 0.0342  0.0835  -0.0498 356 HOH   B O   
7049 O O   . HOH   F .   ? 0.3970 0.3046 0.3541 -0.1203 -0.0137 -0.0559 357 HOH   B O   
7050 O O   . HOH   F .   ? 0.4798 0.5571 0.4795 0.1811  -0.1145 0.1288  358 HOH   B O   
7051 O O   . HOH   F .   ? 0.4791 0.5050 0.5696 0.0058  0.0562  0.0877  359 HOH   B O   
7052 O O   . HOH   F .   ? 0.5277 0.4054 0.6019 0.0328  0.1045  0.1530  360 HOH   B O   
7053 O O   . HOH   F .   ? 0.5459 0.3609 0.4745 0.0004  -0.1536 -0.0596 361 HOH   B O   
7054 O O   . HOH   F .   ? 0.5027 0.6402 0.3584 0.2147  -0.0186 0.0535  362 HOH   B O   
7055 O O   . HOH   F .   ? 0.2400 0.4168 0.6465 -0.0989 -0.0602 -0.0875 363 HOH   B O   
7056 O O   . HOH   F .   ? 0.5842 0.4651 0.4485 0.1038  0.0905  0.0637  364 HOH   B O   
7057 O O   . HOH   F .   ? 0.5021 0.3084 0.5310 -0.1313 -0.0521 0.0181  365 HOH   B O   
7058 O O   . HOH   F .   ? 0.6134 0.2224 0.4344 -0.0097 0.0132  0.0580  366 HOH   B O   
7059 O O   . HOH   F .   ? 0.5010 0.5791 0.4561 -0.0877 -0.0710 -0.0922 367 HOH   B O   
7060 O O   . HOH   F .   ? 0.5430 0.5863 0.3616 0.1969  -0.1293 0.0864  368 HOH   B O   
7061 O O   . HOH   F .   ? 0.5296 0.3807 0.5733 0.0878  -0.1528 0.0627  369 HOH   B O   
7062 O O   . HOH   F .   ? 0.4407 0.5843 0.5282 0.2704  0.0954  0.1299  370 HOH   B O   
7063 O O   . HOH   F .   ? 0.8455 0.7798 0.5611 0.2611  -0.1402 0.0450  371 HOH   B O   
7064 O O   . HOH   F .   ? 0.5124 0.3134 0.4066 0.0913  -0.1517 -0.0535 372 HOH   B O   
7065 O O   . HOH   F .   ? 0.6187 0.3740 0.2780 -0.1180 -0.0844 -0.0230 373 HOH   B O   
7066 O O   . HOH   F .   ? 0.5069 0.6722 0.5869 0.1696  0.0345  0.2500  374 HOH   B O   
7067 O O   . HOH   F .   ? 0.4569 0.5054 0.4704 -0.1087 -0.0338 0.0700  375 HOH   B O   
7068 O O   . HOH   F .   ? 0.2468 0.4376 0.4719 0.0365  -0.0627 -0.0932 376 HOH   B O   
7069 O O   . HOH   F .   ? 0.3639 0.4735 0.2160 0.0202  0.0244  0.0033  377 HOH   B O   
7070 O O   . HOH   F .   ? 0.5441 0.7099 0.4306 -0.1363 -0.0141 -0.1414 378 HOH   B O   
7071 O O   . HOH   F .   ? 0.3697 0.5486 0.5306 0.1119  0.0054  0.0675  379 HOH   B O   
7072 O O   . HOH   F .   ? 0.6342 0.3648 0.5335 -0.0724 -0.0749 0.0017  380 HOH   B O   
7073 O O   . HOH   F .   ? 0.5666 0.6990 0.6707 0.0191  0.2064  0.1986  381 HOH   B O   
7074 O O   . HOH   F .   ? 0.3224 0.2625 0.3231 0.0118  0.0199  0.0225  382 HOH   B O   
7075 O O   . HOH   F .   ? 0.4082 0.8002 0.5505 0.0780  0.1807  0.0896  383 HOH   B O   
7076 O O   . HOH   F .   ? 0.6964 0.4169 0.4609 0.0938  0.0789  -0.0983 384 HOH   B O   
7077 O O   . HOH   F .   ? 0.5717 0.4901 0.4771 0.0529  -0.0656 -0.0444 385 HOH   B O   
7078 O O   . HOH   F .   ? 0.6655 0.4430 0.5241 -0.1037 0.0431  -0.0475 386 HOH   B O   
7079 O O   . HOH   F .   ? 0.7151 0.5551 0.4547 0.2382  0.0660  0.0403  387 HOH   B O   
7080 O O   . HOH   F .   ? 0.2582 0.4242 0.3992 -0.0691 -0.1011 -0.0102 388 HOH   B O   
7081 O O   . HOH   F .   ? 0.4743 0.4042 0.3895 -0.0122 0.0587  -0.0179 389 HOH   B O   
7082 O O   . HOH   F .   ? 0.4021 0.2402 0.3275 0.0862  -0.0303 0.0040  390 HOH   B O   
7083 O O   . HOH   F .   ? 0.4556 0.4159 0.5063 0.0085  0.0586  0.0590  391 HOH   B O   
7084 O O   . HOH   F .   ? 0.4032 0.2362 0.5361 -0.0354 0.0703  0.0576  392 HOH   B O   
7085 O O   . HOH   F .   ? 0.2504 0.3742 0.6746 -0.1017 -0.0762 0.0108  393 HOH   B O   
7086 O O   . HOH   F .   ? 0.4215 0.4578 0.4382 0.0189  0.0813  0.0804  394 HOH   B O   
7087 O O   . HOH   F .   ? 0.4818 0.6701 0.4228 0.1386  0.0262  -0.0982 395 HOH   B O   
7088 O O   . HOH   F .   ? 0.3356 0.3706 0.4041 0.0235  0.0232  -0.0481 396 HOH   B O   
7089 O O   . HOH   F .   ? 0.2290 0.2927 0.6245 -0.0681 -0.0970 0.0624  397 HOH   B O   
7090 O O   . HOH   F .   ? 0.6168 0.6614 0.7376 0.1808  -0.1072 0.2243  398 HOH   B O   
7091 O O   . HOH   F .   ? 0.6050 0.3872 0.2911 -0.2289 -0.0545 0.0825  399 HOH   B O   
7092 O O   . HOH   F .   ? 0.5563 0.6163 0.3682 0.1846  -0.0323 -0.0497 400 HOH   B O   
# 
