data_9GTJ
# 
_entry.id   9GTJ 
# 
_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   9GTJ         pdb_00009gtj 10.2210/pdb9gtj/pdb 
WWPDB D_1292130109 ?            ?                   
# 
_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.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GTJ 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-18 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              anapap@utu.fi 
_pdbx_contact_author.name_first         ANASTASSIOS 
_pdbx_contact_author.name_last          PAPAGEORGIOU 
_pdbx_contact_author.name_mi            C. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7980-1120 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Papageorgiou, A.C.' 1 0000-0002-7980-1120 
'Chronopoulou, E.G.' 2 0000-0001-7269-2817 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Febs J.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1742-464X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Biochemical and structural characterization of chlorite dismutase enzyme from Pseudomonas aeruginosa.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1111/febs.70151 
_citation.pdbx_database_id_PubMed   40458033 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Nokas, D.V.'           1 ?                   
primary 'Panagiotopoulou, E.K.' 2 0009-0006-8737-1489 
primary 'Kapogiannatos, A.I.'   3 ?                   
primary 'Premetis, G.E.'        4 ?                   
primary 'Labrou, N.E.'          5 0000-0003-1925-9867 
primary 'Efthimiadou, E.K.'     6 ?                   
primary 'Papageorgiou, A.C.'    7 ?                   
primary 'Chronopoulou, E.G.'    8 0000-0001-7269-2817 
# 
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 'Chlorite dismutase'              22114.059 2   ? ? ? ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487   2   ? ? ? ? 
3 non-polymer syn IMIDAZOLE                         69.085    2   ? ? ? ? 
4 non-polymer syn 'SODIUM ION'                      22.990    6   ? ? ? ? 
5 non-polymer syn 'CHLORIDE ION'                    35.453    1   ? ? ? ? 
6 water       nat water                             18.015    741 ? ? ? ? 
# 
_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       
;MNTRVFTFAGGETGVWRVVAMNAVAGAPLPGIPRLNVAAGSVSPQPPGTKWLLRGITSNERYVVREEKDRLVAKQPSLGR
AEATCAALIPIRKNPSWWGLSQDERRKIFEEQSRHIHIGLQYLPAVARRLHHCRDLGENEPFDFLTWFEYSPSDETAFNR
LLAELRASVEWQYVDREIDIRLVHEPAHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MNTRVFTFAGGETGVWRVVAMNAVAGAPLPGIPRLNVAAGSVSPQPPGTKWLLRGITSNERYVVREEKDRLVAKQPSLGR
AEATCAALIPIRKNPSWWGLSQDERRKIFEEQSRHIHIGLQYLPAVARRLHHCRDLGENEPFDFLTWFEYSPSDETAFNR
LLAELRASVEWQYVDREIDIRLVHEPAHHHHHH
;
_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 'PROTOPORPHYRIN IX CONTAINING FE' HEM 
3 IMIDAZOLE                         IMD 
4 'SODIUM ION'                      NA  
5 'CHLORIDE ION'                    CL  
6 water                             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASN n 
1 3   THR n 
1 4   ARG n 
1 5   VAL n 
1 6   PHE n 
1 7   THR n 
1 8   PHE n 
1 9   ALA n 
1 10  GLY n 
1 11  GLY n 
1 12  GLU n 
1 13  THR n 
1 14  GLY n 
1 15  VAL n 
1 16  TRP n 
1 17  ARG n 
1 18  VAL n 
1 19  VAL n 
1 20  ALA n 
1 21  MET n 
1 22  ASN n 
1 23  ALA n 
1 24  VAL n 
1 25  ALA n 
1 26  GLY n 
1 27  ALA n 
1 28  PRO n 
1 29  LEU n 
1 30  PRO n 
1 31  GLY n 
1 32  ILE n 
1 33  PRO n 
1 34  ARG n 
1 35  LEU n 
1 36  ASN n 
1 37  VAL n 
1 38  ALA n 
1 39  ALA n 
1 40  GLY n 
1 41  SER n 
1 42  VAL n 
1 43  SER n 
1 44  PRO n 
1 45  GLN n 
1 46  PRO n 
1 47  PRO n 
1 48  GLY n 
1 49  THR n 
1 50  LYS n 
1 51  TRP n 
1 52  LEU n 
1 53  LEU n 
1 54  ARG n 
1 55  GLY n 
1 56  ILE n 
1 57  THR n 
1 58  SER n 
1 59  ASN n 
1 60  GLU n 
1 61  ARG n 
1 62  TYR n 
1 63  VAL n 
1 64  VAL n 
1 65  ARG n 
1 66  GLU n 
1 67  GLU n 
1 68  LYS n 
1 69  ASP n 
1 70  ARG n 
1 71  LEU n 
1 72  VAL n 
1 73  ALA n 
1 74  LYS n 
1 75  GLN n 
1 76  PRO n 
1 77  SER n 
1 78  LEU n 
1 79  GLY n 
1 80  ARG n 
1 81  ALA n 
1 82  GLU n 
1 83  ALA n 
1 84  THR n 
1 85  CYS n 
1 86  ALA n 
1 87  ALA n 
1 88  LEU n 
1 89  ILE n 
1 90  PRO n 
1 91  ILE n 
1 92  ARG n 
1 93  LYS n 
1 94  ASN n 
1 95  PRO n 
1 96  SER n 
1 97  TRP n 
1 98  TRP n 
1 99  GLY n 
1 100 LEU n 
1 101 SER n 
1 102 GLN n 
1 103 ASP n 
1 104 GLU n 
1 105 ARG n 
1 106 ARG n 
1 107 LYS n 
1 108 ILE n 
1 109 PHE n 
1 110 GLU n 
1 111 GLU n 
1 112 GLN n 
1 113 SER n 
1 114 ARG n 
1 115 HIS n 
1 116 ILE n 
1 117 HIS n 
1 118 ILE n 
1 119 GLY n 
1 120 LEU n 
1 121 GLN n 
1 122 TYR n 
1 123 LEU n 
1 124 PRO n 
1 125 ALA n 
1 126 VAL n 
1 127 ALA n 
1 128 ARG n 
1 129 ARG n 
1 130 LEU n 
1 131 HIS n 
1 132 HIS n 
1 133 CYS n 
1 134 ARG n 
1 135 ASP n 
1 136 LEU n 
1 137 GLY n 
1 138 GLU n 
1 139 ASN n 
1 140 GLU n 
1 141 PRO n 
1 142 PHE n 
1 143 ASP n 
1 144 PHE n 
1 145 LEU n 
1 146 THR n 
1 147 TRP n 
1 148 PHE n 
1 149 GLU n 
1 150 TYR n 
1 151 SER n 
1 152 PRO n 
1 153 SER n 
1 154 ASP n 
1 155 GLU n 
1 156 THR n 
1 157 ALA n 
1 158 PHE n 
1 159 ASN n 
1 160 ARG n 
1 161 LEU n 
1 162 LEU n 
1 163 ALA n 
1 164 GLU n 
1 165 LEU n 
1 166 ARG n 
1 167 ALA n 
1 168 SER n 
1 169 VAL n 
1 170 GLU n 
1 171 TRP n 
1 172 GLN n 
1 173 TYR n 
1 174 VAL n 
1 175 ASP n 
1 176 ARG n 
1 177 GLU n 
1 178 ILE n 
1 179 ASP n 
1 180 ILE n 
1 181 ARG n 
1 182 LEU n 
1 183 VAL n 
1 184 HIS n 
1 185 GLU n 
1 186 PRO n 
1 187 ALA n 
1 188 HIS n 
1 189 HIS n 
1 190 HIS n 
1 191 HIS n 
1 192 HIS n 
1 193 HIS 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                   193 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SAMN05216605_1413 
_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      Pseudomonas 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     286 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_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 
ALA 'L-peptide linking' y ALANINE                           ?    'C3 H7 N O2'       89.093  
ARG 'L-peptide linking' y ARGININE                          ?    'C6 H15 N4 O2 1'   175.209 
ASN 'L-peptide linking' y ASPARAGINE                        ?    'C4 H8 N2 O3'      132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                   ?    'C4 H7 N O4'       133.103 
CL  non-polymer         . 'CHLORIDE ION'                    ?    'Cl -1'            35.453  
CYS 'L-peptide linking' y CYSTEINE                          ?    'C3 H7 N O2 S'     121.158 
GLN 'L-peptide linking' y GLUTAMINE                         ?    'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                   ?    'C5 H9 N O4'       147.129 
GLY 'peptide linking'   y GLYCINE                           ?    'C2 H5 N O2'       75.067  
HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE' HEME 'C34 H32 Fe N4 O4' 616.487 
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 
IMD non-polymer         . IMIDAZOLE                         ?    'C3 H5 N2 1'       69.085  
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 
NA  non-polymer         . 'SODIUM ION'                      ?    'Na 1'             22.990  
PHE 'L-peptide linking' y PHENYLALANINE                     ?    'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                           ?    'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                            ?    'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE                         ?    'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                        ?    'C11 H12 N2 O2'    204.225 
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   MET 1   1   1   MET MET A . n 
A 1 2   ASN 2   2   2   ASN ASN A . n 
A 1 3   THR 3   3   3   THR THR A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   THR 7   7   7   THR THR A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   ALA 9   9   9   ALA ALA A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  GLU 12  12  12  GLU GLU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  GLY 14  14  14  GLY GLY A . n 
A 1 15  VAL 15  15  15  VAL VAL A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  ARG 17  17  17  ARG ARG A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  VAL 19  19  19  VAL VAL A . n 
A 1 20  ALA 20  20  20  ALA ALA A . n 
A 1 21  MET 21  21  21  MET MET A . n 
A 1 22  ASN 22  22  22  ASN ASN A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  GLY 31  31  31  GLY GLY A . n 
A 1 32  ILE 32  32  32  ILE ILE A . n 
A 1 33  PRO 33  33  33  PRO PRO A . n 
A 1 34  ARG 34  34  34  ARG ARG A . n 
A 1 35  LEU 35  35  35  LEU LEU A . n 
A 1 36  ASN 36  36  36  ASN ASN A . n 
A 1 37  VAL 37  37  37  VAL VAL 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  GLY 40  40  40  GLY GLY A . n 
A 1 41  SER 41  41  41  SER SER A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  PRO 44  44  44  PRO PRO A . n 
A 1 45  GLN 45  45  45  GLN GLN A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  PRO 47  47  47  PRO PRO A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  THR 49  49  49  THR THR A . n 
A 1 50  LYS 50  50  50  LYS LYS A . n 
A 1 51  TRP 51  51  51  TRP TRP A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ARG 54  54  54  ARG ARG A . n 
A 1 55  GLY 55  55  55  GLY GLY A . n 
A 1 56  ILE 56  56  56  ILE ILE A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  ARG 61  61  61  ARG ARG A . n 
A 1 62  TYR 62  62  62  TYR TYR A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  VAL 64  64  64  VAL VAL A . n 
A 1 65  ARG 65  65  65  ARG ARG A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  GLU 67  67  67  GLU GLU A . n 
A 1 68  LYS 68  68  68  LYS LYS A . n 
A 1 69  ASP 69  69  69  ASP ASP A . n 
A 1 70  ARG 70  70  70  ARG ARG A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  VAL 72  72  72  VAL VAL A . n 
A 1 73  ALA 73  73  73  ALA ALA A . n 
A 1 74  LYS 74  74  74  LYS LYS A . n 
A 1 75  GLN 75  75  75  GLN GLN A . n 
A 1 76  PRO 76  76  76  PRO PRO A . n 
A 1 77  SER 77  77  77  SER SER A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  ARG 80  80  80  ARG ARG A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  GLU 82  82  82  GLU GLU A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  THR 84  84  84  THR THR A . n 
A 1 85  CYS 85  85  85  CYS CYS A . n 
A 1 86  ALA 86  86  86  ALA ALA A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ILE 89  89  89  ILE ILE A . n 
A 1 90  PRO 90  90  90  PRO PRO A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  ARG 92  92  92  ARG ARG A . n 
A 1 93  LYS 93  93  93  LYS LYS A . n 
A 1 94  ASN 94  94  94  ASN ASN A . n 
A 1 95  PRO 95  95  95  PRO PRO A . n 
A 1 96  SER 96  96  96  SER SER A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  TRP 98  98  98  TRP TRP A . n 
A 1 99  GLY 99  99  99  GLY GLY A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 SER 101 101 101 SER SER A . n 
A 1 102 GLN 102 102 102 GLN GLN A . n 
A 1 103 ASP 103 103 103 ASP ASP A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 ARG 106 106 106 ARG ARG A . n 
A 1 107 LYS 107 107 107 LYS LYS A . n 
A 1 108 ILE 108 108 108 ILE ILE A . n 
A 1 109 PHE 109 109 109 PHE PHE A . n 
A 1 110 GLU 110 110 110 GLU GLU A . n 
A 1 111 GLU 111 111 111 GLU GLU A . n 
A 1 112 GLN 112 112 112 GLN GLN A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 ARG 114 114 114 ARG ARG A . n 
A 1 115 HIS 115 115 115 HIS HIS A . n 
A 1 116 ILE 116 116 116 ILE ILE A . n 
A 1 117 HIS 117 117 117 HIS HIS A . n 
A 1 118 ILE 118 118 118 ILE ILE A . n 
A 1 119 GLY 119 119 119 GLY GLY A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 GLN 121 121 121 GLN GLN A . n 
A 1 122 TYR 122 122 122 TYR TYR A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 PRO 124 124 124 PRO PRO A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 VAL 126 126 126 VAL VAL A . n 
A 1 127 ALA 127 127 127 ALA ALA A . n 
A 1 128 ARG 128 128 128 ARG ARG A . n 
A 1 129 ARG 129 129 129 ARG ARG A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 HIS 131 131 131 HIS HIS A . n 
A 1 132 HIS 132 132 132 HIS HIS A . n 
A 1 133 CYS 133 133 133 CYS CYS A . n 
A 1 134 ARG 134 134 134 ARG ARG A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 GLY 137 137 137 GLY GLY A . n 
A 1 138 GLU 138 138 138 GLU GLU A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 GLU 140 140 140 GLU GLU A . n 
A 1 141 PRO 141 141 141 PRO PRO A . n 
A 1 142 PHE 142 142 142 PHE PHE A . n 
A 1 143 ASP 143 143 143 ASP ASP A . n 
A 1 144 PHE 144 144 144 PHE PHE A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 TRP 147 147 147 TRP TRP A . n 
A 1 148 PHE 148 148 148 PHE PHE A . n 
A 1 149 GLU 149 149 149 GLU GLU A . n 
A 1 150 TYR 150 150 150 TYR TYR A . n 
A 1 151 SER 151 151 151 SER SER A . n 
A 1 152 PRO 152 152 152 PRO PRO A . n 
A 1 153 SER 153 153 153 SER SER A . n 
A 1 154 ASP 154 154 154 ASP ASP A . n 
A 1 155 GLU 155 155 155 GLU GLU A . n 
A 1 156 THR 156 156 156 THR THR A . n 
A 1 157 ALA 157 157 157 ALA ALA A . n 
A 1 158 PHE 158 158 158 PHE PHE A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 ARG 160 160 160 ARG ARG A . n 
A 1 161 LEU 161 161 161 LEU LEU A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 ALA 163 163 163 ALA ALA A . n 
A 1 164 GLU 164 164 164 GLU GLU A . n 
A 1 165 LEU 165 165 165 LEU LEU A . n 
A 1 166 ARG 166 166 166 ARG ARG A . n 
A 1 167 ALA 167 167 167 ALA ALA A . n 
A 1 168 SER 168 168 168 SER SER A . n 
A 1 169 VAL 169 169 169 VAL VAL A . n 
A 1 170 GLU 170 170 170 GLU GLU A . n 
A 1 171 TRP 171 171 171 TRP TRP A . n 
A 1 172 GLN 172 172 172 GLN GLN A . n 
A 1 173 TYR 173 173 173 TYR TYR A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 ASP 175 175 175 ASP ASP A . n 
A 1 176 ARG 176 176 176 ARG ARG A . n 
A 1 177 GLU 177 177 177 GLU GLU A . n 
A 1 178 ILE 178 178 178 ILE ILE A . n 
A 1 179 ASP 179 179 179 ASP ASP A . n 
A 1 180 ILE 180 180 180 ILE ILE A . n 
A 1 181 ARG 181 181 181 ARG ARG A . n 
A 1 182 LEU 182 182 182 LEU LEU A . n 
A 1 183 VAL 183 183 183 VAL VAL A . n 
A 1 184 HIS 184 184 184 HIS HIS A . n 
A 1 185 GLU 185 185 185 GLU GLU A . n 
A 1 186 PRO 186 186 186 PRO PRO A . n 
A 1 187 ALA 187 187 ?   ?   ?   A . n 
A 1 188 HIS 188 188 ?   ?   ?   A . n 
A 1 189 HIS 189 189 ?   ?   ?   A . n 
A 1 190 HIS 190 190 ?   ?   ?   A . n 
A 1 191 HIS 191 191 ?   ?   ?   A . n 
A 1 192 HIS 192 192 ?   ?   ?   A . n 
A 1 193 HIS 193 193 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   ASN 2   2   ?   ?   ?   B . n 
B 1 3   THR 3   3   3   THR THR B . n 
B 1 4   ARG 4   4   4   ARG ARG B . n 
B 1 5   VAL 5   5   5   VAL VAL B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   THR 7   7   7   THR THR B . n 
B 1 8   PHE 8   8   8   PHE PHE B . n 
B 1 9   ALA 9   9   9   ALA ALA B . n 
B 1 10  GLY 10  10  10  GLY GLY B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  GLU 12  12  12  GLU GLU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  GLY 14  14  14  GLY GLY B . n 
B 1 15  VAL 15  15  15  VAL VAL B . n 
B 1 16  TRP 16  16  16  TRP TRP B . n 
B 1 17  ARG 17  17  17  ARG ARG B . n 
B 1 18  VAL 18  18  18  VAL VAL B . n 
B 1 19  VAL 19  19  19  VAL VAL B . n 
B 1 20  ALA 20  20  20  ALA ALA B . n 
B 1 21  MET 21  21  21  MET MET B . n 
B 1 22  ASN 22  22  22  ASN ASN B . n 
B 1 23  ALA 23  23  23  ALA ALA B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  ALA 25  25  25  ALA ALA B . n 
B 1 26  GLY 26  26  26  GLY GLY B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  PRO 28  28  28  PRO PRO B . n 
B 1 29  LEU 29  29  29  LEU LEU B . n 
B 1 30  PRO 30  30  30  PRO PRO B . n 
B 1 31  GLY 31  31  31  GLY GLY B . n 
B 1 32  ILE 32  32  32  ILE ILE B . n 
B 1 33  PRO 33  33  33  PRO PRO B . n 
B 1 34  ARG 34  34  34  ARG ARG B . n 
B 1 35  LEU 35  35  35  LEU LEU B . n 
B 1 36  ASN 36  36  36  ASN ASN B . n 
B 1 37  VAL 37  37  37  VAL VAL 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  GLY 40  40  40  GLY GLY B . n 
B 1 41  SER 41  41  41  SER SER B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  SER 43  43  43  SER SER B . n 
B 1 44  PRO 44  44  44  PRO PRO B . n 
B 1 45  GLN 45  45  45  GLN GLN B . n 
B 1 46  PRO 46  46  46  PRO PRO B . n 
B 1 47  PRO 47  47  47  PRO PRO B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  THR 49  49  49  THR THR B . n 
B 1 50  LYS 50  50  50  LYS LYS B . n 
B 1 51  TRP 51  51  51  TRP TRP B . n 
B 1 52  LEU 52  52  52  LEU LEU B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ARG 54  54  54  ARG ARG B . n 
B 1 55  GLY 55  55  55  GLY GLY B . n 
B 1 56  ILE 56  56  56  ILE ILE B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  SER 58  58  58  SER SER B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  GLU 60  60  60  GLU GLU B . n 
B 1 61  ARG 61  61  61  ARG ARG B . n 
B 1 62  TYR 62  62  62  TYR TYR B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  VAL 64  64  64  VAL VAL B . n 
B 1 65  ARG 65  65  65  ARG ARG B . n 
B 1 66  GLU 66  66  66  GLU GLU B . n 
B 1 67  GLU 67  67  67  GLU GLU B . n 
B 1 68  LYS 68  68  68  LYS LYS B . n 
B 1 69  ASP 69  69  69  ASP ASP B . n 
B 1 70  ARG 70  70  70  ARG ARG B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  VAL 72  72  72  VAL VAL B . n 
B 1 73  ALA 73  73  73  ALA ALA B . n 
B 1 74  LYS 74  74  74  LYS LYS B . n 
B 1 75  GLN 75  75  75  GLN GLN B . n 
B 1 76  PRO 76  76  76  PRO PRO B . n 
B 1 77  SER 77  77  77  SER SER B . n 
B 1 78  LEU 78  78  78  LEU LEU B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  ARG 80  80  80  ARG ARG B . n 
B 1 81  ALA 81  81  81  ALA ALA B . n 
B 1 82  GLU 82  82  82  GLU GLU B . n 
B 1 83  ALA 83  83  83  ALA ALA B . n 
B 1 84  THR 84  84  84  THR THR B . n 
B 1 85  CYS 85  85  85  CYS CYS B . n 
B 1 86  ALA 86  86  86  ALA ALA B . n 
B 1 87  ALA 87  87  87  ALA ALA B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ILE 89  89  89  ILE ILE B . n 
B 1 90  PRO 90  90  90  PRO PRO B . n 
B 1 91  ILE 91  91  91  ILE ILE B . n 
B 1 92  ARG 92  92  92  ARG ARG B . n 
B 1 93  LYS 93  93  93  LYS LYS B . n 
B 1 94  ASN 94  94  94  ASN ASN B . n 
B 1 95  PRO 95  95  95  PRO PRO B . n 
B 1 96  SER 96  96  96  SER SER B . n 
B 1 97  TRP 97  97  97  TRP TRP B . n 
B 1 98  TRP 98  98  98  TRP TRP B . n 
B 1 99  GLY 99  99  99  GLY GLY B . n 
B 1 100 LEU 100 100 100 LEU LEU B . n 
B 1 101 SER 101 101 101 SER SER B . n 
B 1 102 GLN 102 102 102 GLN GLN B . n 
B 1 103 ASP 103 103 103 ASP ASP B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ARG 105 105 105 ARG ARG B . n 
B 1 106 ARG 106 106 106 ARG ARG B . n 
B 1 107 LYS 107 107 107 LYS LYS B . n 
B 1 108 ILE 108 108 108 ILE ILE B . n 
B 1 109 PHE 109 109 109 PHE PHE B . n 
B 1 110 GLU 110 110 110 GLU GLU B . n 
B 1 111 GLU 111 111 111 GLU GLU B . n 
B 1 112 GLN 112 112 112 GLN GLN B . n 
B 1 113 SER 113 113 113 SER SER B . n 
B 1 114 ARG 114 114 114 ARG ARG B . n 
B 1 115 HIS 115 115 115 HIS HIS B . n 
B 1 116 ILE 116 116 116 ILE ILE B . n 
B 1 117 HIS 117 117 117 HIS HIS B . n 
B 1 118 ILE 118 118 118 ILE ILE B . n 
B 1 119 GLY 119 119 119 GLY GLY B . n 
B 1 120 LEU 120 120 120 LEU LEU B . n 
B 1 121 GLN 121 121 121 GLN GLN B . n 
B 1 122 TYR 122 122 122 TYR TYR B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 PRO 124 124 124 PRO PRO B . n 
B 1 125 ALA 125 125 125 ALA ALA B . n 
B 1 126 VAL 126 126 126 VAL VAL B . n 
B 1 127 ALA 127 127 127 ALA ALA B . n 
B 1 128 ARG 128 128 128 ARG ARG B . n 
B 1 129 ARG 129 129 129 ARG ARG B . n 
B 1 130 LEU 130 130 130 LEU LEU B . n 
B 1 131 HIS 131 131 131 HIS HIS B . n 
B 1 132 HIS 132 132 132 HIS HIS B . n 
B 1 133 CYS 133 133 133 CYS CYS B . n 
B 1 134 ARG 134 134 134 ARG ARG B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 LEU 136 136 136 LEU LEU B . n 
B 1 137 GLY 137 137 137 GLY GLY B . n 
B 1 138 GLU 138 138 138 GLU GLU B . n 
B 1 139 ASN 139 139 139 ASN ASN B . n 
B 1 140 GLU 140 140 140 GLU GLU B . n 
B 1 141 PRO 141 141 141 PRO PRO B . n 
B 1 142 PHE 142 142 142 PHE PHE B . n 
B 1 143 ASP 143 143 143 ASP ASP B . n 
B 1 144 PHE 144 144 144 PHE PHE B . n 
B 1 145 LEU 145 145 145 LEU LEU B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 TRP 147 147 147 TRP TRP B . n 
B 1 148 PHE 148 148 148 PHE PHE B . n 
B 1 149 GLU 149 149 149 GLU GLU B . n 
B 1 150 TYR 150 150 150 TYR TYR B . n 
B 1 151 SER 151 151 151 SER SER B . n 
B 1 152 PRO 152 152 152 PRO PRO B . n 
B 1 153 SER 153 153 153 SER SER B . n 
B 1 154 ASP 154 154 154 ASP ASP B . n 
B 1 155 GLU 155 155 155 GLU GLU B . n 
B 1 156 THR 156 156 156 THR THR B . n 
B 1 157 ALA 157 157 157 ALA ALA B . n 
B 1 158 PHE 158 158 158 PHE PHE B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 ARG 160 160 160 ARG ARG B . n 
B 1 161 LEU 161 161 161 LEU LEU B . n 
B 1 162 LEU 162 162 162 LEU LEU B . n 
B 1 163 ALA 163 163 163 ALA ALA B . n 
B 1 164 GLU 164 164 164 GLU GLU B . n 
B 1 165 LEU 165 165 165 LEU LEU B . n 
B 1 166 ARG 166 166 166 ARG ARG B . n 
B 1 167 ALA 167 167 167 ALA ALA B . n 
B 1 168 SER 168 168 168 SER SER B . n 
B 1 169 VAL 169 169 169 VAL VAL B . n 
B 1 170 GLU 170 170 170 GLU GLU B . n 
B 1 171 TRP 171 171 171 TRP TRP B . n 
B 1 172 GLN 172 172 172 GLN GLN B . n 
B 1 173 TYR 173 173 173 TYR TYR B . n 
B 1 174 VAL 174 174 174 VAL VAL B . n 
B 1 175 ASP 175 175 175 ASP ASP B . n 
B 1 176 ARG 176 176 176 ARG ARG B . n 
B 1 177 GLU 177 177 177 GLU GLU B . n 
B 1 178 ILE 178 178 178 ILE ILE B . n 
B 1 179 ASP 179 179 179 ASP ASP B . n 
B 1 180 ILE 180 180 180 ILE ILE B . n 
B 1 181 ARG 181 181 181 ARG ARG B . n 
B 1 182 LEU 182 182 182 LEU LEU B . n 
B 1 183 VAL 183 183 183 VAL VAL B . n 
B 1 184 HIS 184 184 184 HIS HIS B . n 
B 1 185 GLU 185 185 185 GLU GLU B . n 
B 1 186 PRO 186 186 186 PRO PRO B . n 
B 1 187 ALA 187 187 ?   ?   ?   B . n 
B 1 188 HIS 188 188 ?   ?   ?   B . n 
B 1 189 HIS 189 189 ?   ?   ?   B . n 
B 1 190 HIS 190 190 ?   ?   ?   B . n 
B 1 191 HIS 191 191 ?   ?   ?   B . n 
B 1 192 HIS 192 192 ?   ?   ?   B . n 
B 1 193 HIS 193 193 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        HEM 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   HEM 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 HEM 1   201 1   HEM HEM A . 
D 3 IMD 1   202 1   IMD IMD A . 
E 4 NA  1   203 2   NA  NA  A . 
F 4 NA  1   204 3   NA  NA  A . 
G 4 NA  1   205 6   NA  NA  A . 
H 4 NA  1   206 7   NA  NA  A . 
I 2 HEM 1   201 2   HEM HEM B . 
J 3 IMD 1   202 2   IMD IMD B . 
K 4 NA  1   203 4   NA  NA  B . 
L 4 NA  1   204 5   NA  NA  B . 
M 5 CL  1   205 1   CL  CL  B . 
N 6 HOH 1   301 168 HOH HOH A . 
N 6 HOH 2   302 396 HOH HOH A . 
N 6 HOH 3   303 274 HOH HOH A . 
N 6 HOH 4   304 163 HOH HOH A . 
N 6 HOH 5   305 653 HOH HOH A . 
N 6 HOH 6   306 650 HOH HOH A . 
N 6 HOH 7   307 678 HOH HOH A . 
N 6 HOH 8   308 365 HOH HOH A . 
N 6 HOH 9   309 594 HOH HOH A . 
N 6 HOH 10  310 344 HOH HOH A . 
N 6 HOH 11  311 608 HOH HOH A . 
N 6 HOH 12  312 526 HOH HOH A . 
N 6 HOH 13  313 209 HOH HOH A . 
N 6 HOH 14  314 275 HOH HOH A . 
N 6 HOH 15  315 293 HOH HOH A . 
N 6 HOH 16  316 214 HOH HOH A . 
N 6 HOH 17  317 544 HOH HOH A . 
N 6 HOH 18  318 108 HOH HOH A . 
N 6 HOH 19  319 709 HOH HOH A . 
N 6 HOH 20  320 646 HOH HOH A . 
N 6 HOH 21  321 598 HOH HOH A . 
N 6 HOH 22  322 346 HOH HOH A . 
N 6 HOH 23  323 253 HOH HOH A . 
N 6 HOH 24  324 37  HOH HOH A . 
N 6 HOH 25  325 73  HOH HOH A . 
N 6 HOH 26  326 103 HOH HOH A . 
N 6 HOH 27  327 686 HOH HOH A . 
N 6 HOH 28  328 78  HOH HOH A . 
N 6 HOH 29  329 377 HOH HOH A . 
N 6 HOH 30  330 147 HOH HOH A . 
N 6 HOH 31  331 277 HOH HOH A . 
N 6 HOH 32  332 13  HOH HOH A . 
N 6 HOH 33  333 41  HOH HOH A . 
N 6 HOH 34  334 87  HOH HOH A . 
N 6 HOH 35  335 132 HOH HOH A . 
N 6 HOH 36  336 370 HOH HOH A . 
N 6 HOH 37  337 63  HOH HOH A . 
N 6 HOH 38  338 338 HOH HOH A . 
N 6 HOH 39  339 156 HOH HOH A . 
N 6 HOH 40  340 75  HOH HOH A . 
N 6 HOH 41  341 153 HOH HOH A . 
N 6 HOH 42  342 16  HOH HOH A . 
N 6 HOH 43  343 196 HOH HOH A . 
N 6 HOH 44  344 85  HOH HOH A . 
N 6 HOH 45  345 265 HOH HOH A . 
N 6 HOH 46  346 17  HOH HOH A . 
N 6 HOH 47  347 420 HOH HOH A . 
N 6 HOH 48  348 643 HOH HOH A . 
N 6 HOH 49  349 68  HOH HOH A . 
N 6 HOH 50  350 418 HOH HOH A . 
N 6 HOH 51  351 62  HOH HOH A . 
N 6 HOH 52  352 356 HOH HOH A . 
N 6 HOH 53  353 246 HOH HOH A . 
N 6 HOH 54  354 470 HOH HOH A . 
N 6 HOH 55  355 27  HOH HOH A . 
N 6 HOH 56  356 524 HOH HOH A . 
N 6 HOH 57  357 97  HOH HOH A . 
N 6 HOH 58  358 24  HOH HOH A . 
N 6 HOH 59  359 150 HOH HOH A . 
N 6 HOH 60  360 437 HOH HOH A . 
N 6 HOH 61  361 15  HOH HOH A . 
N 6 HOH 62  362 227 HOH HOH A . 
N 6 HOH 63  363 391 HOH HOH A . 
N 6 HOH 64  364 52  HOH HOH A . 
N 6 HOH 65  365 292 HOH HOH A . 
N 6 HOH 66  366 642 HOH HOH A . 
N 6 HOH 67  367 403 HOH HOH A . 
N 6 HOH 68  368 315 HOH HOH A . 
N 6 HOH 69  369 680 HOH HOH A . 
N 6 HOH 70  370 625 HOH HOH A . 
N 6 HOH 71  371 500 HOH HOH A . 
N 6 HOH 72  372 76  HOH HOH A . 
N 6 HOH 73  373 67  HOH HOH A . 
N 6 HOH 74  374 351 HOH HOH A . 
N 6 HOH 75  375 50  HOH HOH A . 
N 6 HOH 76  376 236 HOH HOH A . 
N 6 HOH 77  377 57  HOH HOH A . 
N 6 HOH 78  378 359 HOH HOH A . 
N 6 HOH 79  379 99  HOH HOH A . 
N 6 HOH 80  380 463 HOH HOH A . 
N 6 HOH 81  381 31  HOH HOH A . 
N 6 HOH 82  382 442 HOH HOH A . 
N 6 HOH 83  383 454 HOH HOH A . 
N 6 HOH 84  384 143 HOH HOH A . 
N 6 HOH 85  385 96  HOH HOH A . 
N 6 HOH 86  386 133 HOH HOH A . 
N 6 HOH 87  387 197 HOH HOH A . 
N 6 HOH 88  388 71  HOH HOH A . 
N 6 HOH 89  389 350 HOH HOH A . 
N 6 HOH 90  390 155 HOH HOH A . 
N 6 HOH 91  391 337 HOH HOH A . 
N 6 HOH 92  392 389 HOH HOH A . 
N 6 HOH 93  393 118 HOH HOH A . 
N 6 HOH 94  394 174 HOH HOH A . 
N 6 HOH 95  395 458 HOH HOH A . 
N 6 HOH 96  396 36  HOH HOH A . 
N 6 HOH 97  397 228 HOH HOH A . 
N 6 HOH 98  398 55  HOH HOH A . 
N 6 HOH 99  399 20  HOH HOH A . 
N 6 HOH 100 400 684 HOH HOH A . 
N 6 HOH 101 401 647 HOH HOH A . 
N 6 HOH 102 402 127 HOH HOH A . 
N 6 HOH 103 403 25  HOH HOH A . 
N 6 HOH 104 404 575 HOH HOH A . 
N 6 HOH 105 405 30  HOH HOH A . 
N 6 HOH 106 406 166 HOH HOH A . 
N 6 HOH 107 407 656 HOH HOH A . 
N 6 HOH 108 408 267 HOH HOH A . 
N 6 HOH 109 409 373 HOH HOH A . 
N 6 HOH 110 410 255 HOH HOH A . 
N 6 HOH 111 411 415 HOH HOH A . 
N 6 HOH 112 412 109 HOH HOH A . 
N 6 HOH 113 413 4   HOH HOH A . 
N 6 HOH 114 414 149 HOH HOH A . 
N 6 HOH 115 415 543 HOH HOH A . 
N 6 HOH 116 416 517 HOH HOH A . 
N 6 HOH 117 417 371 HOH HOH A . 
N 6 HOH 118 418 588 HOH HOH A . 
N 6 HOH 119 419 194 HOH HOH A . 
N 6 HOH 120 420 72  HOH HOH A . 
N 6 HOH 121 421 60  HOH HOH A . 
N 6 HOH 122 422 392 HOH HOH A . 
N 6 HOH 123 423 394 HOH HOH A . 
N 6 HOH 124 424 607 HOH HOH A . 
N 6 HOH 125 425 33  HOH HOH A . 
N 6 HOH 126 426 563 HOH HOH A . 
N 6 HOH 127 427 134 HOH HOH A . 
N 6 HOH 128 428 376 HOH HOH A . 
N 6 HOH 129 429 235 HOH HOH A . 
N 6 HOH 130 430 12  HOH HOH A . 
N 6 HOH 131 431 66  HOH HOH A . 
N 6 HOH 132 432 475 HOH HOH A . 
N 6 HOH 133 433 162 HOH HOH A . 
N 6 HOH 134 434 704 HOH HOH A . 
N 6 HOH 135 435 307 HOH HOH A . 
N 6 HOH 136 436 117 HOH HOH A . 
N 6 HOH 137 437 59  HOH HOH A . 
N 6 HOH 138 438 258 HOH HOH A . 
N 6 HOH 139 439 18  HOH HOH A . 
N 6 HOH 140 440 91  HOH HOH A . 
N 6 HOH 141 441 611 HOH HOH A . 
N 6 HOH 142 442 691 HOH HOH A . 
N 6 HOH 143 443 587 HOH HOH A . 
N 6 HOH 144 444 349 HOH HOH A . 
N 6 HOH 145 445 601 HOH HOH A . 
N 6 HOH 146 446 125 HOH HOH A . 
N 6 HOH 147 447 358 HOH HOH A . 
N 6 HOH 148 448 29  HOH HOH A . 
N 6 HOH 149 449 84  HOH HOH A . 
N 6 HOH 150 450 11  HOH HOH A . 
N 6 HOH 151 451 568 HOH HOH A . 
N 6 HOH 152 452 727 HOH HOH A . 
N 6 HOH 153 453 334 HOH HOH A . 
N 6 HOH 154 454 404 HOH HOH A . 
N 6 HOH 155 455 237 HOH HOH A . 
N 6 HOH 156 456 367 HOH HOH A . 
N 6 HOH 157 457 126 HOH HOH A . 
N 6 HOH 158 458 245 HOH HOH A . 
N 6 HOH 159 459 423 HOH HOH A . 
N 6 HOH 160 460 494 HOH HOH A . 
N 6 HOH 161 461 469 HOH HOH A . 
N 6 HOH 162 462 407 HOH HOH A . 
N 6 HOH 163 463 700 HOH HOH A . 
N 6 HOH 164 464 46  HOH HOH A . 
N 6 HOH 165 465 464 HOH HOH A . 
N 6 HOH 166 466 148 HOH HOH A . 
N 6 HOH 167 467 140 HOH HOH A . 
N 6 HOH 168 468 164 HOH HOH A . 
N 6 HOH 169 469 241 HOH HOH A . 
N 6 HOH 170 470 698 HOH HOH A . 
N 6 HOH 171 471 702 HOH HOH A . 
N 6 HOH 172 472 743 HOH HOH A . 
N 6 HOH 173 473 529 HOH HOH A . 
N 6 HOH 174 474 443 HOH HOH A . 
N 6 HOH 175 475 412 HOH HOH A . 
N 6 HOH 176 476 115 HOH HOH A . 
N 6 HOH 177 477 553 HOH HOH A . 
N 6 HOH 178 478 414 HOH HOH A . 
N 6 HOH 179 479 462 HOH HOH A . 
N 6 HOH 180 480 313 HOH HOH A . 
N 6 HOH 181 481 82  HOH HOH A . 
N 6 HOH 182 482 410 HOH HOH A . 
N 6 HOH 183 483 224 HOH HOH A . 
N 6 HOH 184 484 605 HOH HOH A . 
N 6 HOH 185 485 507 HOH HOH A . 
N 6 HOH 186 486 301 HOH HOH A . 
N 6 HOH 187 487 419 HOH HOH A . 
N 6 HOH 188 488 111 HOH HOH A . 
N 6 HOH 189 489 225 HOH HOH A . 
N 6 HOH 190 490 22  HOH HOH A . 
N 6 HOH 191 491 450 HOH HOH A . 
N 6 HOH 192 492 291 HOH HOH A . 
N 6 HOH 193 493 217 HOH HOH A . 
N 6 HOH 194 494 501 HOH HOH A . 
N 6 HOH 195 495 592 HOH HOH A . 
N 6 HOH 196 496 43  HOH HOH A . 
N 6 HOH 197 497 518 HOH HOH A . 
N 6 HOH 198 498 179 HOH HOH A . 
N 6 HOH 199 499 570 HOH HOH A . 
N 6 HOH 200 500 45  HOH HOH A . 
N 6 HOH 201 501 283 HOH HOH A . 
N 6 HOH 202 502 249 HOH HOH A . 
N 6 HOH 203 503 324 HOH HOH A . 
N 6 HOH 204 504 703 HOH HOH A . 
N 6 HOH 205 505 70  HOH HOH A . 
N 6 HOH 206 506 369 HOH HOH A . 
N 6 HOH 207 507 294 HOH HOH A . 
N 6 HOH 208 508 606 HOH HOH A . 
N 6 HOH 209 509 436 HOH HOH A . 
N 6 HOH 210 510 559 HOH HOH A . 
N 6 HOH 211 511 427 HOH HOH A . 
N 6 HOH 212 512 406 HOH HOH A . 
N 6 HOH 213 513 663 HOH HOH A . 
N 6 HOH 214 514 405 HOH HOH A . 
N 6 HOH 215 515 694 HOH HOH A . 
N 6 HOH 216 516 152 HOH HOH A . 
N 6 HOH 217 517 446 HOH HOH A . 
N 6 HOH 218 518 471 HOH HOH A . 
N 6 HOH 219 519 706 HOH HOH A . 
N 6 HOH 220 520 660 HOH HOH A . 
N 6 HOH 221 521 718 HOH HOH A . 
N 6 HOH 222 522 400 HOH HOH A . 
N 6 HOH 223 523 286 HOH HOH A . 
N 6 HOH 224 524 522 HOH HOH A . 
N 6 HOH 225 525 707 HOH HOH A . 
N 6 HOH 226 526 538 HOH HOH A . 
N 6 HOH 227 527 618 HOH HOH A . 
N 6 HOH 228 528 444 HOH HOH A . 
N 6 HOH 229 529 79  HOH HOH A . 
N 6 HOH 230 530 665 HOH HOH A . 
N 6 HOH 231 531 724 HOH HOH A . 
N 6 HOH 232 532 424 HOH HOH A . 
N 6 HOH 233 533 160 HOH HOH A . 
N 6 HOH 234 534 652 HOH HOH A . 
N 6 HOH 235 535 644 HOH HOH A . 
N 6 HOH 236 536 655 HOH HOH A . 
N 6 HOH 237 537 551 HOH HOH A . 
N 6 HOH 238 538 715 HOH HOH A . 
N 6 HOH 239 539 542 HOH HOH A . 
N 6 HOH 240 540 636 HOH HOH A . 
N 6 HOH 241 541 633 HOH HOH A . 
N 6 HOH 242 542 624 HOH HOH A . 
N 6 HOH 243 543 590 HOH HOH A . 
N 6 HOH 244 544 564 HOH HOH A . 
N 6 HOH 245 545 635 HOH HOH A . 
N 6 HOH 246 546 3   HOH HOH A . 
N 6 HOH 247 547 583 HOH HOH A . 
N 6 HOH 248 548 416 HOH HOH A . 
N 6 HOH 249 549 683 HOH HOH A . 
N 6 HOH 250 550 299 HOH HOH A . 
N 6 HOH 251 551 640 HOH HOH A . 
N 6 HOH 252 552 729 HOH HOH A . 
N 6 HOH 253 553 120 HOH HOH A . 
N 6 HOH 254 554 726 HOH HOH A . 
N 6 HOH 255 555 586 HOH HOH A . 
N 6 HOH 256 556 348 HOH HOH A . 
N 6 HOH 257 557 720 HOH HOH A . 
N 6 HOH 258 558 555 HOH HOH A . 
N 6 HOH 259 559 439 HOH HOH A . 
N 6 HOH 260 560 202 HOH HOH A . 
N 6 HOH 261 561 92  HOH HOH A . 
N 6 HOH 262 562 154 HOH HOH A . 
N 6 HOH 263 563 670 HOH HOH A . 
N 6 HOH 264 564 593 HOH HOH A . 
N 6 HOH 265 565 604 HOH HOH A . 
N 6 HOH 266 566 399 HOH HOH A . 
N 6 HOH 267 567 426 HOH HOH A . 
N 6 HOH 268 568 557 HOH HOH A . 
N 6 HOH 269 569 303 HOH HOH A . 
N 6 HOH 270 570 382 HOH HOH A . 
N 6 HOH 271 571 201 HOH HOH A . 
N 6 HOH 272 572 725 HOH HOH A . 
N 6 HOH 273 573 239 HOH HOH A . 
N 6 HOH 274 574 561 HOH HOH A . 
N 6 HOH 275 575 205 HOH HOH A . 
N 6 HOH 276 576 536 HOH HOH A . 
N 6 HOH 277 577 649 HOH HOH A . 
N 6 HOH 278 578 449 HOH HOH A . 
N 6 HOH 279 579 626 HOH HOH A . 
N 6 HOH 280 580 276 HOH HOH A . 
N 6 HOH 281 581 339 HOH HOH A . 
N 6 HOH 282 582 610 HOH HOH A . 
N 6 HOH 283 583 696 HOH HOH A . 
N 6 HOH 284 584 573 HOH HOH A . 
N 6 HOH 285 585 451 HOH HOH A . 
N 6 HOH 286 586 499 HOH HOH A . 
N 6 HOH 287 587 534 HOH HOH A . 
N 6 HOH 288 588 628 HOH HOH A . 
N 6 HOH 289 589 272 HOH HOH A . 
N 6 HOH 290 590 136 HOH HOH A . 
N 6 HOH 291 591 567 HOH HOH A . 
N 6 HOH 292 592 539 HOH HOH A . 
N 6 HOH 293 593 250 HOH HOH A . 
N 6 HOH 294 594 329 HOH HOH A . 
N 6 HOH 295 595 520 HOH HOH A . 
N 6 HOH 296 596 711 HOH HOH A . 
N 6 HOH 297 597 304 HOH HOH A . 
N 6 HOH 298 598 541 HOH HOH A . 
N 6 HOH 299 599 122 HOH HOH A . 
N 6 HOH 300 600 131 HOH HOH A . 
N 6 HOH 301 601 158 HOH HOH A . 
N 6 HOH 302 602 440 HOH HOH A . 
N 6 HOH 303 603 195 HOH HOH A . 
N 6 HOH 304 604 735 HOH HOH A . 
N 6 HOH 305 605 600 HOH HOH A . 
N 6 HOH 306 606 511 HOH HOH A . 
N 6 HOH 307 607 65  HOH HOH A . 
N 6 HOH 308 608 591 HOH HOH A . 
N 6 HOH 309 609 183 HOH HOH A . 
N 6 HOH 310 610 532 HOH HOH A . 
N 6 HOH 311 611 495 HOH HOH A . 
N 6 HOH 312 612 141 HOH HOH A . 
N 6 HOH 313 613 123 HOH HOH A . 
N 6 HOH 314 614 535 HOH HOH A . 
N 6 HOH 315 615 629 HOH HOH A . 
N 6 HOH 316 616 165 HOH HOH A . 
N 6 HOH 317 617 352 HOH HOH A . 
N 6 HOH 318 618 662 HOH HOH A . 
N 6 HOH 319 619 489 HOH HOH A . 
N 6 HOH 320 620 282 HOH HOH A . 
N 6 HOH 321 621 326 HOH HOH A . 
N 6 HOH 322 622 730 HOH HOH A . 
N 6 HOH 323 623 309 HOH HOH A . 
N 6 HOH 324 624 667 HOH HOH A . 
N 6 HOH 325 625 273 HOH HOH A . 
N 6 HOH 326 626 740 HOH HOH A . 
N 6 HOH 327 627 279 HOH HOH A . 
N 6 HOH 328 628 498 HOH HOH A . 
N 6 HOH 329 629 483 HOH HOH A . 
N 6 HOH 330 630 668 HOH HOH A . 
N 6 HOH 331 631 316 HOH HOH A . 
N 6 HOH 332 632 221 HOH HOH A . 
N 6 HOH 333 633 741 HOH HOH A . 
N 6 HOH 334 634 363 HOH HOH A . 
N 6 HOH 335 635 513 HOH HOH A . 
N 6 HOH 336 636 216 HOH HOH A . 
N 6 HOH 337 637 226 HOH HOH A . 
N 6 HOH 338 638 206 HOH HOH A . 
N 6 HOH 339 639 533 HOH HOH A . 
N 6 HOH 340 640 496 HOH HOH A . 
N 6 HOH 341 641 184 HOH HOH A . 
N 6 HOH 342 642 178 HOH HOH A . 
N 6 HOH 343 643 480 HOH HOH A . 
N 6 HOH 344 644 637 HOH HOH A . 
N 6 HOH 345 645 187 HOH HOH A . 
N 6 HOH 346 646 546 HOH HOH A . 
N 6 HOH 347 647 361 HOH HOH A . 
N 6 HOH 348 648 481 HOH HOH A . 
N 6 HOH 349 649 477 HOH HOH A . 
N 6 HOH 350 650 242 HOH HOH A . 
N 6 HOH 351 651 137 HOH HOH A . 
N 6 HOH 352 652 478 HOH HOH A . 
N 6 HOH 353 653 484 HOH HOH A . 
N 6 HOH 354 654 505 HOH HOH A . 
N 6 HOH 355 655 675 HOH HOH A . 
N 6 HOH 356 656 268 HOH HOH A . 
N 6 HOH 357 657 531 HOH HOH A . 
N 6 HOH 358 658 701 HOH HOH A . 
N 6 HOH 359 659 106 HOH HOH A . 
N 6 HOH 360 660 322 HOH HOH A . 
N 6 HOH 361 661 44  HOH HOH A . 
N 6 HOH 362 662 95  HOH HOH A . 
N 6 HOH 363 663 584 HOH HOH A . 
N 6 HOH 364 664 619 HOH HOH A . 
N 6 HOH 365 665 102 HOH HOH A . 
N 6 HOH 366 666 676 HOH HOH A . 
N 6 HOH 367 667 448 HOH HOH A . 
N 6 HOH 368 668 270 HOH HOH A . 
N 6 HOH 369 669 232 HOH HOH A . 
N 6 HOH 370 670 666 HOH HOH A . 
N 6 HOH 371 671 383 HOH HOH A . 
N 6 HOH 372 672 515 HOH HOH A . 
N 6 HOH 373 673 509 HOH HOH A . 
N 6 HOH 374 674 554 HOH HOH A . 
N 6 HOH 375 675 549 HOH HOH A . 
N 6 HOH 376 676 621 HOH HOH A . 
N 6 HOH 377 677 384 HOH HOH A . 
N 6 HOH 378 678 622 HOH HOH A . 
N 6 HOH 379 679 737 HOH HOH A . 
N 6 HOH 380 680 327 HOH HOH A . 
N 6 HOH 381 681 438 HOH HOH A . 
N 6 HOH 382 682 413 HOH HOH A . 
N 6 HOH 383 683 514 HOH HOH A . 
N 6 HOH 384 684 708 HOH HOH A . 
N 6 HOH 385 685 93  HOH HOH A . 
N 6 HOH 386 686 722 HOH HOH A . 
N 6 HOH 387 687 523 HOH HOH A . 
N 6 HOH 388 688 487 HOH HOH A . 
N 6 HOH 389 689 634 HOH HOH A . 
N 6 HOH 390 690 738 HOH HOH A . 
N 6 HOH 391 691 422 HOH HOH A . 
N 6 HOH 392 692 488 HOH HOH A . 
N 6 HOH 393 693 582 HOH HOH A . 
N 6 HOH 394 694 452 HOH HOH A . 
N 6 HOH 395 695 492 HOH HOH A . 
N 6 HOH 396 696 525 HOH HOH A . 
N 6 HOH 397 697 732 HOH HOH A . 
N 6 HOH 398 698 630 HOH HOH A . 
O 6 HOH 1   301 175 HOH HOH B . 
O 6 HOH 2   302 260 HOH HOH B . 
O 6 HOH 3   303 692 HOH HOH B . 
O 6 HOH 4   304 717 HOH HOH B . 
O 6 HOH 5   305 659 HOH HOH B . 
O 6 HOH 6   306 688 HOH HOH B . 
O 6 HOH 7   307 648 HOH HOH B . 
O 6 HOH 8   308 613 HOH HOH B . 
O 6 HOH 9   309 576 HOH HOH B . 
O 6 HOH 10  310 521 HOH HOH B . 
O 6 HOH 11  311 566 HOH HOH B . 
O 6 HOH 12  312 100 HOH HOH B . 
O 6 HOH 13  313 157 HOH HOH B . 
O 6 HOH 14  314 353 HOH HOH B . 
O 6 HOH 15  315 312 HOH HOH B . 
O 6 HOH 16  316 58  HOH HOH B . 
O 6 HOH 17  317 14  HOH HOH B . 
O 6 HOH 18  318 112 HOH HOH B . 
O 6 HOH 19  319 180 HOH HOH B . 
O 6 HOH 20  320 433 HOH HOH B . 
O 6 HOH 21  321 53  HOH HOH B . 
O 6 HOH 22  322 615 HOH HOH B . 
O 6 HOH 23  323 139 HOH HOH B . 
O 6 HOH 24  324 252 HOH HOH B . 
O 6 HOH 25  325 512 HOH HOH B . 
O 6 HOH 26  326 510 HOH HOH B . 
O 6 HOH 27  327 284 HOH HOH B . 
O 6 HOH 28  328 130 HOH HOH B . 
O 6 HOH 29  329 49  HOH HOH B . 
O 6 HOH 30  330 208 HOH HOH B . 
O 6 HOH 31  331 61  HOH HOH B . 
O 6 HOH 32  332 589 HOH HOH B . 
O 6 HOH 33  333 101 HOH HOH B . 
O 6 HOH 34  334 104 HOH HOH B . 
O 6 HOH 35  335 238 HOH HOH B . 
O 6 HOH 36  336 311 HOH HOH B . 
O 6 HOH 37  337 5   HOH HOH B . 
O 6 HOH 38  338 341 HOH HOH B . 
O 6 HOH 39  339 35  HOH HOH B . 
O 6 HOH 40  340 116 HOH HOH B . 
O 6 HOH 41  341 28  HOH HOH B . 
O 6 HOH 42  342 651 HOH HOH B . 
O 6 HOH 43  343 88  HOH HOH B . 
O 6 HOH 44  344 445 HOH HOH B . 
O 6 HOH 45  345 86  HOH HOH B . 
O 6 HOH 46  346 119 HOH HOH B . 
O 6 HOH 47  347 114 HOH HOH B . 
O 6 HOH 48  348 21  HOH HOH B . 
O 6 HOH 49  349 135 HOH HOH B . 
O 6 HOH 50  350 261 HOH HOH B . 
O 6 HOH 51  351 121 HOH HOH B . 
O 6 HOH 52  352 10  HOH HOH B . 
O 6 HOH 53  353 181 HOH HOH B . 
O 6 HOH 54  354 192 HOH HOH B . 
O 6 HOH 55  355 355 HOH HOH B . 
O 6 HOH 56  356 269 HOH HOH B . 
O 6 HOH 57  357 465 HOH HOH B . 
O 6 HOH 58  358 219 HOH HOH B . 
O 6 HOH 59  359 467 HOH HOH B . 
O 6 HOH 60  360 129 HOH HOH B . 
O 6 HOH 61  361 581 HOH HOH B . 
O 6 HOH 62  362 421 HOH HOH B . 
O 6 HOH 63  363 333 HOH HOH B . 
O 6 HOH 64  364 83  HOH HOH B . 
O 6 HOH 65  365 220 HOH HOH B . 
O 6 HOH 66  366 428 HOH HOH B . 
O 6 HOH 67  367 336 HOH HOH B . 
O 6 HOH 68  368 468 HOH HOH B . 
O 6 HOH 69  369 695 HOH HOH B . 
O 6 HOH 70  370 161 HOH HOH B . 
O 6 HOH 71  371 69  HOH HOH B . 
O 6 HOH 72  372 447 HOH HOH B . 
O 6 HOH 73  373 596 HOH HOH B . 
O 6 HOH 74  374 259 HOH HOH B . 
O 6 HOH 75  375 90  HOH HOH B . 
O 6 HOH 76  376 199 HOH HOH B . 
O 6 HOH 77  377 330 HOH HOH B . 
O 6 HOH 78  378 39  HOH HOH B . 
O 6 HOH 79  379 48  HOH HOH B . 
O 6 HOH 80  380 506 HOH HOH B . 
O 6 HOH 81  381 56  HOH HOH B . 
O 6 HOH 82  382 385 HOH HOH B . 
O 6 HOH 83  383 223 HOH HOH B . 
O 6 HOH 84  384 159 HOH HOH B . 
O 6 HOH 85  385 485 HOH HOH B . 
O 6 HOH 86  386 1   HOH HOH B . 
O 6 HOH 87  387 51  HOH HOH B . 
O 6 HOH 88  388 113 HOH HOH B . 
O 6 HOH 89  389 40  HOH HOH B . 
O 6 HOH 90  390 290 HOH HOH B . 
O 6 HOH 91  391 343 HOH HOH B . 
O 6 HOH 92  392 366 HOH HOH B . 
O 6 HOH 93  393 402 HOH HOH B . 
O 6 HOH 94  394 379 HOH HOH B . 
O 6 HOH 95  395 94  HOH HOH B . 
O 6 HOH 96  396 310 HOH HOH B . 
O 6 HOH 97  397 434 HOH HOH B . 
O 6 HOH 98  398 357 HOH HOH B . 
O 6 HOH 99  399 375 HOH HOH B . 
O 6 HOH 100 400 9   HOH HOH B . 
O 6 HOH 101 401 200 HOH HOH B . 
O 6 HOH 102 402 32  HOH HOH B . 
O 6 HOH 103 403 171 HOH HOH B . 
O 6 HOH 104 404 2   HOH HOH B . 
O 6 HOH 105 405 502 HOH HOH B . 
O 6 HOH 106 406 360 HOH HOH B . 
O 6 HOH 107 407 19  HOH HOH B . 
O 6 HOH 108 408 47  HOH HOH B . 
O 6 HOH 109 409 264 HOH HOH B . 
O 6 HOH 110 410 677 HOH HOH B . 
O 6 HOH 111 411 504 HOH HOH B . 
O 6 HOH 112 412 390 HOH HOH B . 
O 6 HOH 113 413 386 HOH HOH B . 
O 6 HOH 114 414 372 HOH HOH B . 
O 6 HOH 115 415 182 HOH HOH B . 
O 6 HOH 116 416 81  HOH HOH B . 
O 6 HOH 117 417 243 HOH HOH B . 
O 6 HOH 118 418 690 HOH HOH B . 
O 6 HOH 119 419 263 HOH HOH B . 
O 6 HOH 120 420 89  HOH HOH B . 
O 6 HOH 121 421 42  HOH HOH B . 
O 6 HOH 122 422 474 HOH HOH B . 
O 6 HOH 123 423 144 HOH HOH B . 
O 6 HOH 124 424 302 HOH HOH B . 
O 6 HOH 125 425 287 HOH HOH B . 
O 6 HOH 126 426 393 HOH HOH B . 
O 6 HOH 127 427 7   HOH HOH B . 
O 6 HOH 128 428 151 HOH HOH B . 
O 6 HOH 129 429 146 HOH HOH B . 
O 6 HOH 130 430 54  HOH HOH B . 
O 6 HOH 131 431 26  HOH HOH B . 
O 6 HOH 132 432 128 HOH HOH B . 
O 6 HOH 133 433 318 HOH HOH B . 
O 6 HOH 134 434 251 HOH HOH B . 
O 6 HOH 135 435 472 HOH HOH B . 
O 6 HOH 136 436 105 HOH HOH B . 
O 6 HOH 137 437 38  HOH HOH B . 
O 6 HOH 138 438 331 HOH HOH B . 
O 6 HOH 139 439 34  HOH HOH B . 
O 6 HOH 140 440 347 HOH HOH B . 
O 6 HOH 141 441 558 HOH HOH B . 
O 6 HOH 142 442 687 HOH HOH B . 
O 6 HOH 143 443 335 HOH HOH B . 
O 6 HOH 144 444 244 HOH HOH B . 
O 6 HOH 145 445 466 HOH HOH B . 
O 6 HOH 146 446 638 HOH HOH B . 
O 6 HOH 147 447 453 HOH HOH B . 
O 6 HOH 148 448 193 HOH HOH B . 
O 6 HOH 149 449 674 HOH HOH B . 
O 6 HOH 150 450 295 HOH HOH B . 
O 6 HOH 151 451 170 HOH HOH B . 
O 6 HOH 152 452 297 HOH HOH B . 
O 6 HOH 153 453 431 HOH HOH B . 
O 6 HOH 154 454 332 HOH HOH B . 
O 6 HOH 155 455 186 HOH HOH B . 
O 6 HOH 156 456 8   HOH HOH B . 
O 6 HOH 157 457 387 HOH HOH B . 
O 6 HOH 158 458 345 HOH HOH B . 
O 6 HOH 159 459 189 HOH HOH B . 
O 6 HOH 160 460 411 HOH HOH B . 
O 6 HOH 161 461 503 HOH HOH B . 
O 6 HOH 162 462 210 HOH HOH B . 
O 6 HOH 163 463 124 HOH HOH B . 
O 6 HOH 164 464 459 HOH HOH B . 
O 6 HOH 165 465 6   HOH HOH B . 
O 6 HOH 166 466 231 HOH HOH B . 
O 6 HOH 167 467 172 HOH HOH B . 
O 6 HOH 168 468 580 HOH HOH B . 
O 6 HOH 169 469 169 HOH HOH B . 
O 6 HOH 170 470 368 HOH HOH B . 
O 6 HOH 171 471 425 HOH HOH B . 
O 6 HOH 172 472 177 HOH HOH B . 
O 6 HOH 173 473 401 HOH HOH B . 
O 6 HOH 174 474 167 HOH HOH B . 
O 6 HOH 175 475 479 HOH HOH B . 
O 6 HOH 176 476 395 HOH HOH B . 
O 6 HOH 177 477 257 HOH HOH B . 
O 6 HOH 178 478 190 HOH HOH B . 
O 6 HOH 179 479 508 HOH HOH B . 
O 6 HOH 180 480 617 HOH HOH B . 
O 6 HOH 181 481 456 HOH HOH B . 
O 6 HOH 182 482 64  HOH HOH B . 
O 6 HOH 183 483 681 HOH HOH B . 
O 6 HOH 184 484 110 HOH HOH B . 
O 6 HOH 185 485 657 HOH HOH B . 
O 6 HOH 186 486 723 HOH HOH B . 
O 6 HOH 187 487 623 HOH HOH B . 
O 6 HOH 188 488 710 HOH HOH B . 
O 6 HOH 189 489 278 HOH HOH B . 
O 6 HOH 190 490 493 HOH HOH B . 
O 6 HOH 191 491 473 HOH HOH B . 
O 6 HOH 192 492 429 HOH HOH B . 
O 6 HOH 193 493 693 HOH HOH B . 
O 6 HOH 194 494 719 HOH HOH B . 
O 6 HOH 195 495 682 HOH HOH B . 
O 6 HOH 196 496 569 HOH HOH B . 
O 6 HOH 197 497 388 HOH HOH B . 
O 6 HOH 198 498 612 HOH HOH B . 
O 6 HOH 199 499 138 HOH HOH B . 
O 6 HOH 200 500 716 HOH HOH B . 
O 6 HOH 201 501 308 HOH HOH B . 
O 6 HOH 202 502 545 HOH HOH B . 
O 6 HOH 203 503 319 HOH HOH B . 
O 6 HOH 204 504 198 HOH HOH B . 
O 6 HOH 205 505 435 HOH HOH B . 
O 6 HOH 206 506 211 HOH HOH B . 
O 6 HOH 207 507 552 HOH HOH B . 
O 6 HOH 208 508 460 HOH HOH B . 
O 6 HOH 209 509 731 HOH HOH B . 
O 6 HOH 210 510 254 HOH HOH B . 
O 6 HOH 211 511 664 HOH HOH B . 
O 6 HOH 212 512 672 HOH HOH B . 
O 6 HOH 213 513 685 HOH HOH B . 
O 6 HOH 214 514 298 HOH HOH B . 
O 6 HOH 215 515 80  HOH HOH B . 
O 6 HOH 216 516 323 HOH HOH B . 
O 6 HOH 217 517 317 HOH HOH B . 
O 6 HOH 218 518 571 HOH HOH B . 
O 6 HOH 219 519 572 HOH HOH B . 
O 6 HOH 220 520 669 HOH HOH B . 
O 6 HOH 221 521 560 HOH HOH B . 
O 6 HOH 222 522 739 HOH HOH B . 
O 6 HOH 223 523 23  HOH HOH B . 
O 6 HOH 224 524 556 HOH HOH B . 
O 6 HOH 225 525 658 HOH HOH B . 
O 6 HOH 226 526 540 HOH HOH B . 
O 6 HOH 227 527 654 HOH HOH B . 
O 6 HOH 228 528 378 HOH HOH B . 
O 6 HOH 229 529 234 HOH HOH B . 
O 6 HOH 230 530 281 HOH HOH B . 
O 6 HOH 231 531 285 HOH HOH B . 
O 6 HOH 232 532 74  HOH HOH B . 
O 6 HOH 233 533 300 HOH HOH B . 
O 6 HOH 234 534 713 HOH HOH B . 
O 6 HOH 235 535 417 HOH HOH B . 
O 6 HOH 236 536 574 HOH HOH B . 
O 6 HOH 237 537 490 HOH HOH B . 
O 6 HOH 238 538 632 HOH HOH B . 
O 6 HOH 239 539 528 HOH HOH B . 
O 6 HOH 240 540 256 HOH HOH B . 
O 6 HOH 241 541 305 HOH HOH B . 
O 6 HOH 242 542 441 HOH HOH B . 
O 6 HOH 243 543 461 HOH HOH B . 
O 6 HOH 244 544 364 HOH HOH B . 
O 6 HOH 245 545 548 HOH HOH B . 
O 6 HOH 246 546 712 HOH HOH B . 
O 6 HOH 247 547 212 HOH HOH B . 
O 6 HOH 248 548 577 HOH HOH B . 
O 6 HOH 249 549 325 HOH HOH B . 
O 6 HOH 250 550 734 HOH HOH B . 
O 6 HOH 251 551 742 HOH HOH B . 
O 6 HOH 252 552 689 HOH HOH B . 
O 6 HOH 253 553 266 HOH HOH B . 
O 6 HOH 254 554 289 HOH HOH B . 
O 6 HOH 255 555 306 HOH HOH B . 
O 6 HOH 256 556 550 HOH HOH B . 
O 6 HOH 257 557 98  HOH HOH B . 
O 6 HOH 258 558 191 HOH HOH B . 
O 6 HOH 259 559 381 HOH HOH B . 
O 6 HOH 260 560 455 HOH HOH B . 
O 6 HOH 261 561 342 HOH HOH B . 
O 6 HOH 262 562 271 HOH HOH B . 
O 6 HOH 263 563 296 HOH HOH B . 
O 6 HOH 264 564 288 HOH HOH B . 
O 6 HOH 265 565 203 HOH HOH B . 
O 6 HOH 266 566 562 HOH HOH B . 
O 6 HOH 267 567 185 HOH HOH B . 
O 6 HOH 268 568 247 HOH HOH B . 
O 6 HOH 269 569 176 HOH HOH B . 
O 6 HOH 270 570 627 HOH HOH B . 
O 6 HOH 271 571 262 HOH HOH B . 
O 6 HOH 272 572 145 HOH HOH B . 
O 6 HOH 273 573 280 HOH HOH B . 
O 6 HOH 274 574 328 HOH HOH B . 
O 6 HOH 275 575 497 HOH HOH B . 
O 6 HOH 276 576 230 HOH HOH B . 
O 6 HOH 277 577 482 HOH HOH B . 
O 6 HOH 278 578 530 HOH HOH B . 
O 6 HOH 279 579 207 HOH HOH B . 
O 6 HOH 280 580 362 HOH HOH B . 
O 6 HOH 281 581 585 HOH HOH B . 
O 6 HOH 282 582 579 HOH HOH B . 
O 6 HOH 283 583 699 HOH HOH B . 
O 6 HOH 284 584 77  HOH HOH B . 
O 6 HOH 285 585 188 HOH HOH B . 
O 6 HOH 286 586 229 HOH HOH B . 
O 6 HOH 287 587 733 HOH HOH B . 
O 6 HOH 288 588 397 HOH HOH B . 
O 6 HOH 289 589 380 HOH HOH B . 
O 6 HOH 290 590 320 HOH HOH B . 
O 6 HOH 291 591 527 HOH HOH B . 
O 6 HOH 292 592 222 HOH HOH B . 
O 6 HOH 293 593 486 HOH HOH B . 
O 6 HOH 294 594 142 HOH HOH B . 
O 6 HOH 295 595 240 HOH HOH B . 
O 6 HOH 296 596 697 HOH HOH B . 
O 6 HOH 297 597 233 HOH HOH B . 
O 6 HOH 298 598 645 HOH HOH B . 
O 6 HOH 299 599 728 HOH HOH B . 
O 6 HOH 300 600 603 HOH HOH B . 
O 6 HOH 301 601 714 HOH HOH B . 
O 6 HOH 302 602 398 HOH HOH B . 
O 6 HOH 303 603 736 HOH HOH B . 
O 6 HOH 304 604 476 HOH HOH B . 
O 6 HOH 305 605 595 HOH HOH B . 
O 6 HOH 306 606 213 HOH HOH B . 
O 6 HOH 307 607 321 HOH HOH B . 
O 6 HOH 308 608 679 HOH HOH B . 
O 6 HOH 309 609 721 HOH HOH B . 
O 6 HOH 310 610 537 HOH HOH B . 
O 6 HOH 311 611 516 HOH HOH B . 
O 6 HOH 312 612 107 HOH HOH B . 
O 6 HOH 313 613 354 HOH HOH B . 
O 6 HOH 314 614 314 HOH HOH B . 
O 6 HOH 315 615 639 HOH HOH B . 
O 6 HOH 316 616 374 HOH HOH B . 
O 6 HOH 317 617 173 HOH HOH B . 
O 6 HOH 318 618 457 HOH HOH B . 
O 6 HOH 319 619 597 HOH HOH B . 
O 6 HOH 320 620 204 HOH HOH B . 
O 6 HOH 321 621 705 HOH HOH B . 
O 6 HOH 322 622 409 HOH HOH B . 
O 6 HOH 323 623 248 HOH HOH B . 
O 6 HOH 324 624 744 HOH HOH B . 
O 6 HOH 325 625 641 HOH HOH B . 
O 6 HOH 326 626 340 HOH HOH B . 
O 6 HOH 327 627 519 HOH HOH B . 
O 6 HOH 328 628 673 HOH HOH B . 
O 6 HOH 329 629 218 HOH HOH B . 
O 6 HOH 330 630 215 HOH HOH B . 
O 6 HOH 331 631 631 HOH HOH B . 
O 6 HOH 332 632 609 HOH HOH B . 
O 6 HOH 333 633 408 HOH HOH B . 
O 6 HOH 334 634 491 HOH HOH B . 
O 6 HOH 335 635 661 HOH HOH B . 
O 6 HOH 336 636 602 HOH HOH B . 
O 6 HOH 337 637 432 HOH HOH B . 
O 6 HOH 338 638 430 HOH HOH B . 
O 6 HOH 339 639 547 HOH HOH B . 
O 6 HOH 340 640 616 HOH HOH B . 
O 6 HOH 341 641 578 HOH HOH B . 
O 6 HOH 342 642 620 HOH HOH B . 
O 6 HOH 343 643 671 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0405 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   129.30 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GTJ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     127.460 
_cell.length_a_esd                 ? 
_cell.length_b                     45.971 
_cell.length_b_esd                 ? 
_cell.length_c                     90.156 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9GTJ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9GTJ 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.31 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.77 
_exptl_crystal.description                  Rods 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2M Ammonium citrate dibasic; 20% w/v PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-05-03 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.7749 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.7749 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GTJ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              0.99 
_reflns.d_resolution_low                               49.32 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     217930 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           97.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.050 
_reflns.pdbx_Rpim_I_all                                0.019 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       1488111 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.046 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    0.99 
_reflns_shell.d_res_low                                     1.02 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           141992 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             20381 
_reflns_shell.percent_possible_obs                          92.6 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               7.0 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.8 
_reflns_shell.pdbx_Rrim_I_all                               2.532 
_reflns_shell.pdbx_Rpim_I_all                               0.944 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.364 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  2.346 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.05 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.03 
_refine.aniso_B[2][2]                            0.00 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.01 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               18.259 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.980 
_refine.correlation_coeff_Fo_to_Fc_free          0.977 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9GTJ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            0.99 
_refine.ls_d_res_low                             49.32 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     215927 
_refine.ls_number_reflns_R_free                  2000 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.20 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.14365 
_refine.ls_R_factor_R_free                       0.16067 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.14350 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.021 
_refine.pdbx_overall_ESU_R_Free                  0.022 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             0.702 
_refine.overall_SU_ML                            0.017 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       0.99 
_refine_hist.d_res_low                        49.32 
_refine_hist.number_atoms_solvent             741 
_refine_hist.number_atoms_total               3822 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2978 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         103 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.012  0.012  3224 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  3032 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.727  1.702  4422 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.636  1.586  6878 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.308  5.000  387  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 8.898  5.000  38   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.727 10.000 513  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.092  0.200  454  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.012  0.020  3911 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  837  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.772  2.500  1498 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.773  2.864  1498 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.923  75.021 1874 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.925  75.306 1875 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 1.512  1.512  1726 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.512  ?      1727 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.063  ?      2539 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.983  ?      4110 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 2.827  ?      3746 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 8.424  3.000  3217 ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       0.990 
_refine_ls_shell.d_res_low                        1.016 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             141 
_refine_ls_shell.number_reflns_R_work             15122 
_refine_ls_shell.percent_reflns_obs               92.36 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.326 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.359 
# 
_struct.entry_id                     9GTJ 
_struct.title                        'Chlorite dismutase from Pseudomonas sp.' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9GTJ 
_struct_keywords.text            'Chlorite degradation; Metagenomics; Soil; Bioremediation; Heme, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 ? 
G N N 4 ? 
H N N 4 ? 
I N N 2 ? 
J N N 3 ? 
K N N 4 ? 
L N N 4 ? 
M N N 5 ? 
N N N 6 ? 
O N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A1G8UKZ8_9PSED 
_struct_ref.pdbx_db_accession          A0A1G8UKZ8 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MNTRVFTFAGGETGVWRVVAMNAVAGAPLPGIPRLNVAAGSVSPQPPGTKWLLRGITSNERYVVREEKDRLVAKQPSLGR
AEATCAALIPIRKNPSWWGLSQDERRKIFEEQSRHIHIGLQYLPAVARRLHHCRDLGENEPFDFLTWFEYSPSDETAFNR
LLAELRASVEWQYVDREIDIRLVHEPA
;
_struct_ref.pdbx_align_begin           1 
# 
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 9GTJ A 1 ? 187 ? A0A1G8UKZ8 1 ? 187 ? 1 187 
2 1 9GTJ B 1 ? 187 ? A0A1G8UKZ8 1 ? 187 ? 1 187 
# 
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 9GTJ HIS A 188 ? UNP A0A1G8UKZ8 ? ? 'expression tag' 188 1  
1 9GTJ HIS A 189 ? UNP A0A1G8UKZ8 ? ? 'expression tag' 189 2  
1 9GTJ HIS A 190 ? UNP A0A1G8UKZ8 ? ? 'expression tag' 190 3  
1 9GTJ HIS A 191 ? UNP A0A1G8UKZ8 ? ? 'expression tag' 191 4  
1 9GTJ HIS A 192 ? UNP A0A1G8UKZ8 ? ? 'expression tag' 192 5  
1 9GTJ HIS A 193 ? UNP A0A1G8UKZ8 ? ? 'expression tag' 193 6  
2 9GTJ HIS B 188 ? UNP A0A1G8UKZ8 ? ? 'expression tag' 188 7  
2 9GTJ HIS B 189 ? UNP A0A1G8UKZ8 ? ? 'expression tag' 189 8  
2 9GTJ HIS B 190 ? UNP A0A1G8UKZ8 ? ? 'expression tag' 190 9  
2 9GTJ HIS B 191 ? UNP A0A1G8UKZ8 ? ? 'expression tag' 191 10 
2 9GTJ HIS B 192 ? UNP A0A1G8UKZ8 ? ? 'expression tag' 192 11 
2 9GTJ HIS B 193 ? UNP A0A1G8UKZ8 ? ? 'expression tag' 193 12 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6500  ? 
1 MORE         -122  ? 
1 'SSA (A^2)'  15550 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 VAL A 64  ? GLN A 75  ? VAL A 64  GLN A 75  1 ? 12 
HELX_P HELX_P2  AA2 ASN A 94  ? LEU A 100 ? ASN A 94  LEU A 100 1 ? 7  
HELX_P HELX_P3  AA3 SER A 101 ? GLU A 110 ? SER A 101 GLU A 110 1 ? 10 
HELX_P HELX_P4  AA4 ARG A 114 ? GLN A 121 ? ARG A 114 GLN A 121 1 ? 8  
HELX_P HELX_P5  AA5 SER A 151 ? SER A 153 ? SER A 151 SER A 153 5 ? 3  
HELX_P HELX_P6  AA6 ASP A 154 ? ALA A 167 ? ASP A 154 ALA A 167 1 ? 14 
HELX_P HELX_P7  AA7 SER A 168 ? GLN A 172 ? SER A 168 GLN A 172 5 ? 5  
HELX_P HELX_P8  AA8 VAL B 64  ? GLN B 75  ? VAL B 64  GLN B 75  1 ? 12 
HELX_P HELX_P9  AA9 ASN B 94  ? LEU B 100 ? ASN B 94  LEU B 100 1 ? 7  
HELX_P HELX_P10 AB1 SER B 101 ? GLU B 110 ? SER B 101 GLU B 110 1 ? 10 
HELX_P HELX_P11 AB2 ARG B 114 ? GLN B 121 ? ARG B 114 GLN B 121 1 ? 8  
HELX_P HELX_P12 AB3 SER B 151 ? SER B 153 ? SER B 151 SER B 153 5 ? 3  
HELX_P HELX_P13 AB4 ASP B 154 ? ALA B 167 ? ASP B 154 ALA B 167 1 ? 14 
HELX_P HELX_P14 AB5 SER B 168 ? GLN B 172 ? SER B 168 GLN B 172 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A ASN 59  O   ? ? ? 1_555 F NA  . NA ? ? A ASN 59  A NA  204 1_555 ? ? ? ? ? ? ? 2.809 ? ? 
metalc2  metalc ? ? A TYR 62  OH  ? ? ? 1_555 G NA  . NA ? ? A TYR 62  A NA  205 1_555 ? ? ? ? ? ? ? 2.627 ? ? 
metalc3  metalc ? ? A HIS 115 NE2 ? ? ? 1_555 C HEM . FE ? ? A HIS 115 A HEM 201 1_555 ? ? ? ? ? ? ? 2.049 ? ? 
metalc4  metalc ? ? A LEU 130 O   ? ? ? 1_555 H NA  . NA ? ? A LEU 130 A NA  206 1_555 ? ? ? ? ? ? ? 2.809 ? ? 
metalc5  metalc ? ? C HEM .   FE  ? ? ? 1_555 D IMD . N3 ? ? A HEM 201 A IMD 202 1_555 ? ? ? ? ? ? ? 2.089 ? ? 
metalc6  metalc ? ? C HEM .   O1D ? ? ? 1_555 E NA  . NA ? ? A HEM 201 A NA  203 1_555 ? ? ? ? ? ? ? 2.760 ? ? 
metalc7  metalc ? ? C HEM .   O1A ? ? ? 1_555 F NA  . NA ? ? A HEM 201 A NA  204 1_555 ? ? ? ? ? ? ? 2.746 ? ? 
metalc8  metalc ? ? C HEM .   O1D ? ? ? 1_555 G NA  . NA ? ? A HEM 201 A NA  205 1_555 ? ? ? ? ? ? ? 3.170 ? ? 
metalc9  metalc ? ? C HEM .   O2D ? ? ? 1_555 G NA  . NA ? ? A HEM 201 A NA  205 1_555 ? ? ? ? ? ? ? 2.559 ? ? 
metalc10 metalc ? ? E NA  .   NA  ? ? ? 1_555 N HOH . O  ? ? A NA  203 A HOH 418 1_555 ? ? ? ? ? ? ? 2.888 ? ? 
metalc11 metalc ? ? E NA  .   NA  ? ? ? 1_555 O HOH . O  ? ? A NA  203 B HOH 447 1_555 ? ? ? ? ? ? ? 2.898 ? ? 
metalc12 metalc ? ? F NA  .   NA  ? ? ? 1_555 N HOH . O  ? ? A NA  204 A HOH 546 1_555 ? ? ? ? ? ? ? 2.755 ? ? 
metalc13 metalc ? ? H NA  .   NA  ? ? ? 1_555 N HOH . O  ? ? A NA  206 A HOH 546 1_555 ? ? ? ? ? ? ? 2.790 ? ? 
metalc14 metalc ? ? B HIS 115 NE2 ? ? ? 1_555 I HEM . FE ? ? B HIS 115 B HEM 201 1_555 ? ? ? ? ? ? ? 2.032 ? ? 
metalc15 metalc ? ? B HIS 132 O   ? ? ? 1_555 L NA  . NA ? ? B HIS 132 B NA  204 1_555 ? ? ? ? ? ? ? 3.111 ? ? 
metalc16 metalc ? ? I HEM .   FE  ? ? ? 1_555 J IMD . N3 ? ? B HEM 201 B IMD 202 1_555 ? ? ? ? ? ? ? 2.084 ? ? 
metalc17 metalc ? ? K NA  .   NA  ? ? ? 1_555 O HOH . O  ? ? B NA  203 B HOH 332 1_555 ? ? ? ? ? ? ? 2.725 ? ? 
metalc18 metalc ? ? K NA  .   NA  ? ? ? 1_555 O HOH . O  ? ? B NA  203 B HOH 352 1_555 ? ? ? ? ? ? ? 2.783 ? ? 
metalc19 metalc ? ? L NA  .   NA  ? ? ? 1_555 O HOH . O  ? ? B NA  204 B HOH 337 1_555 ? ? ? ? ? ? ? 2.876 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O   ? A ASN 59  ? A ASN 59  ? 1_555 NA ? F NA  . ? A NA  204 ? 1_555 O1A ? C HEM . ? A HEM 201 ? 1_555 97.2  ? 
2  O   ? A ASN 59  ? A ASN 59  ? 1_555 NA ? F NA  . ? A NA  204 ? 1_555 O   ? N HOH . ? A HOH 546 ? 1_555 107.5 ? 
3  O1A ? C HEM .   ? A HEM 201 ? 1_555 NA ? F NA  . ? A NA  204 ? 1_555 O   ? N HOH . ? A HOH 546 ? 1_555 110.9 ? 
4  OH  ? A TYR 62  ? A TYR 62  ? 1_555 NA ? G NA  . ? A NA  205 ? 1_555 O1D ? C HEM . ? A HEM 201 ? 1_555 103.1 ? 
5  OH  ? A TYR 62  ? A TYR 62  ? 1_555 NA ? G NA  . ? A NA  205 ? 1_555 O2D ? C HEM . ? A HEM 201 ? 1_555 109.8 ? 
6  O1D ? C HEM .   ? A HEM 201 ? 1_555 NA ? G NA  . ? A NA  205 ? 1_555 O2D ? C HEM . ? A HEM 201 ? 1_555 44.2  ? 
7  NE2 ? A HIS 115 ? A HIS 115 ? 1_555 FE ? C HEM . ? A HEM 201 ? 1_555 NA  ? C HEM . ? A HEM 201 ? 1_555 89.6  ? 
8  NE2 ? A HIS 115 ? A HIS 115 ? 1_555 FE ? C HEM . ? A HEM 201 ? 1_555 NB  ? C HEM . ? A HEM 201 ? 1_555 96.6  ? 
9  NA  ? C HEM .   ? A HEM 201 ? 1_555 FE ? C HEM . ? A HEM 201 ? 1_555 NB  ? C HEM . ? A HEM 201 ? 1_555 89.3  ? 
10 NE2 ? A HIS 115 ? A HIS 115 ? 1_555 FE ? C HEM . ? A HEM 201 ? 1_555 NC  ? C HEM . ? A HEM 201 ? 1_555 94.7  ? 
11 NA  ? C HEM .   ? A HEM 201 ? 1_555 FE ? C HEM . ? A HEM 201 ? 1_555 NC  ? C HEM . ? A HEM 201 ? 1_555 175.7 ? 
12 NB  ? C HEM .   ? A HEM 201 ? 1_555 FE ? C HEM . ? A HEM 201 ? 1_555 NC  ? C HEM . ? A HEM 201 ? 1_555 90.6  ? 
13 NE2 ? A HIS 115 ? A HIS 115 ? 1_555 FE ? C HEM . ? A HEM 201 ? 1_555 ND  ? C HEM . ? A HEM 201 ? 1_555 88.9  ? 
14 NA  ? C HEM .   ? A HEM 201 ? 1_555 FE ? C HEM . ? A HEM 201 ? 1_555 ND  ? C HEM . ? A HEM 201 ? 1_555 90.6  ? 
15 NB  ? C HEM .   ? A HEM 201 ? 1_555 FE ? C HEM . ? A HEM 201 ? 1_555 ND  ? C HEM . ? A HEM 201 ? 1_555 174.6 ? 
16 NC  ? C HEM .   ? A HEM 201 ? 1_555 FE ? C HEM . ? A HEM 201 ? 1_555 ND  ? C HEM . ? A HEM 201 ? 1_555 89.1  ? 
17 NE2 ? A HIS 115 ? A HIS 115 ? 1_555 FE ? C HEM . ? A HEM 201 ? 1_555 N3  ? D IMD . ? A IMD 202 ? 1_555 174.6 ? 
18 NA  ? C HEM .   ? A HEM 201 ? 1_555 FE ? C HEM . ? A HEM 201 ? 1_555 N3  ? D IMD . ? A IMD 202 ? 1_555 87.5  ? 
19 NB  ? C HEM .   ? A HEM 201 ? 1_555 FE ? C HEM . ? A HEM 201 ? 1_555 N3  ? D IMD . ? A IMD 202 ? 1_555 87.9  ? 
20 NC  ? C HEM .   ? A HEM 201 ? 1_555 FE ? C HEM . ? A HEM 201 ? 1_555 N3  ? D IMD . ? A IMD 202 ? 1_555 88.3  ? 
21 ND  ? C HEM .   ? A HEM 201 ? 1_555 FE ? C HEM . ? A HEM 201 ? 1_555 N3  ? D IMD . ? A IMD 202 ? 1_555 86.6  ? 
22 O   ? A LEU 130 ? A LEU 130 ? 1_555 NA ? H NA  . ? A NA  206 ? 1_555 O   ? N HOH . ? A HOH 546 ? 1_555 126.1 ? 
23 O1D ? C HEM .   ? A HEM 201 ? 1_555 NA ? E NA  . ? A NA  203 ? 1_555 O   ? N HOH . ? A HOH 418 ? 1_555 119.2 ? 
24 O1D ? C HEM .   ? A HEM 201 ? 1_555 NA ? E NA  . ? A NA  203 ? 1_555 O   ? O HOH . ? B HOH 447 ? 1_555 139.0 ? 
25 O   ? N HOH .   ? A HOH 418 ? 1_555 NA ? E NA  . ? A NA  203 ? 1_555 O   ? O HOH . ? B HOH 447 ? 1_555 98.5  ? 
26 NE2 ? B HIS 115 ? B HIS 115 ? 1_555 FE ? I HEM . ? B HEM 201 ? 1_555 NA  ? I HEM . ? B HEM 201 ? 1_555 89.6  ? 
27 NE2 ? B HIS 115 ? B HIS 115 ? 1_555 FE ? I HEM . ? B HEM 201 ? 1_555 NB  ? I HEM . ? B HEM 201 ? 1_555 93.3  ? 
28 NA  ? I HEM .   ? B HEM 201 ? 1_555 FE ? I HEM . ? B HEM 201 ? 1_555 NB  ? I HEM . ? B HEM 201 ? 1_555 89.6  ? 
29 NE2 ? B HIS 115 ? B HIS 115 ? 1_555 FE ? I HEM . ? B HEM 201 ? 1_555 NC  ? I HEM . ? B HEM 201 ? 1_555 92.2  ? 
30 NA  ? I HEM .   ? B HEM 201 ? 1_555 FE ? I HEM . ? B HEM 201 ? 1_555 NC  ? I HEM . ? B HEM 201 ? 1_555 178.1 ? 
31 NB  ? I HEM .   ? B HEM 201 ? 1_555 FE ? I HEM . ? B HEM 201 ? 1_555 NC  ? I HEM . ? B HEM 201 ? 1_555 89.7  ? 
32 NE2 ? B HIS 115 ? B HIS 115 ? 1_555 FE ? I HEM . ? B HEM 201 ? 1_555 ND  ? I HEM . ? B HEM 201 ? 1_555 89.5  ? 
33 NA  ? I HEM .   ? B HEM 201 ? 1_555 FE ? I HEM . ? B HEM 201 ? 1_555 ND  ? I HEM . ? B HEM 201 ? 1_555 90.6  ? 
34 NB  ? I HEM .   ? B HEM 201 ? 1_555 FE ? I HEM . ? B HEM 201 ? 1_555 ND  ? I HEM . ? B HEM 201 ? 1_555 177.2 ? 
35 NC  ? I HEM .   ? B HEM 201 ? 1_555 FE ? I HEM . ? B HEM 201 ? 1_555 ND  ? I HEM . ? B HEM 201 ? 1_555 90.1  ? 
36 NE2 ? B HIS 115 ? B HIS 115 ? 1_555 FE ? I HEM . ? B HEM 201 ? 1_555 N3  ? J IMD . ? B IMD 202 ? 1_555 177.8 ? 
37 NA  ? I HEM .   ? B HEM 201 ? 1_555 FE ? I HEM . ? B HEM 201 ? 1_555 N3  ? J IMD . ? B IMD 202 ? 1_555 89.0  ? 
38 NB  ? I HEM .   ? B HEM 201 ? 1_555 FE ? I HEM . ? B HEM 201 ? 1_555 N3  ? J IMD . ? B IMD 202 ? 1_555 88.4  ? 
39 NC  ? I HEM .   ? B HEM 201 ? 1_555 FE ? I HEM . ? B HEM 201 ? 1_555 N3  ? J IMD . ? B IMD 202 ? 1_555 89.2  ? 
40 ND  ? I HEM .   ? B HEM 201 ? 1_555 FE ? I HEM . ? B HEM 201 ? 1_555 N3  ? J IMD . ? B IMD 202 ? 1_555 88.8  ? 
41 O   ? B HIS 132 ? B HIS 132 ? 1_555 NA ? L NA  . ? B NA  204 ? 1_555 O   ? O HOH . ? B HOH 337 ? 1_555 115.4 ? 
42 O   ? O HOH .   ? B HOH 332 ? 1_555 NA ? K NA  . ? B NA  203 ? 1_555 O   ? O HOH . ? B HOH 352 ? 1_555 108.9 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 43  A . ? SER 43  A PRO 44  A ? PRO 44  A 1 -2.90 
2 LEU 123 A . ? LEU 123 A PRO 124 A ? PRO 124 A 1 7.67  
3 LEU 123 B . ? LEU 123 B PRO 124 B ? PRO 124 B 1 7.69  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
AA2 ? 9 ? 
# 
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 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA1 8 9 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
AA2 8 9 ? 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 VAL A 5   ? GLY A 11  ? VAL A 5   GLY A 11  
AA1 2 ARG A 34  ? ALA A 39  ? ARG A 34  ALA A 39  
AA1 3 TRP A 16  ? ALA A 25  ? TRP A 16  ALA A 25  
AA1 4 VAL A 174 ? HIS A 184 ? VAL A 174 HIS A 184 
AA1 5 CYS A 85  ? LYS A 93  ? CYS A 85  LYS A 93  
AA1 6 PHE A 144 ? TYR A 150 ? PHE A 144 TYR A 150 
AA1 7 ALA A 127 ? HIS A 132 ? ALA A 127 HIS A 132 
AA1 8 THR A 49  ? ILE A 56  ? THR A 49  ILE A 56  
AA1 9 VAL A 5   ? GLY A 11  ? VAL A 5   GLY A 11  
AA2 1 VAL B 5   ? GLY B 11  ? VAL B 5   GLY B 11  
AA2 2 ARG B 34  ? ALA B 39  ? ARG B 34  ALA B 39  
AA2 3 TRP B 16  ? ALA B 25  ? TRP B 16  ALA B 25  
AA2 4 VAL B 174 ? HIS B 184 ? VAL B 174 HIS B 184 
AA2 5 CYS B 85  ? LYS B 93  ? CYS B 85  LYS B 93  
AA2 6 PHE B 144 ? TYR B 150 ? PHE B 144 TYR B 150 
AA2 7 ALA B 127 ? HIS B 132 ? ALA B 127 HIS B 132 
AA2 8 THR B 49  ? ILE B 56  ? THR B 49  ILE B 56  
AA2 9 VAL B 5   ? GLY B 11  ? VAL B 5   GLY B 11  
# 
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 ALA A 9   ? N ALA A 9   O ASN A 36  ? O ASN A 36  
AA1 2 3 O LEU A 35  ? O LEU A 35  N TRP A 16  ? N TRP A 16  
AA1 3 4 N ASN A 22  ? N ASN A 22  O ASP A 179 ? O ASP A 179 
AA1 4 5 O LEU A 182 ? O LEU A 182 N ALA A 86  ? N ALA A 86  
AA1 5 6 N ILE A 89  ? N ILE A 89  O THR A 146 ? O THR A 146 
AA1 6 7 O GLU A 149 ? O GLU A 149 N ALA A 127 ? N ALA A 127 
AA1 7 8 O HIS A 132 ? O HIS A 132 N ILE A 56  ? N ILE A 56  
AA1 8 9 O LYS A 50  ? O LYS A 50  N GLY A 10  ? N GLY A 10  
AA2 1 2 N ALA B 9   ? N ALA B 9   O ASN B 36  ? O ASN B 36  
AA2 2 3 O LEU B 35  ? O LEU B 35  N TRP B 16  ? N TRP B 16  
AA2 3 4 N ASN B 22  ? N ASN B 22  O ASP B 179 ? O ASP B 179 
AA2 4 5 O LEU B 182 ? O LEU B 182 N ALA B 86  ? N ALA B 86  
AA2 5 6 N ILE B 89  ? N ILE B 89  O THR B 146 ? O THR B 146 
AA2 6 7 O GLU B 149 ? O GLU B 149 N ALA B 127 ? N ALA B 127 
AA2 7 8 O HIS B 132 ? O HIS B 132 N ILE B 56  ? N ILE B 56  
AA2 8 9 O LEU B 53  ? O LEU B 53  N PHE B 8   ? N PHE B 8   
# 
_pdbx_entry_details.entry_id                   9GTJ 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 HZ1  B LYS 93  ? A O B HOH 302 ? ? 1.51 
2  1 H3   A MET 1   ? ? O A HOH 301 ? ? 1.56 
3  1 H2   A MET 1   ? ? O A HOH 301 ? ? 1.56 
4  1 HD22 A ASN 36  ? ? O A HOH 302 ? ? 1.57 
5  1 N    A MET 1   ? ? O A HOH 301 ? ? 1.81 
6  1 ND2  B ASN 94  ? B O B HOH 301 ? ? 1.91 
7  1 NZ   B LYS 93  ? A O B HOH 302 ? ? 1.91 
8  1 O    A HOH 319 ? ? O A HOH 427 ? ? 2.02 
9  1 O    A HOH 307 ? ? O A HOH 434 ? ? 2.03 
10 1 O    A HOH 621 ? ? O A HOH 676 ? ? 2.06 
11 1 O    A HOH 643 ? ? O A HOH 651 ? ? 2.07 
12 1 O    A HOH 521 ? ? O A HOH 554 ? ? 2.07 
13 1 O    A HOH 470 ? ? O A HOH 531 ? ? 2.07 
14 1 O    A HOH 400 ? ? O A HOH 572 ? ? 2.08 
15 1 O    B HOH 490 ? ? O B HOH 491 ? ? 2.09 
16 1 O    B HOH 545 ? ? O B HOH 625 ? ? 2.10 
17 1 O    A HOH 692 ? ? O A HOH 695 ? ? 2.10 
18 1 O    A HOH 426 ? ? O A HOH 544 ? ? 2.11 
19 1 O    B HOH 597 ? ? O B HOH 638 ? ? 2.12 
20 1 O    A HOH 611 ? ? O A HOH 688 ? ? 2.12 
21 1 O    B HOH 495 ? ? O B HOH 551 ? ? 2.14 
22 1 O    B HOH 306 ? ? O B HOH 486 ? ? 2.15 
23 1 O    A HOH 535 ? ? O A HOH 536 ? ? 2.16 
24 1 O    B HOH 453 ? ? O B HOH 549 ? ? 2.16 
25 1 O    A HOH 599 ? ? O A HOH 630 ? ? 2.17 
26 1 O    A HOH 442 ? ? O A HOH 519 ? ? 2.17 
27 1 O    A HOH 584 ? ? O A HOH 690 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 540 ? ? 1_555 O A HOH 564 ? ? 4_556 1.97 
2 1 O A HOH 522 ? ? 1_555 O B HOH 303 ? ? 2_556 2.08 
3 1 O A HOH 619 ? ? 1_555 O B HOH 634 ? ? 2_556 2.09 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CD A GLU 138 ? ? OE2 A GLU 138 ? ? 1.364 1.252 0.112 0.011 N 
2 1 CD B GLU 66  ? ? OE1 B GLU 66  ? ? 1.332 1.252 0.080 0.011 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 4   ? ? CZ A ARG 4   ? ? NH2 A ARG 4   ? ? 115.60 120.30 -4.70 0.50 N 
2 1 NE A ARG 61  ? ? CZ A ARG 61  ? ? NH2 A ARG 61  ? ? 123.33 120.30 3.03  0.50 N 
3 1 NE A ARG 176 ? ? CZ A ARG 176 ? ? NH1 A ARG 176 ? ? 124.40 120.30 4.10  0.50 N 
# 
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 TYR A 62 ? ? -137.58 -37.51 
2 1 TYR B 62 ? ? -132.44 -38.42 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     70 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.118 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     654 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   N 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 693 ? 6.00 . 
2 1 O ? A HOH 694 ? 6.13 . 
3 1 O ? A HOH 695 ? 6.14 . 
4 1 O ? A HOH 696 ? 6.26 . 
5 1 O ? A HOH 697 ? 6.80 . 
6 1 O ? A HOH 698 ? 6.81 . 
7 1 O ? B HOH 642 ? 5.91 . 
8 1 O ? B HOH 643 ? 6.35 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ALA 187 ? A ALA 187 
2  1 Y 1 A HIS 188 ? A HIS 188 
3  1 Y 1 A HIS 189 ? A HIS 189 
4  1 Y 1 A HIS 190 ? A HIS 190 
5  1 Y 1 A HIS 191 ? A HIS 191 
6  1 Y 1 A HIS 192 ? A HIS 192 
7  1 Y 1 A HIS 193 ? A HIS 193 
8  1 Y 1 B MET 1   ? B MET 1   
9  1 Y 1 B ASN 2   ? B ASN 2   
10 1 Y 1 B ALA 187 ? B ALA 187 
11 1 Y 1 B HIS 188 ? B HIS 188 
12 1 Y 1 B HIS 189 ? B HIS 189 
13 1 Y 1 B HIS 190 ? B HIS 190 
14 1 Y 1 B HIS 191 ? B HIS 191 
15 1 Y 1 B HIS 192 ? B HIS 192 
16 1 Y 1 B HIS 193 ? B HIS 193 
# 
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 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HEM CHA  C  N N 138 
HEM CHB  C  N N 139 
HEM CHC  C  N N 140 
HEM CHD  C  N N 141 
HEM C1A  C  Y N 142 
HEM C2A  C  Y N 143 
HEM C3A  C  Y N 144 
HEM C4A  C  Y N 145 
HEM CMA  C  N N 146 
HEM CAA  C  N N 147 
HEM CBA  C  N N 148 
HEM CGA  C  N N 149 
HEM O1A  O  N N 150 
HEM O2A  O  N N 151 
HEM C1B  C  N N 152 
HEM C2B  C  N N 153 
HEM C3B  C  N N 154 
HEM C4B  C  N N 155 
HEM CMB  C  N N 156 
HEM CAB  C  N N 157 
HEM CBB  C  N N 158 
HEM C1C  C  Y N 159 
HEM C2C  C  Y N 160 
HEM C3C  C  Y N 161 
HEM C4C  C  Y N 162 
HEM CMC  C  N N 163 
HEM CAC  C  N N 164 
HEM CBC  C  N N 165 
HEM C1D  C  N N 166 
HEM C2D  C  N N 167 
HEM C3D  C  N N 168 
HEM C4D  C  N N 169 
HEM CMD  C  N N 170 
HEM CAD  C  N N 171 
HEM CBD  C  N N 172 
HEM CGD  C  N N 173 
HEM O1D  O  N N 174 
HEM O2D  O  N N 175 
HEM NA   N  Y N 176 
HEM NB   N  N N 177 
HEM NC   N  Y N 178 
HEM ND   N  N N 179 
HEM FE   FE N N 180 
HEM HHB  H  N N 181 
HEM HHC  H  N N 182 
HEM HHD  H  N N 183 
HEM HMA  H  N N 184 
HEM HMAA H  N N 185 
HEM HMAB H  N N 186 
HEM HAA  H  N N 187 
HEM HAAA H  N N 188 
HEM HBA  H  N N 189 
HEM HBAA H  N N 190 
HEM HMB  H  N N 191 
HEM HMBA H  N N 192 
HEM HMBB H  N N 193 
HEM HAB  H  N N 194 
HEM HBB  H  N N 195 
HEM HBBA H  N N 196 
HEM HMC  H  N N 197 
HEM HMCA H  N N 198 
HEM HMCB H  N N 199 
HEM HAC  H  N N 200 
HEM HBC  H  N N 201 
HEM HBCA H  N N 202 
HEM HMD  H  N N 203 
HEM HMDA H  N N 204 
HEM HMDB H  N N 205 
HEM HAD  H  N N 206 
HEM HADA H  N N 207 
HEM HBD  H  N N 208 
HEM HBDA H  N N 209 
HEM H2A  H  N N 210 
HEM H2D  H  N N 211 
HEM HHA  H  N N 212 
HIS N    N  N N 213 
HIS CA   C  N S 214 
HIS C    C  N N 215 
HIS O    O  N N 216 
HIS CB   C  N N 217 
HIS CG   C  Y N 218 
HIS ND1  N  Y N 219 
HIS CD2  C  Y N 220 
HIS CE1  C  Y N 221 
HIS NE2  N  Y N 222 
HIS OXT  O  N N 223 
HIS H    H  N N 224 
HIS H2   H  N N 225 
HIS HA   H  N N 226 
HIS HB2  H  N N 227 
HIS HB3  H  N N 228 
HIS HD1  H  N N 229 
HIS HD2  H  N N 230 
HIS HE1  H  N N 231 
HIS HE2  H  N N 232 
HIS HXT  H  N N 233 
HOH O    O  N N 234 
HOH H1   H  N N 235 
HOH H2   H  N N 236 
ILE N    N  N N 237 
ILE CA   C  N S 238 
ILE C    C  N N 239 
ILE O    O  N N 240 
ILE CB   C  N S 241 
ILE CG1  C  N N 242 
ILE CG2  C  N N 243 
ILE CD1  C  N N 244 
ILE OXT  O  N N 245 
ILE H    H  N N 246 
ILE H2   H  N N 247 
ILE HA   H  N N 248 
ILE HB   H  N N 249 
ILE HG12 H  N N 250 
ILE HG13 H  N N 251 
ILE HG21 H  N N 252 
ILE HG22 H  N N 253 
ILE HG23 H  N N 254 
ILE HD11 H  N N 255 
ILE HD12 H  N N 256 
ILE HD13 H  N N 257 
ILE HXT  H  N N 258 
IMD N1   N  Y N 259 
IMD C2   C  Y N 260 
IMD N3   N  Y N 261 
IMD C4   C  Y N 262 
IMD C5   C  Y N 263 
IMD HN1  H  N N 264 
IMD H2   H  N N 265 
IMD HN3  H  N N 266 
IMD H4   H  N N 267 
IMD H5   H  N N 268 
LEU N    N  N N 269 
LEU CA   C  N S 270 
LEU C    C  N N 271 
LEU O    O  N N 272 
LEU CB   C  N N 273 
LEU CG   C  N N 274 
LEU CD1  C  N N 275 
LEU CD2  C  N N 276 
LEU OXT  O  N N 277 
LEU H    H  N N 278 
LEU H2   H  N N 279 
LEU HA   H  N N 280 
LEU HB2  H  N N 281 
LEU HB3  H  N N 282 
LEU HG   H  N N 283 
LEU HD11 H  N N 284 
LEU HD12 H  N N 285 
LEU HD13 H  N N 286 
LEU HD21 H  N N 287 
LEU HD22 H  N N 288 
LEU HD23 H  N N 289 
LEU HXT  H  N N 290 
LYS N    N  N N 291 
LYS CA   C  N S 292 
LYS C    C  N N 293 
LYS O    O  N N 294 
LYS CB   C  N N 295 
LYS CG   C  N N 296 
LYS CD   C  N N 297 
LYS CE   C  N N 298 
LYS NZ   N  N N 299 
LYS OXT  O  N N 300 
LYS H    H  N N 301 
LYS H2   H  N N 302 
LYS HA   H  N N 303 
LYS HB2  H  N N 304 
LYS HB3  H  N N 305 
LYS HG2  H  N N 306 
LYS HG3  H  N N 307 
LYS HD2  H  N N 308 
LYS HD3  H  N N 309 
LYS HE2  H  N N 310 
LYS HE3  H  N N 311 
LYS HZ1  H  N N 312 
LYS HZ2  H  N N 313 
LYS HZ3  H  N N 314 
LYS HXT  H  N N 315 
MET N    N  N N 316 
MET CA   C  N S 317 
MET C    C  N N 318 
MET O    O  N N 319 
MET CB   C  N N 320 
MET CG   C  N N 321 
MET SD   S  N N 322 
MET CE   C  N N 323 
MET OXT  O  N N 324 
MET H    H  N N 325 
MET H2   H  N N 326 
MET HA   H  N N 327 
MET HB2  H  N N 328 
MET HB3  H  N N 329 
MET HG2  H  N N 330 
MET HG3  H  N N 331 
MET HE1  H  N N 332 
MET HE2  H  N N 333 
MET HE3  H  N N 334 
MET HXT  H  N N 335 
NA  NA   NA N N 336 
PHE N    N  N N 337 
PHE CA   C  N S 338 
PHE C    C  N N 339 
PHE O    O  N N 340 
PHE CB   C  N N 341 
PHE CG   C  Y N 342 
PHE CD1  C  Y N 343 
PHE CD2  C  Y N 344 
PHE CE1  C  Y N 345 
PHE CE2  C  Y N 346 
PHE CZ   C  Y N 347 
PHE OXT  O  N N 348 
PHE H    H  N N 349 
PHE H2   H  N N 350 
PHE HA   H  N N 351 
PHE HB2  H  N N 352 
PHE HB3  H  N N 353 
PHE HD1  H  N N 354 
PHE HD2  H  N N 355 
PHE HE1  H  N N 356 
PHE HE2  H  N N 357 
PHE HZ   H  N N 358 
PHE HXT  H  N N 359 
PRO N    N  N N 360 
PRO CA   C  N S 361 
PRO C    C  N N 362 
PRO O    O  N N 363 
PRO CB   C  N N 364 
PRO CG   C  N N 365 
PRO CD   C  N N 366 
PRO OXT  O  N N 367 
PRO H    H  N N 368 
PRO HA   H  N N 369 
PRO HB2  H  N N 370 
PRO HB3  H  N N 371 
PRO HG2  H  N N 372 
PRO HG3  H  N N 373 
PRO HD2  H  N N 374 
PRO HD3  H  N N 375 
PRO HXT  H  N N 376 
SER N    N  N N 377 
SER CA   C  N S 378 
SER C    C  N N 379 
SER O    O  N N 380 
SER CB   C  N N 381 
SER OG   O  N N 382 
SER OXT  O  N N 383 
SER H    H  N N 384 
SER H2   H  N N 385 
SER HA   H  N N 386 
SER HB2  H  N N 387 
SER HB3  H  N N 388 
SER HG   H  N N 389 
SER HXT  H  N N 390 
THR N    N  N N 391 
THR CA   C  N S 392 
THR C    C  N N 393 
THR O    O  N N 394 
THR CB   C  N R 395 
THR OG1  O  N N 396 
THR CG2  C  N N 397 
THR OXT  O  N N 398 
THR H    H  N N 399 
THR H2   H  N N 400 
THR HA   H  N N 401 
THR HB   H  N N 402 
THR HG1  H  N N 403 
THR HG21 H  N N 404 
THR HG22 H  N N 405 
THR HG23 H  N N 406 
THR HXT  H  N N 407 
TRP N    N  N N 408 
TRP CA   C  N S 409 
TRP C    C  N N 410 
TRP O    O  N N 411 
TRP CB   C  N N 412 
TRP CG   C  Y N 413 
TRP CD1  C  Y N 414 
TRP CD2  C  Y N 415 
TRP NE1  N  Y N 416 
TRP CE2  C  Y N 417 
TRP CE3  C  Y N 418 
TRP CZ2  C  Y N 419 
TRP CZ3  C  Y N 420 
TRP CH2  C  Y N 421 
TRP OXT  O  N N 422 
TRP H    H  N N 423 
TRP H2   H  N N 424 
TRP HA   H  N N 425 
TRP HB2  H  N N 426 
TRP HB3  H  N N 427 
TRP HD1  H  N N 428 
TRP HE1  H  N N 429 
TRP HE3  H  N N 430 
TRP HZ2  H  N N 431 
TRP HZ3  H  N N 432 
TRP HH2  H  N N 433 
TRP HXT  H  N N 434 
TYR N    N  N N 435 
TYR CA   C  N S 436 
TYR C    C  N N 437 
TYR O    O  N N 438 
TYR CB   C  N N 439 
TYR CG   C  Y N 440 
TYR CD1  C  Y N 441 
TYR CD2  C  Y N 442 
TYR CE1  C  Y N 443 
TYR CE2  C  Y N 444 
TYR CZ   C  Y N 445 
TYR OH   O  N N 446 
TYR OXT  O  N N 447 
TYR H    H  N N 448 
TYR H2   H  N N 449 
TYR HA   H  N N 450 
TYR HB2  H  N N 451 
TYR HB3  H  N N 452 
TYR HD1  H  N N 453 
TYR HD2  H  N N 454 
TYR HE1  H  N N 455 
TYR HE2  H  N N 456 
TYR HH   H  N N 457 
TYR HXT  H  N N 458 
VAL N    N  N N 459 
VAL CA   C  N S 460 
VAL C    C  N N 461 
VAL O    O  N N 462 
VAL CB   C  N N 463 
VAL CG1  C  N N 464 
VAL CG2  C  N N 465 
VAL OXT  O  N N 466 
VAL H    H  N N 467 
VAL H2   H  N N 468 
VAL HA   H  N N 469 
VAL HB   H  N N 470 
VAL HG11 H  N N 471 
VAL HG12 H  N N 472 
VAL HG13 H  N N 473 
VAL HG21 H  N N 474 
VAL HG22 H  N N 475 
VAL HG23 H  N N 476 
VAL HXT  H  N N 477 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HEM CHA C1A  sing N N 129 
HEM CHA C4D  doub N N 130 
HEM CHA HHA  sing N N 131 
HEM CHB C4A  sing N N 132 
HEM CHB C1B  doub N N 133 
HEM CHB HHB  sing N N 134 
HEM CHC C4B  sing N N 135 
HEM CHC C1C  doub N N 136 
HEM CHC HHC  sing N N 137 
HEM CHD C4C  doub N N 138 
HEM CHD C1D  sing N N 139 
HEM CHD HHD  sing N N 140 
HEM C1A C2A  doub Y N 141 
HEM C1A NA   sing Y N 142 
HEM C2A C3A  sing Y N 143 
HEM C2A CAA  sing N N 144 
HEM C3A C4A  doub Y N 145 
HEM C3A CMA  sing N N 146 
HEM C4A NA   sing Y N 147 
HEM CMA HMA  sing N N 148 
HEM CMA HMAA sing N N 149 
HEM CMA HMAB sing N N 150 
HEM CAA CBA  sing N N 151 
HEM CAA HAA  sing N N 152 
HEM CAA HAAA sing N N 153 
HEM CBA CGA  sing N N 154 
HEM CBA HBA  sing N N 155 
HEM CBA HBAA sing N N 156 
HEM CGA O1A  doub N N 157 
HEM CGA O2A  sing N N 158 
HEM C1B C2B  sing N N 159 
HEM C1B NB   sing N N 160 
HEM C2B C3B  doub N N 161 
HEM C2B CMB  sing N N 162 
HEM C3B C4B  sing N N 163 
HEM C3B CAB  sing N N 164 
HEM C4B NB   doub N N 165 
HEM CMB HMB  sing N N 166 
HEM CMB HMBA sing N N 167 
HEM CMB HMBB sing N N 168 
HEM CAB CBB  doub N N 169 
HEM CAB HAB  sing N N 170 
HEM CBB HBB  sing N N 171 
HEM CBB HBBA sing N N 172 
HEM C1C C2C  sing Y N 173 
HEM C1C NC   sing Y N 174 
HEM C2C C3C  doub Y N 175 
HEM C2C CMC  sing N N 176 
HEM C3C C4C  sing Y N 177 
HEM C3C CAC  sing N N 178 
HEM C4C NC   sing Y N 179 
HEM CMC HMC  sing N N 180 
HEM CMC HMCA sing N N 181 
HEM CMC HMCB sing N N 182 
HEM CAC CBC  doub N N 183 
HEM CAC HAC  sing N N 184 
HEM CBC HBC  sing N N 185 
HEM CBC HBCA sing N N 186 
HEM C1D C2D  sing N N 187 
HEM C1D ND   doub N N 188 
HEM C2D C3D  doub N N 189 
HEM C2D CMD  sing N N 190 
HEM C3D C4D  sing N N 191 
HEM C3D CAD  sing N N 192 
HEM C4D ND   sing N N 193 
HEM CMD HMD  sing N N 194 
HEM CMD HMDA sing N N 195 
HEM CMD HMDB sing N N 196 
HEM CAD CBD  sing N N 197 
HEM CAD HAD  sing N N 198 
HEM CAD HADA sing N N 199 
HEM CBD CGD  sing N N 200 
HEM CBD HBD  sing N N 201 
HEM CBD HBDA sing N N 202 
HEM CGD O1D  doub N N 203 
HEM CGD O2D  sing N N 204 
HEM O2A H2A  sing N N 205 
HEM O2D H2D  sing N N 206 
HEM FE  NA   sing N N 207 
HEM FE  NB   sing N N 208 
HEM FE  NC   sing N N 209 
HEM FE  ND   sing N N 210 
HIS N   CA   sing N N 211 
HIS N   H    sing N N 212 
HIS N   H2   sing N N 213 
HIS CA  C    sing N N 214 
HIS CA  CB   sing N N 215 
HIS CA  HA   sing N N 216 
HIS C   O    doub N N 217 
HIS C   OXT  sing N N 218 
HIS CB  CG   sing N N 219 
HIS CB  HB2  sing N N 220 
HIS CB  HB3  sing N N 221 
HIS CG  ND1  sing Y N 222 
HIS CG  CD2  doub Y N 223 
HIS ND1 CE1  doub Y N 224 
HIS ND1 HD1  sing N N 225 
HIS CD2 NE2  sing Y N 226 
HIS CD2 HD2  sing N N 227 
HIS CE1 NE2  sing Y N 228 
HIS CE1 HE1  sing N N 229 
HIS NE2 HE2  sing N N 230 
HIS OXT HXT  sing N N 231 
HOH O   H1   sing N N 232 
HOH O   H2   sing N N 233 
ILE N   CA   sing N N 234 
ILE N   H    sing N N 235 
ILE N   H2   sing N N 236 
ILE CA  C    sing N N 237 
ILE CA  CB   sing N N 238 
ILE CA  HA   sing N N 239 
ILE C   O    doub N N 240 
ILE C   OXT  sing N N 241 
ILE CB  CG1  sing N N 242 
ILE CB  CG2  sing N N 243 
ILE CB  HB   sing N N 244 
ILE CG1 CD1  sing N N 245 
ILE CG1 HG12 sing N N 246 
ILE CG1 HG13 sing N N 247 
ILE CG2 HG21 sing N N 248 
ILE CG2 HG22 sing N N 249 
ILE CG2 HG23 sing N N 250 
ILE CD1 HD11 sing N N 251 
ILE CD1 HD12 sing N N 252 
ILE CD1 HD13 sing N N 253 
ILE OXT HXT  sing N N 254 
IMD N1  C2   sing Y N 255 
IMD N1  C5   sing Y N 256 
IMD N1  HN1  sing N N 257 
IMD C2  N3   doub Y N 258 
IMD C2  H2   sing N N 259 
IMD N3  C4   sing Y N 260 
IMD N3  HN3  sing N N 261 
IMD C4  C5   doub Y N 262 
IMD C4  H4   sing N N 263 
IMD C5  H5   sing N N 264 
LEU N   CA   sing N N 265 
LEU N   H    sing N N 266 
LEU N   H2   sing N N 267 
LEU CA  C    sing N N 268 
LEU CA  CB   sing N N 269 
LEU CA  HA   sing N N 270 
LEU C   O    doub N N 271 
LEU C   OXT  sing N N 272 
LEU CB  CG   sing N N 273 
LEU CB  HB2  sing N N 274 
LEU CB  HB3  sing N N 275 
LEU CG  CD1  sing N N 276 
LEU CG  CD2  sing N N 277 
LEU CG  HG   sing N N 278 
LEU CD1 HD11 sing N N 279 
LEU CD1 HD12 sing N N 280 
LEU CD1 HD13 sing N N 281 
LEU CD2 HD21 sing N N 282 
LEU CD2 HD22 sing N N 283 
LEU CD2 HD23 sing N N 284 
LEU OXT HXT  sing N N 285 
LYS N   CA   sing N N 286 
LYS N   H    sing N N 287 
LYS N   H2   sing N N 288 
LYS CA  C    sing N N 289 
LYS CA  CB   sing N N 290 
LYS CA  HA   sing N N 291 
LYS C   O    doub N N 292 
LYS C   OXT  sing N N 293 
LYS CB  CG   sing N N 294 
LYS CB  HB2  sing N N 295 
LYS CB  HB3  sing N N 296 
LYS CG  CD   sing N N 297 
LYS CG  HG2  sing N N 298 
LYS CG  HG3  sing N N 299 
LYS CD  CE   sing N N 300 
LYS CD  HD2  sing N N 301 
LYS CD  HD3  sing N N 302 
LYS CE  NZ   sing N N 303 
LYS CE  HE2  sing N N 304 
LYS CE  HE3  sing N N 305 
LYS NZ  HZ1  sing N N 306 
LYS NZ  HZ2  sing N N 307 
LYS NZ  HZ3  sing N N 308 
LYS OXT HXT  sing N N 309 
MET N   CA   sing N N 310 
MET N   H    sing N N 311 
MET N   H2   sing N N 312 
MET CA  C    sing N N 313 
MET CA  CB   sing N N 314 
MET CA  HA   sing N N 315 
MET C   O    doub N N 316 
MET C   OXT  sing N N 317 
MET CB  CG   sing N N 318 
MET CB  HB2  sing N N 319 
MET CB  HB3  sing N N 320 
MET CG  SD   sing N N 321 
MET CG  HG2  sing N N 322 
MET CG  HG3  sing N N 323 
MET SD  CE   sing N N 324 
MET CE  HE1  sing N N 325 
MET CE  HE2  sing N N 326 
MET CE  HE3  sing N N 327 
MET OXT HXT  sing N N 328 
PHE N   CA   sing N N 329 
PHE N   H    sing N N 330 
PHE N   H2   sing N N 331 
PHE CA  C    sing N N 332 
PHE CA  CB   sing N N 333 
PHE CA  HA   sing N N 334 
PHE C   O    doub N N 335 
PHE C   OXT  sing N N 336 
PHE CB  CG   sing N N 337 
PHE CB  HB2  sing N N 338 
PHE CB  HB3  sing N N 339 
PHE CG  CD1  doub Y N 340 
PHE CG  CD2  sing Y N 341 
PHE CD1 CE1  sing Y N 342 
PHE CD1 HD1  sing N N 343 
PHE CD2 CE2  doub Y N 344 
PHE CD2 HD2  sing N N 345 
PHE CE1 CZ   doub Y N 346 
PHE CE1 HE1  sing N N 347 
PHE CE2 CZ   sing Y N 348 
PHE CE2 HE2  sing N N 349 
PHE CZ  HZ   sing N N 350 
PHE OXT HXT  sing N N 351 
PRO N   CA   sing N N 352 
PRO N   CD   sing N N 353 
PRO N   H    sing N N 354 
PRO CA  C    sing N N 355 
PRO CA  CB   sing N N 356 
PRO CA  HA   sing N N 357 
PRO C   O    doub N N 358 
PRO C   OXT  sing N N 359 
PRO CB  CG   sing N N 360 
PRO CB  HB2  sing N N 361 
PRO CB  HB3  sing N N 362 
PRO CG  CD   sing N N 363 
PRO CG  HG2  sing N N 364 
PRO CG  HG3  sing N N 365 
PRO CD  HD2  sing N N 366 
PRO CD  HD3  sing N N 367 
PRO OXT HXT  sing N N 368 
SER N   CA   sing N N 369 
SER N   H    sing N N 370 
SER N   H2   sing N N 371 
SER CA  C    sing N N 372 
SER CA  CB   sing N N 373 
SER CA  HA   sing N N 374 
SER C   O    doub N N 375 
SER C   OXT  sing N N 376 
SER CB  OG   sing N N 377 
SER CB  HB2  sing N N 378 
SER CB  HB3  sing N N 379 
SER OG  HG   sing N N 380 
SER OXT HXT  sing N N 381 
THR N   CA   sing N N 382 
THR N   H    sing N N 383 
THR N   H2   sing N N 384 
THR CA  C    sing N N 385 
THR CA  CB   sing N N 386 
THR CA  HA   sing N N 387 
THR C   O    doub N N 388 
THR C   OXT  sing N N 389 
THR CB  OG1  sing N N 390 
THR CB  CG2  sing N N 391 
THR CB  HB   sing N N 392 
THR OG1 HG1  sing N N 393 
THR CG2 HG21 sing N N 394 
THR CG2 HG22 sing N N 395 
THR CG2 HG23 sing N N 396 
THR OXT HXT  sing N N 397 
TRP N   CA   sing N N 398 
TRP N   H    sing N N 399 
TRP N   H2   sing N N 400 
TRP CA  C    sing N N 401 
TRP CA  CB   sing N N 402 
TRP CA  HA   sing N N 403 
TRP C   O    doub N N 404 
TRP C   OXT  sing N N 405 
TRP CB  CG   sing N N 406 
TRP CB  HB2  sing N N 407 
TRP CB  HB3  sing N N 408 
TRP CG  CD1  doub Y N 409 
TRP CG  CD2  sing Y N 410 
TRP CD1 NE1  sing Y N 411 
TRP CD1 HD1  sing N N 412 
TRP CD2 CE2  doub Y N 413 
TRP CD2 CE3  sing Y N 414 
TRP NE1 CE2  sing Y N 415 
TRP NE1 HE1  sing N N 416 
TRP CE2 CZ2  sing Y N 417 
TRP CE3 CZ3  doub Y N 418 
TRP CE3 HE3  sing N N 419 
TRP CZ2 CH2  doub Y N 420 
TRP CZ2 HZ2  sing N N 421 
TRP CZ3 CH2  sing Y N 422 
TRP CZ3 HZ3  sing N N 423 
TRP CH2 HH2  sing N N 424 
TRP OXT HXT  sing N N 425 
TYR N   CA   sing N N 426 
TYR N   H    sing N N 427 
TYR N   H2   sing N N 428 
TYR CA  C    sing N N 429 
TYR CA  CB   sing N N 430 
TYR CA  HA   sing N N 431 
TYR C   O    doub N N 432 
TYR C   OXT  sing N N 433 
TYR CB  CG   sing N N 434 
TYR CB  HB2  sing N N 435 
TYR CB  HB3  sing N N 436 
TYR CG  CD1  doub Y N 437 
TYR CG  CD2  sing Y N 438 
TYR CD1 CE1  sing Y N 439 
TYR CD1 HD1  sing N N 440 
TYR CD2 CE2  doub Y N 441 
TYR CD2 HD2  sing N N 442 
TYR CE1 CZ   doub Y N 443 
TYR CE1 HE1  sing N N 444 
TYR CE2 CZ   sing Y N 445 
TYR CE2 HE2  sing N N 446 
TYR CZ  OH   sing N N 447 
TYR OH  HH   sing N N 448 
TYR OXT HXT  sing N N 449 
VAL N   CA   sing N N 450 
VAL N   H    sing N N 451 
VAL N   H2   sing N N 452 
VAL CA  C    sing N N 453 
VAL CA  CB   sing N N 454 
VAL CA  HA   sing N N 455 
VAL C   O    doub N N 456 
VAL C   OXT  sing N N 457 
VAL CB  CG1  sing N N 458 
VAL CB  CG2  sing N N 459 
VAL CB  HB   sing N N 460 
VAL CG1 HG11 sing N N 461 
VAL CG1 HG12 sing N N 462 
VAL CG1 HG13 sing N N 463 
VAL CG2 HG21 sing N N 464 
VAL CG2 HG22 sing N N 465 
VAL CG2 HG23 sing N N 466 
VAL OXT HXT  sing N N 467 
# 
_pdbx_audit_support.funding_organization   iNEXT-Discovery 
_pdbx_audit_support.country                'European Union' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5k90 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9GTJ 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.007846 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006422 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.021753 
_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]   0.014334 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
FE 
H  
N  
NA 
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    . MET A 1 1   ? -23.313 -17.318 39.981 1.00 23.43  ? 1   MET A N    1 
ATOM   2    C  CA   . MET A 1 1   ? -22.906 -16.246 39.028 1.00 20.65  ? 1   MET A CA   1 
ATOM   3    C  C    . MET A 1 1   ? -22.114 -16.888 37.906 1.00 17.79  ? 1   MET A C    1 
ATOM   4    O  O    . MET A 1 1   ? -21.560 -17.946 38.109 1.00 20.81  ? 1   MET A O    1 
ATOM   5    C  CB   . MET A 1 1   ? -22.016 -15.292 39.785 1.00 18.58  ? 1   MET A CB   1 
ATOM   6    C  CG   . MET A 1 1   ? -22.766 -14.526 40.757 1.00 21.73  ? 1   MET A CG   1 
ATOM   7    S  SD   . MET A 1 1   ? -21.714 -13.397 41.549 1.00 22.93  ? 1   MET A SD   1 
ATOM   8    C  CE   . MET A 1 1   ? -21.462 -12.223 40.244 1.00 20.61  ? 1   MET A CE   1 
ATOM   9    H  H2   . MET A 1 1   ? -23.883 -17.899 39.571 1.00 23.90  ? 1   MET A H2   1 
ATOM   10   H  H3   . MET A 1 1   ? -22.579 -17.773 40.272 1.00 23.90  ? 1   MET A H3   1 
ATOM   11   H  HA   . MET A 1 1   ? -23.702 -15.789 38.674 1.00 31.10  ? 1   MET A HA   1 
ATOM   12   H  HB2  . MET A 1 1   ? -21.318 -15.800 40.241 1.00 24.19  ? 1   MET A HB2  1 
ATOM   13   H  HB3  . MET A 1 1   ? -21.586 -14.687 39.150 1.00 24.21  ? 1   MET A HB3  1 
ATOM   14   H  HG2  . MET A 1 1   ? -23.492 -14.041 40.311 1.00 25.01  ? 1   MET A HG2  1 
ATOM   15   H  HG3  . MET A 1 1   ? -23.156 -15.127 41.425 1.00 25.02  ? 1   MET A HG3  1 
ATOM   16   H  HE1  . MET A 1 1   ? -21.108 -11.405 40.612 1.00 24.65  ? 1   MET A HE1  1 
ATOM   17   H  HE2  . MET A 1 1   ? -20.838 -12.584 39.602 1.00 24.65  ? 1   MET A HE2  1 
ATOM   18   H  HE3  . MET A 1 1   ? -22.304 -12.042 39.808 1.00 24.66  ? 1   MET A HE3  1 
ATOM   19   N  N    . ASN A 1 2   ? -22.064 -16.189 36.785 1.00 21.56  ? 2   ASN A N    1 
ATOM   20   C  CA   . ASN A 1 2   ? -21.256 -16.572 35.672 1.00 20.61  ? 2   ASN A CA   1 
ATOM   21   C  C    . ASN A 1 2   ? -19.873 -15.948 35.883 1.00 18.60  ? 2   ASN A C    1 
ATOM   22   O  O    . ASN A 1 2   ? -19.791 -14.706 36.060 1.00 21.34  ? 2   ASN A O    1 
ATOM   23   C  CB   . ASN A 1 2   ? -21.975 -16.089 34.407 1.00 21.96  ? 2   ASN A CB   1 
ATOM   24   C  CG   . ASN A 1 2   ? -21.282 -16.512 33.133 1.00 20.70  ? 2   ASN A CG   1 
ATOM   25   O  OD1  . ASN A 1 2   ? -20.081 -16.615 33.079 1.00 27.21  ? 2   ASN A OD1  1 
ATOM   26   N  ND2  . ASN A 1 2   ? -22.024 -16.762 32.089 1.00 27.03  ? 2   ASN A ND2  1 
ATOM   27   H  H    . ASN A 1 2   ? -22.564 -15.427 36.718 1.00 30.67  ? 2   ASN A H    1 
ATOM   28   H  HA   . ASN A 1 2   ? -21.184 -17.549 35.643 1.00 39.95  ? 2   ASN A HA   1 
ATOM   29   H  HB2  . ASN A 1 2   ? -22.887 -16.444 34.406 1.00 30.21  ? 2   ASN A HB2  1 
ATOM   30   H  HB3  . ASN A 1 2   ? -22.031 -15.112 34.428 1.00 30.22  ? 2   ASN A HB3  1 
ATOM   31   H  HD21 . ASN A 1 2   ? -22.818 -16.382 32.009 1.00 29.98  ? 2   ASN A HD21 1 
ATOM   32   H  HD22 . ASN A 1 2   ? -21.733 -17.312 31.460 1.00 29.98  ? 2   ASN A HD22 1 
ATOM   33   N  N    . THR A 1 3   ? -18.803 -16.782 35.788 1.00 15.71  ? 3   THR A N    1 
ATOM   34   C  CA   . THR A 1 3   ? -17.420 -16.308 35.962 1.00 13.50  ? 3   THR A CA   1 
ATOM   35   C  C    . THR A 1 3   ? -16.875 -15.541 34.746 1.00 12.05  ? 3   THR A C    1 
ATOM   36   O  O    . THR A 1 3   ? -15.722 -15.137 34.726 1.00 14.17  ? 3   THR A O    1 
ATOM   37   C  CB   . THR A 1 3   ? -16.434 -17.446 36.265 1.00 14.57  ? 3   THR A CB   1 
ATOM   38   O  OG1  . THR A 1 3   ? -16.390 -18.333 35.154 1.00 18.59  ? 3   THR A OG1  1 
ATOM   39   C  CG2  . THR A 1 3   ? -16.778 -18.180 37.537 1.00 17.09  ? 3   THR A CG2  1 
ATOM   40   H  H    . THR A 1 3   ? -18.943 -17.668 35.609 1.00 39.94  ? 3   THR A H    1 
ATOM   41   H  HA   . THR A 1 3   ? -17.416 -15.694 36.732 1.00 16.21  ? 3   THR A HA   1 
ATOM   42   H  HB   . THR A 1 3   ? -15.538 -17.047 36.376 1.00 17.43  ? 3   THR A HB   1 
ATOM   43   H  HG1  . THR A 1 3   ? -15.762 -18.893 35.260 1.00 20.63  ? 3   THR A HG1  1 
ATOM   44   H  HG21 . THR A 1 3   ? -16.094 -18.848 37.724 1.00 20.63  ? 3   THR A HG21 1 
ATOM   45   H  HG22 . THR A 1 3   ? -16.822 -17.547 38.276 1.00 20.63  ? 3   THR A HG22 1 
ATOM   46   H  HG23 . THR A 1 3   ? -17.641 -18.619 37.437 1.00 20.63  ? 3   THR A HG23 1 
ATOM   47   N  N    . ARG A 1 4   ? -17.690 -15.305 33.749 1.00 10.84  ? 4   ARG A N    1 
ATOM   48   C  CA   . ARG A 1 4   ? -17.264 -14.688 32.503 1.00 9.80   ? 4   ARG A CA   1 
ATOM   49   C  C    . ARG A 1 4   ? -17.686 -13.229 32.366 1.00 9.23   ? 4   ARG A C    1 
ATOM   50   O  O    . ARG A 1 4   ? -17.078 -12.511 31.571 1.00 9.62   ? 4   ARG A O    1 
ATOM   51   C  CB   . ARG A 1 4   ? -17.806 -15.493 31.333 1.00 10.48  ? 4   ARG A CB   1 
ATOM   52   C  CG   . ARG A 1 4   ? -17.297 -16.929 31.281 1.00 11.21  ? 4   ARG A CG   1 
ATOM   53   C  CD   . ARG A 1 4   ? -18.214 -17.810 30.389 1.00 13.85  ? 4   ARG A CD   1 
ATOM   54   N  NE   . ARG A 1 4   ? -18.246 -17.276 29.078 1.00 13.14  ? 4   ARG A NE   1 
ATOM   55   C  CZ   . ARG A 1 4   ? -19.287 -17.222 28.281 1.00 10.46  ? 4   ARG A CZ   1 
ATOM   56   N  NH1  . ARG A 1 4   ? -20.431 -17.873 28.529 1.00 11.46  ? 4   ARG A NH1  1 
ATOM   57   N  NH2  . ARG A 1 4   ? -19.140 -16.494 27.213 1.00 11.19  ? 4   ARG A NH2  1 
ATOM   58   H  H    . ARG A 1 4   ? -18.566 -15.551 33.827 1.00 13.17  ? 4   ARG A H    1 
ATOM   59   H  HA   . ARG A 1 4   ? -16.280 -14.723 32.466 1.00 11.98  ? 4   ARG A HA   1 
ATOM   60   H  HB2  . ARG A 1 4   ? -18.783 -15.502 31.384 1.00 13.37  ? 4   ARG A HB2  1 
ATOM   61   H  HB3  . ARG A 1 4   ? -17.554 -15.040 30.501 1.00 13.37  ? 4   ARG A HB3  1 
ATOM   62   H  HG2  . ARG A 1 4   ? -16.385 -16.942 30.920 1.00 14.62  ? 4   ARG A HG2  1 
ATOM   63   H  HG3  . ARG A 1 4   ? -17.273 -17.304 32.187 1.00 14.62  ? 4   ARG A HG3  1 
ATOM   64   H  HD2  . ARG A 1 4   ? -17.870 -18.728 30.365 1.00 38.82  ? 4   ARG A HD2  1 
ATOM   65   H  HD3  . ARG A 1 4   ? -19.120 -17.828 30.764 1.00 38.81  ? 4   ARG A HD3  1 
ATOM   66   H  HE   . ARG A 1 4   ? -17.496 -16.956 28.766 1.00 23.05  ? 4   ARG A HE   1 
ATOM   67   H  HH11 . ARG A 1 4   ? -20.409 -18.711 28.800 1.00 31.57  ? 4   ARG A HH11 1 
ATOM   68   H  HH12 . ARG A 1 4   ? -21.202 -17.461 28.420 1.00 31.57  ? 4   ARG A HH12 1 
ATOM   69   H  HH21 . ARG A 1 4   ? -18.631 -15.776 27.235 1.00 23.05  ? 4   ARG A HH21 1 
ATOM   70   H  HH22 . ARG A 1 4   ? -19.553 -16.720 26.471 1.00 23.05  ? 4   ARG A HH22 1 
ATOM   71   N  N    . VAL A 1 5   ? -18.712 -12.799 33.105 1.00 9.77   ? 5   VAL A N    1 
ATOM   72   C  CA   . VAL A 1 5   ? -19.255 -11.458 32.961 1.00 10.19  ? 5   VAL A CA   1 
ATOM   73   C  C    . VAL A 1 5   ? -18.593 -10.543 33.980 1.00 9.70   ? 5   VAL A C    1 
ATOM   74   O  O    . VAL A 1 5   ? -18.472 -10.881 35.152 1.00 10.20  ? 5   VAL A O    1 
ATOM   75   C  CB   . VAL A 1 5   ? -20.777 -11.435 33.183 1.00 11.61  ? 5   VAL A CB   1 
ATOM   76   C  CG1  . VAL A 1 5   ? -21.334 -10.036 33.140 1.00 12.82  ? 5   VAL A CG1  1 
ATOM   77   C  CG2  . VAL A 1 5   ? -21.488 -12.328 32.174 1.00 12.53  ? 5   VAL A CG2  1 
ATOM   78   H  H    . VAL A 1 5   ? -19.089 -13.358 33.721 1.00 13.17  ? 5   VAL A H    1 
ATOM   79   H  HA   . VAL A 1 5   ? -19.062 -11.132 32.065 1.00 12.22  ? 5   VAL A HA   1 
ATOM   80   H  HB   . VAL A 1 5   ? -20.950 -11.801 34.085 1.00 13.18  ? 5   VAL A HB   1 
ATOM   81   H  HG11 . VAL A 1 5   ? -22.285 -10.069 32.936 1.00 15.34  ? 5   VAL A HG11 1 
ATOM   82   H  HG12 . VAL A 1 5   ? -21.205 -9.607  34.004 1.00 15.34  ? 5   VAL A HG12 1 
ATOM   83   H  HG13 . VAL A 1 5   ? -20.874 -9.523  32.453 1.00 15.34  ? 5   VAL A HG13 1 
ATOM   84   H  HG21 . VAL A 1 5   ? -22.448 -12.292 32.326 1.00 15.34  ? 5   VAL A HG21 1 
ATOM   85   H  HG22 . VAL A 1 5   ? -21.292 -12.020 31.272 1.00 15.34  ? 5   VAL A HG22 1 
ATOM   86   H  HG23 . VAL A 1 5   ? -21.180 -13.245 32.276 1.00 15.34  ? 5   VAL A HG23 1 
ATOM   87   N  N    . PHE A 1 6   ? -18.190 -9.364  33.511 1.00 10.05  ? 6   PHE A N    1 
ATOM   88   C  CA   . PHE A 1 6   ? -17.604 -8.334  34.349 1.00 10.21  ? 6   PHE A CA   1 
ATOM   89   C  C    . PHE A 1 6   ? -18.220 -6.983  34.022 1.00 10.82  ? 6   PHE A C    1 
ATOM   90   O  O    . PHE A 1 6   ? -18.558 -6.699  32.874 1.00 11.50  ? 6   PHE A O    1 
ATOM   91   C  CB   . PHE A 1 6   ? -16.096 -8.241  34.115 1.00 11.06  ? 6   PHE A CB   1 
ATOM   92   C  CG   . PHE A 1 6   ? -15.387 -9.492  34.547 1.00 10.68  ? 6   PHE A CG   1 
ATOM   93   C  CD1  . PHE A 1 6   ? -15.255 -10.582 33.679 1.00 10.74  ? 6   PHE A CD1  1 
ATOM   94   C  CD2  . PHE A 1 6   ? -14.890 -9.612  35.821 1.00 12.19  ? 6   PHE A CD2  1 
ATOM   95   C  CE1  . PHE A 1 6   ? -14.607 -11.740 34.064 1.00 12.10  ? 6   PHE A CE1  1 
ATOM   96   C  CE2  . PHE A 1 6   ? -14.263 -10.780 36.222 1.00 13.02  ? 6   PHE A CE2  1 
ATOM   97   C  CZ   . PHE A 1 6   ? -14.121 -11.825 35.341 1.00 13.31  ? 6   PHE A CZ   1 
ATOM   98   H  H    . PHE A 1 6   ? -18.284 -9.191  32.618 1.00 12.22  ? 6   PHE A H    1 
ATOM   99   H  HA   . PHE A 1 6   ? -17.776 -8.548  35.300 1.00 12.53  ? 6   PHE A HA   1 
ATOM   100  H  HB2  . PHE A 1 6   ? -15.930 -8.086  33.162 1.00 13.48  ? 6   PHE A HB2  1 
ATOM   101  H  HB3  . PHE A 1 6   ? -15.741 -7.478  34.618 1.00 13.48  ? 6   PHE A HB3  1 
ATOM   102  H  HD1  . PHE A 1 6   ? -15.590 -10.511 32.799 1.00 15.33  ? 6   PHE A HD1  1 
ATOM   103  H  HD2  . PHE A 1 6   ? -14.983 -8.896  36.429 1.00 15.33  ? 6   PHE A HD2  1 
ATOM   104  H  HE1  . PHE A 1 6   ? -14.518 -12.465 33.465 1.00 15.33  ? 6   PHE A HE1  1 
ATOM   105  H  HE2  . PHE A 1 6   ? -13.912 -10.847 37.093 1.00 15.33  ? 6   PHE A HE2  1 
ATOM   106  H  HZ   . PHE A 1 6   ? -13.684 -12.613 35.622 1.00 15.33  ? 6   PHE A HZ   1 
ATOM   107  N  N    . THR A 1 7   ? -18.300 -6.150  35.060 1.00 10.45  ? 7   THR A N    1 
ATOM   108  C  CA   . THR A 1 7   ? -18.701 -4.765  34.907 1.00 10.79  ? 7   THR A CA   1 
ATOM   109  C  C    . THR A 1 7   ? -17.568 -3.878  35.370 1.00 10.42  ? 7   THR A C    1 
ATOM   110  O  O    . THR A 1 7   ? -17.068 -4.012  36.486 1.00 13.19  ? 7   THR A O    1 
ATOM   111  C  CB   . THR A 1 7   ? -19.974 -4.450  35.691 1.00 11.78  ? 7   THR A CB   1 
ATOM   112  O  OG1  . THR A 1 7   ? -21.027 -5.283  35.223 1.00 13.41  ? 7   THR A OG1  1 
ATOM   113  C  CG2  . THR A 1 7   ? -20.386 -3.015  35.505 1.00 14.15  ? 7   THR A CG2  1 
ATOM   114  H  H    . THR A 1 7   ? -18.096 -6.456  35.897 1.00 12.53  ? 7   THR A H    1 
ATOM   115  H  HA   . THR A 1 7   ? -18.870 -4.595  33.953 1.00 19.63  ? 7   THR A HA   1 
ATOM   116  H  HB   . THR A 1 7   ? -19.814 -4.626  36.649 1.00 14.27  ? 7   THR A HB   1 
ATOM   117  H  HG1  . THR A 1 7   ? -20.974 -6.044  35.593 1.00 17.79  ? 7   THR A HG1  1 
ATOM   118  H  HG21 . THR A 1 7   ? -21.334 -2.919  35.704 1.00 19.65  ? 7   THR A HG21 1 
ATOM   119  H  HG22 . THR A 1 7   ? -19.872 -2.447  36.106 1.00 19.64  ? 7   THR A HG22 1 
ATOM   120  H  HG23 . THR A 1 7   ? -20.220 -2.744  34.584 1.00 19.64  ? 7   THR A HG23 1 
ATOM   121  N  N    . PHE A 1 8   ? -17.199 -2.940  34.497 1.00 10.20  ? 8   PHE A N    1 
ATOM   122  C  CA   . PHE A 1 8   ? -16.219 -1.917  34.785 1.00 10.50  ? 8   PHE A CA   1 
ATOM   123  C  C    . PHE A 1 8   ? -16.987 -0.658  35.172 1.00 10.66  ? 8   PHE A C    1 
ATOM   124  O  O    . PHE A 1 8   ? -17.674 -0.061  34.335 1.00 11.82  ? 8   PHE A O    1 
ATOM   125  C  CB   . PHE A 1 8   ? -15.329 -1.681  33.550 1.00 10.97  ? 8   PHE A CB   1 
ATOM   126  C  CG   . PHE A 1 8   ? -14.494 -2.890  33.213 1.00 10.75  ? 8   PHE A CG   1 
ATOM   127  C  CD1  . PHE A 1 8   ? -15.012 -3.934  32.470 1.00 12.26  ? 8   PHE A CD1  1 
ATOM   128  C  CD2  . PHE A 1 8   ? -13.196 -3.010  33.695 1.00 12.03  ? 8   PHE A CD2  1 
ATOM   129  C  CE1  . PHE A 1 8   ? -14.224 -5.058  32.203 1.00 12.72  ? 8   PHE A CE1  1 
ATOM   130  C  CE2  . PHE A 1 8   ? -12.422 -4.121  33.442 1.00 12.80  ? 8   PHE A CE2  1 
ATOM   131  C  CZ   . PHE A 1 8   ? -12.942 -5.136  32.699 1.00 13.70  ? 8   PHE A CZ   1 
ATOM   132  H  H    . PHE A 1 8   ? -17.584 -2.942  33.668 1.00 19.63  ? 8   PHE A H    1 
ATOM   133  H  HA   . PHE A 1 8   ? -15.654 -2.204  35.546 1.00 13.19  ? 8   PHE A HA   1 
ATOM   134  H  HB2  . PHE A 1 8   ? -15.900 -1.458  32.786 1.00 16.45  ? 8   PHE A HB2  1 
ATOM   135  H  HB3  . PHE A 1 8   ? -14.740 -0.919  33.725 1.00 16.45  ? 8   PHE A HB3  1 
ATOM   136  H  HD1  . PHE A 1 8   ? -15.894 -3.884  32.138 1.00 14.88  ? 8   PHE A HD1  1 
ATOM   137  H  HD2  . PHE A 1 8   ? -12.838 -2.312  34.220 1.00 14.88  ? 8   PHE A HD2  1 
ATOM   138  H  HE1  . PHE A 1 8   ? -14.575 -5.767  31.687 1.00 14.88  ? 8   PHE A HE1  1 
ATOM   139  H  HE2  . PHE A 1 8   ? -11.539 -4.173  33.772 1.00 14.88  ? 8   PHE A HE2  1 
ATOM   140  H  HZ   . PHE A 1 8   ? -12.412 -5.893  32.508 1.00 14.88  ? 8   PHE A HZ   1 
ATOM   141  N  N    . ALA A 1 9   ? -16.896 -0.294  36.463 1.00 11.07  ? 9   ALA A N    1 
ATOM   142  C  CA   . ALA A 1 9   ? -17.693 0.805   37.015 1.00 11.97  ? 9   ALA A CA   1 
ATOM   143  C  C    . ALA A 1 9   ? -16.768 2.001   37.222 1.00 11.39  ? 9   ALA A C    1 
ATOM   144  O  O    . ALA A 1 9   ? -15.882 1.968   38.073 1.00 12.25  ? 9   ALA A O    1 
ATOM   145  C  CB   . ALA A 1 9   ? -18.342 0.364   38.309 1.00 13.92  ? 9   ALA A CB   1 
ATOM   146  H  H    . ALA A 1 9   ? -16.322 -0.741  37.017 1.00 13.19  ? 9   ALA A H    1 
ATOM   147  H  HA   . ALA A 1 9   ? -18.396 1.050   36.370 1.00 18.13  ? 9   ALA A HA   1 
ATOM   148  H  HB1  . ALA A 1 9   ? -18.863 1.097   38.678 1.00 17.16  ? 9   ALA A HB1  1 
ATOM   149  H  HB2  . ALA A 1 9   ? -18.926 -0.394  38.138 1.00 17.16  ? 9   ALA A HB2  1 
ATOM   150  H  HB3  . ALA A 1 9   ? -17.655 0.105   38.945 1.00 17.16  ? 9   ALA A HB3  1 
ATOM   151  N  N    . GLY A 1 10  ? -16.963 3.036   36.394 1.00 12.03  ? 10  GLY A N    1 
ATOM   152  C  CA   . GLY A 1 10  ? -16.185 4.261   36.502 1.00 12.75  ? 10  GLY A CA   1 
ATOM   153  C  C    . GLY A 1 10  ? -16.858 5.218   37.468 1.00 12.49  ? 10  GLY A C    1 
ATOM   154  O  O    . GLY A 1 10  ? -18.030 5.538   37.302 1.00 13.39  ? 10  GLY A O    1 
ATOM   155  H  H    . GLY A 1 10  ? -17.600 2.977   35.741 1.00 18.13  ? 10  GLY A H    1 
ATOM   156  H  HA2  . GLY A 1 10  ? -15.272 4.047   36.819 1.00 20.56  ? 10  GLY A HA2  1 
ATOM   157  H  HA3  . GLY A 1 10  ? -16.117 4.682   35.609 1.00 20.56  ? 10  GLY A HA3  1 
ATOM   158  N  N    . GLY A 1 11  ? -16.142 5.658   38.494 1.00 12.69  ? 11  GLY A N    1 
ATOM   159  C  CA   . GLY A 1 11  ? -16.806 6.450   39.513 1.00 14.37  ? 11  GLY A CA   1 
ATOM   160  C  C    . GLY A 1 11  ? -15.865 6.725   40.665 1.00 14.34  ? 11  GLY A C    1 
ATOM   161  O  O    . GLY A 1 11  ? -14.663 6.872   40.490 1.00 14.31  ? 11  GLY A O    1 
ATOM   162  H  H    . GLY A 1 11  ? -15.250 5.474   38.565 1.00 20.56  ? 11  GLY A H    1 
ATOM   163  H  HA2  . GLY A 1 11  ? -17.108 7.304   39.117 1.00 25.31  ? 11  GLY A HA2  1 
ATOM   164  H  HA3  . GLY A 1 11  ? -17.599 5.958   39.842 1.00 25.31  ? 11  GLY A HA3  1 
ATOM   165  N  N    . GLU A 1 12  ? -16.452 6.835   41.854 1.00 16.27  ? 12  GLU A N    1 
ATOM   166  C  CA   . GLU A 1 12  ? -15.710 7.302   43.013 1.00 16.82  ? 12  GLU A CA   1 
ATOM   167  C  C    . GLU A 1 12  ? -15.138 6.128   43.819 1.00 17.04  ? 12  GLU A C    1 
ATOM   168  O  O    . GLU A 1 12  ? -14.381 6.381   44.754 1.00 20.70  ? 12  GLU A O    1 
ATOM   169  C  CB   . GLU A 1 12  ? -16.601 8.218   43.865 1.00 16.33  ? 12  GLU A CB   1 
ATOM   170  C  CG   . GLU A 1 12  ? -16.885 9.571   43.227 1.00 16.90  ? 12  GLU A CG   1 
ATOM   171  C  CD   . GLU A 1 12  ? -17.809 10.463  44.048 1.00 16.82  ? 12  GLU A CD   1 
ATOM   172  O  OE1  . GLU A 1 12  ? -18.615 9.919   44.857 1.00 17.12  ? 12  GLU A OE1  1 
ATOM   173  O  OE2  . GLU A 1 12  ? -17.768 11.705  43.844 1.00 19.58  ? 12  GLU A OE2  1 
ATOM   174  H  H    . GLU A 1 12  ? -17.334 6.615   41.951 1.00 25.19  ? 12  GLU A H    1 
ATOM   175  H  HA   . GLU A 1 12  ? -14.953 7.839   42.687 1.00 19.58  ? 12  GLU A HA   1 
ATOM   176  H  HB2  . GLU A 1 12  ? -17.451 7.759   44.029 1.00 25.07  ? 12  GLU A HB2  1 
ATOM   177  H  HB3  . GLU A 1 12  ? -16.165 8.361   44.731 1.00 25.06  ? 12  GLU A HB3  1 
ATOM   178  H  HG2  . GLU A 1 12  ? -16.037 10.044  43.091 1.00 23.12  ? 12  GLU A HG2  1 
ATOM   179  H  HG3  . GLU A 1 12  ? -17.291 9.430   42.346 1.00 23.12  ? 12  GLU A HG3  1 
ATOM   180  N  N    . THR A 1 13  ? -15.429 4.878   43.445 1.00 17.79  ? 13  THR A N    1 
ATOM   181  C  CA   . THR A 1 13  ? -15.075 3.707   44.225 1.00 19.45  ? 13  THR A CA   1 
ATOM   182  C  C    . THR A 1 13  ? -14.248 2.728   43.398 1.00 17.46  ? 13  THR A C    1 
ATOM   183  O  O    . THR A 1 13  ? -14.465 2.580   42.206 1.00 17.02  ? 13  THR A O    1 
ATOM   184  C  CB   . THR A 1 13  ? -16.357 2.992   44.704 1.00 23.90  ? 13  THR A CB   1 
ATOM   185  O  OG1  . THR A 1 13  ? -17.027 3.907   45.561 1.00 31.26  ? 13  THR A OG1  1 
ATOM   186  C  CG2  . THR A 1 13  ? -16.068 1.683   45.394 1.00 28.16  ? 13  THR A CG2  1 
ATOM   187  H  H    . THR A 1 13  ? -15.874 4.749   42.658 1.00 20.85  ? 13  THR A H    1 
ATOM   188  H  HA   . THR A 1 13  ? -14.552 3.991   45.009 1.00 29.89  ? 13  THR A HA   1 
ATOM   189  H  HB   . THR A 1 13  ? -16.925 2.817   43.917 1.00 26.85  ? 13  THR A HB   1 
ATOM   190  H  HG1  . THR A 1 13  ? -17.805 3.616   45.734 1.00 28.95  ? 13  THR A HG1  1 
ATOM   191  H  HG21 . THR A 1 13  ? -16.825 1.439   45.957 1.00 28.95  ? 13  THR A HG21 1 
ATOM   192  H  HG22 . THR A 1 13  ? -15.924 0.987   44.728 1.00 28.95  ? 13  THR A HG22 1 
ATOM   193  H  HG23 . THR A 1 13  ? -15.271 1.774   45.947 1.00 28.95  ? 13  THR A HG23 1 
ATOM   194  N  N    . GLY A 1 14  ? -13.311 2.037   44.051 1.00 17.52  ? 14  GLY A N    1 
ATOM   195  C  CA   . GLY A 1 14  ? -12.645 0.875   43.490 1.00 17.30  ? 14  GLY A CA   1 
ATOM   196  C  C    . GLY A 1 14  ? -11.159 0.862   43.824 1.00 16.30  ? 14  GLY A C    1 
ATOM   197  O  O    . GLY A 1 14  ? -10.609 1.851   44.300 1.00 16.80  ? 14  GLY A O    1 
ATOM   198  H  H    . GLY A 1 14  ? -13.075 2.305   44.893 1.00 29.89  ? 14  GLY A H    1 
ATOM   199  H  HA2  . GLY A 1 14  ? -13.069 0.056   43.848 1.00 20.57  ? 14  GLY A HA2  1 
ATOM   200  H  HA3  . GLY A 1 14  ? -12.759 0.876   42.508 1.00 20.57  ? 14  GLY A HA3  1 
ATOM   201  N  N    . VAL A 1 15  ? -10.521 -0.276  43.571 1.00 15.49  ? 15  VAL A N    1 
ATOM   202  C  CA   . VAL A 1 15  ? -9.122  -0.424  43.930 1.00 15.00  ? 15  VAL A CA   1 
ATOM   203  C  C    . VAL A 1 15  ? -8.194  0.256   42.936 1.00 13.87  ? 15  VAL A C    1 
ATOM   204  O  O    . VAL A 1 15  ? -7.006  0.357   43.222 1.00 16.48  ? 15  VAL A O    1 
ATOM   205  C  CB   . VAL A 1 15  ? -8.718  -1.899  44.103 1.00 16.88  ? 15  VAL A CB   1 
ATOM   206  C  CG1  . VAL A 1 15  ? -9.557  -2.601  45.167 1.00 21.73  ? 15  VAL A CG1  1 
ATOM   207  C  CG2  . VAL A 1 15  ? -8.706  -2.694  42.801 1.00 17.99  ? 15  VAL A CG2  1 
ATOM   208  H  H    . VAL A 1 15  ? -10.959 -0.972  43.173 1.00 27.20  ? 15  VAL A H    1 
ATOM   209  H  HA   . VAL A 1 15  ? -8.996  0.013   44.791 1.00 18.02  ? 15  VAL A HA   1 
ATOM   210  H  HB   . VAL A 1 15  ? -7.787  -1.893  44.437 1.00 20.41  ? 15  VAL A HB   1 
ATOM   211  H  HG11 . VAL A 1 15  ? -9.239  -3.513  45.283 1.00 28.07  ? 15  VAL A HG11 1 
ATOM   212  H  HG12 . VAL A 1 15  ? -9.478  -2.122  46.010 1.00 28.08  ? 15  VAL A HG12 1 
ATOM   213  H  HG13 . VAL A 1 15  ? -10.488 -2.616  44.891 1.00 28.09  ? 15  VAL A HG13 1 
ATOM   214  H  HG21 . VAL A 1 15  ? -8.714  -3.646  43.000 1.00 27.22  ? 15  VAL A HG21 1 
ATOM   215  H  HG22 . VAL A 1 15  ? -9.491  -2.468  42.273 1.00 27.21  ? 15  VAL A HG22 1 
ATOM   216  H  HG23 . VAL A 1 15  ? -7.903  -2.478  42.295 1.00 27.21  ? 15  VAL A HG23 1 
ATOM   217  N  N    . TRP A 1 16  ? -8.720  0.690   41.796 1.00 12.58  ? 16  TRP A N    1 
ATOM   218  C  CA   . TRP A 1 16  ? -7.905  1.296   40.762 1.00 12.46  ? 16  TRP A CA   1 
ATOM   219  C  C    . TRP A 1 16  ? -8.118  2.805   40.766 1.00 12.15  ? 16  TRP A C    1 
ATOM   220  O  O    . TRP A 1 16  ? -9.239  3.275   40.646 1.00 13.11  ? 16  TRP A O    1 
ATOM   221  C  CB   . TRP A 1 16  ? -8.283  0.702   39.403 1.00 11.92  ? 16  TRP A CB   1 
ATOM   222  C  CG   . TRP A 1 16  ? -8.014  -0.762  39.283 1.00 11.51  ? 16  TRP A CG   1 
ATOM   223  C  CD1  . TRP A 1 16  ? -8.929  -1.760  39.364 1.00 12.97  ? 16  TRP A CD1  1 
ATOM   224  C  CD2  . TRP A 1 16  ? -6.723  -1.392  39.109 1.00 11.67  ? 16  TRP A CD2  1 
ATOM   225  N  NE1  . TRP A 1 16  ? -8.309  -2.969  39.243 1.00 13.35  ? 16  TRP A NE1  1 
ATOM   226  C  CE2  . TRP A 1 16  ? -6.966  -2.781  39.091 1.00 12.75  ? 16  TRP A CE2  1 
ATOM   227  C  CE3  . TRP A 1 16  ? -5.405  -0.924  38.957 1.00 12.44  ? 16  TRP A CE3  1 
ATOM   228  C  CZ2  . TRP A 1 16  ? -5.938  -3.703  38.907 1.00 13.18  ? 16  TRP A CZ2  1 
ATOM   229  C  CZ3  . TRP A 1 16  ? -4.398  -1.841  38.771 1.00 12.26  ? 16  TRP A CZ3  1 
ATOM   230  C  CH2  . TRP A 1 16  ? -4.657  -3.212  38.762 1.00 13.12  ? 16  TRP A CH2  1 
ATOM   231  H  H    . TRP A 1 16  ? -9.616  0.596   41.646 1.00 15.05  ? 16  TRP A H    1 
ATOM   232  H  HA   . TRP A 1 16  ? -6.958  1.093   40.941 1.00 17.44  ? 16  TRP A HA   1 
ATOM   233  H  HB2  . TRP A 1 16  ? -9.235  0.865   39.251 1.00 16.18  ? 16  TRP A HB2  1 
ATOM   234  H  HB3  . TRP A 1 16  ? -7.784  1.178   38.710 1.00 16.17  ? 16  TRP A HB3  1 
ATOM   235  H  HD1  . TRP A 1 16  ? -9.857  -1.643  39.499 1.00 15.93  ? 16  TRP A HD1  1 
ATOM   236  H  HE1  . TRP A 1 16  ? -8.714  -3.747  39.263 1.00 15.93  ? 16  TRP A HE1  1 
ATOM   237  H  HE3  . TRP A 1 16  ? -5.220  0.002   38.967 1.00 15.93  ? 16  TRP A HE3  1 
ATOM   238  H  HZ2  . TRP A 1 16  ? -6.113  -4.629  38.890 1.00 15.93  ? 16  TRP A HZ2  1 
ATOM   239  H  HZ3  . TRP A 1 16  ? -3.509  -1.540  38.681 1.00 15.93  ? 16  TRP A HZ3  1 
ATOM   240  H  HH2  . TRP A 1 16  ? -3.945  -3.815  38.643 1.00 15.93  ? 16  TRP A HH2  1 
ATOM   241  N  N    . ARG A 1 17  ? -7.012  3.545   40.866 1.00 12.26  ? 17  ARG A N    1 
ATOM   242  C  CA   . ARG A 1 17  ? -7.020  4.983   40.721 1.00 12.74  ? 17  ARG A CA   1 
ATOM   243  C  C    . ARG A 1 17  ? -6.785  5.332   39.264 1.00 11.90  ? 17  ARG A C    1 
ATOM   244  O  O    . ARG A 1 17  ? -5.825  4.863   38.667 1.00 12.80  ? 17  ARG A O    1 
ATOM   245  C  CB   . ARG A 1 17  ? -5.914  5.583   41.592 1.00 14.74  ? 17  ARG A CB   1 
ATOM   246  C  CG   . ARG A 1 17  ? -5.816  7.096   41.482 1.00 19.43  ? 17  ARG A CG   1 
ATOM   247  C  CD   . ARG A 1 17  ? -4.507  7.682   41.996 1.00 24.32  ? 17  ARG A CD   1 
ATOM   248  N  NE   . ARG A 1 17  ? -4.102  7.056   43.250 1.00 30.24  ? 17  ARG A NE   1 
ATOM   249  C  CZ   . ARG A 1 17  ? -3.100  6.186   43.376 1.00 33.88  ? 17  ARG A CZ   1 
ATOM   250  N  NH1  . ARG A 1 17  ? -2.238  6.043   42.378 1.00 39.30  ? 17  ARG A NH1  1 
ATOM   251  N  NH2  . ARG A 1 17  ? -2.944  5.495   44.502 1.00 24.56  ? 17  ARG A NH2  1 
ATOM   252  H  H    . ARG A 1 17  ? -6.215  3.130   41.032 1.00 17.44  ? 17  ARG A H    1 
ATOM   253  H  HA   . ARG A 1 17  ? -7.894  5.335   41.010 1.00 19.71  ? 17  ARG A HA   1 
ATOM   254  H  HB2  . ARG A 1 17  ? -6.084  5.341   42.526 1.00 17.44  ? 17  ARG A HB2  1 
ATOM   255  H  HB3  . ARG A 1 17  ? -5.057  5.188   41.328 1.00 17.44  ? 17  ARG A HB3  1 
ATOM   256  H  HG2  . ARG A 1 17  ? -5.924  7.357   40.544 1.00 21.25  ? 17  ARG A HG2  1 
ATOM   257  H  HG3  . ARG A 1 17  ? -6.555  7.497   41.987 1.00 21.25  ? 17  ARG A HG3  1 
ATOM   258  H  HD2  . ARG A 1 17  ? -3.808  7.554   41.321 1.00 24.21  ? 17  ARG A HD2  1 
ATOM   259  H  HD3  . ARG A 1 17  ? -4.617  8.646   42.137 1.00 24.22  ? 17  ARG A HD3  1 
ATOM   260  H  HE   . ARG A 1 17  ? -4.546  7.267   43.970 1.00 26.66  ? 17  ARG A HE   1 
ATOM   261  H  HH11 . ARG A 1 17  ? -1.864  6.752   42.013 1.00 23.93  ? 17  ARG A HH11 1 
ATOM   262  H  HH12 . ARG A 1 17  ? -2.040  5.238   42.085 1.00 23.91  ? 17  ARG A HH12 1 
ATOM   263  H  HH21 . ARG A 1 17  ? -3.540  5.561   45.145 1.00 26.66  ? 17  ARG A HH21 1 
ATOM   264  H  HH22 . ARG A 1 17  ? -2.244  4.972   44.600 1.00 26.66  ? 17  ARG A HH22 1 
ATOM   265  N  N    . VAL A 1 18  ? -7.646  6.169   38.692 1.00 12.27  ? 18  VAL A N    1 
ATOM   266  C  CA   . VAL A 1 18  ? -7.471  6.608   37.325 1.00 12.52  ? 18  VAL A CA   1 
ATOM   267  C  C    . VAL A 1 18  ? -6.418  7.700   37.242 1.00 13.31  ? 18  VAL A C    1 
ATOM   268  O  O    . VAL A 1 18  ? -6.498  8.722   37.920 1.00 15.36  ? 18  VAL A O    1 
ATOM   269  C  CB   . VAL A 1 18  ? -8.790  7.116   36.732 1.00 13.57  ? 18  VAL A CB   1 
ATOM   270  C  CG1  . VAL A 1 18  ? -8.566  7.690   35.334 1.00 13.94  ? 18  VAL A CG1  1 
ATOM   271  C  CG2  . VAL A 1 18  ? -9.828  6.024   36.746 1.00 14.12  ? 18  VAL A CG2  1 
ATOM   272  H  H    . VAL A 1 18  ? -8.360  6.481   39.170 1.00 19.71  ? 18  VAL A H    1 
ATOM   273  H  HA   . VAL A 1 18  ? -7.172  5.848   36.795 1.00 21.34  ? 18  VAL A HA   1 
ATOM   274  H  HB   . VAL A 1 18  ? -9.113  7.849   37.312 1.00 16.82  ? 18  VAL A HB   1 
ATOM   275  H  HG11 . VAL A 1 18  ? -9.400  7.657   34.833 1.00 16.68  ? 18  VAL A HG11 1 
ATOM   276  H  HG12 . VAL A 1 18  ? -8.269  8.614   35.404 1.00 16.68  ? 18  VAL A HG12 1 
ATOM   277  H  HG13 . VAL A 1 18  ? -7.890  7.166   34.871 1.00 16.68  ? 18  VAL A HG13 1 
ATOM   278  H  HG21 . VAL A 1 18  ? -10.700 6.404   36.544 1.00 19.73  ? 18  VAL A HG21 1 
ATOM   279  H  HG22 . VAL A 1 18  ? -9.605  5.354   36.076 1.00 19.72  ? 18  VAL A HG22 1 
ATOM   280  H  HG23 . VAL A 1 18  ? -9.855  5.607   37.624 1.00 19.72  ? 18  VAL A HG23 1 
ATOM   281  N  N    . VAL A 1 19  ? -5.407  7.487   36.397 1.00 12.57  ? 19  VAL A N    1 
ATOM   282  C  CA   . VAL A 1 19  ? -4.358  8.476   36.195 1.00 14.30  ? 19  VAL A CA   1 
ATOM   283  C  C    . VAL A 1 19  ? -4.463  9.162   34.838 1.00 15.08  ? 19  VAL A C    1 
ATOM   284  O  O    . VAL A 1 19  ? -3.940  10.250  34.711 1.00 20.06  ? 19  VAL A O    1 
ATOM   285  C  CB   . VAL A 1 19  ? -2.974  7.897   36.505 1.00 17.56  ? 19  VAL A CB   1 
ATOM   286  C  CG1  . VAL A 1 19  ? -2.893  7.401   37.930 1.00 18.95  ? 19  VAL A CG1  1 
ATOM   287  C  CG2  . VAL A 1 19  ? -2.511  6.832   35.573 1.00 19.19  ? 19  VAL A CG2  1 
ATOM   288  H  H    . VAL A 1 19  ? -5.364  6.698   35.936 1.00 21.34  ? 19  VAL A H    1 
ATOM   289  H  HA   . VAL A 1 19  ? -4.509  9.173   36.857 1.00 21.25  ? 19  VAL A HA   1 
ATOM   290  H  HB   . VAL A 1 19  ? -2.333  8.646   36.426 1.00 20.35  ? 19  VAL A HB   1 
ATOM   291  H  HG11 . VAL A 1 19  ? -1.971  7.176   38.144 1.00 21.25  ? 19  VAL A HG11 1 
ATOM   292  H  HG12 . VAL A 1 19  ? -3.205  8.096   38.535 1.00 21.25  ? 19  VAL A HG12 1 
ATOM   293  H  HG13 . VAL A 1 19  ? -3.451  6.610   38.031 1.00 21.25  ? 19  VAL A HG13 1 
ATOM   294  H  HG21 . VAL A 1 19  ? -1.642  6.506   35.861 1.00 21.34  ? 19  VAL A HG21 1 
ATOM   295  H  HG22 . VAL A 1 19  ? -3.148  6.097   35.575 1.00 21.34  ? 19  VAL A HG22 1 
ATOM   296  H  HG23 . VAL A 1 19  ? -2.437  7.194   34.673 1.00 21.34  ? 19  VAL A HG23 1 
ATOM   297  N  N    . ALA A 1 20  ? -5.115  8.582   33.847 1.00 14.09  ? 20  ALA A N    1 
ATOM   298  C  CA   . ALA A 1 20  ? -5.245  9.225   32.556 1.00 15.10  ? 20  ALA A CA   1 
ATOM   299  C  C    . ALA A 1 20  ? -6.441  8.635   31.839 1.00 14.46  ? 20  ALA A C    1 
ATOM   300  O  O    . ALA A 1 20  ? -6.728  7.461   32.026 1.00 13.91  ? 20  ALA A O    1 
ATOM   301  C  CB   . ALA A 1 20  ? -3.987  9.059   31.721 1.00 18.70  ? 20  ALA A CB   1 
ATOM   302  H  H    . ALA A 1 20  ? -5.488  7.757   33.970 1.00 21.34  ? 20  ALA A H    1 
ATOM   303  H  HA   . ALA A 1 20  ? -5.409  10.187  32.698 1.00 17.73  ? 20  ALA A HA   1 
ATOM   304  H  HB1  . ALA A 1 20  ? -4.109  9.490   30.859 1.00 27.23  ? 20  ALA A HB1  1 
ATOM   305  H  HB2  . ALA A 1 20  ? -3.235  9.468   32.182 1.00 27.25  ? 20  ALA A HB2  1 
ATOM   306  H  HB3  . ALA A 1 20  ? -3.808  8.113   31.587 1.00 27.23  ? 20  ALA A HB3  1 
ATOM   307  N  N    . MET A 1 21  ? -7.101  9.430   30.999 1.00 14.99  ? 21  MET A N    1 
ATOM   308  C  CA   . MET A 1 21  ? -8.114  8.961   30.070 1.00 15.51  ? 21  MET A CA   1 
ATOM   309  C  C    . MET A 1 21  ? -7.839  9.585   28.706 1.00 14.87  ? 21  MET A C    1 
ATOM   310  O  O    . MET A 1 21  ? -8.030  10.800  28.535 1.00 19.31  ? 21  MET A O    1 
ATOM   311  C  CB   . MET A 1 21  ? -9.531  9.300   30.531 1.00 17.17  ? 21  MET A CB   1 
ATOM   312  C  CG   . MET A 1 21  ? -9.762  8.801   31.966 1.00 20.90  ? 21  MET A CG   1 
ATOM   313  S  SD   . MET A 1 21  ? -11.384 9.204   32.599 1.00 23.93  ? 21  MET A SD   1 
ATOM   314  C  CE   . MET A 1 21  ? -12.467 8.249   31.503 1.00 20.48  ? 21  MET A CE   1 
ATOM   315  H  H    . MET A 1 21  ? -6.908  10.323  31.007 1.00 17.73  ? 21  MET A H    1 
ATOM   316  H  HA   . MET A 1 21  ? -8.027  7.984   29.988 1.00 18.54  ? 21  MET A HA   1 
ATOM   317  H  HB2  . MET A 1 21  ? -9.661  10.268  30.496 1.00 25.15  ? 21  MET A HB2  1 
ATOM   318  H  HB3  . MET A 1 21  ? -10.176 8.880   29.929 1.00 25.15  ? 21  MET A HB3  1 
ATOM   319  H  HG2  . MET A 1 21  ? -9.646  7.827   31.990 1.00 25.76  ? 21  MET A HG2  1 
ATOM   320  H  HG3  . MET A 1 21  ? -9.089  9.199   32.558 1.00 25.76  ? 21  MET A HG3  1 
ATOM   321  H  HE1  . MET A 1 21  ? -13.360 8.235   31.867 1.00 25.16  ? 21  MET A HE1  1 
ATOM   322  H  HE2  . MET A 1 21  ? -12.482 8.659   30.629 1.00 25.16  ? 21  MET A HE2  1 
ATOM   323  H  HE3  . MET A 1 21  ? -12.134 7.347   31.429 1.00 25.16  ? 21  MET A HE3  1 
ATOM   324  N  N    . ASN A 1 22  ? -7.332  8.783   27.780 1.00 15.45  ? 22  ASN A N    1 
ATOM   325  C  CA   . ASN A 1 22  ? -6.844  9.203   26.488 1.00 16.94  ? 22  ASN A CA   1 
ATOM   326  C  C    . ASN A 1 22  ? -7.945  8.944   25.464 1.00 15.40  ? 22  ASN A C    1 
ATOM   327  O  O    . ASN A 1 22  ? -8.309  7.803   25.257 1.00 15.26  ? 22  ASN A O    1 
ATOM   328  C  CB   . ASN A 1 22  ? -5.553  8.437   26.155 1.00 16.65  ? 22  ASN A CB   1 
ATOM   329  C  CG   . ASN A 1 22  ? -4.486  8.596   27.211 1.00 18.81  ? 22  ASN A CG   1 
ATOM   330  O  OD1  . ASN A 1 22  ? -4.106  7.613   27.889 1.00 22.32  ? 22  ASN A OD1  1 
ATOM   331  N  ND2  . ASN A 1 22  ? -4.081  9.838   27.401 1.00 19.67  ? 22  ASN A ND2  1 
ATOM   332  H  H    . ASN A 1 22  ? -7.291  7.891   27.974 1.00 18.54  ? 22  ASN A H    1 
ATOM   333  H  HA   . ASN A 1 22  ? -6.637  10.166  26.516 1.00 24.57  ? 22  ASN A HA   1 
ATOM   334  H  HB2  . ASN A 1 22  ? -5.765  7.489   26.057 1.00 25.89  ? 22  ASN A HB2  1 
ATOM   335  H  HB3  . ASN A 1 22  ? -5.205  8.760   25.300 1.00 25.92  ? 22  ASN A HB3  1 
ATOM   336  H  HD21 . ASN A 1 22  ? -4.220  10.450  26.778 1.00 24.11  ? 22  ASN A HD21 1 
ATOM   337  H  HD22 . ASN A 1 22  ? -3.669  10.059  28.151 1.00 24.11  ? 22  ASN A HD22 1 
ATOM   338  N  N    . ALA A 1 23  ? -8.432  10.003  24.826 1.00 17.14  ? 23  ALA A N    1 
ATOM   339  C  CA   . ALA A 1 23  ? -9.477  9.893   23.847 1.00 16.97  ? 23  ALA A CA   1 
ATOM   340  C  C    . ALA A 1 23  ? -8.866  9.542   22.480 1.00 14.88  ? 23  ALA A C    1 
ATOM   341  O  O    . ALA A 1 23  ? -8.733  10.412  21.636 1.00 15.99  ? 23  ALA A O    1 
ATOM   342  C  CB   . ALA A 1 23  ? -10.188 11.257  23.806 1.00 20.54  ? 23  ALA A CB   1 
ATOM   343  H  H    . ALA A 1 23  ? -8.091  10.831  25.012 1.00 24.57  ? 23  ALA A H    1 
ATOM   344  H  HA   . ALA A 1 23  ? -10.111 9.191   24.119 1.00 18.71  ? 23  ALA A HA   1 
ATOM   345  H  HB1  . ALA A 1 23  ? -10.970 11.199  23.232 1.00 22.19  ? 23  ALA A HB1  1 
ATOM   346  H  HB2  . ALA A 1 23  ? -10.464 11.506  24.704 1.00 22.19  ? 23  ALA A HB2  1 
ATOM   347  H  HB3  . ALA A 1 23  ? -9.581  11.932  23.458 1.00 22.19  ? 23  ALA A HB3  1 
ATOM   348  N  N    . VAL A 1 24  ? -8.543  8.297   22.191 1.00 14.51  ? 24  VAL A N    1 
ATOM   349  C  CA   . VAL A 1 24  ? -7.731  7.933   21.041 1.00 13.57  ? 24  VAL A CA   1 
ATOM   350  C  C    . VAL A 1 24  ? -8.485  8.076   19.721 1.00 13.73  ? 24  VAL A C    1 
ATOM   351  O  O    . VAL A 1 24  ? -7.959  8.649   18.779 1.00 14.84  ? 24  VAL A O    1 
ATOM   352  C  CB   . VAL A 1 24  ? -7.159  6.517   21.235 1.00 15.45  ? 24  VAL A CB   1 
ATOM   353  C  CG1  . VAL A 1 24  ? -6.355  6.090   20.039 1.00 16.24  ? 24  VAL A CG1  1 
ATOM   354  C  CG2  . VAL A 1 24  ? -6.296  6.441   22.493 1.00 16.74  ? 24  VAL A CG2  1 
ATOM   355  H  H    . VAL A 1 24  ? -8.851  7.629   22.735 1.00 16.04  ? 24  VAL A H    1 
ATOM   356  H  HA   . VAL A 1 24  ? -6.977  8.549   21.013 1.00 16.73  ? 24  VAL A HA   1 
ATOM   357  H  HB   . VAL A 1 24  ? -7.918  5.891   21.340 1.00 18.88  ? 24  VAL A HB   1 
ATOM   358  H  HG11 . VAL A 1 24  ? -5.777  5.346   20.282 1.00 15.68  ? 24  VAL A HG11 1 
ATOM   359  H  HG12 . VAL A 1 24  ? -6.956  5.810   19.327 1.00 15.67  ? 24  VAL A HG12 1 
ATOM   360  H  HG13 . VAL A 1 24  ? -5.811  6.835   19.730 1.00 15.68  ? 24  VAL A HG13 1 
ATOM   361  H  HG21 . VAL A 1 24  ? -5.856  5.574   22.534 1.00 16.04  ? 24  VAL A HG21 1 
ATOM   362  H  HG22 . VAL A 1 24  ? -5.623  7.144   22.468 1.00 16.04  ? 24  VAL A HG22 1 
ATOM   363  H  HG23 . VAL A 1 24  ? -6.856  6.557   23.280 1.00 16.04  ? 24  VAL A HG23 1 
ATOM   364  N  N    . ALA A 1 25  ? -9.713  7.566   19.667 1.00 13.30  ? 25  ALA A N    1 
ATOM   365  C  CA   . ALA A 1 25  ? -10.555 7.677   18.493 1.00 13.34  ? 25  ALA A CA   1 
ATOM   366  C  C    . ALA A 1 25  ? -11.979 7.873   18.951 1.00 12.17  ? 25  ALA A C    1 
ATOM   367  O  O    . ALA A 1 25  ? -12.470 7.100   19.772 1.00 12.22  ? 25  ALA A O    1 
ATOM   368  C  CB   . ALA A 1 25  ? -10.474 6.463   17.621 1.00 14.35  ? 25  ALA A CB   1 
ATOM   369  H  H    . ALA A 1 25  ? -10.039 7.121   20.397 1.00 16.10  ? 25  ALA A H    1 
ATOM   370  H  HA   . ALA A 1 25  ? -10.277 8.467   17.973 1.00 15.82  ? 25  ALA A HA   1 
ATOM   371  H  HB1  . ALA A 1 25  ? -11.046 6.582   16.844 1.00 17.52  ? 25  ALA A HB1  1 
ATOM   372  H  HB2  . ALA A 1 25  ? -9.556  6.332   17.330 1.00 17.52  ? 25  ALA A HB2  1 
ATOM   373  H  HB3  . ALA A 1 25  ? -10.768 5.683   18.122 1.00 17.52  ? 25  ALA A HB3  1 
ATOM   374  N  N    . GLY A 1 26  ? -12.660 8.865   18.403 1.00 12.80  ? 26  GLY A N    1 
ATOM   375  C  CA   . GLY A 1 26  ? -14.041 9.090   18.747 1.00 12.55  ? 26  GLY A CA   1 
ATOM   376  C  C    . GLY A 1 26  ? -14.188 9.715   20.120 1.00 11.65  ? 26  GLY A C    1 
ATOM   377  O  O    . GLY A 1 26  ? -13.227 10.189  20.743 1.00 12.55  ? 26  GLY A O    1 
ATOM   378  H  H    . GLY A 1 26  ? -12.257 9.418   17.797 1.00 15.82  ? 26  GLY A H    1 
ATOM   379  H  HA2  . GLY A 1 26  ? -14.448 9.687   18.070 1.00 15.19  ? 26  GLY A HA2  1 
ATOM   380  H  HA3  . GLY A 1 26  ? -14.523 8.227   18.725 1.00 15.19  ? 26  GLY A HA3  1 
ATOM   381  N  N    . ALA A 1 27  ? -15.439 9.788   20.579 1.00 11.37  ? 27  ALA A N    1 
ATOM   382  C  CA   . ALA A 1 27  ? -15.712 10.551  21.790 1.00 11.70  ? 27  ALA A CA   1 
ATOM   383  C  C    . ALA A 1 27  ? -15.245 9.803   23.031 1.00 12.32  ? 27  ALA A C    1 
ATOM   384  O  O    . ALA A 1 27  ? -15.421 8.594   23.151 1.00 12.81  ? 27  ALA A O    1 
ATOM   385  C  CB   . ALA A 1 27  ? -17.184 10.855  21.916 1.00 11.97  ? 27  ALA A CB   1 
ATOM   386  H  H    . ALA A 1 27  ? -16.123 9.364   20.145 1.00 14.27  ? 27  ALA A H    1 
ATOM   387  H  HA   . ALA A 1 27  ? -15.222 11.402  21.733 1.00 17.74  ? 27  ALA A HA   1 
ATOM   388  H  HB1  . ALA A 1 27  ? -17.362 11.248  22.786 1.00 14.27  ? 27  ALA A HB1  1 
ATOM   389  H  HB2  . ALA A 1 27  ? -17.447 11.481  21.219 1.00 14.27  ? 27  ALA A HB2  1 
ATOM   390  H  HB3  . ALA A 1 27  ? -17.695 10.034  21.822 1.00 14.27  ? 27  ALA A HB3  1 
ATOM   391  N  N    . PRO A 1 28  ? -14.701 10.515  24.018 1.00 13.34  ? 28  PRO A N    1 
ATOM   392  C  CA   . PRO A 1 28  ? -14.326 9.850   25.271 1.00 13.71  ? 28  PRO A CA   1 
ATOM   393  C  C    . PRO A 1 28  ? -15.529 9.659   26.174 1.00 12.93  ? 28  PRO A C    1 
ATOM   394  O  O    . PRO A 1 28  ? -16.630 10.132  25.922 1.00 15.70  ? 28  PRO A O    1 
ATOM   395  C  CB   . PRO A 1 28  ? -13.304 10.787  25.860 1.00 17.64  ? 28  PRO A CB   1 
ATOM   396  C  CG   . PRO A 1 28  ? -13.847 12.111  25.430 1.00 16.72  ? 28  PRO A CG   1 
ATOM   397  C  CD   . PRO A 1 28  ? -14.356 11.941  23.997 1.00 15.29  ? 28  PRO A CD   1 
ATOM   398  H  HA   . PRO A 1 28  ? -13.901 8.978   25.074 1.00 19.19  ? 28  PRO A HA   1 
ATOM   399  H  HB2  . PRO A 1 28  ? -13.267 10.715  26.837 1.00 22.19  ? 28  PRO A HB2  1 
ATOM   400  H  HB3  . PRO A 1 28  ? -12.413 10.627  25.486 1.00 22.19  ? 28  PRO A HB3  1 
ATOM   401  H  HG2  . PRO A 1 28  ? -14.577 12.389  26.020 1.00 19.07  ? 28  PRO A HG2  1 
ATOM   402  H  HG3  . PRO A 1 28  ? -13.146 12.794  25.463 1.00 19.07  ? 28  PRO A HG3  1 
ATOM   403  H  HD2  . PRO A 1 28  ? -15.137 12.497  23.822 1.00 17.74  ? 28  PRO A HD2  1 
ATOM   404  H  HD3  . PRO A 1 28  ? -13.661 12.133  23.341 1.00 17.74  ? 28  PRO A HD3  1 
ATOM   405  N  N    . LEU A 1 29  ? -15.287 8.978   27.279 1.00 13.44  ? 29  LEU A N    1 
ATOM   406  C  CA   . LEU A 1 29  ? -16.233 8.773   28.339 1.00 13.73  ? 29  LEU A CA   1 
ATOM   407  C  C    . LEU A 1 29  ? -16.055 9.884   29.358 1.00 13.75  ? 29  LEU A C    1 
ATOM   408  O  O    . LEU A 1 29  ? -14.973 10.468  29.474 1.00 14.88  ? 29  LEU A O    1 
ATOM   409  C  CB   . LEU A 1 29  ? -15.943 7.420   28.999 1.00 15.17  ? 29  LEU A CB   1 
ATOM   410  C  CG   . LEU A 1 29  ? -16.344 6.213   28.172 1.00 16.55  ? 29  LEU A CG   1 
ATOM   411  C  CD1  . LEU A 1 29  ? -15.605 4.964   28.642 1.00 18.68  ? 29  LEU A CD1  1 
ATOM   412  C  CD2  . LEU A 1 29  ? -17.844 6.025   28.247 1.00 19.20  ? 29  LEU A CD2  1 
ATOM   413  H  H    . LEU A 1 29  ? -14.452 8.621   27.381 1.00 19.19  ? 29  LEU A H    1 
ATOM   414  H  HA   . LEU A 1 29  ? -17.145 8.791   27.973 1.00 26.17  ? 29  LEU A HA   1 
ATOM   415  H  HB2  . LEU A 1 29  ? -14.985 7.365   29.188 1.00 20.72  ? 29  LEU A HB2  1 
ATOM   416  H  HB3  . LEU A 1 29  ? -16.416 7.384   29.854 1.00 20.80  ? 29  LEU A HB3  1 
ATOM   417  H  HG   . LEU A 1 29  ? -16.102 6.384   27.231 1.00 17.78  ? 29  LEU A HG   1 
ATOM   418  H  HD11 . LEU A 1 29  ? -15.860 4.207   28.086 1.00 20.16  ? 29  LEU A HD11 1 
ATOM   419  H  HD12 . LEU A 1 29  ? -14.645 5.108   28.571 1.00 20.17  ? 29  LEU A HD12 1 
ATOM   420  H  HD13 . LEU A 1 29  ? -15.837 4.778   29.569 1.00 20.17  ? 29  LEU A HD13 1 
ATOM   421  H  HD21 . LEU A 1 29  ? -18.095 5.222   27.758 1.00 23.25  ? 29  LEU A HD21 1 
ATOM   422  H  HD22 . LEU A 1 29  ? -18.114 5.934   29.177 1.00 23.22  ? 29  LEU A HD22 1 
ATOM   423  H  HD23 . LEU A 1 29  ? -18.289 6.795   27.854 1.00 23.28  ? 29  LEU A HD23 1 
ATOM   424  N  N    . PRO A 1 30  ? -17.088 10.161  30.171 1.00 14.53  ? 30  PRO A N    1 
ATOM   425  C  CA   . PRO A 1 30  ? -16.943 11.111  31.262 1.00 15.59  ? 30  PRO A CA   1 
ATOM   426  C  C    . PRO A 1 30  ? -15.760 10.761  32.157 1.00 13.98  ? 30  PRO A C    1 
ATOM   427  O  O    . PRO A 1 30  ? -15.535 9.594   32.475 1.00 13.97  ? 30  PRO A O    1 
ATOM   428  C  CB   . PRO A 1 30  ? -18.270 10.920  32.015 1.00 17.15  ? 30  PRO A CB   1 
ATOM   429  C  CG   . PRO A 1 30  ? -19.260 10.528  30.961 1.00 19.02  ? 30  PRO A CG   1 
ATOM   430  C  CD   . PRO A 1 30  ? -18.454 9.654   30.014 1.00 15.23  ? 30  PRO A CD   1 
ATOM   431  H  HA   . PRO A 1 30  ? -16.872 12.034  30.911 1.00 17.76  ? 30  PRO A HA   1 
ATOM   432  H  HB2  . PRO A 1 30  ? -18.189 10.215  32.693 1.00 20.34  ? 30  PRO A HB2  1 
ATOM   433  H  HB3  . PRO A 1 30  ? -18.544 11.752  32.456 1.00 20.34  ? 30  PRO A HB3  1 
ATOM   434  H  HG2  . PRO A 1 30  ? -20.005 10.027  31.350 1.00 37.17  ? 30  PRO A HG2  1 
ATOM   435  H  HG3  . PRO A 1 30  ? -19.613 11.315  30.500 1.00 37.15  ? 30  PRO A HG3  1 
ATOM   436  H  HD2  . PRO A 1 30  ? -18.510 8.714   30.266 1.00 29.11  ? 30  PRO A HD2  1 
ATOM   437  H  HD3  . PRO A 1 30  ? -18.764 9.757   29.095 1.00 29.11  ? 30  PRO A HD3  1 
ATOM   438  N  N    . GLY A 1 31  ? -15.035 11.786  32.589 1.00 14.72  ? 31  GLY A N    1 
ATOM   439  C  CA   . GLY A 1 31  ? -13.926 11.615  33.504 1.00 15.35  ? 31  GLY A CA   1 
ATOM   440  C  C    . GLY A 1 31  ? -14.366 11.017  34.829 1.00 15.13  ? 31  GLY A C    1 
ATOM   441  O  O    . GLY A 1 31  ? -15.443 11.320  35.326 1.00 17.12  ? 31  GLY A O    1 
ATOM   442  H  H    . GLY A 1 31  ? -15.238 12.630  32.302 1.00 17.76  ? 31  GLY A H    1 
ATOM   443  H  HA2  . GLY A 1 31  ? -13.255 11.028  33.083 1.00 18.20  ? 31  GLY A HA2  1 
ATOM   444  H  HA3  . GLY A 1 31  ? -13.505 12.496  33.666 1.00 18.20  ? 31  GLY A HA3  1 
ATOM   445  N  N    . ILE A 1 32  ? -13.486 10.162  35.350 1.00 15.11  ? 32  ILE A N    1 
ATOM   446  C  CA   . ILE A 1 32  ? -13.703 9.380   36.542 1.00 16.15  ? 32  ILE A CA   1 
ATOM   447  C  C    . ILE A 1 32  ? -12.448 9.375   37.390 1.00 15.13  ? 32  ILE A C    1 
ATOM   448  O  O    . ILE A 1 32  ? -11.371 9.256   36.856 1.00 15.66  ? 32  ILE A O    1 
ATOM   449  C  CB   . ILE A 1 32  ? -14.057 7.903   36.178 1.00 16.64  ? 32  ILE A CB   1 
ATOM   450  C  CG1  . ILE A 1 32  ? -13.123 7.237   35.142 1.00 15.96  ? 32  ILE A CG1  1 
ATOM   451  C  CG2  . ILE A 1 32  ? -15.492 7.877   35.731 1.00 16.85  ? 32  ILE A CG2  1 
ATOM   452  C  CD1  . ILE A 1 32  ? -13.095 5.733   35.196 1.00 16.56  ? 32  ILE A CD1  1 
ATOM   453  H  H    . ILE A 1 32  ? -12.684 10.066  34.922 1.00 18.20  ? 32  ILE A H    1 
ATOM   454  H  HA   . ILE A 1 32  ? -14.435 9.767   37.051 1.00 22.25  ? 32  ILE A HA   1 
ATOM   455  H  HB   . ILE A 1 32  ? -13.997 7.372   37.010 1.00 20.53  ? 32  ILE A HB   1 
ATOM   456  H  HG12 . ILE A 1 32  ? -13.409 7.511   34.244 1.00 19.60  ? 32  ILE A HG12 1 
ATOM   457  H  HG13 . ILE A 1 32  ? -12.212 7.571   35.277 1.00 19.60  ? 32  ILE A HG13 1 
ATOM   458  H  HG21 . ILE A 1 32  ? -15.732 6.975   35.457 1.00 20.95  ? 32  ILE A HG21 1 
ATOM   459  H  HG22 . ILE A 1 32  ? -16.068 8.155   36.464 1.00 20.98  ? 32  ILE A HG22 1 
ATOM   460  H  HG23 . ILE A 1 32  ? -15.612 8.483   34.979 1.00 20.96  ? 32  ILE A HG23 1 
ATOM   461  H  HD11 . ILE A 1 32  ? -12.500 5.394   34.505 1.00 20.27  ? 32  ILE A HD11 1 
ATOM   462  H  HD12 . ILE A 1 32  ? -12.775 5.444   36.068 1.00 20.26  ? 32  ILE A HD12 1 
ATOM   463  H  HD13 . ILE A 1 32  ? -13.991 5.386   35.050 1.00 20.28  ? 32  ILE A HD13 1 
ATOM   464  N  N    . PRO A 1 33  ? -12.566 9.374   38.729 1.00 14.32  ? 33  PRO A N    1 
ATOM   465  C  CA   . PRO A 1 33  ? -11.364 9.252   39.559 1.00 14.35  ? 33  PRO A CA   1 
ATOM   466  C  C    . PRO A 1 33  ? -10.919 7.824   39.865 1.00 13.13  ? 33  PRO A C    1 
ATOM   467  O  O    . PRO A 1 33  ? -9.718  7.611   40.112 1.00 13.28  ? 33  PRO A O    1 
ATOM   468  C  CB   . PRO A 1 33  ? -11.716 9.965   40.868 1.00 16.12  ? 33  PRO A CB   1 
ATOM   469  C  CG   . PRO A 1 33  ? -13.197 9.816   40.929 1.00 16.71  ? 33  PRO A CG   1 
ATOM   470  C  CD   . PRO A 1 33  ? -13.702 9.884   39.501 1.00 16.19  ? 33  PRO A CD   1 
ATOM   471  H  HA   . PRO A 1 33  ? -10.622 9.741   39.122 1.00 16.92  ? 33  PRO A HA   1 
ATOM   472  H  HB2  . PRO A 1 33  ? -11.285 9.535   41.637 1.00 18.59  ? 33  PRO A HB2  1 
ATOM   473  H  HB3  . PRO A 1 33  ? -11.457 10.911  40.838 1.00 18.59  ? 33  PRO A HB3  1 
ATOM   474  H  HG2  . PRO A 1 33  ? -13.437 8.960   41.336 1.00 19.58  ? 33  PRO A HG2  1 
ATOM   475  H  HG3  . PRO A 1 33  ? -13.591 10.535  41.464 1.00 19.58  ? 33  PRO A HG3  1 
ATOM   476  H  HD2  . PRO A 1 33  ? -14.490 9.324   39.377 1.00 23.59  ? 33  PRO A HD2  1 
ATOM   477  H  HD3  . PRO A 1 33  ? -13.918 10.800  39.245 1.00 23.59  ? 33  PRO A HD3  1 
ATOM   478  N  N    . ARG A 1 34  ? -11.848 6.858   39.836 1.00 12.75  ? 34  ARG A N    1 
ATOM   479  C  CA   . ARG A 1 34  ? -11.535 5.483   40.199 1.00 12.93  ? 34  ARG A CA   1 
ATOM   480  C  C    . ARG A 1 34  ? -12.309 4.515   39.328 1.00 12.01  ? 34  ARG A C    1 
ATOM   481  O  O    . ARG A 1 34  ? -13.259 4.881   38.662 1.00 12.74  ? 34  ARG A O    1 
ATOM   482  C  CB   . ARG A 1 34  ? -11.867 5.242   41.668 1.00 14.52  ? 34  ARG A CB   1 
ATOM   483  C  CG   . ARG A 1 34  ? -11.156 6.207   42.603 1.00 17.22  ? 34  ARG A CG   1 
ATOM   484  C  CD   . ARG A 1 34  ? -11.148 5.756   44.038 1.00 20.12  ? 34  ARG A CD   1 
ATOM   485  N  NE   . ARG A 1 34  ? -10.241 4.640   44.244 1.00 20.38  ? 34  ARG A NE   1 
ATOM   486  C  CZ   . ARG A 1 34  ? -8.929  4.733   44.444 1.00 23.71  ? 34  ARG A CZ   1 
ATOM   487  N  NH1  . ARG A 1 34  ? -8.329  5.910   44.436 1.00 27.51  ? 34  ARG A NH1  1 
ATOM   488  N  NH2  . ARG A 1 34  ? -8.227  3.626   44.616 1.00 24.17  ? 34  ARG A NH2  1 
ATOM   489  H  H    . ARG A 1 34  ? -12.704 7.063   39.588 1.00 15.33  ? 34  ARG A H    1 
ATOM   490  H  HA   . ARG A 1 34  ? -10.573 5.333   40.059 1.00 15.43  ? 34  ARG A HA   1 
ATOM   491  H  HB2  . ARG A 1 34  ? -12.835 5.332   41.791 1.00 17.34  ? 34  ARG A HB2  1 
ATOM   492  H  HB3  . ARG A 1 34  ? -11.614 4.325   41.902 1.00 17.34  ? 34  ARG A HB3  1 
ATOM   493  H  HG2  . ARG A 1 34  ? -10.230 6.318   42.304 1.00 30.21  ? 34  ARG A HG2  1 
ATOM   494  H  HG3  . ARG A 1 34  ? -11.594 7.083   42.552 1.00 30.21  ? 34  ARG A HG3  1 
ATOM   495  H  HD2  . ARG A 1 34  ? -10.882 6.502   44.614 1.00 36.23  ? 34  ARG A HD2  1 
ATOM   496  H  HD3  . ARG A 1 34  ? -12.054 5.485   44.297 1.00 36.23  ? 34  ARG A HD3  1 
ATOM   497  H  HE   . ARG A 1 34  ? -10.586 3.839   44.236 1.00 25.67  ? 34  ARG A HE   1 
ATOM   498  H  HH11 . ARG A 1 34  ? -8.444  6.459   43.757 1.00 30.23  ? 34  ARG A HH11 1 
ATOM   499  H  HH12 . ARG A 1 34  ? -7.811  6.141   45.110 1.00 30.23  ? 34  ARG A HH12 1 
ATOM   500  H  HH21 . ARG A 1 34  ? -8.558  2.968   45.095 1.00 25.67  ? 34  ARG A HH21 1 
ATOM   501  H  HH22 . ARG A 1 34  ? -7.431  3.552   44.251 1.00 25.67  ? 34  ARG A HH22 1 
ATOM   502  N  N    . LEU A 1 35  ? -11.857 3.256   39.364 1.00 12.26  ? 35  LEU A N    1 
ATOM   503  C  CA   . LEU A 1 35  ? -12.491 2.177   38.621 1.00 12.16  ? 35  LEU A CA   1 
ATOM   504  C  C    . LEU A 1 35  ? -12.622 0.955   39.522 1.00 11.93  ? 35  LEU A C    1 
ATOM   505  O  O    . LEU A 1 35  ? -11.672 0.564   40.196 1.00 12.66  ? 35  LEU A O    1 
ATOM   506  C  CB   . LEU A 1 35  ? -11.639 1.893   37.376 1.00 12.34  ? 35  LEU A CB   1 
ATOM   507  C  CG   . LEU A 1 35  ? -12.215 0.847   36.421 1.00 14.46  ? 35  LEU A CG   1 
ATOM   508  C  CD1  . LEU A 1 35  ? -13.316 1.464   35.561 1.00 15.66  ? 35  LEU A CD1  1 
ATOM   509  C  CD2  . LEU A 1 35  ? -11.117 0.268   35.543 1.00 15.94  ? 35  LEU A CD2  1 
ATOM   510  H  H    . LEU A 1 35  ? -11.122 3.063   39.873 1.00 15.43  ? 35  LEU A H    1 
ATOM   511  H  HA   . LEU A 1 35  ? -13.388 2.469   38.345 1.00 16.45  ? 35  LEU A HA   1 
ATOM   512  H  HB2  . LEU A 1 35  ? -11.521 2.730   36.886 1.00 16.40  ? 35  LEU A HB2  1 
ATOM   513  H  HB3  . LEU A 1 35  ? -10.755 1.594   37.669 1.00 16.39  ? 35  LEU A HB3  1 
ATOM   514  H  HG   . LEU A 1 35  ? -12.608 0.113   36.955 1.00 17.30  ? 35  LEU A HG   1 
ATOM   515  H  HD11 . LEU A 1 35  ? -13.679 0.787   34.963 1.00 16.45  ? 35  LEU A HD11 1 
ATOM   516  H  HD12 . LEU A 1 35  ? -14.025 1.804   36.134 1.00 16.45  ? 35  LEU A HD12 1 
ATOM   517  H  HD13 . LEU A 1 35  ? -12.946 2.195   35.035 1.00 16.45  ? 35  LEU A HD13 1 
ATOM   518  H  HD21 . LEU A 1 35  ? -11.505 -0.360  34.909 1.00 16.56  ? 35  LEU A HD21 1 
ATOM   519  H  HD22 . LEU A 1 35  ? -10.675 0.987   35.059 1.00 16.56  ? 35  LEU A HD22 1 
ATOM   520  H  HD23 . LEU A 1 35  ? -10.466 -0.195  36.099 1.00 16.55  ? 35  LEU A HD23 1 
ATOM   521  N  N    . ASN A 1 36  ? -13.808 0.347   39.486 1.00 12.48  ? 36  ASN A N    1 
ATOM   522  C  CA   . ASN A 1 36  ? -14.088 -0.918  40.148 1.00 13.86  ? 36  ASN A CA   1 
ATOM   523  C  C    . ASN A 1 36  ? -14.367 -1.965  39.076 1.00 12.31  ? 36  ASN A C    1 
ATOM   524  O  O    . ASN A 1 36  ? -15.213 -1.740  38.219 1.00 13.95  ? 36  ASN A O    1 
ATOM   525  C  CB   . ASN A 1 36  ? -15.313 -0.780  41.072 1.00 15.33  ? 36  ASN A CB   1 
ATOM   526  C  CG   . ASN A 1 36  ? -15.716 -2.062  41.793 1.00 17.63  ? 36  ASN A CG   1 
ATOM   527  O  OD1  . ASN A 1 36  ? -16.881 -2.435  41.912 1.00 23.16  ? 36  ASN A OD1  1 
ATOM   528  N  ND2  . ASN A 1 36  ? -14.749 -2.824  42.247 1.00 17.91  ? 36  ASN A ND2  1 
ATOM   529  H  H    . ASN A 1 36  ? -14.487 0.744   39.020 1.00 16.45  ? 36  ASN A H    1 
ATOM   530  H  HA   . ASN A 1 36  ? -13.309 -1.189  40.688 1.00 38.56  ? 36  ASN A HA   1 
ATOM   531  H  HB2  . ASN A 1 36  ? -15.121 -0.091  41.741 1.00 17.17  ? 36  ASN A HB2  1 
ATOM   532  H  HB3  . ASN A 1 36  ? -16.072 -0.470  40.537 1.00 17.17  ? 36  ASN A HB3  1 
ATOM   533  H  HD21 . ASN A 1 36  ? -14.105 -2.474  42.740 1.00 40.64  ? 36  ASN A HD21 1 
ATOM   534  H  HD22 . ASN A 1 36  ? -14.741 -3.687  42.058 1.00 40.64  ? 36  ASN A HD22 1 
ATOM   535  N  N    . VAL A 1 37  ? -13.711 -3.128  39.149 1.00 12.20  ? 37  VAL A N    1 
ATOM   536  C  CA   . VAL A 1 37  ? -13.979 -4.240  38.241 1.00 11.86  ? 37  VAL A CA   1 
ATOM   537  C  C    . VAL A 1 37  ? -14.781 -5.275  39.015 1.00 12.19  ? 37  VAL A C    1 
ATOM   538  O  O    . VAL A 1 37  ? -14.228 -6.004  39.822 1.00 15.90  ? 37  VAL A O    1 
ATOM   539  C  CB   . VAL A 1 37  ? -12.722 -4.870  37.634 1.00 13.38  ? 37  VAL A CB   1 
ATOM   540  C  CG1  . VAL A 1 37  ? -13.123 -5.884  36.561 1.00 14.12  ? 37  VAL A CG1  1 
ATOM   541  C  CG2  . VAL A 1 37  ? -11.796 -3.798  37.085 1.00 15.12  ? 37  VAL A CG2  1 
ATOM   542  H  H    . VAL A 1 37  ? -13.069 -3.235  39.790 1.00 38.56  ? 37  VAL A H    1 
ATOM   543  H  HA   . VAL A 1 37  ? -14.532 -3.910  37.511 1.00 20.27  ? 37  VAL A HA   1 
ATOM   544  H  HB   . VAL A 1 37  ? -12.245 -5.352  38.353 1.00 16.61  ? 37  VAL A HB   1 
ATOM   545  H  HG11 . VAL A 1 37  ? -12.349 -6.100  36.014 1.00 20.27  ? 37  VAL A HG11 1 
ATOM   546  H  HG12 . VAL A 1 37  ? -13.453 -6.694  36.986 1.00 20.27  ? 37  VAL A HG12 1 
ATOM   547  H  HG13 . VAL A 1 37  ? -13.820 -5.505  35.999 1.00 20.27  ? 37  VAL A HG13 1 
ATOM   548  H  HG21 . VAL A 1 37  ? -11.083 -4.216  36.572 1.00 19.91  ? 37  VAL A HG21 1 
ATOM   549  H  HG22 . VAL A 1 37  ? -12.299 -3.196  36.510 1.00 19.90  ? 37  VAL A HG22 1 
ATOM   550  H  HG23 . VAL A 1 37  ? -11.409 -3.294  37.822 1.00 19.90  ? 37  VAL A HG23 1 
ATOM   551  N  N    . ALA A 1 38  ? -16.085 -5.280  38.804 1.00 11.62  ? 38  ALA A N    1 
ATOM   552  C  CA   . ALA A 1 38  ? -16.988 -6.132  39.551 1.00 12.36  ? 38  ALA A CA   1 
ATOM   553  C  C    . ALA A 1 38  ? -17.290 -7.406  38.763 1.00 11.07  ? 38  ALA A C    1 
ATOM   554  O  O    . ALA A 1 38  ? -17.502 -7.375  37.555 1.00 11.49  ? 38  ALA A O    1 
ATOM   555  C  CB   . ALA A 1 38  ? -18.259 -5.372  39.828 1.00 13.77  ? 38  ALA A CB   1 
ATOM   556  H  H    . ALA A 1 38  ? -16.435 -4.729  38.165 1.00 20.26  ? 38  ALA A H    1 
ATOM   557  H  HA   . ALA A 1 38  ? -16.567 -6.377  40.408 1.00 14.60  ? 38  ALA A HA   1 
ATOM   558  H  HB1  . ALA A 1 38  ? -18.882 -5.944  40.307 1.00 16.71  ? 38  ALA A HB1  1 
ATOM   559  H  HB2  . ALA A 1 38  ? -18.059 -4.589  40.367 1.00 16.71  ? 38  ALA A HB2  1 
ATOM   560  H  HB3  . ALA A 1 38  ? -18.660 -5.091  38.988 1.00 16.71  ? 38  ALA A HB3  1 
ATOM   561  N  N    . ALA A 1 39  ? -17.435 -8.516  39.488 1.00 10.98  ? 39  ALA A N    1 
ATOM   562  C  CA   . ALA A 1 39  ? -17.977 -9.724  38.918 1.00 10.78  ? 39  ALA A CA   1 
ATOM   563  C  C    . ALA A 1 39  ? -19.451 -9.510  38.610 1.00 10.76  ? 39  ALA A C    1 
ATOM   564  O  O    . ALA A 1 39  ? -20.212 -8.977  39.412 1.00 11.85  ? 39  ALA A O    1 
ATOM   565  C  CB   . ALA A 1 39  ? -17.820 -10.868 39.885 1.00 12.27  ? 39  ALA A CB   1 
ATOM   566  H  H    . ALA A 1 39  ? -17.186 -8.517  40.368 1.00 14.60  ? 39  ALA A H    1 
ATOM   567  H  HA   . ALA A 1 39  ? -17.496 -9.933  38.083 1.00 12.92  ? 39  ALA A HA   1 
ATOM   568  H  HB1  . ALA A 1 39  ? -18.164 -11.683 39.483 1.00 16.38  ? 39  ALA A HB1  1 
ATOM   569  H  HB2  . ALA A 1 39  ? -16.880 -10.985 40.100 1.00 16.38  ? 39  ALA A HB2  1 
ATOM   570  H  HB3  . ALA A 1 39  ? -18.316 -10.676 40.699 1.00 16.38  ? 39  ALA A HB3  1 
ATOM   571  N  N    . GLY A 1 40  ? -19.901 -10.024 37.457 1.00 10.78  ? 40  GLY A N    1 
ATOM   572  C  CA   . GLY A 1 40  ? -21.294 -10.014 37.111 1.00 11.33  ? 40  GLY A CA   1 
ATOM   573  C  C    . GLY A 1 40  ? -21.793 -8.657  36.628 1.00 11.09  ? 40  GLY A C    1 
ATOM   574  O  O    . GLY A 1 40  ? -21.015 -7.811  36.179 1.00 12.46  ? 40  GLY A O    1 
ATOM   575  H  H    . GLY A 1 40  ? -19.306 -10.394 36.870 1.00 12.92  ? 40  GLY A H    1 
ATOM   576  H  HA2  . GLY A 1 40  ? -21.447 -10.684 36.399 1.00 14.15  ? 40  GLY A HA2  1 
ATOM   577  H  HA3  . GLY A 1 40  ? -21.820 -10.292 37.901 1.00 14.15  ? 40  GLY A HA3  1 
ATOM   578  N  N    . SER A 1 41  ? -23.110 -8.510  36.709 1.00 12.54  ? 41  SER A N    1 
ATOM   579  C  CA   . SER A 1 41  ? -23.820 -7.344  36.244 1.00 14.28  ? 41  SER A CA   1 
ATOM   580  C  C    . SER A 1 41  ? -24.135 -6.491  37.469 1.00 16.21  ? 41  SER A C    1 
ATOM   581  O  O    . SER A 1 41  ? -24.423 -7.013  38.550 1.00 20.90  ? 41  SER A O    1 
ATOM   582  C  CB   . SER A 1 41  ? -25.059 -7.751  35.430 1.00 16.61  ? 41  SER A CB   1 
ATOM   583  O  OG   . SER A 1 41  ? -24.689 -8.519  34.272 1.00 17.96  ? 41  SER A OG   1 
ATOM   584  H  H    . SER A 1 41  ? -23.599 -9.187  37.080 1.00 14.15  ? 41  SER A H    1 
ATOM   585  H  HA   . SER A 1 41  ? -23.213 -6.825  35.651 1.00 17.79  ? 41  SER A HA   1 
ATOM   586  H  HB2  . SER A 1 41  ? -25.661 -8.283  35.997 1.00 18.32  ? 41  SER A HB2  1 
ATOM   587  H  HB3  . SER A 1 41  ? -25.542 -6.942  35.146 1.00 18.32  ? 41  SER A HB3  1 
ATOM   588  H  HG   . SER A 1 41  ? -24.552 -9.318  34.512 1.00 21.34  ? 41  SER A HG   1 
ATOM   589  N  N    . VAL A 1 42  ? -24.047 -5.177  37.342 1.00 16.86  ? 42  VAL A N    1 
ATOM   590  C  CA   . VAL A 1 42  ? -24.247 -4.289  38.468 1.00 16.79  ? 42  VAL A CA   1 
ATOM   591  C  C    . VAL A 1 42  ? -25.540 -3.499  38.274 1.00 18.14  ? 42  VAL A C    1 
ATOM   592  O  O    . VAL A 1 42  ? -25.693 -2.792  37.276 1.00 19.87  ? 42  VAL A O    1 
ATOM   593  C  CB   . VAL A 1 42  ? -23.025 -3.378  38.655 1.00 17.18  ? 42  VAL A CB   1 
ATOM   594  C  CG1  . VAL A 1 42  ? -23.286 -2.308  39.689 1.00 19.08  ? 42  VAL A CG1  1 
ATOM   595  C  CG2  . VAL A 1 42  ? -21.784 -4.173  39.010 1.00 19.46  ? 42  VAL A CG2  1 
ATOM   596  H  H    . VAL A 1 42  ? -23.856 -4.815  36.525 1.00 17.79  ? 42  VAL A H    1 
ATOM   597  H  HA   . VAL A 1 42  ? -24.341 -4.831  39.269 1.00 25.73  ? 42  VAL A HA   1 
ATOM   598  H  HB   . VAL A 1 42  ? -22.856 -2.927  37.791 1.00 20.66  ? 42  VAL A HB   1 
ATOM   599  H  HG11 . VAL A 1 42  ? -22.439 -1.969  40.028 1.00 21.90  ? 42  VAL A HG11 1 
ATOM   600  H  HG12 . VAL A 1 42  ? -23.785 -1.578  39.284 1.00 21.90  ? 42  VAL A HG12 1 
ATOM   601  H  HG13 . VAL A 1 42  ? -23.801 -2.684  40.424 1.00 21.90  ? 42  VAL A HG13 1 
ATOM   602  H  HG21 . VAL A 1 42  ? -21.028 -3.569  39.109 1.00 21.86  ? 42  VAL A HG21 1 
ATOM   603  H  HG22 . VAL A 1 42  ? -21.931 -4.647  39.848 1.00 21.86  ? 42  VAL A HG22 1 
ATOM   604  H  HG23 . VAL A 1 42  ? -21.595 -4.815  38.304 1.00 21.86  ? 42  VAL A HG23 1 
ATOM   605  N  N    . SER A 1 43  ? -26.406 -3.568  39.288 1.00 18.77  ? 43  SER A N    1 
ATOM   606  C  CA   . SER A 1 43  ? -27.629 -2.789  39.339 1.00 21.46  ? 43  SER A CA   1 
ATOM   607  C  C    . SER A 1 43  ? -28.132 -2.747  40.778 1.00 22.65  ? 43  SER A C    1 
ATOM   608  O  O    . SER A 1 43  ? -28.188 -3.792  41.423 1.00 27.13  ? 43  SER A O    1 
ATOM   609  C  CB   . SER A 1 43  ? -28.669 -3.402  38.437 1.00 27.23  ? 43  SER A CB   1 
ATOM   610  O  OG   . SER A 1 43  ? -29.966 -2.929  38.760 1.00 32.10  ? 43  SER A OG   1 
ATOM   611  H  H    . SER A 1 43  ? -26.226 -4.135  39.982 1.00 25.73  ? 43  SER A H    1 
ATOM   612  H  HA   . SER A 1 43  ? -27.431 -1.868  39.031 1.00 30.91  ? 43  SER A HA   1 
ATOM   613  H  HB2  . SER A 1 43  ? -28.462 -3.177  37.501 1.00 28.57  ? 43  SER A HB2  1 
ATOM   614  H  HB3  . SER A 1 43  ? -28.645 -4.381  38.529 1.00 28.57  ? 43  SER A HB3  1 
ATOM   615  H  HG   . SER A 1 43  ? -30.536 -3.439  38.399 1.00 33.18  ? 43  SER A HG   1 
ATOM   616  N  N    . PRO A 1 44  ? -28.545 -1.587  41.327 1.00 22.63  ? 44  PRO A N    1 
ATOM   617  C  CA   . PRO A 1 44  ? -28.496 -0.290  40.647 1.00 22.41  ? 44  PRO A CA   1 
ATOM   618  C  C    . PRO A 1 44  ? -27.063 0.220   40.578 1.00 22.47  ? 44  PRO A C    1 
ATOM   619  O  O    . PRO A 1 44  ? -26.130 -0.421  41.071 1.00 24.97  ? 44  PRO A O    1 
ATOM   620  C  CB   . PRO A 1 44  ? -29.363 0.580   41.567 1.00 23.75  ? 44  PRO A CB   1 
ATOM   621  C  CG   . PRO A 1 44  ? -29.141 -0.017  42.938 1.00 27.43  ? 44  PRO A CG   1 
ATOM   622  C  CD   . PRO A 1 44  ? -29.110 -1.503  42.683 1.00 25.73  ? 44  PRO A CD   1 
ATOM   623  H  HA   . PRO A 1 44  ? -28.902 -0.352  39.747 1.00 30.91  ? 44  PRO A HA   1 
ATOM   624  H  HB2  . PRO A 1 44  ? -29.074 1.517   41.543 1.00 42.18  ? 44  PRO A HB2  1 
ATOM   625  H  HB3  . PRO A 1 44  ? -30.307 0.531   41.312 1.00 42.13  ? 44  PRO A HB3  1 
ATOM   626  H  HG2  . PRO A 1 44  ? -28.295 0.290   43.321 1.00 27.72  ? 44  PRO A HG2  1 
ATOM   627  H  HG3  . PRO A 1 44  ? -29.872 0.218   43.545 1.00 27.72  ? 44  PRO A HG3  1 
ATOM   628  H  HD2  . PRO A 1 44  ? -28.541 -1.960  43.330 1.00 26.81  ? 44  PRO A HD2  1 
ATOM   629  H  HD3  . PRO A 1 44  ? -30.005 -1.887  42.716 1.00 26.81  ? 44  PRO A HD3  1 
ATOM   630  N  N    . GLN A 1 45  ? -26.873 1.366   39.934 1.00 24.76  ? 45  GLN A N    1 
ATOM   631  C  CA   . GLN A 1 45  ? -25.551 1.964   39.942 1.00 26.58  ? 45  GLN A CA   1 
ATOM   632  C  C    . GLN A 1 45  ? -25.145 2.333   41.367 1.00 26.83  ? 45  GLN A C    1 
ATOM   633  O  O    . GLN A 1 45  ? -25.905 3.024   42.035 1.00 31.67  ? 45  GLN A O    1 
ATOM   634  C  CB   . GLN A 1 45  ? -25.522 3.279   39.175 1.00 30.07  ? 45  GLN A CB   1 
ATOM   635  C  CG   . GLN A 1 45  ? -25.651 3.066   37.694 1.00 29.60  ? 45  GLN A CG   1 
ATOM   636  C  CD   . GLN A 1 45  ? -25.128 4.250   36.932 1.00 28.23  ? 45  GLN A CD   1 
ATOM   637  O  OE1  . GLN A 1 45  ? -25.021 5.364   37.452 1.00 33.83  ? 45  GLN A OE1  1 
ATOM   638  N  NE2  . GLN A 1 45  ? -24.987 4.037   35.639 1.00 31.35  ? 45  GLN A NE2  1 
ATOM   639  H  H    . GLN A 1 45  ? -27.558 1.777   39.490 1.00 29.21  ? 45  GLN A H    1 
ATOM   640  H  HA   . GLN A 1 45  ? -24.901 1.335   39.555 1.00 22.07  ? 45  GLN A HA   1 
ATOM   641  H  HB2  . GLN A 1 45  ? -26.256 3.847   39.488 1.00 29.47  ? 45  GLN A HB2  1 
ATOM   642  H  HB3  . GLN A 1 45  ? -24.677 3.738   39.367 1.00 29.47  ? 45  GLN A HB3  1 
ATOM   643  H  HG2  . GLN A 1 45  ? -25.150 2.265   37.432 1.00 21.63  ? 45  GLN A HG2  1 
ATOM   644  H  HG3  . GLN A 1 45  ? -26.595 2.924   37.465 1.00 21.64  ? 45  GLN A HG3  1 
ATOM   645  H  HE21 . GLN A 1 45  ? -25.318 3.303   35.271 1.00 22.38  ? 45  GLN A HE21 1 
ATOM   646  H  HE22 . GLN A 1 45  ? -24.562 4.628   35.138 1.00 22.38  ? 45  GLN A HE22 1 
ATOM   647  N  N    . PRO A 1 46  ? -23.955 1.902   41.878 1.00 26.11  ? 46  PRO A N    1 
ATOM   648  C  CA   . PRO A 1 46  ? -23.525 2.308   43.216 1.00 25.21  ? 46  PRO A CA   1 
ATOM   649  C  C    . PRO A 1 46  ? -23.399 3.819   43.316 1.00 23.17  ? 46  PRO A C    1 
ATOM   650  O  O    . PRO A 1 46  ? -23.078 4.510   42.347 1.00 21.32  ? 46  PRO A O    1 
ATOM   651  C  CB   . PRO A 1 46  ? -22.145 1.662   43.396 1.00 27.84  ? 46  PRO A CB   1 
ATOM   652  C  CG   . PRO A 1 46  ? -22.171 0.489   42.447 1.00 27.30  ? 46  PRO A CG   1 
ATOM   653  C  CD   . PRO A 1 46  ? -23.017 0.948   41.270 1.00 27.84  ? 46  PRO A CD   1 
ATOM   654  H  HA   . PRO A 1 46  ? -24.155 1.957   43.892 1.00 27.91  ? 46  PRO A HA   1 
ATOM   655  H  HB2  . PRO A 1 46  ? -21.427 2.288   43.159 1.00 27.47  ? 46  PRO A HB2  1 
ATOM   656  H  HB3  . PRO A 1 46  ? -22.014 1.362   44.321 1.00 27.47  ? 46  PRO A HB3  1 
ATOM   657  H  HG2  . PRO A 1 46  ? -21.267 0.259   42.154 1.00 29.67  ? 46  PRO A HG2  1 
ATOM   658  H  HG3  . PRO A 1 46  ? -22.572 -0.294  42.877 1.00 29.66  ? 46  PRO A HG3  1 
ATOM   659  H  HD2  . PRO A 1 46  ? -22.469 1.380   40.589 1.00 22.48  ? 46  PRO A HD2  1 
ATOM   660  H  HD3  . PRO A 1 46  ? -23.492 0.198   40.868 1.00 22.47  ? 46  PRO A HD3  1 
ATOM   661  N  N    . PRO A 1 47  ? -23.665 4.403   44.493 1.00 22.78  ? 47  PRO A N    1 
ATOM   662  C  CA   . PRO A 1 47  ? -23.411 5.826   44.682 1.00 20.77  ? 47  PRO A CA   1 
ATOM   663  C  C    . PRO A 1 47  ? -22.005 6.219   44.243 1.00 19.15  ? 47  PRO A C    1 
ATOM   664  O  O    . PRO A 1 47  ? -21.016 5.510   44.496 1.00 22.30  ? 47  PRO A O    1 
ATOM   665  C  CB   . PRO A 1 47  ? -23.635 6.021   46.186 1.00 23.43  ? 47  PRO A CB   1 
ATOM   666  C  CG   . PRO A 1 47  ? -24.672 4.971   46.525 1.00 26.61  ? 47  PRO A CG   1 
ATOM   667  C  CD   . PRO A 1 47  ? -24.308 3.784   45.660 1.00 26.37  ? 47  PRO A CD   1 
ATOM   668  H  HA   . PRO A 1 47  ? -24.086 6.346   44.179 1.00 21.11  ? 47  PRO A HA   1 
ATOM   669  H  HB2  . PRO A 1 47  ? -22.807 5.871   46.690 1.00 26.57  ? 47  PRO A HB2  1 
ATOM   670  H  HB3  . PRO A 1 47  ? -23.971 6.922   46.380 1.00 26.57  ? 47  PRO A HB3  1 
ATOM   671  H  HG2  . PRO A 1 47  ? -24.633 4.736   47.474 1.00 28.04  ? 47  PRO A HG2  1 
ATOM   672  H  HG3  . PRO A 1 47  ? -25.574 5.291   46.315 1.00 28.04  ? 47  PRO A HG3  1 
ATOM   673  H  HD2  . PRO A 1 47  ? -23.693 3.185   46.123 1.00 27.91  ? 47  PRO A HD2  1 
ATOM   674  H  HD3  . PRO A 1 47  ? -25.104 3.284   45.399 1.00 27.91  ? 47  PRO A HD3  1 
ATOM   675  N  N    . GLY A 1 48  ? -21.956 7.301   43.476 1.00 17.27  ? 48  GLY A N    1 
ATOM   676  C  CA   . GLY A 1 48  ? -20.698 7.857   42.974 1.00 18.27  ? 48  GLY A CA   1 
ATOM   677  C  C    . GLY A 1 48  ? -20.304 7.413   41.565 1.00 18.59  ? 48  GLY A C    1 
ATOM   678  O  O    . GLY A 1 48  ? -19.264 7.850   41.054 1.00 20.03  ? 48  GLY A O    1 
ATOM   679  H  H    . GLY A 1 48  ? -22.736 7.720   43.250 1.00 21.11  ? 48  GLY A H    1 
ATOM   680  H  HA2  . GLY A 1 48  ? -20.769 8.844   42.985 1.00 20.69  ? 48  GLY A HA2  1 
ATOM   681  H  HA3  . GLY A 1 48  ? -19.971 7.611   43.600 1.00 20.69  ? 48  GLY A HA3  1 
ATOM   682  N  N    . THR A 1 49  ? -21.087 6.511   40.963 1.00 16.96  ? 49  THR A N    1 
ATOM   683  C  CA   . THR A 1 49  ? -20.782 5.973   39.651 1.00 15.52  ? 49  THR A CA   1 
ATOM   684  C  C    . THR A 1 49  ? -21.150 6.969   38.577 1.00 16.66  ? 49  THR A C    1 
ATOM   685  O  O    . THR A 1 49  ? -22.168 7.648   38.723 1.00 20.22  ? 49  THR A O    1 
ATOM   686  C  CB   . THR A 1 49  ? -21.598 4.716   39.406 1.00 15.77  ? 49  THR A CB   1 
ATOM   687  O  OG1  . THR A 1 49  ? -21.333 3.752   40.419 1.00 18.21  ? 49  THR A OG1  1 
ATOM   688  C  CG2  . THR A 1 49  ? -21.317 4.101   38.057 1.00 17.24  ? 49  THR A CG2  1 
ATOM   689  H  H    . THR A 1 49  ? -21.844 6.224   41.386 1.00 19.87  ? 49  THR A H    1 
ATOM   690  H  HA   . THR A 1 49  ? -19.822 5.761   39.600 1.00 25.30  ? 49  THR A HA   1 
ATOM   691  H  HB   . THR A 1 49  ? -22.554 4.961   39.446 1.00 19.87  ? 49  THR A HB   1 
ATOM   692  H  HG1  . THR A 1 49  ? -21.863 3.869   41.068 1.00 19.87  ? 49  THR A HG1  1 
ATOM   693  H  HG21 . THR A 1 49  ? -21.508 3.146   38.089 1.00 19.76  ? 49  THR A HG21 1 
ATOM   694  H  HG22 . THR A 1 49  ? -21.882 4.520   37.383 1.00 19.76  ? 49  THR A HG22 1 
ATOM   695  H  HG23 . THR A 1 49  ? -20.381 4.236   37.825 1.00 19.76  ? 49  THR A HG23 1 
ATOM   696  N  N    . LYS A 1 50  ? -20.297 7.129   37.568 1.00 16.41  ? 50  LYS A N    1 
ATOM   697  C  CA   . LYS A 1 50  ? -20.660 7.862   36.373 1.00 17.87  ? 50  LYS A CA   1 
ATOM   698  C  C    . LYS A 1 50  ? -21.090 6.967   35.216 1.00 16.29  ? 50  LYS A C    1 
ATOM   699  O  O    . LYS A 1 50  ? -21.958 7.362   34.457 1.00 19.68  ? 50  LYS A O    1 
ATOM   700  C  CB   . LYS A 1 50  ? -19.549 8.757   35.865 1.00 21.87  ? 50  LYS A CB   1 
ATOM   701  C  CG   . LYS A 1 50  ? -19.355 10.020  36.655 1.00 25.94  ? 50  LYS A CG   1 
ATOM   702  C  CD   . LYS A 1 50  ? -18.697 11.053  35.779 1.00 28.58  ? 50  LYS A CD   1 
ATOM   703  C  CE   . LYS A 1 50  ? -18.090 12.203  36.522 1.00 31.39  ? 50  LYS A CE   1 
ATOM   704  N  NZ   . LYS A 1 50  ? -17.436 13.103  35.555 1.00 27.28  ? 50  LYS A NZ   1 
ATOM   705  H  H    . LYS A 1 50  ? -19.458 6.771   37.627 1.00 25.30  ? 50  LYS A H    1 
ATOM   706  H  HA   . LYS A 1 50  ? -21.425 8.438   36.600 1.00 25.49  ? 50  LYS A HA   1 
ATOM   707  H  HB2  . LYS A 1 50  ? -18.711 8.249   35.876 1.00 34.61  ? 50  LYS A HB2  1 
ATOM   708  H  HB3  . LYS A 1 50  ? -19.743 8.997   34.934 1.00 34.61  ? 50  LYS A HB3  1 
ATOM   709  H  HG2  . LYS A 1 50  ? -20.224 10.353  36.966 1.00 25.49  ? 50  LYS A HG2  1 
ATOM   710  H  HG3  . LYS A 1 50  ? -18.791 9.837   37.436 1.00 25.49  ? 50  LYS A HG3  1 
ATOM   711  H  HD2  . LYS A 1 50  ? -17.995 10.617  35.250 1.00 37.98  ? 50  LYS A HD2  1 
ATOM   712  H  HD3  . LYS A 1 50  ? -19.364 11.405  35.153 1.00 38.05  ? 50  LYS A HD3  1 
ATOM   713  H  HE2  . LYS A 1 50  ? -18.781 12.692  37.007 1.00 34.27  ? 50  LYS A HE2  1 
ATOM   714  H  HE3  . LYS A 1 50  ? -17.430 11.878  37.163 1.00 34.27  ? 50  LYS A HE3  1 
ATOM   715  H  HZ1  . LYS A 1 50  ? -16.789 12.654  35.104 1.00 36.14  ? 50  LYS A HZ1  1 
ATOM   716  H  HZ2  . LYS A 1 50  ? -18.048 13.416  34.963 1.00 36.12  ? 50  LYS A HZ2  1 
ATOM   717  H  HZ3  . LYS A 1 50  ? -17.060 13.803  35.992 1.00 36.12  ? 50  LYS A HZ3  1 
ATOM   718  N  N    . TRP A 1 51  ? -20.501 5.786   35.073 1.00 13.98  ? 51  TRP A N    1 
ATOM   719  C  CA   . TRP A 1 51  ? -20.871 4.901   33.987 1.00 13.69  ? 51  TRP A CA   1 
ATOM   720  C  C    . TRP A 1 51  ? -20.476 3.470   34.338 1.00 12.41  ? 51  TRP A C    1 
ATOM   721  O  O    . TRP A 1 51  ? -19.605 3.244   35.168 1.00 12.54  ? 51  TRP A O    1 
ATOM   722  C  CB   . TRP A 1 51  ? -20.265 5.324   32.641 1.00 14.49  ? 51  TRP A CB   1 
ATOM   723  C  CG   . TRP A 1 51  ? -18.830 5.735   32.658 1.00 13.15  ? 51  TRP A CG   1 
ATOM   724  C  CD1  . TRP A 1 51  ? -18.384 7.023   32.579 1.00 13.85  ? 51  TRP A CD1  1 
ATOM   725  C  CD2  . TRP A 1 51  ? -17.653 4.905   32.668 1.00 12.35  ? 51  TRP A CD2  1 
ATOM   726  N  NE1  . TRP A 1 51  ? -17.017 7.058   32.555 1.00 13.29  ? 51  TRP A NE1  1 
ATOM   727  C  CE2  . TRP A 1 51  ? -16.537 5.773   32.603 1.00 12.64  ? 51  TRP A CE2  1 
ATOM   728  C  CE3  . TRP A 1 51  ? -17.440 3.527   32.747 1.00 12.63  ? 51  TRP A CE3  1 
ATOM   729  C  CZ2  . TRP A 1 51  ? -15.242 5.282   32.585 1.00 13.29  ? 51  TRP A CZ2  1 
ATOM   730  C  CZ3  . TRP A 1 51  ? -16.153 3.051   32.732 1.00 12.90  ? 51  TRP A CZ3  1 
ATOM   731  C  CH2  . TRP A 1 51  ? -15.054 3.919   32.664 1.00 13.71  ? 51  TRP A CH2  1 
ATOM   732  H  H    . TRP A 1 51  ? -19.849 5.526   35.657 1.00 25.30  ? 51  TRP A H    1 
ATOM   733  H  HA   . TRP A 1 51  ? -21.852 4.936   33.896 1.00 15.89  ? 51  TRP A HA   1 
ATOM   734  H  HB2  . TRP A 1 51  ? -20.368 4.577   32.017 1.00 17.09  ? 51  TRP A HB2  1 
ATOM   735  H  HB3  . TRP A 1 51  ? -20.798 6.069   32.295 1.00 17.09  ? 51  TRP A HB3  1 
ATOM   736  H  HD1  . TRP A 1 51  ? -18.937 7.788   32.540 1.00 16.08  ? 51  TRP A HD1  1 
ATOM   737  H  HE1  . TRP A 1 51  ? -16.529 7.785   32.506 1.00 16.08  ? 51  TRP A HE1  1 
ATOM   738  H  HE3  . TRP A 1 51  ? -18.171 2.931   32.763 1.00 16.08  ? 51  TRP A HE3  1 
ATOM   739  H  HZ2  . TRP A 1 51  ? -14.507 5.871   32.569 1.00 16.08  ? 51  TRP A HZ2  1 
ATOM   740  H  HZ3  . TRP A 1 51  ? -16.004 2.119   32.772 1.00 16.08  ? 51  TRP A HZ3  1 
ATOM   741  H  HH2  . TRP A 1 51  ? -14.181 3.569   32.676 1.00 16.08  ? 51  TRP A HH2  1 
ATOM   742  N  N    . LEU A 1 52  ? -21.146 2.535   33.668 1.00 12.61  ? 52  LEU A N    1 
ATOM   743  C  CA   . LEU A 1 52  ? -20.909 1.113   33.774 1.00 12.72  ? 52  LEU A CA   1 
ATOM   744  C  C    . LEU A 1 52  ? -20.638 0.589   32.372 1.00 12.75  ? 52  LEU A C    1 
ATOM   745  O  O    . LEU A 1 52  ? -21.400 0.913   31.462 1.00 16.22  ? 52  LEU A O    1 
ATOM   746  C  CB   . LEU A 1 52  ? -22.124 0.384   34.337 1.00 13.86  ? 52  LEU A CB   1 
ATOM   747  C  CG   . LEU A 1 52  ? -22.565 0.759   35.741 1.00 13.52  ? 52  LEU A CG   1 
ATOM   748  C  CD1  . LEU A 1 52  ? -23.793 -0.052  36.119 1.00 16.56  ? 52  LEU A CD1  1 
ATOM   749  C  CD2  . LEU A 1 52  ? -21.472 0.578   36.767 1.00 13.96  ? 52  LEU A CD2  1 
ATOM   750  H  H    . LEU A 1 52  ? -21.805 2.812   33.097 1.00 15.89  ? 52  LEU A H    1 
ATOM   751  H  HA   . LEU A 1 52  ? -20.122 0.953   34.343 1.00 19.75  ? 52  LEU A HA   1 
ATOM   752  H  HB2  . LEU A 1 52  ? -22.876 0.539   33.731 1.00 16.30  ? 52  LEU A HB2  1 
ATOM   753  H  HB3  . LEU A 1 52  ? -21.934 -0.575  34.324 1.00 16.30  ? 52  LEU A HB3  1 
ATOM   754  H  HG   . LEU A 1 52  ? -22.821 1.714   35.735 1.00 16.24  ? 52  LEU A HG   1 
ATOM   755  H  HD11 . LEU A 1 52  ? -24.079 0.190   37.017 1.00 20.55  ? 52  LEU A HD11 1 
ATOM   756  H  HD12 . LEU A 1 52  ? -24.511 0.135   35.489 1.00 20.54  ? 52  LEU A HD12 1 
ATOM   757  H  HD13 . LEU A 1 52  ? -23.577 -1.000  36.092 1.00 20.54  ? 52  LEU A HD13 1 
ATOM   758  H  HD21 . LEU A 1 52  ? -21.846 0.677   37.661 1.00 19.77  ? 52  LEU A HD21 1 
ATOM   759  H  HD22 . LEU A 1 52  ? -21.084 -0.309  36.675 1.00 19.77  ? 52  LEU A HD22 1 
ATOM   760  H  HD23 . LEU A 1 52  ? -20.782 1.250   36.629 1.00 19.77  ? 52  LEU A HD23 1 
ATOM   761  N  N    . LEU A 1 53  ? -19.593 -0.217  32.201 1.00 11.07  ? 53  LEU A N    1 
ATOM   762  C  CA   . LEU A 1 53  ? -19.362 -0.935  30.944 1.00 11.37  ? 53  LEU A CA   1 
ATOM   763  C  C    . LEU A 1 53  ? -19.310 -2.426  31.265 1.00 10.84  ? 53  LEU A C    1 
ATOM   764  O  O    . LEU A 1 53  ? -18.484 -2.872  32.053 1.00 14.41  ? 53  LEU A O    1 
ATOM   765  C  CB   . LEU A 1 53  ? -18.035 -0.510  30.302 1.00 11.49  ? 53  LEU A CB   1 
ATOM   766  C  CG   . LEU A 1 53  ? -17.923 0.944   29.886 1.00 13.37  ? 53  LEU A CG   1 
ATOM   767  C  CD1  . LEU A 1 53  ? -16.501 1.241   29.400 1.00 14.71  ? 53  LEU A CD1  1 
ATOM   768  C  CD2  . LEU A 1 53  ? -18.946 1.272   28.808 1.00 17.18  ? 53  LEU A CD2  1 
ATOM   769  H  H    . LEU A 1 53  ? -18.998 -0.329  32.885 1.00 19.75  ? 53  LEU A H    1 
ATOM   770  H  HA   . LEU A 1 53  ? -20.108 -0.760  30.327 1.00 17.98  ? 53  LEU A HA   1 
ATOM   771  H  HB2  . LEU A 1 53  ? -17.315 -0.704  30.935 1.00 17.75  ? 53  LEU A HB2  1 
ATOM   772  H  HB3  . LEU A 1 53  ? -17.888 -1.067  29.512 1.00 17.75  ? 53  LEU A HB3  1 
ATOM   773  H  HG   . LEU A 1 53  ? -18.108 1.511   30.676 1.00 16.14  ? 53  LEU A HG   1 
ATOM   774  H  HD11 . LEU A 1 53  ? -16.428 2.182   29.165 1.00 19.85  ? 53  LEU A HD11 1 
ATOM   775  H  HD12 . LEU A 1 53  ? -15.866 1.034   30.108 1.00 19.85  ? 53  LEU A HD12 1 
ATOM   776  H  HD13 . LEU A 1 53  ? -16.304 0.696   28.619 1.00 19.85  ? 53  LEU A HD13 1 
ATOM   777  H  HD21 . LEU A 1 53  ? -18.730 2.132   28.406 1.00 17.97  ? 53  LEU A HD21 1 
ATOM   778  H  HD22 . LEU A 1 53  ? -18.930 0.581   28.124 1.00 17.97  ? 53  LEU A HD22 1 
ATOM   779  H  HD23 . LEU A 1 53  ? -19.834 1.315   29.205 1.00 17.97  ? 53  LEU A HD23 1 
ATOM   780  N  N    . ARG A 1 54  ? -20.119 -3.210  30.596 1.00 11.36  ? 54  ARG A N    1 
ATOM   781  C  CA   . ARG A 1 54  ? -20.188 -4.651  30.818 1.00 10.87  ? 54  ARG A CA   1 
ATOM   782  C  C    . ARG A 1 54  ? -19.646 -5.393  29.619 1.00 9.58   ? 54  ARG A C    1 
ATOM   783  O  O    . ARG A 1 54  ? -19.856 -4.994  28.476 1.00 10.36  ? 54  ARG A O    1 
ATOM   784  C  CB   . ARG A 1 54  ? -21.634 -5.058  31.051 1.00 12.70  ? 54  ARG A CB   1 
ATOM   785  C  CG   . ARG A 1 54  ? -21.826 -6.494  31.470 1.00 14.63  ? 54  ARG A CG   1 
ATOM   786  C  CD   . ARG A 1 54  ? -23.217 -6.749  31.989 1.00 16.75  ? 54  ARG A CD   1 
ATOM   787  N  NE   . ARG A 1 54  ? -24.260 -6.441  31.006 1.00 17.88  ? 54  ARG A NE   1 
ATOM   788  C  CZ   . ARG A 1 54  ? -25.322 -7.179  30.798 1.00 17.78  ? 54  ARG A CZ   1 
ATOM   789  N  NH1  . ARG A 1 54  ? -25.562 -8.183  31.605 1.00 21.32  ? 54  ARG A NH1  1 
ATOM   790  N  NH2  . ARG A 1 54  ? -26.131 -6.913  29.794 1.00 18.56  ? 54  ARG A NH2  1 
ATOM   791  H  H    . ARG A 1 54  ? -20.665 -2.844  29.961 1.00 17.98  ? 54  ARG A H    1 
ATOM   792  H  HA   . ARG A 1 54  ? -19.655 -4.880  31.612 1.00 11.99  ? 54  ARG A HA   1 
ATOM   793  H  HB2  . ARG A 1 54  ? -22.012 -4.476  31.742 1.00 20.43  ? 54  ARG A HB2  1 
ATOM   794  H  HB3  . ARG A 1 54  ? -22.134 -4.903  30.223 1.00 20.43  ? 54  ARG A HB3  1 
ATOM   795  H  HG2  . ARG A 1 54  ? -21.659 -7.082  30.703 1.00 17.23  ? 54  ARG A HG2  1 
ATOM   796  H  HG3  . ARG A 1 54  ? -21.177 -6.717  32.171 1.00 17.23  ? 54  ARG A HG3  1 
ATOM   797  H  HD2  . ARG A 1 54  ? -23.286 -7.691  32.251 1.00 20.71  ? 54  ARG A HD2  1 
ATOM   798  H  HD3  . ARG A 1 54  ? -23.364 -6.205  32.791 1.00 20.71  ? 54  ARG A HD3  1 
ATOM   799  H  HE   . ARG A 1 54  ? -24.175 -5.713  30.535 1.00 20.44  ? 54  ARG A HE   1 
ATOM   800  H  HH11 . ARG A 1 54  ? -25.011 -8.869  31.631 1.00 20.73  ? 54  ARG A HH11 1 
ATOM   801  H  HH12 . ARG A 1 54  ? -26.280 -8.170  32.116 1.00 20.72  ? 54  ARG A HH12 1 
ATOM   802  H  HH21 . ARG A 1 54  ? -25.936 -6.267  29.230 1.00 20.45  ? 54  ARG A HH21 1 
ATOM   803  H  HH22 . ARG A 1 54  ? -26.867 -7.383  29.689 1.00 20.45  ? 54  ARG A HH22 1 
ATOM   804  N  N    . GLY A 1 55  ? -18.971 -6.505  29.886 1.00 9.19   ? 55  GLY A N    1 
ATOM   805  C  CA   . GLY A 1 55  ? -18.507 -7.382  28.825 1.00 9.23   ? 55  GLY A CA   1 
ATOM   806  C  C    . GLY A 1 55  ? -18.362 -8.797  29.346 1.00 8.98   ? 55  GLY A C    1 
ATOM   807  O  O    . GLY A 1 55  ? -18.395 -9.020  30.548 1.00 10.31  ? 55  GLY A O    1 
ATOM   808  H  H    . GLY A 1 55  ? -18.792 -6.729  30.754 1.00 11.99  ? 55  GLY A H    1 
ATOM   809  H  HA2  . GLY A 1 55  ? -19.155 -7.369  28.077 1.00 11.11  ? 55  GLY A HA2  1 
ATOM   810  H  HA3  . GLY A 1 55  ? -17.632 -7.058  28.492 1.00 11.11  ? 55  GLY A HA3  1 
ATOM   811  N  N    . ILE A 1 56  ? -18.162 -9.732  28.413 1.00 8.29   ? 56  ILE A N    1 
ATOM   812  C  CA   . ILE A 1 56  ? -18.095 -11.149 28.771 1.00 8.31   ? 56  ILE A CA   1 
ATOM   813  C  C    . ILE A 1 56  ? -16.879 -11.774 28.101 1.00 7.86   ? 56  ILE A C    1 
ATOM   814  O  O    . ILE A 1 56  ? -16.637 -11.584 26.903 1.00 8.35   ? 56  ILE A O    1 
ATOM   815  C  CB   . ILE A 1 56  ? -19.422 -11.864 28.444 1.00 8.66   ? 56  ILE A CB   1 
ATOM   816  C  CG1  . ILE A 1 56  ? -19.507 -13.220 29.147 1.00 8.76   ? 56  ILE A CG1  1 
ATOM   817  C  CG2  . ILE A 1 56  ? -19.673 -12.000 26.949 1.00 9.90   ? 56  ILE A CG2  1 
ATOM   818  C  CD1  . ILE A 1 56  ? -20.828 -13.926 28.995 1.00 9.51   ? 56  ILE A CD1  1 
ATOM   819  H  H    . ILE A 1 56  ? -18.064 -9.488  27.538 1.00 12.01  ? 56  ILE A H    1 
ATOM   820  H  HA   . ILE A 1 56  ? -17.964 -11.205 29.731 1.00 11.65  ? 56  ILE A HA   1 
ATOM   821  H  HB   . ILE A 1 56  ? -20.149 -11.303 28.812 1.00 10.30  ? 56  ILE A HB   1 
ATOM   822  H  HG12 . ILE A 1 56  ? -18.801 -13.800 28.793 1.00 11.64  ? 56  ILE A HG12 1 
ATOM   823  H  HG13 . ILE A 1 56  ? -19.334 -13.087 30.102 1.00 11.64  ? 56  ILE A HG13 1 
ATOM   824  H  HG21 . ILE A 1 56  ? -20.627 -12.100 26.786 1.00 12.01  ? 56  ILE A HG21 1 
ATOM   825  H  HG22 . ILE A 1 56  ? -19.350 -11.206 26.490 1.00 12.01  ? 56  ILE A HG22 1 
ATOM   826  H  HG23 . ILE A 1 56  ? -19.205 -12.782 26.609 1.00 12.01  ? 56  ILE A HG23 1 
ATOM   827  H  HD11 . ILE A 1 56  ? -20.904 -14.625 29.667 1.00 11.67  ? 56  ILE A HD11 1 
ATOM   828  H  HD12 . ILE A 1 56  ? -21.554 -13.288 29.109 1.00 11.67  ? 56  ILE A HD12 1 
ATOM   829  H  HD13 . ILE A 1 56  ? -20.885 -14.324 28.109 1.00 11.67  ? 56  ILE A HD13 1 
ATOM   830  N  N    . THR A 1 57  ? -16.106 -12.551 28.867 1.00 8.07   ? 57  THR A N    1 
ATOM   831  C  CA   . THR A 1 57  ? -15.064 -13.345 28.247 1.00 8.56   ? 57  THR A CA   1 
ATOM   832  C  C    . THR A 1 57  ? -15.716 -14.444 27.424 1.00 8.45   ? 57  THR A C    1 
ATOM   833  O  O    . THR A 1 57  ? -16.821 -14.912 27.738 1.00 9.13   ? 57  THR A O    1 
ATOM   834  C  CB   . THR A 1 57  ? -14.053 -13.887 29.260 1.00 9.34   ? 57  THR A CB   1 
ATOM   835  O  OG1  . THR A 1 57  ? -14.710 -14.801 30.126 1.00 9.79   ? 57  THR A OG1  1 
ATOM   836  C  CG2  . THR A 1 57  ? -13.430 -12.800 30.098 1.00 10.02  ? 57  THR A CG2  1 
ATOM   837  H  H    . THR A 1 57  ? -16.231 -12.592 29.772 1.00 11.66  ? 57  THR A H    1 
ATOM   838  H  HA   . THR A 1 57  ? -14.580 -12.754 27.632 1.00 10.31  ? 57  THR A HA   1 
ATOM   839  H  HB   . THR A 1 57  ? -13.341 -14.363 28.770 1.00 21.89  ? 57  THR A HB   1 
ATOM   840  H  HG1  . THR A 1 57  ? -14.134 -15.257 30.550 1.00 12.02  ? 57  THR A HG1  1 
ATOM   841  H  HG21 . THR A 1 57  ? -12.694 -13.171 30.618 1.00 11.67  ? 57  THR A HG21 1 
ATOM   842  H  HG22 . THR A 1 57  ? -13.092 -12.095 29.517 1.00 11.67  ? 57  THR A HG22 1 
ATOM   843  H  HG23 . THR A 1 57  ? -14.098 -12.429 30.702 1.00 11.67  ? 57  THR A HG23 1 
ATOM   844  N  N    . SER A 1 58  ? -15.050 -14.886 26.343 1.00 8.58   ? 58  SER A N    1 
ATOM   845  C  CA   . SER A 1 58  ? -15.696 -15.791 25.413 1.00 8.53   ? 58  SER A CA   1 
ATOM   846  C  C    . SER A 1 58  ? -14.675 -16.709 24.766 1.00 8.52   ? 58  SER A C    1 
ATOM   847  O  O    . SER A 1 58  ? -13.479 -16.682 25.042 1.00 9.48   ? 58  SER A O    1 
ATOM   848  C  CB   . SER A 1 58  ? -16.514 -14.993 24.406 1.00 8.80   ? 58  SER A CB   1 
ATOM   849  O  OG   . SER A 1 58  ? -17.344 -15.829 23.612 1.00 9.31   ? 58  SER A OG   1 
ATOM   850  H  H    . SER A 1 58  ? -14.178 -14.658 26.215 1.00 10.31  ? 58  SER A H    1 
ATOM   851  H  HA   . SER A 1 58  ? -16.323 -16.362 25.932 1.00 18.22  ? 58  SER A HA   1 
ATOM   852  H  HB2  . SER A 1 58  ? -17.073 -14.342 24.887 1.00 10.62  ? 58  SER A HB2  1 
ATOM   853  H  HB3  . SER A 1 58  ? -15.903 -14.493 23.819 1.00 10.62  ? 58  SER A HB3  1 
ATOM   854  H  HG   . SER A 1 58  ? -17.929 -16.177 24.114 1.00 13.21  ? 58  SER A HG   1 
ATOM   855  N  N    . ASN A 1 59  ? -15.187 -17.572 23.880 1.00 8.75   ? 59  ASN A N    1 
ATOM   856  C  CA   . ASN A 1 59  ? -14.323 -18.480 23.142 1.00 9.00   ? 59  ASN A CA   1 
ATOM   857  C  C    . ASN A 1 59  ? -13.499 -17.705 22.118 1.00 8.60   ? 59  ASN A C    1 
ATOM   858  O  O    . ASN A 1 59  ? -13.862 -16.612 21.660 1.00 9.00   ? 59  ASN A O    1 
ATOM   859  C  CB   . ASN A 1 59  ? -15.125 -19.588 22.472 1.00 9.40   ? 59  ASN A CB   1 
ATOM   860  C  CG   . ASN A 1 59  ? -16.176 -19.043 21.527 1.00 9.14   ? 59  ASN A CG   1 
ATOM   861  O  OD1  . ASN A 1 59  ? -17.245 -18.621 21.963 1.00 9.85   ? 59  ASN A OD1  1 
ATOM   862  N  ND2  . ASN A 1 59  ? -15.894 -19.079 20.232 1.00 9.57   ? 59  ASN A ND2  1 
ATOM   863  H  H    . ASN A 1 59  ? -16.089 -17.595 23.735 1.00 13.21  ? 59  ASN A H    1 
ATOM   864  H  HA   . ASN A 1 59  ? -13.707 -18.906 23.783 1.00 15.58  ? 59  ASN A HA   1 
ATOM   865  H  HB2  . ASN A 1 59  ? -14.513 -20.166 21.973 1.00 12.92  ? 59  ASN A HB2  1 
ATOM   866  H  HB3  . ASN A 1 59  ? -15.561 -20.129 23.161 1.00 12.93  ? 59  ASN A HB3  1 
ATOM   867  H  HD21 . ASN A 1 59  ? -16.542 -19.195 19.642 1.00 12.75  ? 59  ASN A HD21 1 
ATOM   868  H  HD22 . ASN A 1 59  ? -15.058 -18.988 19.959 1.00 12.75  ? 59  ASN A HD22 1 
ATOM   869  N  N    . GLU A 1 60  ? -12.415 -18.340 21.699 1.00 9.39   ? 60  GLU A N    1 
ATOM   870  C  CA   . GLU A 1 60  ? -11.558 -17.799 20.656 1.00 9.36   ? 60  GLU A CA   1 
ATOM   871  C  C    . GLU A 1 60  ? -12.318 -17.718 19.342 1.00 8.74   ? 60  GLU A C    1 
ATOM   872  O  O    . GLU A 1 60  ? -13.078 -18.616 18.970 1.00 9.25   ? 60  GLU A O    1 
ATOM   873  C  CB   . GLU A 1 60  ? -10.324 -18.681 20.493 1.00 10.02  ? 60  GLU A CB   1 
ATOM   874  C  CG   . GLU A 1 60  ? -9.413  -18.569 21.706 1.00 11.27  ? 60  GLU A CG   1 
ATOM   875  C  CD   . GLU A 1 60  ? -8.621  -19.807 22.046 1.00 13.11  ? 60  GLU A CD   1 
ATOM   876  O  OE1  . GLU A 1 60  ? -9.012  -20.904 21.613 1.00 14.36  ? 60  GLU A OE1  1 
ATOM   877  O  OE2  . GLU A 1 60  ? -7.651  -19.655 22.801 1.00 16.25  ? 60  GLU A OE2  1 
ATOM   878  H  H    . GLU A 1 60  ? -12.196 -19.145 22.074 1.00 15.58  ? 60  GLU A H    1 
ATOM   879  H  HA   . GLU A 1 60  ? -11.273 -16.899 20.920 1.00 15.61  ? 60  GLU A HA   1 
ATOM   880  H  HB2  . GLU A 1 60  ? -10.608 -19.611 20.377 1.00 15.59  ? 60  GLU A HB2  1 
ATOM   881  H  HB3  . GLU A 1 60  ? -9.838  -18.404 19.690 1.00 15.59  ? 60  GLU A HB3  1 
ATOM   882  H  HG2  . GLU A 1 60  ? -8.785  -17.832 21.561 1.00 15.59  ? 60  GLU A HG2  1 
ATOM   883  H  HG3  . GLU A 1 60  ? -9.958  -18.335 22.487 1.00 15.59  ? 60  GLU A HG3  1 
ATOM   884  N  N    . ARG A 1 61  ? -12.048 -16.623 18.621 1.00 8.92   ? 61  ARG A N    1 
ATOM   885  C  CA   . ARG A 1 61  ? -12.663 -16.345 17.342 1.00 8.96   ? 61  ARG A CA   1 
ATOM   886  C  C    . ARG A 1 61  ? -11.678 -16.461 16.185 1.00 8.97   ? 61  ARG A C    1 
ATOM   887  O  O    . ARG A 1 61  ? -12.114 -16.574 15.037 1.00 10.44  ? 61  ARG A O    1 
ATOM   888  C  CB   . ARG A 1 61  ? -13.231 -14.919 17.363 1.00 10.00  ? 61  ARG A CB   1 
ATOM   889  C  CG   . ARG A 1 61  ? -14.139 -14.630 18.546 1.00 10.52  ? 61  ARG A CG   1 
ATOM   890  C  CD   . ARG A 1 61  ? -15.298 -15.638 18.672 1.00 11.15  ? 61  ARG A CD   1 
ATOM   891  N  NE   . ARG A 1 61  ? -16.048 -15.427 19.899 1.00 11.45  ? 61  ARG A NE   1 
ATOM   892  C  CZ   . ARG A 1 61  ? -17.011 -14.511 20.011 1.00 9.84   ? 61  ARG A CZ   1 
ATOM   893  N  NH1  . ARG A 1 61  ? -17.307 -13.747 18.948 1.00 11.43  ? 61  ARG A NH1  1 
ATOM   894  N  NH2  . ARG A 1 61  ? -17.637 -14.244 21.155 1.00 11.91  ? 61  ARG A NH2  1 
ATOM   895  H  H    . ARG A 1 61  ? -11.465 -16.009 18.961 1.00 15.61  ? 61  ARG A H    1 
ATOM   896  H  HA   . ARG A 1 61  ? -13.397 -16.982 17.195 1.00 13.46  ? 61  ARG A HA   1 
ATOM   897  H  HB2  . ARG A 1 61  ? -12.483 -14.286 17.379 1.00 14.55  ? 61  ARG A HB2  1 
ATOM   898  H  HB3  . ARG A 1 61  ? -13.732 -14.769 16.536 1.00 14.55  ? 61  ARG A HB3  1 
ATOM   899  H  HG2  . ARG A 1 61  ? -13.611 -14.652 19.369 1.00 13.44  ? 61  ARG A HG2  1 
ATOM   900  H  HG3  . ARG A 1 61  ? -14.511 -13.731 18.454 1.00 13.44  ? 61  ARG A HG3  1 
ATOM   901  H  HD2  . ARG A 1 61  ? -15.896 -15.551 17.899 1.00 13.45  ? 61  ARG A HD2  1 
ATOM   902  H  HD3  . ARG A 1 61  ? -14.938 -16.550 18.673 1.00 13.45  ? 61  ARG A HD3  1 
ATOM   903  H  HE   . ARG A 1 61  ? -15.861 -15.921 20.594 1.00 13.44  ? 61  ARG A HE   1 
ATOM   904  H  HH11 . ARG A 1 61  ? -16.713 -13.608 18.319 1.00 13.44  ? 61  ARG A HH11 1 
ATOM   905  H  HH12 . ARG A 1 61  ? -18.106 -13.380 18.886 1.00 13.44  ? 61  ARG A HH12 1 
ATOM   906  H  HH21 . ARG A 1 61  ? -17.709 -14.867 21.770 1.00 13.44  ? 61  ARG A HH21 1 
ATOM   907  H  HH22 . ARG A 1 61  ? -17.977 -13.444 21.292 1.00 13.44  ? 61  ARG A HH22 1 
ATOM   908  N  N    . TYR A 1 62  ? -10.377 -16.406 16.477 1.00 9.20   ? 62  TYR A N    1 
ATOM   909  C  CA   . TYR A 1 62  ? -9.353  -16.331 15.435 1.00 9.83   ? 62  TYR A CA   1 
ATOM   910  C  C    . TYR A 1 62  ? -8.147  -17.228 15.708 1.00 9.67   ? 62  TYR A C    1 
ATOM   911  O  O    . TYR A 1 62  ? -7.575  -17.778 14.766 1.00 10.58  ? 62  TYR A O    1 
ATOM   912  C  CB   . TYR A 1 62  ? -8.831  -14.891 15.235 1.00 10.07  ? 62  TYR A CB   1 
ATOM   913  C  CG   . TYR A 1 62  ? -9.921  -13.954 14.755 1.00 9.92   ? 62  TYR A CG   1 
ATOM   914  C  CD1  . TYR A 1 62  ? -10.481 -14.095 13.498 1.00 9.95   ? 62  TYR A CD1  1 
ATOM   915  C  CD2  . TYR A 1 62  ? -10.443 -12.975 15.589 1.00 10.46  ? 62  TYR A CD2  1 
ATOM   916  C  CE1  . TYR A 1 62  ? -11.552 -13.308 13.105 1.00 10.43  ? 62  TYR A CE1  1 
ATOM   917  C  CE2  . TYR A 1 62  ? -11.501 -12.177 15.206 1.00 10.41  ? 62  TYR A CE2  1 
ATOM   918  C  CZ   . TYR A 1 62  ? -12.072 -12.345 13.959 1.00 9.68   ? 62  TYR A CZ   1 
ATOM   919  O  OH   . TYR A 1 62  ? -13.135 -11.609 13.538 1.00 10.37  ? 62  TYR A OH   1 
ATOM   920  H  H    . TYR A 1 62  ? -10.117 -16.395 17.352 1.00 15.61  ? 62  TYR A H    1 
ATOM   921  H  HA   . TYR A 1 62  ? -9.760  -16.629 14.583 1.00 11.98  ? 62  TYR A HA   1 
ATOM   922  H  HB2  . TYR A 1 62  ? -8.470  -14.562 16.085 1.00 12.24  ? 62  TYR A HB2  1 
ATOM   923  H  HB3  . TYR A 1 62  ? -8.103  -14.905 14.578 1.00 12.24  ? 62  TYR A HB3  1 
ATOM   924  H  HD1  . TYR A 1 62  ? -10.169 -14.774 12.923 1.00 12.24  ? 62  TYR A HD1  1 
ATOM   925  H  HD2  . TYR A 1 62  ? -10.091 -12.878 16.458 1.00 12.24  ? 62  TYR A HD2  1 
ATOM   926  H  HE1  . TYR A 1 62  ? -11.934 -13.428 12.251 1.00 12.24  ? 62  TYR A HE1  1 
ATOM   927  H  HE2  . TYR A 1 62  ? -11.845 -11.536 15.799 1.00 12.24  ? 62  TYR A HE2  1 
ATOM   928  H  HH   . TYR A 1 62  ? -13.917 -11.956 13.596 1.00 12.88  ? 62  TYR A HH   1 
ATOM   929  N  N    . VAL A 1 63  ? -7.723  -17.352 16.963 1.00 10.34  ? 63  VAL A N    1 
ATOM   930  C  CA   A VAL A 1 63  ? -6.447  -17.974 17.227 0.52 10.90  ? 63  VAL A CA   1 
ATOM   931  C  CA   B VAL A 1 63  ? -6.515  -18.049 17.409 0.48 11.03  ? 63  VAL A CA   1 
ATOM   932  C  C    . VAL A 1 63  ? -6.513  -19.459 16.857 1.00 10.57  ? 63  VAL A C    1 
ATOM   933  O  O    . VAL A 1 63  ? -7.488  -20.192 17.064 1.00 11.99  ? 63  VAL A O    1 
ATOM   934  C  CB   A VAL A 1 63  ? -6.052  -17.688 18.688 0.52 12.40  ? 63  VAL A CB   1 
ATOM   935  C  CB   B VAL A 1 63  ? -6.432  -18.135 18.956 0.48 11.55  ? 63  VAL A CB   1 
ATOM   936  C  CG1  A VAL A 1 63  ? -6.908  -18.460 19.659 0.52 13.56  ? 63  VAL A CG1  1 
ATOM   937  C  CG1  B VAL A 1 63  ? -5.458  -19.187 19.460 0.48 11.73  ? 63  VAL A CG1  1 
ATOM   938  C  CG2  A VAL A 1 63  ? -4.602  -17.973 18.985 0.52 11.45  ? 63  VAL A CG2  1 
ATOM   939  C  CG2  B VAL A 1 63  ? -6.077  -16.800 19.589 0.48 12.22  ? 63  VAL A CG2  1 
ATOM   940  H  H    A VAL A 1 63  ? -8.223  -17.037 17.659 0.52 15.62  ? 63  VAL A H    1 
ATOM   941  H  H    B VAL A 1 63  ? -8.229  -16.955 17.612 0.48 15.61  ? 63  VAL A H    1 
ATOM   942  H  HA   A VAL A 1 63  ? -5.786  -17.549 16.651 0.52 16.17  ? 63  VAL A HA   1 
ATOM   943  H  HA   B VAL A 1 63  ? -5.734  -17.574 17.074 0.48 16.17  ? 63  VAL A HA   1 
ATOM   944  H  HB   A VAL A 1 63  ? -6.208  -16.725 18.852 0.52 15.62  ? 63  VAL A HB   1 
ATOM   945  H  HB   B VAL A 1 63  ? -7.332  -18.386 19.281 0.48 15.16  ? 63  VAL A HB   1 
ATOM   946  H  HG11 A VAL A 1 63  ? -6.876  -18.029 20.530 0.52 15.63  ? 63  VAL A HG11 1 
ATOM   947  H  HG11 B VAL A 1 63  ? -5.216  -18.989 20.381 0.48 14.47  ? 63  VAL A HG11 1 
ATOM   948  H  HG12 A VAL A 1 63  ? -7.824  -18.480 19.340 0.52 15.63  ? 63  VAL A HG12 1 
ATOM   949  H  HG12 B VAL A 1 63  ? -5.875  -20.065 19.417 0.48 14.47  ? 63  VAL A HG12 1 
ATOM   950  H  HG13 A VAL A 1 63  ? -6.573  -19.370 19.737 0.52 15.63  ? 63  VAL A HG13 1 
ATOM   951  H  HG13 B VAL A 1 63  ? -4.656  -19.180 18.908 0.48 14.47  ? 63  VAL A HG13 1 
ATOM   952  H  HG21 A VAL A 1 63  ? -4.382  -17.648 19.876 0.52 15.85  ? 63  VAL A HG21 1 
ATOM   953  H  HG21 B VAL A 1 63  ? -6.336  -16.805 20.527 0.48 15.42  ? 63  VAL A HG21 1 
ATOM   954  H  HG22 A VAL A 1 63  ? -4.443  -18.932 18.943 0.52 15.85  ? 63  VAL A HG22 1 
ATOM   955  H  HG22 B VAL A 1 63  ? -5.118  -16.655 19.518 0.48 15.42  ? 63  VAL A HG22 1 
ATOM   956  H  HG23 A VAL A 1 63  ? -4.043  -17.524 18.330 0.52 15.85  ? 63  VAL A HG23 1 
ATOM   957  H  HG23 B VAL A 1 63  ? -6.548  -16.085 19.127 0.48 15.42  ? 63  VAL A HG23 1 
ATOM   958  N  N    . VAL A 1 64  ? -5.398  -19.909 16.270 1.00 10.85  ? 64  VAL A N    1 
ATOM   959  C  CA   . VAL A 1 64  ? -5.216  -21.306 15.918 1.00 11.32  ? 64  VAL A CA   1 
ATOM   960  C  C    . VAL A 1 64  ? -4.362  -22.009 16.959 1.00 11.01  ? 64  VAL A C    1 
ATOM   961  O  O    . VAL A 1 64  ? -3.681  -21.371 17.749 1.00 10.95  ? 64  VAL A O    1 
ATOM   962  C  CB   . VAL A 1 64  ? -4.643  -21.477 14.503 1.00 12.37  ? 64  VAL A CB   1 
ATOM   963  C  CG1  . VAL A 1 64  ? -5.521  -20.755 13.506 1.00 14.00  ? 64  VAL A CG1  1 
ATOM   964  C  CG2  . VAL A 1 64  ? -3.195  -21.025 14.391 1.00 13.76  ? 64  VAL A CG2  1 
ATOM   965  H  H    . VAL A 1 64  ? -4.723  -19.321 16.084 1.00 16.17  ? 64  VAL A H    1 
ATOM   966  H  HA   . VAL A 1 64  ? -6.092  -21.727 15.929 1.00 15.12  ? 64  VAL A HA   1 
ATOM   967  H  HB   . VAL A 1 64  ? -4.672  -22.440 14.287 1.00 14.87  ? 64  VAL A HB   1 
ATOM   968  H  HG11 . VAL A 1 64  ? -5.293  -21.042 12.605 1.00 16.60  ? 64  VAL A HG11 1 
ATOM   969  H  HG12 . VAL A 1 64  ? -6.454  -20.962 13.685 1.00 16.60  ? 64  VAL A HG12 1 
ATOM   970  H  HG13 . VAL A 1 64  ? -5.381  -19.795 13.585 1.00 16.60  ? 64  VAL A HG13 1 
ATOM   971  H  HG21 . VAL A 1 64  ? -3.020  -20.710 13.487 1.00 16.17  ? 64  VAL A HG21 1 
ATOM   972  H  HG22 . VAL A 1 64  ? -3.027  -20.306 15.021 1.00 16.17  ? 64  VAL A HG22 1 
ATOM   973  H  HG23 . VAL A 1 64  ? -2.605  -21.773 14.591 1.00 16.17  ? 64  VAL A HG23 1 
ATOM   974  N  N    . ARG A 1 65  ? -4.400  -23.344 16.972 1.00 11.76  ? 65  ARG A N    1 
ATOM   975  C  CA   . ARG A 1 65  ? -3.746  -24.120 18.017 1.00 12.03  ? 65  ARG A CA   1 
ATOM   976  C  C    . ARG A 1 65  ? -2.274  -23.745 18.184 1.00 11.88  ? 65  ARG A C    1 
ATOM   977  O  O    . ARG A 1 65  ? -1.794  -23.602 19.306 1.00 12.08  ? 65  ARG A O    1 
ATOM   978  C  CB   . ARG A 1 65  ? -3.912  -25.614 17.718 1.00 13.77  ? 65  ARG A CB   1 
ATOM   979  C  CG   . ARG A 1 65  ? -3.128  -26.535 18.640 1.00 14.88  ? 65  ARG A CG   1 
ATOM   980  C  CD   . ARG A 1 65  ? -3.338  -26.307 20.116 1.00 15.78  ? 65  ARG A CD   1 
ATOM   981  N  NE   . ARG A 1 65  ? -4.728  -26.404 20.475 1.00 16.33  ? 65  ARG A NE   1 
ATOM   982  C  CZ   . ARG A 1 65  ? -5.234  -25.960 21.618 1.00 19.08  ? 65  ARG A CZ   1 
ATOM   983  N  NH1  . ARG A 1 65  ? -4.429  -25.465 22.559 1.00 22.83  ? 65  ARG A NH1  1 
ATOM   984  N  NH2  . ARG A 1 65  ? -6.545  -26.025 21.794 1.00 22.35  ? 65  ARG A NH2  1 
ATOM   985  H  H    . ARG A 1 65  ? -4.846  -23.786 16.308 1.00 17.71  ? 65  ARG A H    1 
ATOM   986  H  HA   . ARG A 1 65  ? -4.206  -23.924 18.865 1.00 16.19  ? 65  ARG A HA   1 
ATOM   987  H  HB2  . ARG A 1 65  ? -4.863  -25.839 17.784 1.00 17.70  ? 65  ARG A HB2  1 
ATOM   988  H  HB3  . ARG A 1 65  ? -3.629  -25.779 16.795 1.00 17.70  ? 65  ARG A HB3  1 
ATOM   989  H  HG2  . ARG A 1 65  ? -3.373  -27.463 18.436 1.00 17.09  ? 65  ARG A HG2  1 
ATOM   990  H  HG3  . ARG A 1 65  ? -2.172  -26.438 18.445 1.00 17.09  ? 65  ARG A HG3  1 
ATOM   991  H  HD2  . ARG A 1 65  ? -2.827  -26.974 20.622 1.00 28.79  ? 65  ARG A HD2  1 
ATOM   992  H  HD3  . ARG A 1 65  ? -3.001  -25.421 20.360 1.00 28.82  ? 65  ARG A HD3  1 
ATOM   993  H  HE   . ARG A 1 65  ? -5.270  -26.786 19.912 1.00 17.29  ? 65  ARG A HE   1 
ATOM   994  H  HH11 . ARG A 1 65  ? -3.558  -25.572 22.500 1.00 30.23  ? 65  ARG A HH11 1 
ATOM   995  H  HH12 . ARG A 1 65  ? -4.774  -25.045 23.251 1.00 30.31  ? 65  ARG A HH12 1 
ATOM   996  H  HH21 . ARG A 1 65  ? -7.084  -25.941 21.106 1.00 16.90  ? 65  ARG A HH21 1 
ATOM   997  H  HH22 . ARG A 1 65  ? -6.873  -26.151 22.600 1.00 16.91  ? 65  ARG A HH22 1 
ATOM   998  N  N    . GLU A 1 66  ? -1.539  -23.603 17.090 1.00 12.88  ? 66  GLU A N    1 
ATOM   999  C  CA   . GLU A 1 66  ? -0.119  -23.331 17.223 1.00 14.56  ? 66  GLU A CA   1 
ATOM   1000 C  C    . GLU A 1 66  ? 0.106   -21.989 17.942 1.00 13.15  ? 66  GLU A C    1 
ATOM   1001 O  O    . GLU A 1 66  ? 1.059   -21.841 18.718 1.00 14.51  ? 66  GLU A O    1 
ATOM   1002 C  CB   . GLU A 1 66  ? 0.497   -23.408 15.830 1.00 18.85  ? 66  GLU A CB   1 
ATOM   1003 C  CG   . GLU A 1 66  ? 1.996   -23.341 15.826 1.00 23.73  ? 66  GLU A CG   1 
ATOM   1004 C  CD   . GLU A 1 66  ? 2.543   -21.925 15.779 1.00 28.04  ? 66  GLU A CD   1 
ATOM   1005 O  OE1  . GLU A 1 66  ? 1.733   -20.983 15.548 1.00 30.10  ? 66  GLU A OE1  1 
ATOM   1006 O  OE2  . GLU A 1 66  ? 3.766   -21.756 15.975 1.00 33.05  ? 66  GLU A OE2  1 
ATOM   1007 H  H    . GLU A 1 66  ? -1.913  -23.674 16.259 1.00 37.74  ? 66  GLU A H    1 
ATOM   1008 H  HA   . GLU A 1 66  ? 0.276   -24.046 17.775 1.00 19.75  ? 66  GLU A HA   1 
ATOM   1009 H  HB2  . GLU A 1 66  ? 0.218   -24.250 15.413 1.00 37.74  ? 66  GLU A HB2  1 
ATOM   1010 H  HB3  . GLU A 1 66  ? 0.139   -22.675 15.289 1.00 37.74  ? 66  GLU A HB3  1 
ATOM   1011 H  HG2  . GLU A 1 66  ? 2.340   -23.782 16.632 1.00 19.75  ? 66  GLU A HG2  1 
ATOM   1012 H  HG3  . GLU A 1 66  ? 2.337   -23.833 15.049 1.00 19.75  ? 66  GLU A HG3  1 
ATOM   1013 N  N    . GLU A 1 67  ? -0.746  -21.003 17.652 1.00 11.96  ? 67  GLU A N    1 
ATOM   1014 C  CA   . GLU A 1 67  ? -0.672  -19.708 18.312 1.00 12.30  ? 67  GLU A CA   1 
ATOM   1015 C  C    . GLU A 1 67  ? -1.061  -19.827 19.775 1.00 11.67  ? 67  GLU A C    1 
ATOM   1016 O  O    . GLU A 1 67  ? -0.410  -19.261 20.648 1.00 12.53  ? 67  GLU A O    1 
ATOM   1017 C  CB   . GLU A 1 67  ? -1.592  -18.708 17.613 1.00 12.09  ? 67  GLU A CB   1 
ATOM   1018 C  CG   . GLU A 1 67  ? -1.138  -18.315 16.235 1.00 13.11  ? 67  GLU A CG   1 
ATOM   1019 C  CD   . GLU A 1 67  ? -2.173  -17.687 15.325 1.00 12.81  ? 67  GLU A CD   1 
ATOM   1020 O  OE1  . GLU A 1 67  ? -3.372  -17.796 15.581 1.00 12.13  ? 67  GLU A OE1  1 
ATOM   1021 O  OE2  . GLU A 1 67  ? -1.732  -17.108 14.314 1.00 14.94  ? 67  GLU A OE2  1 
ATOM   1022 H  H    . GLU A 1 67  ? -1.390  -21.137 17.018 1.00 15.84  ? 67  GLU A H    1 
ATOM   1023 H  HA   . GLU A 1 67  ? 0.256   -19.381 18.256 1.00 14.96  ? 67  GLU A HA   1 
ATOM   1024 H  HB2  . GLU A 1 67  ? -2.486  -19.101 17.552 1.00 15.84  ? 67  GLU A HB2  1 
ATOM   1025 H  HB3  . GLU A 1 67  ? -1.656  -17.902 18.168 1.00 15.84  ? 67  GLU A HB3  1 
ATOM   1026 H  HG2  . GLU A 1 67  ? -0.392  -17.683 16.324 1.00 15.63  ? 67  GLU A HG2  1 
ATOM   1027 H  HG3  . GLU A 1 67  ? -0.786  -19.112 15.786 1.00 15.63  ? 67  GLU A HG3  1 
ATOM   1028 N  N    . LYS A 1 68  ? -2.155  -20.554 20.040 1.00 11.65  ? 68  LYS A N    1 
ATOM   1029 C  CA   A LYS A 1 68  ? -2.627  -20.742 21.402 0.58 11.77  ? 68  LYS A CA   1 
ATOM   1030 C  CA   B LYS A 1 68  ? -2.626  -20.749 21.393 0.42 12.12  ? 68  LYS A CA   1 
ATOM   1031 C  C    . LYS A 1 68  ? -1.538  -21.357 22.272 1.00 11.76  ? 68  LYS A C    1 
ATOM   1032 O  O    . LYS A 1 68  ? -1.327  -20.930 23.404 1.00 12.38  ? 68  LYS A O    1 
ATOM   1033 C  CB   A LYS A 1 68  ? -3.906  -21.589 21.440 0.58 12.27  ? 68  LYS A CB   1 
ATOM   1034 C  CB   B LYS A 1 68  ? -3.873  -21.629 21.351 0.42 13.40  ? 68  LYS A CB   1 
ATOM   1035 C  CG   A LYS A 1 68  ? -4.484  -21.788 22.831 0.58 12.88  ? 68  LYS A CG   1 
ATOM   1036 C  CG   B LYS A 1 68  ? -4.462  -21.877 22.715 0.42 14.71  ? 68  LYS A CG   1 
ATOM   1037 C  CD   A LYS A 1 68  ? -4.793  -20.508 23.617 0.58 13.58  ? 68  LYS A CD   1 
ATOM   1038 C  CD   B LYS A 1 68  ? -5.817  -22.476 22.643 0.42 17.38  ? 68  LYS A CD   1 
ATOM   1039 C  CE   A LYS A 1 68  ? -5.514  -20.781 24.920 0.58 14.56  ? 68  LYS A CE   1 
ATOM   1040 C  CE   B LYS A 1 68  ? -6.363  -22.691 24.032 0.42 18.65  ? 68  LYS A CE   1 
ATOM   1041 N  NZ   A LYS A 1 68  ? -6.856  -21.404 24.728 0.58 14.57  ? 68  LYS A NZ   1 
ATOM   1042 N  NZ   B LYS A 1 68  ? -6.346  -21.447 24.838 0.42 21.47  ? 68  LYS A NZ   1 
ATOM   1043 H  H    A LYS A 1 68  ? -2.621  -20.938 19.354 0.58 14.17  ? 68  LYS A H    1 
ATOM   1044 H  H    B LYS A 1 68  ? -2.622  -20.934 19.352 0.42 14.17  ? 68  LYS A H    1 
ATOM   1045 H  HA   A LYS A 1 68  ? -2.839  -19.852 21.766 0.58 16.41  ? 68  LYS A HA   1 
ATOM   1046 H  HA   B LYS A 1 68  ? -2.873  -19.870 21.763 0.42 14.62  ? 68  LYS A HA   1 
ATOM   1047 H  HB2  A LYS A 1 68  ? -4.582  -21.163 20.878 0.58 14.47  ? 68  LYS A HB2  1 
ATOM   1048 H  HB2  B LYS A 1 68  ? -4.547  -21.197 20.787 0.42 15.87  ? 68  LYS A HB2  1 
ATOM   1049 H  HB3  A LYS A 1 68  ? -3.707  -22.469 21.055 0.58 14.47  ? 68  LYS A HB3  1 
ATOM   1050 H  HB3  B LYS A 1 68  ? -3.640  -22.489 20.944 0.42 15.87  ? 68  LYS A HB3  1 
ATOM   1051 H  HG2  A LYS A 1 68  ? -5.313  -22.306 22.745 0.58 17.65  ? 68  LYS A HG2  1 
ATOM   1052 H  HG2  B LYS A 1 68  ? -3.872  -22.480 23.216 0.42 17.27  ? 68  LYS A HG2  1 
ATOM   1053 H  HG3  A LYS A 1 68  ? -3.856  -22.331 23.353 0.58 17.65  ? 68  LYS A HG3  1 
ATOM   1054 H  HG3  B LYS A 1 68  ? -4.511  -21.027 23.202 0.42 17.27  ? 68  LYS A HG3  1 
ATOM   1055 H  HD2  A LYS A 1 68  ? -3.951  -20.043 23.814 0.58 16.41  ? 68  LYS A HD2  1 
ATOM   1056 H  HD2  B LYS A 1 68  ? -6.415  -21.877 22.148 0.42 28.82  ? 68  LYS A HD2  1 
ATOM   1057 H  HD3  A LYS A 1 68  ? -5.341  -19.915 23.063 0.58 16.41  ? 68  LYS A HD3  1 
ATOM   1058 H  HD3  B LYS A 1 68  ? -5.777  -23.332 22.170 0.42 28.85  ? 68  LYS A HD3  1 
ATOM   1059 H  HE2  A LYS A 1 68  ? -4.973  -21.377 25.467 0.58 35.16  ? 68  LYS A HE2  1 
ATOM   1060 H  HE2  B LYS A 1 68  ? -7.280  -23.016 23.974 0.42 35.81  ? 68  LYS A HE2  1 
ATOM   1061 H  HE3  A LYS A 1 68  ? -5.625  -19.944 25.409 0.58 35.15  ? 68  LYS A HE3  1 
ATOM   1062 H  HE3  B LYS A 1 68  ? -5.831  -23.369 24.490 0.42 35.62  ? 68  LYS A HE3  1 
ATOM   1063 H  HZ1  A LYS A 1 68  ? -7.374  -21.248 25.456 0.58 17.65  ? 68  LYS A HZ1  1 
ATOM   1064 H  HZ1  B LYS A 1 68  ? -5.501  -21.121 24.884 0.42 21.81  ? 68  LYS A HZ1  1 
ATOM   1065 H  HZ2  A LYS A 1 68  ? -7.257  -21.052 23.997 0.58 17.65  ? 68  LYS A HZ2  1 
ATOM   1066 H  HZ2  B LYS A 1 68  ? -6.884  -20.825 24.454 0.42 21.81  ? 68  LYS A HZ2  1 
ATOM   1067 H  HZ3  A LYS A 1 68  ? -6.766  -22.299 24.615 0.58 17.65  ? 68  LYS A HZ3  1 
ATOM   1068 H  HZ3  B LYS A 1 68  ? -6.645  -21.619 25.677 0.42 21.81  ? 68  LYS A HZ3  1 
ATOM   1069 N  N    . ASP A 1 69  ? -0.851  -22.362 21.760 1.00 11.70  ? 69  ASP A N    1 
ATOM   1070 C  CA   . ASP A 1 69  ? 0.156   -23.007 22.589 1.00 12.41  ? 69  ASP A CA   1 
ATOM   1071 C  C    . ASP A 1 69  ? 1.277   -22.028 22.939 1.00 12.16  ? 69  ASP A C    1 
ATOM   1072 O  O    . ASP A 1 69  ? 1.813   -22.075 24.057 1.00 12.66  ? 69  ASP A O    1 
ATOM   1073 C  CB   . ASP A 1 69  ? 0.683   -24.260 21.901 1.00 14.97  ? 69  ASP A CB   1 
ATOM   1074 C  CG   . ASP A 1 69  ? -0.310  -25.408 21.856 1.00 16.12  ? 69  ASP A CG   1 
ATOM   1075 O  OD1  . ASP A 1 69  ? -1.309  -25.386 22.630 1.00 17.38  ? 69  ASP A OD1  1 
ATOM   1076 O  OD2  . ASP A 1 69  ? -0.070  -26.312 21.074 1.00 20.52  ? 69  ASP A OD2  1 
ATOM   1077 H  H    . ASP A 1 69  ? -1.001  -22.657 20.907 1.00 19.58  ? 69  ASP A H    1 
ATOM   1078 H  HA   . ASP A 1 69  ? -0.278  -23.286 23.430 1.00 15.23  ? 69  ASP A HA   1 
ATOM   1079 H  HB2  . ASP A 1 69  ? 0.935   -24.036 20.982 1.00 19.58  ? 69  ASP A HB2  1 
ATOM   1080 H  HB3  . ASP A 1 69  ? 1.485   -24.568 22.371 1.00 19.58  ? 69  ASP A HB3  1 
ATOM   1081 N  N    . ARG A 1 70  ? 1.638   -21.131 22.015 1.00 11.93  ? 70  ARG A N    1 
ATOM   1082 C  CA   . ARG A 1 70  ? 2.621   -20.108 22.318 1.00 12.96  ? 70  ARG A CA   1 
ATOM   1083 C  C    . ARG A 1 70  ? 2.131   -19.148 23.388 1.00 11.84  ? 70  ARG A C    1 
ATOM   1084 O  O    . ARG A 1 70  ? 2.884   -18.791 24.300 1.00 12.15  ? 70  ARG A O    1 
ATOM   1085 C  CB   . ARG A 1 70  ? 2.998   -19.300 21.078 1.00 14.49  ? 70  ARG A CB   1 
ATOM   1086 C  CG   . ARG A 1 70  ? 3.788   -20.118 20.086 1.00 16.69  ? 70  ARG A CG   1 
ATOM   1087 C  CD   . ARG A 1 70  ? 4.480   -19.344 19.014 1.00 25.51  ? 70  ARG A CD   1 
ATOM   1088 N  NE   . ARG A 1 70  ? 3.850   -19.625 17.759 1.00 31.61  ? 70  ARG A NE   1 
ATOM   1089 C  CZ   . ARG A 1 70  ? 3.544   -18.704 16.863 1.00 35.20  ? 70  ARG A CZ   1 
ATOM   1090 N  NH1  . ARG A 1 70  ? 4.241   -17.581 16.814 1.00 39.77  ? 70  ARG A NH1  1 
ATOM   1091 N  NH2  . ARG A 1 70  ? 2.581   -18.936 15.988 1.00 28.96  ? 70  ARG A NH2  1 
ATOM   1092 H  H    . ARG A 1 70  ? 1.270   -21.162 21.179 1.00 18.66  ? 70  ARG A H    1 
ATOM   1093 H  HA   . ARG A 1 70  ? 3.431   -20.555 22.654 1.00 25.22  ? 70  ARG A HA   1 
ATOM   1094 H  HB2  . ARG A 1 70  ? 2.181   -18.973 20.649 1.00 25.89  ? 70  ARG A HB2  1 
ATOM   1095 H  HB3  . ARG A 1 70  ? 3.532   -18.524 21.353 1.00 25.89  ? 70  ARG A HB3  1 
ATOM   1096 H  HG2  . ARG A 1 70  ? 4.464   -20.633 20.575 1.00 25.22  ? 70  ARG A HG2  1 
ATOM   1097 H  HG3  . ARG A 1 70  ? 3.183   -20.763 19.664 1.00 25.22  ? 70  ARG A HG3  1 
ATOM   1098 H  HD2  . ARG A 1 70  ? 4.427   -18.384 19.210 1.00 25.90  ? 70  ARG A HD2  1 
ATOM   1099 H  HD3  . ARG A 1 70  ? 5.426   -19.602 18.976 1.00 25.90  ? 70  ARG A HD3  1 
ATOM   1100 H  HE   . ARG A 1 70  ? 3.670   -20.454 17.568 1.00 25.22  ? 70  ARG A HE   1 
ATOM   1101 H  HH11 . ARG A 1 70  ? 5.121   -17.611 16.787 1.00 29.31  ? 70  ARG A HH11 1 
ATOM   1102 H  HH12 . ARG A 1 70  ? 3.823   -16.805 16.808 1.00 29.31  ? 70  ARG A HH12 1 
ATOM   1103 H  HH21 . ARG A 1 70  ? 1.771   -19.127 16.269 1.00 26.51  ? 70  ARG A HH21 1 
ATOM   1104 H  HH22 . ARG A 1 70  ? 2.755   -18.900 15.127 1.00 26.51  ? 70  ARG A HH22 1 
ATOM   1105 N  N    . LEU A 1 71  ? 0.896   -18.695 23.240 1.00 11.57  ? 71  LEU A N    1 
ATOM   1106 C  CA   . LEU A 1 71  ? 0.303   -17.783 24.190 1.00 11.81  ? 71  LEU A CA   1 
ATOM   1107 C  C    . LEU A 1 71  ? 0.230   -18.388 25.585 1.00 11.63  ? 71  LEU A C    1 
ATOM   1108 O  O    . LEU A 1 71  ? 0.557   -17.731 26.574 1.00 12.21  ? 71  LEU A O    1 
ATOM   1109 C  CB   . LEU A 1 71  ? -1.094  -17.397 23.703 1.00 11.92  ? 71  LEU A CB   1 
ATOM   1110 C  CG   . LEU A 1 71  ? -1.108  -16.483 22.485 1.00 13.10  ? 71  LEU A CG   1 
ATOM   1111 C  CD1  . LEU A 1 71  ? -2.469  -16.518 21.814 1.00 14.01  ? 71  LEU A CD1  1 
ATOM   1112 C  CD2  . LEU A 1 71  ? -0.787  -15.049 22.854 1.00 14.09  ? 71  LEU A CD2  1 
ATOM   1113 H  H    . LEU A 1 71  ? 0.405   -18.957 22.515 1.00 15.95  ? 71  LEU A H    1 
ATOM   1114 H  HA   . LEU A 1 71  ? 0.865   -16.976 24.231 1.00 15.96  ? 71  LEU A HA   1 
ATOM   1115 H  HB2  . LEU A 1 71  ? -1.585  -18.215 23.488 1.00 15.95  ? 71  LEU A HB2  1 
ATOM   1116 H  HB3  . LEU A 1 71  ? -1.566  -16.950 24.434 1.00 15.95  ? 71  LEU A HB3  1 
ATOM   1117 H  HG   . LEU A 1 71  ? -0.430  -16.804 21.840 1.00 15.02  ? 71  LEU A HG   1 
ATOM   1118 H  HD11 . LEU A 1 71  ? -2.458  -15.948 21.026 1.00 15.93  ? 71  LEU A HD11 1 
ATOM   1119 H  HD12 . LEU A 1 71  ? -2.678  -17.431 21.549 1.00 15.93  ? 71  LEU A HD12 1 
ATOM   1120 H  HD13 . LEU A 1 71  ? -3.146  -16.199 22.436 1.00 15.93  ? 71  LEU A HD13 1 
ATOM   1121 H  HD21 . LEU A 1 71  ? -0.879  -14.483 22.067 1.00 15.96  ? 71  LEU A HD21 1 
ATOM   1122 H  HD22 . LEU A 1 71  ? -1.401  -14.746 23.545 1.00 15.96  ? 71  LEU A HD22 1 
ATOM   1123 H  HD23 . LEU A 1 71  ? 0.126   -14.995 23.185 1.00 15.96  ? 71  LEU A HD23 1 
ATOM   1124 N  N    . VAL A 1 72  ? -0.266  -19.629 25.694 1.00 11.47  ? 72  VAL A N    1 
ATOM   1125 C  CA   . VAL A 1 72  ? -0.438  -20.256 26.991 1.00 11.61  ? 72  VAL A CA   1 
ATOM   1126 C  C    . VAL A 1 72  ? 0.904   -20.333 27.713 1.00 11.49  ? 72  VAL A C    1 
ATOM   1127 O  O    . VAL A 1 72  ? 0.989   -20.122 28.913 1.00 12.26  ? 72  VAL A O    1 
ATOM   1128 C  CB   . VAL A 1 72  ? -1.126  -21.628 26.868 1.00 12.77  ? 72  VAL A CB   1 
ATOM   1129 C  CG1  . VAL A 1 72  ? -1.077  -22.408 28.176 1.00 13.66  ? 72  VAL A CG1  1 
ATOM   1130 C  CG2  . VAL A 1 72  ? -2.566  -21.440 26.399 1.00 14.18  ? 72  VAL A CG2  1 
ATOM   1131 H  H    . VAL A 1 72  ? -0.499  -20.093 24.941 1.00 32.20  ? 72  VAL A H    1 
ATOM   1132 H  HA   . VAL A 1 72  ? -1.022  -19.681 27.518 1.00 14.04  ? 72  VAL A HA   1 
ATOM   1133 H  HB   . VAL A 1 72  ? -0.642  -22.148 26.180 1.00 23.60  ? 72  VAL A HB   1 
ATOM   1134 H  HG11 . VAL A 1 72  ? -1.762  -23.099 28.167 1.00 16.08  ? 72  VAL A HG11 1 
ATOM   1135 H  HG12 . VAL A 1 72  ? -0.204  -22.822 28.276 1.00 16.08  ? 72  VAL A HG12 1 
ATOM   1136 H  HG13 . VAL A 1 72  ? -1.237  -21.804 28.921 1.00 16.08  ? 72  VAL A HG13 1 
ATOM   1137 H  HG21 . VAL A 1 72  ? -2.945  -22.305 26.162 1.00 32.25  ? 72  VAL A HG21 1 
ATOM   1138 H  HG22 . VAL A 1 72  ? -3.092  -21.043 27.115 1.00 32.22  ? 72  VAL A HG22 1 
ATOM   1139 H  HG23 . VAL A 1 72  ? -2.585  -20.855 25.623 1.00 32.22  ? 72  VAL A HG23 1 
ATOM   1140 N  N    . ALA A 1 73  ? 1.968   -20.691 26.988 1.00 11.37  ? 73  ALA A N    1 
ATOM   1141 C  CA   . ALA A 1 73  ? 3.273   -20.846 27.610 1.00 12.05  ? 73  ALA A CA   1 
ATOM   1142 C  C    . ALA A 1 73  ? 3.798   -19.490 28.099 1.00 12.07  ? 73  ALA A C    1 
ATOM   1143 O  O    . ALA A 1 73  ? 4.435   -19.415 29.147 1.00 13.37  ? 73  ALA A O    1 
ATOM   1144 C  CB   . ALA A 1 73  ? 4.255   -21.512 26.676 1.00 12.46  ? 73  ALA A CB   1 
ATOM   1145 H  H    . ALA A 1 73  ? 1.881   -20.846 26.091 1.00 13.81  ? 73  ALA A H    1 
ATOM   1146 H  HA   . ALA A 1 73  ? 3.163   -21.428 28.399 1.00 14.49  ? 73  ALA A HA   1 
ATOM   1147 H  HB1  . ALA A 1 73  ? 5.119   -21.590 27.115 1.00 15.19  ? 73  ALA A HB1  1 
ATOM   1148 H  HB2  . ALA A 1 73  ? 3.931   -22.398 26.441 1.00 15.19  ? 73  ALA A HB2  1 
ATOM   1149 H  HB3  . ALA A 1 73  ? 4.350   -20.978 25.869 1.00 15.19  ? 73  ALA A HB3  1 
ATOM   1150 N  N    . LYS A 1 74  ? 3.577   -18.416 27.328 1.00 11.71  ? 74  LYS A N    1 
ATOM   1151 C  CA   . LYS A 1 74  ? 4.313   -17.178 27.557 1.00 11.99  ? 74  LYS A CA   1 
ATOM   1152 C  C    . LYS A 1 74  ? 3.540   -16.149 28.388 1.00 11.95  ? 74  LYS A C    1 
ATOM   1153 O  O    . LYS A 1 74  ? 4.148   -15.240 28.954 1.00 12.56  ? 74  LYS A O    1 
ATOM   1154 C  CB   . LYS A 1 74  ? 4.685   -16.566 26.205 1.00 13.30  ? 74  LYS A CB   1 
ATOM   1155 C  CG   . LYS A 1 74  ? 5.924   -15.678 26.175 1.00 14.03  ? 74  LYS A CG   1 
ATOM   1156 C  CD   . LYS A 1 74  ? 6.251   -15.109 24.826 1.00 14.41  ? 74  LYS A CD   1 
ATOM   1157 C  CE   . LYS A 1 74  ? 7.555   -14.355 24.797 1.00 15.76  ? 74  LYS A CE   1 
ATOM   1158 N  NZ   . LYS A 1 74  ? 7.791   -13.772 23.470 1.00 17.15  ? 74  LYS A NZ   1 
ATOM   1159 H  H    . LYS A 1 74  ? 2.967   -18.453 26.649 1.00 16.28  ? 74  LYS A H    1 
ATOM   1160 H  HA   . LYS A 1 74  ? 5.145   -17.398 28.035 1.00 14.48  ? 74  LYS A HA   1 
ATOM   1161 H  HB2  . LYS A 1 74  ? 4.819   -17.297 25.566 1.00 15.97  ? 74  LYS A HB2  1 
ATOM   1162 H  HB3  . LYS A 1 74  ? 3.923   -16.037 25.889 1.00 15.97  ? 74  LYS A HB3  1 
ATOM   1163 H  HG2  . LYS A 1 74  ? 5.795   -14.939 26.807 1.00 16.97  ? 74  LYS A HG2  1 
ATOM   1164 H  HG3  . LYS A 1 74  ? 6.688   -16.204 26.486 1.00 16.97  ? 74  LYS A HG3  1 
ATOM   1165 H  HD2  . LYS A 1 74  ? 6.294   -15.840 24.173 1.00 17.30  ? 74  LYS A HD2  1 
ATOM   1166 H  HD3  . LYS A 1 74  ? 5.529   -14.503 24.552 1.00 17.30  ? 74  LYS A HD3  1 
ATOM   1167 H  HE2  . LYS A 1 74  ? 7.539   -13.644 25.462 1.00 18.85  ? 74  LYS A HE2  1 
ATOM   1168 H  HE3  . LYS A 1 74  ? 8.288   -14.959 25.015 1.00 18.85  ? 74  LYS A HE3  1 
ATOM   1169 H  HZ1  . LYS A 1 74  ? 7.801   -14.428 22.843 1.00 20.22  ? 74  LYS A HZ1  1 
ATOM   1170 H  HZ2  . LYS A 1 74  ? 7.132   -13.182 23.271 1.00 20.22  ? 74  LYS A HZ2  1 
ATOM   1171 H  HZ3  . LYS A 1 74  ? 8.589   -13.342 23.461 1.00 20.22  ? 74  LYS A HZ3  1 
ATOM   1172 N  N    . GLN A 1 75  ? 2.212   -16.241 28.385 1.00 11.40  ? 75  GLN A N    1 
ATOM   1173 C  CA   . GLN A 1 75  ? 1.433   -15.168 28.969 1.00 11.78  ? 75  GLN A CA   1 
ATOM   1174 C  C    . GLN A 1 75  ? 1.475   -15.234 30.485 1.00 11.57  ? 75  GLN A C    1 
ATOM   1175 O  O    . GLN A 1 75  ? 1.426   -16.318 31.077 1.00 13.15  ? 75  GLN A O    1 
ATOM   1176 C  CB   . GLN A 1 75  ? -0.004  -15.236 28.450 1.00 12.28  ? 75  GLN A CB   1 
ATOM   1177 C  CG   . GLN A 1 75  ? -0.789  -16.400 29.026 1.00 13.49  ? 75  GLN A CG   1 
ATOM   1178 C  CD   . GLN A 1 75  ? -2.012  -16.724 28.202 1.00 14.83  ? 75  GLN A CD   1 
ATOM   1179 O  OE1  . GLN A 1 75  ? -2.386  -16.017 27.257 1.00 16.26  ? 75  GLN A OE1  1 
ATOM   1180 N  NE2  . GLN A 1 75  ? -2.691  -17.793 28.582 1.00 15.92  ? 75  GLN A NE2  1 
ATOM   1181 H  H    . GLN A 1 75  ? 1.789   -16.963 28.019 1.00 16.28  ? 75  GLN A H    1 
ATOM   1182 H  HA   . GLN A 1 75  ? 1.826   -14.315 28.679 1.00 14.45  ? 75  GLN A HA   1 
ATOM   1183 H  HB2  . GLN A 1 75  ? -0.459  -14.398 28.675 1.00 14.68  ? 75  GLN A HB2  1 
ATOM   1184 H  HB3  . GLN A 1 75  ? 0.021   -15.312 27.473 1.00 14.68  ? 75  GLN A HB3  1 
ATOM   1185 H  HG2  . GLN A 1 75  ? -0.212  -17.191 29.071 1.00 16.28  ? 75  GLN A HG2  1 
ATOM   1186 H  HG3  . GLN A 1 75  ? -1.070  -16.180 29.940 1.00 16.28  ? 75  GLN A HG3  1 
ATOM   1187 H  HE21 . GLN A 1 75  ? -2.422  -18.265 29.280 1.00 18.63  ? 75  GLN A HE21 1 
ATOM   1188 H  HE22 . GLN A 1 75  ? -3.416  -18.037 28.139 1.00 18.63  ? 75  GLN A HE22 1 
ATOM   1189 N  N    . PRO A 1 76  ? 1.478   -14.068 31.162 1.00 11.64  ? 76  PRO A N    1 
ATOM   1190 C  CA   . PRO A 1 76  ? 1.485   -14.041 32.606 1.00 13.03  ? 76  PRO A CA   1 
ATOM   1191 C  C    . PRO A 1 76  ? 0.085   -14.136 33.168 1.00 13.53  ? 76  PRO A C    1 
ATOM   1192 O  O    . PRO A 1 76  ? -0.897  -13.884 32.490 1.00 14.86  ? 76  PRO A O    1 
ATOM   1193 C  CB   . PRO A 1 76  ? 2.072   -12.674 32.923 1.00 13.34  ? 76  PRO A CB   1 
ATOM   1194 C  CG   . PRO A 1 76  ? 1.544   -11.823 31.781 1.00 13.00  ? 76  PRO A CG   1 
ATOM   1195 C  CD   . PRO A 1 76  ? 1.631   -12.742 30.566 1.00 11.82  ? 76  PRO A CD   1 
ATOM   1196 H  HA   . PRO A 1 76  ? 2.067   -14.757 32.965 1.00 20.98  ? 76  PRO A HA   1 
ATOM   1197 H  HB2  . PRO A 1 76  ? 1.756   -12.341 33.790 1.00 15.99  ? 76  PRO A HB2  1 
ATOM   1198 H  HB3  . PRO A 1 76  ? 3.053   -12.698 32.923 1.00 15.99  ? 76  PRO A HB3  1 
ATOM   1199 H  HG2  . PRO A 1 76  ? 0.619   -11.553 31.948 1.00 13.20  ? 76  PRO A HG2  1 
ATOM   1200 H  HG3  . PRO A 1 76  ? 2.092   -11.022 31.656 1.00 13.20  ? 76  PRO A HG3  1 
ATOM   1201 H  HD2  . PRO A 1 76  ? 0.916   -12.556 29.931 1.00 14.45  ? 76  PRO A HD2  1 
ATOM   1202 H  HD3  . PRO A 1 76  ? 2.492   -12.655 30.117 1.00 14.45  ? 76  PRO A HD3  1 
ATOM   1203 N  N    . SER A 1 77  ? 0.011   -14.504 34.455 1.00 15.34  ? 77  SER A N    1 
ATOM   1204 C  CA   . SER A 1 77  ? -1.224  -14.443 35.227 1.00 16.63  ? 77  SER A CA   1 
ATOM   1205 C  C    . SER A 1 77  ? -1.725  -13.002 35.385 1.00 15.87  ? 77  SER A C    1 
ATOM   1206 O  O    . SER A 1 77  ? -0.961  -12.052 35.552 1.00 15.83  ? 77  SER A O    1 
ATOM   1207 C  CB   . SER A 1 77  ? -1.039  -15.095 36.606 1.00 19.48  ? 77  SER A CB   1 
ATOM   1208 O  OG   . SER A 1 77  ? -0.804  -16.518 36.515 1.00 25.44  ? 77  SER A OG   1 
ATOM   1209 H  H    . SER A 1 77  ? 0.768   -14.806 34.869 1.00 20.98  ? 77  SER A H    1 
ATOM   1210 H  HA   . SER A 1 77  ? -1.915  -14.958 34.731 1.00 29.39  ? 77  SER A HA   1 
ATOM   1211 H  HB2  . SER A 1 77  ? -0.278  -14.670 37.063 1.00 22.62  ? 77  SER A HB2  1 
ATOM   1212 H  HB3  . SER A 1 77  ? -1.844  -14.935 37.149 1.00 22.62  ? 77  SER A HB3  1 
ATOM   1213 H  HG   . SER A 1 77  ? -0.785  -16.838 37.298 1.00 28.69  ? 77  SER A HG   1 
ATOM   1214 N  N    . LEU A 1 78  ? -3.048  -12.847 35.406 1.00 17.44  ? 78  LEU A N    1 
ATOM   1215 C  CA   . LEU A 1 78  ? -3.692  -11.653 35.943 1.00 18.22  ? 78  LEU A CA   1 
ATOM   1216 C  C    . LEU A 1 78  ? -3.501  -11.605 37.463 1.00 19.36  ? 78  LEU A C    1 
ATOM   1217 O  O    . LEU A 1 78  ? -3.389  -12.648 38.106 1.00 20.15  ? 78  LEU A O    1 
ATOM   1218 C  CB   . LEU A 1 78  ? -5.179  -11.708 35.603 1.00 19.83  ? 78  LEU A CB   1 
ATOM   1219 C  CG   . LEU A 1 78  ? -5.455  -11.474 34.125 1.00 21.91  ? 78  LEU A CG   1 
ATOM   1220 C  CD1  . LEU A 1 78  ? -6.873  -11.864 33.847 1.00 27.67  ? 78  LEU A CD1  1 
ATOM   1221 C  CD2  . LEU A 1 78  ? -5.232  -10.028 33.734 1.00 19.60  ? 78  LEU A CD2  1 
ATOM   1222 H  H    . LEU A 1 78  ? -3.575  -13.514 35.070 1.00 28.92  ? 78  LEU A H    1 
ATOM   1223 H  HA   . LEU A 1 78  ? -3.280  -10.857 35.538 1.00 26.85  ? 78  LEU A HA   1 
ATOM   1224 H  HB2  . LEU A 1 78  ? -5.530  -12.584 35.860 1.00 28.42  ? 78  LEU A HB2  1 
ATOM   1225 H  HB3  . LEU A 1 78  ? -5.648  -11.029 36.126 1.00 28.48  ? 78  LEU A HB3  1 
ATOM   1226 H  HG   . LEU A 1 78  ? -4.854  -12.048 33.589 1.00 25.25  ? 78  LEU A HG   1 
ATOM   1227 H  HD11 . LEU A 1 78  ? -7.056  -11.771 32.898 1.00 26.44  ? 78  LEU A HD11 1 
ATOM   1228 H  HD12 . LEU A 1 78  ? -7.013  -12.785 34.118 1.00 26.60  ? 78  LEU A HD12 1 
ATOM   1229 H  HD13 . LEU A 1 78  ? -7.470  -11.283 34.350 1.00 26.51  ? 78  LEU A HD13 1 
ATOM   1230 H  HD21 . LEU A 1 78  ? -5.573  -9.878  32.835 1.00 26.88  ? 78  LEU A HD21 1 
ATOM   1231 H  HD22 . LEU A 1 78  ? -5.700  -9.446  34.358 1.00 26.90  ? 78  LEU A HD22 1 
ATOM   1232 H  HD23 . LEU A 1 78  ? -4.280  -9.828  33.755 1.00 26.88  ? 78  LEU A HD23 1 
ATOM   1233 N  N    . GLY A 1 79  ? -3.443  -10.400 38.054 1.00 18.26  ? 79  GLY A N    1 
ATOM   1234 C  CA   . GLY A 1 79  ? -3.374  -10.224 39.498 1.00 19.24  ? 79  GLY A CA   1 
ATOM   1235 C  C    . GLY A 1 79  ? -1.966  -10.296 40.088 1.00 19.85  ? 79  GLY A C    1 
ATOM   1236 O  O    . GLY A 1 79  ? -1.832  -10.429 41.301 1.00 21.85  ? 79  GLY A O    1 
ATOM   1237 H  H    . GLY A 1 79  ? -3.445  -9.654  37.526 1.00 26.85  ? 79  GLY A H    1 
ATOM   1238 H  HA2  . GLY A 1 79  ? -3.768  -9.346  39.724 1.00 32.46  ? 79  GLY A HA2  1 
ATOM   1239 H  HA3  . GLY A 1 79  ? -3.936  -10.917 39.927 1.00 32.45  ? 79  GLY A HA3  1 
ATOM   1240 N  N    . ARG A 1 80  ? -0.906  -10.215 39.272 1.00 18.21  ? 80  ARG A N    1 
ATOM   1241 C  CA   . ARG A 1 80  ? 0.448   -10.240 39.828 1.00 17.98  ? 80  ARG A CA   1 
ATOM   1242 C  C    . ARG A 1 80  ? 0.672   -9.043  40.751 1.00 19.95  ? 80  ARG A C    1 
ATOM   1243 O  O    . ARG A 1 80  ? 0.265   -7.924  40.435 1.00 19.33  ? 80  ARG A O    1 
ATOM   1244 C  CB   . ARG A 1 80  ? 1.494   -10.126 38.723 1.00 16.32  ? 80  ARG A CB   1 
ATOM   1245 C  CG   . ARG A 1 80  ? 1.551   -11.319 37.775 1.00 14.50  ? 80  ARG A CG   1 
ATOM   1246 C  CD   . ARG A 1 80  ? 2.452   -11.077 36.585 1.00 14.02  ? 80  ARG A CD   1 
ATOM   1247 N  NE   . ARG A 1 80  ? 1.902   -10.000 35.750 1.00 12.99  ? 80  ARG A NE   1 
ATOM   1248 C  CZ   . ARG A 1 80  ? 2.494   -9.496  34.678 1.00 12.35  ? 80  ARG A CZ   1 
ATOM   1249 N  NH1  . ARG A 1 80  ? 3.664   -9.936  34.279 1.00 13.00  ? 80  ARG A NH1  1 
ATOM   1250 N  NH2  . ARG A 1 80  ? 1.877   -8.545  33.984 1.00 12.41  ? 80  ARG A NH2  1 
ATOM   1251 H  H    . ARG A 1 80  ? -1.020  -10.138 38.368 1.00 17.87  ? 80  ARG A H    1 
ATOM   1252 H  HA   . ARG A 1 80  ? 0.580   -11.077 40.329 1.00 21.93  ? 80  ARG A HA   1 
ATOM   1253 H  HB2  . ARG A 1 80  ? 1.307   -9.317  38.203 1.00 16.64  ? 80  ARG A HB2  1 
ATOM   1254 H  HB3  . ARG A 1 80  ? 2.375   -10.016 39.139 1.00 16.64  ? 80  ARG A HB3  1 
ATOM   1255 H  HG2  . ARG A 1 80  ? 1.876   -12.104 38.264 1.00 17.87  ? 80  ARG A HG2  1 
ATOM   1256 H  HG3  . ARG A 1 80  ? 0.647   -11.519 37.454 1.00 17.87  ? 80  ARG A HG3  1 
ATOM   1257 H  HD2  . ARG A 1 80  ? 3.349   -10.829 36.894 1.00 16.57  ? 80  ARG A HD2  1 
ATOM   1258 H  HD3  . ARG A 1 80  ? 2.525   -11.900 36.055 1.00 16.57  ? 80  ARG A HD3  1 
ATOM   1259 H  HE   . ARG A 1 80  ? 1.124   -9.674  35.970 1.00 16.63  ? 80  ARG A HE   1 
ATOM   1260 H  HH11 . ARG A 1 80  ? 3.848   -10.797 34.314 1.00 16.61  ? 80  ARG A HH11 1 
ATOM   1261 H  HH12 . ARG A 1 80  ? 4.263   -9.367  33.969 1.00 16.61  ? 80  ARG A HH12 1 
ATOM   1262 H  HH21 . ARG A 1 80  ? 1.075   -8.274  34.223 1.00 16.62  ? 80  ARG A HH21 1 
ATOM   1263 H  HH22 . ARG A 1 80  ? 2.273   -8.187  33.285 1.00 16.62  ? 80  ARG A HH22 1 
ATOM   1264 N  N    . ALA A 1 81  ? 1.375   -9.264  41.874 1.00 23.54  ? 81  ALA A N    1 
ATOM   1265 C  CA   . ALA A 1 81  ? 1.563   -8.204  42.855 1.00 25.39  ? 81  ALA A CA   1 
ATOM   1266 C  C    . ALA A 1 81  ? 2.341   -7.014  42.272 1.00 23.65  ? 81  ALA A C    1 
ATOM   1267 O  O    . ALA A 1 81  ? 2.073   -5.866  42.617 1.00 24.87  ? 81  ALA A O    1 
ATOM   1268 C  CB   . ALA A 1 81  ? 2.244   -8.770  44.082 1.00 28.38  ? 81  ALA A CB   1 
ATOM   1269 H  H    . ALA A 1 81  ? 1.743   -10.086 42.028 1.00 21.93  ? 81  ALA A H    1 
ATOM   1270 H  HA   . ALA A 1 81  ? 0.671   -7.879  43.121 1.00 25.32  ? 81  ALA A HA   1 
ATOM   1271 H  HB1  . ALA A 1 81  ? 2.363   -8.066  44.741 1.00 27.29  ? 81  ALA A HB1  1 
ATOM   1272 H  HB2  . ALA A 1 81  ? 1.695   -9.477  44.462 1.00 27.29  ? 81  ALA A HB2  1 
ATOM   1273 H  HB3  . ALA A 1 81  ? 3.111   -9.132  43.836 1.00 27.29  ? 81  ALA A HB3  1 
ATOM   1274 N  N    . GLU A 1 82  ? 3.319   -7.274  41.399 1.00 22.77  ? 82  GLU A N    1 
ATOM   1275 C  CA   . GLU A 1 82  ? 4.151   -6.203  40.872 1.00 21.73  ? 82  GLU A CA   1 
ATOM   1276 C  C    . GLU A 1 82  ? 3.468   -5.463  39.729 1.00 18.46  ? 82  GLU A C    1 
ATOM   1277 O  O    . GLU A 1 82  ? 3.959   -4.406  39.334 1.00 18.12  ? 82  GLU A O    1 
ATOM   1278 C  CB   . GLU A 1 82  ? 5.537   -6.692  40.432 1.00 24.45  ? 82  GLU A CB   1 
ATOM   1279 C  CG   . GLU A 1 82  ? 5.669   -7.287  39.052 1.00 26.19  ? 82  GLU A CG   1 
ATOM   1280 C  CD   . GLU A 1 82  ? 5.218   -8.727  38.956 1.00 26.01  ? 82  GLU A CD   1 
ATOM   1281 O  OE1  . GLU A 1 82  ? 5.275   -9.281  37.817 1.00 26.60  ? 82  GLU A OE1  1 
ATOM   1282 O  OE2  . GLU A 1 82  ? 4.853   -9.315  40.035 1.00 28.82  ? 82  GLU A OE2  1 
ATOM   1283 H  H    . GLU A 1 82  ? 3.476   -8.133  41.130 1.00 24.86  ? 82  GLU A H    1 
ATOM   1284 H  HA   . GLU A 1 82  ? 4.288   -5.555  41.602 1.00 23.65  ? 82  GLU A HA   1 
ATOM   1285 H  HB2  . GLU A 1 82  ? 6.151   -5.931  40.492 1.00 24.94  ? 82  GLU A HB2  1 
ATOM   1286 H  HB3  . GLU A 1 82  ? 5.841   -7.357  41.084 1.00 24.94  ? 82  GLU A HB3  1 
ATOM   1287 H  HG2  . GLU A 1 82  ? 5.146   -6.753  38.421 1.00 39.73  ? 82  GLU A HG2  1 
ATOM   1288 H  HG3  . GLU A 1 82  ? 6.608   -7.237  38.773 1.00 39.73  ? 82  GLU A HG3  1 
ATOM   1289 N  N    . ALA A 1 83  ? 2.353   -5.997  39.212 1.00 15.47  ? 83  ALA A N    1 
ATOM   1290 C  CA   . ALA A 1 83  ? 1.719   -5.392  38.040 1.00 13.73  ? 83  ALA A CA   1 
ATOM   1291 C  C    . ALA A 1 83  ? 0.666   -4.398  38.513 1.00 12.34  ? 83  ALA A C    1 
ATOM   1292 O  O    . ALA A 1 83  ? -0.531  -4.641  38.443 1.00 13.78  ? 83  ALA A O    1 
ATOM   1293 C  CB   . ALA A 1 83  ? 1.161   -6.472  37.123 1.00 14.43  ? 83  ALA A CB   1 
ATOM   1294 H  H    . ALA A 1 83  ? 1.983   -6.747  39.580 1.00 18.40  ? 83  ALA A H    1 
ATOM   1295 H  HA   . ALA A 1 83  ? 2.406   -4.894  37.542 1.00 15.44  ? 83  ALA A HA   1 
ATOM   1296 H  HB1  . ALA A 1 83  ? 0.736   -6.057  36.353 1.00 30.30  ? 83  ALA A HB1  1 
ATOM   1297 H  HB2  . ALA A 1 83  ? 1.884   -7.048  36.821 1.00 30.37  ? 83  ALA A HB2  1 
ATOM   1298 H  HB3  . ALA A 1 83  ? 0.506   -7.003  37.606 1.00 30.30  ? 83  ALA A HB3  1 
ATOM   1299 N  N    . THR A 1 84  ? 1.148   -3.273  39.034 1.00 12.22  ? 84  THR A N    1 
ATOM   1300 C  CA   . THR A 1 84  ? 0.293   -2.289  39.685 1.00 12.01  ? 84  THR A CA   1 
ATOM   1301 C  C    . THR A 1 84  ? -0.298  -1.274  38.702 1.00 10.94  ? 84  THR A C    1 
ATOM   1302 O  O    . THR A 1 84  ? -1.185  -0.524  39.089 1.00 11.81  ? 84  THR A O    1 
ATOM   1303 C  CB   . THR A 1 84  ? 1.059   -1.590  40.826 1.00 12.04  ? 84  THR A CB   1 
ATOM   1304 O  OG1  . THR A 1 84  ? 2.266   -1.055  40.300 1.00 12.23  ? 84  THR A OG1  1 
ATOM   1305 C  CG2  . THR A 1 84  ? 1.383   -2.537  41.956 1.00 13.61  ? 84  THR A CG2  1 
ATOM   1306 H  H    . THR A 1 84  ? 2.045   -3.106  38.981 1.00 15.44  ? 84  THR A H    1 
ATOM   1307 H  HA   . THR A 1 84  ? -0.457  -2.778  40.091 1.00 32.97  ? 84  THR A HA   1 
ATOM   1308 H  HB   . THR A 1 84  ? 0.502   -0.852  41.174 1.00 15.62  ? 84  THR A HB   1 
ATOM   1309 H  HG1  . THR A 1 84  ? 2.131   -0.265  40.022 1.00 15.62  ? 84  THR A HG1  1 
ATOM   1310 H  HG21 . THR A 1 84  ? 1.828   -2.050  42.672 1.00 19.43  ? 84  THR A HG21 1 
ATOM   1311 H  HG22 . THR A 1 84  ? 0.560   -2.932  42.296 1.00 19.43  ? 84  THR A HG22 1 
ATOM   1312 H  HG23 . THR A 1 84  ? 1.970   -3.243  41.631 1.00 19.43  ? 84  THR A HG23 1 
ATOM   1313 N  N    . CYS A 1 85  ? 0.186   -1.243  37.453 1.00 11.12  ? 85  CYS A N    1 
ATOM   1314 C  CA   . CYS A 1 85  ? -0.465  -0.475  36.419 1.00 10.69  ? 85  CYS A CA   1 
ATOM   1315 C  C    . CYS A 1 85  ? -1.507  -1.329  35.720 1.00 10.77  ? 85  CYS A C    1 
ATOM   1316 O  O    . CYS A 1 85  ? -1.297  -2.531  35.504 1.00 10.99  ? 85  CYS A O    1 
ATOM   1317 C  CB   . CYS A 1 85  ? 0.500   -0.018  35.346 1.00 11.70  ? 85  CYS A CB   1 
ATOM   1318 S  SG   . CYS A 1 85  ? 1.770   1.148   35.859 1.00 13.78  ? 85  CYS A SG   1 
ATOM   1319 H  H    . CYS A 1 85  ? 0.945   -1.708  37.247 1.00 13.96  ? 85  CYS A H    1 
ATOM   1320 H  HA   . CYS A 1 85  ? -0.897  0.311   36.823 1.00 13.23  ? 85  CYS A HA   1 
ATOM   1321 H  HB2  . CYS A 1 85  ? 0.945   -0.803  34.971 1.00 13.98  ? 85  CYS A HB2  1 
ATOM   1322 H  HB3  . CYS A 1 85  ? -0.013  0.398   34.623 1.00 13.98  ? 85  CYS A HB3  1 
ATOM   1323 H  HG   . CYS A 1 85  ? 1.031   2.024   36.227 1.00 16.52  ? 85  CYS A HG   1 
ATOM   1324 N  N    . ALA A 1 86  ? -2.578  -0.688  35.275 1.00 10.98  ? 86  ALA A N    1 
ATOM   1325 C  CA   . ALA A 1 86  ? -3.527  -1.347  34.410 1.00 10.67  ? 86  ALA A CA   1 
ATOM   1326 C  C    . ALA A 1 86  ? -4.005  -0.362  33.356 1.00 9.79   ? 86  ALA A C    1 
ATOM   1327 O  O    . ALA A 1 86  ? -3.899  0.858   33.499 1.00 10.60  ? 86  ALA A O    1 
ATOM   1328 C  CB   . ALA A 1 86  ? -4.678  -1.969  35.188 1.00 11.32  ? 86  ALA A CB   1 
ATOM   1329 H  H    . ALA A 1 86  ? -2.725  0.182   35.516 1.00 13.23  ? 86  ALA A H    1 
ATOM   1330 H  HA   . ALA A 1 86  ? -3.052  -2.070  33.943 1.00 12.48  ? 86  ALA A HA   1 
ATOM   1331 H  HB1  . ALA A 1 86  ? -5.312  -2.368  34.569 1.00 15.79  ? 86  ALA A HB1  1 
ATOM   1332 H  HB2  . ALA A 1 86  ? -4.334  -2.655  35.784 1.00 15.79  ? 86  ALA A HB2  1 
ATOM   1333 H  HB3  . ALA A 1 86  ? -5.126  -1.283  35.711 1.00 15.79  ? 86  ALA A HB3  1 
ATOM   1334 N  N    . ALA A 1 87  ? -4.580  -0.919  32.300 1.00 9.78   ? 87  ALA A N    1 
ATOM   1335 C  CA   . ALA A 1 87  ? -5.225  -0.132  31.263 1.00 9.69   ? 87  ALA A CA   1 
ATOM   1336 C  C    . ALA A 1 87  ? -6.548  -0.804  30.915 1.00 9.36   ? 87  ALA A C    1 
ATOM   1337 O  O    . ALA A 1 87  ? -6.605  -2.013  30.717 1.00 9.79   ? 87  ALA A O    1 
ATOM   1338 C  CB   . ALA A 1 87  ? -4.350  0.009   30.025 1.00 10.37  ? 87  ALA A CB   1 
ATOM   1339 H  H    . ALA A 1 87  ? -4.571  -1.829  32.216 1.00 12.48  ? 87  ALA A H    1 
ATOM   1340 H  HA   . ALA A 1 87  ? -5.412  0.763   31.621 1.00 11.21  ? 87  ALA A HA   1 
ATOM   1341 H  HB1  . ALA A 1 87  ? -4.830  0.506   29.342 1.00 12.71  ? 87  ALA A HB1  1 
ATOM   1342 H  HB2  . ALA A 1 87  ? -3.534  0.484   30.256 1.00 12.71  ? 87  ALA A HB2  1 
ATOM   1343 H  HB3  . ALA A 1 87  ? -4.124  -0.873  29.684 1.00 12.71  ? 87  ALA A HB3  1 
ATOM   1344 N  N    . LEU A 1 88  ? -7.581  0.017   30.796 1.00 8.99   ? 88  LEU A N    1 
ATOM   1345 C  CA   . LEU A 1 88  ? -8.872  -0.388  30.270 1.00 8.83   ? 88  LEU A CA   1 
ATOM   1346 C  C    . LEU A 1 88  ? -9.052  0.332   28.950 1.00 8.98   ? 88  LEU A C    1 
ATOM   1347 O  O    . LEU A 1 88  ? -9.013  1.568   28.902 1.00 9.39   ? 88  LEU A O    1 
ATOM   1348 C  CB   . LEU A 1 88  ? -10.010 -0.007  31.224 1.00 9.34   ? 88  LEU A CB   1 
ATOM   1349 C  CG   . LEU A 1 88  ? -11.422 -0.222  30.684 1.00 10.19  ? 88  LEU A CG   1 
ATOM   1350 C  CD1  . LEU A 1 88  ? -11.732 -1.657  30.336 1.00 10.95  ? 88  LEU A CD1  1 
ATOM   1351 C  CD2  . LEU A 1 88  ? -12.467 0.316   31.669 1.00 11.70  ? 88  LEU A CD2  1 
ATOM   1352 H  H    . LEU A 1 88  ? -7.480  0.886   31.060 1.00 11.21  ? 88  LEU A H    1 
ATOM   1353 H  HA   . LEU A 1 88  ? -8.871  -1.360  30.118 1.00 13.10  ? 88  LEU A HA   1 
ATOM   1354 H  HB2  . LEU A 1 88  ? -9.910  -0.529  32.045 1.00 11.19  ? 88  LEU A HB2  1 
ATOM   1355 H  HB3  . LEU A 1 88  ? -9.909  0.937   31.461 1.00 11.19  ? 88  LEU A HB3  1 
ATOM   1356 H  HG   . LEU A 1 88  ? -11.506 0.307   29.853 1.00 17.25  ? 88  LEU A HG   1 
ATOM   1357 H  HD11 . LEU A 1 88  ? -12.670 -1.736  30.088 1.00 13.67  ? 88  LEU A HD11 1 
ATOM   1358 H  HD12 . LEU A 1 88  ? -11.176 -1.938  29.589 1.00 13.67  ? 88  LEU A HD12 1 
ATOM   1359 H  HD13 . LEU A 1 88  ? -11.553 -2.224  31.106 1.00 13.67  ? 88  LEU A HD13 1 
ATOM   1360 H  HD21 . LEU A 1 88  ? -13.358 0.189   31.300 1.00 13.70  ? 88  LEU A HD21 1 
ATOM   1361 H  HD22 . LEU A 1 88  ? -12.394 -0.163  32.513 1.00 13.70  ? 88  LEU A HD22 1 
ATOM   1362 H  HD23 . LEU A 1 88  ? -12.312 1.265   31.821 1.00 13.70  ? 88  LEU A HD23 1 
ATOM   1363 N  N    . ILE A 1 89  ? -9.196  -0.446  27.857 1.00 8.74   ? 89  ILE A N    1 
ATOM   1364 C  CA   . ILE A 1 89  ? -9.237  0.119   26.513 1.00 9.07   ? 89  ILE A CA   1 
ATOM   1365 C  C    . ILE A 1 89  ? -10.496 -0.426  25.832 1.00 8.63   ? 89  ILE A C    1 
ATOM   1366 O  O    . ILE A 1 89  ? -10.505 -1.491  25.201 1.00 9.24   ? 89  ILE A O    1 
ATOM   1367 C  CB   . ILE A 1 89  ? -7.956  -0.157  25.714 1.00 9.23   ? 89  ILE A CB   1 
ATOM   1368 C  CG1  . ILE A 1 89  ? -6.729  0.316   26.495 1.00 10.35  ? 89  ILE A CG1  1 
ATOM   1369 C  CG2  . ILE A 1 89  ? -8.056  0.503   24.351 1.00 10.37  ? 89  ILE A CG2  1 
ATOM   1370 C  CD1  . ILE A 1 89  ? -5.402  0.103   25.797 1.00 10.85  ? 89  ILE A CD1  1 
ATOM   1371 H  H    . ILE A 1 89  ? -9.272  -1.351  27.955 1.00 13.10  ? 89  ILE A H    1 
ATOM   1372 H  HA   . ILE A 1 89  ? -9.328  1.081   26.593 1.00 17.25  ? 89  ILE A HA   1 
ATOM   1373 H  HB   . ILE A 1 89  ? -7.878  -1.131  25.583 1.00 12.63  ? 89  ILE A HB   1 
ATOM   1374 H  HG12 . ILE A 1 89  ? -6.831  1.272   26.684 1.00 12.62  ? 89  ILE A HG12 1 
ATOM   1375 H  HG13 . ILE A 1 89  ? -6.705  -0.156  27.353 1.00 12.62  ? 89  ILE A HG13 1 
ATOM   1376 H  HG21 . ILE A 1 89  ? -7.294  0.243   23.806 1.00 12.97  ? 89  ILE A HG21 1 
ATOM   1377 H  HG22 . ILE A 1 89  ? -8.876  0.224   23.909 1.00 12.97  ? 89  ILE A HG22 1 
ATOM   1378 H  HG23 . ILE A 1 89  ? -8.060  1.470   24.457 1.00 12.97  ? 89  ILE A HG23 1 
ATOM   1379 H  HD11 . ILE A 1 89  ? -4.677  0.206   26.438 1.00 13.00  ? 89  ILE A HD11 1 
ATOM   1380 H  HD12 . ILE A 1 89  ? -5.374  -0.792  25.418 1.00 13.00  ? 89  ILE A HD12 1 
ATOM   1381 H  HD13 . ILE A 1 89  ? -5.299  0.759   25.085 1.00 13.00  ? 89  ILE A HD13 1 
ATOM   1382 N  N    . PRO A 1 90  ? -11.613 0.323   25.934 1.00 8.81   ? 90  PRO A N    1 
ATOM   1383 C  CA   . PRO A 1 90  ? -12.816 -0.001  25.166 1.00 9.16   ? 90  PRO A CA   1 
ATOM   1384 C  C    . PRO A 1 90  ? -12.593 0.313   23.692 1.00 9.37   ? 90  PRO A C    1 
ATOM   1385 O  O    . PRO A 1 90  ? -12.055 1.370   23.367 1.00 10.44  ? 90  PRO A O    1 
ATOM   1386 C  CB   . PRO A 1 90  ? -13.887 0.891   25.814 1.00 9.88   ? 90  PRO A CB   1 
ATOM   1387 C  CG   . PRO A 1 90  ? -13.315 1.251   27.175 1.00 10.55  ? 90  PRO A CG   1 
ATOM   1388 C  CD   . PRO A 1 90  ? -11.846 1.417   26.886 1.00 9.45   ? 90  PRO A CD   1 
ATOM   1389 H  HA   . PRO A 1 90  ? -13.049 -0.954  25.293 1.00 11.17  ? 90  PRO A HA   1 
ATOM   1390 H  HB2  . PRO A 1 90  ? -14.043 1.698   25.278 1.00 12.06  ? 90  PRO A HB2  1 
ATOM   1391 H  HB3  . PRO A 1 90  ? -14.734 0.406   25.909 1.00 12.06  ? 90  PRO A HB3  1 
ATOM   1392 H  HG2  . PRO A 1 90  ? -13.705 2.082   27.514 1.00 12.61  ? 90  PRO A HG2  1 
ATOM   1393 H  HG3  . PRO A 1 90  ? -13.469 0.534   27.824 1.00 12.61  ? 90  PRO A HG3  1 
ATOM   1394 H  HD2  . PRO A 1 90  ? -11.659 2.285   26.484 1.00 17.26  ? 90  PRO A HD2  1 
ATOM   1395 H  HD3  . PRO A 1 90  ? -11.312 1.310   27.694 1.00 17.25  ? 90  PRO A HD3  1 
ATOM   1396 N  N    . ILE A 1 91  ? -13.059 -0.604  22.830 1.00 9.26   ? 91  ILE A N    1 
ATOM   1397 C  CA   . ILE A 1 91  ? -12.856 -0.523  21.399 1.00 9.64   ? 91  ILE A CA   1 
ATOM   1398 C  C    . ILE A 1 91  ? -14.166 -0.833  20.685 1.00 9.26   ? 91  ILE A C    1 
ATOM   1399 O  O    . ILE A 1 91  ? -14.889 -1.776  21.048 1.00 9.56   ? 91  ILE A O    1 
ATOM   1400 C  CB   . ILE A 1 91  ? -11.772 -1.510  20.938 1.00 10.27  ? 91  ILE A CB   1 
ATOM   1401 C  CG1  . ILE A 1 91  ? -10.441 -0.977  21.464 1.00 12.85  ? 91  ILE A CG1  1 
ATOM   1402 C  CG2  . ILE A 1 91  ? -11.781 -1.742  19.431 1.00 11.31  ? 91  ILE A CG2  1 
ATOM   1403 C  CD1  . ILE A 1 91  ? -9.256  -1.851  21.310 1.00 14.12  ? 91  ILE A CD1  1 
ATOM   1404 H  H    . ILE A 1 91  ? -13.529 -1.315  23.159 1.00 11.17  ? 91  ILE A H    1 
ATOM   1405 H  HA   . ILE A 1 91  ? -12.576 0.379   21.170 1.00 15.84  ? 91  ILE A HA   1 
ATOM   1406 H  HB   . ILE A 1 91  ? -11.945 -2.377  21.381 1.00 12.30  ? 91  ILE A HB   1 
ATOM   1407 H  HG12 . ILE A 1 91  ? -10.253 -0.128  21.009 1.00 15.84  ? 91  ILE A HG12 1 
ATOM   1408 H  HG13 . ILE A 1 91  ? -10.545 -0.779  22.417 1.00 15.84  ? 91  ILE A HG13 1 
ATOM   1409 H  HG21 . ILE A 1 91  ? -10.926 -2.113  19.151 1.00 14.99  ? 91  ILE A HG21 1 
ATOM   1410 H  HG22 . ILE A 1 91  ? -12.491 -2.365  19.199 1.00 14.99  ? 91  ILE A HG22 1 
ATOM   1411 H  HG23 . ILE A 1 91  ? -11.930 -0.897  18.970 1.00 14.99  ? 91  ILE A HG23 1 
ATOM   1412 H  HD11 . ILE A 1 91  ? -8.507  -1.470  21.801 1.00 14.99  ? 91  ILE A HD11 1 
ATOM   1413 H  HD12 . ILE A 1 91  ? -9.456  -2.736  21.660 1.00 14.99  ? 91  ILE A HD12 1 
ATOM   1414 H  HD13 . ILE A 1 91  ? -9.021  -1.921  20.368 1.00 14.99  ? 91  ILE A HD13 1 
ATOM   1415 N  N    . ARG A 1 92  ? -14.489 -0.055  19.642 1.00 9.52   ? 92  ARG A N    1 
ATOM   1416 C  CA   . ARG A 1 92  ? -15.573 -0.354  18.733 1.00 9.78   ? 92  ARG A CA   1 
ATOM   1417 C  C    . ARG A 1 92  ? -15.025 -0.513  17.320 1.00 9.81   ? 92  ARG A C    1 
ATOM   1418 O  O    . ARG A 1 92  ? -14.150 0.265   16.921 1.00 11.10  ? 92  ARG A O    1 
ATOM   1419 C  CB   . ARG A 1 92  ? -16.635 0.748   18.789 1.00 10.37  ? 92  ARG A CB   1 
ATOM   1420 C  CG   . ARG A 1 92  ? -17.964 0.378   18.146 1.00 11.42  ? 92  ARG A CG   1 
ATOM   1421 C  CD   . ARG A 1 92  ? -18.915 1.530   18.179 1.00 13.66  ? 92  ARG A CD   1 
ATOM   1422 N  NE   . ARG A 1 92  ? -18.622 2.469   17.145 1.00 14.85  ? 92  ARG A NE   1 
ATOM   1423 C  CZ   . ARG A 1 92  ? -19.342 3.554   16.856 1.00 16.65  ? 92  ARG A CZ   1 
ATOM   1424 N  NH1  . ARG A 1 92  ? -20.292 3.948   17.676 1.00 20.13  ? 92  ARG A NH1  1 
ATOM   1425 N  NH2  . ARG A 1 92  ? -19.068 4.244   15.755 1.00 18.32  ? 92  ARG A NH2  1 
ATOM   1426 H  H    . ARG A 1 92  ? -14.001 0.704   19.496 1.00 15.84  ? 92  ARG A H    1 
ATOM   1427 H  HA   . ARG A 1 92  ? -15.987 -1.204  19.007 1.00 11.44  ? 92  ARG A HA   1 
ATOM   1428 H  HB2  . ARG A 1 92  ? -16.793 0.980   19.728 1.00 21.69  ? 92  ARG A HB2  1 
ATOM   1429 H  HB3  . ARG A 1 92  ? -16.281 1.543   18.340 1.00 21.58  ? 92  ARG A HB3  1 
ATOM   1430 H  HG2  . ARG A 1 92  ? -17.816 0.106   17.215 1.00 25.58  ? 92  ARG A HG2  1 
ATOM   1431 H  HG3  . ARG A 1 92  ? -18.360 -0.381  18.626 1.00 25.58  ? 92  ARG A HG3  1 
ATOM   1432 H  HD2  . ARG A 1 92  ? -19.831 1.199   18.067 1.00 25.80  ? 92  ARG A HD2  1 
ATOM   1433 H  HD3  . ARG A 1 92  ? -18.857 1.976   19.050 1.00 25.65  ? 92  ARG A HD3  1 
ATOM   1434 H  HE   . ARG A 1 92  ? -17.912 2.327   16.666 1.00 25.58  ? 92  ARG A HE   1 
ATOM   1435 H  HH11 . ARG A 1 92  ? -20.257 3.735   18.530 1.00 25.52  ? 92  ARG A HH11 1 
ATOM   1436 H  HH12 . ARG A 1 92  ? -20.962 4.431   17.367 1.00 25.52  ? 92  ARG A HH12 1 
ATOM   1437 H  HH21 . ARG A 1 92  ? -19.167 3.867   14.967 1.00 23.95  ? 92  ARG A HH21 1 
ATOM   1438 H  HH22 . ARG A 1 92  ? -18.790 5.075   15.817 1.00 23.95  ? 92  ARG A HH22 1 
ATOM   1439 N  N    . LYS A 1 93  ? -15.532 -1.516  16.598 1.00 9.99   ? 93  LYS A N    1 
ATOM   1440 C  CA   . LYS A 1 93  ? -15.208 -1.713  15.190 1.00 10.64  ? 93  LYS A CA   1 
ATOM   1441 C  C    . LYS A 1 93  ? -16.410 -1.364  14.334 1.00 11.14  ? 93  LYS A C    1 
ATOM   1442 O  O    . LYS A 1 93  ? -17.540 -1.506  14.788 1.00 11.94  ? 93  LYS A O    1 
ATOM   1443 C  CB   . LYS A 1 93  ? -14.717 -3.143  14.925 1.00 11.00  ? 93  LYS A CB   1 
ATOM   1444 C  CG   . LYS A 1 93  ? -13.355 -3.427  15.564 1.00 11.61  ? 93  LYS A CG   1 
ATOM   1445 C  CD   . LYS A 1 93  ? -12.793 -4.804  15.216 1.00 11.36  ? 93  LYS A CD   1 
ATOM   1446 C  CE   . LYS A 1 93  ? -11.412 -5.011  15.764 1.00 11.82  ? 93  LYS A CE   1 
ATOM   1447 N  NZ   . LYS A 1 93  ? -10.779 -6.245  15.230 1.00 11.48  ? 93  LYS A NZ   1 
ATOM   1448 H  H    . LYS A 1 93  ? -16.105 -2.105  16.999 1.00 11.44  ? 93  LYS A H    1 
ATOM   1449 H  HA   . LYS A 1 93  ? -14.481 -1.094  14.960 1.00 13.58  ? 93  LYS A HA   1 
ATOM   1450 H  HB2  . LYS A 1 93  ? -15.375 -3.776  15.281 1.00 13.19  ? 93  LYS A HB2  1 
ATOM   1451 H  HB3  . LYS A 1 93  ? -14.652 -3.282  13.957 1.00 13.19  ? 93  LYS A HB3  1 
ATOM   1452 H  HG2  . LYS A 1 93  ? -12.720 -2.740  15.269 1.00 14.31  ? 93  LYS A HG2  1 
ATOM   1453 H  HG3  . LYS A 1 93  ? -13.443 -3.356  16.538 1.00 14.31  ? 93  LYS A HG3  1 
ATOM   1454 H  HD2  . LYS A 1 93  ? -13.387 -5.495  15.578 1.00 14.68  ? 93  LYS A HD2  1 
ATOM   1455 H  HD3  . LYS A 1 93  ? -12.769 -4.905  14.241 1.00 14.68  ? 93  LYS A HD3  1 
ATOM   1456 H  HE2  . LYS A 1 93  ? -10.853 -4.245  15.535 1.00 19.95  ? 93  LYS A HE2  1 
ATOM   1457 H  HE3  . LYS A 1 93  ? -11.454 -5.073  16.737 1.00 19.95  ? 93  LYS A HE3  1 
ATOM   1458 H  HZ1  . LYS A 1 93  ? -11.364 -6.937  15.279 1.00 14.33  ? 93  LYS A HZ1  1 
ATOM   1459 H  HZ2  . LYS A 1 93  ? -10.541 -6.118  14.364 1.00 14.33  ? 93  LYS A HZ2  1 
ATOM   1460 H  HZ3  . LYS A 1 93  ? -10.040 -6.447  15.716 1.00 14.33  ? 93  LYS A HZ3  1 
ATOM   1461 N  N    . ASN A 1 94  ? -16.173 -0.935  13.115 1.00 11.85  ? 94  ASN A N    1 
ATOM   1462 C  CA   . ASN A 1 94  ? -17.208 -0.353  12.284 1.00 12.90  ? 94  ASN A CA   1 
ATOM   1463 C  C    . ASN A 1 94  ? -18.118 -1.418  11.693 1.00 12.65  ? 94  ASN A C    1 
ATOM   1464 O  O    . ASN A 1 94  ? -17.850 -2.622  11.726 1.00 12.86  ? 94  ASN A O    1 
ATOM   1465 C  CB   . ASN A 1 94  ? -16.582 0.579   11.243 1.00 14.05  ? 94  ASN A CB   1 
ATOM   1466 C  CG   . ASN A 1 94  ? -15.791 -0.123  10.150 1.00 13.84  ? 94  ASN A CG   1 
ATOM   1467 O  OD1  . ASN A 1 94  ? -16.025 -1.282  9.798  1.00 16.01  ? 94  ASN A OD1  1 
ATOM   1468 N  ND2  . ASN A 1 94  ? -14.858 0.621   9.572  1.00 15.01  ? 94  ASN A ND2  1 
ATOM   1469 H  H    . ASN A 1 94  ? -15.328 -1.008  12.776 1.00 13.58  ? 94  ASN A H    1 
ATOM   1470 H  HA   . ASN A 1 94  ? -17.759 0.215   12.870 1.00 22.04  ? 94  ASN A HA   1 
ATOM   1471 H  HB2  . ASN A 1 94  ? -17.294 1.103   10.826 1.00 21.71  ? 94  ASN A HB2  1 
ATOM   1472 H  HB3  . ASN A 1 94  ? -15.987 1.203   11.707 1.00 21.70  ? 94  ASN A HB3  1 
ATOM   1473 H  HD21 . ASN A 1 94  ? -14.212 0.238   9.106  1.00 21.50  ? 94  ASN A HD21 1 
ATOM   1474 H  HD22 . ASN A 1 94  ? -14.881 1.502   9.650  1.00 21.51  ? 94  ASN A HD22 1 
ATOM   1475 N  N    . PRO A 1 95  ? -19.274 -0.991  11.140 1.00 13.44  ? 95  PRO A N    1 
ATOM   1476 C  CA   . PRO A 1 95  ? -20.213 -1.990  10.616 1.00 13.94  ? 95  PRO A CA   1 
ATOM   1477 C  C    . PRO A 1 95  ? -19.646 -2.846  9.494  1.00 13.97  ? 95  PRO A C    1 
ATOM   1478 O  O    . PRO A 1 95  ? -20.014 -4.014  9.338  1.00 15.57  ? 95  PRO A O    1 
ATOM   1479 C  CB   . PRO A 1 95  ? -21.425 -1.159  10.179 1.00 15.76  ? 95  PRO A CB   1 
ATOM   1480 C  CG   . PRO A 1 95  ? -21.355 0.059   11.112 1.00 16.14  ? 95  PRO A CG   1 
ATOM   1481 C  CD   . PRO A 1 95  ? -19.871 0.356   11.229 1.00 14.79  ? 95  PRO A CD   1 
ATOM   1482 H  HA   . PRO A 1 95  ? -20.490 -2.579  11.362 1.00 16.79  ? 95  PRO A HA   1 
ATOM   1483 H  HB2  . PRO A 1 95  ? -21.351 -0.888  9.239  1.00 40.11  ? 95  PRO A HB2  1 
ATOM   1484 H  HB3  . PRO A 1 95  ? -22.261 -1.655  10.307 1.00 40.08  ? 95  PRO A HB3  1 
ATOM   1485 H  HG2  . PRO A 1 95  ? -21.834 0.821   10.729 1.00 18.92  ? 95  PRO A HG2  1 
ATOM   1486 H  HG3  . PRO A 1 95  ? -21.738 -0.150  11.989 1.00 18.92  ? 95  PRO A HG3  1 
ATOM   1487 H  HD2  . PRO A 1 95  ? -19.566 0.926   10.499 1.00 22.03  ? 95  PRO A HD2  1 
ATOM   1488 H  HD3  . PRO A 1 95  ? -19.663 0.783   12.079 1.00 22.04  ? 95  PRO A HD3  1 
ATOM   1489 N  N    . SER A 1 96  ? -18.777 -2.264  8.661  1.00 14.04  ? 96  SER A N    1 
ATOM   1490 C  CA   . SER A 1 96  ? -18.188 -3.027  7.581  1.00 15.12  ? 96  SER A CA   1 
ATOM   1491 C  C    . SER A 1 96  ? -17.455 -4.257  8.111  1.00 13.72  ? 96  SER A C    1 
ATOM   1492 O  O    . SER A 1 96  ? -17.560 -5.356  7.557  1.00 14.45  ? 96  SER A O    1 
ATOM   1493 C  CB   . SER A 1 96  ? -17.264 -2.155  6.757  1.00 17.70  ? 96  SER A CB   1 
ATOM   1494 O  OG   . SER A 1 96  ? -18.006 -1.157  6.082  1.00 23.91  ? 96  SER A OG   1 
ATOM   1495 H  H    . SER A 1 96  ? -18.555 -1.384  8.763  1.00 20.69  ? 96  SER A H    1 
ATOM   1496 H  HA   . SER A 1 96  ? -18.927 -3.340  6.992  1.00 17.86  ? 96  SER A HA   1 
ATOM   1497 H  HB2  . SER A 1 96  ? -16.599 -1.732  7.345  1.00 20.72  ? 96  SER A HB2  1 
ATOM   1498 H  HB3  . SER A 1 96  ? -16.785 -2.711  6.101  1.00 20.72  ? 96  SER A HB3  1 
ATOM   1499 H  HG   . SER A 1 96  ? -17.473 -0.696  5.614  1.00 25.27  ? 96  SER A HG   1 
ATOM   1500 N  N    . TRP A 1 97  ? -16.677 -4.077  9.181  1.00 12.58  ? 97  TRP A N    1 
ATOM   1501 C  CA   . TRP A 1 97  ? -15.950 -5.184  9.782  1.00 11.85  ? 97  TRP A CA   1 
ATOM   1502 C  C    . TRP A 1 97  ? -16.882 -6.350  10.094 1.00 11.18  ? 97  TRP A C    1 
ATOM   1503 O  O    . TRP A 1 97  ? -16.613 -7.493  9.739  1.00 11.67  ? 97  TRP A O    1 
ATOM   1504 C  CB   . TRP A 1 97  ? -15.261 -4.699  11.055 1.00 11.69  ? 97  TRP A CB   1 
ATOM   1505 C  CG   . TRP A 1 97  ? -14.620 -5.814  11.838 1.00 10.23  ? 97  TRP A CG   1 
ATOM   1506 C  CD1  . TRP A 1 97  ? -15.129 -6.466  12.917 1.00 10.52  ? 97  TRP A CD1  1 
ATOM   1507 C  CD2  . TRP A 1 97  ? -13.356 -6.440  11.561 1.00 10.65  ? 97  TRP A CD2  1 
ATOM   1508 N  NE1  . TRP A 1 97  ? -14.260 -7.424  13.359 1.00 10.50  ? 97  TRP A NE1  1 
ATOM   1509 C  CE2  . TRP A 1 97  ? -13.172 -7.454  12.532 1.00 9.97   ? 97  TRP A CE2  1 
ATOM   1510 C  CE3  . TRP A 1 97  ? -12.378 -6.261  10.580 1.00 12.24  ? 97  TRP A CE3  1 
ATOM   1511 C  CZ2  . TRP A 1 97  ? -12.009 -8.242  12.574 1.00 10.90  ? 97  TRP A CZ2  1 
ATOM   1512 C  CZ3  . TRP A 1 97  ? -11.250 -7.046  10.612 1.00 12.66  ? 97  TRP A CZ3  1 
ATOM   1513 C  CH2  . TRP A 1 97  ? -11.066 -8.005  11.600 1.00 11.91  ? 97  TRP A CH2  1 
ATOM   1514 H  H    . TRP A 1 97  ? -16.591 -3.243  9.544  1.00 14.65  ? 97  TRP A H    1 
ATOM   1515 H  HA   . TRP A 1 97  ? -15.258 -5.482  9.146  1.00 14.36  ? 97  TRP A HA   1 
ATOM   1516 H  HB2  . TRP A 1 97  ? -14.578 -4.043  10.809 1.00 14.67  ? 97  TRP A HB2  1 
ATOM   1517 H  HB3  . TRP A 1 97  ? -15.923 -4.251  11.617 1.00 14.67  ? 97  TRP A HB3  1 
ATOM   1518 H  HD1  . TRP A 1 97  ? -15.949 -6.259  13.335 1.00 13.90  ? 97  TRP A HD1  1 
ATOM   1519 H  HE1  . TRP A 1 97  ? -14.392 -7.935  14.044 1.00 13.90  ? 97  TRP A HE1  1 
ATOM   1520 H  HE3  . TRP A 1 97  ? -12.478 -5.592  9.921  1.00 13.90  ? 97  TRP A HE3  1 
ATOM   1521 H  HZ2  . TRP A 1 97  ? -11.888 -8.908  13.225 1.00 13.90  ? 97  TRP A HZ2  1 
ATOM   1522 H  HZ3  . TRP A 1 97  ? -10.576 -6.916  9.964  1.00 13.90  ? 97  TRP A HZ3  1 
ATOM   1523 H  HH2  . TRP A 1 97  ? -10.290 -8.537  11.580 1.00 13.90  ? 97  TRP A HH2  1 
ATOM   1524 N  N    . TRP A 1 98  ? -18.005 -6.047  10.770 1.00 11.21  ? 98  TRP A N    1 
ATOM   1525 C  CA   . TRP A 1 98  ? -18.867 -7.100  11.266 1.00 11.30  ? 98  TRP A CA   1 
ATOM   1526 C  C    . TRP A 1 98  ? -19.568 -7.860  10.144 1.00 11.75  ? 98  TRP A C    1 
ATOM   1527 O  O    . TRP A 1 98  ? -19.992 -9.008  10.329 1.00 13.48  ? 98  TRP A O    1 
ATOM   1528 C  CB   . TRP A 1 98  ? -19.866 -6.546  12.290 1.00 11.40  ? 98  TRP A CB   1 
ATOM   1529 C  CG   . TRP A 1 98  ? -19.163 -6.040  13.513 1.00 10.62  ? 98  TRP A CG   1 
ATOM   1530 C  CD1  . TRP A 1 98  ? -18.976 -4.754  13.913 1.00 11.35  ? 98  TRP A CD1  1 
ATOM   1531 C  CD2  . TRP A 1 98  ? -18.475 -6.856  14.460 1.00 10.23  ? 98  TRP A CD2  1 
ATOM   1532 N  NE1  . TRP A 1 98  ? -18.234 -4.724  15.057 1.00 10.58  ? 98  TRP A NE1  1 
ATOM   1533 C  CE2  . TRP A 1 98  ? -17.904 -5.997  15.409 1.00 10.19  ? 98  TRP A CE2  1 
ATOM   1534 C  CE3  . TRP A 1 98  ? -18.288 -8.233  14.594 1.00 11.12  ? 98  TRP A CE3  1 
ATOM   1535 C  CZ2  . TRP A 1 98  ? -17.157 -6.468  16.475 1.00 10.58  ? 98  TRP A CZ2  1 
ATOM   1536 C  CZ3  . TRP A 1 98  ? -17.557 -8.696  15.665 1.00 12.21  ? 98  TRP A CZ3  1 
ATOM   1537 C  CH2  . TRP A 1 98  ? -17.003 -7.827  16.595 1.00 11.92  ? 98  TRP A CH2  1 
ATOM   1538 H  H    . TRP A 1 98  ? -18.231 -5.174  10.921 1.00 13.52  ? 98  TRP A H    1 
ATOM   1539 H  HA   . TRP A 1 98  ? -18.290 -7.740  11.745 1.00 13.67  ? 98  TRP A HA   1 
ATOM   1540 H  HB2  . TRP A 1 98  ? -20.373 -5.818  11.877 1.00 13.52  ? 98  TRP A HB2  1 
ATOM   1541 H  HB3  . TRP A 1 98  ? -20.492 -7.256  12.540 1.00 13.52  ? 98  TRP A HB3  1 
ATOM   1542 H  HD1  . TRP A 1 98  ? -19.312 -3.990  13.471 1.00 11.47  ? 98  TRP A HD1  1 
ATOM   1543 H  HE1  . TRP A 1 98  ? -17.998 -3.998  15.489 1.00 11.47  ? 98  TRP A HE1  1 
ATOM   1544 H  HE3  . TRP A 1 98  ? -18.650 -8.832  13.960 1.00 11.47  ? 98  TRP A HE3  1 
ATOM   1545 H  HZ2  . TRP A 1 98  ? -16.805 -5.877  17.118 1.00 11.47  ? 98  TRP A HZ2  1 
ATOM   1546 H  HZ3  . TRP A 1 98  ? -17.421 -9.624  15.764 1.00 11.47  ? 98  TRP A HZ3  1 
ATOM   1547 H  HH2  . TRP A 1 98  ? -16.514 -8.173  17.318 1.00 11.47  ? 98  TRP A HH2  1 
ATOM   1548 N  N    . GLY A 1 99  ? -19.708 -7.221  8.978  1.00 11.92  ? 99  GLY A N    1 
ATOM   1549 C  CA   . GLY A 1 99  ? -20.294 -7.887  7.825  1.00 12.63  ? 99  GLY A CA   1 
ATOM   1550 C  C    . GLY A 1 99  ? -19.331 -8.728  6.994  1.00 12.52  ? 99  GLY A C    1 
ATOM   1551 O  O    . GLY A 1 99  ? -19.768 -9.444  6.098  1.00 14.50  ? 99  GLY A O    1 
ATOM   1552 H  H    . GLY A 1 99  ? -19.447 -6.349  8.899  1.00 14.25  ? 99  GLY A H    1 
ATOM   1553 H  HA2  . GLY A 1 99  ? -21.034 -8.465  8.138  1.00 15.03  ? 99  GLY A HA2  1 
ATOM   1554 H  HA3  . GLY A 1 99  ? -20.694 -7.196  7.240  1.00 15.03  ? 99  GLY A HA3  1 
ATOM   1555 N  N    . LEU A 1 100 ? -18.035 -8.610  7.260  1.00 11.73  ? 100 LEU A N    1 
ATOM   1556 C  CA   . LEU A 1 100 ? -17.058 -9.440  6.566  1.00 11.95  ? 100 LEU A CA   1 
ATOM   1557 C  C    . LEU A 1 100 ? -17.212 -10.900 6.993  1.00 11.48  ? 100 LEU A C    1 
ATOM   1558 O  O    . LEU A 1 100 ? -17.635 -11.192 8.111  1.00 11.88  ? 100 LEU A O    1 
ATOM   1559 C  CB   . LEU A 1 100 ? -15.631 -8.980  6.867  1.00 12.09  ? 100 LEU A CB   1 
ATOM   1560 C  CG   . LEU A 1 100 ? -15.258 -7.565  6.408  1.00 13.59  ? 100 LEU A CG   1 
ATOM   1561 C  CD1  . LEU A 1 100 ? -13.848 -7.244  6.861  1.00 14.19  ? 100 LEU A CD1  1 
ATOM   1562 C  CD2  . LEU A 1 100 ? -15.389 -7.401  4.908  1.00 15.67  ? 100 LEU A CD2  1 
ATOM   1563 H  H    . LEU A 1 100 ? -17.744 -8.002  7.877  1.00 14.24  ? 100 LEU A H    1 
ATOM   1564 H  HA   . LEU A 1 100 ? -17.227 -9.374  5.598  1.00 16.74  ? 100 LEU A HA   1 
ATOM   1565 H  HB2  . LEU A 1 100 ? -15.494 -9.033  7.833  1.00 13.66  ? 100 LEU A HB2  1 
ATOM   1566 H  HB3  . LEU A 1 100 ? -15.013 -9.611  6.448  1.00 13.66  ? 100 LEU A HB3  1 
ATOM   1567 H  HG   . LEU A 1 100 ? -15.873 -6.928  6.843  1.00 14.24  ? 100 LEU A HG   1 
ATOM   1568 H  HD11 . LEU A 1 100 ? -13.611 -6.345  6.574  1.00 16.97  ? 100 LEU A HD11 1 
ATOM   1569 H  HD12 . LEU A 1 100 ? -13.799 -7.297  7.832  1.00 16.97  ? 100 LEU A HD12 1 
ATOM   1570 H  HD13 . LEU A 1 100 ? -13.227 -7.882  6.470  1.00 16.97  ? 100 LEU A HD13 1 
ATOM   1571 H  HD21 . LEU A 1 100 ? -14.988 -6.557  4.636  1.00 16.90  ? 100 LEU A HD21 1 
ATOM   1572 H  HD22 . LEU A 1 100 ? -14.933 -8.135  4.460  1.00 16.89  ? 100 LEU A HD22 1 
ATOM   1573 H  HD23 . LEU A 1 100 ? -16.330 -7.406  4.661  1.00 16.89  ? 100 LEU A HD23 1 
ATOM   1574 N  N    . SER A 1 101 ? -16.795 -11.807 6.099  1.00 11.80  ? 101 SER A N    1 
ATOM   1575 C  CA   A SER A 1 101 ? -16.808 -13.227 6.404  0.54 11.81  ? 101 SER A CA   1 
ATOM   1576 C  CA   B SER A 1 101 ? -16.794 -13.232 6.385  0.46 11.58  ? 101 SER A CA   1 
ATOM   1577 C  C    . SER A 1 101 ? -15.602 -13.597 7.268  1.00 11.15  ? 101 SER A C    1 
ATOM   1578 O  O    . SER A 1 101 ? -14.708 -12.785 7.526  1.00 11.65  ? 101 SER A O    1 
ATOM   1579 C  CB   A SER A 1 101 ? -16.878 -14.037 5.125  0.54 13.93  ? 101 SER A CB   1 
ATOM   1580 C  CB   B SER A 1 101 ? -16.790 -14.026 5.097  0.46 12.96  ? 101 SER A CB   1 
ATOM   1581 O  OG   A SER A 1 101 ? -18.148 -13.866 4.510  0.54 18.07  ? 101 SER A OG   1 
ATOM   1582 O  OG   B SER A 1 101 ? -15.654 -13.709 4.312  0.46 14.86  ? 101 SER A OG   1 
ATOM   1583 H  H    A SER A 1 101 ? -16.495 -11.532 5.280  0.54 16.59  ? 101 SER A H    1 
ATOM   1584 H  H    B SER A 1 101 ? -16.501 -11.525 5.281  0.46 16.74  ? 101 SER A H    1 
ATOM   1585 H  HA   A SER A 1 101 ? -17.627 -13.416 6.932  0.54 14.61  ? 101 SER A HA   1 
ATOM   1586 H  HA   B SER A 1 101 ? -17.625 -13.447 6.883  0.46 14.28  ? 101 SER A HA   1 
ATOM   1587 H  HB2  A SER A 1 101 ? -16.170 -13.741 4.509  0.54 16.44  ? 101 SER A HB2  1 
ATOM   1588 H  HB2  B SER A 1 101 ? -16.788 -14.987 5.304  0.46 16.27  ? 101 SER A HB2  1 
ATOM   1589 H  HB3  A SER A 1 101 ? -16.735 -14.988 5.327  0.54 16.43  ? 101 SER A HB3  1 
ATOM   1590 H  HB3  B SER A 1 101 ? -17.607 -13.824 4.587  0.46 16.27  ? 101 SER A HB3  1 
ATOM   1591 H  HG   A SER A 1 101 ? -18.155 -13.121 4.110  0.54 20.27  ? 101 SER A HG   1 
ATOM   1592 H  HG   B SER A 1 101 ? -15.059 -14.294 4.453  0.46 16.92  ? 101 SER A HG   1 
ATOM   1593 N  N    . GLN A 1 102 ? -15.600 -14.840 7.754  1.00 11.06  ? 102 GLN A N    1 
ATOM   1594 C  CA   . GLN A 1 102 ? -14.604 -15.219 8.746  1.00 11.15  ? 102 GLN A CA   1 
ATOM   1595 C  C    . GLN A 1 102 ? -13.192 -15.210 8.183  1.00 11.19  ? 102 GLN A C    1 
ATOM   1596 O  O    . GLN A 1 102 ? -12.258 -14.792 8.859  1.00 11.50  ? 102 GLN A O    1 
ATOM   1597 C  CB   . GLN A 1 102 ? -14.956 -16.583 9.301  1.00 11.09  ? 102 GLN A CB   1 
ATOM   1598 C  CG   . GLN A 1 102 ? -13.960 -17.143 10.304 1.00 10.86  ? 102 GLN A CG   1 
ATOM   1599 C  CD   . GLN A 1 102 ? -13.818 -16.317 11.554 1.00 10.47  ? 102 GLN A CD   1 
ATOM   1600 O  OE1  . GLN A 1 102 ? -14.735 -15.584 11.945 1.00 11.11  ? 102 GLN A OE1  1 
ATOM   1601 N  NE2  . GLN A 1 102 ? -12.683 -16.482 12.218 1.00 11.36  ? 102 GLN A NE2  1 
ATOM   1602 H  H    . GLN A 1 102 ? -16.221 -15.452 7.482  1.00 16.32  ? 102 GLN A H    1 
ATOM   1603 H  HA   . GLN A 1 102 ? -14.646 -14.565 9.482  1.00 13.47  ? 102 GLN A HA   1 
ATOM   1604 H  HB2  . GLN A 1 102 ? -15.836 -16.525 9.726  1.00 16.26  ? 102 GLN A HB2  1 
ATOM   1605 H  HB3  . GLN A 1 102 ? -15.030 -17.209 8.551  1.00 16.26  ? 102 GLN A HB3  1 
ATOM   1606 H  HG2  . GLN A 1 102 ? -14.242 -18.047 10.557 1.00 21.10  ? 102 GLN A HG2  1 
ATOM   1607 H  HG3  . GLN A 1 102 ? -13.082 -17.219 9.874  1.00 21.11  ? 102 GLN A HG3  1 
ATOM   1608 H  HE21 . GLN A 1 102 ? -12.073 -17.050 11.921 1.00 20.89  ? 102 GLN A HE21 1 
ATOM   1609 H  HE22 . GLN A 1 102 ? -12.535 -16.026 12.960 1.00 20.89  ? 102 GLN A HE22 1 
ATOM   1610 N  N    . ASP A 1 103 ? -13.017 -15.716 6.964  1.00 12.01  ? 103 ASP A N    1 
ATOM   1611 C  CA   . ASP A 1 103 ? -11.707 -15.718 6.356  1.00 12.35  ? 103 ASP A CA   1 
ATOM   1612 C  C    . ASP A 1 103 ? -11.186 -14.300 6.147  1.00 11.92  ? 103 ASP A C    1 
ATOM   1613 O  O    . ASP A 1 103 ? -9.986  -14.038 6.311  1.00 12.59  ? 103 ASP A O    1 
ATOM   1614 C  CB   . ASP A 1 103 ? -11.684 -16.495 5.033  1.00 13.42  ? 103 ASP A CB   1 
ATOM   1615 C  CG   . ASP A 1 103 ? -12.673 -16.081 3.963  1.00 14.17  ? 103 ASP A CG   1 
ATOM   1616 O  OD1  . ASP A 1 103 ? -13.735 -15.528 4.306  1.00 14.07  ? 103 ASP A OD1  1 
ATOM   1617 O  OD2  . ASP A 1 103 ? -12.370 -16.346 2.776  1.00 17.49  ? 103 ASP A OD2  1 
ATOM   1618 H  H    . ASP A 1 103 ? -13.724 -16.074 6.509  1.00 14.22  ? 103 ASP A H    1 
ATOM   1619 H  HA   . ASP A 1 103 ? -11.093 -16.175 6.974  1.00 21.64  ? 103 ASP A HA   1 
ATOM   1620 H  HB2  . ASP A 1 103 ? -10.786 -16.420 4.650  1.00 15.97  ? 103 ASP A HB2  1 
ATOM   1621 H  HB3  . ASP A 1 103 ? -11.844 -17.441 5.232  1.00 15.97  ? 103 ASP A HB3  1 
ATOM   1622 N  N    . GLU A 1 104 ? -12.054 -13.385 5.747  1.00 12.16  ? 104 GLU A N    1 
ATOM   1623 C  CA   . GLU A 1 104 ? -11.658 -12.011 5.514  1.00 12.83  ? 104 GLU A CA   1 
ATOM   1624 C  C    . GLU A 1 104 ? -11.152 -11.376 6.798  1.00 11.85  ? 104 GLU A C    1 
ATOM   1625 O  O    . GLU A 1 104 ? -10.146 -10.665 6.811  1.00 12.62  ? 104 GLU A O    1 
ATOM   1626 C  CB   . GLU A 1 104 ? -12.828 -11.234 4.927  1.00 13.50  ? 104 GLU A CB   1 
ATOM   1627 C  CG   . GLU A 1 104 ? -13.188 -11.679 3.529  1.00 15.01  ? 104 GLU A CG   1 
ATOM   1628 C  CD   . GLU A 1 104 ? -14.520 -11.160 2.999  1.00 15.11  ? 104 GLU A CD   1 
ATOM   1629 O  OE1  . GLU A 1 104 ? -15.366 -10.717 3.784  1.00 16.33  ? 104 GLU A OE1  1 
ATOM   1630 O  OE2  . GLU A 1 104 ? -14.726 -11.240 1.770  1.00 17.31  ? 104 GLU A OE2  1 
ATOM   1631 H  H    . GLU A 1 104 ? -12.927 -13.622 5.613  1.00 16.92  ? 104 GLU A H    1 
ATOM   1632 H  HA   . GLU A 1 104 ? -10.923 -12.012 4.857  1.00 15.55  ? 104 GLU A HA   1 
ATOM   1633 H  HB2  . GLU A 1 104 ? -13.606 -11.350 5.512  1.00 16.91  ? 104 GLU A HB2  1 
ATOM   1634 H  HB3  . GLU A 1 104 ? -12.599 -10.281 4.912  1.00 16.91  ? 104 GLU A HB3  1 
ATOM   1635 H  HG2  . GLU A 1 104 ? -12.480 -11.388 2.915  1.00 16.92  ? 104 GLU A HG2  1 
ATOM   1636 H  HG3  . GLU A 1 104 ? -13.210 -12.659 3.504  1.00 16.92  ? 104 GLU A HG3  1 
ATOM   1637 N  N    . ARG A 1 105 ? -11.867 -11.582 7.912  1.00 11.23  ? 105 ARG A N    1 
ATOM   1638 C  CA   . ARG A 1 105 ? -11.454 -11.017 9.187  1.00 11.18  ? 105 ARG A CA   1 
ATOM   1639 C  C    . ARG A 1 105 ? -10.191 -11.673 9.716  1.00 10.92  ? 105 ARG A C    1 
ATOM   1640 O  O    . ARG A 1 105 ? -9.321  -10.965 10.230 1.00 11.05  ? 105 ARG A O    1 
ATOM   1641 C  CB   . ARG A 1 105 ? -12.598 -11.089 10.195 1.00 10.46  ? 105 ARG A CB   1 
ATOM   1642 C  CG   . ARG A 1 105 ? -13.627 -9.998  9.950  1.00 10.77  ? 105 ARG A CG   1 
ATOM   1643 C  CD   . ARG A 1 105 ? -14.806 -10.002 10.908 1.00 10.14  ? 105 ARG A CD   1 
ATOM   1644 N  NE   . ARG A 1 105 ? -15.881 -10.916 10.521 1.00 10.37  ? 105 ARG A NE   1 
ATOM   1645 C  CZ   . ARG A 1 105 ? -16.026 -12.182 10.902 1.00 10.25  ? 105 ARG A CZ   1 
ATOM   1646 N  NH1  . ARG A 1 105 ? -15.299 -12.712 11.877 1.00 10.71  ? 105 ARG A NH1  1 
ATOM   1647 N  NH2  . ARG A 1 105 ? -16.929 -12.917 10.293 1.00 11.61  ? 105 ARG A NH2  1 
ATOM   1648 H  H    . ARG A 1 105 ? -12.631 -12.082 7.874  1.00 12.88  ? 105 ARG A H    1 
ATOM   1649 H  HA   . ARG A 1 105 ? -11.251 -10.065 9.033  1.00 13.66  ? 105 ARG A HA   1 
ATOM   1650 H  HB2  . ARG A 1 105 ? -13.032 -11.965 10.128 1.00 12.88  ? 105 ARG A HB2  1 
ATOM   1651 H  HB3  . ARG A 1 105 ? -12.235 -10.993 11.100 1.00 12.88  ? 105 ARG A HB3  1 
ATOM   1652 H  HG2  . ARG A 1 105 ? -13.182 -9.126  10.009 1.00 13.66  ? 105 ARG A HG2  1 
ATOM   1653 H  HG3  . ARG A 1 105 ? -13.969 -10.090 9.036  1.00 13.66  ? 105 ARG A HG3  1 
ATOM   1654 H  HD2  . ARG A 1 105 ? -14.487 -10.249 11.800 1.00 12.93  ? 105 ARG A HD2  1 
ATOM   1655 H  HD3  . ARG A 1 105 ? -15.169 -9.094  10.967 1.00 12.93  ? 105 ARG A HD3  1 
ATOM   1656 H  HE   . ARG A 1 105 ? -16.493 -10.597 9.987  1.00 13.03  ? 105 ARG A HE   1 
ATOM   1657 H  HH11 . ARG A 1 105 ? -14.460 -12.932 11.728 1.00 12.88  ? 105 ARG A HH11 1 
ATOM   1658 H  HH12 . ARG A 1 105 ? -15.665 -12.857 12.666 1.00 12.88  ? 105 ARG A HH12 1 
ATOM   1659 H  HH21 . ARG A 1 105 ? -17.348 -12.605 9.586  1.00 13.03  ? 105 ARG A HH21 1 
ATOM   1660 H  HH22 . ARG A 1 105 ? -17.111 -13.723 10.594 1.00 13.03  ? 105 ARG A HH22 1 
ATOM   1661 N  N    . ARG A 1 106 ? -10.063 -12.995 9.603  1.00 10.93  ? 106 ARG A N    1 
ATOM   1662 C  CA   . ARG A 1 106 ? -8.819  -13.631 10.059 1.00 11.06  ? 106 ARG A CA   1 
ATOM   1663 C  C    . ARG A 1 106 ? -7.613  -13.093 9.280  1.00 11.05  ? 106 ARG A C    1 
ATOM   1664 O  O    . ARG A 1 106 ? -6.551  -12.863 9.845  1.00 11.61  ? 106 ARG A O    1 
ATOM   1665 C  CB   . ARG A 1 106 ? -8.919  -15.152 9.913  1.00 11.14  ? 106 ARG A CB   1 
ATOM   1666 C  CG   . ARG A 1 106 ? -7.605  -15.916 10.060 1.00 11.71  ? 106 ARG A CG   1 
ATOM   1667 C  CD   . ARG A 1 106 ? -6.906  -15.787 11.403 1.00 12.01  ? 106 ARG A CD   1 
ATOM   1668 N  NE   . ARG A 1 106 ? -5.542  -16.304 11.294 1.00 12.17  ? 106 ARG A NE   1 
ATOM   1669 C  CZ   . ARG A 1 106 ? -4.727  -16.641 12.296 1.00 11.92  ? 106 ARG A CZ   1 
ATOM   1670 N  NH1  . ARG A 1 106 ? -5.159  -16.750 13.535 1.00 12.04  ? 106 ARG A NH1  1 
ATOM   1671 N  NH2  . ARG A 1 106 ? -3.447  -16.882 12.046 1.00 12.77  ? 106 ARG A NH2  1 
ATOM   1672 H  H    . ARG A 1 106 ? -10.736 -13.505 9.254  1.00 13.45  ? 106 ARG A H    1 
ATOM   1673 H  HA   . ARG A 1 106 ? -8.695  -13.416 11.012 1.00 13.45  ? 106 ARG A HA   1 
ATOM   1674 H  HB2  . ARG A 1 106 ? -9.548  -15.485 10.588 1.00 13.45  ? 106 ARG A HB2  1 
ATOM   1675 H  HB3  . ARG A 1 106 ? -9.298  -15.352 9.032  1.00 13.45  ? 106 ARG A HB3  1 
ATOM   1676 H  HG2  . ARG A 1 106 ? -7.780  -16.868 9.898  1.00 14.74  ? 106 ARG A HG2  1 
ATOM   1677 H  HG3  . ARG A 1 106 ? -6.987  -15.615 9.360  1.00 14.74  ? 106 ARG A HG3  1 
ATOM   1678 H  HD2  . ARG A 1 106 ? -6.882  -14.845 11.676 1.00 14.73  ? 106 ARG A HD2  1 
ATOM   1679 H  HD3  . ARG A 1 106 ? -7.400  -16.294 12.082 1.00 14.73  ? 106 ARG A HD3  1 
ATOM   1680 H  HE   . ARG A 1 106 ? -5.224  -16.404 10.488 1.00 14.74  ? 106 ARG A HE   1 
ATOM   1681 H  HH11 . ARG A 1 106 ? -5.642  -16.104 13.890 1.00 14.74  ? 106 ARG A HH11 1 
ATOM   1682 H  HH12 . ARG A 1 106 ? -4.962  -17.468 14.006 1.00 14.74  ? 106 ARG A HH12 1 
ATOM   1683 H  HH21 . ARG A 1 106 ? -3.045  -16.470 11.382 1.00 14.74  ? 106 ARG A HH21 1 
ATOM   1684 H  HH22 . ARG A 1 106 ? -3.004  -17.454 12.545 1.00 14.74  ? 106 ARG A HH22 1 
ATOM   1685 N  N    . LYS A 1 107 ? -7.790  -12.916 7.964  1.00 11.79  ? 107 LYS A N    1 
ATOM   1686 C  CA   . LYS A 1 107 ? -6.691  -12.394 7.156  1.00 12.73  ? 107 LYS A CA   1 
ATOM   1687 C  C    . LYS A 1 107 ? -6.255  -11.019 7.656  1.00 12.59  ? 107 LYS A C    1 
ATOM   1688 O  O    . LYS A 1 107 ? -5.066  -10.748 7.789  1.00 13.34  ? 107 LYS A O    1 
ATOM   1689 C  CB   . LYS A 1 107 ? -7.089  -12.349 5.684  1.00 14.24  ? 107 LYS A CB   1 
ATOM   1690 C  CG   . LYS A 1 107 ? -6.016  -11.715 4.805  1.00 18.03  ? 107 LYS A CG   1 
ATOM   1691 C  CD   . LYS A 1 107 ? -6.321  -11.777 3.355  1.00 22.93  ? 107 LYS A CD   1 
ATOM   1692 C  CE   . LYS A 1 107 ? -5.191  -11.180 2.551  1.00 28.58  ? 107 LYS A CE   1 
ATOM   1693 N  NZ   . LYS A 1 107 ? -5.426  -11.363 1.104  1.00 34.11  ? 107 LYS A NZ   1 
ATOM   1694 H  H    . LYS A 1 107 ? -8.586  -13.124 7.565  1.00 16.53  ? 107 LYS A H    1 
ATOM   1695 H  HA   . LYS A 1 107 ? -5.928  -13.011 7.250  1.00 18.60  ? 107 LYS A HA   1 
ATOM   1696 H  HB2  . LYS A 1 107 ? -7.260  -13.262 5.372  1.00 16.90  ? 107 LYS A HB2  1 
ATOM   1697 H  HB3  . LYS A 1 107 ? -7.919  -11.835 5.595  1.00 16.90  ? 107 LYS A HB3  1 
ATOM   1698 H  HG2  . LYS A 1 107 ? -5.908  -10.776 5.064  1.00 23.35  ? 107 LYS A HG2  1 
ATOM   1699 H  HG3  . LYS A 1 107 ? -5.164  -12.171 4.971  1.00 23.35  ? 107 LYS A HG3  1 
ATOM   1700 H  HD2  . LYS A 1 107 ? -6.453  -12.712 3.087  1.00 27.31  ? 107 LYS A HD2  1 
ATOM   1701 H  HD3  . LYS A 1 107 ? -7.148  -11.282 3.172  1.00 27.30  ? 107 LYS A HD3  1 
ATOM   1702 H  HE2  . LYS A 1 107 ? -5.115  -10.227 2.746  1.00 23.35  ? 107 LYS A HE2  1 
ATOM   1703 H  HE3  . LYS A 1 107 ? -4.349  -11.610 2.795  1.00 23.35  ? 107 LYS A HE3  1 
ATOM   1704 H  HZ1  . LYS A 1 107 ? -4.715  -11.050 0.635  1.00 28.27  ? 107 LYS A HZ1  1 
ATOM   1705 H  HZ2  . LYS A 1 107 ? -5.539  -12.244 0.919  1.00 28.27  ? 107 LYS A HZ2  1 
ATOM   1706 H  HZ3  . LYS A 1 107 ? -6.170  -10.909 0.853  1.00 28.27  ? 107 LYS A HZ3  1 
ATOM   1707 N  N    . ILE A 1 108 ? -7.212  -10.124 7.906  1.00 12.00  ? 108 ILE A N    1 
ATOM   1708 C  CA   . ILE A 1 108 ? -6.875  -8.802  8.405  1.00 12.50  ? 108 ILE A CA   1 
ATOM   1709 C  C    . ILE A 1 108 ? -6.206  -8.887  9.768  1.00 12.25  ? 108 ILE A C    1 
ATOM   1710 O  O    . ILE A 1 108 ? -5.198  -8.230  10.017 1.00 12.73  ? 108 ILE A O    1 
ATOM   1711 C  CB   . ILE A 1 108 ? -8.106  -7.886  8.425  1.00 12.95  ? 108 ILE A CB   1 
ATOM   1712 C  CG1  . ILE A 1 108 ? -8.579  -7.575  6.995  1.00 14.41  ? 108 ILE A CG1  1 
ATOM   1713 C  CG2  . ILE A 1 108 ? -7.840  -6.624  9.230  1.00 14.16  ? 108 ILE A CG2  1 
ATOM   1714 C  CD1  . ILE A 1 108 ? -10.033 -7.145  6.910  1.00 15.50  ? 108 ILE A CD1  1 
ATOM   1715 H  H    . ILE A 1 108 ? -8.089  -10.337 7.760  1.00 17.18  ? 108 ILE A H    1 
ATOM   1716 H  HA   . ILE A 1 108 ? -6.232  -8.411  7.787  1.00 15.15  ? 108 ILE A HA   1 
ATOM   1717 H  HB   . ILE A 1 108 ? -8.834  -8.379  8.876  1.00 17.18  ? 108 ILE A HB   1 
ATOM   1718 H  HG12 . ILE A 1 108 ? -8.017  -6.861  6.625  1.00 17.18  ? 108 ILE A HG12 1 
ATOM   1719 H  HG13 . ILE A 1 108 ? -8.455  -8.374  6.439  1.00 17.18  ? 108 ILE A HG13 1 
ATOM   1720 H  HG21 . ILE A 1 108 ? -8.464  -5.928  8.962  1.00 17.83  ? 108 ILE A HG21 1 
ATOM   1721 H  HG22 . ILE A 1 108 ? -7.955  -6.810  10.178 1.00 17.83  ? 108 ILE A HG22 1 
ATOM   1722 H  HG23 . ILE A 1 108 ? -6.930  -6.318  9.069  1.00 17.83  ? 108 ILE A HG23 1 
ATOM   1723 H  HD11 . ILE A 1 108 ? -10.288 -7.039  5.977  1.00 17.93  ? 108 ILE A HD11 1 
ATOM   1724 H  HD12 . ILE A 1 108 ? -10.597 -7.820  7.325  1.00 17.93  ? 108 ILE A HD12 1 
ATOM   1725 H  HD13 . ILE A 1 108 ? -10.150 -6.298  7.375  1.00 17.93  ? 108 ILE A HD13 1 
ATOM   1726 N  N    . PHE A 1 109 ? -6.807  -9.660  10.673 1.00 11.33  ? 109 PHE A N    1 
ATOM   1727 C  CA   . PHE A 1 109 ? -6.399  -9.701  12.064 1.00 11.26  ? 109 PHE A CA   1 
ATOM   1728 C  C    . PHE A 1 109 ? -4.975  -10.228 12.220 1.00 11.68  ? 109 PHE A C    1 
ATOM   1729 O  O    . PHE A 1 109 ? -4.184  -9.599  12.942 1.00 12.02  ? 109 PHE A O    1 
ATOM   1730 C  CB   . PHE A 1 109 ? -7.401  -10.585 12.816 1.00 12.06  ? 109 PHE A CB   1 
ATOM   1731 C  CG   . PHE A 1 109 ? -7.034  -10.797 14.257 1.00 12.01  ? 109 PHE A CG   1 
ATOM   1732 C  CD1  . PHE A 1 109 ? -7.286  -9.821  15.208 1.00 13.30  ? 109 PHE A CD1  1 
ATOM   1733 C  CD2  . PHE A 1 109 ? -6.459  -11.978 14.665 1.00 13.08  ? 109 PHE A CD2  1 
ATOM   1734 C  CE1  . PHE A 1 109 ? -6.935  -10.023 16.529 1.00 15.11  ? 109 PHE A CE1  1 
ATOM   1735 C  CE2  . PHE A 1 109 ? -6.075  -12.165 15.976 1.00 15.05  ? 109 PHE A CE2  1 
ATOM   1736 C  CZ   . PHE A 1 109 ? -6.318  -11.183 16.890 1.00 15.72  ? 109 PHE A CZ   1 
ATOM   1737 H  H    . PHE A 1 109 ? -7.509  -10.183 10.410 1.00 16.04  ? 109 PHE A H    1 
ATOM   1738 H  HA   . PHE A 1 109 ? -6.439  -8.783  12.436 1.00 13.77  ? 109 PHE A HA   1 
ATOM   1739 H  HB2  . PHE A 1 109 ? -8.286  -10.166 12.769 1.00 16.04  ? 109 PHE A HB2  1 
ATOM   1740 H  HB3  . PHE A 1 109 ? -7.453  -11.455 12.367 1.00 16.04  ? 109 PHE A HB3  1 
ATOM   1741 H  HD1  . PHE A 1 109 ? -7.690  -9.008  14.948 1.00 16.03  ? 109 PHE A HD1  1 
ATOM   1742 H  HD2  . PHE A 1 109 ? -6.265  -12.643 14.024 1.00 16.03  ? 109 PHE A HD2  1 
ATOM   1743 H  HE1  . PHE A 1 109 ? -7.093  -9.348  17.171 1.00 16.03  ? 109 PHE A HE1  1 
ATOM   1744 H  HE2  . PHE A 1 109 ? -5.671  -12.975 16.242 1.00 16.03  ? 109 PHE A HE2  1 
ATOM   1745 H  HZ   . PHE A 1 109 ? -6.089  -11.323 17.792 1.00 16.03  ? 109 PHE A HZ   1 
ATOM   1746 N  N    . GLU A 1 110 ? -4.662  -11.343 11.557 1.00 11.94  ? 110 GLU A N    1 
ATOM   1747 C  CA   . GLU A 1 110 ? -3.357  -11.938 11.812 1.00 12.32  ? 110 GLU A CA   1 
ATOM   1748 C  C    . GLU A 1 110 ? -2.455  -11.892 10.579 1.00 12.80  ? 110 GLU A C    1 
ATOM   1749 O  O    . GLU A 1 110 ? -1.323  -11.440 10.673 1.00 13.88  ? 110 GLU A O    1 
ATOM   1750 C  CB   . GLU A 1 110 ? -3.431  -13.364 12.357 1.00 13.65  ? 110 GLU A CB   1 
ATOM   1751 C  CG   . GLU A 1 110 ? -2.071  -13.840 12.837 1.00 14.30  ? 110 GLU A CG   1 
ATOM   1752 C  CD   . GLU A 1 110 ? -1.518  -13.008 13.982 1.00 13.77  ? 110 GLU A CD   1 
ATOM   1753 O  OE1  . GLU A 1 110 ? -2.325  -12.369 14.680 1.00 14.21  ? 110 GLU A OE1  1 
ATOM   1754 O  OE2  . GLU A 1 110 ? -0.254  -12.983 14.185 1.00 14.70  ? 110 GLU A OE2  1 
ATOM   1755 H  H    . GLU A 1 110 ? -5.239  -11.730 10.963 1.00 14.49  ? 110 GLU A H    1 
ATOM   1756 H  HA   . GLU A 1 110 ? -2.923  -11.387 12.500 1.00 15.03  ? 110 GLU A HA   1 
ATOM   1757 H  HB2  . GLU A 1 110 ? -4.070  -13.392 13.100 1.00 16.22  ? 110 GLU A HB2  1 
ATOM   1758 H  HB3  . GLU A 1 110 ? -3.754  -13.960 11.650 1.00 16.22  ? 110 GLU A HB3  1 
ATOM   1759 H  HG2  . GLU A 1 110 ? -2.144  -14.771 13.134 1.00 17.02  ? 110 GLU A HG2  1 
ATOM   1760 H  HG3  . GLU A 1 110 ? -1.435  -13.814 12.092 1.00 17.02  ? 110 GLU A HG3  1 
ATOM   1761 N  N    . GLU A 1 111 ? -2.886  -12.395 9.421  1.00 13.74  ? 111 GLU A N    1 
ATOM   1762 C  CA   . GLU A 1 111 ? -1.959  -12.484 8.299  1.00 14.74  ? 111 GLU A CA   1 
ATOM   1763 C  C    . GLU A 1 111 ? -1.442  -11.105 7.904  1.00 14.47  ? 111 GLU A C    1 
ATOM   1764 O  O    . GLU A 1 111 ? -0.265  -10.980 7.573  1.00 16.67  ? 111 GLU A O    1 
ATOM   1765 C  CB   . GLU A 1 111 ? -2.590  -13.302 7.175  1.00 16.26  ? 111 GLU A CB   1 
ATOM   1766 C  CG   . GLU A 1 111 ? -2.358  -14.803 7.430  1.00 18.97  ? 111 GLU A CG   1 
ATOM   1767 C  CD   . GLU A 1 111 ? -2.977  -15.363 8.717  1.00 18.84  ? 111 GLU A CD   1 
ATOM   1768 O  OE1  . GLU A 1 111 ? -4.216  -15.270 8.870  1.00 17.97  ? 111 GLU A OE1  1 
ATOM   1769 O  OE2  . GLU A 1 111 ? -2.207  -15.855 9.615  1.00 20.67  ? 111 GLU A OE2  1 
ATOM   1770 H  H    . GLU A 1 111 ? -3.750  -12.675 9.325  1.00 18.61  ? 111 GLU A H    1 
ATOM   1771 H  HA   . GLU A 1 111 ? -1.180  -12.995 8.620  1.00 20.23  ? 111 GLU A HA   1 
ATOM   1772 H  HB2  . GLU A 1 111 ? -3.551  -13.117 7.135  1.00 18.61  ? 111 GLU A HB2  1 
ATOM   1773 H  HB3  . GLU A 1 111 ? -2.186  -13.046 6.320  1.00 18.61  ? 111 GLU A HB3  1 
ATOM   1774 H  HG2  . GLU A 1 111 ? -2.722  -15.309 6.672  1.00 20.23  ? 111 GLU A HG2  1 
ATOM   1775 H  HG3  . GLU A 1 111 ? -1.392  -14.972 7.455  1.00 20.23  ? 111 GLU A HG3  1 
ATOM   1776 N  N    . GLN A 1 112 ? -2.307  -10.090 7.880  1.00 13.78  ? 112 GLN A N    1 
ATOM   1777 C  CA   . GLN A 1 112 ? -1.901  -8.736  7.575  1.00 15.30  ? 112 GLN A CA   1 
ATOM   1778 C  C    . GLN A 1 112 ? -1.410  -8.003  8.812  1.00 15.07  ? 112 GLN A C    1 
ATOM   1779 O  O    . GLN A 1 112 ? -0.299  -7.479  8.830  1.00 17.64  ? 112 GLN A O    1 
ATOM   1780 C  CB   . GLN A 1 112 ? -3.041  -7.991  6.893  1.00 16.66  ? 112 GLN A CB   1 
ATOM   1781 C  CG   . GLN A 1 112 ? -3.376  -8.589  5.538  1.00 17.56  ? 112 GLN A CG   1 
ATOM   1782 C  CD   . GLN A 1 112 ? -4.497  -7.900  4.799  1.00 20.77  ? 112 GLN A CD   1 
ATOM   1783 O  OE1  . GLN A 1 112 ? -5.583  -7.684  5.279  1.00 21.40  ? 112 GLN A OE1  1 
ATOM   1784 N  NE2  . GLN A 1 112 ? -4.266  -7.593  3.544  1.00 28.62  ? 112 GLN A NE2  1 
ATOM   1785 H  H    . GLN A 1 112 ? -3.189  -10.253 8.057  1.00 20.07  ? 112 GLN A H    1 
ATOM   1786 H  HA   . GLN A 1 112 ? -1.151  -8.785  6.938  1.00 18.57  ? 112 GLN A HA   1 
ATOM   1787 H  HB2  . GLN A 1 112 ? -3.833  -8.026  7.469  1.00 20.07  ? 112 GLN A HB2  1 
ATOM   1788 H  HB3  . GLN A 1 112 ? -2.785  -7.052  6.780  1.00 20.07  ? 112 GLN A HB3  1 
ATOM   1789 H  HG2  . GLN A 1 112 ? -2.570  -8.566  4.979  1.00 25.34  ? 112 GLN A HG2  1 
ATOM   1790 H  HG3  . GLN A 1 112 ? -3.618  -9.531  5.662  1.00 25.34  ? 112 GLN A HG3  1 
ATOM   1791 H  HE21 . GLN A 1 112 ? -3.714  -8.087  3.061  1.00 25.34  ? 112 GLN A HE21 1 
ATOM   1792 H  HE22 . GLN A 1 112 ? -4.665  -6.893  3.179  1.00 25.34  ? 112 GLN A HE22 1 
ATOM   1793 N  N    . SER A 1 113 ? -2.240  -7.945  9.853  1.00 13.00  ? 113 SER A N    1 
ATOM   1794 C  CA   . SER A 1 113 ? -1.926  -7.075  10.978 1.00 12.75  ? 113 SER A CA   1 
ATOM   1795 C  C    . SER A 1 113 ? -0.952  -7.675  11.978 1.00 12.86  ? 113 SER A C    1 
ATOM   1796 O  O    . SER A 1 113 ? -0.380  -6.942  12.760 1.00 13.32  ? 113 SER A O    1 
ATOM   1797 C  CB   . SER A 1 113 ? -3.180  -6.670  11.709 1.00 12.61  ? 113 SER A CB   1 
ATOM   1798 O  OG   . SER A 1 113 ? -4.034  -5.951  10.855 1.00 13.45  ? 113 SER A OG   1 
ATOM   1799 H  H    . SER A 1 113 ? -3.005  -8.445  9.867  1.00 16.75  ? 113 SER A H    1 
ATOM   1800 H  HA   . SER A 1 113 ? -1.510  -6.249  10.612 1.00 16.64  ? 113 SER A HA   1 
ATOM   1801 H  HB2  . SER A 1 113 ? -3.642  -7.471  12.037 1.00 25.98  ? 113 SER A HB2  1 
ATOM   1802 H  HB3  . SER A 1 113 ? -2.943  -6.113  12.483 1.00 25.98  ? 113 SER A HB3  1 
ATOM   1803 H  HG   . SER A 1 113 ? -4.501  -6.501  10.414 1.00 25.97  ? 113 SER A HG   1 
ATOM   1804 N  N    . ARG A 1 114 ? -0.845  -8.991  12.008 1.00 12.65  ? 114 ARG A N    1 
ATOM   1805 C  CA   . ARG A 1 114 ? 0.086   -9.666  12.893 1.00 13.58  ? 114 ARG A CA   1 
ATOM   1806 C  C    . ARG A 1 114 ? -0.212  -9.381  14.362 1.00 12.28  ? 114 ARG A C    1 
ATOM   1807 O  O    . ARG A 1 114 ? 0.700   -9.333  15.173 1.00 12.79  ? 114 ARG A O    1 
ATOM   1808 C  CB   . ARG A 1 114 ? 1.539   -9.288  12.540 1.00 15.16  ? 114 ARG A CB   1 
ATOM   1809 C  CG   . ARG A 1 114 ? 1.865   -9.468  11.057 1.00 18.81  ? 114 ARG A CG   1 
ATOM   1810 C  CD   . ARG A 1 114 ? 3.252   -9.998  10.792 1.00 24.22  ? 114 ARG A CD   1 
ATOM   1811 N  NE   . ARG A 1 114 ? 3.361   -11.405 11.177 1.00 27.23  ? 114 ARG A NE   1 
ATOM   1812 C  CZ   . ARG A 1 114 ? 4.508   -12.072 11.297 1.00 29.99  ? 114 ARG A CZ   1 
ATOM   1813 N  NH1  . ARG A 1 114 ? 5.660   -11.442 11.149 1.00 32.20  ? 114 ARG A NH1  1 
ATOM   1814 N  NH2  . ARG A 1 114 ? 4.497   -13.356 11.623 1.00 35.32  ? 114 ARG A NH2  1 
ATOM   1815 H  H    . ARG A 1 114 ? -1.374  -9.497  11.462 1.00 15.38  ? 114 ARG A H    1 
ATOM   1816 H  HA   . ARG A 1 114 ? -0.018  -10.634 12.749 1.00 16.48  ? 114 ARG A HA   1 
ATOM   1817 H  HB2  . ARG A 1 114 ? 1.695   -8.354  12.790 1.00 18.29  ? 114 ARG A HB2  1 
ATOM   1818 H  HB3  . ARG A 1 114 ? 2.146   -9.846  13.067 1.00 18.29  ? 114 ARG A HB3  1 
ATOM   1819 H  HG2  . ARG A 1 114 ? 1.213   -10.085 10.660 1.00 26.67  ? 114 ARG A HG2  1 
ATOM   1820 H  HG3  . ARG A 1 114 ? 1.768   -8.604  10.604 1.00 26.67  ? 114 ARG A HG3  1 
ATOM   1821 H  HD2  . ARG A 1 114 ? 3.460   -9.904  9.838  1.00 27.41  ? 114 ARG A HD2  1 
ATOM   1822 H  HD3  . ARG A 1 114 ? 3.904   -9.469  11.300 1.00 27.41  ? 114 ARG A HD3  1 
ATOM   1823 H  HE   . ARG A 1 114 ? 2.622   -11.840 11.339 1.00 26.68  ? 114 ARG A HE   1 
ATOM   1824 H  HH11 . ARG A 1 114 ? 5.811   -10.967 10.423 1.00 27.35  ? 114 ARG A HH11 1 
ATOM   1825 H  HH12 . ARG A 1 114 ? 6.277   -11.504 11.774 1.00 27.35  ? 114 ARG A HH12 1 
ATOM   1826 H  HH21 . ARG A 1 114 ? 3.758   -13.728 11.922 1.00 26.69  ? 114 ARG A HH21 1 
ATOM   1827 H  HH22 . ARG A 1 114 ? 5.231   -13.834 11.540 1.00 26.69  ? 114 ARG A HH22 1 
ATOM   1828 N  N    . HIS A 1 115 ? -1.488  -9.290  14.738 1.00 11.69  ? 115 HIS A N    1 
ATOM   1829 C  CA   . HIS A 1 115 ? -1.871  -8.922  16.095 1.00 11.56  ? 115 HIS A CA   1 
ATOM   1830 C  C    . HIS A 1 115 ? -1.195  -9.815  17.134 1.00 11.32  ? 115 HIS A C    1 
ATOM   1831 O  O    . HIS A 1 115 ? -0.623  -9.343  18.107 1.00 11.73  ? 115 HIS A O    1 
ATOM   1832 C  CB   . HIS A 1 115 ? -3.394  -8.990  16.212 1.00 10.93  ? 115 HIS A CB   1 
ATOM   1833 C  CG   . HIS A 1 115 ? -3.964  -8.492  17.496 1.00 10.40  ? 115 HIS A CG   1 
ATOM   1834 N  ND1  . HIS A 1 115 ? -4.900  -7.483  17.496 1.00 11.94  ? 115 HIS A ND1  1 
ATOM   1835 C  CD2  . HIS A 1 115 ? -3.896  -8.882  18.781 1.00 10.17  ? 115 HIS A CD2  1 
ATOM   1836 C  CE1  . HIS A 1 115 ? -5.327  -7.300  18.740 1.00 11.59  ? 115 HIS A CE1  1 
ATOM   1837 N  NE2  . HIS A 1 115 ? -4.719  -8.116  19.556 1.00 9.65   ? 115 HIS A NE2  1 
ATOM   1838 H  H    . HIS A 1 115 ? -2.147  -9.471  14.130 1.00 13.31  ? 115 HIS A H    1 
ATOM   1839 H  HA   . HIS A 1 115 ? -1.580  -7.990  16.252 1.00 13.76  ? 115 HIS A HA   1 
ATOM   1840 H  HB2  . HIS A 1 115 ? -3.785  -8.474  15.474 1.00 13.31  ? 115 HIS A HB2  1 
ATOM   1841 H  HB3  . HIS A 1 115 ? -3.673  -9.924  16.086 1.00 13.31  ? 115 HIS A HB3  1 
ATOM   1842 H  HD1  . HIS A 1 115 ? -5.183  -7.047  16.786 1.00 13.31  ? 115 HIS A HD1  1 
ATOM   1843 H  HD2  . HIS A 1 115 ? -3.346  -9.565  19.110 1.00 13.31  ? 115 HIS A HD2  1 
ATOM   1844 H  HE1  . HIS A 1 115 ? -5.935  -6.628  18.991 1.00 13.31  ? 115 HIS A HE1  1 
ATOM   1845 N  N    . ILE A 1 116 ? -1.325  -11.129 16.947 1.00 11.53  ? 116 ILE A N    1 
ATOM   1846 C  CA   . ILE A 1 116 ? -0.794  -12.088 17.926 1.00 12.43  ? 116 ILE A CA   1 
ATOM   1847 C  C    . ILE A 1 116 ? 0.739   -12.088 17.919 1.00 12.64  ? 116 ILE A C    1 
ATOM   1848 O  O    . ILE A 1 116 ? 1.382   -12.103 18.958 1.00 13.34  ? 116 ILE A O    1 
ATOM   1849 C  CB   . ILE A 1 116 ? -1.383  -13.489 17.676 1.00 13.11  ? 116 ILE A CB   1 
ATOM   1850 C  CG1  . ILE A 1 116 ? -2.913  -13.480 17.809 1.00 14.02  ? 116 ILE A CG1  1 
ATOM   1851 C  CG2  . ILE A 1 116 ? -0.740  -14.491 18.609 1.00 14.75  ? 116 ILE A CG2  1 
ATOM   1852 C  CD1  . ILE A 1 116 ? -3.586  -14.735 17.295 1.00 15.42  ? 116 ILE A CD1  1 
ATOM   1853 H  H    . ILE A 1 116 ? -1.749  -11.442 16.201 1.00 16.77  ? 116 ILE A H    1 
ATOM   1854 H  HA   . ILE A 1 116 ? -1.087  -11.801 18.810 1.00 14.83  ? 116 ILE A HA   1 
ATOM   1855 H  HB   . ILE A 1 116 ? -1.162  -13.749 16.748 1.00 16.43  ? 116 ILE A HB   1 
ATOM   1856 H  HG12 . ILE A 1 116 ? -3.143  -13.364 18.754 1.00 16.77  ? 116 ILE A HG12 1 
ATOM   1857 H  HG13 . ILE A 1 116 ? -3.270  -12.710 17.318 1.00 16.77  ? 116 ILE A HG13 1 
ATOM   1858 H  HG21 . ILE A 1 116 ? -1.307  -15.277 18.689 1.00 16.13  ? 116 ILE A HG21 1 
ATOM   1859 H  HG22 . ILE A 1 116 ? 0.127   -14.757 18.255 1.00 16.13  ? 116 ILE A HG22 1 
ATOM   1860 H  HG23 . ILE A 1 116 ? -0.621  -14.091 19.487 1.00 16.13  ? 116 ILE A HG23 1 
ATOM   1861 H  HD11 . ILE A 1 116 ? -4.552  -14.632 17.349 1.00 16.02  ? 116 ILE A HD11 1 
ATOM   1862 H  HD12 . ILE A 1 116 ? -3.329  -14.886 16.369 1.00 16.02  ? 116 ILE A HD12 1 
ATOM   1863 H  HD13 . ILE A 1 116 ? -3.313  -15.495 17.834 1.00 16.02  ? 116 ILE A HD13 1 
ATOM   1864 N  N    . HIS A 1 117 ? 1.296   -12.106 16.718 1.00 12.86  ? 117 HIS A N    1 
ATOM   1865 C  CA   . HIS A 1 117 ? 2.740   -12.040 16.568 1.00 14.13  ? 117 HIS A CA   1 
ATOM   1866 C  C    . HIS A 1 117 ? 3.329   -10.833 17.298 1.00 13.78  ? 117 HIS A C    1 
ATOM   1867 O  O    . HIS A 1 117 ? 4.362   -10.939 17.972 1.00 15.59  ? 117 HIS A O    1 
ATOM   1868 C  CB   . HIS A 1 117 ? 3.085   -11.996 15.086 1.00 15.64  ? 117 HIS A CB   1 
ATOM   1869 C  CG   . HIS A 1 117 ? 4.517   -11.725 14.831 1.00 19.16  ? 117 HIS A CG   1 
ATOM   1870 N  ND1  . HIS A 1 117 ? 5.466   -12.724 14.855 1.00 22.22  ? 117 HIS A ND1  1 
ATOM   1871 C  CD2  . HIS A 1 117 ? 5.141   -10.587 14.506 1.00 21.75  ? 117 HIS A CD2  1 
ATOM   1872 C  CE1  . HIS A 1 117 ? 6.645   -12.188 14.573 1.00 24.44  ? 117 HIS A CE1  1 
ATOM   1873 N  NE2  . HIS A 1 117 ? 6.476   -10.886 14.349 1.00 24.42  ? 117 HIS A NE2  1 
ATOM   1874 H  H    . HIS A 1 117 ? 0.773   -12.170 15.971 1.00 18.29  ? 117 HIS A H    1 
ATOM   1875 H  HA   . HIS A 1 117 ? 3.126   -12.861 16.962 1.00 16.80  ? 117 HIS A HA   1 
ATOM   1876 H  HB2  . HIS A 1 117 ? 2.845   -12.856 14.680 1.00 18.29  ? 117 HIS A HB2  1 
ATOM   1877 H  HB3  . HIS A 1 117 ? 2.546   -11.296 14.659 1.00 18.29  ? 117 HIS A HB3  1 
ATOM   1878 H  HD2  . HIS A 1 117 ? 4.752   -9.740  14.407 1.00 25.06  ? 117 HIS A HD2  1 
ATOM   1879 H  HE1  . HIS A 1 117 ? 7.462   -12.655 14.532 1.00 25.06  ? 117 HIS A HE1  1 
ATOM   1880 H  HE2  . HIS A 1 117 ? 7.110   -10.315 14.147 1.00 25.06  ? 117 HIS A HE2  1 
ATOM   1881 N  N    . ILE A 1 118 ? 2.693   -9.674  17.140 1.00 12.61  ? 118 ILE A N    1 
ATOM   1882 C  CA   . ILE A 1 118 ? 3.111   -8.461  17.821 1.00 13.15  ? 118 ILE A CA   1 
ATOM   1883 C  C    . ILE A 1 118 ? 2.909   -8.615  19.322 1.00 12.00  ? 118 ILE A C    1 
ATOM   1884 O  O    . ILE A 1 118 ? 3.825   -8.349  20.102 1.00 12.40  ? 118 ILE A O    1 
ATOM   1885 C  CB   . ILE A 1 118 ? 2.376   -7.240  17.250 1.00 13.95  ? 118 ILE A CB   1 
ATOM   1886 C  CG1  . ILE A 1 118 ? 2.866   -6.940  15.828 1.00 16.54  ? 118 ILE A CG1  1 
ATOM   1887 C  CG2  . ILE A 1 118 ? 2.555   -6.039  18.159 1.00 15.91  ? 118 ILE A CG2  1 
ATOM   1888 C  CD1  . ILE A 1 118 ? 2.025   -5.955  15.084 1.00 17.59  ? 118 ILE A CD1  1 
ATOM   1889 H  H    . ILE A 1 118 ? 1.971   -9.635  16.580 1.00 19.16  ? 118 ILE A H    1 
ATOM   1890 H  HA   . ILE A 1 118 ? 4.062   -8.338  17.657 1.00 24.73  ? 118 ILE A HA   1 
ATOM   1891 H  HB   . ILE A 1 118 ? 1.411   -7.455  17.204 1.00 19.17  ? 118 ILE A HB   1 
ATOM   1892 H  HG12 . ILE A 1 118 ? 3.782   -6.593  15.879 1.00 19.86  ? 118 ILE A HG12 1 
ATOM   1893 H  HG13 . ILE A 1 118 ? 2.891   -7.778  15.320 1.00 19.86  ? 118 ILE A HG13 1 
ATOM   1894 H  HG21 . ILE A 1 118 ? 2.343   -5.224  17.672 1.00 19.17  ? 118 ILE A HG21 1 
ATOM   1895 H  HG22 . ILE A 1 118 ? 1.960   -6.116  18.925 1.00 19.17  ? 118 ILE A HG22 1 
ATOM   1896 H  HG23 . ILE A 1 118 ? 3.476   -5.997  18.468 1.00 19.17  ? 118 ILE A HG23 1 
ATOM   1897 H  HD11 . ILE A 1 118 ? 2.210   -6.024  14.131 1.00 19.18  ? 118 ILE A HD11 1 
ATOM   1898 H  HD12 . ILE A 1 118 ? 1.084   -6.144  15.244 1.00 19.18  ? 118 ILE A HD12 1 
ATOM   1899 H  HD13 . ILE A 1 118 ? 2.230   -5.054  15.388 1.00 19.18  ? 118 ILE A HD13 1 
ATOM   1900 N  N    . GLY A 1 119 ? 1.705   -9.016  19.737 1.00 11.63  ? 119 GLY A N    1 
ATOM   1901 C  CA   . GLY A 1 119 ? 1.417   -9.091  21.161 1.00 11.51  ? 119 GLY A CA   1 
ATOM   1902 C  C    . GLY A 1 119 ? 2.360   -10.025 21.923 1.00 11.15  ? 119 GLY A C    1 
ATOM   1903 O  O    . GLY A 1 119 ? 2.765   -9.721  23.032 1.00 11.66  ? 119 GLY A O    1 
ATOM   1904 H  H    . GLY A 1 119 ? 1.056   -9.241  19.133 1.00 14.13  ? 119 GLY A H    1 
ATOM   1905 H  HA2  . GLY A 1 119 ? 1.481   -8.182  21.547 1.00 13.81  ? 119 GLY A HA2  1 
ATOM   1906 H  HA3  . GLY A 1 119 ? 0.488   -9.403  21.279 1.00 13.81  ? 119 GLY A HA3  1 
ATOM   1907 N  N    . LEU A 1 120 ? 2.746   -11.143 21.285 1.00 11.76  ? 120 LEU A N    1 
ATOM   1908 C  CA   . LEU A 1 120 ? 3.642   -12.096 21.939 1.00 12.30  ? 120 LEU A CA   1 
ATOM   1909 C  C    . LEU A 1 120 ? 4.963   -11.437 22.332 1.00 12.41  ? 120 LEU A C    1 
ATOM   1910 O  O    . LEU A 1 120 ? 5.631   -11.916 23.255 1.00 13.56  ? 120 LEU A O    1 
ATOM   1911 C  CB   . LEU A 1 120 ? 3.913   -13.265 20.992 1.00 13.74  ? 120 LEU A CB   1 
ATOM   1912 C  CG   . LEU A 1 120 ? 2.836   -14.345 21.007 1.00 14.77  ? 120 LEU A CG   1 
ATOM   1913 C  CD1  . LEU A 1 120 ? 2.950   -15.213 19.786 1.00 16.51  ? 120 LEU A CD1  1 
ATOM   1914 C  CD2  . LEU A 1 120 ? 2.906   -15.206 22.267 1.00 16.18  ? 120 LEU A CD2  1 
ATOM   1915 H  H    . LEU A 1 120 ? 2.444   -11.319 20.441 1.00 18.06  ? 120 LEU A H    1 
ATOM   1916 H  HA   . LEU A 1 120 ? 3.200   -12.428 22.754 1.00 17.99  ? 120 LEU A HA   1 
ATOM   1917 H  HB2  . LEU A 1 120 ? 3.999   -12.917 20.081 1.00 18.06  ? 120 LEU A HB2  1 
ATOM   1918 H  HB3  . LEU A 1 120 ? 4.768   -13.673 21.236 1.00 18.06  ? 120 LEU A HB3  1 
ATOM   1919 H  HG   . LEU A 1 120 ? 1.953   -13.900 20.986 1.00 17.35  ? 120 LEU A HG   1 
ATOM   1920 H  HD11 . LEU A 1 120 ? 2.279   -15.916 19.823 1.00 18.04  ? 120 LEU A HD11 1 
ATOM   1921 H  HD12 . LEU A 1 120 ? 2.809   -14.673 18.989 1.00 18.04  ? 120 LEU A HD12 1 
ATOM   1922 H  HD13 . LEU A 1 120 ? 3.837   -15.613 19.754 1.00 18.04  ? 120 LEU A HD13 1 
ATOM   1923 H  HD21 . LEU A 1 120 ? 2.260   -15.931 22.201 1.00 17.99  ? 120 LEU A HD21 1 
ATOM   1924 H  HD22 . LEU A 1 120 ? 3.800   -15.577 22.357 1.00 17.99  ? 120 LEU A HD22 1 
ATOM   1925 H  HD23 . LEU A 1 120 ? 2.701   -14.660 23.046 1.00 17.99  ? 120 LEU A HD23 1 
ATOM   1926 N  N    . GLN A 1 121 ? 5.378   -10.386 21.607 1.00 12.51  ? 121 GLN A N    1 
ATOM   1927 C  CA   . GLN A 1 121 ? 6.640   -9.734  21.896 1.00 13.74  ? 121 GLN A CA   1 
ATOM   1928 C  C    . GLN A 1 121 ? 6.612   -8.954  23.203 1.00 13.39  ? 121 GLN A C    1 
ATOM   1929 O  O    . GLN A 1 121 ? 7.654   -8.487  23.634 1.00 16.69  ? 121 GLN A O    1 
ATOM   1930 C  CB   . GLN A 1 121 ? 7.035   -8.840  20.721 1.00 15.05  ? 121 GLN A CB   1 
ATOM   1931 C  CG   . GLN A 1 121 ? 7.223   -9.600  19.408 1.00 18.11  ? 121 GLN A CG   1 
ATOM   1932 C  CD   . GLN A 1 121 ? 7.450   -8.678  18.232 1.00 22.95  ? 121 GLN A CD   1 
ATOM   1933 O  OE1  . GLN A 1 121 ? 8.404   -7.911  18.188 1.00 29.17  ? 121 GLN A OE1  1 
ATOM   1934 N  NE2  . GLN A 1 121 ? 6.581   -8.773  17.245 1.00 29.75  ? 121 GLN A NE2  1 
ATOM   1935 H  H    . GLN A 1 121 ? 4.868   -10.077 20.915 1.00 24.73  ? 121 GLN A H    1 
ATOM   1936 H  HA   . GLN A 1 121 ? 7.324   -10.438 21.982 1.00 16.43  ? 121 GLN A HA   1 
ATOM   1937 H  HB2  . GLN A 1 121 ? 6.343   -8.158  20.601 1.00 18.39  ? 121 GLN A HB2  1 
ATOM   1938 H  HB3  . GLN A 1 121 ? 7.871   -8.381  20.947 1.00 18.39  ? 121 GLN A HB3  1 
ATOM   1939 H  HG2  . GLN A 1 121 ? 7.993   -10.202 19.494 1.00 24.73  ? 121 GLN A HG2  1 
ATOM   1940 H  HG3  . GLN A 1 121 ? 6.432   -10.150 19.237 1.00 24.73  ? 121 GLN A HG3  1 
ATOM   1941 H  HE21 . GLN A 1 121 ? 6.175   -9.542  17.084 1.00 24.73  ? 121 GLN A HE21 1 
ATOM   1942 H  HE22 . GLN A 1 121 ? 6.407   -8.069  16.740 1.00 24.73  ? 121 GLN A HE22 1 
ATOM   1943 N  N    . TYR A 1 122 ? 5.424   -8.752  23.773 1.00 11.64  ? 122 TYR A N    1 
ATOM   1944 C  CA   . TYR A 1 122 ? 5.232   -7.970  24.977 1.00 11.84  ? 122 TYR A CA   1 
ATOM   1945 C  C    . TYR A 1 122 ? 4.813   -8.845  26.158 1.00 11.65  ? 122 TYR A C    1 
ATOM   1946 O  O    . TYR A 1 122 ? 4.368   -8.335  27.180 1.00 11.94  ? 122 TYR A O    1 
ATOM   1947 C  CB   . TYR A 1 122 ? 4.240   -6.830  24.732 1.00 11.94  ? 122 TYR A CB   1 
ATOM   1948 C  CG   . TYR A 1 122 ? 4.757   -5.855  23.715 1.00 12.37  ? 122 TYR A CG   1 
ATOM   1949 C  CD1  . TYR A 1 122 ? 4.538   -6.055  22.358 1.00 12.55  ? 122 TYR A CD1  1 
ATOM   1950 C  CD2  . TYR A 1 122 ? 5.483   -4.742  24.102 1.00 12.65  ? 122 TYR A CD2  1 
ATOM   1951 C  CE1  . TYR A 1 122 ? 5.016   -5.177  21.405 1.00 13.12  ? 122 TYR A CE1  1 
ATOM   1952 C  CE2  . TYR A 1 122 ? 5.968   -3.861  23.149 1.00 13.48  ? 122 TYR A CE2  1 
ATOM   1953 C  CZ   . TYR A 1 122 ? 5.718   -4.062  21.807 1.00 13.80  ? 122 TYR A CZ   1 
ATOM   1954 O  OH   . TYR A 1 122 ? 6.143   -3.135  20.877 1.00 16.11  ? 122 TYR A OH   1 
ATOM   1955 H  H    . TYR A 1 122 ? 4.683   -9.108  23.376 1.00 17.70  ? 122 TYR A H    1 
ATOM   1956 H  HA   . TYR A 1 122 ? 6.102   -7.559  25.212 1.00 14.49  ? 122 TYR A HA   1 
ATOM   1957 H  HB2  . TYR A 1 122 ? 3.392   -7.208  24.420 1.00 14.27  ? 122 TYR A HB2  1 
ATOM   1958 H  HB3  . TYR A 1 122 ? 4.076   -6.361  25.577 1.00 14.27  ? 122 TYR A HB3  1 
ATOM   1959 H  HD1  . TYR A 1 122 ? 4.048   -6.809  22.080 1.00 16.21  ? 122 TYR A HD1  1 
ATOM   1960 H  HD2  . TYR A 1 122 ? 5.654   -4.586  25.016 1.00 16.21  ? 122 TYR A HD2  1 
ATOM   1961 H  HE1  . TYR A 1 122 ? 4.826   -5.316  20.491 1.00 16.21  ? 122 TYR A HE1  1 
ATOM   1962 H  HE2  . TYR A 1 122 ? 6.434   -3.089  23.422 1.00 16.21  ? 122 TYR A HE2  1 
ATOM   1963 H  HH   . TYR A 1 122 ? 6.358   -3.388  20.083 1.00 16.21  ? 122 TYR A HH   1 
ATOM   1964 N  N    . LEU A 1 123 ? 5.007   -10.158 26.019 1.00 11.80  ? 123 LEU A N    1 
ATOM   1965 C  CA   . LEU A 1 123 ? 4.814   -11.119 27.086 1.00 11.76  ? 123 LEU A CA   1 
ATOM   1966 C  C    . LEU A 1 123 ? 6.202   -11.553 27.513 1.00 12.93  ? 123 LEU A C    1 
ATOM   1967 O  O    . LEU A 1 123 ? 7.087   -11.719 26.675 1.00 15.27  ? 123 LEU A O    1 
ATOM   1968 C  CB   . LEU A 1 123 ? 4.004   -12.328 26.584 1.00 12.57  ? 123 LEU A CB   1 
ATOM   1969 C  CG   . LEU A 1 123 ? 2.477   -12.140 26.574 1.00 16.70  ? 123 LEU A CG   1 
ATOM   1970 C  CD1  . LEU A 1 123 ? 1.944   -10.812 26.163 1.00 15.73  ? 123 LEU A CD1  1 
ATOM   1971 C  CD2  . LEU A 1 123 ? 1.857   -13.283 25.791 1.00 15.63  ? 123 LEU A CD2  1 
ATOM   1972 H  H    . LEU A 1 123 ? 5.279   -10.474 25.206 1.00 17.70  ? 123 LEU A H    1 
ATOM   1973 H  HA   . LEU A 1 123 ? 4.352   -10.685 27.837 1.00 14.45  ? 123 LEU A HA   1 
ATOM   1974 H  HB2  . LEU A 1 123 ? 4.297   -12.540 25.675 1.00 17.70  ? 123 LEU A HB2  1 
ATOM   1975 H  HB3  . LEU A 1 123 ? 4.217   -13.098 27.149 1.00 17.70  ? 123 LEU A HB3  1 
ATOM   1976 H  HG   . LEU A 1 123 ? 2.186   -12.265 27.511 1.00 14.45  ? 123 LEU A HG   1 
ATOM   1977 H  HD11 . LEU A 1 123 ? 0.986   -10.880 26.004 1.00 17.93  ? 123 LEU A HD11 1 
ATOM   1978 H  HD12 . LEU A 1 123 ? 2.109   -10.163 26.868 1.00 17.93  ? 123 LEU A HD12 1 
ATOM   1979 H  HD13 . LEU A 1 123 ? 2.387   -10.523 25.348 1.00 17.93  ? 123 LEU A HD13 1 
ATOM   1980 H  HD21 . LEU A 1 123 ? 0.887   -13.236 25.858 1.00 17.94  ? 123 LEU A HD21 1 
ATOM   1981 H  HD22 . LEU A 1 123 ? 2.120   -13.217 24.856 1.00 17.94  ? 123 LEU A HD22 1 
ATOM   1982 H  HD23 . LEU A 1 123 ? 2.165   -14.131 26.155 1.00 17.94  ? 123 LEU A HD23 1 
ATOM   1983 N  N    . PRO A 1 124 ? 6.456   -11.772 28.812 1.00 13.56  ? 124 PRO A N    1 
ATOM   1984 C  CA   . PRO A 1 124 ? 5.468   -11.786 29.890 1.00 14.19  ? 124 PRO A CA   1 
ATOM   1985 C  C    . PRO A 1 124 ? 5.171   -10.444 30.561 1.00 12.96  ? 124 PRO A C    1 
ATOM   1986 O  O    . PRO A 1 124 ? 4.450   -10.424 31.563 1.00 14.29  ? 124 PRO A O    1 
ATOM   1987 C  CB   . PRO A 1 124 ? 6.127   -12.729 30.907 1.00 18.50  ? 124 PRO A CB   1 
ATOM   1988 C  CG   . PRO A 1 124 ? 7.586   -12.385 30.769 1.00 18.85  ? 124 PRO A CG   1 
ATOM   1989 C  CD   . PRO A 1 124 ? 7.783   -12.234 29.279 1.00 16.51  ? 124 PRO A CD   1 
ATOM   1990 H  HA   . PRO A 1 124 ? 4.629   -12.195 29.562 1.00 14.45  ? 124 PRO A HA   1 
ATOM   1991 H  HB2  . PRO A 1 124 ? 5.807   -12.556 31.818 1.00 19.82  ? 124 PRO A HB2  1 
ATOM   1992 H  HB3  . PRO A 1 124 ? 5.960   -13.667 30.682 1.00 19.82  ? 124 PRO A HB3  1 
ATOM   1993 H  HG2  . PRO A 1 124 ? 7.796   -11.551 31.235 1.00 20.59  ? 124 PRO A HG2  1 
ATOM   1994 H  HG3  . PRO A 1 124 ? 8.150   -13.101 31.125 1.00 20.59  ? 124 PRO A HG3  1 
ATOM   1995 H  HD2  . PRO A 1 124 ? 8.475   -11.577 29.079 1.00 19.63  ? 124 PRO A HD2  1 
ATOM   1996 H  HD3  . PRO A 1 124 ? 8.024   -13.085 28.867 1.00 19.63  ? 124 PRO A HD3  1 
ATOM   1997 N  N    . ALA A 1 125 ? 5.665   -9.333  30.034 1.00 11.78  ? 125 ALA A N    1 
ATOM   1998 C  CA   . ALA A 1 125 ? 5.430   -8.065  30.719 1.00 11.64  ? 125 ALA A CA   1 
ATOM   1999 C  C    . ALA A 1 125 ? 3.938   -7.777  30.897 1.00 11.53  ? 125 ALA A C    1 
ATOM   2000 O  O    . ALA A 1 125 ? 3.532   -7.313  31.960 1.00 12.10  ? 125 ALA A O    1 
ATOM   2001 C  CB   . ALA A 1 125 ? 6.052   -6.917  29.972 1.00 12.77  ? 125 ALA A CB   1 
ATOM   2002 H  H    . ALA A 1 125 ? 6.145   -9.348  29.257 1.00 14.73  ? 125 ALA A H    1 
ATOM   2003 H  HA   . ALA A 1 125 ? 5.843   -8.116  31.613 1.00 14.34  ? 125 ALA A HA   1 
ATOM   2004 H  HB1  . ALA A 1 125 ? 5.850   -6.083  30.428 1.00 15.71  ? 125 ALA A HB1  1 
ATOM   2005 H  HB2  . ALA A 1 125 ? 7.015   -7.039  29.933 1.00 15.71  ? 125 ALA A HB2  1 
ATOM   2006 H  HB3  . ALA A 1 125 ? 5.694   -6.886  29.068 1.00 15.71  ? 125 ALA A HB3  1 
ATOM   2007 N  N    . VAL A 1 126 ? 3.141   -8.002  29.846 1.00 11.01  ? 126 VAL A N    1 
ATOM   2008 C  CA   . VAL A 1 126 ? 1.770   -7.512  29.843 1.00 10.78  ? 126 VAL A CA   1 
ATOM   2009 C  C    . VAL A 1 126 ? 0.802   -8.685  29.991 1.00 10.92  ? 126 VAL A C    1 
ATOM   2010 O  O    . VAL A 1 126 ? 0.797   -9.619  29.181 1.00 11.83  ? 126 VAL A O    1 
ATOM   2011 C  CB   . VAL A 1 126 ? 1.489   -6.752  28.545 1.00 11.29  ? 126 VAL A CB   1 
ATOM   2012 C  CG1  . VAL A 1 126 ? 0.058   -6.233  28.482 1.00 11.86  ? 126 VAL A CG1  1 
ATOM   2013 C  CG2  . VAL A 1 126 ? 2.453   -5.609  28.331 1.00 12.21  ? 126 VAL A CG2  1 
ATOM   2014 H  H    . VAL A 1 126 ? 3.453   -8.464  29.121 1.00 13.31  ? 126 VAL A H    1 
ATOM   2015 H  HA   . VAL A 1 126 ? 1.649   -6.904  30.593 1.00 13.18  ? 126 VAL A HA   1 
ATOM   2016 H  HB   . VAL A 1 126 ? 1.610   -7.390  27.799 1.00 13.80  ? 126 VAL A HB   1 
ATOM   2017 H  HG11 . VAL A 1 126 ? -0.008  -5.537  27.805 1.00 14.42  ? 126 VAL A HG11 1 
ATOM   2018 H  HG12 . VAL A 1 126 ? -0.543  -6.963  28.252 1.00 14.42  ? 126 VAL A HG12 1 
ATOM   2019 H  HG13 . VAL A 1 126 ? -0.193  -5.867  29.347 1.00 14.42  ? 126 VAL A HG13 1 
ATOM   2020 H  HG21 . VAL A 1 126 ? 2.195   -5.109  27.538 1.00 14.42  ? 126 VAL A HG21 1 
ATOM   2021 H  HG22 . VAL A 1 126 ? 2.436   -5.020  29.105 1.00 14.42  ? 126 VAL A HG22 1 
ATOM   2022 H  HG23 . VAL A 1 126 ? 3.353   -5.960  28.212 1.00 14.42  ? 126 VAL A HG23 1 
ATOM   2023 N  N    . ALA A 1 127 ? -0.018  -8.619  31.040 1.00 10.51  ? 127 ALA A N    1 
ATOM   2024 C  CA   . ALA A 1 127 ? -1.153  -9.515  31.217 1.00 10.66  ? 127 ALA A CA   1 
ATOM   2025 C  C    . ALA A 1 127 ? -2.375  -8.904  30.534 1.00 10.27  ? 127 ALA A C    1 
ATOM   2026 O  O    . ALA A 1 127 ? -2.478  -7.680  30.432 1.00 10.96  ? 127 ALA A O    1 
ATOM   2027 C  CB   . ALA A 1 127 ? -1.429  -9.738  32.680 1.00 11.49  ? 127 ALA A CB   1 
ATOM   2028 H  H    . ALA A 1 127 ? 0.137   -7.986  31.681 1.00 13.18  ? 127 ALA A H    1 
ATOM   2029 H  HA   . ALA A 1 127 ? -0.950  -10.380 30.791 1.00 12.99  ? 127 ALA A HA   1 
ATOM   2030 H  HB1  . ALA A 1 127 ? -2.082  -10.450 32.783 1.00 13.39  ? 127 ALA A HB1  1 
ATOM   2031 H  HB2  . ALA A 1 127 ? -0.605  -9.986  33.132 1.00 13.39  ? 127 ALA A HB2  1 
ATOM   2032 H  HB3  . ALA A 1 127 ? -1.778  -8.921  33.073 1.00 13.39  ? 127 ALA A HB3  1 
ATOM   2033 N  N    . ARG A 1 128 ? -3.312  -9.761  30.104 1.00 10.42  ? 128 ARG A N    1 
ATOM   2034 C  CA   . ARG A 1 128 ? -4.417  -9.270  29.295 1.00 10.45  ? 128 ARG A CA   1 
ATOM   2035 C  C    . ARG A 1 128 ? -5.692  -10.067 29.553 1.00 10.35  ? 128 ARG A C    1 
ATOM   2036 O  O    . ARG A 1 128 ? -5.623  -11.246 29.892 1.00 10.84  ? 128 ARG A O    1 
ATOM   2037 C  CB   . ARG A 1 128 ? -4.084  -9.308  27.802 1.00 10.88  ? 128 ARG A CB   1 
ATOM   2038 C  CG   . ARG A 1 128 ? -4.092  -10.696 27.188 1.00 11.83  ? 128 ARG A CG   1 
ATOM   2039 C  CD   . ARG A 1 128 ? -3.483  -10.788 25.798 1.00 12.25  ? 128 ARG A CD   1 
ATOM   2040 N  NE   . ARG A 1 128 ? -3.783  -12.052 25.122 1.00 13.27  ? 128 ARG A NE   1 
ATOM   2041 C  CZ   . ARG A 1 128 ? -3.326  -13.240 25.505 1.00 13.13  ? 128 ARG A CZ   1 
ATOM   2042 N  NH1  . ARG A 1 128 ? -2.293  -13.345 26.327 1.00 13.24  ? 128 ARG A NH1  1 
ATOM   2043 N  NH2  . ARG A 1 128 ? -3.853  -14.342 24.994 1.00 15.18  ? 128 ARG A NH2  1 
ATOM   2044 H  H    . ARG A 1 128 ? -3.264  -10.649 30.315 1.00 12.99  ? 128 ARG A H    1 
ATOM   2045 H  HA   . ARG A 1 128 ? -4.585  -8.337  29.548 1.00 12.68  ? 128 ARG A HA   1 
ATOM   2046 H  HB2  . ARG A 1 128 ? -4.734  -8.750  27.326 1.00 13.44  ? 128 ARG A HB2  1 
ATOM   2047 H  HB3  . ARG A 1 128 ? -3.197  -8.912  27.672 1.00 13.44  ? 128 ARG A HB3  1 
ATOM   2048 H  HG2  . ARG A 1 128 ? -3.605  -11.306 27.781 1.00 14.39  ? 128 ARG A HG2  1 
ATOM   2049 H  HG3  . ARG A 1 128 ? -5.019  -11.015 27.138 1.00 14.40  ? 128 ARG A HG3  1 
ATOM   2050 H  HD2  . ARG A 1 128 ? -3.823  -10.047 25.253 1.00 15.28  ? 128 ARG A HD2  1 
ATOM   2051 H  HD3  . ARG A 1 128 ? -2.510  -10.684 25.867 1.00 15.28  ? 128 ARG A HD3  1 
ATOM   2052 H  HE   . ARG A 1 128 ? -4.295  -12.025 24.417 1.00 17.49  ? 128 ARG A HE   1 
ATOM   2053 H  HH11 . ARG A 1 128 ? -2.015  -12.646 26.783 1.00 15.31  ? 128 ARG A HH11 1 
ATOM   2054 H  HH12 . ARG A 1 128 ? -1.883  -14.120 26.417 1.00 15.34  ? 128 ARG A HH12 1 
ATOM   2055 H  HH21 . ARG A 1 128 ? -4.659  -14.319 24.642 1.00 16.37  ? 128 ARG A HH21 1 
ATOM   2056 H  HH22 . ARG A 1 128 ? -3.397  -15.094 25.007 1.00 16.33  ? 128 ARG A HH22 1 
ATOM   2057 N  N    . ARG A 1 129 ? -6.833  -9.434  29.301 1.00 10.15  ? 129 ARG A N    1 
ATOM   2058 C  CA   . ARG A 1 129 ? -8.120  -10.112 29.259 1.00 9.92   ? 129 ARG A CA   1 
ATOM   2059 C  C    . ARG A 1 129 ? -9.021  -9.395  28.272 1.00 9.83   ? 129 ARG A C    1 
ATOM   2060 O  O    . ARG A 1 129 ? -9.152  -8.172  28.280 1.00 12.23  ? 129 ARG A O    1 
ATOM   2061 C  CB   . ARG A 1 129 ? -8.741  -10.178 30.645 1.00 10.99  ? 129 ARG A CB   1 
ATOM   2062 C  CG   . ARG A 1 129 ? -10.025 -11.004 30.652 1.00 12.82  ? 129 ARG A CG   1 
ATOM   2063 C  CD   . ARG A 1 129 ? -10.593 -11.152 32.043 1.00 14.51  ? 129 ARG A CD   1 
ATOM   2064 N  NE   . ARG A 1 129 ? -9.815  -12.116 32.770 1.00 19.19  ? 129 ARG A NE   1 
ATOM   2065 C  CZ   . ARG A 1 129 ? -9.942  -12.316 34.071 1.00 20.95  ? 129 ARG A CZ   1 
ATOM   2066 N  NH1  . ARG A 1 129 ? -10.703 -11.503 34.772 1.00 19.45  ? 129 ARG A NH1  1 
ATOM   2067 N  NH2  . ARG A 1 129 ? -9.270  -13.263 34.709 1.00 25.15  ? 129 ARG A NH2  1 
ATOM   2068 H  H    . ARG A 1 129 ? -6.812  -8.532  29.150 1.00 12.68  ? 129 ARG A H    1 
ATOM   2069 H  HA   . ARG A 1 129 ? -7.971  -11.030 28.939 1.00 18.28  ? 129 ARG A HA   1 
ATOM   2070 H  HB2  . ARG A 1 129 ? -8.097  -10.577 31.266 1.00 24.58  ? 129 ARG A HB2  1 
ATOM   2071 H  HB3  . ARG A 1 129 ? -8.940  -9.269  30.950 1.00 24.57  ? 129 ARG A HB3  1 
ATOM   2072 H  HG2  . ARG A 1 129 ? -10.694 -10.570 30.081 1.00 25.95  ? 129 ARG A HG2  1 
ATOM   2073 H  HG3  . ARG A 1 129 ? -9.842  -11.894 30.282 1.00 25.95  ? 129 ARG A HG3  1 
ATOM   2074 H  HD2  . ARG A 1 129 ? -10.565 -10.287 32.504 1.00 15.28  ? 129 ARG A HD2  1 
ATOM   2075 H  HD3  . ARG A 1 129 ? -11.527 -11.449 31.993 1.00 15.29  ? 129 ARG A HD3  1 
ATOM   2076 H  HE   . ARG A 1 129 ? -9.229  -12.595 32.336 1.00 26.18  ? 129 ARG A HE   1 
ATOM   2077 H  HH11 . ARG A 1 129 ? -11.544 -11.381 34.542 1.00 20.73  ? 129 ARG A HH11 1 
ATOM   2078 H  HH12 . ARG A 1 129 ? -10.369 -11.085 35.472 1.00 20.73  ? 129 ARG A HH12 1 
ATOM   2079 H  HH21 . ARG A 1 129 ? -9.074  -14.013 34.296 1.00 25.72  ? 129 ARG A HH21 1 
ATOM   2080 H  HH22 . ARG A 1 129 ? -9.021  -13.137 35.543 1.00 25.72  ? 129 ARG A HH22 1 
ATOM   2081 N  N    . LEU A 1 130 ? -9.620  -10.172 27.391 1.00 9.22   ? 130 LEU A N    1 
ATOM   2082 C  CA   . LEU A 1 130 ? -10.532 -9.710  26.365 1.00 9.19   ? 130 LEU A CA   1 
ATOM   2083 C  C    . LEU A 1 130 ? -11.979 -9.961  26.759 1.00 8.49   ? 130 LEU A C    1 
ATOM   2084 O  O    . LEU A 1 130 ? -12.339 -11.091 27.108 1.00 9.52   ? 130 LEU A O    1 
ATOM   2085 C  CB   . LEU A 1 130 ? -10.229 -10.449 25.067 1.00 9.60   ? 130 LEU A CB   1 
ATOM   2086 C  CG   . LEU A 1 130 ? -11.134 -10.173 23.868 1.00 9.69   ? 130 LEU A CG   1 
ATOM   2087 C  CD1  . LEU A 1 130 ? -11.056 -8.711  23.438 1.00 10.73  ? 130 LEU A CD1  1 
ATOM   2088 C  CD2  . LEU A 1 130 ? -10.767 -11.111 22.721 1.00 10.59  ? 130 LEU A CD2  1 
ATOM   2089 H  H    . LEU A 1 130 ? -9.451  -11.070 27.431 1.00 17.66  ? 130 LEU A H    1 
ATOM   2090 H  HA   . LEU A 1 130 ? -10.397 -8.744  26.233 1.00 12.84  ? 130 LEU A HA   1 
ATOM   2091 H  HB2  . LEU A 1 130 ? -9.313  -10.232 24.806 1.00 16.93  ? 130 LEU A HB2  1 
ATOM   2092 H  HB3  . LEU A 1 130 ? -10.254 -11.408 25.254 1.00 16.93  ? 130 LEU A HB3  1 
ATOM   2093 H  HG   . LEU A 1 130 ? -12.067 -10.365 24.133 1.00 11.80  ? 130 LEU A HG   1 
ATOM   2094 H  HD11 . LEU A 1 130 ? -11.573 -8.584  22.623 1.00 12.84  ? 130 LEU A HD11 1 
ATOM   2095 H  HD12 . LEU A 1 130 ? -11.418 -8.144  24.142 1.00 12.84  ? 130 LEU A HD12 1 
ATOM   2096 H  HD13 . LEU A 1 130 ? -10.128 -8.469  23.273 1.00 12.84  ? 130 LEU A HD13 1 
ATOM   2097 H  HD21 . LEU A 1 130 ? -11.515 -11.177 22.104 1.00 16.41  ? 130 LEU A HD21 1 
ATOM   2098 H  HD22 . LEU A 1 130 ? -9.991  -10.759 22.251 1.00 16.41  ? 130 LEU A HD22 1 
ATOM   2099 H  HD23 . LEU A 1 130 ? -10.557 -11.991 23.075 1.00 16.41  ? 130 LEU A HD23 1 
ATOM   2100 N  N    . HIS A 1 131 ? -12.801 -8.920  26.699 1.00 8.27   ? 131 HIS A N    1 
ATOM   2101 C  CA   . HIS A 1 131 ? -14.222 -9.037  26.970 1.00 8.42   ? 131 HIS A CA   1 
ATOM   2102 C  C    . HIS A 1 131 ? -14.995 -8.595  25.728 1.00 8.32   ? 131 HIS A C    1 
ATOM   2103 O  O    . HIS A 1 131 ? -14.640 -7.576  25.129 1.00 9.30   ? 131 HIS A O    1 
ATOM   2104 C  CB   . HIS A 1 131 ? -14.662 -8.176  28.162 1.00 8.76   ? 131 HIS A CB   1 
ATOM   2105 C  CG   . HIS A 1 131 ? -13.807 -8.284  29.380 1.00 9.22   ? 131 HIS A CG   1 
ATOM   2106 N  ND1  . HIS A 1 131 ? -12.580 -7.696  29.488 1.00 9.44   ? 131 HIS A ND1  1 
ATOM   2107 C  CD2  . HIS A 1 131 ? -13.994 -8.903  30.564 1.00 10.18  ? 131 HIS A CD2  1 
ATOM   2108 C  CE1  . HIS A 1 131 ? -12.065 -8.004  30.682 1.00 10.44  ? 131 HIS A CE1  1 
ATOM   2109 N  NE2  . HIS A 1 131 ? -12.884 -8.734  31.376 1.00 10.73  ? 131 HIS A NE2  1 
ATOM   2110 H  H    . HIS A 1 131 ? -12.466 -8.098  26.481 1.00 12.84  ? 131 HIS A H    1 
ATOM   2111 H  HA   . HIS A 1 131 ? -14.440 -9.983  27.155 1.00 10.31  ? 131 HIS A HA   1 
ATOM   2112 H  HB2  . HIS A 1 131 ? -14.683 -7.238  27.875 1.00 10.85  ? 131 HIS A HB2  1 
ATOM   2113 H  HB3  . HIS A 1 131 ? -15.581 -8.424  28.401 1.00 10.85  ? 131 HIS A HB3  1 
ATOM   2114 H  HD1  . HIS A 1 131 ? -12.179 -7.224  28.861 1.00 12.05  ? 131 HIS A HD1  1 
ATOM   2115 H  HD2  . HIS A 1 131 ? -14.749 -9.406  30.798 1.00 12.05  ? 131 HIS A HD2  1 
ATOM   2116 H  HE1  . HIS A 1 131 ? -11.223 -7.703  30.979 1.00 12.05  ? 131 HIS A HE1  1 
ATOM   2117 N  N    . HIS A 1 132 ? -16.021 -9.354  25.379 1.00 8.24   ? 132 HIS A N    1 
ATOM   2118 C  CA   . HIS A 1 132 ? -16.874 -9.094  24.229 1.00 8.30   ? 132 HIS A CA   1 
ATOM   2119 C  C    . HIS A 1 132 ? -18.180 -8.449  24.672 1.00 8.42   ? 132 HIS A C    1 
ATOM   2120 O  O    . HIS A 1 132 ? -18.810 -8.902  25.634 1.00 9.31   ? 132 HIS A O    1 
ATOM   2121 C  CB   . HIS A 1 132 ? -17.194 -10.413 23.519 1.00 8.51   ? 132 HIS A CB   1 
ATOM   2122 C  CG   . HIS A 1 132 ? -16.020 -11.129 22.984 1.00 9.09   ? 132 HIS A CG   1 
ATOM   2123 N  ND1  . HIS A 1 132 ? -15.762 -11.188 21.633 1.00 10.11  ? 132 HIS A ND1  1 
ATOM   2124 C  CD2  . HIS A 1 132 ? -15.043 -11.806 23.624 1.00 10.05  ? 132 HIS A CD2  1 
ATOM   2125 C  CE1  . HIS A 1 132 ? -14.647 -11.874 21.486 1.00 10.85  ? 132 HIS A CE1  1 
ATOM   2126 N  NE2  . HIS A 1 132 ? -14.210 -12.285 22.666 1.00 10.88  ? 132 HIS A NE2  1 
ATOM   2127 H  H    . HIS A 1 132 ? -16.208 -10.088 25.890 1.00 10.31  ? 132 HIS A H    1 
ATOM   2128 H  HA   . HIS A 1 132 ? -16.410 -8.482  23.606 1.00 10.42  ? 132 HIS A HA   1 
ATOM   2129 H  HB2  . HIS A 1 132 ? -17.662 -11.002 24.150 1.00 10.33  ? 132 HIS A HB2  1 
ATOM   2130 H  HB3  . HIS A 1 132 ? -17.814 -10.227 22.780 1.00 10.33  ? 132 HIS A HB3  1 
ATOM   2131 H  HD2  . HIS A 1 132 ? -14.973 -11.934 24.549 1.00 15.58  ? 132 HIS A HD2  1 
ATOM   2132 H  HE1  . HIS A 1 132 ? -14.253 -12.074 20.657 1.00 15.58  ? 132 HIS A HE1  1 
ATOM   2133 H  HE2  . HIS A 1 132 ? -13.490 -12.739 22.809 1.00 15.58  ? 132 HIS A HE2  1 
ATOM   2134 N  N    . CYS A 1 133 ? -18.647 -7.470  23.909 1.00 8.46   ? 133 CYS A N    1 
ATOM   2135 C  CA   . CYS A 1 133 ? -19.868 -6.760  24.228 1.00 8.59   ? 133 CYS A CA   1 
ATOM   2136 C  C    . CYS A 1 133 ? -20.959 -6.916  23.182 1.00 8.80   ? 133 CYS A C    1 
ATOM   2137 O  O    . CYS A 1 133 ? -22.132 -6.649  23.498 1.00 9.62   ? 133 CYS A O    1 
ATOM   2138 C  CB   . CYS A 1 133 ? -19.643 -5.268  24.367 1.00 9.35   ? 133 CYS A CB   1 
ATOM   2139 S  SG   . CYS A 1 133 ? -18.259 -4.796  25.428 1.00 10.08  ? 133 CYS A SG   1 
ATOM   2140 H  H    . CYS A 1 133 ? -18.179 -7.224  23.164 1.00 10.42  ? 133 CYS A H    1 
ATOM   2141 H  HA   . CYS A 1 133 ? -20.209 -7.102  25.086 1.00 10.56  ? 133 CYS A HA   1 
ATOM   2142 H  HB2  . CYS A 1 133 ? -19.487 -4.891  23.478 1.00 11.37  ? 133 CYS A HB2  1 
ATOM   2143 H  HB3  . CYS A 1 133 ? -20.457 -4.857  24.724 1.00 11.37  ? 133 CYS A HB3  1 
ATOM   2144 H  HG   . CYS A 1 133 ? -18.660 -5.313  26.438 1.00 12.02  ? 133 CYS A HG   1 
ATOM   2145 N  N    . ARG A 1 134 ? -20.620 -7.262  21.928 1.00 9.03   ? 134 ARG A N    1 
ATOM   2146 C  CA   . ARG A 1 134 ? -21.580 -7.055  20.844 1.00 9.55   ? 134 ARG A CA   1 
ATOM   2147 C  C    . ARG A 1 134 ? -22.709 -8.078  20.849 1.00 9.42   ? 134 ARG A C    1 
ATOM   2148 O  O    . ARG A 1 134 ? -23.710 -7.885  20.154 1.00 10.69  ? 134 ARG A O    1 
ATOM   2149 C  CB   . ARG A 1 134 ? -20.853 -6.981  19.511 1.00 10.54  ? 134 ARG A CB   1 
ATOM   2150 C  CG   . ARG A 1 134 ? -21.634 -6.455  18.354 1.00 12.90  ? 134 ARG A CG   1 
ATOM   2151 C  CD   . ARG A 1 134 ? -20.773 -6.273  17.119 1.00 13.11  ? 134 ARG A CD   1 
ATOM   2152 N  NE   . ARG A 1 134 ? -21.494 -5.689  16.025 1.00 13.59  ? 134 ARG A NE   1 
ATOM   2153 C  CZ   . ARG A 1 134 ? -22.261 -6.338  15.178 1.00 14.42  ? 134 ARG A CZ   1 
ATOM   2154 N  NH1  . ARG A 1 134 ? -22.398 -7.626  15.296 1.00 15.38  ? 134 ARG A NH1  1 
ATOM   2155 N  NH2  . ARG A 1 134 ? -22.885 -5.656  14.224 1.00 16.58  ? 134 ARG A NH2  1 
ATOM   2156 H  H    . ARG A 1 134 ? -19.805 -7.632  21.745 1.00 10.42  ? 134 ARG A H    1 
ATOM   2157 H  HA   . ARG A 1 134 ? -21.994 -6.175  20.995 1.00 13.26  ? 134 ARG A HA   1 
ATOM   2158 H  HB2  . ARG A 1 134 ? -20.061 -6.418  19.629 1.00 15.65  ? 134 ARG A HB2  1 
ATOM   2159 H  HB3  . ARG A 1 134 ? -20.541 -7.883  19.286 1.00 15.65  ? 134 ARG A HB3  1 
ATOM   2160 H  HG2  . ARG A 1 134 ? -22.363 -7.075  18.144 1.00 15.88  ? 134 ARG A HG2  1 
ATOM   2161 H  HG3  . ARG A 1 134 ? -22.031 -5.591  18.597 1.00 15.88  ? 134 ARG A HG3  1 
ATOM   2162 H  HD2  . ARG A 1 134 ? -20.012 -5.696  17.343 1.00 15.66  ? 134 ARG A HD2  1 
ATOM   2163 H  HD3  . ARG A 1 134 ? -20.416 -7.143  16.844 1.00 15.66  ? 134 ARG A HD3  1 
ATOM   2164 H  HE   . ARG A 1 134 ? -21.416 -4.828  15.911 1.00 16.43  ? 134 ARG A HE   1 
ATOM   2165 H  HH11 . ARG A 1 134 ? -22.821 -7.961  15.993 1.00 15.88  ? 134 ARG A HH11 1 
ATOM   2166 H  HH12 . ARG A 1 134 ? -22.069 -8.161  14.678 1.00 15.88  ? 134 ARG A HH12 1 
ATOM   2167 H  HH21 . ARG A 1 134 ? -22.834 -4.778  14.205 1.00 16.43  ? 134 ARG A HH21 1 
ATOM   2168 H  HH22 . ARG A 1 134 ? -23.349 -6.085  13.613 1.00 16.43  ? 134 ARG A HH22 1 
ATOM   2169 N  N    . ASP A 1 135 ? -22.581 -9.154  21.617 1.00 9.37   ? 135 ASP A N    1 
ATOM   2170 C  CA   . ASP A 1 135 ? -23.656 -10.112 21.709 1.00 10.34  ? 135 ASP A CA   1 
ATOM   2171 C  C    . ASP A 1 135 ? -24.443 -9.975  23.008 1.00 11.54  ? 135 ASP A C    1 
ATOM   2172 O  O    . ASP A 1 135 ? -25.359 -10.729 23.265 1.00 14.23  ? 135 ASP A O    1 
ATOM   2173 C  CB   . ASP A 1 135 ? -23.140 -11.502 21.412 1.00 10.54  ? 135 ASP A CB   1 
ATOM   2174 C  CG   . ASP A 1 135 ? -22.524 -11.607 20.024 1.00 10.71  ? 135 ASP A CG   1 
ATOM   2175 O  OD1  . ASP A 1 135 ? -23.099 -11.094 19.059 1.00 11.27  ? 135 ASP A OD1  1 
ATOM   2176 O  OD2  . ASP A 1 135 ? -21.478 -12.247 19.921 1.00 12.89  ? 135 ASP A OD2  1 
ATOM   2177 H  H    . ASP A 1 135 ? -21.807 -9.306  22.079 1.00 13.94  ? 135 ASP A H    1 
ATOM   2178 H  HA   . ASP A 1 135 ? -24.286 -9.903  20.982 1.00 11.99  ? 135 ASP A HA   1 
ATOM   2179 H  HB2  . ASP A 1 135 ? -22.468 -11.752 22.078 1.00 11.97  ? 135 ASP A HB2  1 
ATOM   2180 H  HB3  . ASP A 1 135 ? -23.882 -12.133 21.468 1.00 11.97  ? 135 ASP A HB3  1 
ATOM   2181 N  N    . LEU A 1 136 ? -24.156 -8.935  23.794 1.00 11.86  ? 136 LEU A N    1 
ATOM   2182 C  CA   . LEU A 1 136 ? -25.057 -8.531  24.878 1.00 14.54  ? 136 LEU A CA   1 
ATOM   2183 C  C    . LEU A 1 136 ? -26.336 -7.855  24.326 1.00 15.39  ? 136 LEU A C    1 
ATOM   2184 O  O    . LEU A 1 136 ? -27.381 -7.862  24.954 1.00 17.30  ? 136 LEU A O    1 
ATOM   2185 C  CB   . LEU A 1 136 ? -24.336 -7.583  25.841 1.00 14.54  ? 136 LEU A CB   1 
ATOM   2186 C  CG   . LEU A 1 136 ? -23.010 -7.997  26.484 1.00 13.30  ? 136 LEU A CG   1 
ATOM   2187 C  CD1  . LEU A 1 136 ? -22.385 -6.806  27.197 1.00 13.93  ? 136 LEU A CD1  1 
ATOM   2188 C  CD2  . LEU A 1 136 ? -23.134 -9.139  27.457 1.00 15.58  ? 136 LEU A CD2  1 
ATOM   2189 H  H    . LEU A 1 136 ? -23.385 -8.463  23.662 1.00 13.94  ? 136 LEU A H    1 
ATOM   2190 H  HA   . LEU A 1 136 ? -25.325 -9.342  25.370 1.00 17.45  ? 136 LEU A HA   1 
ATOM   2191 H  HB2  . LEU A 1 136 ? -24.179 -6.746  25.360 1.00 16.99  ? 136 LEU A HB2  1 
ATOM   2192 H  HB3  . LEU A 1 136 ? -24.960 -7.376  26.566 1.00 16.99  ? 136 LEU A HB3  1 
ATOM   2193 H  HG   . LEU A 1 136 ? -22.395 -8.276  25.762 1.00 13.94  ? 136 LEU A HG   1 
ATOM   2194 H  HD11 . LEU A 1 136 ? -21.549 -7.079  27.613 1.00 16.99  ? 136 LEU A HD11 1 
ATOM   2195 H  HD12 . LEU A 1 136 ? -22.210 -6.097  26.554 1.00 16.99  ? 136 LEU A HD12 1 
ATOM   2196 H  HD13 . LEU A 1 136 ? -22.996 -6.480  27.881 1.00 16.99  ? 136 LEU A HD13 1 
ATOM   2197 H  HD21 . LEU A 1 136 ? -22.252 -9.378  27.792 1.00 17.11  ? 136 LEU A HD21 1 
ATOM   2198 H  HD22 . LEU A 1 136 ? -23.702 -8.873  28.200 1.00 17.11  ? 136 LEU A HD22 1 
ATOM   2199 H  HD23 . LEU A 1 136 ? -23.528 -9.907  27.008 1.00 17.11  ? 136 LEU A HD23 1 
ATOM   2200 N  N    . GLY A 1 137 ? -26.245 -7.156  23.187 1.00 16.51  ? 137 GLY A N    1 
ATOM   2201 C  CA   . GLY A 1 137 ? -27.339 -6.407  22.600 1.00 16.57  ? 137 GLY A CA   1 
ATOM   2202 C  C    . GLY A 1 137 ? -26.803 -5.506  21.501 1.00 17.82  ? 137 GLY A C    1 
ATOM   2203 O  O    . GLY A 1 137 ? -25.609 -5.485  21.236 1.00 18.52  ? 137 GLY A O    1 
ATOM   2204 H  H    . GLY A 1 137 ? -25.441 -7.147  22.752 1.00 19.04  ? 137 GLY A H    1 
ATOM   2205 H  HA2  . GLY A 1 137 ? -28.005 -7.036  22.224 1.00 20.97  ? 137 GLY A HA2  1 
ATOM   2206 H  HA3  . GLY A 1 137 ? -27.774 -5.860  23.297 1.00 20.97  ? 137 GLY A HA3  1 
ATOM   2207 N  N    . GLU A 1 138 ? -27.720 -4.762  20.890 1.00 19.17  ? 138 GLU A N    1 
ATOM   2208 C  CA   . GLU A 1 138 ? -27.467 -3.934  19.725 1.00 22.99  ? 138 GLU A CA   1 
ATOM   2209 C  C    . GLU A 1 138 ? -26.993 -2.537  20.161 1.00 20.25  ? 138 GLU A C    1 
ATOM   2210 O  O    . GLU A 1 138 ? -26.598 -1.717  19.310 1.00 24.61  ? 138 GLU A O    1 
ATOM   2211 C  CB   . GLU A 1 138 ? -28.777 -3.983  18.887 1.00 29.57  ? 138 GLU A CB   1 
ATOM   2212 C  CG   . GLU A 1 138 ? -29.682 -5.224  19.211 1.00 34.27  ? 138 GLU A CG   1 
ATOM   2213 C  CD   . GLU A 1 138 ? -30.934 -5.553  18.388 1.00 32.73  ? 138 GLU A CD   1 
ATOM   2214 O  OE1  . GLU A 1 138 ? -30.860 -5.249  17.161 1.00 33.35  ? 138 GLU A OE1  1 
ATOM   2215 O  OE2  . GLU A 1 138 ? -31.976 -6.236  18.943 1.00 26.14  ? 138 GLU A OE2  1 
ATOM   2216 H  H    . GLU A 1 138 ? -28.553 -4.731  21.266 1.00 30.87  ? 138 GLU A H    1 
ATOM   2217 H  HA   . GLU A 1 138 ? -26.747 -4.355  19.200 1.00 25.62  ? 138 GLU A HA   1 
ATOM   2218 H  HB2  . GLU A 1 138 ? -29.288 -3.164  19.056 1.00 29.44  ? 138 GLU A HB2  1 
ATOM   2219 H  HB3  . GLU A 1 138 ? -28.540 -4.000  17.936 1.00 29.44  ? 138 GLU A HB3  1 
ATOM   2220 H  HG2  . GLU A 1 138 ? -29.109 -6.020  19.181 1.00 30.87  ? 138 GLU A HG2  1 
ATOM   2221 H  HG3  . GLU A 1 138 ? -29.981 -5.135  20.139 1.00 30.87  ? 138 GLU A HG3  1 
ATOM   2222 N  N    . ASN A 1 139 ? -27.015 -2.245  21.481 1.00 19.41  ? 139 ASN A N    1 
ATOM   2223 C  CA   . ASN A 1 139 ? -26.937 -0.888  21.996 1.00 21.36  ? 139 ASN A CA   1 
ATOM   2224 C  C    . ASN A 1 139 ? -25.787 -0.730  22.987 1.00 20.01  ? 139 ASN A C    1 
ATOM   2225 O  O    . ASN A 1 139 ? -25.829 0.185   23.807 1.00 22.93  ? 139 ASN A O    1 
ATOM   2226 C  CB   . ASN A 1 139 ? -28.271 -0.482  22.615 1.00 25.39  ? 139 ASN A CB   1 
ATOM   2227 C  CG   . ASN A 1 139 ? -29.415 -0.605  21.628 1.00 29.39  ? 139 ASN A CG   1 
ATOM   2228 O  OD1  . ASN A 1 139 ? -29.393 0.015   20.562 1.00 33.52  ? 139 ASN A OD1  1 
ATOM   2229 N  ND2  . ASN A 1 139 ? -30.407 -1.414  21.963 1.00 33.23  ? 139 ASN A ND2  1 
ATOM   2230 H  H    . ASN A 1 139 ? -27.077 -2.929  22.084 1.00 22.27  ? 139 ASN A H    1 
ATOM   2231 H  HA   . ASN A 1 139 ? -26.772 -0.281  21.237 1.00 23.61  ? 139 ASN A HA   1 
ATOM   2232 H  HB2  . ASN A 1 139 ? -28.449 -1.050  23.392 1.00 21.27  ? 139 ASN A HB2  1 
ATOM   2233 H  HB3  . ASN A 1 139 ? -28.213 0.446   22.922 1.00 21.27  ? 139 ASN A HB3  1 
ATOM   2234 H  HD21 . ASN A 1 139 ? -30.349 -1.911  22.692 1.00 21.42  ? 139 ASN A HD21 1 
ATOM   2235 H  HD22 . ASN A 1 139 ? -31.130 -1.460  21.456 1.00 21.42  ? 139 ASN A HD22 1 
ATOM   2236 N  N    . GLU A 1 140 ? -24.720 -1.544  22.878 1.00 15.63  ? 140 GLU A N    1 
ATOM   2237 C  CA   . GLU A 1 140 ? -23.569 -1.342  23.742 1.00 14.26  ? 140 GLU A CA   1 
ATOM   2238 C  C    . GLU A 1 140 ? -22.681 -0.290  23.110 1.00 14.36  ? 140 GLU A C    1 
ATOM   2239 O  O    . GLU A 1 140 ? -22.542 -0.282  21.879 1.00 15.19  ? 140 GLU A O    1 
ATOM   2240 C  CB   . GLU A 1 140 ? -22.798 -2.640  23.946 1.00 14.66  ? 140 GLU A CB   1 
ATOM   2241 C  CG   . GLU A 1 140 ? -23.659 -3.741  24.465 1.00 16.88  ? 140 GLU A CG   1 
ATOM   2242 C  CD   . GLU A 1 140 ? -24.233 -3.476  25.832 1.00 19.30  ? 140 GLU A CD   1 
ATOM   2243 O  OE1  . GLU A 1 140 ? -23.528 -2.896  26.697 1.00 21.38  ? 140 GLU A OE1  1 
ATOM   2244 O  OE2  . GLU A 1 140 ? -25.414 -3.800  25.997 1.00 24.30  ? 140 GLU A OE2  1 
ATOM   2245 H  H    . GLU A 1 140 ? -24.708 -2.217  22.260 1.00 20.22  ? 140 GLU A H    1 
ATOM   2246 H  HA   . GLU A 1 140 ? -23.883 -1.016  24.615 1.00 17.66  ? 140 GLU A HA   1 
ATOM   2247 H  HB2  . GLU A 1 140 ? -22.407 -2.913  23.090 1.00 13.29  ? 140 GLU A HB2  1 
ATOM   2248 H  HB3  . GLU A 1 140 ? -22.065 -2.477  24.576 1.00 13.29  ? 140 GLU A HB3  1 
ATOM   2249 H  HG2  . GLU A 1 140 ? -24.398 -3.896  23.839 1.00 20.22  ? 140 GLU A HG2  1 
ATOM   2250 H  HG3  . GLU A 1 140 ? -23.130 -4.565  24.507 1.00 20.22  ? 140 GLU A HG3  1 
ATOM   2251 N  N    . PRO A 1 141 ? -22.035 0.578   23.895 1.00 13.65  ? 141 PRO A N    1 
ATOM   2252 C  CA   . PRO A 1 141 ? -21.243 1.631   23.283 1.00 13.78  ? 141 PRO A CA   1 
ATOM   2253 C  C    . PRO A 1 141 ? -19.981 1.142   22.594 1.00 12.46  ? 141 PRO A C    1 
ATOM   2254 O  O    . PRO A 1 141 ? -19.479 1.825   21.708 1.00 13.28  ? 141 PRO A O    1 
ATOM   2255 C  CB   . PRO A 1 141 ? -20.955 2.565   24.455 1.00 15.86  ? 141 PRO A CB   1 
ATOM   2256 C  CG   . PRO A 1 141 ? -21.092 1.711   25.677 1.00 15.80  ? 141 PRO A CG   1 
ATOM   2257 C  CD   . PRO A 1 141 ? -22.182 0.731   25.352 1.00 14.70  ? 141 PRO A CD   1 
ATOM   2258 H  HA   . PRO A 1 141 ? -21.808 2.112   22.627 1.00 16.42  ? 141 PRO A HA   1 
ATOM   2259 H  HB2  . PRO A 1 141 ? -20.049 2.936   24.392 1.00 34.18  ? 141 PRO A HB2  1 
ATOM   2260 H  HB3  . PRO A 1 141 ? -21.598 3.305   24.477 1.00 34.18  ? 141 PRO A HB3  1 
ATOM   2261 H  HG2  . PRO A 1 141 ? -20.253 1.244   25.870 1.00 15.94  ? 141 PRO A HG2  1 
ATOM   2262 H  HG3  . PRO A 1 141 ? -21.335 2.254   26.454 1.00 15.94  ? 141 PRO A HG3  1 
ATOM   2263 H  HD2  . PRO A 1 141 ? -22.046 -0.117  25.813 1.00 17.66  ? 141 PRO A HD2  1 
ATOM   2264 H  HD3  . PRO A 1 141 ? -23.060 1.087   25.584 1.00 17.66  ? 141 PRO A HD3  1 
ATOM   2265 N  N    . PHE A 1 142 ? -19.413 0.026   23.093 1.00 10.74  ? 142 PHE A N    1 
ATOM   2266 C  CA   . PHE A 1 142 ? -18.209 -0.538  22.524 1.00 10.13  ? 142 PHE A CA   1 
ATOM   2267 C  C    . PHE A 1 142 ? -18.453 -1.982  22.150 1.00 10.02  ? 142 PHE A C    1 
ATOM   2268 O  O    . PHE A 1 142 ? -19.401 -2.604  22.636 1.00 10.53  ? 142 PHE A O    1 
ATOM   2269 C  CB   . PHE A 1 142 ? -17.026 -0.409  23.494 1.00 10.93  ? 142 PHE A CB   1 
ATOM   2270 C  CG   . PHE A 1 142 ? -16.797 1.027   23.908 1.00 11.81  ? 142 PHE A CG   1 
ATOM   2271 C  CD1  . PHE A 1 142 ? -16.066 1.894   23.134 1.00 13.76  ? 142 PHE A CD1  1 
ATOM   2272 C  CD2  . PHE A 1 142 ? -17.401 1.489   25.061 1.00 13.89  ? 142 PHE A CD2  1 
ATOM   2273 C  CE1  . PHE A 1 142 ? -15.922 3.225   23.528 1.00 16.57  ? 142 PHE A CE1  1 
ATOM   2274 C  CE2  . PHE A 1 142 ? -17.270 2.806   25.442 1.00 16.78  ? 142 PHE A CE2  1 
ATOM   2275 C  CZ   . PHE A 1 142 ? -16.527 3.653   24.677 1.00 17.88  ? 142 PHE A CZ   1 
ATOM   2276 H  H    . PHE A 1 142 ? -19.791 -0.387  23.815 1.00 13.14  ? 142 PHE A H    1 
ATOM   2277 H  HA   . PHE A 1 142 ? -17.987 -0.041  21.696 1.00 11.44  ? 142 PHE A HA   1 
ATOM   2278 H  HB2  . PHE A 1 142 ? -17.206 -0.954  24.289 1.00 14.46  ? 142 PHE A HB2  1 
ATOM   2279 H  HB3  . PHE A 1 142 ? -16.219 -0.755  23.060 1.00 14.47  ? 142 PHE A HB3  1 
ATOM   2280 H  HD1  . PHE A 1 142 ? -15.660 1.589   22.338 1.00 16.56  ? 142 PHE A HD1  1 
ATOM   2281 H  HD2  . PHE A 1 142 ? -17.925 0.900   25.582 1.00 15.89  ? 142 PHE A HD2  1 
ATOM   2282 H  HE1  . PHE A 1 142 ? -15.409 3.823   23.008 1.00 16.67  ? 142 PHE A HE1  1 
ATOM   2283 H  HE2  . PHE A 1 142 ? -17.672 3.113   26.239 1.00 16.49  ? 142 PHE A HE2  1 
ATOM   2284 H  HZ   . PHE A 1 142 ? -16.423 4.549   24.949 1.00 17.02  ? 142 PHE A HZ   1 
ATOM   2285 N  N    . ASP A 1 143 ? -17.587 -2.530  21.302 1.00 9.25   ? 143 ASP A N    1 
ATOM   2286 C  CA   . ASP A 1 143 ? -17.632 -3.952  20.975 1.00 9.06   ? 143 ASP A CA   1 
ATOM   2287 C  C    . ASP A 1 143 ? -16.760 -4.814  21.871 1.00 8.33   ? 143 ASP A C    1 
ATOM   2288 O  O    . ASP A 1 143 ? -17.072 -5.989  22.064 1.00 8.75   ? 143 ASP A O    1 
ATOM   2289 C  CB   . ASP A 1 143 ? -17.215 -4.193  19.527 1.00 9.34   ? 143 ASP A CB   1 
ATOM   2290 C  CG   . ASP A 1 143 ? -18.167 -3.587  18.509 1.00 9.73   ? 143 ASP A CG   1 
ATOM   2291 O  OD1  . ASP A 1 143 ? -19.395 -3.595  18.781 1.00 11.51  ? 143 ASP A OD1  1 
ATOM   2292 O  OD2  . ASP A 1 143 ? -17.693 -3.122  17.451 1.00 10.50  ? 143 ASP A OD2  1 
ATOM   2293 H  H    . ASP A 1 143 ? -16.945 -2.008  20.913 1.00 11.44  ? 143 ASP A H    1 
ATOM   2294 H  HA   . ASP A 1 143 ? -18.564 -4.258  21.073 1.00 11.22  ? 143 ASP A HA   1 
ATOM   2295 H  HB2  . ASP A 1 143 ? -16.325 -3.811  19.383 1.00 11.48  ? 143 ASP A HB2  1 
ATOM   2296 H  HB3  . ASP A 1 143 ? -17.165 -5.157  19.364 1.00 11.48  ? 143 ASP A HB3  1 
ATOM   2297 N  N    . PHE A 1 144 ? -15.674 -4.248  22.400 1.00 8.54   ? 144 PHE A N    1 
ATOM   2298 C  CA   . PHE A 1 144 ? -14.747 -4.984  23.236 1.00 8.42   ? 144 PHE A CA   1 
ATOM   2299 C  C    . PHE A 1 144 ? -14.346 -4.106  24.402 1.00 8.55   ? 144 PHE A C    1 
ATOM   2300 O  O    . PHE A 1 144 ? -14.196 -2.902  24.257 1.00 9.22   ? 144 PHE A O    1 
ATOM   2301 C  CB   . PHE A 1 144 ? -13.475 -5.372  22.486 1.00 8.95   ? 144 PHE A CB   1 
ATOM   2302 C  CG   . PHE A 1 144 ? -13.743 -6.118  21.214 1.00 8.68   ? 144 PHE A CG   1 
ATOM   2303 C  CD1  . PHE A 1 144 ? -14.034 -7.466  21.234 1.00 9.52   ? 144 PHE A CD1  1 
ATOM   2304 C  CD2  . PHE A 1 144 ? -13.700 -5.461  20.008 1.00 9.62   ? 144 PHE A CD2  1 
ATOM   2305 C  CE1  . PHE A 1 144 ? -14.262 -8.131  20.034 1.00 11.08  ? 144 PHE A CE1  1 
ATOM   2306 C  CE2  . PHE A 1 144 ? -13.937 -6.127  18.826 1.00 11.19  ? 144 PHE A CE2  1 
ATOM   2307 C  CZ   . PHE A 1 144 ? -14.220 -7.463  18.838 1.00 11.40  ? 144 PHE A CZ   1 
ATOM   2308 H  H    . PHE A 1 144 ? -15.500 -3.368  22.226 1.00 11.44  ? 144 PHE A H    1 
ATOM   2309 H  HA   . PHE A 1 144 ? -15.188 -5.799  23.579 1.00 10.12  ? 144 PHE A HA   1 
ATOM   2310 H  HB2  . PHE A 1 144 ? -12.971 -4.557  22.280 1.00 11.47  ? 144 PHE A HB2  1 
ATOM   2311 H  HB3  . PHE A 1 144 ? -12.923 -5.929  23.074 1.00 11.47  ? 144 PHE A HB3  1 
ATOM   2312 H  HD1  . PHE A 1 144 ? -14.061 -7.935  22.053 1.00 11.47  ? 144 PHE A HD1  1 
ATOM   2313 H  HD2  . PHE A 1 144 ? -13.504 -4.538  19.991 1.00 11.47  ? 144 PHE A HD2  1 
ATOM   2314 H  HE1  . PHE A 1 144 ? -14.462 -9.053  20.047 1.00 11.47  ? 144 PHE A HE1  1 
ATOM   2315 H  HE2  . PHE A 1 144 ? -13.903 -5.659  18.007 1.00 11.47  ? 144 PHE A HE2  1 
ATOM   2316 H  HZ   . PHE A 1 144 ? -14.382 -7.921  18.031 1.00 11.47  ? 144 PHE A HZ   1 
ATOM   2317 N  N    . LEU A 1 145 ? -14.099 -4.756  25.548 1.00 8.28   ? 145 LEU A N    1 
ATOM   2318 C  CA   . LEU A 1 145 ? -13.431 -4.113  26.673 1.00 8.35   ? 145 LEU A CA   1 
ATOM   2319 C  C    . LEU A 1 145 ? -12.139 -4.882  26.859 1.00 8.06   ? 145 LEU A C    1 
ATOM   2320 O  O    . LEU A 1 145 ? -12.178 -6.071  27.180 1.00 8.94   ? 145 LEU A O    1 
ATOM   2321 C  CB   . LEU A 1 145 ? -14.271 -4.115  27.949 1.00 9.10   ? 145 LEU A CB   1 
ATOM   2322 C  CG   . LEU A 1 145 ? -15.685 -3.592  27.784 1.00 9.30   ? 145 LEU A CG   1 
ATOM   2323 C  CD1  . LEU A 1 145 ? -16.488 -3.813  29.052 1.00 10.48  ? 145 LEU A CD1  1 
ATOM   2324 C  CD2  . LEU A 1 145 ? -15.720 -2.154  27.340 1.00 10.79  ? 145 LEU A CD2  1 
ATOM   2325 H  H    . LEU A 1 145 ? -14.357 -5.629  25.632 1.00 10.12  ? 145 LEU A H    1 
ATOM   2326 H  HA   . LEU A 1 145 ? -13.215 -3.185  26.425 1.00 12.63  ? 145 LEU A HA   1 
ATOM   2327 H  HB2  . LEU A 1 145 ? -14.315 -5.030  28.291 1.00 10.85  ? 145 LEU A HB2  1 
ATOM   2328 H  HB3  . LEU A 1 145 ? -13.814 -3.570  28.621 1.00 10.85  ? 145 LEU A HB3  1 
ATOM   2329 H  HG   . LEU A 1 145 ? -16.112 -4.128  27.073 1.00 11.28  ? 145 LEU A HG   1 
ATOM   2330 H  HD11 . LEU A 1 145 ? -17.396 -3.488  28.922 1.00 12.71  ? 145 LEU A HD11 1 
ATOM   2331 H  HD12 . LEU A 1 145 ? -16.512 -4.764  29.260 1.00 12.71  ? 145 LEU A HD12 1 
ATOM   2332 H  HD13 . LEU A 1 145 ? -16.074 -3.331  29.788 1.00 12.71  ? 145 LEU A HD13 1 
ATOM   2333 H  HD21 . LEU A 1 145 ? -16.635 -1.825  27.376 1.00 12.66  ? 145 LEU A HD21 1 
ATOM   2334 H  HD22 . LEU A 1 145 ? -15.161 -1.618  27.929 1.00 12.66  ? 145 LEU A HD22 1 
ATOM   2335 H  HD23 . LEU A 1 145 ? -15.388 -2.086  26.429 1.00 12.66  ? 145 LEU A HD23 1 
ATOM   2336 N  N    . THR A 1 146 ? -11.007 -4.242  26.590 1.00 8.48   ? 146 THR A N    1 
ATOM   2337 C  CA   . THR A 1 146 ? -9.710  -4.901  26.731 1.00 8.51   ? 146 THR A CA   1 
ATOM   2338 C  C    . THR A 1 146 ? -9.066  -4.401  28.009 1.00 8.71   ? 146 THR A C    1 
ATOM   2339 O  O    . THR A 1 146 ? -9.159  -3.220  28.337 1.00 9.88   ? 146 THR A O    1 
ATOM   2340 C  CB   . THR A 1 146 ? -8.859  -4.735  25.459 1.00 9.38   ? 146 THR A CB   1 
ATOM   2341 O  OG1  . THR A 1 146 ? -8.442  -3.397  25.260 1.00 9.55   ? 146 THR A OG1  1 
ATOM   2342 C  CG2  . THR A 1 146 ? -9.557  -5.302  24.232 1.00 11.01  ? 146 THR A CG2  1 
ATOM   2343 H  H    . THR A 1 146 ? -11.033 -3.373  26.309 1.00 12.63  ? 146 THR A H    1 
ATOM   2344 H  HA   . THR A 1 146 ? -9.883  -5.864  26.843 1.00 10.49  ? 146 THR A HA   1 
ATOM   2345 H  HB   . THR A 1 146 ? -8.044  -5.273  25.598 1.00 11.75  ? 146 THR A HB   1 
ATOM   2346 H  HG1  . THR A 1 146 ? -9.088  -2.942  24.950 1.00 12.63  ? 146 THR A HG1  1 
ATOM   2347 H  HG21 . THR A 1 146 ? -8.952  -5.271  23.470 1.00 13.29  ? 146 THR A HG21 1 
ATOM   2348 H  HG22 . THR A 1 146 ? -9.816  -6.226  24.401 1.00 13.29  ? 146 THR A HG22 1 
ATOM   2349 H  HG23 . THR A 1 146 ? -10.351 -4.774  24.035 1.00 13.29  ? 146 THR A HG23 1 
ATOM   2350 N  N    . TRP A 1 147 ? -8.448  -5.320  28.739 1.00 8.83   ? 147 TRP A N    1 
ATOM   2351 C  CA   . TRP A 1 147 ? -7.893  -5.053  30.055 1.00 9.13   ? 147 TRP A CA   1 
ATOM   2352 C  C    . TRP A 1 147 ? -6.467  -5.565  30.104 1.00 8.72   ? 147 TRP A C    1 
ATOM   2353 O  O    . TRP A 1 147 ? -6.217  -6.690  29.682 1.00 9.35   ? 147 TRP A O    1 
ATOM   2354 C  CB   . TRP A 1 147 ? -8.737  -5.779  31.115 1.00 9.53   ? 147 TRP A CB   1 
ATOM   2355 C  CG   . TRP A 1 147 ? -8.214  -5.668  32.519 1.00 9.92   ? 147 TRP A CG   1 
ATOM   2356 C  CD1  . TRP A 1 147 ? -7.498  -6.597  33.214 1.00 11.04  ? 147 TRP A CD1  1 
ATOM   2357 C  CD2  . TRP A 1 147 ? -8.313  -4.533  33.383 1.00 9.97   ? 147 TRP A CD2  1 
ATOM   2358 N  NE1  . TRP A 1 147 ? -7.182  -6.143  34.466 1.00 11.36  ? 147 TRP A NE1  1 
ATOM   2359 C  CE2  . TRP A 1 147 ? -7.697  -4.886  34.608 1.00 11.05  ? 147 TRP A CE2  1 
ATOM   2360 C  CE3  . TRP A 1 147 ? -8.901  -3.276  33.276 1.00 11.00  ? 147 TRP A CE3  1 
ATOM   2361 C  CZ2  . TRP A 1 147 ? -7.666  -4.017  35.692 1.00 11.71  ? 147 TRP A CZ2  1 
ATOM   2362 C  CZ3  . TRP A 1 147 ? -8.837  -2.410  34.342 1.00 12.32  ? 147 TRP A CZ3  1 
ATOM   2363 C  CH2  . TRP A 1 147 ? -8.222  -2.774  35.536 1.00 11.90  ? 147 TRP A CH2  1 
ATOM   2364 H  H    . TRP A 1 147 ? -8.361  -6.164  28.399 1.00 10.49  ? 147 TRP A H    1 
ATOM   2365 H  HA   . TRP A 1 147 ? -7.914  -4.086  30.230 1.00 10.94  ? 147 TRP A HA   1 
ATOM   2366 H  HB2  . TRP A 1 147 ? -9.645  -5.413  31.084 1.00 11.48  ? 147 TRP A HB2  1 
ATOM   2367 H  HB3  . TRP A 1 147 ? -8.789  -6.725  30.869 1.00 11.48  ? 147 TRP A HB3  1 
ATOM   2368 H  HD1  . TRP A 1 147 ? -7.278  -7.458  32.892 1.00 14.01  ? 147 TRP A HD1  1 
ATOM   2369 H  HE1  . TRP A 1 147 ? -6.764  -6.601  35.085 1.00 14.01  ? 147 TRP A HE1  1 
ATOM   2370 H  HE3  . TRP A 1 147 ? -9.342  -3.024  32.480 1.00 14.01  ? 147 TRP A HE3  1 
ATOM   2371 H  HZ2  . TRP A 1 147 ? -7.209  -4.249  36.481 1.00 14.01  ? 147 TRP A HZ2  1 
ATOM   2372 H  HZ3  . TRP A 1 147 ? -9.246  -1.562  34.275 1.00 14.01  ? 147 TRP A HZ3  1 
ATOM   2373 H  HH2  . TRP A 1 147 ? -8.195  -2.162  36.250 1.00 14.01  ? 147 TRP A HH2  1 
ATOM   2374 N  N    . PHE A 1 148 ? -5.549  -4.744  30.623 1.00 8.82   ? 148 PHE A N    1 
ATOM   2375 C  CA   . PHE A 1 148 ? -4.140  -5.079  30.663 1.00 9.19   ? 148 PHE A CA   1 
ATOM   2376 C  C    . PHE A 1 148 ? -3.585  -4.719  32.029 1.00 9.19   ? 148 PHE A C    1 
ATOM   2377 O  O    . PHE A 1 148 ? -4.009  -3.757  32.650 1.00 9.85   ? 148 PHE A O    1 
ATOM   2378 C  CB   . PHE A 1 148 ? -3.377  -4.301  29.588 1.00 9.53   ? 148 PHE A CB   1 
ATOM   2379 C  CG   . PHE A 1 148 ? -3.970  -4.500  28.231 1.00 9.45   ? 148 PHE A CG   1 
ATOM   2380 C  CD1  . PHE A 1 148 ? -3.650  -5.626  27.490 1.00 9.66   ? 148 PHE A CD1  1 
ATOM   2381 C  CD2  . PHE A 1 148 ? -4.932  -3.633  27.740 1.00 9.86   ? 148 PHE A CD2  1 
ATOM   2382 C  CE1  . PHE A 1 148 ? -4.279  -5.889  26.287 1.00 10.33  ? 148 PHE A CE1  1 
ATOM   2383 C  CE2  . PHE A 1 148 ? -5.572  -3.882  26.536 1.00 10.39  ? 148 PHE A CE2  1 
ATOM   2384 C  CZ   . PHE A 1 148 ? -5.247  -5.010  25.810 1.00 10.67  ? 148 PHE A CZ   1 
ATOM   2385 H  H    . PHE A 1 148 ? -5.816  -3.940  30.967 1.00 10.94  ? 148 PHE A H    1 
ATOM   2386 H  HA   . PHE A 1 148 ? -4.029  -6.048  30.511 1.00 11.38  ? 148 PHE A HA   1 
ATOM   2387 H  HB2  . PHE A 1 148 ? -3.393  -3.347  29.814 1.00 12.09  ? 148 PHE A HB2  1 
ATOM   2388 H  HB3  . PHE A 1 148 ? -2.443  -4.599  29.582 1.00 12.09  ? 148 PHE A HB3  1 
ATOM   2389 H  HD1  . PHE A 1 148 ? -3.024  -6.243  27.832 1.00 18.56  ? 148 PHE A HD1  1 
ATOM   2390 H  HD2  . PHE A 1 148 ? -5.183  -2.882  28.254 1.00 18.56  ? 148 PHE A HD2  1 
ATOM   2391 H  HE1  . PHE A 1 148 ? -4.039  -6.651  25.784 1.00 18.56  ? 148 PHE A HE1  1 
ATOM   2392 H  HE2  . PHE A 1 148 ? -6.210  -3.272  26.206 1.00 18.56  ? 148 PHE A HE2  1 
ATOM   2393 H  HZ   . PHE A 1 148 ? -5.644  -5.157  24.969 1.00 18.56  ? 148 PHE A HZ   1 
ATOM   2394 N  N    . GLU A 1 149 ? -2.567  -5.490  32.465 1.00 9.53   ? 149 GLU A N    1 
ATOM   2395 C  CA   . GLU A 1 149 ? -1.862  -5.210  33.721 1.00 9.86   ? 149 GLU A CA   1 
ATOM   2396 C  C    . GLU A 1 149 ? -0.361  -5.377  33.484 1.00 9.89   ? 149 GLU A C    1 
ATOM   2397 O  O    . GLU A 1 149 ? 0.069   -6.310  32.808 1.00 10.54  ? 149 GLU A O    1 
ATOM   2398 C  CB   . GLU A 1 149 ? -2.265  -6.165  34.832 1.00 11.08  ? 149 GLU A CB   1 
ATOM   2399 C  CG   . GLU A 1 149 ? -3.752  -6.192  35.116 1.00 11.95  ? 149 GLU A CG   1 
ATOM   2400 C  CD   . GLU A 1 149 ? -4.192  -7.291  36.059 1.00 13.70  ? 149 GLU A CD   1 
ATOM   2401 O  OE1  . GLU A 1 149 ? -3.334  -8.105  36.487 1.00 17.11  ? 149 GLU A OE1  1 
ATOM   2402 O  OE2  . GLU A 1 149 ? -5.392  -7.309  36.367 1.00 14.28  ? 149 GLU A OE2  1 
ATOM   2403 H  H    . GLU A 1 149 ? -2.305  -6.210  31.966 1.00 11.38  ? 149 GLU A H    1 
ATOM   2404 H  HA   . GLU A 1 149 ? -2.049  -4.286  33.998 1.00 12.07  ? 149 GLU A HA   1 
ATOM   2405 H  HB2  . GLU A 1 149 ? -1.973  -7.068  34.586 1.00 13.44  ? 149 GLU A HB2  1 
ATOM   2406 H  HB3  . GLU A 1 149 ? -1.791  -5.909  35.650 1.00 13.44  ? 149 GLU A HB3  1 
ATOM   2407 H  HG2  . GLU A 1 149 ? -4.018  -5.329  35.501 1.00 14.48  ? 149 GLU A HG2  1 
ATOM   2408 H  HG3  . GLU A 1 149 ? -4.237  -6.301  34.271 1.00 14.48  ? 149 GLU A HG3  1 
ATOM   2409 N  N    . TYR A 1 150 ? 0.435   -4.475  34.085 1.00 10.16  ? 150 TYR A N    1 
ATOM   2410 C  CA   . TYR A 1 150 ? 1.871   -4.497  33.898 1.00 10.59  ? 150 TYR A CA   1 
ATOM   2411 C  C    . TYR A 1 150 ? 2.509   -3.713  35.029 1.00 10.70  ? 150 TYR A C    1 
ATOM   2412 O  O    . TYR A 1 150 ? 1.887   -2.879  35.683 1.00 11.54  ? 150 TYR A O    1 
ATOM   2413 C  CB   . TYR A 1 150 ? 2.260   -3.990  32.497 1.00 10.83  ? 150 TYR A CB   1 
ATOM   2414 C  CG   . TYR A 1 150 ? 1.559   -2.721  32.087 1.00 10.69  ? 150 TYR A CG   1 
ATOM   2415 C  CD1  . TYR A 1 150 ? 2.054   -1.465  32.414 1.00 10.97  ? 150 TYR A CD1  1 
ATOM   2416 C  CD2  . TYR A 1 150 ? 0.355   -2.794  31.401 1.00 11.00  ? 150 TYR A CD2  1 
ATOM   2417 C  CE1  . TYR A 1 150 ? 1.351   -0.323  32.082 1.00 11.02  ? 150 TYR A CE1  1 
ATOM   2418 C  CE2  . TYR A 1 150 ? -0.354  -1.666  31.084 1.00 11.03  ? 150 TYR A CE2  1 
ATOM   2419 C  CZ   . TYR A 1 150 ? 0.142   -0.422  31.433 1.00 10.75  ? 150 TYR A CZ   1 
ATOM   2420 O  OH   . TYR A 1 150 ? -0.608  0.673   31.129 1.00 11.80  ? 150 TYR A OH   1 
ATOM   2421 H  H    . TYR A 1 150 ? 0.067   -3.833  34.623 1.00 12.07  ? 150 TYR A H    1 
ATOM   2422 H  HA   . TYR A 1 150 ? 2.175   -5.437  33.977 1.00 17.02  ? 150 TYR A HA   1 
ATOM   2423 H  HB2  . TYR A 1 150 ? 3.228   -3.838  32.480 1.00 13.25  ? 150 TYR A HB2  1 
ATOM   2424 H  HB3  . TYR A 1 150 ? 2.055   -4.692  31.845 1.00 13.25  ? 150 TYR A HB3  1 
ATOM   2425 H  HD1  . TYR A 1 150 ? 2.864   -1.391  32.890 1.00 12.71  ? 150 TYR A HD1  1 
ATOM   2426 H  HD2  . TYR A 1 150 ? -0.009  -3.639  31.195 1.00 12.71  ? 150 TYR A HD2  1 
ATOM   2427 H  HE1  . TYR A 1 150 ? 1.682   0.524   32.330 1.00 12.71  ? 150 TYR A HE1  1 
ATOM   2428 H  HE2  . TYR A 1 150 ? -1.182  -1.736  30.640 1.00 12.71  ? 150 TYR A HE2  1 
ATOM   2429 H  HH   . TYR A 1 150 ? -1.158  0.652   30.468 1.00 12.71  ? 150 TYR A HH   1 
ATOM   2430 N  N    . SER A 1 151 ? 3.814   -3.926  35.200 1.00 12.39  ? 151 SER A N    1 
ATOM   2431 C  CA   A SER A 1 151 ? 4.583   -3.139  36.140 0.50 12.72  ? 151 SER A CA   1 
ATOM   2432 C  CA   B SER A 1 151 ? 4.609   -3.145  36.131 0.50 12.99  ? 151 SER A CA   1 
ATOM   2433 C  C    . SER A 1 151 ? 4.831   -1.737  35.587 1.00 12.68  ? 151 SER A C    1 
ATOM   2434 O  O    . SER A 1 151 ? 4.916   -1.566  34.388 1.00 12.81  ? 151 SER A O    1 
ATOM   2435 C  CB   A SER A 1 151 ? 5.885   -3.819  36.391 0.50 13.89  ? 151 SER A CB   1 
ATOM   2436 C  CB   B SER A 1 151 ? 5.935   -3.839  36.377 0.50 14.37  ? 151 SER A CB   1 
ATOM   2437 O  OG   A SER A 1 151 ? 6.728   -3.627  35.275 0.50 16.68  ? 151 SER A OG   1 
ATOM   2438 O  OG   B SER A 1 151 ? 6.838   -2.999  37.075 0.50 18.02  ? 151 SER A OG   1 
ATOM   2439 H  H    . SER A 1 151 ? 4.231   -4.580  34.715 1.00 17.02  ? 151 SER A H    1 
ATOM   2440 H  HA   . SER A 1 151 ? 4.093   -3.076  36.992 1.00 15.78  ? 151 SER A HA   1 
ATOM   2441 H  HB2  A SER A 1 151 ? 6.306   -3.444  37.197 0.50 17.02  ? 151 SER A HB2  1 
ATOM   2442 H  HB2  B SER A 1 151 ? 5.781   -4.659  36.898 0.50 17.02  ? 151 SER A HB2  1 
ATOM   2443 H  HB3  A SER A 1 151 ? 5.735   -4.781  36.535 0.50 17.02  ? 151 SER A HB3  1 
ATOM   2444 H  HB3  B SER A 1 151 ? 6.332   -4.095  35.514 0.50 17.02  ? 151 SER A HB3  1 
ATOM   2445 H  HG   A SER A 1 151 ? 7.495   -3.929  35.463 0.50 24.65  ? 151 SER A HG   1 
ATOM   2446 H  HG   B SER A 1 151 ? 7.429   -3.484  37.438 0.50 24.65  ? 151 SER A HG   1 
ATOM   2447 N  N    . PRO A 1 152 ? 5.048   -0.734  36.463 1.00 13.30  ? 152 PRO A N    1 
ATOM   2448 C  CA   . PRO A 1 152 ? 5.375   0.593   35.960 1.00 13.67  ? 152 PRO A CA   1 
ATOM   2449 C  C    . PRO A 1 152 ? 6.621   0.608   35.083 1.00 14.33  ? 152 PRO A C    1 
ATOM   2450 O  O    . PRO A 1 152 ? 6.729   1.430   34.175 1.00 15.59  ? 152 PRO A O    1 
ATOM   2451 C  CB   . PRO A 1 152 ? 5.479   1.474   37.211 1.00 16.31  ? 152 PRO A CB   1 
ATOM   2452 C  CG   . PRO A 1 152 ? 5.263   0.599   38.392 1.00 16.86  ? 152 PRO A CG   1 
ATOM   2453 C  CD   . PRO A 1 152 ? 4.811   -0.750  37.914 1.00 14.19  ? 152 PRO A CD   1 
ATOM   2454 H  HA   . PRO A 1 152 ? 4.609   0.913   35.422 1.00 16.49  ? 152 PRO A HA   1 
ATOM   2455 H  HB2  . PRO A 1 152 ? 6.363   1.897   37.259 1.00 18.52  ? 152 PRO A HB2  1 
ATOM   2456 H  HB3  . PRO A 1 152 ? 4.801   2.183   37.185 1.00 18.52  ? 152 PRO A HB3  1 
ATOM   2457 H  HG2  . PRO A 1 152 ? 6.094   0.512   38.902 1.00 18.98  ? 152 PRO A HG2  1 
ATOM   2458 H  HG3  . PRO A 1 152 ? 4.585   0.990   38.980 1.00 18.98  ? 152 PRO A HG3  1 
ATOM   2459 H  HD2  . PRO A 1 152 ? 5.326   -1.458  38.344 1.00 16.83  ? 152 PRO A HD2  1 
ATOM   2460 H  HD3  . PRO A 1 152 ? 3.866   -0.888  38.108 1.00 16.83  ? 152 PRO A HD3  1 
ATOM   2461 N  N    . SER A 1 153 ? 7.587   -0.302  35.322 1.00 13.98  ? 153 SER A N    1 
ATOM   2462 C  CA   . SER A 1 153 ? 8.788   -0.324  34.498 1.00 16.15  ? 153 SER A CA   1 
ATOM   2463 C  C    . SER A 1 153 ? 8.493   -0.769  33.072 1.00 14.68  ? 153 SER A C    1 
ATOM   2464 O  O    . SER A 1 153 ? 9.357   -0.563  32.226 1.00 15.50  ? 153 SER A O    1 
ATOM   2465 C  CB   . SER A 1 153 ? 9.852   -1.155  35.116 1.00 19.52  ? 153 SER A CB   1 
ATOM   2466 O  OG   . SER A 1 153 ? 9.448   -2.487  35.228 1.00 23.45  ? 153 SER A OG   1 
ATOM   2467 H  H    . SER A 1 153 ? 7.501   -0.902  36.007 1.00 16.96  ? 153 SER A H    1 
ATOM   2468 H  HA   . SER A 1 153 ? 9.128   0.608   34.451 1.00 36.51  ? 153 SER A HA   1 
ATOM   2469 H  HB2  . SER A 1 153 ? 10.666  -1.105  34.566 1.00 22.69  ? 153 SER A HB2  1 
ATOM   2470 H  HB3  . SER A 1 153 ? 10.065  -0.801  36.009 1.00 22.69  ? 153 SER A HB3  1 
ATOM   2471 H  HG   . SER A 1 153 ? 10.099  -2.941  35.522 1.00 25.97  ? 153 SER A HG   1 
ATOM   2472 N  N    . ASP A 1 154 ? 7.330   -1.388  32.849 1.00 13.26  ? 154 ASP A N    1 
ATOM   2473 C  CA   . ASP A 1 154 ? 6.928   -1.844  31.525 1.00 12.64  ? 154 ASP A CA   1 
ATOM   2474 C  C    . ASP A 1 154 ? 5.935   -0.917  30.839 1.00 12.59  ? 154 ASP A C    1 
ATOM   2475 O  O    . ASP A 1 154 ? 5.430   -1.253  29.769 1.00 12.88  ? 154 ASP A O    1 
ATOM   2476 C  CB   . ASP A 1 154 ? 6.424   -3.281  31.616 1.00 12.94  ? 154 ASP A CB   1 
ATOM   2477 C  CG   . ASP A 1 154 ? 7.550   -4.266  31.934 1.00 13.35  ? 154 ASP A CG   1 
ATOM   2478 O  OD1  . ASP A 1 154 ? 8.628   -4.096  31.370 1.00 15.30  ? 154 ASP A OD1  1 
ATOM   2479 O  OD2  . ASP A 1 154 ? 7.304   -5.197  32.720 1.00 15.53  ? 154 ASP A OD2  1 
ATOM   2480 H  H    . ASP A 1 154 ? 6.771   -1.554  33.551 1.00 15.75  ? 154 ASP A H    1 
ATOM   2481 H  HA   . ASP A 1 154 ? 7.737   -1.864  30.965 1.00 14.97  ? 154 ASP A HA   1 
ATOM   2482 H  HB2  . ASP A 1 154 ? 5.745   -3.343  32.318 1.00 15.75  ? 154 ASP A HB2  1 
ATOM   2483 H  HB3  . ASP A 1 154 ? 6.015   -3.540  30.766 1.00 15.75  ? 154 ASP A HB3  1 
ATOM   2484 N  N    . GLU A 1 155 ? 5.661   0.245   31.436 1.00 13.29  ? 155 GLU A N    1 
ATOM   2485 C  CA   . GLU A 1 155 ? 4.692   1.143   30.827 1.00 13.46  ? 155 GLU A CA   1 
ATOM   2486 C  C    . GLU A 1 155 ? 5.162   1.644   29.460 1.00 12.93  ? 155 GLU A C    1 
ATOM   2487 O  O    . GLU A 1 155 ? 4.363   1.718   28.524 1.00 13.72  ? 155 GLU A O    1 
ATOM   2488 C  CB   . GLU A 1 155 ? 4.395   2.304   31.773 1.00 15.38  ? 155 GLU A CB   1 
ATOM   2489 C  CG   . GLU A 1 155 ? 3.428   3.313   31.214 1.00 17.03  ? 155 GLU A CG   1 
ATOM   2490 C  CD   . GLU A 1 155 ? 3.145   4.459   32.170 1.00 19.05  ? 155 GLU A CD   1 
ATOM   2491 O  OE1  . GLU A 1 155 ? 4.105   5.027   32.728 1.00 25.49  ? 155 GLU A OE1  1 
ATOM   2492 O  OE2  . GLU A 1 155 ? 2.013   4.883   32.233 1.00 19.95  ? 155 GLU A OE2  1 
ATOM   2493 H  H    . GLU A 1 155 ? 6.071   0.484   32.217 1.00 17.58  ? 155 GLU A H    1 
ATOM   2494 H  HA   . GLU A 1 155 ? 3.857   0.637   30.694 1.00 15.90  ? 155 GLU A HA   1 
ATOM   2495 H  HB2  . GLU A 1 155 ? 4.028   1.941   32.606 1.00 17.75  ? 155 GLU A HB2  1 
ATOM   2496 H  HB3  . GLU A 1 155 ? 5.238   2.755   31.986 1.00 17.75  ? 155 GLU A HB3  1 
ATOM   2497 H  HG2  . GLU A 1 155 ? 3.790   3.684   30.382 1.00 19.21  ? 155 GLU A HG2  1 
ATOM   2498 H  HG3  . GLU A 1 155 ? 2.582   2.866   31.000 1.00 19.21  ? 155 GLU A HG3  1 
ATOM   2499 N  N    . THR A 1 156 ? 6.443   2.002   29.340 1.00 13.63  ? 156 THR A N    1 
ATOM   2500 C  CA   . THR A 1 156 ? 6.921   2.481   28.059 1.00 14.43  ? 156 THR A CA   1 
ATOM   2501 C  C    . THR A 1 156 ? 6.771   1.391   26.987 1.00 14.13  ? 156 THR A C    1 
ATOM   2502 O  O    . THR A 1 156 ? 6.392   1.668   25.844 1.00 14.10  ? 156 THR A O    1 
ATOM   2503 C  CB   . THR A 1 156 ? 8.356   3.003   28.194 1.00 16.08  ? 156 THR A CB   1 
ATOM   2504 O  OG1  . THR A 1 156 ? 8.341   4.108   29.094 1.00 19.35  ? 156 THR A OG1  1 
ATOM   2505 C  CG2  . THR A 1 156 ? 8.927   3.472   26.889 1.00 17.57  ? 156 THR A CG2  1 
ATOM   2506 H  H    . THR A 1 156 ? 7.016   1.952   30.051 1.00 14.97  ? 156 THR A H    1 
ATOM   2507 H  HA   . THR A 1 156 ? 6.349   3.240   27.799 1.00 16.62  ? 156 THR A HA   1 
ATOM   2508 H  HB   . THR A 1 156 ? 8.924   2.286   28.562 1.00 14.97  ? 156 THR A HB   1 
ATOM   2509 H  HG1  . THR A 1 156 ? 8.487   3.834   29.883 1.00 14.97  ? 156 THR A HG1  1 
ATOM   2510 H  HG21 . THR A 1 156 ? 9.777   3.919   27.049 1.00 17.92  ? 156 THR A HG21 1 
ATOM   2511 H  HG22 . THR A 1 156 ? 9.068   2.710   26.300 1.00 17.93  ? 156 THR A HG22 1 
ATOM   2512 H  HG23 . THR A 1 156 ? 8.309   4.096   26.469 1.00 17.91  ? 156 THR A HG23 1 
ATOM   2513 N  N    . ALA A 1 157 ? 7.052   0.136   27.357 1.00 13.65  ? 157 ALA A N    1 
ATOM   2514 C  CA   . ALA A 1 157 ? 6.856   -0.991  26.458 1.00 13.99  ? 157 ALA A CA   1 
ATOM   2515 C  C    . ALA A 1 157 ? 5.382   -1.126  26.037 1.00 12.98  ? 157 ALA A C    1 
ATOM   2516 O  O    . ALA A 1 157 ? 5.085   -1.316  24.870 1.00 13.31  ? 157 ALA A O    1 
ATOM   2517 C  CB   . ALA A 1 157 ? 7.357   -2.278  27.094 1.00 14.93  ? 157 ALA A CB   1 
ATOM   2518 H  H    . ALA A 1 157 ? 7.384   -0.022  28.195 1.00 16.31  ? 157 ALA A H    1 
ATOM   2519 H  HA   . ALA A 1 157 ? 7.386   -0.824  25.646 1.00 16.98  ? 157 ALA A HA   1 
ATOM   2520 H  HB1  . ALA A 1 157 ? 7.268   -3.010  26.460 1.00 17.35  ? 157 ALA A HB1  1 
ATOM   2521 H  HB2  . ALA A 1 157 ? 8.291   -2.177  27.341 1.00 17.35  ? 157 ALA A HB2  1 
ATOM   2522 H  HB3  . ALA A 1 157 ? 6.833   -2.474  27.888 1.00 17.35  ? 157 ALA A HB3  1 
ATOM   2523 N  N    . PHE A 1 158 ? 4.475   -1.037  26.999 1.00 11.82  ? 158 PHE A N    1 
ATOM   2524 C  CA   . PHE A 1 158 ? 3.050   -1.124  26.691 1.00 11.70  ? 158 PHE A CA   1 
ATOM   2525 C  C    . PHE A 1 158 ? 2.668   -0.035  25.671 1.00 11.06  ? 158 PHE A C    1 
ATOM   2526 O  O    . PHE A 1 158 ? 1.894   -0.277  24.747 1.00 11.54  ? 158 PHE A O    1 
ATOM   2527 C  CB   . PHE A 1 158 ? 2.228   -0.991  27.972 1.00 11.17  ? 158 PHE A CB   1 
ATOM   2528 C  CG   . PHE A 1 158 ? 0.751   -1.120  27.763 1.00 10.21  ? 158 PHE A CG   1 
ATOM   2529 C  CD1  . PHE A 1 158 ? 0.208   -2.343  27.425 1.00 10.63  ? 158 PHE A CD1  1 
ATOM   2530 C  CD2  . PHE A 1 158 ? -0.097  -0.043  27.895 1.00 10.56  ? 158 PHE A CD2  1 
ATOM   2531 C  CE1  . PHE A 1 158 ? -1.154  -2.498  27.220 1.00 10.69  ? 158 PHE A CE1  1 
ATOM   2532 C  CE2  . PHE A 1 158 ? -1.456  -0.200  27.702 1.00 10.50  ? 158 PHE A CE2  1 
ATOM   2533 C  CZ   . PHE A 1 158 ? -1.982  -1.419  27.373 1.00 10.57  ? 158 PHE A CZ   1 
ATOM   2534 H  H    . PHE A 1 158 ? 4.738   -0.925  27.867 1.00 13.72  ? 158 PHE A H    1 
ATOM   2535 H  HA   . PHE A 1 158 ? 2.867   -2.010  26.287 1.00 14.31  ? 158 PHE A HA   1 
ATOM   2536 H  HB2  . PHE A 1 158 ? 2.521   -1.681  28.603 1.00 13.62  ? 158 PHE A HB2  1 
ATOM   2537 H  HB3  . PHE A 1 158 ? 2.418   -0.117  28.374 1.00 13.62  ? 158 PHE A HB3  1 
ATOM   2538 H  HD1  . PHE A 1 158 ? 0.778   -3.088  27.327 1.00 13.62  ? 158 PHE A HD1  1 
ATOM   2539 H  HD2  . PHE A 1 158 ? 0.251   0.802   28.131 1.00 13.62  ? 158 PHE A HD2  1 
ATOM   2540 H  HE1  . PHE A 1 158 ? -1.508  -3.343  26.994 1.00 13.62  ? 158 PHE A HE1  1 
ATOM   2541 H  HE2  . PHE A 1 158 ? -2.028  0.544   27.798 1.00 13.62  ? 158 PHE A HE2  1 
ATOM   2542 H  HZ   . PHE A 1 158 ? -2.911  -1.511  27.234 1.00 13.62  ? 158 PHE A HZ   1 
ATOM   2543 N  N    . ASN A 1 159 ? 3.195   1.185   25.850 1.00 11.51  ? 159 ASN A N    1 
ATOM   2544 C  CA   . ASN A 1 159 ? 2.907   2.243   24.910 1.00 12.68  ? 159 ASN A CA   1 
ATOM   2545 C  C    . ASN A 1 159 ? 3.401   1.904   23.504 1.00 13.20  ? 159 ASN A C    1 
ATOM   2546 O  O    . ASN A 1 159 ? 2.778   2.260   22.507 1.00 13.56  ? 159 ASN A O    1 
ATOM   2547 C  CB   . ASN A 1 159 ? 3.442   3.575   25.415 1.00 13.25  ? 159 ASN A CB   1 
ATOM   2548 C  CG   . ASN A 1 159 ? 2.760   4.070   26.685 1.00 13.44  ? 159 ASN A CG   1 
ATOM   2549 O  OD1  . ASN A 1 159 ? 1.662   3.641   27.035 1.00 13.83  ? 159 ASN A OD1  1 
ATOM   2550 N  ND2  . ASN A 1 159 ? 3.411   4.972   27.403 1.00 15.20  ? 159 ASN A ND2  1 
ATOM   2551 H  H    . ASN A 1 159 ? 3.736   1.355   26.568 1.00 16.35  ? 159 ASN A H    1 
ATOM   2552 H  HA   . ASN A 1 159 ? 1.926   2.333   24.863 1.00 15.38  ? 159 ASN A HA   1 
ATOM   2553 H  HB2  . ASN A 1 159 ? 4.401   3.483   25.586 1.00 16.80  ? 159 ASN A HB2  1 
ATOM   2554 H  HB3  . ASN A 1 159 ? 3.326   4.246   24.712 1.00 16.80  ? 159 ASN A HB3  1 
ATOM   2555 H  HD21 . ASN A 1 159 ? 4.194   5.276   27.127 1.00 16.80  ? 159 ASN A HD21 1 
ATOM   2556 H  HD22 . ASN A 1 159 ? 3.063   5.270   28.159 1.00 16.80  ? 159 ASN A HD22 1 
ATOM   2557 N  N    . ARG A 1 160 ? 4.578   1.260   23.420 1.00 13.08  ? 160 ARG A N    1 
ATOM   2558 C  CA   . ARG A 1 160 ? 5.101   0.835   22.136 1.00 14.56  ? 160 ARG A CA   1 
ATOM   2559 C  C    . ARG A 1 160 ? 4.161   -0.187  21.492 1.00 14.04  ? 160 ARG A C    1 
ATOM   2560 O  O    . ARG A 1 160 ? 3.918   -0.134  20.289 1.00 14.70  ? 160 ARG A O    1 
ATOM   2561 C  CB   . ARG A 1 160 ? 6.514   0.239   22.240 1.00 16.13  ? 160 ARG A CB   1 
ATOM   2562 C  CG   . ARG A 1 160 ? 7.629   1.162   22.715 1.00 18.90  ? 160 ARG A CG   1 
ATOM   2563 C  CD   . ARG A 1 160 ? 9.074   0.670   22.512 1.00 18.90  ? 160 ARG A CD   1 
ATOM   2564 N  NE   . ARG A 1 160 ? 9.382   -0.633  23.103 1.00 17.83  ? 160 ARG A NE   1 
ATOM   2565 C  CZ   . ARG A 1 160 ? 9.781   -0.927  24.351 1.00 19.16  ? 160 ARG A CZ   1 
ATOM   2566 N  NH1  . ARG A 1 160 ? 10.163  -0.010  25.220 1.00 19.70  ? 160 ARG A NH1  1 
ATOM   2567 N  NH2  . ARG A 1 160 ? 9.837   -2.205  24.699 1.00 21.24  ? 160 ARG A NH2  1 
ATOM   2568 H  H    . ARG A 1 160 ? 5.063   1.093   24.176 1.00 16.01  ? 160 ARG A H    1 
ATOM   2569 H  HA   . ARG A 1 160 ? 5.143   1.625   21.550 1.00 17.24  ? 160 ARG A HA   1 
ATOM   2570 H  HB2  . ARG A 1 160 ? 6.474   -0.528  22.848 1.00 18.90  ? 160 ARG A HB2  1 
ATOM   2571 H  HB3  . ARG A 1 160 ? 6.761   -0.104  21.356 1.00 18.90  ? 160 ARG A HB3  1 
ATOM   2572 H  HG2  . ARG A 1 160 ? 7.533   2.022   22.254 1.00 21.35  ? 160 ARG A HG2  1 
ATOM   2573 H  HG3  . ARG A 1 160 ? 7.500   1.333   23.671 1.00 21.35  ? 160 ARG A HG3  1 
ATOM   2574 H  HD2  . ARG A 1 160 ? 9.255   0.626   21.549 1.00 19.02  ? 160 ARG A HD2  1 
ATOM   2575 H  HD3  . ARG A 1 160 ? 9.686   1.337   22.892 1.00 19.02  ? 160 ARG A HD3  1 
ATOM   2576 H  HE   . ARG A 1 160 ? 9.295   -1.316  22.568 1.00 19.04  ? 160 ARG A HE   1 
ATOM   2577 H  HH11 . ARG A 1 160 ? 9.782   0.784   25.216 1.00 18.72  ? 160 ARG A HH11 1 
ATOM   2578 H  HH12 . ARG A 1 160 ? 10.796  -0.195  25.804 1.00 18.74  ? 160 ARG A HH12 1 
ATOM   2579 H  HH21 . ARG A 1 160 ? 9.282   -2.783  24.337 1.00 19.04  ? 160 ARG A HH21 1 
ATOM   2580 H  HH22 . ARG A 1 160 ? 10.428  -2.471  25.293 1.00 19.03  ? 160 ARG A HH22 1 
ATOM   2581 N  N    . LEU A 1 161 ? 3.661   -1.154  22.278 1.00 12.65  ? 161 LEU A N    1 
ATOM   2582 C  CA   . LEU A 1 161 ? 2.704   -2.121  21.772 1.00 12.15  ? 161 LEU A CA   1 
ATOM   2583 C  C    . LEU A 1 161 ? 1.487   -1.418  21.179 1.00 12.27  ? 161 LEU A C    1 
ATOM   2584 O  O    . LEU A 1 161 ? 1.052   -1.748  20.075 1.00 12.42  ? 161 LEU A O    1 
ATOM   2585 C  CB   . LEU A 1 161 ? 2.302   -3.057  22.923 1.00 11.90  ? 161 LEU A CB   1 
ATOM   2586 C  CG   . LEU A 1 161 ? 1.058   -3.907  22.733 1.00 12.38  ? 161 LEU A CG   1 
ATOM   2587 C  CD1  . LEU A 1 161 ? 1.166   -4.875  21.566 1.00 13.07  ? 161 LEU A CD1  1 
ATOM   2588 C  CD2  . LEU A 1 161 ? 0.749   -4.626  24.030 1.00 12.75  ? 161 LEU A CD2  1 
ATOM   2589 H  H    . LEU A 1 161 ? 3.934   -1.214  23.149 1.00 14.96  ? 161 LEU A H    1 
ATOM   2590 H  HA   . LEU A 1 161 ? 3.141   -2.645  21.062 1.00 14.91  ? 161 LEU A HA   1 
ATOM   2591 H  HB2  . LEU A 1 161 ? 3.054   -3.657  23.098 1.00 14.96  ? 161 LEU A HB2  1 
ATOM   2592 H  HB3  . LEU A 1 161 ? 2.176   -2.513  23.725 1.00 14.96  ? 161 LEU A HB3  1 
ATOM   2593 H  HG   . LEU A 1 161 ? 0.303   -3.297  22.547 1.00 14.92  ? 161 LEU A HG   1 
ATOM   2594 H  HD11 . LEU A 1 161 ? 0.313   -5.327  21.439 1.00 15.32  ? 161 LEU A HD11 1 
ATOM   2595 H  HD12 . LEU A 1 161 ? 1.396   -4.386  20.757 1.00 15.32  ? 161 LEU A HD12 1 
ATOM   2596 H  HD13 . LEU A 1 161 ? 1.856   -5.534  21.753 1.00 15.32  ? 161 LEU A HD13 1 
ATOM   2597 H  HD21 . LEU A 1 161 ? -0.073  -5.136  23.930 1.00 14.96  ? 161 LEU A HD21 1 
ATOM   2598 H  HD22 . LEU A 1 161 ? 1.481   -5.230  24.249 1.00 14.96  ? 161 LEU A HD22 1 
ATOM   2599 H  HD23 . LEU A 1 161 ? 0.641   -3.975  24.746 1.00 14.96  ? 161 LEU A HD23 1 
ATOM   2600 N  N    . LEU A 1 162 ? 0.927   -0.472  21.926 1.00 11.68  ? 162 LEU A N    1 
ATOM   2601 C  CA   . LEU A 1 162 ? -0.258  0.231   21.436 1.00 12.02  ? 162 LEU A CA   1 
ATOM   2602 C  C    . LEU A 1 162 ? 0.035   0.896   20.098 1.00 12.94  ? 162 LEU A C    1 
ATOM   2603 O  O    . LEU A 1 162 ? -0.800  0.884   19.192 1.00 13.39  ? 162 LEU A O    1 
ATOM   2604 C  CB   . LEU A 1 162 ? -0.720  1.276   22.432 1.00 12.11  ? 162 LEU A CB   1 
ATOM   2605 C  CG   . LEU A 1 162 ? -1.261  0.705   23.737 1.00 11.96  ? 162 LEU A CG   1 
ATOM   2606 C  CD1  . LEU A 1 162 ? -1.522  1.824   24.703 1.00 13.11  ? 162 LEU A CD1  1 
ATOM   2607 C  CD2  . LEU A 1 162 ? -2.495  -0.124  23.502 1.00 13.13  ? 162 LEU A CD2  1 
ATOM   2608 H  H    . LEU A 1 162 ? 1.273   -0.258  22.744 1.00 14.80  ? 162 LEU A H    1 
ATOM   2609 H  HA   . LEU A 1 162 ? -0.973  -0.431  21.302 1.00 15.46  ? 162 LEU A HA   1 
ATOM   2610 H  HB2  . LEU A 1 162 ? 0.033   1.866   22.636 1.00 14.88  ? 162 LEU A HB2  1 
ATOM   2611 H  HB3  . LEU A 1 162 ? -1.418  1.818   22.014 1.00 14.88  ? 162 LEU A HB3  1 
ATOM   2612 H  HG   . LEU A 1 162 ? -0.569  0.118   24.127 1.00 14.80  ? 162 LEU A HG   1 
ATOM   2613 H  HD11 . LEU A 1 162 ? -1.955  1.472   25.500 1.00 15.41  ? 162 LEU A HD11 1 
ATOM   2614 H  HD12 . LEU A 1 162 ? -0.679  2.242   24.950 1.00 15.41  ? 162 LEU A HD12 1 
ATOM   2615 H  HD13 . LEU A 1 162 ? -2.100  2.486   24.286 1.00 15.41  ? 162 LEU A HD13 1 
ATOM   2616 H  HD21 . LEU A 1 162 ? -2.929  -0.309  24.353 1.00 15.46  ? 162 LEU A HD21 1 
ATOM   2617 H  HD22 . LEU A 1 162 ? -3.108  0.363   22.925 1.00 15.46  ? 162 LEU A HD22 1 
ATOM   2618 H  HD23 . LEU A 1 162 ? -2.247  -0.962  23.077 1.00 15.46  ? 162 LEU A HD23 1 
ATOM   2619 N  N    . ALA A 1 163 ? 1.196   1.550   19.979 1.00 13.44  ? 163 ALA A N    1 
ATOM   2620 C  CA   . ALA A 1 163 ? 1.486   2.228   18.728 1.00 14.73  ? 163 ALA A CA   1 
ATOM   2621 C  C    . ALA A 1 163 ? 1.586   1.219   17.571 1.00 14.69  ? 163 ALA A C    1 
ATOM   2622 O  O    . ALA A 1 163 ? 1.154   1.478   16.454 1.00 15.70  ? 163 ALA A O    1 
ATOM   2623 C  CB   . ALA A 1 163 ? 2.759   3.043   18.865 1.00 16.53  ? 163 ALA A CB   1 
ATOM   2624 H  H    . ALA A 1 163 ? 1.799   1.578   20.666 1.00 16.51  ? 163 ALA A H    1 
ATOM   2625 H  HA   . ALA A 1 163 ? 0.742   2.846   18.534 1.00 17.68  ? 163 ALA A HA   1 
ATOM   2626 H  HB1  . ALA A 1 163 ? 3.004   3.412   17.999 1.00 18.13  ? 163 ALA A HB1  1 
ATOM   2627 H  HB2  . ALA A 1 163 ? 2.615   3.768   19.496 1.00 18.13  ? 163 ALA A HB2  1 
ATOM   2628 H  HB3  . ALA A 1 163 ? 3.477   2.473   19.187 1.00 18.13  ? 163 ALA A HB3  1 
ATOM   2629 N  N    . GLU A 1 164 ? 2.172   0.051   17.812 1.00 13.88  ? 164 GLU A N    1 
ATOM   2630 C  CA   . GLU A 1 164 ? 2.233   -0.966  16.773 1.00 13.72  ? 164 GLU A CA   1 
ATOM   2631 C  C    . GLU A 1 164 ? 0.836   -1.384  16.326 1.00 13.45  ? 164 GLU A C    1 
ATOM   2632 O  O    . GLU A 1 164 ? 0.545   -1.432  15.136 1.00 14.19  ? 164 GLU A O    1 
ATOM   2633 C  CB   . GLU A 1 164 ? 3.006   -2.224  17.183 1.00 14.43  ? 164 GLU A CB   1 
ATOM   2634 C  CG   . GLU A 1 164 ? 4.484   -2.023  17.373 1.00 16.34  ? 164 GLU A CG   1 
ATOM   2635 C  CD   . GLU A 1 164 ? 5.244   -3.342  17.342 1.00 16.98  ? 164 GLU A CD   1 
ATOM   2636 O  OE1  . GLU A 1 164 ? 5.238   -3.985  16.266 1.00 18.90  ? 164 GLU A OE1  1 
ATOM   2637 O  OE2  . GLU A 1 164 ? 5.829   -3.732  18.378 1.00 19.13  ? 164 GLU A OE2  1 
ATOM   2638 H  H    . GLU A 1 164 ? 2.545   -0.119  18.629 1.00 17.37  ? 164 GLU A H    1 
ATOM   2639 H  HA   . GLU A 1 164 ? 2.692   -0.569  15.997 1.00 18.60  ? 164 GLU A HA   1 
ATOM   2640 H  HB2  . GLU A 1 164 ? 2.625   -2.561  18.020 1.00 17.40  ? 164 GLU A HB2  1 
ATOM   2641 H  HB3  . GLU A 1 164 ? 2.867   -2.909  16.496 1.00 17.40  ? 164 GLU A HB3  1 
ATOM   2642 H  HG2  . GLU A 1 164 ? 4.829   -1.440  16.664 1.00 18.60  ? 164 GLU A HG2  1 
ATOM   2643 H  HG3  . GLU A 1 164 ? 4.646   -1.583  18.234 1.00 18.60  ? 164 GLU A HG3  1 
ATOM   2644 N  N    . LEU A 1 165 ? -0.034  -1.718  17.273 1.00 12.45  ? 165 LEU A N    1 
ATOM   2645 C  CA   . LEU A 1 165 ? -1.362  -2.173  16.886 1.00 12.58  ? 165 LEU A CA   1 
ATOM   2646 C  C    . LEU A 1 165 ? -2.145  -1.049  16.200 1.00 12.76  ? 165 LEU A C    1 
ATOM   2647 O  O    . LEU A 1 165 ? -2.851  -1.287  15.213 1.00 12.95  ? 165 LEU A O    1 
ATOM   2648 C  CB   . LEU A 1 165 ? -2.125  -2.685  18.105 1.00 12.32  ? 165 LEU A CB   1 
ATOM   2649 C  CG   . LEU A 1 165 ? -1.534  -3.959  18.717 1.00 13.18  ? 165 LEU A CG   1 
ATOM   2650 C  CD1  . LEU A 1 165 ? -2.348  -4.342  19.952 1.00 14.92  ? 165 LEU A CD1  1 
ATOM   2651 C  CD2  . LEU A 1 165 ? -1.527  -5.115  17.748 1.00 16.00  ? 165 LEU A CD2  1 
ATOM   2652 H  H    . LEU A 1 165 ? 0.190   -1.668  18.157 1.00 15.08  ? 165 LEU A H    1 
ATOM   2653 H  HA   . LEU A 1 165 ? -1.255  -2.909  16.242 1.00 24.30  ? 165 LEU A HA   1 
ATOM   2654 H  HB2  . LEU A 1 165 ? -2.135  -1.983  18.786 1.00 15.03  ? 165 LEU A HB2  1 
ATOM   2655 H  HB3  . LEU A 1 165 ? -3.050  -2.862  17.843 1.00 15.03  ? 165 LEU A HB3  1 
ATOM   2656 H  HG   . LEU A 1 165 ? -0.603  -3.774  18.997 1.00 15.10  ? 165 LEU A HG   1 
ATOM   2657 H  HD11 . LEU A 1 165 ? -1.939  -5.111  20.385 1.00 23.30  ? 165 LEU A HD11 1 
ATOM   2658 H  HD12 . LEU A 1 165 ? -2.367  -3.593  20.572 1.00 23.29  ? 165 LEU A HD12 1 
ATOM   2659 H  HD13 . LEU A 1 165 ? -3.256  -4.565  19.685 1.00 23.29  ? 165 LEU A HD13 1 
ATOM   2660 H  HD21 . LEU A 1 165 ? -1.375  -5.945  18.233 1.00 24.29  ? 165 LEU A HD21 1 
ATOM   2661 H  HD22 . LEU A 1 165 ? -2.384  -5.160  17.291 1.00 24.33  ? 165 LEU A HD22 1 
ATOM   2662 H  HD23 . LEU A 1 165 ? -0.817  -4.989  17.095 1.00 24.31  ? 165 LEU A HD23 1 
ATOM   2663 N  N    . ARG A 1 166 ? -2.046  0.176   16.707 1.00 12.62  ? 166 ARG A N    1 
ATOM   2664 C  CA   . ARG A 1 166 ? -2.826  1.268   16.136 1.00 13.13  ? 166 ARG A CA   1 
ATOM   2665 C  C    . ARG A 1 166 ? -2.384  1.625   14.708 1.00 14.02  ? 166 ARG A C    1 
ATOM   2666 O  O    . ARG A 1 166 ? -3.159  2.230   13.977 1.00 14.87  ? 166 ARG A O    1 
ATOM   2667 C  CB   . ARG A 1 166 ? -2.818  2.483   17.066 1.00 13.58  ? 166 ARG A CB   1 
ATOM   2668 C  CG   . ARG A 1 166 ? -3.598  2.205   18.339 1.00 13.22  ? 166 ARG A CG   1 
ATOM   2669 C  CD   . ARG A 1 166 ? -3.332  3.233   19.412 1.00 13.48  ? 166 ARG A CD   1 
ATOM   2670 N  NE   . ARG A 1 166 ? -4.070  2.917   20.632 1.00 13.14  ? 166 ARG A NE   1 
ATOM   2671 C  CZ   . ARG A 1 166 ? -3.882  3.512   21.797 1.00 12.46  ? 166 ARG A CZ   1 
ATOM   2672 N  NH1  . ARG A 1 166 ? -2.880  4.356   21.970 1.00 13.93  ? 166 ARG A NH1  1 
ATOM   2673 N  NH2  . ARG A 1 166 ? -4.660  3.190   22.821 1.00 12.99  ? 166 ARG A NH2  1 
ATOM   2674 H  H    . ARG A 1 166 ? -1.494  0.341   17.417 1.00 16.28  ? 166 ARG A H    1 
ATOM   2675 H  HA   . ARG A 1 166 ? -3.755  0.954   16.080 1.00 15.73  ? 166 ARG A HA   1 
ATOM   2676 H  HB2  . ARG A 1 166 ? -1.892  2.708   17.294 1.00 16.28  ? 166 ARG A HB2  1 
ATOM   2677 H  HB3  . ARG A 1 166 ? -3.218  3.247   16.600 1.00 16.28  ? 166 ARG A HB3  1 
ATOM   2678 H  HG2  . ARG A 1 166 ? -4.557  2.198   18.136 1.00 15.77  ? 166 ARG A HG2  1 
ATOM   2679 H  HG3  . ARG A 1 166 ? -3.356  1.318   18.681 1.00 15.77  ? 166 ARG A HG3  1 
ATOM   2680 H  HD2  . ARG A 1 166 ? -2.371  3.259   19.608 1.00 19.44  ? 166 ARG A HD2  1 
ATOM   2681 H  HD3  . ARG A 1 166 ? -3.601  4.120   19.089 1.00 19.44  ? 166 ARG A HD3  1 
ATOM   2682 H  HE   . ARG A 1 166 ? -4.670  2.286   20.593 1.00 20.70  ? 166 ARG A HE   1 
ATOM   2683 H  HH11 . ARG A 1 166 ? -2.775  5.034   21.417 1.00 20.00  ? 166 ARG A HH11 1 
ATOM   2684 H  HH12 . ARG A 1 166 ? -2.321  4.240   22.642 1.00 20.00  ? 166 ARG A HH12 1 
ATOM   2685 H  HH21 . ARG A 1 166 ? -5.371  2.688   22.693 1.00 20.70  ? 166 ARG A HH21 1 
ATOM   2686 H  HH22 . ARG A 1 166 ? -4.463  3.479   23.628 1.00 20.70  ? 166 ARG A HH22 1 
ATOM   2687 N  N    . ALA A 1 167 ? -1.181  1.210   14.300 1.00 14.05  ? 167 ALA A N    1 
ATOM   2688 C  CA   . ALA A 1 167 ? -0.691  1.395   12.939 1.00 15.11  ? 167 ALA A CA   1 
ATOM   2689 C  C    . ALA A 1 167 ? -1.123  0.282   11.988 1.00 15.28  ? 167 ALA A C    1 
ATOM   2690 O  O    . ALA A 1 167 ? -0.842  0.362   10.793 1.00 17.11  ? 167 ALA A O    1 
ATOM   2691 C  CB   . ALA A 1 167 ? 0.818   1.478   12.976 1.00 16.12  ? 167 ALA A CB   1 
ATOM   2692 H  H    . ALA A 1 167 ? -0.629  0.803   14.904 1.00 19.31  ? 167 ALA A H    1 
ATOM   2693 H  HA   . ALA A 1 167 ? -1.043  2.249   12.595 1.00 18.27  ? 167 ALA A HA   1 
ATOM   2694 H  HB1  . ALA A 1 167 ? 1.157   1.637   12.079 1.00 19.31  ? 167 ALA A HB1  1 
ATOM   2695 H  HB2  . ALA A 1 167 ? 1.090   2.208   13.557 1.00 19.31  ? 167 ALA A HB2  1 
ATOM   2696 H  HB3  . ALA A 1 167 ? 1.182   0.643   13.315 1.00 19.31  ? 167 ALA A HB3  1 
ATOM   2697 N  N    . SER A 1 168 ? -1.810  -0.761  12.474 1.00 14.38  ? 168 SER A N    1 
ATOM   2698 C  CA   . SER A 1 168 ? -2.057  -1.959  11.697 1.00 14.72  ? 168 SER A CA   1 
ATOM   2699 C  C    . SER A 1 168 ? -3.303  -1.816  10.824 1.00 13.91  ? 168 SER A C    1 
ATOM   2700 O  O    . SER A 1 168 ? -4.189  -1.000  11.073 1.00 14.77  ? 168 SER A O    1 
ATOM   2701 C  CB   . SER A 1 168 ? -2.186  -3.167  12.608 1.00 15.47  ? 168 SER A CB   1 
ATOM   2702 O  OG   . SER A 1 168 ? -3.442  -3.177  13.296 1.00 15.31  ? 168 SER A OG   1 
ATOM   2703 H  H    . SER A 1 168 ? -2.141  -0.720  13.325 1.00 17.84  ? 168 SER A H    1 
ATOM   2704 H  HA   . SER A 1 168 ? -1.276  -2.103  11.099 1.00 16.84  ? 168 SER A HA   1 
ATOM   2705 H  HB2  . SER A 1 168 ? -2.102  -3.987  12.071 1.00 25.72  ? 168 SER A HB2  1 
ATOM   2706 H  HB3  . SER A 1 168 ? -1.454  -3.157  13.265 1.00 25.71  ? 168 SER A HB3  1 
ATOM   2707 H  HG   . SER A 1 168 ? -3.389  -2.656  13.961 1.00 17.84  ? 168 SER A HG   1 
ATOM   2708 N  N    . VAL A 1 169 ? -3.434  -2.735  9.868  1.00 14.19  ? 169 VAL A N    1 
ATOM   2709 C  CA   . VAL A 1 169 ? -4.612  -2.779  9.009  1.00 14.75  ? 169 VAL A CA   1 
ATOM   2710 C  C    . VAL A 1 169 ? -5.897  -2.978  9.831  1.00 13.74  ? 169 VAL A C    1 
ATOM   2711 O  O    . VAL A 1 169 ? -6.918  -2.342  9.558  1.00 13.99  ? 169 VAL A O    1 
ATOM   2712 C  CB   . VAL A 1 169 ? -4.473  -3.864  7.918  1.00 16.15  ? 169 VAL A CB   1 
ATOM   2713 C  CG1  . VAL A 1 169 ? -5.738  -4.007  7.084  1.00 17.58  ? 169 VAL A CG1  1 
ATOM   2714 C  CG2  . VAL A 1 169 ? -3.305  -3.532  7.002  1.00 18.55  ? 169 VAL A CG2  1 
ATOM   2715 H  H    . VAL A 1 169 ? -2.777  -3.360  9.752  1.00 17.01  ? 169 VAL A H    1 
ATOM   2716 H  HA   . VAL A 1 169 ? -4.679  -1.917  8.561  1.00 17.62  ? 169 VAL A HA   1 
ATOM   2717 H  HB   . VAL A 1 169 ? -4.289  -4.728  8.362  1.00 20.43  ? 169 VAL A HB   1 
ATOM   2718 H  HG11 . VAL A 1 169 ? -5.524  -4.431  6.235  1.00 17.58  ? 169 VAL A HG11 1 
ATOM   2719 H  HG12 . VAL A 1 169 ? -6.384  -4.555  7.563  1.00 17.59  ? 169 VAL A HG12 1 
ATOM   2720 H  HG13 . VAL A 1 169 ? -6.120  -3.127  6.919  1.00 17.58  ? 169 VAL A HG13 1 
ATOM   2721 H  HG21 . VAL A 1 169 ? -3.252  -4.193  6.290  1.00 17.17  ? 169 VAL A HG21 1 
ATOM   2722 H  HG22 . VAL A 1 169 ? -3.437  -2.650  6.614  1.00 17.17  ? 169 VAL A HG22 1 
ATOM   2723 H  HG23 . VAL A 1 169 ? -2.477  -3.541  7.511  1.00 17.16  ? 169 VAL A HG23 1 
ATOM   2724 N  N    . GLU A 1 170 ? -5.845  -3.819  10.864 1.00 13.04  ? 170 GLU A N    1 
ATOM   2725 C  CA   . GLU A 1 170 ? -6.997  -4.086  11.707 1.00 12.62  ? 170 GLU A CA   1 
ATOM   2726 C  C    . GLU A 1 170 ? -7.576  -2.778  12.253 1.00 12.15  ? 170 GLU A C    1 
ATOM   2727 O  O    . GLU A 1 170 ? -8.785  -2.614  12.348 1.00 12.14  ? 170 GLU A O    1 
ATOM   2728 C  CB   . GLU A 1 170 ? -6.576  -5.015  12.860 1.00 12.76  ? 170 GLU A CB   1 
ATOM   2729 C  CG   . GLU A 1 170 ? -7.683  -5.325  13.852 1.00 12.80  ? 170 GLU A CG   1 
ATOM   2730 C  CD   . GLU A 1 170 ? -7.234  -6.112  15.064 1.00 13.20  ? 170 GLU A CD   1 
ATOM   2731 O  OE1  . GLU A 1 170 ? -6.033  -6.420  15.217 1.00 14.72  ? 170 GLU A OE1  1 
ATOM   2732 O  OE2  . GLU A 1 170 ? -8.120  -6.418  15.905 1.00 13.63  ? 170 GLU A OE2  1 
ATOM   2733 H  H    . GLU A 1 170 ? -5.060  -4.249  11.048 1.00 15.47  ? 170 GLU A H    1 
ATOM   2734 H  HA   . GLU A 1 170 ? -7.684  -4.537  11.166 1.00 15.11  ? 170 GLU A HA   1 
ATOM   2735 H  HB2  . GLU A 1 170 ? -6.250  -5.856  12.477 1.00 15.46  ? 170 GLU A HB2  1 
ATOM   2736 H  HB3  . GLU A 1 170 ? -5.831  -4.595  13.338 1.00 15.46  ? 170 GLU A HB3  1 
ATOM   2737 H  HG2  . GLU A 1 170 ? -8.082  -4.485  14.162 1.00 14.49  ? 170 GLU A HG2  1 
ATOM   2738 H  HG3  . GLU A 1 170 ? -8.384  -5.836  13.396 1.00 14.49  ? 170 GLU A HG3  1 
ATOM   2739 N  N    . TRP A 1 171 ? -6.687  -1.852  12.631 1.00 12.26  ? 171 TRP A N    1 
ATOM   2740 C  CA   . TRP A 1 171 ? -7.127  -0.620  13.248 1.00 12.41  ? 171 TRP A CA   1 
ATOM   2741 C  C    . TRP A 1 171 ? -7.781  0.357   12.267 1.00 12.88  ? 171 TRP A C    1 
ATOM   2742 O  O    . TRP A 1 171 ? -8.414  1.326   12.690 1.00 13.78  ? 171 TRP A O    1 
ATOM   2743 C  CB   . TRP A 1 171 ? -6.005  0.047   14.034 1.00 12.90  ? 171 TRP A CB   1 
ATOM   2744 C  CG   . TRP A 1 171 ? -6.197  -0.038  15.515 1.00 12.62  ? 171 TRP A CG   1 
ATOM   2745 C  CD1  . TRP A 1 171 ? -6.565  0.984   16.341 1.00 13.39  ? 171 TRP A CD1  1 
ATOM   2746 C  CD2  . TRP A 1 171 ? -6.096  -1.210  16.339 1.00 12.81  ? 171 TRP A CD2  1 
ATOM   2747 N  NE1  . TRP A 1 171 ? -6.700  0.533   17.620 1.00 13.85  ? 171 TRP A NE1  1 
ATOM   2748 C  CE2  . TRP A 1 171 ? -6.413  -0.803  17.651 1.00 13.21  ? 171 TRP A CE2  1 
ATOM   2749 C  CE3  . TRP A 1 171 ? -5.763  -2.551  16.100 1.00 13.13  ? 171 TRP A CE3  1 
ATOM   2750 C  CZ2  . TRP A 1 171 ? -6.359  -1.677  18.728 1.00 14.60  ? 171 TRP A CZ2  1 
ATOM   2751 C  CZ3  . TRP A 1 171 ? -5.728  -3.431  17.171 1.00 14.34  ? 171 TRP A CZ3  1 
ATOM   2752 C  CH2  . TRP A 1 171 ? -6.028  -2.989  18.466 1.00 14.61  ? 171 TRP A CH2  1 
ATOM   2753 H  H    . TRP A 1 171 ? -5.793  -1.996  12.508 1.00 15.36  ? 171 TRP A H    1 
ATOM   2754 H  HA   . TRP A 1 171 ? -7.815  -0.872  13.907 1.00 15.11  ? 171 TRP A HA   1 
ATOM   2755 H  HB2  . TRP A 1 171 ? -5.157  -0.378  13.794 1.00 15.36  ? 171 TRP A HB2  1 
ATOM   2756 H  HB3  . TRP A 1 171 ? -5.955  0.989   13.769 1.00 15.36  ? 171 TRP A HB3  1 
ATOM   2757 H  HD1  . TRP A 1 171 ? -6.733  1.873   16.066 1.00 16.85  ? 171 TRP A HD1  1 
ATOM   2758 H  HE1  . TRP A 1 171 ? -6.907  1.027   18.312 1.00 16.85  ? 171 TRP A HE1  1 
ATOM   2759 H  HE3  . TRP A 1 171 ? -5.547  -2.843  15.228 1.00 16.85  ? 171 TRP A HE3  1 
ATOM   2760 H  HZ2  . TRP A 1 171 ? -6.577  -1.389  19.598 1.00 16.85  ? 171 TRP A HZ2  1 
ATOM   2761 H  HZ3  . TRP A 1 171 ? -5.505  -4.337  17.026 1.00 16.85  ? 171 TRP A HZ3  1 
ATOM   2762 H  HH2  . TRP A 1 171 ? -6.014  -3.607  19.176 1.00 16.85  ? 171 TRP A HH2  1 
ATOM   2763 N  N    . GLN A 1 172 ? -7.722  0.069   10.963 1.00 13.14  ? 172 GLN A N    1 
ATOM   2764 C  CA   . GLN A 1 172 ? -8.496  0.840   10.001 1.00 14.92  ? 172 GLN A CA   1 
ATOM   2765 C  C    . GLN A 1 172 ? -9.995  0.709   10.241 1.00 13.51  ? 172 GLN A C    1 
ATOM   2766 O  O    . GLN A 1 172 ? -10.759 1.552   9.804  1.00 15.02  ? 172 GLN A O    1 
ATOM   2767 C  CB   . GLN A 1 172 ? -8.183  0.418   8.567  1.00 16.24  ? 172 GLN A CB   1 
ATOM   2768 C  CG   . GLN A 1 172 ? -6.748  0.674   8.149  1.00 19.80  ? 172 GLN A CG   1 
ATOM   2769 C  CD   . GLN A 1 172 ? -6.431  0.058   6.808  1.00 22.46  ? 172 GLN A CD   1 
ATOM   2770 O  OE1  . GLN A 1 172 ? -7.315  -0.402  6.083  1.00 27.29  ? 172 GLN A OE1  1 
ATOM   2771 N  NE2  . GLN A 1 172 ? -5.154  -0.004  6.496  1.00 24.22  ? 172 GLN A NE2  1 
ATOM   2772 H  H    . GLN A 1 172 ? -7.183  -0.605  10.664 1.00 22.61  ? 172 GLN A H    1 
ATOM   2773 H  HA   . GLN A 1 172 ? -8.251  1.787   10.104 1.00 36.10  ? 172 GLN A HA   1 
ATOM   2774 H  HB2  . GLN A 1 172 ? -8.378  -0.538  8.476  1.00 19.09  ? 172 GLN A HB2  1 
ATOM   2775 H  HB3  . GLN A 1 172 ? -8.782  0.904   7.963  1.00 19.09  ? 172 GLN A HB3  1 
ATOM   2776 H  HG2  . GLN A 1 172 ? -6.593  1.642   8.104  1.00 22.61  ? 172 GLN A HG2  1 
ATOM   2777 H  HG3  . GLN A 1 172 ? -6.141  0.303   8.824  1.00 22.61  ? 172 GLN A HG3  1 
ATOM   2778 H  HE21 . GLN A 1 172 ? -4.557  0.431   6.982  1.00 23.07  ? 172 GLN A HE21 1 
ATOM   2779 H  HE22 . GLN A 1 172 ? -4.891  -0.482  5.800  1.00 23.07  ? 172 GLN A HE22 1 
ATOM   2780 N  N    . TYR A 1 173 ? -10.406 -0.335  10.967 1.00 12.27  ? 173 TYR A N    1 
ATOM   2781 C  CA   . TYR A 1 173 ? -11.814 -0.606  11.228 1.00 12.83  ? 173 TYR A CA   1 
ATOM   2782 C  C    . TYR A 1 173 ? -12.239 -0.152  12.615 1.00 12.19  ? 173 TYR A C    1 
ATOM   2783 O  O    . TYR A 1 173 ? -13.407 -0.285  12.965 1.00 13.40  ? 173 TYR A O    1 
ATOM   2784 C  CB   . TYR A 1 173 ? -12.129 -2.094  11.051 1.00 13.04  ? 173 TYR A CB   1 
ATOM   2785 C  CG   . TYR A 1 173 ? -11.880 -2.615  9.660  1.00 12.65  ? 173 TYR A CG   1 
ATOM   2786 C  CD1  . TYR A 1 173 ? -10.604 -3.003  9.300  1.00 13.55  ? 173 TYR A CD1  1 
ATOM   2787 C  CD2  . TYR A 1 173 ? -12.894 -2.677  8.709  1.00 14.33  ? 173 TYR A CD2  1 
ATOM   2788 C  CE1  . TYR A 1 173 ? -10.317 -3.437  8.014  1.00 14.77  ? 173 TYR A CE1  1 
ATOM   2789 C  CE2  . TYR A 1 173 ? -12.634 -3.132  7.427  1.00 15.01  ? 173 TYR A CE2  1 
ATOM   2790 C  CZ   . TYR A 1 173 ? -11.343 -3.503  7.089  1.00 15.60  ? 173 TYR A CZ   1 
ATOM   2791 O  OH   . TYR A 1 173 ? -11.063 -3.907  5.803  1.00 18.94  ? 173 TYR A OH   1 
ATOM   2792 H  H    . TYR A 1 173 ? -9.787  -0.920  11.297 1.00 14.53  ? 173 TYR A H    1 
ATOM   2793 H  HA   . TYR A 1 173 ? -12.353 -0.101  10.568 1.00 18.38  ? 173 TYR A HA   1 
ATOM   2794 H  HB2  . TYR A 1 173 ? -11.582 -2.603  11.684 1.00 14.67  ? 173 TYR A HB2  1 
ATOM   2795 H  HB3  . TYR A 1 173 ? -13.070 -2.243  11.281 1.00 14.67  ? 173 TYR A HB3  1 
ATOM   2796 H  HD1  . TYR A 1 173 ? -9.906  -2.942  9.931  1.00 17.74  ? 173 TYR A HD1  1 
ATOM   2797 H  HD2  . TYR A 1 173 ? -13.769 -2.415  8.941  1.00 17.74  ? 173 TYR A HD2  1 
ATOM   2798 H  HE1  . TYR A 1 173 ? -9.441  -3.692  7.777  1.00 17.74  ? 173 TYR A HE1  1 
ATOM   2799 H  HE2  . TYR A 1 173 ? -13.322 -3.162  6.783  1.00 17.74  ? 173 TYR A HE2  1 
ATOM   2800 H  HH   . TYR A 1 173 ? -11.661 -4.319  5.341  1.00 17.74  ? 173 TYR A HH   1 
ATOM   2801 N  N    . VAL A 1 174 ? -11.321 0.380   13.417 1.00 12.06  ? 174 VAL A N    1 
ATOM   2802 C  CA   . VAL A 1 174 ? -11.636 0.823   14.768 1.00 12.14  ? 174 VAL A CA   1 
ATOM   2803 C  C    . VAL A 1 174 ? -12.198 2.238   14.694 1.00 12.38  ? 174 VAL A C    1 
ATOM   2804 O  O    . VAL A 1 174 ? -11.497 3.157   14.262 1.00 13.92  ? 174 VAL A O    1 
ATOM   2805 C  CB   . VAL A 1 174 ? -10.395 0.714   15.683 1.00 12.06  ? 174 VAL A CB   1 
ATOM   2806 C  CG1  . VAL A 1 174 ? -10.600 1.441   17.014 1.00 12.26  ? 174 VAL A CG1  1 
ATOM   2807 C  CG2  . VAL A 1 174 ? -10.023 -0.722  15.899 1.00 12.95  ? 174 VAL A CG2  1 
ATOM   2808 H  H    . VAL A 1 174 ? -10.463 0.475   13.117 1.00 14.53  ? 174 VAL A H    1 
ATOM   2809 H  HA   . VAL A 1 174 ? -12.326 0.237   15.125 1.00 14.29  ? 174 VAL A HA   1 
ATOM   2810 H  HB   . VAL A 1 174 ? -9.643  1.152   15.214 1.00 14.53  ? 174 VAL A HB   1 
ATOM   2811 H  HG11 . VAL A 1 174 ? -9.975  1.095   17.674 1.00 15.10  ? 174 VAL A HG11 1 
ATOM   2812 H  HG12 . VAL A 1 174 ? -10.445 2.394   16.892 1.00 15.10  ? 174 VAL A HG12 1 
ATOM   2813 H  HG13 . VAL A 1 174 ? -11.511 1.299   17.326 1.00 15.10  ? 174 VAL A HG13 1 
ATOM   2814 H  HG21 . VAL A 1 174 ? -9.209  -0.770  16.430 1.00 15.11  ? 174 VAL A HG21 1 
ATOM   2815 H  HG22 . VAL A 1 174 ? -10.743 -1.177  16.369 1.00 15.11  ? 174 VAL A HG22 1 
ATOM   2816 H  HG23 . VAL A 1 174 ? -9.874  -1.153  15.040 1.00 15.11  ? 174 VAL A HG23 1 
ATOM   2817 N  N    . ASP A 1 175 ? -13.440 2.425   15.112 1.00 11.94  ? 175 ASP A N    1 
ATOM   2818 C  CA   . ASP A 1 175 ? -14.089 3.727   15.042 1.00 12.80  ? 175 ASP A CA   1 
ATOM   2819 C  C    . ASP A 1 175 ? -14.339 4.352   16.414 1.00 12.49  ? 175 ASP A C    1 
ATOM   2820 O  O    . ASP A 1 175 ? -14.723 5.532   16.484 1.00 13.85  ? 175 ASP A O    1 
ATOM   2821 C  CB   . ASP A 1 175 ? -15.350 3.685   14.168 1.00 14.11  ? 175 ASP A CB   1 
ATOM   2822 C  CG   . ASP A 1 175 ? -16.463 2.786   14.664 1.00 14.22  ? 175 ASP A CG   1 
ATOM   2823 O  OD1  . ASP A 1 175 ? -16.282 2.163   15.721 1.00 14.57  ? 175 ASP A OD1  1 
ATOM   2824 O  OD2  . ASP A 1 175 ? -17.498 2.698   13.946 1.00 16.74  ? 175 ASP A OD2  1 
ATOM   2825 H  H    . ASP A 1 175 ? -13.912 1.717   15.447 1.00 14.29  ? 175 ASP A H    1 
ATOM   2826 H  HA   . ASP A 1 175 ? -13.464 4.328   14.573 1.00 15.28  ? 175 ASP A HA   1 
ATOM   2827 H  HB2  . ASP A 1 175 ? -15.708 4.593   14.094 1.00 16.60  ? 175 ASP A HB2  1 
ATOM   2828 H  HB3  . ASP A 1 175 ? -15.098 3.386   13.271 1.00 16.60  ? 175 ASP A HB3  1 
ATOM   2829 N  N    . ARG A 1 176 ? -14.003 3.649   17.501 1.00 11.46  ? 176 ARG A N    1 
ATOM   2830 C  CA   . ARG A 1 176 ? -13.952 4.239   18.833 1.00 12.03  ? 176 ARG A CA   1 
ATOM   2831 C  C    . ARG A 1 176 ? -12.885 3.504   19.629 1.00 11.74  ? 176 ARG A C    1 
ATOM   2832 O  O    . ARG A 1 176 ? -12.806 2.271   19.594 1.00 12.78  ? 176 ARG A O    1 
ATOM   2833 C  CB   . ARG A 1 176 ? -15.191 4.014   19.675 1.00 15.10  ? 176 ARG A CB   1 
ATOM   2834 C  CG   . ARG A 1 176 ? -16.394 4.660   19.087 1.00 16.38  ? 176 ARG A CG   1 
ATOM   2835 C  CD   . ARG A 1 176 ? -17.522 4.676   20.108 1.00 18.50  ? 176 ARG A CD   1 
ATOM   2836 N  NE   . ARG A 1 176 ? -17.177 5.586   21.221 1.00 15.09  ? 176 ARG A NE   1 
ATOM   2837 C  CZ   . ARG A 1 176 ? -18.077 5.953   22.209 1.00 21.92  ? 176 ARG A CZ   1 
ATOM   2838 N  NH1  . ARG A 1 176 ? -19.208 5.336   22.446 1.00 23.99  ? 176 ARG A NH1  1 
ATOM   2839 N  NH2  . ARG A 1 176 ? -17.764 6.831   23.138 1.00 24.19  ? 176 ARG A NH2  1 
ATOM   2840 H  H    . ARG A 1 176 ? -13.807 2.761   17.413 1.00 14.29  ? 176 ARG A H    1 
ATOM   2841 H  HA   . ARG A 1 176 ? -13.741 5.197   18.776 1.00 14.69  ? 176 ARG A HA   1 
ATOM   2842 H  HB2  . ARG A 1 176 ? -15.352 3.051   19.755 1.00 18.72  ? 176 ARG A HB2  1 
ATOM   2843 H  HB3  . ARG A 1 176 ? -15.035 4.370   20.573 1.00 18.63  ? 176 ARG A HB3  1 
ATOM   2844 H  HG2  . ARG A 1 176 ? -16.180 5.578   18.821 1.00 20.20  ? 176 ARG A HG2  1 
ATOM   2845 H  HG3  . ARG A 1 176 ? -16.681 4.164   18.290 1.00 20.20  ? 176 ARG A HG3  1 
ATOM   2846 H  HD2  . ARG A 1 176 ? -18.349 4.980   19.678 1.00 19.83  ? 176 ARG A HD2  1 
ATOM   2847 H  HD3  . ARG A 1 176 ? -17.668 3.770   20.454 1.00 19.83  ? 176 ARG A HD3  1 
ATOM   2848 H  HE   . ARG A 1 176 ? -16.374 5.921   21.254 1.00 18.60  ? 176 ARG A HE   1 
ATOM   2849 H  HH11 . ARG A 1 176 ? -19.313 4.500   22.188 1.00 18.57  ? 176 ARG A HH11 1 
ATOM   2850 H  HH12 . ARG A 1 176 ? -19.862 5.757   22.862 1.00 18.57  ? 176 ARG A HH12 1 
ATOM   2851 H  HH21 . ARG A 1 176 ? -16.960 7.186   23.149 1.00 18.57  ? 176 ARG A HH21 1 
ATOM   2852 H  HH22 . ARG A 1 176 ? -18.356 7.064   23.745 1.00 18.57  ? 176 ARG A HH22 1 
ATOM   2853 N  N    . GLU A 1 177 ? -12.084 4.275   20.353 1.00 11.75  ? 177 GLU A N    1 
ATOM   2854 C  CA   . GLU A 1 177 ? -11.072 3.727   21.241 1.00 12.02  ? 177 GLU A CA   1 
ATOM   2855 C  C    . GLU A 1 177 ? -10.811 4.755   22.325 1.00 11.73  ? 177 GLU A C    1 
ATOM   2856 O  O    . GLU A 1 177 ? -10.532 5.914   22.031 1.00 13.05  ? 177 GLU A O    1 
ATOM   2857 C  CB   . GLU A 1 177 ? -9.795  3.357   20.484 1.00 12.45  ? 177 GLU A CB   1 
ATOM   2858 C  CG   . GLU A 1 177 ? -8.699  2.830   21.393 1.00 12.48  ? 177 GLU A CG   1 
ATOM   2859 C  CD   . GLU A 1 177 ? -7.459  2.315   20.679 1.00 13.15  ? 177 GLU A CD   1 
ATOM   2860 O  OE1  . GLU A 1 177 ? -7.361  2.484   19.448 1.00 15.45  ? 177 GLU A OE1  1 
ATOM   2861 O  OE2  . GLU A 1 177 ? -6.559  1.774   21.358 1.00 13.75  ? 177 GLU A OE2  1 
ATOM   2862 H  H    . GLU A 1 177 ? -12.165 5.184   20.292 1.00 14.69  ? 177 GLU A H    1 
ATOM   2863 H  HA   . GLU A 1 177 ? -11.436 2.915   21.657 1.00 14.28  ? 177 GLU A HA   1 
ATOM   2864 H  HB2  . GLU A 1 177 ? -10.013 2.674   19.815 1.00 14.81  ? 177 GLU A HB2  1 
ATOM   2865 H  HB3  . GLU A 1 177 ? -9.467  4.150   20.012 1.00 14.81  ? 177 GLU A HB3  1 
ATOM   2866 H  HG2  . GLU A 1 177 ? -8.423  3.545   22.005 1.00 15.28  ? 177 GLU A HG2  1 
ATOM   2867 H  HG3  . GLU A 1 177 ? -9.064  2.101   21.939 1.00 15.28  ? 177 GLU A HG3  1 
ATOM   2868 N  N    . ILE A 1 178 ? -10.906 4.322   23.572 1.00 11.32  ? 178 ILE A N    1 
ATOM   2869 C  CA   . ILE A 1 178 ? -10.563 5.128   24.721 1.00 11.57  ? 178 ILE A CA   1 
ATOM   2870 C  C    . ILE A 1 178 ? -9.511  4.360   25.505 1.00 10.79  ? 178 ILE A C    1 
ATOM   2871 O  O    . ILE A 1 178 ? -9.613  3.149   25.627 1.00 12.32  ? 178 ILE A O    1 
ATOM   2872 C  CB   . ILE A 1 178 ? -11.805 5.420   25.576 1.00 13.57  ? 178 ILE A CB   1 
ATOM   2873 C  CG1  . ILE A 1 178 ? -12.913 6.060   24.745 1.00 16.05  ? 178 ILE A CG1  1 
ATOM   2874 C  CG2  . ILE A 1 178 ? -11.447 6.297   26.766 1.00 17.61  ? 178 ILE A CG2  1 
ATOM   2875 C  CD1  . ILE A 1 178 ? -14.249 6.072   25.413 1.00 18.53  ? 178 ILE A CD1  1 
ATOM   2876 H  H    . ILE A 1 178 ? -11.207 3.471   23.719 1.00 14.28  ? 178 ILE A H    1 
ATOM   2877 H  HA   . ILE A 1 178 ? -10.182 5.972   24.419 1.00 14.11  ? 178 ILE A HA   1 
ATOM   2878 H  HB   . ILE A 1 178 ? -12.145 4.558   25.922 1.00 17.50  ? 178 ILE A HB   1 
ATOM   2879 H  HG12 . ILE A 1 178 ? -12.657 6.984   24.541 1.00 18.71  ? 178 ILE A HG12 1 
ATOM   2880 H  HG13 . ILE A 1 178 ? -12.994 5.577   23.896 1.00 18.71  ? 178 ILE A HG13 1 
ATOM   2881 H  HG21 . ILE A 1 178 ? -12.255 6.532   27.254 1.00 18.05  ? 178 ILE A HG21 1 
ATOM   2882 H  HG22 . ILE A 1 178 ? -10.844 5.816   27.358 1.00 18.05  ? 178 ILE A HG22 1 
ATOM   2883 H  HG23 . ILE A 1 178 ? -11.012 7.109   26.453 1.00 18.05  ? 178 ILE A HG23 1 
ATOM   2884 H  HD11 . ILE A 1 178 ? -14.942 6.248   24.753 1.00 17.75  ? 178 ILE A HD11 1 
ATOM   2885 H  HD12 . ILE A 1 178 ? -14.412 5.210   25.833 1.00 17.75  ? 178 ILE A HD12 1 
ATOM   2886 H  HD13 . ILE A 1 178 ? -14.265 6.769   26.091 1.00 17.78  ? 178 ILE A HD13 1 
ATOM   2887 N  N    . ASP A 1 179 ? -8.512  5.046   26.053 1.00 11.62  ? 179 ASP A N    1 
ATOM   2888 C  CA   . ASP A 1 179 ? -7.433  4.363   26.733 1.00 11.93  ? 179 ASP A CA   1 
ATOM   2889 C  C    . ASP A 1 179 ? -7.313  4.932   28.139 1.00 10.75  ? 179 ASP A C    1 
ATOM   2890 O  O    . ASP A 1 179 ? -6.871  6.075   28.303 1.00 12.49  ? 179 ASP A O    1 
ATOM   2891 C  CB   . ASP A 1 179 ? -6.188  4.571   25.894 1.00 13.58  ? 179 ASP A CB   1 
ATOM   2892 C  CG   . ASP A 1 179 ? -4.919  4.003   26.475 1.00 13.54  ? 179 ASP A CG   1 
ATOM   2893 O  OD1  . ASP A 1 179 ? -4.959  3.485   27.619 1.00 13.95  ? 179 ASP A OD1  1 
ATOM   2894 O  OD2  . ASP A 1 179 ? -3.896  4.023   25.756 1.00 14.79  ? 179 ASP A OD2  1 
ATOM   2895 H  H    . ASP A 1 179 ? -8.502  5.959   26.005 1.00 14.11  ? 179 ASP A H    1 
ATOM   2896 H  HA   . ASP A 1 179 ? -7.634  3.401   26.784 1.00 12.62  ? 179 ASP A HA   1 
ATOM   2897 H  HB2  . ASP A 1 179 ? -6.329  4.157   25.018 1.00 25.47  ? 179 ASP A HB2  1 
ATOM   2898 H  HB3  . ASP A 1 179 ? -6.057  5.529   25.757 1.00 25.48  ? 179 ASP A HB3  1 
ATOM   2899 N  N    . ILE A 1 180 ? -7.785  4.181   29.121 1.00 10.36  ? 180 ILE A N    1 
ATOM   2900 C  CA   . ILE A 1 180 ? -7.822  4.609   30.517 1.00 10.31  ? 180 ILE A CA   1 
ATOM   2901 C  C    . ILE A 1 180 ? -6.672  3.937   31.262 1.00 10.36  ? 180 ILE A C    1 
ATOM   2902 O  O    . ILE A 1 180 ? -6.565  2.714   31.242 1.00 11.05  ? 180 ILE A O    1 
ATOM   2903 C  CB   . ILE A 1 180 ? -9.176  4.230   31.159 1.00 11.06  ? 180 ILE A CB   1 
ATOM   2904 C  CG1  . ILE A 1 180 ? -10.328 4.891   30.393 1.00 12.18  ? 180 ILE A CG1  1 
ATOM   2905 C  CG2  . ILE A 1 180 ? -9.193  4.611   32.629 1.00 12.61  ? 180 ILE A CG2  1 
ATOM   2906 C  CD1  . ILE A 1 180 ? -11.696 4.286   30.693 1.00 14.19  ? 180 ILE A CD1  1 
ATOM   2907 H  H    . ILE A 1 180 ? -8.106  3.349   28.919 1.00 12.62  ? 180 ILE A H    1 
ATOM   2908 H  HA   . ILE A 1 180 ? -7.713  5.574   30.559 1.00 12.64  ? 180 ILE A HA   1 
ATOM   2909 H  HB   . ILE A 1 180 ? -9.284  3.249   31.091 1.00 14.57  ? 180 ILE A HB   1 
ATOM   2910 H  HG12 . ILE A 1 180 ? -10.349 5.845   30.620 1.00 14.89  ? 180 ILE A HG12 1 
ATOM   2911 H  HG13 . ILE A 1 180 ? -10.155 4.814   29.431 1.00 14.89  ? 180 ILE A HG13 1 
ATOM   2912 H  HG21 . ILE A 1 180 ? -10.113 4.694   32.935 1.00 16.06  ? 180 ILE A HG21 1 
ATOM   2913 H  HG22 . ILE A 1 180 ? -8.742  3.924   33.150 1.00 16.06  ? 180 ILE A HG22 1 
ATOM   2914 H  HG23 . ILE A 1 180 ? -8.736  5.461   32.751 1.00 16.06  ? 180 ILE A HG23 1 
ATOM   2915 H  HD11 . ILE A 1 180 ? -12.343 4.603   30.038 1.00 16.07  ? 180 ILE A HD11 1 
ATOM   2916 H  HD12 . ILE A 1 180 ? -11.641 3.316   30.648 1.00 16.07  ? 180 ILE A HD12 1 
ATOM   2917 H  HD13 . ILE A 1 180 ? -11.983 4.552   31.584 1.00 16.07  ? 180 ILE A HD13 1 
ATOM   2918 N  N    . ARG A 1 181 ? -5.828  4.735   31.927 1.00 10.36  ? 181 ARG A N    1 
ATOM   2919 C  CA   . ARG A 1 181 ? -4.709  4.197   32.685 1.00 10.49  ? 181 ARG A CA   1 
ATOM   2920 C  C    . ARG A 1 181 ? -5.001  4.296   34.173 1.00 10.45  ? 181 ARG A C    1 
ATOM   2921 O  O    . ARG A 1 181 ? -5.511  5.306   34.658 1.00 11.35  ? 181 ARG A O    1 
ATOM   2922 C  CB   . ARG A 1 181 ? -3.409  4.947   32.377 1.00 11.25  ? 181 ARG A CB   1 
ATOM   2923 C  CG   . ARG A 1 181 ? -3.054  4.927   30.898 1.00 11.38  ? 181 ARG A CG   1 
ATOM   2924 C  CD   . ARG A 1 181 ? -2.917  3.509   30.372 1.00 11.31  ? 181 ARG A CD   1 
ATOM   2925 N  NE   . ARG A 1 181 ? -2.597  3.476   28.949 1.00 11.56  ? 181 ARG A NE   1 
ATOM   2926 C  CZ   . ARG A 1 181 ? -1.389  3.698   28.438 1.00 11.43  ? 181 ARG A CZ   1 
ATOM   2927 N  NH1  . ARG A 1 181 ? -0.312  3.698   29.206 1.00 12.29  ? 181 ARG A NH1  1 
ATOM   2928 N  NH2  . ARG A 1 181 ? -1.276  3.892   27.134 1.00 13.68  ? 181 ARG A NH2  1 
ATOM   2929 H  H    . ARG A 1 181 ? -5.953  5.640   31.908 1.00 12.64  ? 181 ARG A H    1 
ATOM   2930 H  HA   . ARG A 1 181 ? -4.594  3.250   32.450 1.00 12.93  ? 181 ARG A HA   1 
ATOM   2931 H  HB2  . ARG A 1 181 ? -3.503  5.877   32.672 1.00 13.86  ? 181 ARG A HB2  1 
ATOM   2932 H  HB3  . ARG A 1 181 ? -2.680  4.538   32.888 1.00 13.86  ? 181 ARG A HB3  1 
ATOM   2933 H  HG2  . ARG A 1 181 ? -3.750  5.393   30.388 1.00 13.77  ? 181 ARG A HG2  1 
ATOM   2934 H  HG3  . ARG A 1 181 ? -2.207  5.403   30.760 1.00 13.77  ? 181 ARG A HG3  1 
ATOM   2935 H  HD2  . ARG A 1 181 ? -2.215  3.043   30.873 1.00 12.92  ? 181 ARG A HD2  1 
ATOM   2936 H  HD3  . ARG A 1 181 ? -3.758  3.027   30.517 1.00 12.93  ? 181 ARG A HD3  1 
ATOM   2937 H  HE   . ARG A 1 181 ? -3.240  3.285   28.395 1.00 15.37  ? 181 ARG A HE   1 
ATOM   2938 H  HH11 . ARG A 1 181 ? -0.247  4.271   29.872 1.00 13.53  ? 181 ARG A HH11 1 
ATOM   2939 H  HH12 . ARG A 1 181 ? 0.339   3.126   29.048 1.00 13.53  ? 181 ARG A HH12 1 
ATOM   2940 H  HH21 . ARG A 1 181 ? -1.970  4.165   26.669 1.00 15.37  ? 181 ARG A HH21 1 
ATOM   2941 H  HH22 . ARG A 1 181 ? -0.505  3.750   26.737 1.00 15.37  ? 181 ARG A HH22 1 
ATOM   2942 N  N    . LEU A 1 182 ? -4.643  3.222   34.879 1.00 10.55  ? 182 LEU A N    1 
ATOM   2943 C  CA   . LEU A 1 182 ? -4.960  2.996   36.270 1.00 11.47  ? 182 LEU A CA   1 
ATOM   2944 C  C    . LEU A 1 182 ? -3.696  2.642   37.037 1.00 11.04  ? 182 LEU A C    1 
ATOM   2945 O  O    . LEU A 1 182 ? -2.773  2.025   36.479 1.00 11.45  ? 182 LEU A O    1 
ATOM   2946 C  CB   . LEU A 1 182 ? -5.883  1.787   36.431 1.00 12.59  ? 182 LEU A CB   1 
ATOM   2947 C  CG   . LEU A 1 182 ? -7.264  1.775   35.813 1.00 14.70  ? 182 LEU A CG   1 
ATOM   2948 C  CD1  . LEU A 1 182 ? -8.044  3.023   36.059 1.00 14.22  ? 182 LEU A CD1  1 
ATOM   2949 C  CD2  . LEU A 1 182 ? -7.255  1.371   34.388 1.00 14.68  ? 182 LEU A CD2  1 
ATOM   2950 H  H    . LEU A 1 182 ? -4.155  2.579   34.451 1.00 12.93  ? 182 LEU A H    1 
ATOM   2951 H  HA   . LEU A 1 182 ? -5.371  3.802   36.652 1.00 14.05  ? 182 LEU A HA   1 
ATOM   2952 H  HB2  . LEU A 1 182 ? -5.402  1.010   36.083 1.00 15.97  ? 182 LEU A HB2  1 
ATOM   2953 H  HB3  . LEU A 1 182 ? -5.995  1.637   37.390 1.00 15.97  ? 182 LEU A HB3  1 
ATOM   2954 H  HG   . LEU A 1 182 ? -7.757  1.059   36.286 1.00 17.50  ? 182 LEU A HG   1 
ATOM   2955 H  HD11 . LEU A 1 182 ? -8.960  2.898   35.756 1.00 16.93  ? 182 LEU A HD11 1 
ATOM   2956 H  HD12 . LEU A 1 182 ? -8.042  3.224   37.011 1.00 16.93  ? 182 LEU A HD12 1 
ATOM   2957 H  HD13 . LEU A 1 182 ? -7.639  3.761   35.571 1.00 16.93  ? 182 LEU A HD13 1 
ATOM   2958 H  HD21 . LEU A 1 182 ? -8.170  1.258   34.077 1.00 15.97  ? 182 LEU A HD21 1 
ATOM   2959 H  HD22 . LEU A 1 182 ? -6.816  2.058   33.857 1.00 15.97  ? 182 LEU A HD22 1 
ATOM   2960 H  HD23 . LEU A 1 182 ? -6.775  0.530   34.290 1.00 15.97  ? 182 LEU A HD23 1 
ATOM   2961 N  N    . VAL A 1 183 ? -3.705  2.949   38.339 1.00 11.67  ? 183 VAL A N    1 
ATOM   2962 C  CA   . VAL A 1 183 ? -2.702  2.425   39.256 1.00 11.67  ? 183 VAL A CA   1 
ATOM   2963 C  C    . VAL A 1 183 ? -3.425  1.827   40.452 1.00 12.12  ? 183 VAL A C    1 
ATOM   2964 O  O    . VAL A 1 183 ? -4.395  2.400   40.960 1.00 12.42  ? 183 VAL A O    1 
ATOM   2965 C  CB   . VAL A 1 183 ? -1.687  3.503   39.676 1.00 14.24  ? 183 VAL A CB   1 
ATOM   2966 C  CG1  . VAL A 1 183 ? -0.889  3.103   40.877 1.00 18.86  ? 183 VAL A CG1  1 
ATOM   2967 C  CG2  . VAL A 1 183 ? -0.844  3.952   38.515 1.00 14.86  ? 183 VAL A CG2  1 
ATOM   2968 H  H    . VAL A 1 183 ? -4.355  3.502   38.667 1.00 14.05  ? 183 VAL A H    1 
ATOM   2969 H  HA   . VAL A 1 183 ? -2.219  1.713   38.804 1.00 16.15  ? 183 VAL A HA   1 
ATOM   2970 H  HB   . VAL A 1 183 ? -2.223  4.288   39.948 1.00 23.88  ? 183 VAL A HB   1 
ATOM   2971 H  HG11 . VAL A 1 183 ? -0.242  3.799   41.082 1.00 23.31  ? 183 VAL A HG11 1 
ATOM   2972 H  HG12 . VAL A 1 183 ? -1.481  2.982   41.640 1.00 23.30  ? 183 VAL A HG12 1 
ATOM   2973 H  HG13 . VAL A 1 183 ? -0.421  2.270   40.695 1.00 23.31  ? 183 VAL A HG13 1 
ATOM   2974 H  HG21 . VAL A 1 183 ? -0.216  4.633   38.814 1.00 17.62  ? 183 VAL A HG21 1 
ATOM   2975 H  HG22 . VAL A 1 183 ? -0.352  3.192   38.158 1.00 17.62  ? 183 VAL A HG22 1 
ATOM   2976 H  HG23 . VAL A 1 183 ? -1.416  4.322   37.821 1.00 17.62  ? 183 VAL A HG23 1 
ATOM   2977 N  N    . HIS A 1 184 ? -2.949  0.680   40.916 1.00 12.63  ? 184 HIS A N    1 
ATOM   2978 C  CA   . HIS A 1 184 ? -3.607  0.003   42.023 1.00 13.01  ? 184 HIS A CA   1 
ATOM   2979 C  C    . HIS A 1 184 ? -3.356  0.767   43.312 1.00 13.33  ? 184 HIS A C    1 
ATOM   2980 O  O    . HIS A 1 184 ? -2.247  1.166   43.605 1.00 13.84  ? 184 HIS A O    1 
ATOM   2981 C  CB   . HIS A 1 184 ? -3.115  -1.440  42.106 1.00 13.41  ? 184 HIS A CB   1 
ATOM   2982 C  CG   . HIS A 1 184 ? -4.002  -2.329  42.897 1.00 14.26  ? 184 HIS A CG   1 
ATOM   2983 N  ND1  . HIS A 1 184 ? -4.161  -2.302  44.266 1.00 16.60  ? 184 HIS A ND1  1 
ATOM   2984 C  CD2  . HIS A 1 184 ? -4.787  -3.310  42.436 1.00 15.97  ? 184 HIS A CD2  1 
ATOM   2985 C  CE1  . HIS A 1 184 ? -5.042  -3.232  44.603 1.00 17.71  ? 184 HIS A CE1  1 
ATOM   2986 N  NE2  . HIS A 1 184 ? -5.431  -3.847  43.503 1.00 16.85  ? 184 HIS A NE2  1 
ATOM   2987 H  H    . HIS A 1 184 ? -2.200  0.310   40.546 1.00 16.15  ? 184 HIS A H    1 
ATOM   2988 H  HA   . HIS A 1 184 ? -4.580  -0.004  41.846 1.00 25.67  ? 184 HIS A HA   1 
ATOM   2989 H  HB2  . HIS A 1 184 ? -3.035  -1.798  41.197 1.00 16.15  ? 184 HIS A HB2  1 
ATOM   2990 H  HB3  . HIS A 1 184 ? -2.220  -1.444  42.509 1.00 16.15  ? 184 HIS A HB3  1 
ATOM   2991 H  HD1  . HIS A 1 184 ? -3.760  -1.747  44.819 1.00 39.91  ? 184 HIS A HD1  1 
ATOM   2992 H  HD2  . HIS A 1 184 ? -4.899  -3.567  41.543 1.00 39.91  ? 184 HIS A HD2  1 
ATOM   2993 H  HE1  . HIS A 1 184 ? -5.329  -3.427  45.477 1.00 39.90  ? 184 HIS A HE1  1 
ATOM   2994 N  N    . GLU A 1 185 ? -4.403  0.873   44.130 1.00 14.80  ? 185 GLU A N    1 
ATOM   2995 C  CA   . GLU A 1 185 ? -4.246  1.461   45.454 1.00 16.88  ? 185 GLU A CA   1 
ATOM   2996 C  C    . GLU A 1 185 ? -3.264  0.644   46.294 1.00 17.52  ? 185 GLU A C    1 
ATOM   2997 O  O    . GLU A 1 185 ? -3.084  -0.571  46.113 1.00 18.10  ? 185 GLU A O    1 
ATOM   2998 C  CB   . GLU A 1 185 ? -5.599  1.537   46.158 1.00 20.11  ? 185 GLU A CB   1 
ATOM   2999 C  CG   . GLU A 1 185 ? -6.125  0.193   46.629 1.00 22.47  ? 185 GLU A CG   1 
ATOM   3000 C  CD   . GLU A 1 185 ? -7.518  0.235   47.232 1.00 25.88  ? 185 GLU A CD   1 
ATOM   3001 O  OE1  . GLU A 1 185 ? -8.223  1.259   47.090 1.00 28.50  ? 185 GLU A OE1  1 
ATOM   3002 O  OE2  . GLU A 1 185 ? -7.892  -0.766  47.847 1.00 32.62  ? 185 GLU A OE2  1 
ATOM   3003 H  H    . GLU A 1 185 ? -5.227  0.577   43.866 1.00 25.67  ? 185 GLU A H    1 
ATOM   3004 H  HA   . GLU A 1 185 ? -3.892  2.373   45.346 1.00 25.66  ? 185 GLU A HA   1 
ATOM   3005 H  HB2  . GLU A 1 185 ? -5.517  2.134   46.930 1.00 25.67  ? 185 GLU A HB2  1 
ATOM   3006 H  HB3  . GLU A 1 185 ? -6.248  1.933   45.540 1.00 25.67  ? 185 GLU A HB3  1 
ATOM   3007 H  HG2  . GLU A 1 185 ? -6.135  -0.428  45.870 1.00 26.14  ? 185 GLU A HG2  1 
ATOM   3008 H  HG3  . GLU A 1 185 ? -5.512  -0.172  47.302 1.00 26.14  ? 185 GLU A HG3  1 
ATOM   3009 N  N    . PRO A 1 186 ? -2.581  1.284   47.263 1.00 20.06  ? 186 PRO A N    1 
ATOM   3010 C  CA   . PRO A 1 186 ? -1.578  0.588   48.078 1.00 23.43  ? 186 PRO A CA   1 
ATOM   3011 C  C    . PRO A 1 186 ? -2.097  -0.431  49.101 1.00 27.37  ? 186 PRO A C    1 
ATOM   3012 O  O    . PRO A 1 186 ? -3.277  -0.403  49.307 1.00 26.53  ? 186 PRO A O    1 
ATOM   3013 C  CB   . PRO A 1 186 ? -0.870  1.730   48.837 1.00 26.17  ? 186 PRO A CB   1 
ATOM   3014 C  CG   . PRO A 1 186 ? -1.875  2.859   48.872 1.00 26.14  ? 186 PRO A CG   1 
ATOM   3015 C  CD   . PRO A 1 186 ? -2.689  2.711   47.604 1.00 21.83  ? 186 PRO A CD   1 
ATOM   3016 H  HA   . PRO A 1 186 ? -0.928  0.148   47.476 1.00 26.30  ? 186 PRO A HA   1 
ATOM   3017 H  HB2  . PRO A 1 186 ? -0.631  1.451   49.747 1.00 26.28  ? 186 PRO A HB2  1 
ATOM   3018 H  HB3  . PRO A 1 186 ? -0.055  2.008   48.369 1.00 26.28  ? 186 PRO A HB3  1 
ATOM   3019 H  HG2  . PRO A 1 186 ? -2.449  2.787   49.661 1.00 26.07  ? 186 PRO A HG2  1 
ATOM   3020 H  HG3  . PRO A 1 186 ? -1.421  3.726   48.891 1.00 26.07  ? 186 PRO A HG3  1 
ATOM   3021 H  HD2  . PRO A 1 186 ? -3.618  2.964   47.758 1.00 25.66  ? 186 PRO A HD2  1 
ATOM   3022 H  HD3  . PRO A 1 186 ? -2.326  3.267   46.890 1.00 25.66  ? 186 PRO A HD3  1 
ATOM   3023 N  N    . THR B 1 3   ? -33.302 -5.895  13.835 1.00 28.21  ? 3   THR B N    1 
ATOM   3024 C  CA   . THR B 1 3   ? -33.391 -6.504  15.189 1.00 22.67  ? 3   THR B CA   1 
ATOM   3025 C  C    . THR B 1 3   ? -32.511 -7.753  15.201 1.00 16.91  ? 3   THR B C    1 
ATOM   3026 O  O    . THR B 1 3   ? -32.606 -8.593  14.318 1.00 20.36  ? 3   THR B O    1 
ATOM   3027 C  CB   . THR B 1 3   ? -34.836 -6.958  15.442 1.00 28.39  ? 3   THR B CB   1 
ATOM   3028 O  OG1  . THR B 1 3   ? -35.588 -5.743  15.545 1.00 37.34  ? 3   THR B OG1  1 
ATOM   3029 C  CG2  . THR B 1 3   ? -35.019 -7.791  16.692 1.00 26.03  ? 3   THR B CG2  1 
ATOM   3030 N  N    . ARG B 1 4   ? -31.669 -7.881  16.239 1.00 14.43  ? 4   ARG B N    1 
ATOM   3031 C  CA   . ARG B 1 4   ? -30.840 -9.062  16.415 1.00 11.73  ? 4   ARG B CA   1 
ATOM   3032 C  C    . ARG B 1 4   ? -31.331 -10.006 17.513 1.00 10.98  ? 4   ARG B C    1 
ATOM   3033 O  O    . ARG B 1 4   ? -31.035 -11.187 17.474 1.00 10.54  ? 4   ARG B O    1 
ATOM   3034 C  CB   . ARG B 1 4   ? -29.413 -8.616  16.703 1.00 11.80  ? 4   ARG B CB   1 
ATOM   3035 C  CG   . ARG B 1 4   ? -28.753 -7.886  15.546 1.00 12.09  ? 4   ARG B CG   1 
ATOM   3036 C  CD   . ARG B 1 4   ? -27.405 -7.305  15.914 1.00 12.06  ? 4   ARG B CD   1 
ATOM   3037 N  NE   . ARG B 1 4   ? -26.504 -8.355  16.370 1.00 11.48  ? 4   ARG B NE   1 
ATOM   3038 C  CZ   . ARG B 1 4   ? -25.630 -8.267  17.360 1.00 9.93   ? 4   ARG B CZ   1 
ATOM   3039 N  NH1  . ARG B 1 4   ? -25.368 -7.116  17.941 1.00 10.59  ? 4   ARG B NH1  1 
ATOM   3040 N  NH2  . ARG B 1 4   ? -25.035 -9.369  17.778 1.00 10.39  ? 4   ARG B NH2  1 
ATOM   3041 H  HA   . ARG B 1 4   ? -30.837 -9.561  15.567 1.00 18.64  ? 4   ARG B HA   1 
ATOM   3042 H  HB2  . ARG B 1 4   ? -29.421 -8.027  17.486 1.00 14.13  ? 4   ARG B HB2  1 
ATOM   3043 H  HB3  . ARG B 1 4   ? -28.877 -9.406  16.925 1.00 14.13  ? 4   ARG B HB3  1 
ATOM   3044 H  HG2  . ARG B 1 4   ? -28.637 -8.508  14.796 1.00 14.44  ? 4   ARG B HG2  1 
ATOM   3045 H  HG3  . ARG B 1 4   ? -29.339 -7.159  15.245 1.00 14.44  ? 4   ARG B HG3  1 
ATOM   3046 H  HD2  . ARG B 1 4   ? -27.017 -6.857  15.132 1.00 13.37  ? 4   ARG B HD2  1 
ATOM   3047 H  HD3  . ARG B 1 4   ? -27.520 -6.638  16.623 1.00 13.37  ? 4   ARG B HD3  1 
ATOM   3048 H  HE   . ARG B 1 4   ? -26.540 -9.117  15.946 1.00 13.29  ? 4   ARG B HE   1 
ATOM   3049 H  HH11 . ARG B 1 4   ? -25.129 -6.422  17.452 1.00 13.35  ? 4   ARG B HH11 1 
ATOM   3050 H  HH12 . ARG B 1 4   ? -25.431 -7.042  18.816 1.00 13.35  ? 4   ARG B HH12 1 
ATOM   3051 H  HH21 . ARG B 1 4   ? -25.398 -10.153 17.617 1.00 13.29  ? 4   ARG B HH21 1 
ATOM   3052 H  HH22 . ARG B 1 4   ? -24.276 -9.315  18.219 1.00 13.29  ? 4   ARG B HH22 1 
ATOM   3053 N  N    . VAL B 1 5   ? -31.992 -9.466  18.536 1.00 11.39  ? 5   VAL B N    1 
ATOM   3054 C  CA   . VAL B 1 5   ? -32.394 -10.230 19.699 1.00 11.08  ? 5   VAL B CA   1 
ATOM   3055 C  C    . VAL B 1 5   ? -33.792 -10.792 19.495 1.00 10.85  ? 5   VAL B C    1 
ATOM   3056 O  O    . VAL B 1 5   ? -34.709 -10.042 19.133 1.00 11.92  ? 5   VAL B O    1 
ATOM   3057 C  CB   . VAL B 1 5   ? -32.344 -9.392  20.987 1.00 12.17  ? 5   VAL B CB   1 
ATOM   3058 C  CG1  . VAL B 1 5   ? -32.874 -10.157 22.199 1.00 13.03  ? 5   VAL B CG1  1 
ATOM   3059 C  CG2  . VAL B 1 5   ? -30.924 -8.905  21.258 1.00 14.62  ? 5   VAL B CG2  1 
ATOM   3060 H  H    . VAL B 1 5   ? -32.198 -8.576  18.511 1.00 14.05  ? 5   VAL B H    1 
ATOM   3061 H  HA   . VAL B 1 5   ? -31.776 -10.975 19.800 1.00 12.82  ? 5   VAL B HA   1 
ATOM   3062 H  HB   . VAL B 1 5   ? -32.918 -8.599  20.852 1.00 14.06  ? 5   VAL B HB   1 
ATOM   3063 H  HG11 . VAL B 1 5   ? -32.535 -9.750  23.016 1.00 16.49  ? 5   VAL B HG11 1 
ATOM   3064 H  HG12 . VAL B 1 5   ? -33.846 -10.128 22.204 1.00 16.49  ? 5   VAL B HG12 1 
ATOM   3065 H  HG13 . VAL B 1 5   ? -32.578 -11.083 22.154 1.00 16.49  ? 5   VAL B HG13 1 
ATOM   3066 H  HG21 . VAL B 1 5   ? -30.909 -8.386  22.081 1.00 16.50  ? 5   VAL B HG21 1 
ATOM   3067 H  HG22 . VAL B 1 5   ? -30.330 -9.670  21.348 1.00 16.50  ? 5   VAL B HG22 1 
ATOM   3068 H  HG23 . VAL B 1 5   ? -30.624 -8.348  20.519 1.00 16.50  ? 5   VAL B HG23 1 
ATOM   3069 N  N    . PHE B 1 6   ? -33.941 -12.087 19.775 1.00 10.37  ? 6   PHE B N    1 
ATOM   3070 C  CA   . PHE B 1 6   ? -35.224 -12.744 19.707 1.00 10.77  ? 6   PHE B CA   1 
ATOM   3071 C  C    . PHE B 1 6   ? -35.439 -13.554 20.971 1.00 10.21  ? 6   PHE B C    1 
ATOM   3072 O  O    . PHE B 1 6   ? -34.508 -14.177 21.482 1.00 10.99  ? 6   PHE B O    1 
ATOM   3073 C  CB   . PHE B 1 6   ? -35.344 -13.619 18.463 1.00 12.15  ? 6   PHE B CB   1 
ATOM   3074 C  CG   . PHE B 1 6   ? -35.352 -12.810 17.194 1.00 12.46  ? 6   PHE B CG   1 
ATOM   3075 C  CD1  . PHE B 1 6   ? -34.143 -12.457 16.597 1.00 12.57  ? 6   PHE B CD1  1 
ATOM   3076 C  CD2  . PHE B 1 6   ? -36.537 -12.304 16.639 1.00 14.53  ? 6   PHE B CD2  1 
ATOM   3077 C  CE1  . PHE B 1 6   ? -34.106 -11.671 15.463 1.00 14.71  ? 6   PHE B CE1  1 
ATOM   3078 C  CE2  . PHE B 1 6   ? -36.493 -11.508 15.495 1.00 16.40  ? 6   PHE B CE2  1 
ATOM   3079 C  CZ   . PHE B 1 6   ? -35.280 -11.216 14.908 1.00 17.25  ? 6   PHE B CZ   1 
ATOM   3080 H  H    . PHE B 1 6   ? -33.210 -12.579 20.018 1.00 12.82  ? 6   PHE B H    1 
ATOM   3081 H  HA   . PHE B 1 6   ? -35.927 -12.049 19.665 1.00 12.79  ? 6   PHE B HA   1 
ATOM   3082 H  HB2  . PHE B 1 6   ? -34.591 -14.246 18.443 1.00 14.51  ? 6   PHE B HB2  1 
ATOM   3083 H  HB3  . PHE B 1 6   ? -36.173 -14.139 18.520 1.00 14.51  ? 6   PHE B HB3  1 
ATOM   3084 H  HD1  . PHE B 1 6   ? -33.335 -12.772 16.970 1.00 17.81  ? 6   PHE B HD1  1 
ATOM   3085 H  HD2  . PHE B 1 6   ? -37.367 -12.512 17.038 1.00 17.81  ? 6   PHE B HD2  1 
ATOM   3086 H  HE1  . PHE B 1 6   ? -33.279 -11.466 15.057 1.00 17.81  ? 6   PHE B HE1  1 
ATOM   3087 H  HE2  . PHE B 1 6   ? -37.295 -11.195 15.107 1.00 17.81  ? 6   PHE B HE2  1 
ATOM   3088 H  HZ   . PHE B 1 6   ? -35.254 -10.681 14.131 1.00 17.81  ? 6   PHE B HZ   1 
ATOM   3089 N  N    . THR B 1 7   ? -36.699 -13.593 21.412 1.00 10.23  ? 7   THR B N    1 
ATOM   3090 C  CA   . THR B 1 7   ? -37.076 -14.356 22.577 1.00 10.78  ? 7   THR B CA   1 
ATOM   3091 C  C    . THR B 1 7   ? -38.213 -15.300 22.223 1.00 10.45  ? 7   THR B C    1 
ATOM   3092 O  O    . THR B 1 7   ? -39.231 -14.853 21.702 1.00 12.00  ? 7   THR B O    1 
ATOM   3093 C  CB   . THR B 1 7   ? -37.490 -13.436 23.731 1.00 11.77  ? 7   THR B CB   1 
ATOM   3094 O  OG1  . THR B 1 7   ? -36.503 -12.438 23.982 1.00 12.58  ? 7   THR B OG1  1 
ATOM   3095 C  CG2  . THR B 1 7   ? -37.690 -14.196 25.012 1.00 14.26  ? 7   THR B CG2  1 
ATOM   3096 H  H    . THR B 1 7   ? -37.346 -13.125 20.966 1.00 12.79  ? 7   THR B H    1 
ATOM   3097 H  HA   . THR B 1 7   ? -36.300 -14.888 22.863 1.00 14.90  ? 7   THR B HA   1 
ATOM   3098 H  HB   . THR B 1 7   ? -38.338 -12.993 23.487 1.00 15.94  ? 7   THR B HB   1 
ATOM   3099 H  HG1  . THR B 1 7   ? -36.638 -11.771 23.475 1.00 15.94  ? 7   THR B HG1  1 
ATOM   3100 H  HG21 . THR B 1 7   ? -37.894 -13.573 25.732 1.00 16.63  ? 7   THR B HG21 1 
ATOM   3101 H  HG22 . THR B 1 7   ? -38.428 -14.822 24.907 1.00 16.63  ? 7   THR B HG22 1 
ATOM   3102 H  HG23 . THR B 1 7   ? -36.878 -14.688 25.229 1.00 16.63  ? 7   THR B HG23 1 
ATOM   3103 N  N    . PHE B 1 8   ? -38.022 -16.572 22.526 1.00 10.69  ? 8   PHE B N    1 
ATOM   3104 C  CA   . PHE B 1 8   ? -38.948 -17.642 22.217 1.00 10.76  ? 8   PHE B CA   1 
ATOM   3105 C  C    . PHE B 1 8   ? -39.649 -18.034 23.512 1.00 10.77  ? 8   PHE B C    1 
ATOM   3106 O  O    . PHE B 1 8   ? -39.002 -18.512 24.458 1.00 11.67  ? 8   PHE B O    1 
ATOM   3107 C  CB   . PHE B 1 8   ? -38.172 -18.828 21.632 1.00 11.07  ? 8   PHE B CB   1 
ATOM   3108 C  CG   . PHE B 1 8   ? -37.514 -18.512 20.321 1.00 10.94  ? 8   PHE B CG   1 
ATOM   3109 C  CD1  . PHE B 1 8   ? -36.276 -17.865 20.283 1.00 11.91  ? 8   PHE B CD1  1 
ATOM   3110 C  CD2  . PHE B 1 8   ? -38.155 -18.797 19.129 1.00 12.69  ? 8   PHE B CD2  1 
ATOM   3111 C  CE1  . PHE B 1 8   ? -35.694 -17.570 19.067 1.00 13.73  ? 8   PHE B CE1  1 
ATOM   3112 C  CE2  . PHE B 1 8   ? -37.582 -18.464 17.917 1.00 14.16  ? 8   PHE B CE2  1 
ATOM   3113 C  CZ   . PHE B 1 8   ? -36.351 -17.850 17.893 1.00 14.41  ? 8   PHE B CZ   1 
ATOM   3114 H  H    . PHE B 1 8   ? -37.251 -16.795 22.965 1.00 14.90  ? 8   PHE B H    1 
ATOM   3115 H  HA   . PHE B 1 8   ? -39.615 -17.326 21.559 1.00 13.33  ? 8   PHE B HA   1 
ATOM   3116 H  HB2  . PHE B 1 8   ? -37.487 -19.103 22.276 1.00 13.27  ? 8   PHE B HB2  1 
ATOM   3117 H  HB3  . PHE B 1 8   ? -38.791 -19.578 21.508 1.00 13.27  ? 8   PHE B HB3  1 
ATOM   3118 H  HD1  . PHE B 1 8   ? -35.824 -17.665 21.087 1.00 13.16  ? 8   PHE B HD1  1 
ATOM   3119 H  HD2  . PHE B 1 8   ? -39.005 -19.208 19.146 1.00 13.19  ? 8   PHE B HD2  1 
ATOM   3120 H  HE1  . PHE B 1 8   ? -34.854 -17.140 19.043 1.00 13.17  ? 8   PHE B HE1  1 
ATOM   3121 H  HE2  . PHE B 1 8   ? -38.022 -18.677 17.110 1.00 13.18  ? 8   PHE B HE2  1 
ATOM   3122 H  HZ   . PHE B 1 8   ? -35.945 -17.642 17.067 1.00 13.18  ? 8   PHE B HZ   1 
ATOM   3123 N  N    . ALA B 1 9   ? -40.967 -17.812 23.567 1.00 11.20  ? 9   ALA B N    1 
ATOM   3124 C  CA   . ALA B 1 9   ? -41.767 -18.076 24.758 1.00 11.60  ? 9   ALA B CA   1 
ATOM   3125 C  C    . ALA B 1 9   ? -42.603 -19.317 24.492 1.00 11.49  ? 9   ALA B C    1 
ATOM   3126 O  O    . ALA B 1 9   ? -43.475 -19.312 23.615 1.00 12.72  ? 9   ALA B O    1 
ATOM   3127 C  CB   . ALA B 1 9   ? -42.651 -16.894 25.068 1.00 13.62  ? 9   ALA B CB   1 
ATOM   3128 H  H    . ALA B 1 9   ? -41.389 -17.479 22.827 1.00 13.33  ? 9   ALA B H    1 
ATOM   3129 H  HA   . ALA B 1 9   ? -41.169 -18.245 25.521 1.00 19.10  ? 9   ALA B HA   1 
ATOM   3130 H  HB1  . ALA B 1 9   ? -43.161 -17.073 25.876 1.00 19.83  ? 9   ALA B HB1  1 
ATOM   3131 H  HB2  . ALA B 1 9   ? -42.101 -16.104 25.202 1.00 19.83  ? 9   ALA B HB2  1 
ATOM   3132 H  HB3  . ALA B 1 9   ? -43.261 -16.741 24.328 1.00 19.85  ? 9   ALA B HB3  1 
ATOM   3133 N  N    . GLY B 1 10  ? -42.391 -20.371 25.274 1.00 11.58  ? 10  GLY B N    1 
ATOM   3134 C  CA   . GLY B 1 10  ? -43.223 -21.552 25.189 1.00 12.20  ? 10  GLY B CA   1 
ATOM   3135 C  C    . GLY B 1 10  ? -44.290 -21.462 26.263 1.00 12.09  ? 10  GLY B C    1 
ATOM   3136 O  O    . GLY B 1 10  ? -43.989 -21.203 27.418 1.00 12.43  ? 10  GLY B O    1 
ATOM   3137 H  H    . GLY B 1 10  ? -41.706 -20.357 25.879 1.00 19.10  ? 10  GLY B H    1 
ATOM   3138 H  HA2  . GLY B 1 10  ? -43.640 -21.607 24.294 1.00 22.06  ? 10  GLY B HA2  1 
ATOM   3139 H  HA3  . GLY B 1 10  ? -42.662 -22.344 25.342 1.00 22.06  ? 10  GLY B HA3  1 
ATOM   3140 N  N    . GLY B 1 11  ? -45.555 -21.660 25.881 1.00 12.22  ? 11  GLY B N    1 
ATOM   3141 C  CA   . GLY B 1 11  ? -46.627 -21.517 26.855 1.00 13.05  ? 11  GLY B CA   1 
ATOM   3142 C  C    . GLY B 1 11  ? -47.991 -21.653 26.212 1.00 13.67  ? 11  GLY B C    1 
ATOM   3143 O  O    . GLY B 1 11  ? -48.158 -22.346 25.209 1.00 14.11  ? 11  GLY B O    1 
ATOM   3144 H  H    . GLY B 1 11  ? -45.754 -21.884 25.017 1.00 22.05  ? 11  GLY B H    1 
ATOM   3145 H  HA2  . GLY B 1 11  ? -46.522 -22.212 27.552 1.00 24.49  ? 11  GLY B HA2  1 
ATOM   3146 H  HA3  . GLY B 1 11  ? -46.552 -20.632 27.289 1.00 24.50  ? 11  GLY B HA3  1 
ATOM   3147 N  N    . GLU B 1 12  ? -48.954 -20.971 26.813 1.00 14.70  ? 12  GLU B N    1 
ATOM   3148 C  CA   . GLU B 1 12  ? -50.354 -21.180 26.467 1.00 17.28  ? 12  GLU B CA   1 
ATOM   3149 C  C    . GLU B 1 12  ? -50.815 -20.337 25.284 1.00 19.67  ? 12  GLU B C    1 
ATOM   3150 O  O    . GLU B 1 12  ? -51.926 -20.550 24.799 1.00 21.10  ? 12  GLU B O    1 
ATOM   3151 C  CB   . GLU B 1 12  ? -51.240 -20.922 27.701 1.00 18.67  ? 12  GLU B CB   1 
ATOM   3152 C  CG   . GLU B 1 12  ? -51.107 -21.993 28.780 1.00 19.08  ? 12  GLU B CG   1 
ATOM   3153 C  CD   . GLU B 1 12  ? -51.405 -23.435 28.345 1.00 17.93  ? 12  GLU B CD   1 
ATOM   3154 O  OE1  . GLU B 1 12  ? -50.557 -24.340 28.589 1.00 21.76  ? 12  GLU B OE1  1 
ATOM   3155 O  OE2  . GLU B 1 12  ? -52.540 -23.679 27.826 1.00 20.11  ? 12  GLU B OE2  1 
ATOM   3156 H  H    . GLU B 1 12  ? -48.744 -20.356 27.455 1.00 24.36  ? 12  GLU B H    1 
ATOM   3157 H  HA   . GLU B 1 12  ? -50.459 -22.125 26.215 1.00 19.00  ? 12  GLU B HA   1 
ATOM   3158 H  HB2  . GLU B 1 12  ? -50.998 -20.052 28.084 1.00 24.20  ? 12  GLU B HB2  1 
ATOM   3159 H  HB3  . GLU B 1 12  ? -52.175 -20.875 27.413 1.00 24.20  ? 12  GLU B HB3  1 
ATOM   3160 H  HG2  . GLU B 1 12  ? -50.194 -21.966 29.136 1.00 21.64  ? 12  GLU B HG2  1 
ATOM   3161 H  HG3  . GLU B 1 12  ? -51.712 -21.768 29.518 1.00 21.64  ? 12  GLU B HG3  1 
ATOM   3162 N  N    . THR B 1 13  ? -50.024 -19.340 24.867 1.00 18.82  ? 13  THR B N    1 
ATOM   3163 C  CA   . THR B 1 13  ? -50.404 -18.422 23.800 1.00 21.51  ? 13  THR B CA   1 
ATOM   3164 C  C    . THR B 1 13  ? -49.265 -18.309 22.778 1.00 21.31  ? 13  THR B C    1 
ATOM   3165 O  O    . THR B 1 13  ? -48.082 -18.444 23.081 1.00 22.98  ? 13  THR B O    1 
ATOM   3166 C  CB   . THR B 1 13  ? -50.837 -17.050 24.342 1.00 24.79  ? 13  THR B CB   1 
ATOM   3167 O  OG1  . THR B 1 13  ? -49.667 -16.368 24.795 1.00 29.89  ? 13  THR B OG1  1 
ATOM   3168 C  CG2  . THR B 1 13  ? -51.848 -17.145 25.462 1.00 27.65  ? 13  THR B CG2  1 
ATOM   3169 H  H    . THR B 1 13  ? -49.210 -19.224 25.267 1.00 21.35  ? 13  THR B H    1 
ATOM   3170 H  HA   . THR B 1 13  ? -51.179 -18.816 23.337 1.00 23.51  ? 13  THR B HA   1 
ATOM   3171 H  HB   . THR B 1 13  ? -51.236 -16.537 23.599 1.00 26.22  ? 13  THR B HB   1 
ATOM   3172 H  HG1  . THR B 1 13  ? -49.853 -15.557 24.954 1.00 29.35  ? 13  THR B HG1  1 
ATOM   3173 H  HG21 . THR B 1 13  ? -52.210 -16.261 25.650 1.00 27.10  ? 13  THR B HG21 1 
ATOM   3174 H  HG22 . THR B 1 13  ? -52.571 -17.741 25.199 1.00 27.10  ? 13  THR B HG22 1 
ATOM   3175 H  HG23 . THR B 1 13  ? -51.416 -17.495 26.262 1.00 27.10  ? 13  THR B HG23 1 
ATOM   3176 N  N    . GLY B 1 14  ? -49.631 -18.071 21.527 1.00 21.91  ? 14  GLY B N    1 
ATOM   3177 C  CA   . GLY B 1 14  ? -48.658 -17.812 20.483 1.00 20.35  ? 14  GLY B CA   1 
ATOM   3178 C  C    . GLY B 1 14  ? -49.203 -18.208 19.114 1.00 20.05  ? 14  GLY B C    1 
ATOM   3179 O  O    . GLY B 1 14  ? -50.113 -19.026 18.998 1.00 20.68  ? 14  GLY B O    1 
ATOM   3180 H  H    . GLY B 1 14  ? -50.519 -18.067 21.312 1.00 23.51  ? 14  GLY B H    1 
ATOM   3181 H  HA2  . GLY B 1 14  ? -48.431 -16.849 20.483 1.00 28.90  ? 14  GLY B HA2  1 
ATOM   3182 H  HA3  . GLY B 1 14  ? -47.832 -18.326 20.669 1.00 28.90  ? 14  GLY B HA3  1 
ATOM   3183 N  N    . VAL B 1 15  ? -48.613 -17.645 18.059 1.00 20.02  ? 15  VAL B N    1 
ATOM   3184 C  CA   . VAL B 1 15  ? -49.100 -17.921 16.714 1.00 21.66  ? 15  VAL B CA   1 
ATOM   3185 C  C    . VAL B 1 15  ? -48.649 -19.288 16.197 1.00 18.90  ? 15  VAL B C    1 
ATOM   3186 O  O    . VAL B 1 15  ? -49.182 -19.738 15.191 1.00 21.31  ? 15  VAL B O    1 
ATOM   3187 C  CB   . VAL B 1 15  ? -48.734 -16.822 15.699 1.00 25.90  ? 15  VAL B CB   1 
ATOM   3188 C  CG1  . VAL B 1 15  ? -49.257 -15.455 16.141 1.00 30.45  ? 15  VAL B CG1  1 
ATOM   3189 C  CG2  . VAL B 1 15  ? -47.237 -16.790 15.402 1.00 27.11  ? 15  VAL B CG2  1 
ATOM   3190 H  H    . VAL B 1 15  ? -47.903 -17.081 18.174 1.00 29.11  ? 15  VAL B H    1 
ATOM   3191 H  HA   . VAL B 1 15  ? -50.072 -17.945 16.765 1.00 23.96  ? 15  VAL B HA   1 
ATOM   3192 H  HB   . VAL B 1 15  ? -49.193 -17.049 14.854 1.00 26.80  ? 15  VAL B HB   1 
ATOM   3193 H  HG11 . VAL B 1 15  ? -49.027 -14.787 15.472 1.00 32.42  ? 15  VAL B HG11 1 
ATOM   3194 H  HG12 . VAL B 1 15  ? -50.224 -15.495 16.240 1.00 32.45  ? 15  VAL B HG12 1 
ATOM   3195 H  HG13 . VAL B 1 15  ? -48.855 -15.211 16.992 1.00 32.47  ? 15  VAL B HG13 1 
ATOM   3196 H  HG21 . VAL B 1 15  ? -47.015 -15.963 14.941 1.00 29.36  ? 15  VAL B HG21 1 
ATOM   3197 H  HG22 . VAL B 1 15  ? -46.738 -16.840 16.235 1.00 29.31  ? 15  VAL B HG22 1 
ATOM   3198 H  HG23 . VAL B 1 15  ? -47.001 -17.547 14.838 1.00 29.33  ? 15  VAL B HG23 1 
ATOM   3199 N  N    . TRP B 1 16  ? -47.675 -19.930 16.848 1.00 15.72  ? 16  TRP B N    1 
ATOM   3200 C  CA   . TRP B 1 16  ? -47.207 -21.247 16.440 1.00 14.71  ? 16  TRP B CA   1 
ATOM   3201 C  C    . TRP B 1 16  ? -47.802 -22.306 17.348 1.00 14.61  ? 16  TRP B C    1 
ATOM   3202 O  O    . TRP B 1 16  ? -47.671 -22.224 18.567 1.00 15.79  ? 16  TRP B O    1 
ATOM   3203 C  CB   . TRP B 1 16  ? -45.696 -21.323 16.499 1.00 14.25  ? 16  TRP B CB   1 
ATOM   3204 C  CG   . TRP B 1 16  ? -45.033 -20.414 15.527 1.00 14.83  ? 16  TRP B CG   1 
ATOM   3205 C  CD1  . TRP B 1 16  ? -44.487 -19.197 15.802 1.00 15.94  ? 16  TRP B CD1  1 
ATOM   3206 C  CD2  . TRP B 1 16  ? -44.805 -20.638 14.119 1.00 15.31  ? 16  TRP B CD2  1 
ATOM   3207 N  NE1  . TRP B 1 16  ? -43.969 -18.637 14.665 1.00 17.02  ? 16  TRP B NE1  1 
ATOM   3208 C  CE2  . TRP B 1 16  ? -44.148 -19.490 13.608 1.00 16.23  ? 16  TRP B CE2  1 
ATOM   3209 C  CE3  . TRP B 1 16  ? -45.132 -21.673 13.231 1.00 16.42  ? 16  TRP B CE3  1 
ATOM   3210 C  CZ2  . TRP B 1 16  ? -43.763 -19.365 12.271 1.00 18.19  ? 16  TRP B CZ2  1 
ATOM   3211 C  CZ3  . TRP B 1 16  ? -44.732 -21.564 11.913 1.00 17.79  ? 16  TRP B CZ3  1 
ATOM   3212 C  CH2  . TRP B 1 16  ? -44.079 -20.422 11.442 1.00 18.37  ? 16  TRP B CH2  1 
ATOM   3213 H  H    . TRP B 1 16  ? -47.278 -19.530 17.567 1.00 17.01  ? 16  TRP B H    1 
ATOM   3214 H  HA   . TRP B 1 16  ? -47.491 -21.411 15.510 1.00 27.35  ? 16  TRP B HA   1 
ATOM   3215 H  HB2  . TRP B 1 16  ? -45.409 -21.093 17.404 1.00 17.40  ? 16  TRP B HB2  1 
ATOM   3216 H  HB3  . TRP B 1 16  ? -45.422 -22.244 16.319 1.00 17.40  ? 16  TRP B HB3  1 
ATOM   3217 H  HD1  . TRP B 1 16  ? -44.494 -18.777 16.648 1.00 17.42  ? 16  TRP B HD1  1 
ATOM   3218 H  HE1  . TRP B 1 16  ? -43.574 -17.855 14.624 1.00 17.42  ? 16  TRP B HE1  1 
ATOM   3219 H  HE3  . TRP B 1 16  ? -45.562 -22.454 13.541 1.00 17.42  ? 16  TRP B HE3  1 
ATOM   3220 H  HZ2  . TRP B 1 16  ? -43.316 -18.599 11.955 1.00 17.42  ? 16  TRP B HZ2  1 
ATOM   3221 H  HZ3  . TRP B 1 16  ? -44.945 -22.255 11.306 1.00 17.42  ? 16  TRP B HZ3  1 
ATOM   3222 H  HH2  . TRP B 1 16  ? -43.847 -20.371 10.531 1.00 17.42  ? 16  TRP B HH2  1 
ATOM   3223 N  N    . ARG B 1 17  ? -48.453 -23.292 16.741 1.00 14.82  ? 17  ARG B N    1 
ATOM   3224 C  CA   . ARG B 1 17  ? -48.944 -24.452 17.462 1.00 15.49  ? 17  ARG B CA   1 
ATOM   3225 C  C    . ARG B 1 17  ? -47.843 -25.491 17.550 1.00 14.86  ? 17  ARG B C    1 
ATOM   3226 O  O    . ARG B 1 17  ? -47.274 -25.882 16.533 1.00 16.11  ? 17  ARG B O    1 
ATOM   3227 C  CB   . ARG B 1 17  ? -50.141 -25.052 16.740 1.00 17.53  ? 17  ARG B CB   1 
ATOM   3228 C  CG   . ARG B 1 17  ? -50.694 -26.285 17.435 1.00 22.78  ? 17  ARG B CG   1 
ATOM   3229 C  CD   . ARG B 1 17  ? -52.072 -26.651 16.944 1.00 30.61  ? 17  ARG B CD   1 
ATOM   3230 N  NE   . ARG B 1 17  ? -52.046 -27.273 15.630 1.00 37.02  ? 17  ARG B NE   1 
ATOM   3231 C  CZ   . ARG B 1 17  ? -52.044 -26.634 14.458 1.00 43.26  ? 17  ARG B CZ   1 
ATOM   3232 N  NH1  . ARG B 1 17  ? -51.998 -25.307 14.401 1.00 45.75  ? 17  ARG B NH1  1 
ATOM   3233 N  NH2  . ARG B 1 17  ? -52.089 -27.339 13.336 1.00 45.72  ? 17  ARG B NH2  1 
ATOM   3234 H  H    . ARG B 1 17  ? -48.599 -23.243 15.840 1.00 27.35  ? 17  ARG B H    1 
ATOM   3235 H  HA   . ARG B 1 17  ? -49.213 -24.179 18.369 1.00 30.20  ? 17  ARG B HA   1 
ATOM   3236 H  HB2  . ARG B 1 17  ? -50.846 -24.375 16.676 1.00 31.22  ? 17  ARG B HB2  1 
ATOM   3237 H  HB3  . ARG B 1 17  ? -49.869 -25.295 15.831 1.00 31.22  ? 17  ARG B HB3  1 
ATOM   3238 H  HG2  . ARG B 1 17  ? -50.091 -27.043 17.282 1.00 27.03  ? 17  ARG B HG2  1 
ATOM   3239 H  HG3  . ARG B 1 17  ? -50.734 -26.121 18.401 1.00 27.03  ? 17  ARG B HG3  1 
ATOM   3240 H  HD2  . ARG B 1 17  ? -52.487 -27.269 17.583 1.00 31.55  ? 17  ARG B HD2  1 
ATOM   3241 H  HD3  . ARG B 1 17  ? -52.626 -25.843 16.907 1.00 31.53  ? 17  ARG B HD3  1 
ATOM   3242 H  HE   . ARG B 1 17  ? -52.030 -28.145 15.605 1.00 29.20  ? 17  ARG B HE   1 
ATOM   3243 H  HH11 . ARG B 1 17  ? -52.640 -24.829 14.768 1.00 31.33  ? 17  ARG B HH11 1 
ATOM   3244 H  HH12 . ARG B 1 17  ? -51.325 -24.909 13.993 1.00 31.33  ? 17  ARG B HH12 1 
ATOM   3245 H  HH21 . ARG B 1 17  ? -51.862 -28.189 13.342 1.00 29.20  ? 17  ARG B HH21 1 
ATOM   3246 H  HH22 . ARG B 1 17  ? -52.344 -26.954 12.588 1.00 29.20  ? 17  ARG B HH22 1 
ATOM   3247 N  N    . VAL B 1 18  ? -47.568 -25.999 18.763 1.00 15.04  ? 18  VAL B N    1 
ATOM   3248 C  CA   . VAL B 1 18  ? -46.578 -27.048 18.952 1.00 14.97  ? 18  VAL B CA   1 
ATOM   3249 C  C    . VAL B 1 18  ? -47.231 -28.380 18.615 1.00 15.78  ? 18  VAL B C    1 
ATOM   3250 O  O    . VAL B 1 18  ? -48.219 -28.779 19.241 1.00 18.14  ? 18  VAL B O    1 
ATOM   3251 C  CB   . VAL B 1 18  ? -46.034 -27.063 20.387 1.00 15.71  ? 18  VAL B CB   1 
ATOM   3252 C  CG1  . VAL B 1 18  ? -45.059 -28.213 20.619 1.00 17.29  ? 18  VAL B CG1  1 
ATOM   3253 C  CG2  . VAL B 1 18  ? -45.401 -25.738 20.728 1.00 16.39  ? 18  VAL B CG2  1 
ATOM   3254 H  H    . VAL B 1 18  ? -48.015 -25.681 19.494 1.00 30.22  ? 18  VAL B H    1 
ATOM   3255 H  HA   . VAL B 1 18  ? -45.838 -26.893 18.339 1.00 21.68  ? 18  VAL B HA   1 
ATOM   3256 H  HB   . VAL B 1 18  ? -46.804 -27.193 20.993 1.00 18.72  ? 18  VAL B HB   1 
ATOM   3257 H  HG11 . VAL B 1 18  ? -44.480 -28.003 21.373 1.00 32.48  ? 18  VAL B HG11 1 
ATOM   3258 H  HG12 . VAL B 1 18  ? -45.557 -29.027 20.812 1.00 32.55  ? 18  VAL B HG12 1 
ATOM   3259 H  HG13 . VAL B 1 18  ? -44.517 -28.347 19.823 1.00 32.51  ? 18  VAL B HG13 1 
ATOM   3260 H  HG21 . VAL B 1 18  ? -45.074 -25.760 21.644 1.00 30.28  ? 18  VAL B HG21 1 
ATOM   3261 H  HG22 . VAL B 1 18  ? -44.657 -25.567 20.125 1.00 30.25  ? 18  VAL B HG22 1 
ATOM   3262 H  HG23 . VAL B 1 18  ? -46.059 -25.027 20.638 1.00 30.25  ? 18  VAL B HG23 1 
ATOM   3263 N  N    . VAL B 1 19  ? -46.623 -29.106 17.680 1.00 15.32  ? 19  VAL B N    1 
ATOM   3264 C  CA   . VAL B 1 19  ? -47.131 -30.393 17.265 1.00 16.94  ? 19  VAL B CA   1 
ATOM   3265 C  C    . VAL B 1 19  ? -46.228 -31.554 17.681 1.00 16.82  ? 19  VAL B C    1 
ATOM   3266 O  O    . VAL B 1 19  ? -46.658 -32.707 17.603 1.00 20.68  ? 19  VAL B O    1 
ATOM   3267 C  CB   . VAL B 1 19  ? -47.462 -30.437 15.764 1.00 18.76  ? 19  VAL B CB   1 
ATOM   3268 C  CG1  . VAL B 1 19  ? -48.574 -29.451 15.397 1.00 21.25  ? 19  VAL B CG1  1 
ATOM   3269 C  CG2  . VAL B 1 19  ? -46.242 -30.262 14.891 1.00 19.40  ? 19  VAL B CG2  1 
ATOM   3270 H  H    . VAL B 1 19  ? -45.867 -28.782 17.281 1.00 21.68  ? 19  VAL B H    1 
ATOM   3271 H  HA   . VAL B 1 19  ? -47.974 -30.523 17.734 1.00 19.73  ? 19  VAL B HA   1 
ATOM   3272 H  HB   . VAL B 1 19  ? -47.814 -31.343 15.583 1.00 21.16  ? 19  VAL B HB   1 
ATOM   3273 H  HG11 . VAL B 1 19  ? -48.782 -29.534 14.450 1.00 23.64  ? 19  VAL B HG11 1 
ATOM   3274 H  HG12 . VAL B 1 19  ? -49.370 -29.649 15.922 1.00 23.64  ? 19  VAL B HG12 1 
ATOM   3275 H  HG13 . VAL B 1 19  ? -48.279 -28.543 15.586 1.00 23.64  ? 19  VAL B HG13 1 
ATOM   3276 H  HG21 . VAL B 1 19  ? -46.506 -30.290 13.955 1.00 21.68  ? 19  VAL B HG21 1 
ATOM   3277 H  HG22 . VAL B 1 19  ? -45.824 -29.404 15.082 1.00 21.68  ? 19  VAL B HG22 1 
ATOM   3278 H  HG23 . VAL B 1 19  ? -45.607 -30.978 15.068 1.00 21.68  ? 19  VAL B HG23 1 
ATOM   3279 N  N    . ALA B 1 20  ? -44.998 -31.283 18.115 1.00 15.80  ? 20  ALA B N    1 
ATOM   3280 C  CA   . ALA B 1 20  ? -44.122 -32.337 18.604 1.00 16.28  ? 20  ALA B CA   1 
ATOM   3281 C  C    . ALA B 1 20  ? -43.052 -31.691 19.468 1.00 14.89  ? 20  ALA B C    1 
ATOM   3282 O  O    . ALA B 1 20  ? -42.641 -30.575 19.156 1.00 14.72  ? 20  ALA B O    1 
ATOM   3283 C  CB   . ALA B 1 20  ? -43.495 -33.107 17.449 1.00 18.60  ? 20  ALA B CB   1 
ATOM   3284 H  H    . ALA B 1 20  ? -44.689 -30.423 18.102 1.00 21.68  ? 20  ALA B H    1 
ATOM   3285 H  HA   . ALA B 1 20  ? -44.650 -32.957 19.158 1.00 30.84  ? 20  ALA B HA   1 
ATOM   3286 H  HB1  . ALA B 1 20  ? -42.930 -33.816 17.799 1.00 19.23  ? 20  ALA B HB1  1 
ATOM   3287 H  HB2  . ALA B 1 20  ? -44.195 -33.495 16.897 1.00 19.23  ? 20  ALA B HB2  1 
ATOM   3288 H  HB3  . ALA B 1 20  ? -42.957 -32.503 16.910 1.00 19.23  ? 20  ALA B HB3  1 
ATOM   3289 N  N    . MET B 1 21  ? -42.592 -32.391 20.510 1.00 15.96  ? 21  MET B N    1 
ATOM   3290 C  CA   A MET B 1 21  ? -41.415 -31.969 21.280 0.61 16.94  ? 21  MET B CA   1 
ATOM   3291 C  CA   B MET B 1 21  ? -41.455 -31.980 21.309 0.39 16.81  ? 21  MET B CA   1 
ATOM   3292 C  C    . MET B 1 21  ? -40.691 -33.228 21.736 1.00 16.40  ? 21  MET B C    1 
ATOM   3293 O  O    . MET B 1 21  ? -41.264 -34.145 22.304 1.00 19.22  ? 21  MET B O    1 
ATOM   3294 C  CB   A MET B 1 21  ? -41.646 -31.060 22.518 0.61 21.71  ? 21  MET B CB   1 
ATOM   3295 C  CB   B MET B 1 21  ? -41.864 -31.213 22.572 0.39 21.05  ? 21  MET B CB   1 
ATOM   3296 C  CG   A MET B 1 21  ? -40.301 -30.421 23.279 0.61 18.03  ? 21  MET B CG   1 
ATOM   3297 C  CG   B MET B 1 21  ? -40.681 -30.444 23.203 0.39 23.12  ? 21  MET B CG   1 
ATOM   3298 S  SD   A MET B 1 21  ? -40.736 -28.919 24.250 0.61 30.84  ? 21  MET B SD   1 
ATOM   3299 S  SD   B MET B 1 21  ? -40.909 -30.178 24.931 0.39 22.10  ? 21  MET B SD   1 
ATOM   3300 C  CE   A MET B 1 21  ? -42.464 -28.700 23.837 0.61 16.53  ? 21  MET B CE   1 
ATOM   3301 C  CE   B MET B 1 21  ? -40.740 -28.395 24.951 0.39 22.65  ? 21  MET B CE   1 
ATOM   3302 H  H    A MET B 1 21  ? -43.051 -33.133 20.787 0.61 30.84  ? 21  MET B H    1 
ATOM   3303 H  H    B MET B 1 21  ? -43.019 -33.167 20.735 0.39 30.84  ? 21  MET B H    1 
ATOM   3304 H  HA   A MET B 1 21  ? -40.821 -31.491 20.660 0.61 18.41  ? 21  MET B HA   1 
ATOM   3305 H  HA   B MET B 1 21  ? -40.867 -31.417 20.755 0.39 18.42  ? 21  MET B HA   1 
ATOM   3306 H  HB2  A MET B 1 21  ? -42.215 -30.326 22.229 0.61 24.06  ? 21  MET B HB2  1 
ATOM   3307 H  HB2  B MET B 1 21  ? -42.574 -30.581 22.344 0.39 22.67  ? 21  MET B HB2  1 
ATOM   3308 H  HB3  A MET B 1 21  ? -42.155 -31.574 23.177 0.61 24.04  ? 21  MET B HB3  1 
ATOM   3309 H  HB3  B MET B 1 21  ? -42.223 -31.845 23.227 0.39 22.67  ? 21  MET B HB3  1 
ATOM   3310 H  HG2  A MET B 1 21  ? -39.915 -31.094 23.878 0.61 16.99  ? 21  MET B HG2  1 
ATOM   3311 H  HG2  B MET B 1 21  ? -39.851 -30.947 23.063 0.39 17.05  ? 21  MET B HG2  1 
ATOM   3312 H  HG3  A MET B 1 21  ? -39.628 -30.186 22.605 0.61 16.99  ? 21  MET B HG3  1 
ATOM   3313 H  HG3  B MET B 1 21  ? -40.588 -29.575 22.758 0.39 17.05  ? 21  MET B HG3  1 
ATOM   3314 H  HE1  A MET B 1 21  ? -42.821 -27.966 24.353 0.61 24.43  ? 21  MET B HE1  1 
ATOM   3315 H  HE1  B MET B 1 21  ? -40.310 -28.123 25.768 0.39 21.97  ? 21  MET B HE1  1 
ATOM   3316 H  HE2  A MET B 1 21  ? -42.551 -28.499 22.898 0.61 24.43  ? 21  MET B HE2  1 
ATOM   3317 H  HE2  B MET B 1 21  ? -40.207 -28.115 24.197 0.39 21.97  ? 21  MET B HE2  1 
ATOM   3318 H  HE3  A MET B 1 21  ? -42.954 -29.504 24.047 0.61 24.50  ? 21  MET B HE3  1 
ATOM   3319 H  HE3  B MET B 1 21  ? -41.614 -27.990 24.896 0.39 21.97  ? 21  MET B HE3  1 
ATOM   3320 N  N    . ASN B 1 22  ? -39.407 -33.265 21.437 1.00 15.08  ? 22  ASN B N    1 
ATOM   3321 C  CA   . ASN B 1 22  ? -38.591 -34.411 21.787 1.00 15.83  ? 22  ASN B CA   1 
ATOM   3322 C  C    . ASN B 1 22  ? -37.236 -33.937 22.227 1.00 14.69  ? 22  ASN B C    1 
ATOM   3323 O  O    . ASN B 1 22  ? -36.601 -33.167 21.516 1.00 15.19  ? 22  ASN B O    1 
ATOM   3324 C  CB   . ASN B 1 22  ? -38.417 -35.400 20.630 1.00 19.43  ? 22  ASN B CB   1 
ATOM   3325 C  CG   . ASN B 1 22  ? -39.728 -36.019 20.232 1.00 21.34  ? 22  ASN B CG   1 
ATOM   3326 O  OD1  . ASN B 1 22  ? -40.394 -35.546 19.312 1.00 23.82  ? 22  ASN B OD1  1 
ATOM   3327 N  ND2  . ASN B 1 22  ? -40.077 -37.079 20.942 1.00 23.22  ? 22  ASN B ND2  1 
ATOM   3328 H  H    . ASN B 1 22  ? -39.016 -32.561 21.005 1.00 18.42  ? 22  ASN B H    1 
ATOM   3329 H  HA   . ASN B 1 22  ? -39.020 -34.890 22.534 1.00 17.62  ? 22  ASN B HA   1 
ATOM   3330 H  HB2  . ASN B 1 22  ? -38.034 -34.930 19.861 1.00 23.63  ? 22  ASN B HB2  1 
ATOM   3331 H  HB3  . ASN B 1 22  ? -37.794 -36.105 20.901 1.00 23.63  ? 22  ASN B HB3  1 
ATOM   3332 H  HD21 . ASN B 1 22  ? -39.677 -37.249 21.713 1.00 23.63  ? 22  ASN B HD21 1 
ATOM   3333 H  HD22 . ASN B 1 22  ? -40.713 -37.619 20.648 1.00 23.63  ? 22  ASN B HD22 1 
ATOM   3334 N  N    . ALA B 1 23  ? -36.797 -34.452 23.368 1.00 13.75  ? 23  ALA B N    1 
ATOM   3335 C  CA   . ALA B 1 23  ? -35.439 -34.261 23.813 1.00 13.51  ? 23  ALA B CA   1 
ATOM   3336 C  C    . ALA B 1 23  ? -34.549 -35.263 23.096 1.00 14.14  ? 23  ALA B C    1 
ATOM   3337 O  O    . ALA B 1 23  ? -34.439 -36.428 23.502 1.00 18.13  ? 23  ALA B O    1 
ATOM   3338 C  CB   . ALA B 1 23  ? -35.371 -34.409 25.304 1.00 14.16  ? 23  ALA B CB   1 
ATOM   3339 H  H    . ALA B 1 23  ? -37.364 -34.945 23.887 1.00 17.62  ? 23  ALA B H    1 
ATOM   3340 H  HA   . ALA B 1 23  ? -35.150 -33.350 23.571 1.00 16.97  ? 23  ALA B HA   1 
ATOM   3341 H  HB1  . ALA B 1 23  ? -34.510 -34.092 25.624 1.00 20.17  ? 23  ALA B HB1  1 
ATOM   3342 H  HB2  . ALA B 1 23  ? -36.080 -33.886 25.713 1.00 20.17  ? 23  ALA B HB2  1 
ATOM   3343 H  HB3  . ALA B 1 23  ? -35.482 -35.343 25.545 1.00 20.17  ? 23  ALA B HB3  1 
ATOM   3344 N  N    . VAL B 1 24  ? -33.903 -34.837 22.030 1.00 13.56  ? 24  VAL B N    1 
ATOM   3345 C  CA   . VAL B 1 24  ? -33.038 -35.677 21.237 1.00 13.88  ? 24  VAL B CA   1 
ATOM   3346 C  C    . VAL B 1 24  ? -31.814 -36.070 22.040 1.00 13.89  ? 24  VAL B C    1 
ATOM   3347 O  O    . VAL B 1 24  ? -31.331 -37.184 21.889 1.00 15.39  ? 24  VAL B O    1 
ATOM   3348 C  CB   . VAL B 1 24  ? -32.722 -34.951 19.918 1.00 14.47  ? 24  VAL B CB   1 
ATOM   3349 C  CG1  . VAL B 1 24  ? -31.762 -35.783 19.081 1.00 15.07  ? 24  VAL B CG1  1 
ATOM   3350 C  CG2  . VAL B 1 24  ? -34.006 -34.680 19.141 1.00 16.98  ? 24  VAL B CG2  1 
ATOM   3351 H  H    . VAL B 1 24  ? -33.996 -33.960 21.788 1.00 16.97  ? 24  VAL B H    1 
ATOM   3352 H  HA   . VAL B 1 24  ? -33.528 -36.491 21.021 1.00 16.97  ? 24  VAL B HA   1 
ATOM   3353 H  HB   . VAL B 1 24  ? -32.290 -34.087 20.131 1.00 16.97  ? 24  VAL B HB   1 
ATOM   3354 H  HG11 . VAL B 1 24  ? -31.759 -35.455 18.165 1.00 16.77  ? 24  VAL B HG11 1 
ATOM   3355 H  HG12 . VAL B 1 24  ? -30.865 -35.715 19.450 1.00 16.76  ? 24  VAL B HG12 1 
ATOM   3356 H  HG13 . VAL B 1 24  ? -32.046 -36.714 19.090 1.00 16.77  ? 24  VAL B HG13 1 
ATOM   3357 H  HG21 . VAL B 1 24  ? -33.787 -34.424 18.228 1.00 16.96  ? 24  VAL B HG21 1 
ATOM   3358 H  HG22 . VAL B 1 24  ? -34.554 -35.483 19.128 1.00 16.97  ? 24  VAL B HG22 1 
ATOM   3359 H  HG23 . VAL B 1 24  ? -34.500 -33.958 19.568 1.00 16.97  ? 24  VAL B HG23 1 
ATOM   3360 N  N    . ALA B 1 25  ? -31.293 -35.114 22.810 1.00 13.77  ? 25  ALA B N    1 
ATOM   3361 C  CA   . ALA B 1 25  ? -30.171 -35.329 23.700 1.00 14.52  ? 25  ALA B CA   1 
ATOM   3362 C  C    . ALA B 1 25  ? -30.419 -34.551 24.980 1.00 14.10  ? 25  ALA B C    1 
ATOM   3363 O  O    . ALA B 1 25  ? -30.906 -33.421 24.943 1.00 13.50  ? 25  ALA B O    1 
ATOM   3364 C  CB   . ALA B 1 25  ? -28.850 -34.877 23.115 1.00 15.82  ? 25  ALA B CB   1 
ATOM   3365 H  H    . ALA B 1 25  ? -31.654 -34.276 22.769 1.00 16.53  ? 25  ALA B H    1 
ATOM   3366 H  HA   . ALA B 1 25  ? -30.115 -36.289 23.917 1.00 18.11  ? 25  ALA B HA   1 
ATOM   3367 H  HB1  . ALA B 1 25  ? -28.136 -35.051 23.751 1.00 18.89  ? 25  ALA B HB1  1 
ATOM   3368 H  HB2  . ALA B 1 25  ? -28.676 -35.364 22.292 1.00 18.89  ? 25  ALA B HB2  1 
ATOM   3369 H  HB3  . ALA B 1 25  ? -28.888 -33.925 22.925 1.00 18.89  ? 25  ALA B HB3  1 
ATOM   3370 N  N    . GLY B 1 26  ? -30.039 -35.140 26.098 1.00 15.82  ? 26  GLY B N    1 
ATOM   3371 C  CA   . GLY B 1 26  ? -30.090 -34.453 27.363 1.00 15.28  ? 26  GLY B CA   1 
ATOM   3372 C  C    . GLY B 1 26  ? -31.497 -34.345 27.927 1.00 15.85  ? 26  GLY B C    1 
ATOM   3373 O  O    . GLY B 1 26  ? -32.429 -35.048 27.532 1.00 15.99  ? 26  GLY B O    1 
ATOM   3374 H  H    . GLY B 1 26  ? -29.737 -36.002 26.075 1.00 18.11  ? 26  GLY B H    1 
ATOM   3375 H  HA2  . GLY B 1 26  ? -29.518 -34.938 28.010 1.00 17.66  ? 26  GLY B HA2  1 
ATOM   3376 H  HA3  . GLY B 1 26  ? -29.712 -33.545 27.249 1.00 17.66  ? 26  GLY B HA3  1 
ATOM   3377 N  N    . ALA B 1 27  ? -31.612 -33.453 28.898 1.00 15.13  ? 27  ALA B N    1 
ATOM   3378 C  CA   . ALA B 1 27  ? -32.835 -33.340 29.697 1.00 15.84  ? 27  ALA B CA   1 
ATOM   3379 C  C    . ALA B 1 27  ? -33.966 -32.668 28.938 1.00 15.53  ? 27  ALA B C    1 
ATOM   3380 O  O    . ALA B 1 27  ? -33.760 -31.703 28.215 1.00 15.31  ? 27  ALA B O    1 
ATOM   3381 C  CB   . ALA B 1 27  ? -32.545 -32.575 30.952 1.00 17.47  ? 27  ALA B CB   1 
ATOM   3382 H  H    . ALA B 1 27  ? -30.914 -32.891 29.078 1.00 17.66  ? 27  ALA B H    1 
ATOM   3383 H  HA   . ALA B 1 27  ? -33.119 -34.248 29.946 1.00 31.77  ? 27  ALA B HA   1 
ATOM   3384 H  HB1  . ALA B 1 27  ? -33.346 -32.535 31.501 1.00 30.86  ? 27  ALA B HB1  1 
ATOM   3385 H  HB2  . ALA B 1 27  ? -31.837 -33.019 31.447 1.00 30.85  ? 27  ALA B HB2  1 
ATOM   3386 H  HB3  . ALA B 1 27  ? -32.264 -31.673 30.725 1.00 30.85  ? 27  ALA B HB3  1 
ATOM   3387 N  N    . PRO B 1 28  ? -35.212 -33.145 29.116 1.00 15.62  ? 28  PRO B N    1 
ATOM   3388 C  CA   . PRO B 1 28  ? -36.320 -32.540 28.398 1.00 16.40  ? 28  PRO B CA   1 
ATOM   3389 C  C    . PRO B 1 28  ? -36.609 -31.123 28.874 1.00 15.37  ? 28  PRO B C    1 
ATOM   3390 O  O    . PRO B 1 28  ? -36.312 -30.727 30.005 1.00 17.31  ? 28  PRO B O    1 
ATOM   3391 C  CB   . PRO B 1 28  ? -37.519 -33.418 28.767 1.00 19.37  ? 28  PRO B CB   1 
ATOM   3392 C  CG   . PRO B 1 28  ? -36.951 -34.695 29.308 1.00 23.87  ? 28  PRO B CG   1 
ATOM   3393 C  CD   . PRO B 1 28  ? -35.623 -34.316 29.916 1.00 19.87  ? 28  PRO B CD   1 
ATOM   3394 H  HA   . PRO B 1 28  ? -36.156 -32.566 27.422 1.00 20.78  ? 28  PRO B HA   1 
ATOM   3395 H  HB2  . PRO B 1 28  ? -38.077 -32.978 29.444 1.00 22.25  ? 28  PRO B HB2  1 
ATOM   3396 H  HB3  . PRO B 1 28  ? -38.071 -33.596 27.978 1.00 22.25  ? 28  PRO B HB3  1 
ATOM   3397 H  HG2  . PRO B 1 28  ? -37.544 -35.077 29.987 1.00 24.93  ? 28  PRO B HG2  1 
ATOM   3398 H  HG3  . PRO B 1 28  ? -36.828 -35.351 28.592 1.00 24.93  ? 28  PRO B HG3  1 
ATOM   3399 H  HD2  . PRO B 1 28  ? -35.720 -34.082 30.857 1.00 31.77  ? 28  PRO B HD2  1 
ATOM   3400 H  HD3  . PRO B 1 28  ? -34.982 -35.045 29.832 1.00 31.77  ? 28  PRO B HD3  1 
ATOM   3401 N  N    . LEU B 1 29  ? -37.238 -30.369 27.982 1.00 15.64  ? 29  LEU B N    1 
ATOM   3402 C  CA   . LEU B 1 29  ? -37.878 -29.114 28.308 1.00 15.44  ? 29  LEU B CA   1 
ATOM   3403 C  C    . LEU B 1 29  ? -39.347 -29.374 28.561 1.00 15.45  ? 29  LEU B C    1 
ATOM   3404 O  O    . LEU B 1 29  ? -39.946 -30.237 27.917 1.00 16.78  ? 29  LEU B O    1 
ATOM   3405 C  CB   . LEU B 1 29  ? -37.834 -28.154 27.117 1.00 19.31  ? 29  LEU B CB   1 
ATOM   3406 C  CG   . LEU B 1 29  ? -36.702 -27.167 26.993 1.00 18.86  ? 29  LEU B CG   1 
ATOM   3407 C  CD1  . LEU B 1 29  ? -36.950 -26.312 25.772 1.00 18.07  ? 29  LEU B CD1  1 
ATOM   3408 C  CD2  . LEU B 1 29  ? -36.525 -26.283 28.185 1.00 16.76  ? 29  LEU B CD2  1 
ATOM   3409 H  H    . LEU B 1 29  ? -37.273 -30.659 27.116 1.00 21.45  ? 29  LEU B H    1 
ATOM   3410 H  HA   . LEU B 1 29  ? -37.455 -28.716 29.099 1.00 30.46  ? 29  LEU B HA   1 
ATOM   3411 H  HB2  . LEU B 1 29  ? -37.846 -28.694 26.301 1.00 22.13  ? 29  LEU B HB2  1 
ATOM   3412 H  HB3  . LEU B 1 29  ? -38.666 -27.640 27.126 1.00 22.14  ? 29  LEU B HB3  1 
ATOM   3413 H  HG   . LEU B 1 29  ? -35.864 -27.672 26.855 1.00 16.88  ? 29  LEU B HG   1 
ATOM   3414 H  HD11 . LEU B 1 29  ? -36.195 -25.713 25.636 1.00 22.80  ? 29  LEU B HD11 1 
ATOM   3415 H  HD12 . LEU B 1 29  ? -37.054 -26.882 24.991 1.00 22.76  ? 29  LEU B HD12 1 
ATOM   3416 H  HD13 . LEU B 1 29  ? -37.760 -25.788 25.900 1.00 22.76  ? 29  LEU B HD13 1 
ATOM   3417 H  HD21 . LEU B 1 29  ? -35.894 -25.573 27.973 1.00 25.14  ? 29  LEU B HD21 1 
ATOM   3418 H  HD22 . LEU B 1 29  ? -37.382 -25.891 28.428 1.00 25.17  ? 29  LEU B HD22 1 
ATOM   3419 H  HD23 . LEU B 1 29  ? -36.185 -26.805 28.931 1.00 25.21  ? 29  LEU B HD23 1 
ATOM   3420 N  N    . PRO B 1 30  ? -40.003 -28.574 29.427 1.00 15.41  ? 30  PRO B N    1 
ATOM   3421 C  CA   . PRO B 1 30  ? -41.428 -28.758 29.681 1.00 16.20  ? 30  PRO B CA   1 
ATOM   3422 C  C    . PRO B 1 30  ? -42.256 -28.638 28.414 1.00 15.50  ? 30  PRO B C    1 
ATOM   3423 O  O    . PRO B 1 30  ? -42.079 -27.714 27.623 1.00 14.79  ? 30  PRO B O    1 
ATOM   3424 C  CB   . PRO B 1 30  ? -41.763 -27.641 30.669 1.00 17.61  ? 30  PRO B CB   1 
ATOM   3425 C  CG   . PRO B 1 30  ? -40.472 -27.384 31.392 1.00 18.56  ? 30  PRO B CG   1 
ATOM   3426 C  CD   . PRO B 1 30  ? -39.414 -27.556 30.315 1.00 16.92  ? 30  PRO B CD   1 
ATOM   3427 H  HA   . PRO B 1 30  ? -41.576 -29.637 30.110 1.00 19.63  ? 30  PRO B HA   1 
ATOM   3428 H  HB2  . PRO B 1 30  ? -42.066 -26.834 30.199 1.00 21.25  ? 30  PRO B HB2  1 
ATOM   3429 H  HB3  . PRO B 1 30  ? -42.463 -27.924 31.295 1.00 21.25  ? 30  PRO B HB3  1 
ATOM   3430 H  HG2  . PRO B 1 30  ? -40.451 -26.478 31.761 1.00 34.17  ? 30  PRO B HG2  1 
ATOM   3431 H  HG3  . PRO B 1 30  ? -40.342 -28.028 32.117 1.00 34.16  ? 30  PRO B HG3  1 
ATOM   3432 H  HD2  . PRO B 1 30  ? -39.257 -26.721 29.837 1.00 35.82  ? 30  PRO B HD2  1 
ATOM   3433 H  HD3  . PRO B 1 30  ? -38.573 -27.866 30.699 1.00 35.83  ? 30  PRO B HD3  1 
ATOM   3434 N  N    . GLY B 1 31  ? -43.200 -29.572 28.258 1.00 17.19  ? 31  GLY B N    1 
ATOM   3435 C  CA   . GLY B 1 31  ? -44.120 -29.525 27.145 1.00 17.03  ? 31  GLY B CA   1 
ATOM   3436 C  C    . GLY B 1 31  ? -45.037 -28.318 27.252 1.00 15.69  ? 31  GLY B C    1 
ATOM   3437 O  O    . GLY B 1 31  ? -45.436 -27.916 28.344 1.00 18.30  ? 31  GLY B O    1 
ATOM   3438 H  H    . GLY B 1 31  ? -43.271 -30.255 28.862 1.00 19.63  ? 31  GLY B H    1 
ATOM   3439 H  HA2  . GLY B 1 31  ? -43.606 -29.480 26.302 1.00 23.54  ? 31  GLY B HA2  1 
ATOM   3440 H  HA3  . GLY B 1 31  ? -44.663 -30.353 27.137 1.00 23.53  ? 31  GLY B HA3  1 
ATOM   3441 N  N    . ILE B 1 32  ? -45.341 -27.744 26.093 1.00 14.20  ? 32  ILE B N    1 
ATOM   3442 C  CA   . ILE B 1 32  ? -46.177 -26.563 25.969 1.00 14.53  ? 32  ILE B CA   1 
ATOM   3443 C  C    . ILE B 1 32  ? -46.998 -26.681 24.694 1.00 13.93  ? 32  ILE B C    1 
ATOM   3444 O  O    . ILE B 1 32  ? -46.572 -27.343 23.761 1.00 14.64  ? 32  ILE B O    1 
ATOM   3445 C  CB   . ILE B 1 32  ? -45.386 -25.248 25.926 1.00 16.23  ? 32  ILE B CB   1 
ATOM   3446 C  CG1  . ILE B 1 32  ? -44.631 -25.125 24.580 1.00 20.06  ? 32  ILE B CG1  1 
ATOM   3447 C  CG2  . ILE B 1 32  ? -44.522 -25.052 27.154 1.00 18.99  ? 32  ILE B CG2  1 
ATOM   3448 C  CD1  . ILE B 1 32  ? -43.335 -24.431 24.488 1.00 30.63  ? 32  ILE B CD1  1 
ATOM   3449 H  H    . ILE B 1 32  ? -45.004 -28.109 25.325 1.00 23.43  ? 32  ILE B H    1 
ATOM   3450 H  HA   . ILE B 1 32  ? -46.784 -26.533 26.730 1.00 17.61  ? 32  ILE B HA   1 
ATOM   3451 H  HB   . ILE B 1 32  ? -46.055 -24.520 25.935 1.00 17.61  ? 32  ILE B HB   1 
ATOM   3452 H  HG12 . ILE B 1 32  ? -44.488 -26.034 24.243 1.00 22.39  ? 32  ILE B HG12 1 
ATOM   3453 H  HG13 . ILE B 1 32  ? -45.239 -24.685 23.948 1.00 22.37  ? 32  ILE B HG13 1 
ATOM   3454 H  HG21 . ILE B 1 32  ? -44.265 -24.117 27.229 1.00 21.98  ? 32  ILE B HG21 1 
ATOM   3455 H  HG22 . ILE B 1 32  ? -45.020 -25.313 27.948 1.00 21.98  ? 32  ILE B HG22 1 
ATOM   3456 H  HG23 . ILE B 1 32  ? -43.722 -25.602 27.081 1.00 21.98  ? 32  ILE B HG23 1 
ATOM   3457 H  HD11 . ILE B 1 32  ? -42.691 -25.024 24.067 1.00 22.09  ? 32  ILE B HD11 1 
ATOM   3458 H  HD12 . ILE B 1 32  ? -43.434 -23.635 23.943 1.00 22.09  ? 32  ILE B HD12 1 
ATOM   3459 H  HD13 . ILE B 1 32  ? -43.025 -24.191 25.374 1.00 22.08  ? 32  ILE B HD13 1 
ATOM   3460 N  N    . PRO B 1 33  ? -48.161 -26.005 24.639 1.00 13.93  ? 33  PRO B N    1 
ATOM   3461 C  CA   . PRO B 1 33  ? -48.987 -26.088 23.446 1.00 14.57  ? 33  PRO B CA   1 
ATOM   3462 C  C    . PRO B 1 33  ? -48.679 -25.077 22.353 1.00 13.76  ? 33  PRO B C    1 
ATOM   3463 O  O    . PRO B 1 33  ? -49.026 -25.321 21.198 1.00 14.17  ? 33  PRO B O    1 
ATOM   3464 C  CB   . PRO B 1 33  ? -50.415 -25.855 23.987 1.00 15.26  ? 33  PRO B CB   1 
ATOM   3465 C  CG   . PRO B 1 33  ? -50.203 -24.946 25.164 1.00 15.59  ? 33  PRO B CG   1 
ATOM   3466 C  CD   . PRO B 1 33  ? -48.902 -25.438 25.783 1.00 14.59  ? 33  PRO B CD   1 
ATOM   3467 H  HA   . PRO B 1 33  ? -48.930 -27.005 23.075 1.00 17.04  ? 33  PRO B HA   1 
ATOM   3468 H  HB2  . PRO B 1 33  ? -50.985 -25.427 23.312 1.00 18.11  ? 33  PRO B HB2  1 
ATOM   3469 H  HB3  . PRO B 1 33  ? -50.829 -26.699 24.266 1.00 18.11  ? 33  PRO B HB3  1 
ATOM   3470 H  HG2  . PRO B 1 33  ? -50.124 -24.014 24.877 1.00 19.00  ? 33  PRO B HG2  1 
ATOM   3471 H  HG3  . PRO B 1 33  ? -50.943 -25.020 25.802 1.00 19.00  ? 33  PRO B HG3  1 
ATOM   3472 H  HD2  . PRO B 1 33  ? -48.406 -24.704 26.192 1.00 17.61  ? 33  PRO B HD2  1 
ATOM   3473 H  HD3  . PRO B 1 33  ? -49.072 -26.119 26.460 1.00 17.61  ? 33  PRO B HD3  1 
ATOM   3474 N  N    . ARG B 1 34  ? -48.083 -23.927 22.710 1.00 13.38  ? 34  ARG B N    1 
ATOM   3475 C  CA   . ARG B 1 34  ? -47.904 -22.823 21.780 1.00 13.40  ? 34  ARG B CA   1 
ATOM   3476 C  C    . ARG B 1 34  ? -46.519 -22.215 21.955 1.00 12.54  ? 34  ARG B C    1 
ATOM   3477 O  O    . ARG B 1 34  ? -45.898 -22.343 23.002 1.00 12.68  ? 34  ARG B O    1 
ATOM   3478 C  CB   . ARG B 1 34  ? -48.940 -21.707 21.979 1.00 15.05  ? 34  ARG B CB   1 
ATOM   3479 C  CG   . ARG B 1 34  ? -50.370 -22.178 22.152 1.00 18.95  ? 34  ARG B CG   1 
ATOM   3480 C  CD   . ARG B 1 34  ? -50.935 -22.656 20.899 1.00 23.56  ? 34  ARG B CD   1 
ATOM   3481 N  NE   . ARG B 1 34  ? -51.051 -21.616 19.912 1.00 22.20  ? 34  ARG B NE   1 
ATOM   3482 C  CZ   . ARG B 1 34  ? -51.626 -21.863 18.750 1.00 22.56  ? 34  ARG B CZ   1 
ATOM   3483 N  NH1  . ARG B 1 34  ? -52.295 -22.993 18.617 1.00 25.08  ? 34  ARG B NH1  1 
ATOM   3484 N  NH2  . ARG B 1 34  ? -51.513 -21.018 17.739 1.00 23.59  ? 34  ARG B NH2  1 
ATOM   3485 H  H    . ARG B 1 34  ? -47.779 -23.829 23.566 1.00 16.01  ? 34  ARG B H    1 
ATOM   3486 H  HA   . ARG B 1 34  ? -47.982 -23.171 20.863 1.00 15.73  ? 34  ARG B HA   1 
ATOM   3487 H  HB2  . ARG B 1 34  ? -48.687 -21.190 22.772 1.00 25.94  ? 34  ARG B HB2  1 
ATOM   3488 H  HB3  . ARG B 1 34  ? -48.896 -21.105 21.208 1.00 25.94  ? 34  ARG B HB3  1 
ATOM   3489 H  HG2  . ARG B 1 34  ? -50.402 -22.898 22.816 1.00 19.01  ? 34  ARG B HG2  1 
ATOM   3490 H  HG3  . ARG B 1 34  ? -50.917 -21.435 22.485 1.00 19.01  ? 34  ARG B HG3  1 
ATOM   3491 H  HD2  . ARG B 1 34  ? -50.374 -23.376 20.543 1.00 29.73  ? 34  ARG B HD2  1 
ATOM   3492 H  HD3  . ARG B 1 34  ? -51.824 -23.027 21.077 1.00 29.73  ? 34  ARG B HD3  1 
ATOM   3493 H  HE   . ARG B 1 34  ? -50.756 -20.814 20.085 1.00 25.99  ? 34  ARG B HE   1 
ATOM   3494 H  HH11 . ARG B 1 34  ? -51.865 -23.761 18.612 1.00 30.93  ? 34  ARG B HH11 1 
ATOM   3495 H  HH12 . ARG B 1 34  ? -53.172 -22.975 18.533 1.00 30.93  ? 34  ARG B HH12 1 
ATOM   3496 H  HH21 . ARG B 1 34  ? -51.055 -20.274 17.838 1.00 26.05  ? 34  ARG B HH21 1 
ATOM   3497 H  HH22 . ARG B 1 34  ? -51.895 -21.203 16.970 1.00 26.05  ? 34  ARG B HH22 1 
ATOM   3498 N  N    . LEU B 1 35  ? -46.065 -21.531 20.893 1.00 13.05  ? 35  LEU B N    1 
ATOM   3499 C  CA   . LEU B 1 35  ? -44.800 -20.820 20.895 1.00 12.63  ? 35  LEU B CA   1 
ATOM   3500 C  C    . LEU B 1 35  ? -45.008 -19.426 20.314 1.00 12.61  ? 35  LEU B C    1 
ATOM   3501 O  O    . LEU B 1 35  ? -45.695 -19.277 19.305 1.00 14.45  ? 35  LEU B O    1 
ATOM   3502 C  CB   . LEU B 1 35  ? -43.767 -21.609 20.071 1.00 12.85  ? 35  LEU B CB   1 
ATOM   3503 C  CG   . LEU B 1 35  ? -42.341 -21.071 20.098 1.00 14.63  ? 35  LEU B CG   1 
ATOM   3504 C  CD1  . LEU B 1 35  ? -41.648 -21.372 21.427 1.00 16.42  ? 35  LEU B CD1  1 
ATOM   3505 C  CD2  . LEU B 1 35  ? -41.520 -21.622 18.945 1.00 16.82  ? 35  LEU B CD2  1 
ATOM   3506 H  H    . LEU B 1 35  ? -46.573 -21.509 20.133 1.00 15.73  ? 35  LEU B H    1 
ATOM   3507 H  HA   . LEU B 1 35  ? -44.487 -20.737 21.822 1.00 18.37  ? 35  LEU B HA   1 
ATOM   3508 H  HB2  . LEU B 1 35  ? -43.755 -22.530 20.399 1.00 17.39  ? 35  LEU B HB2  1 
ATOM   3509 H  HB3  . LEU B 1 35  ? -44.070 -21.632 19.142 1.00 17.39  ? 35  LEU B HB3  1 
ATOM   3510 H  HG   . LEU B 1 35  ? -42.383 -20.088 19.996 1.00 17.39  ? 35  LEU B HG   1 
ATOM   3511 H  HD11 . LEU B 1 35  ? -40.756 -20.982 21.425 1.00 18.37  ? 35  LEU B HD11 1 
ATOM   3512 H  HD12 . LEU B 1 35  ? -42.165 -20.993 22.157 1.00 18.37  ? 35  LEU B HD12 1 
ATOM   3513 H  HD13 . LEU B 1 35  ? -41.579 -22.335 21.546 1.00 18.37  ? 35  LEU B HD13 1 
ATOM   3514 H  HD21 . LEU B 1 35  ? -40.613 -21.273 18.996 1.00 19.80  ? 35  LEU B HD21 1 
ATOM   3515 H  HD22 . LEU B 1 35  ? -41.497 -22.593 18.998 1.00 19.80  ? 35  LEU B HD22 1 
ATOM   3516 H  HD23 . LEU B 1 35  ? -41.924 -21.353 18.102 1.00 19.80  ? 35  LEU B HD23 1 
ATOM   3517 N  N    . ASN B 1 36  ? -44.394 -18.438 20.972 1.00 13.15  ? 36  ASN B N    1 
ATOM   3518 C  CA   . ASN B 1 36  ? -44.404 -17.055 20.542 1.00 14.65  ? 36  ASN B CA   1 
ATOM   3519 C  C    . ASN B 1 36  ? -42.968 -16.621 20.297 1.00 13.74  ? 36  ASN B C    1 
ATOM   3520 O  O    . ASN B 1 36  ? -42.095 -16.963 21.095 1.00 14.26  ? 36  ASN B O    1 
ATOM   3521 C  CB   . ASN B 1 36  ? -45.009 -16.145 21.637 1.00 18.35  ? 36  ASN B CB   1 
ATOM   3522 C  CG   . ASN B 1 36  ? -44.969 -14.656 21.372 1.00 21.95  ? 36  ASN B CG   1 
ATOM   3523 O  OD1  . ASN B 1 36  ? -44.110 -13.895 21.842 1.00 25.54  ? 36  ASN B OD1  1 
ATOM   3524 N  ND2  . ASN B 1 36  ? -45.902 -14.259 20.546 1.00 24.43  ? 36  ASN B ND2  1 
ATOM   3525 H  H    . ASN B 1 36  ? -43.940 -18.644 21.739 1.00 18.37  ? 36  ASN B H    1 
ATOM   3526 H  HA   . ASN B 1 36  ? -44.932 -16.963 19.715 1.00 17.11  ? 36  ASN B HA   1 
ATOM   3527 H  HB2  . ASN B 1 36  ? -45.942 -16.409 21.771 1.00 21.14  ? 36  ASN B HB2  1 
ATOM   3528 H  HB3  . ASN B 1 36  ? -44.533 -16.320 22.474 1.00 21.08  ? 36  ASN B HB3  1 
ATOM   3529 H  HD21 . ASN B 1 36  ? -46.317 -14.844 20.030 1.00 23.89  ? 36  ASN B HD21 1 
ATOM   3530 H  HD22 . ASN B 1 36  ? -46.117 -13.402 20.502 1.00 23.84  ? 36  ASN B HD22 1 
ATOM   3531 N  N    . VAL B 1 37  ? -42.732 -15.831 19.256 1.00 13.64  ? 37  VAL B N    1 
ATOM   3532 C  CA   . VAL B 1 37  ? -41.423 -15.271 18.974 1.00 14.09  ? 37  VAL B CA   1 
ATOM   3533 C  C    . VAL B 1 37  ? -41.516 -13.756 19.045 1.00 14.54  ? 37  VAL B C    1 
ATOM   3534 O  O    . VAL B 1 37  ? -42.319 -13.166 18.333 1.00 18.38  ? 37  VAL B O    1 
ATOM   3535 C  CB   . VAL B 1 37  ? -40.877 -15.710 17.602 1.00 16.44  ? 37  VAL B CB   1 
ATOM   3536 C  CG1  . VAL B 1 37  ? -39.438 -15.227 17.442 1.00 18.91  ? 37  VAL B CG1  1 
ATOM   3537 C  CG2  . VAL B 1 37  ? -41.011 -17.212 17.384 1.00 17.56  ? 37  VAL B CG2  1 
ATOM   3538 H  H    . VAL B 1 37  ? -43.421 -15.629 18.691 1.00 17.11  ? 37  VAL B H    1 
ATOM   3539 H  HA   . VAL B 1 37  ? -40.804 -15.574 19.660 1.00 23.34  ? 37  VAL B HA   1 
ATOM   3540 H  HB   . VAL B 1 37  ? -41.422 -15.259 16.911 1.00 19.51  ? 37  VAL B HB   1 
ATOM   3541 H  HG11 . VAL B 1 37  ? -39.029 -15.672 16.680 1.00 23.35  ? 37  VAL B HG11 1 
ATOM   3542 H  HG12 . VAL B 1 37  ? -39.431 -14.265 17.296 1.00 23.34  ? 37  VAL B HG12 1 
ATOM   3543 H  HG13 . VAL B 1 37  ? -38.933 -15.437 18.247 1.00 23.34  ? 37  VAL B HG13 1 
ATOM   3544 H  HG21 . VAL B 1 37  ? -40.494 -17.474 16.603 1.00 23.08  ? 37  VAL B HG21 1 
ATOM   3545 H  HG22 . VAL B 1 37  ? -40.679 -17.685 18.166 1.00 23.08  ? 37  VAL B HG22 1 
ATOM   3546 H  HG23 . VAL B 1 37  ? -41.947 -17.437 17.243 1.00 23.08  ? 37  VAL B HG23 1 
ATOM   3547 N  N    . ALA B 1 38  ? -40.746 -13.136 19.932 1.00 13.90  ? 38  ALA B N    1 
ATOM   3548 C  CA   . ALA B 1 38  ? -40.753 -11.698 20.095 1.00 14.41  ? 38  ALA B CA   1 
ATOM   3549 C  C    . ALA B 1 38  ? -39.390 -11.128 19.712 1.00 13.62  ? 38  ALA B C    1 
ATOM   3550 O  O    . ALA B 1 38  ? -38.368 -11.661 20.075 1.00 14.15  ? 38  ALA B O    1 
ATOM   3551 C  CB   . ALA B 1 38  ? -41.051 -11.320 21.528 1.00 16.88  ? 38  ALA B CB   1 
ATOM   3552 H  H    . ALA B 1 38  ? -40.189 -13.631 20.461 1.00 23.34  ? 38  ALA B H    1 
ATOM   3553 H  HA   . ALA B 1 38  ? -41.441 -11.307 19.507 1.00 26.11  ? 38  ALA B HA   1 
ATOM   3554 H  HB1  . ALA B 1 38  ? -41.058 -10.352 21.615 1.00 19.58  ? 38  ALA B HB1  1 
ATOM   3555 H  HB2  . ALA B 1 38  ? -41.920 -11.674 21.784 1.00 19.58  ? 38  ALA B HB2  1 
ATOM   3556 H  HB3  . ALA B 1 38  ? -40.368 -11.692 22.111 1.00 19.58  ? 38  ALA B HB3  1 
ATOM   3557 N  N    . ALA B 1 39  ? -39.375 -9.964  19.063 1.00 17.83  ? 39  ALA B N    1 
ATOM   3558 C  CA   . ALA B 1 39  ? -38.168 -9.262  18.668 1.00 19.47  ? 39  ALA B CA   1 
ATOM   3559 C  C    . ALA B 1 39  ? -37.789 -8.215  19.713 1.00 20.67  ? 39  ALA B C    1 
ATOM   3560 O  O    . ALA B 1 39  ? -38.637 -7.504  20.237 1.00 26.78  ? 39  ALA B O    1 
ATOM   3561 C  CB   . ALA B 1 39  ? -38.420 -8.608  17.330 1.00 23.78  ? 39  ALA B CB   1 
ATOM   3562 H  H    . ALA B 1 39  ? -40.178 -9.579  18.858 1.00 26.11  ? 39  ALA B H    1 
ATOM   3563 H  HA   . ALA B 1 39  ? -37.432 -9.911  18.578 1.00 21.91  ? 39  ALA B HA   1 
ATOM   3564 H  HB1  . ALA B 1 39  ? -37.725 -7.955  17.150 1.00 26.11  ? 39  ALA B HB1  1 
ATOM   3565 H  HB2  . ALA B 1 39  ? -38.415 -9.284  16.631 1.00 26.11  ? 39  ALA B HB2  1 
ATOM   3566 H  HB3  . ALA B 1 39  ? -39.283 -8.163  17.342 1.00 26.11  ? 39  ALA B HB3  1 
ATOM   3567 N  N    . GLY B 1 40  ? -36.482 -8.047  19.933 1.00 18.95  ? 40  GLY B N    1 
ATOM   3568 C  CA   . GLY B 1 40  ? -35.907 -6.920  20.662 1.00 21.68  ? 40  GLY B CA   1 
ATOM   3569 C  C    . GLY B 1 40  ? -35.455 -7.252  22.085 1.00 20.11  ? 40  GLY B C    1 
ATOM   3570 O  O    . GLY B 1 40  ? -35.714 -8.310  22.618 1.00 19.68  ? 40  GLY B O    1 
ATOM   3571 H  H    . GLY B 1 40  ? -35.907 -8.680  19.608 1.00 21.91  ? 40  GLY B H    1 
ATOM   3572 H  HA2  . GLY B 1 40  ? -35.130 -6.582  20.151 1.00 24.55  ? 40  GLY B HA2  1 
ATOM   3573 H  HA3  . GLY B 1 40  ? -36.574 -6.191  20.698 1.00 24.55  ? 40  GLY B HA3  1 
ATOM   3574 N  N    . SER B 1 41  ? -34.790 -6.293  22.726 1.00 23.30  ? 41  SER B N    1 
ATOM   3575 C  CA   . SER B 1 41  ? -34.143 -6.495  24.006 1.00 24.42  ? 41  SER B CA   1 
ATOM   3576 C  C    . SER B 1 41  ? -35.032 -6.235  25.225 1.00 23.40  ? 41  SER B C    1 
ATOM   3577 O  O    . SER B 1 41  ? -34.592 -6.499  26.352 1.00 27.17  ? 41  SER B O    1 
ATOM   3578 C  CB   . SER B 1 41  ? -32.945 -5.573  24.017 1.00 27.97  ? 41  SER B CB   1 
ATOM   3579 O  OG   . SER B 1 41  ? -33.326 -4.253  23.603 1.00 37.17  ? 41  SER B OG   1 
ATOM   3580 H  H    . SER B 1 41  ? -34.741 -5.465  22.341 1.00 25.17  ? 41  SER B H    1 
ATOM   3581 H  HA   . SER B 1 41  ? -33.819 -7.435  24.049 1.00 25.66  ? 41  SER B HA   1 
ATOM   3582 H  HB2  . SER B 1 41  ? -32.560 -5.540  24.922 1.00 29.31  ? 41  SER B HB2  1 
ATOM   3583 H  HB3  . SER B 1 41  ? -32.262 -5.922  23.403 1.00 29.31  ? 41  SER B HB3  1 
ATOM   3584 H  HG   . SER B 1 41  ? -32.626 -3.783  23.525 1.00 34.58  ? 41  SER B HG   1 
ATOM   3585 N  N    . VAL B 1 42  ? -36.229 -5.657  25.036 1.00 18.03  ? 42  VAL B N    1 
ATOM   3586 C  CA   . VAL B 1 42  ? -37.074 -5.264  26.158 1.00 18.34  ? 42  VAL B CA   1 
ATOM   3587 C  C    . VAL B 1 42  ? -38.506 -5.773  25.968 1.00 16.24  ? 42  VAL B C    1 
ATOM   3588 O  O    . VAL B 1 42  ? -39.487 -5.178  26.436 1.00 18.28  ? 42  VAL B O    1 
ATOM   3589 C  CB   . VAL B 1 42  ? -37.001 -3.751  26.386 1.00 19.37  ? 42  VAL B CB   1 
ATOM   3590 C  CG1  . VAL B 1 42  ? -35.570 -3.328  26.691 1.00 21.07  ? 42  VAL B CG1  1 
ATOM   3591 C  CG2  . VAL B 1 42  ? -37.546 -2.973  25.212 1.00 20.00  ? 42  VAL B CG2  1 
ATOM   3592 H  H    . VAL B 1 42  ? -36.529 -5.508  24.186 1.00 22.59  ? 42  VAL B H    1 
ATOM   3593 H  HA   . VAL B 1 42  ? -36.720 -5.695  26.957 1.00 24.04  ? 42  VAL B HA   1 
ATOM   3594 H  HB   . VAL B 1 42  ? -37.555 -3.540  27.177 1.00 21.87  ? 42  VAL B HB   1 
ATOM   3595 H  HG11 . VAL B 1 42  ? -35.567 -2.420  27.041 1.00 24.04  ? 42  VAL B HG11 1 
ATOM   3596 H  HG12 . VAL B 1 42  ? -35.186 -3.930  27.351 1.00 24.04  ? 42  VAL B HG12 1 
ATOM   3597 H  HG13 . VAL B 1 42  ? -35.040 -3.361  25.875 1.00 24.04  ? 42  VAL B HG13 1 
ATOM   3598 H  HG21 . VAL B 1 42  ? -37.359 -2.026  25.337 1.00 22.59  ? 42  VAL B HG21 1 
ATOM   3599 H  HG22 . VAL B 1 42  ? -37.123 -3.279  24.392 1.00 22.59  ? 42  VAL B HG22 1 
ATOM   3600 H  HG23 . VAL B 1 42  ? -38.508 -3.106  25.150 1.00 22.59  ? 42  VAL B HG23 1 
ATOM   3601 N  N    . SER B 1 43  ? -38.651 -6.949  25.365 1.00 14.30  ? 43  SER B N    1 
ATOM   3602 C  CA   . SER B 1 43  ? -39.958 -7.491  25.067 1.00 14.65  ? 43  SER B CA   1 
ATOM   3603 C  C    . SER B 1 43  ? -40.639 -8.007  26.329 1.00 13.14  ? 43  SER B C    1 
ATOM   3604 O  O    . SER B 1 43  ? -40.018 -8.486  27.274 1.00 12.64  ? 43  SER B O    1 
ATOM   3605 C  CB   . SER B 1 43  ? -39.813 -8.588  24.029 1.00 16.06  ? 43  SER B CB   1 
ATOM   3606 O  OG   . SER B 1 43  ? -38.912 -9.584  24.464 1.00 16.03  ? 43  SER B OG   1 
ATOM   3607 H  H    . SER B 1 43  ? -37.911 -7.435  25.140 1.00 16.80  ? 43  SER B H    1 
ATOM   3608 H  HA   . SER B 1 43  ? -40.514 -6.762  24.681 1.00 33.80  ? 43  SER B HA   1 
ATOM   3609 H  HB2  . SER B 1 43  ? -40.693 -8.994  23.859 1.00 32.22  ? 43  SER B HB2  1 
ATOM   3610 H  HB3  . SER B 1 43  ? -39.488 -8.199  23.186 1.00 32.21  ? 43  SER B HB3  1 
ATOM   3611 H  HG   . SER B 1 43  ? -38.876 -10.190 23.875 1.00 18.69  ? 43  SER B HG   1 
ATOM   3612 N  N    . PRO B 1 44  ? -41.984 -7.977  26.345 1.00 15.49  ? 44  PRO B N    1 
ATOM   3613 C  CA   . PRO B 1 44  ? -42.726 -8.500  27.477 1.00 14.77  ? 44  PRO B CA   1 
ATOM   3614 C  C    . PRO B 1 44  ? -42.815 -10.015 27.446 1.00 13.88  ? 44  PRO B C    1 
ATOM   3615 O  O    . PRO B 1 44  ? -42.658 -10.675 26.408 1.00 16.61  ? 44  PRO B O    1 
ATOM   3616 C  CB   . PRO B 1 44  ? -44.129 -7.928  27.290 1.00 16.80  ? 44  PRO B CB   1 
ATOM   3617 C  CG   . PRO B 1 44  ? -44.267 -7.823  25.782 1.00 21.56  ? 44  PRO B CG   1 
ATOM   3618 C  CD   . PRO B 1 44  ? -42.880 -7.466  25.286 1.00 20.34  ? 44  PRO B CD   1 
ATOM   3619 H  HA   . PRO B 1 44  ? -42.333 -8.180  28.327 1.00 18.19  ? 44  PRO B HA   1 
ATOM   3620 H  HB2  . PRO B 1 44  ? -44.811 -8.526  27.665 1.00 20.18  ? 44  PRO B HB2  1 
ATOM   3621 H  HB3  . PRO B 1 44  ? -44.210 -7.046  27.712 1.00 20.18  ? 44  PRO B HB3  1 
ATOM   3622 H  HG2  . PRO B 1 44  ? -44.564 -8.674  25.399 1.00 24.74  ? 44  PRO B HG2  1 
ATOM   3623 H  HG3  . PRO B 1 44  ? -44.909 -7.126  25.539 1.00 24.74  ? 44  PRO B HG3  1 
ATOM   3624 H  HD2  . PRO B 1 44  ? -42.693 -7.900  24.433 1.00 32.78  ? 44  PRO B HD2  1 
ATOM   3625 H  HD3  . PRO B 1 44  ? -42.783 -6.503  25.177 1.00 32.80  ? 44  PRO B HD3  1 
ATOM   3626 N  N    . GLN B 1 45  ? -43.095 -10.570 28.621 1.00 14.30  ? 45  GLN B N    1 
ATOM   3627 C  CA   . GLN B 1 45  ? -43.371 -11.990 28.731 1.00 15.11  ? 45  GLN B CA   1 
ATOM   3628 C  C    . GLN B 1 45  ? -44.843 -12.205 28.391 1.00 17.80  ? 45  GLN B C    1 
ATOM   3629 O  O    . GLN B 1 45  ? -45.685 -11.623 29.061 1.00 19.39  ? 45  GLN B O    1 
ATOM   3630 C  CB   . GLN B 1 45  ? -43.041 -12.486 30.147 1.00 15.61  ? 45  GLN B CB   1 
ATOM   3631 C  CG   . GLN B 1 45  ? -43.301 -13.952 30.328 1.00 15.61  ? 45  GLN B CG   1 
ATOM   3632 C  CD   . GLN B 1 45  ? -42.875 -14.376 31.705 1.00 16.30  ? 45  GLN B CD   1 
ATOM   3633 O  OE1  . GLN B 1 45  ? -41.742 -14.125 32.182 1.00 19.02  ? 45  GLN B OE1  1 
ATOM   3634 N  NE2  . GLN B 1 45  ? -43.801 -14.966 32.418 1.00 20.11  ? 45  GLN B NE2  1 
ATOM   3635 H  H    . GLN B 1 45  ? -43.118 -10.053 29.375 1.00 18.19  ? 45  GLN B H    1 
ATOM   3636 H  HA   . GLN B 1 45  ? -42.811 -12.474 28.085 1.00 22.97  ? 45  GLN B HA   1 
ATOM   3637 H  HB2  . GLN B 1 45  ? -42.097 -12.297 30.333 1.00 17.80  ? 45  GLN B HB2  1 
ATOM   3638 H  HB3  . GLN B 1 45  ? -43.583 -11.982 30.786 1.00 17.80  ? 45  GLN B HB3  1 
ATOM   3639 H  HG2  . GLN B 1 45  ? -44.256 -14.137 30.206 1.00 20.96  ? 45  GLN B HG2  1 
ATOM   3640 H  HG3  . GLN B 1 45  ? -42.800 -14.463 29.657 1.00 20.96  ? 45  GLN B HG3  1 
ATOM   3641 H  HE21 . GLN B 1 45  ? -44.624 -15.042 32.105 1.00 20.96  ? 45  GLN B HE21 1 
ATOM   3642 H  HE22 . GLN B 1 45  ? -43.604 -15.291 33.216 1.00 20.96  ? 45  GLN B HE22 1 
ATOM   3643 N  N    . PRO B 1 46  ? -45.201 -13.023 27.369 1.00 19.62  ? 46  PRO B N    1 
ATOM   3644 C  CA   . PRO B 1 46  ? -46.604 -13.280 27.062 1.00 22.83  ? 46  PRO B CA   1 
ATOM   3645 C  C    . PRO B 1 46  ? -47.323 -13.922 28.249 1.00 22.65  ? 46  PRO B C    1 
ATOM   3646 O  O    . PRO B 1 46  ? -46.741 -14.629 29.094 1.00 21.68  ? 46  PRO B O    1 
ATOM   3647 C  CB   . PRO B 1 46  ? -46.592 -14.251 25.870 1.00 25.56  ? 46  PRO B CB   1 
ATOM   3648 C  CG   . PRO B 1 46  ? -45.203 -14.159 25.309 1.00 22.68  ? 46  PRO B CG   1 
ATOM   3649 C  CD   . PRO B 1 46  ? -44.298 -13.725 26.441 1.00 20.27  ? 46  PRO B CD   1 
ATOM   3650 H  HA   . PRO B 1 46  ? -47.046 -12.434 26.802 1.00 26.58  ? 46  PRO B HA   1 
ATOM   3651 H  HB2  . PRO B 1 46  ? -46.788 -15.167 26.162 1.00 26.39  ? 46  PRO B HB2  1 
ATOM   3652 H  HB3  . PRO B 1 46  ? -47.256 -13.986 25.198 1.00 26.39  ? 46  PRO B HB3  1 
ATOM   3653 H  HG2  . PRO B 1 46  ? -44.918 -15.029 24.960 1.00 24.69  ? 46  PRO B HG2  1 
ATOM   3654 H  HG3  . PRO B 1 46  ? -45.172 -13.508 24.579 1.00 24.69  ? 46  PRO B HG3  1 
ATOM   3655 H  HD2  . PRO B 1 46  ? -43.883 -14.494 26.873 1.00 22.97  ? 46  PRO B HD2  1 
ATOM   3656 H  HD3  . PRO B 1 46  ? -43.598 -13.128 26.117 1.00 22.97  ? 46  PRO B HD3  1 
ATOM   3657 N  N    . PRO B 1 47  ? -48.659 -13.763 28.299 1.00 25.26  ? 47  PRO B N    1 
ATOM   3658 C  CA   . PRO B 1 47  ? -49.453 -14.393 29.350 1.00 26.31  ? 47  PRO B CA   1 
ATOM   3659 C  C    . PRO B 1 47  ? -49.346 -15.911 29.221 1.00 22.68  ? 47  PRO B C    1 
ATOM   3660 O  O    . PRO B 1 47  ? -49.145 -16.438 28.096 1.00 25.44  ? 47  PRO B O    1 
ATOM   3661 C  CB   . PRO B 1 47  ? -50.865 -13.828 29.165 1.00 30.66  ? 47  PRO B CB   1 
ATOM   3662 C  CG   . PRO B 1 47  ? -50.909 -13.288 27.751 1.00 31.52  ? 47  PRO B CG   1 
ATOM   3663 C  CD   . PRO B 1 47  ? -49.475 -13.008 27.340 1.00 27.44  ? 47  PRO B CD   1 
ATOM   3664 H  HA   . PRO B 1 47  ? -49.104 -14.106 30.231 1.00 25.08  ? 47  PRO B HA   1 
ATOM   3665 H  HB2  . PRO B 1 47  ? -51.538 -14.532 29.286 1.00 28.51  ? 47  PRO B HB2  1 
ATOM   3666 H  HB3  . PRO B 1 47  ? -51.040 -13.114 29.812 1.00 28.51  ? 47  PRO B HB3  1 
ATOM   3667 H  HG2  . PRO B 1 47  ? -51.313 -13.944 27.148 1.00 28.14  ? 47  PRO B HG2  1 
ATOM   3668 H  HG3  . PRO B 1 47  ? -51.440 -12.469 27.717 1.00 28.14  ? 47  PRO B HG3  1 
ATOM   3669 H  HD2  . PRO B 1 47  ? -49.310 -13.312 26.429 1.00 26.58  ? 47  PRO B HD2  1 
ATOM   3670 H  HD3  . PRO B 1 47  ? -49.278 -12.055 27.393 1.00 26.58  ? 47  PRO B HD3  1 
ATOM   3671 N  N    . GLY B 1 48  ? -49.248 -16.584 30.385 1.00 23.16  ? 48  GLY B N    1 
ATOM   3672 C  CA   . GLY B 1 48  ? -49.232 -18.053 30.428 1.00 20.33  ? 48  GLY B CA   1 
ATOM   3673 C  C    . GLY B 1 48  ? -47.935 -18.685 29.916 1.00 17.40  ? 48  GLY B C    1 
ATOM   3674 O  O    . GLY B 1 48  ? -47.927 -19.813 29.459 1.00 17.75  ? 48  GLY B O    1 
ATOM   3675 H  H    . GLY B 1 48  ? -49.189 -16.120 31.170 1.00 25.08  ? 48  GLY B H    1 
ATOM   3676 H  HA2  . GLY B 1 48  ? -49.382 -18.342 31.363 1.00 22.40  ? 48  GLY B HA2  1 
ATOM   3677 H  HA3  . GLY B 1 48  ? -49.989 -18.392 29.887 1.00 22.40  ? 48  GLY B HA3  1 
ATOM   3678 N  N    . THR B 1 49  ? -46.818 -17.968 30.021 1.00 16.44  ? 49  THR B N    1 
ATOM   3679 C  CA   . THR B 1 49  ? -45.507 -18.455 29.606 1.00 14.69  ? 49  THR B CA   1 
ATOM   3680 C  C    . THR B 1 49  ? -44.964 -19.466 30.614 1.00 15.00  ? 49  THR B C    1 
ATOM   3681 O  O    . THR B 1 49  ? -44.932 -19.211 31.820 1.00 17.43  ? 49  THR B O    1 
ATOM   3682 C  CB   . THR B 1 49  ? -44.514 -17.291 29.466 1.00 14.63  ? 49  THR B CB   1 
ATOM   3683 O  OG1  . THR B 1 49  ? -44.915 -16.472 28.372 1.00 16.12  ? 49  THR B OG1  1 
ATOM   3684 C  CG2  . THR B 1 49  ? -43.114 -17.781 29.201 1.00 14.71  ? 49  THR B CG2  1 
ATOM   3685 H  H    . THR B 1 49  ? -46.871 -17.128 30.377 1.00 18.39  ? 49  THR B H    1 
ATOM   3686 H  HA   . THR B 1 49  ? -45.604 -18.895 28.731 1.00 17.89  ? 49  THR B HA   1 
ATOM   3687 H  HB   . THR B 1 49  ? -44.524 -16.759 30.297 1.00 18.39  ? 49  THR B HB   1 
ATOM   3688 H  HG1  . THR B 1 49  ? -45.637 -16.075 28.565 1.00 19.15  ? 49  THR B HG1  1 
ATOM   3689 H  HG21 . THR B 1 49  ? -42.605 -17.083 28.752 1.00 17.16  ? 49  THR B HG21 1 
ATOM   3690 H  HG22 . THR B 1 49  ? -42.681 -18.005 30.044 1.00 17.16  ? 49  THR B HG22 1 
ATOM   3691 H  HG23 . THR B 1 49  ? -43.147 -18.572 28.633 1.00 17.16  ? 49  THR B HG23 1 
ATOM   3692 N  N    . LYS B 1 50  ? -44.490 -20.600 30.095 1.00 14.31  ? 50  LYS B N    1 
ATOM   3693 C  CA   . LYS B 1 50  ? -43.856 -21.638 30.880 1.00 14.71  ? 50  LYS B CA   1 
ATOM   3694 C  C    . LYS B 1 50  ? -42.332 -21.482 30.876 1.00 13.85  ? 50  LYS B C    1 
ATOM   3695 O  O    . LYS B 1 50  ? -41.691 -21.671 31.891 1.00 15.34  ? 50  LYS B O    1 
ATOM   3696 C  CB   . LYS B 1 50  ? -44.220 -23.001 30.304 1.00 16.57  ? 50  LYS B CB   1 
ATOM   3697 C  CG   . LYS B 1 50  ? -43.694 -24.210 31.051 1.00 20.45  ? 50  LYS B CG   1 
ATOM   3698 C  CD   . LYS B 1 50  ? -44.278 -24.353 32.403 1.00 25.75  ? 50  LYS B CD   1 
ATOM   3699 C  CE   . LYS B 1 50  ? -43.899 -25.668 33.045 1.00 28.79  ? 50  LYS B CE   1 
ATOM   3700 N  NZ   . LYS B 1 50  ? -44.505 -25.775 34.393 1.00 35.89  ? 50  LYS B NZ   1 
ATOM   3701 H  H    . LYS B 1 50  ? -44.569 -20.731 29.194 1.00 17.89  ? 50  LYS B H    1 
ATOM   3702 H  HA   . LYS B 1 50  ? -44.183 -21.582 31.807 1.00 44.66  ? 50  LYS B HA   1 
ATOM   3703 H  HB2  . LYS B 1 50  ? -45.197 -23.065 30.267 1.00 27.17  ? 50  LYS B HB2  1 
ATOM   3704 H  HB3  . LYS B 1 50  ? -43.887 -23.041 29.383 1.00 27.17  ? 50  LYS B HB3  1 
ATOM   3705 H  HG2  . LYS B 1 50  ? -43.895 -25.016 30.529 1.00 23.43  ? 50  LYS B HG2  1 
ATOM   3706 H  HG3  . LYS B 1 50  ? -42.719 -24.139 31.128 1.00 23.43  ? 50  LYS B HG3  1 
ATOM   3707 H  HD2  . LYS B 1 50  ? -43.965 -23.618 32.971 1.00 44.68  ? 50  LYS B HD2  1 
ATOM   3708 H  HD3  . LYS B 1 50  ? -45.256 -24.296 32.341 1.00 44.74  ? 50  LYS B HD3  1 
ATOM   3709 H  HE2  . LYS B 1 50  ? -44.213 -26.409 32.492 1.00 46.96  ? 50  LYS B HE2  1 
ATOM   3710 H  HE3  . LYS B 1 50  ? -42.930 -25.732 33.119 1.00 46.93  ? 50  LYS B HE3  1 
ATOM   3711 H  HZ1  . LYS B 1 50  ? -44.187 -26.512 34.815 1.00 41.34  ? 50  LYS B HZ1  1 
ATOM   3712 H  HZ2  . LYS B 1 50  ? -44.298 -25.040 34.882 1.00 41.35  ? 50  LYS B HZ2  1 
ATOM   3713 H  HZ3  . LYS B 1 50  ? -45.407 -25.840 34.320 1.00 41.34  ? 50  LYS B HZ3  1 
ATOM   3714 N  N    . TRP B 1 51  ? -41.739 -21.143 29.726 1.00 12.10  ? 51  TRP B N    1 
ATOM   3715 C  CA   . TRP B 1 51  ? -40.308 -20.923 29.646 1.00 12.08  ? 51  TRP B CA   1 
ATOM   3716 C  C    . TRP B 1 51  ? -40.035 -19.887 28.559 1.00 11.34  ? 51  TRP B C    1 
ATOM   3717 O  O    . TRP B 1 51  ? -40.848 -19.652 27.663 1.00 11.55  ? 51  TRP B O    1 
ATOM   3718 C  CB   . TRP B 1 51  ? -39.497 -22.221 29.445 1.00 12.95  ? 51  TRP B CB   1 
ATOM   3719 C  CG   . TRP B 1 51  ? -39.993 -23.169 28.391 1.00 12.16  ? 51  TRP B CG   1 
ATOM   3720 C  CD1  . TRP B 1 51  ? -40.611 -24.363 28.622 1.00 12.70  ? 51  TRP B CD1  1 
ATOM   3721 C  CD2  . TRP B 1 51  ? -39.853 -23.073 26.962 1.00 11.53  ? 51  TRP B CD2  1 
ATOM   3722 N  NE1  . TRP B 1 51  ? -40.878 -25.015 27.458 1.00 13.31  ? 51  TRP B NE1  1 
ATOM   3723 C  CE2  . TRP B 1 51  ? -40.416 -24.256 26.419 1.00 12.13  ? 51  TRP B CE2  1 
ATOM   3724 C  CE3  . TRP B 1 51  ? -39.332 -22.112 26.092 1.00 12.27  ? 51  TRP B CE3  1 
ATOM   3725 C  CZ2  . TRP B 1 51  ? -40.422 -24.503 25.047 1.00 13.03  ? 51  TRP B CZ2  1 
ATOM   3726 C  CZ3  . TRP B 1 51  ? -39.361 -22.358 24.734 1.00 12.83  ? 51  TRP B CZ3  1 
ATOM   3727 C  CH2  . TRP B 1 51  ? -39.904 -23.541 24.214 1.00 13.19  ? 51  TRP B CH2  1 
ATOM   3728 H  H    . TRP B 1 51  ? -42.242 -21.056 28.968 1.00 17.89  ? 51  TRP B H    1 
ATOM   3729 H  HA   . TRP B 1 51  ? -40.025 -20.536 30.508 1.00 13.94  ? 51  TRP B HA   1 
ATOM   3730 H  HB2  . TRP B 1 51  ? -38.577 -21.968 29.227 1.00 33.87  ? 51  TRP B HB2  1 
ATOM   3731 H  HB3  . TRP B 1 51  ? -39.474 -22.694 30.302 1.00 33.88  ? 51  TRP B HB3  1 
ATOM   3732 H  HD1  . TRP B 1 51  ? -40.819 -24.705 29.478 1.00 22.06  ? 51  TRP B HD1  1 
ATOM   3733 H  HE1  . TRP B 1 51  ? -41.257 -25.803 27.389 1.00 22.06  ? 51  TRP B HE1  1 
ATOM   3734 H  HE3  . TRP B 1 51  ? -38.923 -21.333 26.430 1.00 22.06  ? 51  TRP B HE3  1 
ATOM   3735 H  HZ2  . TRP B 1 51  ? -40.826 -25.278 24.701 1.00 22.07  ? 51  TRP B HZ2  1 
ATOM   3736 H  HZ3  . TRP B 1 51  ? -38.990 -21.723 24.142 1.00 22.06  ? 51  TRP B HZ3  1 
ATOM   3737 H  HH2  . TRP B 1 51  ? -39.932 -23.670 23.282 1.00 22.06  ? 51  TRP B HH2  1 
ATOM   3738 N  N    . LEU B 1 52  ? -38.849 -19.269 28.661 1.00 11.46  ? 52  LEU B N    1 
ATOM   3739 C  CA   A LEU B 1 52  ? -38.406 -18.195 27.770 0.56 10.99  ? 52  LEU B CA   1 
ATOM   3740 C  CA   B LEU B 1 52  ? -38.430 -18.199 27.797 0.44 11.31  ? 52  LEU B CA   1 
ATOM   3741 C  C    . LEU B 1 52  ? -36.971 -18.466 27.416 1.00 11.24  ? 52  LEU B C    1 
ATOM   3742 O  O    . LEU B 1 52  ? -36.148 -18.582 28.314 1.00 14.55  ? 52  LEU B O    1 
ATOM   3743 C  CB   A LEU B 1 52  ? -38.308 -16.806 28.427 0.56 12.20  ? 52  LEU B CB   1 
ATOM   3744 C  CB   B LEU B 1 52  ? -38.650 -16.959 28.679 0.44 13.13  ? 52  LEU B CB   1 
ATOM   3745 C  CG   A LEU B 1 52  ? -39.609 -16.099 28.761 0.56 11.90  ? 52  LEU B CG   1 
ATOM   3746 C  CG   B LEU B 1 52  ? -38.790 -15.627 27.969 0.44 13.33  ? 52  LEU B CG   1 
ATOM   3747 C  CD1  A LEU B 1 52  ? -39.311 -14.870 29.612 0.56 14.13  ? 52  LEU B CD1  1 
ATOM   3748 C  CD1  B LEU B 1 52  ? -39.948 -15.630 26.980 0.44 13.74  ? 52  LEU B CD1  1 
ATOM   3749 C  CD2  A LEU B 1 52  ? -40.405 -15.734 27.519 0.56 12.47  ? 52  LEU B CD2  1 
ATOM   3750 C  CD2  B LEU B 1 52  ? -39.002 -14.504 28.978 0.44 15.05  ? 52  LEU B CD2  1 
ATOM   3751 H  H    A LEU B 1 52  ? -38.282 -19.533 29.327 0.56 13.94  ? 52  LEU B H    1 
ATOM   3752 H  H    B LEU B 1 52  ? -38.274 -19.542 29.317 0.44 13.94  ? 52  LEU B H    1 
ATOM   3753 H  HA   A LEU B 1 52  ? -38.963 -18.168 26.960 0.56 19.09  ? 52  LEU B HA   1 
ATOM   3754 H  HA   B LEU B 1 52  ? -38.997 -18.169 26.994 0.44 19.08  ? 52  LEU B HA   1 
ATOM   3755 H  HB2  A LEU B 1 52  ? -37.799 -16.901 29.256 0.56 16.73  ? 52  LEU B HB2  1 
ATOM   3756 H  HB2  B LEU B 1 52  ? -39.457 -17.104 29.211 0.44 17.68  ? 52  LEU B HB2  1 
ATOM   3757 H  HB3  A LEU B 1 52  ? -37.791 -16.224 27.834 0.56 16.72  ? 52  LEU B HB3  1 
ATOM   3758 H  HB3  B LEU B 1 52  ? -37.900 -16.893 29.303 0.44 17.68  ? 52  LEU B HB3  1 
ATOM   3759 H  HG   A LEU B 1 52  ? -40.159 -16.717 29.302 0.56 20.63  ? 52  LEU B HG   1 
ATOM   3760 H  HG   B LEU B 1 52  ? -37.954 -15.448 27.472 0.44 16.92  ? 52  LEU B HG   1 
ATOM   3761 H  HD11 A LEU B 1 52  ? -40.136 -14.383 29.779 0.56 16.46  ? 52  LEU B HD11 1 
ATOM   3762 H  HD11 B LEU B 1 52  ? -40.069 -14.736 26.617 0.44 16.63  ? 52  LEU B HD11 1 
ATOM   3763 H  HD12 A LEU B 1 52  ? -38.921 -15.149 30.459 0.56 16.46  ? 52  LEU B HD12 1 
ATOM   3764 H  HD12 B LEU B 1 52  ? -39.755 -16.251 26.255 0.44 16.63  ? 52  LEU B HD12 1 
ATOM   3765 H  HD13 A LEU B 1 52  ? -38.684 -14.294 29.142 0.56 16.46  ? 52  LEU B HD13 1 
ATOM   3766 H  HD13 B LEU B 1 52  ? -40.763 -15.908 27.434 0.44 16.63  ? 52  LEU B HD13 1 
ATOM   3767 H  HD21 A LEU B 1 52  ? -41.200 -15.236 27.777 0.56 19.11  ? 52  LEU B HD21 1 
ATOM   3768 H  HD21 B LEU B 1 52  ? -39.139 -13.664 28.506 0.44 17.48  ? 52  LEU B HD21 1 
ATOM   3769 H  HD22 A LEU B 1 52  ? -39.857 -15.186 26.931 0.56 19.11  ? 52  LEU B HD22 1 
ATOM   3770 H  HD22 B LEU B 1 52  ? -39.783 -14.700 29.524 0.44 17.48  ? 52  LEU B HD22 1 
ATOM   3771 H  HD23 A LEU B 1 52  ? -40.668 -16.545 27.052 0.56 19.11  ? 52  LEU B HD23 1 
ATOM   3772 H  HD23 B LEU B 1 52  ? -38.218 -14.429 29.550 0.44 17.48  ? 52  LEU B HD23 1 
ATOM   3773 N  N    . LEU B 1 53  ? -36.675 -18.522 26.114 1.00 10.10  ? 53  LEU B N    1 
ATOM   3774 C  CA   . LEU B 1 53  ? -35.299 -18.709 25.639 1.00 10.34  ? 53  LEU B CA   1 
ATOM   3775 C  C    . LEU B 1 53  ? -34.933 -17.528 24.760 1.00 9.78   ? 53  LEU B C    1 
ATOM   3776 O  O    . LEU B 1 53  ? -35.648 -17.202 23.824 1.00 11.27  ? 53  LEU B O    1 
ATOM   3777 C  CB   . LEU B 1 53  ? -35.200 -20.002 24.830 1.00 10.89  ? 53  LEU B CB   1 
ATOM   3778 C  CG   . LEU B 1 53  ? -35.605 -21.282 25.538 1.00 11.53  ? 53  LEU B CG   1 
ATOM   3779 C  CD1  . LEU B 1 53  ? -35.591 -22.451 24.565 1.00 12.64  ? 53  LEU B CD1  1 
ATOM   3780 C  CD2  . LEU B 1 53  ? -34.746 -21.558 26.750 1.00 13.80  ? 53  LEU B CD2  1 
ATOM   3781 H  H    . LEU B 1 53  ? -37.344 -18.445 25.495 1.00 19.08  ? 53  LEU B H    1 
ATOM   3782 H  HA   . LEU B 1 53  ? -34.689 -18.745 26.411 1.00 15.71  ? 53  LEU B HA   1 
ATOM   3783 H  HB2  . LEU B 1 53  ? -35.759 -19.905 24.033 1.00 13.15  ? 53  LEU B HB2  1 
ATOM   3784 H  HB3  . LEU B 1 53  ? -34.275 -20.100 24.526 1.00 13.15  ? 53  LEU B HB3  1 
ATOM   3785 H  HG   . LEU B 1 53  ? -36.536 -21.168 25.852 1.00 14.10  ? 53  LEU B HG   1 
ATOM   3786 H  HD11 . LEU B 1 53  ? -35.846 -23.266 25.032 1.00 15.65  ? 53  LEU B HD11 1 
ATOM   3787 H  HD12 . LEU B 1 53  ? -36.222 -22.281 23.843 1.00 15.65  ? 53  LEU B HD12 1 
ATOM   3788 H  HD13 . LEU B 1 53  ? -34.697 -22.556 24.195 1.00 15.65  ? 53  LEU B HD13 1 
ATOM   3789 H  HD21 . LEU B 1 53  ? -34.938 -22.450 27.089 1.00 15.70  ? 53  LEU B HD21 1 
ATOM   3790 H  HD22 . LEU B 1 53  ? -33.807 -21.501 26.503 1.00 15.70  ? 53  LEU B HD22 1 
ATOM   3791 H  HD23 . LEU B 1 53  ? -34.940 -20.901 27.442 1.00 15.70  ? 53  LEU B HD23 1 
ATOM   3792 N  N    . ARG B 1 54  ? -33.796 -16.887 25.027 1.00 10.15  ? 54  ARG B N    1 
ATOM   3793 C  CA   . ARG B 1 54  ? -33.362 -15.724 24.277 1.00 9.73   ? 54  ARG B CA   1 
ATOM   3794 C  C    . ARG B 1 54  ? -32.055 -16.041 23.564 1.00 9.22   ? 54  ARG B C    1 
ATOM   3795 O  O    . ARG B 1 54  ? -31.176 -16.722 24.099 1.00 9.67   ? 54  ARG B O    1 
ATOM   3796 C  CB   . ARG B 1 54  ? -33.191 -14.517 25.201 1.00 11.22  ? 54  ARG B CB   1 
ATOM   3797 C  CG   . ARG B 1 54  ? -32.666 -13.257 24.524 1.00 11.21  ? 54  ARG B CG   1 
ATOM   3798 C  CD   . ARG B 1 54  ? -32.775 -12.012 25.367 1.00 12.40  ? 54  ARG B CD   1 
ATOM   3799 N  NE   . ARG B 1 54  ? -34.164 -11.602 25.404 1.00 13.14  ? 54  ARG B NE   1 
ATOM   3800 C  CZ   . ARG B 1 54  ? -34.641 -10.662 26.205 1.00 13.65  ? 54  ARG B CZ   1 
ATOM   3801 N  NH1  . ARG B 1 54  ? -33.828 -9.953  26.954 1.00 16.24  ? 54  ARG B NH1  1 
ATOM   3802 N  NH2  . ARG B 1 54  ? -35.940 -10.404 26.219 1.00 15.07  ? 54  ARG B NH2  1 
ATOM   3803 H  H    . ARG B 1 54  ? -33.266 -17.188 25.707 1.00 15.71  ? 54  ARG B H    1 
ATOM   3804 H  HA   . ARG B 1 54  ? -34.047 -15.511 23.604 1.00 11.40  ? 54  ARG B HA   1 
ATOM   3805 H  HB2  . ARG B 1 54  ? -34.059 -14.315 25.608 1.00 13.51  ? 54  ARG B HB2  1 
ATOM   3806 H  HB3  . ARG B 1 54  ? -32.575 -14.765 25.921 1.00 13.51  ? 54  ARG B HB3  1 
ATOM   3807 H  HG2  . ARG B 1 54  ? -31.723 -13.391 24.289 1.00 15.93  ? 54  ARG B HG2  1 
ATOM   3808 H  HG3  . ARG B 1 54  ? -33.160 -13.115 23.688 1.00 15.93  ? 54  ARG B HG3  1 
ATOM   3809 H  HD2  . ARG B 1 54  ? -32.456 -12.196 26.277 1.00 16.13  ? 54  ARG B HD2  1 
ATOM   3810 H  HD3  . ARG B 1 54  ? -32.225 -11.297 24.981 1.00 16.13  ? 54  ARG B HD3  1 
ATOM   3811 H  HE   . ARG B 1 54  ? -34.723 -11.999 24.865 1.00 15.94  ? 54  ARG B HE   1 
ATOM   3812 H  HH11 . ARG B 1 54  ? -33.140 -9.541  26.588 1.00 16.05  ? 54  ARG B HH11 1 
ATOM   3813 H  HH12 . ARG B 1 54  ? -33.975 -9.888  27.820 1.00 16.05  ? 54  ARG B HH12 1 
ATOM   3814 H  HH21 . ARG B 1 54  ? -36.490 -10.891 25.736 1.00 15.94  ? 54  ARG B HH21 1 
ATOM   3815 H  HH22 . ARG B 1 54  ? -36.250 -9.746  26.713 1.00 15.94  ? 54  ARG B HH22 1 
ATOM   3816 N  N    . GLY B 1 55  ? -31.920 -15.486 22.360 1.00 9.29   ? 55  GLY B N    1 
ATOM   3817 C  CA   . GLY B 1 55  ? -30.672 -15.539 21.620 1.00 9.42   ? 55  GLY B CA   1 
ATOM   3818 C  C    . GLY B 1 55  ? -30.528 -14.321 20.721 1.00 9.13   ? 55  GLY B C    1 
ATOM   3819 O  O    . GLY B 1 55  ? -31.483 -13.565 20.550 1.00 10.73  ? 55  GLY B O    1 
ATOM   3820 H  H    . GLY B 1 55  ? -32.635 -15.059 21.983 1.00 11.40  ? 55  GLY B H    1 
ATOM   3821 H  HA2  . GLY B 1 55  ? -29.913 -15.571 22.255 1.00 13.61  ? 55  GLY B HA2  1 
ATOM   3822 H  HA3  . GLY B 1 55  ? -30.654 -16.361 21.069 1.00 13.61  ? 55  GLY B HA3  1 
ATOM   3823 N  N    . ILE B 1 56  ? -29.330 -14.163 20.162 1.00 8.81   ? 56  ILE B N    1 
ATOM   3824 C  CA   . ILE B 1 56  ? -29.029 -12.991 19.354 1.00 8.99   ? 56  ILE B CA   1 
ATOM   3825 C  C    . ILE B 1 56  ? -28.370 -13.449 18.057 1.00 8.78   ? 56  ILE B C    1 
ATOM   3826 O  O    . ILE B 1 56  ? -27.468 -14.290 18.064 1.00 9.28   ? 56  ILE B O    1 
ATOM   3827 C  CB   . ILE B 1 56  ? -28.197 -11.969 20.152 1.00 8.90   ? 56  ILE B CB   1 
ATOM   3828 C  CG1  . ILE B 1 56  ? -28.173 -10.595 19.478 1.00 9.51   ? 56  ILE B CG1  1 
ATOM   3829 C  CG2  . ILE B 1 56  ? -26.779 -12.447 20.437 1.00 9.26   ? 56  ILE B CG2  1 
ATOM   3830 C  CD1  . ILE B 1 56  ? -27.518 -9.509  20.281 1.00 10.17  ? 56  ILE B CD1  1 
ATOM   3831 H  H    . ILE B 1 56  ? -28.684 -14.798 20.283 1.00 11.82  ? 56  ILE B H    1 
ATOM   3832 H  HA   . ILE B 1 56  ? -29.871 -12.565 19.123 1.00 13.07  ? 56  ILE B HA   1 
ATOM   3833 H  HB   . ILE B 1 56  ? -28.645 -11.853 21.026 1.00 10.92  ? 56  ILE B HB   1 
ATOM   3834 H  HG12 . ILE B 1 56  ? -27.704 -10.675 18.622 1.00 12.90  ? 56  ILE B HG12 1 
ATOM   3835 H  HG13 . ILE B 1 56  ? -29.097 -10.326 19.287 1.00 12.91  ? 56  ILE B HG13 1 
ATOM   3836 H  HG21 . ILE B 1 56  ? -26.458 -12.044 21.262 1.00 11.82  ? 56  ILE B HG21 1 
ATOM   3837 H  HG22 . ILE B 1 56  ? -26.773 -13.414 20.528 1.00 11.82  ? 56  ILE B HG22 1 
ATOM   3838 H  HG23 . ILE B 1 56  ? -26.194 -12.189 19.703 1.00 11.83  ? 56  ILE B HG23 1 
ATOM   3839 H  HD11 . ILE B 1 56  ? -27.752 -8.641  19.909 1.00 11.99  ? 56  ILE B HD11 1 
ATOM   3840 H  HD12 . ILE B 1 56  ? -27.822 -9.557  21.204 1.00 11.99  ? 56  ILE B HD12 1 
ATOM   3841 H  HD13 . ILE B 1 56  ? -26.552 -9.621  20.254 1.00 11.99  ? 56  ILE B HD13 1 
ATOM   3842 N  N    . THR B 1 57  ? -28.802 -12.881 16.927 1.00 9.06   ? 57  THR B N    1 
ATOM   3843 C  CA   . THR B 1 57  ? -28.058 -13.134 15.703 1.00 9.52   ? 57  THR B CA   1 
ATOM   3844 C  C    . THR B 1 57  ? -26.714 -12.408 15.793 1.00 9.13   ? 57  THR B C    1 
ATOM   3845 O  O    . THR B 1 57  ? -26.600 -11.401 16.496 1.00 10.08  ? 57  THR B O    1 
ATOM   3846 C  CB   . THR B 1 57  ? -28.849 -12.720 14.469 1.00 10.67  ? 57  THR B CB   1 
ATOM   3847 O  OG1  . THR B 1 57  ? -29.047 -11.303 14.496 1.00 11.35  ? 57  THR B OG1  1 
ATOM   3848 C  CG2  . THR B 1 57  ? -30.185 -13.420 14.367 1.00 11.74  ? 57  THR B CG2  1 
ATOM   3849 H  H    . THR B 1 57  ? -29.539 -12.341 16.914 1.00 13.20  ? 57  THR B H    1 
ATOM   3850 H  HA   . THR B 1 57  ? -27.885 -14.102 15.646 1.00 11.52  ? 57  THR B HA   1 
ATOM   3851 H  HB   . THR B 1 57  ? -28.314 -12.948 13.672 1.00 21.16  ? 57  THR B HB   1 
ATOM   3852 H  HG1  . THR B 1 57  ? -29.341 -11.042 13.745 1.00 13.63  ? 57  THR B HG1  1 
ATOM   3853 H  HG21 . THR B 1 57  ? -30.583 -13.238 13.497 1.00 13.35  ? 57  THR B HG21 1 
ATOM   3854 H  HG22 . THR B 1 57  ? -30.058 -14.380 14.470 1.00 13.35  ? 57  THR B HG22 1 
ATOM   3855 H  HG23 . THR B 1 57  ? -30.779 -13.096 15.068 1.00 13.35  ? 57  THR B HG23 1 
ATOM   3856 N  N    . SER B 1 58  ? -25.706 -12.957 15.124 1.00 9.55   ? 58  SER B N    1 
ATOM   3857 C  CA   . SER B 1 58  ? -24.366 -12.432 15.309 1.00 9.70   ? 58  SER B CA   1 
ATOM   3858 C  C    . SER B 1 58  ? -23.546 -12.551 14.035 1.00 9.84   ? 58  SER B C    1 
ATOM   3859 O  O    . SER B 1 58  ? -24.006 -13.009 13.005 1.00 10.78  ? 58  SER B O    1 
ATOM   3860 C  CB   . SER B 1 58  ? -23.732 -13.130 16.491 1.00 9.56   ? 58  SER B CB   1 
ATOM   3861 O  OG   . SER B 1 58  ? -22.504 -12.538 16.888 1.00 9.81   ? 58  SER B OG   1 
ATOM   3862 H  H    . SER B 1 58  ? -25.846 -13.657 14.552 1.00 11.52  ? 58  SER B H    1 
ATOM   3863 H  HA   . SER B 1 58  ? -24.444 -11.464 15.527 1.00 11.69  ? 58  SER B HA   1 
ATOM   3864 H  HB2  . SER B 1 58  ? -24.359 -13.109 17.249 1.00 11.68  ? 58  SER B HB2  1 
ATOM   3865 H  HB3  . SER B 1 58  ? -23.574 -14.072 16.258 1.00 11.68  ? 58  SER B HB3  1 
ATOM   3866 H  HG   . SER B 1 58  ? -22.659 -11.749 17.151 1.00 11.71  ? 58  SER B HG   1 
ATOM   3867 N  N    . ASN B 1 59  ? -22.309 -12.091 14.133 1.00 9.55   ? 59  ASN B N    1 
ATOM   3868 C  CA   . ASN B 1 59  ? -21.404 -12.192 13.012 1.00 9.76   ? 59  ASN B CA   1 
ATOM   3869 C  C    . ASN B 1 59  ? -21.021 -13.649 12.751 1.00 9.59   ? 59  ASN B C    1 
ATOM   3870 O  O    . ASN B 1 59  ? -21.086 -14.502 13.628 1.00 9.59   ? 59  ASN B O    1 
ATOM   3871 C  CB   . ASN B 1 59  ? -20.146 -11.349 13.209 1.00 10.46  ? 59  ASN B CB   1 
ATOM   3872 C  CG   . ASN B 1 59  ? -19.374 -11.771 14.453 1.00 9.92   ? 59  ASN B CG   1 
ATOM   3873 O  OD1  . ASN B 1 59  ? -19.759 -11.424 15.574 1.00 10.68  ? 59  ASN B OD1  1 
ATOM   3874 N  ND2  . ASN B 1 59  ? -18.278 -12.489 14.268 1.00 10.69  ? 59  ASN B ND2  1 
ATOM   3875 H  H    . ASN B 1 59  ? -22.024 -11.697 14.906 1.00 11.71  ? 59  ASN B H    1 
ATOM   3876 H  HA   . ASN B 1 59  ? -21.868 -11.844 12.214 1.00 13.17  ? 59  ASN B HA   1 
ATOM   3877 H  HB2  . ASN B 1 59  ? -19.571 -11.442 12.422 1.00 12.71  ? 59  ASN B HB2  1 
ATOM   3878 H  HB3  . ASN B 1 59  ? -20.402 -10.407 13.291 1.00 12.71  ? 59  ASN B HB3  1 
ATOM   3879 H  HD21 . ASN B 1 59  ? -17.674 -12.548 14.911 1.00 12.71  ? 59  ASN B HD21 1 
ATOM   3880 H  HD22 . ASN B 1 59  ? -18.148 -12.912 13.502 1.00 12.71  ? 59  ASN B HD22 1 
ATOM   3881 N  N    . GLU B 1 60  ? -20.598 -13.915 11.518 1.00 9.84   ? 60  GLU B N    1 
ATOM   3882 C  CA   . GLU B 1 60  ? -20.135 -15.232 11.120 1.00 9.92   ? 60  GLU B CA   1 
ATOM   3883 C  C    . GLU B 1 60  ? -18.885 -15.618 11.900 1.00 9.25   ? 60  GLU B C    1 
ATOM   3884 O  O    . GLU B 1 60  ? -17.990 -14.801 12.103 1.00 10.22  ? 60  GLU B O    1 
ATOM   3885 C  CB   . GLU B 1 60  ? -19.853 -15.225 9.627  1.00 10.85  ? 60  GLU B CB   1 
ATOM   3886 C  CG   . GLU B 1 60  ? -21.131 -15.149 8.808  1.00 12.07  ? 60  GLU B CG   1 
ATOM   3887 C  CD   . GLU B 1 60  ? -20.973 -14.537 7.435  1.00 14.81  ? 60  GLU B CD   1 
ATOM   3888 O  OE1  . GLU B 1 60  ? -20.017 -13.749 7.244  1.00 18.18  ? 60  GLU B OE1  1 
ATOM   3889 O  OE2  . GLU B 1 60  ? -21.857 -14.767 6.563  1.00 16.53  ? 60  GLU B OE2  1 
ATOM   3890 H  H    . GLU B 1 60  ? -20.596 -13.245 10.897 1.00 13.17  ? 60  GLU B H    1 
ATOM   3891 H  HA   . GLU B 1 60  ? -20.848 -15.884 11.310 1.00 18.65  ? 60  GLU B HA   1 
ATOM   3892 H  HB2  . GLU B 1 60  ? -19.282 -14.458 9.417  1.00 13.17  ? 60  GLU B HB2  1 
ATOM   3893 H  HB3  . GLU B 1 60  ? -19.367 -16.043 9.391  1.00 13.17  ? 60  GLU B HB3  1 
ATOM   3894 H  HG2  . GLU B 1 60  ? -21.493 -16.054 8.701  1.00 25.39  ? 60  GLU B HG2  1 
ATOM   3895 H  HG3  . GLU B 1 60  ? -21.796 -14.624 9.303  1.00 25.45  ? 60  GLU B HG3  1 
ATOM   3896 N  N    . ARG B 1 61  ? -18.876 -16.873 12.302 1.00 9.36   ? 61  ARG B N    1 
ATOM   3897 C  CA   . ARG B 1 61  ? -17.780 -17.464 13.051 1.00 9.07   ? 61  ARG B CA   1 
ATOM   3898 C  C    . ARG B 1 61  ? -16.961 -18.441 12.237 1.00 9.36   ? 61  ARG B C    1 
ATOM   3899 O  O    . ARG B 1 61  ? -15.807 -18.730 12.596 1.00 10.56  ? 61  ARG B O    1 
ATOM   3900 C  CB   . ARG B 1 61  ? -18.318 -18.187 14.292 1.00 10.10  ? 61  ARG B CB   1 
ATOM   3901 C  CG   . ARG B 1 61  ? -19.278 -17.349 15.118 1.00 9.98   ? 61  ARG B CG   1 
ATOM   3902 C  CD   . ARG B 1 61  ? -18.694 -16.019 15.576 1.00 9.97   ? 61  ARG B CD   1 
ATOM   3903 N  NE   . ARG B 1 61  ? -19.690 -15.213 16.291 1.00 9.99   ? 61  ARG B NE   1 
ATOM   3904 C  CZ   . ARG B 1 61  ? -20.052 -15.441 17.551 1.00 9.28   ? 61  ARG B CZ   1 
ATOM   3905 N  NH1  . ARG B 1 61  ? -19.423 -16.353 18.273 1.00 10.00  ? 61  ARG B NH1  1 
ATOM   3906 N  NH2  . ARG B 1 61  ? -21.065 -14.767 18.077 1.00 10.55  ? 61  ARG B NH2  1 
ATOM   3907 H  H    . ARG B 1 61  ? -19.603 -17.395 12.121 1.00 18.65  ? 61  ARG B H    1 
ATOM   3908 H  HA   . ARG B 1 61  ? -17.184 -16.739 13.347 1.00 12.08  ? 61  ARG B HA   1 
ATOM   3909 H  HB2  . ARG B 1 61  ? -18.777 -19.003 14.005 1.00 13.47  ? 61  ARG B HB2  1 
ATOM   3910 H  HB3  . ARG B 1 61  ? -17.562 -18.449 14.855 1.00 13.47  ? 61  ARG B HB3  1 
ATOM   3911 H  HG2  . ARG B 1 61  ? -20.085 -17.173 14.589 1.00 12.08  ? 61  ARG B HG2  1 
ATOM   3912 H  HG3  . ARG B 1 61  ? -19.549 -17.863 15.907 1.00 12.08  ? 61  ARG B HG3  1 
ATOM   3913 H  HD2  . ARG B 1 61  ? -17.926 -16.185 16.163 1.00 12.08  ? 61  ARG B HD2  1 
ATOM   3914 H  HD3  . ARG B 1 61  ? -18.375 -15.517 14.797 1.00 12.08  ? 61  ARG B HD3  1 
ATOM   3915 H  HE   . ARG B 1 61  ? -20.065 -14.549 15.868 1.00 12.14  ? 61  ARG B HE   1 
ATOM   3916 H  HH11 . ARG B 1 61  ? -19.260 -17.149 17.936 1.00 12.08  ? 61  ARG B HH11 1 
ATOM   3917 H  HH12 . ARG B 1 61  ? -19.172 -16.163 19.095 1.00 12.08  ? 61  ARG B HH12 1 
ATOM   3918 H  HH21 . ARG B 1 61  ? -21.281 -13.978 17.755 1.00 12.14  ? 61  ARG B HH21 1 
ATOM   3919 H  HH22 . ARG B 1 61  ? -21.517 -15.110 18.748 1.00 12.14  ? 61  ARG B HH22 1 
ATOM   3920 N  N    . TYR B 1 62  ? -17.549 -19.003 11.189 1.00 9.11   ? 62  TYR B N    1 
ATOM   3921 C  CA   . TYR B 1 62  ? -16.918 -20.063 10.403 1.00 9.75   ? 62  TYR B CA   1 
ATOM   3922 C  C    . TYR B 1 62  ? -16.994 -19.825 8.901  1.00 10.02  ? 62  TYR B C    1 
ATOM   3923 O  O    . TYR B 1 62  ? -16.070 -20.185 8.169  1.00 11.25  ? 62  TYR B O    1 
ATOM   3924 C  CB   . TYR B 1 62  ? -17.526 -21.444 10.704 1.00 10.07  ? 62  TYR B CB   1 
ATOM   3925 C  CG   . TYR B 1 62  ? -17.371 -21.827 12.156 1.00 9.74   ? 62  TYR B CG   1 
ATOM   3926 C  CD1  . TYR B 1 62  ? -16.134 -22.110 12.691 1.00 9.91   ? 62  TYR B CD1  1 
ATOM   3927 C  CD2  . TYR B 1 62  ? -18.442 -21.865 13.020 1.00 10.24  ? 62  TYR B CD2  1 
ATOM   3928 C  CE1  . TYR B 1 62  ? -15.964 -22.410 14.031 1.00 10.12  ? 62  TYR B CE1  1 
ATOM   3929 C  CE2  . TYR B 1 62  ? -18.293 -22.140 14.362 1.00 10.06  ? 62  TYR B CE2  1 
ATOM   3930 C  CZ   . TYR B 1 62  ? -17.047 -22.402 14.879 1.00 9.61   ? 62  TYR B CZ   1 
ATOM   3931 O  OH   . TYR B 1 62  ? -16.848 -22.677 16.200 1.00 10.29  ? 62  TYR B OH   1 
ATOM   3932 H  H    . TYR B 1 62  ? -18.386 -18.728 10.952 1.00 18.65  ? 62  TYR B H    1 
ATOM   3933 H  HA   . TYR B 1 62  ? -15.959 -20.096 10.648 1.00 11.75  ? 62  TYR B HA   1 
ATOM   3934 H  HB2  . TYR B 1 62  ? -18.478 -21.429 10.472 1.00 12.15  ? 62  TYR B HB2  1 
ATOM   3935 H  HB3  . TYR B 1 62  ? -17.084 -22.115 10.143 1.00 12.15  ? 62  TYR B HB3  1 
ATOM   3936 H  HD1  . TYR B 1 62  ? -15.376 -22.084 12.130 1.00 12.15  ? 62  TYR B HD1  1 
ATOM   3937 H  HD2  . TYR B 1 62  ? -19.300 -21.651 12.693 1.00 12.15  ? 62  TYR B HD2  1 
ATOM   3938 H  HE1  . TYR B 1 62  ? -15.102 -22.580 14.371 1.00 12.15  ? 62  TYR B HE1  1 
ATOM   3939 H  HE2  . TYR B 1 62  ? -19.046 -22.143 14.930 1.00 12.15  ? 62  TYR B HE2  1 
ATOM   3940 H  HH   . TYR B 1 62  ? -17.498 -22.975 16.681 1.00 12.20  ? 62  TYR B HH   1 
ATOM   3941 N  N    . VAL B 1 63  ? -18.115 -19.298 8.410  1.00 10.72  ? 63  VAL B N    1 
ATOM   3942 C  CA   . VAL B 1 63  ? -18.347 -19.166 6.976  1.00 11.93  ? 63  VAL B CA   1 
ATOM   3943 C  C    . VAL B 1 63  ? -17.255 -18.363 6.308  1.00 11.43  ? 63  VAL B C    1 
ATOM   3944 O  O    . VAL B 1 63  ? -16.933 -17.257 6.753  1.00 12.25  ? 63  VAL B O    1 
ATOM   3945 C  CB   . VAL B 1 63  ? -19.675 -18.383 6.736  1.00 15.13  ? 63  VAL B CB   1 
ATOM   3946 C  CG1  . VAL B 1 63  ? -19.858 -17.811 5.321  1.00 16.50  ? 63  VAL B CG1  1 
ATOM   3947 C  CG2  . VAL B 1 63  ? -20.860 -19.191 7.104  1.00 16.46  ? 63  VAL B CG2  1 
ATOM   3948 H  H    . VAL B 1 63  ? -18.765 -19.014 8.986  1.00 18.65  ? 63  VAL B H    1 
ATOM   3949 H  HA   . VAL B 1 63  ? -18.407 -20.049 6.571  1.00 17.48  ? 63  VAL B HA   1 
ATOM   3950 H  HB   . VAL B 1 63  ? -19.656 -17.610 7.353  1.00 18.65  ? 63  VAL B HB   1 
ATOM   3951 H  HG11 . VAL B 1 63  ? -20.797 -17.608 5.171  1.00 18.66  ? 63  VAL B HG11 1 
ATOM   3952 H  HG12 . VAL B 1 63  ? -19.333 -16.997 5.227  1.00 18.66  ? 63  VAL B HG12 1 
ATOM   3953 H  HG13 . VAL B 1 63  ? -19.561 -18.466 4.665  1.00 18.66  ? 63  VAL B HG13 1 
ATOM   3954 H  HG21 . VAL B 1 63  ? -21.635 -18.610 7.191  1.00 18.65  ? 63  VAL B HG21 1 
ATOM   3955 H  HG22 . VAL B 1 63  ? -21.028 -19.851 6.409  1.00 18.65  ? 63  VAL B HG22 1 
ATOM   3956 H  HG23 . VAL B 1 63  ? -20.699 -19.645 7.948  1.00 18.65  ? 63  VAL B HG23 1 
ATOM   3957 N  N    . VAL B 1 64  ? -16.754 -18.889 5.193  1.00 11.74  ? 64  VAL B N    1 
ATOM   3958 C  CA   . VAL B 1 64  ? -15.817 -18.141 4.377  1.00 12.48  ? 64  VAL B CA   1 
ATOM   3959 C  C    . VAL B 1 64  ? -16.568 -17.500 3.210  1.00 12.74  ? 64  VAL B C    1 
ATOM   3960 O  O    . VAL B 1 64  ? -17.684 -17.895 2.879  1.00 12.91  ? 64  VAL B O    1 
ATOM   3961 C  CB   . VAL B 1 64  ? -14.639 -19.005 3.915  1.00 13.77  ? 64  VAL B CB   1 
ATOM   3962 C  CG1  . VAL B 1 64  ? -13.983 -19.662 5.117  1.00 14.39  ? 64  VAL B CG1  1 
ATOM   3963 C  CG2  . VAL B 1 64  ? -15.043 -20.018 2.873  1.00 14.80  ? 64  VAL B CG2  1 
ATOM   3964 H  H    . VAL B 1 64  ? -16.999 -19.730 4.933  1.00 17.48  ? 64  VAL B H    1 
ATOM   3965 H  HA   . VAL B 1 64  ? -15.455 -17.422 4.924  1.00 15.22  ? 64  VAL B HA   1 
ATOM   3966 H  HB   . VAL B 1 64  ? -13.975 -18.402 3.503  1.00 16.39  ? 64  VAL B HB   1 
ATOM   3967 H  HG11 . VAL B 1 64  ? -13.113 -20.014 4.860  1.00 16.84  ? 64  VAL B HG11 1 
ATOM   3968 H  HG12 . VAL B 1 64  ? -13.868 -19.004 5.825  1.00 16.84  ? 64  VAL B HG12 1 
ATOM   3969 H  HG13 . VAL B 1 64  ? -14.544 -20.388 5.438  1.00 16.84  ? 64  VAL B HG13 1 
ATOM   3970 H  HG21 . VAL B 1 64  ? -14.396 -20.746 2.858  1.00 17.48  ? 64  VAL B HG21 1 
ATOM   3971 H  HG22 . VAL B 1 64  ? -15.922 -20.372 3.084  1.00 17.48  ? 64  VAL B HG22 1 
ATOM   3972 H  HG23 . VAL B 1 64  ? -15.068 -19.593 1.999  1.00 17.48  ? 64  VAL B HG23 1 
ATOM   3973 N  N    . ARG B 1 65  ? -15.954 -16.485 2.574  1.00 13.70  ? 65  ARG B N    1 
ATOM   3974 C  CA   . ARG B 1 65  ? -16.665 -15.714 1.553  1.00 14.76  ? 65  ARG B CA   1 
ATOM   3975 C  C    . ARG B 1 65  ? -17.265 -16.621 0.472  1.00 14.87  ? 65  ARG B C    1 
ATOM   3976 O  O    . ARG B 1 65  ? -18.399 -16.410 0.035  1.00 15.59  ? 65  ARG B O    1 
ATOM   3977 C  CB   . ARG B 1 65  ? -15.757 -14.629 0.964  1.00 16.60  ? 65  ARG B CB   1 
ATOM   3978 C  CG   . ARG B 1 65  ? -16.453 -13.791 -0.123 1.00 19.47  ? 65  ARG B CG   1 
ATOM   3979 C  CD   . ARG B 1 65  ? -17.671 -12.984 0.365  1.00 20.81  ? 65  ARG B CD   1 
ATOM   3980 N  NE   . ARG B 1 65  ? -17.395 -11.942 1.377  1.00 21.07  ? 65  ARG B NE   1 
ATOM   3981 C  CZ   . ARG B 1 65  ? -18.287 -11.121 1.961  1.00 22.06  ? 65  ARG B CZ   1 
ATOM   3982 N  NH1  . ARG B 1 65  ? -19.575 -11.191 1.659  1.00 24.55  ? 65  ARG B NH1  1 
ATOM   3983 N  NH2  . ARG B 1 65  ? -17.858 -10.201 2.824  1.00 23.40  ? 65  ARG B NH2  1 
ATOM   3984 H  H    . ARG B 1 65  ? -15.089 -16.272 2.775  1.00 16.77  ? 65  ARG B H    1 
ATOM   3985 H  HA   . ARG B 1 65  ? -17.414 -15.261 2.005  1.00 26.43  ? 65  ARG B HA   1 
ATOM   3986 H  HB2  . ARG B 1 65  ? -15.463 -14.036 1.686  1.00 20.14  ? 65  ARG B HB2  1 
ATOM   3987 H  HB3  . ARG B 1 65  ? -14.964 -15.057 0.579  1.00 20.14  ? 65  ARG B HB3  1 
ATOM   3988 H  HG2  . ARG B 1 65  ? -15.800 -13.165 -0.502 1.00 21.57  ? 65  ARG B HG2  1 
ATOM   3989 H  HG3  . ARG B 1 65  ? -16.743 -14.385 -0.847 1.00 21.57  ? 65  ARG B HG3  1 
ATOM   3990 H  HD2  . ARG B 1 65  ? -18.088 -12.555 -0.413 1.00 26.43  ? 65  ARG B HD2  1 
ATOM   3991 H  HD3  . ARG B 1 65  ? -18.330 -13.609 0.736  1.00 26.43  ? 65  ARG B HD3  1 
ATOM   3992 H  HE   . ARG B 1 65  ? -16.567 -11.848 1.621  1.00 26.45  ? 65  ARG B HE   1 
ATOM   3993 H  HH11 . ARG B 1 65  ? -19.882 -11.867 1.186  1.00 26.43  ? 65  ARG B HH11 1 
ATOM   3994 H  HH12 . ARG B 1 65  ? -20.124 -10.559 1.935  1.00 26.43  ? 65  ARG B HH12 1 
ATOM   3995 H  HH21 . ARG B 1 65  ? -17.086 -9.802  2.691  1.00 26.45  ? 65  ARG B HH21 1 
ATOM   3996 H  HH22 . ARG B 1 65  ? -18.350 -9.993  3.522  1.00 26.45  ? 65  ARG B HH22 1 
ATOM   3997 N  N    . GLU B 1 66  ? -16.515 -17.626 -0.000 1.00 16.33  ? 66  GLU B N    1 
ATOM   3998 C  CA   . GLU B 1 66  ? -17.010 -18.473 -1.073 1.00 17.34  ? 66  GLU B CA   1 
ATOM   3999 C  C    . GLU B 1 66  ? -18.279 -19.225 -0.638 1.00 16.05  ? 66  GLU B C    1 
ATOM   4000 O  O    . GLU B 1 66  ? -19.192 -19.446 -1.440 1.00 17.34  ? 66  GLU B O    1 
ATOM   4001 C  CB   . GLU B 1 66  ? -15.879 -19.425 -1.475 1.00 21.67  ? 66  GLU B CB   1 
ATOM   4002 C  CG   . GLU B 1 66  ? -14.460 -18.809 -1.464 1.00 31.23  ? 66  GLU B CG   1 
ATOM   4003 C  CD   . GLU B 1 66  ? -13.582 -18.797 -0.195 1.00 31.07  ? 66  GLU B CD   1 
ATOM   4004 O  OE1  . GLU B 1 66  ? -12.783 -19.840 0.024  1.00 32.81  ? 66  GLU B OE1  1 
ATOM   4005 O  OE2  . GLU B 1 66  ? -13.577 -17.713 0.552  1.00 20.25  ? 66  GLU B OE2  1 
ATOM   4006 H  H    . GLU B 1 66  ? -15.698 -17.795 0.370  1.00 19.17  ? 66  GLU B H    1 
ATOM   4007 H  HA   . GLU B 1 66  ? -17.232 -17.900 -1.843 1.00 20.73  ? 66  GLU B HA   1 
ATOM   4008 H  HB2  . GLU B 1 66  ? -15.892 -20.191 -0.866 1.00 42.66  ? 66  GLU B HB2  1 
ATOM   4009 H  HB3  . GLU B 1 66  ? -16.067 -19.762 -2.377 1.00 42.66  ? 66  GLU B HB3  1 
ATOM   4010 H  HG2  . GLU B 1 66  ? -13.940 -19.264 -2.161 1.00 31.55  ? 66  GLU B HG2  1 
ATOM   4011 H  HG3  . GLU B 1 66  ? -14.550 -17.879 -1.756 1.00 31.55  ? 66  GLU B HG3  1 
ATOM   4012 N  N    . GLU B 1 67  ? -18.301 -19.662 0.629  1.00 14.46  ? 67  GLU B N    1 
ATOM   4013 C  CA   . GLU B 1 67  ? -19.485 -20.326 1.177  1.00 14.20  ? 67  GLU B CA   1 
ATOM   4014 C  C    . GLU B 1 67  ? -20.645 -19.347 1.289  1.00 13.39  ? 67  GLU B C    1 
ATOM   4015 O  O    . GLU B 1 67  ? -21.783 -19.687 0.974  1.00 14.44  ? 67  GLU B O    1 
ATOM   4016 C  CB   . GLU B 1 67  ? -19.152 -20.930 2.536  1.00 13.98  ? 67  GLU B CB   1 
ATOM   4017 C  CG   . GLU B 1 67  ? -18.235 -22.134 2.432  1.00 15.14  ? 67  GLU B CG   1 
ATOM   4018 C  CD   . GLU B 1 67  ? -17.572 -22.550 3.736  1.00 14.24  ? 67  GLU B CD   1 
ATOM   4019 O  OE1  . GLU B 1 67  ? -17.460 -21.743 4.691  1.00 13.49  ? 67  GLU B OE1  1 
ATOM   4020 O  OE2  . GLU B 1 67  ? -17.063 -23.706 3.756  1.00 15.48  ? 67  GLU B OE2  1 
ATOM   4021 H  H    . GLU B 1 67  ? -17.566 -19.554 1.162  1.00 17.15  ? 67  GLU B H    1 
ATOM   4022 H  HA   . GLU B 1 67  ? -19.744 -21.052 0.564  1.00 16.79  ? 67  GLU B HA   1 
ATOM   4023 H  HB2  . GLU B 1 67  ? -18.725 -20.245 3.090  1.00 17.15  ? 67  GLU B HB2  1 
ATOM   4024 H  HB3  . GLU B 1 67  ? -19.986 -21.200 2.976  1.00 17.15  ? 67  GLU B HB3  1 
ATOM   4025 H  HG2  . GLU B 1 67  ? -18.750 -22.895 2.091  1.00 17.61  ? 67  GLU B HG2  1 
ATOM   4026 H  HG3  . GLU B 1 67  ? -17.531 -21.940 1.777  1.00 17.61  ? 67  GLU B HG3  1 
ATOM   4027 N  N    . LYS B 1 68  ? -20.347 -18.141 1.773  1.00 13.08  ? 68  LYS B N    1 
ATOM   4028 C  CA   . LYS B 1 68  ? -21.375 -17.117 1.885  1.00 13.52  ? 68  LYS B CA   1 
ATOM   4029 C  C    . LYS B 1 68  ? -22.049 -16.886 0.537  1.00 13.97  ? 68  LYS B C    1 
ATOM   4030 O  O    . LYS B 1 68  ? -23.267 -16.762 0.438  1.00 14.54  ? 68  LYS B O    1 
ATOM   4031 C  CB   . LYS B 1 68  ? -20.761 -15.822 2.412  1.00 14.42  ? 68  LYS B CB   1 
ATOM   4032 C  CG   . LYS B 1 68  ? -21.764 -14.711 2.659  1.00 16.69  ? 68  LYS B CG   1 
ATOM   4033 C  CD   . LYS B 1 68  ? -22.937 -15.145 3.493  1.00 19.39  ? 68  LYS B CD   1 
ATOM   4034 C  CE   . LYS B 1 68  ? -23.818 -13.997 3.933  1.00 19.80  ? 68  LYS B CE   1 
ATOM   4035 N  NZ   . LYS B 1 68  ? -23.059 -12.958 4.666  1.00 19.98  ? 68  LYS B NZ   1 
ATOM   4036 H  H    . LYS B 1 68  ? -19.496 -17.951 2.045  1.00 17.28  ? 68  LYS B H    1 
ATOM   4037 H  HA   . LYS B 1 68  ? -22.052 -17.434 2.525  1.00 22.45  ? 68  LYS B HA   1 
ATOM   4038 H  HB2  . LYS B 1 68  ? -20.295 -16.015 3.251  1.00 18.42  ? 68  LYS B HB2  1 
ATOM   4039 H  HB3  . LYS B 1 68  ? -20.097 -15.505 1.766  1.00 18.42  ? 68  LYS B HB3  1 
ATOM   4040 H  HG2  . LYS B 1 68  ? -21.306 -13.971 3.110  1.00 23.07  ? 68  LYS B HG2  1 
ATOM   4041 H  HG3  . LYS B 1 68  ? -22.091 -14.380 1.795  1.00 23.07  ? 68  LYS B HG3  1 
ATOM   4042 H  HD2  . LYS B 1 68  ? -23.482 -15.775 2.975  1.00 22.45  ? 68  LYS B HD2  1 
ATOM   4043 H  HD3  . LYS B 1 68  ? -22.607 -15.616 4.287  1.00 22.45  ? 68  LYS B HD3  1 
ATOM   4044 H  HE2  . LYS B 1 68  ? -24.236 -13.589 3.151  1.00 28.30  ? 68  LYS B HE2  1 
ATOM   4045 H  HE3  . LYS B 1 68  ? -24.527 -14.335 4.511  1.00 28.30  ? 68  LYS B HE3  1 
ATOM   4046 H  HZ1  . LYS B 1 68  ? -22.390 -13.343 5.143  1.00 23.07  ? 68  LYS B HZ1  1 
ATOM   4047 H  HZ2  . LYS B 1 68  ? -22.704 -12.365 4.079  1.00 23.07  ? 68  LYS B HZ2  1 
ATOM   4048 H  HZ3  . LYS B 1 68  ? -23.612 -12.518 5.234  1.00 23.07  ? 68  LYS B HZ3  1 
ATOM   4049 N  N    . ASP B 1 69  ? -21.227 -16.785 -0.508 1.00 13.63  ? 69  ASP B N    1 
ATOM   4050 C  CA   . ASP B 1 69  ? -21.805 -16.528 -1.821 1.00 15.01  ? 69  ASP B CA   1 
ATOM   4051 C  C    . ASP B 1 69  ? -22.736 -17.655 -2.270 1.00 15.13  ? 69  ASP B C    1 
ATOM   4052 O  O    . ASP B 1 69  ? -23.795 -17.397 -2.863 1.00 16.38  ? 69  ASP B O    1 
ATOM   4053 C  CB   . ASP B 1 69  ? -20.681 -16.198 -2.791 1.00 17.15  ? 69  ASP B CB   1 
ATOM   4054 C  CG   . ASP B 1 69  ? -20.175 -14.768 -2.640 1.00 17.83  ? 69  ASP B CG   1 
ATOM   4055 O  OD1  . ASP B 1 69  ? -21.035 -13.838 -2.416 1.00 21.68  ? 69  ASP B OD1  1 
ATOM   4056 O  OD2  . ASP B 1 69  ? -19.030 -14.533 -2.941 1.00 21.26  ? 69  ASP B OD2  1 
ATOM   4057 H  H    . ASP B 1 69  ? -20.322 -16.866 -0.411 1.00 20.12  ? 69  ASP B H    1 
ATOM   4058 H  HA   . ASP B 1 69  ? -22.357 -15.715 -1.739 1.00 18.16  ? 69  ASP B HA   1 
ATOM   4059 H  HB2  . ASP B 1 69  ? -19.932 -16.810 -2.640 1.00 20.12  ? 69  ASP B HB2  1 
ATOM   4060 H  HB3  . ASP B 1 69  ? -20.998 -16.324 -3.708 1.00 20.12  ? 69  ASP B HB3  1 
ATOM   4061 N  N    . ARG B 1 70  ? -22.385 -18.910 -1.968 1.00 15.33  ? 70  ARG B N    1 
ATOM   4062 C  CA   . ARG B 1 70  ? -23.262 -20.029 -2.284 1.00 16.20  ? 70  ARG B CA   1 
ATOM   4063 C  C    . ARG B 1 70  ? -24.575 -19.946 -1.502 1.00 15.87  ? 70  ARG B C    1 
ATOM   4064 O  O    . ARG B 1 70  ? -25.642 -20.199 -2.062 1.00 16.78  ? 70  ARG B O    1 
ATOM   4065 C  CB   . ARG B 1 70  ? -22.576 -21.370 -1.999 1.00 19.09  ? 70  ARG B CB   1 
ATOM   4066 C  CG   . ARG B 1 70  ? -21.507 -21.752 -3.010 1.00 22.78  ? 70  ARG B CG   1 
ATOM   4067 C  CD   . ARG B 1 70  ? -20.409 -22.771 -2.648 1.00 31.27  ? 70  ARG B CD   1 
ATOM   4068 N  NE   . ARG B 1 70  ? -20.573 -23.649 -1.492 1.00 38.55  ? 70  ARG B NE   1 
ATOM   4069 C  CZ   . ARG B 1 70  ? -19.587 -24.058 -0.677 1.00 37.65  ? 70  ARG B CZ   1 
ATOM   4070 N  NH1  . ARG B 1 70  ? -18.332 -23.713 -0.937 1.00 34.82  ? 70  ARG B NH1  1 
ATOM   4071 N  NH2  . ARG B 1 70  ? -19.849 -24.826 0.384  1.00 30.52  ? 70  ARG B NH2  1 
ATOM   4072 H  H    . ARG B 1 70  ? -21.582 -19.074 -1.564 1.00 22.30  ? 70  ARG B H    1 
ATOM   4073 H  HA   . ARG B 1 70  ? -23.473 -19.988 -3.245 1.00 26.98  ? 70  ARG B HA   1 
ATOM   4074 H  HB2  . ARG B 1 70  ? -22.167 -21.329 -1.109 1.00 22.30  ? 70  ARG B HB2  1 
ATOM   4075 H  HB3  . ARG B 1 70  ? -23.259 -22.073 -1.983 1.00 22.30  ? 70  ARG B HB3  1 
ATOM   4076 H  HG2  . ARG B 1 70  ? -21.966 -22.093 -3.807 1.00 26.25  ? 70  ARG B HG2  1 
ATOM   4077 H  HG3  . ARG B 1 70  ? -21.055 -20.926 -3.285 1.00 26.25  ? 70  ARG B HG3  1 
ATOM   4078 H  HD2  . ARG B 1 70  ? -20.270 -23.343 -3.433 1.00 32.60  ? 70  ARG B HD2  1 
ATOM   4079 H  HD3  . ARG B 1 70  ? -19.576 -22.268 -2.522 1.00 32.60  ? 70  ARG B HD3  1 
ATOM   4080 H  HE   . ARG B 1 70  ? -21.376 -23.932 -1.318 1.00 42.85  ? 70  ARG B HE   1 
ATOM   4081 H  HH11 . ARG B 1 70  ? -17.967 -23.935 -1.708 1.00 32.61  ? 70  ARG B HH11 1 
ATOM   4082 H  HH12 . ARG B 1 70  ? -17.867 -23.265 -0.338 1.00 32.61  ? 70  ARG B HH12 1 
ATOM   4083 H  HH21 . ARG B 1 70  ? -20.676 -24.915 0.667  1.00 42.35  ? 70  ARG B HH21 1 
ATOM   4084 H  HH22 . ARG B 1 70  ? -19.193 -25.240 0.797  1.00 42.33  ? 70  ARG B HH22 1 
ATOM   4085 N  N    . LEU B 1 71  ? -24.503 -19.592 -0.219 1.00 15.05  ? 71  LEU B N    1 
ATOM   4086 C  CA   . LEU B 1 71  ? -25.701 -19.475 0.610  1.00 15.36  ? 71  LEU B CA   1 
ATOM   4087 C  C    . LEU B 1 71  ? -26.623 -18.365 0.101  1.00 14.35  ? 71  LEU B C    1 
ATOM   4088 O  O    . LEU B 1 71  ? -27.828 -18.555 0.005  1.00 15.42  ? 71  LEU B O    1 
ATOM   4089 C  CB   . LEU B 1 71  ? -25.262 -19.225 2.057  1.00 14.74  ? 71  LEU B CB   1 
ATOM   4090 C  CG   . LEU B 1 71  ? -24.590 -20.428 2.707  1.00 15.49  ? 71  LEU B CG   1 
ATOM   4091 C  CD1  . LEU B 1 71  ? -23.771 -19.991 3.904  1.00 17.70  ? 71  LEU B CD1  1 
ATOM   4092 C  CD2  . LEU B 1 71  ? -25.615 -21.469 3.100  1.00 18.17  ? 71  LEU B CD2  1 
ATOM   4093 H  H    . LEU B 1 71  ? -23.687 -19.422 0.157  1.00 20.05  ? 71  LEU B H    1 
ATOM   4094 H  HA   . LEU B 1 71  ? -26.190 -20.329 0.563  1.00 20.05  ? 71  LEU B HA   1 
ATOM   4095 H  HB2  . LEU B 1 71  ? -24.641 -18.469 2.070  1.00 20.05  ? 71  LEU B HB2  1 
ATOM   4096 H  HB3  . LEU B 1 71  ? -26.047 -18.978 2.585  1.00 20.05  ? 71  LEU B HB3  1 
ATOM   4097 H  HG   . LEU B 1 71  ? -23.977 -20.834 2.046  1.00 20.05  ? 71  LEU B HG   1 
ATOM   4098 H  HD11 . LEU B 1 71  ? -23.341 -20.766 4.303  1.00 20.05  ? 71  LEU B HD11 1 
ATOM   4099 H  HD12 . LEU B 1 71  ? -23.093 -19.355 3.619  1.00 20.05  ? 71  LEU B HD12 1 
ATOM   4100 H  HD13 . LEU B 1 71  ? -24.354 -19.570 4.560  1.00 20.05  ? 71  LEU B HD13 1 
ATOM   4101 H  HD21 . LEU B 1 71  ? -25.178 -22.182 3.598  1.00 20.05  ? 71  LEU B HD21 1 
ATOM   4102 H  HD22 . LEU B 1 71  ? -26.299 -21.058 3.657  1.00 20.05  ? 71  LEU B HD22 1 
ATOM   4103 H  HD23 . LEU B 1 71  ? -26.027 -21.839 2.300  1.00 20.05  ? 71  LEU B HD23 1 
ATOM   4104 N  N    . VAL B 1 72  ? -26.041 -17.210 -0.238 1.00 13.54  ? 72  VAL B N    1 
ATOM   4105 C  CA   . VAL B 1 72  ? -26.830 -16.091 -0.737 1.00 13.25  ? 72  VAL B CA   1 
ATOM   4106 C  C    . VAL B 1 72  ? -27.601 -16.491 -1.989 1.00 13.58  ? 72  VAL B C    1 
ATOM   4107 O  O    . VAL B 1 72  ? -28.753 -16.101 -2.189 1.00 14.51  ? 72  VAL B O    1 
ATOM   4108 C  CB   . VAL B 1 72  ? -25.944 -14.857 -0.980 1.00 14.42  ? 72  VAL B CB   1 
ATOM   4109 C  CG1  . VAL B 1 72  ? -26.676 -13.764 -1.756 1.00 15.97  ? 72  VAL B CG1  1 
ATOM   4110 C  CG2  . VAL B 1 72  ? -25.442 -14.313 0.346  1.00 15.86  ? 72  VAL B CG2  1 
ATOM   4111 H  H    . VAL B 1 72  ? -25.135 -17.116 -0.157 1.00 18.96  ? 72  VAL B H    1 
ATOM   4112 H  HA   . VAL B 1 72  ? -27.481 -15.860 -0.050 1.00 15.99  ? 72  VAL B HA   1 
ATOM   4113 H  HB   . VAL B 1 72  ? -25.162 -15.144 -1.513 1.00 18.96  ? 72  VAL B HB   1 
ATOM   4114 H  HG11 . VAL B 1 72  ? -26.236 -12.909 -1.605 1.00 19.13  ? 72  VAL B HG11 1 
ATOM   4115 H  HG12 . VAL B 1 72  ? -26.659 -13.972 -2.707 1.00 19.13  ? 72  VAL B HG12 1 
ATOM   4116 H  HG13 . VAL B 1 72  ? -27.599 -13.710 -1.452 1.00 19.13  ? 72  VAL B HG13 1 
ATOM   4117 H  HG21 . VAL B 1 72  ? -24.745 -13.654 0.184  1.00 18.96  ? 72  VAL B HG21 1 
ATOM   4118 H  HG22 . VAL B 1 72  ? -26.179 -13.894 0.824  1.00 18.96  ? 72  VAL B HG22 1 
ATOM   4119 H  HG23 . VAL B 1 72  ? -25.082 -15.039 0.883  1.00 18.96  ? 72  VAL B HG23 1 
ATOM   4120 N  N    . ALA B 1 73  ? -26.962 -17.286 -2.852 1.00 14.80  ? 73  ALA B N    1 
ATOM   4121 C  CA   . ALA B 1 73  ? -27.591 -17.651 -4.112 1.00 16.36  ? 73  ALA B CA   1 
ATOM   4122 C  C    . ALA B 1 73  ? -28.794 -18.575 -3.902 1.00 17.31  ? 73  ALA B C    1 
ATOM   4123 O  O    . ALA B 1 73  ? -29.741 -18.581 -4.700 1.00 21.91  ? 73  ALA B O    1 
ATOM   4124 C  CB   . ALA B 1 73  ? -26.560 -18.268 -5.011 1.00 18.47  ? 73  ALA B CB   1 
ATOM   4125 H  H    . ALA B 1 73  ? -26.125 -17.600 -2.662 1.00 20.29  ? 73  ALA B H    1 
ATOM   4126 H  HA   . ALA B 1 73  ? -27.916 -16.825 -4.540 1.00 18.02  ? 73  ALA B HA   1 
ATOM   4127 H  HB1  . ALA B 1 73  ? -26.967 -18.501 -5.861 1.00 20.63  ? 73  ALA B HB1  1 
ATOM   4128 H  HB2  . ALA B 1 73  ? -25.839 -17.633 -5.162 1.00 20.63  ? 73  ALA B HB2  1 
ATOM   4129 H  HB3  . ALA B 1 73  ? -26.202 -19.069 -4.593 1.00 20.63  ? 73  ALA B HB3  1 
ATOM   4130 N  N    . LYS B 1 74  ? -28.741 -19.407 -2.858 1.00 17.09  ? 74  LYS B N    1 
ATOM   4131 C  CA   . LYS B 1 74  ? -29.670 -20.522 -2.756 1.00 18.09  ? 74  LYS B CA   1 
ATOM   4132 C  C    . LYS B 1 74  ? -30.709 -20.394 -1.639 1.00 17.29  ? 74  LYS B C    1 
ATOM   4133 O  O    . LYS B 1 74  ? -31.778 -20.996 -1.724 1.00 19.53  ? 74  LYS B O    1 
ATOM   4134 C  CB   . LYS B 1 74  ? -28.914 -21.826 -2.491 1.00 21.16  ? 74  LYS B CB   1 
ATOM   4135 C  CG   . LYS B 1 74  ? -28.951 -22.857 -3.593 1.00 27.99  ? 74  LYS B CG   1 
ATOM   4136 C  CD   . LYS B 1 74  ? -28.285 -24.165 -3.219 1.00 27.56  ? 74  LYS B CD   1 
ATOM   4137 C  CE   . LYS B 1 74  ? -29.049 -25.335 -3.796 1.00 29.74  ? 74  LYS B CE   1 
ATOM   4138 N  NZ   . LYS B 1 74  ? -28.420 -26.627 -3.453 1.00 30.74  ? 74  LYS B NZ   1 
ATOM   4139 H  H    . LYS B 1 74  ? -28.114 -19.288 -2.205 1.00 41.59  ? 74  LYS B H    1 
ATOM   4140 H  HA   . LYS B 1 74  ? -30.147 -20.608 -3.613 1.00 26.42  ? 74  LYS B HA   1 
ATOM   4141 H  HB2  . LYS B 1 74  ? -27.976 -21.606 -2.311 1.00 42.77  ? 74  LYS B HB2  1 
ATOM   4142 H  HB3  . LYS B 1 74  ? -29.280 -22.235 -1.678 1.00 42.82  ? 74  LYS B HB3  1 
ATOM   4143 H  HG2  . LYS B 1 74  ? -29.887 -23.030 -3.831 1.00 28.03  ? 74  LYS B HG2  1 
ATOM   4144 H  HG3  . LYS B 1 74  ? -28.505 -22.488 -4.385 1.00 28.03  ? 74  LYS B HG3  1 
ATOM   4145 H  HD2  . LYS B 1 74  ? -27.367 -24.174 -3.564 1.00 44.90  ? 74  LYS B HD2  1 
ATOM   4146 H  HD3  . LYS B 1 74  ? -28.250 -24.249 -2.243 1.00 44.82  ? 74  LYS B HD3  1 
ATOM   4147 H  HE2  . LYS B 1 74  ? -29.961 -25.327 -3.456 1.00 28.03  ? 74  LYS B HE2  1 
ATOM   4148 H  HE3  . LYS B 1 74  ? -29.089 -25.251 -4.767 1.00 28.03  ? 74  LYS B HE3  1 
ATOM   4149 H  HZ1  . LYS B 1 74  ? -28.948 -27.310 -3.730 1.00 29.13  ? 74  LYS B HZ1  1 
ATOM   4150 H  HZ2  . LYS B 1 74  ? -27.611 -26.693 -3.859 1.00 29.13  ? 74  LYS B HZ2  1 
ATOM   4151 H  HZ3  . LYS B 1 74  ? -28.306 -26.684 -2.555 1.00 29.13  ? 74  LYS B HZ3  1 
ATOM   4152 N  N    . GLN B 1 75  ? -30.400 -19.679 -0.557 1.00 15.78  ? 75  GLN B N    1 
ATOM   4153 C  CA   . GLN B 1 75  ? -31.228 -19.748 0.645  1.00 15.28  ? 75  GLN B CA   1 
ATOM   4154 C  C    . GLN B 1 75  ? -32.551 -19.014 0.466  1.00 16.53  ? 75  GLN B C    1 
ATOM   4155 O  O    . GLN B 1 75  ? -32.583 -17.970 -0.187 1.00 19.35  ? 75  GLN B O    1 
ATOM   4156 C  CB   . GLN B 1 75  ? -30.442 -19.207 1.839  1.00 16.01  ? 75  GLN B CB   1 
ATOM   4157 C  CG   . GLN B 1 75  ? -30.257 -17.696 1.785  1.00 18.70  ? 75  GLN B CG   1 
ATOM   4158 C  CD   . GLN B 1 75  ? -29.142 -17.243 2.695  1.00 20.87  ? 75  GLN B CD   1 
ATOM   4159 O  OE1  . GLN B 1 75  ? -28.583 -18.012 3.481  1.00 22.59  ? 75  GLN B OE1  1 
ATOM   4160 N  NE2  . GLN B 1 75  ? -28.775 -15.985 2.549  1.00 25.49  ? 75  GLN B NE2  1 
ATOM   4161 H  H    . GLN B 1 75  ? -29.661 -19.141 -0.559 1.00 40.52  ? 75  GLN B H    1 
ATOM   4162 H  HA   . GLN B 1 75  ? -31.424 -20.696 0.814  1.00 16.76  ? 75  GLN B HA   1 
ATOM   4163 H  HB2  . GLN B 1 75  ? -30.917 -19.445 2.663  1.00 19.93  ? 75  GLN B HB2  1 
ATOM   4164 H  HB3  . GLN B 1 75  ? -29.565 -19.642 1.859  1.00 19.93  ? 75  GLN B HB3  1 
ATOM   4165 H  HG2  . GLN B 1 75  ? -30.055 -17.423 0.865  1.00 39.52  ? 75  GLN B HG2  1 
ATOM   4166 H  HG3  . GLN B 1 75  ? -31.091 -17.256 2.055  1.00 39.50  ? 75  GLN B HG3  1 
ATOM   4167 H  HE21 . GLN B 1 75  ? -29.205 -15.460 1.983  1.00 27.04  ? 75  GLN B HE21 1 
ATOM   4168 H  HE22 . GLN B 1 75  ? -28.097 -15.666 3.018  1.00 27.04  ? 75  GLN B HE22 1 
ATOM   4169 N  N    . PRO B 1 76  ? -33.649 -19.544 1.035  1.00 15.82  ? 76  PRO B N    1 
ATOM   4170 C  CA   . PRO B 1 76  ? -34.940 -18.855 0.988  1.00 16.74  ? 76  PRO B CA   1 
ATOM   4171 C  C    . PRO B 1 76  ? -35.019 -17.810 2.095  1.00 17.36  ? 76  PRO B C    1 
ATOM   4172 O  O    . PRO B 1 76  ? -34.232 -17.818 3.041  1.00 19.68  ? 76  PRO B O    1 
ATOM   4173 C  CB   . PRO B 1 76  ? -35.944 -19.985 1.245  1.00 16.04  ? 76  PRO B CB   1 
ATOM   4174 C  CG   . PRO B 1 76  ? -35.186 -20.893 2.196  1.00 15.08  ? 76  PRO B CG   1 
ATOM   4175 C  CD   . PRO B 1 76  ? -33.742 -20.843 1.712  1.00 14.83  ? 76  PRO B CD   1 
ATOM   4176 H  HA   . PRO B 1 76  ? -35.090 -18.451 0.096  1.00 26.44  ? 76  PRO B HA   1 
ATOM   4177 H  HB2  . PRO B 1 76  ? -36.766 -19.645 1.659  1.00 19.33  ? 76  PRO B HB2  1 
ATOM   4178 H  HB3  . PRO B 1 76  ? -36.171 -20.454 0.414  1.00 19.33  ? 76  PRO B HB3  1 
ATOM   4179 H  HG2  . PRO B 1 76  ? -35.254 -20.564 3.113  1.00 15.79  ? 76  PRO B HG2  1 
ATOM   4180 H  HG3  . PRO B 1 76  ? -35.535 -21.807 2.161  1.00 15.79  ? 76  PRO B HG3  1 
ATOM   4181 H  HD2  . PRO B 1 76  ? -33.120 -20.891 2.462  1.00 16.28  ? 76  PRO B HD2  1 
ATOM   4182 H  HD3  . PRO B 1 76  ? -33.553 -21.573 1.095  1.00 16.29  ? 76  PRO B HD3  1 
ATOM   4183 N  N    . SER B 1 77  ? -36.030 -16.951 1.992  1.00 19.17  ? 77  SER B N    1 
ATOM   4184 C  CA   . SER B 1 77  ? -36.373 -15.993 3.028  1.00 21.13  ? 77  SER B CA   1 
ATOM   4185 C  C    . SER B 1 77  ? -37.184 -16.665 4.134  1.00 18.15  ? 77  SER B C    1 
ATOM   4186 O  O    . SER B 1 77  ? -37.912 -17.621 3.914  1.00 18.06  ? 77  SER B O    1 
ATOM   4187 C  CB   . SER B 1 77  ? -37.181 -14.852 2.439  1.00 24.09  ? 77  SER B CB   1 
ATOM   4188 O  OG   . SER B 1 77  ? -36.508 -14.295 1.323  1.00 31.80  ? 77  SER B OG   1 
ATOM   4189 H  H    . SER B 1 77  ? -36.537 -16.965 1.232  1.00 26.44  ? 77  SER B H    1 
ATOM   4190 H  HA   . SER B 1 77  ? -35.533 -15.629 3.417  1.00 23.25  ? 77  SER B HA   1 
ATOM   4191 H  HB2  . SER B 1 77  ? -38.064 -15.185 2.158  1.00 27.48  ? 77  SER B HB2  1 
ATOM   4192 H  HB3  . SER B 1 77  ? -37.316 -14.158 3.123  1.00 27.48  ? 77  SER B HB3  1 
ATOM   4193 H  HG   . SER B 1 77  ? -36.833 -13.530 1.168  1.00 31.77  ? 77  SER B HG   1 
ATOM   4194 N  N    . LEU B 1 78  ? -37.070 -16.096 5.332  1.00 19.10  ? 78  LEU B N    1 
ATOM   4195 C  CA   . LEU B 1 78  ? -38.004 -16.376 6.416  1.00 18.79  ? 78  LEU B CA   1 
ATOM   4196 C  C    . LEU B 1 78  ? -39.347 -15.752 6.050  1.00 19.78  ? 78  LEU B C    1 
ATOM   4197 O  O    . LEU B 1 78  ? -39.388 -14.776 5.295  1.00 21.16  ? 78  LEU B O    1 
ATOM   4198 C  CB   . LEU B 1 78  ? -37.465 -15.803 7.723  1.00 20.58  ? 78  LEU B CB   1 
ATOM   4199 C  CG   . LEU B 1 78  ? -36.181 -16.506 8.158  1.00 22.15  ? 78  LEU B CG   1 
ATOM   4200 C  CD1  . LEU B 1 78  ? -35.419 -15.651 9.144  1.00 28.03  ? 78  LEU B CD1  1 
ATOM   4201 C  CD2  . LEU B 1 78  ? -36.471 -17.876 8.739  1.00 20.63  ? 78  LEU B CD2  1 
ATOM   4202 H  H    . LEU B 1 78  ? -36.389 -15.506 5.483  1.00 23.24  ? 78  LEU B H    1 
ATOM   4203 H  HA   . LEU B 1 78  ? -38.113 -17.351 6.497  1.00 23.16  ? 78  LEU B HA   1 
ATOM   4204 H  HB2  . LEU B 1 78  ? -37.288 -14.849 7.605  1.00 23.19  ? 78  LEU B HB2  1 
ATOM   4205 H  HB3  . LEU B 1 78  ? -38.142 -15.907 8.421  1.00 23.19  ? 78  LEU B HB3  1 
ATOM   4206 H  HG   . LEU B 1 78  ? -35.611 -16.629 7.360  1.00 23.25  ? 78  LEU B HG   1 
ATOM   4207 H  HD11 . LEU B 1 78  ? -34.579 -16.086 9.369  1.00 23.21  ? 78  LEU B HD11 1 
ATOM   4208 H  HD12 . LEU B 1 78  ? -35.238 -14.782 8.747  1.00 23.21  ? 78  LEU B HD12 1 
ATOM   4209 H  HD13 . LEU B 1 78  ? -35.951 -15.535 9.950  1.00 23.21  ? 78  LEU B HD13 1 
ATOM   4210 H  HD21 . LEU B 1 78  ? -35.650 -18.258 9.093  1.00 23.16  ? 78  LEU B HD21 1 
ATOM   4211 H  HD22 . LEU B 1 78  ? -37.125 -17.794 9.454  1.00 23.16  ? 78  LEU B HD22 1 
ATOM   4212 H  HD23 . LEU B 1 78  ? -36.824 -18.456 8.043  1.00 23.16  ? 78  LEU B HD23 1 
ATOM   4213 N  N    . GLY B 1 79  ? -40.449 -16.347 6.525  1.00 18.55  ? 79  GLY B N    1 
ATOM   4214 C  CA   . GLY B 1 79  ? -41.766 -15.737 6.386  1.00 19.63  ? 79  GLY B CA   1 
ATOM   4215 C  C    . GLY B 1 79  ? -42.473 -16.098 5.084  1.00 20.72  ? 79  GLY B C    1 
ATOM   4216 O  O    . GLY B 1 79  ? -43.476 -15.478 4.777  1.00 23.27  ? 79  GLY B O    1 
ATOM   4217 H  H    . GLY B 1 79  ? -40.379 -17.155 6.947  1.00 23.16  ? 79  GLY B H    1 
ATOM   4218 H  HA2  . GLY B 1 79  ? -42.329 -16.023 7.148  1.00 33.85  ? 79  GLY B HA2  1 
ATOM   4219 H  HA3  . GLY B 1 79  ? -41.670 -14.753 6.439  1.00 33.85  ? 79  GLY B HA3  1 
ATOM   4220 N  N    . ARG B 1 80  ? -42.013 -17.112 4.341  1.00 20.30  ? 80  ARG B N    1 
ATOM   4221 C  CA   . ARG B 1 80  ? -42.718 -17.468 3.109  1.00 26.38  ? 80  ARG B CA   1 
ATOM   4222 C  C    . ARG B 1 80  ? -44.149 -17.903 3.418  1.00 58.37  ? 80  ARG B C    1 
ATOM   4223 O  O    . ARG B 1 80  ? -44.340 -18.677 4.335  1.00 30.19  ? 80  ARG B O    1 
ATOM   4224 C  CB   . ARG B 1 80  ? -42.013 -18.639 2.432  1.00 19.37  ? 80  ARG B CB   1 
ATOM   4225 C  CG   . ARG B 1 80  ? -40.641 -18.288 1.892  1.00 18.35  ? 80  ARG B CG   1 
ATOM   4226 C  CD   . ARG B 1 80  ? -39.882 -19.492 1.371  1.00 17.55  ? 80  ARG B CD   1 
ATOM   4227 N  NE   . ARG B 1 80  ? -39.559 -20.389 2.476  1.00 16.13  ? 80  ARG B NE   1 
ATOM   4228 C  CZ   . ARG B 1 80  ? -38.966 -21.579 2.353  1.00 15.00  ? 80  ARG B CZ   1 
ATOM   4229 N  NH1  . ARG B 1 80  ? -38.653 -22.091 1.177  1.00 15.54  ? 80  ARG B NH1  1 
ATOM   4230 N  NH2  . ARG B 1 80  ? -38.691 -22.283 3.432  1.00 14.28  ? 80  ARG B NH2  1 
ATOM   4231 H  H    . ARG B 1 80  ? -41.275 -17.586 4.596  1.00 19.53  ? 80  ARG B H    1 
ATOM   4232 H  HA   . ARG B 1 80  ? -42.729 -16.691 2.504  1.00 26.60  ? 80  ARG B HA   1 
ATOM   4233 H  HB2  . ARG B 1 80  ? -41.925 -19.369 3.080  1.00 19.52  ? 80  ARG B HB2  1 
ATOM   4234 H  HB3  . ARG B 1 80  ? -42.572 -18.958 1.693  1.00 19.52  ? 80  ARG B HB3  1 
ATOM   4235 H  HG2  . ARG B 1 80  ? -40.739 -17.637 1.164  1.00 19.53  ? 80  ARG B HG2  1 
ATOM   4236 H  HG3  . ARG B 1 80  ? -40.114 -17.865 2.602  1.00 19.53  ? 80  ARG B HG3  1 
ATOM   4237 H  HD2  . ARG B 1 80  ? -40.429 -19.967 0.710  1.00 19.28  ? 80  ARG B HD2  1 
ATOM   4238 H  HD3  . ARG B 1 80  ? -39.056 -19.198 0.933  1.00 19.28  ? 80  ARG B HD3  1 
ATOM   4239 H  HE   . ARG B 1 80  ? -39.761 -20.125 3.282  1.00 19.52  ? 80  ARG B HE   1 
ATOM   4240 H  HH11 . ARG B 1 80  ? -38.231 -21.599 0.581  1.00 19.36  ? 80  ARG B HH11 1 
ATOM   4241 H  HH12 . ARG B 1 80  ? -38.866 -22.926 0.993  1.00 19.36  ? 80  ARG B HH12 1 
ATOM   4242 H  HH21 . ARG B 1 80  ? -39.065 -22.075 4.200  1.00 19.51  ? 80  ARG B HH21 1 
ATOM   4243 H  HH22 . ARG B 1 80  ? -38.133 -22.962 3.381  1.00 19.51  ? 80  ARG B HH22 1 
ATOM   4244 N  N    . ALA B 1 81  ? -45.135 -17.462 2.622  1.00 58.14  ? 81  ALA B N    1 
ATOM   4245 C  CA   . ALA B 1 81  ? -46.533 -17.880 2.798  1.00 70.35  ? 81  ALA B CA   1 
ATOM   4246 C  C    . ALA B 1 81  ? -46.659 -19.389 3.015  1.00 115.65 ? 81  ALA B C    1 
ATOM   4247 O  O    . ALA B 1 81  ? -47.323 -19.847 3.973  1.00 91.56  ? 81  ALA B O    1 
ATOM   4248 C  CB   . ALA B 1 81  ? -47.363 -17.404 1.629  1.00 78.51  ? 81  ALA B CB   1 
ATOM   4249 H  H    . ALA B 1 81  ? -44.928 -16.893 1.932  1.00 26.60  ? 81  ALA B H    1 
ATOM   4250 H  HA   . ALA B 1 81  ? -46.876 -17.436 3.613  1.00 25.53  ? 81  ALA B HA   1 
ATOM   4251 H  HB1  . ALA B 1 81  ? -48.290 -17.670 1.759  1.00 26.63  ? 81  ALA B HB1  1 
ATOM   4252 H  HB2  . ALA B 1 81  ? -47.312 -16.435 1.568  1.00 26.63  ? 81  ALA B HB2  1 
ATOM   4253 H  HB3  . ALA B 1 81  ? -47.025 -17.798 0.807  1.00 26.63  ? 81  ALA B HB3  1 
ATOM   4254 N  N    . GLU B 1 82  ? -45.999 -20.158 2.133  1.00 75.14  ? 82  GLU B N    1 
ATOM   4255 C  CA   . GLU B 1 82  ? -46.228 -21.593 2.070  1.00 28.70  ? 82  GLU B CA   1 
ATOM   4256 C  C    . GLU B 1 82  ? -45.466 -22.344 3.169  1.00 19.53  ? 82  GLU B C    1 
ATOM   4257 O  O    . GLU B 1 82  ? -45.724 -23.522 3.391  1.00 19.58  ? 82  GLU B O    1 
ATOM   4258 C  CB   . GLU B 1 82  ? -45.898 -22.195 0.696  1.00 22.21  ? 82  GLU B CB   1 
ATOM   4259 C  CG   . GLU B 1 82  ? -44.425 -22.410 0.381  1.00 23.40  ? 82  GLU B CG   1 
ATOM   4260 C  CD   . GLU B 1 82  ? -43.596 -21.197 -0.016 1.00 22.98  ? 82  GLU B CD   1 
ATOM   4261 O  OE1  . GLU B 1 82  ? -44.150 -20.064 -0.114 1.00 25.37  ? 82  GLU B OE1  1 
ATOM   4262 O  OE2  . GLU B 1 82  ? -42.373 -21.398 -0.242 1.00 23.54  ? 82  GLU B OE2  1 
ATOM   4263 H  H    . GLU B 1 82  ? -45.409 -19.775 1.545  1.00 24.36  ? 82  GLU B H    1 
ATOM   4264 H  HA   . GLU B 1 82  ? -47.190 -21.740 2.229  1.00 23.31  ? 82  GLU B HA   1 
ATOM   4265 H  HB2  . GLU B 1 82  ? -46.356 -23.058 0.627  1.00 23.64  ? 82  GLU B HB2  1 
ATOM   4266 H  HB3  . GLU B 1 82  ? -46.278 -21.608 0.010  1.00 23.64  ? 82  GLU B HB3  1 
ATOM   4267 H  HG2  . GLU B 1 82  ? -43.997 -22.819 1.162  1.00 25.20  ? 82  GLU B HG2  1 
ATOM   4268 H  HG3  . GLU B 1 82  ? -44.363 -23.062 -0.349 1.00 25.20  ? 82  GLU B HG3  1 
ATOM   4269 N  N    . ALA B 1 83  ? -44.527 -21.684 3.867  1.00 18.59  ? 83  ALA B N    1 
ATOM   4270 C  CA   . ALA B 1 83  ? -43.700 -22.365 4.854  1.00 17.75  ? 83  ALA B CA   1 
ATOM   4271 C  C    . ALA B 1 83  ? -44.408 -22.320 6.209  1.00 17.86  ? 83  ALA B C    1 
ATOM   4272 O  O    . ALA B 1 83  ? -44.021 -21.600 7.127  1.00 19.38  ? 83  ALA B O    1 
ATOM   4273 C  CB   . ALA B 1 83  ? -42.316 -21.754 4.884  1.00 17.99  ? 83  ALA B CB   1 
ATOM   4274 H  H    . ALA B 1 83  ? -44.392 -20.792 3.720  1.00 21.01  ? 83  ALA B H    1 
ATOM   4275 H  HA   . ALA B 1 83  ? -43.614 -23.309 4.585  1.00 21.20  ? 83  ALA B HA   1 
ATOM   4276 H  HB1  . ALA B 1 83  ? -41.777 -22.202 5.558  1.00 20.98  ? 83  ALA B HB1  1 
ATOM   4277 H  HB2  . ALA B 1 83  ? -41.895 -21.858 4.014  1.00 20.98  ? 83  ALA B HB2  1 
ATOM   4278 H  HB3  . ALA B 1 83  ? -42.382 -20.809 5.100  1.00 20.98  ? 83  ALA B HB3  1 
ATOM   4279 N  N    . THR B 1 84  ? -45.457 -23.135 6.331  1.00 18.07  ? 84  THR B N    1 
ATOM   4280 C  CA   . THR B 1 84  ? -46.310 -23.109 7.502  1.00 17.91  ? 84  THR B CA   1 
ATOM   4281 C  C    . THR B 1 84  ? -45.822 -24.037 8.609  1.00 16.93  ? 84  THR B C    1 
ATOM   4282 O  O    . THR B 1 84  ? -46.412 -24.040 9.686  1.00 19.28  ? 84  THR B O    1 
ATOM   4283 C  CB   . THR B 1 84  ? -47.740 -23.480 7.085  1.00 19.92  ? 84  THR B CB   1 
ATOM   4284 O  OG1  . THR B 1 84  ? -47.693 -24.713 6.364  1.00 22.27  ? 84  THR B OG1  1 
ATOM   4285 C  CG2  . THR B 1 84  ? -48.369 -22.413 6.217  1.00 22.36  ? 84  THR B CG2  1 
ATOM   4286 H  H    . THR B 1 84  ? -45.643 -23.731 5.664  1.00 21.20  ? 84  THR B H    1 
ATOM   4287 H  HA   . THR B 1 84  ? -46.320 -22.190 7.851  1.00 41.52  ? 84  THR B HA   1 
ATOM   4288 H  HB   . THR B 1 84  ? -48.286 -23.599 7.898  1.00 22.46  ? 84  THR B HB   1 
ATOM   4289 H  HG1  . THR B 1 84  ? -48.480 -25.009 6.256  1.00 24.58  ? 84  THR B HG1  1 
ATOM   4290 H  HG21 . THR B 1 84  ? -49.285 -22.666 6.003  1.00 23.71  ? 84  THR B HG21 1 
ATOM   4291 H  HG22 . THR B 1 84  ? -48.371 -21.564 6.695  1.00 23.71  ? 84  THR B HG22 1 
ATOM   4292 H  HG23 . THR B 1 84  ? -47.859 -22.320 5.393  1.00 23.71  ? 84  THR B HG23 1 
ATOM   4293 N  N    . CYS B 1 85  ? -44.788 -24.836 8.328  1.00 15.88  ? 85  CYS B N    1 
ATOM   4294 C  CA   . CYS B 1 85  ? -44.156 -25.641 9.351  1.00 15.78  ? 85  CYS B CA   1 
ATOM   4295 C  C    . CYS B 1 85  ? -42.896 -24.924 9.826  1.00 14.27  ? 85  CYS B C    1 
ATOM   4296 O  O    . CYS B 1 85  ? -42.196 -24.290 9.032  1.00 14.74  ? 85  CYS B O    1 
ATOM   4297 C  CB   . CYS B 1 85  ? -43.770 -27.019 8.834  1.00 16.02  ? 85  CYS B CB   1 
ATOM   4298 S  SG   . CYS B 1 85  ? -45.168 -28.069 8.363  1.00 20.77  ? 85  CYS B SG   1 
ATOM   4299 H  H    . CYS B 1 85  ? -44.474 -24.889 7.472  1.00 19.56  ? 85  CYS B H    1 
ATOM   4300 H  HA   . CYS B 1 85  ? -44.778 -25.744 10.106 1.00 17.57  ? 85  CYS B HA   1 
ATOM   4301 H  HB2  . CYS B 1 85  ? -43.187 -26.915 8.056  1.00 19.58  ? 85  CYS B HB2  1 
ATOM   4302 H  HB3  . CYS B 1 85  ? -43.258 -27.485 9.527  1.00 19.58  ? 85  CYS B HB3  1 
ATOM   4303 H  HG   . CYS B 1 85  ? -44.529 -29.033 8.032  1.00 23.09  ? 85  CYS B HG   1 
ATOM   4304 N  N    . ALA B 1 86  ? -42.559 -25.103 11.100 1.00 13.64  ? 86  ALA B N    1 
ATOM   4305 C  CA   . ALA B 1 86  ? -41.310 -24.574 11.620 1.00 12.97  ? 86  ALA B CA   1 
ATOM   4306 C  C    . ALA B 1 86  ? -40.753 -25.543 12.646 1.00 12.00  ? 86  ALA B C    1 
ATOM   4307 O  O    . ALA B 1 86  ? -41.449 -26.419 13.168 1.00 12.81  ? 86  ALA B O    1 
ATOM   4308 C  CB   . ALA B 1 86  ? -41.515 -23.173 12.160 1.00 13.98  ? 86  ALA B CB   1 
ATOM   4309 H  H    . ALA B 1 86  ? -43.117 -25.562 11.660 1.00 17.57  ? 86  ALA B H    1 
ATOM   4310 H  HA   . ALA B 1 86  ? -40.669 -24.526 10.876 1.00 15.19  ? 86  ALA B HA   1 
ATOM   4311 H  HB1  . ALA B 1 86  ? -40.696 -22.864 12.584 1.00 17.39  ? 86  ALA B HB1  1 
ATOM   4312 H  HB2  . ALA B 1 86  ? -41.746 -22.574 11.430 1.00 17.39  ? 86  ALA B HB2  1 
ATOM   4313 H  HB3  . ALA B 1 86  ? -42.234 -23.177 12.813 1.00 17.39  ? 86  ALA B HB3  1 
ATOM   4314 N  N    . ALA B 1 87  ? -39.464 -25.336 12.948 1.00 11.67  ? 87  ALA B N    1 
ATOM   4315 C  CA   . ALA B 1 87  ? -38.816 -26.073 14.020 1.00 11.26  ? 87  ALA B CA   1 
ATOM   4316 C  C    . ALA B 1 87  ? -37.957 -25.106 14.815 1.00 10.54  ? 87  ALA B C    1 
ATOM   4317 O  O    . ALA B 1 87  ? -37.253 -24.276 14.245 1.00 11.27  ? 87  ALA B O    1 
ATOM   4318 C  CB   . ALA B 1 87  ? -37.969 -27.202 13.495 1.00 11.78  ? 87  ALA B CB   1 
ATOM   4319 H  H    . ALA B 1 87  ? -38.978 -24.723 12.475 1.00 15.19  ? 87  ALA B H    1 
ATOM   4320 H  HA   . ALA B 1 87  ? -39.508 -26.442 14.612 1.00 12.97  ? 87  ALA B HA   1 
ATOM   4321 H  HB1  . ALA B 1 87  ? -37.535 -27.656 14.237 1.00 14.12  ? 87  ALA B HB1  1 
ATOM   4322 H  HB2  . ALA B 1 87  ? -38.530 -27.834 13.014 1.00 14.12  ? 87  ALA B HB2  1 
ATOM   4323 H  HB3  . ALA B 1 87  ? -37.292 -26.848 12.893 1.00 14.12  ? 87  ALA B HB3  1 
ATOM   4324 N  N    . LEU B 1 88  ? -38.034 -25.235 16.149 1.00 10.24  ? 88  LEU B N    1 
ATOM   4325 C  CA   . LEU B 1 88  ? -37.118 -24.566 17.056 1.00 9.65   ? 88  LEU B CA   1 
ATOM   4326 C  C    . LEU B 1 88  ? -36.268 -25.674 17.683 1.00 9.30   ? 88  LEU B C    1 
ATOM   4327 O  O    . LEU B 1 88  ? -36.837 -26.575 18.311 1.00 9.86   ? 88  LEU B O    1 
ATOM   4328 C  CB   . LEU B 1 88  ? -37.891 -23.791 18.131 1.00 10.14  ? 88  LEU B CB   1 
ATOM   4329 C  CG   . LEU B 1 88  ? -37.020 -23.208 19.243 1.00 10.85  ? 88  LEU B CG   1 
ATOM   4330 C  CD1  . LEU B 1 88  ? -36.038 -22.174 18.709 1.00 11.70  ? 88  LEU B CD1  1 
ATOM   4331 C  CD2  . LEU B 1 88  ? -37.901 -22.580 20.312 1.00 12.34  ? 88  LEU B CD2  1 
ATOM   4332 H  H    . LEU B 1 88  ? -38.689 -25.763 16.505 1.00 12.97  ? 88  LEU B H    1 
ATOM   4333 H  HA   . LEU B 1 88  ? -36.541 -23.955 16.546 1.00 14.44  ? 88  LEU B HA   1 
ATOM   4334 H  HB2  . LEU B 1 88  ? -38.377 -23.062 17.698 1.00 12.08  ? 88  LEU B HB2  1 
ATOM   4335 H  HB3  . LEU B 1 88  ? -38.550 -24.392 18.533 1.00 12.08  ? 88  LEU B HB3  1 
ATOM   4336 H  HG   . LEU B 1 88  ? -36.505 -23.942 19.658 1.00 11.64  ? 88  LEU B HG   1 
ATOM   4337 H  HD11 . LEU B 1 88  ? -35.622 -21.706 19.453 1.00 15.23  ? 88  LEU B HD11 1 
ATOM   4338 H  HD12 . LEU B 1 88  ? -35.352 -22.619 18.182 1.00 15.22  ? 88  LEU B HD12 1 
ATOM   4339 H  HD13 . LEU B 1 88  ? -36.512 -21.535 18.148 1.00 15.22  ? 88  LEU B HD13 1 
ATOM   4340 H  HD21 . LEU B 1 88  ? -37.343 -22.236 21.031 1.00 15.47  ? 88  LEU B HD21 1 
ATOM   4341 H  HD22 . LEU B 1 88  ? -38.414 -21.851 19.923 1.00 15.47  ? 88  LEU B HD22 1 
ATOM   4342 H  HD23 . LEU B 1 88  ? -38.509 -23.251 20.666 1.00 15.47  ? 88  LEU B HD23 1 
ATOM   4343 N  N    . ILE B 1 89  ? -34.943 -25.585 17.497 1.00 9.35   ? 89  ILE B N    1 
ATOM   4344 C  CA   . ILE B 1 89  ? -34.047 -26.615 17.972 1.00 9.03   ? 89  ILE B CA   1 
ATOM   4345 C  C    . ILE B 1 89  ? -32.984 -25.923 18.819 1.00 8.96   ? 89  ILE B C    1 
ATOM   4346 O  O    . ILE B 1 89  ? -31.928 -25.469 18.335 1.00 9.48   ? 89  ILE B O    1 
ATOM   4347 C  CB   . ILE B 1 89  ? -33.469 -27.479 16.836 1.00 9.17   ? 89  ILE B CB   1 
ATOM   4348 C  CG1  . ILE B 1 89  ? -34.613 -28.077 15.997 1.00 10.30  ? 89  ILE B CG1  1 
ATOM   4349 C  CG2  . ILE B 1 89  ? -32.604 -28.568 17.446 1.00 10.77  ? 89  ILE B CG2  1 
ATOM   4350 C  CD1  . ILE B 1 89  ? -34.156 -28.945 14.844 1.00 10.96  ? 89  ILE B CD1  1 
ATOM   4351 H  H    . ILE B 1 89  ? -34.593 -24.862 17.061 1.00 14.44  ? 89  ILE B H    1 
ATOM   4352 H  HA   . ILE B 1 89  ? -34.552 -27.204 18.552 1.00 11.64  ? 89  ILE B HA   1 
ATOM   4353 H  HB   . ILE B 1 89  ? -32.911 -26.912 16.254 1.00 13.46  ? 89  ILE B HB   1 
ATOM   4354 H  HG12 . ILE B 1 89  ? -35.186 -28.613 16.585 1.00 12.31  ? 89  ILE B HG12 1 
ATOM   4355 H  HG13 . ILE B 1 89  ? -35.156 -27.344 15.637 1.00 12.31  ? 89  ILE B HG13 1 
ATOM   4356 H  HG21 . ILE B 1 89  ? -32.205 -29.103 16.738 1.00 12.96  ? 89  ILE B HG21 1 
ATOM   4357 H  HG22 . ILE B 1 89  ? -31.898 -28.167 17.980 1.00 12.96  ? 89  ILE B HG22 1 
ATOM   4358 H  HG23 . ILE B 1 89  ? -33.150 -29.141 18.011 1.00 12.96  ? 89  ILE B HG23 1 
ATOM   4359 H  HD11 . ILE B 1 89  ? -34.887 -29.060 14.213 1.00 12.97  ? 89  ILE B HD11 1 
ATOM   4360 H  HD12 . ILE B 1 89  ? -33.405 -28.519 14.394 1.00 12.97  ? 89  ILE B HD12 1 
ATOM   4361 H  HD13 . ILE B 1 89  ? -33.879 -29.815 15.180 1.00 12.97  ? 89  ILE B HD13 1 
ATOM   4362 N  N    . PRO B 1 90  ? -33.210 -25.840 20.139 1.00 9.16   ? 90  PRO B N    1 
ATOM   4363 C  CA   . PRO B 1 90  ? -32.196 -25.363 21.067 1.00 8.89   ? 90  PRO B CA   1 
ATOM   4364 C  C    . PRO B 1 90  ? -31.113 -26.429 21.242 1.00 9.14   ? 90  PRO B C    1 
ATOM   4365 O  O    . PRO B 1 90  ? -31.427 -27.608 21.406 1.00 9.87   ? 90  PRO B O    1 
ATOM   4366 C  CB   . PRO B 1 90  ? -32.982 -25.125 22.374 1.00 9.81   ? 90  PRO B CB   1 
ATOM   4367 C  CG   . PRO B 1 90  ? -34.424 -25.003 21.922 1.00 10.03  ? 90  PRO B CG   1 
ATOM   4368 C  CD   . PRO B 1 90  ? -34.513 -26.041 20.817 1.00 9.41   ? 90  PRO B CD   1 
ATOM   4369 H  HA   . PRO B 1 90  ? -31.811 -24.512 20.741 1.00 10.70  ? 90  PRO B HA   1 
ATOM   4370 H  HB2  . PRO B 1 90  ? -32.873 -25.878 22.994 1.00 11.68  ? 90  PRO B HB2  1 
ATOM   4371 H  HB3  . PRO B 1 90  ? -32.685 -24.302 22.818 1.00 11.68  ? 90  PRO B HB3  1 
ATOM   4372 H  HG2  . PRO B 1 90  ? -35.043 -25.209 22.652 1.00 12.20  ? 90  PRO B HG2  1 
ATOM   4373 H  HG3  . PRO B 1 90  ? -34.614 -24.106 21.580 1.00 12.20  ? 90  PRO B HG3  1 
ATOM   4374 H  HD2  . PRO B 1 90  ? -34.592 -26.942 21.180 1.00 11.64  ? 90  PRO B HD2  1 
ATOM   4375 H  HD3  . PRO B 1 90  ? -35.263 -25.861 20.222 1.00 11.64  ? 90  PRO B HD3  1 
ATOM   4376 N  N    . ILE B 1 91  ? -29.844 -25.986 21.221 1.00 8.78   ? 91  ILE B N    1 
ATOM   4377 C  CA   . ILE B 1 91  ? -28.683 -26.858 21.285 1.00 9.33   ? 91  ILE B CA   1 
ATOM   4378 C  C    . ILE B 1 91  ? -27.689 -26.328 22.310 1.00 9.08   ? 91  ILE B C    1 
ATOM   4379 O  O    . ILE B 1 91  ? -27.365 -25.139 22.319 1.00 9.38   ? 91  ILE B O    1 
ATOM   4380 C  CB   . ILE B 1 91  ? -28.019 -26.952 19.889 1.00 9.98   ? 91  ILE B CB   1 
ATOM   4381 C  CG1  . ILE B 1 91  ? -28.932 -27.760 18.970 1.00 11.83  ? 91  ILE B CG1  1 
ATOM   4382 C  CG2  . ILE B 1 91  ? -26.616 -27.539 19.957 1.00 11.27  ? 91  ILE B CG2  1 
ATOM   4383 C  CD1  . ILE B 1 91  ? -28.595 -27.685 17.498 1.00 12.99  ? 91  ILE B CD1  1 
ATOM   4384 H  H    . ILE B 1 91  ? -29.700 -25.085 21.164 1.00 10.70  ? 91  ILE B H    1 
ATOM   4385 H  HA   . ILE B 1 91  ? -28.971 -27.746 21.553 1.00 11.84  ? 91  ILE B HA   1 
ATOM   4386 H  HB   . ILE B 1 91  ? -27.952 -26.036 19.521 1.00 12.13  ? 91  ILE B HB   1 
ATOM   4387 H  HG12 . ILE B 1 91  ? -28.898 -28.700 19.248 1.00 14.68  ? 91  ILE B HG12 1 
ATOM   4388 H  HG13 . ILE B 1 91  ? -29.853 -27.449 19.090 1.00 14.68  ? 91  ILE B HG13 1 
ATOM   4389 H  HG21 . ILE B 1 91  ? -26.356 -27.871 19.080 1.00 14.86  ? 91  ILE B HG21 1 
ATOM   4390 H  HG22 . ILE B 1 91  ? -25.986 -26.852 20.237 1.00 14.86  ? 91  ILE B HG22 1 
ATOM   4391 H  HG23 . ILE B 1 91  ? -26.599 -28.273 20.595 1.00 14.86  ? 91  ILE B HG23 1 
ATOM   4392 H  HD11 . ILE B 1 91  ? -29.343 -28.024 16.977 1.00 14.93  ? 91  ILE B HD11 1 
ATOM   4393 H  HD12 . ILE B 1 91  ? -28.422 -26.760 17.251 1.00 14.92  ? 91  ILE B HD12 1 
ATOM   4394 H  HD13 . ILE B 1 91  ? -27.805 -28.222 17.316 1.00 14.92  ? 91  ILE B HD13 1 
ATOM   4395 N  N    . ARG B 1 92  ? -27.160 -27.245 23.129 1.00 10.15  ? 92  ARG B N    1 
ATOM   4396 C  CA   . ARG B 1 92  ? -26.056 -26.953 24.015 1.00 11.13  ? 92  ARG B CA   1 
ATOM   4397 C  C    . ARG B 1 92  ? -24.891 -27.853 23.648 1.00 11.15  ? 92  ARG B C    1 
ATOM   4398 O  O    . ARG B 1 92  ? -25.052 -29.065 23.478 1.00 12.59  ? 92  ARG B O    1 
ATOM   4399 C  CB   . ARG B 1 92  ? -26.426 -27.163 25.477 1.00 12.28  ? 92  ARG B CB   1 
ATOM   4400 C  CG   . ARG B 1 92  ? -25.357 -26.671 26.444 1.00 15.65  ? 92  ARG B CG   1 
ATOM   4401 C  CD   . ARG B 1 92  ? -25.730 -26.860 27.889 1.00 19.28  ? 92  ARG B CD   1 
ATOM   4402 N  NE   . ARG B 1 92  ? -24.703 -26.397 28.811 1.00 27.76  ? 92  ARG B NE   1 
ATOM   4403 C  CZ   . ARG B 1 92  ? -24.702 -25.224 29.435 1.00 31.62  ? 92  ARG B CZ   1 
ATOM   4404 N  NH1  . ARG B 1 92  ? -25.701 -24.364 29.279 1.00 36.22  ? 92  ARG B NH1  1 
ATOM   4405 N  NH2  . ARG B 1 92  ? -23.700 -24.910 30.235 1.00 37.08  ? 92  ARG B NH2  1 
ATOM   4406 H  H    . ARG B 1 92  ? -27.508 -28.091 23.133 1.00 11.84  ? 92  ARG B H    1 
ATOM   4407 H  HA   . ARG B 1 92  ? -25.786 -26.016 23.887 1.00 18.49  ? 92  ARG B HA   1 
ATOM   4408 H  HB2  . ARG B 1 92  ? -27.264 -26.688 25.660 1.00 14.71  ? 92  ARG B HB2  1 
ATOM   4409 H  HB3  . ARG B 1 92  ? -26.579 -28.119 25.630 1.00 14.71  ? 92  ARG B HB3  1 
ATOM   4410 H  HG2  . ARG B 1 92  ? -24.520 -27.152 26.271 1.00 18.96  ? 92  ARG B HG2  1 
ATOM   4411 H  HG3  . ARG B 1 92  ? -25.192 -25.717 26.283 1.00 18.96  ? 92  ARG B HG3  1 
ATOM   4412 H  HD2  . ARG B 1 92  ? -26.564 -26.380 28.069 1.00 39.28  ? 92  ARG B HD2  1 
ATOM   4413 H  HD3  . ARG B 1 92  ? -25.895 -27.813 28.052 1.00 39.30  ? 92  ARG B HD3  1 
ATOM   4414 H  HE   . ARG B 1 92  ? -24.033 -26.933 28.966 1.00 35.18  ? 92  ARG B HE   1 
ATOM   4415 H  HH11 . ARG B 1 92  ? -25.925 -24.094 28.471 1.00 38.81  ? 92  ARG B HH11 1 
ATOM   4416 H  HH12 . ARG B 1 92  ? -26.135 -24.063 29.984 1.00 38.81  ? 92  ARG B HH12 1 
ATOM   4417 H  HH21 . ARG B 1 92  ? -23.098 -25.515 30.444 1.00 35.18  ? 92  ARG B HH21 1 
ATOM   4418 H  HH22 . ARG B 1 92  ? -23.637 -24.094 30.557 1.00 35.18  ? 92  ARG B HH22 1 
ATOM   4419 N  N    . LYS B 1 93  ? -23.710 -27.240 23.539 1.00 11.10  ? 93  LYS B N    1 
ATOM   4420 C  CA   A LYS B 1 93  ? -22.489 -27.982 23.299 0.50 11.71  ? 93  LYS B CA   1 
ATOM   4421 C  CA   B LYS B 1 93  ? -22.488 -27.982 23.292 0.50 11.77  ? 93  LYS B CA   1 
ATOM   4422 C  C    . LYS B 1 93  ? -21.870 -28.487 24.594 1.00 15.02  ? 93  LYS B C    1 
ATOM   4423 O  O    . LYS B 1 93  ? -22.085 -27.996 25.706 1.00 17.32  ? 93  LYS B O    1 
ATOM   4424 C  CB   A LYS B 1 93  ? -21.432 -27.067 22.744 0.50 14.63  ? 93  LYS B CB   1 
ATOM   4425 C  CB   B LYS B 1 93  ? -21.457 -27.071 22.674 0.50 14.71  ? 93  LYS B CB   1 
ATOM   4426 C  CG   A LYS B 1 93  ? -21.799 -26.427 21.457 0.50 14.89  ? 93  LYS B CG   1 
ATOM   4427 C  CG   B LYS B 1 93  ? -21.871 -26.392 21.409 0.50 16.18  ? 93  LYS B CG   1 
ATOM   4428 C  CD   A LYS B 1 93  ? -21.780 -27.431 20.432 0.50 15.51  ? 93  LYS B CD   1 
ATOM   4429 C  CD   B LYS B 1 93  ? -21.734 -27.290 20.272 0.50 18.64  ? 93  LYS B CD   1 
ATOM   4430 C  CE   A LYS B 1 93  ? -21.331 -26.782 19.154 0.50 12.74  ? 93  LYS B CE   1 
ATOM   4431 C  CE   B LYS B 1 93  ? -21.336 -26.503 19.056 0.50 17.27  ? 93  LYS B CE   1 
ATOM   4432 N  NZ   A LYS B 1 93  ? -20.614 -27.663 18.206 0.50 14.78  ? 93  LYS B NZ   1 
ATOM   4433 N  NZ   B LYS B 1 93  ? -21.360 -27.288 17.814 0.50 21.14  ? 93  LYS B NZ   1 
ATOM   4434 H  H    . LYS B 1 93  ? -23.667 -26.329 23.625 1.00 18.49  ? 93  LYS B H    1 
ATOM   4435 H  HA   . LYS B 1 93  ? -22.668 -28.733 22.681 1.00 17.66  ? 93  LYS B HA   1 
ATOM   4436 H  HB2  A LYS B 1 93  ? -21.248 -26.365 23.401 0.50 14.93  ? 93  LYS B HB2  1 
ATOM   4437 H  HB2  B LYS B 1 93  ? -21.221 -26.383 23.331 0.50 14.93  ? 93  LYS B HB2  1 
ATOM   4438 H  HB3  A LYS B 1 93  ? -20.608 -27.582 22.614 0.50 14.93  ? 93  LYS B HB3  1 
ATOM   4439 H  HB3  B LYS B 1 93  ? -20.650 -27.597 22.493 0.50 14.93  ? 93  LYS B HB3  1 
ATOM   4440 H  HG2  A LYS B 1 93  ? -22.695 -26.033 21.523 0.50 18.49  ? 93  LYS B HG2  1 
ATOM   4441 H  HG2  B LYS B 1 93  ? -22.804 -26.099 21.484 0.50 18.49  ? 93  LYS B HG2  1 
ATOM   4442 H  HG3  A LYS B 1 93  ? -21.156 -25.718 21.244 0.50 18.49  ? 93  LYS B HG3  1 
ATOM   4443 H  HG3  B LYS B 1 93  ? -21.311 -25.599 21.269 0.50 18.49  ? 93  LYS B HG3  1 
ATOM   4444 H  HD2  A LYS B 1 93  ? -21.159 -28.150 20.677 0.50 14.92  ? 93  LYS B HD2  1 
ATOM   4445 H  HD2  B LYS B 1 93  ? -21.050 -27.966 20.465 0.50 14.92  ? 93  LYS B HD2  1 
ATOM   4446 H  HD3  A LYS B 1 93  ? -22.678 -27.810 20.316 0.50 14.92  ? 93  LYS B HD3  1 
ATOM   4447 H  HD3  B LYS B 1 93  ? -22.587 -27.745 20.105 0.50 14.92  ? 93  LYS B HD3  1 
ATOM   4448 H  HE2  A LYS B 1 93  ? -22.112 -26.415 18.698 0.50 18.49  ? 93  LYS B HE2  1 
ATOM   4449 H  HE2  B LYS B 1 93  ? -21.944 -25.749 18.952 0.50 16.52  ? 93  LYS B HE2  1 
ATOM   4450 H  HE3  A LYS B 1 93  ? -20.746 -26.032 19.373 0.50 18.49  ? 93  LYS B HE3  1 
ATOM   4451 H  HE3  B LYS B 1 93  ? -20.441 -26.144 19.184 0.50 16.53  ? 93  LYS B HE3  1 
ATOM   4452 H  HZ1  A LYS B 1 93  ? -19.924 -28.070 18.627 0.50 20.92  ? 93  LYS B HZ1  1 
ATOM   4453 H  HZ1  B LYS B 1 93  ? -20.528 -27.306 17.447 0.50 20.98  ? 93  LYS B HZ1  1 
ATOM   4454 H  HZ2  A LYS B 1 93  ? -21.181 -28.295 17.886 0.50 20.92  ? 93  LYS B HZ2  1 
ATOM   4455 H  HZ2  B LYS B 1 93  ? -21.621 -28.138 17.993 0.50 20.98  ? 93  LYS B HZ2  1 
ATOM   4456 H  HZ3  A LYS B 1 93  ? -20.296 -27.174 17.512 0.50 20.92  ? 93  LYS B HZ3  1 
ATOM   4457 H  HZ3  B LYS B 1 93  ? -21.938 -26.916 17.224 0.50 20.98  ? 93  LYS B HZ3  1 
ATOM   4458 N  N    . ASN B 1 94  ? -21.107 -29.549 24.466 1.00 15.65  ? 94  ASN B N    1 
ATOM   4459 C  CA   A ASN B 1 94  ? -20.335 -29.886 25.630 0.38 16.16  ? 94  ASN B CA   1 
ATOM   4460 C  CA   B ASN B 1 94  ? -20.149 -30.041 25.453 0.62 15.65  ? 94  ASN B CA   1 
ATOM   4461 C  C    . ASN B 1 94  ? -19.277 -28.827 25.849 1.00 15.67  ? 94  ASN B C    1 
ATOM   4462 O  O    . ASN B 1 94  ? -18.761 -28.136 24.955 1.00 18.72  ? 94  ASN B O    1 
ATOM   4463 C  CB   A ASN B 1 94  ? -19.604 -31.193 25.539 0.38 13.92  ? 94  ASN B CB   1 
ATOM   4464 C  CB   B ASN B 1 94  ? -19.442 -31.254 24.812 0.62 14.19  ? 94  ASN B CB   1 
ATOM   4465 C  CG   A ASN B 1 94  ? -18.464 -31.197 24.552 0.38 11.85  ? 94  ASN B CG   1 
ATOM   4466 C  CG   B ASN B 1 94  ? -18.383 -31.930 25.660 0.62 13.68  ? 94  ASN B CG   1 
ATOM   4467 O  OD1  A ASN B 1 94  ? -17.886 -30.200 24.110 0.38 14.57  ? 94  ASN B OD1  1 
ATOM   4468 O  OD1  B ASN B 1 94  ? -17.627 -31.241 26.346 0.62 14.73  ? 94  ASN B OD1  1 
ATOM   4469 N  ND2  A ASN B 1 94  ? -18.183 -32.420 24.151 0.38 15.02  ? 94  ASN B ND2  1 
ATOM   4470 N  ND2  B ASN B 1 94  ? -18.258 -33.243 25.536 0.62 14.18  ? 94  ASN B ND2  1 
ATOM   4471 H  H    A ASN B 1 94  ? -21.054 -30.042 23.698 0.38 17.66  ? 94  ASN B H    1 
ATOM   4472 H  H    B ASN B 1 94  ? -21.185 -30.027 23.690 0.62 17.66  ? 94  ASN B H    1 
ATOM   4473 H  HA   A ASN B 1 94  ? -20.934 -29.924 26.410 0.38 30.05  ? 94  ASN B HA   1 
ATOM   4474 H  HA   B ASN B 1 94  ? -20.643 -30.354 26.242 0.62 30.05  ? 94  ASN B HA   1 
ATOM   4475 H  HB2  A ASN B 1 94  ? -19.255 -31.420 26.424 0.38 29.77  ? 94  ASN B HB2  1 
ATOM   4476 H  HB2  B ASN B 1 94  ? -20.123 -31.918 24.582 0.62 17.66  ? 94  ASN B HB2  1 
ATOM   4477 H  HB3  A ASN B 1 94  ? -20.243 -31.889 25.282 0.38 29.77  ? 94  ASN B HB3  1 
ATOM   4478 H  HB3  B ASN B 1 94  ? -19.026 -30.959 23.977 0.62 17.66  ? 94  ASN B HB3  1 
ATOM   4479 H  HD21 A ASN B 1 94  ? -17.467 -32.568 23.654 0.38 20.08  ? 94  ASN B HD21 1 
ATOM   4480 H  HD21 B ASN B 1 94  ? -17.455 -33.609 25.496 0.62 17.66  ? 94  ASN B HD21 1 
ATOM   4481 H  HD22 A ASN B 1 94  ? -18.709 -33.093 24.380 0.38 20.08  ? 94  ASN B HD22 1 
ATOM   4482 H  HD22 B ASN B 1 94  ? -18.979 -33.754 25.495 0.62 17.66  ? 94  ASN B HD22 1 
ATOM   4483 N  N    . PRO B 1 95  ? -18.921 -28.588 27.116 1.00 18.22  ? 95  PRO B N    1 
ATOM   4484 C  CA   . PRO B 1 95  ? -18.047 -27.461 27.434 1.00 21.81  ? 95  PRO B CA   1 
ATOM   4485 C  C    . PRO B 1 95  ? -16.659 -27.515 26.792 1.00 18.24  ? 95  PRO B C    1 
ATOM   4486 O  O    . PRO B 1 95  ? -16.061 -26.471 26.549 1.00 21.53  ? 95  PRO B O    1 
ATOM   4487 C  CB   . PRO B 1 95  ? -17.890 -27.459 28.966 1.00 26.81  ? 95  PRO B CB   1 
ATOM   4488 C  CG   . PRO B 1 95  ? -18.818 -28.513 29.478 1.00 26.59  ? 95  PRO B CG   1 
ATOM   4489 C  CD   . PRO B 1 95  ? -19.409 -29.278 28.314 1.00 21.35  ? 95  PRO B CD   1 
ATOM   4490 H  HA   . PRO B 1 95  ? -18.500 -26.624 27.161 1.00 23.24  ? 95  PRO B HA   1 
ATOM   4491 H  HB2  . PRO B 1 95  ? -16.965 -27.664 29.222 1.00 26.33  ? 95  PRO B HB2  1 
ATOM   4492 H  HB3  . PRO B 1 95  ? -18.128 -26.582 29.337 1.00 26.33  ? 95  PRO B HB3  1 
ATOM   4493 H  HG2  . PRO B 1 95  ? -18.333 -29.126 30.066 1.00 26.20  ? 95  PRO B HG2  1 
ATOM   4494 H  HG3  . PRO B 1 95  ? -19.535 -28.099 30.000 1.00 26.20  ? 95  PRO B HG3  1 
ATOM   4495 H  HD2  . PRO B 1 95  ? -19.110 -30.206 28.323 1.00 30.04  ? 95  PRO B HD2  1 
ATOM   4496 H  HD3  . PRO B 1 95  ? -20.382 -29.263 28.351 1.00 30.05  ? 95  PRO B HD3  1 
ATOM   4497 N  N    . SER B 1 96  ? -16.136 -28.711 26.512 1.00 15.66  ? 96  SER B N    1 
ATOM   4498 C  CA   . SER B 1 96  ? -14.842 -28.805 25.842 1.00 15.61  ? 96  SER B CA   1 
ATOM   4499 C  C    . SER B 1 96  ? -14.813 -28.128 24.494 1.00 12.23  ? 96  SER B C    1 
ATOM   4500 O  O    . SER B 1 96  ? -13.771 -27.627 24.094 1.00 12.60  ? 96  SER B O    1 
ATOM   4501 C  CB   . SER B 1 96  ? -14.347 -30.245 25.676 1.00 17.84  ? 96  SER B CB   1 
ATOM   4502 O  OG   . SER B 1 96  ? -14.928 -30.971 24.570 1.00 20.43  ? 96  SER B OG   1 
ATOM   4503 H  H    . SER B 1 96  ? -16.578 -29.476 26.743 1.00 19.91  ? 96  SER B H    1 
ATOM   4504 H  HA   . SER B 1 96  ? -14.184 -28.333 26.420 1.00 18.61  ? 96  SER B HA   1 
ATOM   4505 H  HB2  . SER B 1 96  ? -13.370 -30.227 25.562 1.00 19.91  ? 96  SER B HB2  1 
ATOM   4506 H  HB3  . SER B 1 96  ? -14.536 -30.737 26.507 1.00 19.91  ? 96  SER B HB3  1 
ATOM   4507 H  HG   . SER B 1 96  ? -14.329 -31.101 23.986 1.00 19.91  ? 96  SER B HG   1 
ATOM   4508 N  N    . TRP B 1 97  ? -15.938 -28.093 23.786 1.00 11.84  ? 97  TRP B N    1 
ATOM   4509 C  CA   . TRP B 1 97  ? -15.998 -27.443 22.488 1.00 10.29  ? 97  TRP B CA   1 
ATOM   4510 C  C    . TRP B 1 97  ? -15.475 -26.016 22.588 1.00 9.35   ? 97  TRP B C    1 
ATOM   4511 O  O    . TRP B 1 97  ? -14.722 -25.542 21.741 1.00 9.65   ? 97  TRP B O    1 
ATOM   4512 C  CB   . TRP B 1 97  ? -17.445 -27.452 22.014 1.00 10.34  ? 97  TRP B CB   1 
ATOM   4513 C  CG   . TRP B 1 97  ? -17.683 -26.676 20.753 1.00 9.42   ? 97  TRP B CG   1 
ATOM   4514 C  CD1  . TRP B 1 97  ? -18.206 -25.421 20.647 1.00 9.59   ? 97  TRP B CD1  1 
ATOM   4515 C  CD2  . TRP B 1 97  ? -17.426 -27.125 19.420 1.00 8.89   ? 97  TRP B CD2  1 
ATOM   4516 N  NE1  . TRP B 1 97  ? -18.273 -25.043 19.348 1.00 9.31   ? 97  TRP B NE1  1 
ATOM   4517 C  CE2  . TRP B 1 97  ? -17.813 -26.070 18.561 1.00 9.01   ? 97  TRP B CE2  1 
ATOM   4518 C  CE3  . TRP B 1 97  ? -16.902 -28.278 18.851 1.00 10.37  ? 97  TRP B CE3  1 
ATOM   4519 C  CZ2  . TRP B 1 97  ? -17.690 -26.150 17.181 1.00 10.02  ? 97  TRP B CZ2  1 
ATOM   4520 C  CZ3  . TRP B 1 97  ? -16.790 -28.364 17.484 1.00 11.75  ? 97  TRP B CZ3  1 
ATOM   4521 C  CH2  . TRP B 1 97  ? -17.167 -27.308 16.653 1.00 11.59  ? 97  TRP B CH2  1 
ATOM   4522 H  H    . TRP B 1 97  ? -16.691 -28.496 24.113 1.00 12.51  ? 97  TRP B H    1 
ATOM   4523 H  HA   . TRP B 1 97  ? -15.448 -27.955 21.849 1.00 12.57  ? 97  TRP B HA   1 
ATOM   4524 H  HB2  . TRP B 1 97  ? -17.717 -28.382 21.874 1.00 12.51  ? 97  TRP B HB2  1 
ATOM   4525 H  HB3  . TRP B 1 97  ? -18.004 -27.081 22.726 1.00 12.51  ? 97  TRP B HB3  1 
ATOM   4526 H  HD1  . TRP B 1 97  ? -18.472 -24.882 21.372 1.00 12.56  ? 97  TRP B HD1  1 
ATOM   4527 H  HE1  . TRP B 1 97  ? -18.581 -24.275 19.057 1.00 12.56  ? 97  TRP B HE1  1 
ATOM   4528 H  HE3  . TRP B 1 97  ? -16.640 -29.000 19.399 1.00 12.56  ? 97  TRP B HE3  1 
ATOM   4529 H  HZ2  . TRP B 1 97  ? -17.951 -25.433 16.628 1.00 12.56  ? 97  TRP B HZ2  1 
ATOM   4530 H  HZ3  . TRP B 1 97  ? -16.436 -29.150 17.098 1.00 12.56  ? 97  TRP B HZ3  1 
ATOM   4531 H  HH2  . TRP B 1 97  ? -17.080 -27.395 15.720 1.00 12.56  ? 97  TRP B HH2  1 
ATOM   4532 N  N    . TRP B 1 98  ? -15.926 -25.290 23.619 1.00 9.76   ? 98  TRP B N    1 
ATOM   4533 C  CA   . TRP B 1 98  ? -15.639 -23.873 23.718 1.00 10.10  ? 98  TRP B CA   1 
ATOM   4534 C  C    . TRP B 1 98  ? -14.173 -23.608 24.013 1.00 10.52  ? 98  TRP B C    1 
ATOM   4535 O  O    . TRP B 1 98  ? -13.715 -22.511 23.784 1.00 12.72  ? 98  TRP B O    1 
ATOM   4536 C  CB   . TRP B 1 98  ? -16.567 -23.205 24.742 1.00 11.58  ? 98  TRP B CB   1 
ATOM   4537 C  CG   . TRP B 1 98  ? -18.003 -23.347 24.356 1.00 11.33  ? 98  TRP B CG   1 
ATOM   4538 C  CD1  . TRP B 1 98  ? -19.026 -24.059 24.961 1.00 12.45  ? 98  TRP B CD1  1 
ATOM   4539 C  CD2  . TRP B 1 98  ? -18.588 -22.818 23.163 1.00 10.06  ? 98  TRP B CD2  1 
ATOM   4540 N  NE1  . TRP B 1 98  ? -20.166 -23.998 24.199 1.00 12.70  ? 98  TRP B NE1  1 
ATOM   4541 C  CE2  . TRP B 1 98  ? -19.927 -23.247 23.100 1.00 11.11  ? 98  TRP B CE2  1 
ATOM   4542 C  CE3  . TRP B 1 98  ? -18.121 -21.999 22.136 1.00 11.08  ? 98  TRP B CE3  1 
ATOM   4543 C  CZ2  . TRP B 1 98  ? -20.781 -22.863 22.063 1.00 11.75  ? 98  TRP B CZ2  1 
ATOM   4544 C  CZ3  . TRP B 1 98  ? -18.976 -21.642 21.112 1.00 12.95  ? 98  TRP B CZ3  1 
ATOM   4545 C  CH2  . TRP B 1 98  ? -20.284 -22.066 21.079 1.00 13.71  ? 98  TRP B CH2  1 
ATOM   4546 H  H    . TRP B 1 98  ? -16.423 -25.690 24.274 1.00 13.59  ? 98  TRP B H    1 
ATOM   4547 H  HA   . TRP B 1 98  ? -15.845 -23.476 22.840 1.00 15.05  ? 98  TRP B HA   1 
ATOM   4548 H  HB2  . TRP B 1 98  ? -16.419 -23.617 25.618 1.00 36.94  ? 98  TRP B HB2  1 
ATOM   4549 H  HB3  . TRP B 1 98  ? -16.335 -22.256 24.806 1.00 36.94  ? 98  TRP B HB3  1 
ATOM   4550 H  HD1  . TRP B 1 98  ? -18.940 -24.567 25.753 1.00 15.01  ? 98  TRP B HD1  1 
ATOM   4551 H  HE1  . TRP B 1 98  ? -20.932 -24.368 24.406 1.00 14.98  ? 98  TRP B HE1  1 
ATOM   4552 H  HE3  . TRP B 1 98  ? -17.220 -21.718 22.126 1.00 15.05  ? 98  TRP B HE3  1 
ATOM   4553 H  HZ2  . TRP B 1 98  ? -21.683 -23.137 22.057 1.00 15.00  ? 98  TRP B HZ2  1 
ATOM   4554 H  HZ3  . TRP B 1 98  ? -18.650 -21.105 20.407 1.00 15.07  ? 98  TRP B HZ3  1 
ATOM   4555 H  HH2  . TRP B 1 98  ? -20.840 -21.802 20.374 1.00 15.14  ? 98  TRP B HH2  1 
ATOM   4556 N  N    . GLY B 1 99  ? -13.454 -24.580 24.558 1.00 10.15  ? 99  GLY B N    1 
ATOM   4557 C  CA   . GLY B 1 99  ? -12.040 -24.445 24.802 1.00 11.00  ? 99  GLY B CA   1 
ATOM   4558 C  C    . GLY B 1 99  ? -11.143 -24.759 23.610 1.00 10.21  ? 99  GLY B C    1 
ATOM   4559 O  O    . GLY B 1 99  ? -9.957  -24.516 23.666 1.00 11.98  ? 99  GLY B O    1 
ATOM   4560 H  H    . GLY B 1 99  ? -13.865 -25.359 24.803 1.00 12.21  ? 99  GLY B H    1 
ATOM   4561 H  HA2  . GLY B 1 99  ? -11.858 -23.519 25.103 1.00 13.27  ? 99  GLY B HA2  1 
ATOM   4562 H  HA3  . GLY B 1 99  ? -11.795 -25.046 25.549 1.00 13.27  ? 99  GLY B HA3  1 
ATOM   4563 N  N    . LEU B 1 100 ? -11.699 -25.350 22.561 1.00 9.68   ? 100 LEU B N    1 
ATOM   4564 C  CA   . LEU B 1 100 ? -10.931 -25.635 21.356 1.00 9.76   ? 100 LEU B CA   1 
ATOM   4565 C  C    . LEU B 1 100 ? -10.582 -24.340 20.653 1.00 9.80   ? 100 LEU B C    1 
ATOM   4566 O  O    . LEU B 1 100 ? -11.318 -23.342 20.727 1.00 9.88   ? 100 LEU B O    1 
ATOM   4567 C  CB   . LEU B 1 100 ? -11.737 -26.529 20.428 1.00 10.20  ? 100 LEU B CB   1 
ATOM   4568 C  CG   . LEU B 1 100 ? -12.063 -27.922 20.942 1.00 10.96  ? 100 LEU B CG   1 
ATOM   4569 C  CD1  . LEU B 1 100 ? -12.938 -28.621 19.924 1.00 12.94  ? 100 LEU B CD1  1 
ATOM   4570 C  CD2  . LEU B 1 100 ? -10.812 -28.732 21.185 1.00 12.63  ? 100 LEU B CD2  1 
ATOM   4571 H  H    . LEU B 1 100 ? -12.580 -25.590 22.590 1.00 12.95  ? 100 LEU B H    1 
ATOM   4572 H  HA   . LEU B 1 100 ? -10.099 -26.093 21.616 1.00 16.08  ? 100 LEU B HA   1 
ATOM   4573 H  HB2  . LEU B 1 100 ? -12.578 -26.074 20.225 1.00 14.52  ? 100 LEU B HB2  1 
ATOM   4574 H  HB3  . LEU B 1 100 ? -11.244 -26.619 19.588 1.00 14.52  ? 100 LEU B HB3  1 
ATOM   4575 H  HG   . LEU B 1 100 ? -12.562 -27.842 21.791 1.00 12.95  ? 100 LEU B HG   1 
ATOM   4576 H  HD11 . LEU B 1 100 ? -13.168 -29.510 20.248 1.00 14.74  ? 100 LEU B HD11 1 
ATOM   4577 H  HD12 . LEU B 1 100 ? -13.753 -28.107 19.787 1.00 14.73  ? 100 LEU B HD12 1 
ATOM   4578 H  HD13 . LEU B 1 100 ? -12.459 -28.698 19.081 1.00 14.73  ? 100 LEU B HD13 1 
ATOM   4579 H  HD21 . LEU B 1 100 ? -11.049 -29.667 21.313 1.00 15.25  ? 100 LEU B HD21 1 
ATOM   4580 H  HD22 . LEU B 1 100 ? -10.218 -28.651 20.418 1.00 15.26  ? 100 LEU B HD22 1 
ATOM   4581 H  HD23 . LEU B 1 100 ? -10.360 -28.402 21.981 1.00 15.27  ? 100 LEU B HD23 1 
ATOM   4582 N  N    . SER B 1 101 ? -9.457  -24.370 19.929 1.00 9.86   ? 101 SER B N    1 
ATOM   4583 C  CA   A SER B 1 101 ? -9.062  -23.228 19.133 0.62 10.04  ? 101 SER B CA   1 
ATOM   4584 C  CA   B SER B 1 101 ? -9.037  -23.251 19.111 0.38 10.12  ? 101 SER B CA   1 
ATOM   4585 C  C    . SER B 1 101 ? -9.917  -23.113 17.873 1.00 9.28   ? 101 SER B C    1 
ATOM   4586 O  O    . SER B 1 101 ? -10.700 -23.987 17.532 1.00 9.45   ? 101 SER B O    1 
ATOM   4587 C  CB   A SER B 1 101 ? -7.590  -23.327 18.804 0.62 11.24  ? 101 SER B CB   1 
ATOM   4588 C  CB   B SER B 1 101 ? -7.590  -23.414 18.716 0.38 11.36  ? 101 SER B CB   1 
ATOM   4589 O  OG   A SER B 1 101 ? -7.307  -24.512 18.082 0.62 14.63  ? 101 SER B OG   1 
ATOM   4590 O  OG   B SER B 1 101 ? -6.755  -23.429 19.860 0.38 14.42  ? 101 SER B OG   1 
ATOM   4591 H  H    A SER B 1 101 ? -8.932  -25.118 19.929 0.62 16.46  ? 101 SER B H    1 
ATOM   4592 H  H    B SER B 1 101 ? -8.936  -25.120 19.945 0.38 16.46  ? 101 SER B H    1 
ATOM   4593 H  HA   A SER B 1 101 ? -9.205  -22.410 19.677 0.62 12.06  ? 101 SER B HA   1 
ATOM   4594 H  HA   B SER B 1 101 ? -9.125  -22.421 19.649 0.38 12.43  ? 101 SER B HA   1 
ATOM   4595 H  HB2  A SER B 1 101 ? -7.321  -22.546 18.270 0.62 13.77  ? 101 SER B HB2  1 
ATOM   4596 H  HB2  B SER B 1 101 ? -7.480  -24.256 18.219 0.38 13.78  ? 101 SER B HB2  1 
ATOM   4597 H  HB3  A SER B 1 101 ? -7.069  -23.319 19.639 0.62 13.77  ? 101 SER B HB3  1 
ATOM   4598 H  HB3  B SER B 1 101 ? -7.325  -22.673 18.127 0.38 13.78  ? 101 SER B HB3  1 
ATOM   4599 H  HG   A SER B 1 101 ? -7.317  -24.335 17.255 0.62 13.77  ? 101 SER B HG   1 
ATOM   4600 H  HG   B SER B 1 101 ? -6.174  -22.819 19.777 0.38 16.19  ? 101 SER B HG   1 
ATOM   4601 N  N    . GLN B 1 102 ? -9.751  -21.980 17.171 1.00 9.44   ? 102 GLN B N    1 
ATOM   4602 C  CA   . GLN B 1 102 ? -10.631 -21.682 16.044 1.00 9.46   ? 102 GLN B CA   1 
ATOM   4603 C  C    . GLN B 1 102 ? -10.457 -22.691 14.911 1.00 9.42   ? 102 GLN B C    1 
ATOM   4604 O  O    . GLN B 1 102 ? -11.420 -23.132 14.293 1.00 10.27  ? 102 GLN B O    1 
ATOM   4605 C  CB   . GLN B 1 102 ? -10.392 -20.250 15.572 1.00 10.07  ? 102 GLN B CB   1 
ATOM   4606 C  CG   . GLN B 1 102 ? -11.222 -19.878 14.376 1.00 10.07  ? 102 GLN B CG   1 
ATOM   4607 C  CD   . GLN B 1 102 ? -12.702 -19.872 14.635 1.00 10.06  ? 102 GLN B CD   1 
ATOM   4608 O  OE1  . GLN B 1 102 ? -13.168 -19.731 15.774 1.00 10.65  ? 102 GLN B OE1  1 
ATOM   4609 N  NE2  . GLN B 1 102 ? -13.450 -19.982 13.550 1.00 11.47  ? 102 GLN B NE2  1 
ATOM   4610 H  H    . GLN B 1 102 ? -9.097  -21.384 17.398 1.00 13.78  ? 102 GLN B H    1 
ATOM   4611 H  HA   . GLN B 1 102 ? -11.559 -21.747 16.368 1.00 11.45  ? 102 GLN B HA   1 
ATOM   4612 H  HB2  . GLN B 1 102 ? -10.594 -19.638 16.310 1.00 12.65  ? 102 GLN B HB2  1 
ATOM   4613 H  HB3  . GLN B 1 102 ? -9.444  -20.149 15.348 1.00 12.65  ? 102 GLN B HB3  1 
ATOM   4614 H  HG2  . GLN B 1 102 ? -10.954 -18.984 14.073 1.00 17.97  ? 102 GLN B HG2  1 
ATOM   4615 H  HG3  . GLN B 1 102 ? -11.031 -20.504 13.647 1.00 17.97  ? 102 GLN B HG3  1 
ATOM   4616 H  HE21 . GLN B 1 102 ? -13.079 -19.941 12.749 1.00 17.86  ? 102 GLN B HE21 1 
ATOM   4617 H  HE22 . GLN B 1 102 ? -14.323 -20.094 13.626 1.00 17.86  ? 102 GLN B HE22 1 
ATOM   4618 N  N    . ASP B 1 103 ? -9.204  -23.043 14.600 1.00 9.90   ? 103 ASP B N    1 
ATOM   4619 C  CA   . ASP B 1 103 ? -8.942  -24.011 13.553 1.00 10.32  ? 103 ASP B CA   1 
ATOM   4620 C  C    . ASP B 1 103 ? -9.515  -25.378 13.904 1.00 10.17  ? 103 ASP B C    1 
ATOM   4621 O  O    . ASP B 1 103 ? -10.008 -26.095 13.030 1.00 10.66  ? 103 ASP B O    1 
ATOM   4622 C  CB   . ASP B 1 103 ? -7.459  -24.155 13.199 1.00 11.22  ? 103 ASP B CB   1 
ATOM   4623 C  CG   . ASP B 1 103 ? -6.505  -24.456 14.334 1.00 12.00  ? 103 ASP B CG   1 
ATOM   4624 O  OD1  . ASP B 1 103 ? -6.801  -24.133 15.485 1.00 12.48  ? 103 ASP B OD1  1 
ATOM   4625 O  OD2  . ASP B 1 103 ? -5.394  -24.949 14.020 1.00 15.28  ? 103 ASP B OD2  1 
ATOM   4626 H  H    . ASP B 1 103 ? -8.500  -22.664 15.043 1.00 11.72  ? 103 ASP B H    1 
ATOM   4627 H  HA   . ASP B 1 103 ? -9.402  -23.697 12.741 1.00 18.23  ? 103 ASP B HA   1 
ATOM   4628 H  HB2  . ASP B 1 103 ? -7.369  -24.873 12.539 1.00 13.64  ? 103 ASP B HB2  1 
ATOM   4629 H  HB3  . ASP B 1 103 ? -7.163  -23.323 12.777 1.00 13.64  ? 103 ASP B HB3  1 
ATOM   4630 N  N    . GLU B 1 104 ? -9.422  -25.772 15.174 1.00 9.76   ? 104 GLU B N    1 
ATOM   4631 C  CA   . GLU B 1 104 ? -9.939  -27.053 15.609 1.00 10.25  ? 104 GLU B CA   1 
ATOM   4632 C  C    . GLU B 1 104 ? -11.443 -27.114 15.395 1.00 9.55   ? 104 GLU B C    1 
ATOM   4633 O  O    . GLU B 1 104 ? -11.960 -28.136 14.942 1.00 10.57  ? 104 GLU B O    1 
ATOM   4634 C  CB   . GLU B 1 104 ? -9.547  -27.269 17.065 1.00 10.49  ? 104 GLU B CB   1 
ATOM   4635 C  CG   . GLU B 1 104 ? -8.067  -27.522 17.258 1.00 11.91  ? 104 GLU B CG   1 
ATOM   4636 C  CD   . GLU B 1 104 ? -7.533  -27.510 18.675 1.00 11.90  ? 104 GLU B CD   1 
ATOM   4637 O  OE1  . GLU B 1 104 ? -8.182  -26.947 19.593 1.00 12.97  ? 104 GLU B OE1  1 
ATOM   4638 O  OE2  . GLU B 1 104 ? -6.425  -28.027 18.846 1.00 13.92  ? 104 GLU B OE2  1 
ATOM   4639 H  H    . GLU B 1 104 ? -9.019  -25.226 15.786 1.00 13.66  ? 104 GLU B H    1 
ATOM   4640 H  HA   . GLU B 1 104 ? -9.518  -27.756 15.062 1.00 12.95  ? 104 GLU B HA   1 
ATOM   4641 H  HB2  . GLU B 1 104 ? -9.807  -26.478 17.580 1.00 13.65  ? 104 GLU B HB2  1 
ATOM   4642 H  HB3  . GLU B 1 104 ? -10.049 -28.035 17.414 1.00 13.65  ? 104 GLU B HB3  1 
ATOM   4643 H  HG2  . GLU B 1 104 ? -7.851  -28.395 16.866 1.00 13.66  ? 104 GLU B HG2  1 
ATOM   4644 H  HG3  . GLU B 1 104 ? -7.570  -26.849 16.747 1.00 13.66  ? 104 GLU B HG3  1 
ATOM   4645 N  N    . ARG B 1 105 ? -12.151 -26.061 15.769 1.00 9.24   ? 105 ARG B N    1 
ATOM   4646 C  CA   . ARG B 1 105 ? -13.595 -26.044 15.591 1.00 9.44   ? 105 ARG B CA   1 
ATOM   4647 C  C    . ARG B 1 105 ? -13.975 -25.952 14.114 1.00 9.40   ? 105 ARG B C    1 
ATOM   4648 O  O    . ARG B 1 105 ? -14.925 -26.634 13.695 1.00 9.75   ? 105 ARG B O    1 
ATOM   4649 C  CB   . ARG B 1 105 ? -14.220 -24.924 16.413 1.00 9.27   ? 105 ARG B CB   1 
ATOM   4650 C  CG   . ARG B 1 105 ? -14.325 -25.304 17.871 1.00 9.56   ? 105 ARG B CG   1 
ATOM   4651 C  CD   . ARG B 1 105 ? -14.928 -24.235 18.786 1.00 9.03   ? 105 ARG B CD   1 
ATOM   4652 N  NE   . ARG B 1 105 ? -13.956 -23.240 19.202 1.00 9.44   ? 105 ARG B NE   1 
ATOM   4653 C  CZ   . ARG B 1 105 ? -13.672 -22.079 18.601 1.00 9.18   ? 105 ARG B CZ   1 
ATOM   4654 N  NH1  . ARG B 1 105 ? -14.424 -21.585 17.631 1.00 9.65   ? 105 ARG B NH1  1 
ATOM   4655 N  NH2  . ARG B 1 105 ? -12.613 -21.400 19.009 1.00 10.25  ? 105 ARG B NH2  1 
ATOM   4656 H  H    . ARG B 1 105 ? -11.738 -25.339 16.147 1.00 11.16  ? 105 ARG B H    1 
ATOM   4657 H  HA   . ARG B 1 105 ? -13.945 -26.899 15.935 1.00 14.42  ? 105 ARG B HA   1 
ATOM   4658 H  HB2  . ARG B 1 105 ? -13.672 -24.116 16.325 1.00 11.16  ? 105 ARG B HB2  1 
ATOM   4659 H  HB3  . ARG B 1 105 ? -15.115 -24.729 16.063 1.00 11.16  ? 105 ARG B HB3  1 
ATOM   4660 H  HG2  . ARG B 1 105 ? -14.869 -26.116 17.946 1.00 14.42  ? 105 ARG B HG2  1 
ATOM   4661 H  HG3  . ARG B 1 105 ? -13.428 -25.523 18.202 1.00 14.42  ? 105 ARG B HG3  1 
ATOM   4662 H  HD2  . ARG B 1 105 ? -15.664 -23.790 18.315 1.00 11.69  ? 105 ARG B HD2  1 
ATOM   4663 H  HD3  . ARG B 1 105 ? -15.303 -24.669 19.580 1.00 11.69  ? 105 ARG B HD3  1 
ATOM   4664 H  HE   . ARG B 1 105 ? -13.507 -23.418 19.929 1.00 11.70  ? 105 ARG B HE   1 
ATOM   4665 H  HH11 . ARG B 1 105 ? -15.302 -21.640 17.682 1.00 11.69  ? 105 ARG B HH11 1 
ATOM   4666 H  HH12 . ARG B 1 105 ? -14.043 -21.197 16.937 1.00 11.69  ? 105 ARG B HH12 1 
ATOM   4667 H  HH21 . ARG B 1 105 ? -12.021 -21.782 19.536 1.00 11.70  ? 105 ARG B HH21 1 
ATOM   4668 H  HH22 . ARG B 1 105 ? -12.501 -20.568 18.749 1.00 11.70  ? 105 ARG B HH22 1 
ATOM   4669 N  N    . ARG B 1 106 ? -13.296 -25.125 13.322 1.00 9.60   ? 106 ARG B N    1 
ATOM   4670 C  CA   . ARG B 1 106 ? -13.627 -25.061 11.907 1.00 9.76   ? 106 ARG B CA   1 
ATOM   4671 C  C    . ARG B 1 106 ? -13.450 -26.433 11.250 1.00 9.68   ? 106 ARG B C    1 
ATOM   4672 O  O    . ARG B 1 106 ? -14.217 -26.831 10.385 1.00 10.62  ? 106 ARG B O    1 
ATOM   4673 C  CB   . ARG B 1 106 ? -12.766 -24.005 11.214 1.00 10.62  ? 106 ARG B CB   1 
ATOM   4674 C  CG   . ARG B 1 106 ? -12.797 -24.046 9.694  1.00 10.92  ? 106 ARG B CG   1 
ATOM   4675 C  CD   . ARG B 1 106 ? -14.142 -23.722 9.042  1.00 11.54  ? 106 ARG B CD   1 
ATOM   4676 N  NE   . ARG B 1 106 ? -14.090 -24.074 7.643  1.00 11.54  ? 106 ARG B NE   1 
ATOM   4677 C  CZ   . ARG B 1 106 ? -14.937 -23.680 6.698  1.00 11.52  ? 106 ARG B CZ   1 
ATOM   4678 N  NH1  . ARG B 1 106 ? -15.861 -22.779 6.926  1.00 12.72  ? 106 ARG B NH1  1 
ATOM   4679 N  NH2  . ARG B 1 106 ? -14.867 -24.229 5.508  1.00 12.36  ? 106 ARG B NH2  1 
ATOM   4680 H  H    . ARG B 1 106 ? -12.630 -24.596 13.658 1.00 12.92  ? 106 ARG B H    1 
ATOM   4681 H  HA   . ARG B 1 106 ? -14.572 -24.797 11.826 1.00 11.79  ? 106 ARG B HA   1 
ATOM   4682 H  HB2  . ARG B 1 106 ? -13.067 -23.120 11.509 1.00 12.92  ? 106 ARG B HB2  1 
ATOM   4683 H  HB3  . ARG B 1 106 ? -11.839 -24.119 11.510 1.00 12.92  ? 106 ARG B HB3  1 
ATOM   4684 H  HG2  . ARG B 1 106 ? -12.133 -23.409 9.354  1.00 14.03  ? 106 ARG B HG2  1 
ATOM   4685 H  HG3  . ARG B 1 106 ? -12.517 -24.938 9.398  1.00 14.03  ? 106 ARG B HG3  1 
ATOM   4686 H  HD2  . ARG B 1 106 ? -14.857 -24.227 9.484  1.00 14.05  ? 106 ARG B HD2  1 
ATOM   4687 H  HD3  . ARG B 1 106 ? -14.334 -22.764 9.137  1.00 14.05  ? 106 ARG B HD3  1 
ATOM   4688 H  HE   . ARG B 1 106 ? -13.437 -24.595 7.390  1.00 14.03  ? 106 ARG B HE   1 
ATOM   4689 H  HH11 . ARG B 1 106 ? -16.350 -22.825 7.657  1.00 14.04  ? 106 ARG B HH11 1 
ATOM   4690 H  HH12 . ARG B 1 106 ? -15.994 -22.132 6.343  1.00 14.04  ? 106 ARG B HH12 1 
ATOM   4691 H  HH21 . ARG B 1 106 ? -14.499 -25.022 5.410  1.00 14.04  ? 106 ARG B HH21 1 
ATOM   4692 H  HH22 . ARG B 1 106 ? -15.190 -23.803 4.810  1.00 14.04  ? 106 ARG B HH22 1 
ATOM   4693 N  N    . LYS B 1 107 ? -12.377 -27.144 11.632 1.00 10.49  ? 107 LYS B N    1 
ATOM   4694 C  CA   . LYS B 1 107 ? -12.114 -28.463 11.057 1.00 11.10  ? 107 LYS B CA   1 
ATOM   4695 C  C    . LYS B 1 107 ? -13.282 -29.396 11.381 1.00 10.84  ? 107 LYS B C    1 
ATOM   4696 O  O    . LYS B 1 107 ? -13.750 -30.120 10.501 1.00 11.44  ? 107 LYS B O    1 
ATOM   4697 C  CB   . LYS B 1 107 ? -10.784 -29.029 11.561 1.00 11.98  ? 107 LYS B CB   1 
ATOM   4698 C  CG   . LYS B 1 107 ? -10.553 -30.468 11.116 1.00 14.54  ? 107 LYS B CG   1 
ATOM   4699 C  CD   . LYS B 1 107 ? -9.201  -31.012 11.491 1.00 17.78  ? 107 LYS B CD   1 
ATOM   4700 C  CE   . LYS B 1 107 ? -9.096  -32.451 11.039 1.00 22.09  ? 107 LYS B CE   1 
ATOM   4701 N  NZ   . LYS B 1 107 ? -7.758  -33.051 11.246 1.00 27.20  ? 107 LYS B NZ   1 
ATOM   4702 H  H    . LYS B 1 107 ? -11.798 -26.804 12.251 1.00 14.42  ? 107 LYS B H    1 
ATOM   4703 H  HA   . LYS B 1 107 ? -12.060 -28.364 10.079 1.00 18.06  ? 107 LYS B HA   1 
ATOM   4704 H  HB2  . LYS B 1 107 ? -10.053 -28.469 11.225 1.00 14.68  ? 107 LYS B HB2  1 
ATOM   4705 H  HB3  . LYS B 1 107 ? -10.773 -28.991 12.540 1.00 14.68  ? 107 LYS B HB3  1 
ATOM   4706 H  HG2  . LYS B 1 107 ? -11.244 -31.037 11.517 1.00 21.19  ? 107 LYS B HG2  1 
ATOM   4707 H  HG3  . LYS B 1 107 ? -10.656 -30.516 10.141 1.00 21.19  ? 107 LYS B HG3  1 
ATOM   4708 H  HD2  . LYS B 1 107 ? -8.498  -30.480 11.062 1.00 22.37  ? 107 LYS B HD2  1 
ATOM   4709 H  HD3  . LYS B 1 107 ? -9.083  -30.963 12.464 1.00 22.37  ? 107 LYS B HD3  1 
ATOM   4710 H  HE2  . LYS B 1 107 ? -9.753  -32.987 11.523 1.00 21.19  ? 107 LYS B HE2  1 
ATOM   4711 H  HE3  . LYS B 1 107 ? -9.316  -32.504 10.089 1.00 21.19  ? 107 LYS B HE3  1 
ATOM   4712 H  HZ1  . LYS B 1 107 ? -7.810  -33.954 11.170 1.00 27.02  ? 107 LYS B HZ1  1 
ATOM   4713 H  HZ2  . LYS B 1 107 ? -7.179  -32.734 10.623 1.00 27.02  ? 107 LYS B HZ2  1 
ATOM   4714 H  HZ3  . LYS B 1 107 ? -7.450  -32.840 12.072 1.00 27.02  ? 107 LYS B HZ3  1 
ATOM   4715 N  N    . ILE B 1 108 ? -13.726 -29.440 12.630 1.00 10.30  ? 108 ILE B N    1 
ATOM   4716 C  CA   . ILE B 1 108 ? -14.810 -30.326 12.987 1.00 10.31  ? 108 ILE B CA   1 
ATOM   4717 C  C    . ILE B 1 108 ? -16.080 -29.919 12.240 1.00 10.15  ? 108 ILE B C    1 
ATOM   4718 O  O    . ILE B 1 108 ? -16.802 -30.766 11.692 1.00 11.07  ? 108 ILE B O    1 
ATOM   4719 C  CB   . ILE B 1 108 ? -15.019 -30.323 14.509 1.00 10.63  ? 108 ILE B CB   1 
ATOM   4720 C  CG1  . ILE B 1 108 ? -13.834 -30.988 15.228 1.00 11.38  ? 108 ILE B CG1  1 
ATOM   4721 C  CG2  . ILE B 1 108 ? -16.332 -31.049 14.842 1.00 11.58  ? 108 ILE B CG2  1 
ATOM   4722 C  CD1  . ILE B 1 108 ? -13.703 -30.613 16.668 1.00 12.09  ? 108 ILE B CD1  1 
ATOM   4723 H  H    . ILE B 1 108 ? -13.347 -28.912 13.273 1.00 13.65  ? 108 ILE B H    1 
ATOM   4724 H  HA   . ILE B 1 108 ? -14.570 -31.230 12.716 1.00 12.63  ? 108 ILE B HA   1 
ATOM   4725 H  HB   . ILE B 1 108 ? -15.087 -29.385 14.815 1.00 13.65  ? 108 ILE B HB   1 
ATOM   4726 H  HG12 . ILE B 1 108 ? -13.936 -31.962 15.166 1.00 13.65  ? 108 ILE B HG12 1 
ATOM   4727 H  HG13 . ILE B 1 108 ? -13.005 -30.744 14.764 1.00 13.65  ? 108 ILE B HG13 1 
ATOM   4728 H  HG21 . ILE B 1 108 ? -16.297 -31.384 15.755 1.00 17.92  ? 108 ILE B HG21 1 
ATOM   4729 H  HG22 . ILE B 1 108 ? -17.079 -30.430 14.756 1.00 17.92  ? 108 ILE B HG22 1 
ATOM   4730 H  HG23 . ILE B 1 108 ? -16.459 -31.795 14.231 1.00 17.92  ? 108 ILE B HG23 1 
ATOM   4731 H  HD11 . ILE B 1 108 ? -12.894 -31.010 17.036 1.00 17.75  ? 108 ILE B HD11 1 
ATOM   4732 H  HD12 . ILE B 1 108 ? -13.652 -29.644 16.749 1.00 17.75  ? 108 ILE B HD12 1 
ATOM   4733 H  HD13 . ILE B 1 108 ? -14.475 -30.938 17.162 1.00 17.75  ? 108 ILE B HD13 1 
ATOM   4734 N  N    . PHE B 1 109 ? -16.397 -28.627 12.258 1.00 10.44  ? 109 PHE B N    1 
ATOM   4735 C  CA   . PHE B 1 109 ? -17.636 -28.092 11.705 1.00 10.34  ? 109 PHE B CA   1 
ATOM   4736 C  C    . PHE B 1 109 ? -17.781 -28.364 10.210 1.00 10.49  ? 109 PHE B C    1 
ATOM   4737 O  O    . PHE B 1 109 ? -18.843 -28.826 9.775  1.00 10.97  ? 109 PHE B O    1 
ATOM   4738 C  CB   . PHE B 1 109 ? -17.688 -26.607 12.043 1.00 11.12  ? 109 PHE B CB   1 
ATOM   4739 C  CG   . PHE B 1 109 ? -18.837 -25.875 11.407 1.00 10.98  ? 109 PHE B CG   1 
ATOM   4740 C  CD1  . PHE B 1 109 ? -20.130 -25.965 11.912 1.00 12.11  ? 109 PHE B CD1  1 
ATOM   4741 C  CD2  . PHE B 1 109 ? -18.600 -25.086 10.295 1.00 12.23  ? 109 PHE B CD2  1 
ATOM   4742 C  CE1  . PHE B 1 109 ? -21.176 -25.291 11.294 1.00 12.72  ? 109 PHE B CE1  1 
ATOM   4743 C  CE2  . PHE B 1 109 ? -19.647 -24.424 9.671  1.00 13.67  ? 109 PHE B CE2  1 
ATOM   4744 C  CZ   . PHE B 1 109 ? -20.916 -24.535 10.180 1.00 13.52  ? 109 PHE B CZ   1 
ATOM   4745 H  H    . PHE B 1 109 ? -15.810 -28.042 12.644 1.00 17.41  ? 109 PHE B H    1 
ATOM   4746 H  HA   . PHE B 1 109 ? -18.392 -28.537 12.167 1.00 12.39  ? 109 PHE B HA   1 
ATOM   4747 H  HB2  . PHE B 1 109 ? -17.751 -26.512 13.016 1.00 17.41  ? 109 PHE B HB2  1 
ATOM   4748 H  HB3  . PHE B 1 109 ? -16.848 -26.193 11.755 1.00 17.41  ? 109 PHE B HB3  1 
ATOM   4749 H  HD1  . PHE B 1 109 ? -20.299 -26.500 12.671 1.00 17.49  ? 109 PHE B HD1  1 
ATOM   4750 H  HD2  . PHE B 1 109 ? -17.728 -25.027 9.939  1.00 17.47  ? 109 PHE B HD2  1 
ATOM   4751 H  HE1  . PHE B 1 109 ? -22.054 -25.358 11.634 1.00 17.49  ? 109 PHE B HE1  1 
ATOM   4752 H  HE2  . PHE B 1 109 ? -19.485 -23.890 8.911  1.00 17.51  ? 109 PHE B HE2  1 
ATOM   4753 H  HZ   . PHE B 1 109 ? -21.622 -24.069 9.765  1.00 17.49  ? 109 PHE B HZ   1 
ATOM   4754 N  N    . GLU B 1 110 ? -16.760 -28.014 9.428  1.00 11.09  ? 110 GLU B N    1 
ATOM   4755 C  CA   . GLU B 1 110 ? -16.897 -28.082 7.986  1.00 11.67  ? 110 GLU B CA   1 
ATOM   4756 C  C    . GLU B 1 110 ? -16.023 -29.160 7.359  1.00 12.10  ? 110 GLU B C    1 
ATOM   4757 O  O    . GLU B 1 110 ? -16.532 -29.988 6.613  1.00 13.23  ? 110 GLU B O    1 
ATOM   4758 C  CB   . GLU B 1 110 ? -16.666 -26.742 7.292  1.00 12.72  ? 110 GLU B CB   1 
ATOM   4759 C  CG   . GLU B 1 110 ? -17.148 -26.762 5.846  1.00 13.53  ? 110 GLU B CG   1 
ATOM   4760 C  CD   . GLU B 1 110 ? -18.646 -27.045 5.700  1.00 13.03  ? 110 GLU B CD   1 
ATOM   4761 O  OE1  . GLU B 1 110 ? -19.373 -26.749 6.633  1.00 13.17  ? 110 GLU B OE1  1 
ATOM   4762 O  OE2  . GLU B 1 110 ? -19.085 -27.544 4.613  1.00 14.31  ? 110 GLU B OE2  1 
ATOM   4763 H  H    . GLU B 1 110 ? -15.973 -27.728 9.793  1.00 13.26  ? 110 GLU B H    1 
ATOM   4764 H  HA   . GLU B 1 110 ? -17.828 -28.340 7.806  1.00 14.01  ? 110 GLU B HA   1 
ATOM   4765 H  HB2  . GLU B 1 110 ? -17.142 -26.041 7.785  1.00 15.09  ? 110 GLU B HB2  1 
ATOM   4766 H  HB3  . GLU B 1 110 ? -15.709 -26.535 7.312  1.00 15.09  ? 110 GLU B HB3  1 
ATOM   4767 H  HG2  . GLU B 1 110 ? -16.954 -25.894 5.433  1.00 16.23  ? 110 GLU B HG2  1 
ATOM   4768 H  HG3  . GLU B 1 110 ? -16.651 -27.445 5.348  1.00 16.23  ? 110 GLU B HG3  1 
ATOM   4769 N  N    . GLU B 1 111 ? -14.710 -29.168 7.597  1.00 12.37  ? 111 GLU B N    1 
ATOM   4770 C  CA   . GLU B 1 111 ? -13.855 -30.122 6.897  1.00 13.43  ? 111 GLU B CA   1 
ATOM   4771 C  C    . GLU B 1 111 ? -14.293 -31.553 7.189  1.00 12.73  ? 111 GLU B C    1 
ATOM   4772 O  O    . GLU B 1 111 ? -14.307 -32.389 6.275  1.00 14.64  ? 111 GLU B O    1 
ATOM   4773 C  CB   . GLU B 1 111 ? -12.380 -29.864 7.221  1.00 15.98  ? 111 GLU B CB   1 
ATOM   4774 C  CG   . GLU B 1 111 ? -11.407 -30.961 6.810  1.00 21.57  ? 111 GLU B CG   1 
ATOM   4775 C  CD   . GLU B 1 111 ? -9.943  -30.822 7.235  1.00 24.06  ? 111 GLU B CD   1 
ATOM   4776 O  OE1  . GLU B 1 111 ? -9.513  -29.773 7.833  1.00 27.09  ? 111 GLU B OE1  1 
ATOM   4777 O  OE2  . GLU B 1 111 ? -9.225  -31.775 6.974  1.00 28.99  ? 111 GLU B OE2  1 
ATOM   4778 H  H    . GLU B 1 111 ? -14.342 -28.581 8.193  1.00 18.06  ? 111 GLU B H    1 
ATOM   4779 H  HA   . GLU B 1 111 ? -13.977 -29.968 5.932  1.00 16.34  ? 111 GLU B HA   1 
ATOM   4780 H  HB2  . GLU B 1 111 ? -12.112 -29.033 6.779  1.00 18.06  ? 111 GLU B HB2  1 
ATOM   4781 H  HB3  . GLU B 1 111 ? -12.300 -29.724 8.187  1.00 18.06  ? 111 GLU B HB3  1 
ATOM   4782 H  HG2  . GLU B 1 111 ? -11.736 -31.813 7.166  1.00 48.82  ? 111 GLU B HG2  1 
ATOM   4783 H  HG3  . GLU B 1 111 ? -11.427 -31.034 5.833  1.00 48.82  ? 111 GLU B HG3  1 
ATOM   4784 N  N    . GLN B 1 112 ? -14.577 -31.863 8.447  1.00 12.24  ? 112 GLN B N    1 
ATOM   4785 C  CA   . GLN B 1 112 ? -15.025 -33.187 8.847  1.00 12.24  ? 112 GLN B CA   1 
ATOM   4786 C  C    . GLN B 1 112 ? -16.526 -33.371 8.685  1.00 12.33  ? 112 GLN B C    1 
ATOM   4787 O  O    . GLN B 1 112 ? -16.982 -34.329 8.059  1.00 14.68  ? 112 GLN B O    1 
ATOM   4788 C  CB   . GLN B 1 112 ? -14.617 -33.538 10.279 1.00 12.91  ? 112 GLN B CB   1 
ATOM   4789 C  CG   . GLN B 1 112 ? -13.107 -33.626 10.448 1.00 13.62  ? 112 GLN B CG   1 
ATOM   4790 C  CD   . GLN B 1 112 ? -12.759 -33.945 11.870 1.00 14.28  ? 112 GLN B CD   1 
ATOM   4791 O  OE1  . GLN B 1 112 ? -12.635 -33.053 12.690 1.00 17.55  ? 112 GLN B OE1  1 
ATOM   4792 N  NE2  . GLN B 1 112 ? -12.710 -35.206 12.218 1.00 17.70  ? 112 GLN B NE2  1 
ATOM   4793 H  H    . GLN B 1 112 ? -14.482 -31.223 9.093  1.00 15.63  ? 112 GLN B H    1 
ATOM   4794 H  HA   . GLN B 1 112 ? -14.585 -33.835 8.250  1.00 14.81  ? 112 GLN B HA   1 
ATOM   4795 H  HB2  . GLN B 1 112 ? -14.971 -32.854 10.885 1.00 15.70  ? 112 GLN B HB2  1 
ATOM   4796 H  HB3  . GLN B 1 112 ? -15.020 -34.397 10.522 1.00 15.70  ? 112 GLN B HB3  1 
ATOM   4797 H  HG2  . GLN B 1 112 ? -12.751 -34.324 9.859  1.00 18.46  ? 112 GLN B HG2  1 
ATOM   4798 H  HG3  . GLN B 1 112 ? -12.697 -32.772 10.195 1.00 18.46  ? 112 GLN B HG3  1 
ATOM   4799 H  HE21 . GLN B 1 112 ? -13.096 -35.820 11.713 1.00 18.46  ? 112 GLN B HE21 1 
ATOM   4800 H  HE22 . GLN B 1 112 ? -12.290 -35.444 12.959 1.00 18.46  ? 112 GLN B HE22 1 
ATOM   4801 N  N    . SER B 1 113 ? -17.326 -32.471 9.259  1.00 11.30  ? 113 SER B N    1 
ATOM   4802 C  CA   . SER B 1 113 ? -18.759 -32.685 9.346  1.00 11.51  ? 113 SER B CA   1 
ATOM   4803 C  C    . SER B 1 113 ? -19.517 -32.212 8.115  1.00 11.80  ? 113 SER B C    1 
ATOM   4804 O  O    . SER B 1 113 ? -20.673 -32.620 7.921  1.00 12.41  ? 113 SER B O    1 
ATOM   4805 C  CB   . SER B 1 113 ? -19.332 -32.036 10.588 1.00 11.56  ? 113 SER B CB   1 
ATOM   4806 O  OG   . SER B 1 113 ? -18.779 -32.625 11.756 1.00 12.06  ? 113 SER B OG   1 
ATOM   4807 H  H    . SER B 1 113 ? -16.971 -31.704 9.607  1.00 14.73  ? 113 SER B H    1 
ATOM   4808 H  HA   . SER B 1 113 ? -18.908 -33.665 9.426  1.00 17.64  ? 113 SER B HA   1 
ATOM   4809 H  HB2  . SER B 1 113 ? -19.132 -31.076 10.578 1.00 15.95  ? 113 SER B HB2  1 
ATOM   4810 H  HB3  . SER B 1 113 ? -20.310 -32.145 10.595 1.00 15.95  ? 113 SER B HB3  1 
ATOM   4811 H  HG   . SER B 1 113 ? -18.019 -32.281 11.895 1.00 15.30  ? 113 SER B HG   1 
ATOM   4812 N  N    . ARG B 1 114 ? -18.921 -31.318 7.333  1.00 11.59  ? 114 ARG B N    1 
ATOM   4813 C  CA   . ARG B 1 114 ? -19.527 -30.836 6.103  1.00 12.77  ? 114 ARG B CA   1 
ATOM   4814 C  C    . ARG B 1 114 ? -20.863 -30.146 6.353  1.00 11.60  ? 114 ARG B C    1 
ATOM   4815 O  O    . ARG B 1 114 ? -21.769 -30.223 5.531  1.00 12.02  ? 114 ARG B O    1 
ATOM   4816 C  CB   . ARG B 1 114 ? -19.657 -31.991 5.108  1.00 14.79  ? 114 ARG B CB   1 
ATOM   4817 C  CG   . ARG B 1 114 ? -18.356 -32.777 4.901  1.00 18.60  ? 114 ARG B CG   1 
ATOM   4818 C  CD   . ARG B 1 114 ? -18.052 -33.120 3.469  1.00 23.21  ? 114 ARG B CD   1 
ATOM   4819 N  NE   . ARG B 1 114 ? -17.804 -31.947 2.635  1.00 25.41  ? 114 ARG B NE   1 
ATOM   4820 C  CZ   . ARG B 1 114 ? -17.773 -32.009 1.302  1.00 28.82  ? 114 ARG B CZ   1 
ATOM   4821 N  NH1  . ARG B 1 114 ? -17.853 -33.178 0.687  1.00 32.62  ? 114 ARG B NH1  1 
ATOM   4822 N  NH2  . ARG B 1 114 ? -17.699 -30.905 0.581  1.00 34.61  ? 114 ARG B NH2  1 
ATOM   4823 H  H    . ARG B 1 114 ? -18.105 -30.987 7.575  1.00 13.99  ? 114 ARG B H    1 
ATOM   4824 H  HA   . ARG B 1 114 ? -18.916 -30.169 5.714  1.00 15.73  ? 114 ARG B HA   1 
ATOM   4825 H  HB2  . ARG B 1 114 ? -20.352 -32.604 5.424  1.00 18.27  ? 114 ARG B HB2  1 
ATOM   4826 H  HB3  . ARG B 1 114 ? -19.947 -31.628 4.245  1.00 18.27  ? 114 ARG B HB3  1 
ATOM   4827 H  HG2  . ARG B 1 114 ? -17.608 -32.252 5.259  1.00 21.10  ? 114 ARG B HG2  1 
ATOM   4828 H  HG3  . ARG B 1 114 ? -18.405 -33.610 5.417  1.00 21.10  ? 114 ARG B HG3  1 
ATOM   4829 H  HD2  . ARG B 1 114 ? -17.263 -33.702 3.441  1.00 28.64  ? 114 ARG B HD2  1 
ATOM   4830 H  HD3  . ARG B 1 114 ? -18.807 -33.623 3.096  1.00 28.64  ? 114 ARG B HD3  1 
ATOM   4831 H  HE   . ARG B 1 114 ? -17.670 -31.177 3.021  1.00 29.53  ? 114 ARG B HE   1 
ATOM   4832 H  HH11 . ARG B 1 114 ? -17.244 -33.797 0.839  1.00 29.26  ? 114 ARG B HH11 1 
ATOM   4833 H  HH12 . ARG B 1 114 ? -18.513 -33.333 0.124  1.00 29.26  ? 114 ARG B HH12 1 
ATOM   4834 H  HH21 . ARG B 1 114 ? -17.941 -30.136 0.931  1.00 29.53  ? 114 ARG B HH21 1 
ATOM   4835 H  HH22 . ARG B 1 114 ? -17.407 -30.942 -0.248 1.00 29.53  ? 114 ARG B HH22 1 
ATOM   4836 N  N    . HIS B 1 115 ? -20.984 -29.400 7.453  1.00 11.27  ? 115 HIS B N    1 
ATOM   4837 C  CA   . HIS B 1 115 ? -22.256 -28.806 7.841  1.00 10.73  ? 115 HIS B CA   1 
ATOM   4838 C  C    . HIS B 1 115 ? -22.880 -27.967 6.734  1.00 11.35  ? 115 HIS B C    1 
ATOM   4839 O  O    . HIS B 1 115 ? -24.057 -28.144 6.396  1.00 11.88  ? 115 HIS B O    1 
ATOM   4840 C  CB   . HIS B 1 115 ? -22.034 -27.972 9.102  1.00 10.92  ? 115 HIS B CB   1 
ATOM   4841 C  CG   . HIS B 1 115 ? -23.289 -27.422 9.695  1.00 10.34  ? 115 HIS B CG   1 
ATOM   4842 N  ND1  . HIS B 1 115 ? -23.816 -27.959 10.832 1.00 13.91  ? 115 HIS B ND1  1 
ATOM   4843 C  CD2  . HIS B 1 115 ? -24.127 -26.411 9.379  1.00 10.49  ? 115 HIS B CD2  1 
ATOM   4844 C  CE1  . HIS B 1 115 ? -24.878 -27.239 11.177 1.00 13.21  ? 115 HIS B CE1  1 
ATOM   4845 N  NE2  . HIS B 1 115 ? -25.106 -26.282 10.330 1.00 10.07  ? 115 HIS B NE2  1 
ATOM   4846 H  H    . HIS B 1 115 ? -20.249 -29.248 7.975  1.00 13.15  ? 115 HIS B H    1 
ATOM   4847 H  HA   . HIS B 1 115 ? -22.878 -29.543 8.057  1.00 12.95  ? 115 HIS B HA   1 
ATOM   4848 H  HB2  . HIS B 1 115 ? -21.585 -28.531 9.773  1.00 13.15  ? 115 HIS B HB2  1 
ATOM   4849 H  HB3  . HIS B 1 115 ? -21.432 -27.227 8.884  1.00 13.15  ? 115 HIS B HB3  1 
ATOM   4850 H  HD1  . HIS B 1 115 ? -23.474 -28.628 11.292 1.00 18.08  ? 115 HIS B HD1  1 
ATOM   4851 H  HD2  . HIS B 1 115 ? -24.021 -25.831 8.651  1.00 18.08  ? 115 HIS B HD2  1 
ATOM   4852 H  HE1  . HIS B 1 115 ? -25.412 -27.436 11.927 1.00 18.08  ? 115 HIS B HE1  1 
ATOM   4853 N  N    . ILE B 1 116 ? -22.096 -27.022 6.200  1.00 11.57  ? 116 ILE B N    1 
ATOM   4854 C  CA   . ILE B 1 116 ? -22.626 -26.115 5.188  1.00 12.80  ? 116 ILE B CA   1 
ATOM   4855 C  C    . ILE B 1 116 ? -22.893 -26.865 3.889  1.00 13.53  ? 116 ILE B C    1 
ATOM   4856 O  O    . ILE B 1 116 ? -23.912 -26.662 3.212  1.00 13.57  ? 116 ILE B O    1 
ATOM   4857 C  CB   . ILE B 1 116 ? -21.681 -24.917 4.978  1.00 13.56  ? 116 ILE B CB   1 
ATOM   4858 C  CG1  . ILE B 1 116 ? -21.482 -24.138 6.274  1.00 14.32  ? 116 ILE B CG1  1 
ATOM   4859 C  CG2  . ILE B 1 116 ? -22.187 -24.026 3.841  1.00 16.10  ? 116 ILE B CG2  1 
ATOM   4860 C  CD1  . ILE B 1 116 ? -20.392 -23.101 6.213  1.00 15.37  ? 116 ILE B CD1  1 
ATOM   4861 H  H    . ILE B 1 116 ? -21.225 -26.943 6.465  1.00 17.03  ? 116 ILE B H    1 
ATOM   4862 H  HA   . ILE B 1 116 ? -23.476 -25.768 5.514  1.00 15.45  ? 116 ILE B HA   1 
ATOM   4863 H  HB   . ILE B 1 116 ? -20.800 -25.276 4.708  1.00 16.72  ? 116 ILE B HB   1 
ATOM   4864 H  HG12 . ILE B 1 116 ? -22.325 -23.696 6.504  1.00 17.03  ? 116 ILE B HG12 1 
ATOM   4865 H  HG13 . ILE B 1 116 ? -21.270 -24.769 6.993  1.00 17.03  ? 116 ILE B HG13 1 
ATOM   4866 H  HG21 . ILE B 1 116 ? -21.766 -23.151 3.894  1.00 17.62  ? 116 ILE B HG21 1 
ATOM   4867 H  HG22 . ILE B 1 116 ? -21.970 -24.434 2.984  1.00 17.62  ? 116 ILE B HG22 1 
ATOM   4868 H  HG23 . ILE B 1 116 ? -23.152 -23.923 3.913  1.00 17.62  ? 116 ILE B HG23 1 
ATOM   4869 H  HD11 . ILE B 1 116 ? -20.195 -22.783 7.110  1.00 17.57  ? 116 ILE B HD11 1 
ATOM   4870 H  HD12 . ILE B 1 116 ? -19.590 -23.493 5.826  1.00 17.57  ? 116 ILE B HD12 1 
ATOM   4871 H  HD13 . ILE B 1 116 ? -20.684 -22.353 5.664  1.00 17.57  ? 116 ILE B HD13 1 
ATOM   4872 N  N    . HIS B 1 117 ? -21.944 -27.716 3.501  1.00 14.04  ? 117 HIS B N    1 
ATOM   4873 C  CA   . HIS B 1 117 ? -22.102 -28.544 2.321  1.00 14.70  ? 117 HIS B CA   1 
ATOM   4874 C  C    . HIS B 1 117 ? -23.397 -29.343 2.365  1.00 14.29  ? 117 HIS B C    1 
ATOM   4875 O  O    . HIS B 1 117 ? -24.109 -29.438 1.356  1.00 16.05  ? 117 HIS B O    1 
ATOM   4876 C  CB   . HIS B 1 117 ? -20.873 -29.436 2.191  1.00 15.79  ? 117 HIS B CB   1 
ATOM   4877 C  CG   . HIS B 1 117 ? -20.988 -30.441 1.125  1.00 18.71  ? 117 HIS B CG   1 
ATOM   4878 N  ND1  . HIS B 1 117 ? -20.768 -30.158 -0.206 1.00 21.64  ? 117 HIS B ND1  1 
ATOM   4879 C  CD2  . HIS B 1 117 ? -21.303 -31.727 1.196  1.00 19.94  ? 117 HIS B CD2  1 
ATOM   4880 C  CE1  . HIS B 1 117 ? -20.958 -31.257 -0.917 1.00 23.18  ? 117 HIS B CE1  1 
ATOM   4881 N  NE2  . HIS B 1 117 ? -21.294 -32.227 -0.088 1.00 23.20  ? 117 HIS B NE2  1 
ATOM   4882 H  H    . HIS B 1 117 ? -21.169 -27.777 3.982  1.00 18.27  ? 117 HIS B H    1 
ATOM   4883 H  HA   . HIS B 1 117 ? -22.137 -27.944 1.536  1.00 17.48  ? 117 HIS B HA   1 
ATOM   4884 H  HB2  . HIS B 1 117 ? -20.091 -28.869 2.013  1.00 18.27  ? 117 HIS B HB2  1 
ATOM   4885 H  HB3  . HIS B 1 117 ? -20.725 -29.893 3.046  1.00 18.27  ? 117 HIS B HB3  1 
ATOM   4886 H  HD2  . HIS B 1 117 ? -21.515 -32.210 1.971  1.00 23.91  ? 117 HIS B HD2  1 
ATOM   4887 H  HE1  . HIS B 1 117 ? -20.870 -31.332 -1.852 1.00 23.91  ? 117 HIS B HE1  1 
ATOM   4888 H  HE2  . HIS B 1 117 ? -21.462 -33.057 -0.316 1.00 23.91  ? 117 HIS B HE2  1 
ATOM   4889 N  N    . ILE B 1 118 ? -23.679 -29.965 3.509  1.00 13.14  ? 118 ILE B N    1 
ATOM   4890 C  CA   . ILE B 1 118 ? -24.915 -30.699 3.687  1.00 13.39  ? 118 ILE B CA   1 
ATOM   4891 C  C    . ILE B 1 118 ? -26.111 -29.761 3.651  1.00 12.52  ? 118 ILE B C    1 
ATOM   4892 O  O    . ILE B 1 118 ? -27.085 -30.024 2.951  1.00 13.28  ? 118 ILE B O    1 
ATOM   4893 C  CB   . ILE B 1 118 ? -24.845 -31.566 4.965  1.00 13.49  ? 118 ILE B CB   1 
ATOM   4894 C  CG1  . ILE B 1 118 ? -23.813 -32.683 4.818  1.00 14.26  ? 118 ILE B CG1  1 
ATOM   4895 C  CG2  . ILE B 1 118 ? -26.205 -32.121 5.329  1.00 15.10  ? 118 ILE B CG2  1 
ATOM   4896 C  CD1  . ILE B 1 118 ? -23.490 -33.368 6.099  1.00 16.12  ? 118 ILE B CD1  1 
ATOM   4897 H  H    . ILE B 1 118 ? -23.080 -29.934 4.199  1.00 18.09  ? 118 ILE B H    1 
ATOM   4898 H  HA   . ILE B 1 118 ? -25.001 -31.309 2.933  1.00 15.88  ? 118 ILE B HA   1 
ATOM   4899 H  HB   . ILE B 1 118 ? -24.550 -30.981 5.706  1.00 18.11  ? 118 ILE B HB   1 
ATOM   4900 H  HG12 . ILE B 1 118 ? -24.156 -33.347 4.183  1.00 18.08  ? 118 ILE B HG12 1 
ATOM   4901 H  HG13 . ILE B 1 118 ? -22.988 -32.307 4.445  1.00 18.08  ? 118 ILE B HG13 1 
ATOM   4902 H  HG21 . ILE B 1 118 ? -26.103 -32.857 5.957  1.00 18.13  ? 118 ILE B HG21 1 
ATOM   4903 H  HG22 . ILE B 1 118 ? -26.744 -31.423 5.740  1.00 18.13  ? 118 ILE B HG22 1 
ATOM   4904 H  HG23 . ILE B 1 118 ? -26.651 -32.444 4.527  1.00 18.13  ? 118 ILE B HG23 1 
ATOM   4905 H  HD11 . ILE B 1 118 ? -22.629 -33.814 6.021  1.00 18.12  ? 118 ILE B HD11 1 
ATOM   4906 H  HD12 . ILE B 1 118 ? -23.451 -32.715 6.818  1.00 18.12  ? 118 ILE B HD12 1 
ATOM   4907 H  HD13 . ILE B 1 118 ? -24.177 -34.028 6.298  1.00 18.12  ? 118 ILE B HD13 1 
ATOM   4908 N  N    . GLY B 1 119 ? -26.070 -28.709 4.457  1.00 11.99  ? 119 GLY B N    1 
ATOM   4909 C  CA   . GLY B 1 119 ? -27.206 -27.814 4.515  1.00 12.34  ? 119 GLY B CA   1 
ATOM   4910 C  C    . GLY B 1 119 ? -27.621 -27.265 3.158  1.00 13.02  ? 119 GLY B C    1 
ATOM   4911 O  O    . GLY B 1 119 ? -28.811 -27.100 2.880  1.00 13.55  ? 119 GLY B O    1 
ATOM   4912 H  H    . GLY B 1 119 ? -25.336 -28.545 4.977  1.00 14.41  ? 119 GLY B H    1 
ATOM   4913 H  HA2  . GLY B 1 119 ? -27.971 -28.299 4.915  1.00 14.71  ? 119 GLY B HA2  1 
ATOM   4914 H  HA3  . GLY B 1 119 ? -26.983 -27.061 5.114  1.00 14.71  ? 119 GLY B HA3  1 
ATOM   4915 N  N    . LEU B 1 120 ? -26.619 -26.927 2.324  1.00 13.40  ? 120 LEU B N    1 
ATOM   4916 C  CA   . LEU B 1 120 ? -26.879 -26.383 0.996  1.00 14.97  ? 120 LEU B CA   1 
ATOM   4917 C  C    . LEU B 1 120 ? -27.779 -27.307 0.194  1.00 14.99  ? 120 LEU B C    1 
ATOM   4918 O  O    . LEU B 1 120 ? -28.497 -26.837 -0.699 1.00 16.89  ? 120 LEU B O    1 
ATOM   4919 C  CB   . LEU B 1 120 ? -25.574 -26.127 0.239  1.00 15.91  ? 120 LEU B CB   1 
ATOM   4920 C  CG   . LEU B 1 120 ? -24.869 -24.818 0.605  1.00 17.32  ? 120 LEU B CG   1 
ATOM   4921 C  CD1  . LEU B 1 120 ? -23.413 -24.842 0.171  1.00 19.43  ? 120 LEU B CD1  1 
ATOM   4922 C  CD2  . LEU B 1 120 ? -25.572 -23.604 -0.000 1.00 20.48  ? 120 LEU B CD2  1 
ATOM   4923 H  H    . LEU B 1 120 ? -25.752 -27.032 2.596  1.00 41.98  ? 120 LEU B H    1 
ATOM   4924 H  HA   . LEU B 1 120 ? -27.350 -25.527 1.112  1.00 22.84  ? 120 LEU B HA   1 
ATOM   4925 H  HB2  . LEU B 1 120 ? -24.963 -26.871 0.414  1.00 42.00  ? 120 LEU B HB2  1 
ATOM   4926 H  HB3  . LEU B 1 120 ? -25.766 -26.120 -0.719 1.00 41.98  ? 120 LEU B HB3  1 
ATOM   4927 H  HG   . LEU B 1 120 ? -24.892 -24.724 1.589  1.00 20.65  ? 120 LEU B HG   1 
ATOM   4928 H  HD11 . LEU B 1 120 ? -22.968 -24.033 0.478  1.00 43.31  ? 120 LEU B HD11 1 
ATOM   4929 H  HD12 . LEU B 1 120 ? -22.972 -25.620 0.554  1.00 43.29  ? 120 LEU B HD12 1 
ATOM   4930 H  HD13 . LEU B 1 120 ? -23.366 -24.888 -0.799 1.00 43.37  ? 120 LEU B HD13 1 
ATOM   4931 H  HD21 . LEU B 1 120 ? -25.049 -22.803 0.180  1.00 22.84  ? 120 LEU B HD21 1 
ATOM   4932 H  HD22 . LEU B 1 120 ? -25.658 -23.725 -0.962 1.00 22.84  ? 120 LEU B HD22 1 
ATOM   4933 H  HD23 . LEU B 1 120 ? -26.456 -23.509 0.395  1.00 22.84  ? 120 LEU B HD23 1 
ATOM   4934 N  N    . GLN B 1 121 ? -27.706 -28.621 0.459  1.00 15.10  ? 121 GLN B N    1 
ATOM   4935 C  CA   . GLN B 1 121 ? -28.500 -29.580 -0.299 1.00 16.78  ? 121 GLN B CA   1 
ATOM   4936 C  C    . GLN B 1 121 ? -29.990 -29.516 0.023  1.00 16.84  ? 121 GLN B C    1 
ATOM   4937 O  O    . GLN B 1 121 ? -30.787 -30.145 -0.663 1.00 19.41  ? 121 GLN B O    1 
ATOM   4938 C  CB   . GLN B 1 121 ? -27.985 -30.993 -0.062 1.00 18.44  ? 121 GLN B CB   1 
ATOM   4939 C  CG   . GLN B 1 121 ? -26.528 -31.188 -0.467 1.00 21.09  ? 121 GLN B CG   1 
ATOM   4940 C  CD   . GLN B 1 121 ? -26.003 -32.532 -0.020 1.00 24.48  ? 121 GLN B CD   1 
ATOM   4941 O  OE1  . GLN B 1 121 ? -26.647 -33.567 -0.173 1.00 30.90  ? 121 GLN B OE1  1 
ATOM   4942 N  NE2  . GLN B 1 121 ? -24.811 -32.522 0.535  1.00 28.92  ? 121 GLN B NE2  1 
ATOM   4943 H  H    . GLN B 1 121 ? -27.145 -28.926 1.112  1.00 27.43  ? 121 GLN B H    1 
ATOM   4944 H  HA   . GLN B 1 121 ? -28.387 -29.372 -1.256 1.00 19.82  ? 121 GLN B HA   1 
ATOM   4945 H  HB2  . GLN B 1 121 ? -28.086 -31.207 0.889  1.00 22.40  ? 121 GLN B HB2  1 
ATOM   4946 H  HB3  . GLN B 1 121 ? -28.544 -31.618 -0.570 1.00 22.40  ? 121 GLN B HB3  1 
ATOM   4947 H  HG2  . GLN B 1 121 ? -26.451 -31.120 -1.443 1.00 27.43  ? 121 GLN B HG2  1 
ATOM   4948 H  HG3  . GLN B 1 121 ? -25.981 -30.479 -0.071 1.00 27.43  ? 121 GLN B HG3  1 
ATOM   4949 H  HE21 . GLN B 1 121 ? -24.206 -31.931 0.277  1.00 27.43  ? 121 GLN B HE21 1 
ATOM   4950 H  HE22 . GLN B 1 121 ? -24.612 -33.110 1.165  1.00 27.43  ? 121 GLN B HE22 1 
ATOM   4951 N  N    . TYR B 1 122 ? -30.377 -28.752 1.052  1.00 14.71  ? 122 TYR B N    1 
ATOM   4952 C  CA   . TYR B 1 122 ? -31.758 -28.645 1.510  1.00 14.07  ? 122 TYR B CA   1 
ATOM   4953 C  C    . TYR B 1 122 ? -32.310 -27.237 1.318  1.00 14.27  ? 122 TYR B C    1 
ATOM   4954 O  O    . TYR B 1 122 ? -33.330 -26.879 1.898  1.00 14.54  ? 122 TYR B O    1 
ATOM   4955 C  CB   . TYR B 1 122 ? -31.864 -29.114 2.964  1.00 14.53  ? 122 TYR B CB   1 
ATOM   4956 C  CG   . TYR B 1 122 ? -31.503 -30.568 3.124  1.00 13.66  ? 122 TYR B CG   1 
ATOM   4957 C  CD1  . TYR B 1 122 ? -30.185 -30.964 3.306  1.00 14.10  ? 122 TYR B CD1  1 
ATOM   4958 C  CD2  . TYR B 1 122 ? -32.464 -31.557 2.998  1.00 14.46  ? 122 TYR B CD2  1 
ATOM   4959 C  CE1  . TYR B 1 122 ? -29.836 -32.303 3.392  1.00 14.22  ? 122 TYR B CE1  1 
ATOM   4960 C  CE2  . TYR B 1 122 ? -32.142 -32.888 3.088  1.00 14.83  ? 122 TYR B CE2  1 
ATOM   4961 C  CZ   . TYR B 1 122 ? -30.827 -33.264 3.270  1.00 15.05  ? 122 TYR B CZ   1 
ATOM   4962 O  OH   . TYR B 1 122 ? -30.534 -34.593 3.416  1.00 17.27  ? 122 TYR B OH   1 
ATOM   4963 H  H    . TYR B 1 122 ? -29.741 -28.284 1.510  1.00 17.65  ? 122 TYR B H    1 
ATOM   4964 H  HA   . TYR B 1 122 ? -32.310 -29.255 0.958  1.00 17.13  ? 122 TYR B HA   1 
ATOM   4965 H  HB2  . TYR B 1 122 ? -31.265 -28.570 3.516  1.00 17.42  ? 122 TYR B HB2  1 
ATOM   4966 H  HB3  . TYR B 1 122 ? -32.781 -28.974 3.278  1.00 17.42  ? 122 TYR B HB3  1 
ATOM   4967 H  HD1  . TYR B 1 122 ? -29.512 -30.308 3.369  1.00 17.83  ? 122 TYR B HD1  1 
ATOM   4968 H  HD2  . TYR B 1 122 ? -33.363 -31.311 2.854  1.00 17.83  ? 122 TYR B HD2  1 
ATOM   4969 H  HE1  . TYR B 1 122 ? -28.941 -32.557 3.543  1.00 17.83  ? 122 TYR B HE1  1 
ATOM   4970 H  HE2  . TYR B 1 122 ? -32.816 -33.544 3.024  1.00 17.83  ? 122 TYR B HE2  1 
ATOM   4971 H  HH   . TYR B 1 122 ? -29.779 -34.900 3.138  1.00 17.83  ? 122 TYR B HH   1 
ATOM   4972 N  N    . LEU B 1 123 ? -31.629 -26.455 0.479  1.00 14.49  ? 123 LEU B N    1 
ATOM   4973 C  CA   . LEU B 1 123 ? -32.100 -25.157 0.052  1.00 14.92  ? 123 LEU B CA   1 
ATOM   4974 C  C    . LEU B 1 123 ? -32.550 -25.305 -1.390 1.00 16.00  ? 123 LEU B C    1 
ATOM   4975 O  O    . LEU B 1 123 ? -31.855 -25.953 -2.183 1.00 17.92  ? 123 LEU B O    1 
ATOM   4976 C  CB   . LEU B 1 123 ? -30.972 -24.127 0.112  1.00 15.46  ? 123 LEU B CB   1 
ATOM   4977 C  CG   . LEU B 1 123 ? -30.168 -24.078 1.397  1.00 19.65  ? 123 LEU B CG   1 
ATOM   4978 C  CD1  . LEU B 1 123 ? -29.304 -22.853 1.516  1.00 18.98  ? 123 LEU B CD1  1 
ATOM   4979 C  CD2  . LEU B 1 123 ? -31.021 -24.155 2.622  1.00 19.11  ? 123 LEU B CD2  1 
ATOM   4980 H  H    . LEU B 1 123 ? -30.827 -26.748 0.154  1.00 17.65  ? 123 LEU B H    1 
ATOM   4981 H  HA   . LEU B 1 123 ? -32.856 -24.876 0.615  1.00 16.30  ? 123 LEU B HA   1 
ATOM   4982 H  HB2  . LEU B 1 123 ? -30.356 -24.306 -0.626 1.00 18.75  ? 123 LEU B HB2  1 
ATOM   4983 H  HB3  . LEU B 1 123 ? -31.359 -23.242 -0.040 1.00 18.75  ? 123 LEU B HB3  1 
ATOM   4984 H  HG   . LEU B 1 123 ? -29.569 -24.865 1.402  1.00 22.84  ? 123 LEU B HG   1 
ATOM   4985 H  HD11 . LEU B 1 123 ? -28.660 -22.978 2.234  1.00 17.71  ? 123 LEU B HD11 1 
ATOM   4986 H  HD12 . LEU B 1 123 ? -28.830 -22.707 0.678  1.00 17.70  ? 123 LEU B HD12 1 
ATOM   4987 H  HD13 . LEU B 1 123 ? -29.861 -22.080 1.712  1.00 17.69  ? 123 LEU B HD13 1 
ATOM   4988 H  HD21 . LEU B 1 123 ? -30.513 -23.848 3.394  1.00 18.27  ? 123 LEU B HD21 1 
ATOM   4989 H  HD22 . LEU B 1 123 ? -31.805 -23.592 2.507  1.00 18.27  ? 123 LEU B HD22 1 
ATOM   4990 H  HD23 . LEU B 1 123 ? -31.301 -25.075 2.767  1.00 18.27  ? 123 LEU B HD23 1 
ATOM   4991 N  N    . PRO B 1 124 ? -33.634 -24.643 -1.838 1.00 15.89  ? 124 PRO B N    1 
ATOM   4992 C  CA   . PRO B 1 124 ? -34.363 -23.631 -1.075 1.00 15.41  ? 124 PRO B CA   1 
ATOM   4993 C  C    . PRO B 1 124 ? -35.476 -24.140 -0.157 1.00 14.30  ? 124 PRO B C    1 
ATOM   4994 O  O    . PRO B 1 124 ? -36.224 -23.336 0.386  1.00 15.94  ? 124 PRO B O    1 
ATOM   4995 C  CB   . PRO B 1 124 ? -34.970 -22.786 -2.203 1.00 18.06  ? 124 PRO B CB   1 
ATOM   4996 C  CG   . PRO B 1 124 ? -35.311 -23.829 -3.245 1.00 18.50  ? 124 PRO B CG   1 
ATOM   4997 C  CD   . PRO B 1 124 ? -34.088 -24.714 -3.247 1.00 17.18  ? 124 PRO B CD   1 
ATOM   4998 H  HA   . PRO B 1 124 ? -33.721 -23.079 -0.561 1.00 16.30  ? 124 PRO B HA   1 
ATOM   4999 H  HB2  . PRO B 1 124 ? -35.773 -22.309 -1.903 1.00 30.57  ? 124 PRO B HB2  1 
ATOM   5000 H  HB3  . PRO B 1 124 ? -34.322 -22.138 -2.551 1.00 30.58  ? 124 PRO B HB3  1 
ATOM   5001 H  HG2  . PRO B 1 124 ? -36.111 -24.333 -2.992 1.00 21.00  ? 124 PRO B HG2  1 
ATOM   5002 H  HG3  . PRO B 1 124 ? -35.452 -23.419 -4.123 1.00 21.00  ? 124 PRO B HG3  1 
ATOM   5003 H  HD2  . PRO B 1 124 ? -34.313 -25.628 -3.499 1.00 20.03  ? 124 PRO B HD2  1 
ATOM   5004 H  HD3  . PRO B 1 124 ? -33.406 -24.372 -3.854 1.00 20.03  ? 124 PRO B HD3  1 
ATOM   5005 N  N    . ALA B 1 125 ? -35.604 -25.459 0.063  1.00 14.44  ? 125 ALA B N    1 
ATOM   5006 C  CA   . ALA B 1 125 ? -36.695 -25.946 0.894  1.00 14.24  ? 125 ALA B CA   1 
ATOM   5007 C  C    . ALA B 1 125 ? -36.692 -25.301 2.284  1.00 13.62  ? 125 ALA B C    1 
ATOM   5008 O  O    . ALA B 1 125 ? -37.746 -24.901 2.775  1.00 14.07  ? 125 ALA B O    1 
ATOM   5009 C  CB   . ALA B 1 125 ? -36.645 -27.449 1.012  1.00 15.09  ? 125 ALA B CB   1 
ATOM   5010 H  H    . ALA B 1 125 ? -35.015 -26.054 -0.303 1.00 17.24  ? 125 ALA B H    1 
ATOM   5011 H  HA   . ALA B 1 125 ? -37.541 -25.702 0.451  1.00 17.00  ? 125 ALA B HA   1 
ATOM   5012 H  HB1  . ALA B 1 125 ? -37.344 -27.751 1.615  1.00 18.18  ? 125 ALA B HB1  1 
ATOM   5013 H  HB2  . ALA B 1 125 ? -36.779 -27.848 0.136  1.00 18.18  ? 125 ALA B HB2  1 
ATOM   5014 H  HB3  . ALA B 1 125 ? -35.779 -27.719 1.361  1.00 18.18  ? 125 ALA B HB3  1 
ATOM   5015 N  N    . VAL B 1 126 ? -35.522 -25.271 2.938  1.00 12.53  ? 126 VAL B N    1 
ATOM   5016 C  CA   . VAL B 1 126 ? -35.485 -24.961 4.359  1.00 12.98  ? 126 VAL B CA   1 
ATOM   5017 C  C    . VAL B 1 126 ? -34.913 -23.565 4.573  1.00 12.59  ? 126 VAL B C    1 
ATOM   5018 O  O    . VAL B 1 126 ? -33.794 -23.269 4.169  1.00 13.79  ? 126 VAL B O    1 
ATOM   5019 C  CB   . VAL B 1 126 ? -34.640 -25.993 5.116  1.00 12.94  ? 126 VAL B CB   1 
ATOM   5020 C  CG1  . VAL B 1 126 ? -34.578 -25.636 6.598  1.00 13.97  ? 126 VAL B CG1  1 
ATOM   5021 C  CG2  . VAL B 1 126 ? -35.185 -27.395 4.920  1.00 13.65  ? 126 VAL B CG2  1 
ATOM   5022 H  H    . VAL B 1 126 ? -34.741 -25.446 2.497  1.00 15.19  ? 126 VAL B H    1 
ATOM   5023 H  HA   . VAL B 1 126 ? -36.392 -24.986 4.710  1.00 16.24  ? 126 VAL B HA   1 
ATOM   5024 H  HB   . VAL B 1 126 ? -33.722 -25.963 4.750  1.00 15.73  ? 126 VAL B HB   1 
ATOM   5025 H  HG11 . VAL B 1 126 ? -34.379 -26.435 7.118  1.00 16.24  ? 126 VAL B HG11 1 
ATOM   5026 H  HG12 . VAL B 1 126 ? -33.879 -24.975 6.745  1.00 16.24  ? 126 VAL B HG12 1 
ATOM   5027 H  HG13 . VAL B 1 126 ? -35.434 -25.272 6.882  1.00 16.24  ? 126 VAL B HG13 1 
ATOM   5028 H  HG21 . VAL B 1 126 ? -34.685 -28.019 5.476  1.00 16.23  ? 126 VAL B HG21 1 
ATOM   5029 H  HG22 . VAL B 1 126 ? -36.124 -27.418 5.172  1.00 16.23  ? 126 VAL B HG22 1 
ATOM   5030 H  HG23 . VAL B 1 126 ? -35.094 -27.652 3.986  1.00 16.23  ? 126 VAL B HG23 1 
ATOM   5031 N  N    . ALA B 1 127 ? -35.708 -22.699 5.225  1.00 12.06  ? 127 ALA B N    1 
ATOM   5032 C  CA   . ALA B 1 127 ? -35.243 -21.393 5.701  1.00 12.19  ? 127 ALA B CA   1 
ATOM   5033 C  C    . ALA B 1 127 ? -34.712 -21.550 7.120  1.00 11.55  ? 127 ALA B C    1 
ATOM   5034 O  O    . ALA B 1 127 ? -35.149 -22.435 7.848  1.00 12.29  ? 127 ALA B O    1 
ATOM   5035 C  CB   . ALA B 1 127 ? -36.353 -20.361 5.671  1.00 13.17  ? 127 ALA B CB   1 
ATOM   5036 H  H    . ALA B 1 127 ? -36.579 -22.929 5.378  1.00 16.24  ? 127 ALA B H    1 
ATOM   5037 H  HA   . ALA B 1 127 ? -34.507 -21.088 5.122  1.00 15.68  ? 127 ALA B HA   1 
ATOM   5038 H  HB1  . ALA B 1 127 ? -35.979 -19.476 5.820  1.00 15.89  ? 127 ALA B HB1  1 
ATOM   5039 H  HB2  . ALA B 1 127 ? -36.796 -20.383 4.807  1.00 15.89  ? 127 ALA B HB2  1 
ATOM   5040 H  HB3  . ALA B 1 127 ? -37.000 -20.559 6.369  1.00 15.89  ? 127 ALA B HB3  1 
ATOM   5041 N  N    . ARG B 1 128 ? -33.759 -20.685 7.489  1.00 11.82  ? 128 ARG B N    1 
ATOM   5042 C  CA   . ARG B 1 128 ? -33.062 -20.874 8.762  1.00 11.45  ? 128 ARG B CA   1 
ATOM   5043 C  C    . ARG B 1 128 ? -32.687 -19.525 9.382  1.00 11.02  ? 128 ARG B C    1 
ATOM   5044 O  O    . ARG B 1 128 ? -32.479 -18.526 8.695  1.00 12.12  ? 128 ARG B O    1 
ATOM   5045 C  CB   . ARG B 1 128 ? -31.781 -21.702 8.546  1.00 11.45  ? 128 ARG B CB   1 
ATOM   5046 C  CG   . ARG B 1 128 ? -30.644 -20.933 7.888  1.00 12.25  ? 128 ARG B CG   1 
ATOM   5047 C  CD   . ARG B 1 128 ? -29.514 -21.846 7.397  1.00 13.01  ? 128 ARG B CD   1 
ATOM   5048 N  NE   . ARG B 1 128 ? -28.311 -21.056 7.097  1.00 14.42  ? 128 ARG B NE   1 
ATOM   5049 C  CZ   . ARG B 1 128 ? -28.152 -20.304 6.025  1.00 14.81  ? 128 ARG B CZ   1 
ATOM   5050 N  NH1  . ARG B 1 128 ? -28.959 -20.400 4.991  1.00 15.84  ? 128 ARG B NH1  1 
ATOM   5051 N  NH2  . ARG B 1 128 ? -27.178 -19.420 5.971  1.00 17.24  ? 128 ARG B NH2  1 
ATOM   5052 H  H    . ARG B 1 128 ? -33.539 -19.977 6.955  1.00 15.68  ? 128 ARG B H    1 
ATOM   5053 H  HA   . ARG B 1 128 ? -33.655 -21.356 9.379  1.00 13.34  ? 128 ARG B HA   1 
ATOM   5054 H  HB2  . ARG B 1 128 ? -31.475 -22.035 9.415  1.00 13.77  ? 128 ARG B HB2  1 
ATOM   5055 H  HB3  . ARG B 1 128 ? -32.002 -22.477 7.989  1.00 13.77  ? 128 ARG B HB3  1 
ATOM   5056 H  HG2  . ARG B 1 128 ? -30.997 -20.426 7.126  1.00 18.34  ? 128 ARG B HG2  1 
ATOM   5057 H  HG3  . ARG B 1 128 ? -30.274 -20.292 8.530  1.00 18.34  ? 128 ARG B HG3  1 
ATOM   5058 H  HD2  . ARG B 1 128 ? -29.306 -22.510 8.089  1.00 18.21  ? 128 ARG B HD2  1 
ATOM   5059 H  HD3  . ARG B 1 128 ? -29.805 -22.324 6.591  1.00 18.21  ? 128 ARG B HD3  1 
ATOM   5060 H  HE   . ARG B 1 128 ? -27.652 -21.090 7.666  1.00 18.36  ? 128 ARG B HE   1 
ATOM   5061 H  HH11 . ARG B 1 128 ? -29.824 -20.264 5.095  1.00 18.30  ? 128 ARG B HH11 1 
ATOM   5062 H  HH12 . ARG B 1 128 ? -28.630 -20.597 4.196  1.00 18.30  ? 128 ARG B HH12 1 
ATOM   5063 H  HH21 . ARG B 1 128 ? -26.697 -19.253 6.688  1.00 18.33  ? 128 ARG B HH21 1 
ATOM   5064 H  HH22 . ARG B 1 128 ? -27.011 -18.997 5.219  1.00 18.33  ? 128 ARG B HH22 1 
ATOM   5065 N  N    . ARG B 1 129 ? -32.527 -19.545 10.708 1.00 10.76  ? 129 ARG B N    1 
ATOM   5066 C  CA   . ARG B 1 129 ? -31.914 -18.436 11.423 1.00 10.96  ? 129 ARG B CA   1 
ATOM   5067 C  C    . ARG B 1 129 ? -31.175 -19.005 12.640 1.00 10.35  ? 129 ARG B C    1 
ATOM   5068 O  O    . ARG B 1 129 ? -31.711 -19.843 13.380 1.00 11.97  ? 129 ARG B O    1 
ATOM   5069 C  CB   . ARG B 1 129 ? -32.944 -17.382 11.856 1.00 12.35  ? 129 ARG B CB   1 
ATOM   5070 C  CG   . ARG B 1 129 ? -32.322 -16.158 12.512 1.00 13.82  ? 129 ARG B CG   1 
ATOM   5071 C  CD   . ARG B 1 129 ? -33.320 -15.065 12.751 1.00 16.85  ? 129 ARG B CD   1 
ATOM   5072 N  NE   . ARG B 1 129 ? -33.631 -14.400 11.538 1.00 21.79  ? 129 ARG B NE   1 
ATOM   5073 C  CZ   . ARG B 1 129 ? -34.674 -13.579 11.454 1.00 23.37  ? 129 ARG B CZ   1 
ATOM   5074 N  NH1  . ARG B 1 129 ? -35.593 -13.616 12.398 1.00 23.34  ? 129 ARG B NH1  1 
ATOM   5075 N  NH2  . ARG B 1 129 ? -34.845 -12.791 10.415 1.00 27.71  ? 129 ARG B NH2  1 
ATOM   5076 H  H    . ARG B 1 129 ? -32.812 -20.272 11.184 1.00 13.34  ? 129 ARG B H    1 
ATOM   5077 H  HA   . ARG B 1 129 ? -31.258 -18.008 10.827 1.00 18.39  ? 129 ARG B HA   1 
ATOM   5078 H  HB2  . ARG B 1 129 ? -33.450 -17.097 11.068 1.00 23.21  ? 129 ARG B HB2  1 
ATOM   5079 H  HB3  . ARG B 1 129 ? -33.571 -17.796 12.485 1.00 23.21  ? 129 ARG B HB3  1 
ATOM   5080 H  HG2  . ARG B 1 129 ? -31.926 -16.418 13.371 1.00 20.25  ? 129 ARG B HG2  1 
ATOM   5081 H  HG3  . ARG B 1 129 ? -31.602 -15.815 11.941 1.00 20.25  ? 129 ARG B HG3  1 
ATOM   5082 H  HD2  . ARG B 1 129 ? -34.135 -15.451 13.134 1.00 20.18  ? 129 ARG B HD2  1 
ATOM   5083 H  HD3  . ARG B 1 129 ? -32.954 -14.421 13.394 1.00 20.18  ? 129 ARG B HD3  1 
ATOM   5084 H  HE   . ARG B 1 129 ? -33.133 -14.529 10.834 1.00 20.31  ? 129 ARG B HE   1 
ATOM   5085 H  HH11 . ARG B 1 129 ? -35.401 -13.333 13.209 1.00 20.75  ? 129 ARG B HH11 1 
ATOM   5086 H  HH12 . ARG B 1 129 ? -36.398 -13.923 12.214 1.00 20.75  ? 129 ARG B HH12 1 
ATOM   5087 H  HH21 . ARG B 1 129 ? -34.195 -12.687 9.833  1.00 20.38  ? 129 ARG B HH21 1 
ATOM   5088 H  HH22 . ARG B 1 129 ? -35.609 -12.369 10.306 1.00 20.38  ? 129 ARG B HH22 1 
ATOM   5089 N  N    . LEU B 1 130 ? -29.947 -18.536 12.810 1.00 9.86   ? 130 LEU B N    1 
ATOM   5090 C  CA   . LEU B 1 130 ? -29.071 -18.940 13.900 1.00 9.42   ? 130 LEU B CA   1 
ATOM   5091 C  C    . LEU B 1 130 ? -29.045 -17.847 14.973 1.00 9.25   ? 130 LEU B C    1 
ATOM   5092 O  O    . LEU B 1 130 ? -28.709 -16.706 14.663 1.00 10.42  ? 130 LEU B O    1 
ATOM   5093 C  CB   . LEU B 1 130 ? -27.659 -19.168 13.345 1.00 9.59   ? 130 LEU B CB   1 
ATOM   5094 C  CG   . LEU B 1 130 ? -26.586 -19.573 14.358 1.00 9.98   ? 130 LEU B CG   1 
ATOM   5095 C  CD1  . LEU B 1 130 ? -26.916 -20.924 15.004 1.00 11.30  ? 130 LEU B CD1  1 
ATOM   5096 C  CD2  . LEU B 1 130 ? -25.241 -19.631 13.659 1.00 10.93  ? 130 LEU B CD2  1 
ATOM   5097 H  H    . LEU B 1 130 ? -29.629 -17.922 12.212 1.00 18.39  ? 130 LEU B H    1 
ATOM   5098 H  HA   . LEU B 1 130 ? -29.414 -19.775 14.294 1.00 13.46  ? 130 LEU B HA   1 
ATOM   5099 H  HB2  . LEU B 1 130 ? -27.709 -19.862 12.660 1.00 15.45  ? 130 LEU B HB2  1 
ATOM   5100 H  HB3  . LEU B 1 130 ? -27.369 -18.344 12.904 1.00 15.45  ? 130 LEU B HB3  1 
ATOM   5101 H  HG   . LEU B 1 130 ? -26.542 -18.885 15.068 1.00 12.09  ? 130 LEU B HG   1 
ATOM   5102 H  HD11 . LEU B 1 130 ? -26.159 -21.223 15.536 1.00 13.46  ? 130 LEU B HD11 1 
ATOM   5103 H  HD12 . LEU B 1 130 ? -27.697 -20.828 15.577 1.00 13.46  ? 130 LEU B HD12 1 
ATOM   5104 H  HD13 . LEU B 1 130 ? -27.103 -21.579 14.309 1.00 13.46  ? 130 LEU B HD13 1 
ATOM   5105 H  HD21 . LEU B 1 130 ? -24.555 -19.892 14.297 1.00 12.86  ? 130 LEU B HD21 1 
ATOM   5106 H  HD22 . LEU B 1 130 ? -25.278 -20.283 12.938 1.00 12.86  ? 130 LEU B HD22 1 
ATOM   5107 H  HD23 . LEU B 1 130 ? -25.027 -18.755 13.293 1.00 12.86  ? 130 LEU B HD23 1 
ATOM   5108 N  N    . HIS B 1 131 ? -29.321 -18.227 16.217 1.00 9.06   ? 131 HIS B N    1 
ATOM   5109 C  CA   . HIS B 1 131 ? -29.228 -17.312 17.347 1.00 9.21   ? 131 HIS B CA   1 
ATOM   5110 C  C    . HIS B 1 131 ? -28.196 -17.856 18.323 1.00 8.67   ? 131 HIS B C    1 
ATOM   5111 O  O    . HIS B 1 131 ? -28.218 -19.046 18.658 1.00 9.82   ? 131 HIS B O    1 
ATOM   5112 C  CB   . HIS B 1 131 ? -30.571 -17.128 18.068 1.00 9.96   ? 131 HIS B CB   1 
ATOM   5113 C  CG   . HIS B 1 131 ? -31.737 -16.913 17.156 1.00 9.96   ? 131 HIS B CG   1 
ATOM   5114 N  ND1  . HIS B 1 131 ? -32.354 -17.931 16.470 1.00 10.48  ? 131 HIS B ND1  1 
ATOM   5115 C  CD2  . HIS B 1 131 ? -32.451 -15.813 16.890 1.00 11.15  ? 131 HIS B CD2  1 
ATOM   5116 C  CE1  . HIS B 1 131 ? -33.368 -17.406 15.796 1.00 11.45  ? 131 HIS B CE1  1 
ATOM   5117 N  NE2  . HIS B 1 131 ? -33.488 -16.124 16.035 1.00 12.17  ? 131 HIS B NE2  1 
ATOM   5118 H  H    . HIS B 1 131 ? -29.578 -19.090 16.374 1.00 13.46  ? 131 HIS B H    1 
ATOM   5119 H  HA   . HIS B 1 131 ? -28.917 -16.432 17.021 1.00 10.68  ? 131 HIS B HA   1 
ATOM   5120 H  HB2  . HIS B 1 131 ? -30.741 -17.922 18.618 1.00 13.52  ? 131 HIS B HB2  1 
ATOM   5121 H  HB3  . HIS B 1 131 ? -30.497 -16.360 18.674 1.00 13.52  ? 131 HIS B HB3  1 
ATOM   5122 H  HD1  . HIS B 1 131 ? -32.102 -18.775 16.459 1.00 13.25  ? 131 HIS B HD1  1 
ATOM   5123 H  HD2  . HIS B 1 131 ? -32.283 -14.957 17.234 1.00 13.25  ? 131 HIS B HD2  1 
ATOM   5124 H  HE1  . HIS B 1 131 ? -33.935 -17.909 15.237 1.00 13.25  ? 131 HIS B HE1  1 
ATOM   5125 N  N    . HIS B 1 132 ? -27.323 -16.971 18.790 1.00 8.58   ? 132 HIS B N    1 
ATOM   5126 C  CA   . HIS B 1 132 ? -26.278 -17.307 19.757 1.00 8.63   ? 132 HIS B CA   1 
ATOM   5127 C  C    . HIS B 1 132 ? -26.735 -16.915 21.164 1.00 8.54   ? 132 HIS B C    1 
ATOM   5128 O  O    . HIS B 1 132 ? -27.226 -15.795 21.374 1.00 9.57   ? 132 HIS B O    1 
ATOM   5129 C  CB   . HIS B 1 132 ? -25.000 -16.536 19.452 1.00 8.75   ? 132 HIS B CB   1 
ATOM   5130 C  CG   . HIS B 1 132 ? -24.391 -16.866 18.134 1.00 8.87   ? 132 HIS B CG   1 
ATOM   5131 N  ND1  . HIS B 1 132 ? -23.225 -17.576 18.036 1.00 10.05  ? 132 HIS B ND1  1 
ATOM   5132 C  CD2  . HIS B 1 132 ? -24.771 -16.572 16.870 1.00 10.14  ? 132 HIS B CD2  1 
ATOM   5133 C  CE1  . HIS B 1 132 ? -22.907 -17.702 16.769 1.00 11.32  ? 132 HIS B CE1  1 
ATOM   5134 N  NE2  . HIS B 1 132 ? -23.817 -17.122 16.029 1.00 11.01  ? 132 HIS B NE2  1 
ATOM   5135 H  H    . HIS B 1 132 ? -27.374 -16.107 18.496 1.00 10.68  ? 132 HIS B H    1 
ATOM   5136 H  HA   . HIS B 1 132 ? -26.102 -18.280 19.736 1.00 12.73  ? 132 HIS B HA   1 
ATOM   5137 H  HB2  . HIS B 1 132 ? -25.201 -15.575 19.474 1.00 10.68  ? 132 HIS B HB2  1 
ATOM   5138 H  HB3  . HIS B 1 132 ? -24.344 -16.726 20.156 1.00 10.68  ? 132 HIS B HB3  1 
ATOM   5139 H  HD1  . HIS B 1 132 ? -22.769 -17.875 18.709 1.00 13.30  ? 132 HIS B HD1  1 
ATOM   5140 H  HD2  . HIS B 1 132 ? -25.533 -16.095 16.605 1.00 13.30  ? 132 HIS B HD2  1 
ATOM   5141 H  HE1  . HIS B 1 132 ? -22.148 -18.158 16.449 1.00 13.30  ? 132 HIS B HE1  1 
ATOM   5142 N  N    . CYS B 1 133 ? -26.480 -17.782 22.146 1.00 8.78   ? 133 CYS B N    1 
ATOM   5143 C  CA   . CYS B 1 133 ? -26.889 -17.517 23.509 1.00 8.93   ? 133 CYS B CA   1 
ATOM   5144 C  C    . CYS B 1 133 ? -25.745 -17.311 24.481 1.00 8.64   ? 133 CYS B C    1 
ATOM   5145 O  O    . CYS B 1 133 ? -25.981 -16.757 25.557 1.00 9.71   ? 133 CYS B O    1 
ATOM   5146 C  CB   . CYS B 1 133 ? -27.725 -18.661 24.070 1.00 9.18   ? 133 CYS B CB   1 
ATOM   5147 S  SG   . CYS B 1 133 ? -29.143 -19.168 23.066 1.00 9.90   ? 133 CYS B SG   1 
ATOM   5148 H  H    . CYS B 1 133 ? -26.046 -18.564 21.959 1.00 12.73  ? 133 CYS B H    1 
ATOM   5149 H  HA   . CYS B 1 133 ? -27.445 -16.704 23.510 1.00 10.92  ? 133 CYS B HA   1 
ATOM   5150 H  HB2  . CYS B 1 133 ? -27.145 -19.439 24.188 1.00 10.97  ? 133 CYS B HB2  1 
ATOM   5151 H  HB3  . CYS B 1 133 ? -28.056 -18.403 24.955 1.00 10.97  ? 133 CYS B HB3  1 
ATOM   5152 H  HG   . CYS B 1 133 ? -29.721 -18.113 23.077 1.00 11.82  ? 133 CYS B HG   1 
ATOM   5153 N  N    . ARG B 1 134 ? -24.550 -17.830 24.189 1.00 8.77   ? 134 ARG B N    1 
ATOM   5154 C  CA   . ARG B 1 134 ? -23.564 -17.980 25.261 1.00 9.48   ? 134 ARG B CA   1 
ATOM   5155 C  C    . ARG B 1 134 ? -22.908 -16.665 25.667 1.00 9.31   ? 134 ARG B C    1 
ATOM   5156 O  O    . ARG B 1 134 ? -22.248 -16.643 26.716 1.00 10.38  ? 134 ARG B O    1 
ATOM   5157 C  CB   . ARG B 1 134 ? -22.532 -19.032 24.930 1.00 10.22  ? 134 ARG B CB   1 
ATOM   5158 C  CG   . ARG B 1 134 ? -21.343 -18.594 24.127 1.00 11.76  ? 134 ARG B CG   1 
ATOM   5159 C  CD   . ARG B 1 134 ? -20.402 -19.752 23.878 1.00 12.26  ? 134 ARG B CD   1 
ATOM   5160 N  NE   . ARG B 1 134 ? -19.846 -20.302 25.103 1.00 13.08  ? 134 ARG B NE   1 
ATOM   5161 C  CZ   . ARG B 1 134 ? -18.656 -19.968 25.630 1.00 12.11  ? 134 ARG B CZ   1 
ATOM   5162 N  NH1  . ARG B 1 134 ? -17.810 -19.213 24.960 1.00 12.83  ? 134 ARG B NH1  1 
ATOM   5163 N  NH2  . ARG B 1 134 ? -18.374 -20.400 26.810 1.00 13.69  ? 134 ARG B NH2  1 
ATOM   5164 H  H    . ARG B 1 134 ? -24.339 -18.088 23.338 1.00 12.73  ? 134 ARG B H    1 
ATOM   5165 H  HA   . ARG B 1 134 ? -24.056 -18.304 26.049 1.00 15.59  ? 134 ARG B HA   1 
ATOM   5166 H  HB2  . ARG B 1 134 ? -22.209 -19.410 25.774 1.00 13.02  ? 134 ARG B HB2  1 
ATOM   5167 H  HB3  . ARG B 1 134 ? -22.982 -19.752 24.441 1.00 13.02  ? 134 ARG B HB3  1 
ATOM   5168 H  HG2  . ARG B 1 134 ? -21.643 -18.229 23.267 1.00 11.41  ? 134 ARG B HG2  1 
ATOM   5169 H  HG3  . ARG B 1 134 ? -20.861 -17.888 24.608 1.00 11.41  ? 134 ARG B HG3  1 
ATOM   5170 H  HD2  . ARG B 1 134 ? -20.889 -20.460 23.404 1.00 13.37  ? 134 ARG B HD2  1 
ATOM   5171 H  HD3  . ARG B 1 134 ? -19.672 -19.453 23.296 1.00 13.37  ? 134 ARG B HD3  1 
ATOM   5172 H  HE   . ARG B 1 134 ? -20.321 -20.897 25.529 1.00 14.86  ? 134 ARG B HE   1 
ATOM   5173 H  HH11 . ARG B 1 134 ? -18.068 -18.428 24.657 1.00 13.21  ? 134 ARG B HH11 1 
ATOM   5174 H  HH12 . ARG B 1 134 ? -16.987 -19.494 24.823 1.00 13.20  ? 134 ARG B HH12 1 
ATOM   5175 H  HH21 . ARG B 1 134 ? -19.021 -20.605 27.369 1.00 14.86  ? 134 ARG B HH21 1 
ATOM   5176 H  HH22 . ARG B 1 134 ? -17.533 -20.486 27.054 1.00 14.86  ? 134 ARG B HH22 1 
ATOM   5177 N  N    . ASP B 1 135 ? -23.053 -15.604 24.872 1.00 9.14   ? 135 ASP B N    1 
ATOM   5178 C  CA   . ASP B 1 135 ? -22.422 -14.338 25.187 1.00 9.60   ? 135 ASP B CA   1 
ATOM   5179 C  C    . ASP B 1 135 ? -23.429 -13.227 25.494 1.00 10.69  ? 135 ASP B C    1 
ATOM   5180 O  O    . ASP B 1 135 ? -23.077 -12.024 25.430 1.00 12.07  ? 135 ASP B O    1 
ATOM   5181 C  CB   . ASP B 1 135 ? -21.500 -13.905 24.067 1.00 9.64   ? 135 ASP B CB   1 
ATOM   5182 C  CG   . ASP B 1 135 ? -20.468 -14.963 23.754 1.00 9.77   ? 135 ASP B CG   1 
ATOM   5183 O  OD1  . ASP B 1 135 ? -19.759 -15.380 24.673 1.00 10.35  ? 135 ASP B OD1  1 
ATOM   5184 O  OD2  . ASP B 1 135 ? -20.343 -15.328 22.572 1.00 13.19  ? 135 ASP B OD2  1 
ATOM   5185 H  H    . ASP B 1 135 ? -23.537 -15.679 24.105 1.00 11.07  ? 135 ASP B H    1 
ATOM   5186 H  HA   . ASP B 1 135 ? -21.866 -14.468 25.990 1.00 11.67  ? 135 ASP B HA   1 
ATOM   5187 H  HB2  . ASP B 1 135 ? -22.015 -13.715 23.259 1.00 11.97  ? 135 ASP B HB2  1 
ATOM   5188 H  HB3  . ASP B 1 135 ? -21.031 -13.088 24.331 1.00 11.97  ? 135 ASP B HB3  1 
ATOM   5189 N  N    . LEU B 1 136 ? -24.650 -13.618 25.872 1.00 11.08  ? 136 LEU B N    1 
ATOM   5190 C  CA   . LEU B 1 136 ? -25.666 -12.683 26.327 1.00 12.45  ? 136 LEU B CA   1 
ATOM   5191 C  C    . LEU B 1 136 ? -25.316 -12.230 27.744 1.00 15.20  ? 136 LEU B C    1 
ATOM   5192 O  O    . LEU B 1 136 ? -24.576 -12.878 28.468 1.00 19.07  ? 136 LEU B O    1 
ATOM   5193 C  CB   . LEU B 1 136 ? -27.034 -13.366 26.323 1.00 11.70  ? 136 LEU B CB   1 
ATOM   5194 C  CG   . LEU B 1 136 ? -27.633 -13.644 24.972 1.00 12.83  ? 136 LEU B CG   1 
ATOM   5195 C  CD1  . LEU B 1 136 ? -28.811 -14.582 25.091 1.00 13.51  ? 136 LEU B CD1  1 
ATOM   5196 C  CD2  . LEU B 1 136 ? -28.040 -12.359 24.277 1.00 16.20  ? 136 LEU B CD2  1 
ATOM   5197 H  H    . LEU B 1 136 ? -24.857 -14.508 25.855 1.00 14.49  ? 136 LEU B H    1 
ATOM   5198 H  HA   . LEU B 1 136 ? -25.674 -11.902 25.730 1.00 18.87  ? 136 LEU B HA   1 
ATOM   5199 H  HB2  . LEU B 1 136 ? -26.954 -14.213 26.805 1.00 14.49  ? 136 LEU B HB2  1 
ATOM   5200 H  HB3  . LEU B 1 136 ? -27.657 -12.802 26.824 1.00 14.49  ? 136 LEU B HB3  1 
ATOM   5201 H  HG   . LEU B 1 136 ? -26.946 -14.086 24.419 1.00 15.45  ? 136 LEU B HG   1 
ATOM   5202 H  HD11 . LEU B 1 136 ? -29.256 -14.655 24.229 1.00 13.70  ? 136 LEU B HD11 1 
ATOM   5203 H  HD12 . LEU B 1 136 ? -28.500 -15.460 25.371 1.00 13.70  ? 136 LEU B HD12 1 
ATOM   5204 H  HD13 . LEU B 1 136 ? -29.437 -14.235 25.750 1.00 13.70  ? 136 LEU B HD13 1 
ATOM   5205 H  HD21 . LEU B 1 136 ? -28.261 -12.549 23.349 1.00 18.87  ? 136 LEU B HD21 1 
ATOM   5206 H  HD22 . LEU B 1 136 ? -28.818 -11.982 24.723 1.00 18.87  ? 136 LEU B HD22 1 
ATOM   5207 H  HD23 . LEU B 1 136 ? -27.309 -11.722 24.311 1.00 18.87  ? 136 LEU B HD23 1 
ATOM   5208 N  N    . GLY B 1 137 ? -25.931 -11.185 28.240 1.00 17.50  ? 137 GLY B N    1 
ATOM   5209 C  CA   . GLY B 1 137 ? -25.549 -10.886 29.652 1.00 21.54  ? 137 GLY B CA   1 
ATOM   5210 C  C    . GLY B 1 137 ? -26.060 -11.871 30.727 1.00 18.06  ? 137 GLY B C    1 
ATOM   5211 O  O    . GLY B 1 137 ? -25.665 -11.822 31.883 1.00 20.54  ? 137 GLY B O    1 
ATOM   5212 H  H    . GLY B 1 137 ? -26.538 -10.678 27.782 1.00 21.06  ? 137 GLY B H    1 
ATOM   5213 H  HA2  . GLY B 1 137 ? -24.561 -10.839 29.707 1.00 20.78  ? 137 GLY B HA2  1 
ATOM   5214 H  HA3  . GLY B 1 137 ? -25.890 -9.985  29.870 1.00 20.78  ? 137 GLY B HA3  1 
ATOM   5215 N  N    . GLU B 1 138 ? -27.017 -12.708 30.371 1.00 18.99  ? 138 GLU B N    1 
ATOM   5216 C  CA   . GLU B 1 138 ? -27.875 -13.443 31.283 1.00 16.99  ? 138 GLU B CA   1 
ATOM   5217 C  C    . GLU B 1 138 ? -27.779 -14.923 30.927 1.00 15.29  ? 138 GLU B C    1 
ATOM   5218 O  O    . GLU B 1 138 ? -27.637 -15.291 29.762 1.00 16.25  ? 138 GLU B O    1 
ATOM   5219 C  CB   . GLU B 1 138 ? -29.292 -12.899 31.118 1.00 19.76  ? 138 GLU B CB   1 
ATOM   5220 C  CG   . GLU B 1 138 ? -29.746 -12.951 29.665 1.00 21.34  ? 138 GLU B CG   1 
ATOM   5221 C  CD   . GLU B 1 138 ? -30.535 -14.183 29.309 1.00 19.84  ? 138 GLU B CD   1 
ATOM   5222 O  OE1  . GLU B 1 138 ? -30.994 -14.906 30.238 1.00 23.38  ? 138 GLU B OE1  1 
ATOM   5223 O  OE2  . GLU B 1 138 ? -30.712 -14.378 28.090 1.00 19.18  ? 138 GLU B OE2  1 
ATOM   5224 H  H    . GLU B 1 138 ? -27.128 -12.860 29.477 1.00 23.63  ? 138 GLU B H    1 
ATOM   5225 H  HA   . GLU B 1 138 ? -27.570 -13.302 32.209 1.00 29.07  ? 138 GLU B HA   1 
ATOM   5226 H  HB2  . GLU B 1 138 ? -29.903 -13.424 31.675 1.00 22.06  ? 138 GLU B HB2  1 
ATOM   5227 H  HB3  . GLU B 1 138 ? -29.314 -11.971 31.431 1.00 22.06  ? 138 GLU B HB3  1 
ATOM   5228 H  HG2  . GLU B 1 138 ? -30.303 -12.164 29.480 1.00 23.63  ? 138 GLU B HG2  1 
ATOM   5229 H  HG3  . GLU B 1 138 ? -28.968 -12.903 29.075 1.00 23.63  ? 138 GLU B HG3  1 
ATOM   5230 N  N    . ASN B 1 139 ? -27.778 -15.772 31.930 1.00 17.20  ? 139 ASN B N    1 
ATOM   5231 C  CA   . ASN B 1 139 ? -27.630 -17.202 31.770 1.00 19.09  ? 139 ASN B CA   1 
ATOM   5232 C  C    . ASN B 1 139 ? -28.716 -17.790 30.870 1.00 17.27  ? 139 ASN B C    1 
ATOM   5233 O  O    . ASN B 1 139 ? -29.897 -17.515 31.059 1.00 21.41  ? 139 ASN B O    1 
ATOM   5234 C  CB   . ASN B 1 139 ? -27.720 -17.815 33.167 1.00 24.97  ? 139 ASN B CB   1 
ATOM   5235 C  CG   . ASN B 1 139 ? -28.012 -19.292 33.133 1.00 29.48  ? 139 ASN B CG   1 
ATOM   5236 O  OD1  . ASN B 1 139 ? -27.139 -20.071 32.767 1.00 36.07  ? 139 ASN B OD1  1 
ATOM   5237 N  ND2  . ASN B 1 139 ? -29.240 -19.669 33.444 1.00 33.02  ? 139 ASN B ND2  1 
ATOM   5238 H  H    . ASN B 1 139 ? -27.869 -15.438 32.776 1.00 29.07  ? 139 ASN B H    1 
ATOM   5239 H  HA   . ASN B 1 139 ? -26.740 -17.398 31.394 1.00 19.76  ? 139 ASN B HA   1 
ATOM   5240 H  HB2  . ASN B 1 139 ? -26.872 -17.666 33.634 1.00 29.07  ? 139 ASN B HB2  1 
ATOM   5241 H  HB3  . ASN B 1 139 ? -28.428 -17.363 33.671 1.00 29.07  ? 139 ASN B HB3  1 
ATOM   5242 H  HD21 . ASN B 1 139 ? -29.930 -19.168 33.209 1.00 29.07  ? 139 ASN B HD21 1 
ATOM   5243 H  HD22 . ASN B 1 139 ? -29.373 -20.423 33.886 1.00 29.07  ? 139 ASN B HD22 1 
ATOM   5244 N  N    . GLU B 1 140 ? -28.324 -18.604 29.897 1.00 14.93  ? 140 GLU B N    1 
ATOM   5245 C  CA   . GLU B 1 140 ? -29.242 -19.337 29.052 1.00 12.88  ? 140 GLU B CA   1 
ATOM   5246 C  C    . GLU B 1 140 ? -28.881 -20.813 29.142 1.00 12.69  ? 140 GLU B C    1 
ATOM   5247 O  O    . GLU B 1 140 ? -27.713 -21.178 29.194 1.00 14.00  ? 140 GLU B O    1 
ATOM   5248 C  CB   . GLU B 1 140 ? -29.147 -18.885 27.600 1.00 12.35  ? 140 GLU B CB   1 
ATOM   5249 C  CG   . GLU B 1 140 ? -29.808 -17.547 27.351 1.00 12.93  ? 140 GLU B CG   1 
ATOM   5250 C  CD   . GLU B 1 140 ? -31.324 -17.579 27.448 1.00 12.72  ? 140 GLU B CD   1 
ATOM   5251 O  OE1  . GLU B 1 140 ? -31.966 -18.600 27.094 1.00 13.15  ? 140 GLU B OE1  1 
ATOM   5252 O  OE2  . GLU B 1 140 ? -31.907 -16.521 27.812 1.00 15.13  ? 140 GLU B OE2  1 
ATOM   5253 H  H    . GLU B 1 140 ? -27.428 -18.707 29.750 1.00 19.76  ? 140 GLU B H    1 
ATOM   5254 H  HA   . GLU B 1 140 ? -30.159 -19.203 29.380 1.00 15.81  ? 140 GLU B HA   1 
ATOM   5255 H  HB2  . GLU B 1 140 ? -28.201 -18.825 27.352 1.00 12.91  ? 140 GLU B HB2  1 
ATOM   5256 H  HB3  . GLU B 1 140 ? -29.566 -19.561 27.031 1.00 12.91  ? 140 GLU B HB3  1 
ATOM   5257 H  HG2  . GLU B 1 140 ? -29.468 -16.896 28.001 1.00 13.73  ? 140 GLU B HG2  1 
ATOM   5258 H  HG3  . GLU B 1 140 ? -29.560 -17.231 26.456 1.00 13.73  ? 140 GLU B HG3  1 
ATOM   5259 N  N    . PRO B 1 141 ? -29.879 -21.717 29.101 1.00 12.52  ? 141 PRO B N    1 
ATOM   5260 C  CA   . PRO B 1 141 ? -29.605 -23.149 29.208 1.00 12.51  ? 141 PRO B CA   1 
ATOM   5261 C  C    . PRO B 1 141 ? -29.053 -23.770 27.933 1.00 11.59  ? 141 PRO B C    1 
ATOM   5262 O  O    . PRO B 1 141 ? -28.529 -24.873 27.978 1.00 15.06  ? 141 PRO B O    1 
ATOM   5263 C  CB   . PRO B 1 141 ? -30.971 -23.748 29.538 1.00 14.88  ? 141 PRO B CB   1 
ATOM   5264 C  CG   . PRO B 1 141 ? -31.965 -22.745 29.021 1.00 14.49  ? 141 PRO B CG   1 
ATOM   5265 C  CD   . PRO B 1 141 ? -31.318 -21.405 29.199 1.00 13.14  ? 141 PRO B CD   1 
ATOM   5266 H  HA   . PRO B 1 141 ? -28.984 -23.311 29.962 1.00 15.12  ? 141 PRO B HA   1 
ATOM   5267 H  HB2  . PRO B 1 141 ? -31.090 -24.616 29.096 1.00 17.81  ? 141 PRO B HB2  1 
ATOM   5268 H  HB3  . PRO B 1 141 ? -31.073 -23.871 30.506 1.00 17.81  ? 141 PRO B HB3  1 
ATOM   5269 H  HG2  . PRO B 1 141 ? -32.162 -22.910 28.077 1.00 13.67  ? 141 PRO B HG2  1 
ATOM   5270 H  HG3  . PRO B 1 141 ? -32.800 -22.794 29.529 1.00 13.67  ? 141 PRO B HG3  1 
ATOM   5271 H  HD2  . PRO B 1 141 ? -31.592 -20.787 28.497 1.00 15.81  ? 141 PRO B HD2  1 
ATOM   5272 H  HD3  . PRO B 1 141 ? -31.536 -21.019 30.067 1.00 15.81  ? 141 PRO B HD3  1 
ATOM   5273 N  N    . PHE B 1 142 ? -29.189 -23.079 26.801 1.00 10.36  ? 142 PHE B N    1 
ATOM   5274 C  CA   . PHE B 1 142 ? -28.653 -23.568 25.545 1.00 9.81   ? 142 PHE B CA   1 
ATOM   5275 C  C    . PHE B 1 142 ? -27.600 -22.597 25.047 1.00 9.21   ? 142 PHE B C    1 
ATOM   5276 O  O    . PHE B 1 142 ? -27.560 -21.447 25.463 1.00 10.00  ? 142 PHE B O    1 
ATOM   5277 C  CB   . PHE B 1 142 ? -29.780 -23.759 24.520 1.00 10.05  ? 142 PHE B CB   1 
ATOM   5278 C  CG   . PHE B 1 142 ? -30.800 -24.748 25.010 1.00 10.27  ? 142 PHE B CG   1 
ATOM   5279 C  CD1  . PHE B 1 142 ? -30.616 -26.107 24.874 1.00 10.98  ? 142 PHE B CD1  1 
ATOM   5280 C  CD2  . PHE B 1 142 ? -31.951 -24.299 25.638 1.00 10.58  ? 142 PHE B CD2  1 
ATOM   5281 C  CE1  . PHE B 1 142 ? -31.565 -27.009 25.345 1.00 11.60  ? 142 PHE B CE1  1 
ATOM   5282 C  CE2  . PHE B 1 142 ? -32.880 -25.203 26.139 1.00 12.04  ? 142 PHE B CE2  1 
ATOM   5283 C  CZ   . PHE B 1 142 ? -32.696 -26.543 25.976 1.00 12.16  ? 142 PHE B CZ   1 
ATOM   5284 H  H    . PHE B 1 142 ? -29.638 -22.283 26.807 1.00 12.50  ? 142 PHE B H    1 
ATOM   5285 H  HA   . PHE B 1 142 ? -28.219 -24.445 25.701 1.00 18.49  ? 142 PHE B HA   1 
ATOM   5286 H  HB2  . PHE B 1 142 ? -30.212 -22.896 24.355 1.00 13.28  ? 142 PHE B HB2  1 
ATOM   5287 H  HB3  . PHE B 1 142 ? -29.395 -24.077 23.677 1.00 13.28  ? 142 PHE B HB3  1 
ATOM   5288 H  HD1  . PHE B 1 142 ? -29.840 -26.429 24.442 1.00 13.63  ? 142 PHE B HD1  1 
ATOM   5289 H  HD2  . PHE B 1 142 ? -32.084 -23.373 25.761 1.00 13.55  ? 142 PHE B HD2  1 
ATOM   5290 H  HE1  . PHE B 1 142 ? -31.428 -27.937 25.241 1.00 13.67  ? 142 PHE B HE1  1 
ATOM   5291 H  HE2  . PHE B 1 142 ? -33.665 -24.885 26.557 1.00 13.61  ? 142 PHE B HE2  1 
ATOM   5292 H  HZ   . PHE B 1 142 ? -33.341 -27.151 26.299 1.00 13.63  ? 142 PHE B HZ   1 
ATOM   5293 N  N    . ASP B 1 143 ? -26.756 -23.082 24.129 1.00 9.05   ? 143 ASP B N    1 
ATOM   5294 C  CA   . ASP B 1 143 ? -25.780 -22.236 23.449 1.00 8.82   ? 143 ASP B CA   1 
ATOM   5295 C  C    . ASP B 1 143 ? -26.314 -21.619 22.166 1.00 8.46   ? 143 ASP B C    1 
ATOM   5296 O  O    . ASP B 1 143 ? -25.856 -20.536 21.784 1.00 8.94   ? 143 ASP B O    1 
ATOM   5297 C  CB   . ASP B 1 143 ? -24.514 -23.022 23.138 1.00 9.27   ? 143 ASP B CB   1 
ATOM   5298 C  CG   . ASP B 1 143 ? -23.752 -23.434 24.379 1.00 10.20  ? 143 ASP B CG   1 
ATOM   5299 O  OD1  . ASP B 1 143 ? -23.708 -22.635 25.332 1.00 11.95  ? 143 ASP B OD1  1 
ATOM   5300 O  OD2  . ASP B 1 143 ? -23.161 -24.540 24.365 1.00 11.75  ? 143 ASP B OD2  1 
ATOM   5301 H  H    . ASP B 1 143 ? -26.792 -23.969 23.916 1.00 18.49  ? 143 ASP B H    1 
ATOM   5302 H  HA   . ASP B 1 143 ? -25.535 -21.502 24.059 1.00 10.73  ? 143 ASP B HA   1 
ATOM   5303 H  HB2  . ASP B 1 143 ? -24.752 -23.828 22.636 1.00 14.83  ? 143 ASP B HB2  1 
ATOM   5304 H  HB3  . ASP B 1 143 ? -23.924 -22.476 22.579 1.00 14.83  ? 143 ASP B HB3  1 
ATOM   5305 N  N    . PHE B 1 144 ? -27.238 -22.300 21.489 1.00 8.71   ? 144 PHE B N    1 
ATOM   5306 C  CA   . PHE B 1 144 ? -27.796 -21.805 20.244 1.00 8.88   ? 144 PHE B CA   1 
ATOM   5307 C  C    . PHE B 1 144 ? -29.289 -22.073 20.262 1.00 8.74   ? 144 PHE B C    1 
ATOM   5308 O  O    . PHE B 1 144 ? -29.759 -23.085 20.788 1.00 9.39   ? 144 PHE B O    1 
ATOM   5309 C  CB   . PHE B 1 144 ? -27.217 -22.551 19.034 1.00 9.34   ? 144 PHE B CB   1 
ATOM   5310 C  CG   . PHE B 1 144 ? -25.724 -22.430 18.924 1.00 9.15   ? 144 PHE B CG   1 
ATOM   5311 C  CD1  . PHE B 1 144 ? -25.134 -21.299 18.377 1.00 10.57  ? 144 PHE B CD1  1 
ATOM   5312 C  CD2  . PHE B 1 144 ? -24.889 -23.445 19.371 1.00 9.92   ? 144 PHE B CD2  1 
ATOM   5313 C  CE1  . PHE B 1 144 ? -23.764 -21.200 18.269 1.00 11.67  ? 144 PHE B CE1  1 
ATOM   5314 C  CE2  . PHE B 1 144 ? -23.514 -23.333 19.251 1.00 11.32  ? 144 PHE B CE2  1 
ATOM   5315 C  CZ   . PHE B 1 144 ? -22.965 -22.220 18.697 1.00 12.53  ? 144 PHE B CZ   1 
ATOM   5316 H  H    . PHE B 1 144 ? -27.526 -23.106 21.809 1.00 18.49  ? 144 PHE B H    1 
ATOM   5317 H  HA   . PHE B 1 144 ? -27.628 -20.835 20.158 1.00 10.47  ? 144 PHE B HA   1 
ATOM   5318 H  HB2  . PHE B 1 144 ? -27.458 -23.499 19.104 1.00 15.01  ? 144 PHE B HB2  1 
ATOM   5319 H  HB3  . PHE B 1 144 ? -27.628 -22.194 18.219 1.00 15.00  ? 144 PHE B HB3  1 
ATOM   5320 H  HD1  . PHE B 1 144 ? -25.679 -20.596 18.063 1.00 15.47  ? 144 PHE B HD1  1 
ATOM   5321 H  HD2  . PHE B 1 144 ? -25.265 -24.226 19.745 1.00 15.39  ? 144 PHE B HD2  1 
ATOM   5322 H  HE1  . PHE B 1 144 ? -23.379 -20.430 17.884 1.00 15.47  ? 144 PHE B HE1  1 
ATOM   5323 H  HE2  . PHE B 1 144 ? -22.958 -24.030 19.556 1.00 15.71  ? 144 PHE B HE2  1 
ATOM   5324 H  HZ   . PHE B 1 144 ? -22.027 -22.142 18.628 1.00 15.42  ? 144 PHE B HZ   1 
ATOM   5325 N  N    . LEU B 1 145 ? -30.018 -21.163 19.620 1.00 8.49   ? 145 LEU B N    1 
ATOM   5326 C  CA   . LEU B 1 145 ? -31.408 -21.406 19.261 1.00 8.92   ? 145 LEU B CA   1 
ATOM   5327 C  C    . LEU B 1 145 ? -31.434 -21.415 17.744 1.00 8.73   ? 145 LEU B C    1 
ATOM   5328 O  O    . LEU B 1 145 ? -31.134 -20.387 17.123 1.00 9.81   ? 145 LEU B O    1 
ATOM   5329 C  CB   . LEU B 1 145 ? -32.328 -20.336 19.845 1.00 9.29   ? 145 LEU B CB   1 
ATOM   5330 C  CG   . LEU B 1 145 ? -32.214 -20.133 21.340 1.00 9.57   ? 145 LEU B CG   1 
ATOM   5331 C  CD1  . LEU B 1 145 ? -33.069 -18.954 21.799 1.00 10.64  ? 145 LEU B CD1  1 
ATOM   5332 C  CD2  . LEU B 1 145 ? -32.571 -21.378 22.107 1.00 10.74  ? 145 LEU B CD2  1 
ATOM   5333 H  H    . LEU B 1 145 ? -29.642 -20.361 19.397 1.00 10.47  ? 145 LEU B H    1 
ATOM   5334 H  HA   . LEU B 1 145 ? -31.676 -22.292 19.593 1.00 13.45  ? 145 LEU B HA   1 
ATOM   5335 H  HB2  . LEU B 1 145 ? -32.135 -19.486 19.401 1.00 13.47  ? 145 LEU B HB2  1 
ATOM   5336 H  HB3  . LEU B 1 145 ? -33.252 -20.576 19.634 1.00 13.47  ? 145 LEU B HB3  1 
ATOM   5337 H  HG   . LEU B 1 145 ? -31.273 -19.916 21.542 1.00 11.55  ? 145 LEU B HG   1 
ATOM   5338 H  HD11 . LEU B 1 145 ? -32.958 -18.825 22.757 1.00 13.12  ? 145 LEU B HD11 1 
ATOM   5339 H  HD12 . LEU B 1 145 ? -32.791 -18.149 21.330 1.00 13.12  ? 145 LEU B HD12 1 
ATOM   5340 H  HD13 . LEU B 1 145 ? -34.005 -19.135 21.604 1.00 13.12  ? 145 LEU B HD13 1 
ATOM   5341 H  HD21 . LEU B 1 145 ? -32.654 -21.165 23.053 1.00 13.10  ? 145 LEU B HD21 1 
ATOM   5342 H  HD22 . LEU B 1 145 ? -33.417 -21.730 21.780 1.00 13.10  ? 145 LEU B HD22 1 
ATOM   5343 H  HD23 . LEU B 1 145 ? -31.875 -22.046 21.987 1.00 13.10  ? 145 LEU B HD23 1 
ATOM   5344 N  N    . THR B 1 146 ? -31.762 -22.556 17.143 1.00 9.12   ? 146 THR B N    1 
ATOM   5345 C  CA   . THR B 1 146 ? -31.823 -22.664 15.704 1.00 8.96   ? 146 THR B CA   1 
ATOM   5346 C  C    . THR B 1 146 ? -33.289 -22.723 15.296 1.00 9.70   ? 146 THR B C    1 
ATOM   5347 O  O    . THR B 1 146 ? -34.092 -23.373 15.941 1.00 10.51  ? 146 THR B O    1 
ATOM   5348 C  CB   . THR B 1 146 ? -30.981 -23.840 15.197 1.00 9.57   ? 146 THR B CB   1 
ATOM   5349 O  OG1  . THR B 1 146 ? -31.510 -25.096 15.580 1.00 10.00  ? 146 THR B OG1  1 
ATOM   5350 C  CG2  . THR B 1 146 ? -29.534 -23.693 15.617 1.00 11.04  ? 146 THR B CG2  1 
ATOM   5351 H  H    . THR B 1 146 ? -31.954 -23.293 17.648 1.00 13.45  ? 146 THR B H    1 
ATOM   5352 H  HA   . THR B 1 146 ? -31.438 -21.839 15.328 1.00 11.42  ? 146 THR B HA   1 
ATOM   5353 H  HB   . THR B 1 146 ? -31.004 -23.800 14.212 1.00 11.72  ? 146 THR B HB   1 
ATOM   5354 H  HG1  . THR B 1 146 ? -31.363 -25.228 16.405 1.00 13.46  ? 146 THR B HG1  1 
ATOM   5355 H  HG21 . THR B 1 146 ? -28.995 -24.371 15.172 1.00 13.46  ? 146 THR B HG21 1 
ATOM   5356 H  HG22 . THR B 1 146 ? -29.210 -22.809 15.369 1.00 13.46  ? 146 THR B HG22 1 
ATOM   5357 H  HG23 . THR B 1 146 ? -29.461 -23.805 16.582 1.00 13.46  ? 146 THR B HG23 1 
ATOM   5358 N  N    . TRP B 1 147 ? -33.633 -21.948 14.271 1.00 9.80   ? 147 TRP B N    1 
ATOM   5359 C  CA   . TRP B 1 147 ? -35.013 -21.787 13.825 1.00 9.87   ? 147 TRP B CA   1 
ATOM   5360 C  C    . TRP B 1 147 ? -35.086 -22.119 12.348 1.00 9.95   ? 147 TRP B C    1 
ATOM   5361 O  O    . TRP B 1 147 ? -34.279 -21.614 11.576 1.00 10.90  ? 147 TRP B O    1 
ATOM   5362 C  CB   . TRP B 1 147 ? -35.445 -20.347 14.093 1.00 10.64  ? 147 TRP B CB   1 
ATOM   5363 C  CG   . TRP B 1 147 ? -36.798 -20.008 13.564 1.00 11.57  ? 147 TRP B CG   1 
ATOM   5364 C  CD1  . TRP B 1 147 ? -37.100 -19.336 12.409 1.00 13.18  ? 147 TRP B CD1  1 
ATOM   5365 C  CD2  . TRP B 1 147 ? -38.055 -20.316 14.187 1.00 11.65  ? 147 TRP B CD2  1 
ATOM   5366 N  NE1  . TRP B 1 147 ? -38.460 -19.211 12.280 1.00 13.55  ? 147 TRP B NE1  1 
ATOM   5367 C  CE2  . TRP B 1 147 ? -39.070 -19.803 13.354 1.00 13.05  ? 147 TRP B CE2  1 
ATOM   5368 C  CE3  . TRP B 1 147 ? -38.419 -21.015 15.334 1.00 12.85  ? 147 TRP B CE3  1 
ATOM   5369 C  CZ2  . TRP B 1 147 ? -40.423 -19.911 13.681 1.00 14.63  ? 147 TRP B CZ2  1 
ATOM   5370 C  CZ3  . TRP B 1 147 ? -39.753 -21.111 15.656 1.00 14.56  ? 147 TRP B CZ3  1 
ATOM   5371 C  CH2  . TRP B 1 147 ? -40.739 -20.592 14.828 1.00 14.86  ? 147 TRP B CH2  1 
ATOM   5372 H  H    . TRP B 1 147 ? -32.978 -21.497 13.820 1.00 11.42  ? 147 TRP B H    1 
ATOM   5373 H  HA   . TRP B 1 147 ? -35.592 -22.396 14.337 1.00 12.35  ? 147 TRP B HA   1 
ATOM   5374 H  HB2  . TRP B 1 147 ? -35.433 -20.197 15.060 1.00 12.93  ? 147 TRP B HB2  1 
ATOM   5375 H  HB3  . TRP B 1 147 ? -34.784 -19.748 13.689 1.00 12.93  ? 147 TRP B HB3  1 
ATOM   5376 H  HD1  . TRP B 1 147 ? -36.469 -18.991 11.796 1.00 16.77  ? 147 TRP B HD1  1 
ATOM   5377 H  HE1  . TRP B 1 147 ? -38.869 -18.797 11.625 1.00 16.77  ? 147 TRP B HE1  1 
ATOM   5378 H  HE3  . TRP B 1 147 ? -37.758 -21.348 15.920 1.00 16.77  ? 147 TRP B HE3  1 
ATOM   5379 H  HZ2  . TRP B 1 147 ? -41.091 -19.577 13.107 1.00 16.77  ? 147 TRP B HZ2  1 
ATOM   5380 H  HZ3  . TRP B 1 147 ? -40.007 -21.565 16.443 1.00 16.77  ? 147 TRP B HZ3  1 
ATOM   5381 H  HH2  . TRP B 1 147 ? -41.643 -20.698 15.066 1.00 16.77  ? 147 TRP B HH2  1 
ATOM   5382 N  N    . PHE B 1 148 ? -36.089 -22.904 11.960 1.00 10.33  ? 148 PHE B N    1 
ATOM   5383 C  CA   . PHE B 1 148 ? -36.252 -23.336 10.591 1.00 10.55  ? 148 PHE B CA   1 
ATOM   5384 C  C    . PHE B 1 148 ? -37.702 -23.219 10.169 1.00 11.41  ? 148 PHE B C    1 
ATOM   5385 O  O    . PHE B 1 148 ? -38.602 -23.381 10.987 1.00 11.78  ? 148 PHE B O    1 
ATOM   5386 C  CB   . PHE B 1 148 ? -35.799 -24.790 10.418 1.00 10.58  ? 148 PHE B CB   1 
ATOM   5387 C  CG   . PHE B 1 148 ? -34.412 -25.016 10.946 1.00 10.32  ? 148 PHE B CG   1 
ATOM   5388 C  CD1  . PHE B 1 148 ? -33.326 -24.706 10.153 1.00 10.36  ? 148 PHE B CD1  1 
ATOM   5389 C  CD2  . PHE B 1 148 ? -34.202 -25.414 12.254 1.00 10.97  ? 148 PHE B CD2  1 
ATOM   5390 C  CE1  . PHE B 1 148 ? -32.045 -24.818 10.653 1.00 10.95  ? 148 PHE B CE1  1 
ATOM   5391 C  CE2  . PHE B 1 148 ? -32.911 -25.522 12.767 1.00 11.17  ? 148 PHE B CE2  1 
ATOM   5392 C  CZ   . PHE B 1 148 ? -31.833 -25.226 11.952 1.00 10.88  ? 148 PHE B CZ   1 
ATOM   5393 H  H    . PHE B 1 148 ? -36.700 -23.182 12.580 1.00 12.35  ? 148 PHE B H    1 
ATOM   5394 H  HA   . PHE B 1 148 ? -35.705 -22.759 10.007 1.00 13.26  ? 148 PHE B HA   1 
ATOM   5395 H  HB2  . PHE B 1 148 ? -36.425 -25.377 10.891 1.00 12.92  ? 148 PHE B HB2  1 
ATOM   5396 H  HB3  . PHE B 1 148 ? -35.825 -25.019 9.465  1.00 12.92  ? 148 PHE B HB3  1 
ATOM   5397 H  HD1  . PHE B 1 148 ? -33.462 -24.405 9.269  1.00 18.41  ? 148 PHE B HD1  1 
ATOM   5398 H  HD2  . PHE B 1 148 ? -34.943 -25.594 12.811 1.00 18.41  ? 148 PHE B HD2  1 
ATOM   5399 H  HE1  . PHE B 1 148 ? -31.307 -24.626 10.096 1.00 18.41  ? 148 PHE B HE1  1 
ATOM   5400 H  HE2  . PHE B 1 148 ? -32.774 -25.820 13.650 1.00 18.41  ? 148 PHE B HE2  1 
ATOM   5401 H  HZ   . PHE B 1 148 ? -30.955 -25.326 12.277 1.00 18.40  ? 148 PHE B HZ   1 
ATOM   5402 N  N    . GLU B 1 149 ? -37.919 -22.977 8.873  1.00 11.66  ? 149 GLU B N    1 
ATOM   5403 C  CA   . GLU B 1 149 ? -39.258 -22.923 8.303  1.00 12.28  ? 149 GLU B CA   1 
ATOM   5404 C  C    . GLU B 1 149 ? -39.280 -23.650 6.966  1.00 12.37  ? 149 GLU B C    1 
ATOM   5405 O  O    . GLU B 1 149 ? -38.343 -23.547 6.179  1.00 12.86  ? 149 GLU B O    1 
ATOM   5406 C  CB   . GLU B 1 149 ? -39.694 -21.481 8.072  1.00 13.74  ? 149 GLU B CB   1 
ATOM   5407 C  CG   . GLU B 1 149 ? -39.679 -20.601 9.299  1.00 14.52  ? 149 GLU B CG   1 
ATOM   5408 C  CD   . GLU B 1 149 ? -39.933 -19.133 9.009  1.00 15.92  ? 149 GLU B CD   1 
ATOM   5409 O  OE1  . GLU B 1 149 ? -40.171 -18.773 7.834  1.00 18.02  ? 149 GLU B OE1  1 
ATOM   5410 O  OE2  . GLU B 1 149 ? -39.932 -18.348 9.976  1.00 16.31  ? 149 GLU B OE2  1 
ATOM   5411 H  H    . GLU B 1 149 ? -37.204 -22.841 8.320  1.00 13.26  ? 149 GLU B H    1 
ATOM   5412 H  HA   . GLU B 1 149 ? -39.886 -23.358 8.920  1.00 15.24  ? 149 GLU B HA   1 
ATOM   5413 H  HB2  . GLU B 1 149 ? -39.104 -21.087 7.396  1.00 15.93  ? 149 GLU B HB2  1 
ATOM   5414 H  HB3  . GLU B 1 149 ? -40.603 -21.490 7.704  1.00 15.93  ? 149 GLU B HB3  1 
ATOM   5415 H  HG2  . GLU B 1 149 ? -40.362 -20.918 9.928  1.00 17.21  ? 149 GLU B HG2  1 
ATOM   5416 H  HG3  . GLU B 1 149 ? -38.808 -20.682 9.741  1.00 17.21  ? 149 GLU B HG3  1 
ATOM   5417 N  N    . TYR B 1 150 ? -40.378 -24.356 6.708  1.00 13.19  ? 150 TYR B N    1 
ATOM   5418 C  CA   . TYR B 1 150 ? -40.505 -25.159 5.494  1.00 13.45  ? 150 TYR B CA   1 
ATOM   5419 C  C    . TYR B 1 150 ? -41.968 -25.484 5.248  1.00 14.69  ? 150 TYR B C    1 
ATOM   5420 O  O    . TYR B 1 150 ? -42.803 -25.408 6.134  1.00 15.09  ? 150 TYR B O    1 
ATOM   5421 C  CB   . TYR B 1 150 ? -39.630 -26.423 5.548  1.00 14.09  ? 150 TYR B CB   1 
ATOM   5422 C  CG   . TYR B 1 150 ? -39.704 -27.152 6.854  1.00 13.22  ? 150 TYR B CG   1 
ATOM   5423 C  CD1  . TYR B 1 150 ? -40.673 -28.109 7.107  1.00 14.33  ? 150 TYR B CD1  1 
ATOM   5424 C  CD2  . TYR B 1 150 ? -38.804 -26.865 7.879  1.00 13.25  ? 150 TYR B CD2  1 
ATOM   5425 C  CE1  . TYR B 1 150 ? -40.782 -28.728 8.339  1.00 14.80  ? 150 TYR B CE1  1 
ATOM   5426 C  CE2  . TYR B 1 150 ? -38.910 -27.465 9.113  1.00 14.12  ? 150 TYR B CE2  1 
ATOM   5427 C  CZ   . TYR B 1 150 ? -39.914 -28.376 9.355  1.00 13.89  ? 150 TYR B CZ   1 
ATOM   5428 O  OH   . TYR B 1 150 ? -39.982 -28.957 10.583 1.00 15.56  ? 150 TYR B OH   1 
ATOM   5429 H  H    . TYR B 1 150 ? -41.073 -24.340 7.301  1.00 15.24  ? 150 TYR B H    1 
ATOM   5430 H  HA   . TYR B 1 150 ? -40.191 -24.608 4.733  1.00 19.66  ? 150 TYR B HA   1 
ATOM   5431 H  HB2  . TYR B 1 150 ? -39.909 -27.027 4.829  1.00 16.85  ? 150 TYR B HB2  1 
ATOM   5432 H  HB3  . TYR B 1 150 ? -38.699 -26.165 5.380  1.00 16.85  ? 150 TYR B HB3  1 
ATOM   5433 H  HD1  . TYR B 1 150 ? -41.303 -28.312 6.437  1.00 14.12  ? 150 TYR B HD1  1 
ATOM   5434 H  HD2  . TYR B 1 150 ? -38.148 -26.201 7.745  1.00 14.12  ? 150 TYR B HD2  1 
ATOM   5435 H  HE1  . TYR B 1 150 ? -41.469 -29.355 8.499  1.00 14.12  ? 150 TYR B HE1  1 
ATOM   5436 H  HE2  . TYR B 1 150 ? -38.308 -27.236 9.802  1.00 14.12  ? 150 TYR B HE2  1 
ATOM   5437 H  HH   . TYR B 1 150 ? -39.274 -29.032 11.068 1.00 14.12  ? 150 TYR B HH   1 
ATOM   5438 N  N    . SER B 1 151 ? -42.265 -25.824 3.994  1.00 16.45  ? 151 SER B N    1 
ATOM   5439 C  CA   . SER B 1 151 ? -43.590 -26.299 3.642  1.00 16.48  ? 151 SER B CA   1 
ATOM   5440 C  C    . SER B 1 151 ? -43.824 -27.700 4.214  1.00 17.37  ? 151 SER B C    1 
ATOM   5441 O  O    . SER B 1 151 ? -42.885 -28.483 4.393  1.00 17.22  ? 151 SER B O    1 
ATOM   5442 C  CB   . SER B 1 151 ? -43.749 -26.277 2.161  1.00 18.52  ? 151 SER B CB   1 
ATOM   5443 O  OG   . SER B 1 151 ? -42.990 -27.310 1.583  1.00 21.34  ? 151 SER B OG   1 
ATOM   5444 H  H    . SER B 1 151 ? -41.628 -25.761 3.342  1.00 19.66  ? 151 SER B H    1 
ATOM   5445 H  HA   . SER B 1 151 ? -44.255 -25.678 4.039  1.00 24.43  ? 151 SER B HA   1 
ATOM   5446 H  HB2  . SER B 1 151 ? -44.698 -26.394 1.929  1.00 20.21  ? 151 SER B HB2  1 
ATOM   5447 H  HB3  . SER B 1 151 ? -43.448 -25.409 1.810  1.00 20.21  ? 151 SER B HB3  1 
ATOM   5448 H  HG   . SER B 1 151 ? -43.142 -27.322 0.751  1.00 23.93  ? 151 SER B HG   1 
ATOM   5449 N  N    . PRO B 1 152 ? -45.097 -28.097 4.399  1.00 17.71  ? 152 PRO B N    1 
ATOM   5450 C  CA   . PRO B 1 152 ? -45.403 -29.460 4.842  1.00 19.72  ? 152 PRO B CA   1 
ATOM   5451 C  C    . PRO B 1 152 ? -44.751 -30.534 3.972  1.00 19.14  ? 152 PRO B C    1 
ATOM   5452 O  O    . PRO B 1 152 ? -44.309 -31.563 4.469  1.00 21.07  ? 152 PRO B O    1 
ATOM   5453 C  CB   . PRO B 1 152 ? -46.943 -29.477 4.821  1.00 20.98  ? 152 PRO B CB   1 
ATOM   5454 C  CG   . PRO B 1 152 ? -47.355 -28.041 5.063  1.00 21.87  ? 152 PRO B CG   1 
ATOM   5455 C  CD   . PRO B 1 152 ? -46.275 -27.213 4.394  1.00 19.29  ? 152 PRO B CD   1 
ATOM   5456 H  HA   . PRO B 1 152 ? -45.095 -29.566 5.777  1.00 23.09  ? 152 PRO B HA   1 
ATOM   5457 H  HB2  . PRO B 1 152 ? -47.276 -29.791 3.955  1.00 23.48  ? 152 PRO B HB2  1 
ATOM   5458 H  HB3  . PRO B 1 152 ? -47.295 -30.062 5.526  1.00 23.48  ? 152 PRO B HB3  1 
ATOM   5459 H  HG2  . PRO B 1 152 ? -48.231 -27.858 4.665  1.00 40.21  ? 152 PRO B HG2  1 
ATOM   5460 H  HG3  . PRO B 1 152 ? -47.396 -27.849 6.021  1.00 40.21  ? 152 PRO B HG3  1 
ATOM   5461 H  HD2  . PRO B 1 152 ? -46.529 -26.975 3.483  1.00 24.44  ? 152 PRO B HD2  1 
ATOM   5462 H  HD3  . PRO B 1 152 ? -46.103 -26.396 4.897  1.00 24.43  ? 152 PRO B HD3  1 
ATOM   5463 N  N    . SER B 1 153 ? -44.750 -30.325 2.658  1.00 18.84  ? 153 SER B N    1 
ATOM   5464 C  CA   . SER B 1 153 ? -44.195 -31.340 1.771  1.00 19.80  ? 153 SER B CA   1 
ATOM   5465 C  C    . SER B 1 153 ? -42.680 -31.467 1.870  1.00 18.69  ? 153 SER B C    1 
ATOM   5466 O  O    . SER B 1 153 ? -42.123 -32.445 1.338  1.00 19.14  ? 153 SER B O    1 
ATOM   5467 C  CB   . SER B 1 153 ? -44.588 -31.075 0.366  1.00 22.87  ? 153 SER B CB   1 
ATOM   5468 O  OG   . SER B 1 153 ? -44.072 -29.842 -0.110 1.00 23.85  ? 153 SER B OG   1 
ATOM   5469 H  H    . SER B 1 153 ? -45.096 -29.556 2.306  1.00 24.33  ? 153 SER B H    1 
ATOM   5470 H  HA   . SER B 1 153 ? -44.588 -32.216 2.035  1.00 22.53  ? 153 SER B HA   1 
ATOM   5471 H  HB2  . SER B 1 153 ? -44.259 -31.806 -0.205 1.00 24.33  ? 153 SER B HB2  1 
ATOM   5472 H  HB3  . SER B 1 153 ? -45.570 -31.061 0.303  1.00 24.33  ? 153 SER B HB3  1 
ATOM   5473 H  HG   . SER B 1 153 ? -44.668 -29.248 -0.026 1.00 24.33  ? 153 SER B HG   1 
ATOM   5474 N  N    . ASP B 1 154 ? -42.034 -30.498 2.533  1.00 17.55  ? 154 ASP B N    1 
ATOM   5475 C  CA   . ASP B 1 154 ? -40.596 -30.538 2.708  1.00 15.67  ? 154 ASP B CA   1 
ATOM   5476 C  C    . ASP B 1 154 ? -40.202 -31.038 4.092  1.00 15.28  ? 154 ASP B C    1 
ATOM   5477 O  O    . ASP B 1 154 ? -39.019 -31.065 4.408  1.00 14.85  ? 154 ASP B O    1 
ATOM   5478 C  CB   . ASP B 1 154 ? -40.026 -29.155 2.403  1.00 15.69  ? 154 ASP B CB   1 
ATOM   5479 C  CG   . ASP B 1 154 ? -39.922 -28.891 0.917  1.00 16.33  ? 154 ASP B CG   1 
ATOM   5480 O  OD1  . ASP B 1 154 ? -39.744 -29.844 0.148  1.00 18.28  ? 154 ASP B OD1  1 
ATOM   5481 O  OD2  . ASP B 1 154 ? -39.975 -27.710 0.540  1.00 17.41  ? 154 ASP B OD2  1 
ATOM   5482 H  H    . ASP B 1 154 ? -42.498 -29.787 2.869  1.00 18.58  ? 154 ASP B H    1 
ATOM   5483 H  HA   . ASP B 1 154 ? -40.227 -31.167 2.046  1.00 17.71  ? 154 ASP B HA   1 
ATOM   5484 H  HB2  . ASP B 1 154 ? -40.600 -28.470 2.803  1.00 18.58  ? 154 ASP B HB2  1 
ATOM   5485 H  HB3  . ASP B 1 154 ? -39.133 -29.074 2.794  1.00 18.58  ? 154 ASP B HB3  1 
ATOM   5486 N  N    . GLU B 1 155 ? -41.174 -31.455 4.898  1.00 16.46  ? 155 GLU B N    1 
ATOM   5487 C  CA   . GLU B 1 155 ? -40.870 -31.934 6.232  1.00 15.94  ? 155 GLU B CA   1 
ATOM   5488 C  C    . GLU B 1 155 ? -39.963 -33.167 6.234  1.00 15.32  ? 155 GLU B C    1 
ATOM   5489 O  O    . GLU B 1 155 ? -39.031 -33.251 7.041  1.00 15.29  ? 155 GLU B O    1 
ATOM   5490 C  CB   . GLU B 1 155 ? -42.151 -32.232 6.990  1.00 18.72  ? 155 GLU B CB   1 
ATOM   5491 C  CG   . GLU B 1 155 ? -41.911 -32.708 8.385  1.00 20.81  ? 155 GLU B CG   1 
ATOM   5492 C  CD   . GLU B 1 155 ? -43.215 -32.989 9.126  1.00 21.94  ? 155 GLU B CD   1 
ATOM   5493 O  OE1  . GLU B 1 155 ? -44.163 -33.530 8.519  1.00 24.81  ? 155 GLU B OE1  1 
ATOM   5494 O  OE2  . GLU B 1 155 ? -43.284 -32.683 10.293 1.00 25.19  ? 155 GLU B OE2  1 
ATOM   5495 H  H    . GLU B 1 155 ? -42.044 -31.443 4.618  1.00 19.49  ? 155 GLU B H    1 
ATOM   5496 H  HA   . GLU B 1 155 ? -40.397 -31.211 6.706  1.00 18.74  ? 155 GLU B HA   1 
ATOM   5497 H  HB2  . GLU B 1 155 ? -42.697 -31.419 7.020  1.00 21.01  ? 155 GLU B HB2  1 
ATOM   5498 H  HB3  . GLU B 1 155 ? -42.653 -32.916 6.500  1.00 21.01  ? 155 GLU B HB3  1 
ATOM   5499 H  HG2  . GLU B 1 155 ? -41.378 -33.531 8.364  1.00 23.55  ? 155 GLU B HG2  1 
ATOM   5500 H  HG3  . GLU B 1 155 ? -41.403 -32.030 8.878  1.00 23.55  ? 155 GLU B HG3  1 
ATOM   5501 N  N    . THR B 1 156 ? -40.215 -34.129 5.340  1.00 15.26  ? 156 THR B N    1 
ATOM   5502 C  CA   . THR B 1 156 ? -39.359 -35.300 5.336  1.00 15.50  ? 156 THR B CA   1 
ATOM   5503 C  C    . THR B 1 156 ? -37.939 -34.940 4.900  1.00 14.88  ? 156 THR B C    1 
ATOM   5504 O  O    . THR B 1 156 ? -37.008 -35.525 5.420  1.00 15.50  ? 156 THR B O    1 
ATOM   5505 C  CB   . THR B 1 156 ? -39.941 -36.447 4.512  1.00 18.07  ? 156 THR B CB   1 
ATOM   5506 O  OG1  . THR B 1 156 ? -40.174 -35.996 3.190  1.00 20.15  ? 156 THR B OG1  1 
ATOM   5507 C  CG2  . THR B 1 156 ? -41.231 -36.966 5.090  1.00 20.96  ? 156 THR B CG2  1 
ATOM   5508 H  H    . THR B 1 156 ? -40.906 -34.061 4.745  1.00 21.92  ? 156 THR B H    1 
ATOM   5509 H  HA   . THR B 1 156 ? -39.305 -35.615 6.268  1.00 20.93  ? 156 THR B HA   1 
ATOM   5510 H  HB   . THR B 1 156 ? -39.281 -37.181 4.490  1.00 21.73  ? 156 THR B HB   1 
ATOM   5511 H  HG1  . THR B 1 156 ? -40.288 -36.663 2.678  1.00 22.80  ? 156 THR B HG1  1 
ATOM   5512 H  HG21 . THR B 1 156 ? -41.450 -37.820 4.678  1.00 20.93  ? 156 THR B HG21 1 
ATOM   5513 H  HG22 . THR B 1 156 ? -41.131 -37.088 6.051  1.00 20.93  ? 156 THR B HG22 1 
ATOM   5514 H  HG23 . THR B 1 156 ? -41.946 -36.331 4.918  1.00 20.93  ? 156 THR B HG23 1 
ATOM   5515 N  N    . ALA B 1 157 ? -37.769 -33.953 4.012  1.00 14.40  ? 157 ALA B N    1 
ATOM   5516 C  CA   . ALA B 1 157 ? -36.434 -33.502 3.654  1.00 14.42  ? 157 ALA B CA   1 
ATOM   5517 C  C    . ALA B 1 157 ? -35.760 -32.877 4.877  1.00 13.08  ? 157 ALA B C    1 
ATOM   5518 O  O    . ALA B 1 157 ? -34.596 -33.150 5.131  1.00 13.85  ? 157 ALA B O    1 
ATOM   5519 C  CB   . ALA B 1 157 ? -36.505 -32.537 2.494  1.00 15.48  ? 157 ALA B CB   1 
ATOM   5520 H  H    . ALA B 1 157 ? -38.494 -33.560 3.618  1.00 17.21  ? 157 ALA B H    1 
ATOM   5521 H  HA   . ALA B 1 157 ? -35.905 -34.287 3.377  1.00 17.16  ? 157 ALA B HA   1 
ATOM   5522 H  HB1  . ALA B 1 157 ? -35.607 -32.259 2.246  1.00 18.39  ? 157 ALA B HB1  1 
ATOM   5523 H  HB2  . ALA B 1 157 ? -36.930 -32.971 1.735  1.00 18.39  ? 157 ALA B HB2  1 
ATOM   5524 H  HB3  . ALA B 1 157 ? -37.024 -31.756 2.751  1.00 18.39  ? 157 ALA B HB3  1 
ATOM   5525 N  N    . PHE B 1 158 ? -36.489 -32.056 5.647  1.00 13.04  ? 158 PHE B N    1 
ATOM   5526 C  CA   . PHE B 1 158 ? -35.910 -31.495 6.858  1.00 12.11  ? 158 PHE B CA   1 
ATOM   5527 C  C    . PHE B 1 158 ? -35.467 -32.595 7.820  1.00 12.41  ? 158 PHE B C    1 
ATOM   5528 O  O    . PHE B 1 158 ? -34.378 -32.534 8.404  1.00 12.30  ? 158 PHE B O    1 
ATOM   5529 C  CB   . PHE B 1 158 ? -36.924 -30.555 7.499  1.00 12.54  ? 158 PHE B CB   1 
ATOM   5530 C  CG   . PHE B 1 158 ? -36.401 -29.896 8.759  1.00 11.51  ? 158 PHE B CG   1 
ATOM   5531 C  CD1  . PHE B 1 158 ? -35.407 -28.942 8.674  1.00 11.47  ? 158 PHE B CD1  1 
ATOM   5532 C  CD2  . PHE B 1 158 ? -36.883 -30.236 10.008 1.00 12.36  ? 158 PHE B CD2  1 
ATOM   5533 C  CE1  . PHE B 1 158 ? -34.912 -28.331 9.822  1.00 11.66  ? 158 PHE B CE1  1 
ATOM   5534 C  CE2  . PHE B 1 158 ? -36.411 -29.602 11.145 1.00 12.50  ? 158 PHE B CE2  1 
ATOM   5535 C  CZ   . PHE B 1 158 ? -35.410 -28.668 11.057 1.00 11.82  ? 158 PHE B CZ   1 
ATOM   5536 H  H    . PHE B 1 158 ? -37.346 -31.841 5.415  1.00 15.48  ? 158 PHE B H    1 
ATOM   5537 H  HA   . PHE B 1 158 ? -35.110 -30.967 6.605  1.00 14.52  ? 158 PHE B HA   1 
ATOM   5538 H  HB2  . PHE B 1 158 ? -37.164 -29.861 6.850  1.00 15.14  ? 158 PHE B HB2  1 
ATOM   5539 H  HB3  . PHE B 1 158 ? -37.733 -31.063 7.714  1.00 15.14  ? 158 PHE B HB3  1 
ATOM   5540 H  HD1  . PHE B 1 158 ? -35.057 -28.708 7.829  1.00 15.14  ? 158 PHE B HD1  1 
ATOM   5541 H  HD2  . PHE B 1 158 ? -37.572 -30.877 10.082 1.00 15.14  ? 158 PHE B HD2  1 
ATOM   5542 H  HE1  . PHE B 1 158 ? -34.234 -27.678 9.751  1.00 15.14  ? 158 PHE B HE1  1 
ATOM   5543 H  HE2  . PHE B 1 158 ? -36.749 -29.848 11.992 1.00 15.14  ? 158 PHE B HE2  1 
ATOM   5544 H  HZ   . PHE B 1 158 ? -35.080 -28.248 11.835 1.00 15.14  ? 158 PHE B HZ   1 
ATOM   5545 N  N    . ASN B 1 159 ? -36.298 -33.617 7.995  1.00 12.57  ? 159 ASN B N    1 
ATOM   5546 C  CA   . ASN B 1 159 ? -35.952 -34.712 8.888  1.00 13.37  ? 159 ASN B CA   1 
ATOM   5547 C  C    . ASN B 1 159 ? -34.697 -35.419 8.393  1.00 12.90  ? 159 ASN B C    1 
ATOM   5548 O  O    . ASN B 1 159 ? -33.875 -35.857 9.198  1.00 13.58  ? 159 ASN B O    1 
ATOM   5549 C  CB   . ASN B 1 159 ? -37.090 -35.711 9.028  1.00 14.42  ? 159 ASN B CB   1 
ATOM   5550 C  CG   . ASN B 1 159 ? -38.303 -35.138 9.733  1.00 14.60  ? 159 ASN B CG   1 
ATOM   5551 O  OD1  . ASN B 1 159 ? -38.227 -34.120 10.417 1.00 15.50  ? 159 ASN B OD1  1 
ATOM   5552 N  ND2  . ASN B 1 159 ? -39.437 -35.793 9.574  1.00 17.53  ? 159 ASN B ND2  1 
ATOM   5553 H  H    . ASN B 1 159 ? -37.099 -33.637 7.555  1.00 17.54  ? 159 ASN B H    1 
ATOM   5554 H  HA   . ASN B 1 159 ? -35.769 -34.337 9.781  1.00 16.44  ? 159 ASN B HA   1 
ATOM   5555 H  HB2  . ASN B 1 159 ? -37.355 -36.016 8.136  1.00 18.81  ? 159 ASN B HB2  1 
ATOM   5556 H  HB3  . ASN B 1 159 ? -36.769 -36.488 9.529  1.00 18.81  ? 159 ASN B HB3  1 
ATOM   5557 H  HD21 . ASN B 1 159 ? -40.189 -35.459 9.897  1.00 18.81  ? 159 ASN B HD21 1 
ATOM   5558 H  HD22 . ASN B 1 159 ? -39.447 -36.566 9.145  1.00 18.81  ? 159 ASN B HD22 1 
ATOM   5559 N  N    . ARG B 1 160 ? -34.550 -35.557 7.074  1.00 13.28  ? 160 ARG B N    1 
ATOM   5560 C  CA   . ARG B 1 160 ? -33.365 -36.196 6.524  1.00 13.65  ? 160 ARG B CA   1 
ATOM   5561 C  C    . ARG B 1 160 ? -32.099 -35.361 6.782  1.00 12.83  ? 160 ARG B C    1 
ATOM   5562 O  O    . ARG B 1 160 ? -31.053 -35.901 7.128  1.00 13.56  ? 160 ARG B O    1 
ATOM   5563 C  CB   . ARG B 1 160 ? -33.578 -36.442 5.025  1.00 14.40  ? 160 ARG B CB   1 
ATOM   5564 C  CG   . ARG B 1 160 ? -32.424 -37.204 4.404  1.00 15.77  ? 160 ARG B CG   1 
ATOM   5565 C  CD   . ARG B 1 160 ? -32.317 -38.585 4.985  1.00 19.09  ? 160 ARG B CD   1 
ATOM   5566 N  NE   . ARG B 1 160 ? -31.141 -39.238 4.479  1.00 22.75  ? 160 ARG B NE   1 
ATOM   5567 C  CZ   . ARG B 1 160 ? -31.082 -39.886 3.325  1.00 21.49  ? 160 ARG B CZ   1 
ATOM   5568 N  NH1  . ARG B 1 160 ? -32.147 -39.995 2.553  1.00 21.32  ? 160 ARG B NH1  1 
ATOM   5569 N  NH2  . ARG B 1 160 ? -29.962 -40.473 2.953  1.00 26.17  ? 160 ARG B NH2  1 
ATOM   5570 H  H    . ARG B 1 160 ? -35.200 -35.256 6.506  1.00 17.41  ? 160 ARG B H    1 
ATOM   5571 H  HA   . ARG B 1 160 ? -33.258 -37.064 6.972  1.00 26.93  ? 160 ARG B HA   1 
ATOM   5572 H  HB2  . ARG B 1 160 ? -34.406 -36.952 4.900  1.00 17.53  ? 160 ARG B HB2  1 
ATOM   5573 H  HB3  . ARG B 1 160 ? -33.676 -35.580 4.570  1.00 17.53  ? 160 ARG B HB3  1 
ATOM   5574 H  HG2  . ARG B 1 160 ? -32.561 -37.271 3.435  1.00 28.17  ? 160 ARG B HG2  1 
ATOM   5575 H  HG3  . ARG B 1 160 ? -31.586 -36.722 4.562  1.00 28.17  ? 160 ARG B HG3  1 
ATOM   5576 H  HD2  . ARG B 1 160 ? -32.268 -38.533 5.961  1.00 28.92  ? 160 ARG B HD2  1 
ATOM   5577 H  HD3  . ARG B 1 160 ? -33.113 -39.104 4.745  1.00 28.91  ? 160 ARG B HD3  1 
ATOM   5578 H  HE   . ARG B 1 160 ? -30.416 -39.206 4.965  1.00 27.23  ? 160 ARG B HE   1 
ATOM   5579 H  HH11 . ARG B 1 160 ? -32.657 -39.294 2.403  1.00 28.42  ? 160 ARG B HH11 1 
ATOM   5580 H  HH12 . ARG B 1 160 ? -32.340 -40.769 2.184  1.00 28.42  ? 160 ARG B HH12 1 
ATOM   5581 H  HH21 . ARG B 1 160 ? -29.371 -40.712 3.558  1.00 27.23  ? 160 ARG B HH21 1 
ATOM   5582 H  HH22 . ARG B 1 160 ? -29.811 -40.624 2.101  1.00 27.23  ? 160 ARG B HH22 1 
ATOM   5583 N  N    . LEU B 1 161 ? -32.212 -34.047 6.598  1.00 12.18  ? 161 LEU B N    1 
ATOM   5584 C  CA   . LEU B 1 161 ? -31.134 -33.125 6.962  1.00 12.29  ? 161 LEU B CA   1 
ATOM   5585 C  C    . LEU B 1 161 ? -30.708 -33.357 8.419  1.00 11.68  ? 161 LEU B C    1 
ATOM   5586 O  O    . LEU B 1 161 ? -29.508 -33.455 8.720  1.00 11.88  ? 161 LEU B O    1 
ATOM   5587 C  CB   . LEU B 1 161 ? -31.621 -31.691 6.742  1.00 12.41  ? 161 LEU B CB   1 
ATOM   5588 C  CG   . LEU B 1 161 ? -30.807 -30.578 7.397  1.00 12.50  ? 161 LEU B CG   1 
ATOM   5589 C  CD1  . LEU B 1 161 ? -29.386 -30.534 6.872  1.00 13.67  ? 161 LEU B CD1  1 
ATOM   5590 C  CD2  . LEU B 1 161 ? -31.521 -29.260 7.177  1.00 14.08  ? 161 LEU B CD2  1 
ATOM   5591 H  H    . LEU B 1 161 ? -32.976 -33.710 6.226  1.00 15.52  ? 161 LEU B H    1 
ATOM   5592 H  HA   . LEU B 1 161 ? -30.362 -33.302 6.375  1.00 15.23  ? 161 LEU B HA   1 
ATOM   5593 H  HB2  . LEU B 1 161 ? -31.645 -31.525 5.779  1.00 15.52  ? 161 LEU B HB2  1 
ATOM   5594 H  HB3  . LEU B 1 161 ? -32.540 -31.629 7.069  1.00 15.52  ? 161 LEU B HB3  1 
ATOM   5595 H  HG   . LEU B 1 161 ? -30.772 -30.748 8.370  1.00 15.38  ? 161 LEU B HG   1 
ATOM   5596 H  HD11 . LEU B 1 161 ? -28.896 -29.823 7.320  1.00 16.12  ? 161 LEU B HD11 1 
ATOM   5597 H  HD12 . LEU B 1 161 ? -28.948 -31.386 7.045  1.00 16.12  ? 161 LEU B HD12 1 
ATOM   5598 H  HD13 . LEU B 1 161 ? -29.397 -30.365 5.914  1.00 16.12  ? 161 LEU B HD13 1 
ATOM   5599 H  HD21 . LEU B 1 161 ? -31.043 -28.551 7.640  1.00 15.49  ? 161 LEU B HD21 1 
ATOM   5600 H  HD22 . LEU B 1 161 ? -31.553 -29.061 6.225  1.00 15.49  ? 161 LEU B HD22 1 
ATOM   5601 H  HD23 . LEU B 1 161 ? -32.428 -29.319 7.526  1.00 15.49  ? 161 LEU B HD23 1 
ATOM   5602 N  N    . LEU B 1 162 ? -31.678 -33.401 9.332  1.00 11.66  ? 162 LEU B N    1 
ATOM   5603 C  CA   . LEU B 1 162 ? -31.345 -33.592 10.721 1.00 11.79  ? 162 LEU B CA   1 
ATOM   5604 C  C    . LEU B 1 162 ? -30.615 -34.913 10.932 1.00 12.29  ? 162 LEU B C    1 
ATOM   5605 O  O    . LEU B 1 162 ? -29.666 -34.982 11.709 1.00 13.01  ? 162 LEU B O    1 
ATOM   5606 C  CB   . LEU B 1 162 ? -32.610 -33.585 11.579 1.00 11.82  ? 162 LEU B CB   1 
ATOM   5607 C  CG   . LEU B 1 162 ? -33.312 -32.246 11.698 1.00 11.98  ? 162 LEU B CG   1 
ATOM   5608 C  CD1  . LEU B 1 162 ? -34.628 -32.430 12.423 1.00 12.85  ? 162 LEU B CD1  1 
ATOM   5609 C  CD2  . LEU B 1 162 ? -32.449 -31.230 12.422 1.00 13.22  ? 162 LEU B CD2  1 
ATOM   5610 H  H    . LEU B 1 162 ? -32.553 -33.306 9.086  1.00 14.44  ? 162 LEU B H    1 
ATOM   5611 H  HA   . LEU B 1 162 ? -30.753 -32.858 11.002 1.00 15.61  ? 162 LEU B HA   1 
ATOM   5612 H  HB2  . LEU B 1 162 ? -33.239 -34.232 11.203 1.00 14.45  ? 162 LEU B HB2  1 
ATOM   5613 H  HB3  . LEU B 1 162 ? -32.374 -33.891 12.477 1.00 14.45  ? 162 LEU B HB3  1 
ATOM   5614 H  HG   . LEU B 1 162 ? -33.500 -31.907 10.788 1.00 14.44  ? 162 LEU B HG   1 
ATOM   5615 H  HD11 . LEU B 1 162 ? -35.013 -31.560 12.625 1.00 15.62  ? 162 LEU B HD11 1 
ATOM   5616 H  HD12 . LEU B 1 162 ? -35.241 -32.933 11.860 1.00 15.62  ? 162 LEU B HD12 1 
ATOM   5617 H  HD13 . LEU B 1 162 ? -34.476 -32.916 13.252 1.00 15.62  ? 162 LEU B HD13 1 
ATOM   5618 H  HD21 . LEU B 1 162 ? -32.974 -30.432 12.611 1.00 15.61  ? 162 LEU B HD21 1 
ATOM   5619 H  HD22 . LEU B 1 162 ? -32.130 -31.612 13.258 1.00 15.61  ? 162 LEU B HD22 1 
ATOM   5620 H  HD23 . LEU B 1 162 ? -31.689 -30.992 11.865 1.00 15.61  ? 162 LEU B HD23 1 
ATOM   5621 N  N    . ALA B 1 163 ? -31.069 -35.987 10.270 1.00 12.95  ? 163 ALA B N    1 
ATOM   5622 C  CA   . ALA B 1 163 ? -30.403 -37.272 10.408 1.00 14.18  ? 163 ALA B CA   1 
ATOM   5623 C  C    . ALA B 1 163 ? -28.941 -37.158 9.965  1.00 14.53  ? 163 ALA B C    1 
ATOM   5624 O  O    . ALA B 1 163 ? -28.035 -37.744 10.565 1.00 15.46  ? 163 ALA B O    1 
ATOM   5625 C  CB   . ALA B 1 163 ? -31.181 -38.340 9.675  1.00 16.22  ? 163 ALA B CB   1 
ATOM   5626 H  H    . ALA B 1 163 ? -31.804 -35.920 9.731  1.00 15.64  ? 163 ALA B H    1 
ATOM   5627 H  HA   . ALA B 1 163 ? -30.404 -37.505 11.366 1.00 17.41  ? 163 ALA B HA   1 
ATOM   5628 H  HB1  . ALA B 1 163 ? -30.679 -39.172 9.682  1.00 31.32  ? 163 ALA B HB1  1 
ATOM   5629 H  HB2  . ALA B 1 163 ? -32.038 -38.477 10.114 1.00 31.32  ? 163 ALA B HB2  1 
ATOM   5630 H  HB3  . ALA B 1 163 ? -31.331 -38.060 8.756  1.00 31.33  ? 163 ALA B HB3  1 
ATOM   5631 N  N    . GLU B 1 164 ? -28.702 -36.464 8.858  1.00 14.39  ? 164 GLU B N    1 
ATOM   5632 C  CA   . GLU B 1 164 ? -27.346 -36.327 8.328  1.00 14.17  ? 164 GLU B CA   1 
ATOM   5633 C  C    . GLU B 1 164 ? -26.488 -35.556 9.336  1.00 12.85  ? 164 GLU B C    1 
ATOM   5634 O  O    . GLU B 1 164 ? -25.372 -35.962 9.675  1.00 13.88  ? 164 GLU B O    1 
ATOM   5635 C  CB   . GLU B 1 164 ? -27.327 -35.631 6.966  1.00 15.59  ? 164 GLU B CB   1 
ATOM   5636 C  CG   . GLU B 1 164 ? -27.890 -36.376 5.752  1.00 19.39  ? 164 GLU B CG   1 
ATOM   5637 C  CD   . GLU B 1 164 ? -27.294 -35.747 4.481  1.00 21.09  ? 164 GLU B CD   1 
ATOM   5638 O  OE1  . GLU B 1 164 ? -26.047 -35.800 4.306  1.00 23.93  ? 164 GLU B OE1  1 
ATOM   5639 O  OE2  . GLU B 1 164 ? -28.043 -35.156 3.694  1.00 25.57  ? 164 GLU B OE2  1 
ATOM   5640 H  H    . GLU B 1 164 ? -29.394 -36.068 8.411  1.00 18.48  ? 164 GLU B H    1 
ATOM   5641 H  HA   . GLU B 1 164 ? -26.966 -37.230 8.223  1.00 16.83  ? 164 GLU B HA   1 
ATOM   5642 H  HB2  . GLU B 1 164 ? -27.823 -34.791 7.058  1.00 18.48  ? 164 GLU B HB2  1 
ATOM   5643 H  HB3  . GLU B 1 164 ? -26.396 -35.394 6.771  1.00 18.48  ? 164 GLU B HB3  1 
ATOM   5644 H  HG2  . GLU B 1 164 ? -27.647 -37.326 5.796  1.00 32.48  ? 164 GLU B HG2  1 
ATOM   5645 H  HG3  . GLU B 1 164 ? -28.867 -36.300 5.731  1.00 32.48  ? 164 GLU B HG3  1 
ATOM   5646 N  N    . LEU B 1 165 ? -26.979 -34.431 9.852  1.00 12.48  ? 165 LEU B N    1 
ATOM   5647 C  CA   . LEU B 1 165 ? -26.191 -33.653 10.791 1.00 12.05  ? 165 LEU B CA   1 
ATOM   5648 C  C    . LEU B 1 165 ? -25.977 -34.396 12.102 1.00 12.25  ? 165 LEU B C    1 
ATOM   5649 O  O    . LEU B 1 165 ? -24.872 -34.370 12.657 1.00 12.24  ? 165 LEU B O    1 
ATOM   5650 C  CB   . LEU B 1 165 ? -26.869 -32.307 11.050 1.00 12.24  ? 165 LEU B CB   1 
ATOM   5651 C  CG   . LEU B 1 165 ? -26.897 -31.339 9.871  1.00 13.07  ? 165 LEU B CG   1 
ATOM   5652 C  CD1  . LEU B 1 165 ? -27.603 -30.066 10.300 1.00 13.72  ? 165 LEU B CD1  1 
ATOM   5653 C  CD2  . LEU B 1 165 ? -25.512 -31.052 9.293  1.00 14.14  ? 165 LEU B CD2  1 
ATOM   5654 H  H    . LEU B 1 165 ? -27.813 -34.140 9.615  1.00 14.76  ? 165 LEU B H    1 
ATOM   5655 H  HA   . LEU B 1 165 ? -25.309 -33.492 10.384 1.00 16.53  ? 165 LEU B HA   1 
ATOM   5656 H  HB2  . LEU B 1 165 ? -27.790 -32.477 11.332 1.00 14.76  ? 165 LEU B HB2  1 
ATOM   5657 H  HB3  . LEU B 1 165 ? -26.411 -31.871 11.796 1.00 14.76  ? 165 LEU B HB3  1 
ATOM   5658 H  HG   . LEU B 1 165 ? -27.439 -31.754 9.156  1.00 15.77  ? 165 LEU B HG   1 
ATOM   5659 H  HD11 . LEU B 1 165 ? -27.661 -29.456 9.544  1.00 16.49  ? 165 LEU B HD11 1 
ATOM   5660 H  HD12 . LEU B 1 165 ? -28.499 -30.281 10.612 1.00 16.49  ? 165 LEU B HD12 1 
ATOM   5661 H  HD13 . LEU B 1 165 ? -27.102 -29.643 11.019 1.00 16.49  ? 165 LEU B HD13 1 
ATOM   5662 H  HD21 . LEU B 1 165 ? -25.547 -30.248 8.747  1.00 16.53  ? 165 LEU B HD21 1 
ATOM   5663 H  HD22 . LEU B 1 165 ? -24.878 -30.922 10.020 1.00 16.53  ? 165 LEU B HD22 1 
ATOM   5664 H  HD23 . LEU B 1 165 ? -25.227 -31.804 8.745  1.00 16.53  ? 165 LEU B HD23 1 
ATOM   5665 N  N    . ARG B 1 166 ? -26.996 -35.104 12.592 1.00 12.03  ? 166 ARG B N    1 
ATOM   5666 C  CA   . ARG B 1 166 ? -26.869 -35.776 13.881 1.00 12.86  ? 166 ARG B CA   1 
ATOM   5667 C  C    . ARG B 1 166 ? -25.880 -36.943 13.832 1.00 13.68  ? 166 ARG B C    1 
ATOM   5668 O  O    . ARG B 1 166 ? -25.392 -37.352 14.879 1.00 14.65  ? 166 ARG B O    1 
ATOM   5669 C  CB   . ARG B 1 166 ? -28.261 -36.169 14.384 1.00 13.37  ? 166 ARG B CB   1 
ATOM   5670 C  CG   . ARG B 1 166 ? -29.053 -34.958 14.858 1.00 13.13  ? 166 ARG B CG   1 
ATOM   5671 C  CD   . ARG B 1 166 ? -30.507 -35.286 15.073 1.00 13.30  ? 166 ARG B CD   1 
ATOM   5672 N  NE   . ARG B 1 166 ? -31.237 -34.126 15.525 1.00 12.79  ? 166 ARG B NE   1 
ATOM   5673 C  CZ   . ARG B 1 166 ? -32.567 -34.039 15.518 1.00 12.53  ? 166 ARG B CZ   1 
ATOM   5674 N  NH1  . ARG B 1 166 ? -33.302 -35.049 15.075 1.00 13.58  ? 166 ARG B NH1  1 
ATOM   5675 N  NH2  . ARG B 1 166 ? -33.159 -32.946 16.005 1.00 12.81  ? 166 ARG B NH2  1 
ATOM   5676 H  H    . ARG B 1 166 ? -27.780 -35.169 12.127 1.00 16.14  ? 166 ARG B H    1 
ATOM   5677 H  HA   . ARG B 1 166 ? -26.508 -35.117 14.513 1.00 15.44  ? 166 ARG B HA   1 
ATOM   5678 H  HB2  . ARG B 1 166 ? -28.751 -36.613 13.660 1.00 16.14  ? 166 ARG B HB2  1 
ATOM   5679 H  HB3  . ARG B 1 166 ? -28.166 -36.803 15.125 1.00 16.14  ? 166 ARG B HB3  1 
ATOM   5680 H  HG2  . ARG B 1 166 ? -28.672 -34.632 15.700 1.00 15.71  ? 166 ARG B HG2  1 
ATOM   5681 H  HG3  . ARG B 1 166 ? -28.981 -34.240 14.194 1.00 15.71  ? 166 ARG B HG3  1 
ATOM   5682 H  HD2  . ARG B 1 166 ? -30.894 -35.610 14.232 1.00 15.91  ? 166 ARG B HD2  1 
ATOM   5683 H  HD3  . ARG B 1 166 ? -30.585 -36.001 15.740 1.00 15.91  ? 166 ARG B HD3  1 
ATOM   5684 H  HE   . ARG B 1 166 ? -30.784 -33.441 15.814 1.00 15.85  ? 166 ARG B HE   1 
ATOM   5685 H  HH11 . ARG B 1 166 ? -33.248 -35.836 15.468 1.00 15.66  ? 166 ARG B HH11 1 
ATOM   5686 H  HH12 . ARG B 1 166 ? -33.845 -34.929 14.392 1.00 15.66  ? 166 ARG B HH12 1 
ATOM   5687 H  HH21 . ARG B 1 166 ? -32.683 -32.340 16.428 1.00 15.85  ? 166 ARG B HH21 1 
ATOM   5688 H  HH22 . ARG B 1 166 ? -34.024 -32.835 15.900 1.00 15.85  ? 166 ARG B HH22 1 
ATOM   5689 N  N    . ALA B 1 167 ? -25.569 -37.447 12.632 1.00 14.73  ? 167 ALA B N    1 
ATOM   5690 C  CA   . ALA B 1 167 ? -24.559 -38.489 12.454 1.00 15.93  ? 167 ALA B CA   1 
ATOM   5691 C  C    . ALA B 1 167 ? -23.141 -37.919 12.334 1.00 16.27  ? 167 ALA B C    1 
ATOM   5692 O  O    . ALA B 1 167 ? -22.189 -38.689 12.319 1.00 19.34  ? 167 ALA B O    1 
ATOM   5693 C  CB   . ALA B 1 167 ? -24.915 -39.311 11.232 1.00 17.33  ? 167 ALA B CB   1 
ATOM   5694 H  H    . ALA B 1 167 ? -26.014 -37.144 11.894 1.00 19.31  ? 167 ALA B H    1 
ATOM   5695 H  HA   . ALA B 1 167 ? -24.583 -39.081 13.242 1.00 48.24  ? 167 ALA B HA   1 
ATOM   5696 H  HB1  . ALA B 1 167 ? -24.251 -40.010 11.105 1.00 19.50  ? 167 ALA B HB1  1 
ATOM   5697 H  HB2  . ALA B 1 167 ? -25.790 -39.716 11.356 1.00 19.50  ? 167 ALA B HB2  1 
ATOM   5698 H  HB3  . ALA B 1 167 ? -24.933 -38.738 10.448 1.00 19.50  ? 167 ALA B HB3  1 
ATOM   5699 N  N    . SER B 1 168 ? -22.973 -36.600 12.283 1.00 15.28  ? 168 SER B N    1 
ATOM   5700 C  CA   . SER B 1 168 ? -21.682 -35.988 12.004 1.00 14.89  ? 168 SER B CA   1 
ATOM   5701 C  C    . SER B 1 168 ? -20.790 -35.939 13.252 1.00 14.10  ? 168 SER B C    1 
ATOM   5702 O  O    . SER B 1 168 ? -21.254 -35.968 14.386 1.00 15.19  ? 168 SER B O    1 
ATOM   5703 C  CB   . SER B 1 168 ? -21.868 -34.592 11.400 1.00 14.80  ? 168 SER B CB   1 
ATOM   5704 O  OG   . SER B 1 168 ? -22.258 -33.645 12.390 1.00 14.48  ? 168 SER B OG   1 
ATOM   5705 H  H    . SER B 1 168 ? -23.689 -36.053 12.427 1.00 17.78  ? 168 SER B H    1 
ATOM   5706 H  HA   . SER B 1 168 ? -21.223 -36.553 11.327 1.00 17.74  ? 168 SER B HA   1 
ATOM   5707 H  HB2  . SER B 1 168 ? -21.024 -34.304 10.986 1.00 15.95  ? 168 SER B HB2  1 
ATOM   5708 H  HB3  . SER B 1 168 ? -22.555 -34.632 10.697 1.00 15.95  ? 168 SER B HB3  1 
ATOM   5709 H  HG   . SER B 1 168 ? -23.087 -33.734 12.534 1.00 17.78  ? 168 SER B HG   1 
ATOM   5710 N  N    . VAL B 1 169 ? -19.480 -35.760 13.014 1.00 14.57  ? 169 VAL B N    1 
ATOM   5711 C  CA   . VAL B 1 169 ? -18.502 -35.572 14.085 1.00 15.67  ? 169 VAL B CA   1 
ATOM   5712 C  C    . VAL B 1 169 ? -18.921 -34.433 14.999 1.00 14.72  ? 169 VAL B C    1 
ATOM   5713 O  O    . VAL B 1 169 ? -18.820 -34.530 16.221 1.00 16.14  ? 169 VAL B O    1 
ATOM   5714 C  CB   . VAL B 1 169 ? -17.071 -35.323 13.525 1.00 18.03  ? 169 VAL B CB   1 
ATOM   5715 C  CG1  . VAL B 1 169 ? -16.065 -34.978 14.633 1.00 18.06  ? 169 VAL B CG1  1 
ATOM   5716 C  CG2  . VAL B 1 169 ? -16.608 -36.499 12.723 1.00 19.96  ? 169 VAL B CG2  1 
ATOM   5717 H  H    . VAL B 1 169 ? -19.188 -35.744 12.148 1.00 17.82  ? 169 VAL B H    1 
ATOM   5718 H  HA   . VAL B 1 169 ? -18.480 -36.389 14.615 1.00 21.71  ? 169 VAL B HA   1 
ATOM   5719 H  HB   . VAL B 1 169 ? -17.124 -34.546 12.916 1.00 20.47  ? 169 VAL B HB   1 
ATOM   5720 H  HG11 . VAL B 1 169 ? -15.161 -35.163 14.323 1.00 18.00  ? 169 VAL B HG11 1 
ATOM   5721 H  HG12 . VAL B 1 169 ? -16.140 -34.035 14.860 1.00 18.00  ? 169 VAL B HG12 1 
ATOM   5722 H  HG13 . VAL B 1 169 ? -16.252 -35.517 15.422 1.00 18.00  ? 169 VAL B HG13 1 
ATOM   5723 H  HG21 . VAL B 1 169 ? -15.678 -36.372 12.466 1.00 17.90  ? 169 VAL B HG21 1 
ATOM   5724 H  HG22 . VAL B 1 169 ? -16.688 -37.308 13.258 1.00 17.90  ? 169 VAL B HG22 1 
ATOM   5725 H  HG23 . VAL B 1 169 ? -17.154 -36.585 11.924 1.00 17.89  ? 169 VAL B HG23 1 
ATOM   5726 N  N    . GLU B 1 170 ? -19.359 -33.341 14.400 1.00 12.91  ? 170 GLU B N    1 
ATOM   5727 C  CA   . GLU B 1 170 ? -19.733 -32.183 15.174 1.00 12.85  ? 170 GLU B CA   1 
ATOM   5728 C  C    . GLU B 1 170 ? -20.769 -32.528 16.242 1.00 11.99  ? 170 GLU B C    1 
ATOM   5729 O  O    . GLU B 1 170 ? -20.765 -31.980 17.356 1.00 11.76  ? 170 GLU B O    1 
ATOM   5730 C  CB   . GLU B 1 170 ? -20.258 -31.094 14.281 1.00 12.41  ? 170 GLU B CB   1 
ATOM   5731 C  CG   . GLU B 1 170 ? -20.231 -29.915 15.137 1.00 18.05  ? 170 GLU B CG   1 
ATOM   5732 C  CD   . GLU B 1 170 ? -20.903 -28.774 14.538 1.00 19.10  ? 170 GLU B CD   1 
ATOM   5733 O  OE1  . GLU B 1 170 ? -21.641 -28.943 13.470 1.00 17.40  ? 170 GLU B OE1  1 
ATOM   5734 O  OE2  . GLU B 1 170 ? -20.710 -27.714 15.230 1.00 19.18  ? 170 GLU B OE2  1 
ATOM   5735 H  H    . GLU B 1 170 ? -19.425 -33.311 13.489 1.00 15.30  ? 170 GLU B H    1 
ATOM   5736 H  HA   . GLU B 1 170 ? -18.924 -31.853 15.628 1.00 20.78  ? 170 GLU B HA   1 
ATOM   5737 H  HB2  . GLU B 1 170 ? -19.676 -30.974 13.503 1.00 15.30  ? 170 GLU B HB2  1 
ATOM   5738 H  HB3  . GLU B 1 170 ? -21.172 -31.299 13.990 1.00 15.30  ? 170 GLU B HB3  1 
ATOM   5739 H  HG2  . GLU B 1 170 ? -20.667 -30.117 15.985 1.00 20.78  ? 170 GLU B HG2  1 
ATOM   5740 H  HG3  . GLU B 1 170 ? -19.299 -29.670 15.324 1.00 20.78  ? 170 GLU B HG3  1 
ATOM   5741 N  N    . TRP B 1 171 ? -21.698 -33.419 15.903 1.00 11.68  ? 171 TRP B N    1 
ATOM   5742 C  CA   . TRP B 1 171 ? -22.779 -33.739 16.822 1.00 12.22  ? 171 TRP B CA   1 
ATOM   5743 C  C    . TRP B 1 171 ? -22.308 -34.581 18.013 1.00 11.16  ? 171 TRP B C    1 
ATOM   5744 O  O    . TRP B 1 171 ? -23.045 -34.662 19.000 1.00 11.37  ? 171 TRP B O    1 
ATOM   5745 C  CB   . TRP B 1 171 ? -23.970 -34.415 16.116 1.00 12.46  ? 171 TRP B CB   1 
ATOM   5746 C  CG   . TRP B 1 171 ? -25.189 -33.550 16.167 1.00 12.86  ? 171 TRP B CG   1 
ATOM   5747 C  CD1  . TRP B 1 171 ? -26.281 -33.726 16.982 1.00 14.36  ? 171 TRP B CD1  1 
ATOM   5748 C  CD2  . TRP B 1 171 ? -25.417 -32.344 15.437 1.00 12.91  ? 171 TRP B CD2  1 
ATOM   5749 N  NE1  . TRP B 1 171 ? -27.181 -32.730 16.773 1.00 14.98  ? 171 TRP B NE1  1 
ATOM   5750 C  CE2  . TRP B 1 171 ? -26.680 -31.855 15.844 1.00 13.73  ? 171 TRP B CE2  1 
ATOM   5751 C  CE3  . TRP B 1 171 ? -24.685 -31.620 14.484 1.00 13.20  ? 171 TRP B CE3  1 
ATOM   5752 C  CZ2  . TRP B 1 171 ? -27.232 -30.694 15.318 1.00 14.42  ? 171 TRP B CZ2  1 
ATOM   5753 C  CZ3  . TRP B 1 171 ? -25.224 -30.472 13.951 1.00 14.14  ? 171 TRP B CZ3  1 
ATOM   5754 C  CH2  . TRP B 1 171 ? -26.478 -30.015 14.385 1.00 14.09  ? 171 TRP B CH2  1 
ATOM   5755 H  H    . TRP B 1 171 ? -21.668 -33.830 15.087 1.00 15.24  ? 171 TRP B H    1 
ATOM   5756 H  HA   . TRP B 1 171 ? -23.110 -32.883 17.177 1.00 20.31  ? 171 TRP B HA   1 
ATOM   5757 H  HB2  . TRP B 1 171 ? -23.731 -34.591 15.184 1.00 15.24  ? 171 TRP B HB2  1 
ATOM   5758 H  HB3  . TRP B 1 171 ? -24.156 -35.271 16.553 1.00 15.24  ? 171 TRP B HB3  1 
ATOM   5759 H  HD1  . TRP B 1 171 ? -26.408 -34.449 17.577 1.00 18.08  ? 171 TRP B HD1  1 
ATOM   5760 H  HE1  . TRP B 1 171 ? -27.951 -32.653 17.181 1.00 18.08  ? 171 TRP B HE1  1 
ATOM   5761 H  HE3  . TRP B 1 171 ? -23.839 -31.927 14.200 1.00 18.08  ? 171 TRP B HE3  1 
ATOM   5762 H  HZ2  . TRP B 1 171 ? -28.076 -30.383 15.595 1.00 18.08  ? 171 TRP B HZ2  1 
ATOM   5763 H  HZ3  . TRP B 1 171 ? -24.741 -29.978 13.309 1.00 18.08  ? 171 TRP B HZ3  1 
ATOM   5764 H  HH2  . TRP B 1 171 ? -26.829 -29.228 14.006 1.00 18.08  ? 171 TRP B HH2  1 
ATOM   5765 N  N    . GLN B 1 172 ? -21.094 -35.128 17.996 1.00 11.20  ? 172 GLN B N    1 
ATOM   5766 C  CA   . GLN B 1 172 ? -20.566 -35.737 19.208 1.00 11.14  ? 172 GLN B CA   1 
ATOM   5767 C  C    . GLN B 1 172 ? -20.502 -34.728 20.341 1.00 10.68  ? 172 GLN B C    1 
ATOM   5768 O  O    . GLN B 1 172 ? -20.516 -35.115 21.509 1.00 12.14  ? 172 GLN B O    1 
ATOM   5769 C  CB   . GLN B 1 172 ? -19.177 -36.330 18.982 1.00 11.05  ? 172 GLN B CB   1 
ATOM   5770 C  CG   . GLN B 1 172 ? -19.162 -37.489 17.992 1.00 12.03  ? 172 GLN B CG   1 
ATOM   5771 C  CD   . GLN B 1 172 ? -17.765 -38.072 17.924 1.00 11.68  ? 172 GLN B CD   1 
ATOM   5772 O  OE1  . GLN B 1 172 ? -16.976 -37.932 18.844 1.00 12.19  ? 172 GLN B OE1  1 
ATOM   5773 N  NE2  . GLN B 1 172 ? -17.444 -38.754 16.842 1.00 13.52  ? 172 GLN B NE2  1 
ATOM   5774 H  H    . GLN B 1 172 ? -20.595 -35.139 17.231 1.00 15.64  ? 172 GLN B H    1 
ATOM   5775 H  HA   . GLN B 1 172 ? -21.174 -36.464 19.475 1.00 13.43  ? 172 GLN B HA   1 
ATOM   5776 H  HB2  . GLN B 1 172 ? -18.584 -35.621 18.655 1.00 13.53  ? 172 GLN B HB2  1 
ATOM   5777 H  HB3  . GLN B 1 172 ? -18.828 -36.639 19.844 1.00 13.53  ? 172 GLN B HB3  1 
ATOM   5778 H  HG2  . GLN B 1 172 ? -19.795 -38.181 18.281 1.00 15.64  ? 172 GLN B HG2  1 
ATOM   5779 H  HG3  . GLN B 1 172 ? -19.432 -37.172 17.104 1.00 15.64  ? 172 GLN B HG3  1 
ATOM   5780 H  HE21 . GLN B 1 172 ? -17.963 -38.719 16.127 1.00 15.65  ? 172 GLN B HE21 1 
ATOM   5781 H  HE22 . GLN B 1 172 ? -16.708 -39.243 16.829 1.00 15.65  ? 172 GLN B HE22 1 
ATOM   5782 N  N    . TYR B 1 173 ? -20.385 -33.448 20.005 1.00 10.83  ? 173 TYR B N    1 
ATOM   5783 C  CA   . TYR B 1 173 ? -20.233 -32.368 20.975 1.00 11.25  ? 173 TYR B CA   1 
ATOM   5784 C  C    . TYR B 1 173 ? -21.572 -31.771 21.414 1.00 11.63  ? 173 TYR B C    1 
ATOM   5785 O  O    . TYR B 1 173 ? -21.576 -30.792 22.135 1.00 14.21  ? 173 TYR B O    1 
ATOM   5786 C  CB   . TYR B 1 173 ? -19.315 -31.260 20.416 1.00 12.18  ? 173 TYR B CB   1 
ATOM   5787 C  CG   . TYR B 1 173 ? -17.905 -31.720 20.104 1.00 11.83  ? 173 TYR B CG   1 
ATOM   5788 C  CD1  . TYR B 1 173 ? -17.619 -32.359 18.900 1.00 12.27  ? 173 TYR B CD1  1 
ATOM   5789 C  CD2  . TYR B 1 173 ? -16.826 -31.524 20.974 1.00 12.82  ? 173 TYR B CD2  1 
ATOM   5790 C  CE1  . TYR B 1 173 ? -16.361 -32.829 18.586 1.00 13.43  ? 173 TYR B CE1  1 
ATOM   5791 C  CE2  . TYR B 1 173 ? -15.534 -31.961 20.646 1.00 12.53  ? 173 TYR B CE2  1 
ATOM   5792 C  CZ   . TYR B 1 173 ? -15.315 -32.626 19.451 1.00 13.46  ? 173 TYR B CZ   1 
ATOM   5793 O  OH   . TYR B 1 173 ? -14.078 -33.129 19.049 1.00 15.18  ? 173 TYR B OH   1 
ATOM   5794 H  H    . TYR B 1 173 ? -20.381 -33.226 19.119 1.00 21.62  ? 173 TYR B H    1 
ATOM   5795 H  HA   . TYR B 1 173 ? -19.796 -32.743 21.782 1.00 13.73  ? 173 TYR B HA   1 
ATOM   5796 H  HB2  . TYR B 1 173 ? -19.721 -30.905 19.600 1.00 20.83  ? 173 TYR B HB2  1 
ATOM   5797 H  HB3  . TYR B 1 173 ? -19.272 -30.532 21.070 1.00 20.83  ? 173 TYR B HB3  1 
ATOM   5798 H  HD1  . TYR B 1 173 ? -18.325 -32.525 18.298 1.00 21.63  ? 173 TYR B HD1  1 
ATOM   5799 H  HD2  . TYR B 1 173 ? -16.968 -31.081 21.794 1.00 21.63  ? 173 TYR B HD2  1 
ATOM   5800 H  HE1  . TYR B 1 173 ? -16.213 -33.270 17.766 1.00 21.63  ? 173 TYR B HE1  1 
ATOM   5801 H  HE2  . TYR B 1 173 ? -14.823 -31.837 21.253 1.00 21.63  ? 173 TYR B HE2  1 
ATOM   5802 H  HH   . TYR B 1 173 ? -13.430 -33.178 19.613 1.00 18.49  ? 173 TYR B HH   1 
ATOM   5803 N  N    . VAL B 1 174 ? -22.695 -32.303 20.915 1.00 12.05  ? 174 VAL B N    1 
ATOM   5804 C  CA   . VAL B 1 174 ? -24.013 -31.812 21.322 1.00 12.71  ? 174 VAL B CA   1 
ATOM   5805 C  C    . VAL B 1 174 ? -24.446 -32.581 22.562 1.00 12.80  ? 174 VAL B C    1 
ATOM   5806 O  O    . VAL B 1 174 ? -24.641 -33.777 22.504 1.00 14.04  ? 174 VAL B O    1 
ATOM   5807 C  CB   . VAL B 1 174 ? -25.018 -31.949 20.169 1.00 13.96  ? 174 VAL B CB   1 
ATOM   5808 C  CG1  . VAL B 1 174 ? -26.445 -31.689 20.658 1.00 15.35  ? 174 VAL B CG1  1 
ATOM   5809 C  CG2  . VAL B 1 174 ? -24.643 -31.006 19.030 1.00 15.04  ? 174 VAL B CG2  1 
ATOM   5810 H  H    . VAL B 1 174 ? -22.647 -32.983 20.308 1.00 15.52  ? 174 VAL B H    1 
ATOM   5811 H  HA   . VAL B 1 174 ? -23.935 -30.868 21.549 1.00 20.17  ? 174 VAL B HA   1 
ATOM   5812 H  HB   . VAL B 1 174 ? -24.970 -32.878 19.832 1.00 15.52  ? 174 VAL B HB   1 
ATOM   5813 H  HG11 . VAL B 1 174 ? -27.012 -31.463 19.900 1.00 20.06  ? 174 VAL B HG11 1 
ATOM   5814 H  HG12 . VAL B 1 174 ? -26.791 -32.487 21.093 1.00 20.06  ? 174 VAL B HG12 1 
ATOM   5815 H  HG13 . VAL B 1 174 ? -26.443 -30.950 21.291 1.00 20.06  ? 174 VAL B HG13 1 
ATOM   5816 H  HG21 . VAL B 1 174 ? -25.387 -30.932 18.408 1.00 20.31  ? 174 VAL B HG21 1 
ATOM   5817 H  HG22 . VAL B 1 174 ? -24.433 -30.126 19.390 1.00 20.31  ? 174 VAL B HG22 1 
ATOM   5818 H  HG23 . VAL B 1 174 ? -23.867 -31.358 18.563 1.00 20.31  ? 174 VAL B HG23 1 
ATOM   5819 N  N    . ASP B 1 175 ? -24.593 -31.880 23.681 1.00 11.77  ? 175 ASP B N    1 
ATOM   5820 C  CA   A ASP B 1 175 ? -25.011 -32.522 24.903 0.60 12.81  ? 175 ASP B CA   1 
ATOM   5821 C  CA   B ASP B 1 175 ? -24.969 -32.504 24.943 0.40 12.70  ? 175 ASP B CA   1 
ATOM   5822 C  C    . ASP B 1 175 ? -26.457 -32.295 25.280 1.00 13.13  ? 175 ASP B C    1 
ATOM   5823 O  O    . ASP B 1 175 ? -27.002 -33.049 26.100 1.00 16.02  ? 175 ASP B O    1 
ATOM   5824 C  CB   A ASP B 1 175 ? -24.186 -32.053 26.085 0.60 14.18  ? 175 ASP B CB   1 
ATOM   5825 C  CB   B ASP B 1 175 ? -23.932 -32.227 26.064 0.40 13.00  ? 175 ASP B CB   1 
ATOM   5826 C  CG   A ASP B 1 175 ? -22.843 -32.727 26.126 0.60 14.32  ? 175 ASP B CG   1 
ATOM   5827 C  CG   B ASP B 1 175 ? -23.746 -30.803 26.603 0.40 13.42  ? 175 ASP B CG   1 
ATOM   5828 O  OD1  A ASP B 1 175 ? -22.588 -33.644 25.287 0.60 15.72  ? 175 ASP B OD1  1 
ATOM   5829 O  OD1  B ASP B 1 175 ? -24.513 -29.940 26.208 0.40 15.21  ? 175 ASP B OD1  1 
ATOM   5830 O  OD2  A ASP B 1 175 ? -22.072 -32.292 26.980 0.60 16.91  ? 175 ASP B OD2  1 
ATOM   5831 O  OD2  B ASP B 1 175 ? -22.836 -30.585 27.475 0.40 15.02  ? 175 ASP B OD2  1 
ATOM   5832 H  H    A ASP B 1 175 ? -24.425 -30.982 23.685 0.60 20.08  ? 175 ASP B H    1 
ATOM   5833 H  H    B ASP B 1 175 ? -24.449 -30.978 23.665 0.40 20.14  ? 175 ASP B H    1 
ATOM   5834 H  HA   A ASP B 1 175 ? -24.874 -33.493 24.803 0.60 15.00  ? 175 ASP B HA   1 
ATOM   5835 H  HA   B ASP B 1 175 ? -24.882 -33.473 24.787 0.40 15.36  ? 175 ASP B HA   1 
ATOM   5836 H  HB2  A ASP B 1 175 ? -24.051 -31.085 26.026 0.60 19.95  ? 175 ASP B HB2  1 
ATOM   5837 H  HB2  B ASP B 1 175 ? -24.166 -32.792 26.829 0.40 16.42  ? 175 ASP B HB2  1 
ATOM   5838 H  HB3  A ASP B 1 175 ? -24.658 -32.249 26.921 0.60 19.95  ? 175 ASP B HB3  1 
ATOM   5839 H  HB3  B ASP B 1 175 ? -23.058 -32.524 25.738 0.40 16.42  ? 175 ASP B HB3  1 
ATOM   5840 N  N    . ARG B 1 176 ? -27.109 -31.302 24.693 1.00 11.96  ? 176 ARG B N    1 
ATOM   5841 C  CA   . ARG B 1 176 ? -28.543 -31.133 24.884 1.00 11.94  ? 176 ARG B CA   1 
ATOM   5842 C  C    . ARG B 1 176 ? -29.110 -30.623 23.573 1.00 11.21  ? 176 ARG B C    1 
ATOM   5843 O  O    . ARG B 1 176 ? -28.546 -29.727 22.960 1.00 11.32  ? 176 ARG B O    1 
ATOM   5844 C  CB   . ARG B 1 176 ? -28.885 -30.180 26.034 1.00 14.00  ? 176 ARG B CB   1 
ATOM   5845 C  CG   . ARG B 1 176 ? -30.298 -30.315 26.585 1.00 14.37  ? 176 ARG B CG   1 
ATOM   5846 C  CD   . ARG B 1 176 ? -30.576 -29.412 27.791 1.00 14.42  ? 176 ARG B CD   1 
ATOM   5847 N  NE   . ARG B 1 176 ? -31.952 -29.587 28.214 1.00 15.43  ? 176 ARG B NE   1 
ATOM   5848 C  CZ   . ARG B 1 176 ? -32.607 -28.750 28.995 1.00 14.70  ? 176 ARG B CZ   1 
ATOM   5849 N  NH1  . ARG B 1 176 ? -32.010 -27.641 29.390 1.00 17.56  ? 176 ARG B NH1  1 
ATOM   5850 N  NH2  . ARG B 1 176 ? -33.880 -28.978 29.291 1.00 18.46  ? 176 ARG B NH2  1 
ATOM   5851 H  H    . ARG B 1 176 ? -26.659 -30.704 24.169 1.00 20.11  ? 176 ARG B H    1 
ATOM   5852 H  HA   . ARG B 1 176 ? -28.935 -32.012 25.077 1.00 16.14  ? 176 ARG B HA   1 
ATOM   5853 H  HB2  . ARG B 1 176 ? -28.249 -30.337 26.764 1.00 16.66  ? 176 ARG B HB2  1 
ATOM   5854 H  HB3  . ARG B 1 176 ? -28.758 -29.260 25.722 1.00 16.66  ? 176 ARG B HB3  1 
ATOM   5855 H  HG2  . ARG B 1 176 ? -30.940 -30.100 25.876 1.00 13.79  ? 176 ARG B HG2  1 
ATOM   5856 H  HG3  . ARG B 1 176 ? -30.449 -31.248 26.850 1.00 13.79  ? 176 ARG B HG3  1 
ATOM   5857 H  HD2  . ARG B 1 176 ? -29.971 -29.644 28.527 1.00 19.98  ? 176 ARG B HD2  1 
ATOM   5858 H  HD3  . ARG B 1 176 ? -30.420 -28.475 27.544 1.00 19.98  ? 176 ARG B HD3  1 
ATOM   5859 H  HE   . ARG B 1 176 ? -32.377 -30.296 27.935 1.00 24.23  ? 176 ARG B HE   1 
ATOM   5860 H  HH11 . ARG B 1 176 ? -31.315 -27.685 29.931 1.00 20.08  ? 176 ARG B HH11 1 
ATOM   5861 H  HH12 . ARG B 1 176 ? -32.308 -26.860 29.113 1.00 20.08  ? 176 ARG B HH12 1 
ATOM   5862 H  HH21 . ARG B 1 176 ? -34.150 -29.798 29.455 1.00 24.24  ? 176 ARG B HH21 1 
ATOM   5863 H  HH22 . ARG B 1 176 ? -34.447 -28.309 29.325 1.00 24.26  ? 176 ARG B HH22 1 
ATOM   5864 N  N    . GLU B 1 177 ? -30.217 -31.216 23.154 1.00 11.49  ? 177 GLU B N    1 
ATOM   5865 C  CA   . GLU B 1 177 ? -30.863 -30.838 21.908 1.00 10.72  ? 177 GLU B CA   1 
ATOM   5866 C  C    . GLU B 1 177 ? -32.337 -31.160 22.063 1.00 10.74  ? 177 GLU B C    1 
ATOM   5867 O  O    . GLU B 1 177 ? -32.689 -32.301 22.351 1.00 12.02  ? 177 GLU B O    1 
ATOM   5868 C  CB   . GLU B 1 177 ? -30.301 -31.607 20.711 1.00 11.30  ? 177 GLU B CB   1 
ATOM   5869 C  CG   . GLU B 1 177 ? -30.984 -31.293 19.397 1.00 10.80  ? 177 GLU B CG   1 
ATOM   5870 C  CD   . GLU B 1 177 ? -30.388 -31.989 18.183 1.00 11.79  ? 177 GLU B CD   1 
ATOM   5871 O  OE1  . GLU B 1 177 ? -29.400 -32.765 18.372 1.00 14.38  ? 177 GLU B OE1  1 
ATOM   5872 O  OE2  . GLU B 1 177 ? -30.853 -31.733 17.062 1.00 12.92  ? 177 GLU B OE2  1 
ATOM   5873 H  H    . GLU B 1 177 ? -30.589 -31.882 23.658 1.00 16.14  ? 177 GLU B H    1 
ATOM   5874 H  HA   . GLU B 1 177 ? -30.749 -29.874 21.763 1.00 12.65  ? 177 GLU B HA   1 
ATOM   5875 H  HB2  . GLU B 1 177 ? -29.346 -31.399 20.629 1.00 13.47  ? 177 GLU B HB2  1 
ATOM   5876 H  HB3  . GLU B 1 177 ? -30.384 -32.566 20.890 1.00 13.47  ? 177 GLU B HB3  1 
ATOM   5877 H  HG2  . GLU B 1 177 ? -31.929 -31.546 19.461 1.00 13.09  ? 177 GLU B HG2  1 
ATOM   5878 H  HG3  . GLU B 1 177 ? -30.949 -30.324 19.246 1.00 13.09  ? 177 GLU B HG3  1 
ATOM   5879 N  N    . ILE B 1 178 ? -33.176 -30.126 21.925 1.00 10.20  ? 178 ILE B N    1 
ATOM   5880 C  CA   . ILE B 1 178 ? -34.619 -30.291 21.982 1.00 10.49  ? 178 ILE B CA   1 
ATOM   5881 C  C    . ILE B 1 178 ? -35.147 -29.965 20.605 1.00 10.44  ? 178 ILE B C    1 
ATOM   5882 O  O    . ILE B 1 178 ? -34.758 -28.972 20.021 1.00 11.70  ? 178 ILE B O    1 
ATOM   5883 C  CB   . ILE B 1 178 ? -35.251 -29.345 23.035 1.00 11.34  ? 178 ILE B CB   1 
ATOM   5884 C  CG1  . ILE B 1 178 ? -34.558 -29.436 24.409 1.00 12.88  ? 178 ILE B CG1  1 
ATOM   5885 C  CG2  . ILE B 1 178 ? -36.736 -29.649 23.149 1.00 12.96  ? 178 ILE B CG2  1 
ATOM   5886 C  CD1  . ILE B 1 178 ? -34.595 -30.789 25.018 1.00 13.49  ? 178 ILE B CD1  1 
ATOM   5887 H  H    . ILE B 1 178 ? -32.836 -29.288 21.791 1.00 12.65  ? 178 ILE B H    1 
ATOM   5888 H  HA   . ILE B 1 178 ? -34.835 -31.213 22.205 1.00 16.96  ? 178 ILE B HA   1 
ATOM   5889 H  HB   . ILE B 1 178 ? -35.154 -28.418 22.709 1.00 11.64  ? 178 ILE B HB   1 
ATOM   5890 H  HG12 . ILE B 1 178 ? -33.621 -29.161 24.309 1.00 16.88  ? 178 ILE B HG12 1 
ATOM   5891 H  HG13 . ILE B 1 178 ? -34.991 -28.804 25.021 1.00 16.88  ? 178 ILE B HG13 1 
ATOM   5892 H  HG21 . ILE B 1 178 ? -37.088 -29.254 23.966 1.00 16.95  ? 178 ILE B HG21 1 
ATOM   5893 H  HG22 . ILE B 1 178 ? -37.206 -29.277 22.384 1.00 16.95  ? 178 ILE B HG22 1 
ATOM   5894 H  HG23 . ILE B 1 178 ? -36.871 -30.612 23.174 1.00 16.95  ? 178 ILE B HG23 1 
ATOM   5895 H  HD11 . ILE B 1 178 ? -34.177 -30.760 25.895 1.00 16.97  ? 178 ILE B HD11 1 
ATOM   5896 H  HD12 . ILE B 1 178 ? -35.518 -31.081 25.111 1.00 16.97  ? 178 ILE B HD12 1 
ATOM   5897 H  HD13 . ILE B 1 178 ? -34.113 -31.416 24.453 1.00 16.97  ? 178 ILE B HD13 1 
ATOM   5898 N  N    . ASP B 1 179 ? -36.023 -30.820 20.082 1.00 10.85  ? 179 ASP B N    1 
ATOM   5899 C  CA   . ASP B 1 179 ? -36.557 -30.619 18.745 1.00 11.27  ? 179 ASP B CA   1 
ATOM   5900 C  C    . ASP B 1 179 ? -38.048 -30.337 18.871 1.00 10.87  ? 179 ASP B C    1 
ATOM   5901 O  O    . ASP B 1 179 ? -38.813 -31.234 19.225 1.00 12.34  ? 179 ASP B O    1 
ATOM   5902 C  CB   . ASP B 1 179 ? -36.242 -31.848 17.898 1.00 12.17  ? 179 ASP B CB   1 
ATOM   5903 C  CG   . ASP B 1 179 ? -36.628 -31.723 16.442 1.00 12.80  ? 179 ASP B CG   1 
ATOM   5904 O  OD1  . ASP B 1 179 ? -37.384 -30.764 16.109 1.00 13.81  ? 179 ASP B OD1  1 
ATOM   5905 O  OD2  . ASP B 1 179 ? -36.140 -32.527 15.633 1.00 13.80  ? 179 ASP B OD2  1 
ATOM   5906 H  H    . ASP B 1 179 ? -36.299 -31.544 20.565 1.00 16.96  ? 179 ASP B H    1 
ATOM   5907 H  HA   . ASP B 1 179 ? -36.116 -29.839 18.339 1.00 12.31  ? 179 ASP B HA   1 
ATOM   5908 H  HB2  . ASP B 1 179 ? -35.281 -32.025 17.944 1.00 14.57  ? 179 ASP B HB2  1 
ATOM   5909 H  HB3  . ASP B 1 179 ? -36.712 -32.620 18.273 1.00 14.57  ? 179 ASP B HB3  1 
ATOM   5910 N  N    . ILE B 1 180 ? -38.425 -29.081 18.647 1.00 10.80  ? 180 ILE B N    1 
ATOM   5911 C  CA   . ILE B 1 180 ? -39.798 -28.604 18.791 1.00 11.52  ? 180 ILE B CA   1 
ATOM   5912 C  C    . ILE B 1 180 ? -40.338 -28.335 17.394 1.00 11.32  ? 180 ILE B C    1 
ATOM   5913 O  O    . ILE B 1 180 ? -39.760 -27.532 16.667 1.00 11.98  ? 180 ILE B O    1 
ATOM   5914 C  CB   . ILE B 1 180 ? -39.853 -27.324 19.661 1.00 11.60  ? 180 ILE B CB   1 
ATOM   5915 C  CG1  . ILE B 1 180 ? -39.124 -27.535 20.984 1.00 12.59  ? 180 ILE B CG1  1 
ATOM   5916 C  CG2  . ILE B 1 180 ? -41.303 -26.893 19.822 1.00 13.85  ? 180 ILE B CG2  1 
ATOM   5917 C  CD1  . ILE B 1 180 ? -38.937 -26.268 21.808 1.00 14.57  ? 180 ILE B CD1  1 
ATOM   5918 H  H    . ILE B 1 180 ? -37.789 -28.478 18.387 1.00 12.31  ? 180 ILE B H    1 
ATOM   5919 H  HA   . ILE B 1 180 ? -40.334 -29.297 19.215 1.00 15.88  ? 180 ILE B HA   1 
ATOM   5920 H  HB   . ILE B 1 180 ? -39.379 -26.609 19.170 1.00 14.13  ? 180 ILE B HB   1 
ATOM   5921 H  HG12 . ILE B 1 180 ? -39.627 -28.182 21.517 1.00 17.01  ? 180 ILE B HG12 1 
ATOM   5922 H  HG13 . ILE B 1 180 ? -38.241 -27.919 20.800 1.00 17.01  ? 180 ILE B HG13 1 
ATOM   5923 H  HG21 . ILE B 1 180 ? -41.369 -26.224 20.524 1.00 15.88  ? 180 ILE B HG21 1 
ATOM   5924 H  HG22 . ILE B 1 180 ? -41.627 -26.514 18.986 1.00 15.88  ? 180 ILE B HG22 1 
ATOM   5925 H  HG23 . ILE B 1 180 ? -41.848 -27.663 20.059 1.00 15.88  ? 180 ILE B HG23 1 
ATOM   5926 H  HD11 . ILE B 1 180 ? -38.276 -26.428 22.504 1.00 15.73  ? 180 ILE B HD11 1 
ATOM   5927 H  HD12 . ILE B 1 180 ? -38.631 -25.547 21.231 1.00 15.73  ? 180 ILE B HD12 1 
ATOM   5928 H  HD13 . ILE B 1 180 ? -39.783 -26.018 22.217 1.00 15.73  ? 180 ILE B HD13 1 
ATOM   5929 N  N    . ARG B 1 181 ? -41.450 -28.976 17.029 1.00 11.65  ? 181 ARG B N    1 
ATOM   5930 C  CA   . ARG B 1 181 ? -42.061 -28.776 15.733 1.00 12.31  ? 181 ARG B CA   1 
ATOM   5931 C  C    . ARG B 1 181 ? -43.339 -27.965 15.898 1.00 12.58  ? 181 ARG B C    1 
ATOM   5932 O  O    . ARG B 1 181 ? -44.133 -28.202 16.819 1.00 13.10  ? 181 ARG B O    1 
ATOM   5933 C  CB   . ARG B 1 181 ? -42.377 -30.098 15.022 1.00 12.87  ? 181 ARG B CB   1 
ATOM   5934 C  CG   . ARG B 1 181 ? -41.135 -30.953 14.849 1.00 13.27  ? 181 ARG B CG   1 
ATOM   5935 C  CD   . ARG B 1 181 ? -40.045 -30.254 14.043 1.00 12.85  ? 181 ARG B CD   1 
ATOM   5936 N  NE   . ARG B 1 181 ? -38.857 -31.048 13.874 1.00 12.55  ? 181 ARG B NE   1 
ATOM   5937 C  CZ   . ARG B 1 181 ? -38.747 -32.037 12.991 1.00 12.64  ? 181 ARG B CZ   1 
ATOM   5938 N  NH1  . ARG B 1 181 ? -39.637 -32.226 12.028 1.00 13.80  ? 181 ARG B NH1  1 
ATOM   5939 N  NH2  . ARG B 1 181 ? -37.740 -32.872 13.125 1.00 13.66  ? 181 ARG B NH2  1 
ATOM   5940 H  H    . ARG B 1 181 ? -41.841 -29.561 17.612 1.00 15.88  ? 181 ARG B H    1 
ATOM   5941 H  HA   . ARG B 1 181 ? -41.438 -28.260 15.174 1.00 16.76  ? 181 ARG B HA   1 
ATOM   5942 H  HB2  . ARG B 1 181 ? -43.041 -30.592 15.546 1.00 19.22  ? 181 ARG B HB2  1 
ATOM   5943 H  HB3  . ARG B 1 181 ? -42.761 -29.903 14.142 1.00 19.22  ? 181 ARG B HB3  1 
ATOM   5944 H  HG2  . ARG B 1 181 ? -40.778 -31.187 15.732 1.00 15.74  ? 181 ARG B HG2  1 
ATOM   5945 H  HG3  . ARG B 1 181 ? -41.380 -31.787 14.394 1.00 15.74  ? 181 ARG B HG3  1 
ATOM   5946 H  HD2  . ARG B 1 181 ? -40.401 -30.015 13.162 1.00 16.76  ? 181 ARG B HD2  1 
ATOM   5947 H  HD3  . ARG B 1 181 ? -39.799 -29.421 14.497 1.00 16.76  ? 181 ARG B HD3  1 
ATOM   5948 H  HE   . ARG B 1 181 ? -38.166 -30.861 14.369 1.00 16.70  ? 181 ARG B HE   1 
ATOM   5949 H  HH11 . ARG B 1 181 ? -40.483 -32.015 12.158 1.00 16.72  ? 181 ARG B HH11 1 
ATOM   5950 H  HH12 . ARG B 1 181 ? -39.379 -32.571 11.258 1.00 16.72  ? 181 ARG B HH12 1 
ATOM   5951 H  HH21 . ARG B 1 181 ? -37.190 -32.793 13.806 1.00 16.70  ? 181 ARG B HH21 1 
ATOM   5952 H  HH22 . ARG B 1 181 ? -37.619 -33.509 12.532 1.00 16.70  ? 181 ARG B HH22 1 
ATOM   5953 N  N    . LEU B 1 182 ? -43.524 -27.053 14.948 1.00 12.34  ? 182 LEU B N    1 
ATOM   5954 C  CA   . LEU B 1 182 ? -44.583 -26.052 14.977 1.00 13.21  ? 182 LEU B CA   1 
ATOM   5955 C  C    . LEU B 1 182 ? -45.363 -26.062 13.667 1.00 13.20  ? 182 LEU B C    1 
ATOM   5956 O  O    . LEU B 1 182 ? -44.810 -26.328 12.609 1.00 14.00  ? 182 LEU B O    1 
ATOM   5957 C  CB   . LEU B 1 182 ? -43.999 -24.640 15.123 1.00 13.57  ? 182 LEU B CB   1 
ATOM   5958 C  CG   . LEU B 1 182 ? -43.133 -24.290 16.334 1.00 14.47  ? 182 LEU B CG   1 
ATOM   5959 C  CD1  . LEU B 1 182 ? -43.748 -24.701 17.647 1.00 13.92  ? 182 LEU B CD1  1 
ATOM   5960 C  CD2  . LEU B 1 182 ? -41.709 -24.701 16.192 1.00 16.58  ? 182 LEU B CD2  1 
ATOM   5961 H  H    . LEU B 1 182 ? -42.958 -27.055 14.229 1.00 16.76  ? 182 LEU B H    1 
ATOM   5962 H  HA   . LEU B 1 182 ? -45.190 -26.246 15.722 1.00 16.44  ? 182 LEU B HA   1 
ATOM   5963 H  HB2  . LEU B 1 182 ? -43.469 -24.461 14.321 1.00 17.42  ? 182 LEU B HB2  1 
ATOM   5964 H  HB3  . LEU B 1 182 ? -44.750 -24.014 15.109 1.00 17.42  ? 182 LEU B HB3  1 
ATOM   5965 H  HG   . LEU B 1 182 ? -43.113 -23.302 16.358 1.00 17.02  ? 182 LEU B HG   1 
ATOM   5966 H  HD11 . LEU B 1 182 ? -43.223 -24.335 18.380 1.00 16.38  ? 182 LEU B HD11 1 
ATOM   5967 H  HD12 . LEU B 1 182 ? -44.658 -24.362 17.699 1.00 16.38  ? 182 LEU B HD12 1 
ATOM   5968 H  HD13 . LEU B 1 182 ? -43.759 -25.672 17.711 1.00 16.38  ? 182 LEU B HD13 1 
ATOM   5969 H  HD21 . LEU B 1 182 ? -41.181 -24.292 16.900 1.00 17.48  ? 182 LEU B HD21 1 
ATOM   5970 H  HD22 . LEU B 1 182 ? -41.641 -25.669 16.257 1.00 17.48  ? 182 LEU B HD22 1 
ATOM   5971 H  HD23 . LEU B 1 182 ? -41.370 -24.410 15.327 1.00 17.48  ? 182 LEU B HD23 1 
ATOM   5972 N  N    . VAL B 1 183 ? -46.625 -25.666 13.752 1.00 14.01  ? 183 VAL B N    1 
ATOM   5973 C  CA   . VAL B 1 183 ? -47.430 -25.340 12.586 1.00 16.37  ? 183 VAL B CA   1 
ATOM   5974 C  C    . VAL B 1 183 ? -48.071 -23.985 12.828 1.00 15.88  ? 183 VAL B C    1 
ATOM   5975 O  O    . VAL B 1 183 ? -48.625 -23.717 13.899 1.00 17.57  ? 183 VAL B O    1 
ATOM   5976 C  CB   . VAL B 1 183 ? -48.499 -26.410 12.314 1.00 18.78  ? 183 VAL B CB   1 
ATOM   5977 C  CG1  . VAL B 1 183 ? -49.442 -25.945 11.223 1.00 23.26  ? 183 VAL B CG1  1 
ATOM   5978 C  CG2  . VAL B 1 183 ? -47.859 -27.751 11.982 1.00 19.93  ? 183 VAL B CG2  1 
ATOM   5979 H  H    . VAL B 1 183 ? -47.010 -25.596 14.578 1.00 16.44  ? 183 VAL B H    1 
ATOM   5980 H  HA   . VAL B 1 183 ? -46.846 -25.277 11.812 1.00 24.21  ? 183 VAL B HA   1 
ATOM   5981 H  HB   . VAL B 1 183 ? -49.026 -26.522 13.144 1.00 21.07  ? 183 VAL B HB   1 
ATOM   5982 H  HG11 . VAL B 1 183 ? -49.903 -26.713 10.842 1.00 28.21  ? 183 VAL B HG11 1 
ATOM   5983 H  HG12 . VAL B 1 183 ? -50.097 -25.330 11.597 1.00 28.21  ? 183 VAL B HG12 1 
ATOM   5984 H  HG13 . VAL B 1 183 ? -48.936 -25.494 10.524 1.00 28.21  ? 183 VAL B HG13 1 
ATOM   5985 H  HG21 . VAL B 1 183 ? -48.554 -28.401 11.778 1.00 27.52  ? 183 VAL B HG21 1 
ATOM   5986 H  HG22 . VAL B 1 183 ? -47.274 -27.650 11.211 1.00 27.52  ? 183 VAL B HG22 1 
ATOM   5987 H  HG23 . VAL B 1 183 ? -47.339 -28.062 12.743 1.00 27.52  ? 183 VAL B HG23 1 
ATOM   5988 N  N    . HIS B 1 184 ? -47.968 -23.122 11.832 1.00 18.22  ? 184 HIS B N    1 
ATOM   5989 C  CA   . HIS B 1 184 ? -48.494 -21.782 12.007 1.00 20.04  ? 184 HIS B CA   1 
ATOM   5990 C  C    . HIS B 1 184 ? -50.011 -21.815 12.141 1.00 22.33  ? 184 HIS B C    1 
ATOM   5991 O  O    . HIS B 1 184 ? -50.678 -22.565 11.435 1.00 23.95  ? 184 HIS B O    1 
ATOM   5992 C  CB   . HIS B 1 184 ? -48.068 -20.911 10.827 1.00 21.98  ? 184 HIS B CB   1 
ATOM   5993 C  CG   . HIS B 1 184 ? -48.159 -19.464 11.112 1.00 23.09  ? 184 HIS B CG   1 
ATOM   5994 N  ND1  . HIS B 1 184 ? -49.342 -18.755 11.075 1.00 25.61  ? 184 HIS B ND1  1 
ATOM   5995 C  CD2  . HIS B 1 184 ? -47.200 -18.591 11.446 1.00 25.60  ? 184 HIS B CD2  1 
ATOM   5996 C  CE1  . HIS B 1 184 ? -49.086 -17.490 11.383 1.00 26.14  ? 184 HIS B CE1  1 
ATOM   5997 N  NE2  . HIS B 1 184 ? -47.792 -17.371 11.603 1.00 25.87  ? 184 HIS B NE2  1 
ATOM   5998 H  H    . HIS B 1 184 ? -47.580 -23.360 11.039 1.00 24.21  ? 184 HIS B H    1 
ATOM   5999 H  HA   . HIS B 1 184 ? -48.113 -21.406 12.839 1.00 31.84  ? 184 HIS B HA   1 
ATOM   6000 H  HB2  . HIS B 1 184 ? -47.142 -21.131 10.588 1.00 24.21  ? 184 HIS B HB2  1 
ATOM   6001 H  HB3  . HIS B 1 184 ? -48.638 -21.122 10.056 1.00 24.21  ? 184 HIS B HB3  1 
ATOM   6002 H  HD1  . HIS B 1 184 ? -50.135 -19.088 10.883 1.00 50.26  ? 184 HIS B HD1  1 
ATOM   6003 H  HD2  . HIS B 1 184 ? -46.288 -18.772 11.549 1.00 50.26  ? 184 HIS B HD2  1 
ATOM   6004 H  HE1  . HIS B 1 184 ? -49.718 -16.797 11.422 1.00 50.27  ? 184 HIS B HE1  1 
ATOM   6005 N  N    . GLU B 1 185 ? -50.553 -20.970 13.015 1.00 23.60  ? 185 GLU B N    1 
ATOM   6006 C  CA   . GLU B 1 185 ? -52.002 -20.844 13.108 1.00 27.16  ? 185 GLU B CA   1 
ATOM   6007 C  C    . GLU B 1 185 ? -52.552 -20.475 11.735 1.00 29.64  ? 185 GLU B C    1 
ATOM   6008 O  O    . GLU B 1 185 ? -51.899 -19.766 10.969 1.00 27.50  ? 185 GLU B O    1 
ATOM   6009 C  CB   . GLU B 1 185 ? -52.420 -19.812 14.153 1.00 30.30  ? 185 GLU B CB   1 
ATOM   6010 C  CG   . GLU B 1 185 ? -52.058 -18.395 13.774 1.00 35.65  ? 185 GLU B CG   1 
ATOM   6011 C  CD   . GLU B 1 185 ? -52.315 -17.361 14.860 1.00 39.70  ? 185 GLU B CD   1 
ATOM   6012 O  OE1  . GLU B 1 185 ? -52.581 -17.758 16.030 1.00 38.50  ? 185 GLU B OE1  1 
ATOM   6013 O  OE2  . GLU B 1 185 ? -52.245 -16.155 14.532 1.00 43.71  ? 185 GLU B OE2  1 
ATOM   6014 H  H    . GLU B 1 185 ? -50.022 -20.466 13.563 1.00 31.84  ? 185 GLU B H    1 
ATOM   6015 H  HA   . GLU B 1 185 ? -52.365 -21.719 13.368 1.00 27.74  ? 185 GLU B HA   1 
ATOM   6016 H  HB2  . GLU B 1 185 ? -53.389 -19.872 14.283 1.00 26.09  ? 185 GLU B HB2  1 
ATOM   6017 H  HB3  . GLU B 1 185 ? -51.987 -20.036 15.002 1.00 26.09  ? 185 GLU B HB3  1 
ATOM   6018 H  HG2  . GLU B 1 185 ? -51.108 -18.362 13.534 1.00 31.84  ? 185 GLU B HG2  1 
ATOM   6019 H  HG3  . GLU B 1 185 ? -52.572 -18.136 12.980 1.00 31.84  ? 185 GLU B HG3  1 
ATOM   6020 N  N    . PRO B 1 186 ? -53.771 -20.931 11.376 1.00 35.15  ? 186 PRO B N    1 
ATOM   6021 C  CA   . PRO B 1 186 ? -54.425 -20.461 10.161 1.00 38.43  ? 186 PRO B CA   1 
ATOM   6022 C  C    . PRO B 1 186 ? -54.664 -18.945 10.217 1.00 41.22  ? 186 PRO B C    1 
ATOM   6023 O  O    . PRO B 1 186 ? -54.540 -18.361 9.156  1.00 48.69  ? 186 PRO B O    1 
ATOM   6024 C  CB   . PRO B 1 186 ? -55.758 -21.225 10.124 1.00 40.09  ? 186 PRO B CB   1 
ATOM   6025 C  CG   . PRO B 1 186 ? -55.973 -21.682 11.554 1.00 40.65  ? 186 PRO B CG   1 
ATOM   6026 C  CD   . PRO B 1 186 ? -54.587 -21.925 12.096 1.00 37.89  ? 186 PRO B CD   1 
ATOM   6027 H  HA   . PRO B 1 186 ? -53.877 -20.699 9.371  1.00 31.40  ? 186 PRO B HA   1 
ATOM   6028 H  HB2  . PRO B 1 186 ? -56.490 -20.642 9.830  1.00 31.86  ? 186 PRO B HB2  1 
ATOM   6029 H  HB3  . PRO B 1 186 ? -55.704 -21.994 9.517  1.00 31.86  ? 186 PRO B HB3  1 
ATOM   6030 H  HG2  . PRO B 1 186 ? -56.433 -20.992 12.074 1.00 31.62  ? 186 PRO B HG2  1 
ATOM   6031 H  HG3  . PRO B 1 186 ? -56.504 -22.504 11.580 1.00 31.62  ? 186 PRO B HG3  1 
ATOM   6032 H  HD2  . PRO B 1 186 ? -54.558 -21.777 13.059 1.00 27.74  ? 186 PRO B HD2  1 
ATOM   6033 H  HD3  . PRO B 1 186 ? -54.287 -22.833 11.903 1.00 27.74  ? 186 PRO B HD3  1 
HETATM 6034 C  CHA  . HEM C 2 .   ? -7.972  -10.117 20.204 1.00 10.52  ? 201 HEM A CHA  1 
HETATM 6035 C  CHB  . HEM C 2 .   ? -3.575  -11.351 21.738 1.00 10.20  ? 201 HEM A CHB  1 
HETATM 6036 C  CHC  . HEM C 2 .   ? -2.778  -6.799  23.069 1.00 9.60   ? 201 HEM A CHC  1 
HETATM 6037 C  CHD  . HEM C 2 .   ? -7.113  -5.532  21.375 1.00 9.18   ? 201 HEM A CHD  1 
HETATM 6038 C  C1A  . HEM C 2 .   ? -6.843  -10.844 20.499 1.00 10.69  ? 201 HEM A C1A  1 
HETATM 6039 C  C2A  . HEM C 2 .   ? -6.687  -12.276 20.249 1.00 12.28  ? 201 HEM A C2A  1 
HETATM 6040 C  C3A  . HEM C 2 .   ? -5.471  -12.637 20.739 1.00 11.93  ? 201 HEM A C3A  1 
HETATM 6041 C  C4A  . HEM C 2 .   ? -4.851  -11.418 21.199 1.00 10.37  ? 201 HEM A C4A  1 
HETATM 6042 C  CMA  . HEM C 2 .   ? -4.896  -14.034 20.809 1.00 13.68  ? 201 HEM A CMA  1 
HETATM 6043 C  CAA  . HEM C 2 .   ? -7.676  -13.195 19.500 1.00 12.69  ? 201 HEM A CAA  1 
HETATM 6044 C  CBA  . HEM C 2 .   ? -8.565  -13.809 20.459 1.00 13.22  ? 201 HEM A CBA  1 
HETATM 6045 C  CGA  . HEM C 2 .   ? -9.536  -14.706 19.643 1.00 12.06  ? 201 HEM A CGA  1 
HETATM 6046 O  O1A  . HEM C 2 .   ? -10.768 -14.527 19.807 1.00 11.56  ? 201 HEM A O1A  1 
HETATM 6047 O  O2A  . HEM C 2 .   ? -9.094  -15.633 18.863 1.00 11.34  ? 201 HEM A O2A  1 
HETATM 6048 C  C1B  . HEM C 2 .   ? -2.954  -10.204 22.203 1.00 9.83   ? 201 HEM A C1B  1 
HETATM 6049 C  C2B  . HEM C 2 .   ? -1.691  -10.213 22.871 1.00 10.21  ? 201 HEM A C2B  1 
HETATM 6050 C  C3B  . HEM C 2 .   ? -1.490  -8.942  23.333 1.00 9.97   ? 201 HEM A C3B  1 
HETATM 6051 C  C4B  . HEM C 2 .   ? -2.644  -8.165  22.887 1.00 9.38   ? 201 HEM A C4B  1 
HETATM 6052 C  CMB  . HEM C 2 .   ? -0.798  -11.426 23.044 1.00 11.23  ? 201 HEM A CMB  1 
HETATM 6053 C  CAB  . HEM C 2 .   ? -0.399  -8.495  24.191 1.00 10.75  ? 201 HEM A CAB  1 
HETATM 6054 C  CBB  . HEM C 2 .   ? -0.501  -7.694  25.225 1.00 12.07  ? 201 HEM A CBB  1 
HETATM 6055 C  C1C  . HEM C 2 .   ? -3.878  -6.025  22.677 1.00 9.13   ? 201 HEM A C1C  1 
HETATM 6056 C  C2C  . HEM C 2 .   ? -3.988  -4.619  22.902 1.00 9.37   ? 201 HEM A C2C  1 
HETATM 6057 C  C3C  . HEM C 2 .   ? -5.211  -4.245  22.403 1.00 9.57   ? 201 HEM A C3C  1 
HETATM 6058 C  C4C  . HEM C 2 .   ? -5.845  -5.464  21.892 1.00 9.29   ? 201 HEM A C4C  1 
HETATM 6059 C  CMC  . HEM C 2 .   ? -2.973  -3.770  23.592 1.00 10.59  ? 201 HEM A CMC  1 
HETATM 6060 C  CAC  . HEM C 2 .   ? -5.859  -2.923  22.413 1.00 10.33  ? 201 HEM A CAC  1 
HETATM 6061 C  CBC  . HEM C 2 .   ? -5.273  -1.797  22.143 1.00 11.45  ? 201 HEM A CBC  1 
HETATM 6062 C  C1D  . HEM C 2 .   ? -7.760  -6.673  20.955 1.00 9.20   ? 201 HEM A C1D  1 
HETATM 6063 C  C2D  . HEM C 2 .   ? -9.124  -6.711  20.400 1.00 9.70   ? 201 HEM A C2D  1 
HETATM 6064 C  C3D  . HEM C 2 .   ? -9.370  -8.008  20.087 1.00 9.66   ? 201 HEM A C3D  1 
HETATM 6065 C  C4D  . HEM C 2 .   ? -8.154  -8.761  20.416 1.00 9.67   ? 201 HEM A C4D  1 
HETATM 6066 C  CMD  . HEM C 2 .   ? -10.001 -5.521  20.246 1.00 11.07  ? 201 HEM A CMD  1 
HETATM 6067 C  CAD  . HEM C 2 .   ? -10.604 -8.598  19.481 1.00 9.90   ? 201 HEM A CAD  1 
HETATM 6068 C  CBD  . HEM C 2 .   ? -10.477 -8.714  17.982 1.00 11.82  ? 201 HEM A CBD  1 
HETATM 6069 C  CGD  . HEM C 2 .   ? -11.758 -9.111  17.299 1.00 10.88  ? 201 HEM A CGD  1 
HETATM 6070 O  O1D  . HEM C 2 .   ? -12.385 -10.089 17.764 1.00 11.24  ? 201 HEM A O1D  1 
HETATM 6071 O  O2D  . HEM C 2 .   ? -12.087 -8.501  16.228 1.00 11.16  ? 201 HEM A O2D  1 
HETATM 6072 N  NA   . HEM C 2 .   ? -5.697  -10.342 21.048 1.00 9.99   ? 201 HEM A NA   1 
HETATM 6073 N  NB   . HEM C 2 .   ? -3.513  -8.970  22.218 1.00 9.37   ? 201 HEM A NB   1 
HETATM 6074 N  NC   . HEM C 2 .   ? -5.012  -6.522  22.067 1.00 9.19   ? 201 HEM A NC   1 
HETATM 6075 N  ND   . HEM C 2 .   ? -7.199  -7.917  20.938 1.00 9.26   ? 201 HEM A ND   1 
HETATM 6076 FE FE   . HEM C 2 .   ? -5.327  -8.426  21.488 1.00 9.31   ? 201 HEM A FE   1 
HETATM 6077 H  HHB  . HEM C 2 .   ? -3.069  -12.183 21.797 1.00 14.97  ? 201 HEM A HHB  1 
HETATM 6078 H  HHC  . HEM C 2 .   ? -2.053  -6.337  23.527 1.00 14.97  ? 201 HEM A HHC  1 
HETATM 6079 H  HHD  . HEM C 2 .   ? -7.607  -4.695  21.316 1.00 14.99  ? 201 HEM A HHD  1 
HETATM 6080 H  HAB  . HEM C 2 .   ? 0.420   -9.016  24.230 1.00 14.97  ? 201 HEM A HAB  1 
HETATM 6081 H  HAC  . HEM C 2 .   ? -6.781  -2.870  22.121 1.00 14.99  ? 201 HEM A HAC  1 
HETATM 6082 H  HHA  . HEM C 2 .   ? -8.707  -10.603 19.788 1.00 14.98  ? 201 HEM A HHA  1 
HETATM 6083 N  N1   . IMD D 3 .   ? -6.951  -8.549  25.386 1.00 16.55  ? 202 IMD A N1   1 
HETATM 6084 C  C2   . IMD D 3 .   ? -6.575  -7.946  24.254 1.00 13.54  ? 202 IMD A C2   1 
HETATM 6085 N  N3   . IMD D 3 .   ? -6.119  -8.805  23.383 1.00 11.80  ? 202 IMD A N3   1 
HETATM 6086 C  C4   . IMD D 3 .   ? -6.319  -10.025 23.938 1.00 14.03  ? 202 IMD A C4   1 
HETATM 6087 C  C5   . IMD D 3 .   ? -6.801  -9.862  25.186 1.00 12.51  ? 202 IMD A C5   1 
HETATM 6088 H  HN1  . IMD D 3 .   ? -7.279  -8.149  26.111 1.00 18.55  ? 202 IMD A HN1  1 
HETATM 6089 H  H2   . IMD D 3 .   ? -6.564  -7.012  24.133 1.00 18.56  ? 202 IMD A H2   1 
HETATM 6090 H  H4   . IMD D 3 .   ? -6.093  -10.854 23.557 1.00 18.66  ? 202 IMD A H4   1 
HETATM 6091 H  H5   . IMD D 3 .   ? -7.002  -10.551 25.794 1.00 18.49  ? 202 IMD A H5   1 
HETATM 6092 NA NA   . NA  E 4 .   ? -14.945 -11.060 17.413 1.00 13.40  ? 203 NA  A NA   1 
HETATM 6093 NA NA   . NA  F 4 .   ? -12.247 -14.359 22.114 1.00 15.19  ? 204 NA  A NA   1 
HETATM 6094 NA NA   . NA  G 4 .   ? -14.044 -9.696  15.092 1.00 15.78  ? 205 NA  A NA   1 
HETATM 6095 NA NA   . NA  H 4 .   ? -12.698 -13.428 25.592 1.00 16.88  ? 206 NA  A NA   1 
HETATM 6096 C  CHA  . HEM I 2 .   ? -23.974 -22.958 12.065 1.00 10.33  ? 201 HEM B CHA  1 
HETATM 6097 C  CHB  . HEM I 2 .   ? -25.669 -23.414 7.587  1.00 10.39  ? 201 HEM B CHB  1 
HETATM 6098 C  CHC  . HEM I 2 .   ? -29.034 -26.450 9.191  1.00 10.04  ? 201 HEM B CHC  1 
HETATM 6099 C  CHD  . HEM I 2 .   ? -27.294 -26.074 13.652 1.00 9.68   ? 201 HEM B CHD  1 
HETATM 6100 C  C1A  . HEM I 2 .   ? -24.123 -22.809 10.699 1.00 10.54  ? 201 HEM B C1A  1 
HETATM 6101 C  C2A  . HEM I 2 .   ? -23.331 -21.957 9.871  1.00 10.62  ? 201 HEM B C2A  1 
HETATM 6102 C  C3A  . HEM I 2 .   ? -23.839 -22.047 8.604  1.00 10.89  ? 201 HEM B C3A  1 
HETATM 6103 C  C4A  . HEM I 2 .   ? -24.917 -23.002 8.673  1.00 10.20  ? 201 HEM B C4A  1 
HETATM 6104 C  CMA  . HEM I 2 .   ? -23.433 -21.245 7.374  1.00 12.72  ? 201 HEM B CMA  1 
HETATM 6105 C  CAA  . HEM I 2 .   ? -22.128 -21.158 10.299 1.00 10.66  ? 201 HEM B CAA  1 
HETATM 6106 C  CBA  . HEM I 2 .   ? -22.459 -19.756 10.778 1.00 11.33  ? 201 HEM B CBA  1 
HETATM 6107 C  CGA  . HEM I 2 .   ? -21.200 -19.020 11.175 1.00 10.27  ? 201 HEM B CGA  1 
HETATM 6108 O  O1A  . HEM I 2 .   ? -21.172 -18.426 12.279 1.00 10.52  ? 201 HEM B O1A  1 
HETATM 6109 O  O2A  . HEM I 2 .   ? -20.232 -18.975 10.370 1.00 10.75  ? 201 HEM B O2A  1 
HETATM 6110 C  C1B  . HEM I 2 .   ? -26.716 -24.306 7.612  1.00 10.39  ? 201 HEM B C1B  1 
HETATM 6111 C  C2B  . HEM I 2 .   ? -27.554 -24.609 6.486  1.00 10.91  ? 201 HEM B C2B  1 
HETATM 6112 C  C3B  . HEM I 2 .   ? -28.564 -25.395 6.938  1.00 10.63  ? 201 HEM B C3B  1 
HETATM 6113 C  C4B  . HEM I 2 .   ? -28.294 -25.604 8.367  1.00 10.43  ? 201 HEM B C4B  1 
HETATM 6114 C  CMB  . HEM I 2 .   ? -27.358 -24.073 5.082  1.00 12.47  ? 201 HEM B CMB  1 
HETATM 6115 C  CAB  . HEM I 2 .   ? -29.718 -25.848 6.190  1.00 12.06  ? 201 HEM B CAB  1 
HETATM 6116 C  CBB  . HEM I 2 .   ? -30.985 -25.828 6.623  1.00 13.52  ? 201 HEM B CBB  1 
HETATM 6117 C  C1C  . HEM I 2 .   ? -28.820 -26.680 10.535 1.00 9.73   ? 201 HEM B C1C  1 
HETATM 6118 C  C2C  . HEM I 2 .   ? -29.634 -27.512 11.352 1.00 9.67   ? 201 HEM B C2C  1 
HETATM 6119 C  C3C  . HEM I 2 .   ? -29.151 -27.380 12.626 1.00 9.78   ? 201 HEM B C3C  1 
HETATM 6120 C  C4C  . HEM I 2 .   ? -28.039 -26.467 12.563 1.00 9.41   ? 201 HEM B C4C  1 
HETATM 6121 C  CMC  . HEM I 2 .   ? -30.835 -28.279 10.873 1.00 11.24  ? 201 HEM B CMC  1 
HETATM 6122 C  CAC  . HEM I 2 .   ? -29.679 -27.993 13.855 1.00 10.44  ? 201 HEM B CAC  1 
HETATM 6123 C  CBC  . HEM I 2 .   ? -30.136 -29.206 14.041 1.00 11.86  ? 201 HEM B CBC  1 
HETATM 6124 C  C1D  . HEM I 2 .   ? -26.241 -25.176 13.612 1.00 9.57   ? 201 HEM B C1D  1 
HETATM 6125 C  C2D  . HEM I 2 .   ? -25.476 -24.742 14.783 1.00 10.30  ? 201 HEM B C2D  1 
HETATM 6126 C  C3D  . HEM I 2 .   ? -24.574 -23.853 14.341 1.00 10.58  ? 201 HEM B C3D  1 
HETATM 6127 C  C4D  . HEM I 2 .   ? -24.746 -23.761 12.887 1.00 10.03  ? 201 HEM B C4D  1 
HETATM 6128 C  CMD  . HEM I 2 .   ? -25.742 -25.235 16.194 1.00 10.94  ? 201 HEM B CMD  1 
HETATM 6129 C  CAD  . HEM I 2 .   ? -23.565 -23.063 15.149 1.00 11.27  ? 201 HEM B CAD  1 
HETATM 6130 C  CBD  . HEM I 2 .   ? -22.126 -23.453 14.934 1.00 13.45  ? 201 HEM B CBD  1 
HETATM 6131 C  CGD  . HEM I 2 .   ? -21.645 -24.725 15.397 1.00 13.95  ? 201 HEM B CGD  1 
HETATM 6132 O  O1D  . HEM I 2 .   ? -20.988 -24.832 16.513 1.00 17.67  ? 201 HEM B O1D  1 
HETATM 6133 O  O2D  . HEM I 2 .   ? -21.964 -25.677 14.620 1.00 16.93  ? 201 HEM B O2D  1 
HETATM 6134 N  NA   . HEM I 2 .   ? -25.081 -23.470 9.953  1.00 10.24  ? 201 HEM B NA   1 
HETATM 6135 N  NB   . HEM I 2 .   ? -27.190 -24.923 8.733  1.00 9.90   ? 201 HEM B NB   1 
HETATM 6136 N  NC   . HEM I 2 .   ? -27.846 -26.037 11.268 1.00 9.43   ? 201 HEM B NC   1 
HETATM 6137 N  ND   . HEM I 2 .   ? -25.763 -24.555 12.488 1.00 9.67   ? 201 HEM B ND   1 
HETATM 6138 FE FE   . HEM I 2 .   ? -26.438 -24.774 10.615 1.00 9.62   ? 201 HEM B FE   1 
HETATM 6139 H  HHB  . HEM I 2 .   ? -25.456 -23.016 6.723  1.00 15.31  ? 201 HEM B HHB  1 
HETATM 6140 H  HHC  . HEM I 2 .   ? -29.780 -26.924 8.784  1.00 15.38  ? 201 HEM B HHC  1 
HETATM 6141 H  HHD  . HEM I 2 .   ? -27.530 -26.452 14.518 1.00 15.08  ? 201 HEM B HHD  1 
HETATM 6142 H  HAB  . HEM I 2 .   ? -29.693 -25.868 5.221  1.00 15.36  ? 201 HEM B HAB  1 
HETATM 6143 H  HAC  . HEM I 2 .   ? -29.235 -27.730 14.676 1.00 15.03  ? 201 HEM B HAC  1 
HETATM 6144 H  HHA  . HEM I 2 .   ? -23.253 -22.448 12.477 1.00 15.20  ? 201 HEM B HHA  1 
HETATM 6145 N  N1   . IMD J 3 .   ? -29.471 -22.050 11.598 1.00 15.43  ? 202 IMD B N1   1 
HETATM 6146 C  C2   . IMD J 3 .   ? -28.817 -23.211 11.705 1.00 12.85  ? 202 IMD B C2   1 
HETATM 6147 N  N3   . IMD J 3 .   ? -27.747 -23.187 10.948 1.00 11.82  ? 202 IMD B N3   1 
HETATM 6148 C  C4   . IMD J 3 .   ? -27.652 -21.972 10.406 1.00 12.84  ? 202 IMD B C4   1 
HETATM 6149 C  C5   . IMD J 3 .   ? -28.730 -21.275 10.793 1.00 11.38  ? 202 IMD B C5   1 
HETATM 6150 H  HN1  . IMD J 3 .   ? -30.229 -21.832 12.012 1.00 18.40  ? 202 IMD B HN1  1 
HETATM 6151 H  H2   . IMD J 3 .   ? -29.112 -23.953 12.203 1.00 18.40  ? 202 IMD B H2   1 
HETATM 6152 H  H4   . IMD J 3 .   ? -26.986 -21.662 9.817  1.00 18.40  ? 202 IMD B H4   1 
HETATM 6153 H  H5   . IMD J 3 .   ? -28.928 -20.394 10.536 1.00 18.39  ? 202 IMD B H5   1 
HETATM 6154 NA NA   . NA  K 4 .   ? -21.479 -18.783 19.833 1.00 14.72  ? 203 NA  B NA   1 
HETATM 6155 NA NA   . NA  L 4 .   ? -24.526 -14.764 22.525 1.00 16.03  ? 204 NA  B NA   1 
HETATM 6156 CL CL   . CL  M 5 .   ? -20.056 -20.146 17.504 1.00 11.62  ? 205 CL  B CL   1 
HETATM 6157 O  O    . HOH N 6 .   ? -23.448 -19.032 40.553 1.00 17.74  ? 301 HOH A O    1 
HETATM 6158 O  O    . HOH N 6 .   ? -15.216 -4.973  42.822 1.00 40.83  ? 302 HOH A O    1 
HETATM 6159 O  O    . HOH N 6 .   ? 2.220   -16.470 16.572 1.00 29.62  ? 303 HOH A O    1 
HETATM 6160 O  O    . HOH N 6 .   ? 8.276   -1.434  38.053 1.00 26.94  ? 304 HOH A O    1 
HETATM 6161 O  O    . HOH N 6 .   ? -26.708 5.233   42.444 1.00 37.43  ? 305 HOH A O    1 
HETATM 6162 O  O    . HOH N 6 .   ? -24.814 -11.032 34.402 1.00 33.58  ? 306 HOH A O    1 
HETATM 6163 O  O    . HOH N 6 .   ? -6.718  -8.299  38.299 1.00 31.83  ? 307 HOH A O    1 
HETATM 6164 O  O    . HOH N 6 .   ? -7.228  -17.565 24.210 1.00 23.35  ? 308 HOH A O    1 
HETATM 6165 O  O    . HOH N 6 .   ? -9.795  11.092  36.005 1.00 30.30  ? 309 HOH A O    1 
HETATM 6166 O  O    . HOH N 6 .   ? -8.657  -4.235  4.939  1.00 29.68  ? 310 HOH A O    1 
HETATM 6167 O  O    . HOH N 6 .   ? 4.701   -11.889 40.258 1.00 34.32  ? 311 HOH A O    1 
HETATM 6168 O  O    . HOH N 6 .   ? -0.638  -28.837 21.170 1.00 41.72  ? 312 HOH A O    1 
HETATM 6169 O  O    . HOH N 6 .   ? 1.462   -4.735  44.872 1.00 31.69  ? 313 HOH A O    1 
HETATM 6170 O  O    . HOH N 6 .   ? 0.370   -20.998 13.329 1.00 37.79  ? 314 HOH A O    1 
HETATM 6171 O  O    . HOH N 6 .   ? -20.500 3.964   20.622 1.00 19.82  ? 315 HOH A O    1 
HETATM 6172 O  O    . HOH N 6 .   ? 1.674   -26.146 19.138 1.00 26.27  ? 316 HOH A O    1 
HETATM 6173 O  O    . HOH N 6 .   ? -25.029 5.614   33.553 1.00 47.50  ? 317 HOH A O    1 
HETATM 6174 O  O    . HOH N 6 .   ? 0.613   6.723   33.456 1.00 21.64  ? 318 HOH A O    1 
HETATM 6175 O  O    . HOH N 6 .   ? 4.500   -7.351  36.223 1.00 39.88  ? 319 HOH A O    1 
HETATM 6176 O  O    . HOH N 6 .   ? 6.596   -6.168  15.743 1.00 26.35  ? 320 HOH A O    1 
HETATM 6177 O  O    . HOH N 6 .   ? -6.789  -3.121  47.499 1.00 39.90  ? 321 HOH A O    1 
HETATM 6178 O  O    . HOH N 6 .   ? -22.026 8.974   32.377 1.00 37.73  ? 322 HOH A O    1 
HETATM 6179 O  O    . HOH N 6 .   ? -17.782 3.847   11.584 1.00 22.89  ? 323 HOH A O    1 
HETATM 6180 O  O    . HOH N 6 .   ? 1.674   1.271   39.195 1.00 14.04  ? 324 HOH A O    1 
HETATM 6181 O  O    . HOH N 6 .   ? -12.356 -5.249  3.927  1.00 24.10  ? 325 HOH A O    1 
HETATM 6182 O  O    . HOH N 6 .   ? -12.282 -2.639  43.191 1.00 24.10  ? 326 HOH A O    1 
HETATM 6183 O  O    . HOH N 6 .   ? -24.794 -18.669 38.251 1.00 28.36  ? 327 HOH A O    1 
HETATM 6184 O  O    . HOH N 6 .   ? -5.475  -15.585 6.559  1.00 18.58  ? 328 HOH A O    1 
HETATM 6185 O  O    . HOH N 6 .   ? -0.978  3.738   44.201 1.00 20.65  ? 329 HOH A O    1 
HETATM 6186 O  O    . HOH N 6 .   ? -12.968 -12.201 0.021  1.00 20.87  ? 330 HOH A O    1 
HETATM 6187 O  O    . HOH N 6 .   ? -4.597  11.739  25.613 1.00 33.58  ? 331 HOH A O    1 
HETATM 6188 O  O    . HOH N 6 .   ? 5.068   -6.108  33.851 1.00 12.59  ? 332 HOH A O    1 
HETATM 6189 O  O    . HOH N 6 .   ? -2.627  5.906   24.356 1.00 15.38  ? 333 HOH A O    1 
HETATM 6190 O  O    . HOH N 6 .   ? 9.268   -4.812  28.878 1.00 17.02  ? 334 HOH A O    1 
HETATM 6191 O  O    . HOH N 6 .   ? -16.080 13.197  42.401 1.00 21.86  ? 335 HOH A O    1 
HETATM 6192 O  O    . HOH N 6 .   ? -12.106 -12.035 19.580 1.00 15.58  ? 336 HOH A O    1 
HETATM 6193 O  O    . HOH N 6 .   ? -7.736  4.217   17.434 1.00 14.92  ? 337 HOH A O    1 
HETATM 6194 O  O    . HOH N 6 .   ? -7.468  3.796   13.150 1.00 19.83  ? 338 HOH A O    1 
HETATM 6195 O  O    . HOH N 6 .   ? -18.532 7.919   46.647 1.00 24.02  ? 339 HOH A O    1 
HETATM 6196 O  O    . HOH N 6 .   ? -16.404 3.339   40.510 1.00 16.24  ? 340 HOH A O    1 
HETATM 6197 O  O    . HOH N 6 .   ? 1.416   -13.390 12.117 1.00 23.25  ? 341 HOH A O    1 
HETATM 6198 O  O    . HOH N 6 .   ? 4.665   -1.045  41.517 1.00 14.16  ? 342 HOH A O    1 
HETATM 6199 O  O    . HOH N 6 .   ? -1.982  -13.802 40.093 1.00 31.59  ? 343 HOH A O    1 
HETATM 6200 O  O    . HOH N 6 .   ? -21.050 -2.862  16.783 1.00 14.75  ? 344 HOH A O    1 
HETATM 6201 O  O    . HOH N 6 .   ? -3.473  -5.606  14.976 1.00 26.59  ? 345 HOH A O    1 
HETATM 6202 O  O    . HOH N 6 .   ? -0.012  3.101   32.160 1.00 12.88  ? 346 HOH A O    1 
HETATM 6203 O  O    . HOH N 6 .   ? -3.224  12.135  36.512 1.00 33.78  ? 347 HOH A O    1 
HETATM 6204 O  O    . HOH N 6 .   ? 0.505   -15.632 14.678 1.00 20.14  ? 348 HOH A O    1 
HETATM 6205 O  O    . HOH N 6 .   ? -20.227 -1.249  14.612 1.00 15.03  ? 349 HOH A O    1 
HETATM 6206 O  O    . HOH N 6 .   ? -10.862 0.840   47.518 1.00 42.40  ? 350 HOH A O    1 
HETATM 6207 O  O    . HOH N 6 .   ? -14.562 6.565   21.577 1.00 15.88  ? 351 HOH A O    1 
HETATM 6208 O  O    . HOH N 6 .   ? -23.483 -4.217  34.801 1.00 20.46  ? 352 HOH A O    1 
HETATM 6209 O  O    . HOH N 6 .   ? -24.246 0.060   19.799 1.00 24.18  ? 353 HOH A O    1 
HETATM 6210 O  O    . HOH N 6 .   ? -22.513 -4.815  10.017 1.00 25.56  ? 354 HOH A O    1 
HETATM 6211 O  O    . HOH N 6 .   ? -19.833 -19.957 38.694 1.00 15.08  ? 355 HOH A O    1 
HETATM 6212 O  O    . HOH N 6 .   ? 5.007   -23.716 17.388 1.00 39.90  ? 356 HOH A O    1 
HETATM 6213 O  O    . HOH N 6 .   ? -5.007  4.209   14.216 1.00 18.93  ? 357 HOH A O    1 
HETATM 6214 O  O    . HOH N 6 .   ? 0.801   -4.743  11.683 1.00 16.33  ? 358 HOH A O    1 
HETATM 6215 O  O    . HOH N 6 .   ? -10.813 11.170  19.956 1.00 17.36  ? 359 HOH A O    1 
HETATM 6216 O  O    . HOH N 6 .   ? -18.060 -8.192  20.804 1.00 10.76  ? 360 HOH A O    1 
HETATM 6217 O  O    . HOH N 6 .   ? -19.544 -12.144 21.836 1.00 12.06  ? 361 HOH A O    1 
HETATM 6218 O  O    . HOH N 6 .   ? 6.741   -15.763 29.605 1.00 19.81  ? 362 HOH A O    1 
HETATM 6219 O  O    . HOH N 6 .   ? -18.710 4.982   43.145 1.00 22.31  ? 363 HOH A O    1 
HETATM 6220 O  O    . HOH N 6 .   ? -18.911 -5.730  5.221  1.00 17.76  ? 364 HOH A O    1 
HETATM 6221 O  O    . HOH N 6 .   ? -22.806 -8.657  40.192 1.00 18.84  ? 365 HOH A O    1 
HETATM 6222 O  O    . HOH N 6 .   ? -20.532 3.398   46.165 1.00 43.66  ? 366 HOH A O    1 
HETATM 6223 O  O    . HOH N 6 .   ? -21.228 -3.733  20.807 1.00 13.26  ? 367 HOH A O    1 
HETATM 6224 O  O    . HOH N 6 .   ? -7.037  -6.062  43.478 1.00 28.03  ? 368 HOH A O    1 
HETATM 6225 O  O    . HOH N 6 .   ? 8.839   -2.894  21.657 1.00 28.67  ? 369 HOH A O    1 
HETATM 6226 O  O    . HOH N 6 .   ? 9.075   -4.536  37.442 1.00 42.26  ? 370 HOH A O    1 
HETATM 6227 O  O    . HOH N 6 .   ? 8.884   -7.394  32.294 1.00 25.31  ? 371 HOH A O    1 
HETATM 6228 O  O    . HOH N 6 .   ? -18.337 0.718   8.053  1.00 18.84  ? 372 HOH A O    1 
HETATM 6229 O  O    . HOH N 6 .   ? 1.544   -24.311 25.619 1.00 16.62  ? 373 HOH A O    1 
HETATM 6230 O  O    . HOH N 6 .   ? -0.469  -5.202  43.409 1.00 35.01  ? 374 HOH A O    1 
HETATM 6231 O  O    . HOH N 6 .   ? 0.601   4.063   15.712 1.00 18.67  ? 375 HOH A O    1 
HETATM 6232 O  O    . HOH N 6 .   ? -13.925 7.332   14.570 1.00 23.20  ? 376 HOH A O    1 
HETATM 6233 O  O    . HOH N 6 .   ? -18.997 14.139  44.175 1.00 16.91  ? 377 HOH A O    1 
HETATM 6234 O  O    . HOH N 6 .   ? -14.269 -18.046 33.432 1.00 32.46  ? 378 HOH A O    1 
HETATM 6235 O  O    . HOH N 6 .   ? 3.608   -17.967 31.338 1.00 16.84  ? 379 HOH A O    1 
HETATM 6236 O  O    . HOH N 6 .   ? -7.269  -13.111 31.063 1.00 22.31  ? 380 HOH A O    1 
HETATM 6237 O  O    . HOH N 6 .   ? -1.140  -19.525 30.548 1.00 14.80  ? 381 HOH A O    1 
HETATM 6238 O  O    . HOH N 6 .   ? -7.356  -2.287  4.081  1.00 34.16  ? 382 HOH A O    1 
HETATM 6239 O  O    . HOH N 6 .   ? -20.172 -12.075 5.023  1.00 18.58  ? 383 HOH A O    1 
HETATM 6240 O  O    . HOH N 6 .   ? -13.582 -15.279 32.591 1.00 20.29  ? 384 HOH A O    1 
HETATM 6241 O  O    . HOH N 6 .   ? -8.126  -16.062 6.147  1.00 19.24  ? 385 HOH A O    1 
HETATM 6242 O  O    . HOH N 6 .   ? 2.187   6.336   29.898 1.00 20.51  ? 386 HOH A O    1 
HETATM 6243 O  O    . HOH N 6 .   ? -18.937 2.716   41.307 1.00 21.00  ? 387 HOH A O    1 
HETATM 6244 O  O    . HOH N 6 .   ? 5.650   1.113   18.542 1.00 18.02  ? 388 HOH A O    1 
HETATM 6245 O  O    . HOH N 6 .   ? -23.757 9.727   37.851 1.00 25.74  ? 389 HOH A O    1 
HETATM 6246 O  O    . HOH N 6 .   ? -12.285 -16.765 27.528 1.00 19.62  ? 390 HOH A O    1 
HETATM 6247 O  O    . HOH N 6 .   ? -4.185  1.740   11.405 1.00 18.51  ? 391 HOH A O    1 
HETATM 6248 O  O    . HOH N 6 .   ? -19.935 -8.319  42.079 1.00 13.17  ? 392 HOH A O    1 
HETATM 6249 O  O    . HOH N 6 .   ? -0.404  -17.760 32.562 1.00 19.70  ? 393 HOH A O    1 
HETATM 6250 O  O    . HOH N 6 .   ? 0.270   -17.437 38.889 1.00 22.44  ? 394 HOH A O    1 
HETATM 6251 O  O    . HOH N 6 .   ? -22.457 -9.343  5.468  1.00 34.20  ? 395 HOH A O    1 
HETATM 6252 O  O    . HOH N 6 .   ? 1.333   4.607   22.287 1.00 15.08  ? 396 HOH A O    1 
HETATM 6253 O  O    . HOH N 6 .   ? -2.161  -6.691  39.332 1.00 26.71  ? 397 HOH A O    1 
HETATM 6254 O  O    . HOH N 6 .   ? -15.100 -15.518 14.688 1.00 14.56  ? 398 HOH A O    1 
HETATM 6255 O  O    . HOH N 6 .   ? -0.868  -9.379  36.269 1.00 14.64  ? 399 HOH A O    1 
HETATM 6256 O  O    . HOH N 6 .   ? -19.333 9.552   26.137 1.00 31.74  ? 400 HOH A O    1 
HETATM 6257 O  O    . HOH N 6 .   ? -8.075  9.774   40.670 1.00 26.42  ? 401 HOH A O    1 
HETATM 6258 O  O    . HOH N 6 .   ? 4.416   -2.950  13.826 1.00 22.34  ? 402 HOH A O    1 
HETATM 6259 O  O    . HOH N 6 .   ? -14.620 -17.320 28.965 1.00 14.65  ? 403 HOH A O    1 
HETATM 6260 O  O    . HOH N 6 .   ? 1.597   -13.026 7.793  1.00 33.39  ? 404 HOH A O    1 
HETATM 6261 O  O    . HOH N 6 .   ? 1.845   -2.570  12.963 1.00 16.50  ? 405 HOH A O    1 
HETATM 6262 O  O    . HOH N 6 .   ? -11.675 -14.405 0.916  1.00 23.84  ? 406 HOH A O    1 
HETATM 6263 O  O    . HOH N 6 .   ? -9.949  0.247   5.475  1.00 37.43  ? 407 HOH A O    1 
HETATM 6264 O  O    . HOH N 6 .   ? 6.333   -12.899 18.147 1.00 24.65  ? 408 HOH A O    1 
HETATM 6265 O  O    . HOH N 6 .   ? -5.479  9.909   18.932 1.00 26.21  ? 409 HOH A O    1 
HETATM 6266 O  O    . HOH N 6 .   ? -12.916 12.345  29.572 1.00 29.69  ? 410 HOH A O    1 
HETATM 6267 O  O    . HOH N 6 .   ? -27.398 -3.453  23.963 1.00 20.89  ? 411 HOH A O    1 
HETATM 6268 O  O    . HOH N 6 .   ? 3.040   -23.728 19.249 1.00 19.71  ? 412 HOH A O    1 
HETATM 6269 O  O    . HOH N 6 .   ? -19.239 -11.772 18.330 1.00 11.56  ? 413 HOH A O    1 
HETATM 6270 O  O    . HOH N 6 .   ? -9.162  4.432   15.094 1.00 19.24  ? 414 HOH A O    1 
HETATM 6271 O  O    . HOH N 6 .   ? -9.846  3.813   8.447  1.00 36.90  ? 415 HOH A O    1 
HETATM 6272 O  O    . HOH N 6 .   ? -12.945 8.776   44.786 1.00 35.96  ? 416 HOH A O    1 
HETATM 6273 O  O    . HOH N 6 .   ? 8.810   -6.169  24.685 1.00 25.36  ? 417 HOH A O    1 
HETATM 6274 O  O    . HOH N 6 .   ? -17.006 -10.306 19.290 1.00 10.46  ? 418 HOH A O    1 
HETATM 6275 O  O    . HOH N 6 .   ? -6.899  7.806   16.325 1.00 24.40  ? 419 HOH A O    1 
HETATM 6276 O  O    . HOH N 6 .   ? -1.152  -25.156 25.420 1.00 20.69  ? 420 HOH A O    1 
HETATM 6277 O  O    . HOH N 6 .   ? -1.022  3.202   34.623 1.00 17.82  ? 421 HOH A O    1 
HETATM 6278 O  O    . HOH N 6 .   ? -27.206 -0.460  36.850 1.00 30.92  ? 422 HOH A O    1 
HETATM 6279 O  O    . HOH N 6 .   ? -0.500  -18.737 12.380 1.00 27.03  ? 423 HOH A O    1 
HETATM 6280 O  O    . HOH N 6 .   ? -24.526 -0.855  28.358 1.00 35.70  ? 424 HOH A O    1 
HETATM 6281 O  O    . HOH N 6 .   ? -12.099 -9.052  34.060 1.00 14.94  ? 425 HOH A O    1 
HETATM 6282 O  O    . HOH N 6 .   ? -8.999  -12.916 27.493 1.00 19.25  ? 426 HOH A O    1 
HETATM 6283 O  O    . HOH N 6 .   ? 6.338   -7.903  35.604 1.00 20.28  ? 427 HOH A O    1 
HETATM 6284 O  O    . HOH N 6 .   ? -20.955 -2.485  27.771 1.00 18.00  ? 428 HOH A O    1 
HETATM 6285 O  O    . HOH N 6 .   ? -6.222  -13.308 23.870 1.00 20.39  ? 429 HOH A O    1 
HETATM 6286 O  O    . HOH N 6 .   ? -0.935  -11.656 28.135 1.00 12.77  ? 430 HOH A O    1 
HETATM 6287 O  O    . HOH N 6 .   ? 4.140   7.536   34.023 1.00 18.45  ? 431 HOH A O    1 
HETATM 6288 O  O    . HOH N 6 .   ? 6.170   -3.026  40.425 1.00 22.57  ? 432 HOH A O    1 
HETATM 6289 O  O    . HOH N 6 .   ? 0.450   -14.956 9.977  1.00 28.16  ? 433 HOH A O    1 
HETATM 6290 O  O    . HOH N 6 .   ? -7.407  -9.273  36.656 1.00 32.46  ? 434 HOH A O    1 
HETATM 6291 O  O    . HOH N 6 .   ? -20.731 -0.901  19.795 1.00 25.66  ? 435 HOH A O    1 
HETATM 6292 O  O    . HOH N 6 .   ? -21.346 -9.524  17.114 1.00 15.69  ? 436 HOH A O    1 
HETATM 6293 O  O    . HOH N 6 .   ? 5.622   -19.202 23.705 1.00 15.92  ? 437 HOH A O    1 
HETATM 6294 O  O    . HOH N 6 .   ? -11.665 -4.040  40.883 1.00 24.74  ? 438 HOH A O    1 
HETATM 6295 O  O    . HOH N 6 .   ? -2.249  -12.614 30.348 1.00 12.71  ? 439 HOH A O    1 
HETATM 6296 O  O    . HOH N 6 .   ? -10.633 -4.730  12.732 1.00 14.68  ? 440 HOH A O    1 
HETATM 6297 O  O    . HOH N 6 .   ? -9.242  -22.392 25.903 1.00 43.53  ? 441 HOH A O    1 
HETATM 6298 O  O    . HOH N 6 .   ? -25.196 -6.455  12.784 1.00 34.82  ? 442 HOH A O    1 
HETATM 6299 O  O    . HOH N 6 .   ? 10.232  -9.442  22.917 1.00 40.69  ? 443 HOH A O    1 
HETATM 6300 O  O    . HOH N 6 .   ? 0.041   2.778   9.586  1.00 33.04  ? 444 HOH A O    1 
HETATM 6301 O  O    . HOH N 6 .   ? -2.682  12.190  33.057 1.00 40.76  ? 445 HOH A O    1 
HETATM 6302 O  O    . HOH N 6 .   ? -0.065  -0.473  44.408 1.00 17.19  ? 446 HOH A O    1 
HETATM 6303 O  O    . HOH N 6 .   ? -22.103 2.988   29.647 1.00 32.62  ? 447 HOH A O    1 
HETATM 6304 O  O    . HOH N 6 .   ? -8.329  -18.957 12.286 1.00 13.79  ? 448 HOH A O    1 
HETATM 6305 O  O    . HOH N 6 .   ? 6.879   4.062   24.378 1.00 16.77  ? 449 HOH A O    1 
HETATM 6306 O  O    . HOH N 6 .   ? -20.264 -11.745 9.569  1.00 13.72  ? 450 HOH A O    1 
HETATM 6307 O  O    . HOH N 6 .   ? -20.027 1.491   14.490 1.00 22.55  ? 451 HOH A O    1 
HETATM 6308 O  O    . HOH N 6 .   ? 11.174  1.628   31.989 1.00 34.59  ? 452 HOH A O    1 
HETATM 6309 O  O    . HOH N 6 .   ? -16.974 14.490  38.011 1.00 34.72  ? 453 HOH A O    1 
HETATM 6310 O  O    . HOH N 6 .   ? -23.918 -3.269  20.595 1.00 17.06  ? 454 HOH A O    1 
HETATM 6311 O  O    . HOH N 6 .   ? -11.949 8.575   22.730 1.00 18.71  ? 455 HOH A O    1 
HETATM 6312 O  O    . HOH N 6 .   ? -7.585  13.029  21.486 1.00 32.45  ? 456 HOH A O    1 
HETATM 6313 O  O    . HOH N 6 .   ? 6.005   4.100   34.910 1.00 24.72  ? 457 HOH A O    1 
HETATM 6314 O  O    . HOH N 6 .   ? -22.715 -9.395  11.155 1.00 20.68  ? 458 HOH A O    1 
HETATM 6315 O  O    . HOH N 6 .   ? -2.035  11.047  29.015 1.00 34.96  ? 459 HOH A O    1 
HETATM 6316 O  O    . HOH N 6 .   ? -6.101  12.121  30.876 1.00 27.38  ? 460 HOH A O    1 
HETATM 6317 O  O    . HOH N 6 .   ? -9.463  -5.588  39.560 1.00 25.42  ? 461 HOH A O    1 
HETATM 6318 O  O    . HOH N 6 .   ? -12.232 4.576   11.856 1.00 34.72  ? 462 HOH A O    1 
HETATM 6319 O  O    . HOH N 6 .   ? -10.135 -18.144 2.398  1.00 34.00  ? 463 HOH A O    1 
HETATM 6320 O  O    . HOH N 6 .   ? -0.579  5.290   20.485 1.00 16.76  ? 464 HOH A O    1 
HETATM 6321 O  O    . HOH N 6 .   ? -2.121  -28.090 23.267 1.00 39.55  ? 465 HOH A O    1 
HETATM 6322 O  O    . HOH N 6 .   ? -12.747 2.971   46.732 1.00 29.89  ? 466 HOH A O    1 
HETATM 6323 O  O    . HOH N 6 .   ? 8.100   2.452   31.836 1.00 20.40  ? 467 HOH A O    1 
HETATM 6324 O  O    . HOH N 6 .   ? -20.866 -19.931 30.534 1.00 22.68  ? 468 HOH A O    1 
HETATM 6325 O  O    . HOH N 6 .   ? -10.721 11.588  27.771 1.00 22.39  ? 469 HOH A O    1 
HETATM 6326 O  O    . HOH N 6 .   ? 11.063  4.021   30.148 1.00 33.80  ? 470 HOH A O    1 
HETATM 6327 O  O    . HOH N 6 .   ? -20.826 -1.477  5.394  1.00 45.55  ? 471 HOH A O    1 
HETATM 6328 O  O    . HOH N 6 .   ? -6.673  13.373  28.264 1.00 49.28  ? 472 HOH A O    1 
HETATM 6329 O  O    . HOH N 6 .   ? -19.742 -19.395 34.868 1.00 36.68  ? 473 HOH A O    1 
HETATM 6330 O  O    . HOH N 6 .   ? -5.599  4.677   45.427 1.00 32.33  ? 474 HOH A O    1 
HETATM 6331 O  O    . HOH N 6 .   ? -15.359 -3.593  45.012 1.00 34.92  ? 475 HOH A O    1 
HETATM 6332 O  O    . HOH N 6 .   ? -9.734  -9.382  4.203  1.00 18.64  ? 476 HOH A O    1 
HETATM 6333 O  O    . HOH N 6 .   ? -22.015 6.327   17.634 1.00 22.98  ? 477 HOH A O    1 
HETATM 6334 O  O    . HOH N 6 .   ? -25.376 -2.490  43.019 1.00 26.58  ? 478 HOH A O    1 
HETATM 6335 O  O    . HOH N 6 .   ? 8.907   -16.306 22.477 1.00 30.55  ? 479 HOH A O    1 
HETATM 6336 O  O    . HOH N 6 .   ? -8.949  -4.020  17.402 1.00 19.96  ? 480 HOH A O    1 
HETATM 6337 O  O    . HOH N 6 .   ? 5.345   -12.228 35.056 1.00 18.86  ? 481 HOH A O    1 
HETATM 6338 O  O    . HOH N 6 .   ? -4.592  -15.200 34.524 1.00 30.10  ? 482 HOH A O    1 
HETATM 6339 O  O    . HOH N 6 .   ? -24.742 -10.619 37.974 1.00 22.06  ? 483 HOH A O    1 
HETATM 6340 O  O    . HOH N 6 .   ? -6.145  -21.432 27.783 1.00 39.96  ? 484 HOH A O    1 
HETATM 6341 O  O    . HOH N 6 .   ? -5.134  -19.428 28.313 1.00 27.43  ? 485 HOH A O    1 
HETATM 6342 O  O    . HOH N 6 .   ? -1.577  8.050   29.350 1.00 26.08  ? 486 HOH A O    1 
HETATM 6343 O  O    . HOH N 6 .   ? -24.690 -4.199  29.130 1.00 31.91  ? 487 HOH A O    1 
HETATM 6344 O  O    . HOH N 6 .   ? -23.462 3.541   32.128 1.00 24.86  ? 488 HOH A O    1 
HETATM 6345 O  O    . HOH N 6 .   ? -15.351 -8.482  0.898  1.00 27.77  ? 489 HOH A O    1 
HETATM 6346 O  O    . HOH N 6 .   ? -10.569 -18.149 10.988 1.00 12.48  ? 490 HOH A O    1 
HETATM 6347 O  O    . HOH N 6 .   ? -2.108  -4.502  40.944 1.00 32.97  ? 491 HOH A O    1 
HETATM 6348 O  O    . HOH N 6 .   ? -19.489 -1.490  25.635 1.00 12.78  ? 492 HOH A O    1 
HETATM 6349 O  O    . HOH N 6 .   ? -19.445 6.907   14.508 1.00 19.01  ? 493 HOH A O    1 
HETATM 6350 O  O    . HOH N 6 .   ? -4.600  10.127  39.713 1.00 28.59  ? 494 HOH A O    1 
HETATM 6351 O  O    . HOH N 6 .   ? -30.028 -6.702  24.286 1.00 27.55  ? 495 HOH A O    1 
HETATM 6352 O  O    . HOH N 6 .   ? -24.144 -9.284  13.562 1.00 15.51  ? 496 HOH A O    1 
HETATM 6353 O  O    . HOH N 6 .   ? -29.255 2.706   38.761 1.00 33.62  ? 497 HOH A O    1 
HETATM 6354 O  O    . HOH N 6 .   ? -22.238 -2.827  13.542 1.00 21.07  ? 498 HOH A O    1 
HETATM 6355 O  O    . HOH N 6 .   ? 9.321   -9.771  25.760 1.00 30.56  ? 499 HOH A O    1 
HETATM 6356 O  O    . HOH N 6 .   ? 5.808   6.030   25.952 1.00 20.65  ? 500 HOH A O    1 
HETATM 6357 O  O    . HOH N 6 .   ? 7.751   -13.117 20.547 1.00 29.30  ? 501 HOH A O    1 
HETATM 6358 O  O    . HOH N 6 .   ? -7.214  12.641  25.584 1.00 24.57  ? 502 HOH A O    1 
HETATM 6359 O  O    . HOH N 6 .   ? -4.342  -17.290 25.318 1.00 28.87  ? 503 HOH A O    1 
HETATM 6360 O  O    . HOH N 6 .   ? 8.835   -9.124  13.731 1.00 42.42  ? 504 HOH A O    1 
HETATM 6361 O  O    . HOH N 6 .   ? 7.705   -8.818  27.880 1.00 15.42  ? 505 HOH A O    1 
HETATM 6362 O  O    . HOH N 6 .   ? -27.300 -6.831  39.423 1.00 31.11  ? 506 HOH A O    1 
HETATM 6363 O  O    . HOH N 6 .   ? -0.731  -3.991  9.431  1.00 16.64  ? 507 HOH A O    1 
HETATM 6364 O  O    . HOH N 6 .   ? -14.292 3.448   10.451 1.00 36.36  ? 508 HOH A O    1 
HETATM 6365 O  O    . HOH N 6 .   ? -4.469  -2.925  48.159 1.00 38.11  ? 509 HOH A O    1 
HETATM 6366 O  O    . HOH N 6 .   ? -24.734 7.775   35.648 1.00 40.52  ? 510 HOH A O    1 
HETATM 6367 O  O    . HOH N 6 .   ? 0.061   -5.080  7.022  1.00 29.31  ? 511 HOH A O    1 
HETATM 6368 O  O    . HOH N 6 .   ? -14.131 0.231   6.657  1.00 25.14  ? 512 HOH A O    1 
HETATM 6369 O  O    . HOH N 6 .   ? -12.012 0.682   7.183  1.00 43.68  ? 513 HOH A O    1 
HETATM 6370 O  O    . HOH N 6 .   ? 1.680   -12.202 42.579 1.00 29.38  ? 514 HOH A O    1 
HETATM 6371 O  O    . HOH N 6 .   ? 10.013  -11.723 23.787 1.00 44.05  ? 515 HOH A O    1 
HETATM 6372 O  O    . HOH N 6 .   ? -10.556 -17.531 25.181 1.00 22.32  ? 516 HOH A O    1 
HETATM 6373 O  O    . HOH N 6 .   ? -20.980 -10.305 23.954 1.00 11.47  ? 517 HOH A O    1 
HETATM 6374 O  O    . HOH N 6 .   ? -4.705  -7.010  39.333 1.00 32.69  ? 518 HOH A O    1 
HETATM 6375 O  O    . HOH N 6 .   ? -23.532 -6.698  11.408 1.00 35.12  ? 519 HOH A O    1 
HETATM 6376 O  O    . HOH N 6 .   ? -7.059  -14.749 33.178 1.00 32.29  ? 520 HOH A O    1 
HETATM 6377 O  O    . HOH N 6 .   ? -8.426  8.888   43.683 1.00 39.52  ? 521 HOH A O    1 
HETATM 6378 O  O    . HOH N 6 .   ? -25.185 -4.958  41.747 1.00 25.73  ? 522 HOH A O    1 
HETATM 6379 O  O    . HOH N 6 .   ? -18.812 -0.030  42.059 1.00 29.87  ? 523 HOH A O    1 
HETATM 6380 O  O    . HOH N 6 .   ? -4.599  -1.599  3.907  1.00 42.46  ? 524 HOH A O    1 
HETATM 6381 O  O    . HOH N 6 .   ? -22.940 -1.661  30.699 1.00 42.99  ? 525 HOH A O    1 
HETATM 6382 O  O    . HOH N 6 .   ? 0.354   -1.442  8.556  1.00 36.09  ? 526 HOH A O    1 
HETATM 6383 O  O    . HOH N 6 .   ? -2.536  0.385   8.175  1.00 38.50  ? 527 HOH A O    1 
HETATM 6384 O  O    . HOH N 6 .   ? -17.167 9.730   39.590 1.00 25.48  ? 528 HOH A O    1 
HETATM 6385 O  O    . HOH N 6 .   ? 0.052   5.388   24.623 1.00 16.37  ? 529 HOH A O    1 
HETATM 6386 O  O    . HOH N 6 .   ? -28.892 4.197   41.840 1.00 46.47  ? 530 HOH A O    1 
HETATM 6387 O  O    . HOH N 6 .   ? 11.028  5.876   29.227 1.00 42.57  ? 531 HOH A O    1 
HETATM 6388 O  O    . HOH N 6 .   ? -21.511 -8.990  3.412  1.00 35.10  ? 532 HOH A O    1 
HETATM 6389 O  O    . HOH N 6 .   ? -10.294 -7.060  34.791 1.00 21.10  ? 533 HOH A O    1 
HETATM 6390 O  O    . HOH N 6 .   ? -10.391 -14.924 31.126 1.00 35.58  ? 534 HOH A O    1 
HETATM 6391 O  O    . HOH N 6 .   ? -4.026  -14.761 29.872 1.00 23.30  ? 535 HOH A O    1 
HETATM 6392 O  O    . HOH N 6 .   ? -5.445  -16.386 29.865 1.00 31.00  ? 536 HOH A O    1 
HETATM 6393 O  O    . HOH N 6 .   ? -25.076 6.773   40.494 1.00 39.89  ? 537 HOH A O    1 
HETATM 6394 O  O    . HOH N 6 .   ? -20.852 5.827   25.329 1.00 42.97  ? 538 HOH A O    1 
HETATM 6395 O  O    . HOH N 6 .   ? -24.977 -0.723  16.538 1.00 36.13  ? 539 HOH A O    1 
HETATM 6396 O  O    . HOH N 6 .   ? -0.970  11.768  35.128 1.00 45.24  ? 540 HOH A O    1 
HETATM 6397 O  O    . HOH N 6 .   ? 3.015   -7.157  8.345  1.00 43.27  ? 541 HOH A O    1 
HETATM 6398 O  O    . HOH N 6 .   ? -2.495  -3.786  46.944 1.00 40.54  ? 542 HOH A O    1 
HETATM 6399 O  O    . HOH N 6 .   ? -3.200  -16.321 32.072 1.00 28.93  ? 543 HOH A O    1 
HETATM 6400 O  O    . HOH N 6 .   ? -7.279  -12.395 26.386 1.00 18.69  ? 544 HOH A O    1 
HETATM 6401 O  O    . HOH N 6 .   ? -32.878 -2.565  37.058 1.00 39.69  ? 545 HOH A O    1 
HETATM 6402 O  O    . HOH N 6 .   ? -10.687 -14.887 24.323 1.00 12.91  ? 546 HOH A O    1 
HETATM 6403 O  O    . HOH N 6 .   ? -20.986 0.309   6.833  1.00 41.68  ? 547 HOH A O    1 
HETATM 6404 O  O    . HOH N 6 .   ? -27.238 -3.881  44.731 1.00 26.84  ? 548 HOH A O    1 
HETATM 6405 O  O    . HOH N 6 .   ? -6.818  -8.122  1.289  1.00 46.95  ? 549 HOH A O    1 
HETATM 6406 O  O    . HOH N 6 .   ? -11.073 -18.214 8.350  1.00 21.64  ? 550 HOH A O    1 
HETATM 6407 O  O    . HOH N 6 .   ? -2.272  -19.668 10.356 1.00 48.00  ? 551 HOH A O    1 
HETATM 6408 O  O    . HOH N 6 .   ? -8.811  13.472  30.603 1.00 40.97  ? 552 HOH A O    1 
HETATM 6409 O  O    . HOH N 6 .   ? 5.512   -16.065 32.038 1.00 20.26  ? 553 HOH A O    1 
HETATM 6410 O  O    . HOH N 6 .   ? -10.282 8.789   44.587 1.00 36.47  ? 554 HOH A O    1 
HETATM 6411 O  O    . HOH N 6 .   ? -22.710 -19.705 35.328 1.00 42.50  ? 555 HOH A O    1 
HETATM 6412 O  O    . HOH N 6 .   ? -23.681 -2.788  17.720 1.00 16.70  ? 556 HOH A O    1 
HETATM 6413 O  O    . HOH N 6 .   ? -12.503 12.738  37.746 1.00 46.32  ? 557 HOH A O    1 
HETATM 6414 O  O    . HOH N 6 .   ? -23.821 4.056   17.347 1.00 36.32  ? 558 HOH A O    1 
HETATM 6415 O  O    . HOH N 6 .   ? -6.380  -19.613 10.318 1.00 25.67  ? 559 HOH A O    1 
HETATM 6416 O  O    . HOH N 6 .   ? 3.772   8.309   31.412 1.00 23.03  ? 560 HOH A O    1 
HETATM 6417 O  O    . HOH N 6 .   ? 2.361   -1.176  10.653 1.00 24.91  ? 561 HOH A O    1 
HETATM 6418 O  O    . HOH N 6 .   ? -0.731  -3.043  45.094 1.00 25.37  ? 562 HOH A O    1 
HETATM 6419 O  O    . HOH N 6 .   ? -5.149  -10.080 42.558 1.00 43.29  ? 563 HOH A O    1 
HETATM 6420 O  O    . HOH N 6 .   ? 7.321   -9.618  33.519 1.00 28.60  ? 564 HOH A O    1 
HETATM 6421 O  O    . HOH N 6 .   ? -12.867 -8.281  1.004  1.00 39.30  ? 565 HOH A O    1 
HETATM 6422 O  O    . HOH N 6 .   ? -22.273 -21.271 39.227 1.00 23.87  ? 566 HOH A O    1 
HETATM 6423 O  O    . HOH N 6 .   ? -5.380  -4.224  3.067  1.00 33.22  ? 567 HOH A O    1 
HETATM 6424 O  O    . HOH N 6 .   ? -26.839 -9.513  39.408 1.00 31.04  ? 568 HOH A O    1 
HETATM 6425 O  O    . HOH N 6 .   ? -9.850  -13.441 2.776  1.00 29.66  ? 569 HOH A O    1 
HETATM 6426 O  O    . HOH N 6 .   ? -28.777 -7.083  32.759 1.00 30.08  ? 570 HOH A O    1 
HETATM 6427 O  O    . HOH N 6 .   ? 4.753   1.722   15.943 1.00 24.94  ? 571 HOH A O    1 
HETATM 6428 O  O    . HOH N 6 .   ? -20.444 8.042   25.243 1.00 44.45  ? 572 HOH A O    1 
HETATM 6429 O  O    . HOH N 6 .   ? 2.899   4.086   36.013 1.00 24.12  ? 573 HOH A O    1 
HETATM 6430 O  O    . HOH N 6 .   ? 5.637   -6.420  44.059 1.00 47.08  ? 574 HOH A O    1 
HETATM 6431 O  O    . HOH N 6 .   ? 0.409   5.148   35.481 1.00 21.45  ? 575 HOH A O    1 
HETATM 6432 O  O    . HOH N 6 .   ? -21.485 10.922  33.879 1.00 40.84  ? 576 HOH A O    1 
HETATM 6433 O  O    . HOH N 6 .   ? -5.689  -14.809 28.201 1.00 31.01  ? 577 HOH A O    1 
HETATM 6434 O  O    . HOH N 6 .   ? -5.384  11.795  21.269 1.00 36.26  ? 578 HOH A O    1 
HETATM 6435 O  O    . HOH N 6 .   ? -7.629  11.193  34.280 1.00 35.26  ? 579 HOH A O    1 
HETATM 6436 O  O    . HOH N 6 .   ? 3.421   4.077   15.215 1.00 29.95  ? 580 HOH A O    1 
HETATM 6437 O  O    . HOH N 6 .   ? 5.104   -12.940 37.945 1.00 27.50  ? 581 HOH A O    1 
HETATM 6438 O  O    . HOH N 6 .   ? -6.130  3.316   10.300 1.00 36.10  ? 582 HOH A O    1 
HETATM 6439 O  O    . HOH N 6 .   ? -18.768 -20.095 32.800 1.00 49.15  ? 583 HOH A O    1 
HETATM 6440 O  O    . HOH N 6 .   ? -1.257  -5.724  4.721  1.00 34.97  ? 584 HOH A O    1 
HETATM 6441 O  O    . HOH N 6 .   ? 0.960   7.689   28.170 1.00 41.11  ? 585 HOH A O    1 
HETATM 6442 O  O    . HOH N 6 .   ? 5.489   -22.155 23.278 1.00 26.30  ? 586 HOH A O    1 
HETATM 6443 O  O    . HOH N 6 .   ? 9.545   7.486   27.928 1.00 42.80  ? 587 HOH A O    1 
HETATM 6444 O  O    . HOH N 6 .   ? 9.855   -11.548 21.216 1.00 44.76  ? 588 HOH A O    1 
HETATM 6445 O  O    . HOH N 6 .   ? 1.310   7.584   25.647 1.00 25.16  ? 589 HOH A O    1 
HETATM 6446 O  O    . HOH N 6 .   ? -9.498  -7.377  37.244 1.00 21.22  ? 590 HOH A O    1 
HETATM 6447 O  O    . HOH N 6 .   ? -11.390 13.362  35.347 1.00 36.64  ? 591 HOH A O    1 
HETATM 6448 O  O    . HOH N 6 .   ? -26.409 -4.163  14.047 1.00 34.94  ? 592 HOH A O    1 
HETATM 6449 O  O    . HOH N 6 .   ? 9.464   -8.836  29.979 1.00 24.43  ? 593 HOH A O    1 
HETATM 6450 O  O    . HOH N 6 .   ? -14.481 -1.366  4.592  1.00 30.67  ? 594 HOH A O    1 
HETATM 6451 O  O    . HOH N 6 .   ? 10.157  2.511   35.772 1.00 36.51  ? 595 HOH A O    1 
HETATM 6452 O  O    . HOH N 6 .   ? -23.685 -20.991 37.124 1.00 39.18  ? 596 HOH A O    1 
HETATM 6453 O  O    . HOH N 6 .   ? -0.546  4.995   13.442 1.00 29.14  ? 597 HOH A O    1 
HETATM 6454 O  O    . HOH N 6 .   ? 8.798   -12.076 17.171 1.00 35.61  ? 598 HOH A O    1 
HETATM 6455 O  O    . HOH N 6 .   ? 9.366   1.400   38.286 1.00 21.47  ? 599 HOH A O    1 
HETATM 6456 O  O    . HOH N 6 .   ? 5.765   4.628   21.931 1.00 21.58  ? 600 HOH A O    1 
HETATM 6457 O  O    . HOH N 6 .   ? -1.526  7.860   21.097 1.00 25.00  ? 601 HOH A O    1 
HETATM 6458 O  O    . HOH N 6 .   ? -4.975  10.120  23.107 1.00 27.10  ? 602 HOH A O    1 
HETATM 6459 O  O    . HOH N 6 .   ? 3.912   7.611   24.613 1.00 25.10  ? 603 HOH A O    1 
HETATM 6460 O  O    . HOH N 6 .   ? -8.744  3.211   6.011  1.00 46.56  ? 604 HOH A O    1 
HETATM 6461 O  O    . HOH N 6 .   ? -7.237  -11.035 38.772 1.00 33.70  ? 605 HOH A O    1 
HETATM 6462 O  O    . HOH N 6 .   ? -21.601 3.251   12.926 1.00 31.27  ? 606 HOH A O    1 
HETATM 6463 O  O    . HOH N 6 .   ? 7.666   -6.134  27.025 1.00 17.68  ? 607 HOH A O    1 
HETATM 6464 O  O    . HOH N 6 .   ? -22.259 0.501   17.786 1.00 31.60  ? 608 HOH A O    1 
HETATM 6465 O  O    . HOH N 6 .   ? -8.056  -15.563 3.173  1.00 25.72  ? 609 HOH A O    1 
HETATM 6466 O  O    . HOH N 6 .   ? -3.042  -29.998 20.957 1.00 37.58  ? 610 HOH A O    1 
HETATM 6467 O  O    . HOH N 6 .   ? -6.406  -17.345 27.061 1.00 29.04  ? 611 HOH A O    1 
HETATM 6468 O  O    . HOH N 6 .   ? -23.002 4.457   21.363 1.00 27.67  ? 612 HOH A O    1 
HETATM 6469 O  O    . HOH N 6 .   ? 3.536   6.238   22.148 1.00 20.42  ? 613 HOH A O    1 
HETATM 6470 O  O    . HOH N 6 .   ? 3.297   -25.865 24.001 1.00 36.69  ? 614 HOH A O    1 
HETATM 6471 O  O    . HOH N 6 .   ? -14.737 -3.760  4.053  1.00 38.17  ? 615 HOH A O    1 
HETATM 6472 O  O    . HOH N 6 .   ? -21.405 -4.517  5.542  1.00 25.39  ? 616 HOH A O    1 
HETATM 6473 O  O    . HOH N 6 .   ? 0.432   -27.156 16.785 1.00 32.88  ? 617 HOH A O    1 
HETATM 6474 O  O    . HOH N 6 .   ? -20.724 13.419  33.153 1.00 47.30  ? 618 HOH A O    1 
HETATM 6475 O  O    . HOH N 6 .   ? -12.737 -3.874  45.666 1.00 35.81  ? 619 HOH A O    1 
HETATM 6476 O  O    . HOH N 6 .   ? -11.152 -10.220 0.019  1.00 30.77  ? 620 HOH A O    1 
HETATM 6477 O  O    . HOH N 6 .   ? -17.540 6.375   12.106 1.00 23.41  ? 621 HOH A O    1 
HETATM 6478 O  O    . HOH N 6 .   ? -8.987  12.014  38.761 1.00 38.56  ? 622 HOH A O    1 
HETATM 6479 O  O    . HOH N 6 .   ? -1.554  -27.124 14.925 1.00 30.72  ? 623 HOH A O    1 
HETATM 6480 O  O    . HOH N 6 .   ? -12.343 14.932  32.731 1.00 50.74  ? 624 HOH A O    1 
HETATM 6481 O  O    . HOH N 6 .   ? -3.638  -24.961 26.598 1.00 28.65  ? 625 HOH A O    1 
HETATM 6482 O  O    . HOH N 6 .   ? 1.348   -17.485 11.026 1.00 50.91  ? 626 HOH A O    1 
HETATM 6483 O  O    . HOH N 6 .   ? -11.090 12.733  31.646 1.00 30.86  ? 627 HOH A O    1 
HETATM 6484 O  O    . HOH N 6 .   ? 4.645   -24.000 21.500 1.00 28.21  ? 628 HOH A O    1 
HETATM 6485 O  O    . HOH N 6 .   ? -4.213  12.154  38.838 1.00 36.11  ? 629 HOH A O    1 
HETATM 6486 O  O    . HOH N 6 .   ? 10.353  -0.455  38.819 1.00 44.34  ? 630 HOH A O    1 
HETATM 6487 O  O    . HOH N 6 .   ? -9.568  -10.942 1.980  1.00 27.05  ? 631 HOH A O    1 
HETATM 6488 O  O    . HOH N 6 .   ? 3.166   -5.832  10.686 1.00 29.69  ? 632 HOH A O    1 
HETATM 6489 O  O    . HOH N 6 .   ? 0.929   -14.665 5.786  1.00 60.91  ? 633 HOH A O    1 
HETATM 6490 O  O    . HOH N 6 .   ? -0.628  9.700   24.870 1.00 41.78  ? 634 HOH A O    1 
HETATM 6491 O  O    . HOH N 6 .   ? -16.507 -20.790 31.615 1.00 44.92  ? 635 HOH A O    1 
HETATM 6492 O  O    . HOH N 6 .   ? -10.674 -14.793 28.573 1.00 21.89  ? 636 HOH A O    1 
HETATM 6493 O  O    . HOH N 6 .   ? -2.887  8.447   23.486 1.00 23.05  ? 637 HOH A O    1 
HETATM 6494 O  O    . HOH N 6 .   ? -17.170 -4.512  3.325  1.00 24.66  ? 638 HOH A O    1 
HETATM 6495 O  O    . HOH N 6 .   ? -6.910  -6.861  40.553 1.00 35.80  ? 639 HOH A O    1 
HETATM 6496 O  O    . HOH N 6 .   ? -14.152 -19.020 31.046 1.00 25.37  ? 640 HOH A O    1 
HETATM 6497 O  O    . HOH N 6 .   ? 0.626   -14.485 40.097 1.00 34.16  ? 641 HOH A O    1 
HETATM 6498 O  O    . HOH N 6 .   ? 6.227   -17.397 21.557 1.00 25.84  ? 642 HOH A O    1 
HETATM 6499 O  O    . HOH N 6 .   ? -8.196  -13.758 24.740 1.00 30.62  ? 643 HOH A O    1 
HETATM 6500 O  O    . HOH N 6 .   ? -23.478 -6.295  6.921  1.00 40.86  ? 644 HOH A O    1 
HETATM 6501 O  O    . HOH N 6 .   ? -0.845  8.207   31.912 1.00 30.13  ? 645 HOH A O    1 
HETATM 6502 O  O    . HOH N 6 .   ? 9.336   -10.550 39.040 1.00 46.70  ? 646 HOH A O    1 
HETATM 6503 O  O    . HOH N 6 .   ? -13.832 -12.187 -2.479 1.00 33.96  ? 647 HOH A O    1 
HETATM 6504 O  O    . HOH N 6 .   ? -24.066 2.190   28.140 1.00 33.50  ? 648 HOH A O    1 
HETATM 6505 O  O    . HOH N 6 .   ? -7.927  -14.979 29.152 1.00 25.24  ? 649 HOH A O    1 
HETATM 6506 O  O    . HOH N 6 .   ? -11.918 -7.917  3.504  1.00 27.02  ? 650 HOH A O    1 
HETATM 6507 O  O    . HOH N 6 .   ? -8.024  -15.186 23.256 1.00 18.34  ? 651 HOH A O    1 
HETATM 6508 O  O    . HOH N 6 .   ? -24.321 -2.886  9.117  1.00 38.89  ? 652 HOH A O    1 
HETATM 6509 O  O    . HOH N 6 .   ? 11.212  -6.881  28.962 1.00 37.18  ? 653 HOH A O    1 
HETATM 6510 O  O    . HOH N 6 .   ? -28.550 -5.314  34.884 0.50 33.13  ? 654 HOH A O    1 
HETATM 6511 O  O    . HOH N 6 .   ? 0.675   -6.772  46.803 1.00 41.61  ? 655 HOH A O    1 
HETATM 6512 O  O    . HOH N 6 .   ? -10.214 -19.984 4.330  1.00 30.38  ? 656 HOH A O    1 
HETATM 6513 O  O    . HOH N 6 .   ? 5.095   -0.089  14.000 1.00 36.29  ? 657 HOH A O    1 
HETATM 6514 O  O    . HOH N 6 .   ? -4.861  -23.285 28.689 1.00 48.33  ? 658 HOH A O    1 
HETATM 6515 O  O    . HOH N 6 .   ? 6.388   3.582   19.546 1.00 24.82  ? 659 HOH A O    1 
HETATM 6516 O  O    . HOH N 6 .   ? -21.215 7.840   30.001 1.00 32.04  ? 660 HOH A O    1 
HETATM 6517 O  O    . HOH N 6 .   ? -0.400  5.548   17.773 1.00 19.45  ? 661 HOH A O    1 
HETATM 6518 O  O    . HOH N 6 .   ? -5.419  5.471   16.598 1.00 17.34  ? 662 HOH A O    1 
HETATM 6519 O  O    . HOH N 6 .   ? -4.256  -15.263 4.297  1.00 38.61  ? 663 HOH A O    1 
HETATM 6520 O  O    . HOH N 6 .   ? -9.633  -6.582  41.742 1.00 47.02  ? 664 HOH A O    1 
HETATM 6521 O  O    . HOH N 6 .   ? 4.784   -14.772 34.276 1.00 17.13  ? 665 HOH A O    1 
HETATM 6522 O  O    . HOH N 6 .   ? 9.188   -7.721  40.247 1.00 45.46  ? 666 HOH A O    1 
HETATM 6523 O  O    . HOH N 6 .   ? -8.047  14.493  23.701 1.00 30.38  ? 667 HOH A O    1 
HETATM 6524 O  O    . HOH N 6 .   ? -20.528 2.272   8.111  1.00 25.96  ? 668 HOH A O    1 
HETATM 6525 O  O    . HOH N 6 .   ? -8.791  7.050   14.509 1.00 29.43  ? 669 HOH A O    1 
HETATM 6526 O  O    . HOH N 6 .   ? -8.375  -18.199 4.262  1.00 44.22  ? 670 HOH A O    1 
HETATM 6527 O  O    . HOH N 6 .   ? -10.890 14.065  26.858 1.00 30.70  ? 671 HOH A O    1 
HETATM 6528 O  O    . HOH N 6 .   ? 7.055   -4.490  42.868 1.00 33.22  ? 672 HOH A O    1 
HETATM 6529 O  O    . HOH N 6 .   ? 11.896  -5.858  22.576 1.00 35.77  ? 673 HOH A O    1 
HETATM 6530 O  O    . HOH N 6 .   ? -11.189 -20.054 6.840  1.00 24.53  ? 674 HOH A O    1 
HETATM 6531 O  O    . HOH N 6 .   ? -23.735 4.975   24.188 1.00 37.96  ? 675 HOH A O    1 
HETATM 6532 O  O    . HOH N 6 .   ? -16.019 5.923   10.795 1.00 43.25  ? 676 HOH A O    1 
HETATM 6533 O  O    . HOH N 6 .   ? -5.262  9.558   14.957 1.00 39.29  ? 677 HOH A O    1 
HETATM 6534 O  O    . HOH N 6 .   ? 2.057   -12.603 45.252 1.00 35.59  ? 678 HOH A O    1 
HETATM 6535 O  O    . HOH N 6 .   ? 12.929  -6.164  30.705 1.00 49.85  ? 679 HOH A O    1 
HETATM 6536 O  O    . HOH N 6 .   ? -3.102  8.726   18.983 1.00 26.86  ? 680 HOH A O    1 
HETATM 6537 O  O    . HOH N 6 .   ? -7.066  -19.684 8.097  1.00 32.83  ? 681 HOH A O    1 
HETATM 6538 O  O    . HOH N 6 .   ? -21.122 4.705   28.201 1.00 37.46  ? 682 HOH A O    1 
HETATM 6539 O  O    . HOH N 6 .   ? 4.106   1.020   11.356 1.00 36.92  ? 683 HOH A O    1 
HETATM 6540 O  O    . HOH N 6 .   ? -9.632  -6.587  44.180 1.00 44.39  ? 684 HOH A O    1 
HETATM 6541 O  O    . HOH N 6 .   ? -2.972  6.590   17.306 1.00 21.97  ? 685 HOH A O    1 
HETATM 6542 O  O    . HOH N 6 .   ? 3.605   4.266   12.607 1.00 49.46  ? 686 HOH A O    1 
HETATM 6543 O  O    . HOH N 6 .   ? -23.169 1.330   8.136  1.00 34.52  ? 687 HOH A O    1 
HETATM 6544 O  O    . HOH N 6 .   ? -8.134  -17.379 28.290 1.00 36.54  ? 688 HOH A O    1 
HETATM 6545 O  O    . HOH N 6 .   ? 3.539   -10.981 46.601 1.00 46.36  ? 689 HOH A O    1 
HETATM 6546 O  O    . HOH N 6 .   ? -0.535  -3.672  4.466  1.00 50.36  ? 690 HOH A O    1 
HETATM 6547 O  O    . HOH N 6 .   ? -2.821  7.876   14.826 1.00 38.94  ? 691 HOH A O    1 
HETATM 6548 O  O    . HOH N 6 .   ? 3.527   6.632   18.596 1.00 43.37  ? 692 HOH A O    1 
HETATM 6549 O  O    . HOH N 6 .   ? 5.543   5.403   17.597 1.00 45.70  ? 693 HOH A O    1 
HETATM 6550 O  O    . HOH N 6 .   ? 4.095   -3.227  9.326  1.00 46.51  ? 694 HOH A O    1 
HETATM 6551 O  O    . HOH N 6 .   ? 3.071   7.938   20.181 1.00 41.98  ? 695 HOH A O    1 
HETATM 6552 O  O    . HOH N 6 .   ? 1.301   7.580   17.833 1.00 36.30  ? 696 HOH A O    1 
HETATM 6553 O  O    . HOH N 6 .   ? 0.308   -13.510 47.072 1.00 46.07  ? 697 HOH A O    1 
HETATM 6554 O  O    . HOH N 6 .   ? 7.563   7.101   21.604 1.00 35.76  ? 698 HOH A O    1 
HETATM 6555 O  O    . HOH O 6 .   ? -17.763 -33.862 27.269 1.00 28.76  ? 301 HOH B O    1 
HETATM 6556 O  O    . HOH O 6 .   ? -19.675 -29.251 17.721 1.00 20.86  ? 302 HOH B O    1 
HETATM 6557 O  O    . HOH O 6 .   ? -33.187 -6.603  28.046 1.00 43.43  ? 303 HOH B O    1 
HETATM 6558 O  O    . HOH O 6 .   ? -28.211 -34.664 0.978  1.00 45.60  ? 304 HOH B O    1 
HETATM 6559 O  O    . HOH O 6 .   ? -51.031 -15.320 12.627 1.00 50.29  ? 305 HOH B O    1 
HETATM 6560 O  O    . HOH O 6 .   ? -29.945 -38.653 6.529  1.00 32.56  ? 306 HOH B O    1 
HETATM 6561 O  O    . HOH O 6 .   ? -46.987 -15.399 18.672 1.00 33.94  ? 307 HOH B O    1 
HETATM 6562 O  O    . HOH O 6 .   ? -53.241 -17.822 18.394 1.00 47.12  ? 308 HOH B O    1 
HETATM 6563 O  O    . HOH O 6 .   ? -13.975 -25.338 27.237 1.00 37.41  ? 309 HOH B O    1 
HETATM 6564 O  O    . HOH O 6 .   ? -7.103  -32.906 13.668 1.00 43.14  ? 310 HOH B O    1 
HETATM 6565 O  O    . HOH O 6 .   ? -24.267 -37.216 5.501  1.00 23.23  ? 311 HOH B O    1 
HETATM 6566 O  O    . HOH O 6 .   ? -24.124 -15.836 7.180  1.00 20.50  ? 312 HOH B O    1 
HETATM 6567 O  O    . HOH O 6 .   ? -40.597 -15.901 10.461 1.00 28.36  ? 313 HOH B O    1 
HETATM 6568 O  O    . HOH O 6 .   ? -37.260 -10.365 22.368 1.00 14.31  ? 314 HOH B O    1 
HETATM 6569 O  O    . HOH O 6 .   ? -23.781 -15.313 28.828 1.00 20.46  ? 315 HOH B O    1 
HETATM 6570 O  O    . HOH O 6 .   ? -20.400 -34.550 24.238 1.00 17.66  ? 316 HOH B O    1 
HETATM 6571 O  O    . HOH O 6 .   ? -36.166 -35.133 15.468 1.00 16.42  ? 317 HOH B O    1 
HETATM 6572 O  O    . HOH O 6 .   ? -48.019 -23.942 29.086 1.00 20.16  ? 318 HOH B O    1 
HETATM 6573 O  O    . HOH O 6 .   ? -21.104 -12.038 -0.297 1.00 24.02  ? 319 HOH B O    1 
HETATM 6574 O  O    . HOH O 6 .   ? -42.980 -17.875 -0.974 1.00 40.60  ? 320 HOH B O    1 
HETATM 6575 O  O    . HOH O 6 .   ? -39.755 -33.793 1.820  1.00 17.71  ? 321 HOH B O    1 
HETATM 6576 O  O    . HOH O 6 .   ? -48.138 -26.630 8.106  1.00 40.08  ? 322 HOH B O    1 
HETATM 6577 O  O    . HOH O 6 .   ? -11.869 -32.271 20.209 1.00 17.70  ? 323 HOH B O    1 
HETATM 6578 O  O    . HOH O 6 .   ? -22.186 -29.846 17.980 1.00 20.62  ? 324 HOH B O    1 
HETATM 6579 O  O    . HOH O 6 .   ? -20.432 -34.064 28.047 1.00 36.13  ? 325 HOH B O    1 
HETATM 6580 O  O    . HOH O 6 .   ? -26.133 -35.280 27.232 1.00 33.28  ? 326 HOH B O    1 
HETATM 6581 O  O    . HOH O 6 .   ? -45.713 -32.208 6.821  1.00 26.98  ? 327 HOH B O    1 
HETATM 6582 O  O    . HOH O 6 .   ? -26.181 -37.855 17.366 1.00 20.00  ? 328 HOH B O    1 
HETATM 6583 O  O    . HOH O 6 .   ? -42.037 -30.513 11.233 1.00 16.82  ? 329 HOH B O    1 
HETATM 6584 O  O    . HOH O 6 .   ? -37.548 -30.994 -0.816 1.00 22.31  ? 330 HOH B O    1 
HETATM 6585 O  O    . HOH O 6 .   ? -22.602 -30.597 11.615 1.00 18.47  ? 331 HOH B O    1 
HETATM 6586 O  O    . HOH O 6 .   ? -19.506 -17.312 21.002 1.00 10.34  ? 332 HOH B O    1 
HETATM 6587 O  O    . HOH O 6 .   ? -4.941  -29.239 16.992 1.00 19.37  ? 333 HOH B O    1 
HETATM 6588 O  O    . HOH O 6 .   ? -45.847 -17.937 24.447 1.00 22.57  ? 334 HOH B O    1 
HETATM 6589 O  O    . HOH O 6 .   ? -24.572 -36.820 19.370 1.00 21.30  ? 335 HOH B O    1 
HETATM 6590 O  O    . HOH O 6 .   ? -21.760 -25.474 26.520 1.00 17.06  ? 336 HOH B O    1 
HETATM 6591 O  O    . HOH O 6 .   ? -22.271 -14.967 20.752 1.00 11.52  ? 337 HOH B O    1 
HETATM 6592 O  O    . HOH O 6 .   ? -47.331 -26.546 29.647 1.00 26.70  ? 338 HOH B O    1 
HETATM 6593 O  O    . HOH O 6 .   ? -28.410 -34.940 19.586 1.00 16.35  ? 339 HOH B O    1 
HETATM 6594 O  O    . HOH O 6 .   ? -28.487 -39.642 12.418 1.00 20.56  ? 340 HOH B O    1 
HETATM 6595 O  O    . HOH O 6 .   ? -40.313 -25.426 1.922  1.00 15.49  ? 341 HOH B O    1 
HETATM 6596 O  O    . HOH O 6 .   ? -5.872  -29.711 20.874 1.00 28.76  ? 342 HOH B O    1 
HETATM 6597 O  O    . HOH O 6 .   ? -18.434 -25.706 2.578  1.00 20.49  ? 343 HOH B O    1 
HETATM 6598 O  O    . HOH O 6 .   ? -22.910 -16.704 13.412 1.00 11.07  ? 344 HOH B O    1 
HETATM 6599 O  O    . HOH O 6 .   ? -11.194 -33.056 14.971 1.00 15.31  ? 345 HOH B O    1 
HETATM 6600 O  O    . HOH O 6 .   ? -32.210 -39.190 20.310 1.00 25.68  ? 346 HOH B O    1 
HETATM 6601 O  O    . HOH O 6 .   ? -39.749 -33.431 17.740 1.00 20.87  ? 347 HOH B O    1 
HETATM 6602 O  O    . HOH O 6 .   ? -19.230 -23.041 17.545 1.00 12.49  ? 348 HOH B O    1 
HETATM 6603 O  O    . HOH O 6 .   ? -17.449 -29.112 3.118  1.00 21.71  ? 349 HOH B O    1 
HETATM 6604 O  O    . HOH O 6 .   ? -50.781 -27.337 20.718 1.00 27.05  ? 350 HOH B O    1 
HETATM 6605 O  O    . HOH O 6 .   ? -52.863 -26.306 27.213 1.00 18.99  ? 351 HOH B O    1 
HETATM 6606 O  O    . HOH O 6 .   ? -23.595 -19.037 21.623 1.00 11.38  ? 352 HOH B O    1 
HETATM 6607 O  O    . HOH O 6 .   ? -30.081 -14.541 -0.397 1.00 23.10  ? 353 HOH B O    1 
HETATM 6608 O  O    . HOH O 6 .   ? -19.045 -7.821  3.409  1.00 25.18  ? 354 HOH B O    1 
HETATM 6609 O  O    . HOH O 6 .   ? -29.208 -26.881 29.695 1.00 19.51  ? 355 HOH B O    1 
HETATM 6610 O  O    . HOH O 6 .   ? -13.735 -31.792 3.675  1.00 31.65  ? 356 HOH B O    1 
HETATM 6611 O  O    . HOH O 6 .   ? -48.382 -30.627 21.244 1.00 36.33  ? 357 HOH B O    1 
HETATM 6612 O  O    . HOH O 6 .   ? -36.074 -38.111 22.106 1.00 25.02  ? 358 HOH B O    1 
HETATM 6613 O  O    . HOH O 6 .   ? -46.195 -19.456 -1.818 1.00 37.10  ? 359 HOH B O    1 
HETATM 6614 O  O    . HOH O 6 .   ? -41.332 -23.925 -0.230 1.00 21.78  ? 360 HOH B O    1 
HETATM 6615 O  O    . HOH O 6 .   ? -25.798 -26.187 -4.088 1.00 48.21  ? 361 HOH B O    1 
HETATM 6616 O  O    . HOH O 6 .   ? -29.038 -38.325 20.934 1.00 31.23  ? 362 HOH B O    1 
HETATM 6617 O  O    . HOH O 6 .   ? -22.502 -28.177 28.732 1.00 30.56  ? 363 HOH B O    1 
HETATM 6618 O  O    . HOH O 6 .   ? -22.697 -37.858 15.743 1.00 18.17  ? 364 HOH B O    1 
HETATM 6619 O  O    . HOH O 6 .   ? -39.012 -26.841 -1.874 1.00 21.19  ? 365 HOH B O    1 
HETATM 6620 O  O    . HOH O 6 .   ? -47.874 -24.726 2.191  1.00 31.39  ? 366 HOH B O    1 
HETATM 6621 O  O    . HOH O 6 .   ? -25.835 -16.838 28.293 1.00 17.37  ? 367 HOH B O    1 
HETATM 6622 O  O    . HOH O 6 .   ? -30.966 -10.253 12.843 1.00 24.04  ? 368 HOH B O    1 
HETATM 6623 O  O    . HOH O 6 .   ? -4.868  -25.682 11.430 1.00 31.20  ? 369 HOH B O    1 
HETATM 6624 O  O    . HOH O 6 .   ? -23.978 -27.706 14.205 1.00 18.08  ? 370 HOH B O    1 
HETATM 6625 O  O    . HOH O 6 .   ? -54.700 -23.156 29.447 1.00 14.97  ? 371 HOH B O    1 
HETATM 6626 O  O    . HOH O 6 .   ? -21.506 -21.929 26.824 1.00 15.94  ? 372 HOH B O    1 
HETATM 6627 O  O    . HOH O 6 .   ? -43.029 -34.731 24.334 1.00 36.57  ? 373 HOH B O    1 
HETATM 6628 O  O    . HOH O 6 .   ? -21.649 -37.459 22.416 1.00 24.51  ? 374 HOH B O    1 
HETATM 6629 O  O    . HOH O 6 .   ? -20.911 -35.362 8.092  1.00 15.22  ? 375 HOH B O    1 
HETATM 6630 O  O    . HOH O 6 .   ? -26.119 -35.544 20.988 1.00 21.96  ? 376 HOH B O    1 
HETATM 6631 O  O    . HOH O 6 .   ? -33.253 -15.303 0.045  1.00 32.51  ? 377 HOH B O    1 
HETATM 6632 O  O    . HOH O 6 .   ? -32.850 -19.047 5.090  1.00 15.52  ? 378 HOH B O    1 
HETATM 6633 O  O    . HOH O 6 .   ? -23.285 -36.826 8.088  1.00 16.93  ? 379 HOH B O    1 
HETATM 6634 O  O    . HOH O 6 .   ? -51.970 -16.844 20.719 1.00 29.66  ? 380 HOH B O    1 
HETATM 6635 O  O    . HOH O 6 .   ? -9.227  -25.794 10.397 1.00 17.21  ? 381 HOH B O    1 
HETATM 6636 O  O    . HOH O 6 .   ? -12.870 -16.494 -1.827 1.00 31.60  ? 382 HOH B O    1 
HETATM 6637 O  O    . HOH O 6 .   ? -41.778 -29.914 -1.732 1.00 24.72  ? 383 HOH B O    1 
HETATM 6638 O  O    . HOH O 6 .   ? -47.930 -22.091 31.037 1.00 24.94  ? 384 HOH B O    1 
HETATM 6639 O  O    . HOH O 6 .   ? -38.082 -30.204 32.073 1.00 36.35  ? 385 HOH B O    1 
HETATM 6640 O  O    . HOH O 6 .   ? -11.706 -21.008 22.604 1.00 11.25  ? 386 HOH B O    1 
HETATM 6641 O  O    . HOH O 6 .   ? -34.556 -37.034 11.616 1.00 15.69  ? 387 HOH B O    1 
HETATM 6642 O  O    . HOH O 6 .   ? -26.231 -11.998 11.691 1.00 21.14  ? 388 HOH B O    1 
HETATM 6643 O  O    . HOH O 6 .   ? -39.820 -19.259 5.090  1.00 16.33  ? 389 HOH B O    1 
HETATM 6644 O  O    . HOH O 6 .   ? -47.459 -9.539  28.588 1.00 32.58  ? 390 HOH B O    1 
HETATM 6645 O  O    . HOH O 6 .   ? -6.947  -29.356 8.819  1.00 31.94  ? 391 HOH B O    1 
HETATM 6646 O  O    . HOH O 6 .   ? -20.851 -39.687 10.094 1.00 30.89  ? 392 HOH B O    1 
HETATM 6647 O  O    . HOH O 6 .   ? -49.449 -24.894 4.214  1.00 35.74  ? 393 HOH B O    1 
HETATM 6648 O  O    . HOH O 6 .   ? -19.145 -19.114 -4.205 1.00 27.43  ? 394 HOH B O    1 
HETATM 6649 O  O    . HOH O 6 .   ? -39.356 -12.785 32.702 1.00 16.52  ? 395 HOH B O    1 
HETATM 6650 O  O    . HOH O 6 .   ? -15.433 -18.120 15.999 1.00 13.46  ? 396 HOH B O    1 
HETATM 6651 O  O    . HOH O 6 .   ? -16.508 -24.296 28.236 1.00 37.19  ? 397 HOH B O    1 
HETATM 6652 O  O    . HOH O 6 .   ? -44.416 -15.756 0.535  1.00 34.20  ? 398 HOH B O    1 
HETATM 6653 O  O    . HOH O 6 .   ? -42.541 -21.060 34.482 1.00 34.41  ? 399 HOH B O    1 
HETATM 6654 O  O    . HOH O 6 .   ? -26.808 -10.002 13.438 1.00 14.62  ? 400 HOH B O    1 
HETATM 6655 O  O    . HOH O 6 .   ? -23.763 -28.963 -1.379 1.00 26.98  ? 401 HOH B O    1 
HETATM 6656 O  O    . HOH O 6 .   ? -25.203 -20.550 26.675 1.00 15.59  ? 402 HOH B O    1 
HETATM 6657 O  O    . HOH O 6 .   ? -32.603 -37.097 25.632 1.00 20.14  ? 403 HOH B O    1 
HETATM 6658 O  O    . HOH O 6 .   ? -31.095 -20.790 25.582 1.00 12.91  ? 404 HOH B O    1 
HETATM 6659 O  O    . HOH O 6 .   ? -46.483 -15.558 31.854 1.00 27.53  ? 405 HOH B O    1 
HETATM 6660 O  O    . HOH O 6 .   ? -14.926 -23.949 1.956  1.00 33.60  ? 406 HOH B O    1 
HETATM 6661 O  O    . HOH O 6 .   ? -13.289 -20.327 8.510  1.00 13.75  ? 407 HOH B O    1 
HETATM 6662 O  O    . HOH O 6 .   ? -11.127 -28.079 24.916 1.00 17.16  ? 408 HOH B O    1 
HETATM 6663 O  O    . HOH O 6 .   ? -35.097 -27.830 31.545 1.00 30.43  ? 409 HOH B O    1 
HETATM 6664 O  O    . HOH O 6 .   ? -40.490 -12.021 25.233 1.00 20.13  ? 410 HOH B O    1 
HETATM 6665 O  O    . HOH O 6 .   ? -45.335 -29.026 30.926 1.00 31.36  ? 411 HOH B O    1 
HETATM 6666 O  O    . HOH O 6 .   ? -43.524 -8.758  30.729 1.00 16.43  ? 412 HOH B O    1 
HETATM 6667 O  O    . HOH O 6 .   ? -35.795 -31.962 32.487 1.00 31.93  ? 413 HOH B O    1 
HETATM 6668 O  O    . HOH O 6 .   ? -25.289 -21.716 -4.421 1.00 26.64  ? 414 HOH B O    1 
HETATM 6669 O  O    . HOH O 6 .   ? -44.049 -35.541 6.531  1.00 30.20  ? 415 HOH B O    1 
HETATM 6670 O  O    . HOH O 6 .   ? -12.767 -34.391 16.881 1.00 18.55  ? 416 HOH B O    1 
HETATM 6671 O  O    . HOH O 6 .   ? -43.998 -10.991 23.931 1.00 26.19  ? 417 HOH B O    1 
HETATM 6672 O  O    . HOH O 6 .   ? -21.569 -34.921 -0.924 1.00 37.14  ? 418 HOH B O    1 
HETATM 6673 O  O    . HOH O 6 .   ? -33.665 -37.440 28.435 1.00 25.45  ? 419 HOH B O    1 
HETATM 6674 O  O    . HOH O 6 .   ? -10.370 -27.111 8.330  1.00 16.63  ? 420 HOH B O    1 
HETATM 6675 O  O    . HOH O 6 .   ? -36.855 -38.204 6.355  1.00 18.02  ? 421 HOH B O    1 
HETATM 6676 O  O    . HOH O 6 .   ? -29.052 -16.319 11.273 1.00 20.11  ? 422 HOH B O    1 
HETATM 6677 O  O    . HOH O 6 .   ? -42.744 -16.135 14.100 1.00 27.60  ? 423 HOH B O    1 
HETATM 6678 O  O    . HOH O 6 .   ? -44.544 -15.546 17.075 1.00 27.78  ? 424 HOH B O    1 
HETATM 6679 O  O    . HOH O 6 .   ? -52.590 -25.079 20.539 1.00 29.81  ? 425 HOH B O    1 
HETATM 6680 O  O    . HOH O 6 .   ? -33.543 -25.766 30.908 1.00 25.21  ? 426 HOH B O    1 
HETATM 6681 O  O    . HOH O 6 .   ? -26.183 -15.560 13.972 1.00 12.62  ? 427 HOH B O    1 
HETATM 6682 O  O    . HOH O 6 .   ? -44.237 -29.040 11.909 1.00 18.67  ? 428 HOH B O    1 
HETATM 6683 O  O    . HOH O 6 .   ? -35.896 -15.026 14.873 1.00 20.14  ? 429 HOH B O    1 
HETATM 6684 O  O    . HOH O 6 .   ? -2.594  -24.583 14.516 1.00 16.69  ? 430 HOH B O    1 
HETATM 6685 O  O    . HOH O 6 .   ? -31.630 -21.443 4.633  1.00 14.98  ? 431 HOH B O    1 
HETATM 6686 O  O    . HOH O 6 .   ? -4.776  -27.677 14.661 1.00 23.02  ? 432 HOH B O    1 
HETATM 6687 O  O    . HOH O 6 .   ? -27.107 -14.078 3.900  1.00 28.36  ? 433 HOH B O    1 
HETATM 6688 O  O    . HOH O 6 .   ? -38.613 -21.051 -1.506 1.00 22.77  ? 434 HOH B O    1 
HETATM 6689 O  O    . HOH O 6 .   ? -7.472  -25.569 24.672 1.00 44.00  ? 435 HOH B O    1 
HETATM 6690 O  O    . HOH O 6 .   ? -32.881 -37.549 13.702 1.00 17.77  ? 436 HOH B O    1 
HETATM 6691 O  O    . HOH O 6 .   ? -25.605 -4.530  16.688 1.00 16.58  ? 437 HOH B O    1 
HETATM 6692 O  O    . HOH O 6 .   ? -26.777 -32.492 28.921 1.00 32.26  ? 438 HOH B O    1 
HETATM 6693 O  O    . HOH O 6 .   ? -10.396 -30.478 15.567 1.00 13.63  ? 439 HOH B O    1 
HETATM 6694 O  O    . HOH O 6 .   ? -17.475 -18.447 17.890 1.00 10.64  ? 440 HOH B O    1 
HETATM 6695 O  O    . HOH O 6 .   ? -45.561 -30.046 23.663 1.00 35.05  ? 441 HOH B O    1 
HETATM 6696 O  O    . HOH O 6 .   ? -46.132 -34.891 10.146 1.00 43.16  ? 442 HOH B O    1 
HETATM 6697 O  O    . HOH O 6 .   ? -21.822 -19.905 14.684 1.00 13.30  ? 443 HOH B O    1 
HETATM 6698 O  O    . HOH O 6 .   ? -46.593 -28.563 1.280  1.00 24.96  ? 444 HOH B O    1 
HETATM 6699 O  O    . HOH O 6 .   ? -36.095 -14.895 -1.484 1.00 42.10  ? 445 HOH B O    1 
HETATM 6700 O  O    . HOH O 6 .   ? -14.560 -22.133 -0.051 1.00 42.89  ? 446 HOH B O    1 
HETATM 6701 O  O    . HOH O 6 .   ? -16.278 -13.329 16.199 1.00 11.60  ? 447 HOH B O    1 
HETATM 6702 O  O    . HOH O 6 .   ? -43.305 -18.790 7.302  1.00 28.86  ? 448 HOH B O    1 
HETATM 6703 O  O    . HOH O 6 .   ? -31.873 -26.676 -4.998 1.00 53.97  ? 449 HOH B O    1 
HETATM 6704 O  O    . HOH O 6 .   ? -29.225 -32.090 29.847 1.00 21.40  ? 450 HOH B O    1 
HETATM 6705 O  O    . HOH O 6 .   ? -42.839 -34.293 4.065  1.00 20.84  ? 451 HOH B O    1 
HETATM 6706 O  O    . HOH O 6 .   ? -30.933 -9.849  27.339 1.00 19.36  ? 452 HOH B O    1 
HETATM 6707 O  O    . HOH O 6 .   ? -42.655 -17.470 9.375  1.00 34.05  ? 453 HOH B O    1 
HETATM 6708 O  O    . HOH O 6 .   ? -23.895 -36.190 23.985 1.00 31.61  ? 454 HOH B O    1 
HETATM 6709 O  O    . HOH O 6 .   ? -12.647 -31.554 22.826 1.00 21.63  ? 455 HOH B O    1 
HETATM 6710 O  O    . HOH O 6 .   ? -15.698 -18.995 26.980 1.00 13.04  ? 456 HOH B O    1 
HETATM 6711 O  O    . HOH O 6 .   ? -40.148 -24.089 32.499 1.00 34.30  ? 457 HOH B O    1 
HETATM 6712 O  O    . HOH O 6 .   ? -42.865 -25.966 -1.020 1.00 29.31  ? 458 HOH B O    1 
HETATM 6713 O  O    . HOH O 6 .   ? -52.943 -22.752 15.765 1.00 27.73  ? 459 HOH B O    1 
HETATM 6714 O  O    . HOH O 6 .   ? -32.589 -21.583 -4.483 1.00 30.82  ? 460 HOH B O    1 
HETATM 6715 O  O    . HOH O 6 .   ? -31.655 -15.551 33.024 1.00 40.06  ? 461 HOH B O    1 
HETATM 6716 O  O    . HOH O 6 .   ? -13.724 -20.620 26.032 1.00 21.57  ? 462 HOH B O    1 
HETATM 6717 O  O    . HOH O 6 .   ? -12.782 -26.686 7.257  1.00 18.05  ? 463 HOH B O    1 
HETATM 6718 O  O    . HOH O 6 .   ? -37.913 -5.305  22.643 1.00 24.61  ? 464 HOH B O    1 
HETATM 6719 O  O    . HOH O 6 .   ? -12.099 -20.457 10.972 1.00 12.58  ? 465 HOH B O    1 
HETATM 6720 O  O    . HOH O 6 .   ? -41.741 -35.168 11.311 1.00 25.20  ? 466 HOH B O    1 
HETATM 6721 O  O    . HOH O 6 .   ? -13.494 -26.821 5.161  1.00 21.21  ? 467 HOH B O    1 
HETATM 6722 O  O    . HOH O 6 .   ? -44.166 -34.884 20.691 1.00 30.83  ? 468 HOH B O    1 
HETATM 6723 O  O    . HOH O 6 .   ? -41.568 -14.224 23.397 1.00 20.37  ? 469 HOH B O    1 
HETATM 6724 O  O    . HOH O 6 .   ? -41.958 -8.906  18.089 1.00 28.83  ? 470 HOH B O    1 
HETATM 6725 O  O    . HOH O 6 .   ? -51.094 -29.179 18.658 1.00 32.27  ? 471 HOH B O    1 
HETATM 6726 O  O    . HOH O 6 .   ? -12.611 -36.372 14.938 1.00 20.51  ? 472 HOH B O    1 
HETATM 6727 O  O    . HOH O 6 .   ? -46.485 -11.716 31.914 1.00 28.34  ? 473 HOH B O    1 
HETATM 6728 O  O    . HOH O 6 .   ? -54.097 -19.009 23.494 1.00 27.16  ? 474 HOH B O    1 
HETATM 6729 O  O    . HOH O 6 .   ? -35.121 -13.867 5.543  1.00 36.87  ? 475 HOH B O    1 
HETATM 6730 O  O    . HOH O 6 .   ? -47.477 -18.409 26.538 1.00 24.76  ? 476 HOH B O    1 
HETATM 6731 O  O    . HOH O 6 .   ? -37.625 -17.060 -0.513 1.00 27.35  ? 477 HOH B O    1 
HETATM 6732 O  O    . HOH O 6 .   ? -13.887 -37.207 10.355 1.00 25.62  ? 478 HOH B O    1 
HETATM 6733 O  O    . HOH O 6 .   ? -38.129 -12.064 12.075 1.00 29.07  ? 479 HOH B O    1 
HETATM 6734 O  O    . HOH O 6 .   ? -20.577 -27.223 -1.263 1.00 41.17  ? 480 HOH B O    1 
HETATM 6735 O  O    . HOH O 6 .   ? -40.866 -19.636 -2.160 1.00 36.64  ? 481 HOH B O    1 
HETATM 6736 O  O    . HOH O 6 .   ? -34.469 -27.872 -1.335 1.00 18.43  ? 482 HOH B O    1 
HETATM 6737 O  O    . HOH O 6 .   ? -32.381 -28.895 -2.892 1.00 28.42  ? 483 HOH B O    1 
HETATM 6738 O  O    . HOH O 6 .   ? -18.994 -36.197 10.071 1.00 17.64  ? 484 HOH B O    1 
HETATM 6739 O  O    . HOH O 6 .   ? -18.115 -33.305 -2.341 1.00 46.46  ? 485 HOH B O    1 
HETATM 6740 O  O    . HOH O 6 .   ? -29.412 -40.738 6.496  1.00 42.73  ? 486 HOH B O    1 
HETATM 6741 O  O    . HOH O 6 .   ? -25.989 -28.370 -2.847 1.00 38.17  ? 487 HOH B O    1 
HETATM 6742 O  O    . HOH O 6 .   ? -25.900 -16.810 4.985  1.00 32.58  ? 488 HOH B O    1 
HETATM 6743 O  O    . HOH O 6 .   ? -39.053 -38.474 8.091  1.00 21.35  ? 489 HOH B O    1 
HETATM 6744 O  O    . HOH O 6 .   ? -26.948 -19.021 9.032  1.00 18.80  ? 490 HOH B O    1 
HETATM 6745 O  O    . HOH O 6 .   ? -28.816 -18.638 9.896  1.00 18.39  ? 491 HOH B O    1 
HETATM 6746 O  O    . HOH O 6 .   ? -25.125 -19.421 29.111 1.00 32.19  ? 492 HOH B O    1 
HETATM 6747 O  O    . HOH O 6 .   ? -46.740 -29.519 -1.715 1.00 32.07  ? 493 HOH B O    1 
HETATM 6748 O  O    . HOH O 6 .   ? -16.594 -20.795 29.356 1.00 39.74  ? 494 HOH B O    1 
HETATM 6749 O  O    . HOH O 6 .   ? -24.284 -13.798 9.983  1.00 31.36  ? 495 HOH B O    1 
HETATM 6750 O  O    . HOH O 6 .   ? -44.562 -11.195 20.310 1.00 38.60  ? 496 HOH B O    1 
HETATM 6751 O  O    . HOH O 6 .   ? -26.011 -30.355 28.939 1.00 39.93  ? 497 HOH B O    1 
HETATM 6752 O  O    . HOH O 6 .   ? -46.169 -19.697 8.414  1.00 41.52  ? 498 HOH B O    1 
HETATM 6753 O  O    . HOH O 6 .   ? -36.681 -35.836 12.866 1.00 18.44  ? 499 HOH B O    1 
HETATM 6754 O  O    . HOH O 6 .   ? -14.940 -36.786 8.142  1.00 37.16  ? 500 HOH B O    1 
HETATM 6755 O  O    . HOH O 6 .   ? -22.859 -11.331 1.896  1.00 33.90  ? 501 HOH B O    1 
HETATM 6756 O  O    . HOH O 6 .   ? -27.774 -39.965 8.242  1.00 37.28  ? 502 HOH B O    1 
HETATM 6757 O  O    . HOH O 6 .   ? -23.779 -36.379 26.563 1.00 33.53  ? 503 HOH B O    1 
HETATM 6758 O  O    . HOH O 6 .   ? -39.583 -34.455 15.307 1.00 27.68  ? 504 HOH B O    1 
HETATM 6759 O  O    . HOH O 6 .   ? -30.982 -36.182 30.623 1.00 32.94  ? 505 HOH B O    1 
HETATM 6760 O  O    . HOH O 6 .   ? -37.921 -16.892 14.555 1.00 23.98  ? 506 HOH B O    1 
HETATM 6761 O  O    . HOH O 6 .   ? -46.885 -26.418 32.180 1.00 48.12  ? 507 HOH B O    1 
HETATM 6762 O  O    . HOH O 6 .   ? -8.578  -27.480 24.227 1.00 27.89  ? 508 HOH B O    1 
HETATM 6763 O  O    . HOH O 6 .   ? -32.683 -14.886 2.939  1.00 44.76  ? 509 HOH B O    1 
HETATM 6764 O  O    . HOH O 6 .   ? -48.584 -28.886 26.233 1.00 28.39  ? 510 HOH B O    1 
HETATM 6765 O  O    . HOH O 6 .   ? -41.186 -25.865 34.703 1.00 46.23  ? 511 HOH B O    1 
HETATM 6766 O  O    . HOH O 6 .   ? -28.164 -9.862  32.948 1.00 40.98  ? 512 HOH B O    1 
HETATM 6767 O  O    . HOH O 6 .   ? -40.220 -11.724 16.065 1.00 39.08  ? 513 HOH B O    1 
HETATM 6768 O  O    . HOH O 6 .   ? -27.201 -42.376 2.308  1.00 27.08  ? 514 HOH B O    1 
HETATM 6769 O  O    . HOH O 6 .   ? -9.713  -21.553 11.551 1.00 18.23  ? 515 HOH B O    1 
HETATM 6770 O  O    . HOH O 6 .   ? -28.674 -43.026 4.866  1.00 33.31  ? 516 HOH B O    1 
HETATM 6771 O  O    . HOH O 6 .   ? -7.830  -31.121 19.458 1.00 36.37  ? 517 HOH B O    1 
HETATM 6772 O  O    . HOH O 6 .   ? -52.981 -18.832 21.175 1.00 33.15  ? 518 HOH B O    1 
HETATM 6773 O  O    . HOH O 6 .   ? -54.403 -20.311 19.492 1.00 29.96  ? 519 HOH B O    1 
HETATM 6774 O  O    . HOH O 6 .   ? -45.904 -31.610 21.455 1.00 37.99  ? 520 HOH B O    1 
HETATM 6775 O  O    . HOH O 6 .   ? -46.623 -21.795 33.444 1.00 35.36  ? 521 HOH B O    1 
HETATM 6776 O  O    . HOH O 6 .   ? -22.620 -21.677 29.442 1.00 39.06  ? 522 HOH B O    1 
HETATM 6777 O  O    . HOH O 6 .   ? -24.830 -16.082 11.531 1.00 15.35  ? 523 HOH B O    1 
HETATM 6778 O  O    . HOH O 6 .   ? -55.776 -23.214 18.190 1.00 33.77  ? 524 HOH B O    1 
HETATM 6779 O  O    . HOH O 6 .   ? -16.649 -37.562 9.419  1.00 39.84  ? 525 HOH B O    1 
HETATM 6780 O  O    . HOH O 6 .   ? -50.917 -30.534 12.353 1.00 40.04  ? 526 HOH B O    1 
HETATM 6781 O  O    . HOH O 6 .   ? -18.802 -32.568 29.413 1.00 37.47  ? 527 HOH B O    1 
HETATM 6782 O  O    . HOH O 6 .   ? -38.403 -21.238 33.136 1.00 34.76  ? 528 HOH B O    1 
HETATM 6783 O  O    . HOH O 6 .   ? -34.858 -39.022 7.768  1.00 23.87  ? 529 HOH B O    1 
HETATM 6784 O  O    . HOH O 6 .   ? -33.484 -32.449 -0.519 1.00 37.00  ? 530 HOH B O    1 
HETATM 6785 O  O    . HOH O 6 .   ? -7.143  -28.153 13.509 1.00 27.07  ? 531 HOH B O    1 
HETATM 6786 O  O    . HOH O 6 .   ? -24.363 -28.779 16.607 1.00 17.72  ? 532 HOH B O    1 
HETATM 6787 O  O    . HOH O 6 .   ? -45.946 -9.226  31.694 1.00 31.42  ? 533 HOH B O    1 
HETATM 6788 O  O    . HOH O 6 .   ? -55.515 -25.190 13.761 1.00 45.63  ? 534 HOH B O    1 
HETATM 6789 O  O    . HOH O 6 .   ? -46.212 -30.760 11.085 1.00 30.61  ? 535 HOH B O    1 
HETATM 6790 O  O    . HOH O 6 .   ? -23.850 -31.541 -2.811 1.00 37.70  ? 536 HOH B O    1 
HETATM 6791 O  O    . HOH O 6 .   ? -48.197 -31.213 1.958  1.00 36.90  ? 537 HOH B O    1 
HETATM 6792 O  O    . HOH O 6 .   ? -40.351 -13.619 8.945  1.00 42.43  ? 538 HOH B O    1 
HETATM 6793 O  O    . HOH O 6 .   ? -29.243 -34.373 31.528 1.00 40.56  ? 539 HOH B O    1 
HETATM 6794 O  O    . HOH O 6 .   ? -39.065 -24.036 -1.899 1.00 27.28  ? 540 HOH B O    1 
HETATM 6795 O  O    . HOH O 6 .   ? -13.649 -22.793 27.750 1.00 33.89  ? 541 HOH B O    1 
HETATM 6796 O  O    . HOH O 6 .   ? -41.469 -27.598 -2.856 1.00 28.63  ? 542 HOH B O    1 
HETATM 6797 O  O    . HOH O 6 .   ? -40.530 -4.788  22.878 1.00 35.17  ? 543 HOH B O    1 
HETATM 6798 O  O    . HOH O 6 .   ? -47.350 -30.862 25.704 1.00 35.42  ? 544 HOH B O    1 
HETATM 6799 O  O    . HOH O 6 .   ? -13.440 -28.856 29.091 1.00 39.53  ? 545 HOH B O    1 
HETATM 6800 O  O    . HOH O 6 .   ? -22.658 -26.571 -2.591 1.00 50.73  ? 546 HOH B O    1 
HETATM 6801 O  O    . HOH O 6 .   ? -11.136 -20.089 25.138 1.00 21.51  ? 547 HOH B O    1 
HETATM 6802 O  O    . HOH O 6 .   ? -26.639 -40.857 14.163 1.00 35.00  ? 548 HOH B O    1 
HETATM 6803 O  O    . HOH O 6 .   ? -44.805 -17.343 9.233  1.00 37.92  ? 549 HOH B O    1 
HETATM 6804 O  O    . HOH O 6 .   ? -10.884 -32.179 3.562  1.00 49.04  ? 550 HOH B O    1 
HETATM 6805 O  O    . HOH O 6 .   ? -25.230 -13.798 8.064  1.00 50.06  ? 551 HOH B O    1 
HETATM 6806 O  O    . HOH O 6 .   ? -46.619 -10.795 24.529 1.00 37.43  ? 552 HOH B O    1 
HETATM 6807 O  O    . HOH O 6 .   ? -34.495 -38.673 15.793 1.00 29.54  ? 553 HOH B O    1 
HETATM 6808 O  O    . HOH O 6 .   ? -29.785 -30.014 31.532 1.00 32.71  ? 554 HOH B O    1 
HETATM 6809 O  O    . HOH O 6 .   ? -38.339 -39.468 10.297 1.00 36.07  ? 555 HOH B O    1 
HETATM 6810 O  O    . HOH O 6 .   ? -23.948 -40.981 15.068 1.00 48.24  ? 556 HOH B O    1 
HETATM 6811 O  O    . HOH O 6 .   ? -36.662 -27.660 -3.016 1.00 22.70  ? 557 HOH B O    1 
HETATM 6812 O  O    . HOH O 6 .   ? -27.419 -28.803 30.331 1.00 30.75  ? 558 HOH B O    1 
HETATM 6813 O  O    . HOH O 6 .   ? -38.680 -37.765 12.898 1.00 37.58  ? 559 HOH B O    1 
HETATM 6814 O  O    . HOH O 6 .   ? -39.969 -15.750 13.428 1.00 24.80  ? 560 HOH B O    1 
HETATM 6815 O  O    . HOH O 6 .   ? -51.208 -29.444 10.114 1.00 35.29  ? 561 HOH B O    1 
HETATM 6816 O  O    . HOH O 6 .   ? -41.007 -33.353 30.108 1.00 27.18  ? 562 HOH B O    1 
HETATM 6817 O  O    . HOH O 6 .   ? -43.515 -33.046 26.393 1.00 27.91  ? 563 HOH B O    1 
HETATM 6818 O  O    . HOH O 6 .   ? -41.898 -34.710 14.131 1.00 32.96  ? 564 HOH B O    1 
HETATM 6819 O  O    . HOH O 6 .   ? -7.028  -27.572 10.865 1.00 24.75  ? 565 HOH B O    1 
HETATM 6820 O  O    . HOH O 6 .   ? -49.786 -29.723 23.613 1.00 40.65  ? 566 HOH B O    1 
HETATM 6821 O  O    . HOH O 6 .   ? -14.708 -28.649 3.305  1.00 27.40  ? 567 HOH B O    1 
HETATM 6822 O  O    . HOH O 6 .   ? -38.518 -33.587 -0.665 1.00 25.08  ? 568 HOH B O    1 
HETATM 6823 O  O    . HOH O 6 .   ? -35.435 -39.340 10.516 1.00 25.62  ? 569 HOH B O    1 
HETATM 6824 O  O    . HOH O 6 .   ? -24.872 -10.472 9.935  1.00 42.75  ? 570 HOH B O    1 
HETATM 6825 O  O    . HOH O 6 .   ? -6.273  -31.526 16.756 1.00 26.29  ? 571 HOH B O    1 
HETATM 6826 O  O    . HOH O 6 .   ? -34.895 -30.208 0.088  1.00 21.14  ? 572 HOH B O    1 
HETATM 6827 O  O    . HOH O 6 .   ? -23.102 -11.626 9.196  1.00 28.68  ? 573 HOH B O    1 
HETATM 6828 O  O    . HOH O 6 .   ? -21.202 -36.490 27.927 1.00 34.35  ? 574 HOH B O    1 
HETATM 6829 O  O    . HOH O 6 .   ? -8.845  -34.459 14.976 1.00 35.63  ? 575 HOH B O    1 
HETATM 6830 O  O    . HOH O 6 .   ? -11.527 -27.446 27.570 1.00 33.41  ? 576 HOH B O    1 
HETATM 6831 O  O    . HOH O 6 .   ? -18.778 -38.742 9.871  1.00 34.00  ? 577 HOH B O    1 
HETATM 6832 O  O    . HOH O 6 .   ? -55.706 -23.695 15.556 1.00 39.21  ? 578 HOH B O    1 
HETATM 6833 O  O    . HOH O 6 .   ? -22.576 -39.491 8.204  1.00 24.33  ? 579 HOH B O    1 
HETATM 6834 O  O    . HOH O 6 .   ? -47.326 -30.729 8.635  1.00 29.51  ? 580 HOH B O    1 
HETATM 6835 O  O    . HOH O 6 .   ? -26.519 -37.530 23.077 1.00 36.23  ? 581 HOH B O    1 
HETATM 6836 O  O    . HOH O 6 .   ? -9.995  -36.846 15.053 1.00 42.31  ? 582 HOH B O    1 
HETATM 6837 O  O    . HOH O 6 .   ? -29.350 -25.931 32.345 1.00 34.67  ? 583 HOH B O    1 
HETATM 6838 O  O    . HOH O 6 .   ? -10.603 -30.833 24.407 1.00 21.11  ? 584 HOH B O    1 
HETATM 6839 O  O    . HOH O 6 .   ? -36.303 -37.227 17.312 1.00 29.90  ? 585 HOH B O    1 
HETATM 6840 O  O    . HOH O 6 .   ? -14.398 -39.198 12.149 1.00 23.44  ? 586 HOH B O    1 
HETATM 6841 O  O    . HOH O 6 .   ? -21.853 -29.212 31.483 1.00 47.72  ? 587 HOH B O    1 
HETATM 6842 O  O    . HOH O 6 .   ? -35.882 -38.159 19.778 1.00 39.02  ? 588 HOH B O    1 
HETATM 6843 O  O    . HOH O 6 .   ? -37.352 -30.338 -3.457 1.00 34.72  ? 589 HOH B O    1 
HETATM 6844 O  O    . HOH O 6 .   ? -45.521 -25.627 -1.538 1.00 30.36  ? 590 HOH B O    1 
HETATM 6845 O  O    . HOH O 6 .   ? -20.222 -36.279 5.599  1.00 32.56  ? 591 HOH B O    1 
HETATM 6846 O  O    . HOH O 6 .   ? -51.094 -28.357 26.970 1.00 28.58  ? 592 HOH B O    1 
HETATM 6847 O  O    . HOH O 6 .   ? -24.155 -24.395 -3.874 1.00 37.38  ? 593 HOH B O    1 
HETATM 6848 O  O    . HOH O 6 .   ? -7.807  -30.515 14.817 1.00 22.38  ? 594 HOH B O    1 
HETATM 6849 O  O    . HOH O 6 .   ? -22.832 -38.843 20.310 1.00 27.89  ? 595 HOH B O    1 
HETATM 6850 O  O    . HOH O 6 .   ? -26.898 -15.060 6.416  1.00 37.88  ? 596 HOH B O    1 
HETATM 6851 O  O    . HOH O 6 .   ? -28.094 -14.054 11.184 1.00 26.09  ? 597 HOH B O    1 
HETATM 6852 O  O    . HOH O 6 .   ? -20.330 -31.624 30.990 1.00 34.35  ? 598 HOH B O    1 
HETATM 6853 O  O    . HOH O 6 .   ? -10.291 -15.269 -1.165 1.00 43.08  ? 599 HOH B O    1 
HETATM 6854 O  O    . HOH O 6 .   ? -45.973 -32.854 27.108 1.00 33.90  ? 600 HOH B O    1 
HETATM 6855 O  O    . HOH O 6 .   ? -2.698  -30.334 18.070 1.00 35.55  ? 601 HOH B O    1 
HETATM 6856 O  O    . HOH O 6 .   ? -24.504 -17.765 9.125  1.00 18.13  ? 602 HOH B O    1 
HETATM 6857 O  O    . HOH O 6 .   ? -56.160 -20.346 15.112 1.00 40.74  ? 603 HOH B O    1 
HETATM 6858 O  O    . HOH O 6 .   ? -27.507 -16.662 9.477  1.00 26.57  ? 604 HOH B O    1 
HETATM 6859 O  O    . HOH O 6 .   ? -55.399 -15.793 18.922 1.00 43.23  ? 605 HOH B O    1 
HETATM 6860 O  O    . HOH O 6 .   ? -5.744  -22.662 10.164 1.00 29.96  ? 606 HOH B O    1 
HETATM 6861 O  O    . HOH O 6 .   ? -27.599 -7.786  12.045 1.00 27.09  ? 607 HOH B O    1 
HETATM 6862 O  O    . HOH O 6 .   ? -20.300 -42.358 10.521 1.00 27.38  ? 608 HOH B O    1 
HETATM 6863 O  O    . HOH O 6 .   ? -39.720 -13.085 14.117 1.00 43.81  ? 609 HOH B O    1 
HETATM 6864 O  O    . HOH O 6 .   ? -14.429 -15.083 -3.079 1.00 39.10  ? 610 HOH B O    1 
HETATM 6865 O  O    . HOH O 6 .   ? -49.977 -9.552  29.209 1.00 35.72  ? 611 HOH B O    1 
HETATM 6866 O  O    . HOH O 6 .   ? -28.725 -37.299 18.215 1.00 20.10  ? 612 HOH B O    1 
HETATM 6867 O  O    . HOH O 6 .   ? -10.184 -30.953 18.335 1.00 18.88  ? 613 HOH B O    1 
HETATM 6868 O  O    . HOH O 6 .   ? -8.585  -23.315 9.756  1.00 22.67  ? 614 HOH B O    1 
HETATM 6869 O  O    . HOH O 6 .   ? -43.346 -37.952 7.934  1.00 42.91  ? 615 HOH B O    1 
HETATM 6870 O  O    . HOH O 6 .   ? -23.753 -20.392 -6.269 1.00 34.71  ? 616 HOH B O    1 
HETATM 6871 O  O    . HOH O 6 .   ? -30.824 -39.311 13.781 1.00 23.57  ? 617 HOH B O    1 
HETATM 6872 O  O    . HOH O 6 .   ? -27.053 -11.791 2.394  1.00 36.23  ? 618 HOH B O    1 
HETATM 6873 O  O    . HOH O 6 .   ? -10.378 -23.420 28.050 1.00 41.66  ? 619 HOH B O    1 
HETATM 6874 O  O    . HOH O 6 .   ? -1.369  -23.525 12.362 1.00 27.79  ? 620 HOH B O    1 
HETATM 6875 O  O    . HOH O 6 .   ? -37.149 -27.247 32.893 1.00 47.79  ? 621 HOH B O    1 
HETATM 6876 O  O    . HOH O 6 .   ? -34.304 -34.321 33.573 1.00 33.40  ? 622 HOH B O    1 
HETATM 6877 O  O    . HOH O 6 .   ? -9.608  -22.659 7.348  1.00 27.25  ? 623 HOH B O    1 
HETATM 6878 O  O    . HOH O 6 .   ? -50.927 -27.451 4.093  1.00 44.92  ? 624 HOH B O    1 
HETATM 6879 O  O    . HOH O 6 .   ? -11.766 -29.803 28.247 1.00 52.41  ? 625 HOH B O    1 
HETATM 6880 O  O    . HOH O 6 .   ? -49.343 -28.944 8.087  1.00 31.31  ? 626 HOH B O    1 
HETATM 6881 O  O    . HOH O 6 .   ? -43.610 -9.062  21.875 1.00 34.49  ? 627 HOH B O    1 
HETATM 6882 O  O    . HOH O 6 .   ? -26.577 -42.289 9.603  1.00 44.49  ? 628 HOH B O    1 
HETATM 6883 O  O    . HOH O 6 .   ? -30.333 -38.799 16.700 1.00 29.59  ? 629 HOH B O    1 
HETATM 6884 O  O    . HOH O 6 .   ? -36.657 -26.323 -5.460 1.00 29.71  ? 630 HOH B O    1 
HETATM 6885 O  O    . HOH O 6 .   ? -34.862 -25.231 -6.667 1.00 42.04  ? 631 HOH B O    1 
HETATM 6886 O  O    . HOH O 6 .   ? -37.632 -24.752 31.792 1.00 37.86  ? 632 HOH B O    1 
HETATM 6887 O  O    . HOH O 6 .   ? -32.715 -39.462 17.543 1.00 33.49  ? 633 HOH B O    1 
HETATM 6888 O  O    . HOH O 6 .   ? -45.000 -5.519  22.983 1.00 46.12  ? 634 HOH B O    1 
HETATM 6889 O  O    . HOH O 6 .   ? -28.838 -40.964 16.694 1.00 45.64  ? 635 HOH B O    1 
HETATM 6890 O  O    . HOH O 6 .   ? -48.982 -31.624 12.139 1.00 37.13  ? 636 HOH B O    1 
HETATM 6891 O  O    . HOH O 6 .   ? -35.676 -23.702 30.131 1.00 37.19  ? 637 HOH B O    1 
HETATM 6892 O  O    . HOH O 6 .   ? -27.705 -13.876 9.112  1.00 29.09  ? 638 HOH B O    1 
HETATM 6893 O  O    . HOH O 6 .   ? -28.698 -11.100 8.879  1.00 43.54  ? 639 HOH B O    1 
HETATM 6894 O  O    . HOH O 6 .   ? -50.578 -29.544 5.763  1.00 45.75  ? 640 HOH B O    1 
HETATM 6895 O  O    . HOH O 6 .   ? -38.374 -24.124 -5.111 1.00 39.00  ? 641 HOH B O    1 
HETATM 6896 O  O    . HOH O 6 .   ? -37.198 -21.560 -5.411 1.00 40.47  ? 642 HOH B O    1 
HETATM 6897 O  O    . HOH O 6 .   ? 0.194   -25.423 11.046 1.00 45.24  ? 643 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   . MET A 1   ? 0.2555 0.2825 0.3518 -0.0298 0.1067  0.0002  1   MET A N   
2    C  CA  . MET A 1   ? 0.2150 0.2312 0.3384 0.0039  0.0775  0.0139  1   MET A CA  
3    C  C   . MET A 1   ? 0.1758 0.2490 0.2512 0.0145  0.0572  0.0641  1   MET A C   
4    O  O   . MET A 1   ? 0.2955 0.2763 0.2186 0.1104  0.0767  0.0636  1   MET A O   
5    C  CB  . MET A 1   ? 0.2277 0.2365 0.2416 0.0074  0.0676  0.0482  1   MET A CB  
6    C  CG  . MET A 1   ? 0.2494 0.2422 0.3338 0.0344  0.0903  0.0552  1   MET A CG  
7    S  SD  . MET A 1   ? 0.2463 0.3259 0.2990 0.0209  0.0610  0.1012  1   MET A SD  
8    C  CE  . MET A 1   ? 0.2450 0.2379 0.3001 -0.0770 0.0324  0.0631  1   MET A CE  
19   N  N   . ASN A 2   ? 0.2497 0.3244 0.2449 0.0072  0.0122  0.0696  2   ASN A N   
20   C  CA  . ASN A 2   ? 0.2472 0.3027 0.2331 -0.0164 -0.0172 0.0105  2   ASN A CA  
21   C  C   . ASN A 2   ? 0.2432 0.1964 0.2670 -0.0185 0.0079  0.0146  2   ASN A C   
22   O  O   . ASN A 2   ? 0.2767 0.2117 0.3224 0.0220  -0.0293 -0.0003 2   ASN A O   
23   C  CB  . ASN A 2   ? 0.2501 0.3728 0.2115 -0.0473 -0.0038 0.0165  2   ASN A CB  
24   C  CG  . ASN A 2   ? 0.2311 0.3592 0.1959 -0.0823 0.0097  0.0131  2   ASN A CG  
25   O  OD1 . ASN A 2   ? 0.2470 0.5209 0.2658 -0.1366 -0.0324 0.0516  2   ASN A OD1 
26   N  ND2 . ASN A 2   ? 0.2465 0.5281 0.2521 -0.0488 -0.0332 -0.0268 2   ASN A ND2 
33   N  N   . THR A 3   ? 0.2554 0.1647 0.1766 -0.0259 -0.0134 0.0493  3   THR A N   
34   C  CA  . THR A 3   ? 0.2241 0.1507 0.1379 -0.0237 -0.0059 0.0227  3   THR A CA  
35   C  C   . THR A 3   ? 0.2022 0.1226 0.1331 -0.0228 -0.0173 0.0164  3   THR A C   
36   O  O   . THR A 3   ? 0.1994 0.1801 0.1588 -0.0325 -0.0361 0.0453  3   THR A O   
37   C  CB  . THR A 3   ? 0.2559 0.1426 0.1551 -0.0060 -0.0176 0.0349  3   THR A CB  
38   O  OG1 . THR A 3   ? 0.3529 0.1344 0.2189 0.0274  -0.0301 0.0088  3   THR A OG1 
39   C  CG2 . THR A 3   ? 0.2470 0.2017 0.2004 0.0152  -0.0010 0.0679  3   THR A CG2 
47   N  N   . ARG A 4   ? 0.1592 0.1272 0.1251 -0.0103 0.0042  0.0197  4   ARG A N   
48   C  CA  . ARG A 4   ? 0.1429 0.1114 0.1181 -0.0126 0.0025  0.0074  4   ARG A CA  
49   C  C   . ARG A 4   ? 0.1343 0.1007 0.1156 -0.0106 0.0060  0.0029  4   ARG A C   
50   O  O   . ARG A 4   ? 0.1343 0.1124 0.1186 -0.0050 0.0094  0.0032  4   ARG A O   
51   C  CB  . ARG A 4   ? 0.1620 0.1046 0.1315 -0.0027 -0.0101 -0.0019 4   ARG A CB  
52   C  CG  . ARG A 4   ? 0.1899 0.1043 0.1316 0.0103  -0.0227 -0.0043 4   ARG A CG  
53   C  CD  . ARG A 4   ? 0.2249 0.1082 0.1928 -0.0057 -0.0051 0.0153  4   ARG A CD  
54   N  NE  . ARG A 4   ? 0.1773 0.1596 0.1622 0.0253  -0.0317 -0.0214 4   ARG A NE  
55   C  CZ  . ARG A 4   ? 0.1331 0.1191 0.1451 0.0176  -0.0259 -0.0348 4   ARG A CZ  
56   N  NH1 . ARG A 4   ? 0.1635 0.1213 0.1505 -0.0115 -0.0082 -0.0010 4   ARG A NH1 
57   N  NH2 . ARG A 4   ? 0.1353 0.1213 0.1685 -0.0134 -0.0094 -0.0123 4   ARG A NH2 
71   N  N   . VAL A 5   ? 0.1393 0.1029 0.1291 -0.0187 0.0173  -0.0004 5   VAL A N   
72   C  CA  . VAL A 5   ? 0.1370 0.1168 0.1331 -0.0126 0.0162  -0.0094 5   VAL A CA  
73   C  C   . VAL A 5   ? 0.1344 0.1023 0.1318 -0.0042 0.0218  -0.0057 5   VAL A C   
74   O  O   . VAL A 5   ? 0.1485 0.1139 0.1252 -0.0102 0.0129  -0.0048 5   VAL A O   
75   C  CB  . VAL A 5   ? 0.1408 0.1479 0.1523 -0.0235 0.0223  -0.0205 5   VAL A CB  
76   C  CG1 . VAL A 5   ? 0.1468 0.1584 0.1820 -0.0027 0.0153  -0.0320 5   VAL A CG1 
77   C  CG2 . VAL A 5   ? 0.1431 0.1684 0.1643 -0.0257 0.0235  -0.0280 5   VAL A CG2 
87   N  N   . PHE A 6   ? 0.1507 0.1023 0.1286 -0.0043 0.0073  -0.0071 6   PHE A N   
88   C  CA  . PHE A 6   ? 0.1559 0.1010 0.1308 -0.0068 0.0052  -0.0035 6   PHE A CA  
89   C  C   . PHE A 6   ? 0.1606 0.1065 0.1437 -0.0148 0.0005  0.0029  6   PHE A C   
90   O  O   . PHE A 6   ? 0.1845 0.1095 0.1430 0.0048  0.0006  -0.0060 6   PHE A O   
91   C  CB  . PHE A 6   ? 0.1608 0.1088 0.1503 -0.0047 0.0096  0.0037  6   PHE A CB  
92   C  CG  . PHE A 6   ? 0.1380 0.1156 0.1523 -0.0125 0.0163  0.0042  6   PHE A CG  
93   C  CD1 . PHE A 6   ? 0.1473 0.1181 0.1424 -0.0111 0.0212  0.0088  6   PHE A CD1 
94   C  CD2 . PHE A 6   ? 0.1768 0.1281 0.1583 -0.0178 0.0126  0.0041  6   PHE A CD2 
95   C  CE1 . PHE A 6   ? 0.1625 0.1251 0.1722 -0.0047 0.0144  0.0094  6   PHE A CE1 
96   C  CE2 . PHE A 6   ? 0.1763 0.1551 0.1632 -0.0181 -0.0017 0.0159  6   PHE A CE2 
97   C  CZ  . PHE A 6   ? 0.1813 0.1377 0.1867 -0.0035 0.0131  0.0250  6   PHE A CZ  
107  N  N   . THR A 7   ? 0.1653 0.1022 0.1293 -0.0104 0.0129  -0.0011 7   THR A N   
108  C  CA  . THR A 7   ? 0.1649 0.0997 0.1453 -0.0029 0.0111  -0.0031 7   THR A CA  
109  C  C   . THR A 7   ? 0.1624 0.0983 0.1352 -0.0097 0.0147  -0.0075 7   THR A C   
110  O  O   . THR A 7   ? 0.2305 0.1194 0.1511 -0.0523 -0.0059 0.0052  7   THR A O   
111  C  CB  . THR A 7   ? 0.1659 0.1123 0.1693 -0.0177 0.0332  -0.0076 7   THR A CB  
112  O  OG1 . THR A 7   ? 0.1584 0.1255 0.2253 -0.0097 0.0074  0.0155  7   THR A OG1 
113  C  CG2 . THR A 7   ? 0.1829 0.1283 0.2263 0.0102  0.0524  -0.0169 7   THR A CG2 
121  N  N   . PHE A 8   ? 0.1461 0.1010 0.1404 -0.0078 0.0170  0.0001  8   PHE A N   
122  C  CA  . PHE A 8   ? 0.1427 0.1011 0.1550 -0.0040 0.0167  0.0019  8   PHE A CA  
123  C  C   . PHE A 8   ? 0.1188 0.1151 0.1712 -0.0074 0.0133  -0.0056 8   PHE A C   
124  O  O   . PHE A 8   ? 0.1484 0.1105 0.1901 0.0073  -0.0043 -0.0109 8   PHE A O   
125  C  CB  . PHE A 8   ? 0.1423 0.1059 0.1683 -0.0003 0.0316  -0.0036 8   PHE A CB  
126  C  CG  . PHE A 8   ? 0.1477 0.1129 0.1477 0.0043  0.0324  0.0070  8   PHE A CG  
127  C  CD1 . PHE A 8   ? 0.1776 0.1307 0.1573 0.0069  0.0216  -0.0073 8   PHE A CD1 
128  C  CD2 . PHE A 8   ? 0.1448 0.1351 0.1769 0.0037  0.0398  0.0098  8   PHE A CD2 
129  C  CE1 . PHE A 8   ? 0.1921 0.1489 0.1424 0.0011  0.0306  -0.0114 8   PHE A CE1 
130  C  CE2 . PHE A 8   ? 0.1437 0.1625 0.1799 0.0227  0.0428  0.0115  8   PHE A CE2 
131  C  CZ  . PHE A 8   ? 0.1890 0.1626 0.1686 0.0282  0.0363  0.0004  8   PHE A CZ  
141  N  N   . ALA A 9   ? 0.1284 0.1257 0.1661 -0.0071 0.0192  -0.0190 9   ALA A N   
142  C  CA  . ALA A 9   ? 0.1317 0.1447 0.1784 -0.0036 0.0212  -0.0457 9   ALA A CA  
143  C  C   . ALA A 9   ? 0.1184 0.1340 0.1803 0.0032  0.0226  -0.0409 9   ALA A C   
144  O  O   . ALA A 9   ? 0.1220 0.1447 0.1987 0.0071  0.0141  -0.0308 9   ALA A O   
145  C  CB  . ALA A 9   ? 0.1477 0.1937 0.1874 -0.0143 0.0296  -0.0399 9   ALA A CB  
151  N  N   . GLY A 10  ? 0.1197 0.1349 0.2022 0.0015  0.0267  -0.0454 10  GLY A N   
152  C  CA  . GLY A 10  ? 0.1393 0.1323 0.2126 -0.0003 0.0357  -0.0429 10  GLY A CA  
153  C  C   . GLY A 10  ? 0.1283 0.1421 0.2042 0.0083  0.0314  -0.0393 10  GLY A C   
154  O  O   . GLY A 10  ? 0.1395 0.1459 0.2232 0.0115  0.0306  -0.0530 10  GLY A O   
158  N  N   . GLY A 11  ? 0.1298 0.1483 0.2040 0.0162  0.0292  -0.0463 11  GLY A N   
159  C  CA  . GLY A 11  ? 0.1608 0.1778 0.2073 0.0209  0.0160  -0.0619 11  GLY A CA  
160  C  C   . GLY A 11  ? 0.1485 0.1788 0.2176 0.0179  0.0210  -0.0673 11  GLY A C   
161  O  O   . GLY A 11  ? 0.1475 0.1735 0.2224 -0.0011 0.0219  -0.0623 11  GLY A O   
165  N  N   . GLU A 12  ? 0.1363 0.2718 0.2101 0.0411  0.0134  -0.0838 12  GLU A N   
166  C  CA  . GLU A 12  ? 0.1676 0.2569 0.2146 0.0494  0.0030  -0.0698 12  GLU A CA  
167  C  C   . GLU A 12  ? 0.1966 0.2514 0.1994 0.0413  0.0042  -0.0736 12  GLU A C   
168  O  O   . GLU A 12  ? 0.2552 0.2696 0.2616 0.0637  -0.0376 -0.0827 12  GLU A O   
169  C  CB  . GLU A 12  ? 0.1970 0.2177 0.2057 0.0386  0.0066  -0.0564 12  GLU A CB  
170  C  CG  . GLU A 12  ? 0.1957 0.2225 0.2237 0.0103  0.0220  -0.0381 12  GLU A CG  
171  C  CD  . GLU A 12  ? 0.1986 0.2086 0.2317 0.0105  0.0269  -0.0332 12  GLU A CD  
172  O  OE1 . GLU A 12  ? 0.1905 0.2162 0.2437 -0.0050 0.0499  -0.0602 12  GLU A OE1 
173  O  OE2 . GLU A 12  ? 0.2506 0.2253 0.2681 0.0286  0.0055  0.0232  12  GLU A OE2 
180  N  N   . THR A 13  ? 0.1906 0.2486 0.2364 0.0376  0.0180  -0.0410 13  THR A N   
181  C  CA  . THR A 13  ? 0.2197 0.2739 0.2453 0.0289  0.0715  -0.0245 13  THR A CA  
182  C  C   . THR A 13  ? 0.1691 0.2800 0.2141 0.0084  0.0182  -0.0226 13  THR A C   
183  O  O   . THR A 13  ? 0.1825 0.2510 0.2129 0.0028  0.0081  -0.0211 13  THR A O   
184  C  CB  . THR A 13  ? 0.2750 0.3008 0.3319 0.0234  0.1335  0.0487  13  THR A CB  
185  O  OG1 . THR A 13  ? 0.3245 0.3853 0.4778 0.0188  0.1451  0.0326  13  THR A OG1 
186  C  CG2 . THR A 13  ? 0.3273 0.3775 0.3649 0.0152  0.1457  0.0545  13  THR A CG2 
194  N  N   . GLY A 14  ? 0.1697 0.2885 0.2073 0.0293  0.0162  -0.0343 14  GLY A N   
195  C  CA  . GLY A 14  ? 0.1669 0.2679 0.2222 0.0062  0.0118  -0.0266 14  GLY A CA  
196  C  C   . GLY A 14  ? 0.1677 0.2493 0.2022 -0.0029 0.0079  -0.0103 14  GLY A C   
197  O  O   . GLY A 14  ? 0.1837 0.2360 0.2183 0.0293  0.0071  -0.0153 14  GLY A O   
201  N  N   . VAL A 15  ? 0.1688 0.2275 0.1920 -0.0147 0.0061  0.0103  15  VAL A N   
202  C  CA  . VAL A 15  ? 0.1667 0.2083 0.1948 -0.0155 0.0001  0.0039  15  VAL A CA  
203  C  C   . VAL A 15  ? 0.1510 0.1805 0.1954 -0.0191 -0.0020 -0.0138 15  VAL A C   
204  O  O   . VAL A 15  ? 0.1591 0.2630 0.2038 -0.0204 -0.0188 -0.0043 15  VAL A O   
205  C  CB  . VAL A 15  ? 0.1946 0.2247 0.2219 -0.0082 -0.0143 0.0279  15  VAL A CB  
206  C  CG1 . VAL A 15  ? 0.2312 0.2963 0.2981 -0.0315 0.0291  0.0281  15  VAL A CG1 
207  C  CG2 . VAL A 15  ? 0.2160 0.2311 0.2362 -0.0210 -0.0279 0.0209  15  VAL A CG2 
217  N  N   . TRP A 16  ? 0.1427 0.1489 0.1863 -0.0105 0.0052  -0.0306 16  TRP A N   
218  C  CA  . TRP A 16  ? 0.1333 0.1486 0.1914 0.0000  0.0074  -0.0141 16  TRP A CA  
219  C  C   . TRP A 16  ? 0.1300 0.1369 0.1947 0.0021  0.0031  -0.0263 16  TRP A C   
220  O  O   . TRP A 16  ? 0.1319 0.1407 0.2256 0.0064  -0.0010 -0.0279 16  TRP A O   
221  C  CB  . TRP A 16  ? 0.1393 0.1355 0.1779 0.0021  0.0113  -0.0084 16  TRP A CB  
222  C  CG  . TRP A 16  ? 0.1345 0.1293 0.1733 -0.0006 -0.0039 -0.0154 16  TRP A CG  
223  C  CD1 . TRP A 16  ? 0.1584 0.1370 0.1971 -0.0127 -0.0088 -0.0251 16  TRP A CD1 
224  C  CD2 . TRP A 16  ? 0.1446 0.1323 0.1662 0.0040  -0.0071 -0.0232 16  TRP A CD2 
225  N  NE1 . TRP A 16  ? 0.1628 0.1315 0.2126 -0.0285 -0.0106 -0.0241 16  TRP A NE1 
226  C  CE2 . TRP A 16  ? 0.1618 0.1377 0.1847 0.0013  -0.0115 -0.0261 16  TRP A CE2 
227  C  CE3 . TRP A 16  ? 0.1446 0.1564 0.1717 -0.0049 0.0000  -0.0157 16  TRP A CE3 
228  C  CZ2 . TRP A 16  ? 0.1819 0.1244 0.1942 0.0101  -0.0248 -0.0249 16  TRP A CZ2 
229  C  CZ3 . TRP A 16  ? 0.1442 0.1620 0.1597 0.0161  -0.0055 -0.0201 16  TRP A CZ3 
230  C  CH2 . TRP A 16  ? 0.1634 0.1574 0.1776 0.0241  -0.0195 -0.0198 16  TRP A CH2 
241  N  N   . ARG A 17  ? 0.1303 0.1391 0.1963 -0.0028 0.0168  -0.0230 17  ARG A N   
242  C  CA  . ARG A 17  ? 0.1582 0.1259 0.1997 -0.0128 0.0151  -0.0438 17  ARG A CA  
243  C  C   . ARG A 17  ? 0.1382 0.1085 0.2052 -0.0084 0.0075  -0.0266 17  ARG A C   
244  O  O   . ARG A 17  ? 0.1433 0.1347 0.2081 0.0117  0.0139  -0.0262 17  ARG A O   
245  C  CB  . ARG A 17  ? 0.2030 0.1509 0.2061 -0.0167 -0.0031 -0.0432 17  ARG A CB  
246  C  CG  . ARG A 17  ? 0.2906 0.1677 0.2796 -0.0226 -0.0395 -0.0562 17  ARG A CG  
247  C  CD  . ARG A 17  ? 0.3231 0.2242 0.3764 -0.0169 -0.0708 -0.0584 17  ARG A CD  
248  N  NE  . ARG A 17  ? 0.3222 0.3987 0.4277 -0.0240 -0.0727 -0.0271 17  ARG A NE  
249  C  CZ  . ARG A 17  ? 0.3941 0.4390 0.4543 0.0166  -0.0497 -0.0373 17  ARG A CZ  
250  N  NH1 . ARG A 17  ? 0.4560 0.5808 0.4563 -0.0025 -0.0278 -0.1399 17  ARG A NH1 
251  N  NH2 . ARG A 17  ? 0.1916 0.2741 0.4674 -0.0339 -0.0588 -0.0054 17  ARG A NH2 
265  N  N   . VAL A 18  ? 0.1349 0.1231 0.2082 0.0093  0.0037  -0.0276 18  VAL A N   
266  C  CA  . VAL A 18  ? 0.1450 0.1216 0.2091 0.0067  0.0062  -0.0244 18  VAL A CA  
267  C  C   . VAL A 18  ? 0.1615 0.1206 0.2233 -0.0089 0.0118  -0.0306 18  VAL A C   
268  O  O   . VAL A 18  ? 0.1922 0.1280 0.2634 -0.0181 0.0305  -0.0566 18  VAL A O   
269  C  CB  . VAL A 18  ? 0.1650 0.1372 0.2130 0.0102  0.0044  -0.0058 18  VAL A CB  
270  C  CG1 . VAL A 18  ? 0.1641 0.1556 0.2099 0.0167  -0.0008 -0.0034 18  VAL A CG1 
271  C  CG2 . VAL A 18  ? 0.1401 0.1677 0.2287 0.0150  -0.0018 -0.0189 18  VAL A CG2 
281  N  N   . VAL A 19  ? 0.1478 0.1109 0.2187 -0.0068 0.0082  -0.0209 19  VAL A N   
282  C  CA  . VAL A 19  ? 0.1656 0.1232 0.2543 -0.0191 0.0249  -0.0240 19  VAL A CA  
283  C  C   . VAL A 19  ? 0.1881 0.1372 0.2474 -0.0415 0.0071  -0.0023 19  VAL A C   
284  O  O   . VAL A 19  ? 0.3038 0.1646 0.2937 -0.0969 -0.0137 0.0168  19  VAL A O   
285  C  CB  . VAL A 19  ? 0.1724 0.1563 0.3384 -0.0263 0.0193  0.0075  19  VAL A CB  
286  C  CG1 . VAL A 19  ? 0.1864 0.1643 0.3692 -0.0495 -0.0130 0.0252  19  VAL A CG1 
287  C  CG2 . VAL A 19  ? 0.1992 0.1783 0.3515 -0.0386 -0.0099 -0.0361 19  VAL A CG2 
297  N  N   . ALA A 20  ? 0.1737 0.1263 0.2352 -0.0169 0.0117  -0.0066 20  ALA A N   
298  C  CA  . ALA A 20  ? 0.2119 0.1278 0.2341 -0.0278 0.0189  0.0079  20  ALA A CA  
299  C  C   . ALA A 20  ? 0.1997 0.1078 0.2419 0.0119  0.0192  -0.0011 20  ALA A C   
300  O  O   . ALA A 20  ? 0.1979 0.0949 0.2357 0.0037  0.0144  -0.0106 20  ALA A O   
301  C  CB  . ALA A 20  ? 0.2370 0.2115 0.2619 -0.0379 0.0233  0.0215  20  ALA A CB  
307  N  N   . MET A 21  ? 0.2234 0.0870 0.2590 0.0020  0.0035  -0.0008 21  MET A N   
308  C  CA  . MET A 21  ? 0.2278 0.1215 0.2398 0.0124  -0.0009 -0.0019 21  MET A CA  
309  C  C   . MET A 21  ? 0.1869 0.1209 0.2570 0.0086  -0.0048 0.0353  21  MET A C   
310  O  O   . MET A 21  ? 0.2821 0.1281 0.3233 0.0210  0.0003  0.0561  21  MET A O   
311  C  CB  . MET A 21  ? 0.2174 0.1742 0.2605 0.0265  -0.0010 0.0056  21  MET A CB  
312  C  CG  . MET A 21  ? 0.2417 0.2374 0.3149 0.0190  0.0056  0.0254  21  MET A CG  
313  S  SD  . MET A 21  ? 0.2418 0.2938 0.3734 0.0448  0.0213  0.0118  21  MET A SD  
314  C  CE  . MET A 21  ? 0.2693 0.1547 0.3541 0.0093  0.0926  -0.0005 21  MET A CE  
324  N  N   . ASN A 22  ? 0.2096 0.1435 0.2338 -0.0303 -0.0185 0.0282  22  ASN A N   
325  C  CA  . ASN A 22  ? 0.2227 0.1829 0.2378 -0.0125 -0.0167 0.0291  22  ASN A CA  
326  C  C   . ASN A 22  ? 0.2148 0.1520 0.2180 -0.0201 0.0007  0.0369  22  ASN A C   
327  O  O   . ASN A 22  ? 0.2135 0.1194 0.2468 -0.0138 -0.0419 0.0368  22  ASN A O   
328  C  CB  . ASN A 22  ? 0.1873 0.1722 0.2731 -0.0056 -0.0271 0.0145  22  ASN A CB  
329  C  CG  . ASN A 22  ? 0.2206 0.1820 0.3120 0.0073  -0.0553 0.0209  22  ASN A CG  
330  O  OD1 . ASN A 22  ? 0.3044 0.1854 0.3579 0.0107  -0.1062 0.0153  22  ASN A OD1 
331  N  ND2 . ASN A 22  ? 0.2232 0.1815 0.3424 -0.0405 -0.0725 0.0532  22  ASN A ND2 
338  N  N   . ALA A 23  ? 0.2452 0.1623 0.2437 0.0297  0.0129  0.0271  23  ALA A N   
339  C  CA  . ALA A 23  ? 0.1597 0.2172 0.2676 0.0476  0.0169  0.0303  23  ALA A CA  
340  C  C   . ALA A 23  ? 0.1744 0.1512 0.2398 0.0217  0.0081  0.0362  23  ALA A C   
341  O  O   . ALA A 23  ? 0.2151 0.1374 0.2548 0.0115  0.0000  0.0351  23  ALA A O   
342  C  CB  . ALA A 23  ? 0.2140 0.2315 0.3346 0.0655  0.0124  0.0126  23  ALA A CB  
348  N  N   . VAL A 24  ? 0.1548 0.1533 0.2430 0.0116  0.0304  0.0440  24  VAL A N   
349  C  CA  . VAL A 24  ? 0.1463 0.1336 0.2357 0.0158  0.0095  0.0455  24  VAL A CA  
350  C  C   . VAL A 24  ? 0.1453 0.1287 0.2476 0.0005  0.0167  0.0589  24  VAL A C   
351  O  O   . VAL A 24  ? 0.1532 0.1498 0.2609 -0.0069 0.0181  0.0607  24  VAL A O   
352  C  CB  . VAL A 24  ? 0.1735 0.1510 0.2622 0.0256  -0.0035 0.0399  24  VAL A CB  
353  C  CG1 . VAL A 24  ? 0.2215 0.1511 0.2443 0.0406  -0.0202 0.0161  24  VAL A CG1 
354  C  CG2 . VAL A 24  ? 0.2145 0.1628 0.2586 0.0697  -0.0194 0.0229  24  VAL A CG2 
364  N  N   . ALA A 25  ? 0.1327 0.1495 0.2229 0.0111  0.0142  0.0662  25  ALA A N   
365  C  CA  . ALA A 25  ? 0.1418 0.1417 0.2233 0.0107  0.0191  0.0611  25  ALA A CA  
366  C  C   . ALA A 25  ? 0.1387 0.1325 0.1910 0.0144  0.0102  0.0336  25  ALA A C   
367  O  O   . ALA A 25  ? 0.1350 0.1174 0.2115 0.0044  0.0182  0.0402  25  ALA A O   
368  C  CB  . ALA A 25  ? 0.1588 0.1805 0.2059 0.0248  0.0253  0.0359  25  ALA A CB  
374  N  N   . GLY A 26  ? 0.1420 0.1394 0.2048 0.0207  0.0021  0.0407  26  GLY A N   
375  C  CA  . GLY A 26  ? 0.1442 0.1308 0.2019 0.0274  0.0005  0.0215  26  GLY A CA  
376  C  C   . GLY A 26  ? 0.1425 0.1038 0.1964 0.0256  -0.0243 0.0283  26  GLY A C   
377  O  O   . GLY A 26  ? 0.1562 0.1105 0.2101 0.0174  -0.0285 0.0300  26  GLY A O   
381  N  N   . ALA A 27  ? 0.1495 0.1003 0.1822 0.0232  -0.0142 0.0242  27  ALA A N   
382  C  CA  . ALA A 27  ? 0.1595 0.1062 0.1786 0.0172  -0.0208 0.0099  27  ALA A CA  
383  C  C   . ALA A 27  ? 0.1637 0.1104 0.1940 0.0144  -0.0218 0.0137  27  ALA A C   
384  O  O   . ALA A 27  ? 0.1807 0.1063 0.1996 0.0238  -0.0065 0.0284  27  ALA A O   
385  C  CB  . ALA A 27  ? 0.1631 0.1162 0.1753 0.0292  -0.0208 0.0026  27  ALA A CB  
391  N  N   . PRO A 28  ? 0.1732 0.1494 0.1841 0.0012  -0.0284 0.0198  28  PRO A N   
392  C  CA  . PRO A 28  ? 0.1514 0.1826 0.1867 0.0099  -0.0243 0.0239  28  PRO A CA  
393  C  C   . PRO A 28  ? 0.1452 0.1408 0.2052 0.0167  -0.0183 0.0131  28  PRO A C   
394  O  O   . PRO A 28  ? 0.1446 0.2000 0.2516 0.0172  -0.0250 0.0434  28  PRO A O   
395  C  CB  . PRO A 28  ? 0.2074 0.2691 0.1938 -0.0496 -0.0275 0.0216  28  PRO A CB  
396  C  CG  . PRO A 28  ? 0.2368 0.1967 0.2017 -0.0720 -0.0189 -0.0228 28  PRO A CG  
397  C  CD  . PRO A 28  ? 0.2163 0.1679 0.1964 -0.0338 -0.0304 0.0194  28  PRO A CD  
405  N  N   . LEU A 29  ? 0.1647 0.1443 0.2016 0.0233  -0.0111 0.0159  29  LEU A N   
406  C  CA  . LEU A 29  ? 0.1916 0.1320 0.1979 -0.0037 0.0084  0.0177  29  LEU A CA  
407  C  C   . LEU A 29  ? 0.1868 0.1196 0.2159 -0.0063 0.0126  0.0197  29  LEU A C   
408  O  O   . LEU A 29  ? 0.1883 0.1460 0.2310 -0.0146 0.0233  0.0045  29  LEU A O   
409  C  CB  . LEU A 29  ? 0.2495 0.1299 0.1967 0.0038  0.0012  0.0001  29  LEU A CB  
410  C  CG  . LEU A 29  ? 0.2859 0.1586 0.1841 -0.0171 -0.0006 -0.0012 29  LEU A CG  
411  C  CD1 . LEU A 29  ? 0.3451 0.1513 0.2132 -0.0025 -0.0066 -0.0005 29  LEU A CD1 
412  C  CD2 . LEU A 29  ? 0.2837 0.2065 0.2389 -0.0148 0.0033  -0.0377 29  LEU A CD2 
424  N  N   . PRO A 30  ? 0.1828 0.1373 0.2321 0.0120  0.0238  0.0097  30  PRO A N   
425  C  CA  . PRO A 30  ? 0.2129 0.1391 0.2401 0.0144  0.0292  0.0075  30  PRO A CA  
426  C  C   . PRO A 30  ? 0.1849 0.1253 0.2210 0.0093  0.0237  0.0019  30  PRO A C   
427  O  O   . PRO A 30  ? 0.1732 0.1145 0.2430 0.0122  0.0138  -0.0037 30  PRO A O   
428  C  CB  . PRO A 30  ? 0.1911 0.1937 0.2666 0.0362  0.0318  -0.0250 30  PRO A CB  
429  C  CG  . PRO A 30  ? 0.2035 0.2272 0.2917 0.0337  0.0268  -0.0133 30  PRO A CG  
430  C  CD  . PRO A 30  ? 0.1756 0.1598 0.2431 0.0113  0.0172  0.0000  30  PRO A CD  
438  N  N   . GLY A 31  ? 0.1978 0.1065 0.2550 0.0019  0.0120  -0.0033 31  GLY A N   
439  C  CA  . GLY A 31  ? 0.1784 0.1357 0.2691 0.0053  0.0165  -0.0082 31  GLY A CA  
440  C  C   . GLY A 31  ? 0.1697 0.1335 0.2714 0.0017  -0.0017 -0.0243 31  GLY A C   
441  O  O   . GLY A 31  ? 0.1812 0.2097 0.2594 0.0308  0.0121  0.0087  31  GLY A O   
445  N  N   . ILE A 32  ? 0.1633 0.1437 0.2671 -0.0039 -0.0149 -0.0113 32  ILE A N   
446  C  CA  . ILE A 32  ? 0.1687 0.1799 0.2649 -0.0289 -0.0110 0.0019  32  ILE A CA  
447  C  C   . ILE A 32  ? 0.1789 0.1218 0.2740 0.0026  -0.0162 -0.0334 32  ILE A C   
448  O  O   . ILE A 32  ? 0.1802 0.1487 0.2661 0.0064  -0.0063 -0.0417 32  ILE A O   
449  C  CB  . ILE A 32  ? 0.1899 0.2131 0.2289 -0.0290 -0.0093 0.0016  32  ILE A CB  
450  C  CG1 . ILE A 32  ? 0.1659 0.1622 0.2783 0.0063  -0.0145 -0.0308 32  ILE A CG1 
451  C  CG2 . ILE A 32  ? 0.2019 0.1974 0.2408 -0.0456 0.0031  0.0002  32  ILE A CG2 
452  C  CD1 . ILE A 32  ? 0.2057 0.1765 0.2468 0.0117  0.0254  -0.0340 32  ILE A CD1 
464  N  N   . PRO A 33  ? 0.1578 0.1272 0.2591 0.0102  -0.0027 -0.0376 33  PRO A N   
465  C  CA  . PRO A 33  ? 0.1729 0.1257 0.2464 0.0149  -0.0116 -0.0460 33  PRO A CA  
466  C  C   . PRO A 33  ? 0.1595 0.1235 0.2158 0.0143  0.0021  -0.0421 33  PRO A C   
467  O  O   . PRO A 33  ? 0.1493 0.1346 0.2204 0.0093  0.0016  -0.0530 33  PRO A O   
468  C  CB  . PRO A 33  ? 0.1872 0.1527 0.2723 0.0379  -0.0011 -0.0712 33  PRO A CB  
469  C  CG  . PRO A 33  ? 0.1828 0.1635 0.2886 0.0096  0.0198  -0.0669 33  PRO A CG  
470  C  CD  . PRO A 33  ? 0.1710 0.1586 0.2853 0.0172  0.0033  -0.0427 33  PRO A CD  
478  N  N   . ARG A 34  ? 0.1460 0.1237 0.2146 0.0225  0.0058  -0.0387 34  ARG A N   
479  C  CA  . ARG A 34  ? 0.1390 0.1411 0.2111 0.0172  0.0048  -0.0359 34  ARG A CA  
480  C  C   . ARG A 34  ? 0.1209 0.1346 0.2008 0.0111  0.0168  -0.0330 34  ARG A C   
481  O  O   . ARG A 34  ? 0.1374 0.1358 0.2108 0.0141  0.0113  -0.0440 34  ARG A O   
482  C  CB  . ARG A 34  ? 0.1800 0.1641 0.2075 0.0212  0.0001  -0.0329 34  ARG A CB  
483  C  CG  . ARG A 34  ? 0.2523 0.1915 0.2105 0.0182  0.0052  -0.0530 34  ARG A CG  
484  C  CD  . ARG A 34  ? 0.2729 0.2462 0.2451 0.0431  -0.0056 -0.0117 34  ARG A CD  
485  N  NE  . ARG A 34  ? 0.2572 0.2443 0.2728 0.0291  -0.0048 -0.0254 34  ARG A NE  
486  C  CZ  . ARG A 34  ? 0.2865 0.2879 0.3262 -0.0027 -0.0155 -0.0357 34  ARG A CZ  
487  N  NH1 . ARG A 34  ? 0.3913 0.3057 0.3481 -0.0452 -0.0287 -0.0575 34  ARG A NH1 
488  N  NH2 . ARG A 34  ? 0.2807 0.3166 0.3209 -0.0168 -0.0091 -0.0150 34  ARG A NH2 
502  N  N   . LEU A 35  ? 0.1228 0.1238 0.2192 0.0065  0.0087  -0.0345 35  LEU A N   
503  C  CA  . LEU A 35  ? 0.1290 0.1139 0.2188 -0.0029 0.0162  -0.0239 35  LEU A CA  
504  C  C   . LEU A 35  ? 0.1308 0.1186 0.2036 -0.0125 0.0149  -0.0312 35  LEU A C   
505  O  O   . LEU A 35  ? 0.1418 0.1352 0.2039 -0.0075 0.0174  -0.0151 35  LEU A O   
506  C  CB  . LEU A 35  ? 0.1375 0.1373 0.1938 -0.0023 0.0129  -0.0167 35  LEU A CB  
507  C  CG  . LEU A 35  ? 0.1650 0.1927 0.1914 -0.0142 0.0169  -0.0448 35  LEU A CG  
508  C  CD1 . LEU A 35  ? 0.1517 0.2259 0.2172 0.0179  0.0048  -0.0654 35  LEU A CD1 
509  C  CD2 . LEU A 35  ? 0.1878 0.1916 0.2259 0.0102  0.0157  -0.0518 35  LEU A CD2 
521  N  N   . ASN A 36  ? 0.1460 0.1415 0.1866 -0.0162 0.0193  -0.0349 36  ASN A N   
522  C  CA  . ASN A 36  ? 0.1764 0.1657 0.1843 -0.0256 0.0220  -0.0283 36  ASN A CA  
523  C  C   . ASN A 36  ? 0.1633 0.1430 0.1613 -0.0222 0.0076  -0.0075 36  ASN A C   
524  O  O   . ASN A 36  ? 0.2027 0.1382 0.1889 0.0028  -0.0276 -0.0227 36  ASN A O   
525  C  CB  . ASN A 36  ? 0.1724 0.2177 0.1923 -0.0390 0.0233  -0.0377 36  ASN A CB  
526  C  CG  . ASN A 36  ? 0.1679 0.2768 0.2251 -0.0028 0.0583  0.0242  36  ASN A CG  
527  O  OD1 . ASN A 36  ? 0.2213 0.3426 0.3159 -0.0332 0.0331  0.0191  36  ASN A OD1 
528  N  ND2 . ASN A 36  ? 0.1818 0.2871 0.2116 0.0014  0.0382  0.0373  36  ASN A ND2 
535  N  N   . VAL A 37  ? 0.1657 0.1334 0.1643 -0.0288 0.0144  0.0105  37  VAL A N   
536  C  CA  . VAL A 37  ? 0.1546 0.1378 0.1581 -0.0237 0.0090  0.0056  37  VAL A CA  
537  C  C   . VAL A 37  ? 0.1723 0.1350 0.1556 -0.0073 0.0190  0.0108  37  VAL A C   
538  O  O   . VAL A 37  ? 0.2039 0.1942 0.2057 0.0243  0.0470  0.0731  37  VAL A O   
539  C  CB  . VAL A 37  ? 0.1641 0.1630 0.1810 -0.0127 0.0283  0.0013  37  VAL A CB  
540  C  CG1 . VAL A 37  ? 0.1914 0.1346 0.2102 -0.0295 0.0468  -0.0110 37  VAL A CG1 
541  C  CG2 . VAL A 37  ? 0.1749 0.1942 0.2051 -0.0359 0.0266  -0.0164 37  VAL A CG2 
551  N  N   . ALA A 38  ? 0.1712 0.1258 0.1442 -0.0375 0.0036  -0.0043 38  ALA A N   
552  C  CA  . ALA A 38  ? 0.1804 0.1317 0.1575 -0.0376 0.0188  0.0020  38  ALA A CA  
553  C  C   . ALA A 38  ? 0.1467 0.1251 0.1488 -0.0365 0.0162  0.0086  38  ALA A C   
554  O  O   . ALA A 38  ? 0.1780 0.1195 0.1390 -0.0251 0.0096  0.0024  38  ALA A O   
555  C  CB  . ALA A 38  ? 0.1866 0.1535 0.1828 -0.0321 0.0499  -0.0152 38  ALA A CB  
561  N  N   . ALA A 39  ? 0.1416 0.1250 0.1505 -0.0179 0.0055  0.0176  39  ALA A N   
562  C  CA  . ALA A 39  ? 0.1341 0.1277 0.1477 -0.0207 0.0120  0.0113  39  ALA A CA  
563  C  C   . ALA A 39  ? 0.1395 0.1232 0.1461 -0.0264 0.0188  0.0060  39  ALA A C   
564  O  O   . ALA A 39  ? 0.1390 0.1658 0.1455 -0.0284 0.0243  -0.0091 39  ALA A O   
565  C  CB  . ALA A 39  ? 0.1534 0.1411 0.1714 -0.0225 -0.0035 0.0180  39  ALA A CB  
571  N  N   . GLY A 40  ? 0.1348 0.1289 0.1458 -0.0124 0.0210  -0.0009 40  GLY A N   
572  C  CA  . GLY A 40  ? 0.1416 0.1338 0.1550 -0.0168 0.0091  0.0023  40  GLY A CA  
573  C  C   . GLY A 40  ? 0.1283 0.1365 0.1566 -0.0156 0.0151  -0.0039 40  GLY A C   
574  O  O   . GLY A 40  ? 0.1441 0.1382 0.1910 -0.0226 0.0171  0.0084  40  GLY A O   
578  N  N   . SER A 41  ? 0.1387 0.1485 0.1890 -0.0149 0.0237  0.0033  41  SER A N   
579  C  CA  . SER A 41  ? 0.1592 0.1633 0.2200 0.0006  0.0326  0.0126  41  SER A CA  
580  C  C   . SER A 41  ? 0.1678 0.1867 0.2614 -0.0020 0.0712  0.0145  41  SER A C   
581  O  O   . SER A 41  ? 0.3096 0.2114 0.2731 -0.0149 0.1277  -0.0084 41  SER A O   
582  C  CB  . SER A 41  ? 0.1743 0.2071 0.2497 -0.0045 0.0063  0.0244  41  SER A CB  
583  O  OG  . SER A 41  ? 0.1825 0.2622 0.2377 -0.0217 -0.0215 0.0146  41  SER A OG  
589  N  N   . VAL A 42  ? 0.2583 0.1775 0.2045 -0.0169 0.0423  0.0119  42  VAL A N   
590  C  CA  . VAL A 42  ? 0.2343 0.1822 0.2213 -0.0151 0.0446  0.0044  42  VAL A CA  
591  C  C   . VAL A 42  ? 0.2307 0.1916 0.2668 -0.0155 0.0290  0.0241  42  VAL A C   
592  O  O   . VAL A 42  ? 0.2378 0.2242 0.2929 -0.0201 0.0085  0.0398  42  VAL A O   
593  C  CB  . VAL A 42  ? 0.2398 0.1850 0.2279 -0.0015 0.0493  -0.0174 42  VAL A CB  
594  C  CG1 . VAL A 42  ? 0.2456 0.2247 0.2545 0.0068  0.0221  -0.0423 42  VAL A CG1 
595  C  CG2 . VAL A 42  ? 0.2552 0.2609 0.2232 0.0143  0.0452  -0.0518 42  VAL A CG2 
605  N  N   . SER A 43  ? 0.2096 0.1869 0.3164 -0.0173 0.0414  0.0180  43  SER A N   
606  C  CA  . SER A 43  ? 0.2055 0.2229 0.3869 -0.0207 0.0358  0.0180  43  SER A CA  
607  C  C   . SER A 43  ? 0.2421 0.2213 0.3971 0.0002  0.0865  0.0290  43  SER A C   
608  O  O   . SER A 43  ? 0.3101 0.2621 0.4586 -0.0040 0.0954  0.0811  43  SER A O   
609  C  CB  . SER A 43  ? 0.2432 0.3087 0.4827 -0.0184 -0.0281 -0.0210 43  SER A CB  
610  O  OG  . SER A 43  ? 0.2683 0.3834 0.5678 0.0099  -0.0556 -0.0673 43  SER A OG  
616  N  N   . PRO A 44  ? 0.2580 0.2393 0.3625 -0.0087 0.0882  0.0296  44  PRO A N   
617  C  CA  . PRO A 44  ? 0.2468 0.2255 0.3792 -0.0370 0.1017  -0.0072 44  PRO A CA  
618  C  C   . PRO A 44  ? 0.2702 0.1986 0.3847 -0.0538 0.0853  -0.0581 44  PRO A C   
619  O  O   . PRO A 44  ? 0.2521 0.2569 0.4395 -0.0273 0.0860  -0.0815 44  PRO A O   
620  C  CB  . PRO A 44  ? 0.2858 0.2355 0.3808 -0.0016 0.1145  -0.0016 44  PRO A CB  
621  C  CG  . PRO A 44  ? 0.3188 0.3451 0.3782 -0.0065 0.1212  -0.0024 44  PRO A CG  
622  C  CD  . PRO A 44  ? 0.2854 0.3359 0.3562 0.0102  0.1153  0.0477  44  PRO A CD  
630  N  N   . GLN A 45  ? 0.3130 0.2171 0.4107 -0.0954 0.1133  -0.0762 45  GLN A N   
631  C  CA  . GLN A 45  ? 0.3234 0.2389 0.4476 -0.0985 0.1305  -0.1197 45  GLN A CA  
632  C  C   . GLN A 45  ? 0.3304 0.2803 0.4087 -0.0484 0.1526  -0.1565 45  GLN A C   
633  O  O   . GLN A 45  ? 0.3205 0.3958 0.4870 -0.0664 0.1761  -0.1999 45  GLN A O   
634  C  CB  . GLN A 45  ? 0.3563 0.2885 0.4976 -0.0434 0.1379  -0.0704 45  GLN A CB  
635  C  CG  . GLN A 45  ? 0.3466 0.2595 0.5182 -0.0539 0.0524  -0.0944 45  GLN A CG  
636  C  CD  . GLN A 45  ? 0.2142 0.2747 0.5834 -0.0406 0.0825  -0.0649 45  GLN A CD  
637  O  OE1 . GLN A 45  ? 0.3100 0.3494 0.6259 -0.0339 -0.0098 -0.0757 45  GLN A OE1 
638  N  NE2 . GLN A 45  ? 0.3113 0.2988 0.5809 0.0115  0.0720  -0.0144 45  GLN A NE2 
647  N  N   . PRO A 46  ? 0.3400 0.2290 0.4227 -0.0531 0.1362  -0.1073 46  PRO A N   
648  C  CA  . PRO A 46  ? 0.3455 0.2210 0.3910 -0.0022 0.1306  -0.0575 46  PRO A CA  
649  C  C   . PRO A 46  ? 0.2922 0.2200 0.3679 -0.0295 0.1225  -0.0459 46  PRO A C   
650  O  O   . PRO A 46  ? 0.2774 0.2264 0.3063 -0.0614 0.0913  -0.0638 46  PRO A O   
651  C  CB  . PRO A 46  ? 0.3480 0.2528 0.4568 -0.0174 0.1418  -0.0425 46  PRO A CB  
652  C  CG  . PRO A 46  ? 0.3667 0.2120 0.4584 -0.0202 0.1422  -0.0431 46  PRO A CG  
653  C  CD  . PRO A 46  ? 0.3587 0.2684 0.4307 -0.0139 0.1522  -0.0829 46  PRO A CD  
661  N  N   . PRO A 47  ? 0.3093 0.2223 0.3339 -0.0470 0.0994  -0.0450 47  PRO A N   
662  C  CA  . PRO A 47  ? 0.2865 0.2056 0.2971 -0.0103 0.0935  -0.0533 47  PRO A CA  
663  C  C   . PRO A 47  ? 0.2456 0.2023 0.2794 0.0057  0.0385  -0.0786 47  PRO A C   
664  O  O   . PRO A 47  ? 0.2695 0.2738 0.3039 0.0334  0.0616  -0.0558 47  PRO A O   
665  C  CB  . PRO A 47  ? 0.3399 0.2595 0.2906 -0.0283 0.0886  -0.0418 47  PRO A CB  
666  C  CG  . PRO A 47  ? 0.3593 0.2952 0.3566 -0.0366 0.1212  -0.0401 47  PRO A CG  
667  C  CD  . PRO A 47  ? 0.3964 0.2876 0.3177 -0.0442 0.1185  -0.0447 47  PRO A CD  
675  N  N   . GLY A 48  ? 0.2222 0.2185 0.2152 -0.0449 0.0688  -0.0760 48  GLY A N   
676  C  CA  . GLY A 48  ? 0.1616 0.2355 0.2970 -0.0091 0.0522  -0.1062 48  GLY A CA  
677  C  C   . GLY A 48  ? 0.1524 0.2456 0.3084 -0.0143 0.0505  -0.1260 48  GLY A C   
678  O  O   . GLY A 48  ? 0.1563 0.2704 0.3340 -0.0171 0.0668  -0.1473 48  GLY A O   
682  N  N   . THR A 49  ? 0.1493 0.2168 0.2782 -0.0046 0.0496  -0.1047 49  THR A N   
683  C  CA  . THR A 49  ? 0.1629 0.1694 0.2572 0.0136  0.0412  -0.0613 49  THR A CA  
684  C  C   . THR A 49  ? 0.1593 0.1740 0.2994 0.0132  0.0671  -0.0401 49  THR A C   
685  O  O   . THR A 49  ? 0.1928 0.2266 0.3486 0.0519  0.0977  0.0184  49  THR A O   
686  C  CB  . THR A 49  ? 0.2229 0.1647 0.2115 0.0030  0.0407  -0.0381 49  THR A CB  
687  O  OG1 . THR A 49  ? 0.2628 0.1882 0.2407 0.0329  0.0448  -0.0236 49  THR A OG1 
688  C  CG2 . THR A 49  ? 0.2645 0.1666 0.2239 -0.0275 0.0536  -0.0418 49  THR A CG2 
696  N  N   . LYS A 50  ? 0.1745 0.1489 0.2998 0.0178  0.0714  -0.0504 50  LYS A N   
697  C  CA  . LYS A 50  ? 0.1895 0.1438 0.3456 0.0285  0.0809  -0.0336 50  LYS A CA  
698  C  C   . LYS A 50  ? 0.1497 0.1592 0.3100 0.0414  0.0592  -0.0034 50  LYS A C   
699  O  O   . LYS A 50  ? 0.1876 0.1736 0.3866 0.0437  0.0392  0.0059  50  LYS A O   
700  C  CB  . LYS A 50  ? 0.2286 0.1814 0.4208 -0.0128 0.1097  -0.0517 50  LYS A CB  
701  C  CG  . LYS A 50  ? 0.2632 0.2015 0.5207 -0.0189 0.1010  -0.0867 50  LYS A CG  
702  C  CD  . LYS A 50  ? 0.2696 0.2454 0.5707 -0.0276 0.0980  -0.0539 50  LYS A CD  
703  C  CE  . LYS A 50  ? 0.3629 0.2533 0.5765 0.0092  0.0973  -0.0744 50  LYS A CE  
704  N  NZ  . LYS A 50  ? 0.2650 0.1917 0.5796 0.0096  0.0897  -0.0846 50  LYS A NZ  
718  N  N   . TRP A 51  ? 0.1536 0.1362 0.2411 0.0201  0.0438  -0.0062 51  TRP A N   
719  C  CA  . TRP A 51  ? 0.1500 0.1481 0.2220 0.0148  0.0315  -0.0038 51  TRP A CA  
720  C  C   . TRP A 51  ? 0.1158 0.1441 0.2115 0.0045  0.0224  -0.0103 51  TRP A C   
721  O  O   . TRP A 51  ? 0.1284 0.1499 0.1980 0.0066  0.0268  -0.0224 51  TRP A O   
722  C  CB  . TRP A 51  ? 0.1650 0.1557 0.2296 -0.0037 0.0159  0.0094  51  TRP A CB  
723  C  CG  . TRP A 51  ? 0.1522 0.1532 0.1940 -0.0094 0.0248  -0.0199 51  TRP A CG  
724  C  CD1 . TRP A 51  ? 0.1882 0.1428 0.1950 0.0079  0.0334  -0.0003 51  TRP A CD1 
725  C  CD2 . TRP A 51  ? 0.1575 0.1312 0.1801 -0.0143 0.0274  -0.0193 51  TRP A CD2 
726  N  NE1 . TRP A 51  ? 0.1837 0.1324 0.1888 -0.0123 0.0330  -0.0063 51  TRP A NE1 
727  C  CE2 . TRP A 51  ? 0.1673 0.1335 0.1792 -0.0096 0.0353  -0.0152 51  TRP A CE2 
728  C  CE3 . TRP A 51  ? 0.1471 0.1428 0.1898 -0.0172 0.0352  -0.0300 51  TRP A CE3 
729  C  CZ2 . TRP A 51  ? 0.1577 0.1622 0.1849 -0.0153 0.0383  -0.0267 51  TRP A CZ2 
730  C  CZ3 . TRP A 51  ? 0.1631 0.1393 0.1877 -0.0075 0.0391  -0.0214 51  TRP A CZ3 
731  C  CH2 . TRP A 51  ? 0.1574 0.1625 0.2009 -0.0098 0.0469  -0.0275 51  TRP A CH2 
742  N  N   . LEU A 52  ? 0.1315 0.1541 0.1932 0.0246  0.0090  -0.0153 52  LEU A N   
743  C  CA  . LEU A 52  ? 0.1341 0.1590 0.1899 0.0288  0.0128  -0.0257 52  LEU A CA  
744  C  C   . LEU A 52  ? 0.1365 0.1651 0.1826 0.0218  -0.0067 -0.0234 52  LEU A C   
745  O  O   . LEU A 52  ? 0.1848 0.2353 0.1961 0.0610  -0.0130 -0.0297 52  LEU A O   
746  C  CB  . LEU A 52  ? 0.1460 0.1574 0.2229 0.0266  0.0130  -0.0285 52  LEU A CB  
747  C  CG  . LEU A 52  ? 0.1377 0.1579 0.2180 0.0086  0.0254  -0.0084 52  LEU A CG  
748  C  CD1 . LEU A 52  ? 0.1653 0.2069 0.2568 -0.0112 0.0285  0.0015  52  LEU A CD1 
749  C  CD2 . LEU A 52  ? 0.1645 0.1698 0.1958 0.0134  0.0229  -0.0207 52  LEU A CD2 
761  N  N   . LEU A 53  ? 0.1341 0.1213 0.1652 0.0122  0.0101  -0.0135 53  LEU A N   
762  C  CA  . LEU A 53  ? 0.1606 0.1105 0.1609 0.0116  0.0049  -0.0089 53  LEU A CA  
763  C  C   . LEU A 53  ? 0.1503 0.1145 0.1468 0.0061  0.0065  -0.0012 53  LEU A C   
764  O  O   . LEU A 53  ? 0.2242 0.1338 0.1895 -0.0281 -0.0450 0.0200  53  LEU A O   
765  C  CB  . LEU A 53  ? 0.1582 0.1095 0.1687 -0.0033 0.0125  0.0034  53  LEU A CB  
766  C  CG  . LEU A 53  ? 0.1985 0.1171 0.1923 0.0004  0.0386  0.0036  53  LEU A CG  
767  C  CD1 . LEU A 53  ? 0.2149 0.1331 0.2109 -0.0218 0.0424  0.0082  53  LEU A CD1 
768  C  CD2 . LEU A 53  ? 0.2399 0.1625 0.2501 0.0255  0.0220  0.0426  53  LEU A CD2 
780  N  N   . ARG A 54  ? 0.1430 0.1109 0.1776 0.0162  -0.0086 -0.0115 54  ARG A N   
781  C  CA  . ARG A 54  ? 0.1376 0.1077 0.1676 0.0048  0.0013  -0.0031 54  ARG A CA  
782  C  C   . ARG A 54  ? 0.1076 0.0972 0.1592 -0.0010 0.0027  -0.0013 54  ARG A C   
783  O  O   . ARG A 54  ? 0.1347 0.1039 0.1550 0.0063  -0.0021 0.0017  54  ARG A O   
784  C  CB  . ARG A 54  ? 0.1470 0.1546 0.1808 0.0046  0.0464  0.0006  54  ARG A CB  
785  C  CG  . ARG A 54  ? 0.1573 0.1720 0.2263 0.0035  0.0401  0.0071  54  ARG A CG  
786  C  CD  . ARG A 54  ? 0.1679 0.2199 0.2484 -0.0083 0.0248  0.0311  54  ARG A CD  
787  N  NE  . ARG A 54  ? 0.1625 0.2464 0.2703 -0.0222 0.0193  0.0397  54  ARG A NE  
788  C  CZ  . ARG A 54  ? 0.1941 0.2659 0.2154 -0.0330 0.0172  0.0096  54  ARG A CZ  
789  N  NH1 . ARG A 54  ? 0.2449 0.2945 0.2706 -0.0613 -0.0167 0.0485  54  ARG A NH1 
790  N  NH2 . ARG A 54  ? 0.2257 0.2548 0.2247 -0.0436 -0.0125 -0.0007 54  ARG A NH2 
804  N  N   . GLY A 55  ? 0.1120 0.0971 0.1398 0.0031  0.0061  -0.0002 55  GLY A N   
805  C  CA  . GLY A 55  ? 0.1152 0.0971 0.1381 0.0000  0.0129  0.0053  55  GLY A CA  
806  C  C   . GLY A 55  ? 0.1071 0.1073 0.1265 0.0018  0.0093  -0.0024 55  GLY A C   
807  O  O   . GLY A 55  ? 0.1613 0.0975 0.1328 -0.0026 -0.0007 -0.0019 55  GLY A O   
811  N  N   . ILE A 56  ? 0.1012 0.0948 0.1187 0.0002  0.0059  0.0066  56  ILE A N   
812  C  CA  . ILE A 56  ? 0.1076 0.0914 0.1168 -0.0059 0.0013  0.0029  56  ILE A CA  
813  C  C   . ILE A 56  ? 0.0972 0.0830 0.1184 -0.0054 0.0018  0.0013  56  ILE A C   
814  O  O   . ILE A 56  ? 0.1077 0.0991 0.1104 -0.0005 0.0070  0.0091  56  ILE A O   
815  C  CB  . ILE A 56  ? 0.1066 0.0976 0.1246 -0.0092 0.0022  0.0038  56  ILE A CB  
816  C  CG1 . ILE A 56  ? 0.1135 0.1000 0.1192 -0.0098 0.0078  0.0014  56  ILE A CG1 
817  C  CG2 . ILE A 56  ? 0.1173 0.1217 0.1368 -0.0109 -0.0071 0.0149  56  ILE A CG2 
818  C  CD1 . ILE A 56  ? 0.1231 0.1098 0.1281 -0.0113 0.0037  0.0009  56  ILE A CD1 
830  N  N   . THR A 57  ? 0.0970 0.0922 0.1174 -0.0008 0.0016  0.0003  57  THR A N   
831  C  CA  . THR A 57  ? 0.1023 0.1011 0.1219 0.0006  -0.0009 0.0044  57  THR A CA  
832  C  C   . THR A 57  ? 0.1083 0.0917 0.1211 -0.0009 0.0009  0.0084  57  THR A C   
833  O  O   . THR A 57  ? 0.1098 0.1061 0.1311 -0.0125 0.0112  0.0006  57  THR A O   
834  C  CB  . THR A 57  ? 0.1136 0.1050 0.1362 -0.0060 -0.0094 0.0008  57  THR A CB  
835  O  OG1 . THR A 57  ? 0.1322 0.1127 0.1269 0.0013  -0.0122 0.0162  57  THR A OG1 
836  C  CG2 . THR A 57  ? 0.1222 0.1213 0.1372 -0.0044 -0.0132 -0.0013 57  THR A CG2 
844  N  N   . SER A 58  ? 0.1022 0.1016 0.1222 -0.0011 0.0022  0.0002  58  SER A N   
845  C  CA  . SER A 58  ? 0.1072 0.0897 0.1270 -0.0003 0.0023  -0.0001 58  SER A CA  
846  C  C   . SER A 58  ? 0.1055 0.0990 0.1192 0.0028  -0.0002 0.0056  58  SER A C   
847  O  O   . SER A 58  ? 0.1124 0.1055 0.1419 0.0064  -0.0032 -0.0075 58  SER A O   
848  C  CB  . SER A 58  ? 0.1048 0.0960 0.1332 0.0031  -0.0057 -0.0016 58  SER A CB  
849  O  OG  . SER A 58  ? 0.1057 0.1137 0.1341 0.0076  -0.0008 -0.0037 58  SER A OG  
855  N  N   . ASN A 59  ? 0.1145 0.0951 0.1226 0.0086  -0.0031 0.0008  59  ASN A N   
856  C  CA  . ASN A 59  ? 0.1171 0.0950 0.1297 0.0100  -0.0008 0.0027  59  ASN A CA  
857  C  C   . ASN A 59  ? 0.1145 0.0919 0.1203 0.0136  -0.0054 -0.0013 59  ASN A C   
858  O  O   . ASN A 59  ? 0.1204 0.0935 0.1280 0.0108  -0.0019 0.0027  59  ASN A O   
859  C  CB  . ASN A 59  ? 0.1219 0.0992 0.1357 0.0070  0.0000  0.0011  59  ASN A CB  
860  C  CG  . ASN A 59  ? 0.1222 0.0906 0.1342 0.0079  -0.0053 -0.0033 59  ASN A CG  
861  O  OD1 . ASN A 59  ? 0.1189 0.1124 0.1427 0.0136  -0.0026 -0.0106 59  ASN A OD1 
862  N  ND2 . ASN A 59  ? 0.1165 0.1125 0.1345 0.0105  -0.0076 0.0000  59  ASN A ND2 
869  N  N   . GLU A 60  ? 0.1275 0.0986 0.1304 0.0162  0.0072  0.0083  60  GLU A N   
870  C  CA  . GLU A 60  ? 0.1220 0.1050 0.1284 0.0188  -0.0035 -0.0005 60  GLU A CA  
871  C  C   . GLU A 60  ? 0.1051 0.0926 0.1343 0.0137  0.0059  -0.0007 60  GLU A C   
872  O  O   . GLU A 60  ? 0.1163 0.0958 0.1392 0.0062  -0.0006 0.0074  60  GLU A O   
873  C  CB  . GLU A 60  ? 0.1177 0.1157 0.1472 0.0145  -0.0059 0.0035  60  GLU A CB  
874  C  CG  . GLU A 60  ? 0.1344 0.1284 0.1651 0.0169  -0.0188 0.0018  60  GLU A CG  
875  C  CD  . GLU A 60  ? 0.1679 0.1453 0.1847 0.0274  -0.0439 -0.0135 60  GLU A CD  
876  O  OE1 . GLU A 60  ? 0.1780 0.1519 0.2155 0.0330  -0.0351 0.0058  60  GLU A OE1 
877  O  OE2 . GLU A 60  ? 0.2118 0.1621 0.2432 0.0353  -0.0918 0.0074  60  GLU A OE2 
884  N  N   . ARG A 61  ? 0.1040 0.1007 0.1339 0.0098  0.0046  0.0133  61  ARG A N   
885  C  CA  . ARG A 61  ? 0.1031 0.1062 0.1308 0.0082  0.0012  0.0183  61  ARG A CA  
886  C  C   . ARG A 61  ? 0.1015 0.1067 0.1324 0.0071  0.0022  0.0195  61  ARG A C   
887  O  O   . ARG A 61  ? 0.1233 0.1421 0.1312 -0.0034 0.0052  0.0174  61  ARG A O   
888  C  CB  . ARG A 61  ? 0.1100 0.1097 0.1601 0.0134  0.0055  0.0201  61  ARG A CB  
889  C  CG  . ARG A 61  ? 0.1162 0.1204 0.1631 0.0100  0.0093  0.0045  61  ARG A CG  
890  C  CD  . ARG A 61  ? 0.1179 0.1261 0.1797 0.0175  0.0255  -0.0173 61  ARG A CD  
891  N  NE  . ARG A 61  ? 0.1295 0.1302 0.1753 0.0196  -0.0053 0.0080  61  ARG A NE  
892  C  CZ  . ARG A 61  ? 0.1161 0.1078 0.1497 0.0197  0.0007  0.0072  61  ARG A CZ  
893  N  NH1 . ARG A 61  ? 0.1251 0.1444 0.1648 0.0048  0.0132  0.0159  61  ARG A NH1 
894  N  NH2 . ARG A 61  ? 0.1561 0.1244 0.1717 0.0111  0.0302  0.0017  61  ARG A NH2 
908  N  N   . TYR A 62  ? 0.1028 0.1100 0.1367 0.0112  0.0096  0.0138  62  TYR A N   
909  C  CA  . TYR A 62  ? 0.1099 0.1168 0.1467 0.0205  0.0132  0.0219  62  TYR A CA  
910  C  C   . TYR A 62  ? 0.1030 0.1085 0.1556 0.0086  0.0139  0.0182  62  TYR A C   
911  O  O   . TYR A 62  ? 0.1135 0.1274 0.1609 0.0216  0.0198  0.0132  62  TYR A O   
912  C  CB  . TYR A 62  ? 0.1076 0.1228 0.1522 0.0105  0.0130  0.0225  62  TYR A CB  
913  C  CG  . TYR A 62  ? 0.1091 0.1271 0.1405 0.0110  0.0154  0.0173  62  TYR A CG  
914  C  CD1 . TYR A 62  ? 0.1100 0.1363 0.1315 0.0121  0.0178  0.0162  62  TYR A CD1 
915  C  CD2 . TYR A 62  ? 0.1357 0.1234 0.1381 0.0187  0.0020  0.0144  62  TYR A CD2 
916  C  CE1 . TYR A 62  ? 0.1369 0.1355 0.1237 0.0210  0.0145  0.0208  62  TYR A CE1 
917  C  CE2 . TYR A 62  ? 0.1347 0.1182 0.1424 0.0142  0.0079  0.0191  62  TYR A CE2 
918  C  CZ  . TYR A 62  ? 0.1170 0.1186 0.1320 0.0154  0.0146  0.0288  62  TYR A CZ  
919  O  OH  . TYR A 62  ? 0.1232 0.1344 0.1362 0.0243  0.0055  0.0217  62  TYR A OH  
929  N  N   . VAL A 63  ? 0.1060 0.1262 0.1606 0.0195  0.0027  0.0185  63  VAL A N   
930  C  CA  A VAL A 63  ? 0.1053 0.1337 0.1750 0.0178  -0.0077 0.0113  63  VAL A CA  
931  C  CA  B VAL A 63  ? 0.1126 0.1266 0.1796 0.0228  -0.0101 0.0097  63  VAL A CA  
932  C  C   . VAL A 63  ? 0.0993 0.1286 0.1737 0.0133  -0.0127 0.0163  63  VAL A C   
933  O  O   . VAL A 63  ? 0.1144 0.1418 0.1995 0.0076  -0.0085 0.0316  63  VAL A O   
934  C  CB  A VAL A 63  ? 0.1139 0.1808 0.1762 0.0103  -0.0048 0.0078  63  VAL A CB  
935  C  CB  B VAL A 63  ? 0.1232 0.1378 0.1778 0.0134  -0.0020 0.0062  63  VAL A CB  
936  C  CG1 A VAL A 63  ? 0.1037 0.2290 0.1822 0.0136  -0.0205 0.0287  63  VAL A CG1 
937  C  CG1 B VAL A 63  ? 0.1355 0.1334 0.1767 0.0199  -0.0068 0.0010  63  VAL A CG1 
938  C  CG2 A VAL A 63  ? 0.1053 0.1610 0.1689 0.0012  0.0092  0.0276  63  VAL A CG2 
939  C  CG2 B VAL A 63  ? 0.1526 0.1217 0.1898 0.0249  -0.0067 0.0104  63  VAL A CG2 
958  N  N   . VAL A 64  ? 0.1112 0.1192 0.1819 0.0210  -0.0098 0.0118  64  VAL A N   
959  C  CA  . VAL A 64  ? 0.1286 0.1255 0.1759 0.0188  -0.0180 0.0020  64  VAL A CA  
960  C  C   . VAL A 64  ? 0.1241 0.1213 0.1728 0.0202  -0.0162 -0.0051 64  VAL A C   
961  O  O   . VAL A 64  ? 0.1241 0.1192 0.1727 0.0319  -0.0216 -0.0080 64  VAL A O   
962  C  CB  . VAL A 64  ? 0.1284 0.1508 0.1906 0.0189  -0.0181 -0.0081 64  VAL A CB  
963  C  CG1 . VAL A 64  ? 0.1859 0.1636 0.1822 0.0248  -0.0193 0.0012  64  VAL A CG1 
964  C  CG2 . VAL A 64  ? 0.1588 0.1772 0.1866 0.0222  -0.0056 -0.0096 64  VAL A CG2 
974  N  N   . ARG A 65  ? 0.1451 0.1192 0.1821 0.0149  -0.0363 -0.0058 65  ARG A N   
975  C  CA  . ARG A 65  ? 0.1474 0.1139 0.1958 0.0224  -0.0490 -0.0090 65  ARG A CA  
976  C  C   . ARG A 65  ? 0.1599 0.1110 0.1805 0.0337  -0.0335 -0.0162 65  ARG A C   
977  O  O   . ARG A 65  ? 0.1549 0.1170 0.1869 0.0312  -0.0386 -0.0183 65  ARG A O   
978  C  CB  . ARG A 65  ? 0.1790 0.1142 0.2301 0.0277  -0.0540 -0.0106 65  ARG A CB  
979  C  CG  . ARG A 65  ? 0.1956 0.1306 0.2391 0.0299  -0.0666 -0.0079 65  ARG A CG  
980  C  CD  . ARG A 65  ? 0.2056 0.1447 0.2491 0.0098  -0.0651 0.0029  65  ARG A CD  
981  N  NE  . ARG A 65  ? 0.2229 0.1572 0.2403 0.0324  -0.0776 -0.0227 65  ARG A NE  
982  C  CZ  . ARG A 65  ? 0.2455 0.2418 0.2376 0.0438  -0.0860 -0.0380 65  ARG A CZ  
983  N  NH1 . ARG A 65  ? 0.2760 0.3240 0.2674 -0.0049 -0.0863 -0.0660 65  ARG A NH1 
984  N  NH2 . ARG A 65  ? 0.2578 0.3668 0.2245 0.0347  -0.0548 -0.0624 65  ARG A NH2 
998  N  N   . GLU A 66  ? 0.1516 0.1408 0.1968 0.0439  -0.0237 -0.0215 66  GLU A N   
999  C  CA  . GLU A 66  ? 0.1609 0.1676 0.2247 0.0515  -0.0087 -0.0348 66  GLU A CA  
1000 C  C   . GLU A 66  ? 0.1418 0.1513 0.2063 0.0441  -0.0199 -0.0166 66  GLU A C   
1001 O  O   . GLU A 66  ? 0.1369 0.1622 0.2519 0.0442  -0.0385 -0.0036 66  GLU A O   
1002 C  CB  . GLU A 66  ? 0.2018 0.2526 0.2616 0.0725  0.0129  -0.0427 66  GLU A CB  
1003 C  CG  . GLU A 66  ? 0.2382 0.3540 0.3092 0.0531  -0.0063 -0.0495 66  GLU A CG  
1004 C  CD  . GLU A 66  ? 0.2580 0.3978 0.4095 0.0313  -0.0003 -0.0527 66  GLU A CD  
1005 O  OE1 . GLU A 66  ? 0.2814 0.4338 0.4284 0.0496  0.0534  -0.0624 66  GLU A OE1 
1006 O  OE2 . GLU A 66  ? 0.2482 0.4974 0.5100 0.0451  -0.0067 -0.0548 66  GLU A OE2 
1013 N  N   . GLU A 67  ? 0.1350 0.1334 0.1858 0.0278  -0.0228 -0.0062 67  GLU A N   
1014 C  CA  . GLU A 67  ? 0.1299 0.1424 0.1947 0.0288  -0.0181 -0.0071 67  GLU A CA  
1015 C  C   . GLU A 67  ? 0.1296 0.1176 0.1959 0.0299  -0.0298 -0.0018 67  GLU A C   
1016 O  O   . GLU A 67  ? 0.1597 0.1268 0.1894 0.0217  -0.0461 0.0002  67  GLU A O   
1017 C  CB  . GLU A 67  ? 0.1338 0.1349 0.1906 0.0174  -0.0201 0.0077  67  GLU A CB  
1018 C  CG  . GLU A 67  ? 0.1235 0.1690 0.2055 0.0172  -0.0094 0.0133  67  GLU A CG  
1019 C  CD  . GLU A 67  ? 0.1307 0.1644 0.1913 0.0122  -0.0071 0.0267  67  GLU A CD  
1020 O  OE1 . GLU A 67  ? 0.1228 0.1490 0.1891 0.0142  -0.0092 0.0200  67  GLU A OE1 
1021 O  OE2 . GLU A 67  ? 0.1381 0.2183 0.2110 -0.0001 -0.0031 0.0508  67  GLU A OE2 
1028 N  N   . LYS A 68  ? 0.1328 0.1254 0.1840 0.0318  -0.0285 -0.0082 68  LYS A N   
1029 C  CA  A LYS A 68  ? 0.1307 0.1360 0.1804 0.0305  -0.0235 -0.0058 68  LYS A CA  
1030 C  CA  B LYS A 68  ? 0.1343 0.1340 0.1919 0.0315  -0.0237 -0.0022 68  LYS A CA  
1031 C  C   . LYS A 68  ? 0.1388 0.1238 0.1839 0.0171  -0.0272 -0.0013 68  LYS A C   
1032 O  O   . LYS A 68  ? 0.1446 0.1397 0.1860 0.0109  -0.0282 -0.0064 68  LYS A O   
1033 C  CB  A LYS A 68  ? 0.1241 0.1616 0.1803 0.0329  -0.0184 -0.0228 68  LYS A CB  
1034 C  CB  B LYS A 68  ? 0.1340 0.1551 0.2200 0.0334  -0.0199 -0.0099 68  LYS A CB  
1035 C  CG  A LYS A 68  ? 0.1227 0.1725 0.1941 0.0209  -0.0204 -0.0167 68  LYS A CG  
1036 C  CG  B LYS A 68  ? 0.1389 0.1714 0.2484 0.0428  -0.0098 0.0023  68  LYS A CG  
1037 C  CD  A LYS A 68  ? 0.1164 0.2061 0.1932 0.0258  0.0004  -0.0219 68  LYS A CD  
1038 C  CD  B LYS A 68  ? 0.1496 0.2151 0.2954 0.0330  -0.0068 0.0154  68  LYS A CD  
1039 C  CE  A LYS A 68  ? 0.1273 0.2392 0.1867 0.0131  -0.0163 -0.0024 68  LYS A CE  
1040 C  CE  B LYS A 68  ? 0.1245 0.2642 0.3199 0.0400  0.0099  0.0336  68  LYS A CE  
1041 N  NZ  A LYS A 68  ? 0.1338 0.2078 0.2120 0.0194  -0.0072 0.0006  68  LYS A NZ  
1042 N  NZ  B LYS A 68  ? 0.1894 0.2699 0.3563 0.0207  0.0045  0.0299  68  LYS A NZ  
1069 N  N   . ASP A 69  ? 0.1440 0.1126 0.1879 0.0237  -0.0447 -0.0039 69  ASP A N   
1070 C  CA  . ASP A 69  ? 0.1536 0.1116 0.2063 0.0208  -0.0472 -0.0005 69  ASP A CA  
1071 C  C   . ASP A 69  ? 0.1415 0.1156 0.2049 0.0245  -0.0394 -0.0030 69  ASP A C   
1072 O  O   . ASP A 69  ? 0.1555 0.1246 0.2006 0.0169  -0.0487 0.0069  69  ASP A O   
1073 C  CB  . ASP A 69  ? 0.1885 0.1284 0.2517 0.0331  -0.0644 -0.0186 69  ASP A CB  
1074 C  CG  . ASP A 69  ? 0.2194 0.1293 0.2635 0.0247  -0.0837 -0.0224 69  ASP A CG  
1075 O  OD1 . ASP A 69  ? 0.2464 0.1408 0.2729 -0.0212 -0.0987 0.0096  69  ASP A OD1 
1076 O  OD2 . ASP A 69  ? 0.2754 0.1693 0.3348 0.0413  -0.1065 -0.0548 69  ASP A OD2 
1081 N  N   . ARG A 70  ? 0.1267 0.1248 0.2015 0.0285  -0.0262 -0.0049 70  ARG A N   
1082 C  CA  . ARG A 70  ? 0.1322 0.1467 0.2136 0.0185  -0.0295 -0.0009 70  ARG A CA  
1083 C  C   . ARG A 70  ? 0.1297 0.1242 0.1959 0.0203  -0.0344 0.0023  70  ARG A C   
1084 O  O   . ARG A 70  ? 0.1281 0.1315 0.2019 0.0133  -0.0382 0.0021  70  ARG A O   
1085 C  CB  . ARG A 70  ? 0.1384 0.1863 0.2256 0.0010  -0.0123 0.0055  70  ARG A CB  
1086 C  CG  . ARG A 70  ? 0.1673 0.2171 0.2497 -0.0065 -0.0017 -0.0136 70  ARG A CG  
1087 C  CD  . ARG A 70  ? 0.3442 0.3278 0.2972 -0.0223 0.0434  0.0143  70  ARG A CD  
1088 N  NE  . ARG A 70  ? 0.3815 0.3899 0.4296 -0.0388 -0.0490 0.0652  70  ARG A NE  
1089 C  CZ  . ARG A 70  ? 0.3812 0.4583 0.4978 -0.0078 -0.0624 0.0845  70  ARG A CZ  
1090 N  NH1 . ARG A 70  ? 0.4371 0.4432 0.6307 -0.0128 -0.0553 0.0448  70  ARG A NH1 
1091 N  NH2 . ARG A 70  ? 0.1927 0.4540 0.4537 0.0320  -0.0230 0.0564  70  ARG A NH2 
1105 N  N   . LEU A 71  ? 0.1459 0.1084 0.1850 0.0240  -0.0383 -0.0013 71  LEU A N   
1106 C  CA  . LEU A 71  ? 0.1546 0.1139 0.1801 0.0276  -0.0398 -0.0085 71  LEU A CA  
1107 C  C   . LEU A 71  ? 0.1475 0.1173 0.1771 0.0258  -0.0406 -0.0027 71  LEU A C   
1108 O  O   . LEU A 71  ? 0.1678 0.1150 0.1808 0.0270  -0.0458 -0.0065 71  LEU A O   
1109 C  CB  . LEU A 71  ? 0.1578 0.1113 0.1835 0.0382  -0.0422 -0.0055 71  LEU A CB  
1110 C  CG  . LEU A 71  ? 0.1835 0.1185 0.1956 0.0340  -0.0396 -0.0040 71  LEU A CG  
1111 C  CD1 . LEU A 71  ? 0.1865 0.1507 0.1948 0.0531  -0.0478 0.0090  71  LEU A CD1 
1112 C  CD2 . LEU A 71  ? 0.2195 0.1205 0.1954 0.0184  -0.0355 0.0029  71  LEU A CD2 
1124 N  N   . VAL A 72  ? 0.1428 0.1148 0.1782 0.0267  -0.0321 -0.0032 72  VAL A N   
1125 C  CA  . VAL A 72  ? 0.1415 0.1188 0.1808 0.0154  -0.0329 0.0004  72  VAL A CA  
1126 C  C   . VAL A 72  ? 0.1447 0.1065 0.1854 0.0179  -0.0379 0.0062  72  VAL A C   
1127 O  O   . VAL A 72  ? 0.1575 0.1242 0.1838 0.0140  -0.0282 0.0075  72  VAL A O   
1128 C  CB  . VAL A 72  ? 0.1505 0.1411 0.1935 -0.0064 -0.0328 0.0158  72  VAL A CB  
1129 C  CG1 . VAL A 72  ? 0.1495 0.1483 0.2210 -0.0088 -0.0262 0.0062  72  VAL A CG1 
1130 C  CG2 . VAL A 72  ? 0.1424 0.1738 0.2224 0.0014  -0.0384 0.0066  72  VAL A CG2 
1140 N  N   . ALA A 73  ? 0.1442 0.0994 0.1882 0.0157  -0.0323 0.0023  73  ALA A N   
1141 C  CA  . ALA A 73  ? 0.1417 0.1038 0.2123 0.0119  -0.0449 0.0082  73  ALA A CA  
1142 C  C   . ALA A 73  ? 0.1456 0.1108 0.2020 0.0076  -0.0420 0.0041  73  ALA A C   
1143 O  O   . ALA A 73  ? 0.1707 0.1202 0.2170 0.0076  -0.0649 0.0073  73  ALA A O   
1144 C  CB  . ALA A 73  ? 0.1394 0.1174 0.2163 0.0207  -0.0440 -0.0043 73  ALA A CB  
1150 N  N   . LYS A 74  ? 0.1356 0.1010 0.2081 0.0127  -0.0383 0.0053  74  LYS A N   
1151 C  CA  . LYS A 74  ? 0.1455 0.1071 0.2029 0.0028  -0.0308 0.0021  74  LYS A CA  
1152 C  C   . LYS A 74  ? 0.1493 0.1159 0.1888 0.0205  -0.0449 0.0000  74  LYS A C   
1153 O  O   . LYS A 74  ? 0.1516 0.1199 0.2057 0.0029  -0.0379 -0.0089 74  LYS A O   
1154 C  CB  . LYS A 74  ? 0.1605 0.1277 0.2168 0.0157  -0.0234 -0.0022 74  LYS A CB  
1155 C  CG  . LYS A 74  ? 0.1579 0.1362 0.2388 0.0200  -0.0174 0.0013  74  LYS A CG  
1156 C  CD  . LYS A 74  ? 0.1476 0.1393 0.2606 0.0204  0.0093  -0.0058 74  LYS A CD  
1157 C  CE  . LYS A 74  ? 0.1385 0.1657 0.2943 0.0191  0.0188  0.0057  74  LYS A CE  
1158 N  NZ  . LYS A 74  ? 0.1474 0.1861 0.3181 0.0275  0.0099  0.0188  74  LYS A NZ  
1172 N  N   . GLN A 75  ? 0.1454 0.1082 0.1795 0.0108  -0.0276 -0.0032 75  GLN A N   
1173 C  CA  . GLN A 75  ? 0.1524 0.0975 0.1974 0.0073  -0.0294 -0.0027 75  GLN A CA  
1174 C  C   . GLN A 75  ? 0.1509 0.1038 0.1846 0.0102  -0.0280 -0.0091 75  GLN A C   
1175 O  O   . GLN A 75  ? 0.1903 0.1071 0.2020 0.0189  -0.0293 -0.0017 75  GLN A O   
1176 C  CB  . GLN A 75  ? 0.1471 0.1151 0.2044 0.0163  -0.0355 -0.0087 75  GLN A CB  
1177 C  CG  . GLN A 75  ? 0.1415 0.1307 0.2403 0.0210  -0.0274 -0.0190 75  GLN A CG  
1178 C  CD  . GLN A 75  ? 0.1602 0.1271 0.2762 0.0156  -0.0472 -0.0211 75  GLN A CD  
1179 O  OE1 . GLN A 75  ? 0.1644 0.1359 0.3172 0.0113  -0.0746 -0.0153 75  GLN A OE1 
1180 N  NE2 . GLN A 75  ? 0.1555 0.1482 0.3009 0.0083  -0.0179 -0.0204 75  GLN A NE2 
1189 N  N   . PRO A 76  ? 0.1532 0.1050 0.1839 0.0149  -0.0279 -0.0058 76  PRO A N   
1190 C  CA  . PRO A 76  ? 0.1709 0.1325 0.1916 0.0016  -0.0348 -0.0092 76  PRO A CA  
1191 C  C   . PRO A 76  ? 0.1627 0.1525 0.1987 0.0137  -0.0317 -0.0052 76  PRO A C   
1192 O  O   . PRO A 76  ? 0.1537 0.1822 0.2286 0.0076  -0.0182 0.0030  76  PRO A O   
1193 C  CB  . PRO A 76  ? 0.1700 0.1371 0.1996 -0.0009 -0.0476 -0.0133 76  PRO A CB  
1194 C  CG  . PRO A 76  ? 0.1703 0.1208 0.2029 0.0080  -0.0292 -0.0091 76  PRO A CG  
1195 C  CD  . PRO A 76  ? 0.1583 0.1024 0.1881 0.0126  -0.0362 -0.0058 76  PRO A CD  
1203 N  N   . SER A 77  ? 0.1835 0.1875 0.2115 0.0050  -0.0139 -0.0074 77  SER A N   
1204 C  CA  . SER A 77  ? 0.1860 0.2143 0.2313 -0.0009 -0.0076 -0.0081 77  SER A CA  
1205 C  C   . SER A 77  ? 0.1680 0.2320 0.2028 0.0100  -0.0241 0.0124  77  SER A C   
1206 O  O   . SER A 77  ? 0.1889 0.2043 0.2080 0.0024  -0.0091 0.0058  77  SER A O   
1207 C  CB  . SER A 77  ? 0.2861 0.1900 0.2640 -0.0043 0.0147  0.0216  77  SER A CB  
1208 O  OG  . SER A 77  ? 0.4269 0.2149 0.3246 0.0174  0.0373  0.0292  77  SER A OG  
1214 N  N   . LEU A 78  ? 0.1637 0.2623 0.2367 0.0060  -0.0165 0.0266  78  LEU A N   
1215 C  CA  . LEU A 78  ? 0.1693 0.2693 0.2536 0.0255  0.0055  0.0699  78  LEU A CA  
1216 C  C   . LEU A 78  ? 0.2342 0.2614 0.2397 0.0404  0.0351  0.0644  78  LEU A C   
1217 O  O   . LEU A 78  ? 0.2956 0.2273 0.2427 0.0315  0.0398  0.0545  78  LEU A O   
1218 C  CB  . LEU A 78  ? 0.1731 0.3158 0.2646 0.0111  0.0180  0.0983  78  LEU A CB  
1219 C  CG  . LEU A 78  ? 0.1868 0.3410 0.3047 -0.0003 -0.0300 0.0679  78  LEU A CG  
1220 C  CD1 . LEU A 78  ? 0.2107 0.4339 0.4065 -0.0208 -0.0701 0.0754  78  LEU A CD1 
1221 C  CD2 . LEU A 78  ? 0.1995 0.3000 0.2451 0.0500  0.0009  0.0251  78  LEU A CD2 
1233 N  N   . GLY A 79  ? 0.2366 0.2263 0.2308 0.0528  0.0391  0.0748  79  GLY A N   
1234 C  CA  . GLY A 79  ? 0.3096 0.2022 0.2190 0.0456  0.0419  0.0612  79  GLY A CA  
1235 C  C   . GLY A 79  ? 0.3537 0.1943 0.2062 0.0724  0.0272  0.0325  79  GLY A C   
1236 O  O   . GLY A 79  ? 0.4000 0.2358 0.1941 0.0522  0.0223  0.0394  79  GLY A O   
1240 N  N   . ARG A 80  ? 0.3197 0.1787 0.1935 0.0721  0.0064  0.0285  80  ARG A N   
1241 C  CA  . ARG A 80  ? 0.3349 0.1685 0.1795 0.0705  -0.0306 0.0169  80  ARG A CA  
1242 C  C   . ARG A 80  ? 0.4003 0.1921 0.1655 0.0755  -0.0132 0.0170  80  ARG A C   
1243 O  O   . ARG A 80  ? 0.3649 0.1829 0.1864 0.0883  -0.0172 0.0035  80  ARG A O   
1244 C  CB  . ARG A 80  ? 0.2696 0.1410 0.2096 0.0249  -0.0404 0.0117  80  ARG A CB  
1245 C  CG  . ARG A 80  ? 0.2149 0.1403 0.1956 0.0173  -0.0274 0.0016  80  ARG A CG  
1246 C  CD  . ARG A 80  ? 0.2008 0.1284 0.2035 0.0197  -0.0368 0.0065  80  ARG A CD  
1247 N  NE  . ARG A 80  ? 0.1771 0.1349 0.1816 0.0067  -0.0293 -0.0089 80  ARG A NE  
1248 C  CZ  . ARG A 80  ? 0.1494 0.1324 0.1874 0.0101  -0.0336 -0.0142 80  ARG A CZ  
1249 N  NH1 . ARG A 80  ? 0.1516 0.1328 0.2096 0.0029  -0.0302 -0.0207 80  ARG A NH1 
1250 N  NH2 . ARG A 80  ? 0.1468 0.1336 0.1911 0.0051  -0.0240 -0.0119 80  ARG A NH2 
1264 N  N   . ALA A 81  ? 0.5150 0.1971 0.1823 0.0871  -0.0499 0.0059  81  ALA A N   
1265 C  CA  . ALA A 81  ? 0.5406 0.2405 0.1833 0.0890  -0.0562 -0.0026 81  ALA A CA  
1266 C  C   . ALA A 81  ? 0.4627 0.2415 0.1942 0.1110  -0.0996 -0.0242 81  ALA A C   
1267 O  O   . ALA A 81  ? 0.4899 0.2233 0.2317 0.1061  -0.0837 -0.0447 81  ALA A O   
1268 C  CB  . ALA A 81  ? 0.6139 0.2659 0.1984 0.0587  -0.0755 0.0151  81  ALA A CB  
1274 N  N   . GLU A 82  ? 0.3806 0.2403 0.2443 0.1212  -0.1332 -0.0489 82  GLU A N   
1275 C  CA  . GLU A 82  ? 0.3199 0.2470 0.2584 0.1071  -0.1200 -0.0573 82  GLU A CA  
1276 C  C   . GLU A 82  ? 0.2549 0.2076 0.2386 0.0899  -0.0792 -0.0529 82  GLU A C   
1277 O  O   . GLU A 82  ? 0.1936 0.2312 0.2636 0.0524  -0.0931 -0.0742 82  GLU A O   
1278 C  CB  . GLU A 82  ? 0.3092 0.2920 0.3276 0.1327  -0.1498 -0.0923 82  GLU A CB  
1279 C  CG  . GLU A 82  ? 0.3332 0.2755 0.3864 0.1240  -0.1210 -0.1094 82  GLU A CG  
1280 C  CD  . GLU A 82  ? 0.3481 0.2850 0.3549 0.1026  -0.1427 -0.0912 82  GLU A CD  
1281 O  OE1 . GLU A 82  ? 0.3384 0.3048 0.3675 0.0474  -0.1173 -0.1156 82  GLU A OE1 
1282 O  OE2 . GLU A 82  ? 0.3797 0.3348 0.3804 0.1471  -0.1466 -0.0941 82  GLU A OE2 
1289 N  N   . ALA A 83  ? 0.2324 0.1601 0.1952 0.0545  -0.0617 -0.0295 83  ALA A N   
1290 C  CA  . ALA A 83  ? 0.1946 0.1383 0.1887 0.0335  -0.0546 -0.0190 83  ALA A CA  
1291 C  C   . ALA A 83  ? 0.1607 0.1265 0.1815 0.0160  -0.0498 -0.0130 83  ALA A C   
1292 O  O   . ALA A 83  ? 0.1630 0.1383 0.2221 -0.0184 -0.0426 -0.0124 83  ALA A O   
1293 C  CB  . ALA A 83  ? 0.2131 0.1378 0.1971 0.0290  -0.0451 -0.0223 83  ALA A CB  
1299 N  N   . THR A 84  ? 0.1459 0.1190 0.1992 0.0066  -0.0381 -0.0186 84  THR A N   
1300 C  CA  . THR A 84  ? 0.1368 0.1227 0.1967 0.0073  -0.0235 -0.0258 84  THR A CA  
1301 C  C   . THR A 84  ? 0.1156 0.1118 0.1881 -0.0010 -0.0205 -0.0219 84  THR A C   
1302 O  O   . THR A 84  ? 0.1243 0.1446 0.1796 0.0084  -0.0049 -0.0150 84  THR A O   
1303 C  CB  . THR A 84  ? 0.1346 0.1338 0.1888 -0.0056 -0.0279 -0.0218 84  THR A CB  
1304 O  OG1 . THR A 84  ? 0.1323 0.1350 0.1971 -0.0104 -0.0364 -0.0170 84  THR A OG1 
1305 C  CG2 . THR A 84  ? 0.1734 0.1472 0.1962 0.0043  -0.0397 -0.0109 84  THR A CG2 
1313 N  N   . CYS A 85  ? 0.1146 0.1202 0.1875 -0.0001 -0.0218 -0.0156 85  CYS A N   
1314 C  CA  . CYS A 85  ? 0.1087 0.1114 0.1860 0.0023  -0.0171 -0.0212 85  CYS A CA  
1315 C  C   . CYS A 85  ? 0.1132 0.1165 0.1794 0.0062  -0.0114 -0.0089 85  CYS A C   
1316 O  O   . CYS A 85  ? 0.1142 0.1130 0.1901 0.0073  -0.0202 -0.0147 85  CYS A O   
1317 C  CB  . CYS A 85  ? 0.1288 0.1308 0.1848 0.0029  -0.0062 -0.0156 85  CYS A CB  
1318 S  SG  . CYS A 85  ? 0.1351 0.1676 0.2207 -0.0239 -0.0053 -0.0223 85  CYS A SG  
1324 N  N   . ALA A 86  ? 0.1172 0.1156 0.1841 0.0127  -0.0219 -0.0157 86  ALA A N   
1325 C  CA  . ALA A 86  ? 0.1138 0.1134 0.1782 0.0070  -0.0132 -0.0221 86  ALA A CA  
1326 C  C   . ALA A 86  ? 0.0972 0.1040 0.1706 0.0000  -0.0039 -0.0102 86  ALA A C   
1327 O  O   . ALA A 86  ? 0.1165 0.1069 0.1793 0.0037  -0.0063 -0.0129 86  ALA A O   
1328 C  CB  . ALA A 86  ? 0.1267 0.1245 0.1789 -0.0003 -0.0188 -0.0081 86  ALA A CB  
1334 N  N   . ALA A 87  ? 0.0950 0.1014 0.1749 0.0041  -0.0082 -0.0107 87  ALA A N   
1335 C  CA  . ALA A 87  ? 0.1099 0.0884 0.1695 0.0031  -0.0086 -0.0043 87  ALA A CA  
1336 C  C   . ALA A 87  ? 0.0976 0.0952 0.1627 0.0052  -0.0026 -0.0006 87  ALA A C   
1337 O  O   . ALA A 87  ? 0.0947 0.0902 0.1868 0.0000  -0.0108 -0.0045 87  ALA A O   
1338 C  CB  . ALA A 87  ? 0.1072 0.1051 0.1817 -0.0036 0.0026  -0.0031 87  ALA A CB  
1344 N  N   . LEU A 88  ? 0.0902 0.0925 0.1589 0.0063  -0.0019 0.0001  88  LEU A N   
1345 C  CA  . LEU A 88  ? 0.0927 0.0969 0.1456 0.0019  0.0041  -0.0015 88  LEU A CA  
1346 C  C   . LEU A 88  ? 0.0929 0.0927 0.1555 0.0029  0.0068  0.0020  88  LEU A C   
1347 O  O   . LEU A 88  ? 0.1071 0.0865 0.1629 0.0029  0.0068  0.0047  88  LEU A O   
1348 C  CB  . LEU A 88  ? 0.0984 0.1063 0.1502 0.0023  0.0046  -0.0014 88  LEU A CB  
1349 C  CG  . LEU A 88  ? 0.1005 0.1270 0.1593 0.0053  0.0124  0.0048  88  LEU A CG  
1350 C  CD1 . LEU A 88  ? 0.1108 0.1339 0.1710 -0.0121 0.0139  -0.0098 88  LEU A CD1 
1351 C  CD2 . LEU A 88  ? 0.1109 0.1394 0.1941 -0.0001 0.0243  0.0074  88  LEU A CD2 
1363 N  N   . ILE A 89  ? 0.0913 0.0928 0.1479 0.0042  0.0025  0.0134  89  ILE A N   
1364 C  CA  . ILE A 89  ? 0.0985 0.0975 0.1486 0.0034  0.0067  0.0118  89  ILE A CA  
1365 C  C   . ILE A 89  ? 0.0966 0.0871 0.1441 0.0047  0.0090  0.0158  89  ILE A C   
1366 O  O   . ILE A 89  ? 0.1016 0.0995 0.1498 0.0066  0.0022  0.0100  89  ILE A O   
1367 C  CB  . ILE A 89  ? 0.0959 0.1002 0.1544 0.0056  0.0133  0.0057  89  ILE A CB  
1368 C  CG1 . ILE A 89  ? 0.1021 0.1219 0.1692 0.0050  0.0115  0.0098  89  ILE A CG1 
1369 C  CG2 . ILE A 89  ? 0.1141 0.1257 0.1541 -0.0002 0.0148  0.0106  89  ILE A CG2 
1370 C  CD1 . ILE A 89  ? 0.0943 0.1338 0.1841 0.0021  0.0108  0.0054  89  ILE A CD1 
1382 N  N   . PRO A 90  ? 0.0944 0.0905 0.1498 0.0041  0.0046  0.0092  90  PRO A N   
1383 C  CA  . PRO A 90  ? 0.0933 0.0958 0.1586 0.0001  0.0034  0.0113  90  PRO A CA  
1384 C  C   . PRO A 90  ? 0.0932 0.1003 0.1625 0.0013  0.0008  0.0222  90  PRO A C   
1385 O  O   . PRO A 90  ? 0.1220 0.1020 0.1725 -0.0089 -0.0059 0.0270  90  PRO A O   
1386 C  CB  . PRO A 90  ? 0.0935 0.1098 0.1718 0.0017  0.0067  0.0021  90  PRO A CB  
1387 C  CG  . PRO A 90  ? 0.1052 0.1225 0.1730 0.0064  0.0044  -0.0085 90  PRO A CG  
1388 C  CD  . PRO A 90  ? 0.0968 0.0949 0.1671 0.0053  0.0064  0.0002  90  PRO A CD  
1396 N  N   . ILE A 91  ? 0.1038 0.0963 0.1515 0.0025  0.0055  0.0221  91  ILE A N   
1397 C  CA  . ILE A 91  ? 0.1043 0.1111 0.1508 -0.0016 0.0066  0.0220  91  ILE A CA  
1398 C  C   . ILE A 91  ? 0.1096 0.0984 0.1436 0.0039  0.0027  0.0183  91  ILE A C   
1399 O  O   . ILE A 91  ? 0.1097 0.0974 0.1559 0.0078  0.0066  0.0256  91  ILE A O   
1400 C  CB  . ILE A 91  ? 0.1021 0.1300 0.1580 0.0164  0.0097  0.0275  91  ILE A CB  
1401 C  CG1 . ILE A 91  ? 0.1138 0.1924 0.1821 0.0076  0.0047  0.0232  91  ILE A CG1 
1402 C  CG2 . ILE A 91  ? 0.1181 0.1448 0.1669 0.0203  0.0148  0.0269  91  ILE A CG2 
1403 C  CD1 . ILE A 91  ? 0.1605 0.1578 0.2180 0.0277  0.0102  0.0141  91  ILE A CD1 
1415 N  N   . ARG A 92  ? 0.1028 0.1056 0.1531 0.0067  0.0019  0.0230  92  ARG A N   
1416 C  CA  . ARG A 92  ? 0.0996 0.1146 0.1573 0.0101  0.0082  0.0249  92  ARG A CA  
1417 C  C   . ARG A 92  ? 0.1138 0.1053 0.1535 0.0113  0.0082  0.0320  92  ARG A C   
1418 O  O   . ARG A 92  ? 0.1262 0.1263 0.1689 0.0025  0.0116  0.0358  92  ARG A O   
1419 C  CB  . ARG A 92  ? 0.1215 0.1172 0.1552 0.0151  0.0045  0.0300  92  ARG A CB  
1420 C  CG  . ARG A 92  ? 0.1010 0.1395 0.1931 0.0245  -0.0043 0.0266  92  ARG A CG  
1421 C  CD  . ARG A 92  ? 0.1325 0.1677 0.2186 0.0296  -0.0207 0.0278  92  ARG A CD  
1422 N  NE  . ARG A 92  ? 0.1662 0.1618 0.2362 0.0275  -0.0297 0.0117  92  ARG A NE  
1423 C  CZ  . ARG A 92  ? 0.1826 0.1969 0.2529 0.0528  -0.0407 0.0120  92  ARG A CZ  
1424 N  NH1 . ARG A 92  ? 0.2256 0.2401 0.2991 0.1102  -0.0124 0.0266  92  ARG A NH1 
1425 N  NH2 . ARG A 92  ? 0.2054 0.1948 0.2955 0.0304  -0.0410 0.0492  92  ARG A NH2 
1439 N  N   . LYS A 93  ? 0.1220 0.1196 0.1379 0.0128  0.0045  0.0243  93  LYS A N   
1440 C  CA  . LYS A 93  ? 0.1289 0.1410 0.1343 0.0114  0.0098  0.0259  93  LYS A CA  
1441 C  C   . LYS A 93  ? 0.1307 0.1404 0.1522 0.0093  0.0123  0.0324  93  LYS A C   
1442 O  O   . LYS A 93  ? 0.1363 0.1591 0.1581 0.0133  0.0136  0.0393  93  LYS A O   
1443 C  CB  . LYS A 93  ? 0.1332 0.1332 0.1516 0.0111  0.0109  0.0242  93  LYS A CB  
1444 C  CG  . LYS A 93  ? 0.1346 0.1422 0.1642 0.0165  0.0003  0.0179  93  LYS A CG  
1445 C  CD  . LYS A 93  ? 0.1308 0.1373 0.1634 0.0217  0.0150  0.0174  93  LYS A CD  
1446 C  CE  . LYS A 93  ? 0.1279 0.1376 0.1836 0.0167  0.0114  0.0254  93  LYS A CE  
1447 N  NZ  . LYS A 93  ? 0.1200 0.1525 0.1634 0.0194  0.0174  0.0206  93  LYS A NZ  
1461 N  N   . ASN A 94  ? 0.1438 0.1663 0.1399 0.0202  0.0123  0.0405  94  ASN A N   
1462 C  CA  . ASN A 94  ? 0.1508 0.1781 0.1612 0.0358  0.0072  0.0487  94  ASN A CA  
1463 C  C   . ASN A 94  ? 0.1474 0.1842 0.1490 0.0360  0.0063  0.0570  94  ASN A C   
1464 O  O   . ASN A 94  ? 0.1475 0.1847 0.1564 0.0324  0.0018  0.0540  94  ASN A O   
1465 C  CB  . ASN A 94  ? 0.1863 0.1801 0.1671 0.0177  0.0155  0.0578  94  ASN A CB  
1466 C  CG  . ASN A 94  ? 0.1868 0.1798 0.1589 0.0117  0.0222  0.0613  94  ASN A CG  
1467 O  OD1 . ASN A 94  ? 0.2114 0.1975 0.1992 -0.0154 0.0363  0.0347  94  ASN A OD1 
1468 N  ND2 . ASN A 94  ? 0.1885 0.1922 0.1893 0.0180  0.0255  0.0575  94  ASN A ND2 
1475 N  N   . PRO A 95  ? 0.1472 0.1864 0.1769 0.0361  -0.0127 0.0573  95  PRO A N   
1476 C  CA  . PRO A 95  ? 0.1371 0.1981 0.1943 0.0302  -0.0137 0.0584  95  PRO A CA  
1477 C  C   . PRO A 95  ? 0.1504 0.1981 0.1820 0.0381  -0.0190 0.0643  95  PRO A C   
1478 O  O   . PRO A 95  ? 0.1906 0.1981 0.2026 0.0313  -0.0260 0.0523  95  PRO A O   
1479 C  CB  . PRO A 95  ? 0.1573 0.2196 0.2216 0.0423  -0.0193 0.0434  95  PRO A CB  
1480 C  CG  . PRO A 95  ? 0.1645 0.2347 0.2141 0.0611  -0.0176 0.0377  95  PRO A CG  
1481 C  CD  . PRO A 95  ? 0.1601 0.1842 0.2175 0.0431  -0.0079 0.0557  95  PRO A CD  
1489 N  N   . SER A 96  ? 0.1771 0.1822 0.1739 0.0419  -0.0055 0.0663  96  SER A N   
1490 C  CA  . SER A 96  ? 0.2193 0.1931 0.1620 0.0355  -0.0111 0.0561  96  SER A CA  
1491 C  C   . SER A 96  ? 0.1752 0.1819 0.1639 0.0293  -0.0184 0.0494  96  SER A C   
1492 O  O   . SER A 96  ? 0.1951 0.1927 0.1612 0.0202  -0.0200 0.0450  96  SER A O   
1493 C  CB  . SER A 96  ? 0.2988 0.1927 0.1810 0.0565  0.0313  0.0752  96  SER A CB  
1494 O  OG  . SER A 96  ? 0.3678 0.2692 0.2712 0.0486  0.0069  0.1057  96  SER A OG  
1500 N  N   . TRP A 97  ? 0.1573 0.1608 0.1598 0.0144  -0.0099 0.0509  97  TRP A N   
1501 C  CA  . TRP A 97  ? 0.1394 0.1541 0.1566 0.0219  -0.0035 0.0442  97  TRP A CA  
1502 C  C   . TRP A 97  ? 0.1361 0.1522 0.1361 0.0209  -0.0069 0.0353  97  TRP A C   
1503 O  O   . TRP A 97  ? 0.1410 0.1532 0.1491 0.0241  -0.0034 0.0298  97  TRP A O   
1504 C  CB  . TRP A 97  ? 0.1460 0.1414 0.1566 0.0199  -0.0007 0.0358  97  TRP A CB  
1505 C  CG  . TRP A 97  ? 0.1185 0.1341 0.1359 0.0086  0.0045  0.0227  97  TRP A CG  
1506 C  CD1 . TRP A 97  ? 0.1253 0.1316 0.1428 0.0167  0.0021  0.0235  97  TRP A CD1 
1507 C  CD2 . TRP A 97  ? 0.1272 0.1369 0.1404 0.0098  0.0094  0.0220  97  TRP A CD2 
1508 N  NE1 . TRP A 97  ? 0.1309 0.1317 0.1363 0.0207  0.0046  0.0271  97  TRP A NE1 
1509 C  CE2 . TRP A 97  ? 0.1139 0.1284 0.1365 0.0111  0.0058  0.0209  97  TRP A CE2 
1510 C  CE3 . TRP A 97  ? 0.1391 0.1570 0.1690 -0.0039 0.0179  0.0293  97  TRP A CE3 
1511 C  CZ2 . TRP A 97  ? 0.1221 0.1377 0.1543 0.0141  0.0049  0.0139  97  TRP A CZ2 
1512 C  CZ3 . TRP A 97  ? 0.1293 0.1684 0.1832 -0.0009 0.0234  0.0236  97  TRP A CZ3 
1513 C  CH2 . TRP A 97  ? 0.1326 0.1543 0.1654 0.0103  0.0177  0.0107  97  TRP A CH2 
1524 N  N   . TRP A 98  ? 0.1379 0.1501 0.1379 0.0209  -0.0013 0.0269  98  TRP A N   
1525 C  CA  . TRP A 98  ? 0.1307 0.1602 0.1384 0.0210  0.0019  0.0331  98  TRP A CA  
1526 C  C   . TRP A 98  ? 0.1479 0.1613 0.1371 0.0191  -0.0043 0.0246  98  TRP A C   
1527 O  O   . TRP A 98  ? 0.1763 0.1771 0.1586 -0.0031 -0.0121 0.0301  98  TRP A O   
1528 C  CB  . TRP A 98  ? 0.1385 0.1497 0.1447 0.0191  0.0044  0.0248  98  TRP A CB  
1529 C  CG  . TRP A 98  ? 0.1316 0.1347 0.1370 0.0234  0.0049  0.0273  98  TRP A CG  
1530 C  CD1 . TRP A 98  ? 0.1433 0.1410 0.1470 0.0255  0.0098  0.0392  98  TRP A CD1 
1531 C  CD2 . TRP A 98  ? 0.1140 0.1339 0.1407 0.0092  0.0067  0.0310  98  TRP A CD2 
1532 N  NE1 . TRP A 98  ? 0.1321 0.1215 0.1480 0.0168  0.0069  0.0180  98  TRP A NE1 
1533 C  CE2 . TRP A 98  ? 0.1117 0.1268 0.1484 0.0091  0.0119  0.0306  98  TRP A CE2 
1534 C  CE3 . TRP A 98  ? 0.1340 0.1273 0.1609 0.0010  -0.0180 0.0212  98  TRP A CE3 
1535 C  CZ2 . TRP A 98  ? 0.1206 0.1304 0.1506 -0.0014 -0.0011 0.0211  98  TRP A CZ2 
1536 C  CZ3 . TRP A 98  ? 0.1639 0.1247 0.1753 0.0044  -0.0338 0.0199  98  TRP A CZ3 
1537 C  CH2 . TRP A 98  ? 0.1546 0.1337 0.1644 0.0035  -0.0320 0.0309  98  TRP A CH2 
1548 N  N   . GLY A 99  ? 0.1376 0.1778 0.1374 0.0233  -0.0035 0.0214  99  GLY A N   
1549 C  CA  . GLY A 99  ? 0.1480 0.1800 0.1517 0.0310  -0.0035 0.0202  99  GLY A CA  
1550 C  C   . GLY A 99  ? 0.1523 0.1832 0.1400 0.0294  -0.0040 0.0152  99  GLY A C   
1551 O  O   . GLY A 99  ? 0.1675 0.2259 0.1574 0.0231  -0.0131 -0.0016 99  GLY A O   
1555 N  N   . LEU A 100 ? 0.1411 0.1679 0.1365 0.0300  0.0023  0.0211  100 LEU A N   
1556 C  CA  . LEU A 100 ? 0.1474 0.1742 0.1321 0.0325  0.0081  0.0306  100 LEU A CA  
1557 C  C   . LEU A 100 ? 0.1313 0.1774 0.1275 0.0291  0.0073  0.0311  100 LEU A C   
1558 O  O   . LEU A 100 ? 0.1454 0.1757 0.1303 0.0205  0.0103  0.0296  100 LEU A O   
1559 C  CB  . LEU A 100 ? 0.1488 0.1784 0.1319 0.0204  0.0039  0.0308  100 LEU A CB  
1560 C  CG  . LEU A 100 ? 0.1641 0.2047 0.1473 0.0099  0.0047  0.0319  100 LEU A CG  
1561 C  CD1 . LEU A 100 ? 0.1717 0.1974 0.1701 0.0099  0.0167  0.0336  100 LEU A CD1 
1562 C  CD2 . LEU A 100 ? 0.2028 0.2353 0.1573 0.0029  -0.0073 0.0527  100 LEU A CD2 
1574 N  N   . SER A 101 ? 0.1383 0.1815 0.1285 0.0173  0.0014  0.0265  101 SER A N   
1575 C  CA  A SER A 101 ? 0.1345 0.1782 0.1360 0.0193  -0.0014 0.0237  101 SER A CA  
1576 C  CA  B SER A 101 ? 0.1398 0.1742 0.1260 0.0201  0.0063  0.0257  101 SER A CA  
1577 C  C   . SER A 101 ? 0.1335 0.1669 0.1229 0.0208  0.0104  0.0121  101 SER A C   
1578 O  O   . SER A 101 ? 0.1484 0.1602 0.1339 0.0188  0.0039  0.0192  101 SER A O   
1579 C  CB  A SER A 101 ? 0.1835 0.1924 0.1531 0.0265  -0.0179 0.0133  101 SER A CB  
1580 C  CB  B SER A 101 ? 0.1897 0.1723 0.1302 0.0263  0.0042  0.0252  101 SER A CB  
1581 O  OG  A SER A 101 ? 0.2168 0.2470 0.2225 0.0241  -0.0578 -0.0014 101 SER A OG  
1582 O  OG  B SER A 101 ? 0.2400 0.1885 0.1359 0.0205  0.0278  0.0250  101 SER A OG  
1593 N  N   . GLN A 102 ? 0.1314 0.1601 0.1285 0.0166  0.0075  0.0159  102 GLN A N   
1594 C  CA  . GLN A 102 ? 0.1322 0.1615 0.1299 0.0112  0.0058  0.0151  102 GLN A CA  
1595 C  C   . GLN A 102 ? 0.1262 0.1713 0.1274 0.0136  0.0075  0.0188  102 GLN A C   
1596 O  O   . GLN A 102 ? 0.1336 0.1673 0.1357 0.0071  0.0133  0.0156  102 GLN A O   
1597 C  CB  . GLN A 102 ? 0.1349 0.1509 0.1352 0.0130  0.0100  0.0173  102 GLN A CB  
1598 C  CG  . GLN A 102 ? 0.1367 0.1441 0.1319 0.0079  0.0041  0.0059  102 GLN A CG  
1599 C  CD  . GLN A 102 ? 0.1415 0.1327 0.1235 0.0221  0.0158  0.0168  102 GLN A CD  
1600 O  OE1 . GLN A 102 ? 0.1486 0.1427 0.1305 0.0216  0.0142  0.0097  102 GLN A OE1 
1601 N  NE2 . GLN A 102 ? 0.1449 0.1575 0.1289 0.0241  0.0062  0.0175  102 GLN A NE2 
1610 N  N   . ASP A 103 ? 0.1359 0.1807 0.1396 0.0186  0.0000  0.0033  103 ASP A N   
1611 C  CA  . ASP A 103 ? 0.1449 0.1904 0.1336 0.0262  0.0134  0.0026  103 ASP A CA  
1612 C  C   . ASP A 103 ? 0.1384 0.1919 0.1225 0.0242  0.0153  0.0060  103 ASP A C   
1613 O  O   . ASP A 103 ? 0.1414 0.1944 0.1426 0.0244  0.0156  0.0139  103 ASP A O   
1614 C  CB  . ASP A 103 ? 0.1628 0.2090 0.1380 0.0244  0.0117  -0.0064 103 ASP A CB  
1615 C  CG  . ASP A 103 ? 0.1682 0.2318 0.1381 0.0133  0.0224  0.0035  103 ASP A CG  
1616 O  OD1 . ASP A 103 ? 0.1642 0.2265 0.1437 0.0154  0.0000  0.0050  103 ASP A OD1 
1617 O  OD2 . ASP A 103 ? 0.2318 0.2846 0.1479 0.0215  0.0172  0.0040  103 ASP A OD2 
1622 N  N   . GLU A 104 ? 0.1422 0.1869 0.1329 0.0190  0.0184  0.0119  104 GLU A N   
1623 C  CA  . GLU A 104 ? 0.1518 0.1981 0.1373 0.0167  0.0238  0.0265  104 GLU A CA  
1624 C  C   . GLU A 104 ? 0.1361 0.1727 0.1412 0.0104  0.0242  0.0219  104 GLU A C   
1625 O  O   . GLU A 104 ? 0.1489 0.1910 0.1394 0.0070  0.0248  0.0218  104 GLU A O   
1626 C  CB  . GLU A 104 ? 0.1696 0.2104 0.1326 0.0214  0.0136  0.0363  104 GLU A CB  
1627 C  CG  . GLU A 104 ? 0.1804 0.2455 0.1443 0.0301  0.0165  0.0354  104 GLU A CG  
1628 C  CD  . GLU A 104 ? 0.1845 0.2508 0.1386 0.0189  0.0105  0.0527  104 GLU A CD  
1629 O  OE1 . GLU A 104 ? 0.1969 0.2702 0.1533 0.0415  0.0175  0.0429  104 GLU A OE1 
1630 O  OE2 . GLU A 104 ? 0.2058 0.2985 0.1533 0.0239  -0.0021 0.0532  104 GLU A OE2 
1637 N  N   . ARG A 105 ? 0.1401 0.1600 0.1263 0.0145  0.0201  0.0225  105 ARG A N   
1638 C  CA  . ARG A 105 ? 0.1320 0.1660 0.1268 0.0196  0.0178  0.0159  105 ARG A CA  
1639 C  C   . ARG A 105 ? 0.1221 0.1506 0.1419 0.0144  0.0285  0.0187  105 ARG A C   
1640 O  O   . ARG A 105 ? 0.1178 0.1498 0.1521 0.0115  0.0256  0.0145  105 ARG A O   
1641 C  CB  . ARG A 105 ? 0.1151 0.1611 0.1211 0.0160  0.0149  0.0206  105 ARG A CB  
1642 C  CG  . ARG A 105 ? 0.1237 0.1463 0.1389 0.0104  0.0152  0.0212  105 ARG A CG  
1643 C  CD  . ARG A 105 ? 0.1186 0.1320 0.1345 0.0095  0.0108  0.0247  105 ARG A CD  
1644 N  NE  . ARG A 105 ? 0.1219 0.1387 0.1332 0.0114  0.0069  0.0259  105 ARG A NE  
1645 C  CZ  . ARG A 105 ? 0.1263 0.1381 0.1250 0.0124  0.0151  0.0188  105 ARG A CZ  
1646 N  NH1 . ARG A 105 ? 0.1325 0.1484 0.1259 0.0186  0.0156  0.0299  105 ARG A NH1 
1647 N  NH2 . ARG A 105 ? 0.1515 0.1548 0.1346 -0.0094 -0.0022 0.0303  105 ARG A NH2 
1661 N  N   . ARG A 106 ? 0.1216 0.1563 0.1373 0.0187  0.0206  0.0141  106 ARG A N   
1662 C  CA  . ARG A 106 ? 0.1197 0.1580 0.1425 0.0123  0.0163  0.0117  106 ARG A CA  
1663 C  C   . ARG A 106 ? 0.1291 0.1529 0.1379 0.0228  0.0168  0.0057  106 ARG A C   
1664 O  O   . ARG A 106 ? 0.1276 0.1686 0.1447 0.0134  0.0222  0.0149  106 ARG A O   
1665 C  CB  . ARG A 106 ? 0.1283 0.1555 0.1395 0.0099  0.0100  0.0105  106 ARG A CB  
1666 C  CG  . ARG A 106 ? 0.1313 0.1617 0.1518 0.0088  0.0192  0.0097  106 ARG A CG  
1667 C  CD  . ARG A 106 ? 0.1301 0.1713 0.1548 0.0198  0.0161  0.0196  106 ARG A CD  
1668 N  NE  . ARG A 106 ? 0.1218 0.1818 0.1588 0.0288  0.0143  0.0063  106 ARG A NE  
1669 C  CZ  . ARG A 106 ? 0.1239 0.1574 0.1713 0.0258  0.0086  0.0113  106 ARG A CZ  
1670 N  NH1 . ARG A 106 ? 0.1298 0.1687 0.1591 0.0163  0.0120  0.0220  106 ARG A NH1 
1671 N  NH2 . ARG A 106 ? 0.1252 0.1838 0.1762 0.0284  0.0199  0.0197  106 ARG A NH2 
1685 N  N   . LYS A 107 ? 0.1341 0.1731 0.1407 0.0159  0.0270  0.0114  107 LYS A N   
1686 C  CA  . LYS A 107 ? 0.1421 0.1943 0.1470 0.0180  0.0416  0.0202  107 LYS A CA  
1687 C  C   . LYS A 107 ? 0.1366 0.1916 0.1500 0.0118  0.0405  0.0296  107 LYS A C   
1688 O  O   . LYS A 107 ? 0.1368 0.2007 0.1691 0.0032  0.0382  0.0252  107 LYS A O   
1689 C  CB  . LYS A 107 ? 0.1687 0.2268 0.1453 0.0025  0.0375  0.0128  107 LYS A CB  
1690 C  CG  . LYS A 107 ? 0.2333 0.3039 0.1475 -0.0186 0.0573  0.0359  107 LYS A CG  
1691 C  CD  . LYS A 107 ? 0.3123 0.3863 0.1725 -0.0481 0.0523  0.0286  107 LYS A CD  
1692 C  CE  . LYS A 107 ? 0.3845 0.4851 0.2161 -0.0404 0.1037  0.0441  107 LYS A CE  
1693 N  NZ  . LYS A 107 ? 0.4637 0.5814 0.2508 -0.0515 0.0804  0.0785  107 LYS A NZ  
1707 N  N   . ILE A 108 ? 0.1302 0.1742 0.1516 0.0125  0.0293  0.0244  108 ILE A N   
1708 C  CA  . ILE A 108 ? 0.1348 0.1843 0.1556 0.0024  0.0375  0.0253  108 ILE A CA  
1709 C  C   . ILE A 108 ? 0.1293 0.1726 0.1634 0.0033  0.0336  0.0122  108 ILE A C   
1710 O  O   . ILE A 108 ? 0.1253 0.1816 0.1765 -0.0050 0.0271  0.0213  108 ILE A O   
1711 C  CB  . ILE A 108 ? 0.1465 0.1822 0.1633 0.0048  0.0299  0.0372  108 ILE A CB  
1712 C  CG1 . ILE A 108 ? 0.1696 0.2004 0.1775 0.0177  0.0108  0.0505  108 ILE A CG1 
1713 C  CG2 . ILE A 108 ? 0.1622 0.1753 0.2003 0.0129  0.0214  0.0410  108 ILE A CG2 
1714 C  CD1 . ILE A 108 ? 0.1902 0.1961 0.2024 0.0227  0.0192  0.0354  108 ILE A CD1 
1726 N  N   . PHE A 109 ? 0.1210 0.1605 0.1489 0.0076  0.0206  0.0177  109 PHE A N   
1727 C  CA  . PHE A 109 ? 0.1225 0.1513 0.1538 0.0067  0.0219  0.0269  109 PHE A CA  
1728 C  C   . PHE A 109 ? 0.1222 0.1654 0.1562 0.0101  0.0236  0.0193  109 PHE A C   
1729 O  O   . PHE A 109 ? 0.1291 0.1702 0.1571 0.0018  0.0238  0.0197  109 PHE A O   
1730 C  CB  . PHE A 109 ? 0.1248 0.1855 0.1476 -0.0111 0.0184  0.0284  109 PHE A CB  
1731 C  CG  . PHE A 109 ? 0.1213 0.1762 0.1588 -0.0134 0.0210  0.0193  109 PHE A CG  
1732 C  CD1 . PHE A 109 ? 0.1392 0.1959 0.1700 -0.0240 0.0293  0.0052  109 PHE A CD1 
1733 C  CD2 . PHE A 109 ? 0.1474 0.1673 0.1820 -0.0228 0.0139  0.0214  109 PHE A CD2 
1734 C  CE1 . PHE A 109 ? 0.1516 0.2453 0.1771 -0.0489 0.0276  -0.0097 109 PHE A CE1 
1735 C  CE2 . PHE A 109 ? 0.1452 0.2138 0.2128 -0.0397 -0.0063 0.0513  109 PHE A CE2 
1736 C  CZ  . PHE A 109 ? 0.1649 0.2618 0.1704 -0.0692 -0.0016 0.0309  109 PHE A CZ  
1746 N  N   . GLU A 110 ? 0.1304 0.1638 0.1595 0.0155  0.0233  0.0161  110 GLU A N   
1747 C  CA  . GLU A 110 ? 0.1364 0.1611 0.1702 0.0193  0.0245  0.0135  110 GLU A CA  
1748 C  C   . GLU A 110 ? 0.1351 0.1699 0.1813 0.0224  0.0204  0.0026  110 GLU A C   
1749 O  O   . GLU A 110 ? 0.1293 0.2031 0.1947 0.0153  0.0356  -0.0104 110 GLU A O   
1750 C  CB  . GLU A 110 ? 0.1746 0.1595 0.1846 0.0195  0.0005  0.0107  110 GLU A CB  
1751 C  CG  . GLU A 110 ? 0.1652 0.1832 0.1947 0.0294  0.0003  -0.0033 110 GLU A CG  
1752 C  CD  . GLU A 110 ? 0.1707 0.1685 0.1838 0.0206  -0.0056 0.0100  110 GLU A CD  
1753 O  OE1 . GLU A 110 ? 0.1828 0.1757 0.1813 0.0213  -0.0044 -0.0026 110 GLU A OE1 
1754 O  OE2 . GLU A 110 ? 0.1698 0.1809 0.2078 0.0115  -0.0051 -0.0033 110 GLU A OE2 
1761 N  N   . GLU A 111 ? 0.1508 0.1910 0.1800 0.0143  0.0395  0.0004  111 GLU A N   
1762 C  CA  . GLU A 111 ? 0.1797 0.1955 0.1847 0.0227  0.0444  -0.0022 111 GLU A CA  
1763 C  C   . GLU A 111 ? 0.1439 0.2223 0.1835 0.0240  0.0530  0.0099  111 GLU A C   
1764 O  O   . GLU A 111 ? 0.1429 0.2525 0.2377 0.0167  0.0547  0.0036  111 GLU A O   
1765 C  CB  . GLU A 111 ? 0.1919 0.2403 0.1855 0.0207  0.0570  -0.0051 111 GLU A CB  
1766 C  CG  . GLU A 111 ? 0.2132 0.2712 0.2362 0.0158  0.0552  -0.0044 111 GLU A CG  
1767 C  CD  . GLU A 111 ? 0.1771 0.3088 0.2298 0.0205  0.0428  0.0145  111 GLU A CD  
1768 O  OE1 . GLU A 111 ? 0.1639 0.3192 0.1995 -0.0015 0.0396  0.0313  111 GLU A OE1 
1769 O  OE2 . GLU A 111 ? 0.2030 0.3578 0.2245 0.0384  0.0428  0.0218  111 GLU A OE2 
1776 N  N   . GLN A 112 ? 0.1356 0.2078 0.1802 0.0101  0.0578  0.0195  112 GLN A N   
1777 C  CA  . GLN A 112 ? 0.1511 0.2336 0.1966 -0.0076 0.0635  0.0287  112 GLN A CA  
1778 C  C   . GLN A 112 ? 0.1511 0.2269 0.1944 -0.0020 0.0606  0.0288  112 GLN A C   
1779 O  O   . GLN A 112 ? 0.1799 0.2639 0.2265 -0.0391 0.0795  -0.0014 112 GLN A O   
1780 C  CB  . GLN A 112 ? 0.1874 0.2532 0.1925 -0.0115 0.0606  0.0321  112 GLN A CB  
1781 C  CG  . GLN A 112 ? 0.1975 0.2921 0.1774 0.0165  0.0618  0.0322  112 GLN A CG  
1782 C  CD  . GLN A 112 ? 0.2220 0.3278 0.2391 0.0162  0.0513  0.0688  112 GLN A CD  
1783 O  OE1 . GLN A 112 ? 0.2210 0.3516 0.2403 0.0580  0.0389  0.0755  112 GLN A OE1 
1784 N  NE2 . GLN A 112 ? 0.3000 0.4942 0.2932 0.0533  0.0405  0.1308  112 GLN A NE2 
1793 N  N   . SER A 113 ? 0.1338 0.1872 0.1727 0.0033  0.0429  0.0216  113 SER A N   
1794 C  CA  . SER A 113 ? 0.1302 0.1571 0.1971 0.0001  0.0426  0.0251  113 SER A CA  
1795 C  C   . SER A 113 ? 0.1233 0.1781 0.1869 0.0040  0.0379  0.0154  113 SER A C   
1796 O  O   . SER A 113 ? 0.1374 0.1624 0.2063 -0.0048 0.0317  0.0195  113 SER A O   
1797 C  CB  . SER A 113 ? 0.1341 0.1507 0.1942 0.0107  0.0378  0.0272  113 SER A CB  
1798 O  OG  . SER A 113 ? 0.1490 0.1670 0.1947 0.0166  0.0405  0.0286  113 SER A OG  
1804 N  N   . ARG A 114 ? 0.1307 0.1743 0.1756 0.0080  0.0343  0.0061  114 ARG A N   
1805 C  CA  . ARG A 114 ? 0.1297 0.1884 0.1978 0.0321  0.0374  0.0100  114 ARG A CA  
1806 C  C   . ARG A 114 ? 0.1186 0.1589 0.1891 0.0328  0.0264  0.0108  114 ARG A C   
1807 O  O   . ARG A 114 ? 0.1208 0.1673 0.1975 0.0155  0.0192  0.0067  114 ARG A O   
1808 C  CB  . ARG A 114 ? 0.1228 0.2556 0.1975 0.0409  0.0426  0.0265  114 ARG A CB  
1809 C  CG  . ARG A 114 ? 0.1410 0.3493 0.2242 0.0267  0.0436  0.0390  114 ARG A CG  
1810 C  CD  . ARG A 114 ? 0.2284 0.4054 0.2863 0.0697  0.0696  -0.0022 114 ARG A CD  
1811 N  NE  . ARG A 114 ? 0.3322 0.3764 0.3260 0.0968  0.0744  -0.0694 114 ARG A NE  
1812 C  CZ  . ARG A 114 ? 0.2970 0.4878 0.3546 0.0679  0.0321  -0.1173 114 ARG A CZ  
1813 N  NH1 . ARG A 114 ? 0.2573 0.6298 0.3361 0.0359  0.0076  -0.1075 114 ARG A NH1 
1814 N  NH2 . ARG A 114 ? 0.3585 0.5269 0.4563 0.1207  0.0160  -0.0836 114 ARG A NH2 
1828 N  N   . HIS A 115 ? 0.1140 0.1588 0.1711 0.0105  0.0203  0.0086  115 HIS A N   
1829 C  CA  . HIS A 115 ? 0.1096 0.1560 0.1737 0.0120  0.0165  0.0042  115 HIS A CA  
1830 C  C   . HIS A 115 ? 0.1123 0.1372 0.1805 0.0155  0.0167  -0.0002 115 HIS A C   
1831 O  O   . HIS A 115 ? 0.1168 0.1409 0.1876 0.0215  0.0101  -0.0049 115 HIS A O   
1832 C  CB  . HIS A 115 ? 0.1039 0.1453 0.1661 0.0103  0.0091  0.0085  115 HIS A CB  
1833 C  CG  . HIS A 115 ? 0.1021 0.1259 0.1671 0.0068  0.0217  0.0189  115 HIS A CG  
1834 N  ND1 . HIS A 115 ? 0.1416 0.1482 0.1637 0.0323  0.0309  0.0365  115 HIS A ND1 
1835 C  CD2 . HIS A 115 ? 0.1049 0.1140 0.1675 0.0121  0.0145  0.0164  115 HIS A CD2 
1836 C  CE1 . HIS A 115 ? 0.1393 0.1309 0.1701 0.0287  0.0289  0.0270  115 HIS A CE1 
1837 N  NE2 . HIS A 115 ? 0.1030 0.1106 0.1529 0.0070  0.0056  0.0225  115 HIS A NE2 
1845 N  N   . ILE A 116 ? 0.1378 0.1264 0.1738 0.0159  0.0014  0.0053  116 ILE A N   
1846 C  CA  . ILE A 116 ? 0.1573 0.1301 0.1847 0.0104  -0.0091 0.0084  116 ILE A CA  
1847 C  C   . ILE A 116 ? 0.1595 0.1271 0.1936 0.0259  -0.0095 0.0028  116 ILE A C   
1848 O  O   . ILE A 116 ? 0.1604 0.1421 0.2042 0.0163  -0.0182 -0.0017 116 ILE A O   
1849 C  CB  . ILE A 116 ? 0.1666 0.1352 0.1961 0.0048  -0.0133 0.0159  116 ILE A CB  
1850 C  CG1 . ILE A 116 ? 0.1618 0.1616 0.2092 -0.0192 -0.0118 0.0156  116 ILE A CG1 
1851 C  CG2 . ILE A 116 ? 0.2002 0.1461 0.2140 0.0041  -0.0366 0.0216  116 ILE A CG2 
1852 C  CD1 . ILE A 116 ? 0.1851 0.1583 0.2424 -0.0233 -0.0111 0.0259  116 ILE A CD1 
1864 N  N   . HIS A 117 ? 0.1401 0.1463 0.2021 0.0254  -0.0024 -0.0036 117 HIS A N   
1865 C  CA  . HIS A 117 ? 0.1388 0.1730 0.2249 0.0412  -0.0109 -0.0159 117 HIS A CA  
1866 C  C   . HIS A 117 ? 0.1219 0.1802 0.2213 0.0235  0.0123  -0.0133 117 HIS A C   
1867 O  O   . HIS A 117 ? 0.1413 0.1966 0.2543 0.0279  -0.0118 -0.0284 117 HIS A O   
1868 C  CB  . HIS A 117 ? 0.1441 0.2071 0.2430 0.0342  0.0087  -0.0398 117 HIS A CB  
1869 C  CG  . HIS A 117 ? 0.1548 0.2879 0.2853 0.0295  0.0185  -0.0580 117 HIS A CG  
1870 N  ND1 . HIS A 117 ? 0.1725 0.3481 0.3235 0.0778  0.0366  -0.0515 117 HIS A ND1 
1871 C  CD2 . HIS A 117 ? 0.1779 0.3530 0.2952 -0.0035 0.0660  -0.0605 117 HIS A CD2 
1872 C  CE1 . HIS A 117 ? 0.1773 0.3759 0.3753 0.0648  0.0637  -0.0470 117 HIS A CE1 
1873 N  NE2 . HIS A 117 ? 0.1845 0.3776 0.3654 0.0031  0.0712  -0.0380 117 HIS A NE2 
1881 N  N   . ILE A 118 ? 0.1196 0.1569 0.2024 0.0136  0.0136  -0.0133 118 ILE A N   
1882 C  CA  . ILE A 118 ? 0.1235 0.1665 0.2094 -0.0006 0.0140  0.0041  118 ILE A CA  
1883 C  C   . ILE A 118 ? 0.1123 0.1421 0.2012 0.0081  0.0107  -0.0130 118 ILE A C   
1884 O  O   . ILE A 118 ? 0.1095 0.1516 0.2097 0.0043  0.0158  -0.0106 118 ILE A O   
1885 C  CB  . ILE A 118 ? 0.1682 0.1654 0.1963 -0.0109 0.0276  0.0086  118 ILE A CB  
1886 C  CG1 . ILE A 118 ? 0.1962 0.2165 0.2157 -0.0306 0.0199  0.0245  118 ILE A CG1 
1887 C  CG2 . ILE A 118 ? 0.2205 0.1571 0.2266 -0.0169 0.0160  0.0132  118 ILE A CG2 
1888 C  CD1 . ILE A 118 ? 0.2710 0.2004 0.1969 -0.0340 0.0104  0.0221  118 ILE A CD1 
1900 N  N   . GLY A 119 ? 0.1072 0.1351 0.1996 0.0024  0.0165  0.0002  119 GLY A N   
1901 C  CA  . GLY A 119 ? 0.1080 0.1336 0.1957 0.0117  0.0119  -0.0004 119 GLY A CA  
1902 C  C   . GLY A 119 ? 0.0949 0.1388 0.1898 0.0066  0.0074  -0.0091 119 GLY A C   
1903 O  O   . GLY A 119 ? 0.1044 0.1475 0.1910 0.0113  -0.0002 -0.0159 119 GLY A O   
1907 N  N   . LEU A 120 ? 0.1180 0.1319 0.1969 0.0207  -0.0033 -0.0102 120 LEU A N   
1908 C  CA  . LEU A 120 ? 0.1170 0.1374 0.2127 0.0218  -0.0152 -0.0064 120 LEU A CA  
1909 C  C   . LEU A 120 ? 0.1255 0.1288 0.2171 0.0319  -0.0119 -0.0060 120 LEU A C   
1910 O  O   . LEU A 120 ? 0.1334 0.1435 0.2383 0.0272  -0.0226 -0.0079 120 LEU A O   
1911 C  CB  . LEU A 120 ? 0.1479 0.1449 0.2293 0.0266  -0.0274 -0.0216 120 LEU A CB  
1912 C  CG  . LEU A 120 ? 0.1760 0.1302 0.2549 0.0284  -0.0474 -0.0169 120 LEU A CG  
1913 C  CD1 . LEU A 120 ? 0.2110 0.1440 0.2720 0.0375  -0.0478 -0.0295 120 LEU A CD1 
1914 C  CD2 . LEU A 120 ? 0.2284 0.1277 0.2584 0.0224  -0.0337 -0.0107 120 LEU A CD2 
1926 N  N   . GLN A 121 ? 0.1063 0.1497 0.2190 0.0228  0.0076  -0.0133 121 GLN A N   
1927 C  CA  . GLN A 121 ? 0.1073 0.1699 0.2446 0.0169  0.0144  -0.0160 121 GLN A CA  
1928 C  C   . GLN A 121 ? 0.0975 0.1612 0.2499 0.0069  -0.0001 -0.0162 121 GLN A C   
1929 O  O   . GLN A 121 ? 0.1086 0.2284 0.2969 -0.0066 0.0110  -0.0563 121 GLN A O   
1930 C  CB  . GLN A 121 ? 0.1156 0.1982 0.2579 0.0120  0.0203  -0.0100 121 GLN A CB  
1931 C  CG  . GLN A 121 ? 0.1544 0.2818 0.2518 -0.0030 0.0219  -0.0097 121 GLN A CG  
1932 C  CD  . GLN A 121 ? 0.1683 0.4089 0.2949 -0.0375 0.0587  0.0116  121 GLN A CD  
1933 O  OE1 . GLN A 121 ? 0.2575 0.4668 0.3841 -0.0801 0.0465  0.0103  121 GLN A OE1 
1934 N  NE2 . GLN A 121 ? 0.2632 0.4918 0.3753 -0.0240 0.0275  0.0295  121 GLN A NE2 
1943 N  N   . TYR A 122 ? 0.1004 0.1339 0.2077 0.0103  -0.0012 -0.0138 122 TYR A N   
1944 C  CA  . TYR A 122 ? 0.1083 0.1335 0.2080 0.0129  -0.0105 -0.0135 122 TYR A CA  
1945 C  C   . TYR A 122 ? 0.1044 0.1234 0.2146 0.0046  -0.0124 -0.0157 122 TYR A C   
1946 O  O   . TYR A 122 ? 0.1230 0.1219 0.2087 0.0153  -0.0149 -0.0142 122 TYR A O   
1947 C  CB  . TYR A 122 ? 0.1108 0.1233 0.2194 0.0126  -0.0085 -0.0044 122 TYR A CB  
1948 C  CG  . TYR A 122 ? 0.1157 0.1282 0.2257 0.0213  0.0077  -0.0028 122 TYR A CG  
1949 C  CD1 . TYR A 122 ? 0.1066 0.1416 0.2286 0.0177  0.0110  0.0095  122 TYR A CD1 
1950 C  CD2 . TYR A 122 ? 0.1092 0.1313 0.2399 0.0095  -0.0055 0.0019  122 TYR A CD2 
1951 C  CE1 . TYR A 122 ? 0.1218 0.1553 0.2215 0.0142  0.0173  0.0129  122 TYR A CE1 
1952 C  CE2 . TYR A 122 ? 0.1179 0.1385 0.2557 0.0164  0.0105  -0.0012 122 TYR A CE2 
1953 C  CZ  . TYR A 122 ? 0.1144 0.1496 0.2603 -0.0003 0.0287  0.0135  122 TYR A CZ  
1954 O  OH  . TYR A 122 ? 0.1547 0.1813 0.2760 -0.0047 0.0546  0.0241  122 TYR A OH  
1964 N  N   . LEU A 123 ? 0.1212 0.1236 0.2034 0.0122  -0.0060 -0.0170 123 LEU A N   
1965 C  CA  . LEU A 123 ? 0.1267 0.1125 0.2073 0.0181  -0.0166 -0.0087 123 LEU A CA  
1966 C  C   . LEU A 123 ? 0.1358 0.1218 0.2334 0.0336  -0.0245 -0.0185 123 LEU A C   
1967 O  O   . LEU A 123 ? 0.1540 0.1631 0.2628 0.0475  -0.0118 -0.0287 123 LEU A O   
1968 C  CB  . LEU A 123 ? 0.1513 0.1100 0.2161 0.0139  -0.0196 -0.0122 123 LEU A CB  
1969 C  CG  . LEU A 123 ? 0.1724 0.1556 0.3063 -0.0002 -0.0692 -0.0013 123 LEU A CG  
1970 C  CD1 . LEU A 123 ? 0.1248 0.1655 0.3070 0.0308  -0.0248 -0.0557 123 LEU A CD1 
1971 C  CD2 . LEU A 123 ? 0.1850 0.1236 0.2851 -0.0050 -0.0731 0.0148  123 LEU A CD2 
1983 N  N   . PRO A 124 ? 0.1504 0.1213 0.2435 0.0358  -0.0428 -0.0044 124 PRO A N   
1984 C  CA  . PRO A 124 ? 0.1802 0.1306 0.2282 0.0224  -0.0450 0.0068  124 PRO A CA  
1985 C  C   . PRO A 124 ? 0.1349 0.1385 0.2189 0.0139  -0.0380 0.0073  124 PRO A C   
1986 O  O   . PRO A 124 ? 0.1673 0.1600 0.2153 0.0003  -0.0143 0.0109  124 PRO A O   
1987 C  CB  . PRO A 124 ? 0.2819 0.1531 0.2678 0.0528  -0.0544 0.0047  124 PRO A CB  
1988 C  CG  . PRO A 124 ? 0.2544 0.1775 0.2840 0.0866  -0.0925 0.0063  124 PRO A CG  
1989 C  CD  . PRO A 124 ? 0.1825 0.1641 0.2805 0.0675  -0.0677 -0.0099 124 PRO A CD  
1997 N  N   . ALA A 125 ? 0.1083 0.1321 0.2069 0.0070  -0.0261 -0.0006 125 ALA A N   
1998 C  CA  . ALA A 125 ? 0.0992 0.1353 0.2075 0.0104  -0.0211 -0.0163 125 ALA A CA  
1999 C  C   . ALA A 125 ? 0.1111 0.1249 0.2018 0.0029  -0.0195 -0.0144 125 ALA A C   
2000 O  O   . ALA A 125 ? 0.1173 0.1367 0.2054 0.0019  -0.0281 -0.0222 125 ALA A O   
2001 C  CB  . ALA A 125 ? 0.1185 0.1357 0.2311 -0.0076 0.0003  -0.0270 125 ALA A CB  
2007 N  N   . VAL A 126 ? 0.0985 0.1212 0.1985 0.0112  -0.0233 -0.0224 126 VAL A N   
2008 C  CA  . VAL A 126 ? 0.0975 0.1168 0.1952 0.0134  -0.0140 -0.0125 126 VAL A CA  
2009 C  C   . VAL A 126 ? 0.1016 0.1182 0.1951 0.0095  -0.0181 -0.0209 126 VAL A C   
2010 O  O   . VAL A 126 ? 0.1177 0.1247 0.2069 -0.0057 -0.0039 -0.0272 126 VAL A O   
2011 C  CB  . VAL A 126 ? 0.1007 0.1309 0.1974 0.0154  -0.0181 -0.0181 126 VAL A CB  
2012 C  CG1 . VAL A 126 ? 0.1069 0.1150 0.2284 0.0132  -0.0183 -0.0063 126 VAL A CG1 
2013 C  CG2 . VAL A 126 ? 0.1132 0.1258 0.2246 0.0117  -0.0074 -0.0159 126 VAL A CG2 
2023 N  N   . ALA A 127 ? 0.0954 0.1198 0.1841 0.0035  -0.0155 -0.0109 127 ALA A N   
2024 C  CA  . ALA A 127 ? 0.0949 0.1175 0.1924 0.0100  -0.0112 -0.0070 127 ALA A CA  
2025 C  C   . ALA A 127 ? 0.0890 0.1127 0.1884 0.0133  -0.0110 -0.0112 127 ALA A C   
2026 O  O   . ALA A 127 ? 0.1045 0.1036 0.2082 0.0155  -0.0202 -0.0198 127 ALA A O   
2027 C  CB  . ALA A 127 ? 0.1121 0.1380 0.1865 -0.0028 -0.0180 -0.0148 127 ALA A CB  
2033 N  N   . ARG A 128 ? 0.0948 0.1011 0.1997 0.0115  -0.0218 -0.0053 128 ARG A N   
2034 C  CA  . ARG A 128 ? 0.0977 0.0939 0.2053 0.0074  -0.0206 -0.0049 128 ARG A CA  
2035 C  C   . ARG A 128 ? 0.1078 0.0919 0.1935 0.0064  -0.0155 -0.0084 128 ARG A C   
2036 O  O   . ARG A 128 ? 0.1157 0.0927 0.2031 0.0037  -0.0232 0.0034  128 ARG A O   
2037 C  CB  . ARG A 128 ? 0.1083 0.1004 0.2045 0.0002  -0.0292 0.0123  128 ARG A CB  
2038 C  CG  . ARG A 128 ? 0.1434 0.1207 0.1853 0.0057  -0.0268 0.0072  128 ARG A CG  
2039 C  CD  . ARG A 128 ? 0.1448 0.1370 0.1836 0.0134  -0.0283 0.0054  128 ARG A CD  
2040 N  NE  . ARG A 128 ? 0.1471 0.1522 0.2049 0.0167  -0.0369 -0.0079 128 ARG A NE  
2041 C  CZ  . ARG A 128 ? 0.1420 0.1449 0.2117 0.0176  -0.0354 -0.0172 128 ARG A CZ  
2042 N  NH1 . ARG A 128 ? 0.1446 0.1355 0.2228 0.0238  -0.0381 -0.0218 128 ARG A NH1 
2043 N  NH2 . ARG A 128 ? 0.1696 0.1548 0.2523 0.0060  -0.0431 -0.0207 128 ARG A NH2 
2057 N  N   . ARG A 129 ? 0.0993 0.0950 0.1912 0.0033  -0.0187 -0.0122 129 ARG A N   
2058 C  CA  . ARG A 129 ? 0.0988 0.0936 0.1844 0.0020  -0.0158 -0.0035 129 ARG A CA  
2059 C  C   . ARG A 129 ? 0.0965 0.0972 0.1795 0.0000  -0.0122 -0.0029 129 ARG A C   
2060 O  O   . ARG A 129 ? 0.1367 0.0988 0.2290 0.0183  -0.0569 -0.0254 129 ARG A O   
2061 C  CB  . ARG A 129 ? 0.1179 0.1210 0.1784 -0.0079 -0.0149 -0.0026 129 ARG A CB  
2062 C  CG  . ARG A 129 ? 0.1385 0.1597 0.1888 -0.0276 -0.0007 -0.0088 129 ARG A CG  
2063 C  CD  . ARG A 129 ? 0.1684 0.1728 0.2098 -0.0300 -0.0157 0.0169  129 ARG A CD  
2064 N  NE  . ARG A 129 ? 0.2915 0.1975 0.2400 0.0135  0.0170  0.0311  129 ARG A NE  
2065 C  CZ  . ARG A 129 ? 0.3287 0.2371 0.2301 0.0101  -0.0104 0.0709  129 ARG A CZ  
2066 N  NH1 . ARG A 129 ? 0.2213 0.3112 0.2063 0.0191  0.0004  0.0614  129 ARG A NH1 
2067 N  NH2 . ARG A 129 ? 0.4206 0.2462 0.2888 0.0704  -0.0395 0.0568  129 ARG A NH2 
2081 N  N   . LEU A 130 ? 0.1011 0.0918 0.1573 -0.0063 -0.0068 -0.0018 130 LEU A N   
2082 C  CA  . LEU A 130 ? 0.0971 0.0904 0.1616 -0.0018 0.0007  0.0105  130 LEU A CA  
2083 C  C   . LEU A 130 ? 0.0979 0.0906 0.1338 0.0012  0.0029  0.0064  130 LEU A C   
2084 O  O   . LEU A 130 ? 0.1178 0.0841 0.1598 -0.0018 0.0183  0.0077  130 LEU A O   
2085 C  CB  . LEU A 130 ? 0.1048 0.1066 0.1532 0.0019  0.0139  0.0105  130 LEU A CB  
2086 C  CG  . LEU A 130 ? 0.1088 0.1107 0.1487 -0.0001 0.0151  0.0129  130 LEU A CG  
2087 C  CD1 . LEU A 130 ? 0.1325 0.1178 0.1571 0.0094  0.0169  0.0160  130 LEU A CD1 
2088 C  CD2 . LEU A 130 ? 0.1334 0.1197 0.1491 -0.0102 0.0207  0.0031  130 LEU A CD2 
2100 N  N   . HIS A 131 ? 0.0913 0.0897 0.1329 -0.0010 0.0025  0.0127  131 HIS A N   
2101 C  CA  . HIS A 131 ? 0.0920 0.0997 0.1282 -0.0070 0.0001  0.0125  131 HIS A CA  
2102 C  C   . HIS A 131 ? 0.0943 0.0914 0.1301 -0.0052 0.0007  0.0083  131 HIS A C   
2103 O  O   . HIS A 131 ? 0.1168 0.0971 0.1393 -0.0126 -0.0058 0.0159  131 HIS A O   
2104 C  CB  . HIS A 131 ? 0.0877 0.1102 0.1348 -0.0056 0.0052  0.0116  131 HIS A CB  
2105 C  CG  . HIS A 131 ? 0.1022 0.1064 0.1414 -0.0081 -0.0010 0.0135  131 HIS A CG  
2106 N  ND1 . HIS A 131 ? 0.1060 0.1117 0.1406 -0.0166 0.0025  0.0112  131 HIS A ND1 
2107 C  CD2 . HIS A 131 ? 0.1199 0.1289 0.1379 -0.0120 -0.0012 0.0071  131 HIS A CD2 
2108 C  CE1 . HIS A 131 ? 0.1170 0.1340 0.1456 -0.0143 -0.0018 0.0061  131 HIS A CE1 
2109 N  NE2 . HIS A 131 ? 0.1283 0.1389 0.1406 -0.0058 -0.0049 0.0141  131 HIS A NE2 
2117 N  N   . HIS A 132 ? 0.0963 0.0982 0.1184 -0.0016 0.0038  0.0151  132 HIS A N   
2118 C  CA  . HIS A 132 ? 0.0975 0.0981 0.1198 -0.0040 0.0018  0.0120  132 HIS A CA  
2119 C  C   . HIS A 132 ? 0.0971 0.0977 0.1249 0.0016  0.0057  0.0129  132 HIS A C   
2120 O  O   . HIS A 132 ? 0.1067 0.1122 0.1346 0.0118  0.0166  0.0216  132 HIS A O   
2121 C  CB  . HIS A 132 ? 0.0962 0.0952 0.1317 -0.0055 0.0003  0.0095  132 HIS A CB  
2122 C  CG  . HIS A 132 ? 0.1098 0.0920 0.1435 0.0005  0.0031  0.0055  132 HIS A CG  
2123 N  ND1 . HIS A 132 ? 0.1215 0.1115 0.1511 0.0097  0.0137  -0.0019 132 HIS A ND1 
2124 C  CD2 . HIS A 132 ? 0.1132 0.1009 0.1677 0.0067  0.0059  0.0028  132 HIS A CD2 
2125 C  CE1 . HIS A 132 ? 0.1332 0.1023 0.1768 0.0148  0.0218  -0.0105 132 HIS A CE1 
2126 N  NE2 . HIS A 132 ? 0.1165 0.0990 0.1978 0.0071  0.0051  -0.0023 132 HIS A NE2 
2134 N  N   . CYS A 133 ? 0.0911 0.1053 0.1250 0.0056  0.0063  0.0131  133 CYS A N   
2135 C  CA  . CYS A 133 ? 0.0924 0.1084 0.1253 0.0045  0.0070  0.0117  133 CYS A CA  
2136 C  C   . CYS A 133 ? 0.0922 0.1106 0.1315 0.0072  0.0049  0.0095  133 CYS A C   
2137 O  O   . CYS A 133 ? 0.0939 0.1289 0.1426 0.0087  0.0089  0.0044  133 CYS A O   
2138 C  CB  . CYS A 133 ? 0.1033 0.1090 0.1428 -0.0009 0.0047  0.0078  133 CYS A CB  
2139 S  SG  . CYS A 133 ? 0.1146 0.1190 0.1492 0.0033  -0.0022 -0.0010 133 CYS A SG  
2145 N  N   . ARG A 134 ? 0.0938 0.1191 0.1302 0.0102  0.0065  0.0142  134 ARG A N   
2146 C  CA  . ARG A 134 ? 0.1096 0.1149 0.1381 0.0159  0.0040  0.0124  134 ARG A CA  
2147 C  C   . ARG A 134 ? 0.1044 0.1325 0.1208 0.0125  0.0052  0.0020  134 ARG A C   
2148 O  O   . ARG A 134 ? 0.1069 0.1564 0.1428 0.0033  -0.0074 0.0108  134 ARG A O   
2149 C  CB  . ARG A 134 ? 0.1270 0.1275 0.1457 0.0086  0.0012  0.0041  134 ARG A CB  
2150 C  CG  . ARG A 134 ? 0.1434 0.1760 0.1704 0.0129  0.0057  0.0128  134 ARG A CG  
2151 C  CD  . ARG A 134 ? 0.1339 0.1840 0.1802 0.0197  0.0064  0.0427  134 ARG A CD  
2152 N  NE  . ARG A 134 ? 0.1619 0.1878 0.1667 0.0246  0.0032  0.0348  134 ARG A NE  
2153 C  CZ  . ARG A 134 ? 0.1761 0.2031 0.1685 0.0356  -0.0068 0.0292  134 ARG A CZ  
2154 N  NH1 . ARG A 134 ? 0.2178 0.1961 0.1703 -0.0320 0.0441  -0.0151 134 ARG A NH1 
2155 N  NH2 . ARG A 134 ? 0.2045 0.2210 0.2044 0.0278  -0.0271 0.0377  134 ARG A NH2 
2169 N  N   . ASP A 135 ? 0.1159 0.1153 0.1246 -0.0039 0.0016  0.0029  135 ASP A N   
2170 C  CA  . ASP A 135 ? 0.1172 0.1423 0.1330 -0.0097 0.0013  -0.0039 135 ASP A CA  
2171 C  C   . ASP A 135 ? 0.1220 0.1752 0.1413 -0.0351 0.0034  -0.0064 135 ASP A C   
2172 O  O   . ASP A 135 ? 0.1657 0.2191 0.1558 -0.0679 0.0220  -0.0162 135 ASP A O   
2173 C  CB  . ASP A 135 ? 0.1221 0.1331 0.1451 -0.0104 -0.0096 0.0156  135 ASP A CB  
2174 C  CG  . ASP A 135 ? 0.1220 0.1256 0.1594 0.0077  -0.0010 -0.0034 135 ASP A CG  
2175 O  OD1 . ASP A 135 ? 0.1341 0.1415 0.1523 0.0202  -0.0022 0.0063  135 ASP A OD1 
2176 O  OD2 . ASP A 135 ? 0.1551 0.1805 0.1540 0.0457  -0.0066 -0.0229 135 ASP A OD2 
2181 N  N   . LEU A 136 ? 0.1135 0.1911 0.1458 -0.0192 0.0086  -0.0173 136 LEU A N   
2182 C  CA  . LEU A 136 ? 0.1430 0.2256 0.1837 -0.0309 0.0273  -0.0450 136 LEU A CA  
2183 C  C   . LEU A 136 ? 0.1349 0.2402 0.2096 0.0210  0.0172  -0.0061 136 LEU A C   
2184 O  O   . LEU A 136 ? 0.1479 0.2448 0.2644 0.0165  0.0270  -0.0129 136 LEU A O   
2185 C  CB  . LEU A 136 ? 0.1446 0.2282 0.1793 -0.0416 0.0242  -0.0405 136 LEU A CB  
2186 C  CG  . LEU A 136 ? 0.1631 0.1842 0.1580 -0.0400 0.0258  -0.0129 136 LEU A CG  
2187 C  CD1 . LEU A 136 ? 0.1712 0.1788 0.1790 -0.0397 -0.0137 -0.0115 136 LEU A CD1 
2188 C  CD2 . LEU A 136 ? 0.2403 0.1660 0.1855 -0.0438 0.0307  -0.0273 136 LEU A CD2 
2200 N  N   . GLY A 137 ? 0.1406 0.2409 0.2455 0.0239  -0.0080 -0.0066 137 GLY A N   
2201 C  CA  . GLY A 137 ? 0.1675 0.2287 0.2332 0.0412  -0.0038 -0.0253 137 GLY A CA  
2202 C  C   . GLY A 137 ? 0.2016 0.2503 0.2250 0.0511  -0.0148 -0.0026 137 GLY A C   
2203 O  O   . GLY A 137 ? 0.2087 0.2561 0.2388 0.0607  0.0150  0.0099  137 GLY A O   
2207 N  N   . GLU A 138 ? 0.2125 0.2947 0.2211 0.0773  -0.0235 0.0104  138 GLU A N   
2208 C  CA  . GLU A 138 ? 0.2719 0.3355 0.2661 0.0790  -0.0297 0.0609  138 GLU A CA  
2209 C  C   . GLU A 138 ? 0.1921 0.3160 0.2612 0.0720  0.0063  0.1012  138 GLU A C   
2210 O  O   . GLU A 138 ? 0.2399 0.3677 0.3273 0.0473  0.0083  0.1203  138 GLU A O   
2211 C  CB  . GLU A 138 ? 0.3733 0.4043 0.3459 0.0532  -0.0800 0.0856  138 GLU A CB  
2212 C  CG  . GLU A 138 ? 0.4498 0.3920 0.4601 0.0259  -0.0790 0.0273  138 GLU A CG  
2213 C  CD  . GLU A 138 ? 0.4648 0.3539 0.4249 -0.0069 -0.0738 0.0609  138 GLU A CD  
2214 O  OE1 . GLU A 138 ? 0.4731 0.4032 0.3908 0.1075  -0.1272 0.0128  138 GLU A OE1 
2215 O  OE2 . GLU A 138 ? 0.4079 0.2095 0.3755 0.0584  -0.0540 0.0188  138 GLU A OE2 
2222 N  N   . ASN A 139 ? 0.1733 0.2288 0.3352 0.0522  0.0217  0.0571  139 ASN A N   
2223 C  CA  . ASN A 139 ? 0.1870 0.2762 0.3483 0.0681  -0.0063 0.0135  139 ASN A CA  
2224 C  C   . ASN A 139 ? 0.1407 0.2886 0.3310 0.0619  0.0093  -0.0281 139 ASN A C   
2225 O  O   . ASN A 139 ? 0.2115 0.2794 0.3803 0.0763  -0.0003 -0.0383 139 ASN A O   
2226 C  CB  . ASN A 139 ? 0.1914 0.3473 0.4257 0.0663  -0.0111 -0.0219 139 ASN A CB  
2227 C  CG  . ASN A 139 ? 0.1867 0.4649 0.4647 0.0974  -0.0101 -0.0230 139 ASN A CG  
2228 O  OD1 . ASN A 139 ? 0.2971 0.4914 0.4851 0.1492  -0.0535 -0.0182 139 ASN A OD1 
2229 N  ND2 . ASN A 139 ? 0.2145 0.5125 0.5354 0.0421  -0.0644 -0.0757 139 ASN A ND2 
2236 N  N   . GLU A 140 ? 0.1269 0.2039 0.2627 0.0288  0.0197  0.0128  140 GLU A N   
2237 C  CA  . GLU A 140 ? 0.1264 0.1822 0.2330 0.0382  0.0284  0.0066  140 GLU A CA  
2238 C  C   . GLU A 140 ? 0.1362 0.1756 0.2338 0.0414  0.0403  0.0162  140 GLU A C   
2239 O  O   . GLU A 140 ? 0.1411 0.2195 0.2163 0.0230  0.0111  0.0165  140 GLU A O   
2240 C  CB  . GLU A 140 ? 0.1345 0.1826 0.2398 0.0290  0.0367  0.0124  140 GLU A CB  
2241 C  CG  . GLU A 140 ? 0.1505 0.1979 0.2927 0.0502  0.0482  0.0389  140 GLU A CG  
2242 C  CD  . GLU A 140 ? 0.1742 0.2640 0.2952 0.0521  0.0693  0.0427  140 GLU A CD  
2243 O  OE1 . GLU A 140 ? 0.2108 0.3480 0.2532 0.0751  0.0502  0.0569  140 GLU A OE1 
2244 O  OE2 . GLU A 140 ? 0.2123 0.3248 0.3860 0.0156  0.1091  0.0154  140 GLU A OE2 
2251 N  N   . PRO A 141 ? 0.1418 0.1714 0.2054 0.0629  0.0269  0.0093  141 PRO A N   
2252 C  CA  . PRO A 141 ? 0.1503 0.1548 0.2182 0.0461  0.0189  0.0267  141 PRO A CA  
2253 C  C   . PRO A 141 ? 0.1387 0.1310 0.2035 0.0384  0.0142  0.0302  141 PRO A C   
2254 O  O   . PRO A 141 ? 0.1533 0.1476 0.2037 0.0448  0.0051  0.0474  141 PRO A O   
2255 C  CB  . PRO A 141 ? 0.1919 0.1629 0.2475 0.0638  0.0182  -0.0075 141 PRO A CB  
2256 C  CG  . PRO A 141 ? 0.1662 0.2039 0.2298 0.0425  0.0258  -0.0313 141 PRO A CG  
2257 C  CD  . PRO A 141 ? 0.1540 0.1936 0.2108 0.0506  0.0366  0.0051  141 PRO A CD  
2265 N  N   . PHE A 142 ? 0.1289 0.1148 0.1641 0.0393  0.0119  0.0128  142 PHE A N   
2266 C  CA  . PHE A 142 ? 0.1169 0.1116 0.1564 0.0282  0.0097  0.0264  142 PHE A CA  
2267 C  C   . PHE A 142 ? 0.1096 0.1152 0.1560 0.0230  0.0152  0.0193  142 PHE A C   
2268 O  O   . PHE A 142 ? 0.1142 0.1161 0.1697 0.0149  0.0251  0.0218  142 PHE A O   
2269 C  CB  . PHE A 142 ? 0.1298 0.1242 0.1612 0.0350  -0.0018 0.0038  142 PHE A CB  
2270 C  CG  . PHE A 142 ? 0.1586 0.1174 0.1726 0.0392  -0.0231 0.0031  142 PHE A CG  
2271 C  CD1 . PHE A 142 ? 0.2065 0.1253 0.1911 0.0072  -0.0447 0.0301  142 PHE A CD1 
2272 C  CD2 . PHE A 142 ? 0.1750 0.1495 0.2032 0.0608  -0.0251 -0.0184 142 PHE A CD2 
2273 C  CE1 . PHE A 142 ? 0.2589 0.1296 0.2411 0.0068  -0.0395 0.0383  142 PHE A CE1 
2274 C  CE2 . PHE A 142 ? 0.2207 0.1625 0.2542 0.0698  -0.0360 -0.0320 142 PHE A CE2 
2275 C  CZ  . PHE A 142 ? 0.2769 0.1378 0.2646 0.0463  -0.0585 -0.0117 142 PHE A CZ  
2285 N  N   . ASP A 143 ? 0.1058 0.0963 0.1492 0.0148  0.0158  0.0215  143 ASP A N   
2286 C  CA  . ASP A 143 ? 0.0944 0.1092 0.1404 0.0116  0.0109  0.0181  143 ASP A CA  
2287 C  C   . ASP A 143 ? 0.0929 0.0982 0.1251 0.0068  0.0123  0.0112  143 ASP A C   
2288 O  O   . ASP A 143 ? 0.0965 0.1010 0.1348 0.0015  0.0100  0.0203  143 ASP A O   
2289 C  CB  . ASP A 143 ? 0.0953 0.1213 0.1381 0.0085  0.0034  0.0186  143 ASP A CB  
2290 C  CG  . ASP A 143 ? 0.1121 0.1192 0.1383 0.0092  0.0035  0.0200  143 ASP A CG  
2291 O  OD1 . ASP A 143 ? 0.1108 0.1753 0.1512 0.0134  -0.0013 0.0325  143 ASP A OD1 
2292 O  OD2 . ASP A 143 ? 0.1369 0.1284 0.1335 0.0069  0.0108  0.0196  143 ASP A OD2 
2297 N  N   . PHE A 144 ? 0.0986 0.0923 0.1336 0.0069  0.0061  0.0133  144 PHE A N   
2298 C  CA  . PHE A 144 ? 0.0973 0.0917 0.1308 0.0044  0.0042  0.0160  144 PHE A CA  
2299 C  C   . PHE A 144 ? 0.0908 0.0955 0.1383 -0.0029 0.0046  0.0143  144 PHE A C   
2300 O  O   . PHE A 144 ? 0.1188 0.0933 0.1381 0.0018  0.0112  0.0154  144 PHE A O   
2301 C  CB  . PHE A 144 ? 0.1010 0.0996 0.1393 0.0104  0.0045  0.0118  144 PHE A CB  
2302 C  CG  . PHE A 144 ? 0.0899 0.1065 0.1332 0.0085  0.0052  0.0078  144 PHE A CG  
2303 C  CD1 . PHE A 144 ? 0.0967 0.1112 0.1538 0.0020  0.0097  -0.0069 144 PHE A CD1 
2304 C  CD2 . PHE A 144 ? 0.0994 0.1279 0.1380 0.0152  0.0051  0.0178  144 PHE A CD2 
2305 C  CE1 . PHE A 144 ? 0.1070 0.1412 0.1726 0.0068  0.0027  -0.0208 144 PHE A CE1 
2306 C  CE2 . PHE A 144 ? 0.1204 0.1689 0.1356 0.0344  0.0100  0.0173  144 PHE A CE2 
2307 C  CZ  . PHE A 144 ? 0.1021 0.1773 0.1535 0.0203  0.0028  -0.0278 144 PHE A CZ  
2317 N  N   . LEU A 145 ? 0.0891 0.0945 0.1307 0.0002  0.0025  0.0097  145 LEU A N   
2318 C  CA  . LEU A 145 ? 0.0862 0.0950 0.1360 0.0014  0.0000  0.0074  145 LEU A CA  
2319 C  C   . LEU A 145 ? 0.0913 0.0847 0.1302 0.0019  0.0050  0.0119  145 LEU A C   
2320 O  O   . LEU A 145 ? 0.0958 0.0914 0.1524 -0.0045 0.0048  0.0189  145 LEU A O   
2321 C  CB  . LEU A 145 ? 0.0964 0.1039 0.1455 -0.0021 0.0041  0.0015  145 LEU A CB  
2322 C  CG  . LEU A 145 ? 0.0961 0.1115 0.1454 0.0029  0.0074  -0.0050 145 LEU A CG  
2323 C  CD1 . LEU A 145 ? 0.1180 0.1140 0.1661 0.0005  0.0219  -0.0053 145 LEU A CD1 
2324 C  CD2 . LEU A 145 ? 0.1152 0.1250 0.1694 0.0176  0.0197  0.0177  145 LEU A CD2 
2336 N  N   . THR A 146 ? 0.0908 0.0824 0.1489 0.0035  0.0036  0.0085  146 THR A N   
2337 C  CA  . THR A 146 ? 0.0898 0.0811 0.1522 0.0041  -0.0006 0.0069  146 THR A CA  
2338 C  C   . THR A 146 ? 0.0861 0.0855 0.1591 -0.0008 0.0030  0.0107  146 THR A C   
2339 O  O   . THR A 146 ? 0.1261 0.0849 0.1643 0.0082  -0.0079 0.0022  146 THR A O   
2340 C  CB  . THR A 146 ? 0.0932 0.0951 0.1680 -0.0006 0.0077  0.0057  146 THR A CB  
2341 O  OG1 . THR A 146 ? 0.0961 0.0966 0.1700 0.0011  0.0062  0.0186  146 THR A OG1 
2342 C  CG2 . THR A 146 ? 0.1171 0.1432 0.1578 -0.0023 0.0091  0.0000  146 THR A CG2 
2350 N  N   . TRP A 147 ? 0.0892 0.0909 0.1555 -0.0013 -0.0007 0.0022  147 TRP A N   
2351 C  CA  . TRP A 147 ? 0.0939 0.0934 0.1595 0.0009  -0.0029 0.0051  147 TRP A CA  
2352 C  C   . TRP A 147 ? 0.0859 0.0835 0.1619 0.0024  -0.0048 0.0063  147 TRP A C   
2353 O  O   . TRP A 147 ? 0.0924 0.0901 0.1726 0.0030  -0.0116 -0.0001 147 TRP A O   
2354 C  CB  . TRP A 147 ? 0.0965 0.1013 0.1640 -0.0061 0.0076  0.0067  147 TRP A CB  
2355 C  CG  . TRP A 147 ? 0.1019 0.1123 0.1625 -0.0060 0.0041  0.0047  147 TRP A CG  
2356 C  CD1 . TRP A 147 ? 0.1247 0.1290 0.1655 -0.0027 -0.0017 0.0077  147 TRP A CD1 
2357 C  CD2 . TRP A 147 ? 0.1109 0.1241 0.1439 -0.0073 0.0119  0.0010  147 TRP A CD2 
2358 N  NE1 . TRP A 147 ? 0.1320 0.1329 0.1666 0.0039  -0.0025 0.0133  147 TRP A NE1 
2359 C  CE2 . TRP A 147 ? 0.1277 0.1354 0.1566 -0.0067 0.0072  0.0099  147 TRP A CE2 
2360 C  CE3 . TRP A 147 ? 0.1345 0.1294 0.1540 0.0064  0.0056  -0.0053 147 TRP A CE3 
2361 C  CZ2 . TRP A 147 ? 0.1283 0.1508 0.1657 -0.0095 0.0026  0.0048  147 TRP A CZ2 
2362 C  CZ3 . TRP A 147 ? 0.1626 0.1323 0.1729 0.0132  0.0101  -0.0126 147 TRP A CZ3 
2363 C  CH2 . TRP A 147 ? 0.1503 0.1477 0.1539 -0.0048 0.0081  -0.0057 147 TRP A CH2 
2374 N  N   . PHE A 148 ? 0.0862 0.0892 0.1596 0.0039  -0.0008 0.0038  148 PHE A N   
2375 C  CA  . PHE A 148 ? 0.0845 0.0962 0.1684 0.0011  -0.0091 0.0035  148 PHE A CA  
2376 C  C   . PHE A 148 ? 0.0922 0.0941 0.1629 -0.0023 -0.0048 -0.0037 148 PHE A C   
2377 O  O   . PHE A 148 ? 0.1106 0.0995 0.1642 0.0072  -0.0065 -0.0088 148 PHE A O   
2378 C  CB  . PHE A 148 ? 0.0913 0.0954 0.1752 -0.0004 -0.0022 0.0018  148 PHE A CB  
2379 C  CG  . PHE A 148 ? 0.0936 0.1012 0.1643 -0.0086 -0.0002 0.0144  148 PHE A CG  
2380 C  CD1 . PHE A 148 ? 0.0910 0.1074 0.1686 0.0005  -0.0017 0.0058  148 PHE A CD1 
2381 C  CD2 . PHE A 148 ? 0.0870 0.1094 0.1780 -0.0115 -0.0015 0.0230  148 PHE A CD2 
2382 C  CE1 . PHE A 148 ? 0.0986 0.1240 0.1698 -0.0114 0.0118  0.0051  148 PHE A CE1 
2383 C  CE2 . PHE A 148 ? 0.0916 0.1274 0.1758 -0.0083 0.0052  0.0326  148 PHE A CE2 
2384 C  CZ  . PHE A 148 ? 0.1029 0.1418 0.1605 -0.0114 0.0089  0.0231  148 PHE A CZ  
2394 N  N   . GLU A 149 ? 0.1010 0.0938 0.1671 0.0018  -0.0138 -0.0015 149 GLU A N   
2395 C  CA  . GLU A 149 ? 0.1021 0.1085 0.1639 0.0016  -0.0152 -0.0112 149 GLU A CA  
2396 C  C   . GLU A 149 ? 0.1013 0.0989 0.1752 0.0045  -0.0146 -0.0023 149 GLU A C   
2397 O  O   . GLU A 149 ? 0.1082 0.1087 0.1836 0.0045  -0.0166 -0.0157 149 GLU A O   
2398 C  CB  . GLU A 149 ? 0.1148 0.1341 0.1719 0.0012  -0.0126 -0.0011 149 GLU A CB  
2399 C  CG  . GLU A 149 ? 0.1229 0.1550 0.1761 0.0001  -0.0160 0.0115  149 GLU A CG  
2400 C  CD  . GLU A 149 ? 0.1314 0.1941 0.1947 0.0081  -0.0011 0.0442  149 GLU A CD  
2401 O  OE1 . GLU A 149 ? 0.1501 0.2484 0.2514 0.0154  0.0000  0.0985  149 GLU A OE1 
2402 O  OE2 . GLU A 149 ? 0.1439 0.2140 0.1843 -0.0024 -0.0090 0.0451  149 GLU A OE2 
2409 N  N   . TYR A 150 ? 0.0942 0.1090 0.1828 0.0033  -0.0167 -0.0105 150 TYR A N   
2410 C  CA  . TYR A 150 ? 0.0990 0.1149 0.1882 0.0028  -0.0211 -0.0144 150 TYR A CA  
2411 C  C   . TYR A 150 ? 0.0958 0.1157 0.1948 0.0020  -0.0222 -0.0150 150 TYR A C   
2412 O  O   . TYR A 150 ? 0.1083 0.1237 0.2065 0.0127  -0.0214 -0.0322 150 TYR A O   
2413 C  CB  . TYR A 150 ? 0.1016 0.1215 0.1883 0.0079  -0.0105 -0.0150 150 TYR A CB  
2414 C  CG  . TYR A 150 ? 0.1040 0.1205 0.1814 -0.0074 -0.0062 -0.0046 150 TYR A CG  
2415 C  CD1 . TYR A 150 ? 0.1062 0.1226 0.1879 -0.0130 -0.0024 -0.0155 150 TYR A CD1 
2416 C  CD2 . TYR A 150 ? 0.1016 0.1253 0.1908 -0.0104 -0.0048 -0.0043 150 TYR A CD2 
2417 C  CE1 . TYR A 150 ? 0.1188 0.1131 0.1868 -0.0057 -0.0073 -0.0129 150 TYR A CE1 
2418 C  CE2 . TYR A 150 ? 0.1066 0.1149 0.1973 -0.0037 -0.0154 0.0019  150 TYR A CE2 
2419 C  CZ  . TYR A 150 ? 0.1102 0.1087 0.1894 0.0021  -0.0043 0.0000  150 TYR A CZ  
2420 O  OH  . TYR A 150 ? 0.1194 0.1226 0.2061 0.0003  -0.0220 0.0032  150 TYR A OH  
2430 N  N   . SER A 151 ? 0.1044 0.1432 0.2231 0.0066  -0.0309 -0.0330 151 SER A N   
2431 C  CA  A SER A 151 ? 0.1052 0.1502 0.2278 -0.0044 -0.0277 -0.0329 151 SER A CA  
2432 C  CA  B SER A 151 ? 0.1165 0.1481 0.2288 -0.0030 -0.0273 -0.0344 151 SER A CA  
2433 C  C   . SER A 151 ? 0.1116 0.1565 0.2135 -0.0015 -0.0208 -0.0357 151 SER A C   
2434 O  O   . SER A 151 ? 0.1030 0.1605 0.2232 -0.0042 -0.0135 -0.0335 151 SER A O   
2435 C  CB  A SER A 151 ? 0.1131 0.1650 0.2495 -0.0006 -0.0432 -0.0374 151 SER A CB  
2436 C  CB  B SER A 151 ? 0.1294 0.1612 0.2554 0.0054  -0.0387 -0.0344 151 SER A CB  
2437 O  OG  A SER A 151 ? 0.1269 0.2193 0.2873 0.0078  -0.0298 -0.0440 151 SER A OG  
2438 O  OG  B SER A 151 ? 0.1560 0.2069 0.3215 0.0033  -0.0610 -0.0536 151 SER A OG  
2447 N  N   . PRO A 152 ? 0.1268 0.1597 0.2185 -0.0117 -0.0174 -0.0369 152 PRO A N   
2448 C  CA  . PRO A 152 ? 0.1406 0.1456 0.2330 -0.0143 -0.0166 -0.0410 152 PRO A CA  
2449 C  C   . PRO A 152 ? 0.1418 0.1557 0.2470 -0.0133 -0.0181 -0.0465 152 PRO A C   
2450 O  O   . PRO A 152 ? 0.1601 0.1601 0.2720 -0.0254 0.0130  -0.0335 152 PRO A O   
2451 C  CB  . PRO A 152 ? 0.2117 0.1758 0.2318 -0.0086 -0.0225 -0.0427 152 PRO A CB  
2452 C  CG  . PRO A 152 ? 0.2290 0.1724 0.2390 -0.0406 -0.0309 -0.0455 152 PRO A CG  
2453 C  CD  . PRO A 152 ? 0.1418 0.1696 0.2275 -0.0143 -0.0239 -0.0463 152 PRO A CD  
2461 N  N   . SER A 153 ? 0.1225 0.1696 0.2390 -0.0158 -0.0203 -0.0429 153 SER A N   
2462 C  CA  . SER A 153 ? 0.1250 0.2066 0.2818 -0.0053 -0.0153 -0.0555 153 SER A CA  
2463 C  C   . SER A 153 ? 0.1078 0.1847 0.2653 -0.0176 -0.0004 -0.0292 153 SER A C   
2464 O  O   . SER A 153 ? 0.1147 0.2005 0.2735 -0.0254 -0.0017 -0.0241 153 SER A O   
2465 C  CB  . SER A 153 ? 0.1572 0.2892 0.2952 0.0335  -0.0272 -0.0626 153 SER A CB  
2466 O  OG  . SER A 153 ? 0.2383 0.3159 0.3365 0.0752  -0.0734 -0.0332 153 SER A OG  
2472 N  N   . ASP A 154 ? 0.1064 0.1556 0.2416 -0.0126 -0.0063 -0.0290 154 ASP A N   
2473 C  CA  . ASP A 154 ? 0.1100 0.1416 0.2285 -0.0062 -0.0067 -0.0198 154 ASP A CA  
2474 C  C   . ASP A 154 ? 0.0952 0.1291 0.2538 -0.0007 0.0001  -0.0053 154 ASP A C   
2475 O  O   . ASP A 154 ? 0.1082 0.1276 0.2534 -0.0060 -0.0027 -0.0088 154 ASP A O   
2476 C  CB  . ASP A 154 ? 0.1257 0.1480 0.2176 -0.0118 -0.0139 -0.0190 154 ASP A CB  
2477 C  CG  . ASP A 154 ? 0.1059 0.1585 0.2426 -0.0022 -0.0202 -0.0087 154 ASP A CG  
2478 O  OD1 . ASP A 154 ? 0.1237 0.1834 0.2740 0.0144  -0.0002 -0.0104 154 ASP A OD1 
2479 O  OD2 . ASP A 154 ? 0.1362 0.1663 0.2874 0.0027  -0.0202 0.0110  154 ASP A OD2 
2484 N  N   . GLU A 155 ? 0.1149 0.1291 0.2610 -0.0053 0.0055  -0.0124 155 GLU A N   
2485 C  CA  . GLU A 155 ? 0.1048 0.1220 0.2843 0.0049  0.0179  -0.0037 155 GLU A CA  
2486 C  C   . GLU A 155 ? 0.0879 0.1202 0.2829 0.0090  0.0055  0.0043  155 GLU A C   
2487 O  O   . GLU A 155 ? 0.0924 0.1341 0.2945 0.0024  0.0026  0.0071  155 GLU A O   
2488 C  CB  . GLU A 155 ? 0.1387 0.1374 0.3083 -0.0006 0.0250  -0.0181 155 GLU A CB  
2489 C  CG  . GLU A 155 ? 0.1533 0.1435 0.3502 0.0076  0.0409  -0.0066 155 GLU A CG  
2490 C  CD  . GLU A 155 ? 0.1412 0.1521 0.4302 -0.0054 0.0242  -0.0486 155 GLU A CD  
2491 O  OE1 . GLU A 155 ? 0.1892 0.2289 0.5503 0.0335  -0.0605 -0.1424 155 GLU A OE1 
2492 O  OE2 . GLU A 155 ? 0.1587 0.1857 0.4133 -0.0327 0.0562  -0.0840 155 GLU A OE2 
2499 N  N   . THR A 156 ? 0.1004 0.1369 0.2805 -0.0134 0.0037  0.0046  156 THR A N   
2500 C  CA  . THR A 156 ? 0.1072 0.1603 0.2805 -0.0197 0.0093  0.0073  156 THR A CA  
2501 C  C   . THR A 156 ? 0.0852 0.1775 0.2741 -0.0024 0.0155  0.0153  156 THR A C   
2502 O  O   . THR A 156 ? 0.0999 0.1642 0.2716 -0.0147 0.0161  0.0057  156 THR A O   
2503 C  CB  . THR A 156 ? 0.1400 0.1532 0.3178 -0.0371 0.0104  0.0184  156 THR A CB  
2504 O  OG1 . THR A 156 ? 0.1822 0.2143 0.3386 -0.0780 -0.0057 -0.0188 156 THR A OG1 
2505 C  CG2 . THR A 156 ? 0.1321 0.2001 0.3352 -0.0391 0.0108  0.0159  156 THR A CG2 
2513 N  N   . ALA A 157 ? 0.0915 0.1634 0.2634 -0.0087 0.0144  0.0038  157 ALA A N   
2514 C  CA  . ALA A 157 ? 0.0990 0.1550 0.2774 0.0137  0.0087  0.0052  157 ALA A CA  
2515 C  C   . ALA A 157 ? 0.0973 0.1319 0.2638 0.0066  0.0138  0.0115  157 ALA A C   
2516 O  O   . ALA A 157 ? 0.0998 0.1419 0.2639 0.0083  0.0279  0.0091  157 ALA A O   
2517 C  CB  . ALA A 157 ? 0.1095 0.1543 0.3035 0.0152  -0.0101 -0.0150 157 ALA A CB  
2523 N  N   . PHE A 158 ? 0.0810 0.1302 0.2377 0.0067  0.0054  0.0146  158 PHE A N   
2524 C  CA  . PHE A 158 ? 0.0863 0.1313 0.2270 0.0078  0.0058  0.0168  158 PHE A CA  
2525 C  C   . PHE A 158 ? 0.0781 0.1212 0.2207 -0.0026 0.0239  0.0161  158 PHE A C   
2526 O  O   . PHE A 158 ? 0.0919 0.1320 0.2143 -0.0015 0.0202  0.0273  158 PHE A O   
2527 C  CB  . PHE A 158 ? 0.0870 0.1261 0.2111 -0.0007 0.0055  0.0117  158 PHE A CB  
2528 C  CG  . PHE A 158 ? 0.0933 0.1062 0.1884 -0.0027 0.0155  0.0168  158 PHE A CG  
2529 C  CD1 . PHE A 158 ? 0.0953 0.1081 0.2003 0.0005  0.0054  0.0123  158 PHE A CD1 
2530 C  CD2 . PHE A 158 ? 0.1067 0.1114 0.1830 0.0017  0.0087  0.0139  158 PHE A CD2 
2531 C  CE1 . PHE A 158 ? 0.1038 0.1179 0.1844 -0.0130 0.0088  0.0057  158 PHE A CE1 
2532 C  CE2 . PHE A 158 ? 0.0970 0.1157 0.1861 0.0020  0.0158  0.0161  158 PHE A CE2 
2533 C  CZ  . PHE A 158 ? 0.0896 0.1230 0.1890 0.0031  0.0016  0.0218  158 PHE A CZ  
2543 N  N   . ASN A 159 ? 0.0873 0.1290 0.2210 -0.0054 0.0202  0.0259  159 ASN A N   
2544 C  CA  . ASN A 159 ? 0.1034 0.1328 0.2454 -0.0027 0.0244  0.0308  159 ASN A CA  
2545 C  C   . ASN A 159 ? 0.1134 0.1358 0.2520 -0.0214 0.0327  0.0269  159 ASN A C   
2546 O  O   . ASN A 159 ? 0.1389 0.1371 0.2390 -0.0174 0.0335  0.0403  159 ASN A O   
2547 C  CB  . ASN A 159 ? 0.1119 0.1381 0.2533 -0.0085 0.0265  0.0210  159 ASN A CB  
2548 C  CG  . ASN A 159 ? 0.1189 0.1171 0.2746 -0.0029 0.0291  0.0199  159 ASN A CG  
2549 O  OD1 . ASN A 159 ? 0.1132 0.1554 0.2568 0.0024  0.0289  0.0163  159 ASN A OD1 
2550 N  ND2 . ASN A 159 ? 0.1427 0.1404 0.2943 -0.0142 0.0365  0.0068  159 ASN A ND2 
2557 N  N   . ARG A 160 ? 0.1113 0.1296 0.2560 -0.0168 0.0462  0.0204  160 ARG A N   
2558 C  CA  . ARG A 160 ? 0.1296 0.1592 0.2643 -0.0167 0.0657  0.0219  160 ARG A CA  
2559 C  C   . ARG A 160 ? 0.1275 0.1483 0.2573 -0.0081 0.0612  0.0163  160 ARG A C   
2560 O  O   . ARG A 160 ? 0.1435 0.1658 0.2490 -0.0206 0.0684  0.0254  160 ARG A O   
2561 C  CB  . ARG A 160 ? 0.1254 0.1788 0.3086 -0.0263 0.0657  -0.0022 160 ARG A CB  
2562 C  CG  . ARG A 160 ? 0.1387 0.2046 0.3746 -0.0447 0.0638  -0.0002 160 ARG A CG  
2563 C  CD  . ARG A 160 ? 0.1545 0.2104 0.3529 -0.0264 0.0814  -0.0087 160 ARG A CD  
2564 N  NE  . ARG A 160 ? 0.1499 0.2301 0.2972 -0.0026 0.0545  -0.0130 160 ARG A NE  
2565 C  CZ  . ARG A 160 ? 0.1610 0.2512 0.3154 -0.0042 0.0678  -0.0239 160 ARG A CZ  
2566 N  NH1 . ARG A 160 ? 0.1413 0.2662 0.3408 0.0077  0.0332  -0.0389 160 ARG A NH1 
2567 N  NH2 . ARG A 160 ? 0.1574 0.2863 0.3630 0.0284  0.0331  -0.0082 160 ARG A NH2 
2581 N  N   . LEU A 161 ? 0.1062 0.1403 0.2341 -0.0033 0.0412  0.0260  161 LEU A N   
2582 C  CA  . LEU A 161 ? 0.1095 0.1292 0.2229 -0.0022 0.0333  0.0274  161 LEU A CA  
2583 C  C   . LEU A 161 ? 0.1224 0.1335 0.2100 0.0017  0.0426  0.0409  161 LEU A C   
2584 O  O   . LEU A 161 ? 0.1335 0.1405 0.1978 0.0163  0.0394  0.0279  161 LEU A O   
2585 C  CB  . LEU A 161 ? 0.1063 0.1244 0.2214 0.0062  0.0276  0.0309  161 LEU A CB  
2586 C  CG  . LEU A 161 ? 0.1139 0.1332 0.2230 0.0101  0.0187  0.0227  161 LEU A CG  
2587 C  CD1 . LEU A 161 ? 0.1292 0.1329 0.2343 0.0259  0.0085  0.0083  161 LEU A CD1 
2588 C  CD2 . LEU A 161 ? 0.1059 0.1309 0.2475 -0.0061 0.0098  0.0416  161 LEU A CD2 
2600 N  N   . LEU A 162 ? 0.1086 0.1300 0.2048 0.0047  0.0355  0.0247  162 LEU A N   
2601 C  CA  . LEU A 162 ? 0.1210 0.1228 0.2127 0.0076  0.0289  0.0261  162 LEU A CA  
2602 C  C   . LEU A 162 ? 0.1455 0.1363 0.2099 0.0102  0.0439  0.0257  162 LEU A C   
2603 O  O   . LEU A 162 ? 0.1644 0.1449 0.1993 0.0122  0.0337  0.0358  162 LEU A O   
2604 C  CB  . LEU A 162 ? 0.1304 0.1178 0.2116 0.0012  0.0241  0.0308  162 LEU A CB  
2605 C  CG  . LEU A 162 ? 0.1152 0.1309 0.2080 0.0047  0.0287  0.0304  162 LEU A CG  
2606 C  CD1 . LEU A 162 ? 0.1407 0.1358 0.2216 -0.0078 0.0198  0.0188  162 LEU A CD1 
2607 C  CD2 . LEU A 162 ? 0.1390 0.1417 0.2180 -0.0041 0.0432  0.0182  162 LEU A CD2 
2619 N  N   . ALA A 163 ? 0.1592 0.1350 0.2164 -0.0065 0.0403  0.0276  163 ALA A N   
2620 C  CA  . ALA A 163 ? 0.1851 0.1506 0.2240 -0.0168 0.0403  0.0445  163 ALA A CA  
2621 C  C   . ALA A 163 ? 0.1742 0.1585 0.2254 -0.0192 0.0507  0.0497  163 ALA A C   
2622 O  O   . ALA A 163 ? 0.2153 0.1682 0.2127 -0.0058 0.0572  0.0422  163 ALA A O   
2623 C  CB  . ALA A 163 ? 0.2153 0.1668 0.2456 -0.0360 0.0572  0.0408  163 ALA A CB  
2629 N  N   . GLU A 164 ? 0.1553 0.1513 0.2205 -0.0126 0.0597  0.0223  164 GLU A N   
2630 C  CA  . GLU A 164 ? 0.1529 0.1561 0.2122 0.0001  0.0595  0.0387  164 GLU A CA  
2631 C  C   . GLU A 164 ? 0.1539 0.1553 0.2017 0.0048  0.0601  0.0394  164 GLU A C   
2632 O  O   . GLU A 164 ? 0.1543 0.1789 0.2057 0.0035  0.0658  0.0477  164 GLU A O   
2633 C  CB  . GLU A 164 ? 0.1429 0.1668 0.2384 0.0067  0.0536  0.0181  164 GLU A CB  
2634 C  CG  . GLU A 164 ? 0.1474 0.2062 0.2672 0.0014  0.0504  0.0237  164 GLU A CG  
2635 C  CD  . GLU A 164 ? 0.1528 0.2168 0.2753 -0.0039 0.0589  0.0161  164 GLU A CD  
2636 O  OE1 . GLU A 164 ? 0.1603 0.2597 0.2978 0.0312  0.0447  -0.0022 164 GLU A OE1 
2637 O  OE2 . GLU A 164 ? 0.1988 0.2563 0.2716 0.0349  0.0677  0.0260  164 GLU A OE2 
2644 N  N   . LEU A 165 ? 0.1352 0.1433 0.1943 0.0021  0.0518  0.0319  165 LEU A N   
2645 C  CA  . LEU A 165 ? 0.1350 0.1567 0.1864 0.0019  0.0439  0.0405  165 LEU A CA  
2646 C  C   . LEU A 165 ? 0.1399 0.1638 0.1809 0.0031  0.0519  0.0441  165 LEU A C   
2647 O  O   . LEU A 165 ? 0.1478 0.1715 0.1727 0.0005  0.0390  0.0412  165 LEU A O   
2648 C  CB  . LEU A 165 ? 0.1209 0.1692 0.1777 -0.0035 0.0297  0.0383  165 LEU A CB  
2649 C  CG  . LEU A 165 ? 0.1423 0.1584 0.2001 0.0041  0.0472  0.0497  165 LEU A CG  
2650 C  CD1 . LEU A 165 ? 0.1493 0.2075 0.2100 0.0005  0.0449  0.0538  165 LEU A CD1 
2651 C  CD2 . LEU A 165 ? 0.2224 0.1566 0.2289 0.0339  0.0310  0.0363  165 LEU A CD2 
2663 N  N   . ARG A 166 ? 0.1384 0.1518 0.1891 -0.0024 0.0396  0.0379  166 ARG A N   
2664 C  CA  . ARG A 166 ? 0.1518 0.1614 0.1856 -0.0005 0.0403  0.0401  166 ARG A CA  
2665 C  C   . ARG A 166 ? 0.1770 0.1610 0.1947 0.0017  0.0443  0.0432  166 ARG A C   
2666 O  O   . ARG A 166 ? 0.1901 0.1774 0.1974 0.0104  0.0348  0.0476  166 ARG A O   
2667 C  CB  . ARG A 166 ? 0.1560 0.1624 0.1974 0.0070  0.0311  0.0323  166 ARG A CB  
2668 C  CG  . ARG A 166 ? 0.1540 0.1531 0.1952 0.0032  0.0259  0.0277  166 ARG A CG  
2669 C  CD  . ARG A 166 ? 0.1683 0.1392 0.2047 0.0100  0.0272  0.0346  166 ARG A CD  
2670 N  NE  . ARG A 166 ? 0.1545 0.1363 0.2084 0.0233  0.0350  0.0231  166 ARG A NE  
2671 C  CZ  . ARG A 166 ? 0.1451 0.1267 0.2016 0.0213  0.0248  0.0227  166 ARG A CZ  
2672 N  NH1 . ARG A 166 ? 0.1627 0.1469 0.2194 0.0074  0.0130  0.0169  166 ARG A NH1 
2673 N  NH2 . ARG A 166 ? 0.1528 0.1296 0.2109 0.0222  0.0286  0.0260  166 ARG A NH2 
2687 N  N   . ALA A 167 ? 0.1723 0.1632 0.1981 -0.0030 0.0582  0.0456  167 ALA A N   
2688 C  CA  . ALA A 167 ? 0.1903 0.1784 0.2054 -0.0199 0.0661  0.0465  167 ALA A CA  
2689 C  C   . ALA A 167 ? 0.1887 0.1742 0.2176 -0.0065 0.0814  0.0403  167 ALA A C   
2690 O  O   . ALA A 167 ? 0.2355 0.2030 0.2113 -0.0283 0.0823  0.0460  167 ALA A O   
2691 C  CB  . ALA A 167 ? 0.1958 0.2060 0.2105 -0.0198 0.0667  0.0399  167 ALA A CB  
2697 N  N   . SER A 168 ? 0.1766 0.1688 0.2008 -0.0110 0.0644  0.0469  168 SER A N   
2698 C  CA  . SER A 168 ? 0.1789 0.1750 0.2051 -0.0036 0.0680  0.0336  168 SER A CA  
2699 C  C   . SER A 168 ? 0.1758 0.1597 0.1927 -0.0030 0.0689  0.0306  168 SER A C   
2700 O  O   . SER A 168 ? 0.1746 0.1727 0.2140 0.0013  0.0723  0.0302  168 SER A O   
2701 C  CB  . SER A 168 ? 0.2040 0.1710 0.2125 0.0022  0.0852  0.0320  168 SER A CB  
2702 O  OG  . SER A 168 ? 0.1954 0.1769 0.2093 -0.0290 0.0711  0.0229  168 SER A OG  
2708 N  N   . VAL A 169 ? 0.1746 0.1824 0.1821 0.0070  0.0610  0.0357  169 VAL A N   
2709 C  CA  . VAL A 169 ? 0.1883 0.1992 0.1727 0.0262  0.0435  0.0517  169 VAL A CA  
2710 C  C   . VAL A 169 ? 0.1714 0.1867 0.1641 0.0228  0.0349  0.0360  169 VAL A C   
2711 O  O   . VAL A 169 ? 0.1822 0.1803 0.1687 0.0238  0.0270  0.0401  169 VAL A O   
2712 C  CB  . VAL A 169 ? 0.2165 0.2280 0.1687 0.0260  0.0482  0.0428  169 VAL A CB  
2713 C  CG1 . VAL A 169 ? 0.2347 0.2417 0.1913 0.0256  0.0559  0.0544  169 VAL A CG1 
2714 C  CG2 . VAL A 169 ? 0.2197 0.2758 0.2094 0.0067  0.0522  0.0294  169 VAL A CG2 
2724 N  N   . GLU A 170 ? 0.1606 0.1706 0.1642 0.0131  0.0389  0.0333  170 GLU A N   
2725 C  CA  . GLU A 170 ? 0.1479 0.1672 0.1644 0.0080  0.0327  0.0279  170 GLU A CA  
2726 C  C   . GLU A 170 ? 0.1451 0.1645 0.1521 0.0136  0.0323  0.0390  170 GLU A C   
2727 O  O   . GLU A 170 ? 0.1404 0.1557 0.1649 0.0121  0.0260  0.0388  170 GLU A O   
2728 C  CB  . GLU A 170 ? 0.1539 0.1526 0.1782 0.0171  0.0315  0.0322  170 GLU A CB  
2729 C  CG  . GLU A 170 ? 0.1389 0.1661 0.1813 0.0223  0.0263  0.0384  170 GLU A CG  
2730 C  CD  . GLU A 170 ? 0.1415 0.1648 0.1950 0.0259  0.0281  0.0483  170 GLU A CD  
2731 O  OE1 . GLU A 170 ? 0.1486 0.2064 0.2040 0.0418  0.0446  0.0730  170 GLU A OE1 
2732 O  OE2 . GLU A 170 ? 0.1503 0.1821 0.1853 0.0231  0.0299  0.0533  170 GLU A OE2 
2739 N  N   . TRP A 171 ? 0.1358 0.1600 0.1700 0.0141  0.0325  0.0338  171 TRP A N   
2740 C  CA  . TRP A 171 ? 0.1495 0.1470 0.1747 0.0088  0.0385  0.0394  171 TRP A CA  
2741 C  C   . TRP A 171 ? 0.1395 0.1629 0.1868 0.0095  0.0411  0.0446  171 TRP A C   
2742 O  O   . TRP A 171 ? 0.1549 0.1610 0.2074 0.0225  0.0378  0.0502  171 TRP A O   
2743 C  CB  . TRP A 171 ? 0.1401 0.1542 0.1959 0.0031  0.0378  0.0247  171 TRP A CB  
2744 C  CG  . TRP A 171 ? 0.1283 0.1680 0.1829 0.0050  0.0314  0.0196  171 TRP A CG  
2745 C  CD1 . TRP A 171 ? 0.1362 0.1890 0.1835 0.0039  0.0220  0.0061  171 TRP A CD1 
2746 C  CD2 . TRP A 171 ? 0.1338 0.1673 0.1856 0.0030  0.0311  0.0307  171 TRP A CD2 
2747 N  NE1 . TRP A 171 ? 0.1485 0.1977 0.1798 0.0044  0.0347  0.0094  171 TRP A NE1 
2748 C  CE2 . TRP A 171 ? 0.1207 0.1977 0.1835 0.0081  0.0338  0.0214  171 TRP A CE2 
2749 C  CE3 . TRP A 171 ? 0.1321 0.1806 0.1861 0.0108  0.0333  0.0323  171 TRP A CE3 
2750 C  CZ2 . TRP A 171 ? 0.1355 0.2354 0.1836 0.0111  0.0183  0.0277  171 TRP A CZ2 
2751 C  CZ3 . TRP A 171 ? 0.1421 0.2052 0.1975 0.0127  0.0270  0.0567  171 TRP A CZ3 
2752 C  CH2 . TRP A 171 ? 0.1544 0.2124 0.1880 -0.0018 0.0176  0.0559  171 TRP A CH2 
2763 N  N   . GLN A 172 ? 0.1474 0.1724 0.1794 0.0017  0.0360  0.0586  172 GLN A N   
2764 C  CA  . GLN A 172 ? 0.1701 0.2103 0.1864 0.0146  0.0426  0.0798  172 GLN A CA  
2765 C  C   . GLN A 172 ? 0.1685 0.1597 0.1849 0.0152  0.0327  0.0664  172 GLN A C   
2766 O  O   . GLN A 172 ? 0.1814 0.1742 0.2148 0.0181  0.0344  0.0882  172 GLN A O   
2767 C  CB  . GLN A 172 ? 0.2002 0.2202 0.1964 0.0338  0.0519  0.0822  172 GLN A CB  
2768 C  CG  . GLN A 172 ? 0.2182 0.2984 0.2354 0.0293  0.0982  0.1043  172 GLN A CG  
2769 C  CD  . GLN A 172 ? 0.2758 0.3289 0.2485 0.0702  0.0878  0.0962  172 GLN A CD  
2770 O  OE1 . GLN A 172 ? 0.3197 0.4432 0.2738 0.0805  0.0777  0.0558  172 GLN A OE1 
2771 N  NE2 . GLN A 172 ? 0.3133 0.3366 0.2701 0.0876  0.1279  0.1094  172 GLN A NE2 
2780 N  N   . TYR A 173 ? 0.1474 0.1591 0.1597 0.0118  0.0326  0.0508  173 TYR A N   
2781 C  CA  . TYR A 173 ? 0.1458 0.1806 0.1610 0.0093  0.0259  0.0433  173 TYR A CA  
2782 C  C   . TYR A 173 ? 0.1458 0.1668 0.1504 0.0146  0.0213  0.0426  173 TYR A C   
2783 O  O   . TYR A 173 ? 0.1372 0.2051 0.1669 -0.0070 0.0217  0.0349  173 TYR A O   
2784 C  CB  . TYR A 173 ? 0.1620 0.1633 0.1700 0.0082  0.0182  0.0511  173 TYR A CB  
2785 C  CG  . TYR A 173 ? 0.1724 0.1466 0.1614 0.0041  0.0056  0.0471  173 TYR A CG  
2786 C  CD1 . TYR A 173 ? 0.1825 0.1675 0.1645 0.0226  0.0134  0.0382  173 TYR A CD1 
2787 C  CD2 . TYR A 173 ? 0.2013 0.1576 0.1856 0.0085  -0.0025 0.0417  173 TYR A CD2 
2788 C  CE1 . TYR A 173 ? 0.2155 0.1791 0.1666 0.0285  0.0213  0.0390  173 TYR A CE1 
2789 C  CE2 . TYR A 173 ? 0.2182 0.1731 0.1787 0.0226  -0.0232 0.0303  173 TYR A CE2 
2790 C  CZ  . TYR A 173 ? 0.2374 0.1850 0.1699 0.0393  0.0134  0.0411  173 TYR A CZ  
2791 O  OH  . TYR A 173 ? 0.3046 0.2446 0.1703 0.0490  0.0058  0.0250  173 TYR A OH  
2801 N  N   . VAL A 174 ? 0.1333 0.1608 0.1640 0.0054  0.0238  0.0377  174 VAL A N   
2802 C  CA  . VAL A 174 ? 0.1351 0.1629 0.1629 0.0049  0.0191  0.0457  174 VAL A CA  
2803 C  C   . VAL A 174 ? 0.1485 0.1562 0.1657 -0.0008 0.0257  0.0477  174 VAL A C   
2804 O  O   . VAL A 174 ? 0.1616 0.1574 0.2095 -0.0065 0.0372  0.0541  174 VAL A O   
2805 C  CB  . VAL A 174 ? 0.1269 0.1586 0.1726 -0.0075 0.0250  0.0414  174 VAL A CB  
2806 C  CG1 . VAL A 174 ? 0.1398 0.1544 0.1716 -0.0036 0.0172  0.0298  174 VAL A CG1 
2807 C  CG2 . VAL A 174 ? 0.1343 0.1758 0.1817 0.0100  0.0176  0.0499  174 VAL A CG2 
2817 N  N   . ASP A 175 ? 0.1351 0.1459 0.1727 0.0069  0.0113  0.0466  175 ASP A N   
2818 C  CA  . ASP A 175 ? 0.1618 0.1425 0.1821 0.0021  0.0077  0.0501  175 ASP A CA  
2819 C  C   . ASP A 175 ? 0.1530 0.1314 0.1899 0.0051  0.0131  0.0409  175 ASP A C   
2820 O  O   . ASP A 175 ? 0.1698 0.1396 0.2167 0.0217  0.0195  0.0419  175 ASP A O   
2821 C  CB  . ASP A 175 ? 0.1745 0.1685 0.1931 0.0280  -0.0149 0.0511  175 ASP A CB  
2822 C  CG  . ASP A 175 ? 0.1746 0.1665 0.1991 0.0305  -0.0273 0.0445  175 ASP A CG  
2823 O  OD1 . ASP A 175 ? 0.1582 0.1905 0.2048 0.0107  -0.0138 0.0530  175 ASP A OD1 
2824 O  OD2 . ASP A 175 ? 0.1844 0.2174 0.2339 0.0199  -0.0488 0.0614  175 ASP A OD2 
2829 N  N   . ARG A 176 ? 0.1382 0.1288 0.1683 0.0039  0.0075  0.0326  176 ARG A N   
2830 C  CA  . ARG A 176 ? 0.1348 0.1306 0.1918 -0.0142 0.0067  0.0137  176 ARG A CA  
2831 C  C   . ARG A 176 ? 0.1458 0.1324 0.1677 -0.0280 -0.0020 0.0331  176 ARG A C   
2832 O  O   . ARG A 176 ? 0.1919 0.1137 0.1798 -0.0422 -0.0076 0.0374  176 ARG A O   
2833 C  CB  . ARG A 176 ? 0.1655 0.1816 0.2266 -0.0151 0.0297  -0.0292 176 ARG A CB  
2834 C  CG  . ARG A 176 ? 0.2281 0.1489 0.2454 -0.0074 -0.0054 -0.0015 176 ARG A CG  
2835 C  CD  . ARG A 176 ? 0.1757 0.2258 0.3012 0.0016  -0.0110 -0.0035 176 ARG A CD  
2836 N  NE  . ARG A 176 ? 0.0983 0.1762 0.2988 0.0122  -0.0056 0.0448  176 ARG A NE  
2837 C  CZ  . ARG A 176 ? 0.1337 0.3048 0.3941 0.0005  -0.0241 0.0764  176 ARG A CZ  
2838 N  NH1 . ARG A 176 ? 0.1591 0.3455 0.4069 -0.0071 0.0308  0.0507  176 ARG A NH1 
2839 N  NH2 . ARG A 176 ? 0.2227 0.2158 0.4806 -0.0198 -0.1071 0.1215  176 ARG A NH2 
2853 N  N   . GLU A 177 ? 0.1600 0.1119 0.1746 -0.0165 -0.0083 0.0365  177 GLU A N   
2854 C  CA  . GLU A 177 ? 0.1616 0.1175 0.1775 -0.0167 -0.0041 0.0369  177 GLU A CA  
2855 C  C   . GLU A 177 ? 0.1577 0.1064 0.1814 -0.0091 -0.0046 0.0347  177 GLU A C   
2856 O  O   . GLU A 177 ? 0.1907 0.1067 0.1984 -0.0208 -0.0046 0.0356  177 GLU A O   
2857 C  CB  . GLU A 177 ? 0.1748 0.1188 0.1793 -0.0076 0.0062  0.0433  177 GLU A CB  
2858 C  CG  . GLU A 177 ? 0.1675 0.1263 0.1802 -0.0051 0.0105  0.0318  177 GLU A CG  
2859 C  CD  . GLU A 177 ? 0.1849 0.1228 0.1916 0.0141  0.0213  0.0396  177 GLU A CD  
2860 O  OE1 . GLU A 177 ? 0.2259 0.1742 0.1869 0.0508  0.0260  0.0240  177 GLU A OE1 
2861 O  OE2 . GLU A 177 ? 0.1509 0.1644 0.2072 0.0058  0.0249  0.0428  177 GLU A OE2 
2868 N  N   . ILE A 178 ? 0.1496 0.0952 0.1851 -0.0010 -0.0067 0.0253  178 ILE A N   
2869 C  CA  . ILE A 178 ? 0.1422 0.1003 0.1970 0.0037  0.0028  0.0256  178 ILE A CA  
2870 C  C   . ILE A 178 ? 0.1230 0.0980 0.1888 -0.0050 0.0006  0.0191  178 ILE A C   
2871 O  O   . ILE A 178 ? 0.1361 0.1055 0.2263 -0.0079 -0.0162 0.0372  178 ILE A O   
2872 C  CB  . ILE A 178 ? 0.1463 0.1468 0.2223 0.0242  0.0041  0.0110  178 ILE A CB  
2873 C  CG1 . ILE A 178 ? 0.1841 0.1572 0.2681 0.0457  -0.0022 0.0315  178 ILE A CG1 
2874 C  CG2 . ILE A 178 ? 0.2233 0.1887 0.2569 0.0327  0.0136  -0.0154 178 ILE A CG2 
2875 C  CD1 . ILE A 178 ? 0.1990 0.2000 0.3048 0.0487  -0.0087 0.0133  178 ILE A CD1 
2887 N  N   . ASP A 179 ? 0.1354 0.1076 0.1982 -0.0019 -0.0135 0.0143  179 ASP A N   
2888 C  CA  . ASP A 179 ? 0.1179 0.1295 0.2057 0.0113  0.0016  0.0022  179 ASP A CA  
2889 C  C   . ASP A 179 ? 0.1042 0.1142 0.1901 0.0017  -0.0002 0.0142  179 ASP A C   
2890 O  O   . ASP A 179 ? 0.1457 0.1223 0.2063 -0.0166 -0.0014 0.0147  179 ASP A O   
2891 C  CB  . ASP A 179 ? 0.1368 0.1672 0.2116 0.0217  0.0253  0.0166  179 ASP A CB  
2892 C  CG  . ASP A 179 ? 0.1304 0.1768 0.2072 0.0149  0.0144  -0.0013 179 ASP A CG  
2893 O  OD1 . ASP A 179 ? 0.1283 0.1853 0.2165 0.0186  0.0110  0.0281  179 ASP A OD1 
2894 O  OD2 . ASP A 179 ? 0.1349 0.1930 0.2338 0.0131  0.0194  0.0292  179 ASP A OD2 
2899 N  N   . ILE A 180 ? 0.1157 0.1012 0.1767 0.0030  0.0057  -0.0010 180 ILE A N   
2900 C  CA  . ILE A 180 ? 0.1059 0.0945 0.1912 -0.0009 -0.0005 0.0000  180 ILE A CA  
2901 C  C   . ILE A 180 ? 0.1118 0.0960 0.1858 -0.0006 0.0066  0.0036  180 ILE A C   
2902 O  O   . ILE A 180 ? 0.1188 0.0924 0.2086 0.0039  -0.0104 0.0056  180 ILE A O   
2903 C  CB  . ILE A 180 ? 0.1109 0.1127 0.1966 0.0092  0.0047  0.0007  180 ILE A CB  
2904 C  CG1 . ILE A 180 ? 0.1107 0.1398 0.2123 0.0131  0.0017  0.0162  180 ILE A CG1 
2905 C  CG2 . ILE A 180 ? 0.1377 0.1455 0.1959 0.0098  0.0164  -0.0008 180 ILE A CG2 
2906 C  CD1 . ILE A 180 ? 0.1271 0.1753 0.2366 0.0065  0.0006  0.0184  180 ILE A CD1 
2918 N  N   . ARG A 181 ? 0.1133 0.0902 0.1900 -0.0025 0.0063  -0.0051 181 ARG A N   
2919 C  CA  . ARG A 181 ? 0.1124 0.0975 0.1884 0.0024  0.0000  -0.0045 181 ARG A CA  
2920 C  C   . ARG A 181 ? 0.1075 0.1052 0.1843 0.0011  0.0024  -0.0149 181 ARG A C   
2921 O  O   . ARG A 181 ? 0.1297 0.1082 0.1931 0.0102  -0.0035 -0.0148 181 ARG A O   
2922 C  CB  . ARG A 181 ? 0.1227 0.1064 0.1983 -0.0051 0.0028  -0.0096 181 ARG A CB  
2923 C  CG  . ARG A 181 ? 0.1157 0.1070 0.2093 -0.0076 0.0047  0.0008  181 ARG A CG  
2924 C  CD  . ARG A 181 ? 0.1165 0.1217 0.1913 -0.0005 0.0018  -0.0046 181 ARG A CD  
2925 N  NE  . ARG A 181 ? 0.1115 0.1331 0.1943 -0.0003 0.0032  -0.0045 181 ARG A NE  
2926 C  CZ  . ARG A 181 ? 0.1102 0.1188 0.2052 0.0000  0.0090  -0.0020 181 ARG A CZ  
2927 N  NH1 . ARG A 181 ? 0.1115 0.1360 0.2195 0.0038  0.0131  -0.0077 181 ARG A NH1 
2928 N  NH2 . ARG A 181 ? 0.1372 0.1759 0.2064 0.0155  0.0250  0.0180  181 ARG A NH2 
2942 N  N   . LEU A 182 ? 0.1150 0.1080 0.1779 0.0150  0.0036  -0.0150 182 LEU A N   
2943 C  CA  . LEU A 182 ? 0.1289 0.1235 0.1834 0.0127  0.0017  -0.0111 182 LEU A CA  
2944 C  C   . LEU A 182 ? 0.1326 0.1086 0.1781 0.0035  -0.0067 -0.0079 182 LEU A C   
2945 O  O   . LEU A 182 ? 0.1367 0.1234 0.1749 0.0244  -0.0066 -0.0159 182 LEU A O   
2946 C  CB  . LEU A 182 ? 0.1371 0.1515 0.1896 -0.0017 0.0089  -0.0050 182 LEU A CB  
2947 C  CG  . LEU A 182 ? 0.1372 0.1775 0.2438 0.0023  0.0031  -0.0494 182 LEU A CG  
2948 C  CD1 . LEU A 182 ? 0.1649 0.1493 0.2260 0.0096  -0.0041 -0.0204 182 LEU A CD1 
2949 C  CD2 . LEU A 182 ? 0.1423 0.1896 0.2257 0.0128  -0.0044 -0.0072 182 LEU A CD2 
2961 N  N   . VAL A 183 ? 0.1461 0.1188 0.1782 0.0094  -0.0075 -0.0173 183 VAL A N   
2962 C  CA  . VAL A 183 ? 0.1440 0.1184 0.1810 0.0063  -0.0082 -0.0120 183 VAL A CA  
2963 C  C   . VAL A 183 ? 0.1462 0.1322 0.1821 -0.0015 -0.0066 -0.0181 183 VAL A C   
2964 O  O   . VAL A 183 ? 0.1445 0.1474 0.1798 0.0096  0.0001  -0.0128 183 VAL A O   
2965 C  CB  . VAL A 183 ? 0.1902 0.1511 0.1997 -0.0284 -0.0098 -0.0299 183 VAL A CB  
2966 C  CG1 . VAL A 183 ? 0.2135 0.2372 0.2658 -0.0265 -0.0266 -0.0063 183 VAL A CG1 
2967 C  CG2 . VAL A 183 ? 0.1792 0.1665 0.2188 -0.0304 -0.0115 -0.0076 183 VAL A CG2 
2977 N  N   . HIS A 184 ? 0.1532 0.1491 0.1775 0.0072  -0.0040 -0.0043 184 HIS A N   
2978 C  CA  . HIS A 184 ? 0.1676 0.1413 0.1855 -0.0031 -0.0041 -0.0055 184 HIS A CA  
2979 C  C   . HIS A 184 ? 0.1573 0.1650 0.1841 -0.0125 -0.0077 -0.0043 184 HIS A C   
2980 O  O   . HIS A 184 ? 0.1719 0.1766 0.1773 -0.0265 -0.0208 -0.0107 184 HIS A O   
2981 C  CB  . HIS A 184 ? 0.1822 0.1527 0.1744 -0.0014 -0.0101 0.0078  184 HIS A CB  
2982 C  CG  . HIS A 184 ? 0.1812 0.1650 0.1956 -0.0182 -0.0269 0.0215  184 HIS A CG  
2983 N  ND1 . HIS A 184 ? 0.2415 0.1942 0.1949 -0.0558 -0.0187 0.0154  184 HIS A ND1 
2984 C  CD2 . HIS A 184 ? 0.2025 0.1821 0.2219 -0.0481 -0.0154 0.0203  184 HIS A CD2 
2985 C  CE1 . HIS A 184 ? 0.2370 0.2240 0.2118 -0.0622 -0.0173 0.0319  184 HIS A CE1 
2986 N  NE2 . HIS A 184 ? 0.2243 0.1842 0.2316 -0.0587 -0.0136 0.0170  184 HIS A NE2 
2994 N  N   . GLU A 185 ? 0.1796 0.1957 0.1868 -0.0189 0.0035  -0.0177 185 GLU A N   
2995 C  CA  . GLU A 185 ? 0.2179 0.2342 0.1892 -0.0286 -0.0056 -0.0347 185 GLU A CA  
2996 C  C   . GLU A 185 ? 0.2494 0.2161 0.1999 -0.0513 -0.0050 -0.0121 185 GLU A C   
2997 O  O   . GLU A 185 ? 0.2674 0.2094 0.2106 -0.0512 -0.0237 0.0071  185 GLU A O   
2998 C  CB  . GLU A 185 ? 0.2453 0.3057 0.2128 -0.0278 0.0262  -0.0067 185 GLU A CB  
2999 C  CG  . GLU A 185 ? 0.2693 0.3526 0.2317 -0.0451 0.0208  0.0180  185 GLU A CG  
3000 C  CD  . GLU A 185 ? 0.3124 0.4069 0.2638 -0.0221 0.0382  0.0194  185 GLU A CD  
3001 O  OE1 . GLU A 185 ? 0.3144 0.4389 0.3292 0.0194  0.0106  0.0065  185 GLU A OE1 
3002 O  OE2 . GLU A 185 ? 0.3816 0.4936 0.3642 -0.0792 0.0567  0.0525  185 GLU A OE2 
3009 N  N   . PRO A 186 ? 0.2792 0.2631 0.2198 -0.0799 -0.0400 -0.0105 186 PRO A N   
3010 C  CA  . PRO A 186 ? 0.3403 0.3069 0.2430 -0.0695 -0.0606 0.0002  186 PRO A CA  
3011 C  C   . PRO A 186 ? 0.3857 0.3732 0.2811 -0.1324 0.0058  -0.0164 186 PRO A C   
3012 O  O   . PRO A 186 ? 0.3574 0.4041 0.2465 -0.1675 -0.0084 0.0240  186 PRO A O   
3013 C  CB  . PRO A 186 ? 0.3573 0.3356 0.3014 -0.0891 -0.0957 -0.0237 186 PRO A CB  
3014 C  CG  . PRO A 186 ? 0.3933 0.3270 0.2730 -0.0832 -0.0764 -0.0223 186 PRO A CG  
3015 C  CD  . PRO A 186 ? 0.3223 0.2623 0.2447 -0.0795 -0.0305 -0.0326 186 PRO A CD  
3030 N  N   . ARG B 4   ? 0.1288 0.1894 0.2298 0.0253  -0.0170 0.0683  4   ARG B N   
3031 C  CA  . ARG B 4   ? 0.1109 0.1545 0.1799 0.0188  -0.0113 0.0323  4   ARG B CA  
3032 C  C   . ARG B 4   ? 0.1049 0.1414 0.1708 0.0155  -0.0035 0.0177  4   ARG B C   
3033 O  O   . ARG B 4   ? 0.1101 0.1312 0.1589 0.0257  -0.0054 0.0099  4   ARG B O   
3034 C  CB  . ARG B 4   ? 0.1302 0.1485 0.1694 0.0112  -0.0107 0.0310  4   ARG B CB  
3035 C  CG  . ARG B 4   ? 0.1304 0.1515 0.1775 0.0168  -0.0181 0.0312  4   ARG B CG  
3036 C  CD  . ARG B 4   ? 0.1282 0.1488 0.1811 0.0146  -0.0050 0.0260  4   ARG B CD  
3037 N  NE  . ARG B 4   ? 0.1333 0.1414 0.1612 0.0129  -0.0140 0.0129  4   ARG B NE  
3038 C  CZ  . ARG B 4   ? 0.1145 0.1229 0.1398 0.0018  0.0000  0.0072  4   ARG B CZ  
3039 N  NH1 . ARG B 4   ? 0.1273 0.1220 0.1530 0.0116  -0.0040 0.0150  4   ARG B NH1 
3040 N  NH2 . ARG B 4   ? 0.1107 0.1224 0.1614 0.0077  -0.0011 0.0044  4   ARG B NH2 
3053 N  N   . VAL B 5   ? 0.1207 0.1205 0.1915 0.0091  0.0121  0.0045  5   VAL B N   
3054 C  CA  . VAL B 5   ? 0.1245 0.1249 0.1715 0.0177  0.0019  0.0000  5   VAL B CA  
3055 C  C   . VAL B 5   ? 0.1092 0.1324 0.1706 0.0151  0.0082  0.0025  5   VAL B C   
3056 O  O   . VAL B 5   ? 0.1225 0.1385 0.1919 0.0229  -0.0016 0.0059  5   VAL B O   
3057 C  CB  . VAL B 5   ? 0.1282 0.1405 0.1936 0.0201  -0.0050 -0.0124 5   VAL B CB  
3058 C  CG1 . VAL B 5   ? 0.1434 0.1667 0.1848 0.0138  -0.0078 -0.0231 5   VAL B CG1 
3059 C  CG2 . VAL B 5   ? 0.1470 0.1854 0.2230 -0.0020 0.0018  -0.0530 5   VAL B CG2 
3069 N  N   . PHE B 6   ? 0.1102 0.1304 0.1531 0.0146  0.0048  0.0026  6   PHE B N   
3070 C  CA  . PHE B 6   ? 0.1077 0.1390 0.1623 0.0084  0.0003  -0.0019 6   PHE B CA  
3071 C  C   . PHE B 6   ? 0.1001 0.1330 0.1547 0.0113  0.0000  -0.0059 6   PHE B C   
3072 O  O   . PHE B 6   ? 0.1048 0.1482 0.1645 0.0159  0.0065  0.0057  6   PHE B O   
3073 C  CB  . PHE B 6   ? 0.1360 0.1573 0.1681 -0.0088 0.0008  -0.0036 6   PHE B CB  
3074 C  CG  . PHE B 6   ? 0.1341 0.1671 0.1721 0.0069  -0.0018 -0.0011 6   PHE B CG  
3075 C  CD1 . PHE B 6   ? 0.1573 0.1525 0.1677 0.0128  0.0116  0.0055  6   PHE B CD1 
3076 C  CD2 . PHE B 6   ? 0.1455 0.2365 0.1697 0.0147  -0.0153 0.0085  6   PHE B CD2 
3077 C  CE1 . PHE B 6   ? 0.1812 0.1978 0.1796 0.0136  0.0072  0.0158  6   PHE B CE1 
3078 C  CE2 . PHE B 6   ? 0.1709 0.2441 0.2082 0.0375  -0.0221 0.0235  6   PHE B CE2 
3079 C  CZ  . PHE B 6   ? 0.2092 0.2571 0.1889 0.0106  -0.0155 0.0305  6   PHE B CZ  
3089 N  N   . THR B 7   ? 0.0968 0.1387 0.1530 0.0076  0.0054  -0.0109 7   THR B N   
3090 C  CA  . THR B 7   ? 0.1040 0.1434 0.1621 0.0090  0.0090  -0.0021 7   THR B CA  
3091 C  C   . THR B 7   ? 0.0976 0.1390 0.1603 0.0113  0.0083  -0.0039 7   THR B C   
3092 O  O   . THR B 7   ? 0.1026 0.1576 0.1957 0.0096  -0.0056 0.0026  7   THR B O   
3093 C  CB  . THR B 7   ? 0.1233 0.1519 0.1717 0.0124  0.0021  -0.0140 7   THR B CB  
3094 O  OG1 . THR B 7   ? 0.1471 0.1618 0.1688 0.0044  0.0003  -0.0200 7   THR B OG1 
3095 C  CG2 . THR B 7   ? 0.1815 0.1835 0.1767 0.0080  0.0072  -0.0224 7   THR B CG2 
3103 N  N   . PHE B 8   ? 0.1004 0.1422 0.1636 0.0066  0.0181  -0.0006 8   PHE B N   
3104 C  CA  . PHE B 8   ? 0.1028 0.1438 0.1619 0.0078  0.0078  -0.0045 8   PHE B CA  
3105 C  C   . PHE B 8   ? 0.1118 0.1440 0.1535 0.0015  0.0096  -0.0087 8   PHE B C   
3106 O  O   . PHE B 8   ? 0.1211 0.1682 0.1539 0.0025  0.0089  0.0012  8   PHE B O   
3107 C  CB  . PHE B 8   ? 0.1254 0.1316 0.1635 0.0094  0.0155  -0.0058 8   PHE B CB  
3108 C  CG  . PHE B 8   ? 0.1112 0.1374 0.1668 0.0187  0.0101  -0.0047 8   PHE B CG  
3109 C  CD1 . PHE B 8   ? 0.1052 0.1756 0.1716 0.0214  0.0275  -0.0036 8   PHE B CD1 
3110 C  CD2 . PHE B 8   ? 0.1411 0.1754 0.1654 0.0191  0.0106  -0.0143 8   PHE B CD2 
3111 C  CE1 . PHE B 8   ? 0.1213 0.2042 0.1962 0.0212  0.0242  0.0123  8   PHE B CE1 
3112 C  CE2 . PHE B 8   ? 0.1616 0.2045 0.1718 0.0317  0.0081  -0.0061 8   PHE B CE2 
3113 C  CZ  . PHE B 8   ? 0.1594 0.2040 0.1838 0.0399  0.0357  0.0045  8   PHE B CZ  
3123 N  N   . ALA B 9   ? 0.1058 0.1539 0.1655 -0.0035 0.0167  -0.0111 9   ALA B N   
3124 C  CA  . ALA B 9   ? 0.1080 0.1680 0.1644 0.0009  0.0162  -0.0149 9   ALA B CA  
3125 C  C   . ALA B 9   ? 0.1018 0.1668 0.1679 -0.0012 0.0172  -0.0254 9   ALA B C   
3126 O  O   . ALA B 9   ? 0.1194 0.1835 0.1802 -0.0116 0.0022  -0.0208 9   ALA B O   
3127 C  CB  . ALA B 9   ? 0.1348 0.1809 0.2016 0.0117  0.0277  -0.0280 9   ALA B CB  
3133 N  N   . GLY B 10  ? 0.1037 0.1610 0.1752 -0.0086 0.0143  -0.0243 10  GLY B N   
3134 C  CA  . GLY B 10  ? 0.1126 0.1621 0.1888 -0.0163 0.0229  -0.0300 10  GLY B CA  
3135 C  C   . GLY B 10  ? 0.1095 0.1627 0.1871 -0.0197 0.0151  -0.0351 10  GLY B C   
3136 O  O   . GLY B 10  ? 0.1117 0.1759 0.1845 -0.0099 0.0246  -0.0368 10  GLY B O   
3140 N  N   . GLY B 11  ? 0.1043 0.1654 0.1946 -0.0067 0.0125  -0.0363 11  GLY B N   
3141 C  CA  . GLY B 11  ? 0.1001 0.1942 0.2012 -0.0061 0.0201  -0.0425 11  GLY B CA  
3142 C  C   . GLY B 11  ? 0.1115 0.1872 0.2205 0.0047  0.0207  -0.0346 11  GLY B C   
3143 O  O   . GLY B 11  ? 0.1143 0.2083 0.2134 -0.0035 0.0077  -0.0330 11  GLY B O   
3147 N  N   . GLU B 12  ? 0.1119 0.2171 0.2293 0.0159  0.0135  -0.0421 12  GLU B N   
3148 C  CA  . GLU B 12  ? 0.1169 0.2620 0.2776 0.0476  0.0077  -0.0447 12  GLU B CA  
3149 C  C   . GLU B 12  ? 0.1962 0.2585 0.2925 0.0565  0.0078  -0.0432 12  GLU B C   
3150 O  O   . GLU B 12  ? 0.1880 0.3292 0.2844 0.0620  -0.0078 -0.0152 12  GLU B O   
3151 C  CB  . GLU B 12  ? 0.1176 0.3154 0.2761 0.0414  0.0186  -0.0468 12  GLU B CB  
3152 C  CG  . GLU B 12  ? 0.1379 0.3203 0.2665 0.0171  0.0054  -0.0555 12  GLU B CG  
3153 C  CD  . GLU B 12  ? 0.1343 0.3148 0.2321 0.0024  -0.0020 -0.0535 12  GLU B CD  
3154 O  OE1 . GLU B 12  ? 0.1608 0.3184 0.3474 -0.0031 -0.0137 -0.0611 12  GLU B OE1 
3155 O  OE2 . GLU B 12  ? 0.1607 0.3126 0.2907 -0.0133 0.0115  -0.0533 12  GLU B OE2 
3162 N  N   . THR B 13  ? 0.2021 0.2337 0.2791 0.0721  -0.0236 -0.0473 13  THR B N   
3163 C  CA  . THR B 13  ? 0.2813 0.2535 0.2822 0.0912  -0.0047 -0.0597 13  THR B CA  
3164 C  C   . THR B 13  ? 0.2692 0.2647 0.2757 0.0985  -0.0226 -0.0339 13  THR B C   
3165 O  O   . THR B 13  ? 0.2640 0.3214 0.2877 0.0392  -0.0224 -0.0334 13  THR B O   
3166 C  CB  . THR B 13  ? 0.3290 0.2496 0.3631 0.0452  0.0161  -0.0853 13  THR B CB  
3167 O  OG1 . THR B 13  ? 0.3584 0.3277 0.4494 0.0022  -0.0769 -0.0437 13  THR B OG1 
3168 C  CG2 . THR B 13  ? 0.3873 0.2976 0.3656 0.0778  0.0706  -0.0907 13  THR B CG2 
3176 N  N   . GLY B 14  ? 0.2503 0.3055 0.2764 0.1031  -0.0273 -0.0390 14  GLY B N   
3177 C  CA  . GLY B 14  ? 0.2319 0.2617 0.2795 0.0517  -0.0308 -0.0230 14  GLY B CA  
3178 C  C   . GLY B 14  ? 0.2002 0.2597 0.3019 0.0770  -0.0329 -0.0396 14  GLY B C   
3179 O  O   . GLY B 14  ? 0.1808 0.3239 0.2809 0.0663  -0.0180 -0.0543 14  GLY B O   
3183 N  N   . VAL B 15  ? 0.2293 0.2299 0.3013 0.0754  -0.0357 -0.0283 15  VAL B N   
3184 C  CA  . VAL B 15  ? 0.2347 0.2803 0.3080 0.0910  -0.0397 -0.0173 15  VAL B CA  
3185 C  C   . VAL B 15  ? 0.1873 0.2797 0.2509 0.0674  -0.0410 -0.0177 15  VAL B C   
3186 O  O   . VAL B 15  ? 0.1956 0.3326 0.2813 0.0789  -0.0699 -0.0258 15  VAL B O   
3187 C  CB  . VAL B 15  ? 0.3270 0.3136 0.3433 0.0910  -0.0407 0.0122  15  VAL B CB  
3188 C  CG1 . VAL B 15  ? 0.4212 0.3127 0.4229 0.0824  -0.0164 0.0194  15  VAL B CG1 
3189 C  CG2 . VAL B 15  ? 0.3476 0.2931 0.3893 0.0618  -0.0276 0.0088  15  VAL B CG2 
3199 N  N   . TRP B 16  ? 0.1374 0.2532 0.2068 0.0453  -0.0148 -0.0234 16  TRP B N   
3200 C  CA  . TRP B 16  ? 0.1266 0.2400 0.1923 0.0237  -0.0111 -0.0244 16  TRP B CA  
3201 C  C   . TRP B 16  ? 0.1235 0.2349 0.1965 0.0090  -0.0152 -0.0348 16  TRP B C   
3202 O  O   . TRP B 16  ? 0.1566 0.2469 0.1962 0.0028  -0.0174 -0.0447 16  TRP B O   
3203 C  CB  . TRP B 16  ? 0.1263 0.2220 0.1930 0.0240  -0.0155 -0.0213 16  TRP B CB  
3204 C  CG  . TRP B 16  ? 0.1247 0.2402 0.1984 0.0174  -0.0332 -0.0060 16  TRP B CG  
3205 C  CD1 . TRP B 16  ? 0.1528 0.2366 0.2161 0.0200  -0.0277 -0.0071 16  TRP B CD1 
3206 C  CD2 . TRP B 16  ? 0.1338 0.2452 0.2026 0.0357  -0.0321 0.0007  16  TRP B CD2 
3207 N  NE1 . TRP B 16  ? 0.1526 0.2528 0.2411 0.0126  -0.0205 0.0173  16  TRP B NE1 
3208 C  CE2 . TRP B 16  ? 0.1419 0.2542 0.2204 0.0413  -0.0312 0.0243  16  TRP B CE2 
3209 C  CE3 . TRP B 16  ? 0.1507 0.2618 0.2112 0.0399  -0.0220 -0.0109 16  TRP B CE3 
3210 C  CZ2 . TRP B 16  ? 0.1475 0.2992 0.2444 0.0366  -0.0294 0.0239  16  TRP B CZ2 
3211 C  CZ3 . TRP B 16  ? 0.1585 0.2986 0.2189 0.0537  -0.0380 0.0001  16  TRP B CZ3 
3212 C  CH2 . TRP B 16  ? 0.1653 0.3169 0.2155 0.0569  -0.0256 0.0177  16  TRP B CH2 
3223 N  N   . ARG B 17  ? 0.1268 0.2376 0.1987 -0.0033 -0.0139 -0.0498 17  ARG B N   
3224 C  CA  . ARG B 17  ? 0.1297 0.2400 0.2189 0.0000  -0.0067 -0.0476 17  ARG B CA  
3225 C  C   . ARG B 17  ? 0.1206 0.2356 0.2084 -0.0061 0.0100  -0.0446 17  ARG B C   
3226 O  O   . ARG B 17  ? 0.1355 0.2724 0.2040 -0.0018 0.0183  -0.0533 17  ARG B O   
3227 C  CB  . ARG B 17  ? 0.1228 0.2577 0.2854 -0.0024 -0.0170 -0.0573 17  ARG B CB  
3228 C  CG  . ARG B 17  ? 0.1689 0.3184 0.3779 -0.0397 -0.0001 -0.0325 17  ARG B CG  
3229 C  CD  . ARG B 17  ? 0.2356 0.4463 0.4809 -0.0586 -0.0555 -0.0127 17  ARG B CD  
3230 N  NE  . ARG B 17  ? 0.3479 0.5417 0.5167 -0.0755 -0.0478 -0.0403 17  ARG B NE  
3231 C  CZ  . ARG B 17  ? 0.4689 0.6003 0.5744 -0.0920 -0.0301 -0.0645 17  ARG B CZ  
3232 N  NH1 . ARG B 17  ? 0.5385 0.6109 0.5885 -0.0109 -0.0486 -0.1599 17  ARG B NH1 
3233 N  NH2 . ARG B 17  ? 0.5246 0.5790 0.6336 -0.1351 0.0267  -0.1207 17  ARG B NH2 
3247 N  N   . VAL B 18  ? 0.1248 0.2372 0.2093 -0.0071 0.0162  -0.0442 18  VAL B N   
3248 C  CA  . VAL B 18  ? 0.1310 0.2194 0.2183 -0.0060 0.0269  -0.0307 18  VAL B CA  
3249 C  C   . VAL B 18  ? 0.1273 0.2330 0.2390 -0.0131 0.0356  -0.0395 18  VAL B C   
3250 O  O   . VAL B 18  ? 0.1619 0.2398 0.2876 -0.0248 0.0692  -0.0383 18  VAL B O   
3251 C  CB  . VAL B 18  ? 0.1535 0.2317 0.2116 0.0063  0.0315  -0.0266 18  VAL B CB  
3252 C  CG1 . VAL B 18  ? 0.1713 0.2640 0.2214 0.0173  0.0353  -0.0112 18  VAL B CG1 
3253 C  CG2 . VAL B 18  ? 0.1701 0.2528 0.1998 0.0117  0.0092  -0.0402 18  VAL B CG2 
3263 N  N   . VAL B 19  ? 0.1275 0.2294 0.2251 -0.0235 0.0175  -0.0424 19  VAL B N   
3264 C  CA  . VAL B 19  ? 0.1360 0.2498 0.2578 -0.0409 0.0212  -0.0557 19  VAL B CA  
3265 C  C   . VAL B 19  ? 0.1636 0.2207 0.2548 -0.0656 0.0244  -0.0144 19  VAL B C   
3266 O  O   . VAL B 19  ? 0.2133 0.2321 0.3402 -0.0742 -0.0063 -0.0194 19  VAL B O   
3267 C  CB  . VAL B 19  ? 0.1622 0.2738 0.2768 -0.0271 0.0023  -0.0648 19  VAL B CB  
3268 C  CG1 . VAL B 19  ? 0.1862 0.3193 0.3016 -0.0184 -0.0060 -0.0482 19  VAL B CG1 
3269 C  CG2 . VAL B 19  ? 0.1898 0.2846 0.2625 -0.0401 0.0052  -0.0670 19  VAL B CG2 
3279 N  N   . ALA B 20  ? 0.1614 0.2189 0.2200 -0.0314 0.0182  -0.0314 20  ALA B N   
3280 C  CA  . ALA B 20  ? 0.1660 0.1901 0.2623 -0.0393 0.0166  -0.0140 20  ALA B CA  
3281 C  C   . ALA B 20  ? 0.1405 0.1835 0.2415 -0.0341 0.0334  -0.0121 20  ALA B C   
3282 O  O   . ALA B 20  ? 0.1550 0.1789 0.2251 -0.0299 0.0331  -0.0084 20  ALA B O   
3283 C  CB  . ALA B 20  ? 0.2150 0.2100 0.2815 -0.0339 -0.0041 -0.0434 20  ALA B CB  
3289 N  N   . MET B 21  ? 0.1685 0.1874 0.2501 -0.0258 0.0297  0.0077  21  MET B N   
3290 C  CA  A MET B 21  ? 0.1716 0.2074 0.2645 -0.0308 0.0315  0.0057  21  MET B CA  
3291 C  CA  B MET B 21  ? 0.1864 0.1963 0.2557 -0.0281 0.0354  -0.0039 21  MET B CA  
3292 C  C   . MET B 21  ? 0.1950 0.1898 0.2380 -0.0321 0.0328  0.0054  21  MET B C   
3293 O  O   . MET B 21  ? 0.2276 0.2293 0.2731 -0.0593 0.0333  0.0341  21  MET B O   
3294 C  CB  A MET B 21  ? 0.2541 0.2715 0.2989 0.0315  0.0525  0.0214  21  MET B CB  
3295 C  CB  B MET B 21  ? 0.2738 0.2433 0.2828 0.0290  0.0647  0.0019  21  MET B CB  
3296 C  CG  A MET B 21  ? 0.1687 0.2349 0.2812 0.0545  0.1308  0.1422  21  MET B CG  
3297 C  CG  B MET B 21  ? 0.3161 0.2651 0.2972 0.0466  0.1038  -0.0001 21  MET B CG  
3298 S  SD  A MET B 21  ? 0.4565 0.4180 0.2972 -0.0291 0.0260  0.0540  21  MET B SD  
3299 S  SD  B MET B 21  ? 0.2757 0.2918 0.2721 0.0061  0.0658  0.0168  21  MET B SD  
3300 C  CE  A MET B 21  ? 0.3351 0.1703 0.1226 -0.0303 -0.0025 -0.0414 21  MET B CE  
3301 C  CE  B MET B 21  ? 0.2761 0.2744 0.3101 0.0475  0.0468  0.0138  21  MET B CE  
3320 N  N   . ASN B 22  ? 0.1694 0.1657 0.2377 -0.0328 0.0117  0.0253  22  ASN B N   
3321 C  CA  . ASN B 22  ? 0.2111 0.1451 0.2453 -0.0312 0.0012  0.0214  22  ASN B CA  
3322 C  C   . ASN B 22  ? 0.2093 0.1348 0.2140 -0.0339 0.0151  0.0220  22  ASN B C   
3323 O  O   . ASN B 22  ? 0.2055 0.1690 0.2025 -0.0392 0.0185  0.0430  22  ASN B O   
3324 C  CB  . ASN B 22  ? 0.2649 0.1763 0.2969 -0.0315 -0.0058 -0.0153 22  ASN B CB  
3325 C  CG  . ASN B 22  ? 0.2812 0.1903 0.3393 -0.0336 -0.0075 -0.0060 22  ASN B CG  
3326 O  OD1 . ASN B 22  ? 0.3095 0.2617 0.3339 -0.0687 -0.0262 -0.0115 22  ASN B OD1 
3327 N  ND2 . ASN B 22  ? 0.3253 0.1905 0.3662 -0.0953 -0.0325 0.0045  22  ASN B ND2 
3334 N  N   . ALA B 23  ? 0.1884 0.1362 0.1978 -0.0182 0.0365  0.0245  23  ALA B N   
3335 C  CA  . ALA B 23  ? 0.1832 0.1303 0.1998 -0.0107 0.0343  0.0245  23  ALA B CA  
3336 C  C   . ALA B 23  ? 0.1997 0.1273 0.2102 -0.0144 0.0544  0.0212  23  ALA B C   
3337 O  O   . ALA B 23  ? 0.2784 0.1500 0.2604 0.0058  0.0844  0.0540  23  ALA B O   
3338 C  CB  . ALA B 23  ? 0.1944 0.1635 0.1801 -0.0119 0.0233  0.0220  23  ALA B CB  
3344 N  N   . VAL B 24  ? 0.1873 0.1182 0.2097 -0.0059 0.0567  0.0150  24  VAL B N   
3345 C  CA  . VAL B 24  ? 0.1991 0.1333 0.1950 0.0028  0.0475  0.0166  24  VAL B CA  
3346 C  C   . VAL B 24  ? 0.1986 0.1272 0.2019 0.0045  0.0544  0.0325  24  VAL B C   
3347 O  O   . VAL B 24  ? 0.2194 0.1441 0.2212 0.0238  0.0515  0.0275  24  VAL B O   
3348 C  CB  . VAL B 24  ? 0.1989 0.1600 0.1908 0.0147  0.0476  0.0255  24  VAL B CB  
3349 C  CG1 . VAL B 24  ? 0.1824 0.1939 0.1961 0.0177  0.0342  0.0131  24  VAL B CG1 
3350 C  CG2 . VAL B 24  ? 0.2039 0.2362 0.2049 0.0436  0.0433  0.0304  24  VAL B CG2 
3360 N  N   . ALA B 25  ? 0.1748 0.1562 0.1920 0.0199  0.0406  0.0320  25  ALA B N   
3361 C  CA  . ALA B 25  ? 0.1818 0.1719 0.1978 0.0281  0.0327  0.0332  25  ALA B CA  
3362 C  C   . ALA B 25  ? 0.1740 0.1783 0.1833 0.0294  0.0228  0.0422  25  ALA B C   
3363 O  O   . ALA B 25  ? 0.1868 0.1608 0.1650 0.0272  0.0364  0.0395  25  ALA B O   
3364 C  CB  . ALA B 25  ? 0.1731 0.2370 0.1909 0.0349  0.0353  0.0289  25  ALA B CB  
3370 N  N   . GLY B 26  ? 0.2023 0.2070 0.1919 0.0588  0.0256  0.0379  26  GLY B N   
3371 C  CA  . GLY B 26  ? 0.1759 0.2190 0.1857 0.0511  0.0169  0.0311  26  GLY B CA  
3372 C  C   . GLY B 26  ? 0.1869 0.2434 0.1719 0.0278  0.0216  0.0392  26  GLY B C   
3373 O  O   . GLY B 26  ? 0.1910 0.2197 0.1966 0.0168  0.0213  0.0290  26  GLY B O   
3377 N  N   . ALA B 27  ? 0.1764 0.2227 0.1756 0.0167  0.0297  0.0413  27  ALA B N   
3378 C  CA  . ALA B 27  ? 0.1828 0.2458 0.1733 0.0031  0.0383  0.0398  27  ALA B CA  
3379 C  C   . ALA B 27  ? 0.1708 0.2513 0.1679 0.0043  0.0332  0.0257  27  ALA B C   
3380 O  O   . ALA B 27  ? 0.1719 0.2266 0.1831 0.0168  0.0338  0.0279  27  ALA B O   
3381 C  CB  . ALA B 27  ? 0.2034 0.2836 0.1766 -0.0055 0.0287  0.0178  27  ALA B CB  
3387 N  N   . PRO B 28  ? 0.1746 0.2354 0.1832 0.0005  0.0272  0.0214  28  PRO B N   
3388 C  CA  . PRO B 28  ? 0.1496 0.2576 0.2158 0.0207  0.0172  -0.0051 28  PRO B CA  
3389 C  C   . PRO B 28  ? 0.1542 0.2537 0.1758 0.0043  0.0288  -0.0074 28  PRO B C   
3390 O  O   . PRO B 28  ? 0.1887 0.2658 0.2030 0.0313  0.0155  -0.0316 28  PRO B O   
3391 C  CB  . PRO B 28  ? 0.1619 0.2921 0.2817 -0.0022 0.0132  -0.0093 28  PRO B CB  
3392 C  CG  . PRO B 28  ? 0.2267 0.3363 0.3437 -0.0296 0.0047  0.0375  28  PRO B CG  
3393 C  CD  . PRO B 28  ? 0.1963 0.2894 0.2691 -0.0238 0.0348  0.0442  28  PRO B CD  
3401 N  N   . LEU B 29  ? 0.1730 0.2457 0.1753 -0.0079 0.0238  0.0050  29  LEU B N   
3402 C  CA  . LEU B 29  ? 0.1833 0.2046 0.1987 -0.0402 0.0340  0.0132  29  LEU B CA  
3403 C  C   . LEU B 29  ? 0.1748 0.1923 0.2196 -0.0186 0.0222  0.0056  29  LEU B C   
3404 O  O   . LEU B 29  ? 0.1691 0.1742 0.2942 -0.0176 0.0251  -0.0129 29  LEU B O   
3405 C  CB  . LEU B 29  ? 0.2514 0.2698 0.2123 -0.0610 -0.0026 0.0297  29  LEU B CB  
3406 C  CG  . LEU B 29  ? 0.3055 0.1941 0.2167 -0.0507 -0.0138 0.0136  29  LEU B CG  
3407 C  CD1 . LEU B 29  ? 0.3088 0.1691 0.2084 -0.0268 0.0294  0.0218  29  LEU B CD1 
3408 C  CD2 . LEU B 29  ? 0.2249 0.1992 0.2125 -0.0336 0.0153  -0.0053 29  LEU B CD2 
3420 N  N   . PRO B 30  ? 0.1703 0.2052 0.2098 -0.0146 0.0229  0.0082  30  PRO B N   
3421 C  CA  . PRO B 30  ? 0.1779 0.2113 0.2260 -0.0096 0.0341  0.0234  30  PRO B CA  
3422 C  C   . PRO B 30  ? 0.1600 0.1776 0.2512 -0.0048 0.0256  0.0232  30  PRO B C   
3423 O  O   . PRO B 30  ? 0.1721 0.1558 0.2340 -0.0158 0.0182  0.0153  30  PRO B O   
3424 C  CB  . PRO B 30  ? 0.1989 0.2499 0.2201 0.0102  0.0374  0.0197  30  PRO B CB  
3425 C  CG  . PRO B 30  ? 0.2124 0.2786 0.2142 0.0125  0.0340  -0.0025 30  PRO B CG  
3426 C  CD  . PRO B 30  ? 0.2058 0.2454 0.1915 -0.0031 0.0287  -0.0100 30  PRO B CD  
3434 N  N   . GLY B 31  ? 0.1696 0.1700 0.3133 -0.0152 0.0230  0.0298  31  GLY B N   
3435 C  CA  . GLY B 31  ? 0.1747 0.1823 0.2899 -0.0153 0.0240  0.0095  31  GLY B CA  
3436 C  C   . GLY B 31  ? 0.1635 0.1799 0.2527 -0.0212 0.0364  0.0085  31  GLY B C   
3437 O  O   . GLY B 31  ? 0.1964 0.2423 0.2563 0.0211  0.0264  0.0135  31  GLY B O   
3441 N  N   . ILE B 32  ? 0.1511 0.1619 0.2263 -0.0130 0.0291  -0.0058 32  ILE B N   
3442 C  CA  . ILE B 32  ? 0.1594 0.1706 0.2220 -0.0165 0.0199  -0.0144 32  ILE B CA  
3443 C  C   . ILE B 32  ? 0.1297 0.1764 0.2229 -0.0341 0.0257  -0.0273 32  ILE B C   
3444 O  O   . ILE B 32  ? 0.1434 0.1890 0.2236 -0.0240 0.0308  -0.0327 32  ILE B O   
3445 C  CB  . ILE B 32  ? 0.1822 0.1647 0.2695 -0.0263 -0.0020 -0.0221 32  ILE B CB  
3446 C  CG1 . ILE B 32  ? 0.2481 0.2076 0.3065 -0.0109 -0.0057 -0.0193 32  ILE B CG1 
3447 C  CG2 . ILE B 32  ? 0.2263 0.1952 0.2998 -0.0187 -0.0308 -0.0444 32  ILE B CG2 
3448 C  CD1 . ILE B 32  ? 0.3582 0.3218 0.4838 -0.0260 -0.0094 0.0338  32  ILE B CD1 
3460 N  N   . PRO B 33  ? 0.1300 0.1799 0.2191 -0.0181 0.0396  -0.0235 33  PRO B N   
3461 C  CA  . PRO B 33  ? 0.1259 0.2113 0.2161 -0.0236 0.0155  -0.0338 33  PRO B CA  
3462 C  C   . PRO B 33  ? 0.1160 0.1950 0.2118 -0.0205 0.0148  -0.0441 33  PRO B C   
3463 O  O   . PRO B 33  ? 0.1217 0.2130 0.2038 -0.0363 0.0203  -0.0446 33  PRO B O   
3464 C  CB  . PRO B 33  ? 0.1327 0.2293 0.2175 -0.0117 0.0241  -0.0239 33  PRO B CB  
3465 C  CG  . PRO B 33  ? 0.1348 0.2425 0.2149 -0.0065 0.0354  -0.0263 33  PRO B CG  
3466 C  CD  . PRO B 33  ? 0.1523 0.1989 0.2029 -0.0057 0.0324  -0.0187 33  PRO B CD  
3474 N  N   . ARG B 34  ? 0.1188 0.1886 0.2009 -0.0114 0.0062  -0.0284 34  ARG B N   
3475 C  CA  . ARG B 34  ? 0.1179 0.1906 0.2005 -0.0109 -0.0036 -0.0195 34  ARG B CA  
3476 C  C   . ARG B 34  ? 0.1221 0.1784 0.1756 -0.0017 0.0000  -0.0234 34  ARG B C   
3477 O  O   . ARG B 34  ? 0.1181 0.1824 0.1812 -0.0056 0.0087  -0.0174 34  ARG B O   
3478 C  CB  . ARG B 34  ? 0.1139 0.2289 0.2290 0.0094  0.0043  -0.0024 34  ARG B CB  
3479 C  CG  . ARG B 34  ? 0.1357 0.2751 0.3090 0.0005  -0.0007 0.0283  34  ARG B CG  
3480 C  CD  . ARG B 34  ? 0.1844 0.3792 0.3313 -0.0234 0.0061  0.0199  34  ARG B CD  
3481 N  NE  . ARG B 34  ? 0.1337 0.4086 0.3011 -0.0363 -0.0133 -0.0024 34  ARG B NE  
3482 C  CZ  . ARG B 34  ? 0.1201 0.4270 0.3099 0.0096  -0.0219 -0.0153 34  ARG B CZ  
3483 N  NH1 . ARG B 34  ? 0.1416 0.4342 0.3769 -0.0174 0.0060  -0.0517 34  ARG B NH1 
3484 N  NH2 . ARG B 34  ? 0.2003 0.4008 0.2951 0.0164  -0.0371 -0.0104 34  ARG B NH2 
3498 N  N   . LEU B 35  ? 0.1216 0.1871 0.1869 -0.0124 -0.0069 -0.0153 35  LEU B N   
3499 C  CA  . LEU B 35  ? 0.1215 0.1800 0.1780 -0.0024 0.0000  -0.0192 35  LEU B CA  
3500 C  C   . LEU B 35  ? 0.1110 0.1857 0.1824 0.0084  0.0039  -0.0176 35  LEU B C   
3501 O  O   . LEU B 35  ? 0.1632 0.1963 0.1896 0.0037  -0.0087 -0.0130 35  LEU B O   
3502 C  CB  . LEU B 35  ? 0.1164 0.1823 0.1896 0.0090  0.0008  -0.0261 35  LEU B CB  
3503 C  CG  . LEU B 35  ? 0.1292 0.2078 0.2186 0.0007  0.0044  -0.0304 35  LEU B CG  
3504 C  CD1 . LEU B 35  ? 0.1279 0.2686 0.2273 0.0068  -0.0048 -0.0579 35  LEU B CD1 
3505 C  CD2 . LEU B 35  ? 0.1386 0.2886 0.2117 -0.0089 0.0175  -0.0234 35  LEU B CD2 
3517 N  N   . ASN B 36  ? 0.1161 0.1775 0.2059 0.0057  -0.0026 -0.0153 36  ASN B N   
3518 C  CA  . ASN B 36  ? 0.1254 0.1841 0.2470 0.0299  -0.0092 -0.0175 36  ASN B CA  
3519 C  C   . ASN B 36  ? 0.1329 0.1772 0.2117 0.0024  -0.0184 0.0004  36  ASN B C   
3520 O  O   . ASN B 36  ? 0.1306 0.2006 0.2103 -0.0047 -0.0135 0.0265  36  ASN B O   
3521 C  CB  . ASN B 36  ? 0.1764 0.2128 0.3079 0.0503  0.0342  -0.0292 36  ASN B CB  
3522 C  CG  . ASN B 36  ? 0.2072 0.2728 0.3539 0.0559  0.0257  -0.0155 36  ASN B CG  
3523 O  OD1 . ASN B 36  ? 0.2755 0.2554 0.4394 0.0239  0.0911  0.0033  36  ASN B OD1 
3524 N  ND2 . ASN B 36  ? 0.2568 0.3096 0.3616 0.1242  -0.0234 -0.0199 36  ASN B ND2 
3531 N  N   . VAL B 37  ? 0.1238 0.1999 0.1944 0.0326  -0.0182 0.0048  37  VAL B N   
3532 C  CA  . VAL B 37  ? 0.1482 0.1911 0.1961 0.0187  -0.0086 0.0122  37  VAL B CA  
3533 C  C   . VAL B 37  ? 0.1512 0.1917 0.2092 0.0275  -0.0203 0.0240  37  VAL B C   
3534 O  O   . VAL B 37  ? 0.2114 0.2243 0.2623 0.0262  -0.0731 0.0503  37  VAL B O   
3535 C  CB  . VAL B 37  ? 0.1791 0.2214 0.2241 0.0311  0.0071  -0.0030 37  VAL B CB  
3536 C  CG1 . VAL B 37  ? 0.1911 0.2459 0.2813 0.0055  0.0554  0.0037  37  VAL B CG1 
3537 C  CG2 . VAL B 37  ? 0.1883 0.2457 0.2331 0.0160  0.0032  -0.0228 37  VAL B CG2 
3547 N  N   . ALA B 38  ? 0.1302 0.1780 0.2200 0.0278  -0.0122 0.0050  38  ALA B N   
3548 C  CA  . ALA B 38  ? 0.1347 0.1786 0.2340 0.0284  0.0034  0.0171  38  ALA B CA  
3549 C  C   . ALA B 38  ? 0.1237 0.1724 0.2214 0.0315  0.0084  0.0187  38  ALA B C   
3550 O  O   . ALA B 38  ? 0.1241 0.1737 0.2395 0.0279  0.0054  0.0290  38  ALA B O   
3551 C  CB  . ALA B 38  ? 0.1747 0.2103 0.2561 0.0231  0.0327  -0.0165 38  ALA B CB  
3557 N  N   . ALA B 39  ? 0.1613 0.2007 0.3153 0.0487  0.0194  0.0740  39  ALA B N   
3558 C  CA  . ALA B 39  ? 0.1798 0.2288 0.3311 0.0477  0.0582  0.0954  39  ALA B CA  
3559 C  C   . ALA B 39  ? 0.2232 0.1759 0.3860 0.0615  0.0990  0.0633  39  ALA B C   
3560 O  O   . ALA B 39  ? 0.2561 0.2184 0.5429 0.0968  0.1531  0.0635  39  ALA B O   
3561 C  CB  . ALA B 39  ? 0.2615 0.2915 0.3502 0.0361  0.0456  0.1189  39  ALA B CB  
3567 N  N   . GLY B 40  ? 0.2317 0.1595 0.3284 0.0462  0.0946  0.0375  40  GLY B N   
3568 C  CA  . GLY B 40  ? 0.2743 0.1622 0.3869 0.0172  0.0991  0.0119  40  GLY B CA  
3569 C  C   . GLY B 40  ? 0.1918 0.1632 0.4088 -0.0035 0.0714  -0.0373 40  GLY B C   
3570 O  O   . GLY B 40  ? 0.2231 0.1551 0.3694 -0.0125 0.0217  -0.0207 40  GLY B O   
3574 N  N   . SER B 41  ? 0.2064 0.1722 0.5066 -0.0154 0.0480  -0.0469 41  SER B N   
3575 C  CA  . SER B 41  ? 0.1836 0.2152 0.5289 -0.0123 -0.0050 -0.1038 41  SER B CA  
3576 C  C   . SER B 41  ? 0.1880 0.2210 0.4799 -0.0271 -0.0416 -0.0179 41  SER B C   
3577 O  O   . SER B 41  ? 0.1957 0.2919 0.5444 0.0087  -0.0695 0.0677  41  SER B O   
3578 C  CB  . SER B 41  ? 0.2217 0.2626 0.5781 -0.0357 0.0427  -0.1350 41  SER B CB  
3579 O  OG  . SER B 41  ? 0.3728 0.3538 0.6854 -0.0794 0.0597  -0.0579 41  SER B OG  
3585 N  N   . VAL B 42  ? 0.1860 0.1500 0.3491 0.0141  -0.0244 -0.0368 42  VAL B N   
3586 C  CA  . VAL B 42  ? 0.1931 0.1728 0.3307 0.0165  0.0023  -0.0024 42  VAL B CA  
3587 C  C   . VAL B 42  ? 0.1871 0.1796 0.2500 0.0330  -0.0140 -0.0120 42  VAL B C   
3588 O  O   . VAL B 42  ? 0.1958 0.2220 0.2766 0.0364  0.0158  -0.0051 42  VAL B O   
3589 C  CB  . VAL B 42  ? 0.2307 0.1716 0.3335 0.0017  -0.0182 0.0173  42  VAL B CB  
3590 C  CG1 . VAL B 42  ? 0.2501 0.2149 0.3354 -0.0442 -0.0117 -0.0169 42  VAL B CG1 
3591 C  CG2 . VAL B 42  ? 0.2639 0.1901 0.3056 0.0184  0.0381  0.0253  42  VAL B CG2 
3601 N  N   . SER B 43  ? 0.1751 0.1595 0.2087 0.0137  -0.0016 -0.0124 43  SER B N   
3602 C  CA  . SER B 43  ? 0.1706 0.2006 0.1852 0.0175  0.0016  0.0005  43  SER B CA  
3603 C  C   . SER B 43  ? 0.1480 0.1805 0.1706 0.0285  0.0023  0.0048  43  SER B C   
3604 O  O   . SER B 43  ? 0.1584 0.1531 0.1686 0.0243  -0.0053 -0.0095 43  SER B O   
3605 C  CB  . SER B 43  ? 0.1880 0.2232 0.1988 0.0180  0.0001  -0.0056 43  SER B CB  
3606 O  OG  . SER B 43  ? 0.2002 0.2100 0.1988 0.0171  0.0115  -0.0300 43  SER B OG  
3612 N  N   . PRO B 44  ? 0.1484 0.2398 0.2003 0.0185  -0.0064 0.0382  44  PRO B N   
3613 C  CA  . PRO B 44  ? 0.1399 0.2054 0.2156 0.0327  0.0115  0.0177  44  PRO B CA  
3614 C  C   . PRO B 44  ? 0.1409 0.1920 0.1942 0.0326  0.0075  -0.0124 44  PRO B C   
3615 O  O   . PRO B 44  ? 0.1672 0.2548 0.2089 0.0308  0.0208  -0.0356 44  PRO B O   
3616 C  CB  . PRO B 44  ? 0.1698 0.2038 0.2647 0.0608  0.0144  0.0279  44  PRO B CB  
3617 C  CG  . PRO B 44  ? 0.2161 0.3050 0.2981 0.0395  -0.0322 0.0401  44  PRO B CG  
3618 C  CD  . PRO B 44  ? 0.1804 0.3180 0.2742 0.0372  -0.0413 0.0551  44  PRO B CD  
3626 N  N   . GLN B 45  ? 0.1667 0.1747 0.2019 0.0270  -0.0013 -0.0078 45  GLN B N   
3627 C  CA  . GLN B 45  ? 0.1759 0.1735 0.2245 0.0329  0.0099  -0.0397 45  GLN B CA  
3628 C  C   . GLN B 45  ? 0.1850 0.1981 0.2932 0.0426  0.0020  -0.0528 45  GLN B C   
3629 O  O   . GLN B 45  ? 0.1793 0.2225 0.3350 0.0231  0.0191  -0.0790 45  GLN B O   
3630 C  CB  . GLN B 45  ? 0.2316 0.1656 0.1958 0.0038  0.0108  -0.0181 45  GLN B CB  
3631 C  CG  . GLN B 45  ? 0.2249 0.1697 0.1985 0.0107  -0.0158 -0.0158 45  GLN B CG  
3632 C  CD  . GLN B 45  ? 0.2574 0.1745 0.1873 -0.0266 -0.0120 -0.0329 45  GLN B CD  
3633 O  OE1 . GLN B 45  ? 0.2819 0.1906 0.2501 -0.0226 -0.0739 -0.0075 45  GLN B OE1 
3634 N  NE2 . GLN B 45  ? 0.2679 0.2188 0.2775 0.0000  0.0495  -0.0220 45  GLN B NE2 
3643 N  N   . PRO B 46  ? 0.1866 0.2416 0.3170 0.0310  -0.0213 -0.0586 46  PRO B N   
3644 C  CA  . PRO B 46  ? 0.2231 0.2623 0.3819 0.0368  -0.0405 -0.0767 46  PRO B CA  
3645 C  C   . PRO B 46  ? 0.1812 0.2386 0.4406 0.0632  -0.0240 -0.0535 46  PRO B C   
3646 O  O   . PRO B 46  ? 0.1760 0.2193 0.4284 0.0258  0.0012  -0.0796 46  PRO B O   
3647 C  CB  . PRO B 46  ? 0.3108 0.3026 0.3577 0.0458  -0.0568 -0.0776 46  PRO B CB  
3648 C  CG  . PRO B 46  ? 0.3146 0.2675 0.2796 0.0700  -0.0356 -0.0598 46  PRO B CG  
3649 C  CD  . PRO B 46  ? 0.2563 0.2377 0.2759 0.0635  -0.0136 -0.0634 46  PRO B CD  
3657 N  N   . PRO B 47  ? 0.1995 0.2627 0.4973 0.0465  -0.0001 -0.0434 47  PRO B N   
3658 C  CA  . PRO B 47  ? 0.1941 0.2733 0.5320 0.0645  0.0518  -0.0502 47  PRO B CA  
3659 C  C   . PRO B 47  ? 0.1631 0.2420 0.4565 0.0465  0.0775  -0.0758 47  PRO B C   
3660 O  O   . PRO B 47  ? 0.1912 0.2963 0.4788 0.0162  0.0024  -0.0833 47  PRO B O   
3661 C  CB  . PRO B 47  ? 0.2174 0.3769 0.5703 0.0716  0.0347  -0.0158 47  PRO B CB  
3662 C  CG  . PRO B 47  ? 0.2431 0.4234 0.5311 0.0684  0.0294  -0.0380 47  PRO B CG  
3663 C  CD  . PRO B 47  ? 0.2193 0.3210 0.5023 0.0676  -0.0165 -0.0631 47  PRO B CD  
3671 N  N   . GLY B 48  ? 0.1735 0.2828 0.4234 0.0266  0.0541  -0.0957 48  GLY B N   
3672 C  CA  . GLY B 48  ? 0.1717 0.2680 0.3324 -0.0043 0.0628  -0.0817 48  GLY B CA  
3673 C  C   . GLY B 48  ? 0.1483 0.2242 0.2883 -0.0084 0.0421  -0.0669 48  GLY B C   
3674 O  O   . GLY B 48  ? 0.1350 0.2474 0.2917 -0.0151 0.0574  -0.0724 48  GLY B O   
3678 N  N   . THR B 49  ? 0.1476 0.2069 0.2700 -0.0158 0.0483  -0.0671 49  THR B N   
3679 C  CA  . THR B 49  ? 0.1376 0.2047 0.2158 -0.0075 0.0364  -0.0618 49  THR B CA  
3680 C  C   . THR B 49  ? 0.1672 0.1883 0.2144 -0.0251 0.0576  -0.0473 49  THR B C   
3681 O  O   . THR B 49  ? 0.2368 0.2150 0.2102 -0.0095 0.0580  -0.0482 49  THR B O   
3682 C  CB  . THR B 49  ? 0.1346 0.1924 0.2288 0.0079  0.0325  -0.0301 49  THR B CB  
3683 O  OG1 . THR B 49  ? 0.1629 0.1990 0.2503 0.0189  0.0184  -0.0296 49  THR B OG1 
3684 C  CG2 . THR B 49  ? 0.1440 0.1950 0.2198 -0.0120 0.0252  -0.0133 49  THR B CG2 
3692 N  N   . LYS B 50  ? 0.1393 0.1967 0.2074 -0.0247 0.0549  -0.0424 50  LYS B N   
3693 C  CA  . LYS B 50  ? 0.1515 0.1788 0.2285 -0.0226 0.0607  -0.0207 50  LYS B CA  
3694 C  C   . LYS B 50  ? 0.1625 0.1890 0.1745 -0.0319 0.0410  -0.0365 50  LYS B C   
3695 O  O   . LYS B 50  ? 0.1867 0.2180 0.1781 -0.0512 0.0356  -0.0251 50  LYS B O   
3696 C  CB  . LYS B 50  ? 0.1333 0.2026 0.2936 -0.0451 0.0478  -0.0188 50  LYS B CB  
3697 C  CG  . LYS B 50  ? 0.1925 0.2454 0.3392 -0.0118 0.0590  0.0137  50  LYS B CG  
3698 C  CD  . LYS B 50  ? 0.3034 0.3010 0.3739 0.0391  0.0858  0.0419  50  LYS B CD  
3699 C  CE  . LYS B 50  ? 0.3557 0.3264 0.4115 0.0481  0.1021  0.0762  50  LYS B CE  
3700 N  NZ  . LYS B 50  ? 0.4654 0.4535 0.4446 0.0342  0.1314  0.0818  50  LYS B NZ  
3714 N  N   . TRP B 51  ? 0.1320 0.1616 0.1661 -0.0140 0.0335  -0.0276 51  TRP B N   
3715 C  CA  . TRP B 51  ? 0.1345 0.1685 0.1559 -0.0097 0.0280  -0.0184 51  TRP B CA  
3716 C  C   . TRP B 51  ? 0.1221 0.1561 0.1527 -0.0102 0.0209  -0.0336 51  TRP B C   
3717 O  O   . TRP B 51  ? 0.1117 0.1677 0.1593 -0.0045 0.0216  -0.0309 51  TRP B O   
3718 C  CB  . TRP B 51  ? 0.1300 0.1722 0.1896 -0.0139 0.0177  -0.0306 51  TRP B CB  
3719 C  CG  . TRP B 51  ? 0.1166 0.1601 0.1854 -0.0080 0.0212  -0.0171 51  TRP B CG  
3720 C  CD1 . TRP B 51  ? 0.1296 0.1614 0.1916 -0.0091 0.0340  -0.0173 51  TRP B CD1 
3721 C  CD2 . TRP B 51  ? 0.1044 0.1570 0.1765 -0.0076 0.0238  -0.0343 51  TRP B CD2 
3722 N  NE1 . TRP B 51  ? 0.1509 0.1544 0.2004 -0.0125 0.0268  -0.0244 51  TRP B NE1 
3723 C  CE2 . TRP B 51  ? 0.1215 0.1524 0.1869 -0.0038 0.0277  -0.0333 51  TRP B CE2 
3724 C  CE3 . TRP B 51  ? 0.1179 0.1712 0.1770 -0.0087 0.0281  -0.0359 51  TRP B CE3 
3725 C  CZ2 . TRP B 51  ? 0.1308 0.1687 0.1952 -0.0019 0.0271  -0.0424 51  TRP B CZ2 
3726 C  CZ3 . TRP B 51  ? 0.1382 0.1643 0.1848 0.0027  0.0254  -0.0315 51  TRP B CZ3 
3727 C  CH2 . TRP B 51  ? 0.1414 0.1766 0.1830 0.0042  0.0328  -0.0447 51  TRP B CH2 
3738 N  N   . LEU B 52  ? 0.1189 0.1690 0.1476 -0.0117 0.0179  -0.0146 52  LEU B N   
3739 C  CA  A LEU B 52  ? 0.1111 0.1478 0.1587 0.0010  0.0233  -0.0161 52  LEU B CA  
3740 C  CA  B LEU B 52  ? 0.1133 0.1499 0.1662 0.0090  0.0209  -0.0145 52  LEU B CA  
3741 C  C   . LEU B 52  ? 0.1099 0.1646 0.1523 0.0093  0.0146  -0.0003 52  LEU B C   
3742 O  O   . LEU B 52  ? 0.1168 0.2793 0.1566 -0.0005 0.0112  -0.0062 52  LEU B O   
3743 C  CB  A LEU B 52  ? 0.1496 0.1582 0.1555 -0.0149 0.0230  -0.0207 52  LEU B CB  
3744 C  CB  B LEU B 52  ? 0.1514 0.1608 0.1866 0.0292  0.0152  -0.0240 52  LEU B CB  
3745 C  CG  A LEU B 52  ? 0.1357 0.1641 0.1520 -0.0080 0.0310  -0.0166 52  LEU B CG  
3746 C  CG  B LEU B 52  ? 0.1453 0.1583 0.2028 0.0204  0.0256  -0.0230 52  LEU B CG  
3747 C  CD1 A LEU B 52  ? 0.1836 0.1699 0.1833 0.0017  0.0434  -0.0369 52  LEU B CD1 
3748 C  CD1 B LEU B 52  ? 0.1637 0.1716 0.1864 0.0078  0.0233  -0.0081 52  LEU B CD1 
3749 C  CD2 A LEU B 52  ? 0.1351 0.1671 0.1715 0.0131  0.0250  -0.0250 52  LEU B CD2 
3750 C  CD2 B LEU B 52  ? 0.1837 0.1720 0.2160 0.0016  0.0486  -0.0331 52  LEU B CD2 
3773 N  N   . LEU B 53  ? 0.1037 0.1401 0.1397 0.0096  0.0104  -0.0044 53  LEU B N   
3774 C  CA  . LEU B 53  ? 0.1076 0.1425 0.1428 0.0094  0.0218  -0.0058 53  LEU B CA  
3775 C  C   . LEU B 53  ? 0.1007 0.1319 0.1389 0.0106  0.0094  -0.0104 53  LEU B C   
3776 O  O   . LEU B 53  ? 0.1123 0.1524 0.1632 -0.0026 -0.0107 0.0123  53  LEU B O   
3777 C  CB  . LEU B 53  ? 0.1187 0.1348 0.1600 0.0130  0.0168  -0.0057 53  LEU B CB  
3778 C  CG  . LEU B 53  ? 0.1273 0.1367 0.1737 0.0035  0.0219  -0.0028 53  LEU B CG  
3779 C  CD1 . LEU B 53  ? 0.1445 0.1386 0.1969 0.0126  0.0246  -0.0071 53  LEU B CD1 
3780 C  CD2 . LEU B 53  ? 0.1893 0.1481 0.1869 0.0162  0.0064  0.0145  53  LEU B CD2 
3792 N  N   . ARG B 54  ? 0.1020 0.1502 0.1334 -0.0021 0.0103  -0.0013 54  ARG B N   
3793 C  CA  . ARG B 54  ? 0.0976 0.1408 0.1314 0.0038  0.0046  -0.0080 54  ARG B CA  
3794 C  C   . ARG B 54  ? 0.0986 0.1237 0.1278 0.0025  0.0022  -0.0130 54  ARG B C   
3795 O  O   . ARG B 54  ? 0.0991 0.1346 0.1337 0.0018  0.0117  -0.0003 54  ARG B O   
3796 C  CB  . ARG B 54  ? 0.1258 0.1521 0.1481 0.0131  0.0062  -0.0235 54  ARG B CB  
3797 C  CG  . ARG B 54  ? 0.1247 0.1458 0.1550 0.0174  0.0076  -0.0319 54  ARG B CG  
3798 C  CD  . ARG B 54  ? 0.1404 0.1517 0.1789 0.0163  0.0137  -0.0288 54  ARG B CD  
3799 N  NE  . ARG B 54  ? 0.1388 0.1656 0.1945 0.0278  0.0131  -0.0407 54  ARG B NE  
3800 C  CZ  . ARG B 54  ? 0.1400 0.1752 0.2034 -0.0029 0.0214  -0.0510 54  ARG B CZ  
3801 N  NH1 . ARG B 54  ? 0.1584 0.2147 0.2437 -0.0045 0.0230  -0.0829 54  ARG B NH1 
3802 N  NH2 . ARG B 54  ? 0.1494 0.1938 0.2292 0.0302  0.0095  -0.0691 54  ARG B NH2 
3816 N  N   . GLY B 55  ? 0.1018 0.1216 0.1295 0.0026  0.0085  -0.0104 55  GLY B N   
3817 C  CA  . GLY B 55  ? 0.1120 0.1171 0.1285 0.0040  0.0128  -0.0089 55  GLY B CA  
3818 C  C   . GLY B 55  ? 0.0997 0.1166 0.1306 0.0145  0.0078  -0.0053 55  GLY B C   
3819 O  O   . GLY B 55  ? 0.0943 0.1358 0.1774 0.0117  0.0110  0.0112  55  GLY B O   
3823 N  N   . ILE B 56  ? 0.0978 0.1077 0.1290 0.0108  0.0024  -0.0001 56  ILE B N   
3824 C  CA  . ILE B 56  ? 0.0968 0.1102 0.1346 0.0098  0.0000  0.0022  56  ILE B CA  
3825 C  C   . ILE B 56  ? 0.0961 0.1064 0.1309 0.0031  -0.0013 0.0028  56  ILE B C   
3826 O  O   . ILE B 56  ? 0.1063 0.1132 0.1328 0.0137  0.0062  0.0043  56  ILE B O   
3827 C  CB  . ILE B 56  ? 0.1013 0.1072 0.1297 0.0104  0.0051  -0.0029 56  ILE B CB  
3828 C  CG1 . ILE B 56  ? 0.1003 0.1141 0.1467 0.0093  -0.0043 0.0022  56  ILE B CG1 
3829 C  CG2 . ILE B 56  ? 0.1096 0.1018 0.1402 0.0043  -0.0018 -0.0005 56  ILE B CG2 
3830 C  CD1 . ILE B 56  ? 0.1097 0.1188 0.1577 0.0039  -0.0072 0.0012  56  ILE B CD1 
3842 N  N   . THR B 57  ? 0.1012 0.1200 0.1230 0.0096  -0.0025 0.0003  57  THR B N   
3843 C  CA  . THR B 57  ? 0.1117 0.1173 0.1327 -0.0017 -0.0012 0.0080  57  THR B CA  
3844 C  C   . THR B 57  ? 0.1102 0.1134 0.1229 0.0092  0.0014  0.0057  57  THR B C   
3845 O  O   . THR B 57  ? 0.1102 0.1204 0.1523 0.0051  -0.0047 -0.0039 57  THR B O   
3846 C  CB  . THR B 57  ? 0.1232 0.1415 0.1405 0.0045  -0.0060 0.0142  57  THR B CB  
3847 O  OG1 . THR B 57  ? 0.1404 0.1448 0.1460 0.0096  -0.0243 0.0254  57  THR B OG1 
3848 C  CG2 . THR B 57  ? 0.1252 0.1673 0.1534 -0.0026 -0.0142 0.0053  57  THR B CG2 
3856 N  N   . SER B 58  ? 0.1086 0.1190 0.1351 0.0067  0.0051  0.0007  58  SER B N   
3857 C  CA  . SER B 58  ? 0.1054 0.1240 0.1389 0.0099  0.0026  0.0016  58  SER B CA  
3858 C  C   . SER B 58  ? 0.1141 0.1282 0.1313 0.0072  -0.0032 0.0109  58  SER B C   
3859 O  O   . SER B 58  ? 0.1263 0.1463 0.1367 0.0053  -0.0008 0.0058  58  SER B O   
3860 C  CB  . SER B 58  ? 0.1099 0.1151 0.1382 -0.0007 0.0004  0.0017  58  SER B CB  
3861 O  OG  . SER B 58  ? 0.1093 0.1244 0.1389 0.0060  -0.0020 -0.0009 58  SER B OG  
3867 N  N   . ASN B 59  ? 0.1076 0.1246 0.1305 0.0040  0.0051  0.0118  59  ASN B N   
3868 C  CA  . ASN B 59  ? 0.1205 0.1187 0.1315 0.0068  0.0049  0.0176  59  ASN B CA  
3869 C  C   . ASN B 59  ? 0.1123 0.1266 0.1255 0.0053  0.0101  0.0155  59  ASN B C   
3870 O  O   . ASN B 59  ? 0.1217 0.1097 0.1327 0.0041  0.0046  0.0143  59  ASN B O   
3871 C  CB  . ASN B 59  ? 0.1221 0.1312 0.1439 -0.0008 0.0131  0.0147  59  ASN B CB  
3872 C  CG  . ASN B 59  ? 0.1096 0.1244 0.1429 -0.0082 0.0080  0.0102  59  ASN B CG  
3873 O  OD1 . ASN B 59  ? 0.1184 0.1478 0.1396 0.0018  0.0064  0.0091  59  ASN B OD1 
3874 N  ND2 . ASN B 59  ? 0.1182 0.1439 0.1437 0.0111  0.0076  0.0116  59  ASN B ND2 
3881 N  N   . GLU B 60  ? 0.1215 0.1249 0.1274 0.0203  0.0056  0.0147  60  GLU B N   
3882 C  CA  . GLU B 60  ? 0.1236 0.1313 0.1218 0.0100  0.0065  0.0145  60  GLU B CA  
3883 C  C   . GLU B 60  ? 0.1180 0.1197 0.1138 0.0069  0.0084  0.0136  60  GLU B C   
3884 O  O   . GLU B 60  ? 0.1185 0.1265 0.1431 0.0063  0.0025  0.0243  60  GLU B O   
3885 C  CB  . GLU B 60  ? 0.1388 0.1457 0.1275 0.0215  -0.0054 0.0141  60  GLU B CB  
3886 C  CG  . GLU B 60  ? 0.1431 0.1845 0.1308 0.0051  -0.0030 0.0256  60  GLU B CG  
3887 C  CD  . GLU B 60  ? 0.1482 0.2542 0.1601 -0.0134 -0.0160 0.0548  60  GLU B CD  
3888 O  OE1 . GLU B 60  ? 0.1954 0.3083 0.1870 -0.0334 -0.0280 0.0814  60  GLU B OE1 
3889 O  OE2 . GLU B 60  ? 0.1804 0.2756 0.1718 -0.0328 -0.0309 0.0488  60  GLU B OE2 
3896 N  N   . ARG B 61  ? 0.1225 0.1178 0.1153 0.0163  0.0072  0.0066  61  ARG B N   
3897 C  CA  . ARG B 61  ? 0.1125 0.1200 0.1120 0.0153  -0.0041 0.0068  61  ARG B CA  
3898 C  C   . ARG B 61  ? 0.1225 0.1150 0.1180 0.0109  -0.0053 0.0174  61  ARG B C   
3899 O  O   . ARG B 61  ? 0.1300 0.1308 0.1402 0.0250  -0.0097 -0.0008 61  ARG B O   
3900 C  CB  . ARG B 61  ? 0.1452 0.1179 0.1207 0.0110  0.0075  0.0127  61  ARG B CB  
3901 C  CG  . ARG B 61  ? 0.1332 0.1246 0.1214 -0.0011 0.0090  0.0101  61  ARG B CG  
3902 C  CD  . ARG B 61  ? 0.1315 0.1187 0.1285 0.0001  0.0155  -0.0017 61  ARG B CD  
3903 N  NE  . ARG B 61  ? 0.1328 0.1187 0.1278 0.0045  0.0044  0.0093  61  ARG B NE  
3904 C  CZ  . ARG B 61  ? 0.1178 0.1105 0.1240 0.0117  0.0052  0.0023  61  ARG B CZ  
3905 N  NH1 . ARG B 61  ? 0.1328 0.1136 0.1336 0.0089  -0.0057 -0.0001 61  ARG B NH1 
3906 N  NH2 . ARG B 61  ? 0.1291 0.1280 0.1437 0.0128  0.0175  0.0062  61  ARG B NH2 
3920 N  N   . TYR B 62  ? 0.1228 0.1139 0.1093 0.0169  0.0070  0.0082  62  TYR B N   
3921 C  CA  . TYR B 62  ? 0.1256 0.1228 0.1219 0.0161  0.0060  0.0065  62  TYR B CA  
3922 C  C   . TYR B 62  ? 0.1260 0.1321 0.1226 0.0074  0.0084  0.0024  62  TYR B C   
3923 O  O   . TYR B 62  ? 0.1467 0.1562 0.1244 0.0214  0.0172  0.0022  62  TYR B O   
3924 C  CB  . TYR B 62  ? 0.1408 0.1190 0.1225 0.0129  0.0124  -0.0021 62  TYR B CB  
3925 C  CG  . TYR B 62  ? 0.1298 0.1102 0.1300 0.0200  0.0077  0.0075  62  TYR B CG  
3926 C  CD1 . TYR B 62  ? 0.1224 0.1191 0.1350 0.0286  0.0170  0.0141  62  TYR B CD1 
3927 C  CD2 . TYR B 62  ? 0.1305 0.1254 0.1331 0.0055  0.0038  0.0201  62  TYR B CD2 
3928 C  CE1 . TYR B 62  ? 0.1151 0.1251 0.1442 0.0295  0.0020  0.0151  62  TYR B CE1 
3929 C  CE2 . TYR B 62  ? 0.1249 0.1247 0.1324 0.0118  0.0018  0.0151  62  TYR B CE2 
3930 C  CZ  . TYR B 62  ? 0.1312 0.1090 0.1249 0.0229  0.0088  0.0152  62  TYR B CZ  
3931 O  OH  . TYR B 62  ? 0.1357 0.1281 0.1269 0.0249  0.0044  0.0167  62  TYR B OH  
3941 N  N   . VAL B 63  ? 0.1395 0.1553 0.1122 0.0187  0.0025  0.0054  63  VAL B N   
3942 C  CA  . VAL B 63  ? 0.1433 0.1922 0.1177 0.0148  0.0011  0.0014  63  VAL B CA  
3943 C  C   . VAL B 63  ? 0.1471 0.1690 0.1180 0.0236  -0.0034 0.0060  63  VAL B C   
3944 O  O   . VAL B 63  ? 0.1699 0.1720 0.1235 0.0070  0.0057  0.0063  63  VAL B O   
3945 C  CB  . VAL B 63  ? 0.1581 0.2809 0.1358 -0.0116 -0.0218 0.0246  63  VAL B CB  
3946 C  CG1 . VAL B 63  ? 0.1954 0.2611 0.1704 0.0033  -0.0009 0.0170  63  VAL B CG1 
3947 C  CG2 . VAL B 63  ? 0.2402 0.2142 0.1709 -0.0335 -0.0241 0.0188  63  VAL B CG2 
3957 N  N   . VAL B 64  ? 0.1489 0.1810 0.1161 0.0215  0.0110  0.0147  64  VAL B N   
3958 C  CA  . VAL B 64  ? 0.1473 0.1994 0.1274 0.0178  0.0077  0.0262  64  VAL B CA  
3959 C  C   . VAL B 64  ? 0.1465 0.2193 0.1179 0.0148  0.0163  0.0275  64  VAL B C   
3960 O  O   . VAL B 64  ? 0.1565 0.2056 0.1284 0.0235  0.0089  0.0270  64  VAL B O   
3961 C  CB  . VAL B 64  ? 0.1605 0.2240 0.1385 0.0233  0.0083  0.0138  64  VAL B CB  
3962 C  CG1 . VAL B 64  ? 0.1634 0.2376 0.1456 0.0427  0.0194  0.0212  64  VAL B CG1 
3963 C  CG2 . VAL B 64  ? 0.1627 0.2554 0.1442 0.0575  0.0246  0.0041  64  VAL B CG2 
3973 N  N   . ARG B 65  ? 0.1550 0.2276 0.1379 0.0222  0.0123  0.0422  65  ARG B N   
3974 C  CA  . ARG B 65  ? 0.1776 0.2428 0.1402 0.0088  0.0020  0.0481  65  ARG B CA  
3975 C  C   . ARG B 65  ? 0.1861 0.2590 0.1196 0.0066  0.0081  0.0439  65  ARG B C   
3976 O  O   . ARG B 65  ? 0.1835 0.2601 0.1484 0.0073  -0.0096 0.0557  65  ARG B O   
3977 C  CB  . ARG B 65  ? 0.2297 0.2496 0.1513 -0.0161 -0.0064 0.0586  65  ARG B CB  
3978 C  CG  . ARG B 65  ? 0.2713 0.2785 0.1898 -0.0532 -0.0228 0.0933  65  ARG B CG  
3979 C  CD  . ARG B 65  ? 0.2767 0.2879 0.2260 -0.0356 -0.0396 0.1106  65  ARG B CD  
3980 N  NE  . ARG B 65  ? 0.2555 0.3148 0.2302 0.0150  -0.0001 0.0760  65  ARG B NE  
3981 C  CZ  . ARG B 65  ? 0.2532 0.3342 0.2506 0.0302  -0.0157 0.0361  65  ARG B CZ  
3982 N  NH1 . ARG B 65  ? 0.2749 0.3433 0.3142 0.0616  -0.0087 0.0655  65  ARG B NH1 
3983 N  NH2 . ARG B 65  ? 0.2434 0.3839 0.2614 0.0586  -0.0154 0.0002  65  ARG B NH2 
3997 N  N   . GLU B 66  ? 0.2005 0.3043 0.1153 0.0232  0.0215  0.0403  66  GLU B N   
3998 C  CA  . GLU B 66  ? 0.2174 0.3037 0.1377 0.0462  0.0231  0.0222  66  GLU B CA  
3999 C  C   . GLU B 66  ? 0.2182 0.2514 0.1401 0.0477  -0.0077 0.0288  66  GLU B C   
4000 O  O   . GLU B 66  ? 0.2387 0.2786 0.1413 0.0259  -0.0087 0.0261  66  GLU B O   
4001 C  CB  . GLU B 66  ? 0.2615 0.3648 0.1969 0.0584  0.0602  -0.0194 66  GLU B CB  
4002 C  CG  . GLU B 66  ? 0.3508 0.4674 0.3685 0.0306  0.0371  -0.0157 66  GLU B CG  
4003 C  CD  . GLU B 66  ? 0.3958 0.4503 0.3342 0.0630  0.0309  -0.0496 66  GLU B CD  
4004 O  OE1 . GLU B 66  ? 0.4492 0.4687 0.3288 0.0444  0.0747  0.0166  66  GLU B OE1 
4005 O  OE2 . GLU B 66  ? 0.2051 0.3868 0.1773 0.0169  0.0361  -0.0124 66  GLU B OE2 
4012 N  N   . GLU B 67  ? 0.1875 0.2250 0.1369 0.0454  -0.0118 0.0244  67  GLU B N   
4013 C  CA  . GLU B 67  ? 0.1908 0.1991 0.1496 0.0423  -0.0094 0.0296  67  GLU B CA  
4014 C  C   . GLU B 67  ? 0.1738 0.1921 0.1428 0.0293  -0.0117 0.0304  67  GLU B C   
4015 O  O   . GLU B 67  ? 0.1880 0.1955 0.1650 0.0214  -0.0114 0.0373  67  GLU B O   
4016 C  CB  . GLU B 67  ? 0.1829 0.1985 0.1494 0.0384  -0.0095 0.0173  67  GLU B CB  
4017 C  CG  . GLU B 67  ? 0.2376 0.1875 0.1501 0.0449  -0.0322 0.0083  67  GLU B CG  
4018 C  CD  . GLU B 67  ? 0.2018 0.1846 0.1547 0.0386  -0.0224 0.0106  67  GLU B CD  
4019 O  OE1 . GLU B 67  ? 0.2098 0.1647 0.1379 0.0444  -0.0102 0.0150  67  GLU B OE1 
4020 O  OE2 . GLU B 67  ? 0.2437 0.1774 0.1669 0.0395  -0.0386 -0.0017 67  GLU B OE2 
4027 N  N   . LYS B 68  ? 0.1671 0.1870 0.1426 0.0289  -0.0055 0.0316  68  LYS B N   
4028 C  CA  . LYS B 68  ? 0.1608 0.1848 0.1679 0.0268  -0.0078 0.0218  68  LYS B CA  
4029 C  C   . LYS B 68  ? 0.1711 0.1812 0.1784 0.0200  -0.0067 0.0277  68  LYS B C   
4030 O  O   . LYS B 68  ? 0.1642 0.1942 0.1940 0.0170  -0.0104 0.0377  68  LYS B O   
4031 C  CB  . LYS B 68  ? 0.1725 0.1981 0.1769 0.0119  -0.0130 0.0141  68  LYS B CB  
4032 C  CG  . LYS B 68  ? 0.1947 0.2359 0.2031 0.0257  -0.0144 -0.0164 68  LYS B CG  
4033 C  CD  . LYS B 68  ? 0.2367 0.2570 0.2430 0.0226  0.0022  -0.0092 68  LYS B CD  
4034 C  CE  . LYS B 68  ? 0.2399 0.2647 0.2475 0.0203  0.0233  -0.0005 68  LYS B CE  
4035 N  NZ  . LYS B 68  ? 0.2706 0.2239 0.2645 0.0241  0.0274  0.0154  68  LYS B NZ  
4049 N  N   . ASP B 69  ? 0.1692 0.1924 0.1562 0.0215  -0.0185 0.0440  69  ASP B N   
4050 C  CA  . ASP B 69  ? 0.1875 0.2082 0.1744 0.0242  -0.0265 0.0464  69  ASP B CA  
4051 C  C   . ASP B 69  ? 0.2158 0.2056 0.1533 0.0203  -0.0328 0.0382  69  ASP B C   
4052 O  O   . ASP B 69  ? 0.2183 0.2177 0.1864 0.0158  -0.0467 0.0397  69  ASP B O   
4053 C  CB  . ASP B 69  ? 0.2000 0.2675 0.1841 0.0231  -0.0216 0.0711  69  ASP B CB  
4054 C  CG  . ASP B 69  ? 0.1916 0.2546 0.2313 -0.0034 -0.0014 0.0778  69  ASP B CG  
4055 O  OD1 . ASP B 69  ? 0.2077 0.2900 0.3259 -0.0329 -0.0137 0.0278  69  ASP B OD1 
4056 O  OD2 . ASP B 69  ? 0.2104 0.3469 0.2502 0.0087  -0.0175 0.0822  69  ASP B OD2 
4061 N  N   . ARG B 70  ? 0.2166 0.2146 0.1513 0.0256  -0.0198 0.0232  70  ARG B N   
4062 C  CA  . ARG B 70  ? 0.2543 0.2021 0.1591 0.0221  -0.0270 0.0054  70  ARG B CA  
4063 C  C   . ARG B 70  ? 0.2422 0.1889 0.1716 0.0094  -0.0381 0.0358  70  ARG B C   
4064 O  O   . ARG B 70  ? 0.2451 0.1959 0.1963 -0.0060 -0.0533 0.0242  70  ARG B O   
4065 C  CB  . ARG B 70  ? 0.2945 0.2076 0.2230 0.0456  -0.0282 0.0003  70  ARG B CB  
4066 C  CG  . ARG B 70  ? 0.3542 0.2474 0.2638 0.0366  0.0048  0.0070  70  ARG B CG  
4067 C  CD  . ARG B 70  ? 0.4569 0.3795 0.3515 0.0823  -0.0608 0.0228  70  ARG B CD  
4068 N  NE  . ARG B 70  ? 0.4978 0.5113 0.4555 0.0595  -0.0403 0.0521  70  ARG B NE  
4069 C  CZ  . ARG B 70  ? 0.4901 0.5305 0.4099 0.0664  -0.0440 0.0805  70  ARG B CZ  
4070 N  NH1 . ARG B 70  ? 0.4250 0.4916 0.4063 0.1238  -0.0102 0.0115  70  ARG B NH1 
4071 N  NH2 . ARG B 70  ? 0.4068 0.4644 0.2884 0.0597  -0.1125 0.0304  70  ARG B NH2 
4085 N  N   . LEU B 71  ? 0.2219 0.1864 0.1634 -0.0026 -0.0380 0.0436  71  LEU B N   
4086 C  CA  . LEU B 71  ? 0.2198 0.2035 0.1601 -0.0138 -0.0274 0.0503  71  LEU B CA  
4087 C  C   . LEU B 71  ? 0.1861 0.1982 0.1609 -0.0185 -0.0189 0.0528  71  LEU B C   
4088 O  O   . LEU B 71  ? 0.1913 0.2179 0.1763 -0.0283 -0.0257 0.0593  71  LEU B O   
4089 C  CB  . LEU B 71  ? 0.2226 0.1899 0.1475 0.0132  -0.0114 0.0527  71  LEU B CB  
4090 C  CG  . LEU B 71  ? 0.2033 0.2111 0.1738 -0.0017 -0.0127 0.0688  71  LEU B CG  
4091 C  CD1 . LEU B 71  ? 0.2335 0.2572 0.1818 0.0171  -0.0398 0.0613  71  LEU B CD1 
4092 C  CD2 . LEU B 71  ? 0.2359 0.2190 0.2353 -0.0056 0.0091  0.0920  71  LEU B CD2 
4104 N  N   . VAL B 72  ? 0.1610 0.1798 0.1736 -0.0141 -0.0109 0.0462  72  VAL B N   
4105 C  CA  . VAL B 72  ? 0.1583 0.1800 0.1650 -0.0039 -0.0085 0.0417  72  VAL B CA  
4106 C  C   . VAL B 72  ? 0.1679 0.1833 0.1647 -0.0110 -0.0107 0.0581  72  VAL B C   
4107 O  O   . VAL B 72  ? 0.1558 0.2074 0.1879 -0.0111 -0.0196 0.0482  72  VAL B O   
4108 C  CB  . VAL B 72  ? 0.1520 0.1811 0.2147 0.0092  -0.0087 0.0447  72  VAL B CB  
4109 C  CG1 . VAL B 72  ? 0.1729 0.1723 0.2613 0.0006  -0.0185 0.0580  72  VAL B CG1 
4110 C  CG2 . VAL B 72  ? 0.1806 0.1833 0.2387 0.0064  -0.0169 0.0107  72  VAL B CG2 
4120 N  N   . ALA B 73  ? 0.1945 0.1990 0.1686 0.0117  -0.0132 0.0552  73  ALA B N   
4121 C  CA  . ALA B 73  ? 0.2600 0.1926 0.1687 0.0004  -0.0219 0.0415  73  ALA B CA  
4122 C  C   . ALA B 73  ? 0.2712 0.2105 0.1760 -0.0107 -0.0490 0.0540  73  ALA B C   
4123 O  O   . ALA B 73  ? 0.3200 0.2803 0.2321 -0.0144 -0.0879 0.0727  73  ALA B O   
4124 C  CB  . ALA B 73  ? 0.2923 0.2350 0.1744 0.0280  -0.0195 0.0440  73  ALA B CB  
4130 N  N   . LYS B 74  ? 0.2647 0.2143 0.1703 -0.0226 -0.0494 0.0496  74  LYS B N   
4131 C  CA  . LYS B 74  ? 0.2604 0.2267 0.2000 -0.0361 -0.0574 0.0354  74  LYS B CA  
4132 C  C   . LYS B 74  ? 0.2295 0.2261 0.2012 -0.0266 -0.0593 0.0381  74  LYS B C   
4133 O  O   . LYS B 74  ? 0.2374 0.2623 0.2421 -0.0472 -0.0509 0.0397  74  LYS B O   
4134 C  CB  . LYS B 74  ? 0.3405 0.2184 0.2450 -0.0280 -0.0486 0.0365  74  LYS B CB  
4135 C  CG  . LYS B 74  ? 0.4194 0.3329 0.3109 0.0692  -0.0369 -0.0263 74  LYS B CG  
4136 C  CD  . LYS B 74  ? 0.3946 0.3381 0.3142 0.0887  -0.0371 -0.0450 74  LYS B CD  
4137 C  CE  . LYS B 74  ? 0.4494 0.3957 0.2848 0.0486  -0.0358 -0.0387 74  LYS B CE  
4138 N  NZ  . LYS B 74  ? 0.5031 0.4273 0.2372 0.0502  -0.0574 0.0084  74  LYS B NZ  
4152 N  N   . GLN B 75  ? 0.2164 0.2089 0.1743 -0.0180 -0.0236 0.0580  75  GLN B N   
4153 C  CA  . GLN B 75  ? 0.1897 0.2037 0.1868 -0.0186 -0.0368 0.0485  75  GLN B CA  
4154 C  C   . GLN B 75  ? 0.1985 0.2260 0.2033 -0.0237 -0.0457 0.0746  75  GLN B C   
4155 O  O   . GLN B 75  ? 0.2298 0.2406 0.2647 -0.0133 -0.0237 0.1049  75  GLN B O   
4156 C  CB  . GLN B 75  ? 0.2162 0.2178 0.1742 -0.0234 -0.0188 0.0458  75  GLN B CB  
4157 C  CG  . GLN B 75  ? 0.2556 0.2281 0.2266 -0.0280 0.0061  0.0262  75  GLN B CG  
4158 C  CD  . GLN B 75  ? 0.2880 0.2656 0.2394 -0.0838 0.0251  0.0058  75  GLN B CD  
4159 O  OE1 . GLN B 75  ? 0.3219 0.3302 0.2059 -0.1410 -0.0111 0.0207  75  GLN B OE1 
4160 N  NE2 . GLN B 75  ? 0.3747 0.3100 0.2835 -0.1322 0.0547  -0.0203 75  GLN B NE2 
4169 N  N   . PRO B 76  ? 0.1756 0.2472 0.1783 -0.0206 -0.0329 0.0649  76  PRO B N   
4170 C  CA  . PRO B 76  ? 0.2030 0.2504 0.1823 -0.0044 -0.0242 0.0616  76  PRO B CA  
4171 C  C   . PRO B 76  ? 0.2101 0.2392 0.2101 0.0080  -0.0476 0.0348  76  PRO B C   
4172 O  O   . PRO B 76  ? 0.2412 0.2802 0.2262 0.0280  -0.0639 0.0180  76  PRO B O   
4173 C  CB  . PRO B 76  ? 0.1880 0.2497 0.1713 -0.0168 -0.0281 0.0315  76  PRO B CB  
4174 C  CG  . PRO B 76  ? 0.1825 0.2293 0.1609 -0.0115 -0.0332 0.0272  76  PRO B CG  
4175 C  CD  . PRO B 76  ? 0.1850 0.2193 0.1588 -0.0192 -0.0403 0.0459  76  PRO B CD  
4183 N  N   . SER B 77  ? 0.2269 0.2371 0.2642 0.0213  -0.0447 0.0516  77  SER B N   
4184 C  CA  . SER B 77  ? 0.2778 0.2495 0.2755 0.0061  -0.0347 0.0395  77  SER B CA  
4185 C  C   . SER B 77  ? 0.2450 0.2072 0.2373 0.0277  -0.0552 0.0230  77  SER B C   
4186 O  O   . SER B 77  ? 0.2291 0.2153 0.2417 0.0233  -0.0619 0.0256  77  SER B O   
4187 C  CB  . SER B 77  ? 0.3667 0.2683 0.2800 0.0449  -0.0010 0.0664  77  SER B CB  
4188 O  OG  . SER B 77  ? 0.4974 0.3339 0.3770 0.0161  0.0378  0.0794  77  SER B OG  
4194 N  N   . LEU B 78  ? 0.2455 0.2177 0.2625 0.0273  -0.0531 -0.0041 78  LEU B N   
4195 C  CA  . LEU B 78  ? 0.2576 0.2339 0.2221 0.0445  -0.0668 0.0057  78  LEU B CA  
4196 C  C   . LEU B 78  ? 0.2683 0.2198 0.2631 0.0519  -0.0608 0.0054  78  LEU B C   
4197 O  O   . LEU B 78  ? 0.2733 0.2497 0.2809 0.0617  -0.0594 0.0364  78  LEU B O   
4198 C  CB  . LEU B 78  ? 0.3026 0.2188 0.2602 0.0673  -0.0936 -0.0184 78  LEU B CB  
4199 C  CG  . LEU B 78  ? 0.2879 0.3018 0.2517 0.0502  -0.0948 -0.0073 78  LEU B CG  
4200 C  CD1 . LEU B 78  ? 0.3803 0.3709 0.3136 0.0319  -0.1456 -0.0222 78  LEU B CD1 
4201 C  CD2 . LEU B 78  ? 0.2488 0.3101 0.2248 0.0723  -0.0594 -0.0021 78  LEU B CD2 
4213 N  N   . GLY B 79  ? 0.2520 0.2009 0.2518 0.0607  -0.0579 0.0083  79  GLY B N   
4214 C  CA  . GLY B 79  ? 0.2350 0.2285 0.2822 0.0416  -0.0429 0.0151  79  GLY B CA  
4215 C  C   . GLY B 79  ? 0.2512 0.2409 0.2951 0.0672  -0.0684 0.0102  79  GLY B C   
4216 O  O   . GLY B 79  ? 0.2588 0.2976 0.3276 0.0903  -0.0726 0.0004  79  GLY B O   
4220 N  N   . ARG B 80  ? 0.2240 0.2779 0.2693 0.0627  -0.0852 0.0108  80  ARG B N   
4221 C  CA  . ARG B 80  ? 0.3835 0.3351 0.2836 0.0379  -0.1139 0.0081  80  ARG B CA  
4222 C  C   . ARG B 80  ? 1.0101 0.5030 0.7045 -0.2378 0.2980  0.0312  80  ARG B C   
4223 O  O   . ARG B 80  ? 0.4055 0.2904 0.4510 0.0839  0.1352  -0.0180 80  ARG B O   
4224 C  CB  . ARG B 80  ? 0.2269 0.2612 0.2478 0.0174  -0.0796 0.0090  80  ARG B CB  
4225 C  CG  . ARG B 80  ? 0.2359 0.2515 0.2098 0.0304  -0.0668 0.0083  80  ARG B CG  
4226 C  CD  . ARG B 80  ? 0.2207 0.2480 0.1982 0.0276  -0.0586 0.0102  80  ARG B CD  
4227 N  NE  . ARG B 80  ? 0.1863 0.2364 0.1900 0.0260  -0.0548 0.0116  80  ARG B NE  
4228 C  CZ  . ARG B 80  ? 0.1660 0.2366 0.1671 0.0113  -0.0386 -0.0004 80  ARG B CZ  
4229 N  NH1 . ARG B 80  ? 0.1783 0.2423 0.1699 -0.0101 -0.0288 0.0031  80  ARG B NH1 
4230 N  NH2 . ARG B 80  ? 0.1507 0.2178 0.1738 0.0083  -0.0469 0.0095  80  ARG B NH2 
4244 N  N   . ALA B 81  ? 0.8386 0.8065 0.5640 0.3027  -0.1375 0.0549  81  ALA B N   
4245 C  CA  . ALA B 81  ? 0.7599 1.2422 0.6706 0.4437  -0.1433 -0.1447 81  ALA B CA  
4246 C  C   . ALA B 81  ? 1.3953 1.3776 1.6210 0.5781  -0.3372 -0.4281 81  ALA B C   
4247 O  O   . ALA B 81  ? 0.8999 1.7891 0.7896 -0.1299 0.5147  0.7029  81  ALA B O   
4248 C  CB  . ALA B 81  ? 1.0172 1.1183 0.8473 0.5955  -0.1125 -0.0023 81  ALA B CB  
4254 N  N   . GLU B 82  ? 0.7150 1.3128 0.8270 -0.1409 -0.5531 -0.0505 82  GLU B N   
4255 C  CA  . GLU B 82  ? 0.1352 0.7176 0.2376 0.0755  -0.0768 0.0559  82  GLU B CA  
4256 C  C   . GLU B 82  ? 0.1744 0.3174 0.2502 0.0283  -0.0590 -0.0041 82  GLU B C   
4257 O  O   . GLU B 82  ? 0.1766 0.3385 0.2287 0.0112  -0.0643 -0.0257 82  GLU B O   
4258 C  CB  . GLU B 82  ? 0.2327 0.3547 0.2563 -0.0070 -0.0700 0.0352  82  GLU B CB  
4259 C  CG  . GLU B 82  ? 0.2842 0.3459 0.2590 -0.0100 -0.0433 -0.0117 82  GLU B CG  
4260 C  CD  . GLU B 82  ? 0.2670 0.3550 0.2508 0.0024  -0.0727 0.0054  82  GLU B CD  
4261 O  OE1 . GLU B 82  ? 0.3146 0.3748 0.2744 0.0132  -0.0883 0.0158  82  GLU B OE1 
4262 O  OE2 . GLU B 82  ? 0.2569 0.3505 0.2870 0.0215  -0.0638 -0.0130 82  GLU B OE2 
4269 N  N   . ALA B 83  ? 0.1664 0.3059 0.2338 0.0351  -0.0604 -0.0053 83  ALA B N   
4270 C  CA  . ALA B 83  ? 0.1615 0.2915 0.2214 0.0306  -0.0449 -0.0103 83  ALA B CA  
4271 C  C   . ALA B 83  ? 0.1726 0.2814 0.2244 0.0249  -0.0439 -0.0277 83  ALA B C   
4272 O  O   . ALA B 83  ? 0.2000 0.2935 0.2426 0.0174  -0.0462 -0.0424 83  ALA B O   
4273 C  CB  . ALA B 83  ? 0.1715 0.2765 0.2355 0.0295  -0.0558 0.0145  83  ALA B CB  
4279 N  N   . THR B 84  ? 0.1567 0.3047 0.2250 0.0176  -0.0420 -0.0247 84  THR B N   
4280 C  CA  . THR B 84  ? 0.1631 0.3090 0.2081 0.0281  -0.0382 -0.0338 84  THR B CA  
4281 C  C   . THR B 84  ? 0.1557 0.2994 0.1879 0.0062  -0.0290 -0.0339 84  THR B C   
4282 O  O   . THR B 84  ? 0.1812 0.3351 0.2160 0.0389  -0.0026 -0.0398 84  THR B O   
4283 C  CB  . THR B 84  ? 0.1647 0.3707 0.2215 0.0200  -0.0350 -0.0260 84  THR B CB  
4284 O  OG1 . THR B 84  ? 0.1607 0.4339 0.2513 -0.0031 -0.0556 -0.0579 84  THR B OG1 
4285 C  CG2 . THR B 84  ? 0.1828 0.3982 0.2683 0.0387  -0.0457 -0.0084 84  THR B CG2 
4293 N  N   . CYS B 85  ? 0.1291 0.2964 0.1775 -0.0095 -0.0298 -0.0346 85  CYS B N   
4294 C  CA  . CYS B 85  ? 0.1457 0.2673 0.1863 -0.0100 -0.0283 -0.0305 85  CYS B CA  
4295 C  C   . CYS B 85  ? 0.1209 0.2417 0.1794 0.0108  -0.0185 -0.0424 85  CYS B C   
4296 O  O   . CYS B 85  ? 0.1286 0.2539 0.1775 -0.0065 -0.0293 -0.0280 85  CYS B O   
4297 C  CB  . CYS B 85  ? 0.1844 0.2457 0.1786 -0.0280 -0.0212 -0.0502 85  CYS B CB  
4298 S  SG  . CYS B 85  ? 0.2378 0.3172 0.2338 -0.0797 -0.0499 -0.0538 85  CYS B SG  
4304 N  N   . ALA B 86  ? 0.1193 0.2284 0.1704 -0.0054 -0.0167 -0.0282 86  ALA B N   
4305 C  CA  . ALA B 86  ? 0.1215 0.2078 0.1635 -0.0131 -0.0193 -0.0192 86  ALA B CA  
4306 C  C   . ALA B 86  ? 0.1181 0.1859 0.1517 -0.0181 -0.0080 -0.0402 86  ALA B C   
4307 O  O   . ALA B 86  ? 0.1241 0.1870 0.1754 -0.0172 -0.0076 -0.0430 86  ALA B O   
4308 C  CB  . ALA B 86  ? 0.1347 0.2077 0.1887 0.0106  -0.0200 -0.0162 86  ALA B CB  
4314 N  N   . ALA B 87  ? 0.1162 0.1807 0.1464 -0.0108 -0.0120 -0.0234 87  ALA B N   
4315 C  CA  . ALA B 87  ? 0.1183 0.1618 0.1476 -0.0158 -0.0052 -0.0179 87  ALA B CA  
4316 C  C   . ALA B 87  ? 0.1073 0.1480 0.1450 -0.0104 -0.0032 -0.0220 87  ALA B C   
4317 O  O   . ALA B 87  ? 0.1278 0.1645 0.1358 -0.0170 -0.0096 -0.0180 87  ALA B O   
4318 C  CB  . ALA B 87  ? 0.1345 0.1500 0.1629 -0.0183 -0.0030 -0.0316 87  ALA B CB  
4324 N  N   . LEU B 88  ? 0.1025 0.1426 0.1437 -0.0053 -0.0025 -0.0164 88  LEU B N   
4325 C  CA  . LEU B 88  ? 0.1035 0.1304 0.1328 -0.0011 -0.0083 -0.0123 88  LEU B CA  
4326 C  C   . LEU B 88  ? 0.1036 0.1195 0.1300 -0.0019 -0.0043 -0.0178 88  LEU B C   
4327 O  O   . LEU B 88  ? 0.1011 0.1328 0.1407 -0.0066 0.0007  -0.0162 88  LEU B O   
4328 C  CB  . LEU B 88  ? 0.1074 0.1326 0.1449 0.0088  0.0060  -0.0170 88  LEU B CB  
4329 C  CG  . LEU B 88  ? 0.1186 0.1416 0.1516 0.0041  -0.0050 -0.0273 88  LEU B CG  
4330 C  CD1 . LEU B 88  ? 0.1211 0.1657 0.1577 -0.0044 -0.0110 -0.0374 88  LEU B CD1 
4331 C  CD2 . LEU B 88  ? 0.1559 0.1403 0.1726 0.0163  0.0127  -0.0255 88  LEU B CD2 
4343 N  N   . ILE B 89  ? 0.1010 0.1203 0.1337 0.0020  -0.0021 -0.0127 89  ILE B N   
4344 C  CA  . ILE B 89  ? 0.1029 0.1161 0.1241 0.0029  0.0066  -0.0096 89  ILE B CA  
4345 C  C   . ILE B 89  ? 0.0939 0.1130 0.1332 0.0071  0.0035  -0.0054 89  ILE B C   
4346 O  O   . ILE B 89  ? 0.1047 0.1290 0.1264 -0.0036 0.0037  -0.0092 89  ILE B O   
4347 C  CB  . ILE B 89  ? 0.1099 0.1111 0.1272 -0.0012 0.0050  -0.0109 89  ILE B CB  
4348 C  CG1 . ILE B 89  ? 0.1278 0.1290 0.1346 -0.0121 -0.0041 -0.0194 89  ILE B CG1 
4349 C  CG2 . ILE B 89  ? 0.1297 0.1227 0.1566 0.0103  -0.0080 -0.0216 89  ILE B CG2 
4350 C  CD1 . ILE B 89  ? 0.1412 0.1333 0.1418 -0.0057 -0.0032 -0.0164 89  ILE B CD1 
4362 N  N   . PRO B 90  ? 0.0976 0.1205 0.1299 -0.0011 0.0041  -0.0053 90  PRO B N   
4363 C  CA  . PRO B 90  ? 0.1000 0.1114 0.1261 0.0053  -0.0022 -0.0079 90  PRO B CA  
4364 C  C   . PRO B 90  ? 0.1117 0.1122 0.1231 0.0016  0.0048  -0.0059 90  PRO B C   
4365 O  O   . PRO B 90  ? 0.1156 0.1101 0.1491 -0.0021 -0.0046 -0.0033 90  PRO B O   
4366 C  CB  . PRO B 90  ? 0.1167 0.1330 0.1231 0.0105  0.0016  -0.0128 90  PRO B CB  
4367 C  CG  . PRO B 90  ? 0.1089 0.1410 0.1311 -0.0007 0.0061  -0.0107 90  PRO B CG  
4368 C  CD  . PRO B 90  ? 0.0923 0.1349 0.1304 -0.0105 0.0042  -0.0113 90  PRO B CD  
4376 N  N   . ILE B 91  ? 0.1039 0.1044 0.1252 0.0016  0.0006  -0.0101 91  ILE B N   
4377 C  CA  . ILE B 91  ? 0.1054 0.1178 0.1310 0.0125  -0.0002 -0.0137 91  ILE B CA  
4378 C  C   . ILE B 91  ? 0.0966 0.1177 0.1305 0.0118  -0.0045 -0.0158 91  ILE B C   
4379 O  O   . ILE B 91  ? 0.1168 0.1133 0.1262 0.0045  -0.0027 -0.0141 91  ILE B O   
4380 C  CB  . ILE B 91  ? 0.1145 0.1343 0.1302 0.0068  -0.0014 -0.0124 91  ILE B CB  
4381 C  CG1 . ILE B 91  ? 0.1287 0.1712 0.1494 0.0060  -0.0018 -0.0241 91  ILE B CG1 
4382 C  CG2 . ILE B 91  ? 0.1249 0.1571 0.1462 0.0139  -0.0051 -0.0100 91  ILE B CG2 
4383 C  CD1 . ILE B 91  ? 0.1668 0.1787 0.1478 -0.0018 0.0134  -0.0228 91  ILE B CD1 
4395 N  N   . ARG B 92  ? 0.1215 0.1163 0.1475 0.0161  -0.0236 -0.0193 92  ARG B N   
4396 C  CA  . ARG B 92  ? 0.1339 0.1343 0.1547 0.0305  -0.0329 -0.0257 92  ARG B CA  
4397 C  C   . ARG B 92  ? 0.1277 0.1288 0.1670 0.0299  -0.0328 -0.0275 92  ARG B C   
4398 O  O   . ARG B 92  ? 0.1418 0.1207 0.2159 0.0275  -0.0371 -0.0391 92  ARG B O   
4399 C  CB  . ARG B 92  ? 0.1595 0.1536 0.1531 0.0369  -0.0241 -0.0245 92  ARG B CB  
4400 C  CG  . ARG B 92  ? 0.1836 0.2365 0.1742 0.0500  -0.0433 -0.0408 92  ARG B CG  
4401 C  CD  . ARG B 92  ? 0.2464 0.3144 0.1714 0.0762  -0.0537 -0.0497 92  ARG B CD  
4402 N  NE  . ARG B 92  ? 0.2974 0.4243 0.3329 0.0352  -0.0559 -0.0555 92  ARG B NE  
4403 C  CZ  . ARG B 92  ? 0.3367 0.4701 0.3944 0.0183  -0.0772 -0.0886 92  ARG B CZ  
4404 N  NH1 . ARG B 92  ? 0.3382 0.5258 0.5120 0.0437  -0.1066 -0.0909 92  ARG B NH1 
4405 N  NH2 . ARG B 92  ? 0.3846 0.5906 0.4334 -0.0270 -0.0861 -0.1004 92  ARG B NH2 
4419 N  N   . LYS B 93  ? 0.1290 0.1292 0.1635 0.0316  -0.0307 -0.0251 93  LYS B N   
4420 C  CA  A LYS B 93  ? 0.1358 0.1432 0.1659 0.0412  -0.0253 -0.0204 93  LYS B CA  
4421 C  CA  B LYS B 93  ? 0.1350 0.1439 0.1683 0.0418  -0.0268 -0.0219 93  LYS B CA  
4422 C  C   . LYS B 93  ? 0.1744 0.2203 0.1759 0.0822  -0.0325 -0.0421 93  LYS B C   
4423 O  O   . LYS B 93  ? 0.1970 0.2880 0.1730 0.0899  -0.0320 -0.0623 93  LYS B O   
4424 C  CB  A LYS B 93  ? 0.1500 0.1633 0.2425 0.0337  -0.0024 -0.0042 93  LYS B CB  
4425 C  CB  B LYS B 93  ? 0.1391 0.1612 0.2584 0.0346  -0.0058 -0.0135 93  LYS B CB  
4426 C  CG  A LYS B 93  ? 0.1815 0.1971 0.1868 -0.0054 0.0265  -0.0248 93  LYS B CG  
4427 C  CG  B LYS B 93  ? 0.1969 0.2014 0.2163 -0.0037 0.0216  -0.0373 93  LYS B CG  
4428 C  CD  A LYS B 93  ? 0.2695 0.1707 0.1488 -0.0217 -0.0215 0.0122  93  LYS B CD  
4429 C  CD  B LYS B 93  ? 0.2952 0.1825 0.2305 -0.0097 -0.0313 -0.0361 93  LYS B CD  
4430 C  CE  A LYS B 93  ? 0.1656 0.1285 0.1898 -0.0376 -0.0191 0.0430  93  LYS B CE  
4431 C  CE  B LYS B 93  ? 0.2278 0.1995 0.2286 0.0017  -0.0240 -0.0224 93  LYS B CE  
4432 N  NZ  A LYS B 93  ? 0.1364 0.2135 0.2116 0.0068  -0.0275 0.0635  93  LYS B NZ  
4433 N  NZ  B LYS B 93  ? 0.3685 0.1901 0.2443 -0.0383 -0.0492 -0.0226 93  LYS B NZ  
4458 N  N   . ASN B 94  ? 0.1946 0.2464 0.1536 0.1179  -0.0034 -0.0062 94  ASN B N   
4459 C  CA  A ASN B 94  ? 0.1879 0.2604 0.1654 0.0827  0.0075  0.0366  94  ASN B CA  
4460 C  CA  B ASN B 94  ? 0.1887 0.2574 0.1484 0.0736  0.0222  0.0281  94  ASN B CA  
4461 C  C   . ASN B 94  ? 0.2274 0.2151 0.1527 0.1041  0.0196  0.0514  94  ASN B C   
4462 O  O   . ASN B 94  ? 0.1930 0.3147 0.2035 0.1066  0.0325  0.1061  94  ASN B O   
4463 C  CB  A ASN B 94  ? 0.1404 0.2112 0.1771 0.0360  0.0204  0.0406  94  ASN B CB  
4464 C  CB  B ASN B 94  ? 0.1883 0.1697 0.1809 0.0584  -0.0001 0.0468  94  ASN B CB  
4465 C  CG  A ASN B 94  ? 0.1480 0.1303 0.1719 0.0412  0.0185  0.0226  94  ASN B CG  
4466 C  CG  B ASN B 94  ? 0.1662 0.1477 0.2058 0.0264  -0.0214 0.0381  94  ASN B CG  
4467 O  OD1 A ASN B 94  ? 0.1788 0.1297 0.2449 0.0157  0.0642  -0.0223 94  ASN B OD1 
4468 O  OD1 B ASN B 94  ? 0.1859 0.1469 0.2266 0.0040  -0.0434 0.0559  94  ASN B OD1 
4469 N  ND2 A ASN B 94  ? 0.2246 0.1249 0.2211 0.0213  0.0209  0.0124  94  ASN B ND2 
4470 N  ND2 B ASN B 94  ? 0.1570 0.1530 0.2285 0.0270  -0.0263 0.0452  94  ASN B ND2 
4483 N  N   . PRO B 95  ? 0.3582 0.1781 0.1559 0.0329  0.0443  0.0169  95  PRO B N   
4484 C  CA  . PRO B 95  ? 0.4623 0.2001 0.1660 -0.0225 0.0524  -0.0226 95  PRO B CA  
4485 C  C   . PRO B 95  ? 0.3902 0.1459 0.1569 -0.0632 -0.0154 0.0236  95  PRO B C   
4486 O  O   . PRO B 95  ? 0.4839 0.1578 0.1762 -0.0991 -0.0363 0.0154  95  PRO B O   
4487 C  CB  . PRO B 95  ? 0.5423 0.2886 0.1876 -0.0611 0.0734  -0.0511 95  PRO B CB  
4488 C  CG  . PRO B 95  ? 0.4830 0.3215 0.2056 -0.0315 0.0541  0.0090  95  PRO B CG  
4489 C  CD  . PRO B 95  ? 0.4192 0.2500 0.1421 0.0100  0.0596  0.0216  95  PRO B CD  
4497 N  N   . SER B 96  ? 0.3009 0.1381 0.1557 -0.0461 -0.0554 0.0468  96  SER B N   
4498 C  CA  . SER B 96  ? 0.2393 0.1574 0.1962 -0.0564 -0.0843 0.0539  96  SER B CA  
4499 C  C   . SER B 96  ? 0.1847 0.1035 0.1763 -0.0293 -0.0532 0.0370  96  SER B C   
4500 O  O   . SER B 96  ? 0.1604 0.1250 0.1932 -0.0010 -0.0542 0.0296  96  SER B O   
4501 C  CB  . SER B 96  ? 0.2802 0.1552 0.2423 -0.0294 -0.0967 0.0841  96  SER B CB  
4502 O  OG  . SER B 96  ? 0.2918 0.1743 0.3101 -0.0128 -0.0532 0.0324  96  SER B OG  
4508 N  N   . TRP B 97  ? 0.1654 0.1250 0.1593 -0.0254 -0.0447 0.0382  97  TRP B N   
4509 C  CA  . TRP B 97  ? 0.1349 0.1135 0.1424 0.0012  -0.0158 0.0259  97  TRP B CA  
4510 C  C   . TRP B 97  ? 0.1148 0.1061 0.1340 0.0129  -0.0144 0.0134  97  TRP B C   
4511 O  O   . TRP B 97  ? 0.1148 0.1135 0.1382 -0.0015 -0.0068 0.0103  97  TRP B O   
4512 C  CB  . TRP B 97  ? 0.1331 0.1185 0.1412 -0.0113 -0.0070 0.0160  97  TRP B CB  
4513 C  CG  . TRP B 97  ? 0.1050 0.1166 0.1360 -0.0014 0.0012  0.0149  97  TRP B CG  
4514 C  CD1 . TRP B 97  ? 0.1176 0.1082 0.1384 0.0012  0.0063  0.0028  97  TRP B CD1 
4515 C  CD2 . TRP B 97  ? 0.1084 0.0979 0.1315 0.0002  -0.0153 0.0029  97  TRP B CD2 
4516 N  NE1 . TRP B 97  ? 0.1153 0.1019 0.1364 0.0156  -0.0002 0.0105  97  TRP B NE1 
4517 C  CE2 . TRP B 97  ? 0.1113 0.1026 0.1283 0.0121  -0.0017 0.0058  97  TRP B CE2 
4518 C  CE3 . TRP B 97  ? 0.1303 0.1066 0.1570 0.0137  -0.0122 -0.0072 97  TRP B CE3 
4519 C  CZ2 . TRP B 97  ? 0.1131 0.1354 0.1320 0.0134  -0.0023 0.0101  97  TRP B CZ2 
4520 C  CZ3 . TRP B 97  ? 0.1429 0.1383 0.1652 0.0222  -0.0179 -0.0243 97  TRP B CZ3 
4521 C  CH2 . TRP B 97  ? 0.1437 0.1550 0.1415 0.0190  -0.0079 -0.0161 97  TRP B CH2 
4532 N  N   . TRP B 98  ? 0.1263 0.1071 0.1372 0.0107  -0.0018 0.0173  98  TRP B N   
4533 C  CA  . TRP B 98  ? 0.1288 0.1097 0.1451 0.0097  -0.0045 0.0127  98  TRP B CA  
4534 C  C   . TRP B 98  ? 0.1291 0.1070 0.1633 0.0097  -0.0002 0.0067  98  TRP B C   
4535 O  O   . TRP B 98  ? 0.1391 0.1139 0.2302 0.0073  -0.0087 0.0189  98  TRP B O   
4536 C  CB  . TRP B 98  ? 0.1436 0.1436 0.1524 0.0279  -0.0035 0.0008  98  TRP B CB  
4537 C  CG  . TRP B 98  ? 0.1388 0.1351 0.1564 0.0232  0.0059  0.0001  98  TRP B CG  
4538 C  CD1 . TRP B 98  ? 0.1608 0.1529 0.1592 0.0242  0.0168  0.0302  98  TRP B CD1 
4539 C  CD2 . TRP B 98  ? 0.1089 0.0994 0.1740 0.0180  -0.0066 -0.0080 98  TRP B CD2 
4540 N  NE1 . TRP B 98  ? 0.1267 0.1558 0.2000 0.0195  0.0087  0.0047  98  TRP B NE1 
4541 C  CE2 . TRP B 98  ? 0.1243 0.1029 0.1947 0.0139  0.0032  -0.0120 98  TRP B CE2 
4542 C  CE3 . TRP B 98  ? 0.1292 0.1071 0.1846 0.0086  -0.0268 0.0031  98  TRP B CE3 
4543 C  CZ2 . TRP B 98  ? 0.1095 0.1210 0.2157 0.0096  -0.0088 -0.0303 98  TRP B CZ2 
4544 C  CZ3 . TRP B 98  ? 0.1581 0.1334 0.2003 0.0029  -0.0333 0.0134  98  TRP B CZ3 
4545 C  CH2 . TRP B 98  ? 0.1531 0.1467 0.2211 0.0063  -0.0391 0.0049  98  TRP B CH2 
4556 N  N   . GLY B 99  ? 0.1237 0.1244 0.1374 0.0099  -0.0107 0.0078  99  GLY B N   
4557 C  CA  . GLY B 99  ? 0.1328 0.1391 0.1458 0.0003  -0.0122 -0.0003 99  GLY B CA  
4558 C  C   . GLY B 99  ? 0.1171 0.1290 0.1419 0.0116  -0.0146 0.0129  99  GLY B C   
4559 O  O   . GLY B 99  ? 0.1185 0.1729 0.1637 -0.0018 -0.0133 -0.0079 99  GLY B O   
4563 N  N   . LEU B 100 ? 0.1185 0.1144 0.1347 0.0056  -0.0099 0.0149  100 LEU B N   
4564 C  CA  . LEU B 100 ? 0.1170 0.1134 0.1404 0.0076  -0.0083 0.0107  100 LEU B CA  
4565 C  C   . LEU B 100 ? 0.1121 0.1109 0.1490 0.0104  -0.0120 0.0081  100 LEU B C   
4566 O  O   . LEU B 100 ? 0.1194 0.1075 0.1484 0.0172  -0.0019 0.0064  100 LEU B O   
4567 C  CB  . LEU B 100 ? 0.1356 0.1116 0.1402 0.0109  -0.0059 0.0134  100 LEU B CB  
4568 C  CG  . LEU B 100 ? 0.1379 0.1190 0.1592 0.0042  -0.0105 0.0144  100 LEU B CG  
4569 C  CD1 . LEU B 100 ? 0.1694 0.1353 0.1866 -0.0079 -0.0219 0.0082  100 LEU B CD1 
4570 C  CD2 . LEU B 100 ? 0.1656 0.1110 0.2032 0.0083  -0.0152 0.0276  100 LEU B CD2 
4582 N  N   . SER B 101 ? 0.1151 0.1158 0.1438 0.0082  -0.0051 0.0106  101 SER B N   
4583 C  CA  A SER B 101 ? 0.1164 0.1219 0.1428 0.0082  0.0013  0.0143  101 SER B CA  
4584 C  CA  B SER B 101 ? 0.1132 0.1254 0.1459 0.0029  -0.0045 0.0107  101 SER B CA  
4585 C  C   . SER B 101 ? 0.1079 0.1131 0.1315 0.0094  0.0067  0.0015  101 SER B C   
4586 O  O   . SER B 101 ? 0.1098 0.1072 0.1417 0.0059  -0.0028 0.0025  101 SER B O   
4587 C  CB  A SER B 101 ? 0.1267 0.1328 0.1676 0.0178  0.0014  0.0306  101 SER B CB  
4588 C  CB  B SER B 101 ? 0.1172 0.1489 0.1653 0.0001  -0.0083 0.0123  101 SER B CB  
4589 O  OG  A SER B 101 ? 0.1672 0.1434 0.2450 0.0311  0.0530  0.0328  101 SER B OG  
4590 O  OG  B SER B 101 ? 0.1339 0.2113 0.2026 -0.0085 -0.0253 0.0182  101 SER B OG  
4601 N  N   . GLN B 102 ? 0.1064 0.1078 0.1444 0.0066  -0.0018 0.0142  102 GLN B N   
4602 C  CA  . GLN B 102 ? 0.1070 0.1167 0.1357 0.0042  -0.0020 0.0108  102 GLN B CA  
4603 C  C   . GLN B 102 ? 0.1060 0.1124 0.1396 0.0082  -0.0072 0.0125  102 GLN B C   
4604 O  O   . GLN B 102 ? 0.1101 0.1253 0.1547 0.0127  -0.0115 0.0040  102 GLN B O   
4605 C  CB  . GLN B 102 ? 0.1193 0.1172 0.1459 0.0084  0.0021  0.0089  102 GLN B CB  
4606 C  CG  . GLN B 102 ? 0.1190 0.1242 0.1393 0.0092  0.0056  0.0161  102 GLN B CG  
4607 C  CD  . GLN B 102 ? 0.1165 0.1248 0.1408 0.0158  0.0018  0.0187  102 GLN B CD  
4608 O  OE1 . GLN B 102 ? 0.1195 0.1342 0.1510 0.0189  0.0120  0.0219  102 GLN B OE1 
4609 N  NE2 . GLN B 102 ? 0.1282 0.1539 0.1536 0.0131  0.0011  0.0114  102 GLN B NE2 
4618 N  N   . ASP B 103 ? 0.1049 0.1313 0.1400 0.0076  0.0005  0.0032  103 ASP B N   
4619 C  CA  . ASP B 103 ? 0.1163 0.1336 0.1420 0.0124  0.0037  0.0014  103 ASP B CA  
4620 C  C   . ASP B 103 ? 0.1048 0.1308 0.1504 0.0173  0.0053  -0.0070 103 ASP B C   
4621 O  O   . ASP B 103 ? 0.1232 0.1335 0.1483 0.0079  0.0093  -0.0131 103 ASP B O   
4622 C  CB  . ASP B 103 ? 0.1203 0.1444 0.1612 0.0120  0.0062  -0.0039 103 ASP B CB  
4623 C  CG  . ASP B 103 ? 0.1133 0.1534 0.1890 0.0238  -0.0045 -0.0160 103 ASP B CG  
4624 O  OD1 . ASP B 103 ? 0.1347 0.1567 0.1825 0.0247  -0.0228 -0.0156 103 ASP B OD1 
4625 O  OD2 . ASP B 103 ? 0.1386 0.1958 0.2461 0.0439  -0.0057 -0.0210 103 ASP B OD2 
4630 N  N   . GLU B 104 ? 0.1160 0.1061 0.1487 0.0164  -0.0028 -0.0064 104 GLU B N   
4631 C  CA  . GLU B 104 ? 0.1078 0.1264 0.1550 0.0202  0.0029  -0.0056 104 GLU B CA  
4632 C  C   . GLU B 104 ? 0.1158 0.1172 0.1298 0.0159  -0.0021 -0.0010 104 GLU B C   
4633 O  O   . GLU B 104 ? 0.1259 0.1190 0.1566 0.0179  0.0014  -0.0118 104 GLU B O   
4634 C  CB  . GLU B 104 ? 0.1234 0.1235 0.1515 0.0217  -0.0069 0.0019  104 GLU B CB  
4635 C  CG  . GLU B 104 ? 0.1350 0.1455 0.1718 0.0286  -0.0041 0.0088  104 GLU B CG  
4636 C  CD  . GLU B 104 ? 0.1306 0.1297 0.1916 0.0313  -0.0213 -0.0071 104 GLU B CD  
4637 O  OE1 . GLU B 104 ? 0.1541 0.1561 0.1825 0.0328  -0.0185 0.0069  104 GLU B OE1 
4638 O  OE2 . GLU B 104 ? 0.1479 0.1585 0.2224 0.0455  -0.0377 -0.0126 104 GLU B OE2 
4645 N  N   . ARG B 105 ? 0.1060 0.1112 0.1338 0.0153  -0.0045 -0.0048 105 ARG B N   
4646 C  CA  . ARG B 105 ? 0.1121 0.1185 0.1279 0.0161  -0.0012 -0.0046 105 ARG B CA  
4647 C  C   . ARG B 105 ? 0.1106 0.1113 0.1350 0.0162  0.0090  -0.0101 105 ARG B C   
4648 O  O   . ARG B 105 ? 0.1137 0.1203 0.1364 0.0112  -0.0006 -0.0042 105 ARG B O   
4649 C  CB  . ARG B 105 ? 0.1086 0.1167 0.1268 0.0149  -0.0042 0.0006  105 ARG B CB  
4650 C  CG  . ARG B 105 ? 0.1179 0.1118 0.1334 0.0130  -0.0084 0.0103  105 ARG B CG  
4651 C  CD  . ARG B 105 ? 0.1191 0.0992 0.1247 0.0084  -0.0004 0.0071  105 ARG B CD  
4652 N  NE  . ARG B 105 ? 0.1262 0.0999 0.1325 0.0108  -0.0088 0.0073  105 ARG B NE  
4653 C  CZ  . ARG B 105 ? 0.1101 0.0944 0.1442 0.0125  0.0008  0.0050  105 ARG B CZ  
4654 N  NH1 . ARG B 105 ? 0.1149 0.1057 0.1460 0.0153  0.0071  0.0161  105 ARG B NH1 
4655 N  NH2 . ARG B 105 ? 0.1201 0.1034 0.1658 0.0096  -0.0038 0.0117  105 ARG B NH2 
4669 N  N   . ARG B 106 ? 0.1171 0.1175 0.1300 0.0133  0.0058  -0.0004 106 ARG B N   
4670 C  CA  . ARG B 106 ? 0.1134 0.1354 0.1218 0.0118  0.0009  -0.0147 106 ARG B CA  
4671 C  C   . ARG B 106 ? 0.1118 0.1316 0.1243 0.0145  0.0061  -0.0036 106 ARG B C   
4672 O  O   . ARG B 106 ? 0.1327 0.1375 0.1331 0.0083  0.0002  -0.0114 106 ARG B O   
4673 C  CB  . ARG B 106 ? 0.1291 0.1425 0.1316 0.0090  0.0087  -0.0030 106 ARG B CB  
4674 C  CG  . ARG B 106 ? 0.1328 0.1402 0.1420 0.0037  0.0043  0.0019  106 ARG B CG  
4675 C  CD  . ARG B 106 ? 0.1470 0.1556 0.1356 0.0208  0.0094  -0.0025 106 ARG B CD  
4676 N  NE  . ARG B 106 ? 0.1595 0.1530 0.1259 0.0279  0.0087  -0.0052 106 ARG B NE  
4677 C  CZ  . ARG B 106 ? 0.1616 0.1487 0.1273 0.0215  0.0066  0.0153  106 ARG B CZ  
4678 N  NH1 . ARG B 106 ? 0.1800 0.1634 0.1399 0.0494  0.0078  0.0061  106 ARG B NH1 
4679 N  NH2 . ARG B 106 ? 0.1654 0.1719 0.1323 0.0287  -0.0018 0.0036  106 ARG B NH2 
4693 N  N   . LYS B 107 ? 0.1172 0.1394 0.1417 0.0159  0.0108  -0.0158 107 LYS B N   
4694 C  CA  . LYS B 107 ? 0.1202 0.1477 0.1537 0.0151  0.0094  -0.0267 107 LYS B CA  
4695 C  C   . LYS B 107 ? 0.1285 0.1297 0.1534 0.0219  0.0098  -0.0270 107 LYS B C   
4696 O  O   . LYS B 107 ? 0.1393 0.1466 0.1488 0.0102  0.0112  -0.0262 107 LYS B O   
4697 C  CB  . LYS B 107 ? 0.1294 0.1525 0.1733 0.0309  0.0046  -0.0291 107 LYS B CB  
4698 C  CG  . LYS B 107 ? 0.1486 0.1746 0.2293 0.0436  -0.0011 -0.0386 107 LYS B CG  
4699 C  CD  . LYS B 107 ? 0.1908 0.2113 0.2732 0.0936  -0.0092 -0.0339 107 LYS B CD  
4700 C  CE  . LYS B 107 ? 0.2441 0.2288 0.3663 0.0927  -0.0101 -0.0340 107 LYS B CE  
4701 N  NZ  . LYS B 107 ? 0.2764 0.2978 0.4593 0.1269  -0.0302 -0.0257 107 LYS B NZ  
4715 N  N   . ILE B 108 ? 0.1202 0.1278 0.1433 0.0253  0.0054  -0.0146 108 ILE B N   
4716 C  CA  . ILE B 108 ? 0.1183 0.1301 0.1433 0.0180  0.0015  -0.0161 108 ILE B CA  
4717 C  C   . ILE B 108 ? 0.1183 0.1400 0.1272 0.0134  0.0066  -0.0186 108 ILE B C   
4718 O  O   . ILE B 108 ? 0.1275 0.1429 0.1502 0.0134  -0.0016 -0.0215 108 ILE B O   
4719 C  CB  . ILE B 108 ? 0.1297 0.1303 0.1435 0.0192  -0.0017 -0.0093 108 ILE B CB  
4720 C  CG1 . ILE B 108 ? 0.1382 0.1323 0.1618 0.0165  -0.0050 0.0009  108 ILE B CG1 
4721 C  CG2 . ILE B 108 ? 0.1399 0.1475 0.1524 -0.0019 0.0044  0.0003  108 ILE B CG2 
4722 C  CD1 . ILE B 108 ? 0.1435 0.1501 0.1657 0.0149  -0.0093 0.0164  108 ILE B CD1 
4734 N  N   . PHE B 109 ? 0.1237 0.1424 0.1305 0.0298  -0.0015 -0.0179 109 PHE B N   
4735 C  CA  . PHE B 109 ? 0.1144 0.1390 0.1394 0.0208  -0.0001 -0.0170 109 PHE B CA  
4736 C  C   . PHE B 109 ? 0.1224 0.1384 0.1378 0.0188  -0.0029 -0.0093 109 PHE B C   
4737 O  O   . PHE B 109 ? 0.1302 0.1473 0.1392 0.0167  -0.0056 -0.0152 109 PHE B O   
4738 C  CB  . PHE B 109 ? 0.1255 0.1445 0.1526 0.0297  -0.0135 -0.0203 109 PHE B CB  
4739 C  CG  . PHE B 109 ? 0.1236 0.1334 0.1599 0.0195  -0.0186 -0.0226 109 PHE B CG  
4740 C  CD1 . PHE B 109 ? 0.1279 0.1501 0.1821 0.0274  -0.0105 -0.0196 109 PHE B CD1 
4741 C  CD2 . PHE B 109 ? 0.1558 0.1408 0.1678 0.0198  -0.0213 -0.0169 109 PHE B CD2 
4742 C  CE1 . PHE B 109 ? 0.1208 0.1562 0.2060 0.0230  -0.0167 -0.0320 109 PHE B CE1 
4743 C  CE2 . PHE B 109 ? 0.1701 0.1473 0.2019 0.0135  -0.0447 -0.0212 109 PHE B CE2 
4744 C  CZ  . PHE B 109 ? 0.1546 0.1469 0.2119 0.0307  -0.0472 -0.0302 109 PHE B CZ  
4754 N  N   . GLU B 110 ? 0.1349 0.1409 0.1454 0.0172  -0.0042 -0.0101 110 GLU B N   
4755 C  CA  . GLU B 110 ? 0.1375 0.1637 0.1418 0.0128  0.0017  -0.0066 110 GLU B CA  
4756 C  C   . GLU B 110 ? 0.1412 0.1784 0.1401 0.0107  0.0055  -0.0073 110 GLU B C   
4757 O  O   . GLU B 110 ? 0.1558 0.1959 0.1508 0.0005  0.0140  -0.0291 110 GLU B O   
4758 C  CB  . GLU B 110 ? 0.1507 0.1736 0.1590 0.0013  0.0060  0.0099  110 GLU B CB  
4759 C  CG  . GLU B 110 ? 0.1658 0.1943 0.1538 0.0020  0.0060  0.0049  110 GLU B CG  
4760 C  CD  . GLU B 110 ? 0.1580 0.1760 0.1607 0.0116  -0.0024 0.0070  110 GLU B CD  
4761 O  OE1 . GLU B 110 ? 0.1490 0.1896 0.1615 0.0169  -0.0060 0.0064  110 GLU B OE1 
4762 O  OE2 . GLU B 110 ? 0.1803 0.2038 0.1595 0.0103  -0.0037 0.0014  110 GLU B OE2 
4769 N  N   . GLU B 111 ? 0.1390 0.1778 0.1531 0.0171  0.0069  -0.0179 111 GLU B N   
4770 C  CA  . GLU B 111 ? 0.1477 0.1952 0.1671 0.0143  0.0227  -0.0231 111 GLU B CA  
4771 C  C   . GLU B 111 ? 0.1467 0.1742 0.1628 0.0252  0.0152  -0.0302 111 GLU B C   
4772 O  O   . GLU B 111 ? 0.2016 0.1877 0.1668 0.0190  0.0185  -0.0482 111 GLU B O   
4773 C  CB  . GLU B 111 ? 0.1595 0.2190 0.2284 0.0033  0.0431  -0.0460 111 GLU B CB  
4774 C  CG  . GLU B 111 ? 0.2111 0.3035 0.3048 0.0374  0.0324  -0.0431 111 GLU B CG  
4775 C  CD  . GLU B 111 ? 0.2224 0.3425 0.3489 0.0441  0.0498  -0.0811 111 GLU B CD  
4776 O  OE1 . GLU B 111 ? 0.3302 0.3355 0.3636 0.0492  0.0284  -0.0807 111 GLU B OE1 
4777 O  OE2 . GLU B 111 ? 0.3033 0.3408 0.4571 0.0918  0.0059  -0.0673 111 GLU B OE2 
4784 N  N   . GLN B 112 ? 0.1467 0.1546 0.1636 0.0271  0.0146  -0.0399 112 GLN B N   
4785 C  CA  . GLN B 112 ? 0.1411 0.1468 0.1771 0.0280  0.0103  -0.0402 112 GLN B CA  
4786 C  C   . GLN B 112 ? 0.1531 0.1476 0.1676 0.0254  0.0007  -0.0345 112 GLN B C   
4787 O  O   . GLN B 112 ? 0.1658 0.1749 0.2167 0.0188  0.0178  -0.0707 112 GLN B O   
4788 C  CB  . GLN B 112 ? 0.1411 0.1694 0.1797 0.0309  0.0052  -0.0352 112 GLN B CB  
4789 C  CG  . GLN B 112 ? 0.1604 0.1666 0.1903 0.0376  0.0056  -0.0323 112 GLN B CG  
4790 C  CD  . GLN B 112 ? 0.1557 0.1810 0.2059 0.0410  -0.0071 -0.0258 112 GLN B CD  
4791 O  OE1 . GLN B 112 ? 0.2553 0.1990 0.2123 0.0756  -0.0200 -0.0326 112 GLN B OE1 
4792 N  NE2 . GLN B 112 ? 0.2742 0.1914 0.2066 0.0142  0.0061  -0.0113 112 GLN B NE2 
4801 N  N   . SER B 113 ? 0.1343 0.1455 0.1493 0.0204  0.0090  -0.0240 113 SER B N   
4802 C  CA  . SER B 113 ? 0.1346 0.1518 0.1506 0.0082  0.0104  -0.0180 113 SER B CA  
4803 C  C   . SER B 113 ? 0.1487 0.1580 0.1415 0.0151  0.0101  -0.0255 113 SER B C   
4804 O  O   . SER B 113 ? 0.1479 0.1652 0.1585 0.0034  -0.0002 -0.0291 113 SER B O   
4805 C  CB  . SER B 113 ? 0.1384 0.1473 0.1533 0.0035  0.0074  -0.0216 113 SER B CB  
4806 O  OG  . SER B 113 ? 0.1506 0.1561 0.1514 0.0066  0.0082  -0.0096 113 SER B OG  
4812 N  N   . ARG B 114 ? 0.1445 0.1526 0.1433 0.0151  0.0135  -0.0216 114 ARG B N   
4813 C  CA  . ARG B 114 ? 0.1657 0.1754 0.1438 0.0262  0.0034  -0.0256 114 ARG B CA  
4814 C  C   . ARG B 114 ? 0.1619 0.1544 0.1244 0.0147  0.0056  -0.0126 114 ARG B C   
4815 O  O   . ARG B 114 ? 0.1502 0.1684 0.1380 0.0113  -0.0026 -0.0179 114 ARG B O   
4816 C  CB  . ARG B 114 ? 0.1936 0.2075 0.1608 0.0431  -0.0029 -0.0485 114 ARG B CB  
4817 C  CG  . ARG B 114 ? 0.2606 0.2488 0.1970 0.0792  -0.0182 -0.0812 114 ARG B CG  
4818 C  CD  . ARG B 114 ? 0.3009 0.3344 0.2464 0.0916  0.0508  -0.0464 114 ARG B CD  
4819 N  NE  . ARG B 114 ? 0.2879 0.3814 0.2961 0.0582  0.1062  0.0050  114 ARG B NE  
4820 C  CZ  . ARG B 114 ? 0.3049 0.4500 0.3400 0.0762  0.0962  -0.0543 114 ARG B CZ  
4821 N  NH1 . ARG B 114 ? 0.3174 0.5163 0.4057 0.0883  0.0509  -0.1154 114 ARG B NH1 
4822 N  NH2 . ARG B 114 ? 0.3384 0.5427 0.4338 0.0579  0.0850  0.0061  114 ARG B NH2 
4836 N  N   . HIS B 115 ? 0.1352 0.1546 0.1381 0.0196  -0.0011 -0.0141 115 HIS B N   
4837 C  CA  . HIS B 115 ? 0.1283 0.1468 0.1325 0.0132  0.0065  -0.0095 115 HIS B CA  
4838 C  C   . HIS B 115 ? 0.1413 0.1588 0.1310 0.0184  0.0038  -0.0112 115 HIS B C   
4839 O  O   . HIS B 115 ? 0.1501 0.1673 0.1340 0.0131  -0.0052 -0.0113 115 HIS B O   
4840 C  CB  . HIS B 115 ? 0.1382 0.1379 0.1386 0.0189  0.0018  -0.0104 115 HIS B CB  
4841 C  CG  . HIS B 115 ? 0.1291 0.1381 0.1254 0.0142  0.0009  -0.0060 115 HIS B CG  
4842 N  ND1 . HIS B 115 ? 0.1639 0.1883 0.1762 0.0574  0.0397  0.0432  115 HIS B ND1 
4843 C  CD2 . HIS B 115 ? 0.1276 0.1382 0.1328 0.0165  -0.0028 -0.0045 115 HIS B CD2 
4844 C  CE1 . HIS B 115 ? 0.1602 0.1679 0.1736 0.0537  0.0304  0.0370  115 HIS B CE1 
4845 N  NE2 . HIS B 115 ? 0.1266 0.1349 0.1209 0.0146  -0.0100 -0.0066 115 HIS B NE2 
4853 N  N   . ILE B 116 ? 0.1424 0.1567 0.1403 0.0147  -0.0023 0.0012  116 ILE B N   
4854 C  CA  . ILE B 116 ? 0.1594 0.1734 0.1534 0.0145  -0.0052 0.0120  116 ILE B CA  
4855 C  C   . ILE B 116 ? 0.1614 0.1874 0.1652 0.0038  -0.0088 0.0106  116 ILE B C   
4856 O  O   . ILE B 116 ? 0.1745 0.1861 0.1548 0.0005  -0.0226 0.0142  116 ILE B O   
4857 C  CB  . ILE B 116 ? 0.1672 0.1772 0.1707 0.0090  -0.0114 0.0200  116 ILE B CB  
4858 C  CG1 . ILE B 116 ? 0.1799 0.1741 0.1900 0.0193  -0.0170 0.0040  116 ILE B CG1 
4859 C  CG2 . ILE B 116 ? 0.2096 0.1974 0.2046 -0.0047 -0.0333 0.0456  116 ILE B CG2 
4860 C  CD1 . ILE B 116 ? 0.2139 0.1726 0.1972 0.0068  -0.0142 0.0064  116 ILE B CD1 
4872 N  N   . HIS B 117 ? 0.1759 0.2088 0.1486 0.0100  -0.0064 0.0030  117 HIS B N   
4873 C  CA  . HIS B 117 ? 0.1708 0.2389 0.1485 0.0087  0.0021  -0.0100 117 HIS B CA  
4874 C  C   . HIS B 117 ? 0.1735 0.2286 0.1406 0.0148  -0.0091 -0.0155 117 HIS B C   
4875 O  O   . HIS B 117 ? 0.2102 0.2545 0.1449 0.0072  -0.0190 -0.0133 117 HIS B O   
4876 C  CB  . HIS B 117 ? 0.1646 0.2758 0.1595 0.0000  0.0083  -0.0366 117 HIS B CB  
4877 C  CG  . HIS B 117 ? 0.2138 0.3145 0.1823 0.0145  0.0186  -0.0528 117 HIS B CG  
4878 N  ND1 . HIS B 117 ? 0.2712 0.3735 0.1774 0.0128  0.0227  -0.0674 117 HIS B ND1 
4879 C  CD2 . HIS B 117 ? 0.2308 0.3081 0.2187 0.0120  -0.0114 -0.0825 117 HIS B CD2 
4880 C  CE1 . HIS B 117 ? 0.3136 0.3747 0.1923 0.0121  0.0083  -0.0801 117 HIS B CE1 
4881 N  NE2 . HIS B 117 ? 0.2902 0.3522 0.2389 0.0203  -0.0084 -0.0904 117 HIS B NE2 
4889 N  N   . ILE B 118 ? 0.1569 0.1976 0.1446 0.0154  -0.0083 -0.0200 118 ILE B N   
4890 C  CA  . ILE B 118 ? 0.1636 0.1819 0.1633 0.0065  -0.0126 -0.0182 118 ILE B CA  
4891 C  C   . ILE B 118 ? 0.1535 0.1772 0.1448 0.0056  -0.0118 -0.0145 118 ILE B C   
4892 O  O   . ILE B 118 ? 0.1588 0.2024 0.1432 0.0116  -0.0216 -0.0304 118 ILE B O   
4893 C  CB  . ILE B 118 ? 0.1620 0.1761 0.1741 0.0093  -0.0118 -0.0164 118 ILE B CB  
4894 C  CG1 . ILE B 118 ? 0.1778 0.1623 0.2015 0.0055  -0.0211 -0.0164 118 ILE B CG1 
4895 C  CG2 . ILE B 118 ? 0.1880 0.1700 0.2157 -0.0035 -0.0203 0.0012  118 ILE B CG2 
4896 C  CD1 . ILE B 118 ? 0.1787 0.1988 0.2348 0.0150  -0.0337 0.0114  118 ILE B CD1 
4908 N  N   . GLY B 119 ? 0.1427 0.1665 0.1464 0.0110  -0.0121 -0.0115 119 GLY B N   
4909 C  CA  . GLY B 119 ? 0.1569 0.1727 0.1390 0.0157  -0.0146 -0.0154 119 GLY B CA  
4910 C  C   . GLY B 119 ? 0.1751 0.1750 0.1447 0.0299  -0.0211 -0.0164 119 GLY B C   
4911 O  O   . GLY B 119 ? 0.1626 0.1916 0.1604 0.0233  -0.0278 -0.0050 119 GLY B O   
4915 N  N   . LEU B 120 ? 0.1787 0.2002 0.1303 0.0131  -0.0144 -0.0044 120 LEU B N   
4916 C  CA  . LEU B 120 ? 0.1801 0.2383 0.1504 0.0062  -0.0195 0.0090  120 LEU B CA  
4917 C  C   . LEU B 120 ? 0.1877 0.2438 0.1379 0.0064  -0.0185 0.0116  120 LEU B C   
4918 O  O   . LEU B 120 ? 0.2154 0.2729 0.1532 0.0061  -0.0342 0.0255  120 LEU B O   
4919 C  CB  . LEU B 120 ? 0.1977 0.2506 0.1559 -0.0108 -0.0138 0.0345  120 LEU B CB  
4920 C  CG  . LEU B 120 ? 0.2443 0.2389 0.1747 -0.0171 -0.0264 0.0381  120 LEU B CG  
4921 C  CD1 . LEU B 120 ? 0.2331 0.2892 0.2159 -0.0353 -0.0287 0.0651  120 LEU B CD1 
4922 C  CD2 . LEU B 120 ? 0.3044 0.2620 0.2118 -0.0053 -0.0355 0.0576  120 LEU B CD2 
4934 N  N   . GLN B 121 ? 0.1811 0.2428 0.1498 0.0074  -0.0207 -0.0194 121 GLN B N   
4935 C  CA  . GLN B 121 ? 0.2128 0.2623 0.1625 0.0120  -0.0245 -0.0374 121 GLN B CA  
4936 C  C   . GLN B 121 ? 0.2105 0.2684 0.1608 -0.0024 -0.0290 -0.0355 121 GLN B C   
4937 O  O   . GLN B 121 ? 0.2202 0.3316 0.1855 -0.0119 -0.0159 -0.0805 121 GLN B O   
4938 C  CB  . GLN B 121 ? 0.2441 0.2707 0.1858 0.0171  -0.0237 -0.0561 121 GLN B CB  
4939 C  CG  . GLN B 121 ? 0.2567 0.3126 0.2320 0.0238  -0.0376 -0.0777 121 GLN B CG  
4940 C  CD  . GLN B 121 ? 0.3253 0.3123 0.2924 0.0388  -0.0502 -0.1281 121 GLN B CD  
4941 O  OE1 . GLN B 121 ? 0.3905 0.3662 0.4171 -0.0209 -0.0818 -0.0188 121 GLN B OE1 
4942 N  NE2 . GLN B 121 ? 0.3816 0.3955 0.3214 0.0146  -0.0763 -0.0744 121 GLN B NE2 
4951 N  N   . TYR B 122 ? 0.1886 0.2287 0.1415 0.0041  -0.0128 -0.0115 122 TYR B N   
4952 C  CA  . TYR B 122 ? 0.1743 0.2122 0.1479 0.0128  -0.0150 -0.0112 122 TYR B CA  
4953 C  C   . TYR B 122 ? 0.1734 0.2221 0.1464 0.0028  -0.0294 -0.0110 122 TYR B C   
4954 O  O   . TYR B 122 ? 0.1769 0.2166 0.1588 0.0127  -0.0223 -0.0057 122 TYR B O   
4955 C  CB  . TYR B 122 ? 0.1946 0.1999 0.1574 -0.0034 -0.0187 -0.0057 122 TYR B CB  
4956 C  CG  . TYR B 122 ? 0.1728 0.2027 0.1435 0.0001  -0.0107 -0.0136 122 TYR B CG  
4957 C  CD1 . TYR B 122 ? 0.1869 0.1993 0.1494 -0.0049 -0.0252 -0.0004 122 TYR B CD1 
4958 C  CD2 . TYR B 122 ? 0.1727 0.2220 0.1546 -0.0102 -0.0216 0.0002  122 TYR B CD2 
4959 C  CE1 . TYR B 122 ? 0.1674 0.1959 0.1769 -0.0004 -0.0031 -0.0051 122 TYR B CE1 
4960 C  CE2 . TYR B 122 ? 0.1806 0.2081 0.1744 -0.0330 -0.0069 -0.0143 122 TYR B CE2 
4961 C  CZ  . TYR B 122 ? 0.1921 0.2035 0.1759 -0.0205 -0.0009 -0.0075 122 TYR B CZ  
4962 O  OH  . TYR B 122 ? 0.2275 0.2000 0.2283 -0.0028 -0.0100 -0.0355 122 TYR B OH  
4972 N  N   . LEU B 123 ? 0.1703 0.2163 0.1640 0.0082  -0.0282 0.0013  123 LEU B N   
4973 C  CA  . LEU B 123 ? 0.1801 0.2254 0.1610 0.0051  -0.0265 0.0132  123 LEU B CA  
4974 C  C   . LEU B 123 ? 0.1945 0.2644 0.1487 0.0140  -0.0076 0.0166  123 LEU B C   
4975 O  O   . LEU B 123 ? 0.2110 0.3120 0.1577 0.0363  0.0013  0.0160  123 LEU B O   
4976 C  CB  . LEU B 123 ? 0.1914 0.2039 0.1919 -0.0171 -0.0058 0.0272  123 LEU B CB  
4977 C  CG  . LEU B 123 ? 0.2507 0.2686 0.2271 -0.0595 -0.0524 0.0495  123 LEU B CG  
4978 C  CD1 . LEU B 123 ? 0.2164 0.2542 0.2505 -0.0542 -0.0608 0.0863  123 LEU B CD1 
4979 C  CD2 . LEU B 123 ? 0.1837 0.2783 0.2638 -0.0366 -0.0054 -0.0834 123 LEU B CD2 
4991 N  N   . PRO B 124 ? 0.2023 0.2564 0.1448 0.0177  -0.0270 0.0158  124 PRO B N   
4992 C  CA  . PRO B 124 ? 0.1964 0.2399 0.1490 0.0117  -0.0313 0.0162  124 PRO B CA  
4993 C  C   . PRO B 124 ? 0.1663 0.2414 0.1355 0.0078  -0.0352 0.0126  124 PRO B C   
4994 O  O   . PRO B 124 ? 0.1775 0.2568 0.1712 0.0198  -0.0240 0.0035  124 PRO B O   
4995 C  CB  . PRO B 124 ? 0.2446 0.2766 0.1648 0.0274  -0.0392 0.0297  124 PRO B CB  
4996 C  CG  . PRO B 124 ? 0.2347 0.3128 0.1552 0.0282  -0.0324 0.0310  124 PRO B CG  
4997 C  CD  . PRO B 124 ? 0.2219 0.2771 0.1537 0.0113  -0.0280 0.0236  124 PRO B CD  
5005 N  N   . ALA B 125 ? 0.1817 0.2334 0.1335 -0.0057 -0.0357 -0.0076 125 ALA B N   
5006 C  CA  . ALA B 125 ? 0.1528 0.2318 0.1562 -0.0069 -0.0389 -0.0204 125 ALA B CA  
5007 C  C   . ALA B 125 ? 0.1507 0.2264 0.1400 -0.0142 -0.0279 -0.0012 125 ALA B C   
5008 O  O   . ALA B 125 ? 0.1545 0.2239 0.1560 -0.0044 -0.0390 -0.0218 125 ALA B O   
5009 C  CB  . ALA B 125 ? 0.1806 0.2275 0.1650 -0.0118 -0.0139 -0.0233 125 ALA B CB  
5015 N  N   . VAL B 126 ? 0.1492 0.1970 0.1299 -0.0047 -0.0297 -0.0132 126 VAL B N   
5016 C  CA  . VAL B 126 ? 0.1576 0.1967 0.1387 -0.0047 -0.0247 -0.0160 126 VAL B CA  
5017 C  C   . VAL B 126 ? 0.1351 0.1895 0.1537 -0.0030 -0.0260 -0.0013 126 VAL B C   
5018 O  O   . VAL B 126 ? 0.1496 0.2075 0.1665 -0.0159 -0.0178 -0.0154 126 VAL B O   
5019 C  CB  . VAL B 126 ? 0.1607 0.1910 0.1400 -0.0114 -0.0277 -0.0116 126 VAL B CB  
5020 C  CG1 . VAL B 126 ? 0.1901 0.2039 0.1368 -0.0170 -0.0391 0.0013  126 VAL B CG1 
5021 C  CG2 . VAL B 126 ? 0.1667 0.2090 0.1430 -0.0069 -0.0195 -0.0153 126 VAL B CG2 
5031 N  N   . ALA B 127 ? 0.1410 0.1836 0.1333 0.0035  -0.0300 -0.0073 127 ALA B N   
5032 C  CA  . ALA B 127 ? 0.1526 0.1669 0.1436 0.0004  -0.0316 0.0047  127 ALA B CA  
5033 C  C   . ALA B 127 ? 0.1430 0.1617 0.1339 0.0023  -0.0315 -0.0015 127 ALA B C   
5034 O  O   . ALA B 127 ? 0.1465 0.1894 0.1310 -0.0111 -0.0284 -0.0016 127 ALA B O   
5035 C  CB  . ALA B 127 ? 0.1539 0.1776 0.1687 0.0047  -0.0313 0.0094  127 ALA B CB  
5041 N  N   . ARG B 128 ? 0.1361 0.1797 0.1332 -0.0042 -0.0272 0.0027  128 ARG B N   
5042 C  CA  . ARG B 128 ? 0.1347 0.1620 0.1381 0.0024  -0.0298 0.0055  128 ARG B CA  
5043 C  C   . ARG B 128 ? 0.1339 0.1483 0.1364 0.0034  -0.0250 0.0125  128 ARG B C   
5044 O  O   . ARG B 128 ? 0.1625 0.1512 0.1467 -0.0064 -0.0316 0.0173  128 ARG B O   
5045 C  CB  . ARG B 128 ? 0.1390 0.1606 0.1354 0.0066  -0.0212 0.0016  128 ARG B CB  
5046 C  CG  . ARG B 128 ? 0.1448 0.1638 0.1565 0.0079  -0.0124 0.0105  128 ARG B CG  
5047 C  CD  . ARG B 128 ? 0.1438 0.1965 0.1540 0.0041  -0.0053 0.0057  128 ARG B CD  
5048 N  NE  . ARG B 128 ? 0.1542 0.2292 0.1645 0.0009  -0.0140 0.0203  128 ARG B NE  
5049 C  CZ  . ARG B 128 ? 0.1714 0.2222 0.1691 -0.0038 -0.0132 0.0207  128 ARG B CZ  
5050 N  NH1 . ARG B 128 ? 0.1629 0.2680 0.1706 -0.0131 -0.0177 0.0011  128 ARG B NH1 
5051 N  NH2 . ARG B 128 ? 0.1852 0.2696 0.2000 -0.0444 -0.0250 0.0294  128 ARG B NH2 
5065 N  N   . ARG B 129 ? 0.1307 0.1473 0.1306 -0.0005 -0.0270 0.0012  129 ARG B N   
5066 C  CA  . ARG B 129 ? 0.1396 0.1397 0.1370 0.0016  -0.0226 0.0003  129 ARG B CA  
5067 C  C   . ARG B 129 ? 0.1286 0.1443 0.1201 -0.0019 -0.0057 -0.0022 129 ARG B C   
5068 O  O   . ARG B 129 ? 0.1352 0.1765 0.1431 -0.0252 -0.0202 0.0225  129 ARG B O   
5069 C  CB  . ARG B 129 ? 0.1452 0.1598 0.1640 0.0043  -0.0248 -0.0107 129 ARG B CB  
5070 C  CG  . ARG B 129 ? 0.1591 0.1577 0.2082 0.0119  -0.0208 -0.0248 129 ARG B CG  
5071 C  CD  . ARG B 129 ? 0.2191 0.1782 0.2429 0.0263  -0.0139 -0.0203 129 ARG B CD  
5072 N  NE  . ARG B 129 ? 0.2776 0.2425 0.3077 0.0495  0.0176  0.0233  129 ARG B NE  
5073 C  CZ  . ARG B 129 ? 0.3117 0.2592 0.3170 0.0859  -0.0098 0.0413  129 ARG B CZ  
5074 N  NH1 . ARG B 129 ? 0.3126 0.3229 0.2512 0.1305  -0.0146 -0.0305 129 ARG B NH1 
5075 N  NH2 . ARG B 129 ? 0.3995 0.3027 0.3504 0.0713  -0.0079 0.0982  129 ARG B NH2 
5089 N  N   . LEU B 130 ? 0.1144 0.1324 0.1277 -0.0032 -0.0124 0.0041  130 LEU B N   
5090 C  CA  . LEU B 130 ? 0.1165 0.1208 0.1204 -0.0008 -0.0046 -0.0046 130 LEU B CA  
5091 C  C   . LEU B 130 ? 0.1071 0.1135 0.1308 0.0058  -0.0043 -0.0014 130 LEU B C   
5092 O  O   . LEU B 130 ? 0.1380 0.1218 0.1360 -0.0010 0.0064  -0.0060 130 LEU B O   
5093 C  CB  . LEU B 130 ? 0.1137 0.1233 0.1273 0.0043  -0.0032 -0.0011 130 LEU B CB  
5094 C  CG  . LEU B 130 ? 0.1104 0.1388 0.1299 0.0072  -0.0019 -0.0051 130 LEU B CG  
5095 C  CD1 . LEU B 130 ? 0.1249 0.1534 0.1508 0.0101  -0.0034 0.0124  130 LEU B CD1 
5096 C  CD2 . LEU B 130 ? 0.1271 0.1406 0.1472 -0.0019 -0.0105 -0.0082 130 LEU B CD2 
5108 N  N   . HIS B 131 ? 0.1110 0.1142 0.1189 0.0024  -0.0038 -0.0055 131 HIS B N   
5109 C  CA  . HIS B 131 ? 0.1106 0.1141 0.1251 0.0072  -0.0060 -0.0043 131 HIS B CA  
5110 C  C   . HIS B 131 ? 0.1058 0.1069 0.1165 -0.0021 0.0002  -0.0016 131 HIS B C   
5111 O  O   . HIS B 131 ? 0.1161 0.1132 0.1438 -0.0071 -0.0128 -0.0021 131 HIS B O   
5112 C  CB  . HIS B 131 ? 0.1144 0.1338 0.1299 0.0167  -0.0022 -0.0125 131 HIS B CB  
5113 C  CG  . HIS B 131 ? 0.1088 0.1351 0.1344 0.0130  0.0010  -0.0085 131 HIS B CG  
5114 N  ND1 . HIS B 131 ? 0.1150 0.1358 0.1473 0.0128  -0.0061 -0.0180 131 HIS B ND1 
5115 C  CD2 . HIS B 131 ? 0.1141 0.1469 0.1626 0.0213  -0.0057 -0.0165 131 HIS B CD2 
5116 C  CE1 . HIS B 131 ? 0.1145 0.1656 0.1549 0.0115  -0.0060 -0.0248 131 HIS B CE1 
5117 N  NE2 . HIS B 131 ? 0.1247 0.1625 0.1750 0.0261  -0.0181 -0.0085 131 HIS B NE2 
5125 N  N   . HIS B 132 ? 0.1054 0.0988 0.1216 0.0041  0.0014  0.0008  132 HIS B N   
5126 C  CA  . HIS B 132 ? 0.0970 0.1069 0.1240 0.0038  0.0006  -0.0060 132 HIS B CA  
5127 C  C   . HIS B 132 ? 0.0954 0.1059 0.1232 0.0085  0.0059  -0.0063 132 HIS B C   
5128 O  O   . HIS B 132 ? 0.1186 0.1086 0.1365 0.0205  0.0085  -0.0028 132 HIS B O   
5129 C  CB  . HIS B 132 ? 0.1050 0.1061 0.1211 0.0060  0.0031  -0.0067 132 HIS B CB  
5130 C  CG  . HIS B 132 ? 0.1093 0.0989 0.1286 0.0004  0.0067  -0.0052 132 HIS B CG  
5131 N  ND1 . HIS B 132 ? 0.1295 0.1210 0.1311 0.0093  0.0206  -0.0024 132 HIS B ND1 
5132 C  CD2 . HIS B 132 ? 0.1356 0.1130 0.1365 -0.0117 0.0082  -0.0039 132 HIS B CD2 
5133 C  CE1 . HIS B 132 ? 0.1499 0.1374 0.1425 -0.0044 0.0334  -0.0066 132 HIS B CE1 
5134 N  NE2 . HIS B 132 ? 0.1737 0.1170 0.1277 -0.0143 0.0248  -0.0077 132 HIS B NE2 
5142 N  N   . CYS B 133 ? 0.1054 0.1084 0.1198 0.0074  0.0054  -0.0042 133 CYS B N   
5143 C  CA  . CYS B 133 ? 0.1039 0.1105 0.1249 0.0139  0.0016  -0.0087 133 CYS B CA  
5144 C  C   . CYS B 133 ? 0.0997 0.1063 0.1222 -0.0033 0.0075  -0.0040 133 CYS B C   
5145 O  O   . CYS B 133 ? 0.1180 0.1287 0.1221 -0.0026 0.0004  -0.0132 133 CYS B O   
5146 C  CB  . CYS B 133 ? 0.1073 0.1194 0.1220 0.0015  0.0044  -0.0125 133 CYS B CB  
5147 S  SG  . CYS B 133 ? 0.1013 0.1327 0.1419 -0.0001 0.0026  -0.0135 133 CYS B SG  
5153 N  N   . ARG B 134 ? 0.1058 0.0979 0.1295 0.0016  0.0017  -0.0050 134 ARG B N   
5154 C  CA  . ARG B 134 ? 0.1087 0.1150 0.1364 0.0002  -0.0043 0.0084  134 ARG B CA  
5155 C  C   . ARG B 134 ? 0.0993 0.1287 0.1255 0.0023  -0.0021 -0.0016 134 ARG B C   
5156 O  O   . ARG B 134 ? 0.1280 0.1318 0.1346 -0.0004 -0.0084 0.0036  134 ARG B O   
5157 C  CB  . ARG B 134 ? 0.1132 0.1112 0.1639 0.0001  -0.0139 0.0104  134 ARG B CB  
5158 C  CG  . ARG B 134 ? 0.1511 0.1401 0.1555 0.0040  0.0053  0.0085  134 ARG B CG  
5159 C  CD  . ARG B 134 ? 0.1360 0.1534 0.1764 0.0050  0.0037  0.0046  134 ARG B CD  
5160 N  NE  . ARG B 134 ? 0.1686 0.1331 0.1952 0.0252  0.0067  0.0115  134 ARG B NE  
5161 C  CZ  . ARG B 134 ? 0.1530 0.1238 0.1830 0.0159  0.0092  0.0020  134 ARG B CZ  
5162 N  NH1 . ARG B 134 ? 0.1605 0.1422 0.1845 -0.0011 -0.0021 0.0033  134 ARG B NH1 
5163 N  NH2 . ARG B 134 ? 0.1628 0.1873 0.1698 0.0359  -0.0113 -0.0084 134 ARG B NH2 
5177 N  N   . ASP B 135 ? 0.1047 0.1151 0.1272 -0.0031 -0.0046 -0.0004 135 ASP B N   
5178 C  CA  . ASP B 135 ? 0.1064 0.1149 0.1432 -0.0019 0.0022  -0.0177 135 ASP B CA  
5179 C  C   . ASP B 135 ? 0.1079 0.1387 0.1596 -0.0025 -0.0048 -0.0293 135 ASP B C   
5180 O  O   . ASP B 135 ? 0.1099 0.1422 0.2065 -0.0065 0.0026  -0.0395 135 ASP B O   
5181 C  CB  . ASP B 135 ? 0.1118 0.1106 0.1438 0.0055  0.0002  -0.0042 135 ASP B CB  
5182 C  CG  . ASP B 135 ? 0.1168 0.1192 0.1351 -0.0015 0.0013  -0.0035 135 ASP B CG  
5183 O  OD1 . ASP B 135 ? 0.1166 0.1277 0.1490 0.0096  -0.0028 -0.0024 135 ASP B OD1 
5184 O  OD2 . ASP B 135 ? 0.1440 0.2068 0.1503 0.0446  -0.0056 -0.0211 135 ASP B OD2 
5189 N  N   . LEU B 136 ? 0.1056 0.1462 0.1692 0.0068  -0.0008 -0.0241 136 LEU B N   
5190 C  CA  . LEU B 136 ? 0.1187 0.1734 0.1806 -0.0045 0.0082  -0.0446 136 LEU B CA  
5191 C  C   . LEU B 136 ? 0.1578 0.2128 0.2067 -0.0486 0.0326  -0.0578 136 LEU B C   
5192 O  O   . LEU B 136 ? 0.2014 0.3398 0.1834 -0.0226 -0.0147 -0.0425 136 LEU B O   
5193 C  CB  . LEU B 136 ? 0.1020 0.1683 0.1740 0.0018  0.0014  -0.0284 136 LEU B CB  
5194 C  CG  . LEU B 136 ? 0.1236 0.1988 0.1650 -0.0036 0.0168  -0.0213 136 LEU B CG  
5195 C  CD1 . LEU B 136 ? 0.1295 0.1838 0.2000 -0.0166 0.0006  -0.0516 136 LEU B CD1 
5196 C  CD2 . LEU B 136 ? 0.1506 0.2404 0.2243 -0.0414 -0.0036 0.0259  136 LEU B CD2 
5208 N  N   . GLY B 137 ? 0.1930 0.2076 0.2641 -0.0675 0.0728  -0.0984 137 GLY B N   
5209 C  CA  . GLY B 137 ? 0.2942 0.2867 0.2374 -0.1100 0.0319  -0.0558 137 GLY B CA  
5210 C  C   . GLY B 137 ? 0.2381 0.2717 0.1761 -0.0965 0.0228  -0.0411 137 GLY B C   
5211 O  O   . GLY B 137 ? 0.2613 0.3301 0.1889 -0.0790 0.0097  -0.0317 137 GLY B O   
5215 N  N   . GLU B 138 ? 0.2676 0.2751 0.1786 -0.1251 0.0127  -0.0135 138 GLU B N   
5216 C  CA  . GLU B 138 ? 0.2368 0.2199 0.1887 -0.0598 0.0348  -0.0211 138 GLU B CA  
5217 C  C   . GLU B 138 ? 0.2107 0.2134 0.1566 -0.0518 0.0405  -0.0333 138 GLU B C   
5218 O  O   . GLU B 138 ? 0.2296 0.2377 0.1498 -0.0238 0.0251  -0.0360 138 GLU B O   
5219 C  CB  . GLU B 138 ? 0.2617 0.2314 0.2576 -0.0242 0.0142  -0.0549 138 GLU B CB  
5220 C  CG  . GLU B 138 ? 0.2509 0.2511 0.3086 0.0187  0.0196  -0.0582 138 GLU B CG  
5221 C  CD  . GLU B 138 ? 0.2201 0.2576 0.2760 0.0093  0.0357  -0.0322 138 GLU B CD  
5222 O  OE1 . GLU B 138 ? 0.2937 0.2900 0.3044 -0.0457 0.0452  -0.0346 138 GLU B OE1 
5223 O  OE2 . GLU B 138 ? 0.2007 0.2815 0.2462 0.0049  0.0303  -0.0752 138 GLU B OE2 
5230 N  N   . ASN B 139 ? 0.2767 0.2082 0.1685 -0.0579 0.0117  -0.0242 139 ASN B N   
5231 C  CA  . ASN B 139 ? 0.2962 0.2325 0.1966 -0.0200 -0.0366 -0.0335 139 ASN B CA  
5232 C  C   . ASN B 139 ? 0.2725 0.2057 0.1777 -0.0272 -0.0044 -0.0380 139 ASN B C   
5233 O  O   . ASN B 139 ? 0.3137 0.2519 0.2477 -0.0357 0.0578  -0.0702 139 ASN B O   
5234 C  CB  . ASN B 139 ? 0.4422 0.2876 0.2188 -0.0444 -0.0477 -0.0213 139 ASN B CB  
5235 C  CG  . ASN B 139 ? 0.4658 0.2846 0.3696 -0.0089 -0.0102 -0.0119 139 ASN B CG  
5236 O  OD1 . ASN B 139 ? 0.5001 0.3512 0.5192 0.0983  -0.0415 0.0045  139 ASN B OD1 
5237 N  ND2 . ASN B 139 ? 0.4631 0.3850 0.4064 0.0042  0.0213  -0.0103 139 ASN B ND2 
5244 N  N   . GLU B 140 ? 0.1877 0.2246 0.1547 -0.0103 -0.0127 -0.0339 140 GLU B N   
5245 C  CA  . GLU B 140 ? 0.1486 0.1927 0.1478 0.0000  -0.0022 -0.0248 140 GLU B CA  
5246 C  C   . GLU B 140 ? 0.1349 0.2052 0.1420 0.0122  0.0126  -0.0276 140 GLU B C   
5247 O  O   . GLU B 140 ? 0.1406 0.2122 0.1790 0.0090  -0.0073 -0.0195 140 GLU B O   
5248 C  CB  . GLU B 140 ? 0.1410 0.1812 0.1468 0.0120  0.0005  -0.0238 140 GLU B CB  
5249 C  CG  . GLU B 140 ? 0.1371 0.1949 0.1590 0.0057  0.0054  -0.0182 140 GLU B CG  
5250 C  CD  . GLU B 140 ? 0.1424 0.1867 0.1540 0.0229  0.0159  -0.0136 140 GLU B CD  
5251 O  OE1 . GLU B 140 ? 0.1334 0.2127 0.1535 -0.0026 0.0107  -0.0269 140 GLU B OE1 
5252 O  OE2 . GLU B 140 ? 0.1640 0.2134 0.1971 0.0438  0.0287  0.0038  140 GLU B OE2 
5259 N  N   . PRO B 141 ? 0.1447 0.1830 0.1479 0.0094  0.0139  -0.0122 141 PRO B N   
5260 C  CA  . PRO B 141 ? 0.1555 0.1788 0.1408 0.0230  0.0218  0.0086  141 PRO B CA  
5261 C  C   . PRO B 141 ? 0.1344 0.1701 0.1355 0.0129  0.0185  0.0041  141 PRO B C   
5262 O  O   . PRO B 141 ? 0.2231 0.1971 0.1519 0.0565  0.0350  0.0270  141 PRO B O   
5263 C  CB  . PRO B 141 ? 0.1948 0.2077 0.1627 0.0109  0.0495  0.0014  141 PRO B CB  
5264 C  CG  . PRO B 141 ? 0.1534 0.2136 0.1833 0.0041  0.0305  -0.0230 141 PRO B CG  
5265 C  CD  . PRO B 141 ? 0.1496 0.2019 0.1476 0.0144  0.0299  -0.0141 141 PRO B CD  
5273 N  N   . PHE B 142 ? 0.1188 0.1453 0.1293 0.0037  0.0130  -0.0025 142 PHE B N   
5274 C  CA  . PHE B 142 ? 0.1121 0.1333 0.1273 0.0032  0.0165  0.0000  142 PHE B CA  
5275 C  C   . PHE B 142 ? 0.1158 0.1145 0.1195 0.0091  0.0044  -0.0055 142 PHE B C   
5276 O  O   . PHE B 142 ? 0.1274 0.1244 0.1282 0.0036  0.0159  -0.0130 142 PHE B O   
5277 C  CB  . PHE B 142 ? 0.1107 0.1382 0.1329 0.0079  0.0114  -0.0028 142 PHE B CB  
5278 C  CG  . PHE B 142 ? 0.1188 0.1444 0.1268 -0.0002 0.0057  -0.0022 142 PHE B CG  
5279 C  CD1 . PHE B 142 ? 0.1247 0.1431 0.1492 -0.0083 -0.0029 -0.0028 142 PHE B CD1 
5280 C  CD2 . PHE B 142 ? 0.1242 0.1461 0.1317 -0.0017 0.0136  -0.0059 142 PHE B CD2 
5281 C  CE1 . PHE B 142 ? 0.1364 0.1434 0.1609 -0.0139 0.0044  0.0095  142 PHE B CE1 
5282 C  CE2 . PHE B 142 ? 0.1266 0.1781 0.1525 -0.0188 0.0203  -0.0150 142 PHE B CE2 
5283 C  CZ  . PHE B 142 ? 0.1383 0.1691 0.1546 -0.0272 0.0017  0.0056  142 PHE B CZ  
5293 N  N   . ASP B 143 ? 0.1087 0.1091 0.1259 0.0007  0.0018  -0.0049 143 ASP B N   
5294 C  CA  . ASP B 143 ? 0.1005 0.1070 0.1273 0.0064  0.0006  -0.0092 143 ASP B CA  
5295 C  C   . ASP B 143 ? 0.0987 0.1047 0.1178 0.0060  0.0098  -0.0119 143 ASP B C   
5296 O  O   . ASP B 143 ? 0.1059 0.1061 0.1277 -0.0008 0.0019  -0.0089 143 ASP B O   
5297 C  CB  . ASP B 143 ? 0.1017 0.1192 0.1310 0.0087  -0.0026 -0.0024 143 ASP B CB  
5298 C  CG  . ASP B 143 ? 0.1208 0.1149 0.1516 0.0051  -0.0186 -0.0030 143 ASP B CG  
5299 O  OD1 . ASP B 143 ? 0.1592 0.1342 0.1606 0.0160  -0.0340 -0.0174 143 ASP B OD1 
5300 O  OD2 . ASP B 143 ? 0.1522 0.1219 0.1722 0.0211  -0.0367 -0.0052 143 ASP B OD2 
5305 N  N   . PHE B 144 ? 0.0953 0.1146 0.1211 0.0045  -0.0022 -0.0061 144 PHE B N   
5306 C  CA  . PHE B 144 ? 0.0971 0.1163 0.1238 0.0060  -0.0048 0.0000  144 PHE B CA  
5307 C  C   . PHE B 144 ? 0.0988 0.1153 0.1180 0.0058  0.0020  -0.0080 144 PHE B C   
5308 O  O   . PHE B 144 ? 0.0972 0.1165 0.1431 -0.0028 0.0006  0.0019  144 PHE B O   
5309 C  CB  . PHE B 144 ? 0.1030 0.1262 0.1254 0.0030  -0.0011 -0.0099 144 PHE B CB  
5310 C  CG  . PHE B 144 ? 0.0969 0.1231 0.1273 0.0028  -0.0008 -0.0162 144 PHE B CG  
5311 C  CD1 . PHE B 144 ? 0.1250 0.1305 0.1460 -0.0028 0.0152  -0.0177 144 PHE B CD1 
5312 C  CD2 . PHE B 144 ? 0.1122 0.1360 0.1285 0.0141  0.0044  -0.0165 144 PHE B CD2 
5313 C  CE1 . PHE B 144 ? 0.1262 0.1510 0.1661 -0.0213 0.0307  -0.0308 144 PHE B CE1 
5314 C  CE2 . PHE B 144 ? 0.1106 0.1808 0.1387 0.0419  -0.0106 -0.0233 144 PHE B CE2 
5315 C  CZ  . PHE B 144 ? 0.1147 0.1968 0.1643 0.0024  0.0168  -0.0412 144 PHE B CZ  
5325 N  N   . LEU B 145 ? 0.0925 0.1131 0.1170 0.0008  0.0000  -0.0111 145 LEU B N   
5326 C  CA  . LEU B 145 ? 0.0940 0.1231 0.1218 0.0045  -0.0026 -0.0079 145 LEU B CA  
5327 C  C   . LEU B 145 ? 0.1017 0.1069 0.1231 0.0041  0.0000  -0.0089 145 LEU B C   
5328 O  O   . LEU B 145 ? 0.1328 0.1153 0.1244 -0.0020 -0.0040 -0.0024 145 LEU B O   
5329 C  CB  . LEU B 145 ? 0.0993 0.1250 0.1285 -0.0051 -0.0085 -0.0130 145 LEU B CB  
5330 C  CG  . LEU B 145 ? 0.1022 0.1355 0.1258 0.0015  0.0000  -0.0213 145 LEU B CG  
5331 C  CD1 . LEU B 145 ? 0.1319 0.1308 0.1415 0.0035  0.0205  -0.0176 145 LEU B CD1 
5332 C  CD2 . LEU B 145 ? 0.1403 0.1343 0.1334 0.0116  0.0083  -0.0024 145 LEU B CD2 
5344 N  N   . THR B 146 ? 0.1123 0.1103 0.1238 0.0035  0.0013  -0.0082 146 THR B N   
5345 C  CA  . THR B 146 ? 0.1063 0.1123 0.1217 -0.0064 0.0037  -0.0059 146 THR B CA  
5346 C  C   . THR B 146 ? 0.1235 0.1229 0.1222 -0.0045 -0.0031 -0.0113 146 THR B C   
5347 O  O   . THR B 146 ? 0.1117 0.1402 0.1474 -0.0051 -0.0045 0.0038  146 THR B O   
5348 C  CB  . THR B 146 ? 0.1191 0.1204 0.1239 -0.0053 0.0076  -0.0090 146 THR B CB  
5349 O  OG1 . THR B 146 ? 0.1325 0.1171 0.1303 0.0005  -0.0035 -0.0091 146 THR B OG1 
5350 C  CG2 . THR B 146 ? 0.1144 0.1493 0.1558 0.0058  0.0138  -0.0115 146 THR B CG2 
5358 N  N   . TRP B 147 ? 0.1125 0.1314 0.1283 -0.0024 -0.0042 -0.0081 147 TRP B N   
5359 C  CA  . TRP B 147 ? 0.1144 0.1266 0.1339 0.0029  -0.0134 -0.0118 147 TRP B CA  
5360 C  C   . TRP B 147 ? 0.1168 0.1306 0.1305 0.0092  -0.0119 -0.0104 147 TRP B C   
5361 O  O   . TRP B 147 ? 0.1332 0.1450 0.1358 -0.0044 -0.0171 -0.0012 147 TRP B O   
5362 C  CB  . TRP B 147 ? 0.1257 0.1351 0.1434 0.0135  -0.0111 -0.0047 147 TRP B CB  
5363 C  CG  . TRP B 147 ? 0.1357 0.1481 0.1555 0.0136  -0.0207 -0.0104 147 TRP B CG  
5364 C  CD1 . TRP B 147 ? 0.1607 0.1622 0.1777 0.0233  -0.0151 -0.0024 147 TRP B CD1 
5365 C  CD2 . TRP B 147 ? 0.1263 0.1568 0.1592 0.0216  -0.0244 -0.0169 147 TRP B CD2 
5366 N  NE1 . TRP B 147 ? 0.1597 0.1745 0.1804 0.0269  -0.0276 0.0025  147 TRP B NE1 
5367 C  CE2 . TRP B 147 ? 0.1446 0.1698 0.1813 0.0254  -0.0219 -0.0080 147 TRP B CE2 
5368 C  CE3 . TRP B 147 ? 0.1232 0.1974 0.1674 0.0260  -0.0148 -0.0089 147 TRP B CE3 
5369 C  CZ2 . TRP B 147 ? 0.1388 0.2183 0.1986 0.0319  -0.0332 -0.0205 147 TRP B CZ2 
5370 C  CZ3 . TRP B 147 ? 0.1225 0.2365 0.1939 0.0272  -0.0019 0.0043  147 TRP B CZ3 
5371 C  CH2 . TRP B 147 ? 0.1382 0.2213 0.2049 0.0325  -0.0056 -0.0119 147 TRP B CH2 
5382 N  N   . PHE B 148 ? 0.1127 0.1495 0.1301 0.0003  -0.0143 -0.0141 148 PHE B N   
5383 C  CA  . PHE B 148 ? 0.1208 0.1518 0.1279 0.0013  -0.0150 -0.0150 148 PHE B CA  
5384 C  C   . PHE B 148 ? 0.1305 0.1605 0.1424 0.0019  -0.0146 -0.0082 148 PHE B C   
5385 O  O   . PHE B 148 ? 0.1219 0.1787 0.1470 -0.0009 -0.0154 -0.0162 148 PHE B O   
5386 C  CB  . PHE B 148 ? 0.1253 0.1467 0.1299 -0.0019 -0.0127 -0.0130 148 PHE B CB  
5387 C  CG  . PHE B 148 ? 0.1331 0.1269 0.1321 0.0061  -0.0126 -0.0206 148 PHE B CG  
5388 C  CD1 . PHE B 148 ? 0.1317 0.1302 0.1314 0.0019  -0.0199 -0.0166 148 PHE B CD1 
5389 C  CD2 . PHE B 148 ? 0.1474 0.1311 0.1383 -0.0003 -0.0149 -0.0189 148 PHE B CD2 
5390 C  CE1 . PHE B 148 ? 0.1296 0.1430 0.1433 0.0167  -0.0166 -0.0233 148 PHE B CE1 
5391 C  CE2 . PHE B 148 ? 0.1611 0.1258 0.1375 0.0121  -0.0215 -0.0220 148 PHE B CE2 
5392 C  CZ  . PHE B 148 ? 0.1399 0.1355 0.1377 0.0157  -0.0240 -0.0261 148 PHE B CZ  
5402 N  N   . GLU B 149 ? 0.1278 0.1726 0.1425 0.0061  -0.0177 -0.0114 149 GLU B N   
5403 C  CA  . GLU B 149 ? 0.1231 0.1851 0.1582 0.0134  -0.0297 -0.0174 149 GLU B CA  
5404 C  C   . GLU B 149 ? 0.1214 0.1955 0.1528 0.0125  -0.0357 -0.0163 149 GLU B C   
5405 O  O   . GLU B 149 ? 0.1359 0.2011 0.1513 -0.0010 -0.0246 -0.0133 149 GLU B O   
5406 C  CB  . GLU B 149 ? 0.1486 0.1932 0.1799 0.0115  -0.0422 -0.0194 149 GLU B CB  
5407 C  CG  . GLU B 149 ? 0.1801 0.1924 0.1791 0.0322  -0.0502 -0.0145 149 GLU B CG  
5408 C  CD  . GLU B 149 ? 0.2041 0.2141 0.1866 0.0408  -0.0612 -0.0163 149 GLU B CD  
5409 O  OE1 . GLU B 149 ? 0.2697 0.2111 0.2037 0.0498  -0.0448 0.0006  149 GLU B OE1 
5410 O  OE2 . GLU B 149 ? 0.2234 0.2035 0.1928 0.0505  -0.0536 -0.0213 149 GLU B OE2 
5417 N  N   . TYR B 150 ? 0.1331 0.2058 0.1621 0.0060  -0.0322 -0.0262 150 TYR B N   
5418 C  CA  . TYR B 150 ? 0.1438 0.2094 0.1576 0.0004  -0.0343 -0.0309 150 TYR B CA  
5419 C  C   . TYR B 150 ? 0.1368 0.2446 0.1764 0.0056  -0.0379 -0.0383 150 TYR B C   
5420 O  O   . TYR B 150 ? 0.1369 0.2685 0.1678 0.0003  -0.0266 -0.0417 150 TYR B O   
5421 C  CB  . TYR B 150 ? 0.1548 0.2066 0.1736 0.0055  -0.0215 -0.0432 150 TYR B CB  
5422 C  CG  . TYR B 150 ? 0.1482 0.1947 0.1592 0.0019  -0.0196 -0.0369 150 TYR B CG  
5423 C  CD1 . TYR B 150 ? 0.1470 0.2247 0.1728 -0.0194 -0.0281 -0.0384 150 TYR B CD1 
5424 C  CD2 . TYR B 150 ? 0.1466 0.1881 0.1687 0.0021  -0.0292 -0.0350 150 TYR B CD2 
5425 C  CE1 . TYR B 150 ? 0.1617 0.2250 0.1755 -0.0201 -0.0241 -0.0258 150 TYR B CE1 
5426 C  CE2 . TYR B 150 ? 0.1622 0.2055 0.1687 -0.0048 -0.0312 -0.0260 150 TYR B CE2 
5427 C  CZ  . TYR B 150 ? 0.1634 0.2049 0.1591 -0.0046 -0.0254 -0.0283 150 TYR B CZ  
5428 O  OH  . TYR B 150 ? 0.1808 0.2350 0.1752 0.0107  -0.0249 -0.0254 150 TYR B OH  
5438 N  N   . SER B 151 ? 0.1492 0.2910 0.1848 -0.0132 -0.0448 -0.0610 151 SER B N   
5439 C  CA  . SER B 151 ? 0.1427 0.2903 0.1928 -0.0066 -0.0391 -0.0670 151 SER B CA  
5440 C  C   . SER B 151 ? 0.1516 0.3182 0.1902 -0.0160 -0.0421 -0.0573 151 SER B C   
5441 O  O   . SER B 151 ? 0.1571 0.2882 0.2090 -0.0182 -0.0460 -0.0651 151 SER B O   
5442 C  CB  . SER B 151 ? 0.1684 0.3332 0.2017 -0.0068 -0.0597 -0.0537 151 SER B CB  
5443 O  OG  . SER B 151 ? 0.2284 0.3659 0.2166 -0.0056 -0.0429 -0.0612 151 SER B OG  
5449 N  N   . PRO B 152 ? 0.1378 0.3268 0.2083 0.0008  -0.0346 -0.0624 152 PRO B N   
5450 C  CA  . PRO B 152 ? 0.1550 0.3506 0.2437 -0.0180 -0.0174 -0.0550 152 PRO B CA  
5451 C  C   . PRO B 152 ? 0.1639 0.3294 0.2339 -0.0390 -0.0264 -0.0525 152 PRO B C   
5452 O  O   . PRO B 152 ? 0.1840 0.3439 0.2726 -0.0491 -0.0215 -0.0450 152 PRO B O   
5453 C  CB  . PRO B 152 ? 0.1678 0.3655 0.2637 -0.0311 -0.0068 -0.0447 152 PRO B CB  
5454 C  CG  . PRO B 152 ? 0.1827 0.3785 0.2696 -0.0172 -0.0227 -0.0524 152 PRO B CG  
5455 C  CD  . PRO B 152 ? 0.1622 0.3414 0.2292 0.0014  -0.0291 -0.0624 152 PRO B CD  
5463 N  N   . SER B 153 ? 0.1682 0.3180 0.2297 -0.0325 -0.0332 -0.0635 153 SER B N   
5464 C  CA  . SER B 153 ? 0.1736 0.3162 0.2622 -0.0297 -0.0358 -0.0882 153 SER B CA  
5465 C  C   . SER B 153 ? 0.1729 0.2906 0.2465 -0.0299 -0.0403 -0.0909 153 SER B C   
5466 O  O   . SER B 153 ? 0.2038 0.2690 0.2544 -0.0267 -0.0427 -0.0782 153 SER B O   
5467 C  CB  . SER B 153 ? 0.2064 0.3810 0.2813 -0.0051 -0.0668 -0.0972 153 SER B CB  
5468 O  OG  . SER B 153 ? 0.2561 0.3869 0.2630 0.0400  -0.0512 -0.0432 153 SER B OG  
5474 N  N   . ASP B 154 ? 0.1715 0.2643 0.2307 -0.0319 -0.0360 -0.0644 154 ASP B N   
5475 C  CA  . ASP B 154 ? 0.1591 0.2321 0.2039 -0.0296 -0.0277 -0.0676 154 ASP B CA  
5476 C  C   . ASP B 154 ? 0.1579 0.2300 0.1927 -0.0409 -0.0059 -0.0691 154 ASP B C   
5477 O  O   . ASP B 154 ? 0.1510 0.2266 0.1865 -0.0259 -0.0083 -0.0445 154 ASP B O   
5478 C  CB  . ASP B 154 ? 0.1671 0.2209 0.2081 -0.0099 -0.0344 -0.0371 154 ASP B CB  
5479 C  CG  . ASP B 154 ? 0.1864 0.2361 0.1979 -0.0074 -0.0378 -0.0359 154 ASP B CG  
5480 O  OD1 . ASP B 154 ? 0.2367 0.2648 0.1929 0.0015  -0.0052 -0.0288 154 ASP B OD1 
5481 O  OD2 . ASP B 154 ? 0.2264 0.2482 0.1869 0.0009  -0.0444 -0.0204 154 ASP B OD2 
5486 N  N   . GLU B 155 ? 0.1674 0.2674 0.1903 -0.0384 -0.0158 -0.0658 155 GLU B N   
5487 C  CA  . GLU B 155 ? 0.1816 0.2418 0.1820 -0.0403 0.0072  -0.0724 155 GLU B CA  
5488 C  C   . GLU B 155 ? 0.1794 0.2287 0.1738 -0.0413 0.0002  -0.0708 155 GLU B C   
5489 O  O   . GLU B 155 ? 0.1803 0.2280 0.1724 -0.0424 0.0007  -0.0702 155 GLU B O   
5490 C  CB  . GLU B 155 ? 0.1911 0.2879 0.2321 -0.0239 0.0317  -0.0510 155 GLU B CB  
5491 C  CG  . GLU B 155 ? 0.2465 0.3131 0.2309 -0.0347 0.0529  -0.0692 155 GLU B CG  
5492 C  CD  . GLU B 155 ? 0.2509 0.3379 0.2447 -0.0964 0.0335  -0.1026 155 GLU B CD  
5493 O  OE1 . GLU B 155 ? 0.2495 0.4242 0.2689 -0.0929 0.0292  -0.1135 155 GLU B OE1 
5494 O  OE2 . GLU B 155 ? 0.2991 0.3887 0.2690 -0.1060 0.0466  -0.1356 155 GLU B OE2 
5501 N  N   . THR B 156 ? 0.1697 0.2425 0.1674 -0.0508 -0.0089 -0.0667 156 THR B N   
5502 C  CA  . THR B 156 ? 0.1918 0.2278 0.1694 -0.0563 -0.0104 -0.0723 156 THR B CA  
5503 C  C   . THR B 156 ? 0.1928 0.2185 0.1540 -0.0567 -0.0077 -0.0737 156 THR B C   
5504 O  O   . THR B 156 ? 0.2069 0.1952 0.1866 -0.0432 -0.0114 -0.0686 156 THR B O   
5505 C  CB  . THR B 156 ? 0.2289 0.2483 0.2093 -0.0701 -0.0159 -0.0679 156 THR B CB  
5506 O  OG1 . THR B 156 ? 0.2487 0.2790 0.2378 -0.0473 -0.0128 -0.0600 156 THR B OG1 
5507 C  CG2 . THR B 156 ? 0.2437 0.2793 0.2732 -0.1044 0.0141  -0.0872 156 THR B CG2 
5515 N  N   . ALA B 157 ? 0.1798 0.2106 0.1567 -0.0333 -0.0018 -0.0624 157 ALA B N   
5516 C  CA  . ALA B 157 ? 0.1682 0.2135 0.1659 -0.0351 -0.0041 -0.0503 157 ALA B CA  
5517 C  C   . ALA B 157 ? 0.1555 0.1743 0.1669 -0.0380 0.0021  -0.0490 157 ALA B C   
5518 O  O   . ALA B 157 ? 0.1700 0.1920 0.1641 -0.0176 0.0042  -0.0585 157 ALA B O   
5519 C  CB  . ALA B 157 ? 0.1842 0.2338 0.1699 -0.0263 0.0012  -0.0434 157 ALA B CB  
5525 N  N   . PHE B 158 ? 0.1502 0.1824 0.1626 -0.0147 -0.0100 -0.0528 158 PHE B N   
5526 C  CA  . PHE B 158 ? 0.1506 0.1618 0.1474 -0.0183 -0.0067 -0.0463 158 PHE B CA  
5527 C  C   . PHE B 158 ? 0.1650 0.1552 0.1512 -0.0241 0.0051  -0.0474 158 PHE B C   
5528 O  O   . PHE B 158 ? 0.1583 0.1497 0.1593 -0.0134 -0.0090 -0.0450 158 PHE B O   
5529 C  CB  . PHE B 158 ? 0.1505 0.1735 0.1522 -0.0173 -0.0024 -0.0438 158 PHE B CB  
5530 C  CG  . PHE B 158 ? 0.1328 0.1558 0.1486 -0.0078 -0.0020 -0.0343 158 PHE B CG  
5531 C  CD1 . PHE B 158 ? 0.1498 0.1377 0.1482 -0.0001 -0.0132 -0.0238 158 PHE B CD1 
5532 C  CD2 . PHE B 158 ? 0.1569 0.1460 0.1668 -0.0093 0.0024  -0.0354 158 PHE B CD2 
5533 C  CE1 . PHE B 158 ? 0.1500 0.1387 0.1540 -0.0064 -0.0090 -0.0231 158 PHE B CE1 
5534 C  CE2 . PHE B 158 ? 0.1634 0.1544 0.1571 -0.0002 0.0055  -0.0291 158 PHE B CE2 
5535 C  CZ  . PHE B 158 ? 0.1622 0.1458 0.1411 0.0001  -0.0197 -0.0288 158 PHE B CZ  
5545 N  N   . ASN B 159 ? 0.1619 0.1588 0.1569 -0.0295 0.0063  -0.0467 159 ASN B N   
5546 C  CA  . ASN B 159 ? 0.1821 0.1579 0.1679 -0.0248 0.0102  -0.0474 159 ASN B CA  
5547 C  C   . ASN B 159 ? 0.1803 0.1375 0.1723 -0.0322 0.0060  -0.0529 159 ASN B C   
5548 O  O   . ASN B 159 ? 0.1943 0.1544 0.1673 -0.0318 0.0195  -0.0412 159 ASN B O   
5549 C  CB  . ASN B 159 ? 0.1876 0.1657 0.1945 -0.0326 0.0188  -0.0406 159 ASN B CB  
5550 C  CG  . ASN B 159 ? 0.1869 0.1708 0.1970 -0.0304 0.0116  -0.0477 159 ASN B CG  
5551 O  OD1 . ASN B 159 ? 0.1992 0.1960 0.1935 -0.0134 0.0195  -0.0644 159 ASN B OD1 
5552 N  ND2 . ASN B 159 ? 0.1865 0.2001 0.2794 -0.0439 0.0258  -0.0679 159 ASN B ND2 
5559 N  N   . ARG B 160 ? 0.1713 0.1591 0.1742 -0.0282 0.0104  -0.0582 160 ARG B N   
5560 C  CA  . ARG B 160 ? 0.1808 0.1628 0.1748 -0.0194 0.0103  -0.0501 160 ARG B CA  
5561 C  C   . ARG B 160 ? 0.1682 0.1519 0.1672 -0.0099 0.0107  -0.0500 160 ARG B C   
5562 O  O   . ARG B 160 ? 0.1859 0.1525 0.1769 -0.0062 0.0090  -0.0477 160 ARG B O   
5563 C  CB  . ARG B 160 ? 0.1917 0.1819 0.1734 -0.0206 0.0158  -0.0724 160 ARG B CB  
5564 C  CG  . ARG B 160 ? 0.1881 0.2166 0.1944 -0.0184 0.0192  -0.0708 160 ARG B CG  
5565 C  CD  . ARG B 160 ? 0.2471 0.2667 0.2113 0.0595  -0.0319 -0.0753 160 ARG B CD  
5566 N  NE  . ARG B 160 ? 0.2620 0.3454 0.2568 0.0800  -0.0591 -0.1289 160 ARG B NE  
5567 C  CZ  . ARG B 160 ? 0.2353 0.3354 0.2457 0.0687  -0.0559 -0.1341 160 ARG B CZ  
5568 N  NH1 . ARG B 160 ? 0.2333 0.3277 0.2489 0.0437  -0.0518 -0.1453 160 ARG B NH1 
5569 N  NH2 . ARG B 160 ? 0.2525 0.4019 0.3398 0.1027  -0.0701 -0.1452 160 ARG B NH2 
5583 N  N   . LEU B 161 ? 0.1563 0.1527 0.1534 -0.0194 0.0065  -0.0351 161 LEU B N   
5584 C  CA  . LEU B 161 ? 0.1489 0.1602 0.1578 -0.0125 0.0125  -0.0383 161 LEU B CA  
5585 C  C   . LEU B 161 ? 0.1532 0.1344 0.1560 -0.0136 0.0064  -0.0235 161 LEU B C   
5586 O  O   . LEU B 161 ? 0.1533 0.1423 0.1558 -0.0053 0.0012  -0.0249 161 LEU B O   
5587 C  CB  . LEU B 161 ? 0.1685 0.1485 0.1542 -0.0106 -0.0030 -0.0325 161 LEU B CB  
5588 C  CG  . LEU B 161 ? 0.1701 0.1524 0.1524 -0.0204 -0.0160 -0.0261 161 LEU B CG  
5589 C  CD1 . LEU B 161 ? 0.1735 0.1810 0.1647 -0.0380 -0.0161 -0.0127 161 LEU B CD1 
5590 C  CD2 . LEU B 161 ? 0.1977 0.1555 0.1816 -0.0233 -0.0419 -0.0294 161 LEU B CD2 
5602 N  N   . LEU B 162 ? 0.1506 0.1378 0.1543 -0.0083 0.0133  -0.0286 162 LEU B N   
5603 C  CA  . LEU B 162 ? 0.1528 0.1436 0.1516 -0.0011 0.0051  -0.0331 162 LEU B CA  
5604 C  C   . LEU B 162 ? 0.1569 0.1407 0.1691 -0.0018 0.0227  -0.0247 162 LEU B C   
5605 O  O   . LEU B 162 ? 0.1627 0.1530 0.1785 0.0080  0.0084  -0.0099 162 LEU B O   
5606 C  CB  . LEU B 162 ? 0.1458 0.1412 0.1618 -0.0013 0.0028  -0.0280 162 LEU B CB  
5607 C  CG  . LEU B 162 ? 0.1654 0.1394 0.1504 0.0002  0.0097  -0.0219 162 LEU B CG  
5608 C  CD1 . LEU B 162 ? 0.1648 0.1683 0.1551 -0.0109 0.0211  -0.0253 162 LEU B CD1 
5609 C  CD2 . LEU B 162 ? 0.1821 0.1373 0.1829 -0.0118 0.0240  -0.0366 162 LEU B CD2 
5621 N  N   . ALA B 163 ? 0.1621 0.1369 0.1929 0.0032  0.0169  -0.0259 163 ALA B N   
5622 C  CA  . ALA B 163 ? 0.1900 0.1398 0.2089 0.0147  0.0299  -0.0216 163 ALA B CA  
5623 C  C   . ALA B 163 ? 0.1934 0.1406 0.2178 0.0244  0.0297  -0.0237 163 ALA B C   
5624 O  O   . ALA B 163 ? 0.2093 0.1457 0.2322 0.0239  0.0342  -0.0014 163 ALA B O   
5625 C  CB  . ALA B 163 ? 0.2029 0.1339 0.2792 -0.0147 0.0291  -0.0211 163 ALA B CB  
5631 N  N   . GLU B 164 ? 0.1985 0.1404 0.2078 0.0155  0.0339  -0.0372 164 GLU B N   
5632 C  CA  . GLU B 164 ? 0.1913 0.1465 0.2004 0.0303  0.0275  -0.0332 164 GLU B CA  
5633 C  C   . GLU B 164 ? 0.1650 0.1409 0.1822 0.0210  0.0311  -0.0177 164 GLU B C   
5634 O  O   . GLU B 164 ? 0.1642 0.1516 0.2114 0.0260  0.0324  -0.0198 164 GLU B O   
5635 C  CB  . GLU B 164 ? 0.2047 0.1907 0.1967 0.0368  0.0331  -0.0347 164 GLU B CB  
5636 C  CG  . GLU B 164 ? 0.2795 0.2328 0.2241 0.0422  0.0215  -0.0543 164 GLU B CG  
5637 C  CD  . GLU B 164 ? 0.2931 0.2739 0.2342 0.0446  0.0273  -0.0441 164 GLU B CD  
5638 O  OE1 . GLU B 164 ? 0.3047 0.3378 0.2666 0.0310  0.0224  -0.0552 164 GLU B OE1 
5639 O  OE2 . GLU B 164 ? 0.3312 0.2993 0.3408 0.0565  0.0181  0.0106  164 GLU B OE2 
5646 N  N   . LEU B 165 ? 0.1636 0.1280 0.1823 0.0186  0.0147  -0.0095 165 LEU B N   
5647 C  CA  . LEU B 165 ? 0.1460 0.1317 0.1802 0.0132  0.0221  -0.0119 165 LEU B CA  
5648 C  C   . LEU B 165 ? 0.1535 0.1207 0.1909 0.0219  0.0159  -0.0130 165 LEU B C   
5649 O  O   . LEU B 165 ? 0.1552 0.1294 0.1803 0.0145  0.0186  -0.0057 165 LEU B O   
5650 C  CB  . LEU B 165 ? 0.1574 0.1262 0.1815 0.0123  0.0042  -0.0104 165 LEU B CB  
5651 C  CG  . LEU B 165 ? 0.1785 0.1297 0.1884 0.0306  -0.0021 -0.0071 165 LEU B CG  
5652 C  CD1 . LEU B 165 ? 0.2053 0.1274 0.1885 0.0396  -0.0152 -0.0182 165 LEU B CD1 
5653 C  CD2 . LEU B 165 ? 0.1949 0.1491 0.1931 0.0231  0.0170  0.0160  165 LEU B CD2 
5665 N  N   . ARG B 166 ? 0.1672 0.1125 0.1773 0.0171  0.0229  -0.0082 166 ARG B N   
5666 C  CA  . ARG B 166 ? 0.1589 0.1517 0.1781 0.0238  0.0221  0.0050  166 ARG B CA  
5667 C  C   . ARG B 166 ? 0.1726 0.1339 0.2132 0.0102  0.0357  0.0218  166 ARG B C   
5668 O  O   . ARG B 166 ? 0.1644 0.1592 0.2330 0.0236  0.0248  0.0288  166 ARG B O   
5669 C  CB  . ARG B 166 ? 0.1606 0.1484 0.1989 0.0173  0.0176  0.0050  166 ARG B CB  
5670 C  CG  . ARG B 166 ? 0.1597 0.1471 0.1920 0.0120  0.0222  0.0060  166 ARG B CG  
5671 C  CD  . ARG B 166 ? 0.1587 0.1544 0.1922 0.0095  0.0311  0.0000  166 ARG B CD  
5672 N  NE  . ARG B 166 ? 0.1600 0.1488 0.1770 0.0145  0.0269  -0.0005 166 ARG B NE  
5673 C  CZ  . ARG B 166 ? 0.1510 0.1692 0.1557 0.0054  0.0120  -0.0124 166 ARG B CZ  
5674 N  NH1 . ARG B 166 ? 0.1698 0.1623 0.1839 0.0076  0.0072  -0.0082 166 ARG B NH1 
5675 N  NH2 . ARG B 166 ? 0.1461 0.1652 0.1753 0.0056  0.0131  -0.0107 166 ARG B NH2 
5689 N  N   . ALA B 167 ? 0.1937 0.1201 0.2457 0.0152  0.0440  -0.0044 167 ALA B N   
5690 C  CA  . ALA B 167 ? 0.1983 0.1255 0.2815 0.0201  0.0514  -0.0078 167 ALA B CA  
5691 C  C   . ALA B 167 ? 0.1936 0.1209 0.3034 0.0242  0.0708  -0.0094 167 ALA B C   
5692 O  O   . ALA B 167 ? 0.2022 0.1118 0.4209 0.0379  0.0850  0.0041  167 ALA B O   
5693 C  CB  . ALA B 167 ? 0.2400 0.1375 0.2809 0.0277  0.0666  -0.0128 167 ALA B CB  
5699 N  N   . SER B 168 ? 0.1909 0.1153 0.2743 0.0286  0.0608  -0.0098 168 SER B N   
5700 C  CA  . SER B 168 ? 0.1862 0.1346 0.2446 0.0294  0.0622  -0.0154 168 SER B CA  
5701 C  C   . SER B 168 ? 0.1937 0.1200 0.2220 0.0339  0.0636  0.0000  168 SER B C   
5702 O  O   . SER B 168 ? 0.2190 0.1120 0.2460 0.0317  0.0883  0.0076  168 SER B O   
5703 C  CB  . SER B 168 ? 0.1795 0.1300 0.2527 0.0200  0.0486  -0.0108 168 SER B CB  
5704 O  OG  . SER B 168 ? 0.1711 0.1198 0.2590 0.0108  0.0531  -0.0109 168 SER B OG  
5710 N  N   . VAL B 169 ? 0.1785 0.1582 0.2169 0.0537  0.0521  0.0211  169 VAL B N   
5711 C  CA  . VAL B 169 ? 0.1703 0.2159 0.2091 0.0981  0.0319  0.0282  169 VAL B CA  
5712 C  C   . VAL B 169 ? 0.1545 0.2289 0.1757 0.0659  0.0306  0.0300  169 VAL B C   
5713 O  O   . VAL B 169 ? 0.1439 0.2947 0.1747 0.0817  0.0217  0.0481  169 VAL B O   
5714 C  CB  . VAL B 169 ? 0.1624 0.2721 0.2503 0.0857  0.0069  0.0161  169 VAL B CB  
5715 C  CG1 . VAL B 169 ? 0.1803 0.2448 0.2609 0.0604  0.0221  -0.0151 169 VAL B CG1 
5716 C  CG2 . VAL B 169 ? 0.2302 0.2499 0.2780 0.0674  0.0261  0.0218  169 VAL B CG2 
5726 N  N   . GLU B 170 ? 0.1414 0.2010 0.1479 0.0503  0.0108  0.0127  170 GLU B N   
5727 C  CA  . GLU B 170 ? 0.1344 0.2087 0.1449 0.0211  0.0106  -0.0093 170 GLU B CA  
5728 C  C   . GLU B 170 ? 0.1222 0.1808 0.1523 0.0368  0.0044  0.0034  170 GLU B C   
5729 O  O   . GLU B 170 ? 0.1415 0.1593 0.1458 0.0367  0.0023  0.0012  170 GLU B O   
5730 C  CB  . GLU B 170 ? 0.1581 0.1541 0.1590 -0.0043 0.0279  -0.0218 170 GLU B CB  
5731 C  CG  . GLU B 170 ? 0.2892 0.2037 0.1930 -0.0286 0.0598  -0.0414 170 GLU B CG  
5732 C  CD  . GLU B 170 ? 0.2398 0.2415 0.2444 0.0417  0.0663  -0.0597 170 GLU B CD  
5733 O  OE1 . GLU B 170 ? 0.2028 0.1382 0.3202 0.0507  0.0198  0.0137  170 GLU B OE1 
5734 O  OE2 . GLU B 170 ? 0.2604 0.2150 0.2534 0.0424  0.0164  -0.0609 170 GLU B OE2 
5741 N  N   . TRP B 171 ? 0.1218 0.1695 0.1522 0.0281  0.0049  0.0036  171 TRP B N   
5742 C  CA  . TRP B 171 ? 0.1262 0.1827 0.1554 0.0408  0.0023  0.0088  171 TRP B CA  
5743 C  C   . TRP B 171 ? 0.1328 0.1438 0.1473 0.0413  0.0048  0.0039  171 TRP B C   
5744 O  O   . TRP B 171 ? 0.1372 0.1439 0.1507 0.0332  0.0017  0.0070  171 TRP B O   
5745 C  CB  . TRP B 171 ? 0.1288 0.1981 0.1463 0.0352  -0.0071 0.0008  171 TRP B CB  
5746 C  CG  . TRP B 171 ? 0.1207 0.2271 0.1405 0.0415  -0.0059 -0.0117 171 TRP B CG  
5747 C  CD1 . TRP B 171 ? 0.1358 0.2587 0.1511 0.0423  -0.0044 -0.0159 171 TRP B CD1 
5748 C  CD2 . TRP B 171 ? 0.1321 0.2216 0.1367 0.0606  -0.0149 -0.0203 171 TRP B CD2 
5749 N  NE1 . TRP B 171 ? 0.1392 0.2590 0.1707 0.0457  -0.0069 -0.0264 171 TRP B NE1 
5750 C  CE2 . TRP B 171 ? 0.1368 0.2335 0.1512 0.0679  -0.0166 -0.0223 171 TRP B CE2 
5751 C  CE3 . TRP B 171 ? 0.1577 0.1955 0.1483 0.0592  -0.0104 -0.0174 171 TRP B CE3 
5752 C  CZ2 . TRP B 171 ? 0.1585 0.2407 0.1484 0.0711  -0.0258 -0.0356 171 TRP B CZ2 
5753 C  CZ3 . TRP B 171 ? 0.1881 0.2021 0.1471 0.0576  -0.0195 -0.0103 171 TRP B CZ3 
5754 C  CH2 . TRP B 171 ? 0.1857 0.1920 0.1575 0.0780  -0.0264 -0.0294 171 TRP B CH2 
5765 N  N   . GLN B 172 ? 0.1317 0.1357 0.1579 0.0439  -0.0033 -0.0082 172 GLN B N   
5766 C  CA  . GLN B 172 ? 0.1419 0.1243 0.1570 0.0368  -0.0085 -0.0052 172 GLN B CA  
5767 C  C   . GLN B 172 ? 0.1353 0.1148 0.1555 0.0357  -0.0026 -0.0006 172 GLN B C   
5768 O  O   . GLN B 172 ? 0.1756 0.1247 0.1610 0.0399  -0.0025 0.0035  172 GLN B O   
5769 C  CB  . GLN B 172 ? 0.1318 0.1220 0.1659 0.0381  -0.0116 -0.0093 172 GLN B CB  
5770 C  CG  . GLN B 172 ? 0.1353 0.1273 0.1942 0.0304  -0.0085 -0.0233 172 GLN B CG  
5771 C  CD  . GLN B 172 ? 0.1389 0.1077 0.1971 0.0249  -0.0093 -0.0195 172 GLN B CD  
5772 O  OE1 . GLN B 172 ? 0.1443 0.1226 0.1963 0.0404  -0.0168 -0.0179 172 GLN B OE1 
5773 N  NE2 . GLN B 172 ? 0.1624 0.1439 0.2073 0.0354  -0.0022 -0.0423 172 GLN B NE2 
5782 N  N   . TYR B 173 ? 0.1464 0.1121 0.1531 0.0407  0.0018  0.0031  173 TYR B N   
5783 C  CA  . TYR B 173 ? 0.1538 0.1176 0.1557 0.0386  0.0038  0.0112  173 TYR B CA  
5784 C  C   . TYR B 173 ? 0.1666 0.1275 0.1476 0.0507  0.0082  0.0070  173 TYR B C   
5785 O  O   . TYR B 173 ? 0.1828 0.1431 0.2137 0.0498  0.0191  -0.0251 173 TYR B O   
5786 C  CB  . TYR B 173 ? 0.1774 0.1101 0.1753 0.0297  0.0137  0.0185  173 TYR B CB  
5787 C  CG  . TYR B 173 ? 0.1522 0.1122 0.1851 0.0143  0.0018  0.0377  173 TYR B CG  
5788 C  CD1 . TYR B 173 ? 0.1477 0.1215 0.1967 0.0419  0.0178  0.0228  173 TYR B CD1 
5789 C  CD2 . TYR B 173 ? 0.1726 0.1122 0.2021 0.0071  0.0073  0.0398  173 TYR B CD2 
5790 C  CE1 . TYR B 173 ? 0.1518 0.1557 0.2028 0.0352  0.0105  0.0521  173 TYR B CE1 
5791 C  CE2 . TYR B 173 ? 0.1381 0.1232 0.2145 0.0117  -0.0030 0.0559  173 TYR B CE2 
5792 C  CZ  . TYR B 173 ? 0.1567 0.1497 0.2050 0.0264  0.0145  0.0686  173 TYR B CZ  
5793 O  OH  . TYR B 173 ? 0.1461 0.1737 0.2569 0.0413  0.0168  0.0752  173 TYR B OH  
5803 N  N   . VAL B 174 ? 0.1604 0.1530 0.1445 0.0608  0.0101  0.0000  174 VAL B N   
5804 C  CA  . VAL B 174 ? 0.1599 0.1783 0.1448 0.0752  -0.0019 -0.0002 174 VAL B CA  
5805 C  C   . VAL B 174 ? 0.1686 0.1552 0.1624 0.0663  0.0122  -0.0019 174 VAL B C   
5806 O  O   . VAL B 174 ? 0.1983 0.1612 0.1737 0.0397  0.0127  0.0001  174 VAL B O   
5807 C  CB  . VAL B 174 ? 0.1650 0.2022 0.1630 0.0854  0.0028  -0.0102 174 VAL B CB  
5808 C  CG1 . VAL B 174 ? 0.1737 0.2325 0.1768 0.0930  -0.0069 -0.0291 174 VAL B CG1 
5809 C  CG2 . VAL B 174 ? 0.2048 0.2296 0.1370 0.0890  -0.0015 0.0063  174 VAL B CG2 
5819 N  N   . ASP B 175 ? 0.1607 0.1474 0.1389 0.0448  -0.0031 0.0066  175 ASP B N   
5820 C  CA  A ASP B 175 ? 0.1633 0.1674 0.1558 0.0398  0.0053  0.0183  175 ASP B CA  
5821 C  CA  B ASP B 175 ? 0.1643 0.1657 0.1523 0.0418  0.0028  0.0161  175 ASP B CA  
5822 C  C   . ASP B 175 ? 0.1674 0.1854 0.1461 0.0436  0.0052  0.0275  175 ASP B C   
5823 O  O   . ASP B 175 ? 0.1929 0.2269 0.1888 0.0599  0.0281  0.0657  175 ASP B O   
5824 C  CB  A ASP B 175 ? 0.1809 0.1900 0.1676 0.0186  0.0007  0.0223  175 ASP B CB  
5825 C  CB  B ASP B 175 ? 0.1728 0.1648 0.1562 0.0392  -0.0090 0.0289  175 ASP B CB  
5826 C  CG  A ASP B 175 ? 0.1814 0.1835 0.1789 0.0171  -0.0080 0.0466  175 ASP B CG  
5827 C  CG  B ASP B 175 ? 0.1617 0.1860 0.1620 0.0224  -0.0084 0.0132  175 ASP B CG  
5828 O  OD1 A ASP B 175 ? 0.1671 0.1893 0.2408 0.0495  0.0095  0.0393  175 ASP B OD1 
5829 O  OD1 B ASP B 175 ? 0.2030 0.1870 0.1878 0.0249  -0.0511 -0.0075 175 ASP B OD1 
5830 O  OD2 A ASP B 175 ? 0.1694 0.2559 0.2169 -0.0145 -0.0369 0.0803  175 ASP B OD2 
5831 O  OD2 B ASP B 175 ? 0.1879 0.2228 0.1597 0.0230  -0.0113 0.0154  175 ASP B OD2 
5840 N  N   . ARG B 176 ? 0.1434 0.1603 0.1506 0.0413  0.0008  0.0097  176 ARG B N   
5841 C  CA  . ARG B 176 ? 0.1433 0.1612 0.1491 0.0326  0.0000  0.0054  176 ARG B CA  
5842 C  C   . ARG B 176 ? 0.1538 0.1275 0.1444 0.0173  0.0058  0.0087  176 ARG B C   
5843 O  O   . ARG B 176 ? 0.1474 0.1222 0.1603 0.0183  -0.0071 0.0067  176 ARG B O   
5844 C  CB  . ARG B 176 ? 0.1619 0.1947 0.1751 0.0387  0.0060  -0.0068 176 ARG B CB  
5845 C  CG  . ARG B 176 ? 0.1889 0.1758 0.1812 0.0113  0.0218  0.0110  176 ARG B CG  
5846 C  CD  . ARG B 176 ? 0.1672 0.1996 0.1811 0.0311  0.0348  0.0018  176 ARG B CD  
5847 N  NE  . ARG B 176 ? 0.1859 0.2076 0.1926 0.0240  0.0367  0.0247  176 ARG B NE  
5848 C  CZ  . ARG B 176 ? 0.1876 0.1885 0.1821 0.0342  0.0511  0.0163  176 ARG B CZ  
5849 N  NH1 . ARG B 176 ? 0.2675 0.2055 0.1939 0.0368  0.0454  0.0067  176 ARG B NH1 
5850 N  NH2 . ARG B 176 ? 0.2184 0.2530 0.2298 0.0337  0.0616  0.0280  176 ARG B NH2 
5864 N  N   . GLU B 177 ? 0.1485 0.1309 0.1568 0.0111  0.0065  0.0087  177 GLU B N   
5865 C  CA  . GLU B 177 ? 0.1331 0.1172 0.1568 0.0088  0.0073  0.0115  177 GLU B CA  
5866 C  C   . GLU B 177 ? 0.1287 0.1225 0.1569 0.0015  0.0219  0.0147  177 GLU B C   
5867 O  O   . GLU B 177 ? 0.1459 0.1220 0.1888 -0.0067 0.0237  0.0132  177 GLU B O   
5868 C  CB  . GLU B 177 ? 0.1369 0.1303 0.1619 0.0088  0.0122  0.0075  177 GLU B CB  
5869 C  CG  . GLU B 177 ? 0.1257 0.1282 0.1562 0.0082  0.0077  0.0038  177 GLU B CG  
5870 C  CD  . GLU B 177 ? 0.1293 0.1565 0.1622 0.0033  0.0063  0.0071  177 GLU B CD  
5871 O  OE1 . GLU B 177 ? 0.1514 0.1997 0.1953 0.0459  0.0179  -0.0020 177 GLU B OE1 
5872 O  OE2 . GLU B 177 ? 0.1549 0.1693 0.1665 0.0241  0.0029  -0.0101 177 GLU B OE2 
5879 N  N   . ILE B 178 ? 0.1309 0.1123 0.1443 0.0009  0.0150  0.0075  178 ILE B N   
5880 C  CA  . ILE B 178 ? 0.1267 0.1311 0.1407 -0.0052 0.0125  0.0014  178 ILE B CA  
5881 C  C   . ILE B 178 ? 0.1246 0.1204 0.1516 -0.0044 0.0138  -0.0069 178 ILE B C   
5882 O  O   . ILE B 178 ? 0.1677 0.1273 0.1492 -0.0212 -0.0068 0.0074  178 ILE B O   
5883 C  CB  . ILE B 178 ? 0.1410 0.1400 0.1496 0.0051  0.0209  0.0012  178 ILE B CB  
5884 C  CG1 . ILE B 178 ? 0.1771 0.1596 0.1526 -0.0109 0.0169  -0.0114 178 ILE B CG1 
5885 C  CG2 . ILE B 178 ? 0.1424 0.1959 0.1539 0.0110  0.0164  0.0042  178 ILE B CG2 
5886 C  CD1 . ILE B 178 ? 0.1868 0.1739 0.1518 0.0046  0.0061  0.0011  178 ILE B CD1 
5898 N  N   . ASP B 179 ? 0.1344 0.1306 0.1469 -0.0131 0.0140  -0.0001 179 ASP B N   
5899 C  CA  . ASP B 179 ? 0.1307 0.1430 0.1544 -0.0052 0.0088  -0.0120 179 ASP B CA  
5900 C  C   . ASP B 179 ? 0.1288 0.1377 0.1462 -0.0084 0.0167  -0.0094 179 ASP B C   
5901 O  O   . ASP B 179 ? 0.1411 0.1361 0.1916 -0.0205 0.0212  -0.0131 179 ASP B O   
5902 C  CB  . ASP B 179 ? 0.1359 0.1506 0.1760 -0.0010 0.0136  -0.0212 179 ASP B CB  
5903 C  CG  . ASP B 179 ? 0.1352 0.1714 0.1794 -0.0075 0.0100  -0.0382 179 ASP B CG  
5904 O  OD1 . ASP B 179 ? 0.1730 0.1824 0.1694 0.0056  -0.0120 -0.0392 179 ASP B OD1 
5905 O  OD2 . ASP B 179 ? 0.1588 0.1799 0.1854 0.0028  0.0091  -0.0342 179 ASP B OD2 
5910 N  N   . ILE B 180 ? 0.1201 0.1388 0.1513 -0.0172 0.0173  -0.0180 180 ILE B N   
5911 C  CA  . ILE B 180 ? 0.1216 0.1535 0.1622 -0.0134 0.0098  -0.0230 180 ILE B CA  
5912 C  C   . ILE B 180 ? 0.1249 0.1413 0.1637 -0.0107 0.0088  -0.0183 180 ILE B C   
5913 O  O   . ILE B 180 ? 0.1324 0.1669 0.1557 -0.0210 -0.0050 -0.0259 180 ILE B O   
5914 C  CB  . ILE B 180 ? 0.1374 0.1410 0.1621 0.0000  0.0052  -0.0165 180 ILE B CB  
5915 C  CG1 . ILE B 180 ? 0.1740 0.1457 0.1585 -0.0037 0.0003  -0.0197 180 ILE B CG1 
5916 C  CG2 . ILE B 180 ? 0.1458 0.1892 0.1913 0.0102  0.0135  -0.0335 180 ILE B CG2 
5917 C  CD1 . ILE B 180 ? 0.2233 0.1622 0.1679 0.0026  -0.0085 -0.0293 180 ILE B CD1 
5929 N  N   . ARG B 181 ? 0.1221 0.1570 0.1634 -0.0158 -0.0040 -0.0245 181 ARG B N   
5930 C  CA  . ARG B 181 ? 0.1249 0.1830 0.1597 -0.0112 -0.0016 -0.0376 181 ARG B CA  
5931 C  C   . ARG B 181 ? 0.1297 0.1831 0.1652 -0.0137 -0.0031 -0.0435 181 ARG B C   
5932 O  O   . ARG B 181 ? 0.1287 0.1893 0.1794 -0.0138 0.0070  -0.0337 181 ARG B O   
5933 C  CB  . ARG B 181 ? 0.1438 0.1641 0.1811 -0.0245 0.0170  -0.0446 181 ARG B CB  
5934 C  CG  . ARG B 181 ? 0.1432 0.1767 0.1840 -0.0174 0.0132  -0.0453 181 ARG B CG  
5935 C  CD  . ARG B 181 ? 0.1357 0.1599 0.1924 -0.0043 0.0145  -0.0416 181 ARG B CD  
5936 N  NE  . ARG B 181 ? 0.1378 0.1688 0.1700 -0.0119 0.0035  -0.0333 181 ARG B NE  
5937 C  CZ  . ARG B 181 ? 0.1411 0.1613 0.1777 -0.0157 0.0100  -0.0366 181 ARG B CZ  
5938 N  NH1 . ARG B 181 ? 0.1457 0.1933 0.1853 -0.0162 0.0035  -0.0556 181 ARG B NH1 
5939 N  NH2 . ARG B 181 ? 0.1490 0.1856 0.1841 -0.0046 0.0067  -0.0455 181 ARG B NH2 
5953 N  N   . LEU B 182 ? 0.1126 0.1982 0.1578 -0.0048 -0.0033 -0.0338 182 LEU B N   
5954 C  CA  . LEU B 182 ? 0.1156 0.2087 0.1777 -0.0021 -0.0035 -0.0322 182 LEU B CA  
5955 C  C   . LEU B 182 ? 0.1088 0.2100 0.1828 -0.0098 -0.0081 -0.0478 182 LEU B C   
5956 O  O   . LEU B 182 ? 0.1130 0.2378 0.1808 -0.0002 -0.0118 -0.0534 182 LEU B O   
5957 C  CB  . LEU B 182 ? 0.1160 0.2196 0.1799 -0.0022 -0.0095 -0.0262 182 LEU B CB  
5958 C  CG  . LEU B 182 ? 0.1374 0.2231 0.1891 -0.0190 -0.0122 -0.0436 182 LEU B CG  
5959 C  CD1 . LEU B 182 ? 0.1346 0.2125 0.1817 -0.0065 -0.0165 -0.0347 182 LEU B CD1 
5960 C  CD2 . LEU B 182 ? 0.1509 0.2627 0.2161 0.0103  -0.0184 -0.0365 182 LEU B CD2 
5972 N  N   . VAL B 183 ? 0.1067 0.2405 0.1849 0.0128  -0.0106 -0.0467 183 VAL B N   
5973 C  CA  . VAL B 183 ? 0.1149 0.2962 0.2109 0.0110  -0.0258 -0.0507 183 VAL B CA  
5974 C  C   . VAL B 183 ? 0.1326 0.2789 0.1917 0.0225  -0.0450 -0.0507 183 VAL B C   
5975 O  O   . VAL B 183 ? 0.1459 0.3103 0.2111 0.0364  -0.0316 -0.0585 183 VAL B O   
5976 C  CB  . VAL B 183 ? 0.1692 0.3170 0.2273 -0.0070 -0.0372 -0.0739 183 VAL B CB  
5977 C  CG1 . VAL B 183 ? 0.2148 0.3686 0.3000 -0.0048 -0.0821 -0.0672 183 VAL B CG1 
5978 C  CG2 . VAL B 183 ? 0.1865 0.2963 0.2742 -0.0415 -0.0274 -0.0628 183 VAL B CG2 
5988 N  N   . HIS B 184 ? 0.1648 0.3121 0.2152 0.0525  -0.0484 -0.0403 184 HIS B N   
5989 C  CA  . HIS B 184 ? 0.1780 0.3365 0.2469 0.0747  -0.0381 -0.0455 184 HIS B CA  
5990 C  C   . HIS B 184 ? 0.1912 0.3919 0.2652 0.0656  -0.0616 -0.0473 184 HIS B C   
5991 O  O   . HIS B 184 ? 0.1916 0.3975 0.3206 0.0435  -0.0616 -0.0475 184 HIS B O   
5992 C  CB  . HIS B 184 ? 0.2154 0.3559 0.2635 0.0657  -0.0528 -0.0109 184 HIS B CB  
5993 C  CG  . HIS B 184 ? 0.2362 0.3293 0.3116 0.0604  -0.0584 0.0076  184 HIS B CG  
5994 N  ND1 . HIS B 184 ? 0.2367 0.3502 0.3863 0.0516  -0.0442 0.0224  184 HIS B ND1 
5995 C  CD2 . HIS B 184 ? 0.2555 0.3391 0.3779 0.0497  -0.0313 0.0223  184 HIS B CD2 
5996 C  CE1 . HIS B 184 ? 0.2672 0.3326 0.3932 0.0550  -0.0280 0.0186  184 HIS B CE1 
5997 N  NE2 . HIS B 184 ? 0.2816 0.3200 0.3811 0.0358  -0.0158 0.0116  184 HIS B NE2 
6005 N  N   . GLU B 185 ? 0.1839 0.4193 0.2933 0.1017  -0.0720 -0.0451 185 GLU B N   
6006 C  CA  . GLU B 185 ? 0.1930 0.4470 0.3919 0.1020  -0.0809 -0.0016 185 GLU B CA  
6007 C  C   . GLU B 185 ? 0.2049 0.5063 0.4148 0.0467  -0.0807 0.0353  185 GLU B C   
6008 O  O   . GLU B 185 ? 0.2219 0.4394 0.3836 0.0941  -0.0563 0.0293  185 GLU B O   
6009 C  CB  . GLU B 185 ? 0.2267 0.4842 0.4402 0.1123  -0.0327 -0.0141 185 GLU B CB  
6010 C  CG  . GLU B 185 ? 0.3462 0.4921 0.5161 0.1600  -0.0212 -0.0129 185 GLU B CG  
6011 C  CD  . GLU B 185 ? 0.4330 0.5128 0.5626 0.1504  -0.0081 -0.0274 185 GLU B CD  
6012 O  OE1 . GLU B 185 ? 0.3473 0.6048 0.5105 0.1530  -0.0305 -0.0268 185 GLU B OE1 
6013 O  OE2 . GLU B 185 ? 0.5177 0.4928 0.6500 0.1728  -0.0221 0.0000  185 GLU B OE2 
6020 N  N   . PRO B 186 ? 0.2501 0.5809 0.5044 0.0095  -0.1393 0.0675  186 PRO B N   
6021 C  CA  . PRO B 186 ? 0.2916 0.6395 0.5290 0.0008  -0.1659 0.0937  186 PRO B CA  
6022 C  C   . PRO B 186 ? 0.3194 0.6260 0.6208 0.0706  -0.1425 0.1482  186 PRO B C   
6023 O  O   . PRO B 186 ? 0.4879 0.7110 0.6512 0.0372  -0.0692 0.1320  186 PRO B O   
6024 C  CB  . PRO B 186 ? 0.2960 0.6697 0.5574 -0.0149 -0.1596 0.0872  186 PRO B CB  
6025 C  CG  . PRO B 186 ? 0.3125 0.6654 0.5663 -0.0362 -0.1579 0.0900  186 PRO B CG  
6026 C  CD  . PRO B 186 ? 0.2911 0.6017 0.5468 -0.0768 -0.1619 0.0533  186 PRO B CD  
6034 C  CHA . HEM C .   ? 0.0999 0.1211 0.1786 0.0018  -0.0080 0.0274  201 HEM A CHA 
6035 C  CHB . HEM C .   ? 0.0989 0.0987 0.1899 0.0073  -0.0063 0.0239  201 HEM A CHB 
6036 C  CHC . HEM C .   ? 0.0915 0.1105 0.1625 -0.0004 0.0126  0.0236  201 HEM A CHC 
6037 C  CHD . HEM C .   ? 0.0907 0.1174 0.1406 0.0104  0.0028  0.0255  201 HEM A CHD 
6038 C  C1A . HEM C .   ? 0.1042 0.1061 0.1957 -0.0019 -0.0122 0.0203  201 HEM A C1A 
6039 C  C2A . HEM C .   ? 0.1264 0.1232 0.2166 0.0030  -0.0209 0.0208  201 HEM A C2A 
6040 C  C3A . HEM C .   ? 0.1189 0.1156 0.2188 0.0079  -0.0231 0.0219  201 HEM A C3A 
6041 C  C4A . HEM C .   ? 0.0966 0.1109 0.1864 0.0010  -0.0012 0.0237  201 HEM A C4A 
6042 C  CMA . HEM C .   ? 0.1342 0.1244 0.2610 0.0115  -0.0386 0.0293  201 HEM A CMA 
6043 C  CAA . HEM C .   ? 0.1597 0.1518 0.1707 0.0274  0.0164  0.0175  201 HEM A CAA 
6044 C  CBA . HEM C .   ? 0.1492 0.1874 0.1656 0.0016  0.0299  -0.0002 201 HEM A CBA 
6045 C  CGA . HEM C .   ? 0.1320 0.1255 0.2005 -0.0194 0.0014  -0.0105 201 HEM A CGA 
6046 O  O1A . HEM C .   ? 0.1336 0.1192 0.1864 -0.0005 -0.0059 -0.0078 201 HEM A O1A 
6047 O  O2A . HEM C .   ? 0.1082 0.1691 0.1535 -0.0095 -0.0049 -0.0048 201 HEM A O2A 
6048 C  C1B . HEM C .   ? 0.0926 0.1059 0.1749 0.0067  0.0023  0.0231  201 HEM A C1B 
6049 C  C2B . HEM C .   ? 0.0934 0.1057 0.1887 0.0131  -0.0018 0.0200  201 HEM A C2B 
6050 C  C3B . HEM C .   ? 0.0950 0.1082 0.1756 0.0035  0.0088  0.0217  201 HEM A C3B 
6051 C  C4B . HEM C .   ? 0.0882 0.1071 0.1608 0.0012  0.0133  0.0254  201 HEM A C4B 
6052 C  CMB . HEM C .   ? 0.1028 0.1118 0.2120 0.0142  -0.0083 0.0182  201 HEM A CMB 
6053 C  CAB . HEM C .   ? 0.1009 0.1232 0.1841 0.0115  0.0051  0.0119  201 HEM A CAB 
6054 C  CBB . HEM C .   ? 0.1308 0.1289 0.1987 0.0134  0.0062  0.0193  201 HEM A CBB 
6055 C  C1C . HEM C .   ? 0.0857 0.1017 0.1593 0.0020  0.0174  0.0225  201 HEM A C1C 
6056 C  C2C . HEM C .   ? 0.0864 0.1073 0.1622 -0.0005 0.0179  0.0232  201 HEM A C2C 
6057 C  C3C . HEM C .   ? 0.0928 0.1115 0.1593 0.0011  0.0158  0.0283  201 HEM A C3C 
6058 C  C4C . HEM C .   ? 0.0941 0.1025 0.1564 0.0041  0.0167  0.0258  201 HEM A C4C 
6059 C  CMC . HEM C .   ? 0.0974 0.1141 0.1908 -0.0003 0.0091  0.0193  201 HEM A CMC 
6060 C  CAC . HEM C .   ? 0.1081 0.1158 0.1684 0.0064  0.0122  0.0218  201 HEM A CAC 
6061 C  CBC . HEM C .   ? 0.1190 0.1309 0.1850 0.0020  0.0057  0.0231  201 HEM A CBC 
6062 C  C1D . HEM C .   ? 0.0938 0.1125 0.1431 0.0085  0.0107  0.0239  201 HEM A C1D 
6063 C  C2D . HEM C .   ? 0.0917 0.1251 0.1517 0.0137  0.0042  0.0216  201 HEM A C2D 
6064 C  C3D . HEM C .   ? 0.0972 0.1238 0.1458 0.0108  0.0014  0.0219  201 HEM A C3D 
6065 C  C4D . HEM C .   ? 0.1024 0.1118 0.1532 0.0019  -0.0005 0.0233  201 HEM A C4D 
6066 C  CMD . HEM C .   ? 0.0995 0.1423 0.1785 0.0308  -0.0064 0.0121  201 HEM A CMD 
6067 C  CAD . HEM C .   ? 0.0959 0.1408 0.1394 0.0067  -0.0025 0.0235  201 HEM A CAD 
6068 C  CBD . HEM C .   ? 0.1129 0.1775 0.1585 0.0007  0.0040  0.0088  201 HEM A CBD 
6069 C  CGD . HEM C .   ? 0.1258 0.1363 0.1512 0.0130  0.0111  0.0120  201 HEM A CGD 
6070 O  O1D . HEM C .   ? 0.1342 0.1366 0.1560 0.0157  0.0032  0.0051  201 HEM A O1D 
6071 O  O2D . HEM C .   ? 0.1354 0.1431 0.1456 0.0194  -0.0006 0.0072  201 HEM A O2D 
6072 N  NA  . HEM C .   ? 0.0968 0.1067 0.1760 0.0020  -0.0052 0.0207  201 HEM A NA  
6073 N  NB  . HEM C .   ? 0.0904 0.1013 0.1642 0.0045  0.0071  0.0210  201 HEM A NB  
6074 N  NC  . HEM C .   ? 0.0850 0.1033 0.1608 0.0062  0.0149  0.0208  201 HEM A NC  
6075 N  ND  . HEM C .   ? 0.0902 0.1049 0.1565 0.0032  0.0065  0.0216  201 HEM A ND  
6076 FE FE  . HEM C .   ? 0.0936 0.1073 0.1528 0.0079  0.0040  0.0197  201 HEM A FE  
6083 N  N1  . IMD D .   ? 0.1938 0.1814 0.2537 -0.0043 0.0069  0.0459  202 IMD A N1  
6084 C  C2  . IMD D .   ? 0.1537 0.1908 0.1698 0.0314  0.0129  0.0297  202 IMD A C2  
6085 N  N3  . IMD D .   ? 0.1064 0.1370 0.2049 -0.0083 -0.0193 0.0408  202 IMD A N3  
6086 C  C4  . IMD D .   ? 0.1467 0.1412 0.2451 0.0143  -0.0136 0.0462  202 IMD A C4  
6087 C  C5  . IMD D .   ? 0.1228 0.1543 0.1980 0.0038  0.0223  0.0469  202 IMD A C5  
6092 NA NA  . NA  E .   ? 0.1730 0.1622 0.1738 -0.0031 0.0202  0.0150  203 NA  A NA  
6093 NA NA  . NA  F .   ? 0.1836 0.1635 0.2299 0.0096  -0.0011 -0.0045 204 NA  A NA  
6094 NA NA  . NA  G .   ? 0.2030 0.1974 0.1990 0.0396  0.0263  0.0271  205 NA  A NA  
6095 NA NA  . NA  H .   ? 0.1935 0.1781 0.2696 -0.0241 0.0429  -0.0262 206 NA  A NA  
6096 C  CHA . HEM I .   ? 0.1387 0.1237 0.1299 -0.0043 -0.0200 0.0070  201 HEM B CHA 
6097 C  CHB . HEM I .   ? 0.1476 0.1214 0.1254 0.0030  -0.0109 0.0031  201 HEM B CHB 
6098 C  CHC . HEM I .   ? 0.1337 0.1226 0.1251 0.0107  -0.0089 -0.0126 201 HEM B CHC 
6099 C  CHD . HEM I .   ? 0.1225 0.1162 0.1291 0.0119  -0.0082 -0.0081 201 HEM B CHD 
6100 C  C1A . HEM I .   ? 0.1356 0.1349 0.1298 -0.0020 -0.0146 0.0021  201 HEM B C1A 
6101 C  C2A . HEM I .   ? 0.1364 0.1280 0.1390 0.0047  -0.0135 -0.0062 201 HEM B C2A 
6102 C  C3A . HEM I .   ? 0.1545 0.1202 0.1388 0.0036  -0.0112 0.0107  201 HEM B C3A 
6103 C  C4A . HEM I .   ? 0.1404 0.1150 0.1322 0.0038  -0.0176 0.0035  201 HEM B C4A 
6104 C  CMA . HEM I .   ? 0.1780 0.1578 0.1475 -0.0125 -0.0067 0.0161  201 HEM B CMA 
6105 C  CAA . HEM I .   ? 0.1342 0.1346 0.1360 0.0159  -0.0045 0.0001  201 HEM B CAA 
6106 C  CBA . HEM I .   ? 0.1319 0.1446 0.1540 0.0080  0.0100  -0.0141 201 HEM B CBA 
6107 C  CGA . HEM I .   ? 0.1302 0.1277 0.1322 -0.0011 0.0054  -0.0056 201 HEM B CGA 
6108 O  O1A . HEM I .   ? 0.1274 0.1445 0.1278 -0.0076 0.0094  -0.0102 201 HEM B O1A 
6109 O  O2A . HEM I .   ? 0.1264 0.1475 0.1343 0.0009  0.0027  -0.0154 201 HEM B O2A 
6110 C  C1B . HEM I .   ? 0.1513 0.1144 0.1288 0.0094  -0.0125 0.0008  201 HEM B C1B 
6111 C  C2B . HEM I .   ? 0.1599 0.1314 0.1230 0.0038  -0.0228 -0.0081 201 HEM B C2B 
6112 C  C3B . HEM I .   ? 0.1496 0.1219 0.1323 0.0086  -0.0238 -0.0067 201 HEM B C3B 
6113 C  C4B . HEM I .   ? 0.1427 0.1230 0.1306 0.0145  -0.0216 -0.0110 201 HEM B C4B 
6114 C  CMB . HEM I .   ? 0.1944 0.1522 0.1269 -0.0117 -0.0297 0.0047  201 HEM B CMB 
6115 C  CAB . HEM I .   ? 0.1624 0.1513 0.1442 0.0028  -0.0251 -0.0164 201 HEM B CAB 
6116 C  CBB . HEM I .   ? 0.1766 0.1650 0.1719 0.0117  -0.0340 -0.0169 201 HEM B CBB 
6117 C  C1C . HEM I .   ? 0.1278 0.1177 0.1241 0.0152  -0.0112 -0.0149 201 HEM B C1C 
6118 C  C2C . HEM I .   ? 0.1261 0.1132 0.1279 0.0095  -0.0068 -0.0153 201 HEM B C2C 
6119 C  C3C . HEM I .   ? 0.1299 0.1124 0.1291 0.0166  -0.0097 -0.0074 201 HEM B C3C 
6120 C  C4C . HEM I .   ? 0.1251 0.1089 0.1235 0.0086  -0.0085 -0.0096 201 HEM B C4C 
6121 C  CMC . HEM I .   ? 0.1463 0.1317 0.1489 -0.0093 -0.0188 -0.0120 201 HEM B CMC 
6122 C  CAC . HEM I .   ? 0.1223 0.1445 0.1297 0.0035  -0.0133 -0.0130 201 HEM B CAC 
6123 C  CBC . HEM I .   ? 0.1309 0.1462 0.1732 -0.0038 -0.0225 -0.0077 201 HEM B CBC 
6124 C  C1D . HEM I .   ? 0.1257 0.1184 0.1192 0.0106  -0.0061 -0.0100 201 HEM B C1D 
6125 C  C2D . HEM I .   ? 0.1228 0.1446 0.1239 -0.0055 -0.0131 -0.0056 201 HEM B C2D 
6126 C  C3D . HEM I .   ? 0.1340 0.1384 0.1295 0.0012  -0.0132 -0.0115 201 HEM B C3D 
6127 C  C4D . HEM I .   ? 0.1338 0.1201 0.1270 0.0030  -0.0171 -0.0044 201 HEM B C4D 
6128 C  CMD . HEM I .   ? 0.1302 0.1694 0.1158 -0.0122 -0.0124 -0.0060 201 HEM B CMD 
6129 C  CAD . HEM I .   ? 0.1324 0.1512 0.1445 -0.0003 -0.0205 -0.0193 201 HEM B CAD 
6130 C  CBD . HEM I .   ? 0.1580 0.1982 0.1548 0.0496  -0.0292 -0.0305 201 HEM B CBD 
6131 C  CGD . HEM I .   ? 0.1422 0.1716 0.2162 0.0303  -0.0015 -0.0423 201 HEM B CGD 
6132 O  O1D . HEM I .   ? 0.1829 0.2648 0.2237 0.0941  -0.0053 0.0475  201 HEM B O1D 
6133 O  O2D . HEM I .   ? 0.2071 0.1931 0.2429 0.0238  -0.0087 -0.0409 201 HEM B O2D 
6134 N  NA  . HEM I .   ? 0.1366 0.1251 0.1271 0.0071  -0.0182 0.0000  201 HEM B NA  
6135 N  NB  . HEM I .   ? 0.1338 0.1162 0.1262 0.0031  -0.0145 -0.0055 201 HEM B NB  
6136 N  NC  . HEM I .   ? 0.1151 0.1184 0.1246 0.0118  -0.0094 -0.0101 201 HEM B NC  
6137 N  ND  . HEM I .   ? 0.1266 0.1216 0.1190 0.0033  -0.0157 -0.0010 201 HEM B ND  
6138 FE FE  . HEM I .   ? 0.1246 0.1215 0.1195 0.0094  -0.0138 -0.0077 201 HEM B FE  
6145 N  N1  . IMD J .   ? 0.2051 0.1791 0.2020 0.0034  -0.0219 0.0084  202 IMD B N1  
6146 C  C2  . IMD J .   ? 0.1503 0.1732 0.1647 0.0386  -0.0089 -0.0092 202 IMD B C2  
6147 N  N3  . IMD J .   ? 0.1720 0.1370 0.1399 -0.0113 -0.0459 -0.0069 202 IMD B N3  
6148 C  C4  . IMD J .   ? 0.1891 0.1486 0.1502 -0.0141 -0.0350 0.0086  202 IMD B C4  
6149 C  C5  . IMD J .   ? 0.1638 0.1236 0.1449 0.0318  -0.0357 -0.0149 202 IMD B C5  
6154 NA NA  . NA  K .   ? 0.1677 0.1843 0.2072 0.0014  0.0128  -0.0054 203 NA  B NA  
6155 NA NA  . NA  L .   ? 0.1945 0.2200 0.1944 -0.0354 -0.0125 0.0199  204 NA  B NA  
6156 CL CL  . CL  M .   ? 0.1465 0.1284 0.1663 0.0151  0.0169  0.0036  205 CL  B CL  
# 
