data_9F8L
# 
_entry.id   9F8L 
# 
_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   9F8L         pdb_00009f8l 10.2210/pdb9f8l/pdb 
WWPDB D_1292138235 ?            ?                   
# 
_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                        9F8L 
_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' 9F8M unspecified 
PDB 'Contains the same protein complexed with different ligand' 9F8N 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-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                             195.237   2   ? ? ? ? 
3 non-polymer syn '(3-hydroxyphenyl)-[2-(4-hydroxyphenyl)-6-oxidanyl-1-benzothiophen-3-yl]methanone' 362.398   2   ? ? ? ? 
4 non-polymer syn GLYCEROL                                                                           92.094    4   ? ? ? ? 
5 water       nat water                                                                              18.015    346 ? ? ? ? 
# 
_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-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                             MES   
3 '(3-hydroxyphenyl)-[2-(4-hydroxyphenyl)-6-oxidanyl-1-benzothiophen-3-yl]methanone' A1IAL 
4 GLYCEROL                                                                           GOL   
5 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 
A1IAL non-polymer         . '(3-hydroxyphenyl)-[2-(4-hydroxyphenyl)-6-oxidanyl-1-benzothiophen-3-yl]methanone' 
'[6-Hydroxy-2-(4-hydroxyphenyl)benzo[b]thiophen-3-yl](3-hydroxyphenyl)methanone' 'C21 H14 O4 S'   362.398 
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 
MES   non-polymer         . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                             ? 'C6 H13 N O4 S'  
195.237 
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  10  THR THR 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 185 165 165 SER SER 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  10  THR THR B . n 
B 1 31  SER 31  11  11  SER SER 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 185 165 165 SER SER B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IAL 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IAL 
_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 MES   1   201 202 MES   MES A . 
D 3 A1IAL 1   202 204 A1IAL T28 A . 
E 4 GOL   1   203 205 GOL   GOL A . 
F 2 MES   1   201 201 MES   MES B . 
G 4 GOL   1   202 203 GOL   GOL B . 
H 3 A1IAL 1   203 204 A1IAL T28 B . 
I 4 GOL   1   204 206 GOL   GOL B . 
J 4 GOL   1   205 207 GOL   GOL B . 
K 5 HOH   1   301 236 HOH   HOH A . 
K 5 HOH   2   302 71  HOH   HOH A . 
K 5 HOH   3   303 402 HOH   HOH A . 
K 5 HOH   4   304 391 HOH   HOH A . 
K 5 HOH   5   305 401 HOH   HOH A . 
K 5 HOH   6   306 154 HOH   HOH A . 
K 5 HOH   7   307 368 HOH   HOH A . 
K 5 HOH   8   308 262 HOH   HOH A . 
K 5 HOH   9   309 385 HOH   HOH A . 
K 5 HOH   10  310 227 HOH   HOH A . 
K 5 HOH   11  311 397 HOH   HOH A . 
K 5 HOH   12  312 70  HOH   HOH A . 
K 5 HOH   13  313 322 HOH   HOH A . 
K 5 HOH   14  314 339 HOH   HOH A . 
K 5 HOH   15  315 155 HOH   HOH A . 
K 5 HOH   16  316 118 HOH   HOH A . 
K 5 HOH   17  317 36  HOH   HOH A . 
K 5 HOH   18  318 15  HOH   HOH A . 
K 5 HOH   19  319 306 HOH   HOH A . 
K 5 HOH   20  320 193 HOH   HOH A . 
K 5 HOH   21  321 202 HOH   HOH A . 
K 5 HOH   22  322 107 HOH   HOH A . 
K 5 HOH   23  323 407 HOH   HOH A . 
K 5 HOH   24  324 125 HOH   HOH A . 
K 5 HOH   25  325 229 HOH   HOH A . 
K 5 HOH   26  326 365 HOH   HOH A . 
K 5 HOH   27  327 53  HOH   HOH A . 
K 5 HOH   28  328 257 HOH   HOH A . 
K 5 HOH   29  329 248 HOH   HOH A . 
K 5 HOH   30  330 59  HOH   HOH A . 
K 5 HOH   31  331 115 HOH   HOH A . 
K 5 HOH   32  332 9   HOH   HOH A . 
K 5 HOH   33  333 198 HOH   HOH A . 
K 5 HOH   34  334 161 HOH   HOH A . 
K 5 HOH   35  335 13  HOH   HOH A . 
K 5 HOH   36  336 267 HOH   HOH A . 
K 5 HOH   37  337 265 HOH   HOH A . 
K 5 HOH   38  338 90  HOH   HOH A . 
K 5 HOH   39  339 362 HOH   HOH A . 
K 5 HOH   40  340 95  HOH   HOH A . 
K 5 HOH   41  341 3   HOH   HOH A . 
K 5 HOH   42  342 23  HOH   HOH A . 
K 5 HOH   43  343 184 HOH   HOH A . 
K 5 HOH   44  344 57  HOH   HOH A . 
K 5 HOH   45  345 414 HOH   HOH A . 
K 5 HOH   46  346 156 HOH   HOH A . 
K 5 HOH   47  347 168 HOH   HOH A . 
K 5 HOH   48  348 412 HOH   HOH A . 
K 5 HOH   49  349 60  HOH   HOH A . 
K 5 HOH   50  350 121 HOH   HOH A . 
K 5 HOH   51  351 12  HOH   HOH A . 
K 5 HOH   52  352 149 HOH   HOH A . 
K 5 HOH   53  353 204 HOH   HOH A . 
K 5 HOH   54  354 175 HOH   HOH A . 
K 5 HOH   55  355 138 HOH   HOH A . 
K 5 HOH   56  356 143 HOH   HOH A . 
K 5 HOH   57  357 157 HOH   HOH A . 
K 5 HOH   58  358 289 HOH   HOH A . 
K 5 HOH   59  359 24  HOH   HOH A . 
K 5 HOH   60  360 25  HOH   HOH A . 
K 5 HOH   61  361 139 HOH   HOH A . 
K 5 HOH   62  362 11  HOH   HOH A . 
K 5 HOH   63  363 164 HOH   HOH A . 
K 5 HOH   64  364 406 HOH   HOH A . 
K 5 HOH   65  365 254 HOH   HOH A . 
K 5 HOH   66  366 233 HOH   HOH A . 
K 5 HOH   67  367 197 HOH   HOH A . 
K 5 HOH   68  368 235 HOH   HOH A . 
K 5 HOH   69  369 390 HOH   HOH A . 
K 5 HOH   70  370 91  HOH   HOH A . 
K 5 HOH   71  371 187 HOH   HOH A . 
K 5 HOH   72  372 201 HOH   HOH A . 
K 5 HOH   73  373 169 HOH   HOH A . 
K 5 HOH   74  374 101 HOH   HOH A . 
K 5 HOH   75  375 324 HOH   HOH A . 
K 5 HOH   76  376 273 HOH   HOH A . 
K 5 HOH   77  377 48  HOH   HOH A . 
K 5 HOH   78  378 89  HOH   HOH A . 
K 5 HOH   79  379 119 HOH   HOH A . 
K 5 HOH   80  380 77  HOH   HOH A . 
K 5 HOH   81  381 225 HOH   HOH A . 
K 5 HOH   82  382 220 HOH   HOH A . 
K 5 HOH   83  383 356 HOH   HOH A . 
K 5 HOH   84  384 384 HOH   HOH A . 
K 5 HOH   85  385 376 HOH   HOH A . 
K 5 HOH   86  386 51  HOH   HOH A . 
K 5 HOH   87  387 171 HOH   HOH A . 
K 5 HOH   88  388 122 HOH   HOH A . 
K 5 HOH   89  389 26  HOH   HOH A . 
K 5 HOH   90  390 413 HOH   HOH A . 
K 5 HOH   91  391 133 HOH   HOH A . 
K 5 HOH   92  392 400 HOH   HOH A . 
K 5 HOH   93  393 56  HOH   HOH A . 
K 5 HOH   94  394 222 HOH   HOH A . 
K 5 HOH   95  395 242 HOH   HOH A . 
K 5 HOH   96  396 104 HOH   HOH A . 
K 5 HOH   97  397 393 HOH   HOH A . 
K 5 HOH   98  398 190 HOH   HOH A . 
K 5 HOH   99  399 147 HOH   HOH A . 
K 5 HOH   100 400 319 HOH   HOH A . 
K 5 HOH   101 401 114 HOH   HOH A . 
K 5 HOH   102 402 213 HOH   HOH A . 
K 5 HOH   103 403 223 HOH   HOH A . 
K 5 HOH   104 404 396 HOH   HOH A . 
K 5 HOH   105 405 151 HOH   HOH A . 
K 5 HOH   106 406 137 HOH   HOH A . 
K 5 HOH   107 407 92  HOH   HOH A . 
K 5 HOH   108 408 207 HOH   HOH A . 
K 5 HOH   109 409 231 HOH   HOH A . 
K 5 HOH   110 410 78  HOH   HOH A . 
K 5 HOH   111 411 405 HOH   HOH A . 
K 5 HOH   112 412 299 HOH   HOH A . 
K 5 HOH   113 413 250 HOH   HOH A . 
K 5 HOH   114 414 64  HOH   HOH A . 
K 5 HOH   115 415 80  HOH   HOH A . 
K 5 HOH   116 416 72  HOH   HOH A . 
K 5 HOH   117 417 134 HOH   HOH A . 
K 5 HOH   118 418 106 HOH   HOH A . 
K 5 HOH   119 419 268 HOH   HOH A . 
K 5 HOH   120 420 88  HOH   HOH A . 
K 5 HOH   121 421 145 HOH   HOH A . 
K 5 HOH   122 422 217 HOH   HOH A . 
K 5 HOH   123 423 183 HOH   HOH A . 
K 5 HOH   124 424 208 HOH   HOH A . 
K 5 HOH   125 425 96  HOH   HOH A . 
K 5 HOH   126 426 34  HOH   HOH A . 
K 5 HOH   127 427 128 HOH   HOH A . 
K 5 HOH   128 428 279 HOH   HOH A . 
K 5 HOH   129 429 243 HOH   HOH A . 
K 5 HOH   130 430 43  HOH   HOH A . 
K 5 HOH   131 431 278 HOH   HOH A . 
K 5 HOH   132 432 303 HOH   HOH A . 
K 5 HOH   133 433 226 HOH   HOH A . 
K 5 HOH   134 434 355 HOH   HOH A . 
K 5 HOH   135 435 178 HOH   HOH A . 
K 5 HOH   136 436 200 HOH   HOH A . 
K 5 HOH   137 437 327 HOH   HOH A . 
K 5 HOH   138 438 218 HOH   HOH A . 
K 5 HOH   139 439 409 HOH   HOH A . 
K 5 HOH   140 440 307 HOH   HOH A . 
K 5 HOH   141 441 54  HOH   HOH A . 
K 5 HOH   142 442 120 HOH   HOH A . 
K 5 HOH   143 443 260 HOH   HOH A . 
K 5 HOH   144 444 360 HOH   HOH A . 
K 5 HOH   145 445 294 HOH   HOH A . 
K 5 HOH   146 446 338 HOH   HOH A . 
K 5 HOH   147 447 158 HOH   HOH A . 
K 5 HOH   148 448 308 HOH   HOH A . 
K 5 HOH   149 449 329 HOH   HOH A . 
K 5 HOH   150 450 253 HOH   HOH A . 
K 5 HOH   151 451 176 HOH   HOH A . 
K 5 HOH   152 452 305 HOH   HOH A . 
K 5 HOH   153 453 403 HOH   HOH A . 
K 5 HOH   154 454 280 HOH   HOH A . 
K 5 HOH   155 455 330 HOH   HOH A . 
K 5 HOH   156 456 79  HOH   HOH A . 
K 5 HOH   157 457 182 HOH   HOH A . 
K 5 HOH   158 458 358 HOH   HOH A . 
K 5 HOH   159 459 404 HOH   HOH A . 
K 5 HOH   160 460 354 HOH   HOH A . 
K 5 HOH   161 461 288 HOH   HOH A . 
K 5 HOH   162 462 350 HOH   HOH A . 
K 5 HOH   163 463 366 HOH   HOH A . 
K 5 HOH   164 464 295 HOH   HOH A . 
K 5 HOH   165 465 209 HOH   HOH A . 
K 5 HOH   166 466 274 HOH   HOH A . 
K 5 HOH   167 467 293 HOH   HOH A . 
K 5 HOH   168 468 325 HOH   HOH A . 
K 5 HOH   169 469 357 HOH   HOH A . 
K 5 HOH   170 470 394 HOH   HOH A . 
K 5 HOH   171 471 382 HOH   HOH A . 
K 5 HOH   172 472 395 HOH   HOH A . 
L 5 HOH   1   301 74  HOH   HOH B . 
L 5 HOH   2   302 333 HOH   HOH B . 
L 5 HOH   3   303 219 HOH   HOH B . 
L 5 HOH   4   304 160 HOH   HOH B . 
L 5 HOH   5   305 335 HOH   HOH B . 
L 5 HOH   6   306 269 HOH   HOH B . 
L 5 HOH   7   307 230 HOH   HOH B . 
L 5 HOH   8   308 132 HOH   HOH B . 
L 5 HOH   9   309 58  HOH   HOH B . 
L 5 HOH   10  310 323 HOH   HOH B . 
L 5 HOH   11  311 131 HOH   HOH B . 
L 5 HOH   12  312 148 HOH   HOH B . 
L 5 HOH   13  313 399 HOH   HOH B . 
L 5 HOH   14  314 83  HOH   HOH B . 
L 5 HOH   15  315 313 HOH   HOH B . 
L 5 HOH   16  316 211 HOH   HOH B . 
L 5 HOH   17  317 136 HOH   HOH B . 
L 5 HOH   18  318 69  HOH   HOH B . 
L 5 HOH   19  319 371 HOH   HOH B . 
L 5 HOH   20  320 342 HOH   HOH B . 
L 5 HOH   21  321 261 HOH   HOH B . 
L 5 HOH   22  322 140 HOH   HOH B . 
L 5 HOH   23  323 14  HOH   HOH B . 
L 5 HOH   24  324 283 HOH   HOH B . 
L 5 HOH   25  325 29  HOH   HOH B . 
L 5 HOH   26  326 123 HOH   HOH B . 
L 5 HOH   27  327 159 HOH   HOH B . 
L 5 HOH   28  328 8   HOH   HOH B . 
L 5 HOH   29  329 246 HOH   HOH B . 
L 5 HOH   30  330 93  HOH   HOH B . 
L 5 HOH   31  331 40  HOH   HOH B . 
L 5 HOH   32  332 112 HOH   HOH B . 
L 5 HOH   33  333 392 HOH   HOH B . 
L 5 HOH   34  334 127 HOH   HOH B . 
L 5 HOH   35  335 388 HOH   HOH B . 
L 5 HOH   36  336 410 HOH   HOH B . 
L 5 HOH   37  337 129 HOH   HOH B . 
L 5 HOH   38  338 68  HOH   HOH B . 
L 5 HOH   39  339 372 HOH   HOH B . 
L 5 HOH   40  340 130 HOH   HOH B . 
L 5 HOH   41  341 2   HOH   HOH B . 
L 5 HOH   42  342 117 HOH   HOH B . 
L 5 HOH   43  343 63  HOH   HOH B . 
L 5 HOH   44  344 320 HOH   HOH B . 
L 5 HOH   45  345 215 HOH   HOH B . 
L 5 HOH   46  346 378 HOH   HOH B . 
L 5 HOH   47  347 398 HOH   HOH B . 
L 5 HOH   48  348 27  HOH   HOH B . 
L 5 HOH   49  349 32  HOH   HOH B . 
L 5 HOH   50  350 73  HOH   HOH B . 
L 5 HOH   51  351 216 HOH   HOH B . 
L 5 HOH   52  352 415 HOH   HOH B . 
L 5 HOH   53  353 28  HOH   HOH B . 
L 5 HOH   54  354 81  HOH   HOH B . 
L 5 HOH   55  355 167 HOH   HOH B . 
L 5 HOH   56  356 20  HOH   HOH B . 
L 5 HOH   57  357 61  HOH   HOH B . 
L 5 HOH   58  358 94  HOH   HOH B . 
L 5 HOH   59  359 97  HOH   HOH B . 
L 5 HOH   60  360 353 HOH   HOH B . 
L 5 HOH   61  361 22  HOH   HOH B . 
L 5 HOH   62  362 44  HOH   HOH B . 
L 5 HOH   63  363 205 HOH   HOH B . 
L 5 HOH   64  364 172 HOH   HOH B . 
L 5 HOH   65  365 116 HOH   HOH B . 
L 5 HOH   66  366 192 HOH   HOH B . 
L 5 HOH   67  367 6   HOH   HOH B . 
L 5 HOH   68  368 224 HOH   HOH B . 
L 5 HOH   69  369 234 HOH   HOH B . 
L 5 HOH   70  370 82  HOH   HOH B . 
L 5 HOH   71  371 38  HOH   HOH B . 
L 5 HOH   72  372 170 HOH   HOH B . 
L 5 HOH   73  373 255 HOH   HOH B . 
L 5 HOH   74  374 195 HOH   HOH B . 
L 5 HOH   75  375 199 HOH   HOH B . 
L 5 HOH   76  376 337 HOH   HOH B . 
L 5 HOH   77  377 194 HOH   HOH B . 
L 5 HOH   78  378 67  HOH   HOH B . 
L 5 HOH   79  379 17  HOH   HOH B . 
L 5 HOH   80  380 348 HOH   HOH B . 
L 5 HOH   81  381 210 HOH   HOH B . 
L 5 HOH   82  382 76  HOH   HOH B . 
L 5 HOH   83  383 212 HOH   HOH B . 
L 5 HOH   84  384 244 HOH   HOH B . 
L 5 HOH   85  385 46  HOH   HOH B . 
L 5 HOH   86  386 108 HOH   HOH B . 
L 5 HOH   87  387 84  HOH   HOH B . 
L 5 HOH   88  388 150 HOH   HOH B . 
L 5 HOH   89  389 317 HOH   HOH B . 
L 5 HOH   90  390 99  HOH   HOH B . 
L 5 HOH   91  391 272 HOH   HOH B . 
L 5 HOH   92  392 87  HOH   HOH B . 
L 5 HOH   93  393 191 HOH   HOH B . 
L 5 HOH   94  394 144 HOH   HOH B . 
L 5 HOH   95  395 386 HOH   HOH B . 
L 5 HOH   96  396 152 HOH   HOH B . 
L 5 HOH   97  397 126 HOH   HOH B . 
L 5 HOH   98  398 102 HOH   HOH B . 
L 5 HOH   99  399 153 HOH   HOH B . 
L 5 HOH   100 400 326 HOH   HOH B . 
L 5 HOH   101 401 252 HOH   HOH B . 
L 5 HOH   102 402 346 HOH   HOH B . 
L 5 HOH   103 403 340 HOH   HOH B . 
L 5 HOH   104 404 256 HOH   HOH B . 
L 5 HOH   105 405 98  HOH   HOH B . 
L 5 HOH   106 406 85  HOH   HOH B . 
L 5 HOH   107 407 103 HOH   HOH B . 
L 5 HOH   108 408 264 HOH   HOH B . 
L 5 HOH   109 409 135 HOH   HOH B . 
L 5 HOH   110 410 166 HOH   HOH B . 
L 5 HOH   111 411 41  HOH   HOH B . 
L 5 HOH   112 412 86  HOH   HOH B . 
L 5 HOH   113 413 47  HOH   HOH B . 
L 5 HOH   114 414 258 HOH   HOH B . 
L 5 HOH   115 415 185 HOH   HOH B . 
L 5 HOH   116 416 259 HOH   HOH B . 
L 5 HOH   117 417 379 HOH   HOH B . 
L 5 HOH   118 418 287 HOH   HOH B . 
L 5 HOH   119 419 105 HOH   HOH B . 
L 5 HOH   120 420 49  HOH   HOH B . 
L 5 HOH   121 421 124 HOH   HOH B . 
L 5 HOH   122 422 302 HOH   HOH B . 
L 5 HOH   123 423 52  HOH   HOH B . 
L 5 HOH   124 424 196 HOH   HOH B . 
L 5 HOH   125 425 271 HOH   HOH B . 
L 5 HOH   126 426 180 HOH   HOH B . 
L 5 HOH   127 427 374 HOH   HOH B . 
L 5 HOH   128 428 276 HOH   HOH B . 
L 5 HOH   129 429 33  HOH   HOH B . 
L 5 HOH   130 430 314 HOH   HOH B . 
L 5 HOH   131 431 186 HOH   HOH B . 
L 5 HOH   132 432 109 HOH   HOH B . 
L 5 HOH   133 433 336 HOH   HOH B . 
L 5 HOH   134 434 318 HOH   HOH B . 
L 5 HOH   135 435 364 HOH   HOH B . 
L 5 HOH   136 436 363 HOH   HOH B . 
L 5 HOH   137 437 331 HOH   HOH B . 
L 5 HOH   138 438 347 HOH   HOH B . 
L 5 HOH   139 439 373 HOH   HOH B . 
L 5 HOH   140 440 55  HOH   HOH B . 
L 5 HOH   141 441 206 HOH   HOH B . 
L 5 HOH   142 442 110 HOH   HOH B . 
L 5 HOH   143 443 343 HOH   HOH B . 
L 5 HOH   144 444 408 HOH   HOH B . 
L 5 HOH   145 445 146 HOH   HOH B . 
L 5 HOH   146 446 141 HOH   HOH B . 
L 5 HOH   147 447 380 HOH   HOH B . 
L 5 HOH   148 448 290 HOH   HOH B . 
L 5 HOH   149 449 411 HOH   HOH B . 
L 5 HOH   150 450 311 HOH   HOH B . 
L 5 HOH   151 451 315 HOH   HOH B . 
L 5 HOH   152 452 270 HOH   HOH B . 
L 5 HOH   153 453 113 HOH   HOH B . 
L 5 HOH   154 454 381 HOH   HOH B . 
L 5 HOH   155 455 188 HOH   HOH B . 
L 5 HOH   156 456 344 HOH   HOH B . 
L 5 HOH   157 457 375 HOH   HOH B . 
L 5 HOH   158 458 285 HOH   HOH B . 
L 5 HOH   159 459 163 HOH   HOH B . 
L 5 HOH   160 460 251 HOH   HOH B . 
L 5 HOH   161 461 321 HOH   HOH B . 
L 5 HOH   162 462 214 HOH   HOH B . 
L 5 HOH   163 463 351 HOH   HOH B . 
L 5 HOH   164 464 352 HOH   HOH B . 
L 5 HOH   165 465 349 HOH   HOH B . 
L 5 HOH   166 466 312 HOH   HOH B . 
L 5 HOH   167 467 282 HOH   HOH B . 
L 5 HOH   168 468 377 HOH   HOH B . 
L 5 HOH   169 469 281 HOH   HOH B . 
L 5 HOH   170 470 387 HOH   HOH B . 
L 5 HOH   171 471 286 HOH   HOH B . 
L 5 HOH   172 472 341 HOH   HOH B . 
L 5 HOH   173 473 111 HOH   HOH B . 
L 5 HOH   174 474 263 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 GLU 47  ? CD  ? A GLU 67  CD  
7  1 Y 1 A GLU 47  ? OE1 ? A GLU 67  OE1 
8  1 Y 1 A GLU 47  ? OE2 ? A GLU 67  OE2 
9  1 Y 1 A LYS 69  ? CD  ? A LYS 89  CD  
10 1 Y 1 A LYS 69  ? CE  ? A LYS 89  CE  
11 1 Y 1 A LYS 69  ? NZ  ? A LYS 89  NZ  
12 1 Y 1 A GLN 79  ? CG  ? A GLN 99  CG  
13 1 Y 1 A GLN 79  ? CD  ? A GLN 99  CD  
14 1 Y 1 A GLN 79  ? OE1 ? A GLN 99  OE1 
15 1 Y 1 A GLN 79  ? NE2 ? A GLN 99  NE2 
16 1 Y 1 A LYS 136 ? NZ  ? A LYS 156 NZ  
17 1 Y 1 A GLU 157 ? CD  ? A GLU 177 CD  
18 1 Y 1 A GLU 157 ? OE1 ? A GLU 177 OE1 
19 1 Y 1 A GLU 157 ? OE2 ? A GLU 177 OE2 
20 1 Y 1 B THR 10  ? OG1 ? B THR 30  OG1 
21 1 Y 1 B THR 10  ? CG2 ? B THR 30  CG2 
22 1 Y 1 B GLU 12  ? CG  ? B GLU 32  CG  
23 1 Y 1 B GLU 12  ? CD  ? B GLU 32  CD  
24 1 Y 1 B GLU 12  ? OE1 ? B GLU 32  OE1 
25 1 Y 1 B GLU 12  ? OE2 ? B GLU 32  OE2 
26 1 Y 1 B GLN 16  ? CD  ? B GLN 36  CD  
27 1 Y 1 B GLN 16  ? OE1 ? B GLN 36  OE1 
28 1 Y 1 B GLN 16  ? NE2 ? B GLN 36  NE2 
29 1 Y 1 B LYS 25  ? CD  ? B LYS 45  CD  
30 1 Y 1 B LYS 25  ? CE  ? B LYS 45  CE  
31 1 Y 1 B LYS 25  ? NZ  ? B LYS 45  NZ  
32 1 Y 1 B GLU 47  ? CD  ? B GLU 67  CD  
33 1 Y 1 B GLU 47  ? OE1 ? B GLU 67  OE1 
34 1 Y 1 B GLU 47  ? OE2 ? B GLU 67  OE2 
35 1 Y 1 B GLU 68  ? CG  ? B GLU 88  CG  
36 1 Y 1 B GLU 68  ? CD  ? B GLU 88  CD  
37 1 Y 1 B GLU 68  ? OE1 ? B GLU 88  OE1 
38 1 Y 1 B GLU 68  ? OE2 ? B GLU 88  OE2 
39 1 Y 1 B GLU 154 ? CD  ? B GLU 174 CD  
40 1 Y 1 B GLU 154 ? OE1 ? B GLU 174 OE1 
41 1 Y 1 B GLU 154 ? OE2 ? B GLU 174 OE2 
42 1 Y 1 B GLU 157 ? CD  ? B GLU 177 CD  
43 1 Y 1 B GLU 157 ? OE1 ? B GLU 177 OE1 
44 1 Y 1 B GLU 157 ? OE2 ? B GLU 177 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 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? 'Jan 10, 2022'      1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? v0.7.7              2 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? v2.8.3              3 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? v1.20.1-4487        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                   93.64 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9F8L 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     82.995 
_cell.length_a_esd                 ? 
_cell.length_b                     69.369 
_cell.length_b_esd                 ? 
_cell.length_c                     69.182 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9F8L 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9F8L 
_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             2.37 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.2 
_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    
'15% (w/v) PEG monomethyl ether, 0.1 M MES pH 6.14, 0.122 M ammonium acetate, 5% (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         2022-05-19 
_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                                       9F8L 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.38 
_reflns.d_resolution_low                               53.18 
_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                                     79713 
_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                           99.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.051 
_reflns.pdbx_Rpim_I_all                                0.019 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_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                              0.047 
_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                                    1.38 
_reflns_shell.d_res_low                                     1.40 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.1 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3936 
_reflns_shell.percent_possible_obs                          ? 
_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                               6.9 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.741 
_reflns_shell.pdbx_Rpim_I_all                               0.278 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.897 
_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                                  0.686 
_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                               25.879 
_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                                 9F8L 
_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                            1.38 
_refine.ls_d_res_low                             42.99 
_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                     79659 
_refine.ls_number_reflns_R_free                  3961 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.99 
_refine.ls_percent_reflns_R_free                 4.97 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1386 
_refine.ls_R_factor_R_free                       0.1641 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1373 
_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                          1.36 
_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                 16.79 
_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.pdbx_number_atoms_protein        2548 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         100 
_refine_hist.number_atoms_solvent             346 
_refine_hist.number_atoms_total               2994 
_refine_hist.d_res_high                       1.38 
_refine_hist.d_res_low                        42.99 
# 
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  ? 2904 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.172  ? 3953 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 17.623 ? 1071 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.085  ? 371  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.011  ? 526  ? 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' 1.38 1.40  . . 122 2657 99.00  . . . . 0.2256 . . . . . . . . . . . 0.2921 
'X-RAY DIFFRACTION' 1.40 1.41  . . 130 2722 99.00  . . . . 0.2009 . . . . . . . . . . . 0.2360 
'X-RAY DIFFRACTION' 1.41 1.43  . . 157 2682 99.00  . . . . 0.1766 . . . . . . . . . . . 0.2190 
'X-RAY DIFFRACTION' 1.43 1.45  . . 136 2697 99.00  . . . . 0.1603 . . . . . . . . . . . 0.2263 
'X-RAY DIFFRACTION' 1.45 1.47  . . 152 2712 99.00  . . . . 0.1589 . . . . . . . . . . . 0.2032 
'X-RAY DIFFRACTION' 1.47 1.49  . . 141 2670 99.00  . . . . 0.1558 . . . . . . . . . . . 0.2104 
'X-RAY DIFFRACTION' 1.49 1.52  . . 156 2661 99.00  . . . . 0.1470 . . . . . . . . . . . 0.1965 
'X-RAY DIFFRACTION' 1.52 1.54  . . 172 2687 99.00  . . . . 0.1475 . . . . . . . . . . . 0.1987 
'X-RAY DIFFRACTION' 1.54 1.57  . . 131 2693 99.00  . . . . 0.1613 . . . . . . . . . . . 0.2105 
'X-RAY DIFFRACTION' 1.57 1.60  . . 135 2710 99.00  . . . . 0.1550 . . . . . . . . . . . 0.1670 
'X-RAY DIFFRACTION' 1.60 1.63  . . 127 2647 98.00  . . . . 0.1419 . . . . . . . . . . . 0.1714 
'X-RAY DIFFRACTION' 1.63 1.66  . . 149 2688 99.00  . . . . 0.1276 . . . . . . . . . . . 0.1581 
'X-RAY DIFFRACTION' 1.66 1.70  . . 136 2723 99.00  . . . . 0.1232 . . . . . . . . . . . 0.1639 
'X-RAY DIFFRACTION' 1.70 1.74  . . 142 2697 99.00  . . . . 0.1137 . . . . . . . . . . . 0.1542 
'X-RAY DIFFRACTION' 1.74 1.78  . . 154 2695 99.00  . . . . 0.1116 . . . . . . . . . . . 0.1468 
'X-RAY DIFFRACTION' 1.78 1.83  . . 129 2699 99.00  . . . . 0.1114 . . . . . . . . . . . 0.1525 
'X-RAY DIFFRACTION' 1.83 1.88  . . 131 2724 99.00  . . . . 0.1236 . . . . . . . . . . . 0.1800 
'X-RAY DIFFRACTION' 1.88 1.94  . . 137 2696 99.00  . . . . 0.1283 . . . . . . . . . . . 0.1510 
'X-RAY DIFFRACTION' 1.94 2.01  . . 149 2716 99.00  . . . . 0.1247 . . . . . . . . . . . 0.1442 
'X-RAY DIFFRACTION' 2.01 2.09  . . 134 2742 99.00  . . . . 0.1233 . . . . . . . . . . . 0.1601 
'X-RAY DIFFRACTION' 2.09 2.19  . . 134 2703 99.00  . . . . 0.1269 . . . . . . . . . . . 0.1593 
'X-RAY DIFFRACTION' 2.19 2.30  . . 119 2688 98.00  . . . . 0.1264 . . . . . . . . . . . 0.1604 
'X-RAY DIFFRACTION' 2.30 2.45  . . 145 2747 100.00 . . . . 0.1253 . . . . . . . . . . . 0.1610 
'X-RAY DIFFRACTION' 2.45 2.64  . . 135 2708 100.00 . . . . 0.1320 . . . . . . . . . . . 0.1803 
'X-RAY DIFFRACTION' 2.64 2.90  . . 173 2708 99.00  . . . . 0.1338 . . . . . . . . . . . 0.1545 
'X-RAY DIFFRACTION' 2.90 3.32  . . 162 2723 99.00  . . . . 0.1408 . . . . . . . . . . . 0.1670 
'X-RAY DIFFRACTION' 3.32 4.19  . . 133 2708 98.00  . . . . 0.1274 . . . . . . . . . . . 0.1434 
'X-RAY DIFFRACTION' 4.19 42.99 . . 140 2795 99.00  . . . . 0.1639 . . . . . . . . . . . 0.1654 
# 
_struct.entry_id                     9F8L 
_struct.title                        
;Crystal Structure of PhzA/B from Burkholderia cepacia R18194 in complex with [6-Hydroxy-2-(4-hydroxyphenyl)benzo[b]thiophen-3-yl](3-hydroxyphenyl)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        9F8L 
_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 4 ? 
F N N 2 ? 
G N N 4 ? 
H N N 3 ? 
I N N 4 ? 
J N N 4 ? 
K N N 5 ? 
L N N 5 ? 
# 
_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 9F8L A 21 ? 185 ? Q396C9 1 ? 165 ? 1 165 
2 1 9F8L 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 9F8L MET A 1  ? UNP Q396C9 ? ? 'initiating methionine' -19 1  
1 9F8L GLY A 2  ? UNP Q396C9 ? ? 'expression tag'        -18 2  
1 9F8L SER A 3  ? UNP Q396C9 ? ? 'expression tag'        -17 3  
1 9F8L SER A 4  ? UNP Q396C9 ? ? 'expression tag'        -16 4  
1 9F8L HIS A 5  ? UNP Q396C9 ? ? 'expression tag'        -15 5  
1 9F8L HIS A 6  ? UNP Q396C9 ? ? 'expression tag'        -14 6  
1 9F8L HIS A 7  ? UNP Q396C9 ? ? 'expression tag'        -13 7  
1 9F8L HIS A 8  ? UNP Q396C9 ? ? 'expression tag'        -12 8  
1 9F8L HIS A 9  ? UNP Q396C9 ? ? 'expression tag'        -11 9  
1 9F8L HIS A 10 ? UNP Q396C9 ? ? 'expression tag'        -10 10 
1 9F8L SER A 11 ? UNP Q396C9 ? ? 'expression tag'        -9  11 
1 9F8L SER A 12 ? UNP Q396C9 ? ? 'expression tag'        -8  12 
1 9F8L GLY A 13 ? UNP Q396C9 ? ? 'expression tag'        -7  13 
1 9F8L LEU A 14 ? UNP Q396C9 ? ? 'expression tag'        -6  14 
1 9F8L VAL A 15 ? UNP Q396C9 ? ? 'expression tag'        -5  15 
1 9F8L PRO A 16 ? UNP Q396C9 ? ? 'expression tag'        -4  16 
1 9F8L ARG A 17 ? UNP Q396C9 ? ? 'expression tag'        -3  17 
1 9F8L GLY A 18 ? UNP Q396C9 ? ? 'expression tag'        -2  18 
1 9F8L SER A 19 ? UNP Q396C9 ? ? 'expression tag'        -1  19 
1 9F8L HIS A 20 ? UNP Q396C9 ? ? 'expression tag'        0   20 
2 9F8L MET B 1  ? UNP Q396C9 ? ? 'initiating methionine' -19 21 
2 9F8L GLY B 2  ? UNP Q396C9 ? ? 'expression tag'        -18 22 
2 9F8L SER B 3  ? UNP Q396C9 ? ? 'expression tag'        -17 23 
2 9F8L SER B 4  ? UNP Q396C9 ? ? 'expression tag'        -16 24 
2 9F8L HIS B 5  ? UNP Q396C9 ? ? 'expression tag'        -15 25 
2 9F8L HIS B 6  ? UNP Q396C9 ? ? 'expression tag'        -14 26 
2 9F8L HIS B 7  ? UNP Q396C9 ? ? 'expression tag'        -13 27 
2 9F8L HIS B 8  ? UNP Q396C9 ? ? 'expression tag'        -12 28 
2 9F8L HIS B 9  ? UNP Q396C9 ? ? 'expression tag'        -11 29 
2 9F8L HIS B 10 ? UNP Q396C9 ? ? 'expression tag'        -10 30 
2 9F8L SER B 11 ? UNP Q396C9 ? ? 'expression tag'        -9  31 
2 9F8L SER B 12 ? UNP Q396C9 ? ? 'expression tag'        -8  32 
2 9F8L GLY B 13 ? UNP Q396C9 ? ? 'expression tag'        -7  33 
2 9F8L LEU B 14 ? UNP Q396C9 ? ? 'expression tag'        -6  34 
2 9F8L VAL B 15 ? UNP Q396C9 ? ? 'expression tag'        -5  35 
2 9F8L PRO B 16 ? UNP Q396C9 ? ? 'expression tag'        -4  36 
2 9F8L ARG B 17 ? UNP Q396C9 ? ? 'expression tag'        -3  37 
2 9F8L GLY B 18 ? UNP Q396C9 ? ? 'expression tag'        -2  38 
2 9F8L SER B 19 ? UNP Q396C9 ? ? 'expression tag'        -1  39 
2 9F8L HIS B 20 ? UNP Q396C9 ? ? 'expression tag'        0   40 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 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)' 5770  ? 
1 MORE         -9    ? 
1 'SSA (A^2)'  14560 ? 
2 'ABSA (A^2)' 6210  ? 
2 MORE         -7    ? 
2 'SSA (A^2)'  14200 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1,2 A,C,D,E,K     
2 1,3 B,F,G,H,I,J,L 
# 
loop_
_pdbx_struct_assembly_auth_evidence.id 
_pdbx_struct_assembly_auth_evidence.assembly_id 
_pdbx_struct_assembly_auth_evidence.experimental_support 
_pdbx_struct_assembly_auth_evidence.details 
1 1 'gel filtration' ? 
2 2 'gel filtration' ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z       1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 2_655 -x+1,y,-z   -1.0000000000 0.0000000000 0.0000000000 82.9950000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000  
3 'crystal symmetry operation' 2_656 -x+1,y,-z+1 -1.0000000000 0.0000000000 0.0000000000 78.6028244985 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 69.0424356346 
# 
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 THR A 30  ? HIS A 52  ? THR A 10  HIS A 32  1 ? 23 
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 SER B 31  ? HIS B 52  ? SER B 11  HIS B 32  1 ? 22 
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 ? PHE A 112 ? VAL A 85  PHE A 92  
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 ? GLU B 113 ? VAL B 85  GLU B 93  
# 
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 PHE A 161 ? O PHE A 141 N LEU A 145 ? N LEU A 125 
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                   9F8L 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 HE B ARG 160 ? ? O B HOH 301 ? ? 1.57 
2 1 O  B HOH 448 ? ? O B HOH 474 ? ? 2.18 
3 1 O  A HOH 408 ? ? O B HOH 329 ? ? 2.19 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 B GOL 205 ? J GOL . 
2 1 A HOH 441 ? K HOH . 
3 1 B HOH 440 ? L HOH . 
# 
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 B MET -19 ? B MET 1  
31 1 Y 1 B GLY -18 ? B GLY 2  
32 1 Y 1 B SER -17 ? B SER 3  
33 1 Y 1 B SER -16 ? B SER 4  
34 1 Y 1 B HIS -15 ? B HIS 5  
35 1 Y 1 B HIS -14 ? B HIS 6  
36 1 Y 1 B HIS -13 ? B HIS 7  
37 1 Y 1 B HIS -12 ? B HIS 8  
38 1 Y 1 B HIS -11 ? B HIS 9  
39 1 Y 1 B HIS -10 ? B HIS 10 
40 1 Y 1 B SER -9  ? B SER 11 
41 1 Y 1 B SER -8  ? B SER 12 
42 1 Y 1 B GLY -7  ? B GLY 13 
43 1 Y 1 B LEU -6  ? B LEU 14 
44 1 Y 1 B VAL -5  ? B VAL 15 
45 1 Y 1 B PRO -4  ? B PRO 16 
46 1 Y 1 B ARG -3  ? B ARG 17 
47 1 Y 1 B GLY -2  ? B GLY 18 
48 1 Y 1 B SER -1  ? B SER 19 
49 1 Y 1 B HIS 0   ? B HIS 20 
50 1 Y 1 B MET 1   ? B MET 21 
51 1 Y 1 B SER 2   ? B SER 22 
52 1 Y 1 B ASP 3   ? B ASP 23 
53 1 Y 1 B VAL 4   ? B VAL 24 
54 1 Y 1 B GLU 5   ? B GLU 25 
55 1 Y 1 B SER 6   ? B SER 26 
56 1 Y 1 B LEU 7   ? B LEU 27 
57 1 Y 1 B GLU 8   ? B GLU 28 
58 1 Y 1 B ASN 9   ? B ASN 29 
# 
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 
A1IAL C12  C Y N 1   
A1IAL C11  C Y N 2   
A1IAL C17  C Y N 3   
A1IAL C15  C Y N 4   
A1IAL C13  C Y N 5   
A1IAL C14  C Y N 6   
A1IAL C10  C Y N 7   
A1IAL C02  C N N 8   
A1IAL C03  C Y N 9   
A1IAL C04  C Y N 10  
A1IAL C05  C Y N 11  
A1IAL C06  C Y N 12  
A1IAL C07  C Y N 13  
A1IAL C09  C Y N 14  
A1IAL C18  C Y N 15  
A1IAL C20  C Y N 16  
A1IAL C21  C Y N 17  
A1IAL C22  C Y N 18  
A1IAL C24  C Y N 19  
A1IAL C25  C Y N 20  
A1IAL C26  C Y N 21  
A1IAL O01  O N N 22  
A1IAL O08  O N N 23  
A1IAL O16  O N N 24  
A1IAL O23  O N N 25  
A1IAL S19  S Y N 26  
A1IAL H171 H N N 27  
A1IAL H131 H N N 28  
A1IAL H141 H N N 29  
A1IAL H041 H N N 30  
A1IAL H051 H N N 31  
A1IAL H061 H N N 32  
A1IAL H091 H N N 33  
A1IAL H181 H N N 34  
A1IAL H211 H N N 35  
A1IAL H241 H N N 36  
A1IAL H251 H N N 37  
A1IAL H081 H N N 38  
A1IAL H161 H N N 39  
A1IAL H231 H N N 40  
ALA   N    N N N 41  
ALA   CA   C N S 42  
ALA   C    C N N 43  
ALA   O    O N N 44  
ALA   CB   C N N 45  
ALA   OXT  O N N 46  
ALA   H    H N N 47  
ALA   H2   H N N 48  
ALA   HA   H N N 49  
ALA   HB1  H N N 50  
ALA   HB2  H N N 51  
ALA   HB3  H N N 52  
ALA   HXT  H N N 53  
ARG   N    N N N 54  
ARG   CA   C N S 55  
ARG   C    C N N 56  
ARG   O    O N N 57  
ARG   CB   C N N 58  
ARG   CG   C N N 59  
ARG   CD   C N N 60  
ARG   NE   N N N 61  
ARG   CZ   C N N 62  
ARG   NH1  N N N 63  
ARG   NH2  N N N 64  
ARG   OXT  O N N 65  
ARG   H    H N N 66  
ARG   H2   H N N 67  
ARG   HA   H N N 68  
ARG   HB2  H N N 69  
ARG   HB3  H N N 70  
ARG   HG2  H N N 71  
ARG   HG3  H N N 72  
ARG   HD2  H N N 73  
ARG   HD3  H N N 74  
ARG   HE   H N N 75  
ARG   HH11 H N N 76  
ARG   HH12 H N N 77  
ARG   HH21 H N N 78  
ARG   HH22 H N N 79  
ARG   HXT  H N N 80  
ASN   N    N N N 81  
ASN   CA   C N S 82  
ASN   C    C N N 83  
ASN   O    O N N 84  
ASN   CB   C N N 85  
ASN   CG   C N N 86  
ASN   OD1  O N N 87  
ASN   ND2  N N N 88  
ASN   OXT  O N N 89  
ASN   H    H N N 90  
ASN   H2   H N N 91  
ASN   HA   H N N 92  
ASN   HB2  H N N 93  
ASN   HB3  H N N 94  
ASN   HD21 H N N 95  
ASN   HD22 H N N 96  
ASN   HXT  H N N 97  
ASP   N    N N N 98  
ASP   CA   C N S 99  
ASP   C    C N N 100 
ASP   O    O N N 101 
ASP   CB   C N N 102 
ASP   CG   C N N 103 
ASP   OD1  O N N 104 
ASP   OD2  O N N 105 
ASP   OXT  O N N 106 
ASP   H    H N N 107 
ASP   H2   H N N 108 
ASP   HA   H N N 109 
ASP   HB2  H N N 110 
ASP   HB3  H N N 111 
ASP   HD2  H N N 112 
ASP   HXT  H N N 113 
CYS   N    N N N 114 
CYS   CA   C N R 115 
CYS   C    C N N 116 
CYS   O    O N N 117 
CYS   CB   C N N 118 
CYS   SG   S N N 119 
CYS   OXT  O N N 120 
CYS   H    H N N 121 
CYS   H2   H N N 122 
CYS   HA   H N N 123 
CYS   HB2  H N N 124 
CYS   HB3  H N N 125 
CYS   HG   H N N 126 
CYS   HXT  H N N 127 
GLN   N    N N N 128 
GLN   CA   C N S 129 
GLN   C    C N N 130 
GLN   O    O N N 131 
GLN   CB   C N N 132 
GLN   CG   C N N 133 
GLN   CD   C N N 134 
GLN   OE1  O N N 135 
GLN   NE2  N N N 136 
GLN   OXT  O N N 137 
GLN   H    H N N 138 
GLN   H2   H N N 139 
GLN   HA   H N N 140 
GLN   HB2  H N N 141 
GLN   HB3  H N N 142 
GLN   HG2  H N N 143 
GLN   HG3  H N N 144 
GLN   HE21 H N N 145 
GLN   HE22 H N N 146 
GLN   HXT  H N N 147 
GLU   N    N N N 148 
GLU   CA   C N S 149 
GLU   C    C N N 150 
GLU   O    O N N 151 
GLU   CB   C N N 152 
GLU   CG   C N N 153 
GLU   CD   C N N 154 
GLU   OE1  O N N 155 
GLU   OE2  O N N 156 
GLU   OXT  O N N 157 
GLU   H    H N N 158 
GLU   H2   H N N 159 
GLU   HA   H N N 160 
GLU   HB2  H N N 161 
GLU   HB3  H N N 162 
GLU   HG2  H N N 163 
GLU   HG3  H N N 164 
GLU   HE2  H N N 165 
GLU   HXT  H N N 166 
GLY   N    N N N 167 
GLY   CA   C N N 168 
GLY   C    C N N 169 
GLY   O    O N N 170 
GLY   OXT  O N N 171 
GLY   H    H N N 172 
GLY   H2   H N N 173 
GLY   HA2  H N N 174 
GLY   HA3  H N N 175 
GLY   HXT  H N N 176 
GOL   C1   C N N 177 
GOL   O1   O N N 178 
GOL   C2   C N N 179 
GOL   O2   O N N 180 
GOL   C3   C N N 181 
GOL   O3   O N N 182 
GOL   H11  H N N 183 
GOL   H12  H N N 184 
GOL   HO1  H N N 185 
GOL   H2   H N N 186 
GOL   HO2  H N N 187 
GOL   H31  H N N 188 
GOL   H32  H N N 189 
GOL   HO3  H N N 190 
HIS   N    N N N 191 
HIS   CA   C N S 192 
HIS   C    C N N 193 
HIS   O    O N N 194 
HIS   CB   C N N 195 
HIS   CG   C Y N 196 
HIS   ND1  N Y N 197 
HIS   CD2  C Y N 198 
HIS   CE1  C Y N 199 
HIS   NE2  N Y N 200 
HIS   OXT  O N N 201 
HIS   H    H N N 202 
HIS   H2   H N N 203 
HIS   HA   H N N 204 
HIS   HB2  H N N 205 
HIS   HB3  H N N 206 
HIS   HD1  H N N 207 
HIS   HD2  H N N 208 
HIS   HE1  H N N 209 
HIS   HE2  H N N 210 
HIS   HXT  H N N 211 
HOH   O    O N N 212 
HOH   H1   H N N 213 
HOH   H2   H N N 214 
ILE   N    N N N 215 
ILE   CA   C N S 216 
ILE   C    C N N 217 
ILE   O    O N N 218 
ILE   CB   C N S 219 
ILE   CG1  C N N 220 
ILE   CG2  C N N 221 
ILE   CD1  C N N 222 
ILE   OXT  O N N 223 
ILE   H    H N N 224 
ILE   H2   H N N 225 
ILE   HA   H N N 226 
ILE   HB   H N N 227 
ILE   HG12 H N N 228 
ILE   HG13 H N N 229 
ILE   HG21 H N N 230 
ILE   HG22 H N N 231 
ILE   HG23 H N N 232 
ILE   HD11 H N N 233 
ILE   HD12 H N N 234 
ILE   HD13 H N N 235 
ILE   HXT  H N N 236 
LEU   N    N N N 237 
LEU   CA   C N S 238 
LEU   C    C N N 239 
LEU   O    O N N 240 
LEU   CB   C N N 241 
LEU   CG   C N N 242 
LEU   CD1  C N N 243 
LEU   CD2  C N N 244 
LEU   OXT  O N N 245 
LEU   H    H N N 246 
LEU   H2   H N N 247 
LEU   HA   H N N 248 
LEU   HB2  H N N 249 
LEU   HB3  H N N 250 
LEU   HG   H N N 251 
LEU   HD11 H N N 252 
LEU   HD12 H N N 253 
LEU   HD13 H N N 254 
LEU   HD21 H N N 255 
LEU   HD22 H N N 256 
LEU   HD23 H N N 257 
LEU   HXT  H N N 258 
LYS   N    N N N 259 
LYS   CA   C N S 260 
LYS   C    C N N 261 
LYS   O    O N N 262 
LYS   CB   C N N 263 
LYS   CG   C N N 264 
LYS   CD   C N N 265 
LYS   CE   C N N 266 
LYS   NZ   N N N 267 
LYS   OXT  O N N 268 
LYS   H    H N N 269 
LYS   H2   H N N 270 
LYS   HA   H N N 271 
LYS   HB2  H N N 272 
LYS   HB3  H N N 273 
LYS   HG2  H N N 274 
LYS   HG3  H N N 275 
LYS   HD2  H N N 276 
LYS   HD3  H N N 277 
LYS   HE2  H N N 278 
LYS   HE3  H N N 279 
LYS   HZ1  H N N 280 
LYS   HZ2  H N N 281 
LYS   HZ3  H N N 282 
LYS   HXT  H N N 283 
MES   O1   O N N 284 
MES   C2   C N N 285 
MES   C3   C N N 286 
MES   N4   N N N 287 
MES   C5   C N N 288 
MES   C6   C N N 289 
MES   C7   C N N 290 
MES   C8   C N N 291 
MES   S    S N N 292 
MES   O1S  O N N 293 
MES   O2S  O N N 294 
MES   O3S  O N N 295 
MES   H21  H N N 296 
MES   H22  H N N 297 
MES   H31  H N N 298 
MES   H32  H N N 299 
MES   HN4  H N N 300 
MES   H51  H N N 301 
MES   H52  H N N 302 
MES   H61  H N N 303 
MES   H62  H N N 304 
MES   H71  H N N 305 
MES   H72  H N N 306 
MES   H81  H N N 307 
MES   H82  H N N 308 
MET   N    N N N 309 
MET   CA   C N S 310 
MET   C    C N N 311 
MET   O    O N N 312 
MET   CB   C N N 313 
MET   CG   C N N 314 
MET   SD   S N N 315 
MET   CE   C N N 316 
MET   OXT  O N N 317 
MET   H    H N N 318 
MET   H2   H N N 319 
MET   HA   H N N 320 
MET   HB2  H N N 321 
MET   HB3  H N N 322 
MET   HG2  H N N 323 
MET   HG3  H N N 324 
MET   HE1  H N N 325 
MET   HE2  H N N 326 
MET   HE3  H N N 327 
MET   HXT  H N N 328 
PHE   N    N N N 329 
PHE   CA   C N S 330 
PHE   C    C N N 331 
PHE   O    O N N 332 
PHE   CB   C N N 333 
PHE   CG   C Y N 334 
PHE   CD1  C Y N 335 
PHE   CD2  C Y N 336 
PHE   CE1  C Y N 337 
PHE   CE2  C Y N 338 
PHE   CZ   C Y N 339 
PHE   OXT  O N N 340 
PHE   H    H N N 341 
PHE   H2   H N N 342 
PHE   HA   H N N 343 
PHE   HB2  H N N 344 
PHE   HB3  H N N 345 
PHE   HD1  H N N 346 
PHE   HD2  H N N 347 
PHE   HE1  H N N 348 
PHE   HE2  H N N 349 
PHE   HZ   H N N 350 
PHE   HXT  H N N 351 
PRO   N    N N N 352 
PRO   CA   C N S 353 
PRO   C    C N N 354 
PRO   O    O N N 355 
PRO   CB   C N N 356 
PRO   CG   C N N 357 
PRO   CD   C N N 358 
PRO   OXT  O N N 359 
PRO   H    H N N 360 
PRO   HA   H N N 361 
PRO   HB2  H N N 362 
PRO   HB3  H N N 363 
PRO   HG2  H N N 364 
PRO   HG3  H N N 365 
PRO   HD2  H N N 366 
PRO   HD3  H N N 367 
PRO   HXT  H N N 368 
SER   N    N N N 369 
SER   CA   C N S 370 
SER   C    C N N 371 
SER   O    O N N 372 
SER   CB   C N N 373 
SER   OG   O N N 374 
SER   OXT  O N N 375 
SER   H    H N N 376 
SER   H2   H N N 377 
SER   HA   H N N 378 
SER   HB2  H N N 379 
SER   HB3  H N N 380 
SER   HG   H N N 381 
SER   HXT  H N N 382 
THR   N    N N N 383 
THR   CA   C N S 384 
THR   C    C N N 385 
THR   O    O N N 386 
THR   CB   C N R 387 
THR   OG1  O N N 388 
THR   CG2  C N N 389 
THR   OXT  O N N 390 
THR   H    H N N 391 
THR   H2   H N N 392 
THR   HA   H N N 393 
THR   HB   H N N 394 
THR   HG1  H N N 395 
THR   HG21 H N N 396 
THR   HG22 H N N 397 
THR   HG23 H N N 398 
THR   HXT  H N N 399 
TRP   N    N N N 400 
TRP   CA   C N S 401 
TRP   C    C N N 402 
TRP   O    O N N 403 
TRP   CB   C N N 404 
TRP   CG   C Y N 405 
TRP   CD1  C Y N 406 
TRP   CD2  C Y N 407 
TRP   NE1  N Y N 408 
TRP   CE2  C Y N 409 
TRP   CE3  C Y N 410 
TRP   CZ2  C Y N 411 
TRP   CZ3  C Y N 412 
TRP   CH2  C Y N 413 
TRP   OXT  O N N 414 
TRP   H    H N N 415 
TRP   H2   H N N 416 
TRP   HA   H N N 417 
TRP   HB2  H N N 418 
TRP   HB3  H N N 419 
TRP   HD1  H N N 420 
TRP   HE1  H N N 421 
TRP   HE3  H N N 422 
TRP   HZ2  H N N 423 
TRP   HZ3  H N N 424 
TRP   HH2  H N N 425 
TRP   HXT  H N N 426 
TYR   N    N N N 427 
TYR   CA   C N S 428 
TYR   C    C N N 429 
TYR   O    O N N 430 
TYR   CB   C N N 431 
TYR   CG   C Y N 432 
TYR   CD1  C Y N 433 
TYR   CD2  C Y N 434 
TYR   CE1  C Y N 435 
TYR   CE2  C Y N 436 
TYR   CZ   C Y N 437 
TYR   OH   O N N 438 
TYR   OXT  O N N 439 
TYR   H    H N N 440 
TYR   H2   H N N 441 
TYR   HA   H N N 442 
TYR   HB2  H N N 443 
TYR   HB3  H N N 444 
TYR   HD1  H N N 445 
TYR   HD2  H N N 446 
TYR   HE1  H N N 447 
TYR   HE2  H N N 448 
TYR   HH   H N N 449 
TYR   HXT  H N N 450 
VAL   N    N N N 451 
VAL   CA   C N S 452 
VAL   C    C N N 453 
VAL   O    O N N 454 
VAL   CB   C N N 455 
VAL   CG1  C N N 456 
VAL   CG2  C N N 457 
VAL   OXT  O N N 458 
VAL   H    H N N 459 
VAL   H2   H N N 460 
VAL   HA   H N N 461 
VAL   HB   H N N 462 
VAL   HG11 H N N 463 
VAL   HG12 H N N 464 
VAL   HG13 H N N 465 
VAL   HG21 H N N 466 
VAL   HG22 H N N 467 
VAL   HG23 H N N 468 
VAL   HXT  H N N 469 
# 
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 
A1IAL C14 C13  doub Y N 1   
A1IAL C14 C15  sing Y N 2   
A1IAL C13 C12  sing Y N 3   
A1IAL O16 C15  sing N N 4   
A1IAL S19 C20  sing Y N 5   
A1IAL S19 C11  sing Y N 6   
A1IAL C15 C17  doub Y N 7   
A1IAL C21 C20  doub Y N 8   
A1IAL C21 C22  sing Y N 9   
A1IAL C12 C11  sing N N 10  
A1IAL C12 C18  doub Y N 11  
A1IAL C05 C04  doub Y N 12  
A1IAL C05 C06  sing Y N 13  
A1IAL C20 C26  sing Y N 14  
A1IAL C11 C10  doub Y N 15  
A1IAL O23 C22  sing N N 16  
A1IAL C04 C03  sing Y N 17  
A1IAL C22 C24  doub Y N 18  
A1IAL C17 C18  sing Y N 19  
A1IAL C06 C07  doub Y N 20  
A1IAL C26 C10  sing Y N 21  
A1IAL C26 C25  doub Y N 22  
A1IAL C10 C02  sing N N 23  
A1IAL C24 C25  sing Y N 24  
A1IAL C03 C02  sing N N 25  
A1IAL C03 C09  doub Y N 26  
A1IAL C02 O01  doub N N 27  
A1IAL C07 C09  sing Y N 28  
A1IAL C07 O08  sing N N 29  
A1IAL C17 H171 sing N N 30  
A1IAL C13 H131 sing N N 31  
A1IAL C14 H141 sing N N 32  
A1IAL C04 H041 sing N N 33  
A1IAL C05 H051 sing N N 34  
A1IAL C06 H061 sing N N 35  
A1IAL C09 H091 sing N N 36  
A1IAL C18 H181 sing N N 37  
A1IAL C21 H211 sing N N 38  
A1IAL C24 H241 sing N N 39  
A1IAL C25 H251 sing N N 40  
A1IAL O08 H081 sing N N 41  
A1IAL O16 H161 sing N N 42  
A1IAL O23 H231 sing N N 43  
ALA   N   CA   sing N N 44  
ALA   N   H    sing N N 45  
ALA   N   H2   sing N N 46  
ALA   CA  C    sing N N 47  
ALA   CA  CB   sing N N 48  
ALA   CA  HA   sing N N 49  
ALA   C   O    doub N N 50  
ALA   C   OXT  sing N N 51  
ALA   CB  HB1  sing N N 52  
ALA   CB  HB2  sing N N 53  
ALA   CB  HB3  sing N N 54  
ALA   OXT HXT  sing N N 55  
ARG   N   CA   sing N N 56  
ARG   N   H    sing N N 57  
ARG   N   H2   sing N N 58  
ARG   CA  C    sing N N 59  
ARG   CA  CB   sing N N 60  
ARG   CA  HA   sing N N 61  
ARG   C   O    doub N N 62  
ARG   C   OXT  sing N N 63  
ARG   CB  CG   sing N N 64  
ARG   CB  HB2  sing N N 65  
ARG   CB  HB3  sing N N 66  
ARG   CG  CD   sing N N 67  
ARG   CG  HG2  sing N N 68  
ARG   CG  HG3  sing N N 69  
ARG   CD  NE   sing N N 70  
ARG   CD  HD2  sing N N 71  
ARG   CD  HD3  sing N N 72  
ARG   NE  CZ   sing N N 73  
ARG   NE  HE   sing N N 74  
ARG   CZ  NH1  sing N N 75  
ARG   CZ  NH2  doub N N 76  
ARG   NH1 HH11 sing N N 77  
ARG   NH1 HH12 sing N N 78  
ARG   NH2 HH21 sing N N 79  
ARG   NH2 HH22 sing N N 80  
ARG   OXT HXT  sing N N 81  
ASN   N   CA   sing N N 82  
ASN   N   H    sing N N 83  
ASN   N   H2   sing N N 84  
ASN   CA  C    sing N N 85  
ASN   CA  CB   sing N N 86  
ASN   CA  HA   sing N N 87  
ASN   C   O    doub N N 88  
ASN   C   OXT  sing N N 89  
ASN   CB  CG   sing N N 90  
ASN   CB  HB2  sing N N 91  
ASN   CB  HB3  sing N N 92  
ASN   CG  OD1  doub N N 93  
ASN   CG  ND2  sing N N 94  
ASN   ND2 HD21 sing N N 95  
ASN   ND2 HD22 sing N N 96  
ASN   OXT HXT  sing N N 97  
ASP   N   CA   sing N N 98  
ASP   N   H    sing N N 99  
ASP   N   H2   sing N N 100 
ASP   CA  C    sing N N 101 
ASP   CA  CB   sing N N 102 
ASP   CA  HA   sing N N 103 
ASP   C   O    doub N N 104 
ASP   C   OXT  sing N N 105 
ASP   CB  CG   sing N N 106 
ASP   CB  HB2  sing N N 107 
ASP   CB  HB3  sing N N 108 
ASP   CG  OD1  doub N N 109 
ASP   CG  OD2  sing N N 110 
ASP   OD2 HD2  sing N N 111 
ASP   OXT HXT  sing N N 112 
CYS   N   CA   sing N N 113 
CYS   N   H    sing N N 114 
CYS   N   H2   sing N N 115 
CYS   CA  C    sing N N 116 
CYS   CA  CB   sing N N 117 
CYS   CA  HA   sing N N 118 
CYS   C   O    doub N N 119 
CYS   C   OXT  sing N N 120 
CYS   CB  SG   sing N N 121 
CYS   CB  HB2  sing N N 122 
CYS   CB  HB3  sing N N 123 
CYS   SG  HG   sing N N 124 
CYS   OXT HXT  sing N N 125 
GLN   N   CA   sing N N 126 
GLN   N   H    sing N N 127 
GLN   N   H2   sing N N 128 
GLN   CA  C    sing N N 129 
GLN   CA  CB   sing N N 130 
GLN   CA  HA   sing N N 131 
GLN   C   O    doub N N 132 
GLN   C   OXT  sing N N 133 
GLN   CB  CG   sing N N 134 
GLN   CB  HB2  sing N N 135 
GLN   CB  HB3  sing N N 136 
GLN   CG  CD   sing N N 137 
GLN   CG  HG2  sing N N 138 
GLN   CG  HG3  sing N N 139 
GLN   CD  OE1  doub N N 140 
GLN   CD  NE2  sing N N 141 
GLN   NE2 HE21 sing N N 142 
GLN   NE2 HE22 sing N N 143 
GLN   OXT HXT  sing N N 144 
GLU   N   CA   sing N N 145 
GLU   N   H    sing N N 146 
GLU   N   H2   sing N N 147 
GLU   CA  C    sing N N 148 
GLU   CA  CB   sing N N 149 
GLU   CA  HA   sing N N 150 
GLU   C   O    doub N N 151 
GLU   C   OXT  sing N N 152 
GLU   CB  CG   sing N N 153 
GLU   CB  HB2  sing N N 154 
GLU   CB  HB3  sing N N 155 
GLU   CG  CD   sing N N 156 
GLU   CG  HG2  sing N N 157 
GLU   CG  HG3  sing N N 158 
GLU   CD  OE1  doub N N 159 
GLU   CD  OE2  sing N N 160 
GLU   OE2 HE2  sing N N 161 
GLU   OXT HXT  sing N N 162 
GLY   N   CA   sing N N 163 
GLY   N   H    sing N N 164 
GLY   N   H2   sing N N 165 
GLY   CA  C    sing N N 166 
GLY   CA  HA2  sing N N 167 
GLY   CA  HA3  sing N N 168 
GLY   C   O    doub N N 169 
GLY   C   OXT  sing N N 170 
GLY   OXT HXT  sing N N 171 
GOL   C1  O1   sing N N 172 
GOL   C1  C2   sing N N 173 
GOL   C1  H11  sing N N 174 
GOL   C1  H12  sing N N 175 
GOL   O1  HO1  sing N N 176 
GOL   C2  O2   sing N N 177 
GOL   C2  C3   sing N N 178 
GOL   C2  H2   sing N N 179 
GOL   O2  HO2  sing N N 180 
GOL   C3  O3   sing N N 181 
GOL   C3  H31  sing N N 182 
GOL   C3  H32  sing N N 183 
GOL   O3  HO3  sing N N 184 
HIS   N   CA   sing N N 185 
HIS   N   H    sing N N 186 
HIS   N   H2   sing N N 187 
HIS   CA  C    sing N N 188 
HIS   CA  CB   sing N N 189 
HIS   CA  HA   sing N N 190 
HIS   C   O    doub N N 191 
HIS   C   OXT  sing N N 192 
HIS   CB  CG   sing N N 193 
HIS   CB  HB2  sing N N 194 
HIS   CB  HB3  sing N N 195 
HIS   CG  ND1  sing Y N 196 
HIS   CG  CD2  doub Y N 197 
HIS   ND1 CE1  doub Y N 198 
HIS   ND1 HD1  sing N N 199 
HIS   CD2 NE2  sing Y N 200 
HIS   CD2 HD2  sing N N 201 
HIS   CE1 NE2  sing Y N 202 
HIS   CE1 HE1  sing N N 203 
HIS   NE2 HE2  sing N N 204 
HIS   OXT HXT  sing N N 205 
HOH   O   H1   sing N N 206 
HOH   O   H2   sing N N 207 
ILE   N   CA   sing N N 208 
ILE   N   H    sing N N 209 
ILE   N   H2   sing N N 210 
ILE   CA  C    sing N N 211 
ILE   CA  CB   sing N N 212 
ILE   CA  HA   sing N N 213 
ILE   C   O    doub N N 214 
ILE   C   OXT  sing N N 215 
ILE   CB  CG1  sing N N 216 
ILE   CB  CG2  sing N N 217 
ILE   CB  HB   sing N N 218 
ILE   CG1 CD1  sing N N 219 
ILE   CG1 HG12 sing N N 220 
ILE   CG1 HG13 sing N N 221 
ILE   CG2 HG21 sing N N 222 
ILE   CG2 HG22 sing N N 223 
ILE   CG2 HG23 sing N N 224 
ILE   CD1 HD11 sing N N 225 
ILE   CD1 HD12 sing N N 226 
ILE   CD1 HD13 sing N N 227 
ILE   OXT HXT  sing N N 228 
LEU   N   CA   sing N N 229 
LEU   N   H    sing N N 230 
LEU   N   H2   sing N N 231 
LEU   CA  C    sing N N 232 
LEU   CA  CB   sing N N 233 
LEU   CA  HA   sing N N 234 
LEU   C   O    doub N N 235 
LEU   C   OXT  sing N N 236 
LEU   CB  CG   sing N N 237 
LEU   CB  HB2  sing N N 238 
LEU   CB  HB3  sing N N 239 
LEU   CG  CD1  sing N N 240 
LEU   CG  CD2  sing N N 241 
LEU   CG  HG   sing N N 242 
LEU   CD1 HD11 sing N N 243 
LEU   CD1 HD12 sing N N 244 
LEU   CD1 HD13 sing N N 245 
LEU   CD2 HD21 sing N N 246 
LEU   CD2 HD22 sing N N 247 
LEU   CD2 HD23 sing N N 248 
LEU   OXT HXT  sing N N 249 
LYS   N   CA   sing N N 250 
LYS   N   H    sing N N 251 
LYS   N   H2   sing N N 252 
LYS   CA  C    sing N N 253 
LYS   CA  CB   sing N N 254 
LYS   CA  HA   sing N N 255 
LYS   C   O    doub N N 256 
LYS   C   OXT  sing N N 257 
LYS   CB  CG   sing N N 258 
LYS   CB  HB2  sing N N 259 
LYS   CB  HB3  sing N N 260 
LYS   CG  CD   sing N N 261 
LYS   CG  HG2  sing N N 262 
LYS   CG  HG3  sing N N 263 
LYS   CD  CE   sing N N 264 
LYS   CD  HD2  sing N N 265 
LYS   CD  HD3  sing N N 266 
LYS   CE  NZ   sing N N 267 
LYS   CE  HE2  sing N N 268 
LYS   CE  HE3  sing N N 269 
LYS   NZ  HZ1  sing N N 270 
LYS   NZ  HZ2  sing N N 271 
LYS   NZ  HZ3  sing N N 272 
LYS   OXT HXT  sing N N 273 
MES   O1  C2   sing N N 274 
MES   O1  C6   sing N N 275 
MES   C2  C3   sing N N 276 
MES   C2  H21  sing N N 277 
MES   C2  H22  sing N N 278 
MES   C3  N4   sing N N 279 
MES   C3  H31  sing N N 280 
MES   C3  H32  sing N N 281 
MES   N4  C5   sing N N 282 
MES   N4  C7   sing N N 283 
MES   N4  HN4  sing N N 284 
MES   C5  C6   sing N N 285 
MES   C5  H51  sing N N 286 
MES   C5  H52  sing N N 287 
MES   C6  H61  sing N N 288 
MES   C6  H62  sing N N 289 
MES   C7  C8   sing N N 290 
MES   C7  H71  sing N N 291 
MES   C7  H72  sing N N 292 
MES   C8  S    sing N N 293 
MES   C8  H81  sing N N 294 
MES   C8  H82  sing N N 295 
MES   S   O1S  doub N N 296 
MES   S   O2S  doub N N 297 
MES   S   O3S  sing N N 298 
MET   N   CA   sing N N 299 
MET   N   H    sing N N 300 
MET   N   H2   sing N N 301 
MET   CA  C    sing N N 302 
MET   CA  CB   sing N N 303 
MET   CA  HA   sing N N 304 
MET   C   O    doub N N 305 
MET   C   OXT  sing N N 306 
MET   CB  CG   sing N N 307 
MET   CB  HB2  sing N N 308 
MET   CB  HB3  sing N N 309 
MET   CG  SD   sing N N 310 
MET   CG  HG2  sing N N 311 
MET   CG  HG3  sing N N 312 
MET   SD  CE   sing N N 313 
MET   CE  HE1  sing N N 314 
MET   CE  HE2  sing N N 315 
MET   CE  HE3  sing N N 316 
MET   OXT HXT  sing N N 317 
PHE   N   CA   sing N N 318 
PHE   N   H    sing N N 319 
PHE   N   H2   sing N N 320 
PHE   CA  C    sing N N 321 
PHE   CA  CB   sing N N 322 
PHE   CA  HA   sing N N 323 
PHE   C   O    doub N N 324 
PHE   C   OXT  sing N N 325 
PHE   CB  CG   sing N N 326 
PHE   CB  HB2  sing N N 327 
PHE   CB  HB3  sing N N 328 
PHE   CG  CD1  doub Y N 329 
PHE   CG  CD2  sing Y N 330 
PHE   CD1 CE1  sing Y N 331 
PHE   CD1 HD1  sing N N 332 
PHE   CD2 CE2  doub Y N 333 
PHE   CD2 HD2  sing N N 334 
PHE   CE1 CZ   doub Y N 335 
PHE   CE1 HE1  sing N N 336 
PHE   CE2 CZ   sing Y N 337 
PHE   CE2 HE2  sing N N 338 
PHE   CZ  HZ   sing N N 339 
PHE   OXT HXT  sing N N 340 
PRO   N   CA   sing N N 341 
PRO   N   CD   sing N N 342 
PRO   N   H    sing N N 343 
PRO   CA  C    sing N N 344 
PRO   CA  CB   sing N N 345 
PRO   CA  HA   sing N N 346 
PRO   C   O    doub N N 347 
PRO   C   OXT  sing N N 348 
PRO   CB  CG   sing N N 349 
PRO   CB  HB2  sing N N 350 
PRO   CB  HB3  sing N N 351 
PRO   CG  CD   sing N N 352 
PRO   CG  HG2  sing N N 353 
PRO   CG  HG3  sing N N 354 
PRO   CD  HD2  sing N N 355 
PRO   CD  HD3  sing N N 356 
PRO   OXT HXT  sing N N 357 
SER   N   CA   sing N N 358 
SER   N   H    sing N N 359 
SER   N   H2   sing N N 360 
SER   CA  C    sing N N 361 
SER   CA  CB   sing N N 362 
SER   CA  HA   sing N N 363 
SER   C   O    doub N N 364 
SER   C   OXT  sing N N 365 
SER   CB  OG   sing N N 366 
SER   CB  HB2  sing N N 367 
SER   CB  HB3  sing N N 368 
SER   OG  HG   sing N N 369 
SER   OXT HXT  sing N N 370 
THR   N   CA   sing N N 371 
THR   N   H    sing N N 372 
THR   N   H2   sing N N 373 
THR   CA  C    sing N N 374 
THR   CA  CB   sing N N 375 
THR   CA  HA   sing N N 376 
THR   C   O    doub N N 377 
THR   C   OXT  sing N N 378 
THR   CB  OG1  sing N N 379 
THR   CB  CG2  sing N N 380 
THR   CB  HB   sing N N 381 
THR   OG1 HG1  sing N N 382 
THR   CG2 HG21 sing N N 383 
THR   CG2 HG22 sing N N 384 
THR   CG2 HG23 sing N N 385 
THR   OXT HXT  sing N N 386 
TRP   N   CA   sing N N 387 
TRP   N   H    sing N N 388 
TRP   N   H2   sing N N 389 
TRP   CA  C    sing N N 390 
TRP   CA  CB   sing N N 391 
TRP   CA  HA   sing N N 392 
TRP   C   O    doub N N 393 
TRP   C   OXT  sing N N 394 
TRP   CB  CG   sing N N 395 
TRP   CB  HB2  sing N N 396 
TRP   CB  HB3  sing N N 397 
TRP   CG  CD1  doub Y N 398 
TRP   CG  CD2  sing Y N 399 
TRP   CD1 NE1  sing Y N 400 
TRP   CD1 HD1  sing N N 401 
TRP   CD2 CE2  doub Y N 402 
TRP   CD2 CE3  sing Y N 403 
TRP   NE1 CE2  sing Y N 404 
TRP   NE1 HE1  sing N N 405 
TRP   CE2 CZ2  sing Y N 406 
TRP   CE3 CZ3  doub Y N 407 
TRP   CE3 HE3  sing N N 408 
TRP   CZ2 CH2  doub Y N 409 
TRP   CZ2 HZ2  sing N N 410 
TRP   CZ3 CH2  sing Y N 411 
TRP   CZ3 HZ3  sing N N 412 
TRP   CH2 HH2  sing N N 413 
TRP   OXT HXT  sing N N 414 
TYR   N   CA   sing N N 415 
TYR   N   H    sing N N 416 
TYR   N   H2   sing N N 417 
TYR   CA  C    sing N N 418 
TYR   CA  CB   sing N N 419 
TYR   CA  HA   sing N N 420 
TYR   C   O    doub N N 421 
TYR   C   OXT  sing N N 422 
TYR   CB  CG   sing N N 423 
TYR   CB  HB2  sing N N 424 
TYR   CB  HB3  sing N N 425 
TYR   CG  CD1  doub Y N 426 
TYR   CG  CD2  sing Y N 427 
TYR   CD1 CE1  sing Y N 428 
TYR   CD1 HD1  sing N N 429 
TYR   CD2 CE2  doub Y N 430 
TYR   CD2 HD2  sing N N 431 
TYR   CE1 CZ   doub Y N 432 
TYR   CE1 HE1  sing N N 433 
TYR   CE2 CZ   sing Y N 434 
TYR   CE2 HE2  sing N N 435 
TYR   CZ  OH   sing N N 436 
TYR   OH  HH   sing N N 437 
TYR   OXT HXT  sing N N 438 
VAL   N   CA   sing N N 439 
VAL   N   H    sing N N 440 
VAL   N   H2   sing N N 441 
VAL   CA  C    sing N N 442 
VAL   CA  CB   sing N N 443 
VAL   CA  HA   sing N N 444 
VAL   C   O    doub N N 445 
VAL   C   OXT  sing N N 446 
VAL   CB  CG1  sing N N 447 
VAL   CB  CG2  sing N N 448 
VAL   CB  HB   sing N N 449 
VAL   CG1 HG11 sing N N 450 
VAL   CG1 HG12 sing N N 451 
VAL   CG1 HG13 sing N N 452 
VAL   CG2 HG21 sing N N 453 
VAL   CG2 HG22 sing N N 454 
VAL   CG2 HG23 sing N N 455 
VAL   OXT HXT  sing N N 456 
# 
_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                    9F8L 
_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]   0.012049 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000766 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014416 
_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]   0.014484 
_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    . THR   A 1 30  ? 36.551 33.381  -5.888  1.00 67.61  ? 10  THR   A N    1 
ATOM   2    C CA   . THR   A 1 30  ? 35.729 33.347  -7.091  1.00 64.17  ? 10  THR   A CA   1 
ATOM   3    C C    . THR   A 1 30  ? 34.390 32.658  -6.810  1.00 66.50  ? 10  THR   A C    1 
ATOM   4    O O    . THR   A 1 30  ? 34.235 31.960  -5.803  1.00 65.87  ? 10  THR   A O    1 
ATOM   5    C CB   . THR   A 1 30  ? 36.442 32.597  -8.244  1.00 55.44  ? 10  THR   A CB   1 
ATOM   6    O OG1  . THR   A 1 30  ? 36.704 31.243  -7.852  1.00 66.05  ? 10  THR   A OG1  1 
ATOM   7    C CG2  . THR   A 1 30  ? 37.761 33.287  -8.618  1.00 54.40  ? 10  THR   A CG2  1 
ATOM   8    H HA   . THR   A 1 30  ? 35.553 34.255  -7.383  1.00 77.00  ? 10  THR   A HA   1 
ATOM   9    H HB   . THR   A 1 30  ? 35.870 32.602  -9.027  1.00 66.53  ? 10  THR   A HB   1 
ATOM   10   H HG1  . THR   A 1 30  ? 37.204 31.231  -7.178  1.00 79.26  ? 10  THR   A HG1  1 
ATOM   11   H HG21 . THR   A 1 30  ? 38.193 32.807  -9.342  1.00 65.28  ? 10  THR   A HG21 1 
ATOM   12   H HG22 . THR   A 1 30  ? 37.590 34.198  -8.903  1.00 65.28  ? 10  THR   A HG22 1 
ATOM   13   H HG23 . THR   A 1 30  ? 38.356 33.303  -7.852  1.00 65.28  ? 10  THR   A HG23 1 
ATOM   14   N N    . SER   A 1 31  ? 33.421 32.861  -7.709  1.00 67.38  ? 11  SER   A N    1 
ATOM   15   C CA   . SER   A 1 31  ? 32.135 32.181  -7.571  1.00 66.43  ? 11  SER   A CA   1 
ATOM   16   C C    . SER   A 1 31  ? 32.299 30.670  -7.660  1.00 61.22  ? 11  SER   A C    1 
ATOM   17   O O    . SER   A 1 31  ? 31.565 29.919  -7.000  1.00 58.74  ? 11  SER   A O    1 
ATOM   18   C CB   . SER   A 1 31  ? 31.159 32.677  -8.643  1.00 69.29  ? 11  SER   A CB   1 
ATOM   19   H H    . SER   A 1 31  ? 33.483 33.377  -8.394  1.00 80.86  ? 11  SER   A H    1 
ATOM   20   H HA   . SER   A 1 31  ? 31.756 32.395  -6.704  1.00 79.72  ? 11  SER   A HA   1 
ATOM   21   N N    . GLU   A 1 32  ? 33.253 30.202  -8.463  1.00 58.16  ? 12  GLU   A N    1 
ATOM   22   C CA   . GLU   A 1 32  ? 33.497 28.765  -8.546  1.00 55.28  ? 12  GLU   A CA   1 
ATOM   23   C C    . GLU   A 1 32  ? 33.985 28.217  -7.208  1.00 52.96  ? 12  GLU   A C    1 
ATOM   24   O O    . GLU   A 1 32  ? 33.520 27.164  -6.743  1.00 50.68  ? 12  GLU   A O    1 
ATOM   25   C CB   . GLU   A 1 32  ? 34.518 28.473  -9.648  1.00 56.38  ? 12  GLU   A CB   1 
ATOM   26   H H    . GLU   A 1 32  ? 33.763 30.685  -8.960  1.00 69.79  ? 12  GLU   A H    1 
ATOM   27   H HA   . GLU   A 1 32  ? 32.667 28.317  -8.773  1.00 66.34  ? 12  GLU   A HA   1 
ATOM   28   N N    . ASN   A 1 33  ? 34.937 28.911  -6.577  1.00 53.66  ? 13  ASN   A N    1 
ATOM   29   C CA   . ASN   A 1 33  ? 35.468 28.439  -5.301  1.00 54.67  ? 13  ASN   A CA   1 
ATOM   30   C C    . ASN   A 1 33  ? 34.387 28.416  -4.232  1.00 49.22  ? 13  ASN   A C    1 
ATOM   31   O O    . ASN   A 1 33  ? 34.343 27.497  -3.406  1.00 45.85  ? 13  ASN   A O    1 
ATOM   32   C CB   . ASN   A 1 33  ? 36.637 29.312  -4.861  1.00 60.72  ? 13  ASN   A CB   1 
ATOM   33   C CG   . ASN   A 1 33  ? 37.895 29.027  -5.647  1.00 66.62  ? 13  ASN   A CG   1 
ATOM   34   O OD1  . ASN   A 1 33  ? 37.884 28.221  -6.580  1.00 68.57  ? 13  ASN   A OD1  1 
ATOM   35   N ND2  . ASN   A 1 33  ? 38.990 29.689  -5.283  1.00 68.84  ? 13  ASN   A ND2  1 
ATOM   36   H H    . ASN   A 1 33  ? 35.285 29.644  -6.863  1.00 64.40  ? 13  ASN   A H    1 
ATOM   37   H HA   . ASN   A 1 33  ? 35.799 27.534  -5.418  1.00 65.61  ? 13  ASN   A HA   1 
ATOM   38   H HB2  . ASN   A 1 33  ? 36.405 30.245  -4.992  1.00 72.86  ? 13  ASN   A HB2  1 
ATOM   39   H HB3  . ASN   A 1 33  ? 36.823 29.145  -3.923  1.00 72.86  ? 13  ASN   A HB3  1 
ATOM   40   H HD21 . ASN   A 1 33  ? 39.730 29.560  -5.702  1.00 82.61  ? 13  ASN   A HD21 1 
ATOM   41   H HD22 . ASN   A 1 33  ? 38.958 30.247  -4.630  1.00 82.61  ? 13  ASN   A HD22 1 
ATOM   42   N N    . ARG   A 1 34  ? 33.506 29.423  -4.227  1.00 46.82  ? 14  ARG   A N    1 
ATOM   43   C CA   . ARG   A 1 34  ? 32.391 29.425  -3.283  1.00 44.67  ? 14  ARG   A CA   1 
ATOM   44   C C    . ARG   A 1 34  ? 31.510 28.204  -3.482  1.00 40.32  ? 14  ARG   A C    1 
ATOM   45   O O    . ARG   A 1 34  ? 31.102 27.560  -2.510  1.00 38.79  ? 14  ARG   A O    1 
ATOM   46   C CB   . ARG   A 1 34  ? 31.556 30.698  -3.452  1.00 48.67  ? 14  ARG   A CB   1 
ATOM   47   C CG   . ARG   A 1 34  ? 32.351 31.983  -3.428  1.00 54.95  ? 14  ARG   A CG   1 
ATOM   48   C CD   . ARG   A 1 34  ? 31.946 32.887  -2.257  1.00 61.19  ? 14  ARG   A CD   1 
ATOM   49   N NE   . ARG   A 1 34  ? 30.556 33.325  -2.320  1.00 66.12  ? 14  ARG   A NE   1 
ATOM   50   C CZ   . ARG   A 1 34  ? 29.838 33.692  -1.265  1.00 69.14  ? 14  ARG   A CZ   1 
ATOM   51   N NH1  . ARG   A 1 34  ? 30.329 33.628  -0.035  1.00 68.28  ? 14  ARG   A NH1  1 
ATOM   52   N NH2  . ARG   A 1 34  ? 28.595 34.130  -1.446  1.00 71.06  ? 14  ARG   A NH2  1 
ATOM   53   H H    . ARG   A 1 34  ? 33.533 30.103  -4.752  1.00 56.18  ? 14  ARG   A H    1 
ATOM   54   H HA   . ARG   A 1 34  ? 32.749 29.411  -2.381  1.00 53.61  ? 14  ARG   A HA   1 
ATOM   55   H HB2  . ARG   A 1 34  ? 31.098 30.654  -4.305  1.00 58.41  ? 14  ARG   A HB2  1 
ATOM   56   H HB3  . ARG   A 1 34  ? 30.910 30.740  -2.729  1.00 58.41  ? 14  ARG   A HB3  1 
ATOM   57   H HG2  . ARG   A 1 34  ? 33.293 31.774  -3.337  1.00 65.95  ? 14  ARG   A HG2  1 
ATOM   58   H HG3  . ARG   A 1 34  ? 32.196 32.469  -4.253  1.00 65.95  ? 14  ARG   A HG3  1 
ATOM   59   H HD2  . ARG   A 1 34  ? 32.067 32.400  -1.427  1.00 73.43  ? 14  ARG   A HD2  1 
ATOM   60   H HD3  . ARG   A 1 34  ? 32.508 33.678  -2.263  1.00 73.43  ? 14  ARG   A HD3  1 
ATOM   61   H HE   . ARG   A 1 34  ? 30.176 33.348  -3.092  1.00 79.35  ? 14  ARG   A HE   1 
ATOM   62   H HH11 . ARG   A 1 34  ? 31.130 33.345  0.094   1.00 81.94  ? 14  ARG   A HH11 1 
ATOM   63   H HH12 . ARG   A 1 34  ? 29.846 33.871  0.634   1.00 81.94  ? 14  ARG   A HH12 1 
ATOM   64   H HH21 . ARG   A 1 34  ? 28.265 34.174  -2.239  1.00 85.27  ? 14  ARG   A HH21 1 
ATOM   65   H HH22 . ARG   A 1 34  ? 28.121 34.370  -0.769  1.00 85.27  ? 14  ARG   A HH22 1 
ATOM   66   N N    . ALA   A 1 35  ? 31.197 27.881  -4.741  1.00 38.16  ? 15  ALA   A N    1 
ATOM   67   C CA   . ALA   A 1 35  ? 30.347 26.736  -5.033  1.00 37.67  ? 15  ALA   A CA   1 
ATOM   68   C C    . ALA   A 1 35  ? 31.032 25.433  -4.644  1.00 35.25  ? 15  ALA   A C    1 
ATOM   69   O O    . ALA   A 1 35  ? 30.390 24.523  -4.104  1.00 33.94  ? 15  ALA   A O    1 
ATOM   70   C CB   . ALA   A 1 35  ? 29.964 26.737  -6.513  1.00 38.75  ? 15  ALA   A CB   1 
ATOM   71   H H    . ALA   A 1 35  ? 31.464 28.309  -5.438  1.00 45.79  ? 15  ALA   A H    1 
ATOM   72   H HA   . ALA   A 1 35  ? 29.529 26.804  -4.517  1.00 45.20  ? 15  ALA   A HA   1 
ATOM   73   H HB1  . ALA   A 1 35  ? 29.391 25.976  -6.692  1.00 46.51  ? 15  ALA   A HB1  1 
ATOM   74   H HB2  . ALA   A 1 35  ? 29.494 27.561  -6.717  1.00 46.51  ? 15  ALA   A HB2  1 
ATOM   75   H HB3  . ALA   A 1 35  ? 30.771 26.677  -7.048  1.00 46.51  ? 15  ALA   A HB3  1 
ATOM   76   N N    . GLN   A 1 36  ? 32.337 25.332  -4.882  1.00 35.10  ? 16  GLN   A N    1 
ATOM   77   C CA   . GLN   A 1 36  ? 33.056 24.121  -4.503  1.00 34.20  ? 16  GLN   A CA   1 
ATOM   78   C C    . GLN   A 1 36  ? 33.156 23.990  -2.993  1.00 32.87  ? 16  GLN   A C    1 
ATOM   79   O O    . GLN   A 1 36  ? 32.959 22.895  -2.445  1.00 31.46  ? 16  GLN   A O    1 
ATOM   80   C CB   . GLN   A 1 36  ? 34.445 24.132  -5.145  1.00 29.63  ? 16  GLN   A CB   1 
ATOM   81   C CG   . GLN   A 1 36  ? 34.330 24.015  -6.643  1.00 30.28  ? 16  GLN   A CG   1 
ATOM   82   C CD   . GLN   A 1 36  ? 35.648 23.867  -7.312  1.00 30.91  ? 16  GLN   A CD   1 
ATOM   83   O OE1  . GLN   A 1 36  ? 36.406 22.947  -7.001  1.00 33.26  ? 16  GLN   A OE1  1 
ATOM   84   N NE2  . GLN   A 1 36  ? 35.950 24.781  -8.236  1.00 32.75  ? 16  GLN   A NE2  1 
ATOM   85   H H    . GLN   A 1 36  ? 32.821 25.938  -5.254  1.00 42.12  ? 16  GLN   A H    1 
ATOM   86   H HA   . GLN   A 1 36  ? 32.576 23.346  -4.833  1.00 41.05  ? 16  GLN   A HA   1 
ATOM   87   H HB2  . GLN   A 1 36  ? 34.895 24.964  -4.931  1.00 35.56  ? 16  GLN   A HB2  1 
ATOM   88   H HB3  . GLN   A 1 36  ? 34.961 23.380  -4.813  1.00 35.56  ? 16  GLN   A HB3  1 
ATOM   89   H HG2  . GLN   A 1 36  ? 33.795 23.235  -6.859  1.00 36.34  ? 16  GLN   A HG2  1 
ATOM   90   H HG3  . GLN   A 1 36  ? 33.906 24.815  -6.991  1.00 36.34  ? 16  GLN   A HG3  1 
ATOM   91   H HE21 . GLN   A 1 36  ? 35.392 25.411  -8.415  1.00 39.30  ? 16  GLN   A HE21 1 
ATOM   92   H HE22 . GLN   A 1 36  ? 36.701 24.740  -8.652  1.00 39.30  ? 16  GLN   A HE22 1 
ATOM   93   N N    . VAL   A 1 37  ? 33.434 25.091  -2.296  1.00 33.46  ? 17  VAL   A N    1 
ATOM   94   C CA   . VAL   A 1 37  ? 33.516 25.042  -0.839  1.00 35.67  ? 17  VAL   A CA   1 
ATOM   95   C C    . VAL   A 1 37  ? 32.185 24.612  -0.245  1.00 33.97  ? 17  VAL   A C    1 
ATOM   96   O O    . VAL   A 1 37  ? 32.137 23.731  0.616   1.00 32.34  ? 17  VAL   A O    1 
ATOM   97   C CB   . VAL   A 1 37  ? 33.993 26.392  -0.266  1.00 39.35  ? 17  VAL   A CB   1 
ATOM   98   C CG1  . VAL   A 1 37  ? 33.900 26.376  1.264   1.00 42.24  ? 17  VAL   A CG1  1 
ATOM   99   C CG2  . VAL   A 1 37  ? 35.426 26.707  -0.701  1.00 40.66  ? 17  VAL   A CG2  1 
ATOM   100  H H    . VAL   A 1 37  ? 33.576 25.867  -2.637  1.00 40.15  ? 17  VAL   A H    1 
ATOM   101  H HA   . VAL   A 1 37  ? 34.179 24.376  -0.597  1.00 42.80  ? 17  VAL   A HA   1 
ATOM   102  H HB   . VAL   A 1 37  ? 33.417 27.091  -0.613  1.00 47.23  ? 17  VAL   A HB   1 
ATOM   103  H HG11 . VAL   A 1 37  ? 34.435 27.103  1.620   1.00 50.69  ? 17  VAL   A HG11 1 
ATOM   104  H HG12 . VAL   A 1 37  ? 32.972 26.490  1.525   1.00 50.69  ? 17  VAL   A HG12 1 
ATOM   105  H HG13 . VAL   A 1 37  ? 34.234 25.527  1.592   1.00 50.69  ? 17  VAL   A HG13 1 
ATOM   106  H HG21 . VAL   A 1 37  ? 35.586 27.658  -0.594  1.00 48.79  ? 17  VAL   A HG21 1 
ATOM   107  H HG22 . VAL   A 1 37  ? 36.042 26.204  -0.147  1.00 48.79  ? 17  VAL   A HG22 1 
ATOM   108  H HG23 . VAL   A 1 37  ? 35.536 26.456  -1.631  1.00 48.79  ? 17  VAL   A HG23 1 
ATOM   109  N N    . ALA   A 1 38  ? 31.083 25.182  -0.741  1.00 33.02  ? 18  ALA   A N    1 
ATOM   110  C CA   . ALA   A 1 38  ? 29.753 24.842  -0.235  1.00 31.45  ? 18  ALA   A CA   1 
ATOM   111  C C    . ALA   A 1 38  ? 29.441 23.368  -0.462  1.00 29.66  ? 18  ALA   A C    1 
ATOM   112  O O    . ALA   A 1 38  ? 28.919 22.694  0.428   1.00 28.52  ? 18  ALA   A O    1 
ATOM   113  C CB   . ALA   A 1 38  ? 28.696 25.729  -0.900  1.00 31.99  ? 18  ALA   A CB   1 
ATOM   114  H H    . ALA   A 1 38  ? 31.078 25.769  -1.371  1.00 39.63  ? 18  ALA   A H    1 
ATOM   115  H HA   . ALA   A 1 38  ? 29.728 25.011  0.720   1.00 37.74  ? 18  ALA   A HA   1 
ATOM   116  H HB1  . ALA   A 1 38  ? 27.822 25.499  -0.547  1.00 38.39  ? 18  ALA   A HB1  1 
ATOM   117  H HB2  . ALA   A 1 38  ? 28.896 26.659  -0.706  1.00 38.39  ? 18  ALA   A HB2  1 
ATOM   118  H HB3  . ALA   A 1 38  ? 28.715 25.580  -1.858  1.00 38.39  ? 18  ALA   A HB3  1 
ATOM   119  N N    . ALA   A 1 39  ? 29.719 22.871  -1.665  1.00 27.09  ? 19  ALA   A N    1 
ATOM   120  C CA   . ALA   A 1 39  ? 29.464 21.466  -1.959  1.00 27.84  ? 19  ALA   A CA   1 
ATOM   121  C C    . ALA   A 1 39  ? 30.245 20.563  -1.020  1.00 29.79  ? 19  ALA   A C    1 
ATOM   122  O O    . ALA   A 1 39  ? 29.697 19.608  -0.476  1.00 25.40  ? 19  ALA   A O    1 
ATOM   123  C CB   . ALA   A 1 39  ? 29.818 21.169  -3.411  1.00 28.56  ? 19  ALA   A CB   1 
ATOM   124  H H    . ALA   A 1 39  ? 30.050 23.320  -2.320  1.00 32.51  ? 19  ALA   A H    1 
ATOM   125  H HA   . ALA   A 1 39  ? 28.520 21.281  -1.836  1.00 33.41  ? 19  ALA   A HA   1 
ATOM   126  H HB1  . ALA   A 1 39  ? 29.641 20.233  -3.594  1.00 34.27  ? 19  ALA   A HB1  1 
ATOM   127  H HB2  . ALA   A 1 39  ? 29.276 21.728  -3.989  1.00 34.27  ? 19  ALA   A HB2  1 
ATOM   128  H HB3  . ALA   A 1 39  ? 30.759 21.361  -3.552  1.00 34.27  ? 19  ALA   A HB3  1 
ATOM   129  N N    . ARG   A 1 40  ? 31.522 20.865  -0.796  1.00 27.05  ? 20  ARG   A N    1 
ATOM   130  C CA   . ARG   A 1 40  ? 32.334 19.996  0.049   1.00 27.80  ? 20  ARG   A CA   1 
ATOM   131  C C    . ARG   A 1 40  ? 31.824 19.953  1.484   1.00 27.75  ? 20  ARG   A C    1 
ATOM   132  O O    . ARG   A 1 40  ? 31.751 18.880  2.100   1.00 26.12  ? 20  ARG   A O    1 
ATOM   133  C CB   . ARG   A 1 40  ? 33.791 20.475  0.004   1.00 27.36  ? 20  ARG   A CB   1 
ATOM   134  C CG   . ARG   A 1 40  ? 34.718 19.585  0.808   1.00 28.78  ? 20  ARG   A CG   1 
ATOM   135  C CD   . ARG   A 1 40  ? 36.190 20.057  0.722   1.00 29.91  ? 20  ARG   A CD   1 
ATOM   136  N NE   . ARG   A 1 40  ? 36.764 19.863  -0.601  1.00 27.08  ? 20  ARG   A NE   1 
ATOM   137  C CZ   . ARG   A 1 40  ? 37.011 20.810  -1.489  1.00 28.95  ? 20  ARG   A CZ   1 
ATOM   138  N NH1  . ARG   A 1 40  ? 36.715 22.081  -1.241  1.00 27.96  ? 20  ARG   A NH1  1 
ATOM   139  N NH2  . ARG   A 1 40  ? 37.480 20.481  -2.684  1.00 26.39  ? 20  ARG   A NH2  1 
ATOM   140  H H    . ARG   A 1 40  ? 31.932 21.551  -1.113  1.00 32.46  ? 20  ARG   A H    1 
ATOM   141  H HA   . ARG   A 1 40  ? 32.290 19.090  -0.294  1.00 33.36  ? 20  ARG   A HA   1 
ATOM   142  H HB2  . ARG   A 1 40  ? 34.096 20.476  -0.916  1.00 32.83  ? 20  ARG   A HB2  1 
ATOM   143  H HB3  . ARG   A 1 40  ? 33.841 21.372  0.371   1.00 32.83  ? 20  ARG   A HB3  1 
ATOM   144  H HG2  . ARG   A 1 40  ? 34.448 19.601  1.740   1.00 34.54  ? 20  ARG   A HG2  1 
ATOM   145  H HG3  . ARG   A 1 40  ? 34.670 18.679  0.464   1.00 34.54  ? 20  ARG   A HG3  1 
ATOM   146  H HD2  . ARG   A 1 40  ? 36.231 21.003  0.932   1.00 35.89  ? 20  ARG   A HD2  1 
ATOM   147  H HD3  . ARG   A 1 40  ? 36.722 19.553  1.358   1.00 35.89  ? 20  ARG   A HD3  1 
ATOM   148  H HE   . ARG   A 1 40  ? 36.961 19.057  -0.826  1.00 32.50  ? 20  ARG   A HE   1 
ATOM   149  H HH11 . ARG   A 1 40  ? 36.355 22.300  -0.491  1.00 33.55  ? 20  ARG   A HH11 1 
ATOM   150  H HH12 . ARG   A 1 40  ? 36.883 22.684  -1.830  1.00 33.55  ? 20  ARG   A HH12 1 
ATOM   151  H HH21 . ARG   A 1 40  ? 37.622 19.655  -2.877  1.00 31.67  ? 20  ARG   A HH21 1 
ATOM   152  H HH22 . ARG   A 1 40  ? 37.643 21.093  -3.265  1.00 31.67  ? 20  ARG   A HH22 1 
ATOM   153  N N    . GLN   A 1 41  ? 31.409 21.095  2.027   1.00 28.49  ? 21  GLN   A N    1 
ATOM   154  C CA   . GLN   A 1 41  ? 30.914 21.121  3.408   1.00 30.58  ? 21  GLN   A CA   1 
ATOM   155  C C    . GLN   A 1 41  ? 29.617 20.332  3.560   1.00 29.02  ? 21  GLN   A C    1 
ATOM   156  O O    . GLN   A 1 41  ? 29.425 19.605  4.551   1.00 30.12  ? 21  GLN   A O    1 
ATOM   157  C CB   . GLN   A 1 41  ? 30.695 22.565  3.843   1.00 34.79  ? 21  GLN   A CB   1 
ATOM   158  C CG   . GLN   A 1 41  ? 31.983 23.373  3.793   1.00 38.87  ? 21  GLN   A CG   1 
ATOM   159  C CD   . GLN   A 1 41  ? 31.789 24.859  4.038   1.00 44.76  ? 21  GLN   A CD   1 
ATOM   160  O OE1  . GLN   A 1 41  ? 30.662 25.356  4.074   1.00 47.86  ? 21  GLN   A OE1  1 
ATOM   161  N NE2  . GLN   A 1 41  ? 32.901 25.582  4.206   1.00 47.52  ? 21  GLN   A NE2  1 
ATOM   162  H H    . GLN   A 1 41  ? 31.403 21.857  1.628   1.00 34.19  ? 21  GLN   A H    1 
ATOM   163  H HA   . GLN   A 1 41  ? 31.580 20.713  3.983   1.00 36.70  ? 21  GLN   A HA   1 
ATOM   164  H HB2  . GLN   A 1 41  ? 30.051 22.982  3.250   1.00 41.76  ? 21  GLN   A HB2  1 
ATOM   165  H HB3  . GLN   A 1 41  ? 30.364 22.577  4.754   1.00 41.76  ? 21  GLN   A HB3  1 
ATOM   166  H HG2  . GLN   A 1 41  ? 32.587 23.039  4.475   1.00 46.65  ? 21  GLN   A HG2  1 
ATOM   167  H HG3  . GLN   A 1 41  ? 32.383 23.269  2.916   1.00 46.65  ? 21  GLN   A HG3  1 
ATOM   168  H HE21 . GLN   A 1 41  ? 33.671 25.201  4.173   1.00 57.02  ? 21  GLN   A HE21 1 
ATOM   169  H HE22 . GLN   A 1 41  ? 32.846 26.429  4.347   1.00 57.02  ? 21  GLN   A HE22 1 
ATOM   170  N N    . HIS   A 1 42  ? 28.695 20.478  2.612   1.00 26.47  ? 22  HIS   A N    1 
ATOM   171  C CA   . HIS   A 1 42  ? 27.473 19.691  2.680   1.00 25.38  ? 22  HIS   A CA   1 
ATOM   172  C C    . HIS   A 1 42  ? 27.761 18.208  2.516   1.00 24.91  ? 22  HIS   A C    1 
ATOM   173  O O    . HIS   A 1 42  ? 27.222 17.374  3.252   1.00 25.09  ? 22  HIS   A O    1 
ATOM   174  C CB   . HIS   A 1 42  ? 26.528 20.125  1.587   1.00 25.74  ? 22  HIS   A CB   1 
ATOM   175  C CG   . HIS   A 1 42  ? 25.403 19.188  1.397   1.00 25.68  ? 22  HIS   A CG   1 
ATOM   176  N ND1  . HIS   A 1 42  ? 24.267 19.206  2.179   1.00 26.95  ? 22  HIS   A ND1  1 
ATOM   177  C CD2  . HIS   A 1 42  ? 25.266 18.158  0.537   1.00 23.76  ? 22  HIS   A CD2  1 
ATOM   178  C CE1  . HIS   A 1 42  ? 23.457 18.240  1.776   1.00 25.48  ? 22  HIS   A CE1  1 
ATOM   179  N NE2  . HIS   A 1 42  ? 24.040 17.595  0.777   1.00 23.54  ? 22  HIS   A NE2  1 
ATOM   180  H H    . HIS   A 1 42  ? 28.753 21.011  1.940   1.00 31.76  ? 22  HIS   A H    1 
ATOM   181  H HA   . HIS   A 1 42  ? 27.062 19.840  3.546   1.00 30.46  ? 22  HIS   A HA   1 
ATOM   182  H HB2  . HIS   A 1 42  ? 26.161 20.994  1.815   1.00 30.89  ? 22  HIS   A HB2  1 
ATOM   183  H HB3  . HIS   A 1 42  ? 27.017 20.181  0.751   1.00 30.89  ? 22  HIS   A HB3  1 
ATOM   184  H HD2  . HIS   A 1 42  ? 25.886 17.882  -0.100  1.00 28.51  ? 22  HIS   A HD2  1 
ATOM   185  H HE1  . HIS   A 1 42  ? 22.620 18.048  2.133   1.00 30.58  ? 22  HIS   A HE1  1 
ATOM   186  H HE2  . HIS   A 1 42  ? 23.704 16.930  0.349   1.00 28.25  ? 22  HIS   A HE2  1 
ATOM   187  N N    . ASN   A 1 43  ? 28.603 17.863  1.539   1.00 23.00  ? 23  ASN   A N    1 
ATOM   188  C CA   . ASN   A 1 43  ? 28.876 16.458  1.262   1.00 21.64  ? 23  ASN   A CA   1 
ATOM   189  C C    . ASN   A 1 43  ? 29.550 15.786  2.451   1.00 21.74  ? 23  ASN   A C    1 
ATOM   190  O O    . ASN   A 1 43  ? 29.260 14.619  2.763   1.00 21.54  ? 23  ASN   A O    1 
ATOM   191  C CB   . ASN   A 1 43  ? 29.738 16.329  0.008   1.00 22.47  ? 23  ASN   A CB   1 
ATOM   192  C CG   . ASN   A 1 43  ? 29.022 16.774  -1.261  1.00 22.81  ? 23  ASN   A CG   1 
ATOM   193  O OD1  . ASN   A 1 43  ? 27.799 16.891  -1.313  1.00 22.51  ? 23  ASN   A OD1  1 
ATOM   194  N ND2  . ASN   A 1 43  ? 29.799 17.006  -2.315  1.00 25.37  ? 23  ASN   A ND2  1 
ATOM   195  H H    . ASN   A 1 43  ? 29.022 18.416  1.031   1.00 27.61  ? 23  ASN   A H    1 
ATOM   196  H HA   . ASN   A 1 43  ? 28.037 16.002  1.094   1.00 25.97  ? 23  ASN   A HA   1 
ATOM   197  H HB2  . ASN   A 1 43  ? 30.530 16.880  0.112   1.00 26.96  ? 23  ASN   A HB2  1 
ATOM   198  H HB3  . ASN   A 1 43  ? 29.993 15.400  -0.104  1.00 26.96  ? 23  ASN   A HB3  1 
ATOM   199  H HD21 . ASN   A 1 43  ? 29.450 17.259  -3.059  1.00 30.45  ? 23  ASN   A HD21 1 
ATOM   200  H HD22 . ASN   A 1 43  ? 30.651 16.902  -2.253  1.00 30.45  ? 23  ASN   A HD22 1 
ATOM   201  N N    . ARG   A 1 44  ? 30.440 16.504  3.143   1.00 22.92  ? 24  ARG   A N    1 
ATOM   202  C CA   . ARG   A 1 44  ? 31.058 15.930  4.332   1.00 24.05  ? 24  ARG   A CA   1 
ATOM   203  C C    . ARG   A 1 44  ? 30.023 15.538  5.378   1.00 24.10  ? 24  ARG   A C    1 
ATOM   204  O O    . ARG   A 1 44  ? 30.154 14.480  6.015   1.00 23.87  ? 24  ARG   A O    1 
ATOM   205  C CB   . ARG   A 1 44  ? 32.087 16.903  4.921   1.00 26.18  ? 24  ARG   A CB   1 
ATOM   206  C CG   . ARG   A 1 44  ? 32.870 16.255  6.015   1.00 32.65  ? 24  ARG   A CG   1 
ATOM   207  C CD   . ARG   A 1 44  ? 33.739 17.229  6.748   1.00 38.47  ? 24  ARG   A CD   1 
ATOM   208  N NE   . ARG   A 1 44  ? 34.304 16.530  7.891   1.00 45.10  ? 24  ARG   A NE   1 
ATOM   209  C CZ   . ARG   A 1 44  ? 35.532 16.049  7.948   1.00 47.96  ? 24  ARG   A CZ   1 
ATOM   210  N NH1  . ARG   A 1 44  ? 36.391 16.225  6.956   1.00 50.33  ? 24  ARG   A NH1  1 
ATOM   211  N NH2  . ARG   A 1 44  ? 35.908 15.379  9.031   1.00 48.81  ? 24  ARG   A NH2  1 
ATOM   212  H H    . ARG   A 1 44  ? 30.694 17.302  2.948   1.00 27.51  ? 24  ARG   A H    1 
ATOM   213  H HA   . ARG   A 1 44  ? 31.527 15.123  4.069   1.00 28.86  ? 24  ARG   A HA   1 
ATOM   214  H HB2  . ARG   A 1 44  ? 32.702 17.182  4.225   1.00 31.42  ? 24  ARG   A HB2  1 
ATOM   215  H HB3  . ARG   A 1 44  ? 31.628 17.675  5.287   1.00 31.42  ? 24  ARG   A HB3  1 
ATOM   216  H HG2  . ARG   A 1 44  ? 32.257 15.858  6.653   1.00 39.18  ? 24  ARG   A HG2  1 
ATOM   217  H HG3  . ARG   A 1 44  ? 33.442 15.570  5.634   1.00 39.18  ? 24  ARG   A HG3  1 
ATOM   218  H HD2  . ARG   A 1 44  ? 34.456 17.540  6.174   1.00 46.16  ? 24  ARG   A HD2  1 
ATOM   219  H HD3  . ARG   A 1 44  ? 33.212 17.982  7.059   1.00 46.16  ? 24  ARG   A HD3  1 
ATOM   220  H HE   . ARG   A 1 44  ? 33.802 16.422  8.581   1.00 54.12  ? 24  ARG   A HE   1 
ATOM   221  H HH11 . ARG   A 1 44  ? 36.153 16.661  6.253   1.00 60.40  ? 24  ARG   A HH11 1 
ATOM   222  H HH12 . ARG   A 1 44  ? 37.186 15.903  7.013   1.00 60.40  ? 24  ARG   A HH12 1 
ATOM   223  H HH21 . ARG   A 1 44  ? 35.355 15.265  9.680   1.00 58.57  ? 24  ARG   A HH21 1 
ATOM   224  H HH22 . ARG   A 1 44  ? 36.705 15.059  9.084   1.00 58.57  ? 24  ARG   A HH22 1 
ATOM   225  N N    . LYS   A 1 45  ? 28.976 16.362  5.568   1.00 24.60  ? 25  LYS   A N    1 
ATOM   226  C CA   . LYS   A 1 45  ? 27.929 16.009  6.524   1.00 25.43  ? 25  LYS   A CA   1 
ATOM   227  C C    . LYS   A 1 45  ? 27.203 14.729  6.119   1.00 23.96  ? 25  LYS   A C    1 
ATOM   228  O O    . LYS   A 1 45  ? 26.874 13.909  6.977   1.00 23.26  ? 25  LYS   A O    1 
ATOM   229  C CB   . LYS   A 1 45  ? 26.925 17.162  6.674   1.00 28.40  ? 25  LYS   A CB   1 
ATOM   230  C CG   . LYS   A 1 45  ? 27.499 18.357  7.411   1.00 35.40  ? 25  LYS   A CG   1 
ATOM   231  C CD   . LYS   A 1 45  ? 26.411 19.391  7.783   1.00 43.18  ? 25  LYS   A CD   1 
ATOM   232  C CE   . LYS   A 1 45  ? 25.377 18.812  8.765   1.00 49.83  ? 25  LYS   A CE   1 
ATOM   233  N NZ   . LYS   A 1 45  ? 24.556 19.859  9.452   1.00 53.37  ? 25  LYS   A NZ   1 
ATOM   234  H H    . LYS   A 1 45  ? 28.857 17.111  5.164   1.00 29.52  ? 25  LYS   A H    1 
ATOM   235  H HA   . LYS   A 1 45  ? 28.349 15.859  7.386   1.00 30.51  ? 25  LYS   A HA   1 
ATOM   236  H HB2  . LYS   A 1 45  ? 26.651 17.457  5.792   1.00 34.08  ? 25  LYS   A HB2  1 
ATOM   237  H HB3  . LYS   A 1 45  ? 26.155 16.846  7.172   1.00 34.08  ? 25  LYS   A HB3  1 
ATOM   238  H HG2  . LYS   A 1 45  ? 27.921 18.054  8.230   1.00 42.48  ? 25  LYS   A HG2  1 
ATOM   239  H HG3  . LYS   A 1 45  ? 28.153 18.796  6.844   1.00 42.48  ? 25  LYS   A HG3  1 
ATOM   240  H HD2  . LYS   A 1 45  ? 26.830 20.159  8.203   1.00 51.82  ? 25  LYS   A HD2  1 
ATOM   241  H HD3  . LYS   A 1 45  ? 25.944 19.667  6.979   1.00 51.82  ? 25  LYS   A HD3  1 
ATOM   242  H HE2  . LYS   A 1 45  ? 24.771 18.233  8.276   1.00 59.80  ? 25  LYS   A HE2  1 
ATOM   243  H HE3  . LYS   A 1 45  ? 25.842 18.305  9.448   1.00 59.80  ? 25  LYS   A HE3  1 
ATOM   244  H HZ1  . LYS   A 1 45  ? 23.969 19.474  10.000  1.00 64.05  ? 25  LYS   A HZ1  1 
ATOM   245  H HZ2  . LYS   A 1 45  ? 25.083 20.397  9.926   1.00 64.05  ? 25  LYS   A HZ2  1 
ATOM   246  H HZ3  . LYS   A 1 45  ? 24.114 20.344  8.850   1.00 64.05  ? 25  LYS   A HZ3  1 
ATOM   247  N N    . ILE   A 1 46  ? 26.955 14.538  4.816   1.00 21.65  ? 26  ILE   A N    1 
ATOM   248  C CA   . ILE   A 1 46  ? 26.343 13.296  4.337   1.00 20.03  ? 26  ILE   A CA   1 
ATOM   249  C C    . ILE   A 1 46  ? 27.248 12.092  4.625   1.00 20.33  ? 26  ILE   A C    1 
ATOM   250  O O    . ILE   A 1 46  ? 26.768 11.035  5.047   1.00 19.98  ? 26  ILE   A O    1 
ATOM   251  C CB   . ILE   A 1 46  ? 25.986 13.398  2.843   1.00 20.30  ? 26  ILE   A CB   1 
ATOM   252  C CG1  . ILE   A 1 46  ? 25.026 14.568  2.589   1.00 23.12  ? 26  ILE   A CG1  1 
ATOM   253  C CG2  . ILE   A 1 46  ? 25.374 12.065  2.336   1.00 20.63  ? 26  ILE   A CG2  1 
ATOM   254  C CD1  . ILE   A 1 46  ? 23.691 14.422  3.207   1.00 26.85  ? 26  ILE   A CD1  1 
ATOM   255  H H    . ILE   A 1 46  ? 27.129 15.108  4.196   1.00 25.98  ? 26  ILE   A H    1 
ATOM   256  H HA   . ILE   A 1 46  ? 25.517 13.167  4.827   1.00 24.04  ? 26  ILE   A HA   1 
ATOM   257  H HB   . ILE   A 1 46  ? 26.803 13.568  2.350   1.00 24.36  ? 26  ILE   A HB   1 
ATOM   258  H HG12 . ILE   A 1 46  ? 25.425 15.377  2.946   1.00 27.75  ? 26  ILE   A HG12 1 
ATOM   259  H HG13 . ILE   A 1 46  ? 24.896 14.657  1.632   1.00 27.75  ? 26  ILE   A HG13 1 
ATOM   260  H HG21 . ILE   A 1 46  ? 25.004 12.204  1.450   1.00 24.75  ? 26  ILE   A HG21 1 
ATOM   261  H HG22 . ILE   A 1 46  ? 26.071 11.391  2.301   1.00 24.75  ? 26  ILE   A HG22 1 
ATOM   262  H HG23 . ILE   A 1 46  ? 24.675 11.785  2.947   1.00 24.75  ? 26  ILE   A HG23 1 
ATOM   263  H HD11 . ILE   A 1 46  ? 23.154 15.198  2.985   1.00 32.22  ? 26  ILE   A HD11 1 
ATOM   264  H HD12 . ILE   A 1 46  ? 23.270 13.619  2.863   1.00 32.22  ? 26  ILE   A HD12 1 
ATOM   265  H HD13 . ILE   A 1 46  ? 23.794 14.355  4.169   1.00 32.22  ? 26  ILE   A HD13 1 
ATOM   266  N N    . VAL   A 1 47  ? 28.562 12.211  4.384   1.00 19.94  ? 27  VAL   A N    1 
ATOM   267  C CA   . VAL   A 1 47  ? 29.470 11.087  4.661   1.00 19.40  ? 27  VAL   A CA   1 
ATOM   268  C C    . VAL   A 1 47  ? 29.440 10.752  6.139   1.00 19.35  ? 27  VAL   A C    1 
ATOM   269  O O    . VAL   A 1 47  ? 29.339 9.576   6.529   1.00 18.74  ? 27  VAL   A O    1 
ATOM   270  C CB   . VAL   A 1 47  ? 30.899 11.421  4.203   1.00 18.34  ? 27  VAL   A CB   1 
ATOM   271  C CG1  . VAL   A 1 47  ? 31.836 10.305  4.630   1.00 19.66  ? 27  VAL   A CG1  1 
ATOM   272  C CG2  . VAL   A 1 47  ? 30.940 11.644  2.714   1.00 19.66  ? 27  VAL   A CG2  1 
ATOM   273  H H    . VAL   A 1 47  ? 28.944 12.914  4.068   1.00 23.93  ? 27  VAL   A H    1 
ATOM   274  H HA   . VAL   A 1 47  ? 29.166 10.315  4.158   1.00 23.28  ? 27  VAL   A HA   1 
ATOM   275  H HB   . VAL   A 1 47  ? 31.198 12.245  4.619   1.00 22.01  ? 27  VAL   A HB   1 
ATOM   276  H HG11 . VAL   A 1 47  ? 32.676 10.399  4.153   1.00 23.60  ? 27  VAL   A HG11 1 
ATOM   277  H HG12 . VAL   A 1 47  ? 31.989 10.370  5.585   1.00 23.60  ? 27  VAL   A HG12 1 
ATOM   278  H HG13 . VAL   A 1 47  ? 31.428 9.452   4.417   1.00 23.60  ? 27  VAL   A HG13 1 
ATOM   279  H HG21 . VAL   A 1 47  ? 31.860 11.790  2.442   1.00 23.60  ? 27  VAL   A HG21 1 
ATOM   280  H HG22 . VAL   A 1 47  ? 30.583 10.860  2.268   1.00 23.60  ? 27  VAL   A HG22 1 
ATOM   281  H HG23 . VAL   A 1 47  ? 30.403 12.422  2.496   1.00 23.60  ? 27  VAL   A HG23 1 
ATOM   282  N N    . GLU   A 1 48  ? 29.486 11.785  6.992   1.00 20.32  ? 28  GLU   A N    1 
ATOM   283  C CA   . GLU   A 1 48  ? 29.405 11.557  8.426   1.00 22.20  ? 28  GLU   A CA   1 
ATOM   284  C C    . GLU   A 1 48  ? 28.118 10.839  8.791   1.00 21.41  ? 28  GLU   A C    1 
ATOM   285  O O    . GLU   A 1 48  ? 28.132 9.876   9.564   1.00 22.35  ? 28  GLU   A O    1 
ATOM   286  C CB   . GLU   A 1 48  ? 29.482 12.884  9.182   1.00 26.24  ? 28  GLU   A CB   1 
ATOM   287  C CG   . GLU   A 1 48  ? 30.835 13.586  9.056   1.00 32.56  ? 28  GLU   A CG   1 
ATOM   288  C CD   . GLU   A 1 48  ? 30.918 14.963  9.704   1.00 41.85  ? 28  GLU   A CD   1 
ATOM   289  O OE1  . GLU   A 1 48  ? 29.870 15.557  10.059  1.00 46.24  ? 28  GLU   A OE1  1 
ATOM   290  O OE2  . GLU   A 1 48  ? 32.067 15.450  9.845   1.00 46.35  ? 28  GLU   A OE2  1 
ATOM   291  H H    . GLU   A 1 48  ? 29.563 12.610  6.763   1.00 24.39  ? 28  GLU   A H    1 
ATOM   292  H HA   . GLU   A 1 48  ? 30.159 11.007  8.689   1.00 26.64  ? 28  GLU   A HA   1 
ATOM   293  H HB2  . GLU   A 1 48  ? 28.804 13.483  8.832   1.00 31.49  ? 28  GLU   A HB2  1 
ATOM   294  H HB3  . GLU   A 1 48  ? 29.322 12.716  10.124  1.00 31.49  ? 28  GLU   A HB3  1 
ATOM   295  H HG2  . GLU   A 1 48  ? 31.509 13.028  9.475   1.00 39.07  ? 28  GLU   A HG2  1 
ATOM   296  H HG3  . GLU   A 1 48  ? 31.036 13.697  8.114   1.00 39.07  ? 28  GLU   A HG3  1 
ATOM   297  N N    . GLN   A 1 49  ? 26.990 11.294  8.243   1.00 20.07  ? 29  GLN   A N    1 
ATOM   298  C CA   . GLN   A 1 49  ? 25.725 10.649  8.551   1.00 21.51  ? 29  GLN   A CA   1 
ATOM   299  C C    . GLN   A 1 49  ? 25.726 9.193   8.113   1.00 20.59  ? 29  GLN   A C    1 
ATOM   300  O O    . GLN   A 1 49  ? 25.296 8.307   8.865   1.00 21.39  ? 29  GLN   A O    1 
ATOM   301  C CB   . GLN   A 1 49  ? 24.573 11.378  7.884   1.00 23.41  ? 29  GLN   A CB   1 
ATOM   302  C CG   . GLN   A 1 49  ? 23.282 10.826  8.374   0.70 25.44  ? 29  GLN   A CG   1 
ATOM   303  C CD   . GLN   A 1 49  ? 22.096 11.464  7.729   0.59 29.20  ? 29  GLN   A CD   1 
ATOM   304  O OE1  . GLN   A 1 49  ? 22.137 12.630  7.286   0.87 33.15  ? 29  GLN   A OE1  1 
ATOM   305  N NE2  . GLN   A 1 49  ? 21.006 10.703  7.670   0.84 30.38  ? 29  GLN   A NE2  1 
ATOM   306  H H    . GLN   A 1 49  ? 26.936 11.961  7.703   1.00 24.08  ? 29  GLN   A H    1 
ATOM   307  H HA   . GLN   A 1 49  ? 25.599 10.690  9.512   1.00 25.81  ? 29  GLN   A HA   1 
ATOM   308  H HB2  . GLN   A 1 49  ? 24.613 12.322  8.102   1.00 28.10  ? 29  GLN   A HB2  1 
ATOM   309  H HB3  . GLN   A 1 49  ? 24.621 11.256  6.923   1.00 28.10  ? 29  GLN   A HB3  1 
ATOM   310  H HG2  . GLN   A 1 49  ? 23.252 9.876   8.183   0.70 30.53  ? 29  GLN   A HG2  1 
ATOM   311  H HG3  . GLN   A 1 49  ? 23.219 10.975  9.331   0.70 30.53  ? 29  GLN   A HG3  1 
ATOM   312  H HE21 . GLN   A 1 49  ? 21.021 9.906   7.992   0.87 36.46  ? 29  GLN   A HE21 1 
ATOM   313  H HE22 . GLN   A 1 49  ? 20.287 11.009  7.311   0.85 36.46  ? 29  GLN   A HE22 1 
ATOM   314  N N    . TYR   A 1 50  ? 26.196 8.923   6.886   1.00 18.99  ? 30  TYR   A N    1 
ATOM   315  C CA   . TYR   A 1 50  ? 26.268 7.544   6.404   1.00 18.04  ? 30  TYR   A CA   1 
ATOM   316  C C    . TYR   A 1 50  ? 27.074 6.671   7.358   1.00 18.49  ? 30  TYR   A C    1 
ATOM   317  O O    . TYR   A 1 50  ? 26.641 5.579   7.737   1.00 18.18  ? 30  TYR   A O    1 
ATOM   318  C CB   . TYR   A 1 50  ? 26.882 7.522   5.006   1.00 17.91  ? 30  TYR   A CB   1 
ATOM   319  C CG   . TYR   A 1 50  ? 26.946 6.150   4.380   1.00 16.82  ? 30  TYR   A CG   1 
ATOM   320  C CD1  . TYR   A 1 50  ? 27.895 5.211   4.776   1.00 16.74  ? 30  TYR   A CD1  1 
ATOM   321  C CD2  . TYR   A 1 50  ? 26.107 5.811   3.340   1.00 17.43  ? 30  TYR   A CD2  1 
ATOM   322  C CE1  . TYR   A 1 50  ? 27.945 3.974   4.198   1.00 17.25  ? 30  TYR   A CE1  1 
ATOM   323  C CE2  . TYR   A 1 50  ? 26.147 4.553   2.760   1.00 17.70  ? 30  TYR   A CE2  1 
ATOM   324  C CZ   . TYR   A 1 50  ? 27.082 3.648   3.184   1.00 17.61  ? 30  TYR   A CZ   1 
ATOM   325  O OH   . TYR   A 1 50  ? 27.140 2.409   2.597   1.00 20.04  ? 30  TYR   A OH   1 
ATOM   326  H H    . TYR   A 1 50  ? 26.474 9.513   6.325   1.00 22.79  ? 30  TYR   A H    1 
ATOM   327  H HA   . TYR   A 1 50  ? 25.370 7.180   6.351   1.00 21.65  ? 30  TYR   A HA   1 
ATOM   328  H HB2  . TYR   A 1 50  ? 26.349 8.086   4.424   1.00 21.49  ? 30  TYR   A HB2  1 
ATOM   329  H HB3  . TYR   A 1 50  ? 27.788 7.864   5.060   1.00 21.49  ? 30  TYR   A HB3  1 
ATOM   330  H HD1  . TYR   A 1 50  ? 28.503 5.429   5.445   1.00 20.09  ? 30  TYR   A HD1  1 
ATOM   331  H HD2  . TYR   A 1 50  ? 25.502 6.441   3.021   1.00 20.92  ? 30  TYR   A HD2  1 
ATOM   332  H HE1  . TYR   A 1 50  ? 28.567 3.350   4.494   1.00 20.70  ? 30  TYR   A HE1  1 
ATOM   333  H HE2  . TYR   A 1 50  ? 25.544 4.325   2.090   1.00 21.25  ? 30  TYR   A HE2  1 
ATOM   334  H HH   . TYR   A 1 50  ? 26.525 2.331   2.030   1.00 24.05  ? 30  TYR   A HH   1 
ATOM   335  N N    . MET   A 1 51  ? 28.272 7.125   7.730   1.00 18.37  ? 31  MET   A N    1 
ATOM   336  C CA   . MET   A 1 51  ? 29.164 6.310   8.534   1.00 18.88  ? 31  MET   A CA   1 
ATOM   337  C C    . MET   A 1 51  ? 28.629 6.057   9.929   1.00 18.81  ? 31  MET   A C    1 
ATOM   338  O O    . MET   A 1 51  ? 28.985 5.043   10.542  1.00 19.03  ? 31  MET   A O    1 
ATOM   339  C CB   . MET   A 1 51  ? 30.561 6.926   8.618   1.00 20.00  ? 31  MET   A CB   1 
ATOM   340  C CG   . MET   A 1 51  ? 31.272 7.074   7.268   1.00 19.63  ? 31  MET   A CG   1 
ATOM   341  S SD   . MET   A 1 51  ? 31.438 5.574   6.304   1.00 18.12  ? 31  MET   A SD   1 
ATOM   342  C CE   . MET   A 1 51  ? 32.256 4.486   7.461   1.00 18.60  ? 31  MET   A CE   1 
ATOM   343  H H    . MET   A 1 51  ? 28.587 7.899   7.528   1.00 22.05  ? 31  MET   A H    1 
ATOM   344  H HA   . MET   A 1 51  ? 29.248 5.459   8.075   1.00 22.66  ? 31  MET   A HA   1 
ATOM   345  H HB2  . MET   A 1 51  ? 30.486 7.811   9.007   1.00 24.00  ? 31  MET   A HB2  1 
ATOM   346  H HB3  . MET   A 1 51  ? 31.115 6.362   9.180   1.00 24.00  ? 31  MET   A HB3  1 
ATOM   347  H HG2  . MET   A 1 51  ? 30.773 7.707   6.729   1.00 23.56  ? 31  MET   A HG2  1 
ATOM   348  H HG3  . MET   A 1 51  ? 32.168 7.410   7.430   1.00 23.56  ? 31  MET   A HG3  1 
ATOM   349  H HE1  . MET   A 1 51  ? 32.426 3.635   7.028   1.00 22.32  ? 31  MET   A HE1  1 
ATOM   350  H HE2  . MET   A 1 51  ? 33.094 4.890   7.737   1.00 22.32  ? 31  MET   A HE2  1 
ATOM   351  H HE3  . MET   A 1 51  ? 31.682 4.356   8.233   1.00 22.32  ? 31  MET   A HE3  1 
ATOM   352  N N    A HIS   A 1 52  ? 27.782 6.943   10.451  0.53 19.36  ? 32  HIS   A N    1 
ATOM   353  N N    B HIS   A 1 52  ? 27.785 6.950   10.453  0.47 19.39  ? 32  HIS   A N    1 
ATOM   354  C CA   A HIS   A 1 52  ? 27.222 6.760   11.779  0.53 21.01  ? 32  HIS   A CA   1 
ATOM   355  C CA   B HIS   A 1 52  ? 27.214 6.775   11.780  0.47 21.02  ? 32  HIS   A CA   1 
ATOM   356  C C    A HIS   A 1 52  ? 25.823 6.154   11.765  0.53 20.87  ? 32  HIS   A C    1 
ATOM   357  C C    B HIS   A 1 52  ? 25.867 6.062   11.772  0.47 20.89  ? 32  HIS   A C    1 
ATOM   358  O O    A HIS   A 1 52  ? 25.206 6.036   12.828  0.53 24.38  ? 32  HIS   A O    1 
ATOM   359  O O    B HIS   A 1 52  ? 25.330 5.788   12.849  0.47 24.25  ? 32  HIS   A O    1 
ATOM   360  C CB   A HIS   A 1 52  ? 27.242 8.078   12.544  0.53 24.77  ? 32  HIS   A CB   1 
ATOM   361  C CB   B HIS   A 1 52  ? 27.052 8.127   12.469  0.47 24.79  ? 32  HIS   A CB   1 
ATOM   362  C CG   A HIS   A 1 52  ? 28.613 8.473   12.991  0.53 30.60  ? 32  HIS   A CG   1 
ATOM   363  C CG   B HIS   A 1 52  ? 28.344 8.732   12.908  0.47 31.03  ? 32  HIS   A CG   1 
ATOM   364  N ND1  A HIS   A 1 52  ? 29.521 9.092   12.158  0.53 35.07  ? 32  HIS   A ND1  1 
ATOM   365  N ND1  B HIS   A 1 52  ? 29.435 7.974   13.275  0.47 35.56  ? 32  HIS   A ND1  1 
ATOM   366  C CD2  A HIS   A 1 52  ? 29.246 8.298   14.174  0.53 35.28  ? 32  HIS   A CD2  1 
ATOM   367  C CD2  B HIS   A 1 52  ? 28.718 10.025  13.047  0.47 35.60  ? 32  HIS   A CD2  1 
ATOM   368  C CE1  A HIS   A 1 52  ? 30.643 9.310   12.821  0.53 37.22  ? 32  HIS   A CE1  1 
ATOM   369  C CE1  B HIS   A 1 52  ? 30.432 8.776   13.606  0.47 37.23  ? 32  HIS   A CE1  1 
ATOM   370  N NE2  A HIS   A 1 52  ? 30.504 8.832   14.043  0.53 36.67  ? 32  HIS   A NE2  1 
ATOM   371  N NE2  B HIS   A 1 52  ? 30.023 10.024  13.475  0.47 37.34  ? 32  HIS   A NE2  1 
ATOM   372  H H    A HIS   A 1 52  ? 27.519 7.658   10.051  0.53 23.23  ? 32  HIS   A H    1 
ATOM   373  H H    B HIS   A 1 52  ? 27.530 7.668   10.053  0.47 23.27  ? 32  HIS   A H    1 
ATOM   374  H HA   A HIS   A 1 52  ? 27.786 6.138   12.265  0.53 25.22  ? 32  HIS   A HA   1 
ATOM   375  H HA   B HIS   A 1 52  ? 27.833 6.238   12.299  0.47 25.23  ? 32  HIS   A HA   1 
ATOM   376  H HB2  A HIS   A 1 52  ? 26.901 8.780   11.970  0.53 29.73  ? 32  HIS   A HB2  1 
ATOM   377  H HB2  B HIS   A 1 52  ? 26.630 8.744   11.851  0.47 29.75  ? 32  HIS   A HB2  1 
ATOM   378  H HB3  A HIS   A 1 52  ? 26.684 7.992   13.332  0.53 29.73  ? 32  HIS   A HB3  1 
ATOM   379  H HB3  B HIS   A 1 52  ? 26.495 8.012   13.255  0.47 29.75  ? 32  HIS   A HB3  1 
ATOM   380  H HD1  A HIS   A 1 52  ? 29.379 9.303   11.336  0.53 42.08  ? 32  HIS   A HD1  1 
ATOM   381  H HD2  A HIS   A 1 52  ? 28.895 7.892   14.934  0.53 42.34  ? 32  HIS   A HD2  1 
ATOM   382  H HD2  B HIS   A 1 52  ? 28.190 10.773  12.882  0.47 42.72  ? 32  HIS   A HD2  1 
ATOM   383  H HE1  A HIS   A 1 52  ? 31.402 9.729   12.483  0.53 44.67  ? 32  HIS   A HE1  1 
ATOM   384  H HE1  B HIS   A 1 52  ? 31.277 8.507   13.885  0.47 44.68  ? 32  HIS   A HE1  1 
ATOM   385  H HE2  B HIS   A 1 52  ? 30.497 10.724  13.632  0.47 44.82  ? 32  HIS   A HE2  1 
ATOM   386  N N    . THR   A 1 53  ? 25.321 5.742   10.601  1.00 20.12  ? 33  THR   A N    1 
ATOM   387  C CA   . THR   A 1 53  ? 23.996 5.119   10.528  1.00 21.01  ? 33  THR   A CA   1 
ATOM   388  C C    . THR   A 1 53  ? 24.085 3.684   11.006  1.00 22.69  ? 33  THR   A C    1 
ATOM   389  O O    . THR   A 1 53  ? 24.866 2.888   10.467  1.00 23.37  ? 33  THR   A O    1 
ATOM   390  C CB   . THR   A 1 53  ? 23.452 5.170   9.105   1.00 21.25  ? 33  THR   A CB   1 
ATOM   391  O OG1  . THR   A 1 53  ? 23.267 6.531   8.708   1.00 22.62  ? 33  THR   A OG1  1 
ATOM   392  C CG2  . THR   A 1 53  ? 22.087 4.514   9.021   1.00 22.51  ? 33  THR   A CG2  1 
ATOM   393  H H    A THR   A 1 53  ? 25.724 5.811   9.845   0.53 24.14  ? 33  THR   A H    1 
ATOM   394  H H    B THR   A 1 53  ? 25.694 5.873   9.837   0.47 24.14  ? 33  THR   A H    1 
ATOM   395  H HA   . THR   A 1 53  ? 23.384 5.606   11.101  1.00 25.21  ? 33  THR   A HA   1 
ATOM   396  H HB   . THR   A 1 53  ? 24.081 4.712   8.525   1.00 25.50  ? 33  THR   A HB   1 
ATOM   397  H HG1  . THR   A 1 53  ? 24.000 6.942   8.739   1.00 27.14  ? 33  THR   A HG1  1 
ATOM   398  H HG21 . THR   A 1 53  ? 21.672 4.721   8.170   1.00 27.01  ? 33  THR   A HG21 1 
ATOM   399  H HG22 . THR   A 1 53  ? 22.176 3.552   9.103   1.00 27.01  ? 33  THR   A HG22 1 
ATOM   400  H HG23 . THR   A 1 53  ? 21.519 4.840   9.737   1.00 27.01  ? 33  THR   A HG23 1 
ATOM   401  N N    . ARG   A 1 54  ? 23.269 3.352   11.999  1.00 22.20  ? 34  ARG   A N    1 
ATOM   402  C CA   . ARG   A 1 54  ? 23.299 2.049   12.631  1.00 24.41  ? 34  ARG   A CA   1 
ATOM   403  C C    . ARG   A 1 54  ? 21.890 1.617   12.970  1.00 23.71  ? 34  ARG   A C    1 
ATOM   404  O O    . ARG   A 1 54  ? 20.968 2.421   13.012  1.00 25.06  ? 34  ARG   A O    1 
ATOM   405  C CB   . ARG   A 1 54  ? 24.096 2.083   13.945  1.00 30.56  ? 34  ARG   A CB   1 
ATOM   406  C CG   . ARG   A 1 54  ? 25.474 2.618   13.832  1.00 39.98  ? 34  ARG   A CG   1 
ATOM   407  C CD   . ARG   A 1 54  ? 26.167 2.398   15.144  1.00 53.45  ? 34  ARG   A CD   1 
ATOM   408  N NE   . ARG   A 1 54  ? 25.890 3.442   16.126  1.00 32.47  ? 34  ARG   A NE   1 
ATOM   409  C CZ   . ARG   A 1 54  ? 26.731 4.436   16.384  1.00 32.27  ? 34  ARG   A CZ   1 
ATOM   410  N NH1  . ARG   A 1 54  ? 27.803 4.641   15.628  1.00 38.41  ? 34  ARG   A NH1  1 
ATOM   411  N NH2  . ARG   A 1 54  ? 26.532 5.200   17.463  1.00 29.50  ? 34  ARG   A NH2  1 
ATOM   412  H H    . ARG   A 1 54  ? 22.676 3.881   12.329  1.00 26.64  ? 34  ARG   A H    1 
ATOM   413  H HA   . ARG   A 1 54  ? 23.696 1.419   12.010  1.00 29.29  ? 34  ARG   A HA   1 
ATOM   414  H HB2  . ARG   A 1 54  ? 23.619 2.642   14.579  1.00 36.67  ? 34  ARG   A HB2  1 
ATOM   415  H HB3  . ARG   A 1 54  ? 24.163 1.178   14.286  1.00 36.67  ? 34  ARG   A HB3  1 
ATOM   416  H HG2  . ARG   A 1 54  ? 25.958 2.150   13.133  1.00 47.98  ? 34  ARG   A HG2  1 
ATOM   417  H HG3  . ARG   A 1 54  ? 25.449 3.568   13.639  1.00 47.98  ? 34  ARG   A HG3  1 
ATOM   418  H HD2  . ARG   A 1 54  ? 25.873 1.553   15.518  1.00 64.14  ? 34  ARG   A HD2  1 
ATOM   419  H HD3  . ARG   A 1 54  ? 27.125 2.379   14.994  1.00 64.14  ? 34  ARG   A HD3  1 
ATOM   420  H HE   . ARG   A 1 54  ? 25.147 3.411   16.558  1.00 38.97  ? 34  ARG   A HE   1 
ATOM   421  H HH11 . ARG   A 1 54  ? 27.963 4.126   14.958  1.00 46.09  ? 34  ARG   A HH11 1 
ATOM   422  H HH12 . ARG   A 1 54  ? 28.339 5.290   15.808  1.00 46.09  ? 34  ARG   A HH12 1 
ATOM   423  H HH21 . ARG   A 1 54  ? 25.864 5.046   17.982  1.00 35.40  ? 34  ARG   A HH21 1 
ATOM   424  H HH22 . ARG   A 1 54  ? 27.072 5.847   17.637  1.00 35.40  ? 34  ARG   A HH22 1 
ATOM   425  N N    . GLY   A 1 55  ? 21.749 0.329   13.233  1.00 23.62  ? 35  GLY   A N    1 
ATOM   426  C CA   . GLY   A 1 55  ? 20.464 -0.171  13.686  1.00 24.44  ? 35  GLY   A CA   1 
ATOM   427  C C    . GLY   A 1 55  ? 19.379 0.020   12.650  1.00 24.55  ? 35  GLY   A C    1 
ATOM   428  O O    . GLY   A 1 55  ? 19.608 -0.075  11.433  1.00 23.12  ? 35  GLY   A O    1 
ATOM   429  H H    . GLY   A 1 55  ? 22.368 -0.264  13.159  1.00 28.35  ? 35  GLY   A H    1 
ATOM   430  H HA2  . GLY   A 1 55  ? 20.537 -1.119  13.881  1.00 29.33  ? 35  GLY   A HA2  1 
ATOM   431  H HA3  . GLY   A 1 55  ? 20.202 0.298   14.494  1.00 29.33  ? 35  GLY   A HA3  1 
ATOM   432  N N    . GLU   A 1 56  ? 18.166 0.294   13.142  1.00 27.09  ? 36  GLU   A N    1 
ATOM   433  C CA   . GLU   A 1 56  ? 17.021 0.383   12.253  1.00 28.24  ? 36  GLU   A CA   1 
ATOM   434  C C    . GLU   A 1 56  ? 17.150 1.527   11.266  1.00 25.99  ? 36  GLU   A C    1 
ATOM   435  O O    . GLU   A 1 56  ? 16.544 1.483   10.188  1.00 25.98  ? 36  GLU   A O    1 
ATOM   436  C CB   . GLU   A 1 56  ? 15.744 0.581   13.076  1.00 34.64  ? 36  GLU   A CB   1 
ATOM   437  C CG   . GLU   A 1 56  ? 15.427 -0.572  13.995  1.00 44.20  ? 36  GLU   A CG   1 
ATOM   438  C CD   . GLU   A 1 56  ? 15.107 -1.851  13.241  1.00 52.78  ? 36  GLU   A CD   1 
ATOM   439  O OE1  . GLU   A 1 56  ? 14.157 -1.849  12.427  1.00 55.37  ? 36  GLU   A OE1  1 
ATOM   440  O OE2  . GLU   A 1 56  ? 15.819 -2.857  13.458  1.00 56.48  ? 36  GLU   A OE2  1 
ATOM   441  H H    . GLU   A 1 56  ? 17.990 0.430   13.973  1.00 32.51  ? 36  GLU   A H    1 
ATOM   442  H HA   . GLU   A 1 56  ? 16.951 -0.447  11.755  1.00 33.88  ? 36  GLU   A HA   1 
ATOM   443  H HB2  . GLU   A 1 56  ? 15.846 1.376   13.623  1.00 41.57  ? 36  GLU   A HB2  1 
ATOM   444  H HB3  . GLU   A 1 56  ? 14.995 0.690   12.469  1.00 41.57  ? 36  GLU   A HB3  1 
ATOM   445  H HG2  . GLU   A 1 56  ? 16.194 -0.743  14.564  1.00 53.04  ? 36  GLU   A HG2  1 
ATOM   446  H HG3  . GLU   A 1 56  ? 14.656 -0.343  14.538  1.00 53.04  ? 36  GLU   A HG3  1 
ATOM   447  N N    . ALA   A 1 57  ? 17.928 2.559   11.611  1.00 24.89  ? 37  ALA   A N    1 
ATOM   448  C CA   . ALA   A 1 57  ? 18.149 3.671   10.698  1.00 24.05  ? 37  ALA   A CA   1 
ATOM   449  C C    . ALA   A 1 57  ? 18.807 3.230   9.394   1.00 22.13  ? 37  ALA   A C    1 
ATOM   450  O O    . ALA   A 1 57  ? 18.687 3.925   8.379   1.00 22.26  ? 37  ALA   A O    1 
ATOM   451  C CB   . ALA   A 1 57  ? 18.990 4.746   11.393  1.00 26.04  ? 37  ALA   A CB   1 
ATOM   452  H H    . ALA   A 1 57  ? 18.336 2.634   12.365  1.00 29.87  ? 37  ALA   A H    1 
ATOM   453  H HA   . ALA   A 1 57  ? 17.294 4.067   10.465  1.00 28.86  ? 37  ALA   A HA   1 
ATOM   454  H HB1  . ALA   A 1 57  ? 19.137 5.480   10.777  1.00 31.25  ? 37  ALA   A HB1  1 
ATOM   455  H HB2  . ALA   A 1 57  ? 18.514 5.062   12.177  1.00 31.25  ? 37  ALA   A HB2  1 
ATOM   456  H HB3  . ALA   A 1 57  ? 19.841 4.360   11.657  1.00 31.25  ? 37  ALA   A HB3  1 
ATOM   457  N N    . ARG   A 1 58  ? 19.482 2.084   9.385   1.00 20.41  ? 38  ARG   A N    1 
ATOM   458  C CA   . ARG   A 1 58  ? 20.020 1.572   8.135   1.00 19.40  ? 38  ARG   A CA   1 
ATOM   459  C C    . ARG   A 1 58  ? 18.943 1.369   7.077   1.00 20.41  ? 38  ARG   A C    1 
ATOM   460  O O    . ARG   A 1 58  ? 19.247 1.411   5.881   1.00 20.66  ? 38  ARG   A O    1 
ATOM   461  C CB   . ARG   A 1 58  ? 20.789 0.287   8.420   1.00 20.48  ? 38  ARG   A CB   1 
ATOM   462  C CG   . ARG   A 1 58  ? 22.078 0.556   9.221   1.00 22.89  ? 38  ARG   A CG   1 
ATOM   463  C CD   . ARG   A 1 58  ? 22.585 -0.633  10.019  1.00 25.70  ? 38  ARG   A CD   1 
ATOM   464  N NE   . ARG   A 1 58  ? 22.868 -1.753  9.152   1.00 26.69  ? 38  ARG   A NE   1 
ATOM   465  C CZ   . ARG   A 1 58  ? 23.095 -2.986  9.596   1.00 24.47  ? 38  ARG   A CZ   1 
ATOM   466  N NH1  . ARG   A 1 58  ? 23.052 -3.270  10.881  1.00 27.08  ? 38  ARG   A NH1  1 
ATOM   467  N NH2  . ARG   A 1 58  ? 23.311 -3.960  8.725   1.00 24.52  ? 38  ARG   A NH2  1 
ATOM   468  H H    . ARG   A 1 58  ? 19.639 1.596   10.076  1.00 24.49  ? 38  ARG   A H    1 
ATOM   469  H HA   . ARG   A 1 58  ? 20.640 2.217   7.759   1.00 23.29  ? 38  ARG   A HA   1 
ATOM   470  H HB2  . ARG   A 1 58  ? 20.229 -0.313  8.937   1.00 24.58  ? 38  ARG   A HB2  1 
ATOM   471  H HB3  . ARG   A 1 58  ? 21.035 -0.131  7.579   1.00 24.58  ? 38  ARG   A HB3  1 
ATOM   472  H HG2  . ARG   A 1 58  ? 22.780 0.812   8.603   1.00 27.47  ? 38  ARG   A HG2  1 
ATOM   473  H HG3  . ARG   A 1 58  ? 21.908 1.276   9.848   1.00 27.47  ? 38  ARG   A HG3  1 
ATOM   474  H HD2  . ARG   A 1 58  ? 23.401 -0.388  10.481  1.00 30.84  ? 38  ARG   A HD2  1 
ATOM   475  H HD3  . ARG   A 1 58  ? 21.909 -0.904  10.660  1.00 30.84  ? 38  ARG   A HD3  1 
ATOM   476  H HE   . ARG   A 1 58  ? 22.891 -1.615  8.304   1.00 32.02  ? 38  ARG   A HE   1 
ATOM   477  H HH11 . ARG   A 1 58  ? 22.875 -2.653  11.453  1.00 32.50  ? 38  ARG   A HH11 1 
ATOM   478  H HH12 . ARG   A 1 58  ? 23.202 -4.074  11.149  1.00 32.50  ? 38  ARG   A HH12 1 
ATOM   479  H HH21 . ARG   A 1 58  ? 23.304 -3.792  7.882   1.00 29.42  ? 38  ARG   A HH21 1 
ATOM   480  H HH22 . ARG   A 1 58  ? 23.459 -4.760  9.003   1.00 29.42  ? 38  ARG   A HH22 1 
ATOM   481  N N    . LEU   A 1 59  ? 17.687 1.140   7.488   1.00 21.06  ? 39  LEU   A N    1 
ATOM   482  C CA   . LEU   A 1 59  ? 16.627 0.949   6.511   1.00 22.29  ? 39  LEU   A CA   1 
ATOM   483  C C    . LEU   A 1 59  ? 16.324 2.203   5.704   1.00 23.38  ? 39  LEU   A C    1 
ATOM   484  O O    . LEU   A 1 59  ? 15.667 2.101   4.664   1.00 24.15  ? 39  LEU   A O    1 
ATOM   485  C CB   . LEU   A 1 59  ? 15.358 0.452   7.204   1.00 23.55  ? 39  LEU   A CB   1 
ATOM   486  C CG   . LEU   A 1 59  ? 15.481 -0.947  7.820   1.00 27.84  ? 39  LEU   A CG   1 
ATOM   487  C CD1  . LEU   A 1 59  ? 14.194 -1.318  8.556   1.00 31.41  ? 39  LEU   A CD1  1 
ATOM   488  C CD2  . LEU   A 1 59  ? 15.849 -2.002  6.757   1.00 30.51  ? 39  LEU   A CD2  1 
ATOM   489  H H    . LEU   A 1 59  ? 17.437 1.094   8.309   1.00 25.28  ? 39  LEU   A H    1 
ATOM   490  H HA   . LEU   A 1 59  ? 16.909 0.264   5.884   1.00 26.75  ? 39  LEU   A HA   1 
ATOM   491  H HB2  . LEU   A 1 59  ? 15.134 1.069   7.918   1.00 28.26  ? 39  LEU   A HB2  1 
ATOM   492  H HB3  . LEU   A 1 59  ? 14.640 0.425   6.552   1.00 28.26  ? 39  LEU   A HB3  1 
ATOM   493  H HG   . LEU   A 1 59  ? 16.203 -0.942  8.468   1.00 33.41  ? 39  LEU   A HG   1 
ATOM   494  H HD11 . LEU   A 1 59  ? 14.295 -2.200  8.946   1.00 37.69  ? 39  LEU   A HD11 1 
ATOM   495  H HD12 . LEU   A 1 59  ? 14.030 -0.665  9.254   1.00 37.69  ? 39  LEU   A HD12 1 
ATOM   496  H HD13 . LEU   A 1 59  ? 13.458 -1.318  7.924   1.00 37.69  ? 39  LEU   A HD13 1 
ATOM   497  H HD21 . LEU   A 1 59  ? 15.647 -2.885  7.105   1.00 36.62  ? 39  LEU   A HD21 1 
ATOM   498  H HD22 . LEU   A 1 59  ? 15.331 -1.836  5.954   1.00 36.62  ? 39  LEU   A HD22 1 
ATOM   499  H HD23 . LEU   A 1 59  ? 16.797 -1.934  6.560   1.00 36.62  ? 39  LEU   A HD23 1 
ATOM   500  N N    . LYS   A 1 60  ? 16.806 3.370   6.137   1.00 22.92  ? 40  LYS   A N    1 
ATOM   501  C CA   . LYS   A 1 60  ? 16.583 4.627   5.428   1.00 23.90  ? 40  LYS   A CA   1 
ATOM   502  C C    . LYS   A 1 60  ? 17.871 5.229   4.884   1.00 22.49  ? 40  LYS   A C    1 
ATOM   503  O O    . LYS   A 1 60  ? 17.854 6.330   4.332   1.00 23.36  ? 40  LYS   A O    1 
ATOM   504  C CB   . LYS   A 1 60  ? 15.856 5.636   6.327   1.00 28.67  ? 40  LYS   A CB   1 
ATOM   505  C CG   . LYS   A 1 60  ? 14.410 5.196   6.630   1.00 36.90  ? 40  LYS   A CG   1 
ATOM   506  C CD   . LYS   A 1 60  ? 13.941 5.608   8.007   1.00 46.10  ? 40  LYS   A CD   1 
ATOM   507  C CE   . LYS   A 1 60  ? 13.535 7.065   8.066   1.00 51.93  ? 40  LYS   A CE   1 
ATOM   508  N NZ   . LYS   A 1 60  ? 12.451 7.289   9.092   1.00 55.48  ? 40  LYS   A NZ   1 
ATOM   509  H H    . LYS   A 1 60  ? 17.275 3.458   6.853   1.00 27.50  ? 40  LYS   A H    1 
ATOM   510  H HA   . LYS   A 1 60  ? 16.004 4.448   4.672   1.00 28.69  ? 40  LYS   A HA   1 
ATOM   511  H HB2  . LYS   A 1 60  ? 16.332 5.715   7.169   1.00 34.41  ? 40  LYS   A HB2  1 
ATOM   512  H HB3  . LYS   A 1 60  ? 15.825 6.497   5.881   1.00 34.41  ? 40  LYS   A HB3  1 
ATOM   513  H HG2  . LYS   A 1 60  ? 13.815 5.599   5.979   1.00 44.28  ? 40  LYS   A HG2  1 
ATOM   514  H HG3  . LYS   A 1 60  ? 14.357 4.229   6.574   1.00 44.28  ? 40  LYS   A HG3  1 
ATOM   515  H HD2  . LYS   A 1 60  ? 13.172 5.071   8.255   1.00 55.33  ? 40  LYS   A HD2  1 
ATOM   516  H HD3  . LYS   A 1 60  ? 14.660 5.470   8.643   1.00 55.33  ? 40  LYS   A HD3  1 
ATOM   517  H HE2  . LYS   A 1 60  ? 14.303 7.604   8.310   1.00 62.32  ? 40  LYS   A HE2  1 
ATOM   518  H HE3  . LYS   A 1 60  ? 13.197 7.340   7.199   1.00 62.32  ? 40  LYS   A HE3  1 
ATOM   519  H HZ1  . LYS   A 1 60  ? 12.244 8.154   9.133   1.00 66.57  ? 40  LYS   A HZ1  1 
ATOM   520  H HZ2  . LYS   A 1 60  ? 11.722 6.829   8.871   1.00 66.57  ? 40  LYS   A HZ2  1 
ATOM   521  H HZ3  . LYS   A 1 60  ? 12.730 7.021   9.894   1.00 66.57  ? 40  LYS   A HZ3  1 
ATOM   522  N N    . ARG   A 1 61  ? 18.986 4.514   4.983   1.00 20.51  ? 41  ARG   A N    1 
ATOM   523  C CA   . ARG   A 1 61  ? 20.264 5.067   4.530   1.00 20.02  ? 41  ARG   A CA   1 
ATOM   524  C C    . ARG   A 1 61  ? 20.278 5.284   3.031   1.00 19.25  ? 41  ARG   A C    1 
ATOM   525  O O    . ARG   A 1 61  ? 20.997 6.158   2.542   1.00 19.08  ? 41  ARG   A O    1 
ATOM   526  C CB   . ARG   A 1 61  ? 21.402 4.134   4.936   1.00 20.88  ? 41  ARG   A CB   1 
ATOM   527  C CG   . ARG   A 1 61  ? 22.822 4.772   4.870   1.00 21.80  ? 41  ARG   A CG   1 
ATOM   528  C CD   . ARG   A 1 61  ? 23.898 3.780   5.361   1.00 21.82  ? 41  ARG   A CD   1 
ATOM   529  N NE   . ARG   A 1 61  ? 24.003 2.656   4.459   1.00 24.12  ? 41  ARG   A NE   1 
ATOM   530  C CZ   . ARG   A 1 61  ? 24.481 1.458   4.786   1.00 26.50  ? 41  ARG   A CZ   1 
ATOM   531  N NH1  . ARG   A 1 61  ? 24.905 1.191   6.009   1.00 27.61  ? 41  ARG   A NH1  1 
ATOM   532  N NH2  . ARG   A 1 61  ? 24.512 0.502   3.867   1.00 30.58  ? 41  ARG   A NH2  1 
ATOM   533  H H    . ARG   A 1 61  ? 19.033 3.717   5.304   1.00 24.62  ? 41  ARG   A H    1 
ATOM   534  H HA   . ARG   A 1 61  ? 20.416 5.923   4.960   1.00 24.02  ? 41  ARG   A HA   1 
ATOM   535  H HB2  . ARG   A 1 61  ? 21.253 3.846   5.851   1.00 25.06  ? 41  ARG   A HB2  1 
ATOM   536  H HB3  . ARG   A 1 61  ? 21.398 3.367   4.342   1.00 25.06  ? 41  ARG   A HB3  1 
ATOM   537  H HG2  . ARG   A 1 61  ? 23.024 5.015   3.953   1.00 26.17  ? 41  ARG   A HG2  1 
ATOM   538  H HG3  . ARG   A 1 61  ? 22.849 5.560   5.435   1.00 26.17  ? 41  ARG   A HG3  1 
ATOM   539  H HD2  . ARG   A 1 61  ? 24.758 4.226   5.400   1.00 26.19  ? 41  ARG   A HD2  1 
ATOM   540  H HD3  . ARG   A 1 61  ? 23.656 3.448   6.240   1.00 26.19  ? 41  ARG   A HD3  1 
ATOM   541  H HE   . ARG   A 1 61  ? 23.736 2.770   3.649   1.00 28.94  ? 41  ARG   A HE   1 
ATOM   542  H HH11 . ARG   A 1 61  ? 24.876 1.799   6.616   1.00 33.14  ? 41  ARG   A HH11 1 
ATOM   543  H HH12 . ARG   A 1 61  ? 25.210 0.409   6.197   1.00 33.14  ? 41  ARG   A HH12 1 
ATOM   544  H HH21 . ARG   A 1 61  ? 24.225 0.661   3.072   1.00 36.70  ? 41  ARG   A HH21 1 
ATOM   545  H HH22 . ARG   A 1 61  ? 24.819 -0.276  4.066   1.00 36.70  ? 41  ARG   A HH22 1 
ATOM   546  N N    . HIS   A 1 62  ? 19.454 4.551   2.285   1.00 18.85  ? 42  HIS   A N    1 
ATOM   547  C CA   . HIS   A 1 62  ? 19.405 4.728   0.840   1.00 18.90  ? 42  HIS   A CA   1 
ATOM   548  C C    . HIS   A 1 62  ? 18.899 6.116   0.452   1.00 19.29  ? 42  HIS   A C    1 
ATOM   549  O O    . HIS   A 1 62  ? 19.135 6.549   -0.683  1.00 19.26  ? 42  HIS   A O    1 
ATOM   550  C CB   . HIS   A 1 62  ? 18.564 3.630   0.193   1.00 20.13  ? 42  HIS   A CB   1 
ATOM   551  C CG   . HIS   A 1 62  ? 17.126 3.660   0.585   1.00 20.69  ? 42  HIS   A CG   1 
ATOM   552  N ND1  . HIS   A 1 62  ? 16.692 3.334   1.847   1.00 21.58  ? 42  HIS   A ND1  1 
ATOM   553  C CD2  . HIS   A 1 62  ? 16.023 3.972   -0.127  1.00 23.15  ? 42  HIS   A CD2  1 
ATOM   554  C CE1  . HIS   A 1 62  ? 15.370 3.436   1.895   1.00 22.88  ? 42  HIS   A CE1  1 
ATOM   555  N NE2  . HIS   A 1 62  ? 14.944 3.831   0.710   1.00 23.01  ? 42  HIS   A NE2  1 
ATOM   556  H H    . HIS   A 1 62  ? 18.919 3.950   2.590   1.00 22.63  ? 42  HIS   A H    1 
ATOM   557  H HA   . HIS   A 1 62  ? 20.301 4.637   0.480   1.00 22.68  ? 42  HIS   A HA   1 
ATOM   558  H HB2  . HIS   A 1 62  ? 18.610 3.730   -0.771  1.00 24.16  ? 42  HIS   A HB2  1 
ATOM   559  H HB3  . HIS   A 1 62  ? 18.924 2.768   0.455   1.00 24.16  ? 42  HIS   A HB3  1 
ATOM   560  H HD2  . HIS   A 1 62  ? 15.998 4.233   -1.019  1.00 27.78  ? 42  HIS   A HD2  1 
ATOM   561  H HE1  . HIS   A 1 62  ? 14.836 3.259   2.635   1.00 27.46  ? 42  HIS   A HE1  1 
ATOM   562  H HE2  . HIS   A 1 62  ? 14.123 3.976   0.497   1.00 27.62  ? 42  HIS   A HE2  1 
ATOM   563  N N    . LEU   A 1 63  ? 18.234 6.835   1.367   1.00 19.43  ? 43  LEU   A N    1 
ATOM   564  C CA   . LEU   A 1 63  ? 17.785 8.180   1.053   1.00 19.66  ? 43  LEU   A CA   1 
ATOM   565  C C    . LEU   A 1 63  ? 18.939 9.170   0.983   1.00 19.40  ? 43  LEU   A C    1 
ATOM   566  O O    . LEU   A 1 63  ? 18.739 10.323  0.591   1.00 21.29  ? 43  LEU   A O    1 
ATOM   567  C CB   . LEU   A 1 63  ? 16.756 8.646   2.072   1.00 22.46  ? 43  LEU   A CB   1 
ATOM   568  C CG   . LEU   A 1 63  ? 15.519 7.758   2.160   1.00 25.87  ? 43  LEU   A CG   1 
ATOM   569  C CD1  . LEU   A 1 63  ? 14.539 8.290   3.209   1.00 28.75  ? 43  LEU   A CD1  1 
ATOM   570  C CD2  . LEU   A 1 63  ? 14.844 7.708   0.788   1.00 26.82  ? 43  LEU   A CD2  1 
ATOM   571  H H    . LEU   A 1 63  ? 18.039 6.564   2.160   1.00 23.32  ? 43  LEU   A H    1 
ATOM   572  H HA   . LEU   A 1 63  ? 17.346 8.170   0.188   1.00 23.60  ? 43  LEU   A HA   1 
ATOM   573  H HB2  . LEU   A 1 63  ? 17.172 8.660   2.948   1.00 26.96  ? 43  LEU   A HB2  1 
ATOM   574  H HB3  . LEU   A 1 63  ? 16.462 9.538   1.830   1.00 26.96  ? 43  LEU   A HB3  1 
ATOM   575  H HG   . LEU   A 1 63  ? 15.780 6.862   2.428   1.00 31.05  ? 43  LEU   A HG   1 
ATOM   576  H HD11 . LEU   A 1 63  ? 13.766 7.705   3.245   1.00 34.50  ? 43  LEU   A HD11 1 
ATOM   577  H HD12 . LEU   A 1 63  ? 14.980 8.308   4.073   1.00 34.50  ? 43  LEU   A HD12 1 
ATOM   578  H HD13 . LEU   A 1 63  ? 14.264 9.186   2.959   1.00 34.50  ? 43  LEU   A HD13 1 
ATOM   579  H HD21 . LEU   A 1 63  ? 13.952 7.341   0.889   1.00 32.19  ? 43  LEU   A HD21 1 
ATOM   580  H HD22 . LEU   A 1 63  ? 14.794 8.607   0.429   1.00 32.19  ? 43  LEU   A HD22 1 
ATOM   581  H HD23 . LEU   A 1 63  ? 15.369 7.145   0.198   1.00 32.19  ? 43  LEU   A HD23 1 
ATOM   582  N N    . LEU   A 1 64  ? 20.159 8.749   1.316   1.00 17.67  ? 44  LEU   A N    1 
ATOM   583  C CA   . LEU   A 1 64  ? 21.343 9.581   1.139   1.00 17.74  ? 44  LEU   A CA   1 
ATOM   584  C C    . LEU   A 1 64  ? 21.925 9.487   -0.269  1.00 16.75  ? 44  LEU   A C    1 
ATOM   585  O O    . LEU   A 1 64  ? 22.924 10.146  -0.554  1.00 17.83  ? 44  LEU   A O    1 
ATOM   586  C CB   . LEU   A 1 64  ? 22.383 9.195   2.182   1.00 19.22  ? 44  LEU   A CB   1 
ATOM   587  C CG   . LEU   A 1 64  ? 21.990 9.360   3.643   1.00 19.70  ? 44  LEU   A CG   1 
ATOM   588  C CD1  . LEU   A 1 64  ? 23.164 8.970   4.527   1.00 20.63  ? 44  LEU   A CD1  1 
ATOM   589  C CD2  . LEU   A 1 64  ? 21.532 10.783  3.961   1.00 20.18  ? 44  LEU   A CD2  1 
ATOM   590  H H    . LEU   A 1 64  ? 20.327 7.975   1.651   1.00 21.21  ? 44  LEU   A H    1 
ATOM   591  H HA   . LEU   A 1 64  ? 21.114 10.513  1.283   1.00 21.29  ? 44  LEU   A HA   1 
ATOM   592  H HB2  . LEU   A 1 64  ? 22.603 8.259   2.052   1.00 23.06  ? 44  LEU   A HB2  1 
ATOM   593  H HB3  . LEU   A 1 64  ? 23.170 9.744   2.037   1.00 23.06  ? 44  LEU   A HB3  1 
ATOM   594  H HG   . LEU   A 1 64  ? 21.235 8.779   3.828   1.00 23.64  ? 44  LEU   A HG   1 
ATOM   595  H HD11 . LEU   A 1 64  ? 22.906 9.070   5.457   1.00 24.76  ? 44  LEU   A HD11 1 
ATOM   596  H HD12 . LEU   A 1 64  ? 23.402 8.047   4.348   1.00 24.76  ? 44  LEU   A HD12 1 
ATOM   597  H HD13 . LEU   A 1 64  ? 23.916 9.550   4.328   1.00 24.76  ? 44  LEU   A HD13 1 
ATOM   598  H HD21 . LEU   A 1 64  ? 21.376 10.859  4.915   1.00 24.22  ? 44  LEU   A HD21 1 
ATOM   599  H HD22 . LEU   A 1 64  ? 22.224 11.406  3.688   1.00 24.22  ? 44  LEU   A HD22 1 
ATOM   600  H HD23 . LEU   A 1 64  ? 20.712 10.967  3.476   1.00 24.22  ? 44  LEU   A HD23 1 
ATOM   601  N N    . PHE   A 1 65  ? 21.321 8.684   -1.144  1.00 17.93  ? 45  PHE   A N    1 
ATOM   602  C CA   . PHE   A 1 65  ? 21.758 8.460   -2.510  1.00 18.10  ? 45  PHE   A CA   1 
ATOM   603  C C    . PHE   A 1 65  ? 20.868 9.159   -3.520  1.00 18.71  ? 45  PHE   A C    1 
ATOM   604  O O    . PHE   A 1 65  ? 19.676 9.400   -3.281  1.00 20.56  ? 45  PHE   A O    1 
ATOM   605  C CB   . PHE   A 1 65  ? 21.769 6.966   -2.855  1.00 18.08  ? 45  PHE   A CB   1 
ATOM   606  C CG   . PHE   A 1 65  ? 22.845 6.186   -2.159  1.00 16.79  ? 45  PHE   A CG   1 
ATOM   607  C CD1  . PHE   A 1 65  ? 22.749 5.888   -0.816  1.00 17.47  ? 45  PHE   A CD1  1 
ATOM   608  C CD2  . PHE   A 1 65  ? 23.958 5.742   -2.863  1.00 17.03  ? 45  PHE   A CD2  1 
ATOM   609  C CE1  . PHE   A 1 65  ? 23.761 5.153   -0.169  1.00 19.61  ? 45  PHE   A CE1  1 
ATOM   610  C CE2  . PHE   A 1 65  ? 24.951 5.002   -2.246  1.00 16.88  ? 45  PHE   A CE2  1 
ATOM   611  C CZ   . PHE   A 1 65  ? 24.865 4.715   -0.898  1.00 18.41  ? 45  PHE   A CZ   1 
ATOM   612  H H    . PHE   A 1 65  ? 20.614 8.234   -0.953  1.00 21.52  ? 45  PHE   A H    1 
ATOM   613  H HA   . PHE   A 1 65  ? 22.653 8.828   -2.586  1.00 21.72  ? 45  PHE   A HA   1 
ATOM   614  H HB2  . PHE   A 1 65  ? 20.916 6.583   -2.600  1.00 21.70  ? 45  PHE   A HB2  1 
ATOM   615  H HB3  . PHE   A 1 65  ? 21.905 6.869   -3.810  1.00 21.70  ? 45  PHE   A HB3  1 
ATOM   616  H HD1  . PHE   A 1 65  ? 22.008 6.176   -0.333  1.00 20.97  ? 45  PHE   A HD1  1 
ATOM   617  H HD2  . PHE   A 1 65  ? 24.037 5.946   -3.767  1.00 20.44  ? 45  PHE   A HD2  1 
ATOM   618  H HE1  . PHE   A 1 65  ? 23.692 4.961   0.739   1.00 23.54  ? 45  PHE   A HE1  1 
ATOM   619  H HE2  . PHE   A 1 65  ? 25.678 4.698   -2.740  1.00 20.25  ? 45  PHE   A HE2  1 
ATOM   620  H HZ   . PHE   A 1 65  ? 25.541 4.232   -0.479  1.00 22.09  ? 45  PHE   A HZ   1 
ATOM   621  N N    . THR   A 1 66  ? 21.449 9.456   -4.678  1.00 19.30  ? 46  THR   A N    1 
ATOM   622  C CA   . THR   A 1 66  ? 20.651 9.846   -5.836  1.00 20.83  ? 46  THR   A CA   1 
ATOM   623  C C    . THR   A 1 66  ? 19.773 8.681   -6.279  1.00 20.50  ? 46  THR   A C    1 
ATOM   624  O O    . THR   A 1 66  ? 19.998 7.543   -5.905  1.00 20.12  ? 46  THR   A O    1 
ATOM   625  C CB   . THR   A 1 66  ? 21.553 10.263  -6.994  1.00 21.61  ? 46  THR   A CB   1 
ATOM   626  O OG1  . THR   A 1 66  ? 22.350 9.150   -7.412  1.00 21.20  ? 46  THR   A OG1  1 
ATOM   627  C CG2  . THR   A 1 66  ? 22.491 11.420  -6.590  1.00 22.24  ? 46  THR   A CG2  1 
ATOM   628  H H    . THR   A 1 66  ? 22.298 9.439   -4.820  1.00 23.17  ? 46  THR   A H    1 
ATOM   629  H HA   . THR   A 1 66  ? 20.088 10.600  -5.599  1.00 25.00  ? 46  THR   A HA   1 
ATOM   630  H HB   . THR   A 1 66  ? 20.995 10.567  -7.727  1.00 25.93  ? 46  THR   A HB   1 
ATOM   631  H HG1  . THR   A 1 66  ? 21.866 8.575   -7.788  1.00 25.44  ? 46  THR   A HG1  1 
ATOM   632  H HG21 . THR   A 1 66  ? 23.035 11.686  -7.348  1.00 26.69  ? 46  THR   A HG21 1 
ATOM   633  H HG22 . THR   A 1 66  ? 21.969 12.182  -6.294  1.00 26.69  ? 46  THR   A HG22 1 
ATOM   634  H HG23 . THR   A 1 66  ? 23.074 11.138  -5.868  1.00 26.69  ? 46  THR   A HG23 1 
ATOM   635  N N    . GLU   A 1 67  ? 18.772 8.971   -7.106  1.00 22.25  ? 47  GLU   A N    1 
ATOM   636  C CA   . GLU   A 1 67  ? 17.849 7.923   -7.519  1.00 23.78  ? 47  GLU   A CA   1 
ATOM   637  C C    . GLU   A 1 67  ? 18.570 6.794   -8.246  1.00 23.02  ? 47  GLU   A C    1 
ATOM   638  O O    . GLU   A 1 67  ? 18.199 5.622   -8.108  1.00 24.07  ? 47  GLU   A O    1 
ATOM   639  C CB   . GLU   A 1 67  ? 16.756 8.489   -8.421  1.00 26.75  ? 47  GLU   A CB   1 
ATOM   640  C CG   . GLU   A 1 67  ? 15.756 7.438   -8.903  1.00 30.07  ? 47  GLU   A CG   1 
ATOM   641  H H    . GLU   A 1 67  ? 18.611 9.749   -7.435  1.00 26.71  ? 47  GLU   A H    1 
ATOM   642  H HA   . GLU   A 1 67  ? 17.434 7.566   -6.719  1.00 28.53  ? 47  GLU   A HA   1 
ATOM   643  H HB2  . GLU   A 1 67  ? 16.264 9.165   -7.930  1.00 32.10  ? 47  GLU   A HB2  1 
ATOM   644  H HB3  . GLU   A 1 67  ? 17.171 8.885   -9.204  1.00 32.10  ? 47  GLU   A HB3  1 
ATOM   645  N N    . ASP   A 1 68  ? 19.598 7.133   -9.031  1.00 23.36  ? 48  ASP   A N    1 
ATOM   646  C CA   . ASP   A 1 68  ? 20.404 6.165   -9.768  1.00 24.37  ? 48  ASP   A CA   1 
ATOM   647  C C    . ASP   A 1 68  ? 21.718 5.845   -9.054  1.00 22.50  ? 48  ASP   A C    1 
ATOM   648  O O    . ASP   A 1 68  ? 22.649 5.306   -9.674  1.00 23.95  ? 48  ASP   A O    1 
ATOM   649  C CB   . ASP   A 1 68  ? 20.696 6.700   -11.173 1.00 28.56  ? 48  ASP   A CB   1 
ATOM   650  C CG   . ASP   A 1 68  ? 21.470 8.024   -11.157 1.00 33.89  ? 48  ASP   A CG   1 
ATOM   651  O OD1  . ASP   A 1 68  ? 21.681 8.617   -10.075 1.00 34.86  ? 48  ASP   A OD1  1 
ATOM   652  O OD2  . ASP   A 1 68  ? 21.860 8.482   -12.244 1.00 38.13  ? 48  ASP   A OD2  1 
ATOM   653  H H    . ASP   A 1 68  ? 19.853 7.945   -9.154  1.00 28.04  ? 48  ASP   A H    1 
ATOM   654  H HA   . ASP   A 1 68  ? 19.900 5.340   -9.851  1.00 29.25  ? 48  ASP   A HA   1 
ATOM   655  H HB2  . ASP   A 1 68  ? 21.229 6.048   -11.655 1.00 34.28  ? 48  ASP   A HB2  1 
ATOM   656  H HB3  . ASP   A 1 68  ? 19.856 6.849   -11.634 1.00 34.28  ? 48  ASP   A HB3  1 
ATOM   657  N N    . GLY   A 1 69  ? 21.791 6.135   -7.756  1.00 20.56  ? 49  GLY   A N    1 
ATOM   658  C CA   . GLY   A 1 69  ? 23.017 5.920   -7.013  1.00 20.42  ? 49  GLY   A CA   1 
ATOM   659  C C    . GLY   A 1 69  ? 23.354 4.449   -6.887  1.00 19.00  ? 49  GLY   A C    1 
ATOM   660  O O    . GLY   A 1 69  ? 22.486 3.579   -6.919  1.00 18.62  ? 49  GLY   A O    1 
ATOM   661  H H    . GLY   A 1 69  ? 21.144 6.457   -7.288  1.00 24.68  ? 49  GLY   A H    1 
ATOM   662  H HA2  . GLY   A 1 69  ? 23.751 6.365   -7.466  1.00 24.50  ? 49  GLY   A HA2  1 
ATOM   663  H HA3  . GLY   A 1 69  ? 22.924 6.291   -6.122  1.00 24.50  ? 49  GLY   A HA3  1 
ATOM   664  N N    . VAL   A 1 70  ? 24.653 4.176   -6.751  1.00 17.37  ? 50  VAL   A N    1 
ATOM   665  C CA   . VAL   A 1 70  ? 25.211 2.836   -6.655  1.00 17.34  ? 50  VAL   A CA   1 
ATOM   666  C C    . VAL   A 1 70  ? 26.000 2.721   -5.359  1.00 16.95  ? 50  VAL   A C    1 
ATOM   667  O O    . VAL   A 1 70  ? 26.738 3.633   -4.988  1.00 17.30  ? 50  VAL   A O    1 
ATOM   668  C CB   . VAL   A 1 70  ? 26.123 2.534   -7.867  1.00 19.38  ? 50  VAL   A CB   1 
ATOM   669  C CG1  . VAL   A 1 70  ? 26.730 1.150   -7.774  1.00 22.20  ? 50  VAL   A CG1  1 
ATOM   670  C CG2  . VAL   A 1 70  ? 25.383 2.685   -9.175  1.00 21.77  ? 50  VAL   A CG2  1 
ATOM   671  H H    . VAL   A 1 70  ? 25.258 4.786   -6.710  1.00 20.85  ? 50  VAL   A H    1 
ATOM   672  H HA   . VAL   A 1 70  ? 24.490 2.187   -6.628  1.00 20.81  ? 50  VAL   A HA   1 
ATOM   673  H HB   . VAL   A 1 70  ? 26.842 3.184   -7.850  1.00 23.26  ? 50  VAL   A HB   1 
ATOM   674  H HG11 . VAL   A 1 70  ? 27.163 0.938   -8.616  1.00 26.64  ? 50  VAL   A HG11 1 
ATOM   675  H HG12 . VAL   A 1 70  ? 27.382 1.139   -7.055  1.00 26.64  ? 50  VAL   A HG12 1 
ATOM   676  H HG13 . VAL   A 1 70  ? 26.027 0.508   -7.592  1.00 26.64  ? 50  VAL   A HG13 1 
ATOM   677  H HG21 . VAL   A 1 70  ? 25.991 2.492   -9.906  1.00 26.12  ? 50  VAL   A HG21 1 
ATOM   678  H HG22 . VAL   A 1 70  ? 24.639 2.063   -9.191  1.00 26.12  ? 50  VAL   A HG22 1 
ATOM   679  H HG23 . VAL   A 1 70  ? 25.056 3.595   -9.249  1.00 26.12  ? 50  VAL   A HG23 1 
ATOM   680  N N    . GLY   A 1 71  ? 25.882 1.564   -4.695  1.00 16.07  ? 51  GLY   A N    1 
ATOM   681  C CA   . GLY   A 1 71  ? 26.705 1.249   -3.550  1.00 15.70  ? 51  GLY   A CA   1 
ATOM   682  C C    . GLY   A 1 71  ? 27.132 -0.206  -3.615  1.00 17.36  ? 51  GLY   A C    1 
ATOM   683  O O    . GLY   A 1 71  ? 26.620 -0.963  -4.413  1.00 20.45  ? 51  GLY   A O    1 
ATOM   684  H H    . GLY   A 1 71  ? 25.322 0.945   -4.900  1.00 19.29  ? 51  GLY   A H    1 
ATOM   685  H HA2  . GLY   A 1 71  ? 27.496 1.811   -3.544  1.00 18.84  ? 51  GLY   A HA2  1 
ATOM   686  H HA3  . GLY   A 1 71  ? 26.206 1.397   -2.731  1.00 18.84  ? 51  GLY   A HA3  1 
ATOM   687  N N    . GLY   A 1 72  ? 28.066 -0.591  -2.769  1.00 16.17  ? 52  GLY   A N    1 
ATOM   688  C CA   . GLY   A 1 72  ? 28.354 -2.002  -2.641  1.00 16.84  ? 52  GLY   A CA   1 
ATOM   689  C C    . GLY   A 1 72  ? 29.811 -2.269  -2.338  1.00 15.43  ? 52  GLY   A C    1 
ATOM   690  O O    . GLY   A 1 72  ? 30.555 -1.397  -1.898  1.00 16.28  ? 52  GLY   A O    1 
ATOM   691  H H    . GLY   A 1 72  ? 28.534 -0.068  -2.272  1.00 19.41  ? 52  GLY   A H    1 
ATOM   692  H HA2  . GLY   A 1 72  ? 27.820 -2.375  -1.923  1.00 20.21  ? 52  GLY   A HA2  1 
ATOM   693  H HA3  . GLY   A 1 72  ? 28.128 -2.452  -3.470  1.00 20.21  ? 52  GLY   A HA3  1 
ATOM   694  N N    . LEU   A 1 73  ? 30.177 -3.524  -2.582  1.00 15.37  ? 53  LEU   A N    1 
ATOM   695  C CA   . LEU   A 1 73  ? 31.423 -4.106  -2.108  1.00 15.99  ? 53  LEU   A CA   1 
ATOM   696  C C    . LEU   A 1 73  ? 32.328 -4.373  -3.315  1.00 15.21  ? 53  LEU   A C    1 
ATOM   697  O O    . LEU   A 1 73  ? 31.996 -5.163  -4.200  1.00 16.37  ? 53  LEU   A O    1 
ATOM   698  C CB   . LEU   A 1 73  ? 31.109 -5.385  -1.336  1.00 15.46  ? 53  LEU   A CB   1 
ATOM   699  C CG   . LEU   A 1 73  ? 32.367 -6.124  -0.890  1.00 16.29  ? 53  LEU   A CG   1 
ATOM   700  C CD1  . LEU   A 1 73  ? 33.237 -5.288  0.056   1.00 15.97  ? 53  LEU   A CD1  1 
ATOM   701  C CD2  . LEU   A 1 73  ? 31.925 -7.446  -0.227  1.00 17.23  ? 53  LEU   A CD2  1 
ATOM   702  H H    . LEU   A 1 73  ? 29.700 -4.076  -3.037  1.00 18.44  ? 53  LEU   A H    1 
ATOM   703  H HA   . LEU   A 1 73  ? 31.901 -3.498  -1.523  1.00 19.19  ? 53  LEU   A HA   1 
ATOM   704  H HB2  . LEU   A 1 73  ? 30.596 -5.158  -0.545  1.00 18.55  ? 53  LEU   A HB2  1 
ATOM   705  H HB3  . LEU   A 1 73  ? 30.596 -5.979  -1.905  1.00 18.55  ? 53  LEU   A HB3  1 
ATOM   706  H HG   . LEU   A 1 73  ? 32.931 -6.306  -1.658  1.00 19.55  ? 53  LEU   A HG   1 
ATOM   707  H HD11 . LEU   A 1 73  ? 34.001 -5.818  0.333   1.00 19.17  ? 53  LEU   A HD11 1 
ATOM   708  H HD12 . LEU   A 1 73  ? 33.537 -4.493  -0.411  1.00 19.17  ? 53  LEU   A HD12 1 
ATOM   709  H HD13 . LEU   A 1 73  ? 32.710 -5.038  0.831   1.00 19.17  ? 53  LEU   A HD13 1 
ATOM   710  H HD21 . LEU   A 1 73  ? 32.713 -7.961  0.007   1.00 20.68  ? 53  LEU   A HD21 1 
ATOM   711  H HD22 . LEU   A 1 73  ? 31.413 -7.243  0.571   1.00 20.68  ? 53  LEU   A HD22 1 
ATOM   712  H HD23 . LEU   A 1 73  ? 31.378 -7.946  -0.853  1.00 20.68  ? 53  LEU   A HD23 1 
ATOM   713  N N    . TRP   A 1 74  ? 33.487 -3.716  -3.354  1.00 15.67  ? 54  TRP   A N    1 
ATOM   714  C CA   . TRP   A 1 74  ? 34.331 -3.792  -4.531  1.00 16.35  ? 54  TRP   A CA   1 
ATOM   715  C C    . TRP   A 1 74  ? 35.384 -4.893  -4.444  1.00 17.52  ? 54  TRP   A C    1 
ATOM   716  O O    . TRP   A 1 74  ? 36.048 -5.168  -5.445  1.00 23.02  ? 54  TRP   A O    1 
ATOM   717  C CB   . TRP   A 1 74  ? 34.983 -2.425  -4.795  1.00 16.56  ? 54  TRP   A CB   1 
ATOM   718  C CG   . TRP   A 1 74  ? 34.363 -1.730  -5.970  1.00 16.31  ? 54  TRP   A CG   1 
ATOM   719  C CD1  . TRP   A 1 74  ? 34.958 -1.419  -7.151  1.00 18.48  ? 54  TRP   A CD1  1 
ATOM   720  C CD2  . TRP   A 1 74  ? 32.985 -1.321  -6.107  1.00 16.42  ? 54  TRP   A CD2  1 
ATOM   721  N NE1  . TRP   A 1 74  ? 34.067 -0.835  -8.010  1.00 21.22  ? 54  TRP   A NE1  1 
ATOM   722  C CE2  . TRP   A 1 74  ? 32.846 -0.751  -7.395  1.00 19.50  ? 54  TRP   A CE2  1 
ATOM   723  C CE3  . TRP   A 1 74  ? 31.860 -1.374  -5.261  1.00 17.17  ? 54  TRP   A CE3  1 
ATOM   724  C CZ2  . TRP   A 1 74  ? 31.631 -0.250  -7.857  1.00 21.24  ? 54  TRP   A CZ2  1 
ATOM   725  C CZ3  . TRP   A 1 74  ? 30.655 -0.861  -5.726  1.00 18.19  ? 54  TRP   A CZ3  1 
ATOM   726  C CH2  . TRP   A 1 74  ? 30.554 -0.326  -7.020  1.00 19.22  ? 54  TRP   A CH2  1 
ATOM   727  H H    . TRP   A 1 74  ? 33.796 -3.227  -2.717  1.00 18.81  ? 54  TRP   A H    1 
ATOM   728  H HA   . TRP   A 1 74  ? 33.784 -3.997  -5.306  1.00 19.62  ? 54  TRP   A HA   1 
ATOM   729  H HB2  . TRP   A 1 74  ? 34.870 -1.861  -4.014  1.00 19.87  ? 54  TRP   A HB2  1 
ATOM   730  H HB3  . TRP   A 1 74  ? 35.927 -2.551  -4.980  1.00 19.87  ? 54  TRP   A HB3  1 
ATOM   731  H HD1  . TRP   A 1 74  ? 35.852 -1.581  -7.350  1.00 22.18  ? 54  TRP   A HD1  1 
ATOM   732  H HE1  . TRP   A 1 74  ? 34.245 -0.565  -8.806  1.00 25.46  ? 54  TRP   A HE1  1 
ATOM   733  H HE3  . TRP   A 1 74  ? 31.922 -1.744  -4.410  1.00 20.61  ? 54  TRP   A HE3  1 
ATOM   734  H HZ2  . TRP   A 1 74  ? 31.556 0.124   -8.705  1.00 25.49  ? 54  TRP   A HZ2  1 
ATOM   735  H HZ3  . TRP   A 1 74  ? 29.907 -0.873  -5.174  1.00 21.84  ? 54  TRP   A HZ3  1 
ATOM   736  H HH2  . TRP   A 1 74  ? 29.729 -0.014  -7.316  1.00 23.06  ? 54  TRP   A HH2  1 
ATOM   737  N N    . THR   A 1 75  ? 35.551 -5.521  -3.290  1.00 15.36  ? 55  THR   A N    1 
ATOM   738  C CA   . THR   A 1 75  ? 36.594 -6.510  -3.060  1.00 14.61  ? 55  THR   A CA   1 
ATOM   739  C C    . THR   A 1 75  ? 35.919 -7.795  -2.607  1.00 15.02  ? 55  THR   A C    1 
ATOM   740  O O    . THR   A 1 75  ? 35.467 -7.886  -1.463  1.00 16.29  ? 55  THR   A O    1 
ATOM   741  C CB   . THR   A 1 75  ? 37.540 -6.001  -1.989  1.00 15.43  ? 55  THR   A CB   1 
ATOM   742  O OG1  . THR   A 1 75  ? 36.800 -5.518  -0.868  1.00 15.20  ? 55  THR   A OG1  1 
ATOM   743  C CG2  . THR   A 1 75  ? 38.436 -4.859  -2.491  1.00 16.52  ? 55  THR   A CG2  1 
ATOM   744  H H    . THR   A 1 75  ? 35.056 -5.386  -2.601  1.00 18.43  ? 55  THR   A H    1 
ATOM   745  H HA   . THR   A 1 75  ? 37.088 -6.687  -3.876  1.00 17.53  ? 55  THR   A HA   1 
ATOM   746  H HB   . THR   A 1 75  ? 38.110 -6.742  -1.731  1.00 18.52  ? 55  THR   A HB   1 
ATOM   747  H HG1  . THR   A 1 75  ? 36.337 -6.138  -0.541  1.00 18.24  ? 55  THR   A HG1  1 
ATOM   748  H HG21 . THR   A 1 75  ? 39.061 -4.597  -1.796  1.00 19.83  ? 55  THR   A HG21 1 
ATOM   749  H HG22 . THR   A 1 75  ? 38.936 -5.147  -3.271  1.00 19.83  ? 55  THR   A HG22 1 
ATOM   750  H HG23 . THR   A 1 75  ? 37.893 -4.092  -2.731  1.00 19.83  ? 55  THR   A HG23 1 
ATOM   751  N N    . THR   A 1 76  ? 35.881 -8.791  -3.483  1.00 16.74  ? 56  THR   A N    1 
ATOM   752  C CA   . THR   A 1 76  ? 35.249 -10.070 -3.167  1.00 17.33  ? 56  THR   A CA   1 
ATOM   753  C C    . THR   A 1 76  ? 36.137 -11.206 -3.646  1.00 17.58  ? 56  THR   A C    1 
ATOM   754  O O    . THR   A 1 76  ? 37.135 -10.999 -4.330  1.00 18.74  ? 56  THR   A O    1 
ATOM   755  C CB   . THR   A 1 76  ? 33.873 -10.206 -3.836  1.00 22.03  ? 56  THR   A CB   1 
ATOM   756  O OG1  . THR   A 1 76  ? 34.043 -10.401 -5.242  1.00 26.96  ? 56  THR   A OG1  1 
ATOM   757  C CG2  . THR   A 1 76  ? 33.023 -8.957  -3.626  1.00 25.47  ? 56  THR   A CG2  1 
ATOM   758  H H    . THR   A 1 76  ? 36.216 -8.752  -4.274  1.00 20.09  ? 56  THR   A H    1 
ATOM   759  H HA   . THR   A 1 76  ? 35.148 -10.125 -2.204  1.00 20.79  ? 56  THR   A HA   1 
ATOM   760  H HB   . THR   A 1 76  ? 33.411 -10.961 -3.439  1.00 26.44  ? 56  THR   A HB   1 
ATOM   761  H HG1  . THR   A 1 76  ? 34.485 -9.765  -5.569  1.00 32.36  ? 56  THR   A HG1  1 
ATOM   762  H HG21 . THR   A 1 76  ? 32.144 -9.084  -4.017  1.00 30.56  ? 56  THR   A HG21 1 
ATOM   763  H HG22 . THR   A 1 76  ? 32.922 -8.779  -2.678  1.00 30.56  ? 56  THR   A HG22 1 
ATOM   764  H HG23 . THR   A 1 76  ? 33.447 -8.192  -4.046  1.00 30.56  ? 56  THR   A HG23 1 
ATOM   765  N N    . ASP   A 1 77  ? 35.730 -12.437 -3.327  1.00 17.14  ? 57  ASP   A N    1 
ATOM   766  C CA   . ASP   A 1 77  ? 36.526 -13.603 -3.707  1.00 19.38  ? 57  ASP   A CA   1 
ATOM   767  C C    . ASP   A 1 77  ? 36.628 -13.762 -5.213  1.00 21.53  ? 57  ASP   A C    1 
ATOM   768  O O    . ASP   A 1 77  ? 37.641 -14.264 -5.699  1.00 23.91  ? 57  ASP   A O    1 
ATOM   769  C CB   . ASP   A 1 77  ? 35.990 -14.894 -3.070  1.00 20.36  ? 57  ASP   A CB   1 
ATOM   770  C CG   . ASP   A 1 77  ? 34.652 -15.289 -3.555  1.00 25.83  ? 57  ASP   A CG   1 
ATOM   771  O OD1  . ASP   A 1 77  ? 34.532 -15.952 -4.588  1.00 31.96  ? 57  ASP   A OD1  1 
ATOM   772  O OD2  . ASP   A 1 77  ? 33.735 -14.991 -2.852  1.00 29.00  ? 57  ASP   A OD2  1 
ATOM   773  H H    . ASP   A 1 77  ? 35.008 -12.621 -2.898  1.00 20.57  ? 57  ASP   A H    1 
ATOM   774  H HA   . ASP   A 1 77  ? 37.420 -13.463 -3.356  1.00 23.26  ? 57  ASP   A HA   1 
ATOM   775  H HB2  . ASP   A 1 77  ? 36.603 -15.619 -3.271  1.00 24.44  ? 57  ASP   A HB2  1 
ATOM   776  H HB3  . ASP   A 1 77  ? 35.931 -14.767 -2.110  1.00 24.44  ? 57  ASP   A HB3  1 
ATOM   777  N N    . SER   A 1 78  ? 35.613 -13.334 -5.967  1.00 22.67  ? 58  SER   A N    1 
ATOM   778  C CA   . SER   A 1 78  ? 35.618 -13.544 -7.399  1.00 25.32  ? 58  SER   A CA   1 
ATOM   779  C C    . SER   A 1 78  ? 36.451 -12.519 -8.142  1.00 28.28  ? 58  SER   A C    1 
ATOM   780  O O    . SER   A 1 78  ? 36.801 -12.754 -9.301  1.00 32.51  ? 58  SER   A O    1 
ATOM   781  C CB   . SER   A 1 78  ? 34.189 -13.466 -7.920  1.00 29.66  ? 58  SER   A CB   1 
ATOM   782  O OG   . SER   A 1 78  ? 33.725 -12.157 -7.772  1.00 31.85  ? 58  SER   A OG   1 
ATOM   783  H H    . SER   A 1 78  ? 34.919 -12.922 -5.668  1.00 27.20  ? 58  SER   A H    1 
ATOM   784  H HA   . SER   A 1 78  ? 35.984 -14.424 -7.581  1.00 30.39  ? 58  SER   A HA   1 
ATOM   785  H HB2  . SER   A 1 78  ? 34.173 -13.711 -8.858  1.00 35.60  ? 58  SER   A HB2  1 
ATOM   786  H HB3  . SER   A 1 78  ? 33.625 -14.069 -7.410  1.00 35.60  ? 58  SER   A HB3  1 
ATOM   787  H HG   . SER   A 1 78  ? 32.937 -12.098 -8.057  1.00 38.22  ? 58  SER   A HG   1 
ATOM   788  N N    . GLY   A 1 79  ? 36.760 -11.393 -7.523  1.00 26.77  ? 59  GLY   A N    1 
ATOM   789  C CA   . GLY   A 1 79  ? 37.434 -10.315 -8.212  1.00 27.60  ? 59  GLY   A CA   1 
ATOM   790  C C    . GLY   A 1 79  ? 36.529 -9.322  -8.912  1.00 29.67  ? 59  GLY   A C    1 
ATOM   791  O O    . GLY   A 1 79  ? 37.042 -8.348  -9.485  1.00 32.80  ? 59  GLY   A O    1 
ATOM   792  H H    . GLY   A 1 79  ? 36.588 -11.230 -6.696  1.00 32.13  ? 59  GLY   A H    1 
ATOM   793  H HA2  . GLY   A 1 79  ? 37.967 -9.823  -7.568  1.00 33.12  ? 59  GLY   A HA2  1 
ATOM   794  H HA3  . GLY   A 1 79  ? 38.022 -10.698 -8.882  1.00 33.12  ? 59  GLY   A HA3  1 
ATOM   795  N N    . GLN   A 1 80  ? 35.194 -9.528  -8.887  1.00 27.62  ? 60  GLN   A N    1 
ATOM   796  C CA   . GLN   A 1 80  ? 34.238 -8.577  -9.439  1.00 29.27  ? 60  GLN   A CA   1 
ATOM   797  C C    . GLN   A 1 80  ? 33.479 -7.868  -8.322  1.00 25.77  ? 60  GLN   A C    1 
ATOM   798  O O    . GLN   A 1 80  ? 33.172 -8.484  -7.291  1.00 26.99  ? 60  GLN   A O    1 
ATOM   799  C CB   . GLN   A 1 80  ? 33.221 -9.313  -10.328 1.00 34.37  ? 60  GLN   A CB   1 
ATOM   800  C CG   . GLN   A 1 80  ? 33.860 -10.008 -11.513 1.00 41.64  ? 60  GLN   A CG   1 
ATOM   801  C CD   . GLN   A 1 80  ? 34.625 -9.047  -12.420 1.00 46.73  ? 60  GLN   A CD   1 
ATOM   802  O OE1  . GLN   A 1 80  ? 35.756 -9.332  -12.824 1.00 49.38  ? 60  GLN   A OE1  1 
ATOM   803  N NE2  . GLN   A 1 80  ? 34.002 -7.909  -12.755 1.00 48.43  ? 60  GLN   A NE2  1 
ATOM   804  H H    . GLN   A 1 80  ? 34.824 -10.226 -8.547  1.00 33.14  ? 60  GLN   A H    1 
ATOM   805  H HA   . GLN   A 1 80  ? 34.705 -7.910  -9.966  1.00 35.13  ? 60  GLN   A HA   1 
ATOM   806  H HB2  . GLN   A 1 80  ? 32.767 -9.985  -9.796  1.00 41.25  ? 60  GLN   A HB2  1 
ATOM   807  H HB3  . GLN   A 1 80  ? 32.579 -8.671  -10.669 1.00 41.25  ? 60  GLN   A HB3  1 
ATOM   808  H HG2  . GLN   A 1 80  ? 34.485 -10.676 -11.188 1.00 49.98  ? 60  GLN   A HG2  1 
ATOM   809  H HG3  . GLN   A 1 80  ? 33.167 -10.433 -12.042 1.00 49.98  ? 60  GLN   A HG3  1 
ATOM   810  H HE21 . GLN   A 1 80  ? 33.210 -7.750  -12.461 1.00 58.12  ? 60  GLN   A HE21 1 
ATOM   811  H HE22 . GLN   A 1 80  ? 34.395 -7.338  -13.264 1.00 58.12  ? 60  GLN   A HE22 1 
ATOM   812  N N    . PRO   A 1 81  ? 33.160 -6.584  -8.473  1.00 23.75  ? 61  PRO   A N    1 
ATOM   813  C CA   . PRO   A 1 81  ? 32.361 -5.906  -7.439  1.00 20.84  ? 61  PRO   A CA   1 
ATOM   814  C C    . PRO   A 1 81  ? 30.953 -6.459  -7.357  1.00 21.13  ? 61  PRO   A C    1 
ATOM   815  O O    . PRO   A 1 81  ? 30.393 -6.956  -8.334  1.00 24.88  ? 61  PRO   A O    1 
ATOM   816  C CB   . PRO   A 1 81  ? 32.303 -4.451  -7.926  1.00 23.20  ? 61  PRO   A CB   1 
ATOM   817  C CG   . PRO   A 1 81  ? 33.493 -4.285  -8.844  1.00 27.31  ? 61  PRO   A CG   1 
ATOM   818  C CD   . PRO   A 1 81  ? 33.614 -5.650  -9.518  1.00 27.47  ? 61  PRO   A CD   1 
ATOM   819  H HA   . PRO   A 1 81  ? 32.808 -5.973  -6.581  1.00 25.02  ? 61  PRO   A HA   1 
ATOM   820  H HB2  . PRO   A 1 81  ? 31.473 -4.298  -8.405  1.00 27.84  ? 61  PRO   A HB2  1 
ATOM   821  H HB3  . PRO   A 1 81  ? 32.365 -3.849  -7.168  1.00 27.84  ? 61  PRO   A HB3  1 
ATOM   822  H HG2  . PRO   A 1 81  ? 33.322 -3.585  -9.494  1.00 32.77  ? 61  PRO   A HG2  1 
ATOM   823  H HG3  . PRO   A 1 81  ? 34.288 -4.073  -8.331  1.00 32.77  ? 61  PRO   A HG3  1 
ATOM   824  H HD2  . PRO   A 1 81  ? 33.041 -5.701  -10.299 1.00 32.96  ? 61  PRO   A HD2  1 
ATOM   825  H HD3  . PRO   A 1 81  ? 34.533 -5.832  -9.768  1.00 32.96  ? 61  PRO   A HD3  1 
ATOM   826  N N    . ILE   A 1 82  ? 30.378 -6.344  -6.169  1.00 18.46  ? 62  ILE   A N    1 
ATOM   827  C CA   . ILE   A 1 82  ? 28.957 -6.595  -5.952  1.00 19.66  ? 62  ILE   A CA   1 
ATOM   828  C C    . ILE   A 1 82  ? 28.328 -5.216  -5.795  1.00 18.05  ? 62  ILE   A C    1 
ATOM   829  O O    . ILE   A 1 82  ? 28.397 -4.588  -4.718  1.00 19.02  ? 62  ILE   A O    1 
ATOM   830  C CB   . ILE   A 1 82  ? 28.726 -7.493  -4.746  1.00 24.35  ? 62  ILE   A CB   1 
ATOM   831  C CG1  . ILE   A 1 82  ? 29.427 -8.845  -5.027  1.00 28.66  ? 62  ILE   A CG1  1 
ATOM   832  C CG2  . ILE   A 1 82  ? 27.201 -7.660  -4.510  1.00 25.82  ? 62  ILE   A CG2  1 
ATOM   833  C CD1  . ILE   A 1 82  ? 29.457 -9.850  -3.909  1.00 34.76  ? 62  ILE   A CD1  1 
ATOM   834  H H    . ILE   A 1 82  ? 30.799 -6.117  -5.455  1.00 22.15  ? 62  ILE   A H    1 
ATOM   835  H HA   . ILE   A 1 82  ? 28.560 -7.035  -6.719  1.00 23.60  ? 62  ILE   A HA   1 
ATOM   836  H HB   . ILE   A 1 82  ? 29.100 -7.107  -3.938  1.00 29.22  ? 62  ILE   A HB   1 
ATOM   837  H HG12 . ILE   A 1 82  ? 28.971 -9.268  -5.772  1.00 34.39  ? 62  ILE   A HG12 1 
ATOM   838  H HG13 . ILE   A 1 82  ? 30.349 -8.660  -5.263  1.00 34.39  ? 62  ILE   A HG13 1 
ATOM   839  H HG21 . ILE   A 1 82  ? 27.061 -8.255  -3.757  1.00 30.98  ? 62  ILE   A HG21 1 
ATOM   840  H HG22 . ILE   A 1 82  ? 26.813 -6.791  -4.322  1.00 30.98  ? 62  ILE   A HG22 1 
ATOM   841  H HG23 . ILE   A 1 82  ? 26.797 -8.036  -5.308  1.00 30.98  ? 62  ILE   A HG23 1 
ATOM   842  H HD11 . ILE   A 1 82  ? 30.333 -10.266 -3.883  1.00 41.72  ? 62  ILE   A HD11 1 
ATOM   843  H HD12 . ILE   A 1 82  ? 29.282 -9.395  -3.071  1.00 41.72  ? 62  ILE   A HD12 1 
ATOM   844  H HD13 . ILE   A 1 82  ? 28.776 -10.521 -4.070  1.00 41.72  ? 62  ILE   A HD13 1 
ATOM   845  N N    . ALA   A 1 83  ? 27.785 -4.712  -6.898  1.00 19.75  ? 63  ALA   A N    1 
ATOM   846  C CA   . ALA   A 1 83  ? 27.231 -3.371  -6.977  1.00 20.56  ? 63  ALA   A CA   1 
ATOM   847  C C    . ALA   A 1 83  ? 25.714 -3.450  -6.900  1.00 20.58  ? 63  ALA   A C    1 
ATOM   848  O O    . ALA   A 1 83  ? 25.086 -4.250  -7.594  1.00 24.50  ? 63  ALA   A O    1 
ATOM   849  C CB   . ALA   A 1 83  ? 27.622 -2.703  -8.294  1.00 22.97  ? 63  ALA   A CB   1 
ATOM   850  H H    . ALA   A 1 83  ? 27.725 -5.146  -7.638  1.00 23.70  ? 63  ALA   A H    1 
ATOM   851  H HA   . ALA   A 1 83  ? 27.567 -2.840  -6.238  1.00 24.68  ? 63  ALA   A HA   1 
ATOM   852  H HB1  . ALA   A 1 83  ? 27.252 -1.806  -8.316  1.00 27.56  ? 63  ALA   A HB1  1 
ATOM   853  H HB2  . ALA   A 1 83  ? 28.589 -2.663  -8.354  1.00 27.56  ? 63  ALA   A HB2  1 
ATOM   854  H HB3  . ALA   A 1 83  ? 27.266 -3.225  -9.031  1.00 27.56  ? 63  ALA   A HB3  1 
ATOM   855  N N    . ILE   A 1 84  ? 25.152 -2.626  -6.042  1.00 18.22  ? 64  ILE   A N    1 
ATOM   856  C CA   . ILE   A 1 84  ? 23.716 -2.514  -5.864  1.00 19.52  ? 64  ILE   A CA   1 
ATOM   857  C C    . ILE   A 1 84  ? 23.314 -1.218  -6.539  1.00 19.37  ? 64  ILE   A C    1 
ATOM   858  O O    . ILE   A 1 84  ? 23.733 -0.138  -6.110  1.00 19.49  ? 64  ILE   A O    1 
ATOM   859  C CB   . ILE   A 1 84  ? 23.358 -2.529  -4.373  1.00 21.74  ? 64  ILE   A CB   1 
ATOM   860  C CG1  . ILE   A 1 84  ? 23.961 -3.784  -3.710  1.00 26.07  ? 64  ILE   A CG1  1 
ATOM   861  C CG2  . ILE   A 1 84  ? 21.865 -2.496  -4.199  1.00 22.87  ? 64  ILE   A CG2  1 
ATOM   862  C CD1  . ILE   A 1 84  ? 24.347 -3.592  -2.313  1.00 30.90  ? 64  ILE   A CD1  1 
ATOM   863  H H    . ILE   A 1 84  ? 25.598 -2.098  -5.529  1.00 21.87  ? 64  ILE   A H    1 
ATOM   864  H HA   . ILE   A 1 84  ? 23.240 -3.246  -6.286  1.00 23.42  ? 64  ILE   A HA   1 
ATOM   865  H HB   . ILE   A 1 84  ? 23.731 -1.742  -3.945  1.00 26.09  ? 64  ILE   A HB   1 
ATOM   866  H HG12 . ILE   A 1 84  ? 23.305 -4.497  -3.740  1.00 31.29  ? 64  ILE   A HG12 1 
ATOM   867  H HG13 . ILE   A 1 84  ? 24.756 -4.044  -4.202  1.00 31.29  ? 64  ILE   A HG13 1 
ATOM   868  H HG21 . ILE   A 1 84  ? 21.654 -2.598  -3.258  1.00 27.45  ? 64  ILE   A HG21 1 
ATOM   869  H HG22 . ILE   A 1 84  ? 21.528 -1.646  -4.523  1.00 27.45  ? 64  ILE   A HG22 1 
ATOM   870  H HG23 . ILE   A 1 84  ? 21.472 -3.223  -4.707  1.00 27.45  ? 64  ILE   A HG23 1 
ATOM   871  H HD11 . ILE   A 1 84  ? 24.597 -4.449  -1.934  1.00 37.08  ? 64  ILE   A HD11 1 
ATOM   872  H HD12 . ILE   A 1 84  ? 25.098 -2.981  -2.274  1.00 37.08  ? 64  ILE   A HD12 1 
ATOM   873  H HD13 . ILE   A 1 84  ? 23.594 -3.223  -1.826  1.00 37.08  ? 64  ILE   A HD13 1 
ATOM   874  N N    . ARG   A 1 85  ? 22.479 -1.312  -7.570  1.00 22.16  ? 65  ARG   A N    1 
ATOM   875  C CA   . ARG   A 1 85  ? 22.276 -0.224  -8.516  1.00 23.12  ? 65  ARG   A CA   1 
ATOM   876  C C    . ARG   A 1 85  ? 20.890 0.379   -8.349  1.00 23.21  ? 65  ARG   A C    1 
ATOM   877  O O    . ARG   A 1 85  ? 19.877 -0.263  -8.647  1.00 25.40  ? 65  ARG   A O    1 
ATOM   878  C CB   . ARG   A 1 85  ? 22.489 -0.722  -9.939  1.00 25.11  ? 65  ARG   A CB   1 
ATOM   879  C CG   . ARG   A 1 85  ? 23.903 -1.190  -10.163 1.00 27.80  ? 65  ARG   A CG   1 
ATOM   880  C CD   . ARG   A 1 85  ? 24.152 -1.643  -11.612 1.00 31.81  ? 65  ARG   A CD   1 
ATOM   881  N NE   . ARG   A 1 85  ? 25.480 -2.226  -11.756 1.00 36.24  ? 65  ARG   A NE   1 
ATOM   882  C CZ   . ARG   A 1 85  ? 26.603 -1.530  -11.900 1.00 40.48  ? 65  ARG   A CZ   1 
ATOM   883  N NH1  . ARG   A 1 85  ? 26.593 -0.204  -11.993 1.00 41.24  ? 65  ARG   A NH1  1 
ATOM   884  N NH2  . ARG   A 1 85  ? 27.768 -2.182  -11.955 1.00 43.09  ? 65  ARG   A NH2  1 
ATOM   885  H H    . ARG   A 1 85  ? 22.010 -2.011  -7.744  1.00 26.59  ? 65  ARG   A H    1 
ATOM   886  H HA   . ARG   A 1 85  ? 22.913 0.479   -8.315  1.00 27.74  ? 65  ARG   A HA   1 
ATOM   887  H HB2  . ARG   A 1 85  ? 21.891 -1.467  -10.109 1.00 30.13  ? 65  ARG   A HB2  1 
ATOM   888  H HB3  . ARG   A 1 85  ? 22.305 -0.001  -10.561 1.00 30.13  ? 65  ARG   A HB3  1 
ATOM   889  H HG2  . ARG   A 1 85  ? 24.513 -0.462  -9.967  1.00 33.36  ? 65  ARG   A HG2  1 
ATOM   890  H HG3  . ARG   A 1 85  ? 24.085 -1.942  -9.578  1.00 33.36  ? 65  ARG   A HG3  1 
ATOM   891  H HD2  . ARG   A 1 85  ? 23.495 -2.312  -11.859 1.00 38.18  ? 65  ARG   A HD2  1 
ATOM   892  H HD3  . ARG   A 1 85  ? 24.086 -0.879  -12.205 1.00 38.18  ? 65  ARG   A HD3  1 
ATOM   893  H HE   . ARG   A 1 85  ? 25.541 -3.083  -11.747 1.00 43.50  ? 65  ARG   A HE   1 
ATOM   894  H HH11 . ARG   A 1 85  ? 25.848 0.224   -11.961 1.00 49.49  ? 65  ARG   A HH11 1 
ATOM   895  H HH12 . ARG   A 1 85  ? 27.332 0.226   -12.086 1.00 49.49  ? 65  ARG   A HH12 1 
ATOM   896  H HH21 . ARG   A 1 85  ? 27.783 -3.040  -11.898 1.00 51.71  ? 65  ARG   A HH21 1 
ATOM   897  H HH22 . ARG   A 1 85  ? 28.502 -1.744  -12.048 1.00 51.71  ? 65  ARG   A HH22 1 
ATOM   898  N N    . GLY   A 1 86  ? 20.857 1.619   -7.902  1.00 21.88  ? 66  GLY   A N    1 
ATOM   899  C CA   . GLY   A 1 86  ? 19.609 2.342   -7.798  1.00 22.55  ? 66  GLY   A CA   1 
ATOM   900  C C    . GLY   A 1 86  ? 19.209 2.498   -6.350  1.00 21.68  ? 66  GLY   A C    1 
ATOM   901  O O    . GLY   A 1 86  ? 19.346 1.574   -5.533  1.00 20.77  ? 66  GLY   A O    1 
ATOM   902  H H    . GLY   A 1 86  ? 21.548 2.066   -7.652  1.00 26.26  ? 66  GLY   A H    1 
ATOM   903  H HA2  . GLY   A 1 86  ? 19.705 3.222   -8.193  1.00 27.06  ? 66  GLY   A HA2  1 
ATOM   904  H HA3  . GLY   A 1 86  ? 18.909 1.860   -8.266  1.00 27.06  ? 66  GLY   A HA3  1 
ATOM   905  N N    . ARG   A 1 87  ? 18.687 3.685   -6.031  1.00 22.06  ? 67  ARG   A N    1 
ATOM   906  C CA   . ARG   A 1 87  ? 18.261 3.968   -4.669  1.00 21.82  ? 67  ARG   A CA   1 
ATOM   907  C C    . ARG   A 1 87  ? 17.250 2.945   -4.184  1.00 21.85  ? 67  ARG   A C    1 
ATOM   908  O O    . ARG   A 1 87  ? 17.310 2.512   -3.026  1.00 22.53  ? 67  ARG   A O    1 
ATOM   909  C CB   . ARG   A 1 87  ? 17.707 5.398   -4.583  1.00 22.34  ? 67  ARG   A CB   1 
ATOM   910  C CG   . ARG   A 1 87  ? 17.173 5.802   -3.208  1.00 23.87  ? 67  ARG   A CG   1 
ATOM   911  C CD   . ARG   A 1 87  ? 16.814 7.283   -3.203  1.00 28.76  ? 67  ARG   A CD   1 
ATOM   912  N NE   . ARG   A 1 87  ? 15.790 7.525   -4.194  1.00 35.64  ? 67  ARG   A NE   1 
ATOM   913  C CZ   . ARG   A 1 87  ? 15.523 8.717   -4.708  1.00 41.64  ? 67  ARG   A CZ   1 
ATOM   914  N NH1  . ARG   A 1 87  ? 16.238 9.780   -4.380  1.00 42.19  ? 67  ARG   A NH1  1 
ATOM   915  N NH2  . ARG   A 1 87  ? 14.540 8.833   -5.595  1.00 44.90  ? 67  ARG   A NH2  1 
ATOM   916  H H    . ARG   A 1 87  ? 18.571 4.334   -6.583  1.00 26.47  ? 67  ARG   A H    1 
ATOM   917  H HA   . ARG   A 1 87  ? 19.027 3.916   -4.077  1.00 26.19  ? 67  ARG   A HA   1 
ATOM   918  H HB2  . ARG   A 1 87  ? 18.418 6.017   -4.812  1.00 26.81  ? 67  ARG   A HB2  1 
ATOM   919  H HB3  . ARG   A 1 87  ? 16.976 5.483   -5.215  1.00 26.81  ? 67  ARG   A HB3  1 
ATOM   920  H HG2  . ARG   A 1 87  ? 16.377 5.288   -3.002  1.00 28.65  ? 67  ARG   A HG2  1 
ATOM   921  H HG3  . ARG   A 1 87  ? 17.853 5.645   -2.534  1.00 28.65  ? 67  ARG   A HG3  1 
ATOM   922  H HD2  . ARG   A 1 87  ? 16.475 7.537   -2.331  1.00 34.51  ? 67  ARG   A HD2  1 
ATOM   923  H HD3  . ARG   A 1 87  ? 17.596 7.813   -3.422  1.00 34.51  ? 67  ARG   A HD3  1 
ATOM   924  H HE   . ARG   A 1 87  ? 15.326 6.855   -4.466  1.00 42.77  ? 67  ARG   A HE   1 
ATOM   925  H HH11 . ARG   A 1 87  ? 16.889 9.705   -3.823  1.00 50.63  ? 67  ARG   A HH11 1 
ATOM   926  H HH12 . ARG   A 1 87  ? 16.051 10.546  -4.723  1.00 50.63  ? 67  ARG   A HH12 1 
ATOM   927  H HH21 . ARG   A 1 87  ? 14.086 8.140   -5.827  1.00 53.88  ? 67  ARG   A HH21 1 
ATOM   928  H HH22 . ARG   A 1 87  ? 14.357 9.601   -5.936  1.00 53.88  ? 67  ARG   A HH22 1 
ATOM   929  N N    . GLU   A 1 88  ? 16.314 2.544   -5.050  1.00 25.77  ? 68  GLU   A N    1 
ATOM   930  C CA   . GLU   A 1 88  ? 15.309 1.570   -4.646  1.00 27.61  ? 68  GLU   A CA   1 
ATOM   931  C C    . GLU   A 1 88  ? 15.932 0.224   -4.292  1.00 26.66  ? 68  GLU   A C    1 
ATOM   932  O O    . GLU   A 1 88  ? 15.600 -0.371  -3.257  1.00 26.83  ? 68  GLU   A O    1 
ATOM   933  C CB   . GLU   A 1 88  ? 14.263 1.425   -5.755  1.00 31.16  ? 68  GLU   A CB   1 
ATOM   934  C CG   . GLU   A 1 88  ? 13.235 0.334   -5.527  1.00 48.34  ? 68  GLU   A CG   1 
ATOM   935  C CD   . GLU   A 1 88  ? 12.176 0.303   -6.626  1.00 65.96  ? 68  GLU   A CD   1 
ATOM   936  O OE1  . GLU   A 1 88  ? 11.382 1.270   -6.718  1.00 57.49  ? 68  GLU   A OE1  1 
ATOM   937  O OE2  . GLU   A 1 88  ? 12.157 -0.676  -7.409  1.00 55.03  ? 68  GLU   A OE2  1 
ATOM   938  H H    . GLU   A 1 88  ? 16.244 2.818   -5.863  1.00 30.93  ? 68  GLU   A H    1 
ATOM   939  H HA   . GLU   A 1 88  ? 14.864 1.893   -3.847  1.00 33.13  ? 68  GLU   A HA   1 
ATOM   940  H HB2  . GLU   A 1 88  ? 13.783 2.264   -5.836  1.00 37.39  ? 68  GLU   A HB2  1 
ATOM   941  H HB3  . GLU   A 1 88  ? 14.721 1.223   -6.585  1.00 37.39  ? 68  GLU   A HB3  1 
ATOM   942  H HG2  . GLU   A 1 88  ? 13.681 -0.527  -5.512  1.00 58.01  ? 68  GLU   A HG2  1 
ATOM   943  H HG3  . GLU   A 1 88  ? 12.787 0.490   -4.680  1.00 58.01  ? 68  GLU   A HG3  1 
ATOM   944  N N    . LYS   A 1 89  ? 16.852 -0.268  -5.132  1.00 25.79  ? 69  LYS   A N    1 
ATOM   945  C CA   . LYS   A 1 89  ? 17.521 -1.532  -4.837  1.00 24.35  ? 69  LYS   A CA   1 
ATOM   946  C C    . LYS   A 1 89  ? 18.420 -1.424  -3.604  1.00 21.43  ? 69  LYS   A C    1 
ATOM   947  O O    . LYS   A 1 89  ? 18.545 -2.393  -2.847  1.00 21.26  ? 69  LYS   A O    1 
ATOM   948  C CB   . LYS   A 1 89  ? 18.346 -2.004  -6.034  1.00 28.40  ? 69  LYS   A CB   1 
ATOM   949  C CG   . LYS   A 1 89  ? 17.537 -2.565  -7.202  1.00 33.25  ? 69  LYS   A CG   1 
ATOM   950  H H    . LYS   A 1 89  ? 17.100 0.107   -5.865  1.00 30.95  ? 69  LYS   A H    1 
ATOM   951  H HA   . LYS   A 1 89  ? 16.837 -2.197  -4.664  1.00 29.22  ? 69  LYS   A HA   1 
ATOM   952  H HB2  . LYS   A 1 89  ? 18.856 -1.251  -6.371  1.00 34.09  ? 69  LYS   A HB2  1 
ATOM   953  H HB3  . LYS   A 1 89  ? 18.946 -2.705  -5.735  1.00 34.09  ? 69  LYS   A HB3  1 
ATOM   954  N N    . LEU   A 1 90  ? 19.008 -0.252  -3.357  1.00 19.68  ? 70  LEU   A N    1 
ATOM   955  C CA   . LEU   A 1 90  ? 19.758 -0.063  -2.123  1.00 19.01  ? 70  LEU   A CA   1 
ATOM   956  C C    . LEU   A 1 90  ? 18.865 -0.218  -0.903  1.00 18.58  ? 70  LEU   A C    1 
ATOM   957  O O    . LEU   A 1 90  ? 19.255 -0.862  0.075   1.00 19.72  ? 70  LEU   A O    1 
ATOM   958  C CB   . LEU   A 1 90  ? 20.466 1.292   -2.123  1.00 19.44  ? 70  LEU   A CB   1 
ATOM   959  C CG   . LEU   A 1 90  ? 21.692 1.330   -3.011  1.00 18.76  ? 70  LEU   A CG   1 
ATOM   960  C CD1  . LEU   A 1 90  ? 22.064 2.777   -3.371  1.00 20.33  ? 70  LEU   A CD1  1 
ATOM   961  C CD2  . LEU   A 1 90  ? 22.900 0.650   -2.368  1.00 18.94  ? 70  LEU   A CD2  1 
ATOM   962  H H    . LEU   A 1 90  ? 18.988 0.432   -3.878  1.00 23.62  ? 70  LEU   A H    1 
ATOM   963  H HA   . LEU   A 1 90  ? 20.445 -0.745  -2.074  1.00 22.81  ? 70  LEU   A HA   1 
ATOM   964  H HB2  . LEU   A 1 90  ? 19.848 1.969   -2.440  1.00 23.34  ? 70  LEU   A HB2  1 
ATOM   965  H HB3  . LEU   A 1 90  ? 20.748 1.498   -1.218  1.00 23.34  ? 70  LEU   A HB3  1 
ATOM   966  H HG   . LEU   A 1 90  ? 21.470 0.842   -3.820  1.00 22.51  ? 70  LEU   A HG   1 
ATOM   967  H HD11 . LEU   A 1 90  ? 22.846 2.769   -3.944  1.00 24.40  ? 70  LEU   A HD11 1 
ATOM   968  H HD12 . LEU   A 1 90  ? 21.318 3.189   -3.834  1.00 24.40  ? 70  LEU   A HD12 1 
ATOM   969  H HD13 . LEU   A 1 90  ? 22.257 3.265   -2.555  1.00 24.40  ? 70  LEU   A HD13 1 
ATOM   970  H HD21 . LEU   A 1 90  ? 23.653 0.702   -2.976  1.00 22.73  ? 70  LEU   A HD21 1 
ATOM   971  H HD22 . LEU   A 1 90  ? 23.113 1.105   -1.538  1.00 22.73  ? 70  LEU   A HD22 1 
ATOM   972  H HD23 . LEU   A 1 90  ? 22.682 -0.278  -2.189  1.00 22.73  ? 70  LEU   A HD23 1 
ATOM   973  N N    . GLY   A 1 91  ? 17.654 0.357   -0.944  1.00 20.20  ? 71  GLY   A N    1 
ATOM   974  C CA   . GLY   A 1 91  ? 16.755 0.224   0.189   1.00 22.12  ? 71  GLY   A CA   1 
ATOM   975  C C    . GLY   A 1 91  ? 16.314 -1.213  0.392   1.00 22.27  ? 71  GLY   A C    1 
ATOM   976  O O    . GLY   A 1 91  ? 16.221 -1.693  1.528   1.00 23.85  ? 71  GLY   A O    1 
ATOM   977  H H    . GLY   A 1 91  ? 17.344 0.816   -1.603  1.00 24.24  ? 71  GLY   A H    1 
ATOM   978  H HA2  . GLY   A 1 91  ? 17.203 0.525   0.994   1.00 26.54  ? 71  GLY   A HA2  1 
ATOM   979  H HA3  . GLY   A 1 91  ? 15.967 0.770   0.042   1.00 26.54  ? 71  GLY   A HA3  1 
ATOM   980  N N    . GLU   A 1 92  ? 16.105 -1.940  -0.707  1.00 24.15  ? 72  GLU   A N    1 
ATOM   981  C CA   . GLU   A 1 92  ? 15.759 -3.352  -0.604  1.00 27.53  ? 72  GLU   A CA   1 
ATOM   982  C C    . GLU   A 1 92  ? 16.908 -4.157  -0.014  1.00 26.68  ? 72  GLU   A C    1 
ATOM   983  O O    . GLU   A 1 92  ? 16.702 -5.032  0.829   1.00 28.86  ? 72  GLU   A O    1 
ATOM   984  C CB   . GLU   A 1 92  ? 15.399 -3.885  -1.987  1.00 33.33  ? 72  GLU   A CB   1 
ATOM   985  C CG   . GLU   A 1 92  ? 14.056 -3.386  -2.486  1.00 41.15  ? 72  GLU   A CG   1 
ATOM   986  C CD   . GLU   A 1 92  ? 13.771 -3.803  -3.915  1.00 48.19  ? 72  GLU   A CD   1 
ATOM   987  O OE1  . GLU   A 1 92  ? 14.385 -4.794  -4.392  1.00 50.60  ? 72  GLU   A OE1  1 
ATOM   988  O OE2  . GLU   A 1 92  ? 12.923 -3.135  -4.554  1.00 50.31  ? 72  GLU   A OE2  1 
ATOM   989  H H    . GLU   A 1 92  ? 16.158 -1.642  -1.512  1.00 28.98  ? 72  GLU   A H    1 
ATOM   990  H HA   . GLU   A 1 92  ? 14.990 -3.451  -0.021  1.00 33.04  ? 72  GLU   A HA   1 
ATOM   991  H HB2  . GLU   A 1 92  ? 16.078 -3.601  -2.620  1.00 40.00  ? 72  GLU   A HB2  1 
ATOM   992  H HB3  . GLU   A 1 92  ? 15.364 -4.854  -1.951  1.00 40.00  ? 72  GLU   A HB3  1 
ATOM   993  H HG2  . GLU   A 1 92  ? 13.355 -3.748  -1.922  1.00 49.38  ? 72  GLU   A HG2  1 
ATOM   994  H HG3  . GLU   A 1 92  ? 14.045 -2.417  -2.448  1.00 49.38  ? 72  GLU   A HG3  1 
ATOM   995  N N    . HIS   A 1 93  ? 18.132 -3.845  -0.418  1.00 23.70  ? 73  HIS   A N    1 
ATOM   996  C CA   A HIS   A 1 93  ? 19.307 -4.559  0.086   0.52 22.98  ? 73  HIS   A CA   1 
ATOM   997  C CA   B HIS   A 1 93  ? 19.247 -4.615  0.097   0.48 23.35  ? 73  HIS   A CA   1 
ATOM   998  C C    . HIS   A 1 93  ? 19.497 -4.344  1.578   1.00 22.99  ? 73  HIS   A C    1 
ATOM   999  O O    . HIS   A 1 93  ? 19.974 -5.232  2.284   1.00 24.55  ? 73  HIS   A O    1 
ATOM   1000 C CB   A HIS   A 1 93  ? 20.566 -4.079  -0.649  0.52 22.94  ? 73  HIS   A CB   1 
ATOM   1001 C CB   B HIS   A 1 93  ? 20.479 -4.372  -0.757  0.48 24.16  ? 73  HIS   A CB   1 
ATOM   1002 C CG   A HIS   A 1 93  ? 21.854 -4.680  -0.135  0.52 24.08  ? 73  HIS   A CG   1 
ATOM   1003 C CG   B HIS   A 1 93  ? 21.366 -5.570  -0.848  0.48 23.55  ? 73  HIS   A CG   1 
ATOM   1004 N ND1  A HIS   A 1 93  ? 22.276 -5.947  -0.472  0.52 24.35  ? 73  HIS   A ND1  1 
ATOM   1005 N ND1  B HIS   A 1 93  ? 22.506 -5.698  -0.088  0.48 24.44  ? 73  HIS   A ND1  1 
ATOM   1006 C CD2  A HIS   A 1 93  ? 22.821 -4.170  0.668   0.52 25.43  ? 73  HIS   A CD2  1 
ATOM   1007 C CD2  B HIS   A 1 93  ? 21.259 -6.714  -1.565  0.48 25.12  ? 73  HIS   A CD2  1 
ATOM   1008 C CE1  A HIS   A 1 93  ? 23.441 -6.198  0.107   0.52 24.15  ? 73  HIS   A CE1  1 
ATOM   1009 C CE1  B HIS   A 1 93  ? 23.081 -6.857  -0.355  0.48 26.41  ? 73  HIS   A CE1  1 
ATOM   1010 N NE2  A HIS   A 1 93  ? 23.793 -5.135  0.805   0.52 25.54  ? 73  HIS   A NE2  1 
ATOM   1011 N NE2  B HIS   A 1 93  ? 22.345 -7.491  -1.247  0.48 26.19  ? 73  HIS   A NE2  1 
ATOM   1012 H H    A HIS   A 1 93  ? 18.316 -3.225  -0.984  0.52 28.44  ? 73  HIS   A H    1 
ATOM   1013 H H    B HIS   A 1 93  ? 18.335 -3.217  -0.969  0.48 28.44  ? 73  HIS   A H    1 
ATOM   1014 H HA   A HIS   A 1 93  ? 19.183 -5.507  -0.080  0.52 27.58  ? 73  HIS   A HA   1 
ATOM   1015 H HA   B HIS   A 1 93  ? 19.045 -5.561  0.031   0.48 28.02  ? 73  HIS   A HA   1 
ATOM   1016 H HB2  A HIS   A 1 93  ? 20.486 -4.314  -1.587  0.52 27.53  ? 73  HIS   A HB2  1 
ATOM   1017 H HB2  B HIS   A 1 93  ? 20.198 -4.137  -1.655  0.48 28.99  ? 73  HIS   A HB2  1 
ATOM   1018 H HB3  A HIS   A 1 93  ? 20.632 -3.116  -0.553  0.52 27.53  ? 73  HIS   A HB3  1 
ATOM   1019 H HB3  B HIS   A 1 93  ? 20.993 -3.646  -0.370  0.48 28.99  ? 73  HIS   A HB3  1 
ATOM   1020 H HD1  B HIS   A 1 93  ? 22.798 -5.115  0.473   0.48 29.33  ? 73  HIS   A HD1  1 
ATOM   1021 H HD2  A HIS   A 1 93  ? 22.826 -3.324  1.055   0.52 30.52  ? 73  HIS   A HD2  1 
ATOM   1022 H HD2  B HIS   A 1 93  ? 20.578 -6.932  -2.160  0.48 30.15  ? 73  HIS   A HD2  1 
ATOM   1023 H HE1  A HIS   A 1 93  ? 23.927 -6.987  0.033   0.52 28.99  ? 73  HIS   A HE1  1 
ATOM   1024 H HE1  B HIS   A 1 93  ? 23.871 -7.172  0.022   0.48 31.69  ? 73  HIS   A HE1  1 
ATOM   1025 H HE2  A HIS   A 1 93  ? 24.513 -5.058  1.270   0.52 30.65  ? 73  HIS   A HE2  1 
ATOM   1026 N N    . ALA   A 1 94  ? 19.134 -3.159  2.083   1.00 21.41  ? 74  ALA   A N    1 
ATOM   1027 C CA   . ALA   A 1 94  ? 19.293 -2.902  3.509   1.00 21.33  ? 74  ALA   A CA   1 
ATOM   1028 C C    . ALA   A 1 94  ? 18.435 -3.839  4.352   1.00 21.64  ? 74  ALA   A C    1 
ATOM   1029 O O    . ALA   A 1 94  ? 18.803 -4.178  5.487   1.00 21.43  ? 74  ALA   A O    1 
ATOM   1030 C CB   . ALA   A 1 94  ? 18.936 -1.459  3.812   1.00 22.95  ? 74  ALA   A CB   1 
ATOM   1031 H H    . ALA   A 1 94  ? 18.802 -2.507  1.630   1.00 25.70  ? 74  ALA   A H    1 
ATOM   1032 H HA   . ALA   A 1 94  ? 20.221 -3.048  3.751   1.00 25.60  ? 74  ALA   A HA   1 
ATOM   1033 H HB1  . ALA   A 1 94  ? 19.039 -1.302  4.764   1.00 27.55  ? 74  ALA   A HB1  1 
ATOM   1034 H HB2  . ALA   A 1 94  ? 19.531 -0.876  3.315   1.00 27.55  ? 74  ALA   A HB2  1 
ATOM   1035 H HB3  . ALA   A 1 94  ? 18.017 -1.299  3.547   1.00 27.55  ? 74  ALA   A HB3  1 
ATOM   1036 N N    . VAL   A 1 95  ? 17.293 -4.262  3.822   1.00 24.20  ? 75  VAL   A N    1 
ATOM   1037 C CA   . VAL   A 1 95  ? 16.483 -5.231  4.545   1.00 26.48  ? 75  VAL   A CA   1 
ATOM   1038 C C    . VAL   A 1 95  ? 17.270 -6.520  4.750   1.00 25.86  ? 75  VAL   A C    1 
ATOM   1039 O O    . VAL   A 1 95  ? 17.262 -7.107  5.837   1.00 27.82  ? 75  VAL   A O    1 
ATOM   1040 C CB   . VAL   A 1 95  ? 15.168 -5.482  3.783   1.00 29.16  ? 75  VAL   A CB   1 
ATOM   1041 C CG1  . VAL   A 1 95  ? 14.353 -6.593  4.453   1.00 31.00  ? 75  VAL   A CG1  1 
ATOM   1042 C CG2  . VAL   A 1 95  ? 14.353 -4.196  3.676   1.00 31.52  ? 75  VAL   A CG2  1 
ATOM   1043 H H    . VAL   A 1 95  ? 16.974 -4.010  3.065   1.00 29.04  ? 75  VAL   A H    1 
ATOM   1044 H HA   . VAL   A 1 95  ? 16.262 -4.873  5.419   1.00 31.78  ? 75  VAL   A HA   1 
ATOM   1045 H HB   . VAL   A 1 95  ? 15.381 -5.774  2.883   1.00 34.99  ? 75  VAL   A HB   1 
ATOM   1046 H HG11 . VAL   A 1 95  ? 13.428 -6.522  4.170   1.00 37.20  ? 75  VAL   A HG11 1 
ATOM   1047 H HG12 . VAL   A 1 95  ? 14.715 -7.454  4.188   1.00 37.20  ? 75  VAL   A HG12 1 
ATOM   1048 H HG13 . VAL   A 1 95  ? 14.413 -6.492  5.416   1.00 37.20  ? 75  VAL   A HG13 1 
ATOM   1049 H HG21 . VAL   A 1 95  ? 13.511 -4.391  3.235   1.00 37.83  ? 75  VAL   A HG21 1 
ATOM   1050 H HG22 . VAL   A 1 95  ? 14.187 -3.853  4.568   1.00 37.83  ? 75  VAL   A HG22 1 
ATOM   1051 H HG23 . VAL   A 1 95  ? 14.855 -3.546  3.160   1.00 37.83  ? 75  VAL   A HG23 1 
ATOM   1052 N N    . TRP   A 1 96  ? 17.956 -6.980  3.705   1.00 24.80  ? 76  TRP   A N    1 
ATOM   1053 C CA   . TRP   A 1 96  ? 18.818 -8.150  3.822   1.00 24.27  ? 76  TRP   A CA   1 
ATOM   1054 C C    . TRP   A 1 96  ? 19.970 -7.898  4.786   1.00 23.06  ? 76  TRP   A C    1 
ATOM   1055 O O    . TRP   A 1 96  ? 20.244 -8.721  5.668   1.00 23.71  ? 76  TRP   A O    1 
ATOM   1056 C CB   . TRP   A 1 96  ? 19.354 -8.546  2.442   1.00 26.11  ? 76  TRP   A CB   1 
ATOM   1057 C CG   . TRP   A 1 96  ? 20.275 -9.692  2.541   1.00 27.03  ? 76  TRP   A CG   1 
ATOM   1058 C CD1  . TRP   A 1 96  ? 19.935 -11.020 2.536   1.00 29.65  ? 76  TRP   A CD1  1 
ATOM   1059 C CD2  . TRP   A 1 96  ? 21.684 -9.636  2.713   1.00 27.84  ? 76  TRP   A CD2  1 
ATOM   1060 N NE1  . TRP   A 1 96  ? 21.055 -11.788 2.701   1.00 31.54  ? 76  TRP   A NE1  1 
ATOM   1061 C CE2  . TRP   A 1 96  ? 22.145 -10.968 2.810   1.00 28.99  ? 76  TRP   A CE2  1 
ATOM   1062 C CE3  . TRP   A 1 96  ? 22.609 -8.592  2.801   1.00 28.59  ? 76  TRP   A CE3  1 
ATOM   1063 C CZ2  . TRP   A 1 96  ? 23.488 -11.277 2.985   1.00 29.37  ? 76  TRP   A CZ2  1 
ATOM   1064 C CZ3  . TRP   A 1 96  ? 23.953 -8.912  2.975   1.00 28.08  ? 76  TRP   A CZ3  1 
ATOM   1065 C CH2  . TRP   A 1 96  ? 24.373 -10.239 3.066   1.00 27.43  ? 76  TRP   A CH2  1 
ATOM   1066 H H    . TRP   A 1 96  ? 17.939 -6.633  2.918   1.00 29.76  ? 76  TRP   A H    1 
ATOM   1067 H HA   . TRP   A 1 96  ? 18.291 -8.886  4.169   1.00 29.13  ? 76  TRP   A HA   1 
ATOM   1068 H HB2  . TRP   A 1 96  ? 18.613 -8.797  1.869   1.00 31.34  ? 76  TRP   A HB2  1 
ATOM   1069 H HB3  . TRP   A 1 96  ? 19.834 -7.798  2.056   1.00 31.34  ? 76  TRP   A HB3  1 
ATOM   1070 H HD1  . TRP   A 1 96  ? 19.071 -11.349 2.435   1.00 35.59  ? 76  TRP   A HD1  1 
ATOM   1071 H HE1  . TRP   A 1 96  ? 21.071 -12.647 2.732   1.00 37.85  ? 76  TRP   A HE1  1 
ATOM   1072 H HE3  . TRP   A 1 96  ? 22.334 -7.706  2.744   1.00 34.31  ? 76  TRP   A HE3  1 
ATOM   1073 H HZ2  . TRP   A 1 96  ? 23.775 -12.160 3.044   1.00 35.25  ? 76  TRP   A HZ2  1 
ATOM   1074 H HZ3  . TRP   A 1 96  ? 24.582 -8.229  3.032   1.00 33.70  ? 76  TRP   A HZ3  1 
ATOM   1075 H HH2  . TRP   A 1 96  ? 25.277 -10.422 3.185   1.00 32.92  ? 76  TRP   A HH2  1 
ATOM   1076 N N    . SER   A 1 97  ? 20.669 -6.772  4.628   0.94 22.28  ? 77  SER   A N    1 
ATOM   1077 C CA   . SER   A 1 97  ? 21.869 -6.577  5.428   0.94 22.70  ? 77  SER   A CA   1 
ATOM   1078 C C    . SER   A 1 97  ? 21.535 -6.423  6.899   0.94 21.44  ? 77  SER   A C    1 
ATOM   1079 O O    . SER   A 1 97  ? 22.336 -6.797  7.752   0.94 22.31  ? 77  SER   A O    1 
ATOM   1080 C CB   . SER   A 1 97  ? 22.741 -5.456  4.864   0.94 25.67  ? 77  SER   A CB   1 
ATOM   1081 O OG   . SER   A 1 97  ? 22.037 -4.314  4.589   0.94 27.34  ? 77  SER   A OG   1 
ATOM   1082 H H    . SER   A 1 97  ? 20.476 -6.134  4.085   0.94 26.74  ? 77  SER   A H    1 
ATOM   1083 H HA   . SER   A 1 97  ? 22.431 -7.365  5.364   0.94 27.24  ? 77  SER   A HA   1 
ATOM   1084 H HB2  . SER   A 1 97  ? 23.427 -5.244  5.516   0.94 30.81  ? 77  SER   A HB2  1 
ATOM   1085 H HB3  . SER   A 1 97  ? 23.151 -5.769  4.042   0.94 30.81  ? 77  SER   A HB3  1 
ATOM   1086 H HG   . SER   A 1 97  ? 22.555 -3.719  4.301   0.94 32.81  ? 77  SER   A HG   1 
ATOM   1087 N N    A LEU   A 1 98  ? 20.355 -5.895  7.222   0.63 20.07  ? 78  LEU   A N    1 
ATOM   1088 N N    C LEU   A 1 98  ? 20.351 -5.900  7.221   0.37 25.08  ? 78  LEU   A N    1 
ATOM   1089 C CA   A LEU   A 1 98  ? 19.938 -5.824  8.620   0.63 21.53  ? 78  LEU   A CA   1 
ATOM   1090 C CA   C LEU   A 1 98  ? 19.952 -5.834  8.622   0.37 26.56  ? 78  LEU   A CA   1 
ATOM   1091 C C    A LEU   A 1 98  ? 19.715 -7.203  9.238   0.63 22.71  ? 78  LEU   A C    1 
ATOM   1092 C C    C LEU   A 1 98  ? 19.805 -7.224  9.228   0.37 25.93  ? 78  LEU   A C    1 
ATOM   1093 O O    A LEU   A 1 98  ? 19.790 -7.341  10.466  0.63 26.18  ? 78  LEU   A O    1 
ATOM   1094 O O    C LEU   A 1 98  ? 20.052 -7.406  10.426  0.37 26.86  ? 78  LEU   A O    1 
ATOM   1095 C CB   A LEU   A 1 98  ? 18.670 -4.978  8.752   0.63 25.18  ? 78  LEU   A CB   1 
ATOM   1096 C CB   C LEU   A 1 98  ? 18.656 -5.035  8.779   0.37 28.27  ? 78  LEU   A CB   1 
ATOM   1097 C CG   A LEU   A 1 98  ? 18.350 -4.436  10.149  0.63 27.60  ? 78  LEU   A CG   1 
ATOM   1098 C CG   C LEU   A 1 98  ? 18.745 -3.666  9.466   0.37 29.69  ? 78  LEU   A CG   1 
ATOM   1099 C CD1  A LEU   A 1 98  ? 19.511 -3.559  10.644  0.63 28.26  ? 78  LEU   A CD1  1 
ATOM   1100 C CD1  C LEU   A 1 98  ? 17.357 -3.134  9.726   0.37 30.30  ? 78  LEU   A CD1  1 
ATOM   1101 C CD2  A LEU   A 1 98  ? 17.047 -3.672  10.150  0.63 29.07  ? 78  LEU   A CD2  1 
ATOM   1102 C CD2  C LEU   A 1 98  ? 19.538 -3.747  10.775  0.37 30.24  ? 78  LEU   A CD2  1 
ATOM   1103 H H    A LEU   A 1 98  ? 19.788 -5.575  6.660   0.67 24.09  ? 78  LEU   A H    1 
ATOM   1104 H H    C LEU   A 1 98  ? 19.778 -5.586  6.662   0.30 30.10  ? 78  LEU   A H    1 
ATOM   1105 H HA   A LEU   A 1 98  ? 20.640 -5.387  9.127   0.63 25.84  ? 78  LEU   A HA   1 
ATOM   1106 H HA   C LEU   A 1 98  ? 20.641 -5.363  9.117   0.37 31.88  ? 78  LEU   A HA   1 
ATOM   1107 H HB2  A LEU   A 1 98  ? 18.759 -4.212  8.163   0.63 30.22  ? 78  LEU   A HB2  1 
ATOM   1108 H HB2  C LEU   A 1 98  ? 18.293 -4.881  7.893   0.37 33.92  ? 78  LEU   A HB2  1 
ATOM   1109 H HB3  A LEU   A 1 98  ? 17.916 -5.522  8.477   0.63 30.22  ? 78  LEU   A HB3  1 
ATOM   1110 H HB3  C LEU   A 1 98  ? 18.039 -5.571  9.302   0.37 33.92  ? 78  LEU   A HB3  1 
ATOM   1111 H HG   A LEU   A 1 98  ? 18.242 -5.178  10.766  0.63 33.13  ? 78  LEU   A HG   1 
ATOM   1112 H HG   C LEU   A 1 98  ? 19.216 -3.052  8.880   0.37 35.62  ? 78  LEU   A HG   1 
ATOM   1113 H HD11 A LEU   A 1 98  ? 19.197 -3.001  11.372  0.63 33.92  ? 78  LEU   A HD11 1 
ATOM   1114 H HD11 C LEU   A 1 98  ? 17.417 -2.192  9.952   0.37 36.37  ? 78  LEU   A HD11 1 
ATOM   1115 H HD12 A LEU   A 1 98  ? 20.230 -4.132  10.952  0.63 33.92  ? 78  LEU   A HD12 1 
ATOM   1116 H HD12 C LEU   A 1 98  ? 16.820 -3.249  8.927   0.37 36.37  ? 78  LEU   A HD12 1 
ATOM   1117 H HD13 A LEU   A 1 98  ? 19.821 -3.004  9.911   0.63 33.92  ? 78  LEU   A HD13 1 
ATOM   1118 H HD13 C LEU   A 1 98  ? 16.964 -3.626  10.464  0.37 36.37  ? 78  LEU   A HD13 1 
ATOM   1119 H HD21 A LEU   A 1 98  ? 16.869 -3.352  11.048  0.63 34.89  ? 78  LEU   A HD21 1 
ATOM   1120 H HD21 C LEU   A 1 98  ? 19.309 -2.986  11.331  0.37 36.29  ? 78  LEU   A HD21 1 
ATOM   1121 H HD22 A LEU   A 1 98  ? 17.121 -2.921  9.540   0.63 34.89  ? 78  LEU   A HD22 1 
ATOM   1122 H HD22 C LEU   A 1 98  ? 19.309 -4.571  11.232  0.37 36.29  ? 78  LEU   A HD22 1 
ATOM   1123 H HD23 A LEU   A 1 98  ? 16.334 -4.263  9.862   0.63 34.89  ? 78  LEU   A HD23 1 
ATOM   1124 H HD23 C LEU   A 1 98  ? 20.487 -3.734  10.571  0.37 36.29  ? 78  LEU   A HD23 1 
ATOM   1125 N N    . GLN   A 1 99  ? 19.429 -8.216  8.431   1.00 22.86  ? 79  GLN   A N    1 
ATOM   1126 C CA   . GLN   A 1 99  ? 19.316 -9.575  8.940   1.00 25.09  ? 79  GLN   A CA   1 
ATOM   1127 C C    . GLN   A 1 99  ? 20.684 -10.248 9.069   0.81 22.68  ? 79  GLN   A C    1 
ATOM   1128 O O    . GLN   A 1 99  ? 20.980 -10.888 10.087  0.97 24.50  ? 79  GLN   A O    1 
ATOM   1129 C CB   . GLN   A 1 99  ? 18.407 -10.394 8.019   1.00 30.35  ? 79  GLN   A CB   1 
ATOM   1130 H H    A GLN   A 1 99  ? 19.294 -8.144  7.585   0.63 27.43  ? 79  GLN   A H    1 
ATOM   1131 H H    C GLN   A 1 99  ? 19.234 -8.128  7.598   0.37 27.43  ? 79  GLN   A H    1 
ATOM   1132 H HA   . GLN   A 1 99  ? 18.918 -9.543  9.824   1.00 30.11  ? 79  GLN   A HA   1 
ATOM   1133 N N    A CYS   A 1 100 ? 21.523 -10.118 8.030   0.35 22.40  ? 80  CYS   A N    1 
ATOM   1134 N N    B CYS   A 1 100 ? 21.529 -10.113 8.059   0.65 22.40  ? 80  CYS   A N    1 
ATOM   1135 C CA   A CYS   A 1 100 ? 22.812 -10.798 7.953   0.35 20.58  ? 80  CYS   A CA   1 
ATOM   1136 C CA   B CYS   A 1 100 ? 22.781 -10.846 8.033   0.65 20.58  ? 80  CYS   A CA   1 
ATOM   1137 C C    A CYS   A 1 100 ? 23.886 -10.129 8.796   0.35 19.43  ? 80  CYS   A C    1 
ATOM   1138 C C    B CYS   A 1 100 ? 23.942 -10.111 8.698   0.65 19.43  ? 80  CYS   A C    1 
ATOM   1139 O O    A CYS   A 1 100 ? 24.786 -10.812 9.296   0.35 19.16  ? 80  CYS   A O    1 
ATOM   1140 O O    B CYS   A 1 100 ? 24.925 -10.759 9.056   0.65 19.16  ? 80  CYS   A O    1 
ATOM   1141 C CB   A CYS   A 1 100 ? 23.290 -10.817 6.500   0.35 19.91  ? 80  CYS   A CB   1 
ATOM   1142 C CB   B CYS   A 1 100 ? 23.066 -11.270 6.592   0.65 19.91  ? 80  CYS   A CB   1 
ATOM   1143 S SG   A CYS   A 1 100 ? 24.925 -11.569 6.242   0.35 20.43  ? 80  CYS   A SG   1 
ATOM   1144 S SG   B CYS   A 1 100 ? 21.704 -12.321 5.921   0.65 20.43  ? 80  CYS   A SG   1 
ATOM   1145 H H    A CYS   A 1 100 ? 21.360 -9.628  7.342   0.35 26.88  ? 80  CYS   A H    1 
ATOM   1146 H H    B CYS   A 1 100 ? 21.399 -9.604  7.378   0.65 26.88  ? 80  CYS   A H    1 
ATOM   1147 H HA   A CYS   A 1 100 ? 22.691 -11.705 8.275   0.35 24.69  ? 80  CYS   A HA   1 
ATOM   1148 H HA   B CYS   A 1 100 ? 22.714 -11.667 8.545   0.65 24.69  ? 80  CYS   A HA   1 
ATOM   1149 H HB2  A CYS   A 1 100 ? 22.651 -11.321 5.973   0.35 23.89  ? 80  CYS   A HB2  1 
ATOM   1150 H HB2  B CYS   A 1 100 ? 23.148 -10.481 6.035   0.65 23.89  ? 80  CYS   A HB2  1 
ATOM   1151 H HB3  A CYS   A 1 100 ? 23.336 -9.903  6.180   0.35 23.89  ? 80  CYS   A HB3  1 
ATOM   1152 H HB3  B CYS   A 1 100 ? 23.890 -11.782 6.565   0.65 23.89  ? 80  CYS   A HB3  1 
ATOM   1153 H HG   A CYS   A 1 100 ? 25.737 -10.972 6.894   0.35 24.52  ? 80  CYS   A HG   1 
ATOM   1154 H HG   B CYS   A 1 100 ? 22.061 -12.808 4.885   0.65 24.52  ? 80  CYS   A HG   1 
ATOM   1155 N N    . PHE   A 1 101 ? 23.828 -8.809  8.940   1.00 18.68  ? 81  PHE   A N    1 
ATOM   1156 C CA   . PHE   A 1 101 ? 24.786 -8.042  9.739   1.00 18.09  ? 81  PHE   A CA   1 
ATOM   1157 C C    . PHE   A 1 101 ? 23.966 -7.248  10.761  1.00 17.72  ? 81  PHE   A C    1 
ATOM   1158 O O    . PHE   A 1 101 ? 23.827 -6.025  10.665  1.00 18.68  ? 81  PHE   A O    1 
ATOM   1159 C CB   . PHE   A 1 101 ? 25.626 -7.123  8.849   1.00 18.36  ? 81  PHE   A CB   1 
ATOM   1160 C CG   . PHE   A 1 101 ? 26.480 -7.851  7.881   1.00 18.36  ? 81  PHE   A CG   1 
ATOM   1161 C CD1  . PHE   A 1 101 ? 27.699 -8.390  8.280   1.00 18.37  ? 81  PHE   A CD1  1 
ATOM   1162 C CD2  . PHE   A 1 101 ? 26.104 -7.992  6.576   1.00 20.89  ? 81  PHE   A CD2  1 
ATOM   1163 C CE1  . PHE   A 1 101 ? 28.506 -9.084  7.368   1.00 19.94  ? 81  PHE   A CE1  1 
ATOM   1164 C CE2  . PHE   A 1 101 ? 26.891 -8.698  5.688   1.00 25.06  ? 81  PHE   A CE2  1 
ATOM   1165 C CZ   . PHE   A 1 101 ? 28.107 -9.210  6.085   1.00 22.43  ? 81  PHE   A CZ   1 
ATOM   1166 H H    A PHE   A 1 101 ? 23.225 -8.318  8.573   0.35 22.42  ? 81  PHE   A H    1 
ATOM   1167 H H    B PHE   A 1 101 ? 23.181 -8.328  8.641   0.65 22.42  ? 81  PHE   A H    1 
ATOM   1168 H HA   . PHE   A 1 101 ? 25.400 -8.630  10.207  1.00 21.71  ? 81  PHE   A HA   1 
ATOM   1169 H HB2  . PHE   A 1 101 ? 25.030 -6.547  8.344   1.00 22.03  ? 81  PHE   A HB2  1 
ATOM   1170 H HB3  . PHE   A 1 101 ? 26.206 -6.587  9.412   1.00 22.03  ? 81  PHE   A HB3  1 
ATOM   1171 H HD1  . PHE   A 1 101 ? 27.980 -8.289  9.161   1.00 22.05  ? 81  PHE   A HD1  1 
ATOM   1172 H HD2  . PHE   A 1 101 ? 25.309 -7.608  6.282   1.00 25.08  ? 81  PHE   A HD2  1 
ATOM   1173 H HE1  . PHE   A 1 101 ? 29.313 -9.455  7.645   1.00 23.94  ? 81  PHE   A HE1  1 
ATOM   1174 H HE2  . PHE   A 1 101 ? 26.598 -8.829  4.816   1.00 30.07  ? 81  PHE   A HE2  1 
ATOM   1175 H HZ   . PHE   A 1 101 ? 28.653 -9.642  5.468   1.00 26.92  ? 81  PHE   A HZ   1 
ATOM   1176 N N    . PRO   A 1 102 ? 23.363 -7.930  11.737  1.00 18.44  ? 82  PRO   A N    1 
ATOM   1177 C CA   . PRO   A 1 102 ? 22.284 -7.297  12.522  1.00 19.99  ? 82  PRO   A CA   1 
ATOM   1178 C C    . PRO   A 1 102 ? 22.735 -6.186  13.443  1.00 22.34  ? 82  PRO   A C    1 
ATOM   1179 O O    . PRO   A 1 102 ? 21.896 -5.373  13.842  1.00 26.41  ? 82  PRO   A O    1 
ATOM   1180 C CB   . PRO   A 1 102 ? 21.688 -8.470  13.317  1.00 21.69  ? 82  PRO   A CB   1 
ATOM   1181 C CG   . PRO   A 1 102 ? 22.826 -9.476  13.366  1.00 21.31  ? 82  PRO   A CG   1 
ATOM   1182 C CD   . PRO   A 1 102 ? 23.532 -9.351  12.062  1.00 19.13  ? 82  PRO   A CD   1 
ATOM   1183 H HA   . PRO   A 1 102 ? 21.616 -6.942  11.914  1.00 23.99  ? 82  PRO   A HA   1 
ATOM   1184 H HB2  . PRO   A 1 102 ? 21.435 -8.179  14.207  1.00 26.04  ? 82  PRO   A HB2  1 
ATOM   1185 H HB3  . PRO   A 1 102 ? 20.916 -8.832  12.855  1.00 26.04  ? 82  PRO   A HB3  1 
ATOM   1186 H HG2  . PRO   A 1 102 ? 23.421 -9.262  14.102  1.00 25.57  ? 82  PRO   A HG2  1 
ATOM   1187 H HG3  . PRO   A 1 102 ? 22.467 -10.371 13.479  1.00 25.57  ? 82  PRO   A HG3  1 
ATOM   1188 H HD2  . PRO   A 1 102 ? 24.471 -9.577  12.152  1.00 22.96  ? 82  PRO   A HD2  1 
ATOM   1189 H HD3  . PRO   A 1 102 ? 23.119 -9.913  11.388  1.00 22.96  ? 82  PRO   A HD3  1 
ATOM   1190 N N    . ASP   A 1 103 ? 24.013 -6.111  13.797  1.00 21.29  ? 83  ASP   A N    1 
ATOM   1191 C CA   . ASP   A 1 103 ? 24.495 -5.123  14.755  1.00 20.92  ? 83  ASP   A CA   1 
ATOM   1192 C C    . ASP   A 1 103 ? 25.735 -4.386  14.242  1.00 19.03  ? 83  ASP   A C    1 
ATOM   1193 O O    . ASP   A 1 103 ? 26.565 -3.936  15.033  1.00 20.57  ? 83  ASP   A O    1 
ATOM   1194 C CB   . ASP   A 1 103 ? 24.769 -5.762  16.115  1.00 23.42  ? 83  ASP   A CB   1 
ATOM   1195 C CG   . ASP   A 1 103 ? 25.865 -6.825  16.078  1.00 24.46  ? 83  ASP   A CG   1 
ATOM   1196 O OD1  . ASP   A 1 103 ? 26.385 -7.129  14.990  1.00 23.52  ? 83  ASP   A OD1  1 
ATOM   1197 O OD2  . ASP   A 1 103 ? 26.230 -7.341  17.157  1.00 26.86  ? 83  ASP   A OD2  1 
ATOM   1198 H H    . ASP   A 1 103 ? 24.629 -6.628  13.491  1.00 25.56  ? 83  ASP   A H    1 
ATOM   1199 H HA   . ASP   A 1 103 ? 23.798 -4.458  14.874  1.00 25.11  ? 83  ASP   A HA   1 
ATOM   1200 H HB2  . ASP   A 1 103 ? 25.046 -5.071  16.736  1.00 28.11  ? 83  ASP   A HB2  1 
ATOM   1201 H HB3  . ASP   A 1 103 ? 23.955 -6.185  16.432  1.00 28.11  ? 83  ASP   A HB3  1 
ATOM   1202 N N    . TRP   A 1 104 ? 25.880 -4.258  12.919  1.00 17.56  ? 84  TRP   A N    1 
ATOM   1203 C CA   . TRP   A 1 104 ? 27.100 -3.693  12.332  1.00 17.08  ? 84  TRP   A CA   1 
ATOM   1204 C C    . TRP   A 1 104 ? 27.353 -2.262  12.785  1.00 17.45  ? 84  TRP   A C    1 
ATOM   1205 O O    . TRP   A 1 104 ? 26.456 -1.415  12.761  1.00 19.25  ? 84  TRP   A O    1 
ATOM   1206 C CB   . TRP   A 1 104 ? 26.983 -3.698  10.814  1.00 16.65  ? 84  TRP   A CB   1 
ATOM   1207 C CG   . TRP   A 1 104 ? 28.272 -3.425  10.147  1.00 15.89  ? 84  TRP   A CG   1 
ATOM   1208 C CD1  . TRP   A 1 104 ? 28.670 -2.242  9.579   1.00 17.05  ? 84  TRP   A CD1  1 
ATOM   1209 C CD2  . TRP   A 1 104 ? 29.391 -4.307  10.069  1.00 15.12  ? 84  TRP   A CD2  1 
ATOM   1210 N NE1  . TRP   A 1 104 ? 29.955 -2.357  9.124   1.00 17.60  ? 84  TRP   A NE1  1 
ATOM   1211 C CE2  . TRP   A 1 104 ? 30.415 -3.616  9.413   1.00 15.76  ? 84  TRP   A CE2  1 
ATOM   1212 C CE3  . TRP   A 1 104 ? 29.614 -5.624  10.472  1.00 15.58  ? 84  TRP   A CE3  1 
ATOM   1213 C CZ2  . TRP   A 1 104 ? 31.637 -4.202  9.141   1.00 17.27  ? 84  TRP   A CZ2  1 
ATOM   1214 C CZ3  . TRP   A 1 104 ? 30.824 -6.192  10.235  1.00 16.01  ? 84  TRP   A CZ3  1 
ATOM   1215 C CH2  . TRP   A 1 104 ? 31.826 -5.491  9.552   1.00 17.20  ? 84  TRP   A CH2  1 
ATOM   1216 H H    . TRP   A 1 104 ? 25.288 -4.490  12.340  1.00 21.07  ? 84  TRP   A H    1 
ATOM   1217 H HA   . TRP   A 1 104 ? 27.850 -4.237  12.620  1.00 20.50  ? 84  TRP   A HA   1 
ATOM   1218 H HB2  . TRP   A 1 104 ? 26.671 -4.569  10.523  1.00 19.99  ? 84  TRP   A HB2  1 
ATOM   1219 H HB3  . TRP   A 1 104 ? 26.352 -3.013  10.543  1.00 19.99  ? 84  TRP   A HB3  1 
ATOM   1220 H HD1  . TRP   A 1 104 ? 28.145 -1.477  9.512   1.00 20.47  ? 84  TRP   A HD1  1 
ATOM   1221 H HE1  . TRP   A 1 104 ? 30.402 -1.741  8.723   1.00 21.13  ? 84  TRP   A HE1  1 
ATOM   1222 H HE3  . TRP   A 1 104 ? 28.943 -6.107  10.897  1.00 18.69  ? 84  TRP   A HE3  1 
ATOM   1223 H HZ2  . TRP   A 1 104 ? 32.307 -3.736  8.694   1.00 20.72  ? 84  TRP   A HZ2  1 
ATOM   1224 H HZ3  . TRP   A 1 104 ? 30.990 -7.058  10.531  1.00 19.22  ? 84  TRP   A HZ3  1 
ATOM   1225 H HH2  . TRP   A 1 104 ? 32.636 -5.912  9.376   1.00 20.65  ? 84  TRP   A HH2  1 
ATOM   1226 N N    . VAL   A 1 105 ? 28.608 -1.987  13.118  1.00 16.63  ? 85  VAL   A N    1 
ATOM   1227 C CA   . VAL   A 1 105 ? 29.068 -0.648  13.483  1.00 17.36  ? 85  VAL   A CA   1 
ATOM   1228 C C    . VAL   A 1 105 ? 30.335 -0.342  12.709  1.00 16.59  ? 85  VAL   A C    1 
ATOM   1229 O O    . VAL   A 1 105 ? 31.241 -1.178  12.647  1.00 16.40  ? 85  VAL   A O    1 
ATOM   1230 C CB   . VAL   A 1 105 ? 29.324 -0.517  15.008  1.00 18.78  ? 85  VAL   A CB   1 
ATOM   1231 C CG1  . VAL   A 1 105 ? 29.829 0.887   15.384  1.00 20.41  ? 85  VAL   A CG1  1 
ATOM   1232 C CG2  . VAL   A 1 105 ? 28.060 -0.844  15.777  1.00 23.16  ? 85  VAL   A CG2  1 
ATOM   1233 H H    . VAL   A 1 105 ? 29.234 -2.577  13.140  1.00 19.96  ? 85  VAL   A H    1 
ATOM   1234 H HA   . VAL   A 1 105 ? 28.387 -0.003  13.232  1.00 20.84  ? 85  VAL   A HA   1 
ATOM   1235 H HB   . VAL   A 1 105 ? 30.019 -1.148  15.253  1.00 22.54  ? 85  VAL   A HB   1 
ATOM   1236 H HG11 . VAL   A 1 105 ? 29.828 0.974   16.350  1.00 24.49  ? 85  VAL   A HG11 1 
ATOM   1237 H HG12 . VAL   A 1 105 ? 30.730 1.000   15.043  1.00 24.49  ? 85  VAL   A HG12 1 
ATOM   1238 H HG13 . VAL   A 1 105 ? 29.240 1.550   14.991  1.00 24.49  ? 85  VAL   A HG13 1 
ATOM   1239 H HG21 . VAL   A 1 105 ? 28.226 -0.723  16.725  1.00 27.80  ? 85  VAL   A HG21 1 
ATOM   1240 H HG22 . VAL   A 1 105 ? 27.351 -0.249  15.487  1.00 27.80  ? 85  VAL   A HG22 1 
ATOM   1241 H HG23 . VAL   A 1 105 ? 27.812 -1.765  15.600  1.00 27.80  ? 85  VAL   A HG23 1 
ATOM   1242 N N    . TRP   A 1 106 ? 30.433 0.887   12.196  1.00 16.51  ? 86  TRP   A N    1 
ATOM   1243 C CA   . TRP   A 1 106 ? 31.696 1.430   11.698  1.00 16.31  ? 86  TRP   A CA   1 
ATOM   1244 C C    . TRP   A 1 106 ? 32.381 2.197   12.826  1.00 17.62  ? 86  TRP   A C    1 
ATOM   1245 O O    . TRP   A 1 106 ? 31.756 3.038   13.458  1.00 19.08  ? 86  TRP   A O    1 
ATOM   1246 C CB   . TRP   A 1 106 ? 31.483 2.383   10.517  1.00 16.65  ? 86  TRP   A CB   1 
ATOM   1247 C CG   . TRP   A 1 106 ? 30.705 1.821   9.351   1.00 17.19  ? 86  TRP   A CG   1 
ATOM   1248 C CD1  . TRP   A 1 106 ? 29.426 2.141   8.975   1.00 17.36  ? 86  TRP   A CD1  1 
ATOM   1249 C CD2  . TRP   A 1 106 ? 31.150 0.817   8.416   1.00 17.08  ? 86  TRP   A CD2  1 
ATOM   1250 N NE1  . TRP   A 1 106 ? 29.076 1.452   7.839   1.00 17.59  ? 86  TRP   A NE1  1 
ATOM   1251 C CE2  . TRP   A 1 106 ? 30.103 0.614   7.486   1.00 17.06  ? 86  TRP   A CE2  1 
ATOM   1252 C CE3  . TRP   A 1 106 ? 32.328 0.085   8.272   1.00 17.17  ? 86  TRP   A CE3  1 
ATOM   1253 C CZ2  . TRP   A 1 106 ? 30.212 -0.280  6.433   1.00 17.62  ? 86  TRP   A CZ2  1 
ATOM   1254 C CZ3  . TRP   A 1 106 ? 32.421 -0.804  7.217   1.00 17.61  ? 86  TRP   A CZ3  1 
ATOM   1255 C CH2  . TRP   A 1 106 ? 31.383 -0.980  6.323   1.00 18.58  ? 86  TRP   A CH2  1 
ATOM   1256 H H    . TRP   A 1 106 ? 29.771 1.432   12.125  1.00 19.81  ? 86  TRP   A H    1 
ATOM   1257 H HA   . TRP   A 1 106 ? 32.253 0.696   11.397  1.00 19.57  ? 86  TRP   A HA   1 
ATOM   1258 H HB2  . TRP   A 1 106 ? 30.998 3.160   10.838  1.00 19.98  ? 86  TRP   A HB2  1 
ATOM   1259 H HB3  . TRP   A 1 106 ? 32.352 2.650   10.181  1.00 19.98  ? 86  TRP   A HB3  1 
ATOM   1260 H HD1  . TRP   A 1 106 ? 28.874 2.739   9.425   1.00 20.83  ? 86  TRP   A HD1  1 
ATOM   1261 H HE1  . TRP   A 1 106 ? 28.331 1.533   7.417   1.00 21.11  ? 86  TRP   A HE1  1 
ATOM   1262 H HE3  . TRP   A 1 106 ? 33.032 0.193   8.870   1.00 20.60  ? 86  TRP   A HE3  1 
ATOM   1263 H HZ2  . TRP   A 1 106 ? 29.518 -0.400  5.826   1.00 21.15  ? 86  TRP   A HZ2  1 
ATOM   1264 H HZ3  . TRP   A 1 106 ? 33.203 -1.295  7.107   1.00 21.14  ? 86  TRP   A HZ3  1 
ATOM   1265 H HH2  . TRP   A 1 106 ? 31.483 -1.590  5.628   1.00 22.29  ? 86  TRP   A HH2  1 
ATOM   1266 N N    . THR   A 1 107 ? 33.669 1.943   13.037  1.00 17.36  ? 87  THR   A N    1 
ATOM   1267 C CA   . THR   A 1 107 ? 34.435 2.553   14.109  1.00 17.49  ? 87  THR   A CA   1 
ATOM   1268 C C    . THR   A 1 107 ? 35.703 3.203   13.535  1.00 16.17  ? 87  THR   A C    1 
ATOM   1269 O O    . THR   A 1 107 ? 36.078 2.993   12.374  1.00 16.42  ? 87  THR   A O    1 
ATOM   1270 C CB   . THR   A 1 107 ? 34.849 1.525   15.172  1.00 20.47  ? 87  THR   A CB   1 
ATOM   1271 O OG1  . THR   A 1 107 ? 35.765 0.586   14.594  1.00 21.33  ? 87  THR   A OG1  1 
ATOM   1272 C CG2  . THR   A 1 107 ? 33.650 0.785   15.756  1.00 22.72  ? 87  THR   A CG2  1 
ATOM   1273 H H    . THR   A 1 107 ? 34.133 1.404   12.553  1.00 20.83  ? 87  THR   A H    1 
ATOM   1274 H HA   . THR   A 1 107 ? 33.883 3.234   14.524  1.00 20.99  ? 87  THR   A HA   1 
ATOM   1275 H HB   . THR   A 1 107 ? 35.275 1.993   15.907  1.00 24.57  ? 87  THR   A HB   1 
ATOM   1276 H HG1  . THR   A 1 107 ? 36.500 0.962   14.436  1.00 25.60  ? 87  THR   A HG1  1 
ATOM   1277 H HG21 . THR   A 1 107 ? 33.941 0.180   16.456  1.00 27.26  ? 87  THR   A HG21 1 
ATOM   1278 H HG22 . THR   A 1 107 ? 33.018 1.419   16.130  1.00 27.26  ? 87  THR   A HG22 1 
ATOM   1279 H HG23 . THR   A 1 107 ? 33.207 0.272   15.062  1.00 27.26  ? 87  THR   A HG23 1 
ATOM   1280 N N    . ASP   A 1 108 ? 36.389 3.996   14.363  1.00 18.44  ? 88  ASP   A N    1 
ATOM   1281 C CA   . ASP   A 1 108 ? 37.706 4.557   13.979  1.00 18.80  ? 88  ASP   A CA   1 
ATOM   1282 C C    . ASP   A 1 108 ? 37.608 5.317   12.663  1.00 19.51  ? 88  ASP   A C    1 
ATOM   1283 O O    . ASP   A 1 108 ? 38.444 5.190   11.765  1.00 19.61  ? 88  ASP   A O    1 
ATOM   1284 C CB   . ASP   A 1 108 ? 38.781 3.475   13.871  1.00 19.16  ? 88  ASP   A CB   1 
ATOM   1285 C CG   . ASP   A 1 108 ? 38.938 2.729   15.137  0.73 20.93  ? 88  ASP   A CG   1 
ATOM   1286 O OD1  . ASP   A 1 108 ? 39.554 3.310   16.052  0.75 24.12  ? 88  ASP   A OD1  1 
ATOM   1287 O OD2  . ASP   A 1 108 ? 38.399 1.598   15.218  0.69 20.94  ? 88  ASP   A OD2  1 
ATOM   1288 H H    . ASP   A 1 108 ? 36.123 4.226   15.147  1.00 22.13  ? 88  ASP   A H    1 
ATOM   1289 H HA   . ASP   A 1 108 ? 37.972 5.174   14.679  1.00 22.57  ? 88  ASP   A HA   1 
ATOM   1290 H HB2  . ASP   A 1 108 ? 38.533 2.846   13.176  1.00 22.99  ? 88  ASP   A HB2  1 
ATOM   1291 H HB3  . ASP   A 1 108 ? 39.631 3.890   13.656  1.00 22.99  ? 88  ASP   A HB3  1 
ATOM   1292 N N    . ILE   A 1 109 ? 36.553 6.105   12.540  1.00 19.05  ? 89  ILE   A N    1 
ATOM   1293 C CA   . ILE   A 1 109 ? 36.216 6.730   11.270  1.00 18.89  ? 89  ILE   A CA   1 
ATOM   1294 C C    . ILE   A 1 109 ? 37.114 7.940   11.046  1.00 19.49  ? 89  ILE   A C    1 
ATOM   1295 O O    . ILE   A 1 109 ? 37.174 8.855   11.885  1.00 21.12  ? 89  ILE   A O    1 
ATOM   1296 C CB   . ILE   A 1 109 ? 34.737 7.139   11.259  1.00 18.38  ? 89  ILE   A CB   1 
ATOM   1297 C CG1  . ILE   A 1 109 ? 33.821 5.909   11.311  1.00 19.52  ? 89  ILE   A CG1  1 
ATOM   1298 C CG2  . ILE   A 1 109 ? 34.417 8.001   10.038  1.00 21.39  ? 89  ILE   A CG2  1 
ATOM   1299 C CD1  . ILE   A 1 109 ? 32.447 6.267   11.795  1.00 22.05  ? 89  ILE   A CD1  1 
ATOM   1300 H H    . ILE   A 1 109 ? 36.011 6.296   13.181  1.00 22.86  ? 89  ILE   A H    1 
ATOM   1301 H HA   . ILE   A 1 109 ? 36.376 6.099   10.551  1.00 22.67  ? 89  ILE   A HA   1 
ATOM   1302 H HB   . ILE   A 1 109 ? 34.574 7.667   12.056  1.00 22.06  ? 89  ILE   A HB   1 
ATOM   1303 H HG12 . ILE   A 1 109 ? 33.743 5.529   10.422  1.00 23.43  ? 89  ILE   A HG12 1 
ATOM   1304 H HG13 . ILE   A 1 109 ? 34.198 5.254   11.920  1.00 23.43  ? 89  ILE   A HG13 1 
ATOM   1305 H HG21 . ILE   A 1 109 ? 33.456 8.028   9.914   1.00 25.67  ? 89  ILE   A HG21 1 
ATOM   1306 H HG22 . ILE   A 1 109 ? 34.757 8.898   10.187  1.00 25.67  ? 89  ILE   A HG22 1 
ATOM   1307 H HG23 . ILE   A 1 109 ? 34.841 7.612   9.257   1.00 25.67  ? 89  ILE   A HG23 1 
ATOM   1308 H HD11 . ILE   A 1 109 ? 31.903 5.464   11.823  1.00 26.46  ? 89  ILE   A HD11 1 
ATOM   1309 H HD12 . ILE   A 1 109 ? 32.515 6.653   12.682  1.00 26.46  ? 89  ILE   A HD12 1 
ATOM   1310 H HD13 . ILE   A 1 109 ? 32.055 6.911   11.184  1.00 26.46  ? 89  ILE   A HD13 1 
ATOM   1311 N N    A GLN   A 1 110 ? 37.799 7.958   9.901   0.70 18.56  ? 90  GLN   A N    1 
ATOM   1312 N N    B GLN   A 1 110 ? 37.808 7.966   9.909   0.30 19.86  ? 90  GLN   A N    1 
ATOM   1313 C CA   A GLN   A 1 110 ? 38.589 9.100   9.449   0.70 18.37  ? 90  GLN   A CA   1 
ATOM   1314 C CA   B GLN   A 1 110 ? 38.580 9.136   9.493   0.30 20.56  ? 90  GLN   A CA   1 
ATOM   1315 C C    A GLN   A 1 110 ? 38.098 9.509   8.068   0.70 17.55  ? 90  GLN   A C    1 
ATOM   1316 C C    B GLN   A 1 110 ? 38.139 9.526   8.090   0.30 19.55  ? 90  GLN   A C    1 
ATOM   1317 O O    A GLN   A 1 110 ? 38.190 8.724   7.109   0.70 17.99  ? 90  GLN   A O    1 
ATOM   1318 O O    B GLN   A 1 110 ? 38.323 8.756   7.139   0.30 19.79  ? 90  GLN   A O    1 
ATOM   1319 C CB   A GLN   A 1 110 ? 40.063 8.742   9.358   0.70 20.60  ? 90  GLN   A CB   1 
ATOM   1320 C CB   B GLN   A 1 110 ? 40.087 8.870   9.540   0.30 22.90  ? 90  GLN   A CB   1 
ATOM   1321 C CG   A GLN   A 1 110 ? 40.640 8.185   10.608  0.70 24.36  ? 90  GLN   A CG   1 
ATOM   1322 C CG   B GLN   A 1 110 ? 40.942 10.025  9.010   0.30 25.83  ? 90  GLN   A CG   1 
ATOM   1323 C CD   A GLN   A 1 110 ? 42.112 7.953   10.412  0.70 27.15  ? 90  GLN   A CD   1 
ATOM   1324 C CD   B GLN   A 1 110 ? 41.006 11.239  9.932   0.30 29.21  ? 90  GLN   A CD   1 
ATOM   1325 O OE1  A GLN   A 1 110 ? 42.562 6.845   10.038  0.70 28.99  ? 90  GLN   A OE1  1 
ATOM   1326 O OE1  B GLN   A 1 110 ? 40.416 12.279  9.645   0.30 29.62  ? 90  GLN   A OE1  1 
ATOM   1327 N NE2  A GLN   A 1 110 ? 42.883 9.022   10.570  0.70 26.65  ? 90  GLN   A NE2  1 
ATOM   1328 N NE2  B GLN   A 1 110 ? 41.779 11.129  11.009  0.30 30.34  ? 90  GLN   A NE2  1 
ATOM   1329 H H    A GLN   A 1 110 ? 37.821 7.296   9.352   0.70 22.27  ? 90  GLN   A H    1 
ATOM   1330 H H    B GLN   A 1 110 ? 37.848 7.310   9.354   0.30 23.83  ? 90  GLN   A H    1 
ATOM   1331 H HA   A GLN   A 1 110 ? 38.472 9.834   10.071  0.70 22.05  ? 90  GLN   A HA   1 
ATOM   1332 H HA   B GLN   A 1 110 ? 38.394 9.874   10.094  0.30 24.68  ? 90  GLN   A HA   1 
ATOM   1333 H HB2  A GLN   A 1 110 ? 40.176 8.076   8.662   0.70 24.72  ? 90  GLN   A HB2  1 
ATOM   1334 H HB2  B GLN   A 1 110 ? 40.345 8.710   10.461  0.30 27.49  ? 90  GLN   A HB2  1 
ATOM   1335 H HB3  A GLN   A 1 110 ? 40.562 9.543   9.137   0.70 24.72  ? 90  GLN   A HB3  1 
ATOM   1336 H HB3  B GLN   A 1 110 ? 40.281 8.088   9.000   0.30 27.49  ? 90  GLN   A HB3  1 
ATOM   1337 H HG2  A GLN   A 1 110 ? 40.514 8.812   11.337  0.70 29.23  ? 90  GLN   A HG2  1 
ATOM   1338 H HG2  B GLN   A 1 110 ? 41.849 9.705   8.884   0.30 30.99  ? 90  GLN   A HG2  1 
ATOM   1339 H HG3  A GLN   A 1 110 ? 40.214 7.340   10.820  0.70 29.23  ? 90  GLN   A HG3  1 
ATOM   1340 H HG3  B GLN   A 1 110 ? 40.573 10.320  8.163   0.30 30.99  ? 90  GLN   A HG3  1 
ATOM   1341 H HE21 A GLN   A 1 110 ? 42.531 9.780   10.771  0.70 31.99  ? 90  GLN   A HE21 1 
ATOM   1342 H HE21 B GLN   A 1 110 ? 42.211 10.401  11.156  0.30 36.41  ? 90  GLN   A HE21 1 
ATOM   1343 H HE22 A GLN   A 1 110 ? 43.735 8.956   10.472  0.70 31.99  ? 90  GLN   A HE22 1 
ATOM   1344 H HE22 B GLN   A 1 110 ? 41.847 11.788  11.558  0.30 36.41  ? 90  GLN   A HE22 1 
ATOM   1345 N N    . ILE   A 1 111 ? 37.548 10.712  7.967   1.00 19.09  ? 91  ILE   A N    1 
ATOM   1346 C CA   . ILE   A 1 111 ? 36.991 11.192  6.714   1.00 19.86  ? 91  ILE   A CA   1 
ATOM   1347 C C    . ILE   A 1 111 ? 38.012 12.098  6.042   1.00 19.41  ? 91  ILE   A C    1 
ATOM   1348 O O    . ILE   A 1 111 ? 38.530 13.036  6.662   1.00 22.21  ? 91  ILE   A O    1 
ATOM   1349 C CB   . ILE   A 1 111 ? 35.665 11.934  6.954   1.00 20.98  ? 91  ILE   A CB   1 
ATOM   1350 C CG1  . ILE   A 1 111 ? 34.624 10.954  7.481   1.00 22.59  ? 91  ILE   A CG1  1 
ATOM   1351 C CG2  . ILE   A 1 111 ? 35.181 12.557  5.664   1.00 23.42  ? 91  ILE   A CG2  1 
ATOM   1352 C CD1  . ILE   A 1 111 ? 33.334 11.614  7.913   1.00 25.41  ? 91  ILE   A CD1  1 
ATOM   1353 H H    A ILE   A 1 111 ? 37.487 11.271  8.618   0.70 22.91  ? 91  ILE   A H    1 
ATOM   1354 H H    B ILE   A 1 111 ? 37.458 11.269  8.617   0.30 22.91  ? 91  ILE   A H    1 
ATOM   1355 H HA   . ILE   A 1 111 ? 36.822 10.440  6.126   1.00 23.84  ? 91  ILE   A HA   1 
ATOM   1356 H HB   . ILE   A 1 111 ? 35.808 12.635  7.608   1.00 25.18  ? 91  ILE   A HB   1 
ATOM   1357 H HG12 . ILE   A 1 111 ? 34.411 10.318  6.780   1.00 27.11  ? 91  ILE   A HG12 1 
ATOM   1358 H HG13 . ILE   A 1 111 ? 34.992 10.491  8.249   1.00 27.11  ? 91  ILE   A HG13 1 
ATOM   1359 H HG21 . ILE   A 1 111 ? 34.274 12.878  5.789   1.00 28.11  ? 91  ILE   A HG21 1 
ATOM   1360 H HG22 . ILE   A 1 111 ? 35.764 13.297  5.432   1.00 28.11  ? 91  ILE   A HG22 1 
ATOM   1361 H HG23 . ILE   A 1 111 ? 35.201 11.888  4.962   1.00 28.11  ? 91  ILE   A HG23 1 
ATOM   1362 H HD11 . ILE   A 1 111 ? 32.822 10.987  8.447   1.00 30.49  ? 91  ILE   A HD11 1 
ATOM   1363 H HD12 . ILE   A 1 111 ? 33.544 12.402  8.439   1.00 30.49  ? 91  ILE   A HD12 1 
ATOM   1364 H HD13 . ILE   A 1 111 ? 32.829 11.867  7.125   1.00 30.49  ? 91  ILE   A HD13 1 
ATOM   1365 N N    . PHE   A 1 112 ? 38.262 11.842  4.759   1.00 18.33  ? 92  PHE   A N    1 
ATOM   1366 C CA   . PHE   A 1 112 ? 39.190 12.621  3.951   1.00 18.79  ? 92  PHE   A CA   1 
ATOM   1367 C C    . PHE   A 1 112 ? 38.427 13.344  2.846   1.00 19.07  ? 92  PHE   A C    1 
ATOM   1368 O O    . PHE   A 1 112 ? 37.864 12.698  1.951   1.00 19.02  ? 92  PHE   A O    1 
ATOM   1369 C CB   . PHE   A 1 112 ? 40.262 11.723  3.360   1.00 18.46  ? 92  PHE   A CB   1 
ATOM   1370 C CG   . PHE   A 1 112 ? 41.079 11.018  4.385   1.00 19.33  ? 92  PHE   A CG   1 
ATOM   1371 C CD1  . PHE   A 1 112 ? 42.194 11.641  4.925   1.00 20.34  ? 92  PHE   A CD1  1 
ATOM   1372 C CD2  . PHE   A 1 112 ? 40.752 9.733   4.820   1.00 20.96  ? 92  PHE   A CD2  1 
ATOM   1373 C CE1  . PHE   A 1 112 ? 42.967 11.011  5.880   1.00 21.85  ? 92  PHE   A CE1  1 
ATOM   1374 C CE2  . PHE   A 1 112 ? 41.522 9.107   5.782   1.00 21.97  ? 92  PHE   A CE2  1 
ATOM   1375 C CZ   . PHE   A 1 112 ? 42.654 9.755   6.292   1.00 22.19  ? 92  PHE   A CZ   1 
ATOM   1376 H H    . PHE   A 1 112 ? 37.892 11.200  4.323   1.00 22.00  ? 92  PHE   A H    1 
ATOM   1377 H HA   . PHE   A 1 112 ? 39.604 13.294  4.514   1.00 22.55  ? 92  PHE   A HA   1 
ATOM   1378 H HB2  . PHE   A 1 112 ? 39.836 11.050  2.806   1.00 22.15  ? 92  PHE   A HB2  1 
ATOM   1379 H HB3  . PHE   A 1 112 ? 40.862 12.263  2.823   1.00 22.15  ? 92  PHE   A HB3  1 
ATOM   1380 H HD1  . PHE   A 1 112 ? 42.424 12.496  4.640   1.00 24.41  ? 92  PHE   A HD1  1 
ATOM   1381 H HD2  . PHE   A 1 112 ? 40.014 9.295   4.461   1.00 25.16  ? 92  PHE   A HD2  1 
ATOM   1382 H HE1  . PHE   A 1 112 ? 43.704 11.448  6.242   1.00 26.22  ? 92  PHE   A HE1  1 
ATOM   1383 H HE2  . PHE   A 1 112 ? 41.290 8.261   6.090   1.00 26.36  ? 92  PHE   A HE2  1 
ATOM   1384 H HZ   . PHE   A 1 112 ? 43.194 9.324   6.915   1.00 26.63  ? 92  PHE   A HZ   1 
ATOM   1385 N N    . GLU   A 1 113 ? 38.391 14.684  2.929   1.00 20.65  ? 93  GLU   A N    1 
ATOM   1386 C CA   . GLU   A 1 113 ? 38.010 15.486  1.791   1.00 22.47  ? 93  GLU   A CA   1 
ATOM   1387 C C    . GLU   A 1 113 ? 39.121 15.419  0.756   1.00 20.67  ? 93  GLU   A C    1 
ATOM   1388 O O    . GLU   A 1 113 ? 40.231 14.970  1.040   1.00 22.72  ? 93  GLU   A O    1 
ATOM   1389 C CB   . GLU   A 1 113 ? 37.871 16.943  2.210   1.00 28.89  ? 93  GLU   A CB   1 
ATOM   1390 C CG   . GLU   A 1 113 ? 37.069 17.120  3.451   1.00 35.38  ? 93  GLU   A CG   1 
ATOM   1391 C CD   . GLU   A 1 113 ? 37.144 18.534  4.014   1.00 40.87  ? 93  GLU   A CD   1 
ATOM   1392 O OE1  . GLU   A 1 113 ? 38.005 19.336  3.584   1.00 40.91  ? 93  GLU   A OE1  1 
ATOM   1393 O OE2  . GLU   A 1 113 ? 36.342 18.822  4.912   1.00 45.76  ? 93  GLU   A OE2  1 
ATOM   1394 H H    . GLU   A 1 113 ? 38.583 15.136  3.635   1.00 24.79  ? 93  GLU   A H    1 
ATOM   1395 H HA   . GLU   A 1 113 ? 37.171 15.168  1.424   1.00 26.96  ? 93  GLU   A HA   1 
ATOM   1396 H HB2  . GLU   A 1 113 ? 38.754 17.310  2.370   1.00 34.67  ? 93  GLU   A HB2  1 
ATOM   1397 H HB3  . GLU   A 1 113 ? 37.432 17.434  1.498   1.00 34.67  ? 93  GLU   A HB3  1 
ATOM   1398 H HG2  . GLU   A 1 113 ? 36.139 16.926  3.256   1.00 42.46  ? 93  GLU   A HG2  1 
ATOM   1399 H HG3  . GLU   A 1 113 ? 37.400 16.511  4.130   1.00 42.46  ? 93  GLU   A HG3  1 
ATOM   1400 N N    . THR   A 1 114 ? 38.817 15.813  -0.469  1.00 21.67  ? 94  THR   A N    1 
ATOM   1401 C CA   . THR   A 1 114 ? 39.828 15.803  -1.526  1.00 21.33  ? 94  THR   A CA   1 
ATOM   1402 C C    . THR   A 1 114 ? 39.730 17.105  -2.313  1.00 21.91  ? 94  THR   A C    1 
ATOM   1403 O O    . THR   A 1 114 ? 38.865 17.945  -2.054  1.00 23.69  ? 94  THR   A O    1 
ATOM   1404 C CB   . THR   A 1 114 ? 39.704 14.605  -2.481  1.00 20.27  ? 94  THR   A CB   1 
ATOM   1405 O OG1  . THR   A 1 114 ? 38.649 14.817  -3.426  1.00 20.47  ? 94  THR   A OG1  1 
ATOM   1406 C CG2  . THR   A 1 114 ? 39.525 13.276  -1.736  1.00 20.01  ? 94  THR   A CG2  1 
ATOM   1407 H H    . THR   A 1 114 ? 38.041 16.089  -0.716  1.00 26.01  ? 94  THR   A H    1 
ATOM   1408 H HA   . THR   A 1 114 ? 40.691 15.742  -1.087  1.00 25.60  ? 94  THR   A HA   1 
ATOM   1409 H HB   . THR   A 1 114 ? 40.536 14.526  -2.973  1.00 24.32  ? 94  THR   A HB   1 
ATOM   1410 H HG1  . THR   A 1 114 ? 37.921 14.928  -3.023  1.00 24.56  ? 94  THR   A HG1  1 
ATOM   1411 H HG21 . THR   A 1 114 ? 39.521 12.539  -2.367  1.00 24.02  ? 94  THR   A HG21 1 
ATOM   1412 H HG22 . THR   A 1 114 ? 40.252 13.148  -1.106  1.00 24.02  ? 94  THR   A HG22 1 
ATOM   1413 H HG23 . THR   A 1 114 ? 38.685 13.278  -1.250  1.00 24.02  ? 94  THR   A HG23 1 
ATOM   1414 N N    . GLN   A 1 115 ? 40.575 17.251  -3.334  1.00 22.86  ? 95  GLN   A N    1 
ATOM   1415 C CA   . GLN   A 1 115 ? 40.494 18.433  -4.180  1.00 23.68  ? 95  GLN   A CA   1 
ATOM   1416 C C    . GLN   A 1 115 ? 39.198 18.477  -4.974  1.00 24.44  ? 95  GLN   A C    1 
ATOM   1417 O O    . GLN   A 1 115 ? 38.816 19.539  -5.469  1.00 26.39  ? 95  GLN   A O    1 
ATOM   1418 C CB   . GLN   A 1 115 ? 41.682 18.521  -5.141  1.00 24.06  ? 95  GLN   A CB   1 
ATOM   1419 C CG   . GLN   A 1 115 ? 41.749 17.445  -6.219  1.00 23.85  ? 95  GLN   A CG   1 
ATOM   1420 C CD   . GLN   A 1 115 ? 42.528 16.218  -5.808  1.00 25.76  ? 95  GLN   A CD   1 
ATOM   1421 O OE1  . GLN   A 1 115 ? 42.553 15.825  -4.649  1.00 24.62  ? 95  GLN   A OE1  1 
ATOM   1422 N NE2  . GLN   A 1 115 ? 43.216 15.641  -6.768  1.00 29.75  ? 95  GLN   A NE2  1 
ATOM   1423 H H    . GLN   A 1 115 ? 41.190 16.691  -3.551  1.00 27.44  ? 95  GLN   A H    1 
ATOM   1424 H HA   . GLN   A 1 115 ? 40.536 19.210  -3.602  1.00 28.42  ? 95  GLN   A HA   1 
ATOM   1425 H HB2  . GLN   A 1 115 ? 41.642 19.378  -5.594  1.00 28.88  ? 95  GLN   A HB2  1 
ATOM   1426 H HB3  . GLN   A 1 115 ? 42.498 18.458  -4.622  1.00 28.88  ? 95  GLN   A HB3  1 
ATOM   1427 H HG2  . GLN   A 1 115 ? 40.846 17.163  -6.435  1.00 28.62  ? 95  GLN   A HG2  1 
ATOM   1428 H HG3  . GLN   A 1 115 ? 42.177 17.817  -7.005  1.00 28.62  ? 95  GLN   A HG3  1 
ATOM   1429 H HE21 . GLN   A 1 115 ? 43.200 15.966  -7.563  1.00 35.71  ? 95  GLN   A HE21 1 
ATOM   1430 H HE22 . GLN   A 1 115 ? 43.681 14.937  -6.600  1.00 35.71  ? 95  GLN   A HE22 1 
ATOM   1431 N N    . ASP   A 1 116 ? 38.525 17.336  -5.131  1.00 24.05  ? 96  ASP   A N    1 
ATOM   1432 C CA   . ASP   A 1 116 ? 37.227 17.279  -5.786  1.00 25.23  ? 96  ASP   A CA   1 
ATOM   1433 C C    . ASP   A 1 116 ? 36.194 17.430  -4.680  1.00 23.96  ? 96  ASP   A C    1 
ATOM   1434 O O    . ASP   A 1 116 ? 36.104 16.551  -3.804  1.00 24.18  ? 96  ASP   A O    1 
ATOM   1435 C CB   . ASP   A 1 116 ? 37.075 15.921  -6.463  1.00 24.37  ? 96  ASP   A CB   1 
ATOM   1436 C CG   . ASP   A 1 116 ? 35.787 15.773  -7.230  1.00 26.32  ? 96  ASP   A CG   1 
ATOM   1437 O OD1  . ASP   A 1 116 ? 34.826 16.537  -6.980  1.00 25.69  ? 96  ASP   A OD1  1 
ATOM   1438 O OD2  . ASP   A 1 116 ? 35.745 14.843  -8.082  1.00 27.58  ? 96  ASP   A OD2  1 
ATOM   1439 H H    . ASP   A 1 116 ? 38.807 16.570  -4.859  1.00 28.87  ? 96  ASP   A H    1 
ATOM   1440 H HA   . ASP   A 1 116 ? 37.116 17.979  -6.449  1.00 30.27  ? 96  ASP   A HA   1 
ATOM   1441 H HB2  . ASP   A 1 116 ? 37.808 15.798  -7.087  1.00 29.25  ? 96  ASP   A HB2  1 
ATOM   1442 H HB3  . ASP   A 1 116 ? 37.098 15.229  -5.785  1.00 29.25  ? 96  ASP   A HB3  1 
ATOM   1443 N N    . PRO   A 1 117 ? 35.422 18.519  -4.650  1.00 24.12  ? 97  PRO   A N    1 
ATOM   1444 C CA   . PRO   A 1 117 ? 34.437 18.683  -3.566  1.00 23.63  ? 97  PRO   A CA   1 
ATOM   1445 C C    . PRO   A 1 117 ? 33.404 17.588  -3.522  1.00 23.20  ? 97  PRO   A C    1 
ATOM   1446 O O    . PRO   A 1 117 ? 32.739 17.438  -2.491  1.00 23.72  ? 97  PRO   A O    1 
ATOM   1447 C CB   . PRO   A 1 117 ? 33.785 20.035  -3.878  1.00 25.72  ? 97  PRO   A CB   1 
ATOM   1448 C CG   . PRO   A 1 117 ? 33.980 20.196  -5.341  1.00 27.69  ? 97  PRO   A CG   1 
ATOM   1449 C CD   . PRO   A 1 117 ? 35.327 19.595  -5.647  1.00 25.82  ? 97  PRO   A CD   1 
ATOM   1450 H HA   . PRO   A 1 117 ? 34.896 18.733  -2.713  1.00 28.36  ? 97  PRO   A HA   1 
ATOM   1451 H HB2  . PRO   A 1 117 ? 32.843 20.013  -3.649  1.00 30.87  ? 97  PRO   A HB2  1 
ATOM   1452 H HB3  . PRO   A 1 117 ? 34.229 20.742  -3.384  1.00 30.87  ? 97  PRO   A HB3  1 
ATOM   1453 H HG2  . PRO   A 1 117 ? 33.278 19.726  -5.817  1.00 33.22  ? 97  PRO   A HG2  1 
ATOM   1454 H HG3  . PRO   A 1 117 ? 33.964 21.138  -5.571  1.00 33.22  ? 97  PRO   A HG3  1 
ATOM   1455 H HD2  . PRO   A 1 117 ? 35.353 19.238  -6.549  1.00 30.99  ? 97  PRO   A HD2  1 
ATOM   1456 H HD3  . PRO   A 1 117 ? 36.036 20.246  -5.527  1.00 30.99  ? 97  PRO   A HD3  1 
ATOM   1457 N N    . ASN   A 1 118 ? 33.245 16.824  -4.604  1.00 22.02  ? 98  ASN   A N    1 
ATOM   1458 C CA   . ASN   A 1 118 ? 32.279 15.744  -4.684  1.00 22.79  ? 98  ASN   A CA   1 
ATOM   1459 C C    . ASN   A 1 118 ? 32.907 14.365  -4.518  1.00 21.87  ? 98  ASN   A C    1 
ATOM   1460 O O    . ASN   A 1 118 ? 32.248 13.376  -4.834  1.00 22.51  ? 98  ASN   A O    1 
ATOM   1461 C CB   . ASN   A 1 118 ? 31.541 15.838  -6.012  1.00 24.70  ? 98  ASN   A CB   1 
ATOM   1462 C CG   . ASN   A 1 118 ? 30.651 17.050  -6.078  1.00 27.05  ? 98  ASN   A CG   1 
ATOM   1463 O OD1  . ASN   A 1 118 ? 29.821 17.236  -5.210  1.00 28.98  ? 98  ASN   A OD1  1 
ATOM   1464 N ND2  . ASN   A 1 118 ? 30.880 17.906  -7.057  1.00 28.78  ? 98  ASN   A ND2  1 
ATOM   1465 H H    . ASN   A 1 118 ? 33.703 16.921  -5.325  1.00 26.42  ? 98  ASN   A H    1 
ATOM   1466 H HA   . ASN   A 1 118 ? 31.638 15.844  -3.963  1.00 27.35  ? 98  ASN   A HA   1 
ATOM   1467 H HB2  . ASN   A 1 118 ? 32.187 15.897  -6.733  1.00 29.64  ? 98  ASN   A HB2  1 
ATOM   1468 H HB3  . ASN   A 1 118 ? 30.988 15.049  -6.126  1.00 29.64  ? 98  ASN   A HB3  1 
ATOM   1469 H HD21 . ASN   A 1 118 ? 30.395 18.613  -7.132  1.00 34.54  ? 98  ASN   A HD21 1 
ATOM   1470 H HD22 . ASN   A 1 118 ? 31.514 17.758  -7.619  1.00 34.54  ? 98  ASN   A HD22 1 
ATOM   1471 N N    . TRP   A 1 119 ? 34.138 14.272  -4.017  1.00 20.71  ? 99  TRP   A N    1 
ATOM   1472 C CA   . TRP   A 1 119 ? 34.788 12.976  -3.832  1.00 19.06  ? 99  TRP   A CA   1 
ATOM   1473 C C    . TRP   A 1 119 ? 35.449 12.937  -2.464  1.00 18.39  ? 99  TRP   A C    1 
ATOM   1474 O O    . TRP   A 1 119 ? 36.275 13.793  -2.147  1.00 19.97  ? 99  TRP   A O    1 
ATOM   1475 C CB   . TRP   A 1 119 ? 35.812 12.711  -4.928  1.00 19.34  ? 99  TRP   A CB   1 
ATOM   1476 C CG   . TRP   A 1 119 ? 36.139 11.235  -5.153  1.00 18.79  ? 99  TRP   A CG   1 
ATOM   1477 C CD1  . TRP   A 1 119 ? 36.075 10.183  -4.248  1.00 18.33  ? 99  TRP   A CD1  1 
ATOM   1478 C CD2  . TRP   A 1 119 ? 36.545 10.654  -6.406  1.00 19.37  ? 99  TRP   A CD2  1 
ATOM   1479 N NE1  . TRP   A 1 119 ? 36.454 9.010   -4.882  1.00 18.07  ? 99  TRP   A NE1  1 
ATOM   1480 C CE2  . TRP   A 1 119 ? 36.716 9.273   -6.201  1.00 18.73  ? 99  TRP   A CE2  1 
ATOM   1481 C CE3  . TRP   A 1 119 ? 36.763 11.178  -7.687  1.00 20.81  ? 99  TRP   A CE3  1 
ATOM   1482 C CZ2  . TRP   A 1 119 ? 37.133 8.428   -7.214  1.00 20.72  ? 99  TRP   A CZ2  1 
ATOM   1483 C CZ3  . TRP   A 1 119 ? 37.149 10.335  -8.694  1.00 23.43  ? 99  TRP   A CZ3  1 
ATOM   1484 C CH2  . TRP   A 1 119 ? 37.333 8.971   -8.453  1.00 22.67  ? 99  TRP   A CH2  1 
ATOM   1485 H H    . TRP   A 1 119 ? 34.617 14.945  -3.778  1.00 24.85  ? 99  TRP   A H    1 
ATOM   1486 H HA   . TRP   A 1 119 ? 34.115 12.279  -3.861  1.00 22.87  ? 99  TRP   A HA   1 
ATOM   1487 H HB2  . TRP   A 1 119 ? 35.469 13.064  -5.764  1.00 23.22  ? 99  TRP   A HB2  1 
ATOM   1488 H HB3  . TRP   A 1 119 ? 36.639 13.160  -4.693  1.00 23.22  ? 99  TRP   A HB3  1 
ATOM   1489 H HD1  . TRP   A 1 119 ? 35.819 10.254  -3.357  1.00 22.00  ? 99  TRP   A HD1  1 
ATOM   1490 H HE1  . TRP   A 1 119 ? 36.515 8.239   -4.507  1.00 21.69  ? 99  TRP   A HE1  1 
ATOM   1491 H HE3  . TRP   A 1 119 ? 36.647 12.086  -7.850  1.00 24.98  ? 99  TRP   A HE3  1 
ATOM   1492 H HZ2  . TRP   A 1 119 ? 37.273 7.522   -7.057  1.00 24.87  ? 99  TRP   A HZ2  1 
ATOM   1493 H HZ3  . TRP   A 1 119 ? 37.291 10.675  -9.549  1.00 28.12  ? 99  TRP   A HZ3  1 
ATOM   1494 H HH2  . TRP   A 1 119 ? 37.598 8.418   -9.153  1.00 27.20  ? 99  TRP   A HH2  1 
ATOM   1495 N N    . PHE   A 1 120 ? 35.069 11.942  -1.653  1.00 18.59  ? 100 PHE   A N    1 
ATOM   1496 C CA   . PHE   A 1 120 ? 35.605 11.743  -0.319  1.00 18.11  ? 100 PHE   A CA   1 
ATOM   1497 C C    . PHE   A 1 120 ? 36.086 10.311  -0.199  1.00 17.27  ? 100 PHE   A C    1 
ATOM   1498 O O    . PHE   A 1 120 ? 35.560 9.406   -0.857  1.00 18.07  ? 100 PHE   A O    1 
ATOM   1499 C CB   . PHE   A 1 120 ? 34.551 11.929  0.766   1.00 18.83  ? 100 PHE   A CB   1 
ATOM   1500 C CG   . PHE   A 1 120 ? 34.130 13.351  0.971   1.00 20.38  ? 100 PHE   A CG   1 
ATOM   1501 C CD1  . PHE   A 1 120 ? 33.402 14.033  0.006   1.00 23.73  ? 100 PHE   A CD1  1 
ATOM   1502 C CD2  . PHE   A 1 120 ? 34.489 14.029  2.126   1.00 22.12  ? 100 PHE   A CD2  1 
ATOM   1503 C CE1  . PHE   A 1 120 ? 33.053 15.343  0.186   1.00 26.86  ? 100 PHE   A CE1  1 
ATOM   1504 C CE2  . PHE   A 1 120 ? 34.129 15.353  2.313   1.00 24.27  ? 100 PHE   A CE2  1 
ATOM   1505 C CZ   . PHE   A 1 120 ? 33.415 15.990  1.339   1.00 24.79  ? 100 PHE   A CZ   1 
ATOM   1506 H H    . PHE   A 1 120 ? 34.481 11.353  -1.869  1.00 22.31  ? 100 PHE   A H    1 
ATOM   1507 H HA   . PHE   A 1 120 ? 36.328 12.375  -0.183  1.00 21.74  ? 100 PHE   A HA   1 
ATOM   1508 H HB2  . PHE   A 1 120 ? 33.762 11.420  0.523   1.00 22.60  ? 100 PHE   A HB2  1 
ATOM   1509 H HB3  . PHE   A 1 120 ? 34.909 11.604  1.607   1.00 22.60  ? 100 PHE   A HB3  1 
ATOM   1510 H HD1  . PHE   A 1 120 ? 33.148 13.593  -0.773  1.00 28.48  ? 100 PHE   A HD1  1 
ATOM   1511 H HD2  . PHE   A 1 120 ? 34.977 13.588  2.784   1.00 26.54  ? 100 PHE   A HD2  1 
ATOM   1512 H HE1  . PHE   A 1 120 ? 32.573 15.793  -0.471  1.00 32.23  ? 100 PHE   A HE1  1 
ATOM   1513 H HE2  . PHE   A 1 120 ? 34.371 15.803  3.090   1.00 29.12  ? 100 PHE   A HE2  1 
ATOM   1514 H HZ   . PHE   A 1 120 ? 33.168 16.878  1.461   1.00 29.75  ? 100 PHE   A HZ   1 
ATOM   1515 N N    . TRP   A 1 121 ? 37.047 10.107  0.693   1.00 16.53  ? 101 TRP   A N    1 
ATOM   1516 C CA   . TRP   A 1 121 ? 37.494 8.780   1.089   1.00 15.72  ? 101 TRP   A CA   1 
ATOM   1517 C C    . TRP   A 1 121 ? 37.371 8.661   2.599   1.00 16.73  ? 101 TRP   A C    1 
ATOM   1518 O O    . TRP   A 1 121 ? 37.495 9.651   3.321   1.00 19.08  ? 101 TRP   A O    1 
ATOM   1519 C CB   . TRP   A 1 121 ? 38.976 8.526   0.686   1.00 16.57  ? 101 TRP   A CB   1 
ATOM   1520 C CG   . TRP   A 1 121 ? 39.114 8.377   -0.794  1.00 16.26  ? 101 TRP   A CG   1 
ATOM   1521 C CD1  . TRP   A 1 121 ? 39.317 9.373   -1.705  1.00 17.81  ? 101 TRP   A CD1  1 
ATOM   1522 C CD2  . TRP   A 1 121 ? 39.054 7.150   -1.547  1.00 15.92  ? 101 TRP   A CD2  1 
ATOM   1523 N NE1  . TRP   A 1 121 ? 39.357 8.853   -2.975  1.00 18.04  ? 101 TRP   A NE1  1 
ATOM   1524 C CE2  . TRP   A 1 121 ? 39.199 7.487   -2.904  1.00 16.72  ? 101 TRP   A CE2  1 
ATOM   1525 C CE3  . TRP   A 1 121 ? 38.880 5.800   -1.205  1.00 16.52  ? 101 TRP   A CE3  1 
ATOM   1526 C CZ2  . TRP   A 1 121 ? 39.185 6.513   -3.918  1.00 16.64  ? 101 TRP   A CZ2  1 
ATOM   1527 C CZ3  . TRP   A 1 121 ? 38.904 4.852   -2.205  1.00 15.92  ? 101 TRP   A CZ3  1 
ATOM   1528 C CH2  . TRP   A 1 121 ? 39.037 5.206   -3.535  1.00 16.27  ? 101 TRP   A CH2  1 
ATOM   1529 H H    . TRP   A 1 121 ? 37.468 10.741  1.093   1.00 19.84  ? 101 TRP   A H    1 
ATOM   1530 H HA   . TRP   A 1 121 ? 36.944 8.107   0.658   1.00 18.87  ? 101 TRP   A HA   1 
ATOM   1531 H HB2  . TRP   A 1 121 ? 39.520 9.276   0.971   1.00 19.88  ? 101 TRP   A HB2  1 
ATOM   1532 H HB3  . TRP   A 1 121 ? 39.289 7.710   1.107   1.00 19.88  ? 101 TRP   A HB3  1 
ATOM   1533 H HD1  . TRP   A 1 121 ? 39.414 10.274  -1.496  1.00 21.37  ? 101 TRP   A HD1  1 
ATOM   1534 H HE1  . TRP   A 1 121 ? 39.464 9.307   -3.698  1.00 21.65  ? 101 TRP   A HE1  1 
ATOM   1535 H HE3  . TRP   A 1 121 ? 38.750 5.550   -0.319  1.00 19.83  ? 101 TRP   A HE3  1 
ATOM   1536 H HZ2  . TRP   A 1 121 ? 39.274 6.747   -4.814  1.00 19.97  ? 101 TRP   A HZ2  1 
ATOM   1537 H HZ3  . TRP   A 1 121 ? 38.829 3.953   -1.980  1.00 19.10  ? 101 TRP   A HZ3  1 
ATOM   1538 H HH2  . TRP   A 1 121 ? 39.026 4.541   -4.185  1.00 19.52  ? 101 TRP   A HH2  1 
ATOM   1539 N N    . VAL   A 1 122 ? 37.097 7.456   3.083   1.00 15.62  ? 102 VAL   A N    1 
ATOM   1540 C CA   . VAL   A 1 122 ? 36.993 7.191   4.512   1.00 14.98  ? 102 VAL   A CA   1 
ATOM   1541 C C    . VAL   A 1 122 ? 37.848 5.976   4.823   1.00 15.48  ? 102 VAL   A C    1 
ATOM   1542 O O    . VAL   A 1 122 ? 37.727 4.947   4.156   1.00 16.95  ? 102 VAL   A O    1 
ATOM   1543 C CB   . VAL   A 1 122 ? 35.536 6.913   4.918   1.00 16.09  ? 102 VAL   A CB   1 
ATOM   1544 C CG1  . VAL   A 1 122 ? 35.460 6.618   6.361   1.00 18.24  ? 102 VAL   A CG1  1 
ATOM   1545 C CG2  . VAL   A 1 122 ? 34.669 8.117   4.595   1.00 17.24  ? 102 VAL   A CG2  1 
ATOM   1546 H H    . VAL   A 1 122 ? 36.965 6.762   2.593   1.00 18.74  ? 102 VAL   A H    1 
ATOM   1547 H HA   . VAL   A 1 122 ? 37.326 7.952   5.013   1.00 17.98  ? 102 VAL   A HA   1 
ATOM   1548 H HB   . VAL   A 1 122 ? 35.208 6.146   4.423   1.00 19.31  ? 102 VAL   A HB   1 
ATOM   1549 H HG11 . VAL   A 1 122 ? 34.532 6.648   6.641   1.00 21.90  ? 102 VAL   A HG11 1 
ATOM   1550 H HG12 . VAL   A 1 122 ? 35.826 5.734   6.521   1.00 21.90  ? 102 VAL   A HG12 1 
ATOM   1551 H HG13 . VAL   A 1 122 ? 35.974 7.282   6.846   1.00 21.90  ? 102 VAL   A HG13 1 
ATOM   1552 H HG21 . VAL   A 1 122 ? 33.762 7.943   4.893   1.00 20.69  ? 102 VAL   A HG21 1 
ATOM   1553 H HG22 . VAL   A 1 122 ? 35.024 8.895   5.054   1.00 20.69  ? 102 VAL   A HG22 1 
ATOM   1554 H HG23 . VAL   A 1 122 ? 34.680 8.266   3.637   1.00 20.69  ? 102 VAL   A HG23 1 
ATOM   1555 N N    . GLU   A 1 123 ? 38.682 6.082   5.843   1.00 15.06  ? 103 GLU   A N    1 
ATOM   1556 C CA   . GLU   A 1 123 ? 39.351 4.937   6.426   1.00 15.25  ? 103 GLU   A CA   1 
ATOM   1557 C C    . GLU   A 1 123 ? 38.676 4.628   7.758   1.00 15.87  ? 103 GLU   A C    1 
ATOM   1558 O O    . GLU   A 1 123 ? 38.417 5.527   8.548   1.00 17.03  ? 103 GLU   A O    1 
ATOM   1559 C CB   . GLU   A 1 123 ? 40.854 5.221   6.600   1.00 15.02  ? 103 GLU   A CB   1 
ATOM   1560 C CG   . GLU   A 1 123 ? 41.575 4.043   7.221   1.00 16.18  ? 103 GLU   A CG   1 
ATOM   1561 C CD   . GLU   A 1 123 ? 43.081 4.160   7.341   1.00 18.28  ? 103 GLU   A CD   1 
ATOM   1562 O OE1  . GLU   A 1 123 ? 43.658 5.252   7.151   1.00 18.50  ? 103 GLU   A OE1  1 
ATOM   1563 O OE2  . GLU   A 1 123 ? 43.684 3.101   7.632   1.00 19.45  ? 103 GLU   A OE2  1 
ATOM   1564 H H    . GLU   A 1 123 ? 38.881 6.827   6.223   1.00 18.07  ? 103 GLU   A H    1 
ATOM   1565 H HA   . GLU   A 1 123 ? 39.272 4.154   5.858   1.00 18.30  ? 103 GLU   A HA   1 
ATOM   1566 H HB2  . GLU   A 1 123 ? 41.249 5.398   5.732   1.00 18.02  ? 103 GLU   A HB2  1 
ATOM   1567 H HB3  . GLU   A 1 123 ? 40.969 5.990   7.180   1.00 18.02  ? 103 GLU   A HB3  1 
ATOM   1568 H HG2  . GLU   A 1 123 ? 41.228 3.915   8.118   1.00 19.42  ? 103 GLU   A HG2  1 
ATOM   1569 H HG3  . GLU   A 1 123 ? 41.393 3.259   6.680   1.00 19.42  ? 103 GLU   A HG3  1 
ATOM   1570 N N    . CYS   A 1 124 ? 38.339 3.365   7.986   1.00 15.08  ? 104 CYS   A N    1 
ATOM   1571 C CA   . CYS   A 1 124 ? 37.660 3.010   9.218   1.00 15.40  ? 104 CYS   A CA   1 
ATOM   1572 C C    . CYS   A 1 124 ? 37.851 1.535   9.490   1.00 15.80  ? 104 CYS   A C    1 
ATOM   1573 O O    . CYS   A 1 124 ? 38.508 0.815   8.732   1.00 15.92  ? 104 CYS   A O    1 
ATOM   1574 C CB   . CYS   A 1 124 ? 36.162 3.338   9.122   1.00 16.14  ? 104 CYS   A CB   1 
ATOM   1575 S SG   . CYS   A 1 124 ? 35.244 2.352   7.933   1.00 17.32  ? 104 CYS   A SG   1 
ATOM   1576 H H    . CYS   A 1 124 ? 38.491 2.709   7.451   1.00 18.09  ? 104 CYS   A H    1 
ATOM   1577 H HA   . CYS   A 1 124 ? 38.065 3.511   9.943   1.00 18.48  ? 104 CYS   A HA   1 
ATOM   1578 H HB2  . CYS   A 1 124 ? 35.760 3.194   9.992   1.00 19.37  ? 104 CYS   A HB2  1 
ATOM   1579 H HB3  . CYS   A 1 124 ? 36.068 4.268   8.862   1.00 19.37  ? 104 CYS   A HB3  1 
ATOM   1580 H HG   . CYS   A 1 124 ? 34.073 2.591   8.048   1.00 20.79  ? 104 CYS   A HG   1 
ATOM   1581 N N    . ARG   A 1 125 ? 37.291 1.096   10.597  1.00 15.55  ? 105 ARG   A N    1 
ATOM   1582 C CA   . ARG   A 1 125 ? 37.091 -0.320  10.859  1.00 15.23  ? 105 ARG   A CA   1 
ATOM   1583 C C    . ARG   A 1 125 ? 35.598 -0.602  10.951  1.00 15.25  ? 105 ARG   A C    1 
ATOM   1584 O O    . ARG   A 1 125 ? 34.784 0.314   10.993  1.00 16.53  ? 105 ARG   A O    1 
ATOM   1585 C CB   . ARG   A 1 125 ? 37.810 -0.744  12.122  1.00 16.54  ? 105 ARG   A CB   1 
ATOM   1586 C CG   . ARG   A 1 125 ? 39.326 -0.611  11.970  1.00 19.68  ? 105 ARG   A CG   1 
ATOM   1587 C CD   . ARG   A 1 125 ? 40.059 -1.181  13.140  1.00 24.56  ? 105 ARG   A CD   1 
ATOM   1588 N NE   . ARG   A 1 125 ? 39.701 -2.572  13.341  1.00 29.00  ? 105 ARG   A NE   1 
ATOM   1589 C CZ   . ARG   A 1 125 ? 40.157 -3.604  12.645  1.00 28.93  ? 105 ARG   A CZ   1 
ATOM   1590 N NH1  . ARG   A 1 125 ? 41.213 -3.498  11.834  1.00 28.82  ? 105 ARG   A NH1  1 
ATOM   1591 N NH2  . ARG   A 1 125 ? 39.555 -4.780  12.785  1.00 26.94  ? 105 ARG   A NH2  1 
ATOM   1592 H H    . ARG   A 1 125 ? 37.010 1.608   11.228  1.00 18.66  ? 105 ARG   A H    1 
ATOM   1593 H HA   . ARG   A 1 125 ? 37.451 -0.849  10.131  1.00 18.28  ? 105 ARG   A HA   1 
ATOM   1594 H HB2  . ARG   A 1 125 ? 37.526 -0.181  12.859  1.00 19.85  ? 105 ARG   A HB2  1 
ATOM   1595 H HB3  . ARG   A 1 125 ? 37.602 -1.672  12.314  1.00 19.85  ? 105 ARG   A HB3  1 
ATOM   1596 H HG2  . ARG   A 1 125 ? 39.610 -1.087  11.174  1.00 23.62  ? 105 ARG   A HG2  1 
ATOM   1597 H HG3  . ARG   A 1 125 ? 39.558 0.328   11.896  1.00 23.62  ? 105 ARG   A HG3  1 
ATOM   1598 H HD2  . ARG   A 1 125 ? 41.014 -1.129  12.981  1.00 29.48  ? 105 ARG   A HD2  1 
ATOM   1599 H HD3  . ARG   A 1 125 ? 39.828 -0.685  13.940  1.00 29.48  ? 105 ARG   A HD3  1 
ATOM   1600 H HE   . ARG   A 1 125 ? 39.141 -2.743  13.971  1.00 34.80  ? 105 ARG   A HE   1 
ATOM   1601 H HH11 . ARG   A 1 125 ? 41.617 -2.743  11.752  1.00 34.59  ? 105 ARG   A HH11 1 
ATOM   1602 H HH12 . ARG   A 1 125 ? 41.487 -4.183  11.394  1.00 34.59  ? 105 ARG   A HH12 1 
ATOM   1603 H HH21 . ARG   A 1 125 ? 38.884 -4.859  13.318  1.00 32.33  ? 105 ARG   A HH21 1 
ATOM   1604 H HH22 . ARG   A 1 125 ? 39.835 -5.462  12.342  1.00 32.33  ? 105 ARG   A HH22 1 
ATOM   1605 N N    . GLY   A 1 126 ? 35.233 -1.873  10.881  1.00 15.30  ? 106 GLY   A N    1 
ATOM   1606 C CA   . GLY   A 1 126 ? 33.853 -2.288  11.058  1.00 15.09  ? 106 GLY   A CA   1 
ATOM   1607 C C    . GLY   A 1 126 ? 33.807 -3.558  11.873  1.00 15.03  ? 106 GLY   A C    1 
ATOM   1608 O O    . GLY   A 1 126 ? 34.738 -4.373  11.861  1.00 15.97  ? 106 GLY   A O    1 
ATOM   1609 H H    . GLY   A 1 126 ? 35.775 -2.524  10.729  1.00 18.37  ? 106 GLY   A H    1 
ATOM   1610 H HA2  . GLY   A 1 126 ? 33.355 -1.597  11.521  1.00 18.11  ? 106 GLY   A HA2  1 
ATOM   1611 H HA3  . GLY   A 1 126 ? 33.441 -2.450  10.195  1.00 18.11  ? 106 GLY   A HA3  1 
ATOM   1612 N N    . GLU   A 1 127 ? 32.681 -3.747  12.542  1.00 15.38  ? 107 GLU   A N    1 
ATOM   1613 C CA   . GLU   A 1 127 ? 32.542 -4.931  13.366  1.00 15.91  ? 107 GLU   A CA   1 
ATOM   1614 C C    . GLU   A 1 127 ? 31.077 -5.283  13.574  1.00 15.35  ? 107 GLU   A C    1 
ATOM   1615 O O    . GLU   A 1 127 ? 30.210 -4.410  13.700  1.00 16.28  ? 107 GLU   A O    1 
ATOM   1616 C CB   . GLU   A 1 127 ? 33.191 -4.737  14.739  1.00 17.22  ? 107 GLU   A CB   1 
ATOM   1617 C CG   . GLU   A 1 127 ? 32.696 -3.483  15.487  1.00 19.29  ? 107 GLU   A CG   1 
ATOM   1618 C CD   . GLU   A 1 127 ? 32.952 -3.516  16.959  1.00 22.06  ? 107 GLU   A CD   1 
ATOM   1619 O OE1  . GLU   A 1 127 ? 34.100 -3.233  17.361  1.00 23.34  ? 107 GLU   A OE1  1 
ATOM   1620 O OE2  . GLU   A 1 127 ? 31.985 -3.770  17.722  1.00 25.53  ? 107 GLU   A OE2  1 
ATOM   1621 H H    . GLU   A 1 127 ? 32.003 -3.218  12.535  1.00 18.46  ? 107 GLU   A H    1 
ATOM   1622 H HA   . GLU   A 1 127 ? 32.964 -5.664  12.891  1.00 19.09  ? 107 GLU   A HA   1 
ATOM   1623 H HB2  . GLU   A 1 127 ? 32.992 -5.509  15.290  1.00 20.67  ? 107 GLU   A HB2  1 
ATOM   1624 H HB3  . GLU   A 1 127 ? 34.151 -4.652  14.621  1.00 20.67  ? 107 GLU   A HB3  1 
ATOM   1625 H HG2  . GLU   A 1 127 ? 33.149 -2.705  15.126  1.00 23.15  ? 107 GLU   A HG2  1 
ATOM   1626 H HG3  . GLU   A 1 127 ? 31.739 -3.400  15.356  1.00 23.15  ? 107 GLU   A HG3  1 
ATOM   1627 N N    . GLY   A 1 128 ? 30.827 -6.575  13.718  1.00 16.48  ? 108 GLY   A N    1 
ATOM   1628 C CA   . GLY   A 1 128 ? 29.492 -7.045  14.048  1.00 17.09  ? 108 GLY   A CA   1 
ATOM   1629 C C    . GLY   A 1 128 ? 29.362 -8.528  13.815  1.00 16.83  ? 108 GLY   A C    1 
ATOM   1630 O O    . GLY   A 1 128 ? 30.239 -9.175  13.243  1.00 17.34  ? 108 GLY   A O    1 
ATOM   1631 H H    . GLY   A 1 128 ? 31.412 -7.199  13.630  1.00 19.78  ? 108 GLY   A H    1 
ATOM   1632 H HA2  . GLY   A 1 128 ? 29.302 -6.861  14.982  1.00 20.52  ? 108 GLY   A HA2  1 
ATOM   1633 H HA3  . GLY   A 1 128 ? 28.839 -6.586  13.497  1.00 20.52  ? 108 GLY   A HA3  1 
ATOM   1634 N N    . ALA   A 1 129 ? 28.238 -9.068  14.286  1.00 17.75  ? 109 ALA   A N    1 
ATOM   1635 C CA   . ALA   A 1 129 ? 27.897 -10.453 13.976  1.00 18.36  ? 109 ALA   A CA   1 
ATOM   1636 C C    . ALA   A 1 129 ? 27.713 -10.612 12.472  1.00 17.77  ? 109 ALA   A C    1 
ATOM   1637 O O    . ALA   A 1 129 ? 27.257 -9.700  11.781  1.00 18.05  ? 109 ALA   A O    1 
ATOM   1638 C CB   . ALA   A 1 129 ? 26.607 -10.857 14.691  1.00 19.25  ? 109 ALA   A CB   1 
ATOM   1639 H H    . ALA   A 1 129 ? 27.665 -8.660  14.781  1.00 21.30  ? 109 ALA   A H    1 
ATOM   1640 H HA   . ALA   A 1 129 ? 28.609 -11.040 14.277  1.00 22.04  ? 109 ALA   A HA   1 
ATOM   1641 H HB1  . ALA   A 1 129 ? 26.402 -11.780 14.475  1.00 23.10  ? 109 ALA   A HB1  1 
ATOM   1642 H HB2  . ALA   A 1 129 ? 26.733 -10.761 15.648  1.00 23.10  ? 109 ALA   A HB2  1 
ATOM   1643 H HB3  . ALA   A 1 129 ? 25.887 -10.280 14.392  1.00 23.10  ? 109 ALA   A HB3  1 
ATOM   1644 N N    . ILE   A 1 130 ? 28.098 -11.778 11.957  1.00 17.33  ? 110 ILE   A N    1 
ATOM   1645 C CA   . ILE   A 1 130 ? 27.836 -12.132 10.574  1.00 16.72  ? 110 ILE   A CA   1 
ATOM   1646 C C    . ILE   A 1 130 ? 26.970 -13.377 10.598  1.00 17.12  ? 110 ILE   A C    1 
ATOM   1647 O O    . ILE   A 1 130 ? 27.304 -14.362 11.272  1.00 17.91  ? 110 ILE   A O    1 
ATOM   1648 C CB   . ILE   A 1 130 ? 29.136 -12.296 9.759   1.00 17.88  ? 110 ILE   A CB   1 
ATOM   1649 C CG1  . ILE   A 1 130 ? 28.825 -12.626 8.300   1.00 18.50  ? 110 ILE   A CG1  1 
ATOM   1650 C CG2  . ILE   A 1 130 ? 30.107 -13.308 10.423  1.00 19.58  ? 110 ILE   A CG2  1 
ATOM   1651 C CD1  . ILE   A 1 130 ? 30.031 -12.491 7.365   1.00 19.15  ? 110 ILE   A CD1  1 
ATOM   1652 H H    . ILE   A 1 130 ? 28.518 -12.384 12.399  1.00 20.80  ? 110 ILE   A H    1 
ATOM   1653 H HA   . ILE   A 1 130 ? 27.329 -11.435 10.129  1.00 20.06  ? 110 ILE   A HA   1 
ATOM   1654 H HB   . ILE   A 1 130 ? 29.602 -11.445 9.757   1.00 21.46  ? 110 ILE   A HB   1 
ATOM   1655 H HG12 . ILE   A 1 130 ? 28.511 -13.542 8.248   1.00 22.21  ? 110 ILE   A HG12 1 
ATOM   1656 H HG13 . ILE   A 1 130 ? 28.136 -12.020 7.984   1.00 22.21  ? 110 ILE   A HG13 1 
ATOM   1657 H HG21 . ILE   A 1 130 ? 30.920 -13.358 9.897   1.00 23.49  ? 110 ILE   A HG21 1 
ATOM   1658 H HG22 . ILE   A 1 130 ? 30.312 -13.005 11.321  1.00 23.49  ? 110 ILE   A HG22 1 
ATOM   1659 H HG23 . ILE   A 1 130 ? 29.681 -14.179 10.457  1.00 23.49  ? 110 ILE   A HG23 1 
ATOM   1660 H HD11 . ILE   A 1 130 ? 29.744 -12.659 6.454   1.00 22.99  ? 110 ILE   A HD11 1 
ATOM   1661 H HD12 . ILE   A 1 130 ? 30.389 -11.592 7.439   1.00 22.99  ? 110 ILE   A HD12 1 
ATOM   1662 H HD13 . ILE   A 1 130 ? 30.706 -13.138 7.624   1.00 22.99  ? 110 ILE   A HD13 1 
ATOM   1663 N N    . VAL   A 1 131 ? 25.814 -13.280 9.956   1.00 17.99  ? 111 VAL   A N    1 
ATOM   1664 C CA   . VAL   A 1 131 ? 24.797 -14.327 9.956   1.00 18.19  ? 111 VAL   A CA   1 
ATOM   1665 C C    . VAL   A 1 131 ? 24.482 -14.630 8.496   1.00 17.97  ? 111 VAL   A C    1 
ATOM   1666 O O    . VAL   A 1 131 ? 23.394 -14.319 7.985   1.00 19.07  ? 111 VAL   A O    1 
ATOM   1667 C CB   . VAL   A 1 131 ? 23.547 -13.883 10.733  1.00 19.96  ? 111 VAL   A CB   1 
ATOM   1668 C CG1  . VAL   A 1 131 ? 22.578 -15.043 10.885  1.00 22.04  ? 111 VAL   A CG1  1 
ATOM   1669 C CG2  . VAL   A 1 131 ? 23.931 -13.322 12.080  1.00 22.44  ? 111 VAL   A CG2  1 
ATOM   1670 H H    . VAL   A 1 131 ? 25.583 -12.592 9.495   1.00 21.59  ? 111 VAL   A H    1 
ATOM   1671 H HA   . VAL   A 1 131 ? 25.124 -15.131 10.388  1.00 21.84  ? 111 VAL   A HA   1 
ATOM   1672 H HB   . VAL   A 1 131 ? 23.099 -13.182 10.236  1.00 23.96  ? 111 VAL   A HB   1 
ATOM   1673 H HG11 . VAL   A 1 131 ? 21.809 -14.747 11.396  1.00 26.45  ? 111 VAL   A HG11 1 
ATOM   1674 H HG12 . VAL   A 1 131 ? 22.297 -15.337 10.004  1.00 26.45  ? 111 VAL   A HG12 1 
ATOM   1675 H HG13 . VAL   A 1 131 ? 23.024 -15.769 11.349  1.00 26.45  ? 111 VAL   A HG13 1 
ATOM   1676 H HG21 . VAL   A 1 131 ? 23.135 -13.248 12.629  1.00 26.93  ? 111 VAL   A HG21 1 
ATOM   1677 H HG22 . VAL   A 1 131 ? 24.569 -13.919 12.500  1.00 26.93  ? 111 VAL   A HG22 1 
ATOM   1678 H HG23 . VAL   A 1 131 ? 24.329 -12.447 11.955  1.00 26.93  ? 111 VAL   A HG23 1 
ATOM   1679 N N    . PHE   A 1 132 ? 25.413 -15.230 7.830   1.00 18.22  ? 112 PHE   A N    1 
ATOM   1680 C CA   . PHE   A 1 132 ? 25.349 -15.419 6.395   1.00 19.83  ? 112 PHE   A CA   1 
ATOM   1681 C C    . PHE   A 1 132 ? 24.637 -16.728 6.091   1.00 22.49  ? 112 PHE   A C    1 
ATOM   1682 O O    . PHE   A 1 132 ? 24.852 -17.727 6.778   1.00 23.44  ? 112 PHE   A O    1 
ATOM   1683 C CB   . PHE   A 1 132 ? 26.787 -15.534 5.884   1.00 24.06  ? 112 PHE   A CB   1 
ATOM   1684 C CG   . PHE   A 1 132 ? 27.118 -14.725 4.679   1.00 22.28  ? 112 PHE   A CG   1 
ATOM   1685 C CD1  . PHE   A 1 132 ? 27.314 -13.373 4.764   1.00 34.25  ? 112 PHE   A CD1  1 
ATOM   1686 C CD2  . PHE   A 1 132 ? 27.282 -15.363 3.451   1.00 31.90  ? 112 PHE   A CD2  1 
ATOM   1687 C CE1  . PHE   A 1 132 ? 27.673 -12.656 3.647   1.00 30.95  ? 112 PHE   A CE1  1 
ATOM   1688 C CE2  . PHE   A 1 132 ? 27.621 -14.632 2.321   1.00 35.70  ? 112 PHE   A CE2  1 
ATOM   1689 C CZ   . PHE   A 1 132 ? 27.823 -13.278 2.450   1.00 27.01  ? 112 PHE   A CZ   1 
ATOM   1690 H H    . PHE   A 1 132 ? 26.127 -15.555 8.184   1.00 21.87  ? 112 PHE   A H    1 
ATOM   1691 H HA   . PHE   A 1 132 ? 24.879 -14.693 5.956   1.00 23.80  ? 112 PHE   A HA   1 
ATOM   1692 H HB2  . PHE   A 1 132 ? 27.384 -15.250 6.593   1.00 28.87  ? 112 PHE   A HB2  1 
ATOM   1693 H HB3  . PHE   A 1 132 ? 26.955 -16.463 5.660   1.00 28.87  ? 112 PHE   A HB3  1 
ATOM   1694 H HD1  . PHE   A 1 132 ? 27.205 -12.939 5.579   1.00 41.10  ? 112 PHE   A HD1  1 
ATOM   1695 H HD2  . PHE   A 1 132 ? 27.164 -16.284 3.388   1.00 38.28  ? 112 PHE   A HD2  1 
ATOM   1696 H HE1  . PHE   A 1 132 ? 27.813 -11.739 3.712   1.00 37.14  ? 112 PHE   A HE1  1 
ATOM   1697 H HE2  . PHE   A 1 132 ? 27.710 -15.049 1.494   1.00 42.84  ? 112 PHE   A HE2  1 
ATOM   1698 H HZ   . PHE   A 1 132 ? 28.066 -12.779 1.703   1.00 32.41  ? 112 PHE   A HZ   1 
ATOM   1699 N N    . PRO   A 1 133 ? 23.814 -16.763 5.065   1.00 24.36  ? 113 PRO   A N    1 
ATOM   1700 C CA   . PRO   A 1 133 ? 23.053 -17.989 4.772   1.00 26.27  ? 113 PRO   A CA   1 
ATOM   1701 C C    . PRO   A 1 133 ? 23.930 -19.221 4.596   1.00 27.85  ? 113 PRO   A C    1 
ATOM   1702 O O    . PRO   A 1 133 ? 24.839 -19.226 3.773   1.00 29.69  ? 113 PRO   A O    1 
ATOM   1703 C CB   . PRO   A 1 133 ? 22.334 -17.629 3.470   1.00 27.53  ? 113 PRO   A CB   1 
ATOM   1704 C CG   . PRO   A 1 133 ? 22.154 -16.131 3.564   1.00 29.23  ? 113 PRO   A CG   1 
ATOM   1705 C CD   . PRO   A 1 133 ? 23.403 -15.619 4.246   1.00 27.54  ? 113 PRO   A CD   1 
ATOM   1706 H HA   . PRO   A 1 133 ? 22.424 -18.160 5.491   1.00 31.53  ? 113 PRO   A HA   1 
ATOM   1707 H HB2  . PRO   A 1 133 ? 22.881 -17.870 2.707   1.00 33.04  ? 113 PRO   A HB2  1 
ATOM   1708 H HB3  . PRO   A 1 133 ? 21.478 -18.083 3.422   1.00 33.04  ? 113 PRO   A HB3  1 
ATOM   1709 H HG2  . PRO   A 1 133 ? 22.067 -15.753 2.675   1.00 35.08  ? 113 PRO   A HG2  1 
ATOM   1710 H HG3  . PRO   A 1 133 ? 21.365 -15.926 4.090   1.00 35.08  ? 113 PRO   A HG3  1 
ATOM   1711 H HD2  . PRO   A 1 133 ? 24.086 -15.394 3.595   1.00 33.04  ? 113 PRO   A HD2  1 
ATOM   1712 H HD3  . PRO   A 1 133 ? 23.205 -14.848 4.800   1.00 33.04  ? 113 PRO   A HD3  1 
ATOM   1713 N N    . GLY   A 1 134 ? 23.663 -20.257 5.389   1.00 28.50  ? 114 GLY   A N    1 
ATOM   1714 C CA   . GLY   A 1 134 ? 24.360 -21.526 5.260   1.00 28.90  ? 114 GLY   A CA   1 
ATOM   1715 C C    . GLY   A 1 134 ? 25.715 -21.601 5.932   1.00 28.17  ? 114 GLY   A C    1 
ATOM   1716 O O    . GLY   A 1 134 ? 26.437 -22.588 5.735   1.00 30.28  ? 114 GLY   A O    1 
ATOM   1717 H H    . GLY   A 1 134 ? 23.074 -20.247 6.015   1.00 34.21  ? 114 GLY   A H    1 
ATOM   1718 H HA2  . GLY   A 1 134 ? 23.805 -22.222 5.643   1.00 34.69  ? 114 GLY   A HA2  1 
ATOM   1719 H HA3  . GLY   A 1 134 ? 24.491 -21.710 4.316   1.00 34.69  ? 114 GLY   A HA3  1 
ATOM   1720 N N    . TYR   A 1 135 ? 26.096 -20.594 6.706   1.00 23.82  ? 115 TYR   A N    1 
ATOM   1721 C CA   . TYR   A 1 135 ? 27.350 -20.608 7.437   1.00 23.09  ? 115 TYR   A CA   1 
ATOM   1722 C C    . TYR   A 1 135 ? 27.071 -20.482 8.924   1.00 25.02  ? 115 TYR   A C    1 
ATOM   1723 O O    . TYR   A 1 135 ? 26.054 -19.907 9.317   1.00 26.18  ? 115 TYR   A O    1 
ATOM   1724 C CB   . TYR   A 1 135 ? 28.252 -19.445 7.001   1.00 22.32  ? 115 TYR   A CB   1 
ATOM   1725 C CG   . TYR   A 1 135 ? 28.850 -19.644 5.635   1.00 21.24  ? 115 TYR   A CG   1 
ATOM   1726 C CD1  . TYR   A 1 135 ? 28.198 -19.202 4.497   1.00 20.94  ? 115 TYR   A CD1  1 
ATOM   1727 C CD2  . TYR   A 1 135 ? 30.074 -20.268 5.480   1.00 21.81  ? 115 TYR   A CD2  1 
ATOM   1728 C CE1  . TYR   A 1 135 ? 28.730 -19.384 3.249   1.00 22.54  ? 115 TYR   A CE1  1 
ATOM   1729 C CE2  . TYR   A 1 135 ? 30.608 -20.471 4.238   1.00 22.45  ? 115 TYR   A CE2  1 
ATOM   1730 C CZ   . TYR   A 1 135 ? 29.945 -20.024 3.121   1.00 22.07  ? 115 TYR   A CZ   1 
ATOM   1731 O OH   . TYR   A 1 135 ? 30.487 -20.230 1.877   1.00 23.94  ? 115 TYR   A OH   1 
ATOM   1732 H H    . TYR   A 1 135 ? 25.634 -19.878 6.823   1.00 28.58  ? 115 TYR   A H    1 
ATOM   1733 H HA   . TYR   A 1 135 ? 27.817 -21.440 7.267   1.00 27.71  ? 115 TYR   A HA   1 
ATOM   1734 H HB2  . TYR   A 1 135 ? 27.726 -18.630 6.981   1.00 26.78  ? 115 TYR   A HB2  1 
ATOM   1735 H HB3  . TYR   A 1 135 ? 28.979 -19.356 7.636   1.00 26.78  ? 115 TYR   A HB3  1 
ATOM   1736 H HD1  . TYR   A 1 135 ? 27.379 -18.772 4.582   1.00 25.13  ? 115 TYR   A HD1  1 
ATOM   1737 H HD2  . TYR   A 1 135 ? 30.541 -20.553 6.232   1.00 26.18  ? 115 TYR   A HD2  1 
ATOM   1738 H HE1  . TYR   A 1 135 ? 28.278 -19.078 2.496   1.00 27.05  ? 115 TYR   A HE1  1 
ATOM   1739 H HE2  . TYR   A 1 135 ? 31.421 -20.914 4.150   1.00 26.95  ? 115 TYR   A HE2  1 
ATOM   1740 H HH   . TYR   A 1 135 ? 31.224 -20.626 1.947   1.00 28.73  ? 115 TYR   A HH   1 
ATOM   1741 N N    . PRO   A 1 136 ? 27.974 -20.950 9.781   1.00 26.28  ? 116 PRO   A N    1 
ATOM   1742 C CA   . PRO   A 1 136 ? 27.785 -20.737 11.215  1.00 26.50  ? 116 PRO   A CA   1 
ATOM   1743 C C    . PRO   A 1 136 ? 27.786 -19.251 11.520  1.00 24.56  ? 116 PRO   A C    1 
ATOM   1744 O O    . PRO   A 1 136 ? 28.509 -18.476 10.896  1.00 23.30  ? 116 PRO   A O    1 
ATOM   1745 C CB   . PRO   A 1 136 ? 29.005 -21.430 11.840  1.00 29.79  ? 116 PRO   A CB   1 
ATOM   1746 C CG   . PRO   A 1 136 ? 29.509 -22.351 10.798  1.00 30.45  ? 116 PRO   A CG   1 
ATOM   1747 C CD   . PRO   A 1 136 ? 29.223 -21.678 9.497   1.00 27.67  ? 116 PRO   A CD   1 
ATOM   1748 H HA   . PRO   A 1 136 ? 26.972 -21.157 11.536  1.00 31.80  ? 116 PRO   A HA   1 
ATOM   1749 H HB2  . PRO   A 1 136 ? 29.676 -20.768 12.070  1.00 35.75  ? 116 PRO   A HB2  1 
ATOM   1750 H HB3  . PRO   A 1 136 ? 28.736 -21.919 12.633  1.00 35.75  ? 116 PRO   A HB3  1 
ATOM   1751 H HG2  . PRO   A 1 136 ? 30.463 -22.487 10.913  1.00 36.55  ? 116 PRO   A HG2  1 
ATOM   1752 H HG3  . PRO   A 1 136 ? 29.044 -23.200 10.857  1.00 36.55  ? 116 PRO   A HG3  1 
ATOM   1753 H HD2  . PRO   A 1 136 ? 29.936 -21.066 9.257   1.00 33.20  ? 116 PRO   A HD2  1 
ATOM   1754 H HD3  . PRO   A 1 136 ? 29.093 -22.329 8.789   1.00 33.20  ? 116 PRO   A HD3  1 
ATOM   1755 N N    A ARG   A 1 137 ? 26.967 -18.853 12.485  0.58 25.01  ? 117 ARG   A N    1 
ATOM   1756 N N    B ARG   A 1 137 ? 26.972 -18.856 12.494  0.42 25.85  ? 117 ARG   A N    1 
ATOM   1757 C CA   A ARG   A 1 137 ? 27.031 -17.486 12.982  0.58 25.72  ? 117 ARG   A CA   1 
ATOM   1758 C CA   B ARG   A 1 137 ? 27.023 -17.490 12.998  0.42 27.31  ? 117 ARG   A CA   1 
ATOM   1759 C C    A ARG   A 1 137 ? 28.442 -17.203 13.475  0.58 25.27  ? 117 ARG   A C    1 
ATOM   1760 C C    B ARG   A 1 137 ? 28.426 -17.191 13.507  0.42 25.98  ? 117 ARG   A C    1 
ATOM   1761 O O    A ARG   A 1 137 ? 29.076 -18.045 14.117  0.58 27.56  ? 117 ARG   A O    1 
ATOM   1762 O O    B ARG   A 1 137 ? 29.035 -18.008 14.203  0.42 27.69  ? 117 ARG   A O    1 
ATOM   1763 C CB   A ARG   A 1 137 ? 26.040 -17.295 14.129  0.58 29.27  ? 117 ARG   A CB   1 
ATOM   1764 C CB   B ARG   A 1 137 ? 26.016 -17.324 14.137  0.42 31.71  ? 117 ARG   A CB   1 
ATOM   1765 C CG   A ARG   A 1 137 ? 25.906 -15.851 14.583  0.58 32.11  ? 117 ARG   A CG   1 
ATOM   1766 C CG   B ARG   A 1 137 ? 24.567 -17.292 13.685  0.42 35.37  ? 117 ARG   A CG   1 
ATOM   1767 C CD   A ARG   A 1 137 ? 25.004 -15.725 15.811  0.58 35.50  ? 117 ARG   A CD   1 
ATOM   1768 C CD   B ARG   A 1 137 ? 23.604 -17.384 14.864  0.42 38.47  ? 117 ARG   A CD   1 
ATOM   1769 N NE   A ARG   A 1 137 ? 24.841 -14.335 16.225  0.58 38.67  ? 117 ARG   A NE   1 
ATOM   1770 N NE   B ARG   A 1 137 ? 22.242 -17.011 14.500  0.42 40.61  ? 117 ARG   A NE   1 
ATOM   1771 C CZ   A ARG   A 1 137 ? 23.811 -13.566 15.899  0.58 40.95  ? 117 ARG   A CZ   1 
ATOM   1772 C CZ   B ARG   A 1 137 ? 21.735 -15.791 14.626  0.42 42.59  ? 117 ARG   A CZ   1 
ATOM   1773 N NH1  A ARG   A 1 137 ? 22.801 -14.027 15.178  0.58 43.00  ? 117 ARG   A NH1  1 
ATOM   1774 N NH1  B ARG   A 1 137 ? 22.461 -14.782 15.083  0.42 43.29  ? 117 ARG   A NH1  1 
ATOM   1775 N NH2  A ARG   A 1 137 ? 23.793 -12.302 16.312  0.58 41.59  ? 117 ARG   A NH2  1 
ATOM   1776 N NH2  B ARG   A 1 137 ? 20.465 -15.578 14.292  0.42 43.18  ? 117 ARG   A NH2  1 
ATOM   1777 H H    A ARG   A 1 137 ? 26.374 -19.347 12.864  0.58 30.02  ? 117 ARG   A H    1 
ATOM   1778 H H    B ARG   A 1 137 ? 26.386 -19.355 12.876  0.42 31.02  ? 117 ARG   A H    1 
ATOM   1779 H HA   A ARG   A 1 137 ? 26.800 -16.862 12.276  0.58 30.87  ? 117 ARG   A HA   1 
ATOM   1780 H HA   B ARG   A 1 137 ? 26.798 -16.862 12.294  0.42 32.77  ? 117 ARG   A HA   1 
ATOM   1781 H HB2  A ARG   A 1 137 ? 25.165 -17.597 13.839  0.58 35.13  ? 117 ARG   A HB2  1 
ATOM   1782 H HB2  B ARG   A 1 137 ? 26.117 -18.067 14.751  0.42 38.05  ? 117 ARG   A HB2  1 
ATOM   1783 H HB3  A ARG   A 1 137 ? 26.338 -17.819 14.889  0.58 35.13  ? 117 ARG   A HB3  1 
ATOM   1784 H HB3  B ARG   A 1 137 ? 26.200 -16.488 14.594  0.42 38.05  ? 117 ARG   A HB3  1 
ATOM   1785 H HG2  A ARG   A 1 137 ? 26.783 -15.505 14.813  0.58 38.54  ? 117 ARG   A HG2  1 
ATOM   1786 H HG2  B ARG   A 1 137 ? 24.395 -16.460 13.217  0.42 42.45  ? 117 ARG   A HG2  1 
ATOM   1787 H HG3  A ARG   A 1 137 ? 25.519 -15.325 13.866  0.58 38.54  ? 117 ARG   A HG3  1 
ATOM   1788 H HG3  B ARG   A 1 137 ? 24.398 -18.045 13.096  0.42 42.45  ? 117 ARG   A HG3  1 
ATOM   1789 H HD2  A ARG   A 1 137 ? 24.127 -16.085 15.603  0.58 42.60  ? 117 ARG   A HD2  1 
ATOM   1790 H HD2  B ARG   A 1 137 ? 23.589 -18.297 15.191  0.42 46.17  ? 117 ARG   A HD2  1 
ATOM   1791 H HD3  A ARG   A 1 137 ? 25.397 -16.217 16.549  0.58 42.60  ? 117 ARG   A HD3  1 
ATOM   1792 H HD3  B ARG   A 1 137 ? 23.904 -16.785 15.565  0.42 46.17  ? 117 ARG   A HD3  1 
ATOM   1793 H HE   A ARG   A 1 137 ? 25.457 -13.990 16.715  0.58 46.40  ? 117 ARG   A HE   1 
ATOM   1794 H HE   B ARG   A 1 137 ? 21.730 -17.625 14.181  0.42 48.73  ? 117 ARG   A HE   1 
ATOM   1795 H HH11 A ARG   A 1 137 ? 22.802 -14.844 14.910  0.58 51.60  ? 117 ARG   A HH11 1 
ATOM   1796 H HH11 B ARG   A 1 137 ? 23.282 -14.909 15.306  0.42 51.95  ? 117 ARG   A HH11 1 
ATOM   1797 H HH12 A ARG   A 1 137 ? 22.144 -13.509 14.979  0.58 51.60  ? 117 ARG   A HH12 1 
ATOM   1798 H HH12 B ARG   A 1 137 ? 22.112 -13.999 15.156  0.42 51.95  ? 117 ARG   A HH12 1 
ATOM   1799 H HH21 A ARG   A 1 137 ? 24.442 -11.994 16.783  0.58 49.91  ? 117 ARG   A HH21 1 
ATOM   1800 H HH21 B ARG   A 1 137 ? 19.983 -16.227 13.999  0.42 51.82  ? 117 ARG   A HH21 1 
ATOM   1801 H HH22 A ARG   A 1 137 ? 23.131 -11.793 16.107  0.58 49.91  ? 117 ARG   A HH22 1 
ATOM   1802 H HH22 B ARG   A 1 137 ? 20.126 -14.791 14.370  0.42 51.82  ? 117 ARG   A HH22 1 
ATOM   1803 N N    . GLY   A 1 138 ? 28.946 -16.019 13.148  1.00 24.52  ? 118 GLY   A N    1 
ATOM   1804 C CA   . GLY   A 1 138 ? 30.287 -15.637 13.524  1.00 24.18  ? 118 GLY   A CA   1 
ATOM   1805 C C    . GLY   A 1 138 ? 30.342 -14.182 13.938  1.00 21.49  ? 118 GLY   A C    1 
ATOM   1806 O O    . GLY   A 1 138 ? 29.323 -13.478 13.984  1.00 21.90  ? 118 GLY   A O    1 
ATOM   1807 H H    A GLY   A 1 138 ? 28.521 -15.417 12.705  0.58 29.43  ? 118 GLY   A H    1 
ATOM   1808 H H    B GLY   A 1 138 ? 28.531 -15.427 12.683  0.42 29.43  ? 118 GLY   A H    1 
ATOM   1809 H HA2  . GLY   A 1 138 ? 30.586 -16.183 14.267  1.00 29.01  ? 118 GLY   A HA2  1 
ATOM   1810 H HA3  . GLY   A 1 138 ? 30.887 -15.769 12.773  1.00 29.01  ? 118 GLY   A HA3  1 
ATOM   1811 N N    A GLN   A 1 139 ? 31.559 -13.744 14.238  0.36 21.91  ? 119 GLN   A N    1 
ATOM   1812 N N    B GLN   A 1 139 ? 31.551 -13.750 14.259  0.64 21.86  ? 119 GLN   A N    1 
ATOM   1813 C CA   A GLN   A 1 139 ? 31.860 -12.354 14.551  0.36 22.58  ? 119 GLN   A CA   1 
ATOM   1814 C CA   B GLN   A 1 139 ? 31.850 -12.355 14.531  0.64 22.47  ? 119 GLN   A CA   1 
ATOM   1815 C C    A GLN   A 1 139 ? 32.893 -11.866 13.548  0.36 21.44  ? 119 GLN   A C    1 
ATOM   1816 C C    B GLN   A 1 139 ? 32.865 -11.898 13.500  0.64 21.37  ? 119 GLN   A C    1 
ATOM   1817 O O    A GLN   A 1 139 ? 33.973 -12.454 13.423  0.36 24.36  ? 119 GLN   A O    1 
ATOM   1818 O O    B GLN   A 1 139 ? 33.895 -12.550 13.295  0.64 24.45  ? 119 GLN   A O    1 
ATOM   1819 C CB   A GLN   A 1 139 ? 32.392 -12.214 15.977  0.36 26.45  ? 119 GLN   A CB   1 
ATOM   1820 C CB   B GLN   A 1 139 ? 32.410 -12.166 15.938  0.64 26.25  ? 119 GLN   A CB   1 
ATOM   1821 C CG   A GLN   A 1 139 ? 31.349 -12.486 17.058  0.36 31.98  ? 119 GLN   A CG   1 
ATOM   1822 C CG   B GLN   A 1 139 ? 32.563 -10.706 16.357  0.64 31.38  ? 119 GLN   A CG   1 
ATOM   1823 C CD   A GLN   A 1 139 ? 30.220 -11.475 17.043  0.36 36.36  ? 119 GLN   A CD   1 
ATOM   1824 C CD   B GLN   A 1 139 ? 31.218 -9.985  16.521  0.64 35.71  ? 119 GLN   A CD   1 
ATOM   1825 O OE1  A GLN   A 1 139 ? 30.440 -10.284 16.817  0.36 38.61  ? 119 GLN   A OE1  1 
ATOM   1826 O OE1  B GLN   A 1 139 ? 30.154 -10.612 16.507  0.64 38.15  ? 119 GLN   A OE1  1 
ATOM   1827 N NE2  A GLN   A 1 139 ? 29.002 -11.945 17.277  0.36 37.98  ? 119 GLN   A NE2  1 
ATOM   1828 N NE2  B GLN   A 1 139 ? 31.265 -8.665  16.684  0.64 36.55  ? 119 GLN   A NE2  1 
ATOM   1829 H H    A GLN   A 1 139 ? 32.252 -14.253 14.267  0.36 26.29  ? 119 GLN   A H    1 
ATOM   1830 H H    B GLN   A 1 139 ? 32.238 -14.264 14.327  0.64 26.23  ? 119 GLN   A H    1 
ATOM   1831 H HA   A GLN   A 1 139 ? 31.058 -11.814 14.473  0.36 27.10  ? 119 GLN   A HA   1 
ATOM   1832 H HA   B GLN   A 1 139 ? 31.045 -11.817 14.464  0.64 26.96  ? 119 GLN   A HA   1 
ATOM   1833 H HB2  A GLN   A 1 139 ? 33.118 -12.846 16.101  0.36 31.74  ? 119 GLN   A HB2  1 
ATOM   1834 H HB2  B GLN   A 1 139 ? 31.812 -12.593 16.571  0.64 31.50  ? 119 GLN   A HB2  1 
ATOM   1835 H HB3  A GLN   A 1 139 ? 32.716 -11.308 16.100  0.36 31.74  ? 119 GLN   A HB3  1 
ATOM   1836 H HB3  B GLN   A 1 139 ? 33.287 -12.578 15.981  0.64 31.50  ? 119 GLN   A HB3  1 
ATOM   1837 H HG2  A GLN   A 1 139 ? 30.967 -13.366 16.916  0.36 38.38  ? 119 GLN   A HG2  1 
ATOM   1838 H HG2  B GLN   A 1 139 ? 33.028 -10.669 17.207  0.64 37.65  ? 119 GLN   A HG2  1 
ATOM   1839 H HG3  A GLN   A 1 139 ? 31.777 -12.447 17.928  0.36 38.38  ? 119 GLN   A HG3  1 
ATOM   1840 H HG3  B GLN   A 1 139 ? 33.073 -10.236 15.679  0.64 37.65  ? 119 GLN   A HG3  1 
ATOM   1841 H HE21 A GLN   A 1 139 ? 28.886 -12.784 17.427  0.36 45.58  ? 119 GLN   A HE21 1 
ATOM   1842 H HE21 B GLN   A 1 139 ? 32.024 -8.260  16.694  0.64 43.86  ? 119 GLN   A HE21 1 
ATOM   1843 H HE22 A GLN   A 1 139 ? 28.328 -11.410 17.280  0.36 45.58  ? 119 GLN   A HE22 1 
ATOM   1844 H HE22 B GLN   A 1 139 ? 30.537 -8.217  16.780  0.64 43.86  ? 119 GLN   A HE22 1 
ATOM   1845 N N    . TYR   A 1 140 ? 32.556 -10.801 12.841  1.00 18.56  ? 120 TYR   A N    1 
ATOM   1846 C CA   . TYR   A 1 140 ? 33.370 -10.258 11.769  1.00 18.15  ? 120 TYR   A CA   1 
ATOM   1847 C C    . TYR   A 1 140 ? 33.933 -8.905  12.168  1.00 17.01  ? 120 TYR   A C    1 
ATOM   1848 O O    . TYR   A 1 140 ? 33.202 -8.015  12.607  1.00 18.27  ? 120 TYR   A O    1 
ATOM   1849 C CB   . TYR   A 1 140 ? 32.498 -10.149 10.516  1.00 18.53  ? 120 TYR   A CB   1 
ATOM   1850 C CG   . TYR   A 1 140 ? 33.158 -9.591  9.275   1.00 17.18  ? 120 TYR   A CG   1 
ATOM   1851 C CD1  . TYR   A 1 140 ? 34.503 -9.824  8.989   1.00 17.11  ? 120 TYR   A CD1  1 
ATOM   1852 C CD2  . TYR   A 1 140 ? 32.422 -8.818  8.387   1.00 17.24  ? 120 TYR   A CD2  1 
ATOM   1853 C CE1  . TYR   A 1 140 ? 35.082 -9.294  7.849   1.00 16.63  ? 120 TYR   A CE1  1 
ATOM   1854 C CE2  . TYR   A 1 140 ? 32.975 -8.313  7.261   1.00 17.74  ? 120 TYR   A CE2  1 
ATOM   1855 C CZ   . TYR   A 1 140 ? 34.317 -8.557  6.990   1.00 16.71  ? 120 TYR   A CZ   1 
ATOM   1856 O OH   . TYR   A 1 140 ? 34.897 -8.012  5.880   1.00 19.82  ? 120 TYR   A OH   1 
ATOM   1857 H H    A TYR   A 1 140 ? 31.831 -10.358 12.970  0.36 22.28  ? 120 TYR   A H    1 
ATOM   1858 H H    B TYR   A 1 140 ? 31.853 -10.333 13.002  0.64 22.28  ? 120 TYR   A H    1 
ATOM   1859 H HA   . TYR   A 1 140 ? 34.136 -10.825 11.590  1.00 21.78  ? 120 TYR   A HA   1 
ATOM   1860 H HB2  . TYR   A 1 140 ? 32.180 -11.037 10.292  1.00 22.24  ? 120 TYR   A HB2  1 
ATOM   1861 H HB3  . TYR   A 1 140 ? 31.747 -9.570  10.721  1.00 22.24  ? 120 TYR   A HB3  1 
ATOM   1862 H HD1  . TYR   A 1 140 ? 35.015 -10.339 9.569   1.00 20.53  ? 120 TYR   A HD1  1 
ATOM   1863 H HD2  . TYR   A 1 140 ? 31.527 -8.644  8.571   1.00 20.69  ? 120 TYR   A HD2  1 
ATOM   1864 H HE1  . TYR   A 1 140 ? 35.983 -9.439  7.670   1.00 19.96  ? 120 TYR   A HE1  1 
ATOM   1865 H HE2  . TYR   A 1 140 ? 32.462 -7.807  6.673   1.00 21.29  ? 120 TYR   A HE2  1 
ATOM   1866 H HH   . TYR   A 1 140 ? 34.318 -7.611  5.421   1.00 23.78  ? 120 TYR   A HH   1 
ATOM   1867 N N    . ARG   A 1 141 ? 35.245 -8.768  12.045  1.00 16.25  ? 121 ARG   A N    1 
ATOM   1868 C CA   . ARG   A 1 141 ? 35.960 -7.507  12.242  1.00 16.69  ? 121 ARG   A CA   1 
ATOM   1869 C C    . ARG   A 1 141 ? 36.858 -7.277  11.037  1.00 16.38  ? 121 ARG   A C    1 
ATOM   1870 O O    . ARG   A 1 141 ? 37.521 -8.208  10.573  1.00 18.81  ? 121 ARG   A O    1 
ATOM   1871 C CB   . ARG   A 1 141 ? 36.849 -7.574  13.492  1.00 18.83  ? 121 ARG   A CB   1 
ATOM   1872 C CG   . ARG   A 1 141 ? 36.109 -7.740  14.781  1.00 20.75  ? 121 ARG   A CG   1 
ATOM   1873 C CD   . ARG   A 1 141 ? 37.069 -7.868  15.976  1.00 22.44  ? 121 ARG   A CD   1 
ATOM   1874 N NE   . ARG   A 1 141 ? 37.986 -6.739  16.131  1.00 24.87  ? 121 ARG   A NE   1 
ATOM   1875 C CZ   . ARG   A 1 141 ? 37.644 -5.562  16.644  1.00 27.06  ? 121 ARG   A CZ   1 
ATOM   1876 N NH1  . ARG   A 1 141 ? 36.412 -5.330  17.097  1.00 26.27  ? 121 ARG   A NH1  1 
ATOM   1877 N NH2  . ARG   A 1 141 ? 38.542 -4.584  16.674  1.00 31.10  ? 121 ARG   A NH2  1 
ATOM   1878 H H    . ARG   A 1 141 ? 35.769 -9.417  11.838  1.00 19.51  ? 121 ARG   A H    1 
ATOM   1879 H HA   . ARG   A 1 141 ? 35.329 -6.777  12.335  1.00 20.03  ? 121 ARG   A HA   1 
ATOM   1880 H HB2  . ARG   A 1 141 ? 37.450 -8.330  13.402  1.00 22.60  ? 121 ARG   A HB2  1 
ATOM   1881 H HB3  . ARG   A 1 141 ? 37.358 -6.751  13.552  1.00 22.60  ? 121 ARG   A HB3  1 
ATOM   1882 H HG2  . ARG   A 1 141 ? 35.543 -6.966  14.927  1.00 24.90  ? 121 ARG   A HG2  1 
ATOM   1883 H HG3  . ARG   A 1 141 ? 35.567 -8.543  14.739  1.00 24.90  ? 121 ARG   A HG3  1 
ATOM   1884 H HD2  . ARG   A 1 141 ? 36.545 -7.934  16.790  1.00 26.93  ? 121 ARG   A HD2  1 
ATOM   1885 H HD3  . ARG   A 1 141 ? 37.605 -8.668  15.860  1.00 26.93  ? 121 ARG   A HD3  1 
ATOM   1886 H HE   . ARG   A 1 141 ? 38.800 -6.844  15.873  1.00 29.85  ? 121 ARG   A HE   1 
ATOM   1887 H HH11 . ARG   A 1 141 ? 35.817 -5.950  17.061  1.00 31.52  ? 121 ARG   A HH11 1 
ATOM   1888 H HH12 . ARG   A 1 141 ? 36.213 -4.561  17.425  1.00 31.52  ? 121 ARG   A HH12 1 
ATOM   1889 H HH21 . ARG   A 1 141 ? 39.334 -4.717  16.364  1.00 37.33  ? 121 ARG   A HH21 1 
ATOM   1890 H HH22 . ARG   A 1 141 ? 38.333 -3.817  17.003  1.00 37.33  ? 121 ARG   A HH22 1 
ATOM   1891 N N    . ASN   A 1 142 ? 36.902 -6.050  10.528  1.00 15.64  ? 122 ASN   A N    1 
ATOM   1892 C CA   . ASN   A 1 142 ? 37.814 -5.790  9.414   1.00 15.67  ? 122 ASN   A CA   1 
ATOM   1893 C C    . ASN   A 1 142 ? 38.139 -4.309  9.334   1.00 15.78  ? 122 ASN   A C    1 
ATOM   1894 O O    . ASN   A 1 142 ? 37.503 -3.464  9.966   1.00 16.04  ? 122 ASN   A O    1 
ATOM   1895 C CB   . ASN   A 1 142 ? 37.233 -6.293  8.071   1.00 17.15  ? 122 ASN   A CB   1 
ATOM   1896 C CG   . ASN   A 1 142 ? 38.274 -6.829  7.126   1.00 18.67  ? 122 ASN   A CG   1 
ATOM   1897 O OD1  . ASN   A 1 142 ? 39.463 -6.652  7.330   1.00 18.95  ? 122 ASN   A OD1  1 
ATOM   1898 N ND2  . ASN   A 1 142 ? 37.816 -7.489  6.060   1.00 18.35  ? 122 ASN   A ND2  1 
ATOM   1899 H H    . ASN   A 1 142 ? 36.435 -5.380  10.796  1.00 18.77  ? 122 ASN   A H    1 
ATOM   1900 H HA   . ASN   A 1 142 ? 38.642 -6.260  9.596   1.00 18.80  ? 122 ASN   A HA   1 
ATOM   1901 H HB2  . ASN   A 1 142 ? 36.601 -7.007  8.252   1.00 20.59  ? 122 ASN   A HB2  1 
ATOM   1902 H HB3  . ASN   A 1 142 ? 36.783 -5.556  7.629   1.00 20.59  ? 122 ASN   A HB3  1 
ATOM   1903 H HD21 . ASN   A 1 142 ? 38.367 -7.817  5.487   1.00 22.02  ? 122 ASN   A HD21 1 
ATOM   1904 H HD22 . ASN   A 1 142 ? 36.969 -7.586  5.946   1.00 22.02  ? 122 ASN   A HD22 1 
ATOM   1905 N N    . HIS   A 1 143 ? 39.179 -4.026  8.564   1.00 16.02  ? 123 HIS   A N    1 
ATOM   1906 C CA   . HIS   A 1 143 ? 39.554 -2.680  8.161   1.00 15.50  ? 123 HIS   A CA   1 
ATOM   1907 C C    . HIS   A 1 143 ? 38.922 -2.379  6.800   1.00 15.22  ? 123 HIS   A C    1 
ATOM   1908 O O    . HIS   A 1 143 ? 38.832 -3.247  5.938   1.00 16.04  ? 123 HIS   A O    1 
ATOM   1909 C CB   . HIS   A 1 143 ? 41.075 -2.628  8.075   1.00 15.67  ? 123 HIS   A CB   1 
ATOM   1910 C CG   . HIS   A 1 143 ? 41.626 -1.316  7.617   1.00 16.87  ? 123 HIS   A CG   1 
ATOM   1911 N ND1  . HIS   A 1 143 ? 41.862 -1.045  6.290   1.00 18.59  ? 123 HIS   A ND1  1 
ATOM   1912 C CD2  . HIS   A 1 143 ? 41.994 -0.207  8.301   1.00 18.23  ? 123 HIS   A CD2  1 
ATOM   1913 C CE1  . HIS   A 1 143 ? 42.358 0.174   6.172   1.00 18.60  ? 123 HIS   A CE1  1 
ATOM   1914 N NE2  . HIS   A 1 143 ? 42.454 0.700   7.378   1.00 18.68  ? 123 HIS   A NE2  1 
ATOM   1915 H H    . HIS   A 1 143 ? 39.709 -4.625  8.248   1.00 19.22  ? 123 HIS   A H    1 
ATOM   1916 H HA   . HIS   A 1 143 ? 39.246 -2.006  8.787   1.00 18.61  ? 123 HIS   A HA   1 
ATOM   1917 H HB2  . HIS   A 1 143 ? 41.440 -2.808  8.956   1.00 18.81  ? 123 HIS   A HB2  1 
ATOM   1918 H HB3  . HIS   A 1 143 ? 41.372 -3.305  7.448   1.00 18.81  ? 123 HIS   A HB3  1 
ATOM   1919 H HD2  . HIS   A 1 143 ? 41.946 -0.084  9.221   1.00 21.88  ? 123 HIS   A HD2  1 
ATOM   1920 H HE1  . HIS   A 1 143 ? 42.599 0.589   5.375   1.00 22.32  ? 123 HIS   A HE1  1 
ATOM   1921 H HE2  . HIS   A 1 143 ? 42.755 1.486   7.558   1.00 22.42  ? 123 HIS   A HE2  1 
ATOM   1922 N N    . PHE   A 1 144 ? 38.448 -1.151  6.618   1.00 15.29  ? 124 PHE   A N    1 
ATOM   1923 C CA   . PHE   A 1 144 ? 37.783 -0.791  5.388   1.00 13.37  ? 124 PHE   A CA   1 
ATOM   1924 C C    . PHE   A 1 144 ? 38.253 0.560   4.886   1.00 14.72  ? 124 PHE   A C    1 
ATOM   1925 O O    . PHE   A 1 144 ? 38.606 1.469   5.661   1.00 15.69  ? 124 PHE   A O    1 
ATOM   1926 C CB   . PHE   A 1 144 ? 36.259 -0.664  5.601   1.00 15.26  ? 124 PHE   A CB   1 
ATOM   1927 C CG   . PHE   A 1 144 ? 35.580 -1.957  5.972   1.00 15.25  ? 124 PHE   A CG   1 
ATOM   1928 C CD1  . PHE   A 1 144 ? 35.592 -2.413  7.277   1.00 17.41  ? 124 PHE   A CD1  1 
ATOM   1929 C CD2  . PHE   A 1 144 ? 34.943 -2.719  5.011   1.00 16.03  ? 124 PHE   A CD2  1 
ATOM   1930 C CE1  . PHE   A 1 144 ? 34.956 -3.603  7.627   1.00 18.38  ? 124 PHE   A CE1  1 
ATOM   1931 C CE2  . PHE   A 1 144 ? 34.306 -3.930  5.360   1.00 17.13  ? 124 PHE   A CE2  1 
ATOM   1932 C CZ   . PHE   A 1 144 ? 34.324 -4.358  6.655   1.00 17.58  ? 124 PHE   A CZ   1 
ATOM   1933 H H    . PHE   A 1 144 ? 38.503 -0.516  7.194   1.00 18.35  ? 124 PHE   A H    1 
ATOM   1934 H HA   . PHE   A 1 144 ? 37.998 -1.471  4.730   1.00 16.05  ? 124 PHE   A HA   1 
ATOM   1935 H HB2  . PHE   A 1 144 ? 36.097 -0.030  6.318   1.00 18.31  ? 124 PHE   A HB2  1 
ATOM   1936 H HB3  . PHE   A 1 144 ? 35.856 -0.345  4.779   1.00 18.31  ? 124 PHE   A HB3  1 
ATOM   1937 H HD1  . PHE   A 1 144 ? 36.032 -1.919  7.930   1.00 20.89  ? 124 PHE   A HD1  1 
ATOM   1938 H HD2  . PHE   A 1 144 ? 34.934 -2.432  4.126   1.00 19.23  ? 124 PHE   A HD2  1 
ATOM   1939 H HE1  . PHE   A 1 144 ? 34.956 -3.888  8.512   1.00 22.06  ? 124 PHE   A HE1  1 
ATOM   1940 H HE2  . PHE   A 1 144 ? 33.875 -4.435  4.709   1.00 20.56  ? 124 PHE   A HE2  1 
ATOM   1941 H HZ   . PHE   A 1 144 ? 33.910 -5.158  6.886   1.00 21.10  ? 124 PHE   A HZ   1 
ATOM   1942 N N    . LEU   A 1 145 ? 38.198 0.693   3.569   1.00 14.40  ? 125 LEU   A N    1 
ATOM   1943 C CA   . LEU   A 1 145 ? 38.264 1.994   2.913   1.00 13.90  ? 125 LEU   A CA   1 
ATOM   1944 C C    . LEU   A 1 145 ? 36.975 2.186   2.138   1.00 14.62  ? 125 LEU   A C    1 
ATOM   1945 O O    . LEU   A 1 145 ? 36.503 1.271   1.482   1.00 15.83  ? 125 LEU   A O    1 
ATOM   1946 C CB   . LEU   A 1 145 ? 39.446 2.043   1.961   1.00 15.64  ? 125 LEU   A CB   1 
ATOM   1947 C CG   . LEU   A 1 145 ? 40.811 1.825   2.652   1.00 19.43  ? 125 LEU   A CG   1 
ATOM   1948 C CD1  . LEU   A 1 145 ? 41.907 1.669   1.636   1.00 21.96  ? 125 LEU   A CD1  1 
ATOM   1949 C CD2  . LEU   A 1 145 ? 41.146 2.887   3.587   1.00 22.17  ? 125 LEU   A CD2  1 
ATOM   1950 H H    . LEU   A 1 145 ? 38.121 0.033   3.023   1.00 17.28  ? 125 LEU   A H    1 
ATOM   1951 H HA   . LEU   A 1 145 ? 38.362 2.710   3.560   1.00 16.69  ? 125 LEU   A HA   1 
ATOM   1952 H HB2  . LEU   A 1 145 ? 39.337 1.348   1.293   1.00 18.77  ? 125 LEU   A HB2  1 
ATOM   1953 H HB3  . LEU   A 1 145 ? 39.465 2.913   1.533   1.00 18.77  ? 125 LEU   A HB3  1 
ATOM   1954 H HG   . LEU   A 1 145 ? 40.740 1.007   3.169   1.00 23.32  ? 125 LEU   A HG   1 
ATOM   1955 H HD11 . LEU   A 1 145 ? 42.754 1.565   2.098   1.00 26.36  ? 125 LEU   A HD11 1 
ATOM   1956 H HD12 . LEU   A 1 145 ? 41.726 0.884   1.095   1.00 26.36  ? 125 LEU   A HD12 1 
ATOM   1957 H HD13 . LEU   A 1 145 ? 41.931 2.459   1.074   1.00 26.36  ? 125 LEU   A HD13 1 
ATOM   1958 H HD21 . LEU   A 1 145 ? 42.048 2.745   3.916   1.00 26.61  ? 125 LEU   A HD21 1 
ATOM   1959 H HD22 . LEU   A 1 145 ? 41.091 3.740   3.130   1.00 26.61  ? 125 LEU   A HD22 1 
ATOM   1960 H HD23 . LEU   A 1 145 ? 40.518 2.866   4.327   1.00 26.61  ? 125 LEU   A HD23 1 
ATOM   1961 N N    . HIS   A 1 146 ? 36.391 3.371   2.226   1.00 15.12  ? 126 HIS   A N    1 
ATOM   1962 C CA   . HIS   A 1 146 ? 35.217 3.709   1.434   1.00 15.20  ? 126 HIS   A CA   1 
ATOM   1963 C C    . HIS   A 1 146 ? 35.531 4.868   0.505   1.00 14.55  ? 126 HIS   A C    1 
ATOM   1964 O O    . HIS   A 1 146 ? 36.207 5.813   0.908   1.00 16.29  ? 126 HIS   A O    1 
ATOM   1965 C CB   . HIS   A 1 146 ? 34.017 4.135   2.293   1.00 15.88  ? 126 HIS   A CB   1 
ATOM   1966 C CG   . HIS   A 1 146 ? 33.437 3.048   3.136   1.00 16.18  ? 126 HIS   A CG   1 
ATOM   1967 N ND1  . HIS   A 1 146 ? 32.238 2.428   2.839   1.00 19.15  ? 126 HIS   A ND1  1 
ATOM   1968 C CD2  . HIS   A 1 146 ? 33.846 2.544   4.316   1.00 17.97  ? 126 HIS   A CD2  1 
ATOM   1969 C CE1  . HIS   A 1 146 ? 31.969 1.549   3.791   1.00 19.67  ? 126 HIS   A CE1  1 
ATOM   1970 N NE2  . HIS   A 1 146 ? 32.936 1.593   4.691   1.00 17.83  ? 126 HIS   A NE2  1 
ATOM   1971 H H    . HIS   A 1 146 ? 36.658 4.003   2.743   1.00 18.14  ? 126 HIS   A H    1 
ATOM   1972 H HA   . HIS   A 1 146 ? 34.978 2.918   0.926   1.00 18.24  ? 126 HIS   A HA   1 
ATOM   1973 H HB2  . HIS   A 1 146 ? 34.302 4.846   2.889   1.00 19.06  ? 126 HIS   A HB2  1 
ATOM   1974 H HB3  . HIS   A 1 146 ? 33.315 4.456   1.706   1.00 19.06  ? 126 HIS   A HB3  1 
ATOM   1975 H HD2  . HIS   A 1 146 ? 34.607 2.795   4.788   1.00 21.56  ? 126 HIS   A HD2  1 
ATOM   1976 H HE1  . HIS   A 1 146 ? 31.224 0.994   3.821   1.00 23.61  ? 126 HIS   A HE1  1 
ATOM   1977 H HE2  . HIS   A 1 146 ? 32.985 1.105   5.397   1.00 21.40  ? 126 HIS   A HE2  1 
ATOM   1978 N N    . SER   A 1 147 ? 34.963 4.839   -0.694  1.00 14.32  ? 127 SER   A N    1 
ATOM   1979 C CA   . SER   A 1 147 ? 34.932 5.961   -1.630  1.00 14.36  ? 127 SER   A CA   1 
ATOM   1980 C C    . SER   A 1 147 ? 33.500 6.458   -1.764  1.00 14.61  ? 127 SER   A C    1 
ATOM   1981 O O    . SER   A 1 147 ? 32.593 5.643   -1.934  1.00 15.08  ? 127 SER   A O    1 
ATOM   1982 C CB   . SER   A 1 147 ? 35.420 5.432   -2.987  1.00 15.77  ? 127 SER   A CB   1 
ATOM   1983 O OG   . SER   A 1 147 ? 35.362 6.398   -4.031  1.00 16.48  ? 127 SER   A OG   1 
ATOM   1984 H H    . SER   A 1 147 ? 34.567 4.142   -1.007  1.00 17.19  ? 127 SER   A H    1 
ATOM   1985 H HA   . SER   A 1 147 ? 35.477 6.703   -1.325  1.00 17.24  ? 127 SER   A HA   1 
ATOM   1986 H HB2  . SER   A 1 147 ? 36.341 5.145   -2.889  1.00 18.92  ? 127 SER   A HB2  1 
ATOM   1987 H HB3  . SER   A 1 147 ? 34.863 4.679   -3.239  1.00 18.92  ? 127 SER   A HB3  1 
ATOM   1988 H HG   . SER   A 1 147 ? 34.571 6.660   -4.136  1.00 19.77  ? 127 SER   A HG   1 
ATOM   1989 N N    . PHE   A 1 148 ? 33.310 7.785   -1.688  1.00 15.41  ? 128 PHE   A N    1 
ATOM   1990 C CA   . PHE   A 1 148 ? 31.997 8.417   -1.822  1.00 15.03  ? 128 PHE   A CA   1 
ATOM   1991 C C    . PHE   A 1 148 ? 32.088 9.498   -2.890  1.00 15.99  ? 128 PHE   A C    1 
ATOM   1992 O O    . PHE   A 1 148 ? 32.840 10.450  -2.737  1.00 17.64  ? 128 PHE   A O    1 
ATOM   1993 C CB   . PHE   A 1 148 ? 31.549 9.074   -0.505  1.00 16.44  ? 128 PHE   A CB   1 
ATOM   1994 C CG   . PHE   A 1 148 ? 31.193 8.100   0.604   1.00 16.29  ? 128 PHE   A CG   1 
ATOM   1995 C CD1  . PHE   A 1 148 ? 32.121 7.669   1.512   1.00 17.49  ? 128 PHE   A CD1  1 
ATOM   1996 C CD2  . PHE   A 1 148 ? 29.890 7.658   0.755   1.00 16.58  ? 128 PHE   A CD2  1 
ATOM   1997 C CE1  . PHE   A 1 148 ? 31.784 6.799   2.540   1.00 17.67  ? 128 PHE   A CE1  1 
ATOM   1998 C CE2  . PHE   A 1 148 ? 29.556 6.790   1.772   1.00 17.20  ? 128 PHE   A CE2  1 
ATOM   1999 C CZ   . PHE   A 1 148 ? 30.487 6.364   2.663   1.00 17.39  ? 128 PHE   A CZ   1 
ATOM   2000 H H    . PHE   A 1 148 ? 33.945 8.350   -1.556  1.00 18.49  ? 128 PHE   A H    1 
ATOM   2001 H HA   . PHE   A 1 148 ? 31.354 7.740   -2.083  1.00 18.03  ? 128 PHE   A HA   1 
ATOM   2002 H HB2  . PHE   A 1 148 ? 32.270 9.636   -0.180  1.00 19.73  ? 128 PHE   A HB2  1 
ATOM   2003 H HB3  . PHE   A 1 148 ? 30.762 9.613   -0.683  1.00 19.73  ? 128 PHE   A HB3  1 
ATOM   2004 H HD1  . PHE   A 1 148 ? 32.999 7.966   1.440   1.00 21.00  ? 128 PHE   A HD1  1 
ATOM   2005 H HD2  . PHE   A 1 148 ? 29.233 7.950   0.165   1.00 19.90  ? 128 PHE   A HD2  1 
ATOM   2006 H HE1  . PHE   A 1 148 ? 32.432 6.512   3.141   1.00 21.20  ? 128 PHE   A HE1  1 
ATOM   2007 H HE2  . PHE   A 1 148 ? 28.679 6.491   1.849   1.00 20.64  ? 128 PHE   A HE2  1 
ATOM   2008 H HZ   . PHE   A 1 148 ? 30.249 5.784   3.350   1.00 20.88  ? 128 PHE   A HZ   1 
ATOM   2009 N N    . ARG   A 1 149 ? 31.339 9.346   -3.972  1.00 16.34  ? 129 ARG   A N    1 
ATOM   2010 C CA   . ARG   A 1 149 ? 31.234 10.368  -4.994  1.00 17.46  ? 129 ARG   A CA   1 
ATOM   2011 C C    . ARG   A 1 149 ? 29.810 10.918  -4.990  1.00 17.25  ? 129 ARG   A C    1 
ATOM   2012 O O    . ARG   A 1 149 ? 28.846 10.154  -4.901  1.00 17.98  ? 129 ARG   A O    1 
ATOM   2013 C CB   . ARG   A 1 149 ? 31.605 9.812   -6.361  1.00 18.95  ? 129 ARG   A CB   1 
ATOM   2014 C CG   . ARG   A 1 149 ? 33.039 9.331   -6.434  1.00 19.72  ? 129 ARG   A CG   1 
ATOM   2015 C CD   . ARG   A 1 149 ? 33.429 8.942   -7.849  1.00 20.46  ? 129 ARG   A CD   1 
ATOM   2016 N NE   . ARG   A 1 149 ? 33.585 10.120  -8.690  1.00 22.90  ? 129 ARG   A NE   1 
ATOM   2017 C CZ   . ARG   A 1 149 ? 33.936 10.090  -9.962  1.00 24.62  ? 129 ARG   A CZ   1 
ATOM   2018 N NH1  . ARG   A 1 149 ? 34.171 8.945   -10.576 1.00 27.25  ? 129 ARG   A NH1  1 
ATOM   2019 N NH2  . ARG   A 1 149 ? 34.086 11.240  -10.621 1.00 27.20  ? 129 ARG   A NH2  1 
ATOM   2020 H H    . ARG   A 1 149 ? 30.874 8.642   -4.138  1.00 19.61  ? 129 ARG   A H    1 
ATOM   2021 H HA   . ARG   A 1 149 ? 31.843 11.100  -4.811  1.00 20.95  ? 129 ARG   A HA   1 
ATOM   2022 H HB2  . ARG   A 1 149 ? 31.026 9.060   -6.563  1.00 22.74  ? 129 ARG   A HB2  1 
ATOM   2023 H HB3  . ARG   A 1 149 ? 31.488 10.508  -7.026  1.00 22.74  ? 129 ARG   A HB3  1 
ATOM   2024 H HG2  . ARG   A 1 149 ? 33.631 10.041  -6.140  1.00 23.66  ? 129 ARG   A HG2  1 
ATOM   2025 H HG3  . ARG   A 1 149 ? 33.146 8.553   -5.864  1.00 23.66  ? 129 ARG   A HG3  1 
ATOM   2026 H HD2  . ARG   A 1 149 ? 34.272 8.462   -7.832  1.00 24.55  ? 129 ARG   A HD2  1 
ATOM   2027 H HD3  . ARG   A 1 149 ? 32.736 8.381   -8.232  1.00 24.55  ? 129 ARG   A HD3  1 
ATOM   2028 H HE   . ARG   A 1 149 ? 33.440 10.889  -8.333  1.00 27.48  ? 129 ARG   A HE   1 
ATOM   2029 H HH11 . ARG   A 1 149 ? 34.097 8.203   -10.147 1.00 32.70  ? 129 ARG   A HH11 1 
ATOM   2030 H HH12 . ARG   A 1 149 ? 34.398 8.941   -11.406 1.00 32.70  ? 129 ARG   A HH12 1 
ATOM   2031 H HH21 . ARG   A 1 149 ? 33.954 11.988  -10.217 1.00 32.64  ? 129 ARG   A HH21 1 
ATOM   2032 H HH22 . ARG   A 1 149 ? 34.314 11.233  -11.451 1.00 32.64  ? 129 ARG   A HH22 1 
ATOM   2033 N N    . PHE   A 1 150 ? 29.690 12.242  -5.097  1.00 18.15  ? 130 PHE   A N    1 
ATOM   2034 C CA   . PHE   A 1 150 ? 28.445 12.973  -4.935  1.00 18.62  ? 130 PHE   A CA   1 
ATOM   2035 C C    . PHE   A 1 150 ? 27.973 13.594  -6.240  1.00 20.13  ? 130 PHE   A C    1 
ATOM   2036 O O    . PHE   A 1 150 ? 28.774 13.978  -7.109  1.00 23.17  ? 130 PHE   A O    1 
ATOM   2037 C CB   . PHE   A 1 150 ? 28.612 14.075  -3.891  1.00 19.84  ? 130 PHE   A CB   1 
ATOM   2038 C CG   . PHE   A 1 150 ? 28.640 13.557  -2.487  1.00 19.79  ? 130 PHE   A CG   1 
ATOM   2039 C CD1  . PHE   A 1 150 ? 29.787 12.977  -1.945  1.00 21.02  ? 130 PHE   A CD1  1 
ATOM   2040 C CD2  . PHE   A 1 150 ? 27.487 13.596  -1.716  1.00 20.53  ? 130 PHE   A CD2  1 
ATOM   2041 C CE1  . PHE   A 1 150 ? 29.777 12.480  -0.643  1.00 21.02  ? 130 PHE   A CE1  1 
ATOM   2042 C CE2  . PHE   A 1 150 ? 27.477 13.109  -0.426  1.00 21.59  ? 130 PHE   A CE2  1 
ATOM   2043 C CZ   . PHE   A 1 150 ? 28.632 12.540  0.111   1.00 21.32  ? 130 PHE   A CZ   1 
ATOM   2044 H H    . PHE   A 1 150 ? 30.354 12.760  -5.271  1.00 21.78  ? 130 PHE   A H    1 
ATOM   2045 H HA   . PHE   A 1 150 ? 27.758 12.350  -4.652  1.00 22.35  ? 130 PHE   A HA   1 
ATOM   2046 H HB2  . PHE   A 1 150 ? 29.448 14.538  -4.055  1.00 23.81  ? 130 PHE   A HB2  1 
ATOM   2047 H HB3  . PHE   A 1 150 ? 27.869 14.694  -3.966  1.00 23.81  ? 130 PHE   A HB3  1 
ATOM   2048 H HD1  . PHE   A 1 150 ? 30.562 12.923  -2.455  1.00 25.23  ? 130 PHE   A HD1  1 
ATOM   2049 H HD2  . PHE   A 1 150 ? 26.708 13.957  -2.075  1.00 24.64  ? 130 PHE   A HD2  1 
ATOM   2050 H HE1  . PHE   A 1 150 ? 30.550 12.105  -0.284  1.00 25.22  ? 130 PHE   A HE1  1 
ATOM   2051 H HE2  . PHE   A 1 150 ? 26.701 13.160  0.085   1.00 25.91  ? 130 PHE   A HE2  1 
ATOM   2052 H HZ   . PHE   A 1 150 ? 28.626 12.203  0.978   1.00 25.58  ? 130 PHE   A HZ   1 
ATOM   2053 N N    . GLU   A 1 151 ? 26.655 13.769  -6.326  1.00 19.72  ? 131 GLU   A N    1 
ATOM   2054 C CA   . GLU   A 1 151 ? 26.029 14.570  -7.372  1.00 21.37  ? 131 GLU   A CA   1 
ATOM   2055 C C    . GLU   A 1 151 ? 24.833 15.285  -6.760  1.00 20.77  ? 131 GLU   A C    1 
ATOM   2056 O O    . GLU   A 1 151 ? 23.972 14.651  -6.146  1.00 20.83  ? 131 GLU   A O    1 
ATOM   2057 C CB   . GLU   A 1 151 ? 25.595 13.666  -8.521  1.00 26.31  ? 131 GLU   A CB   1 
ATOM   2058 C CG   . GLU   A 1 151 ? 24.836 14.324  -9.655  1.00 31.28  ? 131 GLU   A CG   1 
ATOM   2059 C CD   . GLU   A 1 151 ? 24.337 13.245  -10.607 1.00 39.51  ? 131 GLU   A CD   1 
ATOM   2060 O OE1  . GLU   A 1 151 ? 25.173 12.676  -11.334 1.00 41.65  ? 131 GLU   A OE1  1 
ATOM   2061 O OE2  . GLU   A 1 151 ? 23.132 12.903  -10.563 1.00 43.71  ? 131 GLU   A OE2  1 
ATOM   2062 H H    . GLU   A 1 151 ? 26.090 13.426  -5.776  1.00 23.67  ? 131 GLU   A H    1 
ATOM   2063 H HA   . GLU   A 1 151 ? 26.642 15.240  -7.714  1.00 25.64  ? 131 GLU   A HA   1 
ATOM   2064 H HB2  . GLU   A 1 151 ? 26.390 13.267  -8.907  1.00 31.58  ? 131 GLU   A HB2  1 
ATOM   2065 H HB3  . GLU   A 1 151 ? 25.019 12.975  -8.159  1.00 31.58  ? 131 GLU   A HB3  1 
ATOM   2066 H HG2  . GLU   A 1 151 ? 24.075 14.812  -9.304  1.00 37.54  ? 131 GLU   A HG2  1 
ATOM   2067 H HG3  . GLU   A 1 151 ? 25.422 14.926  -10.139 1.00 37.54  ? 131 GLU   A HG3  1 
ATOM   2068 N N    . ASN   A 1 152 ? 24.812 16.601  -6.869  1.00 22.60  ? 132 ASN   A N    1 
ATOM   2069 C CA   . ASN   A 1 152 ? 23.687 17.409  -6.409  1.00 22.91  ? 132 ASN   A CA   1 
ATOM   2070 C C    . ASN   A 1 152 ? 23.283 17.075  -4.978  1.00 22.52  ? 132 ASN   A C    1 
ATOM   2071 O O    . ASN   A 1 152 ? 22.100 16.934  -4.649  1.00 23.22  ? 132 ASN   A O    1 
ATOM   2072 C CB   . ASN   A 1 152 ? 22.503 17.347  -7.370  1.00 25.09  ? 132 ASN   A CB   1 
ATOM   2073 C CG   . ASN   A 1 152 ? 21.478 18.435  -7.099  1.00 25.91  ? 132 ASN   A CG   1 
ATOM   2074 O OD1  . ASN   A 1 152 ? 21.802 19.480  -6.513  1.00 26.78  ? 132 ASN   A OD1  1 
ATOM   2075 N ND2  . ASN   A 1 152 ? 20.249 18.217  -7.544  1.00 26.63  ? 132 ASN   A ND2  1 
ATOM   2076 H H    . ASN   A 1 152 ? 25.451 17.064  -7.212  1.00 27.12  ? 132 ASN   A H    1 
ATOM   2077 H HA   . ASN   A 1 152 ? 23.988 18.331  -6.398  1.00 27.50  ? 132 ASN   A HA   1 
ATOM   2078 H HB2  . ASN   A 1 152 ? 22.825 17.456  -8.278  1.00 30.11  ? 132 ASN   A HB2  1 
ATOM   2079 H HB3  . ASN   A 1 152 ? 22.062 16.488  -7.275  1.00 30.11  ? 132 ASN   A HB3  1 
ATOM   2080 H HD21 . ASN   A 1 152 ? 19.634 18.805  -7.415  1.00 31.95  ? 132 ASN   A HD21 1 
ATOM   2081 H HD22 . ASN   A 1 152 ? 20.065 17.489  -7.963  1.00 31.95  ? 132 ASN   A HD22 1 
ATOM   2082 N N    . GLY   A 1 153 ? 24.280 16.979  -4.108  1.00 22.93  ? 133 GLY   A N    1 
ATOM   2083 C CA   . GLY   A 1 153 ? 24.026 16.923  -2.685  1.00 23.06  ? 133 GLY   A CA   1 
ATOM   2084 C C    . GLY   A 1 153 ? 23.802 15.552  -2.111  1.00 19.85  ? 133 GLY   A C    1 
ATOM   2085 O O    . GLY   A 1 153 ? 23.627 15.442  -0.892  1.00 20.34  ? 133 GLY   A O    1 
ATOM   2086 H H    . GLY   A 1 153 ? 25.113 16.945  -4.322  1.00 27.52  ? 133 GLY   A H    1 
ATOM   2087 H HA2  . GLY   A 1 153 ? 24.786 17.311  -2.222  1.00 27.68  ? 133 GLY   A HA2  1 
ATOM   2088 H HA3  . GLY   A 1 153 ? 23.236 17.452  -2.493  1.00 27.68  ? 133 GLY   A HA3  1 
ATOM   2089 N N    . LEU   A 1 154 ? 23.818 14.503  -2.938  1.00 18.88  ? 134 LEU   A N    1 
ATOM   2090 C CA   . LEU   A 1 154 ? 23.585 13.131  -2.499  1.00 17.92  ? 134 LEU   A CA   1 
ATOM   2091 C C    . LEU   A 1 154 ? 24.633 12.199  -3.095  1.00 18.23  ? 134 LEU   A C    1 
ATOM   2092 O O    . LEU   A 1 154 ? 25.353 12.547  -4.034  1.00 18.30  ? 134 LEU   A O    1 
ATOM   2093 C CB   . LEU   A 1 154 ? 22.175 12.663  -2.873  1.00 18.65  ? 134 LEU   A CB   1 
ATOM   2094 C CG   . LEU   A 1 154 ? 21.066 13.396  -2.142  1.00 19.96  ? 134 LEU   A CG   1 
ATOM   2095 C CD1  . LEU   A 1 154 ? 19.711 13.043  -2.779  1.00 21.87  ? 134 LEU   A CD1  1 
ATOM   2096 C CD2  . LEU   A 1 154 ? 21.055 13.090  -0.672  1.00 21.75  ? 134 LEU   A CD2  1 
ATOM   2097 H H    . LEU   A 1 154 ? 23.966 14.566  -3.782  1.00 22.66  ? 134 LEU   A H    1 
ATOM   2098 H HA   . LEU   A 1 154 ? 23.678 13.090  -1.534  1.00 21.51  ? 134 LEU   A HA   1 
ATOM   2099 H HB2  . LEU   A 1 154 ? 22.044 12.802  -3.824  1.00 22.38  ? 134 LEU   A HB2  1 
ATOM   2100 H HB3  . LEU   A 1 154 ? 22.095 11.720  -2.661  1.00 22.38  ? 134 LEU   A HB3  1 
ATOM   2101 H HG   . LEU   A 1 154 ? 21.221 14.350  -2.224  1.00 23.96  ? 134 LEU   A HG   1 
ATOM   2102 H HD11 . LEU   A 1 154 ? 19.009 13.531  -2.320  1.00 26.24  ? 134 LEU   A HD11 1 
ATOM   2103 H HD12 . LEU   A 1 154 ? 19.728 13.291  -3.717  1.00 26.24  ? 134 LEU   A HD12 1 
ATOM   2104 H HD13 . LEU   A 1 154 ? 19.560 12.088  -2.693  1.00 26.24  ? 134 LEU   A HD13 1 
ATOM   2105 H HD21 . LEU   A 1 154 ? 20.272 13.498  -0.270  1.00 26.10  ? 134 LEU   A HD21 1 
ATOM   2106 H HD22 . LEU   A 1 154 ? 21.027 12.129  -0.549  1.00 26.10  ? 134 LEU   A HD22 1 
ATOM   2107 H HD23 . LEU   A 1 154 ? 21.860 13.452  -0.268  1.00 26.10  ? 134 LEU   A HD23 1 
ATOM   2108 N N    . ILE   A 1 155 ? 24.698 10.992  -2.548  1.00 17.51  ? 135 ILE   A N    1 
ATOM   2109 C CA   . ILE   A 1 155 ? 25.713 10.019  -2.960  1.00 17.72  ? 135 ILE   A CA   1 
ATOM   2110 C C    . ILE   A 1 155 ? 25.313 9.419   -4.299  1.00 18.04  ? 135 ILE   A C    1 
ATOM   2111 O O    . ILE   A 1 155 ? 24.258 8.793   -4.409  1.00 18.06  ? 135 ILE   A O    1 
ATOM   2112 C CB   . ILE   A 1 155 ? 25.917 8.915   -1.919  1.00 17.03  ? 135 ILE   A CB   1 
ATOM   2113 C CG1  . ILE   A 1 155 ? 26.337 9.494   -0.567  1.00 18.09  ? 135 ILE   A CG1  1 
ATOM   2114 C CG2  . ILE   A 1 155 ? 26.967 7.924   -2.426  1.00 17.14  ? 135 ILE   A CG2  1 
ATOM   2115 C CD1  . ILE   A 1 155 ? 26.146 8.503   0.595   1.00 17.41  ? 135 ILE   A CD1  1 
ATOM   2116 H H    . ILE   A 1 155 ? 24.167 10.707  -1.935  1.00 21.02  ? 135 ILE   A H    1 
ATOM   2117 H HA   . ILE   A 1 155 ? 26.553 10.492  -3.066  1.00 21.26  ? 135 ILE   A HA   1 
ATOM   2118 H HB   . ILE   A 1 155 ? 25.071 8.458   -1.790  1.00 20.44  ? 135 ILE   A HB   1 
ATOM   2119 H HG12 . ILE   A 1 155 ? 27.276 9.734   -0.605  1.00 21.72  ? 135 ILE   A HG12 1 
ATOM   2120 H HG13 . ILE   A 1 155 ? 25.801 10.281  -0.380  1.00 21.72  ? 135 ILE   A HG13 1 
ATOM   2121 H HG21 . ILE   A 1 155 ? 27.231 7.342   -1.696  1.00 20.57  ? 135 ILE   A HG21 1 
ATOM   2122 H HG22 . ILE   A 1 155 ? 26.583 7.398   -3.145  1.00 20.57  ? 135 ILE   A HG22 1 
ATOM   2123 H HG23 . ILE   A 1 155 ? 27.736 8.417   -2.751  1.00 20.57  ? 135 ILE   A HG23 1 
ATOM   2124 H HD11 . ILE   A 1 155 ? 26.356 8.950   1.429   1.00 20.89  ? 135 ILE   A HD11 1 
ATOM   2125 H HD12 . ILE   A 1 155 ? 25.224 8.201   0.604   1.00 20.89  ? 135 ILE   A HD12 1 
ATOM   2126 H HD13 . ILE   A 1 155 ? 26.740 7.747   0.466   1.00 20.89  ? 135 ILE   A HD13 1 
ATOM   2127 N N    . LYS   A 1 156 ? 26.178 9.576   -5.304  1.00 18.62  ? 136 LYS   A N    1 
ATOM   2128 C CA   . LYS   A 1 156 ? 26.048 8.921   -6.598  1.00 18.84  ? 136 LYS   A CA   1 
ATOM   2129 C C    . LYS   A 1 156 ? 26.731 7.560   -6.619  1.00 18.17  ? 136 LYS   A C    1 
ATOM   2130 O O    . LYS   A 1 156 ? 26.238 6.641   -7.275  1.00 18.96  ? 136 LYS   A O    1 
ATOM   2131 C CB   . LYS   A 1 156 ? 26.656 9.831   -7.679  1.00 22.02  ? 136 LYS   A CB   1 
ATOM   2132 C CG   . LYS   A 1 156 ? 26.636 9.299   -9.110  1.00 26.36  ? 136 LYS   A CG   1 
ATOM   2133 C CD   . LYS   A 1 156 ? 25.204 9.198   -9.634  1.00 31.77  ? 136 LYS   A CD   1 
ATOM   2134 C CE   . LYS   A 1 156 ? 25.197 8.832   -11.121 1.00 37.25  ? 136 LYS   A CE   1 
ATOM   2135 H H    . LYS   A 1 156 ? 26.875 10.077  -5.255  1.00 22.35  ? 136 LYS   A H    1 
ATOM   2136 H HA   . LYS   A 1 156 ? 25.110 8.781   -6.804  1.00 22.61  ? 136 LYS   A HA   1 
ATOM   2137 H HB2  . LYS   A 1 156 ? 26.165 10.668  -7.679  1.00 26.42  ? 136 LYS   A HB2  1 
ATOM   2138 H HB3  . LYS   A 1 156 ? 27.585 9.992   -7.449  1.00 26.42  ? 136 LYS   A HB3  1 
ATOM   2139 H HG2  . LYS   A 1 156 ? 27.132 9.902   -9.687  1.00 31.63  ? 136 LYS   A HG2  1 
ATOM   2140 H HG3  . LYS   A 1 156 ? 27.034 8.415   -9.133  1.00 31.63  ? 136 LYS   A HG3  1 
ATOM   2141 H HD2  . LYS   A 1 156 ? 24.728 8.509   -9.145  1.00 38.13  ? 136 LYS   A HD2  1 
ATOM   2142 H HD3  . LYS   A 1 156 ? 24.757 10.052  -9.525  1.00 38.13  ? 136 LYS   A HD3  1 
ATOM   2143 N N    . GLU   A 1 157 ? 27.856 7.408   -5.918  1.00 16.95  ? 137 GLU   A N    1 
ATOM   2144 C CA   . GLU   A 1 157 ? 28.556 6.129   -5.896  1.00 16.25  ? 137 GLU   A CA   1 
ATOM   2145 C C    . GLU   A 1 157 ? 29.282 5.961   -4.575  1.00 15.58  ? 137 GLU   A C    1 
ATOM   2146 O O    . GLU   A 1 157 ? 30.166 6.765   -4.236  1.00 16.77  ? 137 GLU   A O    1 
ATOM   2147 C CB   . GLU   A 1 157 ? 29.563 6.028   -7.044  1.00 17.82  ? 137 GLU   A CB   1 
ATOM   2148 C CG   . GLU   A 1 157 ? 30.261 4.679   -7.149  1.00 19.13  ? 137 GLU   A CG   1 
ATOM   2149 C CD   . GLU   A 1 157 ? 31.423 4.719   -8.105  1.00 22.02  ? 137 GLU   A CD   1 
ATOM   2150 O OE1  . GLU   A 1 157 ? 32.432 5.414   -7.790  1.00 20.84  ? 137 GLU   A OE1  1 
ATOM   2151 O OE2  . GLU   A 1 157 ? 31.348 4.032   -9.158  1.00 25.28  ? 137 GLU   A OE2  1 
ATOM   2152 H H    . GLU   A 1 157 ? 28.228 8.027   -5.451  1.00 20.35  ? 137 GLU   A H    1 
ATOM   2153 H HA   . GLU   A 1 157 ? 27.895 5.423   -5.978  1.00 19.51  ? 137 GLU   A HA   1 
ATOM   2154 H HB2  . GLU   A 1 157 ? 29.096 6.184   -7.880  1.00 21.39  ? 137 GLU   A HB2  1 
ATOM   2155 H HB3  . GLU   A 1 157 ? 30.247 6.704   -6.916  1.00 21.39  ? 137 GLU   A HB3  1 
ATOM   2156 H HG2  . GLU   A 1 157 ? 30.595 4.424   -6.275  1.00 22.96  ? 137 GLU   A HG2  1 
ATOM   2157 H HG3  . GLU   A 1 157 ? 29.628 4.017   -7.468  1.00 22.96  ? 137 GLU   A HG3  1 
ATOM   2158 N N    . GLN   A 1 158 ? 28.953 4.883   -3.886  1.00 15.07  ? 138 GLN   A N    1 
ATOM   2159 C CA   . GLN   A 1 158 ? 29.676 4.442   -2.695  1.00 15.08  ? 138 GLN   A CA   1 
ATOM   2160 C C    . GLN   A 1 158 ? 30.343 3.110   -3.015  1.00 14.84  ? 138 GLN   A C    1 
ATOM   2161 O O    . GLN   A 1 158 ? 29.716 2.231   -3.601  1.00 16.16  ? 138 GLN   A O    1 
ATOM   2162 C CB   . GLN   A 1 158 ? 28.710 4.296   -1.514  1.00 16.47  ? 138 GLN   A CB   1 
ATOM   2163 C CG   . GLN   A 1 158 ? 29.348 3.734   -0.228  1.00 17.24  ? 138 GLN   A CG   1 
ATOM   2164 C CD   . GLN   A 1 158 ? 29.311 2.237   -0.154  1.00 19.08  ? 138 GLN   A CD   1 
ATOM   2165 O OE1  . GLN   A 1 158 ? 28.417 1.604   -0.737  1.00 19.62  ? 138 GLN   A OE1  1 
ATOM   2166 N NE2  . GLN   A 1 158 ? 30.239 1.653   0.581   1.00 21.49  ? 138 GLN   A NE2  1 
ATOM   2167 H H    . GLN   A 1 158 ? 28.294 4.370   -4.091  1.00 18.08  ? 138 GLN   A H    1 
ATOM   2168 H HA   . GLN   A 1 158 ? 30.361 5.082   -2.445  1.00 18.10  ? 138 GLN   A HA   1 
ATOM   2169 H HB2  . GLN   A 1 158 ? 28.346 5.170   -1.302  1.00 19.77  ? 138 GLN   A HB2  1 
ATOM   2170 H HB3  . GLN   A 1 158 ? 27.995 3.693   -1.773  1.00 19.77  ? 138 GLN   A HB3  1 
ATOM   2171 H HG2  . GLN   A 1 158 ? 30.277 4.012   -0.191  1.00 20.69  ? 138 GLN   A HG2  1 
ATOM   2172 H HG3  . GLN   A 1 158 ? 28.868 4.082   0.539   1.00 20.69  ? 138 GLN   A HG3  1 
ATOM   2173 H HE21 . GLN   A 1 158 ? 30.827 2.130   0.990   1.00 25.80  ? 138 GLN   A HE21 1 
ATOM   2174 H HE22 . GLN   A 1 158 ? 30.256 0.796   0.652   1.00 25.80  ? 138 GLN   A HE22 1 
ATOM   2175 N N    . ARG   A 1 159 ? 31.619 2.974   -2.646  1.00 13.98  ? 139 ARG   A N    1 
ATOM   2176 C CA   . ARG   A 1 159 ? 32.343 1.727   -2.868  1.00 14.78  ? 139 ARG   A CA   1 
ATOM   2177 C C    . ARG   A 1 159 ? 33.112 1.397   -1.609  1.00 15.35  ? 139 ARG   A C    1 
ATOM   2178 O O    . ARG   A 1 159 ? 33.781 2.260   -1.042  1.00 16.13  ? 139 ARG   A O    1 
ATOM   2179 C CB   . ARG   A 1 159 ? 33.355 1.843   -4.029  1.00 15.40  ? 139 ARG   A CB   1 
ATOM   2180 C CG   . ARG   A 1 159 ? 32.763 2.232   -5.366  1.00 16.60  ? 139 ARG   A CG   1 
ATOM   2181 C CD   . ARG   A 1 159 ? 33.823 2.412   -6.421  1.00 17.30  ? 139 ARG   A CD   1 
ATOM   2182 N NE   . ARG   A 1 159 ? 34.675 3.566   -6.139  1.00 17.10  ? 139 ARG   A NE   1 
ATOM   2183 C CZ   . ARG   A 1 159 ? 35.938 3.713   -6.568  1.00 16.28  ? 139 ARG   A CZ   1 
ATOM   2184 N NH1  . ARG   A 1 159 ? 36.505 2.829   -7.381  1.00 16.68  ? 139 ARG   A NH1  1 
ATOM   2185 N NH2  . ARG   A 1 159 ? 36.649 4.769   -6.174  1.00 16.43  ? 139 ARG   A NH2  1 
ATOM   2186 H H    . ARG   A 1 159 ? 32.083 3.591   -2.266  1.00 16.77  ? 139 ARG   A H    1 
ATOM   2187 H HA   . ARG   A 1 159 ? 31.706 1.025   -3.075  1.00 17.74  ? 139 ARG   A HA   1 
ATOM   2188 H HB2  . ARG   A 1 159 ? 34.012 2.518   -3.796  1.00 18.48  ? 139 ARG   A HB2  1 
ATOM   2189 H HB3  . ARG   A 1 159 ? 33.789 0.983   -4.144  1.00 18.48  ? 139 ARG   A HB3  1 
ATOM   2190 H HG2  . ARG   A 1 159 ? 32.156 1.535   -5.662  1.00 19.92  ? 139 ARG   A HG2  1 
ATOM   2191 H HG3  . ARG   A 1 159 ? 32.284 3.070   -5.271  1.00 19.92  ? 139 ARG   A HG3  1 
ATOM   2192 H HD2  . ARG   A 1 159 ? 34.383 1.620   -6.452  1.00 20.77  ? 139 ARG   A HD2  1 
ATOM   2193 H HD3  . ARG   A 1 159 ? 33.398 2.551   -7.282  1.00 20.77  ? 139 ARG   A HD3  1 
ATOM   2194 H HE   . ARG   A 1 159 ? 34.342 4.199   -5.662  1.00 20.52  ? 139 ARG   A HE   1 
ATOM   2195 H HH11 . ARG   A 1 159 ? 36.061 2.141   -7.645  1.00 20.02  ? 139 ARG   A HH11 1 
ATOM   2196 H HH12 . ARG   A 1 159 ? 37.316 2.944   -7.643  1.00 20.02  ? 139 ARG   A HH12 1 
ATOM   2197 H HH21 . ARG   A 1 159 ? 36.298 5.352   -5.648  1.00 19.71  ? 139 ARG   A HH21 1 
ATOM   2198 H HH22 . ARG   A 1 159 ? 37.459 4.868   -6.446  1.00 19.71  ? 139 ARG   A HH22 1 
ATOM   2199 N N    B GLU   A 1 160 ? 33.110 0.114   -1.254  0.49 15.52  ? 140 GLU   A N    1 
ATOM   2200 N N    D GLU   A 1 160 ? 33.013 0.162   -1.129  0.51 15.44  ? 140 GLU   A N    1 
ATOM   2201 C CA   B GLU   A 1 160 ? 33.767 -0.371  -0.050  0.49 16.76  ? 140 GLU   A CA   1 
ATOM   2202 C CA   D GLU   A 1 160 ? 33.875 -0.251  -0.029  0.51 16.66  ? 140 GLU   A CA   1 
ATOM   2203 C C    B GLU   A 1 160 ? 34.839 -1.413  -0.369  0.49 13.85  ? 140 GLU   A C    1 
ATOM   2204 C C    D GLU   A 1 160 ? 34.918 -1.241  -0.507  0.51 13.90  ? 140 GLU   A C    1 
ATOM   2205 O O    B GLU   A 1 160 ? 34.572 -2.389  -1.092  0.49 12.46  ? 140 GLU   A O    1 
ATOM   2206 O O    D GLU   A 1 160 ? 34.703 -1.988  -1.465  0.51 12.50  ? 140 GLU   A O    1 
ATOM   2207 C CB   B GLU   A 1 160 ? 32.691 -0.919  0.886   0.49 20.87  ? 140 GLU   A CB   1 
ATOM   2208 C CB   D GLU   A 1 160 ? 33.144 -0.857  1.166   0.51 21.12  ? 140 GLU   A CB   1 
ATOM   2209 C CG   B GLU   A 1 160 ? 33.050 -2.108  1.637   0.49 23.25  ? 140 GLU   A CG   1 
ATOM   2210 C CG   D GLU   A 1 160 ? 32.183 -1.885  0.800   0.51 24.03  ? 140 GLU   A CG   1 
ATOM   2211 C CD   B GLU   A 1 160 ? 32.014 -2.454  2.626   0.49 27.10  ? 140 GLU   A CD   1 
ATOM   2212 C CD   D GLU   A 1 160 ? 30.949 -1.898  1.677   0.51 27.10  ? 140 GLU   A CD   1 
ATOM   2213 O OE1  B GLU   A 1 160 ? 31.095 -1.655  2.740   0.49 25.99  ? 140 GLU   A OE1  1 
ATOM   2214 O OE1  D GLU   A 1 160 ? 30.418 -0.820  2.083   0.51 26.43  ? 140 GLU   A OE1  1 
ATOM   2215 O OE2  B GLU   A 1 160 ? 32.114 -3.493  3.288   0.49 28.85  ? 140 GLU   A OE2  1 
ATOM   2216 O OE2  D GLU   A 1 160 ? 30.470 -3.022  1.917   0.51 28.82  ? 140 GLU   A OE2  1 
ATOM   2217 H H    B GLU   A 1 160 ? 32.724 -0.506  -1.708  0.49 18.62  ? 140 GLU   A H    1 
ATOM   2218 H H    D GLU   A 1 160 ? 32.468 -0.438  -1.416  0.51 18.54  ? 140 GLU   A H    1 
ATOM   2219 H HA   B GLU   A 1 160 ? 34.254 0.345   0.387   0.49 20.11  ? 140 GLU   A HA   1 
ATOM   2220 H HA   D GLU   A 1 160 ? 34.305 0.558   0.289   0.51 19.99  ? 140 GLU   A HA   1 
ATOM   2221 H HB2  B GLU   A 1 160 ? 32.470 -0.228  1.531   0.49 25.04  ? 140 GLU   A HB2  1 
ATOM   2222 H HB2  D GLU   A 1 160 ? 33.796 -1.260  1.760   0.51 25.34  ? 140 GLU   A HB2  1 
ATOM   2223 H HB3  B GLU   A 1 160 ? 31.910 -1.140  0.355   0.49 25.04  ? 140 GLU   A HB3  1 
ATOM   2224 H HB3  D GLU   A 1 160 ? 32.663 -0.153  1.628   0.51 25.34  ? 140 GLU   A HB3  1 
ATOM   2225 H HG2  B GLU   A 1 160 ? 33.151 -2.855  1.026   0.49 27.90  ? 140 GLU   A HG2  1 
ATOM   2226 H HG2  D GLU   A 1 160 ? 31.895 -1.733  -0.114  0.51 28.84  ? 140 GLU   A HG2  1 
ATOM   2227 H HG3  B GLU   A 1 160 ? 33.883 -1.950  2.109   0.49 27.90  ? 140 GLU   A HG3  1 
ATOM   2228 H HG3  D GLU   A 1 160 ? 32.609 -2.753  0.873   0.51 28.84  ? 140 GLU   A HG3  1 
ATOM   2229 N N    . PHE   A 1 161 ? 36.053 -1.196  0.177   1.00 14.23  ? 141 PHE   A N    1 
ATOM   2230 C CA   . PHE   A 1 161 ? 37.217 -2.024  -0.111  1.00 13.28  ? 141 PHE   A CA   1 
ATOM   2231 C C    . PHE   A 1 161 ? 37.745 -2.609  1.190   1.00 14.14  ? 141 PHE   A C    1 
ATOM   2232 O O    . PHE   A 1 161 ? 37.956 -1.884  2.167   1.00 15.66  ? 141 PHE   A O    1 
ATOM   2233 C CB   . PHE   A 1 161 ? 38.327 -1.181  -0.717  1.00 14.69  ? 141 PHE   A CB   1 
ATOM   2234 C CG   . PHE   A 1 161 ? 37.929 -0.445  -1.973  1.00 14.58  ? 141 PHE   A CG   1 
ATOM   2235 C CD1  . PHE   A 1 161 ? 37.329 0.805   -1.913  1.00 15.60  ? 141 PHE   A CD1  1 
ATOM   2236 C CD2  . PHE   A 1 161 ? 38.160 -1.005  -3.223  1.00 15.75  ? 141 PHE   A CD2  1 
ATOM   2237 C CE1  . PHE   A 1 161 ? 36.992 1.465   -3.067  1.00 16.94  ? 141 PHE   A CE1  1 
ATOM   2238 C CE2  . PHE   A 1 161 ? 37.799 -0.355  -4.357  1.00 17.52  ? 141 PHE   A CE2  1 
ATOM   2239 C CZ   . PHE   A 1 161 ? 37.229 0.916   -4.270  1.00 17.01  ? 141 PHE   A CZ   1 
ATOM   2240 H H    B PHE   A 1 161 ? 36.220 -0.557  0.728   0.49 17.08  ? 141 PHE   A H    1 
ATOM   2241 H H    D PHE   A 1 161 ? 36.181 -0.669  0.844   0.51 17.08  ? 141 PHE   A H    1 
ATOM   2242 H HA   . PHE   A 1 161 ? 36.959 -2.738  -0.715  1.00 15.94  ? 141 PHE   A HA   1 
ATOM   2243 H HB2  . PHE   A 1 161 ? 38.606 -0.520  -0.065  1.00 17.64  ? 141 PHE   A HB2  1 
ATOM   2244 H HB3  . PHE   A 1 161 ? 39.071 -1.762  -0.940  1.00 17.64  ? 141 PHE   A HB3  1 
ATOM   2245 H HD1  . PHE   A 1 161 ? 37.156 1.196   -1.088  1.00 18.73  ? 141 PHE   A HD1  1 
ATOM   2246 H HD2  . PHE   A 1 161 ? 38.567 -1.839  -3.282  1.00 18.90  ? 141 PHE   A HD2  1 
ATOM   2247 H HE1  . PHE   A 1 161 ? 36.593 2.303   -3.016  1.00 20.33  ? 141 PHE   A HE1  1 
ATOM   2248 H HE2  . PHE   A 1 161 ? 37.931 -0.753  -5.187  1.00 21.03  ? 141 PHE   A HE2  1 
ATOM   2249 H HZ   . PHE   A 1 161 ? 37.014 1.384   -5.044  1.00 20.41  ? 141 PHE   A HZ   1 
ATOM   2250 N N    . MET   A 1 162 ? 37.965 -3.916  1.202   1.00 14.40  ? 142 MET   A N    1 
ATOM   2251 C CA   . MET   A 1 162 ? 38.462 -4.595  2.381   1.00 14.62  ? 142 MET   A CA   1 
ATOM   2252 C C    . MET   A 1 162 ? 39.298 -5.785  1.929   1.00 14.52  ? 142 MET   A C    1 
ATOM   2253 O O    . MET   A 1 162 ? 39.380 -6.096  0.738   1.00 15.88  ? 142 MET   A O    1 
ATOM   2254 C CB   . MET   A 1 162 ? 37.354 -4.983  3.350   1.00 14.77  ? 142 MET   A CB   1 
ATOM   2255 C CG   . MET   A 1 162 ? 36.185 -5.785  2.781   1.00 15.86  ? 142 MET   A CG   1 
ATOM   2256 S SD   . MET   A 1 162 ? 36.664 -7.335  2.124   1.00 19.24  ? 142 MET   A SD   1 
ATOM   2257 C CE   . MET   A 1 162 ? 35.176 -8.233  1.883   1.00 17.69  ? 142 MET   A CE   1 
ATOM   2258 H H    . MET   A 1 162 ? 37.832 -4.435  0.530   1.00 17.28  ? 142 MET   A H    1 
ATOM   2259 H HA   . MET   A 1 162 ? 39.032 -3.979  2.867   1.00 17.55  ? 142 MET   A HA   1 
ATOM   2260 H HB2  . MET   A 1 162 ? 37.748 -5.520  4.056   1.00 17.72  ? 142 MET   A HB2  1 
ATOM   2261 H HB3  . MET   A 1 162 ? 36.983 -4.167  3.722   1.00 17.72  ? 142 MET   A HB3  1 
ATOM   2262 H HG2  . MET   A 1 162 ? 35.542 -5.947  3.489   1.00 19.04  ? 142 MET   A HG2  1 
ATOM   2263 H HG3  . MET   A 1 162 ? 35.772 -5.274  2.068   1.00 19.04  ? 142 MET   A HG3  1 
ATOM   2264 H HE1  . MET   A 1 162 ? 35.384 -9.084  1.467   1.00 21.24  ? 142 MET   A HE1  1 
ATOM   2265 H HE2  . MET   A 1 162 ? 34.754 -8.381  2.744   1.00 21.24  ? 142 MET   A HE2  1 
ATOM   2266 H HE3  . MET   A 1 162 ? 34.586 -7.719  1.310   1.00 21.24  ? 142 MET   A HE3  1 
ATOM   2267 N N    . ASN   A 1 163 ? 39.896 -6.466  2.897   1.00 14.52  ? 143 ASN   A N    1 
ATOM   2268 C CA   . ASN   A 1 163 ? 40.607 -7.713  2.648   1.00 13.63  ? 143 ASN   A CA   1 
ATOM   2269 C C    . ASN   A 1 163 ? 39.626 -8.866  2.848   1.00 14.08  ? 143 ASN   A C    1 
ATOM   2270 O O    . ASN   A 1 163 ? 39.264 -9.157  3.990   1.00 14.24  ? 143 ASN   A O    1 
ATOM   2271 C CB   . ASN   A 1 163 ? 41.755 -7.833  3.635   1.00 14.60  ? 143 ASN   A CB   1 
ATOM   2272 C CG   . ASN   A 1 163 ? 42.557 -9.079  3.459   1.00 15.56  ? 143 ASN   A CG   1 
ATOM   2273 O OD1  . ASN   A 1 163 ? 42.250 -9.950  2.645   1.00 14.56  ? 143 ASN   A OD1  1 
ATOM   2274 N ND2  . ASN   A 1 163 ? 43.656 -9.153  4.190   1.00 19.73  ? 143 ASN   A ND2  1 
ATOM   2275 H H    . ASN   A 1 163 ? 39.905 -6.223  3.722   1.00 17.42  ? 143 ASN   A H    1 
ATOM   2276 H HA   . ASN   A 1 163 ? 40.950 -7.743  1.741   1.00 16.36  ? 143 ASN   A HA   1 
ATOM   2277 H HB2  . ASN   A 1 163 ? 42.351 -7.076  3.517   1.00 17.52  ? 143 ASN   A HB2  1 
ATOM   2278 H HB3  . ASN   A 1 163 ? 41.396 -7.835  4.536   1.00 17.52  ? 143 ASN   A HB3  1 
ATOM   2279 H HD21 . ASN   A 1 163 ? 44.163 -9.845  4.136   1.00 23.68  ? 143 ASN   A HD21 1 
ATOM   2280 H HD22 . ASN   A 1 163 ? 43.864 -8.509  4.721   1.00 23.68  ? 143 ASN   A HD22 1 
ATOM   2281 N N    . PRO   A 1 164 ? 39.220 -9.579  1.801   1.00 13.37  ? 144 PRO   A N    1 
ATOM   2282 C CA   . PRO   A 1 164 ? 38.222 -10.636 2.003   1.00 14.13  ? 144 PRO   A CA   1 
ATOM   2283 C C    . PRO   A 1 164 ? 38.695 -11.757 2.890   1.00 13.93  ? 144 PRO   A C    1 
ATOM   2284 O O    . PRO   A 1 164 ? 37.862 -12.518 3.402   1.00 15.06  ? 144 PRO   A O    1 
ATOM   2285 C CB   . PRO   A 1 164 ? 37.923 -11.113 0.581   1.00 15.38  ? 144 PRO   A CB   1 
ATOM   2286 C CG   . PRO   A 1 164 ? 38.289 -9.938  -0.302  1.00 15.74  ? 144 PRO   A CG   1 
ATOM   2287 C CD   . PRO   A 1 164 ? 39.456 -9.318  0.375   1.00 13.59  ? 144 PRO   A CD   1 
ATOM   2288 H HA   . PRO   A 1 164 ? 37.412 -10.262 2.383   1.00 16.96  ? 144 PRO   A HA   1 
ATOM   2289 H HB2  . PRO   A 1 164 ? 38.466 -11.890 0.371   1.00 18.46  ? 144 PRO   A HB2  1 
ATOM   2290 H HB3  . PRO   A 1 164 ? 36.982 -11.333 0.496   1.00 18.46  ? 144 PRO   A HB3  1 
ATOM   2291 H HG2  . PRO   A 1 164 ? 38.526 -10.250 -1.190  1.00 18.89  ? 144 PRO   A HG2  1 
ATOM   2292 H HG3  . PRO   A 1 164 ? 37.546 -9.317  -0.355  1.00 18.89  ? 144 PRO   A HG3  1 
ATOM   2293 H HD2  . PRO   A 1 164 ? 40.282 -9.733  0.083   1.00 16.31  ? 144 PRO   A HD2  1 
ATOM   2294 H HD3  . PRO   A 1 164 ? 39.485 -8.364  0.202   1.00 16.31  ? 144 PRO   A HD3  1 
ATOM   2295 N N    . CYS   A 1 165 ? 40.003 -11.938 3.055   1.00 14.16  ? 145 CYS   A N    1 
ATOM   2296 C CA   . CYS   A 1 165 ? 40.487 -13.017 3.907   1.00 14.50  ? 145 CYS   A CA   1 
ATOM   2297 C C    . CYS   A 1 165 ? 39.913 -12.943 5.312   1.00 15.72  ? 145 CYS   A C    1 
ATOM   2298 O O    . CYS   A 1 165 ? 39.648 -13.985 5.928   1.00 16.39  ? 145 CYS   A O    1 
ATOM   2299 C CB   . CYS   A 1 165 ? 42.009 -13.022 3.944   1.00 16.48  ? 145 CYS   A CB   1 
ATOM   2300 S SG   . CYS   A 1 165 ? 42.778 -13.369 2.348   1.00 18.62  ? 145 CYS   A SG   1 
ATOM   2301 H H    . CYS   A 1 165 ? 40.619 -11.460 2.692   1.00 16.99  ? 145 CYS   A H    1 
ATOM   2302 H HA   . CYS   A 1 165 ? 40.199 -13.860 3.522   1.00 17.40  ? 145 CYS   A HA   1 
ATOM   2303 H HB2  . CYS   A 1 165 ? 42.316 -12.150 4.237   1.00 19.78  ? 145 CYS   A HB2  1 
ATOM   2304 H HB3  . CYS   A 1 165 ? 42.303 -13.704 4.568   1.00 19.78  ? 145 CYS   A HB3  1 
ATOM   2305 H HG   . CYS   A 1 165 ? 43.868 -12.866 2.322   1.00 22.35  ? 145 CYS   A HG   1 
ATOM   2306 N N    . GLU   A 1 166 ? 39.686 -11.731 5.836   1.00 15.52  ? 146 GLU   A N    1 
ATOM   2307 C CA   . GLU   A 1 166 ? 39.116 -11.640 7.180   1.00 16.23  ? 146 GLU   A CA   1 
ATOM   2308 C C    . GLU   A 1 166 ? 37.641 -12.053 7.189   1.00 16.61  ? 146 GLU   A C    1 
ATOM   2309 O O    . GLU   A 1 166 ? 37.163 -12.598 8.186   1.00 18.22  ? 146 GLU   A O    1 
ATOM   2310 C CB   . GLU   A 1 166 ? 39.290 -10.223 7.739   1.00 18.92  ? 146 GLU   A CB   1 
ATOM   2311 C CG   . GLU   A 1 166 ? 40.730 -9.824  7.939   1.00 23.47  ? 146 GLU   A CG   1 
ATOM   2312 C CD   . GLU   A 1 166 ? 41.486 -10.822 8.801   1.00 32.56  ? 146 GLU   A CD   1 
ATOM   2313 O OE1  . GLU   A 1 166 ? 40.987 -11.202 9.874   1.00 32.93  ? 146 GLU   A OE1  1 
ATOM   2314 O OE2  . GLU   A 1 166 ? 42.572 -11.263 8.389   1.00 40.93  ? 146 GLU   A OE2  1 
ATOM   2315 H H    . GLU   A 1 166 ? 39.848 -10.980 5.449   1.00 18.62  ? 146 GLU   A H    1 
ATOM   2316 H HA   . GLU   A 1 166 ? 39.597 -12.244 7.768   1.00 19.48  ? 146 GLU   A HA   1 
ATOM   2317 H HB2  . GLU   A 1 166 ? 38.891 -9.592  7.121   1.00 22.70  ? 146 GLU   A HB2  1 
ATOM   2318 H HB3  . GLU   A 1 166 ? 38.846 -10.170 8.600   1.00 22.70  ? 146 GLU   A HB3  1 
ATOM   2319 H HG2  . GLU   A 1 166 ? 41.170 -9.776  7.075   1.00 28.17  ? 146 GLU   A HG2  1 
ATOM   2320 H HG3  . GLU   A 1 166 ? 40.764 -8.959  8.376   1.00 28.17  ? 146 GLU   A HG3  1 
ATOM   2321 N N    . GLN   A 1 167 ? 36.916 -11.790 6.102   1.00 14.91  ? 147 GLN   A N    1 
ATOM   2322 C CA   . GLN   A 1 167 ? 35.541 -12.255 6.020   1.00 14.98  ? 147 GLN   A CA   1 
ATOM   2323 C C    . GLN   A 1 167 ? 35.510 -13.775 5.903   1.00 15.15  ? 147 GLN   A C    1 
ATOM   2324 O O    . GLN   A 1 167 ? 34.683 -14.430 6.548   1.00 15.87  ? 147 GLN   A O    1 
ATOM   2325 C CB   . GLN   A 1 167 ? 34.787 -11.555 4.894   1.00 15.14  ? 147 GLN   A CB   1 
ATOM   2326 C CG   . GLN   A 1 167 ? 33.280 -11.798 5.006   1.00 16.44  ? 147 GLN   A CG   1 
ATOM   2327 C CD   . GLN   A 1 167 ? 32.415 -10.911 4.118   1.00 16.50  ? 147 GLN   A CD   1 
ATOM   2328 O OE1  . GLN   A 1 167 ? 32.861 -9.916  3.588   1.00 18.75  ? 147 GLN   A OE1  1 
ATOM   2329 N NE2  . GLN   A 1 167 ? 31.155 -11.314 3.928   1.00 19.38  ? 147 GLN   A NE2  1 
ATOM   2330 H H    . GLN   A 1 167 ? 37.194 -11.354 5.415   1.00 17.90  ? 147 GLN   A H    1 
ATOM   2331 H HA   . GLN   A 1 167 ? 35.064 -12.013 6.830   1.00 17.98  ? 147 GLN   A HA   1 
ATOM   2332 H HB2  . GLN   A 1 167 ? 34.950 -10.600 4.943   1.00 18.17  ? 147 GLN   A HB2  1 
ATOM   2333 H HB3  . GLN   A 1 167 ? 35.092 -11.900 4.040   1.00 18.17  ? 147 GLN   A HB3  1 
ATOM   2334 H HG2  . GLN   A 1 167 ? 33.098 -12.719 4.761   1.00 19.73  ? 147 GLN   A HG2  1 
ATOM   2335 H HG3  . GLN   A 1 167 ? 33.011 -11.639 5.924   1.00 19.73  ? 147 GLN   A HG3  1 
ATOM   2336 H HE21 . GLN   A 1 167 ? 30.874 -12.038 4.298   1.00 23.26  ? 147 GLN   A HE21 1 
ATOM   2337 H HE22 . GLN   A 1 167 ? 30.624 -10.850 3.435   1.00 23.26  ? 147 GLN   A HE22 1 
ATOM   2338 N N    . PHE   A 1 168 ? 36.432 -14.356 5.124   1.00 15.18  ? 148 PHE   A N    1 
ATOM   2339 C CA   . PHE   A 1 168 ? 36.551 -15.817 5.102   1.00 16.65  ? 148 PHE   A CA   1 
ATOM   2340 C C    . PHE   A 1 168 ? 36.705 -16.373 6.512   1.00 16.40  ? 148 PHE   A C    1 
ATOM   2341 O O    . PHE   A 1 168 ? 35.976 -17.302 6.912   1.00 17.70  ? 148 PHE   A O    1 
ATOM   2342 C CB   . PHE   A 1 168 ? 37.755 -16.268 4.267   1.00 17.44  ? 148 PHE   A CB   1 
ATOM   2343 C CG   . PHE   A 1 168 ? 37.743 -15.902 2.812   1.00 19.29  ? 148 PHE   A CG   1 
ATOM   2344 C CD1  . PHE   A 1 168 ? 36.592 -15.556 2.145   1.00 21.16  ? 148 PHE   A CD1  1 
ATOM   2345 C CD2  . PHE   A 1 168 ? 38.959 -15.879 2.108   1.00 18.64  ? 148 PHE   A CD2  1 
ATOM   2346 C CE1  . PHE   A 1 168 ? 36.624 -15.209 0.797   1.00 24.26  ? 148 PHE   A CE1  1 
ATOM   2347 C CE2  . PHE   A 1 168 ? 39.022 -15.539 0.772   1.00 20.87  ? 148 PHE   A CE2  1 
ATOM   2348 C CZ   . PHE   A 1 168 ? 37.860 -15.182 0.106   1.00 23.78  ? 148 PHE   A CZ   1 
ATOM   2349 H H    . PHE   A 1 168 ? 36.985 -13.938 4.614   1.00 18.22  ? 148 PHE   A H    1 
ATOM   2350 H HA   . PHE   A 1 168 ? 35.744 -16.164 4.692   1.00 19.99  ? 148 PHE   A HA   1 
ATOM   2351 H HB2  . PHE   A 1 168 ? 38.553 -15.872 4.652   1.00 20.93  ? 148 PHE   A HB2  1 
ATOM   2352 H HB3  . PHE   A 1 168 ? 37.809 -17.235 4.316   1.00 20.93  ? 148 PHE   A HB3  1 
ATOM   2353 H HD1  . PHE   A 1 168 ? 35.781 -15.554 2.601   1.00 25.40  ? 148 PHE   A HD1  1 
ATOM   2354 H HD2  . PHE   A 1 168 ? 39.744 -16.099 2.555   1.00 22.37  ? 148 PHE   A HD2  1 
ATOM   2355 H HE1  . PHE   A 1 168 ? 35.835 -14.996 0.352   1.00 29.12  ? 148 PHE   A HE1  1 
ATOM   2356 H HE2  . PHE   A 1 168 ? 39.836 -15.550 0.322   1.00 25.05  ? 148 PHE   A HE2  1 
ATOM   2357 H HZ   . PHE   A 1 168 ? 37.891 -14.926 -0.787  1.00 28.53  ? 148 PHE   A HZ   1 
ATOM   2358 N N    . ARG   A 1 169 ? 37.644 -15.812 7.294   1.00 17.62  ? 149 ARG   A N    1 
ATOM   2359 C CA   . ARG   A 1 169 ? 37.868 -16.293 8.651   1.00 19.06  ? 149 ARG   A CA   1 
ATOM   2360 C C    . ARG   A 1 169 ? 36.592 -16.217 9.479   1.00 18.64  ? 149 ARG   A C    1 
ATOM   2361 O O    . ARG   A 1 169 ? 36.277 -17.148 10.232  1.00 20.38  ? 149 ARG   A O    1 
ATOM   2362 C CB   . ARG   A 1 169 ? 38.988 -15.507 9.320   1.00 22.47  ? 149 ARG   A CB   1 
ATOM   2363 C CG   . ARG   A 1 169 ? 40.337 -15.838 8.809   1.00 24.65  ? 149 ARG   A CG   1 
ATOM   2364 C CD   . ARG   A 1 169 ? 41.418 -15.134 9.634   1.00 28.74  ? 149 ARG   A CD   1 
ATOM   2365 N NE   . ARG   A 1 169 ? 42.714 -15.657 9.243   1.00 33.00  ? 149 ARG   A NE   1 
ATOM   2366 C CZ   . ARG   A 1 169 ? 43.444 -15.189 8.243   1.00 35.25  ? 149 ARG   A CZ   1 
ATOM   2367 N NH1  . ARG   A 1 169 ? 43.139 -14.050 7.638   1.00 36.42  ? 149 ARG   A NH1  1 
ATOM   2368 N NH2  . ARG   A 1 169 ? 44.507 -15.881 7.847   1.00 35.99  ? 149 ARG   A NH2  1 
ATOM   2369 H H    . ARG   A 1 169 ? 38.155 -15.161 7.058   1.00 21.15  ? 149 ARG   A H    1 
ATOM   2370 H HA   . ARG   A 1 169 ? 38.147 -17.221 8.607   1.00 22.87  ? 149 ARG   A HA   1 
ATOM   2371 H HB2  . ARG   A 1 169 ? 38.839 -14.560 9.169   1.00 26.97  ? 149 ARG   A HB2  1 
ATOM   2372 H HB3  . ARG   A 1 169 ? 38.977 -15.696 10.272  1.00 26.97  ? 149 ARG   A HB3  1 
ATOM   2373 H HG2  . ARG   A 1 169 ? 40.480 -16.796 8.868   1.00 29.59  ? 149 ARG   A HG2  1 
ATOM   2374 H HG3  . ARG   A 1 169 ? 40.415 -15.548 7.887   1.00 29.59  ? 149 ARG   A HG3  1 
ATOM   2375 H HD2  . ARG   A 1 169 ? 41.396 -14.179 9.463   1.00 34.48  ? 149 ARG   A HD2  1 
ATOM   2376 H HD3  . ARG   A 1 169 ? 41.278 -15.304 10.579  1.00 34.48  ? 149 ARG   A HD3  1 
ATOM   2377 H HE   . ARG   A 1 169 ? 43.031 -16.318 9.693   1.00 39.60  ? 149 ARG   A HE   1 
ATOM   2378 H HH11 . ARG   A 1 169 ? 42.454 -13.598 7.893   1.00 43.71  ? 149 ARG   A HH11 1 
ATOM   2379 H HH12 . ARG   A 1 169 ? 43.627 -13.764 6.990   1.00 43.71  ? 149 ARG   A HH12 1 
ATOM   2380 H HH21 . ARG   A 1 169 ? 44.711 -16.619 8.240   1.00 43.20  ? 149 ARG   A HH21 1 
ATOM   2381 H HH22 . ARG   A 1 169 ? 44.992 -15.591 7.199   1.00 43.20  ? 149 ARG   A HH22 1 
ATOM   2382 N N    . SER   A 1 170 ? 35.827 -15.134 9.323   1.00 18.35  ? 150 SER   A N    1 
ATOM   2383 C CA   . SER   A 1 170 ? 34.619 -14.966 10.119  1.00 18.58  ? 150 SER   A CA   1 
ATOM   2384 C C    . SER   A 1 170 ? 33.562 -15.995 9.782   1.00 18.91  ? 150 SER   A C    1 
ATOM   2385 O O    . SER   A 1 170 ? 32.701 -16.260 10.631  1.00 20.55  ? 150 SER   A O    1 
ATOM   2386 C CB   . SER   A 1 170 ? 34.023 -13.557 9.939   1.00 19.20  ? 150 SER   A CB   1 
ATOM   2387 O OG   . SER   A 1 170 ? 33.292 -13.396 8.714   1.00 18.68  ? 150 SER   A OG   1 
ATOM   2388 H H    . SER   A 1 170 ? 35.985 -14.494 8.771   1.00 22.02  ? 150 SER   A H    1 
ATOM   2389 H HA   . SER   A 1 170 ? 34.867 -15.064 11.052  1.00 22.30  ? 150 SER   A HA   1 
ATOM   2390 H HB2  . SER   A 1 170 ? 33.420 -13.384 10.678  1.00 23.04  ? 150 SER   A HB2  1 
ATOM   2391 H HB3  . SER   A 1 170 ? 34.750 -12.915 9.946   1.00 23.04  ? 150 SER   A HB3  1 
ATOM   2392 H HG   . SER   A 1 170 ? 33.797 -13.537 8.057   1.00 22.42  ? 150 SER   A HG   1 
ATOM   2393 N N    . LEU   A 1 171 ? 33.615 -16.554 8.573   1.00 17.45  ? 151 LEU   A N    1 
ATOM   2394 C CA   . LEU   A 1 171 ? 32.695 -17.565 8.080   1.00 18.09  ? 151 LEU   A CA   1 
ATOM   2395 C C    . LEU   A 1 171 ? 33.218 -18.987 8.285   1.00 19.74  ? 151 LEU   A C    1 
ATOM   2396 O O    . LEU   A 1 171 ? 32.536 -19.950 7.902   1.00 21.43  ? 151 LEU   A O    1 
ATOM   2397 C CB   . LEU   A 1 171 ? 32.427 -17.325 6.596   1.00 18.55  ? 151 LEU   A CB   1 
ATOM   2398 C CG   . LEU   A 1 171 ? 31.659 -16.045 6.286   1.00 18.02  ? 151 LEU   A CG   1 
ATOM   2399 C CD1  . LEU   A 1 171 ? 31.622 -15.852 4.780   1.00 20.59  ? 151 LEU   A CD1  1 
ATOM   2400 C CD2  . LEU   A 1 171 ? 30.242 -16.062 6.864   1.00 19.96  ? 151 LEU   A CD2  1 
ATOM   2401 H H    . LEU   A 1 171 ? 34.211 -16.349 7.989   1.00 20.95  ? 151 LEU   A H    1 
ATOM   2402 H HA   . LEU   A 1 171 ? 31.853 -17.491 8.556   1.00 21.72  ? 151 LEU   A HA   1 
ATOM   2403 H HB2  . LEU   A 1 171 ? 33.278 -17.275 6.133   1.00 22.26  ? 151 LEU   A HB2  1 
ATOM   2404 H HB3  . LEU   A 1 171 ? 31.907 -18.069 6.253   1.00 22.26  ? 151 LEU   A HB3  1 
ATOM   2405 H HG   . LEU   A 1 171 ? 32.111 -15.296 6.705   1.00 21.63  ? 151 LEU   A HG   1 
ATOM   2406 H HD11 . LEU   A 1 171 ? 31.146 -15.031 4.578   1.00 24.71  ? 151 LEU   A HD11 1 
ATOM   2407 H HD12 . LEU   A 1 171 ? 32.531 -15.798 4.446   1.00 24.71  ? 151 LEU   A HD12 1 
ATOM   2408 H HD13 . LEU   A 1 171 ? 31.165 -16.606 4.376   1.00 24.71  ? 151 LEU   A HD13 1 
ATOM   2409 H HD21 . LEU   A 1 171 ? 29.757 -15.290 6.533   1.00 23.96  ? 151 LEU   A HD21 1 
ATOM   2410 H HD22 . LEU   A 1 171 ? 29.797 -16.877 6.584   1.00 23.96  ? 151 LEU   A HD22 1 
ATOM   2411 H HD23 . LEU   A 1 171 ? 30.295 -16.030 7.832   1.00 23.96  ? 151 LEU   A HD23 1 
ATOM   2412 N N    . GLY   A 1 172 ? 34.406 -19.135 8.866   1.00 19.17  ? 152 GLY   A N    1 
ATOM   2413 C CA   . GLY   A 1 172 ? 35.001 -20.443 9.030   1.00 21.63  ? 152 GLY   A CA   1 
ATOM   2414 C C    . GLY   A 1 172 ? 35.596 -21.046 7.782   1.00 21.93  ? 152 GLY   A C    1 
ATOM   2415 O O    . GLY   A 1 172 ? 35.890 -22.252 7.769   1.00 25.12  ? 152 GLY   A O    1 
ATOM   2416 H H    . GLY   A 1 172 ? 34.883 -18.489 9.173   1.00 23.01  ? 152 GLY   A H    1 
ATOM   2417 H HA2  . GLY   A 1 172 ? 35.709 -20.379 9.691   1.00 25.96  ? 152 GLY   A HA2  1 
ATOM   2418 H HA3  . GLY   A 1 172 ? 34.320 -21.053 9.355   1.00 25.96  ? 152 GLY   A HA3  1 
ATOM   2419 N N    . ILE   A 1 173 ? 35.809 -20.244 6.748   1.00 20.72  ? 153 ILE   A N    1 
ATOM   2420 C CA   . ILE   A 1 173 ? 36.378 -20.677 5.479   1.00 20.74  ? 153 ILE   A CA   1 
ATOM   2421 C C    . ILE   A 1 173 ? 37.898 -20.611 5.615   1.00 21.43  ? 153 ILE   A C    1 
ATOM   2422 O O    . ILE   A 1 173 ? 38.460 -19.580 6.046   1.00 21.98  ? 153 ILE   A O    1 
ATOM   2423 C CB   . ILE   A 1 173 ? 35.893 -19.746 4.346   1.00 20.72  ? 153 ILE   A CB   1 
ATOM   2424 C CG1  . ILE   A 1 173 ? 34.367 -19.849 4.172   1.00 21.14  ? 153 ILE   A CG1  1 
ATOM   2425 C CG2  . ILE   A 1 173 ? 36.621 -20.049 3.040   1.00 21.08  ? 153 ILE   A CG2  1 
ATOM   2426 C CD1  . ILE   A 1 173 ? 33.836 -18.840 3.250   1.00 20.76  ? 153 ILE   A CD1  1 
ATOM   2427 H H    . ILE   A 1 173 ? 35.623 -19.404 6.757   1.00 24.87  ? 153 ILE   A H    1 
ATOM   2428 H HA   . ILE   A 1 173 ? 36.114 -21.588 5.275   1.00 24.89  ? 153 ILE   A HA   1 
ATOM   2429 H HB   . ILE   A 1 173 ? 36.105 -18.833 4.597   1.00 24.87  ? 153 ILE   A HB   1 
ATOM   2430 H HG12 . ILE   A 1 173 ? 34.146 -20.725 3.820   1.00 25.37  ? 153 ILE   A HG12 1 
ATOM   2431 H HG13 . ILE   A 1 173 ? 33.941 -19.722 5.035   1.00 25.37  ? 153 ILE   A HG13 1 
ATOM   2432 H HG21 . ILE   A 1 173 ? 36.226 -19.521 2.328   1.00 25.29  ? 153 ILE   A HG21 1 
ATOM   2433 H HG22 . ILE   A 1 173 ? 37.558 -19.822 3.140   1.00 25.29  ? 153 ILE   A HG22 1 
ATOM   2434 H HG23 . ILE   A 1 173 ? 36.529 -20.994 2.839   1.00 25.29  ? 153 ILE   A HG23 1 
ATOM   2435 H HD11 . ILE   A 1 173 ? 32.873 -18.792 3.354   1.00 24.92  ? 153 ILE   A HD11 1 
ATOM   2436 H HD12 . ILE   A 1 173 ? 34.235 -17.981 3.459   1.00 24.92  ? 153 ILE   A HD12 1 
ATOM   2437 H HD13 . ILE   A 1 173 ? 34.058 -19.096 2.341   1.00 24.92  ? 153 ILE   A HD13 1 
ATOM   2438 N N    . GLU   A 1 174 ? 38.571 -21.695 5.222   1.00 23.70  ? 154 GLU   A N    1 
ATOM   2439 C CA   . GLU   A 1 174 ? 40.025 -21.746 5.262   1.00 25.57  ? 154 GLU   A CA   1 
ATOM   2440 C C    . GLU   A 1 174 ? 40.631 -20.745 4.288   1.00 24.15  ? 154 GLU   A C    1 
ATOM   2441 O O    . GLU   A 1 174 ? 40.229 -20.664 3.124   1.00 25.25  ? 154 GLU   A O    1 
ATOM   2442 C CB   . GLU   A 1 174 ? 40.514 -23.152 4.905   1.00 31.02  ? 154 GLU   A CB   1 
ATOM   2443 C CG   . GLU   A 1 174 ? 42.005 -23.347 5.108   1.00 38.83  ? 154 GLU   A CG   1 
ATOM   2444 C CD   . GLU   A 1 174 ? 42.519 -24.691 4.589   1.00 45.75  ? 154 GLU   A CD   1 
ATOM   2445 O OE1  . GLU   A 1 174 ? 41.747 -25.680 4.599   1.00 47.47  ? 154 GLU   A OE1  1 
ATOM   2446 O OE2  . GLU   A 1 174 ? 43.702 -24.750 4.169   1.00 49.71  ? 154 GLU   A OE2  1 
ATOM   2447 H H    . GLU   A 1 174 ? 38.203 -22.415 4.928   1.00 28.44  ? 154 GLU   A H    1 
ATOM   2448 H HA   . GLU   A 1 174 ? 40.318 -21.522 6.159   1.00 30.68  ? 154 GLU   A HA   1 
ATOM   2449 H HB2  . GLU   A 1 174 ? 40.052 -23.795 5.466   1.00 37.23  ? 154 GLU   A HB2  1 
ATOM   2450 H HB3  . GLU   A 1 174 ? 40.316 -23.324 3.972   1.00 37.23  ? 154 GLU   A HB3  1 
ATOM   2451 H HG2  . GLU   A 1 174 ? 42.479 -22.645 4.635   1.00 46.60  ? 154 GLU   A HG2  1 
ATOM   2452 H HG3  . GLU   A 1 174 ? 42.201 -23.299 6.056   1.00 46.60  ? 154 GLU   A HG3  1 
ATOM   2453 N N    . VAL   A 1 175 ? 41.608 -19.991 4.761   1.00 22.82  ? 155 VAL   A N    1 
ATOM   2454 C CA   . VAL   A 1 175 ? 42.303 -18.993 3.948   1.00 23.55  ? 155 VAL   A CA   1 
ATOM   2455 C C    . VAL   A 1 175 ? 43.608 -19.613 3.479   1.00 24.11  ? 155 VAL   A C    1 
ATOM   2456 O O    . VAL   A 1 175 ? 44.364 -20.100 4.316   1.00 23.87  ? 155 VAL   A O    1 
ATOM   2457 C CB   . VAL   A 1 175 ? 42.600 -17.729 4.757   1.00 24.27  ? 155 VAL   A CB   1 
ATOM   2458 C CG1  . VAL   A 1 175 ? 43.327 -16.700 3.882   1.00 24.87  ? 155 VAL   A CG1  1 
ATOM   2459 C CG2  . VAL   A 1 175 ? 41.297 -17.146 5.284   1.00 26.54  ? 155 VAL   A CG2  1 
ATOM   2460 H H    . VAL   A 1 175 ? 41.898 -20.036 5.570   1.00 27.39  ? 155 VAL   A H    1 
ATOM   2461 H HA   . VAL   A 1 175 ? 41.757 -18.759 3.180   1.00 28.27  ? 155 VAL   A HA   1 
ATOM   2462 H HB   . VAL   A 1 175 ? 43.173 -17.950 5.508   1.00 29.13  ? 155 VAL   A HB   1 
ATOM   2463 H HG11 . VAL   A 1 175 ? 43.322 -15.842 4.333   1.00 29.85  ? 155 VAL   A HG11 1 
ATOM   2464 H HG12 . VAL   A 1 175 ? 44.241 -16.994 3.741   1.00 29.85  ? 155 VAL   A HG12 1 
ATOM   2465 H HG13 . VAL   A 1 175 ? 42.868 -16.629 3.030   1.00 29.85  ? 155 VAL   A HG13 1 
ATOM   2466 H HG21 . VAL   A 1 175 ? 41.485 -16.308 5.735   1.00 31.85  ? 155 VAL   A HG21 1 
ATOM   2467 H HG22 . VAL   A 1 175 ? 40.695 -16.993 4.538   1.00 31.85  ? 155 VAL   A HG22 1 
ATOM   2468 H HG23 . VAL   A 1 175 ? 40.899 -17.774 5.907   1.00 31.85  ? 155 VAL   A HG23 1 
ATOM   2469 N N    . PRO   A 1 176 ? 43.926 -19.595 2.188   1.00 28.49  ? 156 PRO   A N    1 
ATOM   2470 C CA   . PRO   A 1 176 ? 45.224 -20.146 1.774   1.00 28.91  ? 156 PRO   A CA   1 
ATOM   2471 C C    . PRO   A 1 176 ? 46.338 -19.245 2.251   1.00 26.47  ? 156 PRO   A C    1 
ATOM   2472 O O    . PRO   A 1 176 ? 46.148 -18.062 2.542   1.00 25.25  ? 156 PRO   A O    1 
ATOM   2473 C CB   . PRO   A 1 176 ? 45.154 -20.161 0.245   1.00 33.29  ? 156 PRO   A CB   1 
ATOM   2474 C CG   . PRO   A 1 176 ? 44.248 -19.074 -0.067  1.00 32.84  ? 156 PRO   A CG   1 
ATOM   2475 C CD   . PRO   A 1 176 ? 43.168 -19.091 1.030   1.00 31.70  ? 156 PRO   A CD   1 
ATOM   2476 H HA   . PRO   A 1 176 ? 45.344 -21.054 2.093   1.00 34.69  ? 156 PRO   A HA   1 
ATOM   2477 H HB2  . PRO   A 1 176 ? 46.033 -20.006 -0.133  1.00 39.95  ? 156 PRO   A HB2  1 
ATOM   2478 H HB3  . PRO   A 1 176 ? 44.804 -21.011 -0.067  1.00 39.95  ? 156 PRO   A HB3  1 
ATOM   2479 H HG2  . PRO   A 1 176 ? 44.732 -18.234 -0.058  1.00 39.41  ? 156 PRO   A HG2  1 
ATOM   2480 H HG3  . PRO   A 1 176 ? 43.852 -19.220 -0.940  1.00 39.41  ? 156 PRO   A HG3  1 
ATOM   2481 H HD2  . PRO   A 1 176 ? 42.822 -18.200 1.197   1.00 38.04  ? 156 PRO   A HD2  1 
ATOM   2482 H HD3  . PRO   A 1 176 ? 42.441 -19.690 0.798   1.00 38.04  ? 156 PRO   A HD3  1 
ATOM   2483 N N    . GLU   A 1 177 ? 47.505 -19.849 2.371   1.00 29.21  ? 157 GLU   A N    1 
ATOM   2484 C CA   . GLU   A 1 177 ? 48.675 -19.187 2.907   1.00 31.83  ? 157 GLU   A CA   1 
ATOM   2485 C C    . GLU   A 1 177 ? 49.709 -19.184 1.800   1.00 29.99  ? 157 GLU   A C    1 
ATOM   2486 O O    . GLU   A 1 177 ? 50.099 -20.247 1.301   1.00 33.93  ? 157 GLU   A O    1 
ATOM   2487 C CB   . GLU   A 1 177 ? 49.202 -19.935 4.137   1.00 39.93  ? 157 GLU   A CB   1 
ATOM   2488 C CG   . GLU   A 1 177 ? 50.427 -19.299 4.788   1.00 48.36  ? 157 GLU   A CG   1 
ATOM   2489 H H    . GLU   A 1 177 ? 47.647 -20.665 2.141   1.00 35.06  ? 157 GLU   A H    1 
ATOM   2490 H HA   . GLU   A 1 177 ? 48.475 -18.277 3.175   1.00 38.20  ? 157 GLU   A HA   1 
ATOM   2491 H HB2  . GLU   A 1 177 ? 48.499 -19.967 4.804   1.00 47.92  ? 157 GLU   A HB2  1 
ATOM   2492 H HB3  . GLU   A 1 177 ? 49.447 -20.835 3.869   1.00 47.92  ? 157 GLU   A HB3  1 
ATOM   2493 H HG2  . GLU   A 1 177 ? 51.213 -19.491 4.254   1.00 58.03  ? 157 GLU   A HG2  1 
ATOM   2494 H HG3  . GLU   A 1 177 ? 50.291 -18.339 4.846   1.00 58.03  ? 157 GLU   A HG3  1 
ATOM   2495 N N    . VAL   A 1 178 ? 50.150 -17.997 1.416   1.00 26.40  ? 158 VAL   A N    1 
ATOM   2496 C CA   . VAL   A 1 178 ? 51.293 -17.880 0.527   1.00 24.00  ? 158 VAL   A CA   1 
ATOM   2497 C C    . VAL   A 1 178 ? 52.533 -18.356 1.275   1.00 23.83  ? 158 VAL   A C    1 
ATOM   2498 O O    . VAL   A 1 178 ? 52.809 -17.903 2.396   1.00 26.70  ? 158 VAL   A O    1 
ATOM   2499 C CB   . VAL   A 1 178 ? 51.452 -16.423 0.071   1.00 23.99  ? 158 VAL   A CB   1 
ATOM   2500 C CG1  . VAL   A 1 178 ? 52.731 -16.254 -0.720  1.00 24.02  ? 158 VAL   A CG1  1 
ATOM   2501 C CG2  . VAL   A 1 178 ? 50.246 -15.982 -0.746  1.00 25.63  ? 158 VAL   A CG2  1 
ATOM   2502 H H    . VAL   A 1 178 ? 49.807 -17.245 1.656   1.00 31.68  ? 158 VAL   A H    1 
ATOM   2503 H HA   . VAL   A 1 178 ? 51.165 -18.436 -0.258  1.00 28.80  ? 158 VAL   A HA   1 
ATOM   2504 H HB   . VAL   A 1 178 ? 51.504 -15.854 0.855   1.00 28.79  ? 158 VAL   A HB   1 
ATOM   2505 H HG11 . VAL   A 1 178 ? 52.698 -15.409 -1.196  1.00 28.82  ? 158 VAL   A HG11 1 
ATOM   2506 H HG12 . VAL   A 1 178 ? 53.484 -16.259 -0.108  1.00 28.82  ? 158 VAL   A HG12 1 
ATOM   2507 H HG13 . VAL   A 1 178 ? 52.812 -16.986 -1.350  1.00 28.82  ? 158 VAL   A HG13 1 
ATOM   2508 H HG21 . VAL   A 1 178 ? 50.383 -15.068 -1.042  1.00 30.75  ? 158 VAL   A HG21 1 
ATOM   2509 H HG22 . VAL   A 1 178 ? 50.153 -16.567 -1.513  1.00 30.75  ? 158 VAL   A HG22 1 
ATOM   2510 H HG23 . VAL   A 1 178 ? 49.452 -16.034 -0.191  1.00 30.75  ? 158 VAL   A HG23 1 
ATOM   2511 N N    . ARG   A 1 179 ? 53.271 -19.295 0.675   1.00 22.35  ? 159 ARG   A N    1 
ATOM   2512 C CA   . ARG   A 1 179 ? 54.456 -19.845 1.323   1.00 22.53  ? 159 ARG   A CA   1 
ATOM   2513 C C    . ARG   A 1 179 ? 55.533 -18.773 1.371   1.00 21.79  ? 159 ARG   A C    1 
ATOM   2514 O O    . ARG   A 1 179 ? 55.838 -18.144 0.359   1.00 23.06  ? 159 ARG   A O    1 
ATOM   2515 C CB   . ARG   A 1 179 ? 55.000 -21.036 0.533   1.00 24.48  ? 159 ARG   A CB   1 
ATOM   2516 C CG   . ARG   A 1 179 ? 54.091 -22.282 0.528   1.00 27.46  ? 159 ARG   A CG   1 
ATOM   2517 C CD   . ARG   A 1 179 ? 54.750 -23.477 -0.218  1.00 29.20  ? 159 ARG   A CD   1 
ATOM   2518 N NE   . ARG   A 1 179 ? 54.974 -23.184 -1.637  1.00 32.04  ? 159 ARG   A NE   1 
ATOM   2519 C CZ   . ARG   A 1 179 ? 54.081 -23.395 -2.597  1.00 33.97  ? 159 ARG   A CZ   1 
ATOM   2520 N NH1  . ARG   A 1 179 ? 52.888 -23.898 -2.331  1.00 35.10  ? 159 ARG   A NH1  1 
ATOM   2521 N NH2  . ARG   A 1 179 ? 54.396 -23.105 -3.857  1.00 36.46  ? 159 ARG   A NH2  1 
ATOM   2522 H H    . ARG   A 1 179 ? 53.105 -19.626 -0.101  1.00 26.82  ? 159 ARG   A H    1 
ATOM   2523 H HA   . ARG   A 1 179 ? 54.225 -20.140 2.217   1.00 27.03  ? 159 ARG   A HA   1 
ATOM   2524 H HB2  . ARG   A 1 179 ? 55.125 -20.763 -0.390  1.00 29.38  ? 159 ARG   A HB2  1 
ATOM   2525 H HB3  . ARG   A 1 179 ? 55.851 -21.299 0.919   1.00 29.38  ? 159 ARG   A HB3  1 
ATOM   2526 H HG2  . ARG   A 1 179 ? 53.915 -22.554 1.442   1.00 32.96  ? 159 ARG   A HG2  1 
ATOM   2527 H HG3  . ARG   A 1 179 ? 53.257 -22.068 0.080   1.00 32.96  ? 159 ARG   A HG3  1 
ATOM   2528 H HD2  . ARG   A 1 179 ? 55.608 -23.674 0.190   1.00 35.04  ? 159 ARG   A HD2  1 
ATOM   2529 H HD3  . ARG   A 1 179 ? 54.168 -24.251 -0.156  1.00 35.04  ? 159 ARG   A HD3  1 
ATOM   2530 H HE   . ARG   A 1 179 ? 55.735 -22.853 -1.863  1.00 38.45  ? 159 ARG   A HE   1 
ATOM   2531 H HH11 . ARG   A 1 179 ? 52.675 -24.096 -1.522  1.00 42.12  ? 159 ARG   A HH11 1 
ATOM   2532 H HH12 . ARG   A 1 179 ? 52.324 -24.027 -2.968  1.00 42.12  ? 159 ARG   A HH12 1 
ATOM   2533 H HH21 . ARG   A 1 179 ? 55.171 -22.785 -4.044  1.00 43.75  ? 159 ARG   A HH21 1 
ATOM   2534 H HH22 . ARG   A 1 179 ? 53.823 -23.239 -4.485  1.00 43.75  ? 159 ARG   A HH22 1 
ATOM   2535 N N    . ARG   A 1 180 ? 56.087 -18.540 2.551   1.00 22.15  ? 160 ARG   A N    1 
ATOM   2536 C CA   . ARG   A 1 180 ? 57.043 -17.453 2.728   1.00 22.66  ? 160 ARG   A CA   1 
ATOM   2537 C C    . ARG   A 1 180 ? 58.472 -17.920 2.913   1.00 22.78  ? 160 ARG   A C    1 
ATOM   2538 O O    . ARG   A 1 180 ? 59.340 -17.095 3.179   1.00 24.38  ? 160 ARG   A O    1 
ATOM   2539 C CB   . ARG   A 1 180 ? 56.616 -16.580 3.888   1.00 25.93  ? 160 ARG   A CB   1 
ATOM   2540 C CG   . ARG   A 1 180 ? 55.165 -16.043 3.674   1.00 29.47  ? 160 ARG   A CG   1 
ATOM   2541 C CD   . ARG   A 1 180 ? 54.800 -14.900 4.532   1.00 29.85  ? 160 ARG   A CD   1 
ATOM   2542 N NE   . ARG   A 1 180 ? 53.364 -14.612 4.490   1.00 30.26  ? 160 ARG   A NE   1 
ATOM   2543 C CZ   . ARG   A 1 180 ? 52.813 -13.621 5.167   1.00 33.93  ? 160 ARG   A CZ   1 
ATOM   2544 N NH1  . ARG   A 1 180 ? 53.546 -12.818 5.924   1.00 35.69  ? 160 ARG   A NH1  1 
ATOM   2545 N NH2  . ARG   A 1 180 ? 51.498 -13.430 5.082   1.00 34.58  ? 160 ARG   A NH2  1 
ATOM   2546 H H    . ARG   A 1 180 ? 55.928 -18.995 3.263   1.00 26.58  ? 160 ARG   A H    1 
ATOM   2547 H HA   . ARG   A 1 180 ? 57.035 -16.913 1.922   1.00 27.19  ? 160 ARG   A HA   1 
ATOM   2548 H HB2  . ARG   A 1 180 ? 56.635 -17.099 4.707   1.00 31.12  ? 160 ARG   A HB2  1 
ATOM   2549 H HB3  . ARG   A 1 180 ? 57.217 -15.823 3.961   1.00 31.12  ? 160 ARG   A HB3  1 
ATOM   2550 H HG2  . ARG   A 1 180 ? 55.074 -15.756 2.752   1.00 35.37  ? 160 ARG   A HG2  1 
ATOM   2551 H HG3  . ARG   A 1 180 ? 54.539 -16.759 3.862   1.00 35.37  ? 160 ARG   A HG3  1 
ATOM   2552 H HD2  . ARG   A 1 180 ? 55.041 -15.101 5.450   1.00 35.82  ? 160 ARG   A HD2  1 
ATOM   2553 H HD3  . ARG   A 1 180 ? 55.275 -14.110 4.230   1.00 35.82  ? 160 ARG   A HD3  1 
ATOM   2554 H HE   . ARG   A 1 180 ? 52.858 -15.109 4.004   1.00 36.31  ? 160 ARG   A HE   1 
ATOM   2555 H HH11 . ARG   A 1 180 ? 54.396 -12.938 5.981   1.00 42.83  ? 160 ARG   A HH11 1 
ATOM   2556 H HH12 . ARG   A 1 180 ? 53.173 -12.177 6.359   1.00 42.83  ? 160 ARG   A HH12 1 
ATOM   2557 H HH21 . ARG   A 1 180 ? 51.019 -13.949 4.591   1.00 41.50  ? 160 ARG   A HH21 1 
ATOM   2558 H HH22 . ARG   A 1 180 ? 51.128 -12.788 5.518   1.00 41.50  ? 160 ARG   A HH22 1 
ATOM   2559 N N    . ASP   A 1 181 ? 58.735 -19.215 2.766   1.00 22.37  ? 161 ASP   A N    1 
ATOM   2560 C CA   . ASP   A 1 181 ? 60.076 -19.712 3.050   1.00 24.59  ? 161 ASP   A CA   1 
ATOM   2561 C C    . ASP   A 1 181 ? 61.137 -19.002 2.214   1.00 24.16  ? 161 ASP   A C    1 
ATOM   2562 O O    . ASP   A 1 181 ? 62.261 -18.752 2.692   1.00 26.07  ? 161 ASP   A O    1 
ATOM   2563 C CB   . ASP   A 1 181 ? 60.088 -21.220 2.781   1.00 29.54  ? 161 ASP   A CB   1 
ATOM   2564 C CG   . ASP   A 1 181 ? 58.967 -21.922 3.496   1.00 35.85  ? 161 ASP   A CG   1 
ATOM   2565 O OD1  . ASP   A 1 181 ? 59.222 -22.302 4.651   1.00 40.62  ? 161 ASP   A OD1  1 
ATOM   2566 O OD2  . ASP   A 1 181 ? 57.815 -22.002 2.943   1.00 35.96  ? 161 ASP   A OD2  1 
ATOM   2567 H H    . ASP   A 1 181 ? 58.171 -19.811 2.511   1.00 26.85  ? 161 ASP   A H    1 
ATOM   2568 H HA   . ASP   A 1 181 ? 60.298 -19.547 3.979   1.00 29.51  ? 161 ASP   A HA   1 
ATOM   2569 H HB2  . ASP   A 1 181 ? 59.987 -21.376 1.829   1.00 35.45  ? 161 ASP   A HB2  1 
ATOM   2570 H HB3  . ASP   A 1 181 ? 60.928 -21.593 3.092   1.00 35.45  ? 161 ASP   A HB3  1 
ATOM   2571 N N    . GLY   A 1 182 ? 60.824 -18.697 0.965   1.00 21.44  ? 162 GLY   A N    1 
ATOM   2572 C CA   . GLY   A 1 182 ? 61.803 -18.135 0.071   1.00 20.96  ? 162 GLY   A CA   1 
ATOM   2573 C C    . GLY   A 1 182 ? 61.932 -16.641 0.121   1.00 21.17  ? 162 GLY   A C    1 
ATOM   2574 O O    . GLY   A 1 182 ? 62.679 -16.075 -0.678  1.00 22.77  ? 162 GLY   A O    1 
ATOM   2575 H H    . GLY   A 1 182 ? 60.045 -18.809 0.617   1.00 25.73  ? 162 GLY   A H    1 
ATOM   2576 H HA2  . GLY   A 1 182 ? 62.671 -18.512 0.286   1.00 25.16  ? 162 GLY   A HA2  1 
ATOM   2577 H HA3  . GLY   A 1 182 ? 61.569 -18.380 -0.838  1.00 25.16  ? 162 GLY   A HA3  1 
ATOM   2578 N N    . LEU   A 1 183 ? 61.190 -15.980 1.027   1.00 22.23  ? 163 LEU   A N    1 
ATOM   2579 C CA   . LEU   A 1 183 ? 61.123 -14.534 1.064   1.00 24.53  ? 163 LEU   A CA   1 
ATOM   2580 C C    . LEU   A 1 183 ? 62.091 -13.984 2.094   1.00 28.29  ? 163 LEU   A C    1 
ATOM   2581 O O    . LEU   A 1 183 ? 62.405 -14.658 3.079   1.00 31.09  ? 163 LEU   A O    1 
ATOM   2582 C CB   . LEU   A 1 183 ? 59.710 -14.091 1.446   1.00 26.24  ? 163 LEU   A CB   1 
ATOM   2583 C CG   . LEU   A 1 183 ? 58.638 -14.589 0.491   1.00 26.84  ? 163 LEU   A CG   1 
ATOM   2584 C CD1  . LEU   A 1 183 ? 57.229 -14.197 0.996   1.00 27.77  ? 163 LEU   A CD1  1 
ATOM   2585 C CD2  . LEU   A 1 183 ? 58.864 -14.092 -0.936  1.00 27.05  ? 163 LEU   A CD2  1 
ATOM   2586 H H    . LEU   A 1 183 ? 60.715 -16.363 1.634   1.00 26.67  ? 163 LEU   A H    1 
ATOM   2587 H HA   . LEU   A 1 183 ? 61.350 -14.171 0.193   1.00 29.44  ? 163 LEU   A HA   1 
ATOM   2588 H HB2  . LEU   A 1 183 ? 59.504 -14.435 2.330   1.00 31.49  ? 163 LEU   A HB2  1 
ATOM   2589 H HB3  . LEU   A 1 183 ? 59.678 -13.122 1.452   1.00 31.49  ? 163 LEU   A HB3  1 
ATOM   2590 H HG   . LEU   A 1 183 ? 58.691 -15.557 0.462   1.00 32.21  ? 163 LEU   A HG   1 
ATOM   2591 H HD11 . LEU   A 1 183 ? 56.569 -14.485 0.346   1.00 33.33  ? 163 LEU   A HD11 1 
ATOM   2592 H HD12 . LEU   A 1 183 ? 57.066 -14.633 1.847   1.00 33.33  ? 163 LEU   A HD12 1 
ATOM   2593 H HD13 . LEU   A 1 183 ? 57.189 -13.234 1.105   1.00 33.33  ? 163 LEU   A HD13 1 
ATOM   2594 H HD21 . LEU   A 1 183 ? 58.102 -14.340 -1.481  1.00 32.46  ? 163 LEU   A HD21 1 
ATOM   2595 H HD22 . LEU   A 1 183 ? 58.961 -13.127 -0.922  1.00 32.46  ? 163 LEU   A HD22 1 
ATOM   2596 H HD23 . LEU   A 1 183 ? 59.671 -14.500 -1.288  1.00 32.46  ? 163 LEU   A HD23 1 
ATOM   2597 N N    . PRO   A 1 184 ? 62.586 -12.765 1.885   1.00 28.76  ? 164 PRO   A N    1 
ATOM   2598 C CA   . PRO   A 1 184 ? 63.374 -12.110 2.927   1.00 32.62  ? 164 PRO   A CA   1 
ATOM   2599 C C    . PRO   A 1 184 ? 62.599 -12.016 4.230   1.00 37.81  ? 164 PRO   A C    1 
ATOM   2600 O O    . PRO   A 1 184 ? 61.391 -11.749 4.244   1.00 35.90  ? 164 PRO   A O    1 
ATOM   2601 C CB   . PRO   A 1 184 ? 63.632 -10.709 2.352   1.00 32.39  ? 164 PRO   A CB   1 
ATOM   2602 C CG   . PRO   A 1 184 ? 63.425 -10.807 0.914   1.00 31.74  ? 164 PRO   A CG   1 
ATOM   2603 C CD   . PRO   A 1 184 ? 62.420 -11.905 0.696   1.00 29.60  ? 164 PRO   A CD   1 
ATOM   2604 H HA   . PRO   A 1 184 ? 64.211 -12.581 3.064   1.00 39.15  ? 164 PRO   A HA   1 
ATOM   2605 H HB2  . PRO   A 1 184 ? 63.009 -10.078 2.745   1.00 38.87  ? 164 PRO   A HB2  1 
ATOM   2606 H HB3  . PRO   A 1 184 ? 64.544 -10.441 2.548   1.00 38.87  ? 164 PRO   A HB3  1 
ATOM   2607 H HG2  . PRO   A 1 184 ? 63.086 -9.963  0.577   1.00 38.09  ? 164 PRO   A HG2  1 
ATOM   2608 H HG3  . PRO   A 1 184 ? 64.265 -11.024 0.479   1.00 38.09  ? 164 PRO   A HG3  1 
ATOM   2609 H HD2  . PRO   A 1 184 ? 61.520 -11.544 0.655   1.00 35.52  ? 164 PRO   A HD2  1 
ATOM   2610 H HD3  . PRO   A 1 184 ? 62.618 -12.397 -0.116  1.00 35.52  ? 164 PRO   A HD3  1 
ATOM   2611 N N    . SER   A 1 185 ? 63.317 -12.221 5.327   1.00 46.71  ? 165 SER   A N    1 
ATOM   2612 C CA   . SER   A 1 185 ? 62.791 -12.013 6.668   1.00 55.30  ? 165 SER   A CA   1 
ATOM   2613 C C    . SER   A 1 185 ? 62.290 -10.581 6.816   1.00 58.83  ? 165 SER   A C    1 
ATOM   2614 O O    . SER   A 1 185 ? 63.084 -9.639  6.786   1.00 60.94  ? 165 SER   A O    1 
ATOM   2615 C CB   . SER   A 1 185 ? 63.886 -12.275 7.707   1.00 59.19  ? 165 SER   A CB   1 
ATOM   2616 O OG   . SER   A 1 185 ? 63.498 -11.788 8.981   1.00 61.59  ? 165 SER   A OG   1 
ATOM   2617 H H    . SER   A 1 185 ? 64.135 -12.488 5.321   1.00 56.05  ? 165 SER   A H    1 
ATOM   2618 H HA   . SER   A 1 185 ? 62.056 -12.625 6.830   1.00 66.36  ? 165 SER   A HA   1 
ATOM   2619 H HB2  . SER   A 1 185 ? 64.041 -13.230 7.768   1.00 71.03  ? 165 SER   A HB2  1 
ATOM   2620 H HB3  . SER   A 1 185 ? 64.698 -11.823 7.431   1.00 71.03  ? 165 SER   A HB3  1 
ATOM   2621 H HG   . SER   A 1 185 ? 64.098 -11.951 9.546   1.00 73.91  ? 165 SER   A HG   1 
ATOM   2622 N N    . THR   B 1 30  ? 33.671 -33.317 39.966  1.00 69.14  ? 10  THR   B N    1 
ATOM   2623 C CA   . THR   B 1 30  ? 33.383 -32.659 41.232  1.00 67.74  ? 10  THR   B CA   1 
ATOM   2624 C C    . THR   B 1 30  ? 32.054 -31.921 41.131  1.00 64.83  ? 10  THR   B C    1 
ATOM   2625 O O    . THR   B 1 30  ? 31.834 -31.165 40.186  1.00 63.39  ? 10  THR   B O    1 
ATOM   2626 C CB   . THR   B 1 30  ? 34.485 -31.647 41.604  1.00 69.05  ? 10  THR   B CB   1 
ATOM   2627 H HA   . THR   B 1 30  ? 33.332 -33.317 41.943  1.00 81.29  ? 10  THR   B HA   1 
ATOM   2628 N N    . SER   B 1 31  ? 31.167 -32.148 42.106  1.00 62.39  ? 11  SER   B N    1 
ATOM   2629 C CA   . SER   B 1 31  ? 29.887 -31.444 42.120  1.00 59.33  ? 11  SER   B CA   1 
ATOM   2630 C C    . SER   B 1 31  ? 30.091 -29.938 42.212  1.00 55.38  ? 11  SER   B C    1 
ATOM   2631 O O    . SER   B 1 31  ? 29.434 -29.163 41.499  1.00 53.40  ? 11  SER   B O    1 
ATOM   2632 C CB   . SER   B 1 31  ? 29.041 -31.926 43.298  1.00 59.91  ? 11  SER   B CB   1 
ATOM   2633 O OG   . SER   B 1 31  ? 28.957 -33.336 43.300  1.00 61.05  ? 11  SER   B OG   1 
ATOM   2634 H H    . SER   B 1 31  ? 31.282 -32.696 42.759  1.00 74.87  ? 11  SER   B H    1 
ATOM   2635 H HA   . SER   B 1 31  ? 29.413 -31.641 41.297  1.00 71.19  ? 11  SER   B HA   1 
ATOM   2636 H HB2  . SER   B 1 31  ? 29.452 -31.632 44.126  1.00 71.89  ? 11  SER   B HB2  1 
ATOM   2637 H HB3  . SER   B 1 31  ? 28.148 -31.555 43.221  1.00 71.89  ? 11  SER   B HB3  1 
ATOM   2638 H HG   . SER   B 1 31  ? 28.498 -33.595 43.954  1.00 73.27  ? 11  SER   B HG   1 
ATOM   2639 N N    . GLU   B 1 32  ? 30.995 -29.501 43.092  1.00 53.08  ? 12  GLU   B N    1 
ATOM   2640 C CA   . GLU   B 1 32  ? 31.243 -28.071 43.230  1.00 50.98  ? 12  GLU   B CA   1 
ATOM   2641 C C    . GLU   B 1 32  ? 31.747 -27.477 41.922  1.00 47.43  ? 12  GLU   B C    1 
ATOM   2642 O O    . GLU   B 1 32  ? 31.311 -26.390 41.512  1.00 45.71  ? 12  GLU   B O    1 
ATOM   2643 C CB   . GLU   B 1 32  ? 32.258 -27.825 44.346  1.00 53.09  ? 12  GLU   B CB   1 
ATOM   2644 H H    . GLU   B 1 32  ? 31.466 -30.002 43.608  1.00 63.70  ? 12  GLU   B H    1 
ATOM   2645 H HA   . GLU   B 1 32  ? 30.413 -27.628 43.469  1.00 61.18  ? 12  GLU   B HA   1 
ATOM   2646 N N    . ASN   B 1 33  ? 32.681 -28.166 41.259  1.00 47.10  ? 13  ASN   B N    1 
ATOM   2647 C CA   . ASN   B 1 33  ? 33.225 -27.640 40.012  1.00 48.94  ? 13  ASN   B CA   1 
ATOM   2648 C C    . ASN   B 1 33  ? 32.153 -27.595 38.932  1.00 42.68  ? 13  ASN   B C    1 
ATOM   2649 O O    . ASN   B 1 33  ? 32.115 -26.660 38.130  1.00 38.88  ? 13  ASN   B O    1 
ATOM   2650 C CB   . ASN   B 1 33  ? 34.420 -28.470 39.551  1.00 57.23  ? 13  ASN   B CB   1 
ATOM   2651 C CG   . ASN   B 1 33  ? 35.688 -28.163 40.339  1.00 64.63  ? 13  ASN   B CG   1 
ATOM   2652 O OD1  . ASN   B 1 33  ? 35.833 -27.079 40.913  1.00 67.55  ? 13  ASN   B OD1  1 
ATOM   2653 N ND2  . ASN   B 1 33  ? 36.617 -29.118 40.362  1.00 66.74  ? 13  ASN   B ND2  1 
ATOM   2654 H H    . ASN   B 1 33  ? 33.007 -28.922 41.507  1.00 56.53  ? 13  ASN   B H    1 
ATOM   2655 H HA   . ASN   B 1 33  ? 33.544 -26.738 40.169  1.00 58.73  ? 13  ASN   B HA   1 
ATOM   2656 H HB2  . ASN   B 1 33  ? 34.216 -29.411 39.667  1.00 68.68  ? 13  ASN   B HB2  1 
ATOM   2657 H HB3  . ASN   B 1 33  ? 34.595 -28.280 38.616  1.00 68.68  ? 13  ASN   B HB3  1 
ATOM   2658 H HD21 . ASN   B 1 33  ? 37.351 -28.994 40.793  1.00 80.09  ? 13  ASN   B HD21 1 
ATOM   2659 H HD22 . ASN   B 1 33  ? 36.483 -29.859 39.946  1.00 80.09  ? 13  ASN   B HD22 1 
ATOM   2660 N N    . ARG   B 1 34  ? 31.281 -28.603 38.883  1.00 40.36  ? 14  ARG   B N    1 
ATOM   2661 C CA   . ARG   B 1 34  ? 30.208 -28.571 37.894  1.00 38.18  ? 14  ARG   B CA   1 
ATOM   2662 C C    . ARG   B 1 34  ? 29.299 -27.377 38.114  1.00 34.52  ? 14  ARG   B C    1 
ATOM   2663 O O    . ARG   B 1 34  ? 28.864 -26.742 37.149  1.00 33.16  ? 14  ARG   B O    1 
ATOM   2664 C CB   . ARG   B 1 34  ? 29.420 -29.881 37.916  1.00 41.38  ? 14  ARG   B CB   1 
ATOM   2665 C CG   . ARG   B 1 34  ? 30.160 -31.011 37.237  1.00 45.93  ? 14  ARG   B CG   1 
ATOM   2666 C CD   . ARG   B 1 34  ? 29.580 -32.357 37.601  1.00 50.72  ? 14  ARG   B CD   1 
ATOM   2667 N NE   . ARG   B 1 34  ? 28.185 -32.495 37.192  1.00 55.83  ? 14  ARG   B NE   1 
ATOM   2668 C CZ   . ARG   B 1 34  ? 27.785 -32.823 35.969  1.00 59.63  ? 14  ARG   B CZ   1 
ATOM   2669 N NH1  . ARG   B 1 34  ? 28.649 -33.012 34.983  1.00 62.01  ? 14  ARG   B NH1  1 
ATOM   2670 N NH2  . ARG   B 1 34  ? 26.484 -32.973 35.728  1.00 59.23  ? 14  ARG   B NH2  1 
ATOM   2671 H H    . ARG   B 1 34  ? 31.288 -29.294 39.395  1.00 48.43  ? 14  ARG   B H    1 
ATOM   2672 H HA   . ARG   B 1 34  ? 30.599 -28.487 37.010  1.00 45.81  ? 14  ARG   B HA   1 
ATOM   2673 H HB2  . ARG   B 1 34  ? 29.257 -30.138 38.837  1.00 49.66  ? 14  ARG   B HB2  1 
ATOM   2674 H HB3  . ARG   B 1 34  ? 28.577 -29.752 37.453  1.00 49.66  ? 14  ARG   B HB3  1 
ATOM   2675 H HG2  . ARG   B 1 34  ? 30.098 -30.903 36.275  1.00 55.12  ? 14  ARG   B HG2  1 
ATOM   2676 H HG3  . ARG   B 1 34  ? 31.090 -30.996 37.513  1.00 55.12  ? 14  ARG   B HG3  1 
ATOM   2677 H HD2  . ARG   B 1 34  ? 30.093 -33.053 37.160  1.00 60.87  ? 14  ARG   B HD2  1 
ATOM   2678 H HD3  . ARG   B 1 34  ? 29.624 -32.472 38.563  1.00 60.87  ? 14  ARG   B HD3  1 
ATOM   2679 H HE   . ARG   B 1 34  ? 27.579 -32.355 37.786  1.00 67.00  ? 14  ARG   B HE   1 
ATOM   2680 H HH11 . ARG   B 1 34  ? 29.492 -32.924 35.127  1.00 74.41  ? 14  ARG   B HH11 1 
ATOM   2681 H HH12 . ARG   B 1 34  ? 28.367 -33.223 34.199  1.00 74.41  ? 14  ARG   B HH12 1 
ATOM   2682 H HH21 . ARG   B 1 34  ? 25.913 -32.858 36.361  1.00 71.08  ? 14  ARG   B HH21 1 
ATOM   2683 H HH22 . ARG   B 1 34  ? 26.214 -33.184 34.939  1.00 71.08  ? 14  ARG   B HH22 1 
ATOM   2684 N N    . ALA   B 1 35  ? 29.024 -27.036 39.375  1.00 32.73  ? 15  ALA   B N    1 
ATOM   2685 C CA   . ALA   B 1 35  ? 28.162 -25.892 39.657  1.00 32.27  ? 15  ALA   B CA   1 
ATOM   2686 C C    . ALA   B 1 35  ? 28.842 -24.584 39.290  1.00 29.88  ? 15  ALA   B C    1 
ATOM   2687 O O    . ALA   B 1 35  ? 28.195 -23.681 38.763  1.00 28.65  ? 15  ALA   B O    1 
ATOM   2688 C CB   . ALA   B 1 35  ? 27.738 -25.889 41.125  1.00 33.27  ? 15  ALA   B CB   1 
ATOM   2689 H H    . ALA   B 1 35  ? 29.319 -27.445 40.072  1.00 39.27  ? 15  ALA   B H    1 
ATOM   2690 H HA   . ALA   B 1 35  ? 27.358 -25.974 39.121  1.00 38.72  ? 15  ALA   B HA   1 
ATOM   2691 H HB1  . ALA   B 1 35  ? 27.161 -25.125 41.285  1.00 39.93  ? 15  ALA   B HB1  1 
ATOM   2692 H HB2  . ALA   B 1 35  ? 27.259 -26.711 41.317  1.00 39.93  ? 15  ALA   B HB2  1 
ATOM   2693 H HB3  . ALA   B 1 35  ? 28.529 -25.829 41.683  1.00 39.93  ? 15  ALA   B HB3  1 
ATOM   2694 N N    . GLN   B 1 36  ? 30.146 -24.484 39.538  1.00 27.63  ? 16  GLN   B N    1 
ATOM   2695 C CA   . GLN   B 1 36  ? 30.881 -23.278 39.136  1.00 28.22  ? 16  GLN   B CA   1 
ATOM   2696 C C    . GLN   B 1 36  ? 30.935 -23.139 37.624  1.00 28.37  ? 16  GLN   B C    1 
ATOM   2697 O O    . GLN   B 1 36  ? 30.734 -22.046 37.080  1.00 24.57  ? 16  GLN   B O    1 
ATOM   2698 C CB   . GLN   B 1 36  ? 32.294 -23.336 39.716  1.00 29.81  ? 16  GLN   B CB   1 
ATOM   2699 C CG   . GLN   B 1 36  ? 32.312 -23.211 41.214  1.00 30.86  ? 16  GLN   B CG   1 
ATOM   2700 H H    . GLN   B 1 36  ? 30.622 -25.083 39.929  1.00 33.16  ? 16  GLN   B H    1 
ATOM   2701 H HA   . GLN   B 1 36  ? 30.428 -22.496 39.489  1.00 33.87  ? 16  GLN   B HA   1 
ATOM   2702 H HB2  . GLN   B 1 36  ? 32.697 -24.186 39.481  1.00 35.77  ? 16  GLN   B HB2  1 
ATOM   2703 H HB3  . GLN   B 1 36  ? 32.817 -22.607 39.347  1.00 35.77  ? 16  GLN   B HB3  1 
ATOM   2704 N N    . VAL   B 1 37  ? 31.213 -24.230 36.919  1.00 28.78  ? 17  VAL   B N    1 
ATOM   2705 C CA   . VAL   B 1 37  ? 31.278 -24.193 35.464  1.00 29.35  ? 17  VAL   B CA   1 
ATOM   2706 C C    . VAL   B 1 37  ? 29.938 -23.778 34.876  1.00 29.14  ? 17  VAL   B C    1 
ATOM   2707 O O    . VAL   B 1 37  ? 29.877 -22.931 33.984  1.00 29.39  ? 17  VAL   B O    1 
ATOM   2708 C CB   . VAL   B 1 37  ? 31.751 -25.552 34.907  1.00 33.43  ? 17  VAL   B CB   1 
ATOM   2709 C CG1  . VAL   B 1 37  ? 31.662 -25.549 33.387  1.00 36.08  ? 17  VAL   B CG1  1 
ATOM   2710 C CG2  . VAL   B 1 37  ? 33.167 -25.871 35.360  1.00 33.79  ? 17  VAL   B CG2  1 
ATOM   2711 H H    . VAL   B 1 37  ? 31.367 -25.004 37.259  1.00 34.54  ? 17  VAL   B H    1 
ATOM   2712 H HA   . VAL   B 1 37  ? 31.932 -23.524 35.207  1.00 35.22  ? 17  VAL   B HA   1 
ATOM   2713 H HB   . VAL   B 1 37  ? 31.172 -26.249 35.252  1.00 40.12  ? 17  VAL   B HB   1 
ATOM   2714 H HG11 . VAL   B 1 37  ? 32.197 -26.279 33.038  1.00 43.30  ? 17  VAL   B HG11 1 
ATOM   2715 H HG12 . VAL   B 1 37  ? 30.735 -25.665 33.126  1.00 43.30  ? 17  VAL   B HG12 1 
ATOM   2716 H HG13 . VAL   B 1 37  ? 31.997 -24.703 33.053  1.00 43.30  ? 17  VAL   B HG13 1 
ATOM   2717 H HG21 . VAL   B 1 37  ? 33.338 -26.815 35.219  1.00 40.55  ? 17  VAL   B HG21 1 
ATOM   2718 H HG22 . VAL   B 1 37  ? 33.792 -25.340 34.842  1.00 40.55  ? 17  VAL   B HG22 1 
ATOM   2719 H HG23 . VAL   B 1 37  ? 33.252 -25.657 36.302  1.00 40.55  ? 17  VAL   B HG23 1 
ATOM   2720 N N    . ALA   B 1 38  ? 28.839 -24.363 35.374  1.00 27.02  ? 18  ALA   B N    1 
ATOM   2721 C CA   . ALA   B 1 38  ? 27.503 -24.012 34.891  1.00 27.56  ? 18  ALA   B CA   1 
ATOM   2722 C C    . ALA   B 1 38  ? 27.191 -22.544 35.135  1.00 25.75  ? 18  ALA   B C    1 
ATOM   2723 O O    . ALA   B 1 38  ? 26.649 -21.863 34.256  1.00 24.32  ? 18  ALA   B O    1 
ATOM   2724 C CB   . ALA   B 1 38  ? 26.483 -24.885 35.605  1.00 28.28  ? 18  ALA   B CB   1 
ATOM   2725 H H    . ALA   B 1 38  ? 28.843 -24.964 35.990  1.00 32.43  ? 18  ALA   B H    1 
ATOM   2726 H HA   . ALA   B 1 38  ? 27.454 -24.172 33.935  1.00 33.08  ? 18  ALA   B HA   1 
ATOM   2727 H HB1  . ALA   B 1 38  ? 25.595 -24.658 35.287  1.00 33.94  ? 18  ALA   B HB1  1 
ATOM   2728 H HB2  . ALA   B 1 38  ? 26.674 -25.817 35.414  1.00 33.94  ? 18  ALA   B HB2  1 
ATOM   2729 H HB3  . ALA   B 1 38  ? 26.543 -24.725 36.560  1.00 33.94  ? 18  ALA   B HB3  1 
ATOM   2730 N N    . ALA   B 1 39  ? 27.523 -22.037 36.330  1.00 22.99  ? 19  ALA   B N    1 
ATOM   2731 C CA   . ALA   B 1 39  ? 27.276 -20.635 36.623  1.00 22.57  ? 19  ALA   B CA   1 
ATOM   2732 C C    . ALA   B 1 39  ? 28.051 -19.733 35.682  1.00 22.10  ? 19  ALA   B C    1 
ATOM   2733 O O    . ALA   B 1 39  ? 27.501 -18.777 35.147  1.00 21.91  ? 19  ALA   B O    1 
ATOM   2734 C CB   . ALA   B 1 39  ? 27.627 -20.325 38.072  1.00 24.76  ? 19  ALA   B CB   1 
ATOM   2735 H H    . ALA   B 1 39  ? 27.885 -22.481 36.971  1.00 27.59  ? 19  ALA   B H    1 
ATOM   2736 H HA   . ALA   B 1 39  ? 26.330 -20.457 36.502  1.00 27.08  ? 19  ALA   B HA   1 
ATOM   2737 H HB1  . ALA   B 1 39  ? 27.465 -19.384 38.242  1.00 29.71  ? 19  ALA   B HB1  1 
ATOM   2738 H HB2  . ALA   B 1 39  ? 27.072 -20.867 38.655  1.00 29.71  ? 19  ALA   B HB2  1 
ATOM   2739 H HB3  . ALA   B 1 39  ? 28.563 -20.531 38.222  1.00 29.71  ? 19  ALA   B HB3  1 
ATOM   2740 N N    . ARG   B 1 40  ? 29.329 -20.038 35.445  1.00 21.62  ? 20  ARG   B N    1 
ATOM   2741 C CA   . ARG   B 1 40  ? 30.136 -19.199 34.574  1.00 21.89  ? 20  ARG   B CA   1 
ATOM   2742 C C    . ARG   B 1 40  ? 29.595 -19.163 33.147  1.00 22.52  ? 20  ARG   B C    1 
ATOM   2743 O O    . ARG   B 1 40  ? 29.525 -18.084 32.537  1.00 22.33  ? 20  ARG   B O    1 
ATOM   2744 C CB   . ARG   B 1 40  ? 31.589 -19.676 34.608  1.00 22.58  ? 20  ARG   B CB   1 
ATOM   2745 C CG   . ARG   B 1 40  ? 32.507 -18.810 33.779  1.00 23.67  ? 20  ARG   B CG   1 
ATOM   2746 C CD   . ARG   B 1 40  ? 33.957 -19.258 33.874  1.00 22.99  ? 20  ARG   B CD   1 
ATOM   2747 N NE   . ARG   B 1 40  ? 34.565 -19.050 35.189  1.00 22.77  ? 20  ARG   B NE   1 
ATOM   2748 C CZ   . ARG   B 1 40  ? 34.800 -19.996 36.083  1.00 23.19  ? 20  ARG   B CZ   1 
ATOM   2749 N NH1  . ARG   B 1 40  ? 34.488 -21.250 35.848  1.00 24.73  ? 20  ARG   B NH1  1 
ATOM   2750 N NH2  . ARG   B 1 40  ? 35.329 -19.665 37.250  1.00 23.90  ? 20  ARG   B NH2  1 
ATOM   2751 H H    . ARG   B 1 40  ? 29.742 -20.716 35.774  1.00 25.95  ? 20  ARG   B H    1 
ATOM   2752 H HA   . ARG   B 1 40  ? 30.110 -18.288 34.905  1.00 26.27  ? 20  ARG   B HA   1 
ATOM   2753 H HB2  . ARG   B 1 40  ? 31.906 -19.659 35.524  1.00 27.10  ? 20  ARG   B HB2  1 
ATOM   2754 H HB3  . ARG   B 1 40  ? 31.632 -20.580 34.258  1.00 27.10  ? 20  ARG   B HB3  1 
ATOM   2755 H HG2  . ARG   B 1 40  ? 32.236 -18.857 32.849  1.00 28.41  ? 20  ARG   B HG2  1 
ATOM   2756 H HG3  . ARG   B 1 40  ? 32.453 -17.894 34.095  1.00 28.41  ? 20  ARG   B HG3  1 
ATOM   2757 H HD2  . ARG   B 1 40  ? 34.003 -20.207 33.676  1.00 27.59  ? 20  ARG   B HD2  1 
ATOM   2758 H HD3  . ARG   B 1 40  ? 34.480 -18.759 33.227  1.00 27.59  ? 20  ARG   B HD3  1 
ATOM   2759 H HE   . ARG   B 1 40  ? 34.788 -18.246 35.397  1.00 27.32  ? 20  ARG   B HE   1 
ATOM   2760 H HH11 . ARG   B 1 40  ? 34.123 -21.469 35.101  1.00 29.68  ? 20  ARG   B HH11 1 
ATOM   2761 H HH12 . ARG   B 1 40  ? 34.648 -21.851 36.441  1.00 29.68  ? 20  ARG   B HH12 1 
ATOM   2762 H HH21 . ARG   B 1 40  ? 35.516 -18.843 37.420  1.00 28.68  ? 20  ARG   B HH21 1 
ATOM   2763 H HH22 . ARG   B 1 40  ? 35.486 -20.272 37.839  1.00 28.68  ? 20  ARG   B HH22 1 
ATOM   2764 N N    . GLN   B 1 41  ? 29.177 -20.307 32.609  1.00 24.50  ? 21  GLN   B N    1 
ATOM   2765 C CA   . GLN   B 1 41  ? 28.678 -20.331 31.231  1.00 26.89  ? 21  GLN   B CA   1 
ATOM   2766 C C    . GLN   B 1 41  ? 27.390 -19.531 31.091  1.00 25.83  ? 21  GLN   B C    1 
ATOM   2767 O O    . GLN   B 1 41  ? 27.208 -18.791 30.106  1.00 24.90  ? 21  GLN   B O    1 
ATOM   2768 C CB   . GLN   B 1 41  ? 28.429 -21.771 30.797  1.00 31.61  ? 21  GLN   B CB   1 
ATOM   2769 C CG   . GLN   B 1 41  ? 29.705 -22.609 30.796  1.00 38.98  ? 21  GLN   B CG   1 
ATOM   2770 C CD   . GLN   B 1 41  ? 29.454 -24.070 30.450  1.00 46.60  ? 21  GLN   B CD   1 
ATOM   2771 O OE1  . GLN   B 1 41  ? 28.394 -24.619 30.750  1.00 49.84  ? 21  GLN   B OE1  1 
ATOM   2772 N NE2  . GLN   B 1 41  ? 30.436 -24.708 29.816  1.00 51.42  ? 21  GLN   B NE2  1 
ATOM   2773 H H    . GLN   B 1 41  ? 29.172 -21.069 33.008  1.00 29.41  ? 21  GLN   B H    1 
ATOM   2774 H HA   . GLN   B 1 41  ? 29.352 -19.938 30.654  1.00 32.27  ? 21  GLN   B HA   1 
ATOM   2775 H HB2  . GLN   B 1 41  ? 27.798 -22.182 31.409  1.00 37.94  ? 21  GLN   B HB2  1 
ATOM   2776 H HB3  . GLN   B 1 41  ? 28.066 -21.773 29.897  1.00 37.94  ? 21  GLN   B HB3  1 
ATOM   2777 H HG2  . GLN   B 1 41  ? 30.320 -22.247 30.139  1.00 46.78  ? 21  GLN   B HG2  1 
ATOM   2778 H HG3  . GLN   B 1 41  ? 30.105 -22.575 31.679  1.00 46.78  ? 21  GLN   B HG3  1 
ATOM   2779 H HE21 . GLN   B 1 41  ? 31.165 -24.293 29.624  1.00 61.70  ? 21  GLN   B HE21 1 
ATOM   2780 H HE22 . GLN   B 1 41  ? 30.342 -25.535 29.599  1.00 61.70  ? 21  GLN   B HE22 1 
ATOM   2781 N N    . HIS   B 1 42  ? 26.478 -19.669 32.058  1.00 23.15  ? 22  HIS   B N    1 
ATOM   2782 C CA   . HIS   B 1 42  ? 25.253 -18.883 32.012  1.00 21.55  ? 22  HIS   B CA   1 
ATOM   2783 C C    . HIS   B 1 42  ? 25.541 -17.400 32.172  1.00 20.50  ? 22  HIS   B C    1 
ATOM   2784 O O    . HIS   B 1 42  ? 25.010 -16.565 31.429  1.00 20.07  ? 22  HIS   B O    1 
ATOM   2785 C CB   . HIS   B 1 42  ? 24.299 -19.331 33.099  1.00 22.37  ? 22  HIS   B CB   1 
ATOM   2786 C CG   . HIS   B 1 42  ? 23.189 -18.372 33.315  1.00 21.22  ? 22  HIS   B CG   1 
ATOM   2787 N ND1  . HIS   B 1 42  ? 22.044 -18.350 32.536  1.00 22.46  ? 22  HIS   B ND1  1 
ATOM   2788 C CD2  . HIS   B 1 42  ? 23.073 -17.357 34.199  1.00 20.51  ? 22  HIS   B CD2  1 
ATOM   2789 C CE1  . HIS   B 1 42  ? 21.270 -17.367 32.954  1.00 22.33  ? 22  HIS   B CE1  1 
ATOM   2790 N NE2  . HIS   B 1 42  ? 21.862 -16.768 33.970  1.00 20.81  ? 22  HIS   B NE2  1 
ATOM   2791 H H    . HIS   B 1 42  ? 26.547 -20.197 32.733  1.00 27.78  ? 22  HIS   B H    1 
ATOM   2792 H HA   . HIS   B 1 42  ? 24.835 -19.030 31.149  1.00 25.86  ? 22  HIS   B HA   1 
ATOM   2793 H HB2  . HIS   B 1 42  ? 23.914 -20.186 32.849  1.00 26.85  ? 22  HIS   B HB2  1 
ATOM   2794 H HB3  . HIS   B 1 42  ? 24.788 -19.419 33.932  1.00 26.85  ? 22  HIS   B HB3  1 
ATOM   2795 H HD2  . HIS   B 1 42  ? 23.697 -17.107 34.841  1.00 24.62  ? 22  HIS   B HD2  1 
ATOM   2796 H HE1  . HIS   B 1 42  ? 20.445 -17.134 32.593  1.00 26.79  ? 22  HIS   B HE1  1 
ATOM   2797 H HE2  . HIS   B 1 42  ? 21.536 -16.110 34.418  1.00 24.98  ? 22  HIS   B HE2  1 
ATOM   2798 N N    . ASN   B 1 43  ? 26.371 -17.051 33.149  1.00 19.06  ? 23  ASN   B N    1 
ATOM   2799 C CA   . ASN   B 1 43  ? 26.640 -15.641 33.405  1.00 18.82  ? 23  ASN   B CA   1 
ATOM   2800 C C    . ASN   B 1 43  ? 27.313 -14.978 32.205  1.00 18.10  ? 23  ASN   B C    1 
ATOM   2801 O O    . ASN   B 1 43  ? 27.048 -13.809 31.898  1.00 17.90  ? 23  ASN   B O    1 
ATOM   2802 C CB   . ASN   B 1 43  ? 27.514 -15.492 34.649  1.00 19.07  ? 23  ASN   B CB   1 
ATOM   2803 C CG   . ASN   B 1 43  ? 26.814 -15.947 35.926  1.00 18.68  ? 23  ASN   B CG   1 
ATOM   2804 O OD1  . ASN   B 1 43  ? 25.588 -16.046 36.008  1.00 20.07  ? 23  ASN   B OD1  1 
ATOM   2805 N ND2  . ASN   B 1 43  ? 27.614 -16.179 36.956  1.00 20.13  ? 23  ASN   B ND2  1 
ATOM   2806 H H    . ASN   B 1 43  ? 26.784 -17.599 33.669  1.00 22.87  ? 23  ASN   B H    1 
ATOM   2807 H HA   . ASN   B 1 43  ? 25.797 -15.190 33.567  1.00 22.58  ? 23  ASN   B HA   1 
ATOM   2808 H HB2  . ASN   B 1 43  ? 28.314 -16.030 34.539  1.00 22.89  ? 23  ASN   B HB2  1 
ATOM   2809 H HB3  . ASN   B 1 43  ? 27.754 -14.559 34.756  1.00 22.89  ? 23  ASN   B HB3  1 
ATOM   2810 H HD21 . ASN   B 1 43  ? 27.285 -16.439 37.707  1.00 24.16  ? 23  ASN   B HD21 1 
ATOM   2811 H HD22 . ASN   B 1 43  ? 28.464 -16.071 36.874  1.00 24.16  ? 23  ASN   B HD22 1 
ATOM   2812 N N    . ARG   B 1 44  ? 28.200 -15.706 31.517  1.00 18.81  ? 24  ARG   B N    1 
ATOM   2813 C CA   . ARG   B 1 44  ? 28.822 -15.151 30.319  1.00 18.80  ? 24  ARG   B CA   1 
ATOM   2814 C C    . ARG   B 1 44  ? 27.776 -14.764 29.283  1.00 19.88  ? 24  ARG   B C    1 
ATOM   2815 O O    . ARG   B 1 44  ? 27.901 -13.716 28.629  1.00 19.14  ? 24  ARG   B O    1 
ATOM   2816 C CB   . ARG   B 1 44  ? 29.832 -16.136 29.722  1.00 20.50  ? 24  ARG   B CB   1 
ATOM   2817 C CG   . ARG   B 1 44  ? 30.552 -15.566 28.521  1.00 26.77  ? 24  ARG   B CG   1 
ATOM   2818 C CD   . ARG   B 1 44  ? 31.602 -16.531 28.003  1.00 34.36  ? 24  ARG   B CD   1 
ATOM   2819 N NE   . ARG   B 1 44  ? 32.801 -15.872 27.491  1.00 41.38  ? 24  ARG   B NE   1 
ATOM   2820 C CZ   . ARG   B 1 44  ? 32.824 -15.094 26.420  1.00 47.68  ? 24  ARG   B CZ   1 
ATOM   2821 N NH1  . ARG   B 1 44  ? 31.718 -14.818 25.743  1.00 51.01  ? 24  ARG   B NH1  1 
ATOM   2822 N NH2  . ARG   B 1 44  ? 33.974 -14.556 26.036  1.00 50.13  ? 24  ARG   B NH2  1 
ATOM   2823 H H    . ARG   B 1 44  ? 28.451 -16.503 31.720  1.00 22.57  ? 24  ARG   B H    1 
ATOM   2824 H HA   . ARG   B 1 44  ? 29.310 -14.352 30.572  1.00 22.56  ? 24  ARG   B HA   1 
ATOM   2825 H HB2  . ARG   B 1 44  ? 30.495 -16.358 30.394  1.00 24.61  ? 24  ARG   B HB2  1 
ATOM   2826 H HB3  . ARG   B 1 44  ? 29.364 -16.938 29.440  1.00 24.61  ? 24  ARG   B HB3  1 
ATOM   2827 H HG2  . ARG   B 1 44  ? 29.913 -15.398 27.812  1.00 32.13  ? 24  ARG   B HG2  1 
ATOM   2828 H HG3  . ARG   B 1 44  ? 30.993 -14.739 28.773  1.00 32.13  ? 24  ARG   B HG3  1 
ATOM   2829 H HD2  . ARG   B 1 44  ? 31.872 -17.118 28.726  1.00 41.24  ? 24  ARG   B HD2  1 
ATOM   2830 H HD3  . ARG   B 1 44  ? 31.218 -17.051 27.279  1.00 41.24  ? 24  ARG   B HD3  1 
ATOM   2831 H HE   . ARG   B 1 44  ? 33.540 -15.998 27.913  1.00 49.66  ? 24  ARG   B HE   1 
ATOM   2832 H HH11 . ARG   B 1 44  ? 30.965 -15.147 25.996  1.00 61.22  ? 24  ARG   B HH11 1 
ATOM   2833 H HH12 . ARG   B 1 44  ? 31.755 -14.310 25.050  1.00 61.22  ? 24  ARG   B HH12 1 
ATOM   2834 H HH21 . ARG   B 1 44  ? 34.693 -14.714 26.481  1.00 60.16  ? 24  ARG   B HH21 1 
ATOM   2835 H HH22 . ARG   B 1 44  ? 34.001 -14.049 25.342  1.00 60.16  ? 24  ARG   B HH22 1 
ATOM   2836 N N    . LYS   B 1 45  ? 26.719 -15.574 29.132  1.00 21.18  ? 25  LYS   B N    1 
ATOM   2837 C CA   . LYS   B 1 45  ? 25.686 -15.234 28.165  1.00 22.07  ? 25  LYS   B CA   1 
ATOM   2838 C C    . LYS   B 1 45  ? 24.962 -13.957 28.568  1.00 20.39  ? 25  LYS   B C    1 
ATOM   2839 O O    . LYS   B 1 45  ? 24.600 -13.150 27.708  1.00 20.19  ? 25  LYS   B O    1 
ATOM   2840 C CB   . LYS   B 1 45  ? 24.701 -16.405 28.031  1.00 24.17  ? 25  LYS   B CB   1 
ATOM   2841 C CG   . LYS   B 1 45  ? 25.326 -17.594 27.375  1.00 27.92  ? 25  LYS   B CG   1 
ATOM   2842 H H    . LYS   B 1 45  ? 26.585 -16.303 29.567  1.00 25.42  ? 25  LYS   B H    1 
ATOM   2843 H HA   . LYS   B 1 45  ? 26.092 -15.083 27.298  1.00 26.48  ? 25  LYS   B HA   1 
ATOM   2844 H HB2  . LYS   B 1 45  ? 24.399 -16.670 28.914  1.00 29.01  ? 25  LYS   B HB2  1 
ATOM   2845 H HB3  . LYS   B 1 45  ? 23.944 -16.125 27.492  1.00 29.01  ? 25  LYS   B HB3  1 
ATOM   2846 N N    . ILE   B 1 46  ? 24.775 -13.740 29.876  1.00 18.20  ? 26  ILE   B N    1 
ATOM   2847 C CA   . ILE   B 1 46  ? 24.145 -12.510 30.342  1.00 17.55  ? 26  ILE   B CA   1 
ATOM   2848 C C    . ILE   B 1 46  ? 25.042 -11.309 30.059  1.00 17.54  ? 26  ILE   B C    1 
ATOM   2849 O O    . ILE   B 1 46  ? 24.564 -10.254 29.623  1.00 17.72  ? 26  ILE   B O    1 
ATOM   2850 C CB   . ILE   B 1 46  ? 23.793 -12.613 31.832  1.00 18.57  ? 26  ILE   B CB   1 
ATOM   2851 C CG1  . ILE   B 1 46  ? 22.824 -13.768 32.105  1.00 21.20  ? 26  ILE   B CG1  1 
ATOM   2852 C CG2  . ILE   B 1 46  ? 23.226 -11.294 32.341  1.00 19.01  ? 26  ILE   B CG2  1 
ATOM   2853 C CD1  . ILE   B 1 46  ? 21.486 -13.613 31.482  1.00 24.06  ? 26  ILE   B CD1  1 
ATOM   2854 H H    . ILE   B 1 46  ? 25.002 -14.284 30.502  1.00 21.84  ? 26  ILE   B H    1 
ATOM   2855 H HA   . ILE   B 1 46  ? 23.318 -12.388 29.851  1.00 21.06  ? 26  ILE   B HA   1 
ATOM   2856 H HB   . ILE   B 1 46  ? 24.613 -12.804 32.314  1.00 22.28  ? 26  ILE   B HB   1 
ATOM   2857 H HG12 . ILE   B 1 46  ? 23.214 -14.586 31.759  1.00 25.45  ? 26  ILE   B HG12 1 
ATOM   2858 H HG13 . ILE   B 1 46  ? 22.694 -13.841 33.063  1.00 25.45  ? 26  ILE   B HG13 1 
ATOM   2859 H HG21 . ILE   B 1 46  ? 22.812 -11.441 33.206  1.00 22.82  ? 26  ILE   B HG21 1 
ATOM   2860 H HG22 . ILE   B 1 46  ? 23.948 -10.652 32.425  1.00 22.82  ? 26  ILE   B HG22 1 
ATOM   2861 H HG23 . ILE   B 1 46  ? 22.566 -10.969 31.709  1.00 22.82  ? 26  ILE   B HG23 1 
ATOM   2862 H HD11 . ILE   B 1 46  ? 20.933 -14.369 31.731  1.00 28.88  ? 26  ILE   B HD11 1 
ATOM   2863 H HD12 . ILE   B 1 46  ? 21.084 -12.789 31.799  1.00 28.88  ? 26  ILE   B HD12 1 
ATOM   2864 H HD13 . ILE   B 1 46  ? 21.589 -13.580 30.518  1.00 28.88  ? 26  ILE   B HD13 1 
ATOM   2865 N N    . VAL   B 1 47  ? 26.349 -11.435 30.296  1.00 16.54  ? 27  VAL   B N    1 
ATOM   2866 C CA   . VAL   B 1 47  ? 27.262 -10.325 29.984  1.00 16.69  ? 27  VAL   B CA   1 
ATOM   2867 C C    . VAL   B 1 47  ? 27.198 -9.994  28.495  1.00 15.87  ? 27  VAL   B C    1 
ATOM   2868 O O    . VAL   B 1 47  ? 27.130 -8.819  28.101  1.00 16.15  ? 27  VAL   B O    1 
ATOM   2869 C CB   . VAL   B 1 47  ? 28.701 -10.643 30.421  1.00 16.44  ? 27  VAL   B CB   1 
ATOM   2870 C CG1  . VAL   B 1 47  ? 29.614 -9.522  29.979  1.00 17.33  ? 27  VAL   B CG1  1 
ATOM   2871 C CG2  . VAL   B 1 47  ? 28.781 -10.840 31.920  1.00 17.19  ? 27  VAL   B CG2  1 
ATOM   2872 H H    . VAL   B 1 47  ? 26.727 -12.133 30.628  1.00 19.85  ? 27  VAL   B H    1 
ATOM   2873 H HA   . VAL   B 1 47  ? 26.969 -9.548  30.486  1.00 20.03  ? 27  VAL   B HA   1 
ATOM   2874 H HB   . VAL   B 1 47  ? 28.990 -11.470 30.006  1.00 19.73  ? 27  VAL   B HB   1 
ATOM   2875 H HG11 . VAL   B 1 47  ? 30.462 -9.604  30.442  1.00 20.80  ? 27  VAL   B HG11 1 
ATOM   2876 H HG12 . VAL   B 1 47  ? 29.752 -9.587  29.021  1.00 20.80  ? 27  VAL   B HG12 1 
ATOM   2877 H HG13 . VAL   B 1 47  ? 29.199 -8.673  30.196  1.00 20.80  ? 27  VAL   B HG13 1 
ATOM   2878 H HG21 . VAL   B 1 47  ? 29.709 -10.961 32.174  1.00 20.63  ? 27  VAL   B HG21 1 
ATOM   2879 H HG22 . VAL   B 1 47  ? 28.417 -10.056 32.362  1.00 20.63  ? 27  VAL   B HG22 1 
ATOM   2880 H HG23 . VAL   B 1 47  ? 28.266 -11.625 32.163  1.00 20.63  ? 27  VAL   B HG23 1 
ATOM   2881 N N    . GLU   B 1 48  ? 27.270 -11.025 27.648  1.00 17.19  ? 28  GLU   B N    1 
ATOM   2882 C CA   . GLU   B 1 48  ? 27.124 -10.830 26.216  1.00 18.34  ? 28  GLU   B CA   1 
ATOM   2883 C C    . GLU   B 1 48  ? 25.823 -10.097 25.886  1.00 17.84  ? 28  GLU   B C    1 
ATOM   2884 O O    . GLU   B 1 48  ? 25.807 -9.134  25.101  1.00 18.66  ? 28  GLU   B O    1 
ATOM   2885 C CB   . GLU   B 1 48  ? 27.158 -12.182 25.492  1.00 20.98  ? 28  GLU   B CB   1 
ATOM   2886 C CG   . GLU   B 1 48  ? 28.517 -12.851 25.472  1.00 25.61  ? 28  GLU   B CG   1 
ATOM   2887 C CD   . GLU   B 1 48  ? 29.399 -12.400 24.320  1.00 33.69  ? 28  GLU   B CD   1 
ATOM   2888 O OE1  . GLU   B 1 48  ? 29.097 -11.362 23.677  1.00 35.39  ? 28  GLU   B OE1  1 
ATOM   2889 O OE2  . GLU   B 1 48  ? 30.411 -13.093 24.064  1.00 36.58  ? 28  GLU   B OE2  1 
ATOM   2890 H H    . GLU   B 1 48  ? 27.403 -11.842 27.882  1.00 20.63  ? 28  GLU   B H    1 
ATOM   2891 H HA   . GLU   B 1 48  ? 27.869 -10.293 25.903  1.00 22.01  ? 28  GLU   B HA   1 
ATOM   2892 H HB2  . GLU   B 1 48  ? 26.541 -12.784 25.936  1.00 25.18  ? 28  GLU   B HB2  1 
ATOM   2893 H HB3  . GLU   B 1 48  ? 26.885 -12.046 24.572  1.00 25.18  ? 28  GLU   B HB3  1 
ATOM   2894 H HG2  . GLU   B 1 48  ? 28.980 -12.644 26.299  1.00 30.74  ? 28  GLU   B HG2  1 
ATOM   2895 H HG3  . GLU   B 1 48  ? 28.392 -13.810 25.393  1.00 30.74  ? 28  GLU   B HG3  1 
ATOM   2896 N N    A GLN   B 1 49  ? 24.715 -10.534 26.475  0.58 17.21  ? 29  GLN   B N    1 
ATOM   2897 N N    B GLN   B 1 49  ? 24.710 -10.553 26.466  0.42 17.99  ? 29  GLN   B N    1 
ATOM   2898 C CA   A GLN   B 1 49  ? 23.457 -9.874  26.165  0.58 18.57  ? 29  GLN   B CA   1 
ATOM   2899 C CA   B GLN   B 1 49  ? 23.430 -9.901  26.211  0.42 19.38  ? 29  GLN   B CA   1 
ATOM   2900 C C    A GLN   B 1 49  ? 23.469 -8.419  26.610  0.58 17.85  ? 29  GLN   B C    1 
ATOM   2901 C C    B GLN   B 1 49  ? 23.475 -8.433  26.610  0.42 18.29  ? 29  GLN   B C    1 
ATOM   2902 O O    A GLN   B 1 49  ? 23.008 -7.533  25.880  0.58 19.32  ? 29  GLN   B O    1 
ATOM   2903 O O    B GLN   B 1 49  ? 23.058 -7.553  25.848  0.42 19.45  ? 29  GLN   B O    1 
ATOM   2904 C CB   A GLN   B 1 49  ? 22.300 -10.597 26.827  0.58 20.86  ? 29  GLN   B CB   1 
ATOM   2905 C CB   B GLN   B 1 49  ? 22.320 -10.618 26.981  0.42 21.78  ? 29  GLN   B CB   1 
ATOM   2906 C CG   A GLN   B 1 49  ? 21.000 -10.088 26.319  0.58 24.53  ? 29  GLN   B CG   1 
ATOM   2907 C CG   B GLN   B 1 49  ? 21.984 -12.002 26.444  0.42 25.30  ? 29  GLN   B CG   1 
ATOM   2908 C CD   A GLN   B 1 49  ? 19.841 -10.690 27.037  0.58 28.44  ? 29  GLN   B CD   1 
ATOM   2909 C CD   B GLN   B 1 49  ? 20.965 -12.717 27.313  0.42 29.67  ? 29  GLN   B CD   1 
ATOM   2910 O OE1  A GLN   B 1 49  ? 19.927 -11.797 27.565  0.58 32.41  ? 29  GLN   B OE1  1 
ATOM   2911 O OE1  B GLN   B 1 49  ? 19.924 -12.160 27.651  0.42 32.54  ? 29  GLN   B OE1  1 
ATOM   2912 N NE2  A GLN   B 1 49  ? 18.744 -9.953  27.086  0.58 26.57  ? 29  GLN   B NE2  1 
ATOM   2913 N NE2  B GLN   B 1 49  ? 21.264 -13.953 27.681  0.42 32.26  ? 29  GLN   B NE2  1 
ATOM   2914 H H    A GLN   B 1 49  ? 24.667 -11.185 27.036  0.58 20.65  ? 29  GLN   B H    1 
ATOM   2915 H H    B GLN   B 1 49  ? 24.673 -11.225 27.002  0.42 21.59  ? 29  GLN   B H    1 
ATOM   2916 H HA   A GLN   B 1 49  ? 23.331 -9.905  25.204  0.58 22.28  ? 29  GLN   B HA   1 
ATOM   2917 H HA   B GLN   B 1 49  ? 23.235 -9.957  25.263  0.42 23.26  ? 29  GLN   B HA   1 
ATOM   2918 H HB2  A GLN   B 1 49  ? 22.357 -11.546 26.632  0.58 25.03  ? 29  GLN   B HB2  1 
ATOM   2919 H HB2  B GLN   B 1 49  ? 22.599 -10.720 27.904  0.42 26.14  ? 29  GLN   B HB2  1 
ATOM   2920 H HB3  A GLN   B 1 49  ? 22.334 -10.453 27.786  0.58 25.03  ? 29  GLN   B HB3  1 
ATOM   2921 H HB3  B GLN   B 1 49  ? 21.514 -10.080 26.935  0.42 26.14  ? 29  GLN   B HB3  1 
ATOM   2922 H HG2  A GLN   B 1 49  ? 20.965 -9.127  26.442  0.58 29.44  ? 29  GLN   B HG2  1 
ATOM   2923 H HG2  B GLN   B 1 49  ? 21.614 -11.917 25.551  0.42 30.36  ? 29  GLN   B HG2  1 
ATOM   2924 H HG3  A GLN   B 1 49  ? 20.919 -10.306 25.378  0.58 29.44  ? 29  GLN   B HG3  1 
ATOM   2925 H HG3  B GLN   B 1 49  ? 22.791 -12.539 26.419  0.42 30.36  ? 29  GLN   B HG3  1 
ATOM   2926 H HE21 A GLN   B 1 49  ? 18.731 -9.176  26.717  0.58 31.89  ? 29  GLN   B HE21 1 
ATOM   2927 H HE21 B GLN   B 1 49  ? 22.004 -14.310 27.428  0.42 38.71  ? 29  GLN   B HE21 1 
ATOM   2928 H HE22 A GLN   B 1 49  ? 18.044 -10.250 27.487  0.58 31.89  ? 29  GLN   B HE22 1 
ATOM   2929 H HE22 B GLN   B 1 49  ? 20.718 -14.398 28.174  0.42 38.71  ? 29  GLN   B HE22 1 
ATOM   2930 N N    . TYR   B 1 50  ? 23.977 -8.147  27.812  1.00 16.70  ? 30  TYR   B N    1 
ATOM   2931 C CA   . TYR   B 1 50  ? 24.061 -6.768  28.274  1.00 15.93  ? 30  TYR   B CA   1 
ATOM   2932 C C    . TYR   B 1 50  ? 24.843 -5.919  27.295  1.00 15.91  ? 30  TYR   B C    1 
ATOM   2933 O O    . TYR   B 1 50  ? 24.388 -4.838  26.897  1.00 16.03  ? 30  TYR   B O    1 
ATOM   2934 C CB   . TYR   B 1 50  ? 24.674 -6.736  29.669  1.00 15.81  ? 30  TYR   B CB   1 
ATOM   2935 C CG   . TYR   B 1 50  ? 24.760 -5.355  30.267  1.00 14.75  ? 30  TYR   B CG   1 
ATOM   2936 C CD1  . TYR   B 1 50  ? 25.718 -4.433  29.848  1.00 14.77  ? 30  TYR   B CD1  1 
ATOM   2937 C CD2  . TYR   B 1 50  ? 23.909 -4.978  31.280  1.00 16.28  ? 30  TYR   B CD2  1 
ATOM   2938 C CE1  . TYR   B 1 50  ? 25.784 -3.180  30.394  1.00 16.47  ? 30  TYR   B CE1  1 
ATOM   2939 C CE2  . TYR   B 1 50  ? 23.973 -3.716  31.833  1.00 16.47  ? 30  TYR   B CE2  1 
ATOM   2940 C CZ   . TYR   B 1 50  ? 24.922 -2.828  31.393  1.00 17.04  ? 30  TYR   B CZ   1 
ATOM   2941 O OH   . TYR   B 1 50  ? 24.971 -1.587  31.951  1.00 19.49  ? 30  TYR   B OH   1 
ATOM   2942 H H    A TYR   B 1 50  ? 24.274 -8.733  28.367  0.58 20.04  ? 30  TYR   B H    1 
ATOM   2943 H H    B TYR   B 1 50  ? 24.272 -8.729  28.372  0.42 20.04  ? 30  TYR   B H    1 
ATOM   2944 H HA   . TYR   B 1 50  ? 23.170 -6.388  28.337  1.00 19.12  ? 30  TYR   B HA   1 
ATOM   2945 H HB2  . TYR   B 1 50  ? 24.131 -7.281  30.260  1.00 18.98  ? 30  TYR   B HB2  1 
ATOM   2946 H HB3  . TYR   B 1 50  ? 25.574 -7.094  29.621  1.00 18.98  ? 30  TYR   B HB3  1 
ATOM   2947 H HD1  . TYR   B 1 50  ? 26.324 -4.674  29.185  1.00 17.73  ? 30  TYR   B HD1  1 
ATOM   2948 H HD2  . TYR   B 1 50  ? 23.279 -5.585  31.598  1.00 19.54  ? 30  TYR   B HD2  1 
ATOM   2949 H HE1  . TYR   B 1 50  ? 26.414 -2.570  30.086  1.00 19.77  ? 30  TYR   B HE1  1 
ATOM   2950 H HE2  . TYR   B 1 50  ? 23.376 -3.467  32.501  1.00 19.76  ? 30  TYR   B HE2  1 
ATOM   2951 H HH   . TYR   B 1 50  ? 25.555 -1.122  31.565  1.00 23.40  ? 30  TYR   B HH   1 
ATOM   2952 N N    . MET   B 1 51  ? 26.039 -6.380  26.914  1.00 15.79  ? 31  MET   B N    1 
ATOM   2953 C CA   . MET   B 1 51  ? 26.919 -5.560  26.095  1.00 16.23  ? 31  MET   B CA   1 
ATOM   2954 C C    . MET   B 1 51  ? 26.364 -5.328  24.704  1.00 16.67  ? 31  MET   B C    1 
ATOM   2955 O O    . MET   B 1 51  ? 26.737 -4.339  24.062  1.00 17.54  ? 31  MET   B O    1 
ATOM   2956 C CB   . MET   B 1 51  ? 28.305 -6.200  25.993  1.00 16.58  ? 31  MET   B CB   1 
ATOM   2957 C CG   . MET   B 1 51  ? 29.059 -6.324  27.317  1.00 16.70  ? 31  MET   B CG   1 
ATOM   2958 S SD   . MET   B 1 51  ? 29.246 -4.806  28.241  1.00 16.27  ? 31  MET   B SD   1 
ATOM   2959 C CE   . MET   B 1 51  ? 30.022 -3.744  27.021  1.00 17.43  ? 31  MET   B CE   1 
ATOM   2960 H H    . MET   B 1 51  ? 26.354 -7.154  27.116  1.00 18.95  ? 31  MET   B H    1 
ATOM   2961 H HA   . MET   B 1 51  ? 27.023 -4.703  26.538  1.00 19.47  ? 31  MET   B HA   1 
ATOM   2962 H HB2  . MET   B 1 51  ? 28.205 -7.094  25.630  1.00 19.90  ? 31  MET   B HB2  1 
ATOM   2963 H HB3  . MET   B 1 51  ? 28.849 -5.660  25.398  1.00 19.90  ? 31  MET   B HB3  1 
ATOM   2964 H HG2  . MET   B 1 51  ? 28.580 -6.949  27.883  1.00 20.04  ? 31  MET   B HG2  1 
ATOM   2965 H HG3  . MET   B 1 51  ? 29.950 -6.660  27.131  1.00 20.04  ? 31  MET   B HG3  1 
ATOM   2966 H HE1  . MET   B 1 51  ? 30.219 -2.886  27.428  1.00 20.92  ? 31  MET   B HE1  1 
ATOM   2967 H HE2  . MET   B 1 51  ? 30.843 -4.161  26.715  1.00 20.92  ? 31  MET   B HE2  1 
ATOM   2968 H HE3  . MET   B 1 51  ? 29.414 -3.624  26.274  1.00 20.92  ? 31  MET   B HE3  1 
ATOM   2969 N N    . HIS   B 1 52  ? 25.484 -6.210  24.220  1.00 17.28  ? 32  HIS   B N    1 
ATOM   2970 C CA   . HIS   B 1 52  ? 24.895 -6.087  22.896  1.00 18.89  ? 32  HIS   B CA   1 
ATOM   2971 C C    . HIS   B 1 52  ? 23.493 -5.496  22.900  1.00 20.55  ? 32  HIS   B C    1 
ATOM   2972 O O    . HIS   B 1 52  ? 22.850 -5.458  21.848  1.00 23.78  ? 32  HIS   B O    1 
ATOM   2973 C CB   . HIS   B 1 52  ? 24.951 -7.422  22.182  1.00 21.18  ? 32  HIS   B CB   1 
ATOM   2974 C CG   . HIS   B 1 52  ? 26.341 -7.769  21.765  1.00 22.83  ? 32  HIS   B CG   1 
ATOM   2975 N ND1  . HIS   B 1 52  ? 27.172 -8.583  22.502  1.00 27.13  ? 32  HIS   B ND1  1 
ATOM   2976 C CD2  . HIS   B 1 52  ? 27.080 -7.318  20.729  1.00 24.46  ? 32  HIS   B CD2  1 
ATOM   2977 C CE1  . HIS   B 1 52  ? 28.334 -8.692  21.886  1.00 27.59  ? 32  HIS   B CE1  1 
ATOM   2978 N NE2  . HIS   B 1 52  ? 28.312 -7.922  20.816  1.00 27.66  ? 32  HIS   B NE2  1 
ATOM   2979 H H    . HIS   B 1 52  ? 25.211 -6.901  24.654  1.00 20.74  ? 32  HIS   B H    1 
ATOM   2980 H HA   . HIS   B 1 52  ? 25.429 -5.467  22.375  1.00 22.67  ? 32  HIS   B HA   1 
ATOM   2981 H HB2  . HIS   B 1 52  ? 24.630 -8.117  22.777  1.00 25.42  ? 32  HIS   B HB2  1 
ATOM   2982 H HB3  . HIS   B 1 52  ? 24.396 -7.383  21.387  1.00 25.42  ? 32  HIS   B HB3  1 
ATOM   2983 H HD1  . HIS   B 1 52  ? 26.966 -8.960  23.247  1.00 32.56  ? 32  HIS   B HD1  1 
ATOM   2984 H HD2  . HIS   B 1 52  ? 26.807 -6.713  20.078  1.00 29.36  ? 32  HIS   B HD2  1 
ATOM   2985 H HE1  . HIS   B 1 52  ? 29.047 -9.222  22.159  1.00 33.10  ? 32  HIS   B HE1  1 
ATOM   2986 N N    . THR   B 1 53  ? 23.015 -5.014  24.037  1.00 19.81  ? 33  THR   B N    1 
ATOM   2987 C CA   . THR   B 1 53  ? 21.665 -4.444  24.103  1.00 20.10  ? 33  THR   B CA   1 
ATOM   2988 C C    . THR   B 1 53  ? 21.704 -3.015  23.567  1.00 20.76  ? 33  THR   B C    1 
ATOM   2989 O O    . THR   B 1 53  ? 22.437 -2.158  24.091  1.00 21.13  ? 33  THR   B O    1 
ATOM   2990 C CB   . THR   B 1 53  ? 21.145 -4.454  25.531  1.00 20.62  ? 33  THR   B CB   1 
ATOM   2991 O OG1  . THR   B 1 53  ? 21.048 -5.791  26.006  1.00 21.11  ? 33  THR   B OG1  1 
ATOM   2992 C CG2  . THR   B 1 53  ? 19.746 -3.825  25.621  1.00 21.06  ? 33  THR   B CG2  1 
ATOM   2993 H H    . THR   B 1 53  ? 23.444 -5.002  24.782  1.00 23.77  ? 33  THR   B H    1 
ATOM   2994 H HA   . THR   B 1 53  ? 21.063 -4.976  23.559  1.00 24.12  ? 33  THR   B HA   1 
ATOM   2995 H HB   . THR   B 1 53  ? 21.761 -3.943  26.078  1.00 24.74  ? 33  THR   B HB   1 
ATOM   2996 H HG1  . THR   B 1 53  ? 21.803 -6.158  25.988  1.00 25.34  ? 33  THR   B HG1  1 
ATOM   2997 H HG21 . THR   B 1 53  ? 19.358 -4.002  26.493  1.00 25.28  ? 33  THR   B HG21 1 
ATOM   2998 H HG22 . THR   B 1 53  ? 19.805 -2.866  25.492  1.00 25.28  ? 33  THR   B HG22 1 
ATOM   2999 H HG23 . THR   B 1 53  ? 19.169 -4.200  24.938  1.00 25.28  ? 33  THR   B HG23 1 
ATOM   3000 N N    . ARG   B 1 54  ? 20.918 -2.763  22.526  1.00 21.00  ? 34  ARG   B N    1 
ATOM   3001 C CA   . ARG   B 1 54  ? 20.955 -1.497  21.818  1.00 21.99  ? 34  ARG   B CA   1 
ATOM   3002 C C    . ARG   B 1 54  ? 19.543 -1.031  21.526  1.00 23.12  ? 34  ARG   B C    1 
ATOM   3003 O O    . ARG   B 1 54  ? 18.593 -1.814  21.522  1.00 24.33  ? 34  ARG   B O    1 
ATOM   3004 C CB   . ARG   B 1 54  ? 21.721 -1.608  20.509  1.00 21.97  ? 34  ARG   B CB   1 
ATOM   3005 C CG   . ARG   B 1 54  ? 23.198 -1.887  20.732  1.00 21.53  ? 34  ARG   B CG   1 
ATOM   3006 C CD   . ARG   B 1 54  ? 23.900 -2.036  19.446  1.00 21.43  ? 34  ARG   B CD   1 
ATOM   3007 N NE   . ARG   B 1 54  ? 25.309 -2.318  19.672  1.00 21.95  ? 34  ARG   B NE   1 
ATOM   3008 C CZ   . ARG   B 1 54  ? 26.145 -2.648  18.706  1.00 22.78  ? 34  ARG   B CZ   1 
ATOM   3009 N NH1  . ARG   B 1 54  ? 25.750 -2.698  17.452  1.00 23.10  ? 34  ARG   B NH1  1 
ATOM   3010 N NH2  . ARG   B 1 54  ? 27.416 -2.899  19.013  1.00 22.41  ? 34  ARG   B NH2  1 
ATOM   3011 H H    . ARG   B 1 54  ? 20.346 -3.321  22.209  1.00 25.21  ? 34  ARG   B H    1 
ATOM   3012 H HA   . ARG   B 1 54  ? 21.387 -0.839  22.385  1.00 26.39  ? 34  ARG   B HA   1 
ATOM   3013 H HB2  . ARG   B 1 54  ? 21.351 -2.335  19.985  1.00 26.37  ? 34  ARG   B HB2  1 
ATOM   3014 H HB3  . ARG   B 1 54  ? 21.640 -0.773  20.022  1.00 26.37  ? 34  ARG   B HB3  1 
ATOM   3015 H HG2  . ARG   B 1 54  ? 23.598 -1.148  21.218  1.00 25.84  ? 34  ARG   B HG2  1 
ATOM   3016 H HG3  . ARG   B 1 54  ? 23.300 -2.709  21.237  1.00 25.84  ? 34  ARG   B HG3  1 
ATOM   3017 H HD2  . ARG   B 1 54  ? 23.513 -2.772  18.947  1.00 25.72  ? 34  ARG   B HD2  1 
ATOM   3018 H HD3  . ARG   B 1 54  ? 23.826 -1.214  18.936  1.00 25.72  ? 34  ARG   B HD3  1 
ATOM   3019 H HE   . ARG   B 1 54  ? 25.612 -2.266  20.475  1.00 26.35  ? 34  ARG   B HE   1 
ATOM   3020 H HH11 . ARG   B 1 54  ? 24.934 -2.514  17.250  1.00 27.72  ? 34  ARG   B HH11 1 
ATOM   3021 H HH12 . ARG   B 1 54  ? 26.307 -2.916  16.834  1.00 27.72  ? 34  ARG   B HH12 1 
ATOM   3022 H HH21 . ARG   B 1 54  ? 27.680 -2.844  19.829  1.00 26.90  ? 34  ARG   B HH21 1 
ATOM   3023 H HH22 . ARG   B 1 54  ? 27.973 -3.115  18.394  1.00 26.90  ? 34  ARG   B HH22 1 
ATOM   3024 N N    . GLY   B 1 55  ? 19.428 0.262   21.244  1.00 24.08  ? 35  GLY   B N    1 
ATOM   3025 C CA   . GLY   B 1 55  ? 18.140 0.814   20.823  1.00 24.92  ? 35  GLY   B CA   1 
ATOM   3026 C C    . GLY   B 1 55  ? 17.089 0.669   21.895  1.00 25.05  ? 35  GLY   B C    1 
ATOM   3027 O O    . GLY   B 1 55  ? 17.368 0.788   23.098  1.00 23.78  ? 35  GLY   B O    1 
ATOM   3028 H H    . GLY   B 1 55  ? 20.068 0.835   21.286  1.00 28.89  ? 35  GLY   B H    1 
ATOM   3029 H HA2  . GLY   B 1 55  ? 18.243 1.756   20.619  1.00 29.90  ? 35  GLY   B HA2  1 
ATOM   3030 H HA3  . GLY   B 1 55  ? 17.834 0.350   20.027  1.00 29.90  ? 35  GLY   B HA3  1 
ATOM   3031 N N    . GLU   B 1 56  ? 15.855 0.408   21.450  1.00 28.06  ? 36  GLU   B N    1 
ATOM   3032 C CA   . GLU   B 1 56  ? 14.735 0.316   22.373  1.00 30.36  ? 36  GLU   B CA   1 
ATOM   3033 C C    . GLU   B 1 56  ? 14.870 -0.844  23.338  1.00 27.27  ? 36  GLU   B C    1 
ATOM   3034 O O    . GLU   B 1 56  ? 14.289 -0.800  24.426  1.00 26.07  ? 36  GLU   B O    1 
ATOM   3035 C CB   . GLU   B 1 56  ? 13.437 0.153   21.580  1.00 36.88  ? 36  GLU   B CB   1 
ATOM   3036 C CG   . GLU   B 1 56  ? 13.067 1.351   20.746  1.00 45.11  ? 36  GLU   B CG   1 
ATOM   3037 C CD   . GLU   B 1 56  ? 12.057 2.251   21.435  1.00 53.03  ? 36  GLU   B CD   1 
ATOM   3038 O OE1  . GLU   B 1 56  ? 12.415 2.885   22.447  1.00 55.61  ? 36  GLU   B OE1  1 
ATOM   3039 O OE2  . GLU   B 1 56  ? 10.899 2.314   20.971  1.00 55.76  ? 36  GLU   B OE2  1 
ATOM   3040 H H    . GLU   B 1 56  ? 15.648 0.282   20.625  1.00 33.67  ? 36  GLU   B H    1 
ATOM   3041 H HA   . GLU   B 1 56  ? 14.695 1.136   22.890  1.00 36.43  ? 36  GLU   B HA   1 
ATOM   3042 H HB2  . GLU   B 1 56  ? 13.532 -0.605  20.981  1.00 44.26  ? 36  GLU   B HB2  1 
ATOM   3043 H HB3  . GLU   B 1 56  ? 12.711 -0.007  22.203  1.00 44.26  ? 36  GLU   B HB3  1 
ATOM   3044 H HG2  . GLU   B 1 56  ? 13.865 1.873   20.570  1.00 54.14  ? 36  GLU   B HG2  1 
ATOM   3045 H HG3  . GLU   B 1 56  ? 12.678 1.047   19.910  1.00 54.14  ? 36  GLU   B HG3  1 
ATOM   3046 N N    . ALA   B 1 57  ? 15.673 -1.859  22.990  1.00 25.58  ? 37  ALA   B N    1 
ATOM   3047 C CA   . ALA   B 1 57  ? 15.906 -2.954  23.919  1.00 24.65  ? 37  ALA   B CA   1 
ATOM   3048 C C    . ALA   B 1 57  ? 16.574 -2.480  25.205  1.00 22.16  ? 37  ALA   B C    1 
ATOM   3049 O O    . ALA   B 1 57  ? 16.472 -3.147  26.232  1.00 22.40  ? 37  ALA   B O    1 
ATOM   3050 C CB   . ALA   B 1 57  ? 16.746 -4.037  23.245  1.00 26.53  ? 37  ALA   B CB   1 
ATOM   3051 H H    . ALA   B 1 57  ? 16.082 -1.930  22.237  1.00 30.69  ? 37  ALA   B H    1 
ATOM   3052 H HA   . ALA   B 1 57  ? 15.055 -3.352  24.163  1.00 29.58  ? 37  ALA   B HA   1 
ATOM   3053 H HB1  . ALA   B 1 57  ? 16.895 -4.760  23.875  1.00 31.83  ? 37  ALA   B HB1  1 
ATOM   3054 H HB2  . ALA   B 1 57  ? 16.269 -4.368  22.468  1.00 31.83  ? 37  ALA   B HB2  1 
ATOM   3055 H HB3  . ALA   B 1 57  ? 17.595 -3.655  22.973  1.00 31.83  ? 37  ALA   B HB3  1 
ATOM   3056 N N    . ARG   B 1 58  ? 17.244 -1.332  25.181  1.00 20.08  ? 38  ARG   B N    1 
ATOM   3057 C CA   . ARG   B 1 58  ? 17.808 -0.793  26.415  1.00 20.48  ? 38  ARG   B CA   1 
ATOM   3058 C C    . ARG   B 1 58  ? 16.749 -0.559  27.481  1.00 19.92  ? 38  ARG   B C    1 
ATOM   3059 O O    . ARG   B 1 58  ? 17.065 -0.604  28.673  1.00 19.08  ? 38  ARG   B O    1 
ATOM   3060 C CB   . ARG   B 1 58  ? 18.608 0.468   26.096  1.00 21.55  ? 38  ARG   B CB   1 
ATOM   3061 C CG   . ARG   B 1 58  ? 19.856 0.173   25.289  1.00 22.90  ? 38  ARG   B CG   1 
ATOM   3062 C CD   . ARG   B 1 58  ? 20.396 1.359   24.517  1.00 24.20  ? 38  ARG   B CD   1 
ATOM   3063 N NE   . ARG   B 1 58  ? 20.693 2.505   25.360  1.00 26.21  ? 38  ARG   B NE   1 
ATOM   3064 C CZ   . ARG   B 1 58  ? 20.951 3.715   24.873  1.00 25.28  ? 38  ARG   B CZ   1 
ATOM   3065 N NH1  . ARG   B 1 58  ? 20.897 3.958   23.581  1.00 28.66  ? 38  ARG   B NH1  1 
ATOM   3066 N NH2  . ARG   B 1 58  ? 21.162 4.727   25.712  1.00 26.13  ? 38  ARG   B NH2  1 
ATOM   3067 H H    . ARG   B 1 58  ? 17.384 -0.855  24.480  1.00 24.09  ? 38  ARG   B H    1 
ATOM   3068 H HA   . ARG   B 1 58  ? 18.425 -1.435  26.798  1.00 24.58  ? 38  ARG   B HA   1 
ATOM   3069 H HB2  . ARG   B 1 58  ? 18.052 1.075   25.581  1.00 25.87  ? 38  ARG   B HB2  1 
ATOM   3070 H HB3  . ARG   B 1 58  ? 18.878 0.890   26.926  1.00 25.87  ? 38  ARG   B HB3  1 
ATOM   3071 H HG2  . ARG   B 1 58  ? 20.553 -0.124  25.894  1.00 27.48  ? 38  ARG   B HG2  1 
ATOM   3072 H HG3  . ARG   B 1 58  ? 19.653 -0.525  24.648  1.00 27.48  ? 38  ARG   B HG3  1 
ATOM   3073 H HD2  . ARG   B 1 58  ? 21.216 1.097   24.071  1.00 29.04  ? 38  ARG   B HD2  1 
ATOM   3074 H HD3  . ARG   B 1 58  ? 19.736 1.635   23.861  1.00 29.04  ? 38  ARG   B HD3  1 
ATOM   3075 H HE   . ARG   B 1 58  ? 20.702 2.395   26.213  1.00 31.46  ? 38  ARG   B HE   1 
ATOM   3076 H HH11 . ARG   B 1 58  ? 20.692 3.327   23.033  1.00 34.40  ? 38  ARG   B HH11 1 
ATOM   3077 H HH12 . ARG   B 1 58  ? 21.067 4.747   23.284  1.00 34.40  ? 38  ARG   B HH12 1 
ATOM   3078 H HH21 . ARG   B 1 58  ? 21.131 4.596   26.561  1.00 31.36  ? 38  ARG   B HH21 1 
ATOM   3079 H HH22 . ARG   B 1 58  ? 21.329 5.513   25.404  1.00 31.36  ? 38  ARG   B HH22 1 
ATOM   3080 N N    . LEU   B 1 59  ? 15.490 -0.326  27.083  1.00 20.86  ? 39  LEU   B N    1 
ATOM   3081 C CA   . LEU   B 1 59  ? 14.428 -0.135  28.066  1.00 22.42  ? 39  LEU   B CA   1 
ATOM   3082 C C    . LEU   B 1 59  ? 14.127 -1.390  28.871  1.00 23.17  ? 39  LEU   B C    1 
ATOM   3083 O O    . LEU   B 1 59  ? 13.485 -1.281  29.918  1.00 23.15  ? 39  LEU   B O    1 
ATOM   3084 C CB   . LEU   B 1 59  ? 13.146 0.361   27.383  1.00 24.01  ? 39  LEU   B CB   1 
ATOM   3085 C CG   . LEU   B 1 59  ? 13.281 1.724   26.687  1.00 27.13  ? 39  LEU   B CG   1 
ATOM   3086 C CD1  . LEU   B 1 59  ? 12.018 2.094   25.969  1.00 28.44  ? 39  LEU   B CD1  1 
ATOM   3087 C CD2  . LEU   B 1 59  ? 13.667 2.821   27.687  1.00 29.10  ? 39  LEU   B CD2  1 
ATOM   3088 H H    . LEU   B 1 59  ? 15.235 -0.275  26.264  1.00 25.03  ? 39  LEU   B H    1 
ATOM   3089 H HA   . LEU   B 1 59  ? 14.715 0.552   28.688  1.00 26.90  ? 39  LEU   B HA   1 
ATOM   3090 H HB2  . LEU   B 1 59  ? 12.885 -0.287  26.710  1.00 28.81  ? 39  LEU   B HB2  1 
ATOM   3091 H HB3  . LEU   B 1 59  ? 12.450 0.442   28.054  1.00 28.81  ? 39  LEU   B HB3  1 
ATOM   3092 H HG   . LEU   B 1 59  ? 13.990 1.655   26.029  1.00 32.56  ? 39  LEU   B HG   1 
ATOM   3093 H HD11 . LEU   B 1 59  ? 12.137 2.959   25.547  1.00 34.13  ? 39  LEU   B HD11 1 
ATOM   3094 H HD12 . LEU   B 1 59  ? 11.828 1.421   25.297  1.00 34.13  ? 39  LEU   B HD12 1 
ATOM   3095 H HD13 . LEU   B 1 59  ? 11.291 2.136   26.610  1.00 34.13  ? 39  LEU   B HD13 1 
ATOM   3096 H HD21 . LEU   B 1 59  ? 13.621 3.683   27.245  1.00 34.92  ? 39  LEU   B HD21 1 
ATOM   3097 H HD22 . LEU   B 1 59  ? 13.049 2.799   28.434  1.00 34.92  ? 39  LEU   B HD22 1 
ATOM   3098 H HD23 . LEU   B 1 59  ? 14.571 2.658   28.001  1.00 34.92  ? 39  LEU   B HD23 1 
ATOM   3099 N N    . LYS   B 1 60  ? 14.623 -2.560  28.442  1.00 23.94  ? 40  LYS   B N    1 
ATOM   3100 C CA   . LYS   B 1 60  ? 14.411 -3.813  29.162  1.00 23.92  ? 40  LYS   B CA   1 
ATOM   3101 C C    . LYS   B 1 60  ? 15.696 -4.410  29.727  1.00 21.24  ? 40  LYS   B C    1 
ATOM   3102 O O    . LYS   B 1 60  ? 15.663 -5.507  30.286  1.00 22.58  ? 40  LYS   B O    1 
ATOM   3103 C CB   . LYS   B 1 60  ? 13.704 -4.849  28.271  1.00 28.28  ? 40  LYS   B CB   1 
ATOM   3104 C CG   . LYS   B 1 60  ? 12.293 -4.404  27.876  1.00 35.37  ? 40  LYS   B CG   1 
ATOM   3105 C CD   . LYS   B 1 60  ? 11.459 -5.557  27.391  1.00 43.04  ? 40  LYS   B CD   1 
ATOM   3106 C CE   . LYS   B 1 60  ? 11.507 -5.715  25.879  1.00 48.90  ? 40  LYS   B CE   1 
ATOM   3107 N NZ   . LYS   B 1 60  ? 10.192 -6.234  25.339  1.00 52.31  ? 40  LYS   B NZ   1 
ATOM   3108 H H    . LYS   B 1 60  ? 15.091 -2.650  27.726  1.00 28.73  ? 40  LYS   B H    1 
ATOM   3109 H HA   . LYS   B 1 60  ? 13.821 -3.626  29.909  1.00 28.70  ? 40  LYS   B HA   1 
ATOM   3110 H HB2  . LYS   B 1 60  ? 14.220 -4.975  27.459  1.00 33.94  ? 40  LYS   B HB2  1 
ATOM   3111 H HB3  . LYS   B 1 60  ? 13.634 -5.688  28.753  1.00 33.94  ? 40  LYS   B HB3  1 
ATOM   3112 H HG2  . LYS   B 1 60  ? 11.852 -4.015  28.648  1.00 42.45  ? 40  LYS   B HG2  1 
ATOM   3113 H HG3  . LYS   B 1 60  ? 12.351 -3.750  27.162  1.00 42.45  ? 40  LYS   B HG3  1 
ATOM   3114 H HD2  . LYS   B 1 60  ? 11.790 -6.378  27.789  1.00 51.65  ? 40  LYS   B HD2  1 
ATOM   3115 H HD3  . LYS   B 1 60  ? 10.536 -5.412  27.649  1.00 51.65  ? 40  LYS   B HD3  1 
ATOM   3116 H HE2  . LYS   B 1 60  ? 11.687 -4.854  25.470  1.00 58.69  ? 40  LYS   B HE2  1 
ATOM   3117 H HE3  . LYS   B 1 60  ? 12.205 -6.346  25.643  1.00 58.69  ? 40  LYS   B HE3  1 
ATOM   3118 H HZ1  . LYS   B 1 60  ? 10.241 -6.325  24.455  1.00 62.78  ? 40  LYS   B HZ1  1 
ATOM   3119 H HZ2  . LYS   B 1 60  ? 10.006 -7.025  25.701  1.00 62.78  ? 40  LYS   B HZ2  1 
ATOM   3120 H HZ3  . LYS   B 1 60  ? 9.537  -5.665  25.535  1.00 62.78  ? 40  LYS   B HZ3  1 
ATOM   3121 N N    . ARG   B 1 61  ? 16.828 -3.722  29.612  1.00 20.59  ? 41  ARG   B N    1 
ATOM   3122 C CA   . ARG   B 1 61  ? 18.096 -4.283  30.075  1.00 20.45  ? 41  ARG   B CA   1 
ATOM   3123 C C    . ARG   B 1 61  ? 18.111 -4.488  31.577  1.00 19.04  ? 41  ARG   B C    1 
ATOM   3124 O O    . ARG   B 1 61  ? 18.847 -5.352  32.075  1.00 19.25  ? 41  ARG   B O    1 
ATOM   3125 C CB   . ARG   B 1 61  ? 19.232 -3.352  29.657  1.00 21.08  ? 41  ARG   B CB   1 
ATOM   3126 C CG   . ARG   B 1 61  ? 20.615 -3.985  29.762  1.00 20.58  ? 41  ARG   B CG   1 
ATOM   3127 C CD   . ARG   B 1 61  ? 21.715 -3.031  29.218  1.00 21.94  ? 41  ARG   B CD   1 
ATOM   3128 N NE   . ARG   B 1 61  ? 21.814 -1.846  30.053  1.00 23.60  ? 41  ARG   B NE   1 
ATOM   3129 C CZ   . ARG   B 1 61  ? 22.268 -0.647  29.677  1.00 26.78  ? 41  ARG   B CZ   1 
ATOM   3130 N NH1  . ARG   B 1 61  ? 22.733 -0.416  28.457  1.00 27.69  ? 41  ARG   B NH1  1 
ATOM   3131 N NH2  . ARG   B 1 61  ? 22.243 0.350   30.551  1.00 30.75  ? 41  ARG   B NH2  1 
ATOM   3132 H H    . ARG   B 1 61  ? 16.890 -2.934  29.272  1.00 24.72  ? 41  ARG   B H    1 
ATOM   3133 H HA   . ARG   B 1 61  ? 18.240 -5.149  29.662  1.00 24.54  ? 41  ARG   B HA   1 
ATOM   3134 H HB2  . ARG   B 1 61  ? 19.096 -3.089  28.733  1.00 25.30  ? 41  ARG   B HB2  1 
ATOM   3135 H HB3  . ARG   B 1 61  ? 19.221 -2.569  30.230  1.00 25.30  ? 41  ARG   B HB3  1 
ATOM   3136 H HG2  . ARG   B 1 61  ? 20.811 -4.179  30.692  1.00 24.70  ? 41  ARG   B HG2  1 
ATOM   3137 H HG3  . ARG   B 1 61  ? 20.635 -4.803  29.241  1.00 24.70  ? 41  ARG   B HG3  1 
ATOM   3138 H HD2  . ARG   B 1 61  ? 22.572 -3.486  29.222  1.00 26.33  ? 41  ARG   B HD2  1 
ATOM   3139 H HD3  . ARG   B 1 61  ? 21.490 -2.756  28.315  1.00 26.33  ? 41  ARG   B HD3  1 
ATOM   3140 H HE   . ARG   B 1 61  ? 21.556 -1.925  30.869  1.00 28.32  ? 41  ARG   B HE   1 
ATOM   3141 H HH11 . ARG   B 1 61  ? 22.750 -1.050  27.876  1.00 33.23  ? 41  ARG   B HH11 1 
ATOM   3142 H HH12 . ARG   B 1 61  ? 23.018 0.368   28.247  1.00 33.23  ? 41  ARG   B HH12 1 
ATOM   3143 H HH21 . ARG   B 1 61  ? 21.939 0.218   31.344  1.00 36.90  ? 41  ARG   B HH21 1 
ATOM   3144 H HH22 . ARG   B 1 61  ? 22.532 1.127   30.324  1.00 36.90  ? 41  ARG   B HH22 1 
ATOM   3145 N N    . HIS   B 1 62  ? 17.291 -3.740  32.317  1.00 18.65  ? 42  HIS   B N    1 
ATOM   3146 C CA   . HIS   B 1 62  ? 17.242 -3.904  33.763  1.00 18.81  ? 42  HIS   B CA   1 
ATOM   3147 C C    . HIS   B 1 62  ? 16.748 -5.283  34.173  1.00 19.33  ? 42  HIS   B C    1 
ATOM   3148 O O    . HIS   B 1 62  ? 16.985 -5.687  35.317  1.00 19.04  ? 42  HIS   B O    1 
ATOM   3149 C CB   . HIS   B 1 62  ? 16.399 -2.787  34.380  1.00 19.81  ? 42  HIS   B CB   1 
ATOM   3150 C CG   . HIS   B 1 62  ? 14.951 -2.824  33.999  1.00 20.76  ? 42  HIS   B CG   1 
ATOM   3151 N ND1  . HIS   B 1 62  ? 14.500 -2.511  32.738  1.00 21.54  ? 42  HIS   B ND1  1 
ATOM   3152 C CD2  . HIS   B 1 62  ? 13.857 -3.144  34.724  1.00 22.52  ? 42  HIS   B CD2  1 
ATOM   3153 C CE1  . HIS   B 1 62  ? 13.181 -2.620  32.706  1.00 23.03  ? 42  HIS   B CE1  1 
ATOM   3154 N NE2  . HIS   B 1 62  ? 12.771 -3.013  33.895  1.00 23.71  ? 42  HIS   B NE2  1 
ATOM   3155 H H    . HIS   B 1 62  ? 16.760 -3.139  32.007  1.00 22.39  ? 42  HIS   B H    1 
ATOM   3156 H HA   . HIS   B 1 62  ? 18.136 -3.816  34.129  1.00 22.57  ? 42  HIS   B HA   1 
ATOM   3157 H HB2  . HIS   B 1 62  ? 16.450 -2.858  35.346  1.00 23.78  ? 42  HIS   B HB2  1 
ATOM   3158 H HB3  . HIS   B 1 62  ? 16.757 -1.933  34.092  1.00 23.78  ? 42  HIS   B HB3  1 
ATOM   3159 H HD2  . HIS   B 1 62  ? 13.843 -3.403  35.617  1.00 27.02  ? 42  HIS   B HD2  1 
ATOM   3160 H HE1  . HIS   B 1 62  ? 12.637 -2.448  31.971  1.00 27.64  ? 42  HIS   B HE1  1 
ATOM   3161 H HE2  . HIS   B 1 62  ? 11.953 -3.163  34.116  1.00 28.45  ? 42  HIS   B HE2  1 
ATOM   3162 N N    . LEU   B 1 63  ? 16.074 -6.016  33.273  1.00 18.99  ? 43  LEU   B N    1 
ATOM   3163 C CA   . LEU   B 1 63  ? 15.609 -7.357  33.592  1.00 20.05  ? 43  LEU   B CA   1 
ATOM   3164 C C    . LEU   B 1 63  ? 16.764 -8.352  33.665  1.00 19.53  ? 43  LEU   B C    1 
ATOM   3165 O O    . LEU   B 1 63  ? 16.563 -9.505  34.061  1.00 20.68  ? 43  LEU   B O    1 
ATOM   3166 C CB   . LEU   B 1 63  ? 14.597 -7.819  32.553  1.00 21.71  ? 43  LEU   B CB   1 
ATOM   3167 C CG   . LEU   B 1 63  ? 13.347 -6.927  32.471  1.00 24.62  ? 43  LEU   B CG   1 
ATOM   3168 C CD1  . LEU   B 1 63  ? 12.322 -7.458  31.448  1.00 27.36  ? 43  LEU   B CD1  1 
ATOM   3169 C CD2  . LEU   B 1 63  ? 12.684 -6.799  33.845  1.00 26.89  ? 43  LEU   B CD2  1 
ATOM   3170 H H    . LEU   B 1 63  ? 15.879 -5.753  32.478  1.00 22.80  ? 43  LEU   B H    1 
ATOM   3171 H HA   . LEU   B 1 63  ? 15.159 -7.345  34.451  1.00 24.06  ? 43  LEU   B HA   1 
ATOM   3172 H HB2  . LEU   B 1 63  ? 15.022 -7.815  31.682  1.00 26.05  ? 43  LEU   B HB2  1 
ATOM   3173 H HB3  . LEU   B 1 63  ? 14.307 -8.717  32.778  1.00 26.05  ? 43  LEU   B HB3  1 
ATOM   3174 H HG   . LEU   B 1 63  ? 13.633 -6.050  32.172  1.00 29.55  ? 43  LEU   B HG   1 
ATOM   3175 H HD11 . LEU   B 1 63  ? 11.555 -6.864  31.432  1.00 32.83  ? 43  LEU   B HD11 1 
ATOM   3176 H HD12 . LEU   B 1 63  ? 12.736 -7.487  30.572  1.00 32.83  ? 43  LEU   B HD12 1 
ATOM   3177 H HD13 . LEU   B 1 63  ? 12.044 -8.349  31.713  1.00 32.83  ? 43  LEU   B HD13 1 
ATOM   3178 H HD21 . LEU   B 1 63  ? 11.800 -6.416  33.734  1.00 32.27  ? 43  LEU   B HD21 1 
ATOM   3179 H HD22 . LEU   B 1 63  ? 12.615 -7.679  34.245  1.00 32.27  ? 43  LEU   B HD22 1 
ATOM   3180 H HD23 . LEU   B 1 63  ? 13.227 -6.222  34.405  1.00 32.27  ? 43  LEU   B HD23 1 
ATOM   3181 N N    . LEU   B 1 64  ? 17.979 -7.933  33.303  1.00 17.15  ? 44  LEU   B N    1 
ATOM   3182 C CA   . LEU   B 1 64  ? 19.171 -8.744  33.487  1.00 17.38  ? 44  LEU   B CA   1 
ATOM   3183 C C    . LEU   B 1 64  ? 19.733 -8.657  34.903  1.00 17.44  ? 44  LEU   B C    1 
ATOM   3184 O O    . LEU   B 1 64  ? 20.719 -9.340  35.195  1.00 17.69  ? 44  LEU   B O    1 
ATOM   3185 C CB   . LEU   B 1 64  ? 20.230 -8.384  32.443  1.00 18.51  ? 44  LEU   B CB   1 
ATOM   3186 C CG   . LEU   B 1 64  ? 19.830 -8.540  30.984  1.00 19.18  ? 44  LEU   B CG   1 
ATOM   3187 C CD1  . LEU   B 1 64  ? 20.984 -8.163  30.066  1.00 20.98  ? 44  LEU   B CD1  1 
ATOM   3188 C CD2  . LEU   B 1 64  ? 19.359 -9.958  30.677  1.00 20.26  ? 44  LEU   B CD2  1 
ATOM   3189 H H    . LEU   B 1 64  ? 18.135 -7.168  32.943  1.00 20.59  ? 44  LEU   B H    1 
ATOM   3190 H HA   . LEU   B 1 64  ? 18.946 -9.675  33.333  1.00 20.86  ? 44  LEU   B HA   1 
ATOM   3191 H HB2  . LEU   B 1 64  ? 20.476 -7.455  32.573  1.00 22.21  ? 44  LEU   B HB2  1 
ATOM   3192 H HB3  . LEU   B 1 64  ? 21.001 -8.955  32.589  1.00 22.21  ? 44  LEU   B HB3  1 
ATOM   3193 H HG   . LEU   B 1 64  ? 19.089 -7.939  30.812  1.00 23.01  ? 44  LEU   B HG   1 
ATOM   3194 H HD11 . LEU   B 1 64  ? 20.693 -8.240  29.144  1.00 25.18  ? 44  LEU   B HD11 1 
ATOM   3195 H HD12 . LEU   B 1 64  ? 21.251 -7.250  30.253  1.00 25.18  ? 44  LEU   B HD12 1 
ATOM   3196 H HD13 . LEU   B 1 64  ? 21.727 -8.765  30.229  1.00 25.18  ? 44  LEU   B HD13 1 
ATOM   3197 H HD21 . LEU   B 1 64  ? 19.196 -10.038 29.725  1.00 24.31  ? 44  LEU   B HD21 1 
ATOM   3198 H HD22 . LEU   B 1 64  ? 20.048 -10.585 30.949  1.00 24.31  ? 44  LEU   B HD22 1 
ATOM   3199 H HD23 . LEU   B 1 64  ? 18.541 -10.132 31.169  1.00 24.31  ? 44  LEU   B HD23 1 
ATOM   3200 N N    . PHE   B 1 65  ? 19.132 -7.838  35.769  1.00 17.11  ? 45  PHE   B N    1 
ATOM   3201 C CA   . PHE   B 1 65  ? 19.574 -7.613  37.139  1.00 17.29  ? 45  PHE   B CA   1 
ATOM   3202 C C    . PHE   B 1 65  ? 18.683 -8.307  38.160  1.00 17.62  ? 45  PHE   B C    1 
ATOM   3203 O O    . PHE   B 1 65  ? 17.490 -8.556  37.928  1.00 18.64  ? 45  PHE   B O    1 
ATOM   3204 C CB   . PHE   B 1 65  ? 19.572 -6.115  37.466  1.00 16.94  ? 45  PHE   B CB   1 
ATOM   3205 C CG   . PHE   B 1 65  ? 20.673 -5.344  36.780  1.00 16.26  ? 45  PHE   B CG   1 
ATOM   3206 C CD1  . PHE   B 1 65  ? 20.583 -5.058  35.428  1.00 17.81  ? 45  PHE   B CD1  1 
ATOM   3207 C CD2  . PHE   B 1 65  ? 21.781 -4.900  37.490  1.00 16.30  ? 45  PHE   B CD2  1 
ATOM   3208 C CE1  . PHE   B 1 65  ? 21.602 -4.335  34.789  1.00 19.06  ? 45  PHE   B CE1  1 
ATOM   3209 C CE2  . PHE   B 1 65  ? 22.780 -4.156  36.864  1.00 16.85  ? 45  PHE   B CE2  1 
ATOM   3210 C CZ   . PHE   B 1 65  ? 22.686 -3.887  35.510  1.00 17.03  ? 45  PHE   B CZ   1 
ATOM   3211 H H    . PHE   B 1 65  ? 18.432 -7.379  35.573  1.00 20.53  ? 45  PHE   B H    1 
ATOM   3212 H HA   . PHE   B 1 65  ? 20.467 -7.982  37.218  1.00 20.76  ? 45  PHE   B HA   1 
ATOM   3213 H HB2  . PHE   B 1 65  ? 18.724 -5.735  37.185  1.00 20.33  ? 45  PHE   B HB2  1 
ATOM   3214 H HB3  . PHE   B 1 65  ? 19.684 -6.004  38.423  1.00 20.33  ? 45  PHE   B HB3  1 
ATOM   3215 H HD1  . PHE   B 1 65  ? 19.845 -5.346  34.941  1.00 21.38  ? 45  PHE   B HD1  1 
ATOM   3216 H HD2  . PHE   B 1 65  ? 21.858 -5.102  38.395  1.00 19.56  ? 45  PHE   B HD2  1 
ATOM   3217 H HE1  . PHE   B 1 65  ? 21.546 -4.159  33.877  1.00 22.87  ? 45  PHE   B HE1  1 
ATOM   3218 H HE2  . PHE   B 1 65  ? 23.505 -3.842  37.354  1.00 20.23  ? 45  PHE   B HE2  1 
ATOM   3219 H HZ   . PHE   B 1 65  ? 23.357 -3.403  35.086  1.00 20.43  ? 45  PHE   B HZ   1 
ATOM   3220 N N    . THR   B 1 66  ? 19.267 -8.578  39.330  1.00 18.08  ? 46  THR   B N    1 
ATOM   3221 C CA   . THR   B 1 66  ? 18.476 -8.979  40.491  1.00 19.61  ? 46  THR   B CA   1 
ATOM   3222 C C    . THR   B 1 66  ? 17.608 -7.801  40.929  1.00 19.40  ? 46  THR   B C    1 
ATOM   3223 O O    . THR   B 1 66  ? 17.833 -6.658  40.539  1.00 19.14  ? 46  THR   B O    1 
ATOM   3224 C CB   . THR   B 1 66  ? 19.386 -9.378  41.647  1.00 20.10  ? 46  THR   B CB   1 
ATOM   3225 O OG1  . THR   B 1 66  ? 20.160 -8.235  42.049  1.00 20.42  ? 46  THR   B OG1  1 
ATOM   3226 C CG2  . THR   B 1 66  ? 20.315 -10.512 41.240  1.00 20.71  ? 46  THR   B CG2  1 
ATOM   3227 H H    . THR   B 1 66  ? 20.114 -8.538  39.474  1.00 21.70  ? 46  THR   B H    1 
ATOM   3228 H HA   . THR   B 1 66  ? 17.918 -9.740  40.266  1.00 23.54  ? 46  THR   B HA   1 
ATOM   3229 H HB   . THR   B 1 66  ? 18.851 -9.689  42.393  1.00 24.12  ? 46  THR   B HB   1 
ATOM   3230 H HG1  . THR   B 1 66  ? 20.655 -8.437  42.697  1.00 24.50  ? 46  THR   B HG1  1 
ATOM   3231 H HG21 . THR   B 1 66  ? 20.844 -10.797 42.001  1.00 24.85  ? 46  THR   B HG21 1 
ATOM   3232 H HG22 . THR   B 1 66  ? 19.796 -11.266 40.917  1.00 24.85  ? 46  THR   B HG22 1 
ATOM   3233 H HG23 . THR   B 1 66  ? 20.912 -10.216 40.535  1.00 24.85  ? 46  THR   B HG23 1 
ATOM   3234 N N    . GLU   B 1 67  ? 16.587 -8.087  41.732  1.00 21.13  ? 47  GLU   B N    1 
ATOM   3235 C CA   . GLU   B 1 67  ? 15.668 -7.035  42.147  1.00 22.38  ? 47  GLU   B CA   1 
ATOM   3236 C C    . GLU   B 1 67  ? 16.395 -5.897  42.852  1.00 21.55  ? 47  GLU   B C    1 
ATOM   3237 O O    . GLU   B 1 67  ? 16.011 -4.730  42.710  1.00 23.05  ? 47  GLU   B O    1 
ATOM   3238 C CB   . GLU   B 1 67  ? 14.589 -7.612  43.074  1.00 26.19  ? 47  GLU   B CB   1 
ATOM   3239 C CG   . GLU   B 1 67  ? 13.551 -6.575  43.501  1.00 29.90  ? 47  GLU   B CG   1 
ATOM   3240 H H    . GLU   B 1 67  ? 16.408 -8.868  42.045  1.00 25.36  ? 47  GLU   B H    1 
ATOM   3241 H HA   . GLU   B 1 67  ? 15.240 -6.678  41.354  1.00 26.86  ? 47  GLU   B HA   1 
ATOM   3242 H HB2  . GLU   B 1 67  ? 14.125 -8.326  42.610  1.00 31.43  ? 47  GLU   B HB2  1 
ATOM   3243 H HB3  . GLU   B 1 67  ? 15.014 -7.958  43.875  1.00 31.43  ? 47  GLU   B HB3  1 
ATOM   3244 N N    . ASP   B 1 68  ? 17.426 -6.224  43.639  1.00 21.07  ? 48  ASP   B N    1 
ATOM   3245 C CA   . ASP   B 1 68  ? 18.227 -5.245  44.360  1.00 22.36  ? 48  ASP   B CA   1 
ATOM   3246 C C    . ASP   B 1 68  ? 19.535 -4.933  43.643  1.00 20.92  ? 48  ASP   B C    1 
ATOM   3247 O O    . ASP   B 1 68  ? 20.457 -4.390  44.256  1.00 21.66  ? 48  ASP   B O    1 
ATOM   3248 C CB   . ASP   B 1 68  ? 18.520 -5.738  45.781  1.00 27.12  ? 48  ASP   B CB   1 
ATOM   3249 C CG   . ASP   B 1 68  ? 19.299 -7.070  45.813  1.00 32.30  ? 48  ASP   B CG   1 
ATOM   3250 O OD1  . ASP   B 1 68  ? 19.563 -7.686  44.749  1.00 32.33  ? 48  ASP   B OD1  1 
ATOM   3251 O OD2  . ASP   B 1 68  ? 19.643 -7.510  46.929  1.00 37.32  ? 48  ASP   B OD2  1 
ATOM   3252 H H    . ASP   B 1 68  ? 17.683 -7.034  43.773  1.00 25.29  ? 48  ASP   B H    1 
ATOM   3253 H HA   . ASP   B 1 68  ? 17.715 -4.424  44.426  1.00 26.83  ? 48  ASP   B HA   1 
ATOM   3254 H HB2  . ASP   B 1 68  ? 19.051 -5.070  46.243  1.00 32.55  ? 48  ASP   B HB2  1 
ATOM   3255 H HB3  . ASP   B 1 68  ? 17.679 -5.872  46.247  1.00 32.55  ? 48  ASP   B HB3  1 
ATOM   3256 N N    . GLY   B 1 69  ? 19.624 -5.263  42.361  1.00 19.08  ? 49  GLY   B N    1 
ATOM   3257 C CA   . GLY   B 1 69  ? 20.855 -5.062  41.629  1.00 18.72  ? 49  GLY   B CA   1 
ATOM   3258 C C    . GLY   B 1 69  ? 21.186 -3.588  41.477  1.00 18.11  ? 49  GLY   B C    1 
ATOM   3259 O O    . GLY   B 1 69  ? 20.312 -2.721  41.504  1.00 19.03  ? 49  GLY   B O    1 
ATOM   3260 H H    . GLY   B 1 69  ? 18.985 -5.604  41.897  1.00 22.90  ? 49  GLY   B H    1 
ATOM   3261 H HA2  . GLY   B 1 69  ? 21.585 -5.495  42.099  1.00 22.46  ? 49  GLY   B HA2  1 
ATOM   3262 H HA3  . GLY   B 1 69  ? 20.774 -5.452  40.745  1.00 22.46  ? 49  GLY   B HA3  1 
ATOM   3263 N N    . VAL   B 1 70  ? 22.485 -3.304  41.332  1.00 16.52  ? 50  VAL   B N    1 
ATOM   3264 C CA   . VAL   B 1 70  ? 23.024 -1.955  41.229  1.00 16.86  ? 50  VAL   B CA   1 
ATOM   3265 C C    . VAL   B 1 70  ? 23.809 -1.848  39.930  1.00 15.84  ? 50  VAL   B C    1 
ATOM   3266 O O    . VAL   B 1 70  ? 24.547 -2.769  39.565  1.00 15.87  ? 50  VAL   B O    1 
ATOM   3267 C CB   . VAL   B 1 70  ? 23.928 -1.640  42.442  1.00 18.42  ? 50  VAL   B CB   1 
ATOM   3268 C CG1  . VAL   B 1 70  ? 24.565 -0.264  42.299  1.00 20.46  ? 50  VAL   B CG1  1 
ATOM   3269 C CG2  . VAL   B 1 70  ? 23.164 -1.765  43.748  1.00 20.98  ? 50  VAL   B CG2  1 
ATOM   3270 H H    . VAL   B 1 70  ? 23.096 -3.907  41.289  1.00 19.83  ? 50  VAL   B H    1 
ATOM   3271 H HA   . VAL   B 1 70  ? 22.301 -1.308  41.199  1.00 20.23  ? 50  VAL   B HA   1 
ATOM   3272 H HB   . VAL   B 1 70  ? 24.643 -2.295  42.467  1.00 22.11  ? 50  VAL   B HB   1 
ATOM   3273 H HG11 . VAL   B 1 70  ? 24.966 -0.012  43.146  1.00 24.56  ? 50  VAL   B HG11 1 
ATOM   3274 H HG12 . VAL   B 1 70  ? 25.245 -0.301  41.609  1.00 24.56  ? 50  VAL   B HG12 1 
ATOM   3275 H HG13 . VAL   B 1 70  ? 23.880 0.378   42.055  1.00 24.56  ? 50  VAL   B HG13 1 
ATOM   3276 H HG21 . VAL   B 1 70  ? 23.744 -1.500  44.479  1.00 25.18  ? 50  VAL   B HG21 1 
ATOM   3277 H HG22 . VAL   B 1 70  ? 22.387 -1.185  43.715  1.00 25.18  ? 50  VAL   B HG22 1 
ATOM   3278 H HG23 . VAL   B 1 70  ? 22.885 -2.686  43.863  1.00 25.18  ? 50  VAL   B HG23 1 
ATOM   3279 N N    . GLY   B 1 71  ? 23.684 -0.698  39.260  1.00 14.78  ? 51  GLY   B N    1 
ATOM   3280 C CA   . GLY   B 1 71  ? 24.485 -0.386  38.091  1.00 14.75  ? 51  GLY   B CA   1 
ATOM   3281 C C    . GLY   B 1 71  ? 24.928 1.061   38.144  1.00 16.27  ? 51  GLY   B C    1 
ATOM   3282 O O    . GLY   B 1 71  ? 24.416 1.844   38.929  1.00 19.28  ? 51  GLY   B O    1 
ATOM   3283 H H    . GLY   B 1 71  ? 23.131 -0.076  39.471  1.00 17.74  ? 51  GLY   B H    1 
ATOM   3284 H HA2  . GLY   B 1 71  ? 25.270 -0.956  38.065  1.00 17.70  ? 51  GLY   B HA2  1 
ATOM   3285 H HA3  . GLY   B 1 71  ? 23.965 -0.529  37.285  1.00 17.70  ? 51  GLY   B HA3  1 
ATOM   3286 N N    . GLY   B 1 72  ? 25.873 1.421   37.297  1.00 15.99  ? 52  GLY   B N    1 
ATOM   3287 C CA   . GLY   B 1 72  ? 26.182 2.838   37.138  1.00 16.50  ? 52  GLY   B CA   1 
ATOM   3288 C C    . GLY   B 1 72  ? 27.645 3.105   36.853  1.00 15.71  ? 52  GLY   B C    1 
ATOM   3289 O O    . GLY   B 1 72  ? 28.398 2.220   36.436  1.00 16.58  ? 52  GLY   B O    1 
ATOM   3290 H H    . GLY   B 1 72  ? 26.338 0.883   36.814  1.00 19.19  ? 52  GLY   B H    1 
ATOM   3291 H HA2  . GLY   B 1 72  ? 25.662 3.196   36.402  1.00 19.80  ? 52  GLY   B HA2  1 
ATOM   3292 H HA3  . GLY   B 1 72  ? 25.944 3.309   37.952  1.00 19.80  ? 52  GLY   B HA3  1 
ATOM   3293 N N    . LEU   B 1 73  ? 27.995 4.364   37.080  1.00 14.61  ? 53  LEU   B N    1 
ATOM   3294 C CA   . LEU   B 1 73  ? 29.246 4.946   36.614  1.00 14.80  ? 53  LEU   B CA   1 
ATOM   3295 C C    . LEU   B 1 73  ? 30.142 5.229   37.820  1.00 14.60  ? 53  LEU   B C    1 
ATOM   3296 O O    . LEU   B 1 73  ? 29.803 6.017   38.699  1.00 15.76  ? 53  LEU   B O    1 
ATOM   3297 C CB   . LEU   B 1 73  ? 28.936 6.229   35.835  1.00 15.29  ? 53  LEU   B CB   1 
ATOM   3298 C CG   . LEU   B 1 73  ? 30.184 7.001   35.366  1.00 15.97  ? 53  LEU   B CG   1 
ATOM   3299 C CD1  . LEU   B 1 73  ? 31.037 6.153   34.416  1.00 15.43  ? 53  LEU   B CD1  1 
ATOM   3300 C CD2  . LEU   B 1 73  ? 29.755 8.306   34.718  1.00 18.65  ? 53  LEU   B CD2  1 
ATOM   3301 H H    . LEU   B 1 73  ? 27.507 4.920   37.518  1.00 17.53  ? 53  LEU   B H    1 
ATOM   3302 H HA   . LEU   B 1 73  ? 29.726 4.330   36.040  1.00 17.77  ? 53  LEU   B HA   1 
ATOM   3303 H HB2  . LEU   B 1 73  ? 28.421 5.995   35.048  1.00 18.36  ? 53  LEU   B HB2  1 
ATOM   3304 H HB3  . LEU   B 1 73  ? 28.421 6.820   36.406  1.00 18.36  ? 53  LEU   B HB3  1 
ATOM   3305 H HG   . LEU   B 1 73  ? 30.746 7.208   36.129  1.00 19.17  ? 53  LEU   B HG   1 
ATOM   3306 H HD11 . LEU   B 1 73  ? 31.812 6.668   34.142  1.00 18.51  ? 53  LEU   B HD11 1 
ATOM   3307 H HD12 . LEU   B 1 73  ? 31.322 5.349   34.879  1.00 18.51  ? 53  LEU   B HD12 1 
ATOM   3308 H HD13 . LEU   B 1 73  ? 30.506 5.916   33.640  1.00 18.51  ? 53  LEU   B HD13 1 
ATOM   3309 H HD21 . LEU   B 1 73  ? 30.544 8.827   34.503  1.00 22.38  ? 53  LEU   B HD21 1 
ATOM   3310 H HD22 . LEU   B 1 73  ? 29.258 8.109   33.909  1.00 22.38  ? 53  LEU   B HD22 1 
ATOM   3311 H HD23 . LEU   B 1 73  ? 29.194 8.797   35.339  1.00 22.38  ? 53  LEU   B HD23 1 
ATOM   3312 N N    . TRP   B 1 74  ? 31.290 4.572   37.875  1.00 14.39  ? 54  TRP   B N    1 
ATOM   3313 C CA   . TRP   B 1 74  ? 32.148 4.641   39.047  1.00 16.24  ? 54  TRP   B CA   1 
ATOM   3314 C C    . TRP   B 1 74  ? 33.202 5.743   38.961  1.00 17.92  ? 54  TRP   B C    1 
ATOM   3315 O O    . TRP   B 1 74  ? 33.868 6.010   39.971  1.00 21.85  ? 54  TRP   B O    1 
ATOM   3316 C CB   . TRP   B 1 74  ? 32.800 3.272   39.334  1.00 16.05  ? 54  TRP   B CB   1 
ATOM   3317 C CG   . TRP   B 1 74  ? 32.166 2.584   40.505  1.00 16.03  ? 54  TRP   B CG   1 
ATOM   3318 C CD1  . TRP   B 1 74  ? 32.770 2.266   41.688  1.00 18.52  ? 54  TRP   B CD1  1 
ATOM   3319 C CD2  . TRP   B 1 74  ? 30.785 2.183   40.641  1.00 16.05  ? 54  TRP   B CD2  1 
ATOM   3320 N NE1  . TRP   B 1 74  ? 31.872 1.693   42.543  1.00 20.26  ? 54  TRP   B NE1  1 
ATOM   3321 C CE2  . TRP   B 1 74  ? 30.643 1.631   41.928  1.00 17.59  ? 54  TRP   B CE2  1 
ATOM   3322 C CE3  . TRP   B 1 74  ? 29.667 2.226   39.797  1.00 16.66  ? 54  TRP   B CE3  1 
ATOM   3323 C CZ2  . TRP   B 1 74  ? 29.417 1.126   42.397  1.00 18.54  ? 54  TRP   B CZ2  1 
ATOM   3324 C CZ3  . TRP   B 1 74  ? 28.452 1.730   40.273  1.00 17.27  ? 54  TRP   B CZ3  1 
ATOM   3325 C CH2  . TRP   B 1 74  ? 28.348 1.190   41.563  1.00 17.95  ? 54  TRP   B CH2  1 
ATOM   3326 H H    . TRP   B 1 74  ? 31.596 4.076   37.243  1.00 17.28  ? 54  TRP   B H    1 
ATOM   3327 H HA   . TRP   B 1 74  ? 31.597 4.843   39.819  1.00 19.49  ? 54  TRP   B HA   1 
ATOM   3328 H HB2  . TRP   B 1 74  ? 32.699 2.702   38.556  1.00 19.27  ? 54  TRP   B HB2  1 
ATOM   3329 H HB3  . TRP   B 1 74  ? 33.741 3.402   39.531  1.00 19.27  ? 54  TRP   B HB3  1 
ATOM   3330 H HD1  . TRP   B 1 74  ? 33.666 2.417   41.884  1.00 22.23  ? 54  TRP   B HD1  1 
ATOM   3331 H HE1  . TRP   B 1 74  ? 32.047 1.416   43.338  1.00 24.31  ? 54  TRP   B HE1  1 
ATOM   3332 H HE3  . TRP   B 1 74  ? 29.733 2.578   38.938  1.00 19.99  ? 54  TRP   B HE3  1 
ATOM   3333 H HZ2  . TRP   B 1 74  ? 29.342 0.761   43.249  1.00 22.26  ? 54  TRP   B HZ2  1 
ATOM   3334 H HZ3  . TRP   B 1 74  ? 27.701 1.758   39.726  1.00 20.73  ? 54  TRP   B HZ3  1 
ATOM   3335 H HH2  . TRP   B 1 74  ? 27.526 0.867   41.854  1.00 21.54  ? 54  TRP   B HH2  1 
ATOM   3336 N N    . THR   B 1 75  ? 33.372 6.364   37.802  1.00 15.85  ? 55  THR   B N    1 
ATOM   3337 C CA   . THR   B 1 75  ? 34.412 7.356   37.549  1.00 15.00  ? 55  THR   B CA   1 
ATOM   3338 C C    . THR   B 1 75  ? 33.735 8.655   37.101  1.00 15.18  ? 55  THR   B C    1 
ATOM   3339 O O    . THR   B 1 75  ? 33.247 8.746   35.970  1.00 16.63  ? 55  THR   B O    1 
ATOM   3340 C CB   . THR   B 1 75  ? 35.364 6.840   36.486  1.00 15.03  ? 55  THR   B CB   1 
ATOM   3341 O OG1  . THR   B 1 75  ? 34.616 6.359   35.385  1.00 15.47  ? 55  THR   B OG1  1 
ATOM   3342 C CG2  . THR   B 1 75  ? 36.214 5.704   36.984  1.00 15.77  ? 55  THR   B CG2  1 
ATOM   3343 H H    . THR   B 1 75  ? 32.875 6.223   37.114  1.00 19.03  ? 55  THR   B H    1 
ATOM   3344 H HA   . THR   B 1 75  ? 34.909 7.540   38.361  1.00 18.00  ? 55  THR   B HA   1 
ATOM   3345 H HB   . THR   B 1 75  ? 35.949 7.570   36.229  1.00 18.04  ? 55  THR   B HB   1 
ATOM   3346 H HG1  . THR   B 1 75  ? 34.126 6.970   35.082  1.00 18.56  ? 55  THR   B HG1  1 
ATOM   3347 H HG21 . THR   B 1 75  ? 36.835 5.426   36.292  1.00 18.92  ? 55  THR   B HG21 1 
ATOM   3348 H HG22 . THR   B 1 75  ? 36.718 5.984   37.764  1.00 18.92  ? 55  THR   B HG22 1 
ATOM   3349 H HG23 . THR   B 1 75  ? 35.653 4.951   37.225  1.00 18.92  ? 55  THR   B HG23 1 
ATOM   3350 N N    . THR   B 1 76  ? 33.713 9.658   37.977  1.00 16.62  ? 56  THR   B N    1 
ATOM   3351 C CA   . THR   B 1 76  ? 33.055 10.929  37.671  1.00 17.66  ? 56  THR   B CA   1 
ATOM   3352 C C    . THR   B 1 76  ? 33.948 12.075  38.135  1.00 17.81  ? 56  THR   B C    1 
ATOM   3353 O O    . THR   B 1 76  ? 34.949 11.877  38.834  1.00 18.43  ? 56  THR   B O    1 
ATOM   3354 C CB   . THR   B 1 76  ? 31.682 11.072  38.364  1.00 23.38  ? 56  THR   B CB   1 
ATOM   3355 O OG1  . THR   B 1 76  ? 31.892 11.271  39.758  1.00 28.10  ? 56  THR   B OG1  1 
ATOM   3356 C CG2  . THR   B 1 76  ? 30.822 9.841   38.178  1.00 26.27  ? 56  THR   B CG2  1 
ATOM   3357 H H    . THR   B 1 76  ? 34.073 9.627   38.757  1.00 19.95  ? 56  THR   B H    1 
ATOM   3358 H HA   . THR   B 1 76  ? 32.929 10.969  36.710  1.00 21.19  ? 56  THR   B HA   1 
ATOM   3359 H HB   . THR   B 1 76  ? 31.210 11.823  37.971  1.00 28.06  ? 56  THR   B HB   1 
ATOM   3360 H HG1  . THR   B 1 76  ? 32.317 10.622  40.080  1.00 33.72  ? 56  THR   B HG1  1 
ATOM   3361 H HG21 . THR   B 1 76  ? 29.988 9.944   38.662  1.00 31.53  ? 56  THR   B HG21 1 
ATOM   3362 H HG22 . THR   B 1 76  ? 30.627 9.712   37.237  1.00 31.53  ? 56  THR   B HG22 1 
ATOM   3363 H HG23 . THR   B 1 76  ? 31.287 9.059   38.514  1.00 31.53  ? 56  THR   B HG23 1 
ATOM   3364 N N    . ASP   B 1 77  ? 33.534 13.297  37.802  1.00 17.40  ? 57  ASP   B N    1 
ATOM   3365 C CA   . ASP   B 1 77  ? 34.315 14.470  38.187  1.00 20.00  ? 57  ASP   B CA   1 
ATOM   3366 C C    . ASP   B 1 77  ? 34.421 14.632  39.696  1.00 22.59  ? 57  ASP   B C    1 
ATOM   3367 O O    . ASP   B 1 77  ? 35.449 15.109  40.187  1.00 24.88  ? 57  ASP   B O    1 
ATOM   3368 C CB   . ASP   B 1 77  ? 33.780 15.747  37.536  1.00 21.61  ? 57  ASP   B CB   1 
ATOM   3369 C CG   . ASP   B 1 77  ? 32.429 16.129  38.008  1.00 26.67  ? 57  ASP   B CG   1 
ATOM   3370 O OD1  . ASP   B 1 77  ? 32.261 16.796  39.039  1.00 33.39  ? 57  ASP   B OD1  1 
ATOM   3371 O OD2  . ASP   B 1 77  ? 31.522 15.771  37.315  1.00 30.03  ? 57  ASP   B OD2  1 
ATOM   3372 H H    . ASP   B 1 77  ? 32.817 13.471  37.361  1.00 20.88  ? 57  ASP   B H    1 
ATOM   3373 H HA   . ASP   B 1 77  ? 35.213 14.339  37.844  1.00 24.00  ? 57  ASP   B HA   1 
ATOM   3374 H HB2  . ASP   B 1 77  ? 34.383 16.479  37.739  1.00 25.94  ? 57  ASP   B HB2  1 
ATOM   3375 H HB3  . ASP   B 1 77  ? 33.732 15.614  36.576  1.00 25.94  ? 57  ASP   B HB3  1 
ATOM   3376 N N    . SER   B 1 78  ? 33.385 14.245  40.447  1.00 22.95  ? 58  SER   B N    1 
ATOM   3377 C CA   . SER   B 1 78  ? 33.378 14.444  41.884  1.00 26.42  ? 58  SER   B CA   1 
ATOM   3378 C C    . SER   B 1 78  ? 34.205 13.413  42.625  1.00 29.02  ? 58  SER   B C    1 
ATOM   3379 O O    . SER   B 1 78  ? 34.569 13.646  43.780  1.00 32.39  ? 58  SER   B O    1 
ATOM   3380 C CB   . SER   B 1 78  ? 31.942 14.364  42.402  1.00 30.82  ? 58  SER   B CB   1 
ATOM   3381 O OG   . SER   B 1 78  ? 31.474 13.055  42.255  1.00 33.63  ? 58  SER   B OG   1 
ATOM   3382 H H    . SER   B 1 78  ? 32.677 13.866  40.141  1.00 27.54  ? 58  SER   B H    1 
ATOM   3383 H HA   . SER   B 1 78  ? 33.742 15.323  42.075  1.00 31.70  ? 58  SER   B HA   1 
ATOM   3384 H HB2  . SER   B 1 78  ? 31.923 14.611  43.340  1.00 36.98  ? 58  SER   B HB2  1 
ATOM   3385 H HB3  . SER   B 1 78  ? 31.381 14.967  41.889  1.00 36.98  ? 58  SER   B HB3  1 
ATOM   3386 H HG   . SER   B 1 78  ? 31.472 12.840  41.443  1.00 40.36  ? 58  SER   B HG   1 
ATOM   3387 N N    . GLY   B 1 79  ? 34.488 12.271  42.006  1.00 27.83  ? 59  GLY   B N    1 
ATOM   3388 C CA   . GLY   B 1 79  ? 35.179 11.195  42.682  1.00 28.19  ? 59  GLY   B CA   1 
ATOM   3389 C C    . GLY   B 1 79  ? 34.288 10.185  43.376  1.00 29.85  ? 59  GLY   B C    1 
ATOM   3390 O O    . GLY   B 1 79  ? 34.811 9.199   43.916  1.00 34.16  ? 59  GLY   B O    1 
ATOM   3391 H H    . GLY   B 1 79  ? 34.287 12.100  41.188  1.00 33.40  ? 59  GLY   B H    1 
ATOM   3392 H HA2  . GLY   B 1 79  ? 35.714 10.715  42.030  1.00 33.83  ? 59  GLY   B HA2  1 
ATOM   3393 H HA3  . GLY   B 1 79  ? 35.766 11.578  43.352  1.00 33.83  ? 59  GLY   B HA3  1 
ATOM   3394 N N    . GLN   B 1 80  ? 32.949 10.397  43.387  1.00 27.72  ? 60  GLN   B N    1 
ATOM   3395 C CA   . GLN   B 1 80  ? 32.009 9.438   43.945  1.00 28.56  ? 60  GLN   B CA   1 
ATOM   3396 C C    . GLN   B 1 80  ? 31.245 8.740   42.830  1.00 25.62  ? 60  GLN   B C    1 
ATOM   3397 O O    . GLN   B 1 80  ? 30.916 9.365   41.815  1.00 26.70  ? 60  GLN   B O    1 
ATOM   3398 C CB   . GLN   B 1 80  ? 31.009 10.134  44.889  1.00 34.15  ? 60  GLN   B CB   1 
ATOM   3399 C CG   . GLN   B 1 80  ? 31.626 10.511  46.221  1.00 42.72  ? 60  GLN   B CG   1 
ATOM   3400 C CD   . GLN   B 1 80  ? 31.959 9.299   47.077  1.00 49.68  ? 60  GLN   B CD   1 
ATOM   3401 O OE1  . GLN   B 1 80  ? 33.129 8.983   47.295  1.00 52.10  ? 60  GLN   B OE1  1 
ATOM   3402 N NE2  . GLN   B 1 80  ? 30.928 8.619   47.571  1.00 52.48  ? 60  GLN   B NE2  1 
ATOM   3403 H H    . GLN   B 1 80  ? 32.572 11.102  43.069  1.00 33.26  ? 60  GLN   B H    1 
ATOM   3404 H HA   . GLN   B 1 80  ? 32.489 8.769   44.457  1.00 34.28  ? 60  GLN   B HA   1 
ATOM   3405 H HB2  . GLN   B 1 80  ? 30.688 10.945  44.466  1.00 40.98  ? 60  GLN   B HB2  1 
ATOM   3406 H HB3  . GLN   B 1 80  ? 30.267 9.533   45.061  1.00 40.98  ? 60  GLN   B HB3  1 
ATOM   3407 H HG2  . GLN   B 1 80  ? 32.447 11.002  46.061  1.00 51.27  ? 60  GLN   B HG2  1 
ATOM   3408 H HG3  . GLN   B 1 80  ? 31.000 11.064  46.714  1.00 51.27  ? 60  GLN   B HG3  1 
ATOM   3409 H HE21 . GLN   B 1 80  ? 30.124 8.872   47.400  1.00 62.98  ? 60  GLN   B HE21 1 
ATOM   3410 H HE22 . GLN   B 1 80  ? 31.065 7.925   48.061  1.00 62.98  ? 60  GLN   B HE22 1 
ATOM   3411 N N    . PRO   B 1 81  ? 30.961 7.450   42.961  1.00 23.90  ? 61  PRO   B N    1 
ATOM   3412 C CA   . PRO   B 1 81  ? 30.177 6.789   41.918  1.00 21.49  ? 61  PRO   B CA   1 
ATOM   3413 C C    . PRO   B 1 81  ? 28.770 7.349   41.852  1.00 21.81  ? 61  PRO   B C    1 
ATOM   3414 O O    . PRO   B 1 81  ? 28.239 7.848   42.840  1.00 25.24  ? 61  PRO   B O    1 
ATOM   3415 C CB   . PRO   B 1 81  ? 30.138 5.327   42.384  1.00 24.02  ? 61  PRO   B CB   1 
ATOM   3416 C CG   . PRO   B 1 81  ? 31.324 5.163   43.265  1.00 27.81  ? 61  PRO   B CG   1 
ATOM   3417 C CD   . PRO   B 1 81  ? 31.430 6.497   43.982  1.00 26.95  ? 61  PRO   B CD   1 
ATOM   3418 H HA   . PRO   B 1 81  ? 30.615 6.863   41.056  1.00 25.79  ? 61  PRO   B HA   1 
ATOM   3419 H HB2  . PRO   B 1 81  ? 29.317 5.160   42.873  1.00 28.83  ? 61  PRO   B HB2  1 
ATOM   3420 H HB3  . PRO   B 1 81  ? 30.193 4.736   41.616  1.00 28.83  ? 61  PRO   B HB3  1 
ATOM   3421 H HG2  . PRO   B 1 81  ? 31.178 4.438   43.893  1.00 33.38  ? 61  PRO   B HG2  1 
ATOM   3422 H HG3  . PRO   B 1 81  ? 32.116 4.987   42.733  1.00 33.38  ? 61  PRO   B HG3  1 
ATOM   3423 H HD2  . PRO   B 1 81  ? 30.858 6.518   44.765  1.00 32.35  ? 61  PRO   B HD2  1 
ATOM   3424 H HD3  . PRO   B 1 81  ? 32.347 6.684   44.236  1.00 32.35  ? 61  PRO   B HD3  1 
ATOM   3425 N N    . ILE   B 1 82  ? 28.177 7.245   40.671  1.00 19.09  ? 62  ILE   B N    1 
ATOM   3426 C CA   . ILE   B 1 82  ? 26.757 7.489   40.449  1.00 19.93  ? 62  ILE   B CA   1 
ATOM   3427 C C    . ILE   B 1 82  ? 26.125 6.111   40.294  1.00 17.75  ? 62  ILE   B C    1 
ATOM   3428 O O    . ILE   B 1 82  ? 26.207 5.473   39.227  1.00 18.88  ? 62  ILE   B O    1 
ATOM   3429 C CB   . ILE   B 1 82  ? 26.523 8.382   39.236  1.00 24.65  ? 62  ILE   B CB   1 
ATOM   3430 C CG1  . ILE   B 1 82  ? 27.219 9.738   39.500  1.00 28.25  ? 62  ILE   B CG1  1 
ATOM   3431 C CG2  . ILE   B 1 82  ? 24.993 8.584   39.011  1.00 26.06  ? 62  ILE   B CG2  1 
ATOM   3432 C CD1  . ILE   B 1 82  ? 27.401 10.617  38.309  1.00 32.54  ? 62  ILE   B CD1  1 
ATOM   3433 H H    . ILE   B 1 82  ? 28.594 7.026   39.952  1.00 22.91  ? 62  ILE   B H    1 
ATOM   3434 H HA   . ILE   B 1 82  ? 26.361 7.930   41.216  1.00 23.91  ? 62  ILE   B HA   1 
ATOM   3435 H HB   . ILE   B 1 82  ? 26.891 7.972   38.437  1.00 29.59  ? 62  ILE   B HB   1 
ATOM   3436 H HG12 . ILE   B 1 82  ? 26.688 10.233  40.144  1.00 33.90  ? 62  ILE   B HG12 1 
ATOM   3437 H HG13 . ILE   B 1 82  ? 28.101 9.561   39.864  1.00 33.90  ? 62  ILE   B HG13 1 
ATOM   3438 H HG21 . ILE   B 1 82  ? 24.860 9.246   38.315  1.00 31.27  ? 62  ILE   B HG21 1 
ATOM   3439 H HG22 . ILE   B 1 82  ? 24.598 7.739   38.743  1.00 31.27  ? 62  ILE   B HG22 1 
ATOM   3440 H HG23 . ILE   B 1 82  ? 24.590 8.889   39.839  1.00 31.27  ? 62  ILE   B HG23 1 
ATOM   3441 H HD11 . ILE   B 1 82  ? 27.814 11.449  38.590  1.00 39.05  ? 62  ILE   B HD11 1 
ATOM   3442 H HD12 . ILE   B 1 82  ? 27.970 10.166  37.667  1.00 39.05  ? 62  ILE   B HD12 1 
ATOM   3443 H HD13 . ILE   B 1 82  ? 26.533 10.797  37.914  1.00 39.05  ? 62  ILE   B HD13 1 
ATOM   3444 N N    . ALA   B 1 83  ? 25.581 5.606   41.392  1.00 18.83  ? 63  ALA   B N    1 
ATOM   3445 C CA   . ALA   B 1 83  ? 25.037 4.263   41.447  1.00 19.64  ? 63  ALA   B CA   1 
ATOM   3446 C C    . ALA   B 1 83  ? 23.526 4.339   41.370  1.00 20.73  ? 63  ALA   B C    1 
ATOM   3447 O O    . ALA   B 1 83  ? 22.901 5.136   42.070  1.00 24.95  ? 63  ALA   B O    1 
ATOM   3448 C CB   . ALA   B 1 83  ? 25.450 3.596   42.754  1.00 22.18  ? 63  ALA   B CB   1 
ATOM   3449 H H    . ALA   B 1 83  ? 25.516 6.034   42.134  1.00 22.59  ? 63  ALA   B H    1 
ATOM   3450 H HA   . ALA   B 1 83  ? 25.361 3.735   40.701  1.00 23.57  ? 63  ALA   B HA   1 
ATOM   3451 H HB1  . ALA   B 1 83  ? 25.090 2.696   42.777  1.00 26.61  ? 63  ALA   B HB1  1 
ATOM   3452 H HB2  . ALA   B 1 83  ? 26.419 3.566   42.800  1.00 26.61  ? 63  ALA   B HB2  1 
ATOM   3453 H HB3  . ALA   B 1 83  ? 25.099 4.112   43.497  1.00 26.61  ? 63  ALA   B HB3  1 
ATOM   3454 N N    . ILE   B 1 84  ? 22.958 3.499   40.531  1.00 17.51  ? 64  ILE   B N    1 
ATOM   3455 C CA   . ILE   B 1 84  ? 21.520 3.385   40.355  1.00 18.12  ? 64  ILE   B CA   1 
ATOM   3456 C C    . ILE   B 1 84  ? 21.104 2.085   41.038  1.00 19.16  ? 64  ILE   B C    1 
ATOM   3457 O O    . ILE   B 1 84  ? 21.535 0.996   40.643  1.00 19.20  ? 64  ILE   B O    1 
ATOM   3458 C CB   . ILE   B 1 84  ? 21.152 3.407   38.868  1.00 20.57  ? 64  ILE   B CB   1 
ATOM   3459 C CG1  . ILE   B 1 84  ? 21.763 4.643   38.184  1.00 25.47  ? 64  ILE   B CG1  1 
ATOM   3460 C CG2  . ILE   B 1 84  ? 19.639 3.374   38.702  1.00 21.69  ? 64  ILE   B CG2  1 
ATOM   3461 C CD1  . ILE   B 1 84  ? 22.018 4.466   36.732  1.00 30.43  ? 64  ILE   B CD1  1 
ATOM   3462 H H    . ILE   B 1 84  ? 23.402 2.959   40.029  1.00 21.01  ? 64  ILE   B H    1 
ATOM   3463 H HA   . ILE   B 1 84  ? 21.051 4.118   40.784  1.00 21.75  ? 64  ILE   B HA   1 
ATOM   3464 H HB   . ILE   B 1 84  ? 21.520 2.617   38.440  1.00 24.69  ? 64  ILE   B HB   1 
ATOM   3465 H HG12 . ILE   B 1 84  ? 21.152 5.389   38.287  1.00 30.56  ? 64  ILE   B HG12 1 
ATOM   3466 H HG13 . ILE   B 1 84  ? 22.611 4.847   38.609  1.00 30.56  ? 64  ILE   B HG13 1 
ATOM   3467 H HG21 . ILE   B 1 84  ? 19.421 3.492   37.765  1.00 26.03  ? 64  ILE   B HG21 1 
ATOM   3468 H HG22 . ILE   B 1 84  ? 19.306 2.518   39.014  1.00 26.03  ? 64  ILE   B HG22 1 
ATOM   3469 H HG23 . ILE   B 1 84  ? 19.249 4.092   39.225  1.00 26.03  ? 64  ILE   B HG23 1 
ATOM   3470 H HD11 . ILE   B 1 84  ? 22.205 5.331   36.336  1.00 36.52  ? 64  ILE   B HD11 1 
ATOM   3471 H HD12 . ILE   B 1 84  ? 22.781 3.877   36.615  1.00 36.52  ? 64  ILE   B HD12 1 
ATOM   3472 H HD13 . ILE   B 1 84  ? 21.232 4.075   36.319  1.00 36.52  ? 64  ILE   B HD13 1 
ATOM   3473 N N    . ARG   B 1 85  ? 20.263 2.192   42.057  1.00 21.95  ? 65  ARG   B N    1 
ATOM   3474 C CA   . ARG   B 1 85  ? 20.061 1.117   43.013  1.00 21.80  ? 65  ARG   B CA   1 
ATOM   3475 C C    . ARG   B 1 85  ? 18.680 0.509   42.846  1.00 21.73  ? 65  ARG   B C    1 
ATOM   3476 O O    . ARG   B 1 85  ? 17.653 1.142   43.150  1.00 23.46  ? 65  ARG   B O    1 
ATOM   3477 C CB   . ARG   B 1 85  ? 20.294 1.602   44.438  1.00 23.85  ? 65  ARG   B CB   1 
ATOM   3478 C CG   . ARG   B 1 85  ? 21.724 2.102   44.658  1.00 27.42  ? 65  ARG   B CG   1 
ATOM   3479 C CD   . ARG   B 1 85  ? 21.958 2.589   46.088  1.00 30.88  ? 65  ARG   B CD   1 
ATOM   3480 N NE   . ARG   B 1 85  ? 23.319 3.097   46.240  1.00 35.16  ? 65  ARG   B NE   1 
ATOM   3481 C CZ   . ARG   B 1 85  ? 24.396 2.333   46.385  1.00 39.91  ? 65  ARG   B CZ   1 
ATOM   3482 N NH1  . ARG   B 1 85  ? 24.305 1.013   46.452  1.00 40.93  ? 65  ARG   B NH1  1 
ATOM   3483 N NH2  . ARG   B 1 85  ? 25.598 2.906   46.456  1.00 43.18  ? 65  ARG   B NH2  1 
ATOM   3484 H H    . ARG   B 1 85  ? 19.789 2.892   42.216  1.00 26.35  ? 65  ARG   B H    1 
ATOM   3485 H HA   . ARG   B 1 85  ? 20.700 0.414   42.815  1.00 26.17  ? 65  ARG   B HA   1 
ATOM   3486 H HB2  . ARG   B 1 85  ? 19.686 2.333   44.628  1.00 28.62  ? 65  ARG   B HB2  1 
ATOM   3487 H HB3  . ARG   B 1 85  ? 20.134 0.868   45.053  1.00 28.62  ? 65  ARG   B HB3  1 
ATOM   3488 H HG2  . ARG   B 1 85  ? 22.345 1.378   44.481  1.00 32.91  ? 65  ARG   B HG2  1 
ATOM   3489 H HG3  . ARG   B 1 85  ? 21.897 2.843   44.055  1.00 32.91  ? 65  ARG   B HG3  1 
ATOM   3490 H HD2  . ARG   B 1 85  ? 21.336 3.304   46.293  1.00 37.06  ? 65  ARG   B HD2  1 
ATOM   3491 H HD3  . ARG   B 1 85  ? 21.833 1.852   46.706  1.00 37.06  ? 65  ARG   B HD3  1 
ATOM   3492 H HE   . ARG   B 1 85  ? 23.431 3.950   46.235  1.00 42.19  ? 65  ARG   B HE   1 
ATOM   3493 H HH11 . ARG   B 1 85  ? 23.535 0.632   46.401  1.00 49.12  ? 65  ARG   B HH11 1 
ATOM   3494 H HH12 . ARG   B 1 85  ? 25.014 0.537   46.546  1.00 49.12  ? 65  ARG   B HH12 1 
ATOM   3495 H HH21 . ARG   B 1 85  ? 25.670 3.762   46.408  1.00 51.82  ? 65  ARG   B HH21 1 
ATOM   3496 H HH22 . ARG   B 1 85  ? 26.302 2.420   46.550  1.00 51.82  ? 65  ARG   B HH22 1 
ATOM   3497 N N    . GLY   B 1 86  ? 18.668 -0.725  42.383  1.00 21.34  ? 66  GLY   B N    1 
ATOM   3498 C CA   . GLY   B 1 86  ? 17.439 -1.469  42.314  1.00 22.67  ? 66  GLY   B CA   1 
ATOM   3499 C C    . GLY   B 1 86  ? 17.008 -1.635  40.880  1.00 21.27  ? 66  GLY   B C    1 
ATOM   3500 O O    . GLY   B 1 86  ? 17.153 -0.731  40.041  1.00 21.46  ? 66  GLY   B O    1 
ATOM   3501 H H    . GLY   B 1 86  ? 19.362 -1.150  42.104  1.00 25.61  ? 66  GLY   B H    1 
ATOM   3502 H HA2  . GLY   B 1 86  ? 17.563 -2.347  42.708  1.00 27.21  ? 66  GLY   B HA2  1 
ATOM   3503 H HA3  . GLY   B 1 86  ? 16.743 -1.000  42.799  1.00 27.21  ? 66  GLY   B HA3  1 
ATOM   3504 N N    A ARG   B 1 87  ? 16.478 -2.819  40.582  0.42 22.20  ? 67  ARG   B N    1 
ATOM   3505 N N    B ARG   B 1 87  ? 16.455 -2.813  40.591  0.58 22.58  ? 67  ARG   B N    1 
ATOM   3506 C CA   A ARG   B 1 87  ? 16.063 -3.112  39.223  0.42 22.51  ? 67  ARG   B CA   1 
ATOM   3507 C CA   B ARG   B 1 87  ? 16.058 -3.131  39.232  0.58 22.49  ? 67  ARG   B CA   1 
ATOM   3508 C C    A ARG   B 1 87  ? 15.077 -2.076  38.720  0.42 21.47  ? 67  ARG   B C    1 
ATOM   3509 C C    B ARG   B 1 87  ? 15.048 -2.126  38.709  0.58 22.42  ? 67  ARG   B C    1 
ATOM   3510 O O    A ARG   B 1 87  ? 15.156 -1.654  37.562  0.42 20.60  ? 67  ARG   B O    1 
ATOM   3511 O O    B ARG   B 1 87  ? 15.094 -1.759  37.531  0.58 23.36  ? 67  ARG   B O    1 
ATOM   3512 C CB   A ARG   B 1 87  ? 15.445 -4.509  39.170  0.42 23.58  ? 67  ARG   B CB   1 
ATOM   3513 C CB   B ARG   B 1 87  ? 15.500 -4.561  39.175  0.58 21.32  ? 67  ARG   B CB   1 
ATOM   3514 C CG   A ARG   B 1 87  ? 14.889 -4.889  37.819  0.42 25.07  ? 67  ARG   B CG   1 
ATOM   3515 C CG   B ARG   B 1 87  ? 15.004 -5.007  37.812  0.58 21.91  ? 67  ARG   B CG   1 
ATOM   3516 C CD   A ARG   B 1 87  ? 14.030 -6.111  37.921  0.42 26.81  ? 67  ARG   B CD   1 
ATOM   3517 C CD   B ARG   B 1 87  ? 14.699 -6.485  37.787  0.58 24.09  ? 67  ARG   B CD   1 
ATOM   3518 N NE   A ARG   B 1 87  ? 14.778 -7.338  37.717  0.42 28.97  ? 67  ARG   B NE   1 
ATOM   3519 N NE   B ARG   B 1 87  ? 13.668 -6.817  38.756  0.58 28.71  ? 67  ARG   B NE   1 
ATOM   3520 C CZ   A ARG   B 1 87  ? 14.327 -8.547  38.021  0.42 31.15  ? 67  ARG   B CZ   1 
ATOM   3521 C CZ   B ARG   B 1 87  ? 13.523 -8.008  39.321  0.58 34.36  ? 67  ARG   B CZ   1 
ATOM   3522 N NH1  A ARG   B 1 87  ? 13.146 -8.725  38.604  0.42 33.03  ? 67  ARG   B NH1  1 
ATOM   3523 N NH1  B ARG   B 1 87  ? 14.350 -9.009  39.053  0.58 36.78  ? 67  ARG   B NH1  1 
ATOM   3524 N NH2  A ARG   B 1 87  ? 15.069 -9.605  37.726  0.42 32.21  ? 67  ARG   B NH2  1 
ATOM   3525 N NH2  B ARG   B 1 87  ? 12.554 -8.184  40.206  0.58 36.04  ? 67  ARG   B NH2  1 
ATOM   3526 H H    A ARG   B 1 87  ? 16.352 -3.458  41.143  0.42 26.65  ? 67  ARG   B H    1 
ATOM   3527 H H    B ARG   B 1 87  ? 16.302 -3.437  41.163  0.58 27.10  ? 67  ARG   B H    1 
ATOM   3528 H HA   A ARG   B 1 87  ? 16.839 -3.097  38.640  0.42 27.01  ? 67  ARG   B HA   1 
ATOM   3529 H HA   B ARG   B 1 87  ? 16.834 -3.093  38.652  0.58 26.99  ? 67  ARG   B HA   1 
ATOM   3530 H HB2  A ARG   B 1 87  ? 16.126 -5.159  39.402  0.42 28.30  ? 67  ARG   B HB2  1 
ATOM   3531 H HB2  B ARG   B 1 87  ? 16.202 -5.174  39.443  0.58 25.58  ? 67  ARG   B HB2  1 
ATOM   3532 H HB3  A ARG   B 1 87  ? 14.716 -4.549  39.810  0.42 28.30  ? 67  ARG   B HB3  1 
ATOM   3533 H HB3  B ARG   B 1 87  ? 14.753 -4.623  39.791  0.58 25.58  ? 67  ARG   B HB3  1 
ATOM   3534 H HG2  A ARG   B 1 87  ? 14.349 -4.161  37.474  0.42 30.08  ? 67  ARG   B HG2  1 
ATOM   3535 H HG2  B ARG   B 1 87  ? 14.191 -4.525  37.593  0.58 26.30  ? 67  ARG   B HG2  1 
ATOM   3536 H HG3  A ARG   B 1 87  ? 15.620 -5.077  37.209  0.42 30.08  ? 67  ARG   B HG3  1 
ATOM   3537 H HG3  B ARG   B 1 87  ? 15.687 -4.826  37.147  0.58 26.30  ? 67  ARG   B HG3  1 
ATOM   3538 H HD2  A ARG   B 1 87  ? 13.632 -6.146  38.805  0.42 32.18  ? 67  ARG   B HD2  1 
ATOM   3539 H HD2  B ARG   B 1 87  ? 14.385 -6.736  36.905  0.58 28.91  ? 67  ARG   B HD2  1 
ATOM   3540 H HD3  A ARG   B 1 87  ? 13.335 -6.067  37.246  0.42 32.18  ? 67  ARG   B HD3  1 
ATOM   3541 H HD3  B ARG   B 1 87  ? 15.501 -6.985  38.008  0.58 28.91  ? 67  ARG   B HD3  1 
ATOM   3542 H HE   A ARG   B 1 87  ? 15.565 -7.277  37.377  0.42 34.77  ? 67  ARG   B HE   1 
ATOM   3543 H HE   B ARG   B 1 87  ? 13.113 -6.198  38.978  0.58 34.46  ? 67  ARG   B HE   1 
ATOM   3544 H HH11 A ARG   B 1 87  ? 12.654 -8.046  38.793  0.42 39.64  ? 67  ARG   B HH11 1 
ATOM   3545 H HH11 B ARG   B 1 87  ? 14.999 -8.894  38.500  0.58 44.14  ? 67  ARG   B HH11 1 
ATOM   3546 H HH12 A ARG   B 1 87  ? 12.875 -9.519  38.791  0.42 39.64  ? 67  ARG   B HH12 1 
ATOM   3547 H HH12 B ARG   B 1 87  ? 14.237 -9.773  39.431  0.58 44.14  ? 67  ARG   B HH12 1 
ATOM   3548 H HH21 A ARG   B 1 87  ? 15.832 -9.502  37.343  0.42 38.65  ? 67  ARG   B HH21 1 
ATOM   3549 H HH21 B ARG   B 1 87  ? 12.031 -7.531  40.406  0.58 43.25  ? 67  ARG   B HH21 1 
ATOM   3550 H HH22 A ARG   B 1 87  ? 14.788 -10.395 37.918  0.42 38.65  ? 67  ARG   B HH22 1 
ATOM   3551 H HH22 B ARG   B 1 87  ? 12.448 -8.950  40.581  0.58 43.25  ? 67  ARG   B HH22 1 
ATOM   3552 N N    . GLU   B 1 88  ? 14.130 -1.659  39.573  1.00 24.61  ? 68  GLU   B N    1 
ATOM   3553 C CA   . GLU   B 1 88  ? 13.117 -0.702  39.142  1.00 26.70  ? 68  GLU   B CA   1 
ATOM   3554 C C    . GLU   B 1 88  ? 13.736 0.654   38.800  1.00 25.13  ? 68  GLU   B C    1 
ATOM   3555 O O    . GLU   B 1 88  ? 13.414 1.251   37.767  1.00 25.48  ? 68  GLU   B O    1 
ATOM   3556 C CB   . GLU   B 1 88  ? 12.025 -0.585  40.213  1.00 30.36  ? 68  GLU   B CB   1 
ATOM   3557 H H    A GLU   B 1 88  ? 14.058 -1.914  40.391  0.42 29.54  ? 68  GLU   B H    1 
ATOM   3558 H H    B GLU   B 1 88  ? 14.079 -1.882  40.402  0.58 29.54  ? 68  GLU   B H    1 
ATOM   3559 H HA   . GLU   B 1 88  ? 12.692 -1.025  38.332  1.00 32.05  ? 68  GLU   B HA   1 
ATOM   3560 N N    . LYS   B 1 89  ? 14.641 1.146   39.650  1.00 24.51  ? 69  LYS   B N    1 
ATOM   3561 C CA   . LYS   B 1 89  ? 15.325 2.406   39.354  1.00 23.95  ? 69  LYS   B CA   1 
ATOM   3562 C C    . LYS   B 1 89  ? 16.210 2.296   38.113  1.00 21.23  ? 69  LYS   B C    1 
ATOM   3563 O O    . LYS   B 1 89  ? 16.326 3.251   37.342  1.00 21.67  ? 69  LYS   B O    1 
ATOM   3564 C CB   . LYS   B 1 89  ? 16.164 2.839   40.556  1.00 29.57  ? 69  LYS   B CB   1 
ATOM   3565 C CG   . LYS   B 1 89  ? 15.358 3.371   41.742  1.00 38.98  ? 69  LYS   B CG   1 
ATOM   3566 C CD   . LYS   B 1 89  ? 15.164 4.873   41.644  1.00 46.33  ? 69  LYS   B CD   1 
ATOM   3567 C CE   . LYS   B 1 89  ? 14.316 5.415   42.793  1.00 50.99  ? 69  LYS   B CE   1 
ATOM   3568 N NZ   . LYS   B 1 89  ? 14.938 5.103   44.118  1.00 53.50  ? 69  LYS   B NZ   1 
ATOM   3569 H H    . LYS   B 1 89  ? 14.872 0.777   40.391  1.00 29.42  ? 69  LYS   B H    1 
ATOM   3570 H HA   . LYS   B 1 89  ? 14.656 3.087   39.185  1.00 28.74  ? 69  LYS   B HA   1 
ATOM   3571 H HB2  . LYS   B 1 89  ? 16.672 2.074   40.868  1.00 35.49  ? 69  LYS   B HB2  1 
ATOM   3572 H HB3  . LYS   B 1 89  ? 16.766 3.545   40.273  1.00 35.49  ? 69  LYS   B HB3  1 
ATOM   3573 H HG2  . LYS   B 1 89  ? 14.484 2.949   41.753  1.00 46.78  ? 69  LYS   B HG2  1 
ATOM   3574 H HG3  . LYS   B 1 89  ? 15.830 3.176   42.566  1.00 46.78  ? 69  LYS   B HG3  1 
ATOM   3575 H HD2  . LYS   B 1 89  ? 16.030 5.309   41.673  1.00 55.59  ? 69  LYS   B HD2  1 
ATOM   3576 H HD3  . LYS   B 1 89  ? 14.715 5.083   40.810  1.00 55.59  ? 69  LYS   B HD3  1 
ATOM   3577 H HE2  . LYS   B 1 89  ? 14.239 6.379   42.710  1.00 61.19  ? 69  LYS   B HE2  1 
ATOM   3578 H HE3  . LYS   B 1 89  ? 13.436 5.009   42.764  1.00 61.19  ? 69  LYS   B HE3  1 
ATOM   3579 H HZ1  . LYS   B 1 89  ? 14.456 5.463   44.773  1.00 64.20  ? 69  LYS   B HZ1  1 
ATOM   3580 H HZ2  . LYS   B 1 89  ? 14.974 4.221   44.237  1.00 64.20  ? 69  LYS   B HZ2  1 
ATOM   3581 H HZ3  . LYS   B 1 89  ? 15.764 5.432   44.152  1.00 64.20  ? 69  LYS   B HZ3  1 
ATOM   3582 N N    . LEU   B 1 90  ? 16.820 1.134   37.895  1.00 18.97  ? 70  LEU   B N    1 
ATOM   3583 C CA   . LEU   B 1 90  ? 17.582 0.924   36.668  1.00 18.64  ? 70  LEU   B CA   1 
ATOM   3584 C C    . LEU   B 1 90  ? 16.699 1.055   35.435  1.00 18.86  ? 70  LEU   B C    1 
ATOM   3585 O O    . LEU   B 1 90  ? 17.084 1.709   34.453  1.00 20.06  ? 70  LEU   B O    1 
ATOM   3586 C CB   . LEU   B 1 90  ? 18.318 -0.419  36.710  1.00 19.32  ? 70  LEU   B CB   1 
ATOM   3587 C CG   . LEU   B 1 90  ? 19.540 -0.482  37.607  1.00 18.95  ? 70  LEU   B CG   1 
ATOM   3588 C CD1  . LEU   B 1 90  ? 19.902 -1.918  37.942  1.00 19.70  ? 70  LEU   B CD1  1 
ATOM   3589 C CD2  . LEU   B 1 90  ? 20.737 0.199   36.912  1.00 18.83  ? 70  LEU   B CD2  1 
ATOM   3590 H H    . LEU   B 1 90  ? 16.810 0.463   38.432  1.00 22.77  ? 70  LEU   B H    1 
ATOM   3591 H HA   . LEU   B 1 90  ? 18.265 1.610   36.603  1.00 22.37  ? 70  LEU   B HA   1 
ATOM   3592 H HB2  . LEU   B 1 90  ? 17.697 -1.094  37.023  1.00 23.19  ? 70  LEU   B HB2  1 
ATOM   3593 H HB3  . LEU   B 1 90  ? 18.612 -0.630  35.810  1.00 23.19  ? 70  LEU   B HB3  1 
ATOM   3594 H HG   . LEU   B 1 90  ? 19.339 -0.020  38.436  1.00 22.75  ? 70  LEU   B HG   1 
ATOM   3595 H HD11 . LEU   B 1 90  ? 20.706 -1.923  38.485  1.00 23.64  ? 70  LEU   B HD11 1 
ATOM   3596 H HD12 . LEU   B 1 90  ? 19.169 -2.322  38.433  1.00 23.64  ? 70  LEU   B HD12 1 
ATOM   3597 H HD13 . LEU   B 1 90  ? 20.057 -2.406  37.118  1.00 23.64  ? 70  LEU   B HD13 1 
ATOM   3598 H HD21 . LEU   B 1 90  ? 21.512 0.142   37.491  1.00 22.60  ? 70  LEU   B HD21 1 
ATOM   3599 H HD22 . LEU   B 1 90  ? 20.915 -0.255  36.074  1.00 22.60  ? 70  LEU   B HD22 1 
ATOM   3600 H HD23 . LEU   B 1 90  ? 20.517 1.129   36.744  1.00 22.60  ? 70  LEU   B HD23 1 
ATOM   3601 N N    . GLY   B 1 91  ? 15.488 0.474   35.472  1.00 20.03  ? 71  GLY   B N    1 
ATOM   3602 C CA   . GLY   B 1 91  ? 14.594 0.615   34.339  1.00 21.59  ? 71  GLY   B CA   1 
ATOM   3603 C C    . GLY   B 1 91  ? 14.156 2.057   34.140  1.00 21.70  ? 71  GLY   B C    1 
ATOM   3604 O O    . GLY   B 1 91  ? 14.053 2.546   33.007  1.00 24.31  ? 71  GLY   B O    1 
ATOM   3605 H H    . GLY   B 1 91  ? 15.179 0.010   36.126  1.00 24.04  ? 71  GLY   B H    1 
ATOM   3606 H HA2  . GLY   B 1 91  ? 15.043 0.316   33.533  1.00 25.91  ? 71  GLY   B HA2  1 
ATOM   3607 H HA3  . GLY   B 1 91  ? 13.804 0.070   34.481  1.00 25.91  ? 71  GLY   B HA3  1 
ATOM   3608 N N    . GLU   B 1 92  ? 13.957 2.781   35.231  1.00 22.97  ? 72  GLU   B N    1 
ATOM   3609 C CA   . GLU   B 1 92  ? 13.563 4.177   35.097  1.00 25.88  ? 72  GLU   B CA   1 
ATOM   3610 C C    . GLU   B 1 92  ? 14.702 5.004   34.517  1.00 25.24  ? 72  GLU   B C    1 
ATOM   3611 O O    . GLU   B 1 92  ? 14.478 5.886   33.678  1.00 28.41  ? 72  GLU   B O    1 
ATOM   3612 C CB   . GLU   B 1 92  ? 13.127 4.714   36.456  1.00 31.27  ? 72  GLU   B CB   1 
ATOM   3613 C CG   . GLU   B 1 92  ? 11.821 4.101   36.950  1.00 38.37  ? 72  GLU   B CG   1 
ATOM   3614 C CD   . GLU   B 1 92  ? 11.549 4.422   38.402  1.00 45.69  ? 72  GLU   B CD   1 
ATOM   3615 O OE1  . GLU   B 1 92  ? 12.259 5.297   38.954  1.00 49.38  ? 72  GLU   B OE1  1 
ATOM   3616 O OE2  . GLU   B 1 92  ? 10.630 3.800   38.986  1.00 48.24  ? 72  GLU   B OE2  1 
ATOM   3617 H H    . GLU   B 1 92  ? 14.040 2.498   36.039  1.00 27.56  ? 72  GLU   B H    1 
ATOM   3618 H HA   . GLU   B 1 92  ? 12.807 4.249   34.493  1.00 31.06  ? 72  GLU   B HA   1 
ATOM   3619 H HB2  . GLU   B 1 92  ? 13.816 4.515   37.108  1.00 37.52  ? 72  GLU   B HB2  1 
ATOM   3620 H HB3  . GLU   B 1 92  ? 13.000 5.673   36.389  1.00 37.52  ? 72  GLU   B HB3  1 
ATOM   3621 H HG2  . GLU   B 1 92  ? 11.086 4.450   36.421  1.00 46.04  ? 72  GLU   B HG2  1 
ATOM   3622 H HG3  . GLU   B 1 92  ? 11.867 3.137   36.858  1.00 46.04  ? 72  GLU   B HG3  1 
ATOM   3623 N N    . HIS   B 1 93  ? 15.942 4.684   34.901  1.00 22.98  ? 73  HIS   B N    1 
ATOM   3624 C CA   A HIS   B 1 93  ? 17.111 5.405   34.391  0.53 22.71  ? 73  HIS   B CA   1 
ATOM   3625 C CA   B HIS   B 1 93  ? 17.045 5.461   34.381  0.47 23.38  ? 73  HIS   B CA   1 
ATOM   3626 C C    . HIS   B 1 93  ? 17.286 5.193   32.898  1.00 23.26  ? 73  HIS   B C    1 
ATOM   3627 O O    . HIS   B 1 93  ? 17.750 6.091   32.191  1.00 24.57  ? 73  HIS   B O    1 
ATOM   3628 C CB   A HIS   B 1 93  ? 18.391 4.928   35.097  0.53 22.96  ? 73  HIS   B CB   1 
ATOM   3629 C CB   B HIS   B 1 93  ? 18.288 5.221   35.215  0.47 24.50  ? 73  HIS   B CB   1 
ATOM   3630 C CG   A HIS   B 1 93  ? 19.674 5.526   34.550  0.53 22.52  ? 73  HIS   B CG   1 
ATOM   3631 C CG   B HIS   B 1 93  ? 19.183 6.414   35.274  0.47 23.83  ? 73  HIS   B CG   1 
ATOM   3632 N ND1  A HIS   B 1 93  ? 20.106 6.792   34.884  0.53 23.14  ? 73  HIS   B ND1  1 
ATOM   3633 N ND1  B HIS   B 1 93  ? 20.336 6.510   34.526  0.47 25.39  ? 73  HIS   B ND1  1 
ATOM   3634 C CD2  A HIS   B 1 93  ? 20.632 5.012   33.729  0.53 23.52  ? 73  HIS   B CD2  1 
ATOM   3635 C CD2  B HIS   B 1 93  ? 19.079 7.574   35.961  0.47 25.22  ? 73  HIS   B CD2  1 
ATOM   3636 C CE1  A HIS   B 1 93  ? 21.258 7.041   34.284  0.53 22.48  ? 73  HIS   B CE1  1 
ATOM   3637 C CE1  B HIS   B 1 93  ? 20.919 7.669   34.771  0.47 26.87  ? 73  HIS   B CE1  1 
ATOM   3638 N NE2  A HIS   B 1 93  ? 21.603 5.977   33.582  0.53 23.54  ? 73  HIS   B NE2  1 
ATOM   3639 N NE2  B HIS   B 1 93  ? 20.176 8.333   35.638  0.47 26.80  ? 73  HIS   B NE2  1 
ATOM   3640 H H    A HIS   B 1 93  ? 16.133 4.054   35.455  0.53 27.57  ? 73  HIS   B H    1 
ATOM   3641 H H    B HIS   B 1 93  ? 16.152 4.047   35.439  0.47 27.57  ? 73  HIS   B H    1 
ATOM   3642 H HA   A HIS   B 1 93  ? 16.976 6.347   34.575  0.53 27.25  ? 73  HIS   B HA   1 
ATOM   3643 H HA   B HIS   B 1 93  ? 16.834 6.405   34.456  0.47 28.05  ? 73  HIS   B HA   1 
ATOM   3644 H HB2  A HIS   B 1 93  ? 18.333 5.167   36.036  0.53 27.56  ? 73  HIS   B HB2  1 
ATOM   3645 H HB2  B HIS   B 1 93  ? 18.022 5.001   36.121  0.47 29.41  ? 73  HIS   B HB2  1 
ATOM   3646 H HB3  A HIS   B 1 93  ? 18.454 3.964   35.004  0.53 27.56  ? 73  HIS   B HB3  1 
ATOM   3647 H HB3  B HIS   B 1 93  ? 18.790 4.487   34.829  0.47 29.41  ? 73  HIS   B HB3  1 
ATOM   3648 H HD1  B HIS   B 1 93  ? 20.630 5.910   33.985  0.47 30.47  ? 73  HIS   B HD1  1 
ATOM   3649 H HD2  A HIS   B 1 93  ? 20.630 4.166   33.341  0.53 28.23  ? 73  HIS   B HD2  1 
ATOM   3650 H HD2  B HIS   B 1 93  ? 18.393 7.813   36.542  0.47 30.27  ? 73  HIS   B HD2  1 
ATOM   3651 H HE1  A HIS   B 1 93  ? 21.744 7.831   34.347  0.53 26.97  ? 73  HIS   B HE1  1 
ATOM   3652 H HE1  B HIS   B 1 93  ? 21.716 7.967   34.397  0.47 32.25  ? 73  HIS   B HE1  1 
ATOM   3653 H HE2  A HIS   B 1 93  ? 22.317 5.900   33.109  0.53 28.25  ? 73  HIS   B HE2  1 
ATOM   3654 N N    . ALA   B 1 94  ? 16.966 3.984   32.407  1.00 20.87  ? 74  ALA   B N    1 
ATOM   3655 C CA   . ALA   B 1 94  ? 17.119 3.711   30.985  1.00 21.01  ? 74  ALA   B CA   1 
ATOM   3656 C C    . ALA   B 1 94  ? 16.260 4.638   30.134  1.00 21.34  ? 74  ALA   B C    1 
ATOM   3657 O O    . ALA   B 1 94  ? 16.642 4.973   29.010  1.00 22.04  ? 74  ALA   B O    1 
ATOM   3658 C CB   . ALA   B 1 94  ? 16.789 2.262   30.693  1.00 22.07  ? 74  ALA   B CB   1 
ATOM   3659 H H    . ALA   B 1 94  ? 16.667 3.325   32.871  1.00 25.05  ? 74  ALA   B H    1 
ATOM   3660 H HA   . ALA   B 1 94  ? 18.046 3.861   30.739  1.00 25.22  ? 74  ALA   B HA   1 
ATOM   3661 H HB1  . ALA   B 1 94  ? 16.881 2.102   29.741  1.00 26.48  ? 74  ALA   B HB1  1 
ATOM   3662 H HB2  . ALA   B 1 94  ? 17.401 1.693   31.185  1.00 26.48  ? 74  ALA   B HB2  1 
ATOM   3663 H HB3  . ALA   B 1 94  ? 15.877 2.084   30.972  1.00 26.48  ? 74  ALA   B HB3  1 
ATOM   3664 N N    . VAL   B 1 95  ? 15.096 5.051   30.644  1.00 22.65  ? 75  VAL   B N    1 
ATOM   3665 C CA   . VAL   B 1 95  ? 14.276 6.017   29.928  1.00 24.87  ? 75  VAL   B CA   1 
ATOM   3666 C C    . VAL   B 1 95  ? 15.071 7.292   29.670  1.00 25.39  ? 75  VAL   B C    1 
ATOM   3667 O O    . VAL   B 1 95  ? 15.034 7.864   28.573  1.00 27.72  ? 75  VAL   B O    1 
ATOM   3668 C CB   . VAL   B 1 95  ? 12.989 6.298   30.726  1.00 28.90  ? 75  VAL   B CB   1 
ATOM   3669 C CG1  . VAL   B 1 95  ? 12.185 7.410   30.059  1.00 31.68  ? 75  VAL   B CG1  1 
ATOM   3670 C CG2  . VAL   B 1 95  ? 12.153 5.040   30.864  1.00 30.80  ? 75  VAL   B CG2  1 
ATOM   3671 H H    . VAL   B 1 95  ? 14.767 4.789   31.394  1.00 27.18  ? 75  VAL   B H    1 
ATOM   3672 H HA   . VAL   B 1 95  ? 14.024 5.646   29.067  1.00 29.85  ? 75  VAL   B HA   1 
ATOM   3673 H HB   . VAL   B 1 95  ? 13.234 6.590   31.618  1.00 34.68  ? 75  VAL   B HB   1 
ATOM   3674 H HG11 . VAL   B 1 95  ? 11.294 7.428   30.442  1.00 38.02  ? 75  VAL   B HG11 1 
ATOM   3675 H HG12 . VAL   B 1 95  ? 12.629 8.258   30.216  1.00 38.02  ? 75  VAL   B HG12 1 
ATOM   3676 H HG13 . VAL   B 1 95  ? 12.133 7.235   29.107  1.00 38.02  ? 75  VAL   B HG13 1 
ATOM   3677 H HG21 . VAL   B 1 95  ? 11.319 5.263   31.307  1.00 36.96  ? 75  VAL   B HG21 1 
ATOM   3678 H HG22 . VAL   B 1 95  ? 11.973 4.681   29.981  1.00 36.96  ? 75  VAL   B HG22 1 
ATOM   3679 H HG23 . VAL   B 1 95  ? 12.644 4.390   31.391  1.00 36.96  ? 75  VAL   B HG23 1 
ATOM   3680 N N    . TRP   B 1 96  ? 15.787 7.769   30.687  1.00 24.53  ? 76  TRP   B N    1 
ATOM   3681 C CA   . TRP   B 1 96  ? 16.608 8.963   30.525  1.00 24.21  ? 76  TRP   B CA   1 
ATOM   3682 C C    . TRP   B 1 96  ? 17.780 8.706   29.585  1.00 22.60  ? 76  TRP   B C    1 
ATOM   3683 O O    . TRP   B 1 96  ? 18.050 9.501   28.676  1.00 23.27  ? 76  TRP   B O    1 
ATOM   3684 C CB   . TRP   B 1 96  ? 17.130 9.423   31.888  1.00 25.57  ? 76  TRP   B CB   1 
ATOM   3685 C CG   . TRP   B 1 96  ? 18.035 10.556  31.766  1.00 27.64  ? 76  TRP   B CG   1 
ATOM   3686 C CD1  . TRP   B 1 96  ? 17.681 11.878  31.724  1.00 30.00  ? 76  TRP   B CD1  1 
ATOM   3687 C CD2  . TRP   B 1 96  ? 19.457 10.514  31.640  1.00 28.42  ? 76  TRP   B CD2  1 
ATOM   3688 N NE1  . TRP   B 1 96  ? 18.794 12.658  31.564  1.00 31.89  ? 76  TRP   B NE1  1 
ATOM   3689 C CE2  . TRP   B 1 96  ? 19.901 11.852  31.506  1.00 29.88  ? 76  TRP   B CE2  1 
ATOM   3690 C CE3  . TRP   B 1 96  ? 20.398 9.491   31.614  1.00 28.88  ? 76  TRP   B CE3  1 
ATOM   3691 C CZ2  . TRP   B 1 96  ? 21.246 12.179  31.365  1.00 31.01  ? 76  TRP   B CZ2  1 
ATOM   3692 C CZ3  . TRP   B 1 96  ? 21.723 9.815   31.455  1.00 28.66  ? 76  TRP   B CZ3  1 
ATOM   3693 C CH2  . TRP   B 1 96  ? 22.138 11.151  31.327  1.00 29.09  ? 76  TRP   B CH2  1 
ATOM   3694 H H    . TRP   B 1 96  ? 15.813 7.423   31.474  1.00 29.43  ? 76  TRP   B H    1 
ATOM   3695 H HA   . TRP   B 1 96  ? 16.057 9.665   30.145  1.00 29.06  ? 76  TRP   B HA   1 
ATOM   3696 H HB2  . TRP   B 1 96  ? 16.382 9.690   32.444  1.00 30.69  ? 76  TRP   B HB2  1 
ATOM   3697 H HB3  . TRP   B 1 96  ? 17.612 8.693   32.309  1.00 30.69  ? 76  TRP   B HB3  1 
ATOM   3698 H HD1  . TRP   B 1 96  ? 16.811 12.199  31.794  1.00 36.00  ? 76  TRP   B HD1  1 
ATOM   3699 H HE1  . TRP   B 1 96  ? 18.799 13.517  31.509  1.00 38.27  ? 76  TRP   B HE1  1 
ATOM   3700 H HE3  . TRP   B 1 96  ? 20.135 8.603   31.702  1.00 34.66  ? 76  TRP   B HE3  1 
ATOM   3701 H HZ2  . TRP   B 1 96  ? 21.525 13.064  31.299  1.00 37.22  ? 76  TRP   B HZ2  1 
ATOM   3702 H HZ3  . TRP   B 1 96  ? 22.359 9.136   31.432  1.00 34.40  ? 76  TRP   B HZ3  1 
ATOM   3703 H HH2  . TRP   B 1 96  ? 23.042 11.338  31.214  1.00 34.90  ? 76  TRP   B HH2  1 
ATOM   3704 N N    . SER   B 1 97  ? 18.502 7.603   29.792  0.88 20.53  ? 77  SER   B N    1 
ATOM   3705 C CA   . SER   B 1 97  ? 19.704 7.385   29.006  0.88 21.85  ? 77  SER   B CA   1 
ATOM   3706 C C    . SER   B 1 97  ? 19.385 7.159   27.536  0.88 21.07  ? 77  SER   B C    1 
ATOM   3707 O O    . SER   B 1 97  ? 20.172 7.533   26.679  0.88 20.91  ? 77  SER   B O    1 
ATOM   3708 C CB   . SER   B 1 97  ? 20.562 6.309   29.638  0.88 25.71  ? 77  SER   B CB   1 
ATOM   3709 O OG   . SER   B 1 97  ? 19.867 5.152   29.794  0.88 28.19  ? 77  SER   B OG   1 
ATOM   3710 H H    . SER   B 1 97  ? 18.319 6.988   30.364  0.88 24.64  ? 77  SER   B H    1 
ATOM   3711 H HA   . SER   B 1 97  ? 20.260 8.180   29.021  0.88 26.23  ? 77  SER   B HA   1 
ATOM   3712 H HB2  . SER   B 1 97  ? 21.327 6.141   29.066  0.88 30.85  ? 77  SER   B HB2  1 
ATOM   3713 H HB3  . SER   B 1 97  ? 20.860 6.616   30.509  0.88 30.85  ? 77  SER   B HB3  1 
ATOM   3714 H HG   . SER   B 1 97  ? 20.366 4.558   30.117  0.88 33.83  ? 77  SER   B HG   1 
ATOM   3715 N N    A LEU   B 1 98  ? 18.226 6.590   27.214  0.47 23.68  ? 78  LEU   B N    1 
ATOM   3716 N N    B LEU   B 1 98  ? 18.227 6.580   27.228  0.53 22.50  ? 78  LEU   B N    1 
ATOM   3717 C CA   A LEU   B 1 98  ? 17.873 6.456   25.807  0.47 25.72  ? 78  LEU   B CA   1 
ATOM   3718 C CA   B LEU   B 1 98  ? 17.835 6.450   25.832  0.53 23.18  ? 78  LEU   B CA   1 
ATOM   3719 C C    A LEU   B 1 98  ? 17.622 7.803   25.136  0.47 26.46  ? 78  LEU   B C    1 
ATOM   3720 C C    B LEU   B 1 98  ? 17.657 7.813   25.170  0.53 24.72  ? 78  LEU   B C    1 
ATOM   3721 O O    A LEU   B 1 98  ? 17.706 7.894   23.907  0.47 28.28  ? 78  LEU   B O    1 
ATOM   3722 O O    B LEU   B 1 98  ? 17.944 7.963   23.978  0.53 27.23  ? 78  LEU   B O    1 
ATOM   3723 C CB   A LEU   B 1 98  ? 16.669 5.531   25.637  0.47 28.99  ? 78  LEU   B CB   1 
ATOM   3724 C CB   B LEU   B 1 98  ? 16.561 5.612   25.726  0.53 25.30  ? 78  LEU   B CB   1 
ATOM   3725 C CG   A LEU   B 1 98  ? 17.037 4.156   25.085  0.47 30.95  ? 78  LEU   B CG   1 
ATOM   3726 C CG   B LEU   B 1 98  ? 16.164 5.147   24.325  0.53 24.67  ? 78  LEU   B CG   1 
ATOM   3727 C CD1  A LEU   B 1 98  ? 15.871 3.228   25.191  0.47 32.31  ? 78  LEU   B CD1  1 
ATOM   3728 C CD1  B LEU   B 1 98  ? 17.246 4.261   23.672  0.53 26.68  ? 78  LEU   B CD1  1 
ATOM   3729 C CD2  A LEU   B 1 98  ? 17.520 4.257   23.622  0.47 30.88  ? 78  LEU   B CD2  1 
ATOM   3730 C CD2  B LEU   B 1 98  ? 14.826 4.433   24.385  0.53 23.52  ? 78  LEU   B CD2  1 
ATOM   3731 H H    A LEU   B 1 98  ? 17.647 6.284   27.773  0.43 28.41  ? 78  LEU   B H    1 
ATOM   3732 H H    B LEU   B 1 98  ? 17.664 6.263   27.795  0.53 27.01  ? 78  LEU   B H    1 
ATOM   3733 H HA   A LEU   B 1 98  ? 18.616 6.039   25.344  0.47 30.87  ? 78  LEU   B HA   1 
ATOM   3734 H HA   B LEU   B 1 98  ? 18.533 5.982   25.346  0.53 27.82  ? 78  LEU   B HA   1 
ATOM   3735 H HB2  A LEU   B 1 98  ? 16.247 5.404   26.501  0.47 34.79  ? 78  LEU   B HB2  1 
ATOM   3736 H HB2  B LEU   B 1 98  ? 16.679 4.815   26.267  0.53 30.37  ? 78  LEU   B HB2  1 
ATOM   3737 H HB3  A LEU   B 1 98  ? 16.043 5.943   25.020  0.47 34.79  ? 78  LEU   B HB3  1 
ATOM   3738 H HB3  B LEU   B 1 98  ? 15.824 6.140   26.070  0.53 30.37  ? 78  LEU   B HB3  1 
ATOM   3739 H HG   A LEU   B 1 98  ? 17.767 3.792   25.610  0.47 37.15  ? 78  LEU   B HG   1 
ATOM   3740 H HG   B LEU   B 1 98  ? 16.078 5.926   23.752  0.53 29.61  ? 78  LEU   B HG   1 
ATOM   3741 H HD11 A LEU   B 1 98  ? 15.987 2.501   24.560  0.47 38.78  ? 78  LEU   B HD11 1 
ATOM   3742 H HD11 B LEU   B 1 98  ? 16.900 3.900   22.841  0.53 32.01  ? 78  LEU   B HD11 1 
ATOM   3743 H HD12 A LEU   B 1 98  ? 15.826 2.878   26.095  0.47 38.78  ? 78  LEU   B HD12 1 
ATOM   3744 H HD12 B LEU   B 1 98  ? 18.033 4.800   23.496  0.53 32.01  ? 78  LEU   B HD12 1 
ATOM   3745 H HD13 A LEU   B 1 98  ? 15.058 3.717   24.986  0.47 38.78  ? 78  LEU   B HD13 1 
ATOM   3746 H HD13 B LEU   B 1 98  ? 17.470 3.537   24.278  0.53 32.01  ? 78  LEU   B HD13 1 
ATOM   3747 H HD21 A LEU   B 1 98  ? 17.665 3.364   23.274  0.47 37.05  ? 78  LEU   B HD21 1 
ATOM   3748 H HD21 B LEU   B 1 98  ? 14.584 4.140   23.493  0.53 28.23  ? 78  LEU   B HD21 1 
ATOM   3749 H HD22 A LEU   B 1 98  ? 16.842 4.711   23.097  0.47 37.05  ? 78  LEU   B HD22 1 
ATOM   3750 H HD22 B LEU   B 1 98  ? 14.904 3.667   24.975  0.53 28.23  ? 78  LEU   B HD22 1 
ATOM   3751 H HD23 A LEU   B 1 98  ? 18.349 4.761   23.597  0.47 37.05  ? 78  LEU   B HD23 1 
ATOM   3752 H HD23 B LEU   B 1 98  ? 14.156 5.046   24.725  0.53 28.23  ? 78  LEU   B HD23 1 
ATOM   3753 N N    A GLN   B 1 99  ? 17.332 8.850   25.905  0.47 25.02  ? 79  GLN   B N    1 
ATOM   3754 N N    B GLN   B 1 99  ? 17.217 8.823   25.921  0.53 22.82  ? 79  GLN   B N    1 
ATOM   3755 C CA   A GLN   B 1 99  ? 17.192 10.190  25.343  0.47 26.02  ? 79  GLN   B CA   1 
ATOM   3756 C CA   B GLN   B 1 99  ? 17.083 10.161  25.347  0.53 25.01  ? 79  GLN   B CA   1 
ATOM   3757 C C    A GLN   B 1 99  ? 18.524 10.941  25.300  0.47 24.82  ? 79  GLN   B C    1 
ATOM   3758 C C    B GLN   B 1 99  ? 18.437 10.847  25.171  0.53 24.60  ? 79  GLN   B C    1 
ATOM   3759 O O    A GLN   B 1 99  ? 18.807 11.662  24.331  0.47 25.55  ? 79  GLN   B O    1 
ATOM   3760 O O    B GLN   B 1 99  ? 18.696 11.479  24.134  0.53 25.70  ? 79  GLN   B O    1 
ATOM   3761 C CB   A GLN   B 1 99  ? 16.154 10.974  26.149  0.47 29.94  ? 79  GLN   B CB   1 
ATOM   3762 C CB   B GLN   B 1 99  ? 16.166 11.021  26.225  0.53 30.23  ? 79  GLN   B CB   1 
ATOM   3763 C CG   A GLN   B 1 99  ? 14.784 10.301  26.162  0.47 34.46  ? 79  GLN   B CG   1 
ATOM   3764 C CG   B GLN   B 1 99  ? 16.103 12.481  25.799  0.53 36.65  ? 79  GLN   B CG   1 
ATOM   3765 C CD   A GLN   B 1 99  ? 13.826 10.952  27.138  0.47 37.94  ? 79  GLN   B CD   1 
ATOM   3766 C CD   B GLN   B 1 99  ? 14.970 13.260  26.460  0.53 42.70  ? 79  GLN   B CD   1 
ATOM   3767 O OE1  A GLN   B 1 99  ? 13.428 10.345  28.134  0.47 37.94  ? 79  GLN   B OE1  1 
ATOM   3768 O OE1  B GLN   B 1 99  ? 14.380 12.819  27.449  0.53 45.97  ? 79  GLN   B OE1  1 
ATOM   3769 N NE2  A GLN   B 1 99  ? 13.441 12.196  26.852  0.47 39.52  ? 79  GLN   B NE2  1 
ATOM   3770 N NE2  B GLN   B 1 99  ? 14.663 14.428  25.908  0.53 43.22  ? 79  GLN   B NE2  1 
ATOM   3771 H H    A GLN   B 1 99  ? 17.213 8.810   26.755  0.47 30.03  ? 79  GLN   B H    1 
ATOM   3772 H H    B GLN   B 1 99  ? 16.994 8.762   26.749  0.53 27.38  ? 79  GLN   B H    1 
ATOM   3773 H HA   A GLN   B 1 99  ? 16.871 10.127  24.430  0.47 31.23  ? 79  GLN   B HA   1 
ATOM   3774 H HA   B GLN   B 1 99  ? 16.675 10.078  24.471  0.53 30.02  ? 79  GLN   B HA   1 
ATOM   3775 H HB2  A GLN   B 1 99  ? 16.460 11.051  27.067  0.47 35.93  ? 79  GLN   B HB2  1 
ATOM   3776 H HB2  B GLN   B 1 99  ? 15.267 10.661  26.184  0.53 36.28  ? 79  GLN   B HB2  1 
ATOM   3777 H HB3  A GLN   B 1 99  ? 16.052 11.856  25.759  0.47 35.93  ? 79  GLN   B HB3  1 
ATOM   3778 H HB3  B GLN   B 1 99  ? 16.493 10.993  27.138  0.53 36.28  ? 79  GLN   B HB3  1 
ATOM   3779 H HG2  A GLN   B 1 99  ? 14.395 10.357  25.276  0.47 41.36  ? 79  GLN   B HG2  1 
ATOM   3780 H HG2  B GLN   B 1 99  ? 16.938 12.913  26.037  0.53 43.98  ? 79  GLN   B HG2  1 
ATOM   3781 H HG3  A GLN   B 1 99  ? 14.890 9.372   26.420  0.47 41.36  ? 79  GLN   B HG3  1 
ATOM   3782 H HG3  B GLN   B 1 99  ? 15.970 12.521  24.839  0.53 43.98  ? 79  GLN   B HG3  1 
ATOM   3783 H HE21 A GLN   B 1 99  ? 13.736 12.586  26.145  0.47 47.43  ? 79  GLN   B HE21 1 
ATOM   3784 H HE21 B GLN   B 1 99  ? 15.095 14.705  25.218  0.53 51.86  ? 79  GLN   B HE21 1 
ATOM   3785 H HE22 A GLN   B 1 99  ? 12.897 12.609  27.375  0.47 47.43  ? 79  GLN   B HE22 1 
ATOM   3786 H HE22 B GLN   B 1 99  ? 14.032 14.909  26.241  0.53 51.86  ? 79  GLN   B HE22 1 
ATOM   3787 N N    A CYS   B 1 100 ? 19.353 10.774  26.327  0.47 22.82  ? 80  CYS   B N    1 
ATOM   3788 N N    B CYS   B 1 100 ? 19.299 10.749  26.171  0.53 22.28  ? 80  CYS   B N    1 
ATOM   3789 C CA   A CYS   B 1 100 ? 20.635 11.464  26.376  0.47 21.48  ? 80  CYS   B CA   1 
ATOM   3790 C CA   B CYS   B 1 100 ? 20.530 11.524  26.205  0.53 21.47  ? 80  CYS   B CA   1 
ATOM   3791 C C    A CYS   B 1 100 ? 21.681 10.827  25.465  0.47 20.15  ? 80  CYS   B C    1 
ATOM   3792 C C    B CYS   B 1 100 ? 21.720 10.818  25.544  0.53 21.04  ? 80  CYS   B C    1 
ATOM   3793 O O    A CYS   B 1 100 ? 22.539 11.531  24.907  0.47 19.28  ? 80  CYS   B O    1 
ATOM   3794 O O    B CYS   B 1 100 ? 22.716 11.481  25.218  0.53 22.30  ? 80  CYS   B O    1 
ATOM   3795 C CB   A CYS   B 1 100 ? 21.148 11.474  27.813  0.47 22.06  ? 80  CYS   B CB   1 
ATOM   3796 C CB   B CYS   B 1 100 ? 20.799 11.953  27.659  0.53 22.52  ? 80  CYS   B CB   1 
ATOM   3797 S SG   A CYS   B 1 100 ? 22.685 12.374  27.997  0.47 21.88  ? 80  CYS   B SG   1 
ATOM   3798 S SG   B CYS   B 1 100 ? 19.480 13.064  28.341  0.53 23.10  ? 80  CYS   B SG   1 
ATOM   3799 H H    A CYS   B 1 100 ? 19.196 10.269  27.005  0.47 27.39  ? 80  CYS   B H    1 
ATOM   3800 H H    B CYS   B 1 100 ? 19.193 10.234  26.851  0.53 26.74  ? 80  CYS   B H    1 
ATOM   3801 H HA   A CYS   B 1 100 ? 20.506 12.378  26.080  0.47 25.78  ? 80  CYS   B HA   1 
ATOM   3802 H HA   B CYS   B 1 100 ? 20.438 12.344  25.696  0.53 25.77  ? 80  CYS   B HA   1 
ATOM   3803 H HB2  A CYS   B 1 100 ? 20.485 11.895  28.382  0.47 26.48  ? 80  CYS   B HB2  1 
ATOM   3804 H HB2  B CYS   B 1 100 ? 20.841 11.161  28.218  0.53 27.03  ? 80  CYS   B HB2  1 
ATOM   3805 H HB3  A CYS   B 1 100 ? 21.300 10.560  28.100  0.47 26.48  ? 80  CYS   B HB3  1 
ATOM   3806 H HB3  B CYS   B 1 100 ? 21.642 12.430  27.696  0.53 27.03  ? 80  CYS   B HB3  1 
ATOM   3807 H HG   A CYS   B 1 100 ? 23.531 11.843  27.331  0.47 26.26  ? 80  CYS   B HG   1 
ATOM   3808 H HG   B CYS   B 1 100 ? 19.869 13.548  29.368  0.53 27.72  ? 80  CYS   B HG   1 
ATOM   3809 N N    . PHE   B 1 101 ? 21.617 9.516   25.294  1.00 19.89  ? 81  PHE   B N    1 
ATOM   3810 C CA   . PHE   B 1 101 ? 22.591 8.749   24.510  1.00 18.31  ? 81  PHE   B CA   1 
ATOM   3811 C C    . PHE   B 1 101 ? 21.773 7.925   23.515  1.00 19.44  ? 81  PHE   B C    1 
ATOM   3812 O O    . PHE   B 1 101 ? 21.642 6.705   23.652  1.00 19.73  ? 81  PHE   B O    1 
ATOM   3813 C CB   . PHE   B 1 101 ? 23.450 7.859   25.406  1.00 18.42  ? 81  PHE   B CB   1 
ATOM   3814 C CG   . PHE   B 1 101 ? 24.273 8.621   26.396  1.00 19.37  ? 81  PHE   B CG   1 
ATOM   3815 C CD1  . PHE   B 1 101 ? 25.479 9.184   26.026  1.00 19.81  ? 81  PHE   B CD1  1 
ATOM   3816 C CD2  . PHE   B 1 101 ? 23.862 8.783   27.700  1.00 23.15  ? 81  PHE   B CD2  1 
ATOM   3817 C CE1  . PHE   B 1 101 ? 26.245 9.894   26.932  1.00 21.61  ? 81  PHE   B CE1  1 
ATOM   3818 C CE2  . PHE   B 1 101 ? 24.618 9.516   28.594  1.00 25.62  ? 81  PHE   B CE2  1 
ATOM   3819 C CZ   . PHE   B 1 101 ? 25.820 10.044  28.212  1.00 24.01  ? 81  PHE   B CZ   1 
ATOM   3820 H H    A PHE   B 1 101 ? 20.997 9.025   25.632  0.47 23.87  ? 81  PHE   B H    1 
ATOM   3821 H H    B PHE   B 1 101 ? 20.965 9.032   25.578  0.53 23.87  ? 81  PHE   B H    1 
ATOM   3822 H HA   . PHE   B 1 101 ? 23.199 9.337   24.036  1.00 21.98  ? 81  PHE   B HA   1 
ATOM   3823 H HB2  . PHE   B 1 101 ? 22.869 7.260   25.901  1.00 22.11  ? 81  PHE   B HB2  1 
ATOM   3824 H HB3  . PHE   B 1 101 ? 24.056 7.347   24.848  1.00 22.11  ? 81  PHE   B HB3  1 
ATOM   3825 H HD1  . PHE   B 1 101 ? 25.781 9.084   25.152  1.00 23.77  ? 81  PHE   B HD1  1 
ATOM   3826 H HD2  . PHE   B 1 101 ? 23.065 8.395   27.982  1.00 27.78  ? 81  PHE   B HD2  1 
ATOM   3827 H HE1  . PHE   B 1 101 ? 27.053 10.269  26.665  1.00 25.94  ? 81  PHE   B HE1  1 
ATOM   3828 H HE2  . PHE   B 1 101 ? 24.308 9.650   29.461  1.00 30.74  ? 81  PHE   B HE2  1 
ATOM   3829 H HZ   . PHE   B 1 101 ? 26.344 10.504  28.827  1.00 28.81  ? 81  PHE   B HZ   1 
ATOM   3830 N N    . PRO   B 1 102 ? 21.158 8.581   22.527  1.00 20.64  ? 82  PRO   B N    1 
ATOM   3831 C CA   . PRO   B 1 102 ? 20.103 7.916   21.735  1.00 22.08  ? 82  PRO   B CA   1 
ATOM   3832 C C    . PRO   B 1 102 ? 20.590 6.802   20.828  1.00 23.77  ? 82  PRO   B C    1 
ATOM   3833 O O    . PRO   B 1 102 ? 19.791 5.934   20.465  1.00 27.36  ? 82  PRO   B O    1 
ATOM   3834 C CB   . PRO   B 1 102 ? 19.503 9.065   20.918  1.00 23.17  ? 82  PRO   B CB   1 
ATOM   3835 C CG   . PRO   B 1 102 ? 20.622 10.083  20.865  1.00 22.39  ? 82  PRO   B CG   1 
ATOM   3836 C CD   . PRO   B 1 102 ? 21.304 9.998   22.177  1.00 21.19  ? 82  PRO   B CD   1 
ATOM   3837 H HA   . PRO   B 1 102 ? 19.436 7.553   22.338  1.00 26.49  ? 82  PRO   B HA   1 
ATOM   3838 H HB2  . PRO   B 1 102 ? 19.264 8.757   20.030  1.00 27.81  ? 82  PRO   B HB2  1 
ATOM   3839 H HB3  . PRO   B 1 102 ? 18.721 9.424   21.366  1.00 27.81  ? 82  PRO   B HB3  1 
ATOM   3840 H HG2  . PRO   B 1 102 ? 21.233 9.861   20.145  1.00 26.87  ? 82  PRO   B HG2  1 
ATOM   3841 H HG3  . PRO   B 1 102 ? 20.253 10.969  20.725  1.00 26.87  ? 82  PRO   B HG3  1 
ATOM   3842 H HD2  . PRO   B 1 102 ? 22.239 10.242  22.098  1.00 25.43  ? 82  PRO   B HD2  1 
ATOM   3843 H HD3  . PRO   B 1 102 ? 20.867 10.565  22.832  1.00 25.43  ? 82  PRO   B HD3  1 
ATOM   3844 N N    . ASP   B 1 103 ? 21.860 6.796   20.426  1.00 22.25  ? 83  ASP   B N    1 
ATOM   3845 C CA   . ASP   B 1 103 ? 22.350 5.797   19.484  1.00 21.23  ? 83  ASP   B CA   1 
ATOM   3846 C C    . ASP   B 1 103 ? 23.549 5.037   20.045  1.00 19.09  ? 83  ASP   B C    1 
ATOM   3847 O O    . ASP   B 1 103 ? 24.331 4.465   19.284  1.00 21.28  ? 83  ASP   B O    1 
ATOM   3848 C CB   . ASP   B 1 103 ? 22.669 6.401   18.110  1.00 23.62  ? 83  ASP   B CB   1 
ATOM   3849 C CG   . ASP   B 1 103 ? 23.785 7.455   18.164  1.00 24.68  ? 83  ASP   B CG   1 
ATOM   3850 O OD1  . ASP   B 1 103 ? 24.262 7.773   19.265  1.00 23.82  ? 83  ASP   B OD1  1 
ATOM   3851 O OD2  . ASP   B 1 103 ? 24.181 7.988   17.097  1.00 26.84  ? 83  ASP   B OD2  1 
ATOM   3852 H H    . ASP   B 1 103 ? 22.455 7.360   20.686  1.00 26.70  ? 83  ASP   B H    1 
ATOM   3853 H HA   . ASP   B 1 103 ? 21.637 5.158   19.332  1.00 25.48  ? 83  ASP   B HA   1 
ATOM   3854 H HB2  . ASP   B 1 103 ? 22.955 5.692   17.512  1.00 28.35  ? 83  ASP   B HB2  1 
ATOM   3855 H HB3  . ASP   B 1 103 ? 21.871 6.828   17.760  1.00 28.35  ? 83  ASP   B HB3  1 
ATOM   3856 N N    . TRP   B 1 104 ? 23.692 5.013   21.370  1.00 18.30  ? 84  TRP   B N    1 
ATOM   3857 C CA   . TRP   B 1 104 ? 24.893 4.471   22.004  1.00 17.46  ? 84  TRP   B CA   1 
ATOM   3858 C C    . TRP   B 1 104 ? 25.153 3.029   21.616  1.00 16.97  ? 84  TRP   B C    1 
ATOM   3859 O O    . TRP   B 1 104 ? 24.262 2.170   21.706  1.00 19.18  ? 84  TRP   B O    1 
ATOM   3860 C CB   . TRP   B 1 104 ? 24.759 4.502   23.527  1.00 16.66  ? 84  TRP   B CB   1 
ATOM   3861 C CG   . TRP   B 1 104 ? 26.050 4.208   24.230  1.00 16.33  ? 84  TRP   B CG   1 
ATOM   3862 C CD1  . TRP   B 1 104 ? 26.420 3.025   24.839  1.00 17.32  ? 84  TRP   B CD1  1 
ATOM   3863 C CD2  . TRP   B 1 104 ? 27.172 5.083   24.356  1.00 15.66  ? 84  TRP   B CD2  1 
ATOM   3864 N NE1  . TRP   B 1 104 ? 27.684 3.132   25.332  1.00 17.92  ? 84  TRP   B NE1  1 
ATOM   3865 C CE2  . TRP   B 1 104 ? 28.174 4.379   25.057  1.00 16.84  ? 84  TRP   B CE2  1 
ATOM   3866 C CE3  . TRP   B 1 104 ? 27.419 6.400   23.954  1.00 16.30  ? 84  TRP   B CE3  1 
ATOM   3867 C CZ2  . TRP   B 1 104 ? 29.408 4.950   25.373  1.00 16.85  ? 84  TRP   B CZ2  1 
ATOM   3868 C CZ3  . TRP   B 1 104 ? 28.645 6.958   24.249  1.00 16.84  ? 84  TRP   B CZ3  1 
ATOM   3869 C CH2  . TRP   B 1 104 ? 29.636 6.233   24.959  1.00 17.66  ? 84  TRP   B CH2  1 
ATOM   3870 H H    . TRP   B 1 104 ? 23.106 5.305   21.928  1.00 21.96  ? 84  TRP   B H    1 
ATOM   3871 H HA   . TRP   B 1 104 ? 25.635 5.023   21.711  1.00 20.96  ? 84  TRP   B HA   1 
ATOM   3872 H HB2  . TRP   B 1 104 ? 24.463 5.384   23.800  1.00 20.00  ? 84  TRP   B HB2  1 
ATOM   3873 H HB3  . TRP   B 1 104 ? 24.110 3.835   23.800  1.00 20.00  ? 84  TRP   B HB3  1 
ATOM   3874 H HD1  . TRP   B 1 104 ? 25.885 2.267   24.903  1.00 20.79  ? 84  TRP   B HD1  1 
ATOM   3875 H HE1  . TRP   B 1 104 ? 28.108 2.512   25.751  1.00 21.51  ? 84  TRP   B HE1  1 
ATOM   3876 H HE3  . TRP   B 1 104 ? 26.771 6.888   23.499  1.00 19.56  ? 84  TRP   B HE3  1 
ATOM   3877 H HZ2  . TRP   B 1 104 ? 30.052 4.475   25.848  1.00 20.23  ? 84  TRP   B HZ2  1 
ATOM   3878 H HZ3  . TRP   B 1 104 ? 28.826 7.829   23.977  1.00 20.21  ? 84  TRP   B HZ3  1 
ATOM   3879 H HH2  . TRP   B 1 104 ? 30.453 6.636   25.145  1.00 21.19  ? 84  TRP   B HH2  1 
ATOM   3880 N N    . VAL   B 1 105 ? 26.425 2.732   21.326  1.00 16.75  ? 85  VAL   B N    1 
ATOM   3881 C CA   . VAL   B 1 105 ? 26.872 1.363   21.127  1.00 16.71  ? 85  VAL   B CA   1 
ATOM   3882 C C    . VAL   B 1 105 ? 28.160 1.107   21.895  1.00 16.17  ? 85  VAL   B C    1 
ATOM   3883 O O    . VAL   B 1 105 ? 29.036 1.973   21.995  1.00 15.98  ? 85  VAL   B O    1 
ATOM   3884 C CB   . VAL   B 1 105 ? 27.044 1.020   19.640  1.00 18.16  ? 85  VAL   B CB   1 
ATOM   3885 C CG1  . VAL   B 1 105 ? 25.709 1.094   18.926  1.00 20.78  ? 85  VAL   B CG1  1 
ATOM   3886 C CG2  . VAL   B 1 105 ? 28.083 1.909   18.935  1.00 17.98  ? 85  VAL   B CG2  1 
ATOM   3887 H H    . VAL   B 1 105 ? 27.048 3.318   21.240  1.00 20.11  ? 85  VAL   B H    1 
ATOM   3888 H HA   . VAL   B 1 105 ? 26.199 0.774   21.502  1.00 20.06  ? 85  VAL   B HA   1 
ATOM   3889 H HB   . VAL   B 1 105 ? 27.383 0.113   19.592  1.00 21.79  ? 85  VAL   B HB   1 
ATOM   3890 H HG11 . VAL   B 1 105 ? 25.804 0.715   18.038  1.00 24.94  ? 85  VAL   B HG11 1 
ATOM   3891 H HG12 . VAL   B 1 105 ? 25.052 0.590   19.431  1.00 24.94  ? 85  VAL   B HG12 1 
ATOM   3892 H HG13 . VAL   B 1 105 ? 25.436 2.022   18.861  1.00 24.94  ? 85  VAL   B HG13 1 
ATOM   3893 H HG21 . VAL   B 1 105 ? 28.108 1.680   17.993  1.00 21.58  ? 85  VAL   B HG21 1 
ATOM   3894 H HG22 . VAL   B 1 105 ? 27.828 2.839   19.043  1.00 21.58  ? 85  VAL   B HG22 1 
ATOM   3895 H HG23 . VAL   B 1 105 ? 28.953 1.757   19.336  1.00 21.58  ? 85  VAL   B HG23 1 
ATOM   3896 N N    . TRP   B 1 106 ? 28.298 -0.126  22.368  1.00 16.13  ? 86  TRP   B N    1 
ATOM   3897 C CA   . TRP   B 1 106 ? 29.561 -0.651  22.863  1.00 15.39  ? 86  TRP   B CA   1 
ATOM   3898 C C    . TRP   B 1 106 ? 30.233 -1.402  21.718  1.00 16.42  ? 86  TRP   B C    1 
ATOM   3899 O O    . TRP   B 1 106 ? 29.566 -2.129  20.984  1.00 17.55  ? 86  TRP   B O    1 
ATOM   3900 C CB   . TRP   B 1 106 ? 29.338 -1.616  24.034  1.00 15.77  ? 86  TRP   B CB   1 
ATOM   3901 C CG   . TRP   B 1 106 ? 28.573 -1.062  25.193  1.00 15.05  ? 86  TRP   B CG   1 
ATOM   3902 C CD1  . TRP   B 1 106 ? 27.302 -1.404  25.558  1.00 15.36  ? 86  TRP   B CD1  1 
ATOM   3903 C CD2  . TRP   B 1 106 ? 28.978 -0.022  26.110  1.00 14.98  ? 86  TRP   B CD2  1 
ATOM   3904 N NE1  . TRP   B 1 106 ? 26.924 -0.708  26.669  1.00 16.40  ? 86  TRP   B NE1  1 
ATOM   3905 C CE2  . TRP   B 1 106 ? 27.922 0.152   27.029  1.00 16.54  ? 86  TRP   B CE2  1 
ATOM   3906 C CE3  . TRP   B 1 106 ? 30.141 0.744   26.277  1.00 15.55  ? 86  TRP   B CE3  1 
ATOM   3907 C CZ2  . TRP   B 1 106 ? 27.975 1.071   28.066  1.00 16.95  ? 86  TRP   B CZ2  1 
ATOM   3908 C CZ3  . TRP   B 1 106 ? 30.194 1.645   27.334  1.00 16.92  ? 86  TRP   B CZ3  1 
ATOM   3909 C CH2  . TRP   B 1 106 ? 29.125 1.796   28.207  1.00 17.68  ? 86  TRP   B CH2  1 
ATOM   3910 H H    . TRP   B 1 106 ? 27.654 -0.695  22.414  1.00 19.35  ? 86  TRP   B H    1 
ATOM   3911 H HA   . TRP   B 1 106 ? 30.127 0.071   23.180  1.00 18.47  ? 86  TRP   B HA   1 
ATOM   3912 H HB2  . TRP   B 1 106 ? 28.846 -2.384  23.705  1.00 18.92  ? 86  TRP   B HB2  1 
ATOM   3913 H HB3  . TRP   B 1 106 ? 30.205 -1.895  24.368  1.00 18.92  ? 86  TRP   B HB3  1 
ATOM   3914 H HD1  . TRP   B 1 106 ? 26.771 -2.023  25.113  1.00 18.43  ? 86  TRP   B HD1  1 
ATOM   3915 H HE1  . TRP   B 1 106 ? 26.173 -0.796  27.079  1.00 19.69  ? 86  TRP   B HE1  1 
ATOM   3916 H HE3  . TRP   B 1 106 ? 30.860 0.652   25.694  1.00 18.67  ? 86  TRP   B HE3  1 
ATOM   3917 H HZ2  . TRP   B 1 106 ? 27.255 1.189   28.643  1.00 20.34  ? 86  TRP   B HZ2  1 
ATOM   3918 H HZ3  . TRP   B 1 106 ? 30.960 2.157   27.458  1.00 20.31  ? 86  TRP   B HZ3  1 
ATOM   3919 H HH2  . TRP   B 1 106 ? 29.193 2.405   28.906  1.00 21.22  ? 86  TRP   B HH2  1 
ATOM   3920 N N    . THR   B 1 107 ? 31.539 -1.193  21.559  1.00 16.26  ? 87  THR   B N    1 
ATOM   3921 C CA   . THR   B 1 107 ? 32.301 -1.774  20.458  1.00 16.65  ? 87  THR   B CA   1 
ATOM   3922 C C    . THR   B 1 107 ? 33.584 -2.402  21.015  1.00 15.49  ? 87  THR   B C    1 
ATOM   3923 O O    . THR   B 1 107 ? 33.929 -2.229  22.185  1.00 15.58  ? 87  THR   B O    1 
ATOM   3924 C CB   . THR   B 1 107 ? 32.679 -0.722  19.403  1.00 18.60  ? 87  THR   B CB   1 
ATOM   3925 O OG1  . THR   B 1 107 ? 33.648 0.176   19.955  1.00 19.05  ? 87  THR   B OG1  1 
ATOM   3926 C CG2  . THR   B 1 107 ? 31.465 0.078   18.951  1.00 19.83  ? 87  THR   B CG2  1 
ATOM   3927 H H    . THR   B 1 107 ? 32.015 -0.709  22.088  1.00 19.52  ? 87  THR   B H    1 
ATOM   3928 H HA   . THR   B 1 107 ? 31.760 -2.459  20.033  1.00 19.99  ? 87  THR   B HA   1 
ATOM   3929 H HB   . THR   B 1 107 ? 33.044 -1.175  18.627  1.00 22.32  ? 87  THR   B HB   1 
ATOM   3930 H HG1  . THR   B 1 107 ? 34.390 -0.210  20.025  1.00 22.86  ? 87  THR   B HG1  1 
ATOM   3931 H HG21 . THR   B 1 107 ? 31.717 0.690   18.241  1.00 23.79  ? 87  THR   B HG21 1 
ATOM   3932 H HG22 . THR   B 1 107 ? 30.777 -0.520  18.621  1.00 23.79  ? 87  THR   B HG22 1 
ATOM   3933 H HG23 . THR   B 1 107 ? 31.109 0.589   19.694  1.00 23.79  ? 87  THR   B HG23 1 
ATOM   3934 N N    . ASP   B 1 108 ? 34.281 -3.181  20.187  1.00 16.85  ? 88  ASP   B N    1 
ATOM   3935 C CA   . ASP   B 1 108 ? 35.570 -3.758  20.569  1.00 17.20  ? 88  ASP   B CA   1 
ATOM   3936 C C    . ASP   B 1 108 ? 35.450 -4.541  21.876  1.00 16.42  ? 88  ASP   B C    1 
ATOM   3937 O O    . ASP   B 1 108 ? 36.305 -4.464  22.765  1.00 17.76  ? 88  ASP   B O    1 
ATOM   3938 C CB   . ASP   B 1 108 ? 36.656 -2.674  20.654  1.00 18.69  ? 88  ASP   B CB   1 
ATOM   3939 C CG   . ASP   B 1 108 ? 36.767 -1.892  19.371  0.85 21.66  ? 88  ASP   B CG   1 
ATOM   3940 O OD1  . ASP   B 1 108 ? 37.404 -2.404  18.432  0.87 27.49  ? 88  ASP   B OD1  1 
ATOM   3941 O OD2  . ASP   B 1 108 ? 36.126 -0.822  19.246  0.75 19.90  ? 88  ASP   B OD2  1 
ATOM   3942 H H    . ASP   B 1 108 ? 34.027 -3.390  19.392  1.00 20.22  ? 88  ASP   B H    1 
ATOM   3943 H HA   . ASP   B 1 108 ? 35.845 -4.388  19.885  1.00 20.64  ? 88  ASP   B HA   1 
ATOM   3944 H HB2  . ASP   B 1 108 ? 36.435 -2.056  21.368  1.00 22.43  ? 88  ASP   B HB2  1 
ATOM   3945 H HB3  . ASP   B 1 108 ? 37.513 -3.092  20.830  1.00 22.43  ? 88  ASP   B HB3  1 
ATOM   3946 N N    . ILE   B 1 109 ? 34.370 -5.313  21.990  1.00 16.46  ? 89  ILE   B N    1 
ATOM   3947 C CA   . ILE   B 1 109 ? 34.000 -5.919  23.258  1.00 16.46  ? 89  ILE   B CA   1 
ATOM   3948 C C    . ILE   B 1 109 ? 34.880 -7.136  23.500  1.00 16.44  ? 89  ILE   B C    1 
ATOM   3949 O O    . ILE   B 1 109 ? 34.917 -8.061  22.685  1.00 19.56  ? 89  ILE   B O    1 
ATOM   3950 C CB   . ILE   B 1 109 ? 32.522 -6.312  23.230  1.00 17.02  ? 89  ILE   B CB   1 
ATOM   3951 C CG1  . ILE   B 1 109 ? 31.631 -5.059  23.108  1.00 17.85  ? 89  ILE   B CG1  1 
ATOM   3952 C CG2  . ILE   B 1 109 ? 32.154 -7.125  24.472  1.00 18.93  ? 89  ILE   B CG2  1 
ATOM   3953 C CD1  . ILE   B 1 109 ? 30.242 -5.363  22.620  1.00 19.74  ? 89  ILE   B CD1  1 
ATOM   3954 H H    . ILE   B 1 109 ? 33.836 -5.500  21.343  1.00 19.75  ? 89  ILE   B H    1 
ATOM   3955 H HA   . ILE   B 1 109 ? 34.156 -5.291  23.981  1.00 19.75  ? 89  ILE   B HA   1 
ATOM   3956 H HB   . ILE   B 1 109 ? 32.370 -6.868  22.449  1.00 20.42  ? 89  ILE   B HB   1 
ATOM   3957 H HG12 . ILE   B 1 109 ? 31.556 -4.641  23.981  1.00 21.42  ? 89  ILE   B HG12 1 
ATOM   3958 H HG13 . ILE   B 1 109 ? 32.040 -4.443  22.480  1.00 21.42  ? 89  ILE   B HG13 1 
ATOM   3959 H HG21 . ILE   B 1 109 ? 31.188 -7.179  24.540  1.00 22.72  ? 89  ILE   B HG21 1 
ATOM   3960 H HG22 . ILE   B 1 109 ? 32.530 -8.015  24.390  1.00 22.72  ? 89  ILE   B HG22 1 
ATOM   3961 H HG23 . ILE   B 1 109 ? 32.516 -6.684  25.257  1.00 22.72  ? 89  ILE   B HG23 1 
ATOM   3962 H HD11 . ILE   B 1 109 ? 29.742 -4.534  22.554  1.00 23.69  ? 89  ILE   B HD11 1 
ATOM   3963 H HD12 . ILE   B 1 109 ? 30.300 -5.785  21.748  1.00 23.69  ? 89  ILE   B HD12 1 
ATOM   3964 H HD13 . ILE   B 1 109 ? 29.810 -5.961  23.249  1.00 23.69  ? 89  ILE   B HD13 1 
ATOM   3965 N N    . GLN   B 1 110 ? 35.557 -7.154  24.639  1.00 15.64  ? 90  GLN   B N    1 
ATOM   3966 C CA   . GLN   B 1 110 ? 36.357 -8.291  25.087  1.00 16.19  ? 90  GLN   B CA   1 
ATOM   3967 C C    . GLN   B 1 110 ? 35.880 -8.694  26.478  1.00 15.88  ? 90  GLN   B C    1 
ATOM   3968 O O    . GLN   B 1 110 ? 36.023 -7.933  27.443  1.00 15.99  ? 90  GLN   B O    1 
ATOM   3969 C CB   . GLN   B 1 110 ? 37.821 -7.907  25.147  1.00 19.26  ? 90  GLN   B CB   1 
ATOM   3970 C CG   . GLN   B 1 110 ? 38.401 -7.403  23.859  1.00 25.23  ? 90  GLN   B CG   1 
ATOM   3971 C CD   . GLN   B 1 110 ? 39.902 -7.222  24.012  1.00 30.35  ? 90  GLN   B CD   1 
ATOM   3972 O OE1  . GLN   B 1 110 ? 40.669 -8.180  23.824  1.00 33.10  ? 90  GLN   B OE1  1 
ATOM   3973 N NE2  . GLN   B 1 110 ? 40.330 -6.013  24.448  1.00 30.14  ? 90  GLN   B NE2  1 
ATOM   3974 H H    . GLN   B 1 110 ? 35.572 -6.496  25.193  1.00 18.77  ? 90  GLN   B H    1 
ATOM   3975 H HA   . GLN   B 1 110 ? 36.232 -9.037  24.479  1.00 19.43  ? 90  GLN   B HA   1 
ATOM   3976 H HB2  . GLN   B 1 110 ? 37.927 -7.204  25.807  1.00 23.11  ? 90  GLN   B HB2  1 
ATOM   3977 H HB3  . GLN   B 1 110 ? 38.332 -8.688  25.409  1.00 23.11  ? 90  GLN   B HB3  1 
ATOM   3978 H HG2  . GLN   B 1 110 ? 38.234 -8.044  23.151  1.00 30.28  ? 90  GLN   B HG2  1 
ATOM   3979 H HG3  . GLN   B 1 110 ? 38.004 -6.547  23.633  1.00 30.28  ? 90  GLN   B HG3  1 
ATOM   3980 H HE21 . GLN   B 1 110 ? 39.761 -5.393  24.623  1.00 36.17  ? 90  GLN   B HE21 1 
ATOM   3981 H HE22 . GLN   B 1 110 ? 41.171 -5.866  24.549  1.00 36.17  ? 90  GLN   B HE22 1 
ATOM   3982 N N    . ILE   B 1 111 ? 35.322 -9.888  26.594  1.00 15.83  ? 91  ILE   B N    1 
ATOM   3983 C CA   . ILE   B 1 111 ? 34.769 -10.363 27.853  1.00 16.20  ? 91  ILE   B CA   1 
ATOM   3984 C C    . ILE   B 1 111 ? 35.779 -11.278 28.521  1.00 16.56  ? 91  ILE   B C    1 
ATOM   3985 O O    . ILE   B 1 111 ? 36.272 -12.227 27.898  1.00 19.95  ? 91  ILE   B O    1 
ATOM   3986 C CB   . ILE   B 1 111 ? 33.444 -11.101 27.619  1.00 18.52  ? 91  ILE   B CB   1 
ATOM   3987 C CG1  . ILE   B 1 111 ? 32.402 -10.114 27.067  1.00 20.11  ? 91  ILE   B CG1  1 
ATOM   3988 C CG2  . ILE   B 1 111 ? 32.987 -11.753 28.911  1.00 20.79  ? 91  ILE   B CG2  1 
ATOM   3989 C CD1  . ILE   B 1 111 ? 31.114 -10.762 26.574  1.00 23.23  ? 91  ILE   B CD1  1 
ATOM   3990 H H    . ILE   B 1 111 ? 35.250 -10.451 25.948  1.00 19.00  ? 91  ILE   B H    1 
ATOM   3991 H HA   . ILE   B 1 111 ? 34.612 -9.605  28.438  1.00 19.44  ? 91  ILE   B HA   1 
ATOM   3992 H HB   . ILE   B 1 111 ? 33.564 -11.805 26.963  1.00 22.22  ? 91  ILE   B HB   1 
ATOM   3993 H HG12 . ILE   B 1 111 ? 32.164 -9.490  27.771  1.00 24.14  ? 91  ILE   B HG12 1 
ATOM   3994 H HG13 . ILE   B 1 111 ? 32.794 -9.637  26.320  1.00 24.14  ? 91  ILE   B HG13 1 
ATOM   3995 H HG21 . ILE   B 1 111 ? 32.050 -11.990 28.832  1.00 24.95  ? 91  ILE   B HG21 1 
ATOM   3996 H HG22 . ILE   B 1 111 ? 33.518 -12.550 29.068  1.00 24.95  ? 91  ILE   B HG22 1 
ATOM   3997 H HG23 . ILE   B 1 111 ? 33.109 -11.126 29.641  1.00 24.95  ? 91  ILE   B HG23 1 
ATOM   3998 H HD11 . ILE   B 1 111 ? 30.599 -10.104 26.080  1.00 27.88  ? 91  ILE   B HD11 1 
ATOM   3999 H HD12 . ILE   B 1 111 ? 31.337 -11.508 25.996  1.00 27.88  ? 91  ILE   B HD12 1 
ATOM   4000 H HD13 . ILE   B 1 111 ? 30.605 -11.075 27.338  1.00 27.88  ? 91  ILE   B HD13 1 
ATOM   4001 N N    . PHE   B 1 112 ? 36.037 -11.027 29.799  1.00 15.51  ? 92  PHE   B N    1 
ATOM   4002 C CA   . PHE   B 1 112 ? 36.970 -11.803 30.600  1.00 15.34  ? 92  PHE   B CA   1 
ATOM   4003 C C    . PHE   B 1 112 ? 36.210 -12.523 31.702  1.00 16.29  ? 92  PHE   B C    1 
ATOM   4004 O O    . PHE   B 1 112 ? 35.649 -11.873 32.595  1.00 16.30  ? 92  PHE   B O    1 
ATOM   4005 C CB   . PHE   B 1 112 ? 38.061 -10.928 31.198  1.00 15.69  ? 92  PHE   B CB   1 
ATOM   4006 C CG   . PHE   B 1 112 ? 38.889 -10.210 30.166  1.00 16.22  ? 92  PHE   B CG   1 
ATOM   4007 C CD1  . PHE   B 1 112 ? 39.988 -10.839 29.609  1.00 17.20  ? 92  PHE   B CD1  1 
ATOM   4008 C CD2  . PHE   B 1 112 ? 38.568 -8.928  29.746  1.00 17.76  ? 92  PHE   B CD2  1 
ATOM   4009 C CE1  . PHE   B 1 112 ? 40.742 -10.210 28.666  1.00 20.28  ? 92  PHE   B CE1  1 
ATOM   4010 C CE2  . PHE   B 1 112 ? 39.322 -8.286  28.765  1.00 19.06  ? 92  PHE   B CE2  1 
ATOM   4011 C CZ   . PHE   B 1 112 ? 40.424 -8.942  28.243  1.00 20.22  ? 92  PHE   B CZ   1 
ATOM   4012 H H    . PHE   B 1 112 ? 35.668 -10.387 30.239  1.00 18.62  ? 92  PHE   B H    1 
ATOM   4013 H HA   . PHE   B 1 112 ? 37.380 -12.464 30.021  1.00 18.42  ? 92  PHE   B HA   1 
ATOM   4014 H HB2  . PHE   B 1 112 ? 37.648 -10.259 31.767  1.00 18.84  ? 92  PHE   B HB2  1 
ATOM   4015 H HB3  . PHE   B 1 112 ? 38.657 -11.486 31.722  1.00 18.84  ? 92  PHE   B HB3  1 
ATOM   4016 H HD1  . PHE   B 1 112 ? 40.214 -11.699 29.882  1.00 20.64  ? 92  PHE   B HD1  1 
ATOM   4017 H HD2  . PHE   B 1 112 ? 37.840 -8.491  30.123  1.00 21.31  ? 92  PHE   B HD2  1 
ATOM   4018 H HE1  . PHE   B 1 112 ? 41.480 -10.644 28.303  1.00 24.33  ? 92  PHE   B HE1  1 
ATOM   4019 H HE2  . PHE   B 1 112 ? 39.089 -7.436  28.467  1.00 22.87  ? 92  PHE   B HE2  1 
ATOM   4020 H HZ   . PHE   B 1 112 ? 40.952 -8.522  27.603  1.00 24.27  ? 92  PHE   B HZ   1 
ATOM   4021 N N    A GLU   B 1 113 ? 36.144 -13.857 31.616  0.50 17.25  ? 93  GLU   B N    1 
ATOM   4022 N N    B GLU   B 1 113 ? 36.174 -13.854 31.602  0.50 17.16  ? 93  GLU   B N    1 
ATOM   4023 C CA   A GLU   B 1 113 ? 35.740 -14.635 32.774  0.50 18.55  ? 93  GLU   B CA   1 
ATOM   4024 C CA   B GLU   B 1 113 ? 35.836 -14.691 32.733  0.50 18.10  ? 93  GLU   B CA   1 
ATOM   4025 C C    A GLU   B 1 113 ? 36.911 -14.690 33.747  0.50 17.88  ? 93  GLU   B C    1 
ATOM   4026 C C    B GLU   B 1 113 ? 36.914 -14.543 33.796  0.50 17.00  ? 93  GLU   B C    1 
ATOM   4027 O O    A GLU   B 1 113 ? 38.059 -14.438 33.378  0.50 18.62  ? 93  GLU   B O    1 
ATOM   4028 O O    B GLU   B 1 113 ? 38.003 -14.017 33.543  0.50 16.99  ? 93  GLU   B O    1 
ATOM   4029 C CB   A GLU   B 1 113 ? 35.311 -16.042 32.364  0.50 22.69  ? 93  GLU   B CB   1 
ATOM   4030 C CB   B GLU   B 1 113 ? 35.779 -16.144 32.281  0.50 21.65  ? 93  GLU   B CB   1 
ATOM   4031 C CG   A GLU   B 1 113 ? 36.390 -16.845 31.687  0.50 26.40  ? 93  GLU   B CG   1 
ATOM   4032 C CG   B GLU   B 1 113 ? 34.800 -16.363 31.134  0.50 25.03  ? 93  GLU   B CG   1 
ATOM   4033 C CD   A GLU   B 1 113 ? 35.854 -18.123 31.062  0.50 29.07  ? 93  GLU   B CD   1 
ATOM   4034 C CD   B GLU   B 1 113 ? 34.904 -17.744 30.509  0.50 29.80  ? 93  GLU   B CD   1 
ATOM   4035 O OE1  A GLU   B 1 113 ? 34.805 -18.058 30.380  0.50 29.84  ? 93  GLU   B OE1  1 
ATOM   4036 O OE1  B GLU   B 1 113 ? 35.700 -18.573 31.004  0.50 29.11  ? 93  GLU   B OE1  1 
ATOM   4037 O OE2  A GLU   B 1 113 ? 36.481 -19.185 31.260  0.50 30.93  ? 93  GLU   B OE2  1 
ATOM   4038 O OE2  B GLU   B 1 113 ? 34.186 -17.994 29.518  0.50 33.74  ? 93  GLU   B OE2  1 
ATOM   4039 H H    A GLU   B 1 113 ? 36.326 -14.317 30.912  0.50 20.70  ? 93  GLU   B H    1 
ATOM   4040 H H    B GLU   B 1 113 ? 36.344 -14.292 30.882  0.50 20.59  ? 93  GLU   B H    1 
ATOM   4041 H HA   A GLU   B 1 113 ? 34.976 -14.229 33.212  0.50 22.26  ? 93  GLU   B HA   1 
ATOM   4042 H HA   B GLU   B 1 113 ? 34.976 -14.436 33.102  0.50 21.73  ? 93  GLU   B HA   1 
ATOM   4043 H HB2  A GLU   B 1 113 ? 35.039 -16.527 33.159  0.50 27.23  ? 93  GLU   B HB2  1 
ATOM   4044 H HB2  B GLU   B 1 113 ? 36.660 -16.417 31.980  0.50 25.98  ? 93  GLU   B HB2  1 
ATOM   4045 H HB3  A GLU   B 1 113 ? 34.566 -15.971 31.747  0.50 27.23  ? 93  GLU   B HB3  1 
ATOM   4046 H HB3  B GLU   B 1 113 ? 35.496 -16.696 33.026  0.50 25.98  ? 93  GLU   B HB3  1 
ATOM   4047 H HG2  A GLU   B 1 113 ? 36.790 -16.310 30.983  0.50 31.69  ? 93  GLU   B HG2  1 
ATOM   4048 H HG2  B GLU   B 1 113 ? 33.896 -16.254 31.468  0.50 30.03  ? 93  GLU   B HG2  1 
ATOM   4049 H HG3  A GLU   B 1 113 ? 37.063 -17.088 32.342  0.50 31.69  ? 93  GLU   B HG3  1 
ATOM   4050 H HG3  B GLU   B 1 113 ? 34.979 -15.708 30.441  0.50 30.03  ? 93  GLU   B HG3  1 
ATOM   4051 N N    . THR   B 1 114 ? 36.618 -15.008 35.003  1.00 17.40  ? 94  THR   B N    1 
ATOM   4052 C CA   . THR   B 1 114 ? 37.603 -15.004 36.074  1.00 17.33  ? 94  THR   B CA   1 
ATOM   4053 C C    . THR   B 1 114 ? 37.496 -16.313 36.848  1.00 17.94  ? 94  THR   B C    1 
ATOM   4054 O O    . THR   B 1 114 ? 36.633 -17.159 36.576  1.00 19.80  ? 94  THR   B O    1 
ATOM   4055 C CB   . THR   B 1 114 ? 37.520 -13.799 37.029  1.00 17.00  ? 94  THR   B CB   1 
ATOM   4056 O OG1  . THR   B 1 114 ? 36.457 -13.984 37.962  1.00 17.38  ? 94  THR   B OG1  1 
ATOM   4057 C CG2  . THR   B 1 114 ? 37.376 -12.483 36.266  1.00 17.45  ? 94  THR   B CG2  1 
ATOM   4058 H H    A THR   B 1 114 ? 35.831 -15.236 35.265  0.50 20.88  ? 94  THR   B H    1 
ATOM   4059 H H    B THR   B 1 114 ? 35.852 -15.331 35.225  0.50 20.88  ? 94  THR   B H    1 
ATOM   4060 H HA   . THR   B 1 114 ? 38.469 -14.942 35.641  1.00 20.80  ? 94  THR   B HA   1 
ATOM   4061 H HB   . THR   B 1 114 ? 38.348 -13.731 37.529  1.00 20.41  ? 94  THR   B HB   1 
ATOM   4062 H HG1  . THR   B 1 114 ? 35.732 -14.097 37.553  1.00 20.86  ? 94  THR   B HG1  1 
ATOM   4063 H HG21 . THR   B 1 114 ? 37.379 -11.737 36.887  1.00 20.95  ? 94  THR   B HG21 1 
ATOM   4064 H HG22 . THR   B 1 114 ? 38.114 -12.377 35.645  1.00 20.95  ? 94  THR   B HG22 1 
ATOM   4065 H HG23 . THR   B 1 114 ? 36.543 -12.476 35.770  1.00 20.95  ? 94  THR   B HG23 1 
ATOM   4066 N N    . GLN   B 1 115 ? 38.382 -16.468 37.837  1.00 18.69  ? 95  GLN   B N    1 
ATOM   4067 C CA   . GLN   B 1 115 ? 38.311 -17.624 38.714  1.00 19.92  ? 95  GLN   B CA   1 
ATOM   4068 C C    . GLN   B 1 115 ? 37.041 -17.637 39.545  1.00 20.39  ? 95  GLN   B C    1 
ATOM   4069 O O    . GLN   B 1 115 ? 36.656 -18.701 40.062  1.00 22.15  ? 95  GLN   B O    1 
ATOM   4070 C CB   . GLN   B 1 115 ? 39.538 -17.714 39.644  1.00 20.85  ? 95  GLN   B CB   1 
ATOM   4071 C CG   . GLN   B 1 115 ? 39.650 -16.648 40.742  1.00 20.53  ? 95  GLN   B CG   1 
ATOM   4072 C CD   . GLN   B 1 115 ? 40.357 -15.384 40.317  1.00 21.40  ? 95  GLN   B CD   1 
ATOM   4073 O OE1  . GLN   B 1 115 ? 40.367 -14.993 39.156  1.00 19.71  ? 95  GLN   B OE1  1 
ATOM   4074 N NE2  . GLN   B 1 115 ? 40.984 -14.758 41.277  1.00 27.14  ? 95  GLN   B NE2  1 
ATOM   4075 H H    . GLN   B 1 115 ? 39.022 -15.922 38.013  1.00 22.43  ? 95  GLN   B H    1 
ATOM   4076 H HA   . GLN   B 1 115 ? 38.325 -18.414 38.151  1.00 23.90  ? 95  GLN   B HA   1 
ATOM   4077 H HB2  . GLN   B 1 115 ? 39.516 -18.577 40.088  1.00 25.03  ? 95  GLN   B HB2  1 
ATOM   4078 H HB3  . GLN   B 1 115 ? 40.336 -17.643 39.097  1.00 25.03  ? 95  GLN   B HB3  1 
ATOM   4079 H HG2  . GLN   B 1 115 ? 38.756 -16.401 41.026  1.00 24.64  ? 95  GLN   B HG2  1 
ATOM   4080 H HG3  . GLN   B 1 115 ? 40.144 -17.023 41.488  1.00 24.64  ? 95  GLN   B HG3  1 
ATOM   4081 H HE21 . GLN   B 1 115 ? 40.971 -15.075 42.077  1.00 32.56  ? 95  GLN   B HE21 1 
ATOM   4082 H HE22 . GLN   B 1 115 ? 41.410 -14.030 41.110  1.00 32.56  ? 95  GLN   B HE22 1 
ATOM   4083 N N    . ASP   B 1 116 ? 36.387 -16.481 39.713  1.00 20.01  ? 96  ASP   B N    1 
ATOM   4084 C CA   . ASP   B 1 116 ? 35.084 -16.412 40.371  1.00 19.97  ? 96  ASP   B CA   1 
ATOM   4085 C C    . ASP   B 1 116 ? 34.037 -16.565 39.275  1.00 18.74  ? 96  ASP   B C    1 
ATOM   4086 O O    . ASP   B 1 116 ? 33.929 -15.688 38.413  1.00 19.16  ? 96  ASP   B O    1 
ATOM   4087 C CB   . ASP   B 1 116 ? 34.950 -15.060 41.075  1.00 20.01  ? 96  ASP   B CB   1 
ATOM   4088 C CG   . ASP   B 1 116 ? 33.657 -14.891 41.819  1.00 21.32  ? 96  ASP   B CG   1 
ATOM   4089 O OD1  . ASP   B 1 116 ? 32.701 -15.650 41.552  1.00 21.66  ? 96  ASP   B OD1  1 
ATOM   4090 O OD2  . ASP   B 1 116 ? 33.592 -13.958 42.665  1.00 22.77  ? 96  ASP   B OD2  1 
ATOM   4091 H H    . ASP   B 1 116 ? 36.683 -15.717 39.451  1.00 24.02  ? 96  ASP   B H    1 
ATOM   4092 H HA   . ASP   B 1 116 ? 34.967 -17.115 41.029  1.00 23.97  ? 96  ASP   B HA   1 
ATOM   4093 H HB2  . ASP   B 1 116 ? 35.673 -14.967 41.715  1.00 24.01  ? 96  ASP   B HB2  1 
ATOM   4094 H HB3  . ASP   B 1 116 ? 35.003 -14.355 40.411  1.00 24.01  ? 96  ASP   B HB3  1 
ATOM   4095 N N    . PRO   B 1 117 ? 33.253 -17.649 39.260  1.00 19.64  ? 97  PRO   B N    1 
ATOM   4096 C CA   . PRO   B 1 117 ? 32.272 -17.826 38.173  1.00 19.48  ? 97  PRO   B CA   1 
ATOM   4097 C C    . PRO   B 1 117 ? 31.219 -16.736 38.133  1.00 18.01  ? 97  PRO   B C    1 
ATOM   4098 O O    . PRO   B 1 117 ? 30.548 -16.589 37.103  1.00 19.03  ? 97  PRO   B O    1 
ATOM   4099 C CB   . PRO   B 1 117 ? 31.614 -19.181 38.490  1.00 21.89  ? 97  PRO   B CB   1 
ATOM   4100 C CG   . PRO   B 1 117 ? 31.818 -19.345 39.943  1.00 23.97  ? 97  PRO   B CG   1 
ATOM   4101 C CD   . PRO   B 1 117 ? 33.144 -18.695 40.280  1.00 21.62  ? 97  PRO   B CD   1 
ATOM   4102 H HA   . PRO   B 1 117 ? 32.739 -17.877 37.324  1.00 23.38  ? 97  PRO   B HA   1 
ATOM   4103 H HB2  . PRO   B 1 117 ? 30.670 -19.154 38.269  1.00 26.27  ? 97  PRO   B HB2  1 
ATOM   4104 H HB3  . PRO   B 1 117 ? 32.051 -19.890 37.992  1.00 26.27  ? 97  PRO   B HB3  1 
ATOM   4105 H HG2  . PRO   B 1 117 ? 31.095 -18.910 40.421  1.00 28.76  ? 97  PRO   B HG2  1 
ATOM   4106 H HG3  . PRO   B 1 117 ? 31.839 -20.290 40.160  1.00 28.76  ? 97  PRO   B HG3  1 
ATOM   4107 H HD2  . PRO   B 1 117 ? 33.127 -18.312 41.171  1.00 25.94  ? 97  PRO   B HD2  1 
ATOM   4108 H HD3  . PRO   B 1 117 ? 33.872 -19.331 40.206  1.00 25.94  ? 97  PRO   B HD3  1 
ATOM   4109 N N    . ASN   B 1 118 ? 31.072 -15.967 39.215  1.00 17.36  ? 98  ASN   B N    1 
ATOM   4110 C CA   . ASN   B 1 118 ? 30.115 -14.883 39.326  1.00 17.45  ? 98  ASN   B CA   1 
ATOM   4111 C C    . ASN   B 1 118 ? 30.735 -13.505 39.144  1.00 17.22  ? 98  ASN   B C    1 
ATOM   4112 O O    . ASN   B 1 118 ? 30.094 -12.512 39.480  1.00 19.26  ? 98  ASN   B O    1 
ATOM   4113 C CB   . ASN   B 1 118 ? 29.405 -14.998 40.673  1.00 19.04  ? 98  ASN   B CB   1 
ATOM   4114 C CG   . ASN   B 1 118 ? 28.506 -16.196 40.741  1.00 22.63  ? 98  ASN   B CG   1 
ATOM   4115 O OD1  . ASN   B 1 118 ? 27.658 -16.369 39.887  1.00 23.68  ? 98  ASN   B OD1  1 
ATOM   4116 N ND2  . ASN   B 1 118 ? 28.732 -17.051 41.727  1.00 26.35  ? 98  ASN   B ND2  1 
ATOM   4117 H H    . ASN   B 1 118 ? 31.543 -16.064 39.928  1.00 20.83  ? 98  ASN   B H    1 
ATOM   4118 H HA   . ASN   B 1 118 ? 29.452 -14.967 38.623  1.00 20.95  ? 98  ASN   B HA   1 
ATOM   4119 H HB2  . ASN   B 1 118 ? 30.068 -15.077 41.377  1.00 22.85  ? 98  ASN   B HB2  1 
ATOM   4120 H HB3  . ASN   B 1 118 ? 28.863 -14.206 40.815  1.00 22.85  ? 98  ASN   B HB3  1 
ATOM   4121 H HD21 . ASN   B 1 118 ? 28.242 -17.754 41.807  1.00 31.62  ? 98  ASN   B HD21 1 
ATOM   4122 H HD22 . ASN   B 1 118 ? 29.368 -16.903 42.287  1.00 31.62  ? 98  ASN   B HD22 1 
ATOM   4123 N N    . TRP   B 1 119 ? 31.964 -13.411 38.643  1.00 16.67  ? 99  TRP   B N    1 
ATOM   4124 C CA   . TRP   B 1 119 ? 32.595 -12.112 38.423  1.00 16.06  ? 99  TRP   B CA   1 
ATOM   4125 C C    . TRP   B 1 119 ? 33.256 -12.084 37.052  1.00 15.32  ? 99  TRP   B C    1 
ATOM   4126 O O    . TRP   B 1 119 ? 34.073 -12.951 36.736  1.00 16.49  ? 99  TRP   B O    1 
ATOM   4127 C CB   . TRP   B 1 119 ? 33.617 -11.840 39.515  1.00 16.15  ? 99  TRP   B CB   1 
ATOM   4128 C CG   . TRP   B 1 119 ? 33.964 -10.367 39.742  1.00 15.20  ? 99  TRP   B CG   1 
ATOM   4129 C CD1  . TRP   B 1 119 ? 33.917 -9.314  38.839  1.00 15.71  ? 99  TRP   B CD1  1 
ATOM   4130 C CD2  . TRP   B 1 119 ? 34.377 -9.795  40.991  1.00 15.52  ? 99  TRP   B CD2  1 
ATOM   4131 N NE1  . TRP   B 1 119 ? 34.288 -8.143  39.475  1.00 15.00  ? 99  TRP   B NE1  1 
ATOM   4132 C CE2  . TRP   B 1 119 ? 34.562 -8.413  40.790  1.00 14.71  ? 99  TRP   B CE2  1 
ATOM   4133 C CE3  . TRP   B 1 119 ? 34.595 -10.324 42.264  1.00 17.53  ? 99  TRP   B CE3  1 
ATOM   4134 C CZ2  . TRP   B 1 119 ? 34.984 -7.566  41.814  1.00 16.63  ? 99  TRP   B CZ2  1 
ATOM   4135 C CZ3  . TRP   B 1 119 ? 35.010 -9.488  43.277  1.00 19.38  ? 99  TRP   B CZ3  1 
ATOM   4136 C CH2  . TRP   B 1 119 ? 35.212 -8.110  43.042  1.00 18.87  ? 99  TRP   B CH2  1 
ATOM   4137 H H    . TRP   B 1 119 ? 32.451 -14.084 38.422  1.00 20.01  ? 99  TRP   B H    1 
ATOM   4138 H HA   . TRP   B 1 119 ? 31.917 -11.418 38.430  1.00 19.28  ? 99  TRP   B HA   1 
ATOM   4139 H HB2  . TRP   B 1 119 ? 33.270 -12.187 40.352  1.00 19.38  ? 99  TRP   B HB2  1 
ATOM   4140 H HB3  . TRP   B 1 119 ? 34.440 -12.297 39.283  1.00 19.38  ? 99  TRP   B HB3  1 
ATOM   4141 H HD1  . TRP   B 1 119 ? 33.674 -9.385  37.944  1.00 18.85  ? 99  TRP   B HD1  1 
ATOM   4142 H HE1  . TRP   B 1 119 ? 34.339 -7.369  39.104  1.00 18.00  ? 99  TRP   B HE1  1 
ATOM   4143 H HE3  . TRP   B 1 119 ? 34.462 -11.230 42.426  1.00 21.04  ? 99  TRP   B HE3  1 
ATOM   4144 H HZ2  . TRP   B 1 119 ? 35.106 -6.656  41.663  1.00 19.95  ? 99  TRP   B HZ2  1 
ATOM   4145 H HZ3  . TRP   B 1 119 ? 35.159 -9.835  44.126  1.00 23.26  ? 99  TRP   B HZ3  1 
ATOM   4146 H HH2  . TRP   B 1 119 ? 35.506 -7.566  43.736  1.00 22.65  ? 99  TRP   B HH2  1 
ATOM   4147 N N    . PHE   B 1 120 ? 32.881 -11.104 36.237  1.00 15.27  ? 100 PHE   B N    1 
ATOM   4148 C CA   . PHE   B 1 120 ? 33.406 -10.893 34.898  1.00 15.20  ? 100 PHE   B CA   1 
ATOM   4149 C C    . PHE   B 1 120 ? 33.885 -9.460  34.773  1.00 14.59  ? 100 PHE   B C    1 
ATOM   4150 O O    . PHE   B 1 120 ? 33.367 -8.551  35.427  1.00 15.34  ? 100 PHE   B O    1 
ATOM   4151 C CB   . PHE   B 1 120 ? 32.330 -11.100 33.813  1.00 16.07  ? 100 PHE   B CB   1 
ATOM   4152 C CG   . PHE   B 1 120 ? 31.920 -12.531 33.644  1.00 17.13  ? 100 PHE   B CG   1 
ATOM   4153 C CD1  . PHE   B 1 120 ? 31.201 -13.204 34.627  1.00 20.90  ? 100 PHE   B CD1  1 
ATOM   4154 C CD2  . PHE   B 1 120 ? 32.254 -13.213 32.498  1.00 18.99  ? 100 PHE   B CD2  1 
ATOM   4155 C CE1  . PHE   B 1 120 ? 30.859 -14.527 34.460  1.00 23.67  ? 100 PHE   B CE1  1 
ATOM   4156 C CE2  . PHE   B 1 120 ? 31.894 -14.531 32.323  1.00 21.55  ? 100 PHE   B CE2  1 
ATOM   4157 C CZ   . PHE   B 1 120 ? 31.209 -15.175 33.308  1.00 22.34  ? 100 PHE   B CZ   1 
ATOM   4158 H H    . PHE   B 1 120 ? 32.290 -10.517 36.452  1.00 18.33  ? 100 PHE   B H    1 
ATOM   4159 H HA   . PHE   B 1 120 ? 34.137 -11.513 34.753  1.00 18.25  ? 100 PHE   B HA   1 
ATOM   4160 H HB2  . PHE   B 1 120 ? 31.540 -10.592 34.055  1.00 19.29  ? 100 PHE   B HB2  1 
ATOM   4161 H HB3  . PHE   B 1 120 ? 32.678 -10.788 32.964  1.00 19.29  ? 100 PHE   B HB3  1 
ATOM   4162 H HD1  . PHE   B 1 120 ? 30.949 -12.757 35.403  1.00 25.08  ? 100 PHE   B HD1  1 
ATOM   4163 H HD2  . PHE   B 1 120 ? 32.731 -12.777 31.829  1.00 22.79  ? 100 PHE   B HD2  1 
ATOM   4164 H HE1  . PHE   B 1 120 ? 30.393 -14.978 35.127  1.00 28.41  ? 100 PHE   B HE1  1 
ATOM   4165 H HE2  . PHE   B 1 120 ? 32.118 -14.977 31.538  1.00 25.87  ? 100 PHE   B HE2  1 
ATOM   4166 H HZ   . PHE   B 1 120 ? 30.976 -16.069 33.195  1.00 26.81  ? 100 PHE   B HZ   1 
ATOM   4167 N N    . TRP   B 1 121 ? 34.854 -9.271  33.894  1.00 14.34  ? 101 TRP   B N    1 
ATOM   4168 C CA   . TRP   B 1 121 ? 35.293 -7.951  33.485  1.00 13.75  ? 101 TRP   B CA   1 
ATOM   4169 C C    . TRP   B 1 121 ? 35.165 -7.850  31.976  1.00 14.75  ? 101 TRP   B C    1 
ATOM   4170 O O    . TRP   B 1 121 ? 35.295 -8.848  31.269  1.00 16.70  ? 101 TRP   B O    1 
ATOM   4171 C CB   . TRP   B 1 121 ? 36.783 -7.694  33.896  1.00 14.10  ? 101 TRP   B CB   1 
ATOM   4172 C CG   . TRP   B 1 121 ? 36.930 -7.541  35.353  1.00 13.92  ? 101 TRP   B CG   1 
ATOM   4173 C CD1  . TRP   B 1 121 ? 37.131 -8.533  36.269  1.00 15.12  ? 101 TRP   B CD1  1 
ATOM   4174 C CD2  . TRP   B 1 121 ? 36.863 -6.315  36.099  1.00 13.65  ? 101 TRP   B CD2  1 
ATOM   4175 N NE1  . TRP   B 1 121 ? 37.184 -8.012  37.536  1.00 15.38  ? 101 TRP   B NE1  1 
ATOM   4176 C CE2  . TRP   B 1 121 ? 37.009 -6.651  37.468  1.00 14.54  ? 101 TRP   B CE2  1 
ATOM   4177 C CE3  . TRP   B 1 121 ? 36.697 -4.964  35.752  1.00 14.07  ? 101 TRP   B CE3  1 
ATOM   4178 C CZ2  . TRP   B 1 121 ? 36.992 -5.689  38.488  1.00 14.73  ? 101 TRP   B CZ2  1 
ATOM   4179 C CZ3  . TRP   B 1 121 ? 36.704 -4.013  36.768  1.00 13.86  ? 101 TRP   B CZ3  1 
ATOM   4180 C CH2  . TRP   B 1 121 ? 36.849 -4.372  38.110  1.00 14.82  ? 101 TRP   B CH2  1 
ATOM   4181 H H    . TRP   B 1 121 ? 35.283 -9.910  33.510  1.00 17.21  ? 101 TRP   B H    1 
ATOM   4182 H HA   . TRP   B 1 121 ? 34.745 -7.270  33.905  1.00 16.51  ? 101 TRP   B HA   1 
ATOM   4183 H HB2  . TRP   B 1 121 ? 37.327 -8.446  33.612  1.00 16.92  ? 101 TRP   B HB2  1 
ATOM   4184 H HB3  . TRP   B 1 121 ? 37.096 -6.880  33.471  1.00 16.92  ? 101 TRP   B HB3  1 
ATOM   4185 H HD1  . TRP   B 1 121 ? 37.219 -9.436  36.062  1.00 18.14  ? 101 TRP   B HD1  1 
ATOM   4186 H HE1  . TRP   B 1 121 ? 37.308 -8.464  38.257  1.00 18.46  ? 101 TRP   B HE1  1 
ATOM   4187 H HE3  . TRP   B 1 121 ? 36.585 -4.711  34.864  1.00 16.88  ? 101 TRP   B HE3  1 
ATOM   4188 H HZ2  . TRP   B 1 121 ? 37.073 -5.930  39.383  1.00 17.68  ? 101 TRP   B HZ2  1 
ATOM   4189 H HZ3  . TRP   B 1 121 ? 36.609 -3.115  36.548  1.00 16.63  ? 101 TRP   B HZ3  1 
ATOM   4190 H HH2  . TRP   B 1 121 ? 36.850 -3.708  38.761  1.00 17.79  ? 101 TRP   B HH2  1 
ATOM   4191 N N    . VAL   B 1 122 ? 34.892 -6.645  31.483  1.00 14.36  ? 102 VAL   B N    1 
ATOM   4192 C CA   . VAL   B 1 122 ? 34.772 -6.379  30.056  1.00 13.37  ? 102 VAL   B CA   1 
ATOM   4193 C C    . VAL   B 1 122 ? 35.619 -5.160  29.719  1.00 13.31  ? 102 VAL   B C    1 
ATOM   4194 O O    . VAL   B 1 122 ? 35.495 -4.124  30.372  1.00 15.02  ? 102 VAL   B O    1 
ATOM   4195 C CB   . VAL   B 1 122 ? 33.311 -6.143  29.642  1.00 14.62  ? 102 VAL   B CB   1 
ATOM   4196 C CG1  . VAL   B 1 122 ? 33.240 -5.844  28.167  1.00 16.13  ? 102 VAL   B CG1  1 
ATOM   4197 C CG2  . VAL   B 1 122 ? 32.445 -7.340  29.998  1.00 15.89  ? 102 VAL   B CG2  1 
ATOM   4198 H H    . VAL   B 1 122 ? 34.770 -5.947  31.970  1.00 17.23  ? 102 VAL   B H    1 
ATOM   4199 H HA   . VAL   B 1 122 ? 35.116 -7.138  29.560  1.00 16.04  ? 102 VAL   B HA   1 
ATOM   4200 H HB   . VAL   B 1 122 ? 32.961 -5.380  30.129  1.00 17.54  ? 102 VAL   B HB   1 
ATOM   4201 H HG11 . VAL   B 1 122 ? 32.318 -5.913  27.874  1.00 19.36  ? 102 VAL   B HG11 1 
ATOM   4202 H HG12 . VAL   B 1 122 ? 33.571 -4.945  28.011  1.00 19.36  ? 102 VAL   B HG12 1 
ATOM   4203 H HG13 . VAL   B 1 122 ? 33.788 -6.486  27.688  1.00 19.36  ? 102 VAL   B HG13 1 
ATOM   4204 H HG21 . VAL   B 1 122 ? 31.541 -7.181  29.684  1.00 19.07  ? 102 VAL   B HG21 1 
ATOM   4205 H HG22 . VAL   B 1 122 ? 32.809 -8.131  29.570  1.00 19.07  ? 102 VAL   B HG22 1 
ATOM   4206 H HG23 . VAL   B 1 122 ? 32.446 -7.456  30.961  1.00 19.07  ? 102 VAL   B HG23 1 
ATOM   4207 N N    . GLU   B 1 123 ? 36.476 -5.279  28.718  1.00 13.37  ? 103 GLU   B N    1 
ATOM   4208 C CA   . GLU   B 1 123 ? 37.148 -4.133  28.121  1.00 13.27  ? 103 GLU   B CA   1 
ATOM   4209 C C    . GLU   B 1 123 ? 36.460 -3.823  26.801  1.00 14.01  ? 103 GLU   B C    1 
ATOM   4210 O O    . GLU   B 1 123 ? 36.188 -4.725  26.011  1.00 15.28  ? 103 GLU   B O    1 
ATOM   4211 C CB   . GLU   B 1 123 ? 38.644 -4.405  27.901  1.00 13.13  ? 103 GLU   B CB   1 
ATOM   4212 C CG   . GLU   B 1 123 ? 39.348 -3.190  27.304  1.00 15.00  ? 103 GLU   B CG   1 
ATOM   4213 C CD   . GLU   B 1 123 ? 40.852 -3.293  27.200  1.00 16.16  ? 103 GLU   B CD   1 
ATOM   4214 O OE1  . GLU   B 1 123 ? 41.439 -4.391  27.352  1.00 16.19  ? 103 GLU   B OE1  1 
ATOM   4215 O OE2  . GLU   B 1 123 ? 41.462 -2.237  26.916  1.00 17.99  ? 103 GLU   B OE2  1 
ATOM   4216 H H    . GLU   B 1 123 ? 36.690 -6.030  28.358  1.00 16.04  ? 103 GLU   B H    1 
ATOM   4217 H HA   . GLU   B 1 123 ? 37.084 -3.363  28.708  1.00 15.93  ? 103 GLU   B HA   1 
ATOM   4218 H HB2  . GLU   B 1 123 ? 39.060 -4.613  28.752  1.00 15.76  ? 103 GLU   B HB2  1 
ATOM   4219 H HB3  . GLU   B 1 123 ? 38.748 -5.151  27.290  1.00 15.76  ? 103 GLU   B HB3  1 
ATOM   4220 H HG2  . GLU   B 1 123 ? 39.006 -3.049  26.407  1.00 18.00  ? 103 GLU   B HG2  1 
ATOM   4221 H HG3  . GLU   B 1 123 ? 39.150 -2.419  27.858  1.00 18.00  ? 103 GLU   B HG3  1 
ATOM   4222 N N    . CYS   B 1 124 ? 36.149 -2.553  26.563  1.00 13.33  ? 104 CYS   B N    1 
ATOM   4223 C CA   . CYS   B 1 124 ? 35.482 -2.187  25.324  1.00 13.98  ? 104 CYS   B CA   1 
ATOM   4224 C C    . CYS   B 1 124 ? 35.667 -0.701  25.074  1.00 14.22  ? 104 CYS   B C    1 
ATOM   4225 O O    . CYS   B 1 124 ? 36.330 0.015   25.828  1.00 14.80  ? 104 CYS   B O    1 
ATOM   4226 C CB   . CYS   B 1 124 ? 33.976 -2.514  25.407  1.00 14.35  ? 104 CYS   B CB   1 
ATOM   4227 S SG   . CYS   B 1 124 ? 33.064 -1.508  26.611  1.00 15.92  ? 104 CYS   B SG   1 
ATOM   4228 H H    . CYS   B 1 124 ? 36.312 -1.898  27.096  1.00 16.00  ? 104 CYS   B H    1 
ATOM   4229 H HA   . CYS   B 1 124 ? 35.898 -2.681  24.600  1.00 16.78  ? 104 CYS   B HA   1 
ATOM   4230 H HB2  . CYS   B 1 124 ? 33.577 -2.363  24.536  1.00 17.23  ? 104 CYS   B HB2  1 
ATOM   4231 H HB3  . CYS   B 1 124 ? 33.873 -3.444  25.663  1.00 17.23  ? 104 CYS   B HB3  1 
ATOM   4232 H HG   . CYS   B 1 124 ? 31.893 -1.750  26.515  1.00 19.10  ? 104 CYS   B HG   1 
ATOM   4233 N N    . ARG   B 1 125 ? 35.156 -0.267  23.942  1.00 14.52  ? 105 ARG   B N    1 
ATOM   4234 C CA   . ARG   B 1 125 ? 34.962 1.150   23.677  1.00 15.15  ? 105 ARG   B CA   1 
ATOM   4235 C C    . ARG   B 1 125 ? 33.458 1.406   23.579  1.00 16.16  ? 105 ARG   B C    1 
ATOM   4236 O O    . ARG   B 1 125 ? 32.645 0.486   23.543  1.00 16.11  ? 105 ARG   B O    1 
ATOM   4237 C CB   . ARG   B 1 125 ? 35.702 1.583   22.413  1.00 16.71  ? 105 ARG   B CB   1 
ATOM   4238 C CG   . ARG   B 1 125 ? 37.219 1.489   22.554  1.00 18.22  ? 105 ARG   B CG   1 
ATOM   4239 C CD   . ARG   B 1 125 ? 37.914 2.109   21.367  1.00 20.91  ? 105 ARG   B CD   1 
ATOM   4240 N NE   . ARG   B 1 125 ? 37.530 1.450   20.124  1.00 24.38  ? 105 ARG   B NE   1 
ATOM   4241 C CZ   . ARG   B 1 125 ? 37.998 1.767   18.919  1.00 26.53  ? 105 ARG   B CZ   1 
ATOM   4242 N NH1  . ARG   B 1 125 ? 38.891 2.730   18.753  1.00 28.27  ? 105 ARG   B NH1  1 
ATOM   4243 N NH2  . ARG   B 1 125 ? 37.563 1.090   17.852  1.00 26.49  ? 105 ARG   B NH2  1 
ATOM   4244 H H    . ARG   B 1 125 ? 34.908 -0.780  23.298  1.00 17.43  ? 105 ARG   B H    1 
ATOM   4245 H HA   . ARG   B 1 125 ? 35.325 1.691   24.396  1.00 18.18  ? 105 ARG   B HA   1 
ATOM   4246 H HB2  . ARG   B 1 125 ? 35.433 1.010   21.678  1.00 20.05  ? 105 ARG   B HB2  1 
ATOM   4247 H HB3  . ARG   B 1 125 ? 35.476 2.505   22.215  1.00 20.05  ? 105 ARG   B HB3  1 
ATOM   4248 H HG2  . ARG   B 1 125 ? 37.499 1.960   23.354  1.00 21.86  ? 105 ARG   B HG2  1 
ATOM   4249 H HG3  . ARG   B 1 125 ? 37.481 0.556   22.610  1.00 21.86  ? 105 ARG   B HG3  1 
ATOM   4250 H HD2  . ARG   B 1 125 ? 37.670 3.045   21.304  1.00 25.09  ? 105 ARG   B HD2  1 
ATOM   4251 H HD3  . ARG   B 1 125 ? 38.874 2.023   21.474  1.00 25.09  ? 105 ARG   B HD3  1 
ATOM   4252 H HE   . ARG   B 1 125 ? 36.959 0.809   20.174  1.00 29.26  ? 105 ARG   B HE   1 
ATOM   4253 H HH11 . ARG   B 1 125 ? 39.183 3.168   19.433  1.00 33.93  ? 105 ARG   B HH11 1 
ATOM   4254 H HH12 . ARG   B 1 125 ? 39.180 2.918   17.965  1.00 33.93  ? 105 ARG   B HH12 1 
ATOM   4255 H HH21 . ARG   B 1 125 ? 36.987 0.458   17.949  1.00 31.79  ? 105 ARG   B HH21 1 
ATOM   4256 H HH22 . ARG   B 1 125 ? 37.858 1.286   17.069  1.00 31.79  ? 105 ARG   B HH22 1 
ATOM   4257 N N    . GLY   B 1 126 ? 33.079 2.662   23.615  1.00 15.96  ? 106 GLY   B N    1 
ATOM   4258 C CA   . GLY   B 1 126 ? 31.688 3.032   23.408  1.00 16.72  ? 106 GLY   B CA   1 
ATOM   4259 C C    . GLY   B 1 126 ? 31.615 4.352   22.695  1.00 16.60  ? 106 GLY   B C    1 
ATOM   4260 O O    . GLY   B 1 126 ? 32.526 5.189   22.803  1.00 16.89  ? 106 GLY   B O    1 
ATOM   4261 H H    . GLY   B 1 126 ? 33.606 3.327   23.758  1.00 19.15  ? 106 GLY   B H    1 
ATOM   4262 H HA2  . GLY   B 1 126 ? 31.242 2.357   22.873  1.00 20.06  ? 106 GLY   B HA2  1 
ATOM   4263 H HA3  . GLY   B 1 126 ? 31.234 3.108   24.262  1.00 20.06  ? 106 GLY   B HA3  1 
ATOM   4264 N N    . GLU   B 1 127 ? 30.522 4.547   21.963  1.00 17.45  ? 107 GLU   B N    1 
ATOM   4265 C CA   . GLU   B 1 127 ? 30.387 5.802   21.245  1.00 17.77  ? 107 GLU   B CA   1 
ATOM   4266 C C    . GLU   B 1 127 ? 28.937 6.089   20.901  1.00 16.95  ? 107 GLU   B C    1 
ATOM   4267 O O    . GLU   B 1 127 ? 28.110 5.180   20.754  1.00 17.97  ? 107 GLU   B O    1 
ATOM   4268 C CB   . GLU   B 1 127 ? 31.203 5.816   19.955  1.00 19.45  ? 107 GLU   B CB   1 
ATOM   4269 C CG   . GLU   B 1 127 ? 30.846 4.736   18.978  1.00 20.98  ? 107 GLU   B CG   1 
ATOM   4270 C CD   . GLU   B 1 127 ? 31.643 4.867   17.697  1.00 24.82  ? 107 GLU   B CD   1 
ATOM   4271 O OE1  . GLU   B 1 127 ? 31.304 5.766   16.880  1.00 28.36  ? 107 GLU   B OE1  1 
ATOM   4272 O OE2  . GLU   B 1 127 ? 32.638 4.122   17.546  1.00 27.64  ? 107 GLU   B OE2  1 
ATOM   4273 H H    . GLU   B 1 127 ? 29.873 3.989   21.873  1.00 20.94  ? 107 GLU   B H    1 
ATOM   4274 H HA   . GLU   B 1 127 ? 30.699 6.499   21.843  1.00 21.33  ? 107 GLU   B HA   1 
ATOM   4275 H HB2  . GLU   B 1 127 ? 31.066 6.668   19.513  1.00 23.34  ? 107 GLU   B HB2  1 
ATOM   4276 H HB3  . GLU   B 1 127 ? 32.140 5.707   20.182  1.00 23.34  ? 107 GLU   B HB3  1 
ATOM   4277 H HG2  . GLU   B 1 127 ? 31.038 3.870   19.371  1.00 25.18  ? 107 GLU   B HG2  1 
ATOM   4278 H HG3  . GLU   B 1 127 ? 29.903 4.799   18.760  1.00 25.18  ? 107 GLU   B HG3  1 
ATOM   4279 N N    . GLY   B 1 128 ? 28.657 7.374   20.752  1.00 17.73  ? 108 GLY   B N    1 
ATOM   4280 C CA   . GLY   B 1 128 ? 27.357 7.826   20.304  1.00 18.14  ? 108 GLY   B CA   1 
ATOM   4281 C C    . GLY   B 1 128 ? 27.189 9.310   20.514  1.00 18.66  ? 108 GLY   B C    1 
ATOM   4282 O O    . GLY   B 1 128 ? 28.035 9.991   21.097  1.00 18.77  ? 108 GLY   B O    1 
ATOM   4283 H H    . GLY   B 1 128 ? 29.212 8.013   20.907  1.00 21.27  ? 108 GLY   B H    1 
ATOM   4284 H HA2  . GLY   B 1 128 ? 27.253 7.634   19.359  1.00 21.77  ? 108 GLY   B HA2  1 
ATOM   4285 H HA3  . GLY   B 1 128 ? 26.663 7.363   20.799  1.00 21.77  ? 108 GLY   B HA3  1 
ATOM   4286 N N    . ALA   B 1 129 ? 26.060 9.816   20.017  1.00 18.88  ? 109 ALA   B N    1 
ATOM   4287 C CA   . ALA   B 1 129 ? 25.697 11.192  20.309  1.00 20.13  ? 109 ALA   B CA   1 
ATOM   4288 C C    . ALA   B 1 129 ? 25.508 11.356  21.815  1.00 18.59  ? 109 ALA   B C    1 
ATOM   4289 O O    . ALA   B 1 129 ? 25.044 10.444  22.508  1.00 19.43  ? 109 ALA   B O    1 
ATOM   4290 C CB   . ALA   B 1 129 ? 24.386 11.542  19.602  1.00 22.48  ? 109 ALA   B CB   1 
ATOM   4291 H H    . ALA   B 1 129 ? 25.503 9.390   19.520  1.00 22.66  ? 109 ALA   B H    1 
ATOM   4292 H HA   . ALA   B 1 129 ? 26.391 11.795  20.001  1.00 24.16  ? 109 ALA   B HA   1 
ATOM   4293 H HB1  . ALA   B 1 129 ? 24.150 12.459  19.812  1.00 26.98  ? 109 ALA   B HB1  1 
ATOM   4294 H HB2  . ALA   B 1 129 ? 24.508 11.443  18.644  1.00 26.98  ? 109 ALA   B HB2  1 
ATOM   4295 H HB3  . ALA   B 1 129 ? 23.690 10.942  19.911  1.00 26.98  ? 109 ALA   B HB3  1 
ATOM   4296 N N    . ILE   B 1 130 ? 25.864 12.535  22.316  1.00 18.81  ? 110 ILE   B N    1 
ATOM   4297 C CA   . ILE   B 1 130 ? 25.594 12.907  23.700  1.00 18.84  ? 110 ILE   B CA   1 
ATOM   4298 C C    . ILE   B 1 130 ? 24.710 14.146  23.686  1.00 19.48  ? 110 ILE   B C    1 
ATOM   4299 O O    . ILE   B 1 130 ? 25.039 15.149  23.039  1.00 20.79  ? 110 ILE   B O    1 
ATOM   4300 C CB   . ILE   B 1 130 ? 26.878 13.066  24.525  1.00 19.68  ? 110 ILE   B CB   1 
ATOM   4301 C CG1  . ILE   B 1 130 ? 26.556 13.403  25.973  1.00 19.33  ? 110 ILE   B CG1  1 
ATOM   4302 C CG2  . ILE   B 1 130 ? 27.855 14.071  23.902  1.00 20.12  ? 110 ILE   B CG2  1 
ATOM   4303 C CD1  . ILE   B 1 130 ? 27.736 13.306  26.926  1.00 20.03  ? 110 ILE   B CD1  1 
ATOM   4304 H H    . ILE   B 1 130 ? 26.269 13.145  21.866  1.00 22.57  ? 110 ILE   B H    1 
ATOM   4305 H HA   . ILE   B 1 130 ? 25.082 12.210  24.140  1.00 22.61  ? 110 ILE   B HA   1 
ATOM   4306 H HB   . ILE   B 1 130 ? 27.330 12.208  24.516  1.00 23.62  ? 110 ILE   B HB   1 
ATOM   4307 H HG12 . ILE   B 1 130 ? 26.225 14.314  26.011  1.00 23.20  ? 110 ILE   B HG12 1 
ATOM   4308 H HG13 . ILE   B 1 130 ? 25.874 12.790  26.289  1.00 23.20  ? 110 ILE   B HG13 1 
ATOM   4309 H HG21 . ILE   B 1 130 ? 28.662 14.102  24.440  1.00 24.15  ? 110 ILE   B HG21 1 
ATOM   4310 H HG22 . ILE   B 1 130 ? 28.070 13.785  23.000  1.00 24.15  ? 110 ILE   B HG22 1 
ATOM   4311 H HG23 . ILE   B 1 130 ? 27.438 14.946  23.881  1.00 24.15  ? 110 ILE   B HG23 1 
ATOM   4312 H HD11 . ILE   B 1 130 ? 27.420 13.430  27.834  1.00 24.04  ? 110 ILE   B HD11 1 
ATOM   4313 H HD12 . ILE   B 1 130 ? 28.144 12.430  26.835  1.00 24.04  ? 110 ILE   B HD12 1 
ATOM   4314 H HD13 . ILE   B 1 130 ? 28.380 13.996  26.703  1.00 24.04  ? 110 ILE   B HD13 1 
ATOM   4315 N N    . VAL   B 1 131 ? 23.542 14.032  24.319  1.00 19.01  ? 111 VAL   B N    1 
ATOM   4316 C CA   . VAL   B 1 131 ? 22.524 15.087  24.351  1.00 18.93  ? 111 VAL   B CA   1 
ATOM   4317 C C    . VAL   B 1 131 ? 22.240 15.396  25.816  1.00 19.42  ? 111 VAL   B C    1 
ATOM   4318 O O    . VAL   B 1 131 ? 21.156 15.110  26.345  1.00 20.14  ? 111 VAL   B O    1 
ATOM   4319 C CB   . VAL   B 1 131 ? 21.256 14.673  23.588  1.00 21.37  ? 111 VAL   B CB   1 
ATOM   4320 C CG1  . VAL   B 1 131 ? 20.328 15.847  23.404  1.00 21.46  ? 111 VAL   B CG1  1 
ATOM   4321 C CG2  . VAL   B 1 131 ? 21.622 14.062  22.245  1.00 23.56  ? 111 VAL   B CG2  1 
ATOM   4322 H H    . VAL   B 1 131 ? 23.306 13.329  24.754  1.00 22.82  ? 111 VAL   B H    1 
ATOM   4323 H HA   . VAL   B 1 131 ? 22.855 15.890  23.918  1.00 22.72  ? 111 VAL   B HA   1 
ATOM   4324 H HB   . VAL   B 1 131 ? 20.785 14.005  24.110  1.00 25.65  ? 111 VAL   B HB   1 
ATOM   4325 H HG11 . VAL   B 1 131 ? 19.554 15.560  22.894  1.00 25.75  ? 111 VAL   B HG11 1 
ATOM   4326 H HG12 . VAL   B 1 131 ? 20.049 16.169  24.275  1.00 25.75  ? 111 VAL   B HG12 1 
ATOM   4327 H HG13 . VAL   B 1 131 ? 20.797 16.548  22.926  1.00 25.75  ? 111 VAL   B HG13 1 
ATOM   4328 H HG21 . VAL   B 1 131 ? 20.849 14.096  21.661  1.00 28.28  ? 111 VAL   B HG21 1 
ATOM   4329 H HG22 . VAL   B 1 131 ? 22.353 14.568  21.856  1.00 28.28  ? 111 VAL   B HG22 1 
ATOM   4330 H HG23 . VAL   B 1 131 ? 21.894 13.141  22.380  1.00 28.28  ? 111 VAL   B HG23 1 
ATOM   4331 N N    . PHE   B 1 132 ? 23.192 15.987  26.467  1.00 19.38  ? 112 PHE   B N    1 
ATOM   4332 C CA   . PHE   B 1 132 ? 23.192 16.139  27.902  1.00 20.43  ? 112 PHE   B CA   1 
ATOM   4333 C C    . PHE   B 1 132 ? 22.487 17.437  28.254  1.00 23.01  ? 112 PHE   B C    1 
ATOM   4334 O O    . PHE   B 1 132 ? 22.711 18.458  27.595  1.00 24.16  ? 112 PHE   B O    1 
ATOM   4335 C CB   . PHE   B 1 132 ? 24.643 16.191  28.361  1.00 21.73  ? 112 PHE   B CB   1 
ATOM   4336 C CG   . PHE   B 1 132 ? 24.933 15.547  29.705  1.00 22.22  ? 112 PHE   B CG   1 
ATOM   4337 C CD1  . PHE   B 1 132 ? 25.185 14.202  29.825  1.00 26.55  ? 112 PHE   B CD1  1 
ATOM   4338 C CD2  . PHE   B 1 132 ? 24.980 16.339  30.850  1.00 25.62  ? 112 PHE   B CD2  1 
ATOM   4339 C CE1  . PHE   B 1 132 ? 25.505 13.649  31.045  1.00 25.11  ? 112 PHE   B CE1  1 
ATOM   4340 C CE2  . PHE   B 1 132 ? 25.270 15.788  32.094  1.00 27.84  ? 112 PHE   B CE2  1 
ATOM   4341 C CZ   . PHE   B 1 132 ? 25.554 14.439  32.184  1.00 26.37  ? 112 PHE   B CZ   1 
ATOM   4342 H H    . PHE   B 1 132 ? 23.888 16.329  26.093  1.00 23.26  ? 112 PHE   B H    1 
ATOM   4343 H HA   . PHE   B 1 132 ? 22.736 15.414  28.356  1.00 24.52  ? 112 PHE   B HA   1 
ATOM   4344 H HB2  . PHE   B 1 132 ? 25.188 15.735  27.701  1.00 26.07  ? 112 PHE   B HB2  1 
ATOM   4345 H HB3  . PHE   B 1 132 ? 24.909 17.121  28.425  1.00 26.07  ? 112 PHE   B HB3  1 
ATOM   4346 H HD1  . PHE   B 1 132 ? 25.139 13.658  29.072  1.00 31.86  ? 112 PHE   B HD1  1 
ATOM   4347 H HD2  . PHE   B 1 132 ? 24.816 17.252  30.782  1.00 30.75  ? 112 PHE   B HD2  1 
ATOM   4348 H HE1  . PHE   B 1 132 ? 25.691 12.740  31.105  1.00 30.14  ? 112 PHE   B HE1  1 
ATOM   4349 H HE2  . PHE   B 1 132 ? 25.272 16.321  32.856  1.00 33.41  ? 112 PHE   B HE2  1 
ATOM   4350 H HZ   . PHE   B 1 132 ? 25.776 14.063  33.005  1.00 31.64  ? 112 PHE   B HZ   1 
ATOM   4351 N N    . PRO   B 1 133 ? 21.628 17.430  29.264  1.00 23.85  ? 113 PRO   B N    1 
ATOM   4352 C CA   . PRO   B 1 133 ? 20.880 18.648  29.601  1.00 26.05  ? 113 PRO   B CA   1 
ATOM   4353 C C    . PRO   B 1 133 ? 21.784 19.852  29.837  1.00 28.99  ? 113 PRO   B C    1 
ATOM   4354 O O    . PRO   B 1 133 ? 22.691 19.804  30.671  1.00 31.03  ? 113 PRO   B O    1 
ATOM   4355 C CB   . PRO   B 1 133 ? 20.136 18.237  30.876  1.00 25.35  ? 113 PRO   B CB   1 
ATOM   4356 C CG   . PRO   B 1 133 ? 19.895 16.774  30.694  1.00 26.31  ? 113 PRO   B CG   1 
ATOM   4357 C CD   . PRO   B 1 133 ? 21.156 16.264  30.031  1.00 24.74  ? 113 PRO   B CD   1 
ATOM   4358 H HA   . PRO   B 1 133 ? 20.244 18.867  28.902  1.00 31.26  ? 113 PRO   B HA   1 
ATOM   4359 H HB2  . PRO   B 1 133 ? 20.688 18.408  31.655  1.00 30.42  ? 113 PRO   B HB2  1 
ATOM   4360 H HB3  . PRO   B 1 133 ? 19.301 18.725  30.948  1.00 30.42  ? 113 PRO   B HB3  1 
ATOM   4361 H HG2  . PRO   B 1 133 ? 19.757 16.350  31.556  1.00 31.58  ? 113 PRO   B HG2  1 
ATOM   4362 H HG3  . PRO   B 1 133 ? 19.120 16.632  30.127  1.00 31.58  ? 113 PRO   B HG3  1 
ATOM   4363 H HD2  . PRO   B 1 133 ? 21.812 15.998  30.695  1.00 29.69  ? 113 PRO   B HD2  1 
ATOM   4364 H HD3  . PRO   B 1 133 ? 20.959 15.519  29.442  1.00 29.69  ? 113 PRO   B HD3  1 
ATOM   4365 N N    . GLY   B 1 134 ? 21.541 20.922  29.086  1.00 29.17  ? 114 GLY   B N    1 
ATOM   4366 C CA   . GLY   B 1 134 ? 22.242 22.179  29.270  1.00 30.57  ? 114 GLY   B CA   1 
ATOM   4367 C C    . GLY   B 1 134 ? 23.563 22.314  28.534  1.00 29.12  ? 114 GLY   B C    1 
ATOM   4368 O O    . GLY   B 1 134 ? 24.265 23.327  28.722  1.00 29.94  ? 114 GLY   B O    1 
ATOM   4369 H H    . GLY   B 1 134 ? 20.962 20.942  28.451  1.00 35.01  ? 114 GLY   B H    1 
ATOM   4370 H HA2  . GLY   B 1 134 ? 21.666 22.898  28.969  1.00 36.69  ? 114 GLY   B HA2  1 
ATOM   4371 H HA3  . GLY   B 1 134 ? 22.423 22.293  30.216  1.00 36.69  ? 114 GLY   B HA3  1 
ATOM   4372 N N    . TYR   B 1 135 ? 23.923 21.352  27.696  1.00 24.88  ? 115 TYR   B N    1 
ATOM   4373 C CA   . TYR   B 1 135 ? 25.170 21.393  26.947  1.00 24.09  ? 115 TYR   B CA   1 
ATOM   4374 C C    . TYR   B 1 135 ? 24.868 21.229  25.468  1.00 24.96  ? 115 TYR   B C    1 
ATOM   4375 O O    . TYR   B 1 135 ? 23.852 20.635  25.100  1.00 26.35  ? 115 TYR   B O    1 
ATOM   4376 C CB   . TYR   B 1 135 ? 26.109 20.261  27.393  1.00 22.98  ? 115 TYR   B CB   1 
ATOM   4377 C CG   . TYR   B 1 135 ? 26.682 20.463  28.765  1.00 21.67  ? 115 TYR   B CG   1 
ATOM   4378 C CD1  . TYR   B 1 135 ? 26.014 20.015  29.896  1.00 20.77  ? 115 TYR   B CD1  1 
ATOM   4379 C CD2  . TYR   B 1 135 ? 27.889 21.130  28.937  1.00 22.21  ? 115 TYR   B CD2  1 
ATOM   4380 C CE1  . TYR   B 1 135 ? 26.540 20.197  31.164  1.00 20.35  ? 115 TYR   B CE1  1 
ATOM   4381 C CE2  . TYR   B 1 135 ? 28.419 21.342  30.188  1.00 22.07  ? 115 TYR   B CE2  1 
ATOM   4382 C CZ   . TYR   B 1 135 ? 27.744 20.872  31.315  1.00 21.72  ? 115 TYR   B CZ   1 
ATOM   4383 O OH   . TYR   B 1 135 ? 28.284 21.079  32.571  1.00 23.83  ? 115 TYR   B OH   1 
ATOM   4384 H H    . TYR   B 1 135 ? 23.451 20.651  27.542  1.00 29.85  ? 115 TYR   B H    1 
ATOM   4385 H HA   . TYR   B 1 135 ? 25.610 22.245  27.089  1.00 28.91  ? 115 TYR   B HA   1 
ATOM   4386 H HB2  . TYR   B 1 135 ? 25.614 19.427  27.398  1.00 27.58  ? 115 TYR   B HB2  1 
ATOM   4387 H HB3  . TYR   B 1 135 ? 26.849 20.204  26.768  1.00 27.58  ? 115 TYR   B HB3  1 
ATOM   4388 H HD1  . TYR   B 1 135 ? 25.196 19.582  29.800  1.00 24.92  ? 115 TYR   B HD1  1 
ATOM   4389 H HD2  . TYR   B 1 135 ? 28.347 21.441  28.190  1.00 26.65  ? 115 TYR   B HD2  1 
ATOM   4390 H HE1  . TYR   B 1 135 ? 26.090 19.870  31.910  1.00 24.43  ? 115 TYR   B HE1  1 
ATOM   4391 H HE2  . TYR   B 1 135 ? 29.224 21.797  30.282  1.00 26.49  ? 115 TYR   B HE2  1 
ATOM   4392 H HH   . TYR   B 1 135 ? 29.015 21.488  32.506  1.00 28.59  ? 115 TYR   B HH   1 
ATOM   4393 N N    . PRO   B 1 136 ? 25.752 21.699  24.590  1.00 25.33  ? 116 PRO   B N    1 
ATOM   4394 C CA   . PRO   B 1 136 ? 25.517 21.499  23.161  1.00 25.46  ? 116 PRO   B CA   1 
ATOM   4395 C C    . PRO   B 1 136 ? 25.516 20.015  22.833  1.00 23.60  ? 116 PRO   B C    1 
ATOM   4396 O O    . PRO   B 1 136 ? 26.276 19.233  23.409  1.00 22.57  ? 116 PRO   B O    1 
ATOM   4397 C CB   . PRO   B 1 136 ? 26.693 22.223  22.500  1.00 28.15  ? 116 PRO   B CB   1 
ATOM   4398 C CG   . PRO   B 1 136 ? 27.238 23.118  23.541  1.00 28.81  ? 116 PRO   B CG   1 
ATOM   4399 C CD   . PRO   B 1 136 ? 27.007 22.420  24.838  1.00 27.17  ? 116 PRO   B CD   1 
ATOM   4400 H HA   . PRO   B 1 136 ? 24.686 21.910  22.876  1.00 30.55  ? 116 PRO   B HA   1 
ATOM   4401 H HB2  . PRO   B 1 136 ? 27.359 21.577  22.217  1.00 33.79  ? 116 PRO   B HB2  1 
ATOM   4402 H HB3  . PRO   B 1 136 ? 26.379 22.731  21.736  1.00 33.79  ? 116 PRO   B HB3  1 
ATOM   4403 H HG2  . PRO   B 1 136 ? 28.186 23.257  23.390  1.00 34.57  ? 116 PRO   B HG2  1 
ATOM   4404 H HG3  . PRO   B 1 136 ? 26.770 23.967  23.520  1.00 34.57  ? 116 PRO   B HG3  1 
ATOM   4405 H HD2  . PRO   B 1 136 ? 27.729 21.804  25.036  1.00 32.61  ? 116 PRO   B HD2  1 
ATOM   4406 H HD3  . PRO   B 1 136 ? 26.906 23.057  25.563  1.00 32.61  ? 116 PRO   B HD3  1 
ATOM   4407 N N    . ARG   B 1 137 ? 24.661 19.626  21.895  1.00 24.79  ? 117 ARG   B N    1 
ATOM   4408 C CA   . ARG   B 1 137 ? 24.696 18.270  21.373  1.00 26.02  ? 117 ARG   B CA   1 
ATOM   4409 C C    . ARG   B 1 137 ? 26.094 17.975  20.844  1.00 25.62  ? 117 ARG   B C    1 
ATOM   4410 O O    . ARG   B 1 137 ? 26.716 18.805  20.181  1.00 27.06  ? 117 ARG   B O    1 
ATOM   4411 C CB   . ARG   B 1 137 ? 23.669 18.109  20.252  1.00 30.84  ? 117 ARG   B CB   1 
ATOM   4412 C CG   . ARG   B 1 137 ? 23.459 16.670  19.861  0.84 35.71  ? 117 ARG   B CG   1 
ATOM   4413 C CD   . ARG   B 1 137 ? 22.644 16.524  18.594  1.00 40.43  ? 117 ARG   B CD   1 
ATOM   4414 N NE   . ARG   B 1 137 ? 22.390 15.114  18.330  1.00 43.35  ? 117 ARG   B NE   1 
ATOM   4415 C CZ   . ARG   B 1 137 ? 21.254 14.488  18.591  1.00 44.61  ? 117 ARG   B CZ   1 
ATOM   4416 N NH1  . ARG   B 1 137 ? 20.206 15.129  19.091  0.97 45.47  ? 117 ARG   B NH1  1 
ATOM   4417 N NH2  . ARG   B 1 137 ? 21.157 13.188  18.319  0.65 44.53  ? 117 ARG   B NH2  1 
ATOM   4418 H H    . ARG   B 1 137 ? 24.054 20.126  21.547  1.00 29.75  ? 117 ARG   B H    1 
ATOM   4419 H HA   . ARG   B 1 137 ? 24.476 17.636  22.073  1.00 31.23  ? 117 ARG   B HA   1 
ATOM   4420 H HB2  . ARG   B 1 137 ? 22.818 18.467  20.549  1.00 37.01  ? 117 ARG   B HB2  1 
ATOM   4421 H HB3  . ARG   B 1 137 ? 23.977 18.591  19.469  1.00 37.01  ? 117 ARG   B HB3  1 
ATOM   4422 H HG2  . ARG   B 1 137 ? 24.322 16.252  19.712  0.83 42.85  ? 117 ARG   B HG2  1 
ATOM   4423 H HG3  . ARG   B 1 137 ? 22.988 16.213  20.575  0.82 42.85  ? 117 ARG   B HG3  1 
ATOM   4424 H HD2  . ARG   B 1 137 ? 21.794 16.980  18.697  1.00 48.52  ? 117 ARG   B HD2  1 
ATOM   4425 H HD3  . ARG   B 1 137 ? 23.133 16.899  17.845  1.00 48.52  ? 117 ARG   B HD3  1 
ATOM   4426 H HE   . ARG   B 1 137 ? 23.027 14.655  17.978  1.00 52.02  ? 117 ARG   B HE   1 
ATOM   4427 H HH11 . ARG   B 1 137 ? 20.254 15.973  19.253  0.97 54.56  ? 117 ARG   B HH11 1 
ATOM   4428 H HH12 . ARG   B 1 137 ? 19.477 14.702  19.253  0.96 54.56  ? 117 ARG   B HH12 1 
ATOM   4429 H HH21 . ARG   B 1 137 ? 21.826 12.769  17.978  0.65 53.44  ? 117 ARG   B HH21 1 
ATOM   4430 H HH22 . ARG   B 1 137 ? 20.425 12.768  18.483  0.64 53.44  ? 117 ARG   B HH22 1 
ATOM   4431 N N    . GLY   B 1 138 ? 26.600 16.800  21.169  1.00 24.88  ? 118 GLY   B N    1 
ATOM   4432 C CA   . GLY   B 1 138 ? 27.922 16.430  20.739  1.00 26.34  ? 118 GLY   B CA   1 
ATOM   4433 C C    . GLY   B 1 138 ? 28.032 14.969  20.383  1.00 23.58  ? 118 GLY   B C    1 
ATOM   4434 O O    . GLY   B 1 138 ? 27.031 14.238  20.286  1.00 23.90  ? 118 GLY   B O    1 
ATOM   4435 H H    . GLY   B 1 138 ? 26.194 16.203  21.637  1.00 29.86  ? 118 GLY   B H    1 
ATOM   4436 H HA2  . GLY   B 1 138 ? 28.162 16.952  19.958  1.00 31.60  ? 118 GLY   B HA2  1 
ATOM   4437 H HA3  . GLY   B 1 138 ? 28.553 16.618  21.451  1.00 31.60  ? 118 GLY   B HA3  1 
ATOM   4438 N N    . GLN   B 1 139 ? 29.280 14.549  20.180  1.00 22.94  ? 119 GLN   B N    1 
ATOM   4439 C CA   . GLN   B 1 139 ? 29.649 13.162  19.948  1.00 22.36  ? 119 GLN   B CA   1 
ATOM   4440 C C    . GLN   B 1 139 ? 30.615 12.754  21.048  1.00 21.22  ? 119 GLN   B C    1 
ATOM   4441 O O    . GLN   B 1 139 ? 31.597 13.464  21.313  1.00 25.41  ? 119 GLN   B O    1 
ATOM   4442 C CB   . GLN   B 1 139 ? 30.316 12.991  18.576  1.00 26.52  ? 119 GLN   B CB   1 
ATOM   4443 C CG   . GLN   B 1 139 ? 29.309 12.848  17.430  1.00 35.94  ? 119 GLN   B CG   1 
ATOM   4444 C CD   . GLN   B 1 139 ? 28.568 11.495  17.480  1.00 43.22  ? 119 GLN   B CD   1 
ATOM   4445 O OE1  . GLN   B 1 139 ? 29.175 10.434  17.689  1.00 47.76  ? 119 GLN   B OE1  1 
ATOM   4446 N NE2  . GLN   B 1 139 ? 27.264 11.538  17.276  1.00 46.25  ? 119 GLN   B NE2  1 
ATOM   4447 H H    . GLN   B 1 139 ? 29.958 15.077  20.171  1.00 27.53  ? 119 GLN   B H    1 
ATOM   4448 H HA   . GLN   B 1 139 ? 28.865 12.592  19.974  1.00 26.83  ? 119 GLN   B HA   1 
ATOM   4449 H HB2  . GLN   B 1 139 ? 30.866 13.769  18.395  1.00 31.83  ? 119 GLN   B HB2  1 
ATOM   4450 H HB3  . GLN   B 1 139 ? 30.866 12.192  18.591  1.00 31.83  ? 119 GLN   B HB3  1 
ATOM   4451 H HG2  . GLN   B 1 139 ? 28.651 13.558  17.493  1.00 43.13  ? 119 GLN   B HG2  1 
ATOM   4452 H HG3  . GLN   B 1 139 ? 29.779 12.906  16.584  1.00 43.13  ? 119 GLN   B HG3  1 
ATOM   4453 H HE21 . GLN   B 1 139 ? 26.876 12.291  17.126  1.00 55.51  ? 119 GLN   B HE21 1 
ATOM   4454 H HE22 . GLN   B 1 139 ? 26.802 10.813  17.292  1.00 55.51  ? 119 GLN   B HE22 1 
ATOM   4455 N N    . TYR   B 1 140 ? 30.350 11.618  21.671  1.00 18.25  ? 120 TYR   B N    1 
ATOM   4456 C CA   . TYR   B 1 140 ? 31.166 11.093  22.760  1.00 17.09  ? 120 TYR   B CA   1 
ATOM   4457 C C    . TYR   B 1 140 ? 31.714 9.728   22.375  1.00 17.58  ? 120 TYR   B C    1 
ATOM   4458 O O    . TYR   B 1 140 ? 30.968 8.859   21.933  1.00 19.51  ? 120 TYR   B O    1 
ATOM   4459 C CB   . TYR   B 1 140 ? 30.300 11.000  24.019  1.00 17.82  ? 120 TYR   B CB   1 
ATOM   4460 C CG   . TYR   B 1 140 ? 30.945 10.419  25.261  1.00 16.75  ? 120 TYR   B CG   1 
ATOM   4461 C CD1  . TYR   B 1 140 ? 32.280 10.679  25.569  1.00 16.27  ? 120 TYR   B CD1  1 
ATOM   4462 C CD2  . TYR   B 1 140 ? 30.215 9.593   26.130  1.00 16.95  ? 120 TYR   B CD2  1 
ATOM   4463 C CE1  . TYR   B 1 140 ? 32.855 10.142  26.715  1.00 16.64  ? 120 TYR   B CE1  1 
ATOM   4464 C CE2  . TYR   B 1 140 ? 30.783 9.080   27.269  1.00 17.56  ? 120 TYR   B CE2  1 
ATOM   4465 C CZ   . TYR   B 1 140 ? 32.109 9.348   27.543  1.00 17.91  ? 120 TYR   B CZ   1 
ATOM   4466 O OH   . TYR   B 1 140 ? 32.711 8.809   28.665  1.00 19.29  ? 120 TYR   B OH   1 
ATOM   4467 H H    . TYR   B 1 140 ? 29.680 11.115  21.477  1.00 21.90  ? 120 TYR   B H    1 
ATOM   4468 H HA   . TYR   B 1 140 ? 31.931 11.664  22.931  1.00 20.51  ? 120 TYR   B HA   1 
ATOM   4469 H HB2  . TYR   B 1 140 ? 30.007 11.896  24.247  1.00 21.39  ? 120 TYR   B HB2  1 
ATOM   4470 H HB3  . TYR   B 1 140 ? 29.533 10.442  23.813  1.00 21.39  ? 120 TYR   B HB3  1 
ATOM   4471 H HD1  . TYR   B 1 140 ? 32.789 11.215  25.005  1.00 19.53  ? 120 TYR   B HD1  1 
ATOM   4472 H HD2  . TYR   B 1 140 ? 29.330 9.389   25.930  1.00 20.35  ? 120 TYR   B HD2  1 
ATOM   4473 H HE1  . TYR   B 1 140 ? 33.745 10.321  26.918  1.00 19.97  ? 120 TYR   B HE1  1 
ATOM   4474 H HE2  . TYR   B 1 140 ? 30.279 8.557   27.851  1.00 21.08  ? 120 TYR   B HE2  1 
ATOM   4475 H HH   . TYR   B 1 140 ? 32.151 8.367   29.107  1.00 23.15  ? 120 TYR   B HH   1 
ATOM   4476 N N    . ARG   B 1 141 ? 33.018 9.568   22.516  1.00 16.78  ? 121 ARG   B N    1 
ATOM   4477 C CA   . ARG   B 1 141 ? 33.709 8.300   22.318  1.00 17.97  ? 121 ARG   B CA   1 
ATOM   4478 C C    . ARG   B 1 141 ? 34.633 8.091   23.501  1.00 16.74  ? 121 ARG   B C    1 
ATOM   4479 O O    . ARG   B 1 141 ? 35.312 9.023   23.921  1.00 19.21  ? 121 ARG   B O    1 
ATOM   4480 C CB   . ARG   B 1 141 ? 34.566 8.347   21.050  1.00 20.76  ? 121 ARG   B CB   1 
ATOM   4481 C CG   . ARG   B 1 141 ? 33.803 8.621   19.769  1.00 25.70  ? 121 ARG   B CG   1 
ATOM   4482 C CD   . ARG   B 1 141 ? 34.742 8.721   18.559  1.00 33.36  ? 121 ARG   B CD   1 
ATOM   4483 N NE   . ARG   B 1 141 ? 35.640 9.863   18.660  1.00 41.83  ? 121 ARG   B NE   1 
ATOM   4484 C CZ   . ARG   B 1 141 ? 35.330 11.102  18.303  1.00 47.17  ? 121 ARG   B CZ   1 
ATOM   4485 N NH1  . ARG   B 1 141 ? 34.130 11.408  17.828  1.00 47.49  ? 121 ARG   B NH1  1 
ATOM   4486 N NH2  . ARG   B 1 141 ? 36.247 12.060  18.432  1.00 49.86  ? 121 ARG   B NH2  1 
ATOM   4487 H H    . ARG   B 1 141 ? 33.551 10.206  22.735  1.00 20.14  ? 121 ARG   B H    1 
ATOM   4488 H HA   . ARG   B 1 141 ? 33.072 7.571   22.250  1.00 21.57  ? 121 ARG   B HA   1 
ATOM   4489 H HB2  . ARG   B 1 141 ? 35.225 9.052   21.152  1.00 24.91  ? 121 ARG   B HB2  1 
ATOM   4490 H HB3  . ARG   B 1 141 ? 35.010 7.491   20.948  1.00 24.91  ? 121 ARG   B HB3  1 
ATOM   4491 H HG2  . ARG   B 1 141 ? 33.177 7.897   19.608  1.00 30.84  ? 121 ARG   B HG2  1 
ATOM   4492 H HG3  . ARG   B 1 141 ? 33.325 9.461   19.853  1.00 30.84  ? 121 ARG   B HG3  1 
ATOM   4493 H HD2  . ARG   B 1 141 ? 35.280 7.916   18.504  1.00 40.03  ? 121 ARG   B HD2  1 
ATOM   4494 H HD3  . ARG   B 1 141 ? 34.213 8.822   17.752  1.00 40.03  ? 121 ARG   B HD3  1 
ATOM   4495 H HE   . ARG   B 1 141 ? 36.428 9.724   18.974  1.00 50.20  ? 121 ARG   B HE   1 
ATOM   4496 H HH11 . ARG   B 1 141 ? 33.531 10.796  17.745  1.00 56.99  ? 121 ARG   B HH11 1 
ATOM   4497 H HH12 . ARG   B 1 141 ? 33.951 12.218  17.602  1.00 56.99  ? 121 ARG   B HH12 1 
ATOM   4498 H HH21 . ARG   B 1 141 ? 37.027 11.870  18.742  1.00 59.84  ? 121 ARG   B HH21 1 
ATOM   4499 H HH22 . ARG   B 1 141 ? 36.060 12.868  18.204  1.00 59.84  ? 121 ARG   B HH22 1 
ATOM   4500 N N    . ASN   B 1 142 ? 34.677 6.877   24.047  1.00 15.89  ? 122 ASN   B N    1 
ATOM   4501 C CA   . ASN   B 1 142 ? 35.589 6.631   25.159  1.00 15.08  ? 122 ASN   B CA   1 
ATOM   4502 C C    . ASN   B 1 142 ? 35.935 5.143   25.231  1.00 15.15  ? 122 ASN   B C    1 
ATOM   4503 O O    . ASN   B 1 142 ? 35.300 4.293   24.613  1.00 15.61  ? 122 ASN   B O    1 
ATOM   4504 C CB   . ASN   B 1 142 ? 35.011 7.144   26.493  1.00 17.06  ? 122 ASN   B CB   1 
ATOM   4505 C CG   . ASN   B 1 142 ? 36.051 7.666   27.431  1.00 17.64  ? 122 ASN   B CG   1 
ATOM   4506 O OD1  . ASN   B 1 142 ? 37.268 7.492   27.221  1.00 18.07  ? 122 ASN   B OD1  1 
ATOM   4507 N ND2  . ASN   B 1 142 ? 35.594 8.304   28.517  1.00 17.32  ? 122 ASN   B ND2  1 
ATOM   4508 H H    . ASN   B 1 142 ? 34.204 6.203   23.799  1.00 19.07  ? 122 ASN   B H    1 
ATOM   4509 H HA   . ASN   B 1 142 ? 36.419 7.104   24.992  1.00 18.10  ? 122 ASN   B HA   1 
ATOM   4510 H HB2  . ASN   B 1 142 ? 34.389 7.865   26.308  1.00 20.48  ? 122 ASN   B HB2  1 
ATOM   4511 H HB3  . ASN   B 1 142 ? 34.551 6.415   26.936  1.00 20.48  ? 122 ASN   B HB3  1 
ATOM   4512 H HD21 . ASN   B 1 142 ? 36.148 8.625   29.092  1.00 20.79  ? 122 ASN   B HD21 1 
ATOM   4513 H HD22 . ASN   B 1 142 ? 34.748 8.393   28.640  1.00 20.79  ? 122 ASN   B HD22 1 
ATOM   4514 N N    . HIS   B 1 143 ? 36.972 4.874   25.984  1.00 15.25  ? 123 HIS   B N    1 
ATOM   4515 C CA   . HIS   B 1 143 ? 37.356 3.540   26.411  1.00 14.62  ? 123 HIS   B CA   1 
ATOM   4516 C C    . HIS   B 1 143 ? 36.706 3.223   27.758  1.00 13.57  ? 123 HIS   B C    1 
ATOM   4517 O O    . HIS   B 1 143 ? 36.634 4.076   28.632  1.00 14.85  ? 123 HIS   B O    1 
ATOM   4518 C CB   . HIS   B 1 143 ? 38.879 3.466   26.499  1.00 14.99  ? 123 HIS   B CB   1 
ATOM   4519 C CG   . HIS   B 1 143 ? 39.396 2.150   26.953  1.00 15.76  ? 123 HIS   B CG   1 
ATOM   4520 N ND1  . HIS   B 1 143 ? 39.640 1.888   28.277  1.00 16.65  ? 123 HIS   B ND1  1 
ATOM   4521 C CD2  . HIS   B 1 143 ? 39.743 1.037   26.270  1.00 17.86  ? 123 HIS   B CD2  1 
ATOM   4522 C CE1  . HIS   B 1 143 ? 40.119 0.664   28.394  1.00 17.52  ? 123 HIS   B CE1  1 
ATOM   4523 N NE2  . HIS   B 1 143 ? 40.209 0.137   27.187  1.00 17.84  ? 123 HIS   B NE2  1 
ATOM   4524 H H    . HIS   B 1 143 ? 37.506 5.479   26.283  1.00 18.30  ? 123 HIS   B H    1 
ATOM   4525 H HA   . HIS   B 1 143 ? 37.054 2.868   25.780  1.00 17.55  ? 123 HIS   B HA   1 
ATOM   4526 H HB2  . HIS   B 1 143 ? 39.250 3.641   25.620  1.00 17.99  ? 123 HIS   B HB2  1 
ATOM   4527 H HB3  . HIS   B 1 143 ? 39.187 4.137   27.128  1.00 17.99  ? 123 HIS   B HB3  1 
ATOM   4528 H HD2  . HIS   B 1 143 ? 39.677 0.909   25.351  1.00 21.43  ? 123 HIS   B HD2  1 
ATOM   4529 H HE1  . HIS   B 1 143 ? 40.354 0.245   29.191  1.00 21.03  ? 123 HIS   B HE1  1 
ATOM   4530 H HE2  . HIS   B 1 143 ? 40.512 -0.647  27.006  1.00 21.41  ? 123 HIS   B HE2  1 
ATOM   4531 N N    . PHE   B 1 144 ? 36.234 1.987   27.932  1.00 13.86  ? 124 PHE   B N    1 
ATOM   4532 C CA   . PHE   B 1 144 ? 35.570 1.604   29.164  1.00 12.98  ? 124 PHE   B CA   1 
ATOM   4533 C C    . PHE   B 1 144 ? 36.039 0.248   29.672  1.00 13.14  ? 124 PHE   B C    1 
ATOM   4534 O O    . PHE   B 1 144 ? 36.386 -0.663  28.895  1.00 14.32  ? 124 PHE   B O    1 
ATOM   4535 C CB   . PHE   B 1 144 ? 34.047 1.491   28.972  1.00 14.25  ? 124 PHE   B CB   1 
ATOM   4536 C CG   . PHE   B 1 144 ? 33.383 2.781   28.594  1.00 14.60  ? 124 PHE   B CG   1 
ATOM   4537 C CD1  . PHE   B 1 144 ? 33.386 3.205   27.283  1.00 16.60  ? 124 PHE   B CD1  1 
ATOM   4538 C CD2  . PHE   B 1 144 ? 32.722 3.544   29.538  1.00 16.44  ? 124 PHE   B CD2  1 
ATOM   4539 C CE1  . PHE   B 1 144 ? 32.758 4.382   26.923  1.00 17.99  ? 124 PHE   B CE1  1 
ATOM   4540 C CE2  . PHE   B 1 144 ? 32.102 4.737   29.184  1.00 17.94  ? 124 PHE   B CE2  1 
ATOM   4541 C CZ   . PHE   B 1 144 ? 32.119 5.153   27.892  1.00 17.77  ? 124 PHE   B CZ   1 
ATOM   4542 H H    . PHE   B 1 144 ? 36.290 1.358   27.348  1.00 16.64  ? 124 PHE   B H    1 
ATOM   4543 H HA   . PHE   B 1 144 ? 35.799 2.280   29.821  1.00 15.57  ? 124 PHE   B HA   1 
ATOM   4544 H HB2  . PHE   B 1 144 ? 33.870 0.850   28.266  1.00 17.11  ? 124 PHE   B HB2  1 
ATOM   4545 H HB3  . PHE   B 1 144 ? 33.651 1.187   29.803  1.00 17.11  ? 124 PHE   B HB3  1 
ATOM   4546 H HD1  . PHE   B 1 144 ? 33.814 2.694   26.635  1.00 19.92  ? 124 PHE   B HD1  1 
ATOM   4547 H HD2  . PHE   B 1 144 ? 32.691 3.255   30.421  1.00 19.74  ? 124 PHE   B HD2  1 
ATOM   4548 H HE1  . PHE   B 1 144 ? 32.763 4.660   26.036  1.00 21.59  ? 124 PHE   B HE1  1 
ATOM   4549 H HE2  . PHE   B 1 144 ? 31.676 5.250   29.832  1.00 21.53  ? 124 PHE   B HE2  1 
ATOM   4550 H HZ   . PHE   B 1 144 ? 31.704 5.951   27.654  1.00 21.33  ? 124 PHE   B HZ   1 
ATOM   4551 N N    . LEU   B 1 145 ? 35.985 0.106   30.985  1.00 12.89  ? 125 LEU   B N    1 
ATOM   4552 C CA   . LEU   B 1 145 ? 36.058 -1.182  31.669  1.00 12.69  ? 125 LEU   B CA   1 
ATOM   4553 C C    . LEU   B 1 145 ? 34.762 -1.372  32.441  1.00 13.04  ? 125 LEU   B C    1 
ATOM   4554 O O    . LEU   B 1 145 ? 34.301 -0.457  33.113  1.00 14.83  ? 125 LEU   B O    1 
ATOM   4555 C CB   . LEU   B 1 145 ? 37.240 -1.232  32.633  1.00 15.15  ? 125 LEU   B CB   1 
ATOM   4556 C CG   . LEU   B 1 145 ? 38.589 -1.005  31.923  1.00 18.36  ? 125 LEU   B CG   1 
ATOM   4557 C CD1  . LEU   B 1 145 ? 39.697 -0.802  32.863  1.00 19.46  ? 125 LEU   B CD1  1 
ATOM   4558 C CD2  . LEU   B 1 145 ? 38.911 -2.089  30.982  1.00 20.27  ? 125 LEU   B CD2  1 
ATOM   4559 H H    . LEU   B 1 145 ? 35.903 0.768   31.528  1.00 15.47  ? 125 LEU   B H    1 
ATOM   4560 H HA   . LEU   B 1 145 ? 36.166 -1.898  31.022  1.00 15.24  ? 125 LEU   B HA   1 
ATOM   4561 H HB2  . LEU   B 1 145 ? 37.131 -0.540  33.304  1.00 18.18  ? 125 LEU   B HB2  1 
ATOM   4562 H HB3  . LEU   B 1 145 ? 37.265 -2.104  33.058  1.00 18.18  ? 125 LEU   B HB3  1 
ATOM   4563 H HG   . LEU   B 1 145 ? 38.491 -0.186  31.412  1.00 22.03  ? 125 LEU   B HG   1 
ATOM   4564 H HD11 . LEU   B 1 145 ? 40.517 -0.671  32.361  1.00 23.35  ? 125 LEU   B HD11 1 
ATOM   4565 H HD12 . LEU   B 1 145 ? 39.513 -0.020  33.405  1.00 23.35  ? 125 LEU   B HD12 1 
ATOM   4566 H HD13 . LEU   B 1 145 ? 39.778 -1.586  33.429  1.00 23.35  ? 125 LEU   B HD13 1 
ATOM   4567 H HD21 . LEU   B 1 145 ? 39.820 -1.972  30.664  1.00 24.32  ? 125 LEU   B HD21 1 
ATOM   4568 H HD22 . LEU   B 1 145 ? 38.828 -2.940  31.441  1.00 24.32  ? 125 LEU   B HD22 1 
ATOM   4569 H HD23 . LEU   B 1 145 ? 38.292 -2.054  30.236  1.00 24.32  ? 125 LEU   B HD23 1 
ATOM   4570 N N    A HIS   B 1 146 ? 34.167 -2.551  32.337  0.52 13.44  ? 126 HIS   B N    1 
ATOM   4571 N N    B HIS   B 1 146 ? 34.167 -2.552  32.336  0.48 13.47  ? 126 HIS   B N    1 
ATOM   4572 C CA   A HIS   B 1 146 ? 32.993 -2.892  33.120  0.52 13.96  ? 126 HIS   B CA   1 
ATOM   4573 C CA   B HIS   B 1 146 ? 32.992 -2.893  33.119  0.48 13.96  ? 126 HIS   B CA   1 
ATOM   4574 C C    A HIS   B 1 146 ? 33.302 -4.058  34.040  0.52 12.98  ? 126 HIS   B C    1 
ATOM   4575 C C    B HIS   B 1 146 ? 33.301 -4.059  34.039  0.48 13.00  ? 126 HIS   B C    1 
ATOM   4576 O O    A HIS   B 1 146 ? 33.988 -5.006  33.638  0.52 14.09  ? 126 HIS   B O    1 
ATOM   4577 O O    B HIS   B 1 146 ? 33.989 -5.006  33.639  0.48 14.10  ? 126 HIS   B O    1 
ATOM   4578 C CB   A HIS   B 1 146 ? 31.815 -3.321  32.251  0.52 13.99  ? 126 HIS   B CB   1 
ATOM   4579 C CB   B HIS   B 1 146 ? 31.812 -3.320  32.249  0.48 14.02  ? 126 HIS   B CB   1 
ATOM   4580 C CG   A HIS   B 1 146 ? 31.226 -2.243  31.400  0.52 14.40  ? 126 HIS   B CG   1 
ATOM   4581 C CG   B HIS   B 1 146 ? 31.237 -2.242  31.387  0.48 14.43  ? 126 HIS   B CG   1 
ATOM   4582 N ND1  A HIS   B 1 146 ? 30.037 -1.612  31.717  0.52 16.95  ? 126 HIS   B ND1  1 
ATOM   4583 N ND1  B HIS   B 1 146 ? 30.041 -1.613  31.681  0.48 16.99  ? 126 HIS   B ND1  1 
ATOM   4584 C CD2  A HIS   B 1 146 ? 31.595 -1.768  30.190  0.52 17.36  ? 126 HIS   B CD2  1 
ATOM   4585 C CD2  B HIS   B 1 146 ? 31.635 -1.758  30.190  0.48 17.38  ? 126 HIS   B CD2  1 
ATOM   4586 C CE1  A HIS   B 1 146 ? 29.744 -0.747  30.765  0.52 17.98  ? 126 HIS   B CE1  1 
ATOM   4587 C CE1  B HIS   B 1 146 ? 29.767 -0.745  30.725  0.48 17.97  ? 126 HIS   B CE1  1 
ATOM   4588 N NE2  A HIS   B 1 146 ? 30.677 -0.813  29.834  0.52 17.74  ? 126 HIS   B NE2  1 
ATOM   4589 N NE2  B HIS   B 1 146 ? 30.721 -0.807  29.815  0.48 17.74  ? 126 HIS   B NE2  1 
ATOM   4590 H H    A HIS   B 1 146 ? 34.429 -3.178  31.810  0.52 16.13  ? 126 HIS   B H    1 
ATOM   4591 H H    B HIS   B 1 146 ? 34.430 -3.179  31.810  0.48 16.16  ? 126 HIS   B H    1 
ATOM   4592 H HA   A HIS   B 1 146 ? 32.750 -2.105  33.632  0.52 16.76  ? 126 HIS   B HA   1 
ATOM   4593 H HA   B HIS   B 1 146 ? 32.749 -2.106  33.632  0.48 16.75  ? 126 HIS   B HA   1 
ATOM   4594 H HB2  A HIS   B 1 146 ? 32.114 -4.028  31.657  0.52 16.80  ? 126 HIS   B HB2  1 
ATOM   4595 H HB2  B HIS   B 1 146 ? 32.106 -4.034  31.662  0.48 16.82  ? 126 HIS   B HB2  1 
ATOM   4596 H HB3  A HIS   B 1 146 ? 31.111 -3.651  32.830  0.52 16.80  ? 126 HIS   B HB3  1 
ATOM   4597 H HB3  B HIS   B 1 146 ? 31.103 -3.637  32.829  0.48 16.82  ? 126 HIS   B HB3  1 
ATOM   4598 H HD2  A HIS   B 1 146 ? 32.333 -2.037  29.692  0.52 20.84  ? 126 HIS   B HD2  1 
ATOM   4599 H HD2  B HIS   B 1 146 ? 32.387 -2.021  29.710  0.48 20.86  ? 126 HIS   B HD2  1 
ATOM   4600 H HE1  A HIS   B 1 146 ? 29.004 -0.184  30.752  0.52 21.58  ? 126 HIS   B HE1  1 
ATOM   4601 H HE1  B HIS   B 1 146 ? 29.027 -0.184  30.698  0.48 21.57  ? 126 HIS   B HE1  1 
ATOM   4602 H HE2  A HIS   B 1 146 ? 30.704 -0.335  29.120  0.52 21.30  ? 126 HIS   B HE2  1 
ATOM   4603 H HE2  B HIS   B 1 146 ? 30.762 -0.328  29.102  0.48 21.29  ? 126 HIS   B HE2  1 
ATOM   4604 N N    . SER   B 1 147 ? 32.751 -4.008  35.244  1.00 12.59  ? 127 SER   B N    1 
ATOM   4605 C CA   . SER   B 1 147 ? 32.744 -5.119  36.177  1.00 13.29  ? 127 SER   B CA   1 
ATOM   4606 C C    . SER   B 1 147 ? 31.321 -5.625  36.328  1.00 13.33  ? 127 SER   B C    1 
ATOM   4607 O O    . SER   B 1 147 ? 30.403 -4.812  36.520  1.00 13.50  ? 127 SER   B O    1 
ATOM   4608 C CB   . SER   B 1 147 ? 33.232 -4.583  37.527  1.00 13.61  ? 127 SER   B CB   1 
ATOM   4609 O OG   . SER   B 1 147 ? 33.179 -5.550  38.573  1.00 14.44  ? 127 SER   B OG   1 
ATOM   4610 H H    A SER   B 1 147 ? 32.359 -3.309  35.555  0.52 15.11  ? 127 SER   B H    1 
ATOM   4611 H H    B SER   B 1 147 ? 32.360 -3.309  35.555  0.48 15.11  ? 127 SER   B H    1 
ATOM   4612 H HA   . SER   B 1 147 ? 33.298 -5.853  35.867  1.00 15.95  ? 127 SER   B HA   1 
ATOM   4613 H HB2  . SER   B 1 147 ? 34.152 -4.293  37.426  1.00 16.33  ? 127 SER   B HB2  1 
ATOM   4614 H HB3  . SER   B 1 147 ? 32.672 -3.831  37.777  1.00 16.33  ? 127 SER   B HB3  1 
ATOM   4615 H HG   . SER   B 1 147 ? 32.382 -5.765  38.726  1.00 17.33  ? 127 SER   B HG   1 
ATOM   4616 N N    . PHE   B 1 148 ? 31.134 -6.951  36.246  1.00 13.75  ? 128 PHE   B N    1 
ATOM   4617 C CA   . PHE   B 1 148 ? 29.817 -7.585  36.420  1.00 13.93  ? 128 PHE   B CA   1 
ATOM   4618 C C    . PHE   B 1 148 ? 29.919 -8.641  37.505  1.00 13.93  ? 128 PHE   B C    1 
ATOM   4619 O O    . PHE   B 1 148 ? 30.656 -9.605  37.345  1.00 15.51  ? 128 PHE   B O    1 
ATOM   4620 C CB   . PHE   B 1 148 ? 29.321 -8.248  35.141  1.00 14.99  ? 128 PHE   B CB   1 
ATOM   4621 C CG   . PHE   B 1 148 ? 28.992 -7.297  34.024  1.00 14.33  ? 128 PHE   B CG   1 
ATOM   4622 C CD1  . PHE   B 1 148 ? 29.944 -6.908  33.113  1.00 14.38  ? 128 PHE   B CD1  1 
ATOM   4623 C CD2  . PHE   B 1 148 ? 27.710 -6.790  33.872  1.00 14.74  ? 128 PHE   B CD2  1 
ATOM   4624 C CE1  . PHE   B 1 148 ? 29.626 -6.053  32.081  1.00 15.38  ? 128 PHE   B CE1  1 
ATOM   4625 C CE2  . PHE   B 1 148 ? 27.388 -5.949  32.859  1.00 14.86  ? 128 PHE   B CE2  1 
ATOM   4626 C CZ   . PHE   B 1 148 ? 28.330 -5.566  31.955  1.00 15.52  ? 128 PHE   B CZ   1 
ATOM   4627 H H    . PHE   B 1 148 ? 31.765 -7.514  36.086  1.00 16.50  ? 128 PHE   B H    1 
ATOM   4628 H HA   . PHE   B 1 148 ? 29.186 -6.897  36.684  1.00 16.71  ? 128 PHE   B HA   1 
ATOM   4629 H HB2  . PHE   B 1 148 ? 30.010 -8.849  34.819  1.00 17.99  ? 128 PHE   B HB2  1 
ATOM   4630 H HB3  . PHE   B 1 148 ? 28.514 -8.747  35.346  1.00 17.99  ? 128 PHE   B HB3  1 
ATOM   4631 H HD1  . PHE   B 1 148 ? 30.815 -7.225  33.194  1.00 17.25  ? 128 PHE   B HD1  1 
ATOM   4632 H HD2  . PHE   B 1 148 ? 27.052 -7.034  34.483  1.00 17.70  ? 128 PHE   B HD2  1 
ATOM   4633 H HE1  . PHE   B 1 148 ? 30.279 -5.801  31.468  1.00 18.46  ? 128 PHE   B HE1  1 
ATOM   4634 H HE2  . PHE   B 1 148 ? 26.518 -5.631  32.782  1.00 17.83  ? 128 PHE   B HE2  1 
ATOM   4635 H HZ   . PHE   B 1 148 ? 28.110 -4.986  31.262  1.00 18.62  ? 128 PHE   B HZ   1 
ATOM   4636 N N    . ARG   B 1 149 ? 29.146 -8.490  38.580  1.00 14.80  ? 129 ARG   B N    1 
ATOM   4637 C CA   . ARG   B 1 149 ? 29.051 -9.498  39.619  1.00 15.55  ? 129 ARG   B CA   1 
ATOM   4638 C C    . ARG   B 1 149 ? 27.637 -10.050 39.633  1.00 15.22  ? 129 ARG   B C    1 
ATOM   4639 O O    . ARG   B 1 149 ? 26.677 -9.295  39.563  1.00 15.78  ? 129 ARG   B O    1 
ATOM   4640 C CB   . ARG   B 1 149 ? 29.420 -8.933  40.971  1.00 16.31  ? 129 ARG   B CB   1 
ATOM   4641 C CG   . ARG   B 1 149 ? 30.876 -8.471  41.021  1.00 16.44  ? 129 ARG   B CG   1 
ATOM   4642 C CD   . ARG   B 1 149 ? 31.297 -8.049  42.406  1.00 17.70  ? 129 ARG   B CD   1 
ATOM   4643 N NE   . ARG   B 1 149 ? 31.429 -9.199  43.276  1.00 19.32  ? 129 ARG   B NE   1 
ATOM   4644 C CZ   . ARG   B 1 149 ? 31.822 -9.166  44.535  1.00 22.49  ? 129 ARG   B CZ   1 
ATOM   4645 N NH1  . ARG   B 1 149 ? 32.067 -8.022  45.156  1.00 25.39  ? 129 ARG   B NH1  1 
ATOM   4646 N NH2  . ARG   B 1 149 ? 31.999 -10.315 45.181  1.00 24.82  ? 129 ARG   B NH2  1 
ATOM   4647 H H    . ARG   B 1 149 ? 28.660 -7.796  38.727  1.00 17.76  ? 129 ARG   B H    1 
ATOM   4648 H HA   . ARG   B 1 149 ? 29.666 -10.226 39.439  1.00 18.66  ? 129 ARG   B HA   1 
ATOM   4649 H HB2  . ARG   B 1 149 ? 28.852 -8.170  41.163  1.00 19.57  ? 129 ARG   B HB2  1 
ATOM   4650 H HB3  . ARG   B 1 149 ? 29.295 -9.618  41.647  1.00 19.57  ? 129 ARG   B HB3  1 
ATOM   4651 H HG2  . ARG   B 1 149 ? 31.451 -9.201  40.741  1.00 19.74  ? 129 ARG   B HG2  1 
ATOM   4652 H HG3  . ARG   B 1 149 ? 30.990 -7.713  40.427  1.00 19.74  ? 129 ARG   B HG3  1 
ATOM   4653 H HD2  . ARG   B 1 149 ? 32.154 -7.597  42.361  1.00 21.25  ? 129 ARG   B HD2  1 
ATOM   4654 H HD3  . ARG   B 1 149 ? 30.628 -7.455  42.781  1.00 21.25  ? 129 ARG   B HD3  1 
ATOM   4655 H HE   . ARG   B 1 149 ? 31.234 -9.968  42.944  1.00 23.19  ? 129 ARG   B HE   1 
ATOM   4656 H HH11 . ARG   B 1 149 ? 31.971 -7.277  44.737  1.00 30.47  ? 129 ARG   B HH11 1 
ATOM   4657 H HH12 . ARG   B 1 149 ? 32.323 -8.025  45.977  1.00 30.47  ? 129 ARG   B HH12 1 
ATOM   4658 H HH21 . ARG   B 1 149 ? 31.857 -11.061 44.778  1.00 29.79  ? 129 ARG   B HH21 1 
ATOM   4659 H HH22 . ARG   B 1 149 ? 32.255 -10.312 46.002  1.00 29.79  ? 129 ARG   B HH22 1 
ATOM   4660 N N    . PHE   B 1 150 ? 27.528 -11.362 39.745  1.00 16.32  ? 130 PHE   B N    1 
ATOM   4661 C CA   . PHE   B 1 150 ? 26.283 -12.103 39.594  1.00 16.32  ? 130 PHE   B CA   1 
ATOM   4662 C C    . PHE   B 1 150 ? 25.823 -12.733 40.896  1.00 17.74  ? 130 PHE   B C    1 
ATOM   4663 O O    . PHE   B 1 150 ? 26.615 -13.096 41.762  1.00 19.29  ? 130 PHE   B O    1 
ATOM   4664 C CB   . PHE   B 1 150 ? 26.458 -13.211 38.551  1.00 16.29  ? 130 PHE   B CB   1 
ATOM   4665 C CG   . PHE   B 1 150 ? 26.484 -12.705 37.141  1.00 17.57  ? 130 PHE   B CG   1 
ATOM   4666 C CD1  . PHE   B 1 150 ? 27.651 -12.164 36.579  1.00 18.45  ? 130 PHE   B CD1  1 
ATOM   4667 C CD2  . PHE   B 1 150 ? 25.334 -12.720 36.380  1.00 17.95  ? 130 PHE   B CD2  1 
ATOM   4668 C CE1  . PHE   B 1 150 ? 27.627 -11.671 35.277  1.00 18.76  ? 130 PHE   B CE1  1 
ATOM   4669 C CE2  . PHE   B 1 150 ? 25.317 -12.243 35.107  1.00 19.28  ? 130 PHE   B CE2  1 
ATOM   4670 C CZ   . PHE   B 1 150 ? 26.438 -11.694 34.556  1.00 19.63  ? 130 PHE   B CZ   1 
ATOM   4671 H H    . PHE   B 1 150 ? 28.196 -11.876 39.918  1.00 19.59  ? 130 PHE   B H    1 
ATOM   4672 H HA   . PHE   B 1 150 ? 25.591 -11.482 39.319  1.00 19.59  ? 130 PHE   B HA   1 
ATOM   4673 H HB2  . PHE   B 1 150 ? 27.296 -13.669 38.718  1.00 19.55  ? 130 PHE   B HB2  1 
ATOM   4674 H HB3  . PHE   B 1 150 ? 25.718 -13.834 38.629  1.00 19.55  ? 130 PHE   B HB3  1 
ATOM   4675 H HD1  . PHE   B 1 150 ? 28.438 -12.135 37.075  1.00 22.14  ? 130 PHE   B HD1  1 
ATOM   4676 H HD2  . PHE   B 1 150 ? 24.552 -13.064 36.746  1.00 21.54  ? 130 PHE   B HD2  1 
ATOM   4677 H HE1  . PHE   B 1 150 ? 28.401 -11.328 34.891  1.00 22.51  ? 130 PHE   B HE1  1 
ATOM   4678 H HE2  . PHE   B 1 150 ? 24.534 -12.292 34.608  1.00 23.14  ? 130 PHE   B HE2  1 
ATOM   4679 H HZ   . PHE   B 1 150 ? 26.407 -11.335 33.699  1.00 23.56  ? 130 PHE   B HZ   1 
ATOM   4680 N N    . GLU   B 1 151 ? 24.511 -12.883 40.989  1.00 18.28  ? 131 GLU   B N    1 
ATOM   4681 C CA   . GLU   B 1 151 ? 23.866 -13.664 42.047  1.00 18.48  ? 131 GLU   B CA   1 
ATOM   4682 C C    . GLU   B 1 151 ? 22.678 -14.399 41.444  1.00 18.92  ? 131 GLU   B C    1 
ATOM   4683 O O    . GLU   B 1 151 ? 21.800 -13.777 40.846  1.00 19.62  ? 131 GLU   B O    1 
ATOM   4684 C CB   . GLU   B 1 151 ? 23.406 -12.742 43.175  1.00 22.29  ? 131 GLU   B CB   1 
ATOM   4685 C CG   . GLU   B 1 151 ? 22.578 -13.413 44.251  1.00 28.47  ? 131 GLU   B CG   1 
ATOM   4686 C CD   . GLU   B 1 151 ? 22.107 -12.381 45.252  1.00 36.51  ? 131 GLU   B CD   1 
ATOM   4687 O OE1  . GLU   B 1 151 ? 22.957 -11.927 46.040  1.00 39.27  ? 131 GLU   B OE1  1 
ATOM   4688 O OE2  . GLU   B 1 151 ? 20.918 -11.979 45.210  1.00 41.77  ? 131 GLU   B OE2  1 
ATOM   4689 H H    . GLU   B 1 151 ? 23.951 -12.535 40.437  1.00 21.94  ? 131 GLU   B H    1 
ATOM   4690 H HA   . GLU   B 1 151 ? 24.484 -14.321 42.404  1.00 22.18  ? 131 GLU   B HA   1 
ATOM   4691 H HB2  . GLU   B 1 151 ? 24.191 -12.367 43.604  1.00 26.75  ? 131 GLU   B HB2  1 
ATOM   4692 H HB3  . GLU   B 1 151 ? 22.866 -12.033 42.792  1.00 26.75  ? 131 GLU   B HB3  1 
ATOM   4693 H HG2  . GLU   B 1 151 ? 21.802 -13.836 43.850  1.00 34.17  ? 131 GLU   B HG2  1 
ATOM   4694 H HG3  . GLU   B 1 151 ? 23.116 -14.075 44.713  1.00 34.17  ? 131 GLU   B HG3  1 
ATOM   4695 N N    . ASN   B 1 152 ? 22.659 -15.719 41.582  1.00 20.52  ? 132 ASN   B N    1 
ATOM   4696 C CA   . ASN   B 1 152 ? 21.546 -16.553 41.122  1.00 21.39  ? 132 ASN   B CA   1 
ATOM   4697 C C    . ASN   B 1 152 ? 21.130 -16.226 39.690  1.00 20.99  ? 132 ASN   B C    1 
ATOM   4698 O O    . ASN   B 1 152 ? 19.952 -16.069 39.380  1.00 22.59  ? 132 ASN   B O    1 
ATOM   4699 C CB   . ASN   B 1 152 ? 20.357 -16.494 42.081  1.00 23.67  ? 132 ASN   B CB   1 
ATOM   4700 C CG   . ASN   B 1 152 ? 19.326 -17.592 41.803  1.00 25.91  ? 132 ASN   B CG   1 
ATOM   4701 O OD1  . ASN   B 1 152 ? 19.647 -18.634 41.208  1.00 27.51  ? 132 ASN   B OD1  1 
ATOM   4702 N ND2  . ASN   B 1 152 ? 18.093 -17.386 42.260  1.00 26.51  ? 132 ASN   B ND2  1 
ATOM   4703 H H    . ASN   B 1 152 ? 23.293 -16.170 41.948  1.00 24.63  ? 132 ASN   B H    1 
ATOM   4704 H HA   . ASN   B 1 152 ? 21.865 -17.469 41.113  1.00 25.68  ? 132 ASN   B HA   1 
ATOM   4705 H HB2  . ASN   B 1 152 ? 20.677 -16.604 42.991  1.00 28.41  ? 132 ASN   B HB2  1 
ATOM   4706 H HB3  . ASN   B 1 152 ? 19.915 -15.635 41.987  1.00 28.41  ? 132 ASN   B HB3  1 
ATOM   4707 H HD21 . ASN   B 1 152 ? 17.481 -17.976 42.128  1.00 31.81  ? 132 ASN   B HD21 1 
ATOM   4708 H HD22 . ASN   B 1 152 ? 17.908 -16.664 42.689  1.00 31.81  ? 132 ASN   B HD22 1 
ATOM   4709 N N    . GLY   B 1 153 ? 22.115 -16.128 38.803  1.00 20.76  ? 133 GLY   B N    1 
ATOM   4710 C CA   . GLY   B 1 153 ? 21.847 -16.074 37.379  1.00 20.76  ? 133 GLY   B CA   1 
ATOM   4711 C C    . GLY   B 1 153 ? 21.627 -14.698 36.794  1.00 18.29  ? 133 GLY   B C    1 
ATOM   4712 O O    . GLY   B 1 153 ? 21.400 -14.596 35.574  1.00 18.26  ? 133 GLY   B O    1 
ATOM   4713 H H    . GLY   B 1 153 ? 22.950 -16.090 39.007  1.00 24.92  ? 133 GLY   B H    1 
ATOM   4714 H HA2  . GLY   B 1 153 ? 22.599 -16.471 36.911  1.00 24.92  ? 133 GLY   B HA2  1 
ATOM   4715 H HA3  . GLY   B 1 153 ? 21.051 -16.598 37.198  1.00 24.92  ? 133 GLY   B HA3  1 
ATOM   4716 N N    . LEU   B 1 154 ? 21.643 -13.641 37.617  1.00 17.12  ? 134 LEU   B N    1 
ATOM   4717 C CA   . LEU   B 1 154 ? 21.415 -12.276 37.161  1.00 16.21  ? 134 LEU   B CA   1 
ATOM   4718 C C    . LEU   B 1 154 ? 22.473 -11.340 37.743  1.00 17.03  ? 134 LEU   B C    1 
ATOM   4719 O O    . LEU   B 1 154 ? 23.191 -11.679 38.690  1.00 17.05  ? 134 LEU   B O    1 
ATOM   4720 C CB   . LEU   B 1 154 ? 20.001 -11.794 37.532  1.00 17.69  ? 134 LEU   B CB   1 
ATOM   4721 C CG   . LEU   B 1 154 ? 18.880 -12.561 36.840  1.00 19.23  ? 134 LEU   B CG   1 
ATOM   4722 C CD1  . LEU   B 1 154 ? 17.546 -12.233 37.506  1.00 21.93  ? 134 LEU   B CD1  1 
ATOM   4723 C CD2  . LEU   B 1 154 ? 18.811 -12.274 35.363  1.00 19.96  ? 134 LEU   B CD2  1 
ATOM   4724 H H    . LEU   B 1 154 ? 21.788 -13.698 38.462  1.00 20.54  ? 134 LEU   B H    1 
ATOM   4725 H HA   . LEU   B 1 154 ? 21.505 -12.248 36.196  1.00 19.45  ? 134 LEU   B HA   1 
ATOM   4726 H HB2  . LEU   B 1 154 ? 19.880 -11.894 38.489  1.00 21.23  ? 134 LEU   B HB2  1 
ATOM   4727 H HB3  . LEU   B 1 154 ? 19.917 -10.860 37.282  1.00 21.23  ? 134 LEU   B HB3  1 
ATOM   4728 H HG   . LEU   B 1 154 ? 19.062 -13.510 36.930  1.00 23.07  ? 134 LEU   B HG   1 
ATOM   4729 H HD11 . LEU   B 1 154 ? 16.839 -12.720 37.055  1.00 26.32  ? 134 LEU   B HD11 1 
ATOM   4730 H HD12 . LEU   B 1 154 ? 17.585 -12.495 38.439  1.00 26.32  ? 134 LEU   B HD12 1 
ATOM   4731 H HD13 . LEU   B 1 154 ? 17.385 -11.279 37.438  1.00 26.32  ? 134 LEU   B HD13 1 
ATOM   4732 H HD21 . LEU   B 1 154 ? 18.048 -12.739 34.985  1.00 23.95  ? 134 LEU   B HD21 1 
ATOM   4733 H HD22 . LEU   B 1 154 ? 18.714 -11.318 35.231  1.00 23.95  ? 134 LEU   B HD22 1 
ATOM   4734 H HD23 . LEU   B 1 154 ? 19.629 -12.584 34.943  1.00 23.95  ? 134 LEU   B HD23 1 
ATOM   4735 N N    . ILE   B 1 155 ? 22.542 -10.131 37.186  1.00 16.28  ? 135 ILE   B N    1 
ATOM   4736 C CA   . ILE   B 1 155 ? 23.550 -9.158  37.601  1.00 15.59  ? 135 ILE   B CA   1 
ATOM   4737 C C    . ILE   B 1 155 ? 23.148 -8.549  38.938  1.00 16.07  ? 135 ILE   B C    1 
ATOM   4738 O O    . ILE   B 1 155 ? 22.083 -7.939  39.049  1.00 16.96  ? 135 ILE   B O    1 
ATOM   4739 C CB   . ILE   B 1 155 ? 23.740 -8.063  36.550  1.00 15.06  ? 135 ILE   B CB   1 
ATOM   4740 C CG1  . ILE   B 1 155 ? 24.122 -8.659  35.198  1.00 16.40  ? 135 ILE   B CG1  1 
ATOM   4741 C CG2  . ILE   B 1 155 ? 24.786 -7.046  37.048  1.00 15.94  ? 135 ILE   B CG2  1 
ATOM   4742 C CD1  . ILE   B 1 155 ? 23.957 -7.678  34.037  1.00 16.67  ? 135 ILE   B CD1  1 
ATOM   4743 H H    . ILE   B 1 155 ? 22.016 -9.851  36.566  1.00 19.54  ? 135 ILE   B H    1 
ATOM   4744 H HA   . ILE   B 1 155 ? 24.391 -9.626  37.719  1.00 18.71  ? 135 ILE   B HA   1 
ATOM   4745 H HB   . ILE   B 1 155 ? 22.898 -7.599  36.421  1.00 18.07  ? 135 ILE   B HB   1 
ATOM   4746 H HG12 . ILE   B 1 155 ? 25.053 -8.932  35.228  1.00 19.68  ? 135 ILE   B HG12 1 
ATOM   4747 H HG13 . ILE   B 1 155 ? 23.556 -9.427  35.023  1.00 19.68  ? 135 ILE   B HG13 1 
ATOM   4748 H HG21 . ILE   B 1 155 ? 25.043 -6.471  36.311  1.00 19.14  ? 135 ILE   B HG21 1 
ATOM   4749 H HG22 . ILE   B 1 155 ? 24.396 -6.516  37.761  1.00 19.14  ? 135 ILE   B HG22 1 
ATOM   4750 H HG23 . ILE   B 1 155 ? 25.561 -7.526  37.379  1.00 19.14  ? 135 ILE   B HG23 1 
ATOM   4751 H HD11 . ILE   B 1 155 ? 24.178 -8.131  33.207  1.00 20.00  ? 135 ILE   B HD11 1 
ATOM   4752 H HD12 . ILE   B 1 155 ? 23.037 -7.371  34.011  1.00 20.00  ? 135 ILE   B HD12 1 
ATOM   4753 H HD13 . ILE   B 1 155 ? 24.554 -6.925  34.172  1.00 20.00  ? 135 ILE   B HD13 1 
ATOM   4754 N N    . LYS   B 1 156 ? 24.011 -8.688  39.937  1.00 16.25  ? 136 LYS   B N    1 
ATOM   4755 C CA   . LYS   B 1 156 ? 23.864 -8.025  41.226  1.00 16.35  ? 136 LYS   B CA   1 
ATOM   4756 C C    . LYS   B 1 156 ? 24.552 -6.666  41.242  1.00 15.59  ? 136 LYS   B C    1 
ATOM   4757 O O    . LYS   B 1 156 ? 24.074 -5.744  41.912  1.00 17.58  ? 136 LYS   B O    1 
ATOM   4758 C CB   . LYS   B 1 156 ? 24.433 -8.936  42.320  1.00 20.32  ? 136 LYS   B CB   1 
ATOM   4759 C CG   . LYS   B 1 156 ? 24.468 -8.373  43.729  1.00 25.76  ? 136 LYS   B CG   1 
ATOM   4760 C CD   . LYS   B 1 156 ? 23.123 -8.416  44.378  1.00 30.93  ? 136 LYS   B CD   1 
ATOM   4761 C CE   . LYS   B 1 156 ? 23.284 -8.463  45.906  1.00 37.60  ? 136 LYS   B CE   1 
ATOM   4762 N NZ   . LYS   B 1 156 ? 21.976 -8.471  46.606  1.00 42.19  ? 136 LYS   B NZ   1 
ATOM   4763 H H    . LYS   B 1 156 ? 24.715 -9.179  39.892  1.00 19.50  ? 136 LYS   B H    1 
ATOM   4764 H HA   . LYS   B 1 156 ? 22.926 -7.875  41.421  1.00 19.62  ? 136 LYS   B HA   1 
ATOM   4765 H HB2  . LYS   B 1 156 ? 23.892 -9.741  42.350  1.00 24.39  ? 136 LYS   B HB2  1 
ATOM   4766 H HB3  . LYS   B 1 156 ? 25.346 -9.158  42.081  1.00 24.39  ? 136 LYS   B HB3  1 
ATOM   4767 H HG2  . LYS   B 1 156 ? 25.082 -8.897  44.268  1.00 30.92  ? 136 LYS   B HG2  1 
ATOM   4768 H HG3  . LYS   B 1 156 ? 24.761 -7.449  43.697  1.00 30.92  ? 136 LYS   B HG3  1 
ATOM   4769 H HD2  . LYS   B 1 156 ? 22.620 -7.621  44.142  1.00 37.11  ? 136 LYS   B HD2  1 
ATOM   4770 H HD3  . LYS   B 1 156 ? 22.645 -9.209  44.090  1.00 37.11  ? 136 LYS   B HD3  1 
ATOM   4771 H HE2  . LYS   B 1 156 ? 23.763 -9.270  46.151  1.00 45.12  ? 136 LYS   B HE2  1 
ATOM   4772 H HE3  . LYS   B 1 156 ? 23.779 -7.682  46.199  1.00 45.12  ? 136 LYS   B HE3  1 
ATOM   4773 H HZ1  . LYS   B 1 156 ? 22.086 -8.723  47.452  1.00 50.63  ? 136 LYS   B HZ1  1 
ATOM   4774 H HZ2  . LYS   B 1 156 ? 21.618 -7.656  46.591  1.00 50.63  ? 136 LYS   B HZ2  1 
ATOM   4775 H HZ3  . LYS   B 1 156 ? 21.420 -9.038  46.205  1.00 50.63  ? 136 LYS   B HZ3  1 
ATOM   4776 N N    . GLU   B 1 157 ? 25.682 -6.530  40.553  1.00 14.95  ? 137 GLU   B N    1 
ATOM   4777 C CA   . GLU   B 1 157 ? 26.392 -5.250  40.504  1.00 15.20  ? 137 GLU   B CA   1 
ATOM   4778 C C    . GLU   B 1 157 ? 27.119 -5.093  39.175  1.00 14.53  ? 137 GLU   B C    1 
ATOM   4779 O O    . GLU   B 1 157 ? 27.987 -5.904  38.838  1.00 14.69  ? 137 GLU   B O    1 
ATOM   4780 C CB   . GLU   B 1 157 ? 27.405 -5.167  41.644  1.00 16.95  ? 137 GLU   B CB   1 
ATOM   4781 C CG   . GLU   B 1 157 ? 28.101 -3.834  41.734  1.00 17.60  ? 137 GLU   B CG   1 
ATOM   4782 C CD   . GLU   B 1 157 ? 29.280 -3.859  42.670  1.00 19.59  ? 137 GLU   B CD   1 
ATOM   4783 O OE1  . GLU   B 1 157 ? 30.272 -4.539  42.345  1.00 18.75  ? 137 GLU   B OE1  1 
ATOM   4784 O OE2  . GLU   B 1 157 ? 29.234 -3.165  43.708  1.00 23.19  ? 137 GLU   B OE2  1 
ATOM   4785 H H    . GLU   B 1 157 ? 26.058 -7.161  40.106  1.00 17.94  ? 137 GLU   B H    1 
ATOM   4786 H HA   . GLU   B 1 157 ? 25.738 -4.537  40.572  1.00 18.24  ? 137 GLU   B HA   1 
ATOM   4787 H HB2  . GLU   B 1 157 ? 26.945 -5.319  42.484  1.00 20.34  ? 137 GLU   B HB2  1 
ATOM   4788 H HB3  . GLU   B 1 157 ? 28.084 -5.848  41.510  1.00 20.34  ? 137 GLU   B HB3  1 
ATOM   4789 H HG2  . GLU   B 1 157 ? 28.421 -3.584  40.853  1.00 21.12  ? 137 GLU   B HG2  1 
ATOM   4790 H HG3  . GLU   B 1 157 ? 27.473 -3.171  42.060  1.00 21.12  ? 137 GLU   B HG3  1 
ATOM   4791 N N    . GLN   B 1 158 ? 26.786 -4.026  38.460  1.00 14.44  ? 138 GLN   B N    1 
ATOM   4792 C CA   . GLN   B 1 158 ? 27.504 -3.596  37.267  1.00 14.30  ? 138 GLN   B CA   1 
ATOM   4793 C C    . GLN   B 1 158 ? 28.158 -2.260  37.599  1.00 13.32  ? 138 GLN   B C    1 
ATOM   4794 O O    . GLN   B 1 158 ? 27.529 -1.387  38.177  1.00 14.67  ? 138 GLN   B O    1 
ATOM   4795 C CB   . GLN   B 1 158 ? 26.518 -3.448  36.105  1.00 15.21  ? 138 GLN   B CB   1 
ATOM   4796 C CG   . GLN   B 1 158 ? 27.139 -2.902  34.818  1.00 16.34  ? 138 GLN   B CG   1 
ATOM   4797 C CD   . GLN   B 1 158 ? 27.123 -1.403  34.731  1.00 18.27  ? 138 GLN   B CD   1 
ATOM   4798 O OE1  . GLN   B 1 158 ? 26.260 -0.752  35.328  1.00 18.49  ? 138 GLN   B OE1  1 
ATOM   4799 N NE2  . GLN   B 1 158 ? 28.060 -0.832  33.975  1.00 20.08  ? 138 GLN   B NE2  1 
ATOM   4800 H H    . GLN   B 1 158 ? 26.121 -3.515  38.653  1.00 17.33  ? 138 GLN   B H    1 
ATOM   4801 H HA   . GLN   B 1 158 ? 28.190 -4.228  37.002  1.00 17.16  ? 138 GLN   B HA   1 
ATOM   4802 H HB2  . GLN   B 1 158 ? 26.144 -4.320  35.903  1.00 18.25  ? 138 GLN   B HB2  1 
ATOM   4803 H HB3  . GLN   B 1 158 ? 25.813 -2.838  36.373  1.00 18.25  ? 138 GLN   B HB3  1 
ATOM   4804 H HG2  . GLN   B 1 158 ? 28.063 -3.192  34.769  1.00 19.61  ? 138 GLN   B HG2  1 
ATOM   4805 H HG3  . GLN   B 1 158 ? 26.642 -3.247  34.060  1.00 19.61  ? 138 GLN   B HG3  1 
ATOM   4806 H HE21 . GLN   B 1 158 ? 28.637 -1.320  33.565  1.00 24.10  ? 138 GLN   B HE21 1 
ATOM   4807 H HE22 . GLN   B 1 158 ? 28.087 0.024   33.898  1.00 24.10  ? 138 GLN   B HE22 1 
ATOM   4808 N N    . ARG   B 1 159 ? 29.426 -2.112  37.243  1.00 13.75  ? 139 ARG   B N    1 
ATOM   4809 C CA   . ARG   B 1 159 ? 30.146 -0.860  37.441  1.00 14.12  ? 139 ARG   B CA   1 
ATOM   4810 C C    . ARG   B 1 159 ? 30.923 -0.557  36.171  1.00 13.32  ? 139 ARG   B C    1 
ATOM   4811 O O    . ARG   B 1 159 ? 31.576 -1.442  35.606  1.00 14.80  ? 139 ARG   B O    1 
ATOM   4812 C CB   . ARG   B 1 159 ? 31.164 -0.964  38.587  1.00 14.51  ? 139 ARG   B CB   1 
ATOM   4813 C CG   . ARG   B 1 159 ? 30.580 -1.364  39.924  1.00 14.55  ? 139 ARG   B CG   1 
ATOM   4814 C CD   . ARG   B 1 159 ? 31.647 -1.528  40.971  1.00 15.21  ? 139 ARG   B CD   1 
ATOM   4815 N NE   . ARG   B 1 159 ? 32.508 -2.677  40.662  1.00 14.71  ? 139 ARG   B NE   1 
ATOM   4816 C CZ   . ARG   B 1 159 ? 33.760 -2.838  41.100  1.00 14.72  ? 139 ARG   B CZ   1 
ATOM   4817 N NH1  . ARG   B 1 159 ? 34.332 -1.966  41.912  1.00 15.42  ? 139 ARG   B NH1  1 
ATOM   4818 N NH2  . ARG   B 1 159 ? 34.462 -3.894  40.697  1.00 14.54  ? 139 ARG   B NH2  1 
ATOM   4819 H H    . ARG   B 1 159 ? 29.899 -2.731  36.880  1.00 16.50  ? 139 ARG   B H    1 
ATOM   4820 H HA   . ARG   B 1 159 ? 29.507 -0.157  37.636  1.00 16.94  ? 139 ARG   B HA   1 
ATOM   4821 H HB2  . ARG   B 1 159 ? 31.828 -1.630  38.348  1.00 17.41  ? 139 ARG   B HB2  1 
ATOM   4822 H HB3  . ARG   B 1 159 ? 31.587 -0.099  38.701  1.00 17.41  ? 139 ARG   B HB3  1 
ATOM   4823 H HG2  . ARG   B 1 159 ? 29.964 -0.677  40.223  1.00 17.47  ? 139 ARG   B HG2  1 
ATOM   4824 H HG3  . ARG   B 1 159 ? 30.114 -2.210  39.831  1.00 17.47  ? 139 ARG   B HG3  1 
ATOM   4825 H HD2  . ARG   B 1 159 ? 32.198 -0.730  41.000  1.00 18.25  ? 139 ARG   B HD2  1 
ATOM   4826 H HD3  . ARG   B 1 159 ? 31.233 -1.677  41.835  1.00 18.25  ? 139 ARG   B HD3  1 
ATOM   4827 H HE   . ARG   B 1 159 ? 32.180 -3.294  40.160  1.00 17.65  ? 139 ARG   B HE   1 
ATOM   4828 H HH11 . ARG   B 1 159 ? 33.897 -1.272  42.173  1.00 18.50  ? 139 ARG   B HH11 1 
ATOM   4829 H HH12 . ARG   B 1 159 ? 35.140 -2.093  42.180  1.00 18.50  ? 139 ARG   B HH12 1 
ATOM   4830 H HH21 . ARG   B 1 159 ? 34.110 -4.465  40.159  1.00 17.45  ? 139 ARG   B HH21 1 
ATOM   4831 H HH22 . ARG   B 1 159 ? 35.269 -4.005  40.974  1.00 17.45  ? 139 ARG   B HH22 1 
ATOM   4832 N N    B GLU   B 1 160 ? 30.905 0.714   35.790  0.47 14.65  ? 140 GLU   B N    1 
ATOM   4833 N N    C GLU   B 1 160 ? 30.861 0.675   35.697  0.53 13.10  ? 140 GLU   B N    1 
ATOM   4834 C CA   B GLU   B 1 160 ? 31.560 1.227   34.595  0.47 16.58  ? 140 GLU   B CA   1 
ATOM   4835 C CA   C GLU   B 1 160 ? 31.686 1.051   34.558  0.53 14.72  ? 140 GLU   B CA   1 
ATOM   4836 C C    B GLU   B 1 160 ? 32.694 2.158   35.007  0.47 15.03  ? 140 GLU   B C    1 
ATOM   4837 C C    C GLU   B 1 160 ? 32.677 2.137   34.942  0.53 13.76  ? 140 GLU   B C    1 
ATOM   4838 O O    B GLU   B 1 160 ? 32.509 2.995   35.894  0.47 14.86  ? 140 GLU   B O    1 
ATOM   4839 O O    C GLU   B 1 160 ? 32.371 3.038   35.729  0.53 14.10  ? 140 GLU   B O    1 
ATOM   4840 C CB   B GLU   B 1 160 ? 30.522 2.010   33.797  0.47 19.94  ? 140 GLU   B CB   1 
ATOM   4841 C CB   C GLU   B 1 160 ? 30.895 1.456   33.324  0.53 17.16  ? 140 GLU   B CB   1 
ATOM   4842 C CG   B GLU   B 1 160 ? 31.049 2.721   32.578  0.47 23.20  ? 140 GLU   B CG   1 
ATOM   4843 C CG   C GLU   B 1 160 ? 30.146 2.705   33.486  0.53 18.99  ? 140 GLU   B CG   1 
ATOM   4844 C CD   B GLU   B 1 160 ? 29.938 3.354   31.814  0.47 25.88  ? 140 GLU   B CD   1 
ATOM   4845 C CD   C GLU   B 1 160 ? 28.774 2.698   32.845  0.53 21.64  ? 140 GLU   B CD   1 
ATOM   4846 O OE1  B GLU   B 1 160 ? 28.915 2.668   31.613  0.47 26.44  ? 140 GLU   B OE1  1 
ATOM   4847 O OE1  C GLU   B 1 160 ? 28.246 1.641   32.418  0.53 20.86  ? 140 GLU   B OE1  1 
ATOM   4848 O OE2  B GLU   B 1 160 ? 30.063 4.527   31.443  0.47 26.87  ? 140 GLU   B OE2  1 
ATOM   4849 O OE2  C GLU   B 1 160 ? 28.194 3.793   32.813  0.53 24.55  ? 140 GLU   B OE2  1 
ATOM   4850 H H    B GLU   B 1 160 ? 30.499 1.331   36.230  0.47 17.58  ? 140 GLU   B H    1 
ATOM   4851 H H    C GLU   B 1 160 ? 30.359 1.300   36.010  0.53 15.72  ? 140 GLU   B H    1 
ATOM   4852 H HA   B GLU   B 1 160 ? 31.937 0.516   34.055  0.47 19.90  ? 140 GLU   B HA   1 
ATOM   4853 H HA   C GLU   B 1 160 ? 32.192 0.263   34.303  0.53 17.67  ? 140 GLU   B HA   1 
ATOM   4854 H HB2  B GLU   B 1 160 ? 29.837 1.392   33.498  0.47 23.93  ? 140 GLU   B HB2  1 
ATOM   4855 H HB2  C GLU   B 1 160 ? 31.510 1.573   32.584  0.53 20.59  ? 140 GLU   B HB2  1 
ATOM   4856 H HB3  B GLU   B 1 160 ? 30.133 2.682   34.378  0.47 23.93  ? 140 GLU   B HB3  1 
ATOM   4857 H HB3  C GLU   B 1 160 ? 30.258 0.753   33.118  0.53 20.59  ? 140 GLU   B HB3  1 
ATOM   4858 H HG2  B GLU   B 1 160 ? 31.670 3.414   32.850  0.47 27.85  ? 140 GLU   B HG2  1 
ATOM   4859 H HG2  C GLU   B 1 160 ? 30.026 2.874   34.433  0.53 22.79  ? 140 GLU   B HG2  1 
ATOM   4860 H HG3  B GLU   B 1 160 ? 31.496 2.083   31.999  0.47 27.85  ? 140 GLU   B HG3  1 
ATOM   4861 H HG3  C GLU   B 1 160 ? 30.654 3.425   33.081  0.53 22.79  ? 140 GLU   B HG3  1 
ATOM   4862 N N    . PHE   B 1 161 ? 33.868 2.021   34.363  1.00 13.54  ? 141 PHE   B N    1 
ATOM   4863 C CA   . PHE   B 1 161 ? 35.018 2.865   34.651  1.00 13.65  ? 141 PHE   B CA   1 
ATOM   4864 C C    . PHE   B 1 161 ? 35.539 3.444   33.343  1.00 13.21  ? 141 PHE   B C    1 
ATOM   4865 O O    . PHE   B 1 161 ? 35.777 2.708   32.380  1.00 15.10  ? 141 PHE   B O    1 
ATOM   4866 C CB   . PHE   B 1 161 ? 36.134 2.045   35.283  1.00 13.82  ? 141 PHE   B CB   1 
ATOM   4867 C CG   . PHE   B 1 161 ? 35.739 1.299   36.518  1.00 14.24  ? 141 PHE   B CG   1 
ATOM   4868 C CD1  . PHE   B 1 161 ? 35.144 0.052   36.456  1.00 15.33  ? 141 PHE   B CD1  1 
ATOM   4869 C CD2  . PHE   B 1 161 ? 35.946 1.865   37.762  1.00 15.34  ? 141 PHE   B CD2  1 
ATOM   4870 C CE1  . PHE   B 1 161 ? 34.824 -0.619  37.638  1.00 15.39  ? 141 PHE   B CE1  1 
ATOM   4871 C CE2  . PHE   B 1 161 ? 35.651 1.212   38.903  1.00 16.47  ? 141 PHE   B CE2  1 
ATOM   4872 C CZ   . PHE   B 1 161 ? 35.057 -0.026  38.845  1.00 16.08  ? 141 PHE   B CZ   1 
ATOM   4873 H H    B PHE   B 1 161 ? 34.014 1.436   33.750  0.47 16.25  ? 141 PHE   B H    1 
ATOM   4874 H H    C PHE   B 1 161 ? 34.043 1.427   33.767  0.53 16.25  ? 141 PHE   B H    1 
ATOM   4875 H HA   . PHE   B 1 161 ? 34.753 3.584   35.247  1.00 16.39  ? 141 PHE   B HA   1 
ATOM   4876 H HB2  . PHE   B 1 161 ? 36.442 1.393   34.634  1.00 16.59  ? 141 PHE   B HB2  1 
ATOM   4877 H HB3  . PHE   B 1 161 ? 36.859 2.643   35.522  1.00 16.59  ? 141 PHE   B HB3  1 
ATOM   4878 H HD1  . PHE   B 1 161 ? 34.958 -0.337  35.632  1.00 18.40  ? 141 PHE   B HD1  1 
ATOM   4879 H HD2  . PHE   B 1 161 ? 36.300 2.724   37.814  1.00 18.41  ? 141 PHE   B HD2  1 
ATOM   4880 H HE1  . PHE   B 1 161 ? 34.453 -1.470  37.603  1.00 18.47  ? 141 PHE   B HE1  1 
ATOM   4881 H HE2  . PHE   B 1 161 ? 35.849 1.596   39.726  1.00 19.77  ? 141 PHE   B HE2  1 
ATOM   4882 H HZ   . PHE   B 1 161 ? 34.812 -0.460  39.630  1.00 19.30  ? 141 PHE   B HZ   1 
ATOM   4883 N N    . MET   B 1 162 ? 35.778 4.749   33.317  1.00 13.18  ? 142 MET   B N    1 
ATOM   4884 C CA   . MET   B 1 162 ? 36.270 5.435   32.134  1.00 13.66  ? 142 MET   B CA   1 
ATOM   4885 C C    . MET   B 1 162 ? 37.100 6.624   32.599  1.00 14.45  ? 142 MET   B C    1 
ATOM   4886 O O    . MET   B 1 162 ? 37.204 6.909   33.790  1.00 15.69  ? 142 MET   B O    1 
ATOM   4887 C CB   . MET   B 1 162 ? 35.146 5.808   31.160  1.00 14.43  ? 142 MET   B CB   1 
ATOM   4888 C CG   . MET   B 1 162 ? 33.967 6.613   31.721  1.00 15.71  ? 142 MET   B CG   1 
ATOM   4889 S SD   . MET   B 1 162 ? 34.460 8.167   32.407  1.00 18.85  ? 142 MET   B SD   1 
ATOM   4890 C CE   . MET   B 1 162 ? 32.969 9.065   32.593  1.00 16.54  ? 142 MET   B CE   1 
ATOM   4891 H H    . MET   B 1 162 ? 35.659 5.271   33.990  1.00 15.82  ? 142 MET   B H    1 
ATOM   4892 H HA   . MET   B 1 162 ? 36.845 4.833   31.637  1.00 16.40  ? 142 MET   B HA   1 
ATOM   4893 H HB2  . MET   B 1 162 ? 35.535 6.339   30.447  1.00 17.31  ? 142 MET   B HB2  1 
ATOM   4894 H HB3  . MET   B 1 162 ? 34.779 4.986   30.799  1.00 17.31  ? 142 MET   B HB3  1 
ATOM   4895 H HG2  . MET   B 1 162 ? 33.335 6.788   31.006  1.00 18.86  ? 142 MET   B HG2  1 
ATOM   4896 H HG3  . MET   B 1 162 ? 33.538 6.098   32.423  1.00 18.86  ? 142 MET   B HG3  1 
ATOM   4897 H HE1  . MET   B 1 162 ? 33.168 9.929   32.987  1.00 19.85  ? 142 MET   B HE1  1 
ATOM   4898 H HE2  . MET   B 1 162 ? 32.562 9.185   31.720  1.00 19.85  ? 142 MET   B HE2  1 
ATOM   4899 H HE3  . MET   B 1 162 ? 32.370 8.567   33.171  1.00 19.85  ? 142 MET   B HE3  1 
ATOM   4900 N N    . ASN   B 1 163 ? 37.710 7.306   31.627  1.00 14.40  ? 143 ASN   B N    1 
ATOM   4901 C CA   . ASN   B 1 163 ? 38.404 8.556   31.868  1.00 13.76  ? 143 ASN   B CA   1 
ATOM   4902 C C    . ASN   B 1 163 ? 37.423 9.703   31.668  1.00 13.98  ? 143 ASN   B C    1 
ATOM   4903 O O    . ASN   B 1 163 ? 37.068 9.995   30.526  1.00 14.29  ? 143 ASN   B O    1 
ATOM   4904 C CB   . ASN   B 1 163 ? 39.544 8.669   30.883  1.00 15.17  ? 143 ASN   B CB   1 
ATOM   4905 C CG   . ASN   B 1 163 ? 40.354 9.903   31.073  1.00 15.64  ? 143 ASN   B CG   1 
ATOM   4906 O OD1  . ASN   B 1 163 ? 40.038 10.792  31.890  1.00 15.20  ? 143 ASN   B OD1  1 
ATOM   4907 N ND2  . ASN   B 1 163 ? 41.450 9.976   30.336  1.00 19.07  ? 143 ASN   B ND2  1 
ATOM   4908 H H    . ASN   B 1 163 ? 37.733 7.054   30.805  1.00 17.28  ? 143 ASN   B H    1 
ATOM   4909 H HA   . ASN   B 1 163 ? 38.741 8.597   32.777  1.00 16.52  ? 143 ASN   B HA   1 
ATOM   4910 H HB2  . ASN   B 1 163 ? 40.132 7.905   30.991  1.00 18.21  ? 143 ASN   B HB2  1 
ATOM   4911 H HB3  . ASN   B 1 163 ? 39.182 8.684   29.983  1.00 18.21  ? 143 ASN   B HB3  1 
ATOM   4912 H HD21 . ASN   B 1 163 ? 41.964 10.663  30.397  1.00 22.89  ? 143 ASN   B HD21 1 
ATOM   4913 H HD22 . ASN   B 1 163 ? 41.649 9.337   29.795  1.00 22.89  ? 143 ASN   B HD22 1 
ATOM   4914 N N    . PRO   B 1 164 ? 36.989 10.398  32.724  1.00 13.66  ? 144 PRO   B N    1 
ATOM   4915 C CA   . PRO   B 1 164 ? 36.001 11.467  32.528  1.00 14.14  ? 144 PRO   B CA   1 
ATOM   4916 C C    . PRO   B 1 164 ? 36.482 12.594  31.650  1.00 13.87  ? 144 PRO   B C    1 
ATOM   4917 O O    . PRO   B 1 164 ? 35.673 13.361  31.126  1.00 15.74  ? 144 PRO   B O    1 
ATOM   4918 C CB   . PRO   B 1 164 ? 35.724 11.937  33.947  1.00 16.13  ? 144 PRO   B CB   1 
ATOM   4919 C CG   . PRO   B 1 164 ? 36.066 10.784  34.827  1.00 15.98  ? 144 PRO   B CG   1 
ATOM   4920 C CD   . PRO   B 1 164 ? 37.264 10.185  34.154  1.00 14.09  ? 144 PRO   B CD   1 
ATOM   4921 H HA   . PRO   B 1 164 ? 35.189 11.101  32.144  1.00 16.97  ? 144 PRO   B HA   1 
ATOM   4922 H HB2  . PRO   B 1 164 ? 36.281 12.705  34.152  1.00 19.35  ? 144 PRO   B HB2  1 
ATOM   4923 H HB3  . PRO   B 1 164 ? 34.788 12.174  34.037  1.00 19.35  ? 144 PRO   B HB3  1 
ATOM   4924 H HG2  . PRO   B 1 164 ? 36.280 11.092  35.721  1.00 19.17  ? 144 PRO   B HG2  1 
ATOM   4925 H HG3  . PRO   B 1 164 ? 35.329 10.154  34.860  1.00 19.17  ? 144 PRO   B HG3  1 
ATOM   4926 H HD2  . PRO   B 1 164 ? 38.075 10.644  34.422  1.00 16.91  ? 144 PRO   B HD2  1 
ATOM   4927 H HD3  . PRO   B 1 164 ? 37.336 9.239   34.355  1.00 16.91  ? 144 PRO   B HD3  1 
ATOM   4928 N N    . CYS   B 1 165 ? 37.791 12.761  31.475  1.00 14.54  ? 145 CYS   B N    1 
ATOM   4929 C CA   . CYS   B 1 165 ? 38.278 13.844  30.634  1.00 15.77  ? 145 CYS   B CA   1 
ATOM   4930 C C    . CYS   B 1 165 ? 37.732 13.773  29.217  1.00 16.24  ? 145 CYS   B C    1 
ATOM   4931 O O    . CYS   B 1 165 ? 37.477 14.828  28.610  1.00 17.84  ? 145 CYS   B O    1 
ATOM   4932 C CB   . CYS   B 1 165 ? 39.792 13.841  30.606  1.00 16.36  ? 145 CYS   B CB   1 
ATOM   4933 S SG   . CYS   B 1 165 ? 40.565 14.225  32.196  1.00 19.04  ? 145 CYS   B SG   1 
ATOM   4934 H H    . CYS   B 1 165 ? 38.404 12.271  31.826  1.00 17.45  ? 145 CYS   B H    1 
ATOM   4935 H HA   . CYS   B 1 165 ? 37.978 14.681  31.022  1.00 18.93  ? 145 CYS   B HA   1 
ATOM   4936 H HB2  . CYS   B 1 165 ? 40.095 12.960  30.337  1.00 19.64  ? 145 CYS   B HB2  1 
ATOM   4937 H HB3  . CYS   B 1 165 ? 40.091 14.505  29.966  1.00 19.64  ? 145 CYS   B HB3  1 
ATOM   4938 H HG   . CYS   B 1 165 ? 41.668 13.755  32.218  1.00 22.85  ? 145 CYS   B HG   1 
ATOM   4939 N N    . GLU   B 1 166 ? 37.472 12.558  28.693  1.00 15.96  ? 146 GLU   B N    1 
ATOM   4940 C CA   . GLU   B 1 166 ? 36.913 12.456  27.342  1.00 16.42  ? 146 GLU   B CA   1 
ATOM   4941 C C    . GLU   B 1 166 ? 35.440 12.857  27.324  1.00 16.36  ? 146 GLU   B C    1 
ATOM   4942 O O    . GLU   B 1 166 ? 34.951 13.381  26.316  1.00 19.07  ? 146 GLU   B O    1 
ATOM   4943 C CB   . GLU   B 1 166 ? 37.080 11.039  26.780  1.00 18.87  ? 146 GLU   B CB   1 
ATOM   4944 C CG   . GLU   B 1 166 ? 38.480 10.542  26.723  1.00 24.38  ? 146 GLU   B CG   1 
ATOM   4945 C CD   . GLU   B 1 166 ? 39.386 11.259  25.771  1.00 33.20  ? 146 GLU   B CD   1 
ATOM   4946 O OE1  . GLU   B 1 166 ? 38.941 12.064  24.937  1.00 33.87  ? 146 GLU   B OE1  1 
ATOM   4947 O OE2  . GLU   B 1 166 ? 40.599 10.950  25.853  1.00 40.02  ? 146 GLU   B OE2  1 
ATOM   4948 H H    . GLU   B 1 166 ? 37.607 11.807  29.090  1.00 19.15  ? 146 GLU   B H    1 
ATOM   4949 H HA   . GLU   B 1 166 ? 37.409 13.056  26.763  1.00 19.71  ? 146 GLU   B HA   1 
ATOM   4950 H HB2  . GLU   B 1 166 ? 36.578 10.426  27.339  1.00 22.65  ? 146 GLU   B HB2  1 
ATOM   4951 H HB3  . GLU   B 1 166 ? 36.731 11.025  25.875  1.00 22.65  ? 146 GLU   B HB3  1 
ATOM   4952 H HG2  . GLU   B 1 166 ? 38.869 10.626  27.608  1.00 29.26  ? 146 GLU   B HG2  1 
ATOM   4953 H HG3  . GLU   B 1 166 ? 38.462 9.610   26.456  1.00 29.26  ? 146 GLU   B HG3  1 
ATOM   4954 N N    . GLN   B 1 167 ? 34.719 12.599  28.411  1.00 15.52  ? 147 GLN   B N    1 
ATOM   4955 C CA   . GLN   B 1 167 ? 33.347 13.090  28.487  1.00 15.86  ? 147 GLN   B CA   1 
ATOM   4956 C C    . GLN   B 1 167 ? 33.321 14.615  28.614  1.00 15.54  ? 147 GLN   B C    1 
ATOM   4957 O O    . GLN   B 1 167 ? 32.483 15.263  27.988  1.00 16.48  ? 147 GLN   B O    1 
ATOM   4958 C CB   . GLN   B 1 167 ? 32.561 12.388  29.595  1.00 16.34  ? 147 GLN   B CB   1 
ATOM   4959 C CG   . GLN   B 1 167 ? 31.039 12.618  29.454  1.00 17.25  ? 147 GLN   B CG   1 
ATOM   4960 C CD   . GLN   B 1 167 ? 30.173 11.750  30.346  1.00 18.17  ? 147 GLN   B CD   1 
ATOM   4961 O OE1  . GLN   B 1 167 ? 30.615 10.739  30.845  1.00 19.55  ? 147 GLN   B OE1  1 
ATOM   4962 N NE2  . GLN   B 1 167 ? 28.903 12.147  30.518  1.00 20.20  ? 147 GLN   B NE2  1 
ATOM   4963 H H    . GLN   B 1 167 ? 34.991 12.156  29.096  1.00 18.63  ? 147 GLN   B H    1 
ATOM   4964 H HA   . GLN   B 1 167 ? 32.885 12.862  27.665  1.00 19.03  ? 147 GLN   B HA   1 
ATOM   4965 H HB2  . GLN   B 1 167 ? 32.730 11.434  29.551  1.00 19.61  ? 147 GLN   B HB2  1 
ATOM   4966 H HB3  . GLN   B 1 167 ? 32.843 12.735  30.456  1.00 19.61  ? 147 GLN   B HB3  1 
ATOM   4967 H HG2  . GLN   B 1 167 ? 30.847 13.543  29.674  1.00 20.70  ? 147 GLN   B HG2  1 
ATOM   4968 H HG3  . GLN   B 1 167 ? 30.784 12.435  28.536  1.00 20.70  ? 147 GLN   B HG3  1 
ATOM   4969 H HE21 . GLN   B 1 167 ? 28.619 12.860  30.131  1.00 24.24  ? 147 GLN   B HE21 1 
ATOM   4970 H HE22 . GLN   B 1 167 ? 28.373 11.687  31.015  1.00 24.24  ? 147 GLN   B HE22 1 
ATOM   4971 N N    . PHE   B 1 168 ? 34.238 15.199  29.390  1.00 15.93  ? 148 PHE   B N    1 
ATOM   4972 C CA   . PHE   B 1 168 ? 34.358 16.658  29.411  1.00 17.52  ? 148 PHE   B CA   1 
ATOM   4973 C C    . PHE   B 1 168 ? 34.509 17.203  27.995  1.00 17.80  ? 148 PHE   B C    1 
ATOM   4974 O O    . PHE   B 1 168 ? 33.799 18.135  27.597  1.00 19.00  ? 148 PHE   B O    1 
ATOM   4975 C CB   . PHE   B 1 168 ? 35.567 17.115  30.248  1.00 18.42  ? 148 PHE   B CB   1 
ATOM   4976 C CG   . PHE   B 1 168 ? 35.545 16.731  31.698  1.00 19.09  ? 148 PHE   B CG   1 
ATOM   4977 C CD1  . PHE   B 1 168 ? 34.386 16.353  32.351  1.00 21.03  ? 148 PHE   B CD1  1 
ATOM   4978 C CD2  . PHE   B 1 168 ? 36.744 16.704  32.405  1.00 19.96  ? 148 PHE   B CD2  1 
ATOM   4979 C CE1  . PHE   B 1 168 ? 34.432 15.973  33.693  1.00 24.01  ? 148 PHE   B CE1  1 
ATOM   4980 C CE2  . PHE   B 1 168 ? 36.800 16.355  33.708  1.00 21.71  ? 148 PHE   B CE2  1 
ATOM   4981 C CZ   . PHE   B 1 168 ? 35.644 15.980  34.373  1.00 24.77  ? 148 PHE   B CZ   1 
ATOM   4982 H H    . PHE   B 1 168 ? 34.790 14.784  29.901  1.00 19.12  ? 148 PHE   B H    1 
ATOM   4983 H HA   . PHE   B 1 168 ? 33.554 17.010  29.825  1.00 21.03  ? 148 PHE   B HA   1 
ATOM   4984 H HB2  . PHE   B 1 168 ? 36.368 16.728  29.861  1.00 22.10  ? 148 PHE   B HB2  1 
ATOM   4985 H HB3  . PHE   B 1 168 ? 35.614 18.083  30.209  1.00 22.10  ? 148 PHE   B HB3  1 
ATOM   4986 H HD1  . PHE   B 1 168 ? 33.575 16.352  31.895  1.00 25.24  ? 148 PHE   B HD1  1 
ATOM   4987 H HD2  . PHE   B 1 168 ? 37.531 16.935  31.966  1.00 23.95  ? 148 PHE   B HD2  1 
ATOM   4988 H HE1  . PHE   B 1 168 ? 33.654 15.715  34.131  1.00 28.82  ? 148 PHE   B HE1  1 
ATOM   4989 H HE2  . PHE   B 1 168 ? 37.613 16.366  34.158  1.00 26.05  ? 148 PHE   B HE2  1 
ATOM   4990 H HZ   . PHE   B 1 168 ? 35.678 15.735  35.269  1.00 29.73  ? 148 PHE   B HZ   1 
ATOM   4991 N N    A ARG   B 1 169 ? 35.438 16.630  27.217  0.49 18.51  ? 149 ARG   B N    1 
ATOM   4992 N N    B ARG   B 1 169 ? 35.438 16.629  27.217  0.51 18.14  ? 149 ARG   B N    1 
ATOM   4993 C CA   A ARG   B 1 169 ? 35.660 17.100  25.855  0.49 20.41  ? 149 ARG   B CA   1 
ATOM   4994 C CA   B ARG   B 1 169 ? 35.661 17.098  25.854  0.51 19.70  ? 149 ARG   B CA   1 
ATOM   4995 C C    A ARG   B 1 169 ? 34.392 17.008  25.018  0.49 19.88  ? 149 ARG   B C    1 
ATOM   4996 C C    B ARG   B 1 169 ? 34.391 17.010  25.021  0.51 19.63  ? 149 ARG   B C    1 
ATOM   4997 O O    A ARG   B 1 169 ? 34.082 17.926  24.248  0.49 20.88  ? 149 ARG   B O    1 
ATOM   4998 O O    B ARG   B 1 169 ? 34.077 17.932  24.258  0.51 20.84  ? 149 ARG   B O    1 
ATOM   4999 C CB   A ARG   B 1 169 ? 36.796 16.321  25.191  0.49 23.03  ? 149 ARG   B CB   1 
ATOM   5000 C CB   B ARG   B 1 169 ? 36.789 16.311  25.185  0.51 21.44  ? 149 ARG   B CB   1 
ATOM   5001 C CG   A ARG   B 1 169 ? 38.173 16.850  25.510  0.49 25.07  ? 149 ARG   B CG   1 
ATOM   5002 C CG   B ARG   B 1 169 ? 38.155 16.575  25.770  0.51 21.79  ? 149 ARG   B CG   1 
ATOM   5003 C CD   A ARG   B 1 169 ? 39.266 16.089  24.760  0.49 27.80  ? 149 ARG   B CD   1 
ATOM   5004 C CD   B ARG   B 1 169 ? 39.270 15.918  24.946  0.51 24.34  ? 149 ARG   B CD   1 
ATOM   5005 N NE   A ARG   B 1 169 ? 39.711 14.927  25.518  0.49 30.39  ? 149 ARG   B NE   1 
ATOM   5006 N NE   B ARG   B 1 169 ? 40.568 16.485  25.288  0.51 26.72  ? 149 ARG   B NE   1 
ATOM   5007 C CZ   A ARG   B 1 169 ? 40.673 14.951  26.433  0.49 32.17  ? 149 ARG   B CZ   1 
ATOM   5008 C CZ   B ARG   B 1 169 ? 41.320 16.101  26.309  0.51 29.41  ? 149 ARG   B CZ   1 
ATOM   5009 N NH1  A ARG   B 1 169 ? 41.330 16.065  26.717  0.49 34.56  ? 149 ARG   B NH1  1 
ATOM   5010 N NH1  B ARG   B 1 169 ? 40.981 15.079  27.074  0.51 30.53  ? 149 ARG   B NH1  1 
ATOM   5011 N NH2  A ARG   B 1 169 ? 40.962 13.835  27.099  0.49 31.20  ? 149 ARG   B NH2  1 
ATOM   5012 N NH2  B ARG   B 1 169 ? 42.445 16.756  26.567  0.51 28.49  ? 149 ARG   B NH2  1 
ATOM   5013 H H    A ARG   B 1 169 ? 35.944 15.977  27.456  0.49 22.21  ? 149 ARG   B H    1 
ATOM   5014 H H    B ARG   B 1 169 ? 35.943 15.975  27.456  0.51 21.77  ? 149 ARG   B H    1 
ATOM   5015 H HA   A ARG   B 1 169 ? 35.927 18.032  25.898  0.49 24.49  ? 149 ARG   B HA   1 
ATOM   5016 H HA   B ARG   B 1 169 ? 35.934 18.027  25.899  0.51 23.64  ? 149 ARG   B HA   1 
ATOM   5017 H HB2  A ARG   B 1 169 ? 36.757 15.399  25.491  0.49 27.64  ? 149 ARG   B HB2  1 
ATOM   5018 H HB2  B ARG   B 1 169 ? 36.605 15.363  25.281  0.51 25.74  ? 149 ARG   B HB2  1 
ATOM   5019 H HB3  A ARG   B 1 169 ? 36.680 16.361  24.229  0.49 27.64  ? 149 ARG   B HB3  1 
ATOM   5020 H HB3  B ARG   B 1 169 ? 36.819 16.550  24.246  0.51 25.74  ? 149 ARG   B HB3  1 
ATOM   5021 H HG2  A ARG   B 1 169 ? 38.224 17.784  25.253  0.49 30.09  ? 149 ARG   B HG2  1 
ATOM   5022 H HG2  B ARG   B 1 169 ? 38.315 17.531  25.788  0.51 26.15  ? 149 ARG   B HG2  1 
ATOM   5023 H HG3  A ARG   B 1 169 ? 38.339 16.758  26.461  0.49 30.09  ? 149 ARG   B HG3  1 
ATOM   5024 H HG3  B ARG   B 1 169 ? 38.192 16.215  26.670  0.51 26.15  ? 149 ARG   B HG3  1 
ATOM   5025 H HD2  A ARG   B 1 169 ? 38.919 15.784  23.907  0.49 33.37  ? 149 ARG   B HD2  1 
ATOM   5026 H HD2  B ARG   B 1 169 ? 39.291 14.966  25.129  0.51 29.21  ? 149 ARG   B HD2  1 
ATOM   5027 H HD3  A ARG   B 1 169 ? 40.028 16.673  24.619  0.49 33.37  ? 149 ARG   B HD3  1 
ATOM   5028 H HD3  B ARG   B 1 169 ? 39.107 16.071  24.002  0.51 29.21  ? 149 ARG   B HD3  1 
ATOM   5029 H HE   A ARG   B 1 169 ? 39.324 14.175  25.362  0.49 36.47  ? 149 ARG   B HE   1 
ATOM   5030 H HE   B ARG   B 1 169 ? 40.869 17.117  24.789  0.51 32.07  ? 149 ARG   B HE   1 
ATOM   5031 H HH11 A ARG   B 1 169 ? 41.137 16.795  26.305  0.49 41.48  ? 149 ARG   B HH11 1 
ATOM   5032 H HH11 B ARG   B 1 169 ? 40.257 14.644  26.915  0.51 36.63  ? 149 ARG   B HH11 1 
ATOM   5033 H HH12 A ARG   B 1 169 ? 41.950 16.059  27.313  0.49 41.48  ? 149 ARG   B HH12 1 
ATOM   5034 H HH12 B ARG   B 1 169 ? 41.486 14.849  27.732  0.51 36.63  ? 149 ARG   B HH12 1 
ATOM   5035 H HH21 A ARG   B 1 169 ? 40.528 13.111  26.934  0.49 37.44  ? 149 ARG   B HH21 1 
ATOM   5036 H HH21 B ARG   B 1 169 ? 42.678 17.421  26.073  0.51 34.18  ? 149 ARG   B HH21 1 
ATOM   5037 H HH22 A ARG   B 1 169 ? 41.583 13.838  27.694  0.49 37.44  ? 149 ARG   B HH22 1 
ATOM   5038 H HH22 B ARG   B 1 169 ? 42.940 16.516  27.227  0.51 34.18  ? 149 ARG   B HH22 1 
ATOM   5039 N N    . SER   B 1 170 ? 33.635 15.915  25.166  1.00 19.22  ? 150 SER   B N    1 
ATOM   5040 C CA   . SER   B 1 170 ? 32.416 15.759  24.374  1.00 19.48  ? 150 SER   B CA   1 
ATOM   5041 C C    . SER   B 1 170 ? 31.381 16.829  24.674  1.00 19.56  ? 150 SER   B C    1 
ATOM   5042 O O    . SER   B 1 170 ? 30.535 17.096  23.814  1.00 21.65  ? 150 SER   B O    1 
ATOM   5043 C CB   . SER   B 1 170 ? 31.797 14.378  24.590  1.00 19.63  ? 150 SER   B CB   1 
ATOM   5044 O OG   . SER   B 1 170 ? 31.073 14.250  25.812  1.00 20.16  ? 150 SER   B OG   1 
ATOM   5045 H H    A SER   B 1 170 ? 33.802 15.267  25.705  0.49 23.06  ? 150 SER   B H    1 
ATOM   5046 H H    B SER   B 1 170 ? 33.803 15.265  25.703  0.51 23.06  ? 150 SER   B H    1 
ATOM   5047 H HA   . SER   B 1 170 ? 32.671 15.838  23.441  1.00 23.38  ? 150 SER   B HA   1 
ATOM   5048 H HB2  . SER   B 1 170 ? 31.187 14.202  23.856  1.00 23.56  ? 150 SER   B HB2  1 
ATOM   5049 H HB3  . SER   B 1 170 ? 32.512 13.723  24.591  1.00 23.56  ? 150 SER   B HB3  1 
ATOM   5050 H HG   . SER   B 1 170 ? 31.581 14.403  26.464  1.00 24.19  ? 150 SER   B HG   1 
ATOM   5051 N N    . LEU   B 1 171 ? 31.409 17.398  25.881  1.00 18.09  ? 151 LEU   B N    1 
ATOM   5052 C CA   . LEU   B 1 171 ? 30.490 18.419  26.349  1.00 19.11  ? 151 LEU   B CA   1 
ATOM   5053 C C    . LEU   B 1 171 ? 31.037 19.830  26.180  1.00 20.73  ? 151 LEU   B C    1 
ATOM   5054 O O    . LEU   B 1 171 ? 30.364 20.795  26.569  1.00 22.52  ? 151 LEU   B O    1 
ATOM   5055 C CB   . LEU   B 1 171 ? 30.168 18.177  27.826  1.00 19.74  ? 151 LEU   B CB   1 
ATOM   5056 C CG   . LEU   B 1 171 ? 29.438 16.885  28.148  1.00 19.87  ? 151 LEU   B CG   1 
ATOM   5057 C CD1  . LEU   B 1 171 ? 29.372 16.691  29.641  1.00 22.85  ? 151 LEU   B CD1  1 
ATOM   5058 C CD2  . LEU   B 1 171 ? 28.033 16.869  27.529  1.00 20.66  ? 151 LEU   B CD2  1 
ATOM   5059 H H    . LEU   B 1 171 ? 31.991 17.191  26.480  1.00 21.71  ? 151 LEU   B H    1 
ATOM   5060 H HA   . LEU   B 1 171 ? 29.667 18.357  25.838  1.00 22.94  ? 151 LEU   B HA   1 
ATOM   5061 H HB2  . LEU   B 1 171 ? 31.003 18.165  28.318  1.00 23.69  ? 151 LEU   B HB2  1 
ATOM   5062 H HB3  . LEU   B 1 171 ? 29.610 18.907  28.136  1.00 23.69  ? 151 LEU   B HB3  1 
ATOM   5063 H HG   . LEU   B 1 171 ? 29.926 16.141  27.763  1.00 23.85  ? 151 LEU   B HG   1 
ATOM   5064 H HD11 . LEU   B 1 171 ? 28.915 15.857  29.832  1.00 27.42  ? 151 LEU   B HD11 1 
ATOM   5065 H HD12 . LEU   B 1 171 ? 30.274 16.663  29.996  1.00 27.42  ? 151 LEU   B HD12 1 
ATOM   5066 H HD13 . LEU   B 1 171 ? 28.885 17.432  30.035  1.00 27.42  ? 151 LEU   B HD13 1 
ATOM   5067 H HD21 . LEU   B 1 171 ? 27.561 16.079  27.835  1.00 24.80  ? 151 LEU   B HD21 1 
ATOM   5068 H HD22 . LEU   B 1 171 ? 27.556 17.667  27.806  1.00 24.80  ? 151 LEU   B HD22 1 
ATOM   5069 H HD23 . LEU   B 1 171 ? 28.114 16.852  26.562  1.00 24.80  ? 151 LEU   B HD23 1 
ATOM   5070 N N    . GLY   B 1 172 ? 32.245 19.969  25.642  1.00 20.61  ? 152 GLY   B N    1 
ATOM   5071 C CA   . GLY   B 1 172 ? 32.847 21.282  25.455  1.00 22.28  ? 152 GLY   B CA   1 
ATOM   5072 C C    . GLY   B 1 172 ? 33.426 21.879  26.710  1.00 24.27  ? 152 GLY   B C    1 
ATOM   5073 O O    . GLY   B 1 172 ? 33.687 23.087  26.751  1.00 26.04  ? 152 GLY   B O    1 
ATOM   5074 H H    . GLY   B 1 172 ? 32.737 19.317  25.376  1.00 24.73  ? 152 GLY   B H    1 
ATOM   5075 H HA2  . GLY   B 1 172 ? 33.560 21.210  24.802  1.00 26.74  ? 152 GLY   B HA2  1 
ATOM   5076 H HA3  . GLY   B 1 172 ? 32.172 21.892  25.119  1.00 26.74  ? 152 GLY   B HA3  1 
ATOM   5077 N N    . ILE   B 1 173 ? 33.623 21.069  27.744  1.00 22.99  ? 153 ILE   B N    1 
ATOM   5078 C CA   . ILE   B 1 173 ? 34.169 21.511  29.018  1.00 22.29  ? 153 ILE   B CA   1 
ATOM   5079 C C    . ILE   B 1 173 ? 35.693 21.451  28.901  1.00 22.03  ? 153 ILE   B C    1 
ATOM   5080 O O    . ILE   B 1 173 ? 36.259 20.417  28.497  1.00 22.77  ? 153 ILE   B O    1 
ATOM   5081 C CB   . ILE   B 1 173 ? 33.685 20.576  30.140  1.00 22.00  ? 153 ILE   B CB   1 
ATOM   5082 C CG1  . ILE   B 1 173 ? 32.162 20.665  30.280  1.00 21.42  ? 153 ILE   B CG1  1 
ATOM   5083 C CG2  . ILE   B 1 173 ? 34.376 20.874  31.451  1.00 22.82  ? 153 ILE   B CG2  1 
ATOM   5084 C CD1  . ILE   B 1 173 ? 31.631 19.668  31.243  1.00 21.89  ? 153 ILE   B CD1  1 
ATOM   5085 H H    . ILE   B 1 173 ? 33.442 20.228  27.730  1.00 27.59  ? 153 ILE   B H    1 
ATOM   5086 H HA   . ILE   B 1 173 ? 33.892 22.420  29.216  1.00 26.75  ? 153 ILE   B HA   1 
ATOM   5087 H HB   . ILE   B 1 173 ? 33.920 19.667  29.895  1.00 26.40  ? 153 ILE   B HB   1 
ATOM   5088 H HG12 . ILE   B 1 173 ? 31.923 21.550  30.598  1.00 25.70  ? 153 ILE   B HG12 1 
ATOM   5089 H HG13 . ILE   B 1 173 ? 31.753 20.501  29.417  1.00 25.70  ? 153 ILE   B HG13 1 
ATOM   5090 H HG21 . ILE   B 1 173 ? 34.006 20.301  32.141  1.00 27.39  ? 153 ILE   B HG21 1 
ATOM   5091 H HG22 . ILE   B 1 173 ? 35.326 20.704  31.354  1.00 27.39  ? 153 ILE   B HG22 1 
ATOM   5092 H HG23 . ILE   B 1 173 ? 34.229 21.805  31.681  1.00 27.39  ? 153 ILE   B HG23 1 
ATOM   5093 H HD11 . ILE   B 1 173 ? 30.671 19.593  31.122  1.00 26.27  ? 153 ILE   B HD11 1 
ATOM   5094 H HD12 . ILE   B 1 173 ? 32.053 18.811  31.075  1.00 26.27  ? 153 ILE   B HD12 1 
ATOM   5095 H HD13 . ILE   B 1 173 ? 31.828 19.963  32.145  1.00 26.27  ? 153 ILE   B HD13 1 
ATOM   5096 N N    . GLU   B 1 174 ? 36.368 22.544  29.271  1.00 24.06  ? 154 GLU   B N    1 
ATOM   5097 C CA   . GLU   B 1 174 ? 37.825 22.572  29.256  1.00 25.28  ? 154 GLU   B CA   1 
ATOM   5098 C C    . GLU   B 1 174 ? 38.431 21.556  30.219  1.00 23.48  ? 154 GLU   B C    1 
ATOM   5099 O O    . GLU   B 1 174 ? 38.036 21.456  31.383  1.00 24.15  ? 154 GLU   B O    1 
ATOM   5100 C CB   . GLU   B 1 174 ? 38.288 23.976  29.625  1.00 29.95  ? 154 GLU   B CB   1 
ATOM   5101 C CG   . GLU   B 1 174 ? 37.936 25.019  28.589  1.00 35.43  ? 154 GLU   B CG   1 
ATOM   5102 H H    . GLU   B 1 174 ? 36.003 23.278  29.533  1.00 28.87  ? 154 GLU   B H    1 
ATOM   5103 H HA   . GLU   B 1 174 ? 38.137 22.338  28.368  1.00 30.34  ? 154 GLU   B HA   1 
ATOM   5104 H HB2  . GLU   B 1 174 ? 37.869 24.234  30.461  1.00 35.94  ? 154 GLU   B HB2  1 
ATOM   5105 H HB3  . GLU   B 1 174 ? 39.253 23.971  29.726  1.00 35.94  ? 154 GLU   B HB3  1 
ATOM   5106 N N    . VAL   B 1 175 ? 39.426 20.822  29.747  1.00 22.75  ? 155 VAL   B N    1 
ATOM   5107 C CA   . VAL   B 1 175 ? 40.100 19.803  30.553  1.00 23.05  ? 155 VAL   B CA   1 
ATOM   5108 C C    . VAL   B 1 175 ? 41.382 20.418  31.099  1.00 24.82  ? 155 VAL   B C    1 
ATOM   5109 O O    . VAL   B 1 175 ? 42.157 20.966  30.319  1.00 25.08  ? 155 VAL   B O    1 
ATOM   5110 C CB   . VAL   B 1 175 ? 40.422 18.551  29.728  1.00 24.02  ? 155 VAL   B CB   1 
ATOM   5111 C CG1  . VAL   B 1 175 ? 41.145 17.526  30.597  1.00 25.26  ? 155 VAL   B CG1  1 
ATOM   5112 C CG2  . VAL   B 1 175 ? 39.150 17.972  29.136  1.00 27.01  ? 155 VAL   B CG2  1 
ATOM   5113 H H    . VAL   B 1 175 ? 39.737 20.893  28.948  1.00 27.30  ? 155 VAL   B H    1 
ATOM   5114 H HA   . VAL   B 1 175 ? 39.528 19.545  31.293  1.00 27.66  ? 155 VAL   B HA   1 
ATOM   5115 H HB   . VAL   B 1 175 ? 41.009 18.787  28.992  1.00 28.83  ? 155 VAL   B HB   1 
ATOM   5116 H HG11 . VAL   B 1 175 ? 41.134 16.667  30.147  1.00 30.32  ? 155 VAL   B HG11 1 
ATOM   5117 H HG12 . VAL   B 1 175 ? 42.060 17.817  30.733  1.00 30.32  ? 155 VAL   B HG12 1 
ATOM   5118 H HG13 . VAL   B 1 175 ? 40.689 17.458  31.450  1.00 30.32  ? 155 VAL   B HG13 1 
ATOM   5119 H HG21 . VAL   B 1 175 ? 39.362 17.143  28.680  1.00 32.41  ? 155 VAL   B HG21 1 
ATOM   5120 H HG22 . VAL   B 1 175 ? 38.517 17.804  29.852  1.00 32.41  ? 155 VAL   B HG22 1 
ATOM   5121 H HG23 . VAL   B 1 175 ? 38.776 18.609  28.507  1.00 32.41  ? 155 VAL   B HG23 1 
ATOM   5122 N N    . PRO   B 1 176 ? 41.643 20.329  32.403  1.00 28.91  ? 156 PRO   B N    1 
ATOM   5123 C CA   . PRO   B 1 176 ? 42.916 20.812  32.946  1.00 31.10  ? 156 PRO   B CA   1 
ATOM   5124 C C    . PRO   B 1 176 ? 44.090 20.043  32.356  1.00 28.22  ? 156 PRO   B C    1 
ATOM   5125 O O    . PRO   B 1 176 ? 43.974 18.882  31.969  1.00 26.54  ? 156 PRO   B O    1 
ATOM   5126 C CB   . PRO   B 1 176 ? 42.779 20.522  34.449  1.00 34.83  ? 156 PRO   B CB   1 
ATOM   5127 C CG   . PRO   B 1 176 ? 41.359 20.303  34.701  1.00 36.75  ? 156 PRO   B CG   1 
ATOM   5128 C CD   . PRO   B 1 176 ? 40.772 19.758  33.451  1.00 32.71  ? 156 PRO   B CD   1 
ATOM   5129 H HA   . PRO   B 1 176 ? 43.025 21.764  32.790  1.00 37.33  ? 156 PRO   B HA   1 
ATOM   5130 H HB2  . PRO   B 1 176 ? 43.293 19.730  34.674  1.00 41.80  ? 156 PRO   B HB2  1 
ATOM   5131 H HB3  . PRO   B 1 176 ? 43.103 21.282  34.957  1.00 41.80  ? 156 PRO   B HB3  1 
ATOM   5132 H HG2  . PRO   B 1 176 ? 41.256 19.669  35.429  1.00 44.10  ? 156 PRO   B HG2  1 
ATOM   5133 H HG3  . PRO   B 1 176 ? 40.940 21.146  34.934  1.00 44.10  ? 156 PRO   B HG3  1 
ATOM   5134 H HD2  . PRO   B 1 176 ? 40.810 18.789  33.444  1.00 39.25  ? 156 PRO   B HD2  1 
ATOM   5135 H HD3  . PRO   B 1 176 ? 39.855 20.055  33.341  1.00 39.25  ? 156 PRO   B HD3  1 
ATOM   5136 N N    . GLU   B 1 177 ? 45.229 20.713  32.257  1.00 30.57  ? 157 GLU   B N    1 
ATOM   5137 C CA   . GLU   B 1 177 ? 46.427 20.108  31.694  1.00 31.78  ? 157 GLU   B CA   1 
ATOM   5138 C C    . GLU   B 1 177 ? 47.492 20.072  32.775  1.00 30.18  ? 157 GLU   B C    1 
ATOM   5139 O O    . GLU   B 1 177 ? 47.907 21.124  33.275  1.00 33.50  ? 157 GLU   B O    1 
ATOM   5140 C CB   . GLU   B 1 177 ? 46.909 20.912  30.484  1.00 37.03  ? 157 GLU   B CB   1 
ATOM   5141 C CG   . GLU   B 1 177 ? 48.050 20.259  29.730  1.00 40.91  ? 157 GLU   B CG   1 
ATOM   5142 H H    . GLU   B 1 177 ? 45.334 21.528  32.511  1.00 36.69  ? 157 GLU   B H    1 
ATOM   5143 H HA   . GLU   B 1 177 ? 46.245 19.198  31.411  1.00 38.14  ? 157 GLU   B HA   1 
ATOM   5144 H HB2  . GLU   B 1 177 ? 46.169 21.019  29.867  1.00 44.44  ? 157 GLU   B HB2  1 
ATOM   5145 H HB3  . GLU   B 1 177 ? 47.215 21.780  30.789  1.00 44.44  ? 157 GLU   B HB3  1 
ATOM   5146 N N    . VAL   B 1 178 ? 47.943 18.872  33.126  1.00 26.32  ? 158 VAL   B N    1 
ATOM   5147 C CA   . VAL   B 1 178 ? 49.062 18.729  34.042  1.00 23.73  ? 158 VAL   B CA   1 
ATOM   5148 C C    . VAL   B 1 178 ? 50.312 19.236  33.325  1.00 23.87  ? 158 VAL   B C    1 
ATOM   5149 O O    . VAL   B 1 178 ? 50.606 18.814  32.195  1.00 26.05  ? 158 VAL   B O    1 
ATOM   5150 C CB   . VAL   B 1 178 ? 49.216 17.261  34.471  1.00 23.31  ? 158 VAL   B CB   1 
ATOM   5151 C CG1  . VAL   B 1 178 ? 50.506 17.053  35.259  1.00 25.03  ? 158 VAL   B CG1  1 
ATOM   5152 C CG2  . VAL   B 1 178 ? 48.017 16.805  35.290  1.00 24.11  ? 158 VAL   B CG2  1 
ATOM   5153 H H    . VAL   B 1 178 ? 47.617 18.126  32.847  1.00 31.59  ? 158 VAL   B H    1 
ATOM   5154 H HA   . VAL   B 1 178 ? 48.915 19.256  34.843  1.00 28.48  ? 158 VAL   B HA   1 
ATOM   5155 H HB   . VAL   B 1 178 ? 49.260 16.716  33.669  1.00 27.98  ? 158 VAL   B HB   1 
ATOM   5156 H HG11 . VAL   B 1 178 ? 50.482 16.180  35.680  1.00 30.04  ? 158 VAL   B HG11 1 
ATOM   5157 H HG12 . VAL   B 1 178 ? 51.260 17.106  34.650  1.00 30.04  ? 158 VAL   B HG12 1 
ATOM   5158 H HG13 . VAL   B 1 178 ? 50.578 17.745  35.935  1.00 30.04  ? 158 VAL   B HG13 1 
ATOM   5159 H HG21 . VAL   B 1 178 ? 48.145 15.879  35.549  1.00 28.94  ? 158 VAL   B HG21 1 
ATOM   5160 H HG22 . VAL   B 1 178 ? 47.945 17.362  36.081  1.00 28.94  ? 158 VAL   B HG22 1 
ATOM   5161 H HG23 . VAL   B 1 178 ? 47.215 16.890  34.751  1.00 28.94  ? 158 VAL   B HG23 1 
ATOM   5162 N N    . ARG   B 1 179 ? 51.054 20.151  33.963  1.00 23.42  ? 159 ARG   B N    1 
ATOM   5163 C CA   . ARG   B 1 179 ? 52.275 20.678  33.353  1.00 23.64  ? 159 ARG   B CA   1 
ATOM   5164 C C    . ARG   B 1 179 ? 53.345 19.589  33.304  1.00 21.93  ? 159 ARG   B C    1 
ATOM   5165 O O    . ARG   B 1 179 ? 53.642 18.940  34.313  1.00 23.59  ? 159 ARG   B O    1 
ATOM   5166 C CB   . ARG   B 1 179 ? 52.791 21.867  34.156  1.00 25.54  ? 159 ARG   B CB   1 
ATOM   5167 C CG   . ARG   B 1 179 ? 51.887 23.096  34.135  1.00 27.75  ? 159 ARG   B CG   1 
ATOM   5168 C CD   . ARG   B 1 179 ? 52.563 24.268  34.864  1.00 30.75  ? 159 ARG   B CD   1 
ATOM   5169 N NE   . ARG   B 1 179 ? 52.810 23.990  36.282  1.00 34.02  ? 159 ARG   B NE   1 
ATOM   5170 C CZ   . ARG   B 1 179 ? 51.934 24.214  37.254  1.00 35.43  ? 159 ARG   B CZ   1 
ATOM   5171 N NH1  . ARG   B 1 179 ? 50.731 24.701  36.999  1.00 35.48  ? 159 ARG   B NH1  1 
ATOM   5172 N NH2  . ARG   B 1 179 ? 52.267 23.932  38.513  1.00 36.92  ? 159 ARG   B NH2  1 
ATOM   5173 H H    . ARG   B 1 179 ? 50.873 20.476  34.738  1.00 28.10  ? 159 ARG   B H    1 
ATOM   5174 H HA   . ARG   B 1 179 ? 52.083 20.973  32.449  1.00 28.37  ? 159 ARG   B HA   1 
ATOM   5175 H HB2  . ARG   B 1 179 ? 52.890 21.593  35.081  1.00 30.65  ? 159 ARG   B HB2  1 
ATOM   5176 H HB3  . ARG   B 1 179 ? 53.652 22.132  33.794  1.00 30.65  ? 159 ARG   B HB3  1 
ATOM   5177 H HG2  . ARG   B 1 179 ? 51.716 23.360  33.217  1.00 33.30  ? 159 ARG   B HG2  1 
ATOM   5178 H HG3  . ARG   B 1 179 ? 51.050 22.894  34.583  1.00 33.30  ? 159 ARG   B HG3  1 
ATOM   5179 H HD2  . ARG   B 1 179 ? 53.417 24.451  34.442  1.00 36.90  ? 159 ARG   B HD2  1 
ATOM   5180 H HD3  . ARG   B 1 179 ? 51.990 25.048  34.807  1.00 36.90  ? 159 ARG   B HD3  1 
ATOM   5181 H HE   . ARG   B 1 179 ? 53.574 23.659  36.499  1.00 40.83  ? 159 ARG   B HE   1 
ATOM   5182 H HH11 . ARG   B 1 179 ? 50.502 24.879  36.189  1.00 42.58  ? 159 ARG   B HH11 1 
ATOM   5183 H HH12 . ARG   B 1 179 ? 50.178 24.839  37.643  1.00 42.58  ? 159 ARG   B HH12 1 
ATOM   5184 H HH21 . ARG   B 1 179 ? 53.044 23.607  38.690  1.00 44.30  ? 159 ARG   B HH21 1 
ATOM   5185 H HH22 . ARG   B 1 179 ? 51.706 24.074  39.149  1.00 44.30  ? 159 ARG   B HH22 1 
ATOM   5186 N N    . ARG   B 1 180 ? 53.909 19.360  32.130  1.00 21.84  ? 160 ARG   B N    1 
ATOM   5187 C CA   . ARG   B 1 180 ? 54.863 18.272  31.965  1.00 21.53  ? 160 ARG   B CA   1 
ATOM   5188 C C    . ARG   B 1 180 ? 56.298 18.733  31.798  1.00 21.88  ? 160 ARG   B C    1 
ATOM   5189 O O    . ARG   B 1 180 ? 57.166 17.900  31.559  1.00 22.77  ? 160 ARG   B O    1 
ATOM   5190 C CB   . ARG   B 1 180 ? 54.447 17.411  30.790  1.00 24.30  ? 160 ARG   B CB   1 
ATOM   5191 C CG   . ARG   B 1 180 ? 52.995 16.904  30.941  1.00 28.28  ? 160 ARG   B CG   1 
ATOM   5192 C CD   . ARG   B 1 180 ? 52.690 15.737  30.089  1.00 29.64  ? 160 ARG   B CD   1 
ATOM   5193 N NE   . ARG   B 1 180 ? 51.259 15.440  30.087  1.00 31.01  ? 160 ARG   B NE   1 
ATOM   5194 C CZ   . ARG   B 1 180 ? 50.723 14.448  29.405  1.00 35.22  ? 160 ARG   B CZ   1 
ATOM   5195 N NH1  . ARG   B 1 180 ? 51.469 13.640  28.673  1.00 38.12  ? 160 ARG   B NH1  1 
ATOM   5196 N NH2  . ARG   B 1 180 ? 49.409 14.257  29.466  1.00 35.45  ? 160 ARG   B NH2  1 
ATOM   5197 H H    . ARG   B 1 180 ? 53.758 19.817  31.417  1.00 26.21  ? 160 ARG   B H    1 
ATOM   5198 H HA   . ARG   B 1 180 ? 54.844 17.731  32.769  1.00 25.83  ? 160 ARG   B HA   1 
ATOM   5199 H HB2  . ARG   B 1 180 ? 54.505 17.932  29.974  1.00 29.17  ? 160 ARG   B HB2  1 
ATOM   5200 H HB3  . ARG   B 1 180 ? 55.035 16.641  30.734  1.00 29.17  ? 160 ARG   B HB3  1 
ATOM   5201 H HG2  . ARG   B 1 180 ? 52.847 16.644  31.864  1.00 33.94  ? 160 ARG   B HG2  1 
ATOM   5202 H HG3  . ARG   B 1 180 ? 52.386 17.618  30.696  1.00 33.94  ? 160 ARG   B HG3  1 
ATOM   5203 H HD2  . ARG   B 1 180 ? 52.965 15.924  29.178  1.00 35.57  ? 160 ARG   B HD2  1 
ATOM   5204 H HD3  . ARG   B 1 180 ? 53.163 14.961  30.426  1.00 35.57  ? 160 ARG   B HD3  1 
ATOM   5205 H HE   . ARG   B 1 180 ? 50.739 15.940  30.556  1.00 37.21  ? 160 ARG   B HE   1 
ATOM   5206 H HH11 . ARG   B 1 180 ? 51.103 12.997  28.234  1.00 45.75  ? 160 ARG   B HH11 1 
ATOM   5207 H HH12 . ARG   B 1 180 ? 52.320 13.756  28.635  1.00 45.75  ? 160 ARG   B HH12 1 
ATOM   5208 H HH21 . ARG   B 1 180 ? 48.921 14.777  29.946  1.00 42.54  ? 160 ARG   B HH21 1 
ATOM   5209 H HH22 . ARG   B 1 180 ? 49.047 13.613  29.026  1.00 42.54  ? 160 ARG   B HH22 1 
ATOM   5210 N N    . ASP   B 1 181 ? 56.576 20.025  31.939  1.00 23.44  ? 161 ASP   B N    1 
ATOM   5211 C CA   . ASP   B 1 181 ? 57.921 20.507  31.647  1.00 25.51  ? 161 ASP   B CA   1 
ATOM   5212 C C    . ASP   B 1 181 ? 58.961 19.818  32.521  1.00 24.90  ? 161 ASP   B C    1 
ATOM   5213 O O    . ASP   B 1 181 ? 60.095 19.548  32.077  1.00 27.54  ? 161 ASP   B O    1 
ATOM   5214 C CB   . ASP   B 1 181 ? 57.929 22.020  31.879  1.00 30.05  ? 161 ASP   B CB   1 
ATOM   5215 C CG   . ASP   B 1 181 ? 56.790 22.712  31.152  1.00 35.80  ? 161 ASP   B CG   1 
ATOM   5216 O OD1  . ASP   B 1 181 ? 55.647 22.831  31.700  1.00 34.58  ? 161 ASP   B OD1  1 
ATOM   5217 O OD2  . ASP   B 1 181 ? 57.037 23.085  29.995  1.00 39.56  ? 161 ASP   B OD2  1 
ATOM   5218 H H    . ASP   B 1 181 ? 56.020 20.628  32.196  1.00 28.13  ? 161 ASP   B H    1 
ATOM   5219 H HA   . ASP   B 1 181 ? 58.157 20.316  30.725  1.00 30.62  ? 161 ASP   B HA   1 
ATOM   5220 H HB2  . ASP   B 1 181 ? 57.835 22.198  32.828  1.00 36.07  ? 161 ASP   B HB2  1 
ATOM   5221 H HB3  . ASP   B 1 181 ? 58.765 22.389  31.553  1.00 36.07  ? 161 ASP   B HB3  1 
ATOM   5222 N N    . GLY   B 1 182 ? 58.619 19.541  33.768  1.00 21.60  ? 162 GLY   B N    1 
ATOM   5223 C CA   . GLY   B 1 182 ? 59.597 18.988  34.678  1.00 21.14  ? 162 GLY   B CA   1 
ATOM   5224 C C    . GLY   B 1 182 ? 59.736 17.492  34.642  1.00 21.61  ? 162 GLY   B C    1 
ATOM   5225 O O    . GLY   B 1 182 ? 60.475 16.925  35.452  1.00 22.88  ? 162 GLY   B O    1 
ATOM   5226 H H    . GLY   B 1 182 ? 57.837 19.665  34.103  1.00 25.93  ? 162 GLY   B H    1 
ATOM   5227 H HA2  . GLY   B 1 182 ? 60.464 19.368  34.468  1.00 25.37  ? 162 GLY   B HA2  1 
ATOM   5228 H HA3  . GLY   B 1 182 ? 59.353 19.239  35.583  1.00 25.37  ? 162 GLY   B HA3  1 
ATOM   5229 N N    . LEU   B 1 183 ? 59.016 16.842  33.756  1.00 21.73  ? 163 LEU   B N    1 
ATOM   5230 C CA   . LEU   B 1 183 ? 58.929 15.389  33.695  1.00 23.61  ? 163 LEU   B CA   1 
ATOM   5231 C C    . LEU   B 1 183 ? 59.909 14.832  32.673  1.00 26.17  ? 163 LEU   B C    1 
ATOM   5232 O O    . LEU   B 1 183 ? 60.242 15.498  31.688  1.00 28.64  ? 163 LEU   B O    1 
ATOM   5233 C CB   . LEU   B 1 183 ? 57.516 14.973  33.286  1.00 23.88  ? 163 LEU   B CB   1 
ATOM   5234 C CG   . LEU   B 1 183 ? 56.420 15.460  34.237  1.00 25.30  ? 163 LEU   B CG   1 
ATOM   5235 C CD1  . LEU   B 1 183 ? 55.050 15.028  33.730  1.00 27.81  ? 163 LEU   B CD1  1 
ATOM   5236 C CD2  . LEU   B 1 183 ? 56.634 14.965  35.650  1.00 25.60  ? 163 LEU   B CD2  1 
ATOM   5237 H H    . LEU   B 1 183 ? 58.546 17.229  33.149  1.00 26.08  ? 163 LEU   B H    1 
ATOM   5238 H HA   . LEU   B 1 183 ? 59.137 15.011  34.564  1.00 28.33  ? 163 LEU   B HA   1 
ATOM   5239 H HB2  . LEU   B 1 183 ? 57.328 15.337  32.407  1.00 28.66  ? 163 LEU   B HB2  1 
ATOM   5240 H HB3  . LEU   B 1 183 ? 57.474 14.004  33.260  1.00 28.66  ? 163 LEU   B HB3  1 
ATOM   5241 H HG   . LEU   B 1 183 ? 56.455 16.429  34.263  1.00 30.36  ? 163 LEU   B HG   1 
ATOM   5242 H HD11 . LEU   B 1 183 ? 54.368 15.378  34.325  1.00 33.37  ? 163 LEU   B HD11 1 
ATOM   5243 H HD12 . LEU   B 1 183 ? 54.919 15.378  32.835  1.00 33.37  ? 163 LEU   B HD12 1 
ATOM   5244 H HD13 . LEU   B 1 183 ? 55.010 14.059  33.716  1.00 33.37  ? 163 LEU   B HD13 1 
ATOM   5245 H HD21 . LEU   B 1 183 ? 55.865 15.207  36.189  1.00 30.72  ? 163 LEU   B HD21 1 
ATOM   5246 H HD22 . LEU   B 1 183 ? 56.739 14.001  35.635  1.00 30.72  ? 163 LEU   B HD22 1 
ATOM   5247 H HD23 . LEU   B 1 183 ? 57.434 15.379  36.011  1.00 30.72  ? 163 LEU   B HD23 1 
ATOM   5248 N N    . PRO   B 1 184 ? 60.393 13.614  32.879  1.00 26.32  ? 164 PRO   B N    1 
ATOM   5249 C CA   . PRO   B 1 184 ? 61.170 12.961  31.828  1.00 28.65  ? 164 PRO   B CA   1 
ATOM   5250 C C    . PRO   B 1 184 ? 60.370 12.848  30.539  1.00 32.01  ? 164 PRO   B C    1 
ATOM   5251 O O    . PRO   B 1 184 ? 59.187 12.492  30.545  1.00 31.69  ? 164 PRO   B O    1 
ATOM   5252 C CB   . PRO   B 1 184 ? 61.455 11.568  32.409  1.00 28.89  ? 164 PRO   B CB   1 
ATOM   5253 C CG   . PRO   B 1 184 ? 61.251 11.661  33.841  1.00 29.86  ? 164 PRO   B CG   1 
ATOM   5254 C CD   . PRO   B 1 184 ? 60.226 12.745  34.060  1.00 28.51  ? 164 PRO   B CD   1 
ATOM   5255 H HA   . PRO   B 1 184 ? 61.999 13.440  31.671  1.00 34.39  ? 164 PRO   B HA   1 
ATOM   5256 H HB2  . PRO   B 1 184 ? 60.842 10.924  32.019  1.00 34.67  ? 164 PRO   B HB2  1 
ATOM   5257 H HB3  . PRO   B 1 184 ? 62.370 11.316  32.211  1.00 34.67  ? 164 PRO   B HB3  1 
ATOM   5258 H HG2  . PRO   B 1 184 ? 60.926 10.812  34.179  1.00 35.83  ? 164 PRO   B HG2  1 
ATOM   5259 H HG3  . PRO   B 1 184 ? 62.088 11.892  34.274  1.00 35.83  ? 164 PRO   B HG3  1 
ATOM   5260 H HD2  . PRO   B 1 184 ? 59.331 12.372  34.091  1.00 34.22  ? 164 PRO   B HD2  1 
ATOM   5261 H HD3  . PRO   B 1 184 ? 60.410 13.234  34.877  1.00 34.22  ? 164 PRO   B HD3  1 
ATOM   5262 N N    . SER   B 1 185 ? 61.036 13.124  29.428  1.00 38.93  ? 165 SER   B N    1 
ATOM   5263 C CA   . SER   B 1 185 ? 60.421 13.001  28.110  1.00 47.20  ? 165 SER   B CA   1 
ATOM   5264 C C    . SER   B 1 185 ? 61.110 11.891  27.325  1.00 51.75  ? 165 SER   B C    1 
ATOM   5265 O O    . SER   B 1 185 ? 61.501 10.868  27.895  1.00 54.40  ? 165 SER   B O    1 
ATOM   5266 C CB   . SER   B 1 185 ? 60.528 14.323  27.348  1.00 51.28  ? 165 SER   B CB   1 
ATOM   5267 O OG   . SER   B 1 185 ? 61.883 14.674  27.136  1.00 53.94  ? 165 SER   B OG   1 
ATOM   5268 H H    . SER   B 1 185 ? 61.855 13.387  29.407  1.00 46.71  ? 165 SER   B H    1 
ATOM   5269 H HA   . SER   B 1 185 ? 59.479 12.787  28.202  1.00 56.64  ? 165 SER   B HA   1 
ATOM   5270 H HB2  . SER   B 1 185 ? 60.087 14.228  26.489  1.00 61.54  ? 165 SER   B HB2  1 
ATOM   5271 H HB3  . SER   B 1 185 ? 60.098 15.021  27.866  1.00 61.54  ? 165 SER   B HB3  1 
ATOM   5272 H HG   . SER   B 1 185 ? 61.929 15.396  26.709  1.00 64.73  ? 165 SER   B HG   1 
HETATM 5273 O O1   . MES   C 2 .   ? 30.721 -6.374  5.006   1.00 27.58  ? 201 MES   A O1   1 
HETATM 5274 C C2   . MES   C 2 .   ? 29.856 -6.069  3.885   1.00 26.96  ? 201 MES   A C2   1 
HETATM 5275 C C3   . MES   C 2 .   ? 28.455 -5.634  4.238   1.00 47.41  ? 201 MES   A C3   1 
HETATM 5276 N N4   . MES   C 2 .   ? 28.452 -4.604  5.272   1.00 25.84  ? 201 MES   A N4   1 
HETATM 5277 C C5   . MES   C 2 .   ? 29.387 -4.834  6.373   1.00 24.32  ? 201 MES   A C5   1 
HETATM 5278 C C6   . MES   C 2 .   ? 30.754 -5.221  5.856   1.00 36.67  ? 201 MES   A C6   1 
HETATM 5279 C C7   . MES   C 2 .   ? 27.052 -4.359  5.608   1.00 46.94  ? 201 MES   A C7   1 
HETATM 5280 C C8   . MES   C 2 .   ? 26.904 -3.263  6.644   1.00 27.08  ? 201 MES   A C8   1 
HETATM 5281 S S    . MES   C 2 .   ? 25.509 -2.393  6.313   1.00 45.33  ? 201 MES   A S    1 
HETATM 5282 O O1S  . MES   C 2 .   ? 25.375 -1.468  7.454   1.00 35.20  ? 201 MES   A O1S  1 
HETATM 5283 O O2S  . MES   C 2 .   ? 25.860 -1.674  5.082   1.00 46.78  ? 201 MES   A O2S  1 
HETATM 5284 O O3S  . MES   C 2 .   ? 24.313 -3.220  6.107   1.00 57.71  ? 201 MES   A O3S  1 
HETATM 5285 H H21  . MES   C 2 .   ? 29.789 -6.957  3.253   1.00 32.35  ? 201 MES   A H21  1 
HETATM 5286 H H22  . MES   C 2 .   ? 30.323 -5.275  3.298   1.00 32.35  ? 201 MES   A H22  1 
HETATM 5287 H H31  . MES   C 2 .   ? 27.962 -5.247  3.344   1.00 56.89  ? 201 MES   A H31  1 
HETATM 5288 H H32  . MES   C 2 .   ? 27.887 -6.498  4.588   1.00 56.89  ? 201 MES   A H32  1 
HETATM 5289 H HN4  . MES   C 2 .   ? 28.845 -3.740  4.931   1.00 31.01  ? 201 MES   A HN4  1 
HETATM 5290 H H51  . MES   C 2 .   ? 29.003 -5.630  7.015   1.00 29.19  ? 201 MES   A H51  1 
HETATM 5291 H H52  . MES   C 2 .   ? 29.469 -3.927  6.975   1.00 29.19  ? 201 MES   A H52  1 
HETATM 5292 H H61  . MES   C 2 .   ? 31.410 -5.424  6.705   1.00 44.01  ? 201 MES   A H61  1 
HETATM 5293 H H62  . MES   C 2 .   ? 31.175 -4.381  5.300   1.00 44.01  ? 201 MES   A H62  1 
HETATM 5294 H H71  . MES   C 2 .   ? 26.509 -4.076  4.704   1.00 56.33  ? 201 MES   A H71  1 
HETATM 5295 H H72  . MES   C 2 .   ? 26.608 -5.280  5.992   1.00 56.33  ? 201 MES   A H72  1 
HETATM 5296 H H81  . MES   C 2 .   ? 26.846 -3.698  7.643   1.00 32.50  ? 201 MES   A H81  1 
HETATM 5297 H H82  . MES   C 2 .   ? 27.773 -2.602  6.616   1.00 32.50  ? 201 MES   A H82  1 
HETATM 5298 C C12  . A1IAL D 3 .   ? 26.847 -10.794 -1.124  1.00 16.54  ? 202 A1IAL A C12  1 
HETATM 5299 C C11  . A1IAL D 3 .   ? 28.215 -11.079 -0.921  1.00 15.88  ? 202 A1IAL A C11  1 
HETATM 5300 C C17  . A1IAL D 3 .   ? 24.659 -10.140 -0.403  1.00 17.91  ? 202 A1IAL A C17  1 
HETATM 5301 C C15  . A1IAL D 3 .   ? 24.261 -10.188 -1.725  1.00 20.76  ? 202 A1IAL A C15  1 
HETATM 5302 C C13  . A1IAL D 3 .   ? 26.399 -10.823 -2.442  1.00 19.69  ? 202 A1IAL A C13  1 
HETATM 5303 C C14  . A1IAL D 3 .   ? 25.075 -10.545 -2.753  1.00 25.16  ? 202 A1IAL A C14  1 
HETATM 5304 C C10  . A1IAL D 3 .   ? 29.153 -10.557 -0.025  1.00 15.21  ? 202 A1IAL A C10  1 
HETATM 5305 C C02  . A1IAL D 3 .   ? 28.886 -9.473  1.012   1.00 16.15  ? 202 A1IAL A C02  1 
HETATM 5306 C C03  . A1IAL D 3 .   ? 28.135 -8.217  0.596   1.00 16.36  ? 202 A1IAL A C03  1 
HETATM 5307 C C04  . A1IAL D 3 .   ? 28.202 -7.776  -0.714  1.00 15.58  ? 202 A1IAL A C04  1 
HETATM 5308 C C05  . A1IAL D 3 .   ? 27.589 -6.608  -1.104  1.00 19.20  ? 202 A1IAL A C05  1 
HETATM 5309 C C06  . A1IAL D 3 .   ? 26.887 -5.925  -0.159  1.00 20.57  ? 202 A1IAL A C06  1 
HETATM 5310 C C07  . A1IAL D 3 .   ? 26.759 -6.399  1.133   1.00 25.34  ? 202 A1IAL A C07  1 
HETATM 5311 C C09  . A1IAL D 3 .   ? 27.429 -7.532  1.563   1.00 21.31  ? 202 A1IAL A C09  1 
HETATM 5312 C C18  . A1IAL D 3 .   ? 25.998 -10.430 -0.112  1.00 16.96  ? 202 A1IAL A C18  1 
HETATM 5313 C C20  . A1IAL D 3 .   ? 30.537 -12.125 -1.081  1.00 16.07  ? 202 A1IAL A C20  1 
HETATM 5314 C C21  . A1IAL D 3 .   ? 31.718 -12.795 -1.376  1.00 17.34  ? 202 A1IAL A C21  1 
HETATM 5315 C C22  . A1IAL D 3 .   ? 32.848 -12.475 -0.664  1.00 16.84  ? 202 A1IAL A C22  1 
HETATM 5316 C C24  . A1IAL D 3 .   ? 32.832 -11.517 0.338   1.00 17.07  ? 202 A1IAL A C24  1 
HETATM 5317 C C25  . A1IAL D 3 .   ? 31.652 -10.833 0.599   1.00 14.91  ? 202 A1IAL A C25  1 
HETATM 5318 C C26  . A1IAL D 3 .   ? 30.448 -11.149 -0.100  1.00 14.95  ? 202 A1IAL A C26  1 
HETATM 5319 O O01  . A1IAL D 3 .   ? 29.254 -9.582  2.171   1.00 18.41  ? 202 A1IAL A O01  1 
HETATM 5320 O O08  . A1IAL D 3 .   ? 26.022 -5.724  2.108   1.00 36.38  ? 202 A1IAL A O08  1 
HETATM 5321 O O16  . A1IAL D 3 .   ? 22.896 -9.925  -1.994  1.00 27.51  ? 202 A1IAL A O16  1 
HETATM 5322 O O23  . A1IAL D 3 .   ? 34.037 -13.128 -0.917  1.00 19.85  ? 202 A1IAL A O23  1 
HETATM 5323 S S19  . A1IAL D 3 .   ? 28.996 -12.346 -1.829  1.00 17.92  ? 202 A1IAL A S19  1 
HETATM 5324 H H171 . A1IAL D 3 .   ? 23.959 -9.887  0.383   1.00 21.49  ? 202 A1IAL A H171 1 
HETATM 5325 H H131 . A1IAL D 3 .   ? 27.094 -11.066 -3.237  1.00 23.63  ? 202 A1IAL A H131 1 
HETATM 5326 H H141 . A1IAL D 3 .   ? 24.707 -10.609 -3.770  1.00 30.19  ? 202 A1IAL A H141 1 
HETATM 5327 H H041 . A1IAL D 3 .   ? 28.747 -8.362  -1.446  1.00 18.70  ? 202 A1IAL A H041 1 
HETATM 5328 H H051 . A1IAL D 3 .   ? 27.661 -6.247  -2.124  1.00 23.04  ? 202 A1IAL A H051 1 
HETATM 5329 H H061 . A1IAL D 3 .   ? 26.418 -4.987  -0.426  1.00 24.69  ? 202 A1IAL A H061 1 
HETATM 5330 H H091 . A1IAL D 3 .   ? 27.400 -7.860  2.594   1.00 25.57  ? 202 A1IAL A H091 1 
HETATM 5331 H H181 . A1IAL D 3 .   ? 26.361 -10.366 0.906   1.00 20.35  ? 202 A1IAL A H181 1 
HETATM 5332 H H211 . A1IAL D 3 .   ? 31.747 -13.552 -2.150  1.00 20.81  ? 202 A1IAL A H211 1 
HETATM 5333 H H241 . A1IAL D 3 .   ? 33.729 -11.306 0.910   1.00 20.49  ? 202 A1IAL A H241 1 
HETATM 5334 H H251 . A1IAL D 3 .   ? 31.645 -10.047 1.344   1.00 17.89  ? 202 A1IAL A H251 1 
HETATM 5335 H H081 . A1IAL D 3 .   ? 26.303 -4.824  2.121   1.00 43.66  ? 202 A1IAL A H081 1 
HETATM 5336 H H161 . A1IAL D 3 .   ? 22.788 -9.814  -2.924  1.00 33.01  ? 202 A1IAL A H161 1 
HETATM 5337 H H231 . A1IAL D 3 .   ? 34.220 -13.717 -0.200  1.00 23.82  ? 202 A1IAL A H231 1 
HETATM 5338 C C1   . GOL   E 4 .   ? 40.048 19.480  0.849   0.33 40.50  ? 203 GOL   A C1   1 
HETATM 5339 O O1   . GOL   E 4 .   ? 39.269 20.411  1.540   0.33 44.88  ? 203 GOL   A O1   1 
HETATM 5340 C C2   . GOL   E 4 .   ? 40.799 20.254  -0.255  0.33 30.93  ? 203 GOL   A C2   1 
HETATM 5341 O O2   . GOL   E 4 .   ? 41.058 21.560  0.117   0.33 51.81  ? 203 GOL   A O2   1 
HETATM 5342 C C3   . GOL   E 4 .   ? 42.084 19.437  -0.508  0.33 29.03  ? 203 GOL   A C3   1 
HETATM 5343 O O3   . GOL   E 4 .   ? 42.663 19.963  -1.656  0.33 33.72  ? 203 GOL   A O3   1 
HETATM 5344 H H11  . GOL   E 4 .   ? 39.518 18.776  0.444   0.33 48.60  ? 203 GOL   A H11  1 
HETATM 5345 H H12  . GOL   E 4 .   ? 40.691 19.033  1.422   0.33 48.60  ? 203 GOL   A H12  1 
HETATM 5346 H HO1  . GOL   E 4 .   ? 39.160 20.101  2.325   0.33 53.86  ? 203 GOL   A HO1  1 
HETATM 5347 H H2   . GOL   E 4 .   ? 40.265 20.312  -1.063  0.33 37.12  ? 203 GOL   A H2   1 
HETATM 5348 H HO2  . GOL   E 4 .   ? 40.526 21.761  0.748   0.33 62.17  ? 203 GOL   A HO2  1 
HETATM 5349 H H31  . GOL   E 4 .   ? 41.852 18.498  -0.587  0.33 34.84  ? 203 GOL   A H31  1 
HETATM 5350 H H32  . GOL   E 4 .   ? 42.655 19.495  0.274   0.33 34.84  ? 203 GOL   A H32  1 
HETATM 5351 H HO3  . GOL   E 4 .   ? 43.366 19.508  -1.806  0.33 40.47  ? 203 GOL   A HO3  1 
HETATM 5352 O O1   . MES   F 2 .   ? 28.474 7.116   29.438  1.00 24.76  ? 201 MES   B O1   1 
HETATM 5353 C C2   . MES   F 2 .   ? 27.571 6.865   30.548  1.00 24.24  ? 201 MES   B C2   1 
HETATM 5354 C C3   . MES   F 2 .   ? 26.170 6.478   30.141  1.00 32.56  ? 201 MES   B C3   1 
HETATM 5355 N N4   . MES   F 2 .   ? 26.181 5.410   29.144  1.00 23.46  ? 201 MES   B N4   1 
HETATM 5356 C C5   . MES   F 2 .   ? 27.144 5.647   28.076  1.00 22.84  ? 201 MES   B C5   1 
HETATM 5357 C C6   . MES   F 2 .   ? 28.503 5.909   28.670  1.00 29.44  ? 201 MES   B C6   1 
HETATM 5358 C C7   . MES   F 2 .   ? 24.774 5.183   28.740  1.00 26.96  ? 201 MES   B C7   1 
HETATM 5359 C C8   . MES   F 2 .   ? 24.744 4.096   27.667  1.00 25.45  ? 201 MES   B C8   1 
HETATM 5360 S S    . MES   F 2 .   ? 23.527 3.005   27.922  1.00 46.55  ? 201 MES   B S    1 
HETATM 5361 O O1S  . MES   F 2 .   ? 23.115 2.285   26.705  1.00 57.81  ? 201 MES   B O1S  1 
HETATM 5362 O O2S  . MES   F 2 .   ? 22.425 3.517   28.648  1.00 36.28  ? 201 MES   B O2S  1 
HETATM 5363 O O3S  . MES   F 2 .   ? 24.340 2.127   28.766  1.00 33.91  ? 201 MES   B O3S  1 
HETATM 5364 H H21  . MES   F 2 .   ? 27.988 6.065   31.162  1.00 29.09  ? 201 MES   B H21  1 
HETATM 5365 H H22  . MES   F 2 .   ? 27.517 7.767   31.162  1.00 29.09  ? 201 MES   B H22  1 
HETATM 5366 H H31  . MES   F 2 .   ? 25.616 6.145   31.021  1.00 39.07  ? 201 MES   B H31  1 
HETATM 5367 H H32  . MES   F 2 .   ? 25.658 7.351   29.731  1.00 39.07  ? 201 MES   B H32  1 
HETATM 5368 H HN4  . MES   F 2 .   ? 26.528 4.542   29.522  1.00 28.15  ? 201 MES   B HN4  1 
HETATM 5369 H H51  . MES   F 2 .   ? 27.189 4.777   27.418  1.00 27.41  ? 201 MES   B H51  1 
HETATM 5370 H H52  . MES   F 2 .   ? 26.830 6.505   27.477  1.00 27.41  ? 201 MES   B H52  1 
HETATM 5371 H H61  . MES   F 2 .   ? 28.794 5.072   29.308  1.00 35.33  ? 201 MES   B H61  1 
HETATM 5372 H H62  . MES   F 2 .   ? 29.244 5.996   27.873  1.00 35.33  ? 201 MES   B H62  1 
HETATM 5373 H H71  . MES   F 2 .   ? 24.342 6.107   28.350  1.00 32.35  ? 201 MES   B H71  1 
HETATM 5374 H H72  . MES   F 2 .   ? 24.181 4.875   29.604  1.00 32.35  ? 201 MES   B H72  1 
HETATM 5375 H H81  . MES   F 2 .   ? 25.702 3.570   27.661  1.00 30.54  ? 201 MES   B H81  1 
HETATM 5376 H H82  . MES   F 2 .   ? 24.611 4.561   26.688  1.00 30.54  ? 201 MES   B H82  1 
HETATM 5377 C C1   . GOL   G 4 .   ? 31.499 -10.489 22.116  1.00 50.60  ? 202 GOL   B C1   1 
HETATM 5378 O O1   . GOL   G 4 .   ? 32.539 -11.077 22.882  1.00 53.76  ? 202 GOL   B O1   1 
HETATM 5379 C C2   . GOL   G 4 .   ? 32.177 -9.807  20.885  1.00 51.83  ? 202 GOL   B C2   1 
HETATM 5380 O O2   . GOL   G 4 .   ? 33.081 -10.644 20.246  1.00 83.98  ? 202 GOL   B O2   1 
HETATM 5381 C C3   . GOL   G 4 .   ? 31.032 -9.431  19.956  1.00 66.57  ? 202 GOL   B C3   1 
HETATM 5382 O O3   . GOL   G 4 .   ? 31.061 -8.057  19.841  1.00 29.67  ? 202 GOL   B O3   1 
HETATM 5383 H H11  . GOL   G 4 .   ? 30.995 -9.826  22.614  1.00 60.72  ? 202 GOL   B H11  1 
HETATM 5384 H H12  . GOL   G 4 .   ? 30.848 -11.139 21.807  1.00 60.72  ? 202 GOL   B H12  1 
HETATM 5385 H HO1  . GOL   G 4 .   ? 33.130 -11.345 22.331  1.00 64.51  ? 202 GOL   B HO1  1 
HETATM 5386 H H2   . GOL   G 4 .   ? 32.676 -9.029  21.177  1.00 62.20  ? 202 GOL   B H2   1 
HETATM 5387 H HO2  . GOL   G 4 .   ? 33.420 -10.214 19.596  1.00 100.78 ? 202 GOL   B HO2  1 
HETATM 5388 H H31  . GOL   G 4 .   ? 30.201 -9.771  20.324  1.00 79.89  ? 202 GOL   B H31  1 
HETATM 5389 H H32  . GOL   G 4 .   ? 31.146 -9.892  19.111  1.00 79.89  ? 202 GOL   B H32  1 
HETATM 5390 H HO3  . GOL   G 4 .   ? 30.417 -7.833  19.331  1.00 35.61  ? 202 GOL   B HO3  1 
HETATM 5391 C C12  . A1IAL H 3 .   ? 24.629 11.651  35.551  1.00 16.96  ? 203 A1IAL B C12  1 
HETATM 5392 C C11  . A1IAL H 3 .   ? 26.006 11.930  35.354  1.00 17.24  ? 203 A1IAL B C11  1 
HETATM 5393 C C17  . A1IAL H 3 .   ? 22.448 10.995  34.781  1.00 18.20  ? 203 A1IAL B C17  1 
HETATM 5394 C C15  . A1IAL H 3 .   ? 22.053 11.072  36.086  1.00 19.34  ? 203 A1IAL B C15  1 
HETATM 5395 C C13  . A1IAL H 3 .   ? 24.178 11.703  36.870  1.00 19.73  ? 203 A1IAL B C13  1 
HETATM 5396 C C14  . A1IAL H 3 .   ? 22.839 11.422  37.136  1.00 22.13  ? 203 A1IAL B C14  1 
HETATM 5397 C C10  . A1IAL H 3 .   ? 26.939 11.415  34.457  1.00 16.04  ? 203 A1IAL B C10  1 
HETATM 5398 C C02  . A1IAL H 3 .   ? 26.696 10.337  33.434  1.00 16.91  ? 203 A1IAL B C02  1 
HETATM 5399 C C03  . A1IAL H 3 .   ? 25.952 9.075   33.856  1.00 16.85  ? 203 A1IAL B C03  1 
HETATM 5400 C C04  . A1IAL H 3 .   ? 26.011 8.638   35.156  1.00 15.49  ? 203 A1IAL B C04  1 
HETATM 5401 C C05  . A1IAL H 3 .   ? 25.372 7.457   35.520  1.00 19.48  ? 203 A1IAL B C05  1 
HETATM 5402 C C06  . A1IAL H 3 .   ? 24.660 6.797   34.554  1.00 20.71  ? 203 A1IAL B C06  1 
HETATM 5403 C C07  . A1IAL H 3 .   ? 24.510 7.287   33.268  1.00 25.82  ? 203 A1IAL B C07  1 
HETATM 5404 C C09  . A1IAL H 3 .   ? 25.207 8.429   32.888  1.00 21.90  ? 203 A1IAL B C09  1 
HETATM 5405 C C18  . A1IAL H 3 .   ? 23.793 11.298  34.534  1.00 15.93  ? 203 A1IAL B C18  1 
HETATM 5406 C C20  . A1IAL H 3 .   ? 28.353 12.946  35.538  1.00 15.58  ? 203 A1IAL B C20  1 
HETATM 5407 C C21  . A1IAL H 3 .   ? 29.519 13.642  35.816  1.00 17.06  ? 203 A1IAL B C21  1 
HETATM 5408 C C22  . A1IAL H 3 .   ? 30.634 13.305  35.106  1.00 17.20  ? 203 A1IAL B C22  1 
HETATM 5409 C C24  . A1IAL H 3 .   ? 30.612 12.352  34.123  1.00 16.08  ? 203 A1IAL B C24  1 
HETATM 5410 C C25  . A1IAL H 3 .   ? 29.444 11.670  33.846  1.00 16.27  ? 203 A1IAL B C25  1 
HETATM 5411 C C26  . A1IAL H 3 .   ? 28.236 12.006  34.548  1.00 15.24  ? 203 A1IAL B C26  1 
HETATM 5412 O O01  . A1IAL H 3 .   ? 27.025 10.456  32.262  1.00 18.57  ? 203 A1IAL B O01  1 
HETATM 5413 O O08  . A1IAL H 3 .   ? 23.772 6.651   32.271  1.00 35.28  ? 203 A1IAL B O08  1 
HETATM 5414 O O16  . A1IAL H 3 .   ? 20.678 10.814  36.363  1.00 27.74  ? 203 A1IAL B O16  1 
HETATM 5415 O O23  . A1IAL H 3 .   ? 31.831 13.959  35.381  1.00 20.64  ? 203 A1IAL B O23  1 
HETATM 5416 S S19  . A1IAL H 3 .   ? 26.789 13.190  36.258  1.00 18.22  ? 203 A1IAL B S19  1 
HETATM 5417 H H171 . A1IAL H 3 .   ? 21.765 10.718  33.987  1.00 21.84  ? 203 A1IAL B H171 1 
HETATM 5418 H H131 . A1IAL H 3 .   ? 24.858 11.957  37.675  1.00 23.68  ? 203 A1IAL B H131 1 
HETATM 5419 H H141 . A1IAL H 3 .   ? 22.441 11.482  38.142  1.00 26.56  ? 203 A1IAL B H141 1 
HETATM 5420 H H041 . A1IAL H 3 .   ? 26.554 9.212   35.898  1.00 18.59  ? 203 A1IAL B H041 1 
HETATM 5421 H H051 . A1IAL H 3 .   ? 25.436 7.073   36.532  1.00 23.38  ? 203 A1IAL B H051 1 
HETATM 5422 H H061 . A1IAL H 3 .   ? 24.195 5.852   34.807  1.00 24.85  ? 203 A1IAL B H061 1 
HETATM 5423 H H091 . A1IAL H 3 .   ? 25.167 8.799   31.871  1.00 26.28  ? 203 A1IAL B H091 1 
HETATM 5424 H H181 . A1IAL H 3 .   ? 24.174 11.251  33.521  1.00 19.12  ? 203 A1IAL B H181 1 
HETATM 5425 H H211 . A1IAL H 3 .   ? 29.544 14.422  36.567  1.00 20.47  ? 203 A1IAL B H211 1 
HETATM 5426 H H241 . A1IAL H 3 .   ? 31.513 12.132  33.562  1.00 19.30  ? 203 A1IAL B H241 1 
HETATM 5427 H H251 . A1IAL H 3 .   ? 29.438 10.884  33.101  1.00 19.53  ? 203 A1IAL B H251 1 
HETATM 5428 H H081 . A1IAL H 3 .   ? 24.024 5.741   32.260  1.00 42.34  ? 203 A1IAL B H081 1 
HETATM 5429 H H161 . A1IAL H 3 .   ? 20.607 10.521  37.257  1.00 33.29  ? 203 A1IAL B H161 1 
HETATM 5430 H H231 . A1IAL H 3 .   ? 32.540 13.355  35.215  1.00 24.77  ? 203 A1IAL B H231 1 
HETATM 5431 C C1   . GOL   I 4 .   ? 39.770 -11.175 44.931  1.00 54.33  ? 204 GOL   B C1   1 
HETATM 5432 O O1   . GOL   I 4 .   ? 38.697 -10.459 45.418  1.00 65.19  ? 204 GOL   B O1   1 
HETATM 5433 C C2   . GOL   I 4 .   ? 39.218 -12.031 43.771  1.00 63.23  ? 204 GOL   B C2   1 
HETATM 5434 O O2   . GOL   I 4 .   ? 40.203 -12.289 42.847  1.00 62.46  ? 204 GOL   B O2   1 
HETATM 5435 C C3   . GOL   I 4 .   ? 38.684 -13.327 44.444  1.00 61.99  ? 204 GOL   B C3   1 
HETATM 5436 O O3   . GOL   I 4 .   ? 38.139 -14.163 43.433  1.00 47.80  ? 204 GOL   B O3   1 
HETATM 5437 H H11  . GOL   I 4 .   ? 40.172 -11.752 45.599  1.00 65.20  ? 204 GOL   B H11  1 
HETATM 5438 H H12  . GOL   I 4 .   ? 40.486 -10.607 44.606  1.00 65.20  ? 204 GOL   B H12  1 
HETATM 5439 H HO1  . GOL   I 4 .   ? 38.991 -9.995  46.064  1.00 78.23  ? 204 GOL   B HO1  1 
HETATM 5440 H H2   . GOL   I 4 .   ? 38.503 -11.574 43.302  1.00 75.88  ? 204 GOL   B H2   1 
HETATM 5441 H HO2  . GOL   I 4 .   ? 39.822 -12.500 42.117  1.00 74.95  ? 204 GOL   B HO2  1 
HETATM 5442 H H31  . GOL   I 4 .   ? 38.036 -13.077 45.121  1.00 74.39  ? 204 GOL   B H31  1 
HETATM 5443 H H32  . GOL   I 4 .   ? 39.414 -13.744 44.929  1.00 74.39  ? 204 GOL   B H32  1 
HETATM 5444 H HO3  . GOL   I 4 .   ? 37.291 -14.069 43.471  1.00 57.36  ? 204 GOL   B HO3  1 
HETATM 5445 C C1   . GOL   J 4 .   ? 38.565 -18.823 33.600  0.43 33.80  ? 205 GOL   B C1   1 
HETATM 5446 O O1   . GOL   J 4 .   ? 38.517 -19.395 32.324  0.43 48.97  ? 205 GOL   B O1   1 
HETATM 5447 C C2   . GOL   J 4 .   ? 39.437 -19.731 34.465  0.43 37.47  ? 205 GOL   B C2   1 
HETATM 5448 O O2   . GOL   J 4 .   ? 40.213 -20.577 33.700  0.43 37.18  ? 205 GOL   B O2   1 
HETATM 5449 C C3   . GOL   J 4 .   ? 40.290 -18.782 35.301  0.43 43.39  ? 205 GOL   B C3   1 
HETATM 5450 O O3   . GOL   J 4 .   ? 41.027 -19.563 36.194  0.43 39.99  ? 205 GOL   B O3   1 
HETATM 5451 H H11  . GOL   J 4 .   ? 37.687 -18.741 34.005  0.43 40.56  ? 205 GOL   B H11  1 
HETATM 5452 H H12  . GOL   J 4 .   ? 38.939 -17.928 33.595  0.43 40.56  ? 205 GOL   B H12  1 
HETATM 5453 H HO1  . GOL   J 4 .   ? 37.818 -19.883 32.303  0.43 58.77  ? 205 GOL   B HO1  1 
HETATM 5454 H H2   . GOL   J 4 .   ? 38.886 -20.296 35.028  0.43 44.97  ? 205 GOL   B H2   1 
HETATM 5455 H HO2  . GOL   J 4 .   ? 39.920 -20.551 32.902  0.43 44.62  ? 205 GOL   B HO2  1 
HETATM 5456 H H31  . GOL   J 4 .   ? 39.706 -18.144 35.740  0.43 52.07  ? 205 GOL   B H31  1 
HETATM 5457 H H32  . GOL   J 4 .   ? 40.844 -18.255 34.705  0.43 52.07  ? 205 GOL   B H32  1 
HETATM 5458 H HO3  . GOL   J 4 .   ? 41.716 -19.833 35.778  0.43 47.99  ? 205 GOL   B HO3  1 
HETATM 5459 O O    . HOH   K 5 .   ? 18.265 -7.539  12.263  1.00 40.06  ? 301 HOH   A O    1 
HETATM 5460 O O    . HOH   K 5 .   ? 51.666 -16.240 4.001   1.00 37.28  ? 302 HOH   A O    1 
HETATM 5461 O O    . HOH   K 5 .   ? 42.511 13.318  8.999   1.00 59.68  ? 303 HOH   A O    1 
HETATM 5462 O O    . HOH   K 5 .   ? 17.369 10.343  -2.308  1.00 33.13  ? 304 HOH   A O    1 
HETATM 5463 O O    . HOH   K 5 .   ? 23.449 14.677  7.144   1.00 45.00  ? 305 HOH   A O    1 
HETATM 5464 O O    . HOH   K 5 .   ? 29.974 4.855   14.528  1.00 31.69  ? 306 HOH   A O    1 
HETATM 5465 O O    . HOH   K 5 .   ? 28.605 -2.731  3.510   1.00 40.74  ? 307 HOH   A O    1 
HETATM 5466 O O    . HOH   K 5 .   ? 40.856 5.435   15.981  1.00 44.74  ? 308 HOH   A O    1 
HETATM 5467 O O    . HOH   K 5 .   ? 34.447 20.383  4.456   1.00 54.15  ? 309 HOH   A O    1 
HETATM 5468 O O    . HOH   K 5 .   ? 33.182 2.995   -10.611 1.00 37.35  ? 310 HOH   A O    1 
HETATM 5469 O O    . HOH   K 5 .   ? 39.677 23.693  0.431   1.00 56.04  ? 311 HOH   A O    1 
HETATM 5470 O O    . HOH   K 5 .   ? 32.616 -21.579 1.343   1.00 28.58  ? 312 HOH   A O    1 
HETATM 5471 O O    . HOH   K 5 .   ? 24.754 5.990   -11.020 1.00 40.65  ? 313 HOH   A O    1 
HETATM 5472 O O    . HOH   K 5 .   ? 36.175 -14.702 -10.904 1.00 49.42  ? 314 HOH   A O    1 
HETATM 5473 O O    . HOH   K 5 .   ? 27.849 24.147  -4.566  1.00 35.87  ? 315 HOH   A O    1 
HETATM 5474 O O    . HOH   K 5 .   ? 28.364 0.310   3.559   1.00 28.47  ? 316 HOH   A O    1 
HETATM 5475 O O    . HOH   K 5 .   ? 34.058 6.170   -9.694  1.00 30.40  ? 317 HOH   A O    1 
HETATM 5476 O O    . HOH   K 5 .   ? 33.032 -7.220  4.106   1.00 21.24  ? 318 HOH   A O    1 
HETATM 5477 O O    . HOH   K 5 .   ? 25.560 1.646   0.643   1.00 31.63  ? 319 HOH   A O    1 
HETATM 5478 O O    . HOH   K 5 .   ? 33.191 17.563  -8.764  1.00 33.51  ? 320 HOH   A O    1 
HETATM 5479 O O    . HOH   K 5 .   ? 23.023 20.522  -4.429  1.00 40.17  ? 321 HOH   A O    1 
HETATM 5480 O O    . HOH   K 5 .   ? 24.561 -17.811 9.869   1.00 33.94  ? 322 HOH   A O    1 
HETATM 5481 O O    . HOH   K 5 .   ? 20.641 14.191  5.784   1.00 55.50  ? 323 HOH   A O    1 
HETATM 5482 O O    . HOH   K 5 .   ? 31.276 -11.245 -7.433  1.00 37.57  ? 324 HOH   A O    1 
HETATM 5483 O O    . HOH   K 5 .   ? 19.846 -11.896 12.254  1.00 38.59  ? 325 HOH   A O    1 
HETATM 5484 O O    . HOH   K 5 .   ? 62.952 -18.309 5.237   1.00 44.69  ? 326 HOH   A O    1 
HETATM 5485 O O    . HOH   K 5 .   ? 23.092 2.625   1.944   1.00 26.66  ? 327 HOH   A O    1 
HETATM 5486 O O    . HOH   K 5 .   ? 29.150 30.791  -6.246  1.00 40.29  ? 328 HOH   A O    1 
HETATM 5487 O O    . HOH   K 5 .   ? 21.014 7.962   8.906   1.00 34.11  ? 329 HOH   A O    1 
HETATM 5488 O O    . HOH   K 5 .   ? 40.905 4.689   10.837  1.00 26.42  ? 330 HOH   A O    1 
HETATM 5489 O O    . HOH   K 5 .   ? 30.793 19.924  6.831   1.00 35.23  ? 331 HOH   A O    1 
HETATM 5490 O O    . HOH   K 5 .   ? 40.622 -5.123  5.239   1.00 18.66  ? 332 HOH   A O    1 
HETATM 5491 O O    . HOH   K 5 .   ? 39.437 -9.850  11.606  1.00 40.84  ? 333 HOH   A O    1 
HETATM 5492 O O    . HOH   K 5 .   ? 28.923 3.436   -10.164 1.00 37.40  ? 334 HOH   A O    1 
HETATM 5493 O O    . HOH   K 5 .   ? 26.559 -7.134  12.201  1.00 18.84  ? 335 HOH   A O    1 
HETATM 5494 O O    . HOH   K 5 .   ? 45.799 -19.361 6.475   1.00 46.75  ? 336 HOH   A O    1 
HETATM 5495 O O    . HOH   K 5 .   ? 28.959 15.497  -9.337  1.00 42.37  ? 337 HOH   A O    1 
HETATM 5496 O O    . HOH   K 5 .   ? 16.669 12.031  0.258   1.00 29.41  ? 338 HOH   A O    1 
HETATM 5497 O O    . HOH   K 5 .   ? 15.657 -7.319  8.005   1.00 39.87  ? 339 HOH   A O    1 
HETATM 5498 O O    . HOH   K 5 .   ? 27.934 -9.524  17.846  1.00 37.94  ? 340 HOH   A O    1 
HETATM 5499 O O    . HOH   K 5 .   ? 32.942 5.936   -5.167  1.00 16.15  ? 341 HOH   A O    1 
HETATM 5500 O O    . HOH   K 5 .   ? 26.314 2.889   7.908   1.00 20.58  ? 342 HOH   A O    1 
HETATM 5501 O O    . HOH   K 5 .   ? 38.118 -18.950 11.098  1.00 39.09  ? 343 HOH   A O    1 
HETATM 5502 O O    . HOH   K 5 .   ? 31.231 -18.510 11.156  1.00 26.14  ? 344 HOH   A O    1 
HETATM 5503 O O    . HOH   K 5 .   ? 45.455 -22.607 4.436   1.00 31.84  ? 345 HOH   A O    1 
HETATM 5504 O O    . HOH   K 5 .   ? 18.961 6.642   8.196   1.00 32.75  ? 346 HOH   A O    1 
HETATM 5505 O O    . HOH   K 5 .   ? 20.732 -12.301 14.697  1.00 49.95  ? 347 HOH   A O    1 
HETATM 5506 O O    . HOH   K 5 .   ? 14.806 -0.347  3.454   1.00 27.14  ? 348 HOH   A O    1 
HETATM 5507 O O    . HOH   K 5 .   ? 42.155 -2.994  4.382   1.00 22.87  ? 349 HOH   A O    1 
HETATM 5508 O O    . HOH   K 5 .   ? 32.340 -22.599 7.210   1.00 30.40  ? 350 HOH   A O    1 
HETATM 5509 O O    . HOH   K 5 .   ? 23.771 -1.670  13.330  1.00 23.25  ? 351 HOH   A O    1 
HETATM 5510 O O    . HOH   K 5 .   ? 55.442 -22.519 4.247   1.00 42.91  ? 352 HOH   A O    1 
HETATM 5511 O O    . HOH   K 5 .   ? 27.094 23.826  2.162   1.00 36.91  ? 353 HOH   A O    1 
HETATM 5512 O O    . HOH   K 5 .   ? 24.178 20.436  4.654   1.00 40.11  ? 354 HOH   A O    1 
HETATM 5513 O O    . HOH   K 5 .   ? 30.863 12.926  -8.588  1.00 37.04  ? 355 HOH   A O    1 
HETATM 5514 O O    . HOH   K 5 .   ? 21.846 -1.100  1.020   1.00 32.96  ? 356 HOH   A O    1 
HETATM 5515 O O    . HOH   K 5 .   ? 56.306 -12.590 5.989   1.00 48.57  ? 357 HOH   A O    1 
HETATM 5516 O O    . HOH   K 5 .   ? 14.355 3.116   9.722   1.00 43.78  ? 358 HOH   A O    1 
HETATM 5517 O O    . HOH   K 5 .   ? 18.543 1.779   3.220   1.00 21.70  ? 359 HOH   A O    1 
HETATM 5518 O O    . HOH   K 5 .   ? 27.705 -16.405 9.222   1.00 21.23  ? 360 HOH   A O    1 
HETATM 5519 O O    . HOH   K 5 .   ? 26.616 0.757   11.027  1.00 32.98  ? 361 HOH   A O    1 
HETATM 5520 O O    . HOH   K 5 .   ? 36.077 16.732  -1.026  1.00 18.89  ? 362 HOH   A O    1 
HETATM 5521 O O    . HOH   K 5 .   ? 39.552 -19.680 8.605   1.00 35.35  ? 363 HOH   A O    1 
HETATM 5522 O O    . HOH   K 5 .   ? 28.651 -20.418 15.544  1.00 56.34  ? 364 HOH   A O    1 
HETATM 5523 O O    . HOH   K 5 .   ? 21.656 0.351   4.968   1.00 36.60  ? 365 HOH   A O    1 
HETATM 5524 O O    . HOH   K 5 .   ? 18.719 -5.002  -3.811  1.00 37.32  ? 366 HOH   A O    1 
HETATM 5525 O O    . HOH   K 5 .   ? 36.342 -5.421  -8.205  1.00 43.54  ? 367 HOH   A O    1 
HETATM 5526 O O    . HOH   K 5 .   ? 51.320 -24.332 -0.068  1.00 40.80  ? 368 HOH   A O    1 
HETATM 5527 O O    . HOH   K 5 .   ? 52.943 -23.788 -6.136  1.00 45.97  ? 369 HOH   A O    1 
HETATM 5528 O O    . HOH   K 5 .   ? 58.321 -18.723 -0.774  1.00 30.77  ? 370 HOH   A O    1 
HETATM 5529 O O    . HOH   K 5 .   ? 40.499 -7.248  15.025  1.00 43.92  ? 371 HOH   A O    1 
HETATM 5530 O O    . HOH   K 5 .   ? 37.857 14.149  -9.775  1.00 38.85  ? 372 HOH   A O    1 
HETATM 5531 O O    . HOH   K 5 .   ? 22.231 2.786   -10.827 1.00 34.87  ? 373 HOH   A O    1 
HETATM 5532 O O    . HOH   K 5 .   ? 28.959 -6.797  17.575  1.00 30.58  ? 374 HOH   A O    1 
HETATM 5533 O O    . HOH   K 5 .   ? 22.212 -8.951  -4.558  1.00 42.98  ? 375 HOH   A O    1 
HETATM 5534 O O    . HOH   K 5 .   ? 50.811 -22.880 2.057   1.00 43.86  ? 376 HOH   A O    1 
HETATM 5535 O O    . HOH   K 5 .   ? 36.021 -2.062  15.570  1.00 25.55  ? 377 HOH   A O    1 
HETATM 5536 O O    . HOH   K 5 .   ? 43.278 -1.579  11.542  1.00 39.57  ? 378 HOH   A O    1 
HETATM 5537 O O    . HOH   K 5 .   ? 33.318 -15.846 13.516  1.00 35.03  ? 379 HOH   A O    1 
HETATM 5538 O O    . HOH   K 5 .   ? 57.376 -21.803 -2.260  1.00 28.37  ? 380 HOH   A O    1 
HETATM 5539 O O    . HOH   K 5 .   ? 30.737 29.070  -0.132  1.00 47.37  ? 381 HOH   A O    1 
HETATM 5540 O O    . HOH   K 5 .   ? 13.618 0.592   -1.454  1.00 34.74  ? 382 HOH   A O    1 
HETATM 5541 O O    . HOH   K 5 .   ? 21.086 13.786  -8.789  1.00 45.67  ? 383 HOH   A O    1 
HETATM 5542 O O    . HOH   K 5 .   ? 13.301 10.103  -7.831  1.00 47.24  ? 384 HOH   A O    1 
HETATM 5543 O O    . HOH   K 5 .   ? 19.090 -5.873  13.633  1.00 44.32  ? 385 HOH   A O    1 
HETATM 5544 O O    . HOH   K 5 .   ? 29.269 -4.090  16.865  1.00 24.86  ? 386 HOH   A O    1 
HETATM 5545 O O    . HOH   K 5 .   ? 27.040 17.751  -4.247  1.00 32.07  ? 387 HOH   A O    1 
HETATM 5546 O O    . HOH   K 5 .   ? 26.842 17.990  -8.359  1.00 34.71  ? 388 HOH   A O    1 
HETATM 5547 O O    . HOH   K 5 .   ? 36.901 -4.010  13.728  1.00 19.71  ? 389 HOH   A O    1 
HETATM 5548 O O    . HOH   K 5 .   ? 28.911 33.111  -4.681  1.00 31.63  ? 390 HOH   A O    1 
HETATM 5549 O O    . HOH   K 5 .   ? 27.276 -6.356  -9.227  1.00 38.19  ? 391 HOH   A O    1 
HETATM 5550 O O    . HOH   K 5 .   ? 34.354 31.664  -10.708 1.00 54.56  ? 392 HOH   A O    1 
HETATM 5551 O O    . HOH   K 5 .   ? 36.582 -8.046  -6.193  1.00 26.04  ? 393 HOH   A O    1 
HETATM 5552 O O    . HOH   K 5 .   ? 43.125 -12.247 11.532  1.00 52.07  ? 394 HOH   A O    1 
HETATM 5553 O O    . HOH   K 5 .   ? 16.994 0.567   -7.913  1.00 36.99  ? 395 HOH   A O    1 
HETATM 5554 O O    . HOH   K 5 .   ? 37.083 -23.955 4.145   1.00 31.70  ? 396 HOH   A O    1 
HETATM 5555 O O    B HOH   K 5 .   ? 22.541 -3.495  1.840   0.43 26.58  ? 397 HOH   A O    1 
HETATM 5556 O O    . HOH   K 5 .   ? 21.468 -3.981  -8.152  1.00 37.22  ? 398 HOH   A O    1 
HETATM 5557 O O    . HOH   K 5 .   ? 45.159 5.552   9.756   1.00 39.56  ? 399 HOH   A O    1 
HETATM 5558 O O    . HOH   K 5 .   ? 37.744 22.899  -4.410  1.00 44.09  ? 400 HOH   A O    1 
HETATM 5559 O O    . HOH   K 5 .   ? 15.894 3.880   -7.647  1.00 36.24  ? 401 HOH   A O    1 
HETATM 5560 O O    . HOH   K 5 .   ? 24.125 -8.505  18.823  1.00 50.04  ? 402 HOH   A O    1 
HETATM 5561 O O    . HOH   K 5 .   ? 40.473 -7.308  11.629  1.00 43.38  ? 403 HOH   A O    1 
HETATM 5562 O O    . HOH   K 5 .   ? 36.289 23.434  1.328   1.00 44.84  ? 404 HOH   A O    1 
HETATM 5563 O O    . HOH   K 5 .   ? 27.146 5.699   -9.904  1.00 32.35  ? 405 HOH   A O    1 
HETATM 5564 O O    . HOH   K 5 .   ? 33.465 12.991  -7.967  1.00 31.08  ? 406 HOH   A O    1 
HETATM 5565 O O    . HOH   K 5 .   ? 18.297 11.712  -8.120  1.00 36.16  ? 407 HOH   A O    1 
HETATM 5566 O O    . HOH   K 5 .   ? 33.399 9.372   14.371  1.00 42.35  ? 408 HOH   A O    1 
HETATM 5567 O O    . HOH   K 5 .   ? 25.593 -20.961 14.066  1.00 38.14  ? 409 HOH   A O    1 
HETATM 5568 O O    . HOH   K 5 .   ? 42.241 -20.159 7.655   1.00 30.74  ? 410 HOH   A O    1 
HETATM 5569 O O    . HOH   K 5 .   ? 36.166 -11.572 15.220  1.00 51.66  ? 411 HOH   A O    1 
HETATM 5570 O O    . HOH   K 5 .   ? 28.134 2.827   12.331  1.00 28.11  ? 412 HOH   A O    1 
HETATM 5571 O O    . HOH   K 5 .   ? 25.844 -11.694 18.392  1.00 49.49  ? 413 HOH   A O    1 
HETATM 5572 O O    . HOH   K 5 .   ? 36.708 -11.314 11.514  1.00 28.28  ? 414 HOH   A O    1 
HETATM 5573 O O    . HOH   K 5 .   ? 34.838 7.027   14.805  1.00 29.94  ? 415 HOH   A O    1 
HETATM 5574 O O    . HOH   K 5 .   ? 55.045 -19.785 5.060   1.00 32.70  ? 416 HOH   A O    1 
HETATM 5575 O O    . HOH   K 5 .   ? 34.121 -7.146  17.738  1.00 32.70  ? 417 HOH   A O    1 
HETATM 5576 O O    . HOH   K 5 .   ? 44.105 -6.827  6.029   1.00 36.18  ? 418 HOH   A O    1 
HETATM 5577 O O    . HOH   K 5 .   ? 18.682 -3.292  14.250  1.00 56.50  ? 419 HOH   A O    1 
HETATM 5578 O O    . HOH   K 5 .   ? 37.313 12.321  10.500  1.00 33.95  ? 420 HOH   A O    1 
HETATM 5579 O O    . HOH   K 5 .   ? 38.635 -3.754  -6.070  1.00 29.64  ? 421 HOH   A O    1 
HETATM 5580 O O    . HOH   K 5 .   ? 17.657 0.745   16.079  1.00 42.08  ? 422 HOH   A O    1 
HETATM 5581 O O    . HOH   K 5 .   ? 20.827 14.556  -6.001  1.00 30.34  ? 423 HOH   A O    1 
HETATM 5582 O O    . HOH   K 5 .   ? 45.317 8.790   12.344  1.00 53.39  ? 424 HOH   A O    1 
HETATM 5583 O O    . HOH   K 5 .   ? 24.301 1.709   -12.482 1.00 42.82  ? 425 HOH   A O    1 
HETATM 5584 O O    . HOH   K 5 .   ? 21.880 5.641   13.426  1.00 26.27  ? 426 HOH   A O    1 
HETATM 5585 O O    . HOH   K 5 .   ? 35.088 1.444   -9.748  1.00 35.47  ? 427 HOH   A O    1 
HETATM 5586 O O    . HOH   K 5 .   ? 26.364 14.610  9.905   1.00 44.10  ? 428 HOH   A O    1 
HETATM 5587 O O    . HOH   K 5 .   ? 42.413 -5.850  7.181   1.00 37.54  ? 429 HOH   A O    1 
HETATM 5588 O O    . HOH   K 5 .   ? 41.048 -1.991  2.173   1.00 21.64  ? 430 HOH   A O    1 
HETATM 5589 O O    . HOH   K 5 .   ? 47.480 -22.931 2.084   1.00 48.20  ? 431 HOH   A O    1 
HETATM 5590 O O    . HOH   K 5 .   ? 26.092 -23.368 9.285   1.00 39.45  ? 432 HOH   A O    1 
HETATM 5591 O O    . HOH   K 5 .   ? 18.562 3.120   14.853  1.00 45.31  ? 433 HOH   A O    1 
HETATM 5592 O O    . HOH   K 5 .   ? 19.814 15.934  -9.614  1.00 52.44  ? 434 HOH   A O    1 
HETATM 5593 O O    . HOH   K 5 .   ? 21.344 -3.865  16.606  1.00 44.00  ? 435 HOH   A O    1 
HETATM 5594 O O    . HOH   K 5 .   ? 20.981 1.101   1.961   1.00 30.96  ? 436 HOH   A O    1 
HETATM 5595 O O    . HOH   K 5 .   ? 28.928 20.480  -6.952  1.00 46.03  ? 437 HOH   A O    1 
HETATM 5596 O O    . HOH   K 5 .   ? 37.088 0.371   -9.421  1.00 44.31  ? 438 HOH   A O    1 
HETATM 5597 O O    A HOH   K 5 .   ? 32.956 -8.474  15.826  0.54 25.61  ? 439 HOH   A O    1 
HETATM 5598 O O    B HOH   K 5 .   ? 28.858 -13.141 17.120  0.46 31.58  ? 439 HOH   A O    1 
HETATM 5599 O O    . HOH   K 5 .   ? 24.699 -0.527  0.770   1.00 38.48  ? 440 HOH   A O    1 
HETATM 5600 O O    . HOH   K 5 .   ? 41.498 -3.707  0.000   0.50 23.06  ? 441 HOH   A O    1 
HETATM 5601 O O    . HOH   K 5 .   ? 41.996 -6.016  9.849   1.00 37.88  ? 442 HOH   A O    1 
HETATM 5602 O O    . HOH   K 5 .   ? 20.806 4.005   15.971  1.00 40.67  ? 443 HOH   A O    1 
HETATM 5603 O O    . HOH   K 5 .   ? 59.686 -25.333 6.063   1.00 62.89  ? 444 HOH   A O    1 
HETATM 5604 O O    . HOH   K 5 .   ? 34.056 -23.788 5.217   1.00 52.88  ? 445 HOH   A O    1 
HETATM 5605 O O    . HOH   K 5 .   ? 37.192 -13.767 12.699  1.00 62.45  ? 446 HOH   A O    1 
HETATM 5606 O O    . HOH   K 5 .   ? 33.340 10.964  12.479  1.00 49.93  ? 447 HOH   A O    1 
HETATM 5607 O O    . HOH   K 5 .   ? 26.650 -2.380  0.858   1.00 42.13  ? 448 HOH   A O    1 
HETATM 5608 O O    . HOH   K 5 .   ? 36.627 18.183  -9.720  1.00 55.01  ? 449 HOH   A O    1 
HETATM 5609 O O    . HOH   K 5 .   ? 36.787 6.820   16.682  1.00 41.58  ? 450 HOH   A O    1 
HETATM 5610 O O    . HOH   K 5 .   ? 32.752 -20.625 11.893  1.00 37.08  ? 451 HOH   A O    1 
HETATM 5611 O O    . HOH   K 5 .   ? 38.426 -6.680  19.980  1.00 49.50  ? 452 HOH   A O    1 
HETATM 5612 O O    . HOH   K 5 .   ? 39.385 7.886   14.837  1.00 59.90  ? 453 HOH   A O    1 
HETATM 5613 O O    . HOH   K 5 .   ? 21.112 7.753   11.733  1.00 43.72  ? 454 HOH   A O    1 
HETATM 5614 O O    . HOH   K 5 .   ? 41.794 2.270   10.971  1.00 52.41  ? 455 HOH   A O    1 
HETATM 5615 O O    . HOH   K 5 .   ? 22.252 0.320   17.127  1.00 34.99  ? 456 HOH   A O    1 
HETATM 5616 O O    . HOH   K 5 .   ? 25.884 22.818  4.138   1.00 47.51  ? 457 HOH   A O    1 
HETATM 5617 O O    . HOH   K 5 .   ? 26.170 20.302  -5.229  1.00 51.14  ? 458 HOH   A O    1 
HETATM 5618 O O    . HOH   K 5 .   ? 27.727 29.476  -7.987  1.00 53.07  ? 459 HOH   A O    1 
HETATM 5619 O O    . HOH   K 5 .   ? 55.483 -10.356 8.393   1.00 55.08  ? 460 HOH   A O    1 
HETATM 5620 O O    . HOH   K 5 .   ? 26.379 12.121  12.375  1.00 55.62  ? 461 HOH   A O    1 
HETATM 5621 O O    . HOH   K 5 .   ? 33.063 -18.469 14.134  1.00 59.76  ? 462 HOH   A O    1 
HETATM 5622 O O    . HOH   K 5 .   ? 23.445 17.846  6.120   1.00 56.50  ? 463 HOH   A O    1 
HETATM 5623 O O    . HOH   K 5 .   ? 48.863 -23.450 -2.442  1.00 47.50  ? 464 HOH   A O    1 
HETATM 5624 O O    . HOH   K 5 .   ? 19.584 2.773   -11.574 1.00 52.65  ? 465 HOH   A O    1 
HETATM 5625 O O    . HOH   K 5 .   ? 33.278 20.824  6.660   1.00 48.38  ? 466 HOH   A O    1 
HETATM 5626 O O    . HOH   K 5 .   ? 63.108 -5.583  6.348   1.00 48.75  ? 467 HOH   A O    1 
HETATM 5627 O O    . HOH   K 5 .   ? 59.173 -8.580  6.090   1.00 52.15  ? 468 HOH   A O    1 
HETATM 5628 O O    . HOH   K 5 .   ? 29.891 11.370  -10.109 1.00 48.65  ? 469 HOH   A O    1 
HETATM 5629 O O    . HOH   K 5 .   ? 29.796 35.558  -5.807  1.00 56.60  ? 470 HOH   A O    1 
HETATM 5630 O O    . HOH   K 5 .   ? 33.766 20.319  -9.270  1.00 59.04  ? 471 HOH   A O    1 
HETATM 5631 O O    . HOH   K 5 .   ? 33.469 30.173  0.288   1.00 50.81  ? 472 HOH   A O    1 
HETATM 5632 O O    . HOH   L 5 .   ? 49.541 16.948  30.575  1.00 35.66  ? 301 HOH   B O    1 
HETATM 5633 O O    . HOH   L 5 .   ? 58.660 22.079  28.594  1.00 45.28  ? 302 HOH   B O    1 
HETATM 5634 O O    . HOH   L 5 .   ? 32.247 10.198  16.903  1.00 48.25  ? 303 HOH   B O    1 
HETATM 5635 O O    . HOH   L 5 .   ? 17.601 12.492  22.148  1.00 38.75  ? 304 HOH   B O    1 
HETATM 5636 O O    . HOH   L 5 .   ? 26.675 3.362   30.773  1.00 37.00  ? 305 HOH   B O    1 
HETATM 5637 O O    . HOH   L 5 .   ? 63.380 10.275  29.423  1.00 47.27  ? 306 HOH   B O    1 
HETATM 5638 O O    . HOH   L 5 .   ? 16.093 8.279   22.035  1.00 41.29  ? 307 HOH   B O    1 
HETATM 5639 O O    . HOH   L 5 .   ? 30.992 -2.148  45.170  1.00 35.07  ? 308 HOH   B O    1 
HETATM 5640 O O    . HOH   L 5 .   ? 33.928 2.919   19.362  1.00 28.39  ? 309 HOH   B O    1 
HETATM 5641 O O    . HOH   L 5 .   ? 38.741 -1.591  16.430  1.00 45.58  ? 310 HOH   B O    1 
HETATM 5642 O O    . HOH   L 5 .   ? 23.779 7.056   14.760  1.00 33.90  ? 311 HOH   B O    1 
HETATM 5643 O O    . HOH   L 5 .   ? 20.799 -19.588 39.134  1.00 37.01  ? 312 HOH   B O    1 
HETATM 5644 O O    . HOH   L 5 .   ? 26.683 -32.313 39.261  1.00 32.30  ? 313 HOH   B O    1 
HETATM 5645 O O    . HOH   L 5 .   ? 26.168 0.473   31.002  1.00 28.51  ? 314 HOH   B O    1 
HETATM 5646 O O    . HOH   L 5 .   ? 25.527 -11.769 45.983  1.00 54.67  ? 315 HOH   B O    1 
HETATM 5647 O O    . HOH   L 5 .   ? 61.705 15.061  36.739  1.00 35.13  ? 316 HOH   B O    1 
HETATM 5648 O O    . HOH   L 5 .   ? 29.101 12.155  41.793  1.00 39.77  ? 317 HOH   B O    1 
HETATM 5649 O O    . HOH   L 5 .   ? 30.417 22.481  33.040  1.00 29.82  ? 318 HOH   B O    1 
HETATM 5650 O O    . HOH   L 5 .   ? 37.019 12.194  23.145  1.00 54.94  ? 319 HOH   B O    1 
HETATM 5651 O O    . HOH   L 5 .   ? 23.448 -0.761  33.945  1.00 29.55  ? 320 HOH   B O    1 
HETATM 5652 O O    . HOH   L 5 .   ? 28.483 -28.206 34.982  1.00 46.07  ? 321 HOH   B O    1 
HETATM 5653 O O    . HOH   L 5 .   ? 53.383 23.417  30.467  1.00 40.81  ? 322 HOH   B O    1 
HETATM 5654 O O    . HOH   L 5 .   ? 30.781 7.973   30.424  1.00 20.65  ? 323 HOH   B O    1 
HETATM 5655 O O    . HOH   L 5 .   ? 26.080 20.927  18.716  1.00 45.91  ? 324 HOH   B O    1 
HETATM 5656 O O    . HOH   L 5 .   ? 31.912 -5.293  44.303  1.00 31.04  ? 325 HOH   B O    1 
HETATM 5657 O O    . HOH   L 5 .   ? 35.754 -13.330 44.277  1.00 37.68  ? 326 HOH   B O    1 
HETATM 5658 O O    . HOH   L 5 .   ? 18.547 13.085  19.546  1.00 45.91  ? 327 HOH   B O    1 
HETATM 5659 O O    . HOH   L 5 .   ? 38.443 5.933   29.288  1.00 17.78  ? 328 HOH   B O    1 
HETATM 5660 O O    . HOH   L 5 .   ? 32.538 7.737   15.549  1.00 44.71  ? 329 HOH   B O    1 
HETATM 5661 O O    . HOH   L 5 .   ? 25.578 -23.354 39.259  1.00 32.05  ? 330 HOH   B O    1 
HETATM 5662 O O    . HOH   L 5 .   ? 38.703 -3.840  23.797  1.00 25.53  ? 331 HOH   B O    1 
HETATM 5663 O O    . HOH   L 5 .   ? 30.129 23.412  27.141  1.00 31.52  ? 332 HOH   B O    1 
HETATM 5664 O O    A HOH   L 5 .   ? 11.808 -7.186  40.357  0.58 40.35  ? 333 HOH   B O    1 
HETATM 5665 O O    B HOH   L 5 .   ? 15.279 -9.562  36.532  0.42 24.00  ? 333 HOH   B O    1 
HETATM 5666 O O    . HOH   L 5 .   ? 28.496 -19.091 27.764  1.00 32.24  ? 334 HOH   B O    1 
HETATM 5667 O O    . HOH   L 5 .   ? 27.469 10.313  43.598  1.00 43.49  ? 335 HOH   B O    1 
HETATM 5668 O O    . HOH   L 5 .   ? 25.028 14.652  18.058  1.00 43.29  ? 336 HOH   B O    1 
HETATM 5669 O O    . HOH   L 5 .   ? 22.270 18.562  24.430  1.00 35.42  ? 337 HOH   B O    1 
HETATM 5670 O O    . HOH   L 5 .   ? 39.934 3.791   30.160  1.00 22.66  ? 338 HOH   B O    1 
HETATM 5671 O O    . HOH   L 5 .   ? 22.739 -5.712  19.169  1.00 45.19  ? 339 HOH   B O    1 
HETATM 5672 O O    . HOH   L 5 .   ? 19.637 1.978   33.604  1.00 30.31  ? 340 HOH   B O    1 
HETATM 5673 O O    . HOH   L 5 .   ? 30.749 -5.083  39.736  1.00 14.42  ? 341 HOH   B O    1 
HETATM 5674 O O    . HOH   L 5 .   ? 55.902 23.551  34.298  1.00 28.98  ? 342 HOH   B O    1 
HETATM 5675 O O    . HOH   L 5 .   ? 31.043 -16.677 43.432  1.00 32.54  ? 343 HOH   B O    1 
HETATM 5676 O O    . HOH   L 5 .   ? 18.811 -7.327  26.047  1.00 39.86  ? 344 HOH   B O    1 
HETATM 5677 O O    . HOH   L 5 .   ? 24.728 -18.287 37.275  1.00 38.02  ? 345 HOH   B O    1 
HETATM 5678 O O    . HOH   L 5 .   ? 36.084 -7.874  20.241  1.00 52.06  ? 346 HOH   B O    1 
HETATM 5679 O O    . HOH   L 5 .   ? 27.007 -30.051 40.652  1.00 41.27  ? 347 HOH   B O    1 
HETATM 5680 O O    . HOH   L 5 .   ? 24.126 -2.137  26.678  1.00 21.72  ? 348 HOH   B O    1 
HETATM 5681 O O    . HOH   L 5 .   ? 12.647 1.172   31.110  1.00 24.84  ? 349 HOH   B O    1 
HETATM 5682 O O    . HOH   L 5 .   ? 35.179 4.869   16.868  1.00 31.09  ? 350 HOH   B O    1 
HETATM 5683 O O    . HOH   L 5 .   ? 60.783 19.204  29.453  1.00 43.99  ? 351 HOH   B O    1 
HETATM 5684 O O    . HOH   L 5 .   ? 34.159 15.903  45.277  1.00 31.91  ? 352 HOH   B O    1 
HETATM 5685 O O    . HOH   L 5 .   ? 32.582 -5.788  19.619  1.00 24.85  ? 353 HOH   B O    1 
HETATM 5686 O O    . HOH   L 5 .   ? 21.565 2.160   21.205  1.00 28.72  ? 354 HOH   B O    1 
HETATM 5687 O O    . HOH   L 5 .   ? 37.800 -21.193 39.952  1.00 42.66  ? 355 HOH   B O    1 
HETATM 5688 O O    . HOH   L 5 .   ? 24.377 7.819   22.065  1.00 19.48  ? 356 HOH   B O    1 
HETATM 5689 O O    . HOH   L 5 .   ? 29.044 19.356  23.330  1.00 26.00  ? 357 HOH   B O    1 
HETATM 5690 O O    . HOH   L 5 .   ? 22.001 -19.646 30.105  1.00 34.89  ? 358 HOH   B O    1 
HETATM 5691 O O    . HOH   L 5 .   ? 28.785 -12.128 43.158  1.00 30.25  ? 359 HOH   B O    1 
HETATM 5692 O O    . HOH   L 5 .   ? 35.923 19.838  23.498  1.00 39.12  ? 360 HOH   B O    1 
HETATM 5693 O O    . HOH   L 5 .   ? 16.365 -0.949  31.331  1.00 20.39  ? 361 HOH   B O    1 
HETATM 5694 O O    . HOH   L 5 .   ? 20.956 -1.842  32.689  1.00 24.02  ? 362 HOH   B O    1 
HETATM 5695 O O    . HOH   L 5 .   ? 26.822 -14.692 44.023  1.00 46.01  ? 363 HOH   B O    1 
HETATM 5696 O O    . HOH   L 5 .   ? 26.783 -2.466  44.807  1.00 32.88  ? 364 HOH   B O    1 
HETATM 5697 O O    . HOH   L 5 .   ? 28.923 7.170   17.166  1.00 37.70  ? 365 HOH   B O    1 
HETATM 5698 O O    . HOH   L 5 .   ? 37.385 20.404  25.950  1.00 34.95  ? 366 HOH   B O    1 
HETATM 5699 O O    . HOH   L 5 .   ? 33.867 -15.894 35.636  1.00 16.62  ? 367 HOH   B O    1 
HETATM 5700 O O    . HOH   L 5 .   ? 12.083 -2.414  24.972  1.00 40.06  ? 368 HOH   B O    1 
HETATM 5701 O O    . HOH   L 5 .   ? 11.155 -9.287  42.352  1.00 41.89  ? 369 HOH   B O    1 
HETATM 5702 O O    . HOH   L 5 .   ? 31.020 16.696  21.089  1.00 32.15  ? 370 HOH   B O    1 
HETATM 5703 O O    . HOH   L 5 .   ? 25.476 17.195  25.150  1.00 23.11  ? 371 HOH   B O    1 
HETATM 5704 O O    . HOH   L 5 .   ? 24.802 -23.034 32.507  1.00 35.10  ? 372 HOH   B O    1 
HETATM 5705 O O    . HOH   L 5 .   ? 42.113 19.450  25.859  1.00 49.26  ? 373 HOH   B O    1 
HETATM 5706 O O    . HOH   L 5 .   ? 11.523 0.222   35.967  1.00 32.27  ? 374 HOH   B O    1 
HETATM 5707 O O    . HOH   L 5 .   ? 19.468 0.523   29.592  1.00 35.01  ? 375 HOH   B O    1 
HETATM 5708 O O    . HOH   L 5 .   ? 18.825 -12.786 43.508  1.00 51.56  ? 376 HOH   B O    1 
HETATM 5709 O O    . HOH   L 5 .   ? 50.662 24.612  40.726  1.00 38.76  ? 377 HOH   B O    1 
HETATM 5710 O O    . HOH   L 5 .   ? 56.109 19.651  35.487  1.00 32.04  ? 378 HOH   B O    1 
HETATM 5711 O O    . HOH   L 5 .   ? 26.087 -2.148  22.401  1.00 19.71  ? 379 HOH   B O    1 
HETATM 5712 O O    . HOH   L 5 .   ? 36.976 23.375  33.167  1.00 50.32  ? 380 HOH   B O    1 
HETATM 5713 O O    . HOH   L 5 .   ? 16.666 -5.940  26.626  1.00 36.22  ? 381 HOH   B O    1 
HETATM 5714 O O    . HOH   L 5 .   ? 24.416 -0.207  23.513  1.00 27.01  ? 382 HOH   B O    1 
HETATM 5715 O O    . HOH   L 5 .   ? 21.660 -8.440  23.533  1.00 39.24  ? 383 HOH   B O    1 
HETATM 5716 O O    . HOH   L 5 .   ? 55.248 22.587  36.764  1.00 29.50  ? 384 HOH   B O    1 
HETATM 5717 O O    . HOH   L 5 .   ? 34.381 8.881   40.643  1.00 27.38  ? 385 HOH   B O    1 
HETATM 5718 O O    . HOH   L 5 .   ? 24.772 -17.141 42.884  1.00 36.18  ? 386 HOH   B O    1 
HETATM 5719 O O    . HOH   L 5 .   ? 20.086 -1.813  45.446  1.00 32.31  ? 387 HOH   B O    1 
HETATM 5720 O O    . HOH   L 5 .   ? 24.851 -16.912 39.136  1.00 31.40  ? 388 HOH   B O    1 
HETATM 5721 O O    . HOH   L 5 .   ? 16.050 -10.720 42.732  1.00 34.51  ? 389 HOH   B O    1 
HETATM 5722 O O    . HOH   L 5 .   ? 31.390 -12.111 42.583  1.00 30.48  ? 390 HOH   B O    1 
HETATM 5723 O O    . HOH   L 5 .   ? 43.655 20.161  27.998  1.00 45.41  ? 391 HOH   B O    1 
HETATM 5724 O O    . HOH   L 5 .   ? 35.017 -11.584 24.261  1.00 32.09  ? 392 HOH   B O    1 
HETATM 5725 O O    . HOH   L 5 .   ? 38.127 8.719   23.368  1.00 48.05  ? 393 HOH   B O    1 
HETATM 5726 O O    . HOH   L 5 .   ? 13.734 -2.998  42.304  1.00 34.60  ? 394 HOH   B O    1 
HETATM 5727 O O    . HOH   L 5 .   ? 31.955 -19.743 30.093  1.00 45.11  ? 395 HOH   B O    1 
HETATM 5728 O O    . HOH   L 5 .   ? 54.352 13.376  28.527  1.00 45.21  ? 396 HOH   B O    1 
HETATM 5729 O O    . HOH   L 5 .   ? 42.925 -4.723  24.883  1.00 33.25  ? 397 HOH   B O    1 
HETATM 5730 O O    . HOH   L 5 .   ? 25.032 7.250   43.722  1.00 37.86  ? 398 HOH   B O    1 
HETATM 5731 O O    . HOH   L 5 .   ? 26.932 8.641   16.427  1.00 46.36  ? 399 HOH   B O    1 
HETATM 5732 O O    . HOH   L 5 .   ? 40.980 12.683  22.959  1.00 50.53  ? 400 HOH   B O    1 
HETATM 5733 O O    . HOH   L 5 .   ? 24.975 -4.816  44.517  1.00 31.29  ? 401 HOH   B O    1 
HETATM 5734 O O    . HOH   L 5 .   ? 34.901 24.780  30.417  1.00 33.23  ? 402 HOH   B O    1 
HETATM 5735 O O    . HOH   L 5 .   ? 16.609 5.984   38.302  1.00 37.08  ? 403 HOH   B O    1 
HETATM 5736 O O    . HOH   L 5 .   ? 49.194 25.264  34.591  1.00 38.67  ? 404 HOH   B O    1 
HETATM 5737 O O    . HOH   L 5 .   ? 22.014 -0.711  46.962  1.00 38.78  ? 405 HOH   B O    1 
HETATM 5738 O O    . HOH   L 5 .   ? 14.767 0.243   42.420  1.00 35.26  ? 406 HOH   B O    1 
HETATM 5739 O O    . HOH   L 5 .   ? 19.323 4.852   42.805  1.00 33.96  ? 407 HOH   B O    1 
HETATM 5740 O O    . HOH   L 5 .   ? 19.975 9.634   38.939  1.00 44.16  ? 408 HOH   B O    1 
HETATM 5741 O O    . HOH   L 5 .   ? 22.850 2.877   17.330  1.00 35.35  ? 409 HOH   B O    1 
HETATM 5742 O O    . HOH   L 5 .   ? 35.513 -22.072 38.900  1.00 39.99  ? 410 HOH   B O    1 
HETATM 5743 O O    . HOH   L 5 .   ? 19.634 -4.988  21.120  1.00 28.17  ? 411 HOH   B O    1 
HETATM 5744 O O    . HOH   L 5 .   ? 40.061 20.976  26.872  1.00 32.67  ? 412 HOH   B O    1 
HETATM 5745 O O    . HOH   L 5 .   ? 34.829 4.855   20.990  1.00 23.34  ? 413 HOH   B O    1 
HETATM 5746 O O    . HOH   L 5 .   ? 23.999 -13.966 24.929  1.00 38.38  ? 414 HOH   B O    1 
HETATM 5747 O O    . HOH   L 5 .   ? 52.945 20.689  29.656  1.00 35.18  ? 415 HOH   B O    1 
HETATM 5748 O O    . HOH   L 5 .   ? 34.053 -22.639 33.250  1.00 37.53  ? 416 HOH   B O    1 
HETATM 5749 O O    . HOH   L 5 .   ? 43.177 -8.054  22.218  1.00 45.75  ? 417 HOH   B O    1 
HETATM 5750 O O    . HOH   L 5 .   ? 23.295 21.824  20.406  1.00 42.90  ? 418 HOH   B O    1 
HETATM 5751 O O    . HOH   L 5 .   ? 36.423 4.577   40.582  1.00 30.27  ? 419 HOH   B O    1 
HETATM 5752 O O    . HOH   L 5 .   ? 23.199 -1.992  16.023  1.00 24.91  ? 420 HOH   B O    1 
HETATM 5753 O O    . HOH   L 5 .   ? 41.911 7.647   28.486  1.00 35.53  ? 421 HOH   B O    1 
HETATM 5754 O O    . HOH   L 5 .   ? 33.014 -0.516  44.272  1.00 33.22  ? 422 HOH   B O    1 
HETATM 5755 O O    . HOH   L 5 .   ? 34.505 12.152  23.144  1.00 26.67  ? 423 HOH   B O    1 
HETATM 5756 O O    . HOH   L 5 .   ? 18.617 -13.662 40.688  1.00 31.34  ? 424 HOH   B O    1 
HETATM 5757 O O    . HOH   L 5 .   ? 27.361 0.494   45.852  1.00 54.25  ? 425 HOH   B O    1 
HETATM 5758 O O    . HOH   L 5 .   ? 41.828 -16.322 43.792  1.00 47.14  ? 426 HOH   B O    1 
HETATM 5759 O O    . HOH   L 5 .   ? 15.701 -2.735  20.031  1.00 46.91  ? 427 HOH   B O    1 
HETATM 5760 O O    . HOH   L 5 .   ? 21.067 -16.959 28.370  1.00 54.92  ? 428 HOH   B O    1 
HETATM 5761 O O    . HOH   L 5 .   ? 38.867 2.824   32.347  1.00 22.46  ? 429 HOH   B O    1 
HETATM 5762 O O    . HOH   L 5 .   ? 27.129 -19.708 41.992  1.00 45.14  ? 430 HOH   B O    1 
HETATM 5763 O O    . HOH   L 5 .   ? 15.401 -0.198  18.428  1.00 46.07  ? 431 HOH   B O    1 
HETATM 5764 O O    . HOH   L 5 .   ? 18.750 -0.280  32.679  1.00 29.09  ? 432 HOH   B O    1 
HETATM 5765 O O    . HOH   L 5 .   ? 17.277 -14.882 44.023  1.00 56.62  ? 433 HOH   B O    1 
HETATM 5766 O O    . HOH   L 5 .   ? 23.696 24.030  25.223  1.00 34.27  ? 434 HOH   B O    1 
HETATM 5767 O O    . HOH   L 5 .   ? 57.283 25.888  28.464  1.00 57.64  ? 435 HOH   B O    1 
HETATM 5768 O O    . HOH   L 5 .   ? 55.431 20.866  28.319  1.00 56.76  ? 436 HOH   B O    1 
HETATM 5769 O O    . HOH   L 5 .   ? 34.690 14.393  21.479  1.00 52.60  ? 437 HOH   B O    1 
HETATM 5770 O O    . HOH   L 5 .   ? 45.217 23.949  32.020  1.00 56.83  ? 438 HOH   B O    1 
HETATM 5771 O O    . HOH   L 5 .   ? 17.643 -3.860  19.179  1.00 44.19  ? 439 HOH   B O    1 
HETATM 5772 O O    . HOH   L 5 .   ? 39.301 4.477   34.521  0.50 22.99  ? 440 HOH   B O    1 
HETATM 5773 O O    . HOH   L 5 .   ? 36.773 -10.756 21.874  1.00 55.20  ? 441 HOH   B O    1 
HETATM 5774 O O    . HOH   L 5 .   ? 20.265 2.895   19.075  1.00 32.80  ? 442 HOH   B O    1 
HETATM 5775 O O    . HOH   L 5 .   ? 22.619 1.338   33.779  1.00 40.27  ? 443 HOH   B O    1 
HETATM 5776 O O    . HOH   L 5 .   ? 41.499 -23.155 35.535  1.00 67.02  ? 444 HOH   B O    1 
HETATM 5777 O O    . HOH   L 5 .   ? 37.299 5.702   21.911  1.00 30.16  ? 445 HOH   B O    1 
HETATM 5778 O O    . HOH   L 5 .   ? 39.833 6.876   24.797  1.00 37.53  ? 446 HOH   B O    1 
HETATM 5779 O O    . HOH   L 5 .   ? 40.128 -0.804  21.161  1.00 48.46  ? 447 HOH   B O    1 
HETATM 5780 O O    . HOH   L 5 .   ? 24.176 -11.341 22.760  1.00 45.46  ? 448 HOH   B O    1 
HETATM 5781 O O    . HOH   L 5 .   ? 25.459 10.685  14.264  1.00 45.32  ? 449 HOH   B O    1 
HETATM 5782 O O    . HOH   L 5 .   ? 28.503 -6.036  45.806  1.00 55.90  ? 450 HOH   B O    1 
HETATM 5783 O O    . HOH   L 5 .   ? 34.768 -17.581 43.895  1.00 48.23  ? 451 HOH   B O    1 
HETATM 5784 O O    . HOH   L 5 .   ? 29.493 -14.880 44.632  1.00 58.42  ? 452 HOH   B O    1 
HETATM 5785 O O    . HOH   L 5 .   ? 39.269 4.621   23.049  1.00 32.31  ? 453 HOH   B O    1 
HETATM 5786 O O    . HOH   L 5 .   ? 39.899 -1.351  23.630  1.00 46.35  ? 454 HOH   B O    1 
HETATM 5787 O O    . HOH   L 5 .   ? 30.484 21.539  22.725  1.00 35.80  ? 455 HOH   B O    1 
HETATM 5788 O O    . HOH   L 5 .   ? 24.487 3.058   33.616  1.00 46.21  ? 456 HOH   B O    1 
HETATM 5789 O O    . HOH   L 5 .   ? 13.515 -4.501  21.021  1.00 54.75  ? 457 HOH   B O    1 
HETATM 5790 O O    . HOH   L 5 .   ? 37.988 6.692   18.637  1.00 51.99  ? 458 HOH   B O    1 
HETATM 5791 O O    . HOH   L 5 .   ? 23.764 -21.981 30.287  1.00 44.63  ? 459 HOH   B O    1 
HETATM 5792 O O    . HOH   L 5 .   ? 19.177 -7.236  22.781  1.00 43.06  ? 460 HOH   B O    1 
HETATM 5793 O O    . HOH   L 5 .   ? 42.592 3.016   25.691  1.00 39.79  ? 461 HOH   B O    1 
HETATM 5794 O O    . HOH   L 5 .   ? 31.413 -19.175 43.850  1.00 54.44  ? 462 HOH   B O    1 
HETATM 5795 O O    . HOH   L 5 .   ? 23.093 24.134  22.695  1.00 48.65  ? 463 HOH   B O    1 
HETATM 5796 O O    . HOH   L 5 .   ? 30.449 24.354  24.565  1.00 50.55  ? 464 HOH   B O    1 
HETATM 5797 O O    . HOH   L 5 .   ? 46.651 24.272  37.188  1.00 45.92  ? 465 HOH   B O    1 
HETATM 5798 O O    . HOH   L 5 .   ? 27.869 -8.030  45.089  1.00 55.25  ? 466 HOH   B O    1 
HETATM 5799 O O    . HOH   L 5 .   ? 30.944 -20.185 27.932  1.00 41.07  ? 467 HOH   B O    1 
HETATM 5800 O O    . HOH   L 5 .   ? 19.282 -1.450  17.318  1.00 58.43  ? 468 HOH   B O    1 
HETATM 5801 O O    . HOH   L 5 .   ? 17.576 -1.985  46.348  1.00 49.81  ? 469 HOH   B O    1 
HETATM 5802 O O    . HOH   L 5 .   ? 57.020 9.318   28.493  1.00 49.14  ? 470 HOH   B O    1 
HETATM 5803 O O    . HOH   L 5 .   ? 22.986 -20.379 36.391  1.00 47.06  ? 471 HOH   B O    1 
HETATM 5804 O O    . HOH   L 5 .   ? 60.701 6.504   28.398  1.00 43.36  ? 472 HOH   B O    1 
HETATM 5805 O O    . HOH   L 5 .   ? 40.976 2.551   23.467  1.00 36.22  ? 473 HOH   B O    1 
HETATM 5806 O O    . HOH   L 5 .   ? 22.253 -10.406 22.315  1.00 49.81  ? 474 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   . THR A 30  ? 0.7353 0.5846 1.2489 -0.0060 0.0032  0.1442  10  THR A N   
2    C CA  . THR A 30  ? 0.7151 0.5873 1.1355 0.0176  0.0021  0.1685  10  THR A CA  
3    C C   . THR A 30  ? 0.7185 0.5628 1.2454 0.0412  0.0019  0.1971  10  THR A C   
4    O O   . THR A 30  ? 0.7121 0.5265 1.2642 0.0472  -0.0062 0.2331  10  THR A O   
14   N N   . SER A 31  ? 0.7301 0.5712 1.2588 0.0528  0.0112  0.1846  11  SER A N   
15   C CA  . SER A 31  ? 0.7299 0.5568 1.2372 0.0792  0.0314  0.1662  11  SER A CA  
16   C C   . SER A 31  ? 0.6758 0.4732 1.1770 0.1048  0.0694  0.1405  11  SER A C   
17   O O   . SER A 31  ? 0.6613 0.4136 1.1568 0.1365  0.0868  0.1276  11  SER A O   
18   C CB  . SER A 31  ? 0.7619 0.6121 1.2585 0.0854  0.0213  0.1541  11  SER A CB  
21   N N   . GLU A 32  ? 0.6248 0.4528 1.1320 0.0941  0.0965  0.1322  12  GLU A N   
22   C CA  . GLU A 32  ? 0.5802 0.4280 1.0922 0.0907  0.1219  0.1298  12  GLU A CA  
23   C C   . GLU A 32  ? 0.5304 0.4142 1.0674 0.0860  0.1452  0.1238  12  GLU A C   
24   O O   . GLU A 32  ? 0.4902 0.3855 1.0499 0.1302  0.1731  0.1268  12  GLU A O   
25   C CB  . GLU A 32  ? 0.5805 0.4768 1.0846 0.0609  0.1278  0.1288  12  GLU A CB  
28   N N   . ASN A 33  ? 0.5160 0.4465 1.0764 0.0303  0.1311  0.1296  13  ASN A N   
29   C CA  . ASN A 33  ? 0.5225 0.4595 1.0951 -0.0173 0.0941  0.1232  13  ASN A CA  
30   C C   . ASN A 33  ? 0.4569 0.3802 1.0328 -0.0105 0.0823  0.0994  13  ASN A C   
31   O O   . ASN A 33  ? 0.4064 0.3134 1.0223 -0.0273 0.0632  0.0973  13  ASN A O   
32   C CB  . ASN A 33  ? 0.5924 0.5375 1.1770 -0.0480 0.0715  0.1257  13  ASN A CB  
33   C CG  . ASN A 33  ? 0.6684 0.6095 1.2531 -0.0585 0.0549  0.1191  13  ASN A CG  
34   O OD1 . ASN A 33  ? 0.6977 0.6215 1.2861 -0.0726 0.0478  0.1258  13  ASN A OD1 
35   N ND2 . ASN A 33  ? 0.6923 0.6501 1.2732 -0.0502 0.0468  0.1070  13  ASN A ND2 
42   N N   . ARG A 34  ? 0.4389 0.3477 0.9921 0.0325  0.0855  0.0725  14  ARG A N   
43   C CA  . ARG A 34  ? 0.4284 0.3053 0.9635 0.0641  0.0793  0.0606  14  ARG A CA  
44   C C   . ARG A 34  ? 0.3741 0.2817 0.8762 0.0718  0.1087  0.0639  14  ARG A C   
45   O O   . ARG A 34  ? 0.3780 0.2655 0.8303 0.0443  0.0940  0.0351  14  ARG A O   
46   C CB  . ARG A 34  ? 0.5020 0.3201 1.0272 0.0656  0.0664  0.0655  14  ARG A CB  
47   C CG  . ARG A 34  ? 0.5872 0.3870 1.1137 0.0422  0.0529  0.0675  14  ARG A CG  
48   C CD  . ARG A 34  ? 0.6593 0.4663 1.1991 0.0464  0.0313  0.1035  14  ARG A CD  
49   N NE  . ARG A 34  ? 0.7182 0.5140 1.2801 0.0122  0.0174  0.1216  14  ARG A NE  
50   C CZ  . ARG A 34  ? 0.7529 0.5281 1.3458 -0.0348 0.0305  0.1379  14  ARG A CZ  
51   N NH1 . ARG A 34  ? 0.7441 0.4948 1.3553 -0.0503 0.0417  0.1576  14  ARG A NH1 
52   N NH2 . ARG A 34  ? 0.7742 0.5533 1.3723 -0.0502 0.0287  0.1342  14  ARG A NH2 
66   N N   . ALA A 35  ? 0.3448 0.2730 0.8320 0.0721  0.1544  0.0638  15  ALA A N   
67   C CA  . ALA A 35  ? 0.3471 0.3060 0.7779 0.0863  0.1443  0.0555  15  ALA A CA  
68   C C   . ALA A 35  ? 0.3351 0.2788 0.7254 0.0860  0.1309  0.1018  15  ALA A C   
69   O O   . ALA A 35  ? 0.3232 0.2887 0.6775 0.0751  0.1287  0.0996  15  ALA A O   
70   C CB  . ALA A 35  ? 0.3549 0.3522 0.7652 0.1002  0.1448  0.0359  15  ALA A CB  
76   N N   . GLN A 36  ? 0.3298 0.2694 0.7343 0.0897  0.1360  0.1143  16  GLN A N   
77   C CA  . GLN A 36  ? 0.3020 0.2760 0.7215 0.0736  0.1254  0.1017  16  GLN A CA  
78   C C   . GLN A 36  ? 0.2601 0.2520 0.7366 0.0214  0.0769  0.0669  16  GLN A C   
79   O O   . GLN A 36  ? 0.2435 0.2317 0.7202 0.0055  0.0573  0.0540  16  GLN A O   
93   N N   . VAL A 37  ? 0.2862 0.2423 0.7426 0.0135  0.0214  0.0457  17  VAL A N   
94   C CA  . VAL A 37  ? 0.3305 0.2548 0.7697 -0.0112 -0.0095 0.0308  17  VAL A CA  
95   C C   . VAL A 37  ? 0.3117 0.2419 0.7370 -0.0062 -0.0129 0.0157  17  VAL A C   
96   O O   . VAL A 37  ? 0.3027 0.2124 0.7135 -0.0295 -0.0651 0.0160  17  VAL A O   
97   C CB  . VAL A 37  ? 0.3684 0.3026 0.8241 -0.0273 -0.0038 0.0399  17  VAL A CB  
98   C CG1 . VAL A 37  ? 0.4253 0.3352 0.8442 -0.0267 -0.0111 0.0398  17  VAL A CG1 
99   C CG2 . VAL A 37  ? 0.3597 0.3419 0.8431 -0.0267 -0.0024 0.0589  17  VAL A CG2 
109  N N   . ALA A 38  ? 0.3052 0.2277 0.7217 0.0147  0.0282  0.0127  18  ALA A N   
110  C CA  . ALA A 38  ? 0.3003 0.2220 0.6724 0.0219  0.0223  0.0078  18  ALA A CA  
111  C C   . ALA A 38  ? 0.2894 0.2510 0.5863 0.0216  0.0024  0.0426  18  ALA A C   
112  O O   . ALA A 38  ? 0.2766 0.2304 0.5766 0.0313  0.0159  0.0614  18  ALA A O   
113  C CB  . ALA A 38  ? 0.3151 0.2181 0.6822 0.0077  0.0441  0.0193  18  ALA A CB  
153  N N   . GLN A 41  ? 0.2417 0.2397 0.6011 -0.0265 -0.0171 -0.0547 21  GLN A N   
154  C CA  . GLN A 41  ? 0.2736 0.2349 0.6532 -0.0174 -0.0273 -0.0856 21  GLN A CA  
155  C C   . GLN A 41  ? 0.2617 0.2437 0.5973 0.0215  -0.0644 -0.0979 21  GLN A C   
156  O O   . GLN A 41  ? 0.2617 0.2741 0.6084 0.0025  -0.0644 -0.1029 21  GLN A O   
157  C CB  . GLN A 41  ? 0.3460 0.2338 0.7421 -0.0431 -0.0443 -0.0612 21  GLN A CB  
158  C CG  . GLN A 41  ? 0.3831 0.2651 0.8287 -0.0405 -0.0706 -0.0832 21  GLN A CG  
159  C CD  . GLN A 41  ? 0.4422 0.3407 0.9177 -0.0146 -0.0744 -0.0853 21  GLN A CD  
160  O OE1 . GLN A 41  ? 0.4773 0.3760 0.9650 0.0404  -0.0340 -0.1281 21  GLN A OE1 
161  N NE2 . GLN A 41  ? 0.4730 0.3915 0.9408 -0.0163 -0.0965 -0.0455 21  GLN A NE2 
170  N N   . HIS A 42  ? 0.2462 0.2077 0.5516 0.0327  -0.0648 -0.0356 22  HIS A N   
171  C CA  . HIS A 42  ? 0.2314 0.1949 0.5380 0.0415  -0.0408 -0.0659 22  HIS A CA  
172  C C   . HIS A 42  ? 0.2122 0.2217 0.5125 0.0389  -0.0364 -0.0820 22  HIS A C   
173  O O   . HIS A 42  ? 0.2144 0.2419 0.4968 0.0595  -0.0436 -0.0827 22  HIS A O   
174  C CB  . HIS A 42  ? 0.2457 0.1900 0.5422 0.0419  -0.0369 -0.0499 22  HIS A CB  
175  C CG  . HIS A 42  ? 0.2274 0.2371 0.5112 0.0510  -0.0450 -0.0477 22  HIS A CG  
176  N ND1 . HIS A 42  ? 0.2375 0.2792 0.5073 0.0655  -0.0584 -0.0787 22  HIS A ND1 
177  C CD2 . HIS A 42  ? 0.2057 0.2204 0.4765 0.0378  -0.0418 -0.0574 22  HIS A CD2 
178  C CE1 . HIS A 42  ? 0.2196 0.2655 0.4830 0.0536  -0.0484 -0.1073 22  HIS A CE1 
179  N NE2 . HIS A 42  ? 0.1865 0.2380 0.4699 0.0254  -0.0401 -0.0675 22  HIS A NE2 
187  N N   . ASN A 43  ? 0.1848 0.1890 0.5001 0.0221  -0.0183 -0.0643 23  ASN A N   
188  C CA  . ASN A 43  ? 0.1716 0.1621 0.4885 0.0096  -0.0138 -0.0406 23  ASN A CA  
189  C C   . ASN A 43  ? 0.1863 0.1719 0.4677 0.0246  -0.0214 -0.0548 23  ASN A C   
190  O O   . ASN A 43  ? 0.2024 0.1734 0.4426 0.0036  -0.0112 -0.0410 23  ASN A O   
191  C CB  . ASN A 43  ? 0.1913 0.1825 0.4797 0.0088  -0.0094 -0.0004 23  ASN A CB  
192  C CG  . ASN A 43  ? 0.2107 0.1811 0.4748 0.0384  -0.0146 0.0134  23  ASN A CG  
193  O OD1 . ASN A 43  ? 0.2195 0.2036 0.4321 0.0107  -0.0232 0.0249  23  ASN A OD1 
194  N ND2 . ASN A 43  ? 0.2258 0.2066 0.5315 0.0349  0.0057  0.0231  23  ASN A ND2 
201  N N   . ARG A 44  ? 0.1990 0.1952 0.4767 0.0142  -0.0027 -0.0661 24  ARG A N   
202  C CA  . ARG A 44  ? 0.2024 0.2084 0.5029 -0.0205 -0.0374 -0.0888 24  ARG A CA  
203  C C   . ARG A 44  ? 0.2193 0.1980 0.4981 0.0208  -0.0290 -0.1246 24  ARG A C   
204  O O   . ARG A 44  ? 0.2055 0.2145 0.4869 0.0144  -0.0490 -0.1053 24  ARG A O   
205  C CB  . ARG A 44  ? 0.2365 0.2106 0.5475 -0.0106 -0.0414 -0.0750 24  ARG A CB  
206  C CG  . ARG A 44  ? 0.3616 0.2973 0.5814 -0.0519 -0.1033 -0.0909 24  ARG A CG  
207  C CD  . ARG A 44  ? 0.4591 0.3657 0.6367 -0.0364 -0.1330 -0.0629 24  ARG A CD  
208  N NE  . ARG A 44  ? 0.5265 0.4741 0.7129 -0.0110 -0.1317 -0.1018 24  ARG A NE  
209  C CZ  . ARG A 44  ? 0.5492 0.5070 0.7658 0.0019  -0.1099 -0.0956 24  ARG A CZ  
210  N NH1 . ARG A 44  ? 0.5683 0.5480 0.7959 -0.0003 -0.0960 -0.0648 24  ARG A NH1 
211  N NH2 . ARG A 44  ? 0.5603 0.5074 0.7867 -0.0067 -0.0982 -0.0838 24  ARG A NH2 
225  N N   . LYS A 45  ? 0.2400 0.2067 0.4877 0.0229  -0.0139 -0.0898 25  LYS A N   
226  C CA  . LYS A 45  ? 0.2588 0.2058 0.5014 0.0119  -0.0078 -0.1111 25  LYS A CA  
227  C C   . LYS A 45  ? 0.2187 0.2356 0.4561 0.0358  -0.0246 -0.1009 25  LYS A C   
228  O O   . LYS A 45  ? 0.1898 0.2443 0.4497 0.0520  -0.0234 -0.1092 25  LYS A O   
229  C CB  . LYS A 45  ? 0.3095 0.2130 0.5565 0.0438  -0.0290 -0.1437 25  LYS A CB  
230  C CG  . LYS A 45  ? 0.3690 0.3156 0.6604 0.0703  -0.0297 -0.1134 25  LYS A CG  
231  C CD  . LYS A 45  ? 0.4599 0.4235 0.7573 0.0669  0.0116  -0.1193 25  LYS A CD  
232  C CE  . LYS A 45  ? 0.5359 0.5292 0.8282 0.0616  0.0167  -0.1056 25  LYS A CE  
233  N NZ  . LYS A 45  ? 0.5855 0.5828 0.8594 0.0488  0.0142  -0.1003 25  LYS A NZ  
247  N N   . ILE A 46  ? 0.1984 0.2209 0.4031 0.0262  -0.0449 -0.0808 26  ILE A N   
248  C CA  . ILE A 46  ? 0.1862 0.2033 0.3714 0.0190  -0.0377 -0.0745 26  ILE A CA  
249  C C   . ILE A 46  ? 0.1746 0.2209 0.3768 0.0342  -0.0237 -0.0704 26  ILE A C   
250  O O   . ILE A 46  ? 0.1773 0.2088 0.3731 0.0367  -0.0070 -0.0696 26  ILE A O   
251  C CB  . ILE A 46  ? 0.2029 0.1886 0.3797 0.0358  -0.0477 -0.0493 26  ILE A CB  
252  C CG1 . ILE A 46  ? 0.2224 0.2127 0.4433 0.0337  -0.0373 -0.0234 26  ILE A CG1 
253  C CG2 . ILE A 46  ? 0.2118 0.2034 0.3684 0.0176  -0.0328 -0.0584 26  ILE A CG2 
254  C CD1 . ILE A 46  ? 0.2454 0.2757 0.4990 0.0356  -0.0359 -0.0241 26  ILE A CD1 
266  N N   . VAL A 47  ? 0.1749 0.2048 0.3779 0.0242  -0.0191 -0.0660 27  VAL A N   
267  C CA  . VAL A 47  ? 0.1658 0.2112 0.3600 0.0131  -0.0038 -0.0510 27  VAL A CA  
268  C C   . VAL A 47  ? 0.1679 0.2094 0.3578 0.0153  -0.0089 -0.0697 27  VAL A C   
269  O O   . VAL A 47  ? 0.1605 0.2099 0.3414 0.0190  -0.0002 -0.0569 27  VAL A O   
270  C CB  . VAL A 47  ? 0.1720 0.1794 0.3452 0.0161  0.0006  -0.0571 27  VAL A CB  
271  C CG1 . VAL A 47  ? 0.1675 0.2128 0.3666 0.0209  0.0067  -0.0362 27  VAL A CG1 
272  C CG2 . VAL A 47  ? 0.1872 0.1884 0.3713 0.0024  0.0004  -0.0390 27  VAL A CG2 
282  N N   . GLU A 48  ? 0.1758 0.2246 0.3716 0.0098  -0.0082 -0.0717 28  GLU A N   
283  C CA  . GLU A 48  ? 0.2053 0.2629 0.3750 0.0040  0.0002  -0.1006 28  GLU A CA  
284  C C   . GLU A 48  ? 0.2241 0.2479 0.3414 0.0276  0.0087  -0.0988 28  GLU A C   
285  O O   . GLU A 48  ? 0.2503 0.2782 0.3204 0.0422  0.0081  -0.0947 28  GLU A O   
286  C CB  . GLU A 48  ? 0.2613 0.2912 0.4443 -0.0328 0.0217  -0.1433 28  GLU A CB  
287  C CG  . GLU A 48  ? 0.3320 0.3672 0.5377 -0.0440 0.0067  -0.1513 28  GLU A CG  
288  C CD  . GLU A 48  ? 0.4433 0.5074 0.6394 -0.0344 -0.0064 -0.1743 28  GLU A CD  
289  O OE1 . GLU A 48  ? 0.5292 0.5575 0.6700 -0.0171 -0.0199 -0.2254 28  GLU A OE1 
290  O OE2 . GLU A 48  ? 0.4896 0.5772 0.6943 -0.0476 0.0029  -0.1515 28  GLU A OE2 
297  N N   . GLN A 49  ? 0.2108 0.2181 0.3335 0.0183  0.0257  -0.0709 29  GLN A N   
298  C CA  . GLN A 49  ? 0.2187 0.2552 0.3431 0.0261  0.0380  -0.0914 29  GLN A CA  
299  C C   . GLN A 49  ? 0.2046 0.2598 0.3179 0.0236  0.0108  -0.0771 29  GLN A C   
300  O O   . GLN A 49  ? 0.2264 0.2644 0.3217 0.0247  0.0213  -0.0680 29  GLN A O   
301  C CB  . GLN A 49  ? 0.2313 0.2500 0.4082 0.0290  0.0227  -0.1049 29  GLN A CB  
302  C CG  . GLN A 49  ? 0.2362 0.2652 0.4650 0.0348  -0.0198 -0.1300 29  GLN A CG  
303  C CD  . GLN A 49  ? 0.2681 0.3382 0.5031 0.0852  -0.0418 -0.1282 29  GLN A CD  
304  O OE1 . GLN A 49  ? 0.3218 0.4006 0.5371 0.1245  -0.0527 -0.1345 29  GLN A OE1 
305  N NE2 . GLN A 49  ? 0.2625 0.3772 0.5145 0.0326  -0.0220 -0.1089 29  GLN A NE2 
314  N N   . TYR A 50  ? 0.1817 0.2338 0.3060 0.0163  -0.0072 -0.0727 30  TYR A N   
315  C CA  . TYR A 50  ? 0.1791 0.2132 0.2931 0.0207  0.0036  -0.0721 30  TYR A CA  
316  C C   . TYR A 50  ? 0.1851 0.2225 0.2950 0.0272  0.0193  -0.0821 30  TYR A C   
317  O O   . TYR A 50  ? 0.1990 0.2257 0.2661 0.0026  0.0218  -0.0585 30  TYR A O   
318  C CB  . TYR A 50  ? 0.1857 0.2139 0.2806 0.0321  0.0146  -0.0550 30  TYR A CB  
319  C CG  . TYR A 50  ? 0.1661 0.2219 0.2510 0.0388  0.0170  -0.0290 30  TYR A CG  
320  C CD1 . TYR A 50  ? 0.1767 0.2296 0.2296 0.0304  0.0161  -0.0391 30  TYR A CD1 
321  C CD2 . TYR A 50  ? 0.1621 0.2269 0.2732 0.0237  0.0137  -0.0087 30  TYR A CD2 
322  C CE1 . TYR A 50  ? 0.1917 0.2118 0.2518 0.0159  -0.0098 -0.0537 30  TYR A CE1 
323  C CE2 . TYR A 50  ? 0.1705 0.2085 0.2935 0.0276  0.0103  -0.0254 30  TYR A CE2 
324  C CZ  . TYR A 50  ? 0.1867 0.2063 0.2758 0.0146  0.0165  -0.0404 30  TYR A CZ  
325  O OH  . TYR A 50  ? 0.2357 0.2352 0.2904 0.0250  0.0178  -0.0647 30  TYR A OH  
335  N N   . MET A 51  ? 0.1719 0.2297 0.2964 0.0128  0.0012  -0.0788 31  MET A N   
336  C CA  . MET A 51  ? 0.1876 0.2368 0.2928 0.0189  -0.0064 -0.0823 31  MET A CA  
337  C C   . MET A 51  ? 0.2054 0.2561 0.2532 0.0375  0.0019  -0.0729 31  MET A C   
338  O O   . MET A 51  ? 0.2091 0.2794 0.2343 0.0484  0.0059  -0.0525 31  MET A O   
339  C CB  . MET A 51  ? 0.1686 0.2641 0.3271 0.0157  0.0055  -0.0765 31  MET A CB  
340  C CG  . MET A 51  ? 0.1790 0.2333 0.3336 0.0145  0.0099  -0.0601 31  MET A CG  
341  S SD  . MET A 51  ? 0.1737 0.2235 0.2910 0.0146  0.0057  -0.0375 31  MET A SD  
342  C CE  . MET A 51  ? 0.2003 0.2237 0.2825 0.0183  0.0048  -0.0109 31  MET A CE  
352  N N   A HIS A 52  ? 0.2202 0.2787 0.2366 0.0363  -0.0001 -0.0921 32  HIS A N   
353  N N   B HIS A 52  ? 0.2209 0.2786 0.2370 0.0362  -0.0004 -0.0919 32  HIS A N   
354  C CA  A HIS A 52  ? 0.2614 0.2885 0.2483 0.0080  0.0009  -0.1132 32  HIS A CA  
355  C CA  B HIS A 52  ? 0.2616 0.2887 0.2483 0.0083  0.0000  -0.1127 32  HIS A CA  
356  C C   A HIS A 52  ? 0.2560 0.2791 0.2578 0.0110  -0.0008 -0.1045 32  HIS A C   
357  C C   B HIS A 52  ? 0.2558 0.2799 0.2578 0.0121  -0.0016 -0.1036 32  HIS A C   
358  O O   A HIS A 52  ? 0.2975 0.3422 0.2864 -0.0032 0.0029  -0.0950 32  HIS A O   
359  O O   B HIS A 52  ? 0.2950 0.3406 0.2855 0.0019  0.0036  -0.0972 32  HIS A O   
360  C CB  A HIS A 52  ? 0.3216 0.3369 0.2827 -0.0177 0.0083  -0.1506 32  HIS A CB  
361  C CB  B HIS A 52  ? 0.3215 0.3378 0.2826 -0.0191 0.0061  -0.1499 32  HIS A CB  
362  C CG  A HIS A 52  ? 0.3857 0.4132 0.3637 -0.0811 -0.0338 -0.1657 32  HIS A CG  
363  C CG  B HIS A 52  ? 0.3899 0.4201 0.3688 -0.0789 -0.0349 -0.1596 32  HIS A CG  
364  N ND1 A HIS A 52  ? 0.4255 0.4652 0.4416 -0.0701 -0.0644 -0.1652 32  HIS A ND1 
365  N ND1 B HIS A 52  ? 0.4307 0.4770 0.4434 -0.0686 -0.0605 -0.1586 32  HIS A ND1 
366  C CD2 A HIS A 52  ? 0.4291 0.4921 0.4193 -0.0872 -0.0541 -0.1158 32  HIS A CD2 
367  C CD2 B HIS A 52  ? 0.4351 0.4925 0.4250 -0.0896 -0.0619 -0.1190 32  HIS A CD2 
368  C CE1 A HIS A 52  ? 0.4425 0.5075 0.4641 -0.0600 -0.0778 -0.1391 32  HIS A CE1 
369  C CE1 B HIS A 52  ? 0.4427 0.5095 0.4622 -0.0631 -0.0813 -0.1400 32  HIS A CE1 
370  N NE2 A HIS A 52  ? 0.4368 0.5059 0.4505 -0.0845 -0.0802 -0.1357 32  HIS A NE2 
371  N NE2 B HIS A 52  ? 0.4461 0.5167 0.4560 -0.0890 -0.0824 -0.1332 32  HIS A NE2 
386  N N   . THR A 53  ? 0.2233 0.2850 0.2559 0.0294  0.0062  -0.0785 33  THR A N   
387  C CA  . THR A 53  ? 0.2229 0.2990 0.2762 0.0007  0.0167  -0.0618 33  THR A CA  
388  C C   . THR A 53  ? 0.2368 0.3412 0.2839 0.0037  0.0186  -0.0337 33  THR A C   
389  O O   . THR A 53  ? 0.2474 0.3329 0.3075 0.0055  0.0437  -0.0574 33  THR A O   
390  C CB  . THR A 53  ? 0.2253 0.2876 0.2943 -0.0063 0.0121  -0.0605 33  THR A CB  
391  O OG1 . THR A 53  ? 0.2219 0.2909 0.3465 -0.0146 0.0037  -0.0583 33  THR A OG1 
392  C CG2 . THR A 53  ? 0.2424 0.2800 0.3327 -0.0216 0.0255  -0.0360 33  THR A CG2 
401  N N   . ARG A 54  ? 0.2525 0.3325 0.2584 0.0158  -0.0124 0.0001  34  ARG A N   
402  C CA  . ARG A 54  ? 0.2921 0.3475 0.2877 0.0177  0.0099  0.0001  34  ARG A CA  
403  C C   . ARG A 54  ? 0.2669 0.3561 0.2779 0.0185  0.0289  -0.0252 34  ARG A C   
404  O O   . ARG A 54  ? 0.2692 0.3715 0.3115 0.0292  0.0352  -0.0119 34  ARG A O   
425  N N   . GLY A 55  ? 0.2481 0.3770 0.2722 0.0019  0.0488  -0.0057 35  GLY A N   
426  C CA  . GLY A 55  ? 0.2396 0.3859 0.3029 0.0057  0.0583  -0.0266 35  GLY A CA  
427  C C   . GLY A 55  ? 0.2525 0.3835 0.2967 0.0230  0.0666  0.0013  35  GLY A C   
428  O O   . GLY A 55  ? 0.2358 0.3587 0.2837 0.0128  0.0548  -0.0154 35  GLY A O   
432  N N   . GLU A 56  ? 0.2636 0.4256 0.3400 0.0055  0.0617  0.0373  36  GLU A N   
433  C CA  . GLU A 56  ? 0.2556 0.4734 0.3437 0.0087  0.0783  0.0278  36  GLU A CA  
434  C C   . GLU A 56  ? 0.2299 0.4307 0.3268 0.0077  0.0653  -0.0020 36  GLU A C   
435  O O   . GLU A 56  ? 0.2318 0.4300 0.3251 -0.0005 0.0508  0.0194  36  GLU A O   
436  C CB  . GLU A 56  ? 0.3367 0.5808 0.3985 0.0110  0.1168  0.0764  36  GLU A CB  
437  C CG  . GLU A 56  ? 0.4737 0.6932 0.5123 0.0215  0.1103  0.0580  36  GLU A CG  
438  C CD  . GLU A 56  ? 0.6004 0.7911 0.6139 0.0243  0.0650  0.0297  36  GLU A CD  
439  O OE1 . GLU A 56  ? 0.6259 0.8332 0.6447 0.0395  0.0234  0.0193  36  GLU A OE1 
440  O OE2 . GLU A 56  ? 0.6658 0.8217 0.6583 0.0131  0.0635  0.0143  36  GLU A OE2 
447  N N   . ALA A 57  ? 0.2281 0.3982 0.3192 0.0265  0.0467  -0.0407 37  ALA A N   
448  C CA  . ALA A 57  ? 0.2202 0.3617 0.3317 0.0278  0.0471  -0.0541 37  ALA A CA  
449  C C   . ALA A 57  ? 0.1998 0.3114 0.3294 0.0125  0.0272  -0.0463 37  ALA A C   
450  O O   . ALA A 57  ? 0.2030 0.3091 0.3334 0.0198  0.0166  -0.0284 37  ALA A O   
451  C CB  . ALA A 57  ? 0.2722 0.3538 0.3634 0.0671  0.0224  -0.0661 37  ALA A CB  
457  N N   . ARG A 58  ? 0.2142 0.2771 0.2840 -0.0120 0.0267  -0.0245 38  ARG A N   
458  C CA  . ARG A 58  ? 0.2218 0.2457 0.2696 -0.0142 0.0379  0.0013  38  ARG A CA  
459  C C   . ARG A 58  ? 0.2175 0.2754 0.2826 -0.0144 0.0513  0.0113  38  ARG A C   
460  O O   . ARG A 58  ? 0.2241 0.2637 0.2969 0.0016  0.0281  -0.0025 38  ARG A O   
461  C CB  . ARG A 58  ? 0.2476 0.2405 0.2900 0.0168  0.0281  0.0145  38  ARG A CB  
462  C CG  . ARG A 58  ? 0.2821 0.2690 0.3184 0.0251  -0.0023 0.0052  38  ARG A CG  
463  C CD  . ARG A 58  ? 0.3177 0.3300 0.3286 0.0622  -0.0178 -0.0222 38  ARG A CD  
464  N NE  . ARG A 58  ? 0.3439 0.3138 0.3561 0.0123  -0.0110 -0.0199 38  ARG A NE  
465  C CZ  . ARG A 58  ? 0.3113 0.2568 0.3614 0.0016  -0.0201 0.0225  38  ARG A CZ  
466  N NH1 . ARG A 58  ? 0.3207 0.2916 0.4165 0.0088  -0.0149 0.0460  38  ARG A NH1 
467  N NH2 . ARG A 58  ? 0.3017 0.2577 0.3720 -0.0258 0.0360  0.0279  38  ARG A NH2 
481  N N   . LEU A 59  ? 0.2111 0.2941 0.2950 -0.0320 0.0292  0.0215  39  LEU A N   
482  C CA  . LEU A 59  ? 0.2181 0.3076 0.3210 -0.0443 0.0154  0.0073  39  LEU A CA  
483  C C   . LEU A 59  ? 0.2274 0.3258 0.3349 -0.0087 0.0204  0.0090  39  LEU A C   
484  O O   . LEU A 59  ? 0.2520 0.3233 0.3421 -0.0018 0.0126  0.0114  39  LEU A O   
485  C CB  . LEU A 59  ? 0.2234 0.3429 0.3284 -0.0487 0.0263  0.0548  39  LEU A CB  
486  C CG  . LEU A 59  ? 0.2929 0.4121 0.3526 -0.0669 0.0705  0.0406  39  LEU A CG  
487  C CD1 . LEU A 59  ? 0.3107 0.4654 0.4172 -0.1046 0.0626  0.0672  39  LEU A CD1 
488  C CD2 . LEU A 59  ? 0.3446 0.4533 0.3614 -0.0471 0.0767  0.0262  39  LEU A CD2 
500  N N   . LYS A 60  ? 0.2249 0.3077 0.3381 0.0033  0.0262  0.0180  40  LYS A N   
501  C CA  . LYS A 60  ? 0.2426 0.2983 0.3672 0.0216  0.0301  0.0019  40  LYS A CA  
502  C C   . LYS A 60  ? 0.2446 0.2705 0.3393 0.0236  0.0341  -0.0308 40  LYS A C   
503  O O   . LYS A 60  ? 0.2523 0.2501 0.3850 0.0506  0.0321  -0.0169 40  LYS A O   
504  C CB  . LYS A 60  ? 0.2755 0.3823 0.4315 0.0126  0.0774  0.0057  40  LYS A CB  
505  C CG  . LYS A 60  ? 0.3614 0.5186 0.5219 -0.0035 0.1180  -0.0105 40  LYS A CG  
506  C CD  . LYS A 60  ? 0.4617 0.6601 0.6298 -0.0088 0.0851  -0.0091 40  LYS A CD  
507  C CE  . LYS A 60  ? 0.5255 0.7458 0.7017 -0.0072 0.0716  0.0109  40  LYS A CE  
508  N NZ  . LYS A 60  ? 0.5602 0.7998 0.7477 -0.0056 0.0666  0.0222  40  LYS A NZ  
522  N N   . ARG A 61  ? 0.2222 0.2498 0.3073 0.0123  0.0195  -0.0324 41  ARG A N   
523  C CA  . ARG A 61  ? 0.2055 0.2585 0.2965 -0.0115 0.0155  -0.0034 41  ARG A CA  
524  C C   . ARG A 61  ? 0.2001 0.2128 0.3183 0.0080  0.0289  0.0084  41  ARG A C   
525  O O   . ARG A 61  ? 0.1901 0.2064 0.3284 0.0194  0.0182  -0.0003 41  ARG A O   
526  C CB  . ARG A 61  ? 0.2269 0.2710 0.2955 -0.0066 0.0027  0.0009  41  ARG A CB  
527  C CG  . ARG A 61  ? 0.2136 0.2951 0.3196 -0.0113 0.0176  0.0022  41  ARG A CG  
528  C CD  . ARG A 61  ? 0.2200 0.3020 0.3070 0.0012  0.0169  -0.0056 41  ARG A CD  
529  N NE  . ARG A 61  ? 0.3084 0.2587 0.3491 -0.0040 -0.0079 -0.0009 41  ARG A NE  
530  C CZ  . ARG A 61  ? 0.3963 0.2687 0.3418 0.0241  -0.0604 -0.0301 41  ARG A CZ  
531  N NH1 . ARG A 61  ? 0.4401 0.2795 0.3295 0.0454  -0.1148 -0.0783 41  ARG A NH1 
532  N NH2 . ARG A 61  ? 0.4217 0.3434 0.3968 0.0066  -0.0392 -0.0129 41  ARG A NH2 
546  N N   . HIS A 62  ? 0.2123 0.1866 0.3173 0.0192  0.0107  0.0208  42  HIS A N   
547  C CA  . HIS A 62  ? 0.2113 0.1897 0.3170 -0.0148 -0.0099 0.0165  42  HIS A CA  
548  C C   . HIS A 62  ? 0.1890 0.2103 0.3336 0.0066  -0.0230 0.0185  42  HIS A C   
549  O O   . HIS A 62  ? 0.1833 0.2191 0.3292 0.0021  -0.0144 0.0198  42  HIS A O   
550  C CB  . HIS A 62  ? 0.2136 0.2215 0.3297 -0.0407 0.0031  0.0046  42  HIS A CB  
551  C CG  . HIS A 62  ? 0.2213 0.2430 0.3216 -0.0481 -0.0098 0.0121  42  HIS A CG  
552  N ND1 . HIS A 62  ? 0.2068 0.2664 0.3468 -0.0214 -0.0197 0.0103  42  HIS A ND1 
553  C CD2 . HIS A 62  ? 0.2483 0.2979 0.3333 -0.0397 -0.0110 0.0354  42  HIS A CD2 
554  C CE1 . HIS A 62  ? 0.2254 0.2945 0.3493 -0.0333 -0.0233 0.0077  42  HIS A CE1 
555  N NE2 . HIS A 62  ? 0.2465 0.2957 0.3321 -0.0369 -0.0082 0.0232  42  HIS A NE2 
563  N N   . LEU A 63  ? 0.1837 0.1849 0.3696 0.0136  0.0038  0.0124  43  LEU A N   
564  C CA  . LEU A 63  ? 0.1533 0.2053 0.3884 0.0256  0.0265  0.0195  43  LEU A CA  
565  C C   . LEU A 63  ? 0.1678 0.2004 0.3687 0.0081  0.0340  -0.0058 43  LEU A C   
566  O O   . LEU A 63  ? 0.1932 0.2058 0.4097 -0.0020 0.0062  0.0230  43  LEU A O   
567  C CB  . LEU A 63  ? 0.1605 0.2565 0.4363 0.0057  0.0364  0.0318  43  LEU A CB  
568  C CG  . LEU A 63  ? 0.1699 0.3266 0.4865 0.0290  0.0447  0.0574  43  LEU A CG  
569  C CD1 . LEU A 63  ? 0.1843 0.3839 0.5240 0.0747  0.0971  0.0367  43  LEU A CD1 
570  C CD2 . LEU A 63  ? 0.1900 0.3332 0.4957 -0.0040 0.0081  0.0807  43  LEU A CD2 
582  N N   . LEU A 64  ? 0.1615 0.1918 0.3181 0.0219  0.0091  -0.0284 44  LEU A N   
583  C CA  . LEU A 64  ? 0.1655 0.1993 0.3092 0.0023  0.0204  -0.0152 44  LEU A CA  
584  C C   . LEU A 64  ? 0.1470 0.1619 0.3275 0.0065  0.0116  0.0014  44  LEU A C   
585  O O   . LEU A 64  ? 0.1659 0.1921 0.3192 0.0063  0.0193  0.0118  44  LEU A O   
586  C CB  . LEU A 64  ? 0.1880 0.2177 0.3243 -0.0094 -0.0028 -0.0054 44  LEU A CB  
587  C CG  . LEU A 64  ? 0.2087 0.2197 0.3200 0.0209  -0.0054 -0.0113 44  LEU A CG  
588  C CD1 . LEU A 64  ? 0.2375 0.2420 0.3042 0.0058  -0.0065 -0.0140 44  LEU A CD1 
589  C CD2 . LEU A 64  ? 0.2272 0.2197 0.3198 0.0365  0.0092  -0.0197 44  LEU A CD2 
601  N N   . PHE A 65  ? 0.1492 0.1894 0.3425 -0.0041 0.0033  0.0204  45  PHE A N   
602  C CA  . PHE A 65  ? 0.1613 0.1933 0.3329 0.0237  0.0055  0.0431  45  PHE A CA  
603  C C   . PHE A 65  ? 0.1768 0.1853 0.3485 0.0081  -0.0007 0.0395  45  PHE A C   
604  O O   . PHE A 65  ? 0.1694 0.2226 0.3890 0.0187  0.0004  0.0308  45  PHE A O   
605  C CB  . PHE A 65  ? 0.1756 0.2063 0.3049 0.0105  -0.0107 0.0447  45  PHE A CB  
606  C CG  . PHE A 65  ? 0.1715 0.1947 0.2717 0.0125  -0.0224 0.0350  45  PHE A CG  
607  C CD1 . PHE A 65  ? 0.1756 0.2206 0.2675 0.0344  -0.0202 0.0273  45  PHE A CD1 
608  C CD2 . PHE A 65  ? 0.1662 0.2172 0.2636 0.0047  -0.0120 0.0058  45  PHE A CD2 
609  C CE1 . PHE A 65  ? 0.1796 0.2829 0.2826 0.0506  0.0038  0.0370  45  PHE A CE1 
610  C CE2 . PHE A 65  ? 0.1728 0.2267 0.2416 0.0012  -0.0075 0.0120  45  PHE A CE2 
611  C CZ  . PHE A 65  ? 0.1765 0.2751 0.2476 0.0309  -0.0056 0.0423  45  PHE A CZ  
621  N N   . THR A 66  ? 0.1841 0.2030 0.3462 0.0154  -0.0027 0.0449  46  THR A N   
622  C CA  . THR A 66  ? 0.2036 0.2453 0.3425 0.0379  -0.0291 0.0743  46  THR A CA  
623  C C   . THR A 66  ? 0.2041 0.2701 0.3046 0.0245  -0.0464 0.0572  46  THR A C   
624  O O   . THR A 66  ? 0.2031 0.2576 0.3035 0.0158  -0.0424 0.0491  46  THR A O   
625  C CB  . THR A 66  ? 0.2336 0.2444 0.3428 0.0468  0.0098  0.0536  46  THR A CB  
626  O OG1 . THR A 66  ? 0.2267 0.2535 0.3251 0.0472  -0.0013 0.0504  46  THR A OG1 
627  C CG2 . THR A 66  ? 0.2318 0.2522 0.3610 0.0336  0.0244  0.0468  46  THR A CG2 
635  N N   . GLU A 67  ? 0.2124 0.3023 0.3307 0.0389  -0.0604 0.0506  47  GLU A N   
636  C CA  . GLU A 67  ? 0.2125 0.2983 0.3925 0.0366  -0.0895 0.0461  47  GLU A CA  
637  C C   . GLU A 67  ? 0.2197 0.2934 0.3615 0.0313  -0.0974 0.0037  47  GLU A C   
638  O O   . GLU A 67  ? 0.2334 0.2972 0.3837 0.0220  -0.0811 -0.0076 47  GLU A O   
639  C CB  . GLU A 67  ? 0.2512 0.3030 0.4621 0.0347  -0.0851 0.0316  47  GLU A CB  
640  C CG  . GLU A 67  ? 0.3082 0.3328 0.5014 0.0495  -0.0899 0.0538  47  GLU A CG  
645  N N   . ASP A 68  ? 0.2307 0.3107 0.3461 0.0533  -0.1022 0.0166  48  ASP A N   
646  C CA  . ASP A 68  ? 0.2543 0.3360 0.3356 0.0708  -0.0771 0.0166  48  ASP A CA  
647  C C   . ASP A 68  ? 0.2435 0.2788 0.3323 0.0554  -0.0625 0.0073  48  ASP A C   
648  O O   . ASP A 68  ? 0.2757 0.3056 0.3287 0.0727  -0.0270 0.0038  48  ASP A O   
649  C CB  . ASP A 68  ? 0.3242 0.4292 0.3317 0.0598  -0.0696 0.0312  48  ASP A CB  
650  C CG  . ASP A 68  ? 0.3978 0.5094 0.3804 0.0609  -0.0244 0.0815  48  ASP A CG  
651  O OD1 . ASP A 68  ? 0.4005 0.5124 0.4116 0.0642  -0.0493 0.0843  48  ASP A OD1 
652  O OD2 . ASP A 68  ? 0.4471 0.5661 0.4355 0.0317  0.0444  0.0900  48  ASP A OD2 
657  N N   . GLY A 69  ? 0.2265 0.2471 0.3075 0.0217  -0.0846 0.0264  49  GLY A N   
658  C CA  . GLY A 69  ? 0.2253 0.2359 0.3145 0.0505  -0.0872 0.0083  49  GLY A CA  
659  C C   . GLY A 69  ? 0.2064 0.2161 0.2993 0.0273  -0.0580 0.0120  49  GLY A C   
660  O O   . GLY A 69  ? 0.1950 0.2134 0.2991 0.0041  -0.0411 0.0176  49  GLY A O   
664  N N   . VAL A 70  ? 0.1805 0.2016 0.2778 0.0380  -0.0322 0.0156  50  VAL A N   
665  C CA  . VAL A 70  ? 0.1886 0.2009 0.2693 0.0495  -0.0296 -0.0026 50  VAL A CA  
666  C C   . VAL A 70  ? 0.1686 0.1980 0.2773 0.0287  -0.0448 0.0065  50  VAL A C   
667  O O   . VAL A 70  ? 0.1757 0.1879 0.2935 0.0112  -0.0423 0.0061  50  VAL A O   
668  C CB  . VAL A 70  ? 0.2212 0.2393 0.2757 0.0487  -0.0185 -0.0129 50  VAL A CB  
669  C CG1 . VAL A 70  ? 0.2500 0.2843 0.3090 0.0600  0.0219  -0.0140 50  VAL A CG1 
670  C CG2 . VAL A 70  ? 0.2650 0.2689 0.2930 0.0311  -0.0418 -0.0003 50  VAL A CG2 
680  N N   . GLY A 71  ? 0.1674 0.1968 0.2463 0.0075  -0.0215 0.0080  51  GLY A N   
681  C CA  . GLY A 71  ? 0.1619 0.1799 0.2546 0.0200  -0.0476 0.0082  51  GLY A CA  
682  C C   . GLY A 71  ? 0.1967 0.1955 0.2671 0.0038  -0.0571 0.0046  51  GLY A C   
683  O O   . GLY A 71  ? 0.2844 0.1987 0.2939 0.0175  -0.1097 -0.0130 51  GLY A O   
687  N N   . GLY A 72  ? 0.1781 0.1747 0.2615 0.0039  -0.0404 -0.0019 52  GLY A N   
688  C CA  . GLY A 72  ? 0.1996 0.1693 0.2708 -0.0018 -0.0258 0.0023  52  GLY A CA  
689  C C   . GLY A 72  ? 0.1856 0.1523 0.2483 -0.0209 -0.0273 -0.0051 52  GLY A C   
690  O O   . GLY A 72  ? 0.1937 0.1607 0.2640 -0.0002 -0.0406 -0.0065 52  GLY A O   
694  N N   . LEU A 73  ? 0.1885 0.1500 0.2453 -0.0109 -0.0255 -0.0048 53  LEU A N   
695  C CA  . LEU A 73  ? 0.1803 0.1721 0.2551 -0.0128 -0.0216 0.0044  53  LEU A CA  
696  C C   . LEU A 73  ? 0.1855 0.1765 0.2159 -0.0017 -0.0186 -0.0125 53  LEU A C   
697  O O   . LEU A 73  ? 0.2120 0.2000 0.2097 -0.0002 -0.0221 -0.0196 53  LEU A O   
698  C CB  . LEU A 73  ? 0.1771 0.1677 0.2424 0.0069  -0.0218 0.0032  53  LEU A CB  
699  C CG  . LEU A 73  ? 0.1942 0.1842 0.2403 -0.0047 -0.0160 0.0128  53  LEU A CG  
700  C CD1 . LEU A 73  ? 0.1568 0.1956 0.2543 0.0140  -0.0192 0.0046  53  LEU A CD1 
701  C CD2 . LEU A 73  ? 0.2254 0.1853 0.2439 -0.0161 -0.0171 0.0441  53  LEU A CD2 
713  N N   . TRP A 74  ? 0.1926 0.1855 0.2173 0.0180  -0.0185 -0.0164 54  TRP A N   
714  C CA  . TRP A 74  ? 0.2286 0.1866 0.2059 0.0313  0.0033  0.0093  54  TRP A CA  
715  C C   . TRP A 74  ? 0.2630 0.2131 0.1895 0.0469  0.0227  0.0304  54  TRP A C   
716  O O   . TRP A 74  ? 0.3655 0.3015 0.2075 0.1034  0.0280  0.0199  54  TRP A O   
717  C CB  . TRP A 74  ? 0.2084 0.1900 0.2306 0.0047  0.0085  0.0218  54  TRP A CB  
718  C CG  . TRP A 74  ? 0.2189 0.1835 0.2172 -0.0107 0.0197  0.0499  54  TRP A CG  
719  C CD1 . TRP A 74  ? 0.2204 0.2313 0.2503 0.0251  0.0261  0.0428  54  TRP A CD1 
720  C CD2 . TRP A 74  ? 0.2128 0.2057 0.2053 0.0132  0.0063  0.0246  54  TRP A CD2 
721  N NE1 . TRP A 74  ? 0.2679 0.2747 0.2634 0.0580  0.0016  0.0150  54  TRP A NE1 
722  C CE2 . TRP A 74  ? 0.2381 0.2504 0.2524 0.0393  -0.0194 0.0123  54  TRP A CE2 
723  C CE3 . TRP A 74  ? 0.2021 0.1928 0.2575 0.0149  -0.0146 0.0283  54  TRP A CE3 
724  C CZ2 . TRP A 74  ? 0.2782 0.2651 0.2636 0.0266  -0.0386 0.0175  54  TRP A CZ2 
725  C CZ3 . TRP A 74  ? 0.2009 0.2162 0.2741 -0.0023 -0.0257 0.0552  54  TRP A CZ3 
726  C CH2 . TRP A 74  ? 0.2246 0.2443 0.2611 0.0174  -0.0530 0.0600  54  TRP A CH2 
737  N N   . THR A 75  ? 0.2188 0.1811 0.1835 0.0368  0.0002  0.0023  55  THR A N   
738  C CA  . THR A 75  ? 0.2183 0.1658 0.1709 0.0095  0.0100  -0.0220 55  THR A CA  
739  C C   . THR A 75  ? 0.2218 0.1784 0.1705 0.0089  -0.0324 -0.0201 55  THR A C   
740  O O   . THR A 75  ? 0.2462 0.1912 0.1815 0.0047  -0.0184 -0.0011 55  THR A O   
741  C CB  . THR A 75  ? 0.2164 0.1849 0.1849 0.0118  -0.0187 -0.0276 55  THR A CB  
742  O OG1 . THR A 75  ? 0.2163 0.1766 0.1845 0.0114  -0.0063 -0.0133 55  THR A OG1 
743  C CG2 . THR A 75  ? 0.2358 0.1734 0.2185 -0.0145 -0.0090 -0.0006 55  THR A CG2 
751  N N   . THR A 76  ? 0.2216 0.1870 0.2272 0.0053  -0.0140 -0.0398 56  THR A N   
752  C CA  . THR A 76  ? 0.1921 0.1839 0.2822 -0.0064 -0.0056 -0.0582 56  THR A CA  
753  C C   . THR A 76  ? 0.1788 0.1868 0.3024 -0.0106 0.0085  -0.0450 56  THR A C   
754  O O   . THR A 76  ? 0.2009 0.2141 0.2968 -0.0203 0.0122  -0.0516 56  THR A O   
755  C CB  . THR A 76  ? 0.2400 0.2526 0.3445 0.0528  -0.0626 -0.1167 56  THR A CB  
756  O OG1 . THR A 76  ? 0.3327 0.3156 0.3761 0.0952  -0.0974 -0.1505 56  THR A OG1 
757  C CG2 . THR A 76  ? 0.2348 0.3079 0.4248 0.0746  -0.0816 -0.1250 56  THR A CG2 
765  N N   . ASP A 77  ? 0.1643 0.1872 0.2995 0.0032  0.0295  -0.0471 57  ASP A N   
766  C CA  . ASP A 77  ? 0.2068 0.2103 0.3193 0.0024  0.0454  -0.0634 57  ASP A CA  
767  C C   . ASP A 77  ? 0.2359 0.2557 0.3263 0.0057  0.0554  -0.0513 57  ASP A C   
768  O O   . ASP A 77  ? 0.2591 0.3026 0.3467 0.0265  0.0620  -0.0346 57  ASP A O   
769  C CB  . ASP A 77  ? 0.2152 0.2217 0.3367 0.0000  0.0076  -0.0693 57  ASP A CB  
770  C CG  . ASP A 77  ? 0.2966 0.2719 0.4130 -0.0210 0.0090  -0.1214 57  ASP A CG  
771  O OD1 . ASP A 77  ? 0.3779 0.3699 0.4665 -0.0098 -0.0584 -0.1409 57  ASP A OD1 
772  O OD2 . ASP A 77  ? 0.2609 0.3738 0.4670 -0.0324 0.0560  -0.1736 57  ASP A OD2 
777  N N   . SER A 78  ? 0.2817 0.2814 0.2981 0.0029  0.0289  -0.1095 58  SER A N   
778  C CA  . SER A 78  ? 0.3469 0.3163 0.2988 0.0199  0.0213  -0.1390 58  SER A CA  
779  C C   . SER A 78  ? 0.3905 0.3723 0.3117 0.0611  0.0280  -0.0832 58  SER A C   
780  O O   . SER A 78  ? 0.4518 0.4639 0.3194 0.0869  0.0190  -0.0894 58  SER A O   
781  C CB  . SER A 78  ? 0.3846 0.4118 0.3306 0.0421  -0.0385 -0.1384 58  SER A CB  
782  O OG  . SER A 78  ? 0.3856 0.4790 0.3454 0.0472  -0.0497 -0.1727 58  SER A OG  
788  N N   . GLY A 79  ? 0.3885 0.3057 0.3229 0.0670  0.0355  -0.0110 59  GLY A N   
789  C CA  . GLY A 79  ? 0.3989 0.3077 0.3419 0.0753  0.0467  0.0274  59  GLY A CA  
790  C C   . GLY A 79  ? 0.4022 0.3574 0.3678 0.0753  0.0594  0.0378  59  GLY A C   
791  O O   . GLY A 79  ? 0.4499 0.4019 0.3945 0.0709  0.0762  0.0751  59  GLY A O   
795  N N   . GLN A 80  ? 0.3748 0.3553 0.3191 0.0980  0.0563  -0.0082 60  GLN A N   
796  C CA  . GLN A 80  ? 0.4249 0.3849 0.3024 0.0937  0.0247  -0.0593 60  GLN A CA  
797  C C   . GLN A 80  ? 0.3919 0.2966 0.2905 0.0613  0.0126  -0.0586 60  GLN A C   
798  O O   . GLN A 80  ? 0.4080 0.3015 0.3158 0.0584  0.0268  -0.0608 60  GLN A O   
799  C CB  . GLN A 80  ? 0.5082 0.4781 0.3196 0.1139  0.0380  -0.1071 60  GLN A CB  
800  C CG  . GLN A 80  ? 0.5989 0.5799 0.4034 0.1216  0.0492  -0.0915 60  GLN A CG  
801  C CD  . GLN A 80  ? 0.6578 0.6672 0.4503 0.1398  0.0603  -0.0722 60  GLN A CD  
802  O OE1 . GLN A 80  ? 0.6639 0.7263 0.4858 0.1271  0.0650  -0.0513 60  GLN A OE1 
803  N NE2 . GLN A 80  ? 0.7052 0.6917 0.4432 0.1446  0.0525  -0.0817 60  GLN A NE2 
812  N N   . PRO A 81  ? 0.3695 0.2559 0.2767 0.0281  0.0202  -0.0410 61  PRO A N   
813  C CA  . PRO A 81  ? 0.3182 0.2601 0.2136 0.0181  -0.0002 -0.0183 61  PRO A CA  
814  C C   . PRO A 81  ? 0.3002 0.2724 0.2302 0.0216  -0.0345 -0.0364 61  PRO A C   
815  O O   . PRO A 81  ? 0.3485 0.3261 0.2707 0.0116  -0.0405 -0.0514 61  PRO A O   
816  C CB  . PRO A 81  ? 0.3435 0.2663 0.2716 0.0029  0.0089  0.0134  61  PRO A CB  
817  C CG  . PRO A 81  ? 0.4042 0.3040 0.3293 0.0166  0.0396  0.0060  61  PRO A CG  
818  C CD  . PRO A 81  ? 0.4063 0.3035 0.3337 0.0127  0.0355  -0.0300 61  PRO A CD  
826  N N   . ILE A 82  ? 0.2650 0.2196 0.2167 0.0039  -0.0360 -0.0384 62  ILE A N   
827  C CA  . ILE A 82  ? 0.2526 0.2425 0.2519 -0.0319 -0.0508 -0.0218 62  ILE A CA  
828  C C   . ILE A 82  ? 0.2316 0.2290 0.2252 -0.0172 -0.0336 -0.0569 62  ILE A C   
829  O O   . ILE A 82  ? 0.2384 0.2550 0.2292 -0.0233 -0.0330 -0.0431 62  ILE A O   
830  C CB  . ILE A 82  ? 0.2619 0.3135 0.3497 -0.0527 -0.0894 0.0662  62  ILE A CB  
831  C CG1 . ILE A 82  ? 0.2807 0.3742 0.4339 -0.0408 -0.0840 0.1331  62  ILE A CG1 
832  C CG2 . ILE A 82  ? 0.2699 0.3358 0.3751 -0.0919 -0.0988 0.0752  62  ILE A CG2 
833  C CD1 . ILE A 82  ? 0.3712 0.4644 0.4851 -0.0204 -0.0559 0.1198  62  ILE A CD1 
845  N N   . ALA A 83  ? 0.2505 0.2382 0.2616 0.0147  -0.0480 -0.0183 63  ALA A N   
846  C CA  . ALA A 83  ? 0.2443 0.2610 0.2758 0.0352  -0.0387 -0.0451 63  ALA A CA  
847  C C   . ALA A 83  ? 0.2317 0.2649 0.2852 0.0010  -0.0429 -0.0448 63  ALA A C   
848  O O   . ALA A 83  ? 0.2804 0.3232 0.3270 0.0134  -0.0442 -0.1061 63  ALA A O   
849  C CB  . ALA A 83  ? 0.2861 0.2533 0.3331 0.0328  -0.0354 -0.0419 63  ALA A CB  
855  N N   . ILE A 84  ? 0.2014 0.2279 0.2630 -0.0140 -0.0194 -0.0268 64  ILE A N   
856  C CA  . ILE A 84  ? 0.2298 0.2367 0.2750 0.0075  -0.0398 -0.0301 64  ILE A CA  
857  C C   . ILE A 84  ? 0.2264 0.2183 0.2911 0.0060  -0.0686 -0.0384 64  ILE A C   
858  O O   . ILE A 84  ? 0.2337 0.2229 0.2838 -0.0049 -0.0747 -0.0148 64  ILE A O   
859  C CB  . ILE A 84  ? 0.2700 0.2287 0.3273 0.0210  -0.0298 0.0015  64  ILE A CB  
860  C CG1 . ILE A 84  ? 0.3599 0.2674 0.3632 0.0053  0.0157  0.0320  64  ILE A CG1 
861  C CG2 . ILE A 84  ? 0.2715 0.2338 0.3636 0.0170  -0.0227 -0.0111 64  ILE A CG2 
862  C CD1 . ILE A 84  ? 0.4517 0.2855 0.4366 0.0089  -0.0148 0.0632  64  ILE A CD1 
874  N N   . ARG A 85  ? 0.2536 0.2588 0.3294 0.0152  -0.0754 -0.0202 65  ARG A N   
875  C CA  . ARG A 85  ? 0.2447 0.3020 0.3316 0.0113  -0.0878 -0.0018 65  ARG A CA  
876  C C   . ARG A 85  ? 0.2481 0.2901 0.3434 0.0015  -0.0987 -0.0142 65  ARG A C   
877  O O   . ARG A 85  ? 0.2625 0.3067 0.3957 -0.0039 -0.1020 -0.0192 65  ARG A O   
878  C CB  . ARG A 85  ? 0.2825 0.3413 0.3301 0.0080  -0.0615 -0.0292 65  ARG A CB  
879  C CG  . ARG A 85  ? 0.3420 0.3849 0.3292 0.0137  -0.0263 0.0003  65  ARG A CG  
880  C CD  . ARG A 85  ? 0.4114 0.4513 0.3459 0.0461  -0.0286 -0.0098 65  ARG A CD  
881  N NE  . ARG A 85  ? 0.4676 0.5135 0.3959 0.0935  -0.0081 0.0239  65  ARG A NE  
882  C CZ  . ARG A 85  ? 0.5217 0.5956 0.4207 0.1156  0.0382  0.0269  65  ARG A CZ  
883  N NH1 . ARG A 85  ? 0.5263 0.6156 0.4248 0.0902  0.0788  -0.0035 65  ARG A NH1 
884  N NH2 . ARG A 85  ? 0.5503 0.6522 0.4347 0.1382  0.0365  0.0391  65  ARG A NH2 
898  N N   . GLY A 86  ? 0.2436 0.2693 0.3184 0.0048  -0.0781 -0.0006 66  GLY A N   
899  C CA  . GLY A 86  ? 0.2611 0.2748 0.3208 0.0274  -0.0788 -0.0065 66  GLY A CA  
900  C C   . GLY A 86  ? 0.2595 0.2474 0.3169 0.0371  -0.0720 -0.0006 66  GLY A C   
901  O O   . GLY A 86  ? 0.2449 0.2275 0.3167 0.0137  -0.0617 -0.0036 66  GLY A O   
905  N N   . ARG A 87  ? 0.2722 0.2344 0.3313 0.0418  -0.0481 -0.0105 67  ARG A N   
906  C CA  . ARG A 87  ? 0.2551 0.2371 0.3368 0.0492  -0.0280 0.0031  67  ARG A CA  
907  C C   . ARG A 87  ? 0.2470 0.2492 0.3339 0.0480  -0.0692 0.0104  67  ARG A C   
908  O O   . ARG A 87  ? 0.2574 0.2670 0.3315 0.0620  -0.0275 0.0022  67  ARG A O   
909  C CB  . ARG A 87  ? 0.2637 0.2312 0.3537 0.0456  -0.0153 0.0215  67  ARG A CB  
910  C CG  . ARG A 87  ? 0.2609 0.2562 0.3899 0.0758  -0.0199 0.0105  67  ARG A CG  
911  C CD  . ARG A 87  ? 0.3414 0.3204 0.4307 0.1298  0.0193  0.0355  67  ARG A CD  
912  N NE  . ARG A 87  ? 0.4762 0.3641 0.5137 0.1330  0.0713  0.0761  67  ARG A NE  
913  C CZ  . ARG A 87  ? 0.5793 0.4106 0.5920 0.1702  0.1151  0.1123  67  ARG A CZ  
914  N NH1 . ARG A 87  ? 0.6485 0.3479 0.6066 0.2204  0.1656  0.0712  67  ARG A NH1 
915  N NH2 . ARG A 87  ? 0.5815 0.4894 0.6348 0.2012  0.1066  0.1491  67  ARG A NH2 
929  N N   . GLU A 88  ? 0.2508 0.3256 0.4028 0.0128  -0.0724 0.0053  68  GLU A N   
930  C CA  . GLU A 88  ? 0.2797 0.3620 0.4071 -0.0078 -0.1103 0.0216  68  GLU A CA  
931  C C   . GLU A 88  ? 0.2543 0.3558 0.4026 -0.0238 -0.0955 -0.0127 68  GLU A C   
932  O O   . GLU A 88  ? 0.2207 0.3687 0.4300 -0.0267 -0.0879 0.0075  68  GLU A O   
944  N N   . LYS A 89  ? 0.2258 0.3585 0.3956 -0.0273 -0.0843 0.0056  69  LYS A N   
945  C CA  . LYS A 89  ? 0.2589 0.3010 0.3650 -0.0497 -0.0750 0.0083  69  LYS A CA  
946  C C   . LYS A 89  ? 0.2341 0.2434 0.3365 -0.0125 -0.0636 -0.0127 69  LYS A C   
947  O O   . LYS A 89  ? 0.2459 0.2491 0.3127 -0.0301 -0.0326 -0.0140 69  LYS A O   
948  C CB  . LYS A 89  ? 0.3119 0.3988 0.3684 -0.0580 -0.0669 0.0103  69  LYS A CB  
949  C CG  . LYS A 89  ? 0.3676 0.4701 0.4256 -0.0544 -0.0644 0.0375  69  LYS A CG  
954  N N   . LEU A 90  ? 0.1904 0.2265 0.3309 0.0000  -0.0524 -0.0153 70  LEU A N   
955  C CA  . LEU A 90  ? 0.1834 0.2122 0.3264 0.0122  -0.0474 0.0115  70  LEU A CA  
956  C C   . LEU A 90  ? 0.1756 0.2190 0.3113 -0.0080 -0.0430 0.0070  70  LEU A C   
957  O O   . LEU A 90  ? 0.1944 0.2409 0.3137 -0.0058 -0.0215 0.0162  70  LEU A O   
958  C CB  . LEU A 90  ? 0.2085 0.1899 0.3403 -0.0144 -0.0323 0.0071  70  LEU A CB  
959  C CG  . LEU A 90  ? 0.1984 0.1998 0.3143 -0.0122 -0.0492 0.0171  70  LEU A CG  
960  C CD1 . LEU A 90  ? 0.2324 0.2288 0.3112 -0.0185 -0.0266 -0.0055 70  LEU A CD1 
961  C CD2 . LEU A 90  ? 0.1911 0.2221 0.3063 -0.0073 -0.0263 -0.0071 70  LEU A CD2 
973  N N   . GLY A 91  ? 0.1918 0.2487 0.3268 -0.0120 -0.0253 -0.0005 71  GLY A N   
974  C CA  . GLY A 91  ? 0.2048 0.2835 0.3519 0.0066  -0.0243 -0.0065 71  GLY A CA  
975  C C   . GLY A 91  ? 0.2100 0.2746 0.3615 -0.0349 -0.0338 0.0030  71  GLY A C   
976  O O   . GLY A 91  ? 0.2257 0.2963 0.3839 -0.0413 -0.0446 0.0211  71  GLY A O   
980  N N   . GLU A 92  ? 0.2166 0.2953 0.4055 -0.0810 -0.0446 0.0047  72  GLU A N   
981  C CA  . GLU A 92  ? 0.2897 0.3158 0.4405 -0.1049 -0.0320 0.0093  72  GLU A CA  
982  C C   . GLU A 92  ? 0.2979 0.2857 0.4301 -0.0940 0.0071  0.0068  72  GLU A C   
983  O O   . GLU A 92  ? 0.3352 0.2924 0.4688 -0.1007 0.0281  0.0074  72  GLU A O   
984  C CB  . GLU A 92  ? 0.3751 0.4040 0.4872 -0.1123 -0.0848 -0.0289 72  GLU A CB  
985  C CG  . GLU A 92  ? 0.4840 0.5396 0.5397 -0.0889 -0.0921 -0.0439 72  GLU A CG  
986  C CD  . GLU A 92  ? 0.6132 0.6358 0.5817 -0.0499 -0.0991 -0.0386 72  GLU A CD  
987  O OE1 . GLU A 92  ? 0.6601 0.6632 0.5991 -0.0401 -0.0923 -0.0550 72  GLU A OE1 
988  O OE2 . GLU A 92  ? 0.6679 0.6565 0.5869 -0.0486 -0.1051 -0.0249 72  GLU A OE2 
995  N N   . HIS A 93  ? 0.2676 0.2355 0.3972 -0.0430 0.0103  0.0110  73  HIS A N   
996  C CA  A HIS A 93  ? 0.2919 0.2184 0.3628 -0.0025 0.0198  0.0351  73  HIS A CA  
997  C CA  B HIS A 93  ? 0.2841 0.2355 0.3674 -0.0250 0.0224  0.0325  73  HIS A CA  
998  C C   . HIS A 93  ? 0.2920 0.2224 0.3589 -0.0048 0.0377  0.0572  73  HIS A C   
999  O O   . HIS A 93  ? 0.3310 0.2353 0.3662 0.0293  0.0740  0.0754  73  HIS A O   
1000 C CB  A HIS A 93  ? 0.3141 0.2257 0.3318 0.0455  0.0074  0.0654  73  HIS A CB  
1001 C CB  B HIS A 93  ? 0.2963 0.2726 0.3488 -0.0081 0.0107  0.0458  73  HIS A CB  
1002 C CG  A HIS A 93  ? 0.3179 0.2688 0.3280 0.0528  -0.0102 0.0370  73  HIS A CG  
1003 C CG  B HIS A 93  ? 0.3027 0.2610 0.3311 0.0041  -0.0235 0.0247  73  HIS A CG  
1004 N ND1 A HIS A 93  ? 0.3198 0.2806 0.3245 0.0404  -0.0073 0.0484  73  HIS A ND1 
1005 N ND1 B HIS A 93  ? 0.3116 0.2877 0.3292 -0.0131 -0.0559 0.0205  73  HIS A ND1 
1006 C CD2 A HIS A 93  ? 0.3349 0.2984 0.3330 0.0705  -0.0263 0.0312  73  HIS A CD2 
1007 C CD2 B HIS A 93  ? 0.3218 0.2981 0.3346 0.0129  -0.0244 -0.0039 73  HIS A CD2 
1008 C CE1 A HIS A 93  ? 0.3260 0.2649 0.3267 0.0856  0.0017  0.0425  73  HIS A CE1 
1009 C CE1 B HIS A 93  ? 0.3480 0.3116 0.3437 0.0217  -0.0406 0.0046  73  HIS A CE1 
1010 N NE2 A HIS A 93  ? 0.3196 0.3193 0.3315 0.0599  -0.0217 0.0243  73  HIS A NE2 
1011 N NE2 B HIS A 93  ? 0.3564 0.2963 0.3424 0.0227  -0.0174 -0.0162 73  HIS A NE2 
1026 N N   . ALA A 94  ? 0.2411 0.2081 0.3643 0.0016  0.0192  0.0428  74  ALA A N   
1027 C CA  . ALA A 94  ? 0.2080 0.2399 0.3624 -0.0277 0.0071  0.0334  74  ALA A CA  
1028 C C   . ALA A 94  ? 0.2069 0.2555 0.3596 -0.0328 0.0004  0.0301  74  ALA A C   
1029 O O   . ALA A 94  ? 0.2086 0.2548 0.3508 -0.0002 0.0106  0.0293  74  ALA A O   
1030 C CB  . ALA A 94  ? 0.2637 0.2505 0.3578 -0.0402 -0.0204 0.0156  74  ALA A CB  
1036 N N   . VAL A 95  ? 0.2245 0.2992 0.3955 -0.0587 0.0071  0.0354  75  VAL A N   
1037 C CA  . VAL A 95  ? 0.2582 0.3405 0.4073 -0.1145 -0.0024 0.0336  75  VAL A CA  
1038 C C   . VAL A 95  ? 0.3141 0.3291 0.3394 -0.1127 -0.0215 0.0431  75  VAL A C   
1039 O O   . VAL A 95  ? 0.3732 0.3317 0.3521 -0.1215 0.0054  0.0506  75  VAL A O   
1040 C CB  . VAL A 95  ? 0.2714 0.3681 0.4683 -0.1064 0.0041  0.0207  75  VAL A CB  
1041 C CG1 . VAL A 95  ? 0.2919 0.3829 0.5030 -0.1116 0.0280  -0.0087 75  VAL A CG1 
1042 C CG2 . VAL A 95  ? 0.2941 0.4130 0.4904 -0.1074 0.0010  0.0425  75  VAL A CG2 
1052 N N   . TRP A 96  ? 0.3244 0.3006 0.3170 -0.1071 -0.0358 0.0183  76  TRP A N   
1053 C CA  . TRP A 96  ? 0.3490 0.2841 0.2891 -0.1040 -0.0549 0.0176  76  TRP A CA  
1054 C C   . TRP A 96  ? 0.3292 0.2512 0.2957 -0.0509 -0.0458 0.0189  76  TRP A C   
1055 O O   . TRP A 96  ? 0.3612 0.2438 0.2959 -0.0431 -0.0255 0.0029  76  TRP A O   
1056 C CB  . TRP A 96  ? 0.4110 0.2847 0.2964 -0.0750 -0.0429 0.0042  76  TRP A CB  
1057 C CG  . TRP A 96  ? 0.4746 0.2619 0.2904 -0.0506 -0.0336 -0.0150 76  TRP A CG  
1058 C CD1 . TRP A 96  ? 0.5266 0.2856 0.3144 -0.0377 -0.0156 -0.0185 76  TRP A CD1 
1059 C CD2 . TRP A 96  ? 0.4831 0.2704 0.3043 0.0198  -0.0214 0.0140  76  TRP A CD2 
1060 N NE1 . TRP A 96  ? 0.5597 0.3224 0.3160 0.0170  -0.0006 -0.0122 76  TRP A NE1 
1061 C CE2 . TRP A 96  ? 0.5129 0.3048 0.2837 0.0453  -0.0003 0.0114  76  TRP A CE2 
1062 C CE3 . TRP A 96  ? 0.4468 0.3128 0.3266 0.0301  -0.0064 0.0185  76  TRP A CE3 
1063 C CZ2 . TRP A 96  ? 0.5054 0.3366 0.2738 0.0853  -0.0037 0.0140  76  TRP A CZ2 
1064 C CZ3 . TRP A 96  ? 0.4422 0.3264 0.2981 0.0541  0.0006  -0.0408 76  TRP A CZ3 
1065 C CH2 . TRP A 96  ? 0.4588 0.3278 0.2555 0.1012  -0.0015 -0.0422 76  TRP A CH2 
1076 N N   . SER A 97  ? 0.2859 0.2255 0.3352 -0.0279 -0.0450 0.0304  77  SER A N   
1077 C CA  . SER A 97  ? 0.2702 0.2370 0.3551 -0.0141 -0.0490 0.0230  77  SER A CA  
1078 C C   . SER A 97  ? 0.2752 0.2253 0.3139 -0.0326 -0.0529 -0.0085 77  SER A C   
1079 O O   . SER A 97  ? 0.2679 0.2554 0.3241 -0.0343 -0.0705 -0.0112 77  SER A O   
1080 C CB  . SER A 97  ? 0.2606 0.3101 0.4046 -0.0165 -0.0329 0.0343  77  SER A CB  
1081 O OG  . SER A 97  ? 0.2722 0.3303 0.4361 -0.0500 -0.0140 0.0052  77  SER A OG  
1087 N N   A LEU A 98  ? 0.2617 0.2252 0.2756 -0.0154 -0.0233 -0.0185 78  LEU A N   
1088 N N   C LEU A 98  ? 0.3249 0.3044 0.3237 -0.0153 -0.0437 -0.0103 78  LEU A N   
1089 C CA  A LEU A 98  ? 0.2721 0.2812 0.2647 0.0008  -0.0254 -0.0333 78  LEU A CA  
1090 C CA  C LEU A 98  ? 0.3402 0.3365 0.3325 -0.0047 -0.0368 -0.0092 78  LEU A CA  
1091 C C   A LEU A 98  ? 0.2595 0.3248 0.2786 -0.0080 -0.0291 -0.0288 78  LEU A C   
1092 C C   C LEU A 98  ? 0.3204 0.3421 0.3227 -0.0047 -0.0348 -0.0044 78  LEU A C   
1093 O O   A LEU A 98  ? 0.3217 0.3530 0.3200 0.0057  -0.0450 -0.0173 78  LEU A O   
1094 O O   C LEU A 98  ? 0.3392 0.3564 0.3250 -0.0016 -0.0409 -0.0036 78  LEU A O   
1095 C CB  A LEU A 98  ? 0.3272 0.3148 0.3147 0.0152  0.0100  -0.0175 78  LEU A CB  
1096 C CB  C LEU A 98  ? 0.3589 0.3604 0.3546 0.0030  -0.0212 -0.0084 78  LEU A CB  
1097 C CG  A LEU A 98  ? 0.3574 0.3388 0.3525 0.0058  0.0318  -0.0107 78  LEU A CG  
1098 C CG  C LEU A 98  ? 0.3749 0.3802 0.3727 0.0108  -0.0057 -0.0094 78  LEU A CG  
1099 C CD1 A LEU A 98  ? 0.3418 0.3485 0.3834 -0.0074 0.0533  -0.0446 78  LEU A CD1 
1100 C CD1 C LEU A 98  ? 0.3815 0.3893 0.3805 0.0139  0.0010  -0.0100 78  LEU A CD1 
1101 C CD2 A LEU A 98  ? 0.4026 0.3376 0.3643 0.0140  0.0533  0.0331  78  LEU A CD2 
1102 C CD2 C LEU A 98  ? 0.3796 0.3886 0.3808 0.0137  0.0005  -0.0100 78  LEU A CD2 
1125 N N   . GLN A 99  ? 0.2468 0.3107 0.3108 -0.0105 -0.0091 0.0016  79  GLN A N   
1126 C CA  . GLN A 99  ? 0.2690 0.3186 0.3657 -0.0505 -0.0219 0.0314  79  GLN A CA  
1127 C C   . GLN A 99  ? 0.2667 0.2747 0.3203 -0.0559 -0.0070 0.0426  79  GLN A C   
1128 O O   . GLN A 99  ? 0.2950 0.3139 0.3217 -0.0440 0.0015  0.0493  79  GLN A O   
1129 C CB  . GLN A 99  ? 0.3108 0.3830 0.4591 -0.0814 -0.0637 0.0355  79  GLN A CB  
1133 N N   A CYS A 100 ? 0.2863 0.2760 0.2887 -0.0256 -0.0301 0.0189  80  CYS A N   
1134 N N   B CYS A 100 ? 0.2863 0.2760 0.2887 -0.0256 -0.0301 0.0189  80  CYS A N   
1135 C CA  A CYS A 100 ? 0.2782 0.2570 0.2465 -0.0133 -0.0342 0.0111  80  CYS A CA  
1136 C CA  B CYS A 100 ? 0.2782 0.2570 0.2465 -0.0133 -0.0342 0.0111  80  CYS A CA  
1137 C C   A CYS A 100 ? 0.2629 0.2410 0.2341 -0.0211 -0.0151 0.0076  80  CYS A C   
1138 C C   B CYS A 100 ? 0.2629 0.2410 0.2341 -0.0211 -0.0151 0.0076  80  CYS A C   
1139 O O   A CYS A 100 ? 0.2635 0.2383 0.2260 -0.0305 -0.0125 0.0121  80  CYS A O   
1140 O O   B CYS A 100 ? 0.2635 0.2383 0.2260 -0.0305 -0.0125 0.0121  80  CYS A O   
1141 C CB  A CYS A 100 ? 0.2807 0.2529 0.2227 -0.0110 -0.0393 0.0046  80  CYS A CB  
1142 C CB  B CYS A 100 ? 0.2807 0.2529 0.2227 -0.0110 -0.0393 0.0046  80  CYS A CB  
1143 S SG  A CYS A 100 ? 0.2885 0.2488 0.2390 -0.0293 -0.0266 -0.0088 80  CYS A SG  
1144 S SG  B CYS A 100 ? 0.2885 0.2488 0.2390 -0.0293 -0.0266 -0.0088 80  CYS A SG  
1155 N N   . PHE A 101 ? 0.2471 0.2355 0.2272 -0.0247 -0.0017 -0.0006 81  PHE A N   
1156 C CA  . PHE A 101 ? 0.2355 0.2337 0.2180 -0.0414 0.0237  -0.0044 81  PHE A CA  
1157 C C   . PHE A 101 ? 0.2303 0.2279 0.2150 -0.0343 0.0376  -0.0188 81  PHE A C   
1158 O O   . PHE A 101 ? 0.2422 0.2208 0.2467 -0.0226 0.0416  -0.0284 81  PHE A O   
1159 C CB  . PHE A 101 ? 0.2474 0.2358 0.2141 -0.0295 0.0209  0.0080  81  PHE A CB  
1160 C CG  . PHE A 101 ? 0.2638 0.2376 0.1959 -0.0244 0.0017  -0.0275 81  PHE A CG  
1161 C CD1 . PHE A 101 ? 0.2425 0.2306 0.2249 -0.0205 0.0012  -0.0402 81  PHE A CD1 
1162 C CD2 . PHE A 101 ? 0.3013 0.2939 0.1986 0.0035  -0.0004 -0.0605 81  PHE A CD2 
1163 C CE1 . PHE A 101 ? 0.2669 0.2463 0.2445 -0.0377 0.0065  -0.0412 81  PHE A CE1 
1164 C CE2 . PHE A 101 ? 0.3540 0.3616 0.2363 0.0214  0.0381  -0.0450 81  PHE A CE2 
1165 C CZ  . PHE A 101 ? 0.3221 0.2977 0.2323 0.0123  0.0371  -0.0656 81  PHE A CZ  
1176 N N   . PRO A 102 ? 0.2290 0.2589 0.2125 -0.0311 0.0578  0.0079  82  PRO A N   
1177 C CA  . PRO A 102 ? 0.2230 0.2837 0.2528 -0.0358 0.0747  0.0165  82  PRO A CA  
1178 C C   . PRO A 102 ? 0.2394 0.3244 0.2849 -0.0139 0.0839  -0.0303 82  PRO A C   
1179 O O   . PRO A 102 ? 0.2668 0.3554 0.3810 0.0119  0.0682  -0.0789 82  PRO A O   
1180 C CB  . PRO A 102 ? 0.2383 0.3159 0.2700 -0.0663 0.0688  0.0264  82  PRO A CB  
1181 C CG  . PRO A 102 ? 0.2467 0.3161 0.2466 -0.0482 0.0424  0.0292  82  PRO A CG  
1182 C CD  . PRO A 102 ? 0.2472 0.2670 0.2127 -0.0461 0.0290  0.0399  82  PRO A CD  
1190 N N   . ASP A 103 ? 0.2443 0.3392 0.2255 -0.0464 0.0761  -0.0199 83  ASP A N   
1191 C CA  . ASP A 103 ? 0.2466 0.3292 0.2191 -0.0541 0.0883  -0.0527 83  ASP A CA  
1192 C C   . ASP A 103 ? 0.2174 0.3123 0.1932 -0.0340 0.0625  -0.0542 83  ASP A C   
1193 O O   . ASP A 103 ? 0.2408 0.3330 0.2078 -0.0435 0.0480  -0.0378 83  ASP A O   
1194 C CB  . ASP A 103 ? 0.2840 0.3585 0.2474 -0.0640 0.0864  -0.0425 83  ASP A CB  
1195 C CG  . ASP A 103 ? 0.3243 0.3682 0.2369 -0.0669 0.0609  -0.0051 83  ASP A CG  
1196 O OD1 . ASP A 103 ? 0.3018 0.3679 0.2238 -0.0440 0.0727  0.0024  83  ASP A OD1 
1197 O OD2 . ASP A 103 ? 0.3813 0.3927 0.2463 -0.0510 0.0328  -0.0170 83  ASP A OD2 
1202 N N   . TRP A 104 ? 0.1969 0.2868 0.1832 -0.0112 0.0496  -0.0377 84  TRP A N   
1203 C CA  . TRP A 104 ? 0.1976 0.2600 0.1914 -0.0227 0.0348  -0.0586 84  TRP A CA  
1204 C C   . TRP A 104 ? 0.2030 0.2667 0.1931 -0.0036 0.0347  -0.0529 84  TRP A C   
1205 O O   . TRP A 104 ? 0.2129 0.2711 0.2472 -0.0095 0.0454  -0.0436 84  TRP A O   
1206 C CB  . TRP A 104 ? 0.1992 0.2511 0.1824 -0.0215 0.0205  -0.0332 84  TRP A CB  
1207 C CG  . TRP A 104 ? 0.2038 0.2324 0.1673 -0.0143 0.0136  -0.0241 84  TRP A CG  
1208 C CD1 . TRP A 104 ? 0.2344 0.2133 0.2002 0.0041  0.0260  -0.0301 84  TRP A CD1 
1209 C CD2 . TRP A 104 ? 0.2085 0.2191 0.1469 -0.0318 0.0179  -0.0157 84  TRP A CD2 
1210 N NE1 . TRP A 104 ? 0.2285 0.2388 0.2014 -0.0304 0.0325  -0.0327 84  TRP A NE1 
1211 C CE2 . TRP A 104 ? 0.2061 0.2268 0.1657 -0.0427 0.0151  -0.0379 84  TRP A CE2 
1212 C CE3 . TRP A 104 ? 0.2152 0.2412 0.1353 -0.0435 0.0312  -0.0278 84  TRP A CE3 
1213 C CZ2 . TRP A 104 ? 0.2201 0.2746 0.1612 -0.0306 0.0150  -0.0691 84  TRP A CZ2 
1214 C CZ3 . TRP A 104 ? 0.2199 0.2395 0.1489 -0.0223 0.0467  -0.0410 84  TRP A CZ3 
1215 C CH2 . TRP A 104 ? 0.2224 0.2548 0.1763 -0.0233 0.0404  -0.0659 84  TRP A CH2 
1226 N N   . VAL A 105 ? 0.1856 0.2397 0.2066 0.0092  0.0302  -0.0475 85  VAL A N   
1227 C CA  . VAL A 105 ? 0.2034 0.2543 0.2019 -0.0015 0.0434  -0.0535 85  VAL A CA  
1228 C C   . VAL A 105 ? 0.2041 0.2318 0.1945 0.0240  0.0270  -0.0403 85  VAL A C   
1229 O O   . VAL A 105 ? 0.2049 0.2257 0.1924 0.0101  0.0253  -0.0346 85  VAL A O   
1230 C CB  . VAL A 105 ? 0.2411 0.2868 0.1856 -0.0285 0.0575  -0.0867 85  VAL A CB  
1231 C CG1 . VAL A 105 ? 0.2513 0.3372 0.1867 -0.0165 0.0276  -0.0692 85  VAL A CG1 
1232 C CG2 . VAL A 105 ? 0.2992 0.3274 0.2533 -0.0403 0.1008  -0.0720 85  VAL A CG2 
1242 N N   . TRP A 106 ? 0.1918 0.2243 0.2110 0.0016  0.0150  -0.0296 86  TRP A N   
1243 C CA  . TRP A 106 ? 0.1754 0.2424 0.2018 0.0086  0.0100  -0.0276 86  TRP A CA  
1244 C C   . TRP A 106 ? 0.1933 0.2698 0.2063 0.0031  0.0259  -0.0458 86  TRP A C   
1245 O O   . TRP A 106 ? 0.2178 0.2803 0.2268 0.0110  0.0243  -0.0458 86  TRP A O   
1246 C CB  . TRP A 106 ? 0.1808 0.2292 0.2225 -0.0089 0.0250  -0.0543 86  TRP A CB  
1247 C CG  . TRP A 106 ? 0.1908 0.2345 0.2278 -0.0279 0.0078  -0.0568 86  TRP A CG  
1248 C CD1 . TRP A 106 ? 0.1787 0.2356 0.2452 -0.0319 0.0179  -0.0405 86  TRP A CD1 
1249 C CD2 . TRP A 106 ? 0.2085 0.2131 0.2272 -0.0299 0.0361  -0.0436 86  TRP A CD2 
1250 N NE1 . TRP A 106 ? 0.2062 0.2470 0.2151 -0.0193 0.0161  -0.0235 86  TRP A NE1 
1251 C CE2 . TRP A 106 ? 0.2207 0.2181 0.2092 -0.0258 0.0347  -0.0432 86  TRP A CE2 
1252 C CE3 . TRP A 106 ? 0.2188 0.2053 0.2280 -0.0120 0.0489  -0.0206 86  TRP A CE3 
1253 C CZ2 . TRP A 106 ? 0.2393 0.2460 0.1841 -0.0389 0.0147  -0.0126 86  TRP A CZ2 
1254 C CZ3 . TRP A 106 ? 0.2247 0.2115 0.2329 -0.0253 0.0551  -0.0188 86  TRP A CZ3 
1255 C CH2 . TRP A 106 ? 0.2483 0.2531 0.2043 -0.0305 0.0510  -0.0246 86  TRP A CH2 
1266 N N   . THR A 107 ? 0.1886 0.2483 0.2226 -0.0113 0.0265  -0.0522 87  THR A N   
1267 C CA  . THR A 107 ? 0.1928 0.2601 0.2114 -0.0230 0.0073  -0.0508 87  THR A CA  
1268 C C   . THR A 107 ? 0.1863 0.2247 0.2032 -0.0388 0.0172  -0.0644 87  THR A C   
1269 O O   . THR A 107 ? 0.2068 0.2281 0.1890 -0.0150 0.0292  -0.0564 87  THR A O   
1270 C CB  . THR A 107 ? 0.2365 0.2943 0.2469 -0.0211 0.0289  -0.0348 87  THR A CB  
1271 O OG1 . THR A 107 ? 0.2669 0.2918 0.2516 0.0093  0.0186  -0.0052 87  THR A OG1 
1272 C CG2 . THR A 107 ? 0.2331 0.3391 0.2909 -0.0276 0.0276  0.0186  87  THR A CG2 
1280 N N   . ASP A 108 ? 0.1979 0.2451 0.2575 -0.0351 0.0026  -0.0711 88  ASP A N   
1281 C CA  . ASP A 108 ? 0.1944 0.2618 0.2581 -0.0363 0.0145  -0.0892 88  ASP A CA  
1282 C C   . ASP A 108 ? 0.2195 0.2774 0.2444 -0.0434 0.0143  -0.0678 88  ASP A C   
1283 O O   . ASP A 108 ? 0.2236 0.2622 0.2591 -0.0263 0.0050  -0.0520 88  ASP A O   
1284 C CB  . ASP A 108 ? 0.1975 0.2791 0.2513 -0.0204 0.0152  -0.0618 88  ASP A CB  
1285 C CG  . ASP A 108 ? 0.2459 0.3199 0.2293 -0.0289 0.0383  -0.0284 88  ASP A CG  
1286 O OD1 . ASP A 108 ? 0.2741 0.4063 0.2361 -0.0677 0.0454  -0.0110 88  ASP A OD1 
1287 O OD2 . ASP A 108 ? 0.2645 0.3040 0.2272 -0.0200 0.0113  -0.0070 88  ASP A OD2 
1292 N N   . ILE A 109 ? 0.1997 0.2698 0.2541 -0.0256 0.0104  -0.0886 89  ILE A N   
1293 C CA  . ILE A 109 ? 0.1896 0.2729 0.2552 -0.0058 0.0068  -0.0905 89  ILE A CA  
1294 C C   . ILE A 109 ? 0.2171 0.2424 0.2809 -0.0125 0.0110  -0.1037 89  ILE A C   
1295 O O   . ILE A 109 ? 0.2445 0.2554 0.3025 -0.0219 0.0236  -0.1205 89  ILE A O   
1296 C CB  . ILE A 109 ? 0.1901 0.2524 0.2557 -0.0151 0.0119  -0.0886 89  ILE A CB  
1297 C CG1 . ILE A 109 ? 0.1897 0.2628 0.2892 -0.0182 0.0339  -0.0673 89  ILE A CG1 
1298 C CG2 . ILE A 109 ? 0.2431 0.2719 0.2975 0.0093  0.0019  -0.0380 89  ILE A CG2 
1299 C CD1 . ILE A 109 ? 0.1961 0.3276 0.3140 -0.0116 0.0319  -0.0986 89  ILE A CD1 
1311 N N   A GLN A 110 ? 0.2047 0.2134 0.2869 -0.0120 -0.0136 -0.0833 90  GLN A N   
1312 N N   B GLN A 110 ? 0.2155 0.2398 0.2990 -0.0066 0.0034  -0.0845 90  GLN A N   
1313 C CA  A GLN A 110 ? 0.1811 0.2038 0.3130 0.0016  -0.0053 -0.0717 90  GLN A CA  
1314 C CA  B GLN A 110 ? 0.2023 0.2491 0.3298 0.0050  0.0058  -0.0673 90  GLN A CA  
1315 C C   A GLN A 110 ? 0.1841 0.1772 0.3053 -0.0009 0.0076  -0.0543 90  GLN A C   
1316 C C   B GLN A 110 ? 0.1992 0.2242 0.3194 0.0110  0.0145  -0.0552 90  GLN A C   
1317 O O   A GLN A 110 ? 0.2189 0.1669 0.2976 0.0081  0.0148  -0.0509 90  GLN A O   
1318 O O   B GLN A 110 ? 0.2138 0.2233 0.3149 0.0187  0.0262  -0.0380 90  GLN A O   
1319 C CB  A GLN A 110 ? 0.1953 0.2330 0.3542 0.0070  -0.0139 -0.0595 90  GLN A CB  
1320 C CB  B GLN A 110 ? 0.2064 0.2892 0.3745 0.0107  -0.0043 -0.0549 90  GLN A CB  
1321 C CG  A GLN A 110 ? 0.2155 0.2956 0.4142 0.0017  -0.0320 -0.0603 90  GLN A CG  
1322 C CG  B GLN A 110 ? 0.2247 0.3396 0.4169 0.0106  -0.0217 -0.0529 90  GLN A CG  
1323 C CD  A GLN A 110 ? 0.2083 0.3318 0.4915 -0.0050 -0.0297 -0.0534 90  GLN A CD  
1324 C CD  B GLN A 110 ? 0.2685 0.3791 0.4622 0.0220  -0.0120 -0.0643 90  GLN A CD  
1325 O OE1 A GLN A 110 ? 0.2131 0.3233 0.5651 -0.0128 -0.0439 -0.0246 90  GLN A OE1 
1326 O OE1 B GLN A 110 ? 0.2681 0.3804 0.4768 0.0408  0.0152  -0.0934 90  GLN A OE1 
1327 N NE2 A GLN A 110 ? 0.1803 0.3442 0.4881 -0.0701 -0.0093 -0.0820 90  GLN A NE2 
1328 N NE2 B GLN A 110 ? 0.3000 0.3742 0.4785 0.0056  -0.0291 -0.0973 90  GLN A NE2 
1345 N N   . ILE A 111 ? 0.1883 0.2093 0.3276 0.0156  0.0073  -0.0640 91  ILE A N   
1346 C CA  . ILE A 111 ? 0.1886 0.1984 0.3676 0.0124  -0.0026 -0.0594 91  ILE A CA  
1347 C C   . ILE A 111 ? 0.1993 0.1764 0.3615 -0.0118 0.0061  -0.0837 91  ILE A C   
1348 O O   . ILE A 111 ? 0.2552 0.2096 0.3790 -0.0361 -0.0004 -0.0710 91  ILE A O   
1349 C CB  . ILE A 111 ? 0.1968 0.2204 0.3798 0.0331  -0.0087 -0.0458 91  ILE A CB  
1350 C CG1 . ILE A 111 ? 0.2114 0.2942 0.3525 0.0424  0.0223  -0.0247 91  ILE A CG1 
1351 C CG2 . ILE A 111 ? 0.2228 0.2454 0.4215 0.0672  -0.0066 -0.0264 91  ILE A CG2 
1352 C CD1 . ILE A 111 ? 0.2222 0.3661 0.3770 0.0570  0.0336  -0.0358 91  ILE A CD1 
1365 N N   . PHE A 112 ? 0.1821 0.1635 0.3509 -0.0137 0.0222  -0.0556 92  PHE A N   
1366 C CA  . PHE A 112 ? 0.1652 0.1765 0.3721 -0.0183 0.0131  -0.0487 92  PHE A CA  
1367 C C   . PHE A 112 ? 0.1728 0.1669 0.3849 -0.0099 -0.0102 -0.0611 92  PHE A C   
1368 O O   . PHE A 112 ? 0.1876 0.1686 0.3665 -0.0042 -0.0041 -0.0320 92  PHE A O   
1369 C CB  . PHE A 112 ? 0.1765 0.1710 0.3536 -0.0237 0.0145  -0.0242 92  PHE A CB  
1370 C CG  . PHE A 112 ? 0.1825 0.2097 0.3423 -0.0013 0.0144  -0.0032 92  PHE A CG  
1371 C CD1 . PHE A 112 ? 0.1910 0.2370 0.3448 -0.0018 0.0175  -0.0248 92  PHE A CD1 
1372 C CD2 . PHE A 112 ? 0.1856 0.2423 0.3685 0.0184  0.0265  0.0193  92  PHE A CD2 
1373 C CE1 . PHE A 112 ? 0.2041 0.2974 0.3286 0.0162  0.0189  -0.0652 92  PHE A CE1 
1374 C CE2 . PHE A 112 ? 0.2125 0.2428 0.3793 0.0212  0.0246  0.0155  92  PHE A CE2 
1375 C CZ  . PHE A 112 ? 0.2128 0.2775 0.3526 0.0567  0.0395  -0.0109 92  PHE A CZ  
1385 N N   . GLU A 113 ? 0.1869 0.1684 0.4293 -0.0135 0.0078  -0.0588 93  GLU A N   
1386 C CA  . GLU A 113 ? 0.2173 0.1695 0.4668 0.0248  0.0246  -0.0384 93  GLU A CA  
1387 C C   . GLU A 113 ? 0.1668 0.1805 0.4380 0.0051  0.0181  0.0075  93  GLU A C   
1388 O O   . GLU A 113 ? 0.1666 0.2481 0.4485 0.0162  -0.0042 0.0144  93  GLU A O   
1389 C CB  . GLU A 113 ? 0.3131 0.2248 0.5598 0.0653  0.0275  -0.0628 93  GLU A CB  
1390 C CG  . GLU A 113 ? 0.3933 0.3176 0.6334 0.0990  0.0192  -0.1211 93  GLU A CG  
1391 C CD  . GLU A 113 ? 0.4817 0.3867 0.6842 0.0903  0.0062  -0.1695 93  GLU A CD  
1392 O OE1 . GLU A 113 ? 0.4988 0.3665 0.6888 0.1039  -0.0426 -0.1759 93  GLU A OE1 
1393 O OE2 . GLU A 113 ? 0.5307 0.4831 0.7249 0.0698  0.0175  -0.1712 93  GLU A OE2 
1400 N N   . THR A 114 ? 0.1838 0.1871 0.4525 -0.0039 -0.0064 0.0132  94  THR A N   
1401 C CA  . THR A 114 ? 0.1889 0.1494 0.4721 0.0102  0.0132  0.0147  94  THR A CA  
1402 C C   . THR A 114 ? 0.1841 0.1435 0.5047 0.0132  0.0011  0.0200  94  THR A C   
1403 O O   . THR A 114 ? 0.2069 0.1673 0.5257 0.0158  0.0220  0.0364  94  THR A O   
1404 C CB  . THR A 114 ? 0.1900 0.1645 0.4154 0.0249  0.0137  0.0282  94  THR A CB  
1405 O OG1 . THR A 114 ? 0.1941 0.1686 0.4148 0.0147  0.0113  0.0513  94  THR A OG1 
1406 C CG2 . THR A 114 ? 0.2082 0.1558 0.3962 0.0169  0.0528  0.0499  94  THR A CG2 
1414 N N   . GLN A 115 ? 0.1675 0.1894 0.5116 0.0046  0.0039  0.0535  95  GLN A N   
1415 C CA  . GLN A 115 ? 0.1896 0.1821 0.5280 0.0077  0.0176  0.0847  95  GLN A CA  
1416 C C   . GLN A 115 ? 0.1808 0.1939 0.5539 0.0101  0.0121  0.0928  95  GLN A C   
1417 O O   . GLN A 115 ? 0.2149 0.1936 0.5940 0.0309  0.0102  0.0717  95  GLN A O   
1418 C CB  . GLN A 115 ? 0.2082 0.1962 0.5097 -0.0166 0.0409  0.0895  95  GLN A CB  
1419 C CG  . GLN A 115 ? 0.2137 0.2045 0.4877 0.0154  0.0330  0.0977  95  GLN A CG  
1420 C CD  . GLN A 115 ? 0.2489 0.2297 0.5002 0.0439  0.0289  0.1019  95  GLN A CD  
1421 O OE1 . GLN A 115 ? 0.2170 0.1932 0.5253 0.0195  0.0151  0.0776  95  GLN A OE1 
1422 N NE2 . GLN A 115 ? 0.3283 0.2839 0.5182 0.0738  0.0466  0.1073  95  GLN A NE2 
1431 N N   . ASP A 116 ? 0.1809 0.1991 0.5338 -0.0071 -0.0093 0.0952  96  ASP A N   
1432 C CA  . ASP A 116 ? 0.2054 0.2362 0.5168 -0.0122 -0.0078 0.0726  96  ASP A CA  
1433 C C   . ASP A 116 ? 0.1753 0.1911 0.5440 0.0085  -0.0190 0.0995  96  ASP A C   
1434 O O   . ASP A 116 ? 0.1625 0.1765 0.5796 0.0022  -0.0082 0.1015  96  ASP A O   
1435 C CB  . ASP A 116 ? 0.2274 0.2380 0.4606 -0.0124 0.0042  0.0763  96  ASP A CB  
1436 C CG  . ASP A 116 ? 0.2510 0.2767 0.4722 0.0150  0.0140  0.0888  96  ASP A CG  
1437 O OD1 . ASP A 116 ? 0.2149 0.2866 0.4746 -0.0174 0.0232  0.0709  96  ASP A OD1 
1438 O OD2 . ASP A 116 ? 0.3007 0.2719 0.4752 0.0187  -0.0033 0.0974  96  ASP A OD2 
1443 N N   . PRO A 117 ? 0.1892 0.1925 0.5347 0.0108  -0.0221 0.0846  97  PRO A N   
1444 C CA  . PRO A 117 ? 0.1894 0.1827 0.5257 0.0072  -0.0138 0.0735  97  PRO A CA  
1445 C C   . PRO A 117 ? 0.1851 0.1890 0.5074 0.0129  -0.0218 0.0493  97  PRO A C   
1446 O O   . PRO A 117 ? 0.1913 0.2085 0.5015 0.0138  0.0008  0.0385  97  PRO A O   
1447 C CB  . PRO A 117 ? 0.2450 0.1816 0.5505 0.0309  -0.0289 0.0915  97  PRO A CB  
1448 C CG  . PRO A 117 ? 0.2767 0.2117 0.5634 0.0561  -0.0360 0.1081  97  PRO A CG  
1449 C CD  . PRO A 117 ? 0.2317 0.2047 0.5445 0.0244  -0.0436 0.0951  97  PRO A CD  
1457 N N   . ASN A 118 ? 0.1728 0.1646 0.4990 0.0005  -0.0148 0.0488  98  ASN A N   
1458 C CA  . ASN A 118 ? 0.1726 0.1920 0.5013 0.0031  -0.0331 0.0665  98  ASN A CA  
1459 C C   . ASN A 118 ? 0.1605 0.1907 0.4797 0.0265  -0.0181 0.0587  98  ASN A C   
1460 O O   . ASN A 118 ? 0.1700 0.1914 0.4936 0.0212  -0.0260 0.0534  98  ASN A O   
1461 C CB  . ASN A 118 ? 0.1781 0.2258 0.5344 0.0128  -0.0203 0.0809  98  ASN A CB  
1462 C CG  . ASN A 118 ? 0.2250 0.2518 0.5508 0.0370  -0.0135 0.1054  98  ASN A CG  
1463 O OD1 . ASN A 118 ? 0.2532 0.2973 0.5506 0.0665  0.0026  0.1056  98  ASN A OD1 
1464 N ND2 . ASN A 118 ? 0.2609 0.2498 0.5828 0.0329  -0.0549 0.0860  98  ASN A ND2 
1471 N N   . TRP A 119 ? 0.1620 0.1708 0.4539 0.0319  -0.0041 0.0644  99  TRP A N   
1472 C CA  . TRP A 119 ? 0.1477 0.1686 0.4077 0.0133  -0.0152 0.0410  99  TRP A CA  
1473 C C   . TRP A 119 ? 0.1325 0.1775 0.3885 0.0031  -0.0335 0.0108  99  TRP A C   
1474 O O   . TRP A 119 ? 0.1570 0.1971 0.4044 -0.0180 -0.0272 0.0276  99  TRP A O   
1475 C CB  . TRP A 119 ? 0.1703 0.1708 0.3938 0.0022  0.0113  0.0458  99  TRP A CB  
1476 C CG  . TRP A 119 ? 0.1798 0.1790 0.3551 -0.0032 -0.0008 0.0601  99  TRP A CG  
1477 C CD1 . TRP A 119 ? 0.1662 0.1922 0.3381 0.0091  -0.0026 0.0468  99  TRP A CD1 
1478 C CD2 . TRP A 119 ? 0.1847 0.2096 0.3416 0.0109  0.0283  0.0590  99  TRP A CD2 
1479 N NE1 . TRP A 119 ? 0.1685 0.1894 0.3286 0.0202  -0.0091 0.0455  99  TRP A NE1 
1480 C CE2 . TRP A 119 ? 0.1786 0.2093 0.3238 0.0137  0.0091  0.0549  99  TRP A CE2 
1481 C CE3 . TRP A 119 ? 0.2002 0.2387 0.3517 0.0189  0.0245  0.0787  99  TRP A CE3 
1482 C CZ2 . TRP A 119 ? 0.2238 0.2449 0.3185 0.0237  0.0015  0.0590  99  TRP A CZ2 
1483 C CZ3 . TRP A 119 ? 0.2383 0.2764 0.3754 0.0284  0.0270  0.0807  99  TRP A CZ3 
1484 C CH2 . TRP A 119 ? 0.2499 0.2534 0.3578 0.0365  0.0096  0.0590  99  TRP A CH2 
1495 N N   . PHE A 120 ? 0.1525 0.1698 0.3840 0.0010  0.0052  0.0315  100 PHE A N   
1496 C CA  . PHE A 120 ? 0.1653 0.1633 0.3595 0.0102  0.0061  0.0108  100 PHE A CA  
1497 C C   . PHE A 120 ? 0.1703 0.1667 0.3192 0.0005  -0.0087 -0.0009 100 PHE A C   
1498 O O   . PHE A 120 ? 0.1761 0.1764 0.3338 -0.0131 -0.0245 0.0034  100 PHE A O   
1499 C CB  . PHE A 120 ? 0.1562 0.1761 0.3832 0.0062  0.0091  -0.0156 100 PHE A CB  
1500 C CG  . PHE A 120 ? 0.1724 0.2033 0.3985 0.0327  -0.0006 -0.0091 100 PHE A CG  
1501 C CD1 . PHE A 120 ? 0.2395 0.2479 0.4142 0.0610  0.0198  -0.0120 100 PHE A CD1 
1502 C CD2 . PHE A 120 ? 0.1870 0.2087 0.4446 0.0016  0.0135  -0.0419 100 PHE A CD2 
1503 C CE1 . PHE A 120 ? 0.2747 0.2658 0.4799 0.0702  0.0426  0.0194  100 PHE A CE1 
1504 C CE2 . PHE A 120 ? 0.2116 0.2129 0.4974 0.0120  0.0262  -0.0542 100 PHE A CE2 
1505 C CZ  . PHE A 120 ? 0.2502 0.1863 0.5054 0.0388  0.0457  -0.0162 100 PHE A CZ  
1515 N N   . TRP A 121 ? 0.1633 0.1563 0.3083 -0.0130 -0.0078 -0.0001 101 TRP A N   
1516 C CA  . TRP A 121 ? 0.1546 0.1627 0.2799 0.0042  -0.0057 0.0007  101 TRP A CA  
1517 C C   . TRP A 121 ? 0.1691 0.1789 0.2875 -0.0225 0.0117  -0.0101 101 TRP A C   
1518 O O   . TRP A 121 ? 0.2259 0.1720 0.3268 -0.0201 -0.0020 -0.0301 101 TRP A O   
1519 C CB  . TRP A 121 ? 0.1809 0.1740 0.2745 0.0035  -0.0023 0.0032  101 TRP A CB  
1520 C CG  . TRP A 121 ? 0.1758 0.1558 0.2862 0.0298  0.0159  0.0108  101 TRP A CG  
1521 C CD1 . TRP A 121 ? 0.1950 0.1786 0.3028 0.0143  0.0292  0.0112  101 TRP A CD1 
1522 C CD2 . TRP A 121 ? 0.1607 0.1510 0.2932 0.0123  -0.0056 -0.0022 101 TRP A CD2 
1523 N NE1 . TRP A 121 ? 0.2048 0.1901 0.2903 0.0147  0.0346  0.0196  101 TRP A NE1 
1524 C CE2 . TRP A 121 ? 0.1768 0.1656 0.2926 0.0026  0.0069  0.0115  101 TRP A CE2 
1525 C CE3 . TRP A 121 ? 0.1575 0.1602 0.3099 0.0167  -0.0136 -0.0088 101 TRP A CE3 
1526 C CZ2 . TRP A 121 ? 0.1565 0.1887 0.2870 0.0072  0.0142  0.0200  101 TRP A CZ2 
1527 C CZ3 . TRP A 121 ? 0.1470 0.1722 0.2854 0.0076  0.0018  0.0199  101 TRP A CZ3 
1528 C CH2 . TRP A 121 ? 0.1486 0.2012 0.2682 0.0098  -0.0036 0.0101  101 TRP A CH2 
1539 N N   . VAL A 122 ? 0.1718 0.1634 0.2580 -0.0101 -0.0031 -0.0276 102 VAL A N   
1540 C CA  . VAL A 122 ? 0.1516 0.1577 0.2597 0.0070  0.0033  -0.0378 102 VAL A CA  
1541 C C   . VAL A 122 ? 0.1703 0.1595 0.2584 -0.0122 -0.0060 -0.0323 102 VAL A C   
1542 O O   . VAL A 122 ? 0.2038 0.1580 0.2820 0.0080  -0.0445 -0.0395 102 VAL A O   
1543 C CB  . VAL A 122 ? 0.1616 0.1888 0.2608 0.0058  -0.0077 -0.0276 102 VAL A CB  
1544 C CG1 . VAL A 122 ? 0.1729 0.2484 0.2718 0.0155  0.0068  -0.0048 102 VAL A CG1 
1545 C CG2 . VAL A 122 ? 0.1880 0.1943 0.2727 0.0105  0.0055  -0.0232 102 VAL A CG2 
1555 N N   . GLU A 123 ? 0.1609 0.1695 0.2416 -0.0152 0.0105  -0.0335 103 GLU A N   
1556 C CA  . GLU A 123 ? 0.1634 0.1690 0.2469 0.0050  0.0002  -0.0199 103 GLU A CA  
1557 C C   . GLU A 123 ? 0.1691 0.1748 0.2591 0.0085  -0.0005 -0.0477 103 GLU A C   
1558 O O   . GLU A 123 ? 0.2127 0.1745 0.2596 -0.0066 0.0239  -0.0468 103 GLU A O   
1559 C CB  . GLU A 123 ? 0.1549 0.1791 0.2365 0.0082  0.0002  -0.0287 103 GLU A CB  
1560 C CG  . GLU A 123 ? 0.1633 0.2050 0.2464 0.0067  -0.0107 -0.0280 103 GLU A CG  
1561 C CD  . GLU A 123 ? 0.1785 0.2324 0.2835 0.0138  -0.0111 -0.0190 103 GLU A CD  
1562 O OE1 . GLU A 123 ? 0.1771 0.2202 0.3055 -0.0002 0.0038  -0.0462 103 GLU A OE1 
1563 O OE2 . GLU A 123 ? 0.1642 0.2374 0.3374 0.0004  0.0022  -0.0137 103 GLU A OE2 
1570 N N   . CYS A 124 ? 0.1554 0.1815 0.2358 0.0049  0.0277  -0.0535 104 CYS A N   
1571 C CA  . CYS A 124 ? 0.1761 0.2050 0.2039 0.0051  0.0364  -0.0389 104 CYS A CA  
1572 C C   . CYS A 124 ? 0.1968 0.2234 0.1802 -0.0039 0.0217  -0.0531 104 CYS A C   
1573 O O   . CYS A 124 ? 0.1928 0.2151 0.1970 -0.0236 0.0182  -0.0344 104 CYS A O   
1574 C CB  . CYS A 124 ? 0.1895 0.2069 0.2166 0.0004  0.0211  -0.0360 104 CYS A CB  
1575 S SG  . CYS A 124 ? 0.1826 0.2197 0.2558 -0.0063 -0.0072 -0.0321 104 CYS A SG  
1581 N N   . ARG A 125 ? 0.2098 0.2078 0.1731 -0.0006 0.0173  -0.0544 105 ARG A N   
1582 C CA  . ARG A 125 ? 0.2154 0.2063 0.1570 -0.0126 0.0122  -0.0465 105 ARG A CA  
1583 C C   . ARG A 125 ? 0.2030 0.2216 0.1546 -0.0154 0.0204  -0.0440 105 ARG A C   
1584 O O   . ARG A 125 ? 0.2012 0.2087 0.2180 -0.0051 0.0066  -0.0359 105 ARG A O   
1585 C CB  . ARG A 125 ? 0.2103 0.2573 0.1607 -0.0173 0.0223  -0.0359 105 ARG A CB  
1586 C CG  . ARG A 125 ? 0.2299 0.2831 0.2346 -0.0357 -0.0097 0.0022  105 ARG A CG  
1587 C CD  . ARG A 125 ? 0.2765 0.3289 0.3277 -0.0322 -0.0335 0.0160  105 ARG A CD  
1588 N NE  . ARG A 125 ? 0.3192 0.3944 0.3881 0.0114  -0.0137 0.0280  105 ARG A NE  
1589 C CZ  . ARG A 125 ? 0.3178 0.3893 0.3921 0.0294  0.0015  0.0342  105 ARG A CZ  
1590 N NH1 . ARG A 125 ? 0.3385 0.4029 0.3537 0.0540  0.0147  0.0781  105 ARG A NH1 
1591 N NH2 . ARG A 125 ? 0.2829 0.3294 0.4111 -0.0149 0.0040  0.0302  105 ARG A NH2 
1605 N N   . GLY A 126 ? 0.1697 0.2275 0.1842 -0.0011 0.0397  -0.0287 106 GLY A N   
1606 C CA  . GLY A 126 ? 0.1751 0.2096 0.1886 0.0052  0.0335  -0.0330 106 GLY A CA  
1607 C C   . GLY A 126 ? 0.1780 0.2121 0.1810 -0.0039 0.0235  -0.0374 106 GLY A C   
1608 O O   . GLY A 126 ? 0.1916 0.2202 0.1948 0.0004  0.0307  -0.0316 106 GLY A O   
1612 N N   . GLU A 127 ? 0.1831 0.2205 0.1806 0.0007  0.0273  -0.0071 107 GLU A N   
1613 C CA  . GLU A 127 ? 0.2209 0.2172 0.1662 -0.0188 0.0355  -0.0199 107 GLU A CA  
1614 C C   . GLU A 127 ? 0.2038 0.2255 0.1538 -0.0171 0.0295  -0.0336 107 GLU A C   
1615 O O   . GLU A 127 ? 0.1924 0.2310 0.1951 -0.0034 0.0357  -0.0318 107 GLU A O   
1616 C CB  . GLU A 127 ? 0.2450 0.2529 0.1564 -0.0194 -0.0009 -0.0483 107 GLU A CB  
1617 C CG  . GLU A 127 ? 0.2591 0.2950 0.1786 -0.0317 -0.0005 -0.0889 107 GLU A CG  
1618 C CD  . GLU A 127 ? 0.2783 0.3398 0.2199 -0.0531 0.0072  -0.1188 107 GLU A CD  
1619 O OE1 . GLU A 127 ? 0.2880 0.3632 0.2354 -0.0039 -0.0134 -0.0824 107 GLU A OE1 
1620 O OE2 . GLU A 127 ? 0.3212 0.4008 0.2478 -0.0272 0.0401  -0.0683 107 GLU A OE2 
1627 N N   . GLY A 128 ? 0.2230 0.2215 0.1817 -0.0297 0.0279  -0.0027 108 GLY A N   
1628 C CA  . GLY A 128 ? 0.2294 0.2393 0.1807 -0.0386 0.0248  -0.0295 108 GLY A CA  
1629 C C   . GLY A 128 ? 0.2152 0.2315 0.1927 -0.0300 0.0155  -0.0116 108 GLY A C   
1630 O O   . GLY A 128 ? 0.2202 0.2305 0.2079 -0.0182 0.0168  -0.0192 108 GLY A O   
1634 N N   . ALA A 129 ? 0.2430 0.2492 0.1820 -0.0636 0.0349  0.0053  109 ALA A N   
1635 C CA  . ALA A 129 ? 0.2504 0.2567 0.1905 -0.0510 0.0622  0.0031  109 ALA A CA  
1636 C C   . ALA A 129 ? 0.2359 0.2356 0.2037 -0.0512 0.0671  0.0033  109 ALA A C   
1637 O O   . ALA A 129 ? 0.2589 0.2238 0.2030 -0.0303 0.0511  -0.0020 109 ALA A O   
1638 C CB  . ALA A 129 ? 0.2772 0.2657 0.1883 -0.0470 0.0516  0.0164  109 ALA A CB  
1644 N N   . ILE A 130 ? 0.2268 0.2347 0.1969 -0.0269 0.0248  -0.0068 110 ILE A N   
1645 C CA  . ILE A 130 ? 0.2310 0.2296 0.1745 -0.0471 0.0203  -0.0070 110 ILE A CA  
1646 C C   . ILE A 130 ? 0.2439 0.2175 0.1889 -0.0346 0.0076  0.0074  110 ILE A C   
1647 O O   . ILE A 130 ? 0.2516 0.2299 0.1987 -0.0390 -0.0201 0.0046  110 ILE A O   
1648 C CB  . ILE A 130 ? 0.2377 0.2486 0.1931 -0.0417 0.0105  0.0003  110 ILE A CB  
1649 C CG1 . ILE A 130 ? 0.2404 0.2520 0.2105 -0.0278 0.0289  -0.0146 110 ILE A CG1 
1650 C CG2 . ILE A 130 ? 0.2336 0.2737 0.2364 -0.0594 0.0157  -0.0067 110 ILE A CG2 
1651 C CD1 . ILE A 130 ? 0.2412 0.2687 0.2177 -0.0264 0.0518  -0.0011 110 ILE A CD1 
1663 N N   . VAL A 131 ? 0.2367 0.2178 0.2290 -0.0432 0.0080  0.0119  111 VAL A N   
1664 C CA  . VAL A 131 ? 0.2228 0.2283 0.2401 -0.0408 0.0199  0.0258  111 VAL A CA  
1665 C C   . VAL A 131 ? 0.2122 0.2321 0.2383 -0.0520 0.0058  -0.0054 111 VAL A C   
1666 O O   . VAL A 131 ? 0.2409 0.2512 0.2323 -0.0503 0.0005  -0.0217 111 VAL A O   
1667 C CB  . VAL A 131 ? 0.2514 0.2614 0.2456 -0.0375 0.0398  0.0215  111 VAL A CB  
1668 C CG1 . VAL A 131 ? 0.2672 0.3098 0.2603 -0.0653 0.0677  0.0186  111 VAL A CG1 
1669 C CG2 . VAL A 131 ? 0.2797 0.2868 0.2859 -0.0419 0.0791  0.0375  111 VAL A CG2 
1679 N N   . PHE A 132 ? 0.2043 0.2317 0.2562 -0.0444 0.0005  -0.0079 112 PHE A N   
1680 C CA  . PHE A 132 ? 0.2003 0.2879 0.2651 -0.0332 0.0156  -0.0030 112 PHE A CA  
1681 C C   . PHE A 132 ? 0.2343 0.3230 0.2972 -0.0306 0.0082  -0.0441 112 PHE A C   
1682 O O   . PHE A 132 ? 0.2644 0.2825 0.3436 -0.0155 -0.0297 -0.0678 112 PHE A O   
1699 N N   . PRO A 133 ? 0.2462 0.3544 0.3248 -0.0397 -0.0181 -0.0734 113 PRO A N   
1700 C CA  . PRO A 133 ? 0.2224 0.3970 0.3787 -0.0239 -0.0170 -0.1100 113 PRO A CA  
1701 C C   . PRO A 133 ? 0.2376 0.4033 0.4170 -0.0234 -0.0316 -0.1386 113 PRO A C   
1702 O O   . PRO A 133 ? 0.2323 0.4687 0.4270 -0.0134 -0.0092 -0.1662 113 PRO A O   
1703 C CB  . PRO A 133 ? 0.2425 0.4381 0.3653 -0.0083 -0.0287 -0.0862 113 PRO A CB  
1704 C CG  . PRO A 133 ? 0.2653 0.4763 0.3688 -0.0621 -0.0535 -0.0245 113 PRO A CG  
1705 C CD  . PRO A 133 ? 0.2581 0.4474 0.3406 -0.0769 -0.0343 -0.0224 113 PRO A CD  
1713 N N   . GLY A 134 ? 0.2887 0.3453 0.4489 -0.0204 -0.0458 -0.1560 114 GLY A N   
1714 C CA  . GLY A 134 ? 0.2918 0.3411 0.4652 -0.0383 -0.0223 -0.1241 114 GLY A CA  
1715 C C   . GLY A 134 ? 0.3050 0.3097 0.4554 -0.0474 -0.0104 -0.0813 114 GLY A C   
1716 O O   . GLY A 134 ? 0.3547 0.3110 0.4846 -0.0522 -0.0193 -0.0767 114 GLY A O   
1720 N N   . TYR A 135 ? 0.2792 0.2314 0.3942 -0.0602 -0.0126 -0.0487 115 TYR A N   
1721 C CA  . TYR A 135 ? 0.2919 0.2091 0.3762 -0.0488 -0.0173 -0.0068 115 TYR A CA  
1722 C C   . TYR A 135 ? 0.3253 0.2513 0.3740 -0.0535 -0.0251 -0.0001 115 TYR A C   
1723 O O   . TYR A 135 ? 0.3170 0.3185 0.3591 -0.0442 -0.0323 -0.0127 115 TYR A O   
1724 C CB  . TYR A 135 ? 0.2716 0.2107 0.3656 -0.0615 -0.0274 -0.0045 115 TYR A CB  
1725 C CG  . TYR A 135 ? 0.2471 0.2042 0.3557 -0.0488 -0.0028 -0.0044 115 TYR A CG  
1726 C CD1 . TYR A 135 ? 0.2353 0.1994 0.3608 -0.0261 -0.0003 -0.0007 115 TYR A CD1 
1727 C CD2 . TYR A 135 ? 0.2413 0.2129 0.3744 -0.0489 0.0041  0.0401  115 TYR A CD2 
1728 C CE1 . TYR A 135 ? 0.2432 0.2245 0.3886 -0.0244 0.0179  0.0077  115 TYR A CE1 
1729 C CE2 . TYR A 135 ? 0.2296 0.2248 0.3986 -0.0599 0.0236  0.0509  115 TYR A CE2 
1730 C CZ  . TYR A 135 ? 0.2272 0.2153 0.3960 -0.0431 0.0249  0.0041  115 TYR A CZ  
1731 O OH  . TYR A 135 ? 0.2331 0.2400 0.4365 -0.0359 0.0504  -0.0071 115 TYR A OH  
1741 N N   . PRO A 136 ? 0.3721 0.2417 0.3845 -0.0747 -0.0111 0.0216  116 PRO A N   
1742 C CA  . PRO A 136 ? 0.3678 0.2768 0.3620 -0.0866 -0.0117 0.0499  116 PRO A CA  
1743 C C   . PRO A 136 ? 0.3510 0.2556 0.3265 -0.0760 0.0090  0.0596  116 PRO A C   
1744 O O   . PRO A 136 ? 0.3254 0.2570 0.3026 -0.0766 0.0129  0.0725  116 PRO A O   
1745 C CB  . PRO A 136 ? 0.4128 0.3201 0.3990 -0.0668 -0.0145 0.0503  116 PRO A CB  
1746 C CG  . PRO A 136 ? 0.4255 0.3146 0.4169 -0.0426 -0.0156 0.0332  116 PRO A CG  
1747 C CD  . PRO A 136 ? 0.4135 0.2378 0.3998 -0.0498 -0.0150 0.0371  116 PRO A CD  
1755 N N   A ARG A 137 ? 0.3517 0.2722 0.3263 -0.0637 0.0269  0.0404  117 ARG A N   
1756 N N   B ARG A 137 ? 0.3667 0.2848 0.3305 -0.0600 0.0139  0.0391  117 ARG A N   
1757 C CA  A ARG A 137 ? 0.3778 0.3095 0.2900 -0.0474 0.0497  0.0233  117 ARG A CA  
1758 C CA  B ARG A 137 ? 0.3971 0.3281 0.3123 -0.0415 0.0204  0.0216  117 ARG A CA  
1759 C C   A ARG A 137 ? 0.3827 0.2889 0.2886 -0.0220 -0.0090 0.0270  117 ARG A C   
1760 C C   B ARG A 137 ? 0.3879 0.3059 0.2934 -0.0239 -0.0156 0.0257  117 ARG A C   
1761 O O   A ARG A 137 ? 0.4206 0.3164 0.3100 -0.0033 -0.0435 0.0481  117 ARG A O   
1762 O O   B ARG A 137 ? 0.4168 0.3316 0.3037 -0.0100 -0.0333 0.0409  117 ARG A O   
1763 C CB  A ARG A 137 ? 0.4299 0.3931 0.2890 -0.0402 0.1158  -0.0004 117 ARG A CB  
1764 C CB  B ARG A 137 ? 0.4561 0.4128 0.3357 -0.0282 0.0561  -0.0036 117 ARG A CB  
1765 C CG  A ARG A 137 ? 0.4679 0.4468 0.3053 -0.0428 0.1515  0.0246  117 ARG A CG  
1766 C CG  B ARG A 137 ? 0.4990 0.4825 0.3623 -0.0141 0.0784  0.0011  117 ARG A CG  
1767 C CD  A ARG A 137 ? 0.5073 0.5092 0.3321 -0.0464 0.1699  0.0446  117 ARG A CD  
1768 C CD  B ARG A 137 ? 0.5356 0.5368 0.3892 -0.0201 0.1019  0.0150  117 ARG A CD  
1769 N NE  A ARG A 137 ? 0.5301 0.5842 0.3547 -0.0526 0.1943  0.0719  117 ARG A NE  
1770 N NE  B ARG A 137 ? 0.5581 0.5802 0.4044 -0.0409 0.1143  0.0252  117 ARG A NE  
1771 C CZ  A ARG A 137 ? 0.5501 0.6307 0.3750 -0.0653 0.2038  0.0767  117 ARG A CZ  
1772 C CZ  B ARG A 137 ? 0.5772 0.6225 0.4185 -0.0518 0.1339  0.0377  117 ARG A CZ  
1773 N NH1 A ARG A 137 ? 0.5764 0.6579 0.3993 -0.0608 0.1998  0.0631  117 ARG A NH1 
1774 N NH1 B ARG A 137 ? 0.5885 0.6336 0.4225 -0.0623 0.1405  0.0434  117 ARG A NH1 
1775 N NH2 A ARG A 137 ? 0.5480 0.6483 0.3837 -0.0786 0.2036  0.0945  117 ARG A NH2 
1776 N NH2 B ARG A 137 ? 0.5772 0.6377 0.4257 -0.0587 0.1490  0.0418  117 ARG A NH2 
1803 N N   . GLY A 138 ? 0.3579 0.2907 0.2830 -0.0294 -0.0373 0.0269  118 GLY A N   
1804 C CA  . GLY A 138 ? 0.3443 0.2965 0.2777 -0.0112 -0.0595 0.0213  118 GLY A CA  
1805 C C   . GLY A 138 ? 0.3100 0.2654 0.2411 -0.0282 -0.0324 0.0406  118 GLY A C   
1806 O O   . GLY A 138 ? 0.3119 0.2666 0.2535 -0.0085 -0.0195 0.0315  118 GLY A O   
1811 N N   A GLN A 139 ? 0.3102 0.2688 0.2533 -0.0437 -0.0298 0.0344  119 GLN A N   
1812 N N   B GLN A 139 ? 0.3098 0.2675 0.2531 -0.0457 -0.0304 0.0343  119 GLN A N   
1813 C CA  A GLN A 139 ? 0.3196 0.2789 0.2593 -0.0260 -0.0124 0.0309  119 GLN A CA  
1814 C CA  B GLN A 139 ? 0.3181 0.2766 0.2588 -0.0269 -0.0109 0.0309  119 GLN A CA  
1815 C C   A GLN A 139 ? 0.2775 0.2876 0.2495 0.0018  0.0086  0.0370  119 GLN A C   
1816 C C   B GLN A 139 ? 0.2747 0.2883 0.2489 0.0015  0.0089  0.0377  119 GLN A C   
1817 O O   A GLN A 139 ? 0.3152 0.3449 0.2654 0.0514  0.0258  0.0674  119 GLN A O   
1818 O O   B GLN A 139 ? 0.3173 0.3455 0.2662 0.0539  0.0265  0.0679  119 GLN A O   
1819 C CB  A GLN A 139 ? 0.3951 0.3327 0.2770 -0.0176 -0.0393 0.0312  119 GLN A CB  
1820 C CB  B GLN A 139 ? 0.3923 0.3303 0.2747 -0.0169 -0.0381 0.0331  119 GLN A CB  
1821 C CG  A GLN A 139 ? 0.4768 0.4083 0.3300 0.0032  -0.0900 0.0092  119 GLN A CG  
1822 C CG  B GLN A 139 ? 0.4681 0.3988 0.3251 0.0063  -0.0944 0.0116  119 GLN A CG  
1823 C CD  A GLN A 139 ? 0.5454 0.4665 0.3695 0.0400  -0.1279 -0.0291 119 GLN A CD  
1824 C CD  B GLN A 139 ? 0.5380 0.4555 0.3631 0.0452  -0.1411 -0.0225 119 GLN A CD  
1825 O OE1 A GLN A 139 ? 0.5705 0.5175 0.3788 0.0579  -0.1296 -0.0436 119 GLN A OE1 
1826 O OE1 B GLN A 139 ? 0.5661 0.5072 0.3763 0.0546  -0.1368 -0.0484 119 GLN A OE1 
1827 N NE2 A GLN A 139 ? 0.5737 0.4816 0.3876 0.0429  -0.1394 -0.0269 119 GLN A NE2 
1828 N NE2 B GLN A 139 ? 0.5661 0.4567 0.3658 0.0500  -0.1614 -0.0296 119 GLN A NE2 
1845 N N   . TYR A 140 ? 0.2396 0.2282 0.2374 -0.0222 0.0200  -0.0015 120 TYR A N   
1846 C CA  . TYR A 140 ? 0.2333 0.2313 0.2248 -0.0309 0.0427  -0.0093 120 TYR A CA  
1847 C C   . TYR A 140 ? 0.2163 0.2185 0.2114 -0.0072 0.0508  -0.0126 120 TYR A C   
1848 O O   . TYR A 140 ? 0.2097 0.2324 0.2518 -0.0058 0.0430  -0.0297 120 TYR A O   
1849 C CB  . TYR A 140 ? 0.2671 0.2333 0.2035 -0.0467 0.0230  -0.0185 120 TYR A CB  
1850 C CG  . TYR A 140 ? 0.2530 0.2108 0.1888 -0.0456 0.0203  -0.0266 120 TYR A CG  
1851 C CD1 . TYR A 140 ? 0.2483 0.2095 0.1922 -0.0427 0.0238  -0.0317 120 TYR A CD1 
1852 C CD2 . TYR A 140 ? 0.2541 0.2333 0.1675 -0.0229 0.0092  -0.0205 120 TYR A CD2 
1853 C CE1 . TYR A 140 ? 0.2538 0.1990 0.1791 -0.0050 0.0109  -0.0345 120 TYR A CE1 
1854 C CE2 . TYR A 140 ? 0.2780 0.2441 0.1518 0.0135  0.0060  -0.0125 120 TYR A CE2 
1855 C CZ  . TYR A 140 ? 0.2659 0.1984 0.1704 0.0022  0.0305  -0.0232 120 TYR A CZ  
1856 O OH  . TYR A 140 ? 0.3018 0.2448 0.2063 -0.0335 0.0369  -0.0341 120 TYR A OH  
1867 N N   . ARG A 141 ? 0.2109 0.2071 0.1995 -0.0281 0.0369  -0.0115 121 ARG A N   
1868 C CA  . ARG A 141 ? 0.2356 0.2223 0.1760 -0.0177 0.0324  -0.0073 121 ARG A CA  
1869 C C   . ARG A 141 ? 0.2262 0.2086 0.1874 -0.0117 0.0415  -0.0038 121 ARG A C   
1870 O O   . ARG A 141 ? 0.2470 0.2190 0.2484 0.0081  0.0526  -0.0253 121 ARG A O   
1871 C CB  . ARG A 141 ? 0.2581 0.2624 0.1948 -0.0182 0.0122  -0.0258 121 ARG A CB  
1872 C CG  . ARG A 141 ? 0.2826 0.2899 0.2158 -0.0223 -0.0174 -0.0262 121 ARG A CG  
1873 C CD  . ARG A 141 ? 0.2940 0.3093 0.2491 0.0214  -0.0544 -0.0158 121 ARG A CD  
1874 N NE  . ARG A 141 ? 0.3059 0.3553 0.2837 0.0183  -0.0395 -0.0401 121 ARG A NE  
1875 C CZ  . ARG A 141 ? 0.3411 0.3900 0.2970 -0.0236 -0.0236 -0.0589 121 ARG A CZ  
1876 N NH1 . ARG A 141 ? 0.3244 0.4078 0.2657 0.0136  0.0049  -0.0650 121 ARG A NH1 
1877 N NH2 . ARG A 141 ? 0.4053 0.4241 0.3523 -0.0450 -0.0321 -0.0681 121 ARG A NH2 
1891 N N   . ASN A 142 ? 0.2107 0.2150 0.1684 -0.0125 0.0294  -0.0062 122 ASN A N   
1892 C CA  . ASN A 142 ? 0.2236 0.2086 0.1630 -0.0156 0.0364  -0.0264 122 ASN A CA  
1893 C C   . ASN A 142 ? 0.1958 0.2140 0.1896 0.0059  0.0234  -0.0131 122 ASN A C   
1894 O O   . ASN A 142 ? 0.1858 0.2178 0.2058 0.0056  0.0474  -0.0210 122 ASN A O   
1895 C CB  . ASN A 142 ? 0.2626 0.2061 0.1830 -0.0010 0.0568  -0.0420 122 ASN A CB  
1896 C CG  . ASN A 142 ? 0.2709 0.1978 0.2405 -0.0212 0.0595  -0.0322 122 ASN A CG  
1897 O OD1 . ASN A 142 ? 0.2498 0.2043 0.2659 -0.0017 0.0808  -0.0301 122 ASN A OD1 
1898 N ND2 . ASN A 142 ? 0.2664 0.2015 0.2292 -0.0056 0.0379  -0.0334 122 ASN A ND2 
1905 N N   . HIS A 143 ? 0.2009 0.1941 0.2135 -0.0044 0.0349  -0.0109 123 HIS A N   
1906 C CA  . HIS A 143 ? 0.1860 0.2025 0.2005 -0.0047 0.0218  -0.0238 123 HIS A CA  
1907 C C   . HIS A 143 ? 0.1792 0.2070 0.1921 -0.0030 0.0252  -0.0401 123 HIS A C   
1908 O O   . HIS A 143 ? 0.1998 0.1985 0.2111 -0.0023 0.0041  -0.0227 123 HIS A O   
1909 C CB  . HIS A 143 ? 0.1803 0.2122 0.2028 0.0012  0.0110  -0.0113 123 HIS A CB  
1910 C CG  . HIS A 143 ? 0.1860 0.2126 0.2424 0.0150  0.0115  -0.0141 123 HIS A CG  
1911 N ND1 . HIS A 143 ? 0.1942 0.2313 0.2806 0.0068  0.0331  0.0055  123 HIS A ND1 
1912 C CD2 . HIS A 143 ? 0.1952 0.2335 0.2640 0.0065  0.0189  -0.0111 123 HIS A CD2 
1913 C CE1 . HIS A 143 ? 0.1971 0.2158 0.2937 0.0015  0.0332  0.0220  123 HIS A CE1 
1914 N NE2 . HIS A 143 ? 0.2089 0.2114 0.2894 -0.0056 0.0145  0.0004  123 HIS A NE2 
1922 N N   . PHE A 144 ? 0.1773 0.2024 0.2011 0.0126  0.0217  -0.0443 124 PHE A N   
1923 C CA  . PHE A 144 ? 0.1423 0.1673 0.1984 -0.0052 0.0111  -0.0193 124 PHE A CA  
1924 C C   . PHE A 144 ? 0.1675 0.1830 0.2085 -0.0013 0.0111  -0.0396 124 PHE A C   
1925 O O   . PHE A 144 ? 0.2084 0.1709 0.2168 -0.0146 -0.0051 -0.0421 124 PHE A O   
1926 C CB  . PHE A 144 ? 0.1714 0.2000 0.2083 -0.0034 0.0106  -0.0256 124 PHE A CB  
1927 C CG  . PHE A 144 ? 0.1610 0.2062 0.2120 -0.0092 0.0329  -0.0370 124 PHE A CG  
1928 C CD1 . PHE A 144 ? 0.1688 0.2442 0.2483 -0.0191 0.0574  -0.0259 124 PHE A CD1 
1929 C CD2 . PHE A 144 ? 0.1645 0.2376 0.2067 -0.0121 0.0393  -0.0335 124 PHE A CD2 
1930 C CE1 . PHE A 144 ? 0.1929 0.2451 0.2603 -0.0177 0.0593  -0.0279 124 PHE A CE1 
1931 C CE2 . PHE A 144 ? 0.1798 0.2437 0.2272 -0.0199 0.0705  -0.0449 124 PHE A CE2 
1932 C CZ  . PHE A 144 ? 0.1973 0.2232 0.2473 -0.0046 0.0735  -0.0340 124 PHE A CZ  
1942 N N   . LEU A 145 ? 0.1738 0.1709 0.2023 0.0111  0.0204  -0.0252 125 LEU A N   
1943 C CA  . LEU A 145 ? 0.1676 0.1762 0.1844 0.0083  -0.0029 -0.0319 125 LEU A CA  
1944 C C   . LEU A 145 ? 0.1698 0.1687 0.2170 0.0172  -0.0051 -0.0301 125 LEU A C   
1945 O O   . LEU A 145 ? 0.1615 0.1615 0.2782 0.0143  -0.0223 -0.0396 125 LEU A O   
1946 C CB  . LEU A 145 ? 0.1481 0.2234 0.2225 -0.0093 0.0059  -0.0241 125 LEU A CB  
1947 C CG  . LEU A 145 ? 0.1805 0.2694 0.2883 0.0084  0.0286  -0.0461 125 LEU A CG  
1948 C CD1 . LEU A 145 ? 0.2155 0.2719 0.3470 0.0213  0.0426  -0.0573 125 LEU A CD1 
1949 C CD2 . LEU A 145 ? 0.1936 0.3369 0.3118 -0.0482 0.0346  -0.0562 125 LEU A CD2 
1961 N N   . HIS A 146 ? 0.1677 0.1693 0.2372 0.0082  -0.0066 -0.0172 126 HIS A N   
1962 C CA  . HIS A 146 ? 0.1678 0.1833 0.2262 -0.0058 0.0020  -0.0118 126 HIS A CA  
1963 C C   . HIS A 146 ? 0.1610 0.1657 0.2261 0.0047  0.0001  -0.0051 126 HIS A C   
1964 O O   . HIS A 146 ? 0.1801 0.1750 0.2639 -0.0130 0.0075  -0.0112 126 HIS A O   
1965 C CB  . HIS A 146 ? 0.1746 0.1882 0.2406 -0.0006 0.0180  -0.0107 126 HIS A CB  
1966 C CG  . HIS A 146 ? 0.1816 0.2016 0.2315 0.0065  0.0047  -0.0068 126 HIS A CG  
1967 N ND1 . HIS A 146 ? 0.1991 0.2387 0.2898 -0.0122 -0.0113 0.0446  126 HIS A ND1 
1968 C CD2 . HIS A 146 ? 0.2279 0.2044 0.2502 -0.0041 0.0069  -0.0117 126 HIS A CD2 
1969 C CE1 . HIS A 146 ? 0.2095 0.2627 0.2752 -0.0095 -0.0060 0.0429  126 HIS A CE1 
1970 N NE2 . HIS A 146 ? 0.2066 0.2241 0.2467 -0.0007 0.0273  0.0050  126 HIS A NE2 
1978 N N   . SER A 147 ? 0.1507 0.1576 0.2358 0.0000  0.0035  0.0063  127 SER A N   
1979 C CA  . SER A 147 ? 0.1339 0.1502 0.2615 0.0055  -0.0194 0.0156  127 SER A CA  
1980 C C   . SER A 147 ? 0.1423 0.1471 0.2657 0.0021  0.0047  0.0174  127 SER A C   
1981 O O   . SER A 147 ? 0.1489 0.1528 0.2712 -0.0005 -0.0150 0.0137  127 SER A O   
1982 C CB  . SER A 147 ? 0.1586 0.1715 0.2688 0.0119  0.0119  0.0207  127 SER A CB  
1983 O OG  . SER A 147 ? 0.1549 0.1663 0.3047 0.0208  0.0213  0.0396  127 SER A OG  
1989 N N   . PHE A 148 ? 0.1427 0.1487 0.2940 0.0172  0.0020  0.0217  128 PHE A N   
1990 C CA  . PHE A 148 ? 0.1664 0.1326 0.2718 0.0122  -0.0070 0.0072  128 PHE A CA  
1991 C C   . PHE A 148 ? 0.1532 0.1488 0.3056 0.0238  -0.0137 0.0102  128 PHE A C   
1992 O O   . PHE A 148 ? 0.1554 0.1609 0.3539 0.0053  -0.0053 0.0123  128 PHE A O   
1993 C CB  . PHE A 148 ? 0.1813 0.1773 0.2658 0.0068  -0.0173 -0.0218 128 PHE A CB  
1994 C CG  . PHE A 148 ? 0.1621 0.1734 0.2834 -0.0058 -0.0068 -0.0073 128 PHE A CG  
1995 C CD1 . PHE A 148 ? 0.1704 0.1928 0.3014 0.0145  -0.0029 -0.0123 128 PHE A CD1 
1996 C CD2 . PHE A 148 ? 0.1637 0.1867 0.2796 0.0124  -0.0024 -0.0010 128 PHE A CD2 
1997 C CE1 . PHE A 148 ? 0.1793 0.2186 0.2733 0.0126  -0.0093 -0.0245 128 PHE A CE1 
1998 C CE2 . PHE A 148 ? 0.1805 0.2028 0.2700 0.0078  -0.0002 0.0053  128 PHE A CE2 
1999 C CZ  . PHE A 148 ? 0.1872 0.1972 0.2764 0.0023  0.0025  -0.0073 128 PHE A CZ  
2009 N N   . ARG A 149 ? 0.1623 0.1775 0.2809 0.0050  -0.0154 0.0126  129 ARG A N   
2010 C CA  . ARG A 149 ? 0.1589 0.1961 0.3081 0.0145  0.0008  0.0445  129 ARG A CA  
2011 C C   . ARG A 149 ? 0.1376 0.1903 0.3275 0.0149  0.0066  0.0501  129 ARG A C   
2012 O O   . ARG A 149 ? 0.1425 0.1837 0.3567 0.0105  -0.0054 0.0327  129 ARG A O   
2013 C CB  . ARG A 149 ? 0.1687 0.2317 0.3195 0.0388  0.0114  0.0430  129 ARG A CB  
2014 C CG  . ARG A 149 ? 0.1668 0.2544 0.3279 0.0396  0.0362  0.0703  129 ARG A CG  
2015 C CD  . ARG A 149 ? 0.1821 0.2709 0.3242 0.0221  0.0206  0.0926  129 ARG A CD  
2016 N NE  . ARG A 149 ? 0.2338 0.3039 0.3323 0.0103  0.0089  0.1017  129 ARG A NE  
2017 C CZ  . ARG A 149 ? 0.2925 0.3043 0.3384 0.0142  0.0070  0.0970  129 ARG A CZ  
2018 N NH1 . ARG A 149 ? 0.3423 0.3414 0.3514 0.0223  0.0377  0.0849  129 ARG A NH1 
2019 N NH2 . ARG A 149 ? 0.3251 0.3382 0.3699 0.0163  0.0014  0.1038  129 ARG A NH2 
2033 N N   . PHE A 150 ? 0.1481 0.1790 0.3623 0.0226  0.0099  0.0689  130 PHE A N   
2034 C CA  . PHE A 150 ? 0.1603 0.1708 0.3763 0.0196  -0.0059 0.0442  130 PHE A CA  
2035 C C   . PHE A 150 ? 0.1704 0.2044 0.3900 0.0271  0.0006  0.0674  130 PHE A C   
2036 O O   . PHE A 150 ? 0.1892 0.2537 0.4373 0.0224  -0.0117 0.0971  130 PHE A O   
2037 C CB  . PHE A 150 ? 0.1761 0.1764 0.4013 0.0314  0.0131  0.0246  130 PHE A CB  
2038 C CG  . PHE A 150 ? 0.1820 0.1726 0.3974 0.0110  -0.0188 0.0443  130 PHE A CG  
2039 C CD1 . PHE A 150 ? 0.2167 0.1690 0.4130 0.0213  -0.0411 0.0347  130 PHE A CD1 
2040 C CD2 . PHE A 150 ? 0.1934 0.2102 0.3763 -0.0081 -0.0050 0.0238  130 PHE A CD2 
2041 C CE1 . PHE A 150 ? 0.2281 0.1645 0.4059 0.0059  -0.0387 -0.0128 130 PHE A CE1 
2042 C CE2 . PHE A 150 ? 0.2244 0.2300 0.3657 -0.0052 -0.0093 0.0235  130 PHE A CE2 
2043 C CZ  . PHE A 150 ? 0.2354 0.1932 0.3812 0.0028  -0.0288 -0.0035 130 PHE A CZ  
2053 N N   . GLU A 151 ? 0.1638 0.2156 0.3699 0.0308  -0.0033 0.0654  131 GLU A N   
2054 C CA  . GLU A 151 ? 0.1907 0.2446 0.3764 0.0412  -0.0055 0.0729  131 GLU A CA  
2055 C C   . GLU A 151 ? 0.1753 0.2314 0.3822 0.0429  0.0053  0.0736  131 GLU A C   
2056 O O   . GLU A 151 ? 0.1806 0.2411 0.3697 0.0303  0.0090  0.0618  131 GLU A O   
2057 C CB  . GLU A 151 ? 0.2815 0.3206 0.3976 0.0771  -0.0346 0.0909  131 GLU A CB  
2058 C CG  . GLU A 151 ? 0.3556 0.3852 0.4475 0.0785  -0.0469 0.0777  131 GLU A CG  
2059 C CD  . GLU A 151 ? 0.4413 0.5291 0.5305 0.0555  -0.0489 0.0459  131 GLU A CD  
2060 O OE1 . GLU A 151 ? 0.4733 0.5568 0.5523 0.0414  -0.0013 -0.0098 131 GLU A OE1 
2061 O OE2 . GLU A 151 ? 0.4884 0.6007 0.5717 0.0591  -0.1038 0.0691  131 GLU A OE2 
2068 N N   . ASN A 152 ? 0.2060 0.2291 0.4233 0.0554  0.0190  0.0828  132 ASN A N   
2069 C CA  . ASN A 152 ? 0.2244 0.2302 0.4159 0.0408  0.0211  0.0708  132 ASN A CA  
2070 C C   . ASN A 152 ? 0.2250 0.2180 0.4125 0.0468  0.0256  0.0794  132 ASN A C   
2071 O O   . ASN A 152 ? 0.2096 0.2604 0.4120 0.0601  0.0252  0.0308  132 ASN A O   
2072 C CB  . ASN A 152 ? 0.2307 0.2904 0.4322 0.0586  -0.0082 0.0732  132 ASN A CB  
2073 C CG  . ASN A 152 ? 0.2240 0.3179 0.4424 0.0578  -0.0223 0.0535  132 ASN A CG  
2074 O OD1 . ASN A 152 ? 0.2748 0.2906 0.4521 0.0590  -0.0064 0.0524  132 ASN A OD1 
2075 N ND2 . ASN A 152 ? 0.2085 0.3805 0.4226 0.0620  -0.0081 0.0550  132 ASN A ND2 
2082 N N   . GLY A 153 ? 0.2615 0.2027 0.4070 0.0302  0.0077  0.0685  133 GLY A N   
2083 C CA  . GLY A 153 ? 0.2594 0.2056 0.4112 0.0293  -0.0217 0.0422  133 GLY A CA  
2084 C C   . GLY A 153 ? 0.1869 0.1915 0.3758 0.0126  -0.0155 0.0355  133 GLY A C   
2085 O O   . GLY A 153 ? 0.1895 0.1896 0.3935 0.0192  0.0052  0.0119  133 GLY A O   
2089 N N   . LEU A 154 ? 0.1929 0.1843 0.3401 0.0329  -0.0197 0.0300  134 LEU A N   
2090 C CA  . LEU A 154 ? 0.1721 0.1744 0.3343 0.0257  0.0069  0.0194  134 LEU A CA  
2091 C C   . LEU A 154 ? 0.1621 0.1978 0.3327 0.0181  0.0113  0.0218  134 LEU A C   
2092 O O   . LEU A 154 ? 0.1694 0.2134 0.3123 0.0139  -0.0004 0.0372  134 LEU A O   
2093 C CB  . LEU A 154 ? 0.1579 0.1958 0.3547 0.0148  0.0196  0.0210  134 LEU A CB  
2094 C CG  . LEU A 154 ? 0.1846 0.2034 0.3703 0.0195  0.0095  0.0126  134 LEU A CG  
2095 C CD1 . LEU A 154 ? 0.1900 0.2356 0.4051 0.0024  0.0142  0.0191  134 LEU A CD1 
2096 C CD2 . LEU A 154 ? 0.2238 0.2001 0.4023 0.0294  0.0399  -0.0076 134 LEU A CD2 
2108 N N   . ILE A 155 ? 0.1501 0.1837 0.3315 0.0148  0.0139  0.0192  135 ILE A N   
2109 C CA  . ILE A 155 ? 0.1630 0.1879 0.3222 0.0202  0.0120  0.0219  135 ILE A CA  
2110 C C   . ILE A 155 ? 0.1697 0.1939 0.3217 0.0102  -0.0073 0.0294  135 ILE A C   
2111 O O   . ILE A 155 ? 0.1486 0.2182 0.3193 0.0078  -0.0105 0.0295  135 ILE A O   
2112 C CB  . ILE A 155 ? 0.1521 0.1868 0.3080 0.0248  0.0150  0.0101  135 ILE A CB  
2113 C CG1 . ILE A 155 ? 0.1758 0.1874 0.3242 0.0167  0.0373  0.0090  135 ILE A CG1 
2114 C CG2 . ILE A 155 ? 0.1544 0.1866 0.3102 0.0106  0.0076  0.0271  135 ILE A CG2 
2115 C CD1 . ILE A 155 ? 0.1649 0.1967 0.2998 0.0048  0.0217  0.0135  135 ILE A CD1 
2127 N N   . LYS A 156 ? 0.1710 0.2130 0.3235 0.0247  -0.0010 0.0207  136 LYS A N   
2128 C CA  . LYS A 156 ? 0.1847 0.2191 0.3120 0.0467  -0.0042 0.0631  136 LYS A CA  
2129 C C   . LYS A 156 ? 0.1793 0.2093 0.3016 0.0188  -0.0066 0.0506  136 LYS A C   
2130 O O   . LYS A 156 ? 0.1800 0.2237 0.3165 0.0060  -0.0343 0.0312  136 LYS A O   
2131 C CB  . LYS A 156 ? 0.2512 0.2510 0.3343 0.0576  0.0209  0.0724  136 LYS A CB  
2132 C CG  . LYS A 156 ? 0.2769 0.3522 0.3723 0.0354  0.0331  0.0362  136 LYS A CG  
2133 C CD  . LYS A 156 ? 0.3262 0.4803 0.4005 0.0696  0.0383  -0.0205 136 LYS A CD  
2134 C CE  . LYS A 156 ? 0.3980 0.5776 0.4398 0.0498  0.0433  -0.0435 136 LYS A CE  
2143 N N   . GLU A 157 ? 0.1746 0.1901 0.2793 0.0155  -0.0155 0.0246  137 GLU A N   
2144 C CA  . GLU A 157 ? 0.1806 0.1951 0.2418 -0.0037 -0.0149 0.0098  137 GLU A CA  
2145 C C   . GLU A 157 ? 0.1644 0.1659 0.2617 -0.0013 -0.0237 0.0135  137 GLU A C   
2146 O O   . GLU A 157 ? 0.1736 0.1863 0.2773 -0.0071 -0.0248 0.0233  137 GLU A O   
2147 C CB  . GLU A 157 ? 0.1988 0.2317 0.2465 0.0356  -0.0019 0.0152  137 GLU A CB  
2148 C CG  . GLU A 157 ? 0.2219 0.2566 0.2482 0.0434  -0.0001 -0.0011 137 GLU A CG  
2149 C CD  . GLU A 157 ? 0.2441 0.3184 0.2742 0.0508  0.0110  0.0067  137 GLU A CD  
2150 O OE1 . GLU A 157 ? 0.2244 0.2822 0.2851 0.0264  0.0155  0.0377  137 GLU A OE1 
2151 O OE2 . GLU A 157 ? 0.2902 0.3821 0.2883 0.0200  0.0105  -0.0070 137 GLU A OE2 
2158 N N   . GLN A 158 ? 0.1587 0.1532 0.2605 0.0099  -0.0103 0.0207  138 GLN A N   
2159 C CA  . GLN A 158 ? 0.1517 0.1738 0.2475 0.0194  0.0045  0.0157  138 GLN A CA  
2160 C C   . GLN A 158 ? 0.1371 0.1601 0.2664 -0.0061 -0.0171 0.0231  138 GLN A C   
2161 O O   . GLN A 158 ? 0.1373 0.1838 0.2928 0.0042  -0.0292 -0.0073 138 GLN A O   
2162 C CB  . GLN A 158 ? 0.1599 0.2014 0.2645 0.0124  0.0109  -0.0110 138 GLN A CB  
2163 C CG  . GLN A 158 ? 0.1730 0.1918 0.2901 -0.0033 -0.0027 -0.0222 138 GLN A CG  
2164 C CD  . GLN A 158 ? 0.1827 0.2179 0.3241 0.0119  -0.0032 -0.0046 138 GLN A CD  
2165 O OE1 . GLN A 158 ? 0.2189 0.2195 0.3069 0.0118  -0.0244 0.0076  138 GLN A OE1 
2166 N NE2 . GLN A 158 ? 0.2052 0.2389 0.3725 0.0150  0.0014  0.0163  138 GLN A NE2 
2175 N N   . ARG A 159 ? 0.1363 0.1398 0.2548 0.0017  -0.0229 0.0104  139 ARG A N   
2176 C CA  . ARG A 159 ? 0.1571 0.1501 0.2542 0.0052  -0.0078 0.0017  139 ARG A CA  
2177 C C   . ARG A 159 ? 0.1477 0.1663 0.2691 0.0265  -0.0267 0.0166  139 ARG A C   
2178 O O   . ARG A 159 ? 0.1666 0.1668 0.2795 -0.0073 -0.0430 -0.0033 139 ARG A O   
2179 C CB  . ARG A 159 ? 0.1619 0.1778 0.2452 0.0152  0.0030  -0.0063 139 ARG A CB  
2180 C CG  . ARG A 159 ? 0.1805 0.2008 0.2492 0.0064  -0.0133 0.0097  139 ARG A CG  
2181 C CD  . ARG A 159 ? 0.1912 0.2005 0.2656 0.0011  -0.0007 0.0170  139 ARG A CD  
2182 N NE  . ARG A 159 ? 0.1831 0.1994 0.2671 0.0137  0.0139  0.0055  139 ARG A NE  
2183 C CZ  . ARG A 159 ? 0.1618 0.1998 0.2570 0.0228  0.0186  0.0373  139 ARG A CZ  
2184 N NH1 . ARG A 159 ? 0.1714 0.2170 0.2454 0.0159  0.0114  0.0361  139 ARG A NH1 
2185 N NH2 . ARG A 159 ? 0.1696 0.2059 0.2485 0.0121  0.0268  0.0480  139 ARG A NH2 
2199 N N   B GLU A 160 ? 0.1439 0.1653 0.2803 0.0391  -0.0057 0.0162  140 GLU A N   
2200 N N   D GLU A 160 ? 0.1428 0.1649 0.2790 0.0407  -0.0052 0.0148  140 GLU A N   
2201 C CA  B GLU A 160 ? 0.1680 0.1916 0.2771 0.0655  -0.0086 0.0072  140 GLU A CA  
2202 C CA  D GLU A 160 ? 0.1678 0.1880 0.2771 0.0667  -0.0101 0.0082  140 GLU A CA  
2203 C C   B GLU A 160 ? 0.1674 0.1377 0.2211 0.0198  -0.0229 0.0098  140 GLU A C   
2204 C C   D GLU A 160 ? 0.1679 0.1394 0.2207 0.0222  -0.0226 0.0128  140 GLU A C   
2205 O O   B GLU A 160 ? 0.1716 0.1143 0.1876 -0.0209 -0.0120 0.0165  140 GLU A O   
2206 O O   D GLU A 160 ? 0.1791 0.1156 0.1803 -0.0069 -0.0184 0.0220  140 GLU A O   
2207 C CB  B GLU A 160 ? 0.2157 0.2552 0.3218 0.1026  0.0066  -0.0235 140 GLU A CB  
2208 C CB  D GLU A 160 ? 0.2259 0.2536 0.3227 0.1103  0.0130  -0.0218 140 GLU A CB  
2209 C CG  B GLU A 160 ? 0.2519 0.2787 0.3525 0.1141  0.0083  -0.0736 140 GLU A CG  
2210 C CG  D GLU A 160 ? 0.2617 0.2958 0.3556 0.0934  0.0053  -0.0716 140 GLU A CG  
2211 C CD  B GLU A 160 ? 0.2739 0.3610 0.3946 0.0386  -0.0199 -0.0756 140 GLU A CD  
2212 C CD  D GLU A 160 ? 0.2718 0.3634 0.3944 0.0385  -0.0114 -0.0721 140 GLU A CD  
2213 O OE1 B GLU A 160 ? 0.1989 0.3929 0.3956 0.0136  0.0433  -0.0943 140 GLU A OE1 
2214 O OE1 D GLU A 160 ? 0.2195 0.3876 0.3970 0.0083  0.0352  -0.0873 140 GLU A OE1 
2215 O OE2 B GLU A 160 ? 0.3140 0.3569 0.4250 0.0068  -0.0942 -0.0119 140 GLU A OE2 
2216 O OE2 D GLU A 160 ? 0.3113 0.3556 0.4279 0.0110  -0.0828 -0.0146 140 GLU A OE2 
2229 N N   . PHE A 161 ? 0.1579 0.1595 0.2232 0.0270  -0.0116 -0.0070 141 PHE A N   
2230 C CA  . PHE A 161 ? 0.1526 0.1613 0.1907 0.0110  -0.0065 -0.0031 141 PHE A CA  
2231 C C   . PHE A 161 ? 0.1902 0.1624 0.1845 0.0110  -0.0198 -0.0166 141 PHE A C   
2232 O O   . PHE A 161 ? 0.2122 0.1796 0.2030 0.0184  -0.0231 -0.0296 141 PHE A O   
2233 C CB  . PHE A 161 ? 0.1527 0.1724 0.2331 0.0071  0.0012  -0.0135 141 PHE A CB  
2234 C CG  . PHE A 161 ? 0.1499 0.1644 0.2395 0.0057  0.0016  0.0090  141 PHE A CG  
2235 C CD1 . PHE A 161 ? 0.1710 0.1904 0.2314 -0.0065 -0.0089 0.0198  141 PHE A CD1 
2236 C CD2 . PHE A 161 ? 0.1620 0.1959 0.2405 0.0041  0.0062  0.0287  141 PHE A CD2 
2237 C CE1 . PHE A 161 ? 0.1697 0.2089 0.2649 -0.0052 -0.0105 0.0552  141 PHE A CE1 
2238 C CE2 . PHE A 161 ? 0.2008 0.2062 0.2587 -0.0165 0.0167  0.0264  141 PHE A CE2 
2239 C CZ  . PHE A 161 ? 0.1749 0.2043 0.2670 -0.0184 0.0113  0.0589  141 PHE A CZ  
2250 N N   . MET A 162 ? 0.1839 0.1634 0.1998 0.0168  -0.0126 -0.0251 142 MET A N   
2251 C CA  . MET A 162 ? 0.1864 0.1798 0.1893 -0.0027 -0.0061 -0.0232 142 MET A CA  
2252 C C   . MET A 162 ? 0.1918 0.1808 0.1788 0.0244  0.0093  -0.0106 142 MET A C   
2253 O O   . MET A 162 ? 0.2321 0.1860 0.1850 0.0410  0.0057  -0.0146 142 MET A O   
2254 C CB  . MET A 162 ? 0.1869 0.1878 0.1862 0.0039  0.0087  -0.0119 142 MET A CB  
2255 C CG  . MET A 162 ? 0.1754 0.1973 0.2299 -0.0087 0.0350  -0.0008 142 MET A CG  
2256 S SD  . MET A 162 ? 0.2018 0.2144 0.3149 0.0077  -0.0012 -0.0537 142 MET A SD  
2257 C CE  . MET A 162 ? 0.2209 0.2080 0.2433 -0.0123 -0.0049 -0.0279 142 MET A CE  
2267 N N   . ASN A 163 ? 0.1882 0.1793 0.1840 0.0149  -0.0107 -0.0065 143 ASN A N   
2268 C CA  . ASN A 163 ? 0.1884 0.1566 0.1727 0.0084  -0.0096 -0.0002 143 ASN A CA  
2269 C C   . ASN A 163 ? 0.1866 0.1700 0.1783 0.0118  0.0055  -0.0023 143 ASN A C   
2270 O O   . ASN A 163 ? 0.1915 0.1773 0.1723 0.0129  0.0154  -0.0018 143 ASN A O   
2271 C CB  . ASN A 163 ? 0.1889 0.1601 0.2055 0.0142  -0.0101 -0.0183 143 ASN A CB  
2272 C CG  . ASN A 163 ? 0.1867 0.1745 0.2300 -0.0062 -0.0070 -0.0219 143 ASN A CG  
2273 O OD1 . ASN A 163 ? 0.1847 0.1768 0.1915 0.0039  0.0166  -0.0059 143 ASN A OD1 
2274 N ND2 . ASN A 163 ? 0.2079 0.2492 0.2924 0.0434  -0.0503 -0.0326 143 ASN A ND2 
2281 N N   . PRO A 164 ? 0.1938 0.1496 0.1643 0.0021  0.0151  0.0113  144 PRO A N   
2282 C CA  . PRO A 164 ? 0.1870 0.1792 0.1707 -0.0061 -0.0004 0.0084  144 PRO A CA  
2283 C C   . PRO A 164 ? 0.1841 0.1578 0.1872 0.0058  0.0159  0.0132  144 PRO A C   
2284 O O   . PRO A 164 ? 0.1942 0.1726 0.2054 -0.0149 0.0113  0.0090  144 PRO A O   
2285 C CB  . PRO A 164 ? 0.2213 0.1841 0.1790 -0.0161 -0.0038 -0.0093 144 PRO A CB  
2286 C CG  . PRO A 164 ? 0.2214 0.2003 0.1763 -0.0012 0.0026  -0.0184 144 PRO A CG  
2287 C CD  . PRO A 164 ? 0.1930 0.1788 0.1443 0.0035  0.0134  -0.0047 144 PRO A CD  
2295 N N   . CYS A 165 ? 0.1787 0.1642 0.1949 0.0122  0.0043  0.0179  145 CYS A N   
2296 C CA  . CYS A 165 ? 0.1712 0.1741 0.2056 0.0062  -0.0058 0.0186  145 CYS A CA  
2297 C C   . CYS A 165 ? 0.2038 0.1965 0.1967 -0.0048 0.0064  0.0192  145 CYS A C   
2298 O O   . CYS A 165 ? 0.2106 0.2036 0.2086 -0.0143 0.0033  0.0442  145 CYS A O   
2299 C CB  . CYS A 165 ? 0.1918 0.2029 0.2314 0.0204  0.0047  0.0234  145 CYS A CB  
2300 S SG  . CYS A 165 ? 0.2152 0.2179 0.2744 0.0256  0.0398  0.0179  145 CYS A SG  
2306 N N   . GLU A 166 ? 0.2009 0.1981 0.1904 -0.0148 0.0091  0.0188  146 GLU A N   
2307 C CA  . GLU A 166 ? 0.2022 0.2154 0.1990 -0.0346 -0.0124 0.0214  146 GLU A CA  
2308 C C   . GLU A 166 ? 0.2141 0.2148 0.2021 -0.0315 0.0001  0.0189  146 GLU A C   
2309 O O   . GLU A 166 ? 0.2269 0.2498 0.2156 -0.0432 -0.0053 0.0312  146 GLU A O   
2310 C CB  . GLU A 166 ? 0.2210 0.2306 0.2670 -0.0371 -0.0193 0.0136  146 GLU A CB  
2311 C CG  . GLU A 166 ? 0.2660 0.3289 0.2968 -0.0579 -0.0184 -0.0235 146 GLU A CG  
2312 C CD  . GLU A 166 ? 0.3230 0.5279 0.3860 0.0094  -0.0500 -0.0117 146 GLU A CD  
2313 O OE1 . GLU A 166 ? 0.3633 0.5273 0.3606 0.0289  -0.0543 0.0170  146 GLU A OE1 
2314 O OE2 . GLU A 166 ? 0.3798 0.6889 0.4865 0.0652  -0.0214 -0.0356 146 GLU A OE2 
2321 N N   . GLN A 167 ? 0.1843 0.1927 0.1895 -0.0161 -0.0002 0.0147  147 GLN A N   
2322 C CA  . GLN A 167 ? 0.1969 0.2019 0.1703 -0.0141 0.0170  0.0091  147 GLN A CA  
2323 C C   . GLN A 167 ? 0.1831 0.1868 0.2057 -0.0133 0.0188  0.0157  147 GLN A C   
2324 O O   . GLN A 167 ? 0.1861 0.1973 0.2194 -0.0207 0.0332  0.0147  147 GLN A O   
2325 C CB  . GLN A 167 ? 0.1987 0.2054 0.1711 -0.0196 0.0137  0.0269  147 GLN A CB  
2326 C CG  . GLN A 167 ? 0.2198 0.2066 0.1982 -0.0135 -0.0039 0.0283  147 GLN A CG  
2327 C CD  . GLN A 167 ? 0.2214 0.1934 0.2122 -0.0162 0.0147  0.0288  147 GLN A CD  
2328 O OE1 . GLN A 167 ? 0.2384 0.2135 0.2603 -0.0094 0.0108  0.0133  147 GLN A OE1 
2329 N NE2 . GLN A 167 ? 0.2261 0.2618 0.2485 -0.0224 0.0009  0.0184  147 GLN A NE2 
2338 N N   . PHE A 168 ? 0.1946 0.1833 0.1987 -0.0196 0.0184  0.0106  148 PHE A N   
2339 C CA  . PHE A 168 ? 0.1911 0.1936 0.2480 -0.0077 0.0302  0.0116  148 PHE A CA  
2340 C C   . PHE A 168 ? 0.1633 0.1981 0.2616 -0.0351 0.0228  0.0287  148 PHE A C   
2341 O O   . PHE A 168 ? 0.1857 0.2164 0.2703 -0.0235 0.0306  0.0489  148 PHE A O   
2342 C CB  . PHE A 168 ? 0.2084 0.1930 0.2610 0.0067  0.0274  -0.0145 148 PHE A CB  
2343 C CG  . PHE A 168 ? 0.2207 0.2597 0.2526 -0.0480 0.0283  -0.0230 148 PHE A CG  
2344 C CD1 . PHE A 168 ? 0.2264 0.3375 0.2401 -0.0771 0.0246  -0.0053 148 PHE A CD1 
2345 C CD2 . PHE A 168 ? 0.2204 0.2596 0.2282 -0.0382 0.0277  -0.0092 148 PHE A CD2 
2346 C CE1 . PHE A 168 ? 0.2226 0.4348 0.2643 -0.0632 0.0267  -0.0091 148 PHE A CE1 
2347 C CE2 . PHE A 168 ? 0.2084 0.3482 0.2364 -0.0648 0.0158  -0.0126 148 PHE A CE2 
2348 C CZ  . PHE A 168 ? 0.2131 0.4418 0.2484 -0.0638 0.0032  -0.0046 148 PHE A CZ  
2358 N N   . ARG A 169 ? 0.1970 0.1979 0.2745 -0.0225 0.0109  0.0619  149 ARG A N   
2359 C CA  . ARG A 169 ? 0.2277 0.2242 0.2722 -0.0162 0.0057  0.0737  149 ARG A CA  
2360 C C   . ARG A 169 ? 0.2343 0.2362 0.2375 -0.0238 0.0086  0.0629  149 ARG A C   
2361 O O   . ARG A 169 ? 0.2589 0.2742 0.2411 -0.0373 0.0078  0.0953  149 ARG A O   
2362 C CB  . ARG A 169 ? 0.2624 0.3043 0.2870 -0.0458 -0.0066 0.0794  149 ARG A CB  
2363 C CG  . ARG A 169 ? 0.2785 0.3592 0.2989 -0.0413 -0.0402 0.0883  149 ARG A CG  
2364 C CD  . ARG A 169 ? 0.2875 0.4695 0.3347 -0.0125 -0.0655 0.0682  149 ARG A CD  
2365 N NE  . ARG A 169 ? 0.3221 0.5343 0.3974 -0.0138 -0.0302 0.0794  149 ARG A NE  
2366 C CZ  . ARG A 169 ? 0.3158 0.5909 0.4324 -0.0359 -0.0170 0.0926  149 ARG A CZ  
2367 N NH1 . ARG A 169 ? 0.2894 0.6814 0.4129 -0.0419 -0.0669 0.0793  149 ARG A NH1 
2368 N NH2 . ARG A 169 ? 0.3474 0.5564 0.4637 -0.0258 0.0110  0.1255  149 ARG A NH2 
2382 N N   . SER A 170 ? 0.2272 0.2406 0.2293 -0.0273 0.0056  0.0452  150 SER A N   
2383 C CA  . SER A 170 ? 0.2361 0.2443 0.2254 -0.0329 0.0092  0.0283  150 SER A CA  
2384 C C   . SER A 170 ? 0.2449 0.2389 0.2344 -0.0166 0.0255  0.0252  150 SER A C   
2385 O O   . SER A 170 ? 0.2552 0.2669 0.2587 -0.0230 0.0566  0.0120  150 SER A O   
2386 C CB  . SER A 170 ? 0.2676 0.2493 0.2124 -0.0295 0.0092  -0.0108 150 SER A CB  
2387 O OG  . SER A 170 ? 0.2448 0.2325 0.2324 -0.0268 0.0275  -0.0031 150 SER A OG  
2393 N N   . LEU A 171 ? 0.2189 0.2025 0.2416 -0.0235 0.0275  0.0295  151 LEU A N   
2394 C CA  . LEU A 171 ? 0.2263 0.2117 0.2494 -0.0294 0.0331  0.0460  151 LEU A CA  
2395 C C   . LEU A 171 ? 0.2397 0.2263 0.2841 -0.0293 0.0160  0.0506  151 LEU A C   
2396 O O   . LEU A 171 ? 0.2396 0.2449 0.3296 -0.0242 0.0334  0.0460  151 LEU A O   
2397 C CB  . LEU A 171 ? 0.2110 0.2217 0.2719 -0.0248 0.0316  0.0378  151 LEU A CB  
2398 C CG  . LEU A 171 ? 0.1918 0.2174 0.2754 -0.0121 0.0090  0.0216  151 LEU A CG  
2399 C CD1 . LEU A 171 ? 0.2425 0.2735 0.2661 0.0352  -0.0056 0.0356  151 LEU A CD1 
2400 C CD2 . LEU A 171 ? 0.1958 0.2232 0.3393 -0.0319 0.0036  0.0074  151 LEU A CD2 
2412 N N   . GLY A 172 ? 0.2239 0.2127 0.2918 -0.0358 0.0143  0.0753  152 GLY A N   
2413 C CA  . GLY A 172 ? 0.2529 0.2368 0.3322 -0.0161 0.0123  0.0910  152 GLY A CA  
2414 C C   . GLY A 172 ? 0.2557 0.2117 0.3656 -0.0052 0.0360  0.0605  152 GLY A C   
2415 O O   . GLY A 172 ? 0.2890 0.2128 0.4527 0.0110  0.0381  0.0660  152 GLY A O   
2419 N N   . ILE A 173 ? 0.2248 0.2058 0.3566 -0.0106 0.0587  0.0566  153 ILE A N   
2420 C CA  . ILE A 173 ? 0.2138 0.2016 0.3725 0.0043  0.0601  0.0431  153 ILE A CA  
2421 C C   . ILE A 173 ? 0.2107 0.2034 0.4001 0.0095  0.0625  0.0529  153 ILE A C   
2422 O O   . ILE A 173 ? 0.2185 0.2233 0.3934 -0.0119 0.0559  0.0432  153 ILE A O   
2423 C CB  . ILE A 173 ? 0.2180 0.2166 0.3527 0.0023  0.0539  0.0149  153 ILE A CB  
2424 C CG1 . ILE A 173 ? 0.2295 0.2081 0.3654 -0.0240 0.0189  -0.0051 153 ILE A CG1 
2425 C CG2 . ILE A 173 ? 0.2344 0.2288 0.3375 0.0013  0.0491  -0.0099 153 ILE A CG2 
2426 C CD1 . ILE A 173 ? 0.2371 0.2111 0.3406 -0.0531 0.0219  -0.0086 153 ILE A CD1 
2438 N N   . GLU A 174 ? 0.2318 0.2276 0.4410 0.0184  0.0706  0.0532  154 GLU A N   
2439 C CA  . GLU A 174 ? 0.2486 0.2480 0.4747 0.0123  0.0554  0.0750  154 GLU A CA  
2440 C C   . GLU A 174 ? 0.2436 0.2574 0.4163 0.0081  0.0468  0.0593  154 GLU A C   
2441 O O   . GLU A 174 ? 0.2546 0.2747 0.4300 -0.0013 0.0476  0.0363  154 GLU A O   
2442 C CB  . GLU A 174 ? 0.2991 0.2988 0.5806 0.0356  0.0698  0.0768  154 GLU A CB  
2443 C CG  . GLU A 174 ? 0.3960 0.3638 0.7156 0.0520  0.0708  0.0775  154 GLU A CG  
2444 C CD  . GLU A 174 ? 0.4887 0.4145 0.8350 0.0566  0.0620  0.0745  154 GLU A CD  
2445 O OE1 . GLU A 174 ? 0.5430 0.3698 0.8909 0.0367  0.0572  0.0624  154 GLU A OE1 
2446 O OE2 . GLU A 174 ? 0.5249 0.4967 0.8669 0.0603  0.0527  0.0604  154 GLU A OE2 
2453 N N   . VAL A 175 ? 0.2198 0.2667 0.3806 0.0187  0.0459  0.0959  155 VAL A N   
2454 C CA  . VAL A 175 ? 0.2326 0.2798 0.3824 0.0079  0.0404  0.1031  155 VAL A CA  
2455 C C   . VAL A 175 ? 0.2343 0.3023 0.3792 -0.0305 0.0328  0.0285  155 VAL A C   
2456 O O   . VAL A 175 ? 0.2287 0.2849 0.3934 0.0244  0.0234  0.0554  155 VAL A O   
2457 C CB  . VAL A 175 ? 0.2359 0.2686 0.4175 0.0418  0.0616  0.1083  155 VAL A CB  
2458 C CG1 . VAL A 175 ? 0.2723 0.2395 0.4330 0.0093  0.0290  0.1226  155 VAL A CG1 
2459 C CG2 . VAL A 175 ? 0.2370 0.2738 0.4974 0.0645  0.1266  0.0755  155 VAL A CG2 
2469 N N   . PRO A 176 ? 0.2475 0.3935 0.4413 -0.0401 0.0157  0.0225  156 PRO A N   
2470 C CA  . PRO A 176 ? 0.2498 0.4245 0.4240 -0.0484 0.0329  0.0027  156 PRO A CA  
2471 C C   . PRO A 176 ? 0.2193 0.3789 0.4074 -0.0102 0.0476  0.0079  156 PRO A C   
2472 O O   . PRO A 176 ? 0.2260 0.3653 0.3678 -0.0154 0.0181  0.0460  156 PRO A O   
2473 C CB  . PRO A 176 ? 0.3049 0.4831 0.4768 -0.0309 0.0491  0.0022  156 PRO A CB  
2474 C CG  . PRO A 176 ? 0.3139 0.4412 0.4926 0.0350  0.0464  0.0212  156 PRO A CG  
2475 C CD  . PRO A 176 ? 0.2748 0.4287 0.5007 -0.0501 0.0458  0.0437  156 PRO A CD  
2483 N N   . GLU A 177 ? 0.2200 0.3968 0.4931 0.0109  0.0839  -0.0169 157 GLU A N   
2484 C CA  . GLU A 177 ? 0.2546 0.4118 0.5428 0.0508  0.0886  -0.0179 157 GLU A CA  
2485 C C   . GLU A 177 ? 0.2505 0.3868 0.5022 0.0726  0.1070  -0.0532 157 GLU A C   
2486 O O   . GLU A 177 ? 0.3149 0.4119 0.5623 0.0252  0.1439  -0.0854 157 GLU A O   
2487 C CB  . GLU A 177 ? 0.3649 0.5113 0.6408 0.0697  0.0475  0.0313  157 GLU A CB  
2488 C CG  . GLU A 177 ? 0.4912 0.6096 0.7365 0.0654  -0.0019 0.0617  157 GLU A CG  
2495 N N   . VAL A 178 ? 0.2261 0.3598 0.4170 0.0979  0.0169  -0.0325 158 VAL A N   
2496 C CA  . VAL A 178 ? 0.2039 0.3177 0.3901 0.0718  -0.0097 -0.0062 158 VAL A CA  
2497 C C   . VAL A 178 ? 0.1789 0.3232 0.4034 0.0666  0.0088  -0.0007 158 VAL A C   
2498 O O   . VAL A 178 ? 0.1862 0.4318 0.3964 0.0734  -0.0023 0.0029  158 VAL A O   
2499 C CB  . VAL A 178 ? 0.2348 0.2922 0.3845 0.0537  -0.0222 -0.0005 158 VAL A CB  
2500 C CG1 . VAL A 178 ? 0.2589 0.2646 0.3889 0.0144  -0.0200 0.0010  158 VAL A CG1 
2501 C CG2 . VAL A 178 ? 0.2648 0.3080 0.4008 0.0966  -0.0312 -0.0277 158 VAL A CG2 
2511 N N   . ARG A 179 ? 0.1844 0.2441 0.4204 0.0754  0.0284  0.0449  159 ARG A N   
2512 C CA  . ARG A 179 ? 0.1849 0.2337 0.4372 0.0638  0.0162  0.0575  159 ARG A CA  
2513 C C   . ARG A 179 ? 0.1898 0.2383 0.3997 0.0611  0.0171  0.0546  159 ARG A C   
2514 O O   . ARG A 179 ? 0.2383 0.2620 0.3757 0.0165  -0.0056 0.0428  159 ARG A O   
2515 C CB  . ARG A 179 ? 0.1922 0.2234 0.5146 0.0555  0.0011  0.0834  159 ARG A CB  
2516 C CG  . ARG A 179 ? 0.2431 0.2295 0.5707 0.0112  -0.0003 0.0430  159 ARG A CG  
2517 C CD  . ARG A 179 ? 0.2968 0.2183 0.5942 0.0246  -0.0095 0.0294  159 ARG A CD  
2518 N NE  . ARG A 179 ? 0.3409 0.2642 0.6123 0.0828  0.0453  0.0007  159 ARG A NE  
2519 C CZ  . ARG A 179 ? 0.3779 0.2733 0.6393 0.0838  0.1178  0.0058  159 ARG A CZ  
2520 N NH1 . ARG A 179 ? 0.3700 0.3315 0.6319 0.0426  0.1182  -0.0105 159 ARG A NH1 
2521 N NH2 . ARG A 179 ? 0.4241 0.2610 0.7002 0.1128  0.1595  0.0147  159 ARG A NH2 
2535 N N   . ARG A 180 ? 0.2019 0.2531 0.3863 0.0529  0.0355  0.0541  160 ARG A N   
2536 C CA  . ARG A 180 ? 0.1970 0.2684 0.3953 0.0613  0.0434  0.0376  160 ARG A CA  
2537 C C   . ARG A 180 ? 0.2114 0.2970 0.3570 0.0817  0.0376  -0.0157 160 ARG A C   
2538 O O   . ARG A 180 ? 0.2211 0.3336 0.3716 0.0693  0.0043  0.0001  160 ARG A O   
2539 C CB  . ARG A 180 ? 0.2091 0.3090 0.4671 0.0771  0.0778  -0.0008 160 ARG A CB  
2540 C CG  . ARG A 180 ? 0.2785 0.3417 0.4996 0.0825  0.0947  0.0042  160 ARG A CG  
2541 C CD  . ARG A 180 ? 0.3600 0.3138 0.4603 0.1003  0.0721  0.0967  160 ARG A CD  
2542 N NE  . ARG A 180 ? 0.4230 0.3024 0.4241 0.1192  0.1067  0.1226  160 ARG A NE  
2543 C CZ  . ARG A 180 ? 0.4644 0.3775 0.4472 0.0600  0.0525  0.0674  160 ARG A CZ  
2544 N NH1 . ARG A 180 ? 0.4971 0.4060 0.4528 0.0052  -0.0245 0.0318  160 ARG A NH1 
2545 N NH2 . ARG A 180 ? 0.4501 0.3996 0.4640 0.0523  0.0687  0.0484  160 ARG A NH2 
2559 N N   . ASP A 181 ? 0.2203 0.2869 0.3428 0.0789  0.0250  -0.0157 161 ASP A N   
2560 C CA  . ASP A 181 ? 0.2504 0.2875 0.3962 0.0950  0.0222  0.0130  161 ASP A CA  
2561 C C   . ASP A 181 ? 0.2391 0.3064 0.3722 0.0751  -0.0042 0.0163  161 ASP A C   
2562 O O   . ASP A 181 ? 0.2414 0.3695 0.3794 0.0999  -0.0208 0.0306  161 ASP A O   
2563 C CB  . ASP A 181 ? 0.3309 0.3059 0.4855 0.1182  0.0416  0.0328  161 ASP A CB  
2564 C CG  . ASP A 181 ? 0.4298 0.3893 0.5431 0.1387  0.0584  0.1025  161 ASP A CG  
2565 O OD1 . ASP A 181 ? 0.4956 0.5067 0.5409 0.1723  0.0665  0.1783  161 ASP A OD1 
2566 O OD2 . ASP A 181 ? 0.4260 0.3679 0.5724 0.0987  0.0802  0.1296  161 ASP A OD2 
2571 N N   . GLY A 182 ? 0.2333 0.2471 0.3341 0.0617  0.0105  -0.0036 162 GLY A N   
2572 C CA  . GLY A 182 ? 0.2303 0.2465 0.3195 0.0344  0.0120  -0.0071 162 GLY A CA  
2573 C C   . GLY A 182 ? 0.2272 0.2425 0.3345 0.0374  0.0235  0.0105  162 GLY A C   
2574 O O   . GLY A 182 ? 0.2408 0.2732 0.3512 0.0471  0.0269  -0.0084 162 GLY A O   
2578 N N   . LEU A 183 ? 0.2777 0.2274 0.3393 0.0496  0.0479  -0.0091 163 LEU A N   
2579 C CA  . LEU A 183 ? 0.3029 0.2502 0.3788 0.0476  0.0577  0.0084  163 LEU A CA  
2580 C C   . LEU A 183 ? 0.3839 0.2926 0.3982 0.0274  0.0440  -0.0049 163 LEU A C   
2581 O O   . LEU A 183 ? 0.4525 0.3269 0.4017 0.0134  0.0578  -0.0382 163 LEU A O   
2582 C CB  . LEU A 183 ? 0.2760 0.2780 0.4428 0.0727  0.0766  0.0374  163 LEU A CB  
2583 C CG  . LEU A 183 ? 0.2558 0.2861 0.4778 0.0495  0.0878  0.0528  163 LEU A CG  
2584 C CD1 . LEU A 183 ? 0.2725 0.2875 0.4950 0.0849  0.1155  0.0807  163 LEU A CD1 
2585 C CD2 . LEU A 183 ? 0.2511 0.3116 0.4649 0.0303  0.0698  0.0166  163 LEU A CD2 
2597 N N   . PRO A 184 ? 0.3826 0.2985 0.4115 0.0215  0.0323  -0.0127 164 PRO A N   
2598 C CA  . PRO A 184 ? 0.4258 0.3648 0.4487 -0.0272 0.0114  -0.0522 164 PRO A CA  
2599 C C   . PRO A 184 ? 0.4783 0.4474 0.5107 -0.0288 -0.0047 -0.0941 164 PRO A C   
2600 O O   . PRO A 184 ? 0.4621 0.4341 0.4676 -0.0315 0.0006  -0.1628 164 PRO A O   
2601 C CB  . PRO A 184 ? 0.4239 0.3731 0.4334 -0.0977 0.0259  -0.0648 164 PRO A CB  
2602 C CG  . PRO A 184 ? 0.3947 0.3796 0.4316 -0.1095 0.0341  -0.0455 164 PRO A CG  
2603 C CD  . PRO A 184 ? 0.3753 0.3294 0.4199 -0.0592 0.0157  -0.0150 164 PRO A CD  
2611 N N   . SER A 185 ? 0.5718 0.5898 0.6130 -0.0182 -0.0084 -0.0671 165 SER A N   
2612 C CA  . SER A 185 ? 0.6584 0.7329 0.7098 -0.0211 0.0104  -0.0497 165 SER A CA  
2613 C C   . SER A 185 ? 0.7017 0.7802 0.7532 -0.0381 0.0221  -0.0467 165 SER A C   
2614 O O   . SER A 185 ? 0.7299 0.8114 0.7739 -0.0491 0.0266  -0.0533 165 SER A O   
2615 C CB  . SER A 185 ? 0.6901 0.8056 0.7530 -0.0339 0.0021  -0.0468 165 SER A CB  
2616 O OG  . SER A 185 ? 0.7113 0.8373 0.7913 -0.0505 -0.0163 -0.0515 165 SER A OG  
2622 N N   . THR B 30  ? 0.7835 0.6109 1.2326 0.0123  0.0116  0.2157  10  THR B N   
2623 C CA  . THR B 30  ? 0.7686 0.5862 1.2190 -0.0054 0.0075  0.2207  10  THR B CA  
2624 C C   . THR B 30  ? 0.7440 0.5349 1.1842 -0.0458 0.0004  0.2296  10  THR B C   
2625 O O   . THR B 30  ? 0.7405 0.4931 1.1750 -0.0616 0.0076  0.2608  10  THR B O   
2626 C CB  . THR B 30  ? 0.7707 0.6231 1.2295 0.0013  0.0012  0.2114  10  THR B CB  
2628 N N   . SER B 31  ? 0.7170 0.5045 1.1489 -0.0737 -0.0195 0.2114  11  SER B N   
2629 C CA  . SER B 31  ? 0.6777 0.4811 1.0952 -0.1016 -0.0353 0.1969  11  SER B CA  
2630 C C   . SER B 31  ? 0.6279 0.4467 1.0296 -0.1246 -0.0650 0.1919  11  SER B C   
2631 O O   . SER B 31  ? 0.5981 0.4116 1.0191 -0.1483 -0.0790 0.1734  11  SER B O   
2632 C CB  . SER B 31  ? 0.6819 0.5017 1.0926 -0.0959 -0.0285 0.1980  11  SER B CB  
2633 O OG  . SER B 31  ? 0.6902 0.5328 1.0966 -0.0742 -0.0297 0.1948  11  SER B OG  
2639 N N   . GLU B 32  ? 0.5958 0.4503 0.9707 -0.1285 -0.1035 0.1831  12  GLU B N   
2640 C CA  . GLU B 32  ? 0.5540 0.4469 0.9361 -0.1386 -0.1353 0.1718  12  GLU B CA  
2641 C C   . GLU B 32  ? 0.4952 0.3997 0.9070 -0.1290 -0.1723 0.1658  12  GLU B C   
2642 O O   . GLU B 32  ? 0.4618 0.3905 0.8843 -0.1614 -0.2059 0.1582  12  GLU B O   
2643 C CB  . GLU B 32  ? 0.5744 0.5100 0.9326 -0.0987 -0.1383 0.1649  12  GLU B CB  
2646 N N   . ASN B 33  ? 0.4724 0.4035 0.9137 -0.0650 -0.1551 0.1489  13  ASN B N   
2647 C CA  . ASN B 33  ? 0.4878 0.4346 0.9369 0.0019  -0.1053 0.1273  13  ASN B CA  
2648 C C   . ASN B 33  ? 0.3984 0.3573 0.8657 0.0161  -0.0903 0.0879  13  ASN B C   
2649 O O   . ASN B 33  ? 0.3214 0.3046 0.8513 0.0546  -0.0481 0.0556  13  ASN B O   
2650 C CB  . ASN B 33  ? 0.5983 0.5341 1.0420 0.0201  -0.0476 0.1184  13  ASN B CB  
2651 C CG  . ASN B 33  ? 0.7084 0.6160 1.1310 0.0245  -0.0004 0.1096  13  ASN B CG  
2652 O OD1 . ASN B 33  ? 0.7576 0.6406 1.1682 0.0256  0.0272  0.1128  13  ASN B OD1 
2653 N ND2 . ASN B 33  ? 0.7316 0.6466 1.1576 0.0238  0.0020  0.1068  13  ASN B ND2 
2660 N N   . ARG B 34  ? 0.3983 0.3176 0.8174 -0.0280 -0.0944 0.0702  14  ARG B N   
2661 C CA  . ARG B 34  ? 0.4000 0.2669 0.7835 -0.0460 -0.0639 0.0681  14  ARG B CA  
2662 C C   . ARG B 34  ? 0.3562 0.2674 0.6879 -0.0648 -0.0817 0.0835  14  ARG B C   
2663 O O   . ARG B 34  ? 0.3422 0.2650 0.6527 -0.0406 -0.0666 0.0636  14  ARG B O   
2664 C CB  . ARG B 34  ? 0.4635 0.2536 0.8550 -0.0395 -0.0217 0.0607  14  ARG B CB  
2665 C CG  . ARG B 34  ? 0.5216 0.2939 0.9297 -0.0281 -0.0020 0.0359  14  ARG B CG  
2666 C CD  . ARG B 34  ? 0.5665 0.3656 0.9950 -0.0472 0.0126  0.0253  14  ARG B CD  
2667 N NE  . ARG B 34  ? 0.6119 0.4444 1.0649 -0.0256 0.0264  0.0190  14  ARG B NE  
2668 C CZ  . ARG B 34  ? 0.6438 0.4938 1.1279 -0.0102 0.0347  0.0228  14  ARG B CZ  
2669 N NH1 . ARG B 34  ? 0.6813 0.5351 1.1394 -0.0074 0.0502  0.0238  14  ARG B NH1 
2670 N NH2 . ARG B 34  ? 0.6200 0.4798 1.1507 0.0111  0.0267  0.0177  14  ARG B NH2 
2684 N N   . ALA B 35  ? 0.3466 0.2679 0.6288 -0.0788 -0.1160 0.1238  15  ALA B N   
2685 C CA  . ALA B 35  ? 0.3450 0.2936 0.5873 -0.0937 -0.1001 0.1292  15  ALA B CA  
2686 C C   . ALA B 35  ? 0.3278 0.2904 0.5169 -0.0773 -0.0848 0.1294  15  ALA B C   
2687 O O   . ALA B 35  ? 0.2957 0.2879 0.5049 -0.0798 -0.0542 0.0919  15  ALA B O   
2688 C CB  . ALA B 35  ? 0.3590 0.3128 0.5923 -0.1126 -0.0948 0.1283  15  ALA B CB  
2704 N N   . VAL B 37  ? 0.2817 0.2412 0.5706 -0.0248 -0.0011 0.0103  17  VAL B N   
2705 C CA  . VAL B 37  ? 0.2953 0.2152 0.6046 0.0034  0.0324  0.0109  17  VAL B CA  
2706 C C   . VAL B 37  ? 0.2908 0.2331 0.5831 0.0048  0.0519  0.0025  17  VAL B C   
2707 O O   . VAL B 37  ? 0.3132 0.2255 0.5777 0.0266  0.1127  0.0118  17  VAL B O   
2708 C CB  . VAL B 37  ? 0.3403 0.2841 0.6456 0.0152  0.0316  0.0076  17  VAL B CB  
2709 C CG1 . VAL B 37  ? 0.4056 0.3096 0.6555 -0.0016 0.0423  0.0131  17  VAL B CG1 
2710 C CG2 . VAL B 37  ? 0.3163 0.2952 0.6722 0.0178  0.0235  0.0237  17  VAL B CG2 
2720 N N   . ALA B 38  ? 0.2669 0.2025 0.5572 -0.0159 0.0020  0.0115  18  ALA B N   
2721 C CA  . ALA B 38  ? 0.2828 0.2256 0.5388 -0.0223 -0.0071 -0.0053 18  ALA B CA  
2722 C C   . ALA B 38  ? 0.2637 0.2360 0.4786 -0.0152 0.0230  0.0080  18  ALA B C   
2723 O O   . ALA B 38  ? 0.2455 0.2223 0.4560 -0.0243 0.0310  0.0233  18  ALA B O   
2724 C CB  . ALA B 38  ? 0.2762 0.2307 0.5675 -0.0120 -0.0485 -0.0227 18  ALA B CB  
2730 N N   . ALA B 39  ? 0.2093 0.2250 0.4390 -0.0016 0.0465  0.0241  19  ALA B N   
2731 C CA  . ALA B 39  ? 0.2021 0.2251 0.4302 -0.0059 0.0280  0.0159  19  ALA B CA  
2732 C C   . ALA B 39  ? 0.2099 0.2242 0.4055 -0.0167 0.0538  0.0268  19  ALA B C   
2733 O O   . ALA B 39  ? 0.2294 0.2122 0.3906 -0.0036 0.0435  0.0114  19  ALA B O   
2734 C CB  . ALA B 39  ? 0.2250 0.2791 0.4364 -0.0008 0.0116  0.0012  19  ALA B CB  
2740 N N   . ARG B 40  ? 0.2019 0.1934 0.4262 -0.0206 0.0563  0.0288  20  ARG B N   
2741 C CA  . ARG B 40  ? 0.2049 0.1899 0.4368 -0.0102 0.0400  0.0194  20  ARG B CA  
2742 C C   . ARG B 40  ? 0.2034 0.1941 0.4580 -0.0064 0.0240  -0.0165 20  ARG B C   
2743 O O   . ARG B 40  ? 0.2015 0.1971 0.4498 -0.0056 0.0689  0.0002  20  ARG B O   
2744 C CB  . ARG B 40  ? 0.1977 0.2130 0.4471 -0.0275 0.0410  0.0002  20  ARG B CB  
2745 C CG  . ARG B 40  ? 0.2181 0.2240 0.4572 -0.0218 0.0328  -0.0566 20  ARG B CG  
2746 C CD  . ARG B 40  ? 0.2164 0.1955 0.4615 -0.0174 0.0547  -0.0608 20  ARG B CD  
2747 N NE  . ARG B 40  ? 0.2311 0.1832 0.4506 -0.0186 0.0665  -0.0143 20  ARG B NE  
2748 C CZ  . ARG B 40  ? 0.2288 0.1925 0.4596 -0.0359 0.0421  -0.0425 20  ARG B CZ  
2749 N NH1 . ARG B 40  ? 0.2622 0.1870 0.4903 -0.0488 0.0466  -0.0200 20  ARG B NH1 
2750 N NH2 . ARG B 40  ? 0.2354 0.1975 0.4751 -0.0523 0.0400  -0.0289 20  ARG B NH2 
2764 N N   . GLN B 41  ? 0.2192 0.2172 0.4945 0.0020  0.0434  -0.0578 21  GLN B N   
2765 C CA  . GLN B 41  ? 0.2655 0.2269 0.5291 0.0225  0.0584  -0.0971 21  GLN B CA  
2766 C C   . GLN B 41  ? 0.2622 0.2328 0.4863 0.0035  0.0633  -0.0902 21  GLN B C   
2767 O O   . GLN B 41  ? 0.2353 0.2525 0.4581 -0.0114 0.0467  -0.0746 21  GLN B O   
2768 C CB  . GLN B 41  ? 0.3516 0.2366 0.6128 0.0468  0.1014  -0.1219 21  GLN B CB  
2769 C CG  . GLN B 41  ? 0.4489 0.3096 0.7224 0.0437  0.1302  -0.1688 21  GLN B CG  
2770 C CD  . GLN B 41  ? 0.5642 0.3834 0.8229 0.0466  0.1694  -0.1675 21  GLN B CD  
2771 O OE1 . GLN B 41  ? 0.6042 0.4119 0.8775 -0.0047 0.1421  -0.1641 21  GLN B OE1 
2772 N NE2 . GLN B 41  ? 0.6293 0.4687 0.8555 0.0340  0.1758  -0.1581 21  GLN B NE2 
2781 N N   . HIS B 42  ? 0.2466 0.1925 0.4404 -0.0090 0.0497  -0.0572 22  HIS B N   
2782 C CA  . HIS B 42  ? 0.2234 0.1847 0.4106 -0.0192 0.0497  -0.0556 22  HIS B CA  
2783 C C   . HIS B 42  ? 0.2163 0.2021 0.3605 -0.0262 0.0350  -0.0567 22  HIS B C   
2784 O O   . HIS B 42  ? 0.2133 0.2180 0.3312 -0.0515 0.0207  -0.0561 22  HIS B O   
2785 C CB  . HIS B 42  ? 0.2205 0.1814 0.4481 -0.0293 0.0685  -0.0325 22  HIS B CB  
2786 C CG  . HIS B 42  ? 0.1920 0.1948 0.4195 -0.0451 0.0524  -0.0512 22  HIS B CG  
2787 N ND1 . HIS B 42  ? 0.1893 0.2377 0.4261 -0.0389 0.0748  -0.0661 22  HIS B ND1 
2788 C CD2 . HIS B 42  ? 0.1930 0.1926 0.3936 -0.0326 0.0398  -0.0444 22  HIS B CD2 
2789 C CE1 . HIS B 42  ? 0.1901 0.2385 0.4196 -0.0360 0.0793  -0.0638 22  HIS B CE1 
2790 N NE2 . HIS B 42  ? 0.1762 0.2158 0.3987 -0.0252 0.0520  -0.0327 22  HIS B NE2 
2798 N N   . ASN B 43  ? 0.2004 0.1677 0.3560 -0.0188 0.0329  -0.0454 23  ASN B N   
2799 C CA  . ASN B 43  ? 0.1855 0.1601 0.3692 -0.0163 0.0258  -0.0351 23  ASN B CA  
2800 C C   . ASN B 43  ? 0.1806 0.1709 0.3362 -0.0214 0.0350  -0.0566 23  ASN B C   
2801 O O   . ASN B 43  ? 0.1976 0.1769 0.3055 -0.0009 0.0322  -0.0334 23  ASN B O   
2802 C CB  . ASN B 43  ? 0.1601 0.1878 0.3766 -0.0270 0.0459  -0.0138 23  ASN B CB  
2803 C CG  . ASN B 43  ? 0.1712 0.1670 0.3715 -0.0283 0.0300  -0.0088 23  ASN B CG  
2804 O OD1 . ASN B 43  ? 0.1915 0.2136 0.3573 -0.0134 0.0417  -0.0031 23  ASN B OD1 
2805 N ND2 . ASN B 43  ? 0.1947 0.1979 0.3721 -0.0222 0.0048  0.0204  23  ASN B ND2 
2812 N N   . ARG B 44  ? 0.1794 0.1971 0.3381 -0.0012 0.0454  -0.0645 24  ARG B N   
2813 C CA  . ARG B 44  ? 0.1829 0.1991 0.3322 -0.0028 0.0594  -0.0694 24  ARG B CA  
2814 C C   . ARG B 44  ? 0.1996 0.2096 0.3461 -0.0119 0.0424  -0.0943 24  ARG B C   
2815 O O   . ARG B 44  ? 0.1980 0.2067 0.3226 -0.0122 0.0514  -0.0608 24  ARG B O   
2816 C CB  . ARG B 44  ? 0.2173 0.2274 0.3342 -0.0032 0.0586  -0.0437 24  ARG B CB  
2817 C CG  . ARG B 44  ? 0.3133 0.3135 0.3904 0.0785  0.1012  -0.0404 24  ARG B CG  
2818 C CD  . ARG B 44  ? 0.4319 0.3887 0.4849 0.1007  0.0985  -0.0786 24  ARG B CD  
2819 N NE  . ARG B 44  ? 0.5413 0.4565 0.5745 0.1105  0.0986  -0.1398 24  ARG B NE  
2820 C CZ  . ARG B 44  ? 0.6020 0.5465 0.6631 0.1010  0.1063  -0.1143 24  ARG B CZ  
2821 N NH1 . ARG B 44  ? 0.6423 0.5839 0.7119 0.0979  0.0967  -0.0980 24  ARG B NH1 
2822 N NH2 . ARG B 44  ? 0.6147 0.6024 0.6876 0.1074  0.1399  -0.0980 24  ARG B NH2 
2836 N N   . LYS B 45  ? 0.2104 0.2268 0.3676 -0.0085 0.0175  -0.0813 25  LYS B N   
2837 C CA  . LYS B 45  ? 0.2452 0.2308 0.3623 -0.0155 0.0174  -0.0901 25  LYS B CA  
2838 C C   . LYS B 45  ? 0.2167 0.2229 0.3351 -0.0311 0.0081  -0.0768 25  LYS B C   
2839 O O   . LYS B 45  ? 0.2003 0.2276 0.3393 -0.0309 0.0075  -0.0835 25  LYS B O   
2840 C CB  . LYS B 45  ? 0.2857 0.2333 0.3992 -0.0263 0.0263  -0.0844 25  LYS B CB  
2841 C CG  . LYS B 45  ? 0.3288 0.2823 0.4496 -0.0106 0.0022  -0.0430 25  LYS B CG  
2846 N N   . ILE B 46  ? 0.1948 0.1972 0.2994 -0.0104 0.0177  -0.0510 26  ILE B N   
2847 C CA  . ILE B 46  ? 0.1786 0.1837 0.3044 -0.0010 0.0209  -0.0259 26  ILE B CA  
2848 C C   . ILE B 46  ? 0.1706 0.2069 0.2887 -0.0219 0.0387  -0.0404 26  ILE B C   
2849 O O   . ILE B 46  ? 0.1747 0.2008 0.2976 -0.0197 0.0288  -0.0486 26  ILE B O   
2850 C CB  . ILE B 46  ? 0.1879 0.1754 0.3421 -0.0292 0.0441  -0.0336 26  ILE B CB  
2851 C CG1 . ILE B 46  ? 0.1984 0.2104 0.3967 -0.0354 0.0373  -0.0244 26  ILE B CG1 
2852 C CG2 . ILE B 46  ? 0.1872 0.1972 0.3379 -0.0168 0.0379  -0.0241 26  ILE B CG2 
2853 C CD1 . ILE B 46  ? 0.2128 0.2516 0.4498 -0.0505 0.0310  0.0073  26  ILE B CD1 
2865 N N   . VAL B 47  ? 0.1771 0.1759 0.2753 -0.0163 0.0405  -0.0350 27  VAL B N   
2866 C CA  . VAL B 47  ? 0.1703 0.1995 0.2643 -0.0123 0.0307  -0.0443 27  VAL B CA  
2867 C C   . VAL B 47  ? 0.1601 0.1960 0.2466 -0.0269 0.0202  -0.0596 27  VAL B C   
2868 O O   . VAL B 47  ? 0.1574 0.2087 0.2474 -0.0212 0.0173  -0.0343 27  VAL B O   
2869 C CB  . VAL B 47  ? 0.1614 0.1994 0.2637 -0.0173 0.0008  -0.0449 27  VAL B CB  
2870 C CG1 . VAL B 47  ? 0.1489 0.2165 0.2931 -0.0122 0.0112  -0.0255 27  VAL B CG1 
2871 C CG2 . VAL B 47  ? 0.1712 0.2115 0.2704 -0.0117 0.0017  -0.0476 27  VAL B CG2 
2881 N N   . GLU B 48  ? 0.1719 0.2095 0.2715 -0.0051 0.0080  -0.0676 28  GLU B N   
2882 C CA  . GLU B 48  ? 0.1903 0.2542 0.2521 -0.0119 0.0084  -0.0726 28  GLU B CA  
2883 C C   . GLU B 48  ? 0.1945 0.2291 0.2540 -0.0332 0.0089  -0.0512 28  GLU B C   
2884 O O   . GLU B 48  ? 0.2323 0.2262 0.2503 -0.0084 0.0000  -0.0517 28  GLU B O   
2885 C CB  . GLU B 48  ? 0.2189 0.2842 0.2941 -0.0082 0.0067  -0.0751 28  GLU B CB  
2886 C CG  . GLU B 48  ? 0.2743 0.3136 0.3851 -0.0194 0.0321  -0.0553 28  GLU B CG  
2887 C CD  . GLU B 48  ? 0.3700 0.4225 0.4876 0.0129  0.0266  -0.0547 28  GLU B CD  
2888 O OE1 . GLU B 48  ? 0.4027 0.4336 0.5081 0.0357  0.0120  -0.0410 28  GLU B OE1 
2889 O OE2 . GLU B 48  ? 0.3958 0.4804 0.5134 0.0258  0.0513  -0.0919 28  GLU B OE2 
2896 N N   A GLN B 49  ? 0.1817 0.2230 0.2491 -0.0374 0.0069  -0.0634 29  GLN B N   
2897 N N   B GLN B 49  ? 0.1939 0.2324 0.2571 -0.0325 0.0008  -0.0592 29  GLN B N   
2898 C CA  A GLN B 49  ? 0.1768 0.2414 0.2871 -0.0177 -0.0077 -0.0754 29  GLN B CA  
2899 C CA  B GLN B 49  ? 0.2006 0.2515 0.2842 -0.0173 -0.0133 -0.0710 29  GLN B CA  
2900 C C   A GLN B 49  ? 0.1770 0.2456 0.2556 -0.0104 0.0042  -0.0632 29  GLN B C   
2901 C C   B GLN B 49  ? 0.1878 0.2503 0.2569 -0.0144 -0.0061 -0.0682 29  GLN B C   
2902 O O   A GLN B 49  ? 0.2169 0.2656 0.2516 0.0107  -0.0103 -0.0543 29  GLN B O   
2903 O O   B GLN B 49  ? 0.2142 0.2731 0.2516 -0.0074 -0.0299 -0.0676 29  GLN B O   
2904 C CB  A GLN B 49  ? 0.1826 0.2442 0.3655 -0.0127 -0.0172 -0.0821 29  GLN B CB  
2905 C CB  B GLN B 49  ? 0.2255 0.2603 0.3418 -0.0199 -0.0260 -0.0736 29  GLN B CB  
2906 C CG  A GLN B 49  ? 0.2062 0.2934 0.4324 -0.0090 -0.0068 -0.0940 29  GLN B CG  
2907 C CG  B GLN B 49  ? 0.2645 0.2986 0.3980 -0.0400 -0.0452 -0.0775 29  GLN B CG  
2908 C CD  A GLN B 49  ? 0.2444 0.3520 0.4842 -0.0523 0.0236  -0.0986 29  GLN B CD  
2909 C CD  B GLN B 49  ? 0.3056 0.3479 0.4737 -0.0877 -0.0360 -0.0966 29  GLN B CD  
2910 O OE1 A GLN B 49  ? 0.2991 0.4155 0.5166 -0.0902 0.0397  -0.1011 29  GLN B OE1 
2911 O OE1 B GLN B 49  ? 0.3511 0.3847 0.5006 -0.1079 -0.0080 -0.1164 29  GLN B OE1 
2912 N NE2 A GLN B 49  ? 0.1978 0.3343 0.4774 -0.0222 0.0025  -0.1075 29  GLN B NE2 
2913 N NE2 B GLN B 49  ? 0.3166 0.3929 0.5161 -0.0890 -0.0321 -0.0468 29  GLN B NE2 
2930 N N   . TYR B 50  ? 0.1609 0.2268 0.2467 -0.0094 0.0125  -0.0667 30  TYR B N   
2931 C CA  . TYR B 50  ? 0.1572 0.2188 0.2291 -0.0064 0.0197  -0.0489 30  TYR B CA  
2932 C C   . TYR B 50  ? 0.1564 0.2321 0.2160 0.0041  -0.0030 -0.0525 30  TYR B C   
2933 O O   . TYR B 50  ? 0.1678 0.2333 0.2078 0.0098  -0.0008 -0.0407 30  TYR B O   
2934 C CB  . TYR B 50  ? 0.1611 0.2243 0.2153 -0.0192 0.0132  -0.0502 30  TYR B CB  
2935 C CG  . TYR B 50  ? 0.1404 0.2184 0.2016 -0.0061 0.0085  -0.0372 30  TYR B CG  
2936 C CD1 . TYR B 50  ? 0.1504 0.2107 0.2001 -0.0239 0.0177  -0.0481 30  TYR B CD1 
2937 C CD2 . TYR B 50  ? 0.1557 0.2300 0.2327 -0.0090 0.0254  -0.0231 30  TYR B CD2 
2938 C CE1 . TYR B 50  ? 0.1874 0.2115 0.2268 -0.0150 0.0275  -0.0601 30  TYR B CE1 
2939 C CE2 . TYR B 50  ? 0.1642 0.2039 0.2575 -0.0030 0.0180  -0.0558 30  TYR B CE2 
2940 C CZ  . TYR B 50  ? 0.1857 0.1994 0.2623 -0.0125 -0.0043 -0.0491 30  TYR B CZ  
2941 O OH  . TYR B 50  ? 0.2099 0.2217 0.3090 -0.0203 0.0001  -0.0640 30  TYR B OH  
2952 N N   . MET B 51  ? 0.1564 0.2140 0.2295 -0.0063 0.0185  -0.0425 31  MET B N   
2953 C CA  . MET B 51  ? 0.1682 0.2320 0.2162 -0.0059 0.0240  -0.0560 31  MET B CA  
2954 C C   . MET B 51  ? 0.1951 0.2339 0.2044 -0.0035 0.0003  -0.0608 31  MET B C   
2955 O O   . MET B 51  ? 0.2166 0.2484 0.2013 -0.0063 -0.0099 -0.0315 31  MET B O   
2956 C CB  . MET B 51  ? 0.1700 0.2366 0.2234 -0.0095 0.0044  -0.0418 31  MET B CB  
2957 C CG  . MET B 51  ? 0.1748 0.2324 0.2271 -0.0145 0.0081  -0.0347 31  MET B CG  
2958 S SD  . MET B 51  ? 0.1726 0.2304 0.2151 -0.0140 0.0172  -0.0310 31  MET B SD  
2959 C CE  . MET B 51  ? 0.2078 0.2446 0.2097 -0.0113 0.0027  -0.0039 31  MET B CE  
2969 N N   . HIS B 52  ? 0.2062 0.2569 0.1933 -0.0188 -0.0005 -0.0779 32  HIS B N   
2970 C CA  . HIS B 52  ? 0.2329 0.2838 0.2010 0.0084  -0.0069 -0.0958 32  HIS B CA  
2971 C C   . HIS B 52  ? 0.2215 0.3040 0.2553 0.0071  -0.0178 -0.1001 32  HIS B C   
2972 O O   . HIS B 52  ? 0.2351 0.3863 0.2819 0.0221  -0.0181 -0.0926 32  HIS B O   
2973 C CB  . HIS B 52  ? 0.2694 0.3349 0.2005 0.0289  -0.0089 -0.0923 32  HIS B CB  
2974 C CG  . HIS B 52  ? 0.2842 0.3558 0.2275 0.0467  0.0199  -0.1042 32  HIS B CG  
2975 N ND1 . HIS B 52  ? 0.2973 0.4186 0.3148 -0.0017 0.0399  -0.0844 32  HIS B ND1 
2976 C CD2 . HIS B 52  ? 0.2947 0.3917 0.2429 0.0040  0.0759  -0.1100 32  HIS B CD2 
2977 C CE1 . HIS B 52  ? 0.2973 0.4482 0.3025 0.0108  0.0766  -0.0927 32  HIS B CE1 
2978 N NE2 . HIS B 52  ? 0.3161 0.4341 0.3008 -0.0187 0.0789  -0.1278 32  HIS B NE2 
2986 N N   . THR B 53  ? 0.1972 0.2932 0.2621 -0.0227 -0.0230 -0.0676 33  THR B N   
2987 C CA  . THR B 53  ? 0.2007 0.2942 0.2686 0.0110  -0.0063 -0.0386 33  THR B CA  
2988 C C   . THR B 53  ? 0.2063 0.3181 0.2642 0.0070  -0.0065 -0.0271 33  THR B C   
2989 O O   . THR B 53  ? 0.2245 0.3006 0.2777 0.0149  -0.0177 -0.0129 33  THR B O   
2990 C CB  . THR B 53  ? 0.2079 0.2787 0.2966 0.0150  0.0223  -0.0204 33  THR B CB  
2991 O OG1 . THR B 53  ? 0.2040 0.2875 0.3106 0.0129  0.0056  -0.0307 33  THR B OG1 
2992 C CG2 . THR B 53  ? 0.2200 0.2562 0.3239 0.0214  0.0241  -0.0104 33  THR B CG2 
3000 N N   . ARG B 54  ? 0.2200 0.3340 0.2439 0.0065  0.0087  -0.0068 34  ARG B N   
3001 C CA  . ARG B 54  ? 0.2411 0.3613 0.2330 0.0205  0.0021  -0.0012 34  ARG B CA  
3002 C C   . ARG B 54  ? 0.2270 0.3638 0.2875 0.0298  -0.0198 -0.0189 34  ARG B C   
3003 O O   . ARG B 54  ? 0.2319 0.3610 0.3313 0.0136  -0.0104 -0.0142 34  ARG B O   
3004 C CB  . ARG B 54  ? 0.2518 0.3789 0.2041 0.0038  0.0011  -0.0088 34  ARG B CB  
3005 C CG  . ARG B 54  ? 0.2590 0.3869 0.1721 -0.0135 0.0007  -0.0532 34  ARG B CG  
3006 C CD  . ARG B 54  ? 0.2806 0.3474 0.1861 -0.0017 -0.0010 -0.0386 34  ARG B CD  
3007 N NE  . ARG B 54  ? 0.2848 0.3294 0.2198 0.0099  0.0172  -0.0523 34  ARG B NE  
3008 C CZ  . ARG B 54  ? 0.2823 0.3583 0.2249 -0.0146 0.0222  -0.0592 34  ARG B CZ  
3009 N NH1 . ARG B 54  ? 0.2823 0.3794 0.2157 -0.0649 0.0294  -0.0673 34  ARG B NH1 
3010 N NH2 . ARG B 54  ? 0.2716 0.3573 0.2225 -0.0033 0.0312  -0.0689 34  ARG B NH2 
3024 N N   . GLY B 55  ? 0.2372 0.3781 0.2994 0.0352  -0.0369 -0.0023 35  GLY B N   
3025 C CA  . GLY B 55  ? 0.2288 0.3952 0.3226 0.0344  -0.0569 0.0035  35  GLY B CA  
3026 C C   . GLY B 55  ? 0.2259 0.4039 0.3220 0.0397  -0.0794 0.0085  35  GLY B C   
3027 O O   . GLY B 55  ? 0.2206 0.3893 0.2934 0.0324  -0.0523 0.0155  35  GLY B O   
3031 N N   . GLU B 56  ? 0.2335 0.4620 0.3704 0.0541  -0.0758 0.0140  36  GLU B N   
3032 C CA  . GLU B 56  ? 0.2263 0.4964 0.4307 0.0735  -0.0862 -0.0013 36  GLU B CA  
3033 C C   . GLU B 56  ? 0.1975 0.4262 0.4122 0.0274  -0.0743 -0.0180 36  GLU B C   
3034 O O   . GLU B 56  ? 0.1969 0.3813 0.4122 0.0121  -0.0503 -0.0258 36  GLU B O   
3035 C CB  . GLU B 56  ? 0.2998 0.6010 0.5005 0.0610  -0.0994 0.0344  36  GLU B CB  
3036 C CG  . GLU B 56  ? 0.4133 0.7151 0.5855 0.0567  -0.1010 0.0419  36  GLU B CG  
3037 C CD  . GLU B 56  ? 0.5180 0.8139 0.6828 0.0374  -0.1001 0.0246  36  GLU B CD  
3038 O OE1 . GLU B 56  ? 0.5424 0.8569 0.7136 0.0426  -0.1334 0.0176  36  GLU B OE1 
3039 O OE2 . GLU B 56  ? 0.5647 0.8429 0.7110 0.0289  -0.0964 0.0164  36  GLU B OE2 
3046 N N   . ALA B 57  ? 0.2044 0.3857 0.3816 0.0100  -0.0499 -0.0322 37  ALA B N   
3047 C CA  . ALA B 57  ? 0.2125 0.3705 0.3534 -0.0020 -0.0299 -0.0377 37  ALA B CA  
3048 C C   . ALA B 57  ? 0.1942 0.3200 0.3276 0.0057  0.0014  -0.0452 37  ALA B C   
3049 O O   . ALA B 57  ? 0.2011 0.3172 0.3325 -0.0161 -0.0066 -0.0339 37  ALA B O   
3050 C CB  . ALA B 57  ? 0.2590 0.3944 0.3544 -0.0286 -0.0185 -0.0159 37  ALA B CB  
3056 N N   . ARG B 58  ? 0.1893 0.2655 0.3079 0.0074  0.0148  -0.0114 38  ARG B N   
3057 C CA  . ARG B 58  ? 0.2085 0.2634 0.3063 0.0027  0.0093  -0.0043 38  ARG B CA  
3058 C C   . ARG B 58  ? 0.2080 0.2641 0.2847 0.0101  -0.0163 0.0236  38  ARG B C   
3059 O O   . ARG B 58  ? 0.1996 0.2585 0.2668 0.0031  -0.0038 -0.0005 38  ARG B O   
3060 C CB  . ARG B 58  ? 0.2133 0.2718 0.3337 0.0056  0.0048  0.0017  38  ARG B CB  
3061 C CG  . ARG B 58  ? 0.2244 0.2847 0.3609 -0.0027 0.0171  0.0095  38  ARG B CG  
3062 C CD  . ARG B 58  ? 0.2563 0.2843 0.3788 -0.0219 0.0223  -0.0183 38  ARG B CD  
3063 N NE  . ARG B 58  ? 0.2889 0.2954 0.4115 0.0328  0.0338  0.0188  38  ARG B NE  
3064 C CZ  . ARG B 58  ? 0.2696 0.2679 0.4230 0.0461  0.0479  0.0427  38  ARG B CZ  
3065 N NH1 . ARG B 58  ? 0.2994 0.3355 0.4541 0.0311  0.0309  0.0484  38  ARG B NH1 
3066 N NH2 . ARG B 58  ? 0.2889 0.2658 0.4381 0.0407  -0.0021 0.0458  38  ARG B NH2 
3080 N N   . LEU B 59  ? 0.1935 0.2807 0.3181 0.0286  -0.0121 0.0158  39  LEU B N   
3081 C CA  . LEU B 59  ? 0.1917 0.3061 0.3539 0.0226  0.0032  0.0266  39  LEU B CA  
3082 C C   . LEU B 59  ? 0.1888 0.3171 0.3742 0.0102  0.0204  0.0125  39  LEU B C   
3083 O O   . LEU B 59  ? 0.2013 0.3196 0.3585 0.0231  -0.0013 0.0312  39  LEU B O   
3084 C CB  . LEU B 59  ? 0.1942 0.3308 0.3871 0.0158  -0.0014 0.0755  39  LEU B CB  
3085 C CG  . LEU B 59  ? 0.2453 0.3658 0.4197 0.0260  -0.0178 0.0846  39  LEU B CG  
3086 C CD1 . LEU B 59  ? 0.2551 0.3848 0.4405 0.0672  -0.0309 0.1040  39  LEU B CD1 
3087 C CD2 . LEU B 59  ? 0.2768 0.4034 0.4253 0.0218  -0.0261 0.0919  39  LEU B CD2 
3099 N N   . LYS B 60  ? 0.1858 0.3128 0.4108 -0.0060 0.0093  0.0037  40  LYS B N   
3100 C CA  . LYS B 60  ? 0.2024 0.2883 0.4179 -0.0272 -0.0120 0.0026  40  LYS B CA  
3101 C C   . LYS B 60  ? 0.2103 0.2524 0.3443 -0.0260 -0.0283 -0.0136 40  LYS B C   
3102 O O   . LYS B 60  ? 0.2326 0.2485 0.3766 -0.0538 -0.0372 -0.0135 40  LYS B O   
3103 C CB  . LYS B 60  ? 0.2551 0.3464 0.4729 -0.0259 -0.0499 -0.0012 40  LYS B CB  
3104 C CG  . LYS B 60  ? 0.3420 0.4376 0.5643 -0.0425 -0.0709 -0.0045 40  LYS B CG  
3105 C CD  . LYS B 60  ? 0.4212 0.5657 0.6482 -0.0387 -0.0783 -0.0135 40  LYS B CD  
3106 C CE  . LYS B 60  ? 0.4893 0.6571 0.7116 -0.0279 -0.0554 -0.0023 40  LYS B CE  
3107 N NZ  . LYS B 60  ? 0.5167 0.7084 0.7624 -0.0255 -0.0334 -0.0001 40  LYS B NZ  
3121 N N   . ARG B 61  ? 0.1990 0.2581 0.3253 -0.0020 -0.0194 -0.0219 41  ARG B N   
3122 C CA  . ARG B 61  ? 0.1992 0.2610 0.3166 0.0087  -0.0153 -0.0150 41  ARG B CA  
3123 C C   . ARG B 61  ? 0.1943 0.2088 0.3201 -0.0014 -0.0087 -0.0004 41  ARG B C   
3124 O O   . ARG B 61  ? 0.1943 0.1997 0.3372 -0.0311 0.0175  0.0052  41  ARG B O   
3125 C CB  . ARG B 61  ? 0.2148 0.2803 0.3058 0.0211  -0.0011 -0.0165 41  ARG B CB  
3126 C CG  . ARG B 61  ? 0.1930 0.2831 0.3057 0.0281  0.0064  -0.0193 41  ARG B CG  
3127 C CD  . ARG B 61  ? 0.1981 0.3460 0.2895 -0.0036 0.0313  -0.0125 41  ARG B CD  
3128 N NE  . ARG B 61  ? 0.2553 0.3054 0.3359 0.0068  0.0550  -0.0022 41  ARG B NE  
3129 C CZ  . ARG B 61  ? 0.3579 0.3037 0.3558 -0.0144 0.0879  -0.0358 41  ARG B CZ  
3130 N NH1 . ARG B 61  ? 0.3899 0.2692 0.3929 -0.0314 0.1012  -0.0788 41  ARG B NH1 
3131 N NH2 . ARG B 61  ? 0.4271 0.3502 0.3910 -0.0102 0.0842  -0.0434 41  ARG B NH2 
3145 N N   . HIS B 62  ? 0.1962 0.2152 0.2972 -0.0046 0.0175  -0.0064 42  HIS B N   
3146 C CA  . HIS B 62  ? 0.1849 0.2105 0.3191 -0.0113 0.0405  -0.0249 42  HIS B CA  
3147 C C   . HIS B 62  ? 0.1610 0.2263 0.3470 -0.0179 0.0388  -0.0197 42  HIS B C   
3148 O O   . HIS B 62  ? 0.1581 0.2154 0.3500 -0.0085 0.0365  -0.0244 42  HIS B O   
3149 C CB  . HIS B 62  ? 0.2041 0.2107 0.3378 0.0140  0.0417  -0.0116 42  HIS B CB  
3150 C CG  . HIS B 62  ? 0.2076 0.2348 0.3463 0.0305  0.0332  0.0122  42  HIS B CG  
3151 N ND1 . HIS B 62  ? 0.1889 0.2618 0.3676 0.0206  0.0310  -0.0007 42  HIS B ND1 
3152 C CD2 . HIS B 62  ? 0.2229 0.2820 0.3505 0.0044  0.0347  0.0030  42  HIS B CD2 
3153 C CE1 . HIS B 62  ? 0.2119 0.3002 0.3628 0.0346  0.0149  0.0057  42  HIS B CE1 
3154 N NE2 . HIS B 62  ? 0.2344 0.3022 0.3640 0.0170  0.0261  0.0157  42  HIS B NE2 
3162 N N   . LEU B 63  ? 0.1654 0.1885 0.3677 0.0008  0.0135  0.0005  43  LEU B N   
3163 C CA  . LEU B 63  ? 0.1640 0.1931 0.4045 -0.0290 -0.0088 -0.0061 43  LEU B CA  
3164 C C   . LEU B 63  ? 0.1633 0.1869 0.3919 -0.0045 -0.0042 0.0063  43  LEU B C   
3165 O O   . LEU B 63  ? 0.1724 0.2003 0.4130 0.0084  0.0207  0.0186  43  LEU B O   
3166 C CB  . LEU B 63  ? 0.1588 0.2214 0.4445 0.0022  -0.0093 -0.0015 43  LEU B CB  
3167 C CG  . LEU B 63  ? 0.1570 0.2776 0.5009 -0.0288 -0.0170 0.0228  43  LEU B CG  
3168 C CD1 . LEU B 63  ? 0.1850 0.3328 0.5216 -0.0608 -0.0585 0.0252  43  LEU B CD1 
3169 C CD2 . LEU B 63  ? 0.2010 0.2770 0.5435 0.0222  0.0181  0.0566  43  LEU B CD2 
3181 N N   . LEU B 64  ? 0.1566 0.1734 0.3216 -0.0129 0.0021  -0.0090 44  LEU B N   
3182 C CA  . LEU B 64  ? 0.1730 0.1813 0.3059 -0.0062 0.0109  -0.0174 44  LEU B CA  
3183 C C   . LEU B 64  ? 0.1603 0.1846 0.3176 -0.0267 0.0172  -0.0197 44  LEU B C   
3184 O O   . LEU B 64  ? 0.1666 0.1897 0.3158 -0.0126 0.0208  -0.0117 44  LEU B O   
3185 C CB  . LEU B 64  ? 0.1876 0.2069 0.3085 -0.0046 0.0325  -0.0064 44  LEU B CB  
3186 C CG  . LEU B 64  ? 0.1928 0.2087 0.3270 -0.0114 0.0321  -0.0133 44  LEU B CG  
3187 C CD1 . LEU B 64  ? 0.1881 0.2458 0.3632 -0.0068 0.0325  0.0116  44  LEU B CD1 
3188 C CD2 . LEU B 64  ? 0.2186 0.2212 0.3298 -0.0199 0.0134  -0.0372 44  LEU B CD2 
3200 N N   . PHE B 65  ? 0.1410 0.1955 0.3135 -0.0119 0.0105  -0.0197 45  PHE B N   
3201 C CA  . PHE B 65  ? 0.1647 0.1832 0.3091 -0.0132 0.0413  -0.0011 45  PHE B CA  
3202 C C   . PHE B 65  ? 0.1547 0.1794 0.3351 -0.0172 0.0411  0.0049  45  PHE B C   
3203 O O   . PHE B 65  ? 0.1457 0.2176 0.3449 -0.0299 0.0398  -0.0033 45  PHE B O   
3204 C CB  . PHE B 65  ? 0.1659 0.1779 0.2996 -0.0079 0.0570  0.0166  45  PHE B CB  
3205 C CG  . PHE B 65  ? 0.1598 0.1802 0.2776 -0.0146 0.0489  -0.0055 45  PHE B CG  
3206 C CD1 . PHE B 65  ? 0.1668 0.2390 0.2709 -0.0196 0.0329  -0.0064 45  PHE B CD1 
3207 C CD2 . PHE B 65  ? 0.1450 0.1959 0.2783 -0.0142 0.0361  -0.0276 45  PHE B CD2 
3208 C CE1 . PHE B 65  ? 0.1767 0.2696 0.2778 -0.0305 0.0298  -0.0167 45  PHE B CE1 
3209 C CE2 . PHE B 65  ? 0.1493 0.2406 0.2504 -0.0102 0.0356  -0.0519 45  PHE B CE2 
3210 C CZ  . PHE B 65  ? 0.1636 0.2544 0.2288 -0.0335 0.0378  -0.0478 45  PHE B CZ  
3220 N N   . THR B 66  ? 0.1647 0.1931 0.3290 -0.0227 0.0566  -0.0027 46  THR B N   
3221 C CA  . THR B 66  ? 0.1877 0.2204 0.3369 -0.0445 0.0645  0.0287  46  THR B CA  
3222 C C   . THR B 66  ? 0.1849 0.2137 0.3383 -0.0184 0.0798  0.0046  46  THR B C   
3223 O O   . THR B 66  ? 0.1696 0.2193 0.3382 -0.0186 0.0573  0.0085  46  THR B O   
3224 C CB  . THR B 66  ? 0.2230 0.2208 0.3198 -0.0425 0.0551  0.0212  46  THR B CB  
3225 O OG1 . THR B 66  ? 0.2229 0.2337 0.3191 -0.0368 0.0429  0.0342  46  THR B OG1 
3226 C CG2 . THR B 66  ? 0.2315 0.2380 0.3171 -0.0333 0.0485  0.0137  46  THR B CG2 
3234 N N   . GLU B 67  ? 0.1852 0.2525 0.3652 -0.0245 0.0962  0.0022  47  GLU B N   
3235 C CA  . GLU B 67  ? 0.1996 0.2540 0.3966 -0.0426 0.1215  0.0023  47  GLU B CA  
3236 C C   . GLU B 67  ? 0.2088 0.2468 0.3632 -0.0182 0.1246  -0.0121 47  GLU B C   
3237 O O   . GLU B 67  ? 0.2363 0.2453 0.3940 -0.0106 0.1123  -0.0079 47  GLU B O   
3238 C CB  . GLU B 67  ? 0.2253 0.3028 0.4668 -0.0443 0.1404  -0.0140 47  GLU B CB  
3239 C CG  . GLU B 67  ? 0.2784 0.3624 0.4952 -0.0370 0.1676  -0.0044 47  GLU B CG  
3244 N N   . ASP B 68  ? 0.2119 0.2550 0.3337 -0.0421 0.1204  -0.0156 48  ASP B N   
3245 C CA  . ASP B 68  ? 0.2431 0.2760 0.3302 -0.0604 0.1032  -0.0028 48  ASP B CA  
3246 C C   . ASP B 68  ? 0.2212 0.2532 0.3203 -0.0328 0.0658  -0.0063 48  ASP B C   
3247 O O   . ASP B 68  ? 0.2511 0.2591 0.3126 -0.0445 0.0759  -0.0056 48  ASP B O   
3248 C CB  . ASP B 68  ? 0.3205 0.3776 0.3322 -0.0452 0.1445  0.0426  48  ASP B CB  
3249 C CG  . ASP B 68  ? 0.3919 0.4625 0.3729 -0.0349 0.1059  0.0869  48  ASP B CG  
3250 O OD1 . ASP B 68  ? 0.3634 0.4761 0.3888 0.0082  0.1028  0.0630  48  ASP B OD1 
3251 O OD2 . ASP B 68  ? 0.4671 0.5205 0.4304 -0.0425 0.0511  0.0990  48  ASP B OD2 
3256 N N   . GLY B 69  ? 0.1823 0.2338 0.3087 -0.0345 0.0648  -0.0211 49  GLY B N   
3257 C CA  . GLY B 69  ? 0.1667 0.2161 0.3283 -0.0464 0.0789  -0.0121 49  GLY B CA  
3258 C C   . GLY B 69  ? 0.1719 0.2079 0.3082 -0.0204 0.0839  -0.0344 49  GLY B C   
3259 O O   . GLY B 69  ? 0.1793 0.2187 0.3248 -0.0150 0.0887  0.0045  49  GLY B O   
3263 N N   . VAL B 70  ? 0.1766 0.1728 0.2782 -0.0254 0.0643  -0.0122 50  VAL B N   
3264 C CA  . VAL B 70  ? 0.1898 0.1819 0.2688 -0.0336 0.0610  -0.0025 50  VAL B CA  
3265 C C   . VAL B 70  ? 0.1640 0.1766 0.2610 -0.0215 0.0621  -0.0009 50  VAL B C   
3266 O O   . VAL B 70  ? 0.1617 0.1701 0.2710 -0.0092 0.0557  -0.0131 50  VAL B O   
3267 C CB  . VAL B 70  ? 0.2134 0.2218 0.2647 -0.0422 0.0417  -0.0159 50  VAL B CB  
3268 C CG1 . VAL B 70  ? 0.2457 0.2452 0.2865 -0.0469 -0.0035 -0.0258 50  VAL B CG1 
3269 C CG2 . VAL B 70  ? 0.2389 0.2690 0.2893 -0.0301 0.0552  -0.0095 50  VAL B CG2 
3279 N N   . GLY B 71  ? 0.1458 0.1676 0.2481 -0.0128 0.0448  -0.0036 51  GLY B N   
3280 C CA  . GLY B 71  ? 0.1537 0.1726 0.2340 -0.0114 0.0615  -0.0002 51  GLY B CA  
3281 C C   . GLY B 71  ? 0.1932 0.1845 0.2405 0.0052  0.0738  -0.0178 51  GLY B C   
3282 O O   . GLY B 71  ? 0.2562 0.1848 0.2913 -0.0192 0.1449  -0.0330 51  GLY B O   
3286 N N   . GLY B 72  ? 0.1709 0.1845 0.2520 -0.0137 0.0666  -0.0063 52  GLY B N   
3287 C CA  . GLY B 72  ? 0.1762 0.1749 0.2756 -0.0274 0.0569  0.0098  52  GLY B CA  
3288 C C   . GLY B 72  ? 0.1904 0.1566 0.2499 -0.0088 0.0590  0.0108  52  GLY B C   
3289 O O   . GLY B 72  ? 0.2017 0.1708 0.2574 -0.0025 0.0604  -0.0226 52  GLY B O   
3293 N N   . LEU B 73  ? 0.1883 0.1417 0.2250 0.0021  0.0538  0.0081  53  LEU B N   
3294 C CA  . LEU B 73  ? 0.2025 0.1430 0.2169 0.0011  0.0602  -0.0083 53  LEU B CA  
3295 C C   . LEU B 73  ? 0.2079 0.1587 0.1880 -0.0095 0.0570  -0.0259 53  LEU B C   
3296 O O   . LEU B 73  ? 0.2124 0.1879 0.1985 -0.0037 0.0629  -0.0409 53  LEU B O   
3297 C CB  . LEU B 73  ? 0.2065 0.1529 0.2216 -0.0104 0.0573  0.0015  53  LEU B CB  
3298 C CG  . LEU B 73  ? 0.2087 0.1720 0.2260 -0.0061 0.0619  -0.0022 53  LEU B CG  
3299 C CD1 . LEU B 73  ? 0.1886 0.1903 0.2071 0.0056  0.0534  -0.0069 53  LEU B CD1 
3300 C CD2 . LEU B 73  ? 0.2406 0.1894 0.2785 0.0113  0.0546  0.0372  53  LEU B CD2 
3312 N N   . TRP B 74  ? 0.1882 0.1659 0.1927 -0.0152 0.0317  -0.0256 54  TRP B N   
3313 C CA  . TRP B 74  ? 0.2379 0.1938 0.1852 -0.0269 0.0150  -0.0106 54  TRP B CA  
3314 C C   . TRP B 74  ? 0.2664 0.2389 0.1753 -0.0484 0.0023  -0.0088 54  TRP B C   
3315 O O   . TRP B 74  ? 0.3490 0.2859 0.1953 -0.1165 0.0025  0.0010  54  TRP B O   
3316 C CB  . TRP B 74  ? 0.1950 0.1980 0.2168 -0.0321 0.0141  -0.0020 54  TRP B CB  
3317 C CG  . TRP B 74  ? 0.2128 0.2070 0.1892 -0.0015 0.0034  0.0132  54  TRP B CG  
3318 C CD1 . TRP B 74  ? 0.2412 0.2237 0.2387 -0.0357 0.0053  0.0227  54  TRP B CD1 
3319 C CD2 . TRP B 74  ? 0.2274 0.1961 0.1864 -0.0020 0.0151  0.0059  54  TRP B CD2 
3320 N NE1 . TRP B 74  ? 0.2666 0.2511 0.2518 -0.0594 0.0236  0.0083  54  TRP B NE1 
3321 C CE2 . TRP B 74  ? 0.2436 0.2149 0.2096 -0.0503 0.0256  -0.0026 54  TRP B CE2 
3322 C CE3 . TRP B 74  ? 0.2341 0.1794 0.2193 -0.0048 0.0539  0.0290  54  TRP B CE3 
3323 C CZ2 . TRP B 74  ? 0.2806 0.2175 0.2064 -0.0349 0.0578  -0.0045 54  TRP B CZ2 
3324 C CZ3 . TRP B 74  ? 0.2352 0.1798 0.2412 -0.0007 0.0592  0.0267  54  TRP B CZ3 
3325 C CH2 . TRP B 74  ? 0.2449 0.2018 0.2351 -0.0274 0.0651  0.0187  54  TRP B CH2 
3336 N N   . THR B 75  ? 0.2175 0.1902 0.1946 -0.0339 0.0287  -0.0114 55  THR B N   
3337 C CA  . THR B 75  ? 0.2028 0.1789 0.1880 -0.0186 0.0257  -0.0152 55  THR B CA  
3338 C C   . THR B 75  ? 0.2117 0.1720 0.1931 -0.0126 0.0373  -0.0256 55  THR B C   
3339 O O   . THR B 75  ? 0.2303 0.1859 0.2154 -0.0051 0.0178  -0.0191 55  THR B O   
3340 C CB  . THR B 75  ? 0.2051 0.1811 0.1849 -0.0141 0.0386  -0.0240 55  THR B CB  
3341 O OG1 . THR B 75  ? 0.2274 0.1786 0.1815 -0.0150 0.0310  -0.0212 55  THR B OG1 
3342 C CG2 . THR B 75  ? 0.2247 0.1808 0.1935 -0.0031 0.0242  0.0031  55  THR B CG2 
3350 N N   . THR B 76  ? 0.2189 0.1749 0.2376 -0.0241 0.0435  -0.0509 56  THR B N   
3351 C CA  . THR B 76  ? 0.1994 0.1754 0.2961 0.0041  0.0446  -0.0611 56  THR B CA  
3352 C C   . THR B 76  ? 0.1974 0.1740 0.3053 0.0086  0.0166  -0.0335 56  THR B C   
3353 O O   . THR B 76  ? 0.1969 0.1823 0.3211 0.0094  0.0113  -0.0394 56  THR B O   
3354 C CB  . THR B 76  ? 0.2383 0.2594 0.3906 -0.0600 0.0928  -0.1498 56  THR B CB  
3355 O OG1 . THR B 76  ? 0.3146 0.3285 0.4245 -0.1056 0.1395  -0.1641 56  THR B OG1 
3356 C CG2 . THR B 76  ? 0.2465 0.3046 0.4469 -0.0855 0.1224  -0.1582 56  THR B CG2 
3364 N N   . ASP B 77  ? 0.1861 0.1752 0.2997 -0.0121 -0.0005 -0.0474 57  ASP B N   
3365 C CA  . ASP B 77  ? 0.2181 0.1887 0.3529 -0.0265 -0.0080 -0.0549 57  ASP B CA  
3366 C C   . ASP B 77  ? 0.2465 0.2566 0.3552 -0.0106 -0.0205 -0.0779 57  ASP B C   
3367 O O   . ASP B 77  ? 0.2911 0.2816 0.3724 -0.0190 -0.0464 -0.0710 57  ASP B O   
3368 C CB  . ASP B 77  ? 0.2306 0.1911 0.3994 0.0029  0.0237  -0.0609 57  ASP B CB  
3369 C CG  . ASP B 77  ? 0.2769 0.2252 0.5113 0.0202  0.0543  -0.1324 57  ASP B CG  
3370 O OD1 . ASP B 77  ? 0.3443 0.3329 0.5914 -0.0141 0.1267  -0.1798 57  ASP B OD1 
3371 O OD2 . ASP B 77  ? 0.2375 0.3572 0.5462 0.0316  -0.0090 -0.1935 57  ASP B OD2 
3376 N N   . SER B 78  ? 0.2764 0.2695 0.3258 -0.0114 0.0122  -0.1129 58  SER B N   
3377 C CA  . SER B 78  ? 0.3447 0.3421 0.3168 -0.0492 0.0333  -0.1349 58  SER B CA  
3378 C C   . SER B 78  ? 0.4100 0.3815 0.3110 -0.0767 0.0301  -0.0997 58  SER B C   
3379 O O   . SER B 78  ? 0.4725 0.4419 0.3160 -0.0742 0.0204  -0.1001 58  SER B O   
3380 C CB  . SER B 78  ? 0.3833 0.4472 0.3403 -0.0990 0.0641  -0.1586 58  SER B CB  
3381 O OG  . SER B 78  ? 0.4091 0.5093 0.3592 -0.1120 0.0730  -0.1819 58  SER B OG  
3387 N N   . GLY B 79  ? 0.4105 0.3373 0.3095 -0.0842 0.0297  -0.0639 59  GLY B N   
3388 C CA  . GLY B 79  ? 0.4079 0.3323 0.3309 -0.1152 0.0299  -0.0117 59  GLY B CA  
3389 C C   . GLY B 79  ? 0.4192 0.3641 0.3508 -0.1067 0.0082  -0.0031 59  GLY B C   
3390 O O   . GLY B 79  ? 0.5014 0.4325 0.3639 -0.0941 -0.0083 0.0219  59  GLY B O   
3394 N N   . GLN B 80  ? 0.3815 0.3456 0.3259 -0.1081 0.0130  -0.0400 60  GLN B N   
3395 C CA  . GLN B 80  ? 0.4375 0.3577 0.2899 -0.0914 0.0257  -0.0984 60  GLN B CA  
3396 C C   . GLN B 80  ? 0.4140 0.2865 0.2730 -0.0687 -0.0010 -0.0634 60  GLN B C   
3397 O O   . GLN B 80  ? 0.4249 0.2940 0.2956 -0.0659 0.0044  -0.0575 60  GLN B O   
3398 C CB  . GLN B 80  ? 0.5310 0.4808 0.2855 -0.0873 0.0622  -0.1677 60  GLN B CB  
3399 C CG  . GLN B 80  ? 0.6290 0.5980 0.3962 -0.0597 0.0486  -0.1523 60  GLN B CG  
3400 C CD  . GLN B 80  ? 0.6994 0.7187 0.4695 -0.0218 0.0321  -0.1184 60  GLN B CD  
3401 O OE1 . GLN B 80  ? 0.7147 0.7747 0.4900 0.0005  0.0280  -0.1075 60  GLN B OE1 
3402 N NE2 . GLN B 80  ? 0.7364 0.7571 0.5004 -0.0106 0.0347  -0.1022 60  GLN B NE2 
3411 N N   . PRO B 81  ? 0.3880 0.2579 0.2622 -0.0407 -0.0056 -0.0495 61  PRO B N   
3412 C CA  . PRO B 81  ? 0.3240 0.2617 0.2307 -0.0596 0.0211  -0.0392 61  PRO B CA  
3413 C C   . PRO B 81  ? 0.3098 0.2663 0.2524 -0.0239 0.0633  -0.0282 61  PRO B C   
3414 O O   . PRO B 81  ? 0.3680 0.3326 0.2584 -0.0153 0.0839  -0.0575 61  PRO B O   
3415 C CB  . PRO B 81  ? 0.3876 0.2622 0.2629 -0.0548 0.0183  -0.0293 61  PRO B CB  
3416 C CG  . PRO B 81  ? 0.4464 0.3010 0.3093 -0.0323 0.0015  -0.0427 61  PRO B CG  
3417 C CD  . PRO B 81  ? 0.4303 0.2969 0.2968 -0.0219 -0.0100 -0.0629 61  PRO B CD  
3425 N N   . ILE B 82  ? 0.2602 0.2001 0.2648 0.0066  0.0820  -0.0333 62  ILE B N   
3426 C CA  . ILE B 82  ? 0.2444 0.2216 0.2910 0.0300  0.0884  -0.0244 62  ILE B CA  
3427 C C   . ILE B 82  ? 0.2223 0.2073 0.2448 0.0291  0.0923  -0.0622 62  ILE B C   
3428 O O   . ILE B 82  ? 0.2323 0.2434 0.2414 0.0261  0.0739  -0.0688 62  ILE B O   
3429 C CB  . ILE B 82  ? 0.2780 0.2817 0.3769 0.0726  0.1122  0.0504  62  ILE B CB  
3430 C CG1 . ILE B 82  ? 0.2997 0.3177 0.4559 0.0501  0.1014  0.1232  62  ILE B CG1 
3431 C CG2 . ILE B 82  ? 0.2742 0.3181 0.3976 0.1141  0.1414  0.0639  62  ILE B CG2 
3432 C CD1 . ILE B 82  ? 0.3392 0.3876 0.5095 0.0732  0.0543  0.0952  62  ILE B CD1 
3444 N N   . ALA B 83  ? 0.2264 0.2067 0.2821 -0.0194 0.0858  -0.0361 63  ALA B N   
3445 C CA  . ALA B 83  ? 0.2231 0.2304 0.2925 -0.0413 0.0769  -0.0570 63  ALA B CA  
3446 C C   . ALA B 83  ? 0.2093 0.2562 0.3221 -0.0229 0.0838  -0.0553 63  ALA B C   
3447 O O   . ALA B 83  ? 0.2540 0.3175 0.3763 -0.0084 0.0836  -0.1242 63  ALA B O   
3448 C CB  . ALA B 83  ? 0.2775 0.2422 0.3228 -0.0238 0.0521  -0.0255 63  ALA B CB  
3454 N N   . ILE B 84  ? 0.1760 0.2242 0.2650 0.0031  0.0629  -0.0178 64  ILE B N   
3455 C CA  . ILE B 84  ? 0.2081 0.2025 0.2778 -0.0037 0.0563  -0.0204 64  ILE B CA  
3456 C C   . ILE B 84  ? 0.2157 0.1976 0.3147 -0.0120 0.0756  -0.0281 64  ILE B C   
3457 O O   . ILE B 84  ? 0.2175 0.2044 0.3076 0.0047  0.0848  -0.0039 64  ILE B O   
3458 C CB  . ILE B 84  ? 0.2617 0.2095 0.3103 -0.0065 0.0176  -0.0077 64  ILE B CB  
3459 C CG1 . ILE B 84  ? 0.3720 0.2563 0.3392 -0.0154 0.0230  -0.0009 64  ILE B CG1 
3460 C CG2 . ILE B 84  ? 0.2396 0.2491 0.3353 0.0185  0.0081  -0.0349 64  ILE B CG2 
3461 C CD1 . ILE B 84  ? 0.4420 0.3114 0.4028 -0.0263 0.0392  0.0207  64  ILE B CD1 
3473 N N   . ARG B 85  ? 0.2421 0.2580 0.3339 -0.0191 0.1131  -0.0347 65  ARG B N   
3474 C CA  . ARG B 85  ? 0.2412 0.2618 0.3253 -0.0045 0.1208  -0.0424 65  ARG B CA  
3475 C C   . ARG B 85  ? 0.2335 0.2448 0.3474 0.0050  0.1243  -0.0295 65  ARG B C   
3476 O O   . ARG B 85  ? 0.2398 0.2634 0.3879 0.0081  0.1299  -0.0228 65  ARG B O   
3477 C CB  . ARG B 85  ? 0.2806 0.2963 0.3291 -0.0339 0.1152  -0.0587 65  ARG B CB  
3478 C CG  . ARG B 85  ? 0.3485 0.3604 0.3328 -0.0395 0.1068  -0.0545 65  ARG B CG  
3479 C CD  . ARG B 85  ? 0.4139 0.4094 0.3500 -0.0444 0.0765  -0.0489 65  ARG B CD  
3480 N NE  . ARG B 85  ? 0.4569 0.4935 0.3854 -0.0875 0.0424  -0.0339 65  ARG B NE  
3481 C CZ  . ARG B 85  ? 0.5142 0.5758 0.4261 -0.1171 0.0046  -0.0272 65  ARG B CZ  
3482 N NH1 . ARG B 85  ? 0.5224 0.5952 0.4374 -0.1098 -0.0270 -0.0359 65  ARG B NH1 
3483 N NH2 . ARG B 85  ? 0.5544 0.6337 0.4525 -0.1357 0.0065  -0.0158 65  ARG B NH2 
3497 N N   . GLY B 86  ? 0.2378 0.2461 0.3267 -0.0165 0.1015  -0.0221 66  GLY B N   
3498 C CA  . GLY B 86  ? 0.2704 0.2577 0.3332 -0.0321 0.1089  -0.0032 66  GLY B CA  
3499 C C   . GLY B 86  ? 0.2456 0.2268 0.3355 -0.0451 0.1351  -0.0008 66  GLY B C   
3500 O O   . GLY B 86  ? 0.2375 0.2199 0.3578 -0.0178 0.1272  -0.0054 66  GLY B O   
3504 N N   A ARG B 87  ? 0.2387 0.2526 0.3522 -0.0642 0.1133  0.0067  67  ARG B N   
3505 N N   B ARG B 87  ? 0.2460 0.2525 0.3594 -0.0395 0.1119  0.0096  67  ARG B N   
3506 C CA  A ARG B 87  ? 0.2315 0.2725 0.3510 -0.0745 0.0702  0.0126  67  ARG B CA  
3507 C CA  B ARG B 87  ? 0.2318 0.2731 0.3495 -0.0210 0.0899  0.0175  67  ARG B CA  
3508 C C   A ARG B 87  ? 0.2110 0.2700 0.3346 -0.0621 0.0576  0.0118  67  ARG B C   
3509 C C   B ARG B 87  ? 0.2286 0.2854 0.3376 -0.0213 0.0752  0.0301  67  ARG B C   
3510 O O   A ARG B 87  ? 0.2020 0.2558 0.3248 -0.0708 0.0138  -0.0085 67  ARG B O   
3511 O O   B ARG B 87  ? 0.2483 0.2976 0.3417 -0.0287 0.0449  0.0465  67  ARG B O   
3512 C CB  A ARG B 87  ? 0.2542 0.2672 0.3744 -0.0850 0.0435  0.0387  67  ARG B CB  
3513 C CB  B ARG B 87  ? 0.2169 0.2397 0.3533 0.0114  0.1019  0.0460  67  ARG B CB  
3514 C CG  A ARG B 87  ? 0.2754 0.2607 0.4162 -0.0831 0.0151  0.0268  67  ARG B CG  
3515 C CG  B ARG B 87  ? 0.2357 0.1995 0.3972 0.0145  0.0943  0.0176  67  ARG B CG  
3516 C CD  A ARG B 87  ? 0.2859 0.2753 0.4574 -0.1170 -0.0244 0.0160  67  ARG B CD  
3517 C CD  B ARG B 87  ? 0.2767 0.2155 0.4229 -0.0540 0.0542  0.0035  67  ARG B CD  
3518 N NE  A ARG B 87  ? 0.3014 0.2999 0.4995 -0.1412 -0.0329 0.0324  67  ARG B NE  
3519 N NE  B ARG B 87  ? 0.3538 0.2612 0.4758 -0.0825 0.0163  0.0456  67  ARG B NE  
3520 C CZ  A ARG B 87  ? 0.3327 0.3237 0.5272 -0.1802 -0.0324 0.0380  67  ARG B CZ  
3521 C CZ  B ARG B 87  ? 0.4076 0.3419 0.5558 -0.1258 -0.0242 0.0777  67  ARG B CZ  
3522 N NH1 A ARG B 87  ? 0.3848 0.3202 0.5498 -0.1910 -0.0011 0.0363  67  ARG B NH1 
3523 N NH1 B ARG B 87  ? 0.4422 0.3671 0.5882 -0.1503 -0.0313 0.0771  67  ARG B NH1 
3524 N NH2 A ARG B 87  ? 0.3199 0.3490 0.5548 -0.1544 -0.0591 0.0773  67  ARG B NH2 
3525 N NH2 B ARG B 87  ? 0.4140 0.3680 0.5872 -0.1600 -0.0454 0.1197  67  ARG B NH2 
3552 N N   . GLU B 88  ? 0.2321 0.3299 0.3730 -0.0368 0.0618  0.0279  68  GLU B N   
3553 C CA  . GLU B 88  ? 0.2312 0.4026 0.3807 -0.0298 0.0930  0.0382  68  GLU B CA  
3554 C C   . GLU B 88  ? 0.2406 0.3578 0.3564 0.0199  0.0911  -0.0015 68  GLU B C   
3555 O O   . GLU B 88  ? 0.2395 0.3666 0.3618 0.0316  0.0810  0.0291  68  GLU B O   
3556 C CB  . GLU B 88  ? 0.2679 0.4595 0.4261 -0.0094 0.1006  0.0694  68  GLU B CB  
3560 N N   . LYS B 89  ? 0.2388 0.3286 0.3638 0.0149  0.0967  -0.0255 69  LYS B N   
3561 C CA  . LYS B 89  ? 0.2808 0.2738 0.3551 0.0264  0.1102  -0.0434 69  LYS B CA  
3562 C C   . LYS B 89  ? 0.2314 0.2449 0.3302 0.0154  0.0711  -0.0296 69  LYS B C   
3563 O O   . LYS B 89  ? 0.2292 0.2456 0.3486 0.0333  0.0601  -0.0204 69  LYS B O   
3564 C CB  . LYS B 89  ? 0.3745 0.3728 0.3763 0.0389  0.1125  -0.0719 69  LYS B CB  
3565 C CG  . LYS B 89  ? 0.5085 0.5148 0.4578 0.0400  0.1341  -0.0531 69  LYS B CG  
3566 C CD  . LYS B 89  ? 0.6270 0.6184 0.5147 0.0479  0.1661  -0.0778 69  LYS B CD  
3567 C CE  . LYS B 89  ? 0.6978 0.6835 0.5559 0.0604  0.1751  -0.0809 69  LYS B CE  
3568 N NZ  . LYS B 89  ? 0.7282 0.7096 0.5947 0.0661  0.1719  -0.0783 69  LYS B NZ  
3582 N N   . LEU B 90  ? 0.1882 0.2248 0.3078 -0.0014 0.0681  -0.0227 70  LEU B N   
3583 C CA  . LEU B 90  ? 0.1905 0.1973 0.3204 -0.0085 0.0718  -0.0041 70  LEU B CA  
3584 C C   . LEU B 90  ? 0.1763 0.2028 0.3374 0.0010  0.0523  -0.0098 70  LEU B C   
3585 O O   . LEU B 90  ? 0.1784 0.2323 0.3512 0.0145  0.0364  0.0051  70  LEU B O   
3586 C CB  . LEU B 90  ? 0.2061 0.1847 0.3432 -0.0264 0.0485  -0.0053 70  LEU B CB  
3587 C CG  . LEU B 90  ? 0.1935 0.1913 0.3352 -0.0318 0.0633  0.0029  70  LEU B CG  
3588 C CD1 . LEU B 90  ? 0.2371 0.2225 0.2888 -0.0258 0.0549  0.0086  70  LEU B CD1 
3589 C CD2 . LEU B 90  ? 0.1830 0.1914 0.3409 -0.0058 0.0358  -0.0128 70  LEU B CD2 
3601 N N   . GLY B 91  ? 0.1772 0.2391 0.3446 0.0001  0.0338  -0.0008 71  GLY B N   
3602 C CA  . GLY B 91  ? 0.1734 0.2923 0.3546 0.0115  0.0279  -0.0048 71  GLY B CA  
3603 C C   . GLY B 91  ? 0.1926 0.2805 0.3511 0.0068  0.0259  -0.0172 71  GLY B C   
3604 O O   . GLY B 91  ? 0.2088 0.3252 0.3894 0.0253  0.0475  0.0244  71  GLY B O   
3608 N N   . GLU B 92  ? 0.2063 0.2800 0.3862 0.0300  0.0361  -0.0071 72  GLU B N   
3609 C CA  . GLU B 92  ? 0.2877 0.2785 0.4172 0.0684  0.0353  -0.0017 72  GLU B CA  
3610 C C   . GLU B 92  ? 0.2995 0.2615 0.3978 0.0689  -0.0121 -0.0117 72  GLU B C   
3611 O O   . GLU B 92  ? 0.3733 0.2842 0.4218 0.0937  -0.0212 -0.0162 72  GLU B O   
3612 C CB  . GLU B 92  ? 0.3493 0.3689 0.4697 0.0971  0.0925  -0.0311 72  GLU B CB  
3613 C CG  . GLU B 92  ? 0.4251 0.5115 0.5210 0.0944  0.1363  -0.0676 72  GLU B CG  
3614 C CD  . GLU B 92  ? 0.5222 0.6382 0.5754 0.0624  0.1679  -0.1210 72  GLU B CD  
3615 O OE1 . GLU B 92  ? 0.5700 0.7100 0.5961 0.0645  0.1494  -0.1614 72  GLU B OE1 
3616 O OE2 . GLU B 92  ? 0.5589 0.6726 0.6014 0.0606  0.1886  -0.1187 72  GLU B OE2 
3623 N N   . HIS B 93  ? 0.2412 0.2452 0.3865 0.0366  -0.0041 0.0076  73  HIS B N   
3624 C CA  A HIS B 93  ? 0.2525 0.2309 0.3792 -0.0031 -0.0020 0.0095  73  HIS B CA  
3625 C CA  B HIS B 93  ? 0.2648 0.2468 0.3765 0.0055  -0.0019 0.0202  73  HIS B CA  
3626 C C   . HIS B 93  ? 0.2610 0.2494 0.3731 -0.0133 -0.0080 0.0330  73  HIS B C   
3627 O O   . HIS B 93  ? 0.2933 0.2494 0.3908 -0.0585 -0.0152 0.0522  73  HIS B O   
3628 C CB  A HIS B 93  ? 0.2703 0.2462 0.3558 -0.0367 0.0165  0.0176  73  HIS B CB  
3629 C CB  B HIS B 93  ? 0.3010 0.2773 0.3526 -0.0209 0.0205  0.0415  73  HIS B CB  
3630 C CG  A HIS B 93  ? 0.2634 0.2420 0.3500 -0.0313 0.0342  0.0102  73  HIS B CG  
3631 C CG  B HIS B 93  ? 0.3025 0.2676 0.3351 -0.0386 0.0532  0.0347  73  HIS B CG  
3632 N ND1 A HIS B 93  ? 0.2752 0.2544 0.3494 -0.0065 0.0137  0.0223  73  HIS B ND1 
3633 N ND1 B HIS B 93  ? 0.3308 0.2922 0.3415 -0.0012 0.0681  0.0281  73  HIS B ND1 
3634 C CD2 A HIS B 93  ? 0.2764 0.2461 0.3711 -0.0375 0.0626  0.0805  73  HIS B CD2 
3635 C CD2 B HIS B 93  ? 0.3156 0.3029 0.3398 -0.0463 0.0482  0.0263  73  HIS B CD2 
3636 C CE1 A HIS B 93  ? 0.2738 0.2312 0.3489 -0.0419 0.0352  0.0033  73  HIS B CE1 
3637 C CE1 B HIS B 93  ? 0.3582 0.3053 0.3574 -0.0231 0.0624  0.0272  73  HIS B CE1 
3638 N NE2 A HIS B 93  ? 0.2708 0.2644 0.3590 -0.0129 0.0510  0.0096  73  HIS B NE2 
3639 N NE2 B HIS B 93  ? 0.3586 0.3074 0.3521 -0.0372 0.0573  0.0220  73  HIS B NE2 
3654 N N   . ALA B 94  ? 0.2098 0.2295 0.3536 0.0057  -0.0027 0.0149  74  ALA B N   
3655 C CA  . ALA B 94  ? 0.1988 0.2345 0.3649 0.0298  0.0142  -0.0103 74  ALA B CA  
3656 C C   . ALA B 94  ? 0.2193 0.2453 0.3462 0.0367  0.0147  -0.0123 74  ALA B C   
3657 O O   . ALA B 94  ? 0.2276 0.2736 0.3361 0.0165  0.0044  0.0096  74  ALA B O   
3658 C CB  . ALA B 94  ? 0.2148 0.2480 0.3755 0.0291  0.0294  0.0050  74  ALA B CB  
3664 N N   . VAL B 95  ? 0.2370 0.2608 0.3626 0.0549  0.0075  0.0159  75  VAL B N   
3665 C CA  . VAL B 95  ? 0.2585 0.2955 0.3909 0.0997  -0.0130 -0.0031 75  VAL B CA  
3666 C C   . VAL B 95  ? 0.3100 0.3090 0.3457 0.0974  0.0079  0.0073  75  VAL B C   
3667 O O   . VAL B 95  ? 0.3681 0.3414 0.3435 0.0983  -0.0063 0.0194  75  VAL B O   
3668 C CB  . VAL B 95  ? 0.2781 0.3369 0.4828 0.1091  -0.0200 -0.0072 75  VAL B CB  
3669 C CG1 . VAL B 95  ? 0.3028 0.3689 0.5318 0.1154  -0.0328 -0.0105 75  VAL B CG1 
3670 C CG2 . VAL B 95  ? 0.2706 0.3950 0.5044 0.0978  0.0063  -0.0007 75  VAL B CG2 
3680 N N   . TRP B 96  ? 0.2973 0.2732 0.3613 0.1002  0.0299  -0.0064 76  TRP B N   
3681 C CA  . TRP B 96  ? 0.3197 0.2471 0.3531 0.0852  0.0718  0.0023  76  TRP B CA  
3682 C C   . TRP B 96  ? 0.3046 0.2288 0.3253 0.0529  0.0538  0.0086  76  TRP B C   
3683 O O   . TRP B 96  ? 0.3528 0.2242 0.3069 0.0490  0.0400  0.0133  76  TRP B O   
3684 C CB  . TRP B 96  ? 0.3806 0.2404 0.3504 0.0544  0.0763  -0.0108 76  TRP B CB  
3685 C CG  . TRP B 96  ? 0.4528 0.2495 0.3479 0.0188  0.0737  -0.0136 76  TRP B CG  
3686 C CD1 . TRP B 96  ? 0.5046 0.2492 0.3860 0.0326  0.0522  -0.0382 76  TRP B CD1 
3687 C CD2 . TRP B 96  ? 0.4637 0.2783 0.3376 -0.0495 0.0537  -0.0073 76  TRP B CD2 
3688 N NE1 . TRP B 96  ? 0.5283 0.3024 0.3807 -0.0364 0.0381  -0.0284 76  TRP B NE1 
3689 C CE2 . TRP B 96  ? 0.4828 0.3076 0.3447 -0.0801 0.0312  -0.0102 76  TRP B CE2 
3690 C CE3 . TRP B 96  ? 0.4440 0.3005 0.3527 -0.0594 0.0209  -0.0114 76  TRP B CE3 
3691 C CZ2 . TRP B 96  ? 0.4779 0.3744 0.3260 -0.1012 0.0116  -0.0043 76  TRP B CZ2 
3692 C CZ3 . TRP B 96  ? 0.4410 0.3052 0.3427 -0.0670 0.0157  -0.0426 76  TRP B CZ3 
3693 C CH2 . TRP B 96  ? 0.4455 0.3464 0.3131 -0.1079 0.0156  -0.0404 76  TRP B CH2 
3704 N N   . SER B 97  ? 0.2487 0.1932 0.3381 0.0356  0.0398  0.0117  77  SER B N   
3705 C CA  . SER B 97  ? 0.2270 0.2180 0.3852 0.0032  0.0432  -0.0071 77  SER B CA  
3706 C C   . SER B 97  ? 0.2281 0.2293 0.3430 0.0165  0.0393  -0.0163 77  SER B C   
3707 O O   . SER B 97  ? 0.2180 0.2540 0.3222 0.0412  0.0412  -0.0146 77  SER B O   
3708 C CB  . SER B 97  ? 0.2073 0.2973 0.4720 0.0091  0.0468  0.0281  77  SER B CB  
3709 O OG  . SER B 97  ? 0.2034 0.3027 0.5649 0.0266  0.0441  0.0082  77  SER B OG  
3715 N N   A LEU B 98  ? 0.2700 0.2873 0.3422 0.0169  0.0313  -0.0103 78  LEU B N   
3716 N N   B LEU B 98  ? 0.2484 0.2702 0.3363 0.0054  0.0192  -0.0168 78  LEU B N   
3717 C CA  A LEU B 98  ? 0.3070 0.3441 0.3261 0.0049  0.0398  -0.0120 78  LEU B CA  
3718 C CA  B LEU B 98  ? 0.2602 0.3135 0.3070 -0.0153 0.0228  -0.0263 78  LEU B CA  
3719 C C   A LEU B 98  ? 0.3130 0.3696 0.3227 0.0006  0.0250  -0.0125 78  LEU B C   
3720 C C   B LEU B 98  ? 0.2784 0.3403 0.3206 -0.0073 0.0092  -0.0198 78  LEU B C   
3721 O O   A LEU B 98  ? 0.3479 0.4053 0.3212 -0.0168 0.0461  -0.0205 78  LEU B O   
3722 O O   B LEU B 98  ? 0.3336 0.3683 0.3326 -0.0166 0.0407  -0.0166 78  LEU B O   
3723 C CB  A LEU B 98  ? 0.3553 0.3905 0.3557 0.0090  0.0561  0.0065  78  LEU B CB  
3724 C CB  B LEU B 98  ? 0.2842 0.3512 0.3259 -0.0257 0.0325  -0.0030 78  LEU B CB  
3725 C CG  A LEU B 98  ? 0.3880 0.4098 0.3782 0.0213  0.0483  0.0011  78  LEU B CG  
3726 C CG  B LEU B 98  ? 0.2813 0.3380 0.3180 -0.0148 0.0104  -0.0273 78  LEU B CG  
3727 C CD1 A LEU B 98  ? 0.3986 0.4303 0.3988 0.0317  0.0283  0.0167  78  LEU B CD1 
3728 C CD1 B LEU B 98  ? 0.3042 0.3586 0.3507 0.0055  0.0209  -0.0561 78  LEU B CD1 
3729 C CD2 A LEU B 98  ? 0.3912 0.4061 0.3757 0.0301  0.0496  -0.0088 78  LEU B CD2 
3730 C CD2 B LEU B 98  ? 0.2818 0.3143 0.2976 -0.0458 -0.0120 0.0084  78  LEU B CD2 
3753 N N   A GLN B 99  ? 0.2831 0.3296 0.3380 0.0222  0.0048  0.0035  79  GLN B N   
3754 N N   B GLN B 99  ? 0.2425 0.2915 0.3328 0.0182  -0.0118 -0.0082 79  GLN B N   
3755 C CA  A GLN B 99  ? 0.2840 0.3273 0.3772 0.0611  0.0110  0.0271  79  GLN B CA  
3756 C CA  B GLN B 99  ? 0.2626 0.3087 0.3790 0.0698  0.0024  0.0239  79  GLN B CA  
3757 C C   A GLN B 99  ? 0.2704 0.3158 0.3569 0.0466  0.0064  0.0456  79  GLN B C   
3758 C C   B GLN B 99  ? 0.2725 0.3042 0.3578 0.0534  -0.0050 0.0490  79  GLN B C   
3759 O O   A GLN B 99  ? 0.2809 0.3146 0.3751 0.0374  -0.0028 0.0486  79  GLN B O   
3760 O O   B GLN B 99  ? 0.2945 0.3168 0.3652 0.0335  -0.0348 0.0432  79  GLN B O   
3761 C CB  A GLN B 99  ? 0.3304 0.3627 0.4443 0.1052  0.0358  0.0239  79  GLN B CB  
3762 C CB  B GLN B 99  ? 0.3216 0.3635 0.4633 0.1101  0.0358  0.0215  79  GLN B CB  
3763 C CG  A GLN B 99  ? 0.3874 0.4212 0.5007 0.1367  0.0696  0.0306  79  GLN B CG  
3764 C CG  B GLN B 99  ? 0.3924 0.4579 0.5422 0.1172  0.0746  0.0350  79  GLN B CG  
3765 C CD  A GLN B 99  ? 0.4282 0.4438 0.5694 0.1888  0.0999  0.0159  79  GLN B CD  
3766 C CD  B GLN B 99  ? 0.4592 0.5454 0.6176 0.1241  0.1075  0.0485  79  GLN B CD  
3767 O OE1 A GLN B 99  ? 0.4428 0.4142 0.5843 0.1764  0.1000  -0.0102 79  GLN B OE1 
3768 O OE1 B GLN B 99  ? 0.5086 0.5917 0.6461 0.1281  0.1315  0.0487  79  GLN B OE1 
3769 N NE2 A GLN B 99  ? 0.4331 0.4639 0.6046 0.2356  0.1144  0.0310  79  GLN B NE2 
3770 N NE2 B GLN B 99  ? 0.4534 0.5461 0.6425 0.1327  0.1205  0.0475  79  GLN B NE2 
3787 N N   A CYS B 100 ? 0.2562 0.2925 0.3183 0.0329  0.0265  0.0264  80  CYS B N   
3788 N N   B CYS B 100 ? 0.2581 0.2707 0.3178 0.0491  0.0248  0.0415  80  CYS B N   
3789 C CA  A CYS B 100 ? 0.2422 0.2692 0.3048 0.0121  0.0244  0.0156  80  CYS B CA  
3790 C CA  B CYS B 100 ? 0.2430 0.2599 0.3128 0.0360  0.0188  0.0318  80  CYS B CA  
3791 C C   A CYS B 100 ? 0.2230 0.2493 0.2931 0.0280  0.0253  0.0461  80  CYS B C   
3792 C C   B CYS B 100 ? 0.2327 0.2577 0.3089 0.0336  0.0302  0.0309  80  CYS B C   
3793 O O   A CYS B 100 ? 0.2244 0.2164 0.2916 0.0350  0.0281  0.0785  80  CYS B O   
3794 O O   B CYS B 100 ? 0.2554 0.2592 0.3325 0.0236  0.0485  0.0074  80  CYS B O   
3795 C CB  A CYS B 100 ? 0.2683 0.2681 0.3017 -0.0078 0.0304  0.0099  80  CYS B CB  
3796 C CB  B CYS B 100 ? 0.2703 0.2700 0.3154 0.0263  0.0185  0.0684  80  CYS B CB  
3797 S SG  A CYS B 100 ? 0.2821 0.2498 0.2993 0.0148  0.0454  -0.0112 80  CYS B SG  
3798 S SG  B CYS B 100 ? 0.3142 0.2450 0.3184 0.0392  0.0258  0.0020  80  CYS B SG  
3809 N N   . PHE B 101 ? 0.2141 0.2505 0.2911 0.0411  0.0214  0.0333  81  PHE B N   
3810 C CA  . PHE B 101 ? 0.1909 0.2541 0.2507 0.0372  -0.0041 0.0273  81  PHE B CA  
3811 C C   . PHE B 101 ? 0.1960 0.2758 0.2669 0.0345  -0.0194 0.0328  81  PHE B C   
3812 O O   . PHE B 101 ? 0.2262 0.2594 0.2638 0.0218  -0.0270 0.0273  81  PHE B O   
3813 C CB  . PHE B 101 ? 0.2146 0.2525 0.2328 0.0305  -0.0140 0.0232  81  PHE B CB  
3814 C CG  . PHE B 101 ? 0.2391 0.2556 0.2410 0.0441  -0.0280 -0.0127 81  PHE B CG  
3815 C CD1 . PHE B 101 ? 0.2311 0.2731 0.2482 0.0256  -0.0212 -0.0047 81  PHE B CD1 
3816 C CD2 . PHE B 101 ? 0.2841 0.2920 0.3033 0.0306  0.0050  -0.0388 81  PHE B CD2 
3817 C CE1 . PHE B 101 ? 0.2546 0.2901 0.2763 0.0557  -0.0216 -0.0261 81  PHE B CE1 
3818 C CE2 . PHE B 101 ? 0.3196 0.3407 0.3129 0.0172  0.0097  -0.0393 81  PHE B CE2 
3819 C CZ  . PHE B 101 ? 0.2987 0.3144 0.2989 0.0230  -0.0342 -0.0699 81  PHE B CZ  
3830 N N   . PRO B 102 ? 0.1994 0.3065 0.2784 0.0306  -0.0355 0.0430  82  PRO B N   
3831 C CA  . PRO B 102 ? 0.2074 0.3425 0.2888 0.0428  -0.0713 0.0524  82  PRO B CA  
3832 C C   . PRO B 102 ? 0.2493 0.3556 0.2982 0.0235  -0.0734 0.0187  82  PRO B C   
3833 O O   . PRO B 102 ? 0.2912 0.3957 0.3527 -0.0094 -0.0539 -0.0191 82  PRO B O   
3834 C CB  . PRO B 102 ? 0.2199 0.3488 0.3116 0.0377  -0.0553 0.0655  82  PRO B CB  
3835 C CG  . PRO B 102 ? 0.2222 0.3278 0.3006 0.0424  -0.0371 0.0860  82  PRO B CG  
3836 C CD  . PRO B 102 ? 0.2254 0.2999 0.2798 0.0404  -0.0229 0.0665  82  PRO B CD  
3844 N N   . ASP B 103 ? 0.2264 0.3423 0.2764 0.0548  -0.0727 0.0113  83  ASP B N   
3845 C CA  . ASP B 103 ? 0.2500 0.3161 0.2405 0.0421  -0.0659 0.0065  83  ASP B CA  
3846 C C   . ASP B 103 ? 0.2206 0.2992 0.2053 0.0476  -0.0537 -0.0289 83  ASP B C   
3847 O O   . ASP B 103 ? 0.2798 0.3226 0.2060 0.0562  -0.0405 -0.0296 83  ASP B O   
3848 C CB  . ASP B 103 ? 0.2974 0.3595 0.2406 0.0500  -0.0660 0.0297  83  ASP B CB  
3849 C CG  . ASP B 103 ? 0.3415 0.3625 0.2336 0.0246  -0.0589 0.0204  83  ASP B CG  
3850 O OD1 . ASP B 103 ? 0.3131 0.3580 0.2338 0.0477  -0.0499 -0.0102 83  ASP B OD1 
3851 O OD2 . ASP B 103 ? 0.3931 0.3670 0.2594 -0.0128 -0.0330 0.0106  83  ASP B OD2 
3856 N N   . TRP B 104 ? 0.2116 0.2755 0.2080 0.0504  -0.0535 -0.0070 84  TRP B N   
3857 C CA  . TRP B 104 ? 0.2090 0.2676 0.1868 0.0328  -0.0278 -0.0295 84  TRP B CA  
3858 C C   . TRP B 104 ? 0.1998 0.2575 0.1875 0.0256  -0.0159 -0.0259 84  TRP B C   
3859 O O   . TRP B 104 ? 0.2318 0.2613 0.2354 0.0210  -0.0032 -0.0349 84  TRP B O   
3860 C CB  . TRP B 104 ? 0.1964 0.2445 0.1921 0.0327  -0.0143 -0.0375 84  TRP B CB  
3861 C CG  . TRP B 104 ? 0.1965 0.2289 0.1949 0.0361  -0.0149 -0.0349 84  TRP B CG  
3862 C CD1 . TRP B 104 ? 0.2219 0.2116 0.2245 0.0320  0.0043  -0.0240 84  TRP B CD1 
3863 C CD2 . TRP B 104 ? 0.1966 0.2156 0.1828 0.0478  -0.0153 -0.0098 84  TRP B CD2 
3864 N NE1 . TRP B 104 ? 0.2211 0.2327 0.2271 0.0425  -0.0150 -0.0216 84  TRP B NE1 
3865 C CE2 . TRP B 104 ? 0.2055 0.2360 0.1984 0.0544  0.0008  -0.0203 84  TRP B CE2 
3866 C CE3 . TRP B 104 ? 0.2199 0.2429 0.1564 0.0619  -0.0093 -0.0084 84  TRP B CE3 
3867 C CZ2 . TRP B 104 ? 0.2161 0.2560 0.1682 0.0452  -0.0002 -0.0189 84  TRP B CZ2 
3868 C CZ3 . TRP B 104 ? 0.2310 0.2497 0.1590 0.0388  -0.0163 -0.0108 84  TRP B CZ3 
3869 C CH2 . TRP B 104 ? 0.2260 0.2668 0.1781 0.0386  -0.0113 -0.0083 84  TRP B CH2 
3880 N N   . VAL B 105 ? 0.1975 0.2413 0.1976 0.0137  -0.0107 -0.0406 85  VAL B N   
3881 C CA  . VAL B 105 ? 0.2008 0.2557 0.1784 0.0123  -0.0281 -0.0370 85  VAL B CA  
3882 C C   . VAL B 105 ? 0.2014 0.2414 0.1713 -0.0045 -0.0123 -0.0321 85  VAL B C   
3883 O O   . VAL B 105 ? 0.1979 0.2308 0.1782 0.0039  -0.0168 -0.0284 85  VAL B O   
3884 C CB  . VAL B 105 ? 0.2233 0.2835 0.1831 0.0226  -0.0285 -0.0589 85  VAL B CB  
3885 C CG1 . VAL B 105 ? 0.2329 0.3307 0.2258 0.0272  -0.0410 -0.0738 85  VAL B CG1 
3886 C CG2 . VAL B 105 ? 0.2435 0.2673 0.1722 0.0274  -0.0171 -0.0572 85  VAL B CG2 
3896 N N   . TRP B 106 ? 0.1908 0.2317 0.1901 -0.0094 0.0120  -0.0147 86  TRP B N   
3897 C CA  . TRP B 106 ? 0.1813 0.2389 0.1644 0.0160  0.0033  -0.0179 86  TRP B CA  
3898 C C   . TRP B 106 ? 0.1976 0.2460 0.1803 -0.0023 -0.0049 -0.0381 86  TRP B C   
3899 O O   . TRP B 106 ? 0.2038 0.2831 0.1799 -0.0013 -0.0045 -0.0434 86  TRP B O   
3900 C CB  . TRP B 106 ? 0.1730 0.2561 0.1698 0.0319  -0.0076 -0.0176 86  TRP B CB  
3901 C CG  . TRP B 106 ? 0.1750 0.2406 0.1560 0.0031  -0.0038 -0.0138 86  TRP B CG  
3902 C CD1 . TRP B 106 ? 0.1730 0.2317 0.1788 0.0019  0.0054  -0.0288 86  TRP B CD1 
3903 C CD2 . TRP B 106 ? 0.1969 0.2262 0.1459 0.0082  -0.0330 -0.0198 86  TRP B CD2 
3904 N NE1 . TRP B 106 ? 0.1971 0.2538 0.1722 0.0225  0.0124  -0.0304 86  TRP B NE1 
3905 C CE2 . TRP B 106 ? 0.2175 0.2381 0.1728 0.0224  0.0017  -0.0341 86  TRP B CE2 
3906 C CE3 . TRP B 106 ? 0.2172 0.2163 0.1574 0.0045  -0.0430 -0.0255 86  TRP B CE3 
3907 C CZ2 . TRP B 106 ? 0.2473 0.2290 0.1675 0.0485  -0.0023 -0.0073 86  TRP B CZ2 
3908 C CZ3 . TRP B 106 ? 0.2179 0.2209 0.2041 0.0240  -0.0497 -0.0312 86  TRP B CZ3 
3909 C CH2 . TRP B 106 ? 0.2550 0.2424 0.1743 0.0360  -0.0532 -0.0259 86  TRP B CH2 
3920 N N   . THR B 107 ? 0.1979 0.2484 0.1715 0.0038  0.0015  -0.0419 87  THR B N   
3921 C CA  . THR B 107 ? 0.2042 0.2723 0.1562 0.0095  0.0142  -0.0318 87  THR B CA  
3922 C C   . THR B 107 ? 0.1964 0.2359 0.1562 0.0148  0.0143  -0.0308 87  THR B C   
3923 O O   . THR B 107 ? 0.2164 0.2420 0.1334 0.0176  -0.0024 -0.0369 87  THR B O   
3924 C CB  . THR B 107 ? 0.2282 0.3080 0.1703 0.0265  -0.0110 -0.0176 87  THR B CB  
3925 O OG1 . THR B 107 ? 0.2467 0.2822 0.1948 0.0323  -0.0029 -0.0101 87  THR B OG1 
3926 C CG2 . THR B 107 ? 0.2478 0.3191 0.1863 0.0382  0.0168  0.0128  87  THR B CG2 
3934 N N   . ASP B 108 ? 0.2095 0.2420 0.1885 0.0397  0.0115  -0.0446 88  ASP B N   
3935 C CA  . ASP B 108 ? 0.2168 0.2451 0.1914 0.0336  0.0165  -0.0385 88  ASP B CA  
3936 C C   . ASP B 108 ? 0.2138 0.2427 0.1673 0.0207  0.0355  -0.0318 88  ASP B C   
3937 O O   . ASP B 108 ? 0.2339 0.2526 0.1880 0.0319  0.0108  -0.0366 88  ASP B O   
3938 C CB  . ASP B 108 ? 0.2231 0.2684 0.2184 0.0221  0.0402  -0.0167 88  ASP B CB  
3939 C CG  . ASP B 108 ? 0.3025 0.2975 0.2227 0.0283  0.0619  -0.0443 88  ASP B CG  
3940 O OD1 . ASP B 108 ? 0.4097 0.3618 0.2727 0.0318  0.1198  -0.0294 88  ASP B OD1 
3941 O OD2 . ASP B 108 ? 0.2515 0.2838 0.2206 0.0172  0.0385  -0.0494 88  ASP B OD2 
3946 N N   . ILE B 109 ? 0.2041 0.2609 0.1602 0.0172  0.0272  -0.0409 89  ILE B N   
3947 C CA  . ILE B 109 ? 0.2038 0.2525 0.1689 0.0242  0.0064  -0.0551 89  ILE B CA  
3948 C C   . ILE B 109 ? 0.2143 0.2281 0.1822 0.0138  0.0172  -0.0656 89  ILE B C   
3949 O O   . ILE B 109 ? 0.2653 0.2473 0.2306 0.0291  -0.0079 -0.0932 89  ILE B O   
3950 C CB  . ILE B 109 ? 0.2050 0.2545 0.1869 0.0218  0.0007  -0.0487 89  ILE B CB  
3951 C CG1 . ILE B 109 ? 0.1943 0.2625 0.2212 0.0200  0.0003  -0.0536 89  ILE B CG1 
3952 C CG2 . ILE B 109 ? 0.2383 0.2727 0.2081 0.0214  0.0008  -0.0238 89  ILE B CG2 
3953 C CD1 . ILE B 109 ? 0.1931 0.3104 0.2463 0.0282  -0.0102 -0.0841 89  ILE B CD1 
3965 N N   . GLN B 110 ? 0.2147 0.1871 0.1922 0.0028  0.0081  -0.0426 90  GLN B N   
3966 C CA  . GLN B 110 ? 0.1998 0.1967 0.2186 0.0156  0.0093  -0.0469 90  GLN B CA  
3967 C C   . GLN B 110 ? 0.1948 0.1945 0.2140 0.0077  0.0116  -0.0310 90  GLN B C   
3968 O O   . GLN B 110 ? 0.2070 0.1803 0.2203 -0.0013 0.0160  -0.0347 90  GLN B O   
3969 C CB  . GLN B 110 ? 0.2197 0.2594 0.2526 0.0177  0.0228  -0.0241 90  GLN B CB  
3970 C CG  . GLN B 110 ? 0.2552 0.3289 0.3745 0.0212  0.0425  -0.0274 90  GLN B CG  
3971 C CD  . GLN B 110 ? 0.2741 0.3643 0.5148 0.0319  0.0385  -0.0358 90  GLN B CD  
3972 O OE1 . GLN B 110 ? 0.2813 0.4269 0.5495 0.0675  -0.0102 -0.0842 90  GLN B OE1 
3973 N NE2 . GLN B 110 ? 0.2382 0.3070 0.6000 0.0447  0.0520  0.0257  90  GLN B NE2 
3982 N N   . ILE B 111 ? 0.1839 0.2011 0.2164 0.0032  0.0220  -0.0387 91  ILE B N   
3983 C CA  . ILE B 111 ? 0.1965 0.1967 0.2222 -0.0142 0.0061  -0.0455 91  ILE B CA  
3984 C C   . ILE B 111 ? 0.2117 0.1753 0.2421 0.0118  0.0167  -0.0710 91  ILE B C   
3985 O O   . ILE B 111 ? 0.2844 0.2053 0.2681 0.0498  -0.0015 -0.0713 91  ILE B O   
3986 C CB  . ILE B 111 ? 0.2113 0.2358 0.2564 -0.0379 0.0112  -0.0385 91  ILE B CB  
3987 C CG1 . ILE B 111 ? 0.2040 0.3115 0.2485 -0.0389 -0.0053 -0.0218 91  ILE B CG1 
3988 C CG2 . ILE B 111 ? 0.2339 0.2496 0.3062 -0.0534 0.0076  -0.0340 91  ILE B CG2 
3989 C CD1 . ILE B 111 ? 0.2334 0.3716 0.2775 -0.0470 0.0158  -0.0394 91  ILE B CD1 
4001 N N   . PHE B 112 ? 0.1708 0.1703 0.2482 0.0069  0.0196  -0.0351 92  PHE B N   
4002 C CA  . PHE B 112 ? 0.1572 0.1648 0.2609 0.0183  0.0149  -0.0238 92  PHE B CA  
4003 C C   . PHE B 112 ? 0.1640 0.1644 0.2904 0.0110  0.0277  -0.0505 92  PHE B C   
4004 O O   . PHE B 112 ? 0.1762 0.1709 0.2722 0.0054  0.0307  -0.0257 92  PHE B O   
4005 C CB  . PHE B 112 ? 0.1677 0.1805 0.2480 0.0130  0.0104  -0.0274 92  PHE B CB  
4006 C CG  . PHE B 112 ? 0.1636 0.1934 0.2593 0.0100  0.0070  -0.0074 92  PHE B CG  
4007 C CD1 . PHE B 112 ? 0.1906 0.2115 0.2513 0.0227  0.0028  0.0007  92  PHE B CD1 
4008 C CD2 . PHE B 112 ? 0.1726 0.2364 0.2657 -0.0277 -0.0055 0.0284  92  PHE B CD2 
4009 C CE1 . PHE B 112 ? 0.2273 0.2912 0.2518 -0.0232 0.0103  -0.0104 92  PHE B CE1 
4010 C CE2 . PHE B 112 ? 0.2092 0.2460 0.2689 -0.0296 0.0047  0.0267  92  PHE B CE2 
4011 C CZ  . PHE B 112 ? 0.2258 0.2851 0.2573 -0.0522 -0.0088 0.0143  92  PHE B CZ  
4021 N N   A GLU B 113 ? 0.1904 0.1615 0.3033 0.0055  0.0194  -0.0438 93  GLU B N   
4022 N N   B GLU B 113 ? 0.1723 0.1691 0.3105 -0.0020 0.0136  -0.0479 93  GLU B N   
4023 C CA  A GLU B 113 ? 0.2106 0.1550 0.3391 -0.0036 0.0289  -0.0350 93  GLU B CA  
4024 C CA  B GLU B 113 ? 0.1828 0.1636 0.3413 -0.0278 0.0161  -0.0471 93  GLU B CA  
4025 C C   A GLU B 113 ? 0.1801 0.1881 0.3111 0.0009  0.0304  -0.0083 93  GLU B C   
4026 C C   B GLU B 113 ? 0.1657 0.1529 0.3274 -0.0026 0.0183  -0.0133 93  GLU B C   
4027 O O   A GLU B 113 ? 0.1667 0.2404 0.3003 0.0046  0.0404  -0.0034 93  GLU B O   
4028 O O   B GLU B 113 ? 0.1555 0.1493 0.3405 -0.0161 -0.0003 -0.0018 93  GLU B O   
4029 C CB  A GLU B 113 ? 0.2540 0.1917 0.4163 -0.0062 0.0470  -0.0394 93  GLU B CB  
4030 C CB  B GLU B 113 ? 0.2099 0.2182 0.3943 -0.0697 0.0178  -0.0694 93  GLU B CB  
4031 C CG  A GLU B 113 ? 0.2820 0.2379 0.4832 -0.0430 0.0557  -0.0943 93  GLU B CG  
4032 C CG  B GLU B 113 ? 0.2286 0.2731 0.4491 -0.0827 -0.0092 -0.1108 93  GLU B CG  
4033 C CD  A GLU B 113 ? 0.3003 0.2643 0.5399 -0.0468 0.0494  -0.0954 93  GLU B CD  
4034 C CD  B GLU B 113 ? 0.2807 0.3389 0.5124 -0.0310 -0.0372 -0.0796 93  GLU B CD  
4035 O OE1 A GLU B 113 ? 0.2864 0.2794 0.5677 -0.0285 0.0053  -0.1269 93  GLU B OE1 
4036 O OE1 B GLU B 113 ? 0.2710 0.3157 0.5191 0.0488  -0.0356 -0.0749 93  GLU B OE1 
4037 O OE2 A GLU B 113 ? 0.3441 0.2796 0.5515 -0.0721 0.0835  -0.0558 93  GLU B OE2 
4038 O OE2 B GLU B 113 ? 0.3172 0.4093 0.5555 -0.0679 -0.0555 -0.0580 93  GLU B OE2 
4051 N N   . THR B 114 ? 0.1634 0.1766 0.3209 -0.0011 0.0324  0.0001  94  THR B N   
4052 C CA  . THR B 114 ? 0.1640 0.1528 0.3416 -0.0196 0.0174  0.0209  94  THR B CA  
4053 C C   . THR B 114 ? 0.1558 0.1654 0.3604 -0.0271 0.0245  0.0226  94  THR B C   
4054 O O   . THR B 114 ? 0.1870 0.1682 0.3969 -0.0246 0.0119  0.0265  94  THR B O   
4055 C CB  . THR B 114 ? 0.1757 0.1576 0.3127 -0.0322 0.0156  0.0517  94  THR B CB  
4056 O OG1 . THR B 114 ? 0.1859 0.1593 0.3150 -0.0300 0.0158  0.0402  94  THR B OG1 
4057 C CG2 . THR B 114 ? 0.1844 0.1663 0.3123 -0.0191 -0.0016 0.0413  94  THR B CG2 
4066 N N   . GLN B 115 ? 0.1466 0.1789 0.3846 -0.0110 0.0094  0.0233  95  GLN B N   
4067 C CA  . GLN B 115 ? 0.1866 0.1690 0.4011 -0.0101 0.0161  0.0792  95  GLN B CA  
4068 C C   . GLN B 115 ? 0.1789 0.1866 0.4090 -0.0086 0.0345  0.0853  95  GLN B C   
4069 O O   . GLN B 115 ? 0.2011 0.1964 0.4439 -0.0306 0.0369  0.0819  95  GLN B O   
4070 C CB  . GLN B 115 ? 0.2013 0.1899 0.4010 0.0073  -0.0049 0.0756  95  GLN B CB  
4071 C CG  . GLN B 115 ? 0.2224 0.2095 0.3480 -0.0316 -0.0079 0.0877  95  GLN B CG  
4072 C CD  . GLN B 115 ? 0.2659 0.2174 0.3296 -0.0456 -0.0040 0.0719  95  GLN B CD  
4073 O OE1 . GLN B 115 ? 0.2033 0.1985 0.3471 -0.0143 0.0006  0.0507  95  GLN B OE1 
4074 N NE2 . GLN B 115 ? 0.3728 0.2942 0.3639 -0.1002 0.0154  0.0740  95  GLN B NE2 
4083 N N   . ASP B 116 ? 0.1780 0.2049 0.3773 0.0045  0.0293  0.0564  96  ASP B N   
4084 C CA  . ASP B 116 ? 0.1977 0.2207 0.3404 0.0092  0.0272  0.0542  96  ASP B CA  
4085 C C   . ASP B 116 ? 0.1792 0.1681 0.3645 0.0006  0.0410  0.0545  96  ASP B C   
4086 O O   . ASP B 116 ? 0.1647 0.1601 0.4032 -0.0115 0.0422  0.0533  96  ASP B O   
4087 C CB  . ASP B 116 ? 0.2178 0.2277 0.3145 -0.0044 0.0192  0.0537  96  ASP B CB  
4088 C CG  . ASP B 116 ? 0.2607 0.2359 0.3134 0.0008  0.0231  0.0494  96  ASP B CG  
4089 O OD1 . ASP B 116 ? 0.2462 0.2561 0.3206 -0.0009 0.0262  0.0228  96  ASP B OD1 
4090 O OD2 . ASP B 116 ? 0.3037 0.2445 0.3167 -0.0202 0.0418  0.0437  96  ASP B OD2 
4095 N N   . PRO B 117 ? 0.1866 0.1678 0.3918 -0.0151 0.0370  0.0382  97  PRO B N   
4096 C CA  . PRO B 117 ? 0.2011 0.1616 0.3775 -0.0289 0.0180  0.0231  97  PRO B CA  
4097 C C   . PRO B 117 ? 0.1820 0.1721 0.3301 -0.0153 0.0404  0.0301  97  PRO B C   
4098 O O   . PRO B 117 ? 0.2097 0.1891 0.3241 0.0034  0.0230  0.0228  97  PRO B O   
4099 C CB  . PRO B 117 ? 0.2315 0.1859 0.4141 -0.0479 0.0402  0.0580  97  PRO B CB  
4100 C CG  . PRO B 117 ? 0.2591 0.2301 0.4213 -0.0640 0.0398  0.0886  97  PRO B CG  
4101 C CD  . PRO B 117 ? 0.2141 0.2031 0.4041 -0.0408 0.0571  0.0724  97  PRO B CD  
4109 N N   . ASN B 118 ? 0.1690 0.1643 0.3262 -0.0024 0.0354  0.0394  98  ASN B N   
4110 C CA  . ASN B 118 ? 0.1597 0.1752 0.3281 -0.0027 0.0531  0.0367  98  ASN B CA  
4111 C C   . ASN B 118 ? 0.1436 0.1845 0.3261 -0.0234 0.0308  0.0319  98  ASN B C   
4112 O O   . ASN B 118 ? 0.1685 0.1853 0.3777 -0.0101 0.0637  0.0256  98  ASN B O   
4113 C CB  . ASN B 118 ? 0.1718 0.2145 0.3371 -0.0116 0.0368  0.0552  98  ASN B CB  
4114 C CG  . ASN B 118 ? 0.2366 0.2478 0.3754 -0.0404 0.0436  0.0684  98  ASN B CG  
4115 O OD1 . ASN B 118 ? 0.2616 0.2626 0.3753 -0.0737 0.0407  0.0415  98  ASN B OD1 
4116 N ND2 . ASN B 118 ? 0.2801 0.2861 0.4347 -0.0515 0.0725  0.0592  98  ASN B ND2 
4123 N N   . TRP B 119 ? 0.1565 0.1720 0.3049 -0.0259 0.0305  0.0296  99  TRP B N   
4124 C CA  . TRP B 119 ? 0.1655 0.1546 0.2901 -0.0185 0.0406  0.0294  99  TRP B CA  
4125 C C   . TRP B 119 ? 0.1416 0.1604 0.2799 -0.0040 0.0550  0.0228  99  TRP B C   
4126 O O   . TRP B 119 ? 0.1466 0.1836 0.2962 0.0163  0.0359  0.0155  99  TRP B O   
4127 C CB  . TRP B 119 ? 0.1518 0.1783 0.2833 -0.0112 0.0152  0.0164  99  TRP B CB  
4128 C CG  . TRP B 119 ? 0.1516 0.1758 0.2502 -0.0171 0.0224  0.0169  99  TRP B CG  
4129 C CD1 . TRP B 119 ? 0.1722 0.1908 0.2337 -0.0185 0.0211  0.0117  99  TRP B CD1 
4130 C CD2 . TRP B 119 ? 0.1625 0.1974 0.2297 -0.0168 0.0133  0.0118  99  TRP B CD2 
4131 N NE1 . TRP B 119 ? 0.1836 0.1649 0.2214 -0.0227 0.0135  0.0212  99  TRP B NE1 
4132 C CE2 . TRP B 119 ? 0.1749 0.1865 0.1973 -0.0118 0.0111  0.0147  99  TRP B CE2 
4133 C CE3 . TRP B 119 ? 0.1938 0.2285 0.2436 0.0058  0.0079  0.0422  99  TRP B CE3 
4134 C CZ2 . TRP B 119 ? 0.2245 0.1988 0.2083 -0.0036 0.0300  0.0185  99  TRP B CZ2 
4135 C CZ3 . TRP B 119 ? 0.2256 0.2532 0.2575 -0.0153 -0.0025 0.0497  99  TRP B CZ3 
4136 C CH2 . TRP B 119 ? 0.2398 0.2318 0.2453 -0.0226 0.0166  0.0448  99  TRP B CH2 
4147 N N   . PHE B 120 ? 0.1547 0.1608 0.2646 -0.0032 0.0228  0.0150  100 PHE B N   
4148 C CA  . PHE B 120 ? 0.1556 0.1495 0.2725 -0.0013 0.0181  0.0026  100 PHE B CA  
4149 C C   . PHE B 120 ? 0.1499 0.1590 0.2452 0.0106  0.0247  -0.0008 100 PHE B C   
4150 O O   . PHE B 120 ? 0.1488 0.1618 0.2720 0.0101  0.0278  -0.0106 100 PHE B O   
4151 C CB  . PHE B 120 ? 0.1540 0.1725 0.2841 -0.0153 0.0180  -0.0286 100 PHE B CB  
4152 C CG  . PHE B 120 ? 0.1606 0.1879 0.3023 -0.0259 0.0259  -0.0015 100 PHE B CG  
4153 C CD1 . PHE B 120 ? 0.2368 0.2267 0.3304 -0.0700 0.0203  0.0067  100 PHE B CD1 
4154 C CD2 . PHE B 120 ? 0.1777 0.2015 0.3423 -0.0026 0.0116  -0.0341 100 PHE B CD2 
4155 C CE1 . PHE B 120 ? 0.2692 0.2600 0.3702 -0.0853 -0.0379 0.0442  100 PHE B CE1 
4156 C CE2 . PHE B 120 ? 0.2187 0.2060 0.3941 0.0017  -0.0154 -0.0398 100 PHE B CE2 
4157 C CZ  . PHE B 120 ? 0.2572 0.1933 0.3982 -0.0554 -0.0454 0.0196  100 PHE B CZ  
4167 N N   . TRP B 121 ? 0.1491 0.1667 0.2289 0.0102  0.0378  -0.0029 101 TRP B N   
4168 C CA  . TRP B 121 ? 0.1620 0.1547 0.2058 0.0126  0.0094  -0.0151 101 TRP B CA  
4169 C C   . TRP B 121 ? 0.1625 0.1679 0.2300 0.0229  0.0158  -0.0217 101 TRP B C   
4170 O O   . TRP B 121 ? 0.2148 0.1711 0.2486 0.0142  0.0213  -0.0157 101 TRP B O   
4171 C CB  . TRP B 121 ? 0.1640 0.1728 0.1989 0.0121  0.0188  -0.0103 101 TRP B CB  
4172 C CG  . TRP B 121 ? 0.1632 0.1681 0.1976 -0.0118 0.0183  0.0114  101 TRP B CG  
4173 C CD1 . TRP B 121 ? 0.1804 0.1842 0.2097 -0.0143 0.0113  0.0005  101 TRP B CD1 
4174 C CD2 . TRP B 121 ? 0.1558 0.1590 0.2037 -0.0023 0.0328  -0.0026 101 TRP B CD2 
4175 N NE1 . TRP B 121 ? 0.1869 0.1849 0.2125 -0.0146 0.0057  0.0194  101 TRP B NE1 
4176 C CE2 . TRP B 121 ? 0.1608 0.1748 0.2167 -0.0181 0.0246  0.0122  101 TRP B CE2 
4177 C CE3 . TRP B 121 ? 0.1504 0.1803 0.2037 -0.0026 0.0364  -0.0119 101 TRP B CE3 
4178 C CZ2 . TRP B 121 ? 0.1343 0.2100 0.2153 -0.0137 0.0124  -0.0061 101 TRP B CZ2 
4179 C CZ3 . TRP B 121 ? 0.1560 0.1816 0.1889 -0.0184 0.0393  -0.0184 101 TRP B CZ3 
4180 C CH2 . TRP B 121 ? 0.1551 0.2155 0.1925 -0.0063 0.0295  -0.0208 101 TRP B CH2 
4191 N N   . VAL B 122 ? 0.1641 0.1649 0.2165 0.0122  0.0107  -0.0335 102 VAL B N   
4192 C CA  . VAL B 122 ? 0.1426 0.1638 0.2014 -0.0003 0.0067  -0.0382 102 VAL B CA  
4193 C C   . VAL B 122 ? 0.1485 0.1498 0.2074 -0.0016 0.0206  -0.0232 102 VAL B C   
4194 O O   . VAL B 122 ? 0.1900 0.1538 0.2269 -0.0121 0.0529  -0.0261 102 VAL B O   
4195 C CB  . VAL B 122 ? 0.1489 0.1984 0.2080 0.0032  0.0051  -0.0196 102 VAL B CB  
4196 C CG1 . VAL B 122 ? 0.1596 0.2504 0.2028 0.0059  -0.0065 -0.0229 102 VAL B CG1 
4197 C CG2 . VAL B 122 ? 0.1627 0.2156 0.2254 -0.0206 0.0154  -0.0097 102 VAL B CG2 
4207 N N   . GLU B 123 ? 0.1465 0.1696 0.1916 0.0121  0.0238  -0.0196 103 GLU B N   
4208 C CA  . GLU B 123 ? 0.1523 0.1687 0.1831 -0.0019 0.0254  -0.0244 103 GLU B CA  
4209 C C   . GLU B 123 ? 0.1630 0.1807 0.1886 -0.0072 0.0194  -0.0309 103 GLU B C   
4210 O O   . GLU B 123 ? 0.1954 0.1881 0.1971 0.0008  0.0122  -0.0297 103 GLU B O   
4211 C CB  . GLU B 123 ? 0.1546 0.1633 0.1810 -0.0020 0.0257  -0.0105 103 GLU B CB  
4212 C CG  . GLU B 123 ? 0.1598 0.2093 0.2008 0.0245  0.0215  -0.0021 103 GLU B CG  
4213 C CD  . GLU B 123 ? 0.1678 0.2155 0.2305 0.0144  0.0297  -0.0231 103 GLU B CD  
4214 O OE1 . GLU B 123 ? 0.1814 0.2023 0.2315 0.0055  0.0189  -0.0246 103 GLU B OE1 
4215 O OE2 . GLU B 123 ? 0.1649 0.2078 0.3108 0.0085  0.0327  0.0073  103 GLU B OE2 
4222 N N   . CYS B 124 ? 0.1571 0.1816 0.1677 0.0142  -0.0003 -0.0270 104 CYS B N   
4223 C CA  . CYS B 124 ? 0.1815 0.2024 0.1472 -0.0039 0.0014  -0.0204 104 CYS B CA  
4224 C C   . CYS B 124 ? 0.1907 0.2113 0.1383 -0.0055 -0.0014 -0.0294 104 CYS B C   
4225 O O   . CYS B 124 ? 0.1897 0.1900 0.1825 0.0126  0.0014  -0.0177 104 CYS B O   
4226 C CB  . CYS B 124 ? 0.1961 0.2045 0.1447 -0.0073 -0.0009 -0.0093 104 CYS B CB  
4227 S SG  . CYS B 124 ? 0.1715 0.2231 0.2100 0.0133  0.0292  -0.0206 104 CYS B SG  
4233 N N   . ARG B 125 ? 0.2105 0.2130 0.1281 -0.0060 0.0049  -0.0349 105 ARG B N   
4234 C CA  . ARG B 125 ? 0.2185 0.2072 0.1497 -0.0003 -0.0039 -0.0224 105 ARG B CA  
4235 C C   . ARG B 125 ? 0.2082 0.2340 0.1718 -0.0027 -0.0011 -0.0089 105 ARG B C   
4236 O O   . ARG B 125 ? 0.2012 0.2179 0.1928 0.0157  0.0070  -0.0373 105 ARG B O   
4237 C CB  . ARG B 125 ? 0.2354 0.2433 0.1560 0.0213  0.0001  -0.0045 105 ARG B CB  
4238 C CG  . ARG B 125 ? 0.2198 0.2763 0.1960 0.0253  0.0105  -0.0047 105 ARG B CG  
4239 C CD  . ARG B 125 ? 0.2242 0.3429 0.2271 0.0017  0.0221  -0.0101 105 ARG B CD  
4240 N NE  . ARG B 125 ? 0.2628 0.4039 0.2596 -0.0186 0.0320  -0.0031 105 ARG B NE  
4241 C CZ  . ARG B 125 ? 0.2694 0.4557 0.2829 -0.0379 0.0302  0.0100  105 ARG B CZ  
4242 N NH1 . ARG B 125 ? 0.2478 0.4907 0.3355 -0.0345 0.0447  0.0238  105 ARG B NH1 
4243 N NH2 . ARG B 125 ? 0.2966 0.4336 0.2763 -0.0244 0.0171  0.0150  105 ARG B NH2 
4257 N N   . GLY B 126 ? 0.1845 0.2258 0.1959 -0.0075 -0.0172 0.0069  106 GLY B N   
4258 C CA  . GLY B 126 ? 0.1828 0.2386 0.2136 0.0123  -0.0160 0.0048  106 GLY B CA  
4259 C C   . GLY B 126 ? 0.1677 0.2365 0.2266 0.0130  -0.0123 -0.0101 106 GLY B C   
4260 O O   . GLY B 126 ? 0.1926 0.2162 0.2330 0.0181  -0.0211 -0.0125 106 GLY B O   
4264 N N   . GLU B 127 ? 0.1900 0.2284 0.2444 0.0248  -0.0179 -0.0103 107 GLU B N   
4265 C CA  . GLU B 127 ? 0.2096 0.2386 0.2270 0.0476  -0.0195 -0.0019 107 GLU B CA  
4266 C C   . GLU B 127 ? 0.2075 0.2430 0.1936 0.0325  0.0081  0.0038  107 GLU B C   
4267 O O   . GLU B 127 ? 0.2128 0.2404 0.2296 0.0073  0.0032  -0.0292 107 GLU B O   
4268 C CB  . GLU B 127 ? 0.2161 0.2801 0.2426 0.0436  0.0047  -0.0304 107 GLU B CB  
4269 C CG  . GLU B 127 ? 0.2545 0.3245 0.2182 0.0534  0.0076  -0.0011 107 GLU B CG  
4270 C CD  . GLU B 127 ? 0.3415 0.3493 0.2523 0.0704  -0.0137 -0.0044 107 GLU B CD  
4271 O OE1 . GLU B 127 ? 0.4374 0.3718 0.2683 0.0362  -0.0196 -0.0071 107 GLU B OE1 
4272 O OE2 . GLU B 127 ? 0.3441 0.3918 0.3143 0.0630  0.0159  -0.0068 107 GLU B OE2 
4279 N N   . GLY B 128 ? 0.2292 0.2548 0.1894 0.0543  0.0056  0.0100  108 GLY B N   
4280 C CA  . GLY B 128 ? 0.2123 0.2729 0.2040 0.0518  -0.0145 0.0081  108 GLY B CA  
4281 C C   . GLY B 128 ? 0.2202 0.2714 0.2171 0.0425  -0.0099 0.0239  108 GLY B C   
4282 O O   . GLY B 128 ? 0.2121 0.2617 0.2394 0.0315  -0.0084 0.0052  108 GLY B O   
4286 N N   . ALA B 129 ? 0.2368 0.2605 0.2201 0.0444  -0.0082 0.0339  109 ALA B N   
4287 C CA  . ALA B 129 ? 0.2601 0.2735 0.2311 0.0505  -0.0143 0.0307  109 ALA B CA  
4288 C C   . ALA B 129 ? 0.2364 0.2313 0.2387 0.0469  -0.0058 0.0461  109 ALA B C   
4289 O O   . ALA B 129 ? 0.2527 0.2389 0.2465 0.0259  0.0096  0.0291  109 ALA B O   
4290 C CB  . ALA B 129 ? 0.3036 0.3137 0.2368 0.0826  -0.0176 0.0593  109 ALA B CB  
4296 N N   . ILE B 130 ? 0.2281 0.2412 0.2451 0.0457  0.0160  0.0330  110 ILE B N   
4297 C CA  . ILE B 130 ? 0.2214 0.2316 0.2627 0.0566  0.0367  0.0291  110 ILE B CA  
4298 C C   . ILE B 130 ? 0.2351 0.2341 0.2709 0.0620  0.0387  0.0434  110 ILE B C   
4299 O O   . ILE B 130 ? 0.2388 0.2525 0.2987 0.0534  0.0289  0.0515  110 ILE B O   
4300 C CB  . ILE B 130 ? 0.2260 0.2531 0.2685 0.0549  0.0242  0.0413  110 ILE B CB  
4301 C CG1 . ILE B 130 ? 0.2179 0.2479 0.2685 0.0517  -0.0155 0.0128  110 ILE B CG1 
4302 C CG2 . ILE B 130 ? 0.2477 0.2574 0.2593 0.0584  0.0228  0.0219  110 ILE B CG2 
4303 C CD1 . ILE B 130 ? 0.2251 0.2528 0.2831 0.0327  -0.0055 0.0038  110 ILE B CD1 
4315 N N   . VAL B 131 ? 0.2221 0.2320 0.2682 0.0473  0.0246  0.0359  111 VAL B N   
4316 C CA  . VAL B 131 ? 0.2254 0.2160 0.2777 0.0509  -0.0034 0.0485  111 VAL B CA  
4317 C C   . VAL B 131 ? 0.2144 0.2228 0.3006 0.0517  -0.0070 0.0280  111 VAL B C   
4318 O O   . VAL B 131 ? 0.2240 0.2372 0.3040 0.0301  -0.0070 -0.0082 111 VAL B O   
4319 C CB  . VAL B 131 ? 0.2636 0.2654 0.2829 0.0555  -0.0192 0.0463  111 VAL B CB  
4320 C CG1 . VAL B 131 ? 0.2628 0.2767 0.2756 0.0649  -0.0229 0.0483  111 VAL B CG1 
4321 C CG2 . VAL B 131 ? 0.2533 0.3328 0.3091 0.0580  -0.0391 0.0491  111 VAL B CG2 
4331 N N   . PHE B 132 ? 0.1901 0.2521 0.2940 0.0406  0.0085  0.0418  112 PHE B N   
4332 C CA  . PHE B 132 ? 0.2105 0.2562 0.3095 0.0025  0.0116  0.0389  112 PHE B CA  
4333 C C   . PHE B 132 ? 0.2406 0.2717 0.3619 -0.0061 0.0123  -0.0055 112 PHE B C   
4334 O O   . PHE B 132 ? 0.2857 0.2267 0.4054 -0.0064 0.0672  -0.0413 112 PHE B O   
4335 C CB  . PHE B 132 ? 0.2353 0.2892 0.3009 -0.0073 0.0181  0.0397  112 PHE B CB  
4336 C CG  . PHE B 132 ? 0.2534 0.2513 0.3395 0.0210  0.0698  0.0416  112 PHE B CG  
4337 C CD1 . PHE B 132 ? 0.2687 0.3431 0.3968 0.0300  0.1217  0.0372  112 PHE B CD1 
4338 C CD2 . PHE B 132 ? 0.2955 0.3093 0.3687 0.0111  0.0412  0.0461  112 PHE B CD2 
4339 C CE1 . PHE B 132 ? 0.2374 0.3433 0.3733 0.0633  0.0931  0.0584  112 PHE B CE1 
4340 C CE2 . PHE B 132 ? 0.2956 0.3439 0.4182 0.0052  -0.0205 0.0518  112 PHE B CE2 
4341 C CZ  . PHE B 132 ? 0.2610 0.3207 0.4200 0.0446  -0.0049 0.0839  112 PHE B CZ  
4351 N N   . PRO B 133 ? 0.2239 0.3187 0.3634 0.0249  0.0276  -0.0092 113 PRO B N   
4352 C CA  . PRO B 133 ? 0.2348 0.3643 0.3905 -0.0023 0.0383  -0.0579 113 PRO B CA  
4353 C C   . PRO B 133 ? 0.2568 0.3873 0.4573 -0.0158 0.0665  -0.1327 113 PRO B C   
4354 O O   . PRO B 133 ? 0.2379 0.4657 0.4751 -0.0356 0.0619  -0.1630 113 PRO B O   
4355 C CB  . PRO B 133 ? 0.2345 0.3795 0.3489 -0.0090 0.0475  -0.0433 113 PRO B CB  
4356 C CG  . PRO B 133 ? 0.2395 0.3983 0.3618 0.0360  0.0590  -0.0082 113 PRO B CG  
4357 C CD  . PRO B 133 ? 0.2174 0.3691 0.3534 0.0440  0.0423  -0.0088 113 PRO B CD  
4365 N N   . GLY B 134 ? 0.2876 0.3197 0.5009 -0.0152 0.0874  -0.1172 114 GLY B N   
4366 C CA  . GLY B 134 ? 0.2919 0.3290 0.5406 -0.0083 0.0743  -0.0928 114 GLY B CA  
4367 C C   . GLY B 134 ? 0.2860 0.2946 0.5259 0.0225  0.0532  -0.0673 114 GLY B C   
4368 O O   . GLY B 134 ? 0.3143 0.2720 0.5511 0.0276  0.0583  -0.0870 114 GLY B O   
4372 N N   . TYR B 135 ? 0.2736 0.2203 0.4512 0.0640  0.0415  -0.0315 115 TYR B N   
4373 C CA  . TYR B 135 ? 0.2791 0.2112 0.4250 0.0432  0.0426  -0.0057 115 TYR B CA  
4374 C C   . TYR B 135 ? 0.2882 0.2287 0.4315 0.0324  0.0554  0.0041  115 TYR B C   
4375 O O   . TYR B 135 ? 0.2842 0.2574 0.4594 -0.0096 0.0503  -0.0088 115 TYR B O   
4376 C CB  . TYR B 135 ? 0.2642 0.2062 0.4028 0.0450  0.0446  -0.0062 115 TYR B CB  
4377 C CG  . TYR B 135 ? 0.2410 0.2080 0.3743 0.0387  0.0379  -0.0148 115 TYR B CG  
4378 C CD1 . TYR B 135 ? 0.2254 0.2039 0.3596 0.0261  0.0277  -0.0254 115 TYR B CD1 
4379 C CD2 . TYR B 135 ? 0.2265 0.2293 0.3878 0.0694  0.0460  0.0157  115 TYR B CD2 
4380 C CE1 . TYR B 135 ? 0.2207 0.2088 0.3437 0.0213  0.0148  -0.0107 115 TYR B CE1 
4381 C CE2 . TYR B 135 ? 0.2300 0.2260 0.3826 0.0544  0.0217  0.0459  115 TYR B CE2 
4382 C CZ  . TYR B 135 ? 0.2275 0.2229 0.3748 0.0417  0.0138  0.0303  115 TYR B CZ  
4383 O OH  . TYR B 135 ? 0.2288 0.2485 0.4279 0.0455  0.0125  0.0293  115 TYR B OH  
4393 N N   . PRO B 136 ? 0.3074 0.2225 0.4326 0.0581  0.0304  0.0157  116 PRO B N   
4394 C CA  . PRO B 136 ? 0.3214 0.2362 0.4096 0.0576  0.0284  0.0556  116 PRO B CA  
4395 C C   . PRO B 136 ? 0.3003 0.2382 0.3580 0.0879  0.0178  0.0734  116 PRO B C   
4396 O O   . PRO B 136 ? 0.2914 0.2255 0.3406 0.0918  0.0109  0.0562  116 PRO B O   
4397 C CB  . PRO B 136 ? 0.3647 0.2726 0.4323 0.0183  0.0309  0.0629  116 PRO B CB  
4398 C CG  . PRO B 136 ? 0.3549 0.2951 0.4444 0.0046  0.0305  0.0318  116 PRO B CG  
4399 C CD  . PRO B 136 ? 0.3366 0.2430 0.4526 0.0316  0.0337  0.0237  116 PRO B CD  
4407 N N   . ARG B 137 ? 0.3239 0.2835 0.3344 0.0606  0.0012  0.0553  117 ARG B N   
4408 C CA  . ARG B 137 ? 0.3580 0.3030 0.3277 0.0572  -0.0055 0.0469  117 ARG B CA  
4409 C C   . ARG B 137 ? 0.3630 0.2623 0.3479 0.0451  0.0340  0.0478  117 ARG B C   
4410 O O   . ARG B 137 ? 0.4013 0.2849 0.3420 0.0086  0.0529  0.0721  117 ARG B O   
4411 C CB  . ARG B 137 ? 0.4367 0.3755 0.3596 0.0385  -0.0311 0.0302  117 ARG B CB  
4412 C CG  . ARG B 137 ? 0.4971 0.4620 0.3975 0.0470  -0.0703 0.0447  117 ARG B CG  
4413 C CD  . ARG B 137 ? 0.5535 0.5364 0.4462 0.0414  -0.0886 0.0525  117 ARG B CD  
4414 N NE  . ARG B 137 ? 0.5788 0.5952 0.4729 0.0317  -0.1163 0.0864  117 ARG B NE  
4415 C CZ  . ARG B 137 ? 0.5874 0.6298 0.4775 0.0452  -0.1442 0.1148  117 ARG B CZ  
4416 N NH1 . ARG B 137 ? 0.6027 0.6433 0.4814 0.0571  -0.1343 0.1050  117 ARG B NH1 
4417 N NH2 . ARG B 137 ? 0.5797 0.6367 0.4755 0.0578  -0.1763 0.1204  117 ARG B NH2 
4431 N N   . GLY B 138 ? 0.3451 0.2475 0.3528 0.0720  0.0705  0.0382  118 GLY B N   
4432 C CA  . GLY B 138 ? 0.3599 0.2746 0.3660 0.0604  0.0862  0.0221  118 GLY B CA  
4433 C C   . GLY B 138 ? 0.3345 0.2552 0.3061 0.0659  0.0491  0.0526  118 GLY B C   
4434 O O   . GLY B 138 ? 0.3340 0.2734 0.3005 0.0547  0.0312  0.0555  118 GLY B O   
4438 N N   . GLN B 139 ? 0.3267 0.2682 0.2766 0.0942  0.0380  0.0761  119 GLN B N   
4439 C CA  . GLN B 139 ? 0.3228 0.3042 0.2223 0.0818  0.0022  0.0709  119 GLN B CA  
4440 C C   . GLN B 139 ? 0.2987 0.2789 0.2287 0.0338  0.0051  0.0869  119 GLN B C   
4441 O O   . GLN B 139 ? 0.3386 0.3292 0.2977 -0.0100 0.0012  0.1044  119 GLN B O   
4442 C CB  . GLN B 139 ? 0.3632 0.4228 0.2216 0.1031  -0.0157 0.0651  119 GLN B CB  
4443 C CG  . GLN B 139 ? 0.4689 0.5738 0.3226 0.0462  0.0365  0.0400  119 GLN B CG  
4444 C CD  . GLN B 139 ? 0.5542 0.6643 0.4234 0.0107  0.0732  0.0126  119 GLN B CD  
4445 O OE1 . GLN B 139 ? 0.6064 0.7233 0.4849 0.0116  0.0904  -0.0070 119 GLN B OE1 
4446 N NE2 . GLN B 139 ? 0.5895 0.7017 0.4661 -0.0056 0.0998  0.0035  119 GLN B NE2 
4455 N N   . TYR B 140 ? 0.2518 0.2221 0.2194 0.0353  -0.0122 0.0163  120 TYR B N   
4456 C CA  . TYR B 140 ? 0.2389 0.2093 0.2010 0.0363  -0.0257 0.0072  120 TYR B CA  
4457 C C   . TYR B 140 ? 0.2215 0.2353 0.2110 0.0391  -0.0268 0.0093  120 TYR B C   
4458 O O   . TYR B 140 ? 0.2393 0.2408 0.2611 0.0365  -0.0227 -0.0243 120 TYR B O   
4459 C CB  . TYR B 140 ? 0.2510 0.2274 0.1987 0.0382  -0.0062 -0.0125 120 TYR B CB  
4460 C CG  . TYR B 140 ? 0.2356 0.2013 0.1993 0.0263  -0.0086 -0.0046 120 TYR B CG  
4461 C CD1 . TYR B 140 ? 0.2335 0.1833 0.2014 0.0286  -0.0117 0.0065  120 TYR B CD1 
4462 C CD2 . TYR B 140 ? 0.2230 0.2125 0.2085 0.0407  -0.0022 -0.0092 120 TYR B CD2 
4463 C CE1 . TYR B 140 ? 0.2513 0.1963 0.1844 0.0178  -0.0125 -0.0018 120 TYR B CE1 
4464 C CE2 . TYR B 140 ? 0.2527 0.2249 0.1896 0.0345  0.0088  0.0026  120 TYR B CE2 
4465 C CZ  . TYR B 140 ? 0.2616 0.2129 0.2059 0.0248  -0.0209 -0.0141 120 TYR B CZ  
4466 O OH  . TYR B 140 ? 0.2678 0.2416 0.2233 0.0383  -0.0060 -0.0209 120 TYR B OH  
4476 N N   . ARG B 141 ? 0.2124 0.2302 0.1949 0.0383  -0.0088 0.0318  121 ARG B N   
4477 C CA  . ARG B 141 ? 0.2358 0.2350 0.2119 0.0388  0.0055  0.0187  121 ARG B CA  
4478 C C   . ARG B 141 ? 0.2045 0.2054 0.2260 0.0210  -0.0069 0.0163  121 ARG B C   
4479 O O   . ARG B 141 ? 0.2402 0.2157 0.2737 0.0131  -0.0269 0.0040  121 ARG B O   
4480 C CB  . ARG B 141 ? 0.2979 0.2916 0.1991 0.0688  0.0412  0.0180  121 ARG B CB  
4481 C CG  . ARG B 141 ? 0.3823 0.3458 0.2482 0.0400  0.0510  0.0064  121 ARG B CG  
4482 C CD  . ARG B 141 ? 0.4781 0.4312 0.3580 -0.0016 0.0570  -0.0146 121 ARG B CD  
4483 N NE  . ARG B 141 ? 0.5706 0.5567 0.4621 -0.0079 0.0546  -0.0045 121 ARG B NE  
4484 C CZ  . ARG B 141 ? 0.6242 0.6309 0.5371 -0.0009 0.0487  0.0378  121 ARG B CZ  
4485 N NH1 . ARG B 141 ? 0.6254 0.6573 0.5216 0.0136  0.0551  0.0864  121 ARG B NH1 
4486 N NH2 . ARG B 141 ? 0.6518 0.6545 0.5882 -0.0153 0.0441  0.0258  121 ARG B NH2 
4500 N N   . ASN B 142 ? 0.1841 0.2078 0.2117 0.0213  -0.0037 0.0280  122 ASN B N   
4501 C CA  . ASN B 142 ? 0.2103 0.1884 0.1743 0.0154  -0.0126 0.0042  122 ASN B CA  
4502 C C   . ASN B 142 ? 0.2063 0.1919 0.1774 0.0068  -0.0124 -0.0040 122 ASN B C   
4503 O O   . ASN B 142 ? 0.1962 0.2009 0.1959 0.0056  -0.0108 -0.0180 122 ASN B O   
4504 C CB  . ASN B 142 ? 0.2642 0.2125 0.1715 0.0218  -0.0150 -0.0251 122 ASN B CB  
4505 C CG  . ASN B 142 ? 0.2568 0.1861 0.2271 0.0422  -0.0288 -0.0273 122 ASN B CG  
4506 O OD1 . ASN B 142 ? 0.2213 0.2103 0.2550 0.0266  -0.0372 -0.0091 122 ASN B OD1 
4507 N ND2 . ASN B 142 ? 0.2594 0.1758 0.2229 0.0345  -0.0386 -0.0114 122 ASN B ND2 
4514 N N   . HIS B 143 ? 0.1977 0.1862 0.1955 0.0132  -0.0050 -0.0064 123 HIS B N   
4515 C CA  . HIS B 143 ? 0.1975 0.1856 0.1724 0.0114  -0.0023 -0.0166 123 HIS B CA  
4516 C C   . HIS B 143 ? 0.1865 0.1807 0.1481 -0.0002 -0.0078 -0.0423 123 HIS B C   
4517 O O   . HIS B 143 ? 0.2018 0.1888 0.1735 -0.0126 0.0132  -0.0329 123 HIS B O   
4518 C CB  . HIS B 143 ? 0.1836 0.1862 0.1995 0.0147  0.0094  0.0106  123 HIS B CB  
4519 C CG  . HIS B 143 ? 0.1723 0.2144 0.2120 0.0007  0.0155  -0.0065 123 HIS B CG  
4520 N ND1 . HIS B 143 ? 0.1983 0.2112 0.2230 0.0100  -0.0213 0.0111  123 HIS B ND1 
4521 C CD2 . HIS B 143 ? 0.1980 0.2359 0.2445 0.0033  0.0203  0.0114  123 HIS B CD2 
4522 C CE1 . HIS B 143 ? 0.2129 0.1960 0.2567 -0.0020 -0.0282 0.0176  123 HIS B CE1 
4523 N NE2 . HIS B 143 ? 0.2132 0.2014 0.2630 0.0105  -0.0021 -0.0031 123 HIS B NE2 
4531 N N   . PHE B 144 ? 0.1980 0.1710 0.1576 0.0089  -0.0116 -0.0296 124 PHE B N   
4532 C CA  . PHE B 144 ? 0.1705 0.1764 0.1460 0.0070  -0.0116 -0.0113 124 PHE B CA  
4533 C C   . PHE B 144 ? 0.1688 0.1739 0.1564 0.0015  0.0192  -0.0127 124 PHE B C   
4534 O O   . PHE B 144 ? 0.2133 0.1701 0.1607 0.0166  0.0336  -0.0282 124 PHE B O   
4535 C CB  . PHE B 144 ? 0.1779 0.1993 0.1643 0.0005  -0.0094 -0.0102 124 PHE B CB  
4536 C CG  . PHE B 144 ? 0.1487 0.2090 0.1971 0.0168  -0.0162 -0.0215 124 PHE B CG  
4537 C CD1 . PHE B 144 ? 0.1707 0.2375 0.2223 0.0239  -0.0334 -0.0320 124 PHE B CD1 
4538 C CD2 . PHE B 144 ? 0.1696 0.2116 0.2435 0.0214  -0.0026 -0.0372 124 PHE B CD2 
4539 C CE1 . PHE B 144 ? 0.1962 0.2337 0.2535 0.0304  -0.0294 -0.0220 124 PHE B CE1 
4540 C CE2 . PHE B 144 ? 0.1712 0.2392 0.2711 0.0219  -0.0225 -0.0599 124 PHE B CE2 
4541 C CZ  . PHE B 144 ? 0.1694 0.2346 0.2712 0.0196  -0.0297 -0.0416 124 PHE B CZ  
4551 N N   . LEU B 145 ? 0.1641 0.1615 0.1640 0.0056  0.0156  -0.0127 125 LEU B N   
4552 C CA  . LEU B 145 ? 0.1596 0.1660 0.1566 0.0085  0.0260  -0.0140 125 LEU B CA  
4553 C C   . LEU B 145 ? 0.1493 0.1612 0.1850 -0.0084 0.0204  -0.0136 125 LEU B C   
4554 O O   . LEU B 145 ? 0.1640 0.1644 0.2348 -0.0131 0.0424  -0.0416 125 LEU B O   
4555 C CB  . LEU B 145 ? 0.1527 0.2330 0.1897 0.0182  0.0036  -0.0094 125 LEU B CB  
4556 C CG  . LEU B 145 ? 0.1873 0.2902 0.2199 0.0118  -0.0118 -0.0262 125 LEU B CG  
4557 C CD1 . LEU B 145 ? 0.2077 0.2699 0.2615 -0.0219 -0.0102 -0.0195 125 LEU B CD1 
4558 C CD2 . LEU B 145 ? 0.1762 0.3672 0.2265 0.0245  -0.0190 -0.0366 125 LEU B CD2 
4570 N N   A HIS B 146 ? 0.1611 0.1520 0.1974 -0.0171 0.0249  -0.0082 126 HIS B N   
4571 N N   B HIS B 146 ? 0.1615 0.1526 0.1974 -0.0172 0.0248  -0.0081 126 HIS B N   
4572 C CA  A HIS B 146 ? 0.1644 0.1705 0.1955 -0.0068 0.0245  0.0079  126 HIS B CA  
4573 C CA  B HIS B 146 ? 0.1644 0.1704 0.1955 -0.0068 0.0242  0.0079  126 HIS B CA  
4574 C C   A HIS B 146 ? 0.1619 0.1579 0.1732 -0.0098 0.0455  -0.0170 126 HIS B C   
4575 C C   B HIS B 146 ? 0.1623 0.1583 0.1734 -0.0096 0.0452  -0.0169 126 HIS B C   
4576 O O   A HIS B 146 ? 0.1840 0.1690 0.1823 0.0152  0.0297  -0.0264 126 HIS B O   
4577 O O   B HIS B 146 ? 0.1841 0.1693 0.1822 0.0149  0.0300  -0.0261 126 HIS B O   
4578 C CB  A HIS B 146 ? 0.1516 0.1839 0.1961 -0.0006 0.0043  0.0160  126 HIS B CB  
4579 C CB  B HIS B 146 ? 0.1520 0.1842 0.1962 -0.0007 0.0043  0.0160  126 HIS B CB  
4580 C CG  A HIS B 146 ? 0.1610 0.2138 0.1723 0.0035  0.0044  0.0015  126 HIS B CG  
4581 C CG  B HIS B 146 ? 0.1615 0.2142 0.1726 0.0034  0.0047  0.0018  126 HIS B CG  
4582 N ND1 A HIS B 146 ? 0.1694 0.2540 0.2206 0.0234  0.0195  0.0292  126 HIS B ND1 
4583 N ND1 B HIS B 146 ? 0.1708 0.2542 0.2206 0.0233  0.0189  0.0290  126 HIS B ND1 
4584 C CD2 A HIS B 146 ? 0.2150 0.2270 0.2176 0.0150  0.0048  -0.0018 126 HIS B CD2 
4585 C CD2 B HIS B 146 ? 0.2158 0.2271 0.2174 0.0154  0.0051  -0.0018 126 HIS B CD2 
4586 C CE1 A HIS B 146 ? 0.1955 0.2737 0.2138 0.0148  0.0100  0.0344  126 HIS B CE1 
4587 C CE1 B HIS B 146 ? 0.1957 0.2733 0.2137 0.0157  0.0100  0.0344  126 HIS B CE1 
4588 N NE2 A HIS B 146 ? 0.2114 0.2406 0.2221 0.0066  -0.0064 0.0160  126 HIS B NE2 
4589 N NE2 B HIS B 146 ? 0.2114 0.2406 0.2220 0.0068  -0.0066 0.0162  126 HIS B NE2 
4604 N N   . SER B 147 ? 0.1539 0.1348 0.1894 -0.0020 0.0304  -0.0221 127 SER B N   
4605 C CA  . SER B 147 ? 0.1512 0.1428 0.2109 -0.0063 0.0354  -0.0050 127 SER B CA  
4606 C C   . SER B 147 ? 0.1537 0.1444 0.2082 0.0074  0.0189  -0.0047 127 SER B C   
4607 O O   . SER B 147 ? 0.1446 0.1456 0.2226 -0.0035 0.0259  -0.0040 127 SER B O   
4608 C CB  . SER B 147 ? 0.1567 0.1683 0.1920 -0.0085 0.0158  0.0082  127 SER B CB  
4609 O OG  . SER B 147 ? 0.1538 0.1771 0.2175 -0.0071 0.0164  0.0287  127 SER B OG  
4616 N N   . PHE B 148 ? 0.1385 0.1564 0.2273 -0.0034 0.0167  0.0111  128 PHE B N   
4617 C CA  . PHE B 148 ? 0.1519 0.1473 0.2298 -0.0046 0.0271  -0.0054 128 PHE B CA  
4618 C C   . PHE B 148 ? 0.1371 0.1529 0.2392 -0.0006 0.0360  -0.0103 128 PHE B C   
4619 O O   . PHE B 148 ? 0.1545 0.1675 0.2672 -0.0087 0.0538  -0.0034 128 PHE B O   
4620 C CB  . PHE B 148 ? 0.1701 0.1674 0.2319 -0.0261 0.0445  -0.0228 128 PHE B CB  
4621 C CG  . PHE B 148 ? 0.1646 0.1655 0.2144 -0.0038 0.0208  -0.0066 128 PHE B CG  
4622 C CD1 . PHE B 148 ? 0.1657 0.1695 0.2109 -0.0149 0.0213  -0.0126 128 PHE B CD1 
4623 C CD2 . PHE B 148 ? 0.1497 0.2014 0.2090 -0.0014 0.0297  0.0035  128 PHE B CD2 
4624 C CE1 . PHE B 148 ? 0.1748 0.1990 0.2106 -0.0100 0.0189  -0.0470 128 PHE B CE1 
4625 C CE2 . PHE B 148 ? 0.1489 0.2069 0.2087 0.0026  0.0138  -0.0028 128 PHE B CE2 
4626 C CZ  . PHE B 148 ? 0.1790 0.1989 0.2116 -0.0085 0.0156  -0.0059 128 PHE B CZ  
4636 N N   . ARG B 149 ? 0.1511 0.1710 0.2400 -0.0056 0.0411  -0.0035 129 ARG B N   
4637 C CA  . ARG B 149 ? 0.1518 0.1943 0.2447 -0.0081 0.0309  0.0232  129 ARG B CA  
4638 C C   . ARG B 149 ? 0.1453 0.1815 0.2514 0.0053  0.0264  0.0214  129 ARG B C   
4639 O O   . ARG B 149 ? 0.1541 0.1683 0.2769 -0.0121 0.0230  0.0147  129 ARG B O   
4640 C CB  . ARG B 149 ? 0.1751 0.1999 0.2446 -0.0069 0.0117  0.0341  129 ARG B CB  
4641 C CG  . ARG B 149 ? 0.1702 0.2104 0.2441 -0.0261 0.0160  0.0440  129 ARG B CG  
4642 C CD  . ARG B 149 ? 0.1863 0.2381 0.2481 -0.0172 0.0186  0.0378  129 ARG B CD  
4643 N NE  . ARG B 149 ? 0.2131 0.2665 0.2545 -0.0227 0.0172  0.0485  129 ARG B NE  
4644 C CZ  . ARG B 149 ? 0.2862 0.2977 0.2705 -0.0358 0.0054  0.0346  129 ARG B CZ  
4645 N NH1 . ARG B 149 ? 0.3594 0.3229 0.2823 -0.0217 -0.0238 0.0165  129 ARG B NH1 
4646 N NH2 . ARG B 149 ? 0.3116 0.3393 0.2922 -0.0070 0.0131  0.0625  129 ARG B NH2 
4660 N N   . PHE B 150 ? 0.1536 0.1702 0.2962 -0.0168 0.0189  0.0397  130 PHE B N   
4661 C CA  . PHE B 150 ? 0.1525 0.1672 0.3003 -0.0174 0.0286  0.0326  130 PHE B CA  
4662 C C   . PHE B 150 ? 0.1705 0.2012 0.3022 -0.0311 0.0304  0.0204  130 PHE B C   
4663 O O   . PHE B 150 ? 0.1924 0.2401 0.3004 -0.0319 0.0415  0.0402  130 PHE B O   
4664 C CB  . PHE B 150 ? 0.1716 0.1451 0.3022 -0.0154 0.0238  -0.0021 130 PHE B CB  
4665 C CG  . PHE B 150 ? 0.1898 0.1725 0.3053 -0.0100 0.0435  0.0149  130 PHE B CG  
4666 C CD1 . PHE B 150 ? 0.2068 0.1725 0.3215 -0.0165 0.0389  -0.0071 130 PHE B CD1 
4667 C CD2 . PHE B 150 ? 0.1985 0.1987 0.2846 0.0026  0.0586  -0.0047 130 PHE B CD2 
4668 C CE1 . PHE B 150 ? 0.2199 0.1814 0.3112 -0.0065 0.0496  -0.0436 130 PHE B CE1 
4669 C CE2 . PHE B 150 ? 0.2248 0.2088 0.2990 -0.0075 0.0642  -0.0046 130 PHE B CE2 
4670 C CZ  . PHE B 150 ? 0.2514 0.1812 0.3131 -0.0110 0.0609  -0.0279 130 PHE B CZ  
4680 N N   . GLU B 151 ? 0.1731 0.2190 0.3023 -0.0330 0.0378  0.0432  131 GLU B N   
4681 C CA  . GLU B 151 ? 0.2050 0.2148 0.2823 -0.0307 0.0510  0.0463  131 GLU B CA  
4682 C C   . GLU B 151 ? 0.1846 0.2063 0.3277 -0.0352 0.0525  0.0328  131 GLU B C   
4683 O O   . GLU B 151 ? 0.1935 0.2042 0.3476 -0.0209 0.0443  0.0178  131 GLU B O   
4684 C CB  . GLU B 151 ? 0.2607 0.2938 0.2924 -0.0357 0.0554  0.0523  131 GLU B CB  
4685 C CG  . GLU B 151 ? 0.3407 0.3833 0.3578 -0.0361 0.0554  0.0472  131 GLU B CG  
4686 C CD  . GLU B 151 ? 0.4227 0.5253 0.4392 -0.0201 0.0577  0.0245  131 GLU B CD  
4687 O OE1 . GLU B 151 ? 0.4761 0.5614 0.4543 -0.0152 0.0522  0.0124  131 GLU B OE1 
4688 O OE2 . GLU B 151 ? 0.4718 0.6162 0.4990 -0.0039 0.0490  0.0228  131 GLU B OE2 
4695 N N   . ASN B 152 ? 0.2183 0.2244 0.3369 -0.0489 0.0357  0.0389  132 ASN B N   
4696 C CA  . ASN B 152 ? 0.2298 0.2259 0.3571 -0.0535 0.0335  0.0259  132 ASN B CA  
4697 C C   . ASN B 152 ? 0.2295 0.2148 0.3531 -0.0458 0.0047  0.0431  132 ASN B C   
4698 O O   . ASN B 152 ? 0.2117 0.2796 0.3670 -0.0354 0.0085  0.0175  132 ASN B O   
4699 C CB  . ASN B 152 ? 0.2258 0.2646 0.4088 -0.0663 0.0310  0.0434  132 ASN B CB  
4700 C CG  . ASN B 152 ? 0.2292 0.3063 0.4488 -0.0646 0.0406  0.0306  132 ASN B CG  
4701 O OD1 . ASN B 152 ? 0.2641 0.2913 0.4896 -0.0578 0.0402  0.0248  132 ASN B OD1 
4702 N ND2 . ASN B 152 ? 0.2008 0.3624 0.4438 -0.0560 0.0412  0.0242  132 ASN B ND2 
4709 N N   . GLY B 153 ? 0.2620 0.1989 0.3278 -0.0222 0.0397  0.0393  133 GLY B N   
4710 C CA  . GLY B 153 ? 0.2399 0.2031 0.3458 -0.0165 0.0392  0.0290  133 GLY B CA  
4711 C C   . GLY B 153 ? 0.1866 0.1897 0.3184 -0.0144 0.0167  0.0080  133 GLY B C   
4712 O O   . GLY B 153 ? 0.1756 0.1928 0.3252 -0.0101 0.0071  -0.0162 133 GLY B O   
4716 N N   . LEU B 154 ? 0.1748 0.1813 0.2942 -0.0370 0.0451  -0.0069 134 LEU B N   
4717 C CA  . LEU B 154 ? 0.1515 0.1645 0.2998 -0.0291 0.0197  -0.0134 134 LEU B CA  
4718 C C   . LEU B 154 ? 0.1636 0.1854 0.2979 -0.0242 0.0200  -0.0076 134 LEU B C   
4719 O O   . LEU B 154 ? 0.1715 0.2022 0.2742 -0.0233 0.0395  0.0190  134 LEU B O   
4720 C CB  . LEU B 154 ? 0.1685 0.1785 0.3249 -0.0239 0.0114  -0.0105 134 LEU B CB  
4721 C CG  . LEU B 154 ? 0.1756 0.1973 0.3575 -0.0308 0.0070  0.0013  134 LEU B CG  
4722 C CD1 . LEU B 154 ? 0.1659 0.2584 0.4090 -0.0232 0.0160  -0.0110 134 LEU B CD1 
4723 C CD2 . LEU B 154 ? 0.2094 0.2127 0.3361 -0.0513 -0.0350 -0.0162 134 LEU B CD2 
4735 N N   . ILE B 155 ? 0.1456 0.1766 0.2964 -0.0284 0.0257  -0.0067 135 ILE B N   
4736 C CA  . ILE B 155 ? 0.1498 0.1599 0.2825 -0.0167 0.0337  -0.0149 135 ILE B CA  
4737 C C   . ILE B 155 ? 0.1565 0.1682 0.2857 -0.0102 0.0346  -0.0043 135 ILE B C   
4738 O O   . ILE B 155 ? 0.1406 0.2092 0.2944 -0.0085 0.0354  0.0143  135 ILE B O   
4739 C CB  . ILE B 155 ? 0.1505 0.1614 0.2601 -0.0213 0.0208  -0.0118 135 ILE B CB  
4740 C CG1 . ILE B 155 ? 0.1708 0.1651 0.2871 -0.0222 0.0006  -0.0223 135 ILE B CG1 
4741 C CG2 . ILE B 155 ? 0.1529 0.1689 0.2839 -0.0027 0.0349  -0.0020 135 ILE B CG2 
4742 C CD1 . ILE B 155 ? 0.1579 0.1881 0.2872 0.0060  0.0152  0.0057  135 ILE B CD1 
4754 N N   . LYS B 156 ? 0.1508 0.1940 0.2724 -0.0186 0.0431  -0.0009 136 LYS B N   
4755 C CA  . LYS B 156 ? 0.1695 0.1856 0.2659 -0.0271 0.0542  0.0206  136 LYS B CA  
4756 C C   . LYS B 156 ? 0.1526 0.1875 0.2522 -0.0138 0.0599  0.0207  136 LYS B C   
4757 O O   . LYS B 156 ? 0.1751 0.2182 0.2747 -0.0017 0.0708  0.0070  136 LYS B O   
4758 C CB  . LYS B 156 ? 0.2627 0.2164 0.2929 -0.0446 0.0605  0.0174  136 LYS B CB  
4759 C CG  . LYS B 156 ? 0.3138 0.3341 0.3308 -0.0026 0.0605  -0.0084 136 LYS B CG  
4760 C CD  . LYS B 156 ? 0.3686 0.4579 0.3484 -0.0290 0.0841  -0.0301 136 LYS B CD  
4761 C CE  . LYS B 156 ? 0.4419 0.5738 0.4128 -0.0288 0.1039  -0.0354 136 LYS B CE  
4762 N NZ  . LYS B 156 ? 0.4757 0.6517 0.4755 -0.0209 0.0912  -0.0294 136 LYS B NZ  
4776 N N   . GLU B 157 ? 0.1341 0.1912 0.2425 -0.0120 0.0498  0.0026  137 GLU B N   
4777 C CA  . GLU B 157 ? 0.1589 0.1862 0.2324 -0.0153 0.0590  -0.0004 137 GLU B CA  
4778 C C   . GLU B 157 ? 0.1513 0.1641 0.2367 -0.0163 0.0509  -0.0015 137 GLU B C   
4779 O O   . GLU B 157 ? 0.1487 0.1774 0.2319 0.0027  0.0479  0.0088  137 GLU B O   
4780 C CB  . GLU B 157 ? 0.1985 0.2181 0.2272 -0.0354 0.0308  0.0028  137 GLU B CB  
4781 C CG  . GLU B 157 ? 0.2026 0.2470 0.2189 -0.0303 0.0309  -0.0187 137 GLU B CG  
4782 C CD  . GLU B 157 ? 0.2252 0.2922 0.2268 -0.0410 0.0254  -0.0426 137 GLU B CD  
4783 O OE1 . GLU B 157 ? 0.2266 0.2571 0.2287 -0.0233 0.0263  -0.0090 137 GLU B OE1 
4784 O OE2 . GLU B 157 ? 0.2821 0.3525 0.2463 -0.0111 0.0059  -0.0430 137 GLU B OE2 
4791 N N   . GLN B 158 ? 0.1549 0.1538 0.2398 -0.0022 0.0493  0.0051  138 GLN B N   
4792 C CA  . GLN B 158 ? 0.1469 0.1704 0.2259 -0.0132 0.0325  -0.0117 138 GLN B CA  
4793 C C   . GLN B 158 ? 0.1238 0.1629 0.2193 0.0047  0.0305  -0.0055 138 GLN B C   
4794 O O   . GLN B 158 ? 0.1449 0.1719 0.2405 -0.0021 0.0402  -0.0243 138 GLN B O   
4795 C CB  . GLN B 158 ? 0.1522 0.1786 0.2470 -0.0298 0.0305  -0.0149 138 GLN B CB  
4796 C CG  . GLN B 158 ? 0.1627 0.2035 0.2544 -0.0148 0.0371  -0.0118 138 GLN B CG  
4797 C CD  . GLN B 158 ? 0.1840 0.2310 0.2789 -0.0130 0.0276  -0.0110 138 GLN B CD  
4798 O OE1 . GLN B 158 ? 0.2166 0.2158 0.2702 -0.0040 0.0498  -0.0030 138 GLN B OE1 
4799 N NE2 . GLN B 158 ? 0.1883 0.2537 0.3210 0.0061  0.0226  -0.0024 138 GLN B NE2 
4808 N N   . ARG B 159 ? 0.1263 0.1663 0.2297 -0.0057 0.0356  -0.0099 139 ARG B N   
4809 C CA  . ARG B 159 ? 0.1631 0.1420 0.2311 -0.0170 0.0242  -0.0036 139 ARG B CA  
4810 C C   . ARG B 159 ? 0.1485 0.1337 0.2237 -0.0071 0.0470  0.0067  139 ARG B C   
4811 O O   . ARG B 159 ? 0.1790 0.1489 0.2344 0.0058  0.0693  -0.0170 139 ARG B O   
4812 C CB  . ARG B 159 ? 0.1596 0.1687 0.2228 -0.0087 0.0243  -0.0169 139 ARG B CB  
4813 C CG  . ARG B 159 ? 0.1531 0.1834 0.2164 0.0122  0.0487  0.0024  139 ARG B CG  
4814 C CD  . ARG B 159 ? 0.1638 0.2036 0.2103 0.0050  0.0317  0.0056  139 ARG B CD  
4815 N NE  . ARG B 159 ? 0.1537 0.1862 0.2189 -0.0143 0.0251  -0.0135 139 ARG B NE  
4816 C CZ  . ARG B 159 ? 0.1594 0.1875 0.2124 -0.0252 0.0241  -0.0020 139 ARG B CZ  
4817 N NH1 . ARG B 159 ? 0.1763 0.2133 0.1960 -0.0227 0.0158  0.0244  139 ARG B NH1 
4818 N NH2 . ARG B 159 ? 0.1715 0.1896 0.1912 -0.0197 0.0153  0.0146  139 ARG B NH2 
4832 N N   B GLU B 160 ? 0.1729 0.1571 0.2266 -0.0105 0.0383  0.0032  140 GLU B N   
4833 N N   C GLU B 160 ? 0.1336 0.1484 0.2156 -0.0060 0.0379  -0.0063 140 GLU B N   
4834 C CA  B GLU B 160 ? 0.2033 0.1903 0.2364 -0.0190 0.0268  -0.0077 140 GLU B CA  
4835 C CA  C GLU B 160 ? 0.1518 0.1835 0.2240 -0.0289 0.0148  -0.0013 140 GLU B CA  
4836 C C   B GLU B 160 ? 0.1854 0.1665 0.2192 -0.0121 0.0287  -0.0064 140 GLU B C   
4837 C C   C GLU B 160 ? 0.1518 0.1486 0.2224 0.0017  0.0256  0.0081  140 GLU B C   
4838 O O   B GLU B 160 ? 0.1871 0.1685 0.2088 -0.0175 0.0306  -0.0112 140 GLU B O   
4839 O O   C GLU B 160 ? 0.1430 0.1675 0.2252 0.0124  0.0474  -0.0058 140 GLU B O   
4840 C CB  B GLU B 160 ? 0.2488 0.2347 0.2741 -0.0215 0.0222  -0.0177 140 GLU B CB  
4841 C CB  C GLU B 160 ? 0.1893 0.1977 0.2648 -0.0428 -0.0145 -0.0063 140 GLU B CB  
4842 C CG  B GLU B 160 ? 0.2855 0.2859 0.3101 -0.0271 0.0146  -0.0253 140 GLU B CG  
4843 C CG  C GLU B 160 ? 0.2188 0.2089 0.2936 -0.0045 -0.0054 -0.0332 140 GLU B CG  
4844 C CD  B GLU B 160 ? 0.3173 0.3236 0.3424 -0.0307 0.0108  -0.0344 140 GLU B CD  
4845 C CD  C GLU B 160 ? 0.2661 0.2101 0.3460 -0.0105 -0.0096 0.0116  140 GLU B CD  
4846 O OE1 B GLU B 160 ? 0.3167 0.3377 0.3499 -0.0342 0.0077  -0.0369 140 GLU B OE1 
4847 O OE1 C GLU B 160 ? 0.2464 0.2084 0.3376 0.0174  0.0308  -0.0047 140 GLU B OE1 
4848 O OE2 B GLU B 160 ? 0.3281 0.3382 0.3546 -0.0227 0.0120  -0.0322 140 GLU B OE2 
4849 O OE2 C GLU B 160 ? 0.3219 0.1946 0.4161 -0.0156 -0.0272 0.0008  140 GLU B OE2 
4862 N N   . PHE B 161 ? 0.1629 0.1410 0.2103 -0.0070 0.0310  -0.0172 141 PHE B N   
4863 C CA  . PHE B 161 ? 0.1571 0.1602 0.2014 -0.0226 0.0203  -0.0091 141 PHE B CA  
4864 C C   . PHE B 161 ? 0.1720 0.1628 0.1671 -0.0149 0.0205  -0.0234 141 PHE B C   
4865 O O   . PHE B 161 ? 0.2193 0.1749 0.1796 -0.0218 0.0386  -0.0265 141 PHE B O   
4866 C CB  . PHE B 161 ? 0.1477 0.1630 0.2144 0.0068  0.0178  -0.0069 141 PHE B CB  
4867 C CG  . PHE B 161 ? 0.1513 0.1667 0.2228 0.0010  0.0106  0.0163  141 PHE B CG  
4868 C CD1 . PHE B 161 ? 0.1661 0.1820 0.2343 0.0152  0.0217  0.0101  141 PHE B CD1 
4869 C CD2 . PHE B 161 ? 0.1786 0.1837 0.2205 0.0020  -0.0128 0.0302  141 PHE B CD2 
4870 C CE1 . PHE B 161 ? 0.1532 0.2006 0.2308 0.0106  0.0106  0.0338  141 PHE B CE1 
4871 C CE2 . PHE B 161 ? 0.1947 0.2026 0.2285 0.0192  -0.0005 0.0457  141 PHE B CE2 
4872 C CZ  . PHE B 161 ? 0.1714 0.2151 0.2244 0.0080  0.0151  0.0438  141 PHE B CZ  
4883 N N   . MET B 162 ? 0.1801 0.1679 0.1526 -0.0100 0.0291  -0.0260 142 MET B N   
4884 C CA  . MET B 162 ? 0.1893 0.1619 0.1678 0.0243  0.0253  -0.0065 142 MET B CA  
4885 C C   . MET B 162 ? 0.2048 0.1954 0.1489 -0.0125 0.0128  -0.0145 142 MET B C   
4886 O O   . MET B 162 ? 0.2271 0.1880 0.1809 -0.0393 0.0130  -0.0010 142 MET B O   
4887 C CB  . MET B 162 ? 0.1843 0.1717 0.1920 0.0038  0.0147  0.0130  142 MET B CB  
4888 C CG  . MET B 162 ? 0.1748 0.1930 0.2291 0.0299  -0.0038 0.0102  142 MET B CG  
4889 S SD  . MET B 162 ? 0.1994 0.2115 0.3051 -0.0062 0.0315  -0.0472 142 MET B SD  
4890 C CE  . MET B 162 ? 0.1960 0.1785 0.2539 0.0259  0.0305  -0.0117 142 MET B CE  
4900 N N   . ASN B 163 ? 0.1989 0.1711 0.1769 -0.0014 0.0398  -0.0015 143 ASN B N   
4901 C CA  . ASN B 163 ? 0.1854 0.1584 0.1790 0.0075  0.0356  0.0047  143 ASN B CA  
4902 C C   . ASN B 163 ? 0.1735 0.1848 0.1728 -0.0115 0.0103  -0.0016 143 ASN B C   
4903 O O   . ASN B 163 ? 0.1649 0.1883 0.1896 -0.0115 0.0060  0.0094  143 ASN B O   
4904 C CB  . ASN B 163 ? 0.1803 0.1909 0.2052 -0.0073 0.0366  -0.0150 143 ASN B CB  
4905 C CG  . ASN B 163 ? 0.1774 0.1835 0.2334 -0.0068 0.0378  -0.0121 143 ASN B CG  
4906 O OD1 . ASN B 163 ? 0.1796 0.1806 0.2171 -0.0031 0.0048  0.0101  143 ASN B OD1 
4907 N ND2 . ASN B 163 ? 0.1788 0.2456 0.3001 -0.0259 0.0659  -0.0284 143 ASN B ND2 
4914 N N   . PRO B 164 ? 0.1839 0.1663 0.1686 -0.0133 0.0000  0.0186  144 PRO B N   
4915 C CA  . PRO B 164 ? 0.1689 0.1883 0.1798 0.0087  0.0105  0.0246  144 PRO B CA  
4916 C C   . PRO B 164 ? 0.1700 0.1480 0.2088 0.0171  0.0197  0.0060  144 PRO B C   
4917 O O   . PRO B 164 ? 0.1871 0.1642 0.2466 0.0226  0.0270  0.0136  144 PRO B O   
4918 C CB  . PRO B 164 ? 0.2155 0.1960 0.2011 0.0203  0.0284  0.0101  144 PRO B CB  
4919 C CG  . PRO B 164 ? 0.2001 0.2047 0.2021 0.0138  0.0218  -0.0074 144 PRO B CG  
4920 C CD  . PRO B 164 ? 0.1803 0.1937 0.1612 -0.0102 0.0119  0.0116  144 PRO B CD  
4928 N N   . CYS B 165 ? 0.1645 0.1644 0.2235 0.0040  0.0191  0.0193  145 CYS B N   
4929 C CA  . CYS B 165 ? 0.1847 0.1806 0.2338 0.0081  0.0253  0.0181  145 CYS B CA  
4930 C C   . CYS B 165 ? 0.1942 0.1955 0.2272 0.0143  0.0297  0.0089  145 CYS B C   
4931 O O   . CYS B 165 ? 0.2020 0.2052 0.2707 0.0251  0.0244  0.0469  145 CYS B O   
4932 C CB  . CYS B 165 ? 0.1951 0.1919 0.2346 -0.0021 0.0085  0.0298  145 CYS B CB  
4933 S SG  . CYS B 165 ? 0.2043 0.2206 0.2985 -0.0251 -0.0008 0.0222  145 CYS B SG  
4939 N N   . GLU B 166 ? 0.1932 0.2001 0.2129 0.0255  0.0296  0.0173  146 GLU B N   
4940 C CA  . GLU B 166 ? 0.1958 0.1964 0.2316 0.0218  0.0173  0.0265  146 GLU B CA  
4941 C C   . GLU B 166 ? 0.2015 0.2083 0.2118 0.0395  0.0017  0.0276  146 GLU B C   
4942 O O   . GLU B 166 ? 0.2122 0.2673 0.2450 0.0521  0.0123  0.0570  146 GLU B O   
4943 C CB  . GLU B 166 ? 0.1948 0.2312 0.2910 0.0155  0.0643  0.0397  146 GLU B CB  
4944 C CG  . GLU B 166 ? 0.2316 0.3369 0.3577 0.0591  0.0728  0.0346  146 GLU B CG  
4945 C CD  . GLU B 166 ? 0.2968 0.4874 0.4773 0.0700  0.0949  0.0696  146 GLU B CD  
4946 O OE1 . GLU B 166 ? 0.3536 0.4541 0.4792 0.0310  0.1212  0.1497  146 GLU B OE1 
4947 O OE2 . GLU B 166 ? 0.3251 0.6137 0.5815 0.0275  0.0467  0.0356  146 GLU B OE2 
4954 N N   . GLN B 167 ? 0.1897 0.1871 0.2129 0.0266  0.0191  0.0224  147 GLN B N   
4955 C CA  . GLN B 167 ? 0.1938 0.1949 0.2137 0.0250  0.0044  0.0382  147 GLN B CA  
4956 C C   . GLN B 167 ? 0.1723 0.1843 0.2336 0.0247  0.0063  0.0311  147 GLN B C   
4957 O O   . GLN B 167 ? 0.1791 0.1940 0.2531 0.0263  -0.0064 0.0185  147 GLN B O   
4958 C CB  . GLN B 167 ? 0.1894 0.2160 0.2152 0.0214  0.0062  0.0225  147 GLN B CB  
4959 C CG  . GLN B 167 ? 0.1938 0.2224 0.2390 0.0143  0.0021  0.0213  147 GLN B CG  
4960 C CD  . GLN B 167 ? 0.1904 0.2448 0.2550 0.0199  -0.0175 0.0283  147 GLN B CD  
4961 O OE1 . GLN B 167 ? 0.2105 0.2484 0.2837 0.0368  0.0176  0.0347  147 GLN B OE1 
4962 N NE2 . GLN B 167 ? 0.1888 0.2871 0.2915 0.0148  0.0046  0.0432  147 GLN B NE2 
4971 N N   . PHE B 168 ? 0.1708 0.1758 0.2587 0.0187  0.0116  0.0230  148 PHE B N   
4972 C CA  . PHE B 168 ? 0.1676 0.1855 0.3125 0.0053  0.0167  0.0322  148 PHE B CA  
4973 C C   . PHE B 168 ? 0.1738 0.1915 0.3110 0.0259  0.0159  0.0409  148 PHE B C   
4974 O O   . PHE B 168 ? 0.1865 0.2045 0.3308 0.0213  -0.0079 0.0705  148 PHE B O   
4975 C CB  . PHE B 168 ? 0.1793 0.1934 0.3269 -0.0010 0.0085  0.0292  148 PHE B CB  
4976 C CG  . PHE B 168 ? 0.1847 0.2411 0.2994 0.0278  0.0151  0.0086  148 PHE B CG  
4977 C CD1 . PHE B 168 ? 0.2068 0.3313 0.2608 0.0664  0.0046  0.0207  148 PHE B CD1 
4978 C CD2 . PHE B 168 ? 0.2085 0.2592 0.2905 0.0220  0.0189  -0.0218 148 PHE B CD2 
4979 C CE1 . PHE B 168 ? 0.2152 0.4352 0.2618 0.0482  0.0063  -0.0062 148 PHE B CE1 
4980 C CE2 . PHE B 168 ? 0.2078 0.3480 0.2689 0.0643  0.0248  -0.0065 148 PHE B CE2 
4981 C CZ  . PHE B 168 ? 0.2229 0.4481 0.2701 0.0601  0.0381  0.0074  148 PHE B CZ  
4991 N N   A ARG B 169 ? 0.1905 0.2137 0.2988 0.0254  0.0290  0.0460  149 ARG B N   
4992 N N   B ARG B 169 ? 0.1834 0.2055 0.3002 0.0208  0.0286  0.0474  149 ARG B N   
4993 C CA  A ARG B 169 ? 0.2254 0.2527 0.2971 0.0359  0.0363  0.0691  149 ARG B CA  
4994 C CA  B ARG B 169 ? 0.2091 0.2424 0.2968 0.0282  0.0320  0.0770  149 ARG B CA  
4995 C C   A ARG B 169 ? 0.2217 0.2563 0.2774 0.0336  0.0267  0.0696  149 ARG B C   
4996 C C   B ARG B 169 ? 0.2188 0.2486 0.2783 0.0301  0.0255  0.0727  149 ARG B C   
4997 O O   A ARG B 169 ? 0.2326 0.2756 0.2852 0.0444  0.0221  0.0977  149 ARG B O   
4998 O O   B ARG B 169 ? 0.2367 0.2672 0.2880 0.0422  0.0214  0.1010  149 ARG B O   
4999 C CB  A ARG B 169 ? 0.2523 0.3021 0.3205 0.0555  0.0500  0.0842  149 ARG B CB  
5000 C CB  B ARG B 169 ? 0.2021 0.2963 0.3163 0.0324  0.0367  0.1063  149 ARG B CB  
5001 C CG  A ARG B 169 ? 0.2896 0.3345 0.3285 0.0772  0.0662  0.0649  149 ARG B CG  
5002 C CG  B ARG B 169 ? 0.1997 0.3115 0.3165 0.0312  0.0290  0.1170  149 ARG B CG  
5003 C CD  A ARG B 169 ? 0.3257 0.3808 0.3498 0.0888  0.0658  0.0442  149 ARG B CD  
5004 C CD  B ARG B 169 ? 0.2285 0.3557 0.3405 0.0161  -0.0018 0.1137  149 ARG B CD  
5005 N NE  A ARG B 169 ? 0.3613 0.4037 0.3895 0.1027  0.0683  0.0234  149 ARG B NE  
5006 N NE  B ARG B 169 ? 0.2472 0.3705 0.3975 -0.0147 -0.0133 0.1252  149 ARG B NE  
5007 C CZ  A ARG B 169 ? 0.3552 0.4379 0.4290 0.1064  0.0676  0.0005  149 ARG B CZ  
5008 C CZ  B ARG B 169 ? 0.2550 0.4094 0.4528 -0.0165 -0.0092 0.1489  149 ARG B CZ  
5009 N NH1 A ARG B 169 ? 0.3913 0.4669 0.4549 0.0737  0.0463  0.0025  149 ARG B NH1 
5010 N NH1 B ARG B 169 ? 0.2584 0.4366 0.4647 0.0246  -0.0205 0.1936  149 ARG B NH1 
5011 N NH2 A ARG B 169 ? 0.3126 0.4240 0.4487 0.1587  0.0862  -0.0284 149 ARG B NH2 
5012 N NH2 B ARG B 169 ? 0.2344 0.3897 0.4581 -0.0517 0.0124  0.1730  149 ARG B NH2 
5039 N N   . SER B 170 ? 0.2178 0.2454 0.2668 0.0423  0.0158  0.0585  150 SER B N   
5040 C CA  . SER B 170 ? 0.2351 0.2447 0.2603 0.0438  0.0049  0.0413  150 SER B CA  
5041 C C   . SER B 170 ? 0.2367 0.2263 0.2802 0.0255  0.0161  0.0371  150 SER B C   
5042 O O   . SER B 170 ? 0.2521 0.2780 0.2924 0.0484  -0.0094 0.0457  150 SER B O   
5043 C CB  . SER B 170 ? 0.2588 0.2411 0.2460 0.0359  0.0271  0.0275  150 SER B CB  
5044 O OG  . SER B 170 ? 0.2498 0.2294 0.2865 0.0462  0.0099  0.0299  150 SER B OG  
5051 N N   . LEU B 171 ? 0.2021 0.1964 0.2887 0.0319  0.0199  0.0387  151 LEU B N   
5052 C CA  . LEU B 171 ? 0.2147 0.2015 0.3099 0.0470  0.0281  0.0436  151 LEU B CA  
5053 C C   . LEU B 171 ? 0.2203 0.2161 0.3512 0.0410  0.0139  0.0544  151 LEU B C   
5054 O O   . LEU B 171 ? 0.2373 0.2199 0.3984 0.0306  0.0074  0.0667  151 LEU B O   
5055 C CB  . LEU B 171 ? 0.2006 0.2241 0.3251 0.0193  0.0138  0.0285  151 LEU B CB  
5056 C CG  . LEU B 171 ? 0.1928 0.2211 0.3410 0.0125  0.0108  0.0029  151 LEU B CG  
5057 C CD1 . LEU B 171 ? 0.2578 0.2666 0.3435 -0.0037 0.0295  0.0035  151 LEU B CD1 
5058 C CD2 . LEU B 171 ? 0.1852 0.2275 0.3722 0.0349  -0.0043 0.0016  151 LEU B CD2 
5070 N N   . GLY B 172 ? 0.2199 0.2081 0.3549 0.0251  0.0125  0.0867  152 GLY B N   
5071 C CA  . GLY B 172 ? 0.2288 0.2284 0.3893 0.0237  0.0227  0.1050  152 GLY B CA  
5072 C C   . GLY B 172 ? 0.2381 0.2280 0.4559 0.0312  -0.0177 0.0589  152 GLY B C   
5073 O O   . GLY B 172 ? 0.2717 0.2235 0.4941 0.0052  -0.0311 0.0751  152 GLY B O   
5077 N N   . ILE B 173 ? 0.2057 0.2136 0.4540 0.0345  -0.0402 0.0618  153 ILE B N   
5078 C CA  . ILE B 173 ? 0.2029 0.2153 0.4285 0.0179  -0.0326 0.0586  153 ILE B CA  
5079 C C   . ILE B 173 ? 0.1948 0.2094 0.4327 0.0135  -0.0137 0.0563  153 ILE B C   
5080 O O   . ILE B 173 ? 0.2045 0.2160 0.4445 0.0266  -0.0049 0.0374  153 ILE B O   
5081 C CB  . ILE B 173 ? 0.2115 0.2120 0.4122 0.0030  -0.0327 0.0057  153 ILE B CB  
5082 C CG1 . ILE B 173 ? 0.1987 0.1934 0.4216 0.0264  -0.0177 0.0015  153 ILE B CG1 
5083 C CG2 . ILE B 173 ? 0.2385 0.2431 0.3854 0.0202  -0.0374 -0.0249 153 ILE B CG2 
5084 C CD1 . ILE B 173 ? 0.2163 0.2029 0.4125 0.0292  -0.0189 0.0024  153 ILE B CD1 
5096 N N   . GLU B 174 ? 0.2143 0.2407 0.4590 -0.0154 -0.0206 0.0769  154 GLU B N   
5097 C CA  . GLU B 174 ? 0.2391 0.2445 0.4770 -0.0031 -0.0182 0.0871  154 GLU B CA  
5098 C C   . GLU B 174 ? 0.2109 0.2663 0.4147 -0.0073 -0.0095 0.0608  154 GLU B C   
5099 O O   . GLU B 174 ? 0.2391 0.2553 0.4230 0.0056  -0.0075 0.0418  154 GLU B O   
5100 C CB  . GLU B 174 ? 0.2894 0.2934 0.5550 0.0133  -0.0405 0.0840  154 GLU B CB  
5101 C CG  . GLU B 174 ? 0.3720 0.3739 0.6000 0.0181  -0.0388 0.0611  154 GLU B CG  
5106 N N   . VAL B 175 ? 0.1900 0.2904 0.3837 -0.0148 -0.0115 0.0867  155 VAL B N   
5107 C CA  . VAL B 175 ? 0.2069 0.2834 0.3852 -0.0252 -0.0136 0.0854  155 VAL B CA  
5108 C C   . VAL B 175 ? 0.2150 0.3214 0.4065 0.0272  0.0085  0.0284  155 VAL B C   
5109 O O   . VAL B 175 ? 0.2135 0.3009 0.4385 -0.0121 -0.0120 0.0328  155 VAL B O   
5110 C CB  . VAL B 175 ? 0.2229 0.2694 0.4202 -0.0350 -0.0450 0.0987  155 VAL B CB  
5111 C CG1 . VAL B 175 ? 0.2622 0.2438 0.4538 -0.0233 -0.0391 0.1096  155 VAL B CG1 
5112 C CG2 . VAL B 175 ? 0.2568 0.2799 0.4893 -0.0340 -0.0943 0.0632  155 VAL B CG2 
5122 N N   . PRO B 176 ? 0.2399 0.4221 0.4364 0.0852  -0.0382 0.0025  156 PRO B N   
5123 C CA  . PRO B 176 ? 0.2660 0.4634 0.4523 0.1249  -0.0618 -0.0300 156 PRO B CA  
5124 C C   . PRO B 176 ? 0.2163 0.3759 0.4799 0.0488  -0.0427 0.0061  156 PRO B C   
5125 O O   . PRO B 176 ? 0.2180 0.3456 0.4448 0.0360  0.0148  0.0326  156 PRO B O   
5126 C CB  . PRO B 176 ? 0.3340 0.5519 0.4373 0.1551  -0.0740 -0.0602 156 PRO B CB  
5127 C CG  . PRO B 176 ? 0.3770 0.5537 0.4656 0.1021  -0.0378 -0.0334 156 PRO B CG  
5128 C CD  . PRO B 176 ? 0.2836 0.5075 0.4516 0.0971  -0.0582 0.0080  156 PRO B CD  
5136 N N   . GLU B 177 ? 0.2235 0.4018 0.5362 0.0036  -0.0732 -0.0193 157 GLU B N   
5137 C CA  . GLU B 177 ? 0.2501 0.3970 0.5603 -0.0407 -0.0598 -0.0139 157 GLU B CA  
5138 C C   . GLU B 177 ? 0.2582 0.3603 0.5280 -0.0414 -0.0681 -0.0540 157 GLU B C   
5139 O O   . GLU B 177 ? 0.3205 0.3910 0.5614 0.0059  -0.1339 -0.0815 157 GLU B O   
5140 C CB  . GLU B 177 ? 0.3083 0.4782 0.6203 -0.0644 -0.0292 0.0212  157 GLU B CB  
5141 C CG  . GLU B 177 ? 0.3579 0.5333 0.6631 -0.0554 -0.0043 0.0278  157 GLU B CG  
5146 N N   . VAL B 178 ? 0.2001 0.3361 0.4638 -0.0938 -0.0045 -0.0388 158 VAL B N   
5147 C CA  . VAL B 178 ? 0.1898 0.2958 0.4160 -0.0806 0.0284  -0.0313 158 VAL B CA  
5148 C C   . VAL B 178 ? 0.1751 0.3162 0.4155 -0.0660 0.0325  -0.0159 158 VAL B C   
5149 O O   . VAL B 178 ? 0.1939 0.4043 0.3916 -0.0642 0.0398  -0.0316 158 VAL B O   
5150 C CB  . VAL B 178 ? 0.2063 0.2779 0.4014 -0.0640 0.0452  -0.0063 158 VAL B CB  
5151 C CG1 . VAL B 178 ? 0.2653 0.2799 0.4058 -0.0375 0.0358  0.0281  158 VAL B CG1 
5152 C CG2 . VAL B 178 ? 0.2246 0.2737 0.4178 -0.0776 0.0964  -0.0380 158 VAL B CG2 
5162 N N   . ARG B 179 ? 0.1820 0.2546 0.4530 -0.0697 0.0338  0.0321  159 ARG B N   
5163 C CA  . ARG B 179 ? 0.1874 0.2277 0.4831 -0.0388 0.0233  0.0394  159 ARG B CA  
5164 C C   . ARG B 179 ? 0.1865 0.2211 0.4255 -0.0453 0.0090  0.0359  159 ARG B C   
5165 O O   . ARG B 179 ? 0.2229 0.2589 0.4145 -0.0224 0.0191  0.0356  159 ARG B O   
5166 C CB  . ARG B 179 ? 0.1841 0.2145 0.5718 -0.0364 0.0171  0.0675  159 ARG B CB  
5167 C CG  . ARG B 179 ? 0.2226 0.2124 0.6191 -0.0088 0.0246  0.0412  159 ARG B CG  
5168 C CD  . ARG B 179 ? 0.3037 0.2123 0.6522 -0.0203 0.0322  0.0205  159 ARG B CD  
5169 N NE  . ARG B 179 ? 0.3563 0.2699 0.6664 -0.0833 -0.0076 -0.0333 159 ARG B NE  
5170 C CZ  . ARG B 179 ? 0.3871 0.2733 0.6855 -0.0902 -0.0622 -0.0404 159 ARG B CZ  
5171 N NH1 . ARG B 179 ? 0.3706 0.2962 0.6812 -0.0446 -0.0613 -0.0335 159 ARG B NH1 
5172 N NH2 . ARG B 179 ? 0.4171 0.2658 0.7198 -0.1219 -0.0957 -0.0333 159 ARG B NH2 
5186 N N   . ARG B 180 ? 0.1907 0.2299 0.4090 -0.0597 -0.0265 0.0178  160 ARG B N   
5187 C CA  . ARG B 180 ? 0.1907 0.2396 0.3875 -0.0480 -0.0054 0.0359  160 ARG B CA  
5188 C C   . ARG B 180 ? 0.2037 0.2434 0.3843 -0.0756 0.0036  0.0173  160 ARG B C   
5189 O O   . ARG B 180 ? 0.2075 0.2655 0.3919 -0.0537 0.0218  0.0033  160 ARG B O   
5190 C CB  . ARG B 180 ? 0.2022 0.2934 0.4277 -0.0434 -0.0475 0.0075  160 ARG B CB  
5191 C CG  . ARG B 180 ? 0.2651 0.3224 0.4869 -0.0623 -0.0955 0.0058  160 ARG B CG  
5192 C CD  . ARG B 180 ? 0.3319 0.3203 0.4738 -0.0729 -0.1275 0.0881  160 ARG B CD  
5193 N NE  . ARG B 180 ? 0.3755 0.3480 0.4545 -0.1211 -0.1353 0.1059  160 ARG B NE  
5194 C CZ  . ARG B 180 ? 0.4175 0.4262 0.4942 -0.1115 -0.1032 0.0711  160 ARG B CZ  
5195 N NH1 . ARG B 180 ? 0.4963 0.4433 0.5088 -0.0559 -0.0574 0.0405  160 ARG B NH1 
5196 N NH2 . ARG B 180 ? 0.3753 0.4450 0.5265 -0.1400 -0.1172 0.0728  160 ARG B NH2 
5210 N N   . ASP B 181 ? 0.2117 0.2591 0.4197 -0.0916 0.0164  0.0188  161 ASP B N   
5211 C CA  . ASP B 181 ? 0.2484 0.2628 0.4580 -0.1185 0.0091  0.0278  161 ASP B CA  
5212 C C   . ASP B 181 ? 0.2226 0.2897 0.4338 -0.0922 0.0338  0.0093  161 ASP B C   
5213 O O   . ASP B 181 ? 0.2238 0.3692 0.4533 -0.1064 0.0557  0.0268  161 ASP B O   
5214 C CB  . ASP B 181 ? 0.3216 0.2968 0.5234 -0.1393 -0.0318 0.0347  161 ASP B CB  
5215 C CG  . ASP B 181 ? 0.4205 0.3805 0.5593 -0.1198 -0.0419 0.0967  161 ASP B CG  
5216 O OD1 . ASP B 181 ? 0.4159 0.3193 0.5786 -0.0581 -0.0571 0.0793  161 ASP B OD1 
5217 O OD2 . ASP B 181 ? 0.4735 0.4776 0.5518 -0.1473 -0.0345 0.1688  161 ASP B OD2 
5222 N N   . GLY B 182 ? 0.2147 0.2266 0.3794 -0.0606 0.0111  -0.0054 162 GLY B N   
5223 C CA  . GLY B 182 ? 0.2065 0.2311 0.3654 -0.0453 0.0175  -0.0237 162 GLY B CA  
5224 C C   . GLY B 182 ? 0.2211 0.2291 0.3707 -0.0302 0.0066  -0.0157 162 GLY B C   
5225 O O   . GLY B 182 ? 0.2270 0.2459 0.3962 -0.0380 0.0205  -0.0179 162 GLY B O   
5229 N N   . LEU B 183 ? 0.2455 0.2083 0.3718 -0.0460 -0.0061 -0.0328 163 LEU B N   
5230 C CA  . LEU B 183 ? 0.2663 0.2337 0.3969 -0.0399 -0.0145 -0.0305 163 LEU B CA  
5231 C C   . LEU B 183 ? 0.3159 0.2849 0.3934 -0.0207 0.0004  -0.0495 163 LEU B C   
5232 O O   . LEU B 183 ? 0.3538 0.3245 0.4099 -0.0258 0.0157  -0.0814 163 LEU B O   
5233 C CB  . LEU B 183 ? 0.2531 0.2228 0.4315 -0.0735 -0.0251 0.0089  163 LEU B CB  
5234 C CG  . LEU B 183 ? 0.2346 0.2616 0.4649 -0.0709 -0.0481 0.0559  163 LEU B CG  
5235 C CD1 . LEU B 183 ? 0.2473 0.2782 0.5310 -0.1031 -0.0866 0.0669  163 LEU B CD1 
5236 C CD2 . LEU B 183 ? 0.2368 0.2993 0.4363 -0.0181 -0.0508 0.0267  163 LEU B CD2 
5248 N N   . PRO B 184 ? 0.3209 0.2833 0.3959 -0.0271 0.0013  -0.0525 164 PRO B N   
5249 C CA  . PRO B 184 ? 0.3547 0.3160 0.4179 0.0098  0.0415  -0.0624 164 PRO B CA  
5250 C C   . PRO B 184 ? 0.3832 0.3799 0.4531 -0.0068 0.0550  -0.0829 164 PRO B C   
5251 O O   . PRO B 184 ? 0.3663 0.3921 0.4457 -0.0093 0.0442  -0.1175 164 PRO B O   
5252 C CB  . PRO B 184 ? 0.3883 0.3039 0.4055 0.0925  0.0337  -0.0562 164 PRO B CB  
5253 C CG  . PRO B 184 ? 0.3868 0.3289 0.4187 0.0828  0.0318  -0.0448 164 PRO B CG  
5254 C CD  . PRO B 184 ? 0.3422 0.3124 0.4287 0.0288  0.0240  -0.0314 164 PRO B CD  
5262 N N   . SER B 185 ? 0.4788 0.4733 0.5268 -0.0323 0.0578  -0.0601 165 SER B N   
5263 C CA  . SER B 185 ? 0.5632 0.6151 0.6150 -0.0148 0.0345  -0.0603 165 SER B CA  
5264 C C   . SER B 185 ? 0.6213 0.6866 0.6584 0.0278  0.0199  -0.0773 165 SER B C   
5265 O O   . SER B 185 ? 0.6552 0.7300 0.6815 0.0355  0.0113  -0.0875 165 SER B O   
5266 C CB  . SER B 185 ? 0.5803 0.6998 0.6682 -0.0226 0.0352  -0.0418 165 SER B CB  
5267 O OG  . SER B 185 ? 0.5882 0.7503 0.7110 -0.0393 0.0379  -0.0501 165 SER B OG  
# 
