data_9F8N
# 
_entry.id   9F8N 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9F8N         pdb_00009f8n 10.2210/pdb9f8n/pdb 
WWPDB D_1292138237 ?            ?                   
# 
_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       2025-04-16 
_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                        9F8N 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-06 
_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           N 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'Contains the same protein complexed with different ligand' 9F8H unspecified 
PDB 'Contains the same protein complexed with different ligand' 9F8I unspecified 
PDB 'Contains the same protein complexed with different ligand' 9F8J unspecified 
PDB 'Contains the same protein complexed with different ligand' 9F8K unspecified 
PDB 'Contains the same protein complexed with different ligand' 9F8L unspecified 
PDB 'Contains the same protein complexed with different ligand' 9F8M unspecified 
PDB 'Contains the same protein complexed with different ligand' 9F8O unspecified 
PDB 'Contains the same protein complexed with different ligand' 9F8P unspecified 
PDB 'Contains the same protein complexed with different ligand' 9F8R unspecified 
PDB 'Contains the same protein complexed with different ligand' 9F8S unspecified 
PDB 'Contains the same protein complexed with different ligand' 9F8Q unspecified 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
3 wulf.blankenfeldt@helmholtz-hzi.de Wulf   Blankenfeldt ? 'principal investigator/group leader' 0000-0001-9886-9668 
4 c.kunick@tu-braunschweig.de        Conrad Kunick       ? 'principal investigator/group leader' 0000-0001-7041-5322 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Thiemann, M.'     1 0009-0009-1111-0671 
'Zimmermann, M.'   2 0009-0005-8293-7255 
'Kunick, C.'       3 0000-0001-7041-5322 
'Blankenfeldt, W.' 4 0000-0001-9886-9668 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                7390 
_citation.page_last                 7420 
_citation.title                     
;From Bones to Bugs: Structure-Based Development of Raloxifene-Derived Pathoblockers That Inhibit Pyocyanin Production in Pseudomonas aeruginosa.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c03065 
_citation.pdbx_database_id_PubMed   40156840 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Thiemann, M.'        1  0009-0009-1111-0671 
primary 'Zimmermann, M.'      2  0009-0005-8293-7255 
primary 'Diederich, C.'       3  ?                   
primary 'Zhan, H.'            4  0009-0002-7304-9174 
primary 'Lebedev, M.'         5  0000-0001-7461-0977 
primary 'Pletz, J.'           6  ?                   
primary 'Baumgarten, J.'      7  0009-0003-6748-6316 
primary 'Handke, M.'          8  0009-0007-7175-3615 
primary 'Musken, M.'          9  ?                   
primary 'Breinbauer, R.'      10 0000-0001-6009-7359 
primary 'Krasteva-Christ, G.' 11 0000-0002-0113-521X 
primary 'Zanin, E.'           12 ?                   
primary 'Empting, M.'         13 ?                   
primary 'Schiedel, M.'        14 0000-0001-7365-3617 
primary 'Kunick, C.'          15 ?                   
primary 'Blankenfeldt, W.'    16 0000-0001-9886-9668 
# 
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 'Phenazine biosynthesis protein A/B'                                                             21531.025 2   ? 
? ? ? 
2 non-polymer syn '[2-(4-hydroxyphenyl)-6-oxidanyl-1-benzothiophen-3-yl]-[2-(2-methylpropylamino)phenyl]methanone' 417.520   2   ? 
? ? ? 
3 non-polymer syn GLYCEROL                                                                                         92.094    2   ? 
? ? ? 
4 water       nat water                                                                                            18.015    380 ? 
? ? ? 
# 
_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       
;MGSSHHHHHHSSGLVPRGSHMSDVESLENTSENRAQVAARQHNRKIVEQYMHTRGEARLKRHLLFTEDGVGGLWTTDSGQ
PIAIRGREKLGEHAVWSLQCFPDWVWTDIQIFETQDPNWFWVECRGEGAIVFPGYPRGQYRNHFLHSFRFENGLIKEQRE
FMNPCEQFRSLGIEVPEVRRDGLPS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSSGLVPRGSHMSDVESLENTSENRAQVAARQHNRKIVEQYMHTRGEARLKRHLLFTEDGVGGLWTTDSGQ
PIAIRGREKLGEHAVWSLQCFPDWVWTDIQIFETQDPNWFWVECRGEGAIVFPGYPRGQYRNHFLHSFRFENGLIKEQRE
FMNPCEQFRSLGIEVPEVRRDGLPS
;
_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 '[2-(4-hydroxyphenyl)-6-oxidanyl-1-benzothiophen-3-yl]-[2-(2-methylpropylamino)phenyl]methanone' A1IAD 
3 GLYCEROL                                                                                         GOL   
4 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   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  PRO n 
1 17  ARG n 
1 18  GLY n 
1 19  SER n 
1 20  HIS n 
1 21  MET n 
1 22  SER n 
1 23  ASP n 
1 24  VAL n 
1 25  GLU n 
1 26  SER n 
1 27  LEU n 
1 28  GLU n 
1 29  ASN n 
1 30  THR n 
1 31  SER n 
1 32  GLU n 
1 33  ASN n 
1 34  ARG n 
1 35  ALA n 
1 36  GLN n 
1 37  VAL n 
1 38  ALA n 
1 39  ALA n 
1 40  ARG n 
1 41  GLN n 
1 42  HIS n 
1 43  ASN n 
1 44  ARG n 
1 45  LYS n 
1 46  ILE n 
1 47  VAL n 
1 48  GLU n 
1 49  GLN n 
1 50  TYR n 
1 51  MET n 
1 52  HIS n 
1 53  THR n 
1 54  ARG n 
1 55  GLY n 
1 56  GLU n 
1 57  ALA n 
1 58  ARG n 
1 59  LEU n 
1 60  LYS n 
1 61  ARG n 
1 62  HIS n 
1 63  LEU n 
1 64  LEU n 
1 65  PHE n 
1 66  THR n 
1 67  GLU n 
1 68  ASP n 
1 69  GLY n 
1 70  VAL n 
1 71  GLY n 
1 72  GLY n 
1 73  LEU n 
1 74  TRP n 
1 75  THR n 
1 76  THR n 
1 77  ASP n 
1 78  SER n 
1 79  GLY n 
1 80  GLN n 
1 81  PRO n 
1 82  ILE n 
1 83  ALA n 
1 84  ILE n 
1 85  ARG n 
1 86  GLY n 
1 87  ARG n 
1 88  GLU n 
1 89  LYS n 
1 90  LEU n 
1 91  GLY n 
1 92  GLU n 
1 93  HIS n 
1 94  ALA n 
1 95  VAL n 
1 96  TRP n 
1 97  SER n 
1 98  LEU n 
1 99  GLN n 
1 100 CYS n 
1 101 PHE n 
1 102 PRO n 
1 103 ASP n 
1 104 TRP n 
1 105 VAL n 
1 106 TRP n 
1 107 THR n 
1 108 ASP n 
1 109 ILE n 
1 110 GLN n 
1 111 ILE n 
1 112 PHE n 
1 113 GLU n 
1 114 THR n 
1 115 GLN n 
1 116 ASP n 
1 117 PRO n 
1 118 ASN n 
1 119 TRP n 
1 120 PHE n 
1 121 TRP n 
1 122 VAL n 
1 123 GLU n 
1 124 CYS n 
1 125 ARG n 
1 126 GLY n 
1 127 GLU n 
1 128 GLY n 
1 129 ALA n 
1 130 ILE n 
1 131 VAL n 
1 132 PHE n 
1 133 PRO n 
1 134 GLY n 
1 135 TYR n 
1 136 PRO n 
1 137 ARG n 
1 138 GLY n 
1 139 GLN n 
1 140 TYR n 
1 141 ARG n 
1 142 ASN n 
1 143 HIS n 
1 144 PHE n 
1 145 LEU n 
1 146 HIS n 
1 147 SER n 
1 148 PHE n 
1 149 ARG n 
1 150 PHE n 
1 151 GLU n 
1 152 ASN n 
1 153 GLY n 
1 154 LEU n 
1 155 ILE n 
1 156 LYS n 
1 157 GLU n 
1 158 GLN n 
1 159 ARG n 
1 160 GLU n 
1 161 PHE n 
1 162 MET n 
1 163 ASN n 
1 164 PRO n 
1 165 CYS n 
1 166 GLU n 
1 167 GLN n 
1 168 PHE n 
1 169 ARG n 
1 170 SER n 
1 171 LEU n 
1 172 GLY n 
1 173 ILE n 
1 174 GLU n 
1 175 VAL n 
1 176 PRO n 
1 177 GLU n 
1 178 VAL n 
1 179 ARG n 
1 180 ARG n 
1 181 ASP n 
1 182 GLY n 
1 183 LEU n 
1 184 PRO n 
1 185 SER 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                   185 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 Bcep18194_B1568 
_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      'Burkholderia lata' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     482957 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_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 
A1IAD non-polymer         . '[2-(4-hydroxyphenyl)-6-oxidanyl-1-benzothiophen-3-yl]-[2-(2-methylpropylamino)phenyl]methanone' 
'[6-Hydroxy-2-(4-hydroxyphenyl)benzo[b]thiophen-3-yl][2-(isobutylamino)phenyl]methanone' 'C25 H23 N O3 S' 417.520 
ALA   'L-peptide linking' y ALANINE                                                                                          ? 
'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                                         ? 
'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                       ? 
'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                                  ? 
'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                         ? 
'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                                        ? 
'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                                  ? 
'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                                          ? 
'C2 H5 N O2'     75.067  
GOL   non-polymer         . GLYCEROL                                                                                         
'GLYCERIN; PROPANE-1,2,3-TRIOL'                                                          'C3 H8 O3'       92.094  
HIS   'L-peptide linking' y HISTIDINE                                                                                        ? 
'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                                            ? 
'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                       ? 
'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                          ? 
'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                                           ? 
'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                                       ? 
'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                    ? 
'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                                          ? 
'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                                           ? 
'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                                                        ? 
'C4 H9 N O3'     119.119 
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   -19 ?   ?   ?   A . n 
A 1 2   GLY 2   -18 ?   ?   ?   A . n 
A 1 3   SER 3   -17 ?   ?   ?   A . n 
A 1 4   SER 4   -16 ?   ?   ?   A . n 
A 1 5   HIS 5   -15 ?   ?   ?   A . n 
A 1 6   HIS 6   -14 ?   ?   ?   A . n 
A 1 7   HIS 7   -13 ?   ?   ?   A . n 
A 1 8   HIS 8   -12 ?   ?   ?   A . n 
A 1 9   HIS 9   -11 ?   ?   ?   A . n 
A 1 10  HIS 10  -10 ?   ?   ?   A . n 
A 1 11  SER 11  -9  ?   ?   ?   A . n 
A 1 12  SER 12  -8  ?   ?   ?   A . n 
A 1 13  GLY 13  -7  ?   ?   ?   A . n 
A 1 14  LEU 14  -6  ?   ?   ?   A . n 
A 1 15  VAL 15  -5  ?   ?   ?   A . n 
A 1 16  PRO 16  -4  ?   ?   ?   A . n 
A 1 17  ARG 17  -3  ?   ?   ?   A . n 
A 1 18  GLY 18  -2  ?   ?   ?   A . n 
A 1 19  SER 19  -1  ?   ?   ?   A . n 
A 1 20  HIS 20  0   ?   ?   ?   A . n 
A 1 21  MET 21  1   ?   ?   ?   A . n 
A 1 22  SER 22  2   ?   ?   ?   A . n 
A 1 23  ASP 23  3   ?   ?   ?   A . n 
A 1 24  VAL 24  4   ?   ?   ?   A . n 
A 1 25  GLU 25  5   ?   ?   ?   A . n 
A 1 26  SER 26  6   ?   ?   ?   A . n 
A 1 27  LEU 27  7   ?   ?   ?   A . n 
A 1 28  GLU 28  8   ?   ?   ?   A . n 
A 1 29  ASN 29  9   ?   ?   ?   A . n 
A 1 30  THR 30  10  ?   ?   ?   A . n 
A 1 31  SER 31  11  11  SER SER A . n 
A 1 32  GLU 32  12  12  GLU GLU A . n 
A 1 33  ASN 33  13  13  ASN ASN A . n 
A 1 34  ARG 34  14  14  ARG ARG A . n 
A 1 35  ALA 35  15  15  ALA ALA A . n 
A 1 36  GLN 36  16  16  GLN GLN A . n 
A 1 37  VAL 37  17  17  VAL VAL A . n 
A 1 38  ALA 38  18  18  ALA ALA A . n 
A 1 39  ALA 39  19  19  ALA ALA A . n 
A 1 40  ARG 40  20  20  ARG ARG A . n 
A 1 41  GLN 41  21  21  GLN GLN A . n 
A 1 42  HIS 42  22  22  HIS HIS A . n 
A 1 43  ASN 43  23  23  ASN ASN A . n 
A 1 44  ARG 44  24  24  ARG ARG A . n 
A 1 45  LYS 45  25  25  LYS LYS A . n 
A 1 46  ILE 46  26  26  ILE ILE A . n 
A 1 47  VAL 47  27  27  VAL VAL A . n 
A 1 48  GLU 48  28  28  GLU GLU A . n 
A 1 49  GLN 49  29  29  GLN GLN A . n 
A 1 50  TYR 50  30  30  TYR TYR A . n 
A 1 51  MET 51  31  31  MET MET A . n 
A 1 52  HIS 52  32  32  HIS HIS A . n 
A 1 53  THR 53  33  33  THR THR A . n 
A 1 54  ARG 54  34  34  ARG ARG A . n 
A 1 55  GLY 55  35  35  GLY GLY A . n 
A 1 56  GLU 56  36  36  GLU GLU A . n 
A 1 57  ALA 57  37  37  ALA ALA A . n 
A 1 58  ARG 58  38  38  ARG ARG A . n 
A 1 59  LEU 59  39  39  LEU LEU A . n 
A 1 60  LYS 60  40  40  LYS LYS A . n 
A 1 61  ARG 61  41  41  ARG ARG A . n 
A 1 62  HIS 62  42  42  HIS HIS A . n 
A 1 63  LEU 63  43  43  LEU LEU A . n 
A 1 64  LEU 64  44  44  LEU LEU A . n 
A 1 65  PHE 65  45  45  PHE PHE A . n 
A 1 66  THR 66  46  46  THR THR A . n 
A 1 67  GLU 67  47  47  GLU GLU A . n 
A 1 68  ASP 68  48  48  ASP ASP A . n 
A 1 69  GLY 69  49  49  GLY GLY A . n 
A 1 70  VAL 70  50  50  VAL VAL A . n 
A 1 71  GLY 71  51  51  GLY GLY A . n 
A 1 72  GLY 72  52  52  GLY GLY A . n 
A 1 73  LEU 73  53  53  LEU LEU A . n 
A 1 74  TRP 74  54  54  TRP TRP A . n 
A 1 75  THR 75  55  55  THR THR A . n 
A 1 76  THR 76  56  56  THR THR A . n 
A 1 77  ASP 77  57  57  ASP ASP A . n 
A 1 78  SER 78  58  58  SER SER A . n 
A 1 79  GLY 79  59  59  GLY GLY A . n 
A 1 80  GLN 80  60  60  GLN GLN A . n 
A 1 81  PRO 81  61  61  PRO PRO A . n 
A 1 82  ILE 82  62  62  ILE ILE A . n 
A 1 83  ALA 83  63  63  ALA ALA A . n 
A 1 84  ILE 84  64  64  ILE ILE A . n 
A 1 85  ARG 85  65  65  ARG ARG A . n 
A 1 86  GLY 86  66  66  GLY GLY A . n 
A 1 87  ARG 87  67  67  ARG ARG A . n 
A 1 88  GLU 88  68  68  GLU GLU A . n 
A 1 89  LYS 89  69  69  LYS LYS A . n 
A 1 90  LEU 90  70  70  LEU LEU A . n 
A 1 91  GLY 91  71  71  GLY GLY A . n 
A 1 92  GLU 92  72  72  GLU GLU A . n 
A 1 93  HIS 93  73  73  HIS HIS A . n 
A 1 94  ALA 94  74  74  ALA ALA A . n 
A 1 95  VAL 95  75  75  VAL VAL A . n 
A 1 96  TRP 96  76  76  TRP TRP A . n 
A 1 97  SER 97  77  77  SER SER A . n 
A 1 98  LEU 98  78  78  LEU LEU A . n 
A 1 99  GLN 99  79  79  GLN GLN A . n 
A 1 100 CYS 100 80  80  CYS CYS A . n 
A 1 101 PHE 101 81  81  PHE PHE A . n 
A 1 102 PRO 102 82  82  PRO PRO A . n 
A 1 103 ASP 103 83  83  ASP ASP A . n 
A 1 104 TRP 104 84  84  TRP TRP A . n 
A 1 105 VAL 105 85  85  VAL VAL A . n 
A 1 106 TRP 106 86  86  TRP TRP A . n 
A 1 107 THR 107 87  87  THR THR A . n 
A 1 108 ASP 108 88  88  ASP ASP A . n 
A 1 109 ILE 109 89  89  ILE ILE A . n 
A 1 110 GLN 110 90  90  GLN GLN A . n 
A 1 111 ILE 111 91  91  ILE ILE A . n 
A 1 112 PHE 112 92  92  PHE PHE A . n 
A 1 113 GLU 113 93  93  GLU GLU A . n 
A 1 114 THR 114 94  94  THR THR A . n 
A 1 115 GLN 115 95  95  GLN GLN A . n 
A 1 116 ASP 116 96  96  ASP ASP A . n 
A 1 117 PRO 117 97  97  PRO PRO A . n 
A 1 118 ASN 118 98  98  ASN ASN A . n 
A 1 119 TRP 119 99  99  TRP TRP A . n 
A 1 120 PHE 120 100 100 PHE PHE A . n 
A 1 121 TRP 121 101 101 TRP TRP A . n 
A 1 122 VAL 122 102 102 VAL VAL A . n 
A 1 123 GLU 123 103 103 GLU GLU A . n 
A 1 124 CYS 124 104 104 CYS CYS A . n 
A 1 125 ARG 125 105 105 ARG ARG A . n 
A 1 126 GLY 126 106 106 GLY GLY A . n 
A 1 127 GLU 127 107 107 GLU GLU A . n 
A 1 128 GLY 128 108 108 GLY GLY A . n 
A 1 129 ALA 129 109 109 ALA ALA A . n 
A 1 130 ILE 130 110 110 ILE ILE A . n 
A 1 131 VAL 131 111 111 VAL VAL A . n 
A 1 132 PHE 132 112 112 PHE PHE A . n 
A 1 133 PRO 133 113 113 PRO PRO A . n 
A 1 134 GLY 134 114 114 GLY GLY A . n 
A 1 135 TYR 135 115 115 TYR TYR A . n 
A 1 136 PRO 136 116 116 PRO PRO A . n 
A 1 137 ARG 137 117 117 ARG ARG A . n 
A 1 138 GLY 138 118 118 GLY GLY A . n 
A 1 139 GLN 139 119 119 GLN GLN A . n 
A 1 140 TYR 140 120 120 TYR TYR A . n 
A 1 141 ARG 141 121 121 ARG ARG A . n 
A 1 142 ASN 142 122 122 ASN ASN A . n 
A 1 143 HIS 143 123 123 HIS HIS A . n 
A 1 144 PHE 144 124 124 PHE PHE A . n 
A 1 145 LEU 145 125 125 LEU LEU A . n 
A 1 146 HIS 146 126 126 HIS HIS A . n 
A 1 147 SER 147 127 127 SER SER A . n 
A 1 148 PHE 148 128 128 PHE PHE A . n 
A 1 149 ARG 149 129 129 ARG ARG A . n 
A 1 150 PHE 150 130 130 PHE PHE A . n 
A 1 151 GLU 151 131 131 GLU GLU A . n 
A 1 152 ASN 152 132 132 ASN ASN A . n 
A 1 153 GLY 153 133 133 GLY GLY A . n 
A 1 154 LEU 154 134 134 LEU LEU A . n 
A 1 155 ILE 155 135 135 ILE ILE A . n 
A 1 156 LYS 156 136 136 LYS LYS A . n 
A 1 157 GLU 157 137 137 GLU GLU A . n 
A 1 158 GLN 158 138 138 GLN GLN A . n 
A 1 159 ARG 159 139 139 ARG ARG A . n 
A 1 160 GLU 160 140 140 GLU GLU A . n 
A 1 161 PHE 161 141 141 PHE PHE A . n 
A 1 162 MET 162 142 142 MET MET A . n 
A 1 163 ASN 163 143 143 ASN ASN A . n 
A 1 164 PRO 164 144 144 PRO PRO A . n 
A 1 165 CYS 165 145 145 CYS CYS A . n 
A 1 166 GLU 166 146 146 GLU GLU A . n 
A 1 167 GLN 167 147 147 GLN GLN A . n 
A 1 168 PHE 168 148 148 PHE PHE A . n 
A 1 169 ARG 169 149 149 ARG ARG A . n 
A 1 170 SER 170 150 150 SER SER A . n 
A 1 171 LEU 171 151 151 LEU LEU A . n 
A 1 172 GLY 172 152 152 GLY GLY A . n 
A 1 173 ILE 173 153 153 ILE ILE A . n 
A 1 174 GLU 174 154 154 GLU GLU A . n 
A 1 175 VAL 175 155 155 VAL VAL A . n 
A 1 176 PRO 176 156 156 PRO PRO A . n 
A 1 177 GLU 177 157 157 GLU GLU A . n 
A 1 178 VAL 178 158 158 VAL VAL A . n 
A 1 179 ARG 179 159 159 ARG ARG A . n 
A 1 180 ARG 180 160 160 ARG ARG A . n 
A 1 181 ASP 181 161 161 ASP ASP A . n 
A 1 182 GLY 182 162 162 GLY GLY A . n 
A 1 183 LEU 183 163 163 LEU LEU A . n 
A 1 184 PRO 184 164 164 PRO PRO A . n 
A 1 185 SER 185 165 ?   ?   ?   A . n 
B 1 1   MET 1   -19 ?   ?   ?   B . n 
B 1 2   GLY 2   -18 ?   ?   ?   B . n 
B 1 3   SER 3   -17 ?   ?   ?   B . n 
B 1 4   SER 4   -16 ?   ?   ?   B . n 
B 1 5   HIS 5   -15 ?   ?   ?   B . n 
B 1 6   HIS 6   -14 ?   ?   ?   B . n 
B 1 7   HIS 7   -13 ?   ?   ?   B . n 
B 1 8   HIS 8   -12 ?   ?   ?   B . n 
B 1 9   HIS 9   -11 ?   ?   ?   B . n 
B 1 10  HIS 10  -10 ?   ?   ?   B . n 
B 1 11  SER 11  -9  ?   ?   ?   B . n 
B 1 12  SER 12  -8  ?   ?   ?   B . n 
B 1 13  GLY 13  -7  ?   ?   ?   B . n 
B 1 14  LEU 14  -6  ?   ?   ?   B . n 
B 1 15  VAL 15  -5  ?   ?   ?   B . n 
B 1 16  PRO 16  -4  ?   ?   ?   B . n 
B 1 17  ARG 17  -3  ?   ?   ?   B . n 
B 1 18  GLY 18  -2  ?   ?   ?   B . n 
B 1 19  SER 19  -1  ?   ?   ?   B . n 
B 1 20  HIS 20  0   ?   ?   ?   B . n 
B 1 21  MET 21  1   ?   ?   ?   B . n 
B 1 22  SER 22  2   ?   ?   ?   B . n 
B 1 23  ASP 23  3   ?   ?   ?   B . n 
B 1 24  VAL 24  4   ?   ?   ?   B . n 
B 1 25  GLU 25  5   ?   ?   ?   B . n 
B 1 26  SER 26  6   ?   ?   ?   B . n 
B 1 27  LEU 27  7   ?   ?   ?   B . n 
B 1 28  GLU 28  8   ?   ?   ?   B . n 
B 1 29  ASN 29  9   ?   ?   ?   B . n 
B 1 30  THR 30  10  ?   ?   ?   B . n 
B 1 31  SER 31  11  ?   ?   ?   B . n 
B 1 32  GLU 32  12  12  GLU GLU B . n 
B 1 33  ASN 33  13  13  ASN ASN B . n 
B 1 34  ARG 34  14  14  ARG ARG B . n 
B 1 35  ALA 35  15  15  ALA ALA B . n 
B 1 36  GLN 36  16  16  GLN GLN B . n 
B 1 37  VAL 37  17  17  VAL VAL B . n 
B 1 38  ALA 38  18  18  ALA ALA B . n 
B 1 39  ALA 39  19  19  ALA ALA B . n 
B 1 40  ARG 40  20  20  ARG ARG B . n 
B 1 41  GLN 41  21  21  GLN GLN B . n 
B 1 42  HIS 42  22  22  HIS HIS B . n 
B 1 43  ASN 43  23  23  ASN ASN B . n 
B 1 44  ARG 44  24  24  ARG ARG B . n 
B 1 45  LYS 45  25  25  LYS LYS B . n 
B 1 46  ILE 46  26  26  ILE ILE B . n 
B 1 47  VAL 47  27  27  VAL VAL B . n 
B 1 48  GLU 48  28  28  GLU GLU B . n 
B 1 49  GLN 49  29  29  GLN GLN B . n 
B 1 50  TYR 50  30  30  TYR TYR B . n 
B 1 51  MET 51  31  31  MET MET B . n 
B 1 52  HIS 52  32  32  HIS HIS B . n 
B 1 53  THR 53  33  33  THR THR B . n 
B 1 54  ARG 54  34  34  ARG ARG B . n 
B 1 55  GLY 55  35  35  GLY GLY B . n 
B 1 56  GLU 56  36  36  GLU GLU B . n 
B 1 57  ALA 57  37  37  ALA ALA B . n 
B 1 58  ARG 58  38  38  ARG ARG B . n 
B 1 59  LEU 59  39  39  LEU LEU B . n 
B 1 60  LYS 60  40  40  LYS LYS B . n 
B 1 61  ARG 61  41  41  ARG ARG B . n 
B 1 62  HIS 62  42  42  HIS HIS B . n 
B 1 63  LEU 63  43  43  LEU LEU B . n 
B 1 64  LEU 64  44  44  LEU LEU B . n 
B 1 65  PHE 65  45  45  PHE PHE B . n 
B 1 66  THR 66  46  46  THR THR B . n 
B 1 67  GLU 67  47  47  GLU GLU B . n 
B 1 68  ASP 68  48  48  ASP ASP B . n 
B 1 69  GLY 69  49  49  GLY GLY B . n 
B 1 70  VAL 70  50  50  VAL VAL B . n 
B 1 71  GLY 71  51  51  GLY GLY B . n 
B 1 72  GLY 72  52  52  GLY GLY B . n 
B 1 73  LEU 73  53  53  LEU LEU B . n 
B 1 74  TRP 74  54  54  TRP TRP B . n 
B 1 75  THR 75  55  55  THR THR B . n 
B 1 76  THR 76  56  56  THR THR B . n 
B 1 77  ASP 77  57  57  ASP ASP B . n 
B 1 78  SER 78  58  58  SER SER B . n 
B 1 79  GLY 79  59  59  GLY GLY B . n 
B 1 80  GLN 80  60  60  GLN GLN B . n 
B 1 81  PRO 81  61  61  PRO PRO B . n 
B 1 82  ILE 82  62  62  ILE ILE B . n 
B 1 83  ALA 83  63  63  ALA ALA B . n 
B 1 84  ILE 84  64  64  ILE ILE B . n 
B 1 85  ARG 85  65  65  ARG ARG B . n 
B 1 86  GLY 86  66  66  GLY GLY B . n 
B 1 87  ARG 87  67  67  ARG ARG B . n 
B 1 88  GLU 88  68  68  GLU GLU B . n 
B 1 89  LYS 89  69  69  LYS LYS B . n 
B 1 90  LEU 90  70  70  LEU LEU B . n 
B 1 91  GLY 91  71  71  GLY GLY B . n 
B 1 92  GLU 92  72  72  GLU GLU B . n 
B 1 93  HIS 93  73  73  HIS HIS B . n 
B 1 94  ALA 94  74  74  ALA ALA B . n 
B 1 95  VAL 95  75  75  VAL VAL B . n 
B 1 96  TRP 96  76  76  TRP TRP B . n 
B 1 97  SER 97  77  77  SER SER B . n 
B 1 98  LEU 98  78  78  LEU LEU B . n 
B 1 99  GLN 99  79  79  GLN GLN B . n 
B 1 100 CYS 100 80  80  CYS CYS B . n 
B 1 101 PHE 101 81  81  PHE PHE B . n 
B 1 102 PRO 102 82  82  PRO PRO B . n 
B 1 103 ASP 103 83  83  ASP ASP B . n 
B 1 104 TRP 104 84  84  TRP TRP B . n 
B 1 105 VAL 105 85  85  VAL VAL B . n 
B 1 106 TRP 106 86  86  TRP TRP B . n 
B 1 107 THR 107 87  87  THR THR B . n 
B 1 108 ASP 108 88  88  ASP ASP B . n 
B 1 109 ILE 109 89  89  ILE ILE B . n 
B 1 110 GLN 110 90  90  GLN GLN B . n 
B 1 111 ILE 111 91  91  ILE ILE B . n 
B 1 112 PHE 112 92  92  PHE PHE B . n 
B 1 113 GLU 113 93  93  GLU GLU B . n 
B 1 114 THR 114 94  94  THR THR B . n 
B 1 115 GLN 115 95  95  GLN GLN B . n 
B 1 116 ASP 116 96  96  ASP ASP B . n 
B 1 117 PRO 117 97  97  PRO PRO B . n 
B 1 118 ASN 118 98  98  ASN ASN B . n 
B 1 119 TRP 119 99  99  TRP TRP B . n 
B 1 120 PHE 120 100 100 PHE PHE B . n 
B 1 121 TRP 121 101 101 TRP TRP B . n 
B 1 122 VAL 122 102 102 VAL VAL B . n 
B 1 123 GLU 123 103 103 GLU GLU B . n 
B 1 124 CYS 124 104 104 CYS CYS B . n 
B 1 125 ARG 125 105 105 ARG ARG B . n 
B 1 126 GLY 126 106 106 GLY GLY B . n 
B 1 127 GLU 127 107 107 GLU GLU B . n 
B 1 128 GLY 128 108 108 GLY GLY B . n 
B 1 129 ALA 129 109 109 ALA ALA B . n 
B 1 130 ILE 130 110 110 ILE ILE B . n 
B 1 131 VAL 131 111 111 VAL VAL B . n 
B 1 132 PHE 132 112 112 PHE PHE B . n 
B 1 133 PRO 133 113 113 PRO PRO B . n 
B 1 134 GLY 134 114 114 GLY GLY B . n 
B 1 135 TYR 135 115 115 TYR TYR B . n 
B 1 136 PRO 136 116 116 PRO PRO B . n 
B 1 137 ARG 137 117 117 ARG ARG B . n 
B 1 138 GLY 138 118 118 GLY GLY B . n 
B 1 139 GLN 139 119 119 GLN GLN B . n 
B 1 140 TYR 140 120 120 TYR TYR B . n 
B 1 141 ARG 141 121 121 ARG ARG B . n 
B 1 142 ASN 142 122 122 ASN ASN B . n 
B 1 143 HIS 143 123 123 HIS HIS B . n 
B 1 144 PHE 144 124 124 PHE PHE B . n 
B 1 145 LEU 145 125 125 LEU LEU B . n 
B 1 146 HIS 146 126 126 HIS HIS B . n 
B 1 147 SER 147 127 127 SER SER B . n 
B 1 148 PHE 148 128 128 PHE PHE B . n 
B 1 149 ARG 149 129 129 ARG ARG B . n 
B 1 150 PHE 150 130 130 PHE PHE B . n 
B 1 151 GLU 151 131 131 GLU GLU B . n 
B 1 152 ASN 152 132 132 ASN ASN B . n 
B 1 153 GLY 153 133 133 GLY GLY B . n 
B 1 154 LEU 154 134 134 LEU LEU B . n 
B 1 155 ILE 155 135 135 ILE ILE B . n 
B 1 156 LYS 156 136 136 LYS LYS B . n 
B 1 157 GLU 157 137 137 GLU GLU B . n 
B 1 158 GLN 158 138 138 GLN GLN B . n 
B 1 159 ARG 159 139 139 ARG ARG B . n 
B 1 160 GLU 160 140 140 GLU GLU B . n 
B 1 161 PHE 161 141 141 PHE PHE B . n 
B 1 162 MET 162 142 142 MET MET B . n 
B 1 163 ASN 163 143 143 ASN ASN B . n 
B 1 164 PRO 164 144 144 PRO PRO B . n 
B 1 165 CYS 165 145 145 CYS CYS B . n 
B 1 166 GLU 166 146 146 GLU GLU B . n 
B 1 167 GLN 167 147 147 GLN GLN B . n 
B 1 168 PHE 168 148 148 PHE PHE B . n 
B 1 169 ARG 169 149 149 ARG ARG B . n 
B 1 170 SER 170 150 150 SER SER B . n 
B 1 171 LEU 171 151 151 LEU LEU B . n 
B 1 172 GLY 172 152 152 GLY GLY B . n 
B 1 173 ILE 173 153 153 ILE ILE B . n 
B 1 174 GLU 174 154 154 GLU GLU B . n 
B 1 175 VAL 175 155 155 VAL VAL B . n 
B 1 176 PRO 176 156 156 PRO PRO B . n 
B 1 177 GLU 177 157 157 GLU GLU B . n 
B 1 178 VAL 178 158 158 VAL VAL B . n 
B 1 179 ARG 179 159 159 ARG ARG B . n 
B 1 180 ARG 180 160 160 ARG ARG B . n 
B 1 181 ASP 181 161 161 ASP ASP B . n 
B 1 182 GLY 182 162 162 GLY GLY B . n 
B 1 183 LEU 183 163 163 LEU LEU B . n 
B 1 184 PRO 184 164 164 PRO PRO B . n 
B 1 185 SER 185 165 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IAD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IAD 
_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 A1IAD 1   201 201 A1IAD KT9 A . 
D 3 GOL   1   202 205 GOL   GOL A . 
E 3 GOL   1   203 206 GOL   GOL A . 
F 2 A1IAD 1   201 201 A1IAD KT9 B . 
G 4 HOH   1   301 181 HOH   HOH A . 
G 4 HOH   2   302 513 HOH   HOH A . 
G 4 HOH   3   303 73  HOH   HOH A . 
G 4 HOH   4   304 315 HOH   HOH A . 
G 4 HOH   5   305 288 HOH   HOH A . 
G 4 HOH   6   306 330 HOH   HOH A . 
G 4 HOH   7   307 208 HOH   HOH A . 
G 4 HOH   8   308 244 HOH   HOH A . 
G 4 HOH   9   309 539 HOH   HOH A . 
G 4 HOH   10  310 290 HOH   HOH A . 
G 4 HOH   11  311 26  HOH   HOH A . 
G 4 HOH   12  312 241 HOH   HOH A . 
G 4 HOH   13  313 365 HOH   HOH A . 
G 4 HOH   14  314 568 HOH   HOH A . 
G 4 HOH   15  315 57  HOH   HOH A . 
G 4 HOH   16  316 256 HOH   HOH A . 
G 4 HOH   17  317 176 HOH   HOH A . 
G 4 HOH   18  318 277 HOH   HOH A . 
G 4 HOH   19  319 191 HOH   HOH A . 
G 4 HOH   20  320 402 HOH   HOH A . 
G 4 HOH   21  321 177 HOH   HOH A . 
G 4 HOH   22  322 87  HOH   HOH A . 
G 4 HOH   23  323 409 HOH   HOH A . 
G 4 HOH   24  324 7   HOH   HOH A . 
G 4 HOH   25  325 3   HOH   HOH A . 
G 4 HOH   26  326 55  HOH   HOH A . 
G 4 HOH   27  327 490 HOH   HOH A . 
G 4 HOH   28  328 17  HOH   HOH A . 
G 4 HOH   29  329 15  HOH   HOH A . 
G 4 HOH   30  330 203 HOH   HOH A . 
G 4 HOH   31  331 30  HOH   HOH A . 
G 4 HOH   32  332 45  HOH   HOH A . 
G 4 HOH   33  333 300 HOH   HOH A . 
G 4 HOH   34  334 71  HOH   HOH A . 
G 4 HOH   35  335 328 HOH   HOH A . 
G 4 HOH   36  336 142 HOH   HOH A . 
G 4 HOH   37  337 281 HOH   HOH A . 
G 4 HOH   38  338 298 HOH   HOH A . 
G 4 HOH   39  339 570 HOH   HOH A . 
G 4 HOH   40  340 497 HOH   HOH A . 
G 4 HOH   41  341 325 HOH   HOH A . 
G 4 HOH   42  342 130 HOH   HOH A . 
G 4 HOH   43  343 137 HOH   HOH A . 
G 4 HOH   44  344 154 HOH   HOH A . 
G 4 HOH   45  345 186 HOH   HOH A . 
G 4 HOH   46  346 100 HOH   HOH A . 
G 4 HOH   47  347 146 HOH   HOH A . 
G 4 HOH   48  348 173 HOH   HOH A . 
G 4 HOH   49  349 199 HOH   HOH A . 
G 4 HOH   50  350 350 HOH   HOH A . 
G 4 HOH   51  351 105 HOH   HOH A . 
G 4 HOH   52  352 396 HOH   HOH A . 
G 4 HOH   53  353 36  HOH   HOH A . 
G 4 HOH   54  354 106 HOH   HOH A . 
G 4 HOH   55  355 115 HOH   HOH A . 
G 4 HOH   56  356 273 HOH   HOH A . 
G 4 HOH   57  357 103 HOH   HOH A . 
G 4 HOH   58  358 78  HOH   HOH A . 
G 4 HOH   59  359 46  HOH   HOH A . 
G 4 HOH   60  360 236 HOH   HOH A . 
G 4 HOH   61  361 168 HOH   HOH A . 
G 4 HOH   62  362 206 HOH   HOH A . 
G 4 HOH   63  363 434 HOH   HOH A . 
G 4 HOH   64  364 249 HOH   HOH A . 
G 4 HOH   65  365 56  HOH   HOH A . 
G 4 HOH   66  366 338 HOH   HOH A . 
G 4 HOH   67  367 195 HOH   HOH A . 
G 4 HOH   68  368 487 HOH   HOH A . 
G 4 HOH   69  369 136 HOH   HOH A . 
G 4 HOH   70  370 301 HOH   HOH A . 
G 4 HOH   71  371 261 HOH   HOH A . 
G 4 HOH   72  372 504 HOH   HOH A . 
G 4 HOH   73  373 31  HOH   HOH A . 
G 4 HOH   74  374 545 HOH   HOH A . 
G 4 HOH   75  375 82  HOH   HOH A . 
G 4 HOH   76  376 286 HOH   HOH A . 
G 4 HOH   77  377 240 HOH   HOH A . 
G 4 HOH   78  378 279 HOH   HOH A . 
G 4 HOH   79  379 52  HOH   HOH A . 
G 4 HOH   80  380 50  HOH   HOH A . 
G 4 HOH   81  381 160 HOH   HOH A . 
G 4 HOH   82  382 70  HOH   HOH A . 
G 4 HOH   83  383 14  HOH   HOH A . 
G 4 HOH   84  384 167 HOH   HOH A . 
G 4 HOH   85  385 59  HOH   HOH A . 
G 4 HOH   86  386 75  HOH   HOH A . 
G 4 HOH   87  387 28  HOH   HOH A . 
G 4 HOH   88  388 8   HOH   HOH A . 
G 4 HOH   89  389 85  HOH   HOH A . 
G 4 HOH   90  390 161 HOH   HOH A . 
G 4 HOH   91  391 267 HOH   HOH A . 
G 4 HOH   92  392 210 HOH   HOH A . 
G 4 HOH   93  393 174 HOH   HOH A . 
G 4 HOH   94  394 114 HOH   HOH A . 
G 4 HOH   95  395 305 HOH   HOH A . 
G 4 HOH   96  396 204 HOH   HOH A . 
G 4 HOH   97  397 170 HOH   HOH A . 
G 4 HOH   98  398 211 HOH   HOH A . 
G 4 HOH   99  399 268 HOH   HOH A . 
G 4 HOH   100 400 118 HOH   HOH A . 
G 4 HOH   101 401 139 HOH   HOH A . 
G 4 HOH   102 402 458 HOH   HOH A . 
G 4 HOH   103 403 91  HOH   HOH A . 
G 4 HOH   104 404 359 HOH   HOH A . 
G 4 HOH   105 405 164 HOH   HOH A . 
G 4 HOH   106 406 316 HOH   HOH A . 
G 4 HOH   107 407 134 HOH   HOH A . 
G 4 HOH   108 408 368 HOH   HOH A . 
G 4 HOH   109 409 49  HOH   HOH A . 
G 4 HOH   110 410 517 HOH   HOH A . 
G 4 HOH   111 411 546 HOH   HOH A . 
G 4 HOH   112 412 149 HOH   HOH A . 
G 4 HOH   113 413 364 HOH   HOH A . 
G 4 HOH   114 414 363 HOH   HOH A . 
G 4 HOH   115 415 89  HOH   HOH A . 
G 4 HOH   116 416 44  HOH   HOH A . 
G 4 HOH   117 417 218 HOH   HOH A . 
G 4 HOH   118 418 197 HOH   HOH A . 
G 4 HOH   119 419 53  HOH   HOH A . 
G 4 HOH   120 420 79  HOH   HOH A . 
G 4 HOH   121 421 138 HOH   HOH A . 
G 4 HOH   122 422 571 HOH   HOH A . 
G 4 HOH   123 423 162 HOH   HOH A . 
G 4 HOH   124 424 515 HOH   HOH A . 
G 4 HOH   125 425 179 HOH   HOH A . 
G 4 HOH   126 426 94  HOH   HOH A . 
G 4 HOH   127 427 227 HOH   HOH A . 
G 4 HOH   128 428 209 HOH   HOH A . 
G 4 HOH   129 429 157 HOH   HOH A . 
G 4 HOH   130 430 441 HOH   HOH A . 
G 4 HOH   131 431 23  HOH   HOH A . 
G 4 HOH   132 432 102 HOH   HOH A . 
G 4 HOH   133 433 242 HOH   HOH A . 
G 4 HOH   134 434 205 HOH   HOH A . 
G 4 HOH   135 435 21  HOH   HOH A . 
G 4 HOH   136 436 516 HOH   HOH A . 
G 4 HOH   137 437 332 HOH   HOH A . 
G 4 HOH   138 438 234 HOH   HOH A . 
G 4 HOH   139 439 435 HOH   HOH A . 
G 4 HOH   140 440 382 HOH   HOH A . 
G 4 HOH   141 441 263 HOH   HOH A . 
G 4 HOH   142 442 573 HOH   HOH A . 
G 4 HOH   143 443 237 HOH   HOH A . 
G 4 HOH   144 444 514 HOH   HOH A . 
G 4 HOH   145 445 212 HOH   HOH A . 
G 4 HOH   146 446 442 HOH   HOH A . 
G 4 HOH   147 447 399 HOH   HOH A . 
G 4 HOH   148 448 101 HOH   HOH A . 
G 4 HOH   149 449 559 HOH   HOH A . 
G 4 HOH   150 450 258 HOH   HOH A . 
G 4 HOH   151 451 560 HOH   HOH A . 
G 4 HOH   152 452 217 HOH   HOH A . 
G 4 HOH   153 453 310 HOH   HOH A . 
G 4 HOH   154 454 436 HOH   HOH A . 
G 4 HOH   155 455 483 HOH   HOH A . 
G 4 HOH   156 456 96  HOH   HOH A . 
G 4 HOH   157 457 200 HOH   HOH A . 
G 4 HOH   158 458 549 HOH   HOH A . 
G 4 HOH   159 459 111 HOH   HOH A . 
G 4 HOH   160 460 523 HOH   HOH A . 
G 4 HOH   161 461 81  HOH   HOH A . 
G 4 HOH   162 462 274 HOH   HOH A . 
G 4 HOH   163 463 180 HOH   HOH A . 
G 4 HOH   164 464 446 HOH   HOH A . 
G 4 HOH   165 465 92  HOH   HOH A . 
G 4 HOH   166 466 175 HOH   HOH A . 
G 4 HOH   167 467 518 HOH   HOH A . 
G 4 HOH   168 468 190 HOH   HOH A . 
G 4 HOH   169 469 381 HOH   HOH A . 
G 4 HOH   170 470 561 HOH   HOH A . 
G 4 HOH   171 471 135 HOH   HOH A . 
G 4 HOH   172 472 552 HOH   HOH A . 
G 4 HOH   173 473 331 HOH   HOH A . 
G 4 HOH   174 474 444 HOH   HOH A . 
G 4 HOH   175 475 346 HOH   HOH A . 
G 4 HOH   176 476 463 HOH   HOH A . 
G 4 HOH   177 477 428 HOH   HOH A . 
G 4 HOH   178 478 265 HOH   HOH A . 
G 4 HOH   179 479 283 HOH   HOH A . 
G 4 HOH   180 480 326 HOH   HOH A . 
G 4 HOH   181 481 165 HOH   HOH A . 
G 4 HOH   182 482 275 HOH   HOH A . 
G 4 HOH   183 483 525 HOH   HOH A . 
G 4 HOH   184 484 313 HOH   HOH A . 
G 4 HOH   185 485 351 HOH   HOH A . 
G 4 HOH   186 486 540 HOH   HOH A . 
G 4 HOH   187 487 491 HOH   HOH A . 
G 4 HOH   188 488 418 HOH   HOH A . 
G 4 HOH   189 489 112 HOH   HOH A . 
G 4 HOH   190 490 280 HOH   HOH A . 
G 4 HOH   191 491 520 HOH   HOH A . 
G 4 HOH   192 492 271 HOH   HOH A . 
G 4 HOH   193 493 445 HOH   HOH A . 
H 4 HOH   1   301 563 HOH   HOH B . 
H 4 HOH   2   302 498 HOH   HOH B . 
H 4 HOH   3   303 63  HOH   HOH B . 
H 4 HOH   4   304 385 HOH   HOH B . 
H 4 HOH   5   305 397 HOH   HOH B . 
H 4 HOH   6   306 141 HOH   HOH B . 
H 4 HOH   7   307 172 HOH   HOH B . 
H 4 HOH   8   308 37  HOH   HOH B . 
H 4 HOH   9   309 219 HOH   HOH B . 
H 4 HOH   10  310 124 HOH   HOH B . 
H 4 HOH   11  311 90  HOH   HOH B . 
H 4 HOH   12  312 293 HOH   HOH B . 
H 4 HOH   13  313 400 HOH   HOH B . 
H 4 HOH   14  314 39  HOH   HOH B . 
H 4 HOH   15  315 65  HOH   HOH B . 
H 4 HOH   16  316 245 HOH   HOH B . 
H 4 HOH   17  317 126 HOH   HOH B . 
H 4 HOH   18  318 16  HOH   HOH B . 
H 4 HOH   19  319 220 HOH   HOH B . 
H 4 HOH   20  320 4   HOH   HOH B . 
H 4 HOH   21  321 6   HOH   HOH B . 
H 4 HOH   22  322 297 HOH   HOH B . 
H 4 HOH   23  323 98  HOH   HOH B . 
H 4 HOH   24  324 18  HOH   HOH B . 
H 4 HOH   25  325 144 HOH   HOH B . 
H 4 HOH   26  326 398 HOH   HOH B . 
H 4 HOH   27  327 67  HOH   HOH B . 
H 4 HOH   28  328 221 HOH   HOH B . 
H 4 HOH   29  329 449 HOH   HOH B . 
H 4 HOH   30  330 119 HOH   HOH B . 
H 4 HOH   31  331 187 HOH   HOH B . 
H 4 HOH   32  332 10  HOH   HOH B . 
H 4 HOH   33  333 230 HOH   HOH B . 
H 4 HOH   34  334 215 HOH   HOH B . 
H 4 HOH   35  335 40  HOH   HOH B . 
H 4 HOH   36  336 129 HOH   HOH B . 
H 4 HOH   37  337 189 HOH   HOH B . 
H 4 HOH   38  338 567 HOH   HOH B . 
H 4 HOH   39  339 496 HOH   HOH B . 
H 4 HOH   40  340 482 HOH   HOH B . 
H 4 HOH   41  341 97  HOH   HOH B . 
H 4 HOH   42  342 231 HOH   HOH B . 
H 4 HOH   43  343 262 HOH   HOH B . 
H 4 HOH   44  344 156 HOH   HOH B . 
H 4 HOH   45  345 69  HOH   HOH B . 
H 4 HOH   46  346 109 HOH   HOH B . 
H 4 HOH   47  347 479 HOH   HOH B . 
H 4 HOH   48  348 127 HOH   HOH B . 
H 4 HOH   49  349 394 HOH   HOH B . 
H 4 HOH   50  350 5   HOH   HOH B . 
H 4 HOH   51  351 378 HOH   HOH B . 
H 4 HOH   52  352 182 HOH   HOH B . 
H 4 HOH   53  353 473 HOH   HOH B . 
H 4 HOH   54  354 235 HOH   HOH B . 
H 4 HOH   55  355 147 HOH   HOH B . 
H 4 HOH   56  356 306 HOH   HOH B . 
H 4 HOH   57  357 47  HOH   HOH B . 
H 4 HOH   58  358 60  HOH   HOH B . 
H 4 HOH   59  359 11  HOH   HOH B . 
H 4 HOH   60  360 64  HOH   HOH B . 
H 4 HOH   61  361 27  HOH   HOH B . 
H 4 HOH   62  362 13  HOH   HOH B . 
H 4 HOH   63  363 202 HOH   HOH B . 
H 4 HOH   64  364 62  HOH   HOH B . 
H 4 HOH   65  365 390 HOH   HOH B . 
H 4 HOH   66  366 303 HOH   HOH B . 
H 4 HOH   67  367 260 HOH   HOH B . 
H 4 HOH   68  368 29  HOH   HOH B . 
H 4 HOH   69  369 367 HOH   HOH B . 
H 4 HOH   70  370 238 HOH   HOH B . 
H 4 HOH   71  371 541 HOH   HOH B . 
H 4 HOH   72  372 108 HOH   HOH B . 
H 4 HOH   73  373 9   HOH   HOH B . 
H 4 HOH   74  374 121 HOH   HOH B . 
H 4 HOH   75  375 304 HOH   HOH B . 
H 4 HOH   76  376 68  HOH   HOH B . 
H 4 HOH   77  377 222 HOH   HOH B . 
H 4 HOH   78  378 489 HOH   HOH B . 
H 4 HOH   79  379 153 HOH   HOH B . 
H 4 HOH   80  380 327 HOH   HOH B . 
H 4 HOH   81  381 58  HOH   HOH B . 
H 4 HOH   82  382 183 HOH   HOH B . 
H 4 HOH   83  383 12  HOH   HOH B . 
H 4 HOH   84  384 239 HOH   HOH B . 
H 4 HOH   85  385 22  HOH   HOH B . 
H 4 HOH   86  386 95  HOH   HOH B . 
H 4 HOH   87  387 117 HOH   HOH B . 
H 4 HOH   88  388 201 HOH   HOH B . 
H 4 HOH   89  389 84  HOH   HOH B . 
H 4 HOH   90  390 155 HOH   HOH B . 
H 4 HOH   91  391 374 HOH   HOH B . 
H 4 HOH   92  392 76  HOH   HOH B . 
H 4 HOH   93  393 521 HOH   HOH B . 
H 4 HOH   94  394 557 HOH   HOH B . 
H 4 HOH   95  395 116 HOH   HOH B . 
H 4 HOH   96  396 371 HOH   HOH B . 
H 4 HOH   97  397 562 HOH   HOH B . 
H 4 HOH   98  398 329 HOH   HOH B . 
H 4 HOH   99  399 337 HOH   HOH B . 
H 4 HOH   100 400 99  HOH   HOH B . 
H 4 HOH   101 401 493 HOH   HOH B . 
H 4 HOH   102 402 294 HOH   HOH B . 
H 4 HOH   103 403 401 HOH   HOH B . 
H 4 HOH   104 404 272 HOH   HOH B . 
H 4 HOH   105 405 356 HOH   HOH B . 
H 4 HOH   106 406 93  HOH   HOH B . 
H 4 HOH   107 407 361 HOH   HOH B . 
H 4 HOH   108 408 411 HOH   HOH B . 
H 4 HOH   109 409 159 HOH   HOH B . 
H 4 HOH   110 410 266 HOH   HOH B . 
H 4 HOH   111 411 340 HOH   HOH B . 
H 4 HOH   112 412 131 HOH   HOH B . 
H 4 HOH   113 413 72  HOH   HOH B . 
H 4 HOH   114 414 158 HOH   HOH B . 
H 4 HOH   115 415 533 HOH   HOH B . 
H 4 HOH   116 416 224 HOH   HOH B . 
H 4 HOH   117 417 133 HOH   HOH B . 
H 4 HOH   118 418 196 HOH   HOH B . 
H 4 HOH   119 419 77  HOH   HOH B . 
H 4 HOH   120 420 322 HOH   HOH B . 
H 4 HOH   121 421 123 HOH   HOH B . 
H 4 HOH   122 422 150 HOH   HOH B . 
H 4 HOH   123 423 148 HOH   HOH B . 
H 4 HOH   124 424 536 HOH   HOH B . 
H 4 HOH   125 425 569 HOH   HOH B . 
H 4 HOH   126 426 324 HOH   HOH B . 
H 4 HOH   127 427 34  HOH   HOH B . 
H 4 HOH   128 428 509 HOH   HOH B . 
H 4 HOH   129 429 529 HOH   HOH B . 
H 4 HOH   130 430 125 HOH   HOH B . 
H 4 HOH   131 431 485 HOH   HOH B . 
H 4 HOH   132 432 120 HOH   HOH B . 
H 4 HOH   133 433 184 HOH   HOH B . 
H 4 HOH   134 434 198 HOH   HOH B . 
H 4 HOH   135 435 38  HOH   HOH B . 
H 4 HOH   136 436 19  HOH   HOH B . 
H 4 HOH   137 437 519 HOH   HOH B . 
H 4 HOH   138 438 412 HOH   HOH B . 
H 4 HOH   139 439 388 HOH   HOH B . 
H 4 HOH   140 440 128 HOH   HOH B . 
H 4 HOH   141 441 247 HOH   HOH B . 
H 4 HOH   142 442 566 HOH   HOH B . 
H 4 HOH   143 443 565 HOH   HOH B . 
H 4 HOH   144 444 214 HOH   HOH B . 
H 4 HOH   145 445 362 HOH   HOH B . 
H 4 HOH   146 446 415 HOH   HOH B . 
H 4 HOH   147 447 169 HOH   HOH B . 
H 4 HOH   148 448 287 HOH   HOH B . 
H 4 HOH   149 449 20  HOH   HOH B . 
H 4 HOH   150 450 477 HOH   HOH B . 
H 4 HOH   151 451 259 HOH   HOH B . 
H 4 HOH   152 452 132 HOH   HOH B . 
H 4 HOH   153 453 550 HOH   HOH B . 
H 4 HOH   154 454 223 HOH   HOH B . 
H 4 HOH   155 455 438 HOH   HOH B . 
H 4 HOH   156 456 572 HOH   HOH B . 
H 4 HOH   157 457 166 HOH   HOH B . 
H 4 HOH   158 458 450 HOH   HOH B . 
H 4 HOH   159 459 276 HOH   HOH B . 
H 4 HOH   160 460 291 HOH   HOH B . 
H 4 HOH   161 461 264 HOH   HOH B . 
H 4 HOH   162 462 492 HOH   HOH B . 
H 4 HOH   163 463 422 HOH   HOH B . 
H 4 HOH   164 464 369 HOH   HOH B . 
H 4 HOH   165 465 185 HOH   HOH B . 
H 4 HOH   166 466 312 HOH   HOH B . 
H 4 HOH   167 467 430 HOH   HOH B . 
H 4 HOH   168 468 481 HOH   HOH B . 
H 4 HOH   169 469 564 HOH   HOH B . 
H 4 HOH   170 470 457 HOH   HOH B . 
H 4 HOH   171 471 42  HOH   HOH B . 
H 4 HOH   172 472 299 HOH   HOH B . 
H 4 HOH   173 473 232 HOH   HOH B . 
H 4 HOH   174 474 375 HOH   HOH B . 
H 4 HOH   175 475 392 HOH   HOH B . 
H 4 HOH   176 476 309 HOH   HOH B . 
H 4 HOH   177 477 225 HOH   HOH B . 
H 4 HOH   178 478 246 HOH   HOH B . 
H 4 HOH   179 479 307 HOH   HOH B . 
H 4 HOH   180 480 508 HOH   HOH B . 
H 4 HOH   181 481 226 HOH   HOH B . 
H 4 HOH   182 482 320 HOH   HOH B . 
H 4 HOH   183 483 551 HOH   HOH B . 
H 4 HOH   184 484 461 HOH   HOH B . 
H 4 HOH   185 485 558 HOH   HOH B . 
H 4 HOH   186 486 410 HOH   HOH B . 
H 4 HOH   187 487 537 HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A SER 11  ? OG  ? A SER 31  OG  
2  1 Y 1 A GLU 12  ? CG  ? A GLU 32  CG  
3  1 Y 1 A GLU 12  ? CD  ? A GLU 32  CD  
4  1 Y 1 A GLU 12  ? OE1 ? A GLU 32  OE1 
5  1 Y 1 A GLU 12  ? OE2 ? A GLU 32  OE2 
6  1 Y 1 A ASN 13  ? CG  ? A ASN 33  CG  
7  1 Y 1 A ASN 13  ? OD1 ? A ASN 33  OD1 
8  1 Y 1 A ASN 13  ? ND2 ? A ASN 33  ND2 
9  1 Y 1 A ARG 14  ? CG  ? A ARG 34  CG  
10 1 Y 1 A ARG 14  ? CD  ? A ARG 34  CD  
11 1 Y 1 A ARG 14  ? NE  ? A ARG 34  NE  
12 1 Y 1 A ARG 14  ? CZ  ? A ARG 34  CZ  
13 1 Y 1 A ARG 14  ? NH1 ? A ARG 34  NH1 
14 1 Y 1 A ARG 14  ? NH2 ? A ARG 34  NH2 
15 1 Y 1 A GLN 21  ? CD  ? A GLN 41  CD  
16 1 Y 1 A GLN 21  ? OE1 ? A GLN 41  OE1 
17 1 Y 1 A GLN 21  ? NE2 ? A GLN 41  NE2 
18 1 Y 1 A LYS 25  ? CD  ? A LYS 45  CD  
19 1 Y 1 A LYS 25  ? CE  ? A LYS 45  CE  
20 1 Y 1 A LYS 25  ? NZ  ? A LYS 45  NZ  
21 1 Y 1 A LYS 40  ? CE  ? A LYS 60  CE  
22 1 Y 1 A LYS 40  ? NZ  ? A LYS 60  NZ  
23 1 Y 1 A GLU 68  ? CD  ? A GLU 88  CD  
24 1 Y 1 A GLU 68  ? OE1 ? A GLU 88  OE1 
25 1 Y 1 A GLU 68  ? OE2 ? A GLU 88  OE2 
26 1 Y 1 A LYS 69  ? CD  ? A LYS 89  CD  
27 1 Y 1 A LYS 69  ? CE  ? A LYS 89  CE  
28 1 Y 1 A LYS 69  ? NZ  ? A LYS 89  NZ  
29 1 Y 1 A TRP 76  ? CG  ? A TRP 96  CG  
30 1 Y 1 A TRP 76  ? CD1 ? A TRP 96  CD1 
31 1 Y 1 A TRP 76  ? CD2 ? A TRP 96  CD2 
32 1 Y 1 A TRP 76  ? NE1 ? A TRP 96  NE1 
33 1 Y 1 A TRP 76  ? CE2 ? A TRP 96  CE2 
34 1 Y 1 A TRP 76  ? CE3 ? A TRP 96  CE3 
35 1 Y 1 A TRP 76  ? CZ2 ? A TRP 96  CZ2 
36 1 Y 1 A TRP 76  ? CZ3 ? A TRP 96  CZ3 
37 1 Y 1 A TRP 76  ? CH2 ? A TRP 96  CH2 
38 1 Y 1 A GLU 154 ? CD  ? A GLU 174 CD  
39 1 Y 1 A GLU 154 ? OE1 ? A GLU 174 OE1 
40 1 Y 1 A GLU 154 ? OE2 ? A GLU 174 OE2 
41 1 Y 1 A GLU 157 ? CD  ? A GLU 177 CD  
42 1 Y 1 A GLU 157 ? OE1 ? A GLU 177 OE1 
43 1 Y 1 A GLU 157 ? OE2 ? A GLU 177 OE2 
44 1 Y 1 B GLU 12  ? CG  ? B GLU 32  CG  
45 1 Y 1 B GLU 12  ? CD  ? B GLU 32  CD  
46 1 Y 1 B GLU 12  ? OE1 ? B GLU 32  OE1 
47 1 Y 1 B GLU 12  ? OE2 ? B GLU 32  OE2 
48 1 Y 1 B ASN 13  ? CG  ? B ASN 33  CG  
49 1 Y 1 B ASN 13  ? OD1 ? B ASN 33  OD1 
50 1 Y 1 B ASN 13  ? ND2 ? B ASN 33  ND2 
51 1 Y 1 B ARG 14  ? CG  ? B ARG 34  CG  
52 1 Y 1 B ARG 14  ? CD  ? B ARG 34  CD  
53 1 Y 1 B ARG 14  ? NE  ? B ARG 34  NE  
54 1 Y 1 B ARG 14  ? CZ  ? B ARG 34  CZ  
55 1 Y 1 B ARG 14  ? NH1 ? B ARG 34  NH1 
56 1 Y 1 B ARG 14  ? NH2 ? B ARG 34  NH2 
57 1 Y 1 B LYS 25  ? CE  ? B LYS 45  CE  
58 1 Y 1 B LYS 25  ? NZ  ? B LYS 45  NZ  
59 1 Y 1 B GLU 47  ? CD  ? B GLU 67  CD  
60 1 Y 1 B GLU 47  ? OE1 ? B GLU 67  OE1 
61 1 Y 1 B GLU 47  ? OE2 ? B GLU 67  OE2 
62 1 Y 1 B GLU 68  ? CD  ? B GLU 88  CD  
63 1 Y 1 B GLU 68  ? OE1 ? B GLU 88  OE1 
64 1 Y 1 B GLU 68  ? OE2 ? B GLU 88  OE2 
65 1 Y 1 B LYS 69  ? CD  ? B LYS 89  CD  
66 1 Y 1 B LYS 69  ? CE  ? B LYS 89  CE  
67 1 Y 1 B LYS 69  ? NZ  ? B LYS 89  NZ  
68 1 Y 1 B TRP 76  ? CG  ? B TRP 96  CG  
69 1 Y 1 B TRP 76  ? CD1 ? B TRP 96  CD1 
70 1 Y 1 B TRP 76  ? CD2 ? B TRP 96  CD2 
71 1 Y 1 B TRP 76  ? NE1 ? B TRP 96  NE1 
72 1 Y 1 B TRP 76  ? CE2 ? B TRP 96  CE2 
73 1 Y 1 B TRP 76  ? CE3 ? B TRP 96  CE3 
74 1 Y 1 B TRP 76  ? CZ2 ? B TRP 96  CZ2 
75 1 Y 1 B TRP 76  ? CZ3 ? B TRP 96  CZ3 
76 1 Y 1 B TRP 76  ? CH2 ? B TRP 96  CH2 
77 1 Y 1 B GLU 154 ? CG  ? B GLU 174 CG  
78 1 Y 1 B GLU 154 ? CD  ? B GLU 174 CD  
79 1 Y 1 B GLU 154 ? OE1 ? B GLU 174 OE1 
80 1 Y 1 B GLU 154 ? OE2 ? B GLU 174 OE2 
# 
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        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? 'Jan 10, 2022'       2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? v0.7.7               3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? v2.8.3               4 
? 'data processing' ? ? ? ? ? ? ? ? ? ? ? autoPROC    ? ? ? 'v1.0.5 (20211020)'  5 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? v4.2                 6 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   100.72 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9F8N 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     54.016 
_cell.length_a_esd                 ? 
_cell.length_b                     68.849 
_cell.length_b_esd                 ? 
_cell.length_c                     54.170 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9F8N 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 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                   9F8N 
_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             2.38 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.3 
_exptl_crystal.description                  ? 
_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, SITTING DROP' 
_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    '16.7% (w/v) PEG 3350, 0.1 M MES pH 6.48, 6.67% (v/v) glycerol' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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 EIGER2 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         2022-02-24 
_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   1.0332 
_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, DESY BEAMLINE P11' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0332 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   P11 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, DESY' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9F8N 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.32 
_reflns.d_resolution_low                               42.03 
_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                                     90832 
_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                           98.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.89 
_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                                0.043 
_reflns.pdbx_Rpim_I_all                                0.017 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       601099 
_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                              0.040 
_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                                    1.32 
_reflns_shell.d_res_low                                     1.39 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           73865 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             12735 
_reflns_shell.percent_possible_obs                          94.7 
_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                               5.8 
_reflns_shell.pdbx_chi_squared                              0.67 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.9 
_reflns_shell.pdbx_Rrim_I_all                               0.500 
_reflns_shell.pdbx_Rpim_I_all                               0.203 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.938 
_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                                  0.455 
_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]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               27.218 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_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                                 9F8N 
_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                            1.32 
_refine.ls_d_res_low                             42.03 
_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                     90741 
_refine.ls_number_reflns_R_free                  4440 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.31 
_refine.ls_percent_reflns_R_free                 4.89 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1366 
_refine.ls_R_factor_R_free                       0.1604 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1354 
_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                    'FLAT BULK SOLVENT MODEL' 
_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                          1.37 
_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       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 15.69 
_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                             ? 
_refine.overall_SU_ML                            0.14 
_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                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.32 
_refine_hist.d_res_low                        42.03 
_refine_hist.number_atoms_solvent             380 
_refine_hist.number_atoms_total               2932 
_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        2480 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         72 
_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' ? 0.010  ? 2834 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.072  ? 3861 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.972 ? 1019 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.084  ? 359  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.011  ? 516  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_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 
_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 
_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 
'X-RAY DIFFRACTION' 1.32 1.33  . . 133 2547 88.00  . . . . 0.2572 . . . . . . . . . . . 0.2616 
'X-RAY DIFFRACTION' 1.33 1.35  . . 149 2713 92.00  . . . . 0.2301 . . . . . . . . . . . 0.2704 
'X-RAY DIFFRACTION' 1.35 1.36  . . 156 2785 97.00  . . . . 0.1982 . . . . . . . . . . . 0.2384 
'X-RAY DIFFRACTION' 1.36 1.38  . . 178 2863 99.00  . . . . 0.1820 . . . . . . . . . . . 0.2087 
'X-RAY DIFFRACTION' 1.38 1.40  . . 145 2855 99.00  . . . . 0.1693 . . . . . . . . . . . 0.1832 
'X-RAY DIFFRACTION' 1.40 1.42  . . 128 2906 99.00  . . . . 0.1523 . . . . . . . . . . . 0.1639 
'X-RAY DIFFRACTION' 1.42 1.44  . . 136 2926 99.00  . . . . 0.1441 . . . . . . . . . . . 0.1992 
'X-RAY DIFFRACTION' 1.44 1.46  . . 151 2902 99.00  . . . . 0.1361 . . . . . . . . . . . 0.1893 
'X-RAY DIFFRACTION' 1.46 1.48  . . 155 2859 99.00  . . . . 0.1309 . . . . . . . . . . . 0.2153 
'X-RAY DIFFRACTION' 1.48 1.51  . . 187 2916 100.00 . . . . 0.1221 . . . . . . . . . . . 0.1834 
'X-RAY DIFFRACTION' 1.51 1.53  . . 118 2878 99.00  . . . . 0.1146 . . . . . . . . . . . 0.1433 
'X-RAY DIFFRACTION' 1.53 1.56  . . 166 2888 99.00  . . . . 0.1138 . . . . . . . . . . . 0.1424 
'X-RAY DIFFRACTION' 1.56 1.59  . . 141 2913 99.00  . . . . 0.1196 . . . . . . . . . . . 0.1584 
'X-RAY DIFFRACTION' 1.59 1.62  . . 145 2841 98.00  . . . . 0.1110 . . . . . . . . . . . 0.1450 
'X-RAY DIFFRACTION' 1.62 1.66  . . 126 2869 98.00  . . . . 0.1183 . . . . . . . . . . . 0.1398 
'X-RAY DIFFRACTION' 1.66 1.70  . . 145 2902 99.00  . . . . 0.1204 . . . . . . . . . . . 0.1757 
'X-RAY DIFFRACTION' 1.70 1.74  . . 157 2914 99.00  . . . . 0.1217 . . . . . . . . . . . 0.1605 
'X-RAY DIFFRACTION' 1.74 1.79  . . 136 2903 99.00  . . . . 0.1185 . . . . . . . . . . . 0.1508 
'X-RAY DIFFRACTION' 1.79 1.84  . . 141 2914 99.00  . . . . 0.1144 . . . . . . . . . . . 0.1371 
'X-RAY DIFFRACTION' 1.84 1.90  . . 132 2927 99.00  . . . . 0.1133 . . . . . . . . . . . 0.1563 
'X-RAY DIFFRACTION' 1.90 1.97  . . 164 2884 100.00 . . . . 0.1177 . . . . . . . . . . . 0.1391 
'X-RAY DIFFRACTION' 1.97 2.04  . . 168 2899 99.00  . . . . 0.1190 . . . . . . . . . . . 0.1480 
'X-RAY DIFFRACTION' 2.04 2.14  . . 137 2938 99.00  . . . . 0.1217 . . . . . . . . . . . 0.1459 
'X-RAY DIFFRACTION' 2.14 2.25  . . 133 2872 97.00  . . . . 0.1237 . . . . . . . . . . . 0.1625 
'X-RAY DIFFRACTION' 2.25 2.39  . . 179 2856 99.00  . . . . 0.1186 . . . . . . . . . . . 0.1594 
'X-RAY DIFFRACTION' 2.39 2.58  . . 128 2985 100.00 . . . . 0.1230 . . . . . . . . . . . 0.1427 
'X-RAY DIFFRACTION' 2.58 2.83  . . 162 2887 99.00  . . . . 0.1370 . . . . . . . . . . . 0.1420 
'X-RAY DIFFRACTION' 2.83 3.24  . . 139 2923 99.00  . . . . 0.1425 . . . . . . . . . . . 0.1739 
'X-RAY DIFFRACTION' 3.25 4.09  . . 155 2919 99.00  . . . . 0.1354 . . . . . . . . . . . 0.1486 
'X-RAY DIFFRACTION' 4.09 42.03 . . 150 2917 97.00  . . . . 0.1640 . . . . . . . . . . . 0.1801 
# 
_struct.entry_id                     9F8N 
_struct.title                        
;Crystal Structure of PhzA/B from Burkholderia cepacia R18194 in complex with [6-Hydroxy-2-(4-hydroxyphenyl)benzo[b]thiophen-3-yl][2-(isobutylamino)phenyl]methanone
;
_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        9F8N 
_struct_keywords.text            
;pyocyanin, phenazine biosynthesis, virulence, inhibitor, ketosteroid-isomerase, cocrystal, PhzA/B, Burkholderia cepacia, BIOSYNTHETIC PROTEIN
;
_struct_keywords.pdbx_keywords   'BIOSYNTHETIC PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 2 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q396C9_BURL3 
_struct_ref.pdbx_db_accession          Q396C9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSDVESLENTSENRAQVAARQHNRKIVEQYMHTRGEARLKRHLLFTEDGVGGLWTTDSGQPIAIRGREKLGEHAVWSLQC
FPDWVWTDIQIFETQDPNWFWVECRGEGAIVFPGYPRGQYRNHFLHSFRFENGLIKEQREFMNPCEQFRSLGIEVPEVRR
DGLPS
;
_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 9F8N A 21 ? 185 ? Q396C9 1 ? 165 ? 1 165 
2 1 9F8N B 21 ? 185 ? Q396C9 1 ? 165 ? 1 165 
# 
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 9F8N MET A 1  ? UNP Q396C9 ? ? 'initiating methionine' -19 1  
1 9F8N GLY A 2  ? UNP Q396C9 ? ? 'expression tag'        -18 2  
1 9F8N SER A 3  ? UNP Q396C9 ? ? 'expression tag'        -17 3  
1 9F8N SER A 4  ? UNP Q396C9 ? ? 'expression tag'        -16 4  
1 9F8N HIS A 5  ? UNP Q396C9 ? ? 'expression tag'        -15 5  
1 9F8N HIS A 6  ? UNP Q396C9 ? ? 'expression tag'        -14 6  
1 9F8N HIS A 7  ? UNP Q396C9 ? ? 'expression tag'        -13 7  
1 9F8N HIS A 8  ? UNP Q396C9 ? ? 'expression tag'        -12 8  
1 9F8N HIS A 9  ? UNP Q396C9 ? ? 'expression tag'        -11 9  
1 9F8N HIS A 10 ? UNP Q396C9 ? ? 'expression tag'        -10 10 
1 9F8N SER A 11 ? UNP Q396C9 ? ? 'expression tag'        -9  11 
1 9F8N SER A 12 ? UNP Q396C9 ? ? 'expression tag'        -8  12 
1 9F8N GLY A 13 ? UNP Q396C9 ? ? 'expression tag'        -7  13 
1 9F8N LEU A 14 ? UNP Q396C9 ? ? 'expression tag'        -6  14 
1 9F8N VAL A 15 ? UNP Q396C9 ? ? 'expression tag'        -5  15 
1 9F8N PRO A 16 ? UNP Q396C9 ? ? 'expression tag'        -4  16 
1 9F8N ARG A 17 ? UNP Q396C9 ? ? 'expression tag'        -3  17 
1 9F8N GLY A 18 ? UNP Q396C9 ? ? 'expression tag'        -2  18 
1 9F8N SER A 19 ? UNP Q396C9 ? ? 'expression tag'        -1  19 
1 9F8N HIS A 20 ? UNP Q396C9 ? ? 'expression tag'        0   20 
2 9F8N MET B 1  ? UNP Q396C9 ? ? 'initiating methionine' -19 21 
2 9F8N GLY B 2  ? UNP Q396C9 ? ? 'expression tag'        -18 22 
2 9F8N SER B 3  ? UNP Q396C9 ? ? 'expression tag'        -17 23 
2 9F8N SER B 4  ? UNP Q396C9 ? ? 'expression tag'        -16 24 
2 9F8N HIS B 5  ? UNP Q396C9 ? ? 'expression tag'        -15 25 
2 9F8N HIS B 6  ? UNP Q396C9 ? ? 'expression tag'        -14 26 
2 9F8N HIS B 7  ? UNP Q396C9 ? ? 'expression tag'        -13 27 
2 9F8N HIS B 8  ? UNP Q396C9 ? ? 'expression tag'        -12 28 
2 9F8N HIS B 9  ? UNP Q396C9 ? ? 'expression tag'        -11 29 
2 9F8N HIS B 10 ? UNP Q396C9 ? ? 'expression tag'        -10 30 
2 9F8N SER B 11 ? UNP Q396C9 ? ? 'expression tag'        -9  31 
2 9F8N SER B 12 ? UNP Q396C9 ? ? 'expression tag'        -8  32 
2 9F8N GLY B 13 ? UNP Q396C9 ? ? 'expression tag'        -7  33 
2 9F8N LEU B 14 ? UNP Q396C9 ? ? 'expression tag'        -6  34 
2 9F8N VAL B 15 ? UNP Q396C9 ? ? 'expression tag'        -5  35 
2 9F8N PRO B 16 ? UNP Q396C9 ? ? 'expression tag'        -4  36 
2 9F8N ARG B 17 ? UNP Q396C9 ? ? 'expression tag'        -3  37 
2 9F8N GLY B 18 ? UNP Q396C9 ? ? 'expression tag'        -2  38 
2 9F8N SER B 19 ? UNP Q396C9 ? ? 'expression tag'        -1  39 
2 9F8N HIS B 20 ? UNP Q396C9 ? ? 'expression tag'        0   40 
# 
_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)' 6450  ? 
1 MORE         -27   ? 
1 'SSA (A^2)'  13670 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_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]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 SER A 31  ? HIS A 52  ? SER A 11  HIS A 32  1 ? 22 
HELX_P HELX_P2 AA2 ARG A 54  ? LEU A 63  ? ARG A 34  LEU A 43  5 ? 10 
HELX_P HELX_P3 AA3 GLY A 86  ? PHE A 101 ? GLY A 66  PHE A 81  1 ? 16 
HELX_P HELX_P4 AA4 ASN A 163 ? LEU A 171 ? ASN A 143 LEU A 151 1 ? 9  
HELX_P HELX_P5 AA5 ASN B 33  ? THR B 53  ? ASN B 13  THR B 33  1 ? 21 
HELX_P HELX_P6 AA6 ARG B 54  ? LEU B 63  ? ARG B 34  LEU B 43  5 ? 10 
HELX_P HELX_P7 AA7 GLY B 86  ? PHE B 101 ? GLY B 66  PHE B 81  1 ? 16 
HELX_P HELX_P8 AA8 ASN B 163 ? LEU B 171 ? ASN B 143 LEU B 151 1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? 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 ILE A 82  ? ARG A 85  ? ILE A 62  ARG A 65  
AA1 2 PHE A 65  ? LEU A 73  ? PHE A 45  LEU A 53  
AA1 3 LEU A 154 ? PHE A 161 ? LEU A 134 PHE A 141 
AA1 4 GLY A 138 ? GLU A 151 ? GLY A 118 GLU A 131 
AA1 5 TRP A 119 ? ILE A 130 ? TRP A 99  ILE A 110 
AA1 6 VAL A 105 ? GLU A 113 ? VAL A 85  GLU A 93  
AA2 1 ILE B 82  ? ARG B 85  ? ILE B 62  ARG B 65  
AA2 2 PHE B 65  ? LEU B 73  ? PHE B 45  LEU B 53  
AA2 3 LEU B 154 ? PHE B 161 ? LEU B 134 PHE B 141 
AA2 4 GLY B 138 ? GLU B 151 ? GLY B 118 GLU B 131 
AA2 5 TRP B 119 ? ILE B 130 ? TRP B 99  ILE B 110 
AA2 6 VAL B 105 ? PHE B 112 ? VAL B 85  PHE B 92  
# 
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 O ILE A 84  ? O ILE A 64  N GLY A 71  ? N GLY A 51  
AA1 2 3 N VAL A 70  ? N VAL A 50  O GLN A 158 ? O GLN A 138 
AA1 3 4 O LYS A 156 ? O LYS A 136 N ARG A 149 ? N ARG A 129 
AA1 4 5 O TYR A 140 ? O TYR A 120 N GLY A 128 ? N GLY A 108 
AA1 5 6 O TRP A 121 ? O TRP A 101 N PHE A 112 ? N PHE A 92  
AA2 1 2 O ILE B 84  ? O ILE B 64  N GLY B 71  ? N GLY B 51  
AA2 2 3 N VAL B 70  ? N VAL B 50  O GLN B 158 ? O GLN B 138 
AA2 3 4 O LYS B 156 ? O LYS B 136 N ARG B 149 ? N ARG B 129 
AA2 4 5 O TYR B 140 ? O TYR B 120 N GLY B 128 ? N GLY B 108 
AA2 5 6 O TRP B 121 ? O TRP B 101 N PHE B 112 ? N PHE B 92  
# 
_pdbx_entry_details.entry_id                   9F8N 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_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 O A HOH 424 ? ? O A HOH 436 ? ? 1.93 
2 1 O A HOH 410 ? ? O A HOH 412 ? ? 1.96 
3 1 O A HOH 424 ? ? O A HOH 444 ? ? 1.97 
4 1 O B HOH 394 ? ? O B HOH 408 ? ? 2.05 
5 1 O A HOH 302 ? ? O A HOH 424 ? ? 2.09 
6 1 O B HOH 440 ? ? O B HOH 446 ? ? 2.12 
7 1 O A HOH 432 ? ? O A HOH 443 ? ? 2.15 
8 1 O A HOH 339 ? ? O A HOH 430 ? ? 2.15 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     422 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     456 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_546 
_pdbx_validate_symm_contact.dist              2.02 
# 
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 MET -19 ? A MET 1   
2  1 Y 1 A GLY -18 ? A GLY 2   
3  1 Y 1 A SER -17 ? A SER 3   
4  1 Y 1 A SER -16 ? A SER 4   
5  1 Y 1 A HIS -15 ? A HIS 5   
6  1 Y 1 A HIS -14 ? A HIS 6   
7  1 Y 1 A HIS -13 ? A HIS 7   
8  1 Y 1 A HIS -12 ? A HIS 8   
9  1 Y 1 A HIS -11 ? A HIS 9   
10 1 Y 1 A HIS -10 ? A HIS 10  
11 1 Y 1 A SER -9  ? A SER 11  
12 1 Y 1 A SER -8  ? A SER 12  
13 1 Y 1 A GLY -7  ? A GLY 13  
14 1 Y 1 A LEU -6  ? A LEU 14  
15 1 Y 1 A VAL -5  ? A VAL 15  
16 1 Y 1 A PRO -4  ? A PRO 16  
17 1 Y 1 A ARG -3  ? A ARG 17  
18 1 Y 1 A GLY -2  ? A GLY 18  
19 1 Y 1 A SER -1  ? A SER 19  
20 1 Y 1 A HIS 0   ? A HIS 20  
21 1 Y 1 A MET 1   ? A MET 21  
22 1 Y 1 A SER 2   ? A SER 22  
23 1 Y 1 A ASP 3   ? A ASP 23  
24 1 Y 1 A VAL 4   ? A VAL 24  
25 1 Y 1 A GLU 5   ? A GLU 25  
26 1 Y 1 A SER 6   ? A SER 26  
27 1 Y 1 A LEU 7   ? A LEU 27  
28 1 Y 1 A GLU 8   ? A GLU 28  
29 1 Y 1 A ASN 9   ? A ASN 29  
30 1 Y 1 A THR 10  ? A THR 30  
31 1 Y 1 A SER 165 ? A SER 185 
32 1 Y 1 B MET -19 ? B MET 1   
33 1 Y 1 B GLY -18 ? B GLY 2   
34 1 Y 1 B SER -17 ? B SER 3   
35 1 Y 1 B SER -16 ? B SER 4   
36 1 Y 1 B HIS -15 ? B HIS 5   
37 1 Y 1 B HIS -14 ? B HIS 6   
38 1 Y 1 B HIS -13 ? B HIS 7   
39 1 Y 1 B HIS -12 ? B HIS 8   
40 1 Y 1 B HIS -11 ? B HIS 9   
41 1 Y 1 B HIS -10 ? B HIS 10  
42 1 Y 1 B SER -9  ? B SER 11  
43 1 Y 1 B SER -8  ? B SER 12  
44 1 Y 1 B GLY -7  ? B GLY 13  
45 1 Y 1 B LEU -6  ? B LEU 14  
46 1 Y 1 B VAL -5  ? B VAL 15  
47 1 Y 1 B PRO -4  ? B PRO 16  
48 1 Y 1 B ARG -3  ? B ARG 17  
49 1 Y 1 B GLY -2  ? B GLY 18  
50 1 Y 1 B SER -1  ? B SER 19  
51 1 Y 1 B HIS 0   ? B HIS 20  
52 1 Y 1 B MET 1   ? B MET 21  
53 1 Y 1 B SER 2   ? B SER 22  
54 1 Y 1 B ASP 3   ? B ASP 23  
55 1 Y 1 B VAL 4   ? B VAL 24  
56 1 Y 1 B GLU 5   ? B GLU 25  
57 1 Y 1 B SER 6   ? B SER 26  
58 1 Y 1 B LEU 7   ? B LEU 27  
59 1 Y 1 B GLU 8   ? B GLU 28  
60 1 Y 1 B ASN 9   ? B ASN 29  
61 1 Y 1 B THR 10  ? B THR 30  
62 1 Y 1 B SER 11  ? B SER 31  
63 1 Y 1 B SER 165 ? B SER 185 
# 
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 
A1IAD C10  C Y N 1   
A1IAD C15  C Y N 2   
A1IAD C11  C Y N 3   
A1IAD C12  C N N 4   
A1IAD C14  C Y N 5   
A1IAD C01  C N N 6   
A1IAD C02  C N N 7   
A1IAD C03  C N N 8   
A1IAD C04  C N N 9   
A1IAD C06  C Y N 10  
A1IAD C07  C Y N 11  
A1IAD C08  C Y N 12  
A1IAD C09  C Y N 13  
A1IAD C16  C Y N 14  
A1IAD C17  C Y N 15  
A1IAD C18  C Y N 16  
A1IAD C19  C Y N 17  
A1IAD C21  C Y N 18  
A1IAD C22  C Y N 19  
A1IAD C24  C Y N 20  
A1IAD C25  C Y N 21  
A1IAD C26  C Y N 22  
A1IAD C28  C Y N 23  
A1IAD C29  C Y N 24  
A1IAD C30  C Y N 25  
A1IAD N05  N N N 26  
A1IAD O13  O N N 27  
A1IAD O20  O N N 28  
A1IAD O27  O N N 29  
A1IAD S23  S Y N 30  
A1IAD H101 H N N 31  
A1IAD H011 H N N 32  
A1IAD H012 H N N 33  
A1IAD H013 H N N 34  
A1IAD H021 H N N 35  
A1IAD H033 H N N 36  
A1IAD H032 H N N 37  
A1IAD H031 H N N 38  
A1IAD H041 H N N 39  
A1IAD H042 H N N 40  
A1IAD H071 H N N 41  
A1IAD H081 H N N 42  
A1IAD H091 H N N 43  
A1IAD H171 H N N 44  
A1IAD H181 H N N 45  
A1IAD H211 H N N 46  
A1IAD H221 H N N 47  
A1IAD H251 H N N 48  
A1IAD H281 H N N 49  
A1IAD H291 H N N 50  
A1IAD H051 H N N 51  
A1IAD H201 H N N 52  
A1IAD H271 H N N 53  
ALA   N    N N N 54  
ALA   CA   C N S 55  
ALA   C    C N N 56  
ALA   O    O N N 57  
ALA   CB   C N N 58  
ALA   OXT  O N N 59  
ALA   H    H N N 60  
ALA   H2   H N N 61  
ALA   HA   H N N 62  
ALA   HB1  H N N 63  
ALA   HB2  H N N 64  
ALA   HB3  H N N 65  
ALA   HXT  H N N 66  
ARG   N    N N N 67  
ARG   CA   C N S 68  
ARG   C    C N N 69  
ARG   O    O N N 70  
ARG   CB   C N N 71  
ARG   CG   C N N 72  
ARG   CD   C N N 73  
ARG   NE   N N N 74  
ARG   CZ   C N N 75  
ARG   NH1  N N N 76  
ARG   NH2  N N N 77  
ARG   OXT  O N N 78  
ARG   H    H N N 79  
ARG   H2   H N N 80  
ARG   HA   H N N 81  
ARG   HB2  H N N 82  
ARG   HB3  H N N 83  
ARG   HG2  H N N 84  
ARG   HG3  H N N 85  
ARG   HD2  H N N 86  
ARG   HD3  H N N 87  
ARG   HE   H N N 88  
ARG   HH11 H N N 89  
ARG   HH12 H N N 90  
ARG   HH21 H N N 91  
ARG   HH22 H N N 92  
ARG   HXT  H N N 93  
ASN   N    N N N 94  
ASN   CA   C N S 95  
ASN   C    C N N 96  
ASN   O    O N N 97  
ASN   CB   C N N 98  
ASN   CG   C N N 99  
ASN   OD1  O N N 100 
ASN   ND2  N N N 101 
ASN   OXT  O N N 102 
ASN   H    H N N 103 
ASN   H2   H N N 104 
ASN   HA   H N N 105 
ASN   HB2  H N N 106 
ASN   HB3  H N N 107 
ASN   HD21 H N N 108 
ASN   HD22 H N N 109 
ASN   HXT  H N N 110 
ASP   N    N N N 111 
ASP   CA   C N S 112 
ASP   C    C N N 113 
ASP   O    O N N 114 
ASP   CB   C N N 115 
ASP   CG   C N N 116 
ASP   OD1  O N N 117 
ASP   OD2  O N N 118 
ASP   OXT  O N N 119 
ASP   H    H N N 120 
ASP   H2   H N N 121 
ASP   HA   H N N 122 
ASP   HB2  H N N 123 
ASP   HB3  H N N 124 
ASP   HD2  H N N 125 
ASP   HXT  H N N 126 
CYS   N    N N N 127 
CYS   CA   C N R 128 
CYS   C    C N N 129 
CYS   O    O N N 130 
CYS   CB   C N N 131 
CYS   SG   S N N 132 
CYS   OXT  O N N 133 
CYS   H    H N N 134 
CYS   H2   H N N 135 
CYS   HA   H N N 136 
CYS   HB2  H N N 137 
CYS   HB3  H N N 138 
CYS   HG   H N N 139 
CYS   HXT  H N N 140 
GLN   N    N N N 141 
GLN   CA   C N S 142 
GLN   C    C N N 143 
GLN   O    O N N 144 
GLN   CB   C N N 145 
GLN   CG   C N N 146 
GLN   CD   C N N 147 
GLN   OE1  O N N 148 
GLN   NE2  N N N 149 
GLN   OXT  O N N 150 
GLN   H    H N N 151 
GLN   H2   H N N 152 
GLN   HA   H N N 153 
GLN   HB2  H N N 154 
GLN   HB3  H N N 155 
GLN   HG2  H N N 156 
GLN   HG3  H N N 157 
GLN   HE21 H N N 158 
GLN   HE22 H N N 159 
GLN   HXT  H N N 160 
GLU   N    N N N 161 
GLU   CA   C N S 162 
GLU   C    C N N 163 
GLU   O    O N N 164 
GLU   CB   C N N 165 
GLU   CG   C N N 166 
GLU   CD   C N N 167 
GLU   OE1  O N N 168 
GLU   OE2  O N N 169 
GLU   OXT  O N N 170 
GLU   H    H N N 171 
GLU   H2   H N N 172 
GLU   HA   H N N 173 
GLU   HB2  H N N 174 
GLU   HB3  H N N 175 
GLU   HG2  H N N 176 
GLU   HG3  H N N 177 
GLU   HE2  H N N 178 
GLU   HXT  H N N 179 
GLY   N    N N N 180 
GLY   CA   C N N 181 
GLY   C    C N N 182 
GLY   O    O N N 183 
GLY   OXT  O N N 184 
GLY   H    H N N 185 
GLY   H2   H N N 186 
GLY   HA2  H N N 187 
GLY   HA3  H N N 188 
GLY   HXT  H N N 189 
GOL   C1   C N N 190 
GOL   O1   O N N 191 
GOL   C2   C N N 192 
GOL   O2   O N N 193 
GOL   C3   C N N 194 
GOL   O3   O N N 195 
GOL   H11  H N N 196 
GOL   H12  H N N 197 
GOL   HO1  H N N 198 
GOL   H2   H N N 199 
GOL   HO2  H N N 200 
GOL   H31  H N N 201 
GOL   H32  H N N 202 
GOL   HO3  H N N 203 
HIS   N    N N N 204 
HIS   CA   C N S 205 
HIS   C    C N N 206 
HIS   O    O N N 207 
HIS   CB   C N N 208 
HIS   CG   C Y N 209 
HIS   ND1  N Y N 210 
HIS   CD2  C Y N 211 
HIS   CE1  C Y N 212 
HIS   NE2  N Y N 213 
HIS   OXT  O N N 214 
HIS   H    H N N 215 
HIS   H2   H N N 216 
HIS   HA   H N N 217 
HIS   HB2  H N N 218 
HIS   HB3  H N N 219 
HIS   HD1  H N N 220 
HIS   HD2  H N N 221 
HIS   HE1  H N N 222 
HIS   HE2  H N N 223 
HIS   HXT  H N N 224 
HOH   O    O N N 225 
HOH   H1   H N N 226 
HOH   H2   H N N 227 
ILE   N    N N N 228 
ILE   CA   C N S 229 
ILE   C    C N N 230 
ILE   O    O N N 231 
ILE   CB   C N S 232 
ILE   CG1  C N N 233 
ILE   CG2  C N N 234 
ILE   CD1  C N N 235 
ILE   OXT  O N N 236 
ILE   H    H N N 237 
ILE   H2   H N N 238 
ILE   HA   H N N 239 
ILE   HB   H N N 240 
ILE   HG12 H N N 241 
ILE   HG13 H N N 242 
ILE   HG21 H N N 243 
ILE   HG22 H N N 244 
ILE   HG23 H N N 245 
ILE   HD11 H N N 246 
ILE   HD12 H N N 247 
ILE   HD13 H N N 248 
ILE   HXT  H N N 249 
LEU   N    N N N 250 
LEU   CA   C N S 251 
LEU   C    C N N 252 
LEU   O    O N N 253 
LEU   CB   C N N 254 
LEU   CG   C N N 255 
LEU   CD1  C N N 256 
LEU   CD2  C N N 257 
LEU   OXT  O N N 258 
LEU   H    H N N 259 
LEU   H2   H N N 260 
LEU   HA   H N N 261 
LEU   HB2  H N N 262 
LEU   HB3  H N N 263 
LEU   HG   H N N 264 
LEU   HD11 H N N 265 
LEU   HD12 H N N 266 
LEU   HD13 H N N 267 
LEU   HD21 H N N 268 
LEU   HD22 H N N 269 
LEU   HD23 H N N 270 
LEU   HXT  H N N 271 
LYS   N    N N N 272 
LYS   CA   C N S 273 
LYS   C    C N N 274 
LYS   O    O N N 275 
LYS   CB   C N N 276 
LYS   CG   C N N 277 
LYS   CD   C N N 278 
LYS   CE   C N N 279 
LYS   NZ   N N N 280 
LYS   OXT  O N N 281 
LYS   H    H N N 282 
LYS   H2   H N N 283 
LYS   HA   H N N 284 
LYS   HB2  H N N 285 
LYS   HB3  H N N 286 
LYS   HG2  H N N 287 
LYS   HG3  H N N 288 
LYS   HD2  H N N 289 
LYS   HD3  H N N 290 
LYS   HE2  H N N 291 
LYS   HE3  H N N 292 
LYS   HZ1  H N N 293 
LYS   HZ2  H N N 294 
LYS   HZ3  H N N 295 
LYS   HXT  H N N 296 
MET   N    N N N 297 
MET   CA   C N S 298 
MET   C    C N N 299 
MET   O    O N N 300 
MET   CB   C N N 301 
MET   CG   C N N 302 
MET   SD   S N N 303 
MET   CE   C N N 304 
MET   OXT  O N N 305 
MET   H    H N N 306 
MET   H2   H N N 307 
MET   HA   H N N 308 
MET   HB2  H N N 309 
MET   HB3  H N N 310 
MET   HG2  H N N 311 
MET   HG3  H N N 312 
MET   HE1  H N N 313 
MET   HE2  H N N 314 
MET   HE3  H N N 315 
MET   HXT  H N N 316 
PHE   N    N N N 317 
PHE   CA   C N S 318 
PHE   C    C N N 319 
PHE   O    O N N 320 
PHE   CB   C N N 321 
PHE   CG   C Y N 322 
PHE   CD1  C Y N 323 
PHE   CD2  C Y N 324 
PHE   CE1  C Y N 325 
PHE   CE2  C Y N 326 
PHE   CZ   C Y N 327 
PHE   OXT  O N N 328 
PHE   H    H N N 329 
PHE   H2   H N N 330 
PHE   HA   H N N 331 
PHE   HB2  H N N 332 
PHE   HB3  H N N 333 
PHE   HD1  H N N 334 
PHE   HD2  H N N 335 
PHE   HE1  H N N 336 
PHE   HE2  H N N 337 
PHE   HZ   H N N 338 
PHE   HXT  H N N 339 
PRO   N    N N N 340 
PRO   CA   C N S 341 
PRO   C    C N N 342 
PRO   O    O N N 343 
PRO   CB   C N N 344 
PRO   CG   C N N 345 
PRO   CD   C N N 346 
PRO   OXT  O N N 347 
PRO   H    H N N 348 
PRO   HA   H N N 349 
PRO   HB2  H N N 350 
PRO   HB3  H N N 351 
PRO   HG2  H N N 352 
PRO   HG3  H N N 353 
PRO   HD2  H N N 354 
PRO   HD3  H N N 355 
PRO   HXT  H N N 356 
SER   N    N N N 357 
SER   CA   C N S 358 
SER   C    C N N 359 
SER   O    O N N 360 
SER   CB   C N N 361 
SER   OG   O N N 362 
SER   OXT  O N N 363 
SER   H    H N N 364 
SER   H2   H N N 365 
SER   HA   H N N 366 
SER   HB2  H N N 367 
SER   HB3  H N N 368 
SER   HG   H N N 369 
SER   HXT  H N N 370 
THR   N    N N N 371 
THR   CA   C N S 372 
THR   C    C N N 373 
THR   O    O N N 374 
THR   CB   C N R 375 
THR   OG1  O N N 376 
THR   CG2  C N N 377 
THR   OXT  O N N 378 
THR   H    H N N 379 
THR   H2   H N N 380 
THR   HA   H N N 381 
THR   HB   H N N 382 
THR   HG1  H N N 383 
THR   HG21 H N N 384 
THR   HG22 H N N 385 
THR   HG23 H N N 386 
THR   HXT  H N N 387 
TRP   N    N N N 388 
TRP   CA   C N S 389 
TRP   C    C N N 390 
TRP   O    O N N 391 
TRP   CB   C N N 392 
TRP   CG   C Y N 393 
TRP   CD1  C Y N 394 
TRP   CD2  C Y N 395 
TRP   NE1  N Y N 396 
TRP   CE2  C Y N 397 
TRP   CE3  C Y N 398 
TRP   CZ2  C Y N 399 
TRP   CZ3  C Y N 400 
TRP   CH2  C Y N 401 
TRP   OXT  O N N 402 
TRP   H    H N N 403 
TRP   H2   H N N 404 
TRP   HA   H N N 405 
TRP   HB2  H N N 406 
TRP   HB3  H N N 407 
TRP   HD1  H N N 408 
TRP   HE1  H N N 409 
TRP   HE3  H N N 410 
TRP   HZ2  H N N 411 
TRP   HZ3  H N N 412 
TRP   HH2  H N N 413 
TRP   HXT  H N N 414 
TYR   N    N N N 415 
TYR   CA   C N S 416 
TYR   C    C N N 417 
TYR   O    O N N 418 
TYR   CB   C N N 419 
TYR   CG   C Y N 420 
TYR   CD1  C Y N 421 
TYR   CD2  C Y N 422 
TYR   CE1  C Y N 423 
TYR   CE2  C Y N 424 
TYR   CZ   C Y N 425 
TYR   OH   O N N 426 
TYR   OXT  O N N 427 
TYR   H    H N N 428 
TYR   H2   H N N 429 
TYR   HA   H N N 430 
TYR   HB2  H N N 431 
TYR   HB3  H N N 432 
TYR   HD1  H N N 433 
TYR   HD2  H N N 434 
TYR   HE1  H N N 435 
TYR   HE2  H N N 436 
TYR   HH   H N N 437 
TYR   HXT  H N N 438 
VAL   N    N N N 439 
VAL   CA   C N S 440 
VAL   C    C N N 441 
VAL   O    O N N 442 
VAL   CB   C N N 443 
VAL   CG1  C N N 444 
VAL   CG2  C N N 445 
VAL   OXT  O N N 446 
VAL   H    H N N 447 
VAL   H2   H N N 448 
VAL   HA   H N N 449 
VAL   HB   H N N 450 
VAL   HG11 H N N 451 
VAL   HG12 H N N 452 
VAL   HG13 H N N 453 
VAL   HG21 H N N 454 
VAL   HG22 H N N 455 
VAL   HG23 H N N 456 
VAL   HXT  H N N 457 
# 
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 
A1IAD C03 C02  sing N N 1   
A1IAD C08 C07  doub Y N 2   
A1IAD C08 C09  sing Y N 3   
A1IAD O20 C19  sing N N 4   
A1IAD C07 C06  sing Y N 5   
A1IAD C09 C10  doub Y N 6   
A1IAD C02 C04  sing N N 7   
A1IAD C02 C01  sing N N 8   
A1IAD C04 N05  sing N N 9   
A1IAD C19 C18  doub Y N 10  
A1IAD C19 C21  sing Y N 11  
A1IAD C18 C17  sing Y N 12  
A1IAD C06 N05  sing N N 13  
A1IAD C06 C11  doub Y N 14  
A1IAD C10 C11  sing Y N 15  
A1IAD C21 C22  doub Y N 16  
A1IAD C11 C12  sing N N 17  
A1IAD C17 C16  doub Y N 18  
A1IAD C22 C16  sing Y N 19  
A1IAD C16 C15  sing N N 20  
A1IAD C12 O13  doub N N 21  
A1IAD C12 C14  sing N N 22  
A1IAD C15 C14  doub Y N 23  
A1IAD C15 S23  sing Y N 24  
A1IAD C14 C30  sing Y N 25  
A1IAD C30 C29  doub Y N 26  
A1IAD C30 C24  sing Y N 27  
A1IAD S23 C24  sing Y N 28  
A1IAD C29 C28  sing Y N 29  
A1IAD C24 C25  doub Y N 30  
A1IAD C28 C26  doub Y N 31  
A1IAD C25 C26  sing Y N 32  
A1IAD C26 O27  sing N N 33  
A1IAD C10 H101 sing N N 34  
A1IAD C01 H011 sing N N 35  
A1IAD C01 H012 sing N N 36  
A1IAD C01 H013 sing N N 37  
A1IAD C02 H021 sing N N 38  
A1IAD C03 H033 sing N N 39  
A1IAD C03 H032 sing N N 40  
A1IAD C03 H031 sing N N 41  
A1IAD C04 H041 sing N N 42  
A1IAD C04 H042 sing N N 43  
A1IAD C07 H071 sing N N 44  
A1IAD C08 H081 sing N N 45  
A1IAD C09 H091 sing N N 46  
A1IAD C17 H171 sing N N 47  
A1IAD C18 H181 sing N N 48  
A1IAD C21 H211 sing N N 49  
A1IAD C22 H221 sing N N 50  
A1IAD C25 H251 sing N N 51  
A1IAD C28 H281 sing N N 52  
A1IAD C29 H291 sing N N 53  
A1IAD N05 H051 sing N N 54  
A1IAD O20 H201 sing N N 55  
A1IAD O27 H271 sing N N 56  
ALA   N   CA   sing N N 57  
ALA   N   H    sing N N 58  
ALA   N   H2   sing N N 59  
ALA   CA  C    sing N N 60  
ALA   CA  CB   sing N N 61  
ALA   CA  HA   sing N N 62  
ALA   C   O    doub N N 63  
ALA   C   OXT  sing N N 64  
ALA   CB  HB1  sing N N 65  
ALA   CB  HB2  sing N N 66  
ALA   CB  HB3  sing N N 67  
ALA   OXT HXT  sing N N 68  
ARG   N   CA   sing N N 69  
ARG   N   H    sing N N 70  
ARG   N   H2   sing N N 71  
ARG   CA  C    sing N N 72  
ARG   CA  CB   sing N N 73  
ARG   CA  HA   sing N N 74  
ARG   C   O    doub N N 75  
ARG   C   OXT  sing N N 76  
ARG   CB  CG   sing N N 77  
ARG   CB  HB2  sing N N 78  
ARG   CB  HB3  sing N N 79  
ARG   CG  CD   sing N N 80  
ARG   CG  HG2  sing N N 81  
ARG   CG  HG3  sing N N 82  
ARG   CD  NE   sing N N 83  
ARG   CD  HD2  sing N N 84  
ARG   CD  HD3  sing N N 85  
ARG   NE  CZ   sing N N 86  
ARG   NE  HE   sing N N 87  
ARG   CZ  NH1  sing N N 88  
ARG   CZ  NH2  doub N N 89  
ARG   NH1 HH11 sing N N 90  
ARG   NH1 HH12 sing N N 91  
ARG   NH2 HH21 sing N N 92  
ARG   NH2 HH22 sing N N 93  
ARG   OXT HXT  sing N N 94  
ASN   N   CA   sing N N 95  
ASN   N   H    sing N N 96  
ASN   N   H2   sing N N 97  
ASN   CA  C    sing N N 98  
ASN   CA  CB   sing N N 99  
ASN   CA  HA   sing N N 100 
ASN   C   O    doub N N 101 
ASN   C   OXT  sing N N 102 
ASN   CB  CG   sing N N 103 
ASN   CB  HB2  sing N N 104 
ASN   CB  HB3  sing N N 105 
ASN   CG  OD1  doub N N 106 
ASN   CG  ND2  sing N N 107 
ASN   ND2 HD21 sing N N 108 
ASN   ND2 HD22 sing N N 109 
ASN   OXT HXT  sing N N 110 
ASP   N   CA   sing N N 111 
ASP   N   H    sing N N 112 
ASP   N   H2   sing N N 113 
ASP   CA  C    sing N N 114 
ASP   CA  CB   sing N N 115 
ASP   CA  HA   sing N N 116 
ASP   C   O    doub N N 117 
ASP   C   OXT  sing N N 118 
ASP   CB  CG   sing N N 119 
ASP   CB  HB2  sing N N 120 
ASP   CB  HB3  sing N N 121 
ASP   CG  OD1  doub N N 122 
ASP   CG  OD2  sing N N 123 
ASP   OD2 HD2  sing N N 124 
ASP   OXT HXT  sing N N 125 
CYS   N   CA   sing N N 126 
CYS   N   H    sing N N 127 
CYS   N   H2   sing N N 128 
CYS   CA  C    sing N N 129 
CYS   CA  CB   sing N N 130 
CYS   CA  HA   sing N N 131 
CYS   C   O    doub N N 132 
CYS   C   OXT  sing N N 133 
CYS   CB  SG   sing N N 134 
CYS   CB  HB2  sing N N 135 
CYS   CB  HB3  sing N N 136 
CYS   SG  HG   sing N N 137 
CYS   OXT HXT  sing N N 138 
GLN   N   CA   sing N N 139 
GLN   N   H    sing N N 140 
GLN   N   H2   sing N N 141 
GLN   CA  C    sing N N 142 
GLN   CA  CB   sing N N 143 
GLN   CA  HA   sing N N 144 
GLN   C   O    doub N N 145 
GLN   C   OXT  sing N N 146 
GLN   CB  CG   sing N N 147 
GLN   CB  HB2  sing N N 148 
GLN   CB  HB3  sing N N 149 
GLN   CG  CD   sing N N 150 
GLN   CG  HG2  sing N N 151 
GLN   CG  HG3  sing N N 152 
GLN   CD  OE1  doub N N 153 
GLN   CD  NE2  sing N N 154 
GLN   NE2 HE21 sing N N 155 
GLN   NE2 HE22 sing N N 156 
GLN   OXT HXT  sing N N 157 
GLU   N   CA   sing N N 158 
GLU   N   H    sing N N 159 
GLU   N   H2   sing N N 160 
GLU   CA  C    sing N N 161 
GLU   CA  CB   sing N N 162 
GLU   CA  HA   sing N N 163 
GLU   C   O    doub N N 164 
GLU   C   OXT  sing N N 165 
GLU   CB  CG   sing N N 166 
GLU   CB  HB2  sing N N 167 
GLU   CB  HB3  sing N N 168 
GLU   CG  CD   sing N N 169 
GLU   CG  HG2  sing N N 170 
GLU   CG  HG3  sing N N 171 
GLU   CD  OE1  doub N N 172 
GLU   CD  OE2  sing N N 173 
GLU   OE2 HE2  sing N N 174 
GLU   OXT HXT  sing N N 175 
GLY   N   CA   sing N N 176 
GLY   N   H    sing N N 177 
GLY   N   H2   sing N N 178 
GLY   CA  C    sing N N 179 
GLY   CA  HA2  sing N N 180 
GLY   CA  HA3  sing N N 181 
GLY   C   O    doub N N 182 
GLY   C   OXT  sing N N 183 
GLY   OXT HXT  sing N N 184 
GOL   C1  O1   sing N N 185 
GOL   C1  C2   sing N N 186 
GOL   C1  H11  sing N N 187 
GOL   C1  H12  sing N N 188 
GOL   O1  HO1  sing N N 189 
GOL   C2  O2   sing N N 190 
GOL   C2  C3   sing N N 191 
GOL   C2  H2   sing N N 192 
GOL   O2  HO2  sing N N 193 
GOL   C3  O3   sing N N 194 
GOL   C3  H31  sing N N 195 
GOL   C3  H32  sing N N 196 
GOL   O3  HO3  sing N N 197 
HIS   N   CA   sing N N 198 
HIS   N   H    sing N N 199 
HIS   N   H2   sing N N 200 
HIS   CA  C    sing N N 201 
HIS   CA  CB   sing N N 202 
HIS   CA  HA   sing N N 203 
HIS   C   O    doub N N 204 
HIS   C   OXT  sing N N 205 
HIS   CB  CG   sing N N 206 
HIS   CB  HB2  sing N N 207 
HIS   CB  HB3  sing N N 208 
HIS   CG  ND1  sing Y N 209 
HIS   CG  CD2  doub Y N 210 
HIS   ND1 CE1  doub Y N 211 
HIS   ND1 HD1  sing N N 212 
HIS   CD2 NE2  sing Y N 213 
HIS   CD2 HD2  sing N N 214 
HIS   CE1 NE2  sing Y N 215 
HIS   CE1 HE1  sing N N 216 
HIS   NE2 HE2  sing N N 217 
HIS   OXT HXT  sing N N 218 
HOH   O   H1   sing N N 219 
HOH   O   H2   sing N N 220 
ILE   N   CA   sing N N 221 
ILE   N   H    sing N N 222 
ILE   N   H2   sing N N 223 
ILE   CA  C    sing N N 224 
ILE   CA  CB   sing N N 225 
ILE   CA  HA   sing N N 226 
ILE   C   O    doub N N 227 
ILE   C   OXT  sing N N 228 
ILE   CB  CG1  sing N N 229 
ILE   CB  CG2  sing N N 230 
ILE   CB  HB   sing N N 231 
ILE   CG1 CD1  sing N N 232 
ILE   CG1 HG12 sing N N 233 
ILE   CG1 HG13 sing N N 234 
ILE   CG2 HG21 sing N N 235 
ILE   CG2 HG22 sing N N 236 
ILE   CG2 HG23 sing N N 237 
ILE   CD1 HD11 sing N N 238 
ILE   CD1 HD12 sing N N 239 
ILE   CD1 HD13 sing N N 240 
ILE   OXT HXT  sing N N 241 
LEU   N   CA   sing N N 242 
LEU   N   H    sing N N 243 
LEU   N   H2   sing N N 244 
LEU   CA  C    sing N N 245 
LEU   CA  CB   sing N N 246 
LEU   CA  HA   sing N N 247 
LEU   C   O    doub N N 248 
LEU   C   OXT  sing N N 249 
LEU   CB  CG   sing N N 250 
LEU   CB  HB2  sing N N 251 
LEU   CB  HB3  sing N N 252 
LEU   CG  CD1  sing N N 253 
LEU   CG  CD2  sing N N 254 
LEU   CG  HG   sing N N 255 
LEU   CD1 HD11 sing N N 256 
LEU   CD1 HD12 sing N N 257 
LEU   CD1 HD13 sing N N 258 
LEU   CD2 HD21 sing N N 259 
LEU   CD2 HD22 sing N N 260 
LEU   CD2 HD23 sing N N 261 
LEU   OXT HXT  sing N N 262 
LYS   N   CA   sing N N 263 
LYS   N   H    sing N N 264 
LYS   N   H2   sing N N 265 
LYS   CA  C    sing N N 266 
LYS   CA  CB   sing N N 267 
LYS   CA  HA   sing N N 268 
LYS   C   O    doub N N 269 
LYS   C   OXT  sing N N 270 
LYS   CB  CG   sing N N 271 
LYS   CB  HB2  sing N N 272 
LYS   CB  HB3  sing N N 273 
LYS   CG  CD   sing N N 274 
LYS   CG  HG2  sing N N 275 
LYS   CG  HG3  sing N N 276 
LYS   CD  CE   sing N N 277 
LYS   CD  HD2  sing N N 278 
LYS   CD  HD3  sing N N 279 
LYS   CE  NZ   sing N N 280 
LYS   CE  HE2  sing N N 281 
LYS   CE  HE3  sing N N 282 
LYS   NZ  HZ1  sing N N 283 
LYS   NZ  HZ2  sing N N 284 
LYS   NZ  HZ3  sing N N 285 
LYS   OXT HXT  sing N N 286 
MET   N   CA   sing N N 287 
MET   N   H    sing N N 288 
MET   N   H2   sing N N 289 
MET   CA  C    sing N N 290 
MET   CA  CB   sing N N 291 
MET   CA  HA   sing N N 292 
MET   C   O    doub N N 293 
MET   C   OXT  sing N N 294 
MET   CB  CG   sing N N 295 
MET   CB  HB2  sing N N 296 
MET   CB  HB3  sing N N 297 
MET   CG  SD   sing N N 298 
MET   CG  HG2  sing N N 299 
MET   CG  HG3  sing N N 300 
MET   SD  CE   sing N N 301 
MET   CE  HE1  sing N N 302 
MET   CE  HE2  sing N N 303 
MET   CE  HE3  sing N N 304 
MET   OXT HXT  sing N N 305 
PHE   N   CA   sing N N 306 
PHE   N   H    sing N N 307 
PHE   N   H2   sing N N 308 
PHE   CA  C    sing N N 309 
PHE   CA  CB   sing N N 310 
PHE   CA  HA   sing N N 311 
PHE   C   O    doub N N 312 
PHE   C   OXT  sing N N 313 
PHE   CB  CG   sing N N 314 
PHE   CB  HB2  sing N N 315 
PHE   CB  HB3  sing N N 316 
PHE   CG  CD1  doub Y N 317 
PHE   CG  CD2  sing Y N 318 
PHE   CD1 CE1  sing Y N 319 
PHE   CD1 HD1  sing N N 320 
PHE   CD2 CE2  doub Y N 321 
PHE   CD2 HD2  sing N N 322 
PHE   CE1 CZ   doub Y N 323 
PHE   CE1 HE1  sing N N 324 
PHE   CE2 CZ   sing Y N 325 
PHE   CE2 HE2  sing N N 326 
PHE   CZ  HZ   sing N N 327 
PHE   OXT HXT  sing N N 328 
PRO   N   CA   sing N N 329 
PRO   N   CD   sing N N 330 
PRO   N   H    sing N N 331 
PRO   CA  C    sing N N 332 
PRO   CA  CB   sing N N 333 
PRO   CA  HA   sing N N 334 
PRO   C   O    doub N N 335 
PRO   C   OXT  sing N N 336 
PRO   CB  CG   sing N N 337 
PRO   CB  HB2  sing N N 338 
PRO   CB  HB3  sing N N 339 
PRO   CG  CD   sing N N 340 
PRO   CG  HG2  sing N N 341 
PRO   CG  HG3  sing N N 342 
PRO   CD  HD2  sing N N 343 
PRO   CD  HD3  sing N N 344 
PRO   OXT HXT  sing N N 345 
SER   N   CA   sing N N 346 
SER   N   H    sing N N 347 
SER   N   H2   sing N N 348 
SER   CA  C    sing N N 349 
SER   CA  CB   sing N N 350 
SER   CA  HA   sing N N 351 
SER   C   O    doub N N 352 
SER   C   OXT  sing N N 353 
SER   CB  OG   sing N N 354 
SER   CB  HB2  sing N N 355 
SER   CB  HB3  sing N N 356 
SER   OG  HG   sing N N 357 
SER   OXT HXT  sing N N 358 
THR   N   CA   sing N N 359 
THR   N   H    sing N N 360 
THR   N   H2   sing N N 361 
THR   CA  C    sing N N 362 
THR   CA  CB   sing N N 363 
THR   CA  HA   sing N N 364 
THR   C   O    doub N N 365 
THR   C   OXT  sing N N 366 
THR   CB  OG1  sing N N 367 
THR   CB  CG2  sing N N 368 
THR   CB  HB   sing N N 369 
THR   OG1 HG1  sing N N 370 
THR   CG2 HG21 sing N N 371 
THR   CG2 HG22 sing N N 372 
THR   CG2 HG23 sing N N 373 
THR   OXT HXT  sing N N 374 
TRP   N   CA   sing N N 375 
TRP   N   H    sing N N 376 
TRP   N   H2   sing N N 377 
TRP   CA  C    sing N N 378 
TRP   CA  CB   sing N N 379 
TRP   CA  HA   sing N N 380 
TRP   C   O    doub N N 381 
TRP   C   OXT  sing N N 382 
TRP   CB  CG   sing N N 383 
TRP   CB  HB2  sing N N 384 
TRP   CB  HB3  sing N N 385 
TRP   CG  CD1  doub Y N 386 
TRP   CG  CD2  sing Y N 387 
TRP   CD1 NE1  sing Y N 388 
TRP   CD1 HD1  sing N N 389 
TRP   CD2 CE2  doub Y N 390 
TRP   CD2 CE3  sing Y N 391 
TRP   NE1 CE2  sing Y N 392 
TRP   NE1 HE1  sing N N 393 
TRP   CE2 CZ2  sing Y N 394 
TRP   CE3 CZ3  doub Y N 395 
TRP   CE3 HE3  sing N N 396 
TRP   CZ2 CH2  doub Y N 397 
TRP   CZ2 HZ2  sing N N 398 
TRP   CZ3 CH2  sing Y N 399 
TRP   CZ3 HZ3  sing N N 400 
TRP   CH2 HH2  sing N N 401 
TRP   OXT HXT  sing N N 402 
TYR   N   CA   sing N N 403 
TYR   N   H    sing N N 404 
TYR   N   H2   sing N N 405 
TYR   CA  C    sing N N 406 
TYR   CA  CB   sing N N 407 
TYR   CA  HA   sing N N 408 
TYR   C   O    doub N N 409 
TYR   C   OXT  sing N N 410 
TYR   CB  CG   sing N N 411 
TYR   CB  HB2  sing N N 412 
TYR   CB  HB3  sing N N 413 
TYR   CG  CD1  doub Y N 414 
TYR   CG  CD2  sing Y N 415 
TYR   CD1 CE1  sing Y N 416 
TYR   CD1 HD1  sing N N 417 
TYR   CD2 CE2  doub Y N 418 
TYR   CD2 HD2  sing N N 419 
TYR   CE1 CZ   doub Y N 420 
TYR   CE1 HE1  sing N N 421 
TYR   CE2 CZ   sing Y N 422 
TYR   CE2 HE2  sing N N 423 
TYR   CZ  OH   sing N N 424 
TYR   OH  HH   sing N N 425 
TYR   OXT HXT  sing N N 426 
VAL   N   CA   sing N N 427 
VAL   N   H    sing N N 428 
VAL   N   H2   sing N N 429 
VAL   CA  C    sing N N 430 
VAL   CA  CB   sing N N 431 
VAL   CA  HA   sing N N 432 
VAL   C   O    doub N N 433 
VAL   C   OXT  sing N N 434 
VAL   CB  CG1  sing N N 435 
VAL   CB  CG2  sing N N 436 
VAL   CB  HB   sing N N 437 
VAL   CG1 HG11 sing N N 438 
VAL   CG1 HG12 sing N N 439 
VAL   CG1 HG13 sing N N 440 
VAL   CG2 HG21 sing N N 441 
VAL   CG2 HG22 sing N N 442 
VAL   CG2 HG23 sing N N 443 
VAL   OXT HXT  sing N N 444 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_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   3EX9 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9F8N 
_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]   0.018513 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003505 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014525 
_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]   0.018788 
_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 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    . SER   A 1 31  ? -16.697 24.941 -5.548 1.00 62.77 ? 11  SER   A N    1 
ATOM   2    C CA   . SER   A 1 31  ? -16.984 23.756 -4.743 1.00 61.04 ? 11  SER   A CA   1 
ATOM   3    C C    . SER   A 1 31  ? -16.203 23.769 -3.428 1.00 55.44 ? 11  SER   A C    1 
ATOM   4    O O    . SER   A 1 31  ? -15.220 23.029 -3.252 1.00 52.32 ? 11  SER   A O    1 
ATOM   5    C CB   . SER   A 1 31  ? -16.643 22.485 -5.525 1.00 63.79 ? 11  SER   A CB   1 
ATOM   6    H HA   . SER   A 1 31  ? -17.931 23.748 -4.532 1.00 73.25 ? 11  SER   A HA   1 
ATOM   7    N N    . GLU   A 1 32  ? -16.649 24.622 -2.505 1.00 52.21 ? 12  GLU   A N    1 
ATOM   8    C CA   . GLU   A 1 32  ? -15.998 24.718 -1.203 1.00 50.59 ? 12  GLU   A CA   1 
ATOM   9    C C    . GLU   A 1 32  ? -16.032 23.376 -0.482 1.00 48.54 ? 12  GLU   A C    1 
ATOM   10   O O    . GLU   A 1 32  ? -15.011 22.905 0.030  1.00 47.29 ? 12  GLU   A O    1 
ATOM   11   C CB   . GLU   A 1 32  ? -16.679 25.807 -0.371 1.00 51.67 ? 12  GLU   A CB   1 
ATOM   12   H H    . GLU   A 1 32  ? -17.321 25.150 -2.607 1.00 62.65 ? 12  GLU   A H    1 
ATOM   13   H HA   . GLU   A 1 32  ? -15.068 24.967 -1.322 1.00 60.71 ? 12  GLU   A HA   1 
ATOM   14   N N    . ASN   A 1 33  ? -17.200 22.727 -0.454 1.00 49.70 ? 13  ASN   A N    1 
ATOM   15   C CA   . ASN   A 1 33  ? -17.310 21.457 0.258  1.00 49.02 ? 13  ASN   A CA   1 
ATOM   16   C C    . ASN   A 1 33  ? -16.411 20.400 -0.377 1.00 46.51 ? 13  ASN   A C    1 
ATOM   17   O O    . ASN   A 1 33  ? -15.737 19.642 0.327  1.00 44.24 ? 13  ASN   A O    1 
ATOM   18   C CB   . ASN   A 1 33  ? -18.761 20.975 0.286  1.00 51.37 ? 13  ASN   A CB   1 
ATOM   19   H H    . ASN   A 1 33  ? -17.925 22.996 -0.831 1.00 59.65 ? 13  ASN   A H    1 
ATOM   20   H HA   . ASN   A 1 33  ? -17.029 21.593 1.176  1.00 58.82 ? 13  ASN   A HA   1 
ATOM   21   N N    . ARG   A 1 34  ? -16.400 20.326 -1.711 1.00 44.87 ? 14  ARG   A N    1 
ATOM   22   C CA   . ARG   A 1 34  ? -15.541 19.359 -2.388 1.00 42.90 ? 14  ARG   A CA   1 
ATOM   23   C C    . ARG   A 1 34  ? -14.075 19.582 -2.030 1.00 39.25 ? 14  ARG   A C    1 
ATOM   24   O O    . ARG   A 1 34  ? -13.334 18.625 -1.783 1.00 38.00 ? 14  ARG   A O    1 
ATOM   25   C CB   . ARG   A 1 34  ? -15.738 19.444 -3.901 1.00 45.03 ? 14  ARG   A CB   1 
ATOM   26   H H    . ARG   A 1 34  ? -16.874 20.815 -2.237 1.00 53.85 ? 14  ARG   A H    1 
ATOM   27   H HA   . ARG   A 1 34  ? -15.791 18.467 -2.102 1.00 51.48 ? 14  ARG   A HA   1 
ATOM   28   N N    . ALA   A 1 35  ? -13.639 20.841 -1.998 1.00 36.69 ? 15  ALA   A N    1 
ATOM   29   C CA   . ALA   A 1 35  ? -12.261 21.133 -1.622 1.00 35.45 ? 15  ALA   A CA   1 
ATOM   30   C C    . ALA   A 1 35  ? -11.973 20.735 -0.176 1.00 32.51 ? 15  ALA   A C    1 
ATOM   31   O O    . ALA   A 1 35  ? -10.906 20.196 0.137  1.00 31.03 ? 15  ALA   A O    1 
ATOM   32   C CB   . ALA   A 1 35  ? -11.982 22.618 -1.847 1.00 37.67 ? 15  ALA   A CB   1 
ATOM   33   H H    . ALA   A 1 35  ? -14.114 21.533 -2.188 1.00 44.03 ? 15  ALA   A H    1 
ATOM   34   H HA   . ALA   A 1 35  ? -11.661 20.619 -2.184 1.00 42.54 ? 15  ALA   A HA   1 
ATOM   35   H HB1  . ALA   A 1 35  ? -11.063 22.808 -1.603 1.00 45.20 ? 15  ALA   A HB1  1 
ATOM   36   H HB2  . ALA   A 1 35  ? -12.125 22.828 -2.783 1.00 45.20 ? 15  ALA   A HB2  1 
ATOM   37   H HB3  . ALA   A 1 35  ? -12.585 23.140 -1.295 1.00 45.20 ? 15  ALA   A HB3  1 
ATOM   38   N N    . GLN   A 1 36  ? -12.906 20.996 0.723  1.00 32.57 ? 16  GLN   A N    1 
ATOM   39   C CA   . GLN   A 1 36  ? -12.687 20.606 2.106  1.00 33.13 ? 16  GLN   A CA   1 
ATOM   40   C C    . GLN   A 1 36  ? -12.635 19.095 2.257  1.00 31.29 ? 16  GLN   A C    1 
ATOM   41   O O    . GLN   A 1 36  ? -11.813 18.574 3.015  1.00 30.64 ? 16  GLN   A O    1 
ATOM   42   C CB   . GLN   A 1 36  ? -13.794 21.194 2.959  0.88 35.35 ? 16  GLN   A CB   1 
ATOM   43   C CG   . GLN   A 1 36  ? -13.718 22.703 3.068  1.00 41.29 ? 16  GLN   A CG   1 
ATOM   44   C CD   . GLN   A 1 36  ? -14.828 23.262 3.908  0.59 45.94 ? 16  GLN   A CD   1 
ATOM   45   O OE1  . GLN   A 1 36  ? -14.740 23.265 5.132  0.66 48.66 ? 16  GLN   A OE1  1 
ATOM   46   N NE2  . GLN   A 1 36  ? -15.899 23.714 3.261  0.54 46.89 ? 16  GLN   A NE2  1 
ATOM   47   H H    . GLN   A 1 36  ? -13.656 21.386 0.565  1.00 39.09 ? 16  GLN   A H    1 
ATOM   48   H HA   . GLN   A 1 36  ? -11.835 20.956 2.411  1.00 39.75 ? 16  GLN   A HA   1 
ATOM   49   H HB2  . GLN   A 1 36  ? -14.651 20.965 2.565  0.88 42.42 ? 16  GLN   A HB2  1 
ATOM   50   H HB3  . GLN   A 1 36  ? -13.732 20.826 3.854  0.88 42.42 ? 16  GLN   A HB3  1 
ATOM   51   H HG2  . GLN   A 1 36  ? -12.874 22.952 3.476  1.00 49.56 ? 16  GLN   A HG2  1 
ATOM   52   H HG3  . GLN   A 1 36  ? -13.784 23.091 2.181  1.00 49.56 ? 16  GLN   A HG3  1 
ATOM   53   H HE21 . GLN   A 1 36  ? -15.930 23.677 2.402  0.54 56.27 ? 16  GLN   A HE21 1 
ATOM   54   H HE22 . GLN   A 1 36  ? -16.560 24.043 3.701  0.54 56.27 ? 16  GLN   A HE22 1 
ATOM   55   N N    . VAL   A 1 37  ? -13.511 18.376 1.565  1.00 32.11 ? 17  VAL   A N    1 
ATOM   56   C CA   . VAL   A 1 37  ? -13.515 16.920 1.656  1.00 33.52 ? 17  VAL   A CA   1 
ATOM   57   C C    . VAL   A 1 37  ? -12.195 16.352 1.150  1.00 32.49 ? 17  VAL   A C    1 
ATOM   58   O O    . VAL   A 1 37  ? -11.597 15.474 1.785  1.00 32.83 ? 17  VAL   A O    1 
ATOM   59   C CB   . VAL   A 1 37  ? -14.729 16.351 0.898  1.00 38.23 ? 17  VAL   A CB   1 
ATOM   60   C CG1  . VAL   A 1 37  ? -14.628 14.834 0.775  1.00 40.58 ? 17  VAL   A CG1  1 
ATOM   61   C CG2  . VAL   A 1 37  ? -16.010 16.751 1.604  1.00 38.87 ? 17  VAL   A CG2  1 
ATOM   62   H H    . VAL   A 1 37  ? -14.109 18.703 1.040  1.00 38.53 ? 17  VAL   A H    1 
ATOM   63   H HA   . VAL   A 1 37  ? -13.601 16.660 2.586  1.00 40.22 ? 17  VAL   A HA   1 
ATOM   64   H HB   . VAL   A 1 37  ? -14.744 16.717 -0.000 1.00 45.88 ? 17  VAL   A HB   1 
ATOM   65   H HG11 . VAL   A 1 37  ? -15.495 14.480 0.524  1.00 48.70 ? 17  VAL   A HG11 1 
ATOM   66   H HG12 . VAL   A 1 37  ? -13.971 14.615 0.096  1.00 48.70 ? 17  VAL   A HG12 1 
ATOM   67   H HG13 . VAL   A 1 37  ? -14.355 14.466 1.630  1.00 48.70 ? 17  VAL   A HG13 1 
ATOM   68   H HG21 . VAL   A 1 37  ? -16.767 16.493 1.055  1.00 46.64 ? 17  VAL   A HG21 1 
ATOM   69   H HG22 . VAL   A 1 37  ? -16.053 16.298 2.461  1.00 46.64 ? 17  VAL   A HG22 1 
ATOM   70   H HG23 . VAL   A 1 37  ? -16.010 17.712 1.738  1.00 46.64 ? 17  VAL   A HG23 1 
ATOM   71   N N    . ALA   A 1 38  ? -11.702 16.871 0.018  1.00 29.51 ? 18  ALA   A N    1 
ATOM   72   C CA   . ALA   A 1 38  ? -10.443 16.387 -0.543 1.00 28.73 ? 18  ALA   A CA   1 
ATOM   73   C C    . ALA   A 1 38  ? -9.287  16.644 0.406  1.00 26.60 ? 18  ALA   A C    1 
ATOM   74   O O    . ALA   A 1 38  ? -8.405  15.791 0.579  1.00 26.97 ? 18  ALA   A O    1 
ATOM   75   C CB   . ALA   A 1 38  ? -10.174 17.103 -1.859 1.00 29.04 ? 18  ALA   A CB   1 
ATOM   76   H H    . ALA   A 1 38  ? -12.075 17.498 -0.438 1.00 35.41 ? 18  ALA   A H    1 
ATOM   77   H HA   . ALA   A 1 38  ? -10.514 15.432 -0.698 1.00 34.48 ? 18  ALA   A HA   1 
ATOM   78   H HB1  . ALA   A 1 38  ? -9.333  16.785 -2.225 1.00 34.85 ? 18  ALA   A HB1  1 
ATOM   79   H HB2  . ALA   A 1 38  ? -10.897 16.911 -2.477 1.00 34.85 ? 18  ALA   A HB2  1 
ATOM   80   H HB3  . ALA   A 1 38  ? -10.124 18.057 -1.695 1.00 34.85 ? 18  ALA   A HB3  1 
ATOM   81   N N    . ALA   A 1 39  ? -9.254  17.832 1.004  1.00 24.72 ? 19  ALA   A N    1 
ATOM   82   C CA   . ALA   A 1 39  ? -8.187  18.144 1.936  1.00 24.77 ? 19  ALA   A CA   1 
ATOM   83   C C    . ALA   A 1 39  ? -8.231  17.184 3.110  1.00 24.30 ? 19  ALA   A C    1 
ATOM   84   O O    . ALA   A 1 39  ? -7.202  16.659 3.539  1.00 23.81 ? 19  ALA   A O    1 
ATOM   85   C CB   . ALA   A 1 39  ? -8.314  19.585 2.416  1.00 26.43 ? 19  ALA   A CB   1 
ATOM   86   H H    . ALA   A 1 39  ? -9.829  18.462 0.887  1.00 29.66 ? 19  ALA   A H    1 
ATOM   87   H HA   . ALA   A 1 39  ? -7.330  18.057 1.489  1.00 29.73 ? 19  ALA   A HA   1 
ATOM   88   H HB1  . ALA   A 1 39  ? -7.603  19.771 3.048  1.00 31.71 ? 19  ALA   A HB1  1 
ATOM   89   H HB2  . ALA   A 1 39  ? -8.243  20.179 1.653  1.00 31.71 ? 19  ALA   A HB2  1 
ATOM   90   H HB3  . ALA   A 1 39  ? -9.177  19.699 2.845  1.00 31.71 ? 19  ALA   A HB3  1 
ATOM   91   N N    . ARG   A 1 40  ? -9.420  16.971 3.677  1.00 24.76 ? 20  ARG   A N    1 
ATOM   92   C CA   . ARG   A 1 40  ? -9.501  16.123 4.863  1.00 23.88 ? 20  ARG   A CA   1 
ATOM   93   C C    . ARG   A 1 40  ? -9.065  14.687 4.569  1.00 23.64 ? 20  ARG   A C    1 
ATOM   94   O O    . ARG   A 1 40  ? -8.322  14.085 5.355  1.00 24.36 ? 20  ARG   A O    1 
ATOM   95   C CB   . ARG   A 1 40  ? -10.914 16.188 5.429  1.00 25.13 ? 20  ARG   A CB   1 
ATOM   96   C CG   . ARG   A 1 40  ? -11.066 15.397 6.706  1.00 25.45 ? 20  ARG   A CG   1 
ATOM   97   C CD   . ARG   A 1 40  ? -12.496 15.471 7.279  1.00 25.81 ? 20  ARG   A CD   1 
ATOM   98   N NE   . ARG   A 1 40  ? -12.823 16.781 7.832  1.00 26.87 ? 20  ARG   A NE   1 
ATOM   99   C CZ   . ARG   A 1 40  ? -13.599 17.681 7.245  1.00 27.01 ? 20  ARG   A CZ   1 
ATOM   100  N NH1  . ARG   A 1 40  ? -14.149 17.452 6.069  1.00 28.54 ? 20  ARG   A NH1  1 
ATOM   101  N NH2  . ARG   A 1 40  ? -13.835 18.833 7.863  1.00 27.26 ? 20  ARG   A NH2  1 
ATOM   102  H H    . ARG   A 1 40  ? -10.168 17.294 3.403  1.00 29.71 ? 20  ARG   A H    1 
ATOM   103  H HA   . ARG   A 1 40  ? -8.892  16.456 5.541  1.00 28.65 ? 20  ARG   A HA   1 
ATOM   104  H HB2  . ARG   A 1 40  ? -11.136 17.113 5.621  1.00 30.16 ? 20  ARG   A HB2  1 
ATOM   105  H HB3  . ARG   A 1 40  ? -11.534 15.827 4.776  1.00 30.16 ? 20  ARG   A HB3  1 
ATOM   106  H HG2  . ARG   A 1 40  ? -10.861 14.465 6.529  1.00 30.54 ? 20  ARG   A HG2  1 
ATOM   107  H HG3  . ARG   A 1 40  ? -10.456 15.750 7.373  1.00 30.54 ? 20  ARG   A HG3  1 
ATOM   108  H HD2  . ARG   A 1 40  ? -13.130 15.280 6.570  1.00 30.98 ? 20  ARG   A HD2  1 
ATOM   109  H HD3  . ARG   A 1 40  ? -12.585 14.817 7.989  1.00 30.98 ? 20  ARG   A HD3  1 
ATOM   110  H HE   . ARG   A 1 40  ? -12.487 16.984 8.597  1.00 32.25 ? 20  ARG   A HE   1 
ATOM   111  H HH11 . ARG   A 1 40  ? -14.007 16.706 5.666  1.00 34.25 ? 20  ARG   A HH11 1 
ATOM   112  H HH12 . ARG   A 1 40  ? -14.649 18.049 5.705  1.00 34.25 ? 20  ARG   A HH12 1 
ATOM   113  H HH21 . ARG   A 1 40  ? -13.486 18.987 8.633  1.00 32.71 ? 20  ARG   A HH21 1 
ATOM   114  H HH22 . ARG   A 1 40  ? -14.337 19.425 7.492  1.00 32.71 ? 20  ARG   A HH22 1 
ATOM   115  N N    . GLN   A 1 41  ? -9.431  14.151 3.407  1.00 23.31 ? 21  GLN   A N    1 
ATOM   116  C CA   . GLN   A 1 41  ? -9.069  12.774 3.102  1.00 22.04 ? 21  GLN   A CA   1 
ATOM   117  C C    . GLN   A 1 41  ? -7.562  12.633 2.909  1.00 23.29 ? 21  GLN   A C    1 
ATOM   118  O O    . GLN   A 1 41  ? -6.956  11.650 3.363  1.00 23.87 ? 21  GLN   A O    1 
ATOM   119  C CB   . GLN   A 1 41  ? -9.801  12.308 1.856  1.00 28.50 ? 21  GLN   A CB   1 
ATOM   120  C CG   . GLN   A 1 41  ? -11.312 12.304 2.040  1.00 37.59 ? 21  GLN   A CG   1 
ATOM   121  H H    . GLN   A 1 41  ? -9.879  14.554 2.794  1.00 27.97 ? 21  GLN   A H    1 
ATOM   122  H HA   . GLN   A 1 41  ? -9.337  12.209 3.844  1.00 26.44 ? 21  GLN   A HA   1 
ATOM   123  H HB2  . GLN   A 1 41  ? -9.588  12.904 1.121  1.00 34.20 ? 21  GLN   A HB2  1 
ATOM   124  H HB3  . GLN   A 1 41  ? -9.521  11.404 1.643  1.00 34.20 ? 21  GLN   A HB3  1 
ATOM   125  N N    . HIS   A 1 42  ? -6.942  13.601 2.221  1.00 22.51 ? 22  HIS   A N    1 
ATOM   126  C CA   . HIS   A 1 42  ? -5.499  13.552 2.055  1.00 19.64 ? 22  HIS   A CA   1 
ATOM   127  C C    . HIS   A 1 42  ? -4.794  13.727 3.387  1.00 19.37 ? 22  HIS   A C    1 
ATOM   128  O O    . HIS   A 1 42  ? -3.869  12.979 3.711  1.00 19.62 ? 22  HIS   A O    1 
ATOM   129  C CB   . HIS   A 1 42  ? -5.060  14.648 1.094  1.00 21.37 ? 22  HIS   A CB   1 
ATOM   130  C CG   . HIS   A 1 42  ? -3.601  14.874 1.126  1.00 21.87 ? 22  HIS   A CG   1 
ATOM   131  N ND1  . HIS   A 1 42  ? -2.712  14.055 0.463  1.00 23.93 ? 22  HIS   A ND1  1 
ATOM   132  C CD2  . HIS   A 1 42  ? -2.865  15.766 1.818  1.00 20.88 ? 22  HIS   A CD2  1 
ATOM   133  C CE1  . HIS   A 1 42  ? -1.485  14.459 0.730  1.00 22.48 ? 22  HIS   A CE1  1 
ATOM   134  N NE2  . HIS   A 1 42  ? -1.547  15.505 1.535  1.00 22.71 ? 22  HIS   A NE2  1 
ATOM   135  H H    . HIS   A 1 42  ? -7.330  14.276 1.854  1.00 27.01 ? 22  HIS   A H    1 
ATOM   136  H HA   . HIS   A 1 42  ? -5.254  12.689 1.685  1.00 23.57 ? 22  HIS   A HA   1 
ATOM   137  H HB2  . HIS   A 1 42  ? -5.307  14.395 0.191  1.00 25.64 ? 22  HIS   A HB2  1 
ATOM   138  H HB3  . HIS   A 1 42  ? -5.500  15.477 1.338  1.00 25.64 ? 22  HIS   A HB3  1 
ATOM   139  H HD2  . HIS   A 1 42  ? -3.189  16.432 2.380  1.00 25.06 ? 22  HIS   A HD2  1 
ATOM   140  H HE1  . HIS   A 1 42  ? -0.704  14.071 0.406  1.00 26.98 ? 22  HIS   A HE1  1 
ATOM   141  H HE2  . HIS   A 1 42  ? -0.873  15.949 1.832  1.00 27.25 ? 22  HIS   A HE2  1 
ATOM   142  N N    . ASN   A 1 43  ? -5.225  14.729 4.168  1.00 19.50 ? 23  ASN   A N    1 
ATOM   143  C CA   . ASN   A 1 43  ? -4.559  14.995 5.433  1.00 19.85 ? 23  ASN   A CA   1 
ATOM   144  C C    . ASN   A 1 43  ? -4.658  13.799 6.373  1.00 19.27 ? 23  ASN   A C    1 
ATOM   145  O O    . ASN   A 1 43  ? -3.704  13.498 7.101  1.00 19.14 ? 23  ASN   A O    1 
ATOM   146  C CB   . ASN   A 1 43  ? -5.151  16.237 6.103  1.00 20.01 ? 23  ASN   A CB   1 
ATOM   147  C CG   . ASN   A 1 43  ? -4.900  17.514 5.324  1.00 20.38 ? 23  ASN   A CG   1 
ATOM   148  O OD1  . ASN   A 1 43  ? -4.011  17.594 4.473  1.00 21.29 ? 23  ASN   A OD1  1 
ATOM   149  N ND2  . ASN   A 1 43  ? -5.671  18.540 5.648  1.00 22.54 ? 23  ASN   A ND2  1 
ATOM   150  H H    . ASN   A 1 43  ? -5.883  15.251 3.986  1.00 23.40 ? 23  ASN   A H    1 
ATOM   151  H HA   . ASN   A 1 43  ? -3.622  15.169 5.251  1.00 23.82 ? 23  ASN   A HA   1 
ATOM   152  H HB2  . ASN   A 1 43  ? -6.110  16.122 6.186  1.00 24.02 ? 23  ASN   A HB2  1 
ATOM   153  H HB3  . ASN   A 1 43  ? -4.752  16.340 6.981  1.00 24.02 ? 23  ASN   A HB3  1 
ATOM   154  H HD21 . ASN   A 1 43  ? -5.578  19.293 5.242  1.00 27.05 ? 23  ASN   A HD21 1 
ATOM   155  H HD22 . ASN   A 1 43  ? -6.265  18.455 6.264  1.00 27.05 ? 23  ASN   A HD22 1 
ATOM   156  N N    A ARG   A 1 44  ? -5.795  13.103 6.366  0.45 20.95 ? 24  ARG   A N    1 
ATOM   157  N N    B ARG   A 1 44  ? -5.800  13.099 6.369  0.55 19.47 ? 24  ARG   A N    1 
ATOM   158  C CA   A ARG   A 1 44  ? -5.915  11.917 7.204  0.45 22.21 ? 24  ARG   A CA   1 
ATOM   159  C CA   B ARG   A 1 44  ? -5.933  11.898 7.191  0.55 19.62 ? 24  ARG   A CA   1 
ATOM   160  C C    A ARG   A 1 44  ? -4.858  10.881 6.842  0.45 21.59 ? 24  ARG   A C    1 
ATOM   161  C C    B ARG   A 1 44  ? -4.877  10.858 6.831  0.55 19.55 ? 24  ARG   A C    1 
ATOM   162  O O    A ARG   A 1 44  ? -4.280  10.239 7.728  0.45 21.88 ? 24  ARG   A O    1 
ATOM   163  O O    B ARG   A 1 44  ? -4.322  10.186 7.708  0.55 19.67 ? 24  ARG   A O    1 
ATOM   164  C CB   A ARG   A 1 44  ? -7.312  11.320 7.086  0.45 25.17 ? 24  ARG   A CB   1 
ATOM   165  C CB   B ARG   A 1 44  ? -7.332  11.304 7.039  0.55 21.16 ? 24  ARG   A CB   1 
ATOM   166  C CG   A ARG   A 1 44  ? -7.587  10.288 8.171  0.45 29.06 ? 24  ARG   A CG   1 
ATOM   167  C CG   B ARG   A 1 44  ? -7.486  9.965  7.758  0.55 24.97 ? 24  ARG   A CG   1 
ATOM   168  C CD   A ARG   A 1 44  ? -8.691  9.351  7.771  0.45 31.88 ? 24  ARG   A CD   1 
ATOM   169  C CD   B ARG   A 1 44  ? -8.944  9.491  7.745  0.55 31.14 ? 24  ARG   A CD   1 
ATOM   170  N NE   A ARG   A 1 44  ? -8.748  8.227  8.689  0.45 33.90 ? 24  ARG   A NE   1 
ATOM   171  N NE   B ARG   A 1 44  ? -9.589  9.556  9.051  0.55 35.77 ? 24  ARG   A NE   1 
ATOM   172  C CZ   A ARG   A 1 44  ? -9.543  8.166  9.745  0.45 33.95 ? 24  ARG   A CZ   1 
ATOM   173  C CZ   B ARG   A 1 44  ? -9.445  8.651  10.011 0.55 37.51 ? 24  ARG   A CZ   1 
ATOM   174  N NH1  A ARG   A 1 44  ? -10.387 9.144  10.030 0.45 34.41 ? 24  ARG   A NH1  1 
ATOM   175  N NH1  B ARG   A 1 44  ? -8.703  7.571  9.838  0.55 35.32 ? 24  ARG   A NH1  1 
ATOM   176  N NH2  A ARG   A 1 44  ? -9.494  7.093  10.525 0.45 33.07 ? 24  ARG   A NH2  1 
ATOM   177  N NH2  B ARG   A 1 44  ? -10.058 8.837  11.176 0.55 41.29 ? 24  ARG   A NH2  1 
ATOM   178  H H    A ARG   A 1 44  ? -6.491  13.292 5.898  0.45 25.14 ? 24  ARG   A H    1 
ATOM   179  H H    B ARG   A 1 44  ? -6.497  13.297 5.906  0.55 23.36 ? 24  ARG   A H    1 
ATOM   180  H HA   A ARG   A 1 44  ? -5.783  12.178 8.129  0.45 26.66 ? 24  ARG   A HA   1 
ATOM   181  H HA   B ARG   A 1 44  ? -5.810  12.149 8.120  0.55 23.55 ? 24  ARG   A HA   1 
ATOM   182  H HB2  A ARG   A 1 44  ? -7.970  12.029 7.169  0.45 30.20 ? 24  ARG   A HB2  1 
ATOM   183  H HB2  B ARG   A 1 44  ? -7.981  11.921 7.412  0.55 25.40 ? 24  ARG   A HB2  1 
ATOM   184  H HB3  A ARG   A 1 44  ? -7.400  10.884 6.224  0.45 30.20 ? 24  ARG   A HB3  1 
ATOM   185  H HB3  B ARG   A 1 44  ? -7.514  11.161 6.097  0.55 25.40 ? 24  ARG   A HB3  1 
ATOM   186  H HG2  A ARG   A 1 44  ? -6.786  9.765  8.329  0.45 34.87 ? 24  ARG   A HG2  1 
ATOM   187  H HG2  B ARG   A 1 44  ? -6.943  9.296  7.313  0.55 29.97 ? 24  ARG   A HG2  1 
ATOM   188  H HG3  A ARG   A 1 44  ? -7.853  10.741 8.987  0.45 34.87 ? 24  ARG   A HG3  1 
ATOM   189  H HG3  B ARG   A 1 44  ? -7.204  10.062 8.681  0.55 29.97 ? 24  ARG   A HG3  1 
ATOM   190  H HD2  A ARG   A 1 44  ? -9.541  9.817  7.797  0.45 38.26 ? 24  ARG   A HD2  1 
ATOM   191  H HD2  B ARG   A 1 44  ? -9.450  10.050 7.136  0.55 37.37 ? 24  ARG   A HD2  1 
ATOM   192  H HD3  A ARG   A 1 44  ? -8.525  9.014  6.877  0.45 38.26 ? 24  ARG   A HD3  1 
ATOM   193  H HD3  B ARG   A 1 44  ? -8.970  8.568  7.448  0.55 37.37 ? 24  ARG   A HD3  1 
ATOM   194  H HE   A ARG   A 1 44  ? -8.231  7.557  8.537  0.45 40.68 ? 24  ARG   A HE   1 
ATOM   195  H HE   B ARG   A 1 44  ? -10.100 10.229 9.211  0.55 42.93 ? 24  ARG   A HE   1 
ATOM   196  H HH11 A ARG   A 1 44  ? -10.426 9.839  9.525  0.45 41.29 ? 24  ARG   A HH11 1 
ATOM   197  H HH11 B ARG   A 1 44  ? -8.299  7.442  9.090  0.55 42.39 ? 24  ARG   A HH11 1 
ATOM   198  H HH12 A ARG   A 1 44  ? -10.896 9.086  10.721 0.45 41.29 ? 24  ARG   A HH12 1 
ATOM   199  H HH12 B ARG   A 1 44  ? -8.624  6.998  10.474 0.55 42.39 ? 24  ARG   A HH12 1 
ATOM   200  H HH21 A ARG   A 1 44  ? -8.951  6.452  10.342 0.45 39.69 ? 24  ARG   A HH21 1 
ATOM   201  H HH21 B ARG   A 1 44  ? -10.541 9.538  11.301 0.55 49.55 ? 24  ARG   A HH21 1 
ATOM   202  H HH22 A ARG   A 1 44  ? -10.005 7.039  11.215 0.45 39.69 ? 24  ARG   A HH22 1 
ATOM   203  H HH22 B ARG   A 1 44  ? -9.972  8.257  11.805 0.55 49.55 ? 24  ARG   A HH22 1 
ATOM   204  N N    . LYS   A 1 45  ? -4.565  10.727 5.546  1.00 20.57 ? 25  LYS   A N    1 
ATOM   205  C CA   . LYS   A 1 45  ? -3.552  9.761  5.144  1.00 22.09 ? 25  LYS   A CA   1 
ATOM   206  C C    . LYS   A 1 45  ? -2.179  10.152 5.673  1.00 19.85 ? 25  LYS   A C    1 
ATOM   207  O O    . LYS   A 1 45  ? -1.403  9.290  6.078  1.00 20.39 ? 25  LYS   A O    1 
ATOM   208  C CB   . LYS   A 1 45  ? -3.536  9.638  3.621  1.00 24.41 ? 25  LYS   A CB   1 
ATOM   209  C CG   . LYS   A 1 45  ? -4.811  9.020  3.090  1.00 29.09 ? 25  LYS   A CG   1 
ATOM   210  H H    A LYS   A 1 45  ? -4.931  11.160 4.900  0.45 24.68 ? 25  LYS   A H    1 
ATOM   211  H H    B LYS   A 1 45  ? -4.917  11.175 4.902  0.55 24.68 ? 25  LYS   A H    1 
ATOM   212  H HA   . LYS   A 1 45  ? -3.773  8.892  5.514  1.00 26.50 ? 25  LYS   A HA   1 
ATOM   213  H HB2  . LYS   A 1 45  ? -3.441  10.521 3.231  1.00 29.29 ? 25  LYS   A HB2  1 
ATOM   214  H HB3  . LYS   A 1 45  ? -2.792  9.076  3.354  1.00 29.29 ? 25  LYS   A HB3  1 
ATOM   215  N N    . ILE   A 1 46  ? -1.886  11.451 5.713  1.00 18.58 ? 26  ILE   A N    1 
ATOM   216  C CA   . ILE   A 1 46  ? -0.618  11.918 6.270  1.00 18.85 ? 26  ILE   A CA   1 
ATOM   217  C C    . ILE   A 1 46  ? -0.562  11.636 7.772  1.00 17.49 ? 26  ILE   A C    1 
ATOM   218  O O    . ILE   A 1 46  ? 0.484   11.244 8.301  1.00 18.13 ? 26  ILE   A O    1 
ATOM   219  C CB   . ILE   A 1 46  ? -0.407  13.410 5.950  1.00 19.99 ? 26  ILE   A CB   1 
ATOM   220  C CG1  . ILE   A 1 46  ? -0.352  13.673 4.432  1.00 22.68 ? 26  ILE   A CG1  1 
ATOM   221  C CG2  . ILE   A 1 46  ? 0.847   13.916 6.634  1.00 20.37 ? 26  ILE   A CG2  1 
ATOM   222  C CD1  . ILE   A 1 46  ? 0.802   13.022 3.724  1.00 26.54 ? 26  ILE   A CD1  1 
ATOM   223  H H    . ILE   A 1 46  ? -2.400  12.078 5.427  1.00 22.30 ? 26  ILE   A H    1 
ATOM   224  H HA   . ILE   A 1 46  ? 0.105   11.426 5.851  1.00 22.63 ? 26  ILE   A HA   1 
ATOM   225  H HB   . ILE   A 1 46  ? -1.173  13.895 6.293  1.00 23.99 ? 26  ILE   A HB   1 
ATOM   226  H HG12 . ILE   A 1 46  ? -1.168  13.336 4.031  1.00 27.22 ? 26  ILE   A HG12 1 
ATOM   227  H HG13 . ILE   A 1 46  ? -0.281  14.630 4.288  1.00 27.22 ? 26  ILE   A HG13 1 
ATOM   228  H HG21 . ILE   A 1 46  ? 1.095   14.771 6.248  1.00 24.44 ? 26  ILE   A HG21 1 
ATOM   229  H HG22 . ILE   A 1 46  ? 0.670   14.019 7.582  1.00 24.44 ? 26  ILE   A HG22 1 
ATOM   230  H HG23 . ILE   A 1 46  ? 1.562   13.273 6.499  1.00 24.44 ? 26  ILE   A HG23 1 
ATOM   231  H HD11 . ILE   A 1 46  ? 0.772   13.263 2.785  1.00 31.85 ? 26  ILE   A HD11 1 
ATOM   232  H HD12 . ILE   A 1 46  ? 1.631   13.333 4.120  1.00 31.85 ? 26  ILE   A HD12 1 
ATOM   233  H HD13 . ILE   A 1 46  ? 0.729   12.060 3.821  1.00 31.85 ? 26  ILE   A HD13 1 
ATOM   234  N N    . VAL   A 1 47  ? -1.666  11.887 8.501  1.00 17.75 ? 27  VAL   A N    1 
ATOM   235  C CA   . VAL   A 1 47  ? -1.695  11.567 9.935  1.00 18.20 ? 27  VAL   A CA   1 
ATOM   236  C C    . VAL   A 1 47  ? -1.439  10.083 10.159 1.00 18.68 ? 27  VAL   A C    1 
ATOM   237  O O    . VAL   A 1 47  ? -0.644  9.693  11.024 1.00 18.33 ? 27  VAL   A O    1 
ATOM   238  C CB   . VAL   A 1 47  ? -3.017  12.005 10.585 1.00 18.00 ? 27  VAL   A CB   1 
ATOM   239  C CG1  . VAL   A 1 47  ? -3.035  11.575 12.056 1.00 18.68 ? 27  VAL   A CG1  1 
ATOM   240  C CG2  . VAL   A 1 47  ? -3.194  13.522 10.479 1.00 19.15 ? 27  VAL   A CG2  1 
ATOM   241  H H    . VAL   A 1 47  ? -2.391  12.233 8.194  1.00 21.31 ? 27  VAL   A H    1 
ATOM   242  H HA   . VAL   A 1 47  ? -0.980  12.069 10.358 1.00 21.84 ? 27  VAL   A HA   1 
ATOM   243  H HB   . VAL   A 1 47  ? -3.756  11.581 10.120 1.00 21.60 ? 27  VAL   A HB   1 
ATOM   244  H HG11 . VAL   A 1 47  ? -3.742  12.054 12.516 1.00 22.42 ? 27  VAL   A HG11 1 
ATOM   245  H HG12 . VAL   A 1 47  ? -3.197  10.620 12.104 1.00 22.42 ? 27  VAL   A HG12 1 
ATOM   246  H HG13 . VAL   A 1 47  ? -2.177  11.785 12.457 1.00 22.42 ? 27  VAL   A HG13 1 
ATOM   247  H HG21 . VAL   A 1 47  ? -4.021  13.775 10.919 1.00 22.98 ? 27  VAL   A HG21 1 
ATOM   248  H HG22 . VAL   A 1 47  ? -2.443  13.958 10.911 1.00 22.98 ? 27  VAL   A HG22 1 
ATOM   249  H HG23 . VAL   A 1 47  ? -3.228  13.772 9.543  1.00 22.98 ? 27  VAL   A HG23 1 
ATOM   250  N N    . GLU   A 1 48  ? -2.118  9.238  9.382  1.00 19.05 ? 28  GLU   A N    1 
ATOM   251  C CA   . GLU   A 1 48  ? -1.905  7.802  9.484  1.00 19.77 ? 28  GLU   A CA   1 
ATOM   252  C C    . GLU   A 1 48  ? -0.438  7.466  9.243  1.00 19.43 ? 28  GLU   A C    1 
ATOM   253  O O    . GLU   A 1 48  ? 0.170   6.699  9.996  1.00 19.69 ? 28  GLU   A O    1 
ATOM   254  C CB   . GLU   A 1 48  ? -2.768  7.067  8.457  1.00 22.70 ? 28  GLU   A CB   1 
ATOM   255  C CG   . GLU   A 1 48  ? -4.257  7.039  8.751  1.00 27.52 ? 28  GLU   A CG   1 
ATOM   256  C CD   . GLU   A 1 48  ? -4.671  5.901  9.676  1.00 34.25 ? 28  GLU   A CD   1 
ATOM   257  O OE1  . GLU   A 1 48  ? -3.788  5.238  10.267 1.00 35.93 ? 28  GLU   A OE1  1 
ATOM   258  O OE2  . GLU   A 1 48  ? -5.894  5.674  9.820  1.00 38.15 ? 28  GLU   A OE2  1 
ATOM   259  H H    . GLU   A 1 48  ? -2.701  9.471  8.795  1.00 22.86 ? 28  GLU   A H    1 
ATOM   260  H HA   . GLU   A 1 48  ? -2.163  7.509  10.372 1.00 23.73 ? 28  GLU   A HA   1 
ATOM   261  H HB2  . GLU   A 1 48  ? -2.652  7.501  7.597  1.00 27.24 ? 28  GLU   A HB2  1 
ATOM   262  H HB3  . GLU   A 1 48  ? -2.466  6.147  8.408  1.00 27.24 ? 28  GLU   A HB3  1 
ATOM   263  H HG2  . GLU   A 1 48  ? -4.509  7.874  9.175  1.00 33.02 ? 28  GLU   A HG2  1 
ATOM   264  H HG3  . GLU   A 1 48  ? -4.739  6.932  7.916  1.00 33.02 ? 28  GLU   A HG3  1 
ATOM   265  N N    A GLN   A 1 49  ? 0.165   8.057  8.209  0.61 19.27 ? 29  GLN   A N    1 
ATOM   266  N N    C GLN   A 1 49  ? 0.137   8.010  8.166  0.39 18.91 ? 29  GLN   A N    1 
ATOM   267  C CA   A GLN   A 1 49  ? 1.557   7.738  7.914  0.61 19.48 ? 29  GLN   A CA   1 
ATOM   268  C CA   C GLN   A 1 49  ? 1.549   7.782  7.882  0.39 19.17 ? 29  GLN   A CA   1 
ATOM   269  C C    A GLN   A 1 49  ? 2.492   8.208  9.024  0.61 19.23 ? 29  GLN   A C    1 
ATOM   270  C C    C GLN   A 1 49  ? 2.403   8.159  9.087  0.39 17.71 ? 29  GLN   A C    1 
ATOM   271  O O    A GLN   A 1 49  ? 3.473   7.525  9.353  0.61 20.78 ? 29  GLN   A O    1 
ATOM   272  O O    C GLN   A 1 49  ? 3.201   7.353  9.577  0.39 17.13 ? 29  GLN   A O    1 
ATOM   273  C CB   A GLN   A 1 49  ? 1.963   8.341  6.572  0.61 20.41 ? 29  GLN   A CB   1 
ATOM   274  C CB   C GLN   A 1 49  ? 1.971   8.572  6.636  0.39 21.53 ? 29  GLN   A CB   1 
ATOM   275  C CG   A GLN   A 1 49  ? 3.351   7.935  6.213  0.61 22.14 ? 29  GLN   A CG   1 
ATOM   276  C CG   C GLN   A 1 49  ? 1.525   7.959  5.303  0.39 24.53 ? 29  GLN   A CG   1 
ATOM   277  C CD   A GLN   A 1 49  ? 3.876   8.624  5.029  0.61 25.24 ? 29  GLN   A CD   1 
ATOM   278  C CD   C GLN   A 1 49  ? 1.927   8.798  4.097  0.39 25.41 ? 29  GLN   A CD   1 
ATOM   279  O OE1  A GLN   A 1 49  ? 3.147   9.239  4.261  0.61 27.10 ? 29  GLN   A OE1  1 
ATOM   280  O OE1  C GLN   A 1 49  ? 3.117   8.966  3.807  0.39 26.37 ? 29  GLN   A OE1  1 
ATOM   281  N NE2  A GLN   A 1 49  ? 5.179   8.550  4.883  0.61 24.08 ? 29  GLN   A NE2  1 
ATOM   282  N NE2  C GLN   A 1 49  ? 0.927   9.310  3.372  0.39 28.54 ? 29  GLN   A NE2  1 
ATOM   283  H H    A GLN   A 1 49  ? -0.199  8.628  7.680  0.61 23.13 ? 29  GLN   A H    1 
ATOM   284  H H    C GLN   A 1 49  ? -0.266  8.508  7.592  0.39 22.69 ? 29  GLN   A H    1 
ATOM   285  H HA   A GLN   A 1 49  ? 1.644   6.774  7.846  0.61 23.38 ? 29  GLN   A HA   1 
ATOM   286  H HA   C GLN   A 1 49  ? 1.691   6.842  7.692  0.39 23.00 ? 29  GLN   A HA   1 
ATOM   287  H HB2  A GLN   A 1 49  ? 1.360   8.027  5.880  0.61 24.49 ? 29  GLN   A HB2  1 
ATOM   288  H HB2  C GLN   A 1 49  ? 1.588   9.461  6.691  0.39 25.83 ? 29  GLN   A HB2  1 
ATOM   289  H HB3  A GLN   A 1 49  ? 1.928   9.309  6.629  0.61 24.49 ? 29  GLN   A HB3  1 
ATOM   290  H HB3  C GLN   A 1 49  ? 2.940   8.628  6.622  0.39 25.83 ? 29  GLN   A HB3  1 
ATOM   291  H HG2  A GLN   A 1 49  ? 3.939   8.136  6.959  0.61 26.57 ? 29  GLN   A HG2  1 
ATOM   292  H HG2  C GLN   A 1 49  ? 1.932   7.084  5.206  0.39 29.43 ? 29  GLN   A HG2  1 
ATOM   293  H HG3  A GLN   A 1 49  ? 3.362   6.982  6.031  0.61 26.57 ? 29  GLN   A HG3  1 
ATOM   294  H HG3  C GLN   A 1 49  ? 0.558   7.878  5.301  0.39 29.43 ? 29  GLN   A HG3  1 
ATOM   295  H HE21 A GLN   A 1 49  ? 5.652   8.121  5.459  0.61 28.90 ? 29  GLN   A HE21 1 
ATOM   296  H HE21 C GLN   A 1 49  ? 0.111   9.158  3.597  0.39 34.25 ? 29  GLN   A HE21 1 
ATOM   297  H HE22 A GLN   A 1 49  ? 5.559   8.930  4.212  0.61 28.90 ? 29  GLN   A HE22 1 
ATOM   298  H HE22 C GLN   A 1 49  ? 1.099   9.791  2.681  0.39 34.25 ? 29  GLN   A HE22 1 
ATOM   299  N N    . TYR   A 1 50  ? 2.228   9.387  9.589  1.00 17.31 ? 30  TYR   A N    1 
ATOM   300  C CA   . TYR   A 1 50  ? 3.034   9.853  10.704 1.00 17.24 ? 30  TYR   A CA   1 
ATOM   301  C C    . TYR   A 1 50  ? 2.960   8.873  11.861 1.00 16.73 ? 30  TYR   A C    1 
ATOM   302  O O    . TYR   A 1 50  ? 3.981   8.479  12.429 1.00 17.45 ? 30  TYR   A O    1 
ATOM   303  C CB   . TYR   A 1 50  ? 2.584   11.252 11.119 1.00 17.42 ? 30  TYR   A CB   1 
ATOM   304  C CG   . TYR   A 1 50  ? 3.397   11.872 12.225 1.00 17.13 ? 30  TYR   A CG   1 
ATOM   305  C CD1  . TYR   A 1 50  ? 3.273   11.455 13.534 1.00 16.83 ? 30  TYR   A CD1  1 
ATOM   306  C CD2  . TYR   A 1 50  ? 4.266   12.908 11.963 1.00 18.34 ? 30  TYR   A CD2  1 
ATOM   307  C CE1  . TYR   A 1 50  ? 3.999   12.042 14.544 1.00 17.36 ? 30  TYR   A CE1  1 
ATOM   308  C CE2  . TYR   A 1 50  ? 5.026   13.476 12.962 1.00 19.12 ? 30  TYR   A CE2  1 
ATOM   309  C CZ   . TYR   A 1 50  ? 4.874   13.055 14.251 1.00 18.93 ? 30  TYR   A CZ   1 
ATOM   310  O OH   . TYR   A 1 50  ? 5.635   13.661 15.218 1.00 21.16 ? 30  TYR   A OH   1 
ATOM   311  H H    A TYR   A 1 50  ? 1.599   9.922  9.347  0.61 20.77 ? 30  TYR   A H    1 
ATOM   312  H H    C TYR   A 1 50  ? 1.653   9.958  9.300  0.39 20.77 ? 30  TYR   A H    1 
ATOM   313  H HA   . TYR   A 1 50  ? 3.963   9.918  10.432 1.00 20.69 ? 30  TYR   A HA   1 
ATOM   314  H HB2  . TYR   A 1 50  ? 2.646   11.837 10.348 1.00 20.91 ? 30  TYR   A HB2  1 
ATOM   315  H HB3  . TYR   A 1 50  ? 1.665   11.202 11.425 1.00 20.91 ? 30  TYR   A HB3  1 
ATOM   316  H HD1  . TYR   A 1 50  ? 2.685   10.764 13.738 1.00 20.19 ? 30  TYR   A HD1  1 
ATOM   317  H HD2  . TYR   A 1 50  ? 4.342   13.230 11.094 1.00 22.00 ? 30  TYR   A HD2  1 
ATOM   318  H HE1  . TYR   A 1 50  ? 3.896   11.752 15.422 1.00 20.83 ? 30  TYR   A HE1  1 
ATOM   319  H HE2  . TYR   A 1 50  ? 5.640   14.144 12.758 1.00 22.95 ? 30  TYR   A HE2  1 
ATOM   320  H HH   . TYR   A 1 50  ? 5.480   13.312 15.966 1.00 25.39 ? 30  TYR   A HH   1 
ATOM   321  N N    . MET   A 1 51  ? 1.741   8.517  12.263 1.00 16.62 ? 31  MET   A N    1 
ATOM   322  C CA   . MET   A 1 51  ? 1.565   7.686  13.442 1.00 16.51 ? 31  MET   A CA   1 
ATOM   323  C C    . MET   A 1 51  ? 2.140   6.293  13.279 1.00 17.83 ? 31  MET   A C    1 
ATOM   324  O O    . MET   A 1 51  ? 2.475   5.656  14.290 1.00 19.42 ? 31  MET   A O    1 
ATOM   325  C CB   . MET   A 1 51  ? 0.091   7.581  13.829 1.00 17.12 ? 31  MET   A CB   1 
ATOM   326  C CG   . MET   A 1 51  ? -0.553  8.930  14.188 1.00 17.73 ? 31  MET   A CG   1 
ATOM   327  S SD   . MET   A 1 51  ? 0.229   9.879  15.470 1.00 17.65 ? 31  MET   A SD   1 
ATOM   328  C CE   . MET   A 1 51  ? 0.303   8.693  16.804 1.00 18.21 ? 31  MET   A CE   1 
ATOM   329  H H    . MET   A 1 51  ? 1.009   8.743  11.872 1.00 19.94 ? 31  MET   A H    1 
ATOM   330  H HA   . MET   A 1 51  ? 2.028   8.130  14.168 1.00 19.82 ? 31  MET   A HA   1 
ATOM   331  H HB2  . MET   A 1 51  ? -0.401  7.207  13.082 1.00 20.55 ? 31  MET   A HB2  1 
ATOM   332  H HB3  . MET   A 1 51  ? 0.013   7.001  14.602 1.00 20.55 ? 31  MET   A HB3  1 
ATOM   333  H HG2  . MET   A 1 51  ? -0.556  9.482  13.390 1.00 21.28 ? 31  MET   A HG2  1 
ATOM   334  H HG3  . MET   A 1 51  ? -1.463  8.760  14.478 1.00 21.28 ? 31  MET   A HG3  1 
ATOM   335  H HE1  . MET   A 1 51  ? 0.705   9.114  17.579 1.00 21.85 ? 31  MET   A HE1  1 
ATOM   336  H HE2  . MET   A 1 51  ? -0.598  8.400  17.016 1.00 21.85 ? 31  MET   A HE2  1 
ATOM   337  H HE3  . MET   A 1 51  ? 0.839   7.935  16.523 1.00 21.85 ? 31  MET   A HE3  1 
ATOM   338  N N    . HIS   A 1 52  ? 2.273   5.812  12.043 1.00 17.97 ? 32  HIS   A N    1 
ATOM   339  C CA   . HIS   A 1 52  ? 2.812   4.497  11.761 1.00 18.87 ? 32  HIS   A CA   1 
ATOM   340  C C    . HIS   A 1 52  ? 4.277   4.529  11.373 1.00 19.74 ? 32  HIS   A C    1 
ATOM   341  O O    . HIS   A 1 52  ? 4.829   3.487  11.018 1.00 22.33 ? 32  HIS   A O    1 
ATOM   342  C CB   . HIS   A 1 52  ? 1.913   3.819  10.738 1.00 21.41 ? 32  HIS   A CB   1 
ATOM   343  C CG   . HIS   A 1 52  ? 0.601   3.394  11.336 1.00 23.41 ? 32  HIS   A CG   1 
ATOM   344  N ND1  . HIS   A 1 52  ? -0.545  4.158  11.262 1.00 28.54 ? 32  HIS   A ND1  1 
ATOM   345  C CD2  . HIS   A 1 52  ? 0.286   2.335  12.117 1.00 26.23 ? 32  HIS   A CD2  1 
ATOM   346  C CE1  . HIS   A 1 52  ? -1.532  3.538  11.888 1.00 29.77 ? 32  HIS   A CE1  1 
ATOM   347  N NE2  . HIS   A 1 52  ? -1.048  2.439  12.430 1.00 29.19 ? 32  HIS   A NE2  1 
ATOM   348  H H    . HIS   A 1 52  ? 2.050   6.246  11.335 1.00 21.56 ? 32  HIS   A H    1 
ATOM   349  H HA   . HIS   A 1 52  ? 2.792   3.930  12.548 1.00 22.64 ? 32  HIS   A HA   1 
ATOM   350  H HB2  . HIS   A 1 52  ? 1.731   4.438  10.014 1.00 25.70 ? 32  HIS   A HB2  1 
ATOM   351  H HB3  . HIS   A 1 52  ? 2.360   3.029  10.394 1.00 25.70 ? 32  HIS   A HB3  1 
ATOM   352  H HD1  . HIS   A 1 52  ? -0.609  4.920  10.869 1.00 34.25 ? 32  HIS   A HD1  1 
ATOM   353  H HD2  . HIS   A 1 52  ? 0.866   1.662  12.392 1.00 31.48 ? 32  HIS   A HD2  1 
ATOM   354  H HE1  . HIS   A 1 52  ? -2.414  3.828  11.937 1.00 35.73 ? 32  HIS   A HE1  1 
ATOM   355  N N    . THR   A 1 53  ? 4.920   5.686  11.440 1.00 19.10 ? 33  THR   A N    1 
ATOM   356  C CA   . THR   A 1 53  ? 6.343   5.780  11.099 1.00 19.00 ? 33  THR   A CA   1 
ATOM   357  C C    . THR   A 1 53  ? 7.188   5.224  12.242 1.00 20.04 ? 33  THR   A C    1 
ATOM   358  O O    . THR   A 1 53  ? 7.167   5.753  13.362 1.00 20.80 ? 33  THR   A O    1 
ATOM   359  C CB   . THR   A 1 53  ? 6.715   7.231  10.800 1.00 20.13 ? 33  THR   A CB   1 
ATOM   360  O OG1  . THR   A 1 53  ? 5.991   7.682  9.655  1.00 20.77 ? 33  THR   A OG1  1 
ATOM   361  C CG2  . THR   A 1 53  ? 8.189   7.343  10.461 1.00 21.92 ? 33  THR   A CG2  1 
ATOM   362  H H    . THR   A 1 53  ? 4.562   6.431  11.677 1.00 22.93 ? 33  THR   A H    1 
ATOM   363  H HA   . THR   A 1 53  ? 6.523   5.248  10.308 1.00 22.80 ? 33  THR   A HA   1 
ATOM   364  H HB   . THR   A 1 53  ? 6.511   7.771  11.579 1.00 24.15 ? 33  THR   A HB   1 
ATOM   365  H HG1  . THR   A 1 53  ? 5.165   7.653  9.808  1.00 24.93 ? 33  THR   A HG1  1 
ATOM   366  H HG21 . THR   A 1 53  ? 8.378   8.221  10.093 1.00 26.30 ? 33  THR   A HG21 1 
ATOM   367  H HG22 . THR   A 1 53  ? 8.724   7.215  11.260 1.00 26.30 ? 33  THR   A HG22 1 
ATOM   368  H HG23 . THR   A 1 53  ? 8.431   6.669  9.808  1.00 26.30 ? 33  THR   A HG23 1 
ATOM   369  N N    . ARG   A 1 54  ? 7.957   4.187  11.933 1.00 20.50 ? 34  ARG   A N    1 
ATOM   370  C CA   . ARG   A 1 54  ? 8.751   3.470  12.909 1.00 21.01 ? 34  ARG   A CA   1 
ATOM   371  C C    . ARG   A 1 54  ? 10.130  3.173  12.347 1.00 23.52 ? 34  ARG   A C    1 
ATOM   372  O O    . ARG   A 1 54  ? 10.349  3.202  11.137 1.00 24.12 ? 34  ARG   A O    1 
ATOM   373  C CB   . ARG   A 1 54  ? 8.082   2.140  13.273 1.00 21.65 ? 34  ARG   A CB   1 
ATOM   374  C CG   . ARG   A 1 54  ? 6.748   2.329  13.980 1.00 20.92 ? 34  ARG   A CG   1 
ATOM   375  C CD   . ARG   A 1 54  ? 6.080   1.010  14.199 1.00 20.25 ? 34  ARG   A CD   1 
ATOM   376  N NE   . ARG   A 1 54  ? 4.825   1.180  14.915 1.00 21.22 ? 34  ARG   A NE   1 
ATOM   377  C CZ   . ARG   A 1 54  ? 3.994   0.188  15.154 1.00 21.86 ? 34  ARG   A CZ   1 
ATOM   378  N NH1  . ARG   A 1 54  ? 4.307   -1.051 14.813 1.00 22.76 ? 34  ARG   A NH1  1 
ATOM   379  N NH2  . ARG   A 1 54  ? 2.829   0.447  15.745 1.00 22.56 ? 34  ARG   A NH2  1 
ATOM   380  H H    . ARG   A 1 54  ? 8.036   3.872  11.137 1.00 24.60 ? 34  ARG   A H    1 
ATOM   381  H HA   . ARG   A 1 54  ? 8.854   4.026  13.697 1.00 25.21 ? 34  ARG   A HA   1 
ATOM   382  H HB2  . ARG   A 1 54  ? 7.923   1.634  12.461 1.00 25.99 ? 34  ARG   A HB2  1 
ATOM   383  H HB3  . ARG   A 1 54  ? 8.668   1.642  13.864 1.00 25.99 ? 34  ARG   A HB3  1 
ATOM   384  H HG2  . ARG   A 1 54  ? 6.893   2.749  14.843 1.00 25.11 ? 34  ARG   A HG2  1 
ATOM   385  H HG3  . ARG   A 1 54  ? 6.167   2.883  13.436 1.00 25.11 ? 34  ARG   A HG3  1 
ATOM   386  H HD2  . ARG   A 1 54  ? 5.892   0.595  13.343 1.00 24.30 ? 34  ARG   A HD2  1 
ATOM   387  H HD3  . ARG   A 1 54  ? 6.660   0.437  14.725 1.00 24.30 ? 34  ARG   A HD3  1 
ATOM   388  H HE   . ARG   A 1 54  ? 4.617   1.966  15.196 1.00 25.47 ? 34  ARG   A HE   1 
ATOM   389  H HH11 . ARG   A 1 54  ? 5.060   -1.215 14.430 1.00 27.32 ? 34  ARG   A HH11 1 
ATOM   390  H HH12 . ARG   A 1 54  ? 3.758   -1.693 14.973 1.00 27.32 ? 34  ARG   A HH12 1 
ATOM   391  H HH21 . ARG   A 1 54  ? 2.628   1.253  15.966 1.00 27.07 ? 34  ARG   A HH21 1 
ATOM   392  H HH22 . ARG   A 1 54  ? 2.277   -0.193 15.907 1.00 27.07 ? 34  ARG   A HH22 1 
ATOM   393  N N    . GLY   A 1 55  ? 11.055  2.873  13.251 1.00 23.34 ? 35  GLY   A N    1 
ATOM   394  C CA   . GLY   A 1 55  ? 12.368  2.416  12.826 1.00 25.19 ? 35  GLY   A CA   1 
ATOM   395  C C    . GLY   A 1 55  ? 13.073  3.446  11.967 1.00 25.18 ? 35  GLY   A C    1 
ATOM   396  O O    . GLY   A 1 55  ? 12.983  4.658  12.208 1.00 24.67 ? 35  GLY   A O    1 
ATOM   397  H H    . GLY   A 1 55  ? 10.949  2.924  14.103 1.00 28.01 ? 35  GLY   A H    1 
ATOM   398  H HA2  . GLY   A 1 55  ? 12.916  2.239  13.606 1.00 30.23 ? 35  GLY   A HA2  1 
ATOM   399  H HA3  . GLY   A 1 55  ? 12.275  1.599  12.312 1.00 30.23 ? 35  GLY   A HA3  1 
ATOM   400  N N    . GLU   A 1 56  ? 13.825  2.961  10.971 1.00 28.04 ? 36  GLU   A N    1 
ATOM   401  C CA   . GLU   A 1 56  ? 14.627  3.860  10.156 1.00 29.64 ? 36  GLU   A CA   1 
ATOM   402  C C    . GLU   A 1 56  ? 13.788  4.877  9.401  1.00 28.31 ? 36  GLU   A C    1 
ATOM   403  O O    . GLU   A 1 56  ? 14.291  5.959  9.086  1.00 28.26 ? 36  GLU   A O    1 
ATOM   404  C CB   . GLU   A 1 56  ? 15.470  3.055  9.164  1.00 36.29 ? 36  GLU   A CB   1 
ATOM   405  C CG   . GLU   A 1 56  ? 16.463  2.143  9.829  1.00 41.62 ? 36  GLU   A CG   1 
ATOM   406  C CD   . GLU   A 1 56  ? 17.438  2.894  10.718 1.00 46.22 ? 36  GLU   A CD   1 
ATOM   407  O OE1  . GLU   A 1 56  ? 18.058  3.874  10.246 1.00 47.62 ? 36  GLU   A OE1  1 
ATOM   408  O OE2  . GLU   A 1 56  ? 17.570  2.507  11.898 1.00 48.75 ? 36  GLU   A OE2  1 
ATOM   409  H H    . GLU   A 1 56  ? 13.883  2.130  10.756 1.00 33.65 ? 36  GLU   A H    1 
ATOM   410  H HA   . GLU   A 1 56  ? 15.225  4.349  10.743 1.00 35.57 ? 36  GLU   A HA   1 
ATOM   411  H HB2  . GLU   A 1 56  ? 14.880  2.508  8.622  1.00 43.55 ? 36  GLU   A HB2  1 
ATOM   412  H HB3  . GLU   A 1 56  ? 15.963  3.671  8.599  1.00 43.55 ? 36  GLU   A HB3  1 
ATOM   413  H HG2  . GLU   A 1 56  ? 15.985  1.503  10.380 1.00 49.95 ? 36  GLU   A HG2  1 
ATOM   414  H HG3  . GLU   A 1 56  ? 16.973  1.678  9.147  1.00 49.95 ? 36  GLU   A HG3  1 
ATOM   415  N N    . ALA   A 1 57  ? 12.517  4.574  9.135  1.00 25.96 ? 37  ALA   A N    1 
ATOM   416  C CA   . ALA   A 1 57  ? 11.648  5.527  8.456  1.00 25.23 ? 37  ALA   A CA   1 
ATOM   417  C C    . ALA   A 1 57  ? 11.490  6.804  9.266  1.00 22.76 ? 37  ALA   A C    1 
ATOM   418  O O    . ALA   A 1 57  ? 11.155  7.843  8.704  1.00 22.35 ? 37  ALA   A O    1 
ATOM   419  C CB   . ALA   A 1 57  ? 10.285  4.902  8.172  1.00 28.42 ? 37  ALA   A CB   1 
ATOM   420  H H    . ALA   A 1 57  ? 12.138  3.828  9.336  1.00 31.16 ? 37  ALA   A H    1 
ATOM   421  H HA   . ALA   A 1 57  ? 12.038  5.757  7.598  1.00 30.28 ? 37  ALA   A HA   1 
ATOM   422  H HB1  . ALA   A 1 57  ? 9.725   5.556  7.726  1.00 34.10 ? 37  ALA   A HB1  1 
ATOM   423  H HB2  . ALA   A 1 57  ? 10.405  4.126  7.603  1.00 34.10 ? 37  ALA   A HB2  1 
ATOM   424  H HB3  . ALA   A 1 57  ? 9.878   4.637  9.012  1.00 34.10 ? 37  ALA   A HB3  1 
ATOM   425  N N    . ARG   A 1 58  ? 11.747  6.760  10.567 1.00 20.73 ? 38  ARG   A N    1 
ATOM   426  C CA   . ARG   A 1 58  ? 11.683  7.988  11.357 1.00 20.71 ? 38  ARG   A CA   1 
ATOM   427  C C    . ARG   A 1 58  ? 12.647  9.044  10.827 1.00 21.32 ? 38  ARG   A C    1 
ATOM   428  O O    . ARG   A 1 58  ? 12.411  10.242 10.999 1.00 21.31 ? 38  ARG   A O    1 
ATOM   429  C CB   . ARG   A 1 58  ? 11.940  7.672  12.824 1.00 21.63 ? 38  ARG   A CB   1 
ATOM   430  C CG   . ARG   A 1 58  ? 10.783  6.874  13.427 1.00 22.90 ? 38  ARG   A CG   1 
ATOM   431  C CD   . ARG   A 1 58  ? 11.177  6.036  14.636 1.00 25.96 ? 38  ARG   A CD   1 
ATOM   432  N NE   . ARG   A 1 58  ? 11.710  6.841  15.714 1.00 26.73 ? 38  ARG   A NE   1 
ATOM   433  C CZ   . ARG   A 1 58  ? 12.221  6.343  16.835 1.00 25.10 ? 38  ARG   A CZ   1 
ATOM   434  N NH1  . ARG   A 1 58  ? 12.351  5.041  17.026 1.00 26.71 ? 38  ARG   A NH1  1 
ATOM   435  N NH2  . ARG   A 1 58  ? 12.649  7.171  17.777 1.00 25.97 ? 38  ARG   A NH2  1 
ATOM   436  H H    . ARG   A 1 58  ? 11.957  6.052  11.008 1.00 24.88 ? 38  ARG   A H    1 
ATOM   437  H HA   . ARG   A 1 58  ? 10.791  8.366  11.299 1.00 24.86 ? 38  ARG   A HA   1 
ATOM   438  H HB2  . ARG   A 1 58  ? 12.751  7.145  12.903 1.00 25.96 ? 38  ARG   A HB2  1 
ATOM   439  H HB3  . ARG   A 1 58  ? 12.033  8.500  13.321 1.00 25.96 ? 38  ARG   A HB3  1 
ATOM   440  H HG2  . ARG   A 1 58  ? 10.091  7.492  13.709 1.00 27.49 ? 38  ARG   A HG2  1 
ATOM   441  H HG3  . ARG   A 1 58  ? 10.435  6.271  12.751 1.00 27.49 ? 38  ARG   A HG3  1 
ATOM   442  H HD2  . ARG   A 1 58  ? 10.394  5.569  14.967 1.00 31.15 ? 38  ARG   A HD2  1 
ATOM   443  H HD3  . ARG   A 1 58  ? 11.858  5.397  14.372 1.00 31.15 ? 38  ARG   A HD3  1 
ATOM   444  H HE   . ARG   A 1 58  ? 11.695  7.696  15.624 1.00 32.07 ? 38  ARG   A HE   1 
ATOM   445  H HH11 . ARG   A 1 58  ? 12.102  4.490  16.415 1.00 32.05 ? 38  ARG   A HH11 1 
ATOM   446  H HH12 . ARG   A 1 58  ? 12.685  4.746  17.761 1.00 32.05 ? 38  ARG   A HH12 1 
ATOM   447  H HH21 . ARG   A 1 58  ? 12.594  8.021  17.659 1.00 31.17 ? 38  ARG   A HH21 1 
ATOM   448  H HH22 . ARG   A 1 58  ? 12.981  6.859  18.506 1.00 31.17 ? 38  ARG   A HH22 1 
ATOM   449  N N    . LEU   A 1 59  ? 13.741  8.622  10.178 1.00 22.08 ? 39  LEU   A N    1 
ATOM   450  C CA   . LEU   A 1 59  ? 14.708  9.573  9.632  1.00 23.57 ? 39  LEU   A CA   1 
ATOM   451  C C    . LEU   A 1 59  ? 14.113  10.442 8.534  1.00 23.92 ? 39  LEU   A C    1 
ATOM   452  O O    . LEU   A 1 59  ? 14.705  11.475 8.201  1.00 24.59 ? 39  LEU   A O    1 
ATOM   453  C CB   . LEU   A 1 59  ? 15.959  8.845  9.107  1.00 25.94 ? 39  LEU   A CB   1 
ATOM   454  C CG   . LEU   A 1 59  ? 16.779  8.148  10.193 1.00 29.39 ? 39  LEU   A CG   1 
ATOM   455  C CD1  . LEU   A 1 59  ? 17.899  7.348  9.554  1.00 30.88 ? 39  LEU   A CD1  1 
ATOM   456  C CD2  . LEU   A 1 59  ? 17.347  9.154  11.199 1.00 30.84 ? 39  LEU   A CD2  1 
ATOM   457  H H    . LEU   A 1 59  ? 13.942  7.796  10.044 1.00 26.50 ? 39  LEU   A H    1 
ATOM   458  H HA   . LEU   A 1 59  ? 14.993  10.155 10.354 1.00 28.28 ? 39  LEU   A HA   1 
ATOM   459  H HB2  . LEU   A 1 59  ? 15.680  8.170  8.469  1.00 31.12 ? 39  LEU   A HB2  1 
ATOM   460  H HB3  . LEU   A 1 59  ? 16.535  9.494  8.672  1.00 31.12 ? 39  LEU   A HB3  1 
ATOM   461  H HG   . LEU   A 1 59  ? 16.200  7.546  10.686 1.00 35.27 ? 39  LEU   A HG   1 
ATOM   462  H HD11 . LEU   A 1 59  ? 18.410  6.907  10.251 1.00 37.05 ? 39  LEU   A HD11 1 
ATOM   463  H HD12 . LEU   A 1 59  ? 17.513  6.686  8.958  1.00 37.05 ? 39  LEU   A HD12 1 
ATOM   464  H HD13 . LEU   A 1 59  ? 18.472  7.950  9.054  1.00 37.05 ? 39  LEU   A HD13 1 
ATOM   465  H HD21 . LEU   A 1 59  ? 17.993  8.704  11.766 1.00 37.00 ? 39  LEU   A HD21 1 
ATOM   466  H HD22 . LEU   A 1 59  ? 17.778  9.876  10.715 1.00 37.00 ? 39  LEU   A HD22 1 
ATOM   467  H HD23 . LEU   A 1 59  ? 16.621  9.505  11.739 1.00 37.00 ? 39  LEU   A HD23 1 
ATOM   468  N N    . LYS   A 1 60  ? 12.986  10.041 7.939  1.00 23.19 ? 40  LYS   A N    1 
ATOM   469  C CA   . LYS   A 1 60  ? 12.351  10.803 6.868  1.00 23.25 ? 40  LYS   A CA   1 
ATOM   470  C C    . LYS   A 1 60  ? 10.978  11.355 7.253  1.00 21.94 ? 40  LYS   A C    1 
ATOM   471  O O    . LYS   A 1 60  ? 10.276  11.920 6.412  1.00 22.47 ? 40  LYS   A O    1 
ATOM   472  C CB   . LYS   A 1 60  ? 12.227  9.961  5.602  1.00 26.86 ? 40  LYS   A CB   1 
ATOM   473  C CG   . LYS   A 1 60  ? 13.571  9.642  4.945  1.00 33.36 ? 40  LYS   A CG   1 
ATOM   474  C CD   . LYS   A 1 60  ? 13.368  8.978  3.604  1.00 38.12 ? 40  LYS   A CD   1 
ATOM   475  H H    . LYS   A 1 60  ? 12.566  9.319  8.144  1.00 27.84 ? 40  LYS   A H    1 
ATOM   476  H HA   . LYS   A 1 60  ? 12.928  11.557 6.670  1.00 27.90 ? 40  LYS   A HA   1 
ATOM   477  H HB2  . LYS   A 1 60  ? 11.799  9.120  5.826  1.00 32.23 ? 40  LYS   A HB2  1 
ATOM   478  H HB3  . LYS   A 1 60  ? 11.688  10.445 4.956  1.00 32.23 ? 40  LYS   A HB3  1 
ATOM   479  H HG2  . LYS   A 1 60  ? 14.069  10.464 4.809  1.00 40.04 ? 40  LYS   A HG2  1 
ATOM   480  H HG3  . LYS   A 1 60  ? 14.075  9.039  5.514  1.00 40.04 ? 40  LYS   A HG3  1 
ATOM   481  N N    . ARG   A 1 61  ? 10.586  11.238 8.521  1.00 20.54 ? 41  ARG   A N    1 
ATOM   482  C CA   . ARG   A 1 61  ? 9.268   11.721 8.935  1.00 20.17 ? 41  ARG   A CA   1 
ATOM   483  C C    . ARG   A 1 61  ? 9.130   13.230 8.758  1.00 19.71 ? 41  ARG   A C    1 
ATOM   484  O O    . ARG   A 1 61  ? 8.015   13.729 8.548  1.00 19.62 ? 41  ARG   A O    1 
ATOM   485  C CB   . ARG   A 1 61  ? 9.000   11.296 10.382 1.00 20.98 ? 41  ARG   A CB   1 
ATOM   486  C CG   . ARG   A 1 61  ? 7.524   11.418 10.834 1.00 20.41 ? 41  ARG   A CG   1 
ATOM   487  C CD   . ARG   A 1 61  ? 7.375   10.898 12.252 1.00 21.51 ? 41  ARG   A CD   1 
ATOM   488  N NE   . ARG   A 1 61  ? 7.976   11.827 13.193 1.00 22.61 ? 41  ARG   A NE   1 
ATOM   489  C CZ   . ARG   A 1 61  ? 8.146   11.581 14.483 1.00 24.20 ? 41  ARG   A CZ   1 
ATOM   490  N NH1  . ARG   A 1 61  ? 7.767   10.436 15.012 1.00 25.95 ? 41  ARG   A NH1  1 
ATOM   491  N NH2  . ARG   A 1 61  ? 8.793   12.471 15.234 1.00 25.74 ? 41  ARG   A NH2  1 
ATOM   492  H H    . ARG   A 1 61  ? 11.054  10.888 9.152  1.00 24.65 ? 41  ARG   A H    1 
ATOM   493  H HA   . ARG   A 1 61  ? 8.587   11.314 8.377  1.00 24.21 ? 41  ARG   A HA   1 
ATOM   494  H HB2  . ARG   A 1 61  ? 9.260   10.367 10.483 1.00 25.18 ? 41  ARG   A HB2  1 
ATOM   495  H HB3  . ARG   A 1 61  ? 9.532   11.854 10.970 1.00 25.18 ? 41  ARG   A HB3  1 
ATOM   496  H HG2  . ARG   A 1 61  ? 7.251   12.349 10.813 1.00 24.50 ? 41  ARG   A HG2  1 
ATOM   497  H HG3  . ARG   A 1 61  ? 6.957   10.893 10.248 1.00 24.50 ? 41  ARG   A HG3  1 
ATOM   498  H HD2  . ARG   A 1 61  ? 6.434   10.803 12.467 1.00 25.81 ? 41  ARG   A HD2  1 
ATOM   499  H HD3  . ARG   A 1 61  ? 7.822   10.041 12.333 1.00 25.81 ? 41  ARG   A HD3  1 
ATOM   500  H HE   . ARG   A 1 61  ? 8.240   12.588 12.892 1.00 27.13 ? 41  ARG   A HE   1 
ATOM   501  H HH11 . ARG   A 1 61  ? 7.403   9.833  14.518 1.00 31.14 ? 41  ARG   A HH11 1 
ATOM   502  H HH12 . ARG   A 1 61  ? 7.884   10.291 15.852 1.00 31.14 ? 41  ARG   A HH12 1 
ATOM   503  H HH21 . ARG   A 1 61  ? 9.095   13.194 14.879 1.00 30.89 ? 41  ARG   A HH21 1 
ATOM   504  H HH22 . ARG   A 1 61  ? 8.909   12.322 16.073 1.00 30.89 ? 41  ARG   A HH22 1 
ATOM   505  N N    . HIS   A 1 62  ? 10.242  13.967 8.809  1.00 19.50 ? 42  HIS   A N    1 
ATOM   506  C CA   . HIS   A 1 62  ? 10.178  15.409 8.638  1.00 19.66 ? 42  HIS   A CA   1 
ATOM   507  C C    . HIS   A 1 62  ? 9.674   15.792 7.251  1.00 20.56 ? 42  HIS   A C    1 
ATOM   508  O O    . HIS   A 1 62  ? 9.249   16.928 7.055  1.00 20.72 ? 42  HIS   A O    1 
ATOM   509  C CB   . HIS   A 1 62  ? 11.550  16.038 8.878  1.00 21.24 ? 42  HIS   A CB   1 
ATOM   510  C CG   . HIS   A 1 62  ? 12.609  15.592 7.926  1.00 22.62 ? 42  HIS   A CG   1 
ATOM   511  N ND1  . HIS   A 1 62  ? 13.181  14.339 7.969  1.00 23.56 ? 42  HIS   A ND1  1 
ATOM   512  C CD2  . HIS   A 1 62  ? 13.223  16.255 6.918  1.00 25.52 ? 42  HIS   A CD2  1 
ATOM   513  C CE1  . HIS   A 1 62  ? 14.109  14.253 7.030  1.00 24.48 ? 42  HIS   A CE1  1 
ATOM   514  N NE2  . HIS   A 1 62  ? 14.145  15.399 6.378  1.00 26.45 ? 42  HIS   A NE2  1 
ATOM   515  H H    . HIS   A 1 62  ? 11.033  13.657 8.940  1.00 23.40 ? 42  HIS   A H    1 
ATOM   516  H HA   . HIS   A 1 62  ? 9.568   15.771 9.299  1.00 23.59 ? 42  HIS   A HA   1 
ATOM   517  H HB2  . HIS   A 1 62  ? 11.467  17.001 8.795  1.00 25.49 ? 42  HIS   A HB2  1 
ATOM   518  H HB3  . HIS   A 1 62  ? 11.844  15.807 9.773  1.00 25.49 ? 42  HIS   A HB3  1 
ATOM   519  H HD2  . HIS   A 1 62  ? 13.051  17.127 6.644  1.00 30.63 ? 42  HIS   A HD2  1 
ATOM   520  H HE1  . HIS   A 1 62  ? 14.643  13.511 6.859  1.00 29.37 ? 42  HIS   A HE1  1 
ATOM   521  H HE2  . HIS   A 1 62  ? 14.666  15.580 5.718  1.00 31.75 ? 42  HIS   A HE2  1 
ATOM   522  N N    . LEU   A 1 63  ? 9.728   14.882 6.273  1.00 19.48 ? 43  LEU   A N    1 
ATOM   523  C CA   . LEU   A 1 63  ? 9.234   15.214 4.942  1.00 20.55 ? 43  LEU   A CA   1 
ATOM   524  C C    . LEU   A 1 63  ? 7.710   15.284 4.904  1.00 20.07 ? 43  LEU   A C    1 
ATOM   525  O O    . LEU   A 1 63  ? 7.130   15.699 3.900  1.00 21.18 ? 43  LEU   A O    1 
ATOM   526  C CB   . LEU   A 1 63  ? 9.753   14.209 3.920  1.00 23.20 ? 43  LEU   A CB   1 
ATOM   527  C CG   . LEU   A 1 63  ? 11.285  14.186 3.786  1.00 27.19 ? 43  LEU   A CG   1 
ATOM   528  C CD1  . LEU   A 1 63  ? 11.753  13.098 2.812  1.00 30.66 ? 43  LEU   A CD1  1 
ATOM   529  C CD2  . LEU   A 1 63  ? 11.847  15.552 3.341  1.00 28.76 ? 43  LEU   A CD2  1 
ATOM   530  H H    . LEU   A 1 63  ? 10.039  14.084 6.357  1.00 23.38 ? 43  LEU   A H    1 
ATOM   531  H HA   . LEU   A 1 63  ? 9.579   16.081 4.678  1.00 24.66 ? 43  LEU   A HA   1 
ATOM   532  H HB2  . LEU   A 1 63  ? 9.466   13.321 4.186  1.00 27.84 ? 43  LEU   A HB2  1 
ATOM   533  H HB3  . LEU   A 1 63  ? 9.383   14.431 3.052  1.00 27.84 ? 43  LEU   A HB3  1 
ATOM   534  H HG   . LEU   A 1 63  ? 11.639  13.985 4.666  1.00 32.63 ? 43  LEU   A HG   1 
ATOM   535  H HD11 . LEU   A 1 63  ? 12.721  13.120 2.757  1.00 36.80 ? 43  LEU   A HD11 1 
ATOM   536  H HD12 . LEU   A 1 63  ? 11.460  12.234 3.140  1.00 36.80 ? 43  LEU   A HD12 1 
ATOM   537  H HD13 . LEU   A 1 63  ? 11.368  13.269 1.939  1.00 36.80 ? 43  LEU   A HD13 1 
ATOM   538  H HD21 . LEU   A 1 63  ? 12.787  15.450 3.121  1.00 34.51 ? 43  LEU   A HD21 1 
ATOM   539  H HD22 . LEU   A 1 63  ? 11.356  15.857 2.562  1.00 34.51 ? 43  LEU   A HD22 1 
ATOM   540  H HD23 . LEU   A 1 63  ? 11.745  16.187 4.066  1.00 34.51 ? 43  LEU   A HD23 1 
ATOM   541  N N    . LEU   A 1 64  ? 7.035   14.911 5.979  1.00 18.90 ? 44  LEU   A N    1 
ATOM   542  C CA   . LEU   A 1 64  ? 5.589   15.101 6.092  1.00 18.31 ? 44  LEU   A CA   1 
ATOM   543  C C    . LEU   A 1 64  ? 5.205   16.507 6.527  1.00 17.96 ? 44  LEU   A C    1 
ATOM   544  O O    . LEU   A 1 64  ? 4.001   16.789 6.637  1.00 18.84 ? 44  LEU   A O    1 
ATOM   545  C CB   . LEU   A 1 64  ? 5.004   14.081 7.066  1.00 18.75 ? 44  LEU   A CB   1 
ATOM   546  C CG   . LEU   A 1 64  ? 5.227   12.616 6.675  1.00 19.59 ? 44  LEU   A CG   1 
ATOM   547  C CD1  . LEU   A 1 64  ? 4.584   11.703 7.725  1.00 20.65 ? 44  LEU   A CD1  1 
ATOM   548  C CD2  . LEU   A 1 64  ? 4.720   12.282 5.257  1.00 21.47 ? 44  LEU   A CD2  1 
ATOM   549  H H    . LEU   A 1 64  ? 7.392   14.540 6.668  1.00 22.68 ? 44  LEU   A H    1 
ATOM   550  H HA   . LEU   A 1 64  ? 5.189   14.946 5.222  1.00 21.97 ? 44  LEU   A HA   1 
ATOM   551  H HB2  . LEU   A 1 64  ? 5.412   14.218 7.935  1.00 22.50 ? 44  LEU   A HB2  1 
ATOM   552  H HB3  . LEU   A 1 64  ? 4.046   14.226 7.123  1.00 22.50 ? 44  LEU   A HB3  1 
ATOM   553  H HG   . LEU   A 1 64  ? 6.183   12.451 6.651  1.00 23.51 ? 44  LEU   A HG   1 
ATOM   554  H HD11 . LEU   A 1 64  ? 4.723   10.778 7.466  1.00 24.78 ? 44  LEU   A HD11 1 
ATOM   555  H HD12 . LEU   A 1 64  ? 4.997   11.871 8.586  1.00 24.78 ? 44  LEU   A HD12 1 
ATOM   556  H HD13 . LEU   A 1 64  ? 3.634   11.895 7.770  1.00 24.78 ? 44  LEU   A HD13 1 
ATOM   557  H HD21 . LEU   A 1 64  ? 4.786   11.325 5.115  1.00 25.76 ? 44  LEU   A HD21 1 
ATOM   558  H HD22 . LEU   A 1 64  ? 3.795   12.565 5.178  1.00 25.76 ? 44  LEU   A HD22 1 
ATOM   559  H HD23 . LEU   A 1 64  ? 5.266   12.752 4.607  1.00 25.76 ? 44  LEU   A HD23 1 
ATOM   560  N N    . PHE   A 1 65  ? 6.184   17.366 6.799  1.00 18.46 ? 45  PHE   A N    1 
ATOM   561  C CA   . PHE   A 1 65  ? 5.989   18.734 7.255  1.00 18.17 ? 45  PHE   A CA   1 
ATOM   562  C C    . PHE   A 1 65  ? 6.264   19.725 6.126  1.00 19.41 ? 45  PHE   A C    1 
ATOM   563  O O    . PHE   A 1 65  ? 7.032   19.458 5.202  1.00 21.33 ? 45  PHE   A O    1 
ATOM   564  C CB   . PHE   A 1 65  ? 6.932   19.063 8.418  1.00 18.76 ? 45  PHE   A CB   1 
ATOM   565  C CG   . PHE   A 1 65  ? 6.585   18.380 9.712  1.00 18.56 ? 45  PHE   A CG   1 
ATOM   566  C CD1  . PHE   A 1 65  ? 6.875   17.034 9.894  1.00 19.82 ? 45  PHE   A CD1  1 
ATOM   567  C CD2  . PHE   A 1 65  ? 5.993   19.090 10.762 1.00 18.84 ? 45  PHE   A CD2  1 
ATOM   568  C CE1  . PHE   A 1 65  ? 6.572   16.404 11.090 1.00 20.22 ? 45  PHE   A CE1  1 
ATOM   569  C CE2  . PHE   A 1 65  ? 5.703   18.463 11.975 1.00 19.13 ? 45  PHE   A CE2  1 
ATOM   570  C CZ   . PHE   A 1 65  ? 5.973   17.122 12.129 1.00 19.69 ? 45  PHE   A CZ   1 
ATOM   571  H H    . PHE   A 1 65  ? 7.017   17.165 6.723  1.00 22.15 ? 45  PHE   A H    1 
ATOM   572  H HA   . PHE   A 1 65  ? 5.069   18.827 7.550  1.00 21.81 ? 45  PHE   A HA   1 
ATOM   573  H HB2  . PHE   A 1 65  ? 7.830   18.790 8.174  1.00 22.51 ? 45  PHE   A HB2  1 
ATOM   574  H HB3  . PHE   A 1 65  ? 6.907   20.020 8.575  1.00 22.51 ? 45  PHE   A HB3  1 
ATOM   575  H HD1  . PHE   A 1 65  ? 7.277   16.552 9.208  1.00 23.79 ? 45  PHE   A HD1  1 
ATOM   576  H HD2  . PHE   A 1 65  ? 5.789   19.991 10.650 1.00 22.61 ? 45  PHE   A HD2  1 
ATOM   577  H HE1  . PHE   A 1 65  ? 6.767   15.501 11.202 1.00 24.26 ? 45  PHE   A HE1  1 
ATOM   578  H HE2  . PHE   A 1 65  ? 5.330   18.949 12.675 1.00 22.96 ? 45  PHE   A HE2  1 
ATOM   579  H HZ   . PHE   A 1 65  ? 5.757   16.693 12.925 1.00 23.63 ? 45  PHE   A HZ   1 
ATOM   580  N N    . THR   A 1 66  ? 5.652   20.906 6.246  1.00 20.20 ? 46  THR   A N    1 
ATOM   581  C CA   . THR   A 1 66  ? 6.072   22.044 5.429  1.00 21.58 ? 46  THR   A CA   1 
ATOM   582  C C    . THR   A 1 66  ? 7.503   22.436 5.818  1.00 21.98 ? 46  THR   A C    1 
ATOM   583  O O    . THR   A 1 66  ? 8.016   22.050 6.866  1.00 21.94 ? 46  THR   A O    1 
ATOM   584  C CB   . THR   A 1 66  ? 5.153   23.239 5.684  1.00 23.67 ? 46  THR   A CB   1 
ATOM   585  O OG1  . THR   A 1 66  ? 5.246   23.625 7.065  1.00 24.37 ? 46  THR   A OG1  1 
ATOM   586  C CG2  . THR   A 1 66  ? 3.693   22.910 5.358  1.00 24.62 ? 46  THR   A CG2  1 
ATOM   587  H H    . THR   A 1 66  ? 5.001   21.071 6.784  1.00 24.25 ? 46  THR   A H    1 
ATOM   588  H HA   . THR   A 1 66  ? 6.034   21.813 4.487  1.00 25.90 ? 46  THR   A HA   1 
ATOM   589  H HB   . THR   A 1 66  ? 5.427   23.971 5.110  1.00 28.40 ? 46  THR   A HB   1 
ATOM   590  H HG1  . THR   A 1 66  ? 4.744   24.282 7.214  1.00 29.24 ? 46  THR   A HG1  1 
ATOM   591  H HG21 . THR   A 1 66  ? 3.140   23.697 5.479  1.00 29.54 ? 46  THR   A HG21 1 
ATOM   592  H HG22 . THR   A 1 66  ? 3.618   22.610 4.438  1.00 29.54 ? 46  THR   A HG22 1 
ATOM   593  H HG23 . THR   A 1 66  ? 3.372   22.207 5.945  1.00 29.54 ? 46  THR   A HG23 1 
ATOM   594  N N    . GLU   A 1 67  ? 8.157   23.226 4.970  1.00 23.74 ? 47  GLU   A N    1 
ATOM   595  C CA   . GLU   A 1 67  ? 9.541   23.581 5.256  1.00 24.75 ? 47  GLU   A CA   1 
ATOM   596  C C    . GLU   A 1 67  ? 9.686   24.309 6.582  1.00 24.97 ? 47  GLU   A C    1 
ATOM   597  O O    . GLU   A 1 67  ? 10.686  24.124 7.292  1.00 25.97 ? 47  GLU   A O    1 
ATOM   598  C CB   . GLU   A 1 67  ? 10.103  24.477 4.141  1.00 26.82 ? 47  GLU   A CB   1 
ATOM   599  C CG   . GLU   A 1 67  ? 11.608  24.746 4.268  1.00 31.29 ? 47  GLU   A CG   1 
ATOM   600  C CD   . GLU   A 1 67  ? 12.454  23.484 4.007  1.00 50.00 ? 47  GLU   A CD   1 
ATOM   601  O OE1  . GLU   A 1 67  ? 12.168  22.738 3.034  1.00 60.89 ? 47  GLU   A OE1  1 
ATOM   602  O OE2  . GLU   A 1 67  ? 13.404  23.234 4.782  1.00 61.19 ? 47  GLU   A OE2  1 
ATOM   603  H H    . GLU   A 1 67  ? 7.833   23.559 4.246  1.00 28.48 ? 47  GLU   A H    1 
ATOM   604  H HA   . GLU   A 1 67  ? 10.047  22.755 5.295  1.00 29.70 ? 47  GLU   A HA   1 
ATOM   605  H HB2  . GLU   A 1 67  ? 9.950   24.045 3.286  1.00 32.18 ? 47  GLU   A HB2  1 
ATOM   606  H HB3  . GLU   A 1 67  ? 9.646   25.332 4.167  1.00 32.18 ? 47  GLU   A HB3  1 
ATOM   607  H HG2  . GLU   A 1 67  ? 11.865  25.421 3.620  1.00 37.55 ? 47  GLU   A HG2  1 
ATOM   608  H HG3  . GLU   A 1 67  ? 11.800  25.057 5.166  1.00 37.55 ? 47  GLU   A HG3  1 
ATOM   609  N N    . ASP   A 1 68  ? 8.707   25.140 6.935  1.00 26.55 ? 48  ASP   A N    1 
ATOM   610  C CA   . ASP   A 1 68  ? 8.714   25.866 8.195  1.00 27.11 ? 48  ASP   A CA   1 
ATOM   611  C C    . ASP   A 1 68  ? 7.854   25.191 9.265  1.00 25.20 ? 48  ASP   A C    1 
ATOM   612  O O    . ASP   A 1 68  ? 7.480   25.830 10.255 1.00 25.94 ? 48  ASP   A O    1 
ATOM   613  C CB   . ASP   A 1 68  ? 8.261   27.306 7.971  1.00 31.47 ? 48  ASP   A CB   1 
ATOM   614  C CG   . ASP   A 1 68  ? 6.812   27.416 7.481  1.00 36.70 ? 48  ASP   A CG   1 
ATOM   615  O OD1  . ASP   A 1 68  ? 6.135   26.396 7.205  1.00 37.67 ? 48  ASP   A OD1  1 
ATOM   616  O OD2  . ASP   A 1 68  ? 6.343   28.564 7.364  1.00 41.63 ? 48  ASP   A OD2  1 
ATOM   617  H H    . ASP   A 1 68  ? 8.016   25.300 6.449  1.00 31.86 ? 48  ASP   A H    1 
ATOM   618  H HA   . ASP   A 1 68  ? 9.624   25.891 8.531  1.00 32.53 ? 48  ASP   A HA   1 
ATOM   619  H HB2  . ASP   A 1 68  ? 8.330   27.791 8.808  1.00 37.76 ? 48  ASP   A HB2  1 
ATOM   620  H HB3  . ASP   A 1 68  ? 8.833   27.715 7.302  1.00 37.76 ? 48  ASP   A HB3  1 
ATOM   621  N N    . GLY   A 1 69  ? 7.525   23.916 9.061  1.00 22.21 ? 49  GLY   A N    1 
ATOM   622  C CA   . GLY   A 1 69  ? 6.687   23.210 10.012 1.00 21.51 ? 49  GLY   A CA   1 
ATOM   623  C C    . GLY   A 1 69  ? 7.352   23.054 11.366 1.00 20.49 ? 49  GLY   A C    1 
ATOM   624  O O    . GLY   A 1 69  ? 8.579   23.039 11.494 1.00 22.21 ? 49  GLY   A O    1 
ATOM   625  H H    . GLY   A 1 69  ? 7.774   23.445 8.386  1.00 26.65 ? 49  GLY   A H    1 
ATOM   626  H HA2  . GLY   A 1 69  ? 5.858   23.699 10.134 1.00 25.82 ? 49  GLY   A HA2  1 
ATOM   627  H HA3  . GLY   A 1 69  ? 6.484   22.326 9.668  1.00 25.82 ? 49  GLY   A HA3  1 
ATOM   628  N N    . VAL   A 1 70  ? 6.516   22.924 12.385 1.00 19.53 ? 50  VAL   A N    1 
ATOM   629  C CA   . VAL   A 1 70  ? 6.941   22.836 13.770 1.00 19.34 ? 50  VAL   A CA   1 
ATOM   630  C C    . VAL   A 1 70  ? 6.349   21.569 14.370 1.00 18.63 ? 50  VAL   A C    1 
ATOM   631  O O    . VAL   A 1 70  ? 5.174   21.253 14.147 1.00 19.21 ? 50  VAL   A O    1 
ATOM   632  C CB   . VAL   A 1 70  ? 6.477   24.073 14.574 1.00 21.80 ? 50  VAL   A CB   1 
ATOM   633  C CG1  . VAL   A 1 70  ? 6.852   23.940 16.045 1.00 24.64 ? 50  VAL   A CG1  1 
ATOM   634  C CG2  . VAL   A 1 70  ? 7.023   25.371 13.980 1.00 24.51 ? 50  VAL   A CG2  1 
ATOM   635  H H    . VAL   A 1 70  ? 5.662   22.883 12.294 1.00 23.44 ? 50  VAL   A H    1 
ATOM   636  H HA   . VAL   A 1 70  ? 7.909   22.779 13.814 1.00 23.21 ? 50  VAL   A HA   1 
ATOM   637  H HB   . VAL   A 1 70  ? 5.510   24.120 14.516 1.00 26.16 ? 50  VAL   A HB   1 
ATOM   638  H HG11 . VAL   A 1 70  ? 6.720   24.796 16.483 1.00 29.57 ? 50  VAL   A HG11 1 
ATOM   639  H HG12 . VAL   A 1 70  ? 6.286   23.268 16.456 1.00 29.57 ? 50  VAL   A HG12 1 
ATOM   640  H HG13 . VAL   A 1 70  ? 7.782   23.674 16.112 1.00 29.57 ? 50  VAL   A HG13 1 
ATOM   641  H HG21 . VAL   A 1 70  ? 6.723   26.117 14.522 1.00 29.42 ? 50  VAL   A HG21 1 
ATOM   642  H HG22 . VAL   A 1 70  ? 7.992   25.333 13.976 1.00 29.42 ? 50  VAL   A HG22 1 
ATOM   643  H HG23 . VAL   A 1 70  ? 6.692   25.467 13.073 1.00 29.42 ? 50  VAL   A HG23 1 
ATOM   644  N N    . GLY   A 1 71  ? 7.169   20.858 15.145 1.00 18.57 ? 51  GLY   A N    1 
ATOM   645  C CA   . GLY   A 1 71  ? 6.712   19.713 15.899 1.00 17.96 ? 51  GLY   A CA   1 
ATOM   646  C C    . GLY   A 1 71  ? 7.266   19.777 17.313 1.00 18.81 ? 51  GLY   A C    1 
ATOM   647  O O    . GLY   A 1 71  ? 8.164   20.542 17.583 1.00 24.38 ? 51  GLY   A O    1 
ATOM   648  H H    . GLY   A 1 71  ? 8.006   21.029 15.246 1.00 22.28 ? 51  GLY   A H    1 
ATOM   649  H HA2  . GLY   A 1 71  ? 5.742   19.707 15.939 1.00 21.55 ? 51  GLY   A HA2  1 
ATOM   650  H HA3  . GLY   A 1 71  ? 7.015   18.894 15.476 1.00 21.55 ? 51  GLY   A HA3  1 
ATOM   651  N N    . GLY   A 1 72  ? 6.726   18.974 18.204 1.00 18.23 ? 52  GLY   A N    1 
ATOM   652  C CA   . GLY   A 1 72  ? 7.359   18.837 19.496 1.00 18.38 ? 52  GLY   A CA   1 
ATOM   653  C C    . GLY   A 1 72  ? 6.395   18.516 20.617 1.00 17.95 ? 52  GLY   A C    1 
ATOM   654  O O    . GLY   A 1 72  ? 5.247   18.125 20.397 1.00 18.16 ? 52  GLY   A O    1 
ATOM   655  H H    . GLY   A 1 72  ? 6.012   18.510 18.088 1.00 21.87 ? 52  GLY   A H    1 
ATOM   656  H HA2  . GLY   A 1 72  ? 8.015   18.123 19.453 1.00 22.05 ? 52  GLY   A HA2  1 
ATOM   657  H HA3  . GLY   A 1 72  ? 7.809   19.667 19.718 1.00 22.05 ? 52  GLY   A HA3  1 
ATOM   658  N N    . LEU   A 1 73  ? 6.908   18.696 21.837 1.00 17.59 ? 53  LEU   A N    1 
ATOM   659  C CA   . LEU   A 1 73  ? 6.302   18.228 23.080 1.00 17.86 ? 53  LEU   A CA   1 
ATOM   660  C C    . LEU   A 1 73  ? 5.797   19.437 23.859 1.00 17.43 ? 53  LEU   A C    1 
ATOM   661  O O    . LEU   A 1 73  ? 6.575   20.317 24.235 1.00 18.70 ? 53  LEU   A O    1 
ATOM   662  C CB   . LEU   A 1 73  ? 7.329   17.446 23.899 1.00 18.39 ? 53  LEU   A CB   1 
ATOM   663  C CG   . LEU   A 1 73  ? 6.834   16.994 25.268 1.00 18.99 ? 53  LEU   A CG   1 
ATOM   664  C CD1  . LEU   A 1 73  ? 5.637   16.085 25.162 1.00 18.75 ? 53  LEU   A CD1  1 
ATOM   665  C CD2  . LEU   A 1 73  ? 7.997   16.316 25.972 1.00 21.11 ? 53  LEU   A CD2  1 
ATOM   666  H H    . LEU   A 1 73  ? 7.650   19.109 21.974 1.00 21.11 ? 53  LEU   A H    1 
ATOM   667  H HA   . LEU   A 1 73  ? 5.546   17.651 22.891 1.00 21.43 ? 53  LEU   A HA   1 
ATOM   668  H HB2  . LEU   A 1 73  ? 7.580   16.652 23.401 1.00 22.07 ? 53  LEU   A HB2  1 
ATOM   669  H HB3  . LEU   A 1 73  ? 8.106   18.009 24.039 1.00 22.07 ? 53  LEU   A HB3  1 
ATOM   670  H HG   . LEU   A 1 73  ? 6.532   17.754 25.789 1.00 22.79 ? 53  LEU   A HG   1 
ATOM   671  H HD11 . LEU   A 1 73  ? 5.402   15.767 26.047 1.00 22.51 ? 53  LEU   A HD11 1 
ATOM   672  H HD12 . LEU   A 1 73  ? 4.896   16.583 24.782 1.00 22.51 ? 53  LEU   A HD12 1 
ATOM   673  H HD13 . LEU   A 1 73  ? 5.859   15.335 24.589 1.00 22.51 ? 53  LEU   A HD13 1 
ATOM   674  H HD21 . LEU   A 1 73  ? 7.738   16.114 26.885 1.00 25.33 ? 53  LEU   A HD21 1 
ATOM   675  H HD22 . LEU   A 1 73  ? 8.217   15.497 25.502 1.00 25.33 ? 53  LEU   A HD22 1 
ATOM   676  H HD23 . LEU   A 1 73  ? 8.760   16.915 25.970 1.00 25.33 ? 53  LEU   A HD23 1 
ATOM   677  N N    . TRP   A 1 74  ? 4.473   19.494 24.071 1.00 17.27 ? 54  TRP   A N    1 
ATOM   678  C CA   . TRP   A 1 74  ? 3.884   20.669 24.692 1.00 18.50 ? 54  TRP   A CA   1 
ATOM   679  C C    . TRP   A 1 74  ? 3.745   20.550 26.202 1.00 19.98 ? 54  TRP   A C    1 
ATOM   680  O O    . TRP   A 1 74  ? 3.368   21.530 26.833 1.00 23.99 ? 54  TRP   A O    1 
ATOM   681  C CB   . TRP   A 1 74  ? 2.519   20.955 24.030 1.00 18.04 ? 54  TRP   A CB   1 
ATOM   682  C CG   . TRP   A 1 74  ? 2.607   22.157 23.102 1.00 18.41 ? 54  TRP   A CG   1 
ATOM   683  C CD1  . TRP   A 1 74  ? 1.947   23.339 23.238 1.00 20.87 ? 54  TRP   A CD1  1 
ATOM   684  C CD2  . TRP   A 1 74  ? 3.440   22.301 21.928 1.00 18.59 ? 54  TRP   A CD2  1 
ATOM   685  N NE1  . TRP   A 1 74  ? 2.289   24.197 22.224 1.00 21.91 ? 54  TRP   A NE1  1 
ATOM   686  C CE2  . TRP   A 1 74  ? 3.211   23.592 21.408 1.00 21.05 ? 54  TRP   A CE2  1 
ATOM   687  C CE3  . TRP   A 1 74  ? 4.331   21.451 21.247 1.00 19.85 ? 54  TRP   A CE3  1 
ATOM   688  C CZ2  . TRP   A 1 74  ? 3.871   24.074 20.262 1.00 23.13 ? 54  TRP   A CZ2  1 
ATOM   689  C CZ3  . TRP   A 1 74  ? 4.987   21.932 20.109 1.00 21.05 ? 54  TRP   A CZ3  1 
ATOM   690  C CH2  . TRP   A 1 74  ? 4.750   23.232 19.636 1.00 22.73 ? 54  TRP   A CH2  1 
ATOM   691  H H    . TRP   A 1 74  ? 3.914   18.874 23.865 1.00 20.73 ? 54  TRP   A H    1 
ATOM   692  H HA   . TRP   A 1 74  ? 4.453   21.440 24.539 1.00 22.21 ? 54  TRP   A HA   1 
ATOM   693  H HB2  . TRP   A 1 74  ? 2.245   20.184 23.510 1.00 21.65 ? 54  TRP   A HB2  1 
ATOM   694  H HB3  . TRP   A 1 74  ? 1.860   21.143 24.717 1.00 21.65 ? 54  TRP   A HB3  1 
ATOM   695  H HD1  . TRP   A 1 74  ? 1.348   23.537 23.922 1.00 25.05 ? 54  TRP   A HD1  1 
ATOM   696  H HE1  . TRP   A 1 74  ? 1.975   24.990 22.117 1.00 26.30 ? 54  TRP   A HE1  1 
ATOM   697  H HE3  . TRP   A 1 74  ? 4.482   20.584 21.548 1.00 23.82 ? 54  TRP   A HE3  1 
ATOM   698  H HZ2  . TRP   A 1 74  ? 3.716   24.934 19.941 1.00 27.76 ? 54  TRP   A HZ2  1 
ATOM   699  H HZ3  . TRP   A 1 74  ? 5.588   21.383 19.660 1.00 25.26 ? 54  TRP   A HZ3  1 
ATOM   700  H HH2  . TRP   A 1 74  ? 5.201   23.528 18.879 1.00 27.28 ? 54  TRP   A HH2  1 
ATOM   701  N N    . THR   A 1 75  ? 4.056   19.408 26.791 1.00 17.27 ? 55  THR   A N    1 
ATOM   702  C CA   . THR   A 1 75  ? 3.892   19.150 28.222 1.00 17.17 ? 55  THR   A CA   1 
ATOM   703  C C    . THR   A 1 75  ? 5.244   18.688 28.759 1.00 17.53 ? 55  THR   A C    1 
ATOM   704  O O    . THR   A 1 75  ? 5.631   17.539 28.535 1.00 18.67 ? 55  THR   A O    1 
ATOM   705  C CB   . THR   A 1 75  ? 2.831   18.086 28.431 1.00 16.65 ? 55  THR   A CB   1 
ATOM   706  O OG1  . THR   A 1 75  ? 3.091   16.975 27.578 1.00 16.30 ? 55  THR   A OG1  1 
ATOM   707  C CG2  . THR   A 1 75  ? 1.427   18.575 28.122 1.00 17.26 ? 55  THR   A CG2  1 
ATOM   708  H H    . THR   A 1 75  ? 4.380   18.733 26.368 1.00 20.73 ? 55  THR   A H    1 
ATOM   709  H HA   . THR   A 1 75  ? 3.633   19.961 28.689 1.00 20.60 ? 55  THR   A HA   1 
ATOM   710  H HB   . THR   A 1 75  ? 2.863   17.834 29.367 1.00 19.98 ? 55  THR   A HB   1 
ATOM   711  H HG1  . THR   A 1 75  ? 3.832   16.631 27.773 1.00 19.57 ? 55  THR   A HG1  1 
ATOM   712  H HG21 . THR   A 1 75  ? 0.785   17.867 28.288 1.00 20.71 ? 55  THR   A HG21 1 
ATOM   713  H HG22 . THR   A 1 75  ? 1.209   19.335 28.685 1.00 20.71 ? 55  THR   A HG22 1 
ATOM   714  H HG23 . THR   A 1 75  ? 1.366   18.844 27.192 1.00 20.71 ? 55  THR   A HG23 1 
ATOM   715  N N    . THR   A 1 76  ? 5.954   19.559 29.475 1.00 19.11 ? 56  THR   A N    1 
ATOM   716  C CA   . THR   A 1 76  ? 7.281   19.246 29.982 1.00 19.79 ? 56  THR   A CA   1 
ATOM   717  C C    . THR   A 1 76  ? 7.375   19.652 31.446 1.00 19.78 ? 56  THR   A C    1 
ATOM   718  O O    . THR   A 1 76  ? 6.538   20.379 31.989 1.00 20.53 ? 56  THR   A O    1 
ATOM   719  C CB   . THR   A 1 76  ? 8.404   19.981 29.205 1.00 24.06 ? 56  THR   A CB   1 
ATOM   720  O OG1  . THR   A 1 76  ? 8.371   21.374 29.540 1.00 29.67 ? 56  THR   A OG1  1 
ATOM   721  C CG2  . THR   A 1 76  ? 8.265   19.797 27.709 1.00 24.72 ? 56  THR   A CG2  1 
ATOM   722  H H    . THR   A 1 76  ? 5.680   20.348 29.681 1.00 22.93 ? 56  THR   A H    1 
ATOM   723  H HA   . THR   A 1 76  ? 7.410   18.289 29.893 1.00 23.75 ? 56  THR   A HA   1 
ATOM   724  H HB   . THR   A 1 76  ? 9.263   19.606 29.453 1.00 28.88 ? 56  THR   A HB   1 
ATOM   725  H HG1  . THR   A 1 76  ? 8.964   21.787 29.111 1.00 35.60 ? 56  THR   A HG1  1 
ATOM   726  H HG21 . THR   A 1 76  ? 9.015   20.209 27.253 1.00 29.67 ? 56  THR   A HG21 1 
ATOM   727  H HG22 . THR   A 1 76  ? 8.245   18.852 27.491 1.00 29.67 ? 56  THR   A HG22 1 
ATOM   728  H HG23 . THR   A 1 76  ? 7.443   20.209 27.399 1.00 29.67 ? 56  THR   A HG23 1 
ATOM   729  N N    . ASP   A 1 77  ? 8.484   19.244 32.055 1.00 20.21 ? 57  ASP   A N    1 
ATOM   730  C CA   . ASP   A 1 77  ? 8.741   19.578 33.447 1.00 23.01 ? 57  ASP   A CA   1 
ATOM   731  C C    . ASP   A 1 77  ? 8.799   21.078 33.655 1.00 24.18 ? 57  ASP   A C    1 
ATOM   732  O O    . ASP   A 1 77  ? 8.322   21.586 34.674 1.00 26.61 ? 57  ASP   A O    1 
ATOM   733  C CB   . ASP   A 1 77  ? 10.019  18.897 33.971 1.00 23.81 ? 57  ASP   A CB   1 
ATOM   734  C CG   . ASP   A 1 77  ? 11.288  19.293 33.240 1.00 26.63 ? 57  ASP   A CG   1 
ATOM   735  O OD1  . ASP   A 1 77  ? 11.404  19.127 32.038 1.00 30.29 ? 57  ASP   A OD1  1 
ATOM   736  O OD2  . ASP   A 1 77  ? 12.205  19.794 33.903 1.00 29.95 ? 57  ASP   A OD2  1 
ATOM   737  H H    . ASP   A 1 77  ? 9.102   18.773 31.684 1.00 24.25 ? 57  ASP   A H    1 
ATOM   738  H HA   . ASP   A 1 77  ? 8.006   19.228 33.975 1.00 27.61 ? 57  ASP   A HA   1 
ATOM   739  H HB2  . ASP   A 1 77  ? 10.134  19.131 34.905 1.00 28.58 ? 57  ASP   A HB2  1 
ATOM   740  H HB3  . ASP   A 1 77  ? 9.917   17.936 33.880 1.00 28.58 ? 57  ASP   A HB3  1 
ATOM   741  N N    . SER   A 1 78  ? 9.382   21.806 32.708 1.00 25.34 ? 58  SER   A N    1 
ATOM   742  C CA   . SER   A 1 78  ? 9.605   23.222 32.919 1.00 28.72 ? 58  SER   A CA   1 
ATOM   743  C C    . SER   A 1 78  ? 8.352   24.043 32.697 1.00 27.47 ? 58  SER   A C    1 
ATOM   744  O O    . SER   A 1 78  ? 8.312   25.207 33.108 1.00 31.79 ? 58  SER   A O    1 
ATOM   745  C CB   . SER   A 1 78  ? 10.693  23.691 31.949 1.00 30.32 ? 58  SER   A CB   1 
ATOM   746  O OG   . SER   A 1 78  ? 10.244  23.606 30.605 1.00 32.16 ? 58  SER   A OG   1 
ATOM   747  H H    . SER   A 1 78  ? 9.653   21.504 31.950 1.00 30.41 ? 58  SER   A H    1 
ATOM   748  H HA   . SER   A 1 78  ? 9.900   23.376 33.830 1.00 34.47 ? 58  SER   A HA   1 
ATOM   749  H HB2  . SER   A 1 78  ? 10.918  24.614 32.149 1.00 36.38 ? 58  SER   A HB2  1 
ATOM   750  H HB3  . SER   A 1 78  ? 11.476  23.128 32.057 1.00 36.38 ? 58  SER   A HB3  1 
ATOM   751  H HG   . SER   A 1 78  ? 10.057  22.809 30.415 1.00 38.60 ? 58  SER   A HG   1 
ATOM   752  N N    . GLY   A 1 79  ? 7.341   23.475 32.046 1.00 25.94 ? 59  GLY   A N    1 
ATOM   753  C CA   . GLY   A 1 79  ? 6.148   24.207 31.692 1.00 26.15 ? 59  GLY   A CA   1 
ATOM   754  C C    . GLY   A 1 79  ? 6.185   24.931 30.355 1.00 29.77 ? 59  GLY   A C    1 
ATOM   755  O O    . GLY   A 1 79  ? 5.190   25.568 29.986 1.00 33.92 ? 59  GLY   A O    1 
ATOM   756  H H    . GLY   A 1 79  ? 7.329   22.652 31.799 1.00 31.13 ? 59  GLY   A H    1 
ATOM   757  H HA2  . GLY   A 1 79  ? 5.404   23.585 31.666 1.00 31.38 ? 59  GLY   A HA2  1 
ATOM   758  H HA3  . GLY   A 1 79  ? 5.981   24.871 32.378 1.00 31.38 ? 59  GLY   A HA3  1 
ATOM   759  N N    . GLN   A 1 80  ? 7.287   24.885 29.638 1.00 27.04 ? 60  GLN   A N    1 
ATOM   760  C CA   . GLN   A 1 80  ? 7.373   25.452 28.299 1.00 29.34 ? 60  GLN   A CA   1 
ATOM   761  C C    . GLN   A 1 80  ? 7.466   24.334 27.276 1.00 25.61 ? 60  GLN   A C    1 
ATOM   762  O O    . GLN   A 1 80  ? 8.129   23.325 27.533 1.00 27.32 ? 60  GLN   A O    1 
ATOM   763  C CB   . GLN   A 1 80  ? 8.622   26.327 28.145 1.00 33.26 ? 60  GLN   A CB   1 
ATOM   764  C CG   . GLN   A 1 80  ? 8.643   27.532 29.066 1.00 38.82 ? 60  GLN   A CG   1 
ATOM   765  C CD   . GLN   A 1 80  ? 7.434   28.427 28.866 1.00 44.27 ? 60  GLN   A CD   1 
ATOM   766  O OE1  . GLN   A 1 80  ? 6.786   28.839 29.829 1.00 48.28 ? 60  GLN   A OE1  1 
ATOM   767  N NE2  . GLN   A 1 80  ? 7.132   28.744 27.611 1.00 45.41 ? 60  GLN   A NE2  1 
ATOM   768  H H    . GLN   A 1 80  ? 8.020   24.523 29.906 1.00 32.45 ? 60  GLN   A H    1 
ATOM   769  H HA   . GLN   A 1 80  ? 6.589   25.997 28.131 1.00 35.21 ? 60  GLN   A HA   1 
ATOM   770  H HB2  . GLN   A 1 80  ? 9.405   25.789 28.343 1.00 39.91 ? 60  GLN   A HB2  1 
ATOM   771  H HB3  . GLN   A 1 80  ? 8.665   26.651 27.232 1.00 39.91 ? 60  GLN   A HB3  1 
ATOM   772  H HG2  . GLN   A 1 80  ? 8.645   27.228 29.988 1.00 46.58 ? 60  GLN   A HG2  1 
ATOM   773  H HG3  . GLN   A 1 80  ? 9.440   28.055 28.888 1.00 46.58 ? 60  GLN   A HG3  1 
ATOM   774  H HE21 . GLN   A 1 80  ? 7.613   28.444 26.964 1.00 54.50 ? 60  GLN   A HE21 1 
ATOM   775  H HE22 . GLN   A 1 80  ? 6.456   29.249 27.445 1.00 54.50 ? 60  GLN   A HE22 1 
ATOM   776  N N    . PRO   A 1 81  ? 6.835   24.480 26.111 1.00 25.07 ? 61  PRO   A N    1 
ATOM   777  C CA   . PRO   A 1 81  ? 6.985   23.458 25.071 1.00 23.22 ? 61  PRO   A CA   1 
ATOM   778  C C    . PRO   A 1 81  ? 8.422   23.337 24.594 1.00 23.32 ? 61  PRO   A C    1 
ATOM   779  O O    . PRO   A 1 81  ? 9.192   24.301 24.611 1.00 25.59 ? 61  PRO   A O    1 
ATOM   780  C CB   . PRO   A 1 81  ? 6.088   23.967 23.932 1.00 25.68 ? 61  PRO   A CB   1 
ATOM   781  C CG   . PRO   A 1 81  ? 5.078   24.871 24.617 1.00 30.40 ? 61  PRO   A CG   1 
ATOM   782  C CD   . PRO   A 1 81  ? 5.888   25.538 25.717 1.00 28.69 ? 61  PRO   A CD   1 
ATOM   783  H HA   . PRO   A 1 81  ? 6.669   22.602 25.400 1.00 27.86 ? 61  PRO   A HA   1 
ATOM   784  H HB2  . PRO   A 1 81  ? 6.619   24.462 23.289 1.00 30.81 ? 61  PRO   A HB2  1 
ATOM   785  H HB3  . PRO   A 1 81  ? 5.649   23.221 23.496 1.00 30.81 ? 61  PRO   A HB3  1 
ATOM   786  H HG2  . PRO   A 1 81  ? 4.730   25.524 23.990 1.00 36.48 ? 61  PRO   A HG2  1 
ATOM   787  H HG3  . PRO   A 1 81  ? 4.350   24.345 24.985 1.00 36.48 ? 61  PRO   A HG3  1 
ATOM   788  H HD2  . PRO   A 1 81  ? 6.358   26.316 25.379 1.00 34.43 ? 61  PRO   A HD2  1 
ATOM   789  H HD3  . PRO   A 1 81  ? 5.320   25.790 26.462 1.00 34.43 ? 61  PRO   A HD3  1 
ATOM   790  N N    . ILE   A 1 82  ? 8.757   22.133 24.139 1.00 21.61 ? 62  ILE   A N    1 
ATOM   791  C CA   . ILE   A 1 82  ? 9.974   21.883 23.373 1.00 22.70 ? 62  ILE   A CA   1 
ATOM   792  C C    . ILE   A 1 82  ? 9.530   21.836 21.925 1.00 21.89 ? 62  ILE   A C    1 
ATOM   793  O O    . ILE   A 1 82  ? 8.959   20.843 21.467 1.00 23.11 ? 62  ILE   A O    1 
ATOM   794  C CB   . ILE   A 1 82  ? 10.658  20.582 23.777 1.00 26.42 ? 62  ILE   A CB   1 
ATOM   795  C CG1  . ILE   A 1 82  ? 11.085  20.703 25.231 1.00 28.62 ? 62  ILE   A CG1  1 
ATOM   796  C CG2  . ILE   A 1 82  ? 11.870  20.293 22.883 1.00 28.72 ? 62  ILE   A CG2  1 
ATOM   797  C CD1  . ILE   A 1 82  ? 11.451  19.383 25.866 1.00 32.53 ? 62  ILE   A CD1  1 
ATOM   798  H H    . ILE   A 1 82  ? 8.283   21.427 24.265 1.00 25.93 ? 62  ILE   A H    1 
ATOM   799  H HA   . ILE   A 1 82  ? 10.604  22.608 23.512 1.00 27.25 ? 62  ILE   A HA   1 
ATOM   800  H HB   . ILE   A 1 82  ? 10.038  19.844 23.670 1.00 31.71 ? 62  ILE   A HB   1 
ATOM   801  H HG12 . ILE   A 1 82  ? 11.862  21.282 25.281 1.00 34.34 ? 62  ILE   A HG12 1 
ATOM   802  H HG13 . ILE   A 1 82  ? 10.353  21.084 25.741 1.00 34.34 ? 62  ILE   A HG13 1 
ATOM   803  H HG21 . ILE   A 1 82  ? 12.355  19.534 23.242 1.00 34.47 ? 62  ILE   A HG21 1 
ATOM   804  H HG22 . ILE   A 1 82  ? 11.560  20.093 21.986 1.00 34.47 ? 62  ILE   A HG22 1 
ATOM   805  H HG23 . ILE   A 1 82  ? 12.444  21.075 22.867 1.00 34.47 ? 62  ILE   A HG23 1 
ATOM   806  H HD11 . ILE   A 1 82  ? 11.622  19.524 26.810 1.00 39.04 ? 62  ILE   A HD11 1 
ATOM   807  H HD12 . ILE   A 1 82  ? 10.715  18.763 25.752 1.00 39.04 ? 62  ILE   A HD12 1 
ATOM   808  H HD13 . ILE   A 1 82  ? 12.247  19.035 25.434 1.00 39.04 ? 62  ILE   A HD13 1 
ATOM   809  N N    . ALA   A 1 83  ? 9.733   22.936 21.218 1.00 22.59 ? 63  ALA   A N    1 
ATOM   810  C CA   . ALA   A 1 83  ? 9.265   23.085 19.854 1.00 24.51 ? 63  ALA   A CA   1 
ATOM   811  C C    . ALA   A 1 83  ? 10.471  22.963 18.943 1.00 25.13 ? 63  ALA   A C    1 
ATOM   812  O O    . ALA   A 1 83  ? 11.465  23.670 19.124 1.00 27.98 ? 63  ALA   A O    1 
ATOM   813  C CB   . ALA   A 1 83  ? 8.600   24.450 19.661 1.00 28.15 ? 63  ALA   A CB   1 
ATOM   814  H H    . ALA   A 1 83  ? 10.151  23.626 21.516 1.00 27.11 ? 63  ALA   A H    1 
ATOM   815  H HA   . ALA   A 1 83  ? 8.616   22.398 19.633 1.00 29.42 ? 63  ALA   A HA   1 
ATOM   816  H HB1  . ALA   A 1 83  ? 8.303   24.529 18.741 1.00 33.78 ? 63  ALA   A HB1  1 
ATOM   817  H HB2  . ALA   A 1 83  ? 7.840   24.519 20.260 1.00 33.78 ? 63  ALA   A HB2  1 
ATOM   818  H HB3  . ALA   A 1 83  ? 9.244   25.146 19.862 1.00 33.78 ? 63  ALA   A HB3  1 
ATOM   819  N N    . ILE   A 1 84  ? 10.365  22.081 17.967 1.00 22.39 ? 64  ILE   A N    1 
ATOM   820  C CA   . ILE   A 1 84  ? 11.410  21.806 16.997 1.00 23.41 ? 64  ILE   A CA   1 
ATOM   821  C C    . ILE   A 1 84  ? 10.952  22.504 15.720 1.00 22.64 ? 64  ILE   A C    1 
ATOM   822  O O    . ILE   A 1 84  ? 9.930   22.135 15.128 1.00 22.97 ? 64  ILE   A O    1 
ATOM   823  C CB   . ILE   A 1 84  ? 11.582  20.291 16.807 1.00 26.43 ? 64  ILE   A CB   1 
ATOM   824  C CG1  . ILE   A 1 84  ? 11.738  19.553 18.162 1.00 29.89 ? 64  ILE   A CG1  1 
ATOM   825  C CG2  . ILE   A 1 84  ? 12.753  20.024 15.868 1.00 28.46 ? 64  ILE   A CG2  1 
ATOM   826  C CD1  . ILE   A 1 84  ? 12.952  19.916 18.899 1.00 35.11 ? 64  ILE   A CD1  1 
ATOM   827  H H    . ILE   A 1 84  ? 9.661   21.604 17.838 1.00 26.87 ? 64  ILE   A H    1 
ATOM   828  H HA   . ILE   A 1 84  ? 12.268  22.166 17.268 1.00 28.09 ? 64  ILE   A HA   1 
ATOM   829  H HB   . ILE   A 1 84  ? 10.775  19.936 16.403 1.00 31.72 ? 64  ILE   A HB   1 
ATOM   830  H HG12 . ILE   A 1 84  ? 10.976  19.767 18.723 1.00 35.87 ? 64  ILE   A HG12 1 
ATOM   831  H HG13 . ILE   A 1 84  ? 11.769  18.598 17.994 1.00 35.87 ? 64  ILE   A HG13 1 
ATOM   832  H HG21 . ILE   A 1 84  ? 12.915  19.069 15.829 1.00 34.15 ? 64  ILE   A HG21 1 
ATOM   833  H HG22 . ILE   A 1 84  ? 12.532  20.359 14.985 1.00 34.15 ? 64  ILE   A HG22 1 
ATOM   834  H HG23 . ILE   A 1 84  ? 13.540  20.480 16.207 1.00 34.15 ? 64  ILE   A HG23 1 
ATOM   835  H HD11 . ILE   A 1 84  ? 12.951  19.458 19.754 1.00 42.14 ? 64  ILE   A HD11 1 
ATOM   836  H HD12 . ILE   A 1 84  ? 13.727  19.649 18.381 1.00 42.14 ? 64  ILE   A HD12 1 
ATOM   837  H HD13 . ILE   A 1 84  ? 12.961  20.876 19.038 1.00 42.14 ? 64  ILE   A HD13 1 
ATOM   838  N N    . ARG   A 1 85  ? 11.688  23.535 15.302 1.00 25.02 ? 65  ARG   A N    1 
ATOM   839  C CA   . ARG   A 1 85  ? 11.204  24.502 14.322 1.00 26.30 ? 65  ARG   A CA   1 
ATOM   840  C C    . ARG   A 1 85  ? 11.899  24.326 12.977 1.00 26.12 ? 65  ARG   A C    1 
ATOM   841  O O    . ARG   A 1 85  ? 13.108  24.580 12.847 1.00 27.75 ? 65  ARG   A O    1 
ATOM   842  C CB   . ARG   A 1 85  ? 11.387  25.930 14.840 1.00 28.37 ? 65  ARG   A CB   1 
ATOM   843  C CG   . ARG   A 1 85  ? 10.577  26.185 16.098 1.00 31.27 ? 65  ARG   A CG   1 
ATOM   844  C CD   . ARG   A 1 85  ? 10.741  27.608 16.623 1.00 35.13 ? 65  ARG   A CD   1 
ATOM   845  N NE   . ARG   A 1 85  ? 10.020  27.808 17.876 1.00 38.07 ? 65  ARG   A NE   1 
ATOM   846  C CZ   . ARG   A 1 85  ? 8.718   28.045 17.969 1.00 41.11 ? 65  ARG   A CZ   1 
ATOM   847  N NH1  . ARG   A 1 85  ? 7.954   28.153 16.892 1.00 42.84 ? 65  ARG   A NH1  1 
ATOM   848  N NH2  . ARG   A 1 85  ? 8.169   28.188 19.173 1.00 43.63 ? 65  ARG   A NH2  1 
ATOM   849  H H    . ARG   A 1 85  ? 12.486  23.696 15.578 1.00 30.03 ? 65  ARG   A H    1 
ATOM   850  H HA   . ARG   A 1 85  ? 10.264  24.318 14.175 1.00 31.56 ? 65  ARG   A HA   1 
ATOM   851  H HB2  . ARG   A 1 85  ? 12.323  26.077 15.046 1.00 34.04 ? 65  ARG   A HB2  1 
ATOM   852  H HB3  . ARG   A 1 85  ? 11.095  26.555 14.158 1.00 34.04 ? 65  ARG   A HB3  1 
ATOM   853  H HG2  . ARG   A 1 85  ? 9.637   26.043 15.905 1.00 37.53 ? 65  ARG   A HG2  1 
ATOM   854  H HG3  . ARG   A 1 85  ? 10.868  25.574 16.793 1.00 37.53 ? 65  ARG   A HG3  1 
ATOM   855  H HD2  . ARG   A 1 85  ? 11.681  27.784 16.781 1.00 42.16 ? 65  ARG   A HD2  1 
ATOM   856  H HD3  . ARG   A 1 85  ? 10.391  28.232 15.968 1.00 42.16 ? 65  ARG   A HD3  1 
ATOM   857  H HE   . ARG   A 1 85  ? 10.472  27.769 18.607 1.00 45.68 ? 65  ARG   A HE   1 
ATOM   858  H HH11 . ARG   A 1 85  ? 8.300   28.069 16.109 1.00 51.40 ? 65  ARG   A HH11 1 
ATOM   859  H HH12 . ARG   A 1 85  ? 7.112   28.307 16.975 1.00 51.40 ? 65  ARG   A HH12 1 
ATOM   860  H HH21 . ARG   A 1 85  ? 8.657   28.125 19.878 1.00 52.36 ? 65  ARG   A HH21 1 
ATOM   861  H HH22 . ARG   A 1 85  ? 7.326   28.342 19.246 1.00 52.36 ? 65  ARG   A HH22 1 
ATOM   862  N N    . GLY   A 1 86  ? 11.128  23.890 11.994 1.00 25.61 ? 66  GLY   A N    1 
ATOM   863  C CA   . GLY   A 1 86  ? 11.572  23.801 10.626 1.00 26.04 ? 66  GLY   A CA   1 
ATOM   864  C C    . GLY   A 1 86  ? 11.921  22.382 10.259 1.00 26.23 ? 66  GLY   A C    1 
ATOM   865  O O    . GLY   A 1 86  ? 12.356  21.575 11.088 1.00 25.11 ? 66  GLY   A O    1 
ATOM   866  H H    . GLY   A 1 86  ? 10.315  23.630 12.103 1.00 30.74 ? 66  GLY   A H    1 
ATOM   867  H HA2  . GLY   A 1 86  ? 10.868  24.111 10.034 1.00 31.25 ? 66  GLY   A HA2  1 
ATOM   868  H HA3  . GLY   A 1 86  ? 12.357  24.356 10.501 1.00 31.25 ? 66  GLY   A HA3  1 
ATOM   869  N N    . ARG   A 1 87  ? 11.728  22.071 8.991  1.00 30.34 ? 67  ARG   A N    1 
ATOM   870  C CA   . ARG   A 1 87  ? 11.969  20.721 8.507  1.00 31.72 ? 67  ARG   A CA   1 
ATOM   871  C C    . ARG   A 1 87  ? 13.405  20.265 8.764  1.00 33.92 ? 67  ARG   A C    1 
ATOM   872  O O    . ARG   A 1 87  ? 13.628  19.102 9.121  1.00 35.29 ? 67  ARG   A O    1 
ATOM   873  C CB   . ARG   A 1 87  ? 11.568  20.720 7.038  1.00 32.17 ? 67  ARG   A CB   1 
ATOM   874  C CG   . ARG   A 1 87  ? 11.195  19.461 6.463  1.00 29.45 ? 67  ARG   A CG   1 
ATOM   875  C CD   . ARG   A 1 87  ? 11.173  19.610 5.002  1.00 31.82 ? 67  ARG   A CD   1 
ATOM   876  N NE   . ARG   A 1 87  ? 9.882   19.225 4.497  1.00 32.40 ? 67  ARG   A NE   1 
ATOM   877  C CZ   . ARG   A 1 87  ? 9.523   19.401 3.242  1.00 32.81 ? 67  ARG   A CZ   1 
ATOM   878  N NH1  . ARG   A 1 87  ? 10.308  20.052 2.391  1.00 36.44 ? 67  ARG   A NH1  1 
ATOM   879  N NH2  . ARG   A 1 87  ? 8.361   18.906 2.836  1.00 31.65 ? 67  ARG   A NH2  1 
ATOM   880  H H    . ARG   A 1 87  ? 11.458  22.621 8.387  1.00 36.40 ? 67  ARG   A H    1 
ATOM   881  H HA   . ARG   A 1 87  ? 11.433  20.062 8.975  1.00 38.06 ? 67  ARG   A HA   1 
ATOM   882  H HB2  . ARG   A 1 87  ? 10.808  21.313 6.936  1.00 38.60 ? 67  ARG   A HB2  1 
ATOM   883  H HB3  . ARG   A 1 87  ? 12.320  21.053 6.523  1.00 38.60 ? 67  ARG   A HB3  1 
ATOM   884  H HG2  . ARG   A 1 87  ? 11.842  18.779 6.703  1.00 35.34 ? 67  ARG   A HG2  1 
ATOM   885  H HG3  . ARG   A 1 87  ? 10.312  19.202 6.770  1.00 35.34 ? 67  ARG   A HG3  1 
ATOM   886  H HD2  . ARG   A 1 87  ? 11.339  20.535 4.763  1.00 38.19 ? 67  ARG   A HD2  1 
ATOM   887  H HD3  . ARG   A 1 87  ? 11.847  19.038 4.603  1.00 38.19 ? 67  ARG   A HD3  1 
ATOM   888  H HE   . ARG   A 1 87  ? 9.320   18.865 5.039  1.00 38.88 ? 67  ARG   A HE   1 
ATOM   889  H HH11 . ARG   A 1 87  ? 11.063  20.366 2.656  1.00 43.73 ? 67  ARG   A HH11 1 
ATOM   890  H HH12 . ARG   A 1 87  ? 10.062  20.159 1.574  1.00 43.73 ? 67  ARG   A HH12 1 
ATOM   891  H HH21 . ARG   A 1 87  ? 7.859   18.480 3.389  1.00 37.98 ? 67  ARG   A HH21 1 
ATOM   892  H HH22 . ARG   A 1 87  ? 8.111   19.011 2.020  1.00 37.98 ? 67  ARG   A HH22 1 
ATOM   893  N N    . GLU   A 1 88  ? 14.395  21.148 8.625  1.00 36.31 ? 68  GLU   A N    1 
ATOM   894  C CA   . GLU   A 1 88  ? 15.778  20.729 8.869  1.00 39.02 ? 68  GLU   A CA   1 
ATOM   895  C C    . GLU   A 1 88  ? 16.016  20.325 10.327 1.00 35.94 ? 68  GLU   A C    1 
ATOM   896  O O    . GLU   A 1 88  ? 16.622  19.280 10.607 1.00 37.33 ? 68  GLU   A O    1 
ATOM   897  C CB   . GLU   A 1 88  ? 16.720  21.857 8.442  1.00 46.25 ? 68  GLU   A CB   1 
ATOM   898  C CG   . GLU   A 1 88  ? 18.149  21.738 8.963  1.00 51.96 ? 68  GLU   A CG   1 
ATOM   899  H H    . GLU   A 1 88  ? 14.298  21.972 8.397  1.00 43.57 ? 68  GLU   A H    1 
ATOM   900  H HA   . GLU   A 1 88  ? 15.969  19.942 8.335  1.00 46.82 ? 68  GLU   A HA   1 
ATOM   901  H HB2  . GLU   A 1 88  ? 16.764  21.870 7.473  1.00 55.50 ? 68  GLU   A HB2  1 
ATOM   902  H HB3  . GLU   A 1 88  ? 16.360  22.697 8.769  1.00 55.50 ? 68  GLU   A HB3  1 
ATOM   903  N N    . LYS   A 1 89  ? 15.573  21.147 11.277 1.00 31.87 ? 69  LYS   A N    1 
ATOM   904  C CA   . LYS   A 1 89  ? 15.713  20.763 12.678 1.00 31.32 ? 69  LYS   A CA   1 
ATOM   905  C C    . LYS   A 1 89  ? 14.896  19.523 13.020 1.00 27.66 ? 69  LYS   A C    1 
ATOM   906  O O    . LYS   A 1 89  ? 15.305  18.728 13.869 1.00 27.93 ? 69  LYS   A O    1 
ATOM   907  C CB   . LYS   A 1 89  ? 15.334  21.925 13.591 1.00 33.33 ? 69  LYS   A CB   1 
ATOM   908  C CG   . LYS   A 1 89  ? 16.407  22.995 13.700 1.00 35.07 ? 69  LYS   A CG   1 
ATOM   909  H H    . LYS   A 1 89  ? 15.199  21.909 11.141 1.00 38.24 ? 69  LYS   A H    1 
ATOM   910  H HA   . LYS   A 1 89  ? 16.646  20.551 12.841 1.00 37.58 ? 69  LYS   A HA   1 
ATOM   911  H HB2  . LYS   A 1 89  ? 14.532  22.345 13.244 1.00 40.00 ? 69  LYS   A HB2  1 
ATOM   912  H HB3  . LYS   A 1 89  ? 15.169  21.580 14.482 1.00 40.00 ? 69  LYS   A HB3  1 
ATOM   913  N N    . LEU   A 1 90  ? 13.732  19.337 12.396 1.00 24.48 ? 70  LEU   A N    1 
ATOM   914  C CA   . LEU   A 1 90  ? 12.981  18.108 12.647 1.00 22.89 ? 70  LEU   A CA   1 
ATOM   915  C C    . LEU   A 1 90  ? 13.769  16.884 12.195 1.00 23.40 ? 70  LEU   A C    1 
ATOM   916  O O    . LEU   A 1 90  ? 13.804  15.870 12.898 1.00 24.20 ? 70  LEU   A O    1 
ATOM   917  C CB   . LEU   A 1 90  ? 11.628  18.173 11.949 1.00 21.79 ? 70  LEU   A CB   1 
ATOM   918  C CG   . LEU   A 1 90  ? 10.617  19.091 12.648 1.00 22.57 ? 70  LEU   A CG   1 
ATOM   919  C CD1  . LEU   A 1 90  ? 9.499   19.487 11.703 1.00 25.15 ? 70  LEU   A CD1  1 
ATOM   920  C CD2  . LEU   A 1 90  ? 10.026  18.451 13.922 1.00 23.15 ? 70  LEU   A CD2  1 
ATOM   921  H H    . LEU   A 1 90  ? 13.369  19.886 11.843 1.00 29.37 ? 70  LEU   A H    1 
ATOM   922  H HA   . LEU   A 1 90  ? 12.820  18.024 13.600 1.00 27.47 ? 70  LEU   A HA   1 
ATOM   923  H HB2  . LEU   A 1 90  ? 11.758  18.506 11.047 1.00 26.14 ? 70  LEU   A HB2  1 
ATOM   924  H HB3  . LEU   A 1 90  ? 11.249  17.280 11.921 1.00 26.14 ? 70  LEU   A HB3  1 
ATOM   925  H HG   . LEU   A 1 90  ? 11.096  19.890 12.919 1.00 27.09 ? 70  LEU   A HG   1 
ATOM   926  H HD11 . LEU   A 1 90  ? 8.878   20.065 12.173 1.00 30.18 ? 70  LEU   A HD11 1 
ATOM   927  H HD12 . LEU   A 1 90  ? 9.878   19.955 10.943 1.00 30.18 ? 70  LEU   A HD12 1 
ATOM   928  H HD13 . LEU   A 1 90  ? 9.041   18.686 11.403 1.00 30.18 ? 70  LEU   A HD13 1 
ATOM   929  H HD21 . LEU   A 1 90  ? 9.379   19.061 14.310 1.00 27.79 ? 70  LEU   A HD21 1 
ATOM   930  H HD22 . LEU   A 1 90  ? 9.593   17.617 13.684 1.00 27.79 ? 70  LEU   A HD22 1 
ATOM   931  H HD23 . LEU   A 1 90  ? 10.744  18.284 14.553 1.00 27.79 ? 70  LEU   A HD23 1 
ATOM   932  N N    . GLY   A 1 91  ? 14.437  16.969 11.037 1.00 24.78 ? 71  GLY   A N    1 
ATOM   933  C CA   . GLY   A 1 91  ? 15.273  15.857 10.598 1.00 27.02 ? 71  GLY   A CA   1 
ATOM   934  C C    . GLY   A 1 91  ? 16.427  15.559 11.550 1.00 28.05 ? 71  GLY   A C    1 
ATOM   935  O O    . GLY   A 1 91  ? 16.756  14.398 11.800 1.00 29.43 ? 71  GLY   A O    1 
ATOM   936  H H    . GLY   A 1 91  ? 14.422  17.643 10.504 1.00 29.74 ? 71  GLY   A H    1 
ATOM   937  H HA2  . GLY   A 1 91  ? 14.727  15.058 10.525 1.00 32.43 ? 71  GLY   A HA2  1 
ATOM   938  H HA3  . GLY   A 1 91  ? 15.646  16.064 9.727  1.00 32.43 ? 71  GLY   A HA3  1 
ATOM   939  N N    . GLU   A 1 92  ? 17.027  16.594 12.133 1.00 31.20 ? 72  GLU   A N    1 
ATOM   940  C CA   . GLU   A 1 92  ? 18.088  16.375 13.120 1.00 34.25 ? 72  GLU   A CA   1 
ATOM   941  C C    . GLU   A 1 92  ? 17.551  15.708 14.388 1.00 33.32 ? 72  GLU   A C    1 
ATOM   942  O O    . GLU   A 1 92  ? 18.200  14.819 14.965 1.00 33.77 ? 72  GLU   A O    1 
ATOM   943  C CB   . GLU   A 1 92  ? 18.719  17.715 13.474 1.00 38.94 ? 72  GLU   A CB   1 
ATOM   944  C CG   . GLU   A 1 92  ? 19.405  18.376 12.292 1.00 43.77 ? 72  GLU   A CG   1 
ATOM   945  C CD   . GLU   A 1 92  ? 19.951  19.762 12.632 1.00 49.12 ? 72  GLU   A CD   1 
ATOM   946  O OE1  . GLU   A 1 92  ? 19.721  20.232 13.774 1.00 50.85 ? 72  GLU   A OE1  1 
ATOM   947  O OE2  . GLU   A 1 92  ? 20.601  20.377 11.758 1.00 52.28 ? 72  GLU   A OE2  1 
ATOM   948  H H    . GLU   A 1 92  ? 16.843  17.420 11.981 1.00 37.44 ? 72  GLU   A H    1 
ATOM   949  H HA   . GLU   A 1 92  ? 18.760  15.790 12.735 1.00 41.10 ? 72  GLU   A HA   1 
ATOM   950  H HB2  . GLU   A 1 92  ? 18.027  18.315 13.792 1.00 46.72 ? 72  GLU   A HB2  1 
ATOM   951  H HB3  . GLU   A 1 92  ? 19.384  17.577 14.167 1.00 46.72 ? 72  GLU   A HB3  1 
ATOM   952  H HG2  . GLU   A 1 92  ? 20.148  17.822 12.006 1.00 52.53 ? 72  GLU   A HG2  1 
ATOM   953  H HG3  . GLU   A 1 92  ? 18.767  18.474 11.568 1.00 52.53 ? 72  GLU   A HG3  1 
ATOM   954  N N    . HIS   A 1 93  ? 16.380  16.155 14.858 1.00 30.95 ? 73  HIS   A N    1 
ATOM   955  C CA   . HIS   A 1 93  ? 15.737  15.545 16.023 1.00 30.76 ? 73  HIS   A CA   1 
ATOM   956  C C    . HIS   A 1 93  ? 15.541  14.052 15.823 1.00 28.38 ? 73  HIS   A C    1 
ATOM   957  O O    . HIS   A 1 93  ? 15.694  13.264 16.762 1.00 28.17 ? 73  HIS   A O    1 
ATOM   958  C CB   . HIS   A 1 93  ? 14.375  16.204 16.300 1.00 31.74 ? 73  HIS   A CB   1 
ATOM   959  C CG   . HIS   A 1 93  ? 13.475  15.432 17.236 1.00 31.22 ? 73  HIS   A CG   1 
ATOM   960  N ND1  . HIS   A 1 93  ? 13.623  15.453 18.609 1.00 32.95 ? 73  HIS   A ND1  1 
ATOM   961  C CD2  . HIS   A 1 93  ? 12.374  14.676 16.995 1.00 31.85 ? 73  HIS   A CD2  1 
ATOM   962  C CE1  . HIS   A 1 93  ? 12.666  14.732 19.167 1.00 32.07 ? 73  HIS   A CE1  1 
ATOM   963  N NE2  . HIS   A 1 93  ? 11.889  14.257 18.212 1.00 33.75 ? 73  HIS   A NE2  1 
ATOM   964  H H    . HIS   A 1 93  ? 15.938  16.811 14.519 1.00 37.15 ? 73  HIS   A H    1 
ATOM   965  H HA   . HIS   A 1 93  ? 16.310  15.691 16.792 1.00 36.92 ? 73  HIS   A HA   1 
ATOM   966  H HB2  . HIS   A 1 93  ? 14.530  17.075 16.698 1.00 38.09 ? 73  HIS   A HB2  1 
ATOM   967  H HB3  . HIS   A 1 93  ? 13.904  16.303 15.458 1.00 38.09 ? 73  HIS   A HB3  1 
ATOM   968  H HD1  . HIS   A 1 93  ? 14.242  15.871 19.035 1.00 39.55 ? 73  HIS   A HD1  1 
ATOM   969  H HD2  . HIS   A 1 93  ? 12.015  14.477 16.160 1.00 38.22 ? 73  HIS   A HD2  1 
ATOM   970  H HE1  . HIS   A 1 93  ? 12.559  14.583 20.079 1.00 38.49 ? 73  HIS   A HE1  1 
ATOM   971  N N    . ALA   A 1 94  ? 15.230  13.636 14.601 1.00 26.56 ? 74  ALA   A N    1 
ATOM   972  C CA   . ALA   A 1 94  ? 15.001  12.220 14.363 1.00 26.21 ? 74  ALA   A CA   1 
ATOM   973  C C    . ALA   A 1 94  ? 16.255  11.400 14.634 1.00 25.32 ? 74  ALA   A C    1 
ATOM   974  O O    . ALA   A 1 94  ? 16.165  10.266 15.114 1.00 25.28 ? 74  ALA   A O    1 
ATOM   975  C CB   . ALA   A 1 94  ? 14.495  12.019 12.943 1.00 28.19 ? 74  ALA   A CB   1 
ATOM   976  H H    . ALA   A 1 94  ? 15.148  14.142 13.910 1.00 31.88 ? 74  ALA   A H    1 
ATOM   977  H HA   . ALA   A 1 94  ? 14.316  11.897 14.969 1.00 31.45 ? 74  ALA   A HA   1 
ATOM   978  H HB1  . ALA   A 1 94  ? 14.335  11.074 12.796 1.00 33.83 ? 74  ALA   A HB1  1 
ATOM   979  H HB2  . ALA   A 1 94  ? 13.670  12.516 12.829 1.00 33.83 ? 74  ALA   A HB2  1 
ATOM   980  H HB3  . ALA   A 1 94  ? 15.165  12.342 12.320 1.00 33.83 ? 74  ALA   A HB3  1 
ATOM   981  N N    . VAL   A 1 95  ? 17.429  11.936 14.312 1.00 26.38 ? 75  VAL   A N    1 
ATOM   982  C CA   . VAL   A 1 95  ? 18.667  11.224 14.601 1.00 28.82 ? 75  VAL   A CA   1 
ATOM   983  C C    . VAL   A 1 95  ? 18.784  10.982 16.095 1.00 28.87 ? 75  VAL   A C    1 
ATOM   984  O O    . VAL   A 1 95  ? 19.098  9.872  16.545 1.00 29.30 ? 75  VAL   A O    1 
ATOM   985  C CB   . VAL   A 1 95  ? 19.863  12.023 14.060 1.00 34.09 ? 75  VAL   A CB   1 
ATOM   986  C CG1  . VAL   A 1 95  ? 21.149  11.348 14.445 1.00 35.09 ? 75  VAL   A CG1  1 
ATOM   987  C CG2  . VAL   A 1 95  ? 19.769  12.189 12.529 1.00 36.19 ? 75  VAL   A CG2  1 
ATOM   988  H H    . VAL   A 1 95  ? 17.533  12.700 13.930 1.00 31.66 ? 75  VAL   A H    1 
ATOM   989  H HA   . VAL   A 1 95  ? 18.654  10.362 14.158 1.00 34.59 ? 75  VAL   A HA   1 
ATOM   990  H HB   . VAL   A 1 95  ? 19.852  12.911 14.451 1.00 40.91 ? 75  VAL   A HB   1 
ATOM   991  H HG11 . VAL   A 1 95  ? 21.891  11.829 14.046 1.00 42.11 ? 75  VAL   A HG11 1 
ATOM   992  H HG12 . VAL   A 1 95  ? 21.233  11.354 15.412 1.00 42.11 ? 75  VAL   A HG12 1 
ATOM   993  H HG13 . VAL   A 1 95  ? 21.136  10.434 14.121 1.00 42.11 ? 75  VAL   A HG13 1 
ATOM   994  H HG21 . VAL   A 1 95  ? 20.560  12.654 12.212 1.00 43.43 ? 75  VAL   A HG21 1 
ATOM   995  H HG22 . VAL   A 1 95  ? 19.715  11.312 12.119 1.00 43.43 ? 75  VAL   A HG22 1 
ATOM   996  H HG23 . VAL   A 1 95  ? 18.975  12.704 12.315 1.00 43.43 ? 75  VAL   A HG23 1 
ATOM   997  N N    A TRP   A 1 96  ? 18.498  12.014 16.888 0.54 26.69 ? 76  TRP   A N    1 
ATOM   998  N N    B TRP   A 1 96  ? 18.540  12.024 16.894 0.46 30.17 ? 76  TRP   A N    1 
ATOM   999  C CA   A TRP   A 1 96  ? 18.564  11.880 18.336 0.54 28.01 ? 76  TRP   A CA   1 
ATOM   1000 C CA   B TRP   A 1 96  ? 18.648  11.887 18.342 0.46 33.35 ? 76  TRP   A CA   1 
ATOM   1001 C C    A TRP   A 1 96  ? 17.543  10.865 18.826 0.54 27.47 ? 76  TRP   A C    1 
ATOM   1002 C C    B TRP   A 1 96  ? 17.553  10.987 18.892 0.46 32.95 ? 76  TRP   A C    1 
ATOM   1003 O O    A TRP   A 1 96  ? 17.855  10.003 19.653 0.54 30.54 ? 76  TRP   A O    1 
ATOM   1004 O O    B TRP   A 1 96  ? 17.761  10.303 19.899 0.46 34.71 ? 76  TRP   A O    1 
ATOM   1005 C CB   A TRP   A 1 96  ? 18.342  13.240 18.998 0.54 28.19 ? 76  TRP   A CB   1 
ATOM   1006 C CB   B TRP   A 1 96  ? 18.586  13.265 19.004 0.46 34.93 ? 76  TRP   A CB   1 
ATOM   1007 H H    A TRP   A 1 96  ? 18.266  12.795 16.613 0.54 32.04 ? 76  TRP   A H    1 
ATOM   1008 H H    B TRP   A 1 96  ? 18.314  12.808 16.624 0.46 36.21 ? 76  TRP   A H    1 
ATOM   1009 H HA   A TRP   A 1 96  ? 19.448  11.570 18.588 0.54 33.62 ? 76  TRP   A HA   1 
ATOM   1010 H HA   B TRP   A 1 96  ? 19.506  11.491 18.559 0.46 40.02 ? 76  TRP   A HA   1 
ATOM   1011 N N    A SER   A 1 97  ? 16.307  10.956 18.323 0.54 27.37 ? 77  SER   A N    1 
ATOM   1012 N N    B SER   A 1 97  ? 16.386  10.979 18.248 0.46 31.63 ? 77  SER   A N    1 
ATOM   1013 C CA   A SER   A 1 97  ? 15.244  10.080 18.798 0.54 30.32 ? 77  SER   A CA   1 
ATOM   1014 C CA   B SER   A 1 97  ? 15.280  10.155 18.714 0.46 30.92 ? 77  SER   A CA   1 
ATOM   1015 C C    A SER   A 1 97  ? 15.544  8.623  18.485 0.54 29.67 ? 77  SER   A C    1 
ATOM   1016 C C    B SER   A 1 97  ? 15.550  8.678  18.472 0.46 29.97 ? 77  SER   A C    1 
ATOM   1017 O O    A SER   A 1 97  ? 15.218  7.736  19.278 0.54 30.50 ? 77  SER   A O    1 
ATOM   1018 O O    B SER   A 1 97  ? 15.210  7.835  19.306 0.46 30.60 ? 77  SER   A O    1 
ATOM   1019 C CB   A SER   A 1 97  ? 13.913  10.503 18.183 0.54 33.87 ? 77  SER   A CB   1 
ATOM   1020 C CB   B SER   A 1 97  ? 14.008  10.602 18.003 0.46 30.94 ? 77  SER   A CB   1 
ATOM   1021 O OG   A SER   A 1 97  ? 13.798  10.031 16.854 0.54 36.46 ? 77  SER   A OG   1 
ATOM   1022 O OG   B SER   A 1 97  ? 12.886  9.951  18.551 0.46 29.44 ? 77  SER   A OG   1 
ATOM   1023 H H    A SER   A 1 97  ? 16.064  11.511 17.713 0.54 32.85 ? 77  SER   A H    1 
ATOM   1024 H H    B SER   A 1 97  ? 16.212  11.439 17.543 0.46 37.96 ? 77  SER   A H    1 
ATOM   1025 H HA   A SER   A 1 97  ? 15.173  10.165 19.762 0.54 36.39 ? 77  SER   A HA   1 
ATOM   1026 H HA   B SER   A 1 97  ? 15.161  10.273 19.670 0.46 37.11 ? 77  SER   A HA   1 
ATOM   1027 H HB2  A SER   A 1 97  ? 13.189  10.134 18.713 0.54 40.64 ? 77  SER   A HB2  1 
ATOM   1028 H HB2  B SER   A 1 97  ? 13.903  11.560 18.111 0.46 37.13 ? 77  SER   A HB2  1 
ATOM   1029 H HB3  A SER   A 1 97  ? 13.861  11.472 18.179 0.54 40.64 ? 77  SER   A HB3  1 
ATOM   1030 H HB3  B SER   A 1 97  ? 14.075  10.379 17.062 0.46 37.13 ? 77  SER   A HB3  1 
ATOM   1031 H HG   A SER   A 1 97  ? 14.439  10.316 16.392 0.54 43.75 ? 77  SER   A HG   1 
ATOM   1032 H HG   B SER   A 1 97  ? 12.197  10.146 18.111 0.46 35.33 ? 77  SER   A HG   1 
ATOM   1033 N N    . LEU   A 1 98  ? 16.166  8.342  17.342 1.00 30.06 ? 78  LEU   A N    1 
ATOM   1034 C CA   . LEU   A 1 98  ? 16.487  6.945  17.059 1.00 32.87 ? 78  LEU   A CA   1 
ATOM   1035 C C    . LEU   A 1 98  ? 17.528  6.388  18.023 1.00 32.88 ? 78  LEU   A C    1 
ATOM   1036 O O    . LEU   A 1 98  ? 17.546  5.177  18.298 1.00 34.64 ? 78  LEU   A O    1 
ATOM   1037 C CB   . LEU   A 1 98  ? 16.923  6.788  15.611 0.85 34.43 ? 78  LEU   A CB   1 
ATOM   1038 C CG   . LEU   A 1 98  ? 15.753  6.500  14.674 0.80 37.17 ? 78  LEU   A CG   1 
ATOM   1039 C CD1  . LEU   A 1 98  ? 16.156  6.689  13.250 1.00 40.91 ? 78  LEU   A CD1  1 
ATOM   1040 C CD2  . LEU   A 1 98  ? 15.221  5.088  14.922 1.00 36.46 ? 78  LEU   A CD2  1 
ATOM   1041 H H    A LEU   A 1 98  ? 16.402  8.913  16.743 0.54 36.07 ? 78  LEU   A H    1 
ATOM   1042 H H    B LEU   A 1 98  ? 16.408  8.896  16.729 0.46 36.07 ? 78  LEU   A H    1 
ATOM   1043 H HA   . LEU   A 1 98  ? 15.686  6.411  17.176 1.00 39.44 ? 78  LEU   A HA   1 
ATOM   1044 H HB2  . LEU   A 1 98  ? 17.349  7.609  15.319 0.85 41.32 ? 78  LEU   A HB2  1 
ATOM   1045 H HB3  . LEU   A 1 98  ? 17.549  6.049  15.548 0.85 41.32 ? 78  LEU   A HB3  1 
ATOM   1046 H HG   . LEU   A 1 98  ? 15.033  7.126  14.851 0.80 44.60 ? 78  LEU   A HG   1 
ATOM   1047 H HD11 . LEU   A 1 98  ? 15.398  6.492  12.678 1.00 49.09 ? 78  LEU   A HD11 1 
ATOM   1048 H HD12 . LEU   A 1 98  ? 16.439  7.608  13.121 1.00 49.09 ? 78  LEU   A HD12 1 
ATOM   1049 H HD13 . LEU   A 1 98  ? 16.889  6.086  13.047 1.00 49.09 ? 78  LEU   A HD13 1 
ATOM   1050 H HD21 . LEU   A 1 98  ? 14.646  4.833  14.183 1.00 43.75 ? 78  LEU   A HD21 1 
ATOM   1051 H HD22 . LEU   A 1 98  ? 15.971  4.475  14.984 1.00 43.75 ? 78  LEU   A HD22 1 
ATOM   1052 H HD23 . LEU   A 1 98  ? 14.718  5.081  15.751 1.00 43.75 ? 78  LEU   A HD23 1 
ATOM   1053 N N    . GLN   A 1 99  ? 18.372  7.245  18.576 1.00 30.13 ? 79  GLN   A N    1 
ATOM   1054 C CA   . GLN   A 1 99  ? 19.303  6.784  19.593 1.00 31.30 ? 79  GLN   A CA   1 
ATOM   1055 C C    . GLN   A 1 99  ? 18.636  6.681  20.958 1.00 28.94 ? 79  GLN   A C    1 
ATOM   1056 O O    . GLN   A 1 99  ? 18.852  5.708  21.684 1.00 30.40 ? 79  GLN   A O    1 
ATOM   1057 C CB   . GLN   A 1 99  ? 20.482  7.748  19.649 1.00 35.13 ? 79  GLN   A CB   1 
ATOM   1058 C CG   . GLN   A 1 99  ? 21.459  7.465  20.784 1.00 42.68 ? 79  GLN   A CG   1 
ATOM   1059 C CD   . GLN   A 1 99  ? 22.854  8.070  20.571 1.00 50.19 ? 79  GLN   A CD   1 
ATOM   1060 O OE1  . GLN   A 1 99  ? 23.014  9.128  19.945 1.00 53.00 ? 79  GLN   A OE1  1 
ATOM   1061 N NE2  . GLN   A 1 99  ? 23.872  7.385  21.098 1.00 52.46 ? 79  GLN   A NE2  1 
ATOM   1062 H H    . GLN   A 1 99  ? 18.425  8.082  18.385 1.00 36.16 ? 79  GLN   A H    1 
ATOM   1063 H HA   . GLN   A 1 99  ? 19.629  5.901  19.359 1.00 37.56 ? 79  GLN   A HA   1 
ATOM   1064 H HB2  . GLN   A 1 99  ? 20.973  7.688  18.815 1.00 42.16 ? 79  GLN   A HB2  1 
ATOM   1065 H HB3  . GLN   A 1 99  ? 20.142  8.649  19.770 1.00 42.16 ? 79  GLN   A HB3  1 
ATOM   1066 H HG2  . GLN   A 1 99  ? 21.099  7.837  21.605 1.00 51.22 ? 79  GLN   A HG2  1 
ATOM   1067 H HG3  . GLN   A 1 99  ? 21.564  6.505  20.873 1.00 51.22 ? 79  GLN   A HG3  1 
ATOM   1068 H HE21 . GLN   A 1 99  ? 23.723  6.654  21.526 1.00 62.95 ? 79  GLN   A HE21 1 
ATOM   1069 H HE22 . GLN   A 1 99  ? 24.677  7.675  21.010 1.00 62.95 ? 79  GLN   A HE22 1 
ATOM   1070 N N    . CYS   A 1 100 ? 17.840  7.669  21.336 1.00 26.74 ? 80  CYS   A N    1 
ATOM   1071 C CA   . CYS   A 1 100 ? 17.300  7.717  22.691 1.00 27.10 ? 80  CYS   A CA   1 
ATOM   1072 C C    . CYS   A 1 100 ? 16.017  6.926  22.852 1.00 24.70 ? 80  CYS   A C    1 
ATOM   1073 O O    . CYS   A 1 100 ? 15.701  6.509  23.966 1.00 25.28 ? 80  CYS   A O    1 
ATOM   1074 C CB   . CYS   A 1 100 ? 17.126  9.175  23.100 1.00 32.78 ? 80  CYS   A CB   1 
ATOM   1075 S SG   . CYS   A 1 100 ? 18.719  10.028 23.222 1.00 40.19 ? 80  CYS   A SG   1 
ATOM   1076 H H    . CYS   A 1 100 ? 17.598  8.322  20.831 1.00 32.10 ? 80  CYS   A H    1 
ATOM   1077 H HA   . CYS   A 1 100 ? 17.925  7.319  23.318 1.00 32.52 ? 80  CYS   A HA   1 
ATOM   1078 H HB2  . CYS   A 1 100 ? 16.585  9.631  22.437 1.00 39.34 ? 80  CYS   A HB2  1 
ATOM   1079 H HB3  . CYS   A 1 100 ? 16.692  9.214  23.967 1.00 39.34 ? 80  CYS   A HB3  1 
ATOM   1080 H HG   . CYS   A 1 100 ? 18.528  11.167 23.549 1.00 48.23 ? 80  CYS   A HG   1 
ATOM   1081 N N    . PHE   A 1 101 ? 15.306  6.672  21.764 1.00 21.82 ? 81  PHE   A N    1 
ATOM   1082 C CA   . PHE   A 1 101 ? 14.065  5.901  21.778 1.00 20.72 ? 81  PHE   A CA   1 
ATOM   1083 C C    . PHE   A 1 101 ? 14.138  4.914  20.619 1.00 20.55 ? 81  PHE   A C    1 
ATOM   1084 O O    . PHE   A 1 101 ? 13.434  5.045  19.613 1.00 20.94 ? 81  PHE   A O    1 
ATOM   1085 C CB   . PHE   A 1 101 ? 12.859  6.836  21.685 1.00 21.52 ? 81  PHE   A CB   1 
ATOM   1086 C CG   . PHE   A 1 101 ? 12.727  7.768  22.855 1.00 23.05 ? 81  PHE   A CG   1 
ATOM   1087 C CD1  . PHE   A 1 101 ? 12.049  7.389  24.012 1.00 23.30 ? 81  PHE   A CD1  1 
ATOM   1088 C CD2  . PHE   A 1 101 ? 13.297  9.029  22.824 1.00 28.40 ? 81  PHE   A CD2  1 
ATOM   1089 C CE1  . PHE   A 1 101 ? 11.928  8.254  25.090 1.00 25.76 ? 81  PHE   A CE1  1 
ATOM   1090 C CE2  . PHE   A 1 101 ? 13.191  9.883  23.946 1.00 30.87 ? 81  PHE   A CE2  1 
ATOM   1091 C CZ   . PHE   A 1 101 ? 12.499  9.480  25.065 1.00 29.21 ? 81  PHE   A CZ   1 
ATOM   1092 H H    . PHE   A 1 101 ? 15.527  6.942  20.979 1.00 26.19 ? 81  PHE   A H    1 
ATOM   1093 H HA   . PHE   A 1 101 ? 13.969  5.396  22.601 1.00 24.86 ? 81  PHE   A HA   1 
ATOM   1094 H HB2  . PHE   A 1 101 ? 12.945  7.377  20.884 1.00 25.82 ? 81  PHE   A HB2  1 
ATOM   1095 H HB3  . PHE   A 1 101 ? 12.052  6.301  21.639 1.00 25.82 ? 81  PHE   A HB3  1 
ATOM   1096 H HD1  . PHE   A 1 101 ? 11.670  6.541  24.063 1.00 27.96 ? 81  PHE   A HD1  1 
ATOM   1097 H HD2  . PHE   A 1 101 ? 13.751  9.315  22.064 1.00 34.09 ? 81  PHE   A HD2  1 
ATOM   1098 H HE1  . PHE   A 1 101 ? 11.448  7.987  25.841 1.00 30.92 ? 81  PHE   A HE1  1 
ATOM   1099 H HE2  . PHE   A 1 101 ? 13.591  10.722 23.927 1.00 37.05 ? 81  PHE   A HE2  1 
ATOM   1100 H HZ   . PHE   A 1 101 ? 12.425  10.047 25.798 1.00 35.05 ? 81  PHE   A HZ   1 
ATOM   1101 N N    . PRO   A 1 102 ? 15.013  3.909  20.725 1.00 21.74 ? 82  PRO   A N    1 
ATOM   1102 C CA   . PRO   A 1 102 ? 15.391  3.125  19.531 1.00 21.82 ? 82  PRO   A CA   1 
ATOM   1103 C C    . PRO   A 1 102 ? 14.280  2.255  18.959 1.00 22.41 ? 82  PRO   A C    1 
ATOM   1104 O O    . PRO   A 1 102 ? 14.342  1.928  17.775 1.00 26.08 ? 82  PRO   A O    1 
ATOM   1105 C CB   . PRO   A 1 102 ? 16.580  2.270  20.028 1.00 24.46 ? 82  PRO   A CB   1 
ATOM   1106 C CG   . PRO   A 1 102 ? 16.348  2.181  21.528 1.00 25.92 ? 82  PRO   A CG   1 
ATOM   1107 C CD   . PRO   A 1 102 ? 15.809  3.534  21.907 1.00 23.44 ? 82  PRO   A CD   1 
ATOM   1108 H HA   . PRO   A 1 102 ? 15.694  3.729  18.835 1.00 26.19 ? 82  PRO   A HA   1 
ATOM   1109 H HB2  . PRO   A 1 102 ? 16.559  1.393  19.615 1.00 29.35 ? 82  PRO   A HB2  1 
ATOM   1110 H HB3  . PRO   A 1 102 ? 17.419  2.712  19.827 1.00 29.35 ? 82  PRO   A HB3  1 
ATOM   1111 H HG2  . PRO   A 1 102 ? 15.704  1.483  21.724 1.00 31.10 ? 82  PRO   A HG2  1 
ATOM   1112 H HG3  . PRO   A 1 102 ? 17.184  1.999  21.983 1.00 31.10 ? 82  PRO   A HG3  1 
ATOM   1113 H HD2  . PRO   A 1 102 ? 15.251  3.477  22.698 1.00 28.13 ? 82  PRO   A HD2  1 
ATOM   1114 H HD3  . PRO   A 1 102 ? 16.530  4.166  22.056 1.00 28.13 ? 82  PRO   A HD3  1 
ATOM   1115 N N    . ASP   A 1 103 ? 13.281  1.863  19.749 1.00 21.50 ? 83  ASP   A N    1 
ATOM   1116 C CA   . ASP   A 1 103 ? 12.229  0.962  19.291 1.00 21.10 ? 83  ASP   A CA   1 
ATOM   1117 C C    . ASP   A 1 103 ? 10.843  1.559  19.489 1.00 19.37 ? 83  ASP   A C    1 
ATOM   1118 O O    . ASP   A 1 103 ? 9.856   0.812  19.557 1.00 21.59 ? 83  ASP   A O    1 
ATOM   1119 C CB   . ASP   A 1 103 ? 12.322  -0.416 19.953 1.00 22.21 ? 83  ASP   A CB   1 
ATOM   1120 C CG   . ASP   A 1 103 ? 12.174  -0.379 21.469 1.00 23.81 ? 83  ASP   A CG   1 
ATOM   1121 O OD1  . ASP   A 1 103 ? 11.991  0.698  22.053 1.00 23.66 ? 83  ASP   A OD1  1 
ATOM   1122 O OD2  . ASP   A 1 103 ? 12.296  -1.453 22.096 1.00 27.81 ? 83  ASP   A OD2  1 
ATOM   1123 H H    . ASP   A 1 103 ? 13.191  2.110  20.567 1.00 25.80 ? 83  ASP   A H    1 
ATOM   1124 H HA   . ASP   A 1 103 ? 12.360  0.819  18.341 1.00 25.32 ? 83  ASP   A HA   1 
ATOM   1125 H HB2  . ASP   A 1 103 ? 11.616  -0.980 19.601 1.00 26.65 ? 83  ASP   A HB2  1 
ATOM   1126 H HB3  . ASP   A 1 103 ? 13.188  -0.802 19.750 1.00 26.65 ? 83  ASP   A HB3  1 
ATOM   1127 N N    . TRP   A 1 104 ? 10.746  2.883  19.574 1.00 19.12 ? 84  TRP   A N    1 
ATOM   1128 C CA   . TRP   A 1 104 ? 9.491   3.545  19.926 1.00 18.50 ? 84  TRP   A CA   1 
ATOM   1129 C C    . TRP   A 1 104 ? 8.376   3.215  18.955 1.00 19.20 ? 84  TRP   A C    1 
ATOM   1130 O O    . TRP   A 1 104 ? 8.543   3.305  17.730 1.00 20.15 ? 84  TRP   A O    1 
ATOM   1131 C CB   . TRP   A 1 104 ? 9.666   5.064  19.910 1.00 18.03 ? 84  TRP   A CB   1 
ATOM   1132 C CG   . TRP   A 1 104 ? 8.509   5.813  20.461 1.00 18.65 ? 84  TRP   A CG   1 
ATOM   1133 C CD1  . TRP   A 1 104 ? 7.528   6.462  19.748 1.00 19.63 ? 84  TRP   A CD1  1 
ATOM   1134 C CD2  . TRP   A 1 104 ? 8.148   5.921  21.840 1.00 18.18 ? 84  TRP   A CD2  1 
ATOM   1135 N NE1  . TRP   A 1 104 ? 6.621   7.014  20.621 1.00 19.35 ? 84  TRP   A NE1  1 
ATOM   1136 C CE2  . TRP   A 1 104 ? 6.972   6.692  21.905 1.00 18.86 ? 84  TRP   A CE2  1 
ATOM   1137 C CE3  . TRP   A 1 104 ? 8.744   5.492  23.030 1.00 19.04 ? 84  TRP   A CE3  1 
ATOM   1138 C CZ2  . TRP   A 1 104 ? 6.367   7.022  23.110 1.00 19.52 ? 84  TRP   A CZ2  1 
ATOM   1139 C CZ3  . TRP   A 1 104 ? 8.128   5.786  24.219 1.00 18.94 ? 84  TRP   A CZ3  1 
ATOM   1140 C CH2  . TRP   A 1 104 ? 6.943   6.556  24.254 1.00 20.01 ? 84  TRP   A CH2  1 
ATOM   1141 H H    . TRP   A 1 104 ? 11.396  3.426  19.432 1.00 22.94 ? 84  TRP   A H    1 
ATOM   1142 H HA   . TRP   A 1 104 ? 9.250   3.235  20.813 1.00 22.20 ? 84  TRP   A HA   1 
ATOM   1143 H HB2  . TRP   A 1 104 ? 10.445  5.293  20.440 1.00 21.64 ? 84  TRP   A HB2  1 
ATOM   1144 H HB3  . TRP   A 1 104 ? 9.793   5.352  18.992 1.00 21.64 ? 84  TRP   A HB3  1 
ATOM   1145 H HD1  . TRP   A 1 104 ? 7.486   6.519  18.821 1.00 23.55 ? 84  TRP   A HD1  1 
ATOM   1146 H HE1  . TRP   A 1 104 ? 5.939   7.487  20.395 1.00 23.22 ? 84  TRP   A HE1  1 
ATOM   1147 H HE3  . TRP   A 1 104 ? 9.543   5.016  23.015 1.00 22.85 ? 84  TRP   A HE3  1 
ATOM   1148 H HZ2  . TRP   A 1 104 ? 5.597   7.543  23.137 1.00 23.42 ? 84  TRP   A HZ2  1 
ATOM   1149 H HZ3  . TRP   A 1 104 ? 8.496   5.474  25.015 1.00 22.73 ? 84  TRP   A HZ3  1 
ATOM   1150 H HH2  . TRP   A 1 104 ? 6.549   6.748  25.073 1.00 24.01 ? 84  TRP   A HH2  1 
ATOM   1151 N N    . VAL   A 1 105 ? 7.211   2.904  19.513 1.00 17.67 ? 85  VAL   A N    1 
ATOM   1152 C CA   . VAL   A 1 105 ? 6.005   2.719  18.730 1.00 17.66 ? 85  VAL   A CA   1 
ATOM   1153 C C    . VAL   A 1 105 ? 4.850   3.468  19.367 1.00 17.53 ? 85  VAL   A C    1 
ATOM   1154 O O    . VAL   A 1 105 ? 4.721   3.535  20.589 1.00 17.99 ? 85  VAL   A O    1 
ATOM   1155 C CB   . VAL   A 1 105 ? 5.645   1.224  18.558 1.00 19.39 ? 85  VAL   A CB   1 
ATOM   1156 C CG1  . VAL   A 1 105 ? 6.717   0.480  17.738 1.00 20.58 ? 85  VAL   A CG1  1 
ATOM   1157 C CG2  . VAL   A 1 105 ? 5.416   0.518  19.888 1.00 19.93 ? 85  VAL   A CG2  1 
ATOM   1158 H H    . VAL   A 1 105 ? 7.097   2.793  20.358 1.00 21.21 ? 85  VAL   A H    1 
ATOM   1159 H HA   . VAL   A 1 105 ? 6.157   3.105  17.853 1.00 21.19 ? 85  VAL   A HA   1 
ATOM   1160 H HB   . VAL   A 1 105 ? 4.807   1.196  18.072 1.00 23.27 ? 85  VAL   A HB   1 
ATOM   1161 H HG11 . VAL   A 1 105 ? 6.386   -0.404 17.515 1.00 24.70 ? 85  VAL   A HG11 1 
ATOM   1162 H HG12 . VAL   A 1 105 ? 6.898   0.981  16.927 1.00 24.70 ? 85  VAL   A HG12 1 
ATOM   1163 H HG13 . VAL   A 1 105 ? 7.526   0.406  18.269 1.00 24.70 ? 85  VAL   A HG13 1 
ATOM   1164 H HG21 . VAL   A 1 105 ? 5.264   -0.426 19.722 1.00 23.91 ? 85  VAL   A HG21 1 
ATOM   1165 H HG22 . VAL   A 1 105 ? 6.200   0.633  20.446 1.00 23.91 ? 85  VAL   A HG22 1 
ATOM   1166 H HG23 . VAL   A 1 105 ? 4.640   0.906  20.322 1.00 23.91 ? 85  VAL   A HG23 1 
ATOM   1167 N N    . TRP   A 1 106 ? 3.982   3.978  18.506 1.00 16.97 ? 86  TRP   A N    1 
ATOM   1168 C CA   . TRP   A 1 106 ? 2.651   4.437  18.875 1.00 16.54 ? 86  TRP   A CA   1 
ATOM   1169 C C    . TRP   A 1 106 ? 1.665   3.287  18.700 1.00 17.45 ? 86  TRP   A C    1 
ATOM   1170 O O    . TRP   A 1 106 ? 1.710   2.561  17.703 1.00 18.74 ? 86  TRP   A O    1 
ATOM   1171 C CB   . TRP   A 1 106 ? 2.240   5.603  18.005 1.00 16.41 ? 86  TRP   A CB   1 
ATOM   1172 C CG   . TRP   A 1 106 ? 3.174   6.750  17.914 1.00 16.36 ? 86  TRP   A CG   1 
ATOM   1173 C CD1  . TRP   A 1 106 ? 3.914   7.100  16.830 1.00 17.20 ? 86  TRP   A CD1  1 
ATOM   1174 C CD2  . TRP   A 1 106 ? 3.524   7.695  18.965 1.00 16.41 ? 86  TRP   A CD2  1 
ATOM   1175 N NE1  . TRP   A 1 106 ? 4.625   8.234  17.103 1.00 17.20 ? 86  TRP   A NE1  1 
ATOM   1176 C CE2  . TRP   A 1 106 ? 4.449   8.595  18.407 1.00 16.55 ? 86  TRP   A CE2  1 
ATOM   1177 C CE3  . TRP   A 1 106 ? 3.143   7.868  20.294 1.00 17.31 ? 86  TRP   A CE3  1 
ATOM   1178 C CZ2  . TRP   A 1 106 ? 4.975   9.662  19.117 1.00 17.79 ? 86  TRP   A CZ2  1 
ATOM   1179 C CZ3  . TRP   A 1 106 ? 3.683   8.952  21.011 1.00 17.55 ? 86  TRP   A CZ3  1 
ATOM   1180 C CH2  . TRP   A 1 106 ? 4.576   9.823  20.412 1.00 17.90 ? 86  TRP   A CH2  1 
ATOM   1181 H H    . TRP   A 1 106 ? 4.146   4.073  17.668 1.00 20.37 ? 86  TRP   A H    1 
ATOM   1182 H HA   . TRP   A 1 106 ? 2.637   4.731  19.799 1.00 19.85 ? 86  TRP   A HA   1 
ATOM   1183 H HB2  . TRP   A 1 106 ? 2.115   5.271  17.102 1.00 19.69 ? 86  TRP   A HB2  1 
ATOM   1184 H HB3  . TRP   A 1 106 ? 1.402   5.951  18.349 1.00 19.69 ? 86  TRP   A HB3  1 
ATOM   1185 H HD1  . TRP   A 1 106 ? 3.933   6.638  16.024 1.00 20.64 ? 86  TRP   A HD1  1 
ATOM   1186 H HE1  . TRP   A 1 106 ? 5.112   8.659  16.535 1.00 20.64 ? 86  TRP   A HE1  1 
ATOM   1187 H HE3  . TRP   A 1 106 ? 2.546   7.281  20.698 1.00 20.78 ? 86  TRP   A HE3  1 
ATOM   1188 H HZ2  . TRP   A 1 106 ? 5.579   10.249 18.723 1.00 21.35 ? 86  TRP   A HZ2  1 
ATOM   1189 H HZ3  . TRP   A 1 106 ? 3.437   9.084  21.898 1.00 21.06 ? 86  TRP   A HZ3  1 
ATOM   1190 H HH2  . TRP   A 1 106 ? 4.914   10.536 20.904 1.00 21.48 ? 86  TRP   A HH2  1 
ATOM   1191 N N    . THR   A 1 107 ? 0.767   3.130  19.672 1.00 17.26 ? 87  THR   A N    1 
ATOM   1192 C CA   . THR   A 1 107 ? -0.178  2.020  19.712 1.00 18.31 ? 87  THR   A CA   1 
ATOM   1193 C C    . THR   A 1 107 ? -1.565  2.583  20.038 1.00 17.69 ? 87  THR   A C    1 
ATOM   1194 O O    . THR   A 1 107 ? -1.708  3.740  20.420 1.00 17.20 ? 87  THR   A O    1 
ATOM   1195 C CB   . THR   A 1 107 ? 0.212   0.940  20.750 1.00 20.64 ? 87  THR   A CB   1 
ATOM   1196 O OG1  . THR   A 1 107 ? 0.048   1.468  22.072 1.00 21.76 ? 87  THR   A OG1  1 
ATOM   1197 C CG2  . THR   A 1 107 ? 1.663   0.504  20.586 1.00 23.07 ? 87  THR   A CG2  1 
ATOM   1198 H H    . THR   A 1 107 ? 0.686   3.670  20.337 1.00 20.71 ? 87  THR   A H    1 
ATOM   1199 H HA   . THR   A 1 107 ? -0.196  1.589  18.843 1.00 21.97 ? 87  THR   A HA   1 
ATOM   1200 H HB   . THR   A 1 107 ? -0.357  0.165  20.618 1.00 24.77 ? 87  THR   A HB   1 
ATOM   1201 H HG1  . THR   A 1 107 ? -0.769  1.559  22.245 1.00 26.11 ? 87  THR   A HG1  1 
ATOM   1202 H HG21 . THR   A 1 107 ? 1.870   -0.203 21.216 1.00 27.69 ? 87  THR   A HG21 1 
ATOM   1203 H HG22 . THR   A 1 107 ? 1.812   0.177  19.685 1.00 27.69 ? 87  THR   A HG22 1 
ATOM   1204 H HG23 . THR   A 1 107 ? 2.255   1.255  20.750 1.00 27.69 ? 87  THR   A HG23 1 
ATOM   1205 N N    . ASP   A 1 108 ? -2.605  1.763  19.890 1.00 18.50 ? 88  ASP   A N    1 
ATOM   1206 C CA   . ASP   A 1 108 ? -3.964  2.158  20.274 1.00 19.15 ? 88  ASP   A CA   1 
ATOM   1207 C C    . ASP   A 1 108 ? -4.360  3.458  19.584 1.00 18.84 ? 88  ASP   A C    1 
ATOM   1208 O O    . ASP   A 1 108 ? -4.963  4.357  20.168 1.00 18.65 ? 88  ASP   A O    1 
ATOM   1209 C CB   . ASP   A 1 108 ? -4.093  2.230  21.795 1.00 21.05 ? 88  ASP   A CB   1 
ATOM   1210 C CG   . ASP   A 1 108 ? -3.685  0.934  22.430 0.84 24.67 ? 88  ASP   A CG   1 
ATOM   1211 O OD1  . ASP   A 1 108 ? -4.461  -0.034 22.335 1.00 31.00 ? 88  ASP   A OD1  1 
ATOM   1212 O OD2  . ASP   A 1 108 ? -2.528  0.838  22.888 0.70 23.16 ? 88  ASP   A OD2  1 
ATOM   1213 H H    . ASP   A 1 108 ? -2.551  0.968  19.567 1.00 22.20 ? 88  ASP   A H    1 
ATOM   1214 H HA   . ASP   A 1 108 ? -4.596  1.486  19.973 1.00 22.98 ? 88  ASP   A HA   1 
ATOM   1215 H HB2  . ASP   A 1 108 ? -3.519  2.934  22.135 1.00 25.26 ? 88  ASP   A HB2  1 
ATOM   1216 H HB3  . ASP   A 1 108 ? -5.016  2.412  22.033 1.00 25.26 ? 88  ASP   A HB3  1 
ATOM   1217 N N    . ILE   A 1 109 ? -4.020  3.565  18.309 1.00 17.98 ? 89  ILE   A N    1 
ATOM   1218 C CA   . ILE   A 1 109 ? -4.127  4.833  17.592 1.00 17.37 ? 89  ILE   A CA   1 
ATOM   1219 C C    . ILE   A 1 109 ? -5.580  5.068  17.201 1.00 18.23 ? 89  ILE   A C    1 
ATOM   1220 O O    . ILE   A 1 109 ? -6.187  4.236  16.520 1.00 20.97 ? 89  ILE   A O    1 
ATOM   1221 C CB   . ILE   A 1 109 ? -3.220  4.836  16.352 1.00 18.48 ? 89  ILE   A CB   1 
ATOM   1222 C CG1  . ILE   A 1 109 ? -1.740  4.742  16.761 1.00 19.64 ? 89  ILE   A CG1  1 
ATOM   1223 C CG2  . ILE   A 1 109 ? -3.505  6.061  15.470 1.00 19.97 ? 89  ILE   A CG2  1 
ATOM   1224 C CD1  . ILE   A 1 109 ? -0.853  4.223  15.603 1.00 21.66 ? 89  ILE   A CD1  1 
ATOM   1225 H H    . ILE   A 1 109 ? -3.721  2.916  17.831 1.00 21.58 ? 89  ILE   A H    1 
ATOM   1226 H HA   . ILE   A 1 109 ? -3.855  5.552  18.183 1.00 20.85 ? 89  ILE   A HA   1 
ATOM   1227 H HB   . ILE   A 1 109 ? -3.421  4.050  15.820 1.00 22.18 ? 89  ILE   A HB   1 
ATOM   1228 H HG12 . ILE   A 1 109 ? -1.423  5.622  17.016 1.00 23.57 ? 89  ILE   A HG12 1 
ATOM   1229 H HG13 . ILE   A 1 109 ? -1.654  4.129  17.508 1.00 23.57 ? 89  ILE   A HG13 1 
ATOM   1230 H HG21 . ILE   A 1 109 ? -2.772  6.178  14.846 1.00 23.96 ? 89  ILE   A HG21 1 
ATOM   1231 H HG22 . ILE   A 1 109 ? -4.333  5.915  14.985 1.00 23.96 ? 89  ILE   A HG22 1 
ATOM   1232 H HG23 . ILE   A 1 109 ? -3.587  6.845  16.035 1.00 23.96 ? 89  ILE   A HG23 1 
ATOM   1233 H HD11 . ILE   A 1 109 ? 0.064   4.157  15.912 1.00 25.99 ? 89  ILE   A HD11 1 
ATOM   1234 H HD12 . ILE   A 1 109 ? -1.173  3.349  15.327 1.00 25.99 ? 89  ILE   A HD12 1 
ATOM   1235 H HD13 . ILE   A 1 109 ? -0.908  4.844  14.860 1.00 25.99 ? 89  ILE   A HD13 1 
ATOM   1236 N N    . GLN   A 1 110 ? -6.119  6.221  17.611 1.00 17.00 ? 90  GLN   A N    1 
ATOM   1237 C CA   . GLN   A 1 110 ? -7.459  6.651  17.243 1.00 17.37 ? 90  GLN   A CA   1 
ATOM   1238 C C    . GLN   A 1 110 ? -7.327  8.043  16.645 1.00 16.96 ? 90  GLN   A C    1 
ATOM   1239 O O    . GLN   A 1 110 ? -6.962  8.998  17.345 1.00 17.56 ? 90  GLN   A O    1 
ATOM   1240 C CB   . GLN   A 1 110 ? -8.358  6.699  18.466 1.00 21.70 ? 90  GLN   A CB   1 
ATOM   1241 C CG   . GLN   A 1 110 ? -8.463  5.450  19.255 1.00 27.17 ? 90  GLN   A CG   1 
ATOM   1242 C CD   . GLN   A 1 110 ? -9.445  5.646  20.402 1.00 30.74 ? 90  GLN   A CD   1 
ATOM   1243 O OE1  . GLN   A 1 110 ? -9.073  6.056  21.546 1.00 33.72 ? 90  GLN   A OE1  1 
ATOM   1244 N NE2  . GLN   A 1 110 ? -10.726 5.473  20.074 1.00 30.97 ? 90  GLN   A NE2  1 
ATOM   1245 H H    . GLN   A 1 110 ? -5.711  6.784  18.117 1.00 20.40 ? 90  GLN   A H    1 
ATOM   1246 H HA   . GLN   A 1 110 ? -7.849  6.046  16.592 1.00 20.85 ? 90  GLN   A HA   1 
ATOM   1247 H HB2  . GLN   A 1 110 ? -8.019  7.385  19.063 1.00 26.04 ? 90  GLN   A HB2  1 
ATOM   1248 H HB3  . GLN   A 1 110 ? -9.254  6.927  18.173 1.00 26.04 ? 90  GLN   A HB3  1 
ATOM   1249 H HG2  . GLN   A 1 110 ? -8.784  4.731  18.689 1.00 32.61 ? 90  GLN   A HG2  1 
ATOM   1250 H HG3  . GLN   A 1 110 ? -7.595  5.221  19.622 1.00 32.61 ? 90  GLN   A HG3  1 
ATOM   1251 H HE21 . GLN   A 1 110 ? -10.938 5.267  19.266 1.00 37.17 ? 90  GLN   A HE21 1 
ATOM   1252 H HE22 . GLN   A 1 110 ? -11.339 5.567  20.669 1.00 37.17 ? 90  GLN   A HE22 1 
ATOM   1253 N N    . ILE   A 1 111 ? -7.674  8.174  15.373 1.00 17.19 ? 91  ILE   A N    1 
ATOM   1254 C CA   . ILE   A 1 111 ? -7.563  9.436  14.656 1.00 17.12 ? 91  ILE   A CA   1 
ATOM   1255 C C    . ILE   A 1 111 ? -8.930  10.118 14.610 1.00 17.92 ? 91  ILE   A C    1 
ATOM   1256 O O    . ILE   A 1 111 ? -9.938  9.509  14.221 1.00 20.80 ? 91  ILE   A O    1 
ATOM   1257 C CB   . ILE   A 1 111 ? -6.999  9.212  13.237 1.00 19.89 ? 91  ILE   A CB   1 
ATOM   1258 C CG1  . ILE   A 1 111 ? -5.566  8.639  13.303 1.00 22.64 ? 91  ILE   A CG1  1 
ATOM   1259 C CG2  . ILE   A 1 111 ? -7.039  10.524 12.453 1.00 21.69 ? 91  ILE   A CG2  1 
ATOM   1260 C CD1  . ILE   A 1 111 ? -5.040  8.159  11.974 1.00 25.56 ? 91  ILE   A CD1  1 
ATOM   1261 H H    . ILE   A 1 111 ? -7.983  7.531  14.892 1.00 20.63 ? 91  ILE   A H    1 
ATOM   1262 H HA   . ILE   A 1 111 ? -6.963  10.024 15.140 1.00 20.55 ? 91  ILE   A HA   1 
ATOM   1263 H HB   . ILE   A 1 111 ? -7.551  8.560  12.777 1.00 23.87 ? 91  ILE   A HB   1 
ATOM   1264 H HG12 . ILE   A 1 111 ? -4.968  9.331  13.626 1.00 27.17 ? 91  ILE   A HG12 1 
ATOM   1265 H HG13 . ILE   A 1 111 ? -5.559  7.885  13.913 1.00 27.17 ? 91  ILE   A HG13 1 
ATOM   1266 H HG21 . ILE   A 1 111 ? -6.510  10.426 11.646 1.00 26.02 ? 91  ILE   A HG21 1 
ATOM   1267 H HG22 . ILE   A 1 111 ? -7.959  10.726 12.223 1.00 26.02 ? 91  ILE   A HG22 1 
ATOM   1268 H HG23 . ILE   A 1 111 ? -6.673  11.232 13.005 1.00 26.02 ? 91  ILE   A HG23 1 
ATOM   1269 H HD11 . ILE   A 1 111 ? -4.237  7.635  12.122 1.00 30.67 ? 91  ILE   A HD11 1 
ATOM   1270 H HD12 . ILE   A 1 111 ? -5.717  7.613  11.545 1.00 30.67 ? 91  ILE   A HD12 1 
ATOM   1271 H HD13 . ILE   A 1 111 ? -4.835  8.929  11.420 1.00 30.67 ? 91  ILE   A HD13 1 
ATOM   1272 N N    . PHE   A 1 112 ? -8.957  11.399 14.990 1.00 16.92 ? 92  PHE   A N    1 
ATOM   1273 C CA   . PHE   A 1 112 ? -10.169 12.205 14.963 1.00 17.33 ? 92  PHE   A CA   1 
ATOM   1274 C C    . PHE   A 1 112 ? -10.030 13.297 13.914 1.00 17.82 ? 92  PHE   A C    1 
ATOM   1275 O O    . PHE   A 1 112 ? -9.174  14.191 14.020 1.00 18.17 ? 92  PHE   A O    1 
ATOM   1276 C CB   . PHE   A 1 112 ? -10.439 12.803 16.340 1.00 17.64 ? 92  PHE   A CB   1 
ATOM   1277 C CG   . PHE   A 1 112 ? -10.627 11.776 17.390 1.00 18.50 ? 92  PHE   A CG   1 
ATOM   1278 C CD1  . PHE   A 1 112 ? -11.882 11.219 17.620 1.00 19.67 ? 92  PHE   A CD1  1 
ATOM   1279 C CD2  . PHE   A 1 112 ? -9.553  11.340 18.154 1.00 19.57 ? 92  PHE   A CD2  1 
ATOM   1280 C CE1  . PHE   A 1 112 ? -12.057 10.238 18.559 1.00 21.58 ? 92  PHE   A CE1  1 
ATOM   1281 C CE2  . PHE   A 1 112 ? -9.726  10.339 19.105 1.00 20.79 ? 92  PHE   A CE2  1 
ATOM   1282 C CZ   . PHE   A 1 112 ? -11.001 9.818  19.321 1.00 22.23 ? 92  PHE   A CZ   1 
ATOM   1283 H H    . PHE   A 1 112 ? -8.268  11.827 15.274 1.00 20.31 ? 92  PHE   A H    1 
ATOM   1284 H HA   . PHE   A 1 112 ? -10.916 11.643 14.705 1.00 20.80 ? 92  PHE   A HA   1 
ATOM   1285 H HB2  . PHE   A 1 112 ? -9.687  13.358 16.595 1.00 21.17 ? 92  PHE   A HB2  1 
ATOM   1286 H HB3  . PHE   A 1 112 ? -11.247 13.338 16.297 1.00 21.17 ? 92  PHE   A HB3  1 
ATOM   1287 H HD1  . PHE   A 1 112 ? -12.612 11.518 17.129 1.00 23.60 ? 92  PHE   A HD1  1 
ATOM   1288 H HD2  . PHE   A 1 112 ? -8.713  11.720 18.031 1.00 23.48 ? 92  PHE   A HD2  1 
ATOM   1289 H HE1  . PHE   A 1 112 ? -12.896 9.856  18.679 1.00 25.90 ? 92  PHE   A HE1  1 
ATOM   1290 H HE2  . PHE   A 1 112 ? -9.000  10.021 19.591 1.00 24.95 ? 92  PHE   A HE2  1 
ATOM   1291 H HZ   . PHE   A 1 112 ? -11.134 9.182  19.986 1.00 26.68 ? 92  PHE   A HZ   1 
ATOM   1292 N N    . GLU   A 1 113 ? -10.863 13.198 12.878 1.00 18.09 ? 93  GLU   A N    1 
ATOM   1293 C CA   . GLU   A 1 113 ? -11.072 14.334 12.003 1.00 20.04 ? 93  GLU   A CA   1 
ATOM   1294 C C    . GLU   A 1 113 ? -11.870 15.384 12.776 1.00 19.66 ? 93  GLU   A C    1 
ATOM   1295 O O    . GLU   A 1 113 ? -12.503 15.081 13.794 1.00 20.88 ? 93  GLU   A O    1 
ATOM   1296 C CB   . GLU   A 1 113 ? -11.877 13.903 10.782 1.00 24.49 ? 93  GLU   A CB   1 
ATOM   1297 C CG   . GLU   A 1 113 ? -11.358 12.672 10.081 1.00 29.83 ? 93  GLU   A CG   1 
ATOM   1298 C CD   . GLU   A 1 113 ? -12.372 12.126 9.071  1.00 36.63 ? 93  GLU   A CD   1 
ATOM   1299 O OE1  . GLU   A 1 113 ? -13.500 12.654 9.007  1.00 38.65 ? 93  GLU   A OE1  1 
ATOM   1300 O OE2  . GLU   A 1 113 ? -12.048 11.170 8.354  1.00 43.01 ? 93  GLU   A OE2  1 
ATOM   1301 H H    . GLU   A 1 113 ? -11.309 12.493 12.668 1.00 21.71 ? 93  GLU   A H    1 
ATOM   1302 H HA   . GLU   A 1 113 ? -10.227 14.703 11.701 1.00 24.05 ? 93  GLU   A HA   1 
ATOM   1303 H HB2  . GLU   A 1 113 ? -12.786 13.717 11.063 1.00 29.39 ? 93  GLU   A HB2  1 
ATOM   1304 H HB3  . GLU   A 1 113 ? -11.871 14.629 10.138 1.00 29.39 ? 93  GLU   A HB3  1 
ATOM   1305 H HG2  . GLU   A 1 113 ? -10.543 12.895 9.604  1.00 35.79 ? 93  GLU   A HG2  1 
ATOM   1306 H HG3  . GLU   A 1 113 ? -11.180 11.981 10.738 1.00 35.79 ? 93  GLU   A HG3  1 
ATOM   1307 N N    . THR   A 1 114 ? -11.878 16.615 12.285 1.00 19.50 ? 94  THR   A N    1 
ATOM   1308 C CA   . THR   A 1 114 ? -12.660 17.671 12.913 1.00 19.87 ? 94  THR   A CA   1 
ATOM   1309 C C    . THR   A 1 114 ? -13.405 18.464 11.841 1.00 20.69 ? 94  THR   A C    1 
ATOM   1310 O O    . THR   A 1 114 ? -13.279 18.206 10.643 1.00 21.34 ? 94  THR   A O    1 
ATOM   1311 C CB   . THR   A 1 114 ? -11.822 18.617 13.788 1.00 20.36 ? 94  THR   A CB   1 
ATOM   1312 O OG1  . THR   A 1 114 ? -11.108 19.557 12.961 1.00 19.84 ? 94  THR   A OG1  1 
ATOM   1313 C CG2  . THR   A 1 114 ? -10.866 17.877 14.712 1.00 19.65 ? 94  THR   A CG2  1 
ATOM   1314 H H    . THR   A 1 114 ? -11.439 16.863 11.588 1.00 23.40 ? 94  THR   A H    1 
ATOM   1315 H HA   . THR   A 1 114 ? -13.303 17.236 13.494 1.00 23.84 ? 94  THR   A HA   1 
ATOM   1316 H HB   . THR   A 1 114 ? -12.428 19.104 14.368 1.00 24.44 ? 94  THR   A HB   1 
ATOM   1317 H HG1  . THR   A 1 114 ? -10.585 19.148 12.446 1.00 23.82 ? 94  THR   A HG1  1 
ATOM   1318 H HG21 . THR   A 1 114 ? -10.403 18.508 15.286 1.00 23.58 ? 94  THR   A HG21 1 
ATOM   1319 H HG22 . THR   A 1 114 ? -11.357 17.250 15.266 1.00 23.58 ? 94  THR   A HG22 1 
ATOM   1320 H HG23 . THR   A 1 114 ? -10.211 17.388 14.189 1.00 23.58 ? 94  THR   A HG23 1 
ATOM   1321 N N    . GLN   A 1 115 ? -14.176 19.465 12.281 1.00 20.83 ? 95  GLN   A N    1 
ATOM   1322 C CA   . GLN   A 1 115 ? -14.866 20.332 11.329 1.00 22.50 ? 95  GLN   A CA   1 
ATOM   1323 C C    . GLN   A 1 115 ? -13.888 21.148 10.491 1.00 22.68 ? 95  GLN   A C    1 
ATOM   1324 O O    . GLN   A 1 115 ? -14.260 21.653 9.433  1.00 23.92 ? 95  GLN   A O    1 
ATOM   1325 C CB   . GLN   A 1 115 ? -15.860 21.267 12.028 1.00 22.94 ? 95  GLN   A CB   1 
ATOM   1326 C CG   . GLN   A 1 115 ? -15.255 22.350 12.909 1.00 23.07 ? 95  GLN   A CG   1 
ATOM   1327 C CD   . GLN   A 1 115 ? -15.033 21.925 14.358 1.00 23.68 ? 95  GLN   A CD   1 
ATOM   1328 O OE1  . GLN   A 1 115 ? -14.758 20.778 14.676 1.00 20.69 ? 95  GLN   A OE1  1 
ATOM   1329 N NE2  . GLN   A 1 115 ? -15.289 22.852 15.240 1.00 26.72 ? 95  GLN   A NE2  1 
ATOM   1330 H H    . GLN   A 1 115 ? -14.311 19.657 13.108 1.00 25.00 ? 95  GLN   A H    1 
ATOM   1331 H HA   . GLN   A 1 115 ? -15.388 19.768 10.737 1.00 27.00 ? 95  GLN   A HA   1 
ATOM   1332 H HB2  . GLN   A 1 115 ? -16.387 21.713 11.347 1.00 27.53 ? 95  GLN   A HB2  1 
ATOM   1333 H HB3  . GLN   A 1 115 ? -16.436 20.728 12.593 1.00 27.53 ? 95  GLN   A HB3  1 
ATOM   1334 H HG2  . GLN   A 1 115 ? -14.394 22.603 12.541 1.00 27.69 ? 95  GLN   A HG2  1 
ATOM   1335 H HG3  . GLN   A 1 115 ? -15.851 23.115 12.915 1.00 27.69 ? 95  GLN   A HG3  1 
ATOM   1336 H HE21 . GLN   A 1 115 ? -15.558 23.627 14.984 1.00 32.06 ? 95  GLN   A HE21 1 
ATOM   1337 H HE22 . GLN   A 1 115 ? -15.187 22.688 16.078 1.00 32.06 ? 95  GLN   A HE22 1 
ATOM   1338 N N    . ASP   A 1 116 ? -12.645 21.296 10.953 1.00 21.78 ? 96  ASP   A N    1 
ATOM   1339 C CA   . ASP   A 1 116 ? -11.600 21.955 10.176 1.00 21.40 ? 96  ASP   A CA   1 
ATOM   1340 C C    . ASP   A 1 116 ? -10.885 20.862 9.401  1.00 20.75 ? 96  ASP   A C    1 
ATOM   1341 O O    . ASP   A 1 116 ? -10.239 20.001 10.018 1.00 20.43 ? 96  ASP   A O    1 
ATOM   1342 C CB   . ASP   A 1 116 ? -10.659 22.674 11.123 1.00 22.83 ? 96  ASP   A CB   1 
ATOM   1343 C CG   . ASP   A 1 116 ? -9.544  23.415 10.434 1.00 23.84 ? 96  ASP   A CG   1 
ATOM   1344 O OD1  . ASP   A 1 116 ? -9.263  23.143 9.257  1.00 24.35 ? 96  ASP   A OD1  1 
ATOM   1345 O OD2  . ASP   A 1 116 ? -8.909  24.239 11.143 1.00 25.25 ? 96  ASP   A OD2  1 
ATOM   1346 H H    . ASP   A 1 116 ? -12.381 21.018 11.723 1.00 26.14 ? 96  ASP   A H    1 
ATOM   1347 H HA   . ASP   A 1 116 ? -11.956 22.605 9.550  1.00 25.68 ? 96  ASP   A HA   1 
ATOM   1348 H HB2  . ASP   A 1 116 ? -11.168 23.319 11.638 1.00 27.40 ? 96  ASP   A HB2  1 
ATOM   1349 H HB3  . ASP   A 1 116 ? -10.255 22.021 11.716 1.00 27.40 ? 96  ASP   A HB3  1 
ATOM   1350 N N    . PRO   A 1 117 ? -10.987 20.837 8.070  1.00 21.56 ? 97  PRO   A N    1 
ATOM   1351 C CA   . PRO   A 1 117 ? -10.318 19.768 7.312  1.00 21.88 ? 97  PRO   A CA   1 
ATOM   1352 C C    . PRO   A 1 117 ? -8.813  19.740 7.476  1.00 21.29 ? 97  PRO   A C    1 
ATOM   1353 O O    . PRO   A 1 117 ? -8.188  18.718 7.147  1.00 21.86 ? 97  PRO   A O    1 
ATOM   1354 C CB   . PRO   A 1 117 ? -10.683 20.087 5.857  1.00 23.88 ? 97  PRO   A CB   1 
ATOM   1355 C CG   . PRO   A 1 117 ? -10.897 21.544 5.851  1.00 25.50 ? 97  PRO   A CG   1 
ATOM   1356 C CD   . PRO   A 1 117 ? -11.570 21.857 7.171  1.00 23.41 ? 97  PRO   A CD   1 
ATOM   1357 H HA   . PRO   A 1 117 ? -10.690 18.911 7.573  1.00 26.26 ? 97  PRO   A HA   1 
ATOM   1358 H HB2  . PRO   A 1 117 ? -9.954  19.837 5.268  1.00 28.65 ? 97  PRO   A HB2  1 
ATOM   1359 H HB3  . PRO   A 1 117 ? -11.491 19.613 5.605  1.00 28.65 ? 97  PRO   A HB3  1 
ATOM   1360 H HG2  . PRO   A 1 117 ? -10.044 22.002 5.781  1.00 30.60 ? 97  PRO   A HG2  1 
ATOM   1361 H HG3  . PRO   A 1 117 ? -11.467 21.790 5.106  1.00 30.60 ? 97  PRO   A HG3  1 
ATOM   1362 H HD2  . PRO   A 1 117 ? -11.352 22.753 7.472  1.00 28.10 ? 97  PRO   A HD2  1 
ATOM   1363 H HD3  . PRO   A 1 117 ? -12.533 21.754 7.105  1.00 28.10 ? 97  PRO   A HD3  1 
ATOM   1364 N N    . ASN   A 1 118 ? -8.219  20.828 7.976  1.00 20.49 ? 98  ASN   A N    1 
ATOM   1365 C CA   . ASN   A 1 118 ? -6.793  20.928 8.228  1.00 20.26 ? 98  ASN   A CA   1 
ATOM   1366 C C    . ASN   A 1 118 ? -6.406  20.748 9.692  1.00 20.08 ? 98  ASN   A C    1 
ATOM   1367 O O    . ASN   A 1 118 ? -5.268  21.061 10.054 1.00 22.01 ? 98  ASN   A O    1 
ATOM   1368 C CB   . ASN   A 1 118 ? -6.281  22.261 7.714  1.00 22.09 ? 98  ASN   A CB   1 
ATOM   1369 C CG   . ASN   A 1 118 ? -6.371  22.345 6.219  1.00 25.31 ? 98  ASN   A CG   1 
ATOM   1370 O OD1  . ASN   A 1 118 ? -5.872  21.481 5.523  1.00 26.51 ? 98  ASN   A OD1  1 
ATOM   1371 N ND2  . ASN   A 1 118 ? -7.050  23.346 5.724  1.00 28.74 ? 98  ASN   A ND2  1 
ATOM   1372 H H    . ASN   A 1 118 ? -8.644  21.546 8.183  1.00 24.58 ? 98  ASN   A H    1 
ATOM   1373 H HA   . ASN   A 1 118 ? -6.358  20.211 7.741  1.00 24.32 ? 98  ASN   A HA   1 
ATOM   1374 H HB2  . ASN   A 1 118 ? -6.814  22.978 8.092  1.00 26.50 ? 98  ASN   A HB2  1 
ATOM   1375 H HB3  . ASN   A 1 118 ? -5.351  22.368 7.970  1.00 26.50 ? 98  ASN   A HB3  1 
ATOM   1376 H HD21 . ASN   A 1 118 ? -7.128  23.434 4.872  1.00 34.49 ? 98  ASN   A HD21 1 
ATOM   1377 H HD22 . ASN   A 1 118 ? -7.419  23.918 6.251  1.00 34.49 ? 98  ASN   A HD22 1 
ATOM   1378 N N    . TRP   A 1 119 ? -7.282  20.212 10.538 1.00 18.46 ? 99  TRP   A N    1 
ATOM   1379 C CA   . TRP   A 1 119 ? -6.953  19.987 11.952 1.00 17.52 ? 99  TRP   A CA   1 
ATOM   1380 C C    . TRP   A 1 119 ? -7.459  18.621 12.386 1.00 17.56 ? 99  TRP   A C    1 
ATOM   1381 O O    . TRP   A 1 119 ? -8.653  18.324 12.238 1.00 18.48 ? 99  TRP   A O    1 
ATOM   1382 C CB   . TRP   A 1 119 ? -7.561  21.089 12.824 1.00 18.36 ? 99  TRP   A CB   1 
ATOM   1383 C CG   . TRP   A 1 119 ? -6.879  21.320 14.158 1.00 18.15 ? 99  TRP   A CG   1 
ATOM   1384 C CD1  . TRP   A 1 119 ? -6.189  20.409 14.937 1.00 18.06 ? 99  TRP   A CD1  1 
ATOM   1385 C CD2  . TRP   A 1 119 ? -6.836  22.568 14.876 1.00 18.30 ? 99  TRP   A CD2  1 
ATOM   1386 N NE1  . TRP   A 1 119 ? -5.740  21.033 16.088 1.00 17.96 ? 99  TRP   A NE1  1 
ATOM   1387 C CE2  . TRP   A 1 119 ? -6.111  22.352 16.065 1.00 17.82 ? 99  TRP   A CE2  1 
ATOM   1388 C CE3  . TRP   A 1 119 ? -7.335  23.854 14.617 1.00 20.06 ? 99  TRP   A CE3  1 
ATOM   1389 C CZ2  . TRP   A 1 119 ? -5.887  23.368 16.999 1.00 19.33 ? 99  TRP   A CZ2  1 
ATOM   1390 C CZ3  . TRP   A 1 119 ? -7.090  24.876 15.539 1.00 21.78 ? 99  TRP   A CZ3  1 
ATOM   1391 C CH2  . TRP   A 1 119 ? -6.376  24.620 16.718 1.00 21.08 ? 99  TRP   A CH2  1 
ATOM   1392 H H    . TRP   A 1 119 ? -8.078  19.969 10.321 1.00 22.15 ? 99  TRP   A H    1 
ATOM   1393 H HA   . TRP   A 1 119 ? -5.989  19.986 12.061 1.00 21.03 ? 99  TRP   A HA   1 
ATOM   1394 H HB2  . TRP   A 1 119 ? -7.520  21.924 12.331 1.00 22.03 ? 99  TRP   A HB2  1 
ATOM   1395 H HB3  . TRP   A 1 119 ? -8.485  20.858 13.008 1.00 22.03 ? 99  TRP   A HB3  1 
ATOM   1396 H HD1  . TRP   A 1 119 ? -6.047  19.516 14.721 1.00 21.68 ? 99  TRP   A HD1  1 
ATOM   1397 H HE1  . TRP   A 1 119 ? -5.297  20.652 16.719 1.00 21.55 ? 99  TRP   A HE1  1 
ATOM   1398 H HE3  . TRP   A 1 119 ? -7.821  24.024 13.843 1.00 24.08 ? 99  TRP   A HE3  1 
ATOM   1399 H HZ2  . TRP   A 1 119 ? -5.422  23.200 17.786 1.00 23.20 ? 99  TRP   A HZ2  1 
ATOM   1400 H HZ3  . TRP   A 1 119 ? -7.404  25.734 15.368 1.00 26.13 ? 99  TRP   A HZ3  1 
ATOM   1401 H HH2  . TRP   A 1 119 ? -6.229  25.312 17.321 1.00 25.29 ? 99  TRP   A HH2  1 
ATOM   1402 N N    . PHE   A 1 120 ? -6.544  17.794 12.887 1.00 17.54 ? 100 PHE   A N    1 
ATOM   1403 C CA   . PHE   A 1 120 ? -6.834  16.470 13.399 1.00 17.07 ? 100 PHE   A CA   1 
ATOM   1404 C C    . PHE   A 1 120 ? -6.298  16.352 14.814 1.00 16.63 ? 100 PHE   A C    1 
ATOM   1405 O O    . PHE   A 1 120 ? -5.305  16.994 15.181 1.00 17.49 ? 100 PHE   A O    1 
ATOM   1406 C CB   . PHE   A 1 120 ? -6.127  15.372 12.548 1.00 18.08 ? 100 PHE   A CB   1 
ATOM   1407 C CG   . PHE   A 1 120 ? -6.711  15.213 11.184 1.00 19.01 ? 100 PHE   A CG   1 
ATOM   1408 C CD1  . PHE   A 1 120 ? -6.546  16.192 10.205 1.00 23.60 ? 100 PHE   A CD1  1 
ATOM   1409 C CD2  . PHE   A 1 120 ? -7.416  14.072 10.854 1.00 20.95 ? 100 PHE   A CD2  1 
ATOM   1410 C CE1  . PHE   A 1 120 ? -7.111  16.041 8.961  1.00 25.75 ? 100 PHE   A CE1  1 
ATOM   1411 C CE2  . PHE   A 1 120 ? -7.966  13.913 9.588  1.00 23.81 ? 100 PHE   A CE2  1 
ATOM   1412 C CZ   . PHE   A 1 120 ? -7.817  14.905 8.660  1.00 24.91 ? 100 PHE   A CZ   1 
ATOM   1413 H H    . PHE   A 1 120 ? -5.709  17.993 12.941 1.00 21.05 ? 100 PHE   A H    1 
ATOM   1414 H HA   . PHE   A 1 120 ? -7.794  16.331 13.392 1.00 20.49 ? 100 PHE   A HA   1 
ATOM   1415 H HB2  . PHE   A 1 120 ? -5.192  15.609 12.445 1.00 21.70 ? 100 PHE   A HB2  1 
ATOM   1416 H HB3  . PHE   A 1 120 ? -6.206  14.521 13.006 1.00 21.70 ? 100 PHE   A HB3  1 
ATOM   1417 H HD1  . PHE   A 1 120 ? -6.048  16.955 10.395 1.00 28.32 ? 100 PHE   A HD1  1 
ATOM   1418 H HD2  . PHE   A 1 120 ? -7.523  13.401 11.488 1.00 25.15 ? 100 PHE   A HD2  1 
ATOM   1419 H HE1  . PHE   A 1 120 ? -7.014  16.710 8.322  1.00 30.90 ? 100 PHE   A HE1  1 
ATOM   1420 H HE2  . PHE   A 1 120 ? -8.431  13.137 9.374  1.00 28.57 ? 100 PHE   A HE2  1 
ATOM   1421 H HZ   . PHE   A 1 120 ? -8.198  14.809 7.817  1.00 29.89 ? 100 PHE   A HZ   1 
ATOM   1422 N N    . TRP   A 1 121 ? -6.919  15.466 15.578 1.00 16.24 ? 101 TRP   A N    1 
ATOM   1423 C CA   . TRP   A 1 121 ? -6.415  15.050 16.877 1.00 15.74 ? 101 TRP   A CA   1 
ATOM   1424 C C    . TRP   A 1 121 ? -6.236  13.542 16.856 1.00 15.89 ? 101 TRP   A C    1 
ATOM   1425 O O    . TRP   A 1 121 ? -6.964  12.832 16.164 1.00 17.67 ? 101 TRP   A O    1 
ATOM   1426 C CB   . TRP   A 1 121 ? -7.364  15.468 18.040 1.00 15.85 ? 101 TRP   A CB   1 
ATOM   1427 C CG   . TRP   A 1 121 ? -7.393  16.935 18.223 1.00 16.22 ? 101 TRP   A CG   1 
ATOM   1428 C CD1  . TRP   A 1 121 ? -8.181  17.849 17.553 1.00 17.94 ? 101 TRP   A CD1  1 
ATOM   1429 C CD2  . TRP   A 1 121 ? -6.592  17.689 19.140 1.00 15.81 ? 101 TRP   A CD2  1 
ATOM   1430 N NE1  . TRP   A 1 121 ? -7.884  19.127 17.997 1.00 17.35 ? 101 TRP   A NE1  1 
ATOM   1431 C CE2  . TRP   A 1 121 ? -6.906  19.050 18.963 1.00 16.12 ? 101 TRP   A CE2  1 
ATOM   1432 C CE3  . TRP   A 1 121 ? -5.617  17.343 20.074 1.00 15.97 ? 101 TRP   A CE3  1 
ATOM   1433 C CZ2  . TRP   A 1 121 ? -6.305  20.062 19.732 1.00 16.86 ? 101 TRP   A CZ2  1 
ATOM   1434 C CZ3  . TRP   A 1 121 ? -5.030  18.350 20.836 1.00 16.26 ? 101 TRP   A CZ3  1 
ATOM   1435 C CH2  . TRP   A 1 121 ? -5.343  19.681 20.633 1.00 16.92 ? 101 TRP   A CH2  1 
ATOM   1436 H H    . TRP   A 1 121 ? -7.656  15.081 15.359 1.00 19.49 ? 101 TRP   A H    1 
ATOM   1437 H HA   . TRP   A 1 121 ? -5.560  15.471 17.055 1.00 18.89 ? 101 TRP   A HA   1 
ATOM   1438 H HB2  . TRP   A 1 121 ? -8.265  15.169 17.840 1.00 19.02 ? 101 TRP   A HB2  1 
ATOM   1439 H HB3  . TRP   A 1 121 ? -7.055  15.064 18.866 1.00 19.02 ? 101 TRP   A HB3  1 
ATOM   1440 H HD1  . TRP   A 1 121 ? -8.814  17.639 16.904 1.00 21.53 ? 101 TRP   A HD1  1 
ATOM   1441 H HE1  . TRP   A 1 121 ? -8.252  19.852 17.715 1.00 20.82 ? 101 TRP   A HE1  1 
ATOM   1442 H HE3  . TRP   A 1 121 ? -5.363  16.455 20.187 1.00 19.16 ? 101 TRP   A HE3  1 
ATOM   1443 H HZ2  . TRP   A 1 121 ? -6.550  20.954 19.634 1.00 20.23 ? 101 TRP   A HZ2  1 
ATOM   1444 H HZ3  . TRP   A 1 121 ? -4.415  18.122 21.495 1.00 19.51 ? 101 TRP   A HZ3  1 
ATOM   1445 H HH2  . TRP   A 1 121 ? -4.891  20.333 21.118 1.00 20.31 ? 101 TRP   A HH2  1 
ATOM   1446 N N    . VAL   A 1 122 ? -5.263  13.074 17.628 1.00 15.23 ? 102 VAL   A N    1 
ATOM   1447 C CA   . VAL   A 1 122 ? -5.024  11.644 17.763 1.00 15.16 ? 102 VAL   A CA   1 
ATOM   1448 C C    . VAL   A 1 122 ? -4.897  11.311 19.235 1.00 15.41 ? 102 VAL   A C    1 
ATOM   1449 O O    . VAL   A 1 122 ? -4.164  11.983 19.964 1.00 17.25 ? 102 VAL   A O    1 
ATOM   1450 C CB   . VAL   A 1 122 ? -3.742  11.208 17.017 1.00 16.05 ? 102 VAL   A CB   1 
ATOM   1451 C CG1  . VAL   A 1 122 ? -3.501  9.725  17.180 1.00 17.81 ? 102 VAL   A CG1  1 
ATOM   1452 C CG2  . VAL   A 1 122 ? -3.826  11.606 15.531 1.00 18.64 ? 102 VAL   A CG2  1 
ATOM   1453 H H    . VAL   A 1 122 ? -4.728  13.567 18.086 1.00 18.28 ? 102 VAL   A H    1 
ATOM   1454 H HA   . VAL   A 1 122 ? -5.782  11.161 17.398 1.00 18.20 ? 102 VAL   A HA   1 
ATOM   1455 H HB   . VAL   A 1 122 ? -2.981  11.667 17.405 1.00 19.26 ? 102 VAL   A HB   1 
ATOM   1456 H HG11 . VAL   A 1 122 ? -2.796  9.451  16.573 1.00 21.37 ? 102 VAL   A HG11 1 
ATOM   1457 H HG12 . VAL   A 1 122 ? -3.237  9.546  18.096 1.00 21.37 ? 102 VAL   A HG12 1 
ATOM   1458 H HG13 . VAL   A 1 122 ? -4.320  9.247  16.973 1.00 21.37 ? 102 VAL   A HG13 1 
ATOM   1459 H HG21 . VAL   A 1 122 ? -3.038  11.277 15.071 1.00 22.37 ? 102 VAL   A HG21 1 
ATOM   1460 H HG22 . VAL   A 1 122 ? -4.624  11.213 15.143 1.00 22.37 ? 102 VAL   A HG22 1 
ATOM   1461 H HG23 . VAL   A 1 122 ? -3.868  12.573 15.465 1.00 22.37 ? 102 VAL   A HG23 1 
ATOM   1462 N N    . GLU   A 1 123 ? -5.600  10.280 19.667 1.00 14.82 ? 103 GLU   A N    1 
ATOM   1463 C CA   . GLU   A 1 123 ? -5.408  9.700  20.986 1.00 15.07 ? 103 GLU   A CA   1 
ATOM   1464 C C    . GLU   A 1 123 ? -4.672  8.373  20.787 1.00 15.12 ? 103 GLU   A C    1 
ATOM   1465 O O    . GLU   A 1 123 ? -5.038  7.578  19.911 1.00 16.12 ? 103 GLU   A O    1 
ATOM   1466 C CB   . GLU   A 1 123 ? -6.748  9.487  21.715 1.00 15.58 ? 103 GLU   A CB   1 
ATOM   1467 C CG   . GLU   A 1 123 ? -6.522  8.848  23.094 1.00 16.49 ? 103 GLU   A CG   1 
ATOM   1468 C CD   . GLU   A 1 123 ? -7.754  8.745  23.960 1.00 17.77 ? 103 GLU   A CD   1 
ATOM   1469 O OE1  . GLU   A 1 123 ? -8.895  8.912  23.488 1.00 18.08 ? 103 GLU   A OE1  1 
ATOM   1470 O OE2  . GLU   A 1 123 ? -7.556  8.447  25.156 1.00 20.06 ? 103 GLU   A OE2  1 
ATOM   1471 H H    . GLU   A 1 123 ? -6.209  9.888  19.204 1.00 17.78 ? 103 GLU   A H    1 
ATOM   1472 H HA   . GLU   A 1 123 ? -4.880  10.286 21.550 1.00 18.09 ? 103 GLU   A HA   1 
ATOM   1473 H HB2  . GLU   A 1 123 ? -7.188  10.342 21.839 1.00 18.70 ? 103 GLU   A HB2  1 
ATOM   1474 H HB3  . GLU   A 1 123 ? -7.311  8.897  21.190 1.00 18.70 ? 103 GLU   A HB3  1 
ATOM   1475 H HG2  . GLU   A 1 123 ? -6.182  7.949  22.964 1.00 19.79 ? 103 GLU   A HG2  1 
ATOM   1476 H HG3  . GLU   A 1 123 ? -5.871  9.382  23.577 1.00 19.79 ? 103 GLU   A HG3  1 
ATOM   1477 N N    . CYS   A 1 124 ? -3.626  8.134  21.578 1.00 15.01 ? 104 CYS   A N    1 
ATOM   1478 C CA   . CYS   A 1 124 ? -2.895  6.875  21.422 1.00 15.04 ? 104 CYS   A CA   1 
ATOM   1479 C C    . CYS   A 1 124 ? -2.093  6.618  22.688 1.00 15.68 ? 104 CYS   A C    1 
ATOM   1480 O O    . CYS   A 1 124 ? -2.145  7.386  23.649 1.00 16.65 ? 104 CYS   A O    1 
ATOM   1481 C CB   . CYS   A 1 124 ? -1.943  6.963  20.219 1.00 16.85 ? 104 CYS   A CB   1 
ATOM   1482 S SG   . CYS   A 1 124 ? -0.590  8.154  20.397 1.00 18.04 ? 104 CYS   A SG   1 
ATOM   1483 H H    . CYS   A 1 124 ? -3.331  8.663  22.189 1.00 18.01 ? 104 CYS   A H    1 
ATOM   1484 H HA   . CYS   A 1 124 ? -3.533  6.156  21.298 1.00 18.05 ? 104 CYS   A HA   1 
ATOM   1485 H HB2  . CYS   A 1 124 ? -1.545  6.089  20.079 1.00 20.22 ? 104 CYS   A HB2  1 
ATOM   1486 H HB3  . CYS   A 1 124 ? -2.458  7.222  19.439 1.00 20.22 ? 104 CYS   A HB3  1 
ATOM   1487 H HG   . CYS   A 1 124 ? 0.151   8.047  19.460 1.00 21.65 ? 104 CYS   A HG   1 
ATOM   1488 N N    . ARG   A 1 125 ? -1.369  5.511  22.690 1.00 16.12 ? 105 ARG   A N    1 
ATOM   1489 C CA   . ARG   A 1 125 ? -0.323  5.283  23.662 1.00 16.53 ? 105 ARG   A CA   1 
ATOM   1490 C C    . ARG   A 1 125 ? 0.995   5.207  22.909 1.00 16.65 ? 105 ARG   A C    1 
ATOM   1491 O O    . ARG   A 1 125 ? 1.041   5.101  21.683 1.00 17.76 ? 105 ARG   A O    1 
ATOM   1492 C CB   . ARG   A 1 125 ? -0.582  4.014  24.469 1.00 17.68 ? 105 ARG   A CB   1 
ATOM   1493 C CG   . ARG   A 1 125 ? -1.839  4.170  25.350 1.00 19.97 ? 105 ARG   A CG   1 
ATOM   1494 C CD   . ARG   A 1 125 ? -2.034  2.992  26.301 1.00 22.76 ? 105 ARG   A CD   1 
ATOM   1495 N NE   . ARG   A 1 125 ? -2.162  1.740  25.548 1.00 26.75 ? 105 ARG   A NE   1 
ATOM   1496 C CZ   . ARG   A 1 125 ? -2.283  0.537  26.091 1.00 28.14 ? 105 ARG   A CZ   1 
ATOM   1497 N NH1  . ARG   A 1 125 ? -2.293  0.372  27.403 1.00 29.60 ? 105 ARG   A NH1  1 
ATOM   1498 N NH2  . ARG   A 1 125 ? -2.389  -0.528 25.298 1.00 27.63 ? 105 ARG   A NH2  1 
ATOM   1499 H H    . ARG   A 1 125 ? -1.470  4.869  22.127 1.00 19.35 ? 105 ARG   A H    1 
ATOM   1500 H HA   . ARG   A 1 125 ? -0.278  6.011  24.302 1.00 19.83 ? 105 ARG   A HA   1 
ATOM   1501 H HB2  . ARG   A 1 125 ? -0.721  3.269  23.863 1.00 21.22 ? 105 ARG   A HB2  1 
ATOM   1502 H HB3  . ARG   A 1 125 ? 0.177   3.837  25.045 1.00 21.22 ? 105 ARG   A HB3  1 
ATOM   1503 H HG2  . ARG   A 1 125 ? -1.756  4.976  25.883 1.00 23.96 ? 105 ARG   A HG2  1 
ATOM   1504 H HG3  . ARG   A 1 125 ? -2.622  4.228  24.780 1.00 23.96 ? 105 ARG   A HG3  1 
ATOM   1505 H HD2  . ARG   A 1 125 ? -1.267  2.920  26.891 1.00 27.31 ? 105 ARG   A HD2  1 
ATOM   1506 H HD3  . ARG   A 1 125 ? -2.841  3.124  26.821 1.00 27.31 ? 105 ARG   A HD3  1 
ATOM   1507 H HE   . ARG   A 1 125 ? -2.158  1.790  24.689 1.00 32.10 ? 105 ARG   A HE   1 
ATOM   1508 H HH11 . ARG   A 1 125 ? -2.219  1.054  27.923 1.00 35.53 ? 105 ARG   A HH11 1 
ATOM   1509 H HH12 . ARG   A 1 125 ? -2.372  -0.416 27.737 1.00 35.53 ? 105 ARG   A HH12 1 
ATOM   1510 H HH21 . ARG   A 1 125 ? -2.378  -0.431 24.444 1.00 33.16 ? 105 ARG   A HH21 1 
ATOM   1511 H HH22 . ARG   A 1 125 ? -2.468  -1.313 25.641 1.00 33.16 ? 105 ARG   A HH22 1 
ATOM   1512 N N    . GLY   A 1 126 ? 2.082   5.277  23.651 1.00 17.09 ? 106 GLY   A N    1 
ATOM   1513 C CA   . GLY   A 1 126 ? 3.406   5.093  23.081 1.00 18.68 ? 106 GLY   A CA   1 
ATOM   1514 C C    . GLY   A 1 126 ? 4.257   4.317  24.053 1.00 18.52 ? 106 GLY   A C    1 
ATOM   1515 O O    . GLY   A 1 126 ? 4.068   4.397  25.264 1.00 19.27 ? 106 GLY   A O    1 
ATOM   1516 H H    . GLY   A 1 126 ? 2.083   5.432  24.497 1.00 20.51 ? 106 GLY   A H    1 
ATOM   1517 H HA2  . GLY   A 1 126 ? 3.345   4.602  22.247 1.00 22.41 ? 106 GLY   A HA2  1 
ATOM   1518 H HA3  . GLY   A 1 126 ? 3.819   5.954  22.912 1.00 22.41 ? 106 GLY   A HA3  1 
ATOM   1519 N N    . GLU   A 1 127 ? 5.197   3.549  23.505 1.00 18.52 ? 107 GLU   A N    1 
ATOM   1520 C CA   . GLU   A 1 127 ? 6.080   2.797  24.366 1.00 19.71 ? 107 GLU   A CA   1 
ATOM   1521 C C    . GLU   A 1 127 ? 7.391   2.453  23.688 1.00 19.21 ? 107 GLU   A C    1 
ATOM   1522 O O    . GLU   A 1 127 ? 7.472   2.290  22.465 1.00 18.98 ? 107 GLU   A O    1 
ATOM   1523 C CB   . GLU   A 1 127 ? 5.431   1.509  24.844 1.00 21.74 ? 107 GLU   A CB   1 
ATOM   1524 C CG   . GLU   A 1 127 ? 5.076   0.551  23.756 1.00 24.38 ? 107 GLU   A CG   1 
ATOM   1525 C CD   . GLU   A 1 127 ? 4.501   -0.670 24.379 1.00 28.60 ? 107 GLU   A CD   1 
ATOM   1526 O OE1  . GLU   A 1 127 ? 5.285   -1.448 24.963 1.00 32.66 ? 107 GLU   A OE1  1 
ATOM   1527 O OE2  . GLU   A 1 127 ? 3.262   -0.803 24.383 1.00 31.41 ? 107 GLU   A OE2  1 
ATOM   1528 H H    . GLU   A 1 127 ? 5.333   3.455  22.661 1.00 22.22 ? 107 GLU   A H    1 
ATOM   1529 H HA   . GLU   A 1 127 ? 6.288   3.375  25.116 1.00 23.65 ? 107 GLU   A HA   1 
ATOM   1530 H HB2  . GLU   A 1 127 ? 6.047   1.057  25.442 1.00 26.08 ? 107 GLU   A HB2  1 
ATOM   1531 H HB3  . GLU   A 1 127 ? 4.613   1.732  25.316 1.00 26.08 ? 107 GLU   A HB3  1 
ATOM   1532 H HG2  . GLU   A 1 127 ? 4.417   0.948  23.165 1.00 29.25 ? 107 GLU   A HG2  1 
ATOM   1533 H HG3  . GLU   A 1 127 ? 5.869   0.309  23.253 1.00 29.25 ? 107 GLU   A HG3  1 
ATOM   1534 N N    . GLY   A 1 128 ? 8.399   2.275  24.524 1.00 18.34 ? 108 GLY   A N    1 
ATOM   1535 C CA   . GLY   A 1 128 ? 9.678   1.802  24.043 1.00 18.85 ? 108 GLY   A CA   1 
ATOM   1536 C C    . GLY   A 1 128 ? 10.733  1.974  25.095 1.00 19.80 ? 108 GLY   A C    1 
ATOM   1537 O O    . GLY   A 1 128 ? 10.504  2.566  26.157 1.00 20.15 ? 108 GLY   A O    1 
ATOM   1538 H H    . GLY   A 1 128 ? 8.367   2.422  25.371 1.00 22.01 ? 108 GLY   A H    1 
ATOM   1539 H HA2  . GLY   A 1 128 ? 9.615   0.862  23.814 1.00 22.62 ? 108 GLY   A HA2  1 
ATOM   1540 H HA3  . GLY   A 1 128 ? 9.938   2.303  23.255 1.00 22.62 ? 108 GLY   A HA3  1 
ATOM   1541 N N    . ALA   A 1 129 ? 11.913  1.464  24.766 1.00 20.17 ? 109 ALA   A N    1 
ATOM   1542 C CA   . ALA   A 1 129 ? 13.067  1.704  25.611 1.00 21.33 ? 109 ALA   A CA   1 
ATOM   1543 C C    . ALA   A 1 129 ? 13.379  3.204  25.636 1.00 20.77 ? 109 ALA   A C    1 
ATOM   1544 O O    . ALA   A 1 129 ? 13.215  3.909  24.636 1.00 21.77 ? 109 ALA   A O    1 
ATOM   1545 C CB   . ALA   A 1 129 ? 14.271  0.936  25.057 1.00 24.05 ? 109 ALA   A CB   1 
ATOM   1546 H H    . ALA   A 1 129 ? 12.067  0.983  24.069 1.00 24.21 ? 109 ALA   A H    1 
ATOM   1547 H HA   . ALA   A 1 129 ? 12.893  1.402  26.516 1.00 25.60 ? 109 ALA   A HA   1 
ATOM   1548 H HB1  . ALA   A 1 129 ? 15.037  1.093  25.631 1.00 28.86 ? 109 ALA   A HB1  1 
ATOM   1549 H HB2  . ALA   A 1 129 ? 14.060  -0.010 25.039 1.00 28.86 ? 109 ALA   A HB2  1 
ATOM   1550 H HB3  . ALA   A 1 129 ? 14.460  1.251  24.160 1.00 28.86 ? 109 ALA   A HB3  1 
ATOM   1551 N N    . ILE   A 1 130 ? 13.825  3.701  26.787 1.00 21.35 ? 110 ILE   A N    1 
ATOM   1552 C CA   . ILE   A 1 130 ? 14.282  5.085  26.931 1.00 20.82 ? 110 ILE   A CA   1 
ATOM   1553 C C    . ILE   A 1 130 ? 15.756  5.059  27.314 1.00 22.14 ? 110 ILE   A C    1 
ATOM   1554 O O    . ILE   A 1 130 ? 16.131  4.470  28.335 1.00 23.05 ? 110 ILE   A O    1 
ATOM   1555 C CB   . ILE   A 1 130 ? 13.425  5.898  27.931 1.00 21.46 ? 110 ILE   A CB   1 
ATOM   1556 C CG1  . ILE   A 1 130 ? 13.903  7.347  28.003 1.00 22.07 ? 110 ILE   A CG1  1 
ATOM   1557 C CG2  . ILE   A 1 130 ? 13.300  5.241  29.326 1.00 22.18 ? 110 ILE   A CG2  1 
ATOM   1558 C CD1  . ILE   A 1 130 ? 12.896  8.278  28.671 1.00 22.53 ? 110 ILE   A CD1  1 
ATOM   1559 H H    . ILE   A 1 130 ? 13.873  3.248  27.516 1.00 25.62 ? 110 ILE   A H    1 
ATOM   1560 H HA   . ILE   A 1 130 ? 14.212  5.535  26.074 1.00 24.99 ? 110 ILE   A HA   1 
ATOM   1561 H HB   . ILE   A 1 130 ? 12.521  5.899  27.578 1.00 25.75 ? 110 ILE   A HB   1 
ATOM   1562 H HG12 . ILE   A 1 130 ? 14.727  7.381  28.513 1.00 26.48 ? 110 ILE   A HG12 1 
ATOM   1563 H HG13 . ILE   A 1 130 ? 14.057  7.672  27.102 1.00 26.48 ? 110 ILE   A HG13 1 
ATOM   1564 H HG21 . ILE   A 1 130 ? 12.702  5.774  29.873 1.00 26.61 ? 110 ILE   A HG21 1 
ATOM   1565 H HG22 . ILE   A 1 130 ? 12.943  4.345  29.222 1.00 26.61 ? 110 ILE   A HG22 1 
ATOM   1566 H HG23 . ILE   A 1 130 ? 14.178  5.202  29.736 1.00 26.61 ? 110 ILE   A HG23 1 
ATOM   1567 H HD11 . ILE   A 1 130 ? 13.223  9.189  28.615 1.00 27.04 ? 110 ILE   A HD11 1 
ATOM   1568 H HD12 . ILE   A 1 130 ? 12.044  8.203  28.214 1.00 27.04 ? 110 ILE   A HD12 1 
ATOM   1569 H HD13 . ILE   A 1 130 ? 12.797  8.019  29.601 1.00 27.04 ? 110 ILE   A HD13 1 
ATOM   1570 N N    . VAL   A 1 131 ? 16.583  5.689  26.482 1.00 21.65 ? 111 VAL   A N    1 
ATOM   1571 C CA   . VAL   A 1 131 ? 18.034  5.717  26.637 1.00 22.63 ? 111 VAL   A CA   1 
ATOM   1572 C C    . VAL   A 1 131 ? 18.440  7.176  26.661 1.00 22.05 ? 111 VAL   A C    1 
ATOM   1573 O O    . VAL   A 1 131 ? 19.025  7.703  25.708 1.00 23.69 ? 111 VAL   A O    1 
ATOM   1574 C CB   . VAL   A 1 131 ? 18.719  4.966  25.491 1.00 24.48 ? 111 VAL   A CB   1 
ATOM   1575 C CG1  . VAL   A 1 131 ? 20.197  4.811  25.780 1.00 25.92 ? 111 VAL   A CG1  1 
ATOM   1576 C CG2  . VAL   A 1 131 ? 18.016  3.622  25.274 1.00 26.38 ? 111 VAL   A CG2  1 
ATOM   1577 H H    . VAL   A 1 131 ? 16.316  6.127  25.791 1.00 25.98 ? 111 VAL   A H    1 
ATOM   1578 H HA   . VAL   A 1 131 ? 18.303  5.290  27.465 1.00 27.16 ? 111 VAL   A HA   1 
ATOM   1579 H HB   . VAL   A 1 131 ? 18.650  5.467  24.663 1.00 29.38 ? 111 VAL   A HB   1 
ATOM   1580 H HG11 . VAL   A 1 131 ? 20.606  4.293  25.069 1.00 31.10 ? 111 VAL   A HG11 1 
ATOM   1581 H HG12 . VAL   A 1 131 ? 20.605  5.690  25.825 1.00 31.10 ? 111 VAL   A HG12 1 
ATOM   1582 H HG13 . VAL   A 1 131 ? 20.307  4.352  26.628 1.00 31.10 ? 111 VAL   A HG13 1 
ATOM   1583 H HG21 . VAL   A 1 131 ? 18.600  3.039  24.765 1.00 31.66 ? 111 VAL   A HG21 1 
ATOM   1584 H HG22 . VAL   A 1 131 ? 17.822  3.225  26.137 1.00 31.66 ? 111 VAL   A HG22 1 
ATOM   1585 H HG23 . VAL   A 1 131 ? 17.191  3.773  24.786 1.00 31.66 ? 111 VAL   A HG23 1 
ATOM   1586 N N    . PHE   A 1 132 ? 18.103  7.844  27.734 1.00 21.78 ? 112 PHE   A N    1 
ATOM   1587 C CA   . PHE   A 1 132 ? 18.253  9.272  27.851 1.00 22.32 ? 112 PHE   A CA   1 
ATOM   1588 C C    . PHE   A 1 132 ? 19.635  9.565  28.405 1.00 23.72 ? 112 PHE   A C    1 
ATOM   1589 O O    . PHE   A 1 132 ? 20.111  8.889  29.314 1.00 25.02 ? 112 PHE   A O    1 
ATOM   1590 C CB   . PHE   A 1 132 ? 17.205  9.761  28.841 1.00 25.28 ? 112 PHE   A CB   1 
ATOM   1591 C CG   . PHE   A 1 132 ? 16.473  10.970 28.428 1.00 26.02 ? 112 PHE   A CG   1 
ATOM   1592 C CD1  . PHE   A 1 132 ? 15.529  10.908 27.422 1.00 31.12 ? 112 PHE   A CD1  1 
ATOM   1593 C CD2  . PHE   A 1 132 ? 16.670  12.169 29.103 1.00 31.80 ? 112 PHE   A CD2  1 
ATOM   1594 C CE1  . PHE   A 1 132 ? 14.795  12.023 27.082 1.00 33.50 ? 112 PHE   A CE1  1 
ATOM   1595 C CE2  . PHE   A 1 132 ? 15.958  13.309 28.749 1.00 34.71 ? 112 PHE   A CE2  1 
ATOM   1596 C CZ   . PHE   A 1 132 ? 15.014  13.233 27.746 1.00 34.51 ? 112 PHE   A CZ   1 
ATOM   1597 H H    . PHE   A 1 132 ? 17.771  7.483  28.440 1.00 26.14 ? 112 PHE   A H    1 
ATOM   1598 H HA   . PHE   A 1 132 ? 18.150  9.732  27.003 1.00 26.79 ? 112 PHE   A HA   1 
ATOM   1599 H HB2  . PHE   A 1 132 ? 16.552  9.055  28.969 1.00 30.34 ? 112 PHE   A HB2  1 
ATOM   1600 H HB3  . PHE   A 1 132 ? 17.646  9.961  29.681 1.00 30.34 ? 112 PHE   A HB3  1 
ATOM   1601 H HD1  . PHE   A 1 132 ? 15.388  10.107 26.970 1.00 37.34 ? 112 PHE   A HD1  1 
ATOM   1602 H HD2  . PHE   A 1 132 ? 17.286  12.209 29.799 1.00 38.16 ? 112 PHE   A HD2  1 
ATOM   1603 H HE1  . PHE   A 1 132 ? 14.153  11.970 26.410 1.00 40.20 ? 112 PHE   A HE1  1 
ATOM   1604 H HE2  . PHE   A 1 132 ? 16.116  14.115 29.185 1.00 41.66 ? 112 PHE   A HE2  1 
ATOM   1605 H HZ   . PHE   A 1 132 ? 14.524  13.987 27.511 1.00 41.41 ? 112 PHE   A HZ   1 
ATOM   1606 N N    . PRO   A 1 133 ? 20.323  10.578 27.856 1.00 25.26 ? 113 PRO   A N    1 
ATOM   1607 C CA   . PRO   A 1 133 ? 21.712  10.811 28.285 1.00 25.62 ? 113 PRO   A CA   1 
ATOM   1608 C C    . PRO   A 1 133 ? 21.790  11.075 29.782 1.00 26.27 ? 113 PRO   A C    1 
ATOM   1609 O O    . PRO   A 1 133 ? 21.129  11.955 30.309 1.00 29.33 ? 113 PRO   A O    1 
ATOM   1610 C CB   . PRO   A 1 133 ? 22.109  12.055 27.484 1.00 27.78 ? 113 PRO   A CB   1 
ATOM   1611 C CG   . PRO   A 1 133 ? 21.247  11.996 26.259 1.00 29.07 ? 113 PRO   A CG   1 
ATOM   1612 C CD   . PRO   A 1 133 ? 19.944  11.414 26.706 1.00 27.15 ? 113 PRO   A CD   1 
ATOM   1613 H HA   . PRO   A 1 133 ? 22.277  10.058 28.051 1.00 30.74 ? 113 PRO   A HA   1 
ATOM   1614 H HB2  . PRO   A 1 133 ? 21.928  12.856 28.000 1.00 33.33 ? 113 PRO   A HB2  1 
ATOM   1615 H HB3  . PRO   A 1 133 ? 23.050  12.016 27.251 1.00 33.33 ? 113 PRO   A HB3  1 
ATOM   1616 H HG2  . PRO   A 1 133 ? 21.121  12.889 25.904 1.00 34.88 ? 113 PRO   A HG2  1 
ATOM   1617 H HG3  . PRO   A 1 133 ? 21.666  11.429 25.592 1.00 34.88 ? 113 PRO   A HG3  1 
ATOM   1618 H HD2  . PRO   A 1 133 ? 19.328  12.114 26.975 1.00 32.58 ? 113 PRO   A HD2  1 
ATOM   1619 H HD3  . PRO   A 1 133 ? 19.548  10.875 26.003 1.00 32.58 ? 113 PRO   A HD3  1 
ATOM   1620 N N    . GLY   A 1 134 ? 22.634  10.284 30.463 1.00 27.82 ? 114 GLY   A N    1 
ATOM   1621 C CA   . GLY   A 1 134 ? 22.904  10.486 31.877 1.00 28.82 ? 114 GLY   A CA   1 
ATOM   1622 C C    . GLY   A 1 134 ? 21.902  9.856  32.818 1.00 28.59 ? 114 GLY   A C    1 
ATOM   1623 O O    . GLY   A 1 134 ? 21.985  10.090 34.030 1.00 30.19 ? 114 GLY   A O    1 
ATOM   1624 H H    . GLY   A 1 134 ? 23.060  9.621  30.118 1.00 33.39 ? 114 GLY   A H    1 
ATOM   1625 H HA2  . GLY   A 1 134 ? 23.776  10.113 32.082 1.00 34.58 ? 114 GLY   A HA2  1 
ATOM   1626 H HA3  . GLY   A 1 134 ? 22.919  11.439 32.056 1.00 34.58 ? 114 GLY   A HA3  1 
ATOM   1627 N N    . TYR   A 1 135 ? 20.966  9.069  32.312 1.00 25.73 ? 115 TYR   A N    1 
ATOM   1628 C CA   . TYR   A 1 135 ? 20.003  8.358  33.135 1.00 24.58 ? 115 TYR   A CA   1 
ATOM   1629 C C    . TYR   A 1 135 ? 20.098  6.873  32.846 1.00 25.31 ? 115 TYR   A C    1 
ATOM   1630 O O    . TYR   A 1 135 ? 20.533  6.467  31.762 1.00 26.92 ? 115 TYR   A O    1 
ATOM   1631 C CB   . TYR   A 1 135 ? 18.568  8.819  32.849 1.00 23.88 ? 115 TYR   A CB   1 
ATOM   1632 C CG   . TYR   A 1 135 ? 18.268  10.204 33.334 1.00 23.16 ? 115 TYR   A CG   1 
ATOM   1633 C CD1  . TYR   A 1 135 ? 18.529  11.307 32.544 1.00 23.11 ? 115 TYR   A CD1  1 
ATOM   1634 C CD2  . TYR   A 1 135 ? 17.759  10.417 34.607 1.00 23.39 ? 115 TYR   A CD2  1 
ATOM   1635 C CE1  . TYR   A 1 135 ? 18.244  12.574 32.994 1.00 23.71 ? 115 TYR   A CE1  1 
ATOM   1636 C CE2  . TYR   A 1 135 ? 17.507  11.673 35.069 1.00 23.88 ? 115 TYR   A CE2  1 
ATOM   1637 C CZ   . TYR   A 1 135 ? 17.738  12.754 34.258 1.00 23.67 ? 115 TYR   A CZ   1 
ATOM   1638 O OH   . TYR   A 1 135 ? 17.497  14.034 34.697 1.00 26.42 ? 115 TYR   A OH   1 
ATOM   1639 H H    . TYR   A 1 135 ? 20.867  8.927  31.470 1.00 30.88 ? 115 TYR   A H    1 
ATOM   1640 H HA   . TYR   A 1 135 ? 20.195  8.527  34.071 1.00 29.50 ? 115 TYR   A HA   1 
ATOM   1641 H HB2  . TYR   A 1 135 ? 18.421  8.803  31.890 1.00 28.66 ? 115 TYR   A HB2  1 
ATOM   1642 H HB3  . TYR   A 1 135 ? 17.953  8.212  33.289 1.00 28.66 ? 115 TYR   A HB3  1 
ATOM   1643 H HD1  . TYR   A 1 135 ? 18.901  11.190 31.699 1.00 27.73 ? 115 TYR   A HD1  1 
ATOM   1644 H HD2  . TYR   A 1 135 ? 17.585  9.687  35.156 1.00 28.07 ? 115 TYR   A HD2  1 
ATOM   1645 H HE1  . TYR   A 1 135 ? 18.393  13.309 32.443 1.00 28.45 ? 115 TYR   A HE1  1 
ATOM   1646 H HE2  . TYR   A 1 135 ? 17.179  11.797 35.930 1.00 28.66 ? 115 TYR   A HE2  1 
ATOM   1647 H HH   . TYR   A 1 135 ? 17.189  14.016 35.479 1.00 31.71 ? 115 TYR   A HH   1 
ATOM   1648 N N    . PRO   A 1 136 ? 19.695  6.021  33.785 1.00 25.20 ? 116 PRO   A N    1 
ATOM   1649 C CA   . PRO   A 1 136 ? 19.742  4.580  33.509 1.00 25.94 ? 116 PRO   A CA   1 
ATOM   1650 C C    . PRO   A 1 136 ? 18.803  4.228  32.366 1.00 24.48 ? 116 PRO   A C    1 
ATOM   1651 O O    . PRO   A 1 136 ? 17.736  4.810  32.215 1.00 24.71 ? 116 PRO   A O    1 
ATOM   1652 C CB   . PRO   A 1 136 ? 19.307  3.941  34.831 1.00 28.08 ? 116 PRO   A CB   1 
ATOM   1653 C CG   . PRO   A 1 136 ? 19.552  5.018  35.859 1.00 29.63 ? 116 PRO   A CG   1 
ATOM   1654 C CD   . PRO   A 1 136 ? 19.267  6.313  35.162 1.00 27.33 ? 116 PRO   A CD   1 
ATOM   1655 H HA   . PRO   A 1 136 ? 20.644  4.289  33.302 1.00 31.12 ? 116 PRO   A HA   1 
ATOM   1656 H HB2  . PRO   A 1 136 ? 18.367  3.701  34.793 1.00 33.69 ? 116 PRO   A HB2  1 
ATOM   1657 H HB3  . PRO   A 1 136 ? 19.843  3.154  35.014 1.00 33.69 ? 116 PRO   A HB3  1 
ATOM   1658 H HG2  . PRO   A 1 136 ? 18.955  4.894  36.613 1.00 35.56 ? 116 PRO   A HG2  1 
ATOM   1659 H HG3  . PRO   A 1 136 ? 20.475  4.983  36.157 1.00 35.56 ? 116 PRO   A HG3  1 
ATOM   1660 H HD2  . PRO   A 1 136 ? 18.322  6.529  35.197 1.00 32.80 ? 116 PRO   A HD2  1 
ATOM   1661 H HD3  . PRO   A 1 136 ? 19.787  7.038  35.544 1.00 32.80 ? 116 PRO   A HD3  1 
ATOM   1662 N N    A ARG   A 1 137 ? 19.220  3.273  31.545 0.51 25.86 ? 117 ARG   A N    1 
ATOM   1663 N N    B ARG   A 1 137 ? 19.213  3.264  31.553 0.49 24.72 ? 117 ARG   A N    1 
ATOM   1664 C CA   A ARG   A 1 137 ? 18.326  2.753  30.524 0.51 27.74 ? 117 ARG   A CA   1 
ATOM   1665 C CA   B ARG   A 1 137 ? 18.331  2.730  30.524 0.49 26.23 ? 117 ARG   A CA   1 
ATOM   1666 C C    A ARG   A 1 137 ? 17.065  2.226  31.195 0.51 27.69 ? 117 ARG   A C    1 
ATOM   1667 C C    B ARG   A 1 137 ? 17.067  2.185  31.172 0.49 26.95 ? 117 ARG   A C    1 
ATOM   1668 O O    A ARG   A 1 137 ? 17.118  1.593  32.255 0.51 29.17 ? 117 ARG   A O    1 
ATOM   1669 O O    B ARG   A 1 137 ? 17.122  1.492  32.194 0.49 28.62 ? 117 ARG   A O    1 
ATOM   1670 C CB   A ARG   A 1 137 ? 19.004  1.628  29.747 0.51 32.01 ? 117 ARG   A CB   1 
ATOM   1671 C CB   B ARG   A 1 137 ? 19.057  1.620  29.768 0.49 29.48 ? 117 ARG   A CB   1 
ATOM   1672 C CG   A ARG   A 1 137 ? 18.249  1.255  28.482 0.51 34.74 ? 117 ARG   A CG   1 
ATOM   1673 C CG   B ARG   A 1 137 ? 20.220  2.115  28.933 0.49 30.74 ? 117 ARG   A CG   1 
ATOM   1674 C CD   A ARG   A 1 137 ? 18.663  -0.096 27.929 0.51 37.56 ? 117 ARG   A CD   1 
ATOM   1675 C CD   B ARG   A 1 137 ? 21.095  0.974  28.423 0.49 35.47 ? 117 ARG   A CD   1 
ATOM   1676 N NE   A ARG   A 1 137 ? 17.944  -0.391 26.695 0.51 39.11 ? 117 ARG   A NE   1 
ATOM   1677 N NE   B ARG   A 1 137 ? 22.041  1.435  27.414 0.49 37.54 ? 117 ARG   A NE   1 
ATOM   1678 C CZ   A ARG   A 1 137 ? 18.363  -0.059 25.480 0.51 40.08 ? 117 ARG   A CZ   1 
ATOM   1679 C CZ   B ARG   A 1 137 ? 21.861  1.322  26.102 0.49 38.72 ? 117 ARG   A CZ   1 
ATOM   1680 N NH1  A ARG   A 1 137 ? 19.514  0.564  25.290 0.51 41.82 ? 117 ARG   A NH1  1 
ATOM   1681 N NH1  B ARG   A 1 137 ? 20.762  0.787  25.596 0.49 38.76 ? 117 ARG   A NH1  1 
ATOM   1682 N NH2  A ARG   A 1 137 ? 17.608  -0.363 24.428 0.51 39.52 ? 117 ARG   A NH2  1 
ATOM   1683 N NH2  B ARG   A 1 137 ? 22.811  1.753  25.279 0.49 38.94 ? 117 ARG   A NH2  1 
ATOM   1684 H H    A ARG   A 1 137 ? 20.002  2.916  31.558 0.51 31.03 ? 117 ARG   A H    1 
ATOM   1685 H H    B ARG   A 1 137 ? 19.993  2.903  31.575 0.49 29.66 ? 117 ARG   A H    1 
ATOM   1686 H HA   A ARG   A 1 137 ? 18.095  3.453  29.894 0.51 33.29 ? 117 ARG   A HA   1 
ATOM   1687 H HA   B ARG   A 1 137 ? 18.084  3.425  29.894 0.49 31.48 ? 117 ARG   A HA   1 
ATOM   1688 H HB2  A ARG   A 1 137 ? 19.896  1.912  29.492 0.51 38.41 ? 117 ARG   A HB2  1 
ATOM   1689 H HB2  B ARG   A 1 137 ? 19.403  0.980  30.410 0.49 35.38 ? 117 ARG   A HB2  1 
ATOM   1690 H HB3  A ARG   A 1 137 ? 19.055  0.840  30.310 0.51 38.41 ? 117 ARG   A HB3  1 
ATOM   1691 H HB3  B ARG   A 1 137 ? 18.428  1.184  29.172 0.49 35.38 ? 117 ARG   A HB3  1 
ATOM   1692 H HG2  A ARG   A 1 137 ? 17.300  1.220  28.678 0.51 41.69 ? 117 ARG   A HG2  1 
ATOM   1693 H HG2  B ARG   A 1 137 ? 19.877  2.598  28.165 0.49 36.89 ? 117 ARG   A HG2  1 
ATOM   1694 H HG3  A ARG   A 1 137 ? 18.423  1.923  27.801 0.51 41.69 ? 117 ARG   A HG3  1 
ATOM   1695 H HG3  B ARG   A 1 137 ? 20.773  2.700  29.474 0.49 36.89 ? 117 ARG   A HG3  1 
ATOM   1696 H HD2  A ARG   A 1 137 ? 19.614  -0.090 27.738 0.51 45.07 ? 117 ARG   A HD2  1 
ATOM   1697 H HD2  B ARG   A 1 137 ? 21.598  0.599  29.163 0.49 42.57 ? 117 ARG   A HD2  1 
ATOM   1698 H HD3  A ARG   A 1 137 ? 18.459  -0.787 28.578 0.51 45.07 ? 117 ARG   A HD3  1 
ATOM   1699 H HD3  B ARG   A 1 137 ? 20.533  0.291  28.024 0.49 42.57 ? 117 ARG   A HD3  1 
ATOM   1700 H HE   A ARG   A 1 137 ? 17.196  -0.810 26.758 0.51 46.93 ? 117 ARG   A HE   1 
ATOM   1701 H HE   B ARG   A 1 137 ? 22.767  1.807  27.686 0.49 45.05 ? 117 ARG   A HE   1 
ATOM   1702 H HH11 A ARG   A 1 137 ? 20.011  0.763  25.963 0.51 50.19 ? 117 ARG   A HH11 1 
ATOM   1703 H HH11 B ARG   A 1 137 ? 20.142  0.502  26.119 0.49 46.52 ? 117 ARG   A HH11 1 
ATOM   1704 H HH12 A ARG   A 1 137 ? 19.766  0.769  24.494 0.51 50.19 ? 117 ARG   A HH12 1 
ATOM   1705 H HH12 B ARG   A 1 137 ? 20.668  0.725  24.743 0.49 46.52 ? 117 ARG   A HH12 1 
ATOM   1706 H HH21 A ARG   A 1 137 ? 16.859  -0.770 24.539 0.51 47.42 ? 117 ARG   A HH21 1 
ATOM   1707 H HH21 B ARG   A 1 137 ? 23.531  2.100  25.597 0.49 46.73 ? 117 ARG   A HH21 1 
ATOM   1708 H HH22 A ARG   A 1 137 ? 17.870  -0.153 23.636 0.51 47.42 ? 117 ARG   A HH22 1 
ATOM   1709 H HH22 B ARG   A 1 137 ? 22.706  1.685  24.428 0.49 46.73 ? 117 ARG   A HH22 1 
ATOM   1710 N N    . GLY   A 1 138 ? 15.927  2.512  30.590 1.00 26.37 ? 118 GLY   A N    1 
ATOM   1711 C CA   . GLY   A 1 138 ? 14.687  2.026  31.124 1.00 27.26 ? 118 GLY   A CA   1 
ATOM   1712 C C    . GLY   A 1 138 ? 13.660  1.755  30.060 1.00 25.58 ? 118 GLY   A C    1 
ATOM   1713 O O    . GLY   A 1 138 ? 13.967  1.653  28.868 1.00 25.69 ? 118 GLY   A O    1 
ATOM   1714 H H    A GLY   A 1 138 ? 15.854  2.982  29.874 0.51 31.65 ? 118 GLY   A H    1 
ATOM   1715 H H    B GLY   A 1 138 ? 15.854  3.008  29.892 0.49 31.65 ? 118 GLY   A H    1 
ATOM   1716 H HA2  . GLY   A 1 138 ? 14.848  1.202  31.608 1.00 32.71 ? 118 GLY   A HA2  1 
ATOM   1717 H HA3  . GLY   A 1 138 ? 14.323  2.686  31.736 1.00 32.71 ? 118 GLY   A HA3  1 
ATOM   1718 N N    A GLN   A 1 139 ? 12.419  1.620  30.494 0.59 23.96 ? 119 GLN   A N    1 
ATOM   1719 N N    B GLN   A 1 139 ? 12.418  1.619  30.502 0.41 25.07 ? 119 GLN   A N    1 
ATOM   1720 C CA   A GLN   A 1 139 ? 11.280  1.425  29.610 0.59 22.70 ? 119 GLN   A CA   1 
ATOM   1721 C CA   B GLN   A 1 139 ? 11.268  1.414  29.636 0.41 24.45 ? 119 GLN   A CA   1 
ATOM   1722 C C    A GLN   A 1 139 ? 10.292  2.534  29.915 0.59 22.66 ? 119 GLN   A C    1 
ATOM   1723 C C    B GLN   A 1 139 ? 10.293  2.542  29.925 0.41 23.54 ? 119 GLN   A C    1 
ATOM   1724 O O    A GLN   A 1 139 ? 10.025  2.822  31.085 0.59 25.21 ? 119 GLN   A O    1 
ATOM   1725 O O    B GLN   A 1 139 ? 10.026  2.847  31.092 0.41 25.68 ? 119 GLN   A O    1 
ATOM   1726 C CB   A GLN   A 1 139 ? 10.658  0.048  29.843 0.59 25.59 ? 119 GLN   A CB   1 
ATOM   1727 C CB   B GLN   A 1 139 ? 10.627  0.058  29.932 0.41 27.00 ? 119 GLN   A CB   1 
ATOM   1728 C CG   A GLN   A 1 139 ? 11.646  -1.108 29.581 0.59 28.75 ? 119 GLN   A CG   1 
ATOM   1729 C CG   B GLN   A 1 139 ? 9.459   -0.296 29.047 0.41 29.19 ? 119 GLN   A CG   1 
ATOM   1730 C CD   A GLN   A 1 139 ? 11.890  -1.359 28.104 0.59 35.49 ? 119 GLN   A CD   1 
ATOM   1731 C CD   B GLN   A 1 139 ? 9.822   -0.459 27.582 0.41 31.96 ? 119 GLN   A CD   1 
ATOM   1732 O OE1  A GLN   A 1 139 ? 11.007  -1.177 27.264 0.59 37.23 ? 119 GLN   A OE1  1 
ATOM   1733 O OE1  B GLN   A 1 139 ? 10.975  -0.713 27.217 0.41 33.92 ? 119 GLN   A OE1  1 
ATOM   1734 N NE2  A GLN   A 1 139 ? 13.096  -1.799 27.785 0.59 39.15 ? 119 GLN   A NE2  1 
ATOM   1735 N NE2  B GLN   A 1 139 ? 8.825   -0.313 26.735 0.41 30.43 ? 119 GLN   A NE2  1 
ATOM   1736 H H    A GLN   A 1 139 ? 12.202  1.638  31.326 0.59 28.75 ? 119 GLN   A H    1 
ATOM   1737 H H    B GLN   A 1 139 ? 12.209  1.644  31.336 0.41 30.09 ? 119 GLN   A H    1 
ATOM   1738 H HA   A GLN   A 1 139 ? 11.534  1.474  28.675 0.59 27.25 ? 119 GLN   A HA   1 
ATOM   1739 H HA   B GLN   A 1 139 ? 11.513  1.433  28.698 0.41 29.34 ? 119 GLN   A HA   1 
ATOM   1740 H HB2  A GLN   A 1 139 ? 10.364  -0.012 30.766 0.59 30.71 ? 119 GLN   A HB2  1 
ATOM   1741 H HB2  B GLN   A 1 139 ? 11.300  -0.631 29.818 0.41 32.40 ? 119 GLN   A HB2  1 
ATOM   1742 H HB3  A GLN   A 1 139 ? 9.902   -0.061 29.246 0.59 30.71 ? 119 GLN   A HB3  1 
ATOM   1743 H HB3  B GLN   A 1 139 ? 10.309  0.062  30.848 0.41 32.40 ? 119 GLN   A HB3  1 
ATOM   1744 H HG2  A GLN   A 1 139 ? 12.497  -0.894 29.992 0.59 34.50 ? 119 GLN   A HG2  1 
ATOM   1745 H HG2  B GLN   A 1 139 ? 9.080   -1.135 29.352 0.41 35.03 ? 119 GLN   A HG2  1 
ATOM   1746 H HG3  A GLN   A 1 139 ? 11.286  -1.923 29.966 0.59 34.50 ? 119 GLN   A HG3  1 
ATOM   1747 H HG3  B GLN   A 1 139 ? 8.796   0.410  29.109 0.41 35.03 ? 119 GLN   A HG3  1 
ATOM   1748 H HE21 A GLN   A 1 139 ? 13.684  -1.926 28.400 0.59 46.98 ? 119 GLN   A HE21 1 
ATOM   1749 H HE21 B GLN   A 1 139 ? 8.035   -0.137 27.026 0.41 36.51 ? 119 GLN   A HE21 1 
ATOM   1750 H HE22 A GLN   A 1 139 ? 13.292  -1.959 26.963 0.59 46.98 ? 119 GLN   A HE22 1 
ATOM   1751 H HE22 B GLN   A 1 139 ? 8.963   -0.393 25.890 0.41 36.51 ? 119 GLN   A HE22 1 
ATOM   1752 N N    . TYR   A 1 140 ? 9.786   3.172  28.868 1.00 20.45 ? 120 TYR   A N    1 
ATOM   1753 C CA   . TYR   A 1 140 ? 8.848   4.282  28.977 1.00 18.86 ? 120 TYR   A CA   1 
ATOM   1754 C C    . TYR   A 1 140 ? 7.556   3.913  28.265 1.00 18.39 ? 120 TYR   A C    1 
ATOM   1755 O O    . TYR   A 1 140 ? 7.575   3.461  27.119 1.00 20.65 ? 120 TYR   A O    1 
ATOM   1756 C CB   . TYR   A 1 140 ? 9.473   5.524  28.341 1.00 18.43 ? 120 TYR   A CB   1 
ATOM   1757 C CG   . TYR   A 1 140 ? 8.605   6.754  28.291 1.00 18.16 ? 120 TYR   A CG   1 
ATOM   1758 C CD1  . TYR   A 1 140 ? 7.758   7.091  29.336 1.00 17.51 ? 120 TYR   A CD1  1 
ATOM   1759 C CD2  . TYR   A 1 140 ? 8.661   7.613  27.207 1.00 18.63 ? 120 TYR   A CD2  1 
ATOM   1760 C CE1  . TYR   A 1 140 ? 6.968   8.238  29.275 1.00 17.78 ? 120 TYR   A CE1  1 
ATOM   1761 C CE2  . TYR   A 1 140 ? 7.905   8.759  27.144 1.00 19.07 ? 120 TYR   A CE2  1 
ATOM   1762 C CZ   . TYR   A 1 140 ? 7.049   9.059  28.172 1.00 18.44 ? 120 TYR   A CZ   1 
ATOM   1763 O OH   . TYR   A 1 140 ? 6.268   10.194 28.131 1.00 19.66 ? 120 TYR   A OH   1 
ATOM   1764 H H    A TYR   A 1 140 ? 9.977   2.972  28.054 0.59 24.54 ? 120 TYR   A H    1 
ATOM   1765 H H    B TYR   A 1 140 ? 9.977   2.966  28.055 0.41 24.54 ? 120 TYR   A H    1 
ATOM   1766 H HA   . TYR   A 1 140 ? 8.631   4.466  29.905 1.00 22.63 ? 120 TYR   A HA   1 
ATOM   1767 H HB2  . TYR   A 1 140 ? 10.268  5.756  28.847 1.00 22.12 ? 120 TYR   A HB2  1 
ATOM   1768 H HB3  . TYR   A 1 140 ? 9.714   5.307  27.427 1.00 22.12 ? 120 TYR   A HB3  1 
ATOM   1769 H HD1  . TYR   A 1 140 ? 7.717   6.545  30.087 1.00 21.02 ? 120 TYR   A HD1  1 
ATOM   1770 H HD2  . TYR   A 1 140 ? 9.229   7.409  26.499 1.00 22.36 ? 120 TYR   A HD2  1 
ATOM   1771 H HE1  . TYR   A 1 140 ? 6.390   8.446  29.973 1.00 21.34 ? 120 TYR   A HE1  1 
ATOM   1772 H HE2  . TYR   A 1 140 ? 7.973   9.326  26.409 1.00 22.89 ? 120 TYR   A HE2  1 
ATOM   1773 H HH   . TYR   A 1 140 ? 6.425   10.625 27.427 1.00 23.59 ? 120 TYR   A HH   1 
ATOM   1774 N N    A ARG   A 1 141 ? 6.441   4.070  28.963 0.47 18.49 ? 121 ARG   A N    1 
ATOM   1775 N N    B ARG   A 1 141 ? 6.436   4.086  28.966 0.53 18.70 ? 121 ARG   A N    1 
ATOM   1776 C CA   A ARG   A 1 141 ? 5.110   3.895  28.410 0.47 18.84 ? 121 ARG   A CA   1 
ATOM   1777 C CA   B ARG   A 1 141 ? 5.099   3.881  28.430 0.53 19.02 ? 121 ARG   A CA   1 
ATOM   1778 C C    A ARG   A 1 141 ? 4.288   5.104  28.827 0.47 18.05 ? 121 ARG   A C    1 
ATOM   1779 C C    B ARG   A 1 141 ? 4.240   5.066  28.847 0.53 18.20 ? 121 ARG   A C    1 
ATOM   1780 O O    A ARG   A 1 141 ? 4.421   5.590  29.954 0.47 19.15 ? 121 ARG   A O    1 
ATOM   1781 O O    B ARG   A 1 141 ? 4.259   5.462  30.016 0.53 19.84 ? 121 ARG   A O    1 
ATOM   1782 C CB   A ARG   A 1 141 ? 4.458   2.631  28.989 0.47 22.53 ? 121 ARG   A CB   1 
ATOM   1783 C CB   B ARG   A 1 141 ? 4.466   2.627  29.045 0.53 22.73 ? 121 ARG   A CB   1 
ATOM   1784 C CG   A ARG   A 1 141 ? 5.148   1.320  28.656 0.47 26.72 ? 121 ARG   A CG   1 
ATOM   1785 C CG   B ARG   A 1 141 ? 5.050   1.290  28.629 0.53 27.79 ? 121 ARG   A CG   1 
ATOM   1786 C CD   A ARG   A 1 141 ? 4.603   0.163  29.499 0.47 30.40 ? 121 ARG   A CD   1 
ATOM   1787 C CD   B ARG   A 1 141 ? 4.191   0.107  29.125 0.53 32.58 ? 121 ARG   A CD   1 
ATOM   1788 N NE   A ARG   A 1 141 ? 5.114   0.232  30.861 0.47 34.72 ? 121 ARG   A NE   1 
ATOM   1789 N NE   B ARG   A 1 141 ? 2.769   0.329  28.876 0.53 35.76 ? 121 ARG   A NE   1 
ATOM   1790 C CZ   A ARG   A 1 141 ? 6.274   -0.278 31.251 0.47 38.79 ? 121 ARG   A CZ   1 
ATOM   1791 C CZ   B ARG   A 1 141 ? 1.800   -0.533 29.153 0.53 38.10 ? 121 ARG   A CZ   1 
ATOM   1792 N NH1  A ARG   A 1 141 ? 7.051   -0.948 30.416 0.47 39.57 ? 121 ARG   A NH1  1 
ATOM   1793 N NH1  B ARG   A 1 141 ? 2.059   -1.746 29.606 0.53 38.15 ? 121 ARG   A NH1  1 
ATOM   1794 N NH2  A ARG   A 1 141 ? 6.665   -0.108 32.509 0.47 41.26 ? 121 ARG   A NH2  1 
ATOM   1795 N NH2  B ARG   A 1 141 ? 0.537   -0.175 28.940 0.53 36.87 ? 121 ARG   A NH2  1 
ATOM   1796 H H    A ARG   A 1 141 ? 6.431   4.288  29.795 0.47 22.19 ? 121 ARG   A H    1 
ATOM   1797 H H    B ARG   A 1 141 ? 6.429   4.333  29.790 0.53 22.44 ? 121 ARG   A H    1 
ATOM   1798 H HA   A ARG   A 1 141 ? 5.136   3.822  27.443 0.47 22.61 ? 121 ARG   A HA   1 
ATOM   1799 H HA   B ARG   A 1 141 ? 5.139   3.804  27.464 0.53 22.82 ? 121 ARG   A HA   1 
ATOM   1800 H HB2  A ARG   A 1 141 ? 4.445   2.712  29.956 0.47 27.04 ? 121 ARG   A HB2  1 
ATOM   1801 H HB2  B ARG   A 1 141 ? 4.556   2.687  30.009 0.53 27.28 ? 121 ARG   A HB2  1 
ATOM   1802 H HB3  A ARG   A 1 141 ? 3.551   2.574  28.649 0.47 27.04 ? 121 ARG   A HB3  1 
ATOM   1803 H HB3  B ARG   A 1 141 ? 3.527   2.614  28.800 0.53 27.28 ? 121 ARG   A HB3  1 
ATOM   1804 H HG2  A ARG   A 1 141 ? 5.001   1.109  27.721 0.47 32.06 ? 121 ARG   A HG2  1 
ATOM   1805 H HG2  B ARG   A 1 141 ? 5.094   1.247  27.661 0.53 33.35 ? 121 ARG   A HG2  1 
ATOM   1806 H HG3  A ARG   A 1 141 ? 6.098   1.403  28.832 0.47 32.06 ? 121 ARG   A HG3  1 
ATOM   1807 H HG3  B ARG   A 1 141 ? 5.939   1.198  29.006 0.53 33.35 ? 121 ARG   A HG3  1 
ATOM   1808 H HD2  A ARG   A 1 141 ? 3.635   0.213  29.531 0.47 36.48 ? 121 ARG   A HD2  1 
ATOM   1809 H HD2  B ARG   A 1 141 ? 4.459   -0.700 28.660 0.53 39.09 ? 121 ARG   A HD2  1 
ATOM   1810 H HD3  A ARG   A 1 141 ? 4.879   -0.681 29.109 0.47 36.48 ? 121 ARG   A HD3  1 
ATOM   1811 H HD3  B ARG   A 1 141 ? 4.319   -0.002 30.080 0.53 39.09 ? 121 ARG   A HD3  1 
ATOM   1812 H HE   A ARG   A 1 141 ? 4.632   0.630  31.452 0.47 41.66 ? 121 ARG   A HE   1 
ATOM   1813 H HE   B ARG   A 1 141 ? 2.543   1.078  28.521 0.53 42.91 ? 121 ARG   A HE   1 
ATOM   1814 H HH11 A ARG   A 1 141 ? 6.808   -1.060 29.599 0.47 47.49 ? 121 ARG   A HH11 1 
ATOM   1815 H HH11 B ARG   A 1 141 ? 2.873   -1.994 29.729 0.53 45.78 ? 121 ARG   A HH11 1 
ATOM   1816 H HH12 A ARG   A 1 141 ? 7.800   -1.271 30.690 0.47 47.49 ? 121 ARG   A HH12 1 
ATOM   1817 H HH12 B ARG   A 1 141 ? 1.414   -2.287 29.779 0.53 45.78 ? 121 ARG   A HH12 1 
ATOM   1818 H HH21 A ARG   A 1 141 ? 6.168   0.328  33.058 0.47 49.51 ? 121 ARG   A HH21 1 
ATOM   1819 H HH21 B ARG   A 1 141 ? 0.359   0.606  28.627 0.53 44.25 ? 121 ARG   A HH21 1 
ATOM   1820 H HH22 A ARG   A 1 141 ? 7.415   -0.434 32.774 0.47 49.51 ? 121 ARG   A HH22 1 
ATOM   1821 H HH22 B ARG   A 1 141 ? -0.101  -0.724 29.115 0.53 44.25 ? 121 ARG   A HH22 1 
ATOM   1822 N N    . ASN   A 1 142 ? 3.456   5.613  27.926 1.00 17.61 ? 122 ASN   A N    1 
ATOM   1823 C CA   . ASN   A 1 142 ? 2.603   6.736  28.306 1.00 16.89 ? 122 ASN   A CA   1 
ATOM   1824 C C    . ASN   A 1 142 ? 1.408   6.823  27.388 1.00 16.79 ? 122 ASN   A C    1 
ATOM   1825 O O    . ASN   A 1 142 ? 1.384   6.220  26.320 1.00 17.32 ? 122 ASN   A O    1 
ATOM   1826 C CB   . ASN   A 1 142 ? 3.360   8.078  28.290 1.00 17.75 ? 122 ASN   A CB   1 
ATOM   1827 C CG   . ASN   A 1 142 ? 2.917   9.021  29.378 1.00 18.91 ? 122 ASN   A CG   1 
ATOM   1828 O OD1  . ASN   A 1 142 ? 1.883   8.822  30.029 1.00 19.75 ? 122 ASN   A OD1  1 
ATOM   1829 N ND2  . ASN   A 1 142 ? 3.716   10.064 29.606 1.00 19.08 ? 122 ASN   A ND2  1 
ATOM   1830 H H    A ASN   A 1 142 ? 3.369   5.337  27.116 0.47 21.13 ? 122 ASN   A H    1 
ATOM   1831 H H    B ASN   A 1 142 ? 3.401   5.363  27.105 0.53 21.13 ? 122 ASN   A H    1 
ATOM   1832 H HA   . ASN   A 1 142 ? 2.284   6.566  29.206 1.00 20.27 ? 122 ASN   A HA   1 
ATOM   1833 H HB2  . ASN   A 1 142 ? 4.307   7.907  28.411 1.00 21.31 ? 122 ASN   A HB2  1 
ATOM   1834 H HB3  . ASN   A 1 142 ? 3.208   8.514  27.437 1.00 21.31 ? 122 ASN   A HB3  1 
ATOM   1835 H HD21 . ASN   A 1 142 ? 3.513   10.636 30.215 1.00 22.89 ? 122 ASN   A HD21 1 
ATOM   1836 H HD22 . ASN   A 1 142 ? 4.433   10.165 29.143 1.00 22.89 ? 122 ASN   A HD22 1 
ATOM   1837 N N    . HIS   A 1 143 ? 0.418   7.585  27.840 1.00 16.84 ? 123 HIS   A N    1 
ATOM   1838 C CA   . HIS   A 1 143 ? -0.726  7.981  27.031 1.00 16.34 ? 123 HIS   A CA   1 
ATOM   1839 C C    . HIS   A 1 143 ? -0.427  9.334  26.396 1.00 16.12 ? 123 HIS   A C    1 
ATOM   1840 O O    . HIS   A 1 143 ? 0.172   10.198 27.030 1.00 17.38 ? 123 HIS   A O    1 
ATOM   1841 C CB   . HIS   A 1 143 ? -1.942  8.059  27.955 1.00 16.64 ? 123 HIS   A CB   1 
ATOM   1842 C CG   . HIS   A 1 143 ? -3.189  8.497  27.277 1.00 17.72 ? 123 HIS   A CG   1 
ATOM   1843 N ND1  . HIS   A 1 143 ? -3.559  9.823  27.218 1.00 18.96 ? 123 HIS   A ND1  1 
ATOM   1844 C CD2  . HIS   A 1 143 ? -4.163  7.799  26.651 1.00 20.40 ? 123 HIS   A CD2  1 
ATOM   1845 C CE1  . HIS   A 1 143 ? -4.708  9.919  26.574 1.00 19.82 ? 123 HIS   A CE1  1 
ATOM   1846 N NE2  . HIS   A 1 143 ? -5.089  8.708  26.220 1.00 19.89 ? 123 HIS   A NE2  1 
ATOM   1847 H H    . HIS   A 1 143 ? 0.386   7.897  28.641 1.00 20.20 ? 123 HIS   A H    1 
ATOM   1848 H HA   . HIS   A 1 143 ? -0.916  7.356  26.314 1.00 19.61 ? 123 HIS   A HA   1 
ATOM   1849 H HB2  . HIS   A 1 143 ? -2.103  7.179  28.330 1.00 19.97 ? 123 HIS   A HB2  1 
ATOM   1850 H HB3  . HIS   A 1 143 ? -1.753  8.693  28.664 1.00 19.97 ? 123 HIS   A HB3  1 
ATOM   1851 H HD1  . HIS   A 1 143 ? -3.114  10.482 27.547 1.00 22.76 ? 123 HIS   A HD1  1 
ATOM   1852 H HD2  . HIS   A 1 143 ? -4.197  6.877  26.536 1.00 24.48 ? 123 HIS   A HD2  1 
ATOM   1853 H HE1  . HIS   A 1 143 ? -5.170  10.707 26.400 1.00 23.79 ? 123 HIS   A HE1  1 
ATOM   1854 H HE2  . HIS   A 1 143 ? -5.807  8.519  25.786 1.00 23.87 ? 123 HIS   A HE2  1 
ATOM   1855 N N    . PHE   A 1 144 ? -0.843  9.514  25.139 1.00 15.28 ? 124 PHE   A N    1 
ATOM   1856 C CA   . PHE   A 1 144 ? -0.568  10.739 24.415 1.00 14.96 ? 124 PHE   A CA   1 
ATOM   1857 C C    . PHE   A 1 144 ? -1.804  11.232 23.690 1.00 15.64 ? 124 PHE   A C    1 
ATOM   1858 O O    . PHE   A 1 144 ? -2.644  10.454 23.213 1.00 16.81 ? 124 PHE   A O    1 
ATOM   1859 C CB   . PHE   A 1 144 ? 0.512   10.504 23.345 1.00 16.14 ? 124 PHE   A CB   1 
ATOM   1860 C CG   . PHE   A 1 144 ? 1.870   10.176 23.902 1.00 16.29 ? 124 PHE   A CG   1 
ATOM   1861 C CD1  . PHE   A 1 144 ? 2.172   8.893  24.319 1.00 17.96 ? 124 PHE   A CD1  1 
ATOM   1862 C CD2  . PHE   A 1 144 ? 2.838   11.143 24.000 1.00 17.59 ? 124 PHE   A CD2  1 
ATOM   1863 C CE1  . PHE   A 1 144 ? 3.446   8.600  24.815 1.00 19.83 ? 124 PHE   A CE1  1 
ATOM   1864 C CE2  . PHE   A 1 144 ? 4.106   10.856 24.485 1.00 19.14 ? 124 PHE   A CE2  1 
ATOM   1865 C CZ   . PHE   A 1 144 ? 4.403   9.587  24.889 1.00 19.83 ? 124 PHE   A CZ   1 
ATOM   1866 H H    . PHE   A 1 144 ? -1.288  8.932  24.688 1.00 18.34 ? 124 PHE   A H    1 
ATOM   1867 H HA   . PHE   A 1 144 ? -0.289  11.413 25.055 1.00 17.96 ? 124 PHE   A HA   1 
ATOM   1868 H HB2  . PHE   A 1 144 ? 0.237   9.763  22.784 1.00 19.37 ? 124 PHE   A HB2  1 
ATOM   1869 H HB3  . PHE   A 1 144 ? 0.600   11.309 22.811 1.00 19.37 ? 124 PHE   A HB3  1 
ATOM   1870 H HD1  . PHE   A 1 144 ? 1.527   8.224  24.270 1.00 21.55 ? 124 PHE   A HD1  1 
ATOM   1871 H HD2  . PHE   A 1 144 ? 2.640   12.012 23.734 1.00 21.12 ? 124 PHE   A HD2  1 
ATOM   1872 H HE1  . PHE   A 1 144 ? 3.648   7.736  25.095 1.00 23.80 ? 124 PHE   A HE1  1 
ATOM   1873 H HE2  . PHE   A 1 144 ? 4.751   11.525 24.535 1.00 22.97 ? 124 PHE   A HE2  1 
ATOM   1874 H HZ   . PHE   A 1 144 ? 5.252   9.389  25.214 1.00 23.80 ? 124 PHE   A HZ   1 
ATOM   1875 N N    . LEU   A 1 145 ? -1.867  12.552 23.554 1.00 14.99 ? 125 LEU   A N    1 
ATOM   1876 C CA   . LEU   A 1 145 ? -2.731  13.196 22.574 1.00 14.52 ? 125 LEU   A CA   1 
ATOM   1877 C C    . LEU   A 1 145 ? -1.839  13.979 21.618 1.00 15.18 ? 125 LEU   A C    1 
ATOM   1878 O O    . LEU   A 1 145 ? -0.890  14.634 22.044 1.00 16.93 ? 125 LEU   A O    1 
ATOM   1879 C CB   . LEU   A 1 145 ? -3.706  14.142 23.284 1.00 16.67 ? 125 LEU   A CB   1 
ATOM   1880 C CG   . LEU   A 1 145 ? -4.575  13.430 24.354 1.00 19.65 ? 125 LEU   A CG   1 
ATOM   1881 C CD1  . LEU   A 1 145 ? -5.292  14.428 25.211 0.85 20.39 ? 125 LEU   A CD1  1 
ATOM   1882 C CD2  . LEU   A 1 145 ? -5.502  12.485 23.770 1.00 21.36 ? 125 LEU   A CD2  1 
ATOM   1883 H H    . LEU   A 1 145 ? -1.409  13.105 24.028 1.00 18.00 ? 125 LEU   A H    1 
ATOM   1884 H HA   . LEU   A 1 145 ? -3.248  12.550 22.067 1.00 17.43 ? 125 LEU   A HA   1 
ATOM   1885 H HB2  . LEU   A 1 145 ? -3.199  14.841 23.726 1.00 20.00 ? 125 LEU   A HB2  1 
ATOM   1886 H HB3  . LEU   A 1 145 ? -4.301  14.532 22.625 1.00 20.00 ? 125 LEU   A HB3  1 
ATOM   1887 H HG   . LEU   A 1 145 ? -3.980  12.918 24.923 1.00 23.58 ? 125 LEU   A HG   1 
ATOM   1888 H HD11 . LEU   A 1 145 ? -5.843  13.954 25.853 0.85 24.46 ? 125 LEU   A HD11 1 
ATOM   1889 H HD12 . LEU   A 1 145 ? -4.638  14.974 25.674 0.85 24.46 ? 125 LEU   A HD12 1 
ATOM   1890 H HD13 . LEU   A 1 145 ? -5.849  14.986 24.646 0.85 24.46 ? 125 LEU   A HD13 1 
ATOM   1891 H HD21 . LEU   A 1 145 ? -6.076  12.133 24.468 1.00 25.63 ? 125 LEU   A HD21 1 
ATOM   1892 H HD22 . LEU   A 1 145 ? -6.036  12.939 23.100 1.00 25.63 ? 125 LEU   A HD22 1 
ATOM   1893 H HD23 . LEU   A 1 145 ? -5.000  11.763 23.359 1.00 25.63 ? 125 LEU   A HD23 1 
ATOM   1894 N N    . HIS   A 1 146 ? -2.171  13.934 20.339 1.00 14.98 ? 126 HIS   A N    1 
ATOM   1895 C CA   . HIS   A 1 146 ? -1.462  14.700 19.343 1.00 15.10 ? 126 HIS   A CA   1 
ATOM   1896 C C    . HIS   A 1 146 ? -2.431  15.612 18.613 1.00 15.32 ? 126 HIS   A C    1 
ATOM   1897 O O    . HIS   A 1 146 ? -3.566  15.232 18.314 1.00 16.29 ? 126 HIS   A O    1 
ATOM   1898 C CB   . HIS   A 1 146 ? -0.830  13.826 18.251 1.00 15.91 ? 126 HIS   A CB   1 
ATOM   1899 C CG   . HIS   A 1 146 ? 0.281   12.950 18.713 1.00 17.85 ? 126 HIS   A CG   1 
ATOM   1900 N ND1  . HIS   A 1 146 ? 1.593   13.204 18.362 1.00 20.10 ? 126 HIS   A ND1  1 
ATOM   1901 C CD2  . HIS   A 1 146 ? 0.285   11.777 19.383 1.00 18.92 ? 126 HIS   A CD2  1 
ATOM   1902 C CE1  . HIS   A 1 146 ? 2.365   12.255 18.856 1.00 20.15 ? 126 HIS   A CE1  1 
ATOM   1903 N NE2  . HIS   A 1 146 ? 1.595   11.380 19.485 1.00 18.86 ? 126 HIS   A NE2  1 
ATOM   1904 H H    . HIS   A 1 146 ? -2.815  13.459 20.023 1.00 17.98 ? 126 HIS   A H    1 
ATOM   1905 H HA   . HIS   A 1 146 ? -0.774  15.198 19.811 1.00 18.12 ? 126 HIS   A HA   1 
ATOM   1906 H HB2  . HIS   A 1 146 ? -1.518  13.252 17.880 1.00 19.10 ? 126 HIS   A HB2  1 
ATOM   1907 H HB3  . HIS   A 1 146 ? -0.474  14.407 17.560 1.00 19.10 ? 126 HIS   A HB3  1 
ATOM   1908 H HD2  . HIS   A 1 146 ? -0.458  11.324 19.713 1.00 22.70 ? 126 HIS   A HD2  1 
ATOM   1909 H HE1  . HIS   A 1 146 ? 3.290   12.209 18.777 1.00 24.18 ? 126 HIS   A HE1  1 
ATOM   1910 H HE2  . HIS   A 1 146 ? 1.873   10.675 19.892 1.00 22.63 ? 126 HIS   A HE2  1 
ATOM   1911 N N    . SER   A 1 147 ? -1.953  16.801 18.299 1.00 15.52 ? 127 SER   A N    1 
ATOM   1912 C CA   . SER   A 1 147 ? -2.641  17.742 17.439 1.00 15.69 ? 127 SER   A CA   1 
ATOM   1913 C C    . SER   A 1 147 ? -1.851  17.916 16.152 1.00 15.12 ? 127 SER   A C    1 
ATOM   1914 O O    . SER   A 1 147 ? -0.634  18.106 16.197 1.00 16.39 ? 127 SER   A O    1 
ATOM   1915 C CB   . SER   A 1 147 ? -2.708  19.077 18.168 1.00 15.93 ? 127 SER   A CB   1 
ATOM   1916 O OG   . SER   A 1 147 ? -3.241  20.135 17.399 1.00 16.54 ? 127 SER   A OG   1 
ATOM   1917 H H    . SER   A 1 147 ? -1.198  17.098 18.584 1.00 18.62 ? 127 SER   A H    1 
ATOM   1918 H HA   . SER   A 1 147 ? -3.528  17.425 17.209 1.00 18.83 ? 127 SER   A HA   1 
ATOM   1919 H HB2  . SER   A 1 147 ? -3.267  18.965 18.953 1.00 19.12 ? 127 SER   A HB2  1 
ATOM   1920 H HB3  . SER   A 1 147 ? -1.808  19.321 18.434 1.00 19.12 ? 127 SER   A HB3  1 
ATOM   1921 H HG   . SER   A 1 147 ? -2.744  20.289 16.739 1.00 19.84 ? 127 SER   A HG   1 
ATOM   1922 N N    . PHE   A 1 148 ? -2.546  17.830 15.013 1.00 15.27 ? 128 PHE   A N    1 
ATOM   1923 C CA   . PHE   A 1 148 ? -1.931  18.016 13.697 1.00 15.74 ? 128 PHE   A CA   1 
ATOM   1924 C C    . PHE   A 1 148 ? -2.699  19.104 12.963 1.00 16.35 ? 128 PHE   A C    1 
ATOM   1925 O O    . PHE   A 1 148 ? -3.887  18.934 12.657 1.00 17.21 ? 128 PHE   A O    1 
ATOM   1926 C CB   . PHE   A 1 148 ? -1.954  16.752 12.831 1.00 16.87 ? 128 PHE   A CB   1 
ATOM   1927 C CG   . PHE   A 1 148 ? -1.110  15.624 13.345 1.00 16.12 ? 128 PHE   A CG   1 
ATOM   1928 C CD1  . PHE   A 1 148 ? -1.607  14.720 14.259 1.00 16.87 ? 128 PHE   A CD1  1 
ATOM   1929 C CD2  . PHE   A 1 148 ? 0.181   15.461 12.910 1.00 17.69 ? 128 PHE   A CD2  1 
ATOM   1930 C CE1  . PHE   A 1 148 ? -0.830  13.678 14.728 1.00 17.25 ? 128 PHE   A CE1  1 
ATOM   1931 C CE2  . PHE   A 1 148 ? 0.958   14.428 13.381 1.00 18.07 ? 128 PHE   A CE2  1 
ATOM   1932 C CZ   . PHE   A 1 148 ? 0.465   13.542 14.291 1.00 17.49 ? 128 PHE   A CZ   1 
ATOM   1933 H H    . PHE   A 1 148 ? -3.389  17.663 14.978 1.00 18.32 ? 128 PHE   A H    1 
ATOM   1934 H HA   . PHE   A 1 148 ? -1.006  18.273 13.840 1.00 18.89 ? 128 PHE   A HA   1 
ATOM   1935 H HB2  . PHE   A 1 148 ? -2.868  16.431 12.777 1.00 20.24 ? 128 PHE   A HB2  1 
ATOM   1936 H HB3  . PHE   A 1 148 ? -1.629  16.978 11.945 1.00 20.24 ? 128 PHE   A HB3  1 
ATOM   1937 H HD1  . PHE   A 1 148 ? -2.481  14.813 14.565 1.00 20.24 ? 128 PHE   A HD1  1 
ATOM   1938 H HD2  . PHE   A 1 148 ? 0.535   16.056 12.290 1.00 21.23 ? 128 PHE   A HD2  1 
ATOM   1939 H HE1  . PHE   A 1 148 ? -1.183  13.070 15.338 1.00 20.70 ? 128 PHE   A HE1  1 
ATOM   1940 H HE2  . PHE   A 1 148 ? 1.831   14.333 13.074 1.00 21.69 ? 128 PHE   A HE2  1 
ATOM   1941 H HZ   . PHE   A 1 148 ? 1.000   12.852 14.612 1.00 20.99 ? 128 PHE   A HZ   1 
ATOM   1942 N N    . ARG   A 1 149 ? -2.015  20.176 12.593 1.00 16.68 ? 129 ARG   A N    1 
ATOM   1943 C CA   . ARG   A 1 149 ? -2.572  21.203 11.721 1.00 18.00 ? 129 ARG   A CA   1 
ATOM   1944 C C    . ARG   A 1 149 ? -1.803  21.227 10.406 1.00 18.35 ? 129 ARG   A C    1 
ATOM   1945 O O    . ARG   A 1 149 ? -0.571  21.141 10.396 1.00 19.24 ? 129 ARG   A O    1 
ATOM   1946 C CB   . ARG   A 1 149 ? -2.499  22.565 12.400 1.00 19.41 ? 129 ARG   A CB   1 
ATOM   1947 C CG   . ARG   A 1 149 ? -3.323  22.599 13.660 1.00 20.38 ? 129 ARG   A CG   1 
ATOM   1948 C CD   . ARG   A 1 149 ? -3.395  23.988 14.274 1.00 21.10 ? 129 ARG   A CD   1 
ATOM   1949 N NE   . ARG   A 1 149 ? -4.238  24.856 13.471 1.00 22.73 ? 129 ARG   A NE   1 
ATOM   1950 C CZ   . ARG   A 1 149 ? -4.525  26.114 13.765 1.00 25.41 ? 129 ARG   A CZ   1 
ATOM   1951 N NH1  . ARG   A 1 149 ? -3.990  26.717 14.807 1.00 27.35 ? 129 ARG   A NH1  1 
ATOM   1952 N NH2  . ARG   A 1 149 ? -5.380  26.777 12.997 1.00 27.29 ? 129 ARG   A NH2  1 
ATOM   1953 H H    . ARG   A 1 149 ? -1.207  20.336 12.840 1.00 20.01 ? 129 ARG   A H    1 
ATOM   1954 H HA   . ARG   A 1 149 ? -3.501  21.008 11.521 1.00 21.60 ? 129 ARG   A HA   1 
ATOM   1955 H HB2  . ARG   A 1 149 ? -1.577  22.759 12.632 1.00 23.29 ? 129 ARG   A HB2  1 
ATOM   1956 H HB3  . ARG   A 1 149 ? -2.838  23.243 11.795 1.00 23.29 ? 129 ARG   A HB3  1 
ATOM   1957 H HG2  . ARG   A 1 149 ? -4.227  22.313 13.456 1.00 24.46 ? 129 ARG   A HG2  1 
ATOM   1958 H HG3  . ARG   A 1 149 ? -2.926  22.002 14.314 1.00 24.46 ? 129 ARG   A HG3  1 
ATOM   1959 H HD2  . ARG   A 1 149 ? -3.772  23.930 15.165 1.00 25.32 ? 129 ARG   A HD2  1 
ATOM   1960 H HD3  . ARG   A 1 149 ? -2.505  24.372 14.314 1.00 25.32 ? 129 ARG   A HD3  1 
ATOM   1961 H HE   . ARG   A 1 149 ? -4.575  24.528 12.750 1.00 27.28 ? 129 ARG   A HE   1 
ATOM   1962 H HH11 . ARG   A 1 149 ? -3.440  26.292 15.313 1.00 32.82 ? 129 ARG   A HH11 1 
ATOM   1963 H HH12 . ARG   A 1 149 ? -4.190  27.535 14.980 1.00 32.82 ? 129 ARG   A HH12 1 
ATOM   1964 H HH21 . ARG   A 1 149 ? -5.739  26.389 12.319 1.00 32.75 ? 129 ARG   A HH21 1 
ATOM   1965 H HH22 . ARG   A 1 149 ? -5.575  27.595 13.178 1.00 32.75 ? 129 ARG   A HH22 1 
ATOM   1966 N N    . PHE   A 1 150 ? -2.539  21.316 9.294  1.00 18.47 ? 130 PHE   A N    1 
ATOM   1967 C CA   . PHE   A 1 150 ? -2.020  21.171 7.943  1.00 18.81 ? 130 PHE   A CA   1 
ATOM   1968 C C    . PHE   A 1 150 ? -2.068  22.476 7.179  1.00 20.02 ? 130 PHE   A C    1 
ATOM   1969 O O    . PHE   A 1 150 ? -2.931  23.328 7.414  1.00 22.63 ? 130 PHE   A O    1 
ATOM   1970 C CB   . PHE   A 1 150 ? -2.848  20.144 7.175  1.00 19.74 ? 130 PHE   A CB   1 
ATOM   1971 C CG   . PHE   A 1 150 ? -2.553  18.731 7.588  1.00 19.07 ? 130 PHE   A CG   1 
ATOM   1972 C CD1  . PHE   A 1 150 ? -3.114  18.173 8.743  1.00 19.58 ? 130 PHE   A CD1  1 
ATOM   1973 C CD2  . PHE   A 1 150 ? -1.656  17.967 6.843  1.00 19.28 ? 130 PHE   A CD2  1 
ATOM   1974 C CE1  . PHE   A 1 150 ? -2.786  16.875 9.126  1.00 19.46 ? 130 PHE   A CE1  1 
ATOM   1975 C CE2  . PHE   A 1 150 ? -1.373  16.683 7.202  1.00 20.43 ? 130 PHE   A CE2  1 
ATOM   1976 C CZ   . PHE   A 1 150 ? -1.906  16.143 8.365  1.00 19.48 ? 130 PHE   A CZ   1 
ATOM   1977 H H    . PHE   A 1 150 ? -3.386  21.468 9.304  1.00 22.16 ? 130 PHE   A H    1 
ATOM   1978 H HA   . PHE   A 1 150 ? -1.092  20.892 7.998  1.00 22.57 ? 130 PHE   A HA   1 
ATOM   1979 H HB2  . PHE   A 1 150 ? -3.789  20.313 7.336  1.00 23.69 ? 130 PHE   A HB2  1 
ATOM   1980 H HB3  . PHE   A 1 150 ? -2.654  20.226 6.228  1.00 23.69 ? 130 PHE   A HB3  1 
ATOM   1981 H HD1  . PHE   A 1 150 ? -3.707  18.671 9.257  1.00 23.50 ? 130 PHE   A HD1  1 
ATOM   1982 H HD2  . PHE   A 1 150 ? -1.246  18.337 6.094  1.00 23.13 ? 130 PHE   A HD2  1 
ATOM   1983 H HE1  . PHE   A 1 150 ? -3.161  16.505 9.892  1.00 23.35 ? 130 PHE   A HE1  1 
ATOM   1984 H HE2  . PHE   A 1 150 ? -0.820  16.164 6.664  1.00 24.52 ? 130 PHE   A HE2  1 
ATOM   1985 H HZ   . PHE   A 1 150 ? -1.666  15.285 8.631  1.00 23.38 ? 130 PHE   A HZ   1 
ATOM   1986 N N    . GLU   A 1 151 ? -1.151  22.590 6.217  1.00 21.52 ? 131 GLU   A N    1 
ATOM   1987 C CA   . GLU   A 1 151 ? -1.169  23.645 5.210  1.00 22.60 ? 131 GLU   A CA   1 
ATOM   1988 C C    . GLU   A 1 151 ? -0.702  23.051 3.887  1.00 22.62 ? 131 GLU   A C    1 
ATOM   1989 O O    . GLU   A 1 151 ? 0.368   22.439 3.826  1.00 23.07 ? 131 GLU   A O    1 
ATOM   1990 C CB   . GLU   A 1 151 ? -0.244  24.779 5.642  1.00 26.26 ? 131 GLU   A CB   1 
ATOM   1991 C CG   . GLU   A 1 151 ? -0.060  25.885 4.670  1.00 31.87 ? 131 GLU   A CG   1 
ATOM   1992 C CD   . GLU   A 1 151 ? 1.006   26.826 5.190  1.00 38.13 ? 131 GLU   A CD   1 
ATOM   1993 O OE1  . GLU   A 1 151 ? 0.646   27.682 6.018  1.00 40.70 ? 131 GLU   A OE1  1 
ATOM   1994 O OE2  . GLU   A 1 151 ? 2.202   26.659 4.827  1.00 40.29 ? 131 GLU   A OE2  1 
ATOM   1995 H H    . GLU   A 1 151 ? -0.489  22.049 6.126  1.00 25.83 ? 131 GLU   A H    1 
ATOM   1996 H HA   . GLU   A 1 151 ? -2.067  23.990 5.087  1.00 27.13 ? 131 GLU   A HA   1 
ATOM   1997 H HB2  . GLU   A 1 151 ? -0.604  25.169 6.454  1.00 31.51 ? 131 GLU   A HB2  1 
ATOM   1998 H HB3  . GLU   A 1 151 ? 0.633   24.403 5.816  1.00 31.51 ? 131 GLU   A HB3  1 
ATOM   1999 H HG2  . GLU   A 1 151 ? 0.223   25.529 3.814  1.00 38.24 ? 131 GLU   A HG2  1 
ATOM   2000 H HG3  . GLU   A 1 151 ? -0.891  26.376 4.567  1.00 38.24 ? 131 GLU   A HG3  1 
ATOM   2001 N N    . ASN   A 1 152 ? -1.524  23.183 2.849  1.00 25.12 ? 132 ASN   A N    1 
ATOM   2002 C CA   . ASN   A 1 152 ? -1.159  22.734 1.503  1.00 26.59 ? 132 ASN   A CA   1 
ATOM   2003 C C    . ASN   A 1 152 ? -0.642  21.295 1.493  1.00 24.74 ? 132 ASN   A C    1 
ATOM   2004 O O    . ASN   A 1 152 ? 0.378   20.978 0.868  1.00 26.84 ? 132 ASN   A O    1 
ATOM   2005 C CB   . ASN   A 1 152 ? -0.158  23.703 0.843  1.00 29.42 ? 132 ASN   A CB   1 
ATOM   2006 C CG   . ASN   A 1 152 ? 0.036   23.452 -0.637 1.00 31.91 ? 132 ASN   A CG   1 
ATOM   2007 O OD1  . ASN   A 1 152 ? -0.869  22.917 -1.301 1.00 33.97 ? 132 ASN   A OD1  1 
ATOM   2008 N ND2  . ASN   A 1 152 ? 1.219   23.848 -1.180 1.00 34.68 ? 132 ASN   A ND2  1 
ATOM   2009 H H    . ASN   A 1 152 ? -2.308  23.534 2.896  1.00 30.15 ? 132 ASN   A H    1 
ATOM   2010 H HA   . ASN   A 1 152 ? -1.966  22.735 0.965  1.00 31.91 ? 132 ASN   A HA   1 
ATOM   2011 H HB2  . ASN   A 1 152 ? -0.483  24.611 0.950  1.00 35.31 ? 132 ASN   A HB2  1 
ATOM   2012 H HB3  . ASN   A 1 152 ? 0.704   23.607 1.277  1.00 35.31 ? 132 ASN   A HB3  1 
ATOM   2013 H HD21 . ASN   A 1 152 ? 1.371   23.724 -2.017 1.00 41.62 ? 132 ASN   A HD21 1 
ATOM   2014 H HD22 . ASN   A 1 152 ? 1.815   24.223 -0.686 1.00 41.62 ? 132 ASN   A HD22 1 
ATOM   2015 N N    . GLY   A 1 153 ? -1.338  20.418 2.221  1.00 24.43 ? 133 GLY   A N    1 
ATOM   2016 C CA   . GLY   A 1 153 ? -1.126  18.995 2.114  1.00 25.08 ? 133 GLY   A CA   1 
ATOM   2017 C C    . GLY   A 1 153 ? -0.065  18.418 3.019  1.00 21.10 ? 133 GLY   A C    1 
ATOM   2018 O O    . GLY   A 1 153 ? 0.172   17.204 2.964  1.00 21.24 ? 133 GLY   A O    1 
ATOM   2019 H H    . GLY   A 1 153 ? -1.945  20.637 2.790  1.00 29.32 ? 133 GLY   A H    1 
ATOM   2020 H HA2  . GLY   A 1 153 ? -1.960  18.545 2.319  1.00 30.10 ? 133 GLY   A HA2  1 
ATOM   2021 H HA3  . GLY   A 1 153 ? -0.872  18.791 1.201  1.00 30.10 ? 133 GLY   A HA3  1 
ATOM   2022 N N    . LEU   A 1 154 ? 0.596   19.241 3.832  1.00 20.02 ? 134 LEU   A N    1 
ATOM   2023 C CA   . LEU   A 1 154 ? 1.642   18.793 4.750  1.00 19.15 ? 134 LEU   A CA   1 
ATOM   2024 C C    . LEU   A 1 154 ? 1.410   19.377 6.138  1.00 19.06 ? 134 LEU   A C    1 
ATOM   2025 O O    . LEU   A 1 154 ? 0.639   20.325 6.324  1.00 19.74 ? 134 LEU   A O    1 
ATOM   2026 C CB   . LEU   A 1 154 ? 3.052   19.154 4.251  1.00 19.96 ? 134 LEU   A CB   1 
ATOM   2027 C CG   . LEU   A 1 154 ? 3.437   18.455 2.947  1.00 21.10 ? 134 LEU   A CG   1 
ATOM   2028 C CD1  . LEU   A 1 154 ? 4.710   19.082 2.381  1.00 23.48 ? 134 LEU   A CD1  1 
ATOM   2029 C CD2  . LEU   A 1 154 ? 3.600   16.966 3.114  1.00 22.58 ? 134 LEU   A CD2  1 
ATOM   2030 H H    . LEU   A 1 154 ? 0.453   20.088 3.870  1.00 24.03 ? 134 LEU   A H    1 
ATOM   2031 H HA   . LEU   A 1 154 ? 1.586   17.827 4.817  1.00 22.98 ? 134 LEU   A HA   1 
ATOM   2032 H HB2  . LEU   A 1 154 ? 3.094   20.112 4.099  1.00 23.95 ? 134 LEU   A HB2  1 
ATOM   2033 H HB3  . LEU   A 1 154 ? 3.697   18.898 4.929  1.00 23.95 ? 134 LEU   A HB3  1 
ATOM   2034 H HG   . LEU   A 1 154 ? 2.714   18.576 2.313  1.00 25.32 ? 134 LEU   A HG   1 
ATOM   2035 H HD11 . LEU   A 1 154 ? 4.944   18.631 1.555  1.00 28.18 ? 134 LEU   A HD11 1 
ATOM   2036 H HD12 . LEU   A 1 154 ? 4.549   20.023 2.210  1.00 28.18 ? 134 LEU   A HD12 1 
ATOM   2037 H HD13 . LEU   A 1 154 ? 5.426   18.981 3.028  1.00 28.18 ? 134 LEU   A HD13 1 
ATOM   2038 H HD21 . LEU   A 1 154 ? 3.937   16.590 2.286  1.00 27.10 ? 134 LEU   A HD21 1 
ATOM   2039 H HD22 . LEU   A 1 154 ? 4.228   16.796 3.834  1.00 27.10 ? 134 LEU   A HD22 1 
ATOM   2040 H HD23 . LEU   A 1 154 ? 2.738   16.576 3.328  1.00 27.10 ? 134 LEU   A HD23 1 
ATOM   2041 N N    . ILE   A 1 155 ? 2.113   18.817 7.119  1.00 18.64 ? 135 ILE   A N    1 
ATOM   2042 C CA   . ILE   A 1 155 ? 1.920   19.226 8.509  1.00 18.63 ? 135 ILE   A CA   1 
ATOM   2043 C C    . ILE   A 1 155 ? 2.621   20.562 8.746  1.00 17.92 ? 135 ILE   A C    1 
ATOM   2044 O O    . ILE   A 1 155 ? 3.833   20.681 8.554  1.00 19.64 ? 135 ILE   A O    1 
ATOM   2045 C CB   . ILE   A 1 155 ? 2.454   18.167 9.482  1.00 17.71 ? 135 ILE   A CB   1 
ATOM   2046 C CG1  . ILE   A 1 155 ? 1.798   16.812 9.279  1.00 18.44 ? 135 ILE   A CG1  1 
ATOM   2047 C CG2  . ILE   A 1 155 ? 2.294   18.682 10.921 1.00 18.65 ? 135 ILE   A CG2  1 
ATOM   2048 C CD1  . ILE   A 1 155 ? 2.555   15.651 9.929  1.00 18.22 ? 135 ILE   A CD1  1 
ATOM   2049 H H    . ILE   A 1 155 ? 2.704   18.203 7.007  1.00 22.36 ? 135 ILE   A H    1 
ATOM   2050 H HA   . ILE   A 1 155 ? 0.969   19.344 8.662  1.00 22.36 ? 135 ILE   A HA   1 
ATOM   2051 H HB   . ILE   A 1 155 ? 3.396   18.026 9.299  1.00 21.26 ? 135 ILE   A HB   1 
ATOM   2052 H HG12 . ILE   A 1 155 ? 0.908   16.837 9.665  1.00 22.13 ? 135 ILE   A HG12 1 
ATOM   2053 H HG13 . ILE   A 1 155 ? 1.742   16.633 8.328  1.00 22.13 ? 135 ILE   A HG13 1 
ATOM   2054 H HG21 . ILE   A 1 155 ? 2.408   17.941 11.537 1.00 22.38 ? 135 ILE   A HG21 1 
ATOM   2055 H HG22 . ILE   A 1 155 ? 2.967   19.359 11.091 1.00 22.38 ? 135 ILE   A HG22 1 
ATOM   2056 H HG23 . ILE   A 1 155 ? 1.408   19.064 11.023 1.00 22.38 ? 135 ILE   A HG23 1 
ATOM   2057 H HD11 . ILE   A 1 155 ? 2.118   14.817 9.692  1.00 21.86 ? 135 ILE   A HD11 1 
ATOM   2058 H HD12 . ILE   A 1 155 ? 3.469   15.648 9.604  1.00 21.86 ? 135 ILE   A HD12 1 
ATOM   2059 H HD13 . ILE   A 1 155 ? 2.546   15.767 10.892 1.00 21.86 ? 135 ILE   A HD13 1 
ATOM   2060 N N    . LYS   A 1 156 ? 1.863   21.555 9.202  1.00 18.47 ? 136 LYS   A N    1 
ATOM   2061 C CA   . LYS   A 1 156 ? 2.383   22.852 9.597  1.00 19.74 ? 136 LYS   A CA   1 
ATOM   2062 C C    . LYS   A 1 156 ? 2.713   22.876 11.083 1.00 18.97 ? 136 LYS   A C    1 
ATOM   2063 O O    . LYS   A 1 156 ? 3.697   23.510 11.491 1.00 19.71 ? 136 LYS   A O    1 
ATOM   2064 C CB   . LYS   A 1 156 ? 1.353   23.938 9.286  1.00 23.70 ? 136 LYS   A CB   1 
ATOM   2065 C CG   . LYS   A 1 156 ? 1.760   25.352 9.661  1.00 27.22 ? 136 LYS   A CG   1 
ATOM   2066 C CD   . LYS   A 1 156 ? 2.897   25.856 8.815  1.00 33.32 ? 136 LYS   A CD   1 
ATOM   2067 C CE   . LYS   A 1 156 ? 3.128   27.350 9.056  1.00 40.85 ? 136 LYS   A CE   1 
ATOM   2068 N NZ   . LYS   A 1 156 ? 1.903   28.177 8.810  1.00 45.37 ? 136 LYS   A NZ   1 
ATOM   2069 H H    . LYS   A 1 156 ? 1.010   21.496 9.295  1.00 22.17 ? 136 LYS   A H    1 
ATOM   2070 H HA   . LYS   A 1 156 ? 3.185   23.059 9.092  1.00 23.69 ? 136 LYS   A HA   1 
ATOM   2071 H HB2  . LYS   A 1 156 ? 1.181   23.931 8.332  1.00 28.45 ? 136 LYS   A HB2  1 
ATOM   2072 H HB3  . LYS   A 1 156 ? 0.539   23.734 9.772  1.00 28.45 ? 136 LYS   A HB3  1 
ATOM   2073 H HG2  . LYS   A 1 156 ? 1.004   25.946 9.536  1.00 32.66 ? 136 LYS   A HG2  1 
ATOM   2074 H HG3  . LYS   A 1 156 ? 2.044   25.367 10.589 1.00 32.66 ? 136 LYS   A HG3  1 
ATOM   2075 H HD2  . LYS   A 1 156 ? 3.710   25.377 9.045  1.00 39.98 ? 136 LYS   A HD2  1 
ATOM   2076 H HD3  . LYS   A 1 156 ? 2.688   25.723 7.878  1.00 39.98 ? 136 LYS   A HD3  1 
ATOM   2077 H HE2  . LYS   A 1 156 ? 3.398   27.483 9.978  1.00 49.02 ? 136 LYS   A HE2  1 
ATOM   2078 H HE3  . LYS   A 1 156 ? 3.825   27.662 8.458  1.00 49.02 ? 136 LYS   A HE3  1 
ATOM   2079 H HZ1  . LYS   A 1 156 ? 2.110   29.042 8.838  1.00 54.44 ? 136 LYS   A HZ1  1 
ATOM   2080 H HZ2  . LYS   A 1 156 ? 1.563   27.987 8.010  1.00 54.44 ? 136 LYS   A HZ2  1 
ATOM   2081 H HZ3  . LYS   A 1 156 ? 1.291   28.006 9.433  1.00 54.44 ? 136 LYS   A HZ3  1 
ATOM   2082 N N    . GLU   A 1 157 ? 1.932   22.173 11.905 1.00 18.47 ? 137 GLU   A N    1 
ATOM   2083 C CA   . GLU   A 1 157 ? 2.181   22.142 13.337 1.00 18.31 ? 137 GLU   A CA   1 
ATOM   2084 C C    . GLU   A 1 157 ? 1.722   20.813 13.906 1.00 17.63 ? 137 GLU   A C    1 
ATOM   2085 O O    . GLU   A 1 157 ? 0.530   20.483 13.842 1.00 17.94 ? 137 GLU   A O    1 
ATOM   2086 C CB   . GLU   A 1 157 ? 1.439   23.279 14.048 1.00 19.88 ? 137 GLU   A CB   1 
ATOM   2087 C CG   . GLU   A 1 157 ? 1.771   23.376 15.521 1.00 21.32 ? 137 GLU   A CG   1 
ATOM   2088 C CD   . GLU   A 1 157 ? 0.821   24.276 16.272 1.00 23.77 ? 137 GLU   A CD   1 
ATOM   2089 O OE1  . GLU   A 1 157 ? -0.383  23.922 16.387 1.00 23.03 ? 137 GLU   A OE1  1 
ATOM   2090 O OE2  . GLU   A 1 157 ? 1.276   25.325 16.780 1.00 27.56 ? 137 GLU   A OE2  1 
ATOM   2091 H H    . GLU   A 1 157 ? 1.253   21.708 11.653 1.00 22.16 ? 137 GLU   A H    1 
ATOM   2092 H HA   . GLU   A 1 157 ? 3.136   22.230 13.482 1.00 21.98 ? 137 GLU   A HA   1 
ATOM   2093 H HB2  . GLU   A 1 157 ? 1.680   24.121 13.631 1.00 23.86 ? 137 GLU   A HB2  1 
ATOM   2094 H HB3  . GLU   A 1 157 ? 0.484   23.130 13.966 1.00 23.86 ? 137 GLU   A HB3  1 
ATOM   2095 H HG2  . GLU   A 1 157 ? 1.721   22.491 15.916 1.00 25.59 ? 137 GLU   A HG2  1 
ATOM   2096 H HG3  . GLU   A 1 157 ? 2.666   23.734 15.621 1.00 25.59 ? 137 GLU   A HG3  1 
ATOM   2097 N N    . GLN   A 1 158 ? 2.647   20.107 14.534 1.00 16.55 ? 138 GLN   A N    1 
ATOM   2098 C CA   . GLN   A 1 158 ? 2.367   18.901 15.298 1.00 15.99 ? 138 GLN   A CA   1 
ATOM   2099 C C    . GLN   A 1 158 ? 2.699   19.216 16.749 1.00 16.00 ? 138 GLN   A C    1 
ATOM   2100 O O    . GLN   A 1 158 ? 3.748   19.795 17.048 1.00 17.80 ? 138 GLN   A O    1 
ATOM   2101 C CB   . GLN   A 1 158 ? 3.197   17.735 14.765 1.00 17.67 ? 138 GLN   A CB   1 
ATOM   2102 C CG   . GLN   A 1 158 ? 3.032   16.427 15.566 1.00 18.36 ? 138 GLN   A CG   1 
ATOM   2103 C CD   . GLN   A 1 158 ? 3.980   16.339 16.780 1.00 20.80 ? 138 GLN   A CD   1 
ATOM   2104 O OE1  . GLN   A 1 158 ? 5.059   16.927 16.769 1.00 21.58 ? 138 GLN   A OE1  1 
ATOM   2105 N NE2  . GLN   A 1 158 ? 3.622   15.549 17.775 1.00 21.76 ? 138 GLN   A NE2  1 
ATOM   2106 H H    . GLN   A 1 158 ? 3.482   20.315 14.533 1.00 19.86 ? 138 GLN   A H    1 
ATOM   2107 H HA   . GLN   A 1 158 ? 1.435   18.638 15.241 1.00 19.19 ? 138 GLN   A HA   1 
ATOM   2108 H HB2  . GLN   A 1 158 ? 2.929   17.556 13.850 1.00 21.21 ? 138 GLN   A HB2  1 
ATOM   2109 H HB3  . GLN   A 1 158 ? 4.134   17.982 14.795 1.00 21.21 ? 138 GLN   A HB3  1 
ATOM   2110 H HG2  . GLN   A 1 158 ? 2.120   16.371 15.893 1.00 22.03 ? 138 GLN   A HG2  1 
ATOM   2111 H HG3  . GLN   A 1 158 ? 3.221   15.675 14.983 1.00 22.03 ? 138 GLN   A HG3  1 
ATOM   2112 H HE21 . GLN   A 1 158 ? 2.884   15.109 17.730 1.00 26.11 ? 138 GLN   A HE21 1 
ATOM   2113 H HE22 . GLN   A 1 158 ? 4.125   15.475 18.468 1.00 26.11 ? 138 GLN   A HE22 1 
ATOM   2114 N N    . ARG   A 1 159 ? 1.796   18.850 17.655 1.00 15.55 ? 139 ARG   A N    1 
ATOM   2115 C CA   . ARG   A 1 159 ? 2.033   19.004 19.086 1.00 15.87 ? 139 ARG   A CA   1 
ATOM   2116 C C    . ARG   A 1 159 ? 1.639   17.726 19.796 1.00 15.78 ? 139 ARG   A C    1 
ATOM   2117 O O    . ARG   A 1 159 ? 0.583   17.167 19.514 1.00 17.29 ? 139 ARG   A O    1 
ATOM   2118 C CB   . ARG   A 1 159 ? 1.226   20.156 19.689 1.00 15.81 ? 139 ARG   A CB   1 
ATOM   2119 C CG   . ARG   A 1 159 ? 1.404   21.519 18.996 1.00 16.42 ? 139 ARG   A CG   1 
ATOM   2120 C CD   . ARG   A 1 159 ? 0.466   22.557 19.582 1.00 17.22 ? 139 ARG   A CD   1 
ATOM   2121 N NE   . ARG   A 1 159 ? -0.910  22.258 19.208 1.00 17.54 ? 139 ARG   A NE   1 
ATOM   2122 C CZ   . ARG   A 1 159 ? -1.974  22.696 19.877 1.00 17.24 ? 139 ARG   A CZ   1 
ATOM   2123 N NH1  . ARG   A 1 159 ? -1.856  23.487 20.920 1.00 17.50 ? 139 ARG   A NH1  1 
ATOM   2124 N NH2  . ARG   A 1 159 ? -3.182  22.310 19.497 1.00 17.24 ? 139 ARG   A NH2  1 
ATOM   2125 H H    . ARG   A 1 159 ? 1.031   18.506 17.463 1.00 18.66 ? 139 ARG   A H    1 
ATOM   2126 H HA   . ARG   A 1 159 ? 2.976   19.183 19.224 1.00 19.05 ? 139 ARG   A HA   1 
ATOM   2127 H HB2  . ARG   A 1 159 ? 0.285   19.927 19.642 1.00 18.97 ? 139 ARG   A HB2  1 
ATOM   2128 H HB3  . ARG   A 1 159 ? 1.495   20.265 20.615 1.00 18.97 ? 139 ARG   A HB3  1 
ATOM   2129 H HG2  . ARG   A 1 159 ? 2.316   21.826 19.116 1.00 19.70 ? 139 ARG   A HG2  1 
ATOM   2130 H HG3  . ARG   A 1 159 ? 1.207   21.427 18.050 1.00 19.70 ? 139 ARG   A HG3  1 
ATOM   2131 H HD2  . ARG   A 1 159 ? 0.534   22.549 20.550 1.00 20.67 ? 139 ARG   A HD2  1 
ATOM   2132 H HD3  . ARG   A 1 159 ? 0.697   23.435 19.241 1.00 20.67 ? 139 ARG   A HD3  1 
ATOM   2133 H HE   . ARG   A 1 159 ? -1.043  21.769 18.513 1.00 21.04 ? 139 ARG   A HE   1 
ATOM   2134 H HH11 . ARG   A 1 159 ? -1.076  23.734 21.185 1.00 21.00 ? 139 ARG   A HH11 1 
ATOM   2135 H HH12 . ARG   A 1 159 ? -2.558  23.757 21.336 1.00 21.00 ? 139 ARG   A HH12 1 
ATOM   2136 H HH21 . ARG   A 1 159 ? -3.274  21.782 18.824 1.00 20.69 ? 139 ARG   A HH21 1 
ATOM   2137 H HH22 . ARG   A 1 159 ? -3.876  22.588 19.923 1.00 20.69 ? 139 ARG   A HH22 1 
ATOM   2138 N N    . GLU   A 1 160 ? 2.437   17.307 20.767 1.00 15.94 ? 140 GLU   A N    1 
ATOM   2139 C CA   . GLU   A 1 160 ? 2.067   16.159 21.584 1.00 16.59 ? 140 GLU   A CA   1 
ATOM   2140 C C    . GLU   A 1 160 ? 1.959   16.534 23.056 1.00 15.64 ? 140 GLU   A C    1 
ATOM   2141 O O    . GLU   A 1 160 ? 2.685   17.400 23.556 1.00 16.64 ? 140 GLU   A O    1 
ATOM   2142 C CB   . GLU   A 1 160 ? 2.906   14.921 21.350 1.00 21.51 ? 140 GLU   A CB   1 
ATOM   2143 C CG   . GLU   A 1 160 ? 4.308   15.015 21.705 1.00 22.58 ? 140 GLU   A CG   1 
ATOM   2144 C CD   . GLU   A 1 160 ? 5.176   14.028 20.907 1.00 24.24 ? 140 GLU   A CD   1 
ATOM   2145 O OE1  . GLU   A 1 160 ? 5.215   14.136 19.677 1.00 25.13 ? 140 GLU   A OE1  1 
ATOM   2146 O OE2  . GLU   A 1 160 ? 5.831   13.148 21.499 1.00 26.98 ? 140 GLU   A OE2  1 
ATOM   2147 H H    . GLU   A 1 160 ? 3.191   17.667 20.970 1.00 19.13 ? 140 GLU   A H    1 
ATOM   2148 H HA   . GLU   A 1 160 ? 1.175   15.893 21.310 1.00 19.90 ? 140 GLU   A HA   1 
ATOM   2149 H HB2  . GLU   A 1 160 ? 2.528   14.198 21.875 1.00 25.81 ? 140 GLU   A HB2  1 
ATOM   2150 H HB3  . GLU   A 1 160 ? 2.865   14.702 20.406 1.00 25.81 ? 140 GLU   A HB3  1 
ATOM   2151 H HG2  . GLU   A 1 160 ? 4.624   15.913 21.519 1.00 27.10 ? 140 GLU   A HG2  1 
ATOM   2152 H HG3  . GLU   A 1 160 ? 4.412   14.815 22.648 1.00 27.10 ? 140 GLU   A HG3  1 
ATOM   2153 N N    . PHE   A 1 161 ? 0.998   15.891 23.723 1.00 15.36 ? 141 PHE   A N    1 
ATOM   2154 C CA   . PHE   A 1 161 ? 0.621   16.198 25.094 1.00 15.07 ? 141 PHE   A CA   1 
ATOM   2155 C C    . PHE   A 1 161 ? 0.560   14.902 25.896 1.00 14.94 ? 141 PHE   A C    1 
ATOM   2156 O O    . PHE   A 1 161 ? -0.081  13.936 25.470 1.00 15.91 ? 141 PHE   A O    1 
ATOM   2157 C CB   . PHE   A 1 161 ? -0.778  16.827 25.160 1.00 15.78 ? 141 PHE   A CB   1 
ATOM   2158 C CG   . PHE   A 1 161 ? -0.915  18.059 24.321 1.00 15.63 ? 141 PHE   A CG   1 
ATOM   2159 C CD1  . PHE   A 1 161 ? -1.240  17.959 22.960 1.00 16.81 ? 141 PHE   A CD1  1 
ATOM   2160 C CD2  . PHE   A 1 161 ? -0.780  19.331 24.887 1.00 16.81 ? 141 PHE   A CD2  1 
ATOM   2161 C CE1  . PHE   A 1 161 ? -1.387  19.118 22.200 1.00 17.09 ? 141 PHE   A CE1  1 
ATOM   2162 C CE2  . PHE   A 1 161 ? -0.924  20.476 24.123 1.00 18.33 ? 141 PHE   A CE2  1 
ATOM   2163 C CZ   . PHE   A 1 161 ? -1.243  20.358 22.768 1.00 18.24 ? 141 PHE   A CZ   1 
ATOM   2164 H H    . PHE   A 1 161 ? 0.535   15.250 23.385 1.00 18.43 ? 141 PHE   A H    1 
ATOM   2165 H HA   . PHE   A 1 161 ? 1.283   16.803 25.465 1.00 18.09 ? 141 PHE   A HA   1 
ATOM   2166 H HB2  . PHE   A 1 161 ? -1.428  16.179 24.846 1.00 18.94 ? 141 PHE   A HB2  1 
ATOM   2167 H HB3  . PHE   A 1 161 ? -0.969  17.070 26.079 1.00 18.94 ? 141 PHE   A HB3  1 
ATOM   2168 H HD1  . PHE   A 1 161 ? -1.357  17.124 22.567 1.00 20.18 ? 141 PHE   A HD1  1 
ATOM   2169 H HD2  . PHE   A 1 161 ? -0.590  19.409 25.794 1.00 20.17 ? 141 PHE   A HD2  1 
ATOM   2170 H HE1  . PHE   A 1 161 ? -1.585  19.049 21.294 1.00 20.51 ? 141 PHE   A HE1  1 
ATOM   2171 H HE2  . PHE   A 1 161 ? -0.809  21.315 24.508 1.00 22.00 ? 141 PHE   A HE2  1 
ATOM   2172 H HZ   . PHE   A 1 161 ? -1.358  21.121 22.250 1.00 21.89 ? 141 PHE   A HZ   1 
ATOM   2173 N N    . MET   A 1 162 ? 1.252   14.868 27.027 1.00 14.94 ? 142 MET   A N    1 
ATOM   2174 C CA   . MET   A 1 162 ? 1.275   13.683 27.875 1.00 15.17 ? 142 MET   A CA   1 
ATOM   2175 C C    . MET   A 1 162 ? 1.410   14.118 29.329 1.00 15.09 ? 142 MET   A C    1 
ATOM   2176 O O    . MET   A 1 162 ? 1.494   15.310 29.631 1.00 17.25 ? 142 MET   A O    1 
ATOM   2177 C CB   . MET   A 1 162 ? 2.350   12.692 27.435 1.00 16.20 ? 142 MET   A CB   1 
ATOM   2178 C CG   . MET   A 1 162 ? 3.762   13.267 27.262 1.00 18.16 ? 142 MET   A CG   1 
ATOM   2179 S SD   . MET   A 1 162 ? 4.432   13.967 28.779 1.00 19.88 ? 142 MET   A SD   1 
ATOM   2180 C CE   . MET   A 1 162 ? 6.154   14.080 28.525 1.00 19.29 ? 142 MET   A CE   1 
ATOM   2181 H H    . MET   A 1 162 ? 1.720   15.524 27.329 1.00 17.93 ? 142 MET   A H    1 
ATOM   2182 H HA   . MET   A 1 162 ? 0.427   13.220 27.784 1.00 18.20 ? 142 MET   A HA   1 
ATOM   2183 H HB2  . MET   A 1 162 ? 2.406   11.989 28.101 1.00 19.44 ? 142 MET   A HB2  1 
ATOM   2184 H HB3  . MET   A 1 162 ? 2.086   12.318 26.579 1.00 19.44 ? 142 MET   A HB3  1 
ATOM   2185 H HG2  . MET   A 1 162 ? 4.357   12.557 26.973 1.00 21.79 ? 142 MET   A HG2  1 
ATOM   2186 H HG3  . MET   A 1 162 ? 3.736   13.970 26.595 1.00 21.79 ? 142 MET   A HG3  1 
ATOM   2187 H HE1  . MET   A 1 162 ? 6.551   14.565 29.265 1.00 23.15 ? 142 MET   A HE1  1 
ATOM   2188 H HE2  . MET   A 1 162 ? 6.525   13.185 28.478 1.00 23.15 ? 142 MET   A HE2  1 
ATOM   2189 H HE3  . MET   A 1 162 ? 6.320   14.550 27.693 1.00 23.15 ? 142 MET   A HE3  1 
ATOM   2190 N N    . ASN   A 1 163 ? 1.406   13.141 30.238 1.00 15.70 ? 143 ASN   A N    1 
ATOM   2191 C CA   . ASN   A 1 163 ? 1.670   13.385 31.648 1.00 15.60 ? 143 ASN   A CA   1 
ATOM   2192 C C    . ASN   A 1 163 ? 3.164   13.188 31.903 1.00 15.63 ? 143 ASN   A C    1 
ATOM   2193 O O    . ASN   A 1 163 ? 3.638   12.034 31.891 1.00 16.77 ? 143 ASN   A O    1 
ATOM   2194 C CB   . ASN   A 1 163 ? 0.871   12.411 32.481 1.00 17.07 ? 143 ASN   A CB   1 
ATOM   2195 C CG   . ASN   A 1 163 ? 1.084   12.616 33.951 1.00 17.60 ? 143 ASN   A CG   1 
ATOM   2196 O OD1  . ASN   A 1 163 ? 1.875   13.466 34.381 1.00 17.64 ? 143 ASN   A OD1  1 
ATOM   2197 N ND2  . ASN   A 1 163 ? 0.378   11.834 34.756 1.00 20.09 ? 143 ASN   A ND2  1 
ATOM   2198 H H    . ASN   A 1 163 ? 1.251   12.315 30.056 1.00 18.84 ? 143 ASN   A H    1 
ATOM   2199 H HA   . ASN   A 1 163 ? 1.429   14.294 31.888 1.00 18.72 ? 143 ASN   A HA   1 
ATOM   2200 H HB2  . ASN   A 1 163 ? -0.073  12.530 32.293 1.00 20.48 ? 143 ASN   A HB2  1 
ATOM   2201 H HB3  . ASN   A 1 163 ? 1.142   11.506 32.260 1.00 20.48 ? 143 ASN   A HB3  1 
ATOM   2202 H HD21 . ASN   A 1 163 ? 0.460   11.908 35.609 1.00 24.10 ? 143 ASN   A HD21 1 
ATOM   2203 H HD22 . ASN   A 1 163 ? -0.162  11.252 34.425 1.00 24.10 ? 143 ASN   A HD22 1 
ATOM   2204 N N    . PRO   A 1 164 ? 3.938   14.250 32.126 1.00 15.44 ? 144 PRO   A N    1 
ATOM   2205 C CA   . PRO   A 1 164 ? 5.393   14.070 32.324 1.00 16.11 ? 144 PRO   A CA   1 
ATOM   2206 C C    . PRO   A 1 164 ? 5.749   13.190 33.502 1.00 16.31 ? 144 PRO   A C    1 
ATOM   2207 O O    . PRO   A 1 164 ? 6.866   12.664 33.543 1.00 17.59 ? 144 PRO   A O    1 
ATOM   2208 C CB   . PRO   A 1 164 ? 5.911   15.500 32.493 1.00 18.80 ? 144 PRO   A CB   1 
ATOM   2209 C CG   . PRO   A 1 164 ? 4.874   16.379 31.828 1.00 19.11 ? 144 PRO   A CG   1 
ATOM   2210 C CD   . PRO   A 1 164 ? 3.570   15.675 32.124 1.00 16.06 ? 144 PRO   A CD   1 
ATOM   2211 H HA   . PRO   A 1 164 ? 5.789   13.689 31.524 1.00 19.33 ? 144 PRO   A HA   1 
ATOM   2212 H HB2  . PRO   A 1 164 ? 5.991   15.712 33.437 1.00 22.57 ? 144 PRO   A HB2  1 
ATOM   2213 H HB3  . PRO   A 1 164 ? 6.773   15.592 32.058 1.00 22.57 ? 144 PRO   A HB3  1 
ATOM   2214 H HG2  . PRO   A 1 164 ? 4.890   17.269 32.215 1.00 22.94 ? 144 PRO   A HG2  1 
ATOM   2215 H HG3  . PRO   A 1 164 ? 5.038   16.430 30.874 1.00 22.94 ? 144 PRO   A HG3  1 
ATOM   2216 H HD2  . PRO   A 1 164 ? 3.224   15.942 32.990 1.00 19.27 ? 144 PRO   A HD2  1 
ATOM   2217 H HD3  . PRO   A 1 164 ? 2.915   15.861 31.434 1.00 19.27 ? 144 PRO   A HD3  1 
ATOM   2218 N N    . CYS   A 1 165 ? 4.859   13.038 34.481 1.00 16.50 ? 145 CYS   A N    1 
ATOM   2219 C CA   . CYS   A 1 165 ? 5.169   12.182 35.621 1.00 17.76 ? 145 CYS   A CA   1 
ATOM   2220 C C    . CYS   A 1 165 ? 5.533   10.763 35.203 1.00 17.40 ? 145 CYS   A C    1 
ATOM   2221 O O    . CYS   A 1 165 ? 6.380   10.137 35.854 1.00 18.26 ? 145 CYS   A O    1 
ATOM   2222 C CB   . CYS   A 1 165 ? 3.984   12.185 36.583 1.00 18.98 ? 145 CYS   A CB   1 
ATOM   2223 S SG   . CYS   A 1 165 ? 3.648   13.759 37.373 1.00 21.39 ? 145 CYS   A SG   1 
ATOM   2224 H H    . CYS   A 1 165 ? 4.086   13.413 34.509 1.00 19.80 ? 145 CYS   A H    1 
ATOM   2225 H HA   . CYS   A 1 165 ? 5.943   12.539 36.084 1.00 21.32 ? 145 CYS   A HA   1 
ATOM   2226 H HB2  . CYS   A 1 165 ? 3.188   11.932 36.090 1.00 22.78 ? 145 CYS   A HB2  1 
ATOM   2227 H HB3  . CYS   A 1 165 ? 4.159   11.539 37.286 1.00 22.78 ? 145 CYS   A HB3  1 
ATOM   2228 H HG   . CYS   A 1 165 ? 2.534   13.743 37.819 1.00 25.66 ? 145 CYS   A HG   1 
ATOM   2229 N N    . GLU   A 1 166 ? 4.935   10.256 34.134 1.00 17.02 ? 146 GLU   A N    1 
ATOM   2230 C CA   . GLU   A 1 166 ? 5.268   8.911  33.691 1.00 17.36 ? 146 GLU   A CA   1 
ATOM   2231 C C    . GLU   A 1 166 ? 6.665   8.861  33.084 1.00 18.02 ? 146 GLU   A C    1 
ATOM   2232 O O    . GLU   A 1 166 ? 7.359   7.846  33.200 1.00 20.00 ? 146 GLU   A O    1 
ATOM   2233 C CB   . GLU   A 1 166 ? 4.237   8.383  32.704 1.00 20.00 ? 146 GLU   A CB   1 
ATOM   2234 C CG   . GLU   A 1 166 ? 2.828   8.327  33.221 1.00 24.86 ? 146 GLU   A CG   1 
ATOM   2235 C CD   . GLU   A 1 166 ? 2.627   7.425  34.379 1.00 31.53 ? 146 GLU   A CD   1 
ATOM   2236 O OE1  . GLU   A 1 166 ? 3.351   6.425  34.560 1.00 31.81 ? 146 GLU   A OE1  1 
ATOM   2237 O OE2  . GLU   A 1 166 ? 1.650   7.721  35.077 1.00 38.01 ? 146 GLU   A OE2  1 
ATOM   2238 H H    . GLU   A 1 166 ? 4.346   10.661 33.657 1.00 20.42 ? 146 GLU   A H    1 
ATOM   2239 H HA   . GLU   A 1 166 ? 5.244   8.322  34.462 1.00 20.83 ? 146 GLU   A HA   1 
ATOM   2240 H HB2  . GLU   A 1 166 ? 4.236   8.960  31.923 1.00 24.00 ? 146 GLU   A HB2  1 
ATOM   2241 H HB3  . GLU   A 1 166 ? 4.489   7.481  32.450 1.00 24.00 ? 146 GLU   A HB3  1 
ATOM   2242 H HG2  . GLU   A 1 166 ? 2.565   9.219  33.498 1.00 29.83 ? 146 GLU   A HG2  1 
ATOM   2243 H HG3  . GLU   A 1 166 ? 2.249   8.018  32.507 1.00 29.83 ? 146 GLU   A HG3  1 
ATOM   2244 N N    . GLN   A 1 167 ? 7.081   9.928  32.413 1.00 16.87 ? 147 GLN   A N    1 
ATOM   2245 C CA   . GLN   A 1 167 ? 8.454   9.989  31.909 1.00 16.96 ? 147 GLN   A CA   1 
ATOM   2246 C C    . GLN   A 1 167 ? 9.442   10.111 33.066 1.00 17.44 ? 147 GLN   A C    1 
ATOM   2247 O O    . GLN   A 1 167 ? 10.509  9.486  33.048 1.00 18.45 ? 147 GLN   A O    1 
ATOM   2248 C CB   . GLN   A 1 167 ? 8.625   11.068 30.847 1.00 18.34 ? 147 GLN   A CB   1 
ATOM   2249 C CG   . GLN   A 1 167 ? 9.903   10.856 30.069 1.00 20.03 ? 147 GLN   A CG   1 
ATOM   2250 C CD   . GLN   A 1 167 ? 10.000  11.715 28.802 1.00 21.56 ? 147 GLN   A CD   1 
ATOM   2251 O OE1  . GLN   A 1 167 ? 9.000   12.211 28.310 1.00 22.59 ? 147 GLN   A OE1  1 
ATOM   2252 N NE2  . GLN   A 1 167 ? 11.201  11.827 28.242 1.00 23.41 ? 147 GLN   A NE2  1 
ATOM   2253 H H    . GLN   A 1 167 ? 6.600   10.619 32.236 1.00 20.24 ? 147 GLN   A H    1 
ATOM   2254 H HA   . GLN   A 1 167 ? 8.660   9.164  31.443 1.00 20.36 ? 147 GLN   A HA   1 
ATOM   2255 H HB2  . GLN   A 1 167 ? 7.878   11.034 30.229 1.00 22.01 ? 147 GLN   A HB2  1 
ATOM   2256 H HB3  . GLN   A 1 167 ? 8.663   11.939 31.273 1.00 22.01 ? 147 GLN   A HB3  1 
ATOM   2257 H HG2  . GLN   A 1 167 ? 10.656  11.081 30.638 1.00 24.04 ? 147 GLN   A HG2  1 
ATOM   2258 H HG3  . GLN   A 1 167 ? 9.955   9.925  29.801 1.00 24.04 ? 147 GLN   A HG3  1 
ATOM   2259 H HE21 . GLN   A 1 167 ? 11.878  11.427 28.591 1.00 28.09 ? 147 GLN   A HE21 1 
ATOM   2260 H HE22 . GLN   A 1 167 ? 11.301  12.299 27.530 1.00 28.09 ? 147 GLN   A HE22 1 
ATOM   2261 N N    . PHE   A 1 168 ? 9.103   10.907 34.093 1.00 17.79 ? 148 PHE   A N    1 
ATOM   2262 C CA   . PHE   A 1 168 ? 9.940   10.927 35.294 1.00 18.53 ? 148 PHE   A CA   1 
ATOM   2263 C C    . PHE   A 1 168 ? 10.154  9.509  35.827 1.00 19.03 ? 148 PHE   A C    1 
ATOM   2264 O O    . PHE   A 1 168 ? 11.284  9.099  36.123 1.00 20.04 ? 148 PHE   A O    1 
ATOM   2265 C CB   . PHE   A 1 168 ? 9.315   11.788 36.401 1.00 19.33 ? 148 PHE   A CB   1 
ATOM   2266 C CG   . PHE   A 1 168 ? 9.096   13.239 36.056 1.00 21.03 ? 148 PHE   A CG   1 
ATOM   2267 C CD1  . PHE   A 1 168 ? 9.778   13.885 35.041 1.00 23.88 ? 148 PHE   A CD1  1 
ATOM   2268 C CD2  . PHE   A 1 168 ? 8.155   13.971 36.792 1.00 21.34 ? 148 PHE   A CD2  1 
ATOM   2269 C CE1  . PHE   A 1 168 ? 9.502   15.233 34.754 1.00 27.89 ? 148 PHE   A CE1  1 
ATOM   2270 C CE2  . PHE   A 1 168 ? 7.894   15.293 36.523 1.00 25.04 ? 148 PHE   A CE2  1 
ATOM   2271 C CZ   . PHE   A 1 168 ? 8.556   15.940 35.506 1.00 27.97 ? 148 PHE   A CZ   1 
ATOM   2272 H H    . PHE   A 1 168 ? 8.418   11.426 34.115 1.00 21.35 ? 148 PHE   A H    1 
ATOM   2273 H HA   . PHE   A 1 168 ? 10.791  11.323 35.050 1.00 22.24 ? 148 PHE   A HA   1 
ATOM   2274 H HB2  . PHE   A 1 168 ? 8.450   11.412 36.627 1.00 23.20 ? 148 PHE   A HB2  1 
ATOM   2275 H HB3  . PHE   A 1 168 ? 9.900   11.762 37.174 1.00 23.20 ? 148 PHE   A HB3  1 
ATOM   2276 H HD1  . PHE   A 1 168 ? 10.420  13.427 34.549 1.00 28.66 ? 148 PHE   A HD1  1 
ATOM   2277 H HD2  . PHE   A 1 168 ? 7.695   13.551 37.483 1.00 25.61 ? 148 PHE   A HD2  1 
ATOM   2278 H HE1  . PHE   A 1 168 ? 9.951   15.658 34.059 1.00 33.47 ? 148 PHE   A HE1  1 
ATOM   2279 H HE2  . PHE   A 1 168 ? 7.266   15.753 37.033 1.00 30.05 ? 148 PHE   A HE2  1 
ATOM   2280 H HZ   . PHE   A 1 168 ? 8.377   16.834 35.320 1.00 33.56 ? 148 PHE   A HZ   1 
ATOM   2281 N N    A ARG   A 1 169 ? 9.061   8.765  35.992 0.68 18.66 ? 149 ARG   A N    1 
ATOM   2282 N N    B ARG   A 1 169 ? 9.065   8.745  35.992 0.32 20.07 ? 149 ARG   A N    1 
ATOM   2283 C CA   A ARG   A 1 169 ? 9.169   7.407  36.514 0.68 19.75 ? 149 ARG   A CA   1 
ATOM   2284 C CA   B ARG   A 1 169 ? 9.216   7.396  36.533 0.32 21.84 ? 149 ARG   A CA   1 
ATOM   2285 C C    A ARG   A 1 169 ? 10.084  6.537  35.658 0.68 20.18 ? 149 ARG   A C    1 
ATOM   2286 C C    B ARG   A 1 169 ? 10.143  6.557  35.658 0.32 20.88 ? 149 ARG   A C    1 
ATOM   2287 O O    A ARG   A 1 169 ? 10.879  5.760  36.190 0.68 21.83 ? 149 ARG   A O    1 
ATOM   2288 O O    B ARG   A 1 169 ? 10.989  5.818  36.168 0.32 21.51 ? 149 ARG   A O    1 
ATOM   2289 C CB   A ARG   A 1 169 ? 7.777   6.796  36.626 0.68 21.80 ? 149 ARG   A CB   1 
ATOM   2290 C CB   B ARG   A 1 169 ? 7.867   6.686  36.676 0.32 25.15 ? 149 ARG   A CB   1 
ATOM   2291 C CG   A ARG   A 1 169 ? 7.026   7.232  37.835 0.68 23.50 ? 149 ARG   A CG   1 
ATOM   2292 C CG   B ARG   A 1 169 ? 6.724   7.542  37.161 0.32 29.14 ? 149 ARG   A CG   1 
ATOM   2293 C CD   A ARG   A 1 169 ? 5.700   6.467  37.911 0.68 28.29 ? 149 ARG   A CD   1 
ATOM   2294 C CD   B ARG   A 1 169 ? 5.531   6.688  37.616 0.32 32.22 ? 149 ARG   A CD   1 
ATOM   2295 N NE   A ARG   A 1 169 ? 4.603   7.279  37.397 0.68 35.83 ? 149 ARG   A NE   1 
ATOM   2296 N NE   B ARG   A 1 169 ? 4.997   7.116  38.908 0.32 34.84 ? 149 ARG   A NE   1 
ATOM   2297 C CZ   A ARG   A 1 169 ? 3.895   8.131  38.129 0.68 39.56 ? 149 ARG   A CZ   1 
ATOM   2298 C CZ   B ARG   A 1 169 ? 4.132   8.109  39.072 0.32 38.99 ? 149 ARG   A CZ   1 
ATOM   2299 N NH1  A ARG   A 1 169 ? 4.119   8.280  39.424 0.68 43.81 ? 149 ARG   A NH1  1 
ATOM   2300 N NH1  B ARG   A 1 169 ? 3.633   8.768  38.039 0.32 41.29 ? 149 ARG   A NH1  1 
ATOM   2301 N NH2  A ARG   A 1 169 ? 2.953   8.864  37.542 0.68 38.54 ? 149 ARG   A NH2  1 
ATOM   2302 N NH2  B ARG   A 1 169 ? 3.755   8.443  40.307 0.32 39.28 ? 149 ARG   A NH2  1 
ATOM   2303 H H    A ARG   A 1 169 ? 8.259   9.019  35.813 0.68 22.39 ? 149 ARG   A H    1 
ATOM   2304 H H    B ARG   A 1 169 ? 8.259   8.979  35.806 0.32 24.09 ? 149 ARG   A H    1 
ATOM   2305 H HA   A ARG   A 1 169 ? 9.561   7.440  37.401 0.68 23.71 ? 149 ARG   A HA   1 
ATOM   2306 H HA   B ARG   A 1 169 ? 9.596   7.480  37.421 0.32 26.21 ? 149 ARG   A HA   1 
ATOM   2307 H HB2  A ARG   A 1 169 ? 7.260   7.055  35.847 0.68 26.16 ? 149 ARG   A HB2  1 
ATOM   2308 H HB2  B ARG   A 1 169 ? 7.615   6.334  35.808 0.32 30.18 ? 149 ARG   A HB2  1 
ATOM   2309 H HB3  A ARG   A 1 169 ? 7.862   5.831  36.662 0.68 26.16 ? 149 ARG   A HB3  1 
ATOM   2310 H HB3  B ARG   A 1 169 ? 7.972   5.960  37.311 0.32 30.18 ? 149 ARG   A HB3  1 
ATOM   2311 H HG2  A ARG   A 1 169 ? 7.544   7.040  38.632 0.68 28.21 ? 149 ARG   A HG2  1 
ATOM   2312 H HG2  B ARG   A 1 169 ? 7.021   8.076  37.914 0.32 34.97 ? 149 ARG   A HG2  1 
ATOM   2313 H HG3  A ARG   A 1 169 ? 6.838   8.182  37.782 0.68 28.21 ? 149 ARG   A HG3  1 
ATOM   2314 H HG3  B ARG   A 1 169 ? 6.428   8.120  36.441 0.32 34.97 ? 149 ARG   A HG3  1 
ATOM   2315 H HD2  A ARG   A 1 169 ? 5.761   5.660  37.377 0.68 33.95 ? 149 ARG   A HD2  1 
ATOM   2316 H HD2  B ARG   A 1 169 ? 4.821   6.759  36.959 0.32 38.66 ? 149 ARG   A HD2  1 
ATOM   2317 H HD3  A ARG   A 1 169 ? 5.509   6.241  38.834 0.68 33.95 ? 149 ARG   A HD3  1 
ATOM   2318 H HD3  B ARG   A 1 169 ? 5.814   5.764  37.699 0.32 38.66 ? 149 ARG   A HD3  1 
ATOM   2319 H HE   A ARG   A 1 169 ? 4.402   7.201  36.565 0.68 43.00 ? 149 ARG   A HE   1 
ATOM   2320 H HE   B ARG   A 1 169 ? 5.262   6.696  39.610 0.32 41.81 ? 149 ARG   A HE   1 
ATOM   2321 H HH11 A ARG   A 1 169 ? 4.734   7.819  39.810 0.68 52.58 ? 149 ARG   A HH11 1 
ATOM   2322 H HH11 B ARG   A 1 169 ? 3.869   8.556  37.239 0.32 49.55 ? 149 ARG   A HH11 1 
ATOM   2323 H HH12 A ARG   A 1 169 ? 3.649   8.837  39.880 0.68 52.58 ? 149 ARG   A HH12 1 
ATOM   2324 H HH12 B ARG   A 1 169 ? 3.074   9.409  38.167 0.32 49.55 ? 149 ARG   A HH12 1 
ATOM   2325 H HH21 A ARG   A 1 169 ? 2.809   8.783  36.698 0.68 46.25 ? 149 ARG   A HH21 1 
ATOM   2326 H HH21 B ARG   A 1 169 ? 4.071   8.016  40.983 0.32 47.14 ? 149 ARG   A HH21 1 
ATOM   2327 H HH22 A ARG   A 1 169 ? 2.489   9.419  38.006 0.68 46.25 ? 149 ARG   A HH22 1 
ATOM   2328 H HH22 B ARG   A 1 169 ? 3.195   9.085  40.426 0.32 47.14 ? 149 ARG   A HH22 1 
ATOM   2329 N N    . SER   A 1 170 ? 10.006  6.670  34.333 1.00 19.62 ? 150 SER   A N    1 
ATOM   2330 C CA   . SER   A 1 170 ? 10.822  5.852  33.446 1.00 20.41 ? 150 SER   A CA   1 
ATOM   2331 C C    . SER   A 1 170 ? 12.299  6.174  33.593 1.00 20.60 ? 150 SER   A C    1 
ATOM   2332 O O    . SER   A 1 170 ? 13.131  5.324  33.285 1.00 21.61 ? 150 SER   A O    1 
ATOM   2333 C CB   . SER   A 1 170 ? 10.383  6.035  31.989 1.00 21.11 ? 150 SER   A CB   1 
ATOM   2334 O OG   . SER   A 1 170 ? 10.873  7.231  31.390 1.00 21.42 ? 150 SER   A OG   1 
ATOM   2335 H H    A SER   A 1 170 ? 9.490   7.226  33.927 0.68 23.54 ? 150 SER   A H    1 
ATOM   2336 H H    B SER   A 1 170 ? 9.460   7.202  33.936 0.32 23.54 ? 150 SER   A H    1 
ATOM   2337 H HA   . SER   A 1 170 ? 10.690  4.917  33.669 1.00 24.49 ? 150 SER   A HA   1 
ATOM   2338 H HB2  . SER   A 1 170 ? 10.712  5.281  31.475 1.00 25.33 ? 150 SER   A HB2  1 
ATOM   2339 H HB3  . SER   A 1 170 ? 9.414   6.056  31.964 1.00 25.33 ? 150 SER   A HB3  1 
ATOM   2340 H HG   . SER   A 1 170 ? 10.611  7.899  31.827 1.00 25.71 ? 150 SER   A HG   1 
ATOM   2341 N N    . LEU   A 1 171 ? 12.626  7.383  34.039 1.00 19.64 ? 151 LEU   A N    1 
ATOM   2342 C CA   . LEU   A 1 171 ? 13.992  7.844  34.224 1.00 20.22 ? 151 LEU   A CA   1 
ATOM   2343 C C    . LEU   A 1 171 ? 14.474  7.678  35.652 1.00 20.66 ? 151 LEU   A C    1 
ATOM   2344 O O    . LEU   A 1 171 ? 15.614  8.047  35.949 1.00 22.45 ? 151 LEU   A O    1 
ATOM   2345 C CB   . LEU   A 1 171 ? 14.070  9.317  33.833 1.00 20.38 ? 151 LEU   A CB   1 
ATOM   2346 C CG   . LEU   A 1 171 ? 13.831  9.598  32.361 1.00 20.81 ? 151 LEU   A CG   1 
ATOM   2347 C CD1  . LEU   A 1 171 ? 13.717  11.107 32.169 1.00 22.58 ? 151 LEU   A CD1  1 
ATOM   2348 C CD2  . LEU   A 1 171 ? 14.964  9.046  31.505 1.00 22.32 ? 151 LEU   A CD2  1 
ATOM   2349 H H    . LEU   A 1 171 ? 12.044  7.980  34.250 1.00 23.57 ? 151 LEU   A H    1 
ATOM   2350 H HA   . LEU   A 1 171 ? 14.586  7.333  33.651 1.00 24.27 ? 151 LEU   A HA   1 
ATOM   2351 H HB2  . LEU   A 1 171 ? 13.399  9.805  34.337 1.00 24.46 ? 151 LEU   A HB2  1 
ATOM   2352 H HB3  . LEU   A 1 171 ? 14.955  9.647  34.054 1.00 24.46 ? 151 LEU   A HB3  1 
ATOM   2353 H HG   . LEU   A 1 171 ? 13.012  9.163  32.074 1.00 24.97 ? 151 LEU   A HG   1 
ATOM   2354 H HD11 . LEU   A 1 171 ? 13.542  11.294 31.233 1.00 27.10 ? 151 LEU   A HD11 1 
ATOM   2355 H HD12 . LEU   A 1 171 ? 12.989  11.441 32.715 1.00 27.10 ? 151 LEU   A HD12 1 
ATOM   2356 H HD13 . LEU   A 1 171 ? 14.551  11.523 32.438 1.00 27.10 ? 151 LEU   A HD13 1 
ATOM   2357 H HD21 . LEU   A 1 171 ? 14.852  9.360  30.594 1.00 26.78 ? 151 LEU   A HD21 1 
ATOM   2358 H HD22 . LEU   A 1 171 ? 15.810  9.359  31.861 1.00 26.78 ? 151 LEU   A HD22 1 
ATOM   2359 H HD23 . LEU   A 1 171 ? 14.934  8.077  31.527 1.00 26.78 ? 151 LEU   A HD23 1 
ATOM   2360 N N    . GLY   A 1 172 ? 13.649  7.103  36.528 1.00 20.94 ? 152 GLY   A N    1 
ATOM   2361 C CA   . GLY   A 1 172 ? 14.029  6.945  37.921 1.00 22.08 ? 152 GLY   A CA   1 
ATOM   2362 C C    . GLY   A 1 172 ? 13.964  8.214  38.745 1.00 23.16 ? 152 GLY   A C    1 
ATOM   2363 O O    . GLY   A 1 172 ? 14.519  8.262  39.845 1.00 26.18 ? 152 GLY   A O    1 
ATOM   2364 H H    . GLY   A 1 172 ? 12.867  6.799  36.337 1.00 25.13 ? 152 GLY   A H    1 
ATOM   2365 H HA2  . GLY   A 1 172 ? 13.439  6.295  38.333 1.00 26.50 ? 152 GLY   A HA2  1 
ATOM   2366 H HA3  . GLY   A 1 172 ? 14.940  6.614  37.959 1.00 26.50 ? 152 GLY   A HA3  1 
ATOM   2367 N N    . ILE   A 1 173 ? 13.303  9.248  38.231 1.00 22.42 ? 153 ILE   A N    1 
ATOM   2368 C CA   . ILE   A 1 173 ? 13.163  10.527 38.913 1.00 22.81 ? 153 ILE   A CA   1 
ATOM   2369 C C    . ILE   A 1 173 ? 11.957  10.438 39.839 1.00 23.72 ? 153 ILE   A C    1 
ATOM   2370 O O    . ILE   A 1 173 ? 10.868  10.014 39.429 1.00 23.61 ? 153 ILE   A O    1 
ATOM   2371 C CB   . ILE   A 1 173 ? 12.978  11.652 37.874 1.00 22.81 ? 153 ILE   A CB   1 
ATOM   2372 C CG1  . ILE   A 1 173 ? 14.224  11.772 36.965 1.00 22.85 ? 153 ILE   A CG1  1 
ATOM   2373 C CG2  . ILE   A 1 173 ? 12.659  12.963 38.577 1.00 23.98 ? 153 ILE   A CG2  1 
ATOM   2374 C CD1  . ILE   A 1 173 ? 14.024  12.716 35.815 1.00 23.54 ? 153 ILE   A CD1  1 
ATOM   2375 H H    . ILE   A 1 173 ? 12.915  9.231  37.464 1.00 26.91 ? 153 ILE   A H    1 
ATOM   2376 H HA   . ILE   A 1 173 ? 13.950  10.716 39.448 1.00 27.37 ? 153 ILE   A HA   1 
ATOM   2377 H HB   . ILE   A 1 173 ? 12.228  11.429 37.301 1.00 27.38 ? 153 ILE   A HB   1 
ATOM   2378 H HG12 . ILE   A 1 173 ? 14.969  12.098 37.494 1.00 27.43 ? 153 ILE   A HG12 1 
ATOM   2379 H HG13 . ILE   A 1 173 ? 14.433  10.897 36.601 1.00 27.43 ? 153 ILE   A HG13 1 
ATOM   2380 H HG21 . ILE   A 1 173 ? 12.714  13.688 37.934 1.00 28.78 ? 153 ILE   A HG21 1 
ATOM   2381 H HG22 . ILE   A 1 173 ? 11.763  12.915 38.945 1.00 28.78 ? 153 ILE   A HG22 1 
ATOM   2382 H HG23 . ILE   A 1 173 ? 13.303  13.104 39.289 1.00 28.78 ? 153 ILE   A HG23 1 
ATOM   2383 H HD11 . ILE   A 1 173 ? 14.733  12.580 35.168 1.00 28.25 ? 153 ILE   A HD11 1 
ATOM   2384 H HD12 . ILE   A 1 173 ? 13.163  12.537 35.406 1.00 28.25 ? 153 ILE   A HD12 1 
ATOM   2385 H HD13 . ILE   A 1 173 ? 14.049  13.627 36.147 1.00 28.25 ? 153 ILE   A HD13 1 
ATOM   2386 N N    . GLU   A 1 174 ? 12.135  10.854 41.086 1.00 25.71 ? 154 GLU   A N    1 
ATOM   2387 C CA   . GLU   A 1 174 ? 11.046  10.784 42.042 1.00 27.71 ? 154 GLU   A CA   1 
ATOM   2388 C C    . GLU   A 1 174 ? 9.932   11.753 41.681 1.00 26.58 ? 154 GLU   A C    1 
ATOM   2389 O O    . GLU   A 1 174 ? 10.178  12.918 41.356 1.00 27.61 ? 154 GLU   A O    1 
ATOM   2390 C CB   . GLU   A 1 174 ? 11.589  11.116 43.419 1.00 31.92 ? 154 GLU   A CB   1 
ATOM   2391 C CG   . GLU   A 1 174 ? 12.203  9.917  44.092 1.00 41.63 ? 154 GLU   A CG   1 
ATOM   2392 H H    . GLU   A 1 174 ? 12.869  11.178 41.398 1.00 30.85 ? 154 GLU   A H    1 
ATOM   2393 H HA   . GLU   A 1 174 ? 10.666  9.892  42.039 1.00 33.25 ? 154 GLU   A HA   1 
ATOM   2394 H HB2  . GLU   A 1 174 ? 12.272  11.799 43.335 1.00 38.30 ? 154 GLU   A HB2  1 
ATOM   2395 H HB3  . GLU   A 1 174 ? 10.864  11.438 43.977 1.00 38.30 ? 154 GLU   A HB3  1 
ATOM   2396 N N    . VAL   A 1 175 ? 8.700   11.258 41.706 1.00 25.00 ? 155 VAL   A N    1 
ATOM   2397 C CA   . VAL   A 1 175 ? 7.534   12.072 41.376 1.00 24.81 ? 155 VAL   A CA   1 
ATOM   2398 C C    . VAL   A 1 175 ? 6.966   12.637 42.664 1.00 25.58 ? 155 VAL   A C    1 
ATOM   2399 O O    . VAL   A 1 175 ? 6.732   11.884 43.605 1.00 23.90 ? 155 VAL   A O    1 
ATOM   2400 C CB   . VAL   A 1 175 ? 6.471   11.240 40.646 1.00 26.14 ? 155 VAL   A CB   1 
ATOM   2401 C CG1  . VAL   A 1 175 ? 5.239   12.085 40.332 1.00 25.76 ? 155 VAL   A CG1  1 
ATOM   2402 C CG2  . VAL   A 1 175 ? 7.047   10.661 39.386 1.00 29.43 ? 155 VAL   A CG2  1 
ATOM   2403 H H    . VAL   A 1 175 ? 8.510   10.446 41.913 1.00 30.00 ? 155 VAL   A H    1 
ATOM   2404 H HA   . VAL   A 1 175 ? 7.808   12.803 40.801 1.00 29.77 ? 155 VAL   A HA   1 
ATOM   2405 H HB   . VAL   A 1 175 ? 6.192   10.512 41.223 1.00 31.37 ? 155 VAL   A HB   1 
ATOM   2406 H HG11 . VAL   A 1 175 ? 4.668   11.594 39.720 1.00 30.91 ? 155 VAL   A HG11 1 
ATOM   2407 H HG12 . VAL   A 1 175 ? 4.762   12.266 41.157 1.00 30.91 ? 155 VAL   A HG12 1 
ATOM   2408 H HG13 . VAL   A 1 175 ? 5.523   12.918 39.924 1.00 30.91 ? 155 VAL   A HG13 1 
ATOM   2409 H HG21 . VAL   A 1 175 ? 6.343   10.206 38.897 1.00 35.32 ? 155 VAL   A HG21 1 
ATOM   2410 H HG22 . VAL   A 1 175 ? 7.413   11.379 38.846 1.00 35.32 ? 155 VAL   A HG22 1 
ATOM   2411 H HG23 . VAL   A 1 175 ? 7.747   10.032 39.619 1.00 35.32 ? 155 VAL   A HG23 1 
ATOM   2412 N N    . PRO   A 1 176 ? 6.741   13.945 42.725 1.00 30.02 ? 156 PRO   A N    1 
ATOM   2413 C CA   . PRO   A 1 176 ? 6.044   14.553 43.863 1.00 33.23 ? 156 PRO   A CA   1 
ATOM   2414 C C    . PRO   A 1 176 ? 4.682   13.906 44.115 1.00 31.18 ? 156 PRO   A C    1 
ATOM   2415 O O    . PRO   A 1 176 ? 3.985   13.500 43.186 1.00 28.52 ? 156 PRO   A O    1 
ATOM   2416 C CB   . PRO   A 1 176 ? 5.897   16.012 43.395 1.00 29.97 ? 156 PRO   A CB   1 
ATOM   2417 C CG   . PRO   A 1 176 ? 6.928   16.202 42.377 1.00 29.98 ? 156 PRO   A CG   1 
ATOM   2418 C CD   . PRO   A 1 176 ? 7.013   14.933 41.664 1.00 29.97 ? 156 PRO   A CD   1 
ATOM   2419 H HA   . PRO   A 1 176 ? 6.572   14.497 44.675 1.00 39.87 ? 156 PRO   A HA   1 
ATOM   2420 H HB2  . PRO   A 1 176 ? 5.013   16.149 43.020 1.00 35.97 ? 156 PRO   A HB2  1 
ATOM   2421 H HB3  . PRO   A 1 176 ? 6.037   16.613 44.144 1.00 35.97 ? 156 PRO   A HB3  1 
ATOM   2422 H HG2  . PRO   A 1 176 ? 6.669   16.918 41.776 1.00 35.97 ? 156 PRO   A HG2  1 
ATOM   2423 H HG3  . PRO   A 1 176 ? 7.774   16.416 42.802 1.00 35.97 ? 156 PRO   A HG3  1 
ATOM   2424 H HD2  . PRO   A 1 176 ? 6.344   14.883 40.963 1.00 35.97 ? 156 PRO   A HD2  1 
ATOM   2425 H HD3  . PRO   A 1 176 ? 7.897   14.804 41.288 1.00 35.97 ? 156 PRO   A HD3  1 
ATOM   2426 N N    . GLU   A 1 177 ? 4.298   13.806 45.385 1.00 33.62 ? 157 GLU   A N    1 
ATOM   2427 C CA   . GLU   A 1 177 ? 3.023   13.201 45.762 1.00 34.38 ? 157 GLU   A CA   1 
ATOM   2428 C C    . GLU   A 1 177 ? 2.147   14.271 46.391 1.00 31.76 ? 157 GLU   A C    1 
ATOM   2429 O O    . GLU   A 1 177 ? 2.461   14.771 47.476 1.00 33.41 ? 157 GLU   A O    1 
ATOM   2430 C CB   . GLU   A 1 177 ? 3.228   12.044 46.742 1.00 38.29 ? 157 GLU   A CB   1 
ATOM   2431 C CG   . GLU   A 1 177 ? 1.953   11.368 47.219 1.00 39.54 ? 157 GLU   A CG   1 
ATOM   2432 H H    . GLU   A 1 177 ? 4.763   14.083 46.052 1.00 40.35 ? 157 GLU   A H    1 
ATOM   2433 H HA   . GLU   A 1 177 ? 2.583   12.858 44.968 1.00 41.26 ? 157 GLU   A HA   1 
ATOM   2434 H HB2  . GLU   A 1 177 ? 3.770   11.367 46.308 1.00 45.96 ? 157 GLU   A HB2  1 
ATOM   2435 H HB3  . GLU   A 1 177 ? 3.686   12.383 47.526 1.00 45.96 ? 157 GLU   A HB3  1 
ATOM   2436 N N    . VAL   A 1 178 ? 1.022   14.570 45.749 1.00 26.67 ? 158 VAL   A N    1 
ATOM   2437 C CA   . VAL   A 1 178 ? 0.059   15.490 46.344 1.00 25.58 ? 158 VAL   A CA   1 
ATOM   2438 C C    . VAL   A 1 178 ? -0.623  14.793 47.524 1.00 24.53 ? 158 VAL   A C    1 
ATOM   2439 O O    . VAL   A 1 178 ? -1.132  13.670 47.402 1.00 28.02 ? 158 VAL   A O    1 
ATOM   2440 C CB   . VAL   A 1 178 ? -0.964  15.918 45.283 1.00 27.03 ? 158 VAL   A CB   1 
ATOM   2441 C CG1  . VAL   A 1 178 ? -2.066  16.774 45.879 1.00 28.10 ? 158 VAL   A CG1  1 
ATOM   2442 C CG2  . VAL   A 1 178 ? -0.275  16.694 44.153 1.00 27.86 ? 158 VAL   A CG2  1 
ATOM   2443 H H    . VAL   A 1 178 ? 0.796   14.259 44.980 1.00 32.01 ? 158 VAL   A H    1 
ATOM   2444 H HA   . VAL   A 1 178 ? 0.513   16.280 46.675 1.00 30.69 ? 158 VAL   A HA   1 
ATOM   2445 H HB   . VAL   A 1 178 ? -1.367  15.112 44.923 1.00 32.44 ? 158 VAL   A HB   1 
ATOM   2446 H HG11 . VAL   A 1 178 ? -2.569  17.188 45.160 1.00 33.72 ? 158 VAL   A HG11 1 
ATOM   2447 H HG12 . VAL   A 1 178 ? -2.652  16.211 46.409 1.00 33.72 ? 158 VAL   A HG12 1 
ATOM   2448 H HG13 . VAL   A 1 178 ? -1.667  17.457 46.440 1.00 33.72 ? 158 VAL   A HG13 1 
ATOM   2449 H HG21 . VAL   A 1 178 ? -0.944  16.976 43.509 1.00 33.44 ? 158 VAL   A HG21 1 
ATOM   2450 H HG22 . VAL   A 1 178 ? 0.171   17.469 44.528 1.00 33.44 ? 158 VAL   A HG22 1 
ATOM   2451 H HG23 . VAL   A 1 178 ? 0.374   16.115 43.723 1.00 33.44 ? 158 VAL   A HG23 1 
ATOM   2452 N N    . ARG   A 1 179 ? -0.667  15.461 48.672 1.00 22.87 ? 159 ARG   A N    1 
ATOM   2453 C CA   . ARG   A 1 179 ? -1.320  14.878 49.840 1.00 24.24 ? 159 ARG   A CA   1 
ATOM   2454 C C    . ARG   A 1 179 ? -2.832  14.941 49.652 1.00 25.14 ? 159 ARG   A C    1 
ATOM   2455 O O    . ARG   A 1 179 ? -3.383  16.013 49.394 1.00 26.21 ? 159 ARG   A O    1 
ATOM   2456 C CB   . ARG   A 1 179 ? -0.926  15.650 51.098 1.00 25.73 ? 159 ARG   A CB   1 
ATOM   2457 C CG   . ARG   A 1 179 ? 0.553   15.627 51.465 1.00 29.40 ? 159 ARG   A CG   1 
ATOM   2458 C CD   . ARG   A 1 179 ? 0.823   16.377 52.792 1.00 32.85 ? 159 ARG   A CD   1 
ATOM   2459 N NE   . ARG   A 1 179 ? 0.535   17.811 52.707 1.00 34.28 ? 159 ARG   A NE   1 
ATOM   2460 C CZ   . ARG   A 1 179 ? 1.414   18.732 52.323 1.00 36.71 ? 159 ARG   A CZ   1 
ATOM   2461 N NH1  . ARG   A 1 179 ? 2.644   18.401 51.953 1.00 36.27 ? 159 ARG   A NH1  1 
ATOM   2462 N NH2  . ARG   A 1 179 ? 1.056   20.014 52.317 1.00 37.82 ? 159 ARG   A NH2  1 
ATOM   2463 H H    . ARG   A 1 179 ? -0.331  16.242 48.800 1.00 27.44 ? 159 ARG   A H    1 
ATOM   2464 H HA   . ARG   A 1 179 ? -1.046  13.954 49.948 1.00 29.09 ? 159 ARG   A HA   1 
ATOM   2465 H HB2  . ARG   A 1 179 ? -1.175  16.579 50.974 1.00 30.87 ? 159 ARG   A HB2  1 
ATOM   2466 H HB3  . ARG   A 1 179 ? -1.412  15.274 51.848 1.00 30.87 ? 159 ARG   A HB3  1 
ATOM   2467 H HG2  . ARG   A 1 179 ? 0.843   14.708 51.571 1.00 35.29 ? 159 ARG   A HG2  1 
ATOM   2468 H HG3  . ARG   A 1 179 ? 1.065   16.058 50.763 1.00 35.29 ? 159 ARG   A HG3  1 
ATOM   2469 H HD2  . ARG   A 1 179 ? 0.262   16.001 53.487 1.00 39.43 ? 159 ARG   A HD2  1 
ATOM   2470 H HD3  . ARG   A 1 179 ? 1.758   16.274 53.028 1.00 39.43 ? 159 ARG   A HD3  1 
ATOM   2471 H HE   . ARG   A 1 179 ? -0.255  18.075 52.920 1.00 41.14 ? 159 ARG   A HE   1 
ATOM   2472 H HH11 . ARG   A 1 179 ? 2.887   17.577 51.958 1.00 43.53 ? 159 ARG   A HH11 1 
ATOM   2473 H HH12 . ARG   A 1 179 ? 3.197   19.012 51.708 1.00 43.53 ? 159 ARG   A HH12 1 
ATOM   2474 H HH21 . ARG   A 1 179 ? 0.263   20.240 52.560 1.00 45.38 ? 159 ARG   A HH21 1 
ATOM   2475 H HH22 . ARG   A 1 179 ? 1.618   20.616 52.070 1.00 45.38 ? 159 ARG   A HH22 1 
ATOM   2476 N N    . ARG   A 1 180 ? -3.511  13.802 49.784 1.00 25.47 ? 160 ARG   A N    1 
ATOM   2477 C CA   . ARG   A 1 180 ? -4.946  13.718 49.510 1.00 26.73 ? 160 ARG   A CA   1 
ATOM   2478 C C    . ARG   A 1 180 ? -5.789  13.509 50.765 1.00 26.38 ? 160 ARG   A C    1 
ATOM   2479 O O    . ARG   A 1 180 ? -7.002  13.300 50.658 1.00 27.20 ? 160 ARG   A O    1 
ATOM   2480 C CB   . ARG   A 1 180 ? -5.200  12.629 48.463 1.00 26.60 ? 160 ARG   A CB   1 
ATOM   2481 C CG   . ARG   A 1 180 ? -4.411  12.855 47.149 1.00 29.66 ? 160 ARG   A CG   1 
ATOM   2482 C CD   . ARG   A 1 180 ? -4.866  11.905 46.056 1.00 31.12 ? 160 ARG   A CD   1 
ATOM   2483 N NE   . ARG   A 1 180 ? -3.958  11.909 44.914 1.00 30.02 ? 160 ARG   A NE   1 
ATOM   2484 C CZ   . ARG   A 1 180 ? -4.198  11.261 43.786 1.00 31.49 ? 160 ARG   A CZ   1 
ATOM   2485 N NH1  . ARG   A 1 180 ? -5.327  10.598 43.604 1.00 34.03 ? 160 ARG   A NH1  1 
ATOM   2486 N NH2  . ARG   A 1 180 ? -3.284  11.272 42.824 1.00 31.45 ? 160 ARG   A NH2  1 
ATOM   2487 H H    . ARG   A 1 180 ? -3.160  13.057 50.032 1.00 30.57 ? 160 ARG   A H    1 
ATOM   2488 H HA   . ARG   A 1 180 ? -5.247  14.559 49.133 1.00 32.08 ? 160 ARG   A HA   1 
ATOM   2489 H HB2  . ARG   A 1 180 ? -4.932  11.771 48.829 1.00 31.92 ? 160 ARG   A HB2  1 
ATOM   2490 H HB3  . ARG   A 1 180 ? -6.146  12.616 48.245 1.00 31.92 ? 160 ARG   A HB3  1 
ATOM   2491 H HG2  . ARG   A 1 180 ? -4.552  13.764 46.842 1.00 35.59 ? 160 ARG   A HG2  1 
ATOM   2492 H HG3  . ARG   A 1 180 ? -3.466  12.703 47.312 1.00 35.59 ? 160 ARG   A HG3  1 
ATOM   2493 H HD2  . ARG   A 1 180 ? -4.901  11.003 46.411 1.00 37.35 ? 160 ARG   A HD2  1 
ATOM   2494 H HD3  . ARG   A 1 180 ? -5.744  12.174 45.745 1.00 37.35 ? 160 ARG   A HD3  1 
ATOM   2495 H HE   . ARG   A 1 180 ? -3.227  12.358 44.978 1.00 36.03 ? 160 ARG   A HE   1 
ATOM   2496 H HH11 . ARG   A 1 180 ? -5.921  10.583 44.226 1.00 40.83 ? 160 ARG   A HH11 1 
ATOM   2497 H HH12 . ARG   A 1 180 ? -5.467  10.182 42.865 1.00 40.83 ? 160 ARG   A HH12 1 
ATOM   2498 H HH21 . ARG   A 1 180 ? -2.545  11.697 42.937 1.00 37.74 ? 160 ARG   A HH21 1 
ATOM   2499 H HH22 . ARG   A 1 180 ? -3.431  10.853 42.087 1.00 37.74 ? 160 ARG   A HH22 1 
ATOM   2500 N N    . ASP   A 1 181 ? -5.182  13.586 51.947 1.00 27.21 ? 161 ASP   A N    1 
ATOM   2501 C CA   . ASP   A 1 181 ? -5.915  13.266 53.167 1.00 28.25 ? 161 ASP   A CA   1 
ATOM   2502 C C    . ASP   A 1 181 ? -7.139  14.150 53.331 1.00 28.38 ? 161 ASP   A C    1 
ATOM   2503 O O    . ASP   A 1 181 ? -8.190  13.707 53.830 1.00 30.41 ? 161 ASP   A O    1 
ATOM   2504 C CB   . ASP   A 1 181 ? -4.968  13.457 54.342 1.00 31.81 ? 161 ASP   A CB   1 
ATOM   2505 C CG   . ASP   A 1 181 ? -3.682  12.708 54.150 1.00 36.71 ? 161 ASP   A CG   1 
ATOM   2506 O OD1  . ASP   A 1 181 ? -3.677  11.510 54.511 1.00 40.70 ? 161 ASP   A OD1  1 
ATOM   2507 O OD2  . ASP   A 1 181 ? -2.715  13.282 53.568 1.00 36.40 ? 161 ASP   A OD2  1 
ATOM   2508 H H    . ASP   A 1 181 ? -4.362  13.817 52.067 1.00 32.66 ? 161 ASP   A H    1 
ATOM   2509 H HA   . ASP   A 1 181 ? -6.224  12.347 53.136 1.00 33.90 ? 161 ASP   A HA   1 
ATOM   2510 H HB2  . ASP   A 1 181 ? -4.759  14.400 54.435 1.00 38.17 ? 161 ASP   A HB2  1 
ATOM   2511 H HB3  . ASP   A 1 181 ? -5.392  13.131 55.151 1.00 38.17 ? 161 ASP   A HB3  1 
ATOM   2512 N N    . GLY   A 1 182 ? -7.023  15.403 52.938 1.00 27.58 ? 162 GLY   A N    1 
ATOM   2513 C CA   . GLY   A 1 182 ? -8.112  16.322 53.137 1.00 28.14 ? 162 GLY   A CA   1 
ATOM   2514 C C    . GLY   A 1 182 ? -9.177  16.291 52.081 1.00 28.09 ? 162 GLY   A C    1 
ATOM   2515 O O    . GLY   A 1 182 ? -10.142 17.051 52.181 1.00 28.56 ? 162 GLY   A O    1 
ATOM   2516 H H    . GLY   A 1 182 ? -6.328  15.738 52.558 1.00 33.10 ? 162 GLY   A H    1 
ATOM   2517 H HA2  . GLY   A 1 182 ? -8.534  16.120 53.987 1.00 33.77 ? 162 GLY   A HA2  1 
ATOM   2518 H HA3  . GLY   A 1 182 ? -7.754  17.223 53.167 1.00 33.77 ? 162 GLY   A HA3  1 
ATOM   2519 N N    . LEU   A 1 183 ? -9.047  15.425 51.087 1.00 29.73 ? 163 LEU   A N    1 
ATOM   2520 C CA   . LEU   A 1 183 ? -9.936  15.352 49.945 1.00 31.95 ? 163 LEU   A CA   1 
ATOM   2521 C C    . LEU   A 1 183 ? -10.864 14.155 50.067 1.00 35.57 ? 163 LEU   A C    1 
ATOM   2522 O O    . LEU   A 1 183 ? -10.519 13.156 50.707 1.00 35.56 ? 163 LEU   A O    1 
ATOM   2523 C CB   . LEU   A 1 183 ? -9.104  15.185 48.670 1.00 33.55 ? 163 LEU   A CB   1 
ATOM   2524 C CG   . LEU   A 1 183 ? -8.041  16.244 48.338 1.00 35.75 ? 163 LEU   A CG   1 
ATOM   2525 C CD1  . LEU   A 1 183 ? -7.137  15.838 47.147 1.00 37.75 ? 163 LEU   A CD1  1 
ATOM   2526 C CD2  . LEU   A 1 183 ? -8.720  17.577 48.054 1.00 37.97 ? 163 LEU   A CD2  1 
ATOM   2527 H H    . LEU   A 1 183 ? -8.418  14.839 51.051 1.00 35.68 ? 163 LEU   A H    1 
ATOM   2528 H HA   . LEU   A 1 183 ? -10.472 16.158 49.886 1.00 38.34 ? 163 LEU   A HA   1 
ATOM   2529 H HB2  . LEU   A 1 183 ? -8.638  14.337 48.736 1.00 40.27 ? 163 LEU   A HB2  1 
ATOM   2530 H HB3  . LEU   A 1 183 ? -9.720  15.168 47.921 1.00 40.27 ? 163 LEU   A HB3  1 
ATOM   2531 H HG   . LEU   A 1 183 ? -7.455  16.330 49.106 1.00 42.90 ? 163 LEU   A HG   1 
ATOM   2532 H HD11 . LEU   A 1 183 ? -6.390  16.455 47.093 1.00 45.31 ? 163 LEU   A HD11 1 
ATOM   2533 H HD12 . LEU   A 1 183 ? -6.810  14.936 47.292 1.00 45.31 ? 163 LEU   A HD12 1 
ATOM   2534 H HD13 . LEU   A 1 183 ? -7.657  15.874 46.329 1.00 45.31 ? 163 LEU   A HD13 1 
ATOM   2535 H HD21 . LEU   A 1 183 ? -8.046  18.230 47.812 1.00 45.56 ? 163 LEU   A HD21 1 
ATOM   2536 H HD22 . LEU   A 1 183 ? -9.348  17.463 47.324 1.00 45.56 ? 163 LEU   A HD22 1 
ATOM   2537 H HD23 . LEU   A 1 183 ? -9.191  17.868 48.852 1.00 45.56 ? 163 LEU   A HD23 1 
ATOM   2538 N N    . PRO   A 1 184 ? -12.061 14.233 49.462 1.00 39.47 ? 164 PRO   A N    1 
ATOM   2539 C CA   . PRO   A 1 184 ? -13.003 13.114 49.480 1.00 42.29 ? 164 PRO   A CA   1 
ATOM   2540 C C    . PRO   A 1 184 ? -12.414 11.846 48.877 1.00 45.80 ? 164 PRO   A C    1 
ATOM   2541 O O    . PRO   A 1 184 ? -11.637 11.975 47.921 1.00 46.79 ? 164 PRO   A O    1 
ATOM   2542 C CB   . PRO   A 1 184 ? -14.156 13.625 48.610 1.00 42.30 ? 164 PRO   A CB   1 
ATOM   2543 C CG   . PRO   A 1 184 ? -14.072 15.104 48.666 1.00 43.52 ? 164 PRO   A CG   1 
ATOM   2544 C CD   . PRO   A 1 184 ? -12.617 15.405 48.754 1.00 42.66 ? 164 PRO   A CD   1 
ATOM   2545 H HA   . PRO   A 1 184 ? -13.313 12.936 50.382 1.00 50.75 ? 164 PRO   A HA   1 
ATOM   2546 H HB2  . PRO   A 1 184 ? -14.046 13.307 47.700 1.00 50.77 ? 164 PRO   A HB2  1 
ATOM   2547 H HB3  . PRO   A 1 184 ? -15.001 13.314 48.970 1.00 50.77 ? 164 PRO   A HB3  1 
ATOM   2548 H HG2  . PRO   A 1 184 ? -14.457 15.488 47.862 1.00 52.23 ? 164 PRO   A HG2  1 
ATOM   2549 H HG3  . PRO   A 1 184 ? -14.542 15.433 49.448 1.00 52.23 ? 164 PRO   A HG3  1 
ATOM   2550 H HD2  . PRO   A 1 184 ? -12.229 15.488 47.868 1.00 51.19 ? 164 PRO   A HD2  1 
ATOM   2551 H HD3  . PRO   A 1 184 ? -12.464 16.218 49.260 1.00 51.19 ? 164 PRO   A HD3  1 
ATOM   2552 N N    . GLU   B 1 32  ? -29.728 7.735  8.216  1.00 59.06 ? 12  GLU   B N    1 
ATOM   2553 C CA   . GLU   B 1 32  ? -28.492 7.571  8.978  1.00 57.12 ? 12  GLU   B CA   1 
ATOM   2554 C C    . GLU   B 1 32  ? -27.756 8.904  9.141  1.00 53.86 ? 12  GLU   B C    1 
ATOM   2555 O O    . GLU   B 1 32  ? -27.419 9.302  10.260 1.00 49.93 ? 12  GLU   B O    1 
ATOM   2556 C CB   . GLU   B 1 32  ? -27.579 6.548  8.289  1.00 59.32 ? 12  GLU   B CB   1 
ATOM   2557 H HA   . GLU   B 1 32  ? -28.708 7.242  9.865  1.00 68.55 ? 12  GLU   B HA   1 
ATOM   2558 N N    . ASN   B 1 33  ? -27.512 9.589  8.017  1.00 54.33 ? 13  ASN   B N    1 
ATOM   2559 C CA   . ASN   B 1 33  ? -26.823 10.875 8.067  1.00 52.11 ? 13  ASN   B CA   1 
ATOM   2560 C C    . ASN   B 1 33  ? -27.633 11.895 8.857  1.00 47.93 ? 13  ASN   B C    1 
ATOM   2561 O O    . ASN   B 1 33  ? -27.074 12.687 9.624  1.00 45.81 ? 13  ASN   B O    1 
ATOM   2562 C CB   . ASN   B 1 33  ? -26.565 11.402 6.654  1.00 53.97 ? 13  ASN   B CB   1 
ATOM   2563 H H    . ASN   B 1 33  ? -27.732 9.333  7.226  1.00 65.20 ? 13  ASN   B H    1 
ATOM   2564 H HA   . ASN   B 1 33  ? -25.966 10.747 8.504  1.00 62.54 ? 13  ASN   B HA   1 
ATOM   2565 N N    . ARG   B 1 34  ? -28.956 11.903 8.668  1.00 45.99 ? 14  ARG   B N    1 
ATOM   2566 C CA   . ARG   B 1 34  ? -29.794 12.843 9.401  1.00 43.13 ? 14  ARG   B CA   1 
ATOM   2567 C C    . ARG   B 1 34  ? -29.717 12.589 10.898 1.00 36.62 ? 14  ARG   B C    1 
ATOM   2568 O O    . ARG   B 1 34  ? -29.687 13.533 11.689 1.00 37.11 ? 14  ARG   B O    1 
ATOM   2569 C CB   . ARG   B 1 34  ? -31.250 12.749 8.945  1.00 45.86 ? 14  ARG   B CB   1 
ATOM   2570 H H    . ARG   B 1 34  ? -29.382 11.384 8.130  1.00 55.19 ? 14  ARG   B H    1 
ATOM   2571 H HA   . ARG   B 1 34  ? -29.475 13.740 9.211  1.00 51.76 ? 14  ARG   B HA   1 
ATOM   2572 N N    . ALA   B 1 35  ? -29.715 11.320 11.307 1.00 32.59 ? 15  ALA   B N    1 
ATOM   2573 C CA   . ALA   B 1 35  ? -29.608 11.010 12.726 1.00 30.14 ? 15  ALA   B CA   1 
ATOM   2574 C C    . ALA   B 1 35  ? -28.237 11.403 13.279 1.00 27.76 ? 15  ALA   B C    1 
ATOM   2575 O O    . ALA   B 1 35  ? -28.131 11.855 14.422 1.00 27.79 ? 15  ALA   B O    1 
ATOM   2576 C CB   . ALA   B 1 35  ? -29.844 9.522  12.950 1.00 31.34 ? 15  ALA   B CB   1 
ATOM   2577 H H    . ALA   B 1 35  ? -29.773 10.635 10.791 1.00 39.11 ? 15  ALA   B H    1 
ATOM   2578 H HA   . ALA   B 1 35  ? -30.288 11.510 13.204 1.00 36.17 ? 15  ALA   B HA   1 
ATOM   2579 H HB1  . ALA   B 1 35  ? -29.764 9.329  13.897 1.00 37.61 ? 15  ALA   B HB1  1 
ATOM   2580 H HB2  . ALA   B 1 35  ? -30.734 9.294  12.639 1.00 37.61 ? 15  ALA   B HB2  1 
ATOM   2581 H HB3  . ALA   B 1 35  ? -29.181 9.019  12.452 1.00 37.61 ? 15  ALA   B HB3  1 
ATOM   2582 N N    . GLN   B 1 36  ? -27.178 11.227 12.488 1.00 32.03 ? 16  GLN   B N    1 
ATOM   2583 C CA   . GLN   B 1 36  ? -25.854 11.637 12.936 1.00 34.90 ? 16  GLN   B CA   1 
ATOM   2584 C C    . GLN   B 1 36  ? -25.756 13.153 13.049 1.00 33.77 ? 16  GLN   B C    1 
ATOM   2585 O O    . GLN   B 1 36  ? -25.185 13.678 14.014 1.00 33.09 ? 16  GLN   B O    1 
ATOM   2586 C CB   . GLN   B 1 36  ? -24.794 11.085 11.984 1.00 39.63 ? 16  GLN   B CB   1 
ATOM   2587 C CG   . GLN   B 1 36  ? -24.480 9.608  12.196 0.80 44.90 ? 16  GLN   B CG   1 
ATOM   2588 C CD   . GLN   B 1 36  ? -23.128 9.209  11.615 1.00 48.72 ? 16  GLN   B CD   1 
ATOM   2589 O OE1  . GLN   B 1 36  ? -22.910 9.301  10.410 0.43 49.70 ? 16  GLN   B OE1  1 
ATOM   2590 N NE2  . GLN   B 1 36  ? -22.213 8.777  12.475 0.36 48.86 ? 16  GLN   B NE2  1 
ATOM   2591 H H    . GLN   B 1 36  ? -27.202 10.878 11.702 1.00 38.43 ? 16  GLN   B H    1 
ATOM   2592 H HA   . GLN   B 1 36  ? -25.685 11.267 13.816 1.00 41.88 ? 16  GLN   B HA   1 
ATOM   2593 H HB2  . GLN   B 1 36  ? -25.108 11.193 11.073 1.00 47.55 ? 16  GLN   B HB2  1 
ATOM   2594 H HB3  . GLN   B 1 36  ? -23.971 11.583 12.113 1.00 47.55 ? 16  GLN   B HB3  1 
ATOM   2595 H HG2  . GLN   B 1 36  ? -24.466 9.420  13.148 0.80 53.88 ? 16  GLN   B HG2  1 
ATOM   2596 H HG3  . GLN   B 1 36  ? -25.163 9.073  11.763 0.80 53.88 ? 16  GLN   B HG3  1 
ATOM   2597 H HE21 . GLN   B 1 36  ? -22.399 8.733  13.313 0.36 58.63 ? 16  GLN   B HE21 1 
ATOM   2598 H HE22 . GLN   B 1 36  ? -21.436 8.541  12.193 0.36 58.63 ? 16  GLN   B HE22 1 
ATOM   2599 N N    . VAL   B 1 37  ? -26.289 13.878 12.073 1.00 29.98 ? 17  VAL   B N    1 
ATOM   2600 C CA   . VAL   B 1 37  ? -26.247 15.337 12.137 1.00 29.98 ? 17  VAL   B CA   1 
ATOM   2601 C C    . VAL   B 1 37  ? -27.017 15.857 13.358 1.00 29.99 ? 17  VAL   B C    1 
ATOM   2602 O O    . VAL   B 1 37  ? -26.535 16.737 14.083 1.00 30.00 ? 17  VAL   B O    1 
ATOM   2603 C CB   . VAL   B 1 37  ? -26.734 15.959 10.816 1.00 29.99 ? 17  VAL   B CB   1 
ATOM   2604 C CG1  . VAL   B 1 37  ? -26.934 17.455 11.013 1.00 29.99 ? 17  VAL   B CG1  1 
ATOM   2605 C CG2  . VAL   B 1 37  ? -25.713 15.680 9.697  1.00 29.99 ? 17  VAL   B CG2  1 
ATOM   2606 H H    . VAL   B 1 37  ? -26.674 13.558 11.374 1.00 35.98 ? 17  VAL   B H    1 
ATOM   2607 H HA   . VAL   B 1 37  ? -25.323 15.607 12.255 1.00 35.98 ? 17  VAL   B HA   1 
ATOM   2608 H HB   . VAL   B 1 37  ? -27.580 15.567 10.551 1.00 35.99 ? 17  VAL   B HB   1 
ATOM   2609 H HG11 . VAL   B 1 37  ? -26.952 17.888 10.145 1.00 35.99 ? 17  VAL   B HG11 1 
ATOM   2610 H HG12 . VAL   B 1 37  ? -27.774 17.604 11.474 1.00 35.99 ? 17  VAL   B HG12 1 
ATOM   2611 H HG13 . VAL   B 1 37  ? -26.200 17.805 11.542 1.00 35.99 ? 17  VAL   B HG13 1 
ATOM   2612 H HG21 . VAL   B 1 37  ? -26.028 16.086 8.874  1.00 35.99 ? 17  VAL   B HG21 1 
ATOM   2613 H HG22 . VAL   B 1 37  ? -24.857 16.062 9.948  1.00 35.99 ? 17  VAL   B HG22 1 
ATOM   2614 H HG23 . VAL   B 1 37  ? -25.626 14.721 9.581  1.00 35.99 ? 17  VAL   B HG23 1 
ATOM   2615 N N    . ALA   B 1 38  ? -28.225 15.318 13.599 1.00 30.31 ? 18  ALA   B N    1 
ATOM   2616 C CA   . ALA   B 1 38  ? -29.017 15.733 14.752 1.00 31.10 ? 18  ALA   B CA   1 
ATOM   2617 C C    . ALA   B 1 38  ? -28.248 15.530 16.044 1.00 28.87 ? 18  ALA   B C    1 
ATOM   2618 O O    . ALA   B 1 38  ? -28.223 16.406 16.915 1.00 29.12 ? 18  ALA   B O    1 
ATOM   2619 C CB   . ALA   B 1 38  ? -30.301 14.908 14.792 1.00 32.08 ? 18  ALA   B CB   1 
ATOM   2620 H H    . ALA   B 1 38  ? -28.599 14.716 13.111 1.00 36.38 ? 18  ALA   B H    1 
ATOM   2621 H HA   . ALA   B 1 38  ? -29.234 16.675 14.666 1.00 37.33 ? 18  ALA   B HA   1 
ATOM   2622 H HB1  . ALA   B 1 38  ? -30.828 15.180 15.559 1.00 38.49 ? 18  ALA   B HB1  1 
ATOM   2623 H HB2  . ALA   B 1 38  ? -30.801 15.062 13.975 1.00 38.49 ? 18  ALA   B HB2  1 
ATOM   2624 H HB3  . ALA   B 1 38  ? -30.070 13.968 14.865 1.00 38.49 ? 18  ALA   B HB3  1 
ATOM   2625 N N    . ALA   B 1 39  ? -27.632 14.357 16.192 1.00 26.50 ? 19  ALA   B N    1 
ATOM   2626 C CA   . ALA   B 1 39  ? -26.886 14.049 17.404 1.00 26.93 ? 19  ALA   B CA   1 
ATOM   2627 C C    . ALA   B 1 39  ? -25.732 15.027 17.591 1.00 25.35 ? 19  ALA   B C    1 
ATOM   2628 O O    . ALA   B 1 39  ? -25.522 15.559 18.685 1.00 25.66 ? 19  ALA   B O    1 
ATOM   2629 C CB   . ALA   B 1 39  ? -26.380 12.603 17.368 1.00 29.55 ? 19  ALA   B CB   1 
ATOM   2630 H H    . ALA   B 1 39  ? -27.632 13.726 15.607 1.00 31.80 ? 19  ALA   B H    1 
ATOM   2631 H HA   . ALA   B 1 39  ? -27.479 14.131 18.167 1.00 32.31 ? 19  ALA   B HA   1 
ATOM   2632 H HB1  . ALA   B 1 39  ? -25.894 12.418 18.187 1.00 35.46 ? 19  ALA   B HB1  1 
ATOM   2633 H HB2  . ALA   B 1 39  ? -27.140 12.004 17.292 1.00 35.46 ? 19  ALA   B HB2  1 
ATOM   2634 H HB3  . ALA   B 1 39  ? -25.794 12.492 16.603 1.00 35.46 ? 19  ALA   B HB3  1 
ATOM   2635 N N    . ARG   B 1 40  ? -24.973 15.290 16.524 1.00 25.65 ? 20  ARG   B N    1 
ATOM   2636 C CA   . ARG   B 1 40  ? -23.801 16.151 16.658 1.00 25.13 ? 20  ARG   B CA   1 
ATOM   2637 C C    . ARG   B 1 40  ? -24.187 17.574 17.071 1.00 25.06 ? 20  ARG   B C    1 
ATOM   2638 O O    . ARG   B 1 40  ? -23.569 18.169 17.967 1.00 25.44 ? 20  ARG   B O    1 
ATOM   2639 C CB   . ARG   B 1 40  ? -23.012 16.148 15.347 1.00 26.67 ? 20  ARG   B CB   1 
ATOM   2640 C CG   . ARG   B 1 40  ? -21.708 16.826 15.481 1.00 26.63 ? 20  ARG   B CG   1 
ATOM   2641 C CD   . ARG   B 1 40  ? -20.859 16.793 14.200 1.00 27.14 ? 20  ARG   B CD   1 
ATOM   2642 N NE   . ARG   B 1 40  ? -20.228 15.501 13.952 1.00 28.02 ? 20  ARG   B NE   1 
ATOM   2643 C CZ   . ARG   B 1 40  ? -20.654 14.603 13.071 1.00 28.30 ? 20  ARG   B CZ   1 
ATOM   2644 N NH1  . ARG   B 1 40  ? -21.696 14.834 12.306 1.00 29.19 ? 20  ARG   B NH1  1 
ATOM   2645 N NH2  . ARG   B 1 40  ? -20.007 13.450 12.955 1.00 28.51 ? 20  ARG   B NH2  1 
ATOM   2646 H H    . ARG   B 1 40  ? -25.113 14.988 15.730 1.00 30.78 ? 20  ARG   B H    1 
ATOM   2647 H HA   . ARG   B 1 40  ? -23.228 15.799 17.357 1.00 30.16 ? 20  ARG   B HA   1 
ATOM   2648 H HB2  . ARG   B 1 40  ? -22.850 15.231 15.075 1.00 32.01 ? 20  ARG   B HB2  1 
ATOM   2649 H HB3  . ARG   B 1 40  ? -23.525 16.610 14.666 1.00 32.01 ? 20  ARG   B HB3  1 
ATOM   2650 H HG2  . ARG   B 1 40  ? -21.861 17.756 15.710 1.00 31.96 ? 20  ARG   B HG2  1 
ATOM   2651 H HG3  . ARG   B 1 40  ? -21.200 16.391 16.183 1.00 31.96 ? 20  ARG   B HG3  1 
ATOM   2652 H HD2  . ARG   B 1 40  ? -21.429 16.994 13.441 1.00 32.57 ? 20  ARG   B HD2  1 
ATOM   2653 H HD3  . ARG   B 1 40  ? -20.156 17.458 14.272 1.00 32.57 ? 20  ARG   B HD3  1 
ATOM   2654 H HE   . ARG   B 1 40  ? -19.527 15.307 14.412 1.00 33.63 ? 20  ARG   B HE   1 
ATOM   2655 H HH11 . ARG   B 1 40  ? -22.119 15.580 12.368 1.00 35.03 ? 20  ARG   B HH11 1 
ATOM   2656 H HH12 . ARG   B 1 40  ? -21.956 14.239 11.741 1.00 35.03 ? 20  ARG   B HH12 1 
ATOM   2657 H HH21 . ARG   B 1 40  ? -19.320 13.290 13.447 1.00 34.22 ? 20  ARG   B HH21 1 
ATOM   2658 H HH22 . ARG   B 1 40  ? -20.276 12.862 12.387 1.00 34.22 ? 20  ARG   B HH22 1 
ATOM   2659 N N    . GLN   B 1 41  ? -25.251 18.117 16.479 1.00 25.72 ? 21  GLN   B N    1 
ATOM   2660 C CA   . GLN   B 1 41  ? -25.636 19.485 16.808 1.00 26.27 ? 21  GLN   B CA   1 
ATOM   2661 C C    . GLN   B 1 41  ? -26.121 19.609 18.251 1.00 25.61 ? 21  GLN   B C    1 
ATOM   2662 O O    . GLN   B 1 41  ? -25.784 20.580 18.945 1.00 25.83 ? 21  GLN   B O    1 
ATOM   2663 C CB   . GLN   B 1 41  ? -26.745 19.938 15.869 1.00 28.40 ? 21  GLN   B CB   1 
ATOM   2664 C CG   . GLN   B 1 41  ? -26.327 20.030 14.406 1.00 42.48 ? 21  GLN   B CG   1 
ATOM   2665 C CD   . GLN   B 1 41  ? -27.517 20.192 13.468 1.00 48.28 ? 21  GLN   B CD   1 
ATOM   2666 O OE1  . GLN   B 1 41  ? -28.619 19.710 13.748 1.00 55.17 ? 21  GLN   B OE1  1 
ATOM   2667 N NE2  . GLN   B 1 41  ? -27.295 20.870 12.345 1.00 70.04 ? 21  GLN   B NE2  1 
ATOM   2668 H H    . GLN   B 1 41  ? -25.753 17.724 15.900 1.00 30.86 ? 21  GLN   B H    1 
ATOM   2669 H HA   . GLN   B 1 41  ? -24.860 20.056 16.696 1.00 31.53 ? 21  GLN   B HA   1 
ATOM   2670 H HB2  . GLN   B 1 41  ? -27.478 19.304 15.926 1.00 34.08 ? 21  GLN   B HB2  1 
ATOM   2671 H HB3  . GLN   B 1 41  ? -27.046 20.818 16.145 1.00 34.08 ? 21  GLN   B HB3  1 
ATOM   2672 H HG2  . GLN   B 1 41  ? -25.745 20.798 14.290 1.00 50.98 ? 21  GLN   B HG2  1 
ATOM   2673 H HG3  . GLN   B 1 41  ? -25.857 19.218 14.159 1.00 50.98 ? 21  GLN   B HG3  1 
ATOM   2674 H HE21 . GLN   B 1 41  ? -26.514 21.188 12.182 1.00 84.05 ? 21  GLN   B HE21 1 
ATOM   2675 H HE22 . GLN   B 1 41  ? -27.934 20.989 11.782 1.00 84.05 ? 21  GLN   B HE22 1 
ATOM   2676 N N    . HIS   B 1 42  ? -26.915 18.640 18.716 1.00 24.25 ? 22  HIS   B N    1 
ATOM   2677 C CA   . HIS   B 1 42  ? -27.353 18.649 20.105 1.00 23.91 ? 22  HIS   B CA   1 
ATOM   2678 C C    . HIS   B 1 42  ? -26.176 18.473 21.055 1.00 22.88 ? 22  HIS   B C    1 
ATOM   2679 O O    . HIS   B 1 42  ? -26.024 19.218 22.026 1.00 22.32 ? 22  HIS   B O    1 
ATOM   2680 C CB   . HIS   B 1 42  ? -28.342 17.531 20.338 1.00 23.90 ? 22  HIS   B CB   1 
ATOM   2681 C CG   . HIS   B 1 42  ? -28.596 17.290 21.779 1.00 23.70 ? 22  HIS   B CG   1 
ATOM   2682 N ND1  . HIS   B 1 42  ? -29.471 18.055 22.524 1.00 26.31 ? 22  HIS   B ND1  1 
ATOM   2683 C CD2  . HIS   B 1 42  ? -28.019 16.420 22.637 1.00 23.32 ? 22  HIS   B CD2  1 
ATOM   2684 C CE1  . HIS   B 1 42  ? -29.447 17.627 23.770 1.00 25.60 ? 22  HIS   B CE1  1 
ATOM   2685 N NE2  . HIS   B 1 42  ? -28.605 16.615 23.857 1.00 24.18 ? 22  HIS   B NE2  1 
ATOM   2686 H H    . HIS   B 1 42  ? -27.208 17.978 18.252 1.00 29.10 ? 22  HIS   B H    1 
ATOM   2687 H HA   . HIS   B 1 42  ? -27.780 19.501 20.283 1.00 28.69 ? 22  HIS   B HA   1 
ATOM   2688 H HB2  . HIS   B 1 42  ? -29.186 17.762 19.918 1.00 28.68 ? 22  HIS   B HB2  1 
ATOM   2689 H HB3  . HIS   B 1 42  ? -27.993 16.712 19.952 1.00 28.68 ? 22  HIS   B HB3  1 
ATOM   2690 H HD2  . HIS   B 1 42  ? -27.350 15.806 22.436 1.00 27.99 ? 22  HIS   B HD2  1 
ATOM   2691 H HE1  . HIS   B 1 42  ? -29.943 17.980 24.473 1.00 30.73 ? 22  HIS   B HE1  1 
ATOM   2692 H HE2  . HIS   B 1 42  ? -28.451 16.154 24.565 1.00 29.02 ? 22  HIS   B HE2  1 
ATOM   2693 N N    . ASN   B 1 43  ? -25.308 17.504 20.766 1.00 21.53 ? 23  ASN   B N    1 
ATOM   2694 C CA   . ASN   B 1 43  ? -24.185 17.236 21.654 1.00 21.15 ? 23  ASN   B CA   1 
ATOM   2695 C C    . ASN   B 1 43  ? -23.248 18.436 21.737 1.00 20.87 ? 23  ASN   B C    1 
ATOM   2696 O O    . ASN   B 1 43  ? -22.717 18.743 22.816 1.00 20.80 ? 23  ASN   B O    1 
ATOM   2697 C CB   . ASN   B 1 43  ? -23.425 16.004 21.180 1.00 21.46 ? 23  ASN   B CB   1 
ATOM   2698 C CG   . ASN   B 1 43  ? -24.229 14.720 21.278 1.00 21.77 ? 23  ASN   B CG   1 
ATOM   2699 O OD1  . ASN   B 1 43  ? -25.230 14.631 21.983 1.00 23.02 ? 23  ASN   B OD1  1 
ATOM   2700 N ND2  . ASN   B 1 43  ? -23.771 13.698 20.544 1.00 23.06 ? 23  ASN   B ND2  1 
ATOM   2701 H H    . ASN   B 1 43  ? -25.348 16.995 20.074 1.00 25.84 ? 23  ASN   B H    1 
ATOM   2702 H HA   . ASN   B 1 43  ? -24.528 17.057 22.543 1.00 25.38 ? 23  ASN   B HA   1 
ATOM   2703 H HB2  . ASN   B 1 43  ? -23.176 16.128 20.250 1.00 25.76 ? 23  ASN   B HB2  1 
ATOM   2704 H HB3  . ASN   B 1 43  ? -22.630 15.898 21.725 1.00 25.76 ? 23  ASN   B HB3  1 
ATOM   2705 H HD21 . ASN   B 1 43  ? -24.182 12.942 20.555 1.00 27.68 ? 23  ASN   B HD21 1 
ATOM   2706 H HD22 . ASN   B 1 43  ? -23.066 13.796 20.061 1.00 27.68 ? 23  ASN   B HD22 1 
ATOM   2707 N N    . ARG   B 1 44  ? -23.047 19.145 20.617 1.00 21.75 ? 24  ARG   B N    1 
ATOM   2708 C CA   . ARG   B 1 44  ? -22.194 20.325 20.661 1.00 22.14 ? 24  ARG   B CA   1 
ATOM   2709 C C    . ARG   B 1 44  ? -22.721 21.357 21.653 1.00 21.42 ? 24  ARG   B C    1 
ATOM   2710 O O    . ARG   B 1 44  ? -21.945 22.005 22.360 1.00 21.78 ? 24  ARG   B O    1 
ATOM   2711 C CB   . ARG   B 1 44  ? -22.056 20.954 19.273 1.00 25.33 ? 24  ARG   B CB   1 
ATOM   2712 C CG   . ARG   B 1 44  ? -21.073 22.102 19.287 1.00 30.63 ? 24  ARG   B CG   1 
ATOM   2713 C CD   . ARG   B 1 44  ? -21.023 22.830 17.991 1.00 37.27 ? 24  ARG   B CD   1 
ATOM   2714 N NE   . ARG   B 1 44  ? -20.213 24.019 18.183 1.00 44.29 ? 24  ARG   B NE   1 
ATOM   2715 C CZ   . ARG   B 1 44  ? -18.934 24.111 17.863 1.00 44.77 ? 24  ARG   B CZ   1 
ATOM   2716 N NH1  . ARG   B 1 44  ? -18.298 23.108 17.282 1.00 48.25 ? 24  ARG   B NH1  1 
ATOM   2717 N NH2  . ARG   B 1 44  ? -18.290 25.247 18.108 1.00 44.68 ? 24  ARG   B NH2  1 
ATOM   2718 H H    . ARG   B 1 44  ? -23.384 18.965 19.846 1.00 26.11 ? 24  ARG   B H    1 
ATOM   2719 H HA   . ARG   B 1 44  ? -21.312 20.042 20.948 1.00 26.58 ? 24  ARG   B HA   1 
ATOM   2720 H HB2  . ARG   B 1 44  ? -21.738 20.285 18.647 1.00 30.40 ? 24  ARG   B HB2  1 
ATOM   2721 H HB3  . ARG   B 1 44  ? -22.919 21.293 18.986 1.00 30.40 ? 24  ARG   B HB3  1 
ATOM   2722 H HG2  . ARG   B 1 44  ? -21.333 22.733 19.976 1.00 36.76 ? 24  ARG   B HG2  1 
ATOM   2723 H HG3  . ARG   B 1 44  ? -20.186 21.756 19.472 1.00 36.76 ? 24  ARG   B HG3  1 
ATOM   2724 H HD2  . ARG   B 1 44  ? -20.616 22.272 17.309 1.00 44.73 ? 24  ARG   B HD2  1 
ATOM   2725 H HD3  . ARG   B 1 44  ? -21.916 23.090 17.717 1.00 44.73 ? 24  ARG   B HD3  1 
ATOM   2726 H HE   . ARG   B 1 44  ? -20.591 24.709 18.529 1.00 53.15 ? 24  ARG   B HE   1 
ATOM   2727 H HH11 . ARG   B 1 44  ? -18.716 22.378 17.106 1.00 57.90 ? 24  ARG   B HH11 1 
ATOM   2728 H HH12 . ARG   B 1 44  ? -17.465 23.186 17.081 1.00 57.90 ? 24  ARG   B HH12 1 
ATOM   2729 H HH21 . ARG   B 1 44  ? -18.706 25.907 18.469 1.00 53.62 ? 24  ARG   B HH21 1 
ATOM   2730 H HH22 . ARG   B 1 44  ? -17.458 25.322 17.905 1.00 53.62 ? 24  ARG   B HH22 1 
ATOM   2731 N N    . LYS   B 1 45  ? -24.048 21.524 21.712 1.00 20.30 ? 25  LYS   B N    1 
ATOM   2732 C CA   . LYS   B 1 45  ? -24.622 22.486 22.644 1.00 21.29 ? 25  LYS   B CA   1 
ATOM   2733 C C    . LYS   B 1 45  ? -24.349 22.096 24.094 1.00 17.97 ? 25  LYS   B C    1 
ATOM   2734 O O    . LYS   B 1 45  ? -24.104 22.954 24.937 1.00 20.01 ? 25  LYS   B O    1 
ATOM   2735 C CB   . LYS   B 1 45  ? -26.128 22.594 22.405 1.00 24.31 ? 25  LYS   B CB   1 
ATOM   2736 C CG   . LYS   B 1 45  ? -26.483 23.241 21.096 1.00 29.06 ? 25  LYS   B CG   1 
ATOM   2737 C CD   . LYS   B 1 45  ? -28.024 23.248 20.899 1.00 37.26 ? 25  LYS   B CD   1 
ATOM   2738 H H    . LYS   B 1 45  ? -24.621 21.099 21.232 1.00 24.37 ? 25  LYS   B H    1 
ATOM   2739 H HA   . LYS   B 1 45  ? -24.216 23.353 22.487 1.00 25.55 ? 25  LYS   B HA   1 
ATOM   2740 H HB2  . LYS   B 1 45  ? -26.510 21.702 22.409 1.00 29.17 ? 25  LYS   B HB2  1 
ATOM   2741 H HB3  . LYS   B 1 45  ? -26.520 23.125 23.115 1.00 29.17 ? 25  LYS   B HB3  1 
ATOM   2742 H HG2  . LYS   B 1 45  ? -26.165 24.157 21.088 1.00 34.88 ? 25  LYS   B HG2  1 
ATOM   2743 H HG3  . LYS   B 1 45  ? -26.081 22.743 20.366 1.00 34.88 ? 25  LYS   B HG3  1 
ATOM   2744 N N    . ILE   B 1 46  ? -24.385 20.797 24.379 1.00 20.30 ? 26  ILE   B N    1 
ATOM   2745 C CA   . ILE   B 1 46  ? -24.071 20.306 25.718 1.00 20.44 ? 26  ILE   B CA   1 
ATOM   2746 C C    . ILE   B 1 46  ? -22.596 20.575 26.048 1.00 19.09 ? 26  ILE   B C    1 
ATOM   2747 O O    . ILE   B 1 46  ? -22.270 20.993 27.164 1.00 19.53 ? 26  ILE   B O    1 
ATOM   2748 C CB   . ILE   B 1 46  ? -24.426 18.813 25.853 1.00 21.25 ? 26  ILE   B CB   1 
ATOM   2749 C CG1  . ILE   B 1 46  ? -25.925 18.521 25.629 1.00 24.06 ? 26  ILE   B CG1  1 
ATOM   2750 C CG2  . ILE   B 1 46  ? -23.976 18.302 27.212 1.00 21.78 ? 26  ILE   B CG2  1 
ATOM   2751 C CD1  . ILE   B 1 46  ? -26.778 19.103 26.645 1.00 28.80 ? 26  ILE   B CD1  1 
ATOM   2752 H H    . ILE   B 1 46  ? -24.588 20.179 23.817 1.00 24.36 ? 26  ILE   B H    1 
ATOM   2753 H HA   . ILE   B 1 46  ? -24.616 20.790 26.357 1.00 24.53 ? 26  ILE   B HA   1 
ATOM   2754 H HB   . ILE   B 1 46  ? -23.953 18.345 25.147 1.00 25.50 ? 26  ILE   B HB   1 
ATOM   2755 H HG12 . ILE   B 1 46  ? -26.191 18.886 24.771 1.00 28.87 ? 26  ILE   B HG12 1 
ATOM   2756 H HG13 . ILE   B 1 46  ? -26.062 17.561 25.639 1.00 28.87 ? 26  ILE   B HG13 1 
ATOM   2757 H HG21 . ILE   B 1 46  ? -24.407 17.451 27.388 1.00 26.13 ? 26  ILE   B HG21 1 
ATOM   2758 H HG22 . ILE   B 1 46  ? -23.013 18.191 27.205 1.00 26.13 ? 26  ILE   B HG22 1 
ATOM   2759 H HG23 . ILE   B 1 46  ? -24.229 18.947 27.892 1.00 26.13 ? 26  ILE   B HG23 1 
ATOM   2760 H HD11 . ILE   B 1 46  ? -27.704 18.917 26.424 1.00 34.57 ? 26  ILE   B HD11 1 
ATOM   2761 H HD12 . ILE   B 1 46  ? -26.557 18.712 27.505 1.00 34.57 ? 26  ILE   B HD12 1 
ATOM   2762 H HD13 . ILE   B 1 46  ? -26.630 20.062 26.670 1.00 34.57 ? 26  ILE   B HD13 1 
ATOM   2763 N N    . VAL   B 1 47  ? -21.671 20.325 25.100 1.00 18.21 ? 27  VAL   B N    1 
ATOM   2764 C CA   . VAL   B 1 47  ? -20.262 20.633 25.356 1.00 17.97 ? 27  VAL   B CA   1 
ATOM   2765 C C    . VAL   B 1 47  ? -20.094 22.114 25.650 1.00 18.54 ? 27  VAL   B C    1 
ATOM   2766 O O    . VAL   B 1 47  ? -19.392 22.500 26.584 1.00 18.81 ? 27  VAL   B O    1 
ATOM   2767 C CB   . VAL   B 1 47  ? -19.378 20.205 24.174 1.00 18.33 ? 27  VAL   B CB   1 
ATOM   2768 C CG1  . VAL   B 1 47  ? -17.921 20.629 24.414 1.00 19.45 ? 27  VAL   B CG1  1 
ATOM   2769 C CG2  . VAL   B 1 47  ? -19.452 18.721 23.949 1.00 19.16 ? 27  VAL   B CG2  1 
ATOM   2770 H H    . VAL   B 1 47  ? -21.834 19.988 24.326 1.00 21.86 ? 27  VAL   B H    1 
ATOM   2771 H HA   . VAL   B 1 47  ? -19.983 20.127 26.135 1.00 21.57 ? 27  VAL   B HA   1 
ATOM   2772 H HB   . VAL   B 1 47  ? -19.705 20.646 23.374 1.00 22.00 ? 27  VAL   B HB   1 
ATOM   2773 H HG11 . VAL   B 1 47  ? -17.349 20.163 23.785 1.00 23.34 ? 27  VAL   B HG11 1 
ATOM   2774 H HG12 . VAL   B 1 47  ? -17.845 21.587 24.284 1.00 23.34 ? 27  VAL   B HG12 1 
ATOM   2775 H HG13 . VAL   B 1 47  ? -17.671 20.398 25.323 1.00 23.34 ? 27  VAL   B HG13 1 
ATOM   2776 H HG21 . VAL   B 1 47  ? -18.861 18.482 23.218 1.00 23.00 ? 27  VAL   B HG21 1 
ATOM   2777 H HG22 . VAL   B 1 47  ? -19.177 18.264 24.759 1.00 23.00 ? 27  VAL   B HG22 1 
ATOM   2778 H HG23 . VAL   B 1 47  ? -20.365 18.481 23.727 1.00 23.00 ? 27  VAL   B HG23 1 
ATOM   2779 N N    . GLU   B 1 48  ? -20.718 22.966 24.833 1.00 19.23 ? 28  GLU   B N    1 
ATOM   2780 C CA   . GLU   B 1 48  ? -20.639 24.401 25.062 1.00 21.05 ? 28  GLU   B CA   1 
ATOM   2781 C C    . GLU   B 1 48  ? -21.155 24.751 26.450 1.00 20.88 ? 28  GLU   B C    1 
ATOM   2782 O O    . GLU   B 1 48  ? -20.515 25.515 27.196 1.00 20.64 ? 28  GLU   B O    1 
ATOM   2783 C CB   . GLU   B 1 48  ? -21.452 25.153 24.016 1.00 25.07 ? 28  GLU   B CB   1 
ATOM   2784 C CG   . GLU   B 1 48  ? -20.899 25.042 22.617 1.00 30.39 ? 28  GLU   B CG   1 
ATOM   2785 C CD   . GLU   B 1 48  ? -21.803 25.613 21.552 0.45 36.59 ? 28  GLU   B CD   1 
ATOM   2786 O OE1  . GLU   B 1 48  ? -22.977 25.925 21.860 0.70 39.70 ? 28  GLU   B OE1  1 
ATOM   2787 O OE2  . GLU   B 1 48  ? -21.321 25.736 20.403 0.64 40.43 ? 28  GLU   B OE2  1 
ATOM   2788 H H    . GLU   B 1 48  ? -21.188 22.738 24.150 1.00 23.07 ? 28  GLU   B H    1 
ATOM   2789 H HA   . GLU   B 1 48  ? -19.711 24.671 24.983 1.00 25.26 ? 28  GLU   B HA   1 
ATOM   2790 H HB2  . GLU   B 1 48  ? -22.354 24.796 24.007 1.00 30.09 ? 28  GLU   B HB2  1 
ATOM   2791 H HB3  . GLU   B 1 48  ? -21.470 26.093 24.253 1.00 30.09 ? 28  GLU   B HB3  1 
ATOM   2792 H HG2  . GLU   B 1 48  ? -20.057 25.521 22.576 1.00 36.46 ? 28  GLU   B HG2  1 
ATOM   2793 H HG3  . GLU   B 1 48  ? -20.758 24.104 22.411 1.00 36.46 ? 28  GLU   B HG3  1 
ATOM   2794 N N    . GLN   B 1 49  ? -22.308 24.187 26.824 1.00 19.61 ? 29  GLN   B N    1 
ATOM   2795 C CA   . GLN   B 1 49  ? -22.857 24.476 28.141 1.00 20.29 ? 29  GLN   B CA   1 
ATOM   2796 C C    . GLN   B 1 49  ? -21.899 24.032 29.241 1.00 19.87 ? 29  GLN   B C    1 
ATOM   2797 O O    . GLN   B 1 49  ? -21.642 24.776 30.194 1.00 20.96 ? 29  GLN   B O    1 
ATOM   2798 C CB   . GLN   B 1 49  ? -24.201 23.800 28.321 1.00 22.52 ? 29  GLN   B CB   1 
ATOM   2799 C CG   . GLN   B 1 49  ? -24.791 24.268 29.609 0.87 25.78 ? 29  GLN   B CG   1 
ATOM   2800 C CD   . GLN   B 1 49  ? -26.091 23.639 29.892 0.68 26.13 ? 29  GLN   B CD   1 
ATOM   2801 O OE1  . GLN   B 1 49  ? -26.811 23.195 28.972 1.00 29.95 ? 29  GLN   B OE1  1 
ATOM   2802 N NE2  . GLN   B 1 49  ? -26.439 23.614 31.180 1.00 27.19 ? 29  GLN   B NE2  1 
ATOM   2803 H H    . GLN   B 1 49  ? -22.777 23.649 26.344 1.00 23.53 ? 29  GLN   B H    1 
ATOM   2804 H HA   . GLN   B 1 49  ? -22.990 25.435 28.209 1.00 24.35 ? 29  GLN   B HA   1 
ATOM   2805 H HB2  . GLN   B 1 49  ? -24.795 24.040 27.592 1.00 27.03 ? 29  GLN   B HB2  1 
ATOM   2806 H HB3  . GLN   B 1 49  ? -24.088 22.837 28.353 1.00 27.03 ? 29  GLN   B HB3  1 
ATOM   2807 H HG2  . GLN   B 1 49  ? -24.186 24.047 30.334 0.87 30.94 ? 29  GLN   B HG2  1 
ATOM   2808 H HG3  . GLN   B 1 49  ? -24.924 25.228 29.568 0.87 30.94 ? 29  GLN   B HG3  1 
ATOM   2809 H HE21 . GLN   B 1 49  ? -25.915 23.951 31.773 1.00 32.63 ? 29  GLN   B HE21 1 
ATOM   2810 H HE22 . GLN   B 1 49  ? -27.186 23.261 31.416 1.00 32.63 ? 29  GLN   B HE22 1 
ATOM   2811 N N    . TYR   B 1 50  ? -21.339 22.823 29.111 1.00 18.50 ? 30  TYR   B N    1 
ATOM   2812 C CA   . TYR   B 1 50  ? -20.409 22.333 30.121 1.00 17.69 ? 30  TYR   B CA   1 
ATOM   2813 C C    . TYR   B 1 50  ? -19.229 23.289 30.277 1.00 18.03 ? 30  TYR   B C    1 
ATOM   2814 O O    . TYR   B 1 50  ? -18.858 23.676 31.391 1.00 18.21 ? 30  TYR   B O    1 
ATOM   2815 C CB   . TYR   B 1 50  ? -19.946 20.917 29.737 1.00 18.26 ? 30  TYR   B CB   1 
ATOM   2816 C CG   . TYR   B 1 50  ? -19.018 20.263 30.747 1.00 17.45 ? 30  TYR   B CG   1 
ATOM   2817 C CD1  . TYR   B 1 50  ? -17.687 20.669 30.906 1.00 17.67 ? 30  TYR   B CD1  1 
ATOM   2818 C CD2  . TYR   B 1 50  ? -19.463 19.216 31.526 1.00 18.68 ? 30  TYR   B CD2  1 
ATOM   2819 C CE1  . TYR   B 1 50  ? -16.864 20.074 31.831 1.00 18.39 ? 30  TYR   B CE1  1 
ATOM   2820 C CE2  . TYR   B 1 50  ? -18.637 18.629 32.476 1.00 18.96 ? 30  TYR   B CE2  1 
ATOM   2821 C CZ   . TYR   B 1 50  ? -17.340 19.036 32.597 1.00 19.13 ? 30  TYR   B CZ   1 
ATOM   2822 O OH   . TYR   B 1 50  ? -16.550 18.412 33.532 1.00 21.17 ? 30  TYR   B OH   1 
ATOM   2823 H H    . TYR   B 1 50  ? -21.482 22.281 28.459 1.00 22.20 ? 30  TYR   B H    1 
ATOM   2824 H HA   . TYR   B 1 50  ? -20.853 22.278 30.981 1.00 21.23 ? 30  TYR   B HA   1 
ATOM   2825 H HB2  . TYR   B 1 50  ? -20.728 20.350 29.647 1.00 21.91 ? 30  TYR   B HB2  1 
ATOM   2826 H HB3  . TYR   B 1 50  ? -19.472 20.966 28.892 1.00 21.91 ? 30  TYR   B HB3  1 
ATOM   2827 H HD1  . TYR   B 1 50  ? -17.354 21.356 30.375 1.00 21.21 ? 30  TYR   B HD1  1 
ATOM   2828 H HD2  . TYR   B 1 50  ? -20.330 18.897 31.413 1.00 22.41 ? 30  TYR   B HD2  1 
ATOM   2829 H HE1  . TYR   B 1 50  ? -15.990 20.372 31.939 1.00 22.07 ? 30  TYR   B HE1  1 
ATOM   2830 H HE2  . TYR   B 1 50  ? -18.967 17.960 33.031 1.00 22.75 ? 30  TYR   B HE2  1 
ATOM   2831 H HH   . TYR   B 1 50  ? -15.785 18.759 33.540 1.00 25.40 ? 30  TYR   B HH   1 
ATOM   2832 N N    . MET   B 1 51  ? -18.615 23.675 29.153 1.00 18.16 ? 31  MET   B N    1 
ATOM   2833 C CA   . MET   B 1 51  ? -17.400 24.482 29.196 1.00 18.17 ? 31  MET   B CA   1 
ATOM   2834 C C    . MET   B 1 51  ? -17.651 25.878 29.746 1.00 18.91 ? 31  MET   B C    1 
ATOM   2835 O O    . MET   B 1 51  ? -16.733 26.506 30.295 1.00 20.06 ? 31  MET   B O    1 
ATOM   2836 C CB   . MET   B 1 51  ? -16.754 24.548 27.810 1.00 19.32 ? 31  MET   B CB   1 
ATOM   2837 C CG   . MET   B 1 51  ? -16.292 23.191 27.269 1.00 19.13 ? 31  MET   B CG   1 
ATOM   2838 S SD   . MET   B 1 51  ? -15.224 22.244 28.333 1.00 18.56 ? 31  MET   B SD   1 
ATOM   2839 C CE   . MET   B 1 51  ? -13.897 23.418 28.717 1.00 19.55 ? 31  MET   B CE   1 
ATOM   2840 H H    . MET   B 1 51  ? -18.883 23.484 28.359 1.00 21.80 ? 31  MET   B H    1 
ATOM   2841 H HA   . MET   B 1 51  ? -16.770 24.040 29.786 1.00 21.80 ? 31  MET   B HA   1 
ATOM   2842 H HB2  . MET   B 1 51  ? -17.400 24.910 27.184 1.00 23.19 ? 31  MET   B HB2  1 
ATOM   2843 H HB3  . MET   B 1 51  ? -15.977 25.126 27.857 1.00 23.19 ? 31  MET   B HB3  1 
ATOM   2844 H HG2  . MET   B 1 51  ? -17.079 22.649 27.099 1.00 22.95 ? 31  MET   B HG2  1 
ATOM   2845 H HG3  . MET   B 1 51  ? -15.809 23.343 26.441 1.00 22.95 ? 31  MET   B HG3  1 
ATOM   2846 H HE1  . MET   B 1 51  ? -13.249 22.983 29.294 1.00 23.47 ? 31  MET   B HE1  1 
ATOM   2847 H HE2  . MET   B 1 51  ? -13.472 23.695 27.891 1.00 23.47 ? 31  MET   B HE2  1 
ATOM   2848 H HE3  . MET   B 1 51  ? -14.277 24.187 29.169 1.00 23.47 ? 31  MET   B HE3  1 
ATOM   2849 N N    A HIS   B 1 52  ? -18.876 26.388 29.605 0.55 18.68 ? 32  HIS   B N    1 
ATOM   2850 N N    B HIS   B 1 52  ? -18.874 26.382 29.618 0.45 18.66 ? 32  HIS   B N    1 
ATOM   2851 C CA   A HIS   B 1 52  ? -19.215 27.706 30.124 0.55 20.46 ? 32  HIS   B CA   1 
ATOM   2852 C CA   B HIS   B 1 52  ? -19.224 27.706 30.114 0.45 19.69 ? 32  HIS   B CA   1 
ATOM   2853 C C    A HIS   B 1 52  ? -19.709 27.688 31.563 0.55 19.52 ? 32  HIS   B C    1 
ATOM   2854 C C    B HIS   B 1 52  ? -19.875 27.673 31.494 0.45 19.94 ? 32  HIS   B C    1 
ATOM   2855 O O    A HIS   B 1 52  ? -19.887 28.763 32.146 0.55 21.05 ? 32  HIS   B O    1 
ATOM   2856 O O    B HIS   B 1 52  ? -20.327 28.717 31.979 0.45 22.07 ? 32  HIS   B O    1 
ATOM   2857 C CB   A HIS   B 1 52  ? -20.257 28.377 29.230 0.55 24.77 ? 32  HIS   B CB   1 
ATOM   2858 C CB   B HIS   B 1 52  ? -20.085 28.421 29.073 0.45 22.16 ? 32  HIS   B CB   1 
ATOM   2859 C CG   A HIS   B 1 52  ? -19.680 28.871 27.950 0.55 28.04 ? 32  HIS   B CG   1 
ATOM   2860 C CG   B HIS   B 1 52  ? -19.306 28.848 27.867 0.45 23.61 ? 32  HIS   B CG   1 
ATOM   2861 N ND1  A HIS   B 1 52  ? -20.448 29.133 26.838 0.55 30.23 ? 32  HIS   B ND1  1 
ATOM   2862 N ND1  B HIS   B 1 52  ? -19.085 28.023 26.782 0.45 23.40 ? 32  HIS   B ND1  1 
ATOM   2863 C CD2  A HIS   B 1 52  ? -18.400 29.149 27.608 0.55 29.05 ? 32  HIS   B CD2  1 
ATOM   2864 C CD2  B HIS   B 1 52  ? -18.649 30.000 27.600 0.45 25.94 ? 32  HIS   B CD2  1 
ATOM   2865 C CE1  A HIS   B 1 52  ? -19.662 29.551 25.862 0.55 30.03 ? 32  HIS   B CE1  1 
ATOM   2866 C CE1  B HIS   B 1 52  ? -18.349 28.663 25.888 0.45 23.61 ? 32  HIS   B CE1  1 
ATOM   2867 N NE2  A HIS   B 1 52  ? -18.414 29.550 26.297 0.55 30.55 ? 32  HIS   B NE2  1 
ATOM   2868 N NE2  B HIS   B 1 52  ? -18.063 29.860 26.368 0.45 26.45 ? 32  HIS   B NE2  1 
ATOM   2869 H H    A HIS   B 1 52  ? -19.527 25.986 29.211 0.55 22.41 ? 32  HIS   B H    1 
ATOM   2870 H H    B HIS   B 1 52  ? -19.527 25.968 29.241 0.45 22.39 ? 32  HIS   B H    1 
ATOM   2871 H HA   A HIS   B 1 52  ? -18.413 28.252 30.105 0.55 24.55 ? 32  HIS   B HA   1 
ATOM   2872 H HA   B HIS   B 1 52  ? -18.421 28.239 30.225 0.45 23.63 ? 32  HIS   B HA   1 
ATOM   2873 H HB2  A HIS   B 1 52  ? -20.953 27.735 29.019 0.55 29.72 ? 32  HIS   B HB2  1 
ATOM   2874 H HB2  B HIS   B 1 52  ? -20.788 27.820 28.778 0.45 26.60 ? 32  HIS   B HB2  1 
ATOM   2875 H HB3  A HIS   B 1 52  ? -20.637 29.135 29.701 0.55 29.72 ? 32  HIS   B HB3  1 
ATOM   2876 H HB3  B HIS   B 1 52  ? -20.473 29.214 29.475 0.45 26.60 ? 32  HIS   B HB3  1 
ATOM   2877 H HD1  B HIS   B 1 52  ? -19.379 27.219 26.700 0.45 28.08 ? 32  HIS   B HD1  1 
ATOM   2878 H HD2  A HIS   B 1 52  ? -17.654 29.080 28.158 0.55 34.86 ? 32  HIS   B HD2  1 
ATOM   2879 H HD2  B HIS   B 1 52  ? -18.603 30.749 28.151 0.45 31.13 ? 32  HIS   B HD2  1 
ATOM   2880 H HE1  A HIS   B 1 52  ? -19.941 29.804 25.011 0.55 36.03 ? 32  HIS   B HE1  1 
ATOM   2881 H HE1  B HIS   B 1 52  ? -18.080 28.328 25.064 0.45 28.34 ? 32  HIS   B HE1  1 
ATOM   2882 H HE2  A HIS   B 1 52  ? -17.722 29.766 25.834 0.55 36.67 ? 32  HIS   B HE2  1 
ATOM   2883 N N    . THR   B 1 53  ? -19.911 26.509 32.148 1.00 18.93 ? 33  THR   B N    1 
ATOM   2884 C CA   . THR   B 1 53  ? -20.513 26.404 33.474 1.00 19.49 ? 33  THR   B CA   1 
ATOM   2885 C C    . THR   B 1 53  ? -19.522 26.899 34.516 1.00 20.24 ? 33  THR   B C    1 
ATOM   2886 O O    . THR   B 1 53  ? -18.379 26.428 34.590 1.00 22.05 ? 33  THR   B O    1 
ATOM   2887 C CB   . THR   B 1 53  ? -20.926 24.965 33.765 1.00 20.36 ? 33  THR   B CB   1 
ATOM   2888 O OG1  . THR   B 1 53  ? -21.959 24.556 32.856 1.00 20.75 ? 33  THR   B OG1  1 
ATOM   2889 C CG2  . THR   B 1 53  ? -21.506 24.828 35.175 1.00 21.60 ? 33  THR   B CG2  1 
ATOM   2890 H H    A THR   B 1 53  ? -19.707 25.751 31.797 0.55 22.72 ? 33  THR   B H    1 
ATOM   2891 H H    B THR   B 1 53  ? -19.594 25.770 31.845 0.45 22.72 ? 33  THR   B H    1 
ATOM   2892 H HA   . THR   B 1 53  ? -21.313 26.951 33.518 1.00 23.39 ? 33  THR   B HA   1 
ATOM   2893 H HB   . THR   B 1 53  ? -20.138 24.406 33.676 1.00 24.43 ? 33  THR   B HB   1 
ATOM   2894 H HG1  . THR   B 1 53  ? -21.671 24.576 32.067 1.00 24.90 ? 33  THR   B HG1  1 
ATOM   2895 H HG21 . THR   B 1 53  ? -21.944 23.968 35.272 1.00 25.92 ? 33  THR   B HG21 1 
ATOM   2896 H HG22 . THR   B 1 53  ? -20.797 24.896 35.834 1.00 25.92 ? 33  THR   B HG22 1 
ATOM   2897 H HG23 . THR   B 1 53  ? -22.154 25.531 35.337 1.00 25.92 ? 33  THR   B HG23 1 
ATOM   2898 N N    . ARG   B 1 54  ? -19.976 27.832 35.343 1.00 20.06 ? 34  ARG   B N    1 
ATOM   2899 C CA   . ARG   B 1 54  ? -19.137 28.375 36.385 1.00 21.16 ? 34  ARG   B CA   1 
ATOM   2900 C C    . ARG   B 1 54  ? -20.010 28.806 37.550 1.00 20.64 ? 34  ARG   B C    1 
ATOM   2901 O O    . ARG   B 1 54  ? -21.241 28.819 37.466 1.00 23.07 ? 34  ARG   B O    1 
ATOM   2902 C CB   . ARG   B 1 54  ? -18.285 29.555 35.932 1.00 25.85 ? 34  ARG   B CB   1 
ATOM   2903 C CG   . ARG   B 1 54  ? -18.934 30.507 35.068 1.00 29.42 ? 34  ARG   B CG   1 
ATOM   2904 C CD   . ARG   B 1 54  ? -17.879 31.456 34.566 1.00 32.77 ? 34  ARG   B CD   1 
ATOM   2905 N NE   . ARG   B 1 54  ? -18.450 32.411 33.646 1.00 30.85 ? 34  ARG   B NE   1 
ATOM   2906 C CZ   . ARG   B 1 54  ? -18.261 32.407 32.339 1.00 27.52 ? 34  ARG   B CZ   1 
ATOM   2907 N NH1  . ARG   B 1 54  ? -17.578 31.445 31.731 1.00 27.41 ? 34  ARG   B NH1  1 
ATOM   2908 N NH2  . ARG   B 1 54  ? -18.734 33.417 31.632 1.00 29.58 ? 34  ARG   B NH2  1 
ATOM   2909 H H    . ARG   B 1 54  ? -20.770 28.163 35.316 1.00 24.08 ? 34  ARG   B H    1 
ATOM   2910 H HA   . ARG   B 1 54  ? -18.539 27.664 36.663 1.00 25.39 ? 34  ARG   B HA   1 
ATOM   2911 H HB2  . ARG   B 1 54  ? -17.991 30.037 36.720 1.00 31.02 ? 34  ARG   B HB2  1 
ATOM   2912 H HB3  . ARG   B 1 54  ? -17.518 29.207 35.450 1.00 31.02 ? 34  ARG   B HB3  1 
ATOM   2913 H HG2  . ARG   B 1 54  ? -19.343 30.054 34.314 1.00 35.30 ? 34  ARG   B HG2  1 
ATOM   2914 H HG3  . ARG   B 1 54  ? -19.605 31.005 35.560 1.00 35.30 ? 34  ARG   B HG3  1 
ATOM   2915 H HD2  . ARG   B 1 54  ? -17.495 31.940 35.314 1.00 39.32 ? 34  ARG   B HD2  1 
ATOM   2916 H HD3  . ARG   B 1 54  ? -17.187 30.958 34.104 1.00 39.32 ? 34  ARG   B HD3  1 
ATOM   2917 H HE   . ARG   B 1 54  ? -18.950 33.028 33.974 1.00 37.02 ? 34  ARG   B HE   1 
ATOM   2918 H HH11 . ARG   B 1 54  ? -17.243 30.799 32.189 1.00 32.90 ? 34  ARG   B HH11 1 
ATOM   2919 H HH12 . ARG   B 1 54  ? -17.470 31.467 30.878 1.00 32.90 ? 34  ARG   B HH12 1 
ATOM   2920 H HH21 . ARG   B 1 54  ? -19.153 34.057 32.024 1.00 35.50 ? 34  ARG   B HH21 1 
ATOM   2921 H HH22 . ARG   B 1 54  ? -18.622 33.435 30.780 1.00 35.50 ? 34  ARG   B HH22 1 
ATOM   2922 N N    . GLY   B 1 55  ? -19.338 29.121 38.649 1.00 21.94 ? 35  GLY   B N    1 
ATOM   2923 C CA   . GLY   B 1 55  ? -20.037 29.629 39.814 1.00 23.65 ? 35  GLY   B CA   1 
ATOM   2924 C C    . GLY   B 1 55  ? -20.993 28.590 40.371 1.00 24.88 ? 35  GLY   B C    1 
ATOM   2925 O O    . GLY   B 1 55  ? -20.751 27.376 40.304 1.00 24.20 ? 35  GLY   B O    1 
ATOM   2926 H H    . GLY   B 1 55  ? -18.486 29.050 38.743 1.00 26.33 ? 35  GLY   B H    1 
ATOM   2927 H HA2  . GLY   B 1 55  ? -19.396 29.863 40.503 1.00 28.38 ? 35  GLY   B HA2  1 
ATOM   2928 H HA3  . GLY   B 1 55  ? -20.543 30.420 39.571 1.00 28.38 ? 35  GLY   B HA3  1 
ATOM   2929 N N    . GLU   B 1 56  ? -22.124 29.068 40.893 1.00 27.46 ? 36  GLU   B N    1 
ATOM   2930 C CA   . GLU   B 1 56  ? -23.087 28.164 41.504 1.00 27.59 ? 36  GLU   B CA   1 
ATOM   2931 C C    . GLU   B 1 56  ? -23.695 27.183 40.509 1.00 25.91 ? 36  GLU   B C    1 
ATOM   2932 O O    . GLU   B 1 56  ? -24.121 26.098 40.923 1.00 25.51 ? 36  GLU   B O    1 
ATOM   2933 C CB   . GLU   B 1 56  ? -24.185 28.981 42.183 1.00 34.97 ? 36  GLU   B CB   1 
ATOM   2934 C CG   . GLU   B 1 56  ? -23.677 29.813 43.342 1.00 41.90 ? 36  GLU   B CG   1 
ATOM   2935 C CD   . GLU   B 1 56  ? -23.019 28.961 44.430 1.00 47.25 ? 36  GLU   B CD   1 
ATOM   2936 O OE1  . GLU   B 1 56  ? -23.717 28.121 45.050 1.00 48.68 ? 36  GLU   B OE1  1 
ATOM   2937 O OE2  . GLU   B 1 56  ? -21.794 29.120 44.645 1.00 49.92 ? 36  GLU   B OE2  1 
ATOM   2938 H H    . GLU   B 1 56  ? -22.350 29.898 40.904 1.00 32.96 ? 36  GLU   B H    1 
ATOM   2939 H HA   . GLU   B 1 56  ? -22.636 27.634 42.180 1.00 33.11 ? 36  GLU   B HA   1 
ATOM   2940 H HB2  . GLU   B 1 56  ? -24.576 29.584 41.532 1.00 41.96 ? 36  GLU   B HB2  1 
ATOM   2941 H HB3  . GLU   B 1 56  ? -24.862 28.376 42.524 1.00 41.96 ? 36  GLU   B HB3  1 
ATOM   2942 H HG2  . GLU   B 1 56  ? -23.018 30.444 43.014 1.00 50.28 ? 36  GLU   B HG2  1 
ATOM   2943 H HG3  . GLU   B 1 56  ? -24.422 30.288 43.741 1.00 50.28 ? 36  GLU   B HG3  1 
ATOM   2944 N N    . ALA   B 1 57  ? -23.699 27.506 39.211 1.00 25.56 ? 37  ALA   B N    1 
ATOM   2945 C CA   . ALA   B 1 57  ? -24.204 26.570 38.211 1.00 23.44 ? 37  ALA   B CA   1 
ATOM   2946 C C    . ALA   B 1 57  ? -23.411 25.266 38.200 1.00 20.75 ? 37  ALA   B C    1 
ATOM   2947 O O    . ALA   B 1 57  ? -23.920 24.236 37.738 1.00 21.83 ? 37  ALA   B O    1 
ATOM   2948 C CB   . ALA   B 1 57  ? -24.198 27.231 36.829 1.00 24.11 ? 37  ALA   B CB   1 
ATOM   2949 H H    . ALA   B 1 57  ? -23.417 28.252 38.890 1.00 30.68 ? 37  ALA   B H    1 
ATOM   2950 H HA   . ALA   B 1 57  ? -25.125 26.344 38.417 1.00 28.13 ? 37  ALA   B HA   1 
ATOM   2951 H HB1  . ALA   B 1 57  ? -24.541 26.601 36.176 1.00 28.93 ? 37  ALA   B HB1  1 
ATOM   2952 H HB2  . ALA   B 1 57  ? -24.760 28.020 36.854 1.00 28.93 ? 37  ALA   B HB2  1 
ATOM   2953 H HB3  . ALA   B 1 57  ? -23.288 27.479 36.602 1.00 28.93 ? 37  ALA   B HB3  1 
ATOM   2954 N N    . ARG   B 1 58  ? -22.189 25.279 38.724 1.00 20.34 ? 38  ARG   B N    1 
ATOM   2955 C CA   . ARG   B 1 58  ? -21.421 24.043 38.794 1.00 20.10 ? 38  ARG   B CA   1 
ATOM   2956 C C    . ARG   B 1 58  ? -22.132 22.984 39.624 1.00 20.58 ? 38  ARG   B C    1 
ATOM   2957 O O    . ARG   B 1 58  ? -21.933 21.788 39.399 1.00 21.42 ? 38  ARG   B O    1 
ATOM   2958 C CB   . ARG   B 1 58  ? -20.034 24.332 39.342 1.00 20.90 ? 38  ARG   B CB   1 
ATOM   2959 C CG   . ARG   B 1 58  ? -19.184 25.152 38.374 1.00 22.49 ? 38  ARG   B CG   1 
ATOM   2960 C CD   . ARG   B 1 58  ? -18.085 25.953 39.070 1.00 25.49 ? 38  ARG   B CD   1 
ATOM   2961 N NE   . ARG   B 1 58  ? -17.156 25.088 39.761 1.00 25.69 ? 38  ARG   B NE   1 
ATOM   2962 C CZ   . ARG   B 1 58  ? -16.126 25.513 40.478 1.00 25.05 ? 38  ARG   B CZ   1 
ATOM   2963 N NH1  . ARG   B 1 58  ? -15.933 26.796 40.724 1.00 25.66 ? 38  ARG   B NH1  1 
ATOM   2964 N NH2  . ARG   B 1 58  ? -15.318 24.622 41.028 1.00 26.17 ? 38  ARG   B NH2  1 
ATOM   2965 H H    . ARG   B 1 58  ? -21.791 25.973 39.039 1.00 24.41 ? 38  ARG   B H    1 
ATOM   2966 H HA   . ARG   B 1 58  ? -21.316 23.681 37.901 1.00 24.13 ? 38  ARG   B HA   1 
ATOM   2967 H HB2  . ARG   B 1 58  ? -20.117 24.832 40.168 1.00 25.09 ? 38  ARG   B HB2  1 
ATOM   2968 H HB3  . ARG   B 1 58  ? -19.577 23.492 39.507 1.00 25.09 ? 38  ARG   B HB3  1 
ATOM   2969 H HG2  . ARG   B 1 58  ? -18.760 24.552 37.741 1.00 26.98 ? 38  ARG   B HG2  1 
ATOM   2970 H HG3  . ARG   B 1 58  ? -19.758 25.778 37.905 1.00 26.98 ? 38  ARG   B HG3  1 
ATOM   2971 H HD2  . ARG   B 1 58  ? -17.592 26.463 38.408 1.00 30.59 ? 38  ARG   B HD2  1 
ATOM   2972 H HD3  . ARG   B 1 58  ? -18.485 26.552 39.719 1.00 30.59 ? 38  ARG   B HD3  1 
ATOM   2973 H HE   . ARG   B 1 58  ? -17.280 24.239 39.703 1.00 30.83 ? 38  ARG   B HE   1 
ATOM   2974 H HH11 . ARG   B 1 58  ? -16.483 27.381 40.416 1.00 30.79 ? 38  ARG   B HH11 1 
ATOM   2975 H HH12 . ARG   B 1 58  ? -15.257 27.047 41.192 1.00 30.79 ? 38  ARG   B HH12 1 
ATOM   2976 H HH21 . ARG   B 1 58  ? -15.465 23.782 40.917 1.00 31.40 ? 38  ARG   B HH21 1 
ATOM   2977 H HH22 . ARG   B 1 58  ? -14.645 24.882 41.496 1.00 31.40 ? 38  ARG   B HH22 1 
ATOM   2978 N N    . LEU   B 1 59  ? -22.979 23.398 40.574 1.00 21.74 ? 39  LEU   B N    1 
ATOM   2979 C CA   . LEU   B 1 59  ? -23.681 22.434 41.403 1.00 23.19 ? 39  LEU   B CA   1 
ATOM   2980 C C    . LEU   B 1 59  ? -24.660 21.592 40.605 1.00 23.62 ? 39  LEU   B C    1 
ATOM   2981 O O    . LEU   B 1 59  ? -25.096 20.556 41.115 1.00 24.06 ? 39  LEU   B O    1 
ATOM   2982 C CB   . LEU   B 1 59  ? -24.422 23.148 42.535 1.00 26.69 ? 39  LEU   B CB   1 
ATOM   2983 C CG   . LEU   B 1 59  ? -23.507 23.767 43.589 1.00 30.82 ? 39  LEU   B CG   1 
ATOM   2984 C CD1  . LEU   B 1 59  ? -24.345 24.557 44.594 1.00 33.65 ? 39  LEU   B CD1  1 
ATOM   2985 C CD2  . LEU   B 1 59  ? -22.667 22.702 44.319 1.00 32.84 ? 39  LEU   B CD2  1 
ATOM   2986 H H    . LEU   B 1 59  ? -23.158 24.221 40.751 1.00 26.09 ? 39  LEU   B H    1 
ATOM   2987 H HA   . LEU   B 1 59  ? -23.027 21.839 41.802 1.00 27.83 ? 39  LEU   B HA   1 
ATOM   2988 H HB2  . LEU   B 1 59  ? -24.956 23.862 42.153 1.00 32.03 ? 39  LEU   B HB2  1 
ATOM   2989 H HB3  . LEU   B 1 59  ? -24.996 22.507 42.983 1.00 32.03 ? 39  LEU   B HB3  1 
ATOM   2990 H HG   . LEU   B 1 59  ? -22.885 24.364 43.144 1.00 36.98 ? 39  LEU   B HG   1 
ATOM   2991 H HD11 . LEU   B 1 59  ? -23.755 24.951 45.256 1.00 40.38 ? 39  LEU   B HD11 1 
ATOM   2992 H HD12 . LEU   B 1 59  ? -24.827 25.255 44.124 1.00 40.38 ? 39  LEU   B HD12 1 
ATOM   2993 H HD13 . LEU   B 1 59  ? -24.971 23.955 45.026 1.00 40.38 ? 39  LEU   B HD13 1 
ATOM   2994 H HD21 . LEU   B 1 59  ? -22.238 23.110 45.087 1.00 39.41 ? 39  LEU   B HD21 1 
ATOM   2995 H HD22 . LEU   B 1 59  ? -23.251 21.984 44.609 1.00 39.41 ? 39  LEU   B HD22 1 
ATOM   2996 H HD23 . LEU   B 1 59  ? -21.996 22.357 43.710 1.00 39.41 ? 39  LEU   B HD23 1 
ATOM   2997 N N    . LYS   B 1 60  ? -25.009 21.999 39.380 1.00 22.77 ? 40  LYS   B N    1 
ATOM   2998 C CA   . LYS   B 1 60  ? -25.954 21.254 38.551 1.00 23.16 ? 40  LYS   B CA   1 
ATOM   2999 C C    . LYS   B 1 60  ? -25.345 20.726 37.257 1.00 21.92 ? 40  LYS   B C    1 
ATOM   3000 O O    . LYS   B 1 60  ? -26.045 20.157 36.419 1.00 22.23 ? 40  LYS   B O    1 
ATOM   3001 C CB   . LYS   B 1 60  ? -27.182 22.110 38.230 1.00 29.97 ? 40  LYS   B CB   1 
ATOM   3002 C CG   . LYS   B 1 60  ? -28.070 22.427 39.475 1.00 29.97 ? 40  LYS   B CG   1 
ATOM   3003 C CD   . LYS   B 1 60  ? -29.195 23.346 39.043 1.00 29.98 ? 40  LYS   B CD   1 
ATOM   3004 C CE   . LYS   B 1 60  ? -30.046 23.722 40.197 1.00 29.98 ? 40  LYS   B CE   1 
ATOM   3005 N NZ   . LYS   B 1 60  ? -31.141 24.575 39.743 1.00 30.00 ? 40  LYS   B NZ   1 
ATOM   3006 H H    . LYS   B 1 60  ? -24.707 22.711 39.005 1.00 27.33 ? 40  LYS   B H    1 
ATOM   3007 H HA   . LYS   B 1 60  ? -26.246 20.484 39.064 1.00 27.80 ? 40  LYS   B HA   1 
ATOM   3008 H HB2  . LYS   B 1 60  ? -26.885 22.954 37.856 1.00 35.96 ? 40  LYS   B HB2  1 
ATOM   3009 H HB3  . LYS   B 1 60  ? -27.733 21.637 37.586 1.00 35.96 ? 40  LYS   B HB3  1 
ATOM   3010 H HG2  . LYS   B 1 60  ? -28.449 21.608 39.831 1.00 35.96 ? 40  LYS   B HG2  1 
ATOM   3011 H HG3  . LYS   B 1 60  ? -27.542 22.871 40.157 1.00 35.96 ? 40  LYS   B HG3  1 
ATOM   3012 H HD2  . LYS   B 1 60  ? -28.822 24.156 38.660 1.00 35.97 ? 40  LYS   B HD2  1 
ATOM   3013 H HD3  . LYS   B 1 60  ? -29.748 22.894 38.387 1.00 35.97 ? 40  LYS   B HD3  1 
ATOM   3014 H HE2  . LYS   B 1 60  ? -30.419 22.924 40.603 1.00 35.98 ? 40  LYS   B HE2  1 
ATOM   3015 H HE3  . LYS   B 1 60  ? -29.519 24.210 40.848 1.00 35.98 ? 40  LYS   B HE3  1 
ATOM   3016 H HZ1  . LYS   B 1 60  ? -31.653 24.806 40.433 1.00 36.00 ? 40  LYS   B HZ1  1 
ATOM   3017 H HZ2  . LYS   B 1 60  ? -30.816 25.312 39.364 1.00 36.00 ? 40  LYS   B HZ2  1 
ATOM   3018 H HZ3  . LYS   B 1 60  ? -31.639 24.140 39.147 1.00 36.00 ? 40  LYS   B HZ3  1 
ATOM   3019 N N    . ARG   B 1 61  ? -24.031 20.826 37.108 1.00 20.52 ? 41  ARG   B N    1 
ATOM   3020 C CA   . ARG   B 1 61  ? -23.366 20.369 35.886 1.00 19.61 ? 41  ARG   B CA   1 
ATOM   3021 C C    . ARG   B 1 61  ? -23.512 18.866 35.692 1.00 20.01 ? 41  ARG   B C    1 
ATOM   3022 O O    . ARG   B 1 61  ? -23.523 18.380 34.549 1.00 19.58 ? 41  ARG   B O    1 
ATOM   3023 C CB   . ARG   B 1 61  ? -21.893 20.761 35.921 1.00 20.46 ? 41  ARG   B CB   1 
ATOM   3024 C CG   . ARG   B 1 61  ? -21.194 20.676 34.557 1.00 20.57 ? 41  ARG   B CG   1 
ATOM   3025 C CD   . ARG   B 1 61  ? -19.754 21.149 34.649 1.00 20.70 ? 41  ARG   B CD   1 
ATOM   3026 N NE   . ARG   B 1 61  ? -18.952 20.246 35.451 1.00 21.75 ? 41  ARG   B NE   1 
ATOM   3027 C CZ   . ARG   B 1 61  ? -17.729 20.506 35.877 1.00 23.28 ? 41  ARG   B CZ   1 
ATOM   3028 N NH1  . ARG   B 1 61  ? -17.128 21.646 35.584 1.00 25.49 ? 41  ARG   B NH1  1 
ATOM   3029 N NH2  . ARG   B 1 61  ? -17.111 19.609 36.633 1.00 26.14 ? 41  ARG   B NH2  1 
ATOM   3030 H H    . ARG   B 1 61  ? -23.497 21.154 37.696 1.00 24.62 ? 41  ARG   B H    1 
ATOM   3031 H HA   . ARG   B 1 61  ? -23.778 20.806 35.123 1.00 23.53 ? 41  ARG   B HA   1 
ATOM   3032 H HB2  . ARG   B 1 61  ? -21.822 21.677 36.233 1.00 24.55 ? 41  ARG   B HB2  1 
ATOM   3033 H HB3  . ARG   B 1 61  ? -21.427 20.167 36.529 1.00 24.55 ? 41  ARG   B HB3  1 
ATOM   3034 H HG2  . ARG   B 1 61  ? -21.195 19.756 34.251 1.00 24.68 ? 41  ARG   B HG2  1 
ATOM   3035 H HG3  . ARG   B 1 61  ? -21.661 21.239 33.920 1.00 24.68 ? 41  ARG   B HG3  1 
ATOM   3036 H HD2  . ARG   B 1 61  ? -19.371 21.189 33.759 1.00 24.84 ? 41  ARG   B HD2  1 
ATOM   3037 H HD3  . ARG   B 1 61  ? -19.729 22.027 35.061 1.00 24.84 ? 41  ARG   B HD3  1 
ATOM   3038 H HE   . ARG   B 1 61  ? -19.297 19.488 35.665 1.00 26.10 ? 41  ARG   B HE   1 
ATOM   3039 H HH11 . ARG   B 1 61  ? -17.534 22.236 35.108 1.00 30.59 ? 41  ARG   B HH11 1 
ATOM   3040 H HH12 . ARG   B 1 61  ? -16.332 21.797 35.870 1.00 30.59 ? 41  ARG   B HH12 1 
ATOM   3041 H HH21 . ARG   B 1 61  ? -17.507 18.874 36.838 1.00 31.36 ? 41  ARG   B HH21 1 
ATOM   3042 H HH22 . ARG   B 1 61  ? -16.315 19.763 36.919 1.00 31.36 ? 41  ARG   B HH22 1 
ATOM   3043 N N    . HIS   B 1 62  ? -23.663 18.118 36.792 1.00 20.20 ? 42  HIS   B N    1 
ATOM   3044 C CA   . HIS   B 1 62  ? -23.828 16.673 36.706 1.00 19.46 ? 42  HIS   B CA   1 
ATOM   3045 C C    . HIS   B 1 62  ? -25.085 16.280 35.936 1.00 20.23 ? 42  HIS   B C    1 
ATOM   3046 O O    . HIS   B 1 62  ? -25.172 15.145 35.454 1.00 20.24 ? 42  HIS   B O    1 
ATOM   3047 C CB   . HIS   B 1 62  ? -23.816 16.033 38.084 1.00 20.79 ? 42  HIS   B CB   1 
ATOM   3048 C CG   . HIS   B 1 62  ? -24.959 16.433 38.953 1.00 20.83 ? 42  HIS   B CG   1 
ATOM   3049 N ND1  . HIS   B 1 62  ? -25.065 17.689 39.509 1.00 22.17 ? 42  HIS   B ND1  1 
ATOM   3050 C CD2  . HIS   B 1 62  ? -26.040 15.736 39.379 1.00 23.88 ? 42  HIS   B CD2  1 
ATOM   3051 C CE1  . HIS   B 1 62  ? -26.153 17.742 40.262 1.00 23.50 ? 42  HIS   B CE1  1 
ATOM   3052 N NE2  . HIS   B 1 62  ? -26.764 16.575 40.187 1.00 25.04 ? 42  HIS   B NE2  1 
ATOM   3053 H H    . HIS   B 1 62  ? -23.672 18.426 37.595 1.00 24.24 ? 42  HIS   B H    1 
ATOM   3054 H HA   . HIS   B 1 62  ? -23.066 16.310 36.228 1.00 23.35 ? 42  HIS   B HA   1 
ATOM   3055 H HB2  . HIS   B 1 62  ? -23.850 15.069 37.979 1.00 24.95 ? 42  HIS   B HB2  1 
ATOM   3056 H HB3  . HIS   B 1 62  ? -22.998 16.289 38.538 1.00 24.95 ? 42  HIS   B HB3  1 
ATOM   3057 H HD2  . HIS   B 1 62  ? -26.251 14.856 39.164 1.00 28.66 ? 42  HIS   B HD2  1 
ATOM   3058 H HE1  . HIS   B 1 62  ? -26.437 18.475 40.759 1.00 28.21 ? 42  HIS   B HE1  1 
ATOM   3059 H HE2  . HIS   B 1 62  ? -27.501 16.372 40.582 1.00 30.05 ? 42  HIS   B HE2  1 
ATOM   3060 N N    . LEU   B 1 63  ? -26.062 17.181 35.820 1.00 20.83 ? 43  LEU   B N    1 
ATOM   3061 C CA   . LEU   B 1 63  ? -27.288 16.874 35.090 1.00 21.08 ? 43  LEU   B CA   1 
ATOM   3062 C C    . LEU   B 1 63  ? -27.052 16.813 33.590 1.00 20.74 ? 43  LEU   B C    1 
ATOM   3063 O O    . LEU   B 1 63  ? -27.919 16.373 32.847 1.00 22.16 ? 43  LEU   B O    1 
ATOM   3064 C CB   . LEU   B 1 63  ? -28.371 17.887 35.440 1.00 23.58 ? 43  LEU   B CB   1 
ATOM   3065 C CG   . LEU   B 1 63  ? -28.779 17.893 36.922 1.00 26.46 ? 43  LEU   B CG   1 
ATOM   3066 C CD1  . LEU   B 1 63  ? -29.846 18.925 37.213 1.00 29.45 ? 43  LEU   B CD1  1 
ATOM   3067 C CD2  . LEU   B 1 63  ? -29.295 16.535 37.387 1.00 28.04 ? 43  LEU   B CD2  1 
ATOM   3068 H H    . LEU   B 1 63  ? -26.038 17.974 36.154 1.00 25.00 ? 43  LEU   B H    1 
ATOM   3069 H HA   . LEU   B 1 63  ? -27.624 16.007 35.366 1.00 25.29 ? 43  LEU   B HA   1 
ATOM   3070 H HB2  . LEU   B 1 63  ? -28.047 18.775 35.220 1.00 28.30 ? 43  LEU   B HB2  1 
ATOM   3071 H HB3  . LEU   B 1 63  ? -29.164 17.685 34.918 1.00 28.30 ? 43  LEU   B HB3  1 
ATOM   3072 H HG   . LEU   B 1 63  ? -27.974 18.113 37.417 1.00 31.75 ? 43  LEU   B HG   1 
ATOM   3073 H HD11 . LEU   B 1 63  ? -30.067 18.894 38.157 1.00 35.34 ? 43  LEU   B HD11 1 
ATOM   3074 H HD12 . LEU   B 1 63  ? -29.507 19.804 36.981 1.00 35.34 ? 43  LEU   B HD12 1 
ATOM   3075 H HD13 . LEU   B 1 63  ? -30.633 18.724 36.683 1.00 35.34 ? 43  LEU   B HD13 1 
ATOM   3076 H HD21 . LEU   B 1 63  ? -29.681 16.630 38.272 1.00 33.65 ? 43  LEU   B HD21 1 
ATOM   3077 H HD22 . LEU   B 1 63  ? -29.969 16.223 36.764 1.00 33.65 ? 43  LEU   B HD22 1 
ATOM   3078 H HD23 . LEU   B 1 63  ? -28.555 15.908 37.415 1.00 33.65 ? 43  LEU   B HD23 1 
ATOM   3079 N N    . LEU   B 1 64  ? -25.870 17.178 33.123 1.00 19.46 ? 44  LEU   B N    1 
ATOM   3080 C CA   . LEU   B 1 64  ? -25.485 16.986 31.732 1.00 20.05 ? 44  LEU   B CA   1 
ATOM   3081 C C    . LEU   B 1 64  ? -24.996 15.573 31.429 1.00 18.75 ? 44  LEU   B C    1 
ATOM   3082 O O    . LEU   B 1 64  ? -24.652 15.301 30.267 1.00 19.95 ? 44  LEU   B O    1 
ATOM   3083 C CB   . LEU   B 1 64  ? -24.438 18.023 31.334 1.00 19.97 ? 44  LEU   B CB   1 
ATOM   3084 C CG   . LEU   B 1 64  ? -24.817 19.496 31.502 1.00 20.55 ? 44  LEU   B CG   1 
ATOM   3085 C CD1  . LEU   B 1 64  ? -23.702 20.420 31.036 1.00 22.17 ? 44  LEU   B CD1  1 
ATOM   3086 C CD2  . LEU   B 1 64  ? -26.128 19.797 30.734 1.00 22.33 ? 44  LEU   B CD2  1 
ATOM   3087 H H    . LEU   B 1 64  ? -25.258 17.547 33.601 1.00 23.36 ? 44  LEU   B H    1 
ATOM   3088 H HA   . LEU   B 1 64  ? -26.262 17.133 31.169 1.00 24.07 ? 44  LEU   B HA   1 
ATOM   3089 H HB2  . LEU   B 1 64  ? -23.648 17.872 31.876 1.00 23.96 ? 44  LEU   B HB2  1 
ATOM   3090 H HB3  . LEU   B 1 64  ? -24.228 17.891 30.397 1.00 23.96 ? 44  LEU   B HB3  1 
ATOM   3091 H HG   . LEU   B 1 64  ? -24.958 19.673 32.446 1.00 24.66 ? 44  LEU   B HG   1 
ATOM   3092 H HD11 . LEU   B 1 64  ? -23.985 21.340 31.153 1.00 26.61 ? 44  LEU   B HD11 1 
ATOM   3093 H HD12 . LEU   B 1 64  ? -22.908 20.248 31.566 1.00 26.61 ? 44  LEU   B HD12 1 
ATOM   3094 H HD13 . LEU   B 1 64  ? -23.518 20.246 30.100 1.00 26.61 ? 44  LEU   B HD13 1 
ATOM   3095 H HD21 . LEU   B 1 64  ? -26.286 20.754 30.742 1.00 26.79 ? 44  LEU   B HD21 1 
ATOM   3096 H HD22 . LEU   B 1 64  ? -26.037 19.485 29.820 1.00 26.79 ? 44  LEU   B HD22 1 
ATOM   3097 H HD23 . LEU   B 1 64  ? -26.863 19.337 31.169 1.00 26.79 ? 44  LEU   B HD23 1 
ATOM   3098 N N    . PHE   B 1 65  ? -24.927 14.690 32.433 1.00 18.55 ? 45  PHE   B N    1 
ATOM   3099 C CA   . PHE   B 1 65  ? -24.434 13.328 32.300 1.00 18.69 ? 45  PHE   B CA   1 
ATOM   3100 C C    . PHE   B 1 65  ? -25.576 12.316 32.334 1.00 19.79 ? 45  PHE   B C    1 
ATOM   3101 O O    . PHE   B 1 65  ? -26.643 12.543 32.920 1.00 22.00 ? 45  PHE   B O    1 
ATOM   3102 C CB   . PHE   B 1 65  ? -23.458 12.975 33.440 1.00 19.08 ? 45  PHE   B CB   1 
ATOM   3103 C CG   . PHE   B 1 65  ? -22.120 13.682 33.353 1.00 18.31 ? 45  PHE   B CG   1 
ATOM   3104 C CD1  . PHE   B 1 65  ? -21.996 15.036 33.667 1.00 19.50 ? 45  PHE   B CD1  1 
ATOM   3105 C CD2  . PHE   B 1 65  ? -20.990 12.981 32.952 1.00 18.65 ? 45  PHE   B CD2  1 
ATOM   3106 C CE1  . PHE   B 1 65  ? -20.762 15.668 33.592 1.00 20.97 ? 45  PHE   B CE1  1 
ATOM   3107 C CE2  . PHE   B 1 65  ? -19.742 13.606 32.889 1.00 19.84 ? 45  PHE   B CE2  1 
ATOM   3108 C CZ   . PHE   B 1 65  ? -19.640 14.951 33.204 1.00 19.81 ? 45  PHE   B CZ   1 
ATOM   3109 H H    . PHE   B 1 65  ? -25.174 14.873 33.237 1.00 22.26 ? 45  PHE   B H    1 
ATOM   3110 H HA   . PHE   B 1 65  ? -23.980 13.262 31.445 1.00 22.43 ? 45  PHE   B HA   1 
ATOM   3111 H HB2  . PHE   B 1 65  ? -23.867 13.221 34.285 1.00 22.89 ? 45  PHE   B HB2  1 
ATOM   3112 H HB3  . PHE   B 1 65  ? -23.289 12.021 33.418 1.00 22.89 ? 45  PHE   B HB3  1 
ATOM   3113 H HD1  . PHE   B 1 65  ? -22.747 15.519 33.929 1.00 23.40 ? 45  PHE   B HD1  1 
ATOM   3114 H HD2  . PHE   B 1 65  ? -21.065 12.082 32.723 1.00 22.39 ? 45  PHE   B HD2  1 
ATOM   3115 H HE1  . PHE   B 1 65  ? -20.688 16.571 33.802 1.00 25.16 ? 45  PHE   B HE1  1 
ATOM   3116 H HE2  . PHE   B 1 65  ? -18.987 13.124 32.639 1.00 23.80 ? 45  PHE   B HE2  1 
ATOM   3117 H HZ   . PHE   B 1 65  ? -18.814 15.376 33.154 1.00 23.77 ? 45  PHE   B HZ   1 
ATOM   3118 N N    . THR   B 1 66  ? -25.313 11.156 31.742 1.00 20.68 ? 46  THR   B N    1 
ATOM   3119 C CA   . THR   B 1 66  ? -26.158 9.988  31.970 1.00 22.38 ? 46  THR   B CA   1 
ATOM   3120 C C    . THR   B 1 66  ? -26.069 9.564  33.438 1.00 22.42 ? 46  THR   B C    1 
ATOM   3121 O O    . THR   B 1 66  ? -25.146 9.924  34.151 1.00 21.83 ? 46  THR   B O    1 
ATOM   3122 C CB   . THR   B 1 66  ? -25.760 8.821  31.070 1.00 23.37 ? 46  THR   B CB   1 
ATOM   3123 O OG1  . THR   B 1 66  ? -24.428 8.410  31.395 1.00 23.67 ? 46  THR   B OG1  1 
ATOM   3124 C CG2  . THR   B 1 66  ? -25.732 9.204  29.598 1.00 24.55 ? 46  THR   B CG2  1 
ATOM   3125 H H    . THR   B 1 66  ? -24.654 11.018 31.206 1.00 24.82 ? 46  THR   B H    1 
ATOM   3126 H HA   . THR   B 1 66  ? -27.076 10.216 31.756 1.00 26.86 ? 46  THR   B HA   1 
ATOM   3127 H HB   . THR   B 1 66  ? -26.412 8.115  31.205 1.00 28.05 ? 46  THR   B HB   1 
ATOM   3128 H HG1  . THR   B 1 66  ? -24.421 8.023  32.140 1.00 28.41 ? 46  THR   B HG1  1 
ATOM   3129 H HG21 . THR   B 1 66  ? -25.509 8.429  29.058 1.00 29.46 ? 46  THR   B HG21 1 
ATOM   3130 H HG22 . THR   B 1 66  ? -26.601 9.537  29.326 1.00 29.46 ? 46  THR   B HG22 1 
ATOM   3131 H HG23 . THR   B 1 66  ? -25.068 9.895  29.448 1.00 29.46 ? 46  THR   B HG23 1 
ATOM   3132 N N    . GLU   B 1 67  ? -27.048 8.778  33.892 1.00 24.86 ? 47  GLU   B N    1 
ATOM   3133 C CA   . GLU   B 1 67  ? -27.055 8.357  35.291 1.00 26.97 ? 47  GLU   B CA   1 
ATOM   3134 C C    . GLU   B 1 67  ? -25.764 7.650  35.670 1.00 26.35 ? 47  GLU   B C    1 
ATOM   3135 O O    . GLU   B 1 67  ? -25.268 7.814  36.796 1.00 28.19 ? 47  GLU   B O    1 
ATOM   3136 C CB   . GLU   B 1 67  ? -28.233 7.418  35.582 1.00 30.80 ? 47  GLU   B CB   1 
ATOM   3137 C CG   . GLU   B 1 67  ? -28.360 6.955  37.047 1.00 34.52 ? 47  GLU   B CG   1 
ATOM   3138 H H    . GLU   B 1 67  ? -27.703 8.481  33.422 1.00 29.83 ? 47  GLU   B H    1 
ATOM   3139 H HA   . GLU   B 1 67  ? -27.156 9.158  35.828 1.00 32.36 ? 47  GLU   B HA   1 
ATOM   3140 H HB2  . GLU   B 1 67  ? -29.055 7.878  35.351 1.00 36.96 ? 47  GLU   B HB2  1 
ATOM   3141 H HB3  . GLU   B 1 67  ? -28.132 6.623  35.035 1.00 36.96 ? 47  GLU   B HB3  1 
ATOM   3142 N N    . ASP   B 1 68  ? -25.197 6.870  34.738 1.00 26.43 ? 48  ASP   B N    1 
ATOM   3143 C CA   . ASP   B 1 68  ? -23.961 6.134  34.964 1.00 27.42 ? 48  ASP   B CA   1 
ATOM   3144 C C    . ASP   B 1 68  ? -22.752 6.832  34.350 1.00 24.91 ? 48  ASP   B C    1 
ATOM   3145 O O    . ASP   B 1 68  ? -21.688 6.221  34.213 1.00 25.15 ? 48  ASP   B O    1 
ATOM   3146 C CB   . ASP   B 1 68  ? -24.087 4.707  34.420 1.00 31.54 ? 48  ASP   B CB   1 
ATOM   3147 C CG   . ASP   B 1 68  ? -24.276 4.662  32.890 1.00 37.23 ? 48  ASP   B CG   1 
ATOM   3148 O OD1  . ASP   B 1 68  ? -24.417 5.729  32.235 1.00 37.68 ? 48  ASP   B OD1  1 
ATOM   3149 O OD2  . ASP   B 1 68  ? -24.295 3.536  32.339 1.00 42.09 ? 48  ASP   B OD2  1 
ATOM   3150 H H    . ASP   B 1 68  ? -25.522 6.754  33.951 1.00 31.72 ? 48  ASP   B H    1 
ATOM   3151 H HA   . ASP   B 1 68  ? -23.811 6.072  35.921 1.00 32.90 ? 48  ASP   B HA   1 
ATOM   3152 H HB2  . ASP   B 1 68  ? -23.280 4.215  34.636 1.00 37.85 ? 48  ASP   B HB2  1 
ATOM   3153 H HB3  . ASP   B 1 68  ? -24.856 4.280  34.829 1.00 37.85 ? 48  ASP   B HB3  1 
ATOM   3154 N N    . GLY   B 1 69  ? -22.890 8.104  33.998 1.00 22.77 ? 49  GLY   B N    1 
ATOM   3155 C CA   . GLY   B 1 69  ? -21.792 8.814  33.377 1.00 22.04 ? 49  GLY   B CA   1 
ATOM   3156 C C    . GLY   B 1 69  ? -20.604 8.969  34.304 1.00 21.32 ? 49  GLY   B C    1 
ATOM   3157 O O    . GLY   B 1 69  ? -20.718 8.963  35.522 1.00 22.90 ? 49  GLY   B O    1 
ATOM   3158 H H    . GLY   B 1 69  ? -23.603 8.571  34.108 1.00 27.33 ? 49  GLY   B H    1 
ATOM   3159 H HA2  . GLY   B 1 69  ? -21.503 8.329  32.588 1.00 26.45 ? 49  GLY   B HA2  1 
ATOM   3160 H HA3  . GLY   B 1 69  ? -22.091 9.698  33.113 1.00 26.45 ? 49  GLY   B HA3  1 
ATOM   3161 N N    . VAL   B 1 70  ? -19.436 9.124  33.690 1.00 19.39 ? 50  VAL   B N    1 
ATOM   3162 C CA   . VAL   B 1 70  ? -18.162 9.238  34.393 1.00 19.26 ? 50  VAL   B CA   1 
ATOM   3163 C C    . VAL   B 1 70  ? -17.492 10.536 33.963 1.00 18.12 ? 50  VAL   B C    1 
ATOM   3164 O O    . VAL   B 1 70  ? -17.498 10.889 32.785 1.00 19.12 ? 50  VAL   B O    1 
ATOM   3165 C CB   . VAL   B 1 70  ? -17.258 8.024  34.071 1.00 21.04 ? 50  VAL   B CB   1 
ATOM   3166 C CG1  . VAL   B 1 70  ? -15.910 8.169  34.747 1.00 23.11 ? 50  VAL   B CG1  1 
ATOM   3167 C CG2  . VAL   B 1 70  ? -17.907 6.701  34.481 1.00 23.85 ? 50  VAL   B CG2  1 
ATOM   3168 H H    . VAL   B 1 70  ? -19.353 9.168  32.836 1.00 23.27 ? 50  VAL   B H    1 
ATOM   3169 H HA   . VAL   B 1 70  ? -18.311 9.277  35.351 1.00 23.12 ? 50  VAL   B HA   1 
ATOM   3170 H HB   . VAL   B 1 70  ? -17.131 8.002  33.109 1.00 25.25 ? 50  VAL   B HB   1 
ATOM   3171 H HG11 . VAL   B 1 70  ? -15.435 7.325  34.689 1.00 27.73 ? 50  VAL   B HG11 1 
ATOM   3172 H HG12 . VAL   B 1 70  ? -15.404 8.864  34.297 1.00 27.73 ? 50  VAL   B HG12 1 
ATOM   3173 H HG13 . VAL   B 1 70  ? -16.047 8.408  35.677 1.00 27.73 ? 50  VAL   B HG13 1 
ATOM   3174 H HG21 . VAL   B 1 70  ? -17.307 5.973  34.259 1.00 28.62 ? 50  VAL   B HG21 1 
ATOM   3175 H HG22 . VAL   B 1 70  ? -18.073 6.714  35.437 1.00 28.62 ? 50  VAL   B HG22 1 
ATOM   3176 H HG23 . VAL   B 1 70  ? -18.744 6.598  34.002 1.00 28.62 ? 50  VAL   B HG23 1 
ATOM   3177 N N    . GLY   B 1 71  ? -16.882 11.221 34.923 1.00 18.01 ? 51  GLY   B N    1 
ATOM   3178 C CA   . GLY   B 1 71  ? -16.050 12.377 34.637 1.00 17.87 ? 51  GLY   B CA   1 
ATOM   3179 C C    . GLY   B 1 71  ? -14.779 12.308 35.461 1.00 18.90 ? 51  GLY   B C    1 
ATOM   3180 O O    . GLY   B 1 71  ? -14.705 11.558 36.413 1.00 24.52 ? 51  GLY   B O    1 
ATOM   3181 H H    . GLY   B 1 71  ? -16.936 11.033 35.761 1.00 21.61 ? 51  GLY   B H    1 
ATOM   3182 H HA2  . GLY   B 1 71  ? -15.817 12.393 33.695 1.00 21.44 ? 51  GLY   B HA2  1 
ATOM   3183 H HA3  . GLY   B 1 71  ? -16.527 13.192 34.858 1.00 21.44 ? 51  GLY   B HA3  1 
ATOM   3184 N N    . GLY   B 1 72  ? -13.794 13.109 35.125 1.00 18.16 ? 52  GLY   B N    1 
ATOM   3185 C CA   . GLY   B 1 72  ? -12.651 13.243 35.993 1.00 18.66 ? 52  GLY   B CA   1 
ATOM   3186 C C    . GLY   B 1 72  ? -11.375 13.578 35.252 1.00 17.43 ? 52  GLY   B C    1 
ATOM   3187 O O    . GLY   B 1 72  ? -11.373 14.016 34.106 1.00 18.34 ? 52  GLY   B O    1 
ATOM   3188 H H    . GLY   B 1 72  ? -13.765 13.580 34.406 1.00 21.79 ? 52  GLY   B H    1 
ATOM   3189 H HA2  . GLY   B 1 72  ? -12.821 13.949 36.636 1.00 22.40 ? 52  GLY   B HA2  1 
ATOM   3190 H HA3  . GLY   B 1 72  ? -12.513 12.409 36.469 1.00 22.40 ? 52  GLY   B HA3  1 
ATOM   3191 N N    . LEU   B 1 73  ? -10.274 13.439 35.997 1.00 17.09 ? 53  LEU   B N    1 
ATOM   3192 C CA   . LEU   B 1 73  ? -8.942  13.899 35.642 1.00 17.70 ? 53  LEU   B CA   1 
ATOM   3193 C C    . LEU   B 1 73  ? -8.074  12.693 35.292 1.00 17.24 ? 53  LEU   B C    1 
ATOM   3194 O O    . LEU   B 1 73  ? -7.869  11.796 36.114 1.00 18.37 ? 53  LEU   B O    1 
ATOM   3195 C CB   . LEU   B 1 73  ? -8.364  14.702 36.810 1.00 18.13 ? 53  LEU   B CB   1 
ATOM   3196 C CG   . LEU   B 1 73  ? -6.916  15.106 36.588 1.00 18.06 ? 53  LEU   B CG   1 
ATOM   3197 C CD1  . LEU   B 1 73  ? -6.733  16.028 35.414 1.00 17.89 ? 53  LEU   B CD1  1 
ATOM   3198 C CD2  . LEU   B 1 73  ? -6.391  15.780 37.870 1.00 19.82 ? 53  LEU   B CD2  1 
ATOM   3199 H H    . LEU   B 1 73  ? -10.281 13.053 36.766 1.00 20.51 ? 53  LEU   B H    1 
ATOM   3200 H HA   . LEU   B 1 73  ? -8.964  14.463 34.854 1.00 21.24 ? 53  LEU   B HA   1 
ATOM   3201 H HB2  . LEU   B 1 73  ? -8.888  15.511 36.926 1.00 21.75 ? 53  LEU   B HB2  1 
ATOM   3202 H HB3  . LEU   B 1 73  ? -8.406  14.163 37.615 1.00 21.75 ? 53  LEU   B HB3  1 
ATOM   3203 H HG   . LEU   B 1 73  ? -6.405  14.307 36.384 1.00 21.67 ? 53  LEU   B HG   1 
ATOM   3204 H HD11 . LEU   B 1 73  ? -5.795  16.260 35.338 1.00 21.47 ? 53  LEU   B HD11 1 
ATOM   3205 H HD12 . LEU   B 1 73  ? -7.028  15.575 34.608 1.00 21.47 ? 53  LEU   B HD12 1 
ATOM   3206 H HD13 . LEU   B 1 73  ? -7.262  16.828 35.556 1.00 21.47 ? 53  LEU   B HD13 1 
ATOM   3207 H HD21 . LEU   B 1 73  ? -5.438  15.938 37.777 1.00 23.79 ? 53  LEU   B HD21 1 
ATOM   3208 H HD22 . LEU   B 1 73  ? -6.855  16.622 37.997 1.00 23.79 ? 53  LEU   B HD22 1 
ATOM   3209 H HD23 . LEU   B 1 73  ? -6.556  15.194 38.626 1.00 23.79 ? 53  LEU   B HD23 1 
ATOM   3210 N N    . TRP   B 1 74  ? -7.593  12.658 34.055 1.00 16.96 ? 54  TRP   B N    1 
ATOM   3211 C CA   . TRP   B 1 74  ? -6.873  11.484 33.579 1.00 18.34 ? 54  TRP   B CA   1 
ATOM   3212 C C    . TRP   B 1 74  ? -5.367  11.596 33.730 1.00 19.46 ? 54  TRP   B C    1 
ATOM   3213 O O    . TRP   B 1 74  ? -4.678  10.612 33.462 1.00 23.78 ? 54  TRP   B O    1 
ATOM   3214 C CB   . TRP   B 1 74  ? -7.281  11.192 32.112 1.00 18.56 ? 54  TRP   B CB   1 
ATOM   3215 C CG   . TRP   B 1 74  ? -8.198  10.009 32.004 1.00 18.13 ? 54  TRP   B CG   1 
ATOM   3216 C CD1  . TRP   B 1 74  ? -7.942  8.839  31.367 1.00 21.03 ? 54  TRP   B CD1  1 
ATOM   3217 C CD2  . TRP   B 1 74  ? -9.510  9.873  32.578 1.00 18.52 ? 54  TRP   B CD2  1 
ATOM   3218 N NE1  . TRP   B 1 74  ? -9.001  7.981  31.492 1.00 22.69 ? 54  TRP   B NE1  1 
ATOM   3219 C CE2  . TRP   B 1 74  ? -9.965  8.576  32.261 1.00 21.25 ? 54  TRP   B CE2  1 
ATOM   3220 C CE3  . TRP   B 1 74  ? -10.342 10.720 33.329 1.00 19.48 ? 54  TRP   B CE3  1 
ATOM   3221 C CZ2  . TRP   B 1 74  ? -11.215 8.104  32.659 1.00 22.97 ? 54  TRP   B CZ2  1 
ATOM   3222 C CZ3  . TRP   B 1 74  ? -11.591 10.239 33.750 1.00 21.45 ? 54  TRP   B CZ3  1 
ATOM   3223 C CH2  . TRP   B 1 74  ? -11.996 8.935  33.418 1.00 22.17 ? 54  TRP   B CH2  1 
ATOM   3224 H H    . TRP   B 1 74  ? -7.669  13.294 33.481 1.00 20.36 ? 54  TRP   B H    1 
ATOM   3225 H HA   . TRP   B 1 74  ? -7.129  10.709 34.103 1.00 22.01 ? 54  TRP   B HA   1 
ATOM   3226 H HB2  . TRP   B 1 74  ? -7.741  11.965 31.749 1.00 22.28 ? 54  TRP   B HB2  1 
ATOM   3227 H HB3  . TRP   B 1 74  ? -6.484  11.005 31.591 1.00 22.28 ? 54  TRP   B HB3  1 
ATOM   3228 H HD1  . TRP   B 1 74  ? -7.156  8.647  30.908 1.00 25.24 ? 54  TRP   B HD1  1 
ATOM   3229 H HE1  . TRP   B 1 74  ? -9.053  7.196  31.144 1.00 27.24 ? 54  TRP   B HE1  1 
ATOM   3230 H HE3  . TRP   B 1 74  ? -10.070 11.584 33.543 1.00 23.38 ? 54  TRP   B HE3  1 
ATOM   3231 H HZ2  . TRP   B 1 74  ? -11.508 7.255  32.418 1.00 27.56 ? 54  TRP   B HZ2  1 
ATOM   3232 H HZ3  . TRP   B 1 74  ? -12.154 10.785 34.251 1.00 25.74 ? 54  TRP   B HZ3  1 
ATOM   3233 H HH2  . TRP   B 1 74  ? -12.818 8.627  33.723 1.00 26.61 ? 54  TRP   B HH2  1 
ATOM   3234 N N    . THR   B 1 75  ? -4.853  12.741 34.164 1.00 17.00 ? 55  THR   B N    1 
ATOM   3235 C CA   . THR   B 1 75  ? -3.419  12.998 34.279 1.00 16.22 ? 55  THR   B CA   1 
ATOM   3236 C C    . THR   B 1 75  ? -3.144  13.464 35.705 1.00 17.00 ? 55  THR   B C    1 
ATOM   3237 O O    . THR   B 1 75  ? -3.445  14.610 36.058 1.00 18.31 ? 55  THR   B O    1 
ATOM   3238 C CB   . THR   B 1 75  ? -3.014  14.063 33.262 1.00 16.80 ? 55  THR   B CB   1 
ATOM   3239 O OG1  . THR   B 1 75  ? -3.890  15.192 33.360 1.00 16.99 ? 55  THR   B OG1  1 
ATOM   3240 C CG2  . THR   B 1 75  ? -3.045  13.527 31.823 1.00 17.85 ? 55  THR   B CG2  1 
ATOM   3241 H H    . THR   B 1 75  ? -5.333  13.412 34.408 1.00 20.40 ? 55  THR   B H    1 
ATOM   3242 H HA   . THR   B 1 75  ? -2.910  12.187 34.123 1.00 19.46 ? 55  THR   B HA   1 
ATOM   3243 H HB   . THR   B 1 75  ? -2.103  14.334 33.455 1.00 20.16 ? 55  THR   B HB   1 
ATOM   3244 H HG1  . THR   B 1 75  ? -3.851  15.520 34.132 1.00 20.39 ? 55  THR   B HG1  1 
ATOM   3245 H HG21 . THR   B 1 75  ? -2.769  14.221 31.204 1.00 21.42 ? 55  THR   B HG21 1 
ATOM   3246 H HG22 . THR   B 1 75  ? -2.443  12.771 31.737 1.00 21.42 ? 55  THR   B HG22 1 
ATOM   3247 H HG23 . THR   B 1 75  ? -3.944  13.241 31.595 1.00 21.42 ? 55  THR   B HG23 1 
ATOM   3248 N N    . THR   B 1 76  ? -2.578  12.580 36.519 1.00 18.89 ? 56  THR   B N    1 
ATOM   3249 C CA   . THR   B 1 76  ? -2.310  12.886 37.918 1.00 19.80 ? 56  THR   B CA   1 
ATOM   3250 C C    . THR   B 1 76  ? -0.893  12.450 38.296 1.00 18.92 ? 56  THR   B C    1 
ATOM   3251 O O    . THR   B 1 76  ? -0.202  11.745 37.549 1.00 19.64 ? 56  THR   B O    1 
ATOM   3252 C CB   . THR   B 1 76  ? -3.292  12.186 38.891 1.00 24.36 ? 56  THR   B CB   1 
ATOM   3253 O OG1  . THR   B 1 76  ? -2.971  10.792 38.950 1.00 29.72 ? 56  THR   B OG1  1 
ATOM   3254 C CG2  . THR   B 1 76  ? -4.745  12.359 38.450 1.00 24.80 ? 56  THR   B CG2  1 
ATOM   3255 H H    . THR   B 1 76  ? -2.338  11.789 36.281 1.00 22.67 ? 56  THR   B H    1 
ATOM   3256 H HA   . THR   B 1 76  ? -2.397  13.847 38.013 1.00 23.76 ? 56  THR   B HA   1 
ATOM   3257 H HB   . THR   B 1 76  ? -3.210  12.587 39.771 1.00 29.23 ? 56  THR   B HB   1 
ATOM   3258 H HG1  . THR   B 1 76  ? -3.516  10.393 39.449 1.00 35.66 ? 56  THR   B HG1  1 
ATOM   3259 H HG21 . THR   B 1 76  ? -5.342  12.035 39.142 1.00 29.76 ? 56  THR   B HG21 1 
ATOM   3260 H HG22 . THR   B 1 76  ? -4.932  13.297 38.286 1.00 29.76 ? 56  THR   B HG22 1 
ATOM   3261 H HG23 . THR   B 1 76  ? -4.906  11.858 37.635 1.00 29.76 ? 56  THR   B HG23 1 
ATOM   3262 N N    . ASP   B 1 77  ? -0.489  12.849 39.506 1.00 20.05 ? 57  ASP   B N    1 
ATOM   3263 C CA   . ASP   B 1 77  ? 0.830   12.503 40.008 1.00 22.11 ? 57  ASP   B CA   1 
ATOM   3264 C C    . ASP   B 1 77  ? 1.005   11.003 40.097 1.00 24.09 ? 57  ASP   B C    1 
ATOM   3265 O O    . ASP   B 1 77  ? 2.096   10.493 39.863 1.00 25.43 ? 57  ASP   B O    1 
ATOM   3266 C CB   . ASP   B 1 77  ? 1.154   13.178 41.356 1.00 23.33 ? 57  ASP   B CB   1 
ATOM   3267 C CG   . ASP   B 1 77  ? 0.218   12.798 42.501 1.00 27.02 ? 57  ASP   B CG   1 
ATOM   3268 O OD1  . ASP   B 1 77  ? -0.989  12.953 42.399 1.00 29.85 ? 57  ASP   B OD1  1 
ATOM   3269 O OD2  . ASP   B 1 77  ? 0.726   12.350 43.546 1.00 30.73 ? 57  ASP   B OD2  1 
ATOM   3270 H H    . ASP   B 1 77  ? -0.962  13.318 40.050 1.00 24.07 ? 57  ASP   B H    1 
ATOM   3271 H HA   . ASP   B 1 77  ? 1.475   12.857 39.376 1.00 26.54 ? 57  ASP   B HA   1 
ATOM   3272 H HB2  . ASP   B 1 77  ? 2.053   12.927 41.619 1.00 27.99 ? 57  ASP   B HB2  1 
ATOM   3273 H HB3  . ASP   B 1 77  ? 1.098   14.140 41.241 1.00 27.99 ? 57  ASP   B HB3  1 
ATOM   3274 N N    . SER   B 1 78  ? -0.039  10.282 40.490 1.00 24.50 ? 58  SER   B N    1 
ATOM   3275 C CA   . SER   B 1 78  ? 0.119   8.861  40.742 1.00 27.17 ? 58  SER   B CA   1 
ATOM   3276 C C    . SER   B 1 78  ? 0.145   8.059  39.460 1.00 27.46 ? 58  SER   B C    1 
ATOM   3277 O O    . SER   B 1 78  ? 0.539   6.895  39.479 1.00 30.61 ? 58  SER   B O    1 
ATOM   3278 C CB   . SER   B 1 78  ? -1.054  8.379  41.602 1.00 29.79 ? 58  SER   B CB   1 
ATOM   3279 O OG   . SER   B 1 78  ? -2.272  8.452  40.877 1.00 31.99 ? 58  SER   B OG   1 
ATOM   3280 H H    . SER   B 1 78  ? -0.833  10.589 40.615 1.00 29.40 ? 58  SER   B H    1 
ATOM   3281 H HA   . SER   B 1 78  ? 0.949   8.704  41.218 1.00 32.61 ? 58  SER   B HA   1 
ATOM   3282 H HB2  . SER   B 1 78  ? -0.896  7.458  41.864 1.00 35.75 ? 58  SER   B HB2  1 
ATOM   3283 H HB3  . SER   B 1 78  ? -1.120  8.941  42.390 1.00 35.75 ? 58  SER   B HB3  1 
ATOM   3284 H HG   . SER   B 1 78  ? -2.426  9.247  40.654 1.00 38.39 ? 58  SER   B HG   1 
ATOM   3285 N N    . GLY   B 1 79  ? -0.290  8.647  38.357 1.00 25.77 ? 59  GLY   B N    1 
ATOM   3286 C CA   . GLY   B 1 79  ? -0.424  7.939  37.109 1.00 26.82 ? 59  GLY   B CA   1 
ATOM   3287 C C    . GLY   B 1 79  ? -1.749  7.236  36.885 1.00 29.22 ? 59  GLY   B C    1 
ATOM   3288 O O    . GLY   B 1 79  ? -1.949  6.663  35.810 1.00 34.03 ? 59  GLY   B O    1 
ATOM   3289 H H    . GLY   B 1 79  ? -0.519  9.475  38.311 1.00 30.92 ? 59  GLY   B H    1 
ATOM   3290 H HA2  . GLY   B 1 79  ? -0.303  8.572  36.383 1.00 32.18 ? 59  GLY   B HA2  1 
ATOM   3291 H HA3  . GLY   B 1 79  ? 0.275   7.268  37.062 1.00 32.18 ? 59  GLY   B HA3  1 
ATOM   3292 N N    . GLN   B 1 80  ? -2.648  7.228  37.864 1.00 26.90 ? 60  GLN   B N    1 
ATOM   3293 C CA   . GLN   B 1 80  ? -3.981  6.669  37.680 1.00 28.20 ? 60  GLN   B CA   1 
ATOM   3294 C C    . GLN   B 1 80  ? -5.007  7.785  37.575 1.00 24.72 ? 60  GLN   B C    1 
ATOM   3295 O O    . GLN   B 1 80  ? -4.878  8.798  38.270 1.00 26.15 ? 60  GLN   B O    1 
ATOM   3296 C CB   . GLN   B 1 80  ? -4.365  5.778  38.867 1.00 32.61 ? 60  GLN   B CB   1 
ATOM   3297 C CG   . GLN   B 1 80  ? -3.510  4.515  38.962 1.00 39.90 ? 60  GLN   B CG   1 
ATOM   3298 C CD   . GLN   B 1 80  ? -3.595  3.656  37.709 1.00 45.62 ? 60  GLN   B CD   1 
ATOM   3299 O OE1  . GLN   B 1 80  ? -4.684  3.388  37.193 1.00 48.26 ? 60  GLN   B OE1  1 
ATOM   3300 N NE2  . GLN   B 1 80  ? -2.442  3.229  37.208 1.00 48.18 ? 60  GLN   B NE2  1 
ATOM   3301 H H    . GLN   B 1 80  ? -2.508  7.545  38.651 1.00 32.28 ? 60  GLN   B H    1 
ATOM   3302 H HA   . GLN   B 1 80  ? -3.999  6.137  36.869 1.00 33.85 ? 60  GLN   B HA   1 
ATOM   3303 H HB2  . GLN   B 1 80  ? -4.250  6.281  39.689 1.00 39.13 ? 60  GLN   B HB2  1 
ATOM   3304 H HB3  . GLN   B 1 80  ? -5.291  5.506  38.771 1.00 39.13 ? 60  GLN   B HB3  1 
ATOM   3305 H HG2  . GLN   B 1 80  ? -2.583  4.770  39.090 1.00 47.89 ? 60  GLN   B HG2  1 
ATOM   3306 H HG3  . GLN   B 1 80  ? -3.815  3.983  39.714 1.00 47.89 ? 60  GLN   B HG3  1 
ATOM   3307 H HE21 . GLN   B 1 80  ? -1.702  3.442  37.592 1.00 57.82 ? 60  GLN   B HE21 1 
ATOM   3308 H HE22 . GLN   B 1 80  ? -2.435  2.741  36.501 1.00 57.82 ? 60  GLN   B HE22 1 
ATOM   3309 N N    . PRO   B 1 81  ? -6.027  7.649  36.721 1.00 24.82 ? 61  PRO   B N    1 
ATOM   3310 C CA   . PRO   B 1 81  ? -7.072  8.679  36.662 1.00 22.58 ? 61  PRO   B CA   1 
ATOM   3311 C C    . PRO   B 1 81  ? -7.821  8.777  37.973 1.00 21.89 ? 61  PRO   B C    1 
ATOM   3312 O O    . PRO   B 1 81  ? -7.926  7.808  38.725 1.00 24.79 ? 61  PRO   B O    1 
ATOM   3313 C CB   . PRO   B 1 81  ? -8.007  8.179  35.552 1.00 24.24 ? 61  PRO   B CB   1 
ATOM   3314 C CG   . PRO   B 1 81  ? -7.104  7.364  34.645 1.00 28.27 ? 61  PRO   B CG   1 
ATOM   3315 C CD   . PRO   B 1 81  ? -6.157  6.676  35.618 1.00 28.16 ? 61  PRO   B CD   1 
ATOM   3316 H HA   . PRO   B 1 81  ? -6.690  9.538  36.422 1.00 27.09 ? 61  PRO   B HA   1 
ATOM   3317 H HB2  . PRO   B 1 81  ? -8.711  7.629  35.931 1.00 29.09 ? 61  PRO   B HB2  1 
ATOM   3318 H HB3  . PRO   B 1 81  ? -8.394  8.931  35.077 1.00 29.09 ? 61  PRO   B HB3  1 
ATOM   3319 H HG2  . PRO   B 1 81  ? -7.625  6.718  34.143 1.00 33.93 ? 61  PRO   B HG2  1 
ATOM   3320 H HG3  . PRO   B 1 81  ? -6.623  7.947  34.037 1.00 33.93 ? 61  PRO   B HG3  1 
ATOM   3321 H HD2  . PRO   B 1 81  ? -6.537  5.842  35.937 1.00 33.79 ? 61  PRO   B HD2  1 
ATOM   3322 H HD3  . PRO   B 1 81  ? -5.296  6.510  35.202 1.00 33.79 ? 61  PRO   B HD3  1 
ATOM   3323 N N    . ILE   B 1 82  ? -8.335  9.969  38.237 1.00 20.35 ? 62  ILE   B N    1 
ATOM   3324 C CA   . ILE   B 1 82  ? -9.323  10.194 39.287 1.00 21.59 ? 62  ILE   B CA   1 
ATOM   3325 C C    . ILE   B 1 82  ? -10.663 10.261 38.571 1.00 20.92 ? 62  ILE   B C    1 
ATOM   3326 O O    . ILE   B 1 82  ? -11.023 11.291 37.981 1.00 22.88 ? 62  ILE   B O    1 
ATOM   3327 C CB   . ILE   B 1 82  ? -9.040  11.461 40.101 1.00 24.67 ? 62  ILE   B CB   1 
ATOM   3328 C CG1  . ILE   B 1 82  ? -7.662  11.340 40.771 1.00 27.07 ? 62  ILE   B CG1  1 
ATOM   3329 C CG2  . ILE   B 1 82  ? -10.187 11.702 41.136 1.00 27.51 ? 62  ILE   B CG2  1 
ATOM   3330 C CD1  . ILE   B 1 82  ? -7.169  12.626 41.370 1.00 30.53 ? 62  ILE   B CD1  1 
ATOM   3331 H H    . ILE   B 1 82  ? -8.122  10.685 37.811 1.00 24.43 ? 62  ILE   B H    1 
ATOM   3332 H HA   . ILE   B 1 82  ? -9.321  9.449  39.908 1.00 25.91 ? 62  ILE   B HA   1 
ATOM   3333 H HB   . ILE   B 1 82  ? -9.018  12.234 39.516 1.00 29.61 ? 62  ILE   B HB   1 
ATOM   3334 H HG12 . ILE   B 1 82  ? -7.717  10.683 41.482 1.00 32.49 ? 62  ILE   B HG12 1 
ATOM   3335 H HG13 . ILE   B 1 82  ? -7.015  11.056 40.106 1.00 32.49 ? 62  ILE   B HG13 1 
ATOM   3336 H HG21 . ILE   B 1 82  ? -9.942  12.442 41.713 1.00 33.01 ? 62  ILE   B HG21 1 
ATOM   3337 H HG22 . ILE   B 1 82  ? -11.005 11.912 40.658 1.00 33.01 ? 62  ILE   B HG22 1 
ATOM   3338 H HG23 . ILE   B 1 82  ? -10.310 10.897 41.664 1.00 33.01 ? 62  ILE   B HG23 1 
ATOM   3339 H HD11 . ILE   B 1 82  ? -6.273  12.491 41.715 1.00 36.63 ? 62  ILE   B HD11 1 
ATOM   3340 H HD12 . ILE   B 1 82  ? -7.160  13.311 40.684 1.00 36.63 ? 62  ILE   B HD12 1 
ATOM   3341 H HD13 . ILE   B 1 82  ? -7.765  12.888 42.090 1.00 36.63 ? 62  ILE   B HD13 1 
ATOM   3342 N N    . ALA   B 1 83  ? -11.369 9.137  38.564 1.00 21.99 ? 63  ALA   B N    1 
ATOM   3343 C CA   . ALA   B 1 83  ? -12.631 9.010  37.858 1.00 23.23 ? 63  ALA   B CA   1 
ATOM   3344 C C    . ALA   B 1 83  ? -13.759 9.093  38.875 1.00 23.67 ? 63  ALA   B C    1 
ATOM   3345 O O    . ALA   B 1 83  ? -13.750 8.393  39.896 1.00 27.18 ? 63  ALA   B O    1 
ATOM   3346 C CB   . ALA   B 1 83  ? -12.687 7.679  37.103 1.00 26.57 ? 63  ALA   B CB   1 
ATOM   3347 H H    . ALA   B 1 83  ? -11.130 8.418  38.971 1.00 26.39 ? 63  ALA   B H    1 
ATOM   3348 H HA   . ALA   B 1 83  ? -12.736 9.727  37.214 1.00 27.88 ? 63  ALA   B HA   1 
ATOM   3349 H HB1  . ALA   B 1 83  ? -13.535 7.616  36.636 1.00 31.88 ? 63  ALA   B HB1  1 
ATOM   3350 H HB2  . ALA   B 1 83  ? -11.956 7.645  36.467 1.00 31.88 ? 63  ALA   B HB2  1 
ATOM   3351 H HB3  . ALA   B 1 83  ? -12.606 6.951  37.739 1.00 31.88 ? 63  ALA   B HB3  1 
ATOM   3352 N N    . ILE   B 1 84  ? -14.728 9.943  38.581 1.00 21.49 ? 64  ILE   B N    1 
ATOM   3353 C CA   . ILE   B 1 84  ? -15.888 10.167 39.417 1.00 22.97 ? 64  ILE   B CA   1 
ATOM   3354 C C    . ILE   B 1 84  ? -17.045 9.474  38.709 1.00 23.06 ? 64  ILE   B C    1 
ATOM   3355 O O    . ILE   B 1 84  ? -17.435 9.878  37.606 1.00 22.91 ? 64  ILE   B O    1 
ATOM   3356 C CB   . ILE   B 1 84  ? -16.133 11.677 39.580 1.00 26.37 ? 64  ILE   B CB   1 
ATOM   3357 C CG1  . ILE   B 1 84  ? -14.853 12.400 40.041 1.00 29.64 ? 64  ILE   B CG1  1 
ATOM   3358 C CG2  . ILE   B 1 84  ? -17.303 11.915 40.524 1.00 27.46 ? 64  ILE   B CG2  1 
ATOM   3359 C CD1  . ILE   B 1 84  ? -14.393 11.977 41.367 1.00 34.96 ? 64  ILE   B CD1  1 
ATOM   3360 H H    . ILE   B 1 84  ? -14.734 10.424 37.868 1.00 25.78 ? 64  ILE   B H    1 
ATOM   3361 H HA   . ILE   B 1 84  ? -15.785 9.780  40.300 1.00 27.56 ? 64  ILE   B HA   1 
ATOM   3362 H HB   . ILE   B 1 84  ? -16.367 12.052 38.717 1.00 31.64 ? 64  ILE   B HB   1 
ATOM   3363 H HG12 . ILE   B 1 84  ? -14.143 12.216 39.406 1.00 35.57 ? 64  ILE   B HG12 1 
ATOM   3364 H HG13 . ILE   B 1 84  ? -15.027 13.354 40.076 1.00 35.57 ? 64  ILE   B HG13 1 
ATOM   3365 H HG21 . ILE   B 1 84  ? -17.367 12.864 40.715 1.00 32.95 ? 64  ILE   B HG21 1 
ATOM   3366 H HG22 . ILE   B 1 84  ? -18.119 11.607 40.099 1.00 32.95 ? 64  ILE   B HG22 1 
ATOM   3367 H HG23 . ILE   B 1 84  ? -17.151 11.422 41.345 1.00 32.95 ? 64  ILE   B HG23 1 
ATOM   3368 H HD11 . ILE   B 1 84  ? -13.587 12.467 41.592 1.00 41.95 ? 64  ILE   B HD11 1 
ATOM   3369 H HD12 . ILE   B 1 84  ? -15.087 12.165 42.017 1.00 41.95 ? 64  ILE   B HD12 1 
ATOM   3370 H HD13 . ILE   B 1 84  ? -14.207 11.025 41.347 1.00 41.95 ? 64  ILE   B HD13 1 
ATOM   3371 N N    . ARG   B 1 85  ? -17.594 8.447  39.332 1.00 25.03 ? 65  ARG   B N    1 
ATOM   3372 C CA   . ARG   B 1 85  ? -18.443 7.480  38.652 1.00 25.95 ? 65  ARG   B CA   1 
ATOM   3373 C C    . ARG   B 1 85  ? -19.897 7.619  39.059 1.00 25.75 ? 65  ARG   B C    1 
ATOM   3374 O O    . ARG   B 1 85  ? -20.278 7.290  40.192 1.00 27.88 ? 65  ARG   B O    1 
ATOM   3375 C CB   . ARG   B 1 85  ? -17.944 6.066  38.933 1.00 28.60 ? 65  ARG   B CB   1 
ATOM   3376 C CG   . ARG   B 1 85  ? -16.535 5.833  38.361 1.00 30.24 ? 65  ARG   B CG   1 
ATOM   3377 C CD   . ARG   B 1 85  ? -16.056 4.409  38.571 1.00 32.93 ? 65  ARG   B CD   1 
ATOM   3378 N NE   . ARG   B 1 85  ? -14.694 4.235  38.081 1.00 35.76 ? 65  ARG   B NE   1 
ATOM   3379 C CZ   . ARG   B 1 85  ? -14.375 4.072  36.803 1.00 38.54 ? 65  ARG   B CZ   1 
ATOM   3380 N NH1  . ARG   B 1 85  ? -15.305 4.014  35.862 1.00 38.58 ? 65  ARG   B NH1  1 
ATOM   3381 N NH2  . ARG   B 1 85  ? -13.094 3.972  36.462 1.00 41.82 ? 65  ARG   B NH2  1 
ATOM   3382 H H    . ARG   B 1 85  ? -17.488 8.283  40.169 1.00 30.04 ? 65  ARG   B H    1 
ATOM   3383 H HA   . ARG   B 1 85  ? -18.408 7.678  37.703 1.00 31.14 ? 65  ARG   B HA   1 
ATOM   3384 H HB2  . ARG   B 1 85  ? -17.910 5.924  39.892 1.00 34.32 ? 65  ARG   B HB2  1 
ATOM   3385 H HB3  . ARG   B 1 85  ? -18.548 5.426  38.525 1.00 34.32 ? 65  ARG   B HB3  1 
ATOM   3386 H HG2  . ARG   B 1 85  ? -16.546 6.010  37.407 1.00 36.29 ? 65  ARG   B HG2  1 
ATOM   3387 H HG3  . ARG   B 1 85  ? -15.910 6.429  38.802 1.00 36.29 ? 65  ARG   B HG3  1 
ATOM   3388 H HD2  . ARG   B 1 85  ? -16.071 4.200  39.518 1.00 39.52 ? 65  ARG   B HD2  1 
ATOM   3389 H HD3  . ARG   B 1 85  ? -16.636 3.799  38.088 1.00 39.52 ? 65  ARG   B HD3  1 
ATOM   3390 H HE   . ARG   B 1 85  ? -14.056 4.240  38.657 1.00 42.92 ? 65  ARG   B HE   1 
ATOM   3391 H HH11 . ARG   B 1 85  ? -16.136 4.083  36.074 1.00 46.30 ? 65  ARG   B HH11 1 
ATOM   3392 H HH12 . ARG   B 1 85  ? -15.078 3.908  35.040 1.00 46.30 ? 65  ARG   B HH12 1 
ATOM   3393 H HH21 . ARG   B 1 85  ? -12.483 4.013  37.067 1.00 50.18 ? 65  ARG   B HH21 1 
ATOM   3394 H HH22 . ARG   B 1 85  ? -12.875 3.865  35.637 1.00 50.18 ? 65  ARG   B HH22 1 
ATOM   3395 N N    . GLY   B 1 86  ? -20.701 8.065  38.114 1.00 25.37 ? 66  GLY   B N    1 
ATOM   3396 C CA   . GLY   B 1 86  ? -22.120 8.174  38.313 1.00 26.13 ? 66  GLY   B CA   1 
ATOM   3397 C C    . GLY   B 1 86  ? -22.556 9.593  38.568 1.00 26.07 ? 66  GLY   B C    1 
ATOM   3398 O O    . GLY   B 1 86  ? -21.845 10.402 39.186 1.00 26.00 ? 66  GLY   B O    1 
ATOM   3399 H H    . GLY   B 1 86  ? -20.438 8.315  37.334 1.00 30.44 ? 66  GLY   B H    1 
ATOM   3400 H HA2  . GLY   B 1 86  ? -22.581 7.850  37.524 1.00 31.36 ? 66  GLY   B HA2  1 
ATOM   3401 H HA3  . GLY   B 1 86  ? -22.380 7.633  39.075 1.00 31.36 ? 66  GLY   B HA3  1 
ATOM   3402 N N    A ARG   B 1 87  ? -23.757 9.906  38.089 0.57 27.88 ? 67  ARG   B N    1 
ATOM   3403 N N    B ARG   B 1 87  ? -23.764 9.899  38.099 0.43 29.26 ? 67  ARG   B N    1 
ATOM   3404 C CA   A ARG   B 1 87  ? -24.280 11.257 38.215 0.57 29.04 ? 67  ARG   B CA   1 
ATOM   3405 C CA   B ARG   B 1 87  ? -24.303 11.246 38.216 0.43 31.33 ? 67  ARG   B CA   1 
ATOM   3406 C C    A ARG   B 1 87  ? -24.340 11.702 39.674 0.57 28.11 ? 67  ARG   B C    1 
ATOM   3407 C C    B ARG   B 1 87  ? -24.355 11.702 39.669 0.43 31.25 ? 67  ARG   B C    1 
ATOM   3408 O O    A ARG   B 1 87  ? -24.011 12.851 39.984 0.57 29.96 ? 67  ARG   B O    1 
ATOM   3409 O O    B ARG   B 1 87  ? -24.056 12.863 39.966 0.43 33.17 ? 67  ARG   B O    1 
ATOM   3410 C CB   A ARG   B 1 87  ? -25.642 11.309 37.525 0.57 28.87 ? 67  ARG   B CB   1 
ATOM   3411 C CB   B ARG   B 1 87  ? -25.687 11.262 37.568 0.43 31.39 ? 67  ARG   B CB   1 
ATOM   3412 C CG   A ARG   B 1 87  ? -26.186 12.666 37.331 0.57 26.98 ? 67  ARG   B CG   1 
ATOM   3413 C CG   B ARG   B 1 87  ? -26.179 12.606 37.129 0.43 28.61 ? 67  ARG   B CG   1 
ATOM   3414 C CD   A ARG   B 1 87  ? -27.625 12.625 36.979 0.57 29.08 ? 67  ARG   B CD   1 
ATOM   3415 C CD   B ARG   B 1 87  ? -27.463 12.459 36.323 0.43 26.77 ? 67  ARG   B CD   1 
ATOM   3416 N NE   A ARG   B 1 87  ? -27.847 12.988 35.594 0.57 28.89 ? 67  ARG   B NE   1 
ATOM   3417 N NE   B ARG   B 1 87  ? -28.406 11.581 37.010 0.43 28.90 ? 67  ARG   B NE   1 
ATOM   3418 C CZ   A ARG   B 1 87  ? -28.996 12.823 34.961 0.57 28.16 ? 67  ARG   B CZ   1 
ATOM   3419 C CZ   B ARG   B 1 87  ? -29.418 10.946 36.433 0.43 32.32 ? 67  ARG   B CZ   1 
ATOM   3420 N NH1  A ARG   B 1 87  ? -30.027 12.232 35.552 0.57 30.72 ? 67  ARG   B NH1  1 
ATOM   3421 N NH1  B ARG   B 1 87  ? -29.677 11.082 35.145 0.43 34.15 ? 67  ARG   B NH1  1 
ATOM   3422 N NH2  A ARG   B 1 87  ? -29.111 13.274 33.716 0.57 25.92 ? 67  ARG   B NH2  1 
ATOM   3423 N NH2  B ARG   B 1 87  ? -30.176 10.137 37.169 0.43 32.65 ? 67  ARG   B NH2  1 
ATOM   3424 H H    A ARG   B 1 87  ? -24.284 9.357  37.689 0.57 33.46 ? 67  ARG   B H    1 
ATOM   3425 H H    B ARG   B 1 87  ? -24.292 9.344  37.709 0.43 35.12 ? 67  ARG   B H    1 
ATOM   3426 H HA   A ARG   B 1 87  ? -23.697 11.893 37.772 0.57 34.85 ? 67  ARG   B HA   1 
ATOM   3427 H HA   B ARG   B 1 87  ? -23.734 11.879 37.751 0.43 37.60 ? 67  ARG   B HA   1 
ATOM   3428 H HB2  A ARG   B 1 87  ? -25.559 10.900 36.649 0.57 34.65 ? 67  ARG   B HB2  1 
ATOM   3429 H HB2  B ARG   B 1 87  ? -25.663 10.694 36.782 0.43 37.66 ? 67  ARG   B HB2  1 
ATOM   3430 H HB3  A ARG   B 1 87  ? -26.279 10.813 38.063 0.57 34.65 ? 67  ARG   B HB3  1 
ATOM   3431 H HB3  B ARG   B 1 87  ? -26.328 10.915 38.208 0.43 37.66 ? 67  ARG   B HB3  1 
ATOM   3432 H HG2  A ARG   B 1 87  ? -26.086 13.173 38.151 0.57 32.38 ? 67  ARG   B HG2  1 
ATOM   3433 H HG2  B ARG   B 1 87  ? -26.362 13.156 37.907 0.43 34.33 ? 67  ARG   B HG2  1 
ATOM   3434 H HG3  A ARG   B 1 87  ? -25.708 13.104 36.610 0.57 32.38 ? 67  ARG   B HG3  1 
ATOM   3435 H HG3  B ARG   B 1 87  ? -25.510 13.033 36.572 0.43 34.33 ? 67  ARG   B HG3  1 
ATOM   3436 H HD2  A ARG   B 1 87  ? -27.964 11.727 37.117 0.57 34.89 ? 67  ARG   B HD2  1 
ATOM   3437 H HD2  B ARG   B 1 87  ? -27.877 13.329 36.211 0.43 32.13 ? 67  ARG   B HD2  1 
ATOM   3438 H HD3  A ARG   B 1 87  ? -28.110 13.252 37.539 0.57 34.89 ? 67  ARG   B HD3  1 
ATOM   3439 H HD3  B ARG   B 1 87  ? -27.259 12.075 35.457 0.43 32.13 ? 67  ARG   B HD3  1 
ATOM   3440 H HE   A ARG   B 1 87  ? -27.191 13.332 35.156 0.57 34.66 ? 67  ARG   B HE   1 
ATOM   3441 H HE   B ARG   B 1 87  ? -28.297 11.467 37.855 0.43 34.69 ? 67  ARG   B HE   1 
ATOM   3442 H HH11 A ARG   B 1 87  ? -29.955 11.949 36.360 0.57 36.86 ? 67  ARG   B HH11 1 
ATOM   3443 H HH11 B ARG   B 1 87  ? -29.185 11.592 34.659 0.43 40.98 ? 67  ARG   B HH11 1 
ATOM   3444 H HH12 A ARG   B 1 87  ? -30.768 12.133 35.125 0.57 36.86 ? 67  ARG   B HH12 1 
ATOM   3445 H HH12 B ARG   B 1 87  ? -30.339 10.660 34.793 0.43 40.98 ? 67  ARG   B HH12 1 
ATOM   3446 H HH21 A ARG   B 1 87  ? -28.446 13.665 33.337 0.57 31.10 ? 67  ARG   B HH21 1 
ATOM   3447 H HH21 B ARG   B 1 87  ? -30.007 10.032 38.006 0.43 39.18 ? 67  ARG   B HH21 1 
ATOM   3448 H HH22 A ARG   B 1 87  ? -29.851 13.175 33.290 0.57 31.10 ? 67  ARG   B HH22 1 
ATOM   3449 H HH22 B ARG   B 1 87  ? -30.835 9.719  36.808 0.43 39.18 ? 67  ARG   B HH22 1 
ATOM   3450 N N    . GLU   B 1 88  ? -24.708 10.806 40.594 1.00 32.00 ? 68  GLU   B N    1 
ATOM   3451 C CA   . GLU   B 1 88  ? -24.757 11.190 42.013 1.00 34.75 ? 68  GLU   B CA   1 
ATOM   3452 C C    . GLU   B 1 88  ? -23.381 11.587 42.566 1.00 34.19 ? 68  GLU   B C    1 
ATOM   3453 O O    . GLU   B 1 88  ? -23.235 12.618 43.242 1.00 34.17 ? 68  GLU   B O    1 
ATOM   3454 C CB   . GLU   B 1 88  ? -25.357 10.053 42.846 1.00 40.53 ? 68  GLU   B CB   1 
ATOM   3455 C CG   . GLU   B 1 88  ? -25.287 10.280 44.356 1.00 43.59 ? 68  GLU   B CG   1 
ATOM   3456 H H    A GLU   B 1 88  ? -24.928 9.991  40.431 0.57 38.40 ? 68  GLU   B H    1 
ATOM   3457 H H    B GLU   B 1 88  ? -24.919 9.988  40.434 0.43 38.40 ? 68  GLU   B H    1 
ATOM   3458 H HA   . GLU   B 1 88  ? -25.333 11.967 42.085 1.00 41.70 ? 68  GLU   B HA   1 
ATOM   3459 H HB2  . GLU   B 1 88  ? -26.291 9.952  42.607 1.00 48.64 ? 68  GLU   B HB2  1 
ATOM   3460 H HB3  . GLU   B 1 88  ? -24.874 9.235  42.649 1.00 48.64 ? 68  GLU   B HB3  1 
ATOM   3461 N N    . LYS   B 1 89  ? -22.361 10.769 42.316 1.00 32.26 ? 69  LYS   B N    1 
ATOM   3462 C CA   . LYS   B 1 89  ? -21.017 11.125 42.765 1.00 31.28 ? 69  LYS   B CA   1 
ATOM   3463 C C    . LYS   B 1 89  ? -20.503 12.384 42.075 1.00 27.66 ? 69  LYS   B C    1 
ATOM   3464 O O    . LYS   B 1 89  ? -19.747 13.144 42.679 1.00 27.99 ? 69  LYS   B O    1 
ATOM   3465 C CB   . LYS   B 1 89  ? -20.058 9.956  42.532 1.00 33.53 ? 69  LYS   B CB   1 
ATOM   3466 C CG   . LYS   B 1 89  ? -20.161 8.817  43.566 1.00 35.80 ? 69  LYS   B CG   1 
ATOM   3467 H H    . LYS   B 1 89  ? -22.417 10.019 41.898 1.00 38.72 ? 69  LYS   B H    1 
ATOM   3468 H HA   . LYS   B 1 89  ? -21.047 11.303 43.718 1.00 37.53 ? 69  LYS   B HA   1 
ATOM   3469 H HB2  . LYS   B 1 89  ? -20.244 9.575  41.660 1.00 40.23 ? 69  LYS   B HB2  1 
ATOM   3470 H HB3  . LYS   B 1 89  ? -19.150 10.293 42.560 1.00 40.23 ? 69  LYS   B HB3  1 
ATOM   3471 N N    . LEU   B 1 90  ? -20.869 12.609 40.810 1.00 24.50 ? 70  LEU   B N    1 
ATOM   3472 C CA   . LEU   B 1 90  ? -20.461 13.841 40.148 1.00 22.58 ? 70  LEU   B CA   1 
ATOM   3473 C C    . LEU   B 1 90  ? -21.067 15.046 40.840 1.00 23.46 ? 70  LEU   B C    1 
ATOM   3474 O O    . LEU   B 1 90  ? -20.394 16.059 41.023 1.00 24.47 ? 70  LEU   B O    1 
ATOM   3475 C CB   . LEU   B 1 90  ? -20.835 13.804 38.673 1.00 22.47 ? 70  LEU   B CB   1 
ATOM   3476 C CG   . LEU   B 1 90  ? -19.947 12.906 37.802 1.00 22.28 ? 70  LEU   B CG   1 
ATOM   3477 C CD1  . LEU   B 1 90  ? -20.670 12.574 36.490 1.00 24.13 ? 70  LEU   B CD1  1 
ATOM   3478 C CD2  . LEU   B 1 90  ? -18.627 13.597 37.509 1.00 23.59 ? 70  LEU   B CD2  1 
ATOM   3479 H H    . LEU   B 1 90  ? -21.342 12.076 40.328 1.00 29.41 ? 70  LEU   B H    1 
ATOM   3480 H HA   . LEU   B 1 90  ? -19.495 13.922 40.193 1.00 27.10 ? 70  LEU   B HA   1 
ATOM   3481 H HB2  . LEU   B 1 90  ? -21.745 13.477 38.596 1.00 26.96 ? 70  LEU   B HB2  1 
ATOM   3482 H HB3  . LEU   B 1 90  ? -20.775 14.705 38.319 1.00 26.96 ? 70  LEU   B HB3  1 
ATOM   3483 H HG   . LEU   B 1 90  ? -19.761 12.080 38.275 1.00 26.74 ? 70  LEU   B HG   1 
ATOM   3484 H HD11 . LEU   B 1 90  ? -20.093 12.017 35.944 1.00 28.96 ? 70  LEU   B HD11 1 
ATOM   3485 H HD12 . LEU   B 1 90  ? -21.491 12.099 36.694 1.00 28.96 ? 70  LEU   B HD12 1 
ATOM   3486 H HD13 . LEU   B 1 90  ? -20.872 13.399 36.023 1.00 28.96 ? 70  LEU   B HD13 1 
ATOM   3487 H HD21 . LEU   B 1 90  ? -18.090 13.022 36.942 1.00 28.31 ? 70  LEU   B HD21 1 
ATOM   3488 H HD22 . LEU   B 1 90  ? -18.804 14.436 37.056 1.00 28.31 ? 70  LEU   B HD22 1 
ATOM   3489 H HD23 . LEU   B 1 90  ? -18.165 13.763 38.345 1.00 28.31 ? 70  LEU   B HD23 1 
ATOM   3490 N N    . GLY   B 1 91  ? -22.340 14.954 41.244 1.00 24.92 ? 71  GLY   B N    1 
ATOM   3491 C CA   . GLY   B 1 91  ? -22.942 16.050 41.987 1.00 26.68 ? 71  GLY   B CA   1 
ATOM   3492 C C    . GLY   B 1 91  ? -22.248 16.316 43.315 1.00 28.38 ? 71  GLY   B C    1 
ATOM   3493 O O    . GLY   B 1 91  ? -22.069 17.468 43.713 1.00 29.01 ? 71  GLY   B O    1 
ATOM   3494 H H    . GLY   B 1 91  ? -22.859 14.283 41.103 1.00 29.91 ? 71  GLY   B H    1 
ATOM   3495 H HA2  . GLY   B 1 91  ? -22.898 16.859 41.454 1.00 32.02 ? 71  GLY   B HA2  1 
ATOM   3496 H HA3  . GLY   B 1 91  ? -23.872 15.841 42.167 1.00 32.02 ? 71  GLY   B HA3  1 
ATOM   3497 N N    . GLU   B 1 92  ? -21.807 15.261 43.998 1.00 30.73 ? 72  GLU   B N    1 
ATOM   3498 C CA   . GLU   B 1 92  ? -21.056 15.441 45.243 1.00 32.52 ? 72  GLU   B CA   1 
ATOM   3499 C C    . GLU   B 1 92  ? -19.692 16.091 45.010 1.00 31.39 ? 72  GLU   B C    1 
ATOM   3500 O O    . GLU   B 1 92  ? -19.228 16.911 45.818 1.00 32.15 ? 72  GLU   B O    1 
ATOM   3501 C CB   . GLU   B 1 92  ? -20.894 14.080 45.917 1.00 39.07 ? 72  GLU   B CB   1 
ATOM   3502 C CG   . GLU   B 1 92  ? -22.223 13.483 46.340 1.00 44.26 ? 72  GLU   B CG   1 
ATOM   3503 C CD   . GLU   B 1 92  ? -22.108 12.042 46.820 1.00 50.45 ? 72  GLU   B CD   1 
ATOM   3504 O OE1  . GLU   B 1 92  ? -20.984 11.494 46.833 1.00 53.17 ? 72  GLU   B OE1  1 
ATOM   3505 O OE2  . GLU   B 1 92  ? -23.154 11.458 47.180 1.00 52.26 ? 72  GLU   B OE2  1 
ATOM   3506 H H    . GLU   B 1 92  ? -21.925 14.441 43.768 1.00 36.88 ? 72  GLU   B H    1 
ATOM   3507 H HA   . GLU   B 1 92  ? -21.554 16.033 45.828 1.00 39.02 ? 72  GLU   B HA   1 
ATOM   3508 H HB2  . GLU   B 1 92  ? -20.471 13.467 45.296 1.00 46.89 ? 72  GLU   B HB2  1 
ATOM   3509 H HB3  . GLU   B 1 92  ? -20.344 14.183 46.710 1.00 46.89 ? 72  GLU   B HB3  1 
ATOM   3510 H HG2  . GLU   B 1 92  ? -22.589 14.011 47.066 1.00 53.11 ? 72  GLU   B HG2  1 
ATOM   3511 H HG3  . GLU   B 1 92  ? -22.829 13.497 45.582 1.00 53.11 ? 72  GLU   B HG3  1 
ATOM   3512 N N    . HIS   B 1 93  ? -19.009 15.685 43.945 1.00 29.75 ? 73  HIS   B N    1 
ATOM   3513 C CA   . HIS   B 1 93  ? -17.720 16.279 43.596 1.00 29.85 ? 73  HIS   B CA   1 
ATOM   3514 C C    . HIS   B 1 93  ? -17.844 17.775 43.378 1.00 28.42 ? 73  HIS   B C    1 
ATOM   3515 O O    . HIS   B 1 93  ? -16.924 18.535 43.704 1.00 28.62 ? 73  HIS   B O    1 
ATOM   3516 C CB   . HIS   B 1 93  ? -17.157 15.634 42.314 1.00 31.41 ? 73  HIS   B CB   1 
ATOM   3517 C CG   . HIS   B 1 93  ? -16.054 16.415 41.643 1.00 32.02 ? 73  HIS   B CG   1 
ATOM   3518 N ND1  . HIS   B 1 93  ? -14.747 16.385 42.078 1.00 32.98 ? 73  HIS   B ND1  1 
ATOM   3519 C CD2  . HIS   B 1 93  ? -16.063 17.211 40.544 1.00 32.57 ? 73  HIS   B CD2  1 
ATOM   3520 C CE1  . HIS   B 1 93  ? -14.001 17.135 41.285 1.00 33.33 ? 73  HIS   B CE1  1 
ATOM   3521 N NE2  . HIS   B 1 93  ? -14.772 17.638 40.339 1.00 34.91 ? 73  HIS   B NE2  1 
ATOM   3522 H H    . HIS   B 1 93  ? -19.267 15.067 43.405 1.00 35.70 ? 73  HIS   B H    1 
ATOM   3523 H HA   . HIS   B 1 93  ? -17.103 16.110 44.325 1.00 35.82 ? 73  HIS   B HA   1 
ATOM   3524 H HB2  . HIS   B 1 93  ? -16.799 14.761 42.541 1.00 37.69 ? 73  HIS   B HB2  1 
ATOM   3525 H HB3  . HIS   B 1 93  ? -17.879 15.540 41.674 1.00 37.69 ? 73  HIS   B HB3  1 
ATOM   3526 H HD1  . HIS   B 1 93  ? -14.460 15.946 42.759 1.00 39.58 ? 73  HIS   B HD1  1 
ATOM   3527 H HD2  . HIS   B 1 93  ? -16.804 17.427 40.026 1.00 39.09 ? 73  HIS   B HD2  1 
ATOM   3528 H HE1  . HIS   B 1 93  ? -13.088 17.284 41.378 1.00 40.00 ? 73  HIS   B HE1  1 
ATOM   3529 N N    . ALA   B 1 94  ? -18.971 18.224 42.838 1.00 26.35 ? 74  ALA   B N    1 
ATOM   3530 C CA   . ALA   B 1 94  ? -19.117 19.646 42.581 1.00 26.06 ? 74  ALA   B CA   1 
ATOM   3531 C C    . ALA   B 1 94  ? -19.071 20.443 43.874 1.00 25.02 ? 74  ALA   B C    1 
ATOM   3532 O O    . ALA   B 1 94  ? -18.548 21.563 43.901 1.00 25.68 ? 74  ALA   B O    1 
ATOM   3533 C CB   . ALA   B 1 94  ? -20.408 19.896 41.830 1.00 27.09 ? 74  ALA   B CB   1 
ATOM   3534 H H    . ALA   B 1 94  ? -19.646 17.738 42.618 1.00 31.62 ? 74  ALA   B H    1 
ATOM   3535 H HA   . ALA   B 1 94  ? -18.384 19.950 42.024 1.00 31.27 ? 74  ALA   B HA   1 
ATOM   3536 H HB1  . ALA   B 1 94  ? -20.496 20.848 41.662 1.00 32.51 ? 74  ALA   B HB1  1 
ATOM   3537 H HB2  . ALA   B 1 94  ? -20.383 19.413 40.989 1.00 32.51 ? 74  ALA   B HB2  1 
ATOM   3538 H HB3  . ALA   B 1 94  ? -21.152 19.585 42.368 1.00 32.51 ? 74  ALA   B HB3  1 
ATOM   3539 N N    . VAL   B 1 95  ? -19.608 19.890 44.954 1.00 27.14 ? 75  VAL   B N    1 
ATOM   3540 C CA   . VAL   B 1 95  ? -19.534 20.580 46.236 1.00 29.86 ? 75  VAL   B CA   1 
ATOM   3541 C C    . VAL   B 1 95  ? -18.081 20.781 46.641 1.00 29.80 ? 75  VAL   B C    1 
ATOM   3542 O O    . VAL   B 1 95  ? -17.675 21.876 47.059 1.00 29.83 ? 75  VAL   B O    1 
ATOM   3543 C CB   . VAL   B 1 95  ? -20.327 19.797 47.295 1.00 34.59 ? 75  VAL   B CB   1 
ATOM   3544 C CG1  . VAL   B 1 95  ? -20.230 20.488 48.637 1.00 37.29 ? 75  VAL   B CG1  1 
ATOM   3545 C CG2  . VAL   B 1 95  ? -21.792 19.663 46.867 1.00 36.56 ? 75  VAL   B CG2  1 
ATOM   3546 H H    . VAL   B 1 95  ? -20.013 19.132 44.972 1.00 32.57 ? 75  VAL   B H    1 
ATOM   3547 H HA   . VAL   B 1 95  ? -19.936 21.459 46.151 1.00 35.84 ? 75  VAL   B HA   1 
ATOM   3548 H HB   . VAL   B 1 95  ? -19.950 18.907 47.381 1.00 41.51 ? 75  VAL   B HB   1 
ATOM   3549 H HG11 . VAL   B 1 95  ? -20.776 20.007 49.279 1.00 44.75 ? 75  VAL   B HG11 1 
ATOM   3550 H HG12 . VAL   B 1 95  ? -19.304 20.490 48.925 1.00 44.75 ? 75  VAL   B HG12 1 
ATOM   3551 H HG13 . VAL   B 1 95  ? -20.551 21.399 48.547 1.00 44.75 ? 75  VAL   B HG13 1 
ATOM   3552 H HG21 . VAL   B 1 95  ? -22.295 19.253 47.588 1.00 43.87 ? 75  VAL   B HG21 1 
ATOM   3553 H HG22 . VAL   B 1 95  ? -22.147 20.546 46.676 1.00 43.87 ? 75  VAL   B HG22 1 
ATOM   3554 H HG23 . VAL   B 1 95  ? -21.840 19.108 46.073 1.00 43.87 ? 75  VAL   B HG23 1 
ATOM   3555 N N    A TRP   B 1 96  ? -17.270 19.725 46.523 0.55 29.07 ? 76  TRP   B N    1 
ATOM   3556 N N    B TRP   B 1 96  ? -17.272 19.724 46.530 0.45 30.07 ? 76  TRP   B N    1 
ATOM   3557 C CA   A TRP   B 1 96  ? -15.855 19.845 46.867 0.55 31.08 ? 76  TRP   B CA   1 
ATOM   3558 C CA   B TRP   B 1 96  ? -15.857 19.846 46.868 0.45 32.17 ? 76  TRP   B CA   1 
ATOM   3559 C C    A TRP   B 1 96  ? -15.141 20.794 45.916 0.55 32.54 ? 76  TRP   B C    1 
ATOM   3560 C C    B TRP   B 1 96  ? -15.151 20.803 45.920 0.45 32.96 ? 76  TRP   B C    1 
ATOM   3561 O O    A TRP   B 1 96  ? -14.266 21.562 46.334 0.55 36.50 ? 76  TRP   B O    1 
ATOM   3562 O O    B TRP   B 1 96  ? -14.295 21.591 46.341 0.45 36.37 ? 76  TRP   B O    1 
ATOM   3563 C CB   A TRP   B 1 96  ? -15.179 18.475 46.848 0.55 31.89 ? 76  TRP   B CB   1 
ATOM   3564 C CB   B TRP   B 1 96  ? -15.179 18.477 46.836 0.45 33.03 ? 76  TRP   B CB   1 
ATOM   3565 H H    A TRP   B 1 96  ? -17.510 18.945 46.252 0.55 34.89 ? 76  TRP   B H    1 
ATOM   3566 H H    B TRP   B 1 96  ? -17.513 18.942 46.266 0.45 36.08 ? 76  TRP   B H    1 
ATOM   3567 H HA   A TRP   B 1 96  ? -15.788 20.199 47.768 0.55 37.30 ? 76  TRP   B HA   1 
ATOM   3568 H HA   B TRP   B 1 96  ? -15.785 20.194 47.771 0.45 38.60 ? 76  TRP   B HA   1 
ATOM   3569 N N    . SER   B 1 97  ? -15.494 20.746 44.632 1.00 30.94 ? 77  SER   B N    1 
ATOM   3570 C CA   . SER   B 1 97  ? -14.855 21.613 43.656 1.00 31.18 ? 77  SER   B CA   1 
ATOM   3571 C C    . SER   B 1 97  ? -15.114 23.079 43.959 1.00 30.69 ? 77  SER   B C    1 
ATOM   3572 O O    . SER   B 1 97  ? -14.221 23.916 43.801 1.00 32.46 ? 77  SER   B O    1 
ATOM   3573 C CB   . SER   B 1 97  ? -15.364 21.242 42.271 1.00 33.61 ? 77  SER   B CB   1 
ATOM   3574 O OG   . SER   B 1 97  ? -14.658 21.970 41.291 1.00 36.89 ? 77  SER   B OG   1 
ATOM   3575 H H    A SER   B 1 97  ? -16.095 20.224 44.306 0.55 37.12 ? 77  SER   B H    1 
ATOM   3576 H H    B SER   B 1 97  ? -16.088 20.217 44.304 0.45 37.12 ? 77  SER   B H    1 
ATOM   3577 H HA   . SER   B 1 97  ? -13.894 21.484 43.682 1.00 37.42 ? 77  SER   B HA   1 
ATOM   3578 H HB2  . SER   B 1 97  ? -15.228 20.293 42.124 1.00 40.33 ? 77  SER   B HB2  1 
ATOM   3579 H HB3  . SER   B 1 97  ? -16.308 21.455 42.210 1.00 40.33 ? 77  SER   B HB3  1 
ATOM   3580 H HG   . SER   B 1 97  ? -14.941 21.769 40.525 1.00 44.27 ? 77  SER   B HG   1 
ATOM   3581 N N    . LEU   B 1 98  ? -16.331 23.424 44.371 1.00 30.00 ? 78  LEU   B N    1 
ATOM   3582 C CA   . LEU   B 1 98  ? -16.599 24.823 44.686 1.00 31.66 ? 78  LEU   B CA   1 
ATOM   3583 C C    . LEU   B 1 98  ? -15.839 25.291 45.919 1.00 32.18 ? 78  LEU   B C    1 
ATOM   3584 O O    . LEU   B 1 98  ? -15.561 26.491 46.048 1.00 34.52 ? 78  LEU   B O    1 
ATOM   3585 C CB   . LEU   B 1 98  ? -18.096 25.035 44.847 0.86 32.78 ? 78  LEU   B CB   1 
ATOM   3586 C CG   . LEU   B 1 98  ? -18.788 25.278 43.504 0.82 33.19 ? 78  LEU   B CG   1 
ATOM   3587 C CD1  . LEU   B 1 98  ? -20.261 25.006 43.620 0.71 36.10 ? 78  LEU   B CD1  1 
ATOM   3588 C CD2  . LEU   B 1 98  ? -18.498 26.719 43.024 0.82 32.15 ? 78  LEU   B CD2  1 
ATOM   3589 H H    . LEU   B 1 98  ? -16.994 22.886 44.472 1.00 36.01 ? 78  LEU   B H    1 
ATOM   3590 H HA   . LEU   B 1 98  ? -16.308 25.381 43.949 1.00 37.99 ? 78  LEU   B HA   1 
ATOM   3591 H HB2  . LEU   B 1 98  ? -18.487 24.245 45.252 0.86 39.33 ? 78  LEU   B HB2  1 
ATOM   3592 H HB3  . LEU   B 1 98  ? -18.249 25.808 45.412 0.86 39.33 ? 78  LEU   B HB3  1 
ATOM   3593 H HG   . LEU   B 1 98  ? -18.443 24.671 42.831 0.82 39.83 ? 78  LEU   B HG   1 
ATOM   3594 H HD11 . LEU   B 1 98  ? -20.682 25.173 42.762 0.71 43.32 ? 78  LEU   B HD11 1 
ATOM   3595 H HD12 . LEU   B 1 98  ? -20.392 24.080 43.879 0.71 43.32 ? 78  LEU   B HD12 1 
ATOM   3596 H HD13 . LEU   B 1 98  ? -20.639 25.594 44.293 0.71 43.32 ? 78  LEU   B HD13 1 
ATOM   3597 H HD21 . LEU   B 1 98  ? -19.011 26.893 42.220 0.82 38.59 ? 78  LEU   B HD21 1 
ATOM   3598 H HD22 . LEU   B 1 98  ? -18.754 27.342 43.722 0.82 38.59 ? 78  LEU   B HD22 1 
ATOM   3599 H HD23 . LEU   B 1 98  ? -17.550 26.804 42.836 0.82 38.59 ? 78  LEU   B HD23 1 
ATOM   3600 N N    . GLN   B 1 99  ? -15.454 24.372 46.799 1.00 28.76 ? 79  GLN   B N    1 
ATOM   3601 C CA   . GLN   B 1 99  ? -14.616 24.742 47.932 1.00 29.73 ? 79  GLN   B CA   1 
ATOM   3602 C C    . GLN   B 1 99  ? -13.157 24.916 47.530 1.00 31.33 ? 79  GLN   B C    1 
ATOM   3603 O O    . GLN   B 1 99  ? -12.519 25.910 47.885 1.00 29.96 ? 79  GLN   B O    1 
ATOM   3604 C CB   . GLN   B 1 99  ? -14.762 23.672 49.018 1.00 33.28 ? 79  GLN   B CB   1 
ATOM   3605 C CG   . GLN   B 1 99  ? -13.857 23.842 50.214 1.00 41.58 ? 79  GLN   B CG   1 
ATOM   3606 C CD   . GLN   B 1 99  ? -14.082 22.763 51.265 1.00 69.61 ? 79  GLN   B CD   1 
ATOM   3607 O OE1  . GLN   B 1 99  ? -15.189 22.612 51.779 1.00 69.34 ? 79  GLN   B OE1  1 
ATOM   3608 N NE2  . GLN   B 1 99  ? -13.033 21.999 51.578 1.00 59.94 ? 79  GLN   B NE2  1 
ATOM   3609 H H    . GLN   B 1 99  ? -15.661 23.539 46.763 1.00 34.51 ? 79  GLN   B H    1 
ATOM   3610 H HA   . GLN   B 1 99  ? -14.911 25.595 48.289 1.00 35.68 ? 79  GLN   B HA   1 
ATOM   3611 H HB2  . GLN   B 1 99  ? -15.677 23.687 49.341 1.00 39.94 ? 79  GLN   B HB2  1 
ATOM   3612 H HB3  . GLN   B 1 99  ? -14.564 22.807 48.624 1.00 39.94 ? 79  GLN   B HB3  1 
ATOM   3613 H HG2  . GLN   B 1 99  ? -12.933 23.792 49.923 1.00 49.90 ? 79  GLN   B HG2  1 
ATOM   3614 H HG3  . GLN   B 1 99  ? -14.030 24.704 50.624 1.00 49.90 ? 79  GLN   B HG3  1 
ATOM   3615 H HE21 . GLN   B 1 99  ? -12.276 22.129 51.192 1.00 71.93 ? 79  GLN   B HE21 1 
ATOM   3616 H HE22 . GLN   B 1 99  ? -13.114 21.377 52.167 1.00 71.93 ? 79  GLN   B HE22 1 
ATOM   3617 N N    . CYS   B 1 100 ? -12.615 23.949 46.805 1.00 28.22 ? 80  CYS   B N    1 
ATOM   3618 C CA   . CYS   B 1 100 ? -11.191 23.934 46.481 1.00 29.55 ? 80  CYS   B CA   1 
ATOM   3619 C C    . CYS   B 1 100 ? -10.826 24.753 45.252 1.00 26.25 ? 80  CYS   B C    1 
ATOM   3620 O O    . CYS   B 1 100 ? -9.667  25.138 45.120 1.00 27.06 ? 80  CYS   B O    1 
ATOM   3621 C CB   . CYS   B 1 100 ? -10.770 22.482 46.298 1.00 36.07 ? 80  CYS   B CB   1 
ATOM   3622 S SG   . CYS   B 1 100 ? -10.927 21.545 47.840 1.00 45.28 ? 80  CYS   B SG   1 
ATOM   3623 H H    . CYS   B 1 100 ? -13.051 23.281 46.483 1.00 33.86 ? 80  CYS   B H    1 
ATOM   3624 H HA   . CYS   B 1 100 ? -10.689 24.327 47.212 1.00 35.46 ? 80  CYS   B HA   1 
ATOM   3625 H HB2  . CYS   B 1 100 ? -11.335 22.066 45.629 1.00 43.28 ? 80  CYS   B HB2  1 
ATOM   3626 H HB3  . CYS   B 1 100 ? -9.842  22.451 46.014 1.00 43.28 ? 80  CYS   B HB3  1 
ATOM   3627 H HG   . CYS   B 1 100 ? -10.585 20.412 47.645 1.00 54.34 ? 80  CYS   B HG   1 
ATOM   3628 N N    . PHE   B 1 101 ? -11.765 24.994 44.346 1.00 23.18 ? 81  PHE   B N    1 
ATOM   3629 C CA   . PHE   B 1 101 ? -11.555 25.809 43.148 1.00 21.64 ? 81  PHE   B CA   1 
ATOM   3630 C C    . PHE   B 1 101 ? -12.730 26.780 43.071 1.00 21.03 ? 81  PHE   B C    1 
ATOM   3631 O O    . PHE   B 1 101 ? -13.621 26.649 42.221 1.00 22.00 ? 81  PHE   B O    1 
ATOM   3632 C CB   . PHE   B 1 101 ? -11.472 24.918 41.910 1.00 22.25 ? 81  PHE   B CB   1 
ATOM   3633 C CG   . PHE   B 1 101 ? -10.305 23.976 41.934 1.00 23.76 ? 81  PHE   B CG   1 
ATOM   3634 C CD1  . PHE   B 1 101 ? -9.034  24.398 41.562 1.00 22.87 ? 81  PHE   B CD1  1 
ATOM   3635 C CD2  . PHE   B 1 101 ? -10.464 22.688 42.363 1.00 29.00 ? 81  PHE   B CD2  1 
ATOM   3636 C CE1  . PHE   B 1 101 ? -7.947  23.529 41.590 1.00 25.45 ? 81  PHE   B CE1  1 
ATOM   3637 C CE2  . PHE   B 1 101 ? -9.386  21.825 42.427 1.00 31.06 ? 81  PHE   B CE2  1 
ATOM   3638 C CZ   . PHE   B 1 101 ? -8.123  22.244 42.035 1.00 28.65 ? 81  PHE   B CZ   1 
ATOM   3639 H H    . PHE   B 1 101 ? -12.566 24.684 44.403 1.00 27.81 ? 81  PHE   B H    1 
ATOM   3640 H HA   . PHE   B 1 101 ? -10.729 26.314 43.200 1.00 25.97 ? 81  PHE   B HA   1 
ATOM   3641 H HB2  . PHE   B 1 101 ? -12.281 24.386 41.851 1.00 26.70 ? 81  PHE   B HB2  1 
ATOM   3642 H HB3  . PHE   B 1 101 ? -11.385 25.479 41.124 1.00 26.70 ? 81  PHE   B HB3  1 
ATOM   3643 H HD1  . PHE   B 1 101 ? -8.907  25.278 41.289 1.00 27.45 ? 81  PHE   B HD1  1 
ATOM   3644 H HD2  . PHE   B 1 101 ? -11.308 22.389 42.615 1.00 34.80 ? 81  PHE   B HD2  1 
ATOM   3645 H HE1  . PHE   B 1 101 ? -7.109  23.817 41.309 1.00 30.54 ? 81  PHE   B HE1  1 
ATOM   3646 H HE2  . PHE   B 1 101 ? -9.508  20.956 42.735 1.00 37.27 ? 81  PHE   B HE2  1 
ATOM   3647 H HZ   . PHE   B 1 101 ? -7.402  21.658 42.073 1.00 34.38 ? 81  PHE   B HZ   1 
ATOM   3648 N N    . PRO   B 1 102 ? -12.778 27.753 43.985 1.00 21.83 ? 82  PRO   B N    1 
ATOM   3649 C CA   . PRO   B 1 102 ? -14.020 28.527 44.176 1.00 23.03 ? 82  PRO   B CA   1 
ATOM   3650 C C    . PRO   B 1 102 ? -14.415 29.427 43.020 1.00 24.09 ? 82  PRO   B C    1 
ATOM   3651 O O    . PRO   B 1 102 ? -15.597 29.784 42.916 1.00 27.07 ? 82  PRO   B O    1 
ATOM   3652 C CB   . PRO   B 1 102 ? -13.727 29.351 45.443 1.00 25.44 ? 82  PRO   B CB   1 
ATOM   3653 C CG   . PRO   B 1 102 ? -12.182 29.414 45.500 1.00 25.16 ? 82  PRO   B CG   1 
ATOM   3654 C CD   . PRO   B 1 102 ? -11.751 28.078 44.995 1.00 22.99 ? 82  PRO   B CD   1 
ATOM   3655 H HA   . PRO   B 1 102 ? -14.750 27.909 44.340 1.00 27.64 ? 82  PRO   B HA   1 
ATOM   3656 H HB2  . PRO   B 1 102 ? -14.111 30.238 45.360 1.00 30.53 ? 82  PRO   B HB2  1 
ATOM   3657 H HB3  . PRO   B 1 102 ? -14.089 28.904 46.224 1.00 30.53 ? 82  PRO   B HB3  1 
ATOM   3658 H HG2  . PRO   B 1 102 ? -11.854 30.126 44.929 1.00 30.19 ? 82  PRO   B HG2  1 
ATOM   3659 H HG3  . PRO   B 1 102 ? -11.886 29.556 46.412 1.00 30.19 ? 82  PRO   B HG3  1 
ATOM   3660 H HD2  . PRO   B 1 102 ? -10.871 28.129 44.590 1.00 27.59 ? 82  PRO   B HD2  1 
ATOM   3661 H HD3  . PRO   B 1 102 ? -11.750 27.422 45.710 1.00 27.59 ? 82  PRO   B HD3  1 
ATOM   3662 N N    . ASP   B 1 103 ? -13.482 29.786 42.141 1.00 23.92 ? 83  ASP   B N    1 
ATOM   3663 C CA   . ASP   B 1 103 ? -13.730 30.739 41.067 1.00 23.23 ? 83  ASP   B CA   1 
ATOM   3664 C C    . ASP   B 1 103 ? -13.229 30.234 39.713 1.00 21.45 ? 83  ASP   B C    1 
ATOM   3665 O O    . ASP   B 1 103 ? -12.922 31.029 38.824 1.00 22.25 ? 83  ASP   B O    1 
ATOM   3666 C CB   . ASP   B 1 103 ? -13.142 32.113 41.404 1.00 24.36 ? 83  ASP   B CB   1 
ATOM   3667 C CG   . ASP   B 1 103 ? -11.615 32.105 41.519 1.00 26.04 ? 83  ASP   B CG   1 
ATOM   3668 O OD1  . ASP   B 1 103 ? -11.009 31.020 41.464 1.00 25.82 ? 83  ASP   B OD1  1 
ATOM   3669 O OD2  . ASP   B 1 103 ? -11.013 33.195 41.652 1.00 30.60 ? 83  ASP   B OD2  1 
ATOM   3670 H H    . ASP   B 1 103 ? -12.678 29.483 42.149 1.00 28.71 ? 83  ASP   B H    1 
ATOM   3671 H HA   . ASP   B 1 103 ? -14.690 30.844 40.977 1.00 27.88 ? 83  ASP   B HA   1 
ATOM   3672 H HB2  . ASP   B 1 103 ? -13.385 32.739 40.703 1.00 29.23 ? 83  ASP   B HB2  1 
ATOM   3673 H HB3  . ASP   B 1 103 ? -13.504 32.410 42.253 1.00 29.23 ? 83  ASP   B HB3  1 
ATOM   3674 N N    . TRP   B 1 104 ? -13.181 28.919 39.532 1.00 20.19 ? 84  TRP   B N    1 
ATOM   3675 C CA   . TRP   B 1 104 ? -12.605 28.325 38.333 1.00 18.77 ? 84  TRP   B CA   1 
ATOM   3676 C C    . TRP   B 1 104 ? -13.360 28.745 37.078 1.00 18.98 ? 84  TRP   B C    1 
ATOM   3677 O O    . TRP   B 1 104 ? -14.594 28.665 37.008 1.00 19.83 ? 84  TRP   B O    1 
ATOM   3678 C CB   . TRP   B 1 104 ? -12.653 26.805 38.459 1.00 18.70 ? 84  TRP   B CB   1 
ATOM   3679 C CG   . TRP   B 1 104 ? -11.879 26.115 37.400 1.00 18.57 ? 84  TRP   B CG   1 
ATOM   3680 C CD1  . TRP   B 1 104 ? -12.355 25.492 36.288 1.00 19.67 ? 84  TRP   B CD1  1 
ATOM   3681 C CD2  . TRP   B 1 104 ? -10.454 26.050 37.325 1.00 17.57 ? 84  TRP   B CD2  1 
ATOM   3682 N NE1  . TRP   B 1 104 ? -11.307 25.006 35.547 1.00 19.93 ? 84  TRP   B NE1  1 
ATOM   3683 C CE2  . TRP   B 1 104 ? -10.128 25.338 36.161 1.00 18.01 ? 84  TRP   B CE2  1 
ATOM   3684 C CE3  . TRP   B 1 104 ? -9.425  26.492 38.150 1.00 18.10 ? 84  TRP   B CE3  1 
ATOM   3685 C CZ2  . TRP   B 1 104 ? -8.820  25.073 35.801 1.00 18.03 ? 84  TRP   B CZ2  1 
ATOM   3686 C CZ3  . TRP   B 1 104 ? -8.112  26.283 37.752 1.00 18.24 ? 84  TRP   B CZ3  1 
ATOM   3687 C CH2  . TRP   B 1 104 ? -7.829  25.543 36.600 1.00 18.28 ? 84  TRP   B CH2  1 
ATOM   3688 H H    . TRP   B 1 104 ? -13.480 28.342 40.095 1.00 24.23 ? 84  TRP   B H    1 
ATOM   3689 H HA   . TRP   B 1 104 ? -11.686 28.624 38.242 1.00 22.52 ? 84  TRP   B HA   1 
ATOM   3690 H HB2  . TRP   B 1 104 ? -12.282 26.548 39.318 1.00 22.44 ? 84  TRP   B HB2  1 
ATOM   3691 H HB3  . TRP   B 1 104 ? -13.576 26.513 38.395 1.00 22.44 ? 84  TRP   B HB3  1 
ATOM   3692 H HD1  . TRP   B 1 104 ? -13.253 25.409 36.064 1.00 23.61 ? 84  TRP   B HD1  1 
ATOM   3693 H HE1  . TRP   B 1 104 ? -11.379 24.562 34.813 1.00 23.92 ? 84  TRP   B HE1  1 
ATOM   3694 H HE3  . TRP   B 1 104 ? -9.613  26.920 38.953 1.00 21.72 ? 84  TRP   B HE3  1 
ATOM   3695 H HZ2  . TRP   B 1 104 ? -8.624  24.587 35.033 1.00 21.64 ? 84  TRP   B HZ2  1 
ATOM   3696 H HZ3  . TRP   B 1 104 ? -7.416  26.638 38.256 1.00 21.89 ? 84  TRP   B HZ3  1 
ATOM   3697 H HH2  . TRP   B 1 104 ? -6.943  25.369 36.376 1.00 21.93 ? 84  TRP   B HH2  1 
ATOM   3698 N N    . VAL   B 1 105 ? -12.591 29.101 36.042 1.00 18.97 ? 85  VAL   B N    1 
ATOM   3699 C CA   . VAL   B 1 105 ? -13.123 29.439 34.722 1.00 18.59 ? 85  VAL   B CA   1 
ATOM   3700 C C    . VAL   B 1 105 ? -12.325 28.680 33.668 1.00 18.16 ? 85  VAL   B C    1 
ATOM   3701 O O    . VAL   B 1 105 ? -11.094 28.648 33.725 1.00 18.17 ? 85  VAL   B O    1 
ATOM   3702 C CB   . VAL   B 1 105 ? -13.041 30.970 34.472 1.00 20.93 ? 85  VAL   B CB   1 
ATOM   3703 C CG1  . VAL   B 1 105 ? -13.520 31.351 33.069 1.00 23.09 ? 85  VAL   B CG1  1 
ATOM   3704 C CG2  . VAL   B 1 105 ? -13.830 31.734 35.530 1.00 25.16 ? 85  VAL   B CG2  1 
ATOM   3705 H H    . VAL   B 1 105 ? -11.734 29.155 36.084 1.00 22.76 ? 85  VAL   B H    1 
ATOM   3706 H HA   . VAL   B 1 105 ? -14.049 29.158 34.657 1.00 22.31 ? 85  VAL   B HA   1 
ATOM   3707 H HB   . VAL   B 1 105 ? -12.108 31.227 34.537 1.00 25.12 ? 85  VAL   B HB   1 
ATOM   3708 H HG11 . VAL   B 1 105 ? -13.602 32.316 33.014 1.00 27.71 ? 85  VAL   B HG11 1 
ATOM   3709 H HG12 . VAL   B 1 105 ? -12.872 31.037 32.418 1.00 27.71 ? 85  VAL   B HG12 1 
ATOM   3710 H HG13 . VAL   B 1 105 ? -14.381 30.935 32.905 1.00 27.71 ? 85  VAL   B HG13 1 
ATOM   3711 H HG21 . VAL   B 1 105 ? -13.794 32.682 35.327 1.00 30.19 ? 85  VAL   B HG21 1 
ATOM   3712 H HG22 . VAL   B 1 105 ? -14.750 31.428 35.519 1.00 30.19 ? 85  VAL   B HG22 1 
ATOM   3713 H HG23 . VAL   B 1 105 ? -13.435 31.566 36.400 1.00 30.19 ? 85  VAL   B HG23 1 
ATOM   3714 N N    . TRP   B 1 106 ? -13.013 28.169 32.654 1.00 17.72 ? 86  TRP   B N    1 
ATOM   3715 C CA   . TRP   B 1 106 ? -12.391 27.683 31.422 1.00 16.98 ? 86  TRP   B CA   1 
ATOM   3716 C C    . TRP   B 1 106 ? -12.363 28.831 30.421 1.00 18.75 ? 86  TRP   B C    1 
ATOM   3717 O O    . TRP   B 1 106 ? -13.382 29.470 30.200 1.00 20.89 ? 86  TRP   B O    1 
ATOM   3718 C CB   . TRP   B 1 106 ? -13.180 26.523 30.853 1.00 17.26 ? 86  TRP   B CB   1 
ATOM   3719 C CG   . TRP   B 1 106 ? -13.416 25.374 31.748 1.00 17.08 ? 86  TRP   B CG   1 
ATOM   3720 C CD1  . TRP   B 1 106 ? -14.617 25.011 32.283 1.00 17.36 ? 86  TRP   B CD1  1 
ATOM   3721 C CD2  . TRP   B 1 106 ? -12.448 24.410 32.231 1.00 16.69 ? 86  TRP   B CD2  1 
ATOM   3722 N NE1  . TRP   B 1 106 ? -14.476 23.860 33.026 1.00 17.77 ? 86  TRP   B NE1  1 
ATOM   3723 C CE2  . TRP   B 1 106 ? -13.160 23.488 33.042 1.00 17.13 ? 86  TRP   B CE2  1 
ATOM   3724 C CE3  . TRP   B 1 106 ? -11.059 24.251 32.083 1.00 17.66 ? 86  TRP   B CE3  1 
ATOM   3725 C CZ2  . TRP   B 1 106 ? -12.542 22.415 33.678 1.00 18.33 ? 86  TRP   B CZ2  1 
ATOM   3726 C CZ3  . TRP   B 1 106 ? -10.456 23.164 32.716 1.00 17.49 ? 86  TRP   B CZ3  1 
ATOM   3727 C CH2  . TRP   B 1 106 ? -11.190 22.270 33.497 1.00 18.19 ? 86  TRP   B CH2  1 
ATOM   3728 H H    . TRP   B 1 106 ? -13.869 28.088 32.654 1.00 21.26 ? 86  TRP   B H    1 
ATOM   3729 H HA   . TRP   B 1 106 ? -11.487 27.377 31.596 1.00 20.38 ? 86  TRP   B HA   1 
ATOM   3730 H HB2  . TRP   B 1 106 ? -14.051 26.855 30.584 1.00 20.71 ? 86  TRP   B HB2  1 
ATOM   3731 H HB3  . TRP   B 1 106 ? -12.701 26.185 30.080 1.00 20.71 ? 86  TRP   B HB3  1 
ATOM   3732 H HD1  . TRP   B 1 106 ? -15.415 25.473 32.164 1.00 20.83 ? 86  TRP   B HD1  1 
ATOM   3733 H HE1  . TRP   B 1 106 ? -15.115 23.440 33.418 1.00 21.33 ? 86  TRP   B HE1  1 
ATOM   3734 H HE3  . TRP   B 1 106 ? -10.558 24.851 31.579 1.00 21.19 ? 86  TRP   B HE3  1 
ATOM   3735 H HZ2  . TRP   B 1 106 ? -13.027 21.821 34.205 1.00 22.00 ? 86  TRP   B HZ2  1 
ATOM   3736 H HZ3  . TRP   B 1 106 ? -9.541  23.032 32.615 1.00 20.99 ? 86  TRP   B HZ3  1 
ATOM   3737 H HH2  . TRP   B 1 106 ? -10.752 21.558 33.906 1.00 21.83 ? 86  TRP   B HH2  1 
ATOM   3738 N N    . THR   B 1 107 ? -11.205 29.072 29.811 1.00 17.03 ? 87  THR   B N    1 
ATOM   3739 C CA   . THR   B 1 107 ? -11.000 30.161 28.854 1.00 18.73 ? 87  THR   B CA   1 
ATOM   3740 C C    . THR   B 1 107 ? -10.463 29.589 27.535 1.00 17.43 ? 87  THR   B C    1 
ATOM   3741 O O    . THR   B 1 107 ? -10.032 28.429 27.471 1.00 17.36 ? 87  THR   B O    1 
ATOM   3742 C CB   . THR   B 1 107 ? -10.018 31.217 29.379 1.00 21.31 ? 87  THR   B CB   1 
ATOM   3743 O OG1  . THR   B 1 107 ? -8.721  30.648 29.500 1.00 22.59 ? 87  THR   B OG1  1 
ATOM   3744 C CG2  . THR   B 1 107 ? -10.434 31.768 30.729 1.00 22.44 ? 87  THR   B CG2  1 
ATOM   3745 H H    . THR   B 1 107 ? -10.497 28.602 29.939 1.00 20.43 ? 87  THR   B H    1 
ATOM   3746 H HA   . THR   B 1 107 ? -11.854 30.593 28.699 1.00 22.48 ? 87  THR   B HA   1 
ATOM   3747 H HB   . THR   B 1 107 ? -10.007 31.956 28.750 1.00 25.57 ? 87  THR   B HB   1 
ATOM   3748 H HG1  . THR   B 1 107 ? -8.406  30.486 28.738 1.00 27.11 ? 87  THR   B HG1  1 
ATOM   3749 H HG21 . THR   B 1 107 ? -9.814  32.459 31.010 1.00 26.93 ? 87  THR   B HG21 1 
ATOM   3750 H HG22 . THR   B 1 107 ? -11.325 32.147 30.672 1.00 26.93 ? 87  THR   B HG22 1 
ATOM   3751 H HG23 . THR   B 1 107 ? -10.435 31.058 31.390 1.00 26.93 ? 87  THR   B HG23 1 
ATOM   3752 N N    . ASP   B 1 108 ? -10.422 30.428 26.480 1.00 18.87 ? 88  ASP   B N    1 
ATOM   3753 C CA   . ASP   B 1 108 ? -9.775  30.051 25.221 1.00 19.98 ? 88  ASP   B CA   1 
ATOM   3754 C C    . ASP   B 1 108 ? -10.352 28.744 24.695 1.00 19.37 ? 88  ASP   B C    1 
ATOM   3755 O O    . ASP   B 1 108 ? -9.638  27.865 24.234 1.00 19.83 ? 88  ASP   B O    1 
ATOM   3756 C CB   . ASP   B 1 108 ? -8.256  29.931 25.386 1.00 21.94 ? 88  ASP   B CB   1 
ATOM   3757 C CG   . ASP   B 1 108 ? -7.645  31.173 25.885 1.00 23.72 ? 88  ASP   B CG   1 
ATOM   3758 O OD1  . ASP   B 1 108 ? -7.483  32.100 25.074 0.50 22.60 ? 88  ASP   B OD1  1 
ATOM   3759 O OD2  . ASP   B 1 108 ? -7.316  31.218 27.086 0.55 21.80 ? 88  ASP   B OD2  1 
ATOM   3760 H H    . ASP   B 1 108 ? -10.763 31.217 26.477 1.00 22.64 ? 88  ASP   B H    1 
ATOM   3761 H HA   . ASP   B 1 108 ? -9.950  30.749 24.570 1.00 23.98 ? 88  ASP   B HA   1 
ATOM   3762 H HB2  . ASP   B 1 108 ? -8.061  29.223 26.019 1.00 26.33 ? 88  ASP   B HB2  1 
ATOM   3763 H HB3  . ASP   B 1 108 ? -7.859  29.725 24.525 1.00 26.33 ? 88  ASP   B HB3  1 
ATOM   3764 N N    . ILE   B 1 109 ? -11.666 28.609 24.759 1.00 18.94 ? 89  ILE   B N    1 
ATOM   3765 C CA   . ILE   B 1 109 ? -12.316 27.339 24.461 1.00 19.06 ? 89  ILE   B CA   1 
ATOM   3766 C C    . ILE   B 1 109 ? -12.394 27.148 22.954 1.00 19.15 ? 89  ILE   B C    1 
ATOM   3767 O O    . ILE   B 1 109 ? -12.914 28.008 22.226 1.00 22.31 ? 89  ILE   B O    1 
ATOM   3768 C CB   . ILE   B 1 109 ? -13.726 27.315 25.078 1.00 19.97 ? 89  ILE   B CB   1 
ATOM   3769 C CG1  . ILE   B 1 109 ? -13.636 27.358 26.620 1.00 20.71 ? 89  ILE   B CG1  1 
ATOM   3770 C CG2  . ILE   B 1 109 ? -14.474 26.080 24.615 1.00 22.39 ? 89  ILE   B CG2  1 
ATOM   3771 C CD1  . ILE   B 1 109 ? -14.940 27.860 27.245 1.00 22.79 ? 89  ILE   B CD1  1 
ATOM   3772 H H    . ILE   B 1 109 ? -12.209 29.240 24.974 1.00 22.73 ? 89  ILE   B H    1 
ATOM   3773 H HA   . ILE   B 1 109 ? -11.786 26.616 24.832 1.00 22.88 ? 89  ILE   B HA   1 
ATOM   3774 H HB   . ILE   B 1 109 ? -14.212 28.100 24.781 1.00 23.97 ? 89  ILE   B HB   1 
ATOM   3775 H HG12 . ILE   B 1 109 ? -13.460 26.465 26.956 1.00 24.85 ? 89  ILE   B HG12 1 
ATOM   3776 H HG13 . ILE   B 1 109 ? -12.920 27.957 26.882 1.00 24.85 ? 89  ILE   B HG13 1 
ATOM   3777 H HG21 . ILE   B 1 109 ? -15.225 25.924 25.210 1.00 26.87 ? 89  ILE   B HG21 1 
ATOM   3778 H HG22 . ILE   B 1 109 ? -14.794 26.226 23.711 1.00 26.87 ? 89  ILE   B HG22 1 
ATOM   3779 H HG23 . ILE   B 1 109 ? -13.873 25.320 24.635 1.00 26.87 ? 89  ILE   B HG23 1 
ATOM   3780 H HD11 . ILE   B 1 109 ? -14.841 27.878 28.210 1.00 27.35 ? 89  ILE   B HD11 1 
ATOM   3781 H HD12 . ILE   B 1 109 ? -15.125 28.753 26.915 1.00 27.35 ? 89  ILE   B HD12 1 
ATOM   3782 H HD13 . ILE   B 1 109 ? -15.661 27.260 26.997 1.00 27.35 ? 89  ILE   B HD13 1 
ATOM   3783 N N    A GLN   B 1 110 ? -11.871 26.020 22.468 0.47 18.12 ? 90  GLN   B N    1 
ATOM   3784 N N    B GLN   B 1 110 ? -11.874 26.014 22.486 0.53 18.51 ? 90  GLN   B N    1 
ATOM   3785 C CA   A GLN   B 1 110 ? -12.043 25.616 21.073 0.47 18.26 ? 90  GLN   B CA   1 
ATOM   3786 C CA   B GLN   B 1 110 ? -11.979 25.554 21.107 0.53 18.88 ? 90  GLN   B CA   1 
ATOM   3787 C C    A GLN   B 1 110 ? -12.594 24.191 21.020 0.47 17.29 ? 90  GLN   B C    1 
ATOM   3788 C C    B GLN   B 1 110 ? -12.645 24.182 21.143 0.53 17.52 ? 90  GLN   B C    1 
ATOM   3789 O O    A GLN   B 1 110 ? -11.905 23.232 21.390 0.47 16.90 ? 90  GLN   B O    1 
ATOM   3790 O O    B GLN   B 1 110 ? -12.124 23.251 21.774 0.53 16.47 ? 90  GLN   B O    1 
ATOM   3791 C CB   A GLN   B 1 110 ? -10.757 25.722 20.260 0.47 19.89 ? 90  GLN   B CB   1 
ATOM   3792 C CB   B GLN   B 1 110 ? -10.583 25.460 20.493 0.53 20.72 ? 90  GLN   B CB   1 
ATOM   3793 C CG   A GLN   B 1 110 ? -11.039 25.393 18.788 0.47 22.45 ? 90  GLN   B CG   1 
ATOM   3794 C CG   B GLN   B 1 110 ? -9.805  26.786 20.458 0.53 23.19 ? 90  GLN   B CG   1 
ATOM   3795 C CD   A GLN   B 1 110 ? -9.997  25.920 17.851 0.47 25.20 ? 90  GLN   B CD   1 
ATOM   3796 C CD   B GLN   B 1 110 ? -8.436  26.631 19.771 0.53 26.49 ? 90  GLN   B CD   1 
ATOM   3797 O OE1  A GLN   B 1 110 ? -8.887  26.252 18.262 0.47 24.68 ? 90  GLN   B OE1  1 
ATOM   3798 O OE1  B GLN   B 1 110 ? -7.432  26.222 20.390 0.53 27.44 ? 90  GLN   B OE1  1 
ATOM   3799 N NE2  A GLN   B 1 110 ? -10.347 25.999 16.573 0.47 26.87 ? 90  GLN   B NE2  1 
ATOM   3800 N NE2  B GLN   B 1 110 ? -8.404  26.922 18.473 0.53 27.04 ? 90  GLN   B NE2  1 
ATOM   3801 H H    A GLN   B 1 110 ? -11.407 25.466 22.934 0.47 21.74 ? 90  GLN   B H    1 
ATOM   3802 H H    B GLN   B 1 110 ? -11.432 25.465 22.978 0.53 22.21 ? 90  GLN   B H    1 
ATOM   3803 H HA   A GLN   B 1 110 ? -12.696 26.215 20.679 0.47 21.91 ? 90  GLN   B HA   1 
ATOM   3804 H HA   B GLN   B 1 110 ? -12.519 26.154 20.569 0.53 22.66 ? 90  GLN   B HA   1 
ATOM   3805 H HB2  A GLN   B 1 110 ? -10.409 26.626 20.317 0.47 23.87 ? 90  GLN   B HB2  1 
ATOM   3806 H HB2  B GLN   B 1 110 ? -10.060 24.829 21.011 0.53 24.87 ? 90  GLN   B HB2  1 
ATOM   3807 H HB3  A GLN   B 1 110 ? -10.103 25.093 20.601 0.47 23.87 ? 90  GLN   B HB3  1 
ATOM   3808 H HB3  B GLN   B 1 110 ? -10.669 25.148 19.579 0.53 24.87 ? 90  GLN   B HB3  1 
ATOM   3809 H HG2  A GLN   B 1 110 ? -11.072 24.429 18.683 0.47 26.94 ? 90  GLN   B HG2  1 
ATOM   3810 H HG2  B GLN   B 1 110 ? -10.319 27.445 19.966 0.53 27.83 ? 90  GLN   B HG2  1 
ATOM   3811 H HG3  A GLN   B 1 110 ? -11.890 25.783 18.537 0.47 26.94 ? 90  GLN   B HG3  1 
ATOM   3812 H HG3  B GLN   B 1 110 ? -9.656  27.093 21.366 0.53 27.83 ? 90  GLN   B HG3  1 
ATOM   3813 H HE21 A GLN   B 1 110 ? -11.134 25.754 16.326 0.47 32.25 ? 90  GLN   B HE21 1 
ATOM   3814 H HE21 B GLN   B 1 110 ? -9.120  27.179 18.072 0.53 32.45 ? 90  GLN   B HE21 1 
ATOM   3815 H HE22 A GLN   B 1 110 ? -9.788  26.295 15.991 0.47 32.25 ? 90  GLN   B HE22 1 
ATOM   3816 H HE22 B GLN   B 1 110 ? -7.666  26.854 18.035 0.53 32.45 ? 90  GLN   B HE22 1 
ATOM   3817 N N    . ILE   B 1 111 ? -13.822 24.070 20.524 1.00 17.95 ? 91  ILE   B N    1 
ATOM   3818 C CA   . ILE   B 1 111 ? -14.540 22.805 20.456 1.00 18.18 ? 91  ILE   B CA   1 
ATOM   3819 C C    . ILE   B 1 111 ? -14.310 22.146 19.102 1.00 18.73 ? 91  ILE   B C    1 
ATOM   3820 O O    . ILE   B 1 111 ? -14.496 22.770 18.048 1.00 20.96 ? 91  ILE   B O    1 
ATOM   3821 C CB   . ILE   B 1 111 ? -16.044 23.018 20.725 1.00 20.63 ? 91  ILE   B CB   1 
ATOM   3822 C CG1  . ILE   B 1 111 ? -16.256 23.563 22.156 1.00 23.38 ? 91  ILE   B CG1  1 
ATOM   3823 C CG2  . ILE   B 1 111 ? -16.790 21.709 20.525 1.00 22.79 ? 91  ILE   B CG2  1 
ATOM   3824 C CD1  . ILE   B 1 111 ? -17.645 24.034 22.483 1.00 25.62 ? 91  ILE   B CD1  1 
ATOM   3825 H H    A ILE   B 1 111 ? -14.275 24.730 20.211 0.47 21.54 ? 91  ILE   B H    1 
ATOM   3826 H H    B ILE   B 1 111 ? -14.225 24.722 20.134 0.53 21.54 ? 91  ILE   B H    1 
ATOM   3827 H HA   . ILE   B 1 111 ? -14.181 22.206 21.129 1.00 21.82 ? 91  ILE   B HA   1 
ATOM   3828 H HB   . ILE   B 1 111 ? -16.392 23.673 20.100 1.00 24.76 ? 91  ILE   B HB   1 
ATOM   3829 H HG12 . ILE   B 1 111 ? -16.038 22.857 22.784 1.00 28.05 ? 91  ILE   B HG12 1 
ATOM   3830 H HG13 . ILE   B 1 111 ? -15.660 24.317 22.284 1.00 28.05 ? 91  ILE   B HG13 1 
ATOM   3831 H HG21 . ILE   B 1 111 ? -17.676 21.788 20.910 1.00 27.35 ? 91  ILE   B HG21 1 
ATOM   3832 H HG22 . ILE   B 1 111 ? -16.857 21.526 19.574 1.00 27.35 ? 91  ILE   B HG22 1 
ATOM   3833 H HG23 . ILE   B 1 111 ? -16.300 20.996 20.965 1.00 27.35 ? 91  ILE   B HG23 1 
ATOM   3834 H HD11 . ILE   B 1 111 ? -17.633 24.478 23.345 1.00 30.74 ? 91  ILE   B HD11 1 
ATOM   3835 H HD12 . ILE   B 1 111 ? -17.939 24.654 21.796 1.00 30.74 ? 91  ILE   B HD12 1 
ATOM   3836 H HD13 . ILE   B 1 111 ? -18.240 23.269 22.513 1.00 30.74 ? 91  ILE   B HD13 1 
ATOM   3837 N N    . PHE   B 1 112 ? -13.947 20.865 19.137 1.00 17.65 ? 92  PHE   B N    1 
ATOM   3838 C CA   . PHE   B 1 112 ? -13.722 20.062 17.939 1.00 18.22 ? 92  PHE   B CA   1 
ATOM   3839 C C    . PHE   B 1 112 ? -14.776 18.973 17.870 1.00 18.06 ? 92  PHE   B C    1 
ATOM   3840 O O    . PHE   B 1 112 ? -14.824 18.081 18.721 1.00 18.40 ? 92  PHE   B O    1 
ATOM   3841 C CB   . PHE   B 1 112 ? -12.324 19.460 17.948 1.00 18.52 ? 92  PHE   B CB   1 
ATOM   3842 C CG   . PHE   B 1 112 ? -11.240 20.492 17.973 1.00 19.39 ? 92  PHE   B CG   1 
ATOM   3843 C CD1  . PHE   B 1 112 ? -10.798 21.076 16.792 1.00 20.33 ? 92  PHE   B CD1  1 
ATOM   3844 C CD2  . PHE   B 1 112 ? -10.678 20.916 19.175 1.00 20.83 ? 92  PHE   B CD2  1 
ATOM   3845 C CE1  . PHE   B 1 112 ? -9.804  22.039 16.796 1.00 22.02 ? 92  PHE   B CE1  1 
ATOM   3846 C CE2  . PHE   B 1 112 ? -9.664  21.908 19.177 1.00 21.72 ? 92  PHE   B CE2  1 
ATOM   3847 C CZ   . PHE   B 1 112 ? -9.249  22.459 17.984 1.00 23.54 ? 92  PHE   B CZ   1 
ATOM   3848 H H    . PHE   B 1 112 ? -13.821 20.428 19.866 1.00 21.18 ? 92  PHE   B H    1 
ATOM   3849 H HA   . PHE   B 1 112 ? -13.818 20.629 17.158 1.00 21.87 ? 92  PHE   B HA   1 
ATOM   3850 H HB2  . PHE   B 1 112 ? -12.226 18.904 18.738 1.00 22.23 ? 92  PHE   B HB2  1 
ATOM   3851 H HB3  . PHE   B 1 112 ? -12.208 18.923 17.149 1.00 22.23 ? 92  PHE   B HB3  1 
ATOM   3852 H HD1  . PHE   B 1 112 ? -11.177 20.814 15.984 1.00 24.39 ? 92  PHE   B HD1  1 
ATOM   3853 H HD2  . PHE   B 1 112 ? -10.968 20.547 19.978 1.00 25.00 ? 92  PHE   B HD2  1 
ATOM   3854 H HE1  . PHE   B 1 112 ? -9.510  22.404 15.993 1.00 26.42 ? 92  PHE   B HE1  1 
ATOM   3855 H HE2  . PHE   B 1 112 ? -9.282  22.185 19.978 1.00 26.06 ? 92  PHE   B HE2  1 
ATOM   3856 H HZ   . PHE   B 1 112 ? -8.591  23.117 17.981 1.00 28.25 ? 92  PHE   B HZ   1 
ATOM   3857 N N    . GLU   B 1 113 ? -15.641 19.072 16.865 1.00 18.71 ? 93  GLU   B N    1 
ATOM   3858 C CA   . GLU   B 1 113 ? -16.470 17.952 16.468 1.00 21.16 ? 93  GLU   B CA   1 
ATOM   3859 C C    . GLU   B 1 113 ? -15.568 16.920 15.804 1.00 20.45 ? 93  GLU   B C    1 
ATOM   3860 O O    . GLU   B 1 113 ? -14.430 17.217 15.426 1.00 21.04 ? 93  GLU   B O    1 
ATOM   3861 C CB   . GLU   B 1 113 ? -17.559 18.405 15.490 1.00 26.42 ? 93  GLU   B CB   1 
ATOM   3862 C CG   . GLU   B 1 113 ? -18.269 19.695 15.865 1.00 31.56 ? 93  GLU   B CG   1 
ATOM   3863 C CD   . GLU   B 1 113 ? -19.064 20.293 14.699 1.00 37.78 ? 93  GLU   B CD   1 
ATOM   3864 O OE1  . GLU   B 1 113 ? -18.955 19.773 13.572 1.00 38.69 ? 93  GLU   B OE1  1 
ATOM   3865 O OE2  . GLU   B 1 113 ? -19.791 21.278 14.917 1.00 41.76 ? 93  GLU   B OE2  1 
ATOM   3866 H H    . GLU   B 1 113 ? -15.764 19.783 16.397 1.00 22.45 ? 93  GLU   B H    1 
ATOM   3867 H HA   . GLU   B 1 113 ? -16.921 17.560 17.233 1.00 25.40 ? 93  GLU   B HA   1 
ATOM   3868 H HB2  . GLU   B 1 113 ? -17.151 18.540 14.620 1.00 31.70 ? 93  GLU   B HB2  1 
ATOM   3869 H HB3  . GLU   B 1 113 ? -18.231 17.708 15.437 1.00 31.70 ? 93  GLU   B HB3  1 
ATOM   3870 H HG2  . GLU   B 1 113 ? -18.888 19.516 16.590 1.00 37.88 ? 93  GLU   B HG2  1 
ATOM   3871 H HG3  . GLU   B 1 113 ? -17.610 20.349 16.145 1.00 37.88 ? 93  GLU   B HG3  1 
ATOM   3872 N N    . THR   B 1 114 ? -16.040 15.687 15.708 1.00 19.96 ? 94  THR   B N    1 
ATOM   3873 C CA   . THR   B 1 114 ? -15.299 14.620 15.052 1.00 20.46 ? 94  THR   B CA   1 
ATOM   3874 C C    . THR   B 1 114 ? -16.214 13.844 14.110 1.00 20.51 ? 94  THR   B C    1 
ATOM   3875 O O    . THR   B 1 114 ? -17.417 14.105 14.007 1.00 21.38 ? 94  THR   B O    1 
ATOM   3876 C CB   . THR   B 1 114 ? -14.603 13.661 16.038 1.00 19.91 ? 94  THR   B CB   1 
ATOM   3877 O OG1  . THR   B 1 114 ? -15.554 12.724 16.562 1.00 20.73 ? 94  THR   B OG1  1 
ATOM   3878 C CG2  . THR   B 1 114 ? -13.903 14.424 17.154 1.00 20.05 ? 94  THR   B CG2  1 
ATOM   3879 H H    . THR   B 1 114 ? -16.802 15.439 16.021 1.00 23.96 ? 94  THR   B H    1 
ATOM   3880 H HA   . THR   B 1 114 ? -14.606 15.050 14.526 1.00 24.55 ? 94  THR   B HA   1 
ATOM   3881 H HB   . THR   B 1 114 ? -13.914 13.162 15.571 1.00 23.89 ? 94  THR   B HB   1 
ATOM   3882 H HG1  . THR   B 1 114 ? -16.160 13.132 16.977 1.00 24.88 ? 94  THR   B HG1  1 
ATOM   3883 H HG21 . THR   B 1 114 ? -13.405 13.809 17.715 1.00 24.06 ? 94  THR   B HG21 1 
ATOM   3884 H HG22 . THR   B 1 114 ? -13.289 15.074 16.777 1.00 24.06 ? 94  THR   B HG22 1 
ATOM   3885 H HG23 . THR   B 1 114 ? -14.557 14.888 17.699 1.00 24.06 ? 94  THR   B HG23 1 
ATOM   3886 N N    . GLN   B 1 115 ? -15.637 12.847 13.433 1.00 20.69 ? 95  GLN   B N    1 
ATOM   3887 C CA   . GLN   B 1 115 ? -16.434 11.988 12.568 1.00 22.60 ? 95  GLN   B CA   1 
ATOM   3888 C C    . GLN   B 1 115 ? -17.444 11.175 13.356 1.00 22.76 ? 95  GLN   B C    1 
ATOM   3889 O O    . GLN   B 1 115 ? -18.425 10.713 12.777 1.00 25.00 ? 95  GLN   B O    1 
ATOM   3890 C CB   . GLN   B 1 115 ? -15.564 11.039 11.739 1.00 22.74 ? 95  GLN   B CB   1 
ATOM   3891 C CG   . GLN   B 1 115 ? -14.827 9.941  12.496 1.00 23.09 ? 95  GLN   B CG   1 
ATOM   3892 C CD   . GLN   B 1 115 ? -13.457 10.354 12.996 1.00 22.86 ? 95  GLN   B CD   1 
ATOM   3893 O OE1  . GLN   B 1 115 ? -13.189 11.503 13.308 1.00 21.07 ? 95  GLN   B OE1  1 
ATOM   3894 N NE2  . GLN   B 1 115 ? -12.561 9.416  12.981 1.00 27.81 ? 95  GLN   B NE2  1 
ATOM   3895 H H    . GLN   B 1 115 ? -14.799 12.654 13.459 1.00 24.83 ? 95  GLN   B H    1 
ATOM   3896 H HA   . GLN   B 1 115 ? -16.901 12.563 11.943 1.00 27.12 ? 95  GLN   B HA   1 
ATOM   3897 H HB2  . GLN   B 1 115 ? -16.135 10.601 11.089 1.00 27.29 ? 95  GLN   B HB2  1 
ATOM   3898 H HB3  . GLN   B 1 115 ? -14.891 11.570 11.286 1.00 27.29 ? 95  GLN   B HB3  1 
ATOM   3899 H HG2  . GLN   B 1 115 ? -15.358 9.684  13.267 1.00 27.71 ? 95  GLN   B HG2  1 
ATOM   3900 H HG3  . GLN   B 1 115 ? -14.710 9.180  11.906 1.00 27.71 ? 95  GLN   B HG3  1 
ATOM   3901 H HE21 . GLN   B 1 115 ? -12.767 8.629  12.701 1.00 33.37 ? 95  GLN   B HE21 1 
ATOM   3902 H HE22 . GLN   B 1 115 ? -11.761 9.580  13.251 1.00 33.37 ? 95  GLN   B HE22 1 
ATOM   3903 N N    . ASP   B 1 116 ? -17.211 10.982 14.653 1.00 21.73 ? 96  ASP   B N    1 
ATOM   3904 C CA   . ASP   B 1 116 ? -18.166 10.330 15.538 1.00 21.90 ? 96  ASP   B CA   1 
ATOM   3905 C C    . ASP   B 1 116 ? -19.075 11.418 16.107 1.00 21.46 ? 96  ASP   B C    1 
ATOM   3906 O O    . ASP   B 1 116 ? -18.599 12.281 16.866 1.00 21.24 ? 96  ASP   B O    1 
ATOM   3907 C CB   . ASP   B 1 116 ? -17.416 9.601  16.648 1.00 22.64 ? 96  ASP   B CB   1 
ATOM   3908 C CG   . ASP   B 1 116 ? -18.322 8.845  17.603 1.00 23.05 ? 96  ASP   B CG   1 
ATOM   3909 O OD1  . ASP   B 1 116 ? -19.540 9.130  17.655 1.00 24.14 ? 96  ASP   B OD1  1 
ATOM   3910 O OD2  . ASP   B 1 116 ? -17.763 7.984  18.340 1.00 25.85 ? 96  ASP   B OD2  1 
ATOM   3911 H H    . ASP   B 1 116 ? -16.489 11.226 15.051 1.00 26.07 ? 96  ASP   B H    1 
ATOM   3912 H HA   . ASP   B 1 116 ? -18.712 9.684  15.063 1.00 26.28 ? 96  ASP   B HA   1 
ATOM   3913 H HB2  . ASP   B 1 116 ? -16.809 8.960  16.246 1.00 27.17 ? 96  ASP   B HB2  1 
ATOM   3914 H HB3  . ASP   B 1 116 ? -16.917 10.252 17.166 1.00 27.17 ? 96  ASP   B HB3  1 
ATOM   3915 N N    . PRO   B 1 117 ? -20.357 11.439 15.762 1.00 22.35 ? 97  PRO   B N    1 
ATOM   3916 C CA   . PRO   B 1 117 ? -21.228 12.510 16.265 1.00 22.04 ? 97  PRO   B CA   1 
ATOM   3917 C C    . PRO   B 1 117 ? -21.352 12.532 17.785 1.00 22.63 ? 97  PRO   B C    1 
ATOM   3918 O O    . PRO   B 1 117 ? -21.789 13.557 18.344 1.00 23.14 ? 97  PRO   B O    1 
ATOM   3919 C CB   . PRO   B 1 117 ? -22.578 12.203 15.606 1.00 24.08 ? 97  PRO   B CB   1 
ATOM   3920 C CG   . PRO   B 1 117 ? -22.536 10.736 15.376 1.00 26.07 ? 97  PRO   B CG   1 
ATOM   3921 C CD   . PRO   B 1 117 ? -21.103 10.436 14.988 1.00 24.35 ? 97  PRO   B CD   1 
ATOM   3922 H HA   . PRO   B 1 117 ? -20.906 13.371 15.956 1.00 26.45 ? 97  PRO   B HA   1 
ATOM   3923 H HB2  . PRO   B 1 117 ? -23.304 12.444 16.201 1.00 28.90 ? 97  PRO   B HB2  1 
ATOM   3924 H HB3  . PRO   B 1 117 ? -22.660 12.687 14.769 1.00 28.90 ? 97  PRO   B HB3  1 
ATOM   3925 H HG2  . PRO   B 1 117 ? -22.779 10.268 16.190 1.00 31.28 ? 97  PRO   B HG2  1 
ATOM   3926 H HG3  . PRO   B 1 117 ? -23.146 10.496 14.661 1.00 31.28 ? 97  PRO   B HG3  1 
ATOM   3927 H HD2  . PRO   B 1 117 ? -20.851 9.535  15.247 1.00 29.22 ? 97  PRO   B HD2  1 
ATOM   3928 H HD3  . PRO   B 1 117 ? -20.966 10.556 14.035 1.00 29.22 ? 97  PRO   B HD3  1 
ATOM   3929 N N    . ASN   B 1 118 ? -20.989 11.435 18.454 1.00 21.69 ? 98  ASN   B N    1 
ATOM   3930 C CA   . ASN   B 1 118 ? -21.012 11.319 19.896 1.00 21.49 ? 98  ASN   B CA   1 
ATOM   3931 C C    . ASN   B 1 118 ? -19.654 11.504 20.561 1.00 21.22 ? 98  ASN   B C    1 
ATOM   3932 O O    . ASN   B 1 118 ? -19.523 11.185 21.744 1.00 22.51 ? 98  ASN   B O    1 
ATOM   3933 C CB   . ASN   B 1 118 ? -21.618 9.983  20.290 1.00 22.58 ? 98  ASN   B CB   1 
ATOM   3934 C CG   . ASN   B 1 118 ? -23.077 9.911  19.954 1.00 26.45 ? 98  ASN   B CG   1 
ATOM   3935 O OD1  . ASN   B 1 118 ? -23.834 10.777 20.346 1.00 28.29 ? 98  ASN   B OD1  1 
ATOM   3936 N ND2  . ASN   B 1 118 ? -23.461 8.933  19.163 1.00 29.27 ? 98  ASN   B ND2  1 
ATOM   3937 H H    . ASN   B 1 118 ? -20.714 10.717 18.068 1.00 26.03 ? 98  ASN   B H    1 
ATOM   3938 H HA   . ASN   B 1 118 ? -21.578 12.028 20.240 1.00 25.79 ? 98  ASN   B HA   1 
ATOM   3939 H HB2  . ASN   B 1 118 ? -21.161 9.272  19.814 1.00 27.10 ? 98  ASN   B HB2  1 
ATOM   3940 H HB3  . ASN   B 1 118 ? -21.520 9.858  21.247 1.00 27.10 ? 98  ASN   B HB3  1 
ATOM   3941 H HD21 . ASN   B 1 118 ? -24.290 8.856  18.945 1.00 35.12 ? 98  ASN   B HD21 1 
ATOM   3942 H HD22 . ASN   B 1 118 ? -22.884 8.371  18.862 1.00 35.12 ? 98  ASN   B HD22 1 
ATOM   3943 N N    . TRP   B 1 119 ? -18.651 12.032 19.858 1.00 19.46 ? 99  TRP   B N    1 
ATOM   3944 C CA   . TRP   B 1 119 ? -17.333 12.248 20.456 1.00 18.31 ? 99  TRP   B CA   1 
ATOM   3945 C C    . TRP   B 1 119 ? -16.831 13.627 20.059 1.00 18.26 ? 99  TRP   B C    1 
ATOM   3946 O O    . TRP   B 1 119 ? -16.724 13.951 18.868 1.00 19.26 ? 99  TRP   B O    1 
ATOM   3947 C CB   . TRP   B 1 119 ? -16.356 11.149 20.014 1.00 18.87 ? 99  TRP   B CB   1 
ATOM   3948 C CG   . TRP   B 1 119 ? -15.171 10.911 20.943 1.00 18.36 ? 99  TRP   B CG   1 
ATOM   3949 C CD1  . TRP   B 1 119 ? -14.558 11.798 21.789 1.00 18.55 ? 99  TRP   B CD1  1 
ATOM   3950 C CD2  . TRP   B 1 119 ? -14.484 9.656  21.111 1.00 19.35 ? 99  TRP   B CD2  1 
ATOM   3951 N NE1  . TRP   B 1 119 ? -13.503 11.169 22.446 1.00 17.88 ? 99  TRP   B NE1  1 
ATOM   3952 C CE2  . TRP   B 1 119 ? -13.456 9.855  22.057 1.00 18.23 ? 99  TRP   B CE2  1 
ATOM   3953 C CE3  . TRP   B 1 119 ? -14.650 8.377  20.563 1.00 20.75 ? 99  TRP   B CE3  1 
ATOM   3954 C CZ2  . TRP   B 1 119 ? -12.596 8.834  22.448 1.00 20.01 ? 99  TRP   B CZ2  1 
ATOM   3955 C CZ3  . TRP   B 1 119 ? -13.759 7.373  20.928 1.00 22.20 ? 99  TRP   B CZ3  1 
ATOM   3956 C CH2  . TRP   B 1 119 ? -12.757 7.605  21.871 1.00 20.89 ? 99  TRP   B CH2  1 
ATOM   3957 H H    . TRP   B 1 119 ? -18.709 12.272 19.034 1.00 23.35 ? 99  TRP   B H    1 
ATOM   3958 H HA   . TRP   B 1 119 ? -17.391 12.227 21.425 1.00 21.98 ? 99  TRP   B HA   1 
ATOM   3959 H HB2  . TRP   B 1 119 ? -16.845 10.314 19.951 1.00 22.64 ? 99  TRP   B HB2  1 
ATOM   3960 H HB3  . TRP   B 1 119 ? -15.998 11.391 19.146 1.00 22.64 ? 99  TRP   B HB3  1 
ATOM   3961 H HD1  . TRP   B 1 119 ? -14.808 12.686 21.906 1.00 22.26 ? 99  TRP   B HD1  1 
ATOM   3962 H HE1  . TRP   B 1 119 ? -12.968 11.545 23.005 1.00 21.46 ? 99  TRP   B HE1  1 
ATOM   3963 H HE3  . TRP   B 1 119 ? -15.342 8.203  19.966 1.00 24.90 ? 99  TRP   B HE3  1 
ATOM   3964 H HZ2  . TRP   B 1 119 ? -11.932 8.983  23.082 1.00 24.01 ? 99  TRP   B HZ2  1 
ATOM   3965 H HZ3  . TRP   B 1 119 ? -13.832 6.533  20.536 1.00 26.64 ? 99  TRP   B HZ3  1 
ATOM   3966 H HH2  . TRP   B 1 119 ? -12.188 6.910  22.111 1.00 25.07 ? 99  TRP   B HH2  1 
ATOM   3967 N N    . PHE   B 1 120 ? -16.490 14.430 21.074 1.00 17.86 ? 100 PHE   B N    1 
ATOM   3968 C CA   . PHE   B 1 120 ? -15.950 15.767 20.908 1.00 16.70 ? 100 PHE   B CA   1 
ATOM   3969 C C    . PHE   B 1 120 ? -14.647 15.885 21.694 1.00 16.78 ? 100 PHE   B C    1 
ATOM   3970 O O    . PHE   B 1 120 ? -14.462 15.227 22.719 1.00 17.38 ? 100 PHE   B O    1 
ATOM   3971 C CB   . PHE   B 1 120 ? -16.886 16.867 21.421 1.00 18.30 ? 100 PHE   B CB   1 
ATOM   3972 C CG   . PHE   B 1 120 ? -18.112 17.027 20.600 1.00 19.46 ? 100 PHE   B CG   1 
ATOM   3973 C CD1  . PHE   B 1 120 ? -19.084 16.045 20.577 1.00 23.45 ? 100 PHE   B CD1  1 
ATOM   3974 C CD2  . PHE   B 1 120 ? -18.299 18.169 19.840 1.00 20.88 ? 100 PHE   B CD2  1 
ATOM   3975 C CE1  . PHE   B 1 120 ? -20.229 16.199 19.793 1.00 26.09 ? 100 PHE   B CE1  1 
ATOM   3976 C CE2  . PHE   B 1 120 ? -19.433 18.327 19.064 1.00 24.36 ? 100 PHE   B CE2  1 
ATOM   3977 C CZ   . PHE   B 1 120 ? -20.386 17.339 19.046 1.00 25.70 ? 100 PHE   B CZ   1 
ATOM   3978 H H    . PHE   B 1 120 ? -16.569 14.205 21.900 1.00 21.43 ? 100 PHE   B H    1 
ATOM   3979 H HA   . PHE   B 1 120 ? -15.797 15.906 19.961 1.00 20.04 ? 100 PHE   B HA   1 
ATOM   3980 H HB2  . PHE   B 1 120 ? -17.160 16.649 22.326 1.00 21.96 ? 100 PHE   B HB2  1 
ATOM   3981 H HB3  . PHE   B 1 120 ? -16.410 17.713 21.414 1.00 21.96 ? 100 PHE   B HB3  1 
ATOM   3982 H HD1  . PHE   B 1 120 ? -18.974 15.276 21.087 1.00 28.14 ? 100 PHE   B HD1  1 
ATOM   3983 H HD2  . PHE   B 1 120 ? -17.653 18.839 19.851 1.00 25.05 ? 100 PHE   B HD2  1 
ATOM   3984 H HE1  . PHE   B 1 120 ? -20.880 15.535 19.778 1.00 31.31 ? 100 PHE   B HE1  1 
ATOM   3985 H HE2  . PHE   B 1 120 ? -19.549 19.098 18.556 1.00 29.23 ? 100 PHE   B HE2  1 
ATOM   3986 H HZ   . PHE   B 1 120 ? -21.147 17.444 18.521 1.00 30.84 ? 100 PHE   B HZ   1 
ATOM   3987 N N    . TRP   B 1 121 ? -13.764 16.766 21.229 1.00 16.66 ? 101 TRP   B N    1 
ATOM   3988 C CA   . TRP   B 1 121 ? -12.578 17.173 21.978 1.00 16.15 ? 101 TRP   B CA   1 
ATOM   3989 C C    . TRP   B 1 121 ? -12.621 18.682 22.154 1.00 16.06 ? 101 TRP   B C    1 
ATOM   3990 O O    . TRP   B 1 121 ? -13.162 19.411 21.317 1.00 17.88 ? 101 TRP   B O    1 
ATOM   3991 C CB   . TRP   B 1 121 ? -11.271 16.765 21.208 1.00 16.61 ? 101 TRP   B CB   1 
ATOM   3992 C CG   . TRP   B 1 121 ? -11.082 15.284 21.242 1.00 17.01 ? 101 TRP   B CG   1 
ATOM   3993 C CD1  . TRP   B 1 121 ? -11.561 14.394 20.349 1.00 17.68 ? 101 TRP   B CD1  1 
ATOM   3994 C CD2  . TRP   B 1 121 ? -10.340 14.528 22.212 1.00 16.50 ? 101 TRP   B CD2  1 
ATOM   3995 N NE1  . TRP   B 1 121 ? -11.235 13.112 20.731 1.00 17.86 ? 101 TRP   B NE1  1 
ATOM   3996 C CE2  . TRP   B 1 121 ? -10.453 13.172 21.856 1.00 16.58 ? 101 TRP   B CE2  1 
ATOM   3997 C CE3  . TRP   B 1 121 ? -9.596  14.866 23.356 1.00 16.87 ? 101 TRP   B CE3  1 
ATOM   3998 C CZ2  . TRP   B 1 121 ? -9.857  12.148 22.598 1.00 16.96 ? 101 TRP   B CZ2  1 
ATOM   3999 C CZ3  . TRP   B 1 121 ? -8.993  13.854 24.075 1.00 16.78 ? 101 TRP   B CZ3  1 
ATOM   4000 C CH2  . TRP   B 1 121 ? -9.138  12.511 23.700 1.00 17.03 ? 101 TRP   B CH2  1 
ATOM   4001 H H    . TRP   B 1 121 ? -13.832 17.151 20.463 1.00 19.99 ? 101 TRP   B H    1 
ATOM   4002 H HA   . TRP   B 1 121 ? -12.558 16.751 22.852 1.00 19.39 ? 101 TRP   B HA   1 
ATOM   4003 H HB2  . TRP   B 1 121 ? -11.339 17.047 20.282 1.00 19.93 ? 101 TRP   B HB2  1 
ATOM   4004 H HB3  . TRP   B 1 121 ? -10.503 17.184 21.627 1.00 19.93 ? 101 TRP   B HB3  1 
ATOM   4005 H HD1  . TRP   B 1 121 ? -12.042 14.614 19.585 1.00 21.22 ? 101 TRP   B HD1  1 
ATOM   4006 H HE1  . TRP   B 1 121 ? -11.482 12.392 20.331 1.00 21.43 ? 101 TRP   B HE1  1 
ATOM   4007 H HE3  . TRP   B 1 121 ? -9.512  15.753 23.622 1.00 20.24 ? 101 TRP   B HE3  1 
ATOM   4008 H HZ2  . TRP   B 1 121 ? -9.947  11.255 22.351 1.00 20.35 ? 101 TRP   B HZ2  1 
ATOM   4009 H HZ3  . TRP   B 1 121 ? -8.481  14.067 24.822 1.00 20.13 ? 101 TRP   B HZ3  1 
ATOM   4010 H HH2  . TRP   B 1 121 ? -8.734  11.851 24.215 1.00 20.44 ? 101 TRP   B HH2  1 
ATOM   4011 N N    . VAL   B 1 122 ? -12.041 19.143 23.250 1.00 15.67 ? 102 VAL   B N    1 
ATOM   4012 C CA   . VAL   B 1 122 ? -11.955 20.565 23.527 1.00 15.31 ? 102 VAL   B CA   1 
ATOM   4013 C C    . VAL   B 1 122 ? -10.531 20.892 23.929 1.00 15.53 ? 102 VAL   B C    1 
ATOM   4014 O O    . VAL   B 1 122 ? -9.959  20.204 24.770 1.00 17.29 ? 102 VAL   B O    1 
ATOM   4015 C CB   . VAL   B 1 122 ? -12.908 20.985 24.660 1.00 16.77 ? 102 VAL   B CB   1 
ATOM   4016 C CG1  . VAL   B 1 122 ? -12.775 22.468 24.963 1.00 18.42 ? 102 VAL   B CG1  1 
ATOM   4017 C CG2  . VAL   B 1 122 ? -14.355 20.614 24.314 1.00 17.75 ? 102 VAL   B CG2  1 
ATOM   4018 H H    . VAL   B 1 122 ? -11.686 18.645 23.854 1.00 18.80 ? 102 VAL   B H    1 
ATOM   4019 H HA   . VAL   B 1 122 ? -12.179 21.054 22.720 1.00 18.37 ? 102 VAL   B HA   1 
ATOM   4020 H HB   . VAL   B 1 122 ? -12.663 20.503 25.465 1.00 20.13 ? 102 VAL   B HB   1 
ATOM   4021 H HG11 . VAL   B 1 122 ? -13.493 22.734 25.558 1.00 22.11 ? 102 VAL   B HG11 1 
ATOM   4022 H HG12 . VAL   B 1 122 ? -11.918 22.629 25.386 1.00 22.11 ? 102 VAL   B HG12 1 
ATOM   4023 H HG13 . VAL   B 1 122 ? -12.832 22.966 24.132 1.00 22.11 ? 102 VAL   B HG13 1 
ATOM   4024 H HG21 . VAL   B 1 122 ? -14.937 20.913 25.031 1.00 21.30 ? 102 VAL   B HG21 1 
ATOM   4025 H HG22 . VAL   B 1 122 ? -14.603 21.049 23.484 1.00 21.30 ? 102 VAL   B HG22 1 
ATOM   4026 H HG23 . VAL   B 1 122 ? -14.419 19.651 24.216 1.00 21.30 ? 102 VAL   B HG23 1 
ATOM   4027 N N    . GLU   B 1 123 ? -9.977  21.944 23.335 1.00 15.32 ? 103 GLU   B N    1 
ATOM   4028 C CA   . GLU   B 1 123 ? -8.707  22.517 23.770 1.00 15.46 ? 103 GLU   B CA   1 
ATOM   4029 C C    . GLU   B 1 123 ? -9.044  23.833 24.469 1.00 16.21 ? 103 GLU   B C    1 
ATOM   4030 O O    . GLU   B 1 123 ? -9.816  24.638 23.938 1.00 17.29 ? 103 GLU   B O    1 
ATOM   4031 C CB   . GLU   B 1 123 ? -7.746  22.749 22.591 1.00 16.11 ? 103 GLU   B CB   1 
ATOM   4032 C CG   . GLU   B 1 123 ? -6.441  23.331 23.096 1.00 17.16 ? 103 GLU   B CG   1 
ATOM   4033 C CD   . GLU   B 1 123 ? -5.345  23.458 22.047 1.00 18.29 ? 103 GLU   B CD   1 
ATOM   4034 O OE1  . GLU   B 1 123 ? -5.602  23.283 20.839 1.00 18.86 ? 103 GLU   B OE1  1 
ATOM   4035 O OE2  . GLU   B 1 123 ? -4.189  23.736 22.471 1.00 19.24 ? 103 GLU   B OE2  1 
ATOM   4036 H H    . GLU   B 1 123 ? -10.325 22.352 22.663 1.00 18.38 ? 103 GLU   B H    1 
ATOM   4037 H HA   . GLU   B 1 123 ? -8.246  21.920 24.380 1.00 18.56 ? 103 GLU   B HA   1 
ATOM   4038 H HB2  . GLU   B 1 123 ? -7.561  21.906 22.148 1.00 19.33 ? 103 GLU   B HB2  1 
ATOM   4039 H HB3  . GLU   B 1 123 ? -8.143  23.373 21.963 1.00 19.33 ? 103 GLU   B HB3  1 
ATOM   4040 H HG2  . GLU   B 1 123 ? -6.615  24.220 23.444 1.00 20.60 ? 103 GLU   B HG2  1 
ATOM   4041 H HG3  . GLU   B 1 123 ? -6.102  22.759 23.802 1.00 20.60 ? 103 GLU   B HG3  1 
ATOM   4042 N N    . CYS   B 1 124 ? -8.491  24.048 25.661 1.00 15.55 ? 104 CYS   B N    1 
ATOM   4043 C CA   . CYS   B 1 124 ? -8.798  25.273 26.385 1.00 15.50 ? 104 CYS   B CA   1 
ATOM   4044 C C    . CYS   B 1 124 ? -7.724  25.529 27.420 1.00 16.31 ? 104 CYS   B C    1 
ATOM   4045 O O    . CYS   B 1 124 ? -6.730  24.804 27.520 1.00 17.30 ? 104 CYS   B O    1 
ATOM   4046 C CB   . CYS   B 1 124 ? -10.176 25.175 27.064 1.00 16.71 ? 104 CYS   B CB   1 
ATOM   4047 S SG   . CYS   B 1 124 ? -10.267 24.015 28.409 1.00 18.25 ? 104 CYS   B SG   1 
ATOM   4048 H H    . CYS   B 1 124 ? -7.948  23.511 26.058 1.00 18.67 ? 104 CYS   B H    1 
ATOM   4049 H HA   . CYS   B 1 124 ? -8.794  26.007 25.751 1.00 18.61 ? 104 CYS   B HA   1 
ATOM   4050 H HB2  . CYS   B 1 124 ? -10.409 26.048 27.416 1.00 20.06 ? 104 CYS   B HB2  1 
ATOM   4051 H HB3  . CYS   B 1 124 ? -10.827 24.901 26.399 1.00 20.06 ? 104 CYS   B HB3  1 
ATOM   4052 H HG   . CYS   B 1 124 ? -9.505  24.357 29.272 1.00 21.91 ? 104 CYS   B HG   1 
ATOM   4053 N N    . ARG   B 1 125 ? -7.899  26.624 28.148 1.00 16.53 ? 105 ARG   B N    1 
ATOM   4054 C CA   . ARG   B 1 125 ? -7.135  26.869 29.361 1.00 16.75 ? 105 ARG   B CA   1 
ATOM   4055 C C    . ARG   B 1 125 ? -8.109  26.944 30.530 1.00 16.75 ? 105 ARG   B C    1 
ATOM   4056 O O    . ARG   B 1 125 ? -9.325  27.019 30.351 1.00 17.32 ? 105 ARG   B O    1 
ATOM   4057 C CB   . ARG   B 1 125 ? -6.307  28.150 29.253 1.00 18.49 ? 105 ARG   B CB   1 
ATOM   4058 C CG   . ARG   B 1 125 ? -5.247  28.009 28.176 1.00 20.43 ? 105 ARG   B CG   1 
ATOM   4059 C CD   . ARG   B 1 125 ? -4.301  29.170 28.150 1.00 24.45 ? 105 ARG   B CD   1 
ATOM   4060 N NE   . ARG   B 1 125 ? -3.673  29.354 29.444 1.00 29.21 ? 105 ARG   B NE   1 
ATOM   4061 C CZ   . ARG   B 1 125 ? -2.649  28.663 29.928 1.00 29.76 ? 105 ARG   B CZ   1 
ATOM   4062 N NH1  . ARG   B 1 125 ? -1.889  27.880 29.158 1.00 29.31 ? 105 ARG   B NH1  1 
ATOM   4063 N NH2  . ARG   B 1 125 ? -2.399  28.744 31.227 1.00 28.16 ? 105 ARG   B NH2  1 
ATOM   4064 H H    . ARG   B 1 125 ? -8.461  27.245 27.957 1.00 19.84 ? 105 ARG   B H    1 
ATOM   4065 H HA   . ARG   B 1 125 ? -6.510  26.144 29.517 1.00 20.10 ? 105 ARG   B HA   1 
ATOM   4066 H HB2  . ARG   B 1 125 ? -6.887  28.893 29.021 1.00 22.19 ? 105 ARG   B HB2  1 
ATOM   4067 H HB3  . ARG   B 1 125 ? -5.867  28.324 30.099 1.00 22.19 ? 105 ARG   B HB3  1 
ATOM   4068 H HG2  . ARG   B 1 125 ? -4.732  27.204 28.341 1.00 24.52 ? 105 ARG   B HG2  1 
ATOM   4069 H HG3  . ARG   B 1 125 ? -5.680  27.954 27.309 1.00 24.52 ? 105 ARG   B HG3  1 
ATOM   4070 H HD2  . ARG   B 1 125 ? -3.607  29.007 27.492 1.00 29.35 ? 105 ARG   B HD2  1 
ATOM   4071 H HD3  . ARG   B 1 125 ? -4.787  29.978 27.926 1.00 29.35 ? 105 ARG   B HD3  1 
ATOM   4072 H HE   . ARG   B 1 125 ? -3.996  29.972 29.947 1.00 35.05 ? 105 ARG   B HE   1 
ATOM   4073 H HH11 . ARG   B 1 125 ? -2.056  27.811 28.317 1.00 35.17 ? 105 ARG   B HH11 1 
ATOM   4074 H HH12 . ARG   B 1 125 ? -1.233  27.445 29.503 1.00 35.17 ? 105 ARG   B HH12 1 
ATOM   4075 H HH21 . ARG   B 1 125 ? -2.894  29.234 31.731 1.00 33.79 ? 105 ARG   B HH21 1 
ATOM   4076 H HH22 . ARG   B 1 125 ? -1.741  28.306 31.566 1.00 33.79 ? 105 ARG   B HH22 1 
ATOM   4077 N N    . GLY   B 1 126 ? -7.570  26.904 31.728 1.00 16.83 ? 106 GLY   B N    1 
ATOM   4078 C CA   . GLY   B 1 126 ? -8.377  27.079 32.921 1.00 17.63 ? 106 GLY   B CA   1 
ATOM   4079 C C    . GLY   B 1 126 ? -7.592  27.872 33.935 1.00 16.69 ? 106 GLY   B C    1 
ATOM   4080 O O    . GLY   B 1 126 ? -6.361  27.855 33.944 1.00 17.64 ? 106 GLY   B O    1 
ATOM   4081 H H    . GLY   B 1 126 ? -6.733  26.775 31.882 1.00 20.20 ? 106 GLY   B H    1 
ATOM   4082 H HA2  . GLY   B 1 126 ? -9.194  27.556 32.704 1.00 21.16 ? 106 GLY   B HA2  1 
ATOM   4083 H HA3  . GLY   B 1 126 ? -8.607  26.215 33.299 1.00 21.16 ? 106 GLY   B HA3  1 
ATOM   4084 N N    . GLU   B 1 127 ? -8.314  28.571 34.802 1.00 16.87 ? 107 GLU   B N    1 
ATOM   4085 C CA   . GLU   B 1 127 ? -7.662  29.386 35.811 1.00 17.48 ? 107 GLU   B CA   1 
ATOM   4086 C C    . GLU   B 1 127 ? -8.576  29.613 37.013 1.00 17.63 ? 107 GLU   B C    1 
ATOM   4087 O O    . GLU   B 1 127 ? -9.799  29.739 36.876 1.00 18.08 ? 107 GLU   B O    1 
ATOM   4088 C CB   . GLU   B 1 127 ? -7.289  30.762 35.232 1.00 18.46 ? 107 GLU   B CB   1 
ATOM   4089 C CG   . GLU   B 1 127 ? -8.484  31.487 34.567 1.00 20.75 ? 107 GLU   B CG   1 
ATOM   4090 C CD   . GLU   B 1 127 ? -8.275  32.966 34.427 1.00 24.23 ? 107 GLU   B CD   1 
ATOM   4091 O OE1  . GLU   B 1 127 ? -7.552  33.344 33.492 1.00 24.97 ? 107 GLU   B OE1  1 
ATOM   4092 O OE2  . GLU   B 1 127 ? -8.844  33.747 35.237 1.00 24.79 ? 107 GLU   B OE2  1 
ATOM   4093 H H    . GLU   B 1 127 ? -9.174  28.587 34.825 1.00 20.24 ? 107 GLU   B H    1 
ATOM   4094 H HA   . GLU   B 1 127 ? -6.876  28.907 36.117 1.00 20.97 ? 107 GLU   B HA   1 
ATOM   4095 H HB2  . GLU   B 1 127 ? -6.959  31.325 35.949 1.00 22.16 ? 107 GLU   B HB2  1 
ATOM   4096 H HB3  . GLU   B 1 127 ? -6.600  30.643 34.559 1.00 22.16 ? 107 GLU   B HB3  1 
ATOM   4097 H HG2  . GLU   B 1 127 ? -8.620  31.120 33.679 1.00 24.91 ? 107 GLU   B HG2  1 
ATOM   4098 H HG3  . GLU   B 1 127 ? -9.276  31.348 35.109 1.00 24.91 ? 107 GLU   B HG3  1 
ATOM   4099 N N    . GLY   B 1 128 ? -7.950  29.732 38.178 1.00 17.95 ? 108 GLY   B N    1 
ATOM   4100 C CA   . GLY   B 1 128 ? -8.669  30.101 39.385 1.00 18.15 ? 108 GLY   B CA   1 
ATOM   4101 C C    . GLY   B 1 128 ? -7.804  29.885 40.598 1.00 18.86 ? 108 GLY   B C    1 
ATOM   4102 O O    . GLY   B 1 128 ? -6.701  29.341 40.526 1.00 19.63 ? 108 GLY   B O    1 
ATOM   4103 H H    . GLY   B 1 128 ? -7.108  29.604 38.294 1.00 21.55 ? 108 GLY   B H    1 
ATOM   4104 H HA2  . GLY   B 1 128 ? -8.924  31.036 39.343 1.00 21.78 ? 108 GLY   B HA2  1 
ATOM   4105 H HA3  . GLY   B 1 128 ? -9.469  29.559 39.470 1.00 21.78 ? 108 GLY   B HA3  1 
ATOM   4106 N N    . ALA   B 1 129 ? -8.310  30.367 41.723 1.00 20.44 ? 109 ALA   B N    1 
ATOM   4107 C CA   . ALA   B 1 129 ? -7.659  30.067 42.984 1.00 20.64 ? 109 ALA   B CA   1 
ATOM   4108 C C    . ALA   B 1 129 ? -7.668  28.563 43.232 1.00 20.08 ? 109 ALA   B C    1 
ATOM   4109 O O    . ALA   B 1 129 ? -8.593  27.847 42.861 1.00 21.14 ? 109 ALA   B O    1 
ATOM   4110 C CB   . ALA   B 1 129 ? -8.404  30.770 44.112 1.00 23.55 ? 109 ALA   B CB   1 
ATOM   4111 H H    . ALA   B 1 129 ? -9.013  30.859 41.781 1.00 24.53 ? 109 ALA   B H    1 
ATOM   4112 H HA   . ALA   B 1 129 ? -6.739  30.373 42.967 1.00 24.77 ? 109 ALA   B HA   1 
ATOM   4113 H HB1  . ALA   B 1 129 ? -7.970  30.562 44.954 1.00 28.26 ? 109 ALA   B HB1  1 
ATOM   4114 H HB2  . ALA   B 1 129 ? -8.382  31.727 43.956 1.00 28.26 ? 109 ALA   B HB2  1 
ATOM   4115 H HB3  . ALA   B 1 129 ? -9.322  30.458 44.127 1.00 28.26 ? 109 ALA   B HB3  1 
ATOM   4116 N N    . ILE   B 1 130 ? -6.610  28.069 43.853 1.00 19.97 ? 110 ILE   B N    1 
ATOM   4117 C CA   . ILE   B 1 130 ? -6.568  26.685 44.305 1.00 19.98 ? 110 ILE   B CA   1 
ATOM   4118 C C    . ILE   B 1 130 ? -6.459  26.708 45.821 1.00 20.73 ? 110 ILE   B C    1 
ATOM   4119 O O    . ILE   B 1 130 ? -5.541  27.314 46.385 1.00 21.88 ? 110 ILE   B O    1 
ATOM   4120 C CB   . ILE   B 1 130 ? -5.432  25.888 43.634 1.00 20.33 ? 110 ILE   B CB   1 
ATOM   4121 C CG1  . ILE   B 1 130 ? -5.432  24.430 44.100 1.00 20.74 ? 110 ILE   B CG1  1 
ATOM   4122 C CG2  . ILE   B 1 130 ? -4.043  26.527 43.818 1.00 22.52 ? 110 ILE   B CG2  1 
ATOM   4123 C CD1  . ILE   B 1 130 ? -4.573  23.529 43.243 1.00 21.30 ? 110 ILE   B CD1  1 
ATOM   4124 H H    . ILE   B 1 130 ? -5.898  28.519 44.027 1.00 23.97 ? 110 ILE   B H    1 
ATOM   4125 H HA   . ILE   B 1 130 ? -7.395  26.232 44.077 1.00 23.98 ? 110 ILE   B HA   1 
ATOM   4126 H HB   . ILE   B 1 130 ? -5.618  25.911 42.682 1.00 24.40 ? 110 ILE   B HB   1 
ATOM   4127 H HG12 . ILE   B 1 130 ? -5.092  24.391 45.008 1.00 24.89 ? 110 ILE   B HG12 1 
ATOM   4128 H HG13 . ILE   B 1 130 ? -6.341  24.091 44.072 1.00 24.89 ? 110 ILE   B HG13 1 
ATOM   4129 H HG21 . ILE   B 1 130 ? -3.394  26.025 43.302 1.00 27.02 ? 110 ILE   B HG21 1 
ATOM   4130 H HG22 . ILE   B 1 130 ? -4.074  27.445 43.508 1.00 27.02 ? 110 ILE   B HG22 1 
ATOM   4131 H HG23 . ILE   B 1 130 ? -3.807  26.504 44.759 1.00 27.02 ? 110 ILE   B HG23 1 
ATOM   4132 H HD11 . ILE   B 1 130 ? -4.696  22.610 43.528 1.00 25.57 ? 110 ILE   B HD11 1 
ATOM   4133 H HD12 . ILE   B 1 130 ? -4.841  23.626 42.316 1.00 25.57 ? 110 ILE   B HD12 1 
ATOM   4134 H HD13 . ILE   B 1 130 ? -3.643  23.786 43.347 1.00 25.57 ? 110 ILE   B HD13 1 
ATOM   4135 N N    . VAL   B 1 131 ? -7.406  26.055 46.476 1.00 21.36 ? 111 VAL   B N    1 
ATOM   4136 C CA   . VAL   B 1 131 ? -7.507  26.052 47.926 1.00 22.20 ? 111 VAL   B CA   1 
ATOM   4137 C C    . VAL   B 1 131 ? -7.540  24.602 48.374 1.00 22.88 ? 111 VAL   B C    1 
ATOM   4138 O O    . VAL   B 1 131 ? -8.591  24.082 48.767 1.00 24.96 ? 111 VAL   B O    1 
ATOM   4139 C CB   . VAL   B 1 131 ? -8.780  26.794 48.360 1.00 23.97 ? 111 VAL   B CB   1 
ATOM   4140 C CG1  . VAL   B 1 131 ? -8.769  27.020 49.856 1.00 26.00 ? 111 VAL   B CG1  1 
ATOM   4141 C CG2  . VAL   B 1 131 ? -8.887  28.115 47.644 1.00 25.73 ? 111 VAL   B CG2  1 
ATOM   4142 H H    . VAL   B 1 131 ? -8.021  25.592 46.092 1.00 25.63 ? 111 VAL   B H    1 
ATOM   4143 H HA   . VAL   B 1 131 ? -6.742  26.490 48.331 1.00 26.65 ? 111 VAL   B HA   1 
ATOM   4144 H HB   . VAL   B 1 131 ? -9.552  26.254 48.130 1.00 28.77 ? 111 VAL   B HB   1 
ATOM   4145 H HG11 . VAL   B 1 131 ? -9.565  27.514 50.107 1.00 31.21 ? 111 VAL   B HG11 1 
ATOM   4146 H HG12 . VAL   B 1 131 ? -8.758  26.161 50.305 1.00 31.21 ? 111 VAL   B HG12 1 
ATOM   4147 H HG13 . VAL   B 1 131 ? -7.977  27.527 50.092 1.00 31.21 ? 111 VAL   B HG13 1 
ATOM   4148 H HG21 . VAL   B 1 131 ? -9.555  28.661 48.087 1.00 30.88 ? 111 VAL   B HG21 1 
ATOM   4149 H HG22 . VAL   B 1 131 ? -8.025  28.559 47.670 1.00 30.88 ? 111 VAL   B HG22 1 
ATOM   4150 H HG23 . VAL   B 1 131 ? -9.149  27.955 46.723 1.00 30.88 ? 111 VAL   B HG23 1 
ATOM   4151 N N    . PHE   B 1 132 ? -6.408  23.932 48.284 1.00 22.00 ? 112 PHE   B N    1 
ATOM   4152 C CA   . PHE   B 1 132 ? -6.310  22.513 48.569 1.00 22.36 ? 112 PHE   B CA   1 
ATOM   4153 C C    . PHE   B 1 132 ? -6.050  22.303 50.047 1.00 22.12 ? 112 PHE   B C    1 
ATOM   4154 O O    . PHE   B 1 132 ? -5.268  23.039 50.655 1.00 23.80 ? 112 PHE   B O    1 
ATOM   4155 C CB   . PHE   B 1 132 ? -5.145  21.897 47.797 1.00 25.37 ? 112 PHE   B CB   1 
ATOM   4156 C CG   . PHE   B 1 132 ? -5.547  20.989 46.682 1.00 25.67 ? 112 PHE   B CG   1 
ATOM   4157 C CD1  . PHE   B 1 132 ? -6.559  21.364 45.816 1.00 28.57 ? 112 PHE   B CD1  1 
ATOM   4158 C CD2  . PHE   B 1 132 ? -4.899  19.785 46.458 1.00 32.67 ? 112 PHE   B CD2  1 
ATOM   4159 C CE1  . PHE   B 1 132 ? -6.916  20.584 44.763 1.00 31.79 ? 112 PHE   B CE1  1 
ATOM   4160 C CE2  . PHE   B 1 132 ? -5.287  18.973 45.395 1.00 35.00 ? 112 PHE   B CE2  1 
ATOM   4161 C CZ   . PHE   B 1 132 ? -6.285  19.387 44.548 1.00 34.07 ? 112 PHE   B CZ   1 
ATOM   4162 H H    . PHE   B 1 132 ? -5.658  24.284 48.053 1.00 26.40 ? 112 PHE   B H    1 
ATOM   4163 H HA   . PHE   B 1 132 ? -7.135  22.071 48.316 1.00 26.84 ? 112 PHE   B HA   1 
ATOM   4164 H HB2  . PHE   B 1 132 ? -4.615  22.614 47.414 1.00 30.45 ? 112 PHE   B HB2  1 
ATOM   4165 H HB3  . PHE   B 1 132 ? -4.605  21.379 48.415 1.00 30.45 ? 112 PHE   B HB3  1 
ATOM   4166 H HD1  . PHE   B 1 132 ? -7.005  22.168 45.958 1.00 34.29 ? 112 PHE   B HD1  1 
ATOM   4167 H HD2  . PHE   B 1 132 ? -4.205  19.520 47.017 1.00 39.20 ? 112 PHE   B HD2  1 
ATOM   4168 H HE1  . PHE   B 1 132 ? -7.590  20.864 44.187 1.00 38.15 ? 112 PHE   B HE1  1 
ATOM   4169 H HE2  . PHE   B 1 132 ? -4.871  18.152 45.260 1.00 42.00 ? 112 PHE   B HE2  1 
ATOM   4170 H HZ   . PHE   B 1 132 ? -6.533  18.854 43.827 1.00 40.89 ? 112 PHE   B HZ   1 
ATOM   4171 N N    . PRO   B 1 133 ? -6.667  21.300 50.644 1.00 23.56 ? 113 PRO   B N    1 
ATOM   4172 C CA   . PRO   B 1 133 ? -6.496  21.107 52.085 1.00 24.75 ? 113 PRO   B CA   1 
ATOM   4173 C C    . PRO   B 1 133 ? -5.042  20.871 52.449 1.00 23.66 ? 113 PRO   B C    1 
ATOM   4174 O O    . PRO   B 1 133 ? -4.391  19.977 51.909 1.00 25.14 ? 113 PRO   B O    1 
ATOM   4175 C CB   . PRO   B 1 133 ? -7.347  19.870 52.386 1.00 25.92 ? 113 PRO   B CB   1 
ATOM   4176 C CG   . PRO   B 1 133 ? -8.368  19.871 51.283 1.00 27.72 ? 113 PRO   B CG   1 
ATOM   4177 C CD   . PRO   B 1 133 ? -7.699  20.429 50.073 1.00 26.85 ? 113 PRO   B CD   1 
ATOM   4178 H HA   . PRO   B 1 133 ? -6.837  21.876 52.569 1.00 29.70 ? 113 PRO   B HA   1 
ATOM   4179 H HB2  . PRO   B 1 133 ? -6.800  19.070 52.359 1.00 31.11 ? 113 PRO   B HB2  1 
ATOM   4180 H HB3  . PRO   B 1 133 ? -7.768  19.955 53.256 1.00 31.11 ? 113 PRO   B HB3  1 
ATOM   4181 H HG2  . PRO   B 1 133 ? -8.666  18.963 51.118 1.00 33.27 ? 113 PRO   B HG2  1 
ATOM   4182 H HG3  . PRO   B 1 133 ? -9.121  20.426 51.540 1.00 33.27 ? 113 PRO   B HG3  1 
ATOM   4183 H HD2  . PRO   B 1 133 ? -7.302  19.723 49.540 1.00 32.22 ? 113 PRO   B HD2  1 
ATOM   4184 H HD3  . PRO   B 1 133 ? -8.325  20.939 49.535 1.00 32.22 ? 113 PRO   B HD3  1 
ATOM   4185 N N    . GLY   B 1 134 ? -4.550  21.662 53.393 1.00 25.31 ? 114 GLY   B N    1 
ATOM   4186 C CA   . GLY   B 1 134 ? -3.200  21.504 53.885 1.00 26.98 ? 114 GLY   B CA   1 
ATOM   4187 C C    . GLY   B 1 134 ? -2.115  22.106 53.025 1.00 26.55 ? 114 GLY   B C    1 
ATOM   4188 O O    . GLY   B 1 134 ? -0.927  21.859 53.287 1.00 28.35 ? 114 GLY   B O    1 
ATOM   4189 H H    . GLY   B 1 134 ? -4.986  22.303 53.765 1.00 30.37 ? 114 GLY   B H    1 
ATOM   4190 H HA2  . GLY   B 1 134 ? -3.142  21.918 54.761 1.00 32.38 ? 114 GLY   B HA2  1 
ATOM   4191 H HA3  . GLY   B 1 134 ? -3.013  20.556 53.971 1.00 32.38 ? 114 GLY   B HA3  1 
ATOM   4192 N N    . TYR   B 1 135 ? -2.480  22.899 52.025 1.00 24.13 ? 115 TYR   B N    1 
ATOM   4193 C CA   . TYR   B 1 135 ? -1.522  23.601 51.187 1.00 23.91 ? 115 TYR   B CA   1 
ATOM   4194 C C    . TYR   B 1 135 ? -1.817  25.088 51.257 1.00 24.27 ? 115 TYR   B C    1 
ATOM   4195 O O    . TYR   B 1 135 ? -2.961  25.478 51.500 1.00 25.84 ? 115 TYR   B O    1 
ATOM   4196 C CB   . TYR   B 1 135 ? -1.606  23.165 49.729 1.00 23.02 ? 115 TYR   B CB   1 
ATOM   4197 C CG   . TYR   B 1 135 ? -1.029  21.793 49.489 1.00 21.78 ? 115 TYR   B CG   1 
ATOM   4198 C CD1  . TYR   B 1 135 ? 0.319   21.619 49.182 1.00 22.09 ? 115 TYR   B CD1  1 
ATOM   4199 C CD2  . TYR   B 1 135 ? -1.821  20.674 49.611 1.00 21.86 ? 115 TYR   B CD2  1 
ATOM   4200 C CE1  . TYR   B 1 135 ? 0.850   20.372 48.985 1.00 22.11 ? 115 TYR   B CE1  1 
ATOM   4201 C CE2  . TYR   B 1 135 ? -1.322  19.423 49.348 1.00 22.17 ? 115 TYR   B CE2  1 
ATOM   4202 C CZ   . TYR   B 1 135 ? 0.024   19.268 49.078 1.00 22.39 ? 115 TYR   B CZ   1 
ATOM   4203 O OH   . TYR   B 1 135 ? 0.488   17.994 48.861 1.00 24.03 ? 115 TYR   B OH   1 
ATOM   4204 H H    . TYR   B 1 135 ? -3.299  23.050 51.809 1.00 28.95 ? 115 TYR   B H    1 
ATOM   4205 H HA   . TYR   B 1 135 ? -0.622  23.415 51.497 1.00 28.70 ? 115 TYR   B HA   1 
ATOM   4206 H HB2  . TYR   B 1 135 ? -2.538  23.148 49.458 1.00 27.63 ? 115 TYR   B HB2  1 
ATOM   4207 H HB3  . TYR   B 1 135 ? -1.113  23.796 49.182 1.00 27.63 ? 115 TYR   B HB3  1 
ATOM   4208 H HD1  . TYR   B 1 135 ? 0.870   22.365 49.109 1.00 26.51 ? 115 TYR   B HD1  1 
ATOM   4209 H HD2  . TYR   B 1 135 ? -2.708  20.767 49.875 1.00 26.23 ? 115 TYR   B HD2  1 
ATOM   4210 H HE1  . TYR   B 1 135 ? 1.754   20.269 48.791 1.00 26.53 ? 115 TYR   B HE1  1 
ATOM   4211 H HE2  . TYR   B 1 135 ? -1.886  18.683 49.351 1.00 26.60 ? 115 TYR   B HE2  1 
ATOM   4212 H HH   . TYR   B 1 135 ? 1.308   18.015 48.678 1.00 28.84 ? 115 TYR   B HH   1 
ATOM   4213 N N    . PRO   B 1 136 ? -0.827  25.943 51.017 1.00 24.01 ? 116 PRO   B N    1 
ATOM   4214 C CA   . PRO   B 1 136 ? -1.116  27.379 50.969 1.00 24.45 ? 116 PRO   B CA   1 
ATOM   4215 C C    . PRO   B 1 136 ? -2.060  27.679 49.814 1.00 23.66 ? 116 PRO   B C    1 
ATOM   4216 O O    . PRO   B 1 136 ? -1.998  27.054 48.756 1.00 23.57 ? 116 PRO   B O    1 
ATOM   4217 C CB   . PRO   B 1 136 ? 0.258   28.019 50.760 1.00 26.32 ? 116 PRO   B CB   1 
ATOM   4218 C CG   . PRO   B 1 136 ? 1.230   26.986 51.207 1.00 28.73 ? 116 PRO   B CG   1 
ATOM   4219 C CD   . PRO   B 1 136 ? 0.608   25.668 50.841 1.00 25.72 ? 116 PRO   B CD   1 
ATOM   4220 H HA   . PRO   B 1 136 ? -1.488  27.698 51.806 1.00 29.34 ? 116 PRO   B HA   1 
ATOM   4221 H HB2  . PRO   B 1 136 ? 0.385   28.233 49.823 1.00 31.59 ? 116 PRO   B HB2  1 
ATOM   4222 H HB3  . PRO   B 1 136 ? 0.334   28.823 51.297 1.00 31.59 ? 116 PRO   B HB3  1 
ATOM   4223 H HG2  . PRO   B 1 136 ? 2.075   27.109 50.747 1.00 34.48 ? 116 PRO   B HG2  1 
ATOM   4224 H HG3  . PRO   B 1 136 ? 1.361   27.051 52.166 1.00 34.48 ? 116 PRO   B HG3  1 
ATOM   4225 H HD2  . PRO   B 1 136 ? 0.809   25.430 49.922 1.00 30.87 ? 116 PRO   B HD2  1 
ATOM   4226 H HD3  . PRO   B 1 136 ? 0.905   24.963 51.438 1.00 30.87 ? 116 PRO   B HD3  1 
ATOM   4227 N N    . ARG   B 1 137 ? -2.954  28.628 50.026 1.00 25.65 ? 117 ARG   B N    1 
ATOM   4228 C CA   . ARG   B 1 137 ? -3.783  29.104 48.929 1.00 26.63 ? 117 ARG   B CA   1 
ATOM   4229 C C    . ARG   B 1 137 ? -2.888  29.606 47.801 1.00 26.63 ? 117 ARG   B C    1 
ATOM   4230 O O    . ARG   B 1 137 ? -1.876  30.261 48.038 1.00 28.18 ? 117 ARG   B O    1 
ATOM   4231 C CB   . ARG   B 1 137 ? -4.682  30.237 49.418 1.00 31.24 ? 117 ARG   B CB   1 
ATOM   4232 C CG   . ARG   B 1 137 ? -5.728  30.644 48.391 1.00 36.24 ? 117 ARG   B CG   1 
ATOM   4233 C CD   . ARG   B 1 137 ? -6.442  31.943 48.766 0.71 40.16 ? 117 ARG   B CD   1 
ATOM   4234 N NE   . ARG   B 1 137 ? -7.620  32.168 47.937 0.83 43.58 ? 117 ARG   B NE   1 
ATOM   4235 C CZ   . ARG   B 1 137 ? -8.854  31.815 48.277 1.00 45.25 ? 117 ARG   B CZ   1 
ATOM   4236 N NH1  . ARG   B 1 137 ? -9.117  31.253 49.451 1.00 47.29 ? 117 ARG   B NH1  1 
ATOM   4237 N NH2  . ARG   B 1 137 ? -9.847  32.038 47.421 0.72 44.41 ? 117 ARG   B NH2  1 
ATOM   4238 H H    . ARG   B 1 137 ? -3.101  29.009 50.782 1.00 30.78 ? 117 ARG   B H    1 
ATOM   4239 H HA   . ARG   B 1 137 ? -4.346  28.387 48.595 1.00 31.95 ? 117 ARG   B HA   1 
ATOM   4240 H HB2  . ARG   B 1 137 ? -5.145  29.949 50.220 1.00 37.49 ? 117 ARG   B HB2  1 
ATOM   4241 H HB3  . ARG   B 1 137 ? -4.134  31.014 49.612 1.00 37.49 ? 117 ARG   B HB3  1 
ATOM   4242 H HG2  . ARG   B 1 137 ? -5.296  30.776 47.533 1.00 43.49 ? 117 ARG   B HG2  1 
ATOM   4243 H HG3  . ARG   B 1 137 ? -6.396  29.944 48.322 1.00 43.49 ? 117 ARG   B HG3  1 
ATOM   4244 H HD2  . ARG   B 1 137 ? -6.726  31.896 49.692 0.71 48.19 ? 117 ARG   B HD2  1 
ATOM   4245 H HD3  . ARG   B 1 137 ? -5.836  32.689 48.642 0.71 48.19 ? 117 ARG   B HD3  1 
ATOM   4246 H HE   . ARG   B 1 137 ? -7.508  32.554 47.177 0.83 52.30 ? 117 ARG   B HE   1 
ATOM   4247 H HH11 . ARG   B 1 137 ? -8.481  31.110 50.012 1.00 56.75 ? 117 ARG   B HH11 1 
ATOM   4248 H HH12 . ARG   B 1 137 ? -9.924  31.033 49.650 1.00 56.75 ? 117 ARG   B HH12 1 
ATOM   4249 H HH21 . ARG   B 1 137 ? -9.686  32.405 46.660 0.72 53.30 ? 117 ARG   B HH21 1 
ATOM   4250 H HH22 . ARG   B 1 137 ? -10.652 31.814 47.628 0.72 53.30 ? 117 ARG   B HH22 1 
ATOM   4251 N N    . GLY   B 1 138 ? -3.266  29.292 46.568 1.00 26.11 ? 118 GLY   B N    1 
ATOM   4252 C CA   . GLY   B 1 138 ? -2.481  29.676 45.416 1.00 26.66 ? 118 GLY   B CA   1 
ATOM   4253 C C    . GLY   B 1 138 ? -3.384  30.064 44.264 1.00 23.03 ? 118 GLY   B C    1 
ATOM   4254 O O    . GLY   B 1 138 ? -4.608  30.103 44.382 1.00 24.24 ? 118 GLY   B O    1 
ATOM   4255 H H    . GLY   B 1 138 ? -3.980  28.853 46.376 1.00 31.33 ? 118 GLY   B H    1 
ATOM   4256 H HA2  . GLY   B 1 138 ? -1.918  30.433 45.640 1.00 32.00 ? 118 GLY   B HA2  1 
ATOM   4257 H HA3  . GLY   B 1 138 ? -1.920  28.935 45.139 1.00 32.00 ? 118 GLY   B HA3  1 
ATOM   4258 N N    A GLN   B 1 139 ? -2.750  30.377 43.151 0.66 21.39 ? 119 GLN   B N    1 
ATOM   4259 N N    B GLN   B 1 139 ? -2.744  30.335 43.133 0.34 23.54 ? 119 GLN   B N    1 
ATOM   4260 C CA   A GLN   B 1 139 ? -3.446  30.633 41.905 0.66 20.25 ? 119 GLN   B CA   1 
ATOM   4261 C CA   B GLN   B 1 139 ? -3.430  30.659 41.891 0.34 24.25 ? 119 GLN   B CA   1 
ATOM   4262 C C    A GLN   B 1 139 ? -2.968  29.565 40.945 0.66 21.29 ? 119 GLN   B C    1 
ATOM   4263 C C    B GLN   B 1 139 ? -2.959  29.673 40.836 0.34 23.29 ? 119 GLN   B C    1 
ATOM   4264 O O    A GLN   B 1 139 ? -1.770  29.320 40.839 0.66 25.23 ? 119 GLN   B O    1 
ATOM   4265 O O    B GLN   B 1 139 ? -1.765  29.614 40.526 0.34 25.45 ? 119 GLN   B O    1 
ATOM   4266 C CB   A GLN   B 1 139 ? -3.130  32.021 41.361 0.66 24.13 ? 119 GLN   B CB   1 
ATOM   4267 C CB   B GLN   B 1 139 ? -3.121  32.090 41.454 0.34 27.36 ? 119 GLN   B CB   1 
ATOM   4268 C CG   A GLN   B 1 139 ? -3.983  32.413 40.155 0.66 27.63 ? 119 GLN   B CG   1 
ATOM   4269 C CG   B GLN   B 1 139 ? -3.578  33.155 42.443 0.34 29.61 ? 119 GLN   B CG   1 
ATOM   4270 C CD   A GLN   B 1 139 ? -5.466  32.659 40.522 0.66 31.20 ? 119 GLN   B CD   1 
ATOM   4271 C CD   B GLN   B 1 139 ? -5.069  33.098 42.728 0.34 34.78 ? 119 GLN   B CD   1 
ATOM   4272 O OE1  A GLN   B 1 139 ? -5.827  32.680 41.703 0.66 34.67 ? 119 GLN   B OE1  1 
ATOM   4273 O OE1  B GLN   B 1 139 ? -5.494  33.258 43.873 0.34 36.93 ? 119 GLN   B OE1  1 
ATOM   4274 N NE2  A GLN   B 1 139 ? -6.320  32.830 39.519 0.66 31.22 ? 119 GLN   B NE2  1 
ATOM   4275 N NE2  B GLN   B 1 139 ? -5.870  32.869 41.687 0.34 37.15 ? 119 GLN   B NE2  1 
ATOM   4276 H H    A GLN   B 1 139 ? -1.896  30.450 43.091 0.66 25.67 ? 119 GLN   B H    1 
ATOM   4277 H H    B GLN   B 1 139 ? -1.887  30.338 43.060 0.34 28.25 ? 119 GLN   B H    1 
ATOM   4278 H HA   A GLN   B 1 139 ? -4.409  30.591 42.017 0.66 24.30 ? 119 GLN   B HA   1 
ATOM   4279 H HA   B GLN   B 1 139 ? -4.389  30.576 42.005 0.34 29.10 ? 119 GLN   B HA   1 
ATOM   4280 H HB2  A GLN   B 1 139 ? -3.287  32.674 42.060 0.66 28.96 ? 119 GLN   B HB2  1 
ATOM   4281 H HB2  B GLN   B 1 139 ? -2.161  32.182 41.346 0.34 32.83 ? 119 GLN   B HB2  1 
ATOM   4282 H HB3  A GLN   B 1 139 ? -2.200  32.045 41.087 0.66 28.96 ? 119 GLN   B HB3  1 
ATOM   4283 H HB3  B GLN   B 1 139 ? -3.568  32.260 40.610 0.34 32.83 ? 119 GLN   B HB3  1 
ATOM   4284 H HG2  A GLN   B 1 139 ? -3.629  33.230 39.771 0.66 33.15 ? 119 GLN   B HG2  1 
ATOM   4285 H HG2  B GLN   B 1 139 ? -3.108  33.028 43.282 0.34 35.53 ? 119 GLN   B HG2  1 
ATOM   4286 H HG3  A GLN   B 1 139 ? -3.951  31.698 39.500 0.66 33.15 ? 119 GLN   B HG3  1 
ATOM   4287 H HG3  B GLN   B 1 139 ? -3.376  34.031 42.078 0.34 35.53 ? 119 GLN   B HG3  1 
ATOM   4288 H HE21 A GLN   B 1 139 ? -6.039  32.800 38.707 0.66 37.46 ? 119 GLN   B HE21 1 
ATOM   4289 H HE21 B GLN   B 1 139 ? -5.536  32.761 40.902 0.34 44.58 ? 119 GLN   B HE21 1 
ATOM   4290 H HE22 A GLN   B 1 139 ? -7.152  32.969 39.682 0.66 37.46 ? 119 GLN   B HE22 1 
ATOM   4291 H HE22 B GLN   B 1 139 ? -6.722  32.828 41.801 0.34 44.58 ? 119 GLN   B HE22 1 
ATOM   4292 N N    . TYR   B 1 140 ? -3.895  28.925 40.270 1.00 20.18 ? 120 TYR   B N    1 
ATOM   4293 C CA   . TYR   B 1 140 ? -3.602  27.836 39.348 1.00 18.83 ? 120 TYR   B CA   1 
ATOM   4294 C C    . TYR   B 1 140 ? -4.037  28.238 37.950 1.00 18.94 ? 120 TYR   B C    1 
ATOM   4295 O O    . TYR   B 1 140 ? -5.172  28.671 37.742 1.00 20.21 ? 120 TYR   B O    1 
ATOM   4296 C CB   . TYR   B 1 140 ? -4.331  26.576 39.842 1.00 19.96 ? 120 TYR   B CB   1 
ATOM   4297 C CG   . TYR   B 1 140 ? -4.211  25.350 38.991 1.00 18.90 ? 120 TYR   B CG   1 
ATOM   4298 C CD1  . TYR   B 1 140 ? -3.034  25.037 38.316 1.00 18.00 ? 120 TYR   B CD1  1 
ATOM   4299 C CD2  . TYR   B 1 140 ? -5.272  24.477 38.871 1.00 19.12 ? 120 TYR   B CD2  1 
ATOM   4300 C CE1  . TYR   B 1 140 ? -2.925  23.889 37.549 1.00 18.01 ? 120 TYR   B CE1  1 
ATOM   4301 C CE2  . TYR   B 1 140 ? -5.182  23.332 38.100 1.00 19.57 ? 120 TYR   B CE2  1 
ATOM   4302 C CZ   . TYR   B 1 140 ? -4.013  23.053 37.436 1.00 18.61 ? 120 TYR   B CZ   1 
ATOM   4303 O OH   . TYR   B 1 140 ? -3.924  21.928 36.669 1.00 19.75 ? 120 TYR   B OH   1 
ATOM   4304 H H    A TYR   B 1 140 ? -4.734  29.104 40.326 0.66 24.22 ? 120 TYR   B H    1 
ATOM   4305 H H    B TYR   B 1 140 ? -4.737  29.032 40.408 0.34 24.22 ? 120 TYR   B H    1 
ATOM   4306 H HA   . TYR   B 1 140 ? -2.652  27.647 39.294 1.00 22.60 ? 120 TYR   B HA   1 
ATOM   4307 H HB2  . TYR   B 1 140 ? -3.978  26.349 40.717 1.00 23.95 ? 120 TYR   B HB2  1 
ATOM   4308 H HB3  . TYR   B 1 140 ? -5.276  26.783 39.909 1.00 23.95 ? 120 TYR   B HB3  1 
ATOM   4309 H HD1  . TYR   B 1 140 ? -2.305  25.611 38.381 1.00 21.60 ? 120 TYR   B HD1  1 
ATOM   4310 H HD2  . TYR   B 1 140 ? -6.066  24.663 39.318 1.00 22.94 ? 120 TYR   B HD2  1 
ATOM   4311 H HE1  . TYR   B 1 140 ? -2.128  23.685 37.116 1.00 21.62 ? 120 TYR   B HE1  1 
ATOM   4312 H HE2  . TYR   B 1 140 ? -5.908  22.754 38.033 1.00 23.48 ? 120 TYR   B HE2  1 
ATOM   4313 H HH   . TYR   B 1 140 ? -4.643  21.496 36.706 1.00 23.70 ? 120 TYR   B HH   1 
ATOM   4314 N N    . ARG   B 1 141 ? -3.140  28.070 36.998 1.00 17.90 ? 121 ARG   B N    1 
ATOM   4315 C CA   . ARG   B 1 141 ? -3.422  28.248 35.588 1.00 18.15 ? 121 ARG   B CA   1 
ATOM   4316 C C    . ARG   B 1 141 ? -2.871  27.042 34.842 1.00 17.89 ? 121 ARG   B C    1 
ATOM   4317 O O    . ARG   B 1 141 ? -1.768  26.584 35.144 1.00 19.69 ? 121 ARG   B O    1 
ATOM   4318 C CB   . ARG   B 1 141 ? -2.671  29.491 35.059 1.00 19.45 ? 121 ARG   B CB   1 
ATOM   4319 C CG   . ARG   B 1 141 ? -3.125  30.809 35.664 1.00 20.47 ? 121 ARG   B CG   1 
ATOM   4320 C CD   . ARG   B 1 141 ? -2.301  32.018 35.128 1.00 23.05 ? 121 ARG   B CD   1 
ATOM   4321 N NE   . ARG   B 1 141 ? -2.360  32.161 33.672 1.00 24.59 ? 121 ARG   B NE   1 
ATOM   4322 C CZ   . ARG   B 1 141 ? -3.402  32.658 33.010 1.00 24.91 ? 121 ARG   B CZ   1 
ATOM   4323 N NH1  . ARG   B 1 141 ? -4.469  33.133 33.641 1.00 25.38 ? 121 ARG   B NH1  1 
ATOM   4324 N NH2  . ARG   B 1 141 ? -3.384  32.666 31.680 1.00 28.22 ? 121 ARG   B NH2  1 
ATOM   4325 H H    . ARG   B 1 141 ? -2.325  27.842 37.150 1.00 21.48 ? 121 ARG   B H    1 
ATOM   4326 H HA   . ARG   B 1 141 ? -4.377  28.336 35.440 1.00 21.78 ? 121 ARG   B HA   1 
ATOM   4327 H HB2  . ARG   B 1 141 ? -1.727  29.389 35.257 1.00 23.34 ? 121 ARG   B HB2  1 
ATOM   4328 H HB3  . ARG   B 1 141 ? -2.805  29.548 34.100 1.00 23.34 ? 121 ARG   B HB3  1 
ATOM   4329 H HG2  . ARG   B 1 141 ? -4.057  30.957 35.442 1.00 24.56 ? 121 ARG   B HG2  1 
ATOM   4330 H HG3  . ARG   B 1 141 ? -3.015  30.773 36.627 1.00 24.56 ? 121 ARG   B HG3  1 
ATOM   4331 H HD2  . ARG   B 1 141 ? -2.649  32.834 35.521 1.00 27.66 ? 121 ARG   B HD2  1 
ATOM   4332 H HD3  . ARG   B 1 141 ? -1.371  31.900 35.378 1.00 27.66 ? 121 ARG   B HD3  1 
ATOM   4333 H HE   . ARG   B 1 141 ? -1.677  31.907 33.216 1.00 29.52 ? 121 ARG   B HE   1 
ATOM   4334 H HH11 . ARG   B 1 141 ? -4.499  33.125 34.500 1.00 30.45 ? 121 ARG   B HH11 1 
ATOM   4335 H HH12 . ARG   B 1 141 ? -5.130  33.449 33.190 1.00 30.45 ? 121 ARG   B HH12 1 
ATOM   4336 H HH21 . ARG   B 1 141 ? -2.704  32.352 31.257 1.00 33.86 ? 121 ARG   B HH21 1 
ATOM   4337 H HH22 . ARG   B 1 141 ? -4.052  32.985 31.243 1.00 33.86 ? 121 ARG   B HH22 1 
ATOM   4338 N N    . ASN   B 1 142 ? -3.612  26.545 33.862 1.00 17.04 ? 122 ASN   B N    1 
ATOM   4339 C CA   . ASN   B 1 142 ? -3.071  25.439 33.088 1.00 16.20 ? 122 ASN   B CA   1 
ATOM   4340 C C    . ASN   B 1 142 ? -3.763  25.365 31.741 1.00 16.21 ? 122 ASN   B C    1 
ATOM   4341 O O    . ASN   B 1 142 ? -4.824  25.950 31.523 1.00 17.48 ? 122 ASN   B O    1 
ATOM   4342 C CB   . ASN   B 1 142 ? -3.220  24.114 33.853 1.00 17.31 ? 122 ASN   B CB   1 
ATOM   4343 C CG   . ASN   B 1 142 ? -2.082  23.152 33.598 1.00 18.78 ? 122 ASN   B CG   1 
ATOM   4344 O OD1  . ASN   B 1 142 ? -1.251  23.359 32.712 1.00 19.93 ? 122 ASN   B OD1  1 
ATOM   4345 N ND2  . ASN   B 1 142 ? -2.011  22.106 34.407 1.00 18.45 ? 122 ASN   B ND2  1 
ATOM   4346 H H    . ASN   B 1 142 ? -4.395  26.819 33.636 1.00 20.45 ? 122 ASN   B H    1 
ATOM   4347 H HA   . ASN   B 1 142 ? -2.130  25.600 32.916 1.00 19.44 ? 122 ASN   B HA   1 
ATOM   4348 H HB2  . ASN   B 1 142 ? -3.245  24.302 34.805 1.00 20.77 ? 122 ASN   B HB2  1 
ATOM   4349 H HB3  . ASN   B 1 142 ? -4.044  23.683 33.578 1.00 20.77 ? 122 ASN   B HB3  1 
ATOM   4350 H HD21 . ASN   B 1 142 ? -1.384  21.527 34.307 1.00 22.14 ? 122 ASN   B HD21 1 
ATOM   4351 H HD22 . ASN   B 1 142 ? -2.593  22.006 35.033 1.00 22.14 ? 122 ASN   B HD22 1 
ATOM   4352 N N    . HIS   B 1 143 ? -3.142  24.616 30.845 1.00 16.64 ? 123 HIS   B N    1 
ATOM   4353 C CA   . HIS   B 1 143 ? -3.707  24.240 29.557 1.00 16.32 ? 123 HIS   B CA   1 
ATOM   4354 C C    . HIS   B 1 143 ? -4.396  22.882 29.722 1.00 15.48 ? 123 HIS   B C    1 
ATOM   4355 O O    . HIS   B 1 143 ? -3.911  22.000 30.434 1.00 17.00 ? 123 HIS   B O    1 
ATOM   4356 C CB   . HIS   B 1 143 ? -2.562  24.150 28.536 1.00 16.65 ? 123 HIS   B CB   1 
ATOM   4357 C CG   . HIS   B 1 143 ? -3.004  23.704 27.183 1.00 17.27 ? 123 HIS   B CG   1 
ATOM   4358 N ND1  . HIS   B 1 143 ? -3.022  22.377 26.813 1.00 18.88 ? 123 HIS   B ND1  1 
ATOM   4359 C CD2  . HIS   B 1 143 ? -3.401  24.407 26.097 1.00 19.41 ? 123 HIS   B CD2  1 
ATOM   4360 C CE1  . HIS   B 1 143 ? -3.457  22.281 25.570 1.00 19.74 ? 123 HIS   B CE1  1 
ATOM   4361 N NE2  . HIS   B 1 143 ? -3.656  23.501 25.102 1.00 19.24 ? 123 HIS   B NE2  1 
ATOM   4362 H H    . HIS   B 1 143 ? -2.353  24.295 30.964 1.00 19.97 ? 123 HIS   B H    1 
ATOM   4363 H HA   . HIS   B 1 143 ? -4.359  24.881 29.234 1.00 19.59 ? 123 HIS   B HA   1 
ATOM   4364 H HB2  . HIS   B 1 143 ? -2.156  25.027 28.443 1.00 19.98 ? 123 HIS   B HB2  1 
ATOM   4365 H HB3  . HIS   B 1 143 ? -1.904  23.514 28.859 1.00 19.98 ? 123 HIS   B HB3  1 
ATOM   4366 H HD2  . HIS   B 1 143 ? -3.484  25.331 26.037 1.00 23.29 ? 123 HIS   B HD2  1 
ATOM   4367 H HE1  . HIS   B 1 143 ? -3.599  21.489 25.104 1.00 23.69 ? 123 HIS   B HE1  1 
ATOM   4368 H HE2  . HIS   B 1 143 ? -3.905  23.694 24.301 1.00 23.09 ? 123 HIS   B HE2  1 
ATOM   4369 N N    . PHE   B 1 144 ? -5.543  22.712 29.059 1.00 15.17 ? 124 PHE   B N    1 
ATOM   4370 C CA   . PHE   B 1 144 ? -6.285  21.464 29.170 1.00 15.48 ? 124 PHE   B CA   1 
ATOM   4371 C C    . PHE   B 1 144 ? -6.786  20.964 27.825 1.00 15.31 ? 124 PHE   B C    1 
ATOM   4372 O O    . PHE   B 1 144 ? -7.083  21.743 26.910 1.00 16.52 ? 124 PHE   B O    1 
ATOM   4373 C CB   . PHE   B 1 144 ? -7.557  21.643 30.038 1.00 16.28 ? 124 PHE   B CB   1 
ATOM   4374 C CG   . PHE   B 1 144 ? -7.276  21.965 31.479 1.00 16.33 ? 124 PHE   B CG   1 
ATOM   4375 C CD1  . PHE   B 1 144 ? -6.948  23.255 31.895 1.00 18.05 ? 124 PHE   B CD1  1 
ATOM   4376 C CD2  . PHE   B 1 144 ? -7.381  20.969 32.424 1.00 17.78 ? 124 PHE   B CD2  1 
ATOM   4377 C CE1  . PHE   B 1 144 ? -6.675  23.538 33.235 1.00 19.00 ? 124 PHE   B CE1  1 
ATOM   4378 C CE2  . PHE   B 1 144 ? -7.117  21.229 33.751 1.00 18.62 ? 124 PHE   B CE2  1 
ATOM   4379 C CZ   . PHE   B 1 144 ? -6.781  22.517 34.162 1.00 18.66 ? 124 PHE   B CZ   1 
ATOM   4380 H H    . PHE   B 1 144 ? -5.903  23.301 28.546 1.00 18.21 ? 124 PHE   B H    1 
ATOM   4381 H HA   . PHE   B 1 144 ? -5.667  20.815 29.540 1.00 18.58 ? 124 PHE   B HA   1 
ATOM   4382 H HB2  . PHE   B 1 144 ? -8.084  22.370 29.671 1.00 19.54 ? 124 PHE   B HB2  1 
ATOM   4383 H HB3  . PHE   B 1 144 ? -8.068  20.819 30.014 1.00 19.54 ? 124 PHE   B HB3  1 
ATOM   4384 H HD1  . PHE   B 1 144 ? -6.911  23.941 31.267 1.00 21.66 ? 124 PHE   B HD1  1 
ATOM   4385 H HD2  . PHE   B 1 144 ? -7.632  20.112 32.164 1.00 21.34 ? 124 PHE   B HD2  1 
ATOM   4386 H HE1  . PHE   B 1 144 ? -6.428  24.394 33.499 1.00 22.80 ? 124 PHE   B HE1  1 
ATOM   4387 H HE2  . PHE   B 1 144 ? -7.162  20.541 34.375 1.00 22.35 ? 124 PHE   B HE2  1 
ATOM   4388 H HZ   . PHE   B 1 144 ? -6.627  22.690 35.063 1.00 22.39 ? 124 PHE   B HZ   1 
ATOM   4389 N N    . LEU   B 1 145 ? -6.897  19.643 27.735 1.00 14.58 ? 125 LEU   B N    1 
ATOM   4390 C CA   . LEU   B 1 145 ? -7.685  18.989 26.695 1.00 15.10 ? 125 LEU   B CA   1 
ATOM   4391 C C    . LEU   B 1 145 ? -8.782  18.214 27.390 1.00 15.04 ? 125 LEU   B C    1 
ATOM   4392 O O    . LEU   B 1 145 ? -8.543  17.569 28.404 1.00 16.53 ? 125 LEU   B O    1 
ATOM   4393 C CB   . LEU   B 1 145 ? -6.784  18.045 25.872 1.00 16.38 ? 125 LEU   B CB   1 
ATOM   4394 C CG   . LEU   B 1 145 ? -5.588  18.767 25.224 1.00 19.03 ? 125 LEU   B CG   1 
ATOM   4395 C CD1  . LEU   B 1 145 ? -4.603  17.784 24.643 1.00 20.54 ? 125 LEU   B CD1  1 
ATOM   4396 C CD2  . LEU   B 1 145 ? -6.005  19.725 24.218 1.00 21.42 ? 125 LEU   B CD2  1 
ATOM   4397 H H    . LEU   B 1 145 ? -6.516  19.093 28.275 1.00 17.50 ? 125 LEU   B H    1 
ATOM   4398 H HA   . LEU   B 1 145 ? -8.085  19.625 26.082 1.00 18.12 ? 125 LEU   B HA   1 
ATOM   4399 H HB2  . LEU   B 1 145 ? -6.436  17.353 26.457 1.00 19.66 ? 125 LEU   B HB2  1 
ATOM   4400 H HB3  . LEU   B 1 145 ? -7.313  17.645 25.164 1.00 19.66 ? 125 LEU   B HB3  1 
ATOM   4401 H HG   . LEU   B 1 145 ? -5.139  19.265 25.925 1.00 22.84 ? 125 LEU   B HG   1 
ATOM   4402 H HD11 . LEU   B 1 145 ? -3.871  18.273 24.238 1.00 24.65 ? 125 LEU   B HD11 1 
ATOM   4403 H HD12 . LEU   B 1 145 ? -4.268  17.215 25.354 1.00 24.65 ? 125 LEU   B HD12 1 
ATOM   4404 H HD13 . LEU   B 1 145 ? -5.053  17.245 23.973 1.00 24.65 ? 125 LEU   B HD13 1 
ATOM   4405 H HD21 . LEU   B 1 145 ? -5.220  20.068 23.763 1.00 25.71 ? 125 LEU   B HD21 1 
ATOM   4406 H HD22 . LEU   B 1 145 ? -6.589  19.282 23.583 1.00 25.71 ? 125 LEU   B HD22 1 
ATOM   4407 H HD23 . LEU   B 1 145 ? -6.479  20.452 24.652 1.00 25.71 ? 125 LEU   B HD23 1 
ATOM   4408 N N    . HIS   B 1 146 ? -9.983  18.252 26.817 1.00 15.30 ? 126 HIS   B N    1 
ATOM   4409 C CA   . HIS   B 1 146 ? -11.091 17.471 27.315 1.00 15.89 ? 126 HIS   B CA   1 
ATOM   4410 C C    . HIS   B 1 146 ? -11.614 16.563 26.215 1.00 15.47 ? 126 HIS   B C    1 
ATOM   4411 O O    . HIS   B 1 146 ? -11.678 16.959 25.055 1.00 16.51 ? 126 HIS   B O    1 
ATOM   4412 C CB   . HIS   B 1 146 ? -12.280 18.347 27.730 1.00 16.38 ? 126 HIS   B CB   1 
ATOM   4413 C CG   . HIS   B 1 146 ? -12.049 19.201 28.930 1.00 17.93 ? 126 HIS   B CG   1 
ATOM   4414 N ND1  . HIS   B 1 146 ? -12.660 18.932 30.129 1.00 19.99 ? 126 HIS   B ND1  1 
ATOM   4415 C CD2  . HIS   B 1 146 ? -11.372 20.360 29.102 1.00 18.73 ? 126 HIS   B CD2  1 
ATOM   4416 C CE1  . HIS   B 1 146 ? -12.348 19.874 31.003 1.00 19.54 ? 126 HIS   B CE1  1 
ATOM   4417 N NE2  . HIS   B 1 146 ? -11.569 20.756 30.403 1.00 19.00 ? 126 HIS   B NE2  1 
ATOM   4418 H H    . HIS   B 1 146 ? -10.174 18.732 26.130 1.00 18.36 ? 126 HIS   B H    1 
ATOM   4419 H HA   . HIS   B 1 146 ? -10.768 16.960 28.073 1.00 19.07 ? 126 HIS   B HA   1 
ATOM   4420 H HB2  . HIS   B 1 146 ? -12.499 18.937 26.992 1.00 19.66 ? 126 HIS   B HB2  1 
ATOM   4421 H HB3  . HIS   B 1 146 ? -13.033 17.768 27.927 1.00 19.66 ? 126 HIS   B HB3  1 
ATOM   4422 H HD2  . HIS   B 1 146 ? -10.867 20.805 28.460 1.00 22.47 ? 126 HIS   B HD2  1 
ATOM   4423 H HE1  . HIS   B 1 146 ? -12.628 19.910 31.889 1.00 23.45 ? 126 HIS   B HE1  1 
ATOM   4424 H HE2  . HIS   B 1 146 ? -11.240 21.463 30.766 1.00 22.80 ? 126 HIS   B HE2  1 
ATOM   4425 N N    . SER   B 1 147 ? -12.044 15.381 26.618 1.00 15.69 ? 127 SER   B N    1 
ATOM   4426 C CA   . SER   B 1 147 ? -12.752 14.435 25.775 1.00 15.60 ? 127 SER   B CA   1 
ATOM   4427 C C    . SER   B 1 147 ? -14.171 14.291 26.300 1.00 16.31 ? 127 SER   B C    1 
ATOM   4428 O O    . SER   B 1 147 ? -14.360 14.083 27.505 1.00 16.67 ? 127 SER   B O    1 
ATOM   4429 C CB   . SER   B 1 147 ? -12.056 13.082 25.861 1.00 16.73 ? 127 SER   B CB   1 
ATOM   4430 O OG   . SER   B 1 147 ? -12.696 12.048 25.139 1.00 16.85 ? 127 SER   B OG   1 
ATOM   4431 H H    . SER   B 1 147 ? -11.931 15.089 27.419 1.00 18.83 ? 127 SER   B H    1 
ATOM   4432 H HA   . SER   B 1 147 ? -12.781 14.742 24.855 1.00 18.72 ? 127 SER   B HA   1 
ATOM   4433 H HB2  . SER   B 1 147 ? -11.157 13.183 25.510 1.00 20.08 ? 127 SER   B HB2  1 
ATOM   4434 H HB3  . SER   B 1 147 ? -12.020 12.820 26.794 1.00 20.08 ? 127 SER   B HB3  1 
ATOM   4435 H HG   . SER   B 1 147 ? -13.461 11.907 25.456 1.00 20.22 ? 127 SER   B HG   1 
ATOM   4436 N N    . PHE   B 1 148 ? -15.153 14.379 25.400 1.00 15.76 ? 128 PHE   B N    1 
ATOM   4437 C CA   . PHE   B 1 148 ? -16.563 14.175 25.730 1.00 16.26 ? 128 PHE   B CA   1 
ATOM   4438 C C    . PHE   B 1 148 ? -17.149 13.106 24.822 1.00 17.29 ? 128 PHE   B C    1 
ATOM   4439 O O    . PHE   B 1 148 ? -17.222 13.298 23.599 1.00 18.67 ? 128 PHE   B O    1 
ATOM   4440 C CB   . PHE   B 1 148 ? -17.392 15.445 25.571 1.00 17.19 ? 128 PHE   B CB   1 
ATOM   4441 C CG   . PHE   B 1 148 ? -17.054 16.563 26.517 1.00 16.57 ? 128 PHE   B CG   1 
ATOM   4442 C CD1  . PHE   B 1 148 ? -16.045 17.486 26.237 1.00 17.15 ? 128 PHE   B CD1  1 
ATOM   4443 C CD2  . PHE   B 1 148 ? -17.742 16.702 27.708 1.00 18.00 ? 128 PHE   B CD2  1 
ATOM   4444 C CE1  . PHE   B 1 148 ? -15.776 18.525 27.108 1.00 17.49 ? 128 PHE   B CE1  1 
ATOM   4445 C CE2  . PHE   B 1 148 ? -17.450 17.748 28.574 1.00 18.84 ? 128 PHE   B CE2  1 
ATOM   4446 C CZ   . PHE   B 1 148 ? -16.480 18.658 28.274 1.00 17.74 ? 128 PHE   B CZ   1 
ATOM   4447 H H    . PHE   B 1 148 ? -15.023 14.561 24.570 1.00 18.91 ? 128 PHE   B H    1 
ATOM   4448 H HA   . PHE   B 1 148 ? -16.601 13.882 26.654 1.00 19.52 ? 128 PHE   B HA   1 
ATOM   4449 H HB2  . PHE   B 1 148 ? -17.265 15.781 24.670 1.00 20.62 ? 128 PHE   B HB2  1 
ATOM   4450 H HB3  . PHE   B 1 148 ? -18.325 15.220 25.713 1.00 20.62 ? 128 PHE   B HB3  1 
ATOM   4451 H HD1  . PHE   B 1 148 ? -15.549 17.401 25.455 1.00 20.59 ? 128 PHE   B HD1  1 
ATOM   4452 H HD2  . PHE   B 1 148 ? -18.406 16.090 27.931 1.00 21.60 ? 128 PHE   B HD2  1 
ATOM   4453 H HE1  . PHE   B 1 148 ? -15.109 19.139 26.900 1.00 20.99 ? 128 PHE   B HE1  1 
ATOM   4454 H HE2  . PHE   B 1 148 ? -17.923 17.829 29.371 1.00 22.60 ? 128 PHE   B HE2  1 
ATOM   4455 H HZ   . PHE   B 1 148 ? -16.300 19.362 28.855 1.00 21.29 ? 128 PHE   B HZ   1 
ATOM   4456 N N    . ARG   B 1 149 ? -17.644 12.022 25.422 1.00 17.55 ? 129 ARG   B N    1 
ATOM   4457 C CA   . ARG   B 1 149 ? -18.378 10.998 24.692 1.00 18.77 ? 129 ARG   B CA   1 
ATOM   4458 C C    . ARG   B 1 149 ? -19.817 10.969 25.203 1.00 18.36 ? 129 ARG   B C    1 
ATOM   4459 O O    . ARG   B 1 149 ? -20.064 11.012 26.415 1.00 19.59 ? 129 ARG   B O    1 
ATOM   4460 C CB   . ARG   B 1 149 ? -17.733 9.636  24.854 1.00 19.60 ? 129 ARG   B CB   1 
ATOM   4461 C CG   . ARG   B 1 149 ? -16.319 9.586  24.308 1.00 20.39 ? 129 ARG   B CG   1 
ATOM   4462 C CD   . ARG   B 1 149 ? -15.733 8.182  24.374 1.00 21.17 ? 129 ARG   B CD   1 
ATOM   4463 N NE   . ARG   B 1 149 ? -16.367 7.333  23.374 1.00 23.91 ? 129 ARG   B NE   1 
ATOM   4464 C CZ   . ARG   B 1 149 ? -16.018 6.083  23.118 1.00 26.81 ? 129 ARG   B CZ   1 
ATOM   4465 N NH1  . ARG   B 1 149 ? -15.074 5.476  23.814 1.00 29.01 ? 129 ARG   B NH1  1 
ATOM   4466 N NH2  . ARG   B 1 149 ? -16.635 5.429  22.137 1.00 28.72 ? 129 ARG   B NH2  1 
ATOM   4467 H H    . ARG   B 1 149 ? -17.564 11.859 26.263 1.00 21.06 ? 129 ARG   B H    1 
ATOM   4468 H HA   . ARG   B 1 149 ? -18.388 11.205 23.745 1.00 22.52 ? 129 ARG   B HA   1 
ATOM   4469 H HB2  . ARG   B 1 149 ? -17.699 9.414  25.797 1.00 23.52 ? 129 ARG   B HB2  1 
ATOM   4470 H HB3  . ARG   B 1 149 ? -18.263 8.978  24.377 1.00 23.52 ? 129 ARG   B HB3  1 
ATOM   4471 H HG2  . ARG   B 1 149 ? -16.325 9.868  23.380 1.00 24.47 ? 129 ARG   B HG2  1 
ATOM   4472 H HG3  . ARG   B 1 149 ? -15.754 10.175 24.831 1.00 24.47 ? 129 ARG   B HG3  1 
ATOM   4473 H HD2  . ARG   B 1 149 ? -14.781 8.217  24.194 1.00 25.41 ? 129 ARG   B HD2  1 
ATOM   4474 H HD3  . ARG   B 1 149 ? -15.892 7.802  25.252 1.00 25.41 ? 129 ARG   B HD3  1 
ATOM   4475 H HE   . ARG   B 1 149 ? -17.015 7.668  22.918 1.00 28.70 ? 129 ARG   B HE   1 
ATOM   4476 H HH11 . ARG   B 1 149 ? -14.673 5.893  24.450 1.00 34.81 ? 129 ARG   B HH11 1 
ATOM   4477 H HH12 . ARG   B 1 149 ? -14.862 4.663  23.632 1.00 34.81 ? 129 ARG   B HH12 1 
ATOM   4478 H HH21 . ARG   B 1 149 ? -17.250 5.819  21.680 1.00 34.47 ? 129 ARG   B HH21 1 
ATOM   4479 H HH22 . ARG   B 1 149 ? -16.417 4.616  21.960 1.00 34.47 ? 129 ARG   B HH22 1 
ATOM   4480 N N    . PHE   B 1 150 ? -20.757 10.874 24.271 1.00 18.60 ? 130 PHE   B N    1 
ATOM   4481 C CA   . PHE   B 1 150 ? -22.180 11.009 24.524 1.00 19.62 ? 130 PHE   B CA   1 
ATOM   4482 C C    . PHE   B 1 150 ? -22.928 9.708  24.303 1.00 21.54 ? 130 PHE   B C    1 
ATOM   4483 O O    . PHE   B 1 150 ? -22.533 8.861  23.494 1.00 23.12 ? 130 PHE   B O    1 
ATOM   4484 C CB   . PHE   B 1 150 ? -22.779 12.064 23.576 1.00 20.05 ? 130 PHE   B CB   1 
ATOM   4485 C CG   . PHE   B 1 150 ? -22.442 13.473 23.957 1.00 19.87 ? 130 PHE   B CG   1 
ATOM   4486 C CD1  . PHE   B 1 150 ? -21.208 14.044 23.626 1.00 20.44 ? 130 PHE   B CD1  1 
ATOM   4487 C CD2  . PHE   B 1 150 ? -23.334 14.221 24.704 1.00 20.20 ? 130 PHE   B CD2  1 
ATOM   4488 C CE1  . PHE   B 1 150 ? -20.910 15.349 24.041 1.00 20.43 ? 130 PHE   B CE1  1 
ATOM   4489 C CE2  . PHE   B 1 150 ? -23.048 15.499 25.082 1.00 20.94 ? 130 PHE   B CE2  1 
ATOM   4490 C CZ   . PHE   B 1 150 ? -21.830 16.066 24.769 1.00 21.07 ? 130 PHE   B CZ   1 
ATOM   4491 H H    . PHE   B 1 150 ? -20.583 10.725 23.442 1.00 22.32 ? 130 PHE   B H    1 
ATOM   4492 H HA   . PHE   B 1 150 ? -22.301 11.264 25.452 1.00 23.55 ? 130 PHE   B HA   1 
ATOM   4493 H HB2  . PHE   B 1 150 ? -22.439 11.909 22.681 1.00 24.07 ? 130 PHE   B HB2  1 
ATOM   4494 H HB3  . PHE   B 1 150 ? -23.745 11.977 23.583 1.00 24.07 ? 130 PHE   B HB3  1 
ATOM   4495 H HD1  . PHE   B 1 150 ? -20.587 13.559 23.131 1.00 24.53 ? 130 PHE   B HD1  1 
ATOM   4496 H HD2  . PHE   B 1 150 ? -24.147 13.843 24.954 1.00 24.24 ? 130 PHE   B HD2  1 
ATOM   4497 H HE1  . PHE   B 1 150 ? -20.089 15.730 23.825 1.00 24.52 ? 130 PHE   B HE1  1 
ATOM   4498 H HE2  . PHE   B 1 150 ? -23.679 15.993 25.554 1.00 25.13 ? 130 PHE   B HE2  1 
ATOM   4499 H HZ   . PHE   B 1 150 ? -21.633 16.930 25.050 1.00 25.29 ? 130 PHE   B HZ   1 
ATOM   4500 N N    A GLU   B 1 151 ? -24.047 9.582  25.014 0.60 21.71 ? 131 GLU   B N    1 
ATOM   4501 N N    B GLU   B 1 151 ? -24.046 9.573  25.016 0.40 22.78 ? 131 GLU   B N    1 
ATOM   4502 C CA   A GLU   B 1 151 ? -25.015 8.512  24.812 0.60 22.53 ? 131 GLU   B CA   1 
ATOM   4503 C CA   B GLU   B 1 151 ? -25.012 8.509  24.761 0.40 24.69 ? 131 GLU   B CA   1 
ATOM   4504 C C    A GLU   B 1 151 ? -26.408 9.101  25.011 0.60 22.94 ? 131 GLU   B C    1 
ATOM   4505 C C    B GLU   B 1 151 ? -26.412 9.053  25.017 0.40 24.20 ? 131 GLU   B C    1 
ATOM   4506 O O    A GLU   B 1 151 ? -26.675 9.721  26.042 0.60 22.51 ? 131 GLU   B O    1 
ATOM   4507 O O    B GLU   B 1 151 ? -26.692 9.564  26.104 0.40 24.14 ? 131 GLU   B O    1 
ATOM   4508 C CB   A GLU   B 1 151 ? -24.773 7.374  25.809 0.60 24.68 ? 131 GLU   B CB   1 
ATOM   4509 C CB   B GLU   B 1 151 ? -24.743 7.284  25.637 0.40 28.24 ? 131 GLU   B CB   1 
ATOM   4510 C CG   A GLU   B 1 151 ? -25.752 6.211  25.736 0.60 28.50 ? 131 GLU   B CG   1 
ATOM   4511 C CG   B GLU   B 1 151 ? -23.468 6.560  25.253 0.40 32.55 ? 131 GLU   B CG   1 
ATOM   4512 C CD   A GLU   B 1 151 ? -25.531 5.241  26.894 0.60 33.39 ? 131 GLU   B CD   1 
ATOM   4513 C CD   B GLU   B 1 151 ? -23.371 5.166  25.831 0.40 36.08 ? 131 GLU   B CD   1 
ATOM   4514 O OE1  A GLU   B 1 151 ? -24.707 4.314  26.749 0.60 37.40 ? 131 GLU   B OE1  1 
ATOM   4515 O OE1  B GLU   B 1 151 ? -24.297 4.754  26.556 0.40 38.41 ? 131 GLU   B OE1  1 
ATOM   4516 O OE2  A GLU   B 1 151 ? -26.153 5.423  27.961 0.60 34.96 ? 131 GLU   B OE2  1 
ATOM   4517 O OE2  B GLU   B 1 151 ? -22.361 4.480  25.560 0.40 35.19 ? 131 GLU   B OE2  1 
ATOM   4518 H H    A GLU   B 1 151 ? -24.274 10.125 25.641 0.60 26.05 ? 131 GLU   B H    1 
ATOM   4519 H H    B GLU   B 1 151 ? -24.270 10.094 25.663 0.40 27.34 ? 131 GLU   B H    1 
ATOM   4520 H HA   A GLU   B 1 151 ? -24.946 8.159  23.911 0.60 27.04 ? 131 GLU   B HA   1 
ATOM   4521 H HA   B GLU   B 1 151 ? -24.948 8.238  23.832 0.40 29.63 ? 131 GLU   B HA   1 
ATOM   4522 H HB2  A GLU   B 1 151 ? -23.886 7.015  25.650 0.60 29.61 ? 131 GLU   B HB2  1 
ATOM   4523 H HB2  B GLU   B 1 151 ? -24.660 7.569  26.561 0.40 33.89 ? 131 GLU   B HB2  1 
ATOM   4524 H HB3  A GLU   B 1 151 ? -24.827 7.740  26.706 0.60 29.61 ? 131 GLU   B HB3  1 
ATOM   4525 H HB3  B GLU   B 1 151 ? -25.481 6.662  25.546 0.40 33.89 ? 131 GLU   B HB3  1 
ATOM   4526 H HG2  A GLU   B 1 151 ? -26.660 6.548  25.787 0.60 34.20 ? 131 GLU   B HG2  1 
ATOM   4527 H HG2  B GLU   B 1 151 ? -23.429 6.484  24.286 0.40 39.06 ? 131 GLU   B HG2  1 
ATOM   4528 H HG3  A GLU   B 1 151 ? -25.622 5.731  24.903 0.60 34.20 ? 131 GLU   B HG3  1 
ATOM   4529 H HG3  B GLU   B 1 151 ? -22.708 7.069  25.576 0.40 39.06 ? 131 GLU   B HG3  1 
ATOM   4530 N N    . ASN   B 1 152 ? -27.271 8.975  24.003 1.00 24.85 ? 132 ASN   B N    1 
ATOM   4531 C CA   . ASN   B 1 152 ? -28.675 9.405  24.102 1.00 28.03 ? 132 ASN   B CA   1 
ATOM   4532 C C    . ASN   B 1 152 ? -28.789 10.821 24.665 1.00 25.83 ? 132 ASN   B C    1 
ATOM   4533 O O    . ASN   B 1 152 ? -29.575 11.103 25.580 1.00 29.03 ? 132 ASN   B O    1 
ATOM   4534 C CB   . ASN   B 1 152 ? -29.535 8.404  24.895 1.00 32.05 ? 132 ASN   B CB   1 
ATOM   4535 C CG   . ASN   B 1 152 ? -31.052 8.699  24.806 1.00 38.19 ? 132 ASN   B CG   1 
ATOM   4536 O OD1  . ASN   B 1 152 ? -31.516 9.352  23.859 1.00 39.85 ? 132 ASN   B OD1  1 
ATOM   4537 N ND2  . ASN   B 1 152 ? -31.826 8.220  25.806 1.00 41.23 ? 132 ASN   B ND2  1 
ATOM   4538 H H    A ASN   B 1 152 ? -27.068 8.640  23.238 0.60 29.82 ? 132 ASN   B H    1 
ATOM   4539 H H    B ASN   B 1 152 ? -27.065 8.671  23.226 0.40 29.82 ? 132 ASN   B H    1 
ATOM   4540 H HA   . ASN   B 1 152 ? -29.033 9.427  23.201 1.00 33.63 ? 132 ASN   B HA   1 
ATOM   4541 H HB2  . ASN   B 1 152 ? -29.384 7.513  24.544 1.00 38.46 ? 132 ASN   B HB2  1 
ATOM   4542 H HB3  . ASN   B 1 152 ? -29.278 8.441  25.830 1.00 38.46 ? 132 ASN   B HB3  1 
ATOM   4543 H HD21 . ASN   B 1 152 ? -32.674 8.360  25.798 1.00 49.47 ? 132 ASN   B HD21 1 
ATOM   4544 H HD22 . ASN   B 1 152 ? -31.470 7.775  26.450 1.00 49.47 ? 132 ASN   B HD22 1 
ATOM   4545 N N    . GLY   B 1 153 ? -27.990 11.724 24.100 1.00 25.64 ? 133 GLY   B N    1 
ATOM   4546 C CA   . GLY   B 1 153 ? -28.163 13.132 24.351 1.00 26.02 ? 133 GLY   B CA   1 
ATOM   4547 C C    . GLY   B 1 153 ? -27.438 13.675 25.552 1.00 22.46 ? 133 GLY   B C    1 
ATOM   4548 O O    . GLY   B 1 153 ? -27.537 14.885 25.809 1.00 22.29 ? 133 GLY   B O    1 
ATOM   4549 H H    . GLY   B 1 153 ? -27.342 11.535 23.566 1.00 30.77 ? 133 GLY   B H    1 
ATOM   4550 H HA2  . GLY   B 1 153 ? -27.851 13.623 23.575 1.00 31.23 ? 133 GLY   B HA2  1 
ATOM   4551 H HA3  . GLY   B 1 153 ? -29.108 13.308 24.477 1.00 31.23 ? 133 GLY   B HA3  1 
ATOM   4552 N N    . LEU   B 1 154 ? -26.741 12.833 26.317 1.00 21.12 ? 134 LEU   B N    1 
ATOM   4553 C CA   . LEU   B 1 154 ? -26.047 13.288 27.516 1.00 20.11 ? 134 LEU   B CA   1 
ATOM   4554 C C    . LEU   B 1 154 ? -24.627 12.732 27.553 1.00 19.38 ? 134 LEU   B C    1 
ATOM   4555 O O    . LEU   B 1 154 ? -24.282 11.786 26.836 1.00 20.13 ? 134 LEU   B O    1 
ATOM   4556 C CB   . LEU   B 1 154 ? -26.794 12.893 28.801 1.00 21.11 ? 134 LEU   B CB   1 
ATOM   4557 C CG   . LEU   B 1 154 ? -28.191 13.501 28.962 1.00 22.83 ? 134 LEU   B CG   1 
ATOM   4558 C CD1  . LEU   B 1 154 ? -28.991 12.819 30.092 1.00 25.11 ? 134 LEU   B CD1  1 
ATOM   4559 C CD2  . LEU   B 1 154 ? -28.102 14.993 29.205 1.00 23.74 ? 134 LEU   B CD2  1 
ATOM   4560 H H    . LEU   B 1 154 ? -26.657 11.992 26.158 1.00 25.34 ? 134 LEU   B H    1 
ATOM   4561 H HA   . LEU   B 1 154 ? -25.992 14.256 27.477 1.00 24.13 ? 134 LEU   B HA   1 
ATOM   4562 H HB2  . LEU   B 1 154 ? -26.894 11.929 28.810 1.00 25.34 ? 134 LEU   B HB2  1 
ATOM   4563 H HB3  . LEU   B 1 154 ? -26.264 13.179 29.561 1.00 25.34 ? 134 LEU   B HB3  1 
ATOM   4564 H HG   . LEU   B 1 154 ? -28.675 13.351 28.135 1.00 27.39 ? 134 LEU   B HG   1 
ATOM   4565 H HD11 . LEU   B 1 154 ? -29.865 13.235 30.154 1.00 30.13 ? 134 LEU   B HD11 1 
ATOM   4566 H HD12 . LEU   B 1 154 ? -29.087 11.876 29.886 1.00 30.13 ? 134 LEU   B HD12 1 
ATOM   4567 H HD13 . LEU   B 1 154 ? -28.512 12.929 30.928 1.00 30.13 ? 134 LEU   B HD13 1 
ATOM   4568 H HD21 . LEU   B 1 154 ? -28.995 15.342 29.357 1.00 28.49 ? 134 LEU   B HD21 1 
ATOM   4569 H HD22 . LEU   B 1 154 ? -27.547 15.155 29.983 1.00 28.49 ? 134 LEU   B HD22 1 
ATOM   4570 H HD23 . LEU   B 1 154 ? -27.710 15.418 28.425 1.00 28.49 ? 134 LEU   B HD23 1 
ATOM   4571 N N    . ILE   B 1 155 ? -23.801 13.299 28.418 1.00 18.50 ? 135 ILE   B N    1 
ATOM   4572 C CA   . ILE   B 1 155 ? -22.400 12.898 28.511 1.00 18.55 ? 135 ILE   B CA   1 
ATOM   4573 C C    . ILE   B 1 155 ? -22.299 11.557 29.232 1.00 18.52 ? 135 ILE   B C    1 
ATOM   4574 O O    . ILE   B 1 155 ? -22.742 11.429 30.376 1.00 19.35 ? 135 ILE   B O    1 
ATOM   4575 C CB   . ILE   B 1 155 ? -21.571 13.947 29.261 1.00 17.96 ? 135 ILE   B CB   1 
ATOM   4576 C CG1  . ILE   B 1 155 ? -21.623 15.312 28.604 1.00 18.56 ? 135 ILE   B CG1  1 
ATOM   4577 C CG2  . ILE   B 1 155 ? -20.110 13.473 29.365 1.00 18.96 ? 135 ILE   B CG2  1 
ATOM   4578 C CD1  . ILE   B 1 155 ? -21.137 16.446 29.475 1.00 19.30 ? 135 ILE   B CD1  1 
ATOM   4579 H H    . ILE   B 1 155 ? -24.026 13.922 28.967 1.00 22.20 ? 135 ILE   B H    1 
ATOM   4580 H HA   . ILE   B 1 155 ? -22.057 12.796 27.609 1.00 22.26 ? 135 ILE   B HA   1 
ATOM   4581 H HB   . ILE   B 1 155 ? -21.961 14.041 30.144 1.00 21.55 ? 135 ILE   B HB   1 
ATOM   4582 H HG12 . ILE   B 1 155 ? -21.066 15.294 27.810 1.00 22.28 ? 135 ILE   B HG12 1 
ATOM   4583 H HG13 . ILE   B 1 155 ? -22.542 15.503 28.361 1.00 22.28 ? 135 ILE   B HG13 1 
ATOM   4584 H HG21 . ILE   B 1 155 ? -19.560 14.211 29.673 1.00 22.75 ? 135 ILE   B HG21 1 
ATOM   4585 H HG22 . ILE   B 1 155 ? -20.061 12.738 29.996 1.00 22.75 ? 135 ILE   B HG22 1 
ATOM   4586 H HG23 . ILE   B 1 155 ? -19.810 13.180 28.491 1.00 22.75 ? 135 ILE   B HG23 1 
ATOM   4587 H HD11 . ILE   B 1 155 ? -21.350 17.289 29.044 1.00 23.16 ? 135 ILE   B HD11 1 
ATOM   4588 H HD12 . ILE   B 1 155 ? -21.578 16.394 30.337 1.00 23.16 ? 135 ILE   B HD12 1 
ATOM   4589 H HD13 . ILE   B 1 155 ? -20.177 16.367 29.590 1.00 23.16 ? 135 ILE   B HD13 1 
ATOM   4590 N N    . LYS   B 1 156 ? -21.711 10.564 28.555 1.00 18.96 ? 136 LYS   B N    1 
ATOM   4591 C CA   . LYS   B 1 156 ? -21.394 9.256  29.112 1.00 20.46 ? 136 LYS   B CA   1 
ATOM   4592 C C    . LYS   B 1 156 ? -20.001 9.251  29.742 1.00 19.36 ? 136 LYS   B C    1 
ATOM   4593 O O    . LYS   B 1 156 ? -19.802 8.602  30.772 1.00 20.17 ? 136 LYS   B O    1 
ATOM   4594 C CB   . LYS   B 1 156 ? -21.521 8.184  28.034 1.00 23.71 ? 136 LYS   B CB   1 
ATOM   4595 C CG   . LYS   B 1 156 ? -21.255 6.800  28.486 1.00 27.67 ? 136 LYS   B CG   1 
ATOM   4596 C CD   . LYS   B 1 156 ? -22.366 6.361  29.434 1.00 35.78 ? 136 LYS   B CD   1 
ATOM   4597 C CE   . LYS   B 1 156 ? -22.759 4.893  29.258 1.00 59.40 ? 136 LYS   B CE   1 
ATOM   4598 N NZ   . LYS   B 1 156 ? -21.927 3.981  30.086 1.00 58.68 ? 136 LYS   B NZ   1 
ATOM   4599 H H    . LYS   B 1 156 ? -21.475 10.632 27.730 1.00 22.76 ? 136 LYS   B H    1 
ATOM   4600 H HA   . LYS   B 1 156 ? -22.032 9.025  29.806 1.00 24.56 ? 136 LYS   B HA   1 
ATOM   4601 H HB2  . LYS   B 1 156 ? -22.425 8.207  27.685 1.00 28.46 ? 136 LYS   B HB2  1 
ATOM   4602 H HB3  . LYS   B 1 156 ? -20.887 8.385  27.327 1.00 28.46 ? 136 LYS   B HB3  1 
ATOM   4603 H HG2  . LYS   B 1 156 ? -21.238 6.201  27.722 1.00 33.21 ? 136 LYS   B HG2  1 
ATOM   4604 H HG3  . LYS   B 1 156 ? -20.407 6.763  28.955 1.00 33.21 ? 136 LYS   B HG3  1 
ATOM   4605 H HD2  . LYS   B 1 156 ? -22.066 6.482  30.348 1.00 42.94 ? 136 LYS   B HD2  1 
ATOM   4606 H HD3  . LYS   B 1 156 ? -23.153 6.902  29.268 1.00 42.94 ? 136 LYS   B HD3  1 
ATOM   4607 H HE2  . LYS   B 1 156 ? -23.685 4.778  29.522 1.00 71.28 ? 136 LYS   B HE2  1 
ATOM   4608 H HE3  . LYS   B 1 156 ? -22.645 4.642  28.328 1.00 71.28 ? 136 LYS   B HE3  1 
ATOM   4609 H HZ1  . LYS   B 1 156 ? -22.178 3.137  29.956 1.00 70.42 ? 136 LYS   B HZ1  1 
ATOM   4610 H HZ2  . LYS   B 1 156 ? -21.069 4.065  29.862 1.00 70.42 ? 136 LYS   B HZ2  1 
ATOM   4611 H HZ3  . LYS   B 1 156 ? -22.021 4.181  30.948 1.00 70.42 ? 136 LYS   B HZ3  1 
ATOM   4612 N N    . GLU   B 1 157 ? -19.032 9.952  29.141 1.00 18.34 ? 137 GLU   B N    1 
ATOM   4613 C CA   . GLU   B 1 157 ? -17.675 9.996  29.672 1.00 17.64 ? 137 GLU   B CA   1 
ATOM   4614 C C    . GLU   B 1 157 ? -17.053 11.342 29.343 1.00 17.00 ? 137 GLU   B C    1 
ATOM   4615 O O    . GLU   B 1 157 ? -16.916 11.703 28.164 1.00 17.83 ? 137 GLU   B O    1 
ATOM   4616 C CB   . GLU   B 1 157 ? -16.833 8.893  29.055 1.00 19.30 ? 137 GLU   B CB   1 
ATOM   4617 C CG   . GLU   B 1 157 ? -15.465 8.793  29.646 1.00 20.62 ? 137 GLU   B CG   1 
ATOM   4618 C CD   . GLU   B 1 157 ? -14.557 7.877  28.846 1.00 23.21 ? 137 GLU   B CD   1 
ATOM   4619 O OE1  . GLU   B 1 157 ? -14.228 8.233  27.687 1.00 23.30 ? 137 GLU   B OE1  1 
ATOM   4620 O OE2  . GLU   B 1 157 ? -14.175 6.809  29.378 1.00 27.13 ? 137 GLU   B OE2  1 
ATOM   4621 H H    . GLU   B 1 157 ? -19.142 10.411 28.422 1.00 22.01 ? 137 GLU   B H    1 
ATOM   4622 H HA   . GLU   B 1 157 ? -17.707 9.894  30.636 1.00 21.17 ? 137 GLU   B HA   1 
ATOM   4623 H HB2  . GLU   B 1 157 ? -17.281 8.043  29.193 1.00 23.17 ? 137 GLU   B HB2  1 
ATOM   4624 H HB3  . GLU   B 1 157 ? -16.736 9.066  28.105 1.00 23.17 ? 137 GLU   B HB3  1 
ATOM   4625 H HG2  . GLU   B 1 157 ? -15.062 9.675  29.666 1.00 24.74 ? 137 GLU   B HG2  1 
ATOM   4626 H HG3  . GLU   B 1 157 ? -15.533 8.439  30.546 1.00 24.74 ? 137 GLU   B HG3  1 
ATOM   4627 N N    . GLN   B 1 158 ? -16.620 12.039 30.390 1.00 16.59 ? 138 GLN   B N    1 
ATOM   4628 C CA   . GLN   B 1 158 ? -15.821 13.252 30.272 1.00 15.73 ? 138 GLN   B CA   1 
ATOM   4629 C C    . GLN   B 1 158 ? -14.464 12.941 30.875 1.00 15.68 ? 138 GLN   B C    1 
ATOM   4630 O O    . GLN   B 1 158 ? -14.378 12.314 31.927 1.00 17.27 ? 138 GLN   B O    1 
ATOM   4631 C CB   . GLN   B 1 158 ? -16.468 14.416 31.018 1.00 17.07 ? 138 GLN   B CB   1 
ATOM   4632 C CG   . GLN   B 1 158 ? -15.704 15.758 31.018 1.00 18.11 ? 138 GLN   B CG   1 
ATOM   4633 C CD   . GLN   B 1 158 ? -14.689 15.823 32.160 1.00 19.31 ? 138 GLN   B CD   1 
ATOM   4634 O OE1  . GLN   B 1 158 ? -14.891 15.195 33.204 1.00 20.56 ? 138 GLN   B OE1  1 
ATOM   4635 N NE2  . GLN   B 1 158 ? -13.650 16.609 31.995 1.00 21.63 ? 138 GLN   B NE2  1 
ATOM   4636 H H    . GLN   B 1 158 ? -16.782 11.819 31.206 1.00 19.91 ? 138 GLN   B H    1 
ATOM   4637 H HA   . GLN   B 1 158 ? -15.727 13.516 29.343 1.00 18.88 ? 138 GLN   B HA   1 
ATOM   4638 H HB2  . GLN   B 1 158 ? -17.335 14.585 30.617 1.00 20.49 ? 138 GLN   B HB2  1 
ATOM   4639 H HB3  . GLN   B 1 158 ? -16.578 14.153 31.946 1.00 20.49 ? 138 GLN   B HB3  1 
ATOM   4640 H HG2  . GLN   B 1 158 ? -15.227 15.856 30.179 1.00 21.73 ? 138 GLN   B HG2  1 
ATOM   4641 H HG3  . GLN   B 1 158 ? -16.335 16.486 31.129 1.00 21.73 ? 138 GLN   B HG3  1 
ATOM   4642 H HE21 . GLN   B 1 158 ? -13.563 17.060 31.269 1.00 25.96 ? 138 GLN   B HE21 1 
ATOM   4643 H HE22 . GLN   B 1 158 ? -13.057 16.673 32.615 1.00 25.96 ? 138 GLN   B HE22 1 
ATOM   4644 N N    . ARG   B 1 159 ? -13.401 13.306 30.172 1.00 14.99 ? 139 ARG   B N    1 
ATOM   4645 C CA   . ARG   B 1 159 ? -12.044 13.178 30.691 1.00 15.33 ? 139 ARG   B CA   1 
ATOM   4646 C C    . ARG   B 1 159 ? -11.273 14.449 30.430 1.00 15.46 ? 139 ARG   B C    1 
ATOM   4647 O O    . ARG   B 1 159 ? -11.340 15.001 29.332 1.00 16.56 ? 139 ARG   B O    1 
ATOM   4648 C CB   . ARG   B 1 159 ? -11.318 12.037 29.961 1.00 15.81 ? 139 ARG   B CB   1 
ATOM   4649 C CG   . ARG   B 1 159 ? -11.980 10.668 30.062 1.00 16.51 ? 139 ARG   B CG   1 
ATOM   4650 C CD   . ARG   B 1 159 ? -11.283 9.594  29.196 1.00 17.86 ? 139 ARG   B CD   1 
ATOM   4651 N NE   . ARG   B 1 159 ? -11.359 9.939  27.784 1.00 17.15 ? 139 ARG   B NE   1 
ATOM   4652 C CZ   . ARG   B 1 159 ? -10.524 9.489  26.852 1.00 16.98 ? 139 ARG   B CZ   1 
ATOM   4653 N NH1  . ARG   B 1 159 ? -9.513  8.703  27.162 1.00 17.66 ? 139 ARG   B NH1  1 
ATOM   4654 N NH2  . ARG   B 1 159 ? -10.673 9.896  25.597 1.00 17.34 ? 139 ARG   B NH2  1 
ATOM   4655 H H    . ARG   B 1 159 ? -13.440 13.635 29.379 1.00 17.99 ? 139 ARG   B H    1 
ATOM   4656 H HA   . ARG   B 1 159 ? -12.074 13.016 31.647 1.00 18.40 ? 139 ARG   B HA   1 
ATOM   4657 H HB2  . ARG   B 1 159 ? -11.264 12.263 29.020 1.00 18.97 ? 139 ARG   B HB2  1 
ATOM   4658 H HB3  . ARG   B 1 159 ? -10.426 11.955 30.335 1.00 18.97 ? 139 ARG   B HB3  1 
ATOM   4659 H HG2  . ARG   B 1 159 ? -11.952 10.371 30.985 1.00 19.82 ? 139 ARG   B HG2  1 
ATOM   4660 H HG3  . ARG   B 1 159 ? -12.901 10.740 29.765 1.00 19.82 ? 139 ARG   B HG3  1 
ATOM   4661 H HD2  . ARG   B 1 159 ? -10.348 9.532  29.448 1.00 21.43 ? 139 ARG   B HD2  1 
ATOM   4662 H HD3  . ARG   B 1 159 ? -11.720 8.738  29.328 1.00 21.43 ? 139 ARG   B HD3  1 
ATOM   4663 H HE   . ARG   B 1 159 ? -11.988 10.471 27.535 1.00 20.58 ? 139 ARG   B HE   1 
ATOM   4664 H HH11 . ARG   B 1 159 ? -9.384  8.472  27.980 1.00 21.19 ? 139 ARG   B HH11 1 
ATOM   4665 H HH12 . ARG   B 1 159 ? -8.983  8.422  26.547 1.00 21.19 ? 139 ARG   B HH12 1 
ATOM   4666 H HH21 . ARG   B 1 159 ? -11.304 10.445 25.394 1.00 20.81 ? 139 ARG   B HH21 1 
ATOM   4667 H HH22 . ARG   B 1 159 ? -10.139 9.612  24.986 1.00 20.81 ? 139 ARG   B HH22 1 
ATOM   4668 N N    . GLU   B 1 160 ? -10.475 14.870 31.404 1.00 15.62 ? 140 GLU   B N    1 
ATOM   4669 C CA   . GLU   B 1 160 ? -9.604  16.012 31.189 1.00 16.90 ? 140 GLU   B CA   1 
ATOM   4670 C C    . GLU   B 1 160 ? -8.141  15.632 31.388 1.00 15.77 ? 140 GLU   B C    1 
ATOM   4671 O O    . GLU   B 1 160 ? -7.801  14.767 32.199 1.00 16.36 ? 140 GLU   B O    1 
ATOM   4672 C CB   . GLU   B 1 160 ? -9.988  17.239 31.994 1.00 21.80 ? 140 GLU   B CB   1 
ATOM   4673 C CG   . GLU   B 1 160 ? -9.913  17.120 33.432 1.00 22.71 ? 140 GLU   B CG   1 
ATOM   4674 C CD   . GLU   B 1 160 ? -10.839 18.111 34.143 1.00 23.19 ? 140 GLU   B CD   1 
ATOM   4675 O OE1  . GLU   B 1 160 ? -12.065 18.035 33.949 1.00 24.51 ? 140 GLU   B OE1  1 
ATOM   4676 O OE2  . GLU   B 1 160 ? -10.347 18.938 34.943 1.00 26.46 ? 140 GLU   B OE2  1 
ATOM   4677 H H    . GLU   B 1 160 ? -10.424 14.514 32.185 1.00 18.74 ? 140 GLU   B H    1 
ATOM   4678 H HA   . GLU   B 1 160 ? -9.696  16.282 30.262 1.00 20.28 ? 140 GLU   B HA   1 
ATOM   4679 H HB2  . GLU   B 1 160 ? -9.397  17.964 31.738 1.00 26.16 ? 140 GLU   B HB2  1 
ATOM   4680 H HB3  . GLU   B 1 160 ? -10.906 17.466 31.775 1.00 26.16 ? 140 GLU   B HB3  1 
ATOM   4681 H HG2  . GLU   B 1 160 ? -10.175 16.223 33.692 1.00 27.25 ? 140 GLU   B HG2  1 
ATOM   4682 H HG3  . GLU   B 1 160 ? -9.004  17.297 33.719 1.00 27.25 ? 140 GLU   B HG3  1 
ATOM   4683 N N    . PHE   B 1 161 ? -7.297  16.283 30.588 1.00 15.79 ? 141 PHE   B N    1 
ATOM   4684 C CA   . PHE   B 1 161 ? -5.883  15.981 30.466 1.00 15.08 ? 141 PHE   B CA   1 
ATOM   4685 C C    . PHE   B 1 161 ? -5.100  17.280 30.582 1.00 14.84 ? 141 PHE   B C    1 
ATOM   4686 O O    . PHE   B 1 161 ? -5.370  18.244 29.859 1.00 16.09 ? 141 PHE   B O    1 
ATOM   4687 C CB   . PHE   B 1 161 ? -5.560  15.359 29.115 1.00 15.75 ? 141 PHE   B CB   1 
ATOM   4688 C CG   . PHE   B 1 161 ? -6.358  14.116 28.802 1.00 15.54 ? 141 PHE   B CG   1 
ATOM   4689 C CD1  . PHE   B 1 161 ? -7.627  14.211 28.237 1.00 16.79 ? 141 PHE   B CD1  1 
ATOM   4690 C CD2  . PHE   B 1 161 ? -5.842  12.863 29.051 1.00 16.64 ? 141 PHE   B CD2  1 
ATOM   4691 C CE1  . PHE   B 1 161 ? -8.331  13.061 27.923 1.00 17.92 ? 141 PHE   B CE1  1 
ATOM   4692 C CE2  . PHE   B 1 161 ? -6.559  11.732 28.751 1.00 18.44 ? 141 PHE   B CE2  1 
ATOM   4693 C CZ   . PHE   B 1 161 ? -7.816  11.849 28.188 1.00 18.28 ? 141 PHE   B CZ   1 
ATOM   4694 H H    . PHE   B 1 161 ? -7.538  16.936 30.083 1.00 18.95 ? 141 PHE   B H    1 
ATOM   4695 H HA   . PHE   B 1 161 ? -5.629  15.367 31.173 1.00 18.10 ? 141 PHE   B HA   1 
ATOM   4696 H HB2  . PHE   B 1 161 ? -5.745  16.011 28.421 1.00 18.90 ? 141 PHE   B HB2  1 
ATOM   4697 H HB3  . PHE   B 1 161 ? -4.621  15.117 29.101 1.00 18.90 ? 141 PHE   B HB3  1 
ATOM   4698 H HD1  . PHE   B 1 161 ? -8.002  15.046 28.071 1.00 20.14 ? 141 PHE   B HD1  1 
ATOM   4699 H HD2  . PHE   B 1 161 ? -4.996  12.783 29.429 1.00 19.97 ? 141 PHE   B HD2  1 
ATOM   4700 H HE1  . PHE   B 1 161 ? -9.168  13.128 27.525 1.00 21.51 ? 141 PHE   B HE1  1 
ATOM   4701 H HE2  . PHE   B 1 161 ? -6.201  10.892 28.926 1.00 22.13 ? 141 PHE   B HE2  1 
ATOM   4702 H HZ   . PHE   B 1 161 ? -8.308  11.084 27.991 1.00 21.94 ? 141 PHE   B HZ   1 
ATOM   4703 N N    . MET   B 1 162 ? -4.101  17.306 31.456 1.00 15.10 ? 142 MET   B N    1 
ATOM   4704 C CA   . MET   B 1 162 ? -3.249  18.481 31.638 1.00 15.80 ? 142 MET   B CA   1 
ATOM   4705 C C    . MET   B 1 162 ? -1.853  18.015 32.044 1.00 15.80 ? 142 MET   B C    1 
ATOM   4706 O O    . MET   B 1 162 ? -1.593  16.819 32.184 1.00 17.58 ? 142 MET   B O    1 
ATOM   4707 C CB   . MET   B 1 162 ? -3.880  19.480 32.625 1.00 17.06 ? 142 MET   B CB   1 
ATOM   4708 C CG   . MET   B 1 162 ? -4.334  18.878 33.977 1.00 19.46 ? 142 MET   B CG   1 
ATOM   4709 S SD   . MET   B 1 162 ? -2.967  18.161 34.917 1.00 20.56 ? 142 MET   B SD   1 
ATOM   4710 C CE   . MET   B 1 162 ? -3.562  18.034 36.559 1.00 20.36 ? 142 MET   B CE   1 
ATOM   4711 H H    . MET   B 1 162 ? -3.890  16.646 31.964 1.00 18.12 ? 142 MET   B H    1 
ATOM   4712 H HA   . MET   B 1 162 ? -3.164  18.949 30.793 1.00 18.97 ? 142 MET   B HA   1 
ATOM   4713 H HB2  . MET   B 1 162 ? -3.227  20.170 32.820 1.00 20.47 ? 142 MET   B HB2  1 
ATOM   4714 H HB3  . MET   B 1 162 ? -4.661  19.872 32.205 1.00 20.47 ? 142 MET   B HB3  1 
ATOM   4715 H HG2  . MET   B 1 162 ? -4.735  19.578 34.516 1.00 23.36 ? 142 MET   B HG2  1 
ATOM   4716 H HG3  . MET   B 1 162 ? -4.983  18.177 33.808 1.00 23.36 ? 142 MET   B HG3  1 
ATOM   4717 H HE1  . MET   B 1 162 ? -2.923  17.532 37.089 1.00 24.44 ? 142 MET   B HE1  1 
ATOM   4718 H HE2  . MET   B 1 162 ? -3.669  18.925 36.926 1.00 24.44 ? 142 MET   B HE2  1 
ATOM   4719 H HE3  . MET   B 1 162 ? -4.417  17.575 36.551 1.00 24.44 ? 142 MET   B HE3  1 
ATOM   4720 N N    . ASN   B 1 163 ? -0.960  18.983 32.221 1.00 16.23 ? 143 ASN   B N    1 
ATOM   4721 C CA   . ASN   B 1 163 ? 0.370   18.753 32.739 1.00 15.90 ? 143 ASN   B CA   1 
ATOM   4722 C C    . ASN   B 1 163 ? 0.338   18.951 34.251 1.00 15.60 ? 143 ASN   B C    1 
ATOM   4723 O O    . ASN   B 1 163 ? 0.219   20.098 34.711 1.00 16.53 ? 143 ASN   B O    1 
ATOM   4724 C CB   . ASN   B 1 163 ? 1.336   19.742 32.114 1.00 16.34 ? 143 ASN   B CB   1 
ATOM   4725 C CG   . ASN   B 1 163 ? 2.747   19.534 32.595 1.00 17.72 ? 143 ASN   B CG   1 
ATOM   4726 O OD1  . ASN   B 1 163 ? 3.025   18.678 33.457 1.00 18.05 ? 143 ASN   B OD1  1 
ATOM   4727 N ND2  . ASN   B 1 163 ? 3.659   20.301 32.040 1.00 21.30 ? 143 ASN   B ND2  1 
ATOM   4728 H H    . ASN   B 1 163 ? -1.112  19.810 32.041 1.00 19.47 ? 143 ASN   B H    1 
ATOM   4729 H HA   . ASN   B 1 163 ? 0.658   17.848 32.543 1.00 19.08 ? 143 ASN   B HA   1 
ATOM   4730 H HB2  . ASN   B 1 163 ? 1.325   19.633 31.150 1.00 19.61 ? 143 ASN   B HB2  1 
ATOM   4731 H HB3  . ASN   B 1 163 ? 1.065   20.644 32.348 1.00 19.61 ? 143 ASN   B HB3  1 
ATOM   4732 H HD21 . ASN   B 1 163 ? 4.483   20.228 32.275 1.00 25.56 ? 143 ASN   B HD21 1 
ATOM   4733 H HD22 . ASN   B 1 163 ? 3.432   20.876 31.442 1.00 25.56 ? 143 ASN   B HD22 1 
ATOM   4734 N N    . PRO   B 1 164 ? 0.429   17.890 35.059 1.00 15.40 ? 144 PRO   B N    1 
ATOM   4735 C CA   . PRO   B 1 164 ? 0.342   18.078 36.517 1.00 16.40 ? 144 PRO   B CA   1 
ATOM   4736 C C    . PRO   B 1 164 ? 1.438   18.935 37.111 1.00 16.11 ? 144 PRO   B C    1 
ATOM   4737 O O    . PRO   B 1 164 ? 1.253   19.480 38.207 1.00 16.97 ? 144 PRO   B O    1 
ATOM   4738 C CB   . PRO   B 1 164 ? 0.421   16.648 37.068 1.00 17.79 ? 144 PRO   B CB   1 
ATOM   4739 C CG   . PRO   B 1 164 ? -0.072  15.775 35.925 1.00 18.25 ? 144 PRO   B CG   1 
ATOM   4740 C CD   . PRO   B 1 164 ? 0.465   16.463 34.691 1.00 16.01 ? 144 PRO   B CD   1 
ATOM   4741 H HA   . PRO   B 1 164 ? -0.520  18.469 36.729 1.00 19.68 ? 144 PRO   B HA   1 
ATOM   4742 H HB2  . PRO   B 1 164 ? 1.338   16.433 37.302 1.00 21.35 ? 144 PRO   B HB2  1 
ATOM   4743 H HB3  . PRO   B 1 164 ? -0.150  16.560 37.847 1.00 21.35 ? 144 PRO   B HB3  1 
ATOM   4744 H HG2  . PRO   B 1 164 ? 0.284   14.877 36.010 1.00 21.90 ? 144 PRO   B HG2  1 
ATOM   4745 H HG3  . PRO   B 1 164 ? -1.042  15.748 35.918 1.00 21.90 ? 144 PRO   B HG3  1 
ATOM   4746 H HD2  . PRO   B 1 164 ? 1.373   16.177 34.504 1.00 19.21 ? 144 PRO   B HD2  1 
ATOM   4747 H HD3  . PRO   B 1 164 ? -0.102  16.289 33.924 1.00 19.21 ? 144 PRO   B HD3  1 
ATOM   4748 N N    . CYS   B 1 165 ? 2.549   19.125 36.407 1.00 16.69 ? 145 CYS   B N    1 
ATOM   4749 C CA   . CYS   B 1 165 ? 3.619   19.956 36.936 1.00 17.78 ? 145 CYS   B CA   1 
ATOM   4750 C C    . CYS   B 1 165 ? 3.156   21.385 37.210 1.00 17.62 ? 145 CYS   B C    1 
ATOM   4751 O O    . CYS   B 1 165 ? 3.606   22.005 38.177 1.00 18.68 ? 145 CYS   B O    1 
ATOM   4752 C CB   . CYS   B 1 165 ? 4.797   19.968 35.964 1.00 19.47 ? 145 CYS   B CB   1 
ATOM   4753 S SG   . CYS   B 1 165 ? 5.611   18.377 35.742 1.00 21.31 ? 145 CYS   B SG   1 
ATOM   4754 H H    . CYS   B 1 165 ? 2.706   18.789 35.632 1.00 20.02 ? 145 CYS   B H    1 
ATOM   4755 H HA   . CYS   B 1 165 ? 3.916   19.574 37.777 1.00 21.34 ? 145 CYS   B HA   1 
ATOM   4756 H HB2  . CYS   B 1 165 ? 4.475   20.254 35.095 1.00 23.36 ? 145 CYS   B HB2  1 
ATOM   4757 H HB3  . CYS   B 1 165 ? 5.462   20.592 36.293 1.00 23.36 ? 145 CYS   B HB3  1 
ATOM   4758 H HG   . CYS   B 1 165 ? 6.252   18.404 34.728 1.00 25.57 ? 145 CYS   B HG   1 
ATOM   4759 N N    . GLU   B 1 166 ? 2.209   21.901 36.423 1.00 17.12 ? 146 GLU   B N    1 
ATOM   4760 C CA   . GLU   B 1 166 ? 1.716   23.247 36.695 1.00 18.52 ? 146 GLU   B CA   1 
ATOM   4761 C C    . GLU   B 1 166 ? 0.867   23.279 37.956 1.00 18.23 ? 146 GLU   B C    1 
ATOM   4762 O O    . GLU   B 1 166 ? 0.867   24.286 38.668 1.00 19.97 ? 146 GLU   B O    1 
ATOM   4763 C CB   . GLU   B 1 166 ? 0.914   23.771 35.494 1.00 20.08 ? 146 GLU   B CB   1 
ATOM   4764 C CG   . GLU   B 1 166 ? 1.706   23.903 34.214 1.00 24.80 ? 146 GLU   B CG   1 
ATOM   4765 C CD   . GLU   B 1 166 ? 2.934   24.726 34.368 1.00 32.14 ? 146 GLU   B CD   1 
ATOM   4766 O OE1  . GLU   B 1 166 ? 2.900   25.763 35.057 1.00 32.06 ? 146 GLU   B OE1  1 
ATOM   4767 O OE2  . GLU   B 1 166 ? 3.931   24.337 33.754 1.00 40.92 ? 146 GLU   B OE2  1 
ATOM   4768 H H    . GLU   B 1 166 ? 1.849   21.504 35.750 1.00 20.55 ? 146 GLU   B H    1 
ATOM   4769 H HA   . GLU   B 1 166 ? 2.473   23.841 36.824 1.00 22.23 ? 146 GLU   B HA   1 
ATOM   4770 H HB2  . GLU   B 1 166 ? 0.182   23.158 35.322 1.00 24.10 ? 146 GLU   B HB2  1 
ATOM   4771 H HB3  . GLU   B 1 166 ? 0.567   24.649 35.715 1.00 24.10 ? 146 GLU   B HB3  1 
ATOM   4772 H HG2  . GLU   B 1 166 ? 1.974   23.019 33.917 1.00 29.76 ? 146 GLU   B HG2  1 
ATOM   4773 H HG3  . GLU   B 1 166 ? 1.148   24.324 33.541 1.00 29.76 ? 146 GLU   B HG3  1 
ATOM   4774 N N    . GLN   B 1 167 ? 0.151   22.199 38.245 1.00 17.06 ? 147 GLN   B N    1 
ATOM   4775 C CA   . GLN   B 1 167 ? -0.621  22.151 39.482 1.00 16.95 ? 147 GLN   B CA   1 
ATOM   4776 C C    . GLN   B 1 167 ? 0.311   21.998 40.676 1.00 17.07 ? 147 GLN   B C    1 
ATOM   4777 O O    . GLN   B 1 167 ? 0.119   22.657 41.703 1.00 18.19 ? 147 GLN   B O    1 
ATOM   4778 C CB   . GLN   B 1 167 ? -1.682  21.062 39.427 1.00 18.01 ? 147 GLN   B CB   1 
ATOM   4779 C CG   . GLN   B 1 167 ? -2.694  21.190 40.566 1.00 19.62 ? 147 GLN   B CG   1 
ATOM   4780 C CD   . GLN   B 1 167 ? -3.947  20.365 40.365 1.00 21.60 ? 147 GLN   B CD   1 
ATOM   4781 O OE1  . GLN   B 1 167 ? -4.256  19.946 39.260 1.00 23.55 ? 147 GLN   B OE1  1 
ATOM   4782 N NE2  . GLN   B 1 167 ? -4.702  20.178 41.436 1.00 23.47 ? 147 GLN   B NE2  1 
ATOM   4783 H H    . GLN   B 1 167 ? 0.095   21.495 37.755 1.00 20.48 ? 147 GLN   B H    1 
ATOM   4784 H HA   . GLN   B 1 167 ? -1.111  22.981 39.591 1.00 20.34 ? 147 GLN   B HA   1 
ATOM   4785 H HB2  . GLN   B 1 167 ? -2.161  21.127 38.586 1.00 21.62 ? 147 GLN   B HB2  1 
ATOM   4786 H HB3  . GLN   B 1 167 ? -1.252  20.195 39.498 1.00 21.62 ? 147 GLN   B HB3  1 
ATOM   4787 H HG2  . GLN   B 1 167 ? -2.275  20.896 41.390 1.00 23.55 ? 147 GLN   B HG2  1 
ATOM   4788 H HG3  . GLN   B 1 167 ? -2.961  22.119 40.643 1.00 23.55 ? 147 GLN   B HG3  1 
ATOM   4789 H HE21 . GLN   B 1 167 ? -4.469  20.519 42.191 1.00 28.16 ? 147 GLN   B HE21 1 
ATOM   4790 H HE22 . GLN   B 1 167 ? -5.425  19.717 41.378 1.00 28.16 ? 147 GLN   B HE22 1 
ATOM   4791 N N    . PHE   B 1 168 ? 1.386   21.212 40.529 1.00 17.80 ? 148 PHE   B N    1 
ATOM   4792 C CA   . PHE   B 1 168 ? 2.413   21.177 41.567 1.00 18.29 ? 148 PHE   B CA   1 
ATOM   4793 C C    . PHE   B 1 168 ? 2.901   22.590 41.885 1.00 18.69 ? 148 PHE   B C    1 
ATOM   4794 O O    . PHE   B 1 168 ? 2.994   22.988 43.053 1.00 19.63 ? 148 PHE   B O    1 
ATOM   4795 C CB   . PHE   B 1 168 ? 3.621   20.336 41.136 1.00 19.51 ? 148 PHE   B CB   1 
ATOM   4796 C CG   . PHE   B 1 168 ? 3.337   18.883 40.865 1.00 20.84 ? 148 PHE   B CG   1 
ATOM   4797 C CD1  . PHE   B 1 168 ? 2.211   18.238 41.348 1.00 22.80 ? 148 PHE   B CD1  1 
ATOM   4798 C CD2  . PHE   B 1 168 ? 4.229   18.156 40.079 1.00 21.38 ? 148 PHE   B CD2  1 
ATOM   4799 C CE1  . PHE   B 1 168 ? 1.990   16.896 41.058 1.00 26.57 ? 148 PHE   B CE1  1 
ATOM   4800 C CE2  . PHE   B 1 168 ? 4.013   16.817 39.779 1.00 25.33 ? 148 PHE   B CE2  1 
ATOM   4801 C CZ   . PHE   B 1 168 ? 2.902   16.175 40.264 1.00 27.94 ? 148 PHE   B CZ   1 
ATOM   4802 H H    . PHE   B 1 168 ? 1.538   20.702 39.853 1.00 21.37 ? 148 PHE   B H    1 
ATOM   4803 H HA   . PHE   B 1 168 ? 2.019   20.767 42.352 1.00 21.95 ? 148 PHE   B HA   1 
ATOM   4804 H HB2  . PHE   B 1 168 ? 3.982   20.717 40.320 1.00 23.42 ? 148 PHE   B HB2  1 
ATOM   4805 H HB3  . PHE   B 1 168 ? 4.286   20.374 41.841 1.00 23.42 ? 148 PHE   B HB3  1 
ATOM   4806 H HD1  . PHE   B 1 168 ? 1.599   18.705 41.870 1.00 27.36 ? 148 PHE   B HD1  1 
ATOM   4807 H HD2  . PHE   B 1 168 ? 4.988   18.578 39.747 1.00 25.65 ? 148 PHE   B HD2  1 
ATOM   4808 H HE1  . PHE   B 1 168 ? 1.232   16.471 41.391 1.00 31.88 ? 148 PHE   B HE1  1 
ATOM   4809 H HE2  . PHE   B 1 168 ? 4.622   16.355 39.249 1.00 30.40 ? 148 PHE   B HE2  1 
ATOM   4810 H HZ   . PHE   B 1 168 ? 2.754   15.277 40.071 1.00 33.52 ? 148 PHE   B HZ   1 
ATOM   4811 N N    . ARG   B 1 169 ? 3.284   23.344 40.842 1.00 19.43 ? 149 ARG   B N    1 
ATOM   4812 C CA   . ARG   B 1 169 ? 3.768   24.701 41.060 1.00 21.03 ? 149 ARG   B CA   1 
ATOM   4813 C C    . ARG   B 1 169 ? 2.755   25.553 41.810 1.00 20.05 ? 149 ARG   B C    1 
ATOM   4814 O O    . ARG   B 1 169 ? 3.122   26.305 42.718 1.00 21.82 ? 149 ARG   B O    1 
ATOM   4815 C CB   . ARG   B 1 169 ? 4.140   25.346 39.733 1.00 23.82 ? 149 ARG   B CB   1 
ATOM   4816 C CG   . ARG   B 1 169 ? 5.415   24.808 39.164 1.00 26.77 ? 149 ARG   B CG   1 
ATOM   4817 C CD   . ARG   B 1 169 ? 5.823   25.548 37.897 1.00 31.30 ? 149 ARG   B CD   1 
ATOM   4818 N NE   . ARG   B 1 169 ? 7.145   25.098 37.506 1.00 37.75 ? 149 ARG   B NE   1 
ATOM   4819 C CZ   . ARG   B 1 169 ? 7.377   24.109 36.659 1.00 40.35 ? 149 ARG   B CZ   1 
ATOM   4820 N NH1  . ARG   B 1 169 ? 6.393   23.528 35.988 1.00 41.52 ? 149 ARG   B NH1  1 
ATOM   4821 N NH2  . ARG   B 1 169 ? 8.627   23.703 36.477 1.00 41.48 ? 149 ARG   B NH2  1 
ATOM   4822 H H    . ARG   B 1 169 ? 3.272   23.093 40.020 1.00 23.32 ? 149 ARG   B H    1 
ATOM   4823 H HA   . ARG   B 1 169 ? 4.569   24.655 41.606 1.00 25.24 ? 149 ARG   B HA   1 
ATOM   4824 H HB2  . ARG   B 1 169 ? 3.431   25.180 39.092 1.00 28.58 ? 149 ARG   B HB2  1 
ATOM   4825 H HB3  . ARG   B 1 169 ? 4.250   26.301 39.866 1.00 28.58 ? 149 ARG   B HB3  1 
ATOM   4826 H HG2  . ARG   B 1 169 ? 6.125   24.909 39.817 1.00 32.12 ? 149 ARG   B HG2  1 
ATOM   4827 H HG3  . ARG   B 1 169 ? 5.297   23.871 38.944 1.00 32.12 ? 149 ARG   B HG3  1 
ATOM   4828 H HD2  . ARG   B 1 169 ? 5.197   25.353 37.182 1.00 37.56 ? 149 ARG   B HD2  1 
ATOM   4829 H HD3  . ARG   B 1 169 ? 5.848   26.503 38.064 1.00 37.56 ? 149 ARG   B HD3  1 
ATOM   4830 H HE   . ARG   B 1 169 ? 7.824   25.502 37.847 1.00 45.30 ? 149 ARG   B HE   1 
ATOM   4831 H HH11 . ARG   B 1 169 ? 5.582   23.792 36.099 1.00 49.83 ? 149 ARG   B HH11 1 
ATOM   4832 H HH12 . ARG   B 1 169 ? 6.565   22.886 35.442 1.00 49.83 ? 149 ARG   B HH12 1 
ATOM   4833 H HH21 . ARG   B 1 169 ? 9.269   24.081 36.907 1.00 49.78 ? 149 ARG   B HH21 1 
ATOM   4834 H HH22 . ARG   B 1 169 ? 8.795   23.061 35.930 1.00 49.78 ? 149 ARG   B HH22 1 
ATOM   4835 N N    . SER   B 1 170 ? 1.474   25.431 41.469 1.00 19.77 ? 150 SER   B N    1 
ATOM   4836 C CA   . SER   B 1 170 ? 0.477   26.254 42.123 1.00 20.22 ? 150 SER   B CA   1 
ATOM   4837 C C    . SER   B 1 170 ? 0.336   25.927 43.601 1.00 19.48 ? 150 SER   B C    1 
ATOM   4838 O O    . SER   B 1 170 ? -0.141  26.778 44.352 1.00 21.15 ? 150 SER   B O    1 
ATOM   4839 C CB   . SER   B 1 170 ? -0.899  26.093 41.452 1.00 20.64 ? 150 SER   B CB   1 
ATOM   4840 O OG   . SER   B 1 170 ? -1.573  24.864 41.773 1.00 20.66 ? 150 SER   B OG   1 
ATOM   4841 H H    . SER   B 1 170 ? 1.168   24.890 40.874 1.00 23.73 ? 150 SER   B H    1 
ATOM   4842 H HA   . SER   B 1 170 ? 0.755   27.179 42.028 1.00 24.26 ? 150 SER   B HA   1 
ATOM   4843 H HB2  . SER   B 1 170 ? -1.462  26.830 41.737 1.00 24.77 ? 150 SER   B HB2  1 
ATOM   4844 H HB3  . SER   B 1 170 ? -0.772  26.126 40.491 1.00 24.77 ? 150 SER   B HB3  1 
ATOM   4845 H HG   . SER   B 1 170 ? -1.095  24.209 41.555 1.00 24.80 ? 150 SER   B HG   1 
ATOM   4846 N N    . LEU   B 1 171 ? 0.710   24.713 44.004 1.00 18.81 ? 151 LEU   B N    1 
ATOM   4847 C CA   . LEU   B 1 171 ? 0.648   24.217 45.370 1.00 19.43 ? 151 LEU   B CA   1 
ATOM   4848 C C    . LEU   B 1 171 ? 1.959   24.402 46.130 1.00 20.85 ? 151 LEU   B C    1 
ATOM   4849 O O    . LEU   B 1 171 ? 2.023   24.019 47.303 1.00 22.74 ? 151 LEU   B O    1 
ATOM   4850 C CB   . LEU   B 1 171 ? 0.261   22.736 45.369 1.00 19.71 ? 151 LEU   B CB   1 
ATOM   4851 C CG   . LEU   B 1 171 ? -1.136  22.419 44.859 1.00 19.59 ? 151 LEU   B CG   1 
ATOM   4852 C CD1  . LEU   B 1 171 ? -1.288  20.936 44.660 1.00 21.47 ? 151 LEU   B CD1  1 
ATOM   4853 C CD2  . LEU   B 1 171 ? -2.177  22.951 45.846 1.00 21.93 ? 151 LEU   B CD2  1 
ATOM   4854 H H    . LEU   B 1 171 ? 1.023   24.121 43.465 1.00 22.57 ? 151 LEU   B H    1 
ATOM   4855 H HA   . LEU   B 1 171 ? -0.040  24.708 45.846 1.00 23.32 ? 151 LEU   B HA   1 
ATOM   4856 H HB2  . LEU   B 1 171 ? 0.889   22.258 44.805 1.00 23.65 ? 151 LEU   B HB2  1 
ATOM   4857 H HB3  . LEU   B 1 171 ? 0.316   22.407 46.280 1.00 23.65 ? 151 LEU   B HB3  1 
ATOM   4858 H HG   . LEU   B 1 171 ? -1.283  22.849 44.002 1.00 23.50 ? 151 LEU   B HG   1 
ATOM   4859 H HD11 . LEU   B 1 171 ? -2.182  20.751 44.333 1.00 25.76 ? 151 LEU   B HD11 1 
ATOM   4860 H HD12 . LEU   B 1 171 ? -0.630  20.634 44.014 1.00 25.76 ? 151 LEU   B HD12 1 
ATOM   4861 H HD13 . LEU   B 1 171 ? -1.147  20.487 45.509 1.00 25.76 ? 151 LEU   B HD13 1 
ATOM   4862 H HD21 . LEU   B 1 171 ? -3.055  22.634 45.581 1.00 26.32 ? 151 LEU   B HD21 1 
ATOM   4863 H HD22 . LEU   B 1 171 ? -1.964  22.628 46.735 1.00 26.32 ? 151 LEU   B HD22 1 
ATOM   4864 H HD23 . LEU   B 1 171 ? -2.158  23.921 45.832 1.00 26.32 ? 151 LEU   B HD23 1 
ATOM   4865 N N    . GLY   B 1 172 ? 2.992   24.975 45.506 1.00 21.13 ? 152 GLY   B N    1 
ATOM   4866 C CA   . GLY   B 1 172 ? 4.283   25.100 46.151 1.00 22.85 ? 152 GLY   B CA   1 
ATOM   4867 C C    . GLY   B 1 172 ? 5.083   23.821 46.229 1.00 23.60 ? 152 GLY   B C    1 
ATOM   4868 O O    . GLY   B 1 172 ? 6.055   23.760 46.981 1.00 25.51 ? 152 GLY   B O    1 
ATOM   4869 H H    . GLY   B 1 172 ? 2.963   25.298 44.710 1.00 25.36 ? 152 GLY   B H    1 
ATOM   4870 H HA2  . GLY   B 1 172 ? 4.813   25.750 45.663 1.00 27.42 ? 152 GLY   B HA2  1 
ATOM   4871 H HA3  . GLY   B 1 172 ? 4.148   25.420 47.057 1.00 27.42 ? 152 GLY   B HA3  1 
ATOM   4872 N N    . ILE   B 1 173 ? 4.705   22.801 45.458 1.00 22.55 ? 153 ILE   B N    1 
ATOM   4873 C CA   . ILE   B 1 173 ? 5.405   21.526 45.414 1.00 22.42 ? 153 ILE   B CA   1 
ATOM   4874 C C    . ILE   B 1 173 ? 6.529   21.617 44.388 1.00 22.78 ? 153 ILE   B C    1 
ATOM   4875 O O    . ILE   B 1 173 ? 6.310   22.040 43.244 1.00 23.83 ? 153 ILE   B O    1 
ATOM   4876 C CB   . ILE   B 1 173 ? 4.427   20.406 45.030 1.00 22.41 ? 153 ILE   B CB   1 
ATOM   4877 C CG1  . ILE   B 1 173 ? 3.331   20.263 46.089 1.00 22.12 ? 153 ILE   B CG1  1 
ATOM   4878 C CG2  . ILE   B 1 173 ? 5.159   19.104 44.816 1.00 23.57 ? 153 ILE   B CG2  1 
ATOM   4879 C CD1  . ILE   B 1 173 ? 2.225   19.378 45.680 1.00 22.65 ? 153 ILE   B CD1  1 
ATOM   4880 H H    . ILE   B 1 173 ? 4.022   22.829 44.936 1.00 27.06 ? 153 ILE   B H    1 
ATOM   4881 H HA   . ILE   B 1 173 ? 5.793   21.336 46.282 1.00 26.90 ? 153 ILE   B HA   1 
ATOM   4882 H HB   . ILE   B 1 173 ? 4.003   20.648 44.192 1.00 26.89 ? 153 ILE   B HB   1 
ATOM   4883 H HG12 . ILE   B 1 173 ? 3.723   19.893 46.896 1.00 26.54 ? 153 ILE   B HG12 1 
ATOM   4884 H HG13 . ILE   B 1 173 ? 2.958   21.139 46.272 1.00 26.54 ? 153 ILE   B HG13 1 
ATOM   4885 H HG21 . ILE   B 1 173 ? 4.512   18.384 44.754 1.00 28.29 ? 153 ILE   B HG21 1 
ATOM   4886 H HG22 . ILE   B 1 173 ? 5.671   19.160 43.994 1.00 28.29 ? 153 ILE   B HG22 1 
ATOM   4887 H HG23 . ILE   B 1 173 ? 5.754   18.949 45.567 1.00 28.29 ? 153 ILE   B HG23 1 
ATOM   4888 H HD11 . ILE   B 1 173 ? 1.473   19.517 46.278 1.00 27.18 ? 153 ILE   B HD11 1 
ATOM   4889 H HD12 . ILE   B 1 173 ? 1.968   19.594 44.770 1.00 27.18 ? 153 ILE   B HD12 1 
ATOM   4890 H HD13 . ILE   B 1 173 ? 2.522   18.456 45.731 1.00 27.18 ? 153 ILE   B HD13 1 
ATOM   4891 N N    . GLU   B 1 174 ? 7.741   21.242 44.801 1.00 24.92 ? 154 GLU   B N    1 
ATOM   4892 C CA   . GLU   B 1 174 ? 8.896   21.255 43.912 1.00 26.66 ? 154 GLU   B CA   1 
ATOM   4893 C C    . GLU   B 1 174 ? 8.704   20.298 42.740 1.00 25.96 ? 154 GLU   B C    1 
ATOM   4894 O O    . GLU   B 1 174 ? 8.308   19.142 42.909 1.00 27.05 ? 154 GLU   B O    1 
ATOM   4895 C CB   . GLU   B 1 174 ? 10.128  20.837 44.713 1.00 28.49 ? 154 GLU   B CB   1 
ATOM   4896 H H    . GLU   B 1 174 ? 7.919   20.973 45.598 1.00 29.90 ? 154 GLU   B H    1 
ATOM   4897 H HA   . GLU   B 1 174 ? 9.018   22.147 43.550 1.00 31.99 ? 154 GLU   B HA   1 
ATOM   4898 N N    . VAL   B 1 175 ? 8.983   20.778 41.541 1.00 25.40 ? 155 VAL   B N    1 
ATOM   4899 C CA   . VAL   B 1 175 ? 8.876   19.969 40.329 1.00 25.62 ? 155 VAL   B CA   1 
ATOM   4900 C C    . VAL   B 1 175 ? 10.268  19.454 39.987 1.00 26.02 ? 155 VAL   B C    1 
ATOM   4901 O O    . VAL   B 1 175 ? 11.189  20.262 39.878 1.00 25.56 ? 155 VAL   B O    1 
ATOM   4902 C CB   . VAL   B 1 175 ? 8.317   20.794 39.156 1.00 27.85 ? 155 VAL   B CB   1 
ATOM   4903 C CG1  . VAL   B 1 175 ? 8.242   19.955 37.878 1.00 28.14 ? 155 VAL   B CG1  1 
ATOM   4904 C CG2  . VAL   B 1 175 ? 6.943   21.325 39.528 1.00 30.87 ? 155 VAL   B CG2  1 
ATOM   4905 H H    . VAL   B 1 175 ? 9.241   21.586 41.397 1.00 30.48 ? 155 VAL   B H    1 
ATOM   4906 H HA   . VAL   B 1 175 ? 8.289   19.215 40.491 1.00 30.75 ? 155 VAL   B HA   1 
ATOM   4907 H HB   . VAL   B 1 175 ? 8.911   21.540 38.978 1.00 33.42 ? 155 VAL   B HB   1 
ATOM   4908 H HG11 . VAL   B 1 175 ? 7.710   20.429 37.220 1.00 33.78 ? 155 VAL   B HG11 1 
ATOM   4909 H HG12 . VAL   B 1 175 ? 9.140   19.815 37.539 1.00 33.78 ? 155 VAL   B HG12 1 
ATOM   4910 H HG13 . VAL   B 1 175 ? 7.829   19.102 38.084 1.00 33.78 ? 155 VAL   B HG13 1 
ATOM   4911 H HG21 . VAL   B 1 175 ? 6.562   21.779 38.761 1.00 37.04 ? 155 VAL   B HG21 1 
ATOM   4912 H HG22 . VAL   B 1 175 ? 6.377   20.581 39.788 1.00 37.04 ? 155 VAL   B HG22 1 
ATOM   4913 H HG23 . VAL   B 1 175 ? 7.034   21.945 40.268 1.00 37.04 ? 155 VAL   B HG23 1 
ATOM   4914 N N    . PRO   B 1 176 ? 10.460  18.152 39.774 1.00 30.32 ? 156 PRO   B N    1 
ATOM   4915 C CA   . PRO   B 1 176 ? 11.790  17.689 39.363 1.00 32.87 ? 156 PRO   B CA   1 
ATOM   4916 C C    . PRO   B 1 176 ? 12.143  18.240 37.998 1.00 30.77 ? 156 PRO   B C    1 
ATOM   4917 O O    . PRO   B 1 176 ? 11.278  18.559 37.172 1.00 27.61 ? 156 PRO   B O    1 
ATOM   4918 C CB   . PRO   B 1 176 ? 11.655  16.163 39.319 1.00 37.61 ? 156 PRO   B CB   1 
ATOM   4919 C CG   . PRO   B 1 176 ? 10.243  15.921 39.112 1.00 37.33 ? 156 PRO   B CG   1 
ATOM   4920 C CD   . PRO   B 1 176 ? 9.504   17.025 39.846 1.00 33.47 ? 156 PRO   B CD   1 
ATOM   4921 H HA   . PRO   B 1 176 ? 12.463  17.931 40.017 1.00 39.45 ? 156 PRO   B HA   1 
ATOM   4922 H HB2  . PRO   B 1 176 ? 12.179  15.806 38.585 1.00 45.14 ? 156 PRO   B HB2  1 
ATOM   4923 H HB3  . PRO   B 1 176 ? 11.954  15.780 40.158 1.00 45.14 ? 156 PRO   B HB3  1 
ATOM   4924 H HG2  . PRO   B 1 176 ? 10.044  15.949 38.164 1.00 44.79 ? 156 PRO   B HG2  1 
ATOM   4925 H HG3  . PRO   B 1 176 ? 10.006  15.053 39.475 1.00 44.79 ? 156 PRO   B HG3  1 
ATOM   4926 H HD2  . PRO   B 1 176 ? 8.672   17.245 39.399 1.00 40.17 ? 156 PRO   B HD2  1 
ATOM   4927 H HD3  . PRO   B 1 176 ? 9.330   16.776 40.767 1.00 40.17 ? 156 PRO   B HD3  1 
ATOM   4928 N N    . GLU   B 1 177 ? 13.445  18.363 37.780 1.00 34.40 ? 157 GLU   B N    1 
ATOM   4929 C CA   . GLU   B 1 177 ? 13.970  18.927 36.550 1.00 36.45 ? 157 GLU   B CA   1 
ATOM   4930 C C    . GLU   B 1 177 ? 14.744  17.833 35.846 1.00 34.29 ? 157 GLU   B C    1 
ATOM   4931 O O    . GLU   B 1 177 ? 15.747  17.347 36.371 1.00 35.32 ? 157 GLU   B O    1 
ATOM   4932 C CB   . GLU   B 1 177 ? 14.870  20.132 36.841 1.00 44.70 ? 157 GLU   B CB   1 
ATOM   4933 C CG   . GLU   B 1 177 ? 15.380  20.847 35.580 1.00 51.03 ? 157 GLU   B CG   1 
ATOM   4934 C CD   . GLU   B 1 177 ? 16.629  21.688 35.824 1.00 57.19 ? 157 GLU   B CD   1 
ATOM   4935 O OE1  . GLU   B 1 177 ? 16.824  22.170 36.959 1.00 59.23 ? 157 GLU   B OE1  1 
ATOM   4936 O OE2  . GLU   B 1 177 ? 17.426  21.851 34.874 1.00 59.59 ? 157 GLU   B OE2  1 
ATOM   4937 H H    . GLU   B 1 177 ? 14.051  18.122 38.340 1.00 41.28 ? 157 GLU   B H    1 
ATOM   4938 H HA   . GLU   B 1 177 ? 13.247  19.228 35.977 1.00 43.74 ? 157 GLU   B HA   1 
ATOM   4939 H HB2  . GLU   B 1 177 ? 14.368  20.777 37.364 1.00 53.64 ? 157 GLU   B HB2  1 
ATOM   4940 H HB3  . GLU   B 1 177 ? 15.643  19.829 37.342 1.00 53.64 ? 157 GLU   B HB3  1 
ATOM   4941 H HG2  . GLU   B 1 177 ? 15.596  20.181 34.908 1.00 61.24 ? 157 GLU   B HG2  1 
ATOM   4942 H HG3  . GLU   B 1 177 ? 14.684  21.436 35.251 1.00 61.24 ? 157 GLU   B HG3  1 
ATOM   4943 N N    . VAL   B 1 178 ? 14.295  17.468 34.651 1.00 28.94 ? 158 VAL   B N    1 
ATOM   4944 C CA   . VAL   B 1 178 ? 15.056  16.550 33.810 1.00 26.45 ? 158 VAL   B CA   1 
ATOM   4945 C C    . VAL   B 1 178 ? 16.333  17.244 33.349 1.00 26.19 ? 158 VAL   B C    1 
ATOM   4946 O O    . VAL   B 1 178 ? 16.302  18.380 32.855 1.00 29.17 ? 158 VAL   B O    1 
ATOM   4947 C CB   . VAL   B 1 178 ? 14.197  16.129 32.608 1.00 27.98 ? 158 VAL   B CB   1 
ATOM   4948 C CG1  . VAL   B 1 178 ? 14.960  15.249 31.662 1.00 29.29 ? 158 VAL   B CG1  1 
ATOM   4949 C CG2  . VAL   B 1 178 ? 12.928  15.392 33.067 1.00 29.26 ? 158 VAL   B CG2  1 
ATOM   4950 H H    . VAL   B 1 178 ? 13.555  17.736 34.304 1.00 34.73 ? 158 VAL   B H    1 
ATOM   4951 H HA   . VAL   B 1 178 ? 15.301  15.761 34.317 1.00 31.74 ? 158 VAL   B HA   1 
ATOM   4952 H HB   . VAL   B 1 178 ? 13.945  16.941 32.141 1.00 33.57 ? 158 VAL   B HB   1 
ATOM   4953 H HG11 . VAL   B 1 178 ? 14.339  14.853 31.030 1.00 35.15 ? 158 VAL   B HG11 1 
ATOM   4954 H HG12 . VAL   B 1 178 ? 15.615  15.786 31.190 1.00 35.15 ? 158 VAL   B HG12 1 
ATOM   4955 H HG13 . VAL   B 1 178 ? 15.405  14.552 32.168 1.00 35.15 ? 158 VAL   B HG13 1 
ATOM   4956 H HG21 . VAL   B 1 178 ? 12.427  15.111 32.285 1.00 35.11 ? 158 VAL   B HG21 1 
ATOM   4957 H HG22 . VAL   B 1 178 ? 13.185  14.618 33.591 1.00 35.11 ? 158 VAL   B HG22 1 
ATOM   4958 H HG23 . VAL   B 1 178 ? 12.390  15.993 33.605 1.00 35.11 ? 158 VAL   B HG23 1 
ATOM   4959 N N    . ARG   B 1 179 ? 17.465  16.564 33.487 1.00 24.74 ? 159 ARG   B N    1 
ATOM   4960 C CA   . ARG   B 1 179 ? 18.731  17.140 33.064 1.00 26.64 ? 159 ARG   B CA   1 
ATOM   4961 C C    . ARG   B 1 179 ? 18.800  17.081 31.542 1.00 25.60 ? 159 ARG   B C    1 
ATOM   4962 O O    . ARG   B 1 179 ? 18.641  16.010 30.954 1.00 27.79 ? 159 ARG   B O    1 
ATOM   4963 C CB   . ARG   B 1 179 ? 19.896  16.358 33.663 1.00 28.31 ? 159 ARG   B CB   1 
ATOM   4964 C CG   . ARG   B 1 179 ? 20.005  16.415 35.176 1.00 31.12 ? 159 ARG   B CG   1 
ATOM   4965 C CD   . ARG   B 1 179 ? 21.285  15.692 35.638 1.00 34.44 ? 159 ARG   B CD   1 
ATOM   4966 N NE   . ARG   B 1 179 ? 21.248  14.258 35.341 1.00 35.80 ? 159 ARG   B NE   1 
ATOM   4967 C CZ   . ARG   B 1 179 ? 20.736  13.342 36.157 1.00 38.02 ? 159 ARG   B CZ   1 
ATOM   4968 N NH1  . ARG   B 1 179 ? 20.186  13.678 37.318 1.00 38.58 ? 159 ARG   B NH1  1 
ATOM   4969 N NH2  . ARG   B 1 179 ? 20.783  12.060 35.807 1.00 40.72 ? 159 ARG   B NH2  1 
ATOM   4970 H H    . ARG   B 1 179 ? 17.524  15.774 33.820 1.00 29.70 ? 159 ARG   B H    1 
ATOM   4971 H HA   . ARG   B 1 179 ? 18.801  18.060 33.363 1.00 31.97 ? 159 ARG   B HA   1 
ATOM   4972 H HB2  . ARG   B 1 179 ? 19.799  15.425 33.415 1.00 33.98 ? 159 ARG   B HB2  1 
ATOM   4973 H HB3  . ARG   B 1 179 ? 20.722  16.714 33.300 1.00 33.98 ? 159 ARG   B HB3  1 
ATOM   4974 H HG2  . ARG   B 1 179 ? 20.048  17.339 35.466 1.00 37.35 ? 159 ARG   B HG2  1 
ATOM   4975 H HG3  . ARG   B 1 179 ? 19.238  15.977 35.576 1.00 37.35 ? 159 ARG   B HG3  1 
ATOM   4976 H HD2  . ARG   B 1 179 ? 22.050  16.075 35.181 1.00 41.33 ? 159 ARG   B HD2  1 
ATOM   4977 H HD3  . ARG   B 1 179 ? 21.382  15.799 36.597 1.00 41.33 ? 159 ARG   B HD3  1 
ATOM   4978 H HE   . ARG   B 1 179 ? 21.580  13.993 34.593 1.00 42.96 ? 159 ARG   B HE   1 
ATOM   4979 H HH11 . ARG   B 1 179 ? 20.157  14.504 37.557 1.00 46.30 ? 159 ARG   B HH11 1 
ATOM   4980 H HH12 . ARG   B 1 179 ? 19.860  13.070 37.832 1.00 46.30 ? 159 ARG   B HH12 1 
ATOM   4981 H HH21 . ARG   B 1 179 ? 21.143  11.831 35.060 1.00 48.86 ? 159 ARG   B HH21 1 
ATOM   4982 H HH22 . ARG   B 1 179 ? 20.454  11.460 36.327 1.00 48.86 ? 159 ARG   B HH22 1 
ATOM   4983 N N    . ARG   B 1 180 ? 19.063  18.217 30.901 1.00 26.50 ? 160 ARG   B N    1 
ATOM   4984 C CA   . ARG   B 1 180 ? 19.039  18.301 29.443 1.00 28.50 ? 160 ARG   B CA   1 
ATOM   4985 C C    . ARG   B 1 180 ? 20.426  18.489 28.830 1.00 28.38 ? 160 ARG   B C    1 
ATOM   4986 O O    . ARG   B 1 180 ? 20.548  18.704 27.612 1.00 28.48 ? 160 ARG   B O    1 
ATOM   4987 C CB   . ARG   B 1 180 ? 18.089  19.420 29.009 1.00 29.17 ? 160 ARG   B CB   1 
ATOM   4988 C CG   . ARG   B 1 180 ? 16.676  19.267 29.604 1.00 31.02 ? 160 ARG   B CG   1 
ATOM   4989 C CD   . ARG   B 1 180 ? 15.656  20.064 28.856 1.00 31.15 ? 160 ARG   B CD   1 
ATOM   4990 N NE   . ARG   B 1 180 ? 14.394  20.120 29.576 1.00 28.85 ? 160 ARG   B NE   1 
ATOM   4991 C CZ   . ARG   B 1 180 ? 13.364  20.844 29.176 1.00 29.97 ? 160 ARG   B CZ   1 
ATOM   4992 N NH1  . ARG   B 1 180 ? 13.408  21.530 28.048 1.00 32.60 ? 160 ARG   B NH1  1 
ATOM   4993 N NH2  . ARG   B 1 180 ? 12.271  20.884 29.922 1.00 30.26 ? 160 ARG   B NH2  1 
ATOM   4994 H H    . ARG   B 1 180 ? 19.258  18.958 31.291 1.00 31.80 ? 160 ARG   B H    1 
ATOM   4995 H HA   . ARG   B 1 180 ? 18.695  17.466 29.089 1.00 34.20 ? 160 ARG   B HA   1 
ATOM   4996 H HB2  . ARG   B 1 180 ? 18.448  20.271 29.303 1.00 35.00 ? 160 ARG   B HB2  1 
ATOM   4997 H HB3  . ARG   B 1 180 ? 18.010  19.410 28.042 1.00 35.00 ? 160 ARG   B HB3  1 
ATOM   4998 H HG2  . ARG   B 1 180 ? 16.414  18.334 29.568 1.00 37.22 ? 160 ARG   B HG2  1 
ATOM   4999 H HG3  . ARG   B 1 180 ? 16.683  19.575 30.524 1.00 37.22 ? 160 ARG   B HG3  1 
ATOM   5000 H HD2  . ARG   B 1 180 ? 15.980  20.970 28.736 1.00 37.38 ? 160 ARG   B HD2  1 
ATOM   5001 H HD3  . ARG   B 1 180 ? 15.496  19.651 27.992 1.00 37.38 ? 160 ARG   B HD3  1 
ATOM   5002 H HE   . ARG   B 1 180 ? 14.315  19.660 30.298 1.00 34.62 ? 160 ARG   B HE   1 
ATOM   5003 H HH11 . ARG   B 1 180 ? 14.115  21.510 27.560 1.00 39.12 ? 160 ARG   B HH11 1 
ATOM   5004 H HH12 . ARG   B 1 180 ? 12.728  21.997 27.802 1.00 39.12 ? 160 ARG   B HH12 1 
ATOM   5005 H HH21 . ARG   B 1 180 ? 12.237  20.441 30.659 1.00 36.31 ? 160 ARG   B HH21 1 
ATOM   5006 H HH22 . ARG   B 1 180 ? 11.595  21.352 29.671 1.00 36.31 ? 160 ARG   B HH22 1 
ATOM   5007 N N    . ASP   B 1 181 ? 21.478  18.403 29.636 1.00 29.96 ? 161 ASP   B N    1 
ATOM   5008 C CA   . ASP   B 1 181 ? 22.813  18.706 29.125 1.00 30.04 ? 161 ASP   B CA   1 
ATOM   5009 C C    . ASP   B 1 181 ? 23.199  17.810 27.956 1.00 29.08 ? 161 ASP   B C    1 
ATOM   5010 O O    . ASP   B 1 181 ? 23.930  18.238 27.039 1.00 30.30 ? 161 ASP   B O    1 
ATOM   5011 C CB   . ASP   B 1 181 ? 23.818  18.537 30.264 1.00 33.00 ? 161 ASP   B CB   1 
ATOM   5012 C CG   . ASP   B 1 181 ? 23.456  19.384 31.446 1.00 38.44 ? 161 ASP   B CG   1 
ATOM   5013 O OD1  . ASP   B 1 181 ? 23.835  20.574 31.413 1.00 40.92 ? 161 ASP   B OD1  1 
ATOM   5014 O OD2  . ASP   B 1 181 ? 22.720  18.889 32.346 1.00 37.76 ? 161 ASP   B OD2  1 
ATOM   5015 H H    . ASP   B 1 181 ? 21.450  18.176 30.465 1.00 35.96 ? 161 ASP   B H    1 
ATOM   5016 H HA   . ASP   B 1 181 ? 22.827  19.621 28.804 1.00 36.05 ? 161 ASP   B HA   1 
ATOM   5017 H HB2  . ASP   B 1 181 ? 23.830  17.609 30.546 1.00 39.60 ? 161 ASP   B HB2  1 
ATOM   5018 H HB3  . ASP   B 1 181 ? 24.698  18.803 29.956 1.00 39.60 ? 161 ASP   B HB3  1 
ATOM   5019 N N    . GLY   B 1 182 ? 22.777  16.550 27.995 1.00 27.47 ? 162 GLY   B N    1 
ATOM   5020 C CA   . GLY   B 1 182 ? 23.199  15.606 26.986 1.00 27.22 ? 162 GLY   B CA   1 
ATOM   5021 C C    . GLY   B 1 182 ? 22.365  15.645 25.735 1.00 28.03 ? 162 GLY   B C    1 
ATOM   5022 O O    . GLY   B 1 182 ? 22.618  14.845 24.823 1.00 28.48 ? 162 GLY   B O    1 
ATOM   5023 H H    . GLY   B 1 182 ? 22.251  16.227 28.594 1.00 32.97 ? 162 GLY   B H    1 
ATOM   5024 H HA2  . GLY   B 1 182 ? 24.118  15.797 26.740 1.00 32.66 ? 162 GLY   B HA2  1 
ATOM   5025 H HA3  . GLY   B 1 182 ? 23.149  14.709 27.352 1.00 32.66 ? 162 GLY   B HA3  1 
ATOM   5026 N N    . LEU   B 1 183 ? 21.355  16.575 25.668 1.00 29.21 ? 163 LEU   B N    1 
ATOM   5027 C CA   . LEU   B 1 183 ? 20.407  16.670 24.575 1.00 29.29 ? 163 LEU   B CA   1 
ATOM   5028 C C    . LEU   B 1 183 ? 20.728  17.862 23.686 1.00 33.62 ? 163 LEU   B C    1 
ATOM   5029 O O    . LEU   B 1 183 ? 21.245  18.867 24.170 1.00 35.91 ? 163 LEU   B O    1 
ATOM   5030 C CB   . LEU   B 1 183 ? 18.990  16.867 25.138 1.00 29.49 ? 163 LEU   B CB   1 
ATOM   5031 C CG   . LEU   B 1 183 ? 18.539  15.865 26.201 1.00 33.41 ? 163 LEU   B CG   1 
ATOM   5032 C CD1  . LEU   B 1 183 ? 17.208  16.274 26.883 1.00 42.61 ? 163 LEU   B CD1  1 
ATOM   5033 C CD2  . LEU   B 1 183 ? 18.428  14.478 25.585 1.00 43.76 ? 163 LEU   B CD2  1 
ATOM   5034 H H    . LEU   B 1 183 ? 21.218  17.167 26.277 1.00 35.05 ? 163 LEU   B H    1 
ATOM   5035 H HA   . LEU   B 1 183 ? 20.442  15.864 24.037 1.00 35.15 ? 163 LEU   B HA   1 
ATOM   5036 H HB2  . LEU   B 1 183 ? 18.944  17.749 25.539 1.00 35.39 ? 163 LEU   B HB2  1 
ATOM   5037 H HB3  . LEU   B 1 183 ? 18.362  16.805 24.401 1.00 35.39 ? 163 LEU   B HB3  1 
ATOM   5038 H HG   . LEU   B 1 183 ? 19.206  15.850 26.905 1.00 40.10 ? 163 LEU   B HG   1 
ATOM   5039 H HD11 . LEU   B 1 183 ? 17.088  15.741 27.685 1.00 51.14 ? 163 LEU   B HD11 1 
ATOM   5040 H HD12 . LEU   B 1 183 ? 17.248  17.215 27.114 1.00 51.14 ? 163 LEU   B HD12 1 
ATOM   5041 H HD13 . LEU   B 1 183 ? 16.476  16.116 26.267 1.00 51.14 ? 163 LEU   B HD13 1 
ATOM   5042 H HD21 . LEU   B 1 183 ? 18.067  13.866 26.245 1.00 52.51 ? 163 LEU   B HD21 1 
ATOM   5043 H HD22 . LEU   B 1 183 ? 17.839  14.520 24.816 1.00 52.51 ? 163 LEU   B HD22 1 
ATOM   5044 H HD23 . LEU   B 1 183 ? 19.311  14.184 25.309 1.00 52.51 ? 163 LEU   B HD23 1 
ATOM   5045 N N    . PRO   B 1 184 ? 20.403  17.804 22.390 1.00 39.54 ? 164 PRO   B N    1 
ATOM   5046 C CA   . PRO   B 1 184 ? 20.596  18.959 21.506 1.00 43.11 ? 164 PRO   B CA   1 
ATOM   5047 C C    . PRO   B 1 184 ? 19.856  20.198 21.983 1.00 43.86 ? 164 PRO   B C    1 
ATOM   5048 O O    . PRO   B 1 184 ? 18.731  20.023 22.456 1.00 45.89 ? 164 PRO   B O    1 
ATOM   5049 C CB   . PRO   B 1 184 ? 19.999  18.483 20.175 1.00 44.57 ? 164 PRO   B CB   1 
ATOM   5050 C CG   . PRO   B 1 184 ? 20.035  16.999 20.244 1.00 46.01 ? 164 PRO   B CG   1 
ATOM   5051 C CD   . PRO   B 1 184 ? 19.806  16.660 21.684 1.00 44.20 ? 164 PRO   B CD   1 
ATOM   5052 H HA   . PRO   B 1 184 ? 21.541  19.155 21.405 1.00 51.73 ? 164 PRO   B HA   1 
ATOM   5053 H HB2  . PRO   B 1 184 ? 19.088  18.805 20.089 1.00 53.49 ? 164 PRO   B HB2  1 
ATOM   5054 H HB3  . PRO   B 1 184 ? 20.537  18.809 19.437 1.00 53.49 ? 164 PRO   B HB3  1 
ATOM   5055 H HG2  . PRO   B 1 184 ? 19.333  16.627 19.686 1.00 55.21 ? 164 PRO   B HG2  1 
ATOM   5056 H HG3  . PRO   B 1 184 ? 20.900  16.677 19.946 1.00 55.21 ? 164 PRO   B HG3  1 
ATOM   5057 H HD2  . PRO   B 1 184 ? 18.858  16.589 21.877 1.00 53.04 ? 164 PRO   B HD2  1 
ATOM   5058 H HD3  . PRO   B 1 184 ? 20.256  15.833 21.921 1.00 53.04 ? 164 PRO   B HD3  1 
HETATM 5059 C C10  A A1IAD C 2 .   ? 11.153  16.473 23.557 0.55 40.20 ? 201 A1IAD A C10  1 
HETATM 5060 C C10  B A1IAD C 2 .   ? 10.980  16.186 23.599 0.45 15.32 ? 201 A1IAD A C10  1 
HETATM 5061 C C15  A A1IAD C 2 .   ? 13.393  16.692 26.131 0.55 23.87 ? 201 A1IAD A C15  1 
HETATM 5062 C C15  B A1IAD C 2 .   ? 13.259  15.886 25.776 0.45 23.15 ? 201 A1IAD A C15  1 
HETATM 5063 C C11  A A1IAD C 2 .   ? 11.077  15.150 23.985 0.55 40.22 ? 201 A1IAD A C11  1 
HETATM 5064 C C11  B A1IAD C 2 .   ? 10.942  14.820 23.850 0.45 16.28 ? 201 A1IAD A C11  1 
HETATM 5065 C C12  A A1IAD C 2 .   ? 11.700  14.812 25.360 0.55 23.04 ? 201 A1IAD A C12  1 
HETATM 5066 C C12  B A1IAD C 2 .   ? 11.406  14.291 25.190 0.45 20.40 ? 201 A1IAD A C12  1 
HETATM 5067 C C14  A A1IAD C 2 .   ? 12.293  15.860 26.327 0.55 35.27 ? 201 A1IAD A C14  1 
HETATM 5068 C C14  B A1IAD C 2 .   ? 12.073  15.283 26.121 0.45 15.97 ? 201 A1IAD A C14  1 
HETATM 5069 C C01  A A1IAD C 2 .   ? 9.067   10.092 23.728 0.55 24.13 ? 201 A1IAD A C01  1 
HETATM 5070 C C01  B A1IAD C 2 .   ? 9.849   9.318  21.379 0.45 58.97 ? 201 A1IAD A C01  1 
HETATM 5071 C C02  A A1IAD C 2 .   ? 9.330   10.716 22.362 0.55 61.55 ? 201 A1IAD A C02  1 
HETATM 5072 C C02  B A1IAD C 2 .   ? 9.773   10.239 22.590 0.45 22.74 ? 201 A1IAD A C02  1 
HETATM 5073 C C03  A A1IAD C 2 .   ? 9.625   9.617  21.323 0.55 28.88 ? 201 A1IAD A C03  1 
HETATM 5074 C C03  B A1IAD C 2 .   ? 8.537   9.944  23.446 0.45 46.36 ? 201 A1IAD A C03  1 
HETATM 5075 C C04  A A1IAD C 2 .   ? 10.458  11.752 22.427 0.55 49.40 ? 201 A1IAD A C04  1 
HETATM 5076 C C04  B A1IAD C 2 .   ? 9.763   11.691 22.138 0.45 26.37 ? 201 A1IAD A C04  1 
HETATM 5077 C C06  A A1IAD C 2 .   ? 10.427  14.217 23.135 0.55 39.50 ? 201 A1IAD A C06  1 
HETATM 5078 C C06  B A1IAD C 2 .   ? 10.426  13.959 22.898 0.45 20.11 ? 201 A1IAD A C06  1 
HETATM 5079 C C07  A A1IAD C 2 .   ? 9.888   14.636 21.919 0.55 49.40 ? 201 A1IAD A C07  1 
HETATM 5080 C C07  B A1IAD C 2 .   ? 9.999   14.432 21.679 0.45 16.75 ? 201 A1IAD A C07  1 
HETATM 5081 C C08  A A1IAD C 2 .   ? 9.980   15.951 21.514 0.55 47.40 ? 201 A1IAD A C08  1 
HETATM 5082 C C08  B A1IAD C 2 .   ? 10.047  15.789 21.449 0.45 17.39 ? 201 A1IAD A C08  1 
HETATM 5083 C C09  A A1IAD C 2 .   ? 10.618  16.865 22.332 0.55 32.24 ? 201 A1IAD A C09  1 
HETATM 5084 C C09  B A1IAD C 2 .   ? 10.550  16.659 22.376 0.45 19.30 ? 201 A1IAD A C09  1 
HETATM 5085 C C16  A A1IAD C 2 .   ? 14.222  16.834 25.014 0.55 24.57 ? 201 A1IAD A C16  1 
HETATM 5086 C C16  B A1IAD C 2 .   ? 14.038  15.787 24.642 0.45 28.52 ? 201 A1IAD A C16  1 
HETATM 5087 C C17  A A1IAD C 2 .   ? 14.482  15.835 24.079 0.55 20.94 ? 201 A1IAD A C17  1 
HETATM 5088 C C17  B A1IAD C 2 .   ? 14.508  14.559 24.221 0.45 46.65 ? 201 A1IAD A C17  1 
HETATM 5089 C C18  A A1IAD C 2 .   ? 15.367  16.100 23.015 0.55 24.24 ? 201 A1IAD A C18  1 
HETATM 5090 C C18  B A1IAD C 2 .   ? 15.293  14.482 23.090 0.45 51.59 ? 201 A1IAD A C18  1 
HETATM 5091 C C19  A A1IAD C 2 .   ? 15.923  17.364 22.893 0.55 32.20 ? 201 A1IAD A C19  1 
HETATM 5092 C C19  B A1IAD C 2 .   ? 15.602  15.628 22.379 0.45 37.28 ? 201 A1IAD A C19  1 
HETATM 5093 C C21  A A1IAD C 2 .   ? 15.649  18.354 23.814 0.55 34.58 ? 201 A1IAD A C21  1 
HETATM 5094 C C21  B A1IAD C 2 .   ? 15.131  16.869 22.791 0.45 34.92 ? 201 A1IAD A C21  1 
HETATM 5095 C C22  A A1IAD C 2 .   ? 14.794  18.086 24.862 0.55 30.37 ? 201 A1IAD A C22  1 
HETATM 5096 C C22  B A1IAD C 2 .   ? 14.352  16.949 23.942 0.45 24.54 ? 201 A1IAD A C22  1 
HETATM 5097 C C24  A A1IAD C 2 .   ? 12.260  16.887 28.461 0.55 24.69 ? 201 A1IAD A C24  1 
HETATM 5098 C C24  B A1IAD C 2 .   ? 12.275  16.551 28.105 0.45 17.49 ? 201 A1IAD A C24  1 
HETATM 5099 C C25  A A1IAD C 2 .   ? 11.717  17.069 29.735 0.55 38.87 ? 201 A1IAD A C25  1 
HETATM 5100 C C25  B A1IAD C 2 .   ? 11.864  16.996 29.379 0.45 17.69 ? 201 A1IAD A C25  1 
HETATM 5101 C C26  A A1IAD C 2 .   ? 10.603  16.328 30.135 0.55 35.02 ? 201 A1IAD A C26  1 
HETATM 5102 C C26  B A1IAD C 2 .   ? 10.673  16.512 29.931 0.45 18.06 ? 201 A1IAD A C26  1 
HETATM 5103 C C28  A A1IAD C 2 .   ? 10.033  15.398 29.273 0.55 26.20 ? 201 A1IAD A C28  1 
HETATM 5104 C C28  B A1IAD C 2 .   ? 9.929   15.586 29.229 0.45 21.12 ? 201 A1IAD A C28  1 
HETATM 5105 C C29  A A1IAD C 2 .   ? 10.569  15.209 28.015 0.55 34.34 ? 201 A1IAD A C29  1 
HETATM 5106 C C29  B A1IAD C 2 .   ? 10.355  15.147 27.990 0.45 16.69 ? 201 A1IAD A C29  1 
HETATM 5107 C C30  A A1IAD C 2 .   ? 11.706  15.965 27.604 0.55 27.32 ? 201 A1IAD A C30  1 
HETATM 5108 C C30  B A1IAD C 2 .   ? 11.561  15.622 27.400 0.45 17.12 ? 201 A1IAD A C30  1 
HETATM 5109 N N05  A A1IAD C 2 .   ? 10.263  12.787 23.451 0.55 41.20 ? 201 A1IAD A N05  1 
HETATM 5110 N N05  B A1IAD C 2 .   ? 10.366  12.536 23.148 0.45 27.70 ? 201 A1IAD A N05  1 
HETATM 5111 O O13  A A1IAD C 2 .   ? 11.761  13.690 25.766 0.55 31.27 ? 201 A1IAD A O13  1 
HETATM 5112 O O13  B A1IAD C 2 .   ? 11.286  13.155 25.500 0.45 22.86 ? 201 A1IAD A O13  1 
HETATM 5113 O O20  A A1IAD C 2 .   ? 16.789  17.650 21.830 0.55 34.36 ? 201 A1IAD A O20  1 
HETATM 5114 O O20  B A1IAD C 2 .   ? 16.400  15.522 21.233 0.45 45.77 ? 201 A1IAD A O20  1 
HETATM 5115 O O27  A A1IAD C 2 .   ? 10.070  16.520 31.412 0.55 44.58 ? 201 A1IAD A O27  1 
HETATM 5116 O O27  B A1IAD C 2 .   ? 10.263  16.943 31.180 0.45 17.80 ? 201 A1IAD A O27  1 
HETATM 5117 S S23  A A1IAD C 2 .   ? 13.622  17.601 27.620 0.55 26.31 ? 201 A1IAD A S23  1 
HETATM 5118 S S23  B A1IAD C 2 .   ? 13.670  16.899 27.094 0.45 22.09 ? 201 A1IAD A S23  1 
HETATM 5119 H H101 A A1IAD C 2 .   ? 11.636  17.209 24.188 0.55 48.24 ? 201 A1IAD A H101 1 
HETATM 5120 H H101 B A1IAD C 2 .   ? 11.342  16.872 24.355 0.45 18.38 ? 201 A1IAD A H101 1 
HETATM 5121 H H011 A A1IAD C 2 .   ? 8.956   9.017  23.619 0.55 28.96 ? 201 A1IAD A H011 1 
HETATM 5122 H H011 B A1IAD C 2 .   ? 9.381   9.802  20.527 0.45 70.76 ? 201 A1IAD A H011 1 
HETATM 5123 H H012 A A1IAD C 2 .   ? 9.901   10.304 24.390 0.55 28.96 ? 201 A1IAD A H012 1 
HETATM 5124 H H012 B A1IAD C 2 .   ? 10.889  9.106  21.150 0.45 70.76 ? 201 A1IAD A H012 1 
HETATM 5125 H H013 A A1IAD C 2 .   ? 8.156   10.509 24.148 0.55 28.96 ? 201 A1IAD A H013 1 
HETATM 5126 H H013 B A1IAD C 2 .   ? 9.330   8.390  21.598 0.45 70.76 ? 201 A1IAD A H013 1 
HETATM 5127 H H021 A A1IAD C 2 .   ? 8.438   11.245 22.050 0.55 73.86 ? 201 A1IAD A H021 1 
HETATM 5128 H H021 B A1IAD C 2 .   ? 10.649  10.059 23.202 0.45 27.29 ? 201 A1IAD A H021 1 
HETATM 5129 H H033 A A1IAD C 2 .   ? 9.841   10.075 20.363 0.55 34.66 ? 201 A1IAD A H033 1 
HETATM 5130 H H033 B A1IAD C 2 .   ? 7.643   10.044 22.838 0.45 55.63 ? 201 A1IAD A H033 1 
HETATM 5131 H H032 A A1IAD C 2 .   ? 10.482  9.033  21.647 0.55 34.66 ? 201 A1IAD A H032 1 
HETATM 5132 H H032 B A1IAD C 2 .   ? 8.599   8.931  23.834 0.45 55.63 ? 201 A1IAD A H032 1 
HETATM 5133 H H031 A A1IAD C 2 .   ? 8.760   8.968  21.227 0.55 34.66 ? 201 A1IAD A H031 1 
HETATM 5134 H H031 B A1IAD C 2 .   ? 8.493   10.647 24.273 0.45 55.63 ? 201 A1IAD A H031 1 
HETATM 5135 H H041 A A1IAD C 2 .   ? 10.532  12.238 21.460 0.55 59.28 ? 201 A1IAD A H041 1 
HETATM 5136 H H041 B A1IAD C 2 .   ? 8.738   12.007 21.970 0.45 31.64 ? 201 A1IAD A H041 1 
HETATM 5137 H H042 A A1IAD C 2 .   ? 11.387  11.233 22.639 0.55 59.28 ? 201 A1IAD A H042 1 
HETATM 5138 H H042 B A1IAD C 2 .   ? 10.322  11.783 21.212 0.45 31.64 ? 201 A1IAD A H042 1 
HETATM 5139 H H071 A A1IAD C 2 .   ? 9.389   13.917 21.283 0.55 59.28 ? 201 A1IAD A H071 1 
HETATM 5140 H H071 B A1IAD C 2 .   ? 9.634   13.754 20.919 0.45 20.10 ? 201 A1IAD A H071 1 
HETATM 5141 H H081 A A1IAD C 2 .   ? 9.557   16.264 20.566 0.55 56.88 ? 201 A1IAD A H081 1 
HETATM 5142 H H081 B A1IAD C 2 .   ? 9.677   16.177 20.507 0.45 20.87 ? 201 A1IAD A H081 1 
HETATM 5143 H H091 A A1IAD C 2 .   ? 10.702  17.898 22.017 0.55 38.69 ? 201 A1IAD A H091 1 
HETATM 5144 H H091 B A1IAD C 2 .   ? 10.610  17.717 22.152 0.45 23.16 ? 201 A1IAD A H091 1 
HETATM 5145 H H171 A A1IAD C 2 .   ? 14.009  14.865 24.170 0.55 25.13 ? 201 A1IAD A H171 1 
HETATM 5146 H H171 B A1IAD C 2 .   ? 14.261  13.662 24.775 0.45 55.98 ? 201 A1IAD A H171 1 
HETATM 5147 H H181 A A1IAD C 2 .   ? 15.611  15.324 22.300 0.55 29.09 ? 201 A1IAD A H181 1 
HETATM 5148 H H181 B A1IAD C 2 .   ? 15.669  13.522 22.757 0.45 61.91 ? 201 A1IAD A H181 1 
HETATM 5149 H H211 A A1IAD C 2 .   ? 16.100  19.332 23.715 0.55 41.49 ? 201 A1IAD A H211 1 
HETATM 5150 H H211 B A1IAD C 2 .   ? 15.366  17.761 22.225 0.45 41.90 ? 201 A1IAD A H211 1 
HETATM 5151 H H221 A A1IAD C 2 .   ? 14.567  18.866 25.577 0.55 36.44 ? 201 A1IAD A H221 1 
HETATM 5152 H H221 B A1IAD C 2 .   ? 13.994  17.909 24.290 0.45 29.45 ? 201 A1IAD A H221 1 
HETATM 5153 H H251 A A1IAD C 2 .   ? 12.161  17.787 30.414 0.55 46.64 ? 201 A1IAD A H251 1 
HETATM 5154 H H251 B A1IAD C 2 .   ? 12.467  17.709 29.927 0.45 21.22 ? 201 A1IAD A H251 1 
HETATM 5155 H H281 A A1IAD C 2 .   ? 9.171   14.822 29.589 0.55 31.44 ? 201 A1IAD A H281 1 
HETATM 5156 H H281 B A1IAD C 2 .   ? 9.007   15.203 29.650 0.45 25.34 ? 201 A1IAD A H281 1 
HETATM 5157 H H291 A A1IAD C 2 .   ? 10.127  14.487 27.340 0.55 41.21 ? 201 A1IAD A H291 1 
HETATM 5158 H H291 B A1IAD C 2 .   ? 9.756   14.421 27.454 0.45 20.03 ? 201 A1IAD A H291 1 
HETATM 5159 H H051 A A1IAD C 2 .   ? 10.013  12.516 24.379 0.55 49.44 ? 201 A1IAD A H051 1 
HETATM 5160 H H051 B A1IAD C 2 .   ? 10.731  12.147 23.992 0.45 33.24 ? 201 A1IAD A H051 1 
HETATM 5161 H H201 A A1IAD C 2 .   ? 16.678  16.993 21.157 0.55 41.23 ? 201 A1IAD A H201 1 
HETATM 5162 H H201 B A1IAD C 2 .   ? 16.984  14.783 21.316 0.45 54.92 ? 201 A1IAD A H201 1 
HETATM 5163 H H271 A A1IAD C 2 .   ? 10.765  16.748 32.009 0.55 53.49 ? 201 A1IAD A H271 1 
HETATM 5164 H H271 B A1IAD C 2 .   ? 10.500  16.305 31.827 0.45 21.36 ? 201 A1IAD A H271 1 
HETATM 5165 C C1   . GOL   D 3 .   ? 5.508   4.593  33.834 1.00 67.29 ? 202 GOL   A C1   1 
HETATM 5166 O O1   . GOL   D 3 .   ? 4.349   4.610  33.036 0.71 55.86 ? 202 GOL   A O1   1 
HETATM 5167 C C2   . GOL   D 3 .   ? 6.600   3.855  33.024 1.00 80.91 ? 202 GOL   A C2   1 
HETATM 5168 O O2   . GOL   D 3 .   ? 6.907   4.542  31.844 0.90 29.19 ? 202 GOL   A O2   1 
HETATM 5169 C C3   . GOL   D 3 .   ? 7.807   3.742  33.995 0.83 71.33 ? 202 GOL   A C3   1 
HETATM 5170 O O3   . GOL   D 3 .   ? 8.482   2.556  33.675 1.00 71.25 ? 202 GOL   A O3   1 
HETATM 5171 H H11  . GOL   D 3 .   ? 5.372   4.139  34.680 1.00 80.75 ? 202 GOL   A H11  1 
HETATM 5172 H H12  . GOL   D 3 .   ? 5.820   5.484  34.058 1.00 80.75 ? 202 GOL   A H12  1 
HETATM 5173 H HO1  . GOL   D 3 .   ? 3.740   4.975  33.499 0.71 67.03 ? 202 GOL   A HO1  1 
HETATM 5174 H H2   . GOL   D 3 .   ? 6.305   2.972  32.751 1.00 97.09 ? 202 GOL   A H2   1 
HETATM 5175 H HO2  . GOL   D 3 .   ? 7.152   5.328  32.052 0.90 35.03 ? 202 GOL   A HO2  1 
HETATM 5176 H H31  . GOL   D 3 .   ? 7.478   3.763  34.907 0.83 85.59 ? 202 GOL   A H31  1 
HETATM 5177 H H32  . GOL   D 3 .   ? 8.358   4.535  33.902 0.83 85.59 ? 202 GOL   A H32  1 
HETATM 5178 H HO3  . GOL   D 3 .   ? 8.907   2.702  32.955 1.00 85.50 ? 202 GOL   A HO3  1 
HETATM 5179 C C1   . GOL   E 3 .   ? -17.007 16.910 11.818 1.00 51.08 ? 203 GOL   A C1   1 
HETATM 5180 O O1   . GOL   E 3 .   ? -17.925 17.957 11.601 1.00 65.99 ? 203 GOL   A O1   1 
HETATM 5181 C C2   . GOL   E 3 .   ? -16.911 16.105 10.510 1.00 42.83 ? 203 GOL   A C2   1 
HETATM 5182 O O2   . GOL   E 3 .   ? -16.849 16.940 9.395  1.00 73.09 ? 203 GOL   A O2   1 
HETATM 5183 C C3   . GOL   E 3 .   ? -15.650 15.233 10.637 1.00 50.33 ? 203 GOL   A C3   1 
HETATM 5184 O O3   . GOL   E 3 .   ? -15.427 14.644 9.390  1.00 68.25 ? 203 GOL   A O3   1 
HETATM 5185 H H11  . GOL   E 3 .   ? -17.279 16.320 12.537 1.00 61.30 ? 203 GOL   A H11  1 
HETATM 5186 H H12  . GOL   E 3 .   ? -16.125 17.234 12.059 1.00 61.30 ? 203 GOL   A H12  1 
HETATM 5187 H HO1  . GOL   E 3 .   ? -18.047 18.332 12.358 1.00 79.19 ? 203 GOL   A HO1  1 
HETATM 5188 H H2   . GOL   E 3 .   ? -17.699 15.549 10.406 1.00 51.40 ? 203 GOL   A H2   1 
HETATM 5189 H HO2  . GOL   E 3 .   ? -17.130 17.711 9.631  1.00 87.71 ? 203 GOL   A HO2  1 
HETATM 5190 H H31  . GOL   E 3 .   ? -15.788 14.587 11.347 1.00 60.40 ? 203 GOL   A H31  1 
HETATM 5191 H H32  . GOL   E 3 .   ? -14.914 15.790 10.936 1.00 60.40 ? 203 GOL   A H32  1 
HETATM 5192 H HO3  . GOL   E 3 .   ? -14.790 14.090 9.493  1.00 81.90 ? 203 GOL   A HO3  1 
HETATM 5193 C C10  A A1IAD F 2 .   ? -9.317  15.889 40.387 0.39 16.51 ? 201 A1IAD B C10  1 
HETATM 5194 C C10  B A1IAD F 2 .   ? -9.243  15.578 40.616 0.61 26.01 ? 201 A1IAD B C10  1 
HETATM 5195 C C15  A A1IAD F 2 .   ? -7.501  16.268 43.034 0.39 19.66 ? 201 A1IAD B C15  1 
HETATM 5196 C C15  B A1IAD F 2 .   ? -7.204  15.430 43.255 0.61 23.69 ? 201 A1IAD B C15  1 
HETATM 5197 C C11  A A1IAD F 2 .   ? -9.041  17.247 40.341 0.39 19.28 ? 201 A1IAD B C11  1 
HETATM 5198 C C11  B A1IAD F 2 .   ? -8.881  16.917 40.571 0.61 23.76 ? 201 A1IAD B C11  1 
HETATM 5199 C C12  A A1IAD F 2 .   ? -7.778  17.781 41.006 0.39 20.23 ? 201 A1IAD B C12  1 
HETATM 5200 C C12  B A1IAD F 2 .   ? -7.645  17.305 41.379 0.61 21.11 ? 201 A1IAD B C12  1 
HETATM 5201 C C14  A A1IAD F 2 .   ? -6.973  16.825 41.891 0.39 15.68 ? 201 A1IAD B C14  1 
HETATM 5202 C C14  B A1IAD F 2 .   ? -6.820  16.259 42.188 0.61 29.21 ? 201 A1IAD B C14  1 
HETATM 5203 C C01  A A1IAD F 2 .   ? -9.183  22.098 37.627 0.39 23.72 ? 201 A1IAD B C01  1 
HETATM 5204 C C01  B A1IAD F 2 .   ? -11.159 22.450 38.522 0.61 52.23 ? 201 A1IAD B C01  1 
HETATM 5205 C C02  A A1IAD F 2 .   ? -10.089 21.813 38.820 0.39 22.36 ? 201 A1IAD B C02  1 
HETATM 5206 C C02  B A1IAD F 2 .   ? -10.154 21.305 38.379 0.61 65.12 ? 201 A1IAD B C02  1 
HETATM 5207 C C03  A A1IAD F 2 .   ? -11.300 22.752 38.842 0.39 26.08 ? 201 A1IAD B C03  1 
HETATM 5208 C C03  B A1IAD F 2 .   ? -8.731  21.864 38.408 0.61 27.97 ? 201 A1IAD B C03  1 
HETATM 5209 C C04  A A1IAD F 2 .   ? -10.528 20.355 38.795 0.39 32.25 ? 201 A1IAD B C04  1 
HETATM 5210 C C04  B A1IAD F 2 .   ? -10.413 20.245 39.454 0.61 42.05 ? 201 A1IAD B C04  1 
HETATM 5211 C C06  A A1IAD F 2 .   ? -9.879  18.098 39.641 0.39 21.05 ? 201 A1IAD B C06  1 
HETATM 5212 C C06  B A1IAD F 2 .   ? -9.631  17.806 39.752 0.61 29.76 ? 201 A1IAD B C06  1 
HETATM 5213 C C07  A A1IAD F 2 .   ? -11.003 17.591 39.031 0.39 15.86 ? 201 A1IAD B C07  1 
HETATM 5214 C C07  B A1IAD F 2 .   ? -10.725 17.322 39.033 0.61 44.57 ? 201 A1IAD B C07  1 
HETATM 5215 C C08  A A1IAD F 2 .   ? -11.271 16.234 39.075 0.39 17.10 ? 201 A1IAD B C08  1 
HETATM 5216 C C08  B A1IAD F 2 .   ? -11.089 15.993 39.100 0.61 34.14 ? 201 A1IAD B C08  1 
HETATM 5217 C C09  A A1IAD F 2 .   ? -10.447 15.388 39.771 0.39 14.87 ? 201 A1IAD B C09  1 
HETATM 5218 C C09  B A1IAD F 2 .   ? -10.351 15.128 39.894 0.61 36.96 ? 201 A1IAD B C09  1 
HETATM 5219 C C16  A A1IAD F 2 .   ? -8.765  16.392 43.572 0.39 24.17 ? 201 A1IAD B C16  1 
HETATM 5220 C C16  B A1IAD F 2 .   ? -8.442  15.259 43.870 0.61 26.35 ? 201 A1IAD B C16  1 
HETATM 5221 C C17  A A1IAD F 2 .   ? -9.418  15.228 43.915 0.39 19.52 ? 201 A1IAD B C17  1 
HETATM 5222 C C17  B A1IAD F 2 .   ? -8.696  14.000 44.377 0.61 26.09 ? 201 A1IAD B C17  1 
HETATM 5223 C C18  A A1IAD F 2 .   ? -10.694 15.289 44.456 0.39 40.61 ? 201 A1IAD B C18  1 
HETATM 5224 C C18  B A1IAD F 2 .   ? -9.891  13.738 45.002 0.61 38.15 ? 201 A1IAD B C18  1 
HETATM 5225 C C19  A A1IAD F 2 .   ? -11.294 16.523 44.656 0.39 31.56 ? 201 A1IAD B C19  1 
HETATM 5226 C C19  B A1IAD F 2 .   ? -10.840 14.724 45.111 0.61 32.03 ? 201 A1IAD B C19  1 
HETATM 5227 C C21  A A1IAD F 2 .   ? -10.635 17.696 44.318 0.39 24.06 ? 201 A1IAD B C21  1 
HETATM 5228 C C21  B A1IAD F 2 .   ? -10.622 15.995 44.615 0.61 26.56 ? 201 A1IAD B C21  1 
HETATM 5229 C C22  A A1IAD F 2 .   ? -9.369  17.632 43.768 0.39 21.91 ? 201 A1IAD B C22  1 
HETATM 5230 C C22  B A1IAD F 2 .   ? -9.405  16.254 43.974 0.61 24.70 ? 201 A1IAD B C22  1 
HETATM 5231 C C24  A A1IAD F 2 .   ? -5.037  15.579 42.517 0.39 14.26 ? 201 A1IAD B C24  1 
HETATM 5232 C C24  B A1IAD F 2 .   ? -4.712  15.227 42.583 0.61 24.47 ? 201 A1IAD B C24  1 
HETATM 5233 C C25  A A1IAD F 2 .   ? -3.712  15.129 42.388 0.39 14.53 ? 201 A1IAD B C25  1 
HETATM 5234 C C25  B A1IAD F 2 .   ? -3.357  15.042 42.306 0.61 33.25 ? 201 A1IAD B C25  1 
HETATM 5235 C C26  A A1IAD F 2 .   ? -2.949  15.580 41.318 0.39 13.07 ? 201 A1IAD B C26  1 
HETATM 5236 C C26  B A1IAD F 2 .   ? -2.752  15.770 41.279 0.61 49.48 ? 201 A1IAD B C26  1 
HETATM 5237 C C28  A A1IAD F 2 .   ? -3.498  16.457 40.414 0.39 15.30 ? 201 A1IAD B C28  1 
HETATM 5238 C C28  B A1IAD F 2 .   ? -3.481  16.684 40.530 0.61 31.79 ? 201 A1IAD B C28  1 
HETATM 5239 C C29  A A1IAD F 2 .   ? -4.796  16.897 40.557 0.39 15.12 ? 201 A1IAD B C29  1 
HETATM 5240 C C29  B A1IAD F 2 .   ? -4.818  16.868 40.813 0.61 30.49 ? 201 A1IAD B C29  1 
HETATM 5241 C C30  A A1IAD F 2 .   ? -5.612  16.464 41.637 0.39 17.04 ? 201 A1IAD B C30  1 
HETATM 5242 C C30  B A1IAD F 2 .   ? -5.451  16.135 41.863 0.61 23.88 ? 201 A1IAD B C30  1 
HETATM 5243 N N05  A A1IAD F 2 .   ? -9.614  19.525 39.559 0.39 46.82 ? 201 A1IAD B N05  1 
HETATM 5244 N N05  B A1IAD F 2 .   ? -9.344  19.250 39.595 0.61 31.45 ? 201 A1IAD B N05  1 
HETATM 5245 O O13  A A1IAD F 2 .   ? -7.414  18.892 40.781 0.39 22.44 ? 201 A1IAD B O13  1 
HETATM 5246 O O13  B A1IAD F 2 .   ? -7.288  18.459 41.393 0.61 26.10 ? 201 A1IAD B O13  1 
HETATM 5247 O O20  A A1IAD F 2 .   ? -12.580 16.595 45.210 0.39 29.20 ? 201 A1IAD B O20  1 
HETATM 5248 O O20  B A1IAD F 2 .   ? -12.030 14.398 45.761 0.61 37.38 ? 201 A1IAD B O20  1 
HETATM 5249 O O27  A A1IAD F 2 .   ? -1.643  15.143 41.144 0.39 14.60 ? 201 A1IAD B O27  1 
HETATM 5250 O O27  B A1IAD F 2 .   ? -1.399  15.571 41.008 0.61 48.72 ? 201 A1IAD B O27  1 
HETATM 5251 S S23  A A1IAD F 2 .   ? -6.253  15.280 43.736 0.39 19.67 ? 201 A1IAD B S23  1 
HETATM 5252 S S23  B A1IAD F 2 .   ? -5.792  14.537 43.771 0.61 26.84 ? 201 A1IAD B S23  1 
HETATM 5253 H H101 A A1IAD F 2 .   ? -8.644  15.219 40.907 0.39 19.81 ? 201 A1IAD B H101 1 
HETATM 5254 H H101 B A1IAD F 2 .   ? -8.666  14.881 41.212 0.61 31.21 ? 201 A1IAD B H101 1 
HETATM 5255 H H011 A A1IAD F 2 .   ? -8.501  22.906 37.875 0.39 28.46 ? 201 A1IAD B H011 1 
HETATM 5256 H H011 B A1IAD F 2 .   ? -10.710 23.258 39.092 0.61 62.68 ? 201 A1IAD B H011 1 
HETATM 5257 H H012 A A1IAD F 2 .   ? -9.789  22.385 36.773 0.39 28.46 ? 201 A1IAD B H012 1 
HETATM 5258 H H012 B A1IAD F 2 .   ? -11.437 22.813 37.536 0.61 62.68 ? 201 A1IAD B H012 1 
HETATM 5259 H H013 A A1IAD F 2 .   ? -8.614  21.206 37.383 0.39 28.46 ? 201 A1IAD B H013 1 
HETATM 5260 H H013 B A1IAD F 2 .   ? -12.045 22.092 39.038 0.61 62.68 ? 201 A1IAD B H013 1 
HETATM 5261 H H021 A A1IAD F 2 .   ? -9.528  21.995 39.728 0.39 26.83 ? 201 A1IAD B H021 1 
HETATM 5262 H H021 B A1IAD F 2 .   ? -10.277 20.811 37.424 0.61 78.14 ? 201 A1IAD B H021 1 
HETATM 5263 H H033 A A1IAD F 2 .   ? -11.877 22.621 37.931 0.39 31.30 ? 201 A1IAD B H033 1 
HETATM 5264 H H033 B A1IAD F 2 .   ? -8.342  21.813 39.420 0.61 33.56 ? 201 A1IAD B H033 1 
HETATM 5265 H H032 A A1IAD F 2 .   ? -11.923 22.520 39.701 0.39 31.30 ? 201 A1IAD B H032 1 
HETATM 5266 H H032 B A1IAD F 2 .   ? -8.741  22.898 38.076 0.61 33.56 ? 201 A1IAD B H032 1 
HETATM 5267 H H031 A A1IAD F 2 .   ? -10.959 23.781 38.909 0.39 31.30 ? 201 A1IAD B H031 1 
HETATM 5268 H H031 B A1IAD F 2 .   ? -8.099  21.278 37.747 0.61 33.56 ? 201 A1IAD B H031 1 
HETATM 5269 H H041 A A1IAD F 2 .   ? -11.522 20.275 39.222 0.39 38.70 ? 201 A1IAD B H041 1 
HETATM 5270 H H041 B A1IAD F 2 .   ? -10.536 20.749 40.406 0.61 50.46 ? 201 A1IAD B H041 1 
HETATM 5271 H H042 A A1IAD F 2 .   ? -10.550 20.007 37.768 0.39 38.70 ? 201 A1IAD B H042 1 
HETATM 5272 H H042 B A1IAD F 2 .   ? -11.331 19.724 39.203 0.61 50.46 ? 201 A1IAD B H042 1 
HETATM 5273 H H071 A A1IAD F 2 .   ? -11.681 18.256 38.513 0.39 19.03 ? 201 A1IAD B H071 1 
HETATM 5274 H H071 B A1IAD F 2 .   ? -11.296 18.000 38.413 0.61 53.49 ? 201 A1IAD B H071 1 
HETATM 5275 H H081 A A1IAD F 2 .   ? -12.136 15.839 38.557 0.39 20.52 ? 201 A1IAD B H081 1 
HETATM 5276 H H081 B A1IAD F 2 .   ? -11.943 15.629 38.540 0.61 40.97 ? 201 A1IAD B H081 1 
HETATM 5277 H H091 A A1IAD F 2 .   ? -10.682 14.333 39.838 0.39 17.84 ? 201 A1IAD B H091 1 
HETATM 5278 H H091 B A1IAD F 2 .   ? -10.638 14.085 39.955 0.61 44.35 ? 201 A1IAD B H091 1 
HETATM 5279 H H171 A A1IAD F 2 .   ? -8.937  14.270 43.763 0.39 23.42 ? 201 A1IAD B H171 1 
HETATM 5280 H H171 B A1IAD F 2 .   ? -7.952  13.218 44.281 0.61 31.31 ? 201 A1IAD B H171 1 
HETATM 5281 H H181 A A1IAD F 2 .   ? -11.218 14.379 44.721 0.39 48.73 ? 201 A1IAD B H181 1 
HETATM 5282 H H181 B A1IAD F 2 .   ? -10.084 12.754 45.410 0.61 45.78 ? 201 A1IAD B H181 1 
HETATM 5283 H H211 A A1IAD F 2 .   ? -11.109 18.655 44.484 0.39 28.87 ? 201 A1IAD B H211 1 
HETATM 5284 H H211 B A1IAD F 2 .   ? -11.371 16.769 44.720 0.61 31.87 ? 201 A1IAD B H211 1 
HETATM 5285 H H221 A A1IAD F 2 .   ? -8.849  18.539 43.492 0.39 26.29 ? 201 A1IAD B H221 1 
HETATM 5286 H H221 B A1IAD F 2 .   ? -9.214  17.234 43.558 0.61 29.64 ? 201 A1IAD B H221 1 
HETATM 5287 H H251 A A1IAD F 2 .   ? -3.292  14.440 43.111 0.39 17.43 ? 201 A1IAD B H251 1 
HETATM 5288 H H251 B A1IAD F 2 .   ? -2.776  14.335 42.885 0.61 39.90 ? 201 A1IAD B H251 1 
HETATM 5289 H H281 A A1IAD F 2 .   ? -2.904  16.807 39.578 0.39 18.36 ? 201 A1IAD B H281 1 
HETATM 5290 H H281 B A1IAD F 2 .   ? -3.006  17.245 39.734 0.61 38.15 ? 201 A1IAD B H281 1 
HETATM 5291 H H291 A A1IAD F 2 .   ? -5.204  17.588 39.830 0.39 18.14 ? 201 A1IAD B H291 1 
HETATM 5292 H H291 B A1IAD F 2 .   ? -5.395  17.576 40.233 0.61 36.59 ? 201 A1IAD B H291 1 
HETATM 5293 H H051 A A1IAD F 2 .   ? -8.824  19.925 40.018 0.39 56.18 ? 201 A1IAD B H051 1 
HETATM 5294 H H051 B A1IAD F 2 .   ? -8.394  19.556 39.584 0.61 37.74 ? 201 A1IAD B H051 1 
HETATM 5295 H H201 A A1IAD F 2 .   ? -12.925 15.720 45.313 0.39 35.04 ? 201 A1IAD B H201 1 
HETATM 5296 H H201 B A1IAD F 2 .   ? -12.693 14.185 45.119 0.61 44.86 ? 201 A1IAD B H201 1 
HETATM 5297 H H271 A A1IAD F 2 .   ? -1.273  15.576 40.393 0.39 17.52 ? 201 A1IAD B H271 1 
HETATM 5298 H H271 B A1IAD F 2 .   ? -1.214  15.844 40.122 0.61 58.47 ? 201 A1IAD B H271 1 
HETATM 5299 O O    . HOH   G 4 .   ? -3.050  9.937  56.203 1.00 42.89 ? 301 HOH   A O    1 
HETATM 5300 O O    . HOH   G 4 .   ? 10.902  11.210 17.956 1.00 36.97 ? 302 HOH   A O    1 
HETATM 5301 O O    . HOH   G 4 .   ? 1.448   0.813  24.321 1.00 30.10 ? 303 HOH   A O    1 
HETATM 5302 O O    . HOH   G 4 .   ? 15.968  17.182 19.453 1.00 46.71 ? 304 HOH   A O    1 
HETATM 5303 O O    . HOH   G 4 .   ? 3.507   10.401 1.832  1.00 44.89 ? 305 HOH   A O    1 
HETATM 5304 O O    . HOH   G 4 .   ? 8.628   28.893 25.625 1.00 61.40 ? 306 HOH   A O    1 
HETATM 5305 O O    . HOH   G 4 .   ? 0.520   26.765 18.667 1.00 40.79 ? 307 HOH   A O    1 
HETATM 5306 O O    . HOH   G 4 .   ? 8.745   26.670 23.833 1.00 48.48 ? 308 HOH   A O    1 
HETATM 5307 O O    . HOH   G 4 .   ? 5.243   29.540 26.103 1.00 63.19 ? 309 HOH   A O    1 
HETATM 5308 O O    . HOH   G 4 .   ? 12.083  14.334 42.390 1.00 54.30 ? 310 HOH   A O    1 
HETATM 5309 O O    . HOH   G 4 .   ? 5.758   12.608 17.583 1.00 26.69 ? 311 HOH   A O    1 
HETATM 5310 O O    . HOH   G 4 .   ? 20.275  3.548  21.473 1.00 40.50 ? 312 HOH   A O    1 
HETATM 5311 O O    . HOH   G 4 .   ? 5.519   27.359 11.034 1.00 41.71 ? 313 HOH   A O    1 
HETATM 5312 O O    . HOH   G 4 .   ? -2.103  25.827 16.842 1.00 34.86 ? 314 HOH   A O    1 
HETATM 5313 O O    . HOH   G 4 .   ? -1.322  11.947 45.446 1.00 29.84 ? 315 HOH   A O    1 
HETATM 5314 O O    . HOH   G 4 .   ? 8.162   -1.278 24.398 1.00 35.24 ? 316 HOH   A O    1 
HETATM 5315 O O    . HOH   G 4 .   ? -8.736  24.944 7.426  1.00 36.15 ? 317 HOH   A O    1 
HETATM 5316 O O    . HOH   G 4 .   ? 2.810   25.189 2.732  1.00 45.44 ? 318 HOH   A O    1 
HETATM 5317 O O    . HOH   G 4 .   ? -0.594  12.084 52.545 1.00 45.41 ? 319 HOH   A O    1 
HETATM 5318 O O    . HOH   G 4 .   ? 11.413  24.989 25.877 1.00 52.59 ? 320 HOH   A O    1 
HETATM 5319 O O    . HOH   G 4 .   ? -3.461  11.725 -0.564 1.00 41.01 ? 321 HOH   A O    1 
HETATM 5320 O O    . HOH   G 4 .   ? 16.693  14.620 37.158 1.00 31.41 ? 322 HOH   A O    1 
HETATM 5321 O O    . HOH   G 4 .   ? -13.802 22.195 -5.345 1.00 39.64 ? 323 HOH   A O    1 
HETATM 5322 O O    . HOH   G 4 .   ? -0.055  10.873 29.597 1.00 20.90 ? 324 HOH   A O    1 
HETATM 5323 O O    . HOH   G 4 .   ? -1.085  21.353 16.232 1.00 18.60 ? 325 HOH   A O    1 
HETATM 5324 O O    . HOH   G 4 .   ? -2.555  11.679 28.863 1.00 23.92 ? 326 HOH   A O    1 
HETATM 5325 O O    . HOH   G 4 .   ? 2.953   25.528 -0.018 1.00 51.70 ? 327 HOH   A O    1 
HETATM 5326 O O    . HOH   G 4 .   ? 12.069  3.519  22.230 1.00 21.85 ? 328 HOH   A O    1 
HETATM 5327 O O    . HOH   G 4 .   ? 7.171   11.895 26.246 1.00 23.40 ? 329 HOH   A O    1 
HETATM 5328 O O    . HOH   G 4 .   ? 11.658  23.987 0.700  1.00 40.57 ? 330 HOH   A O    1 
HETATM 5329 O O    . HOH   G 4 .   ? -6.519  5.340  22.141 1.00 27.09 ? 331 HOH   A O    1 
HETATM 5330 O O    . HOH   G 4 .   ? 7.494   15.597 14.941 1.00 31.65 ? 332 HOH   A O    1 
HETATM 5331 O O    . HOH   G 4 .   ? 7.146   26.399 4.699  1.00 40.61 ? 333 HOH   A O    1 
HETATM 5332 O O    . HOH   G 4 .   ? -8.133  9.279  3.936  1.00 34.87 ? 334 HOH   A O    1 
HETATM 5333 O O    . HOH   G 4 .   ? 2.379   4.646  36.364 1.00 52.78 ? 335 HOH   A O    1 
HETATM 5334 O O    . HOH   G 4 .   ? -4.064  24.678 9.480  1.00 35.30 ? 336 HOH   A O    1 
HETATM 5335 O O    . HOH   G 4 .   ? 2.085   5.097  31.614 1.00 43.29 ? 337 HOH   A O    1 
HETATM 5336 O O    . HOH   G 4 .   ? 14.869  6.371  6.455  1.00 44.40 ? 338 HOH   A O    1 
HETATM 5337 O O    . HOH   G 4 .   ? -4.430  3.591  12.347 1.00 51.99 ? 339 HOH   A O    1 
HETATM 5338 O O    . HOH   G 4 .   ? 7.262   13.141 23.827 1.00 29.64 ? 340 HOH   A O    1 
HETATM 5339 O O    . HOH   G 4 .   ? -8.825  11.048 53.929 1.00 46.49 ? 341 HOH   A O    1 
HETATM 5340 O O    . HOH   G 4 .   ? -4.889  -2.032 24.155 1.00 39.76 ? 342 HOH   A O    1 
HETATM 5341 O O    . HOH   G 4 .   ? 9.939   7.549  40.180 1.00 34.43 ? 343 HOH   A O    1 
HETATM 5342 O O    . HOH   G 4 .   ? 4.721   0.794  10.517 1.00 42.79 ? 344 HOH   A O    1 
HETATM 5343 O O    . HOH   G 4 .   ? 10.681  5.240  38.875 1.00 39.71 ? 345 HOH   A O    1 
HETATM 5344 O O    . HOH   G 4 .   ? 13.982  23.818 7.401  1.00 47.58 ? 346 HOH   A O    1 
HETATM 5345 O O    . HOH   G 4 .   ? 20.660  7.899  15.446 1.00 35.65 ? 347 HOH   A O    1 
HETATM 5346 O O    . HOH   G 4 .   ? -8.614  20.934 -1.186 1.00 38.22 ? 348 HOH   A O    1 
HETATM 5347 O O    . HOH   G 4 .   ? -10.168 25.729 13.078 1.00 38.84 ? 349 HOH   A O    1 
HETATM 5348 O O    . HOH   G 4 .   ? -4.012  25.653 6.426  1.00 44.50 ? 350 HOH   A O    1 
HETATM 5349 O O    . HOH   G 4 .   ? 24.115  8.138  29.595 1.00 37.39 ? 351 HOH   A O    1 
HETATM 5350 O O    . HOH   G 4 .   ? 10.031  26.662 34.683 1.00 54.98 ? 352 HOH   A O    1 
HETATM 5351 O O    . HOH   G 4 .   ? 15.710  4.767  34.072 1.00 27.64 ? 353 HOH   A O    1 
HETATM 5352 O O    . HOH   G 4 .   ? 11.296  -2.206 24.545 1.00 45.17 ? 354 HOH   A O    1 
HETATM 5353 O O    . HOH   G 4 .   ? -0.517  9.367  33.928 1.00 34.68 ? 355 HOH   A O    1 
HETATM 5354 O O    . HOH   G 4 .   ? 6.742   7.331  7.030  1.00 33.06 ? 356 HOH   A O    1 
HETATM 5355 O O    . HOH   G 4 .   ? 17.488  8.629  37.882 1.00 31.12 ? 357 HOH   A O    1 
HETATM 5356 O O    . HOH   G 4 .   ? 14.876  23.766 10.775 1.00 33.27 ? 358 HOH   A O    1 
HETATM 5357 O O    . HOH   G 4 .   ? 7.701   15.888 1.207  1.00 29.38 ? 359 HOH   A O    1 
HETATM 5358 O O    . HOH   G 4 .   ? 11.673  21.790 35.734 1.00 47.01 ? 360 HOH   A O    1 
HETATM 5359 O O    . HOH   G 4 .   ? 7.627   12.024 19.728 1.00 32.35 ? 361 HOH   A O    1 
HETATM 5360 O O    . HOH   G 4 .   ? 20.353  5.757  29.091 1.00 35.34 ? 362 HOH   A O    1 
HETATM 5361 O O    . HOH   G 4 .   ? 14.746  26.720 13.486 1.00 44.20 ? 363 HOH   A O    1 
HETATM 5362 O O    . HOH   G 4 .   ? 12.690  12.964 10.325 1.00 23.42 ? 364 HOH   A O    1 
HETATM 5363 O O    . HOH   G 4 .   ? 10.676  2.814  16.026 1.00 27.69 ? 365 HOH   A O    1 
HETATM 5364 O O    . HOH   G 4 .   ? 18.229  2.955  16.779 1.00 52.84 ? 366 HOH   A O    1 
HETATM 5365 O O    . HOH   G 4 .   ? 4.026   5.166  7.990  1.00 36.60 ? 367 HOH   A O    1 
HETATM 5366 O O    . HOH   G 4 .   ? 6.977   5.124  16.064 1.00 30.73 ? 368 HOH   A O    1 
HETATM 5367 O O    . HOH   G 4 .   ? 3.794   25.999 12.728 1.00 35.26 ? 369 HOH   A O    1 
HETATM 5368 O O    . HOH   G 4 .   ? -11.253 11.679 5.737  1.00 41.28 ? 370 HOH   A O    1 
HETATM 5369 O O    . HOH   G 4 .   ? -7.501  10.205 45.296 1.00 43.11 ? 371 HOH   A O    1 
HETATM 5370 O O    . HOH   G 4 .   ? 16.894  12.754 9.557  1.00 29.03 ? 372 HOH   A O    1 
HETATM 5371 O O    . HOH   G 4 .   ? 7.897   18.472 0.115  1.00 27.11 ? 373 HOH   A O    1 
HETATM 5372 O O    . HOH   G 4 .   ? -7.808  13.811 -1.311 1.00 40.68 ? 374 HOH   A O    1 
HETATM 5373 O O    . HOH   G 4 .   ? 9.286   8.240  6.654  1.00 31.16 ? 375 HOH   A O    1 
HETATM 5374 O O    . HOH   G 4 .   ? 15.868  15.953 4.237  1.00 46.38 ? 376 HOH   A O    1 
HETATM 5375 O O    . HOH   G 4 .   ? 11.248  9.717  15.732 1.00 35.40 ? 377 HOH   A O    1 
HETATM 5376 O O    . HOH   G 4 .   ? -12.239 3.867  21.805 1.00 46.15 ? 378 HOH   A O    1 
HETATM 5377 O O    . HOH   G 4 .   ? 8.820   14.426 12.542 1.00 28.04 ? 379 HOH   A O    1 
HETATM 5378 O O    . HOH   G 4 .   ? 3.445   -3.527 27.929 1.00 30.45 ? 380 HOH   A O    1 
HETATM 5379 O O    . HOH   G 4 .   ? 3.462   13.865 49.943 1.00 43.51 ? 381 HOH   A O    1 
HETATM 5380 O O    . HOH   G 4 .   ? -5.034  17.079 51.406 1.00 31.72 ? 382 HOH   A O    1 
HETATM 5381 O O    . HOH   G 4 .   ? 6.012   8.311  14.371 1.00 20.42 ? 383 HOH   A O    1 
HETATM 5382 O O    . HOH   G 4 .   ? -5.147  9.066  41.246 1.00 38.08 ? 384 HOH   A O    1 
HETATM 5383 O O    . HOH   G 4 .   ? 17.154  6.567  30.086 1.00 26.03 ? 385 HOH   A O    1 
HETATM 5384 O O    . HOH   G 4 .   ? 7.110   24.312 2.581  1.00 33.98 ? 386 HOH   A O    1 
HETATM 5385 O O    . HOH   G 4 .   ? 4.361   3.965  15.543 1.00 25.77 ? 387 HOH   A O    1 
HETATM 5386 O O    . HOH   G 4 .   ? -10.362 17.181 9.845  1.00 19.77 ? 388 HOH   A O    1 
HETATM 5387 O O    . HOH   G 4 .   ? 9.441   26.938 11.969 1.00 37.75 ? 389 HOH   A O    1 
HETATM 5388 O O    . HOH   G 4 .   ? 3.634   26.357 15.592 1.00 38.10 ? 390 HOH   A O    1 
HETATM 5389 O O    . HOH   G 4 .   ? 4.041   15.954 51.626 1.00 42.11 ? 391 HOH   A O    1 
HETATM 5390 O O    . HOH   G 4 .   ? 4.904   9.739  43.970 1.00 42.28 ? 392 HOH   A O    1 
HETATM 5391 O O    . HOH   G 4 .   ? -1.410  6.599  5.158  1.00 36.64 ? 393 HOH   A O    1 
HETATM 5392 O O    . HOH   G 4 .   ? -3.960  20.420 3.345  1.00 34.54 ? 394 HOH   A O    1 
HETATM 5393 O O    . HOH   G 4 .   ? 15.418  1.390  34.539 1.00 51.04 ? 395 HOH   A O    1 
HETATM 5394 O O    . HOH   G 4 .   ? -8.434  11.244 49.290 1.00 52.12 ? 396 HOH   A O    1 
HETATM 5395 O O    . HOH   G 4 .   ? 7.210   15.784 18.458 1.00 32.86 ? 397 HOH   A O    1 
HETATM 5396 O O    . HOH   G 4 .   ? 19.840  0.910  22.463 1.00 49.04 ? 398 HOH   A O    1 
HETATM 5397 O O    . HOH   G 4 .   ? -14.722 15.002 4.690  1.00 40.84 ? 399 HOH   A O    1 
HETATM 5398 O O    . HOH   G 4 .   ? 11.135  11.204 13.387 1.00 29.08 ? 400 HOH   A O    1 
HETATM 5399 O O    . HOH   G 4 .   ? 14.689  11.956 41.807 1.00 37.12 ? 401 HOH   A O    1 
HETATM 5400 O O    . HOH   G 4 .   ? -6.682  1.599  17.556 1.00 45.12 ? 402 HOH   A O    1 
HETATM 5401 O O    . HOH   G 4 .   ? 9.063   13.740 18.064 1.00 32.96 ? 403 HOH   A O    1 
HETATM 5402 O O    . HOH   G 4 .   ? -2.179  11.270 50.088 1.00 37.69 ? 404 HOH   A O    1 
HETATM 5403 O O    . HOH   G 4 .   ? -3.982  24.641 3.188  1.00 42.00 ? 405 HOH   A O    1 
HETATM 5404 O O    . HOH   G 4 .   ? 16.633  19.509 16.301 1.00 45.05 ? 406 HOH   A O    1 
HETATM 5405 O O    . HOH   G 4 .   ? 2.721   22.283 1.922  1.00 35.55 ? 407 HOH   A O    1 
HETATM 5406 O O    . HOH   G 4 .   ? 13.823  24.279 17.097 1.00 37.23 ? 408 HOH   A O    1 
HETATM 5407 O O    . HOH   G 4 .   ? 2.128   2.589  26.413 1.00 25.96 ? 409 HOH   A O    1 
HETATM 5408 O O    . HOH   G 4 .   ? -16.445 19.073 5.392  1.00 51.70 ? 410 HOH   A O    1 
HETATM 5409 O O    . HOH   G 4 .   ? 12.361  2.532  33.286 1.00 32.24 ? 411 HOH   A O    1 
HETATM 5410 O O    . HOH   G 4 .   ? -15.362 20.578 6.023  1.00 43.65 ? 412 HOH   A O    1 
HETATM 5411 O O    . HOH   G 4 .   ? 0.625   22.290 27.380 1.00 30.43 ? 413 HOH   A O    1 
HETATM 5412 O O    . HOH   G 4 .   ? 4.996   22.289 29.293 1.00 28.03 ? 414 HOH   A O    1 
HETATM 5413 O O    . HOH   G 4 .   ? -6.008  24.173 11.161 1.00 31.96 ? 415 HOH   A O    1 
HETATM 5414 O O    . HOH   G 4 .   ? 7.523   2.792  9.420  1.00 28.70 ? 416 HOH   A O    1 
HETATM 5415 O O    . HOH   G 4 .   ? 21.760  1.994  32.176 1.00 37.28 ? 417 HOH   A O    1 
HETATM 5416 O O    . HOH   G 4 .   ? -17.093 25.062 14.583 1.00 46.67 ? 418 HOH   A O    1 
HETATM 5417 O O    . HOH   G 4 .   ? -8.545  5.821  13.864 1.00 32.63 ? 419 HOH   A O    1 
HETATM 5418 O O    . HOH   G 4 .   ? 8.316   8.430  42.380 1.00 32.50 ? 420 HOH   A O    1 
HETATM 5419 O O    . HOH   G 4 .   ? 11.515  14.072 12.526 1.00 31.79 ? 421 HOH   A O    1 
HETATM 5420 O O    . HOH   G 4 .   ? -3.235  1.372  14.079 1.00 30.03 ? 422 HOH   A O    1 
HETATM 5421 O O    . HOH   G 4 .   ? -10.321 6.461  24.275 1.00 35.79 ? 423 HOH   A O    1 
HETATM 5422 O O    . HOH   G 4 .   ? 10.079  9.291  17.960 1.00 38.02 ? 424 HOH   A O    1 
HETATM 5423 O O    . HOH   G 4 .   ? -8.921  3.644  15.588 1.00 53.49 ? 425 HOH   A O    1 
HETATM 5424 O O    . HOH   G 4 .   ? 11.437  25.138 22.202 1.00 39.94 ? 426 HOH   A O    1 
HETATM 5425 O O    . HOH   G 4 .   ? -8.115  5.681  26.032 1.00 47.62 ? 427 HOH   A O    1 
HETATM 5426 O O    . HOH   G 4 .   ? 2.734   22.390 51.778 1.00 42.74 ? 428 HOH   A O    1 
HETATM 5427 O O    . HOH   G 4 .   ? 12.066  1.681  8.697  1.00 45.21 ? 429 HOH   A O    1 
HETATM 5428 O O    . HOH   G 4 .   ? -6.368  4.517  12.504 1.00 49.52 ? 430 HOH   A O    1 
HETATM 5429 O O    . HOH   G 4 .   ? 6.694   -2.455 13.738 1.00 26.22 ? 431 HOH   A O    1 
HETATM 5430 O O    . HOH   G 4 .   ? -0.042  25.833 21.173 1.00 36.79 ? 432 HOH   A O    1 
HETATM 5431 O O    . HOH   G 4 .   ? 8.033   10.432 5.077  1.00 49.54 ? 433 HOH   A O    1 
HETATM 5432 O O    . HOH   G 4 .   ? 7.632   11.404 46.433 1.00 49.07 ? 434 HOH   A O    1 
HETATM 5433 O O    . HOH   G 4 .   ? -2.332  13.958 27.468 1.00 22.25 ? 435 HOH   A O    1 
HETATM 5434 O O    . HOH   G 4 .   ? 8.436   10.303 17.969 1.00 32.67 ? 436 HOH   A O    1 
HETATM 5435 O O    . HOH   G 4 .   ? 17.303  17.572 8.190  1.00 44.08 ? 437 HOH   A O    1 
HETATM 5436 O O    . HOH   G 4 .   ? 13.708  0.025  10.191 1.00 46.62 ? 438 HOH   A O    1 
HETATM 5437 O O    . HOH   G 4 .   ? 5.143   28.034 19.506 1.00 64.21 ? 439 HOH   A O    1 
HETATM 5438 O O    . HOH   G 4 .   ? -18.880 26.631 -3.037 1.00 62.61 ? 440 HOH   A O    1 
HETATM 5439 O O    . HOH   G 4 .   ? 8.882   28.502 14.001 1.00 40.67 ? 441 HOH   A O    1 
HETATM 5440 O O    . HOH   G 4 .   ? -18.620 21.602 -3.409 1.00 58.00 ? 442 HOH   A O    1 
HETATM 5441 O O    . HOH   G 4 .   ? -0.796  25.364 23.130 1.00 38.04 ? 443 HOH   A O    1 
HETATM 5442 O O    . HOH   G 4 .   ? 8.816   8.222  16.894 1.00 36.96 ? 444 HOH   A O    1 
HETATM 5443 O O    . HOH   G 4 .   ? 6.141   13.649 47.872 1.00 47.38 ? 445 HOH   A O    1 
HETATM 5444 O O    . HOH   G 4 .   ? -11.409 7.294  15.828 1.00 50.85 ? 446 HOH   A O    1 
HETATM 5445 O O    . HOH   G 4 .   ? 0.220   -3.507 31.421 1.00 63.57 ? 447 HOH   A O    1 
HETATM 5446 O O    . HOH   G 4 .   ? -0.990  8.952  31.355 1.00 29.67 ? 448 HOH   A O    1 
HETATM 5447 O O    . HOH   G 4 .   ? -6.987  23.478 2.530  1.00 57.64 ? 449 HOH   A O    1 
HETATM 5448 O O    . HOH   G 4 .   ? 22.832  6.631  34.248 1.00 34.22 ? 450 HOH   A O    1 
HETATM 5449 O O    . HOH   G 4 .   ? 6.461   4.863  40.751 1.00 53.20 ? 451 HOH   A O    1 
HETATM 5450 O O    . HOH   G 4 .   ? 9.350   0.954  8.959  1.00 46.23 ? 452 HOH   A O    1 
HETATM 5451 O O    . HOH   G 4 .   ? 5.856   7.427  42.720 1.00 54.35 ? 453 HOH   A O    1 
HETATM 5452 O O    . HOH   G 4 .   ? 6.116   27.615 21.840 1.00 64.21 ? 454 HOH   A O    1 
HETATM 5453 O O    . HOH   G 4 .   ? 17.102  10.527 39.712 1.00 46.71 ? 455 HOH   A O    1 
HETATM 5454 O O    . HOH   G 4 .   ? 11.962  0.502  15.737 1.00 33.41 ? 456 HOH   A O    1 
HETATM 5455 O O    . HOH   G 4 .   ? -5.078  5.676  24.357 1.00 41.31 ? 457 HOH   A O    1 
HETATM 5456 O O    . HOH   G 4 .   ? -20.274 23.705 -1.804 1.00 62.48 ? 458 HOH   A O    1 
HETATM 5457 O O    . HOH   G 4 .   ? 0.761   3.506  28.654 1.00 33.36 ? 459 HOH   A O    1 
HETATM 5458 O O    . HOH   G 4 .   ? 23.175  8.579  16.491 1.00 50.76 ? 460 HOH   A O    1 
HETATM 5459 O O    . HOH   G 4 .   ? -0.356  6.312  31.197 1.00 32.19 ? 461 HOH   A O    1 
HETATM 5460 O O    . HOH   G 4 .   ? -0.179  4.566  7.139  1.00 46.84 ? 462 HOH   A O    1 
HETATM 5461 O O    . HOH   G 4 .   ? 10.733  -0.703 13.165 1.00 36.81 ? 463 HOH   A O    1 
HETATM 5462 O O    . HOH   G 4 .   ? -1.537  9.362  45.779 1.00 52.49 ? 464 HOH   A O    1 
HETATM 5463 O O    . HOH   G 4 .   ? -1.310  4.649  29.085 1.00 33.62 ? 465 HOH   A O    1 
HETATM 5464 O O    . HOH   G 4 .   ? -6.292  11.670 -0.833 1.00 44.39 ? 466 HOH   A O    1 
HETATM 5465 O O    . HOH   G 4 .   ? -6.429  7.494  5.912  1.00 44.32 ? 467 HOH   A O    1 
HETATM 5466 O O    . HOH   G 4 .   ? -12.590 24.892 13.737 1.00 44.48 ? 468 HOH   A O    1 
HETATM 5467 O O    . HOH   G 4 .   ? -12.088 25.637 9.102  1.00 55.37 ? 469 HOH   A O    1 
HETATM 5468 O O    . HOH   G 4 .   ? -7.953  2.537  22.336 1.00 55.47 ? 470 HOH   A O    1 
HETATM 5469 O O    . HOH   G 4 .   ? 15.973  4.089  36.633 1.00 36.97 ? 471 HOH   A O    1 
HETATM 5470 O O    . HOH   G 4 .   ? 18.447  14.910 8.399  1.00 58.80 ? 472 HOH   A O    1 
HETATM 5471 O O    . HOH   G 4 .   ? 14.527  18.801 4.568  1.00 53.76 ? 473 HOH   A O    1 
HETATM 5472 O O    . HOH   G 4 .   ? 5.351   18.733 49.162 1.00 51.97 ? 474 HOH   A O    1 
HETATM 5473 O O    . HOH   G 4 .   ? 9.068   28.157 4.376  1.00 44.33 ? 475 HOH   A O    1 
HETATM 5474 O O    . HOH   G 4 .   ? 15.833  -1.651 20.237 1.00 52.52 ? 476 HOH   A O    1 
HETATM 5475 O O    . HOH   G 4 .   ? 13.008  5.331  5.124  1.00 50.23 ? 477 HOH   A O    1 
HETATM 5476 O O    . HOH   G 4 .   ? -4.996  7.242  30.115 1.00 39.40 ? 478 HOH   A O    1 
HETATM 5477 O O    . HOH   G 4 .   ? 6.542   4.297  7.298  1.00 44.86 ? 479 HOH   A O    1 
HETATM 5478 O O    . HOH   G 4 .   ? 11.512  27.749 10.408 1.00 52.14 ? 480 HOH   A O    1 
HETATM 5479 O O    . HOH   G 4 .   ? -10.684 9.465  4.625  1.00 37.78 ? 481 HOH   A O    1 
HETATM 5480 O O    . HOH   G 4 .   ? -11.624 24.118 -5.452 1.00 41.44 ? 482 HOH   A O    1 
HETATM 5481 O O    . HOH   G 4 .   ? 7.666   3.673  39.036 1.00 55.37 ? 483 HOH   A O    1 
HETATM 5482 O O    . HOH   G 4 .   ? 17.217  4.930  38.771 1.00 45.70 ? 484 HOH   A O    1 
HETATM 5483 O O    . HOH   G 4 .   ? 10.206  6.602  4.559  1.00 44.97 ? 485 HOH   A O    1 
HETATM 5484 O O    . HOH   G 4 .   ? 10.685  30.686 14.372 1.00 56.74 ? 486 HOH   A O    1 
HETATM 5485 O O    . HOH   G 4 .   ? -4.233  5.918  4.962  1.00 44.07 ? 487 HOH   A O    1 
HETATM 5486 O O    . HOH   G 4 .   ? 18.776  -0.742 19.996 1.00 64.91 ? 488 HOH   A O    1 
HETATM 5487 O O    . HOH   G 4 .   ? -4.040  4.923  28.651 1.00 38.39 ? 489 HOH   A O    1 
HETATM 5488 O O    . HOH   G 4 .   ? 1.972   3.938  6.703  1.00 48.66 ? 490 HOH   A O    1 
HETATM 5489 O O    . HOH   G 4 .   ? 19.299  11.901 8.843  1.00 40.94 ? 491 HOH   A O    1 
HETATM 5490 O O    . HOH   G 4 .   ? 20.667  7.960  12.620 1.00 42.32 ? 492 HOH   A O    1 
HETATM 5491 O O    . HOH   G 4 .   ? 4.322   13.498 53.609 1.00 55.77 ? 493 HOH   A O    1 
HETATM 5492 O O    . HOH   H 4 .   ? -31.630 8.423  7.083  1.00 57.99 ? 301 HOH   B O    1 
HETATM 5493 O O    . HOH   H 4 .   ? -6.862  28.369 17.178 1.00 51.33 ? 302 HOH   B O    1 
HETATM 5494 O O    . HOH   H 4 .   ? -22.044 30.579 32.077 1.00 32.46 ? 303 HOH   B O    1 
HETATM 5495 O O    . HOH   H 4 .   ? -20.214 5.214  41.683 1.00 50.15 ? 304 HOH   B O    1 
HETATM 5496 O O    . HOH   H 4 .   ? -27.333 23.091 26.470 1.00 44.00 ? 305 HOH   B O    1 
HETATM 5497 O O    . HOH   H 4 .   ? -29.688 11.136 16.322 1.00 41.42 ? 306 HOH   B O    1 
HETATM 5498 O O    . HOH   H 4 .   ? -12.080 5.353  29.107 1.00 41.54 ? 307 HOH   B O    1 
HETATM 5499 O O    . HOH   H 4 .   ? -14.228 19.485 34.149 1.00 26.94 ? 308 HOH   B O    1 
HETATM 5500 O O    . HOH   H 4 .   ? 25.326  22.335 32.648 1.00 39.68 ? 309 HOH   B O    1 
HETATM 5501 O O    . HOH   H 4 .   ? -19.942 33.179 35.659 1.00 36.10 ? 310 HOH   B O    1 
HETATM 5502 O O    . HOH   H 4 .   ? 14.434  20.154 32.322 1.00 31.63 ? 311 HOH   B O    1 
HETATM 5503 O O    . HOH   H 4 .   ? -14.492 30.055 22.721 1.00 49.19 ? 312 HOH   B O    1 
HETATM 5504 O O    . HOH   H 4 .   ? 24.178  20.773 26.358 1.00 46.95 ? 313 HOH   B O    1 
HETATM 5505 O O    . HOH   H 4 .   ? -17.147 16.477 35.226 1.00 31.53 ? 314 HOH   B O    1 
HETATM 5506 O O    . HOH   H 4 .   ? 3.066   17.485 48.539 1.00 32.63 ? 315 HOH   B O    1 
HETATM 5507 O O    . HOH   H 4 .   ? -14.458 14.832 44.549 1.00 45.13 ? 316 HOH   B O    1 
HETATM 5508 O O    . HOH   H 4 .   ? -21.445 7.279  17.867 1.00 34.17 ? 317 HOH   B O    1 
HETATM 5509 O O    . HOH   H 4 .   ? -7.407  26.961 22.956 1.00 27.93 ? 318 HOH   B O    1 
HETATM 5510 O O    . HOH   H 4 .   ? -12.914 28.131 49.323 1.00 43.29 ? 319 HOH   B O    1 
HETATM 5511 O O    . HOH   H 4 .   ? -14.247 10.845 27.047 1.00 18.30 ? 320 HOH   B O    1 
HETATM 5512 O O    . HOH   H 4 .   ? -1.323  21.303 30.709 1.00 19.91 ? 321 HOH   B O    1 
HETATM 5513 O O    . HOH   H 4 .   ? -31.100 15.762 11.134 1.00 49.48 ? 322 HOH   B O    1 
HETATM 5514 O O    . HOH   H 4 .   ? -24.975 22.909 17.851 1.00 35.36 ? 323 HOH   B O    1 
HETATM 5515 O O    . HOH   H 4 .   ? -5.947  20.202 37.128 1.00 24.38 ? 324 HOH   B O    1 
HETATM 5516 O O    . HOH   H 4 .   ? 3.533   23.512 49.485 1.00 31.87 ? 325 HOH   B O    1 
HETATM 5517 O O    . HOH   H 4 .   ? -8.128  31.953 22.451 1.00 50.33 ? 326 HOH   B O    1 
HETATM 5518 O O    . HOH   H 4 .   ? -13.039 6.506  25.968 1.00 36.22 ? 327 HOH   B O    1 
HETATM 5519 O O    . HOH   H 4 .   ? -30.392 20.430 21.583 1.00 43.34 ? 328 HOH   B O    1 
HETATM 5520 O O    . HOH   H 4 .   ? 8.672   17.555 45.085 1.00 48.69 ? 329 HOH   B O    1 
HETATM 5521 O O    . HOH   H 4 .   ? -1.498  27.446 26.494 1.00 38.82 ? 330 HOH   B O    1 
HETATM 5522 O O    . HOH   H 4 .   ? 0.751   27.621 34.998 1.00 39.29 ? 331 HOH   B O    1 
HETATM 5523 O O    . HOH   H 4 .   ? -10.813 28.261 41.330 1.00 22.22 ? 332 HOH   B O    1 
HETATM 5524 O O    . HOH   H 4 .   ? -20.517 4.553  32.399 1.00 42.08 ? 333 HOH   B O    1 
HETATM 5525 O O    . HOH   H 4 .   ? -8.293  33.835 42.488 1.00 45.95 ? 334 HOH   B O    1 
HETATM 5526 O O    . HOH   H 4 .   ? -1.504  20.505 28.093 1.00 23.55 ? 335 HOH   B O    1 
HETATM 5527 O O    . HOH   H 4 .   ? -5.528  26.039 50.761 1.00 34.23 ? 336 HOH   B O    1 
HETATM 5528 O O    . HOH   H 4 .   ? 5.753   26.904 43.130 1.00 43.14 ? 337 HOH   B O    1 
HETATM 5529 O O    A HOH   H 4 .   ? -7.312  25.350 20.333 0.55 28.37 ? 338 HOH   B O    1 
HETATM 5530 O O    B HOH   H 4 .   ? -11.296 25.554 16.370 0.45 41.43 ? 338 HOH   B O    1 
HETATM 5531 O O    . HOH   H 4 .   ? -8.318  18.929 36.771 1.00 29.39 ? 339 HOH   B O    1 
HETATM 5532 O O    . HOH   H 4 .   ? 19.369  15.910 38.666 1.00 46.28 ? 340 HOH   B O    1 
HETATM 5533 O O    . HOH   H 4 .   ? 23.355  16.285 32.881 1.00 31.74 ? 341 HOH   B O    1 
HETATM 5534 O O    . HOH   H 4 .   ? -20.266 7.465  22.853 1.00 36.45 ? 342 HOH   B O    1 
HETATM 5535 O O    . HOH   H 4 .   ? -5.608  23.881 54.604 1.00 39.86 ? 343 HOH   B O    1 
HETATM 5536 O O    . HOH   H 4 .   ? -18.962 23.904 48.384 1.00 36.63 ? 344 HOH   B O    1 
HETATM 5537 O O    . HOH   H 4 .   ? -25.545 23.922 35.542 1.00 29.73 ? 345 HOH   B O    1 
HETATM 5538 O O    . HOH   H 4 .   ? -9.337  33.567 39.503 1.00 31.41 ? 346 HOH   B O    1 
HETATM 5539 O O    . HOH   H 4 .   ? -20.113 5.863  24.772 1.00 56.71 ? 347 HOH   B O    1 
HETATM 5540 O O    . HOH   H 4 .   ? -24.680 24.941 33.150 1.00 29.18 ? 348 HOH   B O    1 
HETATM 5541 O O    . HOH   H 4 .   ? 12.000  22.332 38.232 1.00 44.21 ? 349 HOH   B O    1 
HETATM 5542 O O    . HOH   H 4 .   ? -17.424 23.784 33.755 1.00 19.62 ? 350 HOH   B O    1 
HETATM 5543 O O    . HOH   H 4 .   ? 2.978   22.746 30.931 1.00 34.77 ? 351 HOH   B O    1 
HETATM 5544 O O    . HOH   H 4 .   ? 2.463   10.196 43.380 1.00 42.20 ? 352 HOH   B O    1 
HETATM 5545 O O    . HOH   H 4 .   ? -19.115 10.610 10.093 1.00 45.95 ? 353 HOH   B O    1 
HETATM 5546 O O    . HOH   H 4 .   ? -29.192 21.777 28.854 1.00 41.00 ? 354 HOH   B O    1 
HETATM 5547 O O    . HOH   H 4 .   ? -15.584 6.529  17.425 1.00 39.86 ? 355 HOH   B O    1 
HETATM 5548 O O    . HOH   H 4 .   ? -26.824 25.460 40.831 1.00 45.11 ? 356 HOH   B O    1 
HETATM 5549 O O    . HOH   H 4 .   ? 0.213   27.249 47.077 1.00 27.36 ? 357 HOH   B O    1 
HETATM 5550 O O    . HOH   H 4 .   ? -24.149 19.306 43.492 1.00 29.55 ? 358 HOH   B O    1 
HETATM 5551 O O    . HOH   H 4 .   ? -22.637 19.097 39.538 1.00 23.04 ? 359 HOH   B O    1 
HETATM 5552 O O    . HOH   H 4 .   ? -20.373 5.119  36.407 1.00 34.43 ? 360 HOH   B O    1 
HETATM 5553 O O    . HOH   H 4 .   ? -3.946  25.337 47.732 1.00 24.21 ? 361 HOH   B O    1 
HETATM 5554 O O    . HOH   H 4 .   ? -16.490 29.268 38.975 1.00 23.14 ? 362 HOH   B O    1 
HETATM 5555 O O    . HOH   H 4 .   ? 7.215   24.591 42.521 1.00 34.10 ? 363 HOH   B O    1 
HETATM 5556 O O    . HOH   H 4 .   ? -19.817 17.669 36.147 1.00 26.65 ? 364 HOH   B O    1 
HETATM 5557 O O    . HOH   H 4 .   ? -29.160 16.086 41.566 1.00 43.87 ? 365 HOH   B O    1 
HETATM 5558 O O    . HOH   H 4 .   ? -15.648 5.753  31.523 1.00 37.48 ? 366 HOH   B O    1 
HETATM 5559 O O    . HOH   H 4 .   ? -31.857 7.975  36.539 1.00 40.61 ? 367 HOH   B O    1 
HETATM 5560 O O    . HOH   H 4 .   ? -6.820  31.565 31.362 1.00 25.47 ? 368 HOH   B O    1 
HETATM 5561 O O    . HOH   H 4 .   ? -17.721 12.277 44.434 1.00 45.86 ? 369 HOH   B O    1 
HETATM 5562 O O    . HOH   H 4 .   ? -0.119  27.648 32.472 1.00 43.33 ? 370 HOH   B O    1 
HETATM 5563 O O    . HOH   H 4 .   ? -11.786 32.896 26.541 1.00 35.86 ? 371 HOH   B O    1 
HETATM 5564 O O    . HOH   H 4 .   ? -31.733 13.644 32.738 1.00 28.77 ? 372 HOH   B O    1 
HETATM 5565 O O    . HOH   H 4 .   ? -18.752 15.100 16.752 1.00 20.11 ? 373 HOH   B O    1 
HETATM 5566 O O    . HOH   H 4 .   ? -13.601 16.331 35.600 1.00 34.25 ? 374 HOH   B O    1 
HETATM 5567 O O    . HOH   H 4 .   ? 0.119   31.168 32.746 1.00 43.52 ? 375 HOH   B O    1 
HETATM 5568 O O    . HOH   H 4 .   ? -22.688 8.071  41.529 1.00 33.54 ? 376 HOH   B O    1 
HETATM 5569 O O    . HOH   H 4 .   ? 21.200  20.053 34.431 1.00 49.72 ? 377 HOH   B O    1 
HETATM 5570 O O    . HOH   H 4 .   ? -17.102 22.314 39.181 1.00 31.36 ? 378 HOH   B O    1 
HETATM 5571 O O    . HOH   H 4 .   ? -19.376 20.834 38.627 1.00 28.94 ? 379 HOH   B O    1 
HETATM 5572 O O    . HOH   H 4 .   ? 18.024  18.345 37.738 1.00 46.87 ? 380 HOH   B O    1 
HETATM 5573 O O    . HOH   H 4 .   ? -10.691 32.822 37.186 1.00 26.06 ? 381 HOH   B O    1 
HETATM 5574 O O    . HOH   H 4 .   ? -12.820 35.246 40.883 1.00 42.15 ? 382 HOH   B O    1 
HETATM 5575 O O    . HOH   H 4 .   ? -4.926  29.718 32.351 1.00 21.99 ? 383 HOH   B O    1 
HETATM 5576 O O    . HOH   H 4 .   ? -30.183 18.450 17.155 1.00 40.21 ? 384 HOH   B O    1 
HETATM 5577 O O    . HOH   H 4 .   ? -7.092  35.645 36.424 1.00 26.08 ? 385 HOH   B O    1 
HETATM 5578 O O    . HOH   H 4 .   ? 20.976  14.897 29.771 1.00 31.59 ? 386 HOH   B O    1 
HETATM 5579 O O    . HOH   H 4 .   ? -18.554 6.050  30.935 1.00 32.94 ? 387 HOH   B O    1 
HETATM 5580 O O    . HOH   H 4 .   ? -28.983 9.716  27.993 1.00 36.73 ? 388 HOH   B O    1 
HETATM 5581 O O    . HOH   H 4 .   ? -2.632  9.899  35.559 1.00 28.79 ? 389 HOH   B O    1 
HETATM 5582 O O    . HOH   H 4 .   ? 11.054  23.123 27.839 1.00 39.14 ? 390 HOH   B O    1 
HETATM 5583 O O    . HOH   H 4 .   ? 4.936   27.727 34.642 1.00 54.45 ? 391 HOH   B O    1 
HETATM 5584 O O    . HOH   H 4 .   ? -16.022 26.268 36.202 1.00 27.20 ? 392 HOH   B O    1 
HETATM 5585 O O    . HOH   H 4 .   ? -29.177 7.607  32.371 1.00 34.72 ? 393 HOH   B O    1 
HETATM 5586 O O    . HOH   H 4 .   ? -21.442 11.697 11.186 1.00 44.05 ? 394 HOH   B O    1 
HETATM 5587 O O    . HOH   H 4 .   ? 0.011   29.541 43.570 1.00 33.81 ? 395 HOH   B O    1 
HETATM 5588 O O    . HOH   H 4 .   ? -23.091 28.064 26.463 1.00 51.04 ? 396 HOH   B O    1 
HETATM 5589 O O    . HOH   H 4 .   ? -4.836  33.160 25.468 1.00 58.27 ? 397 HOH   B O    1 
HETATM 5590 O O    . HOH   H 4 .   ? 13.726  20.714 41.162 1.00 49.32 ? 398 HOH   B O    1 
HETATM 5591 O O    . HOH   H 4 .   ? -0.463  31.002 38.365 1.00 47.24 ? 399 HOH   B O    1 
HETATM 5592 O O    . HOH   H 4 .   ? -22.736 31.879 40.753 1.00 37.55 ? 400 HOH   B O    1 
HETATM 5593 O O    . HOH   H 4 .   ? -15.185 26.413 19.548 1.00 32.14 ? 401 HOH   B O    1 
HETATM 5594 O O    . HOH   H 4 .   ? -23.477 6.594  21.986 1.00 47.43 ? 402 HOH   B O    1 
HETATM 5595 O O    . HOH   H 4 .   ? 19.419  20.671 25.830 1.00 50.81 ? 403 HOH   B O    1 
HETATM 5596 O O    . HOH   H 4 .   ? -26.847 21.640 34.075 1.00 47.89 ? 404 HOH   B O    1 
HETATM 5597 O O    . HOH   H 4 .   ? -20.269 17.877 38.776 1.00 30.72 ? 405 HOH   B O    1 
HETATM 5598 O O    . HOH   H 4 .   ? -5.019  33.758 36.417 1.00 31.67 ? 406 HOH   B O    1 
HETATM 5599 O O    . HOH   H 4 .   ? -26.322 11.738 21.719 1.00 34.54 ? 407 HOH   B O    1 
HETATM 5600 O O    . HOH   H 4 .   ? -22.079 13.189 9.938  1.00 49.04 ? 408 HOH   B O    1 
HETATM 5601 O O    . HOH   H 4 .   ? -24.971 25.739 24.822 1.00 41.22 ? 409 HOH   B O    1 
HETATM 5602 O O    . HOH   H 4 .   ? -16.057 30.560 24.366 1.00 43.39 ? 410 HOH   B O    1 
HETATM 5603 O O    . HOH   H 4 .   ? -17.444 29.529 45.177 1.00 43.26 ? 411 HOH   B O    1 
HETATM 5604 O O    . HOH   H 4 .   ? -3.763  9.755  30.808 1.00 32.37 ? 412 HOH   B O    1 
HETATM 5605 O O    . HOH   H 4 .   ? -10.674 6.879  40.314 1.00 36.51 ? 413 HOH   B O    1 
HETATM 5606 O O    . HOH   H 4 .   ? -18.286 8.136  21.293 1.00 32.65 ? 414 HOH   B O    1 
HETATM 5607 O O    . HOH   H 4 .   ? -25.827 8.008  39.679 1.00 41.82 ? 415 HOH   B O    1 
HETATM 5608 O O    . HOH   H 4 .   ? -17.068 32.198 42.090 1.00 43.07 ? 416 HOH   B O    1 
HETATM 5609 O O    . HOH   H 4 .   ? -16.296 7.593  41.838 1.00 35.27 ? 417 HOH   B O    1 
HETATM 5610 O O    . HOH   H 4 .   ? -2.889  30.001 52.640 1.00 39.28 ? 418 HOH   B O    1 
HETATM 5611 O O    . HOH   H 4 .   ? 7.960   19.988 47.466 1.00 35.98 ? 419 HOH   B O    1 
HETATM 5612 O O    . HOH   H 4 .   ? -11.992 30.688 49.076 1.00 48.75 ? 420 HOH   B O    1 
HETATM 5613 O O    . HOH   H 4 .   ? 15.508  21.713 25.971 1.00 45.89 ? 421 HOH   B O    1 
HETATM 5614 O O    . HOH   H 4 .   ? -14.347 18.174 37.458 1.00 35.17 ? 422 HOH   B O    1 
HETATM 5615 O O    . HOH   H 4 .   ? 19.158  20.789 32.366 1.00 42.54 ? 423 HOH   B O    1 
HETATM 5616 O O    . HOH   H 4 .   ? -13.709 28.638 19.442 1.00 60.84 ? 424 HOH   B O    1 
HETATM 5617 O O    . HOH   H 4 .   ? -4.617  25.775 19.567 1.00 37.60 ? 425 HOH   B O    1 
HETATM 5618 O O    . HOH   H 4 .   ? -22.912 17.435 11.534 1.00 40.12 ? 426 HOH   B O    1 
HETATM 5619 O O    . HOH   H 4 .   ? -22.461 29.192 34.423 1.00 26.37 ? 427 HOH   B O    1 
HETATM 5620 O O    . HOH   H 4 .   ? -30.892 6.356  27.938 1.00 58.03 ? 428 HOH   B O    1 
HETATM 5621 O O    A HOH   H 4 .   ? -5.745  32.684 45.351 0.67 44.80 ? 429 HOH   B O    1 
HETATM 5622 O O    B HOH   H 4 .   ? -5.199  31.816 38.317 0.33 19.63 ? 429 HOH   B O    1 
HETATM 5623 O O    . HOH   H 4 .   ? 9.687   23.664 41.231 1.00 35.55 ? 430 HOH   B O    1 
HETATM 5624 O O    . HOH   H 4 .   ? -12.366 34.905 43.699 1.00 54.00 ? 431 HOH   B O    1 
HETATM 5625 O O    . HOH   H 4 .   ? -26.290 7.705  21.478 1.00 47.96 ? 432 HOH   B O    1 
HETATM 5626 O O    . HOH   H 4 .   ? 19.991  9.565  37.276 1.00 38.01 ? 433 HOH   B O    1 
HETATM 5627 O O    . HOH   H 4 .   ? -18.277 3.575  35.945 1.00 41.32 ? 434 HOH   B O    1 
HETATM 5628 O O    . HOH   H 4 .   ? -0.370  27.400 37.963 1.00 29.89 ? 435 HOH   B O    1 
HETATM 5629 O O    . HOH   H 4 .   ? -2.932  18.200 28.084 1.00 21.59 ? 436 HOH   B O    1 
HETATM 5630 O O    . HOH   H 4 .   ? 1.176   28.987 40.022 1.00 54.58 ? 437 HOH   B O    1 
HETATM 5631 O O    . HOH   H 4 .   ? -26.424 8.599  18.508 1.00 47.29 ? 438 HOH   B O    1 
HETATM 5632 O O    . HOH   H 4 .   ? -25.708 14.387 43.552 1.00 44.33 ? 439 HOH   B O    1 
HETATM 5633 O O    . HOH   H 4 .   ? -9.671  6.282  29.024 1.00 38.96 ? 440 HOH   B O    1 
HETATM 5634 O O    . HOH   H 4 .   ? -7.588  30.138 51.865 1.00 47.75 ? 441 HOH   B O    1 
HETATM 5635 O O    . HOH   H 4 .   ? -14.302 21.437 36.792 1.00 33.52 ? 442 HOH   B O    1 
HETATM 5636 O O    . HOH   H 4 .   ? -15.364 23.714 37.039 1.00 33.75 ? 443 HOH   B O    1 
HETATM 5637 O O    . HOH   H 4 .   ? -23.774 30.511 38.504 1.00 47.03 ? 444 HOH   B O    1 
HETATM 5638 O O    . HOH   H 4 .   ? 0.569   23.224 30.155 1.00 32.52 ? 445 HOH   B O    1 
HETATM 5639 O O    . HOH   H 4 .   ? -7.620  6.707  28.715 1.00 48.19 ? 446 HOH   B O    1 
HETATM 5640 O O    . HOH   H 4 .   ? -16.170 28.376 32.788 1.00 33.44 ? 447 HOH   B O    1 
HETATM 5641 O O    . HOH   H 4 .   ? -9.137  27.895 14.323 1.00 49.99 ? 448 HOH   B O    1 
HETATM 5642 O O    . HOH   H 4 .   ? -1.590  16.047 29.069 1.00 24.30 ? 449 HOH   B O    1 
HETATM 5643 O O    . HOH   H 4 .   ? 15.338  18.401 40.416 1.00 49.42 ? 450 HOH   B O    1 
HETATM 5644 O O    . HOH   H 4 .   ? -0.680  25.175 54.168 1.00 33.99 ? 451 HOH   B O    1 
HETATM 5645 O O    . HOH   H 4 .   ? 0.272   25.852 30.599 1.00 34.17 ? 452 HOH   B O    1 
HETATM 5646 O O    . HOH   H 4 .   ? -30.380 10.250 6.171  1.00 57.74 ? 453 HOH   B O    1 
HETATM 5647 O O    . HOH   H 4 .   ? -22.406 31.616 36.132 1.00 39.68 ? 454 HOH   B O    1 
HETATM 5648 O O    . HOH   H 4 .   ? -23.159 7.139  15.232 1.00 48.30 ? 455 HOH   B O    1 
HETATM 5649 O O    . HOH   H 4 .   ? -4.929  35.997 39.775 1.00 50.41 ? 456 HOH   B O    1 
HETATM 5650 O O    . HOH   H 4 .   ? -5.656  26.695 24.802 1.00 37.66 ? 457 HOH   B O    1 
HETATM 5651 O O    . HOH   H 4 .   ? -22.729 8.066  46.453 1.00 63.64 ? 458 HOH   B O    1 
HETATM 5652 O O    . HOH   H 4 .   ? -17.123 28.746 23.118 1.00 57.27 ? 459 HOH   B O    1 
HETATM 5653 O O    . HOH   H 4 .   ? -14.458 7.373  15.313 1.00 49.18 ? 460 HOH   B O    1 
HETATM 5654 O O    . HOH   H 4 .   ? -32.955 9.790  10.560 1.00 38.99 ? 461 HOH   B O    1 
HETATM 5655 O O    . HOH   H 4 .   ? -17.507 27.590 20.818 1.00 63.96 ? 462 HOH   B O    1 
HETATM 5656 O O    . HOH   H 4 .   ? -19.172 6.864  14.714 1.00 52.20 ? 463 HOH   B O    1 
HETATM 5657 O O    . HOH   H 4 .   ? -30.064 20.655 18.718 1.00 45.86 ? 464 HOH   B O    1 
HETATM 5658 O O    . HOH   H 4 .   ? 2.639   28.057 47.597 1.00 39.93 ? 465 HOH   B O    1 
HETATM 5659 O O    . HOH   H 4 .   ? -6.380  29.497 21.892 1.00 51.37 ? 466 HOH   B O    1 
HETATM 5660 O O    . HOH   H 4 .   ? 4.651   25.934 49.808 1.00 50.75 ? 467 HOH   B O    1 
HETATM 5661 O O    . HOH   H 4 .   ? -12.691 4.349  32.656 1.00 65.05 ? 468 HOH   B O    1 
HETATM 5662 O O    . HOH   H 4 .   ? -4.244  30.778 23.460 1.00 55.67 ? 469 HOH   B O    1 
HETATM 5663 O O    . HOH   H 4 .   ? -2.006  36.160 33.194 1.00 49.71 ? 470 HOH   B O    1 
HETATM 5664 O O    . HOH   H 4 .   ? -18.861 33.017 38.132 1.00 28.47 ? 471 HOH   B O    1 
HETATM 5665 O O    . HOH   H 4 .   ? -14.971 4.334  18.687 1.00 54.87 ? 472 HOH   B O    1 
HETATM 5666 O O    . HOH   H 4 .   ? -24.574 27.547 33.340 1.00 40.71 ? 473 HOH   B O    1 
HETATM 5667 O O    . HOH   H 4 .   ? 6.611   28.163 40.065 1.00 57.72 ? 474 HOH   B O    1 
HETATM 5668 O O    . HOH   H 4 .   ? -27.921 26.689 38.521 1.00 47.83 ? 475 HOH   B O    1 
HETATM 5669 O O    . HOH   H 4 .   ? 16.763  13.380 39.526 1.00 45.57 ? 476 HOH   B O    1 
HETATM 5670 O O    . HOH   H 4 .   ? -6.153  27.813 52.522 1.00 52.11 ? 477 HOH   B O    1 
HETATM 5671 O O    . HOH   H 4 .   ? 0.155   24.831 26.029 1.00 38.44 ? 478 HOH   B O    1 
HETATM 5672 O O    . HOH   H 4 .   ? -22.547 4.369  38.175 1.00 50.73 ? 479 HOH   B O    1 
HETATM 5673 O O    . HOH   H 4 .   ? -18.978 14.026 49.501 1.00 44.60 ? 480 HOH   B O    1 
HETATM 5674 O O    . HOH   H 4 .   ? -23.766 22.662 15.526 1.00 42.70 ? 481 HOH   B O    1 
HETATM 5675 O O    . HOH   H 4 .   ? -18.592 2.768  33.328 1.00 59.30 ? 482 HOH   B O    1 
HETATM 5676 O O    . HOH   H 4 .   ? -29.108 8.400  3.959  1.00 59.50 ? 483 HOH   B O    1 
HETATM 5677 O O    . HOH   H 4 .   ? -29.095 22.232 24.390 1.00 51.09 ? 484 HOH   B O    1 
HETATM 5678 O O    . HOH   H 4 .   ? 1.170   30.207 36.112 1.00 57.24 ? 485 HOH   B O    1 
HETATM 5679 O O    . HOH   H 4 .   ? -25.262 20.265 45.828 1.00 45.38 ? 486 HOH   B O    1 
HETATM 5680 O O    . HOH   H 4 .   ? -16.548 9.703  44.072 1.00 50.38 ? 487 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   . SER A 31  ? 0.8185 0.9002 0.6662 0.2314  -0.0008 0.1120  11  SER A N   
2    C CA  . SER A 31  ? 0.7933 0.8986 0.6272 0.2390  -0.0091 0.0981  11  SER A CA  
3    C C   . SER A 31  ? 0.7127 0.8801 0.5135 0.2755  -0.0044 0.0901  11  SER A C   
4    O O   . SER A 31  ? 0.6892 0.8693 0.4293 0.2895  0.0098  0.0914  11  SER A O   
5    C CB  . SER A 31  ? 0.8252 0.9117 0.6869 0.2179  -0.0159 0.0948  11  SER A CB  
7    N N   . GLU A 32  ? 0.6445 0.8714 0.4678 0.3070  -0.0001 0.0674  12  GLU A N   
8    C CA  . GLU A 32  ? 0.6107 0.8647 0.4469 0.3118  0.0234  0.0552  12  GLU A CA  
9    C C   . GLU A 32  ? 0.5486 0.8641 0.4315 0.3239  0.0138  0.0449  12  GLU A C   
10   O O   . GLU A 32  ? 0.5711 0.8590 0.3666 0.3514  0.0140  0.0264  12  GLU A O   
11   C CB  . GLU A 32  ? 0.6134 0.8648 0.4849 0.3055  0.0374  0.0537  12  GLU A CB  
14   N N   . ASN A 33  ? 0.4879 0.8673 0.5333 0.3053  0.0011  0.0594  13  ASN A N   
15   C CA  . ASN A 33  ? 0.4413 0.8650 0.5561 0.2608  -0.0347 0.0588  13  ASN A CA  
16   C C   . ASN A 33  ? 0.4231 0.8327 0.5113 0.2276  -0.0423 0.0461  13  ASN A C   
17   O O   . ASN A 33  ? 0.3365 0.8372 0.5071 0.1797  -0.0452 0.0349  13  ASN A O   
18   C CB  . ASN A 33  ? 0.4555 0.8943 0.6019 0.2084  -0.0238 0.0464  13  ASN A CB  
21   N N   . ARG A 34  ? 0.4887 0.7917 0.4245 0.1971  -0.0325 0.0304  14  ARG A N   
22   C CA  . ARG A 34  ? 0.5074 0.7378 0.3848 0.1821  -0.0342 0.0325  14  ARG A CA  
23   C C   . ARG A 34  ? 0.4609 0.6813 0.3489 0.1892  -0.0434 0.0359  14  ARG A C   
24   O O   . ARG A 34  ? 0.4405 0.6621 0.3411 0.1747  -0.0379 0.0474  14  ARG A O   
25   C CB  . ARG A 34  ? 0.5712 0.7413 0.3983 0.1606  -0.0149 0.0234  14  ARG A CB  
28   N N   . ALA A 35  ? 0.4585 0.6423 0.2932 0.1745  -0.0007 0.0314  15  ALA A N   
29   C CA  . ALA A 35  ? 0.4647 0.6050 0.2770 0.1695  0.0174  0.0086  15  ALA A CA  
30   C C   . ALA A 35  ? 0.4161 0.5662 0.2528 0.1646  0.0244  0.0219  15  ALA A C   
31   O O   . ALA A 35  ? 0.3631 0.5477 0.2683 0.1146  0.0266  0.0465  15  ALA A O   
32   C CB  . ALA A 35  ? 0.4984 0.6066 0.3262 0.1761  0.0057  0.0168  15  ALA A CB  
38   N N   . GLN A 36  ? 0.4200 0.5789 0.2387 0.1780  0.0360  0.0200  16  GLN A N   
39   C CA  . GLN A 36  ? 0.3738 0.6026 0.2822 0.1644  0.0534  0.0269  16  GLN A CA  
40   C C   . GLN A 36  ? 0.3087 0.5978 0.2823 0.1164  0.0493  0.0480  16  GLN A C   
41   O O   . GLN A 36  ? 0.3021 0.5847 0.2774 0.1139  0.0199  0.0653  16  GLN A O   
42   C CB  . GLN A 36  ? 0.4131 0.6286 0.3015 0.1893  0.0491  -0.0130 16  GLN A CB  
43   C CG  . GLN A 36  ? 0.5342 0.6494 0.3855 0.1935  0.0766  -0.0341 16  GLN A CG  
44   C CD  . GLN A 36  ? 0.5989 0.6774 0.4690 0.1916  0.0984  -0.0222 16  GLN A CD  
45   O OE1 . GLN A 36  ? 0.6464 0.6973 0.5050 0.1649  0.0878  -0.0191 16  GLN A OE1 
46   N NE2 . GLN A 36  ? 0.5962 0.6782 0.5073 0.2224  0.0896  0.0018  16  GLN A NE2 
55   N N   . VAL A 37  ? 0.3080 0.6157 0.2962 0.0702  0.0340  0.0405  17  VAL A N   
56   C CA  . VAL A 37  ? 0.2961 0.6265 0.3509 0.0305  0.0180  0.0424  17  VAL A CA  
57   C C   . VAL A 37  ? 0.2660 0.6067 0.3618 0.0015  0.0110  0.0429  17  VAL A C   
58   O O   . VAL A 37  ? 0.2922 0.6104 0.3448 -0.0218 -0.0254 0.0475  17  VAL A O   
59   C CB  . VAL A 37  ? 0.3665 0.6495 0.4367 0.0208  0.0358  0.0480  17  VAL A CB  
60   C CG1 . VAL A 37  ? 0.4170 0.6527 0.4723 0.0112  -0.0182 0.0521  17  VAL A CG1 
61   C CG2 . VAL A 37  ? 0.3567 0.6668 0.4533 0.0239  0.0668  0.0457  17  VAL A CG2 
71   N N   . ALA A 38  ? 0.2583 0.5675 0.2953 0.0028  0.0097  0.0213  18  ALA A N   
72   C CA  . ALA A 38  ? 0.2989 0.5243 0.2685 0.0417  -0.0009 -0.0073 18  ALA A CA  
73   C C   . ALA A 38  ? 0.2736 0.4657 0.2713 0.0450  -0.0010 0.0131  18  ALA A C   
74   O O   . ALA A 38  ? 0.2962 0.4709 0.2578 0.0245  0.0119  0.0424  18  ALA A O   
75   C CB  . ALA A 38  ? 0.3108 0.5369 0.2557 0.0553  -0.0024 -0.0204 18  ALA A CB  
81   N N   . ALA A 39  ? 0.2671 0.4230 0.2490 0.0282  0.0252  0.0005  19  ALA A N   
82   C CA  . ALA A 39  ? 0.2644 0.4131 0.2638 0.0215  0.0440  -0.0003 19  ALA A CA  
83   C C   . ALA A 39  ? 0.2614 0.4222 0.2396 0.0062  0.0426  0.0377  19  ALA A C   
84   O O   . ALA A 39  ? 0.2338 0.3962 0.2748 0.0260  0.0172  0.0366  19  ALA A O   
85   C CB  . ALA A 39  ? 0.3079 0.4091 0.2871 0.0623  0.0488  0.0160  19  ALA A CB  
91   N N   . ARG A 40  ? 0.2630 0.4441 0.2334 0.0201  0.0398  0.0434  20  ARG A N   
92   C CA  . ARG A 40  ? 0.2354 0.4264 0.2454 0.0342  0.0274  0.0415  20  ARG A CA  
93   C C   . ARG A 40  ? 0.2382 0.3866 0.2732 0.0256  0.0344  0.0264  20  ARG A C   
94   O O   . ARG A 40  ? 0.2570 0.4006 0.2679 0.0132  0.0107  0.0533  20  ARG A O   
95   C CB  . ARG A 40  ? 0.2468 0.4389 0.2692 0.0269  0.0394  0.0587  20  ARG A CB  
96   C CG  . ARG A 40  ? 0.2710 0.4354 0.2605 -0.0093 0.0546  0.0347  20  ARG A CG  
97   C CD  . ARG A 40  ? 0.2822 0.4365 0.2620 -0.0272 0.0304  0.0149  20  ARG A CD  
98   N NE  . ARG A 40  ? 0.3018 0.4682 0.2511 -0.0049 0.0187  0.0208  20  ARG A NE  
99   C CZ  . ARG A 40  ? 0.2867 0.4915 0.2480 0.0122  0.0422  0.0116  20  ARG A CZ  
100  N NH1 . ARG A 40  ? 0.3258 0.5211 0.2374 0.0142  0.0009  0.0097  20  ARG A NH1 
101  N NH2 . ARG A 40  ? 0.2955 0.4971 0.2430 0.0508  0.0388  -0.0017 20  ARG A NH2 
142  N N   . ASN A 43  ? 0.2339 0.2751 0.2319 -0.0033 0.0309  0.0001  23  ASN A N   
143  C CA  . ASN A 43  ? 0.2488 0.2916 0.2137 -0.0189 0.0227  0.0001  23  ASN A CA  
144  C C   . ASN A 43  ? 0.2269 0.2852 0.2200 -0.0189 0.0265  -0.0149 23  ASN A C   
145  O O   . ASN A 43  ? 0.2316 0.2675 0.2281 0.0030  0.0243  0.0005  23  ASN A O   
146  C CB  . ASN A 43  ? 0.2500 0.3015 0.2089 0.0096  0.0346  0.0006  23  ASN A CB  
147  C CG  . ASN A 43  ? 0.2240 0.3214 0.2289 0.0141  0.0394  0.0245  23  ASN A CG  
148  O OD1 . ASN A 43  ? 0.2498 0.2981 0.2611 0.0069  0.0520  0.0176  23  ASN A OD1 
149  N ND2 . ASN A 43  ? 0.2472 0.3595 0.2497 0.0451  0.0430  0.0398  23  ASN A ND2 
156  N N   A ARG A 44  ? 0.2495 0.2915 0.2551 0.0038  0.0090  0.0061  24  ARG A N   
157  N N   B ARG A 44  ? 0.2343 0.2883 0.2170 -0.0193 0.0290  -0.0140 24  ARG A N   
158  C CA  A ARG A 44  ? 0.2517 0.3076 0.2847 0.0048  -0.0106 0.0291  24  ARG A CA  
159  C CA  B ARG A 44  ? 0.2072 0.3013 0.2371 -0.0297 0.0397  -0.0062 24  ARG A CA  
160  C C   A ARG A 44  ? 0.2438 0.3035 0.2728 0.0130  -0.0049 0.0036  24  ARG A C   
161  C C   B ARG A 44  ? 0.2224 0.2911 0.2295 -0.0369 0.0478  -0.0038 24  ARG A C   
162  O O   A ARG A 44  ? 0.2534 0.2916 0.2862 0.0417  -0.0264 0.0042  24  ARG A O   
163  O O   B ARG A 44  ? 0.2508 0.2703 0.2265 -0.0588 0.0779  0.0220  24  ARG A O   
164  C CB  A ARG A 44  ? 0.2972 0.3312 0.3279 -0.0169 -0.0205 0.0486  24  ARG A CB  
165  C CB  B ARG A 44  ? 0.2011 0.3290 0.2741 -0.0408 0.0505  -0.0260 24  ARG A CB  
166  C CG  A ARG A 44  ? 0.3507 0.3621 0.3915 -0.0334 -0.0120 0.0853  24  ARG A CG  
167  C CG  B ARG A 44  ? 0.1852 0.3627 0.4010 -0.0523 0.0537  0.0017  24  ARG A CG  
168  C CD  A ARG A 44  ? 0.4111 0.3959 0.4042 -0.0518 0.0107  0.1037  24  ARG A CD  
169  C CD  B ARG A 44  ? 0.2789 0.4270 0.4772 -0.0640 0.0694  0.0011  24  ARG A CD  
170  N NE  A ARG A 44  ? 0.4629 0.4115 0.4137 -0.0699 0.0401  0.0909  24  ARG A NE  
171  N NE  B ARG A 44  ? 0.3655 0.4780 0.5156 -0.0934 0.0506  -0.0328 24  ARG A NE  
172  C CZ  A ARG A 44  ? 0.4698 0.4296 0.3905 -0.0609 0.0788  0.0847  24  ARG A CZ  
173  C CZ  B ARG A 44  ? 0.4095 0.5082 0.5072 -0.0607 0.0259  -0.0446 24  ARG A CZ  
174  N NH1 A ARG A 44  ? 0.4722 0.4511 0.3841 -0.0380 0.1203  0.0901  24  ARG A NH1 
175  N NH1 B ARG A 44  ? 0.3994 0.5115 0.4313 -0.0389 -0.0138 -0.0966 24  ARG A NH1 
176  N NH2 A ARG A 44  ? 0.4777 0.4155 0.3633 -0.0847 0.1019  0.0918  24  ARG A NH2 
177  N NH2 B ARG A 44  ? 0.4608 0.5321 0.5758 -0.0463 0.0382  -0.0207 24  ARG A NH2 
204  N N   . LYS A 45  ? 0.2432 0.3065 0.2317 -0.0054 0.0187  -0.0113 25  LYS A N   
205  C CA  . LYS A 45  ? 0.2650 0.3092 0.2649 -0.0052 0.0253  -0.0300 25  LYS A CA  
206  C C   . LYS A 45  ? 0.2400 0.2704 0.2438 0.0047  0.0484  -0.0275 25  LYS A C   
207  O O   . LYS A 45  ? 0.2468 0.2795 0.2483 -0.0065 0.0389  -0.0248 25  LYS A O   
208  C CB  . LYS A 45  ? 0.2937 0.3481 0.2857 -0.0115 0.0135  -0.0235 25  LYS A CB  
209  C CG  . LYS A 45  ? 0.3913 0.4141 0.2999 -0.0230 0.0275  -0.0137 25  LYS A CG  
215  N N   . ILE A 46  ? 0.2284 0.2502 0.2274 -0.0032 0.0408  -0.0078 26  ILE A N   
216  C CA  . ILE A 46  ? 0.2303 0.2592 0.2268 -0.0010 0.0633  -0.0027 26  ILE A CA  
217  C C   . ILE A 46  ? 0.2201 0.2392 0.2051 0.0023  0.0527  0.0130  26  ILE A C   
218  O O   . ILE A 46  ? 0.2235 0.2479 0.2175 0.0040  0.0397  0.0102  26  ILE A O   
219  C CB  . ILE A 46  ? 0.2466 0.2819 0.2312 -0.0122 0.0621  0.0106  26  ILE A CB  
220  C CG1 . ILE A 46  ? 0.2663 0.3550 0.2404 -0.0424 0.0658  0.0347  26  ILE A CG1 
221  C CG2 . ILE A 46  ? 0.2568 0.2572 0.2598 -0.0189 0.0622  0.0172  26  ILE A CG2 
222  C CD1 . ILE A 46  ? 0.3159 0.4218 0.2708 -0.0187 0.1008  0.0729  26  ILE A CD1 
234  N N   . VAL A 47  ? 0.2322 0.2421 0.2003 0.0074  0.0616  0.0113  27  VAL A N   
235  C CA  . VAL A 47  ? 0.2211 0.2442 0.2264 -0.0144 0.0508  0.0075  27  VAL A CA  
236  C C   . VAL A 47  ? 0.2257 0.2484 0.2359 -0.0009 0.0553  -0.0080 27  VAL A C   
237  O O   . VAL A 47  ? 0.2203 0.2437 0.2326 0.0057  0.0504  -0.0055 27  VAL A O   
238  C CB  . VAL A 47  ? 0.2160 0.2468 0.2210 0.0073  0.0548  -0.0096 27  VAL A CB  
239  C CG1 . VAL A 47  ? 0.2316 0.2520 0.2261 0.0199  0.0540  0.0001  27  VAL A CG1 
240  C CG2 . VAL A 47  ? 0.2362 0.2605 0.2311 0.0256  0.0449  0.0001  27  VAL A CG2 
250  N N   . GLU A 48  ? 0.2415 0.2411 0.2411 0.0006  0.0491  -0.0115 28  GLU A N   
251  C CA  . GLU A 48  ? 0.2372 0.2469 0.2670 -0.0058 0.0383  -0.0026 28  GLU A CA  
252  C C   . GLU A 48  ? 0.2395 0.2440 0.2549 0.0071  0.0434  -0.0217 28  GLU A C   
253  O O   . GLU A 48  ? 0.2602 0.2240 0.2639 0.0104  0.0365  -0.0150 28  GLU A O   
254  C CB  . GLU A 48  ? 0.2646 0.2950 0.3028 -0.0169 0.0412  -0.0003 28  GLU A CB  
255  C CG  . GLU A 48  ? 0.3281 0.3593 0.3581 -0.0156 0.0683  0.0064  28  GLU A CG  
256  C CD  . GLU A 48  ? 0.3761 0.4560 0.4691 -0.0207 0.0832  -0.0082 28  GLU A CD  
257  O OE1 . GLU A 48  ? 0.3835 0.4828 0.4989 -0.0275 0.0901  0.0167  28  GLU A OE1 
258  O OE2 . GLU A 48  ? 0.3974 0.5017 0.5505 -0.0683 0.0744  -0.0678 28  GLU A OE2 
265  N N   A GLN A 49  ? 0.2313 0.2524 0.2486 -0.0092 0.0634  -0.0321 29  GLN A N   
266  N N   C GLN A 49  ? 0.2354 0.2394 0.2436 -0.0036 0.0487  -0.0241 29  GLN A N   
267  C CA  A GLN A 49  ? 0.2354 0.2681 0.2366 -0.0082 0.0694  -0.0255 29  GLN A CA  
268  C CA  C GLN A 49  ? 0.2410 0.2394 0.2480 -0.0106 0.0586  -0.0192 29  GLN A CA  
269  C C   A GLN A 49  ? 0.2265 0.2435 0.2608 0.0128  0.0501  -0.0247 29  GLN A C   
270  C C   C GLN A 49  ? 0.2143 0.2121 0.2466 -0.0095 0.0641  -0.0222 29  GLN A C   
271  O O   A GLN A 49  ? 0.2348 0.2638 0.2910 0.0293  0.0502  -0.0200 29  GLN A O   
272  O O   C GLN A 49  ? 0.2041 0.2009 0.2459 -0.0186 0.0903  -0.0213 29  GLN A O   
273  C CB  A GLN A 49  ? 0.2231 0.3055 0.2469 -0.0084 0.0627  -0.0322 29  GLN A CB  
274  C CB  C GLN A 49  ? 0.2666 0.2701 0.2812 -0.0069 0.0399  -0.0139 29  GLN A CB  
275  C CG  A GLN A 49  ? 0.2273 0.3409 0.2732 -0.0028 0.0831  -0.0224 29  GLN A CG  
276  C CG  C GLN A 49  ? 0.3200 0.3038 0.3080 -0.0066 0.0515  0.0022  29  GLN A CG  
277  C CD  A GLN A 49  ? 0.2982 0.3917 0.2690 -0.0070 0.0949  -0.0078 29  GLN A CD  
278  C CD  C GLN A 49  ? 0.3394 0.3345 0.2916 0.0003  0.0004  0.0039  29  GLN A CD  
279  O OE1 A GLN A 49  ? 0.3372 0.4162 0.2761 -0.0356 0.0801  -0.0492 29  GLN A OE1 
280  O OE1 C GLN A 49  ? 0.3815 0.3437 0.2768 0.0100  0.0125  -0.0474 29  GLN A OE1 
281  N NE2 A GLN A 49  ? 0.2738 0.3954 0.2456 -0.0090 0.1161  0.0148  29  GLN A NE2 
282  N NE2 C GLN A 49  ? 0.4056 0.3615 0.3173 0.0164  0.0637  0.0449  29  GLN A NE2 
299  N N   . TYR A 50  ? 0.2163 0.2116 0.2298 -0.0030 0.0489  -0.0106 30  TYR A N   
300  C CA  . TYR A 50  ? 0.2131 0.1944 0.2477 -0.0076 0.0518  0.0053  30  TYR A CA  
301  C C   . TYR A 50  ? 0.2307 0.1820 0.2229 -0.0010 0.0666  -0.0010 30  TYR A C   
302  O O   . TYR A 50  ? 0.2260 0.1985 0.2386 -0.0048 0.0459  -0.0102 30  TYR A O   
303  C CB  . TYR A 50  ? 0.2474 0.1748 0.2399 0.0012  0.0631  0.0194  30  TYR A CB  
304  C CG  . TYR A 50  ? 0.2340 0.1818 0.2351 -0.0029 0.0615  -0.0070 30  TYR A CG  
305  C CD1 . TYR A 50  ? 0.2331 0.1721 0.2341 -0.0007 0.0719  -0.0190 30  TYR A CD1 
306  C CD2 . TYR A 50  ? 0.2450 0.1968 0.2548 -0.0095 0.0632  -0.0077 30  TYR A CD2 
307  C CE1 . TYR A 50  ? 0.2259 0.2038 0.2297 -0.0317 0.0626  -0.0167 30  TYR A CE1 
308  C CE2 . TYR A 50  ? 0.2444 0.2254 0.2567 -0.0206 0.0948  -0.0202 30  TYR A CE2 
309  C CZ  . TYR A 50  ? 0.2309 0.2310 0.2572 -0.0320 0.0662  -0.0366 30  TYR A CZ  
310  O OH  . TYR A 50  ? 0.2778 0.2446 0.2814 -0.0433 0.0674  -0.0372 30  TYR A OH  
321  N N   . MET A 51  ? 0.2256 0.1786 0.2272 -0.0050 0.0741  -0.0024 31  MET A N   
322  C CA  . MET A 51  ? 0.2201 0.1647 0.2427 -0.0119 0.0612  -0.0098 31  MET A CA  
323  C C   . MET A 51  ? 0.2344 0.1869 0.2562 -0.0034 0.0340  -0.0365 31  MET A C   
324  O O   . MET A 51  ? 0.2836 0.2015 0.2528 0.0108  0.0362  -0.0152 31  MET A O   
325  C CB  . MET A 51  ? 0.2419 0.1722 0.2365 -0.0043 0.0521  -0.0145 31  MET A CB  
326  C CG  . MET A 51  ? 0.2524 0.1922 0.2290 0.0009  0.0566  -0.0007 31  MET A CG  
327  S SD  . MET A 51  ? 0.2399 0.1919 0.2386 0.0033  0.0609  0.0040  31  MET A SD  
328  C CE  . MET A 51  ? 0.2459 0.1822 0.2638 -0.0007 0.0411  0.0020  31  MET A CE  
338  N N   . HIS A 52  ? 0.2491 0.1701 0.2634 -0.0118 0.0342  -0.0328 32  HIS A N   
339  C CA  . HIS A 52  ? 0.2583 0.1673 0.2913 -0.0216 0.0403  -0.0492 32  HIS A CA  
340  C C   . HIS A 52  ? 0.2486 0.1842 0.3171 -0.0040 0.0400  -0.0349 32  HIS A C   
341  O O   . HIS A 52  ? 0.2661 0.2160 0.3662 0.0143  0.0665  -0.0398 32  HIS A O   
342  C CB  . HIS A 52  ? 0.2919 0.1969 0.3248 -0.0078 0.0734  -0.0410 32  HIS A CB  
343  C CG  . HIS A 52  ? 0.2854 0.2429 0.3613 -0.0102 0.0635  -0.0293 32  HIS A CG  
344  N ND1 . HIS A 52  ? 0.3467 0.3121 0.4258 -0.0372 0.1104  -0.0082 32  HIS A ND1 
345  C CD2 . HIS A 52  ? 0.3414 0.2631 0.3922 -0.0296 0.0218  0.0055  32  HIS A CD2 
346  C CE1 . HIS A 52  ? 0.3785 0.3129 0.4397 -0.0833 0.0992  -0.0260 32  HIS A CE1 
347  N NE2 . HIS A 52  ? 0.3941 0.2988 0.4160 -0.1037 0.0850  -0.0337 32  HIS A NE2 
355  N N   . THR A 53  ? 0.2423 0.2029 0.2806 0.0044  0.0613  -0.0139 33  THR A N   
356  C CA  . THR A 53  ? 0.2207 0.2189 0.2821 0.0071  0.0486  0.0114  33  THR A CA  
357  C C   . THR A 53  ? 0.2577 0.2162 0.2876 -0.0005 0.0703  -0.0052 33  THR A C   
358  O O   . THR A 53  ? 0.2462 0.2354 0.3087 0.0100  0.0544  -0.0215 33  THR A O   
359  C CB  . THR A 53  ? 0.2076 0.2514 0.3057 0.0020  0.0335  0.0118  33  THR A CB  
360  O OG1 . THR A 53  ? 0.2329 0.2637 0.2926 0.0099  0.0504  0.0036  33  THR A OG1 
361  C CG2 . THR A 53  ? 0.2207 0.2658 0.3463 -0.0037 0.0130  0.0254  33  THR A CG2 
369  N N   . ARG A 54  ? 0.2402 0.2418 0.2969 0.0095  0.0525  0.0061  34  ARG A N   
370  C CA  . ARG A 54  ? 0.2256 0.2420 0.3307 0.0175  0.0642  0.0154  34  ARG A CA  
371  C C   . ARG A 54  ? 0.2568 0.2574 0.3793 0.0344  0.0946  0.0246  34  ARG A C   
372  O O   . ARG A 54  ? 0.2736 0.2811 0.3616 0.0176  0.1028  0.0029  34  ARG A O   
373  C CB  . ARG A 54  ? 0.2775 0.2092 0.3360 -0.0052 0.0872  0.0166  34  ARG A CB  
374  C CG  . ARG A 54  ? 0.3001 0.1813 0.3136 -0.0028 0.0861  0.0160  34  ARG A CG  
375  C CD  . ARG A 54  ? 0.3036 0.1724 0.2934 -0.0077 0.0744  0.0082  34  ARG A CD  
376  N NE  . ARG A 54  ? 0.3117 0.1889 0.3057 -0.0220 0.0610  0.0113  34  ARG A NE  
377  C CZ  . ARG A 54  ? 0.3224 0.2009 0.3072 -0.0258 0.0759  0.0078  34  ARG A CZ  
378  N NH1 . ARG A 54  ? 0.3763 0.1835 0.3051 -0.0385 0.0639  -0.0111 34  ARG A NH1 
379  N NH2 . ARG A 54  ? 0.2896 0.2368 0.3307 -0.0279 0.0575  -0.0094 34  ARG A NH2 
393  N N   . GLY A 55  ? 0.2513 0.2665 0.3691 0.0476  0.0830  0.0379  35  GLY A N   
394  C CA  . GLY A 55  ? 0.2551 0.3067 0.3953 0.0675  0.1223  0.0352  35  GLY A CA  
395  C C   . GLY A 55  ? 0.2556 0.3156 0.3857 0.0702  0.1065  0.0175  35  GLY A C   
396  O O   . GLY A 55  ? 0.2452 0.2929 0.3994 0.0374  0.0792  -0.0012 35  GLY A O   
400  N N   . GLU A 56  ? 0.2659 0.3513 0.4482 0.0696  0.1481  0.0149  36  GLU A N   
401  C CA  . GLU A 56  ? 0.2683 0.3854 0.4725 0.0711  0.1533  0.0038  36  GLU A CA  
402  C C   . GLU A 56  ? 0.2855 0.3630 0.4271 0.0541  0.1785  -0.0058 36  GLU A C   
403  O O   . GLU A 56  ? 0.2811 0.3776 0.4153 0.0103  0.1449  0.0083  36  GLU A O   
404  C CB  . GLU A 56  ? 0.3628 0.4455 0.5706 0.0910  0.2002  0.0388  36  GLU A CB  
405  C CG  . GLU A 56  ? 0.4358 0.5165 0.6291 0.0961  0.1634  0.0498  36  GLU A CG  
406  C CD  . GLU A 56  ? 0.5061 0.5703 0.6797 0.0770  0.1282  0.0631  36  GLU A CD  
407  O OE1 . GLU A 56  ? 0.5030 0.5906 0.7157 0.0796  0.1127  0.0789  36  GLU A OE1 
408  O OE2 . GLU A 56  ? 0.5685 0.5977 0.6859 0.0741  0.1151  0.0534  36  GLU A OE2 
415  N N   . ALA A 57  ? 0.2862 0.3360 0.3643 0.0439  0.1299  -0.0083 37  ALA A N   
416  C CA  . ALA A 57  ? 0.3119 0.3409 0.3058 0.0108  0.1071  -0.0381 37  ALA A CA  
417  C C   . ALA A 57  ? 0.2741 0.3077 0.2831 0.0045  0.1005  -0.0119 37  ALA A C   
418  O O   . ALA A 57  ? 0.2447 0.3282 0.2762 -0.0137 0.0563  0.0072  37  ALA A O   
419  C CB  . ALA A 57  ? 0.3945 0.3664 0.3189 0.0022  0.1118  -0.0445 37  ALA A CB  
425  N N   . ARG A 58  ? 0.2298 0.2859 0.2720 0.0248  0.0832  -0.0072 38  ARG A N   
426  C CA  . ARG A 58  ? 0.2274 0.2887 0.2709 0.0354  0.0786  -0.0023 38  ARG A CA  
427  C C   . ARG A 58  ? 0.2256 0.3151 0.2694 0.0106  0.0773  0.0069  38  ARG A C   
428  O O   . ARG A 58  ? 0.2166 0.3042 0.2890 0.0052  0.0474  -0.0006 38  ARG A O   
429  C CB  . ARG A 58  ? 0.2450 0.3091 0.2677 0.0115  0.0608  0.0082  38  ARG A CB  
430  C CG  . ARG A 58  ? 0.2539 0.3431 0.2733 -0.0177 0.0503  0.0162  38  ARG A CG  
431  C CD  . ARG A 58  ? 0.3309 0.3588 0.2966 -0.0513 0.0736  0.0148  38  ARG A CD  
432  N NE  . ARG A 58  ? 0.3403 0.3642 0.3109 -0.0732 0.0271  0.0219  38  ARG A NE  
433  C CZ  . ARG A 58  ? 0.3107 0.3471 0.2958 -0.0379 -0.0029 0.0479  38  ARG A CZ  
434  N NH1 . ARG A 58  ? 0.3290 0.3349 0.3508 0.0045  0.0256  0.0352  38  ARG A NH1 
435  N NH2 . ARG A 58  ? 0.3055 0.3870 0.2944 0.0093  0.0127  0.0224  38  ARG A NH2 
449  N N   . LEU A 59  ? 0.2071 0.3363 0.2957 0.0023  0.0580  0.0281  39  LEU A N   
450  C CA  . LEU A 59  ? 0.2050 0.3628 0.3277 0.0223  0.0733  0.0396  39  LEU A CA  
451  C C   . LEU A 59  ? 0.2348 0.3515 0.3225 0.0195  0.0840  0.0376  39  LEU A C   
452  O O   . LEU A 59  ? 0.2335 0.3661 0.3347 -0.0074 0.0702  0.0411  39  LEU A O   
453  C CB  . LEU A 59  ? 0.2321 0.3837 0.3697 0.0350  0.0846  0.0522  39  LEU A CB  
454  C CG  . LEU A 59  ? 0.2767 0.3994 0.4406 0.0441  0.0560  0.0564  39  LEU A CG  
455  C CD1 . LEU A 59  ? 0.2648 0.4036 0.5047 0.0782  0.0933  0.0903  39  LEU A CD1 
456  C CD2 . LEU A 59  ? 0.3106 0.4203 0.4406 0.0125  0.0193  0.0684  39  LEU A CD2 
468  N N   . LYS A 60  ? 0.2368 0.3468 0.2977 0.0196  0.0804  0.0027  40  LYS A N   
469  C CA  . LYS A 60  ? 0.2507 0.3630 0.2695 0.0187  0.0701  -0.0051 40  LYS A CA  
470  C C   . LYS A 60  ? 0.2401 0.3180 0.2756 0.0138  0.0680  0.0084  40  LYS A C   
471  O O   . LYS A 60  ? 0.2827 0.2998 0.2711 0.0234  0.0662  0.0045  40  LYS A O   
472  C CB  . LYS A 60  ? 0.3041 0.4233 0.2931 0.0552  0.0877  -0.0222 40  LYS A CB  
473  C CG  . LYS A 60  ? 0.4341 0.4872 0.3464 0.0788  0.1188  -0.0382 40  LYS A CG  
474  C CD  . LYS A 60  ? 0.5007 0.5199 0.4280 0.0909  0.1179  -0.0638 40  LYS A CD  
481  N N   . ARG A 61  ? 0.2282 0.2943 0.2579 0.0171  0.0690  0.0119  41  ARG A N   
482  C CA  . ARG A 61  ? 0.2299 0.2814 0.2552 0.0103  0.0543  0.0056  41  ARG A CA  
483  C C   . ARG A 61  ? 0.2241 0.2757 0.2492 0.0119  0.0690  0.0097  41  ARG A C   
484  O O   . ARG A 61  ? 0.2324 0.2758 0.2373 0.0026  0.0588  0.0332  41  ARG A O   
485  C CB  . ARG A 61  ? 0.2485 0.2797 0.2690 0.0076  0.0683  0.0253  41  ARG A CB  
486  C CG  . ARG A 61  ? 0.2226 0.2764 0.2766 -0.0030 0.0693  0.0123  41  ARG A CG  
487  C CD  . ARG A 61  ? 0.2644 0.2778 0.2750 -0.0248 0.0852  -0.0007 41  ARG A CD  
488  N NE  . ARG A 61  ? 0.2708 0.3152 0.2730 -0.0264 0.0658  0.0193  41  ARG A NE  
489  C CZ  . ARG A 61  ? 0.2702 0.3525 0.2969 -0.0535 0.0376  0.0240  41  ARG A CZ  
490  N NH1 . ARG A 61  ? 0.3060 0.3667 0.3133 -0.0598 0.0578  0.0556  41  ARG A NH1 
491  N NH2 . ARG A 61  ? 0.3009 0.3704 0.3068 -0.0449 0.0356  0.0336  41  ARG A NH2 
505  N N   . HIS A 62  ? 0.2349 0.2686 0.2372 0.0083  0.0576  0.0251  42  HIS A N   
506  C CA  . HIS A 62  ? 0.2334 0.2583 0.2552 -0.0093 0.0464  0.0292  42  HIS A CA  
507  C C   . HIS A 62  ? 0.2500 0.2720 0.2594 -0.0100 0.0714  0.0345  42  HIS A C   
508  O O   . HIS A 62  ? 0.2297 0.2884 0.2692 -0.0198 0.0570  0.0269  42  HIS A O   
509  C CB  . HIS A 62  ? 0.2475 0.2749 0.2846 -0.0097 0.0342  0.0357  42  HIS A CB  
510  C CG  . HIS A 62  ? 0.2277 0.3178 0.3138 -0.0121 0.0317  0.0278  42  HIS A CG  
511  N ND1 . HIS A 62  ? 0.2199 0.3522 0.3232 -0.0073 0.0670  0.0176  42  HIS A ND1 
512  C CD2 . HIS A 62  ? 0.2756 0.3360 0.3581 -0.0020 0.0567  0.0613  42  HIS A CD2 
513  C CE1 . HIS A 62  ? 0.2079 0.3589 0.3632 -0.0052 0.0549  0.0370  42  HIS A CE1 
514  N NE2 . HIS A 62  ? 0.2507 0.3567 0.3977 0.0108  0.0578  0.0721  42  HIS A NE2 
522  N N   . LEU A 63  ? 0.2378 0.2608 0.2416 0.0054  0.0629  0.0291  43  LEU A N   
523  C CA  . LEU A 63  ? 0.2412 0.2926 0.2470 0.0203  0.0641  0.0176  43  LEU A CA  
524  C C   . LEU A 63  ? 0.2230 0.2831 0.2566 0.0039  0.0462  -0.0041 43  LEU A C   
525  O O   . LEU A 63  ? 0.2420 0.3268 0.2358 0.0033  0.0590  0.0111  43  LEU A O   
526  C CB  . LEU A 63  ? 0.2596 0.3597 0.2623 0.0439  0.0766  0.0203  43  LEU A CB  
527  C CG  . LEU A 63  ? 0.2806 0.4361 0.3166 0.0556  0.1172  0.0241  43  LEU A CG  
528  C CD1 . LEU A 63  ? 0.3344 0.4928 0.3378 0.0961  0.1349  0.0077  43  LEU A CD1 
529  C CD2 . LEU A 63  ? 0.2848 0.4604 0.3474 0.0062  0.1027  0.0590  43  LEU A CD2 
541  N N   . LEU A 64  ? 0.2348 0.2477 0.2355 -0.0090 0.0646  0.0160  44  LEU A N   
542  C CA  . LEU A 64  ? 0.2127 0.2585 0.2244 0.0018  0.0585  0.0061  44  LEU A CA  
543  C C   . LEU A 64  ? 0.2116 0.2625 0.2083 -0.0102 0.0626  0.0112  44  LEU A C   
544  O O   . LEU A 64  ? 0.2104 0.2649 0.2404 0.0052  0.0529  0.0212  44  LEU A O   
545  C CB  . LEU A 64  ? 0.2118 0.2620 0.2385 0.0047  0.0496  0.0079  44  LEU A CB  
546  C CG  . LEU A 64  ? 0.2275 0.2562 0.2608 -0.0032 0.0353  0.0074  44  LEU A CG  
547  C CD1 . LEU A 64  ? 0.2399 0.2678 0.2767 -0.0040 0.0787  0.0328  44  LEU A CD1 
548  C CD2 . LEU A 64  ? 0.2623 0.2672 0.2861 0.0039  0.0275  0.0035  44  LEU A CD2 
560  N N   . PHE A 65  ? 0.2123 0.2500 0.2391 -0.0011 0.0586  0.0138  45  PHE A N   
561  C CA  . PHE A 65  ? 0.2301 0.2373 0.2230 -0.0046 0.0593  0.0216  45  PHE A CA  
562  C C   . PHE A 65  ? 0.2431 0.2675 0.2269 -0.0118 0.0530  0.0184  45  PHE A C   
563  O O   . PHE A 65  ? 0.2617 0.3030 0.2458 -0.0007 0.0899  0.0291  45  PHE A O   
564  C CB  . PHE A 65  ? 0.2401 0.2339 0.2389 -0.0140 0.0649  0.0243  45  PHE A CB  
565  C CG  . PHE A 65  ? 0.2326 0.2361 0.2364 -0.0311 0.0648  0.0174  45  PHE A CG  
566  C CD1 . PHE A 65  ? 0.2731 0.2441 0.2359 -0.0190 0.0912  0.0302  45  PHE A CD1 
567  C CD2 . PHE A 65  ? 0.2315 0.2336 0.2508 -0.0190 0.0783  0.0179  45  PHE A CD2 
568  C CE1 . PHE A 65  ? 0.2559 0.2552 0.2572 0.0101  0.0913  0.0343  45  PHE A CE1 
569  C CE2 . PHE A 65  ? 0.2440 0.2233 0.2598 -0.0125 0.0768  0.0298  45  PHE A CE2 
570  C CZ  . PHE A 65  ? 0.2658 0.2374 0.2449 0.0045  0.0745  0.0348  45  PHE A CZ  
580  N N   . THR A 66  ? 0.2700 0.2552 0.2424 -0.0134 0.0519  0.0347  46  THR A N   
581  C CA  . THR A 66  ? 0.3041 0.2701 0.2457 -0.0249 0.0343  0.0644  46  THR A CA  
582  C C   . THR A 66  ? 0.2978 0.3009 0.2363 -0.0555 0.0553  0.0337  46  THR A C   
583  O O   . THR A 66  ? 0.2900 0.2976 0.2460 -0.0487 0.0674  0.0295  46  THR A O   
584  C CB  . THR A 66  ? 0.3588 0.2701 0.2703 -0.0113 0.0337  0.0551  46  THR A CB  
585  O OG1 . THR A 66  ? 0.3626 0.2803 0.2830 0.0006  0.0485  0.0456  46  THR A OG1 
586  C CG2 . THR A 66  ? 0.3691 0.2773 0.2889 0.0332  0.0244  0.0367  46  THR A CG2 
594  N N   . GLU A 67  ? 0.3285 0.3262 0.2471 -0.0546 0.0784  0.0523  47  GLU A N   
595  C CA  . GLU A 67  ? 0.3531 0.3446 0.2427 -0.0909 0.0679  0.0990  47  GLU A CA  
596  C C   . GLU A 67  ? 0.3388 0.3592 0.2507 -0.0910 0.0507  0.0866  47  GLU A C   
597  O O   . GLU A 67  ? 0.3209 0.3964 0.2692 -0.0794 0.0547  0.0766  47  GLU A O   
609  N N   . ASP A 68  ? 0.3878 0.3331 0.2877 -0.0975 0.0778  0.0685  48  ASP A N   
610  C CA  . ASP A 68  ? 0.4318 0.3170 0.2812 -0.0766 0.0824  0.0561  48  ASP A CA  
611  C C   . ASP A 68  ? 0.3950 0.2944 0.2681 -0.0613 0.0972  0.0524  48  ASP A C   
612  O O   . ASP A 68  ? 0.4046 0.2985 0.2825 -0.0652 0.0916  0.0452  48  ASP A O   
613  C CB  . ASP A 68  ? 0.5122 0.3298 0.3535 -0.0723 0.0839  0.0769  48  ASP A CB  
614  C CG  . ASP A 68  ? 0.5830 0.3696 0.4418 -0.0384 0.0706  0.0858  48  ASP A CG  
615  O OD1 . ASP A 68  ? 0.5950 0.3969 0.4393 -0.0436 0.1145  0.0782  48  ASP A OD1 
616  O OD2 . ASP A 68  ? 0.6452 0.4163 0.5203 -0.0108 0.0403  0.0652  48  ASP A OD2 
621  N N   . GLY A 69  ? 0.3228 0.2658 0.2551 -0.0553 0.0640  0.0466  49  GLY A N   
622  C CA  . GLY A 69  ? 0.3143 0.2668 0.2362 -0.0489 0.0862  0.0367  49  GLY A CA  
623  C C   . GLY A 69  ? 0.2771 0.2676 0.2337 -0.0399 0.0749  0.0265  49  GLY A C   
624  O O   . GLY A 69  ? 0.2663 0.3105 0.2669 -0.0408 0.0679  0.0422  49  GLY A O   
628  N N   . VAL A 70  ? 0.2566 0.2674 0.2181 -0.0503 0.0598  0.0291  50  VAL A N   
629  C CA  . VAL A 70  ? 0.2615 0.2462 0.2271 -0.0523 0.0542  0.0133  50  VAL A CA  
630  C C   . VAL A 70  ? 0.2326 0.2311 0.2440 -0.0401 0.0614  0.0275  50  VAL A C   
631  O O   . VAL A 70  ? 0.2342 0.2482 0.2477 -0.0349 0.0545  0.0478  50  VAL A O   
632  C CB  . VAL A 70  ? 0.3552 0.2245 0.2486 -0.0329 0.0583  -0.0008 50  VAL A CB  
633  C CG1 . VAL A 70  ? 0.4151 0.2563 0.2649 -0.0227 0.0821  -0.0277 50  VAL A CG1 
634  C CG2 . VAL A 70  ? 0.4017 0.2157 0.3140 -0.0512 0.0735  0.0311  50  VAL A CG2 
644  N N   . GLY A 71  ? 0.2187 0.2307 0.2561 -0.0386 0.0590  0.0252  51  GLY A N   
645  C CA  . GLY A 71  ? 0.2231 0.2106 0.2486 -0.0383 0.0579  0.0393  51  GLY A CA  
646  C C   . GLY A 71  ? 0.2040 0.2537 0.2569 -0.0477 0.0467  0.0424  51  GLY A C   
647  O O   . GLY A 71  ? 0.3122 0.3392 0.2748 -0.1310 0.0205  0.0771  51  GLY A O   
651  N N   . GLY A 72  ? 0.2050 0.2436 0.2440 -0.0459 0.0437  0.0371  52  GLY A N   
652  C CA  . GLY A 72  ? 0.2181 0.2203 0.2599 -0.0202 0.0514  0.0241  52  GLY A CA  
653  C C   . GLY A 72  ? 0.2151 0.2122 0.2547 -0.0168 0.0341  0.0446  52  GLY A C   
654  O O   . GLY A 72  ? 0.2289 0.2194 0.2417 -0.0311 0.0500  0.0239  52  GLY A O   
658  N N   . LEU A 73  ? 0.1894 0.2405 0.2383 -0.0361 0.0201  0.0556  53  LEU A N   
659  C CA  . LEU A 73  ? 0.1952 0.2327 0.2507 -0.0413 0.0257  0.0388  53  LEU A CA  
660  C C   . LEU A 73  ? 0.2131 0.2117 0.2373 -0.0501 0.0323  0.0219  53  LEU A C   
661  O O   . LEU A 73  ? 0.2403 0.2267 0.2434 -0.0565 0.0454  0.0108  53  LEU A O   
662  C CB  . LEU A 73  ? 0.2036 0.2413 0.2539 -0.0313 0.0259  0.0320  53  LEU A CB  
663  C CG  . LEU A 73  ? 0.2027 0.2685 0.2503 -0.0288 0.0362  0.0279  53  LEU A CG  
664  C CD1 . LEU A 73  ? 0.1992 0.2632 0.2502 -0.0163 0.0648  0.0289  53  LEU A CD1 
665  C CD2 . LEU A 73  ? 0.2151 0.2864 0.3005 -0.0186 0.0038  0.0414  53  LEU A CD2 
677  N N   . TRP A 74  ? 0.2192 0.1915 0.2454 -0.0356 0.0375  0.0213  54  TRP A N   
678  C CA  . TRP A 74  ? 0.2474 0.2012 0.2545 -0.0354 0.0538  0.0117  54  TRP A CA  
679  C C   . TRP A 74  ? 0.2962 0.1969 0.2662 -0.0085 0.0405  0.0205  54  TRP A C   
680  O O   . TRP A 74  ? 0.4362 0.2032 0.2721 0.0204  0.0674  0.0125  54  TRP A O   
681  C CB  . TRP A 74  ? 0.2233 0.2113 0.2509 -0.0112 0.0315  0.0280  54  TRP A CB  
682  C CG  . TRP A 74  ? 0.2475 0.2028 0.2492 0.0017  0.0264  0.0041  54  TRP A CG  
683  C CD1 . TRP A 74  ? 0.3157 0.2120 0.2654 0.0108  0.0575  -0.0010 54  TRP A CD1 
684  C CD2 . TRP A 74  ? 0.2391 0.1997 0.2677 -0.0127 0.0317  0.0102  54  TRP A CD2 
685  N NE1 . TRP A 74  ? 0.3400 0.2029 0.2898 0.0100  0.0637  0.0215  54  TRP A NE1 
686  C CE2 . TRP A 74  ? 0.3065 0.1997 0.2937 -0.0079 0.0566  0.0224  54  TRP A CE2 
687  C CE3 . TRP A 74  ? 0.2380 0.2497 0.2665 -0.0052 0.0489  0.0408  54  TRP A CE3 
688  C CZ2 . TRP A 74  ? 0.3376 0.2199 0.3215 -0.0240 0.0547  0.0278  54  TRP A CZ2 
689  C CZ3 . TRP A 74  ? 0.2684 0.2549 0.2765 -0.0201 0.0514  0.0360  54  TRP A CZ3 
690  C CH2 . TRP A 74  ? 0.3245 0.2463 0.2929 -0.0344 0.0560  0.0484  54  TRP A CH2 
701  N N   . THR A 75  ? 0.2406 0.1795 0.2361 -0.0256 0.0384  0.0192  55  THR A N   
702  C CA  . THR A 75  ? 0.2298 0.1808 0.2417 -0.0264 0.0287  0.0176  55  THR A CA  
703  C C   . THR A 75  ? 0.2356 0.1927 0.2379 -0.0370 0.0257  0.0032  55  THR A C   
704  O O   . THR A 75  ? 0.2502 0.1974 0.2618 -0.0198 0.0229  0.0001  55  THR A O   
705  C CB  . THR A 75  ? 0.2330 0.1722 0.2275 -0.0054 0.0348  0.0077  55  THR A CB  
706  O OG1 . THR A 75  ? 0.2171 0.1712 0.2312 -0.0161 0.0270  -0.0031 55  THR A OG1 
707  C CG2 . THR A 75  ? 0.2389 0.1911 0.2256 -0.0005 0.0295  0.0119  55  THR A CG2 
715  N N   . THR A 76  ? 0.2418 0.2353 0.2489 -0.0425 0.0362  -0.0098 56  THR A N   
716  C CA  . THR A 76  ? 0.2398 0.2652 0.2469 -0.0663 0.0399  -0.0093 56  THR A CA  
717  C C   . THR A 76  ? 0.2162 0.2737 0.2615 -0.0251 0.0464  -0.0214 56  THR A C   
718  O O   . THR A 76  ? 0.2201 0.2944 0.2654 -0.0230 0.0387  -0.0251 56  THR A O   
719  C CB  . THR A 76  ? 0.3424 0.3208 0.2511 -0.1108 0.0579  -0.0196 56  THR A CB  
720  O OG1 . THR A 76  ? 0.4830 0.3513 0.2929 -0.2009 0.0682  -0.0225 56  THR A OG1 
721  C CG2 . THR A 76  ? 0.3306 0.3570 0.2517 -0.0947 0.0766  0.0171  56  THR A CG2 
729  N N   . ASP A 77  ? 0.2080 0.3067 0.2532 -0.0164 0.0302  -0.0140 57  ASP A N   
730  C CA  . ASP A 77  ? 0.2460 0.3580 0.2702 -0.0257 0.0308  -0.0146 57  ASP A CA  
731  C C   . ASP A 77  ? 0.2940 0.3467 0.2780 -0.0276 0.0240  -0.0405 57  ASP A C   
732  O O   . ASP A 77  ? 0.3639 0.3595 0.2877 -0.0135 0.0372  -0.0513 57  ASP A O   
733  C CB  . ASP A 77  ? 0.2520 0.3936 0.2592 -0.0256 0.0015  0.0163  57  ASP A CB  
734  C CG  . ASP A 77  ? 0.2657 0.4573 0.2890 -0.0679 0.0061  -0.0191 57  ASP A CG  
735  O OD1 . ASP A 77  ? 0.2675 0.4780 0.4053 -0.0711 0.0687  -0.0731 57  ASP A OD1 
736  O OD2 . ASP A 77  ? 0.3206 0.4891 0.3282 -0.0612 0.0195  -0.0163 57  ASP A OD2 
741  N N   . SER A 78  ? 0.2963 0.3277 0.3388 -0.0654 0.0277  -0.0723 58  SER A N   
742  C CA  . SER A 78  ? 0.3778 0.3262 0.3873 -0.0474 0.0448  -0.0716 58  SER A CA  
743  C C   . SER A 78  ? 0.3709 0.3235 0.3494 -0.0152 0.0333  -0.0843 58  SER A C   
744  O O   . SER A 78  ? 0.4608 0.3445 0.4025 -0.0289 0.0356  -0.1023 58  SER A O   
745  C CB  . SER A 78  ? 0.4158 0.3360 0.4001 -0.0927 0.0545  -0.0538 58  SER A CB  
746  O OG  . SER A 78  ? 0.4853 0.3302 0.4065 -0.1135 0.0703  -0.0365 58  SER A OG  
752  N N   . GLY A 79  ? 0.3418 0.3434 0.3005 -0.0290 0.0139  -0.0540 59  GLY A N   
753  C CA  . GLY A 79  ? 0.3647 0.3418 0.2871 -0.0157 0.0452  -0.0404 59  GLY A CA  
754  C C   . GLY A 79  ? 0.4204 0.3627 0.3481 -0.0033 0.0548  -0.0407 59  GLY A C   
755  O O   . GLY A 79  ? 0.4704 0.4004 0.4182 0.0447  0.0730  -0.0253 59  GLY A O   
759  N N   . GLN A 80  ? 0.3893 0.3201 0.3179 -0.0362 0.0349  -0.0393 60  GLN A N   
760  C CA  . GLN A 80  ? 0.4529 0.3219 0.3400 -0.0715 0.0475  -0.0405 60  GLN A CA  
761  C C   . GLN A 80  ? 0.3890 0.2953 0.2885 -0.0526 0.0448  -0.0252 60  GLN A C   
762  O O   . GLN A 80  ? 0.3978 0.3275 0.3126 -0.0594 0.0356  -0.0354 60  GLN A O   
763  C CB  . GLN A 80  ? 0.5412 0.3325 0.3899 -0.0906 0.0392  -0.0658 60  GLN A CB  
764  C CG  . GLN A 80  ? 0.6511 0.3764 0.4474 -0.0658 0.0719  -0.0974 60  GLN A CG  
765  C CD  . GLN A 80  ? 0.7453 0.4131 0.5237 -0.0342 0.0919  -0.1056 60  GLN A CD  
766  O OE1 . GLN A 80  ? 0.8026 0.4547 0.5770 -0.0157 0.1135  -0.0855 60  GLN A OE1 
767  N NE2 . GLN A 80  ? 0.7772 0.4086 0.5398 -0.0294 0.0899  -0.1233 60  GLN A NE2 
776  N N   . PRO A 81  ? 0.3402 0.2835 0.3286 -0.0388 0.0355  -0.0325 61  PRO A N   
777  C CA  . PRO A 81  ? 0.3094 0.2669 0.3058 -0.0516 0.0373  -0.0167 61  PRO A CA  
778  C C   . PRO A 81  ? 0.3017 0.2676 0.3169 -0.0759 0.0562  0.0058  61  PRO A C   
779  O O   . PRO A 81  ? 0.3584 0.2796 0.3344 -0.1015 0.0713  0.0071  61  PRO A O   
780  C CB  . PRO A 81  ? 0.3350 0.2899 0.3507 -0.0456 0.0532  -0.0162 61  PRO A CB  
781  C CG  . PRO A 81  ? 0.3953 0.3372 0.4227 -0.0166 0.0382  -0.0399 61  PRO A CG  
782  C CD  . PRO A 81  ? 0.3712 0.3134 0.4053 -0.0091 0.0145  -0.0483 61  PRO A CD  
790  N N   . ILE A 82  ? 0.2596 0.2777 0.2838 -0.0751 0.0413  0.0195  62  ILE A N   
791  C CA  . ILE A 82  ? 0.2451 0.2976 0.3200 -0.0810 0.0440  0.0456  62  ILE A CA  
792  C C   . ILE A 82  ? 0.2623 0.2927 0.2767 -0.0782 0.0222  0.0027  62  ILE A C   
793  O O   . ILE A 82  ? 0.2701 0.2911 0.3167 -0.0810 0.0521  -0.0027 62  ILE A O   
794  C CB  . ILE A 82  ? 0.2495 0.3668 0.3876 -0.0304 0.0657  0.0891  62  ILE A CB  
795  C CG1 . ILE A 82  ? 0.3066 0.4155 0.3653 -0.0323 0.0614  0.0993  62  ILE A CG1 
796  C CG2 . ILE A 82  ? 0.2496 0.3902 0.4516 -0.0194 0.0971  0.0813  62  ILE A CG2 
797  C CD1 . ILE A 82  ? 0.3448 0.4407 0.4505 -0.0438 0.0534  0.0924  62  ILE A CD1 
809  N N   . ALA A 83  ? 0.3217 0.2745 0.2620 -0.0710 0.0529  0.0035  63  ALA A N   
810  C CA  . ALA A 83  ? 0.3782 0.2898 0.2634 -0.0861 0.0818  -0.0134 63  ALA A CA  
811  C C   . ALA A 83  ? 0.3580 0.3025 0.2942 -0.1147 0.1076  0.0064  63  ALA A C   
812  O O   . ALA A 83  ? 0.3800 0.3435 0.3396 -0.1431 0.0989  -0.0311 63  ALA A O   
813  C CB  . ALA A 83  ? 0.4359 0.3213 0.3123 -0.0416 0.0632  -0.0123 63  ALA A CB  
819  N N   . ILE A 84  ? 0.2912 0.2854 0.2742 -0.0749 0.0690  0.0037  64  ILE A N   
820  C CA  . ILE A 84  ? 0.3006 0.3257 0.2631 -0.0668 0.0272  0.0035  64  ILE A CA  
821  C C   . ILE A 84  ? 0.2703 0.3407 0.2490 -0.0747 0.0618  0.0291  64  ILE A C   
822  O O   . ILE A 84  ? 0.2610 0.3348 0.2770 -0.0731 0.0562  0.0611  64  ILE A O   
823  C CB  . ILE A 84  ? 0.3246 0.3837 0.2958 -0.0150 -0.0016 -0.0139 64  ILE A CB  
824  C CG1 . ILE A 84  ? 0.3668 0.4305 0.3383 0.0208  -0.0140 -0.0320 64  ILE A CG1 
825  C CG2 . ILE A 84  ? 0.3161 0.4204 0.3446 -0.0101 0.0290  -0.0372 64  ILE A CG2 
826  C CD1 . ILE A 84  ? 0.4616 0.4684 0.4043 0.0188  0.0384  -0.0432 64  ILE A CD1 
838  N N   . ARG A 85  ? 0.3220 0.3634 0.2653 -0.1110 0.0764  0.0350  65  ARG A N   
839  C CA  . ARG A 85  ? 0.3489 0.3614 0.2889 -0.1070 0.0665  0.0451  65  ARG A CA  
840  C C   . ARG A 85  ? 0.3223 0.3809 0.2894 -0.1193 0.0383  0.0398  65  ARG A C   
841  O O   . ARG A 85  ? 0.3041 0.4217 0.3286 -0.1170 0.0526  0.0321  65  ARG A O   
842  C CB  . ARG A 85  ? 0.3874 0.3630 0.3275 -0.0984 0.0571  0.0199  65  ARG A CB  
843  C CG  . ARG A 85  ? 0.4718 0.3697 0.3466 -0.0874 0.0735  0.0054  65  ARG A CG  
844  C CD  . ARG A 85  ? 0.5773 0.3887 0.3688 -0.0907 0.0567  -0.0145 65  ARG A CD  
845  N NE  . ARG A 85  ? 0.6642 0.4126 0.3696 -0.0479 0.0715  0.0014  65  ARG A NE  
846  C CZ  . ARG A 85  ? 0.7162 0.4360 0.4100 -0.0161 0.0909  -0.0071 65  ARG A CZ  
847  N NH1 . ARG A 85  ? 0.7322 0.4458 0.4495 -0.0144 0.0891  -0.0469 65  ARG A NH1 
848  N NH2 . ARG A 85  ? 0.7597 0.4551 0.4428 -0.0058 0.1140  -0.0125 65  ARG A NH2 
862  N N   . GLY A 86  ? 0.3313 0.3656 0.2763 -0.1169 0.0462  0.0372  66  GLY A N   
863  C CA  . GLY A 86  ? 0.3641 0.3562 0.2689 -0.1158 0.0334  0.0632  66  GLY A CA  
864  C C   . GLY A 86  ? 0.3682 0.3605 0.2680 -0.1557 0.0170  0.0486  66  GLY A C   
865  O O   . GLY A 86  ? 0.3402 0.3551 0.2589 -0.1122 0.0459  0.0374  66  GLY A O   
869  N N   . ARG A 87  ? 0.5182 0.3615 0.2729 -0.1464 0.0426  0.0355  67  ARG A N   
870  C CA  . ARG A 87  ? 0.5920 0.3592 0.2540 -0.1253 0.1092  0.0274  67  ARG A CA  
871  C C   . ARG A 87  ? 0.6155 0.3576 0.3155 -0.1376 0.1925  0.0030  67  ARG A C   
872  O O   . ARG A 87  ? 0.6981 0.3292 0.3136 -0.1399 0.1960  -0.0032 67  ARG A O   
873  C CB  . ARG A 87  ? 0.5857 0.3879 0.2487 -0.0858 0.0721  0.0638  67  ARG A CB  
874  C CG  . ARG A 87  ? 0.4208 0.4208 0.2774 -0.0938 0.0039  0.0195  67  ARG A CG  
875  C CD  . ARG A 87  ? 0.4323 0.4608 0.3160 -0.0346 0.0227  -0.0368 67  ARG A CD  
876  N NE  . ARG A 87  ? 0.4155 0.4960 0.3193 0.0104  0.0762  0.0300  67  ARG A NE  
877  C CZ  . ARG A 87  ? 0.4142 0.5616 0.2710 0.0308  0.0733  0.0244  67  ARG A CZ  
878  N NH1 . ARG A 87  ? 0.4491 0.6120 0.3236 -0.0293 0.0570  0.0642  67  ARG A NH1 
879  N NH2 . ARG A 87  ? 0.3527 0.5740 0.2757 0.1067  0.0374  -0.0128 67  ARG A NH2 
893  N N   . GLU A 88  ? 0.5803 0.3989 0.4003 -0.1420 0.2369  0.0044  68  GLU A N   
894  C CA  . GLU A 88  ? 0.5342 0.4251 0.5232 -0.1583 0.2454  0.0158  68  GLU A CA  
895  C C   . GLU A 88  ? 0.4177 0.3970 0.5509 -0.1354 0.2060  -0.0082 68  GLU A C   
896  O O   . GLU A 88  ? 0.4077 0.4119 0.5988 -0.1075 0.2518  -0.0087 68  GLU A O   
897  C CB  . GLU A 88  ? 0.5809 0.4839 0.6924 -0.1761 0.2457  0.0248  68  GLU A CB  
898  C CG  . GLU A 88  ? 0.6450 0.5252 0.8041 -0.2234 0.2205  0.0393  68  GLU A CG  
903  N N   . LYS A 89  ? 0.3364 0.3691 0.5052 -0.0916 0.1508  -0.0187 69  LYS A N   
904  C CA  . LYS A 89  ? 0.3039 0.3687 0.5172 -0.0584 0.0801  -0.0316 69  LYS A CA  
905  C C   . LYS A 89  ? 0.2912 0.3419 0.4179 -0.0519 0.0450  -0.0160 69  LYS A C   
906  O O   . LYS A 89  ? 0.2784 0.3513 0.4313 -0.0551 0.0394  -0.0365 69  LYS A O   
907  C CB  . LYS A 89  ? 0.3401 0.3745 0.5520 -0.0711 0.0786  -0.0427 69  LYS A CB  
908  C CG  . LYS A 89  ? 0.3635 0.3983 0.5706 -0.0954 0.0739  -0.0092 69  LYS A CG  
913  N N   . LEU A 90  ? 0.2778 0.3218 0.3304 -0.0575 0.0628  -0.0111 70  LEU A N   
914  C CA  . LEU A 90  ? 0.2685 0.3154 0.2858 -0.0627 0.0525  0.0135  70  LEU A CA  
915  C C   . LEU A 90  ? 0.2596 0.3365 0.2928 -0.0676 0.0522  0.0064  70  LEU A C   
916  O O   . LEU A 90  ? 0.2586 0.3603 0.3007 -0.0491 0.0509  0.0152  70  LEU A O   
917  C CB  . LEU A 90  ? 0.2575 0.3131 0.2571 -0.0445 0.0446  0.0147  70  LEU A CB  
918  C CG  . LEU A 90  ? 0.2686 0.3107 0.2784 -0.0319 0.0433  0.0366  70  LEU A CG  
919  C CD1 . LEU A 90  ? 0.3107 0.3240 0.3208 -0.0289 0.0404  0.0506  70  LEU A CD1 
920  C CD2 . LEU A 90  ? 0.2726 0.2920 0.3151 -0.0375 0.0770  0.0297  70  LEU A CD2 
932  N N   . GLY A 91  ? 0.2777 0.3481 0.3159 -0.0580 0.0893  0.0164  71  GLY A N   
933  C CA  . GLY A 91  ? 0.2779 0.3844 0.3645 -0.0437 0.1137  -0.0052 71  GLY A CA  
934  C C   . GLY A 91  ? 0.2420 0.4090 0.4149 -0.0273 0.0946  -0.0327 71  GLY A C   
935  O O   . GLY A 91  ? 0.2442 0.4199 0.4540 -0.0137 0.0865  -0.0449 71  GLY A O   
939  N N   . GLU A 92  ? 0.2403 0.4369 0.5083 -0.0597 0.1109  -0.0516 72  GLU A N   
940  C CA  . GLU A 92  ? 0.2582 0.4712 0.5720 -0.0917 0.1092  -0.0812 72  GLU A CA  
941  C C   . GLU A 92  ? 0.2607 0.4852 0.5200 -0.0342 0.0669  -0.0752 72  GLU A C   
942  O O   . GLU A 92  ? 0.2442 0.5055 0.5335 -0.0133 0.0295  -0.0828 72  GLU A O   
943  C CB  . GLU A 92  ? 0.2969 0.5218 0.6607 -0.1263 0.1234  -0.0849 72  GLU A CB  
944  C CG  . GLU A 92  ? 0.3911 0.5475 0.7244 -0.1681 0.1565  -0.0943 72  GLU A CG  
945  C CD  . GLU A 92  ? 0.4831 0.5903 0.7930 -0.1867 0.1716  -0.0889 72  GLU A CD  
946  O OE1 . GLU A 92  ? 0.5192 0.6086 0.8041 -0.1953 0.1705  -0.1071 72  GLU A OE1 
947  O OE2 . GLU A 92  ? 0.5582 0.6069 0.8213 -0.1656 0.1995  -0.0454 72  GLU A OE2 
954  N N   . HIS A 93  ? 0.2364 0.4747 0.4649 0.0148  0.0308  -0.0570 73  HIS A N   
955  C CA  . HIS A 93  ? 0.2806 0.4842 0.4040 0.0352  0.0581  -0.0245 73  HIS A CA  
956  C C   . HIS A 93  ? 0.2743 0.4466 0.3573 0.0518  0.0292  0.0059  73  HIS A C   
957  O O   . HIS A 93  ? 0.2991 0.4298 0.3414 0.0846  0.0281  0.0284  73  HIS A O   
958  C CB  . HIS A 93  ? 0.3011 0.4996 0.4054 0.0507  0.0864  0.0203  73  HIS A CB  
959  C CG  . HIS A 93  ? 0.3074 0.5313 0.3475 0.0564  0.0700  0.0433  73  HIS A CG  
960  N ND1 . HIS A 93  ? 0.3115 0.5519 0.3887 0.0571  0.1096  0.0642  73  HIS A ND1 
961  C CD2 . HIS A 93  ? 0.3091 0.5569 0.3442 0.0227  0.0582  0.0295  73  HIS A CD2 
962  C CE1 . HIS A 93  ? 0.2861 0.5652 0.3673 0.0559  0.0728  0.0701  73  HIS A CE1 
963  N NE2 . HIS A 93  ? 0.3206 0.5648 0.3970 0.0409  0.0477  0.0392  73  HIS A NE2 
971  N N   . ALA A 94  ? 0.2638 0.4285 0.3170 0.0117  0.0275  -0.0077 74  ALA A N   
972  C CA  . ALA A 94  ? 0.2444 0.4506 0.3007 -0.0062 0.0431  0.0114  74  ALA A CA  
973  C C   . ALA A 94  ? 0.2211 0.4381 0.3027 -0.0158 0.0396  0.0111  74  ALA A C   
974  O O   . ALA A 94  ? 0.2560 0.4022 0.3023 -0.0092 0.0497  0.0317  74  ALA A O   
975  C CB  . ALA A 94  ? 0.2900 0.4787 0.3024 -0.0348 0.0376  0.0345  74  ALA A CB  
981  N N   . VAL A 95  ? 0.2174 0.4500 0.3351 0.0052  0.0649  0.0184  75  VAL A N   
982  C CA  . VAL A 95  ? 0.2184 0.4594 0.4173 -0.0201 0.0909  0.0265  75  VAL A CA  
983  C C   . VAL A 95  ? 0.2508 0.4327 0.4135 -0.0332 0.0154  0.0221  75  VAL A C   
984  O O   . VAL A 95  ? 0.2719 0.4169 0.4243 -0.0059 0.0138  0.0214  75  VAL A O   
985  C CB  . VAL A 95  ? 0.2688 0.5049 0.5218 -0.0103 0.1650  0.0601  75  VAL A CB  
986  C CG1 . VAL A 95  ? 0.1907 0.5430 0.5996 -0.0266 0.0928  0.0490  75  VAL A CG1 
987  C CG2 . VAL A 95  ? 0.3345 0.5120 0.5286 0.0150  0.1944  0.0947  75  VAL A CG2 
997  N N   A TRP A 96  ? 0.2179 0.4149 0.3815 -0.0328 -0.0067 0.0236  76  TRP A N   
998  N N   B TRP A 96  ? 0.2713 0.4474 0.4276 -0.0431 0.0131  0.0259  76  TRP A N   
999  C CA  A TRP A 96  ? 0.2567 0.4245 0.3832 -0.0167 -0.0370 0.0485  76  TRP A CA  
1000 C CA  B TRP A 96  ? 0.3336 0.4754 0.4581 -0.0452 0.0016  0.0383  76  TRP A CA  
1001 C C   A TRP A 96  ? 0.2588 0.4572 0.3276 -0.0634 -0.0901 0.0749  76  TRP A C   
1002 C C   B TRP A 96  ? 0.3457 0.4973 0.4091 -0.0695 -0.0284 0.0754  76  TRP A C   
1003 O O   A TRP A 96  ? 0.3426 0.4598 0.3578 -0.0681 -0.1050 0.0804  76  TRP A O   
1004 O O   B TRP A 96  ? 0.4043 0.5058 0.4087 -0.0699 -0.0556 0.0978  76  TRP A O   
1005 C CB  A TRP A 96  ? 0.2638 0.3981 0.4091 0.0025  -0.0327 0.0252  76  TRP A CB  
1006 C CB  B TRP A 96  ? 0.3604 0.4700 0.4968 -0.0337 0.0095  0.0136  76  TRP A CB  
1011 N N   A SER A 97  ? 0.2553 0.4801 0.3047 -0.0637 -0.0332 0.1026  77  SER A N   
1012 N N   B SER A 97  ? 0.3227 0.5013 0.3778 -0.0702 0.0075  0.0840  77  SER A N   
1013 C CA  A SER A 97  ? 0.2811 0.5153 0.3557 -0.0713 0.0181  0.0979  77  SER A CA  
1014 C CA  B SER A 97  ? 0.2904 0.5032 0.3814 -0.0885 0.0462  0.0732  77  SER A CA  
1015 C C   A SER A 97  ? 0.2664 0.5096 0.3512 -0.1036 0.0208  0.0945  77  SER A C   
1016 C C   B SER A 97  ? 0.2729 0.5070 0.3588 -0.1105 0.0224  0.0891  77  SER A C   
1017 O O   A SER A 97  ? 0.3000 0.5067 0.3522 -0.1045 0.0180  0.1343  77  SER A O   
1018 O O   B SER A 97  ? 0.2988 0.5079 0.3560 -0.1102 0.0051  0.1318  77  SER A O   
1019 C CB  A SER A 97  ? 0.3207 0.5538 0.4123 -0.0456 0.0621  0.0866  77  SER A CB  
1020 C CB  B SER A 97  ? 0.2662 0.4897 0.4197 -0.0889 0.1144  0.0320  77  SER A CB  
1021 O OG  A SER A 97  ? 0.3608 0.5817 0.4426 -0.0450 0.0610  0.0783  77  SER A OG  
1022 O OG  B SER A 97  ? 0.2472 0.4556 0.4159 -0.0988 0.1429  -0.0117 77  SER A OG  
1033 N N   . LEU A 98  ? 0.2872 0.5121 0.3427 -0.1197 0.0145  0.0781  78  LEU A N   
1034 C CA  . LEU A 98  ? 0.3382 0.5386 0.3719 -0.1157 0.0124  0.0816  78  LEU A CA  
1035 C C   . LEU A 98  ? 0.3291 0.5348 0.3853 -0.1037 0.0092  0.0864  78  LEU A C   
1036 O O   . LEU A 98  ? 0.3626 0.5386 0.4148 -0.1115 0.0015  0.1026  78  LEU A O   
1037 C CB  . LEU A 98  ? 0.3715 0.5466 0.3901 -0.1055 0.0353  0.1061  78  LEU A CB  
1038 C CG  . LEU A 98  ? 0.3832 0.5620 0.4670 -0.0994 0.0218  0.0761  78  LEU A CG  
1039 C CD1 . LEU A 98  ? 0.4534 0.5849 0.5161 -0.0654 0.0136  0.0811  78  LEU A CD1 
1040 C CD2 . LEU A 98  ? 0.3397 0.5591 0.4864 -0.0823 0.0009  0.0441  78  LEU A CD2 
1053 N N   . GLN A 99  ? 0.2807 0.5213 0.3428 -0.0752 0.0273  0.0760  79  GLN A N   
1054 C CA  . GLN A 99  ? 0.2650 0.5503 0.3740 -0.0656 0.0167  0.0875  79  GLN A CA  
1055 C C   . GLN A 99  ? 0.2595 0.4833 0.3568 -0.0341 -0.0041 0.0901  79  GLN A C   
1056 O O   . GLN A 99  ? 0.3016 0.4672 0.3862 0.0111  -0.0089 0.0844  79  GLN A O   
1057 C CB  . GLN A 99  ? 0.2894 0.6343 0.4111 -0.1060 0.0010  0.0854  79  GLN A CB  
1058 C CG  . GLN A 99  ? 0.3914 0.6950 0.5353 -0.1065 0.0150  0.0772  79  GLN A CG  
1059 C CD  . GLN A 99  ? 0.5071 0.7367 0.6632 -0.1131 0.0772  0.1078  79  GLN A CD  
1060 O OE1 . GLN A 99  ? 0.5483 0.7373 0.7279 -0.1548 0.0671  0.1242  79  GLN A OE1 
1061 N NE2 . GLN A 99  ? 0.5523 0.7569 0.6839 -0.0810 0.1181  0.1112  79  GLN A NE2 
1070 N N   . CYS A 100 ? 0.2668 0.4345 0.3149 -0.0531 0.0021  0.0690  80  CYS A N   
1071 C CA  . CYS A 100 ? 0.3124 0.4085 0.3087 -0.0665 0.0129  0.0702  80  CYS A CA  
1072 C C   . CYS A 100 ? 0.3073 0.3477 0.2834 -0.0314 0.0097  0.0547  80  CYS A C   
1073 O O   . CYS A 100 ? 0.3199 0.3509 0.2896 -0.0386 -0.0131 0.0601  80  CYS A O   
1074 C CB  . CYS A 100 ? 0.4899 0.4387 0.3169 -0.1425 0.0040  0.0829  80  CYS A CB  
1075 S SG  . CYS A 100 ? 0.6646 0.4734 0.3892 -0.2584 -0.0463 0.0799  80  CYS A SG  
1081 N N   . PHE A 101 ? 0.2717 0.2823 0.2751 -0.0170 0.0180  0.0300  81  PHE A N   
1082 C CA  . PHE A 101 ? 0.2502 0.2550 0.2820 -0.0127 0.0380  0.0161  81  PHE A CA  
1083 C C   . PHE A 101 ? 0.2333 0.2414 0.3062 0.0052  0.0475  0.0011  81  PHE A C   
1084 O O   . PHE A 101 ? 0.2579 0.2539 0.2840 0.0203  0.0259  -0.0048 81  PHE A O   
1085 C CB  . PHE A 101 ? 0.2788 0.2710 0.2678 0.0091  0.0325  0.0177  81  PHE A CB  
1086 C CG  . PHE A 101 ? 0.2976 0.2877 0.2906 -0.0220 0.0669  0.0003  81  PHE A CG  
1087 C CD1 . PHE A 101 ? 0.2968 0.3196 0.2690 -0.0025 0.0671  0.0136  81  PHE A CD1 
1088 C CD2 . PHE A 101 ? 0.4258 0.3110 0.3424 -0.0620 0.1653  -0.0397 81  PHE A CD2 
1089 C CE1 . PHE A 101 ? 0.3507 0.3461 0.2821 -0.0135 0.0745  0.0016  81  PHE A CE1 
1090 C CE2 . PHE A 101 ? 0.4828 0.3406 0.3495 -0.0672 0.1696  -0.0682 81  PHE A CE2 
1091 C CZ  . PHE A 101 ? 0.4179 0.3617 0.3301 -0.0109 0.1379  -0.0456 81  PHE A CZ  
1101 N N   . PRO A 102 ? 0.2369 0.2582 0.3311 0.0402  0.0366  0.0091  82  PRO A N   
1102 C CA  . PRO A 102 ? 0.2073 0.2911 0.3308 0.0452  0.0500  -0.0069 82  PRO A CA  
1103 C C   . PRO A 102 ? 0.2356 0.2858 0.3301 0.0365  0.0334  -0.0181 82  PRO A C   
1104 O O   . PRO A 102 ? 0.3081 0.3461 0.3365 0.0055  0.0754  -0.0386 82  PRO A O   
1105 C CB  . PRO A 102 ? 0.2314 0.3304 0.3675 0.0592  0.0427  0.0063  82  PRO A CB  
1106 C CG  . PRO A 102 ? 0.2742 0.3280 0.3826 0.0427  0.0544  0.0067  82  PRO A CG  
1107 C CD  . PRO A 102 ? 0.2556 0.2845 0.3505 0.0303  0.0130  -0.0014 82  PRO A CD  
1115 N N   . ASP A 103 ? 0.2509 0.2314 0.3345 0.0381  0.0443  -0.0316 83  ASP A N   
1116 C CA  . ASP A 103 ? 0.2664 0.2080 0.3272 0.0396  0.0246  -0.0303 83  ASP A CA  
1117 C C   . ASP A 103 ? 0.2481 0.1769 0.3109 0.0332  0.0377  -0.0285 83  ASP A C   
1118 O O   . ASP A 103 ? 0.2773 0.1854 0.3576 0.0208  0.0456  -0.0354 83  ASP A O   
1119 C CB  . ASP A 103 ? 0.2714 0.2103 0.3620 0.0408  0.0386  -0.0168 83  ASP A CB  
1120 C CG  . ASP A 103 ? 0.3229 0.2193 0.3625 0.0535  0.0164  0.0029  83  ASP A CG  
1121 O OD1 . ASP A 103 ? 0.3167 0.2293 0.3532 0.0505  0.0547  -0.0024 83  ASP A OD1 
1122 O OD2 . ASP A 103 ? 0.4060 0.2546 0.3960 0.0519  -0.0078 0.0196  83  ASP A OD2 
1127 N N   . TRP A 104 ? 0.2511 0.1738 0.3014 0.0347  0.0420  -0.0210 84  TRP A N   
1128 C CA  . TRP A 104 ? 0.2372 0.1685 0.2972 0.0306  0.0381  -0.0132 84  TRP A CA  
1129 C C   . TRP A 104 ? 0.2507 0.1762 0.3026 0.0150  0.0556  -0.0195 84  TRP A C   
1130 O O   . TRP A 104 ? 0.2421 0.2231 0.3005 0.0199  0.0387  -0.0256 84  TRP A O   
1131 C CB  . TRP A 104 ? 0.2359 0.1800 0.2691 0.0346  0.0452  -0.0145 84  TRP A CB  
1132 C CG  . TRP A 104 ? 0.2506 0.1921 0.2657 0.0403  0.0163  -0.0185 84  TRP A CG  
1133 C CD1 . TRP A 104 ? 0.2822 0.2038 0.2596 0.0412  0.0345  -0.0089 84  TRP A CD1 
1134 C CD2 . TRP A 104 ? 0.2236 0.2029 0.2641 0.0388  0.0080  -0.0312 84  TRP A CD2 
1135 N NE1 . TRP A 104 ? 0.2509 0.2160 0.2682 0.0604  0.0349  -0.0206 84  TRP A NE1 
1136 C CE2 . TRP A 104 ? 0.2509 0.1991 0.2666 0.0448  0.0251  -0.0219 84  TRP A CE2 
1137 C CE3 . TRP A 104 ? 0.2286 0.2034 0.2916 0.0372  0.0175  -0.0161 84  TRP A CE3 
1138 C CZ2 . TRP A 104 ? 0.2716 0.1970 0.2730 0.0327  0.0401  -0.0242 84  TRP A CZ2 
1139 C CZ3 . TRP A 104 ? 0.2533 0.1996 0.2666 0.0393  0.0359  -0.0106 84  TRP A CZ3 
1140 C CH2 . TRP A 104 ? 0.2777 0.2074 0.2750 0.0200  0.0517  -0.0144 84  TRP A CH2 
1151 N N   . VAL A 105 ? 0.2506 0.1541 0.2667 0.0289  0.0357  -0.0179 85  VAL A N   
1152 C CA  . VAL A 105 ? 0.2606 0.1401 0.2703 0.0495  0.0378  -0.0127 85  VAL A CA  
1153 C C   . VAL A 105 ? 0.2469 0.1484 0.2708 0.0213  0.0390  -0.0107 85  VAL A C   
1154 O O   . VAL A 105 ? 0.2431 0.1809 0.2597 0.0222  0.0255  -0.0051 85  VAL A O   
1155 C CB  . VAL A 105 ? 0.2863 0.1349 0.3154 0.0404  0.0274  -0.0353 85  VAL A CB  
1156 C CG1 . VAL A 105 ? 0.2961 0.1771 0.3087 0.0596  0.0275  -0.0636 85  VAL A CG1 
1157 C CG2 . VAL A 105 ? 0.2684 0.1501 0.3386 0.0206  -0.0017 -0.0204 85  VAL A CG2 
1167 N N   . TRP A 106 ? 0.2227 0.1666 0.2556 0.0182  0.0358  -0.0011 86  TRP A N   
1168 C CA  . TRP A 106 ? 0.2284 0.1479 0.2521 0.0020  0.0452  0.0060  86  TRP A CA  
1169 C C   . TRP A 106 ? 0.2394 0.1467 0.2770 -0.0021 0.0550  -0.0127 86  TRP A C   
1170 O O   . TRP A 106 ? 0.2663 0.1502 0.2955 -0.0002 0.0579  -0.0281 86  TRP A O   
1171 C CB  . TRP A 106 ? 0.2292 0.1460 0.2483 0.0013  0.0506  -0.0027 86  TRP A CB  
1172 C CG  . TRP A 106 ? 0.2220 0.1446 0.2552 0.0039  0.0445  -0.0024 86  TRP A CG  
1173 C CD1 . TRP A 106 ? 0.2339 0.1607 0.2588 -0.0078 0.0617  -0.0039 86  TRP A CD1 
1174 C CD2 . TRP A 106 ? 0.2044 0.1567 0.2624 0.0118  0.0445  -0.0119 86  TRP A CD2 
1175 N NE1 . TRP A 106 ? 0.2340 0.1669 0.2526 -0.0034 0.0663  0.0110  86  TRP A NE1 
1176 C CE2 . TRP A 106 ? 0.2102 0.1581 0.2604 0.0039  0.0500  -0.0008 86  TRP A CE2 
1177 C CE3 . TRP A 106 ? 0.2300 0.1525 0.2753 0.0189  0.0558  -0.0122 86  TRP A CE3 
1178 C CZ2 . TRP A 106 ? 0.2362 0.1495 0.2903 -0.0050 0.0335  0.0121  86  TRP A CZ2 
1179 C CZ3 . TRP A 106 ? 0.2463 0.1584 0.2621 0.0421  0.0526  -0.0056 86  TRP A CZ3 
1180 C CH2 . TRP A 106 ? 0.2501 0.1651 0.2649 0.0194  0.0354  -0.0043 86  TRP A CH2 
1191 N N   . THR A 107 ? 0.2519 0.1372 0.2666 -0.0017 0.0477  0.0038  87  THR A N   
1192 C CA  . THR A 107 ? 0.2872 0.1201 0.2883 -0.0196 0.0593  0.0113  87  THR A CA  
1193 C C   . THR A 107 ? 0.2577 0.1294 0.2852 -0.0125 0.0391  0.0014  87  THR A C   
1194 O O   . THR A 107 ? 0.2446 0.1312 0.2775 -0.0103 0.0278  -0.0125 87  THR A O   
1195 C CB  . THR A 107 ? 0.2883 0.1560 0.3400 -0.0047 0.0848  0.0120  87  THR A CB  
1196 O OG1 . THR A 107 ? 0.3004 0.2105 0.3158 0.0005  0.0429  0.0187  87  THR A OG1 
1197 C CG2 . THR A 107 ? 0.2895 0.1756 0.4116 0.0126  0.1079  0.0624  87  THR A CG2 
1205 N N   . ASP A 108 ? 0.2651 0.1414 0.2965 -0.0196 0.0647  -0.0157 88  ASP A N   
1206 C CA  . ASP A 108 ? 0.2468 0.1579 0.3228 -0.0242 0.0773  -0.0245 88  ASP A CA  
1207 C C   . ASP A 108 ? 0.2488 0.1433 0.3238 -0.0226 0.0283  -0.0259 88  ASP A C   
1208 O O   . ASP A 108 ? 0.2485 0.1574 0.3029 -0.0028 0.0290  -0.0090 88  ASP A O   
1209 C CB  . ASP A 108 ? 0.2600 0.2053 0.3344 -0.0352 0.0758  0.0239  88  ASP A CB  
1210 C CG  . ASP A 108 ? 0.3363 0.2279 0.3731 -0.0687 0.0469  0.0204  88  ASP A CG  
1211 O OD1 . ASP A 108 ? 0.4063 0.2952 0.4763 -0.0971 0.0064  0.0723  88  ASP A OD1 
1212 O OD2 . ASP A 108 ? 0.2980 0.2436 0.3386 -0.0597 0.0527  0.0108  88  ASP A OD2 
1217 N N   . ILE A 109 ? 0.2528 0.1298 0.3005 -0.0189 0.0405  -0.0280 89  ILE A N   
1218 C CA  . ILE A 109 ? 0.2168 0.1513 0.2919 -0.0136 0.0317  -0.0378 89  ILE A CA  
1219 C C   . ILE A 109 ? 0.2276 0.1868 0.2784 -0.0165 0.0426  -0.0473 89  ILE A C   
1220 O O   . ILE A 109 ? 0.2462 0.2142 0.3365 -0.0193 0.0066  -0.0587 89  ILE A O   
1221 C CB  . ILE A 109 ? 0.2418 0.1680 0.2926 -0.0122 0.0511  -0.0285 89  ILE A CB  
1222 C CG1 . ILE A 109 ? 0.2199 0.2059 0.3206 -0.0093 0.0416  -0.0441 89  ILE A CG1 
1223 C CG2 . ILE A 109 ? 0.2952 0.1728 0.2906 0.0010  0.0505  -0.0173 89  ILE A CG2 
1224 C CD1 . ILE A 109 ? 0.2552 0.2296 0.3381 -0.0042 0.0585  -0.0492 89  ILE A CD1 
1236 N N   . GLN A 110 ? 0.2166 0.1801 0.2491 -0.0119 0.0287  -0.0235 90  GLN A N   
1237 C CA  . GLN A 110 ? 0.2085 0.2014 0.2502 -0.0162 0.0312  -0.0218 90  GLN A CA  
1238 C C   . GLN A 110 ? 0.2037 0.1926 0.2479 -0.0068 0.0370  -0.0151 90  GLN A C   
1239 O O   . GLN A 110 ? 0.2408 0.1908 0.2355 -0.0055 0.0291  -0.0064 90  GLN A O   
1240 C CB  . GLN A 110 ? 0.2572 0.2611 0.3063 -0.0202 0.0484  0.0275  90  GLN A CB  
1241 C CG  . GLN A 110 ? 0.2831 0.3765 0.3728 -0.0422 0.0604  0.0097  90  GLN A CG  
1242 C CD  . GLN A 110 ? 0.3091 0.4811 0.3778 -0.0375 0.0573  -0.0184 90  GLN A CD  
1243 O OE1 . GLN A 110 ? 0.3405 0.5717 0.3689 -0.0205 0.0332  0.0277  90  GLN A OE1 
1244 N NE2 . GLN A 110 ? 0.2695 0.4845 0.4229 -0.0446 0.0746  -0.0770 90  GLN A NE2 
1253 N N   . ILE A 111 ? 0.2226 0.2006 0.2298 -0.0141 0.0354  -0.0166 91  ILE A N   
1254 C CA  . ILE A 111 ? 0.2193 0.2083 0.2229 -0.0073 0.0237  -0.0095 91  ILE A CA  
1255 C C   . ILE A 111 ? 0.2026 0.2222 0.2559 -0.0203 0.0150  -0.0280 91  ILE A C   
1256 O O   . ILE A 111 ? 0.2383 0.2459 0.3059 -0.0139 -0.0143 -0.0184 91  ILE A O   
1257 C CB  . ILE A 111 ? 0.2780 0.2292 0.2487 -0.0088 0.0681  -0.0091 91  ILE A CB  
1258 C CG1 . ILE A 111 ? 0.3057 0.2473 0.3072 0.0340  0.1126  -0.0084 91  ILE A CG1 
1259 C CG2 . ILE A 111 ? 0.3243 0.2469 0.2528 -0.0204 0.0675  0.0099  91  ILE A CG2 
1260 C CD1 . ILE A 111 ? 0.3604 0.2466 0.3641 0.0311  0.1157  -0.0188 91  ILE A CD1 
1272 N N   . PHE A 112 ? 0.1981 0.2119 0.2330 -0.0106 0.0355  -0.0231 92  PHE A N   
1273 C CA  . PHE A 112 ? 0.2054 0.2120 0.2411 0.0018  0.0290  -0.0007 92  PHE A CA  
1274 C C   . PHE A 112 ? 0.1927 0.2281 0.2561 -0.0088 0.0475  -0.0091 92  PHE A C   
1275 O O   . PHE A 112 ? 0.2042 0.2452 0.2409 -0.0052 0.0319  0.0120  92  PHE A O   
1276 C CB  . PHE A 112 ? 0.2053 0.2146 0.2504 0.0123  0.0333  0.0020  92  PHE A CB  
1277 C CG  . PHE A 112 ? 0.2271 0.2229 0.2529 0.0180  0.0425  0.0058  92  PHE A CG  
1278 C CD1 . PHE A 112 ? 0.2454 0.2426 0.2593 0.0057  0.0486  0.0079  92  PHE A CD1 
1279 C CD2 . PHE A 112 ? 0.2598 0.2214 0.2622 0.0247  0.0513  0.0027  92  PHE A CD2 
1280 C CE1 . PHE A 112 ? 0.2974 0.2494 0.2733 -0.0029 0.0684  0.0003  92  PHE A CE1 
1281 C CE2 . PHE A 112 ? 0.2968 0.2366 0.2565 0.0438  0.0649  0.0112  92  PHE A CE2 
1282 C CZ  . PHE A 112 ? 0.3540 0.2397 0.2512 0.0279  0.0873  0.0060  92  PHE A CZ  
1292 N N   . GLU A 113 ? 0.2023 0.2581 0.2269 -0.0068 0.0163  -0.0144 93  GLU A N   
1293 C CA  . GLU A 113 ? 0.2477 0.2943 0.2196 0.0207  0.0367  -0.0134 93  GLU A CA  
1294 C C   . GLU A 113 ? 0.2082 0.2934 0.2453 0.0230  0.0444  0.0042  93  GLU A C   
1295 O O   . GLU A 113 ? 0.2247 0.3072 0.2615 0.0191  0.0664  0.0107  93  GLU A O   
1296 C CB  . GLU A 113 ? 0.3391 0.3602 0.2312 0.0295  0.0111  -0.0327 93  GLU A CB  
1297 C CG  . GLU A 113 ? 0.3823 0.4544 0.2966 0.0098  0.0088  -0.0698 93  GLU A CG  
1298 C CD  . GLU A 113 ? 0.5158 0.5165 0.3596 -0.0219 0.0052  -0.1074 93  GLU A CD  
1299 O OE1 . GLU A 113 ? 0.5521 0.5386 0.3779 -0.1179 -0.0508 -0.0781 93  GLU A OE1 
1300 O OE2 . GLU A 113 ? 0.5996 0.5605 0.4742 0.0024  0.0483  -0.0941 93  GLU A OE2 
1307 N N   . THR A 114 ? 0.2134 0.2930 0.2343 0.0348  0.0309  0.0211  94  THR A N   
1308 C CA  . THR A 114 ? 0.2262 0.3091 0.2195 0.0580  0.0324  0.0168  94  THR A CA  
1309 C C   . THR A 114 ? 0.2262 0.3305 0.2294 0.0388  0.0298  0.0399  94  THR A C   
1310 O O   . THR A 114 ? 0.2324 0.3565 0.2218 0.0413  0.0156  0.0134  94  THR A O   
1311 C CB  . THR A 114 ? 0.2502 0.3057 0.2178 0.0400  0.0451  0.0234  94  THR A CB  
1312 O OG1 . THR A 114 ? 0.2351 0.2984 0.2205 0.0516  0.0317  0.0225  94  THR A OG1 
1313 C CG2 . THR A 114 ? 0.2084 0.3135 0.2246 0.0450  0.0223  0.0422  94  THR A CG2 
1321 N N   . GLN A 115 ? 0.2154 0.3366 0.2394 0.0517  0.0292  0.0513  95  GLN A N   
1322 C CA  . GLN A 115 ? 0.2424 0.3621 0.2504 0.0705  0.0138  0.0554  95  GLN A CA  
1323 C C   . GLN A 115 ? 0.2510 0.3610 0.2497 0.0522  0.0214  0.0635  95  GLN A C   
1324 O O   . GLN A 115 ? 0.2644 0.3848 0.2596 0.0532  0.0194  0.0597  95  GLN A O   
1325 C CB  . GLN A 115 ? 0.2591 0.3700 0.2425 0.1073  0.0406  0.0484  95  GLN A CB  
1326 C CG  . GLN A 115 ? 0.2951 0.3431 0.2384 0.1040  0.0362  0.0692  95  GLN A CG  
1327 C CD  . GLN A 115 ? 0.3293 0.3234 0.2471 0.1105  0.0724  0.0588  95  GLN A CD  
1328 O OE1 . GLN A 115 ? 0.2566 0.2908 0.2389 0.0546  0.0405  0.0319  95  GLN A OE1 
1329 N NE2 . GLN A 115 ? 0.3695 0.3798 0.2658 0.0881  0.0579  0.0351  95  GLN A NE2 
1338 N N   . ASP A 116 ? 0.2560 0.3455 0.2261 0.0533  0.0350  0.0480  96  ASP A N   
1339 C CA  . ASP A 116 ? 0.2399 0.3175 0.2556 0.0479  0.0371  0.0391  96  ASP A CA  
1340 C C   . ASP A 116 ? 0.2181 0.3260 0.2445 0.0416  0.0304  0.0524  96  ASP A C   
1341 O O   . ASP A 116 ? 0.2231 0.3277 0.2252 0.0447  0.0455  0.0426  96  ASP A O   
1342 C CB  . ASP A 116 ? 0.2659 0.3132 0.2884 0.0348  0.0400  0.0359  96  ASP A CB  
1343 C CG  . ASP A 116 ? 0.2946 0.3156 0.2956 0.0481  0.0450  0.0384  96  ASP A CG  
1344 O OD1 . ASP A 116 ? 0.3121 0.3041 0.3089 0.0392  0.0548  0.0503  96  ASP A OD1 
1345 O OD2 . ASP A 116 ? 0.3374 0.3138 0.3082 0.0253  0.0507  0.0385  96  ASP A OD2 
1350 N N   . PRO A 117 ? 0.2445 0.3426 0.2323 0.0606  0.0341  0.0609  97  PRO A N   
1351 C CA  . PRO A 117 ? 0.2655 0.3352 0.2306 0.0513  0.0418  0.0460  97  PRO A CA  
1352 C C   . PRO A 117 ? 0.2613 0.3191 0.2283 0.0447  0.0699  0.0439  97  PRO A C   
1353 O O   . PRO A 117 ? 0.2700 0.3225 0.2381 0.0427  0.0581  0.0185  97  PRO A O   
1354 C CB  . PRO A 117 ? 0.3266 0.3462 0.2344 0.0421  0.0447  0.0332  97  PRO A CB  
1355 C CG  . PRO A 117 ? 0.3427 0.3702 0.2558 0.0591  0.0308  0.0454  97  PRO A CG  
1356 C CD  . PRO A 117 ? 0.2703 0.3696 0.2496 0.0691  0.0141  0.0486  97  PRO A CD  
1364 N N   . ASN A 118 ? 0.2601 0.2956 0.2226 0.0135  0.0367  0.0557  98  ASN A N   
1365 C CA  . ASN A 118 ? 0.2404 0.2905 0.2390 0.0184  0.0401  0.0737  98  ASN A CA  
1366 C C   . ASN A 118 ? 0.2354 0.2874 0.2402 0.0256  0.0527  0.0672  98  ASN A C   
1367 O O   . ASN A 118 ? 0.2389 0.3517 0.2457 0.0060  0.0488  0.0826  98  ASN A O   
1368 C CB  . ASN A 118 ? 0.2686 0.3046 0.2660 0.0319  0.0771  0.0899  98  ASN A CB  
1369 C CG  . ASN A 118 ? 0.3509 0.3260 0.2846 0.0456  0.0852  0.1029  98  ASN A CG  
1370 O OD1 . ASN A 118 ? 0.3932 0.3535 0.2606 0.0552  0.0603  0.0674  98  ASN A OD1 
1371 N ND2 . ASN A 118 ? 0.3963 0.3752 0.3206 0.0335  0.0553  0.1146  98  ASN A ND2 
1378 N N   . TRP A 119 ? 0.2397 0.2328 0.2287 0.0268  0.0391  0.0375  99  TRP A N   
1379 C CA  . TRP A 119 ? 0.2100 0.2262 0.2295 0.0360  0.0313  0.0482  99  TRP A CA  
1380 C C   . TRP A 119 ? 0.2213 0.2292 0.2165 0.0203  0.0374  0.0457  99  TRP A C   
1381 O O   . TRP A 119 ? 0.2032 0.2546 0.2445 0.0184  0.0331  0.0475  99  TRP A O   
1382 C CB  . TRP A 119 ? 0.2221 0.2371 0.2384 0.0350  0.0365  0.0354  99  TRP A CB  
1383 C CG  . TRP A 119 ? 0.2260 0.2279 0.2356 0.0352  0.0377  0.0431  99  TRP A CG  
1384 C CD1 . TRP A 119 ? 0.2204 0.2381 0.2277 0.0203  0.0574  0.0267  99  TRP A CD1 
1385 C CD2 . TRP A 119 ? 0.2390 0.1996 0.2568 0.0434  0.0667  0.0339  99  TRP A CD2 
1386 N NE1 . TRP A 119 ? 0.2448 0.2112 0.2263 0.0188  0.0393  0.0409  99  TRP A NE1 
1387 C CE2 . TRP A 119 ? 0.2366 0.1899 0.2506 0.0166  0.0458  0.0459  99  TRP A CE2 
1388 C CE3 . TRP A 119 ? 0.2741 0.2050 0.2832 0.0661  0.0664  0.0375  99  TRP A CE3 
1389 C CZ2 . TRP A 119 ? 0.2937 0.1772 0.2636 0.0108  0.0522  0.0386  99  TRP A CZ2 
1390 C CZ3 . TRP A 119 ? 0.3044 0.2238 0.2993 0.0721  0.0683  0.0403  99  TRP A CZ3 
1391 C CH2 . TRP A 119 ? 0.3050 0.2159 0.2799 0.0380  0.0467  0.0457  99  TRP A CH2 
1402 N N   . PHE A 120 ? 0.2271 0.2066 0.2327 0.0230  0.0490  0.0441  100 PHE A N   
1403 C CA  . PHE A 120 ? 0.2137 0.2112 0.2238 0.0241  0.0347  0.0216  100 PHE A CA  
1404 C C   . PHE A 120 ? 0.1949 0.2101 0.2269 0.0084  0.0313  0.0275  100 PHE A C   
1405 O O   . PHE A 120 ? 0.2076 0.2161 0.2408 -0.0049 0.0398  0.0312  100 PHE A O   
1406 C CB  . PHE A 120 ? 0.2131 0.2469 0.2270 0.0141  0.0488  0.0064  100 PHE A CB  
1407 C CG  . PHE A 120 ? 0.2266 0.2749 0.2207 0.0158  0.0577  0.0103  100 PHE A CG  
1408 C CD1 . PHE A 120 ? 0.3572 0.3143 0.2252 0.0509  0.0949  -0.0175 100 PHE A CD1 
1409 C CD2 . PHE A 120 ? 0.2215 0.3122 0.2624 0.0153  0.0470  -0.0273 100 PHE A CD2 
1410 C CE1 . PHE A 120 ? 0.3866 0.3521 0.2396 0.1017  0.0757  -0.0230 100 PHE A CE1 
1411 C CE2 . PHE A 120 ? 0.2615 0.3745 0.2685 0.0272  0.0382  -0.0548 100 PHE A CE2 
1412 C CZ  . PHE A 120 ? 0.3093 0.3885 0.2485 0.0924  0.0090  -0.0444 100 PHE A CZ  
1422 N N   . TRP A 121 ? 0.2046 0.1973 0.2153 0.0005  0.0411  0.0144  101 TRP A N   
1423 C CA  . TRP A 121 ? 0.2056 0.1762 0.2165 -0.0002 0.0304  0.0112  101 TRP A CA  
1424 C C   . TRP A 121 ? 0.1922 0.1818 0.2299 -0.0232 0.0370  -0.0076 101 TRP A C   
1425 O O   . TRP A 121 ? 0.2226 0.1884 0.2604 -0.0106 0.0015  0.0017  101 TRP A O   
1426 C CB  . TRP A 121 ? 0.1913 0.1904 0.2205 0.0100  0.0304  0.0169  101 TRP A CB  
1427 C CG  . TRP A 121 ? 0.2141 0.1862 0.2159 0.0214  0.0419  0.0137  101 TRP A CG  
1428 C CD1 . TRP A 121 ? 0.2434 0.2088 0.2293 0.0161  0.0401  -0.0078 101 TRP A CD1 
1429 C CD2 . TRP A 121 ? 0.2131 0.1756 0.2121 0.0086  0.0517  0.0182  101 TRP A CD2 
1430 N NE1 . TRP A 121 ? 0.2400 0.1897 0.2295 0.0293  0.0401  0.0084  101 TRP A NE1 
1431 C CE2 . TRP A 121 ? 0.2173 0.1848 0.2103 0.0109  0.0490  0.0134  101 TRP A CE2 
1432 C CE3 . TRP A 121 ? 0.2242 0.1711 0.2114 -0.0007 0.0539  0.0225  101 TRP A CE3 
1433 C CZ2 . TRP A 121 ? 0.2347 0.1776 0.2284 0.0212  0.0620  0.0141  101 TRP A CZ2 
1434 C CZ3 . TRP A 121 ? 0.2365 0.1759 0.2054 -0.0136 0.0526  0.0140  101 TRP A CZ3 
1435 C CH2 . TRP A 121 ? 0.2555 0.1752 0.2123 -0.0017 0.0697  0.0100  101 TRP A CH2 
1446 N N   . VAL A 122 ? 0.1934 0.1718 0.2134 -0.0173 0.0252  0.0067  102 VAL A N   
1447 C CA  . VAL A 122 ? 0.1895 0.1627 0.2240 -0.0181 0.0348  0.0182  102 VAL A CA  
1448 C C   . VAL A 122 ? 0.1938 0.1795 0.2124 -0.0077 0.0445  0.0183  102 VAL A C   
1449 O O   . VAL A 122 ? 0.2183 0.2090 0.2282 -0.0368 0.0180  0.0141  102 VAL A O   
1450 C CB  . VAL A 122 ? 0.1901 0.1905 0.2291 -0.0089 0.0461  0.0126  102 VAL A CB  
1451 C CG1 . VAL A 122 ? 0.2226 0.1873 0.2667 -0.0037 0.0669  -0.0005 102 VAL A CG1 
1452 C CG2 . VAL A 122 ? 0.2273 0.2482 0.2327 0.0037  0.0670  0.0182  102 VAL A CG2 
1462 N N   . GLU A 123 ? 0.1968 0.1584 0.2077 -0.0037 0.0384  0.0064  103 GLU A N   
1463 C CA  . GLU A 123 ? 0.2092 0.1425 0.2210 -0.0071 0.0397  -0.0029 103 GLU A CA  
1464 C C   . GLU A 123 ? 0.2229 0.1386 0.2131 -0.0088 0.0383  -0.0183 103 GLU A C   
1465 O O   . GLU A 123 ? 0.2304 0.1485 0.2337 -0.0039 0.0346  -0.0161 103 GLU A O   
1466 C CB  . GLU A 123 ? 0.2036 0.1625 0.2260 -0.0176 0.0532  -0.0024 103 GLU A CB  
1467 C CG  . GLU A 123 ? 0.2139 0.1889 0.2239 -0.0255 0.0551  0.0064  103 GLU A CG  
1468 C CD  . GLU A 123 ? 0.2213 0.2161 0.2378 -0.0290 0.0594  -0.0010 103 GLU A CD  
1469 O OE1 . GLU A 123 ? 0.2175 0.2307 0.2386 -0.0131 0.0426  0.0070  103 GLU A OE1 
1470 O OE2 . GLU A 123 ? 0.2242 0.2925 0.2454 -0.0109 0.0668  0.0213  103 GLU A OE2 
1477 N N   . CYS A 124 ? 0.2181 0.1360 0.2161 -0.0056 0.0449  -0.0175 104 CYS A N   
1478 C CA  . CYS A 124 ? 0.2073 0.1389 0.2252 0.0036  0.0293  -0.0257 104 CYS A CA  
1479 C C   . CYS A 124 ? 0.2154 0.1336 0.2466 -0.0045 0.0473  -0.0126 104 CYS A C   
1480 O O   . CYS A 124 ? 0.2310 0.1521 0.2497 -0.0022 0.0352  -0.0014 104 CYS A O   
1481 C CB  . CYS A 124 ? 0.2300 0.1684 0.2418 -0.0029 0.0507  -0.0163 104 CYS A CB  
1482 S SG  . CYS A 124 ? 0.2269 0.2011 0.2574 -0.0141 0.0606  0.0038  104 CYS A SG  
1488 N N   . ARG A 125 ? 0.2206 0.1411 0.2510 -0.0016 0.0318  -0.0223 105 ARG A N   
1489 C CA  . ARG A 125 ? 0.2253 0.1466 0.2560 -0.0015 0.0227  -0.0072 105 ARG A CA  
1490 C C   . ARG A 125 ? 0.2244 0.1478 0.2606 0.0047  0.0362  -0.0015 105 ARG A C   
1491 O O   . ARG A 125 ? 0.2379 0.1872 0.2496 -0.0023 0.0310  -0.0149 105 ARG A O   
1492 C CB  . ARG A 125 ? 0.2507 0.1595 0.2617 0.0032  0.0423  0.0135  105 ARG A CB  
1493 C CG  . ARG A 125 ? 0.2845 0.1817 0.2924 -0.0099 0.0467  0.0203  105 ARG A CG  
1494 C CD  . ARG A 125 ? 0.3562 0.1686 0.3399 -0.0141 0.0909  0.0205  105 ARG A CD  
1495 N NE  . ARG A 125 ? 0.4210 0.2045 0.3908 -0.0094 0.0947  0.0226  105 ARG A NE  
1496 C CZ  . ARG A 125 ? 0.4356 0.2345 0.3990 -0.0078 0.1004  0.0156  105 ARG A CZ  
1497 N NH1 . ARG A 125 ? 0.4638 0.2632 0.3978 -0.0070 0.1136  0.0162  105 ARG A NH1 
1498 N NH2 . ARG A 125 ? 0.4570 0.2331 0.3598 0.0024  0.0988  0.0252  105 ARG A NH2 
1512 N N   . GLY A 126 ? 0.2263 0.1791 0.2441 0.0303  0.0286  -0.0147 106 GLY A N   
1513 C CA  . GLY A 126 ? 0.2395 0.2192 0.2509 0.0429  0.0263  -0.0232 106 GLY A CA  
1514 C C   . GLY A 126 ? 0.2273 0.2200 0.2562 0.0375  0.0325  -0.0179 106 GLY A C   
1515 O O   . GLY A 126 ? 0.2405 0.2447 0.2469 0.0516  0.0259  -0.0143 106 GLY A O   
1519 N N   . GLU A 127 ? 0.2280 0.2122 0.2632 0.0392  0.0208  -0.0039 107 GLU A N   
1520 C CA  . GLU A 127 ? 0.2277 0.2258 0.2952 0.0382  0.0258  0.0047  107 GLU A CA  
1521 C C   . GLU A 127 ? 0.2468 0.1888 0.2942 0.0335  0.0364  0.0054  107 GLU A C   
1522 O O   . GLU A 127 ? 0.2294 0.2132 0.2785 0.0200  0.0340  -0.0096 107 GLU A O   
1523 C CB  . GLU A 127 ? 0.2681 0.2621 0.2956 0.0184  0.0384  0.0015  107 GLU A CB  
1524 C CG  . GLU A 127 ? 0.3043 0.2530 0.3688 0.0070  0.0248  0.0176  107 GLU A CG  
1525 C CD  . GLU A 127 ? 0.3693 0.2911 0.4262 0.0020  -0.0185 0.0267  107 GLU A CD  
1526 O OE1 . GLU A 127 ? 0.4312 0.3125 0.4973 0.0217  -0.0252 0.0406  107 GLU A OE1 
1527 O OE2 . GLU A 127 ? 0.3939 0.3254 0.4741 -0.0330 0.0010  0.0398  107 GLU A OE2 
1534 N N   . GLY A 128 ? 0.2259 0.1838 0.2871 0.0260  0.0262  0.0025  108 GLY A N   
1535 C CA  . GLY A 128 ? 0.2236 0.2011 0.2913 0.0302  0.0242  -0.0044 108 GLY A CA  
1536 C C   . GLY A 128 ? 0.2286 0.2116 0.3121 0.0206  0.0489  0.0089  108 GLY A C   
1537 O O   . GLY A 128 ? 0.2399 0.2491 0.2768 0.0221  0.0365  -0.0029 108 GLY A O   
1541 N N   . ALA A 129 ? 0.2324 0.2193 0.3147 0.0416  0.0257  0.0132  109 ALA A N   
1542 C CA  . ALA A 129 ? 0.2296 0.2433 0.3377 0.0350  0.0108  0.0036  109 ALA A CA  
1543 C C   . ALA A 129 ? 0.2550 0.2456 0.2885 0.0018  0.0161  0.0203  109 ALA A C   
1544 O O   . ALA A 129 ? 0.2772 0.2608 0.2891 0.0009  0.0036  0.0429  109 ALA A O   
1545 C CB  . ALA A 129 ? 0.2524 0.2761 0.3854 0.0343  0.0084  0.0183  109 ALA A CB  
1551 N N   . ILE A 130 ? 0.2529 0.2755 0.2826 -0.0154 0.0167  0.0281  110 ILE A N   
1552 C CA  . ILE A 130 ? 0.2413 0.2641 0.2858 -0.0095 0.0125  0.0193  110 ILE A CA  
1553 C C   . ILE A 130 ? 0.2711 0.2780 0.2922 -0.0049 0.0320  0.0500  110 ILE A C   
1554 O O   . ILE A 130 ? 0.2553 0.3056 0.3148 -0.0011 0.0332  0.0579  110 ILE A O   
1555 C CB  . ILE A 130 ? 0.2455 0.2573 0.3125 0.0009  0.0364  0.0324  110 ILE A CB  
1556 C CG1 . ILE A 130 ? 0.2994 0.2594 0.2796 0.0185  0.0334  -0.0099 110 ILE A CG1 
1557 C CG2 . ILE A 130 ? 0.2363 0.2966 0.3097 -0.0160 0.0294  0.0465  110 ILE A CG2 
1558 C CD1 . ILE A 130 ? 0.3050 0.2727 0.2783 -0.0069 0.0336  -0.0035 110 ILE A CD1 
1570 N N   . VAL A 131 ? 0.2490 0.2835 0.2899 0.0022  0.0064  0.0282  111 VAL A N   
1571 C CA  . VAL A 131 ? 0.2520 0.2955 0.3124 0.0251  0.0148  0.0269  111 VAL A CA  
1572 C C   . VAL A 131 ? 0.2407 0.3002 0.2968 0.0044  0.0164  0.0316  111 VAL A C   
1573 O O   . VAL A 131 ? 0.2753 0.3233 0.3016 -0.0176 0.0334  0.0134  111 VAL A O   
1574 C CB  . VAL A 131 ? 0.2661 0.3256 0.3387 0.0262  0.0302  0.0095  111 VAL A CB  
1575 C CG1 . VAL A 131 ? 0.2560 0.3534 0.3753 0.0512  0.0169  0.0100  111 VAL A CG1 
1576 C CG2 . VAL A 131 ? 0.3210 0.3338 0.3475 0.0228  0.0604  -0.0201 111 VAL A CG2 
1586 N N   . PHE A 132 ? 0.2258 0.3073 0.2947 0.0167  0.0181  0.0295  112 PHE A N   
1587 C CA  . PHE A 132 ? 0.2248 0.3152 0.3082 0.0301  0.0504  0.0373  112 PHE A CA  
1588 C C   . PHE A 132 ? 0.2532 0.3297 0.3185 0.0235  0.0667  0.0273  112 PHE A C   
1589 O O   . PHE A 132 ? 0.2628 0.3735 0.3145 -0.0223 0.0039  0.0318  112 PHE A O   
1590 C CB  . PHE A 132 ? 0.2787 0.3325 0.3493 0.0436  0.0720  0.0311  112 PHE A CB  
1591 C CG  . PHE A 132 ? 0.2999 0.3616 0.3272 0.0227  0.0652  0.0370  112 PHE A CG  
1592 C CD1 . PHE A 132 ? 0.3630 0.3831 0.4362 -0.0050 0.0963  0.1024  112 PHE A CD1 
1593 C CD2 . PHE A 132 ? 0.4657 0.4105 0.3321 0.0962  0.0784  0.0325  112 PHE A CD2 
1594 C CE1 . PHE A 132 ? 0.4019 0.4149 0.4561 0.0637  0.0557  0.0972  112 PHE A CE1 
1595 C CE2 . PHE A 132 ? 0.5012 0.4387 0.3790 0.1502  0.0954  0.0141  112 PHE A CE2 
1596 C CZ  . PHE A 132 ? 0.4382 0.4395 0.4335 0.1474  0.0440  0.0576  112 PHE A CZ  
1606 N N   . PRO A 133 ? 0.2665 0.3493 0.3440 -0.0191 0.0536  0.0254  113 PRO A N   
1607 C CA  . PRO A 133 ? 0.2654 0.3569 0.3510 -0.0402 0.0430  0.0198  113 PRO A CA  
1608 C C   . PRO A 133 ? 0.2823 0.3882 0.3277 -0.0400 0.0552  -0.0042 113 PRO A C   
1609 O O   . PRO A 133 ? 0.3439 0.4022 0.3682 -0.0538 0.1180  -0.0148 113 PRO A O   
1610 C CB  . PRO A 133 ? 0.3165 0.3460 0.3930 -0.0494 0.0917  0.0254  113 PRO A CB  
1611 C CG  . PRO A 133 ? 0.3106 0.3530 0.4408 -0.0366 0.0697  0.0663  113 PRO A CG  
1612 C CD  . PRO A 133 ? 0.2747 0.3507 0.4061 -0.0268 0.0737  0.0552  113 PRO A CD  
1620 N N   . GLY A 134 ? 0.3142 0.4263 0.3166 -0.0563 0.0630  -0.0095 114 GLY A N   
1621 C CA  . GLY A 134 ? 0.3384 0.4433 0.3133 -0.0895 0.0494  0.0018  114 GLY A CA  
1622 C C   . GLY A 134 ? 0.3102 0.4537 0.3222 -0.0540 0.0199  0.0401  114 GLY A C   
1623 O O   . GLY A 134 ? 0.3170 0.4967 0.3334 -0.0764 0.0110  0.0224  114 GLY A O   
1627 N N   . TYR A 135 ? 0.2546 0.4114 0.3117 -0.0453 -0.0060 0.0336  115 TYR A N   
1628 C CA  . TYR A 135 ? 0.2425 0.3861 0.3055 -0.0481 0.0054  0.0220  115 TYR A CA  
1629 C C   . TYR A 135 ? 0.2613 0.3833 0.3172 -0.0354 0.0103  0.0356  115 TYR A C   
1630 O O   . TYR A 135 ? 0.2935 0.3815 0.3478 -0.0217 0.0265  0.0406  115 TYR A O   
1631 C CB  . TYR A 135 ? 0.2407 0.3701 0.2966 -0.0579 -0.0127 0.0140  115 TYR A CB  
1632 C CG  . TYR A 135 ? 0.2192 0.3615 0.2995 -0.0382 -0.0021 0.0114  115 TYR A CG  
1633 C CD1 . TYR A 135 ? 0.2283 0.3500 0.2999 -0.0186 -0.0051 0.0154  115 TYR A CD1 
1634 C CD2 . TYR A 135 ? 0.2050 0.3701 0.3136 -0.0150 0.0192  0.0416  115 TYR A CD2 
1635 C CE1 . TYR A 135 ? 0.2510 0.3580 0.2917 -0.0351 0.0214  0.0025  115 TYR A CE1 
1636 C CE2 . TYR A 135 ? 0.2202 0.3801 0.3070 0.0001  0.0228  0.0397  115 TYR A CE2 
1637 C CZ  . TYR A 135 ? 0.2166 0.3799 0.3029 -0.0003 0.0027  0.0290  115 TYR A CZ  
1638 O OH  . TYR A 135 ? 0.2568 0.4169 0.3302 0.0356  0.0389  0.0202  115 TYR A OH  
1648 N N   . PRO A 136 ? 0.2570 0.3746 0.3259 0.0062  0.0186  0.0474  116 PRO A N   
1649 C CA  . PRO A 136 ? 0.2603 0.3627 0.3624 0.0334  0.0171  0.0599  116 PRO A CA  
1650 C C   . PRO A 136 ? 0.2405 0.3492 0.3406 0.0414  0.0023  0.0410  116 PRO A C   
1651 O O   . PRO A 136 ? 0.2342 0.3509 0.3537 0.0461  0.0077  0.0491  116 PRO A O   
1652 C CB  . PRO A 136 ? 0.3103 0.3934 0.3630 0.0138  0.0255  0.0882  116 PRO A CB  
1653 C CG  . PRO A 136 ? 0.3457 0.4165 0.3638 -0.0018 0.0245  0.0811  116 PRO A CG  
1654 C CD  . PRO A 136 ? 0.2975 0.4065 0.3345 -0.0266 0.0226  0.0501  116 PRO A CD  
1662 N N   A ARG A 137 ? 0.2721 0.3509 0.3595 0.0396  0.0094  0.0325  117 ARG A N   
1663 N N   B ARG A 137 ? 0.2314 0.3584 0.3494 0.0274  0.0078  0.0355  117 ARG A N   
1664 C CA  A ARG A 137 ? 0.3203 0.3528 0.3808 0.0466  0.0238  0.0398  117 ARG A CA  
1665 C CA  B ARG A 137 ? 0.2604 0.3666 0.3697 0.0224  0.0395  0.0435  117 ARG A CA  
1666 C C   A ARG A 137 ? 0.3271 0.3556 0.3692 0.0079  0.0061  0.0668  117 ARG A C   
1667 C C   B ARG A 137 ? 0.2996 0.3623 0.3622 -0.0038 0.0124  0.0703  117 ARG A C   
1668 O O   A ARG A 137 ? 0.3630 0.3679 0.3776 0.0134  -0.0055 0.0812  117 ARG A O   
1669 O O   B ARG A 137 ? 0.3407 0.3734 0.3734 0.0045  -0.0109 0.0885  117 ARG A O   
1670 C CB  A ARG A 137 ? 0.4157 0.3737 0.4269 0.0663  0.0398  0.0037  117 ARG A CB  
1671 C CB  B ARG A 137 ? 0.3113 0.3988 0.4100 0.0395  0.0601  0.0048  117 ARG A CB  
1672 C CG  A ARG A 137 ? 0.4637 0.3834 0.4728 0.0942  0.0299  -0.0111 117 ARG A CG  
1673 C CG  B ARG A 137 ? 0.3032 0.4207 0.4441 0.0627  0.0455  -0.0125 117 ARG A CG  
1674 C CD  A ARG A 137 ? 0.4993 0.3933 0.5345 0.1161  0.0332  -0.0219 117 ARG A CD  
1675 C CD  B ARG A 137 ? 0.3791 0.4564 0.5123 0.0764  0.0621  -0.0185 117 ARG A CD  
1676 N NE  A ARG A 137 ? 0.5137 0.4031 0.5692 0.1548  0.0095  -0.0097 117 ARG A NE  
1677 N NE  B ARG A 137 ? 0.4009 0.4848 0.5406 0.0912  0.0712  -0.0198 117 ARG A NE  
1678 C CZ  A ARG A 137 ? 0.5085 0.4132 0.6011 0.1701  0.0022  -0.0174 117 ARG A CZ  
1679 C CZ  B ARG A 137 ? 0.4126 0.5074 0.5512 0.0989  0.0731  -0.0203 117 ARG A CZ  
1680 N NH1 A ARG A 137 ? 0.5333 0.4337 0.6220 0.1662  -0.0100 -0.0170 117 ARG A NH1 
1681 N NH1 B ARG A 137 ? 0.4188 0.5058 0.5483 0.1128  0.0630  -0.0447 117 ARG A NH1 
1682 N NH2 A ARG A 137 ? 0.4805 0.4014 0.6196 0.1850  -0.0054 -0.0247 117 ARG A NH2 
1683 N NH2 B ARG A 137 ? 0.3972 0.5240 0.5583 0.0843  0.0761  -0.0167 117 ARG A NH2 
1710 N N   . GLY A 138 ? 0.2887 0.3567 0.3566 -0.0183 -0.0027 0.0704  118 GLY A N   
1711 C CA  . GLY A 138 ? 0.3023 0.3569 0.3765 -0.0401 0.0008  0.0874  118 GLY A CA  
1712 C C   . GLY A 138 ? 0.2900 0.3131 0.3689 -0.0144 -0.0097 0.0844  118 GLY A C   
1713 O O   . GLY A 138 ? 0.2897 0.3224 0.3642 -0.0133 -0.0148 0.0783  118 GLY A O   
1718 N N   A GLN A 139 ? 0.2628 0.2806 0.3671 0.0237  -0.0286 0.0765  119 GLN A N   
1719 N N   B GLN A 139 ? 0.2910 0.2992 0.3625 0.0076  -0.0122 0.0902  119 GLN A N   
1720 C CA  A GLN A 139 ? 0.2691 0.2336 0.3599 0.0644  0.0060  0.0513  119 GLN A CA  
1721 C CA  B GLN A 139 ? 0.3042 0.2749 0.3499 0.0249  0.0101  0.0758  119 GLN A CA  
1722 C C   A GLN A 139 ? 0.2956 0.2364 0.3290 0.0806  0.0262  0.0445  119 GLN A C   
1723 C C   B GLN A 139 ? 0.3080 0.2564 0.3300 0.0538  0.0296  0.0522  119 GLN A C   
1724 O O   A GLN A 139 ? 0.3910 0.2592 0.3078 0.0821  0.0355  0.0335  119 GLN A O   
1725 O O   B GLN A 139 ? 0.3748 0.2730 0.3279 0.0598  0.0355  0.0475  119 GLN A O   
1726 C CB  A GLN A 139 ? 0.3220 0.2174 0.4329 0.0752  0.0708  0.0314  119 GLN A CB  
1727 C CB  B GLN A 139 ? 0.3524 0.2869 0.3866 0.0174  0.0221  0.0890  119 GLN A CB  
1728 C CG  A GLN A 139 ? 0.3708 0.2264 0.4952 0.0850  0.1037  0.0342  119 GLN A CG  
1729 C CG  B GLN A 139 ? 0.3841 0.3140 0.4109 0.0075  0.0000  0.1276  119 GLN A CG  
1730 C CD  A GLN A 139 ? 0.4762 0.2986 0.5735 0.0720  0.1243  0.0378  119 GLN A CD  
1731 C CD  B GLN A 139 ? 0.4394 0.3479 0.4272 -0.0237 -0.0040 0.1531  119 GLN A CD  
1732 O OE1 A GLN A 139 ? 0.5527 0.3051 0.5568 0.0533  0.1091  0.0449  119 GLN A OE1 
1733 O OE1 B GLN A 139 ? 0.4951 0.3785 0.4153 -0.0090 0.0256  0.1524  119 GLN A OE1 
1734 N NE2 A GLN A 139 ? 0.5100 0.3532 0.6243 0.0835  0.1452  0.0339  119 GLN A NE2 
1735 N NE2 B GLN A 139 ? 0.4440 0.3388 0.3733 -0.0816 -0.0684 0.1611  119 GLN A NE2 
1752 N N   . TYR A 140 ? 0.2601 0.2231 0.2939 0.0523  0.0213  0.0166  120 TYR A N   
1753 C CA  . TYR A 140 ? 0.2531 0.1992 0.2643 0.0403  0.0087  0.0115  120 TYR A CA  
1754 C C   . TYR A 140 ? 0.2392 0.2024 0.2570 0.0414  0.0287  0.0099  120 TYR A C   
1755 O O   . TYR A 140 ? 0.2581 0.2451 0.2814 0.0405  0.0240  -0.0216 120 TYR A O   
1756 C CB  . TYR A 140 ? 0.2317 0.2154 0.2531 0.0256  0.0155  0.0173  120 TYR A CB  
1757 C CG  . TYR A 140 ? 0.2292 0.1977 0.2633 0.0275  0.0250  0.0075  120 TYR A CG  
1758 C CD1 . TYR A 140 ? 0.2247 0.1800 0.2607 0.0193  0.0247  -0.0037 120 TYR A CD1 
1759 C CD2 . TYR A 140 ? 0.2406 0.1986 0.2688 0.0182  0.0296  0.0091  120 TYR A CD2 
1760 C CE1 . TYR A 140 ? 0.2426 0.1779 0.2550 0.0198  0.0280  -0.0073 120 TYR A CE1 
1761 C CE2 . TYR A 140 ? 0.2530 0.1999 0.2717 0.0010  0.0358  0.0132  120 TYR A CE2 
1762 C CZ  . TYR A 140 ? 0.2423 0.1909 0.2675 0.0043  0.0412  -0.0069 120 TYR A CZ  
1763 O OH  . TYR A 140 ? 0.2465 0.2114 0.2891 0.0223  0.0316  -0.0204 120 TYR A OH  
1774 N N   A ARG A 141 ? 0.2321 0.1983 0.2722 0.0428  0.0433  0.0172  121 ARG A N   
1775 N N   B ARG A 141 ? 0.2344 0.2001 0.2761 0.0407  0.0384  0.0200  121 ARG A N   
1776 C CA  A ARG A 141 ? 0.2339 0.1988 0.2832 0.0295  0.0327  0.0155  121 ARG A CA  
1777 C CA  B ARG A 141 ? 0.2384 0.2017 0.2824 0.0251  0.0154  0.0151  121 ARG A CA  
1778 C C   A ARG A 141 ? 0.2054 0.2129 0.2674 0.0199  0.0405  -0.0122 121 ARG A C   
1779 C C   B ARG A 141 ? 0.2256 0.2133 0.2528 0.0171  0.0019  -0.0165 121 ARG A C   
1780 O O   A ARG A 141 ? 0.2081 0.2388 0.2808 0.0316  0.0639  -0.0056 121 ARG A O   
1781 O O   B ARG A 141 ? 0.2851 0.2423 0.2265 0.0460  -0.0271 -0.0062 121 ARG A O   
1782 C CB  A ARG A 141 ? 0.2955 0.1952 0.3652 0.0205  0.0132  0.0423  121 ARG A CB  
1783 C CB  B ARG A 141 ? 0.2881 0.2036 0.3721 0.0120  0.0057  0.0417  121 ARG A CB  
1784 C CG  A ARG A 141 ? 0.3751 0.2239 0.4161 0.0269  0.0193  0.0601  121 ARG A CG  
1785 C CG  B ARG A 141 ? 0.3751 0.2446 0.4362 0.0140  0.0443  0.0593  121 ARG A CG  
1786 C CD  A ARG A 141 ? 0.4191 0.2559 0.4802 0.0437  -0.0402 0.0705  121 ARG A CD  
1787 C CD  B ARG A 141 ? 0.4210 0.2903 0.5265 0.0113  0.0061  0.0563  121 ARG A CD  
1788 N NE  A ARG A 141 ? 0.4890 0.2922 0.5378 0.0399  -0.0422 0.0791  121 ARG A NE  
1789 N NE  B ARG A 141 ? 0.4426 0.3351 0.5810 0.0063  0.0032  0.0792  121 ARG A NE  
1790 C CZ  A ARG A 141 ? 0.5466 0.3359 0.5913 0.0436  -0.0380 0.1029  121 ARG A CZ  
1791 C CZ  B ARG A 141 ? 0.4822 0.3560 0.6095 0.0293  0.0042  0.1080  121 ARG A CZ  
1792 N NH1 A ARG A 141 ? 0.5416 0.3365 0.6255 0.0428  -0.0378 0.1163  121 ARG A NH1 
1793 N NH1 B ARG A 141 ? 0.4961 0.3381 0.6154 0.0378  0.0341  0.1083  121 ARG A NH1 
1794 N NH2 A ARG A 141 ? 0.5793 0.3750 0.6134 0.0463  -0.0541 0.0909  121 ARG A NH2 
1795 N NH2 B ARG A 141 ? 0.4263 0.3652 0.6094 0.0199  -0.0439 0.1269  121 ARG A NH2 
1822 N N   . ASN A 142 ? 0.2150 0.1962 0.2580 0.0286  0.0135  -0.0044 122 ASN A N   
1823 C CA  . ASN A 142 ? 0.2281 0.1744 0.2394 0.0296  0.0227  -0.0089 122 ASN A CA  
1824 C C   . ASN A 142 ? 0.2245 0.1721 0.2413 0.0194  0.0342  0.0080  122 ASN A C   
1825 O O   . ASN A 142 ? 0.2342 0.1807 0.2433 0.0158  0.0187  -0.0151 122 ASN A O   
1826 C CB  . ASN A 142 ? 0.2346 0.1951 0.2449 0.0349  0.0297  -0.0195 122 ASN A CB  
1827 C CG  . ASN A 142 ? 0.2229 0.2466 0.2489 0.0289  0.0024  -0.0259 122 ASN A CG  
1828 O OD1 . ASN A 142 ? 0.2095 0.2735 0.2674 0.0276  0.0237  -0.0427 122 ASN A OD1 
1829 N ND2 . ASN A 142 ? 0.2512 0.2336 0.2400 0.0286  0.0329  -0.0156 122 ASN A ND2 
1837 N N   . HIS A 143 ? 0.2088 0.1916 0.2393 0.0107  0.0334  0.0010  123 HIS A N   
1838 C CA  . HIS A 143 ? 0.2132 0.1758 0.2319 -0.0015 0.0381  0.0081  123 HIS A CA  
1839 C C   . HIS A 143 ? 0.2228 0.1741 0.2155 -0.0021 0.0457  0.0119  123 HIS A C   
1840 O O   . HIS A 143 ? 0.2427 0.1977 0.2198 -0.0157 0.0356  0.0091  123 HIS A O   
1841 C CB  . HIS A 143 ? 0.2122 0.1723 0.2478 -0.0158 0.0451  0.0138  123 HIS A CB  
1842 C CG  . HIS A 143 ? 0.2243 0.1954 0.2535 -0.0106 0.0549  -0.0034 123 HIS A CG  
1843 N ND1 . HIS A 143 ? 0.2406 0.2057 0.2742 0.0018  0.0261  -0.0318 123 HIS A ND1 
1844 C CD2 . HIS A 143 ? 0.2740 0.2465 0.2547 -0.0104 0.0548  0.0329  123 HIS A CD2 
1845 C CE1 . HIS A 143 ? 0.2414 0.2369 0.2748 0.0256  0.0283  0.0047  123 HIS A CE1 
1846 N NE2 . HIS A 143 ? 0.2537 0.2701 0.2318 0.0029  0.0330  0.0137  123 HIS A NE2 
1855 N N   . PHE A 144 ? 0.2108 0.1537 0.2160 0.0068  0.0283  0.0057  124 PHE A N   
1856 C CA  . PHE A 144 ? 0.2154 0.1499 0.2033 0.0147  0.0262  0.0008  124 PHE A CA  
1857 C C   . PHE A 144 ? 0.2218 0.1514 0.2211 -0.0005 0.0364  -0.0061 124 PHE A C   
1858 O O   . PHE A 144 ? 0.2218 0.1609 0.2560 -0.0115 0.0062  0.0013  124 PHE A O   
1859 C CB  . PHE A 144 ? 0.2233 0.1594 0.2306 0.0024  0.0609  -0.0072 124 PHE A CB  
1860 C CG  . PHE A 144 ? 0.2142 0.1644 0.2402 0.0039  0.0636  -0.0088 124 PHE A CG  
1861 C CD1 . PHE A 144 ? 0.2421 0.1805 0.2598 0.0174  0.0538  -0.0020 124 PHE A CD1 
1862 C CD2 . PHE A 144 ? 0.2034 0.1912 0.2740 0.0203  0.0680  -0.0255 124 PHE A CD2 
1863 C CE1 . PHE A 144 ? 0.2629 0.2204 0.2702 0.0313  0.0598  -0.0120 124 PHE A CE1 
1864 C CE2 . PHE A 144 ? 0.2112 0.2418 0.2743 0.0307  0.0359  -0.0503 124 PHE A CE2 
1865 C CZ  . PHE A 144 ? 0.2426 0.2530 0.2579 0.0375  0.0368  -0.0418 124 PHE A CZ  
1875 N N   . LEU A 145 ? 0.2068 0.1547 0.2083 -0.0111 0.0381  -0.0046 125 LEU A N   
1876 C CA  . LEU A 145 ? 0.1768 0.1804 0.1945 -0.0024 0.0419  0.0005  125 LEU A CA  
1877 C C   . LEU A 145 ? 0.1879 0.1757 0.2134 -0.0162 0.0476  0.0049  125 LEU A C   
1878 O O   . LEU A 145 ? 0.2215 0.2100 0.2117 -0.0348 0.0330  0.0117  125 LEU A O   
1879 C CB  . LEU A 145 ? 0.1760 0.2302 0.2271 -0.0149 0.0536  -0.0070 125 LEU A CB  
1880 C CG  . LEU A 145 ? 0.1972 0.2669 0.2826 0.0071  0.0585  -0.0153 125 LEU A CG  
1881 C CD1 . LEU A 145 ? 0.2130 0.3145 0.2471 0.0019  0.0575  -0.0011 125 LEU A CD1 
1882 C CD2 . LEU A 145 ? 0.2070 0.2643 0.3402 -0.0048 0.0729  -0.0202 125 LEU A CD2 
1894 N N   . HIS A 146 ? 0.1992 0.1679 0.2021 -0.0186 0.0338  0.0134  126 HIS A N   
1895 C CA  . HIS A 146 ? 0.1941 0.1643 0.2153 -0.0034 0.0260  0.0134  126 HIS A CA  
1896 C C   . HIS A 146 ? 0.1904 0.1838 0.2079 -0.0059 0.0381  0.0201  126 HIS A C   
1897 O O   . HIS A 146 ? 0.1899 0.1950 0.2341 -0.0090 0.0249  0.0294  126 HIS A O   
1898 C CB  . HIS A 146 ? 0.2174 0.1610 0.2262 0.0197  0.0458  0.0116  126 HIS A CB  
1899 C CG  . HIS A 146 ? 0.2453 0.1828 0.2501 -0.0022 0.0659  0.0060  126 HIS A CG  
1900 N ND1 . HIS A 146 ? 0.2417 0.2182 0.3040 0.0201  0.0715  0.0188  126 HIS A ND1 
1901 C CD2 . HIS A 146 ? 0.2440 0.2130 0.2618 0.0099  0.0373  -0.0049 126 HIS A CD2 
1902 C CE1 . HIS A 146 ? 0.2510 0.2230 0.2916 0.0332  0.0530  0.0177  126 HIS A CE1 
1903 N NE2 . HIS A 146 ? 0.2464 0.2060 0.2642 0.0261  0.0410  0.0191  126 HIS A NE2 
1911 N N   . SER A 147 ? 0.1923 0.1774 0.2198 -0.0164 0.0344  0.0340  127 SER A N   
1912 C CA  . SER A 147 ? 0.1934 0.1807 0.2220 0.0043  0.0562  0.0312  127 SER A CA  
1913 C C   . SER A 147 ? 0.1837 0.1690 0.2219 0.0077  0.0333  0.0088  127 SER A C   
1914 O O   . SER A 147 ? 0.1987 0.1949 0.2292 -0.0031 0.0458  0.0215  127 SER A O   
1915 C CB  . SER A 147 ? 0.2108 0.1596 0.2349 0.0126  0.0714  0.0429  127 SER A CB  
1916 O OG  . SER A 147 ? 0.2318 0.1680 0.2285 0.0213  0.0579  0.0266  127 SER A OG  
1922 N N   . PHE A 148 ? 0.1949 0.1818 0.2034 -0.0002 0.0387  0.0108  128 PHE A N   
1923 C CA  . PHE A 148 ? 0.1978 0.1996 0.2006 -0.0020 0.0366  0.0225  128 PHE A CA  
1924 C C   . PHE A 148 ? 0.2191 0.2013 0.2007 -0.0038 0.0481  0.0239  128 PHE A C   
1925 O O   . PHE A 148 ? 0.2118 0.2118 0.2302 0.0026  0.0280  0.0371  128 PHE A O   
1926 C CB  . PHE A 148 ? 0.2094 0.2060 0.2255 0.0027  0.0195  0.0159  128 PHE A CB  
1927 C CG  . PHE A 148 ? 0.2221 0.1886 0.2019 0.0045  0.0439  0.0084  128 PHE A CG  
1928 C CD1 . PHE A 148 ? 0.2374 0.1926 0.2109 0.0008  0.0531  0.0122  128 PHE A CD1 
1929 C CD2 . PHE A 148 ? 0.2217 0.2040 0.2465 0.0336  0.0804  0.0354  128 PHE A CD2 
1930 C CE1 . PHE A 148 ? 0.2343 0.1966 0.2245 0.0020  0.0532  0.0199  128 PHE A CE1 
1931 C CE2 . PHE A 148 ? 0.2207 0.2108 0.2553 0.0143  0.0756  0.0273  128 PHE A CE2 
1932 C CZ  . PHE A 148 ? 0.2276 0.2013 0.2358 0.0117  0.0561  0.0197  128 PHE A CZ  
1942 N N   . ARG A 149 ? 0.2233 0.1912 0.2192 0.0028  0.0423  0.0231  129 ARG A N   
1943 C CA  . ARG A 149 ? 0.2402 0.2093 0.2346 0.0220  0.0537  0.0427  129 ARG A CA  
1944 C C   . ARG A 149 ? 0.2391 0.2235 0.2347 0.0156  0.0689  0.0511  129 ARG A C   
1945 O O   . ARG A 149 ? 0.2324 0.2445 0.2543 0.0007  0.0751  0.0259  129 ARG A O   
1946 C CB  . ARG A 149 ? 0.2690 0.2153 0.2532 0.0203  0.0694  0.0397  129 ARG A CB  
1947 C CG  . ARG A 149 ? 0.3050 0.2054 0.2641 0.0448  0.0777  0.0346  129 ARG A CG  
1948 C CD  . ARG A 149 ? 0.3225 0.2073 0.2719 0.0443  0.0764  0.0504  129 ARG A CD  
1949 N NE  . ARG A 149 ? 0.3250 0.2190 0.3197 0.0460  0.0685  0.0541  129 ARG A NE  
1950 C CZ  . ARG A 149 ? 0.3583 0.2315 0.3758 0.0486  0.0786  0.0521  129 ARG A CZ  
1951 N NH1 . ARG A 149 ? 0.4315 0.2311 0.3765 0.0251  0.0821  0.0298  129 ARG A NH1 
1952 N NH2 . ARG A 149 ? 0.3718 0.2510 0.4140 0.0813  0.0834  0.0749  129 ARG A NH2 
1966 N N   . PHE A 150 ? 0.2386 0.2424 0.2208 0.0206  0.0525  0.0575  130 PHE A N   
1967 C CA  . PHE A 150 ? 0.2451 0.2477 0.2217 0.0033  0.0688  0.0560  130 PHE A CA  
1968 C C   . PHE A 150 ? 0.2526 0.2582 0.2499 0.0157  0.0667  0.0631  130 PHE A C   
1969 O O   . PHE A 150 ? 0.2922 0.2814 0.2863 0.0423  0.0810  0.0830  130 PHE A O   
1970 C CB  . PHE A 150 ? 0.2639 0.2561 0.2301 -0.0014 0.0345  0.0405  130 PHE A CB  
1971 C CG  . PHE A 150 ? 0.2480 0.2422 0.2342 0.0091  0.0327  0.0441  130 PHE A CG  
1972 C CD1 . PHE A 150 ? 0.2669 0.2432 0.2340 -0.0059 0.0376  0.0403  130 PHE A CD1 
1973 C CD2 . PHE A 150 ? 0.2402 0.2414 0.2508 0.0143  0.0443  0.0493  130 PHE A CD2 
1974 C CE1 . PHE A 150 ? 0.2594 0.2494 0.2304 -0.0099 0.0276  0.0317  130 PHE A CE1 
1975 C CE2 . PHE A 150 ? 0.2442 0.2285 0.3036 0.0138  0.0335  0.0386  130 PHE A CE2 
1976 C CZ  . PHE A 150 ? 0.2407 0.2352 0.2644 -0.0006 0.0108  0.0420  130 PHE A CZ  
1986 N N   . GLU A 151 ? 0.2937 0.2552 0.2688 0.0099  0.0801  0.0747  131 GLU A N   
1987 C CA  . GLU A 151 ? 0.3362 0.2605 0.2621 0.0093  0.0633  0.0791  131 GLU A CA  
1988 C C   . GLU A 151 ? 0.3111 0.2977 0.2505 0.0286  0.0547  0.0707  131 GLU A C   
1989 O O   . GLU A 151 ? 0.3098 0.2763 0.2904 0.0178  0.0689  0.0741  131 GLU A O   
1990 C CB  . GLU A 151 ? 0.4244 0.2707 0.3025 0.0151  0.0718  0.1176  131 GLU A CB  
1991 C CG  . GLU A 151 ? 0.5052 0.3264 0.3793 0.0183  0.0934  0.0868  131 GLU A CG  
1992 C CD  . GLU A 151 ? 0.5943 0.3780 0.4763 -0.0183 0.1166  0.0586  131 GLU A CD  
1993 O OE1 . GLU A 151 ? 0.6372 0.3795 0.5296 0.0032  0.1354  0.0322  131 GLU A OE1 
1994 O OE2 . GLU A 151 ? 0.6179 0.4095 0.5033 -0.0665 0.1295  0.0682  131 GLU A OE2 
2001 N N   . ASN A 152 ? 0.3448 0.3456 0.2641 0.0265  0.0396  0.0650  132 ASN A N   
2002 C CA  . ASN A 152 ? 0.3846 0.3720 0.2538 0.0541  0.0407  0.0570  132 ASN A CA  
2003 C C   . ASN A 152 ? 0.3525 0.3420 0.2457 0.0361  0.0272  0.0662  132 ASN A C   
2004 O O   . ASN A 152 ? 0.3866 0.3595 0.2737 0.0216  0.0630  0.0309  132 ASN A O   
2005 C CB  . ASN A 152 ? 0.4301 0.4132 0.2747 0.0535  0.0779  0.0719  132 ASN A CB  
2006 C CG  . ASN A 152 ? 0.4582 0.4554 0.2988 0.0557  0.0939  0.0466  132 ASN A CG  
2007 O OD1 . ASN A 152 ? 0.4867 0.4959 0.3080 0.0647  0.0655  0.0445  132 ASN A OD1 
2008 N ND2 . ASN A 152 ? 0.4845 0.4344 0.3989 0.0610  0.2167  0.0841  132 ASN A ND2 
2015 N N   . GLY A 153 ? 0.3359 0.3143 0.2781 0.0085  0.0028  0.0529  133 GLY A N   
2016 C CA  . GLY A 153 ? 0.3033 0.3182 0.3314 -0.0235 -0.0136 0.0403  133 GLY A CA  
2017 C C   . GLY A 153 ? 0.2411 0.3012 0.2595 -0.0012 0.0254  0.0466  133 GLY A C   
2018 O O   . GLY A 153 ? 0.2506 0.3046 0.2520 -0.0044 0.0212  0.0241  133 GLY A O   
2022 N N   . LEU A 154 ? 0.2299 0.2808 0.2500 -0.0114 0.0541  0.0220  134 LEU A N   
2023 C CA  . LEU A 154 ? 0.2452 0.2713 0.2110 0.0008  0.0412  0.0329  134 LEU A CA  
2024 C C   . LEU A 154 ? 0.2408 0.2533 0.2302 0.0047  0.0504  0.0371  134 LEU A C   
2025 O O   . LEU A 154 ? 0.2552 0.2537 0.2413 0.0167  0.0696  0.0509  134 LEU A O   
2026 C CB  . LEU A 154 ? 0.2566 0.2806 0.2210 -0.0008 0.0490  0.0273  134 LEU A CB  
2027 C CG  . LEU A 154 ? 0.2625 0.3129 0.2264 -0.0110 0.0533  0.0330  134 LEU A CG  
2028 C CD1 . LEU A 154 ? 0.2883 0.3583 0.2457 -0.0167 0.0614  0.0216  134 LEU A CD1 
2029 C CD2 . LEU A 154 ? 0.2895 0.3250 0.2436 0.0072  0.0305  0.0012  134 LEU A CD2 
2041 N N   . ILE A 155 ? 0.2424 0.2538 0.2119 0.0126  0.0640  0.0466  135 ILE A N   
2042 C CA  . ILE A 155 ? 0.2399 0.2456 0.2225 -0.0034 0.0707  0.0499  135 ILE A CA  
2043 C C   . ILE A 155 ? 0.2200 0.2369 0.2238 -0.0077 0.0631  0.0406  135 ILE A C   
2044 O O   . ILE A 155 ? 0.2262 0.2520 0.2680 -0.0104 0.0807  0.0588  135 ILE A O   
2045 C CB  . ILE A 155 ? 0.2402 0.2195 0.2133 0.0027  0.0604  0.0497  135 ILE A CB  
2046 C CG1 . ILE A 155 ? 0.2621 0.2156 0.2229 0.0074  0.0654  0.0398  135 ILE A CG1 
2047 C CG2 . ILE A 155 ? 0.2540 0.2302 0.2244 0.0109  0.0520  0.0470  135 ILE A CG2 
2048 C CD1 . ILE A 155 ? 0.2567 0.2178 0.2176 0.0039  0.0648  0.0204  135 ILE A CD1 
2060 N N   . LYS A 156 ? 0.2501 0.2140 0.2378 -0.0031 0.0734  0.0295  136 LYS A N   
2061 C CA  . LYS A 156 ? 0.2756 0.2304 0.2441 -0.0029 0.0648  0.0446  136 LYS A CA  
2062 C C   . LYS A 156 ? 0.2296 0.2445 0.2467 -0.0124 0.0511  0.0396  136 LYS A C   
2063 O O   . LYS A 156 ? 0.2339 0.2492 0.2658 -0.0245 0.0588  0.0520  136 LYS A O   
2064 C CB  . LYS A 156 ? 0.3489 0.2550 0.2968 0.0172  0.0615  0.0658  136 LYS A CB  
2065 C CG  . LYS A 156 ? 0.3758 0.2962 0.3620 0.0252  0.0867  0.0703  136 LYS A CG  
2066 C CD  . LYS A 156 ? 0.4557 0.3215 0.4888 -0.0047 0.1217  0.0390  136 LYS A CD  
2067 C CE  . LYS A 156 ? 0.5481 0.3859 0.6180 0.0172  0.1060  0.0304  136 LYS A CE  
2068 N NZ  . LYS A 156 ? 0.6001 0.4448 0.6790 0.0057  0.0848  0.0278  136 LYS A NZ  
2082 N N   . GLU A 157 ? 0.2408 0.2256 0.2352 -0.0211 0.0603  0.0433  137 GLU A N   
2083 C CA  . GLU A 157 ? 0.2414 0.2004 0.2540 -0.0101 0.0556  0.0290  137 GLU A CA  
2084 C C   . GLU A 157 ? 0.2365 0.1984 0.2352 0.0017  0.0530  0.0442  137 GLU A C   
2085 O O   . GLU A 157 ? 0.2176 0.2113 0.2528 -0.0038 0.0553  0.0345  137 GLU A O   
2086 C CB  . GLU A 157 ? 0.3154 0.1955 0.2446 -0.0117 0.0546  0.0133  137 GLU A CB  
2087 C CG  . GLU A 157 ? 0.3387 0.1922 0.2791 -0.0342 0.0762  -0.0072 137 GLU A CG  
2088 C CD  . GLU A 157 ? 0.3773 0.2031 0.3226 -0.0303 0.1082  0.0122  137 GLU A CD  
2089 O OE1 . GLU A 157 ? 0.3621 0.2126 0.3004 -0.0306 0.0936  0.0179  137 GLU A OE1 
2090 O OE2 . GLU A 157 ? 0.3759 0.2518 0.4194 -0.0202 0.0897  0.0070  137 GLU A OE2 
2097 N N   . GLN A 158 ? 0.2175 0.1868 0.2247 -0.0189 0.0567  0.0430  138 GLN A N   
2098 C CA  . GLN A 158 ? 0.2147 0.1756 0.2172 -0.0110 0.0416  0.0163  138 GLN A CA  
2099 C C   . GLN A 158 ? 0.2041 0.1767 0.2272 -0.0213 0.0688  0.0118  138 GLN A C   
2100 O O   . GLN A 158 ? 0.2180 0.2322 0.2259 -0.0316 0.0687  0.0131  138 GLN A O   
2101 C CB  . GLN A 158 ? 0.2566 0.1847 0.2300 -0.0195 0.0665  0.0127  138 GLN A CB  
2102 C CG  . GLN A 158 ? 0.2395 0.1907 0.2675 -0.0119 0.0624  -0.0043 138 GLN A CG  
2103 C CD  . GLN A 158 ? 0.2715 0.2449 0.2740 -0.0024 0.0888  0.0110  138 GLN A CD  
2104 O OE1 . GLN A 158 ? 0.2832 0.2598 0.2768 -0.0255 0.0404  0.0283  138 GLN A OE1 
2105 N NE2 . GLN A 158 ? 0.2736 0.2716 0.2816 0.0046  0.0720  0.0245  138 GLN A NE2 
2114 N N   . ARG A 159 ? 0.1924 0.1844 0.2139 -0.0186 0.0511  0.0249  139 ARG A N   
2115 C CA  . ARG A 159 ? 0.2025 0.1797 0.2208 -0.0063 0.0378  0.0258  139 ARG A CA  
2116 C C   . ARG A 159 ? 0.1863 0.1844 0.2290 -0.0045 0.0358  0.0338  139 ARG A C   
2117 O O   . ARG A 159 ? 0.1936 0.2246 0.2387 -0.0326 0.0274  0.0405  139 ARG A O   
2118 C CB  . ARG A 159 ? 0.2172 0.1588 0.2246 -0.0109 0.0409  0.0102  139 ARG A CB  
2119 C CG  . ARG A 159 ? 0.2353 0.1449 0.2436 -0.0044 0.0464  0.0239  139 ARG A CG  
2120 C CD  . ARG A 159 ? 0.2413 0.1643 0.2489 0.0049  0.0425  0.0293  139 ARG A CD  
2121 N NE  . ARG A 159 ? 0.2393 0.1855 0.2415 0.0049  0.0542  0.0189  139 ARG A NE  
2122 C CZ  . ARG A 159 ? 0.2522 0.1662 0.2367 0.0122  0.0640  0.0304  139 ARG A CZ  
2123 N NH1 . ARG A 159 ? 0.2448 0.1762 0.2438 -0.0011 0.0604  0.0208  139 ARG A NH1 
2124 N NH2 . ARG A 159 ? 0.2452 0.1687 0.2412 0.0097  0.0612  0.0315  139 ARG A NH2 
2138 N N   . GLU A 160 ? 0.1967 0.1877 0.2213 -0.0125 0.0382  0.0375  140 GLU A N   
2139 C CA  . GLU A 160 ? 0.2190 0.1949 0.2163 -0.0134 0.0536  0.0337  140 GLU A CA  
2140 C C   . GLU A 160 ? 0.2011 0.1816 0.2114 -0.0220 0.0336  0.0261  140 GLU A C   
2141 O O   . GLU A 160 ? 0.2056 0.1860 0.2407 -0.0394 0.0432  0.0226  140 GLU A O   
2142 C CB  . GLU A 160 ? 0.2998 0.2535 0.2640 0.0236  0.0837  0.0175  140 GLU A CB  
2143 C CG  . GLU A 160 ? 0.3026 0.2678 0.2875 -0.0182 0.0591  0.0058  140 GLU A CG  
2144 C CD  . GLU A 160 ? 0.3183 0.3201 0.2826 0.0154  0.0619  0.0010  140 GLU A CD  
2145 O OE1 . GLU A 160 ? 0.2956 0.3471 0.3123 0.0375  0.0393  0.0150  140 GLU A OE1 
2146 O OE2 . GLU A 160 ? 0.3660 0.3230 0.3361 0.0175  0.0738  0.0029  140 GLU A OE2 
2153 N N   . PHE A 161 ? 0.1963 0.1790 0.2081 -0.0307 0.0479  0.0147  141 PHE A N   
2154 C CA  . PHE A 161 ? 0.2004 0.1689 0.2034 -0.0338 0.0337  0.0176  141 PHE A CA  
2155 C C   . PHE A 161 ? 0.2147 0.1618 0.1913 -0.0383 0.0350  0.0025  141 PHE A C   
2156 O O   . PHE A 161 ? 0.2266 0.1718 0.2064 -0.0268 0.0341  0.0077  141 PHE A O   
2157 C CB  . PHE A 161 ? 0.1893 0.1827 0.2275 -0.0137 0.0484  0.0357  141 PHE A CB  
2158 C CG  . PHE A 161 ? 0.1958 0.1738 0.2244 -0.0033 0.0486  0.0468  141 PHE A CG  
2159 C CD1 . PHE A 161 ? 0.2065 0.2037 0.2287 -0.0187 0.0648  0.0420  141 PHE A CD1 
2160 C CD2 . PHE A 161 ? 0.2278 0.1586 0.2524 -0.0002 0.0487  0.0214  141 PHE A CD2 
2161 C CE1 . PHE A 161 ? 0.2046 0.2052 0.2395 -0.0008 0.0603  0.0649  141 PHE A CE1 
2162 C CE2 . PHE A 161 ? 0.2073 0.1813 0.3078 0.0102  0.0602  0.0258  141 PHE A CE2 
2163 C CZ  . PHE A 161 ? 0.2276 0.1884 0.2769 0.0080  0.0543  0.0588  141 PHE A CZ  
2173 N N   . MET A 162 ? 0.2148 0.1533 0.1997 -0.0264 0.0258  0.0024  142 MET A N   
2174 C CA  . MET A 162 ? 0.2241 0.1419 0.2104 -0.0236 0.0264  0.0198  142 MET A CA  
2175 C C   . MET A 162 ? 0.2063 0.1457 0.2214 -0.0177 0.0327  0.0132  142 MET A C   
2176 O O   . MET A 162 ? 0.2688 0.1771 0.2095 -0.0064 0.0315  0.0025  142 MET A O   
2177 C CB  . MET A 162 ? 0.2193 0.1693 0.2270 -0.0013 0.0339  0.0068  142 MET A CB  
2178 C CG  . MET A 162 ? 0.2436 0.2171 0.2291 0.0151  0.0355  -0.0150 142 MET A CG  
2179 S SD  . MET A 162 ? 0.2335 0.2662 0.2559 -0.0125 0.0481  -0.0096 142 MET A SD  
2180 C CE  . MET A 162 ? 0.1956 0.2688 0.2686 -0.0089 0.0514  0.0021  142 MET A CE  
2190 N N   . ASN A 163 ? 0.2190 0.1599 0.2177 -0.0110 0.0298  0.0309  143 ASN A N   
2191 C CA  . ASN A 163 ? 0.2040 0.1712 0.2175 -0.0175 0.0276  0.0302  143 ASN A CA  
2192 C C   . ASN A 163 ? 0.2180 0.1687 0.2071 -0.0074 0.0520  0.0058  143 ASN A C   
2193 O O   . ASN A 163 ? 0.2189 0.1765 0.2417 0.0092  0.0412  -0.0007 143 ASN A O   
2194 C CB  . ASN A 163 ? 0.2264 0.1865 0.2355 -0.0052 0.0415  0.0290  143 ASN A CB  
2195 C CG  . ASN A 163 ? 0.2178 0.2230 0.2280 0.0008  0.0401  0.0170  143 ASN A CG  
2196 O OD1 . ASN A 163 ? 0.2178 0.2257 0.2267 0.0118  0.0265  0.0072  143 ASN A OD1 
2197 N ND2 . ASN A 163 ? 0.2757 0.2436 0.2438 -0.0298 0.0872  0.0209  143 ASN A ND2 
2204 N N   . PRO A 164 ? 0.2040 0.1581 0.2245 0.0024  0.0403  -0.0020 144 PRO A N   
2205 C CA  . PRO A 164 ? 0.1947 0.1786 0.2388 -0.0026 0.0405  0.0022  144 PRO A CA  
2206 C C   . PRO A 164 ? 0.1995 0.1972 0.2228 0.0011  0.0431  0.0154  144 PRO A C   
2207 O O   . PRO A 164 ? 0.2040 0.2114 0.2529 0.0103  0.0302  0.0136  144 PRO A O   
2208 C CB  . PRO A 164 ? 0.2029 0.2271 0.2844 -0.0123 0.0317  -0.0022 144 PRO A CB  
2209 C CG  . PRO A 164 ? 0.2247 0.2340 0.2675 0.0052  0.0655  -0.0185 144 PRO A CG  
2210 C CD  . PRO A 164 ? 0.1954 0.1792 0.2357 0.0050  0.0391  -0.0136 144 PRO A CD  
2218 N N   . CYS A 165 ? 0.2026 0.1911 0.2333 0.0012  0.0351  0.0073  145 CYS A N   
2219 C CA  . CYS A 165 ? 0.2300 0.1988 0.2461 0.0197  0.0513  0.0271  145 CYS A CA  
2220 C C   . CYS A 165 ? 0.2073 0.2171 0.2365 0.0023  0.0305  0.0310  145 CYS A C   
2221 O O   . CYS A 165 ? 0.2116 0.2429 0.2394 0.0228  0.0279  0.0210  145 CYS A O   
2222 C CB  . CYS A 165 ? 0.2568 0.2443 0.2202 0.0383  0.0305  0.0179  145 CYS A CB  
2223 S SG  . CYS A 165 ? 0.2826 0.2843 0.2457 0.0457  0.0513  0.0075  145 CYS A SG  
2229 N N   . GLU A 166 ? 0.2012 0.2026 0.2426 0.0102  0.0248  0.0358  146 GLU A N   
2230 C CA  . GLU A 166 ? 0.2022 0.2080 0.2492 0.0178  0.0368  0.0356  146 GLU A CA  
2231 C C   . GLU A 166 ? 0.2147 0.2165 0.2534 0.0188  0.0211  0.0208  146 GLU A C   
2232 O O   . GLU A 166 ? 0.2283 0.2281 0.3034 0.0246  0.0346  0.0365  146 GLU A O   
2233 C CB  . GLU A 166 ? 0.2210 0.2721 0.2668 0.0081  0.0345  0.0415  146 GLU A CB  
2234 C CG  . GLU A 166 ? 0.2762 0.3315 0.3367 0.0015  0.0548  0.0303  146 GLU A CG  
2235 C CD  . GLU A 166 ? 0.3631 0.4281 0.4067 0.0286  0.1038  0.0133  146 GLU A CD  
2236 O OE1 . GLU A 166 ? 0.3684 0.4539 0.3865 0.0314  0.1049  0.0637  146 GLU A OE1 
2237 O OE2 . GLU A 166 ? 0.4799 0.5123 0.4521 0.0194  0.1732  0.0102  146 GLU A OE2 
2244 N N   . GLN A 167 ? 0.2066 0.1994 0.2348 0.0101  0.0456  0.0268  147 GLN A N   
2245 C CA  . GLN A 167 ? 0.2088 0.1960 0.2397 0.0103  0.0429  0.0255  147 GLN A CA  
2246 C C   . GLN A 167 ? 0.1898 0.2265 0.2462 0.0106  0.0509  0.0160  147 GLN A C   
2247 O O   . GLN A 167 ? 0.2048 0.2526 0.2434 0.0248  0.0418  0.0209  147 GLN A O   
2248 C CB  . GLN A 167 ? 0.2334 0.1996 0.2637 -0.0043 0.0322  0.0191  147 GLN A CB  
2249 C CG  . GLN A 167 ? 0.2325 0.2464 0.2822 -0.0046 0.0687  0.0325  147 GLN A CG  
2250 C CD  . GLN A 167 ? 0.2427 0.2798 0.2967 -0.0177 0.0386  0.0401  147 GLN A CD  
2251 O OE1 . GLN A 167 ? 0.2629 0.2998 0.2955 0.0014  0.0347  0.0184  147 GLN A OE1 
2252 N NE2 . GLN A 167 ? 0.2754 0.2931 0.3210 -0.0007 0.0689  0.0586  147 GLN A NE2 
2261 N N   . PHE A 168 ? 0.2068 0.2273 0.2419 0.0244  0.0403  0.0039  148 PHE A N   
2262 C CA  . PHE A 168 ? 0.2087 0.2448 0.2507 0.0212  0.0321  0.0098  148 PHE A CA  
2263 C C   . PHE A 168 ? 0.2050 0.2682 0.2497 0.0231  0.0321  0.0184  148 PHE A C   
2264 O O   . PHE A 168 ? 0.2177 0.2796 0.2641 0.0390  0.0182  0.0105  148 PHE A O   
2265 C CB  . PHE A 168 ? 0.2109 0.2609 0.2625 0.0242  0.0283  -0.0249 148 PHE A CB  
2266 C CG  . PHE A 168 ? 0.2049 0.2585 0.3355 0.0068  0.0462  -0.0489 148 PHE A CG  
2267 C CD1 . PHE A 168 ? 0.2214 0.2453 0.4406 0.0154  0.0643  -0.0389 148 PHE A CD1 
2268 C CD2 . PHE A 168 ? 0.2231 0.2551 0.3326 0.0011  0.0382  -0.0392 148 PHE A CD2 
2269 C CE1 . PHE A 168 ? 0.2794 0.2449 0.5354 0.0008  0.1684  -0.0429 148 PHE A CE1 
2270 C CE2 . PHE A 168 ? 0.2510 0.2436 0.4569 -0.0190 0.0708  -0.0545 148 PHE A CE2 
2271 C CZ  . PHE A 168 ? 0.2880 0.2458 0.5289 -0.0257 0.1592  -0.0400 148 PHE A CZ  
2281 N N   A ARG A 169 ? 0.1984 0.2521 0.2585 0.0353  0.0388  0.0335  149 ARG A N   
2282 N N   B ARG A 169 ? 0.2195 0.2762 0.2671 0.0285  0.0344  0.0369  149 ARG A N   
2283 C CA  A ARG A 169 ? 0.2098 0.2571 0.2837 0.0425  0.0438  0.0580  149 ARG A CA  
2284 C CA  B ARG A 169 ? 0.2433 0.2877 0.2990 0.0343  0.0524  0.0510  149 ARG A CA  
2285 C C   A ARG A 169 ? 0.2230 0.2642 0.2794 0.0404  0.0564  0.0583  149 ARG A C   
2286 C C   B ARG A 169 ? 0.2381 0.2712 0.2842 0.0374  0.0535  0.0529  149 ARG A C   
2287 O O   A ARG A 169 ? 0.2507 0.2767 0.3019 0.0600  0.0408  0.0610  149 ARG A O   
2288 O O   B ARG A 169 ? 0.2437 0.2793 0.2943 0.0410  0.0402  0.0625  149 ARG A O   
2289 C CB  A ARG A 169 ? 0.2212 0.2949 0.3120 0.0643  0.0675  0.0820  149 ARG A CB  
2290 C CB  B ARG A 169 ? 0.2752 0.3326 0.3478 0.0343  0.0604  0.0588  149 ARG A CB  
2291 C CG  A ARG A 169 ? 0.2434 0.3301 0.3196 0.0853  0.1168  0.1219  149 ARG A CG  
2292 C CG  B ARG A 169 ? 0.3079 0.3761 0.4232 0.0211  0.0953  0.0565  149 ARG A CG  
2293 C CD  A ARG A 169 ? 0.2846 0.3949 0.3954 0.0654  0.1495  0.0867  149 ARG A CD  
2294 C CD  B ARG A 169 ? 0.3232 0.4151 0.4859 0.0241  0.1407  0.0412  149 ARG A CD  
2295 N NE  A ARG A 169 ? 0.3672 0.4509 0.5433 0.0222  0.1497  0.0181  149 ARG A NE  
2296 N NE  B ARG A 169 ? 0.3318 0.4399 0.5520 0.0174  0.1478  0.0296  149 ARG A NE  
2297 C CZ  A ARG A 169 ? 0.3826 0.4811 0.6394 -0.0049 0.2013  -0.0140 149 ARG A CZ  
2298 C CZ  B ARG A 169 ? 0.3900 0.4722 0.6192 0.0092  0.1923  -0.0073 149 ARG A CZ  
2299 N NH1 A ARG A 169 ? 0.4674 0.4928 0.7045 -0.0187 0.1448  -0.0135 149 ARG A NH1 
2300 N NH1 B ARG A 169 ? 0.4258 0.4843 0.6587 -0.0034 0.1914  -0.0163 149 ARG A NH1 
2301 N NH2 A ARG A 169 ? 0.3280 0.4985 0.6379 -0.0305 0.2279  -0.0429 149 ARG A NH2 
2302 N NH2 B ARG A 169 ? 0.3673 0.4814 0.6439 0.0449  0.1957  -0.0177 149 ARG A NH2 
2329 N N   . SER A 170 ? 0.2320 0.2477 0.2657 0.0273  0.0473  0.0392  150 SER A N   
2330 C CA  . SER A 170 ? 0.2473 0.2517 0.2764 0.0292  0.0394  0.0068  150 SER A CA  
2331 C C   . SER A 170 ? 0.2351 0.2689 0.2789 0.0327  0.0439  0.0137  150 SER A C   
2332 O O   . SER A 170 ? 0.2423 0.2687 0.3101 0.0391  0.0352  -0.0061 150 SER A O   
2333 C CB  . SER A 170 ? 0.2503 0.2526 0.2990 0.0099  0.0482  0.0020  150 SER A CB  
2334 O OG  . SER A 170 ? 0.2420 0.2707 0.3014 0.0273  0.0418  0.0010  150 SER A OG  
2341 N N   . LEU A 171 ? 0.2067 0.2757 0.2638 0.0232  0.0314  0.0178  151 LEU A N   
2342 C CA  . LEU A 171 ? 0.2123 0.2768 0.2792 0.0231  0.0368  0.0176  151 LEU A CA  
2343 C C   . LEU A 171 ? 0.2245 0.2883 0.2722 0.0208  0.0240  0.0402  151 LEU A C   
2344 O O   . LEU A 171 ? 0.2385 0.3266 0.2879 0.0354  0.0313  0.0211  151 LEU A O   
2345 C CB  . LEU A 171 ? 0.2120 0.2787 0.2839 0.0012  0.0299  0.0124  151 LEU A CB  
2346 C CG  . LEU A 171 ? 0.2249 0.3014 0.2643 -0.0046 0.0434  0.0089  151 LEU A CG  
2347 C CD1 . LEU A 171 ? 0.2772 0.3121 0.2687 -0.0019 0.0473  0.0187  151 LEU A CD1 
2348 C CD2 . LEU A 171 ? 0.2129 0.3385 0.2965 -0.0026 0.0349  0.0075  151 LEU A CD2 
2360 N N   . GLY A 172 ? 0.2415 0.2880 0.2663 0.0393  0.0295  0.0437  152 GLY A N   
2361 C CA  . GLY A 172 ? 0.2628 0.3108 0.2655 0.0621  0.0419  0.0377  152 GLY A CA  
2362 C C   . GLY A 172 ? 0.2428 0.3503 0.2868 0.0694  0.0122  0.0179  152 GLY A C   
2363 O O   . GLY A 172 ? 0.2921 0.4156 0.2871 0.0776  0.0067  0.0196  152 GLY A O   
2367 N N   . ILE A 173 ? 0.2272 0.3322 0.2924 0.0431  0.0008  -0.0021 153 ILE A N   
2368 C CA  . ILE A 173 ? 0.2415 0.3458 0.2794 0.0288  0.0009  -0.0056 153 ILE A CA  
2369 C C   . ILE A 173 ? 0.2511 0.3936 0.2566 0.0531  0.0211  0.0206  153 ILE A C   
2370 O O   . ILE A 173 ? 0.2340 0.3939 0.2692 0.0415  0.0376  0.0028  153 ILE A O   
2371 C CB  . ILE A 173 ? 0.2368 0.3322 0.2978 0.0213  0.0211  -0.0265 153 ILE A CB  
2372 C CG1 . ILE A 173 ? 0.2235 0.3609 0.2840 0.0043  0.0332  -0.0201 153 ILE A CG1 
2373 C CG2 . ILE A 173 ? 0.2827 0.3198 0.3087 0.0306  0.0287  -0.0479 153 ILE A CG2 
2374 C CD1 . ILE A 173 ? 0.2486 0.3470 0.2987 0.0280  0.0146  0.0000  153 ILE A CD1 
2386 N N   . GLU A 174 ? 0.2712 0.4389 0.2667 0.0782  0.0237  0.0122  154 GLU A N   
2387 C CA  . GLU A 174 ? 0.3037 0.4841 0.2649 0.0946  0.0186  -0.0039 154 GLU A CA  
2388 C C   . GLU A 174 ? 0.2966 0.4330 0.2805 0.0858  0.0248  -0.0177 154 GLU A C   
2389 O O   . GLU A 174 ? 0.3140 0.4158 0.3193 0.0760  0.0282  -0.0146 154 GLU A O   
2390 C CB  . GLU A 174 ? 0.3427 0.5853 0.2847 0.0991  -0.0020 -0.0001 154 GLU A CB  
2391 C CG  . GLU A 174 ? 0.4908 0.6755 0.4153 0.0580  0.0216  0.0100  154 GLU A CG  
2396 N N   . VAL A 175 ? 0.2737 0.4059 0.2702 0.0851  0.0451  0.0252  155 VAL A N   
2397 C CA  . VAL A 175 ? 0.2756 0.3944 0.2726 0.0663  0.0669  0.0501  155 VAL A CA  
2398 C C   . VAL A 175 ? 0.2601 0.3688 0.3430 0.0431  0.0472  0.0452  155 VAL A C   
2399 O O   . VAL A 175 ? 0.2874 0.3503 0.2705 0.0472  0.0508  0.0143  155 VAL A O   
2400 C CB  . VAL A 175 ? 0.3022 0.4126 0.2785 0.1084  0.0540  0.0375  155 VAL A CB  
2401 C CG1 . VAL A 175 ? 0.3139 0.4069 0.2579 0.0962  0.0471  0.0482  155 VAL A CG1 
2402 C CG2 . VAL A 175 ? 0.3397 0.4577 0.3208 0.1558  0.0584  -0.0090 155 VAL A CG2 
2412 N N   . PRO A 176 ? 0.2552 0.3878 0.4978 0.0059  0.0902  -0.0138 156 PRO A N   
2413 C CA  . PRO A 176 ? 0.2752 0.4155 0.5717 0.0203  0.1100  -0.0525 156 PRO A CA  
2414 C C   . PRO A 176 ? 0.3038 0.4329 0.4481 0.0394  0.1564  -0.0619 156 PRO A C   
2415 O O   . PRO A 176 ? 0.2809 0.4039 0.3988 0.0434  0.1113  0.0035  156 PRO A O   
2426 N N   . GLU A 177 ? 0.3462 0.4863 0.4451 0.0436  0.1476  -0.1036 157 GLU A N   
2427 C CA  . GLU A 177 ? 0.3995 0.4940 0.4128 0.0321  0.1363  -0.0973 157 GLU A CA  
2428 C C   . GLU A 177 ? 0.3545 0.4746 0.3776 0.0096  0.0863  -0.1260 157 GLU A C   
2429 O O   . GLU A 177 ? 0.3386 0.5129 0.4180 0.0351  0.0577  -0.1569 157 GLU A O   
2430 C CB  . GLU A 177 ? 0.4513 0.5346 0.4691 0.0301  0.1746  -0.0529 157 GLU A CB  
2431 C CG  . GLU A 177 ? 0.4520 0.5546 0.4958 0.0280  0.1481  -0.0070 157 GLU A CG  
2436 N N   . VAL A 178 ? 0.3381 0.4101 0.2651 -0.0253 0.1117  -0.0491 158 VAL A N   
2437 C CA  . VAL A 178 ? 0.3303 0.3991 0.2424 -0.0152 0.1044  0.0057  158 VAL A CA  
2438 C C   . VAL A 178 ? 0.3135 0.3622 0.2563 -0.0021 0.1138  0.0094  158 VAL A C   
2439 O O   . VAL A 178 ? 0.3764 0.3718 0.3163 -0.0342 0.1530  -0.0118 158 VAL A O   
2440 C CB  . VAL A 178 ? 0.3375 0.4370 0.2525 -0.0572 0.0564  0.0461  158 VAL A CB  
2441 C CG1 . VAL A 178 ? 0.3247 0.4352 0.3078 -0.0387 0.0269  0.0623  158 VAL A CG1 
2442 C CG2 . VAL A 178 ? 0.3521 0.4660 0.2406 -0.0979 0.0603  0.0482  158 VAL A CG2 
2452 N N   . ARG A 179 ? 0.2907 0.3562 0.2219 0.0357  0.0801  0.0228  159 ARG A N   
2453 C CA  . ARG A 179 ? 0.3004 0.3785 0.2420 0.0461  0.0756  0.0419  159 ARG A CA  
2454 C C   . ARG A 179 ? 0.3310 0.3749 0.2493 0.0136  0.0734  0.0327  159 ARG A C   
2455 O O   . ARG A 179 ? 0.3266 0.3697 0.2995 0.0167  0.0640  0.0191  159 ARG A O   
2456 C CB  . ARG A 179 ? 0.3048 0.4537 0.2191 0.0295  0.0402  0.0404  159 ARG A CB  
2457 C CG  . ARG A 179 ? 0.3396 0.5134 0.2642 0.0296  -0.0045 0.0281  159 ARG A CG  
2458 C CD  . ARG A 179 ? 0.3862 0.5650 0.2970 0.0069  -0.0027 0.0405  159 ARG A CD  
2459 N NE  . ARG A 179 ? 0.4215 0.5954 0.2856 -0.0211 0.0074  -0.0022 159 ARG A NE  
2460 C CZ  . ARG A 179 ? 0.4491 0.6227 0.3229 0.0551  -0.0218 -0.0151 159 ARG A CZ  
2461 N NH1 . ARG A 179 ? 0.3748 0.6406 0.3628 0.0885  -0.0188 -0.0317 159 ARG A NH1 
2462 N NH2 . ARG A 179 ? 0.5141 0.6451 0.2777 0.0888  -0.0363 -0.0358 159 ARG A NH2 
2476 N N   . ARG A 180 ? 0.3417 0.3687 0.2575 0.0099  0.0865  0.0199  160 ARG A N   
2477 C CA  . ARG A 180 ? 0.3575 0.3787 0.2795 -0.0136 0.1069  -0.0028 160 ARG A CA  
2478 C C   . ARG A 180 ? 0.3752 0.3693 0.2578 -0.0237 0.0915  -0.0219 160 ARG A C   
2479 O O   . ARG A 180 ? 0.3745 0.3637 0.2953 -0.0448 0.0902  -0.0320 160 ARG A O   
2480 C CB  . ARG A 180 ? 0.3357 0.3921 0.2830 -0.0204 0.0968  -0.0269 160 ARG A CB  
2481 C CG  . ARG A 180 ? 0.3809 0.4124 0.3337 -0.0230 0.0755  -0.0370 160 ARG A CG  
2482 C CD  . ARG A 180 ? 0.3904 0.4260 0.3662 -0.0170 0.0872  0.0019  160 ARG A CD  
2483 N NE  . ARG A 180 ? 0.3528 0.4361 0.3516 0.0082  0.0620  0.0236  160 ARG A NE  
2484 C CZ  . ARG A 180 ? 0.3880 0.4354 0.3730 0.0032  0.0503  0.0192  160 ARG A CZ  
2485 N NH1 . ARG A 180 ? 0.4087 0.4377 0.4465 -0.0313 0.0885  0.0158  160 ARG A NH1 
2486 N NH2 . ARG A 180 ? 0.4284 0.4298 0.3368 0.0511  0.0391  0.0367  160 ARG A NH2 
2500 N N   . ASP A 181 ? 0.3985 0.3792 0.2562 -0.0058 0.1028  -0.0081 161 ASP A N   
2501 C CA  . ASP A 181 ? 0.4157 0.4052 0.2524 -0.0146 0.1190  0.0077  161 ASP A CA  
2502 C C   . ASP A 181 ? 0.3911 0.4010 0.2860 -0.0239 0.1133  -0.0210 161 ASP A C   
2503 O O   . ASP A 181 ? 0.4277 0.4082 0.3195 -0.0392 0.1568  -0.0177 161 ASP A O   
2504 C CB  . ASP A 181 ? 0.5111 0.4377 0.2597 0.0206  0.0705  0.0257  161 ASP A CB  
2505 C CG  . ASP A 181 ? 0.5987 0.4660 0.3301 0.0494  0.0446  0.0497  161 ASP A CG  
2506 O OD1 . ASP A 181 ? 0.6783 0.4742 0.3940 0.0628  0.0388  0.0788  161 ASP A OD1 
2507 O OD2 . ASP A 181 ? 0.5630 0.4732 0.3469 0.0637  0.0048  0.0556  161 ASP A OD2 
2512 N N   . GLY A 182 ? 0.3938 0.3773 0.2767 -0.0229 0.0871  -0.0179 162 GLY A N   
2513 C CA  . GLY A 182 ? 0.4090 0.3862 0.2742 -0.0141 0.1107  -0.0040 162 GLY A CA  
2514 C C   . GLY A 182 ? 0.4027 0.4002 0.2643 -0.0185 0.0795  0.0145  162 GLY A C   
2515 O O   . GLY A 182 ? 0.3934 0.3906 0.3010 -0.0464 0.0749  0.0046  162 GLY A O   
2519 N N   . LEU A 183 ? 0.4275 0.4376 0.2644 -0.0007 0.0427  -0.0073 163 LEU A N   
2520 C CA  . LEU A 183 ? 0.4304 0.4833 0.3004 0.0074  0.0239  -0.0534 163 LEU A CA  
2521 C C   . LEU A 183 ? 0.4365 0.5079 0.4073 0.0091  0.0504  -0.0899 163 LEU A C   
2522 O O   . LEU A 183 ? 0.4158 0.4807 0.4544 -0.0039 0.0199  -0.0802 163 LEU A O   
2523 C CB  . LEU A 183 ? 0.4658 0.5306 0.2785 -0.0214 0.0443  -0.0422 163 LEU A CB  
2524 C CG  . LEU A 183 ? 0.4580 0.5668 0.3335 -0.0134 0.0689  -0.0215 163 LEU A CG  
2525 C CD1 . LEU A 183 ? 0.4657 0.6009 0.3679 0.0184  0.1265  -0.0005 163 LEU A CD1 
2526 C CD2 . LEU A 183 ? 0.4754 0.5636 0.4036 -0.0302 -0.0102 -0.0201 163 LEU A CD2 
2538 N N   . PRO A 184 ? 0.4202 0.5658 0.5138 -0.0082 -0.0042 -0.1258 164 PRO A N   
2539 C CA  . PRO A 184 ? 0.3929 0.6084 0.6057 -0.0226 0.0225  -0.1406 164 PRO A CA  
2540 C C   . PRO A 184 ? 0.4567 0.6191 0.6642 -0.0548 0.0968  -0.1645 164 PRO A C   
2541 O O   . PRO A 184 ? 0.4527 0.6413 0.6837 -0.0397 0.1371  -0.2153 164 PRO A O   
2542 C CB  . PRO A 184 ? 0.3803 0.6130 0.6141 -0.0075 -0.0370 -0.1485 164 PRO A CB  
2543 C CG  . PRO A 184 ? 0.4131 0.6201 0.6203 -0.0100 -0.0293 -0.1464 164 PRO A CG  
2544 C CD  . PRO A 184 ? 0.4141 0.6024 0.6043 0.0121  -0.0317 -0.1318 164 PRO A CD  
2552 N N   . GLU B 32  ? 0.5193 1.0843 0.6403 -0.0077 -0.0672 -0.2718 12  GLU B N   
2553 C CA  . GLU B 32  ? 0.4754 1.0768 0.6183 0.0112  -0.0529 -0.2610 12  GLU B CA  
2554 C C   . GLU B 32  ? 0.4477 1.0482 0.5504 0.0280  -0.0066 -0.2665 12  GLU B C   
2555 O O   . GLU B 32  ? 0.3580 1.0389 0.5003 0.0483  -0.0293 -0.2974 12  GLU B O   
2556 C CB  . GLU B 32  ? 0.5168 1.0848 0.6524 0.0249  -0.0100 -0.2555 12  GLU B CB  
2558 N N   . ASN B 33  ? 0.5088 1.0238 0.5319 0.0152  0.0446  -0.2363 13  ASN B N   
2559 C CA  . ASN B 33  ? 0.5211 0.9898 0.4691 0.0024  0.0389  -0.1947 13  ASN B CA  
2560 C C   . ASN B 33  ? 0.4572 0.9392 0.4249 0.0118  0.0146  -0.1525 13  ASN B C   
2561 O O   . ASN B 33  ? 0.4243 0.9469 0.3694 0.0006  -0.0055 -0.1400 13  ASN B O   
2562 C CB  . ASN B 33  ? 0.5530 1.0044 0.4931 -0.0099 0.0555  -0.1649 13  ASN B CB  
2565 N N   . ARG B 34  ? 0.3995 0.8714 0.4766 0.0323  0.0000  -0.1198 14  ARG B N   
2566 C CA  . ARG B 34  ? 0.3728 0.7804 0.4856 0.0433  -0.0229 -0.1104 14  ARG B CA  
2567 C C   . ARG B 34  ? 0.3377 0.6302 0.4235 0.0398  -0.0741 -0.1187 14  ARG B C   
2568 O O   . ARG B 34  ? 0.3281 0.6761 0.4058 0.0477  -0.0397 -0.1142 14  ARG B O   
2569 C CB  . ARG B 34  ? 0.3866 0.8167 0.5392 0.0435  -0.0331 -0.1060 14  ARG B CB  
2582 N N   . GLN B 36  ? 0.3192 0.5224 0.3753 -0.0128 -0.0153 -0.1566 16  GLN B N   
2583 C CA  . GLN B 36  ? 0.2916 0.6451 0.3892 -0.0139 -0.0250 -0.1420 16  GLN B CA  
2584 C C   . GLN B 36  ? 0.2713 0.6607 0.3513 -0.0589 0.0218  -0.0998 16  GLN B C   
2585 O O   . GLN B 36  ? 0.2510 0.6700 0.3363 -0.0651 0.0207  -0.1009 16  GLN B O   
2586 C CB  . GLN B 36  ? 0.3351 0.7277 0.4429 0.0196  0.0293  -0.1722 16  GLN B CB  
2587 C CG  . GLN B 36  ? 0.4004 0.7738 0.5316 0.0532  0.0662  -0.1777 16  GLN B CG  
2588 C CD  . GLN B 36  ? 0.4660 0.8083 0.5770 0.0612  0.1128  -0.1883 16  GLN B CD  
2589 O OE1 . GLN B 36  ? 0.4791 0.8232 0.5859 0.0660  0.1432  -0.1887 16  GLN B OE1 
2590 N NE2 . GLN B 36  ? 0.4525 0.8173 0.5865 0.0467  0.0733  -0.1941 16  GLN B NE2 
2615 N N   . ALA B 38  ? 0.2715 0.5967 0.2836 0.0081  0.0248  0.0108  18  ALA B N   
2616 C CA  . ALA B 38  ? 0.2758 0.5660 0.3400 0.0141  0.0088  -0.0119 18  ALA B CA  
2617 C C   . ALA B 38  ? 0.2650 0.5230 0.3089 0.0063  -0.0007 -0.0359 18  ALA B C   
2618 O O   . ALA B 38  ? 0.2824 0.5185 0.3054 -0.0195 0.0079  -0.0325 18  ALA B O   
2619 C CB  . ALA B 38  ? 0.2691 0.5791 0.3706 -0.0057 0.0227  -0.0324 18  ALA B CB  
2625 N N   . ALA B 39  ? 0.2229 0.4822 0.3016 0.0067  0.0182  -0.0403 19  ALA B N   
2626 C CA  . ALA B 39  ? 0.2337 0.4818 0.3076 0.0072  0.0444  -0.0367 19  ALA B CA  
2627 C C   . ALA B 39  ? 0.2087 0.4789 0.2754 -0.0271 0.0235  -0.0256 19  ALA B C   
2628 O O   . ALA B 39  ? 0.2721 0.4465 0.2565 -0.0395 0.0322  -0.0224 19  ALA B O   
2629 C CB  . ALA B 39  ? 0.2913 0.4645 0.3671 0.0013  0.0485  -0.0644 19  ALA B CB  
2635 N N   . ARG B 40  ? 0.2057 0.5031 0.2658 -0.0277 0.0300  -0.0137 20  ARG B N   
2636 C CA  . ARG B 40  ? 0.1933 0.4941 0.2676 -0.0172 0.0185  -0.0096 20  ARG B CA  
2637 C C   . ARG B 40  ? 0.2182 0.4626 0.2714 -0.0035 0.0365  0.0049  20  ARG B C   
2638 O O   . ARG B 40  ? 0.2372 0.4549 0.2745 -0.0357 0.0285  -0.0107 20  ARG B O   
2639 C CB  . ARG B 40  ? 0.2211 0.5072 0.2851 -0.0058 0.0367  0.0172  20  ARG B CB  
2640 C CG  . ARG B 40  ? 0.2356 0.4939 0.2825 0.0142  0.0266  0.0496  20  ARG B CG  
2641 C CD  . ARG B 40  ? 0.2448 0.4943 0.2923 0.0139  0.0332  0.0670  20  ARG B CD  
2642 N NE  . ARG B 40  ? 0.2571 0.5008 0.3068 0.0177  0.0277  0.0195  20  ARG B NE  
2643 C CZ  . ARG B 40  ? 0.2496 0.5264 0.2991 0.0223  0.0166  0.0217  20  ARG B CZ  
2644 N NH1 . ARG B 40  ? 0.2368 0.5512 0.3210 0.0207  -0.0030 0.0042  20  ARG B NH1 
2645 N NH2 . ARG B 40  ? 0.2222 0.5339 0.3272 0.0094  0.0158  -0.0144 20  ARG B NH2 
2659 N N   . GLN B 41  ? 0.2460 0.4647 0.2663 0.0072  0.0289  0.0360  21  GLN B N   
2660 C CA  . GLN B 41  ? 0.2766 0.4255 0.2962 0.0226  0.0427  0.0358  21  GLN B CA  
2661 C C   . GLN B 41  ? 0.2458 0.4257 0.3017 0.0140  0.0443  0.0675  21  GLN B C   
2662 O O   . GLN B 41  ? 0.2653 0.4084 0.3075 0.0138  0.0492  0.0693  21  GLN B O   
2676 N N   . HIS B 42  ? 0.2130 0.4325 0.2758 0.0198  0.0287  0.0677  22  HIS B N   
2677 C CA  . HIS B 42  ? 0.2016 0.4094 0.2974 0.0125  0.0244  0.0684  22  HIS B CA  
2678 C C   . HIS B 42  ? 0.2171 0.3767 0.2756 0.0216  0.0260  0.0379  22  HIS B C   
2679 O O   . HIS B 42  ? 0.2023 0.3648 0.2811 0.0158  0.0279  0.0259  22  HIS B O   
2680 C CB  . HIS B 42  ? 0.2028 0.4237 0.2815 -0.0121 0.0180  0.0433  22  HIS B CB  
2681 C CG  . HIS B 42  ? 0.2082 0.4090 0.2833 0.0058  0.0485  0.0339  22  HIS B CG  
2682 N ND1 . HIS B 42  ? 0.2585 0.4129 0.3281 0.0167  0.0736  0.0377  22  HIS B ND1 
2683 C CD2 . HIS B 42  ? 0.2182 0.3898 0.2780 -0.0018 0.0158  0.0313  22  HIS B CD2 
2684 C CE1 . HIS B 42  ? 0.2666 0.4120 0.2942 0.0233  0.0565  0.0520  22  HIS B CE1 
2685 N NE2 . HIS B 42  ? 0.2453 0.3962 0.2773 0.0045  0.0383  0.0350  22  HIS B NE2 
2693 N N   . ASN B 43  ? 0.1981 0.3532 0.2668 0.0105  0.0135  0.0324  23  ASN B N   
2694 C CA  . ASN B 43  ? 0.1934 0.3483 0.2620 0.0110  0.0194  0.0271  23  ASN B CA  
2695 C C   . ASN B 43  ? 0.2062 0.3384 0.2483 0.0032  0.0449  0.0164  23  ASN B C   
2696 O O   . ASN B 43  ? 0.2197 0.3199 0.2508 0.0178  0.0314  0.0003  23  ASN B O   
2697 C CB  . ASN B 43  ? 0.1876 0.3591 0.2687 0.0010  0.0284  0.0212  23  ASN B CB  
2698 C CG  . ASN B 43  ? 0.2062 0.3686 0.2522 -0.0091 0.0339  -0.0042 23  ASN B CG  
2699 O OD1 . ASN B 43  ? 0.2235 0.3720 0.2789 -0.0138 0.0374  0.0011  23  ASN B OD1 
2700 N ND2 . ASN B 43  ? 0.2228 0.3740 0.2795 -0.0057 0.0221  -0.0385 23  ASN B ND2 
2707 N N   . ARG B 44  ? 0.2025 0.3648 0.2593 -0.0018 0.0301  0.0270  24  ARG B N   
2708 C CA  . ARG B 44  ? 0.2205 0.3743 0.2467 0.0119  0.0205  0.0399  24  ARG B CA  
2709 C C   . ARG B 44  ? 0.2215 0.3319 0.2606 0.0010  0.0103  0.0577  24  ARG B C   
2710 O O   . ARG B 44  ? 0.2207 0.3368 0.2701 0.0058  0.0315  0.0607  24  ARG B O   
2711 C CB  . ARG B 44  ? 0.2768 0.4311 0.2545 0.0062  0.0328  0.0516  24  ARG B CB  
2712 C CG  . ARG B 44  ? 0.4379 0.4582 0.2676 -0.0417 0.0797  0.0646  24  ARG B CG  
2713 C CD  . ARG B 44  ? 0.5189 0.5088 0.3885 -0.0770 0.0317  0.0885  24  ARG B CD  
2714 N NE  . ARG B 44  ? 0.5817 0.5635 0.5377 -0.0534 0.0441  0.1282  24  ARG B NE  
2715 C CZ  . ARG B 44  ? 0.5140 0.5848 0.6022 0.0170  -0.0254 0.1365  24  ARG B CZ  
2716 N NH1 . ARG B 44  ? 0.5754 0.6075 0.6504 -0.0132 0.0039  0.1142  24  ARG B NH1 
2717 N NH2 . ARG B 44  ? 0.4839 0.5767 0.6372 0.0648  -0.0096 0.1395  24  ARG B NH2 
2744 N N   . ILE B 46  ? 0.2028 0.2843 0.2843 0.0224  0.0561  0.0421  26  ILE B N   
2745 C CA  . ILE B 46  ? 0.2233 0.2972 0.2561 0.0393  0.0603  0.0351  26  ILE B CA  
2746 C C   . ILE B 46  ? 0.1972 0.2715 0.2565 0.0243  0.0554  0.0204  26  ILE B C   
2747 O O   . ILE B 46  ? 0.2231 0.2809 0.2379 0.0133  0.0562  0.0099  26  ILE B O   
2748 C CB  . ILE B 46  ? 0.2150 0.3431 0.2493 0.0164  0.0445  0.0391  26  ILE B CB  
2749 C CG1 . ILE B 46  ? 0.2081 0.4181 0.2879 -0.0028 0.0344  0.0466  26  ILE B CG1 
2750 C CG2 . ILE B 46  ? 0.2393 0.3218 0.2664 -0.0091 0.0356  0.0396  26  ILE B CG2 
2751 C CD1 . ILE B 46  ? 0.2435 0.4832 0.3677 -0.0185 0.0720  0.0069  26  ILE B CD1 
2763 N N   . VAL B 47  ? 0.1831 0.2510 0.2579 0.0232  0.0348  0.0073  27  VAL B N   
2764 C CA  . VAL B 47  ? 0.1974 0.2382 0.2472 0.0257  0.0405  0.0252  27  VAL B CA  
2765 C C   . VAL B 47  ? 0.2103 0.2467 0.2474 0.0232  0.0541  0.0236  27  VAL B C   
2766 O O   . VAL B 47  ? 0.2083 0.2522 0.2543 0.0147  0.0489  0.0120  27  VAL B O   
2767 C CB  . VAL B 47  ? 0.1943 0.2632 0.2390 0.0243  0.0314  0.0093  27  VAL B CB  
2768 C CG1 . VAL B 47  ? 0.1872 0.2925 0.2592 0.0029  0.0359  -0.0035 27  VAL B CG1 
2769 C CG2 . VAL B 47  ? 0.1990 0.2867 0.2424 0.0115  0.0247  0.0076  27  VAL B CG2 
2779 N N   . GLU B 48  ? 0.2211 0.2724 0.2370 0.0288  0.0440  0.0303  28  GLU B N   
2780 C CA  . GLU B 48  ? 0.2516 0.2980 0.2502 0.0394  0.0337  0.0184  28  GLU B CA  
2781 C C   . GLU B 48  ? 0.2392 0.2875 0.2666 0.0474  0.0320  0.0168  28  GLU B C   
2782 O O   . GLU B 48  ? 0.2535 0.2569 0.2739 0.0336  0.0481  0.0316  28  GLU B O   
2783 C CB  . GLU B 48  ? 0.3369 0.3529 0.2627 0.0758  0.0234  0.0638  28  GLU B CB  
2784 C CG  . GLU B 48  ? 0.4178 0.4072 0.3296 0.0476  0.0534  0.0787  28  GLU B CG  
2785 C CD  . GLU B 48  ? 0.5333 0.4632 0.3935 0.0463  0.0577  0.1096  28  GLU B CD  
2786 O OE1 . GLU B 48  ? 0.5888 0.4853 0.4342 0.0505  0.0119  0.1329  28  GLU B OE1 
2787 O OE2 . GLU B 48  ? 0.6172 0.4887 0.4302 0.0487  0.0617  0.1026  28  GLU B OE2 
2794 N N   . GLN B 49  ? 0.2212 0.2663 0.2576 0.0477  0.0419  0.0111  29  GLN B N   
2795 C CA  . GLN B 49  ? 0.2116 0.2870 0.2725 0.0617  0.0348  0.0144  29  GLN B CA  
2796 C C   . GLN B 49  ? 0.2284 0.2709 0.2555 0.0471  0.0754  0.0226  29  GLN B C   
2797 O O   . GLN B 49  ? 0.2700 0.2776 0.2487 0.0597  0.0579  0.0025  29  GLN B O   
2798 C CB  . GLN B 49  ? 0.2612 0.3275 0.2669 0.0706  0.0427  0.0074  29  GLN B CB  
2799 C CG  . GLN B 49  ? 0.2862 0.3805 0.3130 0.0649  0.0690  0.0179  29  GLN B CG  
2800 C CD  . GLN B 49  ? 0.2407 0.4171 0.3350 0.0261  0.0633  0.0469  29  GLN B CD  
2801 O OE1 . GLN B 49  ? 0.2653 0.4520 0.4207 0.0336  0.0632  0.0559  29  GLN B OE1 
2802 N NE2 . GLN B 49  ? 0.2751 0.4157 0.3422 0.0074  0.0559  0.0410  29  GLN B NE2 
2811 N N   . TYR B 50  ? 0.1976 0.2455 0.2597 0.0270  0.0451  0.0264  30  TYR B N   
2812 C CA  . TYR B 50  ? 0.1936 0.2387 0.2400 0.0282  0.0548  0.0202  30  TYR B CA  
2813 C C   . TYR B 50  ? 0.1996 0.2262 0.2592 0.0203  0.0493  0.0227  30  TYR B C   
2814 O O   . TYR B 50  ? 0.2364 0.2151 0.2403 0.0229  0.0430  0.0112  30  TYR B O   
2815 C CB  . TYR B 50  ? 0.2145 0.2174 0.2618 0.0310  0.0657  0.0109  30  TYR B CB  
2816 C CG  . TYR B 50  ? 0.2041 0.1992 0.2598 0.0163  0.0616  0.0158  30  TYR B CG  
2817 C CD1 . TYR B 50  ? 0.2148 0.2040 0.2527 0.0237  0.0636  0.0215  30  TYR B CD1 
2818 C CD2 . TYR B 50  ? 0.2159 0.2150 0.2787 0.0090  0.0781  0.0029  30  TYR B CD2 
2819 C CE1 . TYR B 50  ? 0.2239 0.2186 0.2562 0.0093  0.0670  0.0265  30  TYR B CE1 
2820 C CE2 . TYR B 50  ? 0.2067 0.2299 0.2836 0.0281  0.0885  0.0229  30  TYR B CE2 
2821 C CZ  . TYR B 50  ? 0.2197 0.2408 0.2664 0.0312  0.0692  0.0345  30  TYR B CZ  
2822 O OH  . TYR B 50  ? 0.2475 0.2839 0.2729 0.0325  0.0591  0.0385  30  TYR B OH  
2832 N N   . MET B 51  ? 0.2081 0.2234 0.2586 0.0263  0.0502  0.0300  31  MET B N   
2833 C CA  . MET B 51  ? 0.2106 0.2146 0.2651 0.0293  0.0545  0.0213  31  MET B CA  
2834 C C   . MET B 51  ? 0.2437 0.2066 0.2680 0.0350  0.0398  0.0216  31  MET B C   
2835 O O   . MET B 51  ? 0.2652 0.1995 0.2974 0.0332  0.0500  0.0208  31  MET B O   
2836 C CB  . MET B 51  ? 0.2257 0.2521 0.2563 0.0277  0.0630  0.0096  31  MET B CB  
2837 C CG  . MET B 51  ? 0.2183 0.2660 0.2424 0.0189  0.0610  0.0115  31  MET B CG  
2838 S SD  . MET B 51  ? 0.2244 0.2219 0.2589 0.0095  0.0543  0.0047  31  MET B SD  
2839 C CE  . MET B 51  ? 0.2303 0.2482 0.2644 0.0068  0.0507  -0.0032 31  MET B CE  
2849 N N   A HIS B 52  ? 0.2336 0.1870 0.2890 0.0423  0.0464  0.0367  32  HIS B N   
2850 N N   B HIS B 52  ? 0.2454 0.1842 0.2793 0.0380  0.0474  0.0280  32  HIS B N   
2851 C CA  A HIS B 52  ? 0.2752 0.2051 0.2972 0.0515  0.0259  0.0391  32  HIS B CA  
2852 C CA  B HIS B 52  ? 0.2842 0.1848 0.2790 0.0359  0.0435  0.0203  32  HIS B CA  
2853 C C   A HIS B 52  ? 0.2577 0.2077 0.2763 0.0322  0.0266  0.0311  32  HIS B C   
2854 C C   B HIS B 52  ? 0.2827 0.2007 0.2744 0.0239  0.0669  0.0145  32  HIS B C   
2855 O O   A HIS B 52  ? 0.2922 0.2168 0.2910 0.0503  -0.0014 0.0291  32  HIS B O   
2856 O O   B HIS B 52  ? 0.3450 0.2085 0.2850 0.0161  0.0919  -0.0125 32  HIS B O   
2857 C CB  A HIS B 52  ? 0.3396 0.2618 0.3396 0.1036  0.0469  0.0701  32  HIS B CB  
2858 C CB  B HIS B 52  ? 0.3422 0.1992 0.3006 0.0569  0.0746  0.0214  32  HIS B CB  
2859 C CG  A HIS B 52  ? 0.3910 0.3084 0.3660 0.1311  0.0801  0.0848  32  HIS B CG  
2860 C CG  B HIS B 52  ? 0.3934 0.1918 0.3119 0.0427  0.1262  0.0076  32  HIS B CG  
2861 N ND1 A HIS B 52  ? 0.4348 0.3579 0.3562 0.1197  0.0785  0.0835  32  HIS B ND1 
2862 N ND1 B HIS B 52  ? 0.3851 0.2024 0.3015 0.0277  0.1255  0.0087  32  HIS B ND1 
2863 C CD2 A HIS B 52  ? 0.3926 0.3129 0.3981 0.1637  0.0790  0.0980  32  HIS B CD2 
2864 C CD2 B HIS B 52  ? 0.4480 0.1881 0.3494 0.0004  0.1211  -0.0102 32  HIS B CD2 
2865 C CE1 A HIS B 52  ? 0.4221 0.3727 0.3460 0.1032  0.0579  0.1255  32  HIS B CE1 
2866 C CE1 B HIS B 52  ? 0.4024 0.1546 0.3402 0.0252  0.0911  0.0302  32  HIS B CE1 
2867 N NE2 A HIS B 52  ? 0.4307 0.3470 0.3832 0.1154  0.0721  0.1382  32  HIS B NE2 
2868 N NE2 B HIS B 52  ? 0.4446 0.1810 0.3793 -0.0126 0.1086  0.0144  32  HIS B NE2 
2883 N N   . THR B 53  ? 0.2456 0.2100 0.2636 0.0296  0.0503  0.0235  33  THR B N   
2884 C CA  . THR B 53  ? 0.2427 0.2282 0.2697 0.0153  0.0495  0.0176  33  THR B CA  
2885 C C   . THR B 53  ? 0.2670 0.2120 0.2901 0.0207  0.0595  0.0085  33  THR B C   
2886 O O   . THR B 53  ? 0.2913 0.2551 0.2913 0.0531  0.0486  -0.0159 33  THR B O   
2887 C CB  . THR B 53  ? 0.2480 0.2611 0.2643 0.0248  0.0423  0.0282  33  THR B CB  
2888 O OG1 . THR B 53  ? 0.2496 0.2718 0.2669 0.0246  0.0452  0.0197  33  THR B OG1 
2889 C CG2 . THR B 53  ? 0.3027 0.2601 0.2578 0.0230  0.0588  0.0352  33  THR B CG2 
2898 N N   . ARG B 54  ? 0.2753 0.2095 0.2775 0.0266  0.0461  0.0063  34  ARG B N   
2899 C CA  . ARG B 54  ? 0.2870 0.2341 0.2829 0.0063  0.0554  -0.0054 34  ARG B CA  
2900 C C   . ARG B 54  ? 0.2675 0.2331 0.2836 0.0290  0.0575  -0.0078 34  ARG B C   
2901 O O   . ARG B 54  ? 0.2833 0.2532 0.3399 0.0222  0.0727  -0.0318 34  ARG B O   
2902 C CB  . ARG B 54  ? 0.3676 0.2915 0.3229 -0.0250 0.0745  -0.0032 34  ARG B CB  
2903 C CG  . ARG B 54  ? 0.3789 0.3503 0.3886 -0.0539 0.0847  -0.0091 34  ARG B CG  
2904 C CD  . ARG B 54  ? 0.4504 0.3923 0.4024 -0.1022 0.0094  0.0440  34  ARG B CD  
2905 N NE  . ARG B 54  ? 0.4100 0.4163 0.3459 -0.1156 0.0005  0.0208  34  ARG B NE  
2906 C CZ  . ARG B 54  ? 0.3427 0.3790 0.3239 -0.0644 0.0332  -0.0325 34  ARG B CZ  
2907 N NH1 . ARG B 54  ? 0.3404 0.3261 0.3752 -0.0257 0.0282  -0.0079 34  ARG B NH1 
2908 N NH2 . ARG B 54  ? 0.3837 0.3783 0.3621 -0.0063 0.0122  0.0112  34  ARG B NH2 
2922 N N   . GLY B 55  ? 0.2983 0.2426 0.2928 0.0115  0.0731  -0.0212 35  GLY B N   
2923 C CA  . GLY B 55  ? 0.3200 0.2784 0.3000 0.0241  0.1019  -0.0412 35  GLY B CA  
2924 C C   . GLY B 55  ? 0.3488 0.2871 0.3095 0.0283  0.1292  -0.0470 35  GLY B C   
2925 O O   . GLY B 55  ? 0.3587 0.2771 0.2837 0.0383  0.1073  -0.0279 35  GLY B O   
2929 N N   . GLU B 56  ? 0.3886 0.3214 0.3335 0.0135  0.1606  -0.0528 36  GLU B N   
2930 C CA  . GLU B 56  ? 0.3708 0.3431 0.3346 0.0194  0.1496  -0.0509 36  GLU B CA  
2931 C C   . GLU B 56  ? 0.3288 0.3268 0.3288 0.0365  0.1344  -0.0147 36  GLU B C   
2932 O O   . GLU B 56  ? 0.2996 0.3335 0.3362 0.0247  0.1218  -0.0030 36  GLU B O   
2933 C CB  . GLU B 56  ? 0.4536 0.4188 0.4562 0.0016  0.1661  -0.0796 36  GLU B CB  
2934 C CG  . GLU B 56  ? 0.5309 0.5145 0.5466 -0.0233 0.1302  -0.0462 36  GLU B CG  
2935 C CD  . GLU B 56  ? 0.6181 0.5829 0.5945 -0.0538 0.1086  -0.0322 36  GLU B CD  
2936 O OE1 . GLU B 56  ? 0.6504 0.5996 0.5996 -0.0713 0.1235  -0.0139 36  GLU B OE1 
2937 O OE2 . GLU B 56  ? 0.6640 0.6169 0.6159 -0.0636 0.0757  -0.0474 36  GLU B OE2 
2944 N N   . ALA B 57  ? 0.3206 0.3103 0.3403 0.0532  0.1163  -0.0190 37  ALA B N   
2945 C CA  . ALA B 57  ? 0.2713 0.2865 0.3327 0.0549  0.0908  0.0272  37  ALA B CA  
2946 C C   . ALA B 57  ? 0.2394 0.2679 0.2811 0.0363  0.0724  0.0180  37  ALA B C   
2947 O O   . ALA B 57  ? 0.2622 0.2704 0.2969 0.0071  0.0638  0.0182  37  ALA B O   
2948 C CB  . ALA B 57  ? 0.2677 0.2942 0.3540 0.0434  0.0536  0.0277  37  ALA B CB  
2954 N N   . ARG B 58  ? 0.2358 0.2713 0.2658 0.0340  0.0685  0.0079  38  ARG B N   
2955 C CA  . ARG B 58  ? 0.2477 0.2687 0.2474 0.0318  0.0625  0.0028  38  ARG B CA  
2956 C C   . ARG B 58  ? 0.2403 0.3015 0.2402 0.0209  0.0737  0.0060  38  ARG B C   
2957 O O   . ARG B 58  ? 0.2473 0.3071 0.2594 0.0356  0.0578  0.0149  38  ARG B O   
2958 C CB  . ARG B 58  ? 0.2602 0.2733 0.2608 0.0159  0.0411  0.0160  38  ARG B CB  
2959 C CG  . ARG B 58  ? 0.2816 0.2977 0.2751 0.0047  0.0455  0.0367  38  ARG B CG  
2960 C CD  . ARG B 58  ? 0.3069 0.3138 0.3479 0.0001  0.0209  0.0628  38  ARG B CD  
2961 N NE  . ARG B 58  ? 0.3012 0.3379 0.3371 -0.0324 0.0075  0.0644  38  ARG B NE  
2962 C CZ  . ARG B 58  ? 0.3002 0.3289 0.3225 -0.0117 0.0084  0.0484  38  ARG B CZ  
2963 N NH1 . ARG B 58  ? 0.3208 0.3315 0.3227 0.0105  0.0193  0.0637  38  ARG B NH1 
2964 N NH2 . ARG B 58  ? 0.3013 0.3485 0.3443 0.0204  0.0047  -0.0240 38  ARG B NH2 
2978 N N   . LEU B 59  ? 0.2788 0.3058 0.2416 -0.0003 0.0755  0.0234  39  LEU B N   
2979 C CA  . LEU B 59  ? 0.3155 0.3157 0.2500 -0.0140 0.0996  0.0191  39  LEU B CA  
2980 C C   . LEU B 59  ? 0.3058 0.3180 0.2737 -0.0064 0.1126  0.0140  39  LEU B C   
2981 O O   . LEU B 59  ? 0.3050 0.3291 0.2800 -0.0130 0.0900  0.0182  39  LEU B O   
2982 C CB  . LEU B 59  ? 0.3948 0.3369 0.2825 -0.0144 0.1443  -0.0206 39  LEU B CB  
2983 C CG  . LEU B 59  ? 0.4966 0.3657 0.3086 -0.0096 0.1097  -0.0333 39  LEU B CG  
2984 C CD1 . LEU B 59  ? 0.5381 0.3915 0.3489 -0.0211 0.1131  -0.1191 39  LEU B CD1 
2985 C CD2 . LEU B 59  ? 0.5269 0.3840 0.3368 -0.0308 0.0667  -0.0145 39  LEU B CD2 
2997 N N   . LYS B 60  ? 0.2648 0.3152 0.2852 0.0163  0.0879  0.0103  40  LYS B N   
2998 C CA  . LYS B 60  ? 0.2660 0.3247 0.2895 0.0279  0.0726  0.0133  40  LYS B CA  
2999 C C   . LYS B 60  ? 0.2641 0.2947 0.2739 0.0225  0.0792  0.0331  40  LYS B C   
3000 O O   . LYS B 60  ? 0.2309 0.3127 0.3011 0.0332  0.0563  0.0163  40  LYS B O   
3019 N N   . ARG B 61  ? 0.2287 0.2787 0.2721 0.0269  0.0717  0.0251  41  ARG B N   
3020 C CA  . ARG B 61  ? 0.2151 0.2541 0.2758 0.0165  0.0734  0.0260  41  ARG B CA  
3021 C C   . ARG B 61  ? 0.2243 0.2704 0.2654 0.0149  0.0751  0.0163  41  ARG B C   
3022 O O   . ARG B 61  ? 0.2206 0.2773 0.2461 0.0026  0.0649  0.0120  41  ARG B O   
3023 C CB  . ARG B 61  ? 0.2457 0.2478 0.2839 0.0106  0.0793  0.0000  41  ARG B CB  
3024 C CG  . ARG B 61  ? 0.2585 0.2466 0.2764 0.0048  0.0961  0.0170  41  ARG B CG  
3025 C CD  . ARG B 61  ? 0.2522 0.2651 0.2690 0.0100  0.0694  0.0388  41  ARG B CD  
3026 N NE  . ARG B 61  ? 0.2442 0.2939 0.2883 -0.0169 0.0521  0.0340  41  ARG B NE  
3027 C CZ  . ARG B 61  ? 0.2711 0.3312 0.2824 -0.0176 0.0380  0.0386  41  ARG B CZ  
3028 N NH1 . ARG B 61  ? 0.2950 0.3485 0.3251 -0.0370 0.0561  0.0399  41  ARG B NH1 
3029 N NH2 . ARG B 61  ? 0.3043 0.3714 0.3173 0.0323  0.0318  0.0395  41  ARG B NH2 
3043 N N   . HIS B 62  ? 0.2169 0.2760 0.2744 0.0081  0.0589  0.0414  42  HIS B N   
3044 C CA  . HIS B 62  ? 0.2220 0.2574 0.2599 -0.0001 0.0502  0.0518  42  HIS B CA  
3045 C C   . HIS B 62  ? 0.2262 0.2778 0.2646 -0.0031 0.0678  0.0268  42  HIS B C   
3046 O O   . HIS B 62  ? 0.2393 0.2690 0.2607 -0.0041 0.0700  0.0270  42  HIS B O   
3047 C CB  . HIS B 62  ? 0.2603 0.2615 0.2682 -0.0014 0.0600  0.0306  42  HIS B CB  
3048 C CG  . HIS B 62  ? 0.2634 0.2856 0.2424 -0.0015 0.0548  0.0355  42  HIS B CG  
3049 N ND1 . HIS B 62  ? 0.2788 0.3082 0.2555 0.0096  0.0797  0.0192  42  HIS B ND1 
3050 C CD2 . HIS B 62  ? 0.3212 0.3027 0.2834 -0.0514 0.0911  0.0426  42  HIS B CD2 
3051 C CE1 . HIS B 62  ? 0.3169 0.3157 0.2604 0.0082  0.1024  0.0330  42  HIS B CE1 
3052 N NE2 . HIS B 62  ? 0.3366 0.3094 0.3054 -0.0214 0.0928  0.0246  42  HIS B NE2 
3060 N N   . LEU B 63  ? 0.2234 0.3015 0.2665 -0.0106 0.0779  0.0253  43  LEU B N   
3061 C CA  . LEU B 63  ? 0.1898 0.3424 0.2685 0.0039  0.0562  0.0045  43  LEU B CA  
3062 C C   . LEU B 63  ? 0.2063 0.3377 0.2439 0.0190  0.0493  0.0089  43  LEU B C   
3063 O O   . LEU B 63  ? 0.2108 0.3793 0.2518 0.0011  0.0376  -0.0053 43  LEU B O   
3064 C CB  . LEU B 63  ? 0.2223 0.4000 0.2738 0.0140  0.0723  0.0043  43  LEU B CB  
3065 C CG  . LEU B 63  ? 0.2617 0.4479 0.2956 0.0077  0.1184  -0.0088 43  LEU B CG  
3066 C CD1 . LEU B 63  ? 0.2747 0.4767 0.3675 0.0478  0.1292  -0.0219 43  LEU B CD1 
3067 C CD2 . LEU B 63  ? 0.3009 0.4755 0.2892 -0.0361 0.0859  -0.0059 43  LEU B CD2 
3079 N N   . LEU B 64  ? 0.2029 0.3028 0.2338 0.0036  0.0402  0.0151  44  LEU B N   
3080 C CA  . LEU B 64  ? 0.2208 0.2961 0.2450 0.0035  0.0648  0.0129  44  LEU B CA  
3081 C C   . LEU B 64  ? 0.1855 0.2861 0.2406 -0.0047 0.0461  0.0131  44  LEU B C   
3082 O O   . LEU B 64  ? 0.2257 0.2874 0.2450 0.0010  0.0522  0.0055  44  LEU B O   
3083 C CB  . LEU B 64  ? 0.2335 0.2796 0.2455 -0.0018 0.0656  0.0178  44  LEU B CB  
3084 C CG  . LEU B 64  ? 0.2333 0.2860 0.2615 0.0233  0.0348  0.0113  44  LEU B CG  
3085 C CD1 . LEU B 64  ? 0.2692 0.2817 0.2915 -0.0005 0.0771  0.0405  44  LEU B CD1 
3086 C CD2 . LEU B 64  ? 0.2818 0.2998 0.2667 0.0348  0.0430  0.0071  44  LEU B CD2 
3098 N N   . PHE B 65  ? 0.2028 0.2592 0.2430 0.0031  0.0535  0.0367  45  PHE B N   
3099 C CA  . PHE B 65  ? 0.2064 0.2505 0.2531 -0.0057 0.0636  0.0291  45  PHE B CA  
3100 C C   . PHE B 65  ? 0.1936 0.2998 0.2584 -0.0137 0.0451  0.0283  45  PHE B C   
3101 O O   . PHE B 65  ? 0.1889 0.3506 0.2963 -0.0262 0.0600  0.0294  45  PHE B O   
3102 C CB  . PHE B 65  ? 0.2129 0.2464 0.2655 -0.0109 0.0532  0.0315  45  PHE B CB  
3103 C CG  . PHE B 65  ? 0.2192 0.2349 0.2416 -0.0238 0.0529  0.0200  45  PHE B CG  
3104 C CD1 . PHE B 65  ? 0.2074 0.2479 0.2855 -0.0243 0.0648  0.0152  45  PHE B CD1 
3105 C CD2 . PHE B 65  ? 0.2263 0.2329 0.2495 -0.0128 0.0704  0.0260  45  PHE B CD2 
3106 C CE1 . PHE B 65  ? 0.2215 0.2566 0.3186 -0.0230 0.0888  0.0016  45  PHE B CE1 
3107 C CE2 . PHE B 65  ? 0.2399 0.2297 0.2841 -0.0173 0.0838  0.0293  45  PHE B CE2 
3108 C CZ  . PHE B 65  ? 0.2194 0.2315 0.3016 -0.0155 0.0812  0.0172  45  PHE B CZ  
3118 N N   . THR B 66  ? 0.2143 0.2871 0.2844 -0.0197 0.0493  0.0260  46  THR B N   
3119 C CA  . THR B 66  ? 0.2065 0.2980 0.3457 -0.0453 0.0378  0.0507  46  THR B CA  
3120 C C   . THR B 66  ? 0.2038 0.3206 0.3273 -0.0239 0.0336  0.0833  46  THR B C   
3121 O O   . THR B 66  ? 0.2074 0.3167 0.3051 -0.0275 0.0305  0.0659  46  THR B O   
3122 C CB  . THR B 66  ? 0.2323 0.3037 0.3520 -0.0408 0.0183  0.0120  46  THR B CB  
3123 O OG1 . THR B 66  ? 0.2430 0.3026 0.3539 -0.0179 0.0308  0.0282  46  THR B OG1 
3124 C CG2 . THR B 66  ? 0.2692 0.3021 0.3614 -0.0186 0.0092  -0.0145 46  THR B CG2 
3132 N N   . GLU B 67  ? 0.2105 0.3656 0.3683 -0.0596 0.0442  0.0991  47  GLU B N   
3133 C CA  . GLU B 67  ? 0.2265 0.4035 0.3946 -0.0708 0.0647  0.1307  47  GLU B CA  
3134 C C   . GLU B 67  ? 0.2316 0.3862 0.3835 -0.0482 0.0652  0.1280  47  GLU B C   
3135 O O   . GLU B 67  ? 0.2669 0.4054 0.3987 -0.0559 0.0677  0.1356  47  GLU B O   
3136 C CB  . GLU B 67  ? 0.2675 0.4568 0.4458 -0.0832 0.0523  0.1647  47  GLU B CB  
3137 C CG  . GLU B 67  ? 0.3250 0.4875 0.4993 -0.1137 0.0395  0.1696  47  GLU B CG  
3142 N N   . ASP B 68  ? 0.2302 0.3566 0.4173 -0.0649 0.0541  0.1279  48  ASP B N   
3143 C CA  . ASP B 68  ? 0.2438 0.3265 0.4714 -0.0598 0.0472  0.0878  48  ASP B CA  
3144 C C   . ASP B 68  ? 0.2295 0.2928 0.4241 -0.0526 0.0708  0.1003  48  ASP B C   
3145 O O   . ASP B 68  ? 0.2498 0.2961 0.4097 -0.0385 0.0518  0.0773  48  ASP B O   
3146 C CB  . ASP B 68  ? 0.3026 0.3185 0.5772 -0.0872 0.0400  0.0752  48  ASP B CB  
3147 C CG  . ASP B 68  ? 0.3841 0.3574 0.6730 -0.0699 0.0232  0.0269  48  ASP B CG  
3148 O OD1 . ASP B 68  ? 0.3751 0.3814 0.6753 -0.0671 0.0730  0.0478  48  ASP B OD1 
3149 O OD2 . ASP B 68  ? 0.4710 0.3894 0.7388 -0.0313 0.0197  0.0145  48  ASP B OD2 
3154 N N   . GLY B 69  ? 0.2208 0.2726 0.3718 -0.0521 0.0423  0.0872  49  GLY B N   
3155 C CA  . GLY B 69  ? 0.2054 0.2955 0.3365 -0.0575 0.0650  0.0819  49  GLY B CA  
3156 C C   . GLY B 69  ? 0.2198 0.2858 0.3044 -0.0493 0.0516  0.0946  49  GLY B C   
3157 O O   . GLY B 69  ? 0.2245 0.3499 0.2958 -0.0366 0.0538  0.0816  49  GLY B O   
3161 N N   . VAL B 70  ? 0.2112 0.2324 0.2930 -0.0483 0.0464  0.0534  50  VAL B N   
3162 C CA  . VAL B 70  ? 0.2167 0.2107 0.3046 -0.0289 0.0538  0.0401  50  VAL B CA  
3163 C C   . VAL B 70  ? 0.2004 0.2181 0.2698 -0.0228 0.0669  0.0264  50  VAL B C   
3164 O O   . VAL B 70  ? 0.2220 0.2570 0.2473 -0.0281 0.0650  0.0368  50  VAL B O   
3165 C CB  . VAL B 70  ? 0.2456 0.2023 0.3515 -0.0120 0.0417  0.0355  50  VAL B CB  
3166 C CG1 . VAL B 70  ? 0.2170 0.2347 0.4265 0.0201  0.0043  0.0260  50  VAL B CG1 
3167 C CG2 . VAL B 70  ? 0.3061 0.2032 0.3967 -0.0287 0.0326  0.0339  50  VAL B CG2 
3177 N N   . GLY B 71  ? 0.2222 0.2093 0.2527 -0.0251 0.0544  0.0323  51  GLY B N   
3178 C CA  . GLY B 71  ? 0.2151 0.2045 0.2593 -0.0361 0.0431  0.0473  51  GLY B CA  
3179 C C   . GLY B 71  ? 0.2178 0.2553 0.2449 -0.0347 0.0354  0.0525  51  GLY B C   
3180 O O   . GLY B 71  ? 0.2793 0.3428 0.3094 -0.0790 -0.0110 0.1315  51  GLY B O   
3184 N N   . GLY B 72  ? 0.1984 0.2449 0.2466 -0.0292 0.0432  0.0530  52  GLY B N   
3185 C CA  . GLY B 72  ? 0.1876 0.2523 0.2691 -0.0185 0.0285  0.0299  52  GLY B CA  
3186 C C   . GLY B 72  ? 0.2122 0.2202 0.2301 -0.0197 0.0396  0.0236  52  GLY B C   
3187 O O   . GLY B 72  ? 0.2212 0.2480 0.2278 -0.0141 0.0426  0.0560  52  GLY B O   
3191 N N   . LEU B 73  ? 0.2076 0.2183 0.2234 -0.0206 0.0297  0.0270  53  LEU B N   
3192 C CA  . LEU B 73  ? 0.2094 0.2201 0.2430 -0.0161 0.0560  0.0125  53  LEU B CA  
3193 C C   . LEU B 73  ? 0.2157 0.2094 0.2299 -0.0273 0.0477  0.0651  53  LEU B C   
3194 O O   . LEU B 73  ? 0.2379 0.2151 0.2451 -0.0219 0.0420  0.0730  53  LEU B O   
3195 C CB  . LEU B 73  ? 0.2265 0.2200 0.2422 -0.0220 0.0458  0.0032  53  LEU B CB  
3196 C CG  . LEU B 73  ? 0.2278 0.2257 0.2326 -0.0110 0.0412  0.0303  53  LEU B CG  
3197 C CD1 . LEU B 73  ? 0.2461 0.2075 0.2262 -0.0021 0.0497  0.0276  53  LEU B CD1 
3198 C CD2 . LEU B 73  ? 0.2569 0.2636 0.2327 -0.0266 0.0202  0.0237  53  LEU B CD2 
3210 N N   . TRP B 74  ? 0.2194 0.1995 0.2256 -0.0156 0.0389  0.0500  54  TRP B N   
3211 C CA  . TRP B 74  ? 0.2357 0.1985 0.2625 -0.0209 0.0361  0.0228  54  TRP B CA  
3212 C C   . TRP B 74  ? 0.2512 0.1709 0.3171 -0.0182 0.0328  0.0255  54  TRP B C   
3213 O O   . TRP B 74  ? 0.2703 0.2001 0.4331 0.0018  0.0121  0.0025  54  TRP B O   
3214 C CB  . TRP B 74  ? 0.2450 0.2139 0.2464 -0.0242 0.0489  0.0226  54  TRP B CB  
3215 C CG  . TRP B 74  ? 0.2413 0.1818 0.2656 -0.0042 0.0334  0.0025  54  TRP B CG  
3216 C CD1 . TRP B 74  ? 0.2580 0.2165 0.3244 0.0017  0.0299  -0.0095 54  TRP B CD1 
3217 C CD2 . TRP B 74  ? 0.2454 0.1952 0.2631 -0.0161 0.0324  0.0279  54  TRP B CD2 
3218 N NE1 . TRP B 74  ? 0.2707 0.2279 0.3637 -0.0070 0.0460  0.0054  54  TRP B NE1 
3219 C CE2 . TRP B 74  ? 0.2744 0.1983 0.3348 -0.0174 0.0470  0.0191  54  TRP B CE2 
3220 C CE3 . TRP B 74  ? 0.2394 0.2239 0.2770 -0.0327 0.0492  0.0187  54  TRP B CE3 
3221 C CZ2 . TRP B 74  ? 0.3134 0.2086 0.3506 -0.0498 0.0295  0.0241  54  TRP B CZ2 
3222 C CZ3 . TRP B 74  ? 0.2674 0.2499 0.2976 -0.0319 0.0299  0.0166  54  TRP B CZ3 
3223 C CH2 . TRP B 74  ? 0.2877 0.2382 0.3164 -0.0467 0.0464  0.0071  54  TRP B CH2 
3234 N N   . THR B 75  ? 0.2094 0.1775 0.2590 -0.0084 0.0385  0.0242  55  THR B N   
3235 C CA  . THR B 75  ? 0.2050 0.1728 0.2382 -0.0107 0.0210  0.0509  55  THR B CA  
3236 C C   . THR B 75  ? 0.2210 0.1837 0.2414 -0.0102 0.0148  0.0648  55  THR B C   
3237 O O   . THR B 75  ? 0.2566 0.1865 0.2527 -0.0043 0.0177  0.0394  55  THR B O   
3238 C CB  . THR B 75  ? 0.2105 0.1794 0.2482 -0.0126 0.0259  0.0386  55  THR B CB  
3239 O OG1 . THR B 75  ? 0.2272 0.1865 0.2317 0.0028  0.0232  0.0306  55  THR B OG1 
3240 C CG2 . THR B 75  ? 0.2182 0.2287 0.2311 -0.0097 0.0268  0.0160  55  THR B CG2 
3248 N N   . THR B 76  ? 0.2405 0.2292 0.2480 0.0055  0.0302  0.0712  56  THR B N   
3249 C CA  . THR B 76  ? 0.2456 0.2681 0.2386 0.0045  0.0317  0.0749  56  THR B CA  
3250 C C   . THR B 76  ? 0.2371 0.2604 0.2213 0.0264  0.0289  0.0490  56  THR B C   
3251 O O   . THR B 76  ? 0.2458 0.2547 0.2456 0.0257  0.0515  0.0445  56  THR B O   
3252 C CB  . THR B 76  ? 0.2343 0.3179 0.3733 0.0133  0.0502  0.1568  56  THR B CB  
3253 O OG1 . THR B 76  ? 0.2663 0.3513 0.5116 -0.0068 0.0367  0.2260  56  THR B OG1 
3254 C CG2 . THR B 76  ? 0.2126 0.3477 0.3820 0.0136  0.0672  0.1478  56  THR B CG2 
3262 N N   . ASP B 77  ? 0.2355 0.2930 0.2335 0.0280  0.0272  0.0344  57  ASP B N   
3263 C CA  . ASP B 77  ? 0.2401 0.3380 0.2620 0.0114  0.0377  0.0346  57  ASP B CA  
3264 C C   . ASP B 77  ? 0.2670 0.3456 0.3028 0.0313  0.0408  0.0329  57  ASP B C   
3265 O O   . ASP B 77  ? 0.2682 0.3578 0.3403 0.0611  0.0308  0.0131  57  ASP B O   
3266 C CB  . ASP B 77  ? 0.2502 0.3682 0.2679 0.0107  0.0348  0.0165  57  ASP B CB  
3267 C CG  . ASP B 77  ? 0.2814 0.4375 0.3079 0.0201  0.0197  0.0767  57  ASP B CG  
3268 O OD1 . ASP B 77  ? 0.3821 0.4567 0.2952 0.0856  0.1079  0.0952  57  ASP B OD1 
3269 O OD2 . ASP B 77  ? 0.3278 0.4785 0.3613 0.0089  0.0371  0.0983  57  ASP B OD2 
3274 N N   . SER B 78  ? 0.2979 0.3214 0.3116 0.0597  0.0511  0.0848  58  SER B N   
3275 C CA  . SER B 78  ? 0.3312 0.3124 0.3888 0.0619  0.0484  0.0990  58  SER B CA  
3276 C C   . SER B 78  ? 0.3239 0.3144 0.4052 0.0706  0.0342  0.0598  58  SER B C   
3277 O O   . SER B 78  ? 0.3749 0.3171 0.4709 0.0733  0.0015  0.0253  58  SER B O   
3278 C CB  . SER B 78  ? 0.3432 0.3289 0.4599 0.0524  0.0511  0.1515  58  SER B CB  
3279 O OG  . SER B 78  ? 0.3449 0.3467 0.5237 0.0470  0.0643  0.1848  58  SER B OG  
3285 N N   . GLY B 79  ? 0.2850 0.3272 0.3667 0.0488  0.0243  0.0612  59  GLY B N   
3286 C CA  . GLY B 79  ? 0.2627 0.3696 0.3865 0.0464  0.0389  0.0320  59  GLY B CA  
3287 C C   . GLY B 79  ? 0.3098 0.3706 0.4297 0.0499  0.0432  0.0487  59  GLY B C   
3288 O O   . GLY B 79  ? 0.3931 0.3884 0.5115 0.0237  0.0325  -0.0241 59  GLY B O   
3292 N N   . GLN B 80  ? 0.2616 0.3301 0.4304 0.0467  0.0399  0.0589  60  GLN B N   
3293 C CA  . GLN B 80  ? 0.3012 0.3064 0.4640 0.0323  0.0191  0.0988  60  GLN B CA  
3294 C C   . GLN B 80  ? 0.2703 0.2753 0.3936 0.0333  0.0316  0.0721  60  GLN B C   
3295 O O   . GLN B 80  ? 0.2850 0.2965 0.4121 0.0200  0.0292  0.0775  60  GLN B O   
3296 C CB  . GLN B 80  ? 0.3537 0.3145 0.5709 0.0459  0.0091  0.1616  60  GLN B CB  
3297 C CG  . GLN B 80  ? 0.4463 0.3829 0.6870 0.0682  0.0172  0.1543  60  GLN B CG  
3298 C CD  . GLN B 80  ? 0.5108 0.4363 0.7864 0.0691  0.0152  0.1173  60  GLN B CD  
3299 O OE1 . GLN B 80  ? 0.5442 0.4596 0.8300 0.0594  -0.0119 0.1040  60  GLN B OE1 
3300 N NE2 . GLN B 80  ? 0.5402 0.4603 0.8301 0.0560  0.0514  0.0945  60  GLN B NE2 
3309 N N   . PRO B 81  ? 0.3093 0.2747 0.3590 0.0331  0.0286  0.0629  61  PRO B N   
3310 C CA  . PRO B 81  ? 0.2678 0.2558 0.3342 0.0027  0.0153  0.0656  61  PRO B CA  
3311 C C   . PRO B 81  ? 0.2670 0.2522 0.3125 -0.0158 0.0335  0.0707  61  PRO B C   
3312 O O   . PRO B 81  ? 0.3048 0.2771 0.3600 -0.0165 0.0492  0.1049  61  PRO B O   
3313 C CB  . PRO B 81  ? 0.2955 0.2546 0.3708 0.0178  0.0029  0.0569  61  PRO B CB  
3314 C CG  . PRO B 81  ? 0.3781 0.2860 0.4101 0.0313  0.0046  0.0185  61  PRO B CG  
3315 C CD  . PRO B 81  ? 0.3646 0.2968 0.4086 0.0382  0.0031  0.0213  61  PRO B CD  
3323 N N   . ILE B 82  ? 0.2433 0.2508 0.2792 -0.0218 0.0321  0.0786  62  ILE B N   
3324 C CA  . ILE B 82  ? 0.2658 0.2800 0.2747 -0.0533 0.0493  0.0639  62  ILE B CA  
3325 C C   . ILE B 82  ? 0.2590 0.2659 0.2701 -0.0221 0.0516  0.0729  62  ILE B C   
3326 O O   . ILE B 82  ? 0.2914 0.2809 0.2972 -0.0056 0.0590  0.1143  62  ILE B O   
3327 C CB  . ILE B 82  ? 0.3402 0.3446 0.2527 -0.0809 0.0488  0.0662  62  ILE B CB  
3328 C CG1 . ILE B 82  ? 0.3592 0.3728 0.2967 -0.1015 0.0382  0.0412  62  ILE B CG1 
3329 C CG2 . ILE B 82  ? 0.3889 0.3738 0.2826 -0.0837 0.1055  0.0372  62  ILE B CG2 
3330 C CD1 . ILE B 82  ? 0.4010 0.4013 0.3576 -0.0828 0.0667  0.0176  62  ILE B CD1 
3342 N N   . ALA B 83  ? 0.2341 0.2633 0.3380 -0.0110 0.0224  0.0785  63  ALA B N   
3343 C CA  . ALA B 83  ? 0.2276 0.2663 0.3889 -0.0002 0.0438  0.0719  63  ALA B CA  
3344 C C   . ALA B 83  ? 0.2545 0.2918 0.3533 -0.0023 0.0407  0.1149  63  ALA B C   
3345 O O   . ALA B 83  ? 0.2886 0.3495 0.3945 0.0181  0.0390  0.1727  63  ALA B O   
3346 C CB  . ALA B 83  ? 0.2736 0.2924 0.4434 0.0089  0.0160  0.0552  63  ALA B CB  
3352 N N   . ILE B 84  ? 0.2180 0.2854 0.3130 -0.0020 0.0310  0.0967  64  ILE B N   
3353 C CA  . ILE B 84  ? 0.2266 0.3258 0.3201 0.0178  0.0221  0.0898  64  ILE B CA  
3354 C C   . ILE B 84  ? 0.2190 0.3439 0.3132 -0.0068 0.0378  0.1088  64  ILE B C   
3355 O O   . ILE B 84  ? 0.2480 0.3403 0.2820 -0.0341 0.0485  0.0873  64  ILE B O   
3356 C CB  . ILE B 84  ? 0.2714 0.3766 0.3539 0.0400  -0.0138 0.0354  64  ILE B CB  
3357 C CG1 . ILE B 84  ? 0.3328 0.3935 0.4000 0.0669  -0.0070 0.0207  64  ILE B CG1 
3358 C CG2 . ILE B 84  ? 0.2798 0.4309 0.3324 0.0532  0.0283  0.0378  64  ILE B CG2 
3359 C CD1 . ILE B 84  ? 0.4109 0.4224 0.4949 0.0372  0.0024  0.0287  64  ILE B CD1 
3371 N N   . ARG B 85  ? 0.2642 0.3542 0.3327 -0.0230 0.0608  0.1241  65  ARG B N   
3372 C CA  . ARG B 85  ? 0.2687 0.3591 0.3582 -0.0357 0.0542  0.1234  65  ARG B CA  
3373 C C   . ARG B 85  ? 0.2570 0.3827 0.3385 -0.0447 0.0458  0.1320  65  ARG B C   
3374 O O   . ARG B 85  ? 0.2891 0.4232 0.3471 -0.0474 0.0676  0.1354  65  ARG B O   
3375 C CB  . ARG B 85  ? 0.3053 0.3414 0.4398 -0.0238 0.0540  0.1412  65  ARG B CB  
3376 C CG  . ARG B 85  ? 0.3029 0.3470 0.4991 -0.0157 0.0378  0.1340  65  ARG B CG  
3377 C CD  . ARG B 85  ? 0.3380 0.3535 0.5597 -0.0184 0.0164  0.1380  65  ARG B CD  
3378 N NE  . ARG B 85  ? 0.3560 0.3812 0.6216 -0.0086 -0.0065 0.1041  65  ARG B NE  
3379 C CZ  . ARG B 85  ? 0.4007 0.3984 0.6654 0.0011  -0.0014 0.0763  65  ARG B CZ  
3380 N NH1 . ARG B 85  ? 0.4273 0.3964 0.6421 0.0365  -0.0134 0.0762  65  ARG B NH1 
3381 N NH2 . ARG B 85  ? 0.4500 0.4070 0.7320 -0.0168 0.0518  0.0417  65  ARG B NH2 
3395 N N   . GLY B 86  ? 0.2522 0.3549 0.3567 -0.0478 0.0157  0.1406  66  GLY B N   
3396 C CA  . GLY B 86  ? 0.2662 0.3430 0.3837 -0.0637 0.0079  0.1409  66  GLY B CA  
3397 C C   . GLY B 86  ? 0.2246 0.3609 0.4050 -0.0720 0.0116  0.1397  66  GLY B C   
3398 O O   . GLY B 86  ? 0.2392 0.3519 0.3967 -0.0375 0.0519  0.1457  66  GLY B O   
3402 N N   A ARG B 87  ? 0.2230 0.3685 0.4680 -0.0806 0.0370  0.1275  67  ARG B N   
3403 N N   B ARG B 87  ? 0.2666 0.3794 0.4659 -0.0345 0.0150  0.1049  67  ARG B N   
3404 C CA  A ARG B 87  ? 0.2347 0.3637 0.5050 -0.0802 0.0373  0.1234  67  ARG B CA  
3405 C CA  B ARG B 87  ? 0.2976 0.3854 0.5073 -0.0050 0.0316  0.0898  67  ARG B CA  
3406 C C   A ARG B 87  ? 0.2057 0.3546 0.5076 -0.0395 0.0621  0.1346  67  ARG B C   
3407 C C   B ARG B 87  ? 0.2875 0.3799 0.5201 -0.0057 0.0805  0.1116  67  ARG B C   
3408 O O   A ARG B 87  ? 0.1972 0.3594 0.5818 -0.0151 0.0616  0.1240  67  ARG B O   
3409 O O   B ARG B 87  ? 0.2958 0.3888 0.5759 0.0010  0.0944  0.1052  67  ARG B O   
3410 C CB  A ARG B 87  ? 0.2385 0.3731 0.4854 -0.1198 0.0037  0.1271  67  ARG B CB  
3411 C CB  B ARG B 87  ? 0.3048 0.3952 0.4926 0.0239  -0.0010 0.0704  67  ARG B CB  
3412 C CG  A ARG B 87  ? 0.2665 0.3904 0.3684 -0.1065 0.0184  0.1443  67  ARG B CG  
3413 C CG  B ARG B 87  ? 0.2993 0.3924 0.3954 0.0585  -0.0112 0.0554  67  ARG B CG  
3414 C CD  A ARG B 87  ? 0.2708 0.4278 0.4062 -0.0678 0.0422  0.1005  67  ARG B CD  
3415 C CD  B ARG B 87  ? 0.2589 0.3946 0.3636 0.0868  -0.0432 0.0472  67  ARG B CD  
3416 N NE  A ARG B 87  ? 0.2261 0.4592 0.4122 -0.0494 0.0573  0.0466  67  ARG B NE  
3417 N NE  B ARG B 87  ? 0.2577 0.4143 0.4262 0.0500  -0.0298 0.0017  67  ARG B NE  
3418 C CZ  A ARG B 87  ? 0.1889 0.5026 0.3786 -0.0190 0.0584  0.0328  67  ARG B CZ  
3419 C CZ  B ARG B 87  ? 0.2834 0.4401 0.5045 0.0440  0.0234  -0.0046 67  ARG B CZ  
3420 N NH1 A ARG B 87  ? 0.2223 0.5412 0.4036 -0.0359 0.0301  0.0673  67  ARG B NH1 
3421 N NH1 B ARG B 87  ? 0.3210 0.4410 0.5354 0.0821  -0.0117 -0.0156 67  ARG B NH1 
3422 N NH2 A ARG B 87  ? 0.2066 0.5026 0.2754 0.0521  0.0250  -0.0196 67  ARG B NH2 
3423 N NH2 B ARG B 87  ? 0.2352 0.4611 0.5443 -0.0177 0.0567  -0.0180 67  ARG B NH2 
3450 N N   . GLU B 88  ? 0.3132 0.3880 0.5147 -0.0200 0.1284  0.1345  68  GLU B N   
3451 C CA  . GLU B 88  ? 0.4009 0.4050 0.5144 -0.0368 0.1902  0.1536  68  GLU B CA  
3452 C C   . GLU B 88  ? 0.4446 0.3924 0.4620 -0.0026 0.1871  0.1516  68  GLU B C   
3453 O O   . GLU B 88  ? 0.4655 0.3892 0.4436 -0.0138 0.2167  0.0948  68  GLU B O   
3454 C CB  . GLU B 88  ? 0.5145 0.4389 0.5866 -0.0473 0.2422  0.1461  68  GLU B CB  
3455 C CG  . GLU B 88  ? 0.6003 0.4427 0.6131 -0.0632 0.2474  0.1686  68  GLU B CG  
3461 N N   . LYS B 89  ? 0.4375 0.3832 0.4052 0.0310  0.1588  0.1415  69  LYS B N   
3462 C CA  . LYS B 89  ? 0.4658 0.4004 0.3223 0.0514  0.1158  0.1374  69  LYS B CA  
3463 C C   . LYS B 89  ? 0.4016 0.3588 0.2904 0.0448  0.0796  0.1041  69  LYS B C   
3464 O O   . LYS B 89  ? 0.4187 0.3670 0.2778 0.0683  0.0627  0.0785  69  LYS B O   
3465 C CB  . LYS B 89  ? 0.4765 0.4268 0.3705 0.0555  0.1083  0.1354  69  LYS B CB  
3466 C CG  . LYS B 89  ? 0.4982 0.4492 0.4129 0.0409  0.1207  0.1305  69  LYS B CG  
3471 N N   . LEU B 90  ? 0.3025 0.3256 0.3030 0.0291  0.0717  0.1145  70  LEU B N   
3472 C CA  . LEU B 90  ? 0.2538 0.3222 0.2820 0.0056  0.0535  0.0899  70  LEU B CA  
3473 C C   . LEU B 90  ? 0.2693 0.3405 0.2815 0.0057  0.0695  0.0657  70  LEU B C   
3474 O O   . LEU B 90  ? 0.2909 0.3448 0.2939 0.0187  0.0701  0.0341  70  LEU B O   
3475 C CB  . LEU B 90  ? 0.2354 0.3249 0.2933 -0.0067 0.0440  0.0769  70  LEU B CB  
3476 C CG  . LEU B 90  ? 0.2468 0.3122 0.2874 -0.0237 0.0488  0.0476  70  LEU B CG  
3477 C CD1 . LEU B 90  ? 0.2759 0.3182 0.3229 -0.0250 0.0347  0.0472  70  LEU B CD1 
3478 C CD2 . LEU B 90  ? 0.2747 0.3119 0.3099 -0.0199 0.0687  0.0405  70  LEU B CD2 
3490 N N   . GLY B 91  ? 0.2798 0.3488 0.3183 0.0107  0.0789  0.0837  71  GLY B N   
3491 C CA  . GLY B 91  ? 0.3283 0.3777 0.3077 0.0473  0.0989  0.0523  71  GLY B CA  
3492 C C   . GLY B 91  ? 0.3890 0.3994 0.2901 0.0692  0.1291  0.0504  71  GLY B C   
3493 O O   . GLY B 91  ? 0.4021 0.3928 0.3072 0.0769  0.1274  0.0332  71  GLY B O   
3497 N N   . GLU B 92  ? 0.4430 0.4348 0.2899 0.0931  0.1328  0.0878  72  GLU B N   
3498 C CA  . GLU B 92  ? 0.4712 0.4525 0.3118 0.0877  0.1278  0.0934  72  GLU B CA  
3499 C C   . GLU B 92  ? 0.4452 0.4650 0.2825 0.1035  0.0636  0.0732  72  GLU B C   
3500 O O   . GLU B 92  ? 0.4511 0.4850 0.2857 0.0817  0.0501  0.0703  72  GLU B O   
3501 C CB  . GLU B 92  ? 0.5807 0.4919 0.4120 0.0940  0.1685  0.1470  72  GLU B CB  
3502 C CG  . GLU B 92  ? 0.6474 0.5333 0.5010 0.1121  0.2126  0.1769  72  GLU B CG  
3503 C CD  . GLU B 92  ? 0.7421 0.5859 0.5890 0.0967  0.2476  0.1970  72  GLU B CD  
3504 O OE1 . GLU B 92  ? 0.8019 0.6056 0.6126 0.1222  0.2057  0.2297  72  GLU B OE1 
3505 O OE2 . GLU B 92  ? 0.7603 0.6018 0.6237 0.0641  0.3163  0.1812  72  GLU B OE2 
3512 N N   . HIS B 93  ? 0.4105 0.4605 0.2594 0.0990  0.0564  0.0282  73  HIS B N   
3513 C CA  . HIS B 93  ? 0.3459 0.4719 0.3163 0.0681  0.0285  0.0060  73  HIS B CA  
3514 C C   . HIS B 93  ? 0.3030 0.4561 0.3208 0.0412  0.0386  -0.0034 73  HIS B C   
3515 O O   . HIS B 93  ? 0.3166 0.4593 0.3114 0.0494  0.0542  -0.0293 73  HIS B O   
3516 C CB  . HIS B 93  ? 0.3482 0.4912 0.3540 0.0272  0.0369  -0.0693 73  HIS B CB  
3517 C CG  . HIS B 93  ? 0.3286 0.5340 0.3539 0.0027  0.0365  -0.0401 73  HIS B CG  
3518 N ND1 . HIS B 93  ? 0.3302 0.5593 0.3635 -0.0217 0.0893  -0.0367 73  HIS B ND1 
3519 C CD2 . HIS B 93  ? 0.3184 0.5508 0.3685 -0.0030 0.0528  -0.0316 73  HIS B CD2 
3520 C CE1 . HIS B 93  ? 0.3197 0.5682 0.3785 -0.0453 0.0528  -0.0411 73  HIS B CE1 
3521 N NE2 . HIS B 93  ? 0.3869 0.5594 0.3803 -0.0275 0.0821  -0.0430 73  HIS B NE2 
3529 N N   . ALA B 94  ? 0.2853 0.4287 0.2871 0.0118  0.0154  0.0052  74  ALA B N   
3530 C CA  . ALA B 94  ? 0.3018 0.4204 0.2681 0.0096  0.0699  0.0405  74  ALA B CA  
3531 C C   . ALA B 94  ? 0.2711 0.4238 0.2559 -0.0198 0.0687  0.0390  74  ALA B C   
3532 O O   . ALA B 94  ? 0.2767 0.4135 0.2856 -0.0235 0.0446  0.0435  74  ALA B O   
3533 C CB  . ALA B 94  ? 0.3181 0.4105 0.3008 0.0200  0.0205  0.0551  74  ALA B CB  
3539 N N   . VAL B 95  ? 0.3013 0.4503 0.2798 -0.0097 0.0765  0.0224  75  VAL B N   
3540 C CA  . VAL B 95  ? 0.3958 0.4638 0.2751 -0.0116 0.0958  0.0673  75  VAL B CA  
3541 C C   . VAL B 95  ? 0.4276 0.4364 0.2680 -0.0468 0.0044  0.0579  75  VAL B C   
3542 O O   . VAL B 95  ? 0.4355 0.4264 0.2716 -0.0298 0.0131  0.0301  75  VAL B O   
3543 C CB  . VAL B 95  ? 0.4586 0.5089 0.3466 -0.0133 0.1548  0.0591  75  VAL B CB  
3544 C CG1 . VAL B 95  ? 0.5730 0.5283 0.3155 0.0040  0.1503  0.0650  75  VAL B CG1 
3545 C CG2 . VAL B 95  ? 0.4559 0.5295 0.4036 -0.0202 0.1802  0.0500  75  VAL B CG2 
3555 N N   A TRP B 96  ? 0.4191 0.4222 0.2632 -0.0522 -0.0101 0.0571  76  TRP B N   
3556 N N   B TRP B 96  ? 0.4331 0.4295 0.2798 -0.0579 -0.0151 0.0669  76  TRP B N   
3557 C CA  A TRP B 96  ? 0.4556 0.4365 0.2888 -0.0577 -0.0429 0.0564  76  TRP B CA  
3558 C CA  B TRP B 96  ? 0.4684 0.4431 0.3108 -0.0652 -0.0416 0.0744  76  TRP B CA  
3559 C C   A TRP B 96  ? 0.4265 0.4578 0.3521 -0.0840 -0.0949 0.1001  76  TRP B C   
3560 C C   B TRP B 96  ? 0.4355 0.4593 0.3576 -0.0846 -0.0840 0.1065  76  TRP B C   
3561 O O   A TRP B 96  ? 0.4857 0.4734 0.4276 -0.0953 -0.1341 0.1127  76  TRP B O   
3562 O O   B TRP B 96  ? 0.4936 0.4714 0.4169 -0.0882 -0.1177 0.1208  76  TRP B O   
3563 C CB  A TRP B 96  ? 0.4696 0.4341 0.3080 -0.0375 -0.0077 0.0579  76  TRP B CB  
3564 C CB  B TRP B 96  ? 0.4895 0.4416 0.3237 -0.0532 -0.0160 0.0802  76  TRP B CB  
3569 N N   . SER B 97  ? 0.3651 0.4617 0.3487 -0.0988 -0.0349 0.0973  77  SER B N   
3570 C CA  . SER B 97  ? 0.3523 0.4755 0.3569 -0.0781 0.0399  0.1148  77  SER B CA  
3571 C C   . SER B 97  ? 0.3362 0.4840 0.3457 -0.1021 -0.0154 0.1151  77  SER B C   
3572 O O   . SER B 97  ? 0.3536 0.5045 0.3750 -0.1366 -0.0382 0.1378  77  SER B O   
3573 C CB  . SER B 97  ? 0.4323 0.4801 0.3647 -0.0423 0.1462  0.1207  77  SER B CB  
3574 O OG  . SER B 97  ? 0.5052 0.4848 0.4116 0.0313  0.1925  0.0932  77  SER B OG  
3581 N N   . LEU B 98  ? 0.3442 0.4719 0.3239 -0.0883 -0.0102 0.1037  78  LEU B N   
3582 C CA  . LEU B 98  ? 0.3673 0.4541 0.3814 -0.0743 -0.0241 0.1053  78  LEU B CA  
3583 C C   . LEU B 98  ? 0.4055 0.4170 0.4001 -0.0869 -0.0373 0.0934  78  LEU B C   
3584 O O   . LEU B 98  ? 0.4681 0.4498 0.3937 -0.1266 -0.0487 0.0974  78  LEU B O   
3585 C CB  . LEU B 98  ? 0.3654 0.4752 0.4046 -0.0401 -0.0369 0.0981  78  LEU B CB  
3586 C CG  . LEU B 98  ? 0.3851 0.4961 0.3798 -0.0032 0.0032  0.1043  78  LEU B CG  
3587 C CD1 . LEU B 98  ? 0.4150 0.5217 0.4349 0.0249  0.0165  0.0670  78  LEU B CD1 
3588 C CD2 . LEU B 98  ? 0.4031 0.4953 0.3234 0.0057  0.0335  0.0911  78  LEU B CD2 
3617 N N   . CYS B 100 ? 0.3171 0.3886 0.3665 -0.0441 -0.0092 0.1417  80  CYS B N   
3618 C CA  . CYS B 100 ? 0.3060 0.3574 0.4595 -0.0254 -0.0359 0.1637  80  CYS B CA  
3619 C C   . CYS B 100 ? 0.2918 0.3101 0.3956 -0.0060 0.0020  0.1107  80  CYS B C   
3620 O O   . CYS B 100 ? 0.3058 0.3268 0.3954 -0.0220 -0.0243 0.0931  80  CYS B O   
3621 C CB  . CYS B 100 ? 0.3389 0.3810 0.6505 -0.0474 -0.0764 0.2651  80  CYS B CB  
3622 S SG  . CYS B 100 ? 0.4372 0.4836 0.7996 -0.0918 -0.1065 0.3385  80  CYS B SG  
3628 N N   . PHE B 101 ? 0.2668 0.2930 0.3208 0.0219  0.0327  0.0729  81  PHE B N   
3629 C CA  . PHE B 101 ? 0.2698 0.2601 0.2924 0.0342  0.0287  0.0428  81  PHE B CA  
3630 C C   . PHE B 101 ? 0.2802 0.2554 0.2635 0.0324  0.0456  0.0180  81  PHE B C   
3631 O O   . PHE B 101 ? 0.2856 0.2620 0.2882 0.0452  0.0178  0.0111  81  PHE B O   
3632 C CB  . PHE B 101 ? 0.2747 0.2493 0.3214 0.0439  0.0425  0.0306  81  PHE B CB  
3633 C CG  . PHE B 101 ? 0.2741 0.2638 0.3649 0.0315  0.0670  0.0639  81  PHE B CG  
3634 C CD1 . PHE B 101 ? 0.2560 0.2879 0.3252 0.0054  0.0435  0.0297  81  PHE B CD1 
3635 C CD2 . PHE B 101 ? 0.2941 0.2929 0.5150 0.0583  0.1208  0.1253  81  PHE B CD2 
3636 C CE1 . PHE B 101 ? 0.2650 0.3033 0.3985 0.0217  0.0487  0.0754  81  PHE B CE1 
3637 C CE2 . PHE B 101 ? 0.2921 0.3186 0.5694 0.0776  0.1129  0.1313  81  PHE B CE2 
3638 C CZ  . PHE B 101 ? 0.2662 0.3206 0.5016 0.0565  0.0895  0.1218  81  PHE B CZ  
3648 N N   . PRO B 102 ? 0.2893 0.2723 0.2676 0.0281  0.0445  -0.0135 82  PRO B N   
3649 C CA  . PRO B 102 ? 0.2826 0.2872 0.3054 0.0464  0.0483  -0.0284 82  PRO B CA  
3650 C C   . PRO B 102 ? 0.2930 0.3012 0.3210 0.0578  0.0264  -0.0310 82  PRO B C   
3651 O O   . PRO B 102 ? 0.3313 0.3716 0.3255 0.0834  0.0408  0.0181  82  PRO B O   
3652 C CB  . PRO B 102 ? 0.3275 0.3120 0.3271 0.0078  0.0629  -0.0487 82  PRO B CB  
3653 C CG  . PRO B 102 ? 0.3452 0.2958 0.3150 -0.0056 0.0400  -0.0365 82  PRO B CG  
3654 C CD  . PRO B 102 ? 0.3032 0.2844 0.2860 0.0058  0.0272  -0.0128 82  PRO B CD  
3662 N N   . ASP B 103 ? 0.3166 0.2928 0.2995 0.0852  0.0320  -0.0387 83  ASP B N   
3663 C CA  . ASP B 103 ? 0.3579 0.2615 0.2633 0.1037  0.0339  -0.0493 83  ASP B CA  
3664 C C   . ASP B 103 ? 0.3082 0.2308 0.2761 0.0909  0.0423  -0.0348 83  ASP B C   
3665 O O   . ASP B 103 ? 0.3513 0.2190 0.2751 0.0690  0.0509  -0.0200 83  ASP B O   
3666 C CB  . ASP B 103 ? 0.3760 0.2713 0.2781 0.0947  0.0421  -0.0377 83  ASP B CB  
3667 C CG  . ASP B 103 ? 0.4187 0.2742 0.2967 0.0734  0.0296  -0.0327 83  ASP B CG  
3668 O OD1 . ASP B 103 ? 0.3804 0.2730 0.3276 0.0885  0.0373  -0.0219 83  ASP B OD1 
3669 O OD2 . ASP B 103 ? 0.5237 0.2784 0.3607 0.0386  0.0667  -0.0452 83  ASP B OD2 
3674 N N   . TRP B 104 ? 0.2762 0.2123 0.2787 0.0664  0.0556  -0.0453 84  TRP B N   
3675 C CA  . TRP B 104 ? 0.2717 0.1689 0.2724 0.0436  0.0314  -0.0426 84  TRP B CA  
3676 C C   . TRP B 104 ? 0.2546 0.1836 0.2828 0.0378  0.0128  -0.0421 84  TRP B C   
3677 O O   . TRP B 104 ? 0.2506 0.2101 0.2928 0.0409  0.0327  -0.0354 84  TRP B O   
3678 C CB  . TRP B 104 ? 0.2609 0.1701 0.2797 0.0285  0.0443  -0.0360 84  TRP B CB  
3679 C CG  . TRP B 104 ? 0.2782 0.1547 0.2725 0.0456  0.0527  -0.0201 84  TRP B CG  
3680 C CD1 . TRP B 104 ? 0.2830 0.1889 0.2756 0.0273  0.0412  -0.0339 84  TRP B CD1 
3681 C CD2 . TRP B 104 ? 0.2581 0.1567 0.2529 0.0347  0.0447  -0.0012 84  TRP B CD2 
3682 N NE1 . TRP B 104 ? 0.2890 0.1976 0.2707 0.0349  0.0306  -0.0446 84  TRP B NE1 
3683 C CE2 . TRP B 104 ? 0.2736 0.1630 0.2479 0.0401  0.0466  -0.0171 84  TRP B CE2 
3684 C CE3 . TRP B 104 ? 0.2630 0.1730 0.2518 0.0143  0.0301  0.0045  84  TRP B CE3 
3685 C CZ2 . TRP B 104 ? 0.2697 0.1589 0.2564 0.0269  0.0469  0.0066  84  TRP B CZ2 
3686 C CZ3 . TRP B 104 ? 0.2591 0.1622 0.2717 0.0256  0.0360  -0.0066 84  TRP B CZ3 
3687 C CH2 . TRP B 104 ? 0.2613 0.1713 0.2618 0.0328  0.0380  0.0006  84  TRP B CH2 
3698 N N   . VAL B 105 ? 0.2567 0.1954 0.2685 0.0501  0.0351  -0.0309 85  VAL B N   
3699 C CA  . VAL B 105 ? 0.2631 0.1636 0.2798 0.0632  0.0243  -0.0328 85  VAL B CA  
3700 C C   . VAL B 105 ? 0.2617 0.1442 0.2840 0.0418  0.0337  -0.0164 85  VAL B C   
3701 O O   . VAL B 105 ? 0.2472 0.1778 0.2652 0.0337  0.0249  -0.0172 85  VAL B O   
3702 C CB  . VAL B 105 ? 0.3437 0.1721 0.2795 0.1064  0.0146  -0.0271 85  VAL B CB  
3703 C CG1 . VAL B 105 ? 0.3618 0.1806 0.3350 0.0728  0.0640  0.0095  85  VAL B CG1 
3704 C CG2 . VAL B 105 ? 0.4221 0.2013 0.3326 0.1238  0.0249  -0.0312 85  VAL B CG2 
3714 N N   . TRP B 106 ? 0.2382 0.1759 0.2590 0.0252  0.0304  -0.0136 86  TRP B N   
3715 C CA  . TRP B 106 ? 0.2380 0.1685 0.2389 0.0262  0.0420  0.0041  86  TRP B CA  
3716 C C   . TRP B 106 ? 0.2757 0.1750 0.2617 0.0298  0.0655  0.0100  86  TRP B C   
3717 O O   . TRP B 106 ? 0.2817 0.1986 0.3136 0.0387  0.0612  0.0242  86  TRP B O   
3718 C CB  . TRP B 106 ? 0.2440 0.1739 0.2377 0.0258  0.0423  0.0016  86  TRP B CB  
3719 C CG  . TRP B 106 ? 0.2343 0.1797 0.2350 0.0114  0.0406  -0.0061 86  TRP B CG  
3720 C CD1 . TRP B 106 ? 0.2239 0.1913 0.2442 0.0214  0.0584  -0.0002 86  TRP B CD1 
3721 C CD2 . TRP B 106 ? 0.2296 0.1764 0.2280 0.0184  0.0445  -0.0028 86  TRP B CD2 
3722 N NE1 . TRP B 106 ? 0.2318 0.1929 0.2505 0.0074  0.0437  0.0171  86  TRP B NE1 
3723 C CE2 . TRP B 106 ? 0.2381 0.1785 0.2342 0.0037  0.0325  0.0113  86  TRP B CE2 
3724 C CE3 . TRP B 106 ? 0.2471 0.1703 0.2537 0.0145  0.0570  -0.0073 86  TRP B CE3 
3725 C CZ2 . TRP B 106 ? 0.2790 0.1674 0.2502 0.0207  0.0574  0.0088  86  TRP B CZ2 
3726 C CZ3 . TRP B 106 ? 0.2465 0.1707 0.2473 0.0205  0.0510  -0.0116 86  TRP B CZ3 
3727 C CH2 . TRP B 106 ? 0.2654 0.1712 0.2544 0.0220  0.0566  -0.0134 86  TRP B CH2 
3738 N N   . THR B 107 ? 0.2600 0.1446 0.2423 0.0278  0.0491  0.0077  87  THR B N   
3739 C CA  . THR B 107 ? 0.2920 0.1375 0.2821 0.0228  0.0610  0.0275  87  THR B CA  
3740 C C   . THR B 107 ? 0.2781 0.1234 0.2608 0.0142  0.0691  0.0227  87  THR B C   
3741 O O   . THR B 107 ? 0.2836 0.1269 0.2489 0.0248  0.0513  0.0159  87  THR B O   
3742 C CB  . THR B 107 ? 0.3090 0.1780 0.3227 0.0313  0.0727  -0.0189 87  THR B CB  
3743 O OG1 . THR B 107 ? 0.3156 0.1920 0.3508 0.0094  0.0594  -0.0445 87  THR B OG1 
3744 C CG2 . THR B 107 ? 0.3186 0.2067 0.3274 0.0197  0.0742  -0.0317 87  THR B CG2 
3752 N N   . ASP B 108 ? 0.2930 0.1546 0.2694 0.0225  0.0724  0.0345  88  ASP B N   
3753 C CA  . ASP B 108 ? 0.2972 0.1763 0.2857 0.0220  0.0718  0.0522  88  ASP B CA  
3754 C C   . ASP B 108 ? 0.3117 0.1484 0.2761 0.0286  0.0491  0.0508  88  ASP B C   
3755 O O   . ASP B 108 ? 0.3004 0.1678 0.2852 0.0243  0.0411  0.0356  88  ASP B O   
3756 C CB  . ASP B 108 ? 0.3213 0.1981 0.3144 -0.0206 0.0841  0.0248  88  ASP B CB  
3757 C CG  . ASP B 108 ? 0.3763 0.1877 0.3374 0.0053  0.1033  -0.0100 88  ASP B CG  
3758 O OD1 . ASP B 108 ? 0.4135 0.1386 0.3066 -0.0245 0.1355  -0.0151 88  ASP B OD1 
3759 O OD2 . ASP B 108 ? 0.3645 0.1744 0.2892 -0.0017 0.0679  -0.0429 88  ASP B OD2 
3764 N N   . ILE B 109 ? 0.2880 0.1607 0.2710 0.0370  0.0465  0.0275  89  ILE B N   
3765 C CA  . ILE B 109 ? 0.2802 0.1869 0.2572 0.0424  0.0636  0.0321  89  ILE B CA  
3766 C C   . ILE B 109 ? 0.2676 0.2180 0.2422 0.0527  0.0470  0.0227  89  ILE B C   
3767 O O   . ILE B 109 ? 0.3300 0.2458 0.2719 0.0756  0.0293  0.0440  89  ILE B O   
3768 C CB  . ILE B 109 ? 0.2772 0.2093 0.2724 0.0490  0.0702  0.0409  89  ILE B CB  
3769 C CG1 . ILE B 109 ? 0.2845 0.2415 0.2607 0.0561  0.0765  0.0321  89  ILE B CG1 
3770 C CG2 . ILE B 109 ? 0.3079 0.2219 0.3210 0.0411  0.0605  0.0357  89  ILE B CG2 
3771 C CD1 . ILE B 109 ? 0.3068 0.2863 0.2730 0.0748  0.0736  0.0394  89  ILE B CD1 
3783 N N   A GLN B 110 ? 0.2378 0.2140 0.2365 0.0477  0.0492  0.0232  90  GLN B N   
3784 N N   B GLN B 110 ? 0.2480 0.2149 0.2403 0.0381  0.0473  0.0250  90  GLN B N   
3785 C CA  A GLN B 110 ? 0.2257 0.2213 0.2466 0.0452  0.0513  0.0408  90  GLN B CA  
3786 C CA  B GLN B 110 ? 0.2497 0.2207 0.2470 0.0215  0.0508  0.0376  90  GLN B CA  
3787 C C   A GLN B 110 ? 0.2221 0.2050 0.2297 0.0536  0.0460  0.0373  90  GLN B C   
3788 C C   B GLN B 110 ? 0.2390 0.2071 0.2198 0.0297  0.0456  0.0468  90  GLN B C   
3789 O O   A GLN B 110 ? 0.2361 0.2094 0.1967 0.0414  0.0454  0.0166  90  GLN B O   
3790 O O   B GLN B 110 ? 0.2156 0.2072 0.2028 0.0172  0.0437  0.0411  90  GLN B O   
3791 C CB  A GLN B 110 ? 0.2168 0.2619 0.2769 0.0295  0.0646  0.0416  90  GLN B CB  
3792 C CB  B GLN B 110 ? 0.2743 0.2505 0.2625 -0.0089 0.0641  0.0378  90  GLN B CB  
3793 C CG  A GLN B 110 ? 0.2615 0.2915 0.3000 -0.0058 0.0954  0.0407  90  GLN B CG  
3794 C CG  B GLN B 110 ? 0.3114 0.2919 0.2777 -0.0175 0.0824  0.0320  90  GLN B CG  
3795 C CD  A GLN B 110 ? 0.3001 0.3336 0.3237 -0.0338 0.0815  0.0622  90  GLN B CD  
3796 C CD  B GLN B 110 ? 0.3462 0.3486 0.3116 0.0037  0.0934  0.0460  90  GLN B CD  
3797 O OE1 A GLN B 110 ? 0.2706 0.3362 0.3309 -0.0326 0.0586  0.0810  90  GLN B OE1 
3798 O OE1 B GLN B 110 ? 0.3234 0.3930 0.3260 0.0221  0.0884  0.0526  90  GLN B OE1 
3799 N NE2 A GLN B 110 ? 0.3061 0.3677 0.3473 -0.0354 0.0387  0.0814  90  GLN B NE2 
3800 N NE2 B GLN B 110 ? 0.3494 0.3659 0.3120 0.0053  0.0871  0.0388  90  GLN B NE2 
3817 N N   . ILE B 111 ? 0.2239 0.2150 0.2430 0.0406  0.0337  0.0386  91  ILE B N   
3818 C CA  . ILE B 111 ? 0.2333 0.2303 0.2272 0.0308  0.0346  0.0289  91  ILE B CA  
3819 C C   . ILE B 111 ? 0.2498 0.2339 0.2279 0.0375  0.0362  0.0375  91  ILE B C   
3820 O O   . ILE B 111 ? 0.3087 0.2511 0.2364 0.0477  0.0247  0.0442  91  ILE B O   
3821 C CB  . ILE B 111 ? 0.2256 0.2659 0.2924 0.0323  0.0512  -0.0040 91  ILE B CB  
3822 C CG1 . ILE B 111 ? 0.2393 0.2885 0.3604 0.0381  0.0846  -0.0358 91  ILE B CG1 
3823 C CG2 . ILE B 111 ? 0.2345 0.3069 0.3246 0.0111  0.0296  0.0069  91  ILE B CG2 
3824 C CD1 . ILE B 111 ? 0.2621 0.3083 0.4029 0.0485  0.1084  0.0034  91  ILE B CD1 
3837 N N   . PHE B 112 ? 0.2252 0.2255 0.2200 0.0284  0.0275  0.0206  92  PHE B N   
3838 C CA  . PHE B 112 ? 0.2368 0.2428 0.2129 0.0096  0.0314  0.0234  92  PHE B CA  
3839 C C   . PHE B 112 ? 0.2200 0.2443 0.2220 0.0086  0.0479  0.0261  92  PHE B C   
3840 O O   . PHE B 112 ? 0.2198 0.2435 0.2357 0.0018  0.0348  0.0220  92  PHE B O   
3841 C CB  . PHE B 112 ? 0.2166 0.2461 0.2410 0.0173  0.0309  0.0169  92  PHE B CB  
3842 C CG  . PHE B 112 ? 0.2249 0.2400 0.2718 0.0166  0.0498  0.0065  92  PHE B CG  
3843 C CD1 . PHE B 112 ? 0.2395 0.2413 0.2915 0.0116  0.0776  0.0269  92  PHE B CD1 
3844 C CD2 . PHE B 112 ? 0.2300 0.2785 0.2830 0.0185  0.0412  -0.0037 92  PHE B CD2 
3845 C CE1 . PHE B 112 ? 0.2661 0.2468 0.3237 0.0138  0.0868  0.0237  92  PHE B CE1 
3846 C CE2 . PHE B 112 ? 0.2265 0.2870 0.3117 0.0157  0.0351  -0.0280 92  PHE B CE2 
3847 C CZ  . PHE B 112 ? 0.2478 0.2624 0.3843 0.0264  0.0487  -0.0239 92  PHE B CZ  
3857 N N   . GLU B 113 ? 0.2113 0.2858 0.2138 0.0213  0.0166  0.0124  93  GLU B N   
3858 C CA  . GLU B 113 ? 0.2164 0.3364 0.2513 0.0199  0.0088  -0.0028 93  GLU B CA  
3859 C C   . GLU B 113 ? 0.2078 0.3157 0.2533 0.0110  0.0522  0.0064  93  GLU B C   
3860 O O   . GLU B 113 ? 0.2334 0.2998 0.2664 0.0066  0.0742  0.0002  93  GLU B O   
3861 C CB  . GLU B 113 ? 0.2549 0.4228 0.3260 0.0597  -0.0210 -0.0154 93  GLU B CB  
3862 C CG  . GLU B 113 ? 0.3134 0.5066 0.3792 0.0821  0.0028  0.0429  93  GLU B CG  
3863 C CD  . GLU B 113 ? 0.3904 0.5736 0.4715 0.1289  0.0174  0.0979  93  GLU B CD  
3864 O OE1 . GLU B 113 ? 0.3716 0.6067 0.4918 0.0729  -0.0345 0.1397  93  GLU B OE1 
3865 O OE2 . GLU B 113 ? 0.4562 0.6207 0.5100 0.1237  0.0739  0.0886  93  GLU B OE2 
3872 N N   . THR B 114 ? 0.1923 0.3284 0.2377 -0.0165 0.0402  -0.0069 94  THR B N   
3873 C CA  . THR B 114 ? 0.2087 0.3355 0.2331 -0.0053 0.0492  -0.0254 94  THR B CA  
3874 C C   . THR B 114 ? 0.2086 0.3412 0.2295 -0.0098 0.0158  -0.0301 94  THR B C   
3875 O O   . THR B 114 ? 0.2010 0.3586 0.2529 0.0017  0.0074  -0.0254 94  THR B O   
3876 C CB  . THR B 114 ? 0.1994 0.3221 0.2348 -0.0101 0.0346  -0.0273 94  THR B CB  
3877 O OG1 . THR B 114 ? 0.2087 0.3318 0.2473 -0.0116 0.0298  -0.0360 94  THR B OG1 
3878 C CG2 . THR B 114 ? 0.2028 0.3340 0.2252 -0.0006 0.0287  -0.0260 94  THR B CG2 
3886 N N   . GLN B 115 ? 0.2172 0.3390 0.2300 -0.0116 0.0256  -0.0424 95  GLN B N   
3887 C CA  . GLN B 115 ? 0.2336 0.3697 0.2553 -0.0138 0.0177  -0.0568 95  GLN B CA  
3888 C C   . GLN B 115 ? 0.2248 0.3850 0.2550 -0.0251 0.0197  -0.0424 95  GLN B C   
3889 O O   . GLN B 115 ? 0.2336 0.4327 0.2836 -0.0252 0.0126  -0.0348 95  GLN B O   
3890 C CB  . GLN B 115 ? 0.2291 0.3628 0.2722 -0.0059 0.0288  -0.0906 95  GLN B CB  
3891 C CG  . GLN B 115 ? 0.2363 0.3279 0.3130 -0.0139 0.0319  -0.0899 95  GLN B CG  
3892 C CD  . GLN B 115 ? 0.2350 0.3150 0.3187 0.0027  0.0244  -0.0808 95  GLN B CD  
3893 O OE1 . GLN B 115 ? 0.2301 0.2969 0.2735 -0.0002 0.0259  -0.0550 95  GLN B OE1 
3894 N NE2 . GLN B 115 ? 0.2688 0.3675 0.4202 -0.0017 -0.0079 -0.0892 95  GLN B NE2 
3903 N N   . ASP B 116 ? 0.2132 0.3456 0.2666 -0.0338 0.0195  -0.0273 96  ASP B N   
3904 C CA  . ASP B 116 ? 0.2172 0.3445 0.2705 -0.0346 0.0329  -0.0244 96  ASP B CA  
3905 C C   . ASP B 116 ? 0.2145 0.3515 0.2494 -0.0323 0.0371  -0.0311 96  ASP B C   
3906 O O   . ASP B 116 ? 0.2054 0.3629 0.2389 -0.0276 0.0322  -0.0339 96  ASP B O   
3907 C CB  . ASP B 116 ? 0.2651 0.3304 0.2646 -0.0254 0.0418  -0.0438 96  ASP B CB  
3908 C CG  . ASP B 116 ? 0.2662 0.3277 0.2819 -0.0072 0.0382  -0.0436 96  ASP B CG  
3909 O OD1 . ASP B 116 ? 0.2635 0.3307 0.3231 -0.0193 0.0621  -0.0407 96  ASP B OD1 
3910 O OD2 . ASP B 116 ? 0.3098 0.3309 0.3413 -0.0091 0.0081  -0.0266 96  ASP B OD2 
3915 N N   . PRO B 117 ? 0.2311 0.3472 0.2708 -0.0327 0.0326  -0.0490 97  PRO B N   
3916 C CA  . PRO B 117 ? 0.2119 0.3588 0.2669 -0.0337 0.0149  -0.0365 97  PRO B CA  
3917 C C   . PRO B 117 ? 0.2131 0.3717 0.2749 -0.0334 0.0416  -0.0327 97  PRO B C   
3918 O O   . PRO B 117 ? 0.2166 0.3838 0.2790 -0.0175 0.0284  -0.0182 97  PRO B O   
3919 C CB  . PRO B 117 ? 0.2188 0.3811 0.3151 -0.0262 0.0020  -0.0519 97  PRO B CB  
3920 C CG  . PRO B 117 ? 0.2440 0.3830 0.3634 -0.0505 -0.0061 -0.0623 97  PRO B CG  
3921 C CD  . PRO B 117 ? 0.2466 0.3614 0.3173 -0.0446 0.0249  -0.0519 97  PRO B CD  
3929 N N   . ASN B 118 ? 0.2016 0.3590 0.2634 -0.0368 0.0147  -0.0288 98  ASN B N   
3930 C CA  . ASN B 118 ? 0.2165 0.3440 0.2562 -0.0456 0.0258  -0.0245 98  ASN B CA  
3931 C C   . ASN B 118 ? 0.1948 0.3433 0.2681 -0.0264 0.0375  -0.0245 98  ASN B C   
3932 O O   . ASN B 118 ? 0.2064 0.3792 0.2696 -0.0581 0.0473  -0.0154 98  ASN B O   
3933 C CB  . ASN B 118 ? 0.2035 0.3470 0.3075 -0.0508 0.0490  -0.0412 98  ASN B CB  
3934 C CG  . ASN B 118 ? 0.2372 0.4033 0.3645 -0.0718 0.0525  -0.0781 98  ASN B CG  
3935 O OD1 . ASN B 118 ? 0.2325 0.4302 0.4122 -0.0534 0.0362  -0.0682 98  ASN B OD1 
3936 N ND2 . ASN B 118 ? 0.2558 0.4538 0.4024 -0.0914 0.0484  -0.0619 98  ASN B ND2 
3943 N N   . TRP B 119 ? 0.1942 0.2871 0.2580 -0.0216 0.0190  -0.0294 99  TRP B N   
3944 C CA  . TRP B 119 ? 0.2056 0.2623 0.2278 -0.0063 0.0259  -0.0241 99  TRP B CA  
3945 C C   . TRP B 119 ? 0.2015 0.2628 0.2296 -0.0205 0.0405  0.0019  99  TRP B C   
3946 O O   . TRP B 119 ? 0.2192 0.2824 0.2301 -0.0250 0.0402  -0.0182 99  TRP B O   
3947 C CB  . TRP B 119 ? 0.2152 0.2731 0.2286 -0.0222 0.0406  -0.0229 99  TRP B CB  
3948 C CG  . TRP B 119 ? 0.2104 0.2557 0.2316 -0.0324 0.0395  -0.0231 99  TRP B CG  
3949 C CD1 . TRP B 119 ? 0.1927 0.2656 0.2466 -0.0346 0.0455  -0.0161 99  TRP B CD1 
3950 C CD2 . TRP B 119 ? 0.2282 0.2168 0.2902 0.0023  0.0702  -0.0245 99  TRP B CD2 
3951 N NE1 . TRP B 119 ? 0.1883 0.2328 0.2584 -0.0169 0.0273  -0.0191 99  TRP B NE1 
3952 C CE2 . TRP B 119 ? 0.2161 0.2141 0.2624 -0.0036 0.0383  -0.0205 99  TRP B CE2 
3953 C CE3 . TRP B 119 ? 0.2554 0.2298 0.3030 0.0077  0.0536  -0.0468 99  TRP B CE3 
3954 C CZ2 . TRP B 119 ? 0.2456 0.2301 0.2846 -0.0237 0.0384  -0.0113 99  TRP B CZ2 
3955 C CZ3 . TRP B 119 ? 0.2573 0.2406 0.3456 -0.0122 0.0480  -0.0739 99  TRP B CZ3 
3956 C CH2 . TRP B 119 ? 0.2488 0.2340 0.3109 -0.0161 0.0097  -0.0343 99  TRP B CH2 
3967 N N   . PHE B 120 ? 0.2262 0.2240 0.2283 -0.0098 0.0345  -0.0031 100 PHE B N   
3968 C CA  . PHE B 120 ? 0.2093 0.2148 0.2102 0.0194  0.0368  -0.0003 100 PHE B CA  
3969 C C   . PHE B 120 ? 0.2014 0.2174 0.2187 0.0146  0.0398  -0.0052 100 PHE B C   
3970 O O   . PHE B 120 ? 0.2112 0.2237 0.2257 -0.0132 0.0368  0.0079  100 PHE B O   
3971 C CB  . PHE B 120 ? 0.2083 0.2571 0.2300 0.0209  0.0377  0.0061  100 PHE B CB  
3972 C CG  . PHE B 120 ? 0.1940 0.2979 0.2474 0.0201  0.0550  0.0092  100 PHE B CG  
3973 C CD1 . PHE B 120 ? 0.1918 0.3291 0.3702 0.0193  0.0414  -0.0200 100 PHE B CD1 
3974 C CD2 . PHE B 120 ? 0.2168 0.3279 0.2485 0.0392  0.0433  0.0222  100 PHE B CD2 
3975 C CE1 . PHE B 120 ? 0.2249 0.3635 0.4030 0.0485  0.0387  -0.0773 100 PHE B CE1 
3976 C CE2 . PHE B 120 ? 0.2496 0.3995 0.2764 0.0694  0.0445  0.0081  100 PHE B CE2 
3977 C CZ  . PHE B 120 ? 0.2481 0.4112 0.3172 0.0738  0.0134  -0.0490 100 PHE B CZ  
3987 N N   . TRP B 121 ? 0.2010 0.2183 0.2136 -0.0049 0.0448  0.0122  101 TRP B N   
3988 C CA  . TRP B 121 ? 0.1959 0.1887 0.2292 0.0016  0.0294  0.0134  101 TRP B CA  
3989 C C   . TRP B 121 ? 0.2097 0.1936 0.2069 0.0087  0.0382  0.0232  101 TRP B C   
3990 O O   . TRP B 121 ? 0.2561 0.2042 0.2190 0.0162  0.0124  0.0277  101 TRP B O   
3991 C CB  . TRP B 121 ? 0.1994 0.1969 0.2348 -0.0071 0.0338  -0.0004 101 TRP B CB  
3992 C CG  . TRP B 121 ? 0.1931 0.2075 0.2456 -0.0054 0.0387  -0.0088 101 TRP B CG  
3993 C CD1 . TRP B 121 ? 0.2195 0.2040 0.2483 -0.0061 0.0151  0.0073  101 TRP B CD1 
3994 C CD2 . TRP B 121 ? 0.1908 0.2005 0.2357 -0.0010 0.0409  0.0278  101 TRP B CD2 
3995 N NE1 . TRP B 121 ? 0.2305 0.1896 0.2585 0.0043  0.0339  0.0042  101 TRP B NE1 
3996 C CE2 . TRP B 121 ? 0.1992 0.1885 0.2422 -0.0025 0.0295  0.0184  101 TRP B CE2 
3997 C CE3 . TRP B 121 ? 0.1954 0.2061 0.2394 -0.0138 0.0417  0.0281  101 TRP B CE3 
3998 C CZ2 . TRP B 121 ? 0.1956 0.1940 0.2548 0.0008  0.0633  0.0135  101 TRP B CZ2 
3999 C CZ3 . TRP B 121 ? 0.1955 0.2060 0.2359 -0.0003 0.0441  0.0271  101 TRP B CZ3 
4000 C CH2 . TRP B 121 ? 0.1879 0.1975 0.2618 0.0003  0.0515  0.0146  101 TRP B CH2 
4011 N N   . VAL B 122 ? 0.1992 0.1892 0.2068 0.0093  0.0189  0.0174  102 VAL B N   
4012 C CA  . VAL B 122 ? 0.2020 0.1682 0.2114 0.0143  0.0269  0.0170  102 VAL B CA  
4013 C C   . VAL B 122 ? 0.2081 0.1721 0.2099 0.0155  0.0357  0.0185  102 VAL B C   
4014 O O   . VAL B 122 ? 0.2246 0.2059 0.2266 0.0012  0.0180  0.0568  102 VAL B O   
4015 C CB  . VAL B 122 ? 0.2179 0.1908 0.2285 0.0238  0.0372  0.0143  102 VAL B CB  
4016 C CG1 . VAL B 122 ? 0.2524 0.1951 0.2524 0.0235  0.0753  0.0023  102 VAL B CG1 
4017 C CG2 . VAL B 122 ? 0.2182 0.2272 0.2290 0.0121  0.0445  0.0153  102 VAL B CG2 
4027 N N   . GLU B 123 ? 0.2015 0.1743 0.2063 0.0083  0.0401  0.0293  103 GLU B N   
4028 C CA  . GLU B 123 ? 0.1983 0.1756 0.2136 0.0150  0.0326  0.0186  103 GLU B CA  
4029 C C   . GLU B 123 ? 0.2133 0.1749 0.2276 0.0258  0.0542  0.0164  103 GLU B C   
4030 O O   . GLU B 123 ? 0.2427 0.1702 0.2440 0.0324  0.0356  0.0214  103 GLU B O   
4031 C CB  . GLU B 123 ? 0.2104 0.1889 0.2126 0.0115  0.0467  0.0284  103 GLU B CB  
4032 C CG  . GLU B 123 ? 0.2223 0.2016 0.2281 0.0031  0.0573  0.0216  103 GLU B CG  
4033 C CD  . GLU B 123 ? 0.2333 0.2270 0.2347 0.0136  0.0517  0.0170  103 GLU B CD  
4034 O OE1 . GLU B 123 ? 0.2393 0.2425 0.2350 0.0133  0.0631  0.0143  103 GLU B OE1 
4035 O OE2 . GLU B 123 ? 0.2231 0.2774 0.2304 0.0006  0.0530  0.0194  103 GLU B OE2 
4042 N N   . CYS B 124 ? 0.2230 0.1524 0.2156 0.0160  0.0444  0.0129  104 CYS B N   
4043 C CA  . CYS B 124 ? 0.2084 0.1499 0.2308 0.0246  0.0363  0.0161  104 CYS B CA  
4044 C C   . CYS B 124 ? 0.2218 0.1620 0.2361 0.0373  0.0529  0.0271  104 CYS B C   
4045 O O   . CYS B 124 ? 0.2254 0.1808 0.2511 0.0256  0.0325  0.0056  104 CYS B O   
4046 C CB  . CYS B 124 ? 0.2374 0.1385 0.2592 0.0114  0.0424  0.0133  104 CYS B CB  
4047 S SG  . CYS B 124 ? 0.2358 0.2071 0.2507 -0.0027 0.0514  0.0303  104 CYS B SG  
4053 N N   . ARG B 125 ? 0.2430 0.1506 0.2346 0.0257  0.0497  0.0263  105 ARG B N   
4054 C CA  . ARG B 125 ? 0.2438 0.1503 0.2421 0.0166  0.0425  0.0198  105 ARG B CA  
4055 C C   . ARG B 125 ? 0.2444 0.1398 0.2523 0.0234  0.0498  0.0072  105 ARG B C   
4056 O O   . ARG B 125 ? 0.2475 0.1571 0.2532 0.0340  0.0485  0.0178  105 ARG B O   
4057 C CB  . ARG B 125 ? 0.2616 0.1638 0.2772 -0.0074 0.0575  0.0228  105 ARG B CB  
4058 C CG  . ARG B 125 ? 0.2731 0.2181 0.2851 -0.0264 0.0571  0.0271  105 ARG B CG  
4059 C CD  . ARG B 125 ? 0.3324 0.2825 0.3142 -0.0232 0.0793  0.0191  105 ARG B CD  
4060 N NE  . ARG B 125 ? 0.3582 0.3334 0.4183 0.0048  0.0692  0.0082  105 ARG B NE  
4061 C CZ  . ARG B 125 ? 0.3313 0.3426 0.4568 -0.0077 0.0611  -0.0249 105 ARG B CZ  
4062 N NH1 . ARG B 125 ? 0.3104 0.2936 0.5096 -0.0113 0.0321  -0.0652 105 ARG B NH1 
4063 N NH2 . ARG B 125 ? 0.3204 0.3632 0.3863 -0.0227 0.0749  -0.0481 105 ARG B NH2 
4077 N N   . GLY B 126 ? 0.2246 0.1682 0.2468 0.0147  0.0464  -0.0139 106 GLY B N   
4078 C CA  . GLY B 126 ? 0.2421 0.1855 0.2424 0.0185  0.0379  -0.0168 106 GLY B CA  
4079 C C   . GLY B 126 ? 0.2477 0.1605 0.2260 0.0304  0.0309  0.0028  106 GLY B C   
4080 O O   . GLY B 126 ? 0.2349 0.1775 0.2578 0.0245  0.0270  -0.0024 106 GLY B O   
4084 N N   . GLU B 127 ? 0.2467 0.1673 0.2270 0.0250  0.0327  -0.0154 107 GLU B N   
4085 C CA  . GLU B 127 ? 0.2622 0.1676 0.2342 0.0270  0.0331  -0.0073 107 GLU B CA  
4086 C C   . GLU B 127 ? 0.2762 0.1604 0.2334 0.0196  0.0457  -0.0063 107 GLU B C   
4087 O O   . GLU B 127 ? 0.2675 0.1658 0.2536 0.0210  0.0345  -0.0091 107 GLU B O   
4088 C CB  . GLU B 127 ? 0.2805 0.1536 0.2674 0.0125  0.0258  0.0094  107 GLU B CB  
4089 C CG  . GLU B 127 ? 0.3224 0.1740 0.2922 0.0129  0.0537  0.0131  107 GLU B CG  
4090 C CD  . GLU B 127 ? 0.3787 0.2015 0.3403 0.0385  0.0918  0.0269  107 GLU B CD  
4091 O OE1 . GLU B 127 ? 0.3742 0.1930 0.3816 0.0279  0.0857  0.0084  107 GLU B OE1 
4092 O OE2 . GLU B 127 ? 0.3884 0.2078 0.3456 0.0318  0.0772  0.0027  107 GLU B OE2 
4099 N N   . GLY B 128 ? 0.2800 0.1773 0.2249 0.0072  0.0249  -0.0155 108 GLY B N   
4100 C CA  . GLY B 128 ? 0.2927 0.1802 0.2168 0.0182  0.0270  -0.0165 108 GLY B CA  
4101 C C   . GLY B 128 ? 0.2938 0.1946 0.2281 0.0238  0.0403  -0.0090 108 GLY B C   
4102 O O   . GLY B 128 ? 0.2687 0.2176 0.2595 0.0200  0.0403  -0.0010 108 GLY B O   
4106 N N   . ALA B 129 ? 0.3316 0.2071 0.2380 0.0294  0.0375  -0.0398 109 ALA B N   
4107 C CA  . ALA B 129 ? 0.3289 0.2292 0.2262 0.0206  0.0281  -0.0226 109 ALA B CA  
4108 C C   . ALA B 129 ? 0.2934 0.2393 0.2302 -0.0002 0.0162  -0.0080 109 ALA B C   
4109 O O   . ALA B 129 ? 0.2833 0.2352 0.2847 0.0037  0.0069  -0.0017 109 ALA B O   
4110 C CB  . ALA B 129 ? 0.3994 0.2569 0.2383 0.0112  0.0394  -0.0257 109 ALA B CB  
4116 N N   . ILE B 130 ? 0.2742 0.2528 0.2319 -0.0057 0.0192  0.0258  110 ILE B N   
4117 C CA  . ILE B 130 ? 0.2733 0.2484 0.2374 0.0076  0.0311  0.0334  110 ILE B CA  
4118 C C   . ILE B 130 ? 0.2601 0.2736 0.2539 0.0004  0.0271  0.0254  110 ILE B C   
4119 O O   . ILE B 130 ? 0.2690 0.3040 0.2582 -0.0013 0.0343  0.0163  110 ILE B O   
4120 C CB  . ILE B 130 ? 0.2757 0.2530 0.2438 -0.0035 0.0355  0.0220  110 ILE B CB  
4121 C CG1 . ILE B 130 ? 0.2787 0.2472 0.2620 0.0044  0.0612  0.0193  110 ILE B CG1 
4122 C CG2 . ILE B 130 ? 0.3047 0.2779 0.2729 0.0039  0.0250  0.0131  110 ILE B CG2 
4123 C CD1 . ILE B 130 ? 0.2875 0.2488 0.2731 0.0128  0.0295  0.0118  110 ILE B CD1 
4135 N N   . VAL B 131 ? 0.2636 0.2945 0.2533 -0.0072 0.0358  0.0389  111 VAL B N   
4136 C CA  . VAL B 131 ? 0.2763 0.3112 0.2561 0.0166  0.0423  0.0392  111 VAL B CA  
4137 C C   . VAL B 131 ? 0.2939 0.3116 0.2638 0.0047  0.0229  0.0111  111 VAL B C   
4138 O O   . VAL B 131 ? 0.2893 0.3152 0.3438 0.0115  0.0362  0.0666  111 VAL B O   
4139 C CB  . VAL B 131 ? 0.3141 0.3231 0.2736 0.0322  0.0598  0.0376  111 VAL B CB  
4140 C CG1 . VAL B 131 ? 0.3583 0.3374 0.2924 0.0542  0.0690  0.0223  111 VAL B CG1 
4141 C CG2 . VAL B 131 ? 0.3366 0.3426 0.2986 0.0371  0.0542  0.0025  111 VAL B CG2 
4151 N N   . PHE B 132 ? 0.2916 0.3095 0.2347 0.0134  0.0479  -0.0126 112 PHE B N   
4152 C CA  . PHE B 132 ? 0.2972 0.2906 0.2619 0.0182  0.0342  -0.0272 112 PHE B CA  
4153 C C   . PHE B 132 ? 0.2966 0.2776 0.2664 -0.0019 0.0510  -0.0130 112 PHE B C   
4154 O O   . PHE B 132 ? 0.3335 0.3208 0.2498 -0.0345 0.0077  0.0306  112 PHE B O   
4155 C CB  . PHE B 132 ? 0.3237 0.3099 0.3303 0.0169  0.0822  -0.0425 112 PHE B CB  
4156 C CG  . PHE B 132 ? 0.2934 0.3288 0.3532 0.0021  0.0774  -0.0450 112 PHE B CG  
4157 C CD1 . PHE B 132 ? 0.3763 0.3524 0.3568 -0.0643 0.0300  -0.0681 112 PHE B CD1 
4158 C CD2 . PHE B 132 ? 0.3708 0.3974 0.4729 -0.0133 0.0404  -0.0932 112 PHE B CD2 
4159 C CE1 . PHE B 132 ? 0.4241 0.3780 0.4058 -0.0849 0.0754  -0.0885 112 PHE B CE1 
4160 C CE2 . PHE B 132 ? 0.4163 0.4083 0.5052 0.0039  0.0628  -0.1276 112 PHE B CE2 
4161 C CZ  . PHE B 132 ? 0.4290 0.3946 0.4709 -0.0236 0.0947  -0.1235 112 PHE B CZ  
4171 N N   . PRO B 133 ? 0.3081 0.2774 0.3097 -0.0137 0.0633  0.0151  113 PRO B N   
4172 C CA  . PRO B 133 ? 0.3129 0.3166 0.3109 0.0074  0.0775  0.0439  113 PRO B CA  
4173 C C   . PRO B 133 ? 0.2952 0.3125 0.2911 0.0259  0.0443  0.0502  113 PRO B C   
4174 O O   . PRO B 133 ? 0.3057 0.3169 0.3324 0.0324  0.0677  0.0409  113 PRO B O   
4175 C CB  . PRO B 133 ? 0.2774 0.3375 0.3700 -0.0023 0.0682  0.0483  113 PRO B CB  
4176 C CG  . PRO B 133 ? 0.3539 0.3352 0.3642 -0.0533 0.0754  0.0350  113 PRO B CG  
4177 C CD  . PRO B 133 ? 0.3513 0.3097 0.3591 -0.0510 0.0759  0.0124  113 PRO B CD  
4185 N N   . GLY B 134 ? 0.3143 0.3442 0.3032 -0.0064 0.0345  0.0716  114 GLY B N   
4186 C CA  . GLY B 134 ? 0.3482 0.3643 0.3126 -0.0165 0.0142  0.0736  114 GLY B CA  
4187 C C   . GLY B 134 ? 0.3347 0.3780 0.2959 -0.0268 0.0252  0.0499  114 GLY B C   
4188 O O   . GLY B 134 ? 0.3412 0.4060 0.3298 -0.0130 0.0011  0.0887  114 GLY B O   
4192 N N   . TYR B 135 ? 0.3118 0.3524 0.2525 -0.0368 0.0101  0.0365  115 TYR B N   
4193 C CA  . TYR B 135 ? 0.3066 0.3461 0.2560 -0.0188 0.0033  0.0519  115 TYR B CA  
4194 C C   . TYR B 135 ? 0.3357 0.3300 0.2565 -0.0340 0.0041  0.0564  115 TYR B C   
4195 O O   . TYR B 135 ? 0.3447 0.3181 0.3188 -0.0021 0.0363  0.0218  115 TYR B O   
4196 C CB  . TYR B 135 ? 0.3083 0.3300 0.2364 -0.0075 0.0000  0.0511  115 TYR B CB  
4197 C CG  . TYR B 135 ? 0.2834 0.3125 0.2316 -0.0122 0.0165  0.0355  115 TYR B CG  
4198 C CD1 . TYR B 135 ? 0.2873 0.3093 0.2430 -0.0101 0.0375  0.0334  115 TYR B CD1 
4199 C CD2 . TYR B 135 ? 0.2939 0.3132 0.2235 -0.0349 0.0319  -0.0150 115 TYR B CD2 
4200 C CE1 . TYR B 135 ? 0.2890 0.3101 0.2410 0.0031  0.0436  0.0288  115 TYR B CE1 
4201 C CE2 . TYR B 135 ? 0.2981 0.3283 0.2158 -0.0141 0.0248  -0.0221 115 TYR B CE2 
4202 C CZ  . TYR B 135 ? 0.2879 0.3217 0.2411 -0.0090 0.0310  -0.0107 115 TYR B CZ  
4203 O OH  . TYR B 135 ? 0.2855 0.3390 0.2884 0.0053  0.0351  -0.0114 115 TYR B OH  
4213 N N   . PRO B 136 ? 0.3324 0.3262 0.2536 -0.0377 0.0040  0.0132  116 PRO B N   
4214 C CA  . PRO B 136 ? 0.3589 0.3011 0.2690 -0.0347 -0.0037 -0.0230 116 PRO B CA  
4215 C C   . PRO B 136 ? 0.3536 0.2896 0.2559 -0.0179 0.0162  0.0064  116 PRO B C   
4216 O O   . PRO B 136 ? 0.3692 0.2673 0.2593 -0.0119 0.0241  -0.0295 116 PRO B O   
4217 C CB  . PRO B 136 ? 0.3758 0.3197 0.3046 -0.0424 0.0005  -0.0258 116 PRO B CB  
4218 C CG  . PRO B 136 ? 0.3738 0.3535 0.3644 -0.0480 0.0015  0.0137  116 PRO B CG  
4219 C CD  . PRO B 136 ? 0.3380 0.3518 0.2876 -0.0395 0.0001  0.0376  116 PRO B CD  
4227 N N   . ARG B 137 ? 0.3920 0.2991 0.2835 0.0174  0.0263  -0.0078 117 ARG B N   
4228 C CA  . ARG B 137 ? 0.3794 0.3085 0.3239 0.0204  0.0322  -0.0193 117 ARG B CA  
4229 C C   . ARG B 137 ? 0.3878 0.3010 0.3231 -0.0266 0.0161  0.0223  117 ARG B C   
4230 O O   . ARG B 137 ? 0.4147 0.2986 0.3574 -0.0460 -0.0087 0.0252  117 ARG B O   
4231 C CB  . ARG B 137 ? 0.4207 0.3433 0.4229 0.0526  0.0206  -0.0648 117 ARG B CB  
4232 C CG  . ARG B 137 ? 0.4915 0.3859 0.4995 0.0761  0.0269  -0.1129 117 ARG B CG  
4233 C CD  . ARG B 137 ? 0.5418 0.4222 0.5618 0.0939  0.0319  -0.1252 117 ARG B CD  
4234 N NE  . ARG B 137 ? 0.5888 0.4602 0.6069 0.0841  0.0536  -0.1624 117 ARG B NE  
4235 C CZ  . ARG B 137 ? 0.5946 0.4837 0.6410 0.0904  0.0264  -0.1699 117 ARG B CZ  
4236 N NH1 . ARG B 137 ? 0.6143 0.5016 0.6809 0.0795  0.0274  -0.1653 117 ARG B NH1 
4237 N NH2 . ARG B 137 ? 0.5969 0.4722 0.6183 0.1001  0.0071  -0.1977 117 ARG B NH2 
4251 N N   . GLY B 138 ? 0.3687 0.3069 0.3164 -0.0459 0.0114  0.0548  118 GLY B N   
4252 C CA  . GLY B 138 ? 0.3767 0.3072 0.3292 -0.0416 0.0091  0.0461  118 GLY B CA  
4253 C C   . GLY B 138 ? 0.3322 0.2519 0.2907 -0.0363 0.0056  0.0037  118 GLY B C   
4254 O O   . GLY B 138 ? 0.3198 0.2787 0.3224 -0.0355 0.0164  0.0384  118 GLY B O   
4258 N N   A GLN B 139 ? 0.3333 0.2135 0.2661 -0.0359 0.0127  -0.0191 119 GLN B N   
4259 N N   B GLN B 139 ? 0.3501 0.2395 0.3049 -0.0322 0.0174  -0.0207 119 GLN B N   
4260 C CA  A GLN B 139 ? 0.3247 0.1685 0.2763 -0.0009 -0.0134 -0.0197 119 GLN B CA  
4261 C CA  B GLN B 139 ? 0.3616 0.2251 0.3346 -0.0142 0.0172  -0.0323 119 GLN B CA  
4262 C C   A GLN B 139 ? 0.3110 0.1935 0.3046 0.0042  0.0278  -0.0355 119 GLN B C   
4263 C C   B GLN B 139 ? 0.3373 0.2273 0.3203 -0.0059 0.0258  -0.0395 119 GLN B C   
4264 O O   A GLN B 139 ? 0.2945 0.2388 0.4255 0.0044  0.0124  -0.0711 119 GLN B O   
4265 O O   B GLN B 139 ? 0.3397 0.2506 0.3766 -0.0161 0.0347  -0.0696 119 GLN B O   
4266 C CB  A GLN B 139 ? 0.4264 0.1683 0.3224 0.0012  0.0104  -0.0109 119 GLN B CB  
4267 C CB  B GLN B 139 ? 0.4289 0.2219 0.3887 -0.0084 0.0432  -0.0415 119 GLN B CB  
4268 C CG  A GLN B 139 ? 0.4653 0.2038 0.3805 0.0019  -0.0532 0.0350  119 GLN B CG  
4269 C CG  B GLN B 139 ? 0.4700 0.2297 0.4252 -0.0010 0.0526  -0.0479 119 GLN B CG  
4270 C CD  A GLN B 139 ? 0.4927 0.2323 0.4604 -0.0229 -0.1037 0.0654  119 GLN B CD  
4271 C CD  B GLN B 139 ? 0.5324 0.2787 0.5104 -0.0063 0.0731  -0.0316 119 GLN B CD  
4272 O OE1 A GLN B 139 ? 0.5107 0.2682 0.5383 -0.0043 -0.1072 0.0763  119 GLN B OE1 
4273 O OE1 B GLN B 139 ? 0.5408 0.3057 0.5565 -0.0099 0.1132  -0.0230 119 GLN B OE1 
4274 N NE2 A GLN B 139 ? 0.5150 0.2223 0.4488 -0.0931 -0.1519 0.0692  119 GLN B NE2 
4275 N NE2 B GLN B 139 ? 0.5581 0.2997 0.5538 -0.0031 0.0726  -0.0209 119 GLN B NE2 
4292 N N   . TYR B 140 ? 0.2901 0.2123 0.2643 -0.0032 0.0141  -0.0254 120 TYR B N   
4293 C CA  . TYR B 140 ? 0.2626 0.1967 0.2561 0.0077  0.0165  -0.0282 120 TYR B CA  
4294 C C   . TYR B 140 ? 0.2559 0.2034 0.2605 0.0116  0.0160  -0.0261 120 TYR B C   
4295 O O   . TYR B 140 ? 0.2541 0.2481 0.2655 0.0158  0.0223  -0.0188 120 TYR B O   
4296 C CB  . TYR B 140 ? 0.3013 0.1862 0.2708 0.0102  0.0231  -0.0073 120 TYR B CB  
4297 C CG  . TYR B 140 ? 0.2854 0.1785 0.2544 0.0087  0.0330  -0.0008 120 TYR B CG  
4298 C CD1 . TYR B 140 ? 0.2454 0.1709 0.2677 -0.0033 0.0105  0.0031  120 TYR B CD1 
4299 C CD2 . TYR B 140 ? 0.2731 0.1854 0.2679 -0.0040 0.0172  0.0091  120 TYR B CD2 
4300 C CE1 . TYR B 140 ? 0.2452 0.1684 0.2708 0.0104  -0.0125 -0.0077 120 TYR B CE1 
4301 C CE2 . TYR B 140 ? 0.2731 0.1648 0.3055 0.0007  0.0054  0.0151  120 TYR B CE2 
4302 C CZ  . TYR B 140 ? 0.2747 0.1630 0.2693 0.0198  0.0153  -0.0063 120 TYR B CZ  
4303 O OH  . TYR B 140 ? 0.2741 0.1820 0.2942 0.0192  0.0232  -0.0057 120 TYR B OH  
4314 N N   . ARG B 141 ? 0.2586 0.1844 0.2370 0.0100  0.0410  -0.0248 121 ARG B N   
4315 C CA  . ARG B 141 ? 0.2825 0.1606 0.2466 0.0022  0.0424  -0.0275 121 ARG B CA  
4316 C C   . ARG B 141 ? 0.2713 0.1681 0.2404 0.0135  0.0342  -0.0263 121 ARG B C   
4317 O O   . ARG B 141 ? 0.2590 0.2218 0.2672 0.0318  0.0097  -0.0228 121 ARG B O   
4318 C CB  . ARG B 141 ? 0.3067 0.1490 0.2834 -0.0003 0.0411  -0.0080 121 ARG B CB  
4319 C CG  . ARG B 141 ? 0.3171 0.1626 0.2978 -0.0033 0.0482  -0.0079 121 ARG B CG  
4320 C CD  . ARG B 141 ? 0.2989 0.2099 0.3669 -0.0150 0.0199  0.0054  121 ARG B CD  
4321 N NE  . ARG B 141 ? 0.3200 0.2441 0.3705 -0.0218 0.0525  0.0426  121 ARG B NE  
4322 C CZ  . ARG B 141 ? 0.3234 0.2576 0.3656 -0.0102 0.0398  0.0464  121 ARG B CZ  
4323 N NH1 . ARG B 141 ? 0.3187 0.2372 0.4083 0.0161  0.0453  0.0397  121 ARG B NH1 
4324 N NH2 . ARG B 141 ? 0.3900 0.2874 0.3947 -0.0108 0.0609  0.0547  121 ARG B NH2 
4338 N N   . ASN B 142 ? 0.2614 0.1490 0.2371 0.0085  0.0280  -0.0276 122 ASN B N   
4339 C CA  . ASN B 142 ? 0.2374 0.1433 0.2348 0.0160  0.0157  -0.0136 122 ASN B CA  
4340 C C   . ASN B 142 ? 0.2307 0.1422 0.2431 0.0103  0.0266  -0.0049 122 ASN B C   
4341 O O   . ASN B 142 ? 0.2547 0.1666 0.2428 0.0295  0.0316  -0.0052 122 ASN B O   
4342 C CB  . ASN B 142 ? 0.2508 0.1549 0.2521 0.0268  0.0187  -0.0012 122 ASN B CB  
4343 C CG  . ASN B 142 ? 0.2442 0.2015 0.2678 0.0289  0.0176  -0.0154 122 ASN B CG  
4344 O OD1 . ASN B 142 ? 0.2373 0.2456 0.2743 0.0406  0.0234  -0.0116 122 ASN B OD1 
4345 N ND2 . ASN B 142 ? 0.2540 0.1822 0.2646 0.0353  0.0140  -0.0168 122 ASN B ND2 
4352 N N   . HIS B 143 ? 0.2577 0.1549 0.2198 0.0154  0.0423  -0.0114 123 HIS B N   
4353 C CA  . HIS B 143 ? 0.2331 0.1499 0.2372 0.0069  0.0491  0.0052  123 HIS B CA  
4354 C C   . HIS B 143 ? 0.2053 0.1331 0.2496 0.0136  0.0429  0.0295  123 HIS B C   
4355 O O   . HIS B 143 ? 0.2126 0.1608 0.2726 -0.0065 0.0304  0.0390  123 HIS B O   
4356 C CB  . HIS B 143 ? 0.2375 0.1739 0.2212 -0.0080 0.0508  0.0020  123 HIS B CB  
4357 C CG  . HIS B 143 ? 0.2293 0.2008 0.2261 -0.0055 0.0543  -0.0083 123 HIS B CG  
4358 N ND1 . HIS B 143 ? 0.2457 0.2147 0.2568 0.0145  0.0327  -0.0384 123 HIS B ND1 
4359 C CD2 . HIS B 143 ? 0.2623 0.2227 0.2524 -0.0093 0.0540  0.0227  123 HIS B CD2 
4360 C CE1 . HIS B 143 ? 0.2467 0.2384 0.2651 -0.0053 0.0415  -0.0335 123 HIS B CE1 
4361 N NE2 . HIS B 143 ? 0.2255 0.2609 0.2445 -0.0172 0.0237  -0.0020 123 HIS B NE2 
4369 N N   . PHE B 144 ? 0.2125 0.1353 0.2287 0.0131  0.0232  0.0152  124 PHE B N   
4370 C CA  . PHE B 144 ? 0.2172 0.1429 0.2282 0.0157  0.0296  0.0077  124 PHE B CA  
4371 C C   . PHE B 144 ? 0.2046 0.1321 0.2451 0.0146  0.0381  0.0069  124 PHE B C   
4372 O O   . PHE B 144 ? 0.2413 0.1474 0.2388 0.0095  0.0308  0.0181  124 PHE B O   
4373 C CB  . PHE B 144 ? 0.2147 0.1713 0.2325 0.0274  0.0559  0.0170  124 PHE B CB  
4374 C CG  . PHE B 144 ? 0.2165 0.1645 0.2393 0.0202  0.0572  0.0065  124 PHE B CG  
4375 C CD1 . PHE B 144 ? 0.2446 0.1849 0.2563 0.0270  0.0740  -0.0110 124 PHE B CD1 
4376 C CD2 . PHE B 144 ? 0.2516 0.1862 0.2378 0.0195  0.0720  0.0063  124 PHE B CD2 
4377 C CE1 . PHE B 144 ? 0.2216 0.2192 0.2811 0.0253  0.0685  -0.0210 124 PHE B CE1 
4378 C CE2 . PHE B 144 ? 0.2716 0.2083 0.2278 0.0583  0.0604  -0.0138 124 PHE B CE2 
4379 C CZ  . PHE B 144 ? 0.2464 0.2142 0.2482 0.0336  0.0515  -0.0216 124 PHE B CZ  
4389 N N   . LEU B 145 ? 0.1902 0.1552 0.2086 0.0191  0.0331  0.0215  125 LEU B N   
4390 C CA  . LEU B 145 ? 0.2026 0.1724 0.1986 -0.0023 0.0367  0.0233  125 LEU B CA  
4391 C C   . LEU B 145 ? 0.2181 0.1615 0.1918 0.0017  0.0431  0.0251  125 LEU B C   
4392 O O   . LEU B 145 ? 0.1989 0.2019 0.2272 -0.0017 0.0357  0.0472  125 LEU B O   
4393 C CB  . LEU B 145 ? 0.2261 0.1954 0.2010 0.0050  0.0752  0.0087  125 LEU B CB  
4394 C CG  . LEU B 145 ? 0.2409 0.2387 0.2434 0.0261  0.0588  -0.0010 125 LEU B CG  
4395 C CD1 . LEU B 145 ? 0.2459 0.2868 0.2479 0.0355  0.0360  -0.0077 125 LEU B CD1 
4396 C CD2 . LEU B 145 ? 0.2923 0.2358 0.2860 0.0441  0.0908  0.0349  125 LEU B CD2 
4408 N N   . HIS B 146 ? 0.2141 0.1678 0.1994 -0.0116 0.0242  0.0267  126 HIS B N   
4409 C CA  . HIS B 146 ? 0.2147 0.1791 0.2099 -0.0143 0.0395  0.0009  126 HIS B CA  
4410 C C   . HIS B 146 ? 0.1972 0.1775 0.2129 -0.0095 0.0317  0.0263  126 HIS B C   
4411 O O   . HIS B 146 ? 0.2375 0.1812 0.2084 -0.0116 0.0384  0.0278  126 HIS B O   
4412 C CB  . HIS B 146 ? 0.2183 0.1844 0.2197 -0.0075 0.0537  -0.0081 126 HIS B CB  
4413 C CG  . HIS B 146 ? 0.2443 0.1925 0.2444 -0.0143 0.0603  0.0039  126 HIS B CG  
4414 N ND1 . HIS B 146 ? 0.2957 0.2163 0.2474 -0.0151 0.0840  -0.0105 126 HIS B ND1 
4415 C CD2 . HIS B 146 ? 0.2491 0.2140 0.2484 0.0078  0.0608  -0.0092 126 HIS B CD2 
4416 C CE1 . HIS B 146 ? 0.3061 0.1848 0.2515 -0.0127 0.0790  -0.0203 126 HIS B CE1 
4417 N NE2 . HIS B 146 ? 0.2594 0.1969 0.2656 0.0023  0.0563  -0.0159 126 HIS B NE2 
4425 N N   . SER B 147 ? 0.2065 0.1816 0.2079 -0.0145 0.0380  0.0191  127 SER B N   
4426 C CA  . SER B 147 ? 0.1945 0.1877 0.2106 -0.0207 0.0383  0.0048  127 SER B CA  
4427 C C   . SER B 147 ? 0.1928 0.1817 0.2453 -0.0061 0.0483  0.0037  127 SER B C   
4428 O O   . SER B 147 ? 0.1926 0.2137 0.2269 -0.0114 0.0444  0.0141  127 SER B O   
4429 C CB  . SER B 147 ? 0.1982 0.1948 0.2427 -0.0140 0.0429  -0.0047 127 SER B CB  
4430 O OG  . SER B 147 ? 0.1993 0.1992 0.2416 -0.0019 0.0430  -0.0190 127 SER B OG  
4436 N N   . PHE B 148 ? 0.1806 0.1863 0.2318 -0.0091 0.0432  -0.0003 128 PHE B N   
4437 C CA  . PHE B 148 ? 0.1917 0.1896 0.2368 -0.0165 0.0411  -0.0041 128 PHE B CA  
4438 C C   . PHE B 148 ? 0.1770 0.2223 0.2575 -0.0215 0.0476  0.0002  128 PHE B C   
4439 O O   . PHE B 148 ? 0.2172 0.2571 0.2350 -0.0253 0.0320  0.0020  128 PHE B O   
4440 C CB  . PHE B 148 ? 0.2154 0.2121 0.2255 -0.0065 0.0386  0.0061  128 PHE B CB  
4441 C CG  . PHE B 148 ? 0.1838 0.2117 0.2340 0.0003  0.0500  0.0027  128 PHE B CG  
4442 C CD1 . PHE B 148 ? 0.2092 0.1990 0.2436 0.0124  0.0509  0.0136  128 PHE B CD1 
4443 C CD2 . PHE B 148 ? 0.2127 0.2129 0.2583 -0.0123 0.0665  -0.0055 128 PHE B CD2 
4444 C CE1 . PHE B 148 ? 0.2130 0.1964 0.2553 0.0076  0.0400  0.0057  128 PHE B CE1 
4445 C CE2 . PHE B 148 ? 0.2584 0.2000 0.2572 -0.0134 0.0615  0.0013  128 PHE B CE2 
4446 C CZ  . PHE B 148 ? 0.2430 0.2039 0.2271 -0.0066 0.0310  0.0058  128 PHE B CZ  
4456 N N   . ARG B 149 ? 0.1904 0.2193 0.2570 -0.0295 0.0405  -0.0136 129 ARG B N   
4457 C CA  . ARG B 149 ? 0.2026 0.2256 0.2848 -0.0294 0.0577  -0.0260 129 ARG B CA  
4458 C C   . ARG B 149 ? 0.1886 0.2355 0.2734 -0.0347 0.0560  -0.0040 129 ARG B C   
4459 O O   . ARG B 149 ? 0.2167 0.2743 0.2533 -0.0272 0.0640  0.0043  129 ARG B O   
4460 C CB  . ARG B 149 ? 0.2361 0.2180 0.2905 -0.0087 0.0635  -0.0289 129 ARG B CB  
4461 C CG  . ARG B 149 ? 0.2274 0.2303 0.3171 -0.0035 0.0595  -0.0237 129 ARG B CG  
4462 C CD  . ARG B 149 ? 0.2379 0.2393 0.3273 -0.0180 0.0565  -0.0277 129 ARG B CD  
4463 N NE  . ARG B 149 ? 0.3110 0.2386 0.3589 -0.0301 0.0567  -0.0461 129 ARG B NE  
4464 C CZ  . ARG B 149 ? 0.3569 0.2506 0.4113 -0.0211 0.0497  -0.0406 129 ARG B CZ  
4465 N NH1 . ARG B 149 ? 0.4213 0.2414 0.4395 0.0108  0.0346  -0.0289 129 ARG B NH1 
4466 N NH2 . ARG B 149 ? 0.3945 0.2751 0.4217 -0.0121 0.0540  -0.0480 129 ARG B NH2 
4480 N N   . PHE B 150 ? 0.1873 0.2459 0.2733 -0.0275 0.0374  -0.0081 130 PHE B N   
4481 C CA  . PHE B 150 ? 0.2038 0.2627 0.2791 -0.0390 0.0370  -0.0208 130 PHE B CA  
4482 C C   . PHE B 150 ? 0.2251 0.2841 0.3092 -0.0408 0.0550  -0.0359 130 PHE B C   
4483 O O   . PHE B 150 ? 0.2474 0.2892 0.3417 -0.0544 0.0701  -0.0561 130 PHE B O   
4484 C CB  . PHE B 150 ? 0.2093 0.2804 0.2723 -0.0108 0.0141  -0.0089 130 PHE B CB  
4485 C CG  . PHE B 150 ? 0.2224 0.2768 0.2557 -0.0187 0.0260  -0.0081 130 PHE B CG  
4486 C CD1 . PHE B 150 ? 0.2219 0.2791 0.2755 -0.0316 0.0285  0.0084  130 PHE B CD1 
4487 C CD2 . PHE B 150 ? 0.2451 0.2637 0.2587 -0.0112 0.0302  -0.0157 130 PHE B CD2 
4488 C CE1 . PHE B 150 ? 0.2139 0.2824 0.2801 -0.0210 0.0126  0.0287  130 PHE B CE1 
4489 C CE2 . PHE B 150 ? 0.2774 0.2646 0.2538 -0.0044 0.0531  -0.0078 130 PHE B CE2 
4490 C CZ  . PHE B 150 ? 0.2479 0.2875 0.2651 -0.0259 0.0130  0.0220  130 PHE B CZ  
4500 N N   A GLU B 151 ? 0.2225 0.2947 0.3076 -0.0630 0.0575  -0.0384 131 GLU B N   
4501 N N   B GLU B 151 ? 0.2391 0.3018 0.3247 -0.0496 0.0555  -0.0357 131 GLU B N   
4502 C CA  A GLU B 151 ? 0.2293 0.2909 0.3360 -0.0722 0.0460  -0.0263 131 GLU B CA  
4503 C CA  B GLU B 151 ? 0.2647 0.3112 0.3624 -0.0496 0.0518  -0.0278 131 GLU B CA  
4504 C C   A GLU B 151 ? 0.2105 0.3135 0.3476 -0.0592 0.0316  -0.0085 131 GLU B C   
4505 C C   B GLU B 151 ? 0.2399 0.3195 0.3599 -0.0569 0.0311  -0.0223 131 GLU B C   
4506 O O   A GLU B 151 ? 0.2206 0.3093 0.3256 -0.0440 0.0357  0.0099  131 GLU B O   
4507 O O   B GLU B 151 ? 0.2543 0.3165 0.3463 -0.0613 0.0354  -0.0271 131 GLU B O   
4508 C CB  A GLU B 151 ? 0.2607 0.2812 0.3957 -0.0823 0.0384  -0.0229 131 GLU B CB  
4509 C CB  B GLU B 151 ? 0.3193 0.3217 0.4320 -0.0364 0.0633  -0.0154 131 GLU B CB  
4510 C CG  A GLU B 151 ? 0.3173 0.2998 0.4659 -0.0986 0.0188  -0.0060 131 GLU B CG  
4511 C CG  B GLU B 151 ? 0.3794 0.3444 0.5130 -0.0353 0.0804  0.0088  131 GLU B CG  
4512 C CD  A GLU B 151 ? 0.4070 0.3253 0.5364 -0.0884 0.0471  0.0315  131 GLU B CD  
4513 C CD  B GLU B 151 ? 0.4430 0.3652 0.5629 -0.0336 0.1065  0.0457  131 GLU B CD  
4514 O OE1 A GLU B 151 ? 0.4950 0.3509 0.5752 -0.0656 0.0649  0.0357  131 GLU B OE1 
4515 O OE1 B GLU B 151 ? 0.4877 0.3742 0.5976 -0.0429 0.1068  0.0545  131 GLU B OE1 
4516 O OE2 A GLU B 151 ? 0.4522 0.3306 0.5457 -0.0618 0.0584  0.0581  131 GLU B OE2 
4517 O OE2 B GLU B 151 ? 0.4137 0.3601 0.5633 -0.0108 0.1351  0.0709  131 GLU B OE2 
4530 N N   . ASN B 152 ? 0.2469 0.3272 0.3701 -0.0454 0.0068  -0.0232 132 ASN B N   
4531 C CA  . ASN B 152 ? 0.2392 0.3804 0.4452 -0.0380 0.0027  -0.0311 132 ASN B CA  
4532 C C   . ASN B 152 ? 0.2021 0.3778 0.4015 -0.0328 0.0033  -0.0392 132 ASN B C   
4533 O O   . ASN B 152 ? 0.2268 0.4210 0.4553 -0.0056 0.0145  -0.0415 132 ASN B O   
4534 C CB  . ASN B 152 ? 0.2490 0.4352 0.5336 -0.0419 0.0520  -0.0526 132 ASN B CB  
4535 C CG  . ASN B 152 ? 0.3408 0.4987 0.6118 -0.0514 0.1627  -0.0874 132 ASN B CG  
4536 O OD1 . ASN B 152 ? 0.3405 0.5400 0.6338 -0.0914 0.1119  -0.1185 132 ASN B OD1 
4537 N ND2 . ASN B 152 ? 0.4191 0.4856 0.6617 -0.0535 0.2870  -0.1145 132 ASN B ND2 
4545 N N   . GLY B 153 ? 0.2641 0.3595 0.3506 -0.0472 -0.0201 -0.0206 133 GLY B N   
4546 C CA  . GLY B 153 ? 0.2911 0.3635 0.3342 -0.0339 0.0202  -0.0109 133 GLY B CA  
4547 C C   . GLY B 153 ? 0.2426 0.3374 0.2733 -0.0210 0.0285  -0.0114 133 GLY B C   
4548 O O   . GLY B 153 ? 0.2224 0.3501 0.2743 -0.0081 0.0325  0.0201  133 GLY B O   
4552 N N   . LEU B 154 ? 0.2010 0.3343 0.2671 -0.0289 0.0358  0.0058  134 LEU B N   
4553 C CA  . LEU B 154 ? 0.1792 0.3071 0.2776 -0.0336 0.0229  0.0150  134 LEU B CA  
4554 C C   . LEU B 154 ? 0.1758 0.2775 0.2832 -0.0467 0.0254  0.0077  134 LEU B C   
4555 O O   . LEU B 154 ? 0.2037 0.2692 0.2920 -0.0342 0.0522  -0.0253 134 LEU B O   
4556 C CB  . LEU B 154 ? 0.1970 0.3278 0.2773 -0.0013 0.0482  0.0210  134 LEU B CB  
4557 C CG  . LEU B 154 ? 0.2059 0.3650 0.2964 -0.0221 0.0521  0.0031  134 LEU B CG  
4558 C CD1 . LEU B 154 ? 0.2110 0.4389 0.3040 -0.0307 0.0575  0.0134  134 LEU B CD1 
4559 C CD2 . LEU B 154 ? 0.2200 0.3584 0.3235 0.0407  0.0278  -0.0267 134 LEU B CD2 
4571 N N   . ILE B 155 ? 0.1657 0.2643 0.2728 -0.0333 0.0496  0.0092  135 ILE B N   
4572 C CA  . ILE B 155 ? 0.1714 0.2524 0.2808 -0.0426 0.0577  0.0123  135 ILE B CA  
4573 C C   . ILE B 155 ? 0.1925 0.2632 0.2480 -0.0435 0.0730  -0.0038 135 ILE B C   
4574 O O   . ILE B 155 ? 0.2084 0.2726 0.2541 -0.0267 0.0776  0.0100  135 ILE B O   
4575 C CB  . ILE B 155 ? 0.1813 0.2435 0.2574 -0.0311 0.0604  0.0096  135 ILE B CB  
4576 C CG1 . ILE B 155 ? 0.1974 0.2411 0.2667 -0.0278 0.0336  0.0075  135 ILE B CG1 
4577 C CG2 . ILE B 155 ? 0.2008 0.2568 0.2627 -0.0358 0.0538  0.0114  135 ILE B CG2 
4578 C CD1 . ILE B 155 ? 0.2125 0.2384 0.2823 -0.0111 0.0593  0.0162  135 ILE B CD1 
4590 N N   . LYS B 156 ? 0.2083 0.2628 0.2493 -0.0307 0.0550  0.0012  136 LYS B N   
4591 C CA  . LYS B 156 ? 0.2306 0.2792 0.2676 -0.0385 0.0504  0.0332  136 LYS B CA  
4592 C C   . LYS B 156 ? 0.2122 0.2534 0.2699 -0.0352 0.0497  0.0080  136 LYS B C   
4593 O O   . LYS B 156 ? 0.2222 0.2482 0.2961 -0.0381 0.0532  0.0362  136 LYS B O   
4612 N N   . GLU B 157 ? 0.2135 0.2175 0.2659 -0.0300 0.0528  0.0076  137 GLU B N   
4613 C CA  . GLU B 157 ? 0.2002 0.2037 0.2664 -0.0170 0.0570  0.0082  137 GLU B CA  
4614 C C   . GLU B 157 ? 0.2001 0.2068 0.2389 -0.0252 0.0436  0.0117  137 GLU B C   
4615 O O   . GLU B 157 ? 0.2218 0.2206 0.2352 -0.0287 0.0415  0.0032  137 GLU B O   
4616 C CB  . GLU B 157 ? 0.2184 0.1971 0.3180 -0.0120 0.0495  -0.0013 137 GLU B CB  
4617 C CG  . GLU B 157 ? 0.2363 0.2003 0.3467 -0.0060 0.0539  0.0155  137 GLU B CG  
4618 C CD  . GLU B 157 ? 0.2709 0.2133 0.3976 -0.0034 0.0719  0.0075  137 GLU B CD  
4619 O OE1 . GLU B 157 ? 0.2713 0.2416 0.3722 -0.0157 0.0663  -0.0023 137 GLU B OE1 
4620 O OE2 . GLU B 157 ? 0.3625 0.2322 0.4359 0.0214  0.0953  0.0301  137 GLU B OE2 
4627 N N   . GLN B 158 ? 0.2086 0.1891 0.2327 -0.0176 0.0490  0.0131  138 GLN B N   
4628 C CA  . GLN B 158 ? 0.2075 0.1824 0.2079 -0.0092 0.0346  0.0139  138 GLN B CA  
4629 C C   . GLN B 158 ? 0.2049 0.1810 0.2099 -0.0107 0.0519  0.0168  138 GLN B C   
4630 O O   . GLN B 158 ? 0.1977 0.2348 0.2235 -0.0072 0.0514  0.0371  138 GLN B O   
4631 C CB  . GLN B 158 ? 0.2070 0.1983 0.2434 -0.0054 0.0424  0.0105  138 GLN B CB  
4632 C CG  . GLN B 158 ? 0.2293 0.2036 0.2552 0.0032  0.0558  0.0274  138 GLN B CG  
4633 C CD  . GLN B 158 ? 0.2251 0.2424 0.2661 -0.0005 0.0458  0.0081  138 GLN B CD  
4634 O OE1 . GLN B 158 ? 0.2588 0.2491 0.2734 -0.0218 0.0243  0.0251  138 GLN B OE1 
4635 N NE2 . GLN B 158 ? 0.2535 0.2880 0.2804 0.0145  0.0587  -0.0056 138 GLN B NE2 
4644 N N   . ARG B 159 ? 0.1875 0.1724 0.2096 -0.0165 0.0484  0.0249  139 ARG B N   
4645 C CA  . ARG B 159 ? 0.2079 0.1700 0.2046 -0.0176 0.0437  0.0196  139 ARG B CA  
4646 C C   . ARG B 159 ? 0.1923 0.1886 0.2065 -0.0223 0.0433  0.0312  139 ARG B C   
4647 O O   . ARG B 159 ? 0.2196 0.2057 0.2037 -0.0361 0.0419  0.0414  139 ARG B O   
4648 C CB  . ARG B 159 ? 0.2238 0.1602 0.2167 -0.0078 0.0375  0.0138  139 ARG B CB  
4649 C CG  . ARG B 159 ? 0.2167 0.1658 0.2449 -0.0075 0.0451  0.0171  139 ARG B CG  
4650 C CD  . ARG B 159 ? 0.2355 0.1912 0.2519 -0.0124 0.0651  -0.0112 139 ARG B CD  
4651 N NE  . ARG B 159 ? 0.2082 0.2059 0.2375 0.0002  0.0514  0.0079  139 ARG B NE  
4652 C CZ  . ARG B 159 ? 0.2034 0.1892 0.2527 0.0015  0.0542  0.0043  139 ARG B CZ  
4653 N NH1 . ARG B 159 ? 0.2070 0.1923 0.2716 -0.0059 0.0643  -0.0010 139 ARG B NH1 
4654 N NH2 . ARG B 159 ? 0.2195 0.1904 0.2490 -0.0219 0.0551  -0.0011 139 ARG B NH2 
4668 N N   . GLU B 160 ? 0.1940 0.1890 0.2105 -0.0202 0.0349  0.0321  140 GLU B N   
4669 C CA  . GLU B 160 ? 0.2020 0.2001 0.2400 -0.0287 0.0351  0.0127  140 GLU B CA  
4670 C C   . GLU B 160 ? 0.2035 0.1837 0.2118 -0.0196 0.0367  0.0252  140 GLU B C   
4671 O O   . GLU B 160 ? 0.2156 0.1808 0.2254 -0.0174 0.0235  0.0465  140 GLU B O   
4672 C CB  . GLU B 160 ? 0.2511 0.2793 0.2978 -0.0124 0.0697  -0.0247 140 GLU B CB  
4673 C CG  . GLU B 160 ? 0.2785 0.3013 0.2830 0.0137  0.0767  0.0140  140 GLU B CG  
4674 C CD  . GLU B 160 ? 0.2822 0.3234 0.2756 0.0154  0.0433  -0.0035 140 GLU B CD  
4675 O OE1 . GLU B 160 ? 0.2730 0.3515 0.3068 -0.0056 0.0339  -0.0226 140 GLU B OE1 
4676 O OE2 . GLU B 160 ? 0.3514 0.3188 0.3354 0.0277  -0.0051 -0.0089 140 GLU B OE2 
4683 N N   . PHE B 161 ? 0.2040 0.1850 0.2111 -0.0191 0.0425  0.0327  141 PHE B N   
4684 C CA  . PHE B 161 ? 0.1843 0.1683 0.2204 -0.0048 0.0306  0.0296  141 PHE B CA  
4685 C C   . PHE B 161 ? 0.1927 0.1480 0.2232 -0.0019 0.0356  0.0405  141 PHE B C   
4686 O O   . PHE B 161 ? 0.1982 0.1698 0.2433 -0.0006 0.0230  0.0481  141 PHE B O   
4687 C CB  . PHE B 161 ? 0.2124 0.1653 0.2208 -0.0097 0.0505  0.0207  141 PHE B CB  
4688 C CG  . PHE B 161 ? 0.1957 0.1732 0.2216 -0.0102 0.0497  0.0195  141 PHE B CG  
4689 C CD1 . PHE B 161 ? 0.1997 0.1982 0.2399 -0.0080 0.0634  0.0184  141 PHE B CD1 
4690 C CD2 . PHE B 161 ? 0.2231 0.1752 0.2338 -0.0062 0.0295  0.0020  141 PHE B CD2 
4691 C CE1 . PHE B 161 ? 0.2113 0.2257 0.2440 -0.0338 0.0527  0.0134  141 PHE B CE1 
4692 C CE2 . PHE B 161 ? 0.2633 0.1943 0.2429 -0.0136 0.0352  -0.0182 141 PHE B CE2 
4693 C CZ  . PHE B 161 ? 0.2430 0.2122 0.2395 -0.0466 0.0463  -0.0072 141 PHE B CZ  
4703 N N   . MET B 162 ? 0.2023 0.1509 0.2203 -0.0076 0.0167  0.0372  142 MET B N   
4704 C CA  . MET B 162 ? 0.2187 0.1511 0.2307 -0.0054 0.0208  0.0223  142 MET B CA  
4705 C C   . MET B 162 ? 0.2239 0.1587 0.2180 -0.0101 0.0265  0.0269  142 MET B C   
4706 O O   . MET B 162 ? 0.2123 0.1789 0.2768 -0.0111 0.0155  0.0156  142 MET B O   
4707 C CB  . MET B 162 ? 0.2153 0.1837 0.2491 -0.0068 0.0231  0.0261  142 MET B CB  
4708 C CG  . MET B 162 ? 0.2098 0.2450 0.2847 0.0000  0.0204  0.0254  142 MET B CG  
4709 S SD  . MET B 162 ? 0.2476 0.2754 0.2583 0.0064  0.0416  0.0407  142 MET B SD  
4710 C CE  . MET B 162 ? 0.2518 0.2705 0.2513 -0.0068 0.0556  0.0071  142 MET B CE  
4720 N N   . ASN B 163 ? 0.2165 0.1675 0.2325 -0.0203 0.0268  0.0159  143 ASN B N   
4721 C CA  . ASN B 163 ? 0.2158 0.1584 0.2298 -0.0152 0.0251  0.0165  143 ASN B CA  
4722 C C   . ASN B 163 ? 0.1912 0.1635 0.2380 0.0147  0.0382  0.0160  143 ASN B C   
4723 O O   . ASN B 163 ? 0.2217 0.1716 0.2348 0.0069  0.0377  -0.0004 143 ASN B O   
4724 C CB  . ASN B 163 ? 0.2149 0.1851 0.2208 -0.0217 0.0301  0.0144  143 ASN B CB  
4725 C CG  . ASN B 163 ? 0.2072 0.2188 0.2473 -0.0119 0.0235  0.0151  143 ASN B CG  
4726 O OD1 . ASN B 163 ? 0.2155 0.2136 0.2566 0.0028  0.0312  -0.0035 143 ASN B OD1 
4727 N ND2 . ASN B 163 ? 0.2156 0.2775 0.3160 -0.0288 0.0539  0.0512  143 ASN B ND2 
4734 N N   . PRO B 164 ? 0.2011 0.1645 0.2194 0.0097  0.0294  0.0009  144 PRO B N   
4735 C CA  . PRO B 164 ? 0.2164 0.1812 0.2254 -0.0001 0.0387  -0.0010 144 PRO B CA  
4736 C C   . PRO B 164 ? 0.2005 0.1958 0.2158 0.0005  0.0317  -0.0093 144 PRO B C   
4737 O O   . PRO B 164 ? 0.2288 0.2103 0.2059 0.0059  0.0408  -0.0081 144 PRO B O   
4738 C CB  . PRO B 164 ? 0.2578 0.1814 0.2367 -0.0057 0.0399  0.0290  144 PRO B CB  
4739 C CG  . PRO B 164 ? 0.2414 0.1994 0.2526 -0.0013 0.0343  0.0001  144 PRO B CG  
4740 C CD  . PRO B 164 ? 0.2184 0.1663 0.2234 -0.0001 0.0368  0.0103  144 PRO B CD  
4748 N N   . CYS B 165 ? 0.2006 0.1965 0.2369 -0.0013 0.0422  -0.0186 145 CYS B N   
4749 C CA  . CYS B 165 ? 0.2111 0.2217 0.2428 -0.0244 0.0384  -0.0260 145 CYS B CA  
4750 C C   . CYS B 165 ? 0.2341 0.2091 0.2262 -0.0196 0.0399  -0.0030 145 CYS B C   
4751 O O   . CYS B 165 ? 0.2516 0.2314 0.2270 -0.0197 0.0390  -0.0181 145 CYS B O   
4752 C CB  . CYS B 165 ? 0.2189 0.2508 0.2699 -0.0241 0.0382  -0.0546 145 CYS B CB  
4753 S SG  . CYS B 165 ? 0.2270 0.2883 0.2943 0.0084  0.0389  -0.0388 145 CYS B SG  
4759 N N   . GLU B 166 ? 0.2384 0.1886 0.2236 -0.0252 0.0238  -0.0155 146 GLU B N   
4760 C CA  . GLU B 166 ? 0.2570 0.1956 0.2513 -0.0187 0.0408  -0.0104 146 GLU B CA  
4761 C C   . GLU B 166 ? 0.2552 0.1936 0.2439 -0.0116 0.0390  -0.0059 146 GLU B C   
4762 O O   . GLU B 166 ? 0.3028 0.1967 0.2592 -0.0157 0.0602  -0.0134 146 GLU B O   
4763 C CB  . GLU B 166 ? 0.2562 0.2490 0.2579 -0.0181 0.0243  0.0093  146 GLU B CB  
4764 C CG  . GLU B 166 ? 0.3341 0.3016 0.3064 -0.0193 0.0724  0.0374  146 GLU B CG  
4765 C CD  . GLU B 166 ? 0.3657 0.3813 0.4743 -0.0104 0.1572  0.0385  146 GLU B CD  
4766 O OE1 . GLU B 166 ? 0.3601 0.3780 0.4799 -0.0377 0.1075  -0.0015 146 GLU B OE1 
4767 O OE2 . GLU B 166 ? 0.4159 0.4583 0.6806 0.0031  0.2095  0.0550  146 GLU B OE2 
4774 N N   . GLN B 167 ? 0.2185 0.2098 0.2199 -0.0107 0.0303  -0.0107 147 GLN B N   
4775 C CA  . GLN B 167 ? 0.2112 0.2081 0.2246 -0.0136 0.0313  -0.0098 147 GLN B CA  
4776 C C   . GLN B 167 ? 0.2203 0.2090 0.2193 -0.0047 0.0570  0.0002  147 GLN B C   
4777 O O   . GLN B 167 ? 0.2453 0.2192 0.2268 0.0073  0.0548  -0.0091 147 GLN B O   
4778 C CB  . GLN B 167 ? 0.2302 0.2265 0.2278 0.0037  0.0237  -0.0019 147 GLN B CB  
4779 C CG  . GLN B 167 ? 0.2373 0.2484 0.2598 -0.0073 0.0613  -0.0020 147 GLN B CG  
4780 C CD  . GLN B 167 ? 0.2679 0.2887 0.2643 -0.0129 0.0600  0.0021  147 GLN B CD  
4781 O OE1 . GLN B 167 ? 0.3190 0.2974 0.2782 -0.0206 0.0407  0.0024  147 GLN B OE1 
4782 N NE2 . GLN B 167 ? 0.2808 0.3021 0.3087 -0.0348 0.0615  -0.0120 147 GLN B NE2 
4791 N N   . PHE B 168 ? 0.2205 0.2330 0.2230 0.0096  0.0396  -0.0305 148 PHE B N   
4792 C CA  . PHE B 168 ? 0.2161 0.2441 0.2347 0.0142  0.0370  -0.0248 148 PHE B CA  
4793 C C   . PHE B 168 ? 0.2406 0.2472 0.2221 -0.0029 0.0456  -0.0305 148 PHE B C   
4794 O O   . PHE B 168 ? 0.2607 0.2695 0.2155 0.0051  0.0268  -0.0353 148 PHE B O   
4795 C CB  . PHE B 168 ? 0.2502 0.2645 0.2266 0.0337  0.0306  -0.0063 148 PHE B CB  
4796 C CG  . PHE B 168 ? 0.3038 0.2469 0.2411 0.0390  0.0604  0.0144  148 PHE B CG  
4797 C CD1 . PHE B 168 ? 0.3692 0.2369 0.2602 0.0196  0.0970  -0.0021 148 PHE B CD1 
4798 C CD2 . PHE B 168 ? 0.3116 0.2460 0.2546 0.0379  0.0599  0.0178  148 PHE B CD2 
4799 C CE1 . PHE B 168 ? 0.4330 0.2333 0.3431 0.0230  0.1765  0.0102  148 PHE B CE1 
4800 C CE2 . PHE B 168 ? 0.4259 0.2394 0.2972 0.0415  0.1237  0.0178  148 PHE B CE2 
4801 C CZ  . PHE B 168 ? 0.4841 0.2350 0.3423 0.0133  0.1772  0.0010  148 PHE B CZ  
4811 N N   . ARG B 169 ? 0.2443 0.2603 0.2338 -0.0231 0.0370  -0.0309 149 ARG B N   
4812 C CA  . ARG B 169 ? 0.2750 0.2690 0.2551 -0.0483 0.0390  -0.0272 149 ARG B CA  
4813 C C   . ARG B 169 ? 0.2727 0.2351 0.2538 -0.0376 0.0564  -0.0221 149 ARG B C   
4814 O O   . ARG B 169 ? 0.2918 0.2645 0.2727 -0.0462 0.0407  -0.0470 149 ARG B O   
4815 C CB  . ARG B 169 ? 0.3145 0.3157 0.2748 -0.0757 0.0941  -0.0499 149 ARG B CB  
4816 C CG  . ARG B 169 ? 0.3282 0.3676 0.3212 -0.0971 0.1303  -0.0562 149 ARG B CG  
4817 C CD  . ARG B 169 ? 0.3715 0.4098 0.4079 -0.1180 0.1515  -0.0401 149 ARG B CD  
4818 N NE  . ARG B 169 ? 0.4912 0.4600 0.4830 -0.1062 0.1821  -0.0476 149 ARG B NE  
4819 C CZ  . ARG B 169 ? 0.5370 0.4573 0.5387 -0.0831 0.2403  -0.0479 149 ARG B CZ  
4820 N NH1 . ARG B 169 ? 0.5533 0.4417 0.5826 -0.0961 0.2918  0.0200  149 ARG B NH1 
4821 N NH2 . ARG B 169 ? 0.5560 0.4725 0.5477 -0.0852 0.2321  -0.0969 149 ARG B NH2 
4835 N N   . SER B 170 ? 0.2884 0.2109 0.2519 -0.0346 0.0553  -0.0292 150 SER B N   
4836 C CA  . SER B 170 ? 0.3042 0.2126 0.2514 -0.0096 0.0541  -0.0203 150 SER B CA  
4837 C C   . SER B 170 ? 0.2682 0.2267 0.2452 0.0046  0.0429  -0.0295 150 SER B C   
4838 O O   . SER B 170 ? 0.3228 0.2265 0.2544 0.0198  0.0476  -0.0318 150 SER B O   
4839 C CB  . SER B 170 ? 0.3235 0.2004 0.2603 -0.0020 0.0413  0.0136  150 SER B CB  
4840 O OG  . SER B 170 ? 0.3022 0.2213 0.2617 0.0113  0.0498  -0.0126 150 SER B OG  
4846 N N   . LEU B 171 ? 0.2600 0.2343 0.2203 0.0042  0.0413  -0.0053 151 LEU B N   
4847 C CA  . LEU B 171 ? 0.2592 0.2257 0.2534 -0.0052 0.0387  -0.0055 151 LEU B CA  
4848 C C   . LEU B 171 ? 0.2731 0.2542 0.2650 -0.0184 0.0225  -0.0166 151 LEU B C   
4849 O O   . LEU B 171 ? 0.2941 0.3118 0.2583 -0.0004 0.0262  -0.0148 151 LEU B O   
4850 C CB  . LEU B 171 ? 0.2694 0.2330 0.2464 -0.0004 0.0383  0.0165  151 LEU B CB  
4851 C CG  . LEU B 171 ? 0.2523 0.2522 0.2397 -0.0063 0.0462  0.0094  151 LEU B CG  
4852 C CD1 . LEU B 171 ? 0.2574 0.2611 0.2971 -0.0223 0.0361  0.0201  151 LEU B CD1 
4853 C CD2 . LEU B 171 ? 0.2939 0.2964 0.2430 0.0021  0.0321  0.0072  151 LEU B CD2 
4865 N N   . GLY B 172 ? 0.2767 0.2771 0.2491 -0.0308 0.0235  -0.0313 152 GLY B N   
4866 C CA  . GLY B 172 ? 0.2644 0.3198 0.2840 -0.0283 -0.0001 -0.0309 152 GLY B CA  
4867 C C   . GLY B 172 ? 0.2691 0.3521 0.2755 -0.0112 0.0207  -0.0390 152 GLY B C   
4868 O O   . GLY B 172 ? 0.2736 0.3923 0.3032 0.0021  -0.0022 -0.0499 152 GLY B O   
4872 N N   . ILE B 173 ? 0.2588 0.3367 0.2612 0.0006  0.0310  -0.0464 153 ILE B N   
4873 C CA  . ILE B 173 ? 0.2472 0.3495 0.2552 0.0250  0.0177  -0.0317 153 ILE B CA  
4874 C C   . ILE B 173 ? 0.2275 0.3765 0.2615 0.0135  -0.0082 -0.0535 153 ILE B C   
4875 O O   . ILE B 173 ? 0.2654 0.3689 0.2712 0.0209  0.0191  -0.0346 153 ILE B O   
4876 C CB  . ILE B 173 ? 0.2670 0.3290 0.2554 0.0292  0.0220  -0.0230 153 ILE B CB  
4877 C CG1 . ILE B 173 ? 0.2624 0.3296 0.2483 0.0153  0.0363  0.0058  153 ILE B CG1 
4878 C CG2 . ILE B 173 ? 0.2890 0.3204 0.2863 0.0364  0.0130  -0.0195 153 ILE B CG2 
4879 C CD1 . ILE B 173 ? 0.2679 0.3551 0.2374 0.0172  0.0410  -0.0032 153 ILE B CD1 
4891 N N   . GLU B 174 ? 0.2426 0.4216 0.2826 0.0216  0.0048  -0.0746 154 GLU B N   
4892 C CA  . GLU B 174 ? 0.2559 0.4461 0.3108 0.0124  0.0157  -0.0844 154 GLU B CA  
4893 C C   . GLU B 174 ? 0.2563 0.4201 0.3100 0.0002  0.0308  -0.0815 154 GLU B C   
4894 O O   . GLU B 174 ? 0.2844 0.4191 0.3244 0.0100  0.0418  -0.0620 154 GLU B O   
4895 C CB  . GLU B 174 ? 0.2653 0.4805 0.3367 0.0191  0.0363  -0.0784 154 GLU B CB  
4898 N N   . VAL B 175 ? 0.2385 0.4112 0.3154 -0.0157 0.0426  -0.0865 155 VAL B N   
4899 C CA  . VAL B 175 ? 0.2500 0.4108 0.3128 -0.0230 0.0582  -0.0919 155 VAL B CA  
4900 C C   . VAL B 175 ? 0.3040 0.3958 0.2889 -0.0213 0.0724  -0.0394 155 VAL B C   
4901 O O   . VAL B 175 ? 0.2462 0.3847 0.3404 -0.0095 0.0651  -0.0433 155 VAL B O   
4902 C CB  . VAL B 175 ? 0.2361 0.4654 0.3566 0.0108  0.0396  -0.1397 155 VAL B CB  
4903 C CG1 . VAL B 175 ? 0.2536 0.4675 0.3482 -0.0355 0.0694  -0.1342 155 VAL B CG1 
4904 C CG2 . VAL B 175 ? 0.2634 0.5204 0.3890 0.0614  0.0063  -0.1647 155 VAL B CG2 
4914 N N   . PRO B 176 ? 0.4220 0.4158 0.3142 -0.0159 0.1386  0.0054  156 PRO B N   
4915 C CA  . PRO B 176 ? 0.4960 0.4175 0.3354 0.0040  0.1666  0.0078  156 PRO B CA  
4916 C C   . PRO B 176 ? 0.3696 0.4293 0.3701 0.0294  0.1486  -0.0018 156 PRO B C   
4917 O O   . PRO B 176 ? 0.3189 0.3859 0.3443 -0.0283 0.1010  -0.0352 156 PRO B O   
4918 C CB  . PRO B 176 ? 0.5988 0.4385 0.3919 0.0144  0.1625  -0.0011 156 PRO B CB  
4919 C CG  . PRO B 176 ? 0.5554 0.4476 0.4152 -0.0024 0.0923  -0.0144 156 PRO B CG  
4920 C CD  . PRO B 176 ? 0.4978 0.4520 0.3220 -0.0070 0.1584  -0.0117 156 PRO B CD  
4928 N N   . GLU B 177 ? 0.3769 0.5007 0.4295 0.0865  0.1630  -0.0038 157 GLU B N   
4929 C CA  . GLU B 177 ? 0.3758 0.5422 0.4669 0.0923  0.1779  -0.0040 157 GLU B CA  
4930 C C   . GLU B 177 ? 0.3462 0.5231 0.4336 0.1066  0.1284  0.0150  157 GLU B C   
4931 O O   . GLU B 177 ? 0.3990 0.5443 0.3985 0.1346  0.0962  -0.0002 157 GLU B O   
4932 C CB  . GLU B 177 ? 0.5003 0.6197 0.5783 0.0546  0.2082  -0.0114 157 GLU B CB  
4933 C CG  . GLU B 177 ? 0.6048 0.6783 0.6559 0.0110  0.2362  -0.0134 157 GLU B CG  
4934 C CD  . GLU B 177 ? 0.7261 0.7236 0.7235 -0.0170 0.2259  -0.0190 157 GLU B CD  
4935 O OE1 . GLU B 177 ? 0.7684 0.7353 0.7468 -0.0375 0.2077  -0.0468 157 GLU B OE1 
4936 O OE2 . GLU B 177 ? 0.7543 0.7385 0.7712 -0.0191 0.2297  -0.0011 157 GLU B OE2 
4943 N N   . VAL B 178 ? 0.2168 0.4712 0.4116 0.0442  0.1080  0.0421  158 VAL B N   
4944 C CA  . VAL B 178 ? 0.1842 0.4502 0.3707 0.0120  0.0703  0.0486  158 VAL B CA  
4945 C C   . VAL B 178 ? 0.2044 0.4099 0.3807 0.0072  0.0996  0.0485  158 VAL B C   
4946 O O   . VAL B 178 ? 0.2557 0.3855 0.4671 0.0111  0.1340  0.0608  158 VAL B O   
4947 C CB  . VAL B 178 ? 0.2295 0.4726 0.3608 -0.0312 0.0375  0.0584  158 VAL B CB  
4948 C CG1 . VAL B 178 ? 0.2908 0.4777 0.3445 -0.0259 0.0524  0.0180  158 VAL B CG1 
4949 C CG2 . VAL B 178 ? 0.2412 0.4885 0.3821 -0.0664 0.0310  0.0783  158 VAL B CG2 
4959 N N   . ARG B 179 ? 0.1761 0.4227 0.3414 -0.0156 0.0568  0.0080  159 ARG B N   
4960 C CA  . ARG B 179 ? 0.1933 0.4701 0.3488 -0.0240 0.0563  -0.0184 159 ARG B CA  
4961 C C   . ARG B 179 ? 0.1985 0.4474 0.3267 -0.0303 0.0505  -0.0068 159 ARG B C   
4962 O O   . ARG B 179 ? 0.3013 0.4368 0.3179 -0.0215 0.0628  -0.0176 159 ARG B O   
4963 C CB  . ARG B 179 ? 0.1830 0.5582 0.3345 -0.0350 0.0251  0.0023  159 ARG B CB  
4964 C CG  . ARG B 179 ? 0.2136 0.6228 0.3462 -0.0419 0.0104  -0.0034 159 ARG B CG  
4965 C CD  . ARG B 179 ? 0.2817 0.6549 0.3720 -0.0430 -0.0033 0.0201  159 ARG B CD  
4966 N NE  . ARG B 179 ? 0.2593 0.6726 0.4284 -0.0139 -0.0090 0.0652  159 ARG B NE  
4967 C CZ  . ARG B 179 ? 0.3166 0.6874 0.4406 0.0130  -0.0403 -0.0117 159 ARG B CZ  
4968 N NH1 . ARG B 179 ? 0.3883 0.6863 0.3913 0.0531  -0.0146 -0.0165 159 ARG B NH1 
4969 N NH2 . ARG B 179 ? 0.3242 0.7122 0.5106 0.0266  -0.0979 -0.0544 159 ARG B NH2 
4983 N N   . ARG B 180 ? 0.2189 0.4425 0.3452 -0.0136 0.0638  0.0302  160 ARG B N   
4984 C CA  . ARG B 180 ? 0.2668 0.4580 0.3581 0.0108  0.0960  0.0667  160 ARG B CA  
4985 C C   . ARG B 180 ? 0.2431 0.4549 0.3802 0.0196  0.0922  0.0648  160 ARG B C   
4986 O O   . ARG B 180 ? 0.2436 0.4421 0.3964 0.0005  0.0859  0.0625  160 ARG B O   
4987 C CB  . ARG B 180 ? 0.2611 0.4622 0.3849 0.0283  0.0841  0.0534  160 ARG B CB  
4988 C CG  . ARG B 180 ? 0.2819 0.4660 0.4306 0.0076  0.0895  0.0361  160 ARG B CG  
4989 C CD  . ARG B 180 ? 0.2880 0.4506 0.4449 -0.0373 0.0905  -0.0105 160 ARG B CD  
4990 N NE  . ARG B 180 ? 0.2767 0.4254 0.3940 -0.0285 0.0220  -0.0002 160 ARG B NE  
4991 C CZ  . ARG B 180 ? 0.3091 0.4126 0.4170 0.0026  0.0376  0.0191  160 ARG B CZ  
4992 N NH1 . ARG B 180 ? 0.4016 0.4137 0.4233 -0.0214 0.0756  0.0557  160 ARG B NH1 
4993 N NH2 . ARG B 180 ? 0.2970 0.4147 0.4379 0.0127  0.0316  -0.0239 160 ARG B NH2 
5007 N N   . ASP B 181 ? 0.2397 0.4592 0.4395 0.0146  0.0816  0.0154  161 ASP B N   
5008 C CA  . ASP B 181 ? 0.2108 0.4778 0.4529 0.0072  0.0743  -0.0052 161 ASP B CA  
5009 C C   . ASP B 181 ? 0.2419 0.4249 0.4381 -0.0010 0.0989  0.0022  161 ASP B C   
5010 O O   . ASP B 181 ? 0.2506 0.4129 0.4876 -0.0231 0.1408  0.0180  161 ASP B O   
5011 C CB  . ASP B 181 ? 0.2208 0.5270 0.5060 0.0042  0.0648  -0.0395 161 ASP B CB  
5012 C CG  . ASP B 181 ? 0.3247 0.5700 0.5657 -0.0066 0.0571  -0.0617 161 ASP B CG  
5013 O OD1 . ASP B 181 ? 0.3575 0.5698 0.6274 -0.0520 0.0495  -0.0889 161 ASP B OD1 
5014 O OD2 . ASP B 181 ? 0.3333 0.5931 0.5084 0.0260  0.0125  -0.0486 161 ASP B OD2 
5019 N N   . GLY B 182 ? 0.2281 0.3906 0.4251 0.0253  0.0509  0.0099  162 GLY B N   
5020 C CA  . GLY B 182 ? 0.2387 0.3781 0.4173 0.0176  0.0411  0.0386  162 GLY B CA  
5021 C C   . GLY B 182 ? 0.2428 0.4086 0.4134 0.0123  0.0500  0.0377  162 GLY B C   
5022 O O   . GLY B 182 ? 0.2681 0.3972 0.4167 0.0158  0.0516  0.0543  162 GLY B O   
5026 N N   . LEU B 183 ? 0.2656 0.4274 0.4168 0.0312  0.0279  0.0257  163 LEU B N   
5027 C CA  . LEU B 183 ? 0.2919 0.4336 0.3876 0.0537  0.0092  0.0220  163 LEU B CA  
5028 C C   . LEU B 183 ? 0.3548 0.5080 0.4146 0.0818  0.0129  0.0435  163 LEU B C   
5029 O O   . LEU B 183 ? 0.4097 0.5152 0.4394 0.0546  0.0451  0.0639  163 LEU B O   
5045 N N   . PRO B 184 ? 0.4770 0.5854 0.4400 0.0775  0.0057  0.0437  164 PRO B N   
5046 C CA  . PRO B 184 ? 0.5616 0.6265 0.4497 0.0596  0.0141  0.0511  164 PRO B CA  
5047 C C   . PRO B 184 ? 0.5833 0.6290 0.4541 0.1143  0.0153  0.0984  164 PRO B C   
5048 O O   . PRO B 184 ? 0.6158 0.6287 0.4990 0.1454  0.0289  0.1120  164 PRO B O   
5049 C CB  . PRO B 184 ? 0.6054 0.6476 0.4406 0.0496  0.0314  0.0559  164 PRO B CB  
5050 C CG  . PRO B 184 ? 0.6183 0.6585 0.4714 0.0518  0.0272  0.0378  164 PRO B CG  
5051 C CD  . PRO B 184 ? 0.5857 0.6370 0.4568 0.0725  0.0389  0.0427  164 PRO B CD  
# 
