data_8QM9
# 
_entry.id   8QM9 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8QM9         pdb_00008qm9 10.2210/pdb8qm9/pdb 
WWPDB D_1292133488 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-01-15 ? 
2 'Structure model' 1 1 2025-03-12 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
5 2 'Structure model' '_citation.title'                   
6 2 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8QM9 
_pdbx_database_status.recvd_initial_deposition_date   2023-09-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              Andrew.Woodhead@astx.com 
_pdbx_contact_author.name_first         Andrew 
_pdbx_contact_author.name_last          Woodhead 
_pdbx_contact_author.name_mi            J. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0009-0005-1604-2904 
# 
_audit_author.name               'Cleasby, A.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0003-2619-9532 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                10037 
_citation.page_last                 10037 
_citation.title                     
'Integrating fragment-based screening with targeted protein degradation and genetic rescue to explore eIF4E function.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-024-54356-1 
_citation.pdbx_database_id_PubMed   40016190 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Sharp, S.Y.'          1  ? 
primary 'Martella, M.'         2  ? 
primary 
;D'Agostino, S.
;
3  ? 
primary 'Milton, C.I.'         4  ? 
primary 'Ward, G.'             5  ? 
primary 'Woodhead, A.J.'       6  ? 
primary 'Richardson, C.J.'     7  ? 
primary 'Carr, M.G.'           8  ? 
primary 'Chiarparin, E.'       9  ? 
primary 'Cons, B.D.'           10 ? 
primary 'Coyle, J.'            11 ? 
primary 'East, C.E.'           12 ? 
primary 'Hiscock, S.D.'        13 ? 
primary 'Martinez-Fleites, C.' 14 ? 
primary 'Mortenson, P.N.'      15 ? 
primary 'Palmer, N.'           16 ? 
primary 'Pathuri, P.'          17 ? 
primary 'Powers, M.V.'         18 ? 
primary 'Saalau, S.M.'         19 ? 
primary 'St Denis, J.D.'       20 ? 
primary 'Swabey, K.'           21 ? 
primary 'Vinkovic, M.'         22 ? 
primary 'Walton, H.'           23 ? 
primary 'Williams, G.'         24 ? 
primary 'Clarke, P.A.'         25 ? 
# 
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 'Eukaryotic translation initiation factor 4E'                                                25014.445 2   ? ? ? 
? 
2 non-polymer syn 1,2-ETHANEDIOL                                                                               62.068    3   ? ? ? 
? 
3 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                                                      106.120   4   ? ? ? 
? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                         78.133    2   ? ? ? 
? 
5 non-polymer syn '(2~{R})-2-[(1~{S})-1-[4-(2-fluorophenyl)-2-(2-hydroxyethylamino)phenyl]propoxy]propan-1-ol' 347.424   2   ? ? ? 
? 
6 water       nat water                                                                                        18.015    286 ? ? ? 
? 
# 
_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       
;MHHHHHHGARIIYDRAFLMACRGGGGENLYFQGKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLS
SNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLNRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDK
IAIWTTECENREAVTHIGRVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MHHHHHHGARIIYDRAFLMACRGGGGENLYFQGKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLS
SNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLNRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDK
IAIWTTECENREAVTHIGRVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV
;
_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 1,2-ETHANEDIOL                                                                               EDO 
3 'DI(HYDROXYETHYL)ETHER'                                                                      PEG 
4 'DIMETHYL SULFOXIDE'                                                                         DMS 
5 '(2~{R})-2-[(1~{S})-1-[4-(2-fluorophenyl)-2-(2-hydroxyethylamino)phenyl]propoxy]propan-1-ol' W4K 
6 water                                                                                        HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   GLY n 
1 9   ALA n 
1 10  ARG n 
1 11  ILE n 
1 12  ILE n 
1 13  TYR n 
1 14  ASP n 
1 15  ARG n 
1 16  ALA n 
1 17  PHE n 
1 18  LEU n 
1 19  MET n 
1 20  ALA n 
1 21  CYS n 
1 22  ARG n 
1 23  GLY n 
1 24  GLY n 
1 25  GLY n 
1 26  GLY n 
1 27  GLU n 
1 28  ASN n 
1 29  LEU n 
1 30  TYR n 
1 31  PHE n 
1 32  GLN n 
1 33  GLY n 
1 34  LYS n 
1 35  HIS n 
1 36  PRO n 
1 37  LEU n 
1 38  GLN n 
1 39  ASN n 
1 40  ARG n 
1 41  TRP n 
1 42  ALA n 
1 43  LEU n 
1 44  TRP n 
1 45  PHE n 
1 46  PHE n 
1 47  LYS n 
1 48  ASN n 
1 49  ASP n 
1 50  LYS n 
1 51  SER n 
1 52  LYS n 
1 53  THR n 
1 54  TRP n 
1 55  GLN n 
1 56  ALA n 
1 57  ASN n 
1 58  LEU n 
1 59  ARG n 
1 60  LEU n 
1 61  ILE n 
1 62  SER n 
1 63  LYS n 
1 64  PHE n 
1 65  ASP n 
1 66  THR n 
1 67  VAL n 
1 68  GLU n 
1 69  ASP n 
1 70  PHE n 
1 71  TRP n 
1 72  ALA n 
1 73  LEU n 
1 74  TYR n 
1 75  ASN n 
1 76  HIS n 
1 77  ILE n 
1 78  GLN n 
1 79  LEU n 
1 80  SER n 
1 81  SER n 
1 82  ASN n 
1 83  LEU n 
1 84  MET n 
1 85  PRO n 
1 86  GLY n 
1 87  CYS n 
1 88  ASP n 
1 89  TYR n 
1 90  SER n 
1 91  LEU n 
1 92  PHE n 
1 93  LYS n 
1 94  ASP n 
1 95  GLY n 
1 96  ILE n 
1 97  GLU n 
1 98  PRO n 
1 99  MET n 
1 100 TRP n 
1 101 GLU n 
1 102 ASP n 
1 103 GLU n 
1 104 LYS n 
1 105 ASN n 
1 106 LYS n 
1 107 ARG n 
1 108 GLY n 
1 109 GLY n 
1 110 ARG n 
1 111 TRP n 
1 112 LEU n 
1 113 ILE n 
1 114 THR n 
1 115 LEU n 
1 116 ASN n 
1 117 LYS n 
1 118 GLN n 
1 119 GLN n 
1 120 ARG n 
1 121 ARG n 
1 122 SER n 
1 123 ASP n 
1 124 LEU n 
1 125 ASN n 
1 126 ARG n 
1 127 PHE n 
1 128 TRP n 
1 129 LEU n 
1 130 GLU n 
1 131 THR n 
1 132 LEU n 
1 133 LEU n 
1 134 CYS n 
1 135 LEU n 
1 136 ILE n 
1 137 GLY n 
1 138 GLU n 
1 139 SER n 
1 140 PHE n 
1 141 ASP n 
1 142 ASP n 
1 143 TYR n 
1 144 SER n 
1 145 ASP n 
1 146 ASP n 
1 147 VAL n 
1 148 CYS n 
1 149 GLY n 
1 150 ALA n 
1 151 VAL n 
1 152 VAL n 
1 153 ASN n 
1 154 VAL n 
1 155 ARG n 
1 156 ALA n 
1 157 LYS n 
1 158 GLY n 
1 159 ASP n 
1 160 LYS n 
1 161 ILE n 
1 162 ALA n 
1 163 ILE n 
1 164 TRP n 
1 165 THR n 
1 166 THR n 
1 167 GLU n 
1 168 CYS n 
1 169 GLU n 
1 170 ASN n 
1 171 ARG n 
1 172 GLU n 
1 173 ALA n 
1 174 VAL n 
1 175 THR n 
1 176 HIS n 
1 177 ILE n 
1 178 GLY n 
1 179 ARG n 
1 180 VAL n 
1 181 TYR n 
1 182 LYS n 
1 183 GLU n 
1 184 ARG n 
1 185 LEU n 
1 186 GLY n 
1 187 LEU n 
1 188 PRO n 
1 189 PRO n 
1 190 LYS n 
1 191 ILE n 
1 192 VAL n 
1 193 ILE n 
1 194 GLY n 
1 195 TYR n 
1 196 GLN n 
1 197 SER n 
1 198 HIS n 
1 199 ALA n 
1 200 ASP n 
1 201 THR n 
1 202 ALA n 
1 203 THR n 
1 204 LYS n 
1 205 SER n 
1 206 GLY n 
1 207 SER n 
1 208 THR n 
1 209 THR n 
1 210 LYS n 
1 211 ASN n 
1 212 ARG n 
1 213 PHE n 
1 214 VAL n 
1 215 VAL 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                   215 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 EIF4E 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21-CodonPlus (DE3)-RIPL' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                                      ? 
'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                                                                     ? 
'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                                   ? 
'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                              ? 
'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                                     ? 
'C3 H7 N O2 S'   121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                                         ? 
'C2 H6 O S'      78.133  
EDO non-polymer         . 1,2-ETHANEDIOL                                                                               
'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN 'L-peptide linking' y GLUTAMINE                                                                                    ? 
'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                              ? 
'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                                                                      ? 
'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                                    ? 
'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                                                                        ? 'H2 O' 
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                                   ? 
'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                                                                      ? 
'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                                                                       ? 
'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                                                                   ? 
'C5 H11 N O2 S'  149.211 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'                                                                      ? 
'C4 H10 O3'      106.120 
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 
W4K non-polymer         . '(2~{R})-2-[(1~{S})-1-[4-(2-fluorophenyl)-2-(2-hydroxyethylamino)phenyl]propoxy]propan-1-ol' ? 
'C20 H26 F N O3' 347.424 
# 
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   3   ?   ?   ?   A . n 
A 1 2   HIS 2   4   ?   ?   ?   A . n 
A 1 3   HIS 3   5   ?   ?   ?   A . n 
A 1 4   HIS 4   6   ?   ?   ?   A . n 
A 1 5   HIS 5   7   ?   ?   ?   A . n 
A 1 6   HIS 6   8   ?   ?   ?   A . n 
A 1 7   HIS 7   9   ?   ?   ?   A . n 
A 1 8   GLY 8   10  ?   ?   ?   A . n 
A 1 9   ALA 9   11  11  ALA ALA A . n 
A 1 10  ARG 10  12  12  ARG ARG A . n 
A 1 11  ILE 11  13  13  ILE ILE A . n 
A 1 12  ILE 12  14  14  ILE ILE A . n 
A 1 13  TYR 13  15  15  TYR TYR A . n 
A 1 14  ASP 14  16  16  ASP ASP A . n 
A 1 15  ARG 15  17  17  ARG ARG A . n 
A 1 16  ALA 16  18  18  ALA ALA A . n 
A 1 17  PHE 17  19  19  PHE PHE A . n 
A 1 18  LEU 18  20  20  LEU LEU A . n 
A 1 19  MET 19  21  21  MET MET A . n 
A 1 20  ALA 20  22  22  ALA ALA A . n 
A 1 21  CYS 21  23  23  CYS CYS A . n 
A 1 22  ARG 22  24  24  ARG ARG A . n 
A 1 23  GLY 23  25  25  GLY GLY A . n 
A 1 24  GLY 24  26  26  GLY GLY A . n 
A 1 25  GLY 25  27  27  GLY GLY A . n 
A 1 26  GLY 26  28  28  GLY GLY A . n 
A 1 27  GLU 27  29  29  GLU GLU A . n 
A 1 28  ASN 28  30  30  ASN ASN A . n 
A 1 29  LEU 29  31  31  LEU LEU A . n 
A 1 30  TYR 30  32  32  TYR TYR A . n 
A 1 31  PHE 31  33  33  PHE PHE A . n 
A 1 32  GLN 32  34  34  GLN GLN A . n 
A 1 33  GLY 33  35  35  GLY GLY A . n 
A 1 34  LYS 34  36  36  LYS LYS A . n 
A 1 35  HIS 35  37  37  HIS HIS A . n 
A 1 36  PRO 36  38  38  PRO PRO A . n 
A 1 37  LEU 37  39  39  LEU LEU A . n 
A 1 38  GLN 38  40  40  GLN GLN A . n 
A 1 39  ASN 39  41  41  ASN ASN A . n 
A 1 40  ARG 40  42  42  ARG ARG A . n 
A 1 41  TRP 41  43  43  TRP TRP A . n 
A 1 42  ALA 42  44  44  ALA ALA A . n 
A 1 43  LEU 43  45  45  LEU LEU A . n 
A 1 44  TRP 44  46  46  TRP TRP A . n 
A 1 45  PHE 45  47  47  PHE PHE A . n 
A 1 46  PHE 46  48  48  PHE PHE A . n 
A 1 47  LYS 47  49  49  LYS LYS A . n 
A 1 48  ASN 48  50  50  ASN ASN A . n 
A 1 49  ASP 49  51  51  ASP ASP A . n 
A 1 50  LYS 50  52  52  LYS LYS A . n 
A 1 51  SER 51  53  53  SER SER A . n 
A 1 52  LYS 52  54  54  LYS LYS A . n 
A 1 53  THR 53  55  55  THR THR A . n 
A 1 54  TRP 54  56  56  TRP TRP A . n 
A 1 55  GLN 55  57  57  GLN GLN A . n 
A 1 56  ALA 56  58  58  ALA ALA A . n 
A 1 57  ASN 57  59  59  ASN ASN A . n 
A 1 58  LEU 58  60  60  LEU LEU A . n 
A 1 59  ARG 59  61  61  ARG ARG A . n 
A 1 60  LEU 60  62  62  LEU LEU A . n 
A 1 61  ILE 61  63  63  ILE ILE A . n 
A 1 62  SER 62  64  64  SER SER A . n 
A 1 63  LYS 63  65  65  LYS LYS A . n 
A 1 64  PHE 64  66  66  PHE PHE A . n 
A 1 65  ASP 65  67  67  ASP ASP A . n 
A 1 66  THR 66  68  68  THR THR A . n 
A 1 67  VAL 67  69  69  VAL VAL A . n 
A 1 68  GLU 68  70  70  GLU GLU A . n 
A 1 69  ASP 69  71  71  ASP ASP A . n 
A 1 70  PHE 70  72  72  PHE PHE A . n 
A 1 71  TRP 71  73  73  TRP TRP A . n 
A 1 72  ALA 72  74  74  ALA ALA A . n 
A 1 73  LEU 73  75  75  LEU LEU A . n 
A 1 74  TYR 74  76  76  TYR TYR A . n 
A 1 75  ASN 75  77  77  ASN ASN A . n 
A 1 76  HIS 76  78  78  HIS HIS A . n 
A 1 77  ILE 77  79  79  ILE ILE A . n 
A 1 78  GLN 78  80  80  GLN GLN A . n 
A 1 79  LEU 79  81  81  LEU LEU A . n 
A 1 80  SER 80  82  82  SER SER A . n 
A 1 81  SER 81  83  83  SER SER A . n 
A 1 82  ASN 82  84  84  ASN ASN A . n 
A 1 83  LEU 83  85  85  LEU LEU A . n 
A 1 84  MET 84  86  86  MET MET A . n 
A 1 85  PRO 85  87  87  PRO PRO A . n 
A 1 86  GLY 86  88  88  GLY GLY A . n 
A 1 87  CYS 87  89  89  CYS CYS A . n 
A 1 88  ASP 88  90  90  ASP ASP A . n 
A 1 89  TYR 89  91  91  TYR TYR A . n 
A 1 90  SER 90  92  92  SER SER A . n 
A 1 91  LEU 91  93  93  LEU LEU A . n 
A 1 92  PHE 92  94  94  PHE PHE A . n 
A 1 93  LYS 93  95  95  LYS LYS A . n 
A 1 94  ASP 94  96  96  ASP ASP A . n 
A 1 95  GLY 95  97  97  GLY GLY A . n 
A 1 96  ILE 96  98  98  ILE ILE A . n 
A 1 97  GLU 97  99  99  GLU GLU A . n 
A 1 98  PRO 98  100 100 PRO PRO A . n 
A 1 99  MET 99  101 101 MET MET A . n 
A 1 100 TRP 100 102 102 TRP TRP A . n 
A 1 101 GLU 101 103 103 GLU GLU A . n 
A 1 102 ASP 102 104 104 ASP ASP A . n 
A 1 103 GLU 103 105 105 GLU GLU A . n 
A 1 104 LYS 104 106 106 LYS LYS A . n 
A 1 105 ASN 105 107 107 ASN ASN A . n 
A 1 106 LYS 106 108 108 LYS LYS A . n 
A 1 107 ARG 107 109 109 ARG ARG A . n 
A 1 108 GLY 108 110 110 GLY GLY A . n 
A 1 109 GLY 109 111 111 GLY GLY A . n 
A 1 110 ARG 110 112 112 ARG ARG A . n 
A 1 111 TRP 111 113 113 TRP TRP A . n 
A 1 112 LEU 112 114 114 LEU LEU A . n 
A 1 113 ILE 113 115 115 ILE ILE A . n 
A 1 114 THR 114 116 116 THR THR A . n 
A 1 115 LEU 115 117 117 LEU LEU A . n 
A 1 116 ASN 116 118 118 ASN ASN A . n 
A 1 117 LYS 117 119 119 LYS LYS A . n 
A 1 118 GLN 118 120 120 GLN GLN A . n 
A 1 119 GLN 119 121 121 GLN GLN A . n 
A 1 120 ARG 120 122 122 ARG ARG A . n 
A 1 121 ARG 121 123 123 ARG ARG A . n 
A 1 122 SER 122 124 124 SER SER A . n 
A 1 123 ASP 123 125 125 ASP ASP A . n 
A 1 124 LEU 124 126 126 LEU LEU A . n 
A 1 125 ASN 125 127 127 ASN ASN A . n 
A 1 126 ARG 126 128 128 ARG ARG A . n 
A 1 127 PHE 127 129 129 PHE PHE A . n 
A 1 128 TRP 128 130 130 TRP TRP A . n 
A 1 129 LEU 129 131 131 LEU LEU A . n 
A 1 130 GLU 130 132 132 GLU GLU A . n 
A 1 131 THR 131 133 133 THR THR A . n 
A 1 132 LEU 132 134 134 LEU LEU A . n 
A 1 133 LEU 133 135 135 LEU LEU A . n 
A 1 134 CYS 134 136 136 CYS CYS A . n 
A 1 135 LEU 135 137 137 LEU LEU A . n 
A 1 136 ILE 136 138 138 ILE ILE A . n 
A 1 137 GLY 137 139 139 GLY GLY A . n 
A 1 138 GLU 138 140 140 GLU GLU A . n 
A 1 139 SER 139 141 141 SER SER A . n 
A 1 140 PHE 140 142 142 PHE PHE A . n 
A 1 141 ASP 141 143 143 ASP ASP A . n 
A 1 142 ASP 142 144 144 ASP ASP A . n 
A 1 143 TYR 143 145 145 TYR TYR A . n 
A 1 144 SER 144 146 146 SER SER A . n 
A 1 145 ASP 145 147 147 ASP ASP A . n 
A 1 146 ASP 146 148 148 ASP ASP A . n 
A 1 147 VAL 147 149 149 VAL VAL A . n 
A 1 148 CYS 148 150 150 CYS CYS A . n 
A 1 149 GLY 149 151 151 GLY GLY A . n 
A 1 150 ALA 150 152 152 ALA ALA A . n 
A 1 151 VAL 151 153 153 VAL VAL A . n 
A 1 152 VAL 152 154 154 VAL VAL A . n 
A 1 153 ASN 153 155 155 ASN ASN A . n 
A 1 154 VAL 154 156 156 VAL VAL A . n 
A 1 155 ARG 155 157 157 ARG ARG A . n 
A 1 156 ALA 156 158 158 ALA ALA A . n 
A 1 157 LYS 157 159 159 LYS LYS A . n 
A 1 158 GLY 158 160 160 GLY GLY A . n 
A 1 159 ASP 159 161 161 ASP ASP A . n 
A 1 160 LYS 160 162 162 LYS LYS A . n 
A 1 161 ILE 161 163 163 ILE ILE A . n 
A 1 162 ALA 162 164 164 ALA ALA A . n 
A 1 163 ILE 163 165 165 ILE ILE A . n 
A 1 164 TRP 164 166 166 TRP TRP A . n 
A 1 165 THR 165 167 167 THR THR A . n 
A 1 166 THR 166 168 168 THR THR A . n 
A 1 167 GLU 167 169 169 GLU GLU A . n 
A 1 168 CYS 168 170 170 CYS CYS A . n 
A 1 169 GLU 169 171 171 GLU GLU A . n 
A 1 170 ASN 170 172 172 ASN ASN A . n 
A 1 171 ARG 171 173 173 ARG ARG A . n 
A 1 172 GLU 172 174 174 GLU GLU A . n 
A 1 173 ALA 173 175 175 ALA ALA A . n 
A 1 174 VAL 174 176 176 VAL VAL A . n 
A 1 175 THR 175 177 177 THR THR A . n 
A 1 176 HIS 176 178 178 HIS HIS A . n 
A 1 177 ILE 177 179 179 ILE ILE A . n 
A 1 178 GLY 178 180 180 GLY GLY A . n 
A 1 179 ARG 179 181 181 ARG ARG A . n 
A 1 180 VAL 180 182 182 VAL VAL A . n 
A 1 181 TYR 181 183 183 TYR TYR A . n 
A 1 182 LYS 182 184 184 LYS LYS A . n 
A 1 183 GLU 183 185 185 GLU GLU A . n 
A 1 184 ARG 184 186 186 ARG ARG A . n 
A 1 185 LEU 185 187 187 LEU LEU A . n 
A 1 186 GLY 186 188 188 GLY GLY A . n 
A 1 187 LEU 187 189 189 LEU LEU A . n 
A 1 188 PRO 188 190 190 PRO PRO A . n 
A 1 189 PRO 189 191 191 PRO PRO A . n 
A 1 190 LYS 190 192 192 LYS LYS A . n 
A 1 191 ILE 191 193 193 ILE ILE A . n 
A 1 192 VAL 192 194 194 VAL VAL A . n 
A 1 193 ILE 193 195 195 ILE ILE A . n 
A 1 194 GLY 194 196 196 GLY GLY A . n 
A 1 195 TYR 195 197 197 TYR TYR A . n 
A 1 196 GLN 196 198 198 GLN GLN A . n 
A 1 197 SER 197 199 199 SER SER A . n 
A 1 198 HIS 198 200 200 HIS HIS A . n 
A 1 199 ALA 199 201 201 ALA ALA A . n 
A 1 200 ASP 200 202 202 ASP ASP A . n 
A 1 201 THR 201 203 203 THR THR A . n 
A 1 202 ALA 202 204 204 ALA ALA A . n 
A 1 203 THR 203 205 205 THR THR A . n 
A 1 204 LYS 204 206 206 LYS LYS A . n 
A 1 205 SER 205 207 207 SER SER A . n 
A 1 206 GLY 206 208 208 GLY GLY A . n 
A 1 207 SER 207 209 209 SER SER A . n 
A 1 208 THR 208 210 210 THR THR A . n 
A 1 209 THR 209 211 211 THR THR A . n 
A 1 210 LYS 210 212 212 LYS LYS A . n 
A 1 211 ASN 211 213 213 ASN ASN A . n 
A 1 212 ARG 212 214 214 ARG ARG A . n 
A 1 213 PHE 213 215 215 PHE PHE A . n 
A 1 214 VAL 214 216 216 VAL VAL A . n 
A 1 215 VAL 215 217 217 VAL VAL A . n 
B 1 1   MET 1   3   ?   ?   ?   B . n 
B 1 2   HIS 2   4   ?   ?   ?   B . n 
B 1 3   HIS 3   5   ?   ?   ?   B . n 
B 1 4   HIS 4   6   ?   ?   ?   B . n 
B 1 5   HIS 5   7   ?   ?   ?   B . n 
B 1 6   HIS 6   8   ?   ?   ?   B . n 
B 1 7   HIS 7   9   ?   ?   ?   B . n 
B 1 8   GLY 8   10  ?   ?   ?   B . n 
B 1 9   ALA 9   11  11  ALA ALA B . n 
B 1 10  ARG 10  12  12  ARG ARG B . n 
B 1 11  ILE 11  13  13  ILE ILE B . n 
B 1 12  ILE 12  14  14  ILE ILE B . n 
B 1 13  TYR 13  15  15  TYR TYR B . n 
B 1 14  ASP 14  16  16  ASP ASP B . n 
B 1 15  ARG 15  17  17  ARG ARG B . n 
B 1 16  ALA 16  18  18  ALA ALA B . n 
B 1 17  PHE 17  19  19  PHE PHE B . n 
B 1 18  LEU 18  20  20  LEU LEU B . n 
B 1 19  MET 19  21  21  MET MET B . n 
B 1 20  ALA 20  22  22  ALA ALA B . n 
B 1 21  CYS 21  23  23  CYS CYS B . n 
B 1 22  ARG 22  24  24  ARG ARG B . n 
B 1 23  GLY 23  25  25  GLY GLY B . n 
B 1 24  GLY 24  26  ?   ?   ?   B . n 
B 1 25  GLY 25  27  ?   ?   ?   B . n 
B 1 26  GLY 26  28  ?   ?   ?   B . n 
B 1 27  GLU 27  29  ?   ?   ?   B . n 
B 1 28  ASN 28  30  ?   ?   ?   B . n 
B 1 29  LEU 29  31  ?   ?   ?   B . n 
B 1 30  TYR 30  32  ?   ?   ?   B . n 
B 1 31  PHE 31  33  ?   ?   ?   B . n 
B 1 32  GLN 32  34  ?   ?   ?   B . n 
B 1 33  GLY 33  35  ?   ?   ?   B . n 
B 1 34  LYS 34  36  36  LYS LYS B . n 
B 1 35  HIS 35  37  37  HIS HIS B . n 
B 1 36  PRO 36  38  38  PRO PRO B . n 
B 1 37  LEU 37  39  39  LEU LEU B . n 
B 1 38  GLN 38  40  40  GLN GLN B . n 
B 1 39  ASN 39  41  41  ASN ASN B . n 
B 1 40  ARG 40  42  42  ARG ARG B . n 
B 1 41  TRP 41  43  43  TRP TRP B . n 
B 1 42  ALA 42  44  44  ALA ALA B . n 
B 1 43  LEU 43  45  45  LEU LEU B . n 
B 1 44  TRP 44  46  46  TRP TRP B . n 
B 1 45  PHE 45  47  47  PHE PHE B . n 
B 1 46  PHE 46  48  48  PHE PHE B . n 
B 1 47  LYS 47  49  49  LYS LYS B . n 
B 1 48  ASN 48  50  50  ASN ASN B . n 
B 1 49  ASP 49  51  51  ASP ASP B . n 
B 1 50  LYS 50  52  52  LYS LYS B . n 
B 1 51  SER 51  53  53  SER SER B . n 
B 1 52  LYS 52  54  54  LYS LYS B . n 
B 1 53  THR 53  55  55  THR THR B . n 
B 1 54  TRP 54  56  56  TRP TRP B . n 
B 1 55  GLN 55  57  57  GLN GLN B . n 
B 1 56  ALA 56  58  58  ALA ALA B . n 
B 1 57  ASN 57  59  59  ASN ASN B . n 
B 1 58  LEU 58  60  60  LEU LEU B . n 
B 1 59  ARG 59  61  61  ARG ARG B . n 
B 1 60  LEU 60  62  62  LEU LEU B . n 
B 1 61  ILE 61  63  63  ILE ILE B . n 
B 1 62  SER 62  64  64  SER SER B . n 
B 1 63  LYS 63  65  65  LYS LYS B . n 
B 1 64  PHE 64  66  66  PHE PHE B . n 
B 1 65  ASP 65  67  67  ASP ASP B . n 
B 1 66  THR 66  68  68  THR THR B . n 
B 1 67  VAL 67  69  69  VAL VAL B . n 
B 1 68  GLU 68  70  70  GLU GLU B . n 
B 1 69  ASP 69  71  71  ASP ASP B . n 
B 1 70  PHE 70  72  72  PHE PHE B . n 
B 1 71  TRP 71  73  73  TRP TRP B . n 
B 1 72  ALA 72  74  74  ALA ALA B . n 
B 1 73  LEU 73  75  75  LEU LEU B . n 
B 1 74  TYR 74  76  76  TYR TYR B . n 
B 1 75  ASN 75  77  77  ASN ASN B . n 
B 1 76  HIS 76  78  78  HIS HIS B . n 
B 1 77  ILE 77  79  79  ILE ILE B . n 
B 1 78  GLN 78  80  80  GLN GLN B . n 
B 1 79  LEU 79  81  81  LEU LEU B . n 
B 1 80  SER 80  82  82  SER SER B . n 
B 1 81  SER 81  83  83  SER SER B . n 
B 1 82  ASN 82  84  84  ASN ASN B . n 
B 1 83  LEU 83  85  85  LEU LEU B . n 
B 1 84  MET 84  86  86  MET MET B . n 
B 1 85  PRO 85  87  87  PRO PRO B . n 
B 1 86  GLY 86  88  88  GLY GLY B . n 
B 1 87  CYS 87  89  89  CYS CYS B . n 
B 1 88  ASP 88  90  90  ASP ASP B . n 
B 1 89  TYR 89  91  91  TYR TYR B . n 
B 1 90  SER 90  92  92  SER SER B . n 
B 1 91  LEU 91  93  93  LEU LEU B . n 
B 1 92  PHE 92  94  94  PHE PHE B . n 
B 1 93  LYS 93  95  95  LYS LYS B . n 
B 1 94  ASP 94  96  96  ASP ASP B . n 
B 1 95  GLY 95  97  97  GLY GLY B . n 
B 1 96  ILE 96  98  98  ILE ILE B . n 
B 1 97  GLU 97  99  99  GLU GLU B . n 
B 1 98  PRO 98  100 100 PRO PRO B . n 
B 1 99  MET 99  101 101 MET MET B . n 
B 1 100 TRP 100 102 102 TRP TRP B . n 
B 1 101 GLU 101 103 103 GLU GLU B . n 
B 1 102 ASP 102 104 104 ASP ASP B . n 
B 1 103 GLU 103 105 105 GLU GLU B . n 
B 1 104 LYS 104 106 106 LYS LYS B . n 
B 1 105 ASN 105 107 107 ASN ASN B . n 
B 1 106 LYS 106 108 108 LYS LYS B . n 
B 1 107 ARG 107 109 109 ARG ARG B . n 
B 1 108 GLY 108 110 110 GLY GLY B . n 
B 1 109 GLY 109 111 111 GLY GLY B . n 
B 1 110 ARG 110 112 112 ARG ARG B . n 
B 1 111 TRP 111 113 113 TRP TRP B . n 
B 1 112 LEU 112 114 114 LEU LEU B . n 
B 1 113 ILE 113 115 115 ILE ILE B . n 
B 1 114 THR 114 116 116 THR THR B . n 
B 1 115 LEU 115 117 117 LEU LEU B . n 
B 1 116 ASN 116 118 118 ASN ASN B . n 
B 1 117 LYS 117 119 119 LYS LYS B . n 
B 1 118 GLN 118 120 120 GLN GLN B . n 
B 1 119 GLN 119 121 121 GLN GLN B . n 
B 1 120 ARG 120 122 122 ARG ARG B . n 
B 1 121 ARG 121 123 123 ARG ARG B . n 
B 1 122 SER 122 124 124 SER SER B . n 
B 1 123 ASP 123 125 125 ASP ASP B . n 
B 1 124 LEU 124 126 126 LEU LEU B . n 
B 1 125 ASN 125 127 127 ASN ASN B . n 
B 1 126 ARG 126 128 128 ARG ARG B . n 
B 1 127 PHE 127 129 129 PHE PHE B . n 
B 1 128 TRP 128 130 130 TRP TRP B . n 
B 1 129 LEU 129 131 131 LEU LEU B . n 
B 1 130 GLU 130 132 132 GLU GLU B . n 
B 1 131 THR 131 133 133 THR THR B . n 
B 1 132 LEU 132 134 134 LEU LEU B . n 
B 1 133 LEU 133 135 135 LEU LEU B . n 
B 1 134 CYS 134 136 136 CYS CYS B . n 
B 1 135 LEU 135 137 137 LEU LEU B . n 
B 1 136 ILE 136 138 138 ILE ILE B . n 
B 1 137 GLY 137 139 139 GLY GLY B . n 
B 1 138 GLU 138 140 140 GLU GLU B . n 
B 1 139 SER 139 141 141 SER SER B . n 
B 1 140 PHE 140 142 142 PHE PHE B . n 
B 1 141 ASP 141 143 143 ASP ASP B . n 
B 1 142 ASP 142 144 144 ASP ASP B . n 
B 1 143 TYR 143 145 145 TYR TYR B . n 
B 1 144 SER 144 146 146 SER SER B . n 
B 1 145 ASP 145 147 147 ASP ASP B . n 
B 1 146 ASP 146 148 148 ASP ASP B . n 
B 1 147 VAL 147 149 149 VAL VAL B . n 
B 1 148 CYS 148 150 150 CYS CYS B . n 
B 1 149 GLY 149 151 151 GLY GLY B . n 
B 1 150 ALA 150 152 152 ALA ALA B . n 
B 1 151 VAL 151 153 153 VAL VAL B . n 
B 1 152 VAL 152 154 154 VAL VAL B . n 
B 1 153 ASN 153 155 155 ASN ASN B . n 
B 1 154 VAL 154 156 156 VAL VAL B . n 
B 1 155 ARG 155 157 157 ARG ARG B . n 
B 1 156 ALA 156 158 158 ALA ALA B . n 
B 1 157 LYS 157 159 159 LYS LYS B . n 
B 1 158 GLY 158 160 160 GLY GLY B . n 
B 1 159 ASP 159 161 161 ASP ASP B . n 
B 1 160 LYS 160 162 162 LYS LYS B . n 
B 1 161 ILE 161 163 163 ILE ILE B . n 
B 1 162 ALA 162 164 164 ALA ALA B . n 
B 1 163 ILE 163 165 165 ILE ILE B . n 
B 1 164 TRP 164 166 166 TRP TRP B . n 
B 1 165 THR 165 167 167 THR THR B . n 
B 1 166 THR 166 168 168 THR THR B . n 
B 1 167 GLU 167 169 169 GLU GLU B . n 
B 1 168 CYS 168 170 170 CYS CYS B . n 
B 1 169 GLU 169 171 171 GLU GLU B . n 
B 1 170 ASN 170 172 172 ASN ASN B . n 
B 1 171 ARG 171 173 173 ARG ARG B . n 
B 1 172 GLU 172 174 174 GLU GLU B . n 
B 1 173 ALA 173 175 175 ALA ALA B . n 
B 1 174 VAL 174 176 176 VAL VAL B . n 
B 1 175 THR 175 177 177 THR THR B . n 
B 1 176 HIS 176 178 178 HIS HIS B . n 
B 1 177 ILE 177 179 179 ILE ILE B . n 
B 1 178 GLY 178 180 180 GLY GLY B . n 
B 1 179 ARG 179 181 181 ARG ARG B . n 
B 1 180 VAL 180 182 182 VAL VAL B . n 
B 1 181 TYR 181 183 183 TYR TYR B . n 
B 1 182 LYS 182 184 184 LYS LYS B . n 
B 1 183 GLU 183 185 185 GLU GLU B . n 
B 1 184 ARG 184 186 186 ARG ARG B . n 
B 1 185 LEU 185 187 187 LEU LEU B . n 
B 1 186 GLY 186 188 188 GLY GLY B . n 
B 1 187 LEU 187 189 189 LEU LEU B . n 
B 1 188 PRO 188 190 190 PRO PRO B . n 
B 1 189 PRO 189 191 191 PRO PRO B . n 
B 1 190 LYS 190 192 192 LYS LYS B . n 
B 1 191 ILE 191 193 193 ILE ILE B . n 
B 1 192 VAL 192 194 194 VAL VAL B . n 
B 1 193 ILE 193 195 195 ILE ILE B . n 
B 1 194 GLY 194 196 196 GLY GLY B . n 
B 1 195 TYR 195 197 197 TYR TYR B . n 
B 1 196 GLN 196 198 198 GLN GLN B . n 
B 1 197 SER 197 199 199 SER SER B . n 
B 1 198 HIS 198 200 200 HIS HIS B . n 
B 1 199 ALA 199 201 201 ALA ALA B . n 
B 1 200 ASP 200 202 202 ASP ASP B . n 
B 1 201 THR 201 203 203 THR THR B . n 
B 1 202 ALA 202 204 204 ALA ALA B . n 
B 1 203 THR 203 205 205 THR THR B . n 
B 1 204 LYS 204 206 206 LYS LYS B . n 
B 1 205 SER 205 207 207 SER SER B . n 
B 1 206 GLY 206 208 208 GLY GLY B . n 
B 1 207 SER 207 209 209 SER SER B . n 
B 1 208 THR 208 210 210 THR THR B . n 
B 1 209 THR 209 211 211 THR THR B . n 
B 1 210 LYS 210 212 212 LYS LYS B . n 
B 1 211 ASN 211 213 213 ASN ASN B . n 
B 1 212 ARG 212 214 214 ARG ARG B . n 
B 1 213 PHE 213 215 215 PHE PHE B . n 
B 1 214 VAL 214 216 216 VAL VAL B . n 
B 1 215 VAL 215 217 217 VAL VAL B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 W4K ? ? W4K ? ? 'SUBJECT OF INVESTIGATION' ? 
2 W4K ? ? W4K ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 EDO 1   301 301 EDO EDO A . 
D 3 PEG 1   302 401 PEG PEG A . 
E 4 DMS 1   303 328 DMS DMS A . 
F 5 W4K 1   304 1   W4K L01 A . 
G 2 EDO 1   301 301 EDO EDO B . 
H 2 EDO 1   302 401 EDO EDO B . 
I 3 PEG 1   303 329 PEG PEG B . 
J 4 DMS 1   304 330 DMS DMS B . 
K 3 PEG 1   305 401 PEG PEG B . 
L 3 PEG 1   306 501 PEG PEG B . 
M 5 W4K 1   307 1   W4K L02 B . 
N 6 HOH 1   401 18  HOH HOH A . 
N 6 HOH 2   402 28  HOH HOH A . 
N 6 HOH 3   403 256 HOH HOH A . 
N 6 HOH 4   404 9   HOH HOH A . 
N 6 HOH 5   405 15  HOH HOH A . 
N 6 HOH 6   406 160 HOH HOH A . 
N 6 HOH 7   407 216 HOH HOH A . 
N 6 HOH 8   408 219 HOH HOH A . 
N 6 HOH 9   409 320 HOH HOH A . 
N 6 HOH 10  410 190 HOH HOH A . 
N 6 HOH 11  411 131 HOH HOH A . 
N 6 HOH 12  412 118 HOH HOH A . 
N 6 HOH 13  413 1   HOH HOH A . 
N 6 HOH 14  414 211 HOH HOH A . 
N 6 HOH 15  415 29  HOH HOH A . 
N 6 HOH 16  416 145 HOH HOH A . 
N 6 HOH 17  417 89  HOH HOH A . 
N 6 HOH 18  418 109 HOH HOH A . 
N 6 HOH 19  419 72  HOH HOH A . 
N 6 HOH 20  420 121 HOH HOH A . 
N 6 HOH 21  421 19  HOH HOH A . 
N 6 HOH 22  422 218 HOH HOH A . 
N 6 HOH 23  423 14  HOH HOH A . 
N 6 HOH 24  424 7   HOH HOH A . 
N 6 HOH 25  425 62  HOH HOH A . 
N 6 HOH 26  426 234 HOH HOH A . 
N 6 HOH 27  427 144 HOH HOH A . 
N 6 HOH 28  428 155 HOH HOH A . 
N 6 HOH 29  429 269 HOH HOH A . 
N 6 HOH 30  430 128 HOH HOH A . 
N 6 HOH 31  431 281 HOH HOH A . 
N 6 HOH 32  432 45  HOH HOH A . 
N 6 HOH 33  433 8   HOH HOH A . 
N 6 HOH 34  434 174 HOH HOH A . 
N 6 HOH 35  435 323 HOH HOH A . 
N 6 HOH 36  436 176 HOH HOH A . 
N 6 HOH 37  437 125 HOH HOH A . 
N 6 HOH 38  438 123 HOH HOH A . 
N 6 HOH 39  439 26  HOH HOH A . 
N 6 HOH 40  440 17  HOH HOH A . 
N 6 HOH 41  441 44  HOH HOH A . 
N 6 HOH 42  442 130 HOH HOH A . 
N 6 HOH 43  443 180 HOH HOH A . 
N 6 HOH 44  444 181 HOH HOH A . 
N 6 HOH 45  445 110 HOH HOH A . 
N 6 HOH 46  446 59  HOH HOH A . 
N 6 HOH 47  447 66  HOH HOH A . 
N 6 HOH 48  448 33  HOH HOH A . 
N 6 HOH 49  449 22  HOH HOH A . 
N 6 HOH 50  450 12  HOH HOH A . 
N 6 HOH 51  451 99  HOH HOH A . 
N 6 HOH 52  452 74  HOH HOH A . 
N 6 HOH 53  453 101 HOH HOH A . 
N 6 HOH 54  454 115 HOH HOH A . 
N 6 HOH 55  455 3   HOH HOH A . 
N 6 HOH 56  456 10  HOH HOH A . 
N 6 HOH 57  457 210 HOH HOH A . 
N 6 HOH 58  458 32  HOH HOH A . 
N 6 HOH 59  459 154 HOH HOH A . 
N 6 HOH 60  460 5   HOH HOH A . 
N 6 HOH 61  461 68  HOH HOH A . 
N 6 HOH 62  462 202 HOH HOH A . 
N 6 HOH 63  463 158 HOH HOH A . 
N 6 HOH 64  464 163 HOH HOH A . 
N 6 HOH 65  465 306 HOH HOH A . 
N 6 HOH 66  466 225 HOH HOH A . 
N 6 HOH 67  467 236 HOH HOH A . 
N 6 HOH 68  468 151 HOH HOH A . 
N 6 HOH 69  469 12  HOH HOH A . 
N 6 HOH 70  470 270 HOH HOH A . 
N 6 HOH 71  471 78  HOH HOH A . 
N 6 HOH 72  472 284 HOH HOH A . 
N 6 HOH 73  473 289 HOH HOH A . 
N 6 HOH 74  474 294 HOH HOH A . 
N 6 HOH 75  475 177 HOH HOH A . 
N 6 HOH 76  476 224 HOH HOH A . 
N 6 HOH 77  477 65  HOH HOH A . 
N 6 HOH 78  478 42  HOH HOH A . 
N 6 HOH 79  479 159 HOH HOH A . 
N 6 HOH 80  480 75  HOH HOH A . 
N 6 HOH 81  481 79  HOH HOH A . 
N 6 HOH 82  482 193 HOH HOH A . 
N 6 HOH 83  483 82  HOH HOH A . 
N 6 HOH 84  484 141 HOH HOH A . 
N 6 HOH 85  485 317 HOH HOH A . 
N 6 HOH 86  486 192 HOH HOH A . 
N 6 HOH 87  487 290 HOH HOH A . 
N 6 HOH 88  488 265 HOH HOH A . 
N 6 HOH 89  489 302 HOH HOH A . 
N 6 HOH 90  490 197 HOH HOH A . 
N 6 HOH 91  491 11  HOH HOH A . 
N 6 HOH 92  492 324 HOH HOH A . 
N 6 HOH 93  493 276 HOH HOH A . 
N 6 HOH 94  494 70  HOH HOH A . 
N 6 HOH 95  495 165 HOH HOH A . 
N 6 HOH 96  496 76  HOH HOH A . 
N 6 HOH 97  497 279 HOH HOH A . 
N 6 HOH 98  498 126 HOH HOH A . 
N 6 HOH 99  499 61  HOH HOH A . 
N 6 HOH 100 500 261 HOH HOH A . 
N 6 HOH 101 501 67  HOH HOH A . 
N 6 HOH 102 502 170 HOH HOH A . 
N 6 HOH 103 503 239 HOH HOH A . 
N 6 HOH 104 504 94  HOH HOH A . 
N 6 HOH 105 505 314 HOH HOH A . 
N 6 HOH 106 506 203 HOH HOH A . 
N 6 HOH 107 507 237 HOH HOH A . 
N 6 HOH 108 508 157 HOH HOH A . 
N 6 HOH 109 509 98  HOH HOH A . 
N 6 HOH 110 510 248 HOH HOH A . 
N 6 HOH 111 511 288 HOH HOH A . 
N 6 HOH 112 512 156 HOH HOH A . 
N 6 HOH 113 513 84  HOH HOH A . 
N 6 HOH 114 514 215 HOH HOH A . 
N 6 HOH 115 515 46  HOH HOH A . 
N 6 HOH 116 516 88  HOH HOH A . 
N 6 HOH 117 517 40  HOH HOH A . 
N 6 HOH 118 518 146 HOH HOH A . 
N 6 HOH 119 519 34  HOH HOH A . 
N 6 HOH 120 520 200 HOH HOH A . 
N 6 HOH 121 521 148 HOH HOH A . 
N 6 HOH 122 522 268 HOH HOH A . 
N 6 HOH 123 523 220 HOH HOH A . 
N 6 HOH 124 524 173 HOH HOH A . 
N 6 HOH 125 525 277 HOH HOH A . 
N 6 HOH 126 526 257 HOH HOH A . 
N 6 HOH 127 527 7   HOH HOH A . 
N 6 HOH 128 528 334 HOH HOH A . 
N 6 HOH 129 529 147 HOH HOH A . 
N 6 HOH 130 530 55  HOH HOH A . 
N 6 HOH 131 531 204 HOH HOH A . 
N 6 HOH 132 532 209 HOH HOH A . 
N 6 HOH 133 533 241 HOH HOH A . 
N 6 HOH 134 534 41  HOH HOH A . 
N 6 HOH 135 535 138 HOH HOH A . 
N 6 HOH 136 536 296 HOH HOH A . 
N 6 HOH 137 537 3   HOH HOH A . 
N 6 HOH 138 538 243 HOH HOH A . 
N 6 HOH 139 539 233 HOH HOH A . 
N 6 HOH 140 540 230 HOH HOH A . 
N 6 HOH 141 541 321 HOH HOH A . 
N 6 HOH 142 542 56  HOH HOH A . 
N 6 HOH 143 543 5   HOH HOH A . 
N 6 HOH 144 544 287 HOH HOH A . 
N 6 HOH 145 545 16  HOH HOH A . 
N 6 HOH 146 546 232 HOH HOH A . 
N 6 HOH 147 547 96  HOH HOH A . 
N 6 HOH 148 548 9   HOH HOH A . 
N 6 HOH 149 549 129 HOH HOH A . 
N 6 HOH 150 550 53  HOH HOH A . 
N 6 HOH 151 551 107 HOH HOH A . 
N 6 HOH 152 552 142 HOH HOH A . 
N 6 HOH 153 553 325 HOH HOH A . 
N 6 HOH 154 554 73  HOH HOH A . 
N 6 HOH 155 555 222 HOH HOH A . 
N 6 HOH 156 556 100 HOH HOH A . 
N 6 HOH 157 557 258 HOH HOH A . 
N 6 HOH 158 558 179 HOH HOH A . 
N 6 HOH 159 559 240 HOH HOH A . 
N 6 HOH 160 560 6   HOH HOH A . 
N 6 HOH 161 561 113 HOH HOH A . 
N 6 HOH 162 562 267 HOH HOH A . 
N 6 HOH 163 563 250 HOH HOH A . 
N 6 HOH 164 564 8   HOH HOH A . 
N 6 HOH 165 565 235 HOH HOH A . 
N 6 HOH 166 566 64  HOH HOH A . 
N 6 HOH 167 567 238 HOH HOH A . 
N 6 HOH 168 568 137 HOH HOH A . 
O 6 HOH 1   401 195 HOH HOH B . 
O 6 HOH 2   402 298 HOH HOH B . 
O 6 HOH 3   403 259 HOH HOH B . 
O 6 HOH 4   404 48  HOH HOH B . 
O 6 HOH 5   405 50  HOH HOH B . 
O 6 HOH 6   406 39  HOH HOH B . 
O 6 HOH 7   407 175 HOH HOH B . 
O 6 HOH 8   408 251 HOH HOH B . 
O 6 HOH 9   409 24  HOH HOH B . 
O 6 HOH 10  410 172 HOH HOH B . 
O 6 HOH 11  411 213 HOH HOH B . 
O 6 HOH 12  412 124 HOH HOH B . 
O 6 HOH 13  413 111 HOH HOH B . 
O 6 HOH 14  414 332 HOH HOH B . 
O 6 HOH 15  415 249 HOH HOH B . 
O 6 HOH 16  416 4   HOH HOH B . 
O 6 HOH 17  417 27  HOH HOH B . 
O 6 HOH 18  418 127 HOH HOH B . 
O 6 HOH 19  419 47  HOH HOH B . 
O 6 HOH 20  420 116 HOH HOH B . 
O 6 HOH 21  421 30  HOH HOH B . 
O 6 HOH 22  422 6   HOH HOH B . 
O 6 HOH 23  423 217 HOH HOH B . 
O 6 HOH 24  424 120 HOH HOH B . 
O 6 HOH 25  425 38  HOH HOH B . 
O 6 HOH 26  426 282 HOH HOH B . 
O 6 HOH 27  427 319 HOH HOH B . 
O 6 HOH 28  428 117 HOH HOH B . 
O 6 HOH 29  429 31  HOH HOH B . 
O 6 HOH 30  430 103 HOH HOH B . 
O 6 HOH 31  431 77  HOH HOH B . 
O 6 HOH 32  432 81  HOH HOH B . 
O 6 HOH 33  433 315 HOH HOH B . 
O 6 HOH 34  434 266 HOH HOH B . 
O 6 HOH 35  435 2   HOH HOH B . 
O 6 HOH 36  436 91  HOH HOH B . 
O 6 HOH 37  437 152 HOH HOH B . 
O 6 HOH 38  438 122 HOH HOH B . 
O 6 HOH 39  439 221 HOH HOH B . 
O 6 HOH 40  440 54  HOH HOH B . 
O 6 HOH 41  441 60  HOH HOH B . 
O 6 HOH 42  442 149 HOH HOH B . 
O 6 HOH 43  443 58  HOH HOH B . 
O 6 HOH 44  444 95  HOH HOH B . 
O 6 HOH 45  445 169 HOH HOH B . 
O 6 HOH 46  446 104 HOH HOH B . 
O 6 HOH 47  447 167 HOH HOH B . 
O 6 HOH 48  448 133 HOH HOH B . 
O 6 HOH 49  449 135 HOH HOH B . 
O 6 HOH 50  450 212 HOH HOH B . 
O 6 HOH 51  451 272 HOH HOH B . 
O 6 HOH 52  452 4   HOH HOH B . 
O 6 HOH 53  453 309 HOH HOH B . 
O 6 HOH 54  454 187 HOH HOH B . 
O 6 HOH 55  455 63  HOH HOH B . 
O 6 HOH 56  456 196 HOH HOH B . 
O 6 HOH 57  457 201 HOH HOH B . 
O 6 HOH 58  458 136 HOH HOH B . 
O 6 HOH 59  459 206 HOH HOH B . 
O 6 HOH 60  460 86  HOH HOH B . 
O 6 HOH 61  461 254 HOH HOH B . 
O 6 HOH 62  462 183 HOH HOH B . 
O 6 HOH 63  463 186 HOH HOH B . 
O 6 HOH 64  464 226 HOH HOH B . 
O 6 HOH 65  465 83  HOH HOH B . 
O 6 HOH 66  466 57  HOH HOH B . 
O 6 HOH 67  467 20  HOH HOH B . 
O 6 HOH 68  468 229 HOH HOH B . 
O 6 HOH 69  469 69  HOH HOH B . 
O 6 HOH 70  470 168 HOH HOH B . 
O 6 HOH 71  471 153 HOH HOH B . 
O 6 HOH 72  472 1   HOH HOH B . 
O 6 HOH 73  473 295 HOH HOH B . 
O 6 HOH 74  474 285 HOH HOH B . 
O 6 HOH 75  475 2   HOH HOH B . 
O 6 HOH 76  476 134 HOH HOH B . 
O 6 HOH 77  477 291 HOH HOH B . 
O 6 HOH 78  478 106 HOH HOH B . 
O 6 HOH 79  479 178 HOH HOH B . 
O 6 HOH 80  480 71  HOH HOH B . 
O 6 HOH 81  481 23  HOH HOH B . 
O 6 HOH 82  482 143 HOH HOH B . 
O 6 HOH 83  483 208 HOH HOH B . 
O 6 HOH 84  484 164 HOH HOH B . 
O 6 HOH 85  485 90  HOH HOH B . 
O 6 HOH 86  486 162 HOH HOH B . 
O 6 HOH 87  487 278 HOH HOH B . 
O 6 HOH 88  488 286 HOH HOH B . 
O 6 HOH 89  489 311 HOH HOH B . 
O 6 HOH 90  490 185 HOH HOH B . 
O 6 HOH 91  491 92  HOH HOH B . 
O 6 HOH 92  492 191 HOH HOH B . 
O 6 HOH 93  493 49  HOH HOH B . 
O 6 HOH 94  494 247 HOH HOH B . 
O 6 HOH 95  495 182 HOH HOH B . 
O 6 HOH 96  496 10  HOH HOH B . 
O 6 HOH 97  497 231 HOH HOH B . 
O 6 HOH 98  498 316 HOH HOH B . 
O 6 HOH 99  499 228 HOH HOH B . 
O 6 HOH 100 500 25  HOH HOH B . 
O 6 HOH 101 501 166 HOH HOH B . 
O 6 HOH 102 502 297 HOH HOH B . 
O 6 HOH 103 503 300 HOH HOH B . 
O 6 HOH 104 504 161 HOH HOH B . 
O 6 HOH 105 505 105 HOH HOH B . 
O 6 HOH 106 506 227 HOH HOH B . 
O 6 HOH 107 507 322 HOH HOH B . 
O 6 HOH 108 508 52  HOH HOH B . 
O 6 HOH 109 509 301 HOH HOH B . 
O 6 HOH 110 510 264 HOH HOH B . 
O 6 HOH 111 511 245 HOH HOH B . 
O 6 HOH 112 512 318 HOH HOH B . 
O 6 HOH 113 513 271 HOH HOH B . 
O 6 HOH 114 514 93  HOH HOH B . 
O 6 HOH 115 515 242 HOH HOH B . 
O 6 HOH 116 516 108 HOH HOH B . 
O 6 HOH 117 517 246 HOH HOH B . 
O 6 HOH 118 518 150 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER  ? ? ? '2.11.8 (16-JUL-2021)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                      2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? BUSTER  ? ? ? .                      4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   95.71 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QM9 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     47.284 
_cell.length_a_esd                 ? 
_cell.length_b                     69.273 
_cell.length_b_esd                 ? 
_cell.length_c                     64.656 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8QM9 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8QM9 
_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             2.11 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.60 
_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              8.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;0.002M DTT
38% PEG 400
0.1M pH=8 Tris/HCl
;
_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 PILATUS 300K' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2016-06-10 
_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   1.54178 
_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                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU FR-X' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.54178 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8QM9 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.973 
_reflns.d_resolution_low                               64.33 
_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                                     27418 
_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                           92.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.9 
_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                                0.122 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    1.973 
_reflns_shell.d_res_low                                     1.98 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             307 
_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                               ? 
_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                               1.662 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_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                                  ? 
_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]                            -4.24540 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -4.97550 
_refine.aniso_B[2][2]                            6.62290 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            -2.37750 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               40.360 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.922 
_refine.correlation_coeff_Fo_to_Fc_free          0.909 
_refine.details                                  
;HYDROGENS WERE FULLY REFINED
 WITH FULL OCCUPANCY AT NUCLEAR POSITION.
;
_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                                 8QM9 
_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                            1.973 
_refine.ls_d_res_low                             47.05 
_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                     27229 
_refine.ls_number_reflns_R_free                  1359 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    92.8 
_refine.ls_percent_reflns_R_free                 4.990 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2288 
_refine.ls_R_factor_R_free                       0.2719 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2265 
_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                    ? 
_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                          0.000 
_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          'FOURIER SYNTHESIS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.204 
_refine.pdbx_overall_SU_R_Blow_DPI               0.259 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_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_analyze.entry_id                        8QM9 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.28 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.973 
_refine_hist.d_res_low                        47.05 
_refine_hist.number_atoms_solvent             286 
_refine_hist.number_atoms_total               3693 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3309 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         98 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.012 ? 6829  ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 1.04  ? 12241 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1503  ? t_dihedral_angle_d        2.00  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_incorr_chiral_ct        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_pseud_angle             ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_trig_c_planes           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 1078  ? t_gen_planes              16.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 6829  ? t_it                      10.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 6.94  ? ?     ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 16.15 ? ?     ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 428   ? t_chiral_improper_torsion 5.00  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_sum_occupancies         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_utility_distance        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_utility_angle           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_utility_torsion         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 5384  ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.973 
_refine_ls_shell.d_res_low                        1.99 
_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             523 
_refine_ls_shell.percent_reflns_obs               100.00 
_refine_ls_shell.percent_reflns_R_free            4.04 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.3082 
_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                  0.3863 
# 
_struct.entry_id                     8QM9 
_struct.title                        'Potential drug binding sites for translation initiation factor eIF4E' 
_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        8QM9 
_struct_keywords.text            
'translation initiation factor, translation regulator, protein biosynthesis, RNA binding, TRANSLATION' 
_struct_keywords.pdbx_keywords   TRANSLATION 
# 
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 5 ? 
G N N 2 ? 
H N N 2 ? 
I N N 3 ? 
J N N 4 ? 
K N N 3 ? 
L N N 3 ? 
M N N 5 ? 
N N N 6 ? 
O N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    IF4E_HUMAN 
_struct_ref.pdbx_db_accession          P06730 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;KHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLSSNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLI
TLNKQQRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDKIAIWTTECENREAVTHIGRVYKERLGLPPKIVI
GYQSHADTATKSGSTTKNRFVV
;
_struct_ref.pdbx_align_begin           36 
# 
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 8QM9 A 34 ? 215 ? P06730 36 ? 217 ? 36 217 
2 1 8QM9 B 34 ? 215 ? P06730 36 ? 217 ? 36 217 
# 
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 8QM9 MET A 1   ? UNP P06730 ?   ?   'initiating methionine' 3   1  
1 8QM9 HIS A 2   ? UNP P06730 ?   ?   'expression tag'        4   2  
1 8QM9 HIS A 3   ? UNP P06730 ?   ?   'expression tag'        5   3  
1 8QM9 HIS A 4   ? UNP P06730 ?   ?   'expression tag'        6   4  
1 8QM9 HIS A 5   ? UNP P06730 ?   ?   'expression tag'        7   5  
1 8QM9 HIS A 6   ? UNP P06730 ?   ?   'expression tag'        8   6  
1 8QM9 HIS A 7   ? UNP P06730 ?   ?   'expression tag'        9   7  
1 8QM9 GLY A 8   ? UNP P06730 ?   ?   'expression tag'        10  8  
1 8QM9 ALA A 9   ? UNP P06730 ?   ?   'expression tag'        11  9  
1 8QM9 ARG A 10  ? UNP P06730 ?   ?   'expression tag'        12  10 
1 8QM9 ILE A 11  ? UNP P06730 ?   ?   'expression tag'        13  11 
1 8QM9 ILE A 12  ? UNP P06730 ?   ?   'expression tag'        14  12 
1 8QM9 TYR A 13  ? UNP P06730 ?   ?   'expression tag'        15  13 
1 8QM9 ASP A 14  ? UNP P06730 ?   ?   'expression tag'        16  14 
1 8QM9 ARG A 15  ? UNP P06730 ?   ?   'expression tag'        17  15 
1 8QM9 ALA A 16  ? UNP P06730 ?   ?   'expression tag'        18  16 
1 8QM9 PHE A 17  ? UNP P06730 ?   ?   'expression tag'        19  17 
1 8QM9 LEU A 18  ? UNP P06730 ?   ?   'expression tag'        20  18 
1 8QM9 MET A 19  ? UNP P06730 ?   ?   'expression tag'        21  19 
1 8QM9 ALA A 20  ? UNP P06730 ?   ?   'expression tag'        22  20 
1 8QM9 CYS A 21  ? UNP P06730 ?   ?   'expression tag'        23  21 
1 8QM9 ARG A 22  ? UNP P06730 ?   ?   'expression tag'        24  22 
1 8QM9 GLY A 23  ? UNP P06730 ?   ?   'expression tag'        25  23 
1 8QM9 GLY A 24  ? UNP P06730 ?   ?   'expression tag'        26  24 
1 8QM9 GLY A 25  ? UNP P06730 ?   ?   'expression tag'        27  25 
1 8QM9 GLY A 26  ? UNP P06730 ?   ?   'expression tag'        28  26 
1 8QM9 GLU A 27  ? UNP P06730 ?   ?   'expression tag'        29  27 
1 8QM9 ASN A 28  ? UNP P06730 ?   ?   'expression tag'        30  28 
1 8QM9 LEU A 29  ? UNP P06730 ?   ?   'expression tag'        31  29 
1 8QM9 TYR A 30  ? UNP P06730 ?   ?   'expression tag'        32  30 
1 8QM9 PHE A 31  ? UNP P06730 ?   ?   'expression tag'        33  31 
1 8QM9 GLN A 32  ? UNP P06730 ?   ?   'expression tag'        34  32 
1 8QM9 GLY A 33  ? UNP P06730 ?   ?   'expression tag'        35  33 
1 8QM9 ASN A 125 ? UNP P06730 ASP 127 conflict                127 34 
2 8QM9 MET B 1   ? UNP P06730 ?   ?   'initiating methionine' 3   35 
2 8QM9 HIS B 2   ? UNP P06730 ?   ?   'expression tag'        4   36 
2 8QM9 HIS B 3   ? UNP P06730 ?   ?   'expression tag'        5   37 
2 8QM9 HIS B 4   ? UNP P06730 ?   ?   'expression tag'        6   38 
2 8QM9 HIS B 5   ? UNP P06730 ?   ?   'expression tag'        7   39 
2 8QM9 HIS B 6   ? UNP P06730 ?   ?   'expression tag'        8   40 
2 8QM9 HIS B 7   ? UNP P06730 ?   ?   'expression tag'        9   41 
2 8QM9 GLY B 8   ? UNP P06730 ?   ?   'expression tag'        10  42 
2 8QM9 ALA B 9   ? UNP P06730 ?   ?   'expression tag'        11  43 
2 8QM9 ARG B 10  ? UNP P06730 ?   ?   'expression tag'        12  44 
2 8QM9 ILE B 11  ? UNP P06730 ?   ?   'expression tag'        13  45 
2 8QM9 ILE B 12  ? UNP P06730 ?   ?   'expression tag'        14  46 
2 8QM9 TYR B 13  ? UNP P06730 ?   ?   'expression tag'        15  47 
2 8QM9 ASP B 14  ? UNP P06730 ?   ?   'expression tag'        16  48 
2 8QM9 ARG B 15  ? UNP P06730 ?   ?   'expression tag'        17  49 
2 8QM9 ALA B 16  ? UNP P06730 ?   ?   'expression tag'        18  50 
2 8QM9 PHE B 17  ? UNP P06730 ?   ?   'expression tag'        19  51 
2 8QM9 LEU B 18  ? UNP P06730 ?   ?   'expression tag'        20  52 
2 8QM9 MET B 19  ? UNP P06730 ?   ?   'expression tag'        21  53 
2 8QM9 ALA B 20  ? UNP P06730 ?   ?   'expression tag'        22  54 
2 8QM9 CYS B 21  ? UNP P06730 ?   ?   'expression tag'        23  55 
2 8QM9 ARG B 22  ? UNP P06730 ?   ?   'expression tag'        24  56 
2 8QM9 GLY B 23  ? UNP P06730 ?   ?   'expression tag'        25  57 
2 8QM9 GLY B 24  ? UNP P06730 ?   ?   'expression tag'        26  58 
2 8QM9 GLY B 25  ? UNP P06730 ?   ?   'expression tag'        27  59 
2 8QM9 GLY B 26  ? UNP P06730 ?   ?   'expression tag'        28  60 
2 8QM9 GLU B 27  ? UNP P06730 ?   ?   'expression tag'        29  61 
2 8QM9 ASN B 28  ? UNP P06730 ?   ?   'expression tag'        30  62 
2 8QM9 LEU B 29  ? UNP P06730 ?   ?   'expression tag'        31  63 
2 8QM9 TYR B 30  ? UNP P06730 ?   ?   'expression tag'        32  64 
2 8QM9 PHE B 31  ? UNP P06730 ?   ?   'expression tag'        33  65 
2 8QM9 GLN B 32  ? UNP P06730 ?   ?   'expression tag'        34  66 
2 8QM9 GLY B 33  ? UNP P06730 ?   ?   'expression tag'        35  67 
2 8QM9 ASN B 125 ? UNP P06730 ASP 127 conflict                127 68 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2940  ? 
1 MORE         25    ? 
1 'SSA (A^2)'  20700 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                'monomer in solution' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 14  ? CYS A 21  ? ASP A 16  CYS A 23  1 ? 8  
HELX_P HELX_P2  AA2 ASN A 28  ? GLN A 32  ? ASN A 30  GLN A 34  5 ? 5  
HELX_P HELX_P3  AA3 THR A 53  ? ASN A 57  ? THR A 55  ASN A 59  1 ? 5  
HELX_P HELX_P4  AA4 VAL A 67  ? SER A 81  ? VAL A 69  SER A 83  1 ? 15 
HELX_P HELX_P5  AA5 GLN A 118 ? GLY A 137 ? GLN A 120 GLY A 139 1 ? 20 
HELX_P HELX_P6  AA6 PHE A 140 ? ASP A 145 ? PHE A 142 ASP A 147 5 ? 6  
HELX_P HELX_P7  AA7 ASN A 170 ? GLY A 186 ? ASN A 172 GLY A 188 1 ? 17 
HELX_P HELX_P8  AA8 HIS A 198 ? THR A 203 ? HIS A 200 THR A 205 1 ? 6  
HELX_P HELX_P9  AA9 ASP B 14  ? CYS B 21  ? ASP B 16  CYS B 23  1 ? 8  
HELX_P HELX_P10 AB1 THR B 53  ? LEU B 58  ? THR B 55  LEU B 60  1 ? 6  
HELX_P HELX_P11 AB2 VAL B 67  ? SER B 81  ? VAL B 69  SER B 83  1 ? 15 
HELX_P HELX_P12 AB3 GLN B 118 ? GLY B 137 ? GLN B 120 GLY B 139 1 ? 20 
HELX_P HELX_P13 AB4 PHE B 140 ? ASP B 145 ? PHE B 142 ASP B 147 5 ? 6  
HELX_P HELX_P14 AB5 ASN B 170 ? LEU B 185 ? ASN B 172 LEU B 187 1 ? 16 
HELX_P HELX_P15 AB6 HIS B 198 ? THR B 203 ? HIS B 200 THR B 205 1 ? 6  
# 
_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 ? 8 ? 
AA2 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 58  ? THR A 66  ? LEU A 60  THR A 68  
AA1 2 PRO A 36  ? PHE A 46  ? PRO A 38  PHE A 48  
AA1 3 ASP A 88  ? LYS A 93  ? ASP A 90  LYS A 95  
AA1 4 VAL A 147 ? ASN A 153 ? VAL A 149 ASN A 155 
AA1 5 LYS A 160 ? THR A 165 ? LYS A 162 THR A 167 
AA1 6 GLY A 109 ? THR A 114 ? GLY A 111 THR A 116 
AA1 7 GLY A 194 ? SER A 197 ? GLY A 196 SER A 199 
AA1 8 PHE A 213 ? VAL A 214 ? PHE A 215 VAL A 216 
AA2 1 ARG B 59  ? THR B 66  ? ARG B 61  THR B 68  
AA2 2 PRO B 36  ? LYS B 47  ? PRO B 38  LYS B 49  
AA2 3 CYS B 87  ? LYS B 93  ? CYS B 89  LYS B 95  
AA2 4 VAL B 147 ? ASN B 153 ? VAL B 149 ASN B 155 
AA2 5 LYS B 160 ? THR B 165 ? LYS B 162 THR B 167 
AA2 6 GLY B 109 ? THR B 114 ? GLY B 111 THR B 116 
AA2 7 GLY B 194 ? SER B 197 ? GLY B 196 SER B 199 
AA2 8 PHE B 213 ? VAL B 214 ? PHE B 215 VAL B 216 
# 
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 SER A 62  ? O SER A 64  N LEU A 43  ? N LEU A 45  
AA1 2 3 N ALA A 42  ? N ALA A 44  O PHE A 92  ? O PHE A 94  
AA1 3 4 N TYR A 89  ? N TYR A 91  O VAL A 152 ? O VAL A 154 
AA1 4 5 N ASN A 153 ? N ASN A 155 O LYS A 160 ? O LYS A 162 
AA1 5 6 O THR A 165 ? O THR A 167 N GLY A 109 ? N GLY A 111 
AA1 6 7 N ARG A 110 ? N ARG A 112 O GLN A 196 ? O GLN A 198 
AA1 7 8 N TYR A 195 ? N TYR A 197 O PHE A 213 ? O PHE A 215 
AA2 1 2 O ARG B 59  ? O ARG B 61  N PHE B 45  ? N PHE B 47  
AA2 2 3 N TRP B 44  ? N TRP B 46  O SER B 90  ? O SER B 92  
AA2 3 4 N TYR B 89  ? N TYR B 91  O VAL B 152 ? O VAL B 154 
AA2 4 5 N ASN B 153 ? N ASN B 155 O LYS B 160 ? O LYS B 162 
AA2 5 6 O ILE B 161 ? O ILE B 163 N ILE B 113 ? N ILE B 115 
AA2 6 7 N ARG B 110 ? N ARG B 112 O GLN B 196 ? O GLN B 198 
AA2 7 8 N TYR B 195 ? N TYR B 197 O PHE B 213 ? O PHE B 215 
# 
_pdbx_entry_details.entry_id                   8QM9 
_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_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 TYR A 32  ? ? 55.90   16.21   
2 1 SER A 53  ? ? 20.72   78.31   
3 1 ASP A 67  ? ? -148.16 24.11   
4 1 ASP A 143 ? ? 63.67   -140.65 
5 1 THR A 210 ? ? 67.63   168.18  
6 1 ASN B 50  ? ? -78.91  38.33   
7 1 ASP B 67  ? ? -149.34 24.23   
8 1 ASP B 143 ? ? 62.82   -139.11 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 20.6372 -13.6152 4.1016  -0.1105 ? -0.0179 ? -0.0409 ? -0.0332 ? 0.0022 ? 0.1202  ? 1.0913 ? 
-0.0332 ? 0.0748  ? 1.4647 ? -0.3568 ? 0.3835 ? 0.0896  ? -0.0682 ? 0.1359  ? 0.0244  ? -0.0640 ? 0.0881 ? 0.0793 ? 0.0759 ? 
-0.0256 ? 
2 'X-RAY DIFFRACTION' ? refined 1.4968  -21.4678 32.3461 -0.0026 ? -0.0069 ? -0.0618 ? -0.0490 ? 0.0205 ? -0.0010 ? 1.1049 ? 
0.5893  ? -0.1285 ? 2.1257 ? 0.6369  ? 1.3365 ? -0.1069 ? -0.1871 ? -0.0525 ? -0.0250 ? -0.0762 ? 0.0789 ? 0.0246 ? 0.1096 ? 
0.1831  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? '{ A|11 - A|217 }' 
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? '{ B|11 - B|217 }' 
# 
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 3  ? A MET 1  
2  1 Y 1 A HIS 4  ? A HIS 2  
3  1 Y 1 A HIS 5  ? A HIS 3  
4  1 Y 1 A HIS 6  ? A HIS 4  
5  1 Y 1 A HIS 7  ? A HIS 5  
6  1 Y 1 A HIS 8  ? A HIS 6  
7  1 Y 1 A HIS 9  ? A HIS 7  
8  1 Y 1 A GLY 10 ? A GLY 8  
9  1 Y 1 B MET 3  ? B MET 1  
10 1 Y 1 B HIS 4  ? B HIS 2  
11 1 Y 1 B HIS 5  ? B HIS 3  
12 1 Y 1 B HIS 6  ? B HIS 4  
13 1 Y 1 B HIS 7  ? B HIS 5  
14 1 Y 1 B HIS 8  ? B HIS 6  
15 1 Y 1 B HIS 9  ? B HIS 7  
16 1 Y 1 B GLY 10 ? B GLY 8  
17 1 Y 1 B GLY 26 ? B GLY 24 
18 1 Y 1 B GLY 27 ? B GLY 25 
19 1 Y 1 B GLY 28 ? B GLY 26 
20 1 Y 1 B GLU 29 ? B GLU 27 
21 1 Y 1 B ASN 30 ? B ASN 28 
22 1 Y 1 B LEU 31 ? B LEU 29 
23 1 Y 1 B TYR 32 ? B TYR 30 
24 1 Y 1 B PHE 33 ? B PHE 31 
25 1 Y 1 B GLN 34 ? B GLN 32 
26 1 Y 1 B GLY 35 ? B GLY 33 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
DMS S    S N N 88  
DMS O    O N N 89  
DMS C1   C N N 90  
DMS C2   C N N 91  
DMS H11  H N N 92  
DMS H12  H N N 93  
DMS H13  H N N 94  
DMS H21  H N N 95  
DMS H22  H N N 96  
DMS H23  H N N 97  
EDO C1   C N N 98  
EDO O1   O N N 99  
EDO C2   C N N 100 
EDO O2   O N N 101 
EDO H11  H N N 102 
EDO H12  H N N 103 
EDO HO1  H N N 104 
EDO H21  H N N 105 
EDO H22  H N N 106 
EDO HO2  H N N 107 
GLN N    N N N 108 
GLN CA   C N S 109 
GLN C    C N N 110 
GLN O    O N N 111 
GLN CB   C N N 112 
GLN CG   C N N 113 
GLN CD   C N N 114 
GLN OE1  O N N 115 
GLN NE2  N N N 116 
GLN OXT  O N N 117 
GLN H    H N N 118 
GLN H2   H N N 119 
GLN HA   H N N 120 
GLN HB2  H N N 121 
GLN HB3  H N N 122 
GLN HG2  H N N 123 
GLN HG3  H N N 124 
GLN HE21 H N N 125 
GLN HE22 H N N 126 
GLN HXT  H N N 127 
GLU N    N N N 128 
GLU CA   C N S 129 
GLU C    C N N 130 
GLU O    O N N 131 
GLU CB   C N N 132 
GLU CG   C N N 133 
GLU CD   C N N 134 
GLU OE1  O N N 135 
GLU OE2  O N N 136 
GLU OXT  O N N 137 
GLU H    H N N 138 
GLU H2   H N N 139 
GLU HA   H N N 140 
GLU HB2  H N N 141 
GLU HB3  H N N 142 
GLU HG2  H N N 143 
GLU HG3  H N N 144 
GLU HE2  H N N 145 
GLU HXT  H N N 146 
GLY N    N N N 147 
GLY CA   C N N 148 
GLY C    C N N 149 
GLY O    O N N 150 
GLY OXT  O N N 151 
GLY H    H N N 152 
GLY H2   H N N 153 
GLY HA2  H N N 154 
GLY HA3  H N N 155 
GLY HXT  H N N 156 
HIS N    N N N 157 
HIS CA   C N S 158 
HIS C    C N N 159 
HIS O    O N N 160 
HIS CB   C N N 161 
HIS CG   C Y N 162 
HIS ND1  N Y N 163 
HIS CD2  C Y N 164 
HIS CE1  C Y N 165 
HIS NE2  N Y N 166 
HIS OXT  O N N 167 
HIS H    H N N 168 
HIS H2   H N N 169 
HIS HA   H N N 170 
HIS HB2  H N N 171 
HIS HB3  H N N 172 
HIS HD1  H N N 173 
HIS HD2  H N N 174 
HIS HE1  H N N 175 
HIS HE2  H N N 176 
HIS HXT  H N N 177 
HOH O    O N N 178 
HOH H1   H N N 179 
HOH H2   H N N 180 
ILE N    N N N 181 
ILE CA   C N S 182 
ILE C    C N N 183 
ILE O    O N N 184 
ILE CB   C N S 185 
ILE CG1  C N N 186 
ILE CG2  C N N 187 
ILE CD1  C N N 188 
ILE OXT  O N N 189 
ILE H    H N N 190 
ILE H2   H N N 191 
ILE HA   H N N 192 
ILE HB   H N N 193 
ILE HG12 H N N 194 
ILE HG13 H N N 195 
ILE HG21 H N N 196 
ILE HG22 H N N 197 
ILE HG23 H N N 198 
ILE HD11 H N N 199 
ILE HD12 H N N 200 
ILE HD13 H N N 201 
ILE HXT  H N N 202 
LEU N    N N N 203 
LEU CA   C N S 204 
LEU C    C N N 205 
LEU O    O N N 206 
LEU CB   C N N 207 
LEU CG   C N N 208 
LEU CD1  C N N 209 
LEU CD2  C N N 210 
LEU OXT  O N N 211 
LEU H    H N N 212 
LEU H2   H N N 213 
LEU HA   H N N 214 
LEU HB2  H N N 215 
LEU HB3  H N N 216 
LEU HG   H N N 217 
LEU HD11 H N N 218 
LEU HD12 H N N 219 
LEU HD13 H N N 220 
LEU HD21 H N N 221 
LEU HD22 H N N 222 
LEU HD23 H N N 223 
LEU HXT  H N N 224 
LYS N    N N N 225 
LYS CA   C N S 226 
LYS C    C N N 227 
LYS O    O N N 228 
LYS CB   C N N 229 
LYS CG   C N N 230 
LYS CD   C N N 231 
LYS CE   C N N 232 
LYS NZ   N N N 233 
LYS OXT  O N N 234 
LYS H    H N N 235 
LYS H2   H N N 236 
LYS HA   H N N 237 
LYS HB2  H N N 238 
LYS HB3  H N N 239 
LYS HG2  H N N 240 
LYS HG3  H N N 241 
LYS HD2  H N N 242 
LYS HD3  H N N 243 
LYS HE2  H N N 244 
LYS HE3  H N N 245 
LYS HZ1  H N N 246 
LYS HZ2  H N N 247 
LYS HZ3  H N N 248 
LYS HXT  H N N 249 
MET N    N N N 250 
MET CA   C N S 251 
MET C    C N N 252 
MET O    O N N 253 
MET CB   C N N 254 
MET CG   C N N 255 
MET SD   S N N 256 
MET CE   C N N 257 
MET OXT  O N N 258 
MET H    H N N 259 
MET H2   H N N 260 
MET HA   H N N 261 
MET HB2  H N N 262 
MET HB3  H N N 263 
MET HG2  H N N 264 
MET HG3  H N N 265 
MET HE1  H N N 266 
MET HE2  H N N 267 
MET HE3  H N N 268 
MET HXT  H N N 269 
PEG C1   C N N 270 
PEG O1   O N N 271 
PEG C2   C N N 272 
PEG O2   O N N 273 
PEG C3   C N N 274 
PEG C4   C N N 275 
PEG O4   O N N 276 
PEG H11  H N N 277 
PEG H12  H N N 278 
PEG HO1  H N N 279 
PEG H21  H N N 280 
PEG H22  H N N 281 
PEG H31  H N N 282 
PEG H32  H N N 283 
PEG H41  H N N 284 
PEG H42  H N N 285 
PEG HO4  H N N 286 
PHE N    N N N 287 
PHE CA   C N S 288 
PHE C    C N N 289 
PHE O    O N N 290 
PHE CB   C N N 291 
PHE CG   C Y N 292 
PHE CD1  C Y N 293 
PHE CD2  C Y N 294 
PHE CE1  C Y N 295 
PHE CE2  C Y N 296 
PHE CZ   C Y N 297 
PHE OXT  O N N 298 
PHE H    H N N 299 
PHE H2   H N N 300 
PHE HA   H N N 301 
PHE HB2  H N N 302 
PHE HB3  H N N 303 
PHE HD1  H N N 304 
PHE HD2  H N N 305 
PHE HE1  H N N 306 
PHE HE2  H N N 307 
PHE HZ   H N N 308 
PHE HXT  H N N 309 
PRO N    N N N 310 
PRO CA   C N S 311 
PRO C    C N N 312 
PRO O    O N N 313 
PRO CB   C N N 314 
PRO CG   C N N 315 
PRO CD   C N N 316 
PRO OXT  O N N 317 
PRO H    H N N 318 
PRO HA   H N N 319 
PRO HB2  H N N 320 
PRO HB3  H N N 321 
PRO HG2  H N N 322 
PRO HG3  H N N 323 
PRO HD2  H N N 324 
PRO HD3  H N N 325 
PRO HXT  H N N 326 
SER N    N N N 327 
SER CA   C N S 328 
SER C    C N N 329 
SER O    O N N 330 
SER CB   C N N 331 
SER OG   O N N 332 
SER OXT  O N N 333 
SER H    H N N 334 
SER H2   H N N 335 
SER HA   H N N 336 
SER HB2  H N N 337 
SER HB3  H N N 338 
SER HG   H N N 339 
SER HXT  H N N 340 
THR N    N N N 341 
THR CA   C N S 342 
THR C    C N N 343 
THR O    O N N 344 
THR CB   C N R 345 
THR OG1  O N N 346 
THR CG2  C N N 347 
THR OXT  O N N 348 
THR H    H N N 349 
THR H2   H N N 350 
THR HA   H N N 351 
THR HB   H N N 352 
THR HG1  H N N 353 
THR HG21 H N N 354 
THR HG22 H N N 355 
THR HG23 H N N 356 
THR HXT  H N N 357 
TRP N    N N N 358 
TRP CA   C N S 359 
TRP C    C N N 360 
TRP O    O N N 361 
TRP CB   C N N 362 
TRP CG   C Y N 363 
TRP CD1  C Y N 364 
TRP CD2  C Y N 365 
TRP NE1  N Y N 366 
TRP CE2  C Y N 367 
TRP CE3  C Y N 368 
TRP CZ2  C Y N 369 
TRP CZ3  C Y N 370 
TRP CH2  C Y N 371 
TRP OXT  O N N 372 
TRP H    H N N 373 
TRP H2   H N N 374 
TRP HA   H N N 375 
TRP HB2  H N N 376 
TRP HB3  H N N 377 
TRP HD1  H N N 378 
TRP HE1  H N N 379 
TRP HE3  H N N 380 
TRP HZ2  H N N 381 
TRP HZ3  H N N 382 
TRP HH2  H N N 383 
TRP HXT  H N N 384 
TYR N    N N N 385 
TYR CA   C N S 386 
TYR C    C N N 387 
TYR O    O N N 388 
TYR CB   C N N 389 
TYR CG   C Y N 390 
TYR CD1  C Y N 391 
TYR CD2  C Y N 392 
TYR CE1  C Y N 393 
TYR CE2  C Y N 394 
TYR CZ   C Y N 395 
TYR OH   O N N 396 
TYR OXT  O N N 397 
TYR H    H N N 398 
TYR H2   H N N 399 
TYR HA   H N N 400 
TYR HB2  H N N 401 
TYR HB3  H N N 402 
TYR HD1  H N N 403 
TYR HD2  H N N 404 
TYR HE1  H N N 405 
TYR HE2  H N N 406 
TYR HH   H N N 407 
TYR HXT  H N N 408 
VAL N    N N N 409 
VAL CA   C N S 410 
VAL C    C N N 411 
VAL O    O N N 412 
VAL CB   C N N 413 
VAL CG1  C N N 414 
VAL CG2  C N N 415 
VAL OXT  O N N 416 
VAL H    H N N 417 
VAL H2   H N N 418 
VAL HA   H N N 419 
VAL HB   H N N 420 
VAL HG11 H N N 421 
VAL HG12 H N N 422 
VAL HG13 H N N 423 
VAL HG21 H N N 424 
VAL HG22 H N N 425 
VAL HG23 H N N 426 
VAL HXT  H N N 427 
W4K C1   C N N 428 
W4K C2   C N N 429 
W4K C3   C N S 430 
W4K C5   C N R 431 
W4K C6   C N N 432 
W4K C7   C N N 433 
W4K C10  C Y N 434 
W4K C11  C Y N 435 
W4K C12  C Y N 436 
W4K C13  C Y N 437 
W4K C14  C Y N 438 
W4K C16  C N N 439 
W4K C19  C Y N 440 
W4K C21  C Y N 441 
W4K C22  C Y N 442 
W4K C23  C Y N 443 
W4K C24  C Y N 444 
W4K O4   O N N 445 
W4K O8   O N N 446 
W4K C9   C Y N 447 
W4K N15  N N N 448 
W4K C17  C N N 449 
W4K O18  O N N 450 
W4K C20  C Y N 451 
W4K F25  F N N 452 
W4K H30  H N N 453 
W4K H29  H N N 454 
W4K H28  H N N 455 
W4K H32  H N N 456 
W4K H31  H N N 457 
W4K H26  H N N 458 
W4K H27  H N N 459 
W4K H35  H N N 460 
W4K H34  H N N 461 
W4K H33  H N N 462 
W4K H37  H N N 463 
W4K H36  H N N 464 
W4K H39  H N N 465 
W4K H40  H N N 466 
W4K H41  H N N 467 
W4K H44  H N N 468 
W4K H43  H N N 469 
W4K H49  H N N 470 
W4K H50  H N N 471 
W4K H51  H N N 472 
W4K H38  H N N 473 
W4K H42  H N N 474 
W4K H46  H N N 475 
W4K H45  H N N 476 
W4K H47  H N N 477 
W4K H48  H N N 478 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
EDO C1  O1   sing N N 92  
EDO C1  C2   sing N N 93  
EDO C1  H11  sing N N 94  
EDO C1  H12  sing N N 95  
EDO O1  HO1  sing N N 96  
EDO C2  O2   sing N N 97  
EDO C2  H21  sing N N 98  
EDO C2  H22  sing N N 99  
EDO O2  HO2  sing N N 100 
GLN N   CA   sing N N 101 
GLN N   H    sing N N 102 
GLN N   H2   sing N N 103 
GLN CA  C    sing N N 104 
GLN CA  CB   sing N N 105 
GLN CA  HA   sing N N 106 
GLN C   O    doub N N 107 
GLN C   OXT  sing N N 108 
GLN CB  CG   sing N N 109 
GLN CB  HB2  sing N N 110 
GLN CB  HB3  sing N N 111 
GLN CG  CD   sing N N 112 
GLN CG  HG2  sing N N 113 
GLN CG  HG3  sing N N 114 
GLN CD  OE1  doub N N 115 
GLN CD  NE2  sing N N 116 
GLN NE2 HE21 sing N N 117 
GLN NE2 HE22 sing N N 118 
GLN OXT HXT  sing N N 119 
GLU N   CA   sing N N 120 
GLU N   H    sing N N 121 
GLU N   H2   sing N N 122 
GLU CA  C    sing N N 123 
GLU CA  CB   sing N N 124 
GLU CA  HA   sing N N 125 
GLU C   O    doub N N 126 
GLU C   OXT  sing N N 127 
GLU CB  CG   sing N N 128 
GLU CB  HB2  sing N N 129 
GLU CB  HB3  sing N N 130 
GLU CG  CD   sing N N 131 
GLU CG  HG2  sing N N 132 
GLU CG  HG3  sing N N 133 
GLU CD  OE1  doub N N 134 
GLU CD  OE2  sing N N 135 
GLU OE2 HE2  sing N N 136 
GLU OXT HXT  sing N N 137 
GLY N   CA   sing N N 138 
GLY N   H    sing N N 139 
GLY N   H2   sing N N 140 
GLY CA  C    sing N N 141 
GLY CA  HA2  sing N N 142 
GLY CA  HA3  sing N N 143 
GLY C   O    doub N N 144 
GLY C   OXT  sing N N 145 
GLY OXT HXT  sing N N 146 
HIS N   CA   sing N N 147 
HIS N   H    sing N N 148 
HIS N   H2   sing N N 149 
HIS CA  C    sing N N 150 
HIS CA  CB   sing N N 151 
HIS CA  HA   sing N N 152 
HIS C   O    doub N N 153 
HIS C   OXT  sing N N 154 
HIS CB  CG   sing N N 155 
HIS CB  HB2  sing N N 156 
HIS CB  HB3  sing N N 157 
HIS CG  ND1  sing Y N 158 
HIS CG  CD2  doub Y N 159 
HIS ND1 CE1  doub Y N 160 
HIS ND1 HD1  sing N N 161 
HIS CD2 NE2  sing Y N 162 
HIS CD2 HD2  sing N N 163 
HIS CE1 NE2  sing Y N 164 
HIS CE1 HE1  sing N N 165 
HIS NE2 HE2  sing N N 166 
HIS OXT HXT  sing N N 167 
HOH O   H1   sing N N 168 
HOH O   H2   sing N N 169 
ILE N   CA   sing N N 170 
ILE N   H    sing N N 171 
ILE N   H2   sing N N 172 
ILE CA  C    sing N N 173 
ILE CA  CB   sing N N 174 
ILE CA  HA   sing N N 175 
ILE C   O    doub N N 176 
ILE C   OXT  sing N N 177 
ILE CB  CG1  sing N N 178 
ILE CB  CG2  sing N N 179 
ILE CB  HB   sing N N 180 
ILE CG1 CD1  sing N N 181 
ILE CG1 HG12 sing N N 182 
ILE CG1 HG13 sing N N 183 
ILE CG2 HG21 sing N N 184 
ILE CG2 HG22 sing N N 185 
ILE CG2 HG23 sing N N 186 
ILE CD1 HD11 sing N N 187 
ILE CD1 HD12 sing N N 188 
ILE CD1 HD13 sing N N 189 
ILE OXT HXT  sing N N 190 
LEU N   CA   sing N N 191 
LEU N   H    sing N N 192 
LEU N   H2   sing N N 193 
LEU CA  C    sing N N 194 
LEU CA  CB   sing N N 195 
LEU CA  HA   sing N N 196 
LEU C   O    doub N N 197 
LEU C   OXT  sing N N 198 
LEU CB  CG   sing N N 199 
LEU CB  HB2  sing N N 200 
LEU CB  HB3  sing N N 201 
LEU CG  CD1  sing N N 202 
LEU CG  CD2  sing N N 203 
LEU CG  HG   sing N N 204 
LEU CD1 HD11 sing N N 205 
LEU CD1 HD12 sing N N 206 
LEU CD1 HD13 sing N N 207 
LEU CD2 HD21 sing N N 208 
LEU CD2 HD22 sing N N 209 
LEU CD2 HD23 sing N N 210 
LEU OXT HXT  sing N N 211 
LYS N   CA   sing N N 212 
LYS N   H    sing N N 213 
LYS N   H2   sing N N 214 
LYS CA  C    sing N N 215 
LYS CA  CB   sing N N 216 
LYS CA  HA   sing N N 217 
LYS C   O    doub N N 218 
LYS C   OXT  sing N N 219 
LYS CB  CG   sing N N 220 
LYS CB  HB2  sing N N 221 
LYS CB  HB3  sing N N 222 
LYS CG  CD   sing N N 223 
LYS CG  HG2  sing N N 224 
LYS CG  HG3  sing N N 225 
LYS CD  CE   sing N N 226 
LYS CD  HD2  sing N N 227 
LYS CD  HD3  sing N N 228 
LYS CE  NZ   sing N N 229 
LYS CE  HE2  sing N N 230 
LYS CE  HE3  sing N N 231 
LYS NZ  HZ1  sing N N 232 
LYS NZ  HZ2  sing N N 233 
LYS NZ  HZ3  sing N N 234 
LYS OXT HXT  sing N N 235 
MET N   CA   sing N N 236 
MET N   H    sing N N 237 
MET N   H2   sing N N 238 
MET CA  C    sing N N 239 
MET CA  CB   sing N N 240 
MET CA  HA   sing N N 241 
MET C   O    doub N N 242 
MET C   OXT  sing N N 243 
MET CB  CG   sing N N 244 
MET CB  HB2  sing N N 245 
MET CB  HB3  sing N N 246 
MET CG  SD   sing N N 247 
MET CG  HG2  sing N N 248 
MET CG  HG3  sing N N 249 
MET SD  CE   sing N N 250 
MET CE  HE1  sing N N 251 
MET CE  HE2  sing N N 252 
MET CE  HE3  sing N N 253 
MET OXT HXT  sing N N 254 
PEG C1  O1   sing N N 255 
PEG C1  C2   sing N N 256 
PEG C1  H11  sing N N 257 
PEG C1  H12  sing N N 258 
PEG O1  HO1  sing N N 259 
PEG C2  O2   sing N N 260 
PEG C2  H21  sing N N 261 
PEG C2  H22  sing N N 262 
PEG O2  C3   sing N N 263 
PEG C3  C4   sing N N 264 
PEG C3  H31  sing N N 265 
PEG C3  H32  sing N N 266 
PEG C4  O4   sing N N 267 
PEG C4  H41  sing N N 268 
PEG C4  H42  sing N N 269 
PEG O4  HO4  sing N N 270 
PHE N   CA   sing N N 271 
PHE N   H    sing N N 272 
PHE N   H2   sing N N 273 
PHE CA  C    sing N N 274 
PHE CA  CB   sing N N 275 
PHE CA  HA   sing N N 276 
PHE C   O    doub N N 277 
PHE C   OXT  sing N N 278 
PHE CB  CG   sing N N 279 
PHE CB  HB2  sing N N 280 
PHE CB  HB3  sing N N 281 
PHE CG  CD1  doub Y N 282 
PHE CG  CD2  sing Y N 283 
PHE CD1 CE1  sing Y N 284 
PHE CD1 HD1  sing N N 285 
PHE CD2 CE2  doub Y N 286 
PHE CD2 HD2  sing N N 287 
PHE CE1 CZ   doub Y N 288 
PHE CE1 HE1  sing N N 289 
PHE CE2 CZ   sing Y N 290 
PHE CE2 HE2  sing N N 291 
PHE CZ  HZ   sing N N 292 
PHE OXT HXT  sing N N 293 
PRO N   CA   sing N N 294 
PRO N   CD   sing N N 295 
PRO N   H    sing N N 296 
PRO CA  C    sing N N 297 
PRO CA  CB   sing N N 298 
PRO CA  HA   sing N N 299 
PRO C   O    doub N N 300 
PRO C   OXT  sing N N 301 
PRO CB  CG   sing N N 302 
PRO CB  HB2  sing N N 303 
PRO CB  HB3  sing N N 304 
PRO CG  CD   sing N N 305 
PRO CG  HG2  sing N N 306 
PRO CG  HG3  sing N N 307 
PRO CD  HD2  sing N N 308 
PRO CD  HD3  sing N N 309 
PRO OXT HXT  sing N N 310 
SER N   CA   sing N N 311 
SER N   H    sing N N 312 
SER N   H2   sing N N 313 
SER CA  C    sing N N 314 
SER CA  CB   sing N N 315 
SER CA  HA   sing N N 316 
SER C   O    doub N N 317 
SER C   OXT  sing N N 318 
SER CB  OG   sing N N 319 
SER CB  HB2  sing N N 320 
SER CB  HB3  sing N N 321 
SER OG  HG   sing N N 322 
SER OXT HXT  sing N N 323 
THR N   CA   sing N N 324 
THR N   H    sing N N 325 
THR N   H2   sing N N 326 
THR CA  C    sing N N 327 
THR CA  CB   sing N N 328 
THR CA  HA   sing N N 329 
THR C   O    doub N N 330 
THR C   OXT  sing N N 331 
THR CB  OG1  sing N N 332 
THR CB  CG2  sing N N 333 
THR CB  HB   sing N N 334 
THR OG1 HG1  sing N N 335 
THR CG2 HG21 sing N N 336 
THR CG2 HG22 sing N N 337 
THR CG2 HG23 sing N N 338 
THR OXT HXT  sing N N 339 
TRP N   CA   sing N N 340 
TRP N   H    sing N N 341 
TRP N   H2   sing N N 342 
TRP CA  C    sing N N 343 
TRP CA  CB   sing N N 344 
TRP CA  HA   sing N N 345 
TRP C   O    doub N N 346 
TRP C   OXT  sing N N 347 
TRP CB  CG   sing N N 348 
TRP CB  HB2  sing N N 349 
TRP CB  HB3  sing N N 350 
TRP CG  CD1  doub Y N 351 
TRP CG  CD2  sing Y N 352 
TRP CD1 NE1  sing Y N 353 
TRP CD1 HD1  sing N N 354 
TRP CD2 CE2  doub Y N 355 
TRP CD2 CE3  sing Y N 356 
TRP NE1 CE2  sing Y N 357 
TRP NE1 HE1  sing N N 358 
TRP CE2 CZ2  sing Y N 359 
TRP CE3 CZ3  doub Y N 360 
TRP CE3 HE3  sing N N 361 
TRP CZ2 CH2  doub Y N 362 
TRP CZ2 HZ2  sing N N 363 
TRP CZ3 CH2  sing Y N 364 
TRP CZ3 HZ3  sing N N 365 
TRP CH2 HH2  sing N N 366 
TRP OXT HXT  sing N N 367 
TYR N   CA   sing N N 368 
TYR N   H    sing N N 369 
TYR N   H2   sing N N 370 
TYR CA  C    sing N N 371 
TYR CA  CB   sing N N 372 
TYR CA  HA   sing N N 373 
TYR C   O    doub N N 374 
TYR C   OXT  sing N N 375 
TYR CB  CG   sing N N 376 
TYR CB  HB2  sing N N 377 
TYR CB  HB3  sing N N 378 
TYR CG  CD1  doub Y N 379 
TYR CG  CD2  sing Y N 380 
TYR CD1 CE1  sing Y N 381 
TYR CD1 HD1  sing N N 382 
TYR CD2 CE2  doub Y N 383 
TYR CD2 HD2  sing N N 384 
TYR CE1 CZ   doub Y N 385 
TYR CE1 HE1  sing N N 386 
TYR CE2 CZ   sing Y N 387 
TYR CE2 HE2  sing N N 388 
TYR CZ  OH   sing N N 389 
TYR OH  HH   sing N N 390 
TYR OXT HXT  sing N N 391 
VAL N   CA   sing N N 392 
VAL N   H    sing N N 393 
VAL N   H2   sing N N 394 
VAL CA  C    sing N N 395 
VAL CA  CB   sing N N 396 
VAL CA  HA   sing N N 397 
VAL C   O    doub N N 398 
VAL C   OXT  sing N N 399 
VAL CB  CG1  sing N N 400 
VAL CB  CG2  sing N N 401 
VAL CB  HB   sing N N 402 
VAL CG1 HG11 sing N N 403 
VAL CG1 HG12 sing N N 404 
VAL CG1 HG13 sing N N 405 
VAL CG2 HG21 sing N N 406 
VAL CG2 HG22 sing N N 407 
VAL CG2 HG23 sing N N 408 
VAL OXT HXT  sing N N 409 
W4K C22 C21  doub Y N 410 
W4K C22 C23  sing Y N 411 
W4K C21 C20  sing Y N 412 
W4K C23 C24  doub Y N 413 
W4K C20 C19  doub Y N 414 
W4K C1  C2   sing N N 415 
W4K C24 C19  sing Y N 416 
W4K C24 F25  sing N N 417 
W4K C19 C12  sing N N 418 
W4K C11 C12  doub Y N 419 
W4K C11 C10  sing Y N 420 
W4K C12 C13  sing Y N 421 
W4K C10 C9   doub Y N 422 
W4K C2  C3   sing N N 423 
W4K C13 C14  doub Y N 424 
W4K C9  C14  sing Y N 425 
W4K C9  C3   sing N N 426 
W4K C14 N15  sing N N 427 
W4K C3  O4   sing N N 428 
W4K N15 C16  sing N N 429 
W4K C16 C17  sing N N 430 
W4K O4  C5   sing N N 431 
W4K C17 O18  sing N N 432 
W4K C6  C5   sing N N 433 
W4K C5  C7   sing N N 434 
W4K O8  C7   sing N N 435 
W4K C1  H30  sing N N 436 
W4K C1  H29  sing N N 437 
W4K C1  H28  sing N N 438 
W4K C2  H32  sing N N 439 
W4K C2  H31  sing N N 440 
W4K C3  H26  sing N N 441 
W4K C5  H27  sing N N 442 
W4K C6  H35  sing N N 443 
W4K C6  H34  sing N N 444 
W4K C6  H33  sing N N 445 
W4K C7  H37  sing N N 446 
W4K C7  H36  sing N N 447 
W4K C10 H39  sing N N 448 
W4K C11 H40  sing N N 449 
W4K C13 H41  sing N N 450 
W4K C16 H44  sing N N 451 
W4K C16 H43  sing N N 452 
W4K C21 H49  sing N N 453 
W4K C22 H50  sing N N 454 
W4K C23 H51  sing N N 455 
W4K O8  H38  sing N N 456 
W4K N15 H42  sing N N 457 
W4K C17 H46  sing N N 458 
W4K C17 H45  sing N N 459 
W4K O18 H47  sing N N 460 
W4K C20 H48  sing N N 461 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    8QM9 
_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]   0.021149 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002115 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014436 
_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]   0.015544 
_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 
F 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ALA A 1 9   ? 3.099   -22.659 -9.413  1.00 46.07 ? 11  ALA A N   1 
ATOM   2    C CA  . ALA A 1 9   ? 4.192   -21.934 -10.080 1.00 44.98 ? 11  ALA A CA  1 
ATOM   3    C C   . ALA A 1 9   ? 4.909   -21.062 -9.072  1.00 43.81 ? 11  ALA A C   1 
ATOM   4    O O   . ALA A 1 9   ? 4.263   -20.423 -8.242  1.00 44.74 ? 11  ALA A O   1 
ATOM   5    C CB  . ALA A 1 9   ? 3.642   -21.069 -11.202 1.00 44.78 ? 11  ALA A CB  1 
ATOM   6    N N   . ARG A 1 10  ? 6.247   -21.016 -9.128  1.00 41.97 ? 12  ARG A N   1 
ATOM   7    C CA  . ARG A 1 10  ? 7.028   -20.283 -8.121  1.00 39.08 ? 12  ARG A CA  1 
ATOM   8    C C   . ARG A 1 10  ? 6.720   -18.812 -8.190  1.00 37.29 ? 12  ARG A C   1 
ATOM   9    O O   . ARG A 1 10  ? 6.641   -18.245 -9.277  1.00 38.42 ? 12  ARG A O   1 
ATOM   10   C CB  . ARG A 1 10  ? 8.515   -20.511 -8.335  1.00 39.11 ? 12  ARG A CB  1 
ATOM   11   C CG  . ARG A 1 10  ? 9.418   -19.975 -7.201  1.00 42.00 ? 12  ARG A CG  1 
ATOM   12   C CD  . ARG A 1 10  ? 10.876  -20.277 -7.469  1.00 44.13 ? 12  ARG A CD  1 
ATOM   13   N NE  . ARG A 1 10  ? 11.072  -21.718 -7.542  1.00 46.47 ? 12  ARG A NE  1 
ATOM   14   C CZ  . ARG A 1 10  ? 11.129  -22.531 -6.487  1.00 46.25 ? 12  ARG A CZ  1 
ATOM   15   N NH1 . ARG A 1 10  ? 11.284  -23.843 -6.661  1.00 41.65 ? 12  ARG A NH1 1 
ATOM   16   N NH2 . ARG A 1 10  ? 11.007  -22.041 -5.247  1.00 44.98 ? 12  ARG A NH2 1 
ATOM   17   N N   . ILE A 1 11  ? 6.537   -18.196 -7.039  1.00 35.00 ? 13  ILE A N   1 
ATOM   18   C CA  . ILE A 1 11  ? 6.412   -16.758 -6.953  1.00 33.74 ? 13  ILE A CA  1 
ATOM   19   C C   . ILE A 1 11  ? 7.829   -16.110 -7.007  1.00 32.55 ? 13  ILE A C   1 
ATOM   20   O O   . ILE A 1 11  ? 8.615   -16.202 -6.050  1.00 31.34 ? 13  ILE A O   1 
ATOM   21   C CB  . ILE A 1 11  ? 5.603   -16.371 -5.698  1.00 33.33 ? 13  ILE A CB  1 
ATOM   22   C CG1 . ILE A 1 11  ? 4.222   -17.089 -5.696  1.00 35.14 ? 13  ILE A CG1 1 
ATOM   23   C CG2 . ILE A 1 11  ? 5.381   -14.892 -5.689  1.00 32.97 ? 13  ILE A CG2 1 
ATOM   24   C CD1 . ILE A 1 11  ? 3.478   -17.008 -4.394  1.00 36.38 ? 13  ILE A CD1 1 
ATOM   25   N N   . ILE A 1 12  ? 8.143   -15.456 -8.132  1.00 31.63 ? 14  ILE A N   1 
ATOM   26   C CA  . ILE A 1 12  ? 9.455   -14.859 -8.342  1.00 31.13 ? 14  ILE A CA  1 
ATOM   27   C C   . ILE A 1 12  ? 9.295   -13.386 -8.603  1.00 30.18 ? 14  ILE A C   1 
ATOM   28   O O   . ILE A 1 12  ? 8.546   -12.989 -9.512  1.00 29.49 ? 14  ILE A O   1 
ATOM   29   C CB  . ILE A 1 12  ? 10.159  -15.510 -9.549  1.00 30.66 ? 14  ILE A CB  1 
ATOM   30   C CG1 . ILE A 1 12  ? 10.221  -17.078 -9.399  1.00 30.32 ? 14  ILE A CG1 1 
ATOM   31   C CG2 . ILE A 1 12  ? 11.535  -14.848 -9.754  1.00 30.87 ? 14  ILE A CG2 1 
ATOM   32   C CD1 . ILE A 1 12  ? 10.703  -17.686 -10.545 1.00 32.14 ? 14  ILE A CD1 1 
ATOM   33   N N   . TYR A 1 13  ? 10.003  -12.559 -7.813  1.00 29.86 ? 15  TYR A N   1 
ATOM   34   C CA  . TYR A 1 13  ? 10.038  -11.115 -8.005  1.00 29.69 ? 15  TYR A CA  1 
ATOM   35   C C   . TYR A 1 13  ? 11.460  -10.716 -8.389  1.00 30.23 ? 15  TYR A C   1 
ATOM   36   O O   . TYR A 1 13  ? 12.378  -11.073 -7.652  1.00 30.76 ? 15  TYR A O   1 
ATOM   37   C CB  . TYR A 1 13  ? 9.674   -10.424 -6.703  1.00 30.11 ? 15  TYR A CB  1 
ATOM   38   C CG  . TYR A 1 13  ? 8.276   -10.734 -6.248  1.00 31.88 ? 15  TYR A CG  1 
ATOM   39   C CD1 . TYR A 1 13  ? 7.178   -10.185 -6.896  1.00 33.82 ? 15  TYR A CD1 1 
ATOM   40   C CD2 . TYR A 1 13  ? 8.042   -11.572 -5.179  1.00 33.03 ? 15  TYR A CD2 1 
ATOM   41   C CE1 . TYR A 1 13  ? 5.887   -10.446 -6.477  1.00 34.30 ? 15  TYR A CE1 1 
ATOM   42   C CE2 . TYR A 1 13  ? 6.748   -11.838 -4.741  1.00 33.32 ? 15  TYR A CE2 1 
ATOM   43   C CZ  . TYR A 1 13  ? 5.675   -11.290 -5.409  1.00 34.21 ? 15  TYR A CZ  1 
ATOM   44   O OH  . TYR A 1 13  ? 4.400   -11.563 -5.029  1.00 33.45 ? 15  TYR A OH  1 
ATOM   45   N N   . ASP A 1 14  ? 11.659  -10.032 -9.512  1.00 29.08 ? 16  ASP A N   1 
ATOM   46   C CA  . ASP A 1 14  ? 12.931  -9.350  -9.771  1.00 30.67 ? 16  ASP A CA  1 
ATOM   47   C C   . ASP A 1 14  ? 13.148  -8.097  -8.874  1.00 29.99 ? 16  ASP A C   1 
ATOM   48   O O   . ASP A 1 14  ? 12.222  -7.599  -8.196  1.00 29.85 ? 16  ASP A O   1 
ATOM   49   C CB  . ASP A 1 14  ? 13.128  -9.032  -11.274 1.00 32.31 ? 16  ASP A CB  1 
ATOM   50   C CG  . ASP A 1 14  ? 12.134  -8.105  -11.932 1.00 34.66 ? 16  ASP A CG  1 
ATOM   51   O OD1 . ASP A 1 14  ? 11.617  -7.225  -11.254 1.00 35.10 ? 16  ASP A OD1 1 
ATOM   52   O OD2 . ASP A 1 14  ? 11.877  -8.280  -13.121 1.00 36.82 ? 16  ASP A OD2 1 
ATOM   53   N N   . ARG A 1 15  ? 14.399  -7.600  -8.889  1.00 28.78 ? 17  ARG A N   1 
ATOM   54   C CA  A ARG A 1 15  ? 14.810  -6.456  -8.084  0.50 28.23 ? 17  ARG A CA  1 
ATOM   55   C CA  B ARG A 1 15  ? 14.819  -6.448  -8.091  0.50 28.81 ? 17  ARG A CA  1 
ATOM   56   C C   . ARG A 1 15  ? 13.939  -5.213  -8.320  1.00 30.41 ? 17  ARG A C   1 
ATOM   57   O O   . ARG A 1 15  ? 13.600  -4.540  -7.362  1.00 30.88 ? 17  ARG A O   1 
ATOM   58   C CB  A ARG A 1 15  ? 16.274  -6.122  -8.373  0.50 27.42 ? 17  ARG A CB  1 
ATOM   59   C CB  B ARG A 1 15  ? 16.283  -6.096  -8.399  0.50 29.48 ? 17  ARG A CB  1 
ATOM   60   C CG  A ARG A 1 15  ? 16.844  -5.102  -7.424  0.50 25.84 ? 17  ARG A CG  1 
ATOM   61   C CG  B ARG A 1 15  ? 16.815  -4.959  -7.535  0.50 31.00 ? 17  ARG A CG  1 
ATOM   62   C CD  A ARG A 1 15  ? 18.292  -4.859  -7.742  0.50 23.54 ? 17  ARG A CD  1 
ATOM   63   C CD  B ARG A 1 15  ? 18.183  -4.477  -7.979  0.50 31.70 ? 17  ARG A CD  1 
ATOM   64   N NE  A ARG A 1 15  ? 18.870  -3.805  -6.908  0.50 20.49 ? 17  ARG A NE  1 
ATOM   65   N NE  B ARG A 1 15  ? 19.227  -5.325  -7.427  0.50 29.72 ? 17  ARG A NE  1 
ATOM   66   C CZ  A ARG A 1 15  ? 18.724  -2.496  -7.072  0.50 21.27 ? 17  ARG A CZ  1 
ATOM   67   C CZ  B ARG A 1 15  ? 20.220  -5.932  -8.066  0.50 23.15 ? 17  ARG A CZ  1 
ATOM   68   N NH1 A ARG A 1 15  ? 17.995  -2.021  -8.071  0.50 20.84 ? 17  ARG A NH1 1 
ATOM   69   N NH1 B ARG A 1 15  ? 20.361  -5.805  -9.390  0.50 25.25 ? 17  ARG A NH1 1 
ATOM   70   N NH2 A ARG A 1 15  ? 19.307  -1.650  -6.236  0.50 21.01 ? 17  ARG A NH2 1 
ATOM   71   N NH2 B ARG A 1 15  ? 21.073  -6.667  -7.401  0.50 12.64 ? 17  ARG A NH2 1 
ATOM   72   N N   . ALA A 1 16  ? 13.566  -4.902  -9.587  1.00 32.27 ? 18  ALA A N   1 
ATOM   73   C CA  . ALA A 1 16  ? 12.719  -3.736  -9.890  1.00 34.93 ? 18  ALA A CA  1 
ATOM   74   C C   . ALA A 1 16  ? 11.334  -3.809  -9.282  1.00 37.23 ? 18  ALA A C   1 
ATOM   75   O O   . ALA A 1 16  ? 10.856  -2.836  -8.709  1.00 38.56 ? 18  ALA A O   1 
ATOM   76   C CB  . ALA A 1 16  ? 12.607  -3.546  -11.393 1.00 34.95 ? 18  ALA A CB  1 
ATOM   77   N N   . PHE A 1 17  ? 10.678  -4.961  -9.374  1.00 38.23 ? 19  PHE A N   1 
ATOM   78   C CA  . PHE A 1 17  ? 9.364   -5.149  -8.793  1.00 39.57 ? 19  PHE A CA  1 
ATOM   79   C C   . PHE A 1 17  ? 9.396   -4.911  -7.265  1.00 39.97 ? 19  PHE A C   1 
ATOM   80   O O   . PHE A 1 17  ? 8.635   -4.091  -6.761  1.00 39.57 ? 19  PHE A O   1 
ATOM   81   C CB  . PHE A 1 17  ? 8.832   -6.545  -9.151  1.00 40.47 ? 19  PHE A CB  1 
ATOM   82   C CG  . PHE A 1 17  ? 7.360   -6.667  -8.911  1.00 41.21 ? 19  PHE A CG  1 
ATOM   83   C CD1 . PHE A 1 17  ? 6.872   -6.979  -7.659  1.00 41.51 ? 19  PHE A CD1 1 
ATOM   84   C CD2 . PHE A 1 17  ? 6.457   -6.348  -9.906  1.00 43.54 ? 19  PHE A CD2 1 
ATOM   85   C CE1 . PHE A 1 17  ? 5.502   -7.047  -7.425  1.00 43.04 ? 19  PHE A CE1 1 
ATOM   86   C CE2 . PHE A 1 17  ? 5.093   -6.416  -9.672  1.00 44.71 ? 19  PHE A CE2 1 
ATOM   87   C CZ  . PHE A 1 17  ? 4.627   -6.786  -8.429  1.00 43.59 ? 19  PHE A CZ  1 
ATOM   88   N N   . LEU A 1 18  ? 10.290  -5.603  -6.522  1.00 39.72 ? 20  LEU A N   1 
ATOM   89   C CA  . LEU A 1 18  ? 10.388  -5.426  -5.059  1.00 38.45 ? 20  LEU A CA  1 
ATOM   90   C C   . LEU A 1 18  ? 10.569  -3.943  -4.688  1.00 39.03 ? 20  LEU A C   1 
ATOM   91   O O   . LEU A 1 18  ? 9.882   -3.434  -3.811  1.00 39.95 ? 20  LEU A O   1 
ATOM   92   C CB  . LEU A 1 18  ? 11.524  -6.323  -4.458  1.00 36.44 ? 20  LEU A CB  1 
ATOM   93   C CG  . LEU A 1 18  ? 11.321  -7.827  -4.617  1.00 35.72 ? 20  LEU A CG  1 
ATOM   94   C CD1 . LEU A 1 18  ? 12.513  -8.607  -4.138  1.00 36.75 ? 20  LEU A CD1 1 
ATOM   95   C CD2 . LEU A 1 18  ? 10.083  -8.289  -3.902  1.00 36.40 ? 20  LEU A CD2 1 
ATOM   96   N N   . MET A 1 19  ? 11.457  -3.265  -5.369  1.00 39.67 ? 21  MET A N   1 
ATOM   97   C CA  . MET A 1 19  ? 11.689  -1.845  -5.152  1.00 39.99 ? 21  MET A CA  1 
ATOM   98   C C   . MET A 1 19  ? 10.442  -0.952  -5.411  1.00 42.74 ? 21  MET A C   1 
ATOM   99   O O   . MET A 1 19  ? 10.253  0.033   -4.708  1.00 43.34 ? 21  MET A O   1 
ATOM   100  C CB  . MET A 1 19  ? 12.852  -1.373  -5.999  1.00 38.93 ? 21  MET A CB  1 
ATOM   101  C CG  . MET A 1 19  ? 14.193  -2.004  -5.674  1.00 38.80 ? 21  MET A CG  1 
ATOM   102  S SD  . MET A 1 19  ? 14.753  -1.884  -3.956  1.00 42.31 ? 21  MET A SD  1 
ATOM   103  C CE  . MET A 1 19  ? 16.465  -1.861  -4.145  1.00 45.86 ? 21  MET A CE  1 
ATOM   104  N N   . ALA A 1 20  ? 9.591   -1.287  -6.382  1.00 44.42 ? 22  ALA A N   1 
ATOM   105  C CA  . ALA A 1 20  ? 8.368   -0.505  -6.650  1.00 45.66 ? 22  ALA A CA  1 
ATOM   106  C C   . ALA A 1 20  ? 7.259   -0.762  -5.604  1.00 47.85 ? 22  ALA A C   1 
ATOM   107  O O   . ALA A 1 20  ? 6.411   0.107   -5.355  1.00 47.55 ? 22  ALA A O   1 
ATOM   108  C CB  . ALA A 1 20  ? 7.862   -0.834  -8.041  1.00 45.40 ? 22  ALA A CB  1 
ATOM   109  N N   . CYS A 1 21  ? 7.261   -1.960  -4.974  1.00 49.22 ? 23  CYS A N   1 
ATOM   110  C CA  . CYS A 1 21  ? 6.343   -2.259  -3.865  1.00 50.48 ? 23  CYS A CA  1 
ATOM   111  C C   . CYS A 1 21  ? 6.715   -1.552  -2.527  1.00 50.95 ? 23  CYS A C   1 
ATOM   112  O O   . CYS A 1 21  ? 6.027   -1.767  -1.528  1.00 51.74 ? 23  CYS A O   1 
ATOM   113  C CB  . CYS A 1 21  ? 6.252   -3.764  -3.665  1.00 51.31 ? 23  CYS A CB  1 
ATOM   114  S SG  . CYS A 1 21  ? 5.687   -4.693  -5.113  1.00 55.56 ? 23  CYS A SG  1 
ATOM   115  N N   . ARG A 1 22  ? 7.778   -0.737  -2.519  1.00 50.33 ? 24  ARG A N   1 
ATOM   116  C CA  A ARG A 1 22  ? 8.313   -0.099  -1.318  0.50 50.89 ? 24  ARG A CA  1 
ATOM   117  C CA  B ARG A 1 22  ? 8.345   -0.095  -1.333  0.50 51.31 ? 24  ARG A CA  1 
ATOM   118  C C   . ARG A 1 22  ? 7.662   1.265   -1.062  1.00 54.38 ? 24  ARG A C   1 
ATOM   119  O O   . ARG A 1 22  ? 7.193   1.910   -2.008  1.00 55.30 ? 24  ARG A O   1 
ATOM   120  C CB  A ARG A 1 22  ? 9.821   0.106   -1.499  0.50 48.00 ? 24  ARG A CB  1 
ATOM   121  C CB  B ARG A 1 22  ? 9.835   0.156   -1.613  0.50 49.54 ? 24  ARG A CB  1 
ATOM   122  C CG  A ARG A 1 22  ? 10.513  0.698   -0.307  0.50 44.37 ? 24  ARG A CG  1 
ATOM   123  C CG  B ARG A 1 22  ? 10.681  0.575   -0.461  0.50 48.03 ? 24  ARG A CG  1 
ATOM   124  C CD  A ARG A 1 22  ? 11.990  0.793   -0.555  0.50 42.15 ? 24  ARG A CD  1 
ATOM   125  C CD  B ARG A 1 22  ? 11.807  1.474   -0.957  0.50 47.81 ? 24  ARG A CD  1 
ATOM   126  N NE  A ARG A 1 22  ? 12.721  1.180   0.650   0.50 39.52 ? 24  ARG A NE  1 
ATOM   127  N NE  B ARG A 1 22  ? 13.081  1.272   -0.270  0.50 46.57 ? 24  ARG A NE  1 
ATOM   128  C CZ  A ARG A 1 22  ? 14.048  1.269   0.729   0.50 36.56 ? 24  ARG A CZ  1 
ATOM   129  C CZ  B ARG A 1 22  ? 13.321  1.591   0.998   0.50 44.75 ? 24  ARG A CZ  1 
ATOM   130  N NH1 A ARG A 1 22  ? 14.805  0.998   -0.328  0.50 35.69 ? 24  ARG A NH1 1 
ATOM   131  N NH1 B ARG A 1 22  ? 12.359  2.125   1.752   0.50 42.45 ? 24  ARG A NH1 1 
ATOM   132  N NH2 A ARG A 1 22  ? 14.627  1.626   1.867   0.50 34.61 ? 24  ARG A NH2 1 
ATOM   133  N NH2 B ARG A 1 22  ? 14.517  1.369   1.528   0.50 42.00 ? 24  ARG A NH2 1 
ATOM   134  N N   . GLY A 1 23  ? 7.660   1.687   0.211   1.00 57.93 ? 25  GLY A N   1 
ATOM   135  C CA  . GLY A 1 23  ? 7.086   2.964   0.643   1.00 60.82 ? 25  GLY A CA  1 
ATOM   136  C C   . GLY A 1 23  ? 5.608   2.866   1.012   1.00 63.45 ? 25  GLY A C   1 
ATOM   137  O O   . GLY A 1 23  ? 4.988   3.877   1.386   1.00 64.44 ? 25  GLY A O   1 
ATOM   138  N N   . GLY A 1 24  ? 5.044   1.663   0.907   1.00 63.83 ? 26  GLY A N   1 
ATOM   139  C CA  . GLY A 1 24  ? 3.631   1.418   1.154   1.00 64.60 ? 26  GLY A CA  1 
ATOM   140  C C   . GLY A 1 24  ? 2.756   2.085   0.125   1.00 65.57 ? 26  GLY A C   1 
ATOM   141  O O   . GLY A 1 24  ? 3.224   2.501   -0.943  1.00 65.38 ? 26  GLY A O   1 
ATOM   142  N N   . GLY A 1 25  ? 1.480   2.180   0.465   1.00 66.35 ? 27  GLY A N   1 
ATOM   143  C CA  . GLY A 1 25  ? 0.501   2.898   -0.340  1.00 67.15 ? 27  GLY A CA  1 
ATOM   144  C C   . GLY A 1 25  ? -0.779  2.118   -0.482  1.00 67.51 ? 27  GLY A C   1 
ATOM   145  O O   . GLY A 1 25  ? -1.870  2.668   -0.293  1.00 68.45 ? 27  GLY A O   1 
ATOM   146  N N   . GLY A 1 26  ? -0.638  0.836   -0.818  1.00 66.61 ? 28  GLY A N   1 
ATOM   147  C CA  . GLY A 1 26  ? -1.771  -0.030  -1.122  1.00 65.70 ? 28  GLY A CA  1 
ATOM   148  C C   . GLY A 1 26  ? -2.767  -0.143  0.008   1.00 64.17 ? 28  GLY A C   1 
ATOM   149  O O   . GLY A 1 26  ? -2.379  -0.264  1.174   1.00 64.52 ? 28  GLY A O   1 
ATOM   150  N N   . GLU A 1 27  ? -4.062  -0.096  -0.338  1.00 62.09 ? 29  GLU A N   1 
ATOM   151  C CA  . GLU A 1 27  ? -5.144  -0.224  0.626   1.00 60.33 ? 29  GLU A CA  1 
ATOM   152  C C   . GLU A 1 27  ? -5.258  -1.678  1.168   1.00 57.02 ? 29  GLU A C   1 
ATOM   153  O O   . GLU A 1 27  ? -5.746  -1.866  2.279   1.00 57.47 ? 29  GLU A O   1 
ATOM   154  C CB  . GLU A 1 27  ? -6.478  0.217   -0.031  1.00 64.99 ? 29  GLU A CB  1 
ATOM   155  C CG  . GLU A 1 27  ? -6.563  1.698   -0.381  1.00 72.01 ? 29  GLU A CG  1 
ATOM   156  C CD  . GLU A 1 27  ? -7.741  2.078   -1.268  1.00 81.27 ? 29  GLU A CD  1 
ATOM   157  O OE1 . GLU A 1 27  ? -8.891  2.069   -0.770  1.00 83.86 ? 29  GLU A OE1 1 
ATOM   158  O OE2 . GLU A 1 27  ? -7.514  2.389   -2.463  1.00 83.54 ? 29  GLU A OE2 1 
ATOM   159  N N   . ASN A 1 28  ? -4.803  -2.692  0.390   1.00 53.53 ? 30  ASN A N   1 
ATOM   160  C CA  . ASN A 1 28  ? -4.946  -4.118  0.698   1.00 51.65 ? 30  ASN A CA  1 
ATOM   161  C C   . ASN A 1 28  ? -6.422  -4.435  0.837   1.00 50.78 ? 30  ASN A C   1 
ATOM   162  O O   . ASN A 1 28  ? -6.848  -5.065  1.812   1.00 50.87 ? 30  ASN A O   1 
ATOM   163  C CB  . ASN A 1 28  ? -4.143  -4.604  1.949   1.00 49.66 ? 30  ASN A CB  1 
ATOM   164  C CG  . ASN A 1 28  ? -4.146  -6.113  2.063   1.00 50.32 ? 30  ASN A CG  1 
ATOM   165  O OD1 . ASN A 1 28  ? -4.191  -6.823  1.053   1.00 50.42 ? 30  ASN A OD1 1 
ATOM   166  N ND2 . ASN A 1 28  ? -4.104  -6.654  3.283   1.00 49.73 ? 30  ASN A ND2 1 
ATOM   167  N N   . LEU A 1 29  ? -7.216  -3.999  -0.163  1.00 49.68 ? 31  LEU A N   1 
ATOM   168  C CA  . LEU A 1 29  ? -8.652  -4.265  -0.171  1.00 49.60 ? 31  LEU A CA  1 
ATOM   169  C C   . LEU A 1 29  ? -8.868  -5.782  -0.195  1.00 49.34 ? 31  LEU A C   1 
ATOM   170  O O   . LEU A 1 29  ? -8.077  -6.502  -0.811  1.00 48.95 ? 31  LEU A O   1 
ATOM   171  C CB  . LEU A 1 29  ? -9.345  -3.630  -1.388  1.00 49.97 ? 31  LEU A CB  1 
ATOM   172  C CG  . LEU A 1 29  ? -9.229  -2.124  -1.556  1.00 52.37 ? 31  LEU A CG  1 
ATOM   173  C CD1 . LEU A 1 29  ? -9.952  -1.678  -2.831  1.00 53.60 ? 31  LEU A CD1 1 
ATOM   174  C CD2 . LEU A 1 29  ? -9.795  -1.386  -0.336  1.00 53.28 ? 31  LEU A CD2 1 
ATOM   175  N N   . TYR A 1 30  ? -9.927  -6.254  0.488   1.00 49.21 ? 32  TYR A N   1 
ATOM   176  C CA  . TYR A 1 30  ? -10.275 -7.660  0.601   1.00 48.89 ? 32  TYR A CA  1 
ATOM   177  C C   . TYR A 1 30  ? -9.149  -8.536  1.162   1.00 48.43 ? 32  TYR A C   1 
ATOM   178  O O   . TYR A 1 30  ? -9.228  -9.744  1.030   1.00 48.79 ? 32  TYR A O   1 
ATOM   179  C CB  . TYR A 1 30  ? -10.754 -8.185  -0.760  1.00 49.17 ? 32  TYR A CB  1 
ATOM   180  C CG  . TYR A 1 30  ? -11.741 -7.253  -1.430  1.00 50.19 ? 32  TYR A CG  1 
ATOM   181  C CD1 . TYR A 1 30  ? -13.066 -7.205  -1.024  1.00 51.67 ? 32  TYR A CD1 1 
ATOM   182  C CD2 . TYR A 1 30  ? -11.341 -6.401  -2.447  1.00 50.72 ? 32  TYR A CD2 1 
ATOM   183  C CE1 . TYR A 1 30  ? -13.972 -6.333  -1.618  1.00 52.43 ? 32  TYR A CE1 1 
ATOM   184  C CE2 . TYR A 1 30  ? -12.239 -5.527  -3.054  1.00 52.21 ? 32  TYR A CE2 1 
ATOM   185  C CZ  . TYR A 1 30  ? -13.557 -5.497  -2.637  1.00 53.31 ? 32  TYR A CZ  1 
ATOM   186  O OH  . TYR A 1 30  ? -14.457 -4.631  -3.217  1.00 55.78 ? 32  TYR A OH  1 
ATOM   187  N N   . PHE A 1 31  ? -8.115  -7.967  1.792   1.00 48.45 ? 33  PHE A N   1 
ATOM   188  C CA  . PHE A 1 31  ? -6.920  -8.754  2.200   1.00 49.11 ? 33  PHE A CA  1 
ATOM   189  C C   . PHE A 1 31  ? -6.219  -9.452  1.007   1.00 49.17 ? 33  PHE A C   1 
ATOM   190  O O   . PHE A 1 31  ? -5.540  -10.483 1.183   1.00 48.75 ? 33  PHE A O   1 
ATOM   191  C CB  . PHE A 1 31  ? -7.287  -9.749  3.327   1.00 49.18 ? 33  PHE A CB  1 
ATOM   192  C CG  . PHE A 1 31  ? -7.628  -9.017  4.606   1.00 49.79 ? 33  PHE A CG  1 
ATOM   193  C CD1 . PHE A 1 31  ? -6.650  -8.332  5.314   1.00 50.14 ? 33  PHE A CD1 1 
ATOM   194  C CD2 . PHE A 1 31  ? -8.928  -8.974  5.072   1.00 49.91 ? 33  PHE A CD2 1 
ATOM   195  C CE1 . PHE A 1 31  ? -6.969  -7.641  6.469   1.00 50.59 ? 33  PHE A CE1 1 
ATOM   196  C CE2 . PHE A 1 31  ? -9.245  -8.273  6.231   1.00 50.04 ? 33  PHE A CE2 1 
ATOM   197  C CZ  . PHE A 1 31  ? -8.266  -7.618  6.924   1.00 50.26 ? 33  PHE A CZ  1 
ATOM   198  N N   . GLN A 1 32  ? -6.366  -8.854  -0.214  1.00 48.80 ? 34  GLN A N   1 
ATOM   199  C CA  . GLN A 1 32  ? -5.934  -9.475  -1.476  1.00 47.97 ? 34  GLN A CA  1 
ATOM   200  C C   . GLN A 1 32  ? -5.042  -8.634  -2.341  1.00 46.37 ? 34  GLN A C   1 
ATOM   201  O O   . GLN A 1 32  ? -4.794  -9.006  -3.482  1.00 46.38 ? 34  GLN A O   1 
ATOM   202  C CB  . GLN A 1 32  ? -7.177  -9.892  -2.289  1.00 49.17 ? 34  GLN A CB  1 
ATOM   203  C CG  . GLN A 1 32  ? -7.845  -11.135 -1.752  1.00 51.90 ? 34  GLN A CG  1 
ATOM   204  C CD  . GLN A 1 32  ? -8.947  -11.586 -2.674  1.00 56.77 ? 34  GLN A CD  1 
ATOM   205  O OE1 . GLN A 1 32  ? -8.726  -11.801 -3.876  1.00 57.53 ? 34  GLN A OE1 1 
ATOM   206  N NE2 . GLN A 1 32  ? -10.161 -11.738 -2.138  1.00 57.92 ? 34  GLN A NE2 1 
ATOM   207  N N   . GLY A 1 33  ? -4.550  -7.532  -1.813  1.00 45.73 ? 35  GLY A N   1 
ATOM   208  C CA  . GLY A 1 33  ? -3.778  -6.572  -2.567  1.00 45.56 ? 35  GLY A CA  1 
ATOM   209  C C   . GLY A 1 33  ? -2.297  -6.631  -2.272  1.00 45.60 ? 35  GLY A C   1 
ATOM   210  O O   . GLY A 1 33  ? -1.534  -6.014  -3.004  1.00 46.92 ? 35  GLY A O   1 
ATOM   211  N N   . LYS A 1 34  ? -1.864  -7.350  -1.200  1.00 43.54 ? 36  LYS A N   1 
ATOM   212  C CA  . LYS A 1 34  ? -0.436  -7.517  -0.907  1.00 41.40 ? 36  LYS A CA  1 
ATOM   213  C C   . LYS A 1 34  ? 0.116   -8.614  -1.789  1.00 39.33 ? 36  LYS A C   1 
ATOM   214  O O   . LYS A 1 34  ? -0.620  -9.518  -2.189  1.00 38.60 ? 36  LYS A O   1 
ATOM   215  C CB  . LYS A 1 34  ? -0.201  -7.880  0.571   1.00 40.63 ? 36  LYS A CB  1 
ATOM   216  C CG  . LYS A 1 34  ? -0.341  -6.712  1.511   1.00 40.38 ? 36  LYS A CG  1 
ATOM   217  C CD  . LYS A 1 34  ? -0.252  -7.141  2.954   1.00 41.13 ? 36  LYS A CD  1 
ATOM   218  C CE  . LYS A 1 34  ? -0.166  -5.949  3.889   1.00 41.79 ? 36  LYS A CE  1 
ATOM   219  N NZ  . LYS A 1 34  ? -0.094  -6.372  5.323   1.00 40.74 ? 36  LYS A NZ  1 
ATOM   220  N N   . HIS A 1 35  ? 1.417   -8.540  -2.087  1.00 37.66 ? 37  HIS A N   1 
ATOM   221  C CA  . HIS A 1 35  ? 2.049   -9.457  -3.018  1.00 37.31 ? 37  HIS A CA  1 
ATOM   222  C C   . HIS A 1 35  ? 2.645   -10.595 -2.243  1.00 36.09 ? 37  HIS A C   1 
ATOM   223  O O   . HIS A 1 35  ? 3.588   -10.362 -1.489  1.00 35.47 ? 37  HIS A O   1 
ATOM   224  C CB  . HIS A 1 35  ? 3.111   -8.734  -3.824  1.00 38.39 ? 37  HIS A CB  1 
ATOM   225  C CG  . HIS A 1 35  ? 2.508   -7.699  -4.723  1.00 41.58 ? 37  HIS A CG  1 
ATOM   226  N ND1 . HIS A 1 35  ? 2.376   -6.383  -4.319  1.00 43.19 ? 37  HIS A ND1 1 
ATOM   227  C CD2 . HIS A 1 35  ? 2.018   -7.825  -5.979  1.00 42.37 ? 37  HIS A CD2 1 
ATOM   228  C CE1 . HIS A 1 35  ? 1.812   -5.751  -5.336  1.00 44.27 ? 37  HIS A CE1 1 
ATOM   229  N NE2 . HIS A 1 35  ? 1.577   -6.584  -6.358  1.00 43.73 ? 37  HIS A NE2 1 
ATOM   230  N N   . PRO A 1 36  ? 2.111   -11.825 -2.384  1.00 35.95 ? 38  PRO A N   1 
ATOM   231  C CA  . PRO A 1 36  ? 2.592   -12.921 -1.547  1.00 34.72 ? 38  PRO A CA  1 
ATOM   232  C C   . PRO A 1 36  ? 3.988   -13.370 -1.898  1.00 33.31 ? 38  PRO A C   1 
ATOM   233  O O   . PRO A 1 36  ? 4.346   -13.374 -3.053  1.00 33.44 ? 38  PRO A O   1 
ATOM   234  C CB  . PRO A 1 36  ? 1.608   -14.039 -1.846  1.00 36.28 ? 38  PRO A CB  1 
ATOM   235  C CG  . PRO A 1 36  ? 1.124   -13.750 -3.231  1.00 37.48 ? 38  PRO A CG  1 
ATOM   236  C CD  . PRO A 1 36  ? 1.043   -12.282 -3.295  1.00 36.03 ? 38  PRO A CD  1 
ATOM   237  N N   . LEU A 1 37  ? 4.758   -13.738 -0.903  1.00 32.17 ? 39  LEU A N   1 
ATOM   238  C CA  . LEU A 1 37  ? 6.069   -14.373 -1.119  1.00 30.50 ? 39  LEU A CA  1 
ATOM   239  C C   . LEU A 1 37  ? 5.913   -15.881 -1.326  1.00 29.85 ? 39  LEU A C   1 
ATOM   240  O O   . LEU A 1 37  ? 4.980   -16.472 -0.860  1.00 30.00 ? 39  LEU A O   1 
ATOM   241  C CB  . LEU A 1 37  ? 7.023   -14.046 0.068   1.00 28.32 ? 39  LEU A CB  1 
ATOM   242  C CG  . LEU A 1 37  ? 7.366   -12.527 0.263   1.00 27.08 ? 39  LEU A CG  1 
ATOM   243  C CD1 . LEU A 1 37  ? 8.237   -12.269 1.474   1.00 27.66 ? 39  LEU A CD1 1 
ATOM   244  C CD2 . LEU A 1 37  ? 8.035   -11.938 -0.935  1.00 27.51 ? 39  LEU A CD2 1 
ATOM   245  N N   . GLN A 1 38  ? 6.839   -16.503 -2.040  1.00 30.13 ? 40  GLN A N   1 
ATOM   246  C CA  . GLN A 1 38  ? 6.900   -17.955 -2.181  1.00 29.34 ? 40  GLN A CA  1 
ATOM   247  C C   . GLN A 1 38  ? 7.010   -18.648 -0.830  1.00 30.70 ? 40  GLN A C   1 
ATOM   248  O O   . GLN A 1 38  ? 6.391   -19.697 -0.619  1.00 31.57 ? 40  GLN A O   1 
ATOM   249  C CB  . GLN A 1 38  ? 8.103   -18.337 -3.068  1.00 28.00 ? 40  GLN A CB  1 
ATOM   250  C CG  . GLN A 1 38  ? 8.290   -19.849 -3.281  1.00 28.09 ? 40  GLN A CG  1 
ATOM   251  C CD  . GLN A 1 38  ? 7.230   -20.454 -4.122  1.00 33.27 ? 40  GLN A CD  1 
ATOM   252  O OE1 . GLN A 1 38  ? 6.446   -19.765 -4.784  1.00 34.55 ? 40  GLN A OE1 1 
ATOM   253  N NE2 . GLN A 1 38  ? 7.184   -21.776 -4.133  1.00 36.79 ? 40  GLN A NE2 1 
ATOM   254  N N   . ASN A 1 39  ? 7.805   -18.056 0.070   1.00 30.88 ? 41  ASN A N   1 
ATOM   255  C CA  . ASN A 1 39  ? 8.115   -18.558 1.401   1.00 29.73 ? 41  ASN A CA  1 
ATOM   256  C C   . ASN A 1 39  ? 7.776   -17.540 2.471   1.00 26.61 ? 41  ASN A C   1 
ATOM   257  O O   . ASN A 1 39  ? 7.806   -16.339 2.224   1.00 25.70 ? 41  ASN A O   1 
ATOM   258  C CB  . ASN A 1 39  ? 9.605   -18.864 1.482   1.00 31.44 ? 41  ASN A CB  1 
ATOM   259  C CG  . ASN A 1 39  ? 10.005  -20.055 0.660   1.00 36.05 ? 41  ASN A CG  1 
ATOM   260  O OD1 . ASN A 1 39  ? 10.635  -19.904 -0.368  1.00 41.25 ? 41  ASN A OD1 1 
ATOM   261  N ND2 . ASN A 1 39  ? 9.709   -21.248 0.991   1.00 33.24 ? 41  ASN A ND2 1 
ATOM   262  N N   . ARG A 1 40  ? 7.446   -18.035 3.657   1.00 25.75 ? 42  ARG A N   1 
ATOM   263  C CA  . ARG A 1 40  ? 7.457   -17.254 4.892   1.00 25.53 ? 42  ARG A CA  1 
ATOM   264  C C   . ARG A 1 40  ? 8.873   -17.223 5.464   1.00 24.78 ? 42  ARG A C   1 
ATOM   265  O O   . ARG A 1 40  ? 9.604   -18.230 5.415   1.00 25.31 ? 42  ARG A O   1 
ATOM   266  C CB  . ARG A 1 40  ? 6.487   -17.856 5.896   1.00 28.40 ? 42  ARG A CB  1 
ATOM   267  C CG  . ARG A 1 40  ? 6.247   -17.011 7.140   1.00 33.62 ? 42  ARG A CG  1 
ATOM   268  C CD  . ARG A 1 40  ? 4.786   -17.217 7.612   1.00 40.35 ? 42  ARG A CD  1 
ATOM   269  N NE  . ARG A 1 40  ? 4.463   -16.505 8.858   1.00 47.57 ? 42  ARG A NE  1 
ATOM   270  C CZ  . ARG A 1 40  ? 4.011   -15.252 8.983   1.00 54.36 ? 42  ARG A CZ  1 
ATOM   271  N NH1 . ARG A 1 40  ? 3.819   -14.492 7.912   1.00 54.72 ? 42  ARG A NH1 1 
ATOM   272  N NH2 . ARG A 1 40  ? 3.758   -14.746 10.185  1.00 57.37 ? 42  ARG A NH2 1 
ATOM   273  N N   . TRP A 1 41  ? 9.261   -16.064 6.002   1.00 23.60 ? 43  TRP A N   1 
ATOM   274  C CA  . TRP A 1 41  ? 10.617  -15.763 6.430   1.00 23.86 ? 43  TRP A CA  1 
ATOM   275  C C   . TRP A 1 41  ? 10.567  -15.256 7.824   1.00 25.91 ? 43  TRP A C   1 
ATOM   276  O O   . TRP A 1 41  ? 9.622   -14.527 8.182   1.00 25.45 ? 43  TRP A O   1 
ATOM   277  C CB  . TRP A 1 41  ? 11.291  -14.679 5.551   1.00 23.14 ? 43  TRP A CB  1 
ATOM   278  C CG  . TRP A 1 41  ? 11.426  -15.089 4.123   1.00 22.67 ? 43  TRP A CG  1 
ATOM   279  C CD1 . TRP A 1 41  ? 10.478  -14.972 3.150   1.00 22.76 ? 43  TRP A CD1 1 
ATOM   280  C CD2 . TRP A 1 41  ? 12.516  -15.835 3.539   1.00 22.03 ? 43  TRP A CD2 1 
ATOM   281  N NE1 . TRP A 1 41  ? 10.895  -15.606 2.001   1.00 22.53 ? 43  TRP A NE1 1 
ATOM   282  C CE2 . TRP A 1 41  ? 12.164  -16.111 2.202   1.00 22.67 ? 43  TRP A CE2 1 
ATOM   283  C CE3 . TRP A 1 41  ? 13.735  -16.322 4.028   1.00 21.81 ? 43  TRP A CE3 1 
ATOM   284  C CZ2 . TRP A 1 41  ? 13.012  -16.825 1.340   1.00 23.33 ? 43  TRP A CZ2 1 
ATOM   285  C CZ3 . TRP A 1 41  ? 14.575  -16.987 3.174   1.00 23.09 ? 43  TRP A CZ3 1 
ATOM   286  C CH2 . TRP A 1 41  ? 14.208  -17.238 1.840   1.00 23.26 ? 43  TRP A CH2 1 
ATOM   287  N N   . ALA A 1 42  ? 11.601  -15.608 8.612   1.00 25.36 ? 44  ALA A N   1 
ATOM   288  C CA  . ALA A 1 42  ? 11.738  -15.187 9.980   1.00 25.09 ? 44  ALA A CA  1 
ATOM   289  C C   . ALA A 1 42  ? 13.027  -14.420 10.153  1.00 26.36 ? 44  ALA A C   1 
ATOM   290  O O   . ALA A 1 42  ? 14.077  -14.863 9.700   1.00 26.79 ? 44  ALA A O   1 
ATOM   291  C CB  . ALA A 1 42  ? 11.703  -16.418 10.888  1.00 26.07 ? 44  ALA A CB  1 
ATOM   292  N N   . LEU A 1 43  ? 12.954  -13.235 10.795  1.00 26.36 ? 45  LEU A N   1 
ATOM   293  C CA  . LEU A 1 43  ? 14.102  -12.423 11.145  1.00 26.22 ? 45  LEU A CA  1 
ATOM   294  C C   . LEU A 1 43  ? 14.526  -12.747 12.548  1.00 26.30 ? 45  LEU A C   1 
ATOM   295  O O   . LEU A 1 43  ? 13.688  -12.673 13.433  1.00 26.89 ? 45  LEU A O   1 
ATOM   296  C CB  . LEU A 1 43  ? 13.750  -10.947 11.083  1.00 25.69 ? 45  LEU A CB  1 
ATOM   297  C CG  . LEU A 1 43  ? 14.856  -9.971  11.518  1.00 25.82 ? 45  LEU A CG  1 
ATOM   298  C CD1 . LEU A 1 43  ? 16.149  -10.210 10.757  1.00 24.54 ? 45  LEU A CD1 1 
ATOM   299  C CD2 . LEU A 1 43  ? 14.338  -8.513  11.441  1.00 26.86 ? 45  LEU A CD2 1 
ATOM   300  N N   . TRP A 1 44  ? 15.805  -13.083 12.755  1.00 25.63 ? 46  TRP A N   1 
ATOM   301  C CA  . TRP A 1 44  ? 16.422  -13.401 14.035  1.00 26.77 ? 46  TRP A CA  1 
ATOM   302  C C   . TRP A 1 44  ? 17.531  -12.418 14.385  1.00 29.12 ? 46  TRP A C   1 
ATOM   303  O O   . TRP A 1 44  ? 18.203  -11.891 13.494  1.00 26.84 ? 46  TRP A O   1 
ATOM   304  C CB  . TRP A 1 44  ? 17.047  -14.799 13.984  1.00 26.23 ? 46  TRP A CB  1 
ATOM   305  C CG  . TRP A 1 44  ? 16.116  -15.879 13.547  1.00 26.23 ? 46  TRP A CG  1 
ATOM   306  C CD1 . TRP A 1 44  ? 15.744  -16.195 12.281  1.00 26.65 ? 46  TRP A CD1 1 
ATOM   307  C CD2 . TRP A 1 44  ? 15.423  -16.785 14.402  1.00 27.63 ? 46  TRP A CD2 1 
ATOM   308  N NE1 . TRP A 1 44  ? 14.898  -17.274 12.292  1.00 27.69 ? 46  TRP A NE1 1 
ATOM   309  C CE2 . TRP A 1 44  ? 14.686  -17.659 13.582  1.00 27.92 ? 46  TRP A CE2 1 
ATOM   310  C CE3 . TRP A 1 44  ? 15.408  -16.986 15.780  1.00 29.03 ? 46  TRP A CE3 1 
ATOM   311  C CZ2 . TRP A 1 44  ? 13.901  -18.673 14.102  1.00 29.63 ? 46  TRP A CZ2 1 
ATOM   312  C CZ3 . TRP A 1 44  ? 14.635  -17.984 16.287  1.00 30.40 ? 46  TRP A CZ3 1 
ATOM   313  C CH2 . TRP A 1 44  ? 13.915  -18.838 15.458  1.00 30.59 ? 46  TRP A CH2 1 
ATOM   314  N N   . PHE A 1 45  ? 17.728  -12.189 15.704  1.00 32.82 ? 47  PHE A N   1 
ATOM   315  C CA  . PHE A 1 45  ? 18.840  -11.431 16.295  1.00 35.89 ? 47  PHE A CA  1 
ATOM   316  C C   . PHE A 1 45  ? 19.588  -12.345 17.261  1.00 36.48 ? 47  PHE A C   1 
ATOM   317  O O   . PHE A 1 45  ? 18.974  -13.131 17.984  1.00 35.32 ? 47  PHE A O   1 
ATOM   318  C CB  . PHE A 1 45  ? 18.275  -10.225 17.060  1.00 38.75 ? 47  PHE A CB  1 
ATOM   319  C CG  . PHE A 1 45  ? 19.268  -9.391  17.802  1.00 42.82 ? 47  PHE A CG  1 
ATOM   320  C CD1 . PHE A 1 45  ? 20.178  -8.600  17.123  1.00 45.55 ? 47  PHE A CD1 1 
ATOM   321  C CD2 . PHE A 1 45  ? 19.296  -9.383  19.186  1.00 44.93 ? 47  PHE A CD2 1 
ATOM   322  C CE1 . PHE A 1 45  ? 21.108  -7.841  17.811  1.00 46.75 ? 47  PHE A CE1 1 
ATOM   323  C CE2 . PHE A 1 45  ? 20.234  -8.614  19.874  1.00 46.71 ? 47  PHE A CE2 1 
ATOM   324  C CZ  . PHE A 1 45  ? 21.127  -7.846  19.184  1.00 46.67 ? 47  PHE A CZ  1 
ATOM   325  N N   . PHE A 1 46  ? 20.892  -12.227 17.291  1.00 38.98 ? 48  PHE A N   1 
ATOM   326  C CA  . PHE A 1 46  ? 21.714  -12.991 18.225  1.00 42.30 ? 48  PHE A CA  1 
ATOM   327  C C   . PHE A 1 46  ? 22.769  -12.014 18.775  1.00 45.46 ? 48  PHE A C   1 
ATOM   328  O O   . PHE A 1 46  ? 23.593  -11.511 18.016  1.00 44.45 ? 48  PHE A O   1 
ATOM   329  C CB  . PHE A 1 46  ? 22.245  -14.234 17.531  1.00 42.52 ? 48  PHE A CB  1 
ATOM   330  C CG  . PHE A 1 46  ? 23.281  -15.075 18.212  1.00 45.30 ? 48  PHE A CG  1 
ATOM   331  C CD1 . PHE A 1 46  ? 22.917  -16.117 19.043  1.00 47.28 ? 48  PHE A CD1 1 
ATOM   332  C CD2 . PHE A 1 46  ? 24.621  -14.858 17.986  1.00 47.56 ? 48  PHE A CD2 1 
ATOM   333  C CE1 . PHE A 1 46  ? 23.884  -16.907 19.652  1.00 48.90 ? 48  PHE A CE1 1 
ATOM   334  C CE2 . PHE A 1 46  ? 25.582  -15.660 18.569  1.00 48.55 ? 48  PHE A CE2 1 
ATOM   335  C CZ  . PHE A 1 46  ? 25.211  -16.666 19.406  1.00 48.81 ? 48  PHE A CZ  1 
ATOM   336  N N   . LYS A 1 47  ? 22.686  -11.711 20.101  1.00 49.03 ? 49  LYS A N   1 
ATOM   337  C CA  . LYS A 1 47  ? 23.642  -10.850 20.847  1.00 53.87 ? 49  LYS A CA  1 
ATOM   338  C C   . LYS A 1 47  ? 24.811  -11.657 21.464  1.00 57.40 ? 49  LYS A C   1 
ATOM   339  O O   . LYS A 1 47  ? 24.810  -12.885 21.432  1.00 57.18 ? 49  LYS A O   1 
ATOM   340  C CB  . LYS A 1 47  ? 22.861  -10.115 21.972  1.00 57.32 ? 49  LYS A CB  1 
ATOM   341  C CG  . LYS A 1 47  ? 23.645  -9.025  22.735  1.00 63.01 ? 49  LYS A CG  1 
ATOM   342  C CD  . LYS A 1 47  ? 22.795  -8.325  23.819  1.00 67.23 ? 49  LYS A CD  1 
ATOM   343  C CE  . LYS A 1 47  ? 23.645  -7.685  24.908  1.00 70.43 ? 49  LYS A CE  1 
ATOM   344  N NZ  . LYS A 1 47  ? 22.883  -6.661  25.700  1.00 71.80 ? 49  LYS A NZ  1 
ATOM   345  N N   . ASN A 1 48  ? 25.817  -10.962 22.015  1.00 60.97 ? 50  ASN A N   1 
ATOM   346  C CA  . ASN A 1 48  ? 26.759  -11.573 22.983  1.00 64.46 ? 50  ASN A CA  1 
ATOM   347  C C   . ASN A 1 48  ? 26.490  -10.979 24.381  1.00 66.83 ? 50  ASN A C   1 
ATOM   348  O O   . ASN A 1 48  ? 26.356  -9.748  24.498  1.00 67.07 ? 50  ASN A O   1 
ATOM   349  C CB  . ASN A 1 48  ? 28.236  -11.304 22.570  1.00 67.21 ? 50  ASN A CB  1 
ATOM   350  C CG  . ASN A 1 48  ? 29.183  -12.497 22.684  1.00 72.51 ? 50  ASN A CG  1 
ATOM   351  O OD1 . ASN A 1 48  ? 28.867  -13.617 22.236  1.00 74.34 ? 50  ASN A OD1 1 
ATOM   352  N ND2 . ASN A 1 48  ? 30.375  -12.292 23.280  1.00 73.20 ? 50  ASN A ND2 1 
ATOM   353  N N   . ASP A 1 49  ? 26.421  -11.850 25.441  1.00 67.96 ? 51  ASP A N   1 
ATOM   354  C CA  . ASP A 1 49  ? 26.113  -11.418 26.811  1.00 69.05 ? 51  ASP A CA  1 
ATOM   355  C C   . ASP A 1 49  ? 27.067  -12.023 27.878  1.00 70.26 ? 51  ASP A C   1 
ATOM   356  O O   . ASP A 1 49  ? 28.030  -12.704 27.513  1.00 70.66 ? 51  ASP A O   1 
ATOM   357  C CB  . ASP A 1 49  ? 24.660  -11.784 27.116  1.00 70.75 ? 51  ASP A CB  1 
ATOM   358  C CG  . ASP A 1 49  ? 23.861  -10.701 27.817  1.00 75.50 ? 51  ASP A CG  1 
ATOM   359  O OD1 . ASP A 1 49  ? 24.207  -10.360 28.972  1.00 75.67 ? 51  ASP A OD1 1 
ATOM   360  O OD2 . ASP A 1 49  ? 22.886  -10.198 27.210  1.00 78.16 ? 51  ASP A OD2 1 
ATOM   361  N N   . LYS A 1 50  ? 26.803  -11.749 29.193  1.00 70.63 ? 52  LYS A N   1 
ATOM   362  C CA  . LYS A 1 50  ? 27.561  -12.252 30.343  1.00 71.32 ? 52  LYS A CA  1 
ATOM   363  C C   . LYS A 1 50  ? 27.229  -13.733 30.503  1.00 70.82 ? 52  LYS A C   1 
ATOM   364  O O   . LYS A 1 50  ? 26.476  -14.127 31.388  1.00 70.63 ? 52  LYS A O   1 
ATOM   365  C CB  . LYS A 1 50  ? 27.196  -11.443 31.619  1.00 74.21 ? 52  LYS A CB  1 
ATOM   366  C CG  . LYS A 1 50  ? 27.990  -11.816 32.883  1.00 78.20 ? 52  LYS A CG  1 
ATOM   367  C CD  . LYS A 1 50  ? 27.492  -11.132 34.157  1.00 82.44 ? 52  LYS A CD  1 
ATOM   368  C CE  . LYS A 1 50  ? 28.380  -9.985  34.598  1.00 86.38 ? 52  LYS A CE  1 
ATOM   369  N NZ  . LYS A 1 50  ? 29.526  -10.455 35.423  1.00 88.81 ? 52  LYS A NZ  1 
ATOM   370  N N   . SER A 1 51  ? 27.824  -14.548 29.617  1.00 70.51 ? 53  SER A N   1 
ATOM   371  C CA  . SER A 1 51  ? 27.443  -15.913 29.248  1.00 70.47 ? 53  SER A CA  1 
ATOM   372  C C   . SER A 1 51  ? 25.995  -16.285 29.560  1.00 69.97 ? 53  SER A C   1 
ATOM   373  O O   . SER A 1 51  ? 25.678  -16.940 30.554  1.00 70.40 ? 53  SER A O   1 
ATOM   374  C CB  . SER A 1 51  ? 28.399  -16.933 29.847  1.00 71.80 ? 53  SER A CB  1 
ATOM   375  O OG  . SER A 1 51  ? 28.609  -18.096 29.051  1.00 73.85 ? 53  SER A OG  1 
ATOM   376  N N   . LYS A 1 52  ? 25.121  -15.815 28.697  1.00 68.70 ? 54  LYS A N   1 
ATOM   377  C CA  . LYS A 1 52  ? 23.885  -16.503 28.467  1.00 68.26 ? 54  LYS A CA  1 
ATOM   378  C C   . LYS A 1 52  ? 24.230  -17.689 27.550  1.00 68.29 ? 54  LYS A C   1 
ATOM   379  O O   . LYS A 1 52  ? 25.165  -17.623 26.733  1.00 68.37 ? 54  LYS A O   1 
ATOM   380  C CB  . LYS A 1 52  ? 22.865  -15.544 27.853  1.00 69.84 ? 54  LYS A CB  1 
ATOM   381  C CG  . LYS A 1 52  ? 22.428  -14.418 28.789  1.00 73.47 ? 54  LYS A CG  1 
ATOM   382  C CD  . LYS A 1 52  ? 21.533  -13.419 28.059  1.00 77.21 ? 54  LYS A CD  1 
ATOM   383  C CE  . LYS A 1 52  ? 20.920  -12.405 28.991  1.00 81.20 ? 54  LYS A CE  1 
ATOM   384  N NZ  . LYS A 1 52  ? 20.194  -11.343 28.236  1.00 83.85 ? 54  LYS A NZ  1 
ATOM   385  N N   . THR A 1 53  ? 23.500  -18.785 27.700  1.00 67.92 ? 55  THR A N   1 
ATOM   386  C CA  . THR A 1 53  ? 23.652  -19.940 26.809  1.00 68.11 ? 55  THR A CA  1 
ATOM   387  C C   . THR A 1 53  ? 23.293  -19.532 25.340  1.00 67.09 ? 55  THR A C   1 
ATOM   388  O O   . THR A 1 53  ? 22.636  -18.504 25.111  1.00 67.13 ? 55  THR A O   1 
ATOM   389  C CB  . THR A 1 53  ? 22.832  -21.140 27.381  1.00 70.46 ? 55  THR A CB  1 
ATOM   390  O OG1 . THR A 1 53  ? 23.175  -22.351 26.700  1.00 71.64 ? 55  THR A OG1 1 
ATOM   391  C CG2 . THR A 1 53  ? 21.327  -20.914 27.297  1.00 71.51 ? 55  THR A CG2 1 
ATOM   392  N N   . TRP A 1 54  ? 23.722  -20.335 24.347  1.00 65.80 ? 56  TRP A N   1 
ATOM   393  C CA  . TRP A 1 54  ? 23.552  -20.007 22.916  1.00 64.49 ? 56  TRP A CA  1 
ATOM   394  C C   . TRP A 1 54  ? 22.074  -19.759 22.597  1.00 61.86 ? 56  TRP A C   1 
ATOM   395  O O   . TRP A 1 54  ? 21.727  -18.810 21.875  1.00 61.70 ? 56  TRP A O   1 
ATOM   396  C CB  . TRP A 1 54  ? 24.083  -21.144 22.024  1.00 65.44 ? 56  TRP A CB  1 
ATOM   397  C CG  . TRP A 1 54  ? 25.567  -21.363 22.092  1.00 67.78 ? 56  TRP A CG  1 
ATOM   398  C CD1 . TRP A 1 54  ? 26.232  -22.281 22.850  1.00 69.29 ? 56  TRP A CD1 1 
ATOM   399  C CD2 . TRP A 1 54  ? 26.571  -20.628 21.381  1.00 68.82 ? 56  TRP A CD2 1 
ATOM   400  N NE1 . TRP A 1 54  ? 27.590  -22.165 22.650  1.00 69.93 ? 56  TRP A NE1 1 
ATOM   401  C CE2 . TRP A 1 54  ? 27.822  -21.165 21.738  1.00 69.89 ? 56  TRP A CE2 1 
ATOM   402  C CE3 . TRP A 1 54  ? 26.532  -19.579 20.459  1.00 69.57 ? 56  TRP A CE3 1 
ATOM   403  C CZ2 . TRP A 1 54  ? 29.023  -20.669 21.217  1.00 70.86 ? 56  TRP A CZ2 1 
ATOM   404  C CZ3 . TRP A 1 54  ? 27.721  -19.081 19.957  1.00 70.56 ? 56  TRP A CZ3 1 
ATOM   405  C CH2 . TRP A 1 54  ? 28.947  -19.623 20.337  1.00 70.90 ? 56  TRP A CH2 1 
ATOM   406  N N   . GLN A 1 55  ? 21.206  -20.626 23.157  1.00 59.19 ? 57  GLN A N   1 
ATOM   407  C CA  . GLN A 1 55  ? 19.772  -20.507 23.006  1.00 56.30 ? 57  GLN A CA  1 
ATOM   408  C C   . GLN A 1 55  ? 19.233  -19.196 23.591  1.00 52.20 ? 57  GLN A C   1 
ATOM   409  O O   . GLN A 1 55  ? 18.357  -18.586 22.994  1.00 52.26 ? 57  GLN A O   1 
ATOM   410  C CB  . GLN A 1 55  ? 19.064  -21.720 23.636  1.00 59.23 ? 57  GLN A CB  1 
ATOM   411  C CG  . GLN A 1 55  ? 19.399  -23.060 22.947  1.00 63.57 ? 57  GLN A CG  1 
ATOM   412  C CD  . GLN A 1 55  ? 18.198  -23.968 22.732  1.00 67.10 ? 57  GLN A CD  1 
ATOM   413  O OE1 . GLN A 1 55  ? 17.212  -23.607 22.058  1.00 67.15 ? 57  GLN A OE1 1 
ATOM   414  N NE2 . GLN A 1 55  ? 18.260  -25.184 23.285  1.00 67.80 ? 57  GLN A NE2 1 
ATOM   415  N N   . ALA A 1 56  ? 19.749  -18.760 24.732  1.00 49.19 ? 58  ALA A N   1 
ATOM   416  C CA  . ALA A 1 56  ? 19.261  -17.547 25.387  1.00 47.42 ? 58  ALA A CA  1 
ATOM   417  C C   . ALA A 1 56  ? 19.624  -16.277 24.604  1.00 44.55 ? 58  ALA A C   1 
ATOM   418  O O   . ALA A 1 56  ? 18.909  -15.290 24.717  1.00 44.82 ? 58  ALA A O   1 
ATOM   419  C CB  . ALA A 1 56  ? 19.804  -17.455 26.810  1.00 47.14 ? 58  ALA A CB  1 
ATOM   420  N N   . ASN A 1 57  ? 20.717  -16.300 23.823  1.00 41.96 ? 59  ASN A N   1 
ATOM   421  C CA  . ASN A 1 57  ? 21.099  -15.173 22.978  1.00 40.70 ? 59  ASN A CA  1 
ATOM   422  C C   . ASN A 1 57  ? 20.357  -15.097 21.638  1.00 38.29 ? 59  ASN A C   1 
ATOM   423  O O   . ASN A 1 57  ? 20.341  -14.033 21.042  1.00 37.72 ? 59  ASN A O   1 
ATOM   424  C CB  . ASN A 1 57  ? 22.617  -15.191 22.727  1.00 42.72 ? 59  ASN A CB  1 
ATOM   425  C CG  . ASN A 1 57  ? 23.429  -14.860 23.957  1.00 44.52 ? 59  ASN A CG  1 
ATOM   426  O OD1 . ASN A 1 57  ? 22.989  -14.106 24.847  1.00 45.07 ? 59  ASN A OD1 1 
ATOM   427  N ND2 . ASN A 1 57  ? 24.622  -15.410 24.039  1.00 43.90 ? 59  ASN A ND2 1 
ATOM   428  N N   . LEU A 1 58  ? 19.742  -16.197 21.160  1.00 37.02 ? 60  LEU A N   1 
ATOM   429  C CA  . LEU A 1 58  ? 19.055  -16.212 19.887  1.00 35.88 ? 60  LEU A CA  1 
ATOM   430  C C   . LEU A 1 58  ? 17.605  -15.852 20.096  1.00 36.87 ? 60  LEU A C   1 
ATOM   431  O O   . LEU A 1 58  ? 16.901  -16.475 20.895  1.00 37.12 ? 60  LEU A O   1 
ATOM   432  C CB  . LEU A 1 58  ? 19.256  -17.568 19.174  1.00 36.23 ? 60  LEU A CB  1 
ATOM   433  C CG  . LEU A 1 58  ? 18.699  -17.748 17.730  1.00 38.27 ? 60  LEU A CG  1 
ATOM   434  C CD1 . LEU A 1 58  ? 19.235  -16.677 16.725  1.00 39.27 ? 60  LEU A CD1 1 
ATOM   435  C CD2 . LEU A 1 58  ? 19.019  -19.174 17.175  1.00 38.34 ? 60  LEU A CD2 1 
ATOM   436  N N   . ARG A 1 59  ? 17.149  -14.809 19.380  1.00 37.41 ? 61  ARG A N   1 
ATOM   437  C CA  . ARG A 1 59  ? 15.816  -14.211 19.552  1.00 36.50 ? 61  ARG A CA  1 
ATOM   438  C C   . ARG A 1 59  ? 15.147  -14.087 18.191  1.00 35.38 ? 61  ARG A C   1 
ATOM   439  O O   . ARG A 1 59  ? 15.771  -13.671 17.225  1.00 34.52 ? 61  ARG A O   1 
ATOM   440  C CB  . ARG A 1 59  ? 15.908  -12.809 20.155  1.00 38.28 ? 61  ARG A CB  1 
ATOM   441  C CG  . ARG A 1 59  ? 16.819  -12.707 21.367  1.00 46.02 ? 61  ARG A CG  1 
ATOM   442  C CD  . ARG A 1 59  ? 16.072  -12.705 22.709  1.00 53.03 ? 61  ARG A CD  1 
ATOM   443  N NE  . ARG A 1 59  ? 16.951  -13.078 23.829  1.00 56.82 ? 61  ARG A NE  1 
ATOM   444  C CZ  . ARG A 1 59  ? 17.905  -12.312 24.362  1.00 59.86 ? 61  ARG A CZ  1 
ATOM   445  N NH1 . ARG A 1 59  ? 18.140  -11.091 23.881  1.00 59.83 ? 61  ARG A NH1 1 
ATOM   446  N NH2 . ARG A 1 59  ? 18.634  -12.761 25.375  1.00 61.34 ? 61  ARG A NH2 1 
ATOM   447  N N   . LEU A 1 60  ? 13.886  -14.448 18.124  1.00 35.01 ? 62  LEU A N   1 
ATOM   448  C CA  . LEU A 1 60  ? 13.070  -14.233 16.941  1.00 34.73 ? 62  LEU A CA  1 
ATOM   449  C C   . LEU A 1 60  ? 12.458  -12.862 17.066  1.00 36.51 ? 62  LEU A C   1 
ATOM   450  O O   . LEU A 1 60  ? 11.887  -12.573 18.117  1.00 37.86 ? 62  LEU A O   1 
ATOM   451  C CB  . LEU A 1 60  ? 11.984  -15.290 16.887  1.00 32.79 ? 62  LEU A CB  1 
ATOM   452  C CG  . LEU A 1 60  ? 10.929  -15.092 15.822  1.00 32.64 ? 62  LEU A CG  1 
ATOM   453  C CD1 . LEU A 1 60  ? 11.508  -15.418 14.463  1.00 32.09 ? 62  LEU A CD1 1 
ATOM   454  C CD2 . LEU A 1 60  ? 9.683   -15.921 16.140  1.00 33.83 ? 62  LEU A CD2 1 
ATOM   455  N N   . ILE A 1 61  ? 12.543  -12.038 15.996  1.00 36.47 ? 63  ILE A N   1 
ATOM   456  C CA  . ILE A 1 61  ? 12.046  -10.672 15.965  1.00 37.18 ? 63  ILE A CA  1 
ATOM   457  C C   . ILE A 1 61  ? 10.678  -10.624 15.314  1.00 37.61 ? 63  ILE A C   1 
ATOM   458  O O   . ILE A 1 61  ? 9.763   -10.021 15.857  1.00 39.31 ? 63  ILE A O   1 
ATOM   459  C CB  . ILE A 1 61  ? 13.030  -9.707  15.243  1.00 38.45 ? 63  ILE A CB  1 
ATOM   460  C CG1 . ILE A 1 61  ? 14.452  -9.699  15.888  1.00 39.31 ? 63  ILE A CG1 1 
ATOM   461  C CG2 . ILE A 1 61  ? 12.448  -8.276  15.168  1.00 39.06 ? 63  ILE A CG2 1 
ATOM   462  C CD1 . ILE A 1 61  ? 14.530  -9.898  17.370  1.00 40.74 ? 63  ILE A CD1 1 
ATOM   463  N N   . SER A 1 62  ? 10.535  -11.240 14.153  1.00 36.22 ? 64  SER A N   1 
ATOM   464  C CA  . SER A 1 62  ? 9.335   -11.075 13.351  1.00 34.97 ? 64  SER A CA  1 
ATOM   465  C C   . SER A 1 62  ? 9.302   -12.064 12.196  1.00 34.05 ? 64  SER A C   1 
ATOM   466  O O   . SER A 1 62  ? 10.354  -12.532 11.745  1.00 33.81 ? 64  SER A O   1 
ATOM   467  C CB  . SER A 1 62  ? 9.295   -9.644  12.794  1.00 36.39 ? 64  SER A CB  1 
ATOM   468  O OG  . SER A 1 62  ? 7.975   -9.212  12.528  1.00 41.69 ? 64  SER A OG  1 
ATOM   469  N N   . LYS A 1 63  ? 8.109   -12.383 11.707  1.00 32.26 ? 65  LYS A N   1 
ATOM   470  C CA  . LYS A 1 63  ? 7.930   -13.175 10.500  1.00 31.19 ? 65  LYS A CA  1 
ATOM   471  C C   . LYS A 1 63  ? 7.075   -12.444 9.474   1.00 31.33 ? 65  LYS A C   1 
ATOM   472  O O   . LYS A 1 63  ? 6.267   -11.594 9.857   1.00 32.36 ? 65  LYS A O   1 
ATOM   473  C CB  . LYS A 1 63  ? 7.277   -14.523 10.828  1.00 32.75 ? 65  LYS A CB  1 
ATOM   474  C CG  . LYS A 1 63  ? 8.098   -15.334 11.819  1.00 34.51 ? 65  LYS A CG  1 
ATOM   475  C CD  . LYS A 1 63  ? 7.716   -16.795 11.813  1.00 37.61 ? 65  LYS A CD  1 
ATOM   476  C CE  . LYS A 1 63  ? 8.430   -17.570 12.875  1.00 41.65 ? 65  LYS A CE  1 
ATOM   477  N NZ  . LYS A 1 63  ? 7.797   -18.889 13.064  1.00 45.42 ? 65  LYS A NZ  1 
ATOM   478  N N   . PHE A 1 64  ? 7.234   -12.763 8.167   1.00 28.97 ? 66  PHE A N   1 
ATOM   479  C CA  . PHE A 1 64  ? 6.460   -12.111 7.094   1.00 28.58 ? 66  PHE A CA  1 
ATOM   480  C C   . PHE A 1 64  ? 6.395   -13.026 5.892   1.00 28.25 ? 66  PHE A C   1 
ATOM   481  O O   . PHE A 1 64  ? 7.223   -13.951 5.725   1.00 28.35 ? 66  PHE A O   1 
ATOM   482  C CB  . PHE A 1 64  ? 7.035   -10.722 6.685   1.00 27.78 ? 66  PHE A CB  1 
ATOM   483  C CG  . PHE A 1 64  ? 8.472   -10.776 6.187   1.00 25.75 ? 66  PHE A CG  1 
ATOM   484  C CD1 . PHE A 1 64  ? 8.747   -11.015 4.857   1.00 25.98 ? 66  PHE A CD1 1 
ATOM   485  C CD2 . PHE A 1 64  ? 9.536   -10.662 7.072   1.00 25.12 ? 66  PHE A CD2 1 
ATOM   486  C CE1 . PHE A 1 64  ? 10.071  -11.117 4.409   1.00 27.28 ? 66  PHE A CE1 1 
ATOM   487  C CE2 . PHE A 1 64  ? 10.844  -10.805 6.640   1.00 25.51 ? 66  PHE A CE2 1 
ATOM   488  C CZ  . PHE A 1 64  ? 11.116  -11.005 5.301   1.00 25.62 ? 66  PHE A CZ  1 
ATOM   489  N N   . ASP A 1 65  ? 5.396   -12.797 5.069   1.00 27.90 ? 67  ASP A N   1 
ATOM   490  C CA  . ASP A 1 65  ? 5.215   -13.566 3.855   1.00 28.59 ? 67  ASP A CA  1 
ATOM   491  C C   . ASP A 1 65  ? 4.583   -12.764 2.720   1.00 28.61 ? 67  ASP A C   1 
ATOM   492  O O   . ASP A 1 65  ? 3.977   -13.363 1.815   1.00 28.61 ? 67  ASP A O   1 
ATOM   493  C CB  . ASP A 1 65  ? 4.463   -14.848 4.144   1.00 29.71 ? 67  ASP A CB  1 
ATOM   494  C CG  . ASP A 1 65  ? 3.060   -14.714 4.703   1.00 36.21 ? 67  ASP A CG  1 
ATOM   495  O OD1 . ASP A 1 65  ? 2.651   -13.593 5.035   1.00 38.12 ? 67  ASP A OD1 1 
ATOM   496  O OD2 . ASP A 1 65  ? 2.389   -15.731 4.834   1.00 41.76 ? 67  ASP A OD2 1 
ATOM   497  N N   . THR A 1 66  ? 4.724   -11.438 2.755   1.00 28.91 ? 68  THR A N   1 
ATOM   498  C CA  . THR A 1 66  ? 4.404   -10.570 1.641   1.00 29.82 ? 68  THR A CA  1 
ATOM   499  C C   . THR A 1 66  ? 5.560   -9.574  1.442   1.00 29.79 ? 68  THR A C   1 
ATOM   500  O O   . THR A 1 66  ? 6.335   -9.297  2.369   1.00 29.43 ? 68  THR A O   1 
ATOM   501  C CB  . THR A 1 66  ? 3.071   -9.820  1.841   1.00 31.84 ? 68  THR A CB  1 
ATOM   502  O OG1 . THR A 1 66  ? 3.244   -8.767  2.772   1.00 34.48 ? 68  THR A OG1 1 
ATOM   503  C CG2 . THR A 1 66  ? 1.926   -10.730 2.253   1.00 32.09 ? 68  THR A CG2 1 
ATOM   504  N N   . VAL A 1 67  ? 5.635   -9.028  0.218   1.00 30.09 ? 69  VAL A N   1 
ATOM   505  C CA  . VAL A 1 67  ? 6.592   -7.996  -0.160  1.00 31.03 ? 69  VAL A CA  1 
ATOM   506  C C   . VAL A 1 67  ? 6.390   -6.761  0.721   1.00 31.01 ? 69  VAL A C   1 
ATOM   507  O O   . VAL A 1 67  ? 7.366   -6.181  1.203   1.00 30.77 ? 69  VAL A O   1 
ATOM   508  C CB  . VAL A 1 67  ? 6.454   -7.635  -1.652  1.00 30.86 ? 69  VAL A CB  1 
ATOM   509  C CG1 . VAL A 1 67  ? 7.331   -6.461  -2.000  1.00 31.08 ? 69  VAL A CG1 1 
ATOM   510  C CG2 . VAL A 1 67  ? 6.737   -8.830  -2.563  1.00 30.15 ? 69  VAL A CG2 1 
ATOM   511  N N   . GLU A 1 68  ? 5.134   -6.366  0.937   1.00 30.90 ? 70  GLU A N   1 
ATOM   512  C CA  . GLU A 1 68  ? 4.777   -5.163  1.719   1.00 31.12 ? 70  GLU A CA  1 
ATOM   513  C C   . GLU A 1 68  ? 5.138   -5.294  3.196   1.00 30.95 ? 70  GLU A C   1 
ATOM   514  O O   . GLU A 1 68  ? 5.605   -4.328  3.797   1.00 32.67 ? 70  GLU A O   1 
ATOM   515  C CB  . GLU A 1 68  ? 3.242   -4.871  1.591   1.00 33.57 ? 70  GLU A CB  1 
ATOM   516  C CG  . GLU A 1 68  ? 2.846   -4.371  0.215   1.00 34.55 ? 70  GLU A CG  1 
ATOM   517  C CD  . GLU A 1 68  ? 2.756   -5.429  -0.861  1.00 38.36 ? 70  GLU A CD  1 
ATOM   518  O OE1 . GLU A 1 68  ? 2.770   -6.638  -0.519  1.00 34.84 ? 70  GLU A OE1 1 
ATOM   519  O OE2 . GLU A 1 68  ? 2.680   -5.052  -2.054  1.00 42.07 ? 70  GLU A OE2 1 
ATOM   520  N N   . ASP A 1 69  ? 4.921   -6.481  3.786   1.00 30.11 ? 71  ASP A N   1 
ATOM   521  C CA  . ASP A 1 69  ? 5.326   -6.699  5.185   1.00 29.37 ? 71  ASP A CA  1 
ATOM   522  C C   . ASP A 1 69  ? 6.853   -6.794  5.341   1.00 29.23 ? 71  ASP A C   1 
ATOM   523  O O   . ASP A 1 69  ? 7.397   -6.389  6.372   1.00 29.85 ? 71  ASP A O   1 
ATOM   524  C CB  . ASP A 1 69  ? 4.619   -7.915  5.734   1.00 27.98 ? 71  ASP A CB  1 
ATOM   525  C CG  . ASP A 1 69  ? 3.114   -7.706  5.709   1.00 31.68 ? 71  ASP A CG  1 
ATOM   526  O OD1 . ASP A 1 69  ? 2.671   -6.563  5.988   1.00 33.28 ? 71  ASP A OD1 1 
ATOM   527  O OD2 . ASP A 1 69  ? 2.386   -8.688  5.401   1.00 30.82 ? 71  ASP A OD2 1 
ATOM   528  N N   . PHE A 1 70  ? 7.561   -7.307  4.314   1.00 27.91 ? 72  PHE A N   1 
ATOM   529  C CA  . PHE A 1 70  ? 9.031   -7.175  4.278   1.00 25.50 ? 72  PHE A CA  1 
ATOM   530  C C   . PHE A 1 70  ? 9.467   -5.732  4.367   1.00 25.46 ? 72  PHE A C   1 
ATOM   531  O O   . PHE A 1 70  ? 10.283  -5.392  5.220   1.00 24.06 ? 72  PHE A O   1 
ATOM   532  C CB  . PHE A 1 70  ? 9.612   -7.831  3.011   1.00 24.71 ? 72  PHE A CB  1 
ATOM   533  C CG  . PHE A 1 70  ? 11.050  -7.416  2.785   1.00 24.70 ? 72  PHE A CG  1 
ATOM   534  C CD1 . PHE A 1 70  ? 12.078  -8.001  3.506   1.00 24.55 ? 72  PHE A CD1 1 
ATOM   535  C CD2 . PHE A 1 70  ? 11.369  -6.420  1.867   1.00 24.88 ? 72  PHE A CD2 1 
ATOM   536  C CE1 . PHE A 1 70  ? 13.383  -7.602  3.316   1.00 24.78 ? 72  PHE A CE1 1 
ATOM   537  C CE2 . PHE A 1 70  ? 12.696  -6.025  1.680   1.00 25.33 ? 72  PHE A CE2 1 
ATOM   538  C CZ  . PHE A 1 70  ? 13.683  -6.600  2.409   1.00 24.48 ? 72  PHE A CZ  1 
ATOM   539  N N   . TRP A 1 71  ? 8.932   -4.868  3.491   1.00 26.90 ? 73  TRP A N   1 
ATOM   540  C CA  . TRP A 1 71  ? 9.319   -3.479  3.478   1.00 27.81 ? 73  TRP A CA  1 
ATOM   541  C C   . TRP A 1 71  ? 8.889   -2.758  4.740   1.00 28.42 ? 73  TRP A C   1 
ATOM   542  O O   . TRP A 1 71  ? 9.639   -1.923  5.190   1.00 28.22 ? 73  TRP A O   1 
ATOM   543  C CB  . TRP A 1 71  ? 8.809   -2.740  2.232   1.00 28.80 ? 73  TRP A CB  1 
ATOM   544  C CG  . TRP A 1 71  ? 9.580   -3.051  0.967   1.00 30.10 ? 73  TRP A CG  1 
ATOM   545  C CD1 . TRP A 1 71  ? 9.070   -3.585  -0.174  1.00 31.44 ? 73  TRP A CD1 1 
ATOM   546  C CD2 . TRP A 1 71  ? 10.977  -2.812  0.708   1.00 29.72 ? 73  TRP A CD2 1 
ATOM   547  N NE1 . TRP A 1 71  ? 10.043  -3.670  -1.133  1.00 31.64 ? 73  TRP A NE1 1 
ATOM   548  C CE2 . TRP A 1 71  ? 11.227  -3.215  -0.619  1.00 30.77 ? 73  TRP A CE2 1 
ATOM   549  C CE3 . TRP A 1 71  ? 12.038  -2.289  1.466   1.00 28.93 ? 73  TRP A CE3 1 
ATOM   550  C CZ2 . TRP A 1 71  ? 12.486  -3.122  -1.205  1.00 30.91 ? 73  TRP A CZ2 1 
ATOM   551  C CZ3 . TRP A 1 71  ? 13.289  -2.217  0.891   1.00 30.38 ? 73  TRP A CZ3 1 
ATOM   552  C CH2 . TRP A 1 71  ? 13.510  -2.629  -0.427  1.00 30.84 ? 73  TRP A CH2 1 
ATOM   553  N N   . ALA A 1 72  ? 7.699   -3.041  5.327   1.00 30.45 ? 74  ALA A N   1 
ATOM   554  C CA  . ALA A 1 72  ? 7.345   -2.377  6.622   1.00 30.72 ? 74  ALA A CA  1 
ATOM   555  C C   . ALA A 1 72  ? 8.386   -2.746  7.715   1.00 30.42 ? 74  ALA A C   1 
ATOM   556  O O   . ALA A 1 72  ? 8.827   -1.890  8.467   1.00 31.77 ? 74  ALA A O   1 
ATOM   557  C CB  . ALA A 1 72  ? 5.964   -2.760  7.066   1.00 31.21 ? 74  ALA A CB  1 
ATOM   558  N N   . LEU A 1 73  ? 8.786   -4.009  7.775   1.00 28.96 ? 75  LEU A N   1 
ATOM   559  C CA  . LEU A 1 73  ? 9.809   -4.471  8.709   1.00 28.60 ? 75  LEU A CA  1 
ATOM   560  C C   . LEU A 1 73  ? 11.199  -3.882  8.411   1.00 28.37 ? 75  LEU A C   1 
ATOM   561  O O   . LEU A 1 73  ? 11.880  -3.423  9.337   1.00 29.83 ? 75  LEU A O   1 
ATOM   562  C CB  . LEU A 1 73  ? 9.882   -6.020  8.669   1.00 28.49 ? 75  LEU A CB  1 
ATOM   563  C CG  . LEU A 1 73  ? 10.904  -6.650  9.622   1.00 29.59 ? 75  LEU A CG  1 
ATOM   564  C CD1 . LEU A 1 73  ? 10.607  -6.289  11.067  1.00 29.34 ? 75  LEU A CD1 1 
ATOM   565  C CD2 . LEU A 1 73  ? 10.944  -8.148  9.463   1.00 30.08 ? 75  LEU A CD2 1 
ATOM   566  N N   . TYR A 1 74  ? 11.621  -3.890  7.143   1.00 28.03 ? 76  TYR A N   1 
ATOM   567  C CA  . TYR A 1 74  ? 12.898  -3.287  6.715   1.00 28.49 ? 76  TYR A CA  1 
ATOM   568  C C   . TYR A 1 74  ? 12.941  -1.767  7.021   1.00 31.92 ? 76  TYR A C   1 
ATOM   569  O O   . TYR A 1 74  ? 13.942  -1.274  7.563   1.00 29.34 ? 76  TYR A O   1 
ATOM   570  C CB  . TYR A 1 74  ? 13.118  -3.512  5.209   1.00 27.44 ? 76  TYR A CB  1 
ATOM   571  C CG  . TYR A 1 74  ? 14.482  -3.003  4.755   1.00 27.49 ? 76  TYR A CG  1 
ATOM   572  C CD1 . TYR A 1 74  ? 15.606  -3.822  4.810   1.00 28.48 ? 76  TYR A CD1 1 
ATOM   573  C CD2 . TYR A 1 74  ? 14.644  -1.704  4.297   1.00 27.53 ? 76  TYR A CD2 1 
ATOM   574  C CE1 . TYR A 1 74  ? 16.863  -3.355  4.417   1.00 29.32 ? 76  TYR A CE1 1 
ATOM   575  C CE2 . TYR A 1 74  ? 15.889  -1.217  3.929   1.00 29.18 ? 76  TYR A CE2 1 
ATOM   576  C CZ  . TYR A 1 74  ? 16.998  -2.045  3.979   1.00 30.11 ? 76  TYR A CZ  1 
ATOM   577  O OH  . TYR A 1 74  ? 18.217  -1.529  3.609   1.00 30.80 ? 76  TYR A OH  1 
ATOM   578  N N   . ASN A 1 75  ? 11.839  -1.030  6.664   1.00 34.92 ? 77  ASN A N   1 
ATOM   579  C CA  . ASN A 1 75  ? 11.763  0.422   6.889   1.00 37.45 ? 77  ASN A CA  1 
ATOM   580  C C   . ASN A 1 75  ? 11.769  0.690   8.377   1.00 38.92 ? 77  ASN A C   1 
ATOM   581  O O   . ASN A 1 75  ? 12.497  1.566   8.831   1.00 40.72 ? 77  ASN A O   1 
ATOM   582  C CB  . ASN A 1 75  ? 10.497  1.037   6.248   1.00 41.29 ? 77  ASN A CB  1 
ATOM   583  C CG  . ASN A 1 75  ? 10.553  1.119   4.740   1.00 47.82 ? 77  ASN A CG  1 
ATOM   584  O OD1 . ASN A 1 75  ? 11.647  1.170   4.141   1.00 51.01 ? 77  ASN A OD1 1 
ATOM   585  N ND2 . ASN A 1 75  ? 9.386   1.129   4.082   1.00 47.38 ? 77  ASN A ND2 1 
ATOM   586  N N   . HIS A 1 76  ? 10.975  -0.041  9.152   1.00 40.04 ? 78  HIS A N   1 
ATOM   587  C CA  . HIS A 1 76  ? 11.039  0.041   10.612  1.00 40.90 ? 78  HIS A CA  1 
ATOM   588  C C   . HIS A 1 76  ? 12.468  -0.158  11.169  1.00 39.73 ? 78  HIS A C   1 
ATOM   589  O O   . HIS A 1 76  ? 12.989  0.771   11.755  1.00 39.70 ? 78  HIS A O   1 
ATOM   590  C CB  . HIS A 1 76  ? 10.046  -0.915  11.276  1.00 43.10 ? 78  HIS A CB  1 
ATOM   591  C CG  . HIS A 1 76  ? 10.053  -0.799  12.766  1.00 48.40 ? 78  HIS A CG  1 
ATOM   592  N ND1 . HIS A 1 76  ? 10.603  -1.785  13.568  1.00 51.66 ? 78  HIS A ND1 1 
ATOM   593  C CD2 . HIS A 1 76  ? 9.608   0.205   13.553  1.00 49.83 ? 78  HIS A CD2 1 
ATOM   594  C CE1 . HIS A 1 76  ? 10.457  -1.360  14.816  1.00 52.18 ? 78  HIS A CE1 1 
ATOM   595  N NE2 . HIS A 1 76  ? 9.864   -0.166  14.853  1.00 51.48 ? 78  HIS A NE2 1 
ATOM   596  N N   . ILE A 1 77  ? 13.115  -1.347  10.962  1.00 39.00 ? 79  ILE A N   1 
ATOM   597  C CA  . ILE A 1 77  ? 14.465  -1.626  11.460  1.00 38.25 ? 79  ILE A CA  1 
ATOM   598  C C   . ILE A 1 77  ? 15.466  -0.536  10.996  1.00 38.32 ? 79  ILE A C   1 
ATOM   599  O O   . ILE A 1 77  ? 16.369  -0.161  11.754  1.00 37.82 ? 79  ILE A O   1 
ATOM   600  C CB  . ILE A 1 77  ? 14.939  -3.038  11.013  1.00 37.57 ? 79  ILE A CB  1 
ATOM   601  C CG1 . ILE A 1 77  ? 14.027  -4.187  11.603  1.00 39.50 ? 79  ILE A CG1 1 
ATOM   602  C CG2 . ILE A 1 77  ? 16.420  -3.261  11.337  1.00 36.21 ? 79  ILE A CG2 1 
ATOM   603  C CD1 . ILE A 1 77  ? 14.485  -4.876  12.901  1.00 40.68 ? 79  ILE A CD1 1 
ATOM   604  N N   . GLN A 1 78  ? 15.311  -0.037  9.746   1.00 38.80 ? 80  GLN A N   1 
ATOM   605  C CA  . GLN A 1 78  ? 16.220  0.971   9.215   1.00 39.75 ? 80  GLN A CA  1 
ATOM   606  C C   . GLN A 1 78  ? 16.089  2.283   9.975   1.00 44.00 ? 80  GLN A C   1 
ATOM   607  O O   . GLN A 1 78  ? 17.093  2.932   10.193  1.00 44.58 ? 80  GLN A O   1 
ATOM   608  C CB  . GLN A 1 78  ? 15.990  1.233   7.719   1.00 38.08 ? 80  GLN A CB  1 
ATOM   609  C CG  . GLN A 1 78  ? 17.018  2.194   7.094   1.00 35.63 ? 80  GLN A CG  1 
ATOM   610  C CD  . GLN A 1 78  ? 16.889  2.216   5.591   1.00 37.04 ? 80  GLN A CD  1 
ATOM   611  O OE1 . GLN A 1 78  ? 15.800  2.429   5.067   1.00 35.90 ? 80  GLN A OE1 1 
ATOM   612  N NE2 . GLN A 1 78  ? 17.985  1.971   4.847   1.00 38.35 ? 80  GLN A NE2 1 
ATOM   613  N N   . LEU A 1 79  ? 14.879  2.669   10.364  1.00 46.73 ? 81  LEU A N   1 
ATOM   614  C CA  . LEU A 1 79  ? 14.633  3.898   11.122  1.00 49.68 ? 81  LEU A CA  1 
ATOM   615  C C   . LEU A 1 79  ? 14.960  3.733   12.617  1.00 52.13 ? 81  LEU A C   1 
ATOM   616  O O   . LEU A 1 79  ? 15.464  4.664   13.238  1.00 52.29 ? 81  LEU A O   1 
ATOM   617  C CB  . LEU A 1 79  ? 13.159  4.333   10.974  1.00 50.02 ? 81  LEU A CB  1 
ATOM   618  C CG  . LEU A 1 79  ? 12.702  4.677   9.545   1.00 52.79 ? 81  LEU A CG  1 
ATOM   619  C CD1 . LEU A 1 79  ? 11.195  4.945   9.492   1.00 53.22 ? 81  LEU A CD1 1 
ATOM   620  C CD2 . LEU A 1 79  ? 13.503  5.858   8.951   1.00 53.82 ? 81  LEU A CD2 1 
ATOM   621  N N   . SER A 1 80  ? 14.683  2.565   13.188  1.00 53.08 ? 82  SER A N   1 
ATOM   622  C CA  . SER A 1 80  ? 14.699  2.383   14.629  1.00 54.88 ? 82  SER A CA  1 
ATOM   623  C C   . SER A 1 80  ? 15.998  1.787   15.197  1.00 56.37 ? 82  SER A C   1 
ATOM   624  O O   . SER A 1 80  ? 16.391  2.171   16.300  1.00 57.26 ? 82  SER A O   1 
ATOM   625  C CB  . SER A 1 80  ? 13.505  1.535   15.056  1.00 57.16 ? 82  SER A CB  1 
ATOM   626  O OG  . SER A 1 80  ? 13.555  0.235   14.489  1.00 61.43 ? 82  SER A OG  1 
ATOM   627  N N   . SER A 1 81  ? 16.673  0.884   14.480  1.00 56.31 ? 83  SER A N   1 
ATOM   628  C CA  . SER A 1 81  ? 17.659  0.011   15.131  1.00 57.07 ? 83  SER A CA  1 
ATOM   629  C C   . SER A 1 81  ? 19.089  0.544   15.082  1.00 57.92 ? 83  SER A C   1 
ATOM   630  O O   . SER A 1 81  ? 19.438  1.247   14.143  1.00 58.05 ? 83  SER A O   1 
ATOM   631  C CB  . SER A 1 81  ? 17.611  -1.392  14.532  1.00 57.02 ? 83  SER A CB  1 
ATOM   632  O OG  . SER A 1 81  ? 16.342  -1.981  14.766  1.00 58.95 ? 83  SER A OG  1 
ATOM   633  N N   . ASN A 1 82  ? 19.907  0.191   16.095  1.00 58.46 ? 84  ASN A N   1 
ATOM   634  C CA  . ASN A 1 82  ? 21.337  0.504   16.129  1.00 60.74 ? 84  ASN A CA  1 
ATOM   635  C C   . ASN A 1 82  ? 22.202  -0.669  15.696  1.00 60.64 ? 84  ASN A C   1 
ATOM   636  O O   . ASN A 1 82  ? 21.819  -1.808  15.905  1.00 61.39 ? 84  ASN A O   1 
ATOM   637  C CB  . ASN A 1 82  ? 21.773  0.893   17.550  1.00 64.05 ? 84  ASN A CB  1 
ATOM   638  C CG  . ASN A 1 82  ? 21.295  2.241   18.027  1.00 68.77 ? 84  ASN A CG  1 
ATOM   639  O OD1 . ASN A 1 82  ? 22.116  3.112   18.357  1.00 71.39 ? 84  ASN A OD1 1 
ATOM   640  N ND2 . ASN A 1 82  ? 19.977  2.441   18.081  1.00 69.15 ? 84  ASN A ND2 1 
ATOM   641  N N   . LEU A 1 83  ? 23.384  -0.376  15.126  1.00 60.20 ? 85  LEU A N   1 
ATOM   642  C CA  . LEU A 1 83  ? 24.329  -1.351  14.595  1.00 60.26 ? 85  LEU A CA  1 
ATOM   643  C C   . LEU A 1 83  ? 25.456  -1.647  15.596  1.00 60.37 ? 85  LEU A C   1 
ATOM   644  O O   . LEU A 1 83  ? 26.485  -0.972  15.563  1.00 60.80 ? 85  LEU A O   1 
ATOM   645  C CB  . LEU A 1 83  ? 24.933  -0.787  13.293  1.00 59.96 ? 85  LEU A CB  1 
ATOM   646  C CG  . LEU A 1 83  ? 25.899  -1.698  12.541  1.00 60.65 ? 85  LEU A CG  1 
ATOM   647  C CD1 . LEU A 1 83  ? 25.162  -2.859  11.871  1.00 60.95 ? 85  LEU A CD1 1 
ATOM   648  C CD2 . LEU A 1 83  ? 26.689  -0.909  11.535  1.00 61.53 ? 85  LEU A CD2 1 
ATOM   649  N N   . MET A 1 84  ? 25.281  -2.652  16.464  1.00 59.90 ? 86  MET A N   1 
ATOM   650  C CA  . MET A 1 84  ? 26.285  -2.946  17.488  1.00 60.23 ? 86  MET A CA  1 
ATOM   651  C C   . MET A 1 84  ? 27.162  -4.076  16.978  1.00 58.67 ? 86  MET A C   1 
ATOM   652  O O   . MET A 1 84  ? 26.621  -5.105  16.552  1.00 59.33 ? 86  MET A O   1 
ATOM   653  C CB  . MET A 1 84  ? 25.658  -3.361  18.839  1.00 62.57 ? 86  MET A CB  1 
ATOM   654  C CG  . MET A 1 84  ? 24.344  -2.658  19.195  1.00 66.95 ? 86  MET A CG  1 
ATOM   655  S SD  . MET A 1 84  ? 23.717  -3.112  20.838  1.00 76.75 ? 86  MET A SD  1 
ATOM   656  C CE  . MET A 1 84  ? 24.818  -2.118  21.903  1.00 68.38 ? 86  MET A CE  1 
ATOM   657  N N   . PRO A 1 85  ? 28.496  -3.935  16.988  1.00 56.38 ? 87  PRO A N   1 
ATOM   658  C CA  . PRO A 1 85  ? 29.337  -5.126  16.744  1.00 55.28 ? 87  PRO A CA  1 
ATOM   659  C C   . PRO A 1 85  ? 29.109  -6.227  17.779  1.00 54.18 ? 87  PRO A C   1 
ATOM   660  O O   . PRO A 1 85  ? 28.556  -5.990  18.868  1.00 53.87 ? 87  PRO A O   1 
ATOM   661  C CB  . PRO A 1 85  ? 30.775  -4.593  16.726  1.00 56.40 ? 87  PRO A CB  1 
ATOM   662  C CG  . PRO A 1 85  ? 30.661  -3.072  16.638  1.00 56.95 ? 87  PRO A CG  1 
ATOM   663  C CD  . PRO A 1 85  ? 29.298  -2.708  17.187  1.00 55.74 ? 87  PRO A CD  1 
ATOM   664  N N   . GLY A 1 86  ? 29.529  -7.435  17.405  1.00 52.94 ? 88  GLY A N   1 
ATOM   665  C CA  . GLY A 1 86  ? 29.280  -8.644  18.177  1.00 52.15 ? 88  GLY A CA  1 
ATOM   666  C C   . GLY A 1 86  ? 27.927  -9.282  17.897  1.00 50.58 ? 88  GLY A C   1 
ATOM   667  O O   . GLY A 1 86  ? 27.715  -10.448 18.250  1.00 50.45 ? 88  GLY A O   1 
ATOM   668  N N   . CYS A 1 87  ? 27.002  -8.526  17.255  1.00 49.27 ? 89  CYS A N   1 
ATOM   669  C CA  . CYS A 1 87  ? 25.646  -8.970  16.993  1.00 49.24 ? 89  CYS A CA  1 
ATOM   670  C C   . CYS A 1 87  ? 25.501  -9.619  15.575  1.00 46.36 ? 89  CYS A C   1 
ATOM   671  O O   . CYS A 1 87  ? 26.312  -9.397  14.667  1.00 46.54 ? 89  CYS A O   1 
ATOM   672  C CB  . CYS A 1 87  ? 24.681  -7.811  17.190  1.00 52.14 ? 89  CYS A CB  1 
ATOM   673  S SG  . CYS A 1 87  ? 24.690  -7.122  18.871  1.00 65.30 ? 89  CYS A SG  1 
ATOM   674  N N   . ASP A 1 88  ? 24.477  -10.438 15.413  1.00 43.20 ? 90  ASP A N   1 
ATOM   675  C CA  . ASP A 1 88  ? 24.195  -11.115 14.162  1.00 40.57 ? 90  ASP A CA  1 
ATOM   676  C C   . ASP A 1 88  ? 22.723  -11.003 13.898  1.00 36.46 ? 90  ASP A C   1 
ATOM   677  O O   . ASP A 1 88  ? 21.919  -11.104 14.829  1.00 36.46 ? 90  ASP A O   1 
ATOM   678  C CB  . ASP A 1 88  ? 24.560  -12.609 14.208  1.00 44.02 ? 90  ASP A CB  1 
ATOM   679  C CG  . ASP A 1 88  ? 25.949  -12.937 14.766  1.00 49.11 ? 90  ASP A CG  1 
ATOM   680  O OD1 . ASP A 1 88  ? 26.892  -12.136 14.532  1.00 49.13 ? 90  ASP A OD1 1 
ATOM   681  O OD2 . ASP A 1 88  ? 26.089  -13.993 15.428  1.00 47.72 ? 90  ASP A OD2 1 
ATOM   682  N N   . TYR A 1 89  ? 22.370  -10.772 12.631  1.00 32.58 ? 91  TYR A N   1 
ATOM   683  C CA  . TYR A 1 89  ? 20.997  -10.831 12.149  1.00 31.86 ? 91  TYR A CA  1 
ATOM   684  C C   . TYR A 1 89  ? 20.904  -11.925 11.093  1.00 28.17 ? 91  TYR A C   1 
ATOM   685  O O   . TYR A 1 89  ? 21.858  -12.157 10.326  1.00 27.28 ? 91  TYR A O   1 
ATOM   686  C CB  . TYR A 1 89  ? 20.567  -9.516  11.515  1.00 34.13 ? 91  TYR A CB  1 
ATOM   687  C CG  . TYR A 1 89  ? 20.297  -8.408  12.497  1.00 38.53 ? 91  TYR A CG  1 
ATOM   688  C CD1 . TYR A 1 89  ? 21.313  -7.589  12.941  1.00 40.40 ? 91  TYR A CD1 1 
ATOM   689  C CD2 . TYR A 1 89  ? 19.018  -8.186  12.990  1.00 42.02 ? 91  TYR A CD2 1 
ATOM   690  C CE1 . TYR A 1 89  ? 21.067  -6.570  13.853  1.00 42.26 ? 91  TYR A CE1 1 
ATOM   691  C CE2 . TYR A 1 89  ? 18.757  -7.158  13.883  1.00 43.04 ? 91  TYR A CE2 1 
ATOM   692  C CZ  . TYR A 1 89  ? 19.789  -6.359  14.323  1.00 43.56 ? 91  TYR A CZ  1 
ATOM   693  O OH  . TYR A 1 89  ? 19.548  -5.337  15.209  1.00 47.39 ? 91  TYR A OH  1 
ATOM   694  N N   . SER A 1 90  ? 19.774  -12.573 11.065  1.00 26.61 ? 92  SER A N   1 
ATOM   695  C CA  . SER A 1 90  ? 19.514  -13.665 10.130  1.00 25.32 ? 92  SER A CA  1 
ATOM   696  C C   . SER A 1 90  ? 18.111  -13.628 9.608   1.00 23.37 ? 92  SER A C   1 
ATOM   697  O O   . SER A 1 90  ? 17.179  -13.401 10.376  1.00 24.37 ? 92  SER A O   1 
ATOM   698  C CB  . SER A 1 90  ? 19.759  -15.001 10.799  1.00 26.30 ? 92  SER A CB  1 
ATOM   699  O OG  . SER A 1 90  ? 21.099  -15.096 11.229  1.00 32.69 ? 92  SER A OG  1 
ATOM   700  N N   . LEU A 1 91  ? 17.935  -13.856 8.327   1.00 21.00 ? 93  LEU A N   1 
ATOM   701  C CA  . LEU A 1 91  ? 16.632  -14.089 7.753   1.00 20.31 ? 93  LEU A CA  1 
ATOM   702  C C   . LEU A 1 91  ? 16.633  -15.481 7.243   1.00 20.17 ? 93  LEU A C   1 
ATOM   703  O O   . LEU A 1 91  ? 17.427  -15.805 6.352   1.00 19.77 ? 93  LEU A O   1 
ATOM   704  C CB  . LEU A 1 91  ? 16.314  -13.126 6.620   1.00 19.63 ? 93  LEU A CB  1 
ATOM   705  C CG  . LEU A 1 91  ? 14.827  -13.174 6.128   1.00 19.68 ? 93  LEU A CG  1 
ATOM   706  C CD1 . LEU A 1 91  ? 13.885  -12.501 7.132   1.00 18.98 ? 93  LEU A CD1 1 
ATOM   707  C CD2 . LEU A 1 91  ? 14.647  -12.576 4.745   1.00 19.03 ? 93  LEU A CD2 1 
ATOM   708  N N   . PHE A 1 92  ? 15.767  -16.337 7.800   1.00 19.78 ? 94  PHE A N   1 
ATOM   709  C CA  . PHE A 1 92  ? 15.700  -17.761 7.424   1.00 20.42 ? 94  PHE A CA  1 
ATOM   710  C C   . PHE A 1 92  ? 14.310  -18.128 7.118   1.00 22.81 ? 94  PHE A C   1 
ATOM   711  O O   . PHE A 1 92  ? 13.367  -17.534 7.664   1.00 25.33 ? 94  PHE A O   1 
ATOM   712  C CB  . PHE A 1 92  ? 16.253  -18.691 8.531   1.00 20.40 ? 94  PHE A CB  1 
ATOM   713  C CG  . PHE A 1 92  ? 17.756  -18.892 8.487   1.00 20.74 ? 94  PHE A CG  1 
ATOM   714  C CD1 . PHE A 1 92  ? 18.613  -17.847 8.747   1.00 21.80 ? 94  PHE A CD1 1 
ATOM   715  C CD2 . PHE A 1 92  ? 18.296  -20.100 8.087   1.00 21.84 ? 94  PHE A CD2 1 
ATOM   716  C CE1 . PHE A 1 92  ? 19.981  -18.011 8.630   1.00 23.43 ? 94  PHE A CE1 1 
ATOM   717  C CE2 . PHE A 1 92  ? 19.672  -20.271 7.986   1.00 23.19 ? 94  PHE A CE2 1 
ATOM   718  C CZ  . PHE A 1 92  ? 20.501  -19.231 8.242   1.00 24.04 ? 94  PHE A CZ  1 
ATOM   719  N N   . LYS A 1 93  ? 14.123  -19.122 6.232   1.00 20.31 ? 95  LYS A N   1 
ATOM   720  C CA  . LYS A 1 93  ? 12.805  -19.639 5.974   1.00 21.37 ? 95  LYS A CA  1 
ATOM   721  C C   . LYS A 1 93  ? 12.153  -20.156 7.287   1.00 21.80 ? 95  LYS A C   1 
ATOM   722  O O   . LYS A 1 93  ? 12.817  -20.643 8.226   1.00 18.24 ? 95  LYS A O   1 
ATOM   723  C CB  . LYS A 1 93  ? 12.819  -20.754 4.919   1.00 20.67 ? 95  LYS A CB  1 
ATOM   724  C CG  . LYS A 1 93  ? 13.207  -20.269 3.555   1.00 19.09 ? 95  LYS A CG  1 
ATOM   725  C CD  . LYS A 1 93  ? 13.438  -21.421 2.615   1.00 21.56 ? 95  LYS A CD  1 
ATOM   726  C CE  . LYS A 1 93  ? 13.607  -20.941 1.216   1.00 21.56 ? 95  LYS A CE  1 
ATOM   727  N NZ  . LYS A 1 93  ? 13.988  -22.029 0.337   1.00 20.13 ? 95  LYS A NZ  1 
ATOM   728  N N   . ASP A 1 94  ? 10.853  -19.998 7.335   1.00 24.17 ? 96  ASP A N   1 
ATOM   729  C CA  . ASP A 1 94  ? 10.045  -20.398 8.478   1.00 27.96 ? 96  ASP A CA  1 
ATOM   730  C C   . ASP A 1 94  ? 10.288  -21.880 8.777   1.00 28.73 ? 96  ASP A C   1 
ATOM   731  O O   . ASP A 1 94  ? 10.195  -22.696 7.864   1.00 28.19 ? 96  ASP A O   1 
ATOM   732  C CB  . ASP A 1 94  ? 8.562   -20.113 8.167   1.00 31.49 ? 96  ASP A CB  1 
ATOM   733  C CG  . ASP A 1 94  ? 7.611   -20.078 9.339   1.00 36.88 ? 96  ASP A CG  1 
ATOM   734  O OD1 . ASP A 1 94  ? 8.083   -19.978 10.484  1.00 36.03 ? 96  ASP A OD1 1 
ATOM   735  O OD2 . ASP A 1 94  ? 6.386   -20.129 9.101   1.00 43.77 ? 96  ASP A OD2 1 
ATOM   736  N N   . GLY A 1 95  ? 10.704  -22.157 10.021  1.00 29.47 ? 97  GLY A N   1 
ATOM   737  C CA  . GLY A 1 95  ? 10.959  -23.491 10.524  1.00 29.36 ? 97  GLY A CA  1 
ATOM   738  C C   . GLY A 1 95  ? 12.392  -23.952 10.454  1.00 28.77 ? 97  GLY A C   1 
ATOM   739  O O   . GLY A 1 95  ? 12.650  -25.108 10.748  1.00 28.01 ? 97  GLY A O   1 
ATOM   740  N N   . ILE A 1 96  ? 13.319  -23.089 10.040  1.00 28.37 ? 98  ILE A N   1 
ATOM   741  C CA  . ILE A 1 96  ? 14.761  -23.336 10.073  1.00 28.40 ? 98  ILE A CA  1 
ATOM   742  C C   . ILE A 1 96  ? 15.380  -22.350 11.065  1.00 27.95 ? 98  ILE A C   1 
ATOM   743  O O   . ILE A 1 96  ? 15.301  -21.133 10.861  1.00 27.18 ? 98  ILE A O   1 
ATOM   744  C CB  . ILE A 1 96  ? 15.421  -23.157 8.679   1.00 28.24 ? 98  ILE A CB  1 
ATOM   745  C CG1 . ILE A 1 96  ? 14.693  -23.984 7.585   1.00 29.65 ? 98  ILE A CG1 1 
ATOM   746  C CG2 . ILE A 1 96  ? 16.919  -23.486 8.758   1.00 27.89 ? 98  ILE A CG2 1 
ATOM   747  C CD1 . ILE A 1 96  ? 15.327  -23.837 6.145   1.00 29.58 ? 98  ILE A CD1 1 
ATOM   748  N N   . GLU A 1 97  ? 15.991  -22.873 12.130  1.00 27.93 ? 99  GLU A N   1 
ATOM   749  C CA  . GLU A 1 97  ? 16.768  -22.041 13.028  1.00 29.10 ? 99  GLU A CA  1 
ATOM   750  C C   . GLU A 1 97  ? 18.089  -21.622 12.370  1.00 29.27 ? 99  GLU A C   1 
ATOM   751  O O   . GLU A 1 97  ? 18.653  -22.389 11.585  1.00 28.04 ? 99  GLU A O   1 
ATOM   752  C CB  . GLU A 1 97  ? 16.999  -22.751 14.365  1.00 32.37 ? 99  GLU A CB  1 
ATOM   753  C CG  . GLU A 1 97  ? 15.732  -22.848 15.224  1.00 40.33 ? 99  GLU A CG  1 
ATOM   754  C CD  . GLU A 1 97  ? 15.980  -23.309 16.649  1.00 54.72 ? 99  GLU A CD  1 
ATOM   755  O OE1 . GLU A 1 97  ? 15.523  -22.617 17.587  1.00 58.29 ? 99  GLU A OE1 1 
ATOM   756  O OE2 . GLU A 1 97  ? 16.641  -24.359 16.829  1.00 58.34 ? 99  GLU A OE2 1 
ATOM   757  N N   . PRO A 1 98  ? 18.576  -20.383 12.612  1.00 29.09 ? 100 PRO A N   1 
ATOM   758  C CA  . PRO A 1 98  ? 19.855  -19.962 12.056  1.00 28.86 ? 100 PRO A CA  1 
ATOM   759  C C   . PRO A 1 98  ? 21.076  -20.526 12.730  1.00 30.68 ? 100 PRO A C   1 
ATOM   760  O O   . PRO A 1 98  ? 22.000  -19.780 13.046  1.00 31.32 ? 100 PRO A O   1 
ATOM   761  C CB  . PRO A 1 98  ? 19.782  -18.413 12.174  1.00 28.56 ? 100 PRO A CB  1 
ATOM   762  C CG  . PRO A 1 98  ? 19.024  -18.183 13.344  1.00 28.14 ? 100 PRO A CG  1 
ATOM   763  C CD  . PRO A 1 98  ? 17.927  -19.256 13.317  1.00 28.24 ? 100 PRO A CD  1 
ATOM   764  N N   . MET A 1 99  ? 21.118  -21.840 12.885  1.00 30.84 ? 101 MET A N   1 
ATOM   765  C CA  . MET A 1 99  ? 22.198  -22.528 13.536  1.00 32.83 ? 101 MET A CA  1 
ATOM   766  C C   . MET A 1 99  ? 22.565  -23.722 12.637  1.00 32.88 ? 101 MET A C   1 
ATOM   767  O O   . MET A 1 99  ? 21.682  -24.435 12.110  1.00 33.08 ? 101 MET A O   1 
ATOM   768  C CB  . MET A 1 99  ? 21.796  -22.962 14.961  1.00 35.82 ? 101 MET A CB  1 
ATOM   769  C CG  . MET A 1 99  ? 21.736  -21.772 15.981  1.00 43.37 ? 101 MET A CG  1 
ATOM   770  S SD  . MET A 1 99  ? 23.348  -21.028 16.488  1.00 63.72 ? 101 MET A SD  1 
ATOM   771  C CE  . MET A 1 99  ? 22.789  -19.586 17.351  1.00 68.46 ? 101 MET A CE  1 
ATOM   772  N N   . TRP A 1 100 ? 23.857  -23.938 12.456  1.00 32.55 ? 102 TRP A N   1 
ATOM   773  C CA  . TRP A 1 100 ? 24.324  -24.934 11.488  1.00 34.29 ? 102 TRP A CA  1 
ATOM   774  C C   . TRP A 1 100 ? 23.885  -26.367 11.897  1.00 34.72 ? 102 TRP A C   1 
ATOM   775  O O   . TRP A 1 100 ? 23.836  -27.228 11.026  1.00 34.49 ? 102 TRP A O   1 
ATOM   776  C CB  . TRP A 1 100 ? 25.851  -24.805 11.207  1.00 34.34 ? 102 TRP A CB  1 
ATOM   777  C CG  . TRP A 1 100 ? 26.770  -25.595 12.088  1.00 35.20 ? 102 TRP A CG  1 
ATOM   778  C CD1 . TRP A 1 100 ? 27.372  -25.166 13.230  1.00 36.50 ? 102 TRP A CD1 1 
ATOM   779  C CD2 . TRP A 1 100 ? 27.255  -26.941 11.860  1.00 34.97 ? 102 TRP A CD2 1 
ATOM   780  N NE1 . TRP A 1 100 ? 28.123  -26.189 13.782  1.00 36.74 ? 102 TRP A NE1 1 
ATOM   781  C CE2 . TRP A 1 100 ? 28.088  -27.277 12.948  1.00 35.99 ? 102 TRP A CE2 1 
ATOM   782  C CE3 . TRP A 1 100 ? 27.024  -27.905 10.874  1.00 34.37 ? 102 TRP A CE3 1 
ATOM   783  C CZ2 . TRP A 1 100 ? 28.722  -28.528 13.052  1.00 36.72 ? 102 TRP A CZ2 1 
ATOM   784  C CZ3 . TRP A 1 100 ? 27.645  -29.135 10.975  1.00 35.03 ? 102 TRP A CZ3 1 
ATOM   785  C CH2 . TRP A 1 100 ? 28.500  -29.432 12.051  1.00 36.16 ? 102 TRP A CH2 1 
ATOM   786  N N   . GLU A 1 101 ? 23.530  -26.596 13.196  1.00 34.65 ? 103 GLU A N   1 
ATOM   787  C CA  . GLU A 1 101 ? 23.085  -27.876 13.736  1.00 35.22 ? 103 GLU A CA  1 
ATOM   788  C C   . GLU A 1 101 ? 21.677  -28.221 13.319  1.00 33.58 ? 103 GLU A C   1 
ATOM   789  O O   . GLU A 1 101 ? 21.353  -29.395 13.287  1.00 34.38 ? 103 GLU A O   1 
ATOM   790  C CB  . GLU A 1 101 ? 23.176  -27.906 15.268  1.00 39.30 ? 103 GLU A CB  1 
ATOM   791  C CG  . GLU A 1 101 ? 24.551  -27.594 15.835  1.00 46.40 ? 103 GLU A CG  1 
ATOM   792  C CD  . GLU A 1 101 ? 24.846  -26.137 16.157  1.00 51.17 ? 103 GLU A CD  1 
ATOM   793  O OE1 . GLU A 1 101 ? 24.152  -25.250 15.618  1.00 47.19 ? 103 GLU A OE1 1 
ATOM   794  O OE2 . GLU A 1 101 ? 25.776  -25.884 16.960  1.00 58.32 ? 103 GLU A OE2 1 
ATOM   795  N N   . ASP A 1 102 ? 20.815  -27.225 12.979  1.00 31.61 ? 104 ASP A N   1 
ATOM   796  C CA  . ASP A 1 102 ? 19.502  -27.455 12.359  1.00 29.57 ? 104 ASP A CA  1 
ATOM   797  C C   . ASP A 1 102 ? 19.549  -28.492 11.250  1.00 29.98 ? 104 ASP A C   1 
ATOM   798  O O   . ASP A 1 102 ? 20.498  -28.537 10.458  1.00 29.58 ? 104 ASP A O   1 
ATOM   799  C CB  . ASP A 1 102 ? 18.916  -26.144 11.792  1.00 28.55 ? 104 ASP A CB  1 
ATOM   800  C CG  . ASP A 1 102 ? 17.446  -26.202 11.450  1.00 30.23 ? 104 ASP A CG  1 
ATOM   801  O OD1 . ASP A 1 102 ? 16.628  -25.684 12.248  1.00 29.46 ? 104 ASP A OD1 1 
ATOM   802  O OD2 . ASP A 1 102 ? 17.106  -26.749 10.380  1.00 30.96 ? 104 ASP A OD2 1 
ATOM   803  N N   . GLU A 1 103 ? 18.517  -29.332 11.181  1.00 31.58 ? 105 GLU A N   1 
ATOM   804  C CA  . GLU A 1 103 ? 18.403  -30.369 10.146  1.00 32.59 ? 105 GLU A CA  1 
ATOM   805  C C   . GLU A 1 103 ? 18.602  -29.845 8.749   1.00 31.12 ? 105 GLU A C   1 
ATOM   806  O O   . GLU A 1 103 ? 19.224  -30.521 7.935   1.00 31.68 ? 105 GLU A O   1 
ATOM   807  C CB  . GLU A 1 103 ? 17.017  -31.083 10.217  1.00 36.40 ? 105 GLU A CB  1 
ATOM   808  C CG  . GLU A 1 103 ? 16.987  -32.191 11.255  1.00 43.46 ? 105 GLU A CG  1 
ATOM   809  C CD  . GLU A 1 103 ? 18.034  -33.241 10.957  1.00 52.03 ? 105 GLU A CD  1 
ATOM   810  O OE1 . GLU A 1 103 ? 18.043  -33.728 9.801   1.00 54.40 ? 105 GLU A OE1 1 
ATOM   811  O OE2 . GLU A 1 103 ? 18.852  -33.558 11.856  1.00 53.25 ? 105 GLU A OE2 1 
ATOM   812  N N   . LYS A 1 104 ? 18.087  -28.639 8.476   1.00 29.69 ? 106 LYS A N   1 
ATOM   813  C CA  . LYS A 1 104 ? 18.199  -28.059 7.134   1.00 28.94 ? 106 LYS A CA  1 
ATOM   814  C C   . LYS A 1 104 ? 19.534  -27.344 6.871   1.00 27.52 ? 106 LYS A C   1 
ATOM   815  O O   . LYS A 1 104 ? 19.767  -26.965 5.718   1.00 28.28 ? 106 LYS A O   1 
ATOM   816  C CB  . LYS A 1 104 ? 17.018  -27.126 6.844   1.00 30.94 ? 106 LYS A CB  1 
ATOM   817  C CG  . LYS A 1 104 ? 15.691  -27.888 6.718   1.00 37.59 ? 106 LYS A CG  1 
ATOM   818  C CD  . LYS A 1 104 ? 15.527  -28.485 5.309   1.00 47.01 ? 106 LYS A CD  1 
ATOM   819  C CE  . LYS A 1 104 ? 14.230  -29.252 5.113   1.00 54.47 ? 106 LYS A CE  1 
ATOM   820  N NZ  . LYS A 1 104 ? 14.483  -30.667 4.666   1.00 60.58 ? 106 LYS A NZ  1 
ATOM   821  N N   . ASN A 1 105 ? 20.411  -27.158 7.891   1.00 25.26 ? 107 ASN A N   1 
ATOM   822  C CA  . ASN A 1 105 ? 21.697  -26.557 7.663   1.00 25.35 ? 107 ASN A CA  1 
ATOM   823  C C   . ASN A 1 105 ? 22.870  -27.574 7.887   1.00 27.37 ? 107 ASN A C   1 
ATOM   824  O O   . ASN A 1 105 ? 23.937  -27.359 7.352   1.00 25.82 ? 107 ASN A O   1 
ATOM   825  C CB  . ASN A 1 105 ? 21.890  -25.402 8.586   1.00 25.54 ? 107 ASN A CB  1 
ATOM   826  C CG  . ASN A 1 105 ? 20.840  -24.321 8.475   1.00 24.85 ? 107 ASN A CG  1 
ATOM   827  O OD1 . ASN A 1 105 ? 20.345  -23.985 7.391   1.00 26.44 ? 107 ASN A OD1 1 
ATOM   828  N ND2 . ASN A 1 105 ? 20.494  -23.753 9.608   1.00 22.78 ? 107 ASN A ND2 1 
ATOM   829  N N   . LYS A 1 106 ? 22.669  -28.653 8.675   1.00 29.42 ? 108 LYS A N   1 
ATOM   830  C CA  . LYS A 1 106 ? 23.810  -29.510 9.066   1.00 30.72 ? 108 LYS A CA  1 
ATOM   831  C C   . LYS A 1 106 ? 24.578  -30.066 7.884   1.00 30.07 ? 108 LYS A C   1 
ATOM   832  O O   . LYS A 1 106 ? 25.785  -30.204 7.996   1.00 30.79 ? 108 LYS A O   1 
ATOM   833  C CB  . LYS A 1 106 ? 23.462  -30.637 10.079  1.00 33.86 ? 108 LYS A CB  1 
ATOM   834  C CG  . LYS A 1 106 ? 22.286  -31.557 9.756   1.00 43.43 ? 108 LYS A CG  1 
ATOM   835  C CD  . LYS A 1 106 ? 22.029  -32.564 10.912  1.00 52.31 ? 108 LYS A CD  1 
ATOM   836  C CE  . LYS A 1 106 ? 21.427  -33.894 10.447  1.00 60.27 ? 108 LYS A CE  1 
ATOM   837  N NZ  . LYS A 1 106 ? 21.541  -34.982 11.463  1.00 63.78 ? 108 LYS A NZ  1 
ATOM   838  N N   . ARG A 1 107 ? 23.917  -30.363 6.755   1.00 29.07 ? 109 ARG A N   1 
ATOM   839  C CA  . ARG A 1 107 ? 24.602  -30.892 5.578   1.00 28.02 ? 109 ARG A CA  1 
ATOM   840  C C   . ARG A 1 107 ? 24.996  -29.813 4.571   1.00 25.63 ? 109 ARG A C   1 
ATOM   841  O O   . ARG A 1 107 ? 25.330  -30.143 3.444   1.00 25.06 ? 109 ARG A O   1 
ATOM   842  C CB  . ARG A 1 107 ? 23.712  -31.949 4.928   1.00 30.06 ? 109 ARG A CB  1 
ATOM   843  C CG  . ARG A 1 107 ? 23.471  -33.174 5.859   1.00 36.27 ? 109 ARG A CG  1 
ATOM   844  C CD  . ARG A 1 107 ? 22.519  -34.159 5.243   1.00 44.33 ? 109 ARG A CD  1 
ATOM   845  N NE  . ARG A 1 107 ? 21.191  -33.576 5.020   1.00 53.54 ? 109 ARG A NE  1 
ATOM   846  C CZ  . ARG A 1 107 ? 20.240  -33.445 5.949   1.00 59.46 ? 109 ARG A CZ  1 
ATOM   847  N NH1 . ARG A 1 107 ? 20.451  -33.864 7.196   1.00 60.53 ? 109 ARG A NH1 1 
ATOM   848  N NH2 . ARG A 1 107 ? 19.069  -32.892 5.636   1.00 59.70 ? 109 ARG A NH2 1 
ATOM   849  N N   . GLY A 1 108 ? 24.974  -28.546 4.983   1.00 23.60 ? 110 GLY A N   1 
ATOM   850  C CA  . GLY A 1 108 ? 24.941  -27.405 4.071   1.00 22.47 ? 110 GLY A CA  1 
ATOM   851  C C   . GLY A 1 108 ? 26.200  -26.618 4.119   1.00 22.02 ? 110 GLY A C   1 
ATOM   852  O O   . GLY A 1 108 ? 27.239  -27.113 4.561   1.00 23.83 ? 110 GLY A O   1 
ATOM   853  N N   . GLY A 1 109 ? 26.094  -25.406 3.638   1.00 20.96 ? 111 GLY A N   1 
ATOM   854  C CA  . GLY A 1 109 ? 27.131  -24.410 3.786   1.00 21.92 ? 111 GLY A CA  1 
ATOM   855  C C   . GLY A 1 109 ? 26.683  -23.024 3.383   1.00 22.83 ? 111 GLY A C   1 
ATOM   856  O O   . GLY A 1 109 ? 25.494  -22.737 3.254   1.00 22.30 ? 111 GLY A O   1 
ATOM   857  N N   . ARG A 1 110 ? 27.657  -22.157 3.194   1.00 21.36 ? 112 ARG A N   1 
ATOM   858  C CA  . ARG A 1 110 ? 27.416  -20.789 2.895   1.00 21.43 ? 112 ARG A CA  1 
ATOM   859  C C   . ARG A 1 110 ? 28.339  -20.211 1.833   1.00 20.96 ? 112 ARG A C   1 
ATOM   860  O O   . ARG A 1 110 ? 29.566  -20.486 1.841   1.00 19.64 ? 112 ARG A O   1 
ATOM   861  C CB  . ARG A 1 110 ? 27.498  -19.982 4.181   1.00 23.47 ? 112 ARG A CB  1 
ATOM   862  C CG  . ARG A 1 110 ? 28.896  -19.588 4.595   1.00 25.01 ? 112 ARG A CG  1 
ATOM   863  C CD  . ARG A 1 110 ? 28.936  -19.101 5.990   1.00 24.95 ? 112 ARG A CD  1 
ATOM   864  N NE  . ARG A 1 110 ? 30.325  -18.932 6.415   1.00 27.63 ? 112 ARG A NE  1 
ATOM   865  C CZ  . ARG A 1 110 ? 30.717  -18.271 7.502   1.00 28.46 ? 112 ARG A CZ  1 
ATOM   866  N NH1 . ARG A 1 110 ? 32.015  -18.178 7.805   1.00 29.09 ? 112 ARG A NH1 1 
ATOM   867  N NH2 . ARG A 1 110 ? 29.827  -17.692 8.289   1.00 27.98 ? 112 ARG A NH2 1 
ATOM   868  N N   . TRP A 1 111 ? 27.734  -19.372 0.982   1.00 22.04 ? 113 TRP A N   1 
ATOM   869  C CA  . TRP A 1 111 ? 28.420  -18.414 0.123   1.00 22.58 ? 113 TRP A CA  1 
ATOM   870  C C   . TRP A 1 111 ? 28.772  -17.143 0.958   1.00 22.01 ? 113 TRP A C   1 
ATOM   871  O O   . TRP A 1 111 ? 27.864  -16.457 1.423   1.00 20.31 ? 113 TRP A O   1 
ATOM   872  C CB  . TRP A 1 111 ? 27.544  -18.001 -1.067  1.00 21.41 ? 113 TRP A CB  1 
ATOM   873  C CG  . TRP A 1 111 ? 27.528  -19.009 -2.146  1.00 20.16 ? 113 TRP A CG  1 
ATOM   874  C CD1 . TRP A 1 111 ? 26.465  -19.754 -2.574  1.00 20.77 ? 113 TRP A CD1 1 
ATOM   875  C CD2 . TRP A 1 111 ? 28.615  -19.334 -2.990  1.00 20.12 ? 113 TRP A CD2 1 
ATOM   876  N NE1 . TRP A 1 111 ? 26.861  -20.564 -3.619  1.00 20.99 ? 113 TRP A NE1 1 
ATOM   877  C CE2 . TRP A 1 111 ? 28.198  -20.387 -3.829  1.00 20.92 ? 113 TRP A CE2 1 
ATOM   878  C CE3 . TRP A 1 111 ? 29.949  -18.902 -3.056  1.00 20.81 ? 113 TRP A CE3 1 
ATOM   879  C CZ2 . TRP A 1 111 ? 29.031  -20.908 -4.810  1.00 22.27 ? 113 TRP A CZ2 1 
ATOM   880  C CZ3 . TRP A 1 111 ? 30.760  -19.443 -4.007  1.00 23.00 ? 113 TRP A CZ3 1 
ATOM   881  C CH2 . TRP A 1 111 ? 30.308  -20.433 -4.864  1.00 23.50 ? 113 TRP A CH2 1 
ATOM   882  N N   . LEU A 1 112 ? 30.053  -16.834 1.124   1.00 22.98 ? 114 LEU A N   1 
ATOM   883  C CA  . LEU A 1 112 ? 30.507  -15.811 2.071   1.00 24.24 ? 114 LEU A CA  1 
ATOM   884  C C   . LEU A 1 112 ? 31.089  -14.603 1.400   1.00 24.14 ? 114 LEU A C   1 
ATOM   885  O O   . LEU A 1 112 ? 31.907  -14.740 0.490   1.00 24.53 ? 114 LEU A O   1 
ATOM   886  C CB  . LEU A 1 112 ? 31.562  -16.403 3.018   1.00 24.53 ? 114 LEU A CB  1 
ATOM   887  C CG  . LEU A 1 112 ? 32.064  -15.467 4.173   1.00 26.04 ? 114 LEU A CG  1 
ATOM   888  C CD1 . LEU A 1 112 ? 30.993  -15.223 5.174   1.00 25.12 ? 114 LEU A CD1 1 
ATOM   889  C CD2 . LEU A 1 112 ? 33.274  -16.109 4.905   1.00 29.79 ? 114 LEU A CD2 1 
ATOM   890  N N   . ILE A 1 113 ? 30.671  -13.425 1.827   1.00 21.87 ? 115 ILE A N   1 
ATOM   891  C CA  . ILE A 1 113 ? 31.261  -12.139 1.472   1.00 23.27 ? 115 ILE A CA  1 
ATOM   892  C C   . ILE A 1 113 ? 31.825  -11.505 2.772   1.00 20.84 ? 115 ILE A C   1 
ATOM   893  O O   . ILE A 1 113 ? 31.099  -11.259 3.731   1.00 16.94 ? 115 ILE A O   1 
ATOM   894  C CB  . ILE A 1 113 ? 30.261  -11.106 0.867   1.00 27.92 ? 115 ILE A CB  1 
ATOM   895  C CG1 . ILE A 1 113 ? 29.238  -11.762 -0.049  1.00 31.19 ? 115 ILE A CG1 1 
ATOM   896  C CG2 . ILE A 1 113 ? 30.985  -10.026 0.098   1.00 31.52 ? 115 ILE A CG2 1 
ATOM   897  C CD1 . ILE A 1 113 ? 28.022  -11.523 0.257   1.00 35.00 ? 115 ILE A CD1 1 
ATOM   898  N N   . THR A 1 114 ? 33.093  -11.214 2.780   1.00 22.83 ? 116 THR A N   1 
ATOM   899  C CA  . THR A 1 114 ? 33.717  -10.517 3.885   1.00 26.54 ? 116 THR A CA  1 
ATOM   900  C C   . THR A 1 114 ? 34.032  -9.123  3.391   1.00 29.34 ? 116 THR A C   1 
ATOM   901  O O   . THR A 1 114 ? 34.640  -8.972  2.312   1.00 30.45 ? 116 THR A O   1 
ATOM   902  C CB  . THR A 1 114 ? 34.938  -11.256 4.423   1.00 31.47 ? 116 THR A CB  1 
ATOM   903  O OG1 . THR A 1 114 ? 34.615  -12.647 4.730   1.00 32.42 ? 116 THR A OG1 1 
ATOM   904  C CG2 . THR A 1 114 ? 35.495  -10.548 5.685   1.00 34.67 ? 116 THR A CG2 1 
ATOM   905  N N   . LEU A 1 115 ? 33.612  -8.118  4.187   1.00 29.48 ? 117 LEU A N   1 
ATOM   906  C CA  . LEU A 1 115 ? 33.882  -6.709  4.020   1.00 31.12 ? 117 LEU A CA  1 
ATOM   907  C C   . LEU A 1 115 ? 34.995  -6.297  4.977   1.00 34.09 ? 117 LEU A C   1 
ATOM   908  O O   . LEU A 1 115 ? 35.016  -6.761  6.127   1.00 34.07 ? 117 LEU A O   1 
ATOM   909  C CB  . LEU A 1 115 ? 32.618  -5.943  4.435   1.00 32.20 ? 117 LEU A CB  1 
ATOM   910  C CG  . LEU A 1 115 ? 31.371  -6.172  3.592   1.00 33.86 ? 117 LEU A CG  1 
ATOM   911  C CD1 . LEU A 1 115 ? 30.259  -5.395  4.135   1.00 31.96 ? 117 LEU A CD1 1 
ATOM   912  C CD2 . LEU A 1 115 ? 31.621  -5.830  2.135   1.00 35.72 ? 117 LEU A CD2 1 
ATOM   913  N N   . ASN A 1 116 ? 35.895  -5.407  4.535   1.00 35.73 ? 118 ASN A N   1 
ATOM   914  C CA  . ASN A 1 116 ? 36.878  -4.816  5.469   1.00 38.84 ? 118 ASN A CA  1 
ATOM   915  C C   . ASN A 1 116 ? 36.226  -3.630  6.233   1.00 40.09 ? 118 ASN A C   1 
ATOM   916  O O   . ASN A 1 116 ? 35.126  -3.188  5.896   1.00 38.51 ? 118 ASN A O   1 
ATOM   917  C CB  . ASN A 1 116 ? 38.170  -4.376  4.741   1.00 41.07 ? 118 ASN A CB  1 
ATOM   918  C CG  . ASN A 1 116 ? 39.438  -4.342  5.616   1.00 47.66 ? 118 ASN A CG  1 
ATOM   919  O OD1 . ASN A 1 116 ? 39.415  -4.248  6.870   1.00 49.41 ? 118 ASN A OD1 1 
ATOM   920  N ND2 . ASN A 1 116 ? 40.601  -4.420  4.972   1.00 49.28 ? 118 ASN A ND2 1 
ATOM   921  N N   . LYS A 1 117 ? 36.922  -3.140  7.265   1.00 42.09 ? 119 LYS A N   1 
ATOM   922  C CA  . LYS A 1 117 ? 36.503  -2.057  8.171   1.00 44.53 ? 119 LYS A CA  1 
ATOM   923  C C   . LYS A 1 117 ? 35.879  -0.885  7.405   1.00 44.78 ? 119 LYS A C   1 
ATOM   924  O O   . LYS A 1 117 ? 34.811  -0.405  7.784   1.00 44.12 ? 119 LYS A O   1 
ATOM   925  C CB  . LYS A 1 117 ? 37.719  -1.517  8.978   1.00 47.22 ? 119 LYS A CB  1 
ATOM   926  C CG  . LYS A 1 117 ? 38.402  -2.485  9.947   1.00 52.92 ? 119 LYS A CG  1 
ATOM   927  C CD  . LYS A 1 117 ? 39.797  -1.910  10.344  1.00 59.66 ? 119 LYS A CD  1 
ATOM   928  C CE  . LYS A 1 117 ? 40.554  -2.756  11.342  1.00 64.56 ? 119 LYS A CE  1 
ATOM   929  N NZ  . LYS A 1 117 ? 41.819  -2.089  11.812  1.00 68.48 ? 119 LYS A NZ  1 
ATOM   930  N N   . GLN A 1 118 ? 36.558  -0.450  6.315   1.00 45.55 ? 120 GLN A N   1 
ATOM   931  C CA  . GLN A 1 118 ? 36.145  0.692   5.464   1.00 46.34 ? 120 GLN A CA  1 
ATOM   932  C C   . GLN A 1 118 ? 34.782  0.432   4.784   1.00 44.41 ? 120 GLN A C   1 
ATOM   933  O O   . GLN A 1 118 ? 33.963  1.344   4.617   1.00 42.97 ? 120 GLN A O   1 
ATOM   934  C CB  . GLN A 1 118 ? 37.180  0.932   4.339   1.00 50.31 ? 120 GLN A CB  1 
ATOM   935  C CG  . GLN A 1 118 ? 38.271  1.938   4.652   1.00 57.51 ? 120 GLN A CG  1 
ATOM   936  C CD  . GLN A 1 118 ? 39.330  1.961   3.563   1.00 64.86 ? 120 GLN A CD  1 
ATOM   937  O OE1 . GLN A 1 118 ? 39.742  0.914   3.037   1.00 68.50 ? 120 GLN A OE1 1 
ATOM   938  N NE2 . GLN A 1 118 ? 39.808  3.143   3.199   1.00 64.71 ? 120 GLN A NE2 1 
ATOM   939  N N   . GLN A 1 119 ? 34.546  -0.828  4.391   1.00 43.28 ? 121 GLN A N   1 
ATOM   940  C CA  . GLN A 1 119 ? 33.344  -1.177  3.637   1.00 42.32 ? 121 GLN A CA  1 
ATOM   941  C C   . GLN A 1 119 ? 32.106  -1.304  4.520   1.00 40.63 ? 121 GLN A C   1 
ATOM   942  O O   . GLN A 1 119 ? 31.030  -1.477  3.982   1.00 40.03 ? 121 GLN A O   1 
ATOM   943  C CB  . GLN A 1 119 ? 33.588  -2.441  2.808   1.00 42.88 ? 121 GLN A CB  1 
ATOM   944  C CG  . GLN A 1 119 ? 34.740  -2.302  1.865   1.00 43.80 ? 121 GLN A CG  1 
ATOM   945  C CD  . GLN A 1 119 ? 35.024  -3.623  1.219   1.00 47.38 ? 121 GLN A CD  1 
ATOM   946  O OE1 . GLN A 1 119 ? 35.556  -4.549  1.841   1.00 44.83 ? 121 GLN A OE1 1 
ATOM   947  N NE2 . GLN A 1 119 ? 34.686  -3.751  -0.046  1.00 51.11 ? 121 GLN A NE2 1 
ATOM   948  N N   . ARG A 1 120 ? 32.218  -1.200  5.855   1.00 40.35 ? 122 ARG A N   1 
ATOM   949  C CA  . ARG A 1 120 ? 31.037  -1.051  6.700   1.00 41.65 ? 122 ARG A CA  1 
ATOM   950  C C   . ARG A 1 120 ? 30.172  0.166   6.245   1.00 41.86 ? 122 ARG A C   1 
ATOM   951  O O   . ARG A 1 120 ? 28.981  0.028   5.970   1.00 41.33 ? 122 ARG A O   1 
ATOM   952  C CB  . ARG A 1 120 ? 31.405  -0.916  8.181   1.00 43.48 ? 122 ARG A CB  1 
ATOM   953  C CG  . ARG A 1 120 ? 30.138  -0.795  9.031   1.00 48.96 ? 122 ARG A CG  1 
ATOM   954  C CD  . ARG A 1 120 ? 30.435  -0.912  10.482  1.00 52.63 ? 122 ARG A CD  1 
ATOM   955  N NE  . ARG A 1 120 ? 30.622  -2.296  10.913  1.00 54.26 ? 122 ARG A NE  1 
ATOM   956  C CZ  . ARG A 1 120 ? 31.109  -2.657  12.095  1.00 57.01 ? 122 ARG A CZ  1 
ATOM   957  N NH1 . ARG A 1 120 ? 31.483  -1.733  12.987  1.00 57.01 ? 122 ARG A NH1 1 
ATOM   958  N NH2 . ARG A 1 120 ? 31.231  -3.934  12.400  1.00 57.40 ? 122 ARG A NH2 1 
ATOM   959  N N   . ARG A 1 121 ? 30.799  1.344   6.158   1.00 41.21 ? 123 ARG A N   1 
ATOM   960  C CA  . ARG A 1 121 ? 30.094  2.546   5.799   1.00 41.61 ? 123 ARG A CA  1 
ATOM   961  C C   . ARG A 1 121 ? 29.594  2.439   4.358   1.00 39.57 ? 123 ARG A C   1 
ATOM   962  O O   . ARG A 1 121 ? 28.441  2.701   4.123   1.00 40.37 ? 123 ARG A O   1 
ATOM   963  C CB  . ARG A 1 121 ? 30.998  3.782   5.991   1.00 47.14 ? 123 ARG A CB  1 
ATOM   964  C CG  . ARG A 1 121 ? 31.278  4.124   7.465   1.00 54.68 ? 123 ARG A CG  1 
ATOM   965  C CD  . ARG A 1 121 ? 31.117  5.626   7.741   1.00 60.82 ? 123 ARG A CD  1 
ATOM   966  N NE  . ARG A 1 121 ? 31.187  5.977   9.157   1.00 65.14 ? 123 ARG A NE  1 
ATOM   967  C CZ  . ARG A 1 121 ? 30.236  5.723   10.058  1.00 67.18 ? 123 ARG A CZ  1 
ATOM   968  N NH1 . ARG A 1 121 ? 30.397  6.093   11.323  1.00 67.43 ? 123 ARG A NH1 1 
ATOM   969  N NH2 . ARG A 1 121 ? 29.125  5.077   9.705   1.00 66.31 ? 123 ARG A NH2 1 
ATOM   970  N N   . SER A 1 122 ? 30.419  2.000   3.417   1.00 38.10 ? 124 SER A N   1 
ATOM   971  C CA  . SER A 1 122 ? 30.080  2.002   1.991   1.00 37.96 ? 124 SER A CA  1 
ATOM   972  C C   . SER A 1 122 ? 29.202  0.813   1.461   1.00 35.91 ? 124 SER A C   1 
ATOM   973  O O   . SER A 1 122 ? 28.299  1.041   0.651   1.00 37.81 ? 124 SER A O   1 
ATOM   974  C CB  . SER A 1 122 ? 31.380  2.061   1.193   1.00 41.88 ? 124 SER A CB  1 
ATOM   975  O OG  . SER A 1 122 ? 32.216  0.973   1.551   1.00 44.96 ? 124 SER A OG  1 
ATOM   976  N N   . ASP A 1 123 ? 29.435  -0.425  1.921   1.00 30.86 ? 125 ASP A N   1 
ATOM   977  C CA  . ASP A 1 123 ? 28.841  -1.601  1.297   1.00 28.78 ? 125 ASP A CA  1 
ATOM   978  C C   . ASP A 1 123 ? 27.925  -2.436  2.198   1.00 26.16 ? 125 ASP A C   1 
ATOM   979  O O   . ASP A 1 123 ? 27.157  -3.179  1.642   1.00 26.28 ? 125 ASP A O   1 
ATOM   980  C CB  . ASP A 1 123 ? 29.885  -2.536  0.684   1.00 30.80 ? 125 ASP A CB  1 
ATOM   981  C CG  . ASP A 1 123 ? 30.740  -1.918  -0.401  1.00 39.92 ? 125 ASP A CG  1 
ATOM   982  O OD1 . ASP A 1 123 ? 30.174  -1.405  -1.382  1.00 41.47 ? 125 ASP A OD1 1 
ATOM   983  O OD2 . ASP A 1 123 ? 31.976  -1.960  -0.271  1.00 43.67 ? 125 ASP A OD2 1 
ATOM   984  N N   . LEU A 1 124 ? 27.981  -2.338  3.534   1.00 24.27 ? 126 LEU A N   1 
ATOM   985  C CA  . LEU A 1 124 ? 27.199  -3.226  4.409   1.00 22.86 ? 126 LEU A CA  1 
ATOM   986  C C   . LEU A 1 124 ? 25.693  -3.125  4.146   1.00 20.98 ? 126 LEU A C   1 
ATOM   987  O O   . LEU A 1 124 ? 25.067  -4.134  3.890   1.00 21.32 ? 126 LEU A O   1 
ATOM   988  C CB  . LEU A 1 124 ? 27.491  -2.903  5.875   1.00 22.20 ? 126 LEU A CB  1 
ATOM   989  C CG  . LEU A 1 124 ? 26.820  -3.799  6.937   1.00 23.22 ? 126 LEU A CG  1 
ATOM   990  C CD1 . LEU A 1 124 ? 27.320  -5.196  6.893   1.00 23.94 ? 126 LEU A CD1 1 
ATOM   991  C CD2 . LEU A 1 124 ? 27.053  -3.265  8.333   1.00 24.38 ? 126 LEU A CD2 1 
ATOM   992  N N   . ASN A 1 125 ? 25.112  -1.912  4.205   1.00 21.01 ? 127 ASN A N   1 
ATOM   993  C CA  . ASN A 1 125 ? 23.682  -1.755  4.063   1.00 21.95 ? 127 ASN A CA  1 
ATOM   994  C C   . ASN A 1 125 ? 23.213  -2.189  2.684   1.00 22.17 ? 127 ASN A C   1 
ATOM   995  O O   . ASN A 1 125 ? 22.216  -2.891  2.531   1.00 20.36 ? 127 ASN A O   1 
ATOM   996  C CB  . ASN A 1 125 ? 23.258  -0.348  4.398   1.00 26.05 ? 127 ASN A CB  1 
ATOM   997  C CG  . ASN A 1 125 ? 23.478  0.040   5.859   1.00 31.40 ? 127 ASN A CG  1 
ATOM   998  O OD1 . ASN A 1 125 ? 23.946  1.139   6.152   1.00 32.84 ? 127 ASN A OD1 1 
ATOM   999  N ND2 . ASN A 1 125 ? 23.125  -0.790  6.812   1.00 32.19 ? 127 ASN A ND2 1 
ATOM   1000 N N   . ARG A 1 126 ? 23.962  -1.763  1.667   1.00 23.64 ? 128 ARG A N   1 
ATOM   1001 C CA  . ARG A 1 126 ? 23.673  -2.085  0.277   1.00 22.39 ? 128 ARG A CA  1 
ATOM   1002 C C   . ARG A 1 126 ? 23.728  -3.606  0.069   1.00 21.66 ? 128 ARG A C   1 
ATOM   1003 O O   . ARG A 1 126 ? 22.767  -4.167  -0.436  1.00 20.67 ? 128 ARG A O   1 
ATOM   1004 C CB  . ARG A 1 126 ? 24.654  -1.348  -0.638  1.00 22.49 ? 128 ARG A CB  1 
ATOM   1005 C CG  . ARG A 1 126 ? 24.572  -1.741  -2.114  1.00 26.28 ? 128 ARG A CG  1 
ATOM   1006 C CD  . ARG A 1 126 ? 23.200  -1.547  -2.717  1.00 30.49 ? 128 ARG A CD  1 
ATOM   1007 N NE  . ARG A 1 126 ? 22.695  -0.161  -2.587  1.00 30.02 ? 128 ARG A NE  1 
ATOM   1008 C CZ  . ARG A 1 126 ? 21.453  0.220   -2.861  1.00 30.23 ? 128 ARG A CZ  1 
ATOM   1009 N NH1 . ARG A 1 126 ? 20.560  -0.660  -3.288  1.00 27.80 ? 128 ARG A NH1 1 
ATOM   1010 N NH2 . ARG A 1 126 ? 21.096  1.487   -2.722  1.00 28.61 ? 128 ARG A NH2 1 
ATOM   1011 N N   . PHE A 1 127 ? 24.814  -4.255  0.434   1.00 21.12 ? 129 PHE A N   1 
ATOM   1012 C CA  . PHE A 1 127 ? 24.947  -5.685  0.181   1.00 23.29 ? 129 PHE A CA  1 
ATOM   1013 C C   . PHE A 1 127 ? 23.944  -6.491  1.003   1.00 20.52 ? 129 PHE A C   1 
ATOM   1014 O O   . PHE A 1 127 ? 23.474  -7.490  0.514   1.00 20.00 ? 129 PHE A O   1 
ATOM   1015 C CB  . PHE A 1 127 ? 26.318  -6.192  0.477   1.00 23.94 ? 129 PHE A CB  1 
ATOM   1016 C CG  . PHE A 1 127 ? 27.440  -5.867  -0.470  1.00 26.55 ? 129 PHE A CG  1 
ATOM   1017 C CD1 . PHE A 1 127 ? 27.306  -4.884  -1.431  1.00 28.36 ? 129 PHE A CD1 1 
ATOM   1018 C CD2 . PHE A 1 127 ? 28.622  -6.562  -0.412  1.00 28.01 ? 129 PHE A CD2 1 
ATOM   1019 C CE1 . PHE A 1 127 ? 28.366  -4.591  -2.296  1.00 29.92 ? 129 PHE A CE1 1 
ATOM   1020 C CE2 . PHE A 1 127 ? 29.663  -6.286  -1.285  1.00 29.26 ? 129 PHE A CE2 1 
ATOM   1021 C CZ  . PHE A 1 127 ? 29.540  -5.292  -2.209  1.00 29.61 ? 129 PHE A CZ  1 
ATOM   1022 N N   . TRP A 1 128 ? 23.635  -6.060  2.230   1.00 20.14 ? 130 TRP A N   1 
ATOM   1023 C CA  . TRP A 1 128 ? 22.651  -6.753  3.038   1.00 20.71 ? 130 TRP A CA  1 
ATOM   1024 C C   . TRP A 1 128 ? 21.281  -6.692  2.405   1.00 21.99 ? 130 TRP A C   1 
ATOM   1025 O O   . TRP A 1 128 ? 20.617  -7.713  2.308   1.00 22.52 ? 130 TRP A O   1 
ATOM   1026 C CB  . TRP A 1 128 ? 22.619  -6.230  4.487   1.00 19.71 ? 130 TRP A CB  1 
ATOM   1027 C CG  . TRP A 1 128 ? 21.651  -6.945  5.388   1.00 19.38 ? 130 TRP A CG  1 
ATOM   1028 C CD1 . TRP A 1 128 ? 20.715  -6.385  6.179   1.00 21.48 ? 130 TRP A CD1 1 
ATOM   1029 C CD2 . TRP A 1 128 ? 21.646  -8.336  5.693   1.00 20.41 ? 130 TRP A CD2 1 
ATOM   1030 N NE1 . TRP A 1 128 ? 20.040  -7.359  6.878   1.00 22.64 ? 130 TRP A NE1 1 
ATOM   1031 C CE2 . TRP A 1 128 ? 20.602  -8.563  6.609   1.00 20.97 ? 130 TRP A CE2 1 
ATOM   1032 C CE3 . TRP A 1 128 ? 22.373  -9.444  5.216   1.00 20.18 ? 130 TRP A CE3 1 
ATOM   1033 C CZ2 . TRP A 1 128 ? 20.310  -9.827  7.108   1.00 21.07 ? 130 TRP A CZ2 1 
ATOM   1034 C CZ3 . TRP A 1 128 ? 22.060  -10.701 5.702   1.00 18.91 ? 130 TRP A CZ3 1 
ATOM   1035 C CH2 . TRP A 1 128 ? 21.065  -10.880 6.645   1.00 20.09 ? 130 TRP A CH2 1 
ATOM   1036 N N   . LEU A 1 129 ? 20.824  -5.487  1.980   1.00 21.63 ? 131 LEU A N   1 
ATOM   1037 C CA  . LEU A 1 129 ? 19.547  -5.369  1.284   1.00 22.37 ? 131 LEU A CA  1 
ATOM   1038 C C   . LEU A 1 129 ? 19.537  -6.206  0.010   1.00 21.92 ? 131 LEU A C   1 
ATOM   1039 O O   . LEU A 1 129 ? 18.562  -6.909  -0.228  1.00 22.43 ? 131 LEU A O   1 
ATOM   1040 C CB  . LEU A 1 129 ? 19.242  -3.887  0.933   1.00 23.44 ? 131 LEU A CB  1 
ATOM   1041 C CG  . LEU A 1 129 ? 17.970  -3.665  0.084   1.00 25.64 ? 131 LEU A CG  1 
ATOM   1042 C CD1 . LEU A 1 129 ? 16.769  -4.202  0.777   1.00 26.40 ? 131 LEU A CD1 1 
ATOM   1043 C CD2 . LEU A 1 129 ? 17.794  -2.226  -0.274  1.00 26.92 ? 131 LEU A CD2 1 
ATOM   1044 N N   . GLU A 1 130 ? 20.633  -6.149  -0.807  1.00 20.39 ? 132 GLU A N   1 
ATOM   1045 C CA  . GLU A 1 130 ? 20.622  -6.929  -2.053  1.00 21.32 ? 132 GLU A CA  1 
ATOM   1046 C C   . GLU A 1 130 ? 20.484  -8.441  -1.787  1.00 20.51 ? 132 GLU A C   1 
ATOM   1047 O O   . GLU A 1 130 ? 19.787  -9.170  -2.525  1.00 20.07 ? 132 GLU A O   1 
ATOM   1048 C CB  . GLU A 1 130 ? 21.825  -6.644  -2.918  1.00 23.69 ? 132 GLU A CB  1 
ATOM   1049 C CG  . GLU A 1 130 ? 21.978  -5.193  -3.345  1.00 26.26 ? 132 GLU A CG  1 
ATOM   1050 C CD  . GLU A 1 130 ? 20.841  -4.667  -4.182  1.00 28.57 ? 132 GLU A CD  1 
ATOM   1051 O OE1 . GLU A 1 130 ? 20.155  -5.491  -4.832  1.00 31.99 ? 132 GLU A OE1 1 
ATOM   1052 O OE2 . GLU A 1 130 ? 20.635  -3.431  -4.190  1.00 27.32 ? 132 GLU A OE2 1 
ATOM   1053 N N   . THR A 1 131 ? 21.153  -8.898  -0.743  1.00 20.51 ? 133 THR A N   1 
ATOM   1054 C CA  . THR A 1 131 ? 21.010  -10.267 -0.226  1.00 20.89 ? 133 THR A CA  1 
ATOM   1055 C C   . THR A 1 131 ? 19.546  -10.617 0.140   1.00 20.75 ? 133 THR A C   1 
ATOM   1056 O O   . THR A 1 131 ? 19.048  -11.657 -0.270  1.00 18.00 ? 133 THR A O   1 
ATOM   1057 C CB  . THR A 1 131 ? 21.913  -10.482 0.962   1.00 20.55 ? 133 THR A CB  1 
ATOM   1058 O OG1 . THR A 1 131 ? 23.252  -10.213 0.537   1.00 21.33 ? 133 THR A OG1 1 
ATOM   1059 C CG2 . THR A 1 131 ? 21.798  -11.852 1.512   1.00 19.25 ? 133 THR A CG2 1 
ATOM   1060 N N   . LEU A 1 132 ? 18.885  -9.749  0.907   1.00 22.19 ? 134 LEU A N   1 
ATOM   1061 C CA  . LEU A 1 132 ? 17.507  -9.957  1.313   1.00 21.48 ? 134 LEU A CA  1 
ATOM   1062 C C   . LEU A 1 132 ? 16.567  -10.019 0.113   1.00 20.76 ? 134 LEU A C   1 
ATOM   1063 O O   . LEU A 1 132 ? 15.626  -10.792 0.141   1.00 20.67 ? 134 LEU A O   1 
ATOM   1064 C CB  . LEU A 1 132 ? 17.036  -8.846  2.242   1.00 21.50 ? 134 LEU A CB  1 
ATOM   1065 C CG  . LEU A 1 132 ? 17.755  -8.726  3.577   1.00 21.11 ? 134 LEU A CG  1 
ATOM   1066 C CD1 . LEU A 1 132 ? 17.276  -7.548  4.327   1.00 19.87 ? 134 LEU A CD1 1 
ATOM   1067 C CD2 . LEU A 1 132 ? 17.561  -9.957  4.456   1.00 21.91 ? 134 LEU A CD2 1 
ATOM   1068 N N   . LEU A 1 133 ? 16.817  -9.214  -0.912  1.00 21.01 ? 135 LEU A N   1 
ATOM   1069 C CA  . LEU A 1 133 ? 15.983  -9.238  -2.102  1.00 21.28 ? 135 LEU A CA  1 
ATOM   1070 C C   . LEU A 1 133 ? 16.097  -10.578 -2.869  1.00 19.91 ? 135 LEU A C   1 
ATOM   1071 O O   . LEU A 1 133 ? 15.093  -11.060 -3.385  1.00 20.45 ? 135 LEU A O   1 
ATOM   1072 C CB  . LEU A 1 133 ? 16.256  -8.023  -2.982  1.00 20.22 ? 135 LEU A CB  1 
ATOM   1073 C CG  . LEU A 1 133 ? 16.016  -6.636  -2.347  1.00 20.71 ? 135 LEU A CG  1 
ATOM   1074 C CD1 . LEU A 1 133 ? 16.195  -5.500  -3.345  1.00 20.18 ? 135 LEU A CD1 1 
ATOM   1075 C CD2 . LEU A 1 133 ? 14.606  -6.478  -1.825  1.00 21.81 ? 135 LEU A CD2 1 
ATOM   1076 N N   . CYS A 1 134 ? 17.266  -11.118 -2.948  1.00 19.05 ? 136 CYS A N   1 
ATOM   1077 C CA  . CYS A 1 134 ? 17.573  -12.407 -3.550  1.00 21.11 ? 136 CYS A CA  1 
ATOM   1078 C C   . CYS A 1 134 ? 16.789  -13.526 -2.886  1.00 20.69 ? 136 CYS A C   1 
ATOM   1079 O O   . CYS A 1 134 ? 16.332  -14.471 -3.576  1.00 21.49 ? 136 CYS A O   1 
ATOM   1080 C CB  . CYS A 1 134 ? 19.067  -12.704 -3.489  1.00 22.73 ? 136 CYS A CB  1 
ATOM   1081 S SG  . CYS A 1 134 ? 20.063  -11.799 -4.686  1.00 25.28 ? 136 CYS A SG  1 
ATOM   1082 N N   . LEU A 1 135 ? 16.680  -13.441 -1.523  1.00 19.72 ? 137 LEU A N   1 
ATOM   1083 C CA  . LEU A 1 135 ? 15.973  -14.450 -0.726  1.00 20.93 ? 137 LEU A CA  1 
ATOM   1084 C C   . LEU A 1 135 ? 14.475  -14.352 -0.954  1.00 21.09 ? 137 LEU A C   1 
ATOM   1085 O O   . LEU A 1 135 ? 13.866  -15.293 -1.462  1.00 21.62 ? 137 LEU A O   1 
ATOM   1086 C CB  . LEU A 1 135 ? 16.304  -14.352 0.768   1.00 19.64 ? 137 LEU A CB  1 
ATOM   1087 C CG  . LEU A 1 135 ? 17.421  -15.233 1.316   1.00 18.47 ? 137 LEU A CG  1 
ATOM   1088 C CD1 . LEU A 1 135 ? 18.697  -15.152 0.476   1.00 20.20 ? 137 LEU A CD1 1 
ATOM   1089 C CD2 . LEU A 1 135 ? 17.725  -14.868 2.741   1.00 18.10 ? 137 LEU A CD2 1 
ATOM   1090 N N   . ILE A 1 136 ? 13.863  -13.208 -0.608  1.00 21.96 ? 138 ILE A N   1 
ATOM   1091 C CA  . ILE A 1 136 ? 12.394  -13.098 -0.689  1.00 21.80 ? 138 ILE A CA  1 
ATOM   1092 C C   . ILE A 1 136 ? 11.907  -13.158 -2.117  1.00 21.99 ? 138 ILE A C   1 
ATOM   1093 O O   . ILE A 1 136 ? 10.785  -13.655 -2.352  1.00 23.58 ? 138 ILE A O   1 
ATOM   1094 C CB  . ILE A 1 136 ? 11.813  -11.849 0.072   1.00 21.72 ? 138 ILE A CB  1 
ATOM   1095 C CG1 . ILE A 1 136 ? 12.127  -10.555 -0.676  1.00 21.24 ? 138 ILE A CG1 1 
ATOM   1096 C CG2 . ILE A 1 136 ? 12.317  -11.864 1.537   1.00 22.26 ? 138 ILE A CG2 1 
ATOM   1097 C CD1 . ILE A 1 136 ? 11.720  -9.372  -0.057  1.00 25.03 ? 138 ILE A CD1 1 
ATOM   1098 N N   . GLY A 1 137 ? 12.691  -12.658 -3.050  1.00 22.07 ? 139 GLY A N   1 
ATOM   1099 C CA  . GLY A 1 137 ? 12.319  -12.704 -4.467  1.00 23.48 ? 139 GLY A CA  1 
ATOM   1100 C C   . GLY A 1 137 ? 12.481  -14.017 -5.177  1.00 23.87 ? 139 GLY A C   1 
ATOM   1101 O O   . GLY A 1 137 ? 12.110  -14.117 -6.335  1.00 25.10 ? 139 GLY A O   1 
ATOM   1102 N N   . GLU A 1 138 ? 13.021  -15.051 -4.527  1.00 24.93 ? 140 GLU A N   1 
ATOM   1103 C CA  . GLU A 1 138 ? 13.297  -16.345 -5.186  1.00 24.35 ? 140 GLU A CA  1 
ATOM   1104 C C   . GLU A 1 138 ? 14.191  -16.258 -6.478  1.00 25.23 ? 140 GLU A C   1 
ATOM   1105 O O   . GLU A 1 138 ? 13.826  -16.770 -7.560  1.00 24.77 ? 140 GLU A O   1 
ATOM   1106 C CB  . GLU A 1 138 ? 11.989  -17.080 -5.487  1.00 24.18 ? 140 GLU A CB  1 
ATOM   1107 C CG  . GLU A 1 138 ? 11.111  -17.284 -4.256  1.00 26.82 ? 140 GLU A CG  1 
ATOM   1108 C CD  . GLU A 1 138 ? 11.573  -18.293 -3.215  1.00 30.34 ? 140 GLU A CD  1 
ATOM   1109 O OE1 . GLU A 1 138 ? 11.950  -19.427 -3.605  1.00 27.63 ? 140 GLU A OE1 1 
ATOM   1110 O OE2 . GLU A 1 138 ? 11.529  -17.957 -2.009  1.00 28.80 ? 140 GLU A OE2 1 
ATOM   1111 N N   . SER A 1 139 ? 15.350  -15.641 -6.338  1.00 25.39 ? 141 SER A N   1 
ATOM   1112 C CA  . SER A 1 139 ? 16.198  -15.212 -7.438  1.00 26.09 ? 141 SER A CA  1 
ATOM   1113 C C   . SER A 1 139 ? 17.045  -16.325 -8.078  1.00 24.65 ? 141 SER A C   1 
ATOM   1114 O O   . SER A 1 139 ? 17.688  -16.102 -9.064  1.00 21.90 ? 141 SER A O   1 
ATOM   1115 C CB  . SER A 1 139 ? 17.084  -14.064 -6.972  1.00 28.69 ? 141 SER A CB  1 
ATOM   1116 O OG  . SER A 1 139 ? 16.347  -12.948 -6.492  1.00 28.90 ? 141 SER A OG  1 
ATOM   1117 N N   . PHE A 1 140 ? 17.020  -17.530 -7.523  1.00 26.22 ? 142 PHE A N   1 
ATOM   1118 C CA  . PHE A 1 140 ? 17.877  -18.600 -7.982  1.00 27.43 ? 142 PHE A CA  1 
ATOM   1119 C C   . PHE A 1 140 ? 17.095  -19.647 -8.742  1.00 27.64 ? 142 PHE A C   1 
ATOM   1120 O O   . PHE A 1 140 ? 17.589  -20.732 -8.876  1.00 26.01 ? 142 PHE A O   1 
ATOM   1121 C CB  . PHE A 1 140 ? 18.645  -19.167 -6.768  1.00 27.71 ? 142 PHE A CB  1 
ATOM   1122 C CG  . PHE A 1 140 ? 19.328  -18.057 -5.972  1.00 24.75 ? 142 PHE A CG  1 
ATOM   1123 C CD1 . PHE A 1 140 ? 20.335  -17.305 -6.528  1.00 24.76 ? 142 PHE A CD1 1 
ATOM   1124 C CD2 . PHE A 1 140 ? 18.915  -17.743 -4.691  1.00 25.35 ? 142 PHE A CD2 1 
ATOM   1125 C CE1 . PHE A 1 140 ? 20.942  -16.277 -5.804  1.00 25.76 ? 142 PHE A CE1 1 
ATOM   1126 C CE2 . PHE A 1 140 ? 19.519  -16.708 -3.967  1.00 25.58 ? 142 PHE A CE2 1 
ATOM   1127 C CZ  . PHE A 1 140 ? 20.530  -15.989 -4.524  1.00 25.59 ? 142 PHE A CZ  1 
ATOM   1128 N N   . ASP A 1 141 ? 15.879  -19.331 -9.267  1.00 29.23 ? 143 ASP A N   1 
ATOM   1129 C CA  . ASP A 1 141 ? 15.127  -20.276 -10.117 1.00 31.80 ? 143 ASP A CA  1 
ATOM   1130 C C   . ASP A 1 141 ? 14.759  -21.529 -9.276  1.00 32.18 ? 143 ASP A C   1 
ATOM   1131 O O   . ASP A 1 141 ? 14.425  -21.296 -8.116  1.00 33.36 ? 143 ASP A O   1 
ATOM   1132 C CB  . ASP A 1 141 ? 15.891  -20.534 -11.471 1.00 37.50 ? 143 ASP A CB  1 
ATOM   1133 C CG  . ASP A 1 141 ? 15.862  -19.337 -12.420 1.00 52.10 ? 143 ASP A CG  1 
ATOM   1134 O OD1 . ASP A 1 141 ? 14.834  -18.587 -12.427 1.00 53.48 ? 143 ASP A OD1 1 
ATOM   1135 O OD2 . ASP A 1 141 ? 16.861  -19.136 -13.152 1.00 58.56 ? 143 ASP A OD2 1 
ATOM   1136 N N   . ASP A 1 142 ? 14.797  -22.805 -9.766  1.00 32.42 ? 144 ASP A N   1 
ATOM   1137 C CA  . ASP A 1 142 ? 14.395  -23.922 -8.864  1.00 34.69 ? 144 ASP A CA  1 
ATOM   1138 C C   . ASP A 1 142 ? 15.353  -24.032 -7.682  1.00 33.66 ? 144 ASP A C   1 
ATOM   1139 O O   . ASP A 1 142 ? 14.961  -24.518 -6.613  1.00 34.50 ? 144 ASP A O   1 
ATOM   1140 C CB  . ASP A 1 142 ? 14.287  -25.290 -9.561  1.00 40.81 ? 144 ASP A CB  1 
ATOM   1141 C CG  . ASP A 1 142 ? 13.161  -25.476 -10.577 1.00 51.00 ? 144 ASP A CG  1 
ATOM   1142 O OD1 . ASP A 1 142 ? 12.402  -24.499 -10.829 1.00 52.22 ? 144 ASP A OD1 1 
ATOM   1143 O OD2 . ASP A 1 142 ? 13.038  -26.597 -11.121 1.00 56.89 ? 144 ASP A OD2 1 
ATOM   1144 N N   . TYR A 1 143 ? 16.613  -23.566 -7.875  1.00 31.00 ? 145 TYR A N   1 
ATOM   1145 C CA  . TYR A 1 143 ? 17.644  -23.681 -6.861  1.00 28.75 ? 145 TYR A CA  1 
ATOM   1146 C C   . TYR A 1 143 ? 17.397  -22.777 -5.632  1.00 25.16 ? 145 TYR A C   1 
ATOM   1147 O O   . TYR A 1 143 ? 18.127  -22.885 -4.671  1.00 23.48 ? 145 TYR A O   1 
ATOM   1148 C CB  . TYR A 1 143 ? 19.001  -23.340 -7.485  1.00 29.53 ? 145 TYR A CB  1 
ATOM   1149 C CG  . TYR A 1 143 ? 19.348  -24.174 -8.697  1.00 30.97 ? 145 TYR A CG  1 
ATOM   1150 C CD1 . TYR A 1 143 ? 19.216  -25.552 -8.679  1.00 33.44 ? 145 TYR A CD1 1 
ATOM   1151 C CD2 . TYR A 1 143 ? 19.743  -23.578 -9.881  1.00 33.15 ? 145 TYR A CD2 1 
ATOM   1152 C CE1 . TYR A 1 143 ? 19.569  -26.326 -9.779  1.00 34.85 ? 145 TYR A CE1 1 
ATOM   1153 C CE2 . TYR A 1 143 ? 20.060  -24.334 -11.004 1.00 35.31 ? 145 TYR A CE2 1 
ATOM   1154 C CZ  . TYR A 1 143 ? 19.994  -25.709 -10.944 1.00 37.87 ? 145 TYR A CZ  1 
ATOM   1155 O OH  . TYR A 1 143 ? 20.332  -26.447 -12.071 1.00 43.78 ? 145 TYR A OH  1 
ATOM   1156 N N   . SER A 1 144 ? 16.394  -21.880 -5.665  1.00 25.33 ? 146 SER A N   1 
ATOM   1157 C CA  . SER A 1 144 ? 15.996  -21.138 -4.474  1.00 23.93 ? 146 SER A CA  1 
ATOM   1158 C C   . SER A 1 144 ? 15.502  -22.061 -3.390  1.00 21.60 ? 146 SER A C   1 
ATOM   1159 O O   . SER A 1 144 ? 15.597  -21.688 -2.250  1.00 21.84 ? 146 SER A O   1 
ATOM   1160 C CB  . SER A 1 144 ? 14.996  -20.027 -4.786  1.00 25.91 ? 146 SER A CB  1 
ATOM   1161 O OG  . SER A 1 144 ? 15.554  -18.961 -5.523  1.00 26.33 ? 146 SER A OG  1 
ATOM   1162 N N   . ASP A 1 145 ? 15.000  -23.260 -3.702  1.00 21.86 ? 147 ASP A N   1 
ATOM   1163 C CA  . ASP A 1 145 ? 14.610  -24.216 -2.682  1.00 22.23 ? 147 ASP A CA  1 
ATOM   1164 C C   . ASP A 1 145 ? 15.820  -24.645 -1.851  1.00 21.21 ? 147 ASP A C   1 
ATOM   1165 O O   . ASP A 1 145 ? 15.642  -25.041 -0.667  1.00 20.73 ? 147 ASP A O   1 
ATOM   1166 C CB  . ASP A 1 145 ? 13.879  -25.436 -3.293  1.00 27.54 ? 147 ASP A CB  1 
ATOM   1167 C CG  . ASP A 1 145 ? 12.480  -25.135 -3.807  1.00 35.43 ? 147 ASP A CG  1 
ATOM   1168 O OD1 . ASP A 1 145 ? 11.817  -24.225 -3.257  1.00 36.64 ? 147 ASP A OD1 1 
ATOM   1169 O OD2 . ASP A 1 145 ? 12.051  -25.800 -4.769  1.00 41.34 ? 147 ASP A OD2 1 
ATOM   1170 N N   . ASP A 1 146 ? 17.051  -24.579 -2.426  1.00 19.51 ? 148 ASP A N   1 
ATOM   1171 C CA  . ASP A 1 146 ? 18.231  -24.900 -1.645  1.00 20.08 ? 148 ASP A CA  1 
ATOM   1172 C C   . ASP A 1 146 ? 18.612  -23.817 -0.635  1.00 20.63 ? 148 ASP A C   1 
ATOM   1173 O O   . ASP A 1 146 ? 19.419  -24.090 0.237   1.00 20.40 ? 148 ASP A O   1 
ATOM   1174 C CB  . ASP A 1 146 ? 19.434  -25.237 -2.562  1.00 21.56 ? 148 ASP A CB  1 
ATOM   1175 C CG  . ASP A 1 146 ? 19.503  -26.735 -2.836  1.00 26.55 ? 148 ASP A CG  1 
ATOM   1176 O OD1 . ASP A 1 146 ? 18.477  -27.301 -3.209  1.00 28.31 ? 148 ASP A OD1 1 
ATOM   1177 O OD2 . ASP A 1 146 ? 20.571  -27.330 -2.619  1.00 20.93 ? 148 ASP A OD2 1 
ATOM   1178 N N   . VAL A 1 147 ? 18.068  -22.606 -0.742  1.00 19.82 ? 149 VAL A N   1 
ATOM   1179 C CA  . VAL A 1 147 ? 18.410  -21.524 0.179   1.00 20.41 ? 149 VAL A CA  1 
ATOM   1180 C C   . VAL A 1 147 ? 17.718  -21.791 1.517   1.00 19.35 ? 149 VAL A C   1 
ATOM   1181 O O   . VAL A 1 147 ? 16.546  -22.137 1.542   1.00 18.83 ? 149 VAL A O   1 
ATOM   1182 C CB  . VAL A 1 147 ? 18.007  -20.156 -0.446  1.00 22.08 ? 149 VAL A CB  1 
ATOM   1183 C CG1 . VAL A 1 147 ? 18.214  -19.021 0.537   1.00 24.11 ? 149 VAL A CG1 1 
ATOM   1184 C CG2 . VAL A 1 147 ? 18.770  -19.906 -1.747  1.00 21.71 ? 149 VAL A CG2 1 
ATOM   1185 N N   . CYS A 1 148 ? 18.448  -21.650 2.617   1.00 19.11 ? 150 CYS A N   1 
ATOM   1186 C CA  . CYS A 1 148 ? 17.902  -21.699 3.968   1.00 19.88 ? 150 CYS A CA  1 
ATOM   1187 C C   . CYS A 1 148 ? 17.681  -20.295 4.490   1.00 20.00 ? 150 CYS A C   1 
ATOM   1188 O O   . CYS A 1 148 ? 16.648  -20.002 5.039   1.00 19.75 ? 150 CYS A O   1 
ATOM   1189 C CB  . CYS A 1 148 ? 18.833  -22.483 4.872   1.00 20.31 ? 150 CYS A CB  1 
ATOM   1190 S SG  . CYS A 1 148 ? 19.072  -24.183 4.340   1.00 23.12 ? 150 CYS A SG  1 
ATOM   1191 N N   . GLY A 1 149 ? 18.670  -19.438 4.297   1.00 20.32 ? 151 GLY A N   1 
ATOM   1192 C CA  . GLY A 1 149 ? 18.626  -18.079 4.796   1.00 18.59 ? 151 GLY A CA  1 
ATOM   1193 C C   . GLY A 1 149 ? 19.904  -17.348 4.522   1.00 18.00 ? 151 GLY A C   1 
ATOM   1194 O O   . GLY A 1 149 ? 20.764  -17.822 3.787   1.00 17.67 ? 151 GLY A O   1 
ATOM   1195 N N   . ALA A 1 150 ? 20.029  -16.154 5.129   1.00 17.01 ? 152 ALA A N   1 
ATOM   1196 C CA  . ALA A 1 150 ? 21.209  -15.311 5.033   1.00 18.64 ? 152 ALA A CA  1 
ATOM   1197 C C   . ALA A 1 150 ? 21.544  -14.774 6.403   1.00 18.63 ? 152 ALA A C   1 
ATOM   1198 O O   . ALA A 1 150 ? 20.622  -14.541 7.186   1.00 19.22 ? 152 ALA A O   1 
ATOM   1199 C CB  . ALA A 1 150 ? 20.952  -14.187 4.070   1.00 18.52 ? 152 ALA A CB  1 
ATOM   1200 N N   . VAL A 1 151 ? 22.830  -14.613 6.705   1.00 19.58 ? 153 VAL A N   1 
ATOM   1201 C CA  . VAL A 1 151 ? 23.331  -14.092 7.954   1.00 20.19 ? 153 VAL A CA  1 
ATOM   1202 C C   . VAL A 1 151 ? 24.250  -12.860 7.740   1.00 20.55 ? 153 VAL A C   1 
ATOM   1203 O O   . VAL A 1 151 ? 25.080  -12.840 6.838   1.00 19.73 ? 153 VAL A O   1 
ATOM   1204 C CB  . VAL A 1 151 ? 24.153  -15.158 8.738   1.00 22.50 ? 153 VAL A CB  1 
ATOM   1205 C CG1 . VAL A 1 151 ? 24.668  -14.585 10.066  1.00 23.26 ? 153 VAL A CG1 1 
ATOM   1206 C CG2 . VAL A 1 151 ? 23.362  -16.411 8.993   1.00 24.05 ? 153 VAL A CG2 1 
ATOM   1207 N N   . VAL A 1 152 ? 24.106  -11.870 8.603   1.00 20.53 ? 154 VAL A N   1 
ATOM   1208 C CA  . VAL A 1 152 ? 25.061  -10.791 8.698   1.00 22.05 ? 154 VAL A CA  1 
ATOM   1209 C C   . VAL A 1 152 ? 25.738  -10.828 10.102  1.00 22.07 ? 154 VAL A C   1 
ATOM   1210 O O   . VAL A 1 152 ? 25.089  -10.732 11.138  1.00 19.30 ? 154 VAL A O   1 
ATOM   1211 C CB  . VAL A 1 152 ? 24.485  -9.400  8.286   1.00 23.87 ? 154 VAL A CB  1 
ATOM   1212 C CG1 . VAL A 1 152 ? 23.242  -9.040  9.079   1.00 27.10 ? 154 VAL A CG1 1 
ATOM   1213 C CG2 . VAL A 1 152 ? 25.534  -8.320  8.435   1.00 23.88 ? 154 VAL A CG2 1 
ATOM   1214 N N   . ASN A 1 153 ? 27.052  -10.976 10.114  1.00 23.94 ? 155 ASN A N   1 
ATOM   1215 C CA  . ASN A 1 153 ? 27.832  -10.836 11.336  1.00 26.39 ? 155 ASN A CA  1 
ATOM   1216 C C   . ASN A 1 153 ? 28.517  -9.446  11.366  1.00 27.66 ? 155 ASN A C   1 
ATOM   1217 O O   . ASN A 1 153 ? 29.370  -9.129  10.514  1.00 28.39 ? 155 ASN A O   1 
ATOM   1218 C CB  . ASN A 1 153 ? 28.833  -11.977 11.485  1.00 28.57 ? 155 ASN A CB  1 
ATOM   1219 C CG  . ASN A 1 153 ? 28.351  -13.387 11.142  1.00 29.56 ? 155 ASN A CG  1 
ATOM   1220 O OD1 . ASN A 1 153 ? 28.591  -13.946 10.071  1.00 30.30 ? 155 ASN A OD1 1 
ATOM   1221 N ND2 . ASN A 1 153 ? 27.678  -14.011 12.052  1.00 30.61 ? 155 ASN A ND2 1 
ATOM   1222 N N   . VAL A 1 154 ? 28.122  -8.619  12.357  1.00 27.54 ? 156 VAL A N   1 
ATOM   1223 C CA  . VAL A 1 154 ? 28.617  -7.266  12.524  1.00 29.04 ? 156 VAL A CA  1 
ATOM   1224 C C   . VAL A 1 154 ? 29.810  -7.417  13.399  1.00 30.34 ? 156 VAL A C   1 
ATOM   1225 O O   . VAL A 1 154 ? 29.637  -7.843  14.530  1.00 28.81 ? 156 VAL A O   1 
ATOM   1226 C CB  . VAL A 1 154 ? 27.561  -6.364  13.189  1.00 30.36 ? 156 VAL A CB  1 
ATOM   1227 C CG1 . VAL A 1 154 ? 28.022  -4.917  13.276  1.00 30.27 ? 156 VAL A CG1 1 
ATOM   1228 C CG2 . VAL A 1 154 ? 26.224  -6.471  12.440  1.00 31.47 ? 156 VAL A CG2 1 
ATOM   1229 N N   . ARG A 1 155 ? 31.031  -7.089  12.881  1.00 31.61 ? 157 ARG A N   1 
ATOM   1230 C CA  . ARG A 1 155 ? 32.278  -7.299  13.648  1.00 33.71 ? 157 ARG A CA  1 
ATOM   1231 C C   . ARG A 1 155 ? 33.263  -6.131  13.523  1.00 35.46 ? 157 ARG A C   1 
ATOM   1232 O O   . ARG A 1 155 ? 33.203  -5.413  12.558  1.00 35.90 ? 157 ARG A O   1 
ATOM   1233 C CB  . ARG A 1 155 ? 32.988  -8.619  13.244  1.00 31.21 ? 157 ARG A CB  1 
ATOM   1234 C CG  . ARG A 1 155 ? 32.160  -9.857  13.443  1.00 33.99 ? 157 ARG A CG  1 
ATOM   1235 C CD  . ARG A 1 155 ? 32.184  -10.387 14.856  1.00 38.15 ? 157 ARG A CD  1 
ATOM   1236 N NE  . ARG A 1 155 ? 31.462  -11.662 14.966  1.00 41.19 ? 157 ARG A NE  1 
ATOM   1237 C CZ  . ARG A 1 155 ? 30.132  -11.806 14.991  1.00 42.07 ? 157 ARG A CZ  1 
ATOM   1238 N NH1 . ARG A 1 155 ? 29.331  -10.736 14.923  1.00 39.05 ? 157 ARG A NH1 1 
ATOM   1239 N NH2 . ARG A 1 155 ? 29.591  -13.018 15.082  1.00 42.50 ? 157 ARG A NH2 1 
ATOM   1240 N N   . ALA A 1 156 ? 34.168  -5.976  14.456  1.00 37.74 ? 158 ALA A N   1 
ATOM   1241 C CA  . ALA A 1 156 ? 35.121  -4.834  14.462  1.00 40.74 ? 158 ALA A CA  1 
ATOM   1242 C C   . ALA A 1 156 ? 36.158  -4.995  13.350  1.00 41.69 ? 158 ALA A C   1 
ATOM   1243 O O   . ALA A 1 156 ? 36.487  -4.031  12.670  1.00 42.55 ? 158 ALA A O   1 
ATOM   1244 C CB  . ALA A 1 156 ? 35.828  -4.744  15.820  1.00 42.17 ? 158 ALA A CB  1 
ATOM   1245 N N   . LYS A 1 157 ? 36.643  -6.213  13.188  1.00 41.97 ? 159 LYS A N   1 
ATOM   1246 C CA  . LYS A 1 157 ? 37.615  -6.625  12.185  1.00 42.85 ? 159 LYS A CA  1 
ATOM   1247 C C   . LYS A 1 157 ? 37.060  -6.498  10.762  1.00 42.32 ? 159 LYS A C   1 
ATOM   1248 O O   . LYS A 1 157 ? 37.820  -6.247  9.828   1.00 43.09 ? 159 LYS A O   1 
ATOM   1249 C CB  . LYS A 1 157 ? 38.031  -8.095  12.471  1.00 45.71 ? 159 LYS A CB  1 
ATOM   1250 C CG  . LYS A 1 157 ? 39.005  -8.714  11.505  1.00 49.31 ? 159 LYS A CG  1 
ATOM   1251 C CD  . LYS A 1 157 ? 39.436  -10.104 12.070  1.00 52.38 ? 159 LYS A CD  1 
ATOM   1252 C CE  . LYS A 1 157 ? 39.596  -11.203 11.043  1.00 52.82 ? 159 LYS A CE  1 
ATOM   1253 N NZ  . LYS A 1 157 ? 38.324  -11.488 10.295  1.00 52.11 ? 159 LYS A NZ  1 
ATOM   1254 N N   . GLY A 1 158 ? 35.760  -6.695  10.589  1.00 40.53 ? 160 GLY A N   1 
ATOM   1255 C CA  . GLY A 1 158 ? 35.162  -6.685  9.270   1.00 39.63 ? 160 GLY A CA  1 
ATOM   1256 C C   . GLY A 1 158 ? 33.930  -7.562  9.215   1.00 37.92 ? 160 GLY A C   1 
ATOM   1257 O O   . GLY A 1 158 ? 33.896  -8.672  9.746   1.00 38.85 ? 160 GLY A O   1 
ATOM   1258 N N   . ASP A 1 159 ? 32.943  -7.055  8.543   1.00 33.78 ? 161 ASP A N   1 
ATOM   1259 C CA  . ASP A 1 159 ? 31.628  -7.604  8.595   1.00 29.88 ? 161 ASP A CA  1 
ATOM   1260 C C   . ASP A 1 159 ? 31.534  -8.787  7.656   1.00 28.67 ? 161 ASP A C   1 
ATOM   1261 O O   . ASP A 1 159 ? 32.240  -8.821  6.660   1.00 29.29 ? 161 ASP A O   1 
ATOM   1262 C CB  . ASP A 1 159 ? 30.618  -6.513  8.261   1.00 27.44 ? 161 ASP A CB  1 
ATOM   1263 C CG  . ASP A 1 159 ? 30.623  -5.379  9.286   1.00 29.14 ? 161 ASP A CG  1 
ATOM   1264 O OD1 . ASP A 1 159 ? 30.768  -5.665  10.477  1.00 27.93 ? 161 ASP A OD1 1 
ATOM   1265 O OD2 . ASP A 1 159 ? 30.470  -4.218  8.884   1.00 30.21 ? 161 ASP A OD2 1 
ATOM   1266 N N   . LYS A 1 160 ? 30.663  -9.757  7.989   1.00 26.36 ? 162 LYS A N   1 
ATOM   1267 C CA  . LYS A 1 160 ? 30.426  -10.932 7.127   1.00 24.53 ? 162 LYS A CA  1 
ATOM   1268 C C   . LYS A 1 160 ? 29.000  -10.994 6.711   1.00 20.85 ? 162 LYS A C   1 
ATOM   1269 O O   . LYS A 1 160 ? 28.103  -10.778 7.551   1.00 18.89 ? 162 LYS A O   1 
ATOM   1270 C CB  . LYS A 1 160 ? 30.813  -12.244 7.817   1.00 26.79 ? 162 LYS A CB  1 
ATOM   1271 C CG  . LYS A 1 160 ? 32.299  -12.355 8.071   1.00 30.94 ? 162 LYS A CG  1 
ATOM   1272 C CD  . LYS A 1 160 ? 32.644  -13.678 8.783   1.00 39.97 ? 162 LYS A CD  1 
ATOM   1273 C CE  . LYS A 1 160 ? 32.963  -13.465 10.260  1.00 45.87 ? 162 LYS A CE  1 
ATOM   1274 N NZ  . LYS A 1 160 ? 33.520  -14.706 10.915  1.00 46.89 ? 162 LYS A NZ  1 
ATOM   1275 N N   . ILE A 1 161 ? 28.770  -11.280 5.421   1.00 19.08 ? 163 ILE A N   1 
ATOM   1276 C CA  . ILE A 1 161 ? 27.422  -11.522 4.908   1.00 19.69 ? 163 ILE A CA  1 
ATOM   1277 C C   . ILE A 1 161 ? 27.478  -12.852 4.131   1.00 19.55 ? 163 ILE A C   1 
ATOM   1278 O O   . ILE A 1 161 ? 28.378  -13.050 3.349   1.00 17.60 ? 163 ILE A O   1 
ATOM   1279 C CB  . ILE A 1 161 ? 26.965  -10.398 3.968   1.00 21.39 ? 163 ILE A CB  1 
ATOM   1280 C CG1 . ILE A 1 161 ? 26.926  -9.042  4.670   1.00 22.95 ? 163 ILE A CG1 1 
ATOM   1281 C CG2 . ILE A 1 161 ? 25.597  -10.773 3.313   1.00 22.51 ? 163 ILE A CG2 1 
ATOM   1282 C CD1 . ILE A 1 161 ? 26.660  -7.890  3.735   1.00 25.32 ? 163 ILE A CD1 1 
ATOM   1283 N N   . ALA A 1 162 ? 26.487  -13.725 4.329   1.00 18.99 ? 164 ALA A N   1 
ATOM   1284 C CA  . ALA A 1 162 ? 26.513  -15.070 3.784   1.00 19.55 ? 164 ALA A CA  1 
ATOM   1285 C C   . ALA A 1 162 ? 25.141  -15.557 3.449   1.00 19.99 ? 164 ALA A C   1 
ATOM   1286 O O   . ALA A 1 162 ? 24.208  -15.274 4.206   1.00 21.93 ? 164 ALA A O   1 
ATOM   1287 C CB  . ALA A 1 162 ? 27.165  -16.027 4.768   1.00 19.43 ? 164 ALA A CB  1 
ATOM   1288 N N   . ILE A 1 163 ? 24.978  -16.245 2.313   1.00 17.95 ? 165 ILE A N   1 
ATOM   1289 C CA  . ILE A 1 163 ? 23.782  -17.055 2.052   1.00 17.57 ? 165 ILE A CA  1 
ATOM   1290 C C   . ILE A 1 163 ? 24.060  -18.523 2.373   1.00 18.06 ? 165 ILE A C   1 
ATOM   1291 O O   . ILE A 1 163 ? 24.986  -19.142 1.817   1.00 17.06 ? 165 ILE A O   1 
ATOM   1292 C CB  . ILE A 1 163 ? 23.277  -16.934 0.602   1.00 18.09 ? 165 ILE A CB  1 
ATOM   1293 C CG1 . ILE A 1 163 ? 22.743  -15.498 0.331   1.00 18.00 ? 165 ILE A CG1 1 
ATOM   1294 C CG2 . ILE A 1 163 ? 22.202  -18.008 0.323   1.00 18.00 ? 165 ILE A CG2 1 
ATOM   1295 C CD1 . ILE A 1 163 ? 22.318  -15.239 -1.031  1.00 19.32 ? 165 ILE A CD1 1 
ATOM   1296 N N   . TRP A 1 164 ? 23.205  -19.055 3.260   1.00 18.72 ? 166 TRP A N   1 
ATOM   1297 C CA  . TRP A 1 164 ? 23.208  -20.404 3.769   1.00 19.52 ? 166 TRP A CA  1 
ATOM   1298 C C   . TRP A 1 164 ? 22.340  -21.245 2.830   1.00 19.05 ? 166 TRP A C   1 
ATOM   1299 O O   . TRP A 1 164 ? 21.214  -20.868 2.489   1.00 18.66 ? 166 TRP A O   1 
ATOM   1300 C CB  . TRP A 1 164 ? 22.675  -20.426 5.218   1.00 20.20 ? 166 TRP A CB  1 
ATOM   1301 C CG  . TRP A 1 164 ? 23.650  -19.966 6.248   1.00 21.34 ? 166 TRP A CG  1 
ATOM   1302 C CD1 . TRP A 1 164 ? 24.544  -18.949 6.123   1.00 22.61 ? 166 TRP A CD1 1 
ATOM   1303 C CD2 . TRP A 1 164 ? 23.807  -20.475 7.581   1.00 22.06 ? 166 TRP A CD2 1 
ATOM   1304 N NE1 . TRP A 1 164 ? 25.223  -18.776 7.295   1.00 23.09 ? 166 TRP A NE1 1 
ATOM   1305 C CE2 . TRP A 1 164 ? 24.794  -19.697 8.210   1.00 23.40 ? 166 TRP A CE2 1 
ATOM   1306 C CE3 . TRP A 1 164 ? 23.206  -21.493 8.302   1.00 23.54 ? 166 TRP A CE3 1 
ATOM   1307 C CZ2 . TRP A 1 164 ? 25.234  -19.948 9.510   1.00 24.52 ? 166 TRP A CZ2 1 
ATOM   1308 C CZ3 . TRP A 1 164 ? 23.613  -21.725 9.606   1.00 25.16 ? 166 TRP A CZ3 1 
ATOM   1309 C CH2 . TRP A 1 164 ? 24.635  -20.959 10.184  1.00 25.72 ? 166 TRP A CH2 1 
ATOM   1310 N N   . THR A 1 165 ? 22.869  -22.386 2.398   1.00 19.29 ? 167 THR A N   1 
ATOM   1311 C CA  . THR A 1 165 ? 22.123  -23.350 1.592   1.00 20.50 ? 167 THR A CA  1 
ATOM   1312 C C   . THR A 1 165 ? 22.116  -24.684 2.325   1.00 20.36 ? 167 THR A C   1 
ATOM   1313 O O   . THR A 1 165 ? 22.902  -24.915 3.266   1.00 19.98 ? 167 THR A O   1 
ATOM   1314 C CB  . THR A 1 165 ? 22.615  -23.405 0.110   1.00 23.72 ? 167 THR A CB  1 
ATOM   1315 O OG1 . THR A 1 165 ? 23.770  -24.256 0.000   1.00 24.95 ? 167 THR A OG1 1 
ATOM   1316 C CG2 . THR A 1 165 ? 22.894  -22.029 -0.458  1.00 25.88 ? 167 THR A CG2 1 
ATOM   1317 N N   . THR A 1 166 ? 21.206  -25.564 1.894   1.00 19.52 ? 168 THR A N   1 
ATOM   1318 C CA  . THR A 1 166 ? 20.871  -26.780 2.635   1.00 20.68 ? 168 THR A CA  1 
ATOM   1319 C C   . THR A 1 166 ? 21.808  -28.005 2.439   1.00 20.83 ? 168 THR A C   1 
ATOM   1320 O O   . THR A 1 166 ? 21.866  -28.873 3.350   1.00 20.54 ? 168 THR A O   1 
ATOM   1321 C CB  . THR A 1 166 ? 19.421  -27.159 2.313   1.00 24.13 ? 168 THR A CB  1 
ATOM   1322 O OG1 . THR A 1 166 ? 18.950  -28.085 3.306   1.00 27.13 ? 168 THR A OG1 1 
ATOM   1323 C CG2 . THR A 1 166 ? 19.234  -27.688 0.864   1.00 24.42 ? 168 THR A CG2 1 
ATOM   1324 N N   . GLU A 1 167 ? 22.513  -28.086 1.296   1.00 19.98 ? 169 GLU A N   1 
ATOM   1325 C CA  . GLU A 1 167 ? 23.224  -29.303 0.884   1.00 19.52 ? 169 GLU A CA  1 
ATOM   1326 C C   . GLU A 1 167 ? 24.516  -28.972 0.140   1.00 20.98 ? 169 GLU A C   1 
ATOM   1327 O O   . GLU A 1 167 ? 24.462  -28.605 -1.049  1.00 21.81 ? 169 GLU A O   1 
ATOM   1328 C CB  . GLU A 1 167 ? 22.298  -30.194 0.014   1.00 19.82 ? 169 GLU A CB  1 
ATOM   1329 C CG  . GLU A 1 167 ? 22.873  -31.493 -0.483  1.00 22.14 ? 169 GLU A CG  1 
ATOM   1330 C CD  . GLU A 1 167 ? 23.611  -32.270 0.594   1.00 25.22 ? 169 GLU A CD  1 
ATOM   1331 O OE1 . GLU A 1 167 ? 22.947  -32.836 1.482   1.00 24.98 ? 169 GLU A OE1 1 
ATOM   1332 O OE2 . GLU A 1 167 ? 24.858  -32.273 0.576   1.00 26.27 ? 169 GLU A OE2 1 
ATOM   1333 N N   . CYS A 1 168 ? 25.681  -29.088 0.805   1.00 20.17 ? 170 CYS A N   1 
ATOM   1334 C CA  . CYS A 1 168 ? 26.926  -28.725 0.142   1.00 23.84 ? 170 CYS A CA  1 
ATOM   1335 C C   . CYS A 1 168 ? 27.287  -29.647 -1.001  1.00 25.74 ? 170 CYS A C   1 
ATOM   1336 O O   . CYS A 1 168 ? 28.143  -29.246 -1.762  1.00 28.43 ? 170 CYS A O   1 
ATOM   1337 C CB  . CYS A 1 168 ? 28.070  -28.599 1.143   1.00 27.35 ? 170 CYS A CB  1 
ATOM   1338 S SG  . CYS A 1 168 ? 28.499  -30.170 1.934   1.00 36.09 ? 170 CYS A SG  1 
ATOM   1339 N N   . GLU A 1 169 ? 26.674  -30.840 -1.171  1.00 24.61 ? 171 GLU A N   1 
ATOM   1340 C CA  . GLU A 1 169 ? 26.996  -31.724 -2.294  1.00 25.33 ? 171 GLU A CA  1 
ATOM   1341 C C   . GLU A 1 169 ? 26.125  -31.487 -3.542  1.00 26.54 ? 171 GLU A C   1 
ATOM   1342 O O   . GLU A 1 169 ? 26.312  -32.168 -4.544  1.00 27.38 ? 171 GLU A O   1 
ATOM   1343 C CB  . GLU A 1 169 ? 26.892  -33.230 -1.872  1.00 25.02 ? 171 GLU A CB  1 
ATOM   1344 C CG  . GLU A 1 169 ? 27.748  -33.617 -0.668  1.00 29.84 ? 171 GLU A CG  1 
ATOM   1345 C CD  . GLU A 1 169 ? 29.249  -33.458 -0.751  1.00 30.91 ? 171 GLU A CD  1 
ATOM   1346 O OE1 . GLU A 1 169 ? 29.810  -33.454 -1.876  1.00 30.87 ? 171 GLU A OE1 1 
ATOM   1347 O OE2 . GLU A 1 169 ? 29.871  -33.351 0.338   1.00 29.37 ? 171 GLU A OE2 1 
ATOM   1348 N N   . ASN A 1 170 ? 25.165  -30.550 -3.481  1.00 26.55 ? 172 ASN A N   1 
ATOM   1349 C CA  . ASN A 1 170 ? 24.375  -30.117 -4.662  1.00 24.54 ? 172 ASN A CA  1 
ATOM   1350 C C   . ASN A 1 170 ? 25.164  -29.041 -5.419  1.00 23.53 ? 172 ASN A C   1 
ATOM   1351 O O   . ASN A 1 170 ? 24.853  -27.850 -5.340  1.00 20.94 ? 172 ASN A O   1 
ATOM   1352 C CB  . ASN A 1 170 ? 23.008  -29.553 -4.236  1.00 23.46 ? 172 ASN A CB  1 
ATOM   1353 C CG  . ASN A 1 170 ? 21.954  -30.600 -3.966  1.00 21.43 ? 172 ASN A CG  1 
ATOM   1354 O OD1 . ASN A 1 170 ? 22.126  -31.796 -4.228  1.00 23.96 ? 172 ASN A OD1 1 
ATOM   1355 N ND2 . ASN A 1 170 ? 20.844  -30.168 -3.420  1.00 16.88 ? 172 ASN A ND2 1 
ATOM   1356 N N   . ARG A 1 171 ? 26.191  -29.482 -6.180  1.00 25.08 ? 173 ARG A N   1 
ATOM   1357 C CA  . ARG A 1 171 ? 27.106  -28.536 -6.814  1.00 25.75 ? 173 ARG A CA  1 
ATOM   1358 C C   . ARG A 1 171 ? 26.365  -27.609 -7.789  1.00 26.80 ? 173 ARG A C   1 
ATOM   1359 O O   . ARG A 1 171 ? 26.588  -26.418 -7.752  1.00 25.15 ? 173 ARG A O   1 
ATOM   1360 C CB  . ARG A 1 171 ? 28.247  -29.285 -7.499  1.00 27.51 ? 173 ARG A CB  1 
ATOM   1361 C CG  . ARG A 1 171 ? 29.289  -28.444 -8.264  1.00 33.38 ? 173 ARG A CG  1 
ATOM   1362 C CD  . ARG A 1 171 ? 28.890  -28.169 -9.721  1.00 39.84 ? 173 ARG A CD  1 
ATOM   1363 N NE  . ARG A 1 171 ? 28.604  -29.406 -10.456 1.00 42.42 ? 173 ARG A NE  1 
ATOM   1364 C CZ  . ARG A 1 171 ? 27.889  -29.487 -11.572 1.00 47.37 ? 173 ARG A CZ  1 
ATOM   1365 N NH1 . ARG A 1 171 ? 27.372  -28.396 -12.119 1.00 48.55 ? 173 ARG A NH1 1 
ATOM   1366 N NH2 . ARG A 1 171 ? 27.681  -30.665 -12.151 1.00 49.35 ? 173 ARG A NH2 1 
ATOM   1367 N N   . GLU A 1 172 ? 25.485  -28.157 -8.645  1.00 27.84 ? 174 GLU A N   1 
ATOM   1368 C CA  . GLU A 1 172 ? 24.775  -27.367 -9.672  1.00 30.09 ? 174 GLU A CA  1 
ATOM   1369 C C   . GLU A 1 172 ? 23.893  -26.272 -9.032  1.00 29.51 ? 174 GLU A C   1 
ATOM   1370 O O   . GLU A 1 172 ? 23.827  -25.152 -9.562  1.00 30.19 ? 174 GLU A O   1 
ATOM   1371 C CB  . GLU A 1 172 ? 23.955  -28.314 -10.574 1.00 33.49 ? 174 GLU A CB  1 
ATOM   1372 C CG  . GLU A 1 172 ? 23.217  -27.636 -11.715 1.00 48.09 ? 174 GLU A CG  1 
ATOM   1373 C CD  . GLU A 1 172 ? 23.944  -27.444 -13.040 1.00 61.52 ? 174 GLU A CD  1 
ATOM   1374 O OE1 . GLU A 1 172 ? 23.260  -27.476 -14.095 1.00 63.45 ? 174 GLU A OE1 1 
ATOM   1375 O OE2 . GLU A 1 172 ? 25.187  -27.262 -13.030 1.00 64.77 ? 174 GLU A OE2 1 
ATOM   1376 N N   . ALA A 1 173 ? 23.223  -26.593 -7.894  1.00 28.18 ? 175 ALA A N   1 
ATOM   1377 C CA  . ALA A 1 173 ? 22.379  -25.623 -7.179  1.00 27.75 ? 175 ALA A CA  1 
ATOM   1378 C C   . ALA A 1 173 ? 23.249  -24.508 -6.548  1.00 26.52 ? 175 ALA A C   1 
ATOM   1379 O O   . ALA A 1 173 ? 22.942  -23.307 -6.667  1.00 23.53 ? 175 ALA A O   1 
ATOM   1380 C CB  . ALA A 1 173 ? 21.539  -26.326 -6.111  1.00 27.64 ? 175 ALA A CB  1 
ATOM   1381 N N   . VAL A 1 174 ? 24.321  -24.960 -5.887  1.00 26.19 ? 176 VAL A N   1 
ATOM   1382 C CA  . VAL A 1 174 ? 25.190  -24.163 -5.085  1.00 25.69 ? 176 VAL A CA  1 
ATOM   1383 C C   . VAL A 1 174 ? 25.912  -23.166 -5.990  1.00 26.32 ? 176 VAL A C   1 
ATOM   1384 O O   . VAL A 1 174 ? 25.957  -21.973 -5.667  1.00 25.90 ? 176 VAL A O   1 
ATOM   1385 C CB  . VAL A 1 174 ? 26.160  -25.063 -4.252  1.00 24.39 ? 176 VAL A CB  1 
ATOM   1386 C CG1 . VAL A 1 174 ? 27.338  -24.315 -3.727  1.00 24.97 ? 176 VAL A CG1 1 
ATOM   1387 C CG2 . VAL A 1 174 ? 25.418  -25.749 -3.103  1.00 25.73 ? 176 VAL A CG2 1 
ATOM   1388 N N   . THR A 1 175 ? 26.464  -23.644 -7.107  1.00 26.16 ? 177 THR A N   1 
ATOM   1389 C CA  . THR A 1 175 ? 27.245  -22.816 -7.981  1.00 26.84 ? 177 THR A CA  1 
ATOM   1390 C C   . THR A 1 175 ? 26.372  -21.788 -8.678  1.00 27.25 ? 177 THR A C   1 
ATOM   1391 O O   . THR A 1 175 ? 26.819  -20.664 -8.872  1.00 27.05 ? 177 THR A O   1 
ATOM   1392 C CB  . THR A 1 175 ? 28.130  -23.662 -8.958  1.00 29.28 ? 177 THR A CB  1 
ATOM   1393 O OG1 . THR A 1 175 ? 27.316  -24.517 -9.759  1.00 33.25 ? 177 THR A OG1 1 
ATOM   1394 C CG2 . THR A 1 175 ? 29.113  -24.513 -8.236  1.00 28.27 ? 177 THR A CG2 1 
ATOM   1395 N N   . HIS A 1 176 ? 25.151  -22.163 -9.060  1.00 26.81 ? 178 HIS A N   1 
ATOM   1396 C CA  . HIS A 1 176 ? 24.185  -21.241 -9.644  1.00 25.88 ? 178 HIS A CA  1 
ATOM   1397 C C   . HIS A 1 176 ? 23.773  -20.162 -8.659  1.00 25.27 ? 178 HIS A C   1 
ATOM   1398 O O   . HIS A 1 176 ? 23.723  -18.974 -9.024  1.00 25.18 ? 178 HIS A O   1 
ATOM   1399 C CB  . HIS A 1 176 ? 22.922  -21.987 -10.109 1.00 26.79 ? 178 HIS A CB  1 
ATOM   1400 C CG  . HIS A 1 176 ? 21.907  -21.122 -10.807 1.00 28.33 ? 178 HIS A CG  1 
ATOM   1401 N ND1 . HIS A 1 176 ? 21.790  -21.195 -12.163 1.00 31.20 ? 178 HIS A ND1 1 
ATOM   1402 C CD2 . HIS A 1 176 ? 20.990  -20.235 -10.353 1.00 31.36 ? 178 HIS A CD2 1 
ATOM   1403 C CE1 . HIS A 1 176 ? 20.848  -20.334 -12.535 1.00 31.55 ? 178 HIS A CE1 1 
ATOM   1404 N NE2 . HIS A 1 176 ? 20.321  -19.734 -11.496 1.00 31.47 ? 178 HIS A NE2 1 
ATOM   1405 N N   . ILE A 1 177 ? 23.475  -20.538 -7.385  1.00 23.49 ? 179 ILE A N   1 
ATOM   1406 C CA  . ILE A 1 177 ? 23.206  -19.540 -6.332  1.00 21.53 ? 179 ILE A CA  1 
ATOM   1407 C C   . ILE A 1 177 ? 24.387  -18.513 -6.265  1.00 23.44 ? 179 ILE A C   1 
ATOM   1408 O O   . ILE A 1 177 ? 24.166  -17.313 -6.266  1.00 24.84 ? 179 ILE A O   1 
ATOM   1409 C CB  . ILE A 1 177 ? 22.952  -20.207 -4.936  1.00 18.16 ? 179 ILE A CB  1 
ATOM   1410 C CG1 . ILE A 1 177 ? 21.543  -20.916 -4.889  1.00 19.18 ? 179 ILE A CG1 1 
ATOM   1411 C CG2 . ILE A 1 177 ? 23.013  -19.150 -3.815  1.00 13.56 ? 179 ILE A CG2 1 
ATOM   1412 C CD1 . ILE A 1 177 ? 21.366  -21.889 -3.931  1.00 18.09 ? 179 ILE A CD1 1 
ATOM   1413 N N   . GLY A 1 178 ? 25.593  -19.026 -6.225  1.00 23.96 ? 180 GLY A N   1 
ATOM   1414 C CA  . GLY A 1 178 ? 26.794  -18.238 -6.046  1.00 24.49 ? 180 GLY A CA  1 
ATOM   1415 C C   . GLY A 1 178 ? 27.003  -17.270 -7.199  1.00 25.48 ? 180 GLY A C   1 
ATOM   1416 O O   . GLY A 1 178 ? 27.341  -16.121 -6.954  1.00 25.63 ? 180 GLY A O   1 
ATOM   1417 N N   . ARG A 1 179 ? 26.809  -17.744 -8.470  1.00 26.74 ? 181 ARG A N   1 
ATOM   1418 C CA  . ARG A 1 179 ? 26.926  -16.919 -9.703  1.00 28.55 ? 181 ARG A CA  1 
ATOM   1419 C C   . ARG A 1 179 ? 25.950  -15.771 -9.700  1.00 27.37 ? 181 ARG A C   1 
ATOM   1420 O O   . ARG A 1 179 ? 26.350  -14.629 -9.888  1.00 27.96 ? 181 ARG A O   1 
ATOM   1421 C CB  . ARG A 1 179 ? 26.705  -17.736 -11.015 1.00 31.81 ? 181 ARG A CB  1 
ATOM   1422 C CG  . ARG A 1 179 ? 27.761  -18.765 -11.327 1.00 37.66 ? 181 ARG A CG  1 
ATOM   1423 C CD  . ARG A 1 179 ? 28.815  -18.260 -12.287 1.00 45.83 ? 181 ARG A CD  1 
ATOM   1424 N NE  . ARG A 1 179 ? 29.860  -19.279 -12.450 1.00 51.01 ? 181 ARG A NE  1 
ATOM   1425 C CZ  . ARG A 1 179 ? 31.104  -19.062 -12.862 1.00 54.04 ? 181 ARG A CZ  1 
ATOM   1426 N NH1 . ARG A 1 179 ? 31.506  -17.836 -13.178 1.00 53.63 ? 181 ARG A NH1 1 
ATOM   1427 N NH2 . ARG A 1 179 ? 31.955  -20.068 -12.964 1.00 55.61 ? 181 ARG A NH2 1 
ATOM   1428 N N   . VAL A 1 180 ? 24.687  -16.068 -9.480  1.00 25.59 ? 182 VAL A N   1 
ATOM   1429 C CA  . VAL A 1 180 ? 23.601  -15.083 -9.481  1.00 24.67 ? 182 VAL A CA  1 
ATOM   1430 C C   . VAL A 1 180 ? 23.776  -14.112 -8.313  1.00 25.18 ? 182 VAL A C   1 
ATOM   1431 O O   . VAL A 1 180 ? 23.613  -12.895 -8.481  1.00 26.16 ? 182 VAL A O   1 
ATOM   1432 C CB  . VAL A 1 180 ? 22.257  -15.801 -9.430  1.00 25.12 ? 182 VAL A CB  1 
ATOM   1433 C CG1 . VAL A 1 180 ? 21.097  -14.840 -9.257  1.00 25.87 ? 182 VAL A CG1 1 
ATOM   1434 C CG2 . VAL A 1 180 ? 22.056  -16.664 -10.701 1.00 27.01 ? 182 VAL A CG2 1 
ATOM   1435 N N   . TYR A 1 181 ? 24.104  -14.621 -7.158  1.00 23.17 ? 183 TYR A N   1 
ATOM   1436 C CA  . TYR A 1 181 ? 24.378  -13.777 -5.993  1.00 23.21 ? 183 TYR A CA  1 
ATOM   1437 C C   . TYR A 1 181 ? 25.536  -12.785 -6.219  1.00 24.64 ? 183 TYR A C   1 
ATOM   1438 O O   . TYR A 1 181 ? 25.405  -11.584 -5.909  1.00 23.66 ? 183 TYR A O   1 
ATOM   1439 C CB  . TYR A 1 181 ? 24.656  -14.649 -4.792  1.00 21.86 ? 183 TYR A CB  1 
ATOM   1440 C CG  . TYR A 1 181 ? 24.829  -13.953 -3.465  1.00 21.97 ? 183 TYR A CG  1 
ATOM   1441 C CD1 . TYR A 1 181 ? 24.041  -12.856 -3.110  1.00 23.05 ? 183 TYR A CD1 1 
ATOM   1442 C CD2 . TYR A 1 181 ? 25.725  -14.427 -2.531  1.00 22.57 ? 183 TYR A CD2 1 
ATOM   1443 C CE1 . TYR A 1 181 ? 24.190  -12.240 -1.883  1.00 22.13 ? 183 TYR A CE1 1 
ATOM   1444 C CE2 . TYR A 1 181 ? 25.892  -13.803 -1.318  1.00 21.96 ? 183 TYR A CE2 1 
ATOM   1445 C CZ  . TYR A 1 181 ? 25.111  -12.720 -0.989  1.00 21.75 ? 183 TYR A CZ  1 
ATOM   1446 O OH  . TYR A 1 181 ? 25.252  -12.161 0.253   1.00 21.26 ? 183 TYR A OH  1 
ATOM   1447 N N   . LYS A 1 182 ? 26.671  -13.263 -6.743  1.00 24.01 ? 184 LYS A N   1 
ATOM   1448 C CA  . LYS A 1 182 ? 27.811  -12.378 -7.001  1.00 25.88 ? 184 LYS A CA  1 
ATOM   1449 C C   . LYS A 1 182 ? 27.403  -11.297 -8.049  1.00 27.52 ? 184 LYS A C   1 
ATOM   1450 O O   . LYS A 1 182 ? 27.777  -10.135 -7.913  1.00 28.98 ? 184 LYS A O   1 
ATOM   1451 C CB  . LYS A 1 182 ? 28.998  -13.190 -7.501  1.00 26.25 ? 184 LYS A CB  1 
ATOM   1452 C CG  . LYS A 1 182 ? 30.199  -12.350 -7.818  1.00 31.72 ? 184 LYS A CG  1 
ATOM   1453 C CD  . LYS A 1 182 ? 31.208  -13.131 -8.599  1.00 34.21 ? 184 LYS A CD  1 
ATOM   1454 C CE  . LYS A 1 182 ? 32.517  -12.395 -8.653  1.00 37.83 ? 184 LYS A CE  1 
ATOM   1455 N NZ  . LYS A 1 182 ? 33.613  -13.266 -9.148  1.00 41.39 ? 184 LYS A NZ  1 
ATOM   1456 N N   . GLU A 1 183 ? 26.627  -11.702 -9.074  1.00 26.62 ? 185 GLU A N   1 
ATOM   1457 C CA  . GLU A 1 183 ? 26.057  -10.807 -10.103 1.00 26.51 ? 185 GLU A CA  1 
ATOM   1458 C C   . GLU A 1 183 ? 25.160  -9.689  -9.459  1.00 26.73 ? 185 GLU A C   1 
ATOM   1459 O O   . GLU A 1 183 ? 25.288  -8.478  -9.773  1.00 26.50 ? 185 GLU A O   1 
ATOM   1460 C CB  . GLU A 1 183 ? 25.228  -11.676 -11.069 1.00 27.70 ? 185 GLU A CB  1 
ATOM   1461 C CG  . GLU A 1 183 ? 24.707  -11.057 -12.347 1.00 34.59 ? 185 GLU A CG  1 
ATOM   1462 C CD  . GLU A 1 183 ? 23.532  -11.880 -12.842 1.00 39.73 ? 185 GLU A CD  1 
ATOM   1463 O OE1 . GLU A 1 183 ? 22.408  -11.333 -12.896 1.00 38.17 ? 185 GLU A OE1 1 
ATOM   1464 O OE2 . GLU A 1 183 ? 23.725  -13.086 -13.136 1.00 43.58 ? 185 GLU A OE2 1 
ATOM   1465 N N   . ARG A 1 184 ? 24.282  -10.101 -8.571  1.00 26.16 ? 186 ARG A N   1 
ATOM   1466 C CA  . ARG A 1 184 ? 23.352  -9.214  -7.912  1.00 27.67 ? 186 ARG A CA  1 
ATOM   1467 C C   . ARG A 1 184 ? 24.036  -8.308  -6.928  1.00 29.42 ? 186 ARG A C   1 
ATOM   1468 O O   . ARG A 1 184 ? 23.577  -7.187  -6.719  1.00 29.20 ? 186 ARG A O   1 
ATOM   1469 C CB  . ARG A 1 184 ? 22.239  -10.007 -7.219  1.00 28.58 ? 186 ARG A CB  1 
ATOM   1470 C CG  . ARG A 1 184 ? 21.267  -10.691 -8.205  1.00 30.50 ? 186 ARG A CG  1 
ATOM   1471 C CD  . ARG A 1 184 ? 20.257  -9.725  -8.790  1.00 29.83 ? 186 ARG A CD  1 
ATOM   1472 N NE  . ARG A 1 184 ? 19.300  -9.260  -7.791  1.00 26.51 ? 186 ARG A NE  1 
ATOM   1473 C CZ  . ARG A 1 184 ? 18.039  -9.662  -7.649  1.00 26.34 ? 186 ARG A CZ  1 
ATOM   1474 N NH1 . ARG A 1 184 ? 17.521  -10.566 -8.469  1.00 25.33 ? 186 ARG A NH1 1 
ATOM   1475 N NH2 . ARG A 1 184 ? 17.272  -9.140  -6.699  1.00 28.20 ? 186 ARG A NH2 1 
ATOM   1476 N N   . LEU A 1 185 ? 25.131  -8.768  -6.300  1.00 30.27 ? 187 LEU A N   1 
ATOM   1477 C CA  . LEU A 1 185 ? 25.989  -7.898  -5.527  1.00 31.61 ? 187 LEU A CA  1 
ATOM   1478 C C   . LEU A 1 185 ? 26.796  -6.902  -6.366  1.00 34.54 ? 187 LEU A C   1 
ATOM   1479 O O   . LEU A 1 185 ? 27.328  -5.966  -5.808  1.00 33.65 ? 187 LEU A O   1 
ATOM   1480 C CB  . LEU A 1 185 ? 26.946  -8.723  -4.651  1.00 31.21 ? 187 LEU A CB  1 
ATOM   1481 C CG  . LEU A 1 185 ? 26.279  -9.484  -3.463  1.00 30.74 ? 187 LEU A CG  1 
ATOM   1482 C CD1 . LEU A 1 185 ? 27.234  -10.380 -2.800  1.00 29.71 ? 187 LEU A CD1 1 
ATOM   1483 C CD2 . LEU A 1 185 ? 25.719  -8.544  -2.445  1.00 31.18 ? 187 LEU A CD2 1 
ATOM   1484 N N   . GLY A 1 186 ? 26.881  -7.102  -7.682  1.00 37.12 ? 188 GLY A N   1 
ATOM   1485 C CA  . GLY A 1 186 ? 27.756  -6.332  -8.545  1.00 38.56 ? 188 GLY A CA  1 
ATOM   1486 C C   . GLY A 1 186 ? 29.202  -6.378  -8.126  1.00 40.39 ? 188 GLY A C   1 
ATOM   1487 O O   . GLY A 1 186 ? 29.870  -5.347  -8.158  1.00 41.94 ? 188 GLY A O   1 
ATOM   1488 N N   . LEU A 1 187 ? 29.699  -7.547  -7.719  1.00 40.35 ? 189 LEU A N   1 
ATOM   1489 C CA  . LEU A 1 187 ? 31.099  -7.666  -7.400  1.00 40.77 ? 189 LEU A CA  1 
ATOM   1490 C C   . LEU A 1 187 ? 31.865  -7.740  -8.720  1.00 42.77 ? 189 LEU A C   1 
ATOM   1491 O O   . LEU A 1 187 ? 31.376  -8.373  -9.667  1.00 40.85 ? 189 LEU A O   1 
ATOM   1492 C CB  . LEU A 1 187 ? 31.398  -8.912  -6.541  1.00 39.05 ? 189 LEU A CB  1 
ATOM   1493 C CG  . LEU A 1 187 ? 30.844  -8.911  -5.132  1.00 36.79 ? 189 LEU A CG  1 
ATOM   1494 C CD1 . LEU A 1 187 ? 30.983  -10.295 -4.482  1.00 35.25 ? 189 LEU A CD1 1 
ATOM   1495 C CD2 . LEU A 1 187 ? 31.542  -7.976  -4.289  1.00 37.58 ? 189 LEU A CD2 1 
ATOM   1496 N N   . PRO A 1 188 ? 33.057  -7.077  -8.795  1.00 45.90 ? 190 PRO A N   1 
ATOM   1497 C CA  . PRO A 1 188 ? 33.969  -7.319  -9.927  1.00 48.15 ? 190 PRO A CA  1 
ATOM   1498 C C   . PRO A 1 188 ? 34.265  -8.811  -10.119 1.00 50.82 ? 190 PRO A C   1 
ATOM   1499 O O   . PRO A 1 188 ? 34.459  -9.500  -9.119  1.00 51.94 ? 190 PRO A O   1 
ATOM   1500 C CB  . PRO A 1 188 ? 35.254  -6.573  -9.522  1.00 48.96 ? 190 PRO A CB  1 
ATOM   1501 C CG  . PRO A 1 188 ? 34.857  -5.586  -8.487  1.00 49.00 ? 190 PRO A CG  1 
ATOM   1502 C CD  . PRO A 1 188 ? 33.598  -6.071  -7.853  1.00 46.44 ? 190 PRO A CD  1 
ATOM   1503 N N   . PRO A 1 189 ? 34.318  -9.333  -11.359 1.00 51.71 ? 191 PRO A N   1 
ATOM   1504 C CA  . PRO A 1 189 ? 34.597  -10.775 -11.548 1.00 52.30 ? 191 PRO A CA  1 
ATOM   1505 C C   . PRO A 1 189 ? 35.918  -11.267 -10.971 1.00 52.63 ? 191 PRO A C   1 
ATOM   1506 O O   . PRO A 1 189 ? 36.113  -12.480 -10.850 1.00 53.11 ? 191 PRO A O   1 
ATOM   1507 C CB  . PRO A 1 189 ? 34.538  -10.974 -13.061 1.00 53.24 ? 191 PRO A CB  1 
ATOM   1508 C CG  . PRO A 1 189 ? 34.558  -9.614  -13.664 1.00 53.43 ? 191 PRO A CG  1 
ATOM   1509 C CD  . PRO A 1 189 ? 34.146  -8.622  -12.638 1.00 51.88 ? 191 PRO A CD  1 
ATOM   1510 N N   . LYS A 1 190 ? 36.830  -10.352 -10.613 1.00 52.34 ? 192 LYS A N   1 
ATOM   1511 C CA  . LYS A 1 190 ? 38.076  -10.762 -9.965  1.00 51.36 ? 192 LYS A CA  1 
ATOM   1512 C C   . LYS A 1 190 ? 37.981  -10.834 -8.452  1.00 49.97 ? 192 LYS A C   1 
ATOM   1513 O O   . LYS A 1 190 ? 38.878  -11.391 -7.831  1.00 50.09 ? 192 LYS A O   1 
ATOM   1514 C CB  . LYS A 1 190 ? 39.225  -9.845  -10.419 1.00 54.02 ? 192 LYS A CB  1 
ATOM   1515 C CG  . LYS A 1 190 ? 40.561  -10.579 -10.593 1.00 58.24 ? 192 LYS A CG  1 
ATOM   1516 C CD  . LYS A 1 190 ? 40.595  -11.488 -11.831 1.00 62.15 ? 192 LYS A CD  1 
ATOM   1517 C CE  . LYS A 1 190 ? 41.665  -12.535 -11.766 1.00 65.50 ? 192 LYS A CE  1 
ATOM   1518 N NZ  . LYS A 1 190 ? 41.452  -13.510 -10.663 1.00 68.91 ? 192 LYS A NZ  1 
ATOM   1519 N N   . ILE A 1 191 ? 36.918  -10.268 -7.843  1.00 49.40 ? 193 ILE A N   1 
ATOM   1520 C CA  . ILE A 1 191 ? 36.595  -10.542 -6.453  1.00 49.04 ? 193 ILE A CA  1 
ATOM   1521 C C   . ILE A 1 191 ? 35.949  -11.909 -6.467  1.00 49.41 ? 193 ILE A C   1 
ATOM   1522 O O   . ILE A 1 191 ? 34.844  -12.040 -6.971  1.00 51.05 ? 193 ILE A O   1 
ATOM   1523 C CB  . ILE A 1 191 ? 35.656  -9.454  -5.869  1.00 49.01 ? 193 ILE A CB  1 
ATOM   1524 C CG1 . ILE A 1 191 ? 36.330  -8.056  -5.884  1.00 48.88 ? 193 ILE A CG1 1 
ATOM   1525 C CG2 . ILE A 1 191 ? 35.200  -9.835  -4.453  1.00 50.13 ? 193 ILE A CG2 1 
ATOM   1526 C CD1 . ILE A 1 191 ? 37.759  -7.963  -5.211  1.00 49.30 ? 193 ILE A CD1 1 
ATOM   1527 N N   . VAL A 1 192 ? 36.625  -12.919 -5.946  1.00 47.86 ? 194 VAL A N   1 
ATOM   1528 C CA  . VAL A 1 192 ? 36.108  -14.286 -5.954  1.00 47.33 ? 194 VAL A CA  1 
ATOM   1529 C C   . VAL A 1 192 ? 35.426  -14.586 -4.631  1.00 45.93 ? 194 VAL A C   1 
ATOM   1530 O O   . VAL A 1 192 ? 36.007  -14.329 -3.573  1.00 47.55 ? 194 VAL A O   1 
ATOM   1531 C CB  . VAL A 1 192 ? 37.199  -15.335 -6.268  1.00 47.92 ? 194 VAL A CB  1 
ATOM   1532 C CG1 . VAL A 1 192 ? 37.956  -14.976 -7.545  1.00 48.03 ? 194 VAL A CG1 1 
ATOM   1533 C CG2 . VAL A 1 192 ? 38.155  -15.522 -5.103  1.00 48.02 ? 194 VAL A CG2 1 
ATOM   1534 N N   . ILE A 1 193 ? 34.185  -15.126 -4.678  1.00 41.82 ? 195 ILE A N   1 
ATOM   1535 C CA  . ILE A 1 193 ? 33.493  -15.530 -3.466  1.00 37.54 ? 195 ILE A CA  1 
ATOM   1536 C C   . ILE A 1 193 ? 33.615  -17.023 -3.300  1.00 33.22 ? 195 ILE A C   1 
ATOM   1537 O O   . ILE A 1 193 ? 33.767  -17.746 -4.290  1.00 32.56 ? 195 ILE A O   1 
ATOM   1538 C CB  . ILE A 1 193 ? 32.046  -15.009 -3.353  1.00 37.82 ? 195 ILE A CB  1 
ATOM   1539 C CG1 . ILE A 1 193 ? 31.121  -15.614 -4.404  1.00 38.38 ? 195 ILE A CG1 1 
ATOM   1540 C CG2 . ILE A 1 193 ? 32.039  -13.510 -3.432  1.00 38.41 ? 195 ILE A CG2 1 
ATOM   1541 C CD1 . ILE A 1 193 ? 29.645  -15.365 -4.188  1.00 38.86 ? 195 ILE A CD1 1 
ATOM   1542 N N   . GLY A 1 194 ? 33.569  -17.459 -2.036  1.00 29.07 ? 196 GLY A N   1 
ATOM   1543 C CA  . GLY A 1 194 ? 33.843  -18.840 -1.667  1.00 26.36 ? 196 GLY A CA  1 
ATOM   1544 C C   . GLY A 1 194 ? 32.656  -19.468 -0.955  1.00 23.74 ? 196 GLY A C   1 
ATOM   1545 O O   . GLY A 1 194 ? 31.971  -18.802 -0.167  1.00 23.23 ? 196 GLY A O   1 
ATOM   1546 N N   . TYR A 1 195 ? 32.397  -20.772 -1.233  1.00 22.95 ? 197 TYR A N   1 
ATOM   1547 C CA  . TYR A 1 195 ? 31.320  -21.535 -0.603  1.00 22.99 ? 197 TYR A CA  1 
ATOM   1548 C C   . TYR A 1 195 ? 31.995  -22.471 0.357   1.00 25.88 ? 197 TYR A C   1 
ATOM   1549 O O   . TYR A 1 195 ? 32.884  -23.219 -0.076  1.00 26.86 ? 197 TYR A O   1 
ATOM   1550 C CB  . TYR A 1 195 ? 30.487  -22.315 -1.621  1.00 23.18 ? 197 TYR A CB  1 
ATOM   1551 C CG  . TYR A 1 195 ? 29.355  -23.100 -0.970  1.00 22.93 ? 197 TYR A CG  1 
ATOM   1552 C CD1 . TYR A 1 195 ? 28.094  -22.540 -0.810  1.00 23.95 ? 197 TYR A CD1 1 
ATOM   1553 C CD2 . TYR A 1 195 ? 29.546  -24.408 -0.522  1.00 23.11 ? 197 TYR A CD2 1 
ATOM   1554 C CE1 . TYR A 1 195 ? 27.054  -23.250 -0.216  1.00 23.21 ? 197 TYR A CE1 1 
ATOM   1555 C CE2 . TYR A 1 195 ? 28.510  -25.126 0.085   1.00 22.50 ? 197 TYR A CE2 1 
ATOM   1556 C CZ  . TYR A 1 195 ? 27.269  -24.542 0.243   1.00 24.34 ? 197 TYR A CZ  1 
ATOM   1557 O OH  . TYR A 1 195 ? 26.239  -25.255 0.852   1.00 25.94 ? 197 TYR A OH  1 
ATOM   1558 N N   . GLN A 1 196 ? 31.622  -22.393 1.659   1.00 25.68 ? 198 GLN A N   1 
ATOM   1559 C CA  . GLN A 1 196 ? 32.149  -23.153 2.765   1.00 25.97 ? 198 GLN A CA  1 
ATOM   1560 C C   . GLN A 1 196 ? 31.111  -24.083 3.378   1.00 23.68 ? 198 GLN A C   1 
ATOM   1561 O O   . GLN A 1 196 ? 30.054  -23.619 3.807   1.00 18.97 ? 198 GLN A O   1 
ATOM   1562 C CB  . GLN A 1 196 ? 32.566  -22.203 3.894   1.00 27.61 ? 198 GLN A CB  1 
ATOM   1563 C CG  . GLN A 1 196 ? 33.799  -21.375 3.596   1.00 33.93 ? 198 GLN A CG  1 
ATOM   1564 C CD  . GLN A 1 196 ? 33.854  -20.091 4.398   1.00 42.45 ? 198 GLN A CD  1 
ATOM   1565 O OE1 . GLN A 1 196 ? 32.884  -19.666 5.058   1.00 43.04 ? 198 GLN A OE1 1 
ATOM   1566 N NE2 . GLN A 1 196 ? 35.022  -19.441 4.370   1.00 45.37 ? 198 GLN A NE2 1 
ATOM   1567 N N   . SER A 1 197 ? 31.432  -25.392 3.412   1.00 23.97 ? 199 SER A N   1 
ATOM   1568 C CA  . SER A 1 197 ? 30.637  -26.383 4.143   1.00 25.83 ? 199 SER A CA  1 
ATOM   1569 C C   . SER A 1 197 ? 30.588  -25.998 5.613   1.00 24.17 ? 199 SER A C   1 
ATOM   1570 O O   . SER A 1 197 ? 31.641  -25.625 6.219   1.00 26.87 ? 199 SER A O   1 
ATOM   1571 C CB  . SER A 1 197 ? 31.278  -27.758 3.989   1.00 30.04 ? 199 SER A CB  1 
ATOM   1572 O OG  . SER A 1 197 ? 30.757  -28.730 4.870   1.00 36.16 ? 199 SER A OG  1 
ATOM   1573 N N   . HIS A 1 198 ? 29.434  -26.066 6.189   1.00 20.51 ? 200 HIS A N   1 
ATOM   1574 C CA  . HIS A 1 198 ? 29.284  -25.779 7.616   1.00 23.81 ? 200 HIS A CA  1 
ATOM   1575 C C   . HIS A 1 198 ? 30.167  -26.724 8.451   1.00 29.18 ? 200 HIS A C   1 
ATOM   1576 O O   . HIS A 1 198 ? 30.724  -26.290 9.467   1.00 31.48 ? 200 HIS A O   1 
ATOM   1577 C CB  . HIS A 1 198 ? 27.819  -25.900 8.054   1.00 23.04 ? 200 HIS A CB  1 
ATOM   1578 C CG  . HIS A 1 198 ? 26.960  -24.741 7.614   1.00 23.26 ? 200 HIS A CG  1 
ATOM   1579 N ND1 . HIS A 1 198 ? 25.666  -24.902 7.179   1.00 24.45 ? 200 HIS A ND1 1 
ATOM   1580 C CD2 . HIS A 1 198 ? 27.275  -23.434 7.527   1.00 22.03 ? 200 HIS A CD2 1 
ATOM   1581 C CE1 . HIS A 1 198 ? 25.242  -23.685 6.858   1.00 23.68 ? 200 HIS A CE1 1 
ATOM   1582 N NE2 . HIS A 1 198 ? 26.161  -22.778 7.053   1.00 23.12 ? 200 HIS A NE2 1 
ATOM   1583 N N   . ALA A 1 199 ? 30.301  -27.983 7.991   1.00 31.10 ? 201 ALA A N   1 
ATOM   1584 C CA  . ALA A 1 199 ? 31.138  -28.988 8.648   1.00 34.78 ? 201 ALA A CA  1 
ATOM   1585 C C   . ALA A 1 199 ? 32.637  -28.582 8.714   1.00 37.17 ? 201 ALA A C   1 
ATOM   1586 O O   . ALA A 1 199 ? 33.301  -28.897 9.680   1.00 36.95 ? 201 ALA A O   1 
ATOM   1587 C CB  . ALA A 1 199 ? 30.990  -30.301 7.934   1.00 35.29 ? 201 ALA A CB  1 
ATOM   1588 N N   . ASP A 1 200 ? 33.152  -27.886 7.689   1.00 38.31 ? 202 ASP A N   1 
ATOM   1589 C CA  . ASP A 1 200 ? 34.498  -27.366 7.703   1.00 39.25 ? 202 ASP A CA  1 
ATOM   1590 C C   . ASP A 1 200 ? 34.583  -26.112 8.578   1.00 41.25 ? 202 ASP A C   1 
ATOM   1591 O O   . ASP A 1 200 ? 35.524  -25.990 9.386   1.00 40.29 ? 202 ASP A O   1 
ATOM   1592 C CB  . ASP A 1 200 ? 34.990  -27.078 6.260   1.00 39.76 ? 202 ASP A CB  1 
ATOM   1593 C CG  . ASP A 1 200 ? 35.004  -28.312 5.368   1.00 42.39 ? 202 ASP A CG  1 
ATOM   1594 O OD1 . ASP A 1 200 ? 34.982  -29.436 5.908   1.00 44.08 ? 202 ASP A OD1 1 
ATOM   1595 O OD2 . ASP A 1 200 ? 35.048  -28.154 4.122   1.00 42.10 ? 202 ASP A OD2 1 
ATOM   1596 N N   . THR A 1 201 ? 33.612  -25.181 8.426   1.00 41.78 ? 203 THR A N   1 
ATOM   1597 C CA  . THR A 1 201 ? 33.565  -23.946 9.222   1.00 42.69 ? 203 THR A CA  1 
ATOM   1598 C C   . THR A 1 201 ? 33.445  -24.207 10.714  1.00 44.32 ? 203 THR A C   1 
ATOM   1599 O O   . THR A 1 201 ? 33.924  -23.395 11.507  1.00 44.06 ? 203 THR A O   1 
ATOM   1600 C CB  . THR A 1 201 ? 32.421  -23.057 8.758   1.00 44.58 ? 203 THR A CB  1 
ATOM   1601 O OG1 . THR A 1 201 ? 32.557  -22.873 7.348   1.00 45.37 ? 203 THR A OG1 1 
ATOM   1602 C CG2 . THR A 1 201 ? 32.427  -21.694 9.441   1.00 46.10 ? 203 THR A CG2 1 
ATOM   1603 N N   . ALA A 1 202 ? 32.796  -25.317 11.109  1.00 45.31 ? 204 ALA A N   1 
ATOM   1604 C CA  . ALA A 1 202 ? 32.732  -25.700 12.519  1.00 46.78 ? 204 ALA A CA  1 
ATOM   1605 C C   . ALA A 1 202 ? 34.081  -26.140 13.049  1.00 48.83 ? 204 ALA A C   1 
ATOM   1606 O O   . ALA A 1 202 ? 34.342  -25.936 14.224  1.00 50.41 ? 204 ALA A O   1 
ATOM   1607 C CB  . ALA A 1 202 ? 31.715  -26.795 12.715  1.00 47.00 ? 204 ALA A CB  1 
ATOM   1608 N N   . THR A 1 203 ? 34.948  -26.728 12.206  1.00 49.12 ? 205 THR A N   1 
ATOM   1609 C CA  . THR A 1 203 ? 36.258  -27.172 12.657  1.00 49.15 ? 205 THR A CA  1 
ATOM   1610 C C   . THR A 1 203 ? 37.194  -26.008 12.543  1.00 50.74 ? 205 THR A C   1 
ATOM   1611 O O   . THR A 1 203 ? 37.284  -25.389 11.486  1.00 50.80 ? 205 THR A O   1 
ATOM   1612 C CB  . THR A 1 203 ? 36.773  -28.446 11.898  1.00 49.50 ? 205 THR A CB  1 
ATOM   1613 O OG1 . THR A 1 203 ? 37.415  -28.129 10.665  1.00 49.73 ? 205 THR A OG1 1 
ATOM   1614 C CG2 . THR A 1 203 ? 35.703  -29.463 11.671  1.00 49.17 ? 205 THR A CG2 1 
ATOM   1615 N N   . LYS A 1 204 ? 37.900  -25.698 13.632  1.00 51.34 ? 206 LYS A N   1 
ATOM   1616 C CA  . LYS A 1 204 ? 38.946  -24.691 13.570  1.00 51.94 ? 206 LYS A CA  1 
ATOM   1617 C C   . LYS A 1 204 ? 40.227  -25.459 13.262  1.00 53.30 ? 206 LYS A C   1 
ATOM   1618 O O   . LYS A 1 204 ? 40.679  -26.284 14.060  1.00 51.99 ? 206 LYS A O   1 
ATOM   1619 C CB  . LYS A 1 204 ? 38.985  -23.872 14.864  1.00 52.78 ? 206 LYS A CB  1 
ATOM   1620 C CG  . LYS A 1 204 ? 37.917  -22.783 14.956  1.00 56.40 ? 206 LYS A CG  1 
ATOM   1621 C CD  . LYS A 1 204 ? 36.472  -23.230 14.816  1.00 58.70 ? 206 LYS A CD  1 
ATOM   1622 C CE  . LYS A 1 204 ? 35.652  -22.097 14.240  1.00 65.64 ? 206 LYS A CE  1 
ATOM   1623 N NZ  . LYS A 1 204 ? 34.170  -22.307 14.355  1.00 70.66 ? 206 LYS A NZ  1 
ATOM   1624 N N   . SER A 1 205 ? 40.789  -25.201 12.072  1.00 55.41 ? 207 SER A N   1 
ATOM   1625 C CA  . SER A 1 205 ? 41.957  -25.924 11.522  1.00 57.36 ? 207 SER A CA  1 
ATOM   1626 C C   . SER A 1 205 ? 43.160  -25.003 11.263  1.00 57.47 ? 207 SER A C   1 
ATOM   1627 O O   . SER A 1 205 ? 44.116  -25.437 10.613  1.00 57.53 ? 207 SER A O   1 
ATOM   1628 C CB  . SER A 1 205 ? 41.568  -26.607 10.206  1.00 60.43 ? 207 SER A CB  1 
ATOM   1629 O OG  . SER A 1 205 ? 40.698  -27.698 10.439  1.00 65.26 ? 207 SER A OG  1 
ATOM   1630 N N   . GLY A 1 206 ? 43.122  -23.772 11.771  1.00 57.17 ? 208 GLY A N   1 
ATOM   1631 C CA  . GLY A 1 206 ? 44.225  -22.842 11.598  1.00 57.81 ? 208 GLY A CA  1 
ATOM   1632 C C   . GLY A 1 206 ? 43.753  -21.583 10.916  1.00 58.25 ? 208 GLY A C   1 
ATOM   1633 O O   . GLY A 1 206 ? 42.727  -21.005 11.317  1.00 57.12 ? 208 GLY A O   1 
ATOM   1634 N N   . SER A 1 207 ? 44.514  -21.193 9.869   1.00 59.30 ? 209 SER A N   1 
ATOM   1635 C CA  . SER A 1 207 ? 44.296  -19.989 9.066   1.00 60.60 ? 209 SER A CA  1 
ATOM   1636 C C   . SER A 1 207 ? 43.306  -20.300 7.898   1.00 62.16 ? 209 SER A C   1 
ATOM   1637 O O   . SER A 1 207 ? 43.583  -21.139 7.016   1.00 63.13 ? 209 SER A O   1 
ATOM   1638 C CB  . SER A 1 207 ? 45.627  -19.478 8.514   1.00 61.23 ? 209 SER A CB  1 
ATOM   1639 O OG  . SER A 1 207 ? 45.587  -18.116 8.132   1.00 62.91 ? 209 SER A OG  1 
ATOM   1640 N N   . THR A 1 208 ? 42.143  -19.610 7.907   1.00 61.31 ? 210 THR A N   1 
ATOM   1641 C CA  . THR A 1 208 ? 41.071  -19.765 6.919   1.00 61.20 ? 210 THR A CA  1 
ATOM   1642 C C   . THR A 1 208 ? 40.393  -21.168 7.034   1.00 59.48 ? 210 THR A C   1 
ATOM   1643 O O   . THR A 1 208 ? 40.861  -22.075 7.739   1.00 59.23 ? 210 THR A O   1 
ATOM   1644 C CB  . THR A 1 208 ? 41.577  -19.396 5.471   1.00 63.42 ? 210 THR A CB  1 
ATOM   1645 O OG1 . THR A 1 208 ? 42.292  -18.156 5.508   1.00 64.10 ? 210 THR A OG1 1 
ATOM   1646 C CG2 . THR A 1 208 ? 40.452  -19.237 4.480   1.00 64.02 ? 210 THR A CG2 1 
ATOM   1647 N N   . THR A 1 209 ? 39.259  -21.294 6.346   1.00 57.86 ? 211 THR A N   1 
ATOM   1648 C CA  . THR A 1 209 ? 38.509  -22.530 6.140   1.00 56.24 ? 211 THR A CA  1 
ATOM   1649 C C   . THR A 1 209 ? 38.593  -22.922 4.632   1.00 53.93 ? 211 THR A C   1 
ATOM   1650 O O   . THR A 1 209 ? 38.808  -22.069 3.771   1.00 54.04 ? 211 THR A O   1 
ATOM   1651 C CB  . THR A 1 209 ? 37.060  -22.290 6.608   1.00 57.94 ? 211 THR A CB  1 
ATOM   1652 O OG1 . THR A 1 209 ? 37.098  -21.951 7.994   1.00 59.47 ? 211 THR A OG1 1 
ATOM   1653 C CG2 . THR A 1 209 ? 36.134  -23.497 6.356   1.00 58.18 ? 211 THR A CG2 1 
ATOM   1654 N N   . LYS A 1 210 ? 38.438  -24.209 4.333   1.00 51.79 ? 212 LYS A N   1 
ATOM   1655 C CA  . LYS A 1 210 ? 38.410  -24.693 2.959   1.00 50.71 ? 212 LYS A CA  1 
ATOM   1656 C C   . LYS A 1 210 ? 37.145  -24.151 2.226   1.00 47.57 ? 212 LYS A C   1 
ATOM   1657 O O   . LYS A 1 210 ? 36.080  -24.054 2.820   1.00 47.05 ? 212 LYS A O   1 
ATOM   1658 C CB  . LYS A 1 210 ? 38.396  -26.234 2.958   1.00 54.32 ? 212 LYS A CB  1 
ATOM   1659 C CG  . LYS A 1 210 ? 38.687  -26.888 1.602   1.00 59.45 ? 212 LYS A CG  1 
ATOM   1660 C CD  . LYS A 1 210 ? 37.944  -28.193 1.432   1.00 62.75 ? 212 LYS A CD  1 
ATOM   1661 C CE  . LYS A 1 210 ? 37.927  -28.657 -0.001  1.00 66.17 ? 212 LYS A CE  1 
ATOM   1662 N NZ  . LYS A 1 210 ? 36.953  -29.774 -0.195  1.00 68.15 ? 212 LYS A NZ  1 
ATOM   1663 N N   . ASN A 1 211 ? 37.289  -23.784 0.959   1.00 44.61 ? 213 ASN A N   1 
ATOM   1664 C CA  . ASN A 1 211 ? 36.155  -23.573 0.066   1.00 41.94 ? 213 ASN A CA  1 
ATOM   1665 C C   . ASN A 1 211 ? 35.879  -24.820 -0.765  1.00 41.26 ? 213 ASN A C   1 
ATOM   1666 O O   . ASN A 1 211 ? 36.736  -25.245 -1.556  1.00 42.19 ? 213 ASN A O   1 
ATOM   1667 C CB  . ASN A 1 211 ? 36.440  -22.408 -0.848  1.00 41.10 ? 213 ASN A CB  1 
ATOM   1668 C CG  . ASN A 1 211 ? 36.532  -21.086 -0.131  1.00 41.19 ? 213 ASN A CG  1 
ATOM   1669 O OD1 . ASN A 1 211 ? 35.834  -20.824 0.864   1.00 41.46 ? 213 ASN A OD1 1 
ATOM   1670 N ND2 . ASN A 1 211 ? 37.337  -20.199 -0.606  1.00 40.01 ? 213 ASN A ND2 1 
ATOM   1671 N N   . ARG A 1 212 ? 34.706  -25.431 -0.585  1.00 39.37 ? 214 ARG A N   1 
ATOM   1672 C CA  . ARG A 1 212 ? 34.228  -26.438 -1.537  1.00 39.80 ? 214 ARG A CA  1 
ATOM   1673 C C   . ARG A 1 212 ? 34.117  -25.881 -2.992  1.00 38.86 ? 214 ARG A C   1 
ATOM   1674 O O   . ARG A 1 212 ? 34.541  -26.561 -3.922  1.00 38.99 ? 214 ARG A O   1 
ATOM   1675 C CB  . ARG A 1 212 ? 32.860  -27.044 -1.100  1.00 42.56 ? 214 ARG A CB  1 
ATOM   1676 C CG  . ARG A 1 212 ? 32.728  -28.545 -1.361  1.00 48.10 ? 214 ARG A CG  1 
ATOM   1677 C CD  . ARG A 1 212 ? 33.190  -29.342 -0.162  1.00 51.87 ? 214 ARG A CD  1 
ATOM   1678 N NE  . ARG A 1 212 ? 32.083  -29.897 0.611   1.00 55.59 ? 214 ARG A NE  1 
ATOM   1679 C CZ  . ARG A 1 212 ? 32.196  -30.421 1.826   1.00 58.83 ? 214 ARG A CZ  1 
ATOM   1680 N NH1 . ARG A 1 212 ? 33.379  -30.470 2.433   1.00 60.92 ? 214 ARG A NH1 1 
ATOM   1681 N NH2 . ARG A 1 212 ? 31.131  -30.898 2.446   1.00 59.36 ? 214 ARG A NH2 1 
ATOM   1682 N N   . PHE A 1 213 ? 33.554  -24.654 -3.183  1.00 38.23 ? 215 PHE A N   1 
ATOM   1683 C CA  . PHE A 1 213 ? 33.404  -24.011 -4.507  1.00 38.19 ? 215 PHE A CA  1 
ATOM   1684 C C   . PHE A 1 213 ? 33.815  -22.522 -4.430  1.00 38.01 ? 215 PHE A C   1 
ATOM   1685 O O   . PHE A 1 213 ? 33.864  -21.941 -3.352  1.00 37.21 ? 215 PHE A O   1 
ATOM   1686 C CB  . PHE A 1 213 ? 31.948  -24.139 -5.035  1.00 37.31 ? 215 PHE A CB  1 
ATOM   1687 C CG  . PHE A 1 213 ? 31.339  -25.510 -4.841  1.00 37.59 ? 215 PHE A CG  1 
ATOM   1688 C CD1 . PHE A 1 213 ? 31.736  -26.583 -5.628  1.00 39.43 ? 215 PHE A CD1 1 
ATOM   1689 C CD2 . PHE A 1 213 ? 30.438  -25.750 -3.814  1.00 37.99 ? 215 PHE A CD2 1 
ATOM   1690 C CE1 . PHE A 1 213 ? 31.192  -27.854 -5.425  1.00 39.88 ? 215 PHE A CE1 1 
ATOM   1691 C CE2 . PHE A 1 213 ? 29.880  -27.017 -3.624  1.00 38.65 ? 215 PHE A CE2 1 
ATOM   1692 C CZ  . PHE A 1 213 ? 30.258  -28.058 -4.426  1.00 39.23 ? 215 PHE A CZ  1 
ATOM   1693 N N   . VAL A 1 214 ? 34.124  -21.940 -5.589  1.00 38.43 ? 216 VAL A N   1 
ATOM   1694 C CA  . VAL A 1 214 ? 34.551  -20.539 -5.757  1.00 39.22 ? 216 VAL A CA  1 
ATOM   1695 C C   . VAL A 1 214 ? 33.851  -20.001 -7.062  1.00 37.81 ? 216 VAL A C   1 
ATOM   1696 O O   . VAL A 1 214 ? 33.756  -20.733 -8.039  1.00 38.34 ? 216 VAL A O   1 
ATOM   1697 C CB  . VAL A 1 214 ? 36.116  -20.442 -5.871  1.00 41.59 ? 216 VAL A CB  1 
ATOM   1698 C CG1 . VAL A 1 214 ? 36.588  -19.025 -6.192  1.00 42.78 ? 216 VAL A CG1 1 
ATOM   1699 C CG2 . VAL A 1 214 ? 36.808  -20.946 -4.607  1.00 42.38 ? 216 VAL A CG2 1 
ATOM   1700 N N   . VAL A 1 215 ? 33.364  -18.758 -7.062  1.00 36.31 ? 217 VAL A N   1 
ATOM   1701 C CA  . VAL A 1 215 ? 32.873  -18.093 -8.275  1.00 35.57 ? 217 VAL A CA  1 
ATOM   1702 C C   . VAL A 1 215 ? 33.358  -16.637 -8.303  1.00 36.17 ? 217 VAL A C   1 
ATOM   1703 O O   . VAL A 1 215 ? 33.265  -16.020 -9.379  1.00 37.74 ? 217 VAL A O   1 
ATOM   1704 C CB  . VAL A 1 215 ? 31.329  -18.130 -8.455  1.00 35.09 ? 217 VAL A CB  1 
ATOM   1705 C CG1 . VAL A 1 215 ? 30.788  -19.542 -8.412  1.00 35.53 ? 217 VAL A CG1 1 
ATOM   1706 C CG2 . VAL A 1 215 ? 30.626  -17.291 -7.427  1.00 34.97 ? 217 VAL A CG2 1 
ATOM   1707 O OXT . VAL A 1 215 ? 33.799  -16.099 -7.260  1.00 30.43 ? 217 VAL A OXT 1 
ATOM   1708 N N   . ALA B 1 9   ? -1.694  -13.279 8.838   1.00 55.73 ? 11  ALA B N   1 
ATOM   1709 C CA  . ALA B 1 9   ? -2.803  -14.080 9.350   1.00 55.98 ? 11  ALA B CA  1 
ATOM   1710 C C   . ALA B 1 9   ? -2.386  -14.864 10.613  1.00 55.58 ? 11  ALA B C   1 
ATOM   1711 O O   . ALA B 1 9   ? -1.266  -15.365 10.661  1.00 56.60 ? 11  ALA B O   1 
ATOM   1712 C CB  . ALA B 1 9   ? -3.275  -15.046 8.272   1.00 55.92 ? 11  ALA B CB  1 
ATOM   1713 N N   . ARG B 1 10  ? -3.292  -14.984 11.611  1.00 53.26 ? 12  ARG B N   1 
ATOM   1714 C CA  . ARG B 1 10  ? -2.962  -15.560 12.921  1.00 51.47 ? 12  ARG B CA  1 
ATOM   1715 C C   . ARG B 1 10  ? -3.013  -17.113 12.919  1.00 47.88 ? 12  ARG B C   1 
ATOM   1716 O O   . ARG B 1 10  ? -3.951  -17.706 12.397  1.00 47.50 ? 12  ARG B O   1 
ATOM   1717 C CB  . ARG B 1 10  ? -3.902  -15.027 14.031  1.00 53.59 ? 12  ARG B CB  1 
ATOM   1718 C CG  . ARG B 1 10  ? -4.188  -13.518 13.948  1.00 58.77 ? 12  ARG B CG  1 
ATOM   1719 C CD  . ARG B 1 10  ? -4.344  -12.868 15.302  1.00 63.38 ? 12  ARG B CD  1 
ATOM   1720 N NE  . ARG B 1 10  ? -4.617  -11.437 15.170  1.00 68.88 ? 12  ARG B NE  1 
ATOM   1721 C CZ  . ARG B 1 10  ? -4.545  -10.558 16.169  1.00 72.89 ? 12  ARG B CZ  1 
ATOM   1722 N NH1 . ARG B 1 10  ? -4.205  -10.958 17.396  1.00 74.00 ? 12  ARG B NH1 1 
ATOM   1723 N NH2 . ARG B 1 10  ? -4.809  -9.267  15.950  1.00 71.62 ? 12  ARG B NH2 1 
ATOM   1724 N N   . ILE B 1 11  ? -2.009  -17.740 13.521  1.00 44.38 ? 13  ILE B N   1 
ATOM   1725 C CA  . ILE B 1 11  ? -1.827  -19.197 13.503  1.00 42.10 ? 13  ILE B CA  1 
ATOM   1726 C C   . ILE B 1 11  ? -2.454  -19.852 14.771  1.00 41.42 ? 13  ILE B C   1 
ATOM   1727 O O   . ILE B 1 11  ? -1.876  -19.849 15.864  1.00 40.39 ? 13  ILE B O   1 
ATOM   1728 C CB  . ILE B 1 11  ? -0.323  -19.550 13.369  1.00 40.80 ? 13  ILE B CB  1 
ATOM   1729 C CG1 . ILE B 1 11  ? 0.342   -18.725 12.221  1.00 41.32 ? 13  ILE B CG1 1 
ATOM   1730 C CG2 . ILE B 1 11  ? -0.159  -21.049 13.192  1.00 39.81 ? 13  ILE B CG2 1 
ATOM   1731 C CD1 . ILE B 1 11  ? 1.740   -19.178 11.754  1.00 42.23 ? 13  ILE B CD1 1 
ATOM   1732 N N   . ILE B 1 12  ? -3.630  -20.431 14.594  1.00 41.02 ? 14  ILE B N   1 
ATOM   1733 C CA  . ILE B 1 12  ? -4.397  -20.985 15.693  1.00 40.01 ? 14  ILE B CA  1 
ATOM   1734 C C   . ILE B 1 12  ? -4.571  -22.454 15.457  1.00 40.11 ? 14  ILE B C   1 
ATOM   1735 O O   . ILE B 1 12  ? -5.068  -22.857 14.392  1.00 41.68 ? 14  ILE B O   1 
ATOM   1736 C CB  . ILE B 1 12  ? -5.777  -20.307 15.790  1.00 39.67 ? 14  ILE B CB  1 
ATOM   1737 C CG1 . ILE B 1 12  ? -5.654  -18.749 15.880  1.00 38.64 ? 14  ILE B CG1 1 
ATOM   1738 C CG2 . ILE B 1 12  ? -6.576  -20.944 16.961  1.00 39.79 ? 14  ILE B CG2 1 
ATOM   1739 C CD1 . ILE B 1 12  ? -6.879  -18.107 15.807  1.00 39.39 ? 14  ILE B CD1 1 
ATOM   1740 N N   . TYR B 1 13  ? -4.177  -23.279 16.449  1.00 38.25 ? 15  TYR B N   1 
ATOM   1741 C CA  . TYR B 1 13  ? -4.397  -24.721 16.406  1.00 37.58 ? 15  TYR B CA  1 
ATOM   1742 C C   . TYR B 1 13  ? -5.360  -25.099 17.520  1.00 38.71 ? 15  TYR B C   1 
ATOM   1743 O O   . TYR B 1 13  ? -5.084  -24.748 18.665  1.00 39.69 ? 15  TYR B O   1 
ATOM   1744 C CB  . TYR B 1 13  ? -3.079  -25.432 16.667  1.00 36.21 ? 15  TYR B CB  1 
ATOM   1745 C CG  . TYR B 1 13  ? -2.052  -25.156 15.604  1.00 34.25 ? 15  TYR B CG  1 
ATOM   1746 C CD1 . TYR B 1 13  ? -2.152  -25.736 14.347  1.00 34.65 ? 15  TYR B CD1 1 
ATOM   1747 C CD2 . TYR B 1 13  ? -0.973  -24.327 15.851  1.00 34.68 ? 15  TYR B CD2 1 
ATOM   1748 C CE1 . TYR B 1 13  ? -1.200  -25.508 13.366  1.00 34.05 ? 15  TYR B CE1 1 
ATOM   1749 C CE2 . TYR B 1 13  ? -0.010  -24.094 14.878  1.00 34.42 ? 15  TYR B CE2 1 
ATOM   1750 C CZ  . TYR B 1 13  ? -0.138  -24.681 13.632  1.00 34.85 ? 15  TYR B CZ  1 
ATOM   1751 O OH  . TYR B 1 13  ? 0.785   -24.446 12.656  1.00 35.90 ? 15  TYR B OH  1 
ATOM   1752 N N   . ASP B 1 14  ? -6.480  -25.776 17.210  1.00 37.48 ? 16  ASP B N   1 
ATOM   1753 C CA  . ASP B 1 14  ? -7.280  -26.420 18.254  1.00 36.77 ? 16  ASP B CA  1 
ATOM   1754 C C   . ASP B 1 14  ? -6.590  -27.668 18.866  1.00 36.21 ? 16  ASP B C   1 
ATOM   1755 O O   . ASP B 1 14  ? -5.571  -28.188 18.354  1.00 36.05 ? 16  ASP B O   1 
ATOM   1756 C CB  . ASP B 1 14  ? -8.727  -26.728 17.772  1.00 36.77 ? 16  ASP B CB  1 
ATOM   1757 C CG  . ASP B 1 14  ? -8.911  -27.696 16.629  1.00 37.64 ? 16  ASP B CG  1 
ATOM   1758 O OD1 . ASP B 1 14  ? -8.076  -28.587 16.466  1.00 38.59 ? 16  ASP B OD1 1 
ATOM   1759 O OD2 . ASP B 1 14  ? -9.889  -27.561 15.913  1.00 37.45 ? 16  ASP B OD2 1 
ATOM   1760 N N   . ARG B 1 15  ? -7.166  -28.138 19.975  1.00 34.89 ? 17  ARG B N   1 
ATOM   1761 C CA  . ARG B 1 15  ? -6.622  -29.252 20.729  1.00 33.98 ? 17  ARG B CA  1 
ATOM   1762 C C   . ARG B 1 15  ? -6.482  -30.521 19.890  1.00 35.98 ? 17  ARG B C   1 
ATOM   1763 O O   . ARG B 1 15  ? -5.483  -31.203 20.023  1.00 36.47 ? 17  ARG B O   1 
ATOM   1764 C CB  . ARG B 1 15  ? -7.474  -29.473 21.989  1.00 33.16 ? 17  ARG B CB  1 
ATOM   1765 C CG  . ARG B 1 15  ? -6.878  -30.539 22.900  1.00 35.72 ? 17  ARG B CG  1 
ATOM   1766 C CD  . ARG B 1 15  ? -7.860  -30.842 24.002  1.00 38.02 ? 17  ARG B CD  1 
ATOM   1767 N NE  . ARG B 1 15  ? -7.361  -31.893 24.868  1.00 41.59 ? 17  ARG B NE  1 
ATOM   1768 C CZ  . ARG B 1 15  ? -7.405  -33.196 24.604  1.00 44.16 ? 17  ARG B CZ  1 
ATOM   1769 N NH1 . ARG B 1 15  ? -7.915  -33.635 23.459  1.00 44.83 ? 17  ARG B NH1 1 
ATOM   1770 N NH2 . ARG B 1 15  ? -6.924  -34.065 25.471  1.00 44.56 ? 17  ARG B NH2 1 
ATOM   1771 N N   . ALA B 1 16  ? -7.451  -30.843 19.007  1.00 37.25 ? 18  ALA B N   1 
ATOM   1772 C CA  . ALA B 1 16  ? -7.372  -32.038 18.139  1.00 37.68 ? 18  ALA B CA  1 
ATOM   1773 C C   . ALA B 1 16  ? -6.214  -31.996 17.163  1.00 38.95 ? 18  ALA B C   1 
ATOM   1774 O O   . ALA B 1 16  ? -5.502  -32.991 17.009  1.00 39.23 ? 18  ALA B O   1 
ATOM   1775 C CB  . ALA B 1 16  ? -8.675  -32.234 17.384  1.00 36.56 ? 18  ALA B CB  1 
ATOM   1776 N N   . PHE B 1 17  ? -5.999  -30.867 16.501  1.00 39.95 ? 19  PHE B N   1 
ATOM   1777 C CA  . PHE B 1 17  ? -4.897  -30.720 15.566  1.00 41.45 ? 19  PHE B CA  1 
ATOM   1778 C C   . PHE B 1 17  ? -3.541  -30.963 16.279  1.00 40.99 ? 19  PHE B C   1 
ATOM   1779 O O   . PHE B 1 17  ? -2.769  -31.804 15.834  1.00 40.87 ? 19  PHE B O   1 
ATOM   1780 C CB  . PHE B 1 17  ? -4.964  -29.325 14.903  1.00 43.53 ? 19  PHE B CB  1 
ATOM   1781 C CG  . PHE B 1 17  ? -4.096  -29.241 13.686  1.00 46.31 ? 19  PHE B CG  1 
ATOM   1782 C CD1 . PHE B 1 17  ? -2.755  -28.939 13.796  1.00 47.54 ? 19  PHE B CD1 1 
ATOM   1783 C CD2 . PHE B 1 17  ? -4.593  -29.581 12.442  1.00 48.92 ? 19  PHE B CD2 1 
ATOM   1784 C CE1 . PHE B 1 17  ? -1.938  -28.897 12.671  1.00 48.90 ? 19  PHE B CE1 1 
ATOM   1785 C CE2 . PHE B 1 17  ? -3.776  -29.550 11.318  1.00 49.97 ? 19  PHE B CE2 1 
ATOM   1786 C CZ  . PHE B 1 17  ? -2.452  -29.191 11.442  1.00 49.46 ? 19  PHE B CZ  1 
ATOM   1787 N N   . LEU B 1 18  ? -3.273  -30.273 17.395  1.00 40.21 ? 20  LEU B N   1 
ATOM   1788 C CA  . LEU B 1 18  ? -1.985  -30.419 18.099  1.00 40.61 ? 20  LEU B CA  1 
ATOM   1789 C C   . LEU B 1 18  ? -1.729  -31.876 18.529  1.00 41.53 ? 20  LEU B C   1 
ATOM   1790 O O   . LEU B 1 18  ? -0.608  -32.365 18.440  1.00 42.88 ? 20  LEU B O   1 
ATOM   1791 C CB  . LEU B 1 18  ? -1.931  -29.482 19.333  1.00 40.28 ? 20  LEU B CB  1 
ATOM   1792 C CG  . LEU B 1 18  ? -1.983  -27.995 19.053  1.00 39.79 ? 20  LEU B CG  1 
ATOM   1793 C CD1 . LEU B 1 18  ? -2.143  -27.200 20.316  1.00 38.70 ? 20  LEU B CD1 1 
ATOM   1794 C CD2 . LEU B 1 18  ? -0.767  -27.538 18.320  1.00 40.44 ? 20  LEU B CD2 1 
ATOM   1795 N N   . MET B 1 19  ? -2.767  -32.553 18.998  1.00 40.87 ? 21  MET B N   1 
ATOM   1796 C CA  . MET B 1 19  ? -2.692  -33.960 19.316  1.00 41.50 ? 21  MET B CA  1 
ATOM   1797 C C   . MET B 1 19  ? -2.387  -34.882 18.110  1.00 42.99 ? 21  MET B C   1 
ATOM   1798 O O   . MET B 1 19  ? -1.684  -35.877 18.277  1.00 43.17 ? 21  MET B O   1 
ATOM   1799 C CB  . MET B 1 19  ? -3.973  -34.413 20.002  1.00 41.67 ? 21  MET B CB  1 
ATOM   1800 C CG  . MET B 1 19  ? -4.249  -33.742 21.324  1.00 41.32 ? 21  MET B CG  1 
ATOM   1801 S SD  . MET B 1 19  ? -2.919  -33.852 22.528  1.00 45.15 ? 21  MET B SD  1 
ATOM   1802 C CE  . MET B 1 19  ? -3.903  -33.821 24.043  1.00 44.31 ? 21  MET B CE  1 
ATOM   1803 N N   . ALA B 1 20  ? -2.884  -34.574 16.914  1.00 44.05 ? 22  ALA B N   1 
ATOM   1804 C CA  . ALA B 1 20  ? -2.604  -35.394 15.720  1.00 45.14 ? 22  ALA B CA  1 
ATOM   1805 C C   . ALA B 1 20  ? -1.170  -35.169 15.184  1.00 47.22 ? 22  ALA B C   1 
ATOM   1806 O O   . ALA B 1 20  ? -0.594  -36.061 14.546  1.00 47.43 ? 22  ALA B O   1 
ATOM   1807 C CB  . ALA B 1 20  ? -3.626  -35.079 14.649  1.00 44.44 ? 22  ALA B CB  1 
ATOM   1808 N N   . CYS B 1 21  ? -0.583  -33.974 15.439  1.00 47.31 ? 23  CYS B N   1 
ATOM   1809 C CA  . CYS B 1 21  ? 0.821   -33.703 15.094  1.00 48.42 ? 23  CYS B CA  1 
ATOM   1810 C C   . CYS B 1 21  ? 1.842   -34.401 16.033  1.00 48.47 ? 23  CYS B C   1 
ATOM   1811 O O   . CYS B 1 21  ? 3.050   -34.213 15.838  1.00 49.43 ? 23  CYS B O   1 
ATOM   1812 C CB  . CYS B 1 21  ? 1.065   -32.198 15.065  1.00 49.98 ? 23  CYS B CB  1 
ATOM   1813 S SG  . CYS B 1 21  ? 0.014   -31.273 13.912  1.00 55.40 ? 23  CYS B SG  1 
ATOM   1814 N N   . ARG B 1 22  ? 1.379   -35.184 17.031  1.00 47.25 ? 24  ARG B N   1 
ATOM   1815 C CA  . ARG B 1 22  ? 2.251   -35.812 18.047  1.00 47.06 ? 24  ARG B CA  1 
ATOM   1816 C C   . ARG B 1 22  ? 2.689   -37.224 17.625  1.00 50.14 ? 24  ARG B C   1 
ATOM   1817 O O   . ARG B 1 22  ? 2.004   -37.862 16.824  1.00 51.57 ? 24  ARG B O   1 
ATOM   1818 C CB  . ARG B 1 22  ? 1.507   -35.880 19.395  1.00 44.80 ? 24  ARG B CB  1 
ATOM   1819 C CG  . ARG B 1 22  ? 2.119   -36.708 20.521  1.00 43.39 ? 24  ARG B CG  1 
ATOM   1820 C CD  . ARG B 1 22  ? 1.142   -36.770 21.691  1.00 43.40 ? 24  ARG B CD  1 
ATOM   1821 N NE  . ARG B 1 22  ? 1.800   -37.109 22.956  1.00 43.86 ? 24  ARG B NE  1 
ATOM   1822 C CZ  . ARG B 1 22  ? 1.230   -37.018 24.151  1.00 46.80 ? 24  ARG B CZ  1 
ATOM   1823 N NH1 . ARG B 1 22  ? -0.023  -36.599 24.266  1.00 49.66 ? 24  ARG B NH1 1 
ATOM   1824 N NH2 . ARG B 1 22  ? 1.911   -37.344 25.247  1.00 46.63 ? 24  ARG B NH2 1 
ATOM   1825 N N   . GLY B 1 23  ? 3.808   -37.701 18.191  1.00 50.46 ? 25  GLY B N   1 
ATOM   1826 C CA  . GLY B 1 23  ? 4.305   -39.059 17.987  1.00 51.22 ? 25  GLY B CA  1 
ATOM   1827 C C   . GLY B 1 23  ? 4.253   -39.873 19.266  1.00 52.89 ? 25  GLY B C   1 
ATOM   1828 O O   . GLY B 1 23  ? 3.185   -40.086 19.864  1.00 53.34 ? 25  GLY B O   1 
ATOM   1829 N N   . LYS B 1 34  ? 6.935   -28.839 8.818   1.00 50.24 ? 36  LYS B N   1 
ATOM   1830 C CA  . LYS B 1 34  ? 6.559   -28.609 10.214  1.00 50.36 ? 36  LYS B CA  1 
ATOM   1831 C C   . LYS B 1 34  ? 5.542   -27.506 10.305  1.00 48.42 ? 36  LYS B C   1 
ATOM   1832 O O   . LYS B 1 34  ? 5.526   -26.612 9.459   1.00 49.31 ? 36  LYS B O   1 
ATOM   1833 C CB  . LYS B 1 34  ? 7.783   -28.250 11.072  1.00 53.91 ? 36  LYS B CB  1 
ATOM   1834 C CG  . LYS B 1 34  ? 8.674   -29.432 11.389  1.00 59.67 ? 36  LYS B CG  1 
ATOM   1835 C CD  . LYS B 1 34  ? 9.934   -29.001 12.107  1.00 65.21 ? 36  LYS B CD  1 
ATOM   1836 C CE  . LYS B 1 34  ? 10.717  -30.197 12.622  1.00 69.63 ? 36  LYS B CE  1 
ATOM   1837 N NZ  . LYS B 1 34  ? 11.973  -29.776 13.305  1.00 71.93 ? 36  LYS B NZ  1 
ATOM   1838 N N   . HIS B 1 35  ? 4.693   -27.556 11.335  1.00 46.15 ? 37  HIS B N   1 
ATOM   1839 C CA  . HIS B 1 35  ? 3.591   -26.614 11.467  1.00 44.59 ? 37  HIS B CA  1 
ATOM   1840 C C   . HIS B 1 35  ? 4.044   -25.464 12.332  1.00 43.12 ? 37  HIS B C   1 
ATOM   1841 O O   . HIS B 1 35  ? 4.301   -25.687 13.518  1.00 43.22 ? 37  HIS B O   1 
ATOM   1842 C CB  . HIS B 1 35  ? 2.389   -27.306 12.081  1.00 44.32 ? 37  HIS B CB  1 
ATOM   1843 C CG  . HIS B 1 35  ? 1.831   -28.350 11.169  1.00 45.18 ? 37  HIS B CG  1 
ATOM   1844 N ND1 . HIS B 1 35  ? 2.229   -29.671 11.254  1.00 47.22 ? 37  HIS B ND1 1 
ATOM   1845 C CD2 . HIS B 1 35  ? 0.923   -28.232 10.176  1.00 45.82 ? 37  HIS B CD2 1 
ATOM   1846 C CE1 . HIS B 1 35  ? 1.557   -30.314 10.316  1.00 47.21 ? 37  HIS B CE1 1 
ATOM   1847 N NE2 . HIS B 1 35  ? 0.757   -29.488 9.643   1.00 47.43 ? 37  HIS B NE2 1 
ATOM   1848 N N   . PRO B 1 36  ? 4.167   -24.242 11.776  1.00 41.49 ? 38  PRO B N   1 
ATOM   1849 C CA  . PRO B 1 36  ? 4.706   -23.135 12.568  1.00 39.96 ? 38  PRO B CA  1 
ATOM   1850 C C   . PRO B 1 36  ? 3.789   -22.651 13.658  1.00 38.81 ? 38  PRO B C   1 
ATOM   1851 O O   . PRO B 1 36  ? 2.592   -22.654 13.470  1.00 38.58 ? 38  PRO B O   1 
ATOM   1852 C CB  . PRO B 1 36  ? 4.889   -22.039 11.531  1.00 41.02 ? 38  PRO B CB  1 
ATOM   1853 C CG  . PRO B 1 36  ? 3.887   -22.338 10.496  1.00 41.88 ? 38  PRO B CG  1 
ATOM   1854 C CD  . PRO B 1 36  ? 3.843   -23.802 10.406  1.00 40.84 ? 38  PRO B CD  1 
ATOM   1855 N N   . LEU B 1 37  ? 4.359   -22.211 14.819  1.00 37.41 ? 39  LEU B N   1 
ATOM   1856 C CA  . LEU B 1 37  ? 3.599   -21.563 15.887  1.00 35.23 ? 39  LEU B CA  1 
ATOM   1857 C C   . LEU B 1 37  ? 3.537   -20.060 15.620  1.00 35.64 ? 39  LEU B C   1 
ATOM   1858 O O   . LEU B 1 37  ? 4.422   -19.492 14.987  1.00 35.75 ? 39  LEU B O   1 
ATOM   1859 C CB  . LEU B 1 37  ? 4.233   -21.863 17.256  1.00 33.57 ? 39  LEU B CB  1 
ATOM   1860 C CG  . LEU B 1 37  ? 4.381   -23.351 17.664  1.00 32.01 ? 39  LEU B CG  1 
ATOM   1861 C CD1 . LEU B 1 37  ? 5.017   -23.492 19.094  1.00 31.07 ? 39  LEU B CD1 1 
ATOM   1862 C CD2 . LEU B 1 37  ? 3.082   -24.080 17.607  1.00 31.47 ? 39  LEU B CD2 1 
ATOM   1863 N N   . GLN B 1 38  ? 2.467   -19.418 16.074  1.00 34.77 ? 40  GLN B N   1 
ATOM   1864 C CA  . GLN B 1 38  ? 2.329   -17.960 16.025  1.00 33.31 ? 40  GLN B CA  1 
ATOM   1865 C C   . GLN B 1 38  ? 3.485   -17.259 16.727  1.00 31.89 ? 40  GLN B C   1 
ATOM   1866 O O   . GLN B 1 38  ? 3.924   -16.192 16.293  1.00 32.91 ? 40  GLN B O   1 
ATOM   1867 C CB  . GLN B 1 38  ? 1.002   -17.550 16.715  1.00 35.39 ? 40  GLN B CB  1 
ATOM   1868 C CG  . GLN B 1 38  ? 0.736   -16.037 16.783  1.00 36.68 ? 40  GLN B CG  1 
ATOM   1869 C CD  . GLN B 1 38  ? 0.429   -15.452 15.444  1.00 40.82 ? 40  GLN B CD  1 
ATOM   1870 O OE1 . GLN B 1 38  ? 0.168   -16.156 14.451  1.00 39.44 ? 40  GLN B OE1 1 
ATOM   1871 N NE2 . GLN B 1 38  ? 0.458   -14.122 15.400  1.00 42.48 ? 40  GLN B NE2 1 
ATOM   1872 N N   . ASN B 1 39  ? 3.953   -17.858 17.835  1.00 30.19 ? 41  ASN B N   1 
ATOM   1873 C CA  . ASN B 1 39  ? 5.016   -17.364 18.695  1.00 29.31 ? 41  ASN B CA  1 
ATOM   1874 C C   . ASN B 1 39  ? 6.119   -18.407 18.862  1.00 28.73 ? 41  ASN B C   1 
ATOM   1875 O O   . ASN B 1 39  ? 5.865   -19.624 18.768  1.00 26.73 ? 41  ASN B O   1 
ATOM   1876 C CB  . ASN B 1 39  ? 4.449   -17.046 20.048  1.00 30.12 ? 41  ASN B CB  1 
ATOM   1877 C CG  . ASN B 1 39  ? 3.613   -15.810 20.017  1.00 36.14 ? 41  ASN B CG  1 
ATOM   1878 O OD1 . ASN B 1 39  ? 4.103   -14.753 19.654  1.00 37.58 ? 41  ASN B OD1 1 
ATOM   1879 N ND2 . ASN B 1 39  ? 2.388   -15.877 20.371  1.00 37.42 ? 41  ASN B ND2 1 
ATOM   1880 N N   . ARG B 1 40  ? 7.354   -17.923 19.081  1.00 27.98 ? 42  ARG B N   1 
ATOM   1881 C CA  . ARG B 1 40  ? 8.428   -18.717 19.643  1.00 27.54 ? 42  ARG B CA  1 
ATOM   1882 C C   . ARG B 1 40  ? 8.324   -18.721 21.175  1.00 25.40 ? 42  ARG B C   1 
ATOM   1883 O O   . ARG B 1 40  ? 7.982   -17.706 21.785  1.00 25.07 ? 42  ARG B O   1 
ATOM   1884 C CB  . ARG B 1 40  ? 9.775   -18.157 19.209  1.00 29.99 ? 42  ARG B CB  1 
ATOM   1885 C CG  . ARG B 1 40  ? 10.990  -19.026 19.563  1.00 34.17 ? 42  ARG B CG  1 
ATOM   1886 C CD  . ARG B 1 40  ? 12.060  -18.856 18.474  1.00 37.42 ? 42  ARG B CD  1 
ATOM   1887 N NE  . ARG B 1 40  ? 13.277  -19.641 18.736  1.00 38.44 ? 42  ARG B NE  1 
ATOM   1888 C CZ  . ARG B 1 40  ? 14.384  -19.196 19.329  1.00 40.57 ? 42  ARG B CZ  1 
ATOM   1889 N NH1 . ARG B 1 40  ? 14.477  -17.929 19.727  1.00 37.50 ? 42  ARG B NH1 1 
ATOM   1890 N NH2 . ARG B 1 40  ? 15.423  -20.006 19.497  1.00 41.94 ? 42  ARG B NH2 1 
ATOM   1891 N N   . TRP B 1 41  ? 8.623   -19.885 21.785  1.00 23.80 ? 43  TRP B N   1 
ATOM   1892 C CA  . TRP B 1 41  ? 8.400   -20.137 23.194  1.00 24.97 ? 43  TRP B CA  1 
ATOM   1893 C C   . TRP B 1 41  ? 9.665   -20.663 23.787  1.00 27.09 ? 43  TRP B C   1 
ATOM   1894 O O   . TRP B 1 41  ? 10.404  -21.405 23.129  1.00 28.05 ? 43  TRP B O   1 
ATOM   1895 C CB  . TRP B 1 41  ? 7.292   -21.193 23.436  1.00 23.75 ? 43  TRP B CB  1 
ATOM   1896 C CG  . TRP B 1 41  ? 5.961   -20.765 22.923  1.00 23.25 ? 43  TRP B CG  1 
ATOM   1897 C CD1 . TRP B 1 41  ? 5.504   -20.893 21.645  1.00 24.23 ? 43  TRP B CD1 1 
ATOM   1898 C CD2 . TRP B 1 41  ? 4.973   -19.993 23.629  1.00 23.72 ? 43  TRP B CD2 1 
ATOM   1899 N NE1 . TRP B 1 41  ? 4.297   -20.250 21.503  1.00 23.97 ? 43  TRP B NE1 1 
ATOM   1900 C CE2 . TRP B 1 41  ? 3.932   -19.713 22.719  1.00 24.37 ? 43  TRP B CE2 1 
ATOM   1901 C CE3 . TRP B 1 41  ? 4.876   -19.494 24.929  1.00 24.29 ? 43  TRP B CE3 1 
ATOM   1902 C CZ2 . TRP B 1 41  ? 2.802   -18.982 23.089  1.00 24.76 ? 43  TRP B CZ2 1 
ATOM   1903 C CZ3 . TRP B 1 41  ? 3.751   -18.798 25.294  1.00 25.02 ? 43  TRP B CZ3 1 
ATOM   1904 C CH2 . TRP B 1 41  ? 2.730   -18.547 24.378  1.00 25.12 ? 43  TRP B CH2 1 
ATOM   1905 N N   . ALA B 1 42  ? 9.909   -20.283 25.048  1.00 26.30 ? 44  ALA B N   1 
ATOM   1906 C CA  . ALA B 1 42  ? 11.084  -20.707 25.779  1.00 25.94 ? 44  ALA B CA  1 
ATOM   1907 C C   . ALA B 1 42  ? 10.660  -21.441 27.034  1.00 26.16 ? 44  ALA B C   1 
ATOM   1908 O O   . ALA B 1 42  ? 9.810   -20.970 27.785  1.00 24.84 ? 44  ALA B O   1 
ATOM   1909 C CB  . ALA B 1 42  ? 11.940  -19.494 26.116  1.00 25.34 ? 44  ALA B CB  1 
ATOM   1910 N N   . LEU B 1 43  ? 11.232  -22.621 27.246  1.00 27.18 ? 45  LEU B N   1 
ATOM   1911 C CA  . LEU B 1 43  ? 11.024  -23.410 28.460  1.00 27.58 ? 45  LEU B CA  1 
ATOM   1912 C C   . LEU B 1 43  ? 12.143  -23.135 29.433  1.00 28.77 ? 45  LEU B C   1 
ATOM   1913 O O   . LEU B 1 43  ? 13.317  -23.302 29.063  1.00 29.46 ? 45  LEU B O   1 
ATOM   1914 C CB  . LEU B 1 43  ? 11.012  -24.934 28.160  1.00 27.56 ? 45  LEU B CB  1 
ATOM   1915 C CG  . LEU B 1 43  ? 10.842  -25.849 29.422  1.00 28.22 ? 45  LEU B CG  1 
ATOM   1916 C CD1 . LEU B 1 43  ? 9.515   -25.568 30.174  1.00 28.71 ? 45  LEU B CD1 1 
ATOM   1917 C CD2 . LEU B 1 43  ? 10.918  -27.293 29.053  1.00 27.57 ? 45  LEU B CD2 1 
ATOM   1918 N N   . TRP B 1 44  ? 11.781  -22.744 30.684  1.00 29.31 ? 46  TRP B N   1 
ATOM   1919 C CA  . TRP B 1 44  ? 12.673  -22.431 31.788  1.00 30.84 ? 46  TRP B CA  1 
ATOM   1920 C C   . TRP B 1 44  ? 12.470  -23.389 32.970  1.00 35.30 ? 46  TRP B C   1 
ATOM   1921 O O   . TRP B 1 44  ? 11.362  -23.866 33.202  1.00 34.81 ? 46  TRP B O   1 
ATOM   1922 C CB  . TRP B 1 44  ? 12.389  -21.026 32.302  1.00 30.04 ? 46  TRP B CB  1 
ATOM   1923 C CG  . TRP B 1 44  ? 12.416  -19.955 31.255  1.00 31.43 ? 46  TRP B CG  1 
ATOM   1924 C CD1 . TRP B 1 44  ? 11.422  -19.614 30.372  1.00 32.00 ? 46  TRP B CD1 1 
ATOM   1925 C CD2 . TRP B 1 44  ? 13.505  -19.079 30.986  1.00 32.09 ? 46  TRP B CD2 1 
ATOM   1926 N NE1 . TRP B 1 44  ? 11.826  -18.567 29.591  1.00 32.15 ? 46  TRP B NE1 1 
ATOM   1927 C CE2 . TRP B 1 44  ? 13.102  -18.213 29.947  1.00 32.52 ? 46  TRP B CE2 1 
ATOM   1928 C CE3 . TRP B 1 44  ? 14.756  -18.886 31.576  1.00 33.11 ? 46  TRP B CE3 1 
ATOM   1929 C CZ2 . TRP B 1 44  ? 13.937  -17.227 29.440  1.00 34.07 ? 46  TRP B CZ2 1 
ATOM   1930 C CZ3 . TRP B 1 44  ? 15.579  -17.903 31.072  1.00 34.39 ? 46  TRP B CZ3 1 
ATOM   1931 C CH2 . TRP B 1 44  ? 15.159  -17.075 30.031  1.00 34.70 ? 46  TRP B CH2 1 
ATOM   1932 N N   . PHE B 1 45  ? 13.563  -23.646 33.728  1.00 38.37 ? 47  PHE B N   1 
ATOM   1933 C CA  . PHE B 1 45  ? 13.576  -24.378 35.000  1.00 42.64 ? 47  PHE B CA  1 
ATOM   1934 C C   . PHE B 1 45  ? 14.130  -23.431 36.082  1.00 44.27 ? 47  PHE B C   1 
ATOM   1935 O O   . PHE B 1 45  ? 15.102  -22.721 35.806  1.00 43.66 ? 47  PHE B O   1 
ATOM   1936 C CB  . PHE B 1 45  ? 14.487  -25.606 34.861  1.00 44.94 ? 47  PHE B CB  1 
ATOM   1937 C CG  . PHE B 1 45  ? 14.687  -26.421 36.107  1.00 48.29 ? 47  PHE B CG  1 
ATOM   1938 C CD1 . PHE B 1 45  ? 13.658  -27.188 36.625  1.00 50.63 ? 47  PHE B CD1 1 
ATOM   1939 C CD2 . PHE B 1 45  ? 15.913  -26.439 36.755  1.00 50.23 ? 47  PHE B CD2 1 
ATOM   1940 C CE1 . PHE B 1 45  ? 13.843  -27.937 37.780  1.00 52.21 ? 47  PHE B CE1 1 
ATOM   1941 C CE2 . PHE B 1 45  ? 16.101  -27.197 37.903  1.00 51.61 ? 47  PHE B CE2 1 
ATOM   1942 C CZ  . PHE B 1 45  ? 15.069  -27.943 38.411  1.00 51.93 ? 47  PHE B CZ  1 
ATOM   1943 N N   . PHE B 1 46  ? 13.515  -23.397 37.283  1.00 46.50 ? 48  PHE B N   1 
ATOM   1944 C CA  . PHE B 1 46  ? 13.932  -22.539 38.413  1.00 50.67 ? 48  PHE B CA  1 
ATOM   1945 C C   . PHE B 1 46  ? 13.744  -23.305 39.774  1.00 54.41 ? 48  PHE B C   1 
ATOM   1946 O O   . PHE B 1 46  ? 12.970  -24.265 39.833  1.00 53.81 ? 48  PHE B O   1 
ATOM   1947 C CB  . PHE B 1 46  ? 13.128  -21.213 38.406  1.00 51.71 ? 48  PHE B CB  1 
ATOM   1948 C CG  . PHE B 1 46  ? 13.404  -20.252 39.558  1.00 55.20 ? 48  PHE B CG  1 
ATOM   1949 C CD1 . PHE B 1 46  ? 14.412  -19.311 39.473  1.00 56.37 ? 48  PHE B CD1 1 
ATOM   1950 C CD2 . PHE B 1 46  ? 12.641  -20.293 40.727  1.00 57.56 ? 48  PHE B CD2 1 
ATOM   1951 C CE1 . PHE B 1 46  ? 14.676  -18.448 40.539  1.00 57.59 ? 48  PHE B CE1 1 
ATOM   1952 C CE2 . PHE B 1 46  ? 12.897  -19.411 41.783  1.00 58.15 ? 48  PHE B CE2 1 
ATOM   1953 C CZ  . PHE B 1 46  ? 13.907  -18.490 41.673  1.00 57.57 ? 48  PHE B CZ  1 
ATOM   1954 N N   . LYS B 1 47  ? 14.456  -22.871 40.864  1.00 57.02 ? 49  LYS B N   1 
ATOM   1955 C CA  . LYS B 1 47  ? 14.416  -23.523 42.195  1.00 59.05 ? 49  LYS B CA  1 
ATOM   1956 C C   . LYS B 1 47  ? 14.749  -22.523 43.303  1.00 61.95 ? 49  LYS B C   1 
ATOM   1957 O O   . LYS B 1 47  ? 15.615  -21.680 43.104  1.00 62.07 ? 49  LYS B O   1 
ATOM   1958 C CB  . LYS B 1 47  ? 15.405  -24.712 42.266  1.00 59.22 ? 49  LYS B CB  1 
ATOM   1959 C CG  . LYS B 1 47  ? 15.090  -25.682 43.401  1.00 61.71 ? 49  LYS B CG  1 
ATOM   1960 C CD  . LYS B 1 47  ? 16.175  -26.712 43.659  1.00 65.82 ? 49  LYS B CD  1 
ATOM   1961 C CE  . LYS B 1 47  ? 17.400  -26.188 44.422  1.00 68.37 ? 49  LYS B CE  1 
ATOM   1962 N NZ  . LYS B 1 47  ? 18.341  -27.282 44.867  1.00 67.23 ? 49  LYS B NZ  1 
ATOM   1963 N N   . ASN B 1 48  ? 14.080  -22.615 44.474  1.00 64.21 ? 50  ASN B N   1 
ATOM   1964 C CA  . ASN B 1 48  ? 14.229  -21.622 45.550  1.00 66.80 ? 50  ASN B CA  1 
ATOM   1965 C C   . ASN B 1 48  ? 15.513  -21.794 46.399  1.00 68.88 ? 50  ASN B C   1 
ATOM   1966 O O   . ASN B 1 48  ? 15.458  -21.582 47.619  1.00 69.23 ? 50  ASN B O   1 
ATOM   1967 C CB  . ASN B 1 48  ? 12.982  -21.607 46.482  1.00 68.49 ? 50  ASN B CB  1 
ATOM   1968 C CG  . ASN B 1 48  ? 12.965  -20.374 47.389  1.00 72.98 ? 50  ASN B CG  1 
ATOM   1969 O OD1 . ASN B 1 48  ? 13.109  -19.238 46.912  1.00 74.06 ? 50  ASN B OD1 1 
ATOM   1970 N ND2 . ASN B 1 48  ? 12.808  -20.548 48.717  1.00 73.58 ? 50  ASN B ND2 1 
ATOM   1971 N N   . ASP B 1 49  ? 16.676  -22.161 45.777  1.00 69.81 ? 51  ASP B N   1 
ATOM   1972 C CA  . ASP B 1 49  ? 17.916  -22.315 46.560  1.00 71.16 ? 51  ASP B CA  1 
ATOM   1973 C C   . ASP B 1 49  ? 18.432  -20.956 46.998  1.00 71.90 ? 51  ASP B C   1 
ATOM   1974 O O   . ASP B 1 49  ? 18.418  -20.007 46.213  1.00 71.62 ? 51  ASP B O   1 
ATOM   1975 C CB  . ASP B 1 49  ? 19.020  -23.031 45.768  1.00 73.42 ? 51  ASP B CB  1 
ATOM   1976 C CG  . ASP B 1 49  ? 20.197  -23.503 46.613  1.00 79.22 ? 51  ASP B CG  1 
ATOM   1977 O OD1 . ASP B 1 49  ? 20.115  -23.412 47.864  1.00 80.13 ? 51  ASP B OD1 1 
ATOM   1978 O OD2 . ASP B 1 49  ? 21.202  -23.964 46.026  1.00 81.82 ? 51  ASP B OD2 1 
ATOM   1979 N N   . LYS B 1 50  ? 18.893  -20.870 48.251  1.00 72.37 ? 52  LYS B N   1 
ATOM   1980 C CA  . LYS B 1 50  ? 19.357  -19.601 48.826  1.00 72.99 ? 52  LYS B CA  1 
ATOM   1981 C C   . LYS B 1 50  ? 20.868  -19.418 48.651  1.00 73.49 ? 52  LYS B C   1 
ATOM   1982 O O   . LYS B 1 50  ? 21.331  -18.292 48.397  1.00 72.94 ? 52  LYS B O   1 
ATOM   1983 C CB  . LYS B 1 50  ? 18.934  -19.493 50.307  1.00 73.24 ? 52  LYS B CB  1 
ATOM   1984 C CG  . LYS B 1 50  ? 17.527  -18.912 50.496  1.00 76.43 ? 52  LYS B CG  1 
ATOM   1985 C CD  . LYS B 1 50  ? 17.558  -17.385 50.394  1.00 79.82 ? 52  LYS B CD  1 
ATOM   1986 C CE  . LYS B 1 50  ? 16.297  -16.775 49.868  1.00 81.81 ? 52  LYS B CE  1 
ATOM   1987 N NZ  . LYS B 1 50  ? 16.405  -15.293 49.867  1.00 82.97 ? 52  LYS B NZ  1 
ATOM   1988 N N   . SER B 1 51  ? 21.632  -20.527 48.769  1.00 74.28 ? 53  SER B N   1 
ATOM   1989 C CA  . SER B 1 51  ? 23.085  -20.557 48.512  1.00 75.38 ? 53  SER B CA  1 
ATOM   1990 C C   . SER B 1 51  ? 23.484  -19.824 47.201  1.00 76.31 ? 53  SER B C   1 
ATOM   1991 O O   . SER B 1 51  ? 24.605  -19.311 47.093  1.00 76.21 ? 53  SER B O   1 
ATOM   1992 C CB  . SER B 1 51  ? 23.566  -22.003 48.451  1.00 76.28 ? 53  SER B CB  1 
ATOM   1993 O OG  . SER B 1 51  ? 24.915  -22.103 48.026  1.00 78.18 ? 53  SER B OG  1 
ATOM   1994 N N   . LYS B 1 52  ? 22.554  -19.792 46.226  1.00 76.73 ? 54  LYS B N   1 
ATOM   1995 C CA  . LYS B 1 52  ? 22.747  -19.209 44.899  1.00 77.77 ? 54  LYS B CA  1 
ATOM   1996 C C   . LYS B 1 52  ? 21.783  -18.024 44.709  1.00 79.08 ? 54  LYS B C   1 
ATOM   1997 O O   . LYS B 1 52  ? 20.655  -18.073 45.198  1.00 79.39 ? 54  LYS B O   1 
ATOM   1998 C CB  . LYS B 1 52  ? 22.483  -20.291 43.837  1.00 78.77 ? 54  LYS B CB  1 
ATOM   1999 C CG  . LYS B 1 52  ? 23.136  -21.643 44.153  1.00 81.73 ? 54  LYS B CG  1 
ATOM   2000 C CD  . LYS B 1 52  ? 23.009  -22.624 42.994  1.00 86.36 ? 54  LYS B CD  1 
ATOM   2001 C CE  . LYS B 1 52  ? 23.187  -24.067 43.406  1.00 89.69 ? 54  LYS B CE  1 
ATOM   2002 N NZ  . LYS B 1 52  ? 22.762  -25.001 42.327  1.00 91.46 ? 54  LYS B NZ  1 
ATOM   2003 N N   . THR B 1 53  ? 22.216  -16.962 44.012  1.00 79.69 ? 55  THR B N   1 
ATOM   2004 C CA  . THR B 1 53  ? 21.312  -15.850 43.680  1.00 80.86 ? 55  THR B CA  1 
ATOM   2005 C C   . THR B 1 53  ? 20.211  -16.330 42.710  1.00 81.39 ? 55  THR B C   1 
ATOM   2006 O O   . THR B 1 53  ? 20.375  -17.359 42.047  1.00 81.81 ? 55  THR B O   1 
ATOM   2007 C CB  . THR B 1 53  ? 22.087  -14.595 43.147  1.00 82.98 ? 55  THR B CB  1 
ATOM   2008 O OG1 . THR B 1 53  ? 23.267  -14.998 42.428  1.00 84.76 ? 55  THR B OG1 1 
ATOM   2009 C CG2 . THR B 1 53  ? 22.499  -13.608 44.274  1.00 83.26 ? 55  THR B CG2 1 
ATOM   2010 N N   . TRP B 1 54  ? 19.081  -15.593 42.624  1.00 80.98 ? 56  TRP B N   1 
ATOM   2011 C CA  . TRP B 1 54  ? 17.929  -16.029 41.813  1.00 80.84 ? 56  TRP B CA  1 
ATOM   2012 C C   . TRP B 1 54  ? 18.323  -16.300 40.364  1.00 79.45 ? 56  TRP B C   1 
ATOM   2013 O O   . TRP B 1 54  ? 17.879  -17.289 39.782  1.00 79.60 ? 56  TRP B O   1 
ATOM   2014 C CB  . TRP B 1 54  ? 16.762  -15.010 41.864  1.00 81.52 ? 56  TRP B CB  1 
ATOM   2015 C CG  . TRP B 1 54  ? 16.964  -13.728 41.094  1.00 83.44 ? 56  TRP B CG  1 
ATOM   2016 C CD1 . TRP B 1 54  ? 17.433  -12.543 41.583  1.00 84.85 ? 56  TRP B CD1 1 
ATOM   2017 C CD2 . TRP B 1 54  ? 16.641  -13.490 39.713  1.00 84.15 ? 56  TRP B CD2 1 
ATOM   2018 N NE1 . TRP B 1 54  ? 17.453  -11.590 40.584  1.00 85.23 ? 56  TRP B NE1 1 
ATOM   2019 C CE2 . TRP B 1 54  ? 16.977  -12.148 39.426  1.00 85.08 ? 56  TRP B CE2 1 
ATOM   2020 C CE3 . TRP B 1 54  ? 16.105  -14.283 38.689  1.00 85.00 ? 56  TRP B CE3 1 
ATOM   2021 C CZ2 . TRP B 1 54  ? 16.793  -11.586 38.161  1.00 86.00 ? 56  TRP B CZ2 1 
ATOM   2022 C CZ3 . TRP B 1 54  ? 15.936  -13.729 37.433  1.00 86.10 ? 56  TRP B CZ3 1 
ATOM   2023 C CH2 . TRP B 1 54  ? 16.279  -12.396 37.178  1.00 86.29 ? 56  TRP B CH2 1 
ATOM   2024 N N   . GLN B 1 55  ? 19.166  -15.428 39.793  1.00 77.77 ? 57  GLN B N   1 
ATOM   2025 C CA  . GLN B 1 55  ? 19.608  -15.547 38.410  1.00 76.29 ? 57  GLN B CA  1 
ATOM   2026 C C   . GLN B 1 55  ? 20.467  -16.828 38.214  1.00 73.37 ? 57  GLN B C   1 
ATOM   2027 O O   . GLN B 1 55  ? 20.468  -17.391 37.122  1.00 73.69 ? 57  GLN B O   1 
ATOM   2028 C CB  . GLN B 1 55  ? 20.372  -14.264 37.993  1.00 78.65 ? 57  GLN B CB  1 
ATOM   2029 C CG  . GLN B 1 55  ? 20.645  -14.157 36.492  1.00 83.26 ? 57  GLN B CG  1 
ATOM   2030 C CD  . GLN B 1 55  ? 21.359  -12.877 36.102  1.00 88.53 ? 57  GLN B CD  1 
ATOM   2031 O OE1 . GLN B 1 55  ? 22.199  -12.354 36.844  1.00 90.43 ? 57  GLN B OE1 1 
ATOM   2032 N NE2 . GLN B 1 55  ? 21.049  -12.342 34.919  1.00 89.14 ? 57  GLN B NE2 1 
ATOM   2033 N N   . ALA B 1 56  ? 21.186  -17.284 39.250  1.00 70.48 ? 58  ALA B N   1 
ATOM   2034 C CA  . ALA B 1 56  ? 21.882  -18.573 39.188  1.00 68.08 ? 58  ALA B CA  1 
ATOM   2035 C C   . ALA B 1 56  ? 20.902  -19.756 39.204  1.00 65.17 ? 58  ALA B C   1 
ATOM   2036 O O   . ALA B 1 56  ? 21.229  -20.805 38.649  1.00 65.45 ? 58  ALA B O   1 
ATOM   2037 C CB  . ALA B 1 56  ? 22.883  -18.701 40.332  1.00 67.57 ? 58  ALA B CB  1 
ATOM   2038 N N   . ASN B 1 57  ? 19.722  -19.598 39.828  1.00 62.10 ? 59  ASN B N   1 
ATOM   2039 C CA  . ASN B 1 57  ? 18.701  -20.649 39.852  1.00 60.98 ? 59  ASN B CA  1 
ATOM   2040 C C   . ASN B 1 57  ? 17.823  -20.731 38.603  1.00 58.86 ? 59  ASN B C   1 
ATOM   2041 O O   . ASN B 1 57  ? 17.269  -21.783 38.347  1.00 59.15 ? 59  ASN B O   1 
ATOM   2042 C CB  . ASN B 1 57  ? 17.786  -20.476 41.070  1.00 62.22 ? 59  ASN B CB  1 
ATOM   2043 C CG  . ASN B 1 57  ? 18.465  -20.765 42.380  1.00 63.37 ? 59  ASN B CG  1 
ATOM   2044 O OD1 . ASN B 1 57  ? 19.394  -21.583 42.467  1.00 64.46 ? 59  ASN B OD1 1 
ATOM   2045 N ND2 . ASN B 1 57  ? 18.012  -20.106 43.423  1.00 63.25 ? 59  ASN B ND2 1 
ATOM   2046 N N   . LEU B 1 58  ? 17.662  -19.638 37.864  1.00 57.25 ? 60  LEU B N   1 
ATOM   2047 C CA  . LEU B 1 58  ? 16.907  -19.643 36.635  1.00 55.83 ? 60  LEU B CA  1 
ATOM   2048 C C   . LEU B 1 58  ? 17.763  -20.204 35.511  1.00 54.85 ? 60  LEU B C   1 
ATOM   2049 O O   . LEU B 1 58  ? 18.740  -19.571 35.141  1.00 54.56 ? 60  LEU B O   1 
ATOM   2050 C CB  . LEU B 1 58  ? 16.461  -18.232 36.319  1.00 56.16 ? 60  LEU B CB  1 
ATOM   2051 C CG  . LEU B 1 58  ? 15.621  -18.038 35.062  1.00 58.47 ? 60  LEU B CG  1 
ATOM   2052 C CD1 . LEU B 1 58  ? 14.367  -18.942 35.069  1.00 59.05 ? 60  LEU B CD1 1 
ATOM   2053 C CD2 . LEU B 1 58  ? 15.227  -16.567 34.902  1.00 59.15 ? 60  LEU B CD2 1 
ATOM   2054 N N   . ARG B 1 59  ? 17.404  -21.410 34.981  1.00 54.08 ? 61  ARG B N   1 
ATOM   2055 C CA  . ARG B 1 59  ? 18.073  -22.073 33.853  1.00 52.82 ? 61  ARG B CA  1 
ATOM   2056 C C   . ARG B 1 59  ? 17.137  -22.118 32.637  1.00 51.09 ? 61  ARG B C   1 
ATOM   2057 O O   . ARG B 1 59  ? 15.952  -22.418 32.796  1.00 51.18 ? 61  ARG B O   1 
ATOM   2058 C CB  . ARG B 1 59  ? 18.426  -23.508 34.240  1.00 54.52 ? 61  ARG B CB  1 
ATOM   2059 C CG  . ARG B 1 59  ? 19.538  -24.098 33.409  1.00 59.28 ? 61  ARG B CG  1 
ATOM   2060 C CD  . ARG B 1 59  ? 19.966  -25.485 33.872  1.00 63.70 ? 61  ARG B CD  1 
ATOM   2061 N NE  . ARG B 1 59  ? 20.064  -26.381 32.708  1.00 68.06 ? 61  ARG B NE  1 
ATOM   2062 C CZ  . ARG B 1 59  ? 19.520  -27.593 32.574  1.00 71.96 ? 61  ARG B CZ  1 
ATOM   2063 N NH1 . ARG B 1 59  ? 18.801  -28.128 33.563  1.00 72.71 ? 61  ARG B NH1 1 
ATOM   2064 N NH2 . ARG B 1 59  ? 19.692  -28.281 31.450  1.00 72.57 ? 61  ARG B NH2 1 
ATOM   2065 N N   . LEU B 1 60  ? 17.654  -21.825 31.436  1.00 48.91 ? 62  LEU B N   1 
ATOM   2066 C CA  . LEU B 1 60  ? 16.898  -21.901 30.180  1.00 47.80 ? 62  LEU B CA  1 
ATOM   2067 C C   . LEU B 1 60  ? 17.173  -23.300 29.586  1.00 45.78 ? 62  LEU B C   1 
ATOM   2068 O O   . LEU B 1 60  ? 18.330  -23.712 29.437  1.00 46.20 ? 62  LEU B O   1 
ATOM   2069 C CB  . LEU B 1 60  ? 17.317  -20.755 29.238  1.00 48.97 ? 62  LEU B CB  1 
ATOM   2070 C CG  . LEU B 1 60  ? 16.727  -20.603 27.812  1.00 52.17 ? 62  LEU B CG  1 
ATOM   2071 C CD1 . LEU B 1 60  ? 17.515  -21.376 26.817  1.00 53.74 ? 62  LEU B CD1 1 
ATOM   2072 C CD2 . LEU B 1 60  ? 15.244  -20.897 27.725  1.00 52.70 ? 62  LEU B CD2 1 
ATOM   2073 N N   . ILE B 1 61  ? 16.096  -24.027 29.263  1.00 42.87 ? 63  ILE B N   1 
ATOM   2074 C CA  . ILE B 1 61  ? 16.165  -25.413 28.848  1.00 41.34 ? 63  ILE B CA  1 
ATOM   2075 C C   . ILE B 1 61  ? 16.182  -25.474 27.325  1.00 40.44 ? 63  ILE B C   1 
ATOM   2076 O O   . ILE B 1 61  ? 17.037  -26.160 26.749  1.00 40.69 ? 63  ILE B O   1 
ATOM   2077 C CB  . ILE B 1 61  ? 14.990  -26.241 29.434  1.00 41.10 ? 63  ILE B CB  1 
ATOM   2078 C CG1 . ILE B 1 61  ? 14.956  -26.246 30.998  1.00 42.53 ? 63  ILE B CG1 1 
ATOM   2079 C CG2 . ILE B 1 61  ? 14.988  -27.650 28.858  1.00 40.89 ? 63  ILE B CG2 1 
ATOM   2080 C CD1 . ILE B 1 61  ? 16.383  -26.258 31.787  1.00 45.66 ? 63  ILE B CD1 1 
ATOM   2081 N N   . SER B 1 62  ? 15.253  -24.775 26.658  1.00 39.39 ? 64  SER B N   1 
ATOM   2082 C CA  . SER B 1 62  ? 15.083  -24.936 25.217  1.00 39.25 ? 64  SER B CA  1 
ATOM   2083 C C   . SER B 1 62  ? 14.087  -23.934 24.653  1.00 37.31 ? 64  SER B C   1 
ATOM   2084 O O   . SER B 1 62  ? 13.226  -23.441 25.384  1.00 37.71 ? 64  SER B O   1 
ATOM   2085 C CB  . SER B 1 62  ? 14.581  -26.356 24.932  1.00 41.96 ? 64  SER B CB  1 
ATOM   2086 O OG  . SER B 1 62  ? 14.902  -26.804 23.629  1.00 46.46 ? 64  SER B OG  1 
ATOM   2087 N N   . LYS B 1 63  ? 14.189  -23.642 23.346  1.00 34.94 ? 65  LYS B N   1 
ATOM   2088 C CA  . LYS B 1 63  ? 13.196  -22.844 22.643  1.00 33.64 ? 65  LYS B CA  1 
ATOM   2089 C C   . LYS B 1 63  ? 12.649  -23.585 21.432  1.00 33.76 ? 65  LYS B C   1 
ATOM   2090 O O   . LYS B 1 63  ? 13.302  -24.454 20.912  1.00 34.44 ? 65  LYS B O   1 
ATOM   2091 C CB  . LYS B 1 63  ? 13.795  -21.521 22.187  1.00 33.85 ? 65  LYS B CB  1 
ATOM   2092 C CG  . LYS B 1 63  ? 14.346  -20.693 23.327  1.00 34.18 ? 65  LYS B CG  1 
ATOM   2093 C CD  . LYS B 1 63  ? 14.545  -19.236 22.936  1.00 31.96 ? 65  LYS B CD  1 
ATOM   2094 C CE  . LYS B 1 63  ? 15.194  -18.452 24.031  1.00 34.29 ? 65  LYS B CE  1 
ATOM   2095 N NZ  . LYS B 1 63  ? 15.667  -17.157 23.525  1.00 39.22 ? 65  LYS B NZ  1 
ATOM   2096 N N   . PHE B 1 64  ? 11.455  -23.216 20.971  1.00 33.27 ? 66  PHE B N   1 
ATOM   2097 C CA  . PHE B 1 64  ? 10.833  -23.869 19.827  1.00 32.80 ? 66  PHE B CA  1 
ATOM   2098 C C   . PHE B 1 64  ? 9.779   -22.970 19.223  1.00 33.77 ? 66  PHE B C   1 
ATOM   2099 O O   . PHE B 1 64  ? 9.272   -22.061 19.869  1.00 33.64 ? 66  PHE B O   1 
ATOM   2100 C CB  . PHE B 1 64  ? 10.254  -25.243 20.207  1.00 31.50 ? 66  PHE B CB  1 
ATOM   2101 C CG  . PHE B 1 64  ? 9.182   -25.167 21.271  1.00 29.76 ? 66  PHE B CG  1 
ATOM   2102 C CD1 . PHE B 1 64  ? 7.858   -24.949 20.932  1.00 30.03 ? 66  PHE B CD1 1 
ATOM   2103 C CD2 . PHE B 1 64  ? 9.502   -25.273 22.601  1.00 29.75 ? 66  PHE B CD2 1 
ATOM   2104 C CE1 . PHE B 1 64  ? 6.884   -24.851 21.908  1.00 29.85 ? 66  PHE B CE1 1 
ATOM   2105 C CE2 . PHE B 1 64  ? 8.535   -25.151 23.573  1.00 30.64 ? 66  PHE B CE2 1 
ATOM   2106 C CZ  . PHE B 1 64  ? 7.225   -24.969 23.225  1.00 29.79 ? 66  PHE B CZ  1 
ATOM   2107 N N   . ASP B 1 65  ? 9.439   -23.229 17.965  1.00 35.45 ? 67  ASP B N   1 
ATOM   2108 C CA  . ASP B 1 65  ? 8.428   -22.460 17.261  1.00 36.15 ? 67  ASP B CA  1 
ATOM   2109 C C   . ASP B 1 65  ? 7.671   -23.267 16.221  1.00 36.16 ? 67  ASP B C   1 
ATOM   2110 O O   . ASP B 1 65  ? 7.122   -22.689 15.286  1.00 37.00 ? 67  ASP B O   1 
ATOM   2111 C CB  . ASP B 1 65  ? 9.040   -21.191 16.678  1.00 39.51 ? 67  ASP B CB  1 
ATOM   2112 C CG  . ASP B 1 65  ? 10.150  -21.373 15.664  1.00 49.20 ? 67  ASP B CG  1 
ATOM   2113 O OD1 . ASP B 1 65  ? 10.612  -22.503 15.490  1.00 51.58 ? 67  ASP B OD1 1 
ATOM   2114 O OD2 . ASP B 1 65  ? 10.553  -20.377 15.056  1.00 54.49 ? 67  ASP B OD2 1 
ATOM   2115 N N   . THR B 1 66  ? 7.619   -24.595 16.382  1.00 36.27 ? 68  THR B N   1 
ATOM   2116 C CA  . THR B 1 66  ? 6.749   -25.460 15.621  1.00 35.81 ? 68  THR B CA  1 
ATOM   2117 C C   . THR B 1 66  ? 6.043   -26.424 16.592  1.00 35.04 ? 68  THR B C   1 
ATOM   2118 O O   . THR B 1 66  ? 6.526   -26.680 17.709  1.00 33.40 ? 68  THR B O   1 
ATOM   2119 C CB  . THR B 1 66  ? 7.500   -26.238 14.535  1.00 37.20 ? 68  THR B CB  1 
ATOM   2120 O OG1 . THR B 1 66  ? 8.243   -27.304 15.132  1.00 39.57 ? 68  THR B OG1 1 
ATOM   2121 C CG2 . THR B 1 66  ? 8.389   -25.361 13.673  1.00 37.07 ? 68  THR B CG2 1 
ATOM   2122 N N   . VAL B 1 67  ? 4.901   -26.965 16.124  1.00 35.36 ? 69  VAL B N   1 
ATOM   2123 C CA  . VAL B 1 67  ? 4.118   -27.974 16.843  1.00 35.79 ? 69  VAL B CA  1 
ATOM   2124 C C   . VAL B 1 67  ? 4.980   -29.212 17.078  1.00 37.05 ? 69  VAL B C   1 
ATOM   2125 O O   . VAL B 1 67  ? 4.964   -29.761 18.169  1.00 37.31 ? 69  VAL B O   1 
ATOM   2126 C CB  . VAL B 1 67  ? 2.838   -28.329 16.057  1.00 35.56 ? 69  VAL B CB  1 
ATOM   2127 C CG1 . VAL B 1 67  ? 2.116   -29.483 16.708  1.00 36.50 ? 69  VAL B CG1 1 
ATOM   2128 C CG2 . VAL B 1 67  ? 1.907   -27.128 15.891  1.00 34.78 ? 69  VAL B CG2 1 
ATOM   2129 N N   . GLU B 1 68  ? 5.734   -29.648 16.048  1.00 37.58 ? 70  GLU B N   1 
ATOM   2130 C CA  . GLU B 1 68  ? 6.571   -30.843 16.099  1.00 38.00 ? 70  GLU B CA  1 
ATOM   2131 C C   . GLU B 1 68  ? 7.734   -30.707 17.084  1.00 37.91 ? 70  GLU B C   1 
ATOM   2132 O O   . GLU B 1 68  ? 8.053   -31.667 17.793  1.00 38.29 ? 70  GLU B O   1 
ATOM   2133 C CB  . GLU B 1 68  ? 7.128   -31.180 14.684  1.00 41.91 ? 70  GLU B CB  1 
ATOM   2134 C CG  . GLU B 1 68  ? 6.067   -31.691 13.720  1.00 46.95 ? 70  GLU B CG  1 
ATOM   2135 C CD  . GLU B 1 68  ? 5.153   -30.635 13.142  1.00 54.68 ? 70  GLU B CD  1 
ATOM   2136 O OE1 . GLU B 1 68  ? 5.469   -29.425 13.279  1.00 54.34 ? 70  GLU B OE1 1 
ATOM   2137 O OE2 . GLU B 1 68  ? 4.114   -31.022 12.552  1.00 55.73 ? 70  GLU B OE2 1 
ATOM   2138 N N   . ASP B 1 69  ? 8.378   -29.541 17.129  1.00 37.05 ? 71  ASP B N   1 
ATOM   2139 C CA  . ASP B 1 69  ? 9.456   -29.316 18.097  1.00 36.51 ? 71  ASP B CA  1 
ATOM   2140 C C   . ASP B 1 69  ? 8.934   -29.171 19.539  1.00 34.35 ? 71  ASP B C   1 
ATOM   2141 O O   . ASP B 1 69  ? 9.631   -29.551 20.483  1.00 33.52 ? 71  ASP B O   1 
ATOM   2142 C CB  . ASP B 1 69  ? 10.289  -28.123 17.681  1.00 38.41 ? 71  ASP B CB  1 
ATOM   2143 C CG  . ASP B 1 69  ? 10.923  -28.365 16.327  1.00 42.35 ? 71  ASP B CG  1 
ATOM   2144 O OD1 . ASP B 1 69  ? 11.362  -29.514 16.072  1.00 43.02 ? 71  ASP B OD1 1 
ATOM   2145 O OD2 . ASP B 1 69  ? 10.961  -27.420 15.522  1.00 43.99 ? 71  ASP B OD2 1 
ATOM   2146 N N   . PHE B 1 70  ? 7.709   -28.641 19.711  1.00 33.07 ? 72  PHE B N   1 
ATOM   2147 C CA  . PHE B 1 70  ? 7.022   -28.733 21.003  1.00 31.38 ? 72  PHE B CA  1 
ATOM   2148 C C   . PHE B 1 70  ? 6.883   -30.185 21.461  1.00 31.28 ? 72  PHE B C   1 
ATOM   2149 O O   . PHE B 1 70  ? 7.281   -30.506 22.569  1.00 32.01 ? 72  PHE B O   1 
ATOM   2150 C CB  . PHE B 1 70  ? 5.637   -28.063 20.955  1.00 29.39 ? 72  PHE B CB  1 
ATOM   2151 C CG  . PHE B 1 70  ? 4.795   -28.439 22.149  1.00 28.00 ? 72  PHE B CG  1 
ATOM   2152 C CD1 . PHE B 1 70  ? 4.994   -27.837 23.367  1.00 27.63 ? 72  PHE B CD1 1 
ATOM   2153 C CD2 . PHE B 1 70  ? 3.818   -29.423 22.052  1.00 28.25 ? 72  PHE B CD2 1 
ATOM   2154 C CE1 . PHE B 1 70  ? 4.243   -28.202 24.464  1.00 27.99 ? 72  PHE B CE1 1 
ATOM   2155 C CE2 . PHE B 1 70  ? 3.057   -29.777 23.152  1.00 28.69 ? 72  PHE B CE2 1 
ATOM   2156 C CZ  . PHE B 1 70  ? 3.286   -29.187 24.353  1.00 27.92 ? 72  PHE B CZ  1 
ATOM   2157 N N   . TRP B 1 71  ? 6.317   -31.054 20.608  1.00 31.66 ? 73  TRP B N   1 
ATOM   2158 C CA  . TRP B 1 71  ? 6.108   -32.419 20.975  1.00 32.77 ? 73  TRP B CA  1 
ATOM   2159 C C   . TRP B 1 71  ? 7.425   -33.166 21.166  1.00 33.56 ? 73  TRP B C   1 
ATOM   2160 O O   . TRP B 1 71  ? 7.475   -33.973 22.055  1.00 33.43 ? 73  TRP B O   1 
ATOM   2161 C CB  . TRP B 1 71  ? 5.203   -33.169 19.979  1.00 32.94 ? 73  TRP B CB  1 
ATOM   2162 C CG  . TRP B 1 71  ? 3.737   -32.829 20.106  1.00 31.99 ? 73  TRP B CG  1 
ATOM   2163 C CD1 . TRP B 1 71  ? 2.948   -32.312 19.134  1.00 32.39 ? 73  TRP B CD1 1 
ATOM   2164 C CD2 . TRP B 1 71  ? 2.883   -33.026 21.251  1.00 30.82 ? 73  TRP B CD2 1 
ATOM   2165 N NE1 . TRP B 1 71  ? 1.655   -32.209 19.580  1.00 32.16 ? 73  TRP B NE1 1 
ATOM   2166 C CE2 . TRP B 1 71  ? 1.593   -32.611 20.882  1.00 31.12 ? 73  TRP B CE2 1 
ATOM   2167 C CE3 . TRP B 1 71  ? 3.085   -33.522 22.541  1.00 30.28 ? 73  TRP B CE3 1 
ATOM   2168 C CZ2 . TRP B 1 71  ? 0.516   -32.657 21.752  1.00 31.55 ? 73  TRP B CZ2 1 
ATOM   2169 C CZ3 . TRP B 1 71  ? 2.016   -33.552 23.409  1.00 31.69 ? 73  TRP B CZ3 1 
ATOM   2170 C CH2 . TRP B 1 71  ? 0.750   -33.127 23.019  1.00 31.32 ? 73  TRP B CH2 1 
ATOM   2171 N N   . ALA B 1 72  ? 8.482   -32.917 20.362  1.00 34.43 ? 74  ALA B N   1 
ATOM   2172 C CA  . ALA B 1 72  ? 9.777   -33.596 20.629  1.00 35.74 ? 74  ALA B CA  1 
ATOM   2173 C C   . ALA B 1 72  ? 10.302  -33.225 22.031  1.00 34.67 ? 74  ALA B C   1 
ATOM   2174 O O   . ALA B 1 72  ? 10.778  -34.090 22.772  1.00 34.50 ? 74  ALA B O   1 
ATOM   2175 C CB  . ALA B 1 72  ? 10.803  -33.241 19.572  1.00 37.61 ? 74  ALA B CB  1 
ATOM   2176 N N   . LEU B 1 73  ? 10.195  -31.955 22.398  1.00 32.84 ? 75  LEU B N   1 
ATOM   2177 C CA  . LEU B 1 73  ? 10.591  -31.478 23.720  1.00 32.30 ? 75  LEU B CA  1 
ATOM   2178 C C   . LEU B 1 73  ? 9.703   -32.032 24.848  1.00 31.69 ? 75  LEU B C   1 
ATOM   2179 O O   . LEU B 1 73  ? 10.220  -32.475 25.870  1.00 30.42 ? 75  LEU B O   1 
ATOM   2180 C CB  . LEU B 1 73  ? 10.546  -29.924 23.749  1.00 32.30 ? 75  LEU B CB  1 
ATOM   2181 C CG  . LEU B 1 73  ? 10.970  -29.274 25.049  1.00 33.60 ? 75  LEU B CG  1 
ATOM   2182 C CD1 . LEU B 1 73  ? 12.396  -29.658 25.421  1.00 34.87 ? 75  LEU B CD1 1 
ATOM   2183 C CD2 . LEU B 1 73  ? 10.840  -27.783 24.985  1.00 33.97 ? 75  LEU B CD2 1 
ATOM   2184 N N   . TYR B 1 74  ? 8.369   -31.997 24.664  1.00 31.60 ? 76  TYR B N   1 
ATOM   2185 C CA  . TYR B 1 74  ? 7.418   -32.576 25.616  1.00 31.55 ? 76  TYR B CA  1 
ATOM   2186 C C   . TYR B 1 74  ? 7.639   -34.091 25.812  1.00 32.62 ? 76  TYR B C   1 
ATOM   2187 O O   . TYR B 1 74  ? 7.681   -34.555 26.946  1.00 31.03 ? 76  TYR B O   1 
ATOM   2188 C CB  . TYR B 1 74  ? 5.972   -32.320 25.150  1.00 31.21 ? 76  TYR B CB  1 
ATOM   2189 C CG  . TYR B 1 74  ? 4.957   -32.791 26.174  1.00 31.75 ? 76  TYR B CG  1 
ATOM   2190 C CD1 . TYR B 1 74  ? 4.531   -31.951 27.203  1.00 32.24 ? 76  TYR B CD1 1 
ATOM   2191 C CD2 . TYR B 1 74  ? 4.449   -34.087 26.137  1.00 32.12 ? 76  TYR B CD2 1 
ATOM   2192 C CE1 . TYR B 1 74  ? 3.611   -32.381 28.145  1.00 33.27 ? 76  TYR B CE1 1 
ATOM   2193 C CE2 . TYR B 1 74  ? 3.564   -34.542 27.102  1.00 32.94 ? 76  TYR B CE2 1 
ATOM   2194 C CZ  . TYR B 1 74  ? 3.132   -33.686 28.095  1.00 34.65 ? 76  TYR B CZ  1 
ATOM   2195 O OH  . TYR B 1 74  ? 2.235   -34.165 29.032  1.00 37.17 ? 76  TYR B OH  1 
ATOM   2196 N N   . ASN B 1 75  ? 7.787   -34.849 24.692  1.00 35.47 ? 77  ASN B N   1 
ATOM   2197 C CA  . ASN B 1 75  ? 7.998   -36.307 24.740  1.00 38.33 ? 77  ASN B CA  1 
ATOM   2198 C C   . ASN B 1 75  ? 9.321   -36.589 25.417  1.00 40.08 ? 77  ASN B C   1 
ATOM   2199 O O   . ASN B 1 75  ? 9.374   -37.445 26.299  1.00 42.28 ? 77  ASN B O   1 
ATOM   2200 C CB  . ASN B 1 75  ? 7.980   -36.941 23.343  1.00 40.36 ? 77  ASN B CB  1 
ATOM   2201 C CG  . ASN B 1 75  ? 6.606   -37.008 22.714  1.00 45.78 ? 77  ASN B CG  1 
ATOM   2202 O OD1 . ASN B 1 75  ? 5.577   -37.027 23.414  1.00 48.81 ? 77  ASN B OD1 1 
ATOM   2203 N ND2 . ASN B 1 75  ? 6.547   -37.043 21.374  1.00 45.80 ? 77  ASN B ND2 1 
ATOM   2204 N N   . HIS B 1 76  ? 10.391  -35.879 25.038  1.00 39.78 ? 78  HIS B N   1 
ATOM   2205 C CA  . HIS B 1 76  ? 11.662  -35.977 25.748  1.00 40.15 ? 78  HIS B CA  1 
ATOM   2206 C C   . HIS B 1 76  ? 11.524  -35.745 27.276  1.00 39.64 ? 78  HIS B C   1 
ATOM   2207 O O   . HIS B 1 76  ? 11.789  -36.667 28.028  1.00 38.97 ? 78  HIS B O   1 
ATOM   2208 C CB  . HIS B 1 76  ? 12.715  -35.056 25.138  1.00 42.09 ? 78  HIS B CB  1 
ATOM   2209 C CG  . HIS B 1 76  ? 14.043  -35.189 25.812  1.00 47.51 ? 78  HIS B CG  1 
ATOM   2210 N ND1 . HIS B 1 76  ? 14.548  -34.188 26.631  1.00 50.32 ? 78  HIS B ND1 1 
ATOM   2211 C CD2 . HIS B 1 76  ? 14.921  -36.219 25.786  1.00 49.77 ? 78  HIS B CD2 1 
ATOM   2212 C CE1 . HIS B 1 76  ? 15.716  -34.639 27.073  1.00 51.00 ? 78  HIS B CE1 1 
ATOM   2213 N NE2 . HIS B 1 76  ? 15.986  -35.852 26.583  1.00 51.46 ? 78  HIS B NE2 1 
ATOM   2214 N N   . ILE B 1 77  ? 11.081  -34.542 27.734  1.00 40.05 ? 79  ILE B N   1 
ATOM   2215 C CA  . ILE B 1 77  ? 10.929  -34.225 29.159  1.00 40.96 ? 79  ILE B CA  1 
ATOM   2216 C C   . ILE B 1 77  ? 10.047  -35.280 29.873  1.00 43.00 ? 79  ILE B C   1 
ATOM   2217 O O   . ILE B 1 77  ? 10.322  -35.638 31.026  1.00 42.03 ? 79  ILE B O   1 
ATOM   2218 C CB  . ILE B 1 77  ? 10.353  -32.795 29.354  1.00 40.77 ? 79  ILE B CB  1 
ATOM   2219 C CG1 . ILE B 1 77  ? 11.316  -31.680 28.772  1.00 41.76 ? 79  ILE B CG1 1 
ATOM   2220 C CG2 . ILE B 1 77  ? 9.995   -32.534 30.820  1.00 40.76 ? 79  ILE B CG2 1 
ATOM   2221 C CD1 . ILE B 1 77  ? 12.300  -30.999 29.732  1.00 43.53 ? 79  ILE B CD1 1 
ATOM   2222 N N   . GLN B 1 78  ? 8.984   -35.771 29.189  1.00 44.73 ? 80  GLN B N   1 
ATOM   2223 C CA  . GLN B 1 78  ? 8.074   -36.745 29.791  1.00 45.62 ? 80  GLN B CA  1 
ATOM   2224 C C   . GLN B 1 78  ? 8.780   -38.055 30.042  1.00 49.29 ? 80  GLN B C   1 
ATOM   2225 O O   . GLN B 1 78  ? 8.512   -38.670 31.052  1.00 48.72 ? 80  GLN B O   1 
ATOM   2226 C CB  . GLN B 1 78  ? 6.841   -37.001 28.923  1.00 44.27 ? 80  GLN B CB  1 
ATOM   2227 C CG  . GLN B 1 78  ? 5.802   -37.931 29.570  1.00 42.52 ? 80  GLN B CG  1 
ATOM   2228 C CD  . GLN B 1 78  ? 4.513   -37.952 28.778  1.00 40.09 ? 80  GLN B CD  1 
ATOM   2229 O OE1 . GLN B 1 78  ? 4.533   -38.204 27.579  1.00 40.79 ? 80  GLN B OE1 1 
ATOM   2230 N NE2 . GLN B 1 78  ? 3.355   -37.686 29.428  1.00 37.79 ? 80  GLN B NE2 1 
ATOM   2231 N N   . LEU B 1 79  ? 9.664   -38.488 29.135  1.00 53.01 ? 81  LEU B N   1 
ATOM   2232 C CA  . LEU B 1 79  ? 10.421  -39.737 29.288  1.00 56.46 ? 81  LEU B CA  1 
ATOM   2233 C C   . LEU B 1 79  ? 11.598  -39.580 30.252  1.00 59.60 ? 81  LEU B C   1 
ATOM   2234 O O   . LEU B 1 79  ? 11.868  -40.491 31.031  1.00 59.93 ? 81  LEU B O   1 
ATOM   2235 C CB  . LEU B 1 79  ? 10.936  -40.213 27.909  1.00 57.06 ? 81  LEU B CB  1 
ATOM   2236 C CG  . LEU B 1 79  ? 9.853   -40.557 26.866  1.00 59.18 ? 81  LEU B CG  1 
ATOM   2237 C CD1 . LEU B 1 79  ? 10.479  -40.868 25.504  1.00 59.32 ? 81  LEU B CD1 1 
ATOM   2238 C CD2 . LEU B 1 79  ? 8.937   -41.707 27.347  1.00 60.49 ? 81  LEU B CD2 1 
ATOM   2239 N N   . SER B 1 80  ? 12.275  -38.433 30.219  1.00 61.46 ? 82  SER B N   1 
ATOM   2240 C CA  . SER B 1 80  ? 13.574  -38.272 30.861  1.00 63.37 ? 82  SER B CA  1 
ATOM   2241 C C   . SER B 1 80  ? 13.540  -37.630 32.245  1.00 64.71 ? 82  SER B C   1 
ATOM   2242 O O   . SER B 1 80  ? 14.377  -37.985 33.073  1.00 65.18 ? 82  SER B O   1 
ATOM   2243 C CB  . SER B 1 80  ? 14.503  -37.463 29.955  1.00 65.79 ? 82  SER B CB  1 
ATOM   2244 O OG  . SER B 1 80  ? 14.002  -36.154 29.730  1.00 70.34 ? 82  SER B OG  1 
ATOM   2245 N N   . SER B 1 81  ? 12.613  -36.706 32.520  1.00 65.72 ? 83  SER B N   1 
ATOM   2246 C CA  . SER B 1 81  ? 12.781  -35.810 33.675  1.00 67.39 ? 83  SER B CA  1 
ATOM   2247 C C   . SER B 1 81  ? 12.109  -36.304 34.945  1.00 67.91 ? 83  SER B C   1 
ATOM   2248 O O   . SER B 1 81  ? 11.098  -36.998 34.871  1.00 67.90 ? 83  SER B O   1 
ATOM   2249 C CB  . SER B 1 81  ? 12.285  -34.407 33.337  1.00 69.56 ? 83  SER B CB  1 
ATOM   2250 O OG  . SER B 1 81  ? 13.066  -33.850 32.287  1.00 73.13 ? 83  SER B OG  1 
ATOM   2251 N N   . ASN B 1 82  ? 12.678  -35.943 36.111  1.00 68.14 ? 84  ASN B N   1 
ATOM   2252 C CA  . ASN B 1 82  ? 12.087  -36.246 37.423  1.00 69.03 ? 84  ASN B CA  1 
ATOM   2253 C C   . ASN B 1 82  ? 11.324  -35.053 37.982  1.00 68.41 ? 84  ASN B C   1 
ATOM   2254 O O   . ASN B 1 82  ? 11.692  -33.907 37.703  1.00 69.24 ? 84  ASN B O   1 
ATOM   2255 C CB  . ASN B 1 82  ? 13.172  -36.613 38.445  1.00 71.39 ? 84  ASN B CB  1 
ATOM   2256 C CG  . ASN B 1 82  ? 13.833  -37.957 38.231  1.00 76.34 ? 84  ASN B CG  1 
ATOM   2257 O OD1 . ASN B 1 82  ? 13.811  -38.820 39.115  1.00 78.29 ? 84  ASN B OD1 1 
ATOM   2258 N ND2 . ASN B 1 82  ? 14.446  -38.171 37.072  1.00 76.77 ? 84  ASN B ND2 1 
ATOM   2259 N N   . LEU B 1 83  ? 10.286  -35.325 38.791  1.00 66.92 ? 85  LEU B N   1 
ATOM   2260 C CA  . LEU B 1 83  ? 9.403   -34.319 39.372  1.00 66.32 ? 85  LEU B CA  1 
ATOM   2261 C C   . LEU B 1 83  ? 9.799   -33.995 40.816  1.00 65.32 ? 85  LEU B C   1 
ATOM   2262 O O   . LEU B 1 83  ? 9.303   -34.638 41.732  1.00 65.23 ? 85  LEU B O   1 
ATOM   2263 C CB  . LEU B 1 83  ? 7.962   -34.858 39.339  1.00 66.25 ? 85  LEU B CB  1 
ATOM   2264 C CG  . LEU B 1 83  ? 6.871   -33.920 39.856  1.00 66.44 ? 85  LEU B CG  1 
ATOM   2265 C CD1 . LEU B 1 83  ? 6.616   -32.775 38.865  1.00 66.90 ? 85  LEU B CD1 1 
ATOM   2266 C CD2 . LEU B 1 83  ? 5.601   -34.684 40.133  1.00 66.17 ? 85  LEU B CD2 1 
ATOM   2267 N N   . MET B 1 84  ? 10.668  -33.000 41.023  1.00 65.10 ? 86  MET B N   1 
ATOM   2268 C CA  . MET B 1 84  ? 11.153  -32.687 42.373  1.00 65.65 ? 86  MET B CA  1 
ATOM   2269 C C   . MET B 1 84  ? 10.315  -31.530 42.906  1.00 64.93 ? 86  MET B C   1 
ATOM   2270 O O   . MET B 1 84  ? 10.184  -30.513 42.210  1.00 65.42 ? 86  MET B O   1 
ATOM   2271 C CB  . MET B 1 84  ? 12.648  -32.293 42.404  1.00 66.98 ? 86  MET B CB  1 
ATOM   2272 C CG  . MET B 1 84  ? 13.537  -33.024 41.409  1.00 70.66 ? 86  MET B CG  1 
ATOM   2273 S SD  . MET B 1 84  ? 15.297  -32.592 41.642  1.00 78.28 ? 86  MET B SD  1 
ATOM   2274 C CE  . MET B 1 84  ? 15.750  -32.200 39.991  1.00 75.43 ? 86  MET B CE  1 
ATOM   2275 N N   . PRO B 1 85  ? 9.727   -31.637 44.111  1.00 63.40 ? 87  PRO B N   1 
ATOM   2276 C CA  . PRO B 1 85  ? 9.173   -30.422 44.737  1.00 62.25 ? 87  PRO B CA  1 
ATOM   2277 C C   . PRO B 1 85  ? 10.236  -29.345 44.979  1.00 60.83 ? 87  PRO B C   1 
ATOM   2278 O O   . PRO B 1 85  ? 11.441  -29.610 44.971  1.00 60.08 ? 87  PRO B O   1 
ATOM   2279 C CB  . PRO B 1 85  ? 8.519   -30.918 46.031  1.00 63.69 ? 87  PRO B CB  1 
ATOM   2280 C CG  . PRO B 1 85  ? 8.448   -32.445 45.915  1.00 64.56 ? 87  PRO B CG  1 
ATOM   2281 C CD  . PRO B 1 85  ? 9.523   -32.848 44.942  1.00 63.11 ? 87  PRO B CD  1 
ATOM   2282 N N   . GLY B 1 86  ? 9.760   -28.123 45.175  1.00 60.02 ? 88  GLY B N   1 
ATOM   2283 C CA  . GLY B 1 86  ? 10.592  -26.931 45.261  1.00 59.18 ? 88  GLY B CA  1 
ATOM   2284 C C   . GLY B 1 86  ? 10.936  -26.323 43.909  1.00 57.62 ? 88  GLY B C   1 
ATOM   2285 O O   . GLY B 1 86  ? 11.374  -25.167 43.856  1.00 57.65 ? 88  GLY B O   1 
ATOM   2286 N N   . CYS B 1 87  ? 10.741  -27.092 42.807  1.00 55.67 ? 89  CYS B N   1 
ATOM   2287 C CA  . CYS B 1 87  ? 11.122  -26.681 41.467  1.00 55.24 ? 89  CYS B CA  1 
ATOM   2288 C C   . CYS B 1 87  ? 9.940   -26.027 40.692  1.00 52.53 ? 89  CYS B C   1 
ATOM   2289 O O   . CYS B 1 87  ? 8.764   -26.219 41.016  1.00 53.08 ? 89  CYS B O   1 
ATOM   2290 C CB  . CYS B 1 87  ? 11.704  -27.864 40.709  1.00 58.52 ? 89  CYS B CB  1 
ATOM   2291 S SG  . CYS B 1 87  ? 13.190  -28.567 41.480  1.00 71.20 ? 89  CYS B SG  1 
ATOM   2292 N N   . ASP B 1 88  ? 10.267  -25.232 39.684  1.00 48.75 ? 90  ASP B N   1 
ATOM   2293 C CA  . ASP B 1 88  ? 9.284   -24.549 38.864  1.00 45.28 ? 90  ASP B CA  1 
ATOM   2294 C C   . ASP B 1 88  ? 9.705   -24.700 37.427  1.00 41.19 ? 90  ASP B C   1 
ATOM   2295 O O   . ASP B 1 88  ? 10.904  -24.636 37.112  1.00 39.29 ? 90  ASP B O   1 
ATOM   2296 C CB  . ASP B 1 88  ? 9.197   -23.046 39.184  1.00 47.54 ? 90  ASP B CB  1 
ATOM   2297 C CG  . ASP B 1 88  ? 9.096   -22.688 40.661  1.00 51.59 ? 90  ASP B CG  1 
ATOM   2298 O OD1 . ASP B 1 88  ? 8.454   -23.452 41.413  1.00 53.71 ? 90  ASP B OD1 1 
ATOM   2299 O OD2 . ASP B 1 88  ? 9.650   -21.634 41.059  1.00 51.09 ? 90  ASP B OD2 1 
ATOM   2300 N N   . TYR B 1 89  ? 8.715   -24.916 36.548  1.00 38.55 ? 91  TYR B N   1 
ATOM   2301 C CA  . TYR B 1 89  ? 8.891   -24.872 35.102  1.00 36.12 ? 91  TYR B CA  1 
ATOM   2302 C C   . TYR B 1 89  ? 8.000   -23.782 34.530  1.00 32.01 ? 91  TYR B C   1 
ATOM   2303 O O   . TYR B 1 89  ? 6.903   -23.511 35.048  1.00 30.72 ? 91  TYR B O   1 
ATOM   2304 C CB  . TYR B 1 89  ? 8.488   -26.197 34.458  1.00 37.76 ? 91  TYR B CB  1 
ATOM   2305 C CG  . TYR B 1 89  ? 9.463   -27.322 34.672  1.00 40.32 ? 91  TYR B CG  1 
ATOM   2306 C CD1 . TYR B 1 89  ? 9.386   -28.126 35.793  1.00 41.09 ? 91  TYR B CD1 1 
ATOM   2307 C CD2 . TYR B 1 89  ? 10.468  -27.577 33.753  1.00 42.74 ? 91  TYR B CD2 1 
ATOM   2308 C CE1 . TYR B 1 89  ? 10.279  -29.159 36.000  1.00 43.24 ? 91  TYR B CE1 1 
ATOM   2309 C CE2 . TYR B 1 89  ? 11.362  -28.618 33.939  1.00 43.68 ? 91  TYR B CE2 1 
ATOM   2310 C CZ  . TYR B 1 89  ? 11.272  -29.404 35.073  1.00 45.00 ? 91  TYR B CZ  1 
ATOM   2311 O OH  . TYR B 1 89  ? 12.152  -30.451 35.290  1.00 47.43 ? 91  TYR B OH  1 
ATOM   2312 N N   . SER B 1 90  ? 8.459   -23.180 33.466  1.00 30.03 ? 92  SER B N   1 
ATOM   2313 C CA  . SER B 1 90  ? 7.769   -22.057 32.834  1.00 29.01 ? 92  SER B CA  1 
ATOM   2314 C C   . SER B 1 90  ? 7.957   -22.089 31.362  1.00 27.46 ? 92  SER B C   1 
ATOM   2315 O O   . SER B 1 90  ? 9.097   -22.254 30.897  1.00 26.34 ? 92  SER B O   1 
ATOM   2316 C CB  . SER B 1 90  ? 8.309   -20.720 33.305  1.00 30.72 ? 92  SER B CB  1 
ATOM   2317 O OG  . SER B 1 90  ? 8.152   -20.507 34.683  1.00 35.69 ? 92  SER B OG  1 
ATOM   2318 N N   . LEU B 1 91  ? 6.870   -21.885 30.628  1.00 25.95 ? 93  LEU B N   1 
ATOM   2319 C CA  . LEU B 1 91  ? 6.930   -21.681 29.208  1.00 25.03 ? 93  LEU B CA  1 
ATOM   2320 C C   . LEU B 1 91  ? 6.487   -20.262 28.954  1.00 24.96 ? 93  LEU B C   1 
ATOM   2321 O O   . LEU B 1 91  ? 5.342   -19.916 29.259  1.00 24.42 ? 93  LEU B O   1 
ATOM   2322 C CB  . LEU B 1 91  ? 6.021   -22.643 28.430  1.00 25.18 ? 93  LEU B CB  1 
ATOM   2323 C CG  . LEU B 1 91  ? 6.235   -22.617 26.896  1.00 26.48 ? 93  LEU B CG  1 
ATOM   2324 C CD1 . LEU B 1 91  ? 7.544   -23.327 26.501  1.00 27.41 ? 93  LEU B CD1 1 
ATOM   2325 C CD2 . LEU B 1 91  ? 5.051   -23.211 26.126  1.00 26.08 ? 93  LEU B CD2 1 
ATOM   2326 N N   . PHE B 1 92  ? 7.382   -19.440 28.410  1.00 24.84 ? 94  PHE B N   1 
ATOM   2327 C CA  . PHE B 1 92  ? 7.096   -18.015 28.158  1.00 25.53 ? 94  PHE B CA  1 
ATOM   2328 C C   . PHE B 1 92  ? 7.446   -17.675 26.769  1.00 25.58 ? 94  PHE B C   1 
ATOM   2329 O O   . PHE B 1 92  ? 8.326   -18.288 26.179  1.00 25.43 ? 94  PHE B O   1 
ATOM   2330 C CB  . PHE B 1 92  ? 7.868   -17.084 29.121  1.00 26.40 ? 94  PHE B CB  1 
ATOM   2331 C CG  . PHE B 1 92  ? 7.155   -16.855 30.435  1.00 26.92 ? 94  PHE B CG  1 
ATOM   2332 C CD1 . PHE B 1 92  ? 7.012   -17.884 31.351  1.00 27.03 ? 94  PHE B CD1 1 
ATOM   2333 C CD2 . PHE B 1 92  ? 6.593   -15.631 30.730  1.00 27.93 ? 94  PHE B CD2 1 
ATOM   2334 C CE1 . PHE B 1 92  ? 6.308   -17.689 32.526  1.00 28.00 ? 94  PHE B CE1 1 
ATOM   2335 C CE2 . PHE B 1 92  ? 5.905   -15.434 31.915  1.00 28.10 ? 94  PHE B CE2 1 
ATOM   2336 C CZ  . PHE B 1 92  ? 5.759   -16.460 32.800  1.00 27.76 ? 94  PHE B CZ  1 
ATOM   2337 N N   . LYS B 1 93  ? 6.746   -16.679 26.193  1.00 26.87 ? 95  LYS B N   1 
ATOM   2338 C CA  . LYS B 1 93  ? 7.095   -16.185 24.869  1.00 26.04 ? 95  LYS B CA  1 
ATOM   2339 C C   . LYS B 1 93  ? 8.562   -15.712 24.851  1.00 27.67 ? 95  LYS B C   1 
ATOM   2340 O O   . LYS B 1 93  ? 9.106   -15.197 25.834  1.00 27.20 ? 95  LYS B O   1 
ATOM   2341 C CB  . LYS B 1 93  ? 6.155   -15.082 24.398  1.00 23.72 ? 95  LYS B CB  1 
ATOM   2342 C CG  . LYS B 1 93  ? 4.750   -15.533 24.171  1.00 22.57 ? 95  LYS B CG  1 
ATOM   2343 C CD  . LYS B 1 93  ? 3.823   -14.385 23.946  1.00 24.81 ? 95  LYS B CD  1 
ATOM   2344 C CE  . LYS B 1 93  ? 2.469   -14.854 23.491  1.00 27.85 ? 95  LYS B CE  1 
ATOM   2345 N NZ  . LYS B 1 93  ? 1.518   -13.735 23.440  1.00 24.89 ? 95  LYS B NZ  1 
ATOM   2346 N N   . ASP B 1 94  ? 9.191   -15.920 23.715  1.00 29.11 ? 96  ASP B N   1 
ATOM   2347 C CA  . ASP B 1 94  ? 10.583  -15.550 23.487  1.00 31.17 ? 96  ASP B CA  1 
ATOM   2348 C C   . ASP B 1 94  ? 10.772  -14.054 23.797  1.00 32.92 ? 96  ASP B C   1 
ATOM   2349 O O   . ASP B 1 94  ? 10.027  -13.227 23.270  1.00 32.53 ? 96  ASP B O   1 
ATOM   2350 C CB  . ASP B 1 94  ? 10.949  -15.881 22.027  1.00 33.73 ? 96  ASP B CB  1 
ATOM   2351 C CG  . ASP B 1 94  ? 12.429  -15.947 21.688  1.00 40.49 ? 96  ASP B CG  1 
ATOM   2352 O OD1 . ASP B 1 94  ? 13.251  -16.032 22.619  1.00 40.29 ? 96  ASP B OD1 1 
ATOM   2353 O OD2 . ASP B 1 94  ? 12.758  -15.935 20.490  1.00 44.16 ? 96  ASP B OD2 1 
ATOM   2354 N N   . GLY B 1 95  ? 11.709  -13.773 24.707  1.00 34.16 ? 97  GLY B N   1 
ATOM   2355 C CA  . GLY B 1 95  ? 12.065  -12.429 25.121  1.00 35.29 ? 97  GLY B CA  1 
ATOM   2356 C C   . GLY B 1 95  ? 11.367  -11.920 26.362  1.00 35.99 ? 97  GLY B C   1 
ATOM   2357 O O   . GLY B 1 95  ? 11.541  -10.755 26.704  1.00 37.02 ? 97  GLY B O   1 
ATOM   2358 N N   . ILE B 1 96  ? 10.577  -12.754 27.035  1.00 35.39 ? 98  ILE B N   1 
ATOM   2359 C CA  . ILE B 1 96  ? 9.985   -12.477 28.335  1.00 36.00 ? 98  ILE B CA  1 
ATOM   2360 C C   . ILE B 1 96  ? 10.612  -13.463 29.332  1.00 38.08 ? 98  ILE B C   1 
ATOM   2361 O O   . ILE B 1 96  ? 10.444  -14.688 29.197  1.00 38.43 ? 98  ILE B O   1 
ATOM   2362 C CB  . ILE B 1 96  ? 8.439   -12.637 28.333  1.00 35.60 ? 98  ILE B CB  1 
ATOM   2363 C CG1 . ILE B 1 96  ? 7.776   -11.826 27.193  1.00 36.52 ? 98  ILE B CG1 1 
ATOM   2364 C CG2 . ILE B 1 96  ? 7.860   -12.280 29.719  1.00 35.13 ? 98  ILE B CG2 1 
ATOM   2365 C CD1 . ILE B 1 96  ? 6.209   -11.948 27.144  1.00 37.93 ? 98  ILE B CD1 1 
ATOM   2366 N N   . GLU B 1 97  ? 11.312  -12.930 30.323  1.00 39.55 ? 99  GLU B N   1 
ATOM   2367 C CA  . GLU B 1 97  ? 11.777  -13.745 31.427  1.00 42.77 ? 99  GLU B CA  1 
ATOM   2368 C C   . GLU B 1 97  ? 10.608  -14.133 32.339  1.00 43.58 ? 99  GLU B C   1 
ATOM   2369 O O   . GLU B 1 97  ? 9.647   -13.364 32.493  1.00 43.41 ? 99  GLU B O   1 
ATOM   2370 C CB  . GLU B 1 97  ? 12.894  -13.026 32.210  1.00 47.28 ? 99  GLU B CB  1 
ATOM   2371 C CG  . GLU B 1 97  ? 14.208  -12.976 31.444  1.00 54.79 ? 99  GLU B CG  1 
ATOM   2372 C CD  . GLU B 1 97  ? 15.390  -12.518 32.268  1.00 65.33 ? 99  GLU B CD  1 
ATOM   2373 O OE1 . GLU B 1 97  ? 16.443  -13.198 32.219  1.00 68.44 ? 99  GLU B OE1 1 
ATOM   2374 O OE2 . GLU B 1 97  ? 15.269  -11.480 32.959  1.00 67.73 ? 99  GLU B OE2 1 
ATOM   2375 N N   . PRO B 1 98  ? 10.697  -15.338 32.926  1.00 43.80 ? 100 PRO B N   1 
ATOM   2376 C CA  . PRO B 1 98  ? 9.619   -15.819 33.771  1.00 44.85 ? 100 PRO B CA  1 
ATOM   2377 C C   . PRO B 1 98  ? 9.673   -15.215 35.174  1.00 44.83 ? 100 PRO B C   1 
ATOM   2378 O O   . PRO B 1 98  ? 9.661   -15.944 36.140  1.00 45.18 ? 100 PRO B O   1 
ATOM   2379 C CB  . PRO B 1 98  ? 9.873   -17.334 33.783  1.00 46.53 ? 100 PRO B CB  1 
ATOM   2380 C CG  . PRO B 1 98  ? 11.327  -17.443 33.788  1.00 47.13 ? 100 PRO B CG  1 
ATOM   2381 C CD  . PRO B 1 98  ? 11.776  -16.342 32.841  1.00 44.77 ? 100 PRO B CD  1 
ATOM   2382 N N   . MET B 1 99  ? 9.735   -13.894 35.276  1.00 44.89 ? 101 MET B N   1 
ATOM   2383 C CA  . MET B 1 99  ? 9.852   -13.186 36.530  1.00 45.14 ? 101 MET B CA  1 
ATOM   2384 C C   . MET B 1 99  ? 8.909   -11.988 36.453  1.00 45.37 ? 101 MET B C   1 
ATOM   2385 O O   . MET B 1 99  ? 8.826   -11.291 35.420  1.00 44.67 ? 101 MET B O   1 
ATOM   2386 C CB  . MET B 1 99  ? 11.316  -12.777 36.782  1.00 45.94 ? 101 MET B CB  1 
ATOM   2387 C CG  . MET B 1 99  ? 12.252  -13.977 37.168  1.00 50.04 ? 101 MET B CG  1 
ATOM   2388 S SD  . MET B 1 99  ? 12.058  -14.684 38.840  1.00 66.63 ? 101 MET B SD  1 
ATOM   2389 C CE  . MET B 1 99  ? 12.967  -16.211 38.652  1.00 67.49 ? 101 MET B CE  1 
ATOM   2390 N N   . TRP B 1 100 ? 8.186   -11.744 37.546  1.00 45.98 ? 102 TRP B N   1 
ATOM   2391 C CA  . TRP B 1 100 ? 7.124   -10.733 37.527  1.00 47.33 ? 102 TRP B CA  1 
ATOM   2392 C C   . TRP B 1 100 ? 7.699   -9.313  37.294  1.00 46.47 ? 102 TRP B C   1 
ATOM   2393 O O   . TRP B 1 100 ? 6.941   -8.444  36.874  1.00 46.97 ? 102 TRP B O   1 
ATOM   2394 C CB  . TRP B 1 100 ? 6.198   -10.842 38.778  1.00 48.27 ? 102 TRP B CB  1 
ATOM   2395 C CG  . TRP B 1 100 ? 6.608   -10.048 39.978  1.00 49.98 ? 102 TRP B CG  1 
ATOM   2396 C CD1 . TRP B 1 100 ? 7.397   -10.475 41.007  1.00 51.57 ? 102 TRP B CD1 1 
ATOM   2397 C CD2 . TRP B 1 100 ? 6.214   -8.702  40.307  1.00 50.58 ? 102 TRP B CD2 1 
ATOM   2398 N NE1 . TRP B 1 100 ? 7.569   -9.460  41.928  1.00 51.86 ? 102 TRP B NE1 1 
ATOM   2399 C CE2 . TRP B 1 100 ? 6.841   -8.365  41.525  1.00 51.59 ? 102 TRP B CE2 1 
ATOM   2400 C CE3 . TRP B 1 100 ? 5.425   -7.740  39.675  1.00 51.38 ? 102 TRP B CE3 1 
ATOM   2401 C CZ2 . TRP B 1 100 ? 6.670   -7.127  42.133  1.00 52.35 ? 102 TRP B CZ2 1 
ATOM   2402 C CZ3 . TRP B 1 100 ? 5.267   -6.508  40.275  1.00 52.41 ? 102 TRP B CZ3 1 
ATOM   2403 C CH2 . TRP B 1 100 ? 5.870   -6.221  41.500  1.00 52.47 ? 102 TRP B CH2 1 
ATOM   2404 N N   . GLU B 1 101 ? 9.027   -9.098  37.529  1.00 45.18 ? 103 GLU B N   1 
ATOM   2405 C CA  . GLU B 1 101 ? 9.717   -7.826  37.350  1.00 44.15 ? 103 GLU B CA  1 
ATOM   2406 C C   . GLU B 1 101 ? 9.960   -7.499  35.898  1.00 42.42 ? 103 GLU B C   1 
ATOM   2407 O O   . GLU B 1 101 ? 10.088  -6.325  35.591  1.00 42.13 ? 103 GLU B O   1 
ATOM   2408 C CB  . GLU B 1 101 ? 11.073  -7.811  38.086  1.00 46.01 ? 103 GLU B CB  1 
ATOM   2409 C CG  . GLU B 1 101 ? 10.984  -8.100  39.581  1.00 50.60 ? 103 GLU B CG  1 
ATOM   2410 C CD  . GLU B 1 101 ? 11.127  -9.553  40.004  1.00 54.30 ? 103 GLU B CD  1 
ATOM   2411 O OE1 . GLU B 1 101 ? 10.925  -10.450 39.154  1.00 52.41 ? 103 GLU B OE1 1 
ATOM   2412 O OE2 . GLU B 1 101 ? 11.442  -9.793  41.193  1.00 56.48 ? 103 GLU B OE2 1 
ATOM   2413 N N   . ASP B 1 102 ? 10.011  -8.502  34.966  1.00 41.30 ? 104 ASP B N   1 
ATOM   2414 C CA  . ASP B 1 102 ? 10.051  -8.264  33.493  1.00 40.86 ? 104 ASP B CA  1 
ATOM   2415 C C   . ASP B 1 102 ? 9.079   -7.143  33.096  1.00 40.74 ? 104 ASP B C   1 
ATOM   2416 O O   . ASP B 1 102 ? 8.021   -7.008  33.721  1.00 39.72 ? 104 ASP B O   1 
ATOM   2417 C CB  . ASP B 1 102 ? 9.656   -9.536  32.687  1.00 41.16 ? 104 ASP B CB  1 
ATOM   2418 C CG  . ASP B 1 102 ? 9.978   -9.522  31.191  1.00 44.95 ? 104 ASP B CG  1 
ATOM   2419 O OD1 . ASP B 1 102 ? 11.085  -9.962  30.818  1.00 46.34 ? 104 ASP B OD1 1 
ATOM   2420 O OD2 . ASP B 1 102 ? 9.109   -9.092  30.389  1.00 43.60 ? 104 ASP B OD2 1 
ATOM   2421 N N   . GLU B 1 103 ? 9.452   -6.361  32.083  1.00 41.43 ? 105 GLU B N   1 
ATOM   2422 C CA  . GLU B 1 103 ? 8.610   -5.291  31.550  1.00 42.65 ? 105 GLU B CA  1 
ATOM   2423 C C   . GLU B 1 103 ? 7.242   -5.824  31.035  1.00 41.25 ? 105 GLU B C   1 
ATOM   2424 O O   . GLU B 1 103 ? 6.264   -5.075  31.081  1.00 42.12 ? 105 GLU B O   1 
ATOM   2425 C CB  . GLU B 1 103 ? 9.377   -4.498  30.465  1.00 47.63 ? 105 GLU B CB  1 
ATOM   2426 C CG  . GLU B 1 103 ? 9.663   -5.289  29.199  1.00 56.63 ? 105 GLU B CG  1 
ATOM   2427 C CD  . GLU B 1 103 ? 10.540  -4.588  28.176  1.00 69.14 ? 105 GLU B CD  1 
ATOM   2428 O OE1 . GLU B 1 103 ? 10.801  -3.371  28.341  1.00 70.77 ? 105 GLU B OE1 1 
ATOM   2429 O OE2 . GLU B 1 103 ? 10.958  -5.260  27.202  1.00 72.32 ? 105 GLU B OE2 1 
ATOM   2430 N N   . LYS B 1 104 ? 7.163   -7.087  30.564  1.00 38.89 ? 106 LYS B N   1 
ATOM   2431 C CA  . LYS B 1 104 ? 5.886   -7.670  30.098  1.00 37.36 ? 106 LYS B CA  1 
ATOM   2432 C C   . LYS B 1 104 ? 5.059   -8.347  31.194  1.00 35.25 ? 106 LYS B C   1 
ATOM   2433 O O   . LYS B 1 104 ? 3.910   -8.709  30.912  1.00 35.52 ? 106 LYS B O   1 
ATOM   2434 C CB  . LYS B 1 104 ? 6.130   -8.631  28.923  1.00 39.97 ? 106 LYS B CB  1 
ATOM   2435 C CG  . LYS B 1 104 ? 6.604   -7.906  27.658  1.00 45.32 ? 106 LYS B CG  1 
ATOM   2436 C CD  . LYS B 1 104 ? 5.413   -7.295  26.885  1.00 52.51 ? 106 LYS B CD  1 
ATOM   2437 C CE  . LYS B 1 104 ? 5.818   -6.546  25.633  1.00 58.42 ? 106 LYS B CE  1 
ATOM   2438 N NZ  . LYS B 1 104 ? 5.336   -5.112  25.664  1.00 63.96 ? 106 LYS B NZ  1 
ATOM   2439 N N   . ASN B 1 105 ? 5.587   -8.517  32.427  1.00 33.05 ? 107 ASN B N   1 
ATOM   2440 C CA  . ASN B 1 105 ? 4.817   -9.102  33.500  1.00 32.58 ? 107 ASN B CA  1 
ATOM   2441 C C   . ASN B 1 105 ? 4.531   -8.077  34.637  1.00 34.77 ? 107 ASN B C   1 
ATOM   2442 O O   . ASN B 1 105 ? 3.572   -8.266  35.379  1.00 34.41 ? 107 ASN B O   1 
ATOM   2443 C CB  . ASN B 1 105 ? 5.561   -10.269 34.078  1.00 32.27 ? 107 ASN B CB  1 
ATOM   2444 C CG  . ASN B 1 105 ? 5.899   -11.367 33.099  1.00 32.91 ? 107 ASN B CG  1 
ATOM   2445 O OD1 . ASN B 1 105 ? 5.120   -11.706 32.196  1.00 32.42 ? 107 ASN B OD1 1 
ATOM   2446 N ND2 . ASN B 1 105 ? 7.072   -11.955 33.279  1.00 32.06 ? 107 ASN B ND2 1 
ATOM   2447 N N   . LYS B 1 106 ? 5.336   -7.021  34.790  1.00 36.91 ? 108 LYS B N   1 
ATOM   2448 C CA  . LYS B 1 106 ? 5.209   -6.145  35.989  1.00 39.08 ? 108 LYS B CA  1 
ATOM   2449 C C   . LYS B 1 106 ? 3.810   -5.570  36.168  1.00 37.36 ? 108 LYS B C   1 
ATOM   2450 O O   . LYS B 1 106 ? 3.386   -5.424  37.307  1.00 37.53 ? 108 LYS B O   1 
ATOM   2451 C CB  . LYS B 1 106 ? 6.285   -5.038  36.098  1.00 44.46 ? 108 LYS B CB  1 
ATOM   2452 C CG  . LYS B 1 106 ? 6.509   -4.127  34.885  1.00 53.61 ? 108 LYS B CG  1 
ATOM   2453 C CD  . LYS B 1 106 ? 7.672   -3.133  35.141  1.00 62.06 ? 108 LYS B CD  1 
ATOM   2454 C CE  . LYS B 1 106 ? 7.537   -1.818  34.380  1.00 68.46 ? 108 LYS B CE  1 
ATOM   2455 N NZ  . LYS B 1 106 ? 8.410   -0.731  34.922  1.00 72.68 ? 108 LYS B NZ  1 
ATOM   2456 N N   . ARG B 1 107 ? 3.080   -5.268  35.068  1.00 35.46 ? 109 ARG B N   1 
ATOM   2457 C CA  . ARG B 1 107 ? 1.729   -4.721  35.181  1.00 34.58 ? 109 ARG B CA  1 
ATOM   2458 C C   . ARG B 1 107 ? 0.616   -5.796  35.111  1.00 32.09 ? 109 ARG B C   1 
ATOM   2459 O O   . ARG B 1 107 ? -0.543  -5.450  34.937  1.00 31.14 ? 109 ARG B O   1 
ATOM   2460 C CB  . ARG B 1 107 ? 1.539   -3.676  34.089  1.00 38.49 ? 109 ARG B CB  1 
ATOM   2461 C CG  . ARG B 1 107 ? 2.501   -2.464  34.258  1.00 43.84 ? 109 ARG B CG  1 
ATOM   2462 C CD  . ARG B 1 107 ? 2.364   -1.488  33.120  1.00 50.32 ? 109 ARG B CD  1 
ATOM   2463 N NE  . ARG B 1 107 ? 2.733   -2.097  31.834  1.00 59.74 ? 109 ARG B NE  1 
ATOM   2464 C CZ  . ARG B 1 107 ? 3.981   -2.251  31.375  1.00 64.59 ? 109 ARG B CZ  1 
ATOM   2465 N NH1 . ARG B 1 107 ? 5.023   -1.833  32.096  1.00 64.35 ? 109 ARG B NH1 1 
ATOM   2466 N NH2 . ARG B 1 107 ? 4.195   -2.824  30.191  1.00 64.86 ? 109 ARG B NH2 1 
ATOM   2467 N N   . GLY B 1 108 ? 0.984   -7.054  35.273  1.00 30.48 ? 110 GLY B N   1 
ATOM   2468 C CA  . GLY B 1 108 ? 0.170   -8.184  34.864  1.00 31.45 ? 110 GLY B CA  1 
ATOM   2469 C C   . GLY B 1 108 ? -0.360  -8.951  36.033  1.00 30.97 ? 110 GLY B C   1 
ATOM   2470 O O   . GLY B 1 108 ? -0.429  -8.439  37.171  1.00 30.52 ? 110 GLY B O   1 
ATOM   2471 N N   . GLY B 1 109 ? -0.760  -10.159 35.729  1.00 30.48 ? 111 GLY B N   1 
ATOM   2472 C CA  . GLY B 1 109 ? -1.105  -11.134 36.731  1.00 30.41 ? 111 GLY B CA  1 
ATOM   2473 C C   . GLY B 1 109 ? -1.303  -12.512 36.152  1.00 29.17 ? 111 GLY B C   1 
ATOM   2474 O O   . GLY B 1 109 ? -0.868  -12.813 35.040  1.00 27.59 ? 111 GLY B O   1 
ATOM   2475 N N   . ARG B 1 110 ? -1.995  -13.356 36.909  1.00 29.03 ? 112 ARG B N   1 
ATOM   2476 C CA  . ARG B 1 110 ? -2.075  -14.757 36.612  1.00 27.14 ? 112 ARG B CA  1 
ATOM   2477 C C   . ARG B 1 110 ? -3.438  -15.336 36.988  1.00 26.96 ? 112 ARG B C   1 
ATOM   2478 O O   . ARG B 1 110 ? -3.959  -15.007 38.052  1.00 27.05 ? 112 ARG B O   1 
ATOM   2479 C CB  . ARG B 1 110 ? -0.944  -15.482 37.325  1.00 27.32 ? 112 ARG B CB  1 
ATOM   2480 C CG  . ARG B 1 110 ? -1.111  -15.511 38.800  1.00 28.83 ? 112 ARG B CG  1 
ATOM   2481 C CD  . ARG B 1 110 ? -0.047  -16.279 39.414  1.00 31.26 ? 112 ARG B CD  1 
ATOM   2482 N NE  . ARG B 1 110 ? -0.284  -16.402 40.846  1.00 37.98 ? 112 ARG B NE  1 
ATOM   2483 C CZ  . ARG B 1 110 ? 0.538   -17.006 41.697  1.00 41.32 ? 112 ARG B CZ  1 
ATOM   2484 N NH1 . ARG B 1 110 ? 0.238   -17.063 42.995  1.00 43.99 ? 112 ARG B NH1 1 
ATOM   2485 N NH2 . ARG B 1 110 ? 1.661   -17.565 41.265  1.00 40.80 ? 112 ARG B NH2 1 
ATOM   2486 N N   . TRP B 1 111 ? -4.009  -16.168 36.106  1.00 26.80 ? 113 TRP B N   1 
ATOM   2487 C CA  . TRP B 1 111 ? -5.084  -17.108 36.429  1.00 27.68 ? 113 TRP B CA  1 
ATOM   2488 C C   . TRP B 1 111 ? -4.487  -18.313 37.108  1.00 26.76 ? 113 TRP B C   1 
ATOM   2489 O O   . TRP B 1 111 ? -3.637  -18.947 36.517  1.00 27.34 ? 113 TRP B O   1 
ATOM   2490 C CB  . TRP B 1 111 ? -5.809  -17.621 35.192  1.00 28.32 ? 113 TRP B CB  1 
ATOM   2491 C CG  . TRP B 1 111 ? -6.706  -16.606 34.624  1.00 29.69 ? 113 TRP B CG  1 
ATOM   2492 C CD1 . TRP B 1 111 ? -6.515  -15.854 33.499  1.00 30.85 ? 113 TRP B CD1 1 
ATOM   2493 C CD2 . TRP B 1 111 ? -7.934  -16.178 35.197  1.00 30.21 ? 113 TRP B CD2 1 
ATOM   2494 N NE1 . TRP B 1 111 ? -7.554  -14.960 33.354  1.00 30.49 ? 113 TRP B NE1 1 
ATOM   2495 C CE2 . TRP B 1 111 ? -8.440  -15.147 34.385  1.00 30.61 ? 113 TRP B CE2 1 
ATOM   2496 C CE3 . TRP B 1 111 ? -8.660  -16.573 36.336  1.00 30.97 ? 113 TRP B CE3 1 
ATOM   2497 C CZ2 . TRP B 1 111 ? -9.618  -14.502 34.681  1.00 32.34 ? 113 TRP B CZ2 1 
ATOM   2498 C CZ3 . TRP B 1 111 ? -9.847  -15.944 36.608  1.00 31.61 ? 113 TRP B CZ3 1 
ATOM   2499 C CH2 . TRP B 1 111 ? -10.312 -14.921 35.789  1.00 32.73 ? 113 TRP B CH2 1 
ATOM   2500 N N   . LEU B 1 112 ? -4.917  -18.626 38.293  1.00 26.69 ? 114 LEU B N   1 
ATOM   2501 C CA  . LEU B 1 112 ? -4.271  -19.637 39.128  1.00 28.37 ? 114 LEU B CA  1 
ATOM   2502 C C   . LEU B 1 112 ? -5.151  -20.844 39.375  1.00 29.35 ? 114 LEU B C   1 
ATOM   2503 O O   . LEU B 1 112 ? -6.329  -20.671 39.699  1.00 31.47 ? 114 LEU B O   1 
ATOM   2504 C CB  . LEU B 1 112 ? -3.892  -19.029 40.490  1.00 28.84 ? 114 LEU B CB  1 
ATOM   2505 C CG  . LEU B 1 112 ? -3.088  -19.939 41.458  1.00 31.41 ? 114 LEU B CG  1 
ATOM   2506 C CD1 . LEU B 1 112 ? -1.706  -20.212 40.937  1.00 31.11 ? 114 LEU B CD1 1 
ATOM   2507 C CD2 . LEU B 1 112 ? -2.974  -19.298 42.866  1.00 32.19 ? 114 LEU B CD2 1 
ATOM   2508 N N   . ILE B 1 113 ? -4.560  -22.056 39.228  1.00 27.58 ? 115 ILE B N   1 
ATOM   2509 C CA  . ILE B 1 113 ? -5.145  -23.361 39.522  1.00 29.34 ? 115 ILE B CA  1 
ATOM   2510 C C   . ILE B 1 113 ? -4.274  -23.988 40.613  1.00 29.46 ? 115 ILE B C   1 
ATOM   2511 O O   . ILE B 1 113 ? -3.104  -24.317 40.368  1.00 25.39 ? 115 ILE B O   1 
ATOM   2512 C CB  . ILE B 1 113 ? -5.168  -24.347 38.280  1.00 31.91 ? 115 ILE B CB  1 
ATOM   2513 C CG1 . ILE B 1 113 ? -5.469  -23.638 36.926  1.00 34.03 ? 115 ILE B CG1 1 
ATOM   2514 C CG2 . ILE B 1 113 ? -6.102  -25.492 38.531  1.00 32.73 ? 115 ILE B CG2 1 
ATOM   2515 C CD1 . ILE B 1 113 ? -6.847  -22.948 36.814  1.00 35.38 ? 115 ILE B CD1 1 
ATOM   2516 N N   . THR B 1 114 ? -4.832  -24.135 41.823  1.00 32.05 ? 116 THR B N   1 
ATOM   2517 C CA  . THR B 1 114 ? -4.168  -24.786 42.884  1.00 36.29 ? 116 THR B CA  1 
ATOM   2518 C C   . THR B 1 114 ? -4.695  -26.204 42.888  1.00 41.10 ? 116 THR B C   1 
ATOM   2519 O O   . THR B 1 114 ? -5.906  -26.422 42.987  1.00 42.33 ? 116 THR B O   1 
ATOM   2520 C CB  . THR B 1 114 ? -4.435  -24.055 44.186  1.00 39.71 ? 116 THR B CB  1 
ATOM   2521 O OG1 . THR B 1 114 ? -5.823  -24.171 44.465  1.00 42.75 ? 116 THR B OG1 1 
ATOM   2522 C CG2 . THR B 1 114 ? -3.976  -22.553 44.154  1.00 38.95 ? 116 THR B CG2 1 
ATOM   2523 N N   . LEU B 1 115 ? -3.802  -27.167 42.758  1.00 42.86 ? 117 LEU B N   1 
ATOM   2524 C CA  . LEU B 1 115 ? -4.135  -28.556 42.944  1.00 45.04 ? 117 LEU B CA  1 
ATOM   2525 C C   . LEU B 1 115 ? -3.804  -28.950 44.390  1.00 47.55 ? 117 LEU B C   1 
ATOM   2526 O O   . LEU B 1 115 ? -2.723  -28.608 44.905  1.00 47.90 ? 117 LEU B O   1 
ATOM   2527 C CB  . LEU B 1 115 ? -3.334  -29.395 41.966  1.00 44.88 ? 117 LEU B CB  1 
ATOM   2528 C CG  . LEU B 1 115 ? -3.537  -29.065 40.472  1.00 46.71 ? 117 LEU B CG  1 
ATOM   2529 C CD1 . LEU B 1 115 ? -2.823  -30.061 39.623  1.00 47.95 ? 117 LEU B CD1 1 
ATOM   2530 C CD2 . LEU B 1 115 ? -5.011  -29.089 40.062  1.00 47.35 ? 117 LEU B CD2 1 
ATOM   2531 N N   . ASN B 1 116 ? -4.731  -29.647 45.039  1.00 48.99 ? 118 ASN B N   1 
ATOM   2532 C CA  . ASN B 1 116 ? -4.440  -30.222 46.345  1.00 51.93 ? 118 ASN B CA  1 
ATOM   2533 C C   . ASN B 1 116 ? -3.589  -31.504 46.196  1.00 54.03 ? 118 ASN B C   1 
ATOM   2534 O O   . ASN B 1 116 ? -3.347  -31.958 45.081  1.00 54.05 ? 118 ASN B O   1 
ATOM   2535 C CB  . ASN B 1 116 ? -5.719  -30.393 47.207  1.00 53.89 ? 118 ASN B CB  1 
ATOM   2536 C CG  . ASN B 1 116 ? -6.779  -31.365 46.760  1.00 58.71 ? 118 ASN B CG  1 
ATOM   2537 O OD1 . ASN B 1 116 ? -6.541  -32.314 45.994  1.00 59.70 ? 118 ASN B OD1 1 
ATOM   2538 N ND2 . ASN B 1 116 ? -8.004  -31.137 47.258  1.00 60.74 ? 118 ASN B ND2 1 
ATOM   2539 N N   . LYS B 1 117 ? -3.138  -32.066 47.320  1.00 55.66 ? 119 LYS B N   1 
ATOM   2540 C CA  . LYS B 1 117 ? -2.167  -33.158 47.377  1.00 57.50 ? 119 LYS B CA  1 
ATOM   2541 C C   . LYS B 1 117 ? -2.537  -34.354 46.498  1.00 58.56 ? 119 LYS B C   1 
ATOM   2542 O O   . LYS B 1 117 ? -1.690  -34.878 45.783  1.00 58.30 ? 119 LYS B O   1 
ATOM   2543 C CB  . LYS B 1 117 ? -2.000  -33.633 48.842  1.00 60.64 ? 119 LYS B CB  1 
ATOM   2544 C CG  . LYS B 1 117 ? -1.228  -32.669 49.738  1.00 66.42 ? 119 LYS B CG  1 
ATOM   2545 C CD  . LYS B 1 117 ? -2.060  -31.498 50.289  1.00 71.84 ? 119 LYS B CD  1 
ATOM   2546 C CE  . LYS B 1 117 ? -1.410  -30.916 51.542  1.00 75.91 ? 119 LYS B CE  1 
ATOM   2547 N NZ  . LYS B 1 117 ? -1.864  -29.518 51.830  1.00 76.95 ? 119 LYS B NZ  1 
ATOM   2548 N N   . GLN B 1 118 ? -3.793  -34.785 46.557  1.00 59.78 ? 120 GLN B N   1 
ATOM   2549 C CA  . GLN B 1 118 ? -4.247  -35.950 45.801  1.00 60.87 ? 120 GLN B CA  1 
ATOM   2550 C C   . GLN B 1 118 ? -4.388  -35.627 44.303  1.00 60.34 ? 120 GLN B C   1 
ATOM   2551 O O   . GLN B 1 118 ? -4.144  -36.508 43.466  1.00 60.35 ? 120 GLN B O   1 
ATOM   2552 C CB  . GLN B 1 118 ? -5.560  -36.495 46.395  1.00 63.39 ? 120 GLN B CB  1 
ATOM   2553 C CG  . GLN B 1 118 ? -6.794  -35.622 46.168  1.00 68.12 ? 120 GLN B CG  1 
ATOM   2554 C CD  . GLN B 1 118 ? -7.710  -35.507 47.376  1.00 73.66 ? 120 GLN B CD  1 
ATOM   2555 O OE1 . GLN B 1 118 ? -7.687  -36.324 48.309  1.00 74.69 ? 120 GLN B OE1 1 
ATOM   2556 N NE2 . GLN B 1 118 ? -8.552  -34.473 47.380  1.00 75.12 ? 120 GLN B NE2 1 
ATOM   2557 N N   . GLN B 1 119 ? -4.778  -34.361 43.972  1.00 59.14 ? 121 GLN B N   1 
ATOM   2558 C CA  . GLN B 1 119 ? -4.863  -33.880 42.594  1.00 57.99 ? 121 GLN B CA  1 
ATOM   2559 C C   . GLN B 1 119 ? -3.531  -33.870 41.886  1.00 56.67 ? 121 GLN B C   1 
ATOM   2560 O O   . GLN B 1 119 ? -3.546  -33.729 40.681  1.00 57.34 ? 121 GLN B O   1 
ATOM   2561 C CB  . GLN B 1 119 ? -5.459  -32.466 42.510  1.00 59.51 ? 121 GLN B CB  1 
ATOM   2562 C CG  . GLN B 1 119 ? -6.950  -32.364 42.748  1.00 62.50 ? 121 GLN B CG  1 
ATOM   2563 C CD  . GLN B 1 119 ? -7.387  -30.945 42.522  1.00 66.25 ? 121 GLN B CD  1 
ATOM   2564 O OE1 . GLN B 1 119 ? -7.289  -30.088 43.412  1.00 67.22 ? 121 GLN B OE1 1 
ATOM   2565 N NE2 . GLN B 1 119 ? -7.866  -30.650 41.322  1.00 67.74 ? 121 GLN B NE2 1 
ATOM   2566 N N   . ARG B 1 120 ? -2.372  -34.004 42.574  1.00 55.31 ? 122 ARG B N   1 
ATOM   2567 C CA  . ARG B 1 120 ? -1.095  -34.111 41.867  1.00 55.21 ? 122 ARG B CA  1 
ATOM   2568 C C   . ARG B 1 120 ? -1.112  -35.353 40.959  1.00 56.73 ? 122 ARG B C   1 
ATOM   2569 O O   . ARG B 1 120 ? -1.024  -35.255 39.730  1.00 58.00 ? 122 ARG B O   1 
ATOM   2570 C CB  . ARG B 1 120 ? 0.102   -34.152 42.835  1.00 55.19 ? 122 ARG B CB  1 
ATOM   2571 C CG  . ARG B 1 120 ? 1.430   -34.552 42.170  1.00 56.13 ? 122 ARG B CG  1 
ATOM   2572 C CD  . ARG B 1 120 ? 2.540   -34.629 43.174  1.00 58.08 ? 122 ARG B CD  1 
ATOM   2573 N NE  . ARG B 1 120 ? 2.962   -33.289 43.559  1.00 60.75 ? 122 ARG B NE  1 
ATOM   2574 C CZ  . ARG B 1 120 ? 4.017   -33.014 44.316  1.00 63.33 ? 122 ARG B CZ  1 
ATOM   2575 N NH1 . ARG B 1 120 ? 4.781   -33.998 44.802  1.00 63.66 ? 122 ARG B NH1 1 
ATOM   2576 N NH2 . ARG B 1 120 ? 4.318   -31.764 44.602  1.00 62.45 ? 122 ARG B NH2 1 
ATOM   2577 N N   . ARG B 1 121 ? -1.260  -36.518 41.587  1.00 55.86 ? 123 ARG B N   1 
ATOM   2578 C CA  . ARG B 1 121 ? -1.179  -37.815 40.917  1.00 56.18 ? 123 ARG B CA  1 
ATOM   2579 C C   . ARG B 1 121 ? -2.171  -37.859 39.729  1.00 54.59 ? 123 ARG B C   1 
ATOM   2580 O O   . ARG B 1 121 ? -1.798  -38.269 38.643  1.00 55.00 ? 123 ARG B O   1 
ATOM   2581 C CB  . ARG B 1 121 ? -1.438  -39.007 41.898  1.00 58.86 ? 123 ARG B CB  1 
ATOM   2582 C CG  . ARG B 1 121 ? -1.423  -38.688 43.406  1.00 64.08 ? 123 ARG B CG  1 
ATOM   2583 C CD  . ARG B 1 121 ? -1.505  -39.900 44.321  1.00 68.58 ? 123 ARG B CD  1 
ATOM   2584 N NE  . ARG B 1 121 ? -2.561  -39.700 45.324  1.00 72.39 ? 123 ARG B NE  1 
ATOM   2585 C CZ  . ARG B 1 121 ? -3.854  -39.989 45.158  1.00 75.29 ? 123 ARG B CZ  1 
ATOM   2586 N NH1 . ARG B 1 121 ? -4.722  -39.758 46.139  1.00 74.74 ? 123 ARG B NH1 1 
ATOM   2587 N NH2 . ARG B 1 121 ? -4.288  -40.517 44.014  1.00 75.81 ? 123 ARG B NH2 1 
ATOM   2588 N N   . SER B 1 122 ? -3.402  -37.386 39.960  1.00 52.60 ? 124 SER B N   1 
ATOM   2589 C CA  . SER B 1 122 ? -4.517  -37.391 39.011  1.00 51.47 ? 124 SER B CA  1 
ATOM   2590 C C   . SER B 1 122 ? -4.572  -36.231 37.969  1.00 48.70 ? 124 SER B C   1 
ATOM   2591 O O   . SER B 1 122 ? -4.908  -36.476 36.803  1.00 49.34 ? 124 SER B O   1 
ATOM   2592 C CB  . SER B 1 122 ? -5.825  -37.411 39.804  1.00 53.90 ? 124 SER B CB  1 
ATOM   2593 O OG  . SER B 1 122 ? -5.860  -36.301 40.690  1.00 56.03 ? 124 SER B OG  1 
ATOM   2594 N N   . ASP B 1 123 ? -4.238  -34.993 38.356  1.00 45.29 ? 125 ASP B N   1 
ATOM   2595 C CA  . ASP B 1 123 ? -4.512  -33.819 37.514  1.00 42.20 ? 125 ASP B CA  1 
ATOM   2596 C C   . ASP B 1 123 ? -3.286  -33.022 37.080  1.00 37.80 ? 125 ASP B C   1 
ATOM   2597 O O   . ASP B 1 123 ? -3.422  -32.293 36.122  1.00 36.79 ? 125 ASP B O   1 
ATOM   2598 C CB  . ASP B 1 123 ? -5.505  -32.862 38.165  1.00 44.87 ? 125 ASP B CB  1 
ATOM   2599 C CG  . ASP B 1 123 ? -6.871  -33.442 38.446  1.00 48.95 ? 125 ASP B CG  1 
ATOM   2600 O OD1 . ASP B 1 123 ? -7.498  -33.962 37.506  1.00 49.91 ? 125 ASP B OD1 1 
ATOM   2601 O OD2 . ASP B 1 123 ? -7.321  -33.354 39.600  1.00 51.27 ? 125 ASP B OD2 1 
ATOM   2602 N N   . LEU B 1 124 ? -2.109  -33.131 37.729  1.00 35.66 ? 126 LEU B N   1 
ATOM   2603 C CA  . LEU B 1 124 ? -0.964  -32.272 37.397  1.00 33.37 ? 126 LEU B CA  1 
ATOM   2604 C C   . LEU B 1 124 ? -0.531  -32.410 35.925  1.00 30.28 ? 126 LEU B C   1 
ATOM   2605 O O   . LEU B 1 124 ? -0.447  -31.408 35.219  1.00 29.00 ? 126 LEU B O   1 
ATOM   2606 C CB  . LEU B 1 124 ? 0.218   -32.595 38.318  1.00 33.20 ? 126 LEU B CB  1 
ATOM   2607 C CG  . LEU B 1 124 ? 1.487   -31.730 38.164  1.00 32.67 ? 126 LEU B CG  1 
ATOM   2608 C CD1 . LEU B 1 124 ? 1.259   -30.331 38.579  1.00 31.54 ? 126 LEU B CD1 1 
ATOM   2609 C CD2 . LEU B 1 124 ? 2.625   -32.275 39.009  1.00 35.54 ? 126 LEU B CD2 1 
ATOM   2610 N N   . ASN B 1 125 ? -0.257  -33.621 35.467  1.00 29.40 ? 127 ASN B N   1 
ATOM   2611 C CA  . ASN B 1 125 ? 0.247   -33.832 34.113  1.00 29.68 ? 127 ASN B CA  1 
ATOM   2612 C C   . ASN B 1 125 ? -0.777  -33.407 33.075  1.00 29.18 ? 127 ASN B C   1 
ATOM   2613 O O   . ASN B 1 125 ? -0.440  -32.733 32.089  1.00 29.28 ? 127 ASN B O   1 
ATOM   2614 C CB  . ASN B 1 125 ? 0.694   -35.254 33.916  1.00 31.69 ? 127 ASN B CB  1 
ATOM   2615 C CG  . ASN B 1 125 ? 1.897   -35.654 34.781  1.00 35.42 ? 127 ASN B CG  1 
ATOM   2616 O OD1 . ASN B 1 125 ? 1.925   -36.719 35.384  1.00 35.76 ? 127 ASN B OD1 1 
ATOM   2617 N ND2 . ASN B 1 125 ? 2.933   -34.847 34.850  1.00 37.38 ? 127 ASN B ND2 1 
ATOM   2618 N N   . ARG B 1 126 ? -2.018  -33.786 33.304  1.00 28.18 ? 128 ARG B N   1 
ATOM   2619 C CA  . ARG B 1 126 ? -3.125  -33.454 32.429  1.00 27.85 ? 128 ARG B CA  1 
ATOM   2620 C C   . ARG B 1 126 ? -3.320  -31.934 32.354  1.00 27.29 ? 128 ARG B C   1 
ATOM   2621 O O   . ARG B 1 126 ? -3.341  -31.395 31.267  1.00 27.61 ? 128 ARG B O   1 
ATOM   2622 C CB  . ARG B 1 126 ? -4.406  -34.160 32.926  1.00 29.53 ? 128 ARG B CB  1 
ATOM   2623 C CG  . ARG B 1 126 ? -5.691  -33.747 32.190  1.00 32.57 ? 128 ARG B CG  1 
ATOM   2624 C CD  . ARG B 1 126 ? -5.617  -33.979 30.698  1.00 34.16 ? 128 ARG B CD  1 
ATOM   2625 N NE  . ARG B 1 126 ? -5.307  -35.378 30.346  1.00 36.20 ? 128 ARG B NE  1 
ATOM   2626 C CZ  . ARG B 1 126 ? -5.019  -35.793 29.115  1.00 38.09 ? 128 ARG B CZ  1 
ATOM   2627 N NH1 . ARG B 1 126 ? -5.003  -34.929 28.097  1.00 39.78 ? 128 ARG B NH1 1 
ATOM   2628 N NH2 . ARG B 1 126 ? -4.741  -37.068 28.890  1.00 36.58 ? 128 ARG B NH2 1 
ATOM   2629 N N   . PHE B 1 127 ? -3.445  -31.258 33.483  1.00 27.42 ? 129 PHE B N   1 
ATOM   2630 C CA  . PHE B 1 127 ? -3.707  -29.817 33.466  1.00 29.40 ? 129 PHE B CA  1 
ATOM   2631 C C   . PHE B 1 127 ? -2.516  -29.057 32.922  1.00 27.11 ? 129 PHE B C   1 
ATOM   2632 O O   . PHE B 1 127 ? -2.724  -28.063 32.269  1.00 26.68 ? 129 PHE B O   1 
ATOM   2633 C CB  . PHE B 1 127 ? -4.037  -29.283 34.830  1.00 31.75 ? 129 PHE B CB  1 
ATOM   2634 C CG  . PHE B 1 127 ? -5.387  -29.568 35.415  1.00 35.87 ? 129 PHE B CG  1 
ATOM   2635 C CD1 . PHE B 1 127 ? -6.208  -30.542 34.882  1.00 37.90 ? 129 PHE B CD1 1 
ATOM   2636 C CD2 . PHE B 1 127 ? -5.847  -28.846 36.494  1.00 38.76 ? 129 PHE B CD2 1 
ATOM   2637 C CE1 . PHE B 1 127 ? -7.461  -30.790 35.437  1.00 39.16 ? 129 PHE B CE1 1 
ATOM   2638 C CE2 . PHE B 1 127 ? -7.091  -29.099 37.042  1.00 39.58 ? 129 PHE B CE2 1 
ATOM   2639 C CZ  . PHE B 1 127 ? -7.890  -30.073 36.506  1.00 38.99 ? 129 PHE B CZ  1 
ATOM   2640 N N   . TRP B 1 128 ? -1.281  -29.511 33.198  1.00 25.43 ? 130 TRP B N   1 
ATOM   2641 C CA  . TRP B 1 128 ? -0.105  -28.843 32.657  1.00 23.56 ? 130 TRP B CA  1 
ATOM   2642 C C   . TRP B 1 128 ? -0.069  -28.933 31.148  1.00 21.81 ? 130 TRP B C   1 
ATOM   2643 O O   . TRP B 1 128 ? 0.156   -27.943 30.497  1.00 22.22 ? 130 TRP B O   1 
ATOM   2644 C CB  . TRP B 1 128 ? 1.202   -29.383 33.274  1.00 23.07 ? 130 TRP B CB  1 
ATOM   2645 C CG  . TRP B 1 128 ? 2.445   -28.701 32.797  1.00 21.23 ? 130 TRP B CG  1 
ATOM   2646 C CD1 . TRP B 1 128 ? 3.561   -29.294 32.314  1.00 22.00 ? 130 TRP B CD1 1 
ATOM   2647 C CD2 . TRP B 1 128 ? 2.750   -27.299 32.901  1.00 21.17 ? 130 TRP B CD2 1 
ATOM   2648 N NE1 . TRP B 1 128 ? 4.509   -28.350 32.012  1.00 22.40 ? 130 TRP B NE1 1 
ATOM   2649 C CE2 . TRP B 1 128 ? 4.037   -27.111 32.360  1.00 22.17 ? 130 TRP B CE2 1 
ATOM   2650 C CE3 . TRP B 1 128 ? 2.026   -26.176 33.324  1.00 21.06 ? 130 TRP B CE3 1 
ATOM   2651 C CZ2 . TRP B 1 128 ? 4.649   -25.860 32.302  1.00 23.12 ? 130 TRP B CZ2 1 
ATOM   2652 C CZ3 . TRP B 1 128 ? 2.620   -24.930 33.241  1.00 21.76 ? 130 TRP B CZ3 1 
ATOM   2653 C CH2 . TRP B 1 128 ? 3.916   -24.778 32.747  1.00 22.81 ? 130 TRP B CH2 1 
ATOM   2654 N N   . LEU B 1 129 ? -0.282  -30.134 30.574  1.00 22.14 ? 131 LEU B N   1 
ATOM   2655 C CA  . LEU B 1 129 ? -0.348  -30.283 29.124  1.00 22.83 ? 131 LEU B CA  1 
ATOM   2656 C C   . LEU B 1 129 ? -1.471  -29.426 28.533  1.00 23.54 ? 131 LEU B C   1 
ATOM   2657 O O   . LEU B 1 129 ? -1.231  -28.747 27.526  1.00 22.79 ? 131 LEU B O   1 
ATOM   2658 C CB  . LEU B 1 129 ? -0.555  -31.765 28.716  1.00 22.52 ? 131 LEU B CB  1 
ATOM   2659 C CG  . LEU B 1 129 ? -0.762  -32.015 27.222  1.00 22.77 ? 131 LEU B CG  1 
ATOM   2660 C CD1 . LEU B 1 129 ? 0.419   -31.497 26.433  1.00 22.78 ? 131 LEU B CD1 1 
ATOM   2661 C CD2 . LEU B 1 129 ? -1.028  -33.435 26.930  1.00 23.91 ? 131 LEU B CD2 1 
ATOM   2662 N N   . GLU B 1 130 ? -2.685  -29.445 29.148  1.00 23.31 ? 132 GLU B N   1 
ATOM   2663 C CA  . GLU B 1 130 ? -3.782  -28.674 28.572  1.00 23.36 ? 132 GLU B CA  1 
ATOM   2664 C C   . GLU B 1 130 ? -3.459  -27.160 28.548  1.00 24.61 ? 132 GLU B C   1 
ATOM   2665 O O   . GLU B 1 130 ? -3.802  -26.425 27.586  1.00 23.36 ? 132 GLU B O   1 
ATOM   2666 C CB  . GLU B 1 130 ? -5.104  -28.925 29.292  1.00 24.09 ? 132 GLU B CB  1 
ATOM   2667 C CG  . GLU B 1 130 ? -5.578  -30.355 29.264  1.00 29.08 ? 132 GLU B CG  1 
ATOM   2668 C CD  . GLU B 1 130 ? -5.849  -30.907 27.874  1.00 34.55 ? 132 GLU B CD  1 
ATOM   2669 O OE1 . GLU B 1 130 ? -6.115  -30.095 26.957  1.00 31.37 ? 132 GLU B OE1 1 
ATOM   2670 O OE2 . GLU B 1 130 ? -5.789  -32.146 27.700  1.00 35.56 ? 132 GLU B OE2 1 
ATOM   2671 N N   . THR B 1 131 ? -2.801  -26.699 29.617  1.00 24.99 ? 133 THR B N   1 
ATOM   2672 C CA  . THR B 1 131 ? -2.258  -25.340 29.687  1.00 25.67 ? 133 THR B CA  1 
ATOM   2673 C C   . THR B 1 131 ? -1.288  -25.026 28.537  1.00 26.55 ? 133 THR B C   1 
ATOM   2674 O O   . THR B 1 131 ? -1.402  -23.977 27.901  1.00 26.19 ? 133 THR B O   1 
ATOM   2675 C CB  . THR B 1 131 ? -1.581  -25.117 31.021  1.00 24.96 ? 133 THR B CB  1 
ATOM   2676 O OG1 . THR B 1 131 ? -2.535  -25.344 32.033  1.00 25.36 ? 133 THR B OG1 1 
ATOM   2677 C CG2 . THR B 1 131 ? -1.008  -23.753 31.132  1.00 24.60 ? 133 THR B CG2 1 
ATOM   2678 N N   . LEU B 1 132 ? -0.320  -25.918 28.296  1.00 26.76 ? 134 LEU B N   1 
ATOM   2679 C CA  . LEU B 1 132 ? 0.660   -25.735 27.223  1.00 27.04 ? 134 LEU B CA  1 
ATOM   2680 C C   . LEU B 1 132 ? -0.006  -25.682 25.857  1.00 26.97 ? 134 LEU B C   1 
ATOM   2681 O O   . LEU B 1 132 ? 0.437   -24.918 25.015  1.00 28.04 ? 134 LEU B O   1 
ATOM   2682 C CB  . LEU B 1 132 ? 1.685   -26.864 27.235  1.00 26.96 ? 134 LEU B CB  1 
ATOM   2683 C CG  . LEU B 1 132 ? 2.556   -26.980 28.469  1.00 28.29 ? 134 LEU B CG  1 
ATOM   2684 C CD1 . LEU B 1 132 ? 3.420   -28.178 28.390  1.00 28.85 ? 134 LEU B CD1 1 
ATOM   2685 C CD2 . LEU B 1 132 ? 3.461   -25.759 28.659  1.00 29.33 ? 134 LEU B CD2 1 
ATOM   2686 N N   . LEU B 1 133 ? -1.050  -26.468 25.636  1.00 25.94 ? 135 LEU B N   1 
ATOM   2687 C CA  . LEU B 1 133 ? -1.748  -26.451 24.361  1.00 25.98 ? 135 LEU B CA  1 
ATOM   2688 C C   . LEU B 1 133 ? -2.467  -25.121 24.095  1.00 23.91 ? 135 LEU B C   1 
ATOM   2689 O O   . LEU B 1 133 ? -2.472  -24.665 22.961  1.00 25.43 ? 135 LEU B O   1 
ATOM   2690 C CB  . LEU B 1 133 ? -2.678  -27.654 24.235  1.00 26.56 ? 135 LEU B CB  1 
ATOM   2691 C CG  . LEU B 1 133 ? -2.008  -29.060 24.327  1.00 26.59 ? 135 LEU B CG  1 
ATOM   2692 C CD1 . LEU B 1 133 ? -3.015  -30.183 24.076  1.00 26.35 ? 135 LEU B CD1 1 
ATOM   2693 C CD2 . LEU B 1 133 ? -0.934  -29.256 23.302  1.00 27.30 ? 135 LEU B CD2 1 
ATOM   2694 N N   . CYS B 1 134 ? -3.059  -24.522 25.115  1.00 21.83 ? 136 CYS B N   1 
ATOM   2695 C CA  . CYS B 1 134 ? -3.696  -23.255 25.105  1.00 21.35 ? 136 CYS B CA  1 
ATOM   2696 C C   . CYS B 1 134 ? -2.714  -22.140 24.681  1.00 22.80 ? 136 CYS B C   1 
ATOM   2697 O O   . CYS B 1 134 ? -3.107  -21.205 23.944  1.00 22.47 ? 136 CYS B O   1 
ATOM   2698 C CB  . CYS B 1 134 ? -4.294  -22.927 26.477  1.00 24.75 ? 136 CYS B CB  1 
ATOM   2699 S SG  . CYS B 1 134 ? -5.842  -23.781 26.840  1.00 24.69 ? 136 CYS B SG  1 
ATOM   2700 N N   . LEU B 1 135 ? -1.464  -22.224 25.192  1.00 22.37 ? 137 LEU B N   1 
ATOM   2701 C CA  . LEU B 1 135 ? -0.413  -21.272 24.881  1.00 23.12 ? 137 LEU B CA  1 
ATOM   2702 C C   . LEU B 1 135 ? 0.047   -21.408 23.436  1.00 24.02 ? 137 LEU B C   1 
ATOM   2703 O O   . LEU B 1 135 ? -0.127  -20.471 22.655  1.00 24.68 ? 137 LEU B O   1 
ATOM   2704 C CB  . LEU B 1 135 ? 0.785   -21.385 25.833  1.00 22.36 ? 137 LEU B CB  1 
ATOM   2705 C CG  . LEU B 1 135 ? 0.795   -20.461 27.073  1.00 23.90 ? 137 LEU B CG  1 
ATOM   2706 C CD1 . LEU B 1 135 ? -0.514  -20.509 27.851  1.00 22.49 ? 137 LEU B CD1 1 
ATOM   2707 C CD2 . LEU B 1 135 ? 1.952   -20.835 27.968  1.00 24.36 ? 137 LEU B CD2 1 
ATOM   2708 N N   . ILE B 1 136 ? 0.598   -22.558 23.049  1.00 25.08 ? 138 ILE B N   1 
ATOM   2709 C CA  . ILE B 1 136 ? 1.173   -22.708 21.698  1.00 25.77 ? 138 ILE B CA  1 
ATOM   2710 C C   . ILE B 1 136 ? 0.116   -22.663 20.626  1.00 27.11 ? 138 ILE B C   1 
ATOM   2711 O O   . ILE B 1 136 ? 0.396   -22.194 19.512  1.00 28.52 ? 138 ILE B O   1 
ATOM   2712 C CB  . ILE B 1 136 ? 2.085   -23.969 21.541  1.00 26.32 ? 138 ILE B CB  1 
ATOM   2713 C CG1 . ILE B 1 136 ? 1.257   -25.267 21.514  1.00 25.41 ? 138 ILE B CG1 1 
ATOM   2714 C CG2 . ILE B 1 136 ? 3.185   -23.951 22.652  1.00 25.96 ? 138 ILE B CG2 1 
ATOM   2715 C CD1 . ILE B 1 136 ? 1.980   -26.450 21.451  1.00 27.26 ? 138 ILE B CD1 1 
ATOM   2716 N N   . GLY B 1 137 ? -1.083  -23.135 20.933  1.00 27.78 ? 139 GLY B N   1 
ATOM   2717 C CA  . GLY B 1 137 ? -2.193  -23.094 19.975  1.00 29.81 ? 139 GLY B CA  1 
ATOM   2718 C C   . GLY B 1 137 ? -2.893  -21.757 19.798  1.00 30.89 ? 139 GLY B C   1 
ATOM   2719 O O   . GLY B 1 137 ? -3.773  -21.653 18.963  1.00 29.52 ? 139 GLY B O   1 
ATOM   2720 N N   . GLU B 1 138 ? -2.519  -20.720 20.553  1.00 31.48 ? 140 GLU B N   1 
ATOM   2721 C CA  . GLU B 1 138 ? -3.200  -19.401 20.489  1.00 30.97 ? 140 GLU B CA  1 
ATOM   2722 C C   . GLU B 1 138 ? -4.736  -19.453 20.749  1.00 31.41 ? 140 GLU B C   1 
ATOM   2723 O O   . GLU B 1 138 ? -5.551  -18.953 19.938  1.00 31.30 ? 140 GLU B O   1 
ATOM   2724 C CB  . GLU B 1 138 ? -2.899  -18.698 19.171  1.00 32.18 ? 140 GLU B CB  1 
ATOM   2725 C CG  . GLU B 1 138 ? -1.405  -18.525 18.915  1.00 34.76 ? 140 GLU B CG  1 
ATOM   2726 C CD  . GLU B 1 138 ? -0.635  -17.539 19.777  1.00 35.85 ? 140 GLU B CD  1 
ATOM   2727 O OE1 . GLU B 1 138 ? -1.115  -16.398 19.965  1.00 31.47 ? 140 GLU B OE1 1 
ATOM   2728 O OE2 . GLU B 1 138 ? 0.461   -17.913 20.257  1.00 35.91 ? 140 GLU B OE2 1 
ATOM   2729 N N   . SER B 1 139 ? -5.099  -20.039 21.924  1.00 31.46 ? 141 SER B N   1 
ATOM   2730 C CA  . SER B 1 139 ? -6.449  -20.481 22.207  1.00 32.11 ? 141 SER B CA  1 
ATOM   2731 C C   . SER B 1 139 ? -7.398  -19.379 22.659  1.00 32.40 ? 141 SER B C   1 
ATOM   2732 O O   . SER B 1 139 ? -8.588  -19.644 22.874  1.00 32.08 ? 141 SER B O   1 
ATOM   2733 C CB  . SER B 1 139 ? -6.405  -21.626 23.226  1.00 34.01 ? 141 SER B CB  1 
ATOM   2734 O OG  . SER B 1 139 ? -5.759  -22.774 22.678  1.00 33.94 ? 141 SER B OG  1 
ATOM   2735 N N   . PHE B 1 140 ? -6.912  -18.157 22.801  1.00 32.63 ? 142 PHE B N   1 
ATOM   2736 C CA  . PHE B 1 140 ? -7.703  -17.071 23.347  1.00 34.40 ? 142 PHE B CA  1 
ATOM   2737 C C   . PHE B 1 140 ? -8.056  -16.044 22.306  1.00 34.42 ? 142 PHE B C   1 
ATOM   2738 O O   . PHE B 1 140 ? -8.398  -14.936 22.689  1.00 32.52 ? 142 PHE B O   1 
ATOM   2739 C CB  . PHE B 1 140 ? -6.959  -16.476 24.565  1.00 34.51 ? 142 PHE B CB  1 
ATOM   2740 C CG  . PHE B 1 140 ? -6.548  -17.566 25.548  1.00 34.48 ? 142 PHE B CG  1 
ATOM   2741 C CD1 . PHE B 1 140 ? -7.500  -18.313 26.214  1.00 34.07 ? 142 PHE B CD1 1 
ATOM   2742 C CD2 . PHE B 1 140 ? -5.216  -17.886 25.741  1.00 34.94 ? 142 PHE B CD2 1 
ATOM   2743 C CE1 . PHE B 1 140 ? -7.137  -19.310 27.084  1.00 34.30 ? 142 PHE B CE1 1 
ATOM   2744 C CE2 . PHE B 1 140 ? -4.848  -18.917 26.621  1.00 34.20 ? 142 PHE B CE2 1 
ATOM   2745 C CZ  . PHE B 1 140 ? -5.807  -19.609 27.288  1.00 33.50 ? 142 PHE B CZ  1 
ATOM   2746 N N   . ASP B 1 141 ? -8.007  -16.386 20.990  1.00 36.33 ? 143 ASP B N   1 
ATOM   2747 C CA  . ASP B 1 141 ? -8.438  -15.449 19.931  1.00 38.91 ? 143 ASP B CA  1 
ATOM   2748 C C   . ASP B 1 141 ? -7.504  -14.193 19.968  1.00 38.86 ? 143 ASP B C   1 
ATOM   2749 O O   . ASP B 1 141 ? -6.314  -14.435 20.158  1.00 39.38 ? 143 ASP B O   1 
ATOM   2750 C CB  . ASP B 1 141 ? -9.980  -15.191 20.014  1.00 43.61 ? 143 ASP B CB  1 
ATOM   2751 C CG  . ASP B 1 141 ? -10.810 -16.395 19.575  1.00 56.50 ? 143 ASP B CG  1 
ATOM   2752 O OD1 . ASP B 1 141 ? -10.354 -17.142 18.673  1.00 59.00 ? 143 ASP B OD1 1 
ATOM   2753 O OD2 . ASP B 1 141 ? -11.914 -16.600 20.138  1.00 61.26 ? 143 ASP B OD2 1 
ATOM   2754 N N   . ASP B 1 142 ? -7.954  -12.917 19.810  1.00 39.30 ? 144 ASP B N   1 
ATOM   2755 C CA  . ASP B 1 142 ? -6.979  -11.798 19.845  1.00 40.61 ? 144 ASP B CA  1 
ATOM   2756 C C   . ASP B 1 142 ? -6.323  -11.699 21.240  1.00 39.60 ? 144 ASP B C   1 
ATOM   2757 O O   . ASP B 1 142 ? -5.203  -11.178 21.369  1.00 39.04 ? 144 ASP B O   1 
ATOM   2758 C CB  . ASP B 1 142 ? -7.573  -10.424 19.493  1.00 44.55 ? 144 ASP B CB  1 
ATOM   2759 C CG  . ASP B 1 142 ? -8.033  -10.191 18.069  1.00 54.34 ? 144 ASP B CG  1 
ATOM   2760 O OD1 . ASP B 1 142 ? -7.984  -11.162 17.248  1.00 53.87 ? 144 ASP B OD1 1 
ATOM   2761 O OD2 . ASP B 1 142 ? -8.450  -9.022  17.761  1.00 58.73 ? 144 ASP B OD2 1 
ATOM   2762 N N   . TYR B 1 143 ? -7.006  -12.210 22.285  1.00 38.61 ? 145 TYR B N   1 
ATOM   2763 C CA  . TYR B 1 143 ? -6.528  -12.002 23.645  1.00 37.46 ? 145 TYR B CA  1 
ATOM   2764 C C   . TYR B 1 143 ? -5.384  -12.942 23.998  1.00 33.45 ? 145 TYR B C   1 
ATOM   2765 O O   . TYR B 1 143 ? -4.924  -12.860 25.102  1.00 31.11 ? 145 TYR B O   1 
ATOM   2766 C CB  . TYR B 1 143 ? -7.669  -12.138 24.660  1.00 39.89 ? 145 TYR B CB  1 
ATOM   2767 C CG  . TYR B 1 143 ? -8.964  -11.441 24.260  1.00 42.36 ? 145 TYR B CG  1 
ATOM   2768 C CD1 . TYR B 1 143 ? -9.040  -10.059 24.180  1.00 44.15 ? 145 TYR B CD1 1 
ATOM   2769 C CD2 . TYR B 1 143 ? -10.090 -12.171 23.918  1.00 44.36 ? 145 TYR B CD2 1 
ATOM   2770 C CE1 . TYR B 1 143 ? -10.230 -9.422  23.831  1.00 46.19 ? 145 TYR B CE1 1 
ATOM   2771 C CE2 . TYR B 1 143 ? -11.272 -11.549 23.536  1.00 46.27 ? 145 TYR B CE2 1 
ATOM   2772 C CZ  . TYR B 1 143 ? -11.340 -10.176 23.500  1.00 48.87 ? 145 TYR B CZ  1 
ATOM   2773 O OH  . TYR B 1 143 ? -12.518 -9.564  23.121  1.00 55.11 ? 145 TYR B OH  1 
ATOM   2774 N N   . SER B 1 144 ? -4.921  -13.835 23.074  1.00 32.10 ? 146 SER B N   1 
ATOM   2775 C CA  . SER B 1 144 ? -3.685  -14.588 23.257  1.00 29.98 ? 146 SER B CA  1 
ATOM   2776 C C   . SER B 1 144 ? -2.467  -13.677 23.206  1.00 29.45 ? 146 SER B C   1 
ATOM   2777 O O   . SER B 1 144 ? -1.406  -14.081 23.706  1.00 30.01 ? 146 SER B O   1 
ATOM   2778 C CB  . SER B 1 144 ? -3.521  -15.688 22.206  1.00 30.09 ? 146 SER B CB  1 
ATOM   2779 O OG  . SER B 1 144 ? -4.239  -16.883 22.495  1.00 31.24 ? 146 SER B OG  1 
ATOM   2780 N N   . ASP B 1 145 ? -2.563  -12.477 22.593  1.00 28.18 ? 147 ASP B N   1 
ATOM   2781 C CA  . ASP B 1 145 ? -1.463  -11.527 22.662  1.00 29.27 ? 147 ASP B CA  1 
ATOM   2782 C C   . ASP B 1 145 ? -1.234  -11.065 24.101  1.00 28.42 ? 147 ASP B C   1 
ATOM   2783 O O   . ASP B 1 145 ? -0.097  -10.674 24.437  1.00 31.25 ? 147 ASP B O   1 
ATOM   2784 C CB  . ASP B 1 145 ? -1.701  -10.325 21.707  1.00 34.25 ? 147 ASP B CB  1 
ATOM   2785 C CG  . ASP B 1 145 ? -1.604  -10.687 20.236  1.00 43.27 ? 147 ASP B CG  1 
ATOM   2786 O OD1 . ASP B 1 145 ? -0.860  -11.656 19.903  1.00 44.28 ? 147 ASP B OD1 1 
ATOM   2787 O OD2 . ASP B 1 145 ? -2.276  -10.019 19.412  1.00 48.50 ? 147 ASP B OD2 1 
ATOM   2788 N N   . ASP B 1 146 ? -2.275  -11.103 24.959  1.00 24.50 ? 148 ASP B N   1 
ATOM   2789 C CA  . ASP B 1 146 ? -2.062  -10.762 26.359  1.00 25.58 ? 148 ASP B CA  1 
ATOM   2790 C C   . ASP B 1 146 ? -1.349  -11.845 27.153  1.00 24.88 ? 148 ASP B C   1 
ATOM   2791 O O   . ASP B 1 146 ? -0.904  -11.571 28.254  1.00 24.84 ? 148 ASP B O   1 
ATOM   2792 C CB  . ASP B 1 146 ? -3.401  -10.383 27.031  1.00 29.15 ? 148 ASP B CB  1 
ATOM   2793 C CG  . ASP B 1 146 ? -3.661  -8.887  26.958  1.00 33.09 ? 148 ASP B CG  1 
ATOM   2794 O OD1 . ASP B 1 146 ? -3.547  -8.332  25.863  1.00 35.34 ? 148 ASP B OD1 1 
ATOM   2795 O OD2 . ASP B 1 146 ? -3.929  -8.283  28.010  1.00 33.04 ? 148 ASP B OD2 1 
ATOM   2796 N N   . VAL B 1 147 ? -1.226  -13.069 26.627  1.00 24.25 ? 149 VAL B N   1 
ATOM   2797 C CA  . VAL B 1 147 ? -0.550  -14.163 27.344  1.00 22.77 ? 149 VAL B CA  1 
ATOM   2798 C C   . VAL B 1 147 ? 0.953   -13.928 27.300  1.00 22.16 ? 149 VAL B C   1 
ATOM   2799 O O   . VAL B 1 147 ? 1.493   -13.629 26.259  1.00 22.04 ? 149 VAL B O   1 
ATOM   2800 C CB  . VAL B 1 147 ? -0.956  -15.520 26.733  1.00 21.95 ? 149 VAL B CB  1 
ATOM   2801 C CG1 . VAL B 1 147 ? -0.180  -16.668 27.379  1.00 21.47 ? 149 VAL B CG1 1 
ATOM   2802 C CG2 . VAL B 1 147 ? -2.478  -15.754 26.858  1.00 22.30 ? 149 VAL B CG2 1 
ATOM   2803 N N   . CYS B 1 148 ? 1.624   -14.043 28.447  1.00 21.96 ? 150 CYS B N   1 
ATOM   2804 C CA  . CYS B 1 148 ? 3.086   -14.001 28.544  1.00 22.06 ? 150 CYS B CA  1 
ATOM   2805 C C   . CYS B 1 148 ? 3.632   -15.427 28.605  1.00 22.41 ? 150 CYS B C   1 
ATOM   2806 O O   . CYS B 1 148 ? 4.574   -15.740 27.919  1.00 22.68 ? 150 CYS B O   1 
ATOM   2807 C CB  . CYS B 1 148 ? 3.501   -13.209 29.769  1.00 23.08 ? 150 CYS B CB  1 
ATOM   2808 S SG  . CYS B 1 148 ? 2.948   -11.506 29.705  1.00 27.87 ? 150 CYS B SG  1 
ATOM   2809 N N   . GLY B 1 149 ? 3.008   -16.258 29.419  1.00 21.72 ? 151 GLY B N   1 
ATOM   2810 C CA  . GLY B 1 149 ? 3.450   -17.621 29.624  1.00 21.15 ? 151 GLY B CA  1 
ATOM   2811 C C   . GLY B 1 149 ? 2.630   -18.324 30.666  1.00 20.96 ? 151 GLY B C   1 
ATOM   2812 O O   . GLY B 1 149 ? 1.600   -17.814 31.114  1.00 19.64 ? 151 GLY B O   1 
ATOM   2813 N N   . ALA B 1 150 ? 3.101   -19.511 31.057  1.00 20.94 ? 152 ALA B N   1 
ATOM   2814 C CA  . ALA B 1 150 ? 2.483   -20.329 32.097  1.00 21.57 ? 152 ALA B CA  1 
ATOM   2815 C C   . ALA B 1 150 ? 3.563   -20.879 33.002  1.00 23.71 ? 152 ALA B C   1 
ATOM   2816 O O   . ALA B 1 150 ? 4.672   -21.163 32.524  1.00 24.22 ? 152 ALA B O   1 
ATOM   2817 C CB  . ALA B 1 150 ? 1.708   -21.466 31.459  1.00 19.66 ? 152 ALA B CB  1 
ATOM   2818 N N   . VAL B 1 151 ? 3.257   -21.008 34.305  1.00 24.25 ? 153 VAL B N   1 
ATOM   2819 C CA  . VAL B 1 151 ? 4.150   -21.533 35.305  1.00 25.25 ? 153 VAL B CA  1 
ATOM   2820 C C   . VAL B 1 151 ? 3.537   -22.743 36.047  1.00 24.02 ? 153 VAL B C   1 
ATOM   2821 O O   . VAL B 1 151 ? 2.356   -22.748 36.389  1.00 22.44 ? 153 VAL B O   1 
ATOM   2822 C CB  . VAL B 1 151 ? 4.517   -20.460 36.364  1.00 27.71 ? 153 VAL B CB  1 
ATOM   2823 C CG1 . VAL B 1 151 ? 5.475   -21.029 37.414  1.00 28.39 ? 153 VAL B CG1 1 
ATOM   2824 C CG2 . VAL B 1 151 ? 5.113   -19.224 35.735  1.00 30.18 ? 153 VAL B CG2 1 
ATOM   2825 N N   . VAL B 1 152 ? 4.363   -23.742 36.322  1.00 23.73 ? 154 VAL B N   1 
ATOM   2826 C CA  . VAL B 1 152 ? 4.004   -24.800 37.245  1.00 24.56 ? 154 VAL B CA  1 
ATOM   2827 C C   . VAL B 1 152 ? 4.960   -24.768 38.454  1.00 26.57 ? 154 VAL B C   1 
ATOM   2828 O O   . VAL B 1 152 ? 6.182   -24.882 38.320  1.00 24.71 ? 154 VAL B O   1 
ATOM   2829 C CB  . VAL B 1 152 ? 3.855   -26.195 36.561  1.00 24.89 ? 154 VAL B CB  1 
ATOM   2830 C CG1 . VAL B 1 152 ? 5.111   -26.595 35.794  1.00 26.33 ? 154 VAL B CG1 1 
ATOM   2831 C CG2 . VAL B 1 152 ? 3.506   -27.269 37.591  1.00 25.17 ? 154 VAL B CG2 1 
ATOM   2832 N N   . ASN B 1 153 ? 4.399   -24.588 39.647  1.00 29.63 ? 155 ASN B N   1 
ATOM   2833 C CA  . ASN B 1 153 ? 5.149   -24.714 40.889  1.00 32.07 ? 155 ASN B CA  1 
ATOM   2834 C C   . ASN B 1 153 ? 4.838   -26.097 41.530  1.00 35.61 ? 155 ASN B C   1 
ATOM   2835 O O   . ASN B 1 153 ? 3.707   -26.374 41.950  1.00 36.72 ? 155 ASN B O   1 
ATOM   2836 C CB  . ASN B 1 153 ? 4.855   -23.550 41.831  1.00 32.64 ? 155 ASN B CB  1 
ATOM   2837 C CG  . ASN B 1 153 ? 4.785   -22.153 41.227  1.00 35.34 ? 155 ASN B CG  1 
ATOM   2838 O OD1 . ASN B 1 153 ? 3.723   -21.581 40.958  1.00 34.69 ? 155 ASN B OD1 1 
ATOM   2839 N ND2 . ASN B 1 153 ? 5.921   -21.548 41.013  1.00 36.92 ? 155 ASN B ND2 1 
ATOM   2840 N N   . VAL B 1 154 ? 5.837   -26.985 41.560  1.00 37.28 ? 156 VAL B N   1 
ATOM   2841 C CA  . VAL B 1 154 ? 5.713   -28.329 42.153  1.00 39.92 ? 156 VAL B CA  1 
ATOM   2842 C C   . VAL B 1 154 ? 6.077   -28.196 43.642  1.00 41.50 ? 156 VAL B C   1 
ATOM   2843 O O   . VAL B 1 154 ? 7.191   -27.778 43.956  1.00 40.47 ? 156 VAL B O   1 
ATOM   2844 C CB  . VAL B 1 154 ? 6.639   -29.315 41.420  1.00 40.20 ? 156 VAL B CB  1 
ATOM   2845 C CG1 . VAL B 1 154 ? 6.513   -30.722 41.947  1.00 40.61 ? 156 VAL B CG1 1 
ATOM   2846 C CG2 . VAL B 1 154 ? 6.297   -29.317 39.942  1.00 41.53 ? 156 VAL B CG2 1 
ATOM   2847 N N   . ARG B 1 155 ? 5.140   -28.524 44.531  1.00 43.16 ? 157 ARG B N   1 
ATOM   2848 C CA  . ARG B 1 155 ? 5.277   -28.230 45.962  1.00 46.66 ? 157 ARG B CA  1 
ATOM   2849 C C   . ARG B 1 155 ? 4.715   -29.367 46.804  1.00 49.87 ? 157 ARG B C   1 
ATOM   2850 O O   . ARG B 1 155 ? 3.960   -30.188 46.292  1.00 51.11 ? 157 ARG B O   1 
ATOM   2851 C CB  . ARG B 1 155 ? 4.566   -26.916 46.345  1.00 46.84 ? 157 ARG B CB  1 
ATOM   2852 C CG  . ARG B 1 155 ? 5.094   -25.696 45.668  1.00 50.14 ? 157 ARG B CG  1 
ATOM   2853 C CD  . ARG B 1 155 ? 6.443   -25.307 46.208  1.00 53.09 ? 157 ARG B CD  1 
ATOM   2854 N NE  . ARG B 1 155 ? 6.925   -24.038 45.662  1.00 57.44 ? 157 ARG B NE  1 
ATOM   2855 C CZ  . ARG B 1 155 ? 7.442   -23.881 44.444  1.00 59.87 ? 157 ARG B CZ  1 
ATOM   2856 N NH1 . ARG B 1 155 ? 7.544   -24.919 43.614  1.00 58.74 ? 157 ARG B NH1 1 
ATOM   2857 N NH2 . ARG B 1 155 ? 7.856   -22.686 44.041  1.00 59.38 ? 157 ARG B NH2 1 
ATOM   2858 N N   . ALA B 1 156 ? 5.073   -29.416 48.082  1.00 50.86 ? 158 ALA B N   1 
ATOM   2859 C CA  . ALA B 1 156 ? 4.614   -30.500 48.962  1.00 52.96 ? 158 ALA B CA  1 
ATOM   2860 C C   . ALA B 1 156 ? 3.169   -30.273 49.385  1.00 53.92 ? 158 ALA B C   1 
ATOM   2861 O O   . ALA B 1 156 ? 2.382   -31.211 49.412  1.00 54.29 ? 158 ALA B O   1 
ATOM   2862 C CB  . ALA B 1 156 ? 5.514   -30.583 50.197  1.00 53.48 ? 158 ALA B CB  1 
ATOM   2863 N N   . LYS B 1 157 ? 2.849   -29.017 49.715  1.00 54.14 ? 159 LYS B N   1 
ATOM   2864 C CA  . LYS B 1 157 ? 1.522   -28.564 50.131  1.00 54.33 ? 159 LYS B CA  1 
ATOM   2865 C C   . LYS B 1 157 ? 0.489   -28.695 49.011  1.00 53.29 ? 159 LYS B C   1 
ATOM   2866 O O   . LYS B 1 157 ? -0.689  -28.914 49.292  1.00 55.38 ? 159 LYS B O   1 
ATOM   2867 C CB  . LYS B 1 157 ? 1.622   -27.088 50.585  1.00 56.43 ? 159 LYS B CB  1 
ATOM   2868 C CG  . LYS B 1 157 ? 0.333   -26.440 51.028  1.00 61.12 ? 159 LYS B CG  1 
ATOM   2869 C CD  . LYS B 1 157 ? 0.666   -25.046 51.631  1.00 66.46 ? 159 LYS B CD  1 
ATOM   2870 C CE  . LYS B 1 157 ? -0.313  -23.948 51.303  1.00 71.10 ? 159 LYS B CE  1 
ATOM   2871 N NZ  . LYS B 1 157 ? -0.425  -23.688 49.834  1.00 73.06 ? 159 LYS B NZ  1 
ATOM   2872 N N   . GLY B 1 158 ? 0.909   -28.557 47.762  1.00 50.74 ? 160 GLY B N   1 
ATOM   2873 C CA  . GLY B 1 158 ? -0.020  -28.608 46.648  1.00 48.39 ? 160 GLY B CA  1 
ATOM   2874 C C   . GLY B 1 158 ? 0.472   -27.788 45.499  1.00 46.00 ? 160 GLY B C   1 
ATOM   2875 O O   . GLY B 1 158 ? 0.965   -26.670 45.671  1.00 45.94 ? 160 GLY B O   1 
ATOM   2876 N N   . ASP B 1 159 ? 0.307   -28.344 44.322  1.00 42.93 ? 161 ASP B N   1 
ATOM   2877 C CA  . ASP B 1 159 ? 0.939   -27.816 43.149  1.00 39.75 ? 161 ASP B CA  1 
ATOM   2878 C C   . ASP B 1 159 ? 0.161   -26.625 42.636  1.00 36.17 ? 161 ASP B C   1 
ATOM   2879 O O   . ASP B 1 159 ? -1.053  -26.553 42.833  1.00 34.71 ? 161 ASP B O   1 
ATOM   2880 C CB  . ASP B 1 159 ? 1.059   -28.928 42.118  1.00 40.31 ? 161 ASP B CB  1 
ATOM   2881 C CG  . ASP B 1 159 ? 1.959   -30.054 42.584  1.00 41.99 ? 161 ASP B CG  1 
ATOM   2882 O OD1 . ASP B 1 159 ? 2.954   -29.776 43.260  1.00 40.89 ? 161 ASP B OD1 1 
ATOM   2883 O OD2 . ASP B 1 159 ? 1.667   -31.195 42.268  1.00 45.78 ? 161 ASP B OD2 1 
ATOM   2884 N N   . LYS B 1 160 ? 0.864   -25.679 41.981  1.00 34.30 ? 162 LYS B N   1 
ATOM   2885 C CA  . LYS B 1 160 ? 0.219   -24.510 41.367  1.00 31.66 ? 162 LYS B CA  1 
ATOM   2886 C C   . LYS B 1 160 ? 0.490   -24.487 39.897  1.00 29.93 ? 162 LYS B C   1 
ATOM   2887 O O   . LYS B 1 160 ? 1.635   -24.749 39.466  1.00 28.35 ? 162 LYS B O   1 
ATOM   2888 C CB  . LYS B 1 160 ? 0.700   -23.203 41.983  1.00 34.17 ? 162 LYS B CB  1 
ATOM   2889 C CG  . LYS B 1 160 ? 0.273   -23.042 43.434  1.00 40.30 ? 162 LYS B CG  1 
ATOM   2890 C CD  . LYS B 1 160 ? 0.773   -21.724 44.036  1.00 47.71 ? 162 LYS B CD  1 
ATOM   2891 C CE  . LYS B 1 160 ? 1.958   -21.932 44.973  1.00 54.43 ? 162 LYS B CE  1 
ATOM   2892 N NZ  . LYS B 1 160 ? 2.325   -20.685 45.722  1.00 58.79 ? 162 LYS B NZ  1 
ATOM   2893 N N   . ILE B 1 161 ? -0.566  -24.195 39.105  1.00 27.86 ? 163 ILE B N   1 
ATOM   2894 C CA  . ILE B 1 161 ? -0.430  -23.979 37.677  1.00 26.77 ? 163 ILE B CA  1 
ATOM   2895 C C   . ILE B 1 161 ? -1.119  -22.650 37.370  1.00 26.06 ? 163 ILE B C   1 
ATOM   2896 O O   . ILE B 1 161 ? -2.230  -22.421 37.846  1.00 24.62 ? 163 ILE B O   1 
ATOM   2897 C CB  . ILE B 1 161 ? -1.091  -25.106 36.872  1.00 28.04 ? 163 ILE B CB  1 
ATOM   2898 C CG1 . ILE B 1 161 ? -0.473  -26.466 37.174  1.00 29.53 ? 163 ILE B CG1 1 
ATOM   2899 C CG2 . ILE B 1 161 ? -1.075  -24.759 35.359  1.00 28.81 ? 163 ILE B CG2 1 
ATOM   2900 C CD1 . ILE B 1 161 ? -1.226  -27.618 36.540  1.00 30.66 ? 163 ILE B CD1 1 
ATOM   2901 N N   . ALA B 1 162 ? -0.487  -21.793 36.555  1.00 24.33 ? 164 ALA B N   1 
ATOM   2902 C CA  . ALA B 1 162 ? -0.977  -20.447 36.322  1.00 24.01 ? 164 ALA B CA  1 
ATOM   2903 C C   . ALA B 1 162 ? -0.663  -19.998 34.916  1.00 24.35 ? 164 ALA B C   1 
ATOM   2904 O O   . ALA B 1 162 ? 0.426   -20.301 34.425  1.00 25.33 ? 164 ALA B O   1 
ATOM   2905 C CB  . ALA B 1 162 ? -0.366  -19.477 37.313  1.00 23.40 ? 164 ALA B CB  1 
ATOM   2906 N N   . ILE B 1 163 ? -1.607  -19.316 34.259  1.00 22.72 ? 165 ILE B N   1 
ATOM   2907 C CA  . ILE B 1 163 ? -1.301  -18.510 33.067  1.00 21.76 ? 165 ILE B CA  1 
ATOM   2908 C C   . ILE B 1 163 ? -1.109  -17.054 33.426  1.00 21.15 ? 165 ILE B C   1 
ATOM   2909 O O   . ILE B 1 163 ? -2.018  -16.417 33.996  1.00 20.42 ? 165 ILE B O   1 
ATOM   2910 C CB  . ILE B 1 163 ? -2.390  -18.638 31.981  1.00 21.36 ? 165 ILE B CB  1 
ATOM   2911 C CG1 . ILE B 1 163 ? -2.418  -20.084 31.414  1.00 22.13 ? 165 ILE B CG1 1 
ATOM   2912 C CG2 . ILE B 1 163 ? -2.142  -17.592 30.865  1.00 22.40 ? 165 ILE B CG2 1 
ATOM   2913 C CD1 . ILE B 1 163 ? -3.475  -20.342 30.428  1.00 23.18 ? 165 ILE B CD1 1 
ATOM   2914 N N   . TRP B 1 164 ? 0.064   -16.536 33.045  1.00 22.37 ? 166 TRP B N   1 
ATOM   2915 C CA  . TRP B 1 164 ? 0.555   -15.197 33.249  1.00 22.83 ? 166 TRP B CA  1 
ATOM   2916 C C   . TRP B 1 164 ? 0.112   -14.364 32.041  1.00 24.24 ? 166 TRP B C   1 
ATOM   2917 O O   . TRP B 1 164 ? 0.299   -14.751 30.891  1.00 23.42 ? 166 TRP B O   1 
ATOM   2918 C CB  . TRP B 1 164 ? 2.084   -15.183 33.408  1.00 23.68 ? 166 TRP B CB  1 
ATOM   2919 C CG  . TRP B 1 164 ? 2.581   -15.639 34.740  1.00 25.46 ? 166 TRP B CG  1 
ATOM   2920 C CD1 . TRP B 1 164 ? 2.066   -16.641 35.504  1.00 26.29 ? 166 TRP B CD1 1 
ATOM   2921 C CD2 . TRP B 1 164 ? 3.723   -15.141 35.450  1.00 26.54 ? 166 TRP B CD2 1 
ATOM   2922 N NE1 . TRP B 1 164 ? 2.805   -16.794 36.644  1.00 26.48 ? 166 TRP B NE1 1 
ATOM   2923 C CE2 . TRP B 1 164 ? 3.840   -15.900 36.633  1.00 27.50 ? 166 TRP B CE2 1 
ATOM   2924 C CE3 . TRP B 1 164 ? 4.667   -14.142 35.196  1.00 27.84 ? 166 TRP B CE3 1 
ATOM   2925 C CZ2 . TRP B 1 164 ? 4.825   -15.647 37.592  1.00 28.58 ? 166 TRP B CZ2 1 
ATOM   2926 C CZ3 . TRP B 1 164 ? 5.682   -13.925 36.121  1.00 28.67 ? 166 TRP B CZ3 1 
ATOM   2927 C CH2 . TRP B 1 164 ? 5.749   -14.680 37.304  1.00 29.87 ? 166 TRP B CH2 1 
ATOM   2928 N N   . THR B 1 165 ? -0.494  -13.208 32.311  1.00 25.41 ? 167 THR B N   1 
ATOM   2929 C CA  . THR B 1 165 ? -0.868  -12.260 31.285  1.00 26.25 ? 167 THR B CA  1 
ATOM   2930 C C   . THR B 1 165 ? -0.202  -10.937 31.580  1.00 26.32 ? 167 THR B C   1 
ATOM   2931 O O   . THR B 1 165 ? 0.302   -10.699 32.699  1.00 26.61 ? 167 THR B O   1 
ATOM   2932 C CB  . THR B 1 165 ? -2.428  -12.188 31.079  1.00 29.47 ? 167 THR B CB  1 
ATOM   2933 O OG1 . THR B 1 165 ? -3.019  -11.310 32.056  1.00 30.49 ? 167 THR B OG1 1 
ATOM   2934 C CG2 . THR B 1 165 ? -3.085  -13.561 31.099  1.00 29.89 ? 167 THR B CG2 1 
ATOM   2935 N N   . THR B 1 166 ? -0.182  -10.065 30.568  1.00 26.02 ? 168 THR B N   1 
ATOM   2936 C CA  . THR B 1 166 ? 0.655   -8.859  30.583  1.00 27.94 ? 168 THR B CA  1 
ATOM   2937 C C   . THR B 1 166 ? 0.087   -7.625  31.327  1.00 27.74 ? 168 THR B C   1 
ATOM   2938 O O   . THR B 1 166 ? 0.872   -6.756  31.748  1.00 26.85 ? 168 THR B O   1 
ATOM   2939 C CB  . THR B 1 166 ? 1.003   -8.497  29.118  1.00 31.95 ? 168 THR B CB  1 
ATOM   2940 O OG1 . THR B 1 166 ? 2.103   -7.592  29.112  1.00 35.14 ? 168 THR B OG1 1 
ATOM   2941 C CG2 . THR B 1 166 ? -0.210  -7.946  28.319  1.00 32.37 ? 168 THR B CG2 1 
ATOM   2942 N N   . GLU B 1 167 ? -1.258  -7.532  31.469  1.00 27.58 ? 169 GLU B N   1 
ATOM   2943 C CA  . GLU B 1 167 ? -1.926  -6.293  31.915  1.00 28.02 ? 169 GLU B CA  1 
ATOM   2944 C C   . GLU B 1 167 ? -3.168  -6.599  32.745  1.00 29.93 ? 169 GLU B C   1 
ATOM   2945 O O   . GLU B 1 167 ? -4.212  -6.941  32.176  1.00 28.98 ? 169 GLU B O   1 
ATOM   2946 C CB  . GLU B 1 167 ? -2.295  -5.415  30.693  1.00 25.13 ? 169 GLU B CB  1 
ATOM   2947 C CG  . GLU B 1 167 ? -2.980  -4.085  30.991  1.00 26.92 ? 169 GLU B CG  1 
ATOM   2948 C CD  . GLU B 1 167 ? -2.331  -3.318  32.118  1.00 35.01 ? 169 GLU B CD  1 
ATOM   2949 O OE1 . GLU B 1 167 ? -1.234  -2.763  31.913  1.00 39.11 ? 169 GLU B OE1 1 
ATOM   2950 O OE2 . GLU B 1 167 ? -2.905  -3.302  33.223  1.00 38.46 ? 169 GLU B OE2 1 
ATOM   2951 N N   . CYS B 1 168 ? -3.079  -6.479  34.077  1.00 32.46 ? 170 CYS B N   1 
ATOM   2952 C CA  . CYS B 1 168 ? -4.230  -6.819  34.915  1.00 36.10 ? 170 CYS B CA  1 
ATOM   2953 C C   . CYS B 1 168 ? -5.413  -5.887  34.730  1.00 36.50 ? 170 CYS B C   1 
ATOM   2954 O O   . CYS B 1 168 ? -6.474  -6.269  35.163  1.00 38.63 ? 170 CYS B O   1 
ATOM   2955 C CB  . CYS B 1 168 ? -3.830  -6.922  36.385  1.00 39.70 ? 170 CYS B CB  1 
ATOM   2956 S SG  . CYS B 1 168 ? -3.308  -5.334  37.107  1.00 47.90 ? 170 CYS B SG  1 
ATOM   2957 N N   . GLU B 1 169 ? -5.281  -4.694  34.100  1.00 34.82 ? 171 GLU B N   1 
ATOM   2958 C CA  . GLU B 1 169 ? -6.417  -3.804  33.877  1.00 33.78 ? 171 GLU B CA  1 
ATOM   2959 C C   . GLU B 1 169 ? -7.158  -4.048  32.544  1.00 33.84 ? 171 GLU B C   1 
ATOM   2960 O O   . GLU B 1 169 ? -8.143  -3.358  32.258  1.00 33.64 ? 171 GLU B O   1 
ATOM   2961 C CB  . GLU B 1 169 ? -5.991  -2.300  33.978  1.00 33.30 ? 171 GLU B CB  1 
ATOM   2962 C CG  . GLU B 1 169 ? -5.288  -1.920  35.270  1.00 30.87 ? 171 GLU B CG  1 
ATOM   2963 C CD  . GLU B 1 169 ? -6.051  -2.077  36.581  1.00 34.62 ? 171 GLU B CD  1 
ATOM   2964 O OE1 . GLU B 1 169 ? -7.306  -2.101  36.586  1.00 34.75 ? 171 GLU B OE1 1 
ATOM   2965 O OE2 . GLU B 1 169 ? -5.374  -2.152  37.627  1.00 39.28 ? 171 GLU B OE2 1 
ATOM   2966 N N   . ASN B 1 170 ? -6.691  -5.002  31.724  1.00 33.84 ? 172 ASN B N   1 
ATOM   2967 C CA  . ASN B 1 170 ? -7.407  -5.430  30.503  1.00 33.86 ? 172 ASN B CA  1 
ATOM   2968 C C   . ASN B 1 170 ? -8.450  -6.480  30.880  1.00 32.81 ? 172 ASN B C   1 
ATOM   2969 O O   . ASN B 1 170 ? -8.258  -7.676  30.651  1.00 31.05 ? 172 ASN B O   1 
ATOM   2970 C CB  . ASN B 1 170 ? -6.435  -6.003  29.463  1.00 35.61 ? 172 ASN B CB  1 
ATOM   2971 C CG  . ASN B 1 170 ? -5.696  -4.969  28.645  1.00 36.73 ? 172 ASN B CG  1 
ATOM   2972 O OD1 . ASN B 1 170 ? -5.992  -3.772  28.671  1.00 37.98 ? 172 ASN B OD1 1 
ATOM   2973 N ND2 . ASN B 1 170 ? -4.714  -5.433  27.886  1.00 34.65 ? 172 ASN B ND2 1 
ATOM   2974 N N   . ARG B 1 171 ? -9.578  -6.024  31.462  1.00 33.77 ? 173 ARG B N   1 
ATOM   2975 C CA  . ARG B 1 171 ? -10.571 -6.957  31.998  1.00 35.68 ? 173 ARG B CA  1 
ATOM   2976 C C   . ARG B 1 171 ? -11.126 -7.876  30.914  1.00 35.03 ? 173 ARG B C   1 
ATOM   2977 O O   . ARG B 1 171 ? -11.213 -9.074  31.138  1.00 33.79 ? 173 ARG B O   1 
ATOM   2978 C CB  . ARG B 1 171 ? -11.688 -6.185  32.716  1.00 38.99 ? 173 ARG B CB  1 
ATOM   2979 C CG  . ARG B 1 171 ? -12.846 -7.019  33.313  1.00 42.18 ? 173 ARG B CG  1 
ATOM   2980 C CD  . ARG B 1 171 ? -13.963 -7.306  32.316  1.00 47.88 ? 173 ARG B CD  1 
ATOM   2981 N NE  . ARG B 1 171 ? -14.496 -6.080  31.723  1.00 51.77 ? 173 ARG B NE  1 
ATOM   2982 C CZ  . ARG B 1 171 ? -15.186 -5.999  30.589  1.00 55.34 ? 173 ARG B CZ  1 
ATOM   2983 N NH1 . ARG B 1 171 ? -15.442 -7.088  29.879  1.00 55.98 ? 173 ARG B NH1 1 
ATOM   2984 N NH2 . ARG B 1 171 ? -15.618 -4.817  30.149  1.00 56.16 ? 173 ARG B NH2 1 
ATOM   2985 N N   . GLU B 1 172 ? -11.493 -7.327  29.739  1.00 35.30 ? 174 GLU B N   1 
ATOM   2986 C CA  . GLU B 1 172 ? -12.104 -8.112  28.645  1.00 35.25 ? 174 GLU B CA  1 
ATOM   2987 C C   . GLU B 1 172 ? -11.154 -9.233  28.134  1.00 33.56 ? 174 GLU B C   1 
ATOM   2988 O O   . GLU B 1 172 ? -11.609 -10.356 27.824  1.00 31.68 ? 174 GLU B O   1 
ATOM   2989 C CB  . GLU B 1 172 ? -12.529 -7.173  27.510  1.00 38.91 ? 174 GLU B CB  1 
ATOM   2990 C CG  . GLU B 1 172 ? -13.225 -7.838  26.331  1.00 55.11 ? 174 GLU B CG  1 
ATOM   2991 C CD  . GLU B 1 172 ? -14.736 -8.011  26.387  1.00 74.96 ? 174 GLU B CD  1 
ATOM   2992 O OE1 . GLU B 1 172 ? -15.373 -7.995  25.304  1.00 78.75 ? 174 GLU B OE1 1 
ATOM   2993 O OE2 . GLU B 1 172 ? -15.285 -8.172  27.504  1.00 81.26 ? 174 GLU B OE2 1 
ATOM   2994 N N   . ALA B 1 173 ? -9.839  -8.933  28.049  1.00 33.05 ? 175 ALA B N   1 
ATOM   2995 C CA  . ALA B 1 173 ? -8.838  -9.929  27.622  1.00 32.31 ? 175 ALA B CA  1 
ATOM   2996 C C   . ALA B 1 173 ? -8.670  -11.027 28.697  1.00 30.73 ? 175 ALA B C   1 
ATOM   2997 O O   . ALA B 1 173 ? -8.659  -12.232 28.402  1.00 28.87 ? 175 ALA B O   1 
ATOM   2998 C CB  . ALA B 1 173 ? -7.495  -9.229  27.343  1.00 31.61 ? 175 ALA B CB  1 
ATOM   2999 N N   . VAL B 1 174 ? -8.551  -10.561 29.944  1.00 30.70 ? 176 VAL B N   1 
ATOM   3000 C CA  . VAL B 1 174 ? -8.222  -11.352 31.085  1.00 30.62 ? 176 VAL B CA  1 
ATOM   3001 C C   . VAL B 1 174 ? -9.344  -12.338 31.341  1.00 31.21 ? 176 VAL B C   1 
ATOM   3002 O O   . VAL B 1 174 ? -9.083  -13.538 31.499  1.00 31.35 ? 176 VAL B O   1 
ATOM   3003 C CB  . VAL B 1 174 ? -7.890  -10.448 32.316  1.00 29.92 ? 176 VAL B CB  1 
ATOM   3004 C CG1 . VAL B 1 174 ? -7.956  -11.188 33.617  1.00 30.69 ? 176 VAL B CG1 1 
ATOM   3005 C CG2 . VAL B 1 174 ? -6.524  -9.781  32.159  1.00 29.43 ? 176 VAL B CG2 1 
ATOM   3006 N N   . THR B 1 175 ? -10.572 -11.849 31.393  1.00 31.19 ? 177 THR B N   1 
ATOM   3007 C CA  . THR B 1 175 ? -11.698 -12.683 31.769  1.00 32.29 ? 177 THR B CA  1 
ATOM   3008 C C   . THR B 1 175 ? -11.965 -13.707 30.627  1.00 32.82 ? 177 THR B C   1 
ATOM   3009 O O   . THR B 1 175 ? -12.310 -14.885 30.905  1.00 33.76 ? 177 THR B O   1 
ATOM   3010 C CB  . THR B 1 175 ? -12.895 -11.815 32.234  1.00 36.12 ? 177 THR B CB  1 
ATOM   3011 O OG1 . THR B 1 175 ? -13.356 -10.963 31.180  1.00 39.37 ? 177 THR B OG1 1 
ATOM   3012 C CG2 . THR B 1 175 ? -12.542 -10.900 33.417  1.00 35.88 ? 177 THR B CG2 1 
ATOM   3013 N N   . HIS B 1 176 ? -11.806 -13.305 29.366  1.00 33.12 ? 178 HIS B N   1 
ATOM   3014 C CA  . HIS B 1 176 ? -11.950 -14.246 28.241  1.00 33.79 ? 178 HIS B CA  1 
ATOM   3015 C C   . HIS B 1 176 ? -10.913 -15.360 28.313  1.00 31.97 ? 178 HIS B C   1 
ATOM   3016 O O   . HIS B 1 176 ? -11.243 -16.538 28.133  1.00 31.83 ? 178 HIS B O   1 
ATOM   3017 C CB  . HIS B 1 176 ? -11.838 -13.511 26.894  1.00 37.42 ? 178 HIS B CB  1 
ATOM   3018 C CG  . HIS B 1 176 ? -11.810 -14.418 25.693  1.00 44.83 ? 178 HIS B CG  1 
ATOM   3019 N ND1 . HIS B 1 176 ? -10.588 -14.760 25.118  1.00 48.61 ? 178 HIS B ND1 1 
ATOM   3020 C CD2 . HIS B 1 176 ? -12.786 -15.051 25.006  1.00 47.20 ? 178 HIS B CD2 1 
ATOM   3021 C CE1 . HIS B 1 176 ? -10.858 -15.561 24.106  1.00 50.42 ? 178 HIS B CE1 1 
ATOM   3022 N NE2 . HIS B 1 176 ? -12.147 -15.779 23.984  1.00 49.54 ? 178 HIS B NE2 1 
ATOM   3023 N N   . ILE B 1 177 ? -9.642  -15.019 28.568  1.00 30.65 ? 179 ILE B N   1 
ATOM   3024 C CA  . ILE B 1 177 ? -8.610  -16.036 28.815  1.00 29.59 ? 179 ILE B CA  1 
ATOM   3025 C C   . ILE B 1 177 ? -9.045  -17.027 29.917  1.00 30.12 ? 179 ILE B C   1 
ATOM   3026 O O   . ILE B 1 177 ? -8.921  -18.254 29.739  1.00 31.85 ? 179 ILE B O   1 
ATOM   3027 C CB  . ILE B 1 177 ? -7.225  -15.408 29.197  1.00 27.88 ? 179 ILE B CB  1 
ATOM   3028 C CG1 . ILE B 1 177 ? -6.567  -14.695 28.006  1.00 26.32 ? 179 ILE B CG1 1 
ATOM   3029 C CG2 . ILE B 1 177 ? -6.258  -16.494 29.767  1.00 26.80 ? 179 ILE B CG2 1 
ATOM   3030 C CD1 . ILE B 1 177 ? -5.571  -13.675 28.368  1.00 26.85 ? 179 ILE B CD1 1 
ATOM   3031 N N   . GLY B 1 178 ? -9.525  -16.479 31.012  1.00 28.36 ? 180 GLY B N   1 
ATOM   3032 C CA  . GLY B 1 178 ? -9.889  -17.252 32.190  1.00 28.91 ? 180 GLY B CA  1 
ATOM   3033 C C   . GLY B 1 178 ? -11.010 -18.206 31.900  1.00 29.53 ? 180 GLY B C   1 
ATOM   3034 O O   . GLY B 1 178 ? -10.981 -19.354 32.331  1.00 29.15 ? 180 GLY B O   1 
ATOM   3035 N N   . ARG B 1 179 ? -11.986 -17.740 31.162  1.00 31.02 ? 181 ARG B N   1 
ATOM   3036 C CA  . ARG B 1 179 ? -13.186 -18.515 30.819  1.00 32.03 ? 181 ARG B CA  1 
ATOM   3037 C C   . ARG B 1 179 ? -12.867 -19.693 29.896  1.00 31.77 ? 181 ARG B C   1 
ATOM   3038 O O   . ARG B 1 179 ? -13.337 -20.807 30.121  1.00 31.03 ? 181 ARG B O   1 
ATOM   3039 C CB  . ARG B 1 179 ? -14.160 -17.585 30.101  1.00 34.51 ? 181 ARG B CB  1 
ATOM   3040 C CG  . ARG B 1 179 ? -15.572 -17.983 30.167  1.00 44.80 ? 181 ARG B CG  1 
ATOM   3041 C CD  . ARG B 1 179 ? -16.194 -17.438 31.426  1.00 49.80 ? 181 ARG B CD  1 
ATOM   3042 N NE  . ARG B 1 179 ? -16.287 -15.986 31.410  1.00 53.52 ? 181 ARG B NE  1 
ATOM   3043 C CZ  . ARG B 1 179 ? -16.863 -15.259 32.359  1.00 55.69 ? 181 ARG B CZ  1 
ATOM   3044 N NH1 . ARG B 1 179 ? -17.443 -15.853 33.413  1.00 53.49 ? 181 ARG B NH1 1 
ATOM   3045 N NH2 . ARG B 1 179 ? -16.874 -13.935 32.267  1.00 55.72 ? 181 ARG B NH2 1 
ATOM   3046 N N   . VAL B 1 180 ? -12.098 -19.419 28.830  1.00 31.81 ? 182 VAL B N   1 
ATOM   3047 C CA  . VAL B 1 180 ? -11.645 -20.434 27.860  1.00 31.94 ? 182 VAL B CA  1 
ATOM   3048 C C   . VAL B 1 180 ? -10.689 -21.406 28.542  1.00 30.79 ? 182 VAL B C   1 
ATOM   3049 O O   . VAL B 1 180 ? -10.784 -22.617 28.338  1.00 31.64 ? 182 VAL B O   1 
ATOM   3050 C CB  . VAL B 1 180 ? -10.986 -19.733 26.660  1.00 33.95 ? 182 VAL B CB  1 
ATOM   3051 C CG1 . VAL B 1 180 ? -10.332 -20.719 25.722  1.00 35.36 ? 182 VAL B CG1 1 
ATOM   3052 C CG2 . VAL B 1 180 ? -12.019 -18.877 25.909  1.00 35.59 ? 182 VAL B CG2 1 
ATOM   3053 N N   . TYR B 1 181 ? -9.784  -20.895 29.343  1.00 28.48 ? 183 TYR B N   1 
ATOM   3054 C CA  . TYR B 1 181 ? -8.873  -21.755 30.116  1.00 29.10 ? 183 TYR B CA  1 
ATOM   3055 C C   . TYR B 1 181 ? -9.601  -22.710 31.064  1.00 31.42 ? 183 TYR B C   1 
ATOM   3056 O O   . TYR B 1 181 ? -9.274  -23.897 31.092  1.00 33.36 ? 183 TYR B O   1 
ATOM   3057 C CB  . TYR B 1 181 ? -7.895  -20.873 30.888  1.00 27.28 ? 183 TYR B CB  1 
ATOM   3058 C CG  . TYR B 1 181 ? -6.788  -21.570 31.638  1.00 25.82 ? 183 TYR B CG  1 
ATOM   3059 C CD1 . TYR B 1 181 ? -6.138  -22.672 31.102  1.00 25.77 ? 183 TYR B CD1 1 
ATOM   3060 C CD2 . TYR B 1 181 ? -6.338  -21.081 32.858  1.00 25.84 ? 183 TYR B CD2 1 
ATOM   3061 C CE1 . TYR B 1 181 ? -5.123  -23.305 31.795  1.00 24.92 ? 183 TYR B CE1 1 
ATOM   3062 C CE2 . TYR B 1 181 ? -5.325  -21.701 33.549  1.00 24.68 ? 183 TYR B CE2 1 
ATOM   3063 C CZ  . TYR B 1 181 ? -4.709  -22.804 33.011  1.00 25.49 ? 183 TYR B CZ  1 
ATOM   3064 O OH  . TYR B 1 181 ? -3.658  -23.372 33.688  1.00 27.21 ? 183 TYR B OH  1 
ATOM   3065 N N   . LYS B 1 182 ? -10.566 -22.221 31.847  1.00 31.83 ? 184 LYS B N   1 
ATOM   3066 C CA  . LYS B 1 182 ? -11.319 -23.074 32.763  1.00 34.53 ? 184 LYS B CA  1 
ATOM   3067 C C   . LYS B 1 182 ? -12.093 -24.145 31.961  1.00 37.28 ? 184 LYS B C   1 
ATOM   3068 O O   . LYS B 1 182 ? -12.149 -25.302 32.380  1.00 38.99 ? 184 LYS B O   1 
ATOM   3069 C CB  . LYS B 1 182 ? -12.291 -22.221 33.602  1.00 36.86 ? 184 LYS B CB  1 
ATOM   3070 C CG  . LYS B 1 182 ? -13.135 -23.028 34.552  1.00 39.51 ? 184 LYS B CG  1 
ATOM   3071 C CD  . LYS B 1 182 ? -14.256 -22.205 35.089  1.00 44.18 ? 184 LYS B CD  1 
ATOM   3072 C CE  . LYS B 1 182 ? -14.919 -22.898 36.238  1.00 47.06 ? 184 LYS B CE  1 
ATOM   3073 N NZ  . LYS B 1 182 ? -15.828 -21.975 36.978  1.00 49.26 ? 184 LYS B NZ  1 
ATOM   3074 N N   . GLU B 1 183 ? -12.667 -23.749 30.807  1.00 36.73 ? 185 GLU B N   1 
ATOM   3075 C CA  . GLU B 1 183 ? -13.356 -24.647 29.849  1.00 36.50 ? 185 GLU B CA  1 
ATOM   3076 C C   . GLU B 1 183 ? -12.402 -25.784 29.350  1.00 35.77 ? 185 GLU B C   1 
ATOM   3077 O O   . GLU B 1 183 ? -12.753 -26.975 29.352  1.00 33.87 ? 185 GLU B O   1 
ATOM   3078 C CB  . GLU B 1 183 ? -13.844 -23.792 28.671  1.00 40.46 ? 185 GLU B CB  1 
ATOM   3079 C CG  . GLU B 1 183 ? -14.769 -24.410 27.648  1.00 49.14 ? 185 GLU B CG  1 
ATOM   3080 C CD  . GLU B 1 183 ? -14.684 -23.615 26.360  1.00 57.03 ? 185 GLU B CD  1 
ATOM   3081 O OE1 . GLU B 1 183 ? -14.247 -24.205 25.346  1.00 56.19 ? 185 GLU B OE1 1 
ATOM   3082 O OE2 . GLU B 1 183 ? -15.020 -22.404 26.370  1.00 61.18 ? 185 GLU B OE2 1 
ATOM   3083 N N   . ARG B 1 184 ? -11.203 -25.396 28.936  1.00 34.76 ? 186 ARG B N   1 
ATOM   3084 C CA  . ARG B 1 184 ? -10.217 -26.308 28.405  1.00 33.46 ? 186 ARG B CA  1 
ATOM   3085 C C   . ARG B 1 184 ? -9.651  -27.203 29.472  1.00 35.33 ? 186 ARG B C   1 
ATOM   3086 O O   . ARG B 1 184 ? -9.293  -28.326 29.171  1.00 35.57 ? 186 ARG B O   1 
ATOM   3087 C CB  . ARG B 1 184 ? -9.095  -25.537 27.701  1.00 32.96 ? 186 ARG B CB  1 
ATOM   3088 C CG  . ARG B 1 184 ? -9.536  -24.876 26.399  1.00 31.75 ? 186 ARG B CG  1 
ATOM   3089 C CD  . ARG B 1 184 ? -9.631  -25.866 25.239  1.00 33.01 ? 186 ARG B CD  1 
ATOM   3090 N NE  . ARG B 1 184 ? -8.319  -26.355 24.822  1.00 31.87 ? 186 ARG B NE  1 
ATOM   3091 C CZ  . ARG B 1 184 ? -7.628  -25.974 23.750  1.00 32.99 ? 186 ARG B CZ  1 
ATOM   3092 N NH1 . ARG B 1 184 ? -8.117  -25.063 22.916  1.00 33.50 ? 186 ARG B NH1 1 
ATOM   3093 N NH2 . ARG B 1 184 ? -6.441  -26.505 23.496  1.00 33.12 ? 186 ARG B NH2 1 
ATOM   3094 N N   . LEU B 1 185 ? -9.558  -26.722 30.728  1.00 36.74 ? 187 LEU B N   1 
ATOM   3095 C CA  . LEU B 1 185 ? -9.248  -27.574 31.854  1.00 38.63 ? 187 LEU B CA  1 
ATOM   3096 C C   . LEU B 1 185 ? -10.383 -28.549 32.229  1.00 42.87 ? 187 LEU B C   1 
ATOM   3097 O O   . LEU B 1 185 ? -10.118 -29.482 32.973  1.00 43.46 ? 187 LEU B O   1 
ATOM   3098 C CB  . LEU B 1 185 ? -8.815  -26.718 33.056  1.00 37.95 ? 187 LEU B CB  1 
ATOM   3099 C CG  . LEU B 1 185 ? -7.442  -25.992 32.917  1.00 38.91 ? 187 LEU B CG  1 
ATOM   3100 C CD1 . LEU B 1 185 ? -7.036  -25.352 34.204  1.00 39.52 ? 187 LEU B CD1 1 
ATOM   3101 C CD2 . LEU B 1 185 ? -6.324  -26.962 32.589  1.00 38.19 ? 187 LEU B CD2 1 
ATOM   3102 N N   . GLY B 1 186 ? -11.606 -28.354 31.704  1.00 45.40 ? 188 GLY B N   1 
ATOM   3103 C CA  . GLY B 1 186 ? -12.788 -29.112 32.085  1.00 48.00 ? 188 GLY B CA  1 
ATOM   3104 C C   . GLY B 1 186 ? -13.113 -29.040 33.552  1.00 51.95 ? 188 GLY B C   1 
ATOM   3105 O O   . GLY B 1 186 ? -13.668 -29.985 34.103  1.00 52.73 ? 188 GLY B O   1 
ATOM   3106 N N   . LEU B 1 187 ? -12.779 -27.923 34.200  1.00 54.38 ? 189 LEU B N   1 
ATOM   3107 C CA  . LEU B 1 187 ? -13.196 -27.686 35.567  1.00 56.32 ? 189 LEU B CA  1 
ATOM   3108 C C   . LEU B 1 187 ? -14.713 -27.484 35.586  1.00 59.28 ? 189 LEU B C   1 
ATOM   3109 O O   . LEU B 1 187 ? -15.252 -26.829 34.682  1.00 59.62 ? 189 LEU B O   1 
ATOM   3110 C CB  . LEU B 1 187 ? -12.532 -26.437 36.130  1.00 55.79 ? 189 LEU B CB  1 
ATOM   3111 C CG  . LEU B 1 187 ? -11.010 -26.439 36.223  1.00 56.30 ? 189 LEU B CG  1 
ATOM   3112 C CD1 . LEU B 1 187 ? -10.511 -25.105 36.738  1.00 56.41 ? 189 LEU B CD1 1 
ATOM   3113 C CD2 . LEU B 1 187 ? -10.504 -27.572 37.094  1.00 55.96 ? 189 LEU B CD2 1 
ATOM   3114 N N   . PRO B 1 188 ? -15.418 -28.028 36.599  1.00 60.75 ? 190 PRO B N   1 
ATOM   3115 C CA  . PRO B 1 188 ? -16.856 -27.750 36.693  1.00 61.59 ? 190 PRO B CA  1 
ATOM   3116 C C   . PRO B 1 188 ? -17.119 -26.290 37.019  1.00 63.17 ? 190 PRO B C   1 
ATOM   3117 O O   . PRO B 1 188 ? -16.286 -25.620 37.649  1.00 63.42 ? 190 PRO B O   1 
ATOM   3118 C CB  . PRO B 1 188 ? -17.351 -28.649 37.826  1.00 62.37 ? 190 PRO B CB  1 
ATOM   3119 C CG  . PRO B 1 188 ? -16.185 -29.374 38.347  1.00 62.82 ? 190 PRO B CG  1 
ATOM   3120 C CD  . PRO B 1 188 ? -14.941 -28.897 37.692  1.00 60.82 ? 190 PRO B CD  1 
ATOM   3121 N N   . PRO B 1 189 ? -18.285 -25.768 36.614  1.00 63.92 ? 191 PRO B N   1 
ATOM   3122 C CA  . PRO B 1 189 ? -18.533 -24.321 36.809  1.00 64.08 ? 191 PRO B CA  1 
ATOM   3123 C C   . PRO B 1 189 ? -18.586 -23.847 38.264  1.00 63.90 ? 191 PRO B C   1 
ATOM   3124 O O   . PRO B 1 189 ? -18.515 -22.648 38.502  1.00 63.18 ? 191 PRO B O   1 
ATOM   3125 C CB  . PRO B 1 189 ? -19.851 -24.063 36.073  1.00 64.64 ? 191 PRO B CB  1 
ATOM   3126 C CG  . PRO B 1 189 ? -20.471 -25.397 35.842  1.00 65.23 ? 191 PRO B CG  1 
ATOM   3127 C CD  . PRO B 1 189 ? -19.419 -26.453 35.957  1.00 63.84 ? 191 PRO B CD  1 
ATOM   3128 N N   . LYS B 1 190 ? -18.712 -24.811 39.221  1.00 64.54 ? 192 LYS B N   1 
ATOM   3129 C CA  . LYS B 1 190 ? -18.729 -24.620 40.681  1.00 64.96 ? 192 LYS B CA  1 
ATOM   3130 C C   . LYS B 1 190 ? -17.328 -24.327 41.201  1.00 64.43 ? 192 LYS B C   1 
ATOM   3131 O O   . LYS B 1 190 ? -17.190 -23.599 42.193  1.00 65.26 ? 192 LYS B O   1 
ATOM   3132 C CB  . LYS B 1 190 ? -19.186 -25.911 41.412  1.00 67.48 ? 192 LYS B CB  1 
ATOM   3133 C CG  . LYS B 1 190 ? -20.494 -26.575 40.968  1.00 72.20 ? 192 LYS B CG  1 
ATOM   3134 C CD  . LYS B 1 190 ? -20.531 -28.045 41.478  1.00 76.18 ? 192 LYS B CD  1 
ATOM   3135 C CE  . LYS B 1 190 ? -21.738 -28.841 41.035  1.00 78.10 ? 192 LYS B CE  1 
ATOM   3136 N NZ  . LYS B 1 190 ? -22.810 -28.840 42.056  1.00 79.48 ? 192 LYS B NZ  1 
ATOM   3137 N N   . ILE B 1 191 ? -16.285 -24.917 40.555  1.00 62.77 ? 193 ILE B N   1 
ATOM   3138 C CA  . ILE B 1 191 ? -14.886 -24.674 40.897  1.00 61.14 ? 193 ILE B CA  1 
ATOM   3139 C C   . ILE B 1 191 ? -14.562 -23.323 40.297  1.00 58.84 ? 193 ILE B C   1 
ATOM   3140 O O   . ILE B 1 191 ? -14.507 -23.207 39.088  1.00 59.34 ? 193 ILE B O   1 
ATOM   3141 C CB  . ILE B 1 191 ? -13.977 -25.802 40.330  1.00 61.65 ? 193 ILE B CB  1 
ATOM   3142 C CG1 . ILE B 1 191 ? -14.363 -27.190 40.931  1.00 62.64 ? 193 ILE B CG1 1 
ATOM   3143 C CG2 . ILE B 1 191 ? -12.492 -25.477 40.560  1.00 61.97 ? 193 ILE B CG2 1 
ATOM   3144 C CD1 . ILE B 1 191 ? -14.409 -27.280 42.492  1.00 64.21 ? 193 ILE B CD1 1 
ATOM   3145 N N   . VAL B 1 192 ? -14.361 -22.308 41.126  1.00 56.52 ? 194 VAL B N   1 
ATOM   3146 C CA  . VAL B 1 192 ? -14.082 -20.959 40.643  1.00 54.36 ? 194 VAL B CA  1 
ATOM   3147 C C   . VAL B 1 192 ? -12.585 -20.707 40.630  1.00 50.82 ? 194 VAL B C   1 
ATOM   3148 O O   . VAL B 1 192 ? -11.920 -20.971 41.628  1.00 50.77 ? 194 VAL B O   1 
ATOM   3149 C CB  . VAL B 1 192 ? -14.827 -19.874 41.454  1.00 55.61 ? 194 VAL B CB  1 
ATOM   3150 C CG1 . VAL B 1 192 ? -16.316 -20.183 41.560  1.00 55.59 ? 194 VAL B CG1 1 
ATOM   3151 C CG2 . VAL B 1 192 ? -14.209 -19.681 42.836  1.00 56.96 ? 194 VAL B CG2 1 
ATOM   3152 N N   . ILE B 1 193 ? -12.047 -20.200 39.494  1.00 47.65 ? 195 ILE B N   1 
ATOM   3153 C CA  . ILE B 1 193 ? -10.632 -19.837 39.419  1.00 44.21 ? 195 ILE B CA  1 
ATOM   3154 C C   . ILE B 1 193 ? -10.500 -18.344 39.582  1.00 41.74 ? 195 ILE B C   1 
ATOM   3155 O O   . ILE B 1 193 ? -11.436 -17.605 39.277  1.00 40.86 ? 195 ILE B O   1 
ATOM   3156 C CB  . ILE B 1 193 ? -9.891  -20.401 38.176  1.00 43.12 ? 195 ILE B CB  1 
ATOM   3157 C CG1 . ILE B 1 193 ? -10.406 -19.811 36.864  1.00 42.61 ? 195 ILE B CG1 1 
ATOM   3158 C CG2 . ILE B 1 193 ? -10.013 -21.897 38.165  1.00 44.11 ? 195 ILE B CG2 1 
ATOM   3159 C CD1 . ILE B 1 193 ? -9.561  -20.100 35.645  1.00 43.05 ? 195 ILE B CD1 1 
ATOM   3160 N N   . GLY B 1 194 ? -9.331  -17.923 40.066  1.00 39.70 ? 196 GLY B N   1 
ATOM   3161 C CA  . GLY B 1 194 ? -9.088  -16.540 40.413  1.00 38.21 ? 196 GLY B CA  1 
ATOM   3162 C C   . GLY B 1 194 ? -7.911  -15.951 39.656  1.00 37.44 ? 196 GLY B C   1 
ATOM   3163 O O   . GLY B 1 194 ? -6.910  -16.634 39.414  1.00 37.45 ? 196 GLY B O   1 
ATOM   3164 N N   . TYR B 1 195 ? -8.014  -14.654 39.288  1.00 36.42 ? 197 TYR B N   1 
ATOM   3165 C CA  . TYR B 1 195 ? -6.957  -13.924 38.588  1.00 33.92 ? 197 TYR B CA  1 
ATOM   3166 C C   . TYR B 1 195 ? -6.357  -12.990 39.605  1.00 32.54 ? 197 TYR B C   1 
ATOM   3167 O O   . TYR B 1 195 ? -7.104  -12.224 40.192  1.00 32.57 ? 197 TYR B O   1 
ATOM   3168 C CB  . TYR B 1 195 ? -7.480  -13.135 37.392  1.00 32.44 ? 197 TYR B CB  1 
ATOM   3169 C CG  . TYR B 1 195 ? -6.380  -12.378 36.649  1.00 32.07 ? 197 TYR B CG  1 
ATOM   3170 C CD1 . TYR B 1 195 ? -5.694  -12.963 35.591  1.00 32.08 ? 197 TYR B CD1 1 
ATOM   3171 C CD2 . TYR B 1 195 ? -6.041  -11.075 36.998  1.00 31.51 ? 197 TYR B CD2 1 
ATOM   3172 C CE1 . TYR B 1 195 ? -4.689  -12.274 34.910  1.00 32.66 ? 197 TYR B CE1 1 
ATOM   3173 C CE2 . TYR B 1 195 ? -5.018  -10.392 36.347  1.00 31.51 ? 197 TYR B CE2 1 
ATOM   3174 C CZ  . TYR B 1 195 ? -4.349  -10.986 35.290  1.00 31.39 ? 197 TYR B CZ  1 
ATOM   3175 O OH  . TYR B 1 195 ? -3.340  -10.288 34.627  1.00 29.82 ? 197 TYR B OH  1 
ATOM   3176 N N   . GLN B 1 196 ? -5.028  -13.070 39.823  1.00 31.36 ? 198 GLN B N   1 
ATOM   3177 C CA  . GLN B 1 196 ? -4.290  -12.295 40.801  1.00 31.61 ? 198 GLN B CA  1 
ATOM   3178 C C   . GLN B 1 196 ? -3.266  -11.404 40.115  1.00 32.39 ? 198 GLN B C   1 
ATOM   3179 O O   . GLN B 1 196 ? -2.385  -11.897 39.420  1.00 32.35 ? 198 GLN B O   1 
ATOM   3180 C CB  . GLN B 1 196 ? -3.524  -13.210 41.772  1.00 31.49 ? 198 GLN B CB  1 
ATOM   3181 C CG  . GLN B 1 196 ? -4.350  -14.307 42.435  1.00 38.71 ? 198 GLN B CG  1 
ATOM   3182 C CD  . GLN B 1 196 ? -3.462  -15.323 43.141  1.00 46.54 ? 198 GLN B CD  1 
ATOM   3183 O OE1 . GLN B 1 196 ? -2.573  -15.947 42.556  1.00 49.41 ? 198 GLN B OE1 1 
ATOM   3184 N NE2 . GLN B 1 196 ? -3.688  -15.523 44.412  1.00 48.37 ? 198 GLN B NE2 1 
ATOM   3185 N N   . SER B 1 197 ? -3.353  -10.089 40.325  1.00 33.76 ? 199 SER B N   1 
ATOM   3186 C CA  . SER B 1 197 ? -2.289  -9.143  39.951  1.00 34.23 ? 199 SER B CA  1 
ATOM   3187 C C   . SER B 1 197 ? -0.932  -9.600  40.558  1.00 32.24 ? 199 SER B C   1 
ATOM   3188 O O   . SER B 1 197 ? -0.885  -10.096 41.689  1.00 33.77 ? 199 SER B O   1 
ATOM   3189 C CB  . SER B 1 197 ? -2.676  -7.739  40.430  1.00 38.69 ? 199 SER B CB  1 
ATOM   3190 O OG  . SER B 1 197 ? -1.652  -6.776  40.250  1.00 45.25 ? 199 SER B OG  1 
ATOM   3191 N N   . HIS B 1 198 ? 0.116   -9.492  39.816  1.00 31.01 ? 200 HIS B N   1 
ATOM   3192 C CA  . HIS B 1 198 ? 1.475   -9.806  40.301  1.00 33.47 ? 200 HIS B CA  1 
ATOM   3193 C C   . HIS B 1 198 ? 1.863   -8.877  41.454  1.00 35.91 ? 200 HIS B C   1 
ATOM   3194 O O   . HIS B 1 198 ? 2.546   -9.305  42.386  1.00 36.69 ? 200 HIS B O   1 
ATOM   3195 C CB  . HIS B 1 198 ? 2.510   -9.707  39.181  1.00 32.71 ? 200 HIS B CB  1 
ATOM   3196 C CG  . HIS B 1 198 ? 2.460   -10.803 38.163  1.00 33.15 ? 200 HIS B CG  1 
ATOM   3197 N ND1 . HIS B 1 198 ? 2.240   -12.126 38.471  1.00 34.03 ? 200 HIS B ND1 1 
ATOM   3198 C CD2 . HIS B 1 198 ? 2.565   -10.694 36.824  1.00 33.47 ? 200 HIS B CD2 1 
ATOM   3199 C CE1 . HIS B 1 198 ? 2.251   -12.763 37.300  1.00 34.47 ? 200 HIS B CE1 1 
ATOM   3200 N NE2 . HIS B 1 198 ? 2.437   -11.956 36.308  1.00 33.43 ? 200 HIS B NE2 1 
ATOM   3201 N N   . ALA B 1 199 ? 1.407   -7.617  41.391  1.00 37.83 ? 201 ALA B N   1 
ATOM   3202 C CA  . ALA B 1 199 ? 1.660   -6.624  42.454  1.00 39.34 ? 201 ALA B CA  1 
ATOM   3203 C C   . ALA B 1 199 ? 1.079   -7.048  43.821  1.00 41.24 ? 201 ALA B C   1 
ATOM   3204 O O   . ALA B 1 199 ? 1.677   -6.758  44.853  1.00 40.89 ? 201 ALA B O   1 
ATOM   3205 C CB  . ALA B 1 199 ? 1.097   -5.297  42.035  1.00 39.37 ? 201 ALA B CB  1 
ATOM   3206 N N   . ASP B 1 200 ? -0.075  -7.726  43.835  1.00 41.86 ? 202 ASP B N   1 
ATOM   3207 C CA  . ASP B 1 200 ? -0.645  -8.259  45.070  1.00 42.93 ? 202 ASP B CA  1 
ATOM   3208 C C   . ASP B 1 200 ? 0.098   -9.533  45.492  1.00 45.30 ? 202 ASP B C   1 
ATOM   3209 O O   . ASP B 1 200 ? 0.436   -9.686  46.674  1.00 45.35 ? 202 ASP B O   1 
ATOM   3210 C CB  . ASP B 1 200 ? -2.161  -8.524  44.895  1.00 43.14 ? 202 ASP B CB  1 
ATOM   3211 C CG  . ASP B 1 200 ? -2.946  -7.258  44.549  1.00 46.67 ? 202 ASP B CG  1 
ATOM   3212 O OD1 . ASP B 1 200 ? -2.431  -6.141  44.827  1.00 48.96 ? 202 ASP B OD1 1 
ATOM   3213 O OD2 . ASP B 1 200 ? -4.077  -7.377  43.998  1.00 45.90 ? 202 ASP B OD2 1 
ATOM   3214 N N   . THR B 1 201 ? 0.361   -10.448 44.537  1.00 46.48 ? 203 THR B N   1 
ATOM   3215 C CA  . THR B 1 201 ? 1.088   -11.698 44.811  1.00 48.08 ? 203 THR B CA  1 
ATOM   3216 C C   . THR B 1 201 ? 2.499   -11.462 45.331  1.00 49.06 ? 203 THR B C   1 
ATOM   3217 O O   . THR B 1 201 ? 3.016   -12.297 46.072  1.00 49.32 ? 203 THR B O   1 
ATOM   3218 C CB  . THR B 1 201 ? 1.139   -12.565 43.568  1.00 50.73 ? 203 THR B CB  1 
ATOM   3219 O OG1 . THR B 1 201 ? -0.204  -12.716 43.092  1.00 53.16 ? 203 THR B OG1 1 
ATOM   3220 C CG2 . THR B 1 201 ? 1.738   -13.941 43.830  1.00 52.18 ? 203 THR B CG2 1 
ATOM   3221 N N   . ALA B 1 202 ? 3.134   -10.353 44.942  1.00 49.86 ? 204 ALA B N   1 
ATOM   3222 C CA  . ALA B 1 202 ? 4.443   -9.990  45.491  1.00 50.51 ? 204 ALA B CA  1 
ATOM   3223 C C   . ALA B 1 202 ? 4.357   -9.579  46.941  1.00 51.33 ? 204 ALA B C   1 
ATOM   3224 O O   . ALA B 1 202 ? 5.305   -9.813  47.670  1.00 51.87 ? 204 ALA B O   1 
ATOM   3225 C CB  . ALA B 1 202 ? 5.069   -8.875  44.687  1.00 50.66 ? 204 ALA B CB  1 
ATOM   3226 N N   . THR B 1 203 ? 3.237   -8.979  47.375  1.00 51.30 ? 205 THR B N   1 
ATOM   3227 C CA  . THR B 1 203 ? 3.089   -8.564  48.761  1.00 50.84 ? 205 THR B CA  1 
ATOM   3228 C C   . THR B 1 203 ? 2.580   -9.744  49.535  1.00 50.08 ? 205 THR B C   1 
ATOM   3229 O O   . THR B 1 203 ? 1.583   -10.344 49.153  1.00 48.85 ? 205 THR B O   1 
ATOM   3230 C CB  . THR B 1 203 ? 2.190   -7.291  48.933  1.00 51.88 ? 205 THR B CB  1 
ATOM   3231 O OG1 . THR B 1 203 ? 0.810   -7.602  48.976  1.00 52.09 ? 205 THR B OG1 1 
ATOM   3232 C CG2 . THR B 1 203 ? 2.449   -6.247  47.885  1.00 52.22 ? 205 THR B CG2 1 
ATOM   3233 N N   . LYS B 1 204 ? 3.264   -10.082 50.628  1.00 50.21 ? 206 LYS B N   1 
ATOM   3234 C CA  . LYS B 1 204 ? 2.765   -11.103 51.524  1.00 50.00 ? 206 LYS B CA  1 
ATOM   3235 C C   . LYS B 1 204 ? 1.915   -10.360 52.556  1.00 49.41 ? 206 LYS B C   1 
ATOM   3236 O O   . LYS B 1 204 ? 2.421   -9.543  53.321  1.00 47.65 ? 206 LYS B O   1 
ATOM   3237 C CB  . LYS B 1 204 ? 3.927   -11.925 52.103  1.00 50.72 ? 206 LYS B CB  1 
ATOM   3238 C CG  . LYS B 1 204 ? 4.456   -13.004 51.154  1.00 54.53 ? 206 LYS B CG  1 
ATOM   3239 C CD  . LYS B 1 204 ? 4.938   -12.544 49.798  1.00 58.33 ? 206 LYS B CD  1 
ATOM   3240 C CE  . LYS B 1 204 ? 4.750   -13.662 48.783  1.00 63.14 ? 206 LYS B CE  1 
ATOM   3241 N NZ  . LYS B 1 204 ? 5.471   -13.435 47.487  1.00 65.68 ? 206 LYS B NZ  1 
ATOM   3242 N N   . SER B 1 205 ? 0.604   -10.642 52.536  1.00 50.87 ? 207 SER B N   1 
ATOM   3243 C CA  . SER B 1 205 ? -0.426  -9.986  53.356  1.00 53.15 ? 207 SER B CA  1 
ATOM   3244 C C   . SER B 1 205 ? -1.190  -10.972 54.255  1.00 53.19 ? 207 SER B C   1 
ATOM   3245 O O   . SER B 1 205 ? -2.245  -10.618 54.770  1.00 52.95 ? 207 SER B O   1 
ATOM   3246 C CB  . SER B 1 205 ? -1.433  -9.275  52.444  1.00 56.31 ? 207 SER B CB  1 
ATOM   3247 O OG  . SER B 1 205 ? -0.837  -8.159  51.798  1.00 61.04 ? 207 SER B OG  1 
ATOM   3248 N N   . GLY B 1 206 ? -0.676  -12.177 54.435  1.00 53.47 ? 208 GLY B N   1 
ATOM   3249 C CA  . GLY B 1 206 ? -1.331  -13.182 55.259  1.00 55.18 ? 208 GLY B CA  1 
ATOM   3250 C C   . GLY B 1 206 ? -1.497  -14.501 54.534  1.00 56.59 ? 208 GLY B C   1 
ATOM   3251 O O   . GLY B 1 206 ? -0.579  -14.927 53.824  1.00 56.32 ? 208 GLY B O   1 
ATOM   3252 N N   . SER B 1 207 ? -2.660  -15.195 54.705  1.00 57.46 ? 209 SER B N   1 
ATOM   3253 C CA  . SER B 1 207 ? -2.749  -16.604 54.236  1.00 57.69 ? 209 SER B CA  1 
ATOM   3254 C C   . SER B 1 207 ? -2.991  -16.761 52.733  1.00 57.83 ? 209 SER B C   1 
ATOM   3255 O O   . SER B 1 207 ? -2.450  -17.718 52.149  1.00 59.29 ? 209 SER B O   1 
ATOM   3256 C CB  . SER B 1 207 ? -3.778  -17.432 55.017  1.00 58.39 ? 209 SER B CB  1 
ATOM   3257 O OG  . SER B 1 207 ? -4.829  -16.684 55.607  1.00 59.71 ? 209 SER B OG  1 
ATOM   3258 N N   . THR B 1 208 ? -3.782  -15.865 52.086  1.00 56.35 ? 210 THR B N   1 
ATOM   3259 C CA  . THR B 1 208 ? -3.921  -15.945 50.612  1.00 55.57 ? 210 THR B CA  1 
ATOM   3260 C C   . THR B 1 208 ? -3.705  -14.515 49.985  1.00 53.51 ? 210 THR B C   1 
ATOM   3261 O O   . THR B 1 208 ? -3.268  -13.583 50.677  1.00 53.25 ? 210 THR B O   1 
ATOM   3262 C CB  . THR B 1 208 ? -5.256  -16.730 50.194  1.00 57.77 ? 210 THR B CB  1 
ATOM   3263 O OG1 . THR B 1 208 ? -6.288  -16.594 51.174  1.00 58.68 ? 210 THR B OG1 1 
ATOM   3264 C CG2 . THR B 1 208 ? -5.024  -18.247 49.976  1.00 58.95 ? 210 THR B CG2 1 
ATOM   3265 N N   . THR B 1 209 ? -3.961  -14.372 48.677  1.00 51.76 ? 211 THR B N   1 
ATOM   3266 C CA  . THR B 1 209 ? -3.856  -13.122 47.917  1.00 50.68 ? 211 THR B CA  1 
ATOM   3267 C C   . THR B 1 209 ? -5.253  -12.698 47.362  1.00 48.68 ? 211 THR B C   1 
ATOM   3268 O O   . THR B 1 209 ? -6.131  -13.541 47.193  1.00 48.56 ? 211 THR B O   1 
ATOM   3269 C CB  . THR B 1 209 ? -2.798  -13.330 46.816  1.00 51.37 ? 211 THR B CB  1 
ATOM   3270 O OG1 . THR B 1 209 ? -1.562  -13.699 47.440  1.00 53.70 ? 211 THR B OG1 1 
ATOM   3271 C CG2 . THR B 1 209 ? -2.622  -12.129 45.888  1.00 50.46 ? 211 THR B CG2 1 
ATOM   3272 N N   . LYS B 1 210 ? -5.445  -11.403 47.096  1.00 46.60 ? 212 LYS B N   1 
ATOM   3273 C CA  . LYS B 1 210 ? -6.687  -10.901 46.536  1.00 45.85 ? 212 LYS B CA  1 
ATOM   3274 C C   . LYS B 1 210 ? -6.807  -11.306 45.078  1.00 44.13 ? 212 LYS B C   1 
ATOM   3275 O O   . LYS B 1 210 ? -5.807  -11.318 44.369  1.00 44.49 ? 212 LYS B O   1 
ATOM   3276 C CB  . LYS B 1 210 ? -6.719  -9.377  46.574  1.00 50.03 ? 212 LYS B CB  1 
ATOM   3277 C CG  . LYS B 1 210 ? -7.128  -8.742  47.888  1.00 56.75 ? 212 LYS B CG  1 
ATOM   3278 C CD  . LYS B 1 210 ? -7.664  -7.322  47.651  1.00 62.51 ? 212 LYS B CD  1 
ATOM   3279 C CE  . LYS B 1 210 ? -6.756  -6.424  46.803  1.00 66.19 ? 212 LYS B CE  1 
ATOM   3280 N NZ  . LYS B 1 210 ? -6.921  -6.616  45.318  1.00 67.00 ? 212 LYS B NZ  1 
ATOM   3281 N N   . ASN B 1 211 ? -8.010  -11.642 44.643  1.00 42.76 ? 213 ASN B N   1 
ATOM   3282 C CA  . ASN B 1 211 ? -8.360  -11.834 43.244  1.00 42.80 ? 213 ASN B CA  1 
ATOM   3283 C C   . ASN B 1 211 ? -8.963  -10.579 42.626  1.00 43.45 ? 213 ASN B C   1 
ATOM   3284 O O   . ASN B 1 211 ? -10.008 -10.093 43.073  1.00 44.46 ? 213 ASN B O   1 
ATOM   3285 C CB  . ASN B 1 211 ? -9.350  -12.961 43.101  1.00 44.72 ? 213 ASN B CB  1 
ATOM   3286 C CG  . ASN B 1 211 ? -8.827  -14.313 43.524  1.00 49.88 ? 213 ASN B CG  1 
ATOM   3287 O OD1 . ASN B 1 211 ? -9.539  -15.102 44.145  1.00 51.65 ? 213 ASN B OD1 1 
ATOM   3288 N ND2 . ASN B 1 211 ? -7.602  -14.666 43.210  1.00 51.11 ? 213 ASN B ND2 1 
ATOM   3289 N N   . ARG B 1 212 ? -8.323  -10.058 41.607  1.00 43.05 ? 214 ARG B N   1 
ATOM   3290 C CA  . ARG B 1 212 ? -8.881  -8.981  40.788  1.00 44.05 ? 214 ARG B CA  1 
ATOM   3291 C C   . ARG B 1 212 ? -10.150 -9.472  40.023  1.00 44.29 ? 214 ARG B C   1 
ATOM   3292 O O   . ARG B 1 212 ? -11.132 -8.730  39.956  1.00 44.37 ? 214 ARG B O   1 
ATOM   3293 C CB  . ARG B 1 212 ? -7.783  -8.437  39.831  1.00 46.04 ? 214 ARG B CB  1 
ATOM   3294 C CG  . ARG B 1 212 ? -8.064  -7.120  39.142  1.00 49.43 ? 214 ARG B CG  1 
ATOM   3295 C CD  . ARG B 1 212 ? -7.957  -5.906  40.037  1.00 52.22 ? 214 ARG B CD  1 
ATOM   3296 N NE  . ARG B 1 212 ? -6.636  -5.666  40.646  1.00 55.41 ? 214 ARG B NE  1 
ATOM   3297 C CZ  . ARG B 1 212 ? -5.561  -5.193  40.003  1.00 58.46 ? 214 ARG B CZ  1 
ATOM   3298 N NH1 . ARG B 1 212 ? -4.421  -5.003  40.653  1.00 56.70 ? 214 ARG B NH1 1 
ATOM   3299 N NH2 . ARG B 1 212 ? -5.623  -4.907  38.704  1.00 60.27 ? 214 ARG B NH2 1 
ATOM   3300 N N   . PHE B 1 213 ? -10.141 -10.708 39.465  1.00 43.99 ? 215 PHE B N   1 
ATOM   3301 C CA  . PHE B 1 213 ? -11.296 -11.328 38.762  1.00 44.46 ? 215 PHE B CA  1 
ATOM   3302 C C   . PHE B 1 213 ? -11.451 -12.803 39.177  1.00 45.79 ? 215 PHE B C   1 
ATOM   3303 O O   . PHE B 1 213 ? -10.515 -13.411 39.701  1.00 45.75 ? 215 PHE B O   1 
ATOM   3304 C CB  . PHE B 1 213 ? -11.142 -11.229 37.214  1.00 44.10 ? 215 PHE B CB  1 
ATOM   3305 C CG  . PHE B 1 213 ? -10.682 -9.885  36.730  1.00 44.55 ? 215 PHE B CG  1 
ATOM   3306 C CD1 . PHE B 1 213 ? -11.547 -8.808  36.707  1.00 45.51 ? 215 PHE B CD1 1 
ATOM   3307 C CD2 . PHE B 1 213 ? -9.367  -9.683  36.346  1.00 45.66 ? 215 PHE B CD2 1 
ATOM   3308 C CE1 . PHE B 1 213 ? -11.115 -7.562  36.287  1.00 46.69 ? 215 PHE B CE1 1 
ATOM   3309 C CE2 . PHE B 1 213 ? -8.937  -8.437  35.912  1.00 46.44 ? 215 PHE B CE2 1 
ATOM   3310 C CZ  . PHE B 1 213 ? -9.813  -7.385  35.891  1.00 46.87 ? 215 PHE B CZ  1 
ATOM   3311 N N   . VAL B 1 214 ? -12.648 -13.365 38.940  1.00 46.20 ? 216 VAL B N   1 
ATOM   3312 C CA  . VAL B 1 214 ? -13.017 -14.751 39.251  1.00 46.50 ? 216 VAL B CA  1 
ATOM   3313 C C   . VAL B 1 214 ? -13.870 -15.282 38.042  1.00 46.50 ? 216 VAL B C   1 
ATOM   3314 O O   . VAL B 1 214 ? -14.669 -14.535 37.491  1.00 46.15 ? 216 VAL B O   1 
ATOM   3315 C CB  . VAL B 1 214 ? -13.817 -14.803 40.605  1.00 48.32 ? 216 VAL B CB  1 
ATOM   3316 C CG1 . VAL B 1 214 ? -14.360 -16.205 40.901  1.00 49.85 ? 216 VAL B CG1 1 
ATOM   3317 C CG2 . VAL B 1 214 ? -12.964 -14.315 41.788  1.00 48.35 ? 216 VAL B CG2 1 
ATOM   3318 N N   . VAL B 1 215 ? -13.682 -16.546 37.625  1.00 46.87 ? 217 VAL B N   1 
ATOM   3319 C CA  . VAL B 1 215 ? -14.562 -17.207 36.655  1.00 47.96 ? 217 VAL B CA  1 
ATOM   3320 C C   . VAL B 1 215 ? -14.853 -18.637 37.092  1.00 48.06 ? 217 VAL B C   1 
ATOM   3321 O O   . VAL B 1 215 ? -15.803 -19.225 36.535  1.00 48.36 ? 217 VAL B O   1 
ATOM   3322 C CB  . VAL B 1 215 ? -14.039 -17.208 35.193  1.00 49.61 ? 217 VAL B CB  1 
ATOM   3323 C CG1 . VAL B 1 215 ? -13.717 -15.805 34.706  1.00 51.46 ? 217 VAL B CG1 1 
ATOM   3324 C CG2 . VAL B 1 215 ? -12.828 -18.082 35.039  1.00 50.11 ? 217 VAL B CG2 1 
ATOM   3325 O OXT . VAL B 1 215 ? -14.144 -19.184 37.966  1.00 46.67 ? 217 VAL B OXT 1 
HETATM 3326 C C1  . EDO C 2 .   ? 14.171  -26.147 2.644   1.00 52.18 ? 301 EDO A C1  1 
HETATM 3327 O O1  . EDO C 2 .   ? 13.344  -25.752 3.747   1.00 52.50 ? 301 EDO A O1  1 
HETATM 3328 C C2  . EDO C 2 .   ? 15.577  -25.517 2.810   1.00 51.94 ? 301 EDO A C2  1 
HETATM 3329 O O2  . EDO C 2 .   ? 16.177  -25.341 1.547   1.00 51.80 ? 301 EDO A O2  1 
HETATM 3330 C C1  . PEG D 3 .   ? 4.929   -1.797  -10.435 1.00 77.02 ? 302 PEG A C1  1 
HETATM 3331 O O1  . PEG D 3 .   ? 6.160   -2.499  -10.550 1.00 76.98 ? 302 PEG A O1  1 
HETATM 3332 C C2  . PEG D 3 .   ? 3.827   -2.662  -9.894  1.00 76.97 ? 302 PEG A C2  1 
HETATM 3333 O O2  . PEG D 3 .   ? 4.140   -3.091  -8.575  1.00 76.89 ? 302 PEG A O2  1 
HETATM 3334 C C3  . PEG D 3 .   ? 3.189   -2.682  -7.606  1.00 76.52 ? 302 PEG A C3  1 
HETATM 3335 C C4  . PEG D 3 .   ? 3.790   -1.643  -6.729  1.00 76.34 ? 302 PEG A C4  1 
HETATM 3336 O O4  . PEG D 3 .   ? 2.819   -1.068  -5.883  1.00 76.35 ? 302 PEG A O4  1 
HETATM 3337 S S   . DMS E 4 .   ? 28.485  -21.734 11.620  1.00 67.92 ? 303 DMS A S   1 
HETATM 3338 O O   . DMS E 4 .   ? 27.137  -21.804 12.286  1.00 68.21 ? 303 DMS A O   1 
HETATM 3339 C C1  . DMS E 4 .   ? 29.233  -23.334 11.836  1.00 67.45 ? 303 DMS A C1  1 
HETATM 3340 C C2  . DMS E 4 .   ? 28.183  -21.837 9.875   1.00 67.91 ? 303 DMS A C2  1 
HETATM 3341 C C1  . W4K F 5 .   ? 20.672  -2.648  12.665  1.00 32.20 ? 304 W4K A C1  1 
HETATM 3342 C C2  . W4K F 5 .   ? 20.218  -2.789  11.268  1.00 30.31 ? 304 W4K A C2  1 
HETATM 3343 C C3  . W4K F 5 .   ? 20.705  -4.076  10.592  1.00 27.87 ? 304 W4K A C3  1 
HETATM 3344 C C5  . W4K F 5 .   ? 22.465  -4.673  8.927   1.00 25.29 ? 304 W4K A C5  1 
HETATM 3345 C C6  . W4K F 5 .   ? 23.504  -5.309  9.844   1.00 26.48 ? 304 W4K A C6  1 
HETATM 3346 C C7  . W4K F 5 .   ? 23.102  -4.036  7.702   1.00 23.92 ? 304 W4K A C7  1 
HETATM 3347 C C10 . W4K F 5 .   ? 19.159  -6.062  10.405  1.00 25.89 ? 304 W4K A C10 1 
HETATM 3348 C C11 . W4K F 5 .   ? 18.085  -6.730  9.852   1.00 25.68 ? 304 W4K A C11 1 
HETATM 3349 C C12 . W4K F 5 .   ? 17.340  -6.155  8.835   1.00 26.10 ? 304 W4K A C12 1 
HETATM 3350 C C13 . W4K F 5 .   ? 17.699  -4.887  8.388   1.00 26.85 ? 304 W4K A C13 1 
HETATM 3351 C C14 . W4K F 5 .   ? 18.773  -4.206  8.938   1.00 25.79 ? 304 W4K A C14 1 
HETATM 3352 C C16 . W4K F 5 .   ? 18.732  -2.489  7.123   1.00 28.36 ? 304 W4K A C16 1 
HETATM 3353 C C19 . W4K F 5 .   ? 16.186  -6.857  8.208   1.00 26.88 ? 304 W4K A C19 1 
HETATM 3354 C C21 . W4K F 5 .   ? 13.916  -6.762  7.396   1.00 27.60 ? 304 W4K A C21 1 
HETATM 3355 C C22 . W4K F 5 .   ? 14.003  -8.072  6.980   1.00 27.45 ? 304 W4K A C22 1 
HETATM 3356 C C23 . W4K F 5 .   ? 15.173  -8.775  7.172   1.00 27.61 ? 304 W4K A C23 1 
HETATM 3357 C C24 . W4K F 5 .   ? 16.247  -8.164  7.766   1.00 27.02 ? 304 W4K A C24 1 
HETATM 3358 O O4  . W4K F 5 .   ? 21.724  -3.667  9.610   1.00 25.42 ? 304 W4K A O4  1 
HETATM 3359 O O8  . W4K F 5 .   ? 22.104  -3.547  6.822   1.00 25.08 ? 304 W4K A O8  1 
HETATM 3360 C C9  . W4K F 5 .   ? 19.532  -4.801  9.949   1.00 26.16 ? 304 W4K A C9  1 
HETATM 3361 N N15 . W4K F 5 .   ? 19.115  -2.957  8.462   1.00 27.05 ? 304 W4K A N15 1 
HETATM 3362 C C17 . W4K F 5 .   ? 18.888  -0.985  6.993   1.00 30.10 ? 304 W4K A C17 1 
HETATM 3363 O O18 . W4K F 5 .   ? 20.117  -0.554  7.565   1.00 32.08 ? 304 W4K A O18 1 
HETATM 3364 C C20 . W4K F 5 .   ? 15.005  -6.151  7.995   1.00 27.35 ? 304 W4K A C20 1 
HETATM 3365 F F25 . W4K F 5 .   ? 17.387  -8.865  7.974   1.00 26.95 ? 304 W4K A F25 1 
HETATM 3366 H H30 . W4K F 5 .   ? 20.100  -3.187  13.252  1.00 32.20 ? 304 W4K A H30 1 
HETATM 3367 H H29 . W4K F 5 .   ? 20.619  -1.707  12.933  1.00 32.19 ? 304 W4K A H29 1 
HETATM 3368 H H28 . W4K F 5 .   ? 21.599  -2.956  12.740  1.00 32.20 ? 304 W4K A H28 1 
HETATM 3369 H H32 . W4K F 5 .   ? 20.540  -2.017  10.751  1.00 30.31 ? 304 W4K A H32 1 
HETATM 3370 H H31 . W4K F 5 .   ? 19.234  -2.772  11.251  1.00 30.31 ? 304 W4K A H31 1 
HETATM 3371 H H26 . W4K F 5 .   ? 21.120  -4.663  11.270  1.00 27.88 ? 304 W4K A H26 1 
HETATM 3372 H H27 . W4K F 5 .   ? 21.842  -5.376  8.622   1.00 25.35 ? 304 W4K A H27 1 
HETATM 3373 H H35 . W4K F 5 .   ? 24.391  -5.229  9.437   1.00 26.45 ? 304 W4K A H35 1 
HETATM 3374 H H34 . W4K F 5 .   ? 23.289  -6.258  9.974   1.00 26.47 ? 304 W4K A H34 1 
HETATM 3375 H H33 . W4K F 5 .   ? 23.499  -4.853  10.709  1.00 26.50 ? 304 W4K A H33 1 
HETATM 3376 H H37 . W4K F 5 .   ? 23.649  -4.701  7.236   1.00 23.93 ? 304 W4K A H37 1 
HETATM 3377 H H36 . W4K F 5 .   ? 23.686  -3.299  7.980   1.00 23.92 ? 304 W4K A H36 1 
HETATM 3378 H H39 . W4K F 5 .   ? 19.657  -6.473  11.108  1.00 25.89 ? 304 W4K A H39 1 
HETATM 3379 H H40 . W4K F 5 .   ? 17.856  -7.601  10.170  1.00 25.72 ? 304 W4K A H40 1 
HETATM 3380 H H41 . W4K F 5 .   ? 17.201  -4.484  7.680   1.00 26.83 ? 304 W4K A H41 1 
HETATM 3381 H H44 . W4K F 5 .   ? 17.800  -2.733  6.946   1.00 28.38 ? 304 W4K A H44 1 
HETATM 3382 H H43 . W4K F 5 .   ? 19.295  -2.933  6.451   1.00 28.34 ? 304 W4K A H43 1 
HETATM 3383 H H49 . W4K F 5 .   ? 13.109  -6.270  7.256   1.00 27.60 ? 304 W4K A H49 1 
HETATM 3384 H H50 . W4K F 5 .   ? 13.255  -8.491  6.559   1.00 27.46 ? 304 W4K A H50 1 
HETATM 3385 H H51 . W4K F 5 .   ? 15.238  -9.685  6.891   1.00 27.63 ? 304 W4K A H51 1 
HETATM 3386 H H38 . W4K F 5 .   ? 21.506  -3.143  7.283   1.00 25.08 ? 304 W4K A H38 1 
HETATM 3387 H H42 . W4K F 5 .   ? 19.042  -2.333  9.060   1.00 27.07 ? 304 W4K A H42 1 
HETATM 3388 H H46 . W4K F 5 .   ? 18.141  -0.537  7.446   1.00 30.08 ? 304 W4K A H46 1 
HETATM 3389 H H45 . W4K F 5 .   ? 18.864  -0.735  6.042   1.00 30.09 ? 304 W4K A H45 1 
HETATM 3390 H H47 . W4K F 5 .   ? 20.769  -0.840  7.070   1.00 32.06 ? 304 W4K A H47 1 
HETATM 3391 H H48 . W4K F 5 .   ? 14.941  -5.241  8.276   1.00 27.34 ? 304 W4K A H48 1 
HETATM 3392 C C1  . EDO G 2 .   ? -10.075 -31.976 21.150  1.00 48.97 ? 301 EDO B C1  1 
HETATM 3393 O O1  . EDO G 2 .   ? -10.645 -32.559 22.334  1.00 50.05 ? 301 EDO B O1  1 
HETATM 3394 C C2  . EDO G 2 .   ? -10.913 -30.738 20.632  1.00 47.54 ? 301 EDO B C2  1 
HETATM 3395 O O2  . EDO G 2 .   ? -10.231 -30.014 19.566  1.00 46.48 ? 301 EDO B O2  1 
HETATM 3396 C C1  . EDO H 2 .   ? 1.973   -16.230 49.815  1.00 59.37 ? 302 EDO B C1  1 
HETATM 3397 O O1  . EDO H 2 .   ? 3.360   -16.099 50.170  1.00 59.84 ? 302 EDO B O1  1 
HETATM 3398 C C2  . EDO H 2 .   ? 1.300   -14.828 49.669  1.00 58.94 ? 302 EDO B C2  1 
HETATM 3399 O O2  . EDO H 2 .   ? 1.193   -14.436 48.296  1.00 58.70 ? 302 EDO B O2  1 
HETATM 3400 C C1  . PEG I 3 .   ? 2.532   -9.765  26.015  1.00 54.74 ? 303 PEG B C1  1 
HETATM 3401 O O1  . PEG I 3 .   ? 2.074   -8.650  25.235  1.00 55.52 ? 303 PEG B O1  1 
HETATM 3402 C C2  . PEG I 3 .   ? 3.457   -10.615 25.218  1.00 53.92 ? 303 PEG B C2  1 
HETATM 3403 O O2  . PEG I 3 .   ? 4.540   -9.827  24.737  1.00 53.00 ? 303 PEG B O2  1 
HETATM 3404 C C3  . PEG I 3 .   ? 5.419   -10.526 23.859  1.00 51.97 ? 303 PEG B C3  1 
HETATM 3405 C C4  . PEG I 3 .   ? 6.667   -9.730  23.624  1.00 51.12 ? 303 PEG B C4  1 
HETATM 3406 O O4  . PEG I 3 .   ? 7.745   -10.541 23.186  1.00 50.39 ? 303 PEG B O4  1 
HETATM 3407 S S   . DMS J 4 .   ? 4.953   -12.962 42.241  1.00 84.94 ? 304 DMS B S   1 
HETATM 3408 O O   . DMS J 4 .   ? 4.466   -11.721 41.545  1.00 85.02 ? 304 DMS B O   1 
HETATM 3409 C C1  . DMS J 4 .   ? 5.572   -14.027 40.963  1.00 84.63 ? 304 DMS B C1  1 
HETATM 3410 C C2  . DMS J 4 .   ? 6.510   -12.532 42.983  1.00 84.99 ? 304 DMS B C2  1 
HETATM 3411 C C1  . PEG K 3 .   ? 10.893  -12.320 44.332  1.00 42.99 ? 305 PEG B C1  1 
HETATM 3412 O O1  . PEG K 3 .   ? 9.928   -11.467 43.680  1.00 43.03 ? 305 PEG B O1  1 
HETATM 3413 C C2  . PEG K 3 .   ? 11.672  -11.583 45.401  1.00 43.35 ? 305 PEG B C2  1 
HETATM 3414 O O2  . PEG K 3 .   ? 10.788  -11.186 46.448  1.00 43.61 ? 305 PEG B O2  1 
HETATM 3415 C C3  . PEG K 3 .   ? 11.416  -10.929 47.699  1.00 44.46 ? 305 PEG B C3  1 
HETATM 3416 C C4  . PEG K 3 .   ? 11.928  -12.198 48.334  1.00 44.95 ? 305 PEG B C4  1 
HETATM 3417 O O4  . PEG K 3 .   ? 12.833  -11.893 49.390  1.00 45.48 ? 305 PEG B O4  1 
HETATM 3418 C C1  . PEG L 3 .   ? 6.092   -19.859 44.904  1.00 57.75 ? 306 PEG B C1  1 
HETATM 3419 O O1  . PEG L 3 .   ? 4.803   -19.279 44.757  1.00 56.35 ? 306 PEG B O1  1 
HETATM 3420 C C2  . PEG L 3 .   ? 7.098   -19.330 43.919  1.00 58.68 ? 306 PEG B C2  1 
HETATM 3421 O O2  . PEG L 3 .   ? 7.282   -17.930 44.125  1.00 60.24 ? 306 PEG B O2  1 
HETATM 3422 C C3  . PEG L 3 .   ? 8.653   -17.550 44.278  1.00 60.62 ? 306 PEG B C3  1 
HETATM 3423 C C4  . PEG L 3 .   ? 8.887   -16.173 43.759  1.00 60.86 ? 306 PEG B C4  1 
HETATM 3424 O O4  . PEG L 3 .   ? 10.260  -15.795 43.897  1.00 61.00 ? 306 PEG B O4  1 
HETATM 3425 C C1  . W4K M 5 .   ? 8.762   -33.157 35.657  1.00 36.01 ? 307 W4K B C1  1 
HETATM 3426 C C2  . W4K M 5 .   ? 8.337   -32.727 34.285  1.00 34.44 ? 307 W4K B C2  1 
HETATM 3427 C C3  . W4K M 5 .   ? 7.404   -31.519 34.283  1.00 32.23 ? 307 W4K B C3  1 
HETATM 3428 C C5  . W4K M 5 .   ? 5.164   -30.992 35.020  1.00 29.98 ? 307 W4K B C5  1 
HETATM 3429 C C6  . W4K M 5 .   ? 5.592   -30.262 36.289  1.00 30.28 ? 307 W4K B C6  1 
HETATM 3430 C C7  . W4K M 5 .   ? 3.812   -31.698 35.140  1.00 29.12 ? 307 W4K B C7  1 
HETATM 3431 C C10 . W4K M 5 .   ? 7.932   -29.629 32.730  1.00 29.29 ? 307 W4K B C10 1 
HETATM 3432 C C11 . W4K M 5 .   ? 7.909   -29.001 31.507  1.00 28.62 ? 307 W4K B C11 1 
HETATM 3433 C C12 . W4K M 5 .   ? 7.315   -29.602 30.404  1.00 27.44 ? 307 W4K B C12 1 
HETATM 3434 C C13 . W4K M 5 .   ? 6.731   -30.852 30.561  1.00 28.13 ? 307 W4K B C13 1 
HETATM 3435 C C14 . W4K M 5 .   ? 6.729   -31.506 31.783  1.00 29.02 ? 307 W4K B C14 1 
HETATM 3436 C C16 . W4K M 5 .   ? 5.563   -33.394 30.739  1.00 30.02 ? 307 W4K B C16 1 
HETATM 3437 C C19 . W4K M 5 .   ? 7.306   -28.933 29.074  1.00 26.58 ? 307 W4K B C19 1 
HETATM 3438 C C21 . W4K M 5 .   ? 7.750   -29.104 26.713  1.00 26.06 ? 307 W4K B C21 1 
HETATM 3439 C C22 . W4K M 5 .   ? 7.341   -27.796 26.537  1.00 24.76 ? 307 W4K B C22 1 
HETATM 3440 C C23 . W4K M 5 .   ? 6.926   -27.055 27.619  1.00 24.02 ? 307 W4K B C23 1 
HETATM 3441 C C24 . W4K M 5 .   ? 6.904   -27.622 28.863  1.00 23.97 ? 307 W4K B C24 1 
HETATM 3442 O O4  . W4K M 5 .   ? 6.120   -32.005 34.719  1.00 31.81 ? 307 W4K B O4  1 
HETATM 3443 O O8  . W4K M 5 .   ? 3.424   -32.249 33.886  1.00 29.16 ? 307 W4K B O8  1 
HETATM 3444 C C9  . W4K M 5 .   ? 7.343   -30.879 32.904  1.00 30.60 ? 307 W4K B C9  1 
HETATM 3445 N N15 . W4K M 5 .   ? 6.137   -32.721 31.890  1.00 28.97 ? 307 W4K B N15 1 
HETATM 3446 C C17 . W4K M 5 .   ? 5.052   -34.781 31.087  1.00 31.70 ? 307 W4K B C17 1 
HETATM 3447 O O18 . W4K M 5 .   ? 4.201   -34.733 32.224  1.00 32.45 ? 307 W4K B O18 1 
HETATM 3448 C C20 . W4K M 5 .   ? 7.731   -29.673 27.969  1.00 25.77 ? 307 W4K B C20 1 
HETATM 3449 F F25 . W4K M 5 .   ? 6.483   -26.888 29.918  1.00 22.24 ? 307 W4K B F25 1 
HETATM 3450 H H30 . W4K M 5 .   ? 8.732   -32.392 36.264  1.00 36.02 ? 307 W4K B H30 1 
HETATM 3451 H H29 . W4K M 5 .   ? 9.676   -33.509 35.621  1.00 36.02 ? 307 W4K B H29 1 
HETATM 3452 H H28 . W4K M 5 .   ? 8.157   -33.855 35.983  1.00 36.02 ? 307 W4K B H28 1 
HETATM 3453 H H32 . W4K M 5 .   ? 7.882   -33.479 33.844  1.00 34.44 ? 307 W4K B H32 1 
HETATM 3454 H H31 . W4K M 5 .   ? 9.139   -32.508 33.758  1.00 34.46 ? 307 W4K B H31 1 
HETATM 3455 H H26 . W4K M 5 .   ? 7.737   -30.856 34.931  1.00 32.22 ? 307 W4K B H26 1 
HETATM 3456 H H27 . W4K M 5 .   ? 5.123   -30.350 34.274  1.00 29.95 ? 307 W4K B H27 1 
HETATM 3457 H H35 . W4K M 5 .   ? 6.206   -30.827 36.801  1.00 30.27 ? 307 W4K B H35 1 
HETATM 3458 H H34 . W4K M 5 .   ? 4.801   -30.063 36.833  1.00 30.29 ? 307 W4K B H34 1 
HETATM 3459 H H33 . W4K M 5 .   ? 6.041   -29.426 36.049  1.00 30.26 ? 307 W4K B H33 1 
HETATM 3460 H H37 . W4K M 5 .   ? 3.131   -31.054 35.439  1.00 29.12 ? 307 W4K B H37 1 
HETATM 3461 H H36 . W4K M 5 .   ? 3.873   -32.416 35.809  1.00 29.10 ? 307 W4K B H36 1 
HETATM 3462 H H39 . W4K M 5 .   ? 8.348   -29.198 33.473  1.00 29.28 ? 307 W4K B H39 1 
HETATM 3463 H H40 . W4K M 5 .   ? 8.319   -28.144 31.411  1.00 28.65 ? 307 W4K B H40 1 
HETATM 3464 H H41 . W4K M 5 .   ? 6.318   -31.266 29.807  1.00 28.10 ? 307 W4K B H41 1 
HETATM 3465 H H44 . W4K M 5 .   ? 6.243   -33.468 30.036  1.00 30.02 ? 307 W4K B H44 1 
HETATM 3466 H H43 . W4K M 5 .   ? 4.819   -32.855 30.386  1.00 30.00 ? 307 W4K B H43 1 
HETATM 3467 H H49 . W4K M 5 .   ? 8.045   -29.617 25.962  1.00 26.08 ? 307 W4K B H49 1 
HETATM 3468 H H50 . W4K M 5 .   ? 7.355   -27.405 25.667  1.00 24.79 ? 307 W4K B H50 1 
HETATM 3469 H H51 . W4K M 5 .   ? 6.637   -26.153 27.500  1.00 24.02 ? 307 W4K B H51 1 
HETATM 3470 H H38 . W4K M 5 .   ? 4.112   -32.559 33.498  1.00 29.15 ? 307 W4K B H38 1 
HETATM 3471 H H42 . W4K M 5 .   ? 5.842   -32.953 32.677  1.00 28.93 ? 307 W4K B H42 1 
HETATM 3472 H H46 . W4K M 5 .   ? 5.817   -35.376 31.272  1.00 31.71 ? 307 W4K B H46 1 
HETATM 3473 H H45 . W4K M 5 .   ? 4.555   -35.151 30.319  1.00 31.66 ? 307 W4K B H45 1 
HETATM 3474 H H47 . W4K M 5 .   ? 4.650   -34.986 32.921  1.00 32.46 ? 307 W4K B H47 1 
HETATM 3475 H H48 . W4K M 5 .   ? 8.014   -30.576 28.085  1.00 25.74 ? 307 W4K B H48 1 
HETATM 3476 O O   . HOH N 6 .   ? 25.659  -22.082 14.013  1.00 33.97 ? 401 HOH A O   1 
HETATM 3477 O O   . HOH N 6 .   ? 29.375  -33.884 2.593   1.00 28.46 ? 402 HOH A O   1 
HETATM 3478 O O   . HOH N 6 .   ? 29.362  -9.398  -10.600 1.00 42.78 ? 403 HOH A O   1 
HETATM 3479 O O   . HOH N 6 .   ? 33.585  1.727   7.435   1.00 41.15 ? 404 HOH A O   1 
HETATM 3480 O O   . HOH N 6 .   ? 3.222   -10.853 6.308   1.00 31.58 ? 405 HOH A O   1 
HETATM 3481 O O   . HOH N 6 .   ? 18.198  -17.743 -11.565 1.00 36.10 ? 406 HOH A O   1 
HETATM 3482 O O   . HOH N 6 .   ? 10.267  -16.102 -0.879  1.00 20.39 ? 407 HOH A O   1 
HETATM 3483 O O   . HOH N 6 .   ? 26.726  0.693   4.983   1.00 34.03 ? 408 HOH A O   1 
HETATM 3484 O O   . HOH N 6 .   ? 33.127  -17.074 11.787  1.00 46.72 ? 409 HOH A O   1 
HETATM 3485 O O   . HOH N 6 .   ? 20.430  -32.562 1.867   1.00 39.39 ? 410 HOH A O   1 
HETATM 3486 O O   . HOH N 6 .   ? 36.444  -11.405 8.540   1.00 33.48 ? 411 HOH A O   1 
HETATM 3487 O O   . HOH N 6 .   ? 20.086  -29.013 -11.910 1.00 43.38 ? 412 HOH A O   1 
HETATM 3488 O O   . HOH N 6 .   ? 13.536  -19.258 10.508  1.00 21.81 ? 413 HOH A O   1 
HETATM 3489 O O   . HOH N 6 .   ? 20.374  -2.808  4.373   1.00 35.23 ? 414 HOH A O   1 
HETATM 3490 O O   . HOH N 6 .   ? 34.067  -26.279 2.582   1.00 23.90 ? 415 HOH A O   1 
HETATM 3491 O O   . HOH N 6 .   ? 7.212   -9.154  10.010  1.00 41.04 ? 416 HOH A O   1 
HETATM 3492 O O   . HOH N 6 .   ? 29.650  -21.845 -11.941 1.00 46.58 ? 417 HOH A O   1 
HETATM 3493 O O   . HOH N 6 .   ? 22.755  -26.629 -1.323  1.00 18.91 ? 418 HOH A O   1 
HETATM 3494 O O   . HOH N 6 .   ? 3.238   -0.677  -3.319  1.00 41.69 ? 419 HOH A O   1 
HETATM 3495 O O   . HOH N 6 .   ? 27.824  -0.480  -2.107  1.00 45.66 ? 420 HOH A O   1 
HETATM 3496 O O   . HOH N 6 .   ? 28.252  -13.024 18.329  1.00 41.81 ? 421 HOH A O   1 
HETATM 3497 O O   . HOH N 6 .   ? 20.706  2.018   7.485   1.00 32.98 ? 422 HOH A O   1 
HETATM 3498 O O   . HOH N 6 .   ? 27.187  0.947   7.681   1.00 43.25 ? 423 HOH A O   1 
HETATM 3499 O O   . HOH N 6 .   ? 22.803  -23.854 5.695   1.00 23.13 ? 424 HOH A O   1 
HETATM 3500 O O   . HOH N 6 .   ? 36.951  -24.394 -4.071  1.00 58.77 ? 425 HOH A O   1 
HETATM 3501 O O   . HOH N 6 .   ? 28.662  -14.144 -11.129 1.00 32.22 ? 426 HOH A O   1 
HETATM 3502 O O   . HOH N 6 .   ? 33.722  0.046   -0.496  1.00 44.25 ? 427 HOH A O   1 
HETATM 3503 O O   . HOH N 6 .   ? -7.031  -5.811  -3.168  1.00 36.84 ? 428 HOH A O   1 
HETATM 3504 O O   . HOH N 6 .   ? 13.690  3.322   6.444   1.00 51.11 ? 429 HOH A O   1 
HETATM 3505 O O   . HOH N 6 .   ? 30.472  -15.722 21.860  1.00 51.33 ? 430 HOH A O   1 
HETATM 3506 O O   . HOH N 6 .   ? 11.485  -27.455 4.647   1.00 59.61 ? 431 HOH A O   1 
HETATM 3507 O O   . HOH N 6 .   ? 16.188  -17.095 -3.059  1.00 22.99 ? 432 HOH A O   1 
HETATM 3508 O O   . HOH N 6 .   ? 19.303  -8.012  -5.174  1.00 15.34 ? 433 HOH A O   1 
HETATM 3509 O O   . HOH N 6 .   ? 5.472   -21.409 6.918   1.00 37.24 ? 434 HOH A O   1 
HETATM 3510 O O   . HOH N 6 .   ? 38.494  -26.399 8.904   1.00 50.90 ? 435 HOH A O   1 
HETATM 3511 O O   . HOH N 6 .   ? 13.394  -16.461 -13.261 1.00 53.16 ? 436 HOH A O   1 
HETATM 3512 O O   . HOH N 6 .   ? 36.079  -21.770 10.511  1.00 49.95 ? 437 HOH A O   1 
HETATM 3513 O O   . HOH N 6 .   ? 14.751  -12.269 -8.594  1.00 35.25 ? 438 HOH A O   1 
HETATM 3514 O O   . HOH N 6 .   ? 12.352  -21.593 -1.981  1.00 29.33 ? 439 HOH A O   1 
HETATM 3515 O O   . HOH N 6 .   ? 30.082  -22.413 6.273   1.00 30.25 ? 440 HOH A O   1 
HETATM 3516 O O   . HOH N 6 .   ? 14.450  -16.952 -10.262 1.00 28.02 ? 441 HOH A O   1 
HETATM 3517 O O   . HOH N 6 .   ? 11.888  -0.333  -9.176  1.00 40.99 ? 442 HOH A O   1 
HETATM 3518 O O   . HOH N 6 .   ? 35.611  -14.000 6.905   1.00 39.45 ? 443 HOH A O   1 
HETATM 3519 O O   . HOH N 6 .   ? 37.439  -19.361 3.062   1.00 58.15 ? 444 HOH A O   1 
HETATM 3520 O O   . HOH N 6 .   ? 25.895  0.406   1.859   1.00 18.87 ? 445 HOH A O   1 
HETATM 3521 O O   . HOH N 6 .   ? 27.187  -16.847 8.261   1.00 21.05 ? 446 HOH A O   1 
HETATM 3522 O O   . HOH N 6 .   ? 5.071   -1.678  3.180   1.00 38.41 ? 447 HOH A O   1 
HETATM 3523 O O   . HOH N 6 .   ? 14.430  -27.205 9.811   1.00 39.94 ? 448 HOH A O   1 
HETATM 3524 O O   . HOH N 6 .   ? 8.522   -14.786 -3.663  1.00 23.87 ? 449 HOH A O   1 
HETATM 3525 O O   . HOH N 6 .   ? 27.666  -14.283 7.474   1.00 18.29 ? 450 HOH A O   1 
HETATM 3526 O O   . HOH N 6 .   ? 23.302  -17.424 12.331  1.00 30.62 ? 451 HOH A O   1 
HETATM 3527 O O   . HOH N 6 .   ? -11.416 -11.467 1.308   1.00 38.00 ? 452 HOH A O   1 
HETATM 3528 O O   . HOH N 6 .   ? -2.872  -10.056 0.440   1.00 37.82 ? 453 HOH A O   1 
HETATM 3529 O O   . HOH N 6 .   ? 21.014  -14.427 13.950  1.00 36.42 ? 454 HOH A O   1 
HETATM 3530 O O   . HOH N 6 .   ? 14.800  -10.358 -6.178  1.00 26.03 ? 455 HOH A O   1 
HETATM 3531 O O   . HOH N 6 .   ? 21.223  -29.710 5.956   1.00 26.96 ? 456 HOH A O   1 
HETATM 3532 O O   . HOH N 6 .   ? 22.250  -0.834  9.486   1.00 31.08 ? 457 HOH A O   1 
HETATM 3533 O O   . HOH N 6 .   ? 27.957  -29.187 6.328   1.00 29.19 ? 458 HOH A O   1 
HETATM 3534 O O   . HOH N 6 .   ? 8.479   -3.615  -11.738 1.00 42.52 ? 459 HOH A O   1 
HETATM 3535 O O   . HOH N 6 .   ? 27.036  -15.904 25.444  1.00 68.30 ? 460 HOH A O   1 
HETATM 3536 O O   . HOH N 6 .   ? 18.941  1.126   -6.705  1.00 44.67 ? 461 HOH A O   1 
HETATM 3537 O O   . HOH N 6 .   ? 24.279  2.301   14.812  1.00 60.53 ? 462 HOH A O   1 
HETATM 3538 O O   . HOH N 6 .   ? 33.222  -4.142  7.775   1.00 45.90 ? 463 HOH A O   1 
HETATM 3539 O O   . HOH N 6 .   ? 32.084  -22.559 -11.598 1.00 37.63 ? 464 HOH A O   1 
HETATM 3540 O O   . HOH N 6 .   ? 32.251  -30.183 11.990  1.00 41.70 ? 465 HOH A O   1 
HETATM 3541 O O   . HOH N 6 .   ? 8.148   -22.220 12.241  1.00 44.22 ? 466 HOH A O   1 
HETATM 3542 O O   . HOH N 6 .   ? 29.135  -15.836 15.001  1.00 48.19 ? 467 HOH A O   1 
HETATM 3543 O O   . HOH N 6 .   ? 30.546  5.035   13.977  1.00 42.55 ? 468 HOH A O   1 
HETATM 3544 O O   . HOH N 6 .   ? 25.976  -32.937 -11.772 1.00 49.44 ? 469 HOH A O   1 
HETATM 3545 O O   . HOH N 6 .   ? 9.443   -22.482 5.102   1.00 44.77 ? 470 HOH A O   1 
HETATM 3546 O O   . HOH N 6 .   ? 35.327  -13.992 2.289   1.00 42.75 ? 471 HOH A O   1 
HETATM 3547 O O   . HOH N 6 .   ? 38.360  -22.048 10.586  1.00 54.60 ? 472 HOH A O   1 
HETATM 3548 O O   . HOH N 6 .   ? 33.458  -7.774  16.602  1.00 40.59 ? 473 HOH A O   1 
HETATM 3549 O O   . HOH N 6 .   ? 33.637  -1.438  -2.577  1.00 46.76 ? 474 HOH A O   1 
HETATM 3550 O O   . HOH N 6 .   ? 16.507  -29.474 13.261  1.00 43.29 ? 475 HOH A O   1 
HETATM 3551 O O   . HOH N 6 .   ? 27.363  3.548   7.973   1.00 38.48 ? 476 HOH A O   1 
HETATM 3552 O O   . HOH N 6 .   ? 12.053  -24.198 0.207   1.00 33.05 ? 477 HOH A O   1 
HETATM 3553 O O   . HOH N 6 .   ? 11.218  -20.033 11.943  1.00 34.18 ? 478 HOH A O   1 
HETATM 3554 O O   . HOH N 6 .   ? 9.299   -23.457 -1.993  1.00 51.09 ? 479 HOH A O   1 
HETATM 3555 O O   . HOH N 6 .   ? 14.870  -6.060  -11.935 1.00 33.55 ? 480 HOH A O   1 
HETATM 3556 O O   . HOH N 6 .   ? 40.820  -21.331 1.769   1.00 47.31 ? 481 HOH A O   1 
HETATM 3557 O O   . HOH N 6 .   ? 35.936  -15.616 12.308  1.00 56.70 ? 482 HOH A O   1 
HETATM 3558 O O   . HOH N 6 .   ? 18.668  -7.491  -11.095 1.00 32.75 ? 483 HOH A O   1 
HETATM 3559 O O   . HOH N 6 .   ? 28.881  -6.494  21.749  1.00 49.89 ? 484 HOH A O   1 
HETATM 3560 O O   . HOH N 6 .   ? 25.282  -24.434 -12.040 1.00 37.09 ? 485 HOH A O   1 
HETATM 3561 O O   . HOH N 6 .   ? 35.518  -29.280 -4.588  1.00 52.05 ? 486 HOH A O   1 
HETATM 3562 O O   . HOH N 6 .   ? 30.403  2.684   10.925  1.00 40.09 ? 487 HOH A O   1 
HETATM 3563 O O   . HOH N 6 .   ? 17.356  -13.978 -11.136 1.00 39.65 ? 488 HOH A O   1 
HETATM 3564 O O   . HOH N 6 .   ? 16.285  -15.594 26.122  1.00 45.69 ? 489 HOH A O   1 
HETATM 3565 O O   . HOH N 6 .   ? -8.813  4.955   -3.304  1.00 67.58 ? 490 HOH A O   1 
HETATM 3566 O O   . HOH N 6 .   ? 24.947  -31.103 -8.533  1.00 29.76 ? 491 HOH A O   1 
HETATM 3567 O O   . HOH N 6 .   ? 23.741  -4.823  15.057  1.00 47.51 ? 492 HOH A O   1 
HETATM 3568 O O   . HOH N 6 .   ? 19.385  1.251   20.783  1.00 45.97 ? 493 HOH A O   1 
HETATM 3569 O O   . HOH N 6 .   ? 34.120  -3.809  10.140  1.00 41.92 ? 494 HOH A O   1 
HETATM 3570 O O   . HOH N 6 .   ? 30.520  -11.524 18.802  1.00 49.97 ? 495 HOH A O   1 
HETATM 3571 O O   . HOH N 6 .   ? 7.715   -21.070 3.915   1.00 40.84 ? 496 HOH A O   1 
HETATM 3572 O O   . HOH N 6 .   ? 31.697  -15.196 15.600  1.00 49.01 ? 497 HOH A O   1 
HETATM 3573 O O   . HOH N 6 .   ? 27.203  -7.311  -11.875 1.00 38.05 ? 498 HOH A O   1 
HETATM 3574 O O   . HOH N 6 .   ? 22.376  -29.520 -7.475  1.00 30.81 ? 499 HOH A O   1 
HETATM 3575 O O   . HOH N 6 .   ? 12.896  -1.181  17.152  1.00 59.33 ? 500 HOH A O   1 
HETATM 3576 O O   . HOH N 6 .   ? 14.480  -18.713 -1.377  1.00 24.68 ? 501 HOH A O   1 
HETATM 3577 O O   . HOH N 6 .   ? 14.174  -25.726 14.162  1.00 52.24 ? 502 HOH A O   1 
HETATM 3578 O O   . HOH N 6 .   ? 21.238  -34.595 14.544  1.00 51.10 ? 503 HOH A O   1 
HETATM 3579 O O   . HOH N 6 .   ? 34.586  -19.594 -14.603 1.00 52.97 ? 504 HOH A O   1 
HETATM 3580 O O   . HOH N 6 .   ? 5.571   4.977   4.275   1.00 49.23 ? 505 HOH A O   1 
HETATM 3581 O O   . HOH N 6 .   ? 23.273  -6.184  -10.556 1.00 47.02 ? 506 HOH A O   1 
HETATM 3582 O O   . HOH N 6 .   ? 26.773  -19.891 25.023  1.00 48.35 ? 507 HOH A O   1 
HETATM 3583 O O   . HOH N 6 .   ? 27.487  -17.040 11.112  1.00 24.62 ? 508 HOH A O   1 
HETATM 3584 O O   . HOH N 6 .   ? 31.273  -16.126 12.674  1.00 34.23 ? 509 HOH A O   1 
HETATM 3585 O O   . HOH N 6 .   ? 40.050  -23.198 -0.609  1.00 50.87 ? 510 HOH A O   1 
HETATM 3586 O O   . HOH N 6 .   ? 35.654  -11.619 12.159  1.00 51.56 ? 511 HOH A O   1 
HETATM 3587 O O   . HOH N 6 .   ? 18.924  -12.185 -10.935 1.00 38.98 ? 512 HOH A O   1 
HETATM 3588 O O   . HOH N 6 .   ? 30.792  -22.132 23.338  1.00 50.59 ? 513 HOH A O   1 
HETATM 3589 O O   . HOH N 6 .   ? 30.339  9.217   12.306  1.00 69.55 ? 514 HOH A O   1 
HETATM 3590 O O   . HOH N 6 .   ? 16.438  -8.811  -11.198 1.00 32.82 ? 515 HOH A O   1 
HETATM 3591 O O   . HOH N 6 .   ? 11.834  -21.253 -11.218 1.00 55.23 ? 516 HOH A O   1 
HETATM 3592 O O   . HOH N 6 .   ? 38.133  -17.148 -1.646  1.00 43.29 ? 517 HOH A O   1 
HETATM 3593 O O   . HOH N 6 .   ? -3.729  -5.280  6.285   1.00 53.35 ? 518 HOH A O   1 
HETATM 3594 O O   . HOH N 6 .   ? 5.282   -11.776 13.359  1.00 53.86 ? 519 HOH A O   1 
HETATM 3595 O O   . HOH N 6 .   ? 35.504  -17.437 -11.398 1.00 38.11 ? 520 HOH A O   1 
HETATM 3596 O O   . HOH N 6 .   ? 6.466   -10.450 15.502  1.00 58.74 ? 521 HOH A O   1 
HETATM 3597 O O   . HOH N 6 .   ? 19.103  -22.830 18.504  1.00 43.53 ? 522 HOH A O   1 
HETATM 3598 O O   . HOH N 6 .   ? 34.137  -24.225 -8.038  1.00 55.92 ? 523 HOH A O   1 
HETATM 3599 O O   . HOH N 6 .   ? 36.945  1.939   8.959   1.00 67.69 ? 524 HOH A O   1 
HETATM 3600 O O   . HOH N 6 .   ? 29.472  -24.508 21.085  1.00 39.67 ? 525 HOH A O   1 
HETATM 3601 O O   . HOH N 6 .   ? 25.842  -16.608 13.243  1.00 51.38 ? 526 HOH A O   1 
HETATM 3602 O O   . HOH N 6 .   ? -1.531  -10.626 -5.295  1.00 56.07 ? 527 HOH A O   1 
HETATM 3603 O O   . HOH N 6 .   ? 31.915  -13.050 -12.126 1.00 56.29 ? 528 HOH A O   1 
HETATM 3604 O O   . HOH N 6 .   ? 34.610  4.206   6.422   1.00 39.09 ? 529 HOH A O   1 
HETATM 3605 O O   . HOH N 6 .   ? 27.244  -17.309 22.861  1.00 48.75 ? 530 HOH A O   1 
HETATM 3606 O O   . HOH N 6 .   ? 12.146  -27.172 8.029   1.00 48.92 ? 531 HOH A O   1 
HETATM 3607 O O   . HOH N 6 .   ? 23.729  0.687   20.208  1.00 60.89 ? 532 HOH A O   1 
HETATM 3608 O O   . HOH N 6 .   ? 35.362  -21.305 17.446  1.00 36.84 ? 533 HOH A O   1 
HETATM 3609 O O   . HOH N 6 .   ? 34.150  -11.811 17.143  1.00 43.17 ? 534 HOH A O   1 
HETATM 3610 O O   . HOH N 6 .   ? 26.282  -20.579 29.874  1.00 27.79 ? 535 HOH A O   1 
HETATM 3611 O O   . HOH N 6 .   ? 33.347  -19.361 16.061  1.00 56.81 ? 536 HOH A O   1 
HETATM 3612 O O   . HOH N 6 .   ? 32.321  -19.707 12.818  1.00 41.24 ? 537 HOH A O   1 
HETATM 3613 O O   . HOH N 6 .   ? 32.942  -32.333 6.101   1.00 41.90 ? 538 HOH A O   1 
HETATM 3614 O O   . HOH N 6 .   ? 9.630   -28.071 -10.903 1.00 56.82 ? 539 HOH A O   1 
HETATM 3615 O O   . HOH N 6 .   ? 28.413  -31.585 5.452   1.00 40.65 ? 540 HOH A O   1 
HETATM 3616 O O   . HOH N 6 .   ? 35.529  -17.663 9.782   1.00 51.83 ? 541 HOH A O   1 
HETATM 3617 O O   . HOH N 6 .   ? 16.806  -6.191  17.690  1.00 50.23 ? 542 HOH A O   1 
HETATM 3618 O O   . HOH N 6 .   ? 30.073  -19.394 12.826  1.00 49.36 ? 543 HOH A O   1 
HETATM 3619 O O   . HOH N 6 .   ? 10.715  -29.915 5.048   1.00 64.10 ? 544 HOH A O   1 
HETATM 3620 O O   . HOH N 6 .   ? 21.060  3.856   22.017  1.00 49.32 ? 545 HOH A O   1 
HETATM 3621 O O   . HOH N 6 .   ? 22.728  -16.157 14.649  1.00 47.69 ? 546 HOH A O   1 
HETATM 3622 O O   . HOH N 6 .   ? 13.930  -5.104  -14.310 1.00 43.88 ? 547 HOH A O   1 
HETATM 3623 O O   . HOH N 6 .   ? 16.670  -4.067  -11.916 1.00 37.86 ? 548 HOH A O   1 
HETATM 3624 O O   . HOH N 6 .   ? 29.259  -11.451 -12.035 1.00 51.75 ? 549 HOH A O   1 
HETATM 3625 O O   . HOH N 6 .   ? 45.893  -19.226 4.194   1.00 42.65 ? 550 HOH A O   1 
HETATM 3626 O O   . HOH N 6 .   ? 19.072  -28.761 -15.064 1.00 39.57 ? 551 HOH A O   1 
HETATM 3627 O O   . HOH N 6 .   ? 12.809  -22.886 -14.471 1.00 41.08 ? 552 HOH A O   1 
HETATM 3628 O O   . HOH N 6 .   ? 23.552  -3.163  -7.112  1.00 44.35 ? 553 HOH A O   1 
HETATM 3629 O O   . HOH N 6 .   ? 14.949  -13.537 -10.872 1.00 42.90 ? 554 HOH A O   1 
HETATM 3630 O O   . HOH N 6 .   ? 35.850  -16.223 7.801   1.00 38.22 ? 555 HOH A O   1 
HETATM 3631 O O   . HOH N 6 .   ? 32.660  5.534   2.925   1.00 41.95 ? 556 HOH A O   1 
HETATM 3632 O O   . HOH N 6 .   ? 33.277  -9.286  18.820  1.00 42.25 ? 557 HOH A O   1 
HETATM 3633 O O   . HOH N 6 .   ? 37.656  -15.251 2.569   1.00 53.32 ? 558 HOH A O   1 
HETATM 3634 O O   . HOH N 6 .   ? 5.422   -26.662 -8.926  1.00 62.39 ? 559 HOH A O   1 
HETATM 3635 O O   . HOH N 6 .   ? 26.660  -30.329 15.429  1.00 48.14 ? 560 HOH A O   1 
HETATM 3636 O O   . HOH N 6 .   ? 29.125  -22.167 18.195  1.00 38.61 ? 561 HOH A O   1 
HETATM 3637 O O   . HOH N 6 .   ? 0.556   -17.851 -1.881  1.00 54.06 ? 562 HOH A O   1 
HETATM 3638 O O   . HOH N 6 .   ? 27.394  3.424   13.884  1.00 51.07 ? 563 HOH A O   1 
HETATM 3639 O O   . HOH N 6 .   ? 7.451   2.145   -9.950  1.00 39.36 ? 564 HOH A O   1 
HETATM 3640 O O   . HOH N 6 .   ? 29.551  -18.977 15.623  1.00 37.77 ? 565 HOH A O   1 
HETATM 3641 O O   . HOH N 6 .   ? 42.823  -20.483 1.071   1.00 51.62 ? 566 HOH A O   1 
HETATM 3642 O O   . HOH N 6 .   ? 2.534   -23.890 -4.005  1.00 48.81 ? 567 HOH A O   1 
HETATM 3643 O O   . HOH N 6 .   ? 30.560  -24.431 19.065  1.00 26.65 ? 568 HOH A O   1 
HETATM 3644 O O   . HOH O 6 .   ? -10.444 -19.203 17.595  1.00 29.82 ? 401 HOH B O   1 
HETATM 3645 O O   . HOH O 6 .   ? 5.012   -18.511 12.826  1.00 34.16 ? 402 HOH B O   1 
HETATM 3646 O O   . HOH O 6 .   ? -6.151  -1.791  27.202  1.00 40.20 ? 403 HOH B O   1 
HETATM 3647 O O   . HOH O 6 .   ? 12.910  -21.887 17.759  1.00 44.36 ? 404 HOH B O   1 
HETATM 3648 O O   . HOH O 6 .   ? 0.405   -2.941  30.045  1.00 52.93 ? 405 HOH B O   1 
HETATM 3649 O O   . HOH O 6 .   ? -4.943  -9.170  42.498  1.00 33.86 ? 406 HOH B O   1 
HETATM 3650 O O   . HOH O 6 .   ? -11.115 -17.862 22.146  1.00 37.47 ? 407 HOH B O   1 
HETATM 3651 O O   . HOH O 6 .   ? 10.174  -8.892  27.696  1.00 45.61 ? 408 HOH B O   1 
HETATM 3652 O O   . HOH O 6 .   ? 10.953  -16.564 27.571  1.00 26.00 ? 409 HOH B O   1 
HETATM 3653 O O   . HOH O 6 .   ? 17.476  -20.264 20.973  1.00 40.48 ? 410 HOH B O   1 
HETATM 3654 O O   . HOH O 6 .   ? 2.032   -33.065 31.319  1.00 36.91 ? 411 HOH B O   1 
HETATM 3655 O O   . HOH O 6 .   ? -6.189  -35.406 17.473  1.00 46.50 ? 412 HOH B O   1 
HETATM 3656 O O   . HOH O 6 .   ? -3.723  -9.033  30.458  1.00 21.47 ? 413 HOH B O   1 
HETATM 3657 O O   . HOH O 6 .   ? 2.324   -18.926 43.351  1.00 48.23 ? 414 HOH B O   1 
HETATM 3658 O O   . HOH O 6 .   ? 2.379   -11.792 21.891  1.00 36.58 ? 415 HOH B O   1 
HETATM 3659 O O   . HOH O 6 .   ? -2.767  -35.976 35.356  1.00 30.98 ? 416 HOH B O   1 
HETATM 3660 O O   . HOH O 6 .   ? 0.076   -21.346 16.839  1.00 29.49 ? 417 HOH B O   1 
HETATM 3661 O O   . HOH O 6 .   ? -6.878  -15.828 46.085  1.00 55.92 ? 418 HOH B O   1 
HETATM 3662 O O   . HOH O 6 .   ? -1.079  -24.284 47.323  1.00 37.69 ? 419 HOH B O   1 
HETATM 3663 O O   . HOH O 6 .   ? 3.373   -5.898  32.100  1.00 32.63 ? 420 HOH B O   1 
HETATM 3664 O O   . HOH O 6 .   ? 2.540   -11.855 33.586  1.00 28.94 ? 421 HOH B O   1 
HETATM 3665 O O   . HOH O 6 .   ? -5.836  -27.580 25.866  1.00 27.68 ? 422 HOH B O   1 
HETATM 3666 O O   . HOH O 6 .   ? 15.365  -34.179 30.959  1.00 73.11 ? 423 HOH B O   1 
HETATM 3667 O O   . HOH O 6 .   ? -8.677  -28.965 26.640  1.00 33.99 ? 424 HOH B O   1 
HETATM 3668 O O   . HOH O 6 .   ? -8.133  -18.937 19.193  1.00 33.90 ? 425 HOH B O   1 
HETATM 3669 O O   . HOH O 6 .   ? 5.113   -16.572 43.283  1.00 51.47 ? 426 HOH B O   1 
HETATM 3670 O O   . HOH O 6 .   ? 11.369  -16.475 46.260  1.00 62.50 ? 427 HOH B O   1 
HETATM 3671 O O   . HOH O 6 .   ? -7.053  -23.567 20.444  1.00 31.26 ? 428 HOH B O   1 
HETATM 3672 O O   . HOH O 6 .   ? -0.013  -14.174 21.042  1.00 36.28 ? 429 HOH B O   1 
HETATM 3673 O O   . HOH O 6 .   ? 11.665  -25.151 16.820  1.00 30.40 ? 430 HOH B O   1 
HETATM 3674 O O   . HOH O 6 .   ? -2.488  -18.566 23.969  1.00 29.34 ? 431 HOH B O   1 
HETATM 3675 O O   . HOH O 6 .   ? -16.446 -20.111 26.613  1.00 57.36 ? 432 HOH B O   1 
HETATM 3676 O O   . HOH O 6 .   ? -15.870 -9.756  30.157  1.00 43.75 ? 433 HOH B O   1 
HETATM 3677 O O   . HOH O 6 .   ? -7.728  -19.565 41.775  1.00 41.93 ? 434 HOH B O   1 
HETATM 3678 O O   . HOH O 6 .   ? -5.096  -25.393 21.334  1.00 26.70 ? 435 HOH B O   1 
HETATM 3679 O O   . HOH O 6 .   ? 0.161   -12.992 40.384  1.00 44.27 ? 436 HOH B O   1 
HETATM 3680 O O   . HOH O 6 .   ? -7.036  -36.730 26.191  1.00 50.43 ? 437 HOH B O   1 
HETATM 3681 O O   . HOH O 6 .   ? 1.880   -21.308 38.903  1.00 22.37 ? 438 HOH B O   1 
HETATM 3682 O O   . HOH O 6 .   ? 2.204   -19.971 19.517  1.00 23.81 ? 439 HOH B O   1 
HETATM 3683 O O   . HOH O 6 .   ? 26.083  -23.503 50.184  1.00 55.89 ? 440 HOH B O   1 
HETATM 3684 O O   . HOH O 6 .   ? 1.022   -6.447  38.566  1.00 37.27 ? 441 HOH B O   1 
HETATM 3685 O O   . HOH O 6 .   ? 5.438   -18.842 40.203  1.00 40.81 ? 442 HOH B O   1 
HETATM 3686 O O   . HOH O 6 .   ? 14.723  -13.741 48.142  1.00 51.22 ? 443 HOH B O   1 
HETATM 3687 O O   . HOH O 6 .   ? 4.210   -15.577 13.507  1.00 34.59 ? 444 HOH B O   1 
HETATM 3688 O O   . HOH O 6 .   ? 13.239  -15.784 26.074  1.00 34.75 ? 445 HOH B O   1 
HETATM 3689 O O   . HOH O 6 .   ? 7.826   -23.805 48.389  1.00 27.90 ? 446 HOH B O   1 
HETATM 3690 O O   . HOH O 6 .   ? -3.293  -9.898  48.288  1.00 41.37 ? 447 HOH B O   1 
HETATM 3691 O O   . HOH O 6 .   ? 2.909   -18.832 38.991  1.00 21.61 ? 448 HOH B O   1 
HETATM 3692 O O   . HOH O 6 .   ? -15.585 -13.533 29.710  1.00 39.84 ? 449 HOH B O   1 
HETATM 3693 O O   . HOH O 6 .   ? 5.753   -34.818 35.500  1.00 47.68 ? 450 HOH B O   1 
HETATM 3694 O O   . HOH O 6 .   ? 17.618  -29.702 43.410  1.00 69.44 ? 451 HOH B O   1 
HETATM 3695 O O   . HOH O 6 .   ? -13.378 -26.691 24.049  1.00 51.61 ? 452 HOH B O   1 
HETATM 3696 O O   . HOH O 6 .   ? -11.917 -9.099  20.275  1.00 49.05 ? 453 HOH B O   1 
HETATM 3697 O O   . HOH O 6 .   ? -9.790  -27.096 20.838  1.00 38.69 ? 454 HOH B O   1 
HETATM 3698 O O   . HOH O 6 .   ? -0.226  -17.227 23.047  1.00 32.52 ? 455 HOH B O   1 
HETATM 3699 O O   . HOH O 6 .   ? 8.728   -13.446 39.904  1.00 47.55 ? 456 HOH B O   1 
HETATM 3700 O O   . HOH O 6 .   ? -10.224 -30.649 39.521  1.00 60.98 ? 457 HOH B O   1 
HETATM 3701 O O   . HOH O 6 .   ? 7.579   -14.965 19.324  1.00 36.35 ? 458 HOH B O   1 
HETATM 3702 O O   . HOH O 6 .   ? 0.396   -28.707 53.596  1.00 51.19 ? 459 HOH B O   1 
HETATM 3703 O O   . HOH O 6 .   ? 8.182   -18.261 37.293  1.00 43.63 ? 460 HOH B O   1 
HETATM 3704 O O   . HOH O 6 .   ? 12.608  -29.210 20.604  1.00 38.87 ? 461 HOH B O   1 
HETATM 3705 O O   . HOH O 6 .   ? -7.444  -35.274 34.796  1.00 53.56 ? 462 HOH B O   1 
HETATM 3706 O O   . HOH O 6 .   ? 7.781   -19.490 39.797  1.00 46.00 ? 463 HOH B O   1 
HETATM 3707 O O   . HOH O 6 .   ? -5.684  -13.905 53.403  1.00 55.80 ? 464 HOH B O   1 
HETATM 3708 O O   . HOH O 6 .   ? -11.985 -30.604 17.162  1.00 48.52 ? 465 HOH B O   1 
HETATM 3709 O O   . HOH O 6 .   ? 12.392  -6.290  31.229  1.00 41.93 ? 466 HOH B O   1 
HETATM 3710 O O   . HOH O 6 .   ? -11.234 -3.424  31.318  1.00 34.22 ? 467 HOH B O   1 
HETATM 3711 O O   . HOH O 6 .   ? 8.293   -12.992 46.234  1.00 36.60 ? 468 HOH B O   1 
HETATM 3712 O O   . HOH O 6 .   ? -1.802  -3.601  43.147  1.00 42.60 ? 469 HOH B O   1 
HETATM 3713 O O   . HOH O 6 .   ? -9.079  -5.959  27.481  1.00 42.40 ? 470 HOH B O   1 
HETATM 3714 O O   . HOH O 6 .   ? 18.965  -15.503 45.867  1.00 46.32 ? 471 HOH B O   1 
HETATM 3715 O O   . HOH O 6 .   ? -14.673 -11.072 38.121  1.00 50.21 ? 472 HOH B O   1 
HETATM 3716 O O   . HOH O 6 .   ? -10.802 -23.390 23.098  1.00 56.83 ? 473 HOH B O   1 
HETATM 3717 O O   . HOH O 6 .   ? 10.523  -30.554 38.964  1.00 55.59 ? 474 HOH B O   1 
HETATM 3718 O O   . HOH O 6 .   ? 1.475   -38.309 13.530  1.00 59.40 ? 475 HOH B O   1 
HETATM 3719 O O   . HOH O 6 .   ? -11.130 -4.199  28.885  1.00 32.89 ? 476 HOH B O   1 
HETATM 3720 O O   . HOH O 6 .   ? -9.025  -15.005 16.571  1.00 51.95 ? 477 HOH B O   1 
HETATM 3721 O O   . HOH O 6 .   ? -0.350  -4.282  38.522  1.00 42.63 ? 478 HOH B O   1 
HETATM 3722 O O   . HOH O 6 .   ? -6.643  -19.014 53.414  1.00 39.21 ? 479 HOH B O   1 
HETATM 3723 O O   . HOH O 6 .   ? 10.079  -23.549 46.713  1.00 34.35 ? 480 HOH B O   1 
HETATM 3724 O O   . HOH O 6 .   ? 20.299  -19.797 30.948  1.00 40.94 ? 481 HOH B O   1 
HETATM 3725 O O   . HOH O 6 .   ? 2.984   -12.729 17.202  1.00 48.57 ? 482 HOH B O   1 
HETATM 3726 O O   . HOH O 6 .   ? 12.886  -40.624 34.642  1.00 52.31 ? 483 HOH B O   1 
HETATM 3727 O O   . HOH O 6 .   ? -5.514  -33.250 49.482  1.00 66.35 ? 484 HOH B O   1 
HETATM 3728 O O   . HOH O 6 .   ? 20.898  -21.902 51.818  1.00 44.39 ? 485 HOH B O   1 
HETATM 3729 O O   . HOH O 6 .   ? 19.913  -23.742 26.394  1.00 46.42 ? 486 HOH B O   1 
HETATM 3730 O O   . HOH O 6 .   ? -1.850  -29.907 7.418   1.00 48.71 ? 487 HOH B O   1 
HETATM 3731 O O   . HOH O 6 .   ? 12.502  -4.286  34.033  1.00 65.40 ? 488 HOH B O   1 
HETATM 3732 O O   . HOH O 6 .   ? 15.384  -33.628 34.964  1.00 60.49 ? 489 HOH B O   1 
HETATM 3733 O O   . HOH O 6 .   ? 17.997  -35.078 29.453  1.00 64.99 ? 490 HOH B O   1 
HETATM 3734 O O   . HOH O 6 .   ? 2.554   -3.311  45.388  1.00 41.28 ? 491 HOH B O   1 
HETATM 3735 O O   . HOH O 6 .   ? 13.312  -6.694  33.878  1.00 47.50 ? 492 HOH B O   1 
HETATM 3736 O O   . HOH O 6 .   ? -9.280  -21.408 19.718  1.00 44.60 ? 493 HOH B O   1 
HETATM 3737 O O   . HOH O 6 .   ? 24.002  -21.932 36.497  1.00 48.66 ? 494 HOH B O   1 
HETATM 3738 O O   . HOH O 6 .   ? -17.823 -22.727 33.828  1.00 56.22 ? 495 HOH B O   1 
HETATM 3739 O O   . HOH O 6 .   ? -4.122  -15.744 17.322  1.00 37.14 ? 496 HOH B O   1 
HETATM 3740 O O   . HOH O 6 .   ? 4.278   -4.304  43.475  1.00 52.74 ? 497 HOH B O   1 
HETATM 3741 O O   . HOH O 6 .   ? -22.863 -28.760 45.892  1.00 44.89 ? 498 HOH B O   1 
HETATM 3742 O O   . HOH O 6 .   ? -9.770  -15.981 49.672  1.00 54.07 ? 499 HOH B O   1 
HETATM 3743 O O   . HOH O 6 .   ? 2.694   -36.856 39.193  1.00 45.70 ? 500 HOH B O   1 
HETATM 3744 O O   . HOH O 6 .   ? -23.322 -32.307 43.827  1.00 44.84 ? 501 HOH B O   1 
HETATM 3745 O O   . HOH O 6 .   ? 17.954  -36.833 38.238  1.00 57.07 ? 502 HOH B O   1 
HETATM 3746 O O   . HOH O 6 .   ? -2.270  -39.225 16.189  1.00 50.58 ? 503 HOH B O   1 
HETATM 3747 O O   . HOH O 6 .   ? 8.237   -13.970 50.440  1.00 43.90 ? 504 HOH B O   1 
HETATM 3748 O O   . HOH O 6 .   ? -13.030 -6.175  20.827  1.00 51.52 ? 505 HOH B O   1 
HETATM 3749 O O   . HOH O 6 .   ? -11.631 -27.948 22.943  1.00 35.08 ? 506 HOH B O   1 
HETATM 3750 O O   . HOH O 6 .   ? -10.627 -36.674 21.885  1.00 54.95 ? 507 HOH B O   1 
HETATM 3751 O O   . HOH O 6 .   ? 9.550   -26.125 48.800  1.00 40.99 ? 508 HOH B O   1 
HETATM 3752 O O   . HOH O 6 .   ? -7.362  -20.657 51.437  1.00 26.95 ? 509 HOH B O   1 
HETATM 3753 O O   . HOH O 6 .   ? -11.643 -28.905 25.263  1.00 41.52 ? 510 HOH B O   1 
HETATM 3754 O O   . HOH O 6 .   ? -9.963  -6.159  23.079  1.00 42.84 ? 511 HOH B O   1 
HETATM 3755 O O   . HOH O 6 .   ? -13.475 -27.314 18.885  1.00 33.04 ? 512 HOH B O   1 
HETATM 3756 O O   . HOH O 6 .   ? 8.492   -11.548 50.284  1.00 52.00 ? 513 HOH B O   1 
HETATM 3757 O O   . HOH O 6 .   ? 3.730   -20.756 50.789  1.00 43.98 ? 514 HOH B O   1 
HETATM 3758 O O   . HOH O 6 .   ? -9.752  -14.511 14.169  1.00 45.09 ? 515 HOH B O   1 
HETATM 3759 O O   . HOH O 6 .   ? 2.827   -38.892 42.832  1.00 42.24 ? 516 HOH B O   1 
HETATM 3760 O O   . HOH O 6 .   ? -14.124 -27.083 21.394  1.00 44.56 ? 517 HOH B O   1 
HETATM 3761 O O   . HOH O 6 .   ? 4.690   -37.879 40.538  1.00 37.00 ? 518 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   . ALA A 9   ? 0.5063 0.4597 0.7845 -0.0336 -0.1985 0.0273  11  ALA A N   
2    C CA  . ALA A 9   ? 0.5006 0.4540 0.7544 -0.0282 -0.1941 0.0257  11  ALA A CA  
3    C C   . ALA A 9   ? 0.4792 0.4460 0.7395 -0.0267 -0.1769 0.0266  11  ALA A C   
4    O O   . ALA A 9   ? 0.4789 0.4562 0.7649 -0.0300 -0.1708 0.0303  11  ALA A O   
5    C CB  . ALA A 9   ? 0.4984 0.4506 0.7525 -0.0286 -0.2044 0.0297  11  ALA A CB  
6    N N   . ARG A 10  ? 0.4636 0.4299 0.7012 -0.0217 -0.1687 0.0232  12  ARG A N   
7    C CA  . ARG A 10  ? 0.4213 0.3996 0.6639 -0.0204 -0.1532 0.0234  12  ARG A CA  
8    C C   . ARG A 10  ? 0.3906 0.3784 0.6479 -0.0214 -0.1498 0.0279  12  ARG A C   
9    O O   . ARG A 10  ? 0.4081 0.3931 0.6585 -0.0200 -0.1565 0.0303  12  ARG A O   
10   C CB  . ARG A 10  ? 0.4313 0.4068 0.6479 -0.0148 -0.1470 0.0196  12  ARG A CB  
11   C CG  . ARG A 10  ? 0.4628 0.4495 0.6835 -0.0139 -0.1323 0.0192  12  ARG A CG  
12   C CD  . ARG A 10  ? 0.4984 0.4825 0.6958 -0.0083 -0.1272 0.0161  12  ARG A CD  
13   N NE  . ARG A 10  ? 0.5357 0.5095 0.7204 -0.0068 -0.1316 0.0123  12  ARG A NE  
14   C CZ  . ARG A 10  ? 0.5307 0.5053 0.7213 -0.0084 -0.1280 0.0109  12  ARG A CZ  
15   N NH1 . ARG A 10  ? 0.4796 0.4436 0.6593 -0.0069 -0.1328 0.0077  12  ARG A NH1 
16   N NH2 . ARG A 10  ? 0.5054 0.4910 0.7126 -0.0116 -0.1195 0.0128  12  ARG A NH2 
17   N N   . ILE A 11  ? 0.3513 0.3500 0.6285 -0.0237 -0.1393 0.0292  13  ILE A N   
18   C CA  . ILE A 11  ? 0.3275 0.3354 0.6190 -0.0241 -0.1338 0.0325  13  ILE A CA  
19   C C   . ILE A 11  ? 0.3168 0.3282 0.5917 -0.0199 -0.1249 0.0308  13  ILE A C   
20   O O   . ILE A 11  ? 0.3010 0.3169 0.5728 -0.0192 -0.1148 0.0278  13  ILE A O   
21   C CB  . ILE A 11  ? 0.3101 0.3270 0.6293 -0.0281 -0.1258 0.0337  13  ILE A CB  
22   C CG1 . ILE A 11  ? 0.3281 0.3417 0.6653 -0.0321 -0.1345 0.0362  13  ILE A CG1 
23   C CG2 . ILE A 11  ? 0.2974 0.3224 0.6329 -0.0283 -0.1209 0.0368  13  ILE A CG2 
24   C CD1 . ILE A 11  ? 0.3330 0.3544 0.6948 -0.0356 -0.1254 0.0372  13  ILE A CD1 
25   N N   . ILE A 12  ? 0.3092 0.3185 0.5741 -0.0172 -0.1291 0.0335  14  ILE A N   
26   C CA  . ILE A 12  ? 0.3067 0.3190 0.5570 -0.0132 -0.1216 0.0331  14  ILE A CA  
27   C C   . ILE A 12  ? 0.2878 0.3070 0.5519 -0.0136 -0.1191 0.0379  14  ILE A C   
28   O O   . ILE A 12  ? 0.2785 0.2950 0.5470 -0.0143 -0.1280 0.0425  14  ILE A O   
29   C CB  . ILE A 12  ? 0.3136 0.3161 0.5353 -0.0087 -0.1276 0.0322  14  ILE A CB  
30   C CG1 . ILE A 12  ? 0.3167 0.3102 0.5252 -0.0081 -0.1316 0.0270  14  ILE A CG1 
31   C CG2 . ILE A 12  ? 0.3189 0.3257 0.5283 -0.0044 -0.1185 0.0327  14  ILE A CG2 
32   C CD1 . ILE A 12  ? 0.3518 0.3347 0.5347 -0.0040 -0.1377 0.0255  14  ILE A CD1 
33   N N   . TYR A 13  ? 0.2785 0.3062 0.5498 -0.0134 -0.1078 0.0370  15  TYR A N   
34   C CA  . TYR A 13  ? 0.2698 0.3039 0.5543 -0.0135 -0.1042 0.0412  15  TYR A CA  
35   C C   . TYR A 13  ? 0.2815 0.3172 0.5499 -0.0096 -0.0984 0.0417  15  TYR A C   
36   O O   . TYR A 13  ? 0.2897 0.3278 0.5512 -0.0086 -0.0912 0.0374  15  TYR A O   
37   C CB  . TYR A 13  ? 0.2646 0.3068 0.5727 -0.0167 -0.0954 0.0392  15  TYR A CB  
38   C CG  . TYR A 13  ? 0.2807 0.3228 0.6078 -0.0204 -0.0989 0.0394  15  TYR A CG  
39   C CD1 . TYR A 13  ? 0.2998 0.3416 0.6437 -0.0219 -0.1061 0.0449  15  TYR A CD1 
40   C CD2 . TYR A 13  ? 0.2943 0.3368 0.6239 -0.0224 -0.0950 0.0351  15  TYR A CD2 
41   C CE1 . TYR A 13  ? 0.2987 0.3412 0.6633 -0.0253 -0.1089 0.0458  15  TYR A CE1 
42   C CE2 . TYR A 13  ? 0.2913 0.3343 0.6404 -0.0258 -0.0970 0.0361  15  TYR A CE2 
43   C CZ  . TYR A 13  ? 0.2965 0.3397 0.6636 -0.0272 -0.1041 0.0414  15  TYR A CZ  
44   O OH  . TYR A 13  ? 0.2794 0.3236 0.6680 -0.0304 -0.1063 0.0432  15  TYR A OH  
45   N N   . ASP A 14  ? 0.2692 0.3037 0.5320 -0.0073 -0.1016 0.0472  16  ASP A N   
46   C CA  . ASP A 14  ? 0.2906 0.3290 0.5456 -0.0042 -0.0943 0.0492  16  ASP A CA  
47   C C   . ASP A 14  ? 0.2714 0.3193 0.5488 -0.0065 -0.0854 0.0494  16  ASP A C   
48   O O   . ASP A 14  ? 0.2613 0.3124 0.5605 -0.0100 -0.0849 0.0487  16  ASP A O   
49   C CB  . ASP A 14  ? 0.3179 0.3518 0.5580 -0.0009 -0.0997 0.0558  16  ASP A CB  
50   C CG  . ASP A 14  ? 0.3428 0.3770 0.5971 -0.0027 -0.1064 0.0628  16  ASP A CG  
51   O OD1 . ASP A 14  ? 0.3378 0.3784 0.6174 -0.0059 -0.1033 0.0637  16  ASP A OD1 
52   O OD2 . ASP A 14  ? 0.3773 0.4049 0.6168 -0.0010 -0.1149 0.0671  16  ASP A OD2 
53   N N   . ARG A 15  ? 0.2564 0.3084 0.5287 -0.0042 -0.0782 0.0502  17  ARG A N   
54   C CA  A ARG A 15  ? 0.2406 0.3005 0.5315 -0.0061 -0.0702 0.0497  17  ARG A CA  
55   C CA  B ARG A 15  ? 0.2480 0.3079 0.5388 -0.0061 -0.0702 0.0498  17  ARG A CA  
56   C C   . ARG A 15  ? 0.2601 0.3223 0.5731 -0.0083 -0.0718 0.0546  17  ARG A C   
57   O O   . ARG A 15  ? 0.2580 0.3244 0.5908 -0.0113 -0.0672 0.0516  17  ARG A O   
58   C CB  A ARG A 15  ? 0.2323 0.2955 0.5141 -0.0031 -0.0642 0.0518  17  ARG A CB  
59   C CB  B ARG A 15  ? 0.2583 0.3216 0.5402 -0.0030 -0.0642 0.0520  17  ARG A CB  
60   C CG  A ARG A 15  ? 0.2039 0.2745 0.5034 -0.0054 -0.0565 0.0499  17  ARG A CG  
61   C CG  B ARG A 15  ? 0.2687 0.3395 0.5696 -0.0054 -0.0567 0.0508  17  ARG A CG  
62   C CD  A ARG A 15  ? 0.1760 0.2502 0.4683 -0.0026 -0.0514 0.0526  17  ARG A CD  
63   C CD  B ARG A 15  ? 0.2778 0.3525 0.5741 -0.0027 -0.0516 0.0549  17  ARG A CD  
64   N NE  A ARG A 15  ? 0.1291 0.2100 0.4395 -0.0052 -0.0452 0.0511  17  ARG A NE  
65   N NE  B ARG A 15  ? 0.2564 0.3324 0.5405 -0.0012 -0.0479 0.0503  17  ARG A NE  
66   C CZ  A ARG A 15  ? 0.1319 0.2156 0.4607 -0.0067 -0.0437 0.0552  17  ARG A CZ  
67   C CZ  B ARG A 15  ? 0.1791 0.2543 0.4462 0.0032  -0.0463 0.0526  17  ARG A CZ  
68   N NH1 A ARG A 15  ? 0.1261 0.2073 0.4584 -0.0059 -0.0478 0.0622  17  ARG A NH1 
69   N NH1 B ARG A 15  ? 0.2101 0.2826 0.4667 0.0068  -0.0476 0.0597  17  ARG A NH1 
70   N NH2 A ARG A 15  ? 0.1219 0.2105 0.4659 -0.0093 -0.0386 0.0524  17  ARG A NH2 
71   N NH2 B ARG A 15  ? 0.0477 0.1247 0.3079 0.0040  -0.0432 0.0482  17  ARG A NH2 
72   N N   . ALA A 16  ? 0.2860 0.3449 0.5953 -0.0067 -0.0784 0.0623  18  ALA A N   
73   C CA  . ALA A 16  ? 0.3116 0.3726 0.6430 -0.0085 -0.0809 0.0682  18  ALA A CA  
74   C C   . ALA A 16  ? 0.3345 0.3952 0.6850 -0.0119 -0.0843 0.0657  18  ALA A C   
75   O O   . ALA A 16  ? 0.3417 0.4066 0.7168 -0.0142 -0.0805 0.0658  18  ALA A O   
76   C CB  . ALA A 16  ? 0.3170 0.3739 0.6371 -0.0060 -0.0885 0.0774  18  ALA A CB  
77   N N   . PHE A 17  ? 0.3520 0.4077 0.6928 -0.0124 -0.0910 0.0634  19  PHE A N   
78   C CA  . PHE A 17  ? 0.3626 0.4185 0.7224 -0.0156 -0.0939 0.0616  19  PHE A CA  
79   C C   . PHE A 17  ? 0.3609 0.4220 0.7358 -0.0179 -0.0832 0.0544  19  PHE A C   
80   O O   . PHE A 17  ? 0.3464 0.4110 0.7461 -0.0200 -0.0801 0.0547  19  PHE A O   
81   C CB  . PHE A 17  ? 0.3813 0.4304 0.7260 -0.0157 -0.1030 0.0601  19  PHE A CB  
82   C CG  . PHE A 17  ? 0.3836 0.4325 0.7497 -0.0189 -0.1085 0.0613  19  PHE A CG  
83   C CD1 . PHE A 17  ? 0.3816 0.4337 0.7619 -0.0215 -0.1023 0.0558  19  PHE A CD1 
84   C CD2 . PHE A 17  ? 0.4111 0.4576 0.7856 -0.0195 -0.1194 0.0686  19  PHE A CD2 
85   C CE1 . PHE A 17  ? 0.3931 0.4460 0.7962 -0.0244 -0.1062 0.0576  19  PHE A CE1 
86   C CE2 . PHE A 17  ? 0.4178 0.4652 0.8158 -0.0226 -0.1245 0.0704  19  PHE A CE2 
87   C CZ  . PHE A 17  ? 0.3976 0.4483 0.8103 -0.0249 -0.1174 0.0648  19  PHE A CZ  
88   N N   . LEU A 18  ? 0.3626 0.4241 0.7225 -0.0174 -0.0774 0.0479  20  LEU A N   
89   C CA  . LEU A 18  ? 0.3417 0.4074 0.7118 -0.0196 -0.0677 0.0408  20  LEU A CA  
90   C C   . LEU A 18  ? 0.3411 0.4116 0.7303 -0.0205 -0.0609 0.0410  20  LEU A C   
91   O O   . LEU A 18  ? 0.3456 0.4184 0.7539 -0.0227 -0.0556 0.0376  20  LEU A O   
92   C CB  . LEU A 18  ? 0.3234 0.3889 0.6723 -0.0186 -0.0637 0.0352  20  LEU A CB  
93   C CG  . LEU A 18  ? 0.3216 0.3818 0.6538 -0.0180 -0.0693 0.0339  20  LEU A CG  
94   C CD1 . LEU A 18  ? 0.3411 0.4011 0.6541 -0.0165 -0.0656 0.0296  20  LEU A CD1 
95   C CD2 . LEU A 18  ? 0.3260 0.3857 0.6714 -0.0210 -0.0698 0.0319  20  LEU A CD2 
96   N N   . MET A 19  ? 0.3503 0.4219 0.7351 -0.0186 -0.0607 0.0449  21  MET A N   
97   C CA  . MET A 19  ? 0.3469 0.4222 0.7503 -0.0194 -0.0552 0.0458  21  MET A CA  
98   C C   . MET A 19  ? 0.3729 0.4486 0.8024 -0.0206 -0.0574 0.0503  21  MET A C   
99   O O   . MET A 19  ? 0.3730 0.4511 0.8226 -0.0221 -0.0510 0.0474  21  MET A O   
100  C CB  . MET A 19  ? 0.3363 0.4126 0.7303 -0.0170 -0.0554 0.0511  21  MET A CB  
101  C CG  . MET A 19  ? 0.3409 0.4183 0.7150 -0.0157 -0.0517 0.0472  21  MET A CG  
102  S SD  . MET A 19  ? 0.3826 0.4634 0.7616 -0.0186 -0.0430 0.0365  21  MET A SD  
103  C CE  . MET A 19  ? 0.4308 0.5147 0.7970 -0.0167 -0.0404 0.0376  21  MET A CE  
104  N N   . ALA A 20  ? 0.3950 0.4680 0.8248 -0.0199 -0.0666 0.0569  22  ALA A N   
105  C CA  . ALA A 20  ? 0.4017 0.4753 0.8578 -0.0210 -0.0697 0.0621  22  ALA A CA  
106  C C   . ALA A 20  ? 0.4232 0.4979 0.8970 -0.0233 -0.0660 0.0566  22  ALA A C   
107  O O   . ALA A 20  ? 0.4097 0.4864 0.9106 -0.0243 -0.0636 0.0581  22  ALA A O   
108  C CB  . ALA A 20  ? 0.4019 0.4721 0.8510 -0.0198 -0.0821 0.0713  22  ALA A CB  
109  N N   . CYS A 21  ? 0.4458 0.5192 0.9051 -0.0241 -0.0650 0.0507  23  CYS A N   
110  C CA  . CYS A 21  ? 0.4565 0.5312 0.9303 -0.0262 -0.0594 0.0454  23  CYS A CA  
111  C C   . CYS A 21  ? 0.4588 0.5363 0.9408 -0.0272 -0.0463 0.0371  23  CYS A C   
112  O O   . CYS A 21  ? 0.4652 0.5437 0.9570 -0.0286 -0.0399 0.0323  23  CYS A O   
113  C CB  . CYS A 21  ? 0.4739 0.5460 0.9296 -0.0268 -0.0628 0.0428  23  CYS A CB  
114  S SG  . CYS A 21  ? 0.5328 0.5998 0.9785 -0.0261 -0.0787 0.0506  23  CYS A SG  
115  N N   . ARG A 22  ? 0.4521 0.5304 0.9298 -0.0264 -0.0426 0.0356  24  ARG A N   
116  C CA  A ARG A 22  ? 0.4575 0.5372 0.9389 -0.0275 -0.0319 0.0271  24  ARG A CA  
117  C CA  B ARG A 22  ? 0.4630 0.5427 0.9439 -0.0275 -0.0320 0.0271  24  ARG A CA  
118  C C   . ARG A 22  ? 0.4917 0.5723 1.0022 -0.0279 -0.0266 0.0268  24  ARG A C   
119  O O   . ARG A 22  ? 0.4980 0.5789 1.0242 -0.0270 -0.0318 0.0348  24  ARG A O   
120  C CB  A ARG A 22  ? 0.4265 0.5066 0.8908 -0.0267 -0.0317 0.0262  24  ARG A CB  
121  C CB  B ARG A 22  ? 0.4458 0.5259 0.9105 -0.0266 -0.0323 0.0270  24  ARG A CB  
122  C CG  A ARG A 22  ? 0.3800 0.4608 0.8451 -0.0282 -0.0228 0.0172  24  ARG A CG  
123  C CG  B ARG A 22  ? 0.4275 0.5085 0.8889 -0.0279 -0.0240 0.0181  24  ARG A CG  
124  C CD  A ARG A 22  ? 0.3565 0.4384 0.8065 -0.0276 -0.0239 0.0175  24  ARG A CD  
125  C CD  B ARG A 22  ? 0.4242 0.5063 0.8861 -0.0273 -0.0244 0.0207  24  ARG A CD  
126  N NE  A ARG A 22  ? 0.3239 0.4061 0.7716 -0.0295 -0.0170 0.0083  24  ARG A NE  
127  N NE  B ARG A 22  ? 0.4134 0.4965 0.8595 -0.0281 -0.0214 0.0147  24  ARG A NE  
128  C CZ  A ARG A 22  ? 0.2896 0.3733 0.7262 -0.0297 -0.0171 0.0070  24  ARG A CZ  
129  C CZ  B ARG A 22  ? 0.3900 0.4727 0.8376 -0.0303 -0.0148 0.0053  24  ARG A CZ  
130  N NH1 A ARG A 22  ? 0.2813 0.3665 0.7083 -0.0276 -0.0223 0.0144  24  ARG A NH1 
131  N NH1 B ARG A 22  ? 0.3562 0.4371 0.8195 -0.0316 -0.0091 0.0001  24  ARG A NH1 
132  N NH2 A ARG A 22  ? 0.2655 0.3489 0.7006 -0.0319 -0.0121 -0.0016 24  ARG A NH2 
133  N NH2 B ARG A 22  ? 0.3597 0.4434 0.7927 -0.0311 -0.0139 0.0010  24  ARG A NH2 
134  N N   . GLY A 23  ? 0.5346 0.6152 1.0513 -0.0292 -0.0163 0.0176  25  GLY A N   
135  C CA  . GLY A 23  ? 0.5623 0.6426 1.1060 -0.0294 -0.0093 0.0150  25  GLY A CA  
136  C C   . GLY A 23  ? 0.5885 0.6694 1.1530 -0.0294 -0.0056 0.0152  25  GLY A C   
137  O O   . GLY A 23  ? 0.5929 0.6734 1.1822 -0.0291 0.0011  0.0131  25  GLY A O   
138  N N   . GLY A 24  ? 0.5958 0.6775 1.1520 -0.0297 -0.0096 0.0179  26  GLY A N   
139  C CA  . GLY A 24  ? 0.5982 0.6813 1.1750 -0.0300 -0.0072 0.0197  26  GLY A CA  
140  C C   . GLY A 24  ? 0.6011 0.6855 1.2048 -0.0290 -0.0140 0.0294  26  GLY A C   
141  O O   . GLY A 24  ? 0.5996 0.6835 1.2011 -0.0282 -0.0226 0.0360  26  GLY A O   
142  N N   . GLY A 25  ? 0.6018 0.6880 1.2312 -0.0290 -0.0099 0.0306  27  GLY A N   
143  C CA  . GLY A 25  ? 0.6009 0.6889 1.2615 -0.0281 -0.0152 0.0396  27  GLY A CA  
144  C C   . GLY A 25  ? 0.5994 0.6900 1.2756 -0.0288 -0.0193 0.0451  27  GLY A C   
145  O O   . GLY A 25  ? 0.5997 0.6928 1.3084 -0.0282 -0.0149 0.0477  27  GLY A O   
146  N N   . GLY A 26  ? 0.5956 0.6854 1.2499 -0.0301 -0.0277 0.0472  28  GLY A N   
147  C CA  . GLY A 26  ? 0.5792 0.6708 1.2462 -0.0314 -0.0347 0.0534  28  GLY A CA  
148  C C   . GLY A 26  ? 0.5514 0.6463 1.2405 -0.0318 -0.0222 0.0499  28  GLY A C   
149  O O   . GLY A 26  ? 0.5599 0.6542 1.2374 -0.0318 -0.0091 0.0407  28  GLY A O   
150  N N   . GLU A 27  ? 0.5133 0.6115 1.2344 -0.0322 -0.0262 0.0576  29  GLU A N   
151  C CA  . GLU A 27  ? 0.4812 0.5833 1.2277 -0.0324 -0.0144 0.0562  29  GLU A CA  
152  C C   . GLU A 27  ? 0.4448 0.5469 1.1748 -0.0345 -0.0136 0.0543  29  GLU A C   
153  O O   . GLU A 27  ? 0.4468 0.5512 1.1857 -0.0346 0.0005  0.0501  29  GLU A O   
154  C CB  . GLU A 27  ? 0.5250 0.6313 1.3130 -0.0322 -0.0209 0.0666  29  GLU A CB  
155  C CG  . GLU A 27  ? 0.6059 0.7128 1.4173 -0.0298 -0.0192 0.0689  29  GLU A CG  
156  C CD  . GLU A 27  ? 0.7093 0.8200 1.5586 -0.0297 -0.0299 0.0811  29  GLU A CD  
157  O OE1 . GLU A 27  ? 0.7295 0.8450 1.6117 -0.0295 -0.0230 0.0835  29  GLU A OE1 
158  O OE2 . GLU A 27  ? 0.7395 0.8487 1.5859 -0.0299 -0.0451 0.0888  29  GLU A OE2 
159  N N   . ASN A 28  ? 0.4097 0.5088 1.1154 -0.0362 -0.0280 0.0575  30  ASN A N   
160  C CA  . ASN A 28  ? 0.3907 0.4890 1.0828 -0.0385 -0.0303 0.0573  30  ASN A CA  
161  C C   . ASN A 28  ? 0.3664 0.4694 1.0936 -0.0399 -0.0300 0.0639  30  ASN A C   
162  O O   . ASN A 28  ? 0.3654 0.4706 1.0968 -0.0409 -0.0195 0.0617  30  ASN A O   
163  C CB  . ASN A 28  ? 0.3748 0.4716 1.0404 -0.0385 -0.0167 0.0475  30  ASN A CB  
164  C CG  . ASN A 28  ? 0.3893 0.4844 1.0382 -0.0408 -0.0219 0.0486  30  ASN A CG  
165  O OD1 . ASN A 28  ? 0.3936 0.4859 1.0362 -0.0420 -0.0376 0.0540  30  ASN A OD1 
166  N ND2 . ASN A 28  ? 0.3843 0.4801 1.0251 -0.0414 -0.0090 0.0436  30  ASN A ND2 
167  N N   . LEU A 29  ? 0.3430 0.4479 1.0967 -0.0401 -0.0418 0.0728  31  LEU A N   
168  C CA  . LEU A 29  ? 0.3278 0.4377 1.1190 -0.0417 -0.0439 0.0806  31  LEU A CA  
169  C C   . LEU A 29  ? 0.3288 0.4370 1.1088 -0.0450 -0.0517 0.0826  31  LEU A C   
170  O O   . LEU A 29  ? 0.3365 0.4387 1.0846 -0.0459 -0.0635 0.0813  31  LEU A O   
171  C CB  . LEU A 29  ? 0.3232 0.4347 1.1408 -0.0418 -0.0591 0.0907  31  LEU A CB  
172  C CG  . LEU A 29  ? 0.3480 0.4609 1.1810 -0.0387 -0.0542 0.0910  31  LEU A CG  
173  C CD1 . LEU A 29  ? 0.3549 0.4691 1.2126 -0.0393 -0.0719 0.1027  31  LEU A CD1 
174  C CD2 . LEU A 29  ? 0.3486 0.4664 1.2094 -0.0366 -0.0328 0.0866  31  LEU A CD2 
175  N N   . TYR A 30  ? 0.3165 0.4298 1.1235 -0.0465 -0.0444 0.0857  32  TYR A N   
176  C CA  . TYR A 30  ? 0.3142 0.4264 1.1170 -0.0498 -0.0500 0.0882  32  TYR A CA  
177  C C   . TYR A 30  ? 0.3242 0.4310 1.0849 -0.0501 -0.0456 0.0802  32  TYR A C   
178  O O   . TYR A 30  ? 0.3328 0.4368 1.0843 -0.0528 -0.0537 0.0822  32  TYR A O   
179  C CB  . TYR A 30  ? 0.3163 0.4258 1.1262 -0.0525 -0.0741 0.0967  32  TYR A CB  
180  C CG  . TYR A 30  ? 0.3145 0.4289 1.1636 -0.0522 -0.0809 0.1052  32  TYR A CG  
181  C CD1 . TYR A 30  ? 0.3158 0.4379 1.2094 -0.0533 -0.0757 0.1119  32  TYR A CD1 
182  C CD2 . TYR A 30  ? 0.3242 0.4360 1.1670 -0.0506 -0.0919 0.1072  32  TYR A CD2 
183  C CE1 . TYR A 30  ? 0.3110 0.4381 1.2430 -0.0528 -0.0820 0.1202  32  TYR A CE1 
184  C CE2 . TYR A 30  ? 0.3294 0.4457 1.2087 -0.0502 -0.0986 0.1158  32  TYR A CE2 
185  C CZ  . TYR A 30  ? 0.3257 0.4497 1.2502 -0.0513 -0.0940 0.1222  32  TYR A CZ  
186  O OH  . TYR A 30  ? 0.3424 0.4713 1.3057 -0.0508 -0.1006 0.1313  32  TYR A OH  
187  N N   . PHE A 31  ? 0.3331 0.4383 1.0695 -0.0475 -0.0334 0.0715  33  PHE A N   
188  C CA  . PHE A 31  ? 0.3569 0.4569 1.0521 -0.0476 -0.0316 0.0645  33  PHE A CA  
189  C C   . PHE A 31  ? 0.3687 0.4618 1.0377 -0.0485 -0.0510 0.0659  33  PHE A C   
190  O O   . PHE A 31  ? 0.3740 0.4626 1.0156 -0.0493 -0.0532 0.0627  33  PHE A O   
191  C CB  . PHE A 31  ? 0.3571 0.4589 1.0527 -0.0494 -0.0207 0.0638  33  PHE A CB  
192  C CG  . PHE A 31  ? 0.3585 0.4654 1.0680 -0.0477 0.0011  0.0598  33  PHE A CG  
193  C CD1 . PHE A 31  ? 0.3711 0.4763 1.0577 -0.0453 0.0129  0.0506  33  PHE A CD1 
194  C CD2 . PHE A 31  ? 0.3457 0.4588 1.0918 -0.0483 0.0097  0.0652  33  PHE A CD2 
195  C CE1 . PHE A 31  ? 0.3722 0.4806 1.0694 -0.0436 0.0326  0.0460  33  PHE A CE1 
196  C CE2 . PHE A 31  ? 0.3422 0.4592 1.0999 -0.0462 0.0308  0.0610  33  PHE A CE2 
197  C CZ  . PHE A 31  ? 0.3545 0.4687 1.0865 -0.0438 0.0421  0.0510  33  PHE A CZ  
198  N N   . GLN A 32  ? 0.3618 0.4537 1.0387 -0.0479 -0.0648 0.0706  34  GLN A N   
199  C CA  . GLN A 32  ? 0.3606 0.4456 1.0165 -0.0487 -0.0842 0.0731  34  GLN A CA  
200  C C   . GLN A 32  ? 0.3473 0.4293 0.9853 -0.0461 -0.0900 0.0721  34  GLN A C   
201  O O   . GLN A 32  ? 0.3544 0.4308 0.9771 -0.0464 -0.1059 0.0749  34  GLN A O   
202  C CB  . GLN A 32  ? 0.3667 0.4521 1.0494 -0.0515 -0.0995 0.0821  34  GLN A CB  
203  C CG  . GLN A 32  ? 0.3983 0.4838 1.0899 -0.0548 -0.0995 0.0837  34  GLN A CG  
204  C CD  . GLN A 32  ? 0.4524 0.5369 1.1677 -0.0580 -0.1175 0.0923  34  GLN A CD  
205  O OE1 . GLN A 32  ? 0.4692 0.5471 1.1697 -0.0585 -0.1357 0.0942  34  GLN A OE1 
206  N NE2 . GLN A 32  ? 0.4523 0.5434 1.2051 -0.0603 -0.1130 0.0979  34  GLN A NE2 
207  N N   . GLY A 33  ? 0.3378 0.4230 0.9768 -0.0437 -0.0773 0.0680  35  GLY A N   
208  C CA  . GLY A 33  ? 0.3399 0.4234 0.9678 -0.0414 -0.0812 0.0681  35  GLY A CA  
209  C C   . GLY A 33  ? 0.3532 0.4335 0.9459 -0.0396 -0.0754 0.0605  35  GLY A C   
210  O O   . GLY A 33  ? 0.3750 0.4532 0.9546 -0.0378 -0.0798 0.0611  35  GLY A O   
211  N N   . LYS A 34  ? 0.3322 0.4123 0.9099 -0.0401 -0.0653 0.0539  36  LYS A N   
212  C CA  . LYS A 34  ? 0.3171 0.3943 0.8617 -0.0386 -0.0610 0.0471  36  LYS A CA  
213  C C   . LYS A 34  ? 0.3016 0.3726 0.8201 -0.0386 -0.0742 0.0485  36  LYS A C   
214  O O   . LYS A 34  ? 0.2915 0.3600 0.8151 -0.0404 -0.0836 0.0523  36  LYS A O   
215  C CB  . LYS A 34  ? 0.3088 0.3879 0.8470 -0.0392 -0.0463 0.0402  36  LYS A CB  
216  C CG  . LYS A 34  ? 0.2990 0.3824 0.8529 -0.0385 -0.0315 0.0360  36  LYS A CG  
217  C CD  . LYS A 34  ? 0.3105 0.3951 0.8571 -0.0393 -0.0176 0.0298  36  LYS A CD  
218  C CE  . LYS A 34  ? 0.3152 0.4021 0.8705 -0.0382 -0.0029 0.0235  36  LYS A CE  
219  N NZ  . LYS A 34  ? 0.3051 0.3925 0.8503 -0.0390 0.0107  0.0174  36  LYS A NZ  
220  N N   . HIS A 35  ? 0.2905 0.3586 0.7818 -0.0365 -0.0748 0.0451  37  HIS A N   
221  C CA  . HIS A 35  ? 0.2969 0.3585 0.7622 -0.0356 -0.0863 0.0460  37  HIS A CA  
222  C C   . HIS A 35  ? 0.2887 0.3482 0.7344 -0.0359 -0.0820 0.0408  37  HIS A C   
223  O O   . HIS A 35  ? 0.2844 0.3457 0.7176 -0.0348 -0.0723 0.0356  37  HIS A O   
224  C CB  . HIS A 35  ? 0.3165 0.3768 0.7654 -0.0327 -0.0886 0.0463  37  HIS A CB  
225  C CG  . HIS A 35  ? 0.3504 0.4120 0.8174 -0.0324 -0.0948 0.0530  37  HIS A CG  
226  N ND1 . HIS A 35  ? 0.3622 0.4293 0.8496 -0.0321 -0.0864 0.0533  37  HIS A ND1 
227  C CD2 . HIS A 35  ? 0.3617 0.4194 0.8288 -0.0324 -0.1090 0.0595  37  HIS A CD2 
228  C CE1 . HIS A 35  ? 0.3716 0.4384 0.8721 -0.0319 -0.0954 0.0606  37  HIS A CE1 
229  N NE2 . HIS A 35  ? 0.3706 0.4320 0.8589 -0.0321 -0.1095 0.0647  37  HIS A NE2 
230  N N   . PRO A 36  ? 0.2890 0.3443 0.7326 -0.0375 -0.0893 0.0422  38  PRO A N   
231  C CA  . PRO A 36  ? 0.2793 0.3326 0.7073 -0.0380 -0.0846 0.0381  38  PRO A CA  
232  C C   . PRO A 36  ? 0.2734 0.3221 0.6701 -0.0352 -0.0867 0.0345  38  PRO A C   
233  O O   . PRO A 36  ? 0.2806 0.3247 0.6652 -0.0333 -0.0960 0.0361  38  PRO A O   
234  C CB  . PRO A 36  ? 0.2976 0.3468 0.7341 -0.0406 -0.0942 0.0416  38  PRO A CB  
235  C CG  . PRO A 36  ? 0.3122 0.3579 0.7539 -0.0404 -0.1083 0.0463  38  PRO A CG  
236  C CD  . PRO A 36  ? 0.2870 0.3388 0.7432 -0.0393 -0.1030 0.0480  38  PRO A CD  
237  N N   . LEU A 37  ? 0.2627 0.3128 0.6468 -0.0349 -0.0778 0.0300  39  LEU A N   
238  C CA  . LEU A 37  ? 0.2522 0.2981 0.6085 -0.0323 -0.0794 0.0270  39  LEU A CA  
239  C C   . LEU A 37  ? 0.2497 0.2885 0.5960 -0.0327 -0.0871 0.0273  39  LEU A C   
240  O O   . LEU A 37  ? 0.2472 0.2858 0.6068 -0.0356 -0.0875 0.0290  39  LEU A O   
241  C CB  . LEU A 37  ? 0.2258 0.2765 0.5737 -0.0318 -0.0673 0.0223  39  LEU A CB  
242  C CG  . LEU A 37  ? 0.2055 0.2621 0.5613 -0.0312 -0.0601 0.0208  39  LEU A CG  
243  C CD1 . LEU A 37  ? 0.2143 0.2747 0.5619 -0.0314 -0.0497 0.0157  39  LEU A CD1 
244  C CD2 . LEU A 37  ? 0.2141 0.2692 0.5620 -0.0284 -0.0659 0.0226  39  LEU A CD2 
245  N N   . GLN A 38  ? 0.2629 0.2955 0.5864 -0.0298 -0.0928 0.0258  40  GLN A N   
246  C CA  . GLN A 38  ? 0.2595 0.2842 0.5711 -0.0296 -0.0991 0.0250  40  GLN A CA  
247  C C   . GLN A 38  ? 0.2756 0.3028 0.5880 -0.0314 -0.0911 0.0236  40  GLN A C   
248  O O   . GLN A 38  ? 0.2865 0.3096 0.6034 -0.0335 -0.0949 0.0249  40  GLN A O   
249  C CB  . GLN A 38  ? 0.2532 0.2717 0.5389 -0.0252 -0.1035 0.0227  40  GLN A CB  
250  C CG  . GLN A 38  ? 0.2622 0.2711 0.5340 -0.0242 -0.1099 0.0210  40  GLN A CG  
251  C CD  . GLN A 38  ? 0.3286 0.3295 0.6059 -0.0261 -0.1224 0.0227  40  GLN A CD  
252  O OE1 . GLN A 38  ? 0.3409 0.3425 0.6293 -0.0274 -0.1280 0.0255  40  GLN A OE1 
253  N NE2 . GLN A 38  ? 0.3784 0.3708 0.6486 -0.0263 -0.1278 0.0211  40  GLN A NE2 
254  N N   . ASN A 39  ? 0.2772 0.3109 0.5852 -0.0307 -0.0805 0.0212  41  ASN A N   
255  C CA  . ASN A 39  ? 0.2628 0.2993 0.5675 -0.0320 -0.0722 0.0198  41  ASN A CA  
256  C C   . ASN A 39  ? 0.2162 0.2609 0.5339 -0.0341 -0.0611 0.0189  41  ASN A C   
257  O O   . ASN A 39  ? 0.2012 0.2498 0.5255 -0.0336 -0.0586 0.0180  41  ASN A O   
258  C CB  . ASN A 39  ? 0.2921 0.3276 0.5749 -0.0287 -0.0707 0.0170  41  ASN A CB  
259  C CG  . ASN A 39  ? 0.3582 0.3848 0.6268 -0.0262 -0.0795 0.0170  41  ASN A CG  
260  O OD1 . ASN A 39  ? 0.4289 0.4521 0.6863 -0.0228 -0.0841 0.0161  41  ASN A OD1 
261  N ND2 . ASN A 39  ? 0.3245 0.3463 0.5922 -0.0274 -0.0822 0.0180  41  ASN A ND2 
262  N N   . ARG A 40  ? 0.2036 0.2503 0.5245 -0.0365 -0.0543 0.0192  42  ARG A N   
263  C CA  . ARG A 40  ? 0.1973 0.2506 0.5222 -0.0380 -0.0422 0.0169  42  ARG A CA  
264  C C   . ARG A 40  ? 0.1943 0.2487 0.4985 -0.0364 -0.0388 0.0132  42  ARG A C   
265  O O   . ARG A 40  ? 0.2072 0.2580 0.4965 -0.0351 -0.0430 0.0137  42  ARG A O   
266  C CB  . ARG A 40  ? 0.2297 0.2842 0.5652 -0.0411 -0.0362 0.0194  42  ARG A CB  
267  C CG  . ARG A 40  ? 0.2920 0.3525 0.6329 -0.0426 -0.0229 0.0169  42  ARG A CG  
268  C CD  . ARG A 40  ? 0.3693 0.4317 0.7320 -0.0453 -0.0175 0.0209  42  ARG A CD  
269  N NE  . ARG A 40  ? 0.4577 0.5250 0.8248 -0.0464 -0.0033 0.0184  42  ARG A NE  
270  C CZ  . ARG A 40  ? 0.5379 0.6088 0.9188 -0.0461 0.0037  0.0156  42  ARG A CZ  
271  N NH1 . ARG A 40  ? 0.5382 0.6093 0.9317 -0.0449 -0.0026 0.0158  42  ARG A NH1 
272  N NH2 . ARG A 40  ? 0.5748 0.6486 0.9564 -0.0469 0.0171  0.0125  42  ARG A NH2 
273  N N   . TRP A 41  ? 0.1776 0.2369 0.4822 -0.0365 -0.0315 0.0094  43  TRP A N   
274  C CA  . TRP A 41  ? 0.1857 0.2468 0.4740 -0.0352 -0.0294 0.0058  43  TRP A CA  
275  C C   . TRP A 41  ? 0.2107 0.2755 0.4982 -0.0375 -0.0193 0.0024  43  TRP A C   
276  O O   . TRP A 41  ? 0.1993 0.2662 0.5015 -0.0391 -0.0128 0.0013  43  TRP A O   
277  C CB  . TRP A 41  ? 0.1759 0.2385 0.4649 -0.0330 -0.0319 0.0041  43  TRP A CB  
278  C CG  . TRP A 41  ? 0.1721 0.2306 0.4586 -0.0303 -0.0413 0.0073  43  TRP A CG  
279  C CD1 . TRP A 41  ? 0.1700 0.2262 0.4686 -0.0302 -0.0466 0.0103  43  TRP A CD1 
280  C CD2 . TRP A 41  ? 0.1706 0.2260 0.4405 -0.0273 -0.0469 0.0079  43  TRP A CD2 
281  N NE1 . TRP A 41  ? 0.1723 0.2233 0.4605 -0.0275 -0.0554 0.0122  43  TRP A NE1 
282  C CE2 . TRP A 41  ? 0.1800 0.2305 0.4508 -0.0253 -0.0549 0.0105  43  TRP A CE2 
283  C CE3 . TRP A 41  ? 0.1726 0.2287 0.4274 -0.0259 -0.0459 0.0065  43  TRP A CE3 
284  C CZ2 . TRP A 41  ? 0.1950 0.2408 0.4507 -0.0217 -0.0607 0.0112  43  TRP A CZ2 
285  C CZ3 . TRP A 41  ? 0.1940 0.2464 0.4370 -0.0223 -0.0515 0.0077  43  TRP A CZ3 
286  C CH2 . TRP A 41  ? 0.1980 0.2450 0.4408 -0.0200 -0.0583 0.0097  43  TRP A CH2 
287  N N   . ALA A 42  ? 0.2093 0.2747 0.4796 -0.0375 -0.0179 0.0005  44  ALA A N   
288  C CA  . ALA A 42  ? 0.2072 0.2750 0.4712 -0.0397 -0.0094 -0.0033 44  ALA A CA  
289  C C   . ALA A 42  ? 0.2260 0.2958 0.4797 -0.0390 -0.0101 -0.0078 44  ALA A C   
290  O O   . ALA A 42  ? 0.2348 0.3043 0.4788 -0.0371 -0.0165 -0.0064 44  ALA A O   
291  C CB  . ALA A 42  ? 0.2238 0.2901 0.4766 -0.0410 -0.0080 -0.0004 44  ALA A CB  
292  N N   . LEU A 43  ? 0.2242 0.2960 0.4814 -0.0405 -0.0033 -0.0133 45  LEU A N   
293  C CA  . LEU A 43  ? 0.2246 0.2981 0.4736 -0.0408 -0.0036 -0.0182 45  LEU A CA  
294  C C   . LEU A 43  ? 0.2313 0.3046 0.4634 -0.0430 0.0000  -0.0209 45  LEU A C   
295  O O   . LEU A 43  ? 0.2391 0.3115 0.4711 -0.0449 0.0078  -0.0229 45  LEU A O   
296  C CB  . LEU A 43  ? 0.2131 0.2875 0.4756 -0.0414 0.0012  -0.0231 45  LEU A CB  
297  C CG  . LEU A 43  ? 0.2163 0.2919 0.4728 -0.0423 0.0011  -0.0290 45  LEU A CG  
298  C CD1 . LEU A 43  ? 0.2014 0.2788 0.4523 -0.0405 -0.0074 -0.0260 45  LEU A CD1 
299  C CD2 . LEU A 43  ? 0.2242 0.2996 0.4968 -0.0429 0.0065  -0.0339 45  LEU A CD2 
300  N N   . TRP A 44  ? 0.2271 0.3014 0.4453 -0.0428 -0.0056 -0.0208 46  TRP A N   
301  C CA  . TRP A 44  ? 0.2476 0.3218 0.4478 -0.0449 -0.0046 -0.0228 46  TRP A CA  
302  C C   . TRP A 44  ? 0.2785 0.3543 0.4736 -0.0461 -0.0069 -0.0285 46  TRP A C   
303  O O   . TRP A 44  ? 0.2462 0.3240 0.4496 -0.0445 -0.0115 -0.0284 46  TRP A O   
304  C CB  . TRP A 44  ? 0.2444 0.3184 0.4339 -0.0437 -0.0111 -0.0165 46  TRP A CB  
305  C CG  . TRP A 44  ? 0.2434 0.3151 0.4382 -0.0426 -0.0110 -0.0105 46  TRP A CG  
306  C CD1 . TRP A 44  ? 0.2452 0.3157 0.4517 -0.0401 -0.0149 -0.0071 46  TRP A CD1 
307  C CD2 . TRP A 44  ? 0.2638 0.3337 0.4523 -0.0443 -0.0069 -0.0072 46  TRP A CD2 
308  N NE1 . TRP A 44  ? 0.2586 0.3264 0.4671 -0.0403 -0.0145 -0.0022 46  TRP A NE1 
309  C CE2 . TRP A 44  ? 0.2648 0.3326 0.4634 -0.0428 -0.0093 -0.0017 46  TRP A CE2 
310  C CE3 . TRP A 44  ? 0.2864 0.3560 0.4606 -0.0469 -0.0020 -0.0079 46  TRP A CE3 
311  C CZ2 . TRP A 44  ? 0.2874 0.3532 0.4852 -0.0441 -0.0065 0.0032  46  TRP A CZ2 
312  C CZ3 . TRP A 44  ? 0.3050 0.3730 0.4770 -0.0479 0.0015  -0.0026 46  TRP A CZ3 
313  C CH2 . TRP A 44  ? 0.3038 0.3700 0.4884 -0.0466 -0.0009 0.0032  46  TRP A CH2 
314  N N   . PHE A 45  ? 0.3305 0.4051 0.5114 -0.0490 -0.0037 -0.0333 47  PHE A N   
315  C CA  . PHE A 45  ? 0.3719 0.4473 0.5444 -0.0510 -0.0072 -0.0389 47  PHE A CA  
316  C C   . PHE A 45  ? 0.3862 0.4616 0.5383 -0.0525 -0.0116 -0.0366 47  PHE A C   
317  O O   . PHE A 45  ? 0.3757 0.4491 0.5172 -0.0534 -0.0076 -0.0341 47  PHE A O   
318  C CB  . PHE A 45  ? 0.4091 0.4814 0.5818 -0.0534 0.0007  -0.0480 47  PHE A CB  
319  C CG  . PHE A 45  ? 0.4641 0.5355 0.6273 -0.0562 -0.0028 -0.0552 47  PHE A CG  
320  C CD1 . PHE A 45  ? 0.4942 0.5680 0.6685 -0.0560 -0.0089 -0.0566 47  PHE A CD1 
321  C CD2 . PHE A 45  ? 0.4988 0.5666 0.6417 -0.0592 0.0000  -0.0605 47  PHE A CD2 
322  C CE1 . PHE A 45  ? 0.5121 0.5848 0.6793 -0.0590 -0.0131 -0.0632 47  PHE A CE1 
323  C CE2 . PHE A 45  ? 0.5251 0.5912 0.6585 -0.0621 -0.0047 -0.0676 47  PHE A CE2 
324  C CZ  . PHE A 45  ? 0.5193 0.5880 0.6659 -0.0621 -0.0116 -0.0690 47  PHE A CZ  
325  N N   . PHE A 46  ? 0.4184 0.4963 0.5664 -0.0530 -0.0197 -0.0367 48  PHE A N   
326  C CA  . PHE A 46  ? 0.4664 0.5447 0.5961 -0.0546 -0.0253 -0.0343 48  PHE A CA  
327  C C   . PHE A 46  ? 0.5077 0.5867 0.6329 -0.0575 -0.0306 -0.0406 48  PHE A C   
328  O O   . PHE A 46  ? 0.4895 0.5720 0.6273 -0.0565 -0.0360 -0.0404 48  PHE A O   
329  C CB  . PHE A 46  ? 0.4675 0.5484 0.5997 -0.0515 -0.0316 -0.0250 48  PHE A CB  
330  C CG  . PHE A 46  ? 0.5066 0.5892 0.6254 -0.0522 -0.0393 -0.0206 48  PHE A CG  
331  C CD1 . PHE A 46  ? 0.5373 0.6176 0.6415 -0.0531 -0.0383 -0.0162 48  PHE A CD1 
332  C CD2 . PHE A 46  ? 0.5327 0.6193 0.6550 -0.0518 -0.0477 -0.0198 48  PHE A CD2 
333  C CE1 . PHE A 46  ? 0.5611 0.6430 0.6539 -0.0537 -0.0461 -0.0112 48  PHE A CE1 
334  C CE2 . PHE A 46  ? 0.5479 0.6365 0.6603 -0.0523 -0.0555 -0.0148 48  PHE A CE2 
335  C CZ  . PHE A 46  ? 0.5570 0.6431 0.6544 -0.0532 -0.0549 -0.0106 48  PHE A CZ  
336  N N   . LYS A 47  ? 0.5602 0.6355 0.6672 -0.0612 -0.0288 -0.0466 49  LYS A N   
337  C CA  . LYS A 47  ? 0.6246 0.6990 0.7232 -0.0648 -0.0349 -0.0535 49  LYS A CA  
338  C C   . LYS A 47  ? 0.6731 0.7500 0.7578 -0.0663 -0.0457 -0.0485 49  LYS A C   
339  O O   . LYS A 47  ? 0.6714 0.7500 0.7512 -0.0644 -0.0473 -0.0400 49  LYS A O   
340  C CB  . LYS A 47  ? 0.6755 0.7431 0.7593 -0.0679 -0.0268 -0.0633 49  LYS A CB  
341  C CG  . LYS A 47  ? 0.7514 0.8158 0.8268 -0.0720 -0.0322 -0.0731 49  LYS A CG  
342  C CD  . LYS A 47  ? 0.8130 0.8692 0.8722 -0.0744 -0.0228 -0.0838 49  LYS A CD  
343  C CE  . LYS A 47  ? 0.8614 0.9129 0.9017 -0.0791 -0.0302 -0.0925 49  LYS A CE  
344  N NZ  . LYS A 47  ? 0.8852 0.9278 0.9151 -0.0809 -0.0206 -0.1053 49  LYS A NZ  
345  N N   . ASN A 48  ? 0.7200 0.7970 0.7997 -0.0696 -0.0538 -0.0535 50  ASN A N   
346  C CA  . ASN A 48  ? 0.7700 0.8477 0.8315 -0.0723 -0.0638 -0.0505 50  ASN A CA  
347  C C   . ASN A 48  ? 0.8105 0.8810 0.8477 -0.0770 -0.0622 -0.0600 50  ASN A C   
348  O O   . ASN A 48  ? 0.8138 0.8804 0.8541 -0.0790 -0.0598 -0.0703 50  ASN A O   
349  C CB  . ASN A 48  ? 0.7984 0.8821 0.8732 -0.0728 -0.0762 -0.0482 50  ASN A CB  
350  C CG  . ASN A 48  ? 0.8649 0.9537 0.9364 -0.0718 -0.0858 -0.0378 50  ASN A CG  
351  O OD1 . ASN A 48  ? 0.8869 0.9774 0.9603 -0.0680 -0.0831 -0.0294 50  ASN A OD1 
352  N ND2 . ASN A 48  ? 0.8742 0.9653 0.9418 -0.0751 -0.0979 -0.0381 50  ASN A ND2 
353  N N   . ASP A 49  ? 0.8339 0.9020 0.8463 -0.0786 -0.0636 -0.0565 51  ASP A N   
354  C CA  . ASP A 49  ? 0.8595 0.9199 0.8442 -0.0827 -0.0613 -0.0649 51  ASP A CA  
355  C C   . ASP A 49  ? 0.8827 0.9428 0.8441 -0.0861 -0.0736 -0.0612 51  ASP A C   
356  O O   . ASP A 49  ? 0.8826 0.9492 0.8530 -0.0852 -0.0844 -0.0522 51  ASP A O   
357  C CB  . ASP A 49  ? 0.8857 0.9418 0.8608 -0.0811 -0.0462 -0.0649 51  ASP A CB  
358  C CG  . ASP A 49  ? 0.9525 1.0004 0.9157 -0.0830 -0.0360 -0.0778 51  ASP A CG  
359  O OD1 . ASP A 49  ? 0.9651 1.0072 0.9028 -0.0869 -0.0396 -0.0844 51  ASP A OD1 
360  O OD2 . ASP A 49  ? 0.9811 1.0281 0.9604 -0.0806 -0.0245 -0.0812 51  ASP A OD2 
361  N N   . LYS A 50  ? 0.9000 0.9524 0.8313 -0.0898 -0.0720 -0.0681 52  LYS A N   
362  C CA  . LYS A 50  ? 0.9183 0.9689 0.8226 -0.0935 -0.0833 -0.0653 52  LYS A CA  
363  C C   . LYS A 50  ? 0.9138 0.9671 0.8099 -0.0912 -0.0809 -0.0519 52  LYS A C   
364  O O   . LYS A 50  ? 0.9213 0.9694 0.7930 -0.0920 -0.0731 -0.0513 52  LYS A O   
365  C CB  . LYS A 50  ? 0.9689 1.0088 0.8420 -0.0977 -0.0798 -0.0780 52  LYS A CB  
366  C CG  . LYS A 50  ? 1.0311 1.0677 0.8724 -0.1023 -0.0926 -0.0765 52  LYS A CG  
367  C CD  . LYS A 50  ? 1.1005 1.1252 0.9066 -0.1058 -0.0873 -0.0888 52  LYS A CD  
368  C CE  . LYS A 50  ? 1.1545 1.1738 0.9538 -0.1108 -0.0998 -0.1013 52  LYS A CE  
369  N NZ  . LYS A 50  ? 1.1918 1.2116 0.9710 -0.1151 -0.1187 -0.0964 52  LYS A NZ  
370  N N   . SER A 51  ? 0.9000 0.9614 0.8176 -0.0882 -0.0875 -0.0409 53  SER A N   
371  C CA  . SER A 51  ? 0.8965 0.9615 0.8195 -0.0845 -0.0839 -0.0280 53  SER A CA  
372  C C   . SER A 51  ? 0.8953 0.9557 0.8075 -0.0833 -0.0682 -0.0274 53  SER A C   
373  O O   . SER A 51  ? 0.9100 0.9670 0.7979 -0.0849 -0.0661 -0.0229 53  SER A O   
374  C CB  . SER A 51  ? 0.9162 0.9841 0.8278 -0.0857 -0.0970 -0.0174 53  SER A CB  
375  O OG  . SER A 51  ? 0.9342 1.0078 0.8640 -0.0815 -0.0991 -0.0051 53  SER A OG  
376  N N   . LYS A 52  ? 0.8729 0.9333 0.8040 -0.0807 -0.0571 -0.0317 54  LYS A N   
377  C CA  . LYS A 52  ? 0.8663 0.9259 0.8013 -0.0780 -0.0444 -0.0265 54  LYS A CA  
378  C C   . LYS A 52  ? 0.8586 0.9239 0.8122 -0.0745 -0.0500 -0.0142 54  LYS A C   
379  O O   . LYS A 52  ? 0.8523 0.9224 0.8231 -0.0729 -0.0593 -0.0127 54  LYS A O   
380  C CB  . LYS A 52  ? 0.8819 0.9396 0.8322 -0.0765 -0.0320 -0.0352 54  LYS A CB  
381  C CG  . LYS A 52  ? 0.9362 0.9870 0.8683 -0.0795 -0.0247 -0.0477 54  LYS A CG  
382  C CD  . LYS A 52  ? 0.9772 1.0269 0.9295 -0.0776 -0.0137 -0.0559 54  LYS A CD  
383  C CE  . LYS A 52  ? 1.0360 1.0780 0.9712 -0.0797 -0.0038 -0.0682 54  LYS A CE  
384  N NZ  . LYS A 52  ? 1.0623 1.1034 1.0203 -0.0778 0.0052  -0.0762 54  LYS A NZ  
385  N N   . THR A 53  ? 0.8553 0.9199 0.8054 -0.0731 -0.0441 -0.0053 55  THR A N   
386  C CA  . THR A 53  ? 0.8505 0.9188 0.8185 -0.0695 -0.0479 0.0055  55  THR A CA  
387  C C   . THR A 53  ? 0.8274 0.8980 0.8238 -0.0659 -0.0443 0.0023  55  THR A C   
388  O O   . THR A 53  ? 0.8265 0.8956 0.8286 -0.0663 -0.0365 -0.0065 55  THR A O   
389  C CB  . THR A 53  ? 0.8844 0.9504 0.8423 -0.0694 -0.0417 0.0153  55  THR A CB  
390  O OG1 . THR A 53  ? 0.8939 0.9623 0.8658 -0.0664 -0.0477 0.0259  55  THR A OG1 
391  C CG2 . THR A 53  ? 0.8972 0.9603 0.8595 -0.0690 -0.0263 0.0124  55  THR A CG2 
392  N N   . TRP A 54  ? 0.8042 0.8780 0.8179 -0.0623 -0.0499 0.0094  56  TRP A N   
393  C CA  . TRP A 54  ? 0.7788 0.8545 0.8170 -0.0588 -0.0482 0.0071  56  TRP A CA  
394  C C   . TRP A 54  ? 0.7441 0.8169 0.7894 -0.0583 -0.0360 0.0041  56  TRP A C   
395  O O   . TRP A 54  ? 0.7375 0.8107 0.7961 -0.0575 -0.0322 -0.0025 56  TRP A O   
396  C CB  . TRP A 54  ? 0.7858 0.8635 0.8371 -0.0547 -0.0546 0.0159  56  TRP A CB  
397  C CG  . TRP A 54  ? 0.8142 0.8959 0.8652 -0.0541 -0.0663 0.0193  56  TRP A CG  
398  C CD1 . TRP A 54  ? 0.8368 0.9190 0.8769 -0.0548 -0.0735 0.0270  56  TRP A CD1 
399  C CD2 . TRP A 54  ? 0.8217 0.9078 0.8853 -0.0527 -0.0721 0.0157  56  TRP A CD2 
400  N NE1 . TRP A 54  ? 0.8412 0.9282 0.8876 -0.0539 -0.0837 0.0284  56  TRP A NE1 
401  C CE2 . TRP A 54  ? 0.8349 0.9245 0.8962 -0.0526 -0.0826 0.0215  56  TRP A CE2 
402  C CE3 . TRP A 54  ? 0.8258 0.9135 0.9040 -0.0516 -0.0693 0.0089  56  TRP A CE3 
403  C CZ2 . TRP A 54  ? 0.8412 0.9362 0.9150 -0.0513 -0.0899 0.0206  56  TRP A CZ2 
404  C CZ3 . TRP A 54  ? 0.8331 0.9257 0.9221 -0.0505 -0.0762 0.0081  56  TRP A CZ3 
405  C CH2 . TRP A 54  ? 0.8367 0.9331 0.9241 -0.0504 -0.0862 0.0138  56  TRP A CH2 
406  N N   . GLN A 55  ? 0.7137 0.7838 0.7515 -0.0590 -0.0301 0.0100  57  GLN A N   
407  C CA  . GLN A 55  ? 0.6754 0.7432 0.7205 -0.0589 -0.0184 0.0087  57  GLN A CA  
408  C C   . GLN A 55  ? 0.6262 0.6925 0.6647 -0.0613 -0.0098 -0.0015 57  GLN A C   
409  O O   . GLN A 55  ? 0.6221 0.6880 0.6755 -0.0603 -0.0025 -0.0057 57  GLN A O   
410  C CB  . GLN A 55  ? 0.7157 0.7813 0.7534 -0.0596 -0.0141 0.0180  57  GLN A CB  
411  C CG  . GLN A 55  ? 0.7672 0.8330 0.8151 -0.0569 -0.0215 0.0278  57  GLN A CG  
412  C CD  . GLN A 55  ? 0.8094 0.8728 0.8673 -0.0564 -0.0150 0.0345  57  GLN A CD  
413  O OE1 . GLN A 55  ? 0.8050 0.8679 0.8785 -0.0557 -0.0087 0.0315  57  GLN A OE1 
414  N NE2 . GLN A 55  ? 0.8212 0.8830 0.8719 -0.0569 -0.0171 0.0444  57  GLN A NE2 
415  N N   . ALA A 56  ? 0.5959 0.6606 0.6124 -0.0643 -0.0110 -0.0055 58  ALA A N   
416  C CA  . ALA A 56  ? 0.5775 0.6392 0.5851 -0.0664 -0.0025 -0.0161 58  ALA A CA  
417  C C   . ALA A 56  ? 0.5357 0.5986 0.5584 -0.0658 -0.0049 -0.0254 58  ALA A C   
418  O O   . ALA A 56  ? 0.5389 0.5993 0.5647 -0.0663 0.0040  -0.0336 58  ALA A O   
419  C CB  . ALA A 56  ? 0.5850 0.6437 0.5625 -0.0699 -0.0047 -0.0183 58  ALA A CB  
420  N N   . ASN A 57  ? 0.4982 0.5648 0.5312 -0.0645 -0.0163 -0.0237 59  ASN A N   
421  C CA  . ASN A 57  ? 0.4762 0.5445 0.5257 -0.0637 -0.0188 -0.0307 59  ASN A CA  
422  C C   . ASN A 57  ? 0.4368 0.5067 0.5113 -0.0603 -0.0144 -0.0291 59  ASN A C   
423  O O   . ASN A 57  ? 0.4251 0.4954 0.5127 -0.0599 -0.0133 -0.0353 59  ASN A O   
424  C CB  . ASN A 57  ? 0.5001 0.5722 0.5509 -0.0638 -0.0321 -0.0290 59  ASN A CB  
425  C CG  . ASN A 57  ? 0.5307 0.6011 0.5598 -0.0678 -0.0382 -0.0331 59  ASN A CG  
426  O OD1 . ASN A 57  ? 0.5440 0.6096 0.5588 -0.0707 -0.0325 -0.0414 59  ASN A OD1 
427  N ND2 . ASN A 57  ? 0.5227 0.5965 0.5488 -0.0681 -0.0499 -0.0276 59  ASN A ND2 
428  N N   . LEU A 58  ? 0.4184 0.4887 0.4995 -0.0581 -0.0126 -0.0209 60  LEU A N   
429  C CA  . LEU A 58  ? 0.3963 0.4676 0.4993 -0.0551 -0.0102 -0.0190 60  LEU A CA  
430  C C   . LEU A 58  ? 0.4078 0.4767 0.5164 -0.0558 0.0016  -0.0216 60  LEU A C   
431  O O   . LEU A 58  ? 0.4147 0.4818 0.5139 -0.0570 0.0079  -0.0184 60  LEU A O   
432  C CB  . LEU A 58  ? 0.3987 0.4709 0.5070 -0.0524 -0.0161 -0.0094 60  LEU A CB  
433  C CG  . LEU A 58  ? 0.4176 0.4899 0.5465 -0.0491 -0.0163 -0.0069 60  LEU A CG  
434  C CD1 . LEU A 58  ? 0.4253 0.4999 0.5669 -0.0475 -0.0194 -0.0117 60  LEU A CD1 
435  C CD2 . LEU A 58  ? 0.4183 0.4899 0.5486 -0.0465 -0.0228 0.0016  60  LEU A CD2 
436  N N   . ARG A 59  ? 0.4090 0.4782 0.5341 -0.0549 0.0052  -0.0269 61  ARG A N   
437  C CA  . ARG A 59  ? 0.3952 0.4626 0.5291 -0.0552 0.0167  -0.0306 61  ARG A CA  
438  C C   . ARG A 59  ? 0.3723 0.4412 0.5308 -0.0527 0.0164  -0.0280 61  ARG A C   
439  O O   . ARG A 59  ? 0.3577 0.4283 0.5257 -0.0511 0.0097  -0.0287 61  ARG A O   
440  C CB  . ARG A 59  ? 0.4197 0.4851 0.5496 -0.0570 0.0216  -0.0412 61  ARG A CB  
441  C CG  . ARG A 59  ? 0.5268 0.5902 0.6316 -0.0597 0.0187  -0.0454 61  ARG A CG  
442  C CD  . ARG A 59  ? 0.6229 0.6822 0.7098 -0.0617 0.0296  -0.0487 61  ARG A CD  
443  N NE  . ARG A 59  ? 0.6807 0.7381 0.7401 -0.0643 0.0246  -0.0491 61  ARG A NE  
444  C CZ  . ARG A 59  ? 0.7242 0.7796 0.7706 -0.0665 0.0188  -0.0567 61  ARG A CZ  
445  N NH1 . ARG A 59  ? 0.7198 0.7746 0.7789 -0.0665 0.0177  -0.0650 61  ARG A NH1 
446  N NH2 . ARG A 59  ? 0.7519 0.8057 0.7731 -0.0690 0.0134  -0.0558 61  ARG A NH2 
447  N N   . LEU A 60  ? 0.3644 0.4327 0.5331 -0.0524 0.0236  -0.0247 62  LEU A N   
448  C CA  . LEU A 60  ? 0.3527 0.4219 0.5450 -0.0505 0.0237  -0.0226 62  LEU A CA  
449  C C   . LEU A 60  ? 0.3717 0.4406 0.5749 -0.0508 0.0319  -0.0300 62  LEU A C   
450  O O   . LEU A 60  ? 0.3914 0.4587 0.5883 -0.0523 0.0420  -0.0336 62  LEU A O   
451  C CB  . LEU A 60  ? 0.3257 0.3945 0.5256 -0.0504 0.0270  -0.0152 62  LEU A CB  
452  C CG  . LEU A 60  ? 0.3153 0.3848 0.5401 -0.0491 0.0276  -0.0129 62  LEU A CG  
453  C CD1 . LEU A 60  ? 0.3063 0.3758 0.5371 -0.0469 0.0158  -0.0097 62  LEU A CD1 
454  C CD2 . LEU A 60  ? 0.3276 0.3968 0.5610 -0.0501 0.0339  -0.0068 62  LEU A CD2 
455  N N   . ILE A 61  ? 0.3654 0.4353 0.5850 -0.0493 0.0281  -0.0317 63  ILE A N   
456  C CA  . ILE A 61  ? 0.3701 0.4395 0.6031 -0.0492 0.0346  -0.0383 63  ILE A CA  
457  C C   . ILE A 61  ? 0.3674 0.4378 0.6238 -0.0481 0.0391  -0.0345 63  ILE A C   
458  O O   . ILE A 61  ? 0.3863 0.4559 0.6513 -0.0484 0.0496  -0.0380 63  ILE A O   
459  C CB  . ILE A 61  ? 0.3843 0.4546 0.6220 -0.0485 0.0276  -0.0420 63  ILE A CB  
460  C CG1 . ILE A 61  ? 0.4022 0.4722 0.6192 -0.0500 0.0221  -0.0456 63  ILE A CG1 
461  C CG2 . ILE A 61  ? 0.3869 0.4561 0.6412 -0.0484 0.0343  -0.0483 63  ILE A CG2 
462  C CD1 . ILE A 61  ? 0.4282 0.4956 0.6242 -0.0525 0.0274  -0.0498 63  ILE A CD1 
463  N N   . SER A 62  ? 0.3458 0.4175 0.6129 -0.0466 0.0312  -0.0276 64  SER A N   
464  C CA  . SER A 62  ? 0.3216 0.3943 0.6128 -0.0456 0.0326  -0.0239 64  SER A CA  
465  C C   . SER A 62  ? 0.3084 0.3811 0.6043 -0.0444 0.0222  -0.0161 64  SER A C   
466  O O   . SER A 62  ? 0.3097 0.3818 0.5930 -0.0434 0.0136  -0.0148 64  SER A O   
467  C CB  . SER A 62  ? 0.3343 0.4074 0.6410 -0.0446 0.0335  -0.0283 64  SER A CB  
468  O OG  . SER A 62  ? 0.3932 0.4672 0.7236 -0.0442 0.0392  -0.0266 64  SER A OG  
469  N N   . LYS A 63  ? 0.2795 0.3525 0.5937 -0.0443 0.0227  -0.0111 65  LYS A N   
470  C CA  . LYS A 63  ? 0.2641 0.3361 0.5849 -0.0433 0.0121  -0.0047 65  LYS A CA  
471  C C   . LYS A 63  ? 0.2577 0.3305 0.6021 -0.0424 0.0096  -0.0028 65  LYS A C   
472  O O   . LYS A 63  ? 0.2648 0.3396 0.6251 -0.0429 0.0180  -0.0047 65  LYS A O   
473  C CB  . LYS A 63  ? 0.2844 0.3551 0.6048 -0.0446 0.0121  0.0010  65  LYS A CB  
474  C CG  . LYS A 63  ? 0.3147 0.3844 0.6121 -0.0454 0.0138  0.0005  65  LYS A CG  
475  C CD  . LYS A 63  ? 0.3551 0.4226 0.6514 -0.0462 0.0101  0.0073  65  LYS A CD  
476  C CE  . LYS A 63  ? 0.4136 0.4803 0.6887 -0.0471 0.0124  0.0078  65  LYS A CE  
477  N NZ  . LYS A 63  ? 0.4609 0.5257 0.7392 -0.0484 0.0116  0.0150  65  LYS A NZ  
478  N N   . PHE A 64  ? 0.2276 0.2987 0.5744 -0.0410 -0.0017 0.0012  66  PHE A N   
479  C CA  . PHE A 64  ? 0.2155 0.2871 0.5833 -0.0402 -0.0061 0.0041  66  PHE A CA  
480  C C   . PHE A 64  ? 0.2130 0.2812 0.5792 -0.0394 -0.0186 0.0095  66  PHE A C   
481  O O   . PHE A 64  ? 0.2215 0.2867 0.5689 -0.0385 -0.0241 0.0098  66  PHE A O   
482  C CB  . PHE A 64  ? 0.2038 0.2769 0.5748 -0.0388 -0.0056 0.0006  66  PHE A CB  
483  C CG  . PHE A 64  ? 0.1850 0.2569 0.5365 -0.0371 -0.0120 -0.0007 66  PHE A CG  
484  C CD1 . PHE A 64  ? 0.1893 0.2591 0.5387 -0.0352 -0.0223 0.0034  66  PHE A CD1 
485  C CD2 . PHE A 64  ? 0.1823 0.2549 0.5172 -0.0374 -0.0077 -0.0057 66  PHE A CD2 
486  C CE1 . PHE A 64  ? 0.2118 0.2808 0.5439 -0.0332 -0.0267 0.0027  66  PHE A CE1 
487  C CE2 . PHE A 64  ? 0.1926 0.2648 0.5119 -0.0358 -0.0133 -0.0061 66  PHE A CE2 
488  C CZ  . PHE A 64  ? 0.1947 0.2653 0.5134 -0.0335 -0.0221 -0.0018 66  PHE A CZ  
489  N N   . ASP A 65  ? 0.2020 0.2702 0.5879 -0.0396 -0.0234 0.0136  67  ASP A N   
490  C CA  . ASP A 65  ? 0.2126 0.2764 0.5974 -0.0390 -0.0362 0.0182  67  ASP A CA  
491  C C   . ASP A 65  ? 0.2070 0.2711 0.6089 -0.0384 -0.0429 0.0216  67  ASP A C   
492  O O   . ASP A 65  ? 0.2064 0.2670 0.6137 -0.0388 -0.0533 0.0260  67  ASP A O   
493  C CB  . ASP A 65  ? 0.2262 0.2878 0.6148 -0.0410 -0.0383 0.0216  67  ASP A CB  
494  C CG  . ASP A 65  ? 0.2987 0.3639 0.7132 -0.0435 -0.0321 0.0246  67  ASP A CG  
495  O OD1 . ASP A 65  ? 0.3165 0.3861 0.7458 -0.0434 -0.0242 0.0232  67  ASP A OD1 
496  O OD2 . ASP A 65  ? 0.3675 0.4310 0.7882 -0.0454 -0.0346 0.0285  67  ASP A OD2 
497  N N   . THR A 66  ? 0.2069 0.2745 0.6171 -0.0375 -0.0377 0.0196  68  THR A N   
498  C CA  . THR A 66  ? 0.2141 0.2818 0.6371 -0.0365 -0.0442 0.0231  68  THR A CA  
499  C C   . THR A 66  ? 0.2168 0.2857 0.6294 -0.0344 -0.0420 0.0201  68  THR A C   
500  O O   . THR A 66  ? 0.2149 0.2855 0.6178 -0.0344 -0.0335 0.0146  68  THR A O   
501  C CB  . THR A 66  ? 0.2280 0.2996 0.6822 -0.0379 -0.0400 0.0257  68  THR A CB  
502  O OG1 . THR A 66  ? 0.2580 0.3334 0.7187 -0.0376 -0.0274 0.0208  68  THR A OG1 
503  C CG2 . THR A 66  ? 0.2264 0.2984 0.6944 -0.0402 -0.0397 0.0289  68  THR A CG2 
504  N N   . VAL A 67  ? 0.2201 0.2878 0.6354 -0.0329 -0.0501 0.0241  69  VAL A N   
505  C CA  . VAL A 67  ? 0.2333 0.3022 0.6434 -0.0310 -0.0488 0.0232  69  VAL A CA  
506  C C   . VAL A 67  ? 0.2259 0.2990 0.6534 -0.0319 -0.0380 0.0196  69  VAL A C   
507  O O   . VAL A 67  ? 0.2252 0.2995 0.6444 -0.0314 -0.0322 0.0150  69  VAL A O   
508  C CB  . VAL A 67  ? 0.2310 0.2978 0.6436 -0.0294 -0.0593 0.0298  69  VAL A CB  
509  C CG1 . VAL A 67  ? 0.2335 0.3023 0.6451 -0.0278 -0.0568 0.0300  69  VAL A CG1 
510  C CG2 . VAL A 67  ? 0.2308 0.2919 0.6228 -0.0282 -0.0699 0.0321  69  VAL A CG2 
511  N N   . GLU A 68  ? 0.2156 0.2906 0.6679 -0.0331 -0.0352 0.0214  70  GLU A N   
512  C CA  . GLU A 68  ? 0.2109 0.2889 0.6826 -0.0335 -0.0245 0.0178  70  GLU A CA  
513  C C   . GLU A 68  ? 0.2116 0.2904 0.6740 -0.0346 -0.0127 0.0096  70  GLU A C   
514  O O   . GLU A 68  ? 0.2326 0.3120 0.6967 -0.0344 -0.0051 0.0041  70  GLU A O   
515  C CB  . GLU A 68  ? 0.2310 0.3111 0.7334 -0.0342 -0.0242 0.0224  70  GLU A CB  
516  C CG  . GLU A 68  ? 0.2391 0.3189 0.7547 -0.0333 -0.0353 0.0304  70  GLU A CG  
517  C CD  . GLU A 68  ? 0.2925 0.3690 0.7959 -0.0334 -0.0493 0.0363  70  GLU A CD  
518  O OE1 . GLU A 68  ? 0.2531 0.3277 0.7430 -0.0344 -0.0504 0.0346  70  GLU A OE1 
519  O OE2 . GLU A 68  ? 0.3389 0.4141 0.8455 -0.0325 -0.0592 0.0425  70  GLU A OE2 
520  N N   . ASP A 69  ? 0.2046 0.2827 0.6568 -0.0357 -0.0115 0.0089  71  ASP A N   
521  C CA  . ASP A 69  ? 0.1994 0.2777 0.6388 -0.0368 -0.0011 0.0019  71  ASP A CA  
522  C C   . ASP A 69  ? 0.2066 0.2837 0.6203 -0.0363 -0.0027 -0.0022 71  ASP A C   
523  O O   . ASP A 69  ? 0.2171 0.2944 0.6226 -0.0370 0.0052  -0.0089 71  ASP A O   
524  C CB  . ASP A 69  ? 0.1824 0.2606 0.6202 -0.0382 0.0006  0.0038  71  ASP A CB  
525  C CG  . ASP A 69  ? 0.2188 0.2992 0.6856 -0.0389 0.0038  0.0078  71  ASP A CG  
526  O OD1 . ASP A 69  ? 0.2324 0.3147 0.7174 -0.0383 0.0115  0.0054  71  ASP A OD1 
527  O OD2 . ASP A 69  ? 0.2061 0.2862 0.6787 -0.0399 -0.0015 0.0133  71  ASP A OD2 
528  N N   . PHE A 70  ? 0.1946 0.2702 0.5956 -0.0350 -0.0130 0.0017  72  PHE A N   
529  C CA  . PHE A 70  ? 0.1705 0.2459 0.5524 -0.0340 -0.0147 -0.0011 72  PHE A CA  
530  C C   . PHE A 70  ? 0.1665 0.2435 0.5574 -0.0339 -0.0104 -0.0044 72  PHE A C   
531  O O   . PHE A 70  ? 0.1518 0.2291 0.5333 -0.0347 -0.0055 -0.0104 72  PHE A O   
532  C CB  . PHE A 70  ? 0.1652 0.2386 0.5351 -0.0319 -0.0254 0.0042  72  PHE A CB  
533  C CG  . PHE A 70  ? 0.1691 0.2434 0.5260 -0.0304 -0.0263 0.0027  72  PHE A CG  
534  C CD1 . PHE A 70  ? 0.1731 0.2477 0.5119 -0.0306 -0.0246 -0.0009 72  PHE A CD1 
535  C CD2 . PHE A 70  ? 0.1685 0.2437 0.5331 -0.0290 -0.0289 0.0057  72  PHE A CD2 
536  C CE1 . PHE A 70  ? 0.1785 0.2546 0.5085 -0.0294 -0.0255 -0.0017 72  PHE A CE1 
537  C CE2 . PHE A 70  ? 0.1769 0.2536 0.5319 -0.0279 -0.0291 0.0050  72  PHE A CE2 
538  C CZ  . PHE A 70  ? 0.1714 0.2487 0.5101 -0.0281 -0.0274 0.0012  72  PHE A CZ  
539  N N   . TRP A 71  ? 0.1784 0.2558 0.5879 -0.0330 -0.0130 -0.0003 73  TRP A N   
540  C CA  . TRP A 71  ? 0.1860 0.2644 0.6063 -0.0328 -0.0096 -0.0026 73  TRP A CA  
541  C C   . TRP A 71  ? 0.1903 0.2687 0.6209 -0.0344 0.0014  -0.0102 73  TRP A C   
542  O O   . TRP A 71  ? 0.1884 0.2664 0.6174 -0.0349 0.0050  -0.0156 73  TRP A O   
543  C CB  . TRP A 71  ? 0.1923 0.2711 0.6309 -0.0315 -0.0152 0.0046  73  TRP A CB  
544  C CG  . TRP A 71  ? 0.2132 0.2914 0.6390 -0.0296 -0.0247 0.0109  73  TRP A CG  
545  C CD1 . TRP A 71  ? 0.2308 0.3075 0.6563 -0.0283 -0.0337 0.0183  73  TRP A CD1 
546  C CD2 . TRP A 71  ? 0.2128 0.2917 0.6248 -0.0286 -0.0259 0.0105  73  TRP A CD2 
547  N NE1 . TRP A 71  ? 0.2385 0.3144 0.6493 -0.0263 -0.0395 0.0222  73  TRP A NE1 
548  C CE2 . TRP A 71  ? 0.2293 0.3071 0.6327 -0.0263 -0.0344 0.0180  73  TRP A CE2 
549  C CE3 . TRP A 71  ? 0.2042 0.2843 0.6107 -0.0294 -0.0207 0.0047  73  TRP A CE3 
550  C CZ2 . TRP A 71  ? 0.2352 0.3137 0.6255 -0.0245 -0.0364 0.0202  73  TRP A CZ2 
551  C CZ3 . TRP A 71  ? 0.2259 0.3072 0.6213 -0.0281 -0.0238 0.0072  73  TRP A CZ3 
552  C CH2 . TRP A 71  ? 0.2344 0.3152 0.6222 -0.0255 -0.0309 0.0150  73  TRP A CH2 
553  N N   . ALA A 72  ? 0.2124 0.2908 0.6538 -0.0351 0.0070  -0.0110 74  ALA A N   
554  C CA  . ALA A 72  ? 0.2139 0.2915 0.6618 -0.0361 0.0193  -0.0193 74  ALA A CA  
555  C C   . ALA A 72  ? 0.2191 0.2953 0.6414 -0.0375 0.0229  -0.0268 74  ALA A C   
556  O O   . ALA A 72  ? 0.2373 0.3117 0.6581 -0.0383 0.0288  -0.0345 74  ALA A O   
557  C CB  . ALA A 72  ? 0.2151 0.2935 0.6773 -0.0364 0.0254  -0.0181 74  ALA A CB  
558  N N   . LEU A 73  ? 0.2070 0.2835 0.6098 -0.0379 0.0184  -0.0245 75  LEU A N   
559  C CA  . LEU A 73  ? 0.2109 0.2865 0.5893 -0.0392 0.0199  -0.0299 75  LEU A CA  
560  C C   . LEU A 73  ? 0.2107 0.2865 0.5808 -0.0391 0.0149  -0.0319 75  LEU A C   
561  O O   . LEU A 73  ? 0.2327 0.3072 0.5934 -0.0407 0.0186  -0.0392 75  LEU A O   
562  C CB  . LEU A 73  ? 0.2147 0.2906 0.5772 -0.0392 0.0151  -0.0252 75  LEU A CB  
563  C CG  . LEU A 73  ? 0.2371 0.3124 0.5748 -0.0405 0.0156  -0.0292 75  LEU A CG  
564  C CD1 . LEU A 73  ? 0.2361 0.3098 0.5689 -0.0423 0.0262  -0.0368 75  LEU A CD1 
565  C CD2 . LEU A 73  ? 0.2475 0.3227 0.5727 -0.0401 0.0104  -0.0237 75  LEU A CD2 
566  N N   . TYR A 74  ? 0.2049 0.2821 0.5781 -0.0374 0.0065  -0.0254 76  TYR A N   
567  C CA  . TYR A 74  ? 0.2117 0.2899 0.5808 -0.0371 0.0022  -0.0256 76  TYR A CA  
568  C C   . TYR A 74  ? 0.2504 0.3276 0.6348 -0.0381 0.0071  -0.0309 76  TYR A C   
569  O O   . TYR A 74  ? 0.2201 0.2970 0.5977 -0.0395 0.0075  -0.0362 76  TYR A O   
570  C CB  . TYR A 74  ? 0.1972 0.2767 0.5687 -0.0346 -0.0061 -0.0167 76  TYR A CB  
571  C CG  . TYR A 74  ? 0.1988 0.2800 0.5657 -0.0340 -0.0097 -0.0157 76  TYR A CG  
572  C CD1 . TYR A 74  ? 0.2171 0.2996 0.5655 -0.0334 -0.0133 -0.0152 76  TYR A CD1 
573  C CD2 . TYR A 74  ? 0.1937 0.2755 0.5768 -0.0340 -0.0091 -0.0149 76  TYR A CD2 
574  C CE1 . TYR A 74  ? 0.2275 0.3124 0.5741 -0.0328 -0.0159 -0.0137 76  TYR A CE1 
575  C CE2 . TYR A 74  ? 0.2146 0.2985 0.5956 -0.0337 -0.0117 -0.0135 76  TYR A CE2 
576  C CZ  . TYR A 74  ? 0.2317 0.3174 0.5949 -0.0331 -0.0149 -0.0128 76  TYR A CZ  
577  O OH  . TYR A 74  ? 0.2393 0.3277 0.6033 -0.0328 -0.0169 -0.0107 76  TYR A OH  
578  N N   . ASN A 75  ? 0.2812 0.3578 0.6878 -0.0374 0.0102  -0.0294 77  ASN A N   
579  C CA  . ASN A 75  ? 0.3080 0.3828 0.7322 -0.0380 0.0151  -0.0341 77  ASN A CA  
580  C C   . ASN A 75  ? 0.3301 0.4016 0.7471 -0.0401 0.0236  -0.0452 77  ASN A C   
581  O O   . ASN A 75  ? 0.3536 0.4230 0.7705 -0.0415 0.0250  -0.0516 77  ASN A O   
582  C CB  . ASN A 75  ? 0.3479 0.4227 0.7983 -0.0366 0.0168  -0.0296 77  ASN A CB  
583  C CG  . ASN A 75  ? 0.4270 0.5041 0.8858 -0.0348 0.0080  -0.0190 77  ASN A CG  
584  O OD1 . ASN A 75  ? 0.4700 0.5483 0.9198 -0.0345 0.0023  -0.0160 77  ASN A OD1 
585  N ND2 . ASN A 75  ? 0.4155 0.4932 0.8916 -0.0336 0.0065  -0.0128 77  ASN A ND2 
586  N N   . HIS A 76  ? 0.3467 0.4175 0.7572 -0.0403 0.0294  -0.0476 78  HIS A N   
587  C CA  . HIS A 76  ? 0.3630 0.4303 0.7607 -0.0422 0.0376  -0.0578 78  HIS A CA  
588  C C   . HIS A 76  ? 0.3561 0.4228 0.7307 -0.0442 0.0331  -0.0623 78  HIS A C   
589  O O   . HIS A 76  ? 0.3570 0.4203 0.7312 -0.0457 0.0353  -0.0704 78  HIS A O   
590  C CB  . HIS A 76  ? 0.3928 0.4602 0.7847 -0.0420 0.0441  -0.0574 78  HIS A CB  
591  C CG  . HIS A 76  ? 0.4661 0.5295 0.8433 -0.0437 0.0535  -0.0676 78  HIS A CG  
592  N ND1 . HIS A 76  ? 0.5163 0.5795 0.8671 -0.0452 0.0527  -0.0691 78  HIS A ND1 
593  C CD2 . HIS A 76  ? 0.4833 0.5422 0.8678 -0.0438 0.0635  -0.0767 78  HIS A CD2 
594  C CE1 . HIS A 76  ? 0.5276 0.5862 0.8689 -0.0464 0.0620  -0.0787 78  HIS A CE1 
595  N NE2 . HIS A 76  ? 0.5133 0.5689 0.8739 -0.0455 0.0691  -0.0841 78  HIS A NE2 
596  N N   . ILE A 77  ? 0.3519 0.4214 0.7085 -0.0442 0.0263  -0.0571 79  ILE A N   
597  C CA  . ILE A 77  ? 0.3490 0.4187 0.6856 -0.0459 0.0213  -0.0601 79  ILE A CA  
598  C C   . ILE A 77  ? 0.3468 0.4169 0.6924 -0.0466 0.0166  -0.0614 79  ILE A C   
599  O O   . ILE A 77  ? 0.3443 0.4126 0.6801 -0.0489 0.0154  -0.0681 79  ILE A O   
600  C CB  . ILE A 77  ? 0.3441 0.4173 0.6661 -0.0449 0.0143  -0.0523 79  ILE A CB  
601  C CG1 . ILE A 77  ? 0.3720 0.4445 0.6843 -0.0448 0.0186  -0.0509 79  ILE A CG1 
602  C CG2 . ILE A 77  ? 0.3318 0.4064 0.6376 -0.0462 0.0080  -0.0538 79  ILE A CG2 
603  C CD1 . ILE A 77  ? 0.3953 0.4664 0.6840 -0.0469 0.0203  -0.0553 79  ILE A CD1 
604  N N   . GLN A 78  ? 0.3459 0.4181 0.7102 -0.0446 0.0136  -0.0547 80  GLN A N   
605  C CA  . GLN A 78  ? 0.3541 0.4272 0.7290 -0.0451 0.0096  -0.0542 80  GLN A CA  
606  C C   . GLN A 78  ? 0.4060 0.4741 0.7917 -0.0472 0.0151  -0.0639 80  GLN A C   
607  O O   . GLN A 78  ? 0.4136 0.4810 0.7993 -0.0492 0.0120  -0.0676 80  GLN A O   
608  C CB  . GLN A 78  ? 0.3264 0.4024 0.7181 -0.0425 0.0059  -0.0441 80  GLN A CB  
609  C CG  . GLN A 78  ? 0.2913 0.3689 0.6936 -0.0428 0.0019  -0.0416 80  GLN A CG  
610  C CD  . GLN A 78  ? 0.3046 0.3853 0.7175 -0.0400 -0.0022 -0.0303 80  GLN A CD  
611  O OE1 . GLN A 78  ? 0.2861 0.3659 0.7120 -0.0385 -0.0006 -0.0268 80  GLN A OE1 
612  N NE2 . GLN A 78  ? 0.3218 0.4063 0.7290 -0.0389 -0.0076 -0.0239 80  GLN A NE2 
613  N N   . LEU A 79  ? 0.4384 0.5030 0.8342 -0.0466 0.0231  -0.0680 81  LEU A N   
614  C CA  . LEU A 79  ? 0.4743 0.5329 0.8804 -0.0481 0.0297  -0.0782 81  LEU A CA  
615  C C   . LEU A 79  ? 0.5143 0.5681 0.8983 -0.0507 0.0334  -0.0898 81  LEU A C   
616  O O   . LEU A 79  ? 0.5178 0.5664 0.9025 -0.0529 0.0342  -0.0990 81  LEU A O   
617  C CB  . LEU A 79  ? 0.4724 0.5292 0.8989 -0.0459 0.0379  -0.0779 81  LEU A CB  
618  C CG  . LEU A 79  ? 0.4983 0.5588 0.9487 -0.0435 0.0340  -0.0669 81  LEU A CG  
619  C CD1 . LEU A 79  ? 0.4975 0.5568 0.9678 -0.0414 0.0416  -0.0661 81  LEU A CD1 
620  C CD2 . LEU A 79  ? 0.5066 0.5663 0.9720 -0.0442 0.0297  -0.0659 81  LEU A CD2 
621  N N   . SER A 80  ? 0.5325 0.5874 0.8969 -0.0506 0.0353  -0.0893 82  SER A N   
622  C CA  . SER A 80  ? 0.5641 0.6139 0.9072 -0.0527 0.0407  -0.0995 82  SER A CA  
623  C C   . SER A 80  ? 0.5909 0.6415 0.9094 -0.0554 0.0327  -0.1011 82  SER A C   
624  O O   . SER A 80  ? 0.6088 0.6538 0.9130 -0.0580 0.0342  -0.1114 82  SER A O   
625  C CB  . SER A 80  ? 0.5948 0.6448 0.9323 -0.0511 0.0491  -0.0979 82  SER A CB  
626  O OG  . SER A 80  ? 0.6493 0.7054 0.9794 -0.0501 0.0436  -0.0875 82  SER A OG  
627  N N   . SER A 81  ? 0.5897 0.6467 0.9031 -0.0547 0.0242  -0.0915 83  SER A N   
628  C CA  . SER A 81  ? 0.6070 0.6653 0.8961 -0.0567 0.0180  -0.0918 83  SER A CA  
629  C C   . SER A 81  ? 0.6176 0.6769 0.9063 -0.0591 0.0089  -0.0935 83  SER A C   
630  O O   . SER A 81  ? 0.6120 0.6736 0.9200 -0.0584 0.0057  -0.0899 83  SER A O   
631  C CB  . SER A 81  ? 0.6067 0.6708 0.8890 -0.0545 0.0144  -0.0810 83  SER A CB  
632  O OG  . SER A 81  ? 0.6320 0.6949 0.9129 -0.0531 0.0222  -0.0797 83  SER A OG  
633  N N   . ASN A 82  ? 0.6320 0.6898 0.8994 -0.0620 0.0046  -0.0983 84  ASN A N   
634  C CA  . ASN A 82  ? 0.6606 0.7203 0.9269 -0.0646 -0.0054 -0.0989 84  ASN A CA  
635  C C   . ASN A 82  ? 0.6596 0.7266 0.9179 -0.0635 -0.0133 -0.0890 84  ASN A C   
636  O O   . ASN A 82  ? 0.6734 0.7416 0.9176 -0.0621 -0.0118 -0.0851 84  ASN A O   
637  C CB  . ASN A 82  ? 0.7109 0.7638 0.9588 -0.0689 -0.0069 -0.1107 84  ASN A CB  
638  C CG  . ASN A 82  ? 0.7708 0.8153 1.0269 -0.0705 -0.0011 -0.1225 84  ASN A CG  
639  O OD1 . ASN A 82  ? 0.8042 0.8452 1.0631 -0.0739 -0.0069 -0.1292 84  ASN A OD1 
640  N ND2 . ASN A 82  ? 0.7752 0.8159 1.0362 -0.0682 0.0103  -0.1252 84  ASN A ND2 
641  N N   . LEU A 83  ? 0.6492 0.7207 0.9174 -0.0642 -0.0214 -0.0850 85  LEU A N   
642  C CA  . LEU A 83  ? 0.6486 0.7275 0.9135 -0.0626 -0.0286 -0.0755 85  LEU A CA  
643  C C   . LEU A 83  ? 0.6550 0.7343 0.9045 -0.0662 -0.0369 -0.0785 85  LEU A C   
644  O O   . LEU A 83  ? 0.6566 0.7378 0.9157 -0.0686 -0.0434 -0.0796 85  LEU A O   
645  C CB  . LEU A 83  ? 0.6355 0.7196 0.9230 -0.0608 -0.0314 -0.0683 85  LEU A CB  
646  C CG  . LEU A 83  ? 0.6417 0.7335 0.9292 -0.0582 -0.0371 -0.0579 85  LEU A CG  
647  C CD1 . LEU A 83  ? 0.6472 0.7404 0.9282 -0.0537 -0.0337 -0.0508 85  LEU A CD1 
648  C CD2 . LEU A 83  ? 0.6442 0.7407 0.9530 -0.0574 -0.0396 -0.0526 85  LEU A CD2 
649  N N   . MET A 84  ? 0.6570 0.7348 0.8841 -0.0667 -0.0371 -0.0792 86  MET A N   
650  C CA  . MET A 84  ? 0.6665 0.7443 0.8776 -0.0703 -0.0456 -0.0819 86  MET A CA  
651  C C   . MET A 84  ? 0.6443 0.7300 0.8549 -0.0680 -0.0523 -0.0710 86  MET A C   
652  O O   . MET A 84  ? 0.6536 0.7410 0.8597 -0.0643 -0.0487 -0.0644 86  MET A O   
653  C CB  . MET A 84  ? 0.7071 0.7783 0.8920 -0.0725 -0.0423 -0.0887 86  MET A CB  
654  C CG  . MET A 84  ? 0.7654 0.8291 0.9494 -0.0725 -0.0310 -0.0973 86  MET A CG  
655  S SD  . MET A 84  ? 0.9030 0.9589 1.0543 -0.0750 -0.0262 -0.1051 86  MET A SD  
656  C CE  . MET A 84  ? 0.8025 0.8526 0.9430 -0.0809 -0.0357 -0.1167 86  MET A CE  
657  N N   . PRO A 85  ? 0.6119 0.7021 0.8282 -0.0698 -0.0618 -0.0687 87  PRO A N   
658  C CA  . PRO A 85  ? 0.5967 0.6938 0.8098 -0.0675 -0.0679 -0.0589 87  PRO A CA  
659  C C   . PRO A 85  ? 0.5920 0.6866 0.7801 -0.0683 -0.0694 -0.0589 87  PRO A C   
660  O O   . PRO A 85  ? 0.5960 0.6839 0.7670 -0.0716 -0.0674 -0.0670 87  PRO A O   
661  C CB  . PRO A 85  ? 0.6049 0.7071 0.8309 -0.0701 -0.0777 -0.0576 87  PRO A CB  
662  C CG  . PRO A 85  ? 0.6082 0.7069 0.8487 -0.0730 -0.0761 -0.0652 87  PRO A CG  
663  C CD  . PRO A 85  ? 0.5999 0.6896 0.8284 -0.0738 -0.0675 -0.0743 87  PRO A CD  
664  N N   . GLY A 86  ? 0.5752 0.6749 0.7614 -0.0651 -0.0723 -0.0494 88  GLY A N   
665  C CA  . GLY A 86  ? 0.5727 0.6707 0.7381 -0.0649 -0.0732 -0.0467 88  GLY A CA  
666  C C   . GLY A 86  ? 0.5559 0.6504 0.7155 -0.0619 -0.0634 -0.0452 88  GLY A C   
667  O O   . GLY A 86  ? 0.5587 0.6528 0.7053 -0.0607 -0.0636 -0.0403 88  GLY A O   
668  N N   . CYS A 87  ? 0.5364 0.6285 0.7072 -0.0607 -0.0553 -0.0487 89  CYS A N   
669  C CA  . CYS A 87  ? 0.5379 0.6266 0.7063 -0.0584 -0.0463 -0.0479 89  CYS A CA  
670  C C   . CYS A 87  ? 0.4959 0.5881 0.6775 -0.0532 -0.0451 -0.0393 89  CYS A C   
671  O O   . CYS A 87  ? 0.4921 0.5889 0.6873 -0.0511 -0.0488 -0.0355 89  CYS A O   
672  C CB  . CYS A 87  ? 0.5749 0.6585 0.7477 -0.0601 -0.0385 -0.0565 89  CYS A CB  
673  S SG  . CYS A 87  ? 0.7502 0.8274 0.9034 -0.0657 -0.0384 -0.0679 89  CYS A SG  
674  N N   . ASP A 88  ? 0.4581 0.5479 0.6354 -0.0512 -0.0401 -0.0363 90  ASP A N   
675  C CA  . ASP A 88  ? 0.4213 0.5124 0.6078 -0.0466 -0.0393 -0.0294 90  ASP A CA  
676  C C   . ASP A 88  ? 0.3691 0.4564 0.5598 -0.0460 -0.0316 -0.0309 90  ASP A C   
677  O O   . ASP A 88  ? 0.3733 0.4572 0.5548 -0.0483 -0.0268 -0.0342 90  ASP A O   
678  C CB  . ASP A 88  ? 0.4679 0.5598 0.6448 -0.0444 -0.0433 -0.0224 90  ASP A CB  
679  C CG  . ASP A 88  ? 0.5331 0.6289 0.7040 -0.0453 -0.0512 -0.0202 90  ASP A CG  
680  O OD1 . ASP A 88  ? 0.5291 0.6286 0.7090 -0.0459 -0.0549 -0.0214 90  ASP A OD1 
681  O OD2 . ASP A 88  ? 0.5199 0.6149 0.6783 -0.0455 -0.0539 -0.0166 90  ASP A OD2 
682  N N   . TYR A 89  ? 0.3150 0.4030 0.5199 -0.0430 -0.0304 -0.0280 91  TYR A N   
683  C CA  . TYR A 89  ? 0.3046 0.3896 0.5163 -0.0419 -0.0249 -0.0274 91  TYR A CA  
684  C C   . TYR A 89  ? 0.2575 0.3424 0.4704 -0.0380 -0.0279 -0.0201 91  TYR A C   
685  O O   . TYR A 89  ? 0.2449 0.3322 0.4594 -0.0353 -0.0326 -0.0164 91  TYR A O   
686  C CB  . TYR A 89  ? 0.3280 0.4130 0.5559 -0.0420 -0.0217 -0.0304 91  TYR A CB  
687  C CG  . TYR A 89  ? 0.3841 0.4672 0.6127 -0.0455 -0.0170 -0.0387 91  TYR A CG  
688  C CD1 . TYR A 89  ? 0.4075 0.4919 0.6356 -0.0478 -0.0200 -0.0431 91  TYR A CD1 
689  C CD2 . TYR A 89  ? 0.4288 0.5085 0.6593 -0.0467 -0.0094 -0.0422 91  TYR A CD2 
690  C CE1 . TYR A 89  ? 0.4324 0.5135 0.6598 -0.0511 -0.0159 -0.0518 91  TYR A CE1 
691  C CE2 . TYR A 89  ? 0.4426 0.5195 0.6732 -0.0495 -0.0041 -0.0506 91  TYR A CE2 
692  C CZ  . TYR A 89  ? 0.4500 0.5271 0.6779 -0.0517 -0.0076 -0.0559 91  TYR A CZ  
693  O OH  . TYR A 89  ? 0.5003 0.5732 0.7271 -0.0544 -0.0028 -0.0653 91  TYR A OH  
694  N N   . SER A 90  ? 0.2389 0.3206 0.4515 -0.0377 -0.0250 -0.0184 92  SER A N   
695  C CA  . SER A 90  ? 0.2231 0.3029 0.4361 -0.0345 -0.0282 -0.0125 92  SER A CA  
696  C C   . SER A 90  ? 0.1960 0.2729 0.4190 -0.0343 -0.0252 -0.0117 92  SER A C   
697  O O   . SER A 90  ? 0.2083 0.2842 0.4334 -0.0369 -0.0196 -0.0142 92  SER A O   
698  C CB  . SER A 90  ? 0.2403 0.3187 0.4403 -0.0345 -0.0305 -0.0094 92  SER A CB  
699  O OG  . SER A 90  ? 0.3228 0.4042 0.5151 -0.0344 -0.0345 -0.0092 92  SER A OG  
700  N N   . LEU A 91  ? 0.1644 0.2399 0.3936 -0.0313 -0.0287 -0.0081 93  LEU A N   
701  C CA  . LEU A 91  ? 0.1538 0.2261 0.3918 -0.0311 -0.0282 -0.0061 93  LEU A CA  
702  C C   . LEU A 91  ? 0.1555 0.2241 0.3868 -0.0289 -0.0333 -0.0017 93  LEU A C   
703  O O   . LEU A 91  ? 0.1522 0.2199 0.3790 -0.0256 -0.0381 0.0003  93  LEU A O   
704  C CB  . LEU A 91  ? 0.1408 0.2135 0.3916 -0.0298 -0.0291 -0.0056 93  LEU A CB  
705  C CG  . LEU A 91  ? 0.1382 0.2082 0.4014 -0.0303 -0.0289 -0.0036 93  LEU A CG  
706  C CD1 . LEU A 91  ? 0.1256 0.1971 0.3985 -0.0336 -0.0212 -0.0070 93  LEU A CD1 
707  C CD2 . LEU A 91  ? 0.1272 0.1965 0.3993 -0.0281 -0.0329 -0.0010 93  LEU A CD2 
708  N N   . PHE A 92  ? 0.1517 0.2176 0.3823 -0.0306 -0.0321 -0.0002 94  PHE A N   
709  C CA  . PHE A 92  ? 0.1632 0.2244 0.3882 -0.0290 -0.0372 0.0038  94  PHE A CA  
710  C C   . PHE A 92  ? 0.1912 0.2489 0.4266 -0.0302 -0.0376 0.0059  94  PHE A C   
711  O O   . PHE A 92  ? 0.2191 0.2789 0.4645 -0.0330 -0.0320 0.0048  94  PHE A O   
712  C CB  . PHE A 92  ? 0.1670 0.2282 0.3800 -0.0299 -0.0365 0.0051  94  PHE A CB  
713  C CG  . PHE A 92  ? 0.1742 0.2371 0.3768 -0.0274 -0.0400 0.0052  94  PHE A CG  
714  C CD1 . PHE A 92  ? 0.1862 0.2542 0.3879 -0.0278 -0.0383 0.0021  94  PHE A CD1 
715  C CD2 . PHE A 92  ? 0.1915 0.2507 0.3876 -0.0244 -0.0450 0.0085  94  PHE A CD2 
716  C CE1 . PHE A 92  ? 0.2082 0.2784 0.4036 -0.0254 -0.0417 0.0030  94  PHE A CE1 
717  C CE2 . PHE A 92  ? 0.2102 0.2714 0.3995 -0.0216 -0.0477 0.0091  94  PHE A CE2 
718  C CZ  . PHE A 92  ? 0.2189 0.2860 0.4085 -0.0221 -0.0461 0.0067  94  PHE A CZ  
719  N N   . LYS A 93  ? 0.1618 0.2139 0.3960 -0.0282 -0.0442 0.0088  95  LYS A N   
720  C CA  . LYS A 93  ? 0.1729 0.2213 0.4178 -0.0299 -0.0461 0.0113  95  LYS A CA  
721  C C   . LYS A 93  ? 0.1771 0.2267 0.4245 -0.0334 -0.0403 0.0130  95  LYS A C   
722  O O   . LYS A 93  ? 0.1354 0.1860 0.3716 -0.0339 -0.0378 0.0134  95  LYS A O   
723  C CB  . LYS A 93  ? 0.1679 0.2087 0.4087 -0.0274 -0.0550 0.0134  95  LYS A CB  
724  C CG  . LYS A 93  ? 0.1495 0.1881 0.3878 -0.0240 -0.0602 0.0123  95  LYS A CG  
725  C CD  . LYS A 93  ? 0.1866 0.2166 0.4160 -0.0210 -0.0682 0.0131  95  LYS A CD  
726  C CE  . LYS A 93  ? 0.1887 0.2157 0.4148 -0.0178 -0.0732 0.0124  95  LYS A CE  
727  N NZ  . LYS A 93  ? 0.1776 0.1955 0.3917 -0.0143 -0.0800 0.0120  95  LYS A NZ  
728  N N   . ASP A 94  ? 0.2020 0.2518 0.4646 -0.0359 -0.0380 0.0146  96  ASP A N   
729  C CA  . ASP A 94  ? 0.2477 0.2990 0.5156 -0.0391 -0.0312 0.0170  96  ASP A CA  
730  C C   . ASP A 94  ? 0.2618 0.3086 0.5212 -0.0392 -0.0348 0.0209  96  ASP A C   
731  O O   . ASP A 94  ? 0.2564 0.2974 0.5173 -0.0379 -0.0432 0.0229  96  ASP A O   
732  C CB  . ASP A 94  ? 0.2850 0.3368 0.5747 -0.0412 -0.0299 0.0191  96  ASP A CB  
733  C CG  . ASP A 94  ? 0.3489 0.4041 0.6482 -0.0443 -0.0196 0.0210  96  ASP A CG  
734  O OD1 . ASP A 94  ? 0.3413 0.3990 0.6287 -0.0451 -0.0120 0.0195  96  ASP A OD1 
735  O OD2 . ASP A 94  ? 0.4296 0.4850 0.7485 -0.0460 -0.0192 0.0243  96  ASP A OD2 
736  N N   . GLY A 95  ? 0.2739 0.3230 0.5228 -0.0405 -0.0289 0.0217  97  GLY A N   
737  C CA  . GLY A 95  ? 0.2763 0.3219 0.5173 -0.0409 -0.0310 0.0263  97  GLY A CA  
738  C C   . GLY A 95  ? 0.2749 0.3190 0.4993 -0.0380 -0.0361 0.0256  97  GLY A C   
739  O O   . GLY A 95  ? 0.2683 0.3088 0.4872 -0.0378 -0.0389 0.0297  97  GLY A O   
740  N N   . ILE A 96  ? 0.2710 0.3178 0.4891 -0.0357 -0.0373 0.0210  98  ILE A N   
741  C CA  . ILE A 96  ? 0.2759 0.3230 0.4802 -0.0330 -0.0409 0.0204  98  ILE A CA  
742  C C   . ILE A 96  ? 0.2706 0.3241 0.4672 -0.0346 -0.0353 0.0172  98  ILE A C   
743  O O   . ILE A 96  ? 0.2582 0.3151 0.4594 -0.0349 -0.0324 0.0128  98  ILE A O   
744  C CB  . ILE A 96  ? 0.2747 0.3195 0.4788 -0.0288 -0.0472 0.0181  98  ILE A CB  
745  C CG1 . ILE A 96  ? 0.2929 0.3300 0.5036 -0.0274 -0.0534 0.0198  98  ILE A CG1 
746  C CG2 . ILE A 96  ? 0.2739 0.3197 0.4661 -0.0257 -0.0500 0.0182  98  ILE A CG2 
747  C CD1 . ILE A 96  ? 0.2943 0.3280 0.5017 -0.0228 -0.0593 0.0173  98  ILE A CD1 
748  N N   . GLU A 97  ? 0.2739 0.3285 0.4588 -0.0356 -0.0344 0.0195  99  GLU A N   
749  C CA  . GLU A 97  ? 0.2903 0.3500 0.4654 -0.0370 -0.0315 0.0162  99  GLU A CA  
750  C C   . GLU A 97  ? 0.2926 0.3545 0.4650 -0.0339 -0.0368 0.0138  99  GLU A C   
751  O O   . GLU A 97  ? 0.2779 0.3371 0.4504 -0.0304 -0.0425 0.0164  99  GLU A O   
752  C CB  . GLU A 97  ? 0.3358 0.3958 0.4983 -0.0392 -0.0298 0.0200  99  GLU A CB  
753  C CG  . GLU A 97  ? 0.4363 0.4956 0.6004 -0.0427 -0.0218 0.0219  99  GLU A CG  
754  C CD  . GLU A 97  ? 0.6235 0.6836 0.7721 -0.0452 -0.0189 0.0253  99  GLU A CD  
755  O OE1 . GLU A 97  ? 0.6701 0.7320 0.8127 -0.0480 -0.0109 0.0224  99  GLU A OE1 
756  O OE2 . GLU A 97  ? 0.6722 0.7306 0.8139 -0.0443 -0.0245 0.0308  99  GLU A OE2 
757  N N   . PRO A 98  ? 0.2892 0.3556 0.4605 -0.0349 -0.0347 0.0088  100 PRO A N   
758  C CA  . PRO A 98  ? 0.2856 0.3549 0.4561 -0.0323 -0.0393 0.0074  100 PRO A CA  
759  C C   . PRO A 98  ? 0.3114 0.3827 0.4716 -0.0319 -0.0436 0.0100  100 PRO A C   
760  O O   . PRO A 98  ? 0.3189 0.3945 0.4766 -0.0326 -0.0450 0.0075  100 PRO A O   
761  C CB  . PRO A 98  ? 0.2791 0.3519 0.4542 -0.0343 -0.0353 0.0013  100 PRO A CB  
762  C CG  . PRO A 98  ? 0.2754 0.3480 0.4458 -0.0382 -0.0294 -0.0007 100 PRO A CG  
763  C CD  . PRO A 98  ? 0.2773 0.3458 0.4499 -0.0383 -0.0276 0.0039  100 PRO A CD  
764  N N   . MET A 99  ? 0.3159 0.3840 0.4718 -0.0307 -0.0464 0.0154  101 MET A N   
765  C CA  . MET A 99  ? 0.3434 0.4131 0.4908 -0.0302 -0.0510 0.0192  101 MET A CA  
766  C C   . MET A 99  ? 0.3442 0.4099 0.4953 -0.0255 -0.0556 0.0237  101 MET A C   
767  O O   . MET A 99  ? 0.3473 0.4072 0.5024 -0.0245 -0.0551 0.0254  101 MET A O   
768  C CB  . MET A 99  ? 0.3852 0.4543 0.5215 -0.0342 -0.0489 0.0219  101 MET A CB  
769  C CG  . MET A 99  ? 0.4822 0.5548 0.6109 -0.0386 -0.0449 0.0165  101 MET A CG  
770  S SD  . MET A 99  ? 0.7401 0.8184 0.8625 -0.0394 -0.0510 0.0140  101 MET A SD  
771  C CE  . MET A 99  ? 0.8019 0.8810 0.9183 -0.0442 -0.0448 0.0055  101 MET A CE  
772  N N   . TRP A 100 ? 0.3392 0.4076 0.4899 -0.0225 -0.0601 0.0256  102 TRP A N   
773  C CA  . TRP A 100 ? 0.3613 0.4256 0.5160 -0.0170 -0.0636 0.0287  102 TRP A CA  
774  C C   . TRP A 100 ? 0.3697 0.4280 0.5214 -0.0170 -0.0654 0.0341  102 TRP A C   
775  O O   . TRP A 100 ? 0.3676 0.4198 0.5230 -0.0130 -0.0674 0.0354  102 TRP A O   
776  C CB  . TRP A 100 ? 0.3594 0.4288 0.5166 -0.0134 -0.0669 0.0298  102 TRP A CB  
777  C CG  . TRP A 100 ? 0.3708 0.4423 0.5244 -0.0132 -0.0715 0.0354  102 TRP A CG  
778  C CD1 . TRP A 100 ? 0.3869 0.4644 0.5355 -0.0169 -0.0739 0.0364  102 TRP A CD1 
779  C CD2 . TRP A 100 ? 0.3686 0.4361 0.5239 -0.0089 -0.0749 0.0407  102 TRP A CD2 
780  N NE1 . TRP A 100 ? 0.3905 0.4682 0.5373 -0.0155 -0.0790 0.0429  102 TRP A NE1 
781  C CE2 . TRP A 100 ? 0.3812 0.4530 0.5332 -0.0104 -0.0793 0.0457  102 TRP A CE2 
782  C CE3 . TRP A 100 ? 0.3624 0.4222 0.5213 -0.0041 -0.0750 0.0415  102 TRP A CE3 
783  C CZ2 . TRP A 100 ? 0.3906 0.4599 0.5447 -0.0070 -0.0835 0.0521  102 TRP A CZ2 
784  C CZ3 . TRP A 100 ? 0.3713 0.4279 0.5318 -0.0006 -0.0786 0.0469  102 TRP A CZ3 
785  C CH2 . TRP A 100 ? 0.3843 0.4461 0.5434 -0.0019 -0.0826 0.0525  102 TRP A CH2 
786  N N   . GLU A 101 ? 0.3709 0.4302 0.5155 -0.0214 -0.0645 0.0371  103 GLU A N   
787  C CA  . GLU A 101 ? 0.3806 0.4348 0.5227 -0.0221 -0.0658 0.0433  103 GLU A CA  
788  C C   . GLU A 101 ? 0.3601 0.4082 0.5076 -0.0233 -0.0627 0.0428  103 GLU A C   
789  O O   . GLU A 101 ? 0.3715 0.4136 0.5212 -0.0225 -0.0647 0.0476  103 GLU A O   
790  C CB  . GLU A 101 ? 0.4348 0.4924 0.5660 -0.0266 -0.0653 0.0471  103 GLU A CB  
791  C CG  . GLU A 101 ? 0.5245 0.5883 0.6502 -0.0264 -0.0700 0.0481  103 GLU A CG  
792  C CD  . GLU A 101 ? 0.5841 0.6540 0.7061 -0.0291 -0.0683 0.0417  103 GLU A CD  
793  O OE1 . GLU A 101 ? 0.5322 0.6021 0.6587 -0.0298 -0.0634 0.0356  103 GLU A OE1 
794  O OE2 . GLU A 101 ? 0.6753 0.7499 0.7906 -0.0307 -0.0724 0.0430  103 GLU A OE2 
795  N N   . ASP A 102 ? 0.3335 0.3827 0.4848 -0.0253 -0.0581 0.0376  104 ASP A N   
796  C CA  . ASP A 102 ? 0.3066 0.3505 0.4664 -0.0260 -0.0563 0.0369  104 ASP A CA  
797  C C   . ASP A 102 ? 0.3126 0.3487 0.4777 -0.0218 -0.0616 0.0382  104 ASP A C   
798  O O   . ASP A 102 ? 0.3081 0.3435 0.4724 -0.0173 -0.0650 0.0364  104 ASP A O   
799  C CB  . ASP A 102 ? 0.2909 0.3375 0.4564 -0.0270 -0.0526 0.0307  104 ASP A CB  
800  C CG  . ASP A 102 ? 0.3101 0.3531 0.4854 -0.0290 -0.0501 0.0306  104 ASP A CG  
801  O OD1 . ASP A 102 ? 0.2989 0.3448 0.4756 -0.0330 -0.0439 0.0304  104 ASP A OD1 
802  O OD2 . ASP A 102 ? 0.3193 0.3562 0.5009 -0.0267 -0.0544 0.0306  104 ASP A OD2 
803  N N   . GLU A 103 ? 0.3331 0.3629 0.5039 -0.0233 -0.0621 0.0411  105 GLU A N   
804  C CA  . GLU A 103 ? 0.3473 0.3678 0.5231 -0.0198 -0.0678 0.0415  105 GLU A CA  
805  C C   . GLU A 103 ? 0.3290 0.3472 0.5062 -0.0160 -0.0701 0.0355  105 GLU A C   
806  O O   . GLU A 103 ? 0.3388 0.3509 0.5141 -0.0113 -0.0744 0.0346  105 GLU A O   
807  C CB  . GLU A 103 ? 0.3945 0.4091 0.5794 -0.0232 -0.0679 0.0447  105 GLU A CB  
808  C CG  . GLU A 103 ? 0.4849 0.4975 0.6689 -0.0251 -0.0679 0.0523  105 GLU A CG  
809  C CD  . GLU A 103 ? 0.5963 0.6034 0.7772 -0.0205 -0.0737 0.0544  105 GLU A CD  
810  O OE1 . GLU A 103 ? 0.6279 0.6268 0.8123 -0.0169 -0.0786 0.0511  105 GLU A OE1 
811  O OE2 . GLU A 103 ? 0.6128 0.6233 0.7872 -0.0203 -0.0735 0.0591  105 GLU A OE2 
812  N N   . LYS A 104 ? 0.3085 0.3311 0.4885 -0.0178 -0.0670 0.0315  106 LYS A N   
813  C CA  . LYS A 104 ? 0.2994 0.3200 0.4802 -0.0145 -0.0691 0.0266  106 LYS A CA  
814  C C   . LYS A 104 ? 0.2815 0.3077 0.4564 -0.0109 -0.0680 0.0244  106 LYS A C   
815  O O   . LYS A 104 ? 0.2920 0.3162 0.4663 -0.0074 -0.0694 0.0212  106 LYS A O   
816  C CB  . LYS A 104 ? 0.3214 0.3438 0.5103 -0.0178 -0.0670 0.0243  106 LYS A CB  
817  C CG  . LYS A 104 ? 0.4049 0.4206 0.6027 -0.0205 -0.0696 0.0265  106 LYS A CG  
818  C CD  . LYS A 104 ? 0.5276 0.5332 0.7254 -0.0171 -0.0771 0.0242  106 LYS A CD  
819  C CE  . LYS A 104 ? 0.6210 0.6195 0.8291 -0.0201 -0.0815 0.0262  106 LYS A CE  
820  N NZ  . LYS A 104 ? 0.7032 0.6906 0.9080 -0.0174 -0.0881 0.0268  106 LYS A NZ  
821  N N   . ASN A 105 ? 0.2519 0.2851 0.4227 -0.0117 -0.0658 0.0263  107 ASN A N   
822  C CA  . ASN A 105 ? 0.2522 0.2909 0.4201 -0.0086 -0.0654 0.0250  107 ASN A CA  
823  C C   . ASN A 105 ? 0.2793 0.3169 0.4437 -0.0048 -0.0684 0.0286  107 ASN A C   
824  O O   . ASN A 105 ? 0.2589 0.2991 0.4231 -0.0006 -0.0686 0.0280  107 ASN A O   
825  C CB  . ASN A 105 ? 0.2518 0.2995 0.4191 -0.0125 -0.0618 0.0238  107 ASN A CB  
826  C CG  . ASN A 105 ? 0.2408 0.2903 0.4131 -0.0159 -0.0581 0.0202  107 ASN A CG  
827  O OD1 . ASN A 105 ? 0.2604 0.3070 0.4372 -0.0143 -0.0586 0.0180  107 ASN A OD1 
828  N ND2 . ASN A 105 ? 0.2135 0.2675 0.3846 -0.0205 -0.0543 0.0197  107 ASN A ND2 
829  N N   . LYS A 106 ? 0.3068 0.3411 0.4700 -0.0062 -0.0703 0.0331  108 LYS A N   
830  C CA  . LYS A 106 ? 0.3237 0.3583 0.4852 -0.0031 -0.0731 0.0375  108 LYS A CA  
831  C C   . LYS A 106 ? 0.3167 0.3461 0.4796 0.0039  -0.0750 0.0362  108 LYS A C   
832  O O   . LYS A 106 ? 0.3243 0.3576 0.4879 0.0072  -0.0757 0.0384  108 LYS A O   
833  C CB  . LYS A 106 ? 0.3650 0.3962 0.5253 -0.0056 -0.0750 0.0436  108 LYS A CB  
834  C CG  . LYS A 106 ? 0.4883 0.5097 0.6522 -0.0066 -0.0762 0.0445  108 LYS A CG  
835  C CD  . LYS A 106 ? 0.6015 0.6211 0.7649 -0.0096 -0.0774 0.0519  108 LYS A CD  
836  C CE  . LYS A 106 ? 0.7042 0.7124 0.8734 -0.0082 -0.0808 0.0542  108 LYS A CE  
837  N NZ  . LYS A 106 ? 0.7492 0.7555 0.9187 -0.0096 -0.0826 0.0626  108 LYS A NZ  
838  N N   . ARG A 107 ? 0.3069 0.3275 0.4701 0.0062  -0.0757 0.0326  109 ARG A N   
839  C CA  . ARG A 107 ? 0.2961 0.3104 0.4581 0.0133  -0.0768 0.0305  109 ARG A CA  
840  C C   . ARG A 107 ? 0.2652 0.2830 0.4256 0.0162  -0.0737 0.0263  109 ARG A C   
841  O O   . ARG A 107 ? 0.2612 0.2725 0.4184 0.0219  -0.0737 0.0236  109 ARG A O   
842  C CB  . ARG A 107 ? 0.3266 0.3275 0.4880 0.0144  -0.0803 0.0289  109 ARG A CB  
843  C CG  . ARG A 107 ? 0.4057 0.4022 0.5703 0.0124  -0.0833 0.0342  109 ARG A CG  
844  C CD  . ARG A 107 ? 0.5118 0.4949 0.6777 0.0126  -0.0874 0.0325  109 ARG A CD  
845  N NE  . ARG A 107 ? 0.6281 0.6104 0.7958 0.0077  -0.0878 0.0300  109 ARG A NE  
846  C CZ  . ARG A 107 ? 0.7002 0.6860 0.8730 0.0012  -0.0869 0.0335  109 ARG A CZ  
847  N NH1 . ARG A 107 ? 0.7118 0.7019 0.8862 -0.0013 -0.0856 0.0398  109 ARG A NH1 
848  N NH2 . ARG A 107 ? 0.7021 0.6874 0.8788 -0.0026 -0.0870 0.0313  109 ARG A NH2 
849  N N   . GLY A 108 ? 0.2357 0.2632 0.3978 0.0124  -0.0710 0.0257  110 GLY A N   
850  C CA  . GLY A 108 ? 0.2205 0.2509 0.3824 0.0134  -0.0683 0.0221  110 GLY A CA  
851  C C   . GLY A 108 ? 0.2106 0.2506 0.3754 0.0154  -0.0654 0.0232  110 GLY A C   
852  O O   . GLY A 108 ? 0.2318 0.2750 0.3986 0.0178  -0.0659 0.0263  110 GLY A O   
853  N N   . GLY A 109 ? 0.1951 0.2397 0.3616 0.0144  -0.0627 0.0210  111 GLY A N   
854  C CA  . GLY A 109 ? 0.2021 0.2569 0.3738 0.0147  -0.0600 0.0220  111 GLY A CA  
855  C C   . GLY A 109 ? 0.2114 0.2701 0.3859 0.0121  -0.0575 0.0196  111 GLY A C   
856  O O   . GLY A 109 ? 0.2062 0.2613 0.3798 0.0090  -0.0579 0.0173  111 GLY A O   
857  N N   . ARG A 110 ? 0.1883 0.2549 0.3684 0.0134  -0.0548 0.0207  112 ARG A N   
858  C CA  . ARG A 110 ? 0.1860 0.2572 0.3711 0.0110  -0.0524 0.0192  112 ARG A CA  
859  C C   . ARG A 110 ? 0.1776 0.2524 0.3663 0.0158  -0.0488 0.0211  112 ARG A C   
860  O O   . ARG A 110 ? 0.1582 0.2374 0.3506 0.0194  -0.0476 0.0240  112 ARG A O   
861  C CB  . ARG A 110 ? 0.2074 0.2862 0.3981 0.0048  -0.0529 0.0185  112 ARG A CB  
862  C CG  . ARG A 110 ? 0.2217 0.3093 0.4193 0.0054  -0.0529 0.0209  112 ARG A CG  
863  C CD  . ARG A 110 ? 0.2187 0.3113 0.4180 -0.0008 -0.0552 0.0195  112 ARG A CD  
864  N NE  . ARG A 110 ? 0.2477 0.3482 0.4539 -0.0003 -0.0571 0.0224  112 ARG A NE  
865  C CZ  . ARG A 110 ? 0.2553 0.3615 0.4645 -0.0054 -0.0599 0.0213  112 ARG A CZ  
866  N NH1 . ARG A 110 ? 0.2583 0.3717 0.4753 -0.0048 -0.0627 0.0246  112 ARG A NH1 
867  N NH2 . ARG A 110 ? 0.2513 0.3559 0.4559 -0.0110 -0.0599 0.0169  112 ARG A NH2 
868  N N   . TRP A 111 ? 0.1917 0.2651 0.3806 0.0156  -0.0469 0.0200  113 TRP A N   
869  C CA  . TRP A 111 ? 0.1951 0.2735 0.3893 0.0182  -0.0428 0.0223  113 TRP A CA  
870  C C   . TRP A 111 ? 0.1805 0.2687 0.3871 0.0129  -0.0422 0.0224  113 TRP A C   
871  O O   . TRP A 111 ? 0.1582 0.2462 0.3673 0.0078  -0.0432 0.0197  113 TRP A O   
872  C CB  . TRP A 111 ? 0.1840 0.2566 0.3729 0.0195  -0.0421 0.0216  113 TRP A CB  
873  C CG  . TRP A 111 ? 0.1754 0.2388 0.3517 0.0257  -0.0420 0.0216  113 TRP A CG  
874  C CD1 . TRP A 111 ? 0.1900 0.2430 0.3562 0.0260  -0.0460 0.0189  113 TRP A CD1 
875  C CD2 . TRP A 111 ? 0.1762 0.2396 0.3487 0.0326  -0.0377 0.0241  113 TRP A CD2 
876  N NE1 . TRP A 111 ? 0.1992 0.2446 0.3537 0.0327  -0.0449 0.0188  113 TRP A NE1 
877  C CE2 . TRP A 111 ? 0.1951 0.2468 0.3530 0.0372  -0.0392 0.0219  113 TRP A CE2 
878  C CE3 . TRP A 111 ? 0.1791 0.2514 0.3602 0.0356  -0.0324 0.0281  113 TRP A CE3 
879  C CZ2 . TRP A 111 ? 0.2161 0.2641 0.3659 0.0448  -0.0347 0.0231  113 TRP A CZ2 
880  C CZ3 . TRP A 111 ? 0.2098 0.2794 0.3847 0.0431  -0.0276 0.0301  113 TRP A CZ3 
881  C CH2 . TRP A 111 ? 0.2256 0.2830 0.3843 0.0479  -0.0283 0.0273  113 TRP A CH2 
882  N N   . LEU A 112 ? 0.1873 0.2834 0.4025 0.0143  -0.0405 0.0254  114 LEU A N   
883  C CA  . LEU A 112 ? 0.1965 0.3011 0.4234 0.0090  -0.0415 0.0251  114 LEU A CA  
884  C C   . LEU A 112 ? 0.1894 0.3001 0.4277 0.0095  -0.0378 0.0278  114 LEU A C   
885  O O   . LEU A 112 ? 0.1929 0.3056 0.4335 0.0150  -0.0340 0.0322  114 LEU A O   
886  C CB  . LEU A 112 ? 0.1974 0.3070 0.4276 0.0087  -0.0444 0.0268  114 LEU A CB  
887  C CG  . LEU A 112 ? 0.2106 0.3280 0.4508 0.0026  -0.0475 0.0256  114 LEU A CG  
888  C CD1 . LEU A 112 ? 0.2023 0.3161 0.4360 -0.0036 -0.0501 0.0202  114 LEU A CD1 
889  C CD2 . LEU A 112 ? 0.2548 0.3777 0.4993 0.0033  -0.0513 0.0289  114 LEU A CD2 
890  N N   . ILE A 113 ? 0.1573 0.2705 0.4032 0.0041  -0.0383 0.0255  115 ILE A N   
891  C CA  . ILE A 113 ? 0.1680 0.2878 0.4283 0.0031  -0.0358 0.0280  115 ILE A CA  
892  C C   . ILE A 113 ? 0.1318 0.2578 0.4022 -0.0028 -0.0395 0.0256  115 ILE A C   
893  O O   . ILE A 113 ? 0.0843 0.2078 0.3515 -0.0080 -0.0423 0.0201  115 ILE A O   
894  C CB  . ILE A 113 ? 0.2270 0.3439 0.4900 0.0013  -0.0337 0.0270  115 ILE A CB  
895  C CG1 . ILE A 113 ? 0.2756 0.3841 0.5254 0.0047  -0.0330 0.0269  115 ILE A CG1 
896  C CG2 . ILE A 113 ? 0.2661 0.3888 0.5426 0.0024  -0.0299 0.0320  115 ILE A CG2 
897  C CD1 . ILE A 113 ? 0.3260 0.4300 0.5738 0.0011  -0.0348 0.0230  115 ILE A CD1 
898  N N   . THR A 114 ? 0.1504 0.2840 0.4330 -0.0021 -0.0394 0.0296  116 THR A N   
899  C CA  . THR A 114 ? 0.1919 0.3313 0.4852 -0.0078 -0.0439 0.0276  116 THR A CA  
900  C C   . THR A 114 ? 0.2203 0.3642 0.5303 -0.0095 -0.0414 0.0295  116 THR A C   
901  O O   . THR A 114 ? 0.2305 0.3780 0.5484 -0.0049 -0.0366 0.0361  116 THR A O   
902  C CB  . THR A 114 ? 0.2512 0.3963 0.5483 -0.0065 -0.0476 0.0309  116 THR A CB  
903  O OG1 . THR A 114 ? 0.2700 0.4101 0.5518 -0.0040 -0.0494 0.0302  116 THR A OG1 
904  C CG2 . THR A 114 ? 0.2872 0.4370 0.5931 -0.0134 -0.0543 0.0279  116 THR A CG2 
905  N N   . LEU A 115 ? 0.2207 0.3637 0.5357 -0.0159 -0.0442 0.0239  117 LEU A N   
906  C CA  . LEU A 115 ? 0.2345 0.3810 0.5669 -0.0191 -0.0433 0.0244  117 LEU A CA  
907  C C   . LEU A 115 ? 0.2660 0.4187 0.6106 -0.0236 -0.0493 0.0236  117 LEU A C   
908  O O   . LEU A 115 ? 0.2691 0.4205 0.6049 -0.0268 -0.0550 0.0187  117 LEU A O   
909  C CB  . LEU A 115 ? 0.2514 0.3914 0.5806 -0.0235 -0.0432 0.0171  117 LEU A CB  
910  C CG  . LEU A 115 ? 0.2777 0.4113 0.5975 -0.0204 -0.0388 0.0174  117 LEU A CG  
911  C CD1 . LEU A 115 ? 0.2552 0.3837 0.5755 -0.0248 -0.0387 0.0106  117 LEU A CD1 
912  C CD2 . LEU A 115 ? 0.2980 0.4339 0.6253 -0.0157 -0.0338 0.0253  117 LEU A CD2 
913  N N   . ASN A 116 ? 0.2777 0.4370 0.6428 -0.0241 -0.0484 0.0285  118 ASN A N   
914  C CA  . ASN A 116 ? 0.3105 0.4752 0.6900 -0.0296 -0.0553 0.0271  118 ASN A CA  
915  C C   . ASN A 116 ? 0.3271 0.4867 0.7095 -0.0365 -0.0584 0.0183  118 ASN A C   
916  O O   . ASN A 116 ? 0.3107 0.4642 0.6883 -0.0365 -0.0540 0.0150  118 ASN A O   
917  C CB  . ASN A 116 ? 0.3277 0.5021 0.7307 -0.0276 -0.0534 0.0365  118 ASN A CB  
918  C CG  . ASN A 116 ? 0.4041 0.5858 0.8210 -0.0313 -0.0617 0.0376  118 ASN A CG  
919  O OD1 . ASN A 116 ? 0.4288 0.6081 0.8405 -0.0373 -0.0704 0.0303  118 ASN A OD1 
920  N ND2 . ASN A 116 ? 0.4153 0.6064 0.8507 -0.0279 -0.0593 0.0472  118 ASN A ND2 
921  N N   . LYS A 117 ? 0.3490 0.5108 0.7394 -0.0424 -0.0663 0.0143  119 LYS A N   
922  C CA  . LYS A 117 ? 0.3811 0.5374 0.7735 -0.0494 -0.0704 0.0047  119 LYS A CA  
923  C C   . LYS A 117 ? 0.3809 0.5344 0.7861 -0.0496 -0.0644 0.0046  119 LYS A C   
924  O O   . LYS A 117 ? 0.3777 0.5233 0.7753 -0.0520 -0.0628 -0.0034 119 LYS A O   
925  C CB  . LYS A 117 ? 0.4085 0.5697 0.8159 -0.0550 -0.0799 0.0036  119 LYS A CB  
926  C CG  . LYS A 117 ? 0.4834 0.6471 0.8802 -0.0563 -0.0884 0.0031  119 LYS A CG  
927  C CD  . LYS A 117 ? 0.5589 0.7300 0.9779 -0.0608 -0.0975 0.0058  119 LYS A CD  
928  C CE  . LYS A 117 ? 0.6226 0.7967 1.0337 -0.0627 -0.1077 0.0059  119 LYS A CE  
929  N NZ  . LYS A 117 ? 0.6626 0.8431 1.0961 -0.0682 -0.1182 0.0075  119 LYS A NZ  
930  N N   . GLN A 118 ? 0.3819 0.5420 0.8068 -0.0468 -0.0606 0.0142  120 GLN A N   
931  C CA  . GLN A 118 ? 0.3872 0.5461 0.8274 -0.0468 -0.0550 0.0168  120 GLN A CA  
932  C C   . GLN A 118 ? 0.3697 0.5222 0.7954 -0.0428 -0.0481 0.0163  120 GLN A C   
933  O O   . GLN A 118 ? 0.3513 0.4987 0.7827 -0.0445 -0.0456 0.0133  120 GLN A O   
934  C CB  . GLN A 118 ? 0.4276 0.5957 0.8883 -0.0434 -0.0511 0.0294  120 GLN A CB  
935  C CG  . GLN A 118 ? 0.5081 0.6817 0.9953 -0.0485 -0.0560 0.0313  120 GLN A CG  
936  C CD  . GLN A 118 ? 0.5914 0.7752 1.0978 -0.0443 -0.0510 0.0450  120 GLN A CD  
937  O OE1 . GLN A 118 ? 0.6384 0.8270 1.1372 -0.0384 -0.0472 0.0516  120 GLN A OE1 
938  N NE2 . GLN A 118 ? 0.5797 0.7669 1.1121 -0.0471 -0.0502 0.0497  120 GLN A NE2 
939  N N   . GLN A 119 ? 0.3613 0.5138 0.7694 -0.0375 -0.0456 0.0194  121 GLN A N   
940  C CA  . GLN A 119 ? 0.3553 0.5022 0.7505 -0.0335 -0.0400 0.0201  121 GLN A CA  
941  C C   . GLN A 119 ? 0.3415 0.4802 0.7221 -0.0364 -0.0414 0.0100  121 GLN A C   
942  O O   . GLN A 119 ? 0.3380 0.4721 0.7109 -0.0339 -0.0376 0.0101  121 GLN A O   
943  C CB  . GLN A 119 ? 0.3657 0.5149 0.7486 -0.0267 -0.0369 0.0271  121 GLN A CB  
944  C CG  . GLN A 119 ? 0.3700 0.5272 0.7670 -0.0231 -0.0335 0.0375  121 GLN A CG  
945  C CD  . GLN A 119 ? 0.4195 0.5779 0.8028 -0.0164 -0.0305 0.0426  121 GLN A CD  
946  O OE1 . GLN A 119 ? 0.3888 0.5490 0.7655 -0.0158 -0.0338 0.0412  121 GLN A OE1 
947  N NE2 . GLN A 119 ? 0.4690 0.6258 0.8472 -0.0110 -0.0243 0.0485  121 GLN A NE2 
948  N N   . ARG A 120 ? 0.3399 0.4766 0.7166 -0.0415 -0.0466 0.0014  122 ARG A N   
949  C CA  . ARG A 120 ? 0.3627 0.4914 0.7284 -0.0445 -0.0463 -0.0083 122 ARG A CA  
950  C C   . ARG A 120 ? 0.3624 0.4869 0.7412 -0.0456 -0.0420 -0.0100 122 ARG A C   
951  O O   . ARG A 120 ? 0.3594 0.4792 0.7318 -0.0438 -0.0380 -0.0114 122 ARG A O   
952  C CB  . ARG A 120 ? 0.3884 0.5152 0.7485 -0.0502 -0.0523 -0.0173 122 ARG A CB  
953  C CG  . ARG A 120 ? 0.4650 0.5832 0.8121 -0.0526 -0.0501 -0.0273 122 ARG A CG  
954  C CD  . ARG A 120 ? 0.5164 0.6319 0.8514 -0.0573 -0.0556 -0.0358 122 ARG A CD  
955  N NE  . ARG A 120 ? 0.5428 0.6599 0.8590 -0.0557 -0.0582 -0.0336 122 ARG A NE  
956  C CZ  . ARG A 120 ? 0.5821 0.6983 0.8857 -0.0592 -0.0645 -0.0382 122 ARG A CZ  
957  N NH1 . ARG A 120 ? 0.5821 0.6955 0.8885 -0.0648 -0.0693 -0.0461 122 ARG A NH1 
958  N NH2 . ARG A 120 ? 0.5918 0.7095 0.8797 -0.0573 -0.0665 -0.0350 122 ARG A NH2 
959  N N   . ARG A 121 ? 0.3468 0.4734 0.7457 -0.0485 -0.0432 -0.0094 123 ARG A N   
960  C CA  . ARG A 121 ? 0.3483 0.4709 0.7619 -0.0497 -0.0398 -0.0108 123 ARG A CA  
961  C C   . ARG A 121 ? 0.3208 0.4449 0.7377 -0.0444 -0.0346 -0.0009 123 ARG A C   
962  O O   . ARG A 121 ? 0.3328 0.4519 0.7491 -0.0437 -0.0314 -0.0026 123 ARG A O   
963  C CB  . ARG A 121 ? 0.4102 0.5347 0.8462 -0.0541 -0.0430 -0.0114 123 ARG A CB  
964  C CG  . ARG A 121 ? 0.5082 0.6286 0.9408 -0.0602 -0.0489 -0.0234 123 ARG A CG  
965  C CD  . ARG A 121 ? 0.5814 0.6964 1.0331 -0.0646 -0.0492 -0.0294 123 ARG A CD  
966  N NE  . ARG A 121 ? 0.6406 0.7491 1.0854 -0.0702 -0.0542 -0.0427 123 ARG A NE  
967  C CZ  . ARG A 121 ? 0.6753 0.7760 1.1013 -0.0711 -0.0523 -0.0531 123 ARG A CZ  
968  N NH1 . ARG A 121 ? 0.6830 0.7775 1.1015 -0.0762 -0.0570 -0.0651 123 ARG A NH1 
969  N NH2 . ARG A 121 ? 0.6687 0.7679 1.0829 -0.0669 -0.0458 -0.0515 123 ARG A NH2 
970  N N   . SER A 122 ? 0.2993 0.4300 0.7183 -0.0406 -0.0338 0.0093  124 SER A N   
971  C CA  . SER A 122 ? 0.2964 0.4282 0.7177 -0.0356 -0.0291 0.0192  124 SER A CA  
972  C C   . SER A 122 ? 0.2785 0.4072 0.6788 -0.0309 -0.0273 0.0207  124 SER A C   
973  O O   . SER A 122 ? 0.3035 0.4290 0.7041 -0.0287 -0.0248 0.0241  124 SER A O   
974  C CB  . SER A 122 ? 0.3398 0.4797 0.7717 -0.0332 -0.0279 0.0295  124 SER A CB  
975  O OG  . SER A 122 ? 0.3811 0.5250 0.8022 -0.0317 -0.0301 0.0297  124 SER A OG  
976  N N   . ASP A 123 ? 0.2201 0.3492 0.6032 -0.0294 -0.0292 0.0184  125 ASP A N   
977  C CA  . ASP A 123 ? 0.2007 0.3271 0.5657 -0.0246 -0.0279 0.0210  125 ASP A CA  
978  C C   . ASP A 123 ? 0.1746 0.2957 0.5237 -0.0260 -0.0298 0.0131  125 ASP A C   
979  O O   . ASP A 123 ? 0.1810 0.2986 0.5189 -0.0228 -0.0289 0.0148  125 ASP A O   
980  C CB  . ASP A 123 ? 0.2270 0.3582 0.5851 -0.0199 -0.0273 0.0279  125 ASP A CB  
981  C CG  . ASP A 123 ? 0.3363 0.4730 0.7075 -0.0172 -0.0237 0.0375  125 ASP A CG  
982  O OD1 . ASP A 123 ? 0.3557 0.4904 0.7296 -0.0153 -0.0209 0.0424  125 ASP A OD1 
983  O OD2 . ASP A 123 ? 0.3790 0.5222 0.7580 -0.0169 -0.0238 0.0407  125 ASP A OD2 
984  N N   . LEU A 124 ? 0.1514 0.2715 0.4992 -0.0305 -0.0322 0.0050  126 LEU A N   
985  C CA  . LEU A 124 ? 0.1405 0.2561 0.4720 -0.0315 -0.0331 -0.0013 126 LEU A CA  
986  C C   . LEU A 124 ? 0.1191 0.2289 0.4491 -0.0311 -0.0303 -0.0032 126 LEU A C   
987  O O   . LEU A 124 ? 0.1283 0.2355 0.4462 -0.0286 -0.0302 -0.0018 126 LEU A O   
988  C CB  . LEU A 124 ? 0.1328 0.2477 0.4630 -0.0368 -0.0358 -0.0098 126 LEU A CB  
989  C CG  . LEU A 124 ? 0.1531 0.2637 0.4655 -0.0382 -0.0363 -0.0160 126 LEU A CG  
990  C CD1 . LEU A 124 ? 0.1661 0.2787 0.4648 -0.0353 -0.0388 -0.0118 126 LEU A CD1 
991  C CD2 . LEU A 124 ? 0.1690 0.2779 0.4794 -0.0436 -0.0385 -0.0247 126 LEU A CD2 
992  N N   . ASN A 125 ? 0.1155 0.2233 0.4595 -0.0336 -0.0281 -0.0060 127 ASN A N   
993  C CA  . ASN A 125 ? 0.1285 0.2313 0.4742 -0.0335 -0.0255 -0.0078 127 ASN A CA  
994  C C   . ASN A 125 ? 0.1319 0.2344 0.4760 -0.0291 -0.0256 0.0005  127 ASN A C   
995  O O   . ASN A 125 ? 0.1126 0.2118 0.4492 -0.0278 -0.0256 0.0005  127 ASN A O   
996  C CB  . ASN A 125 ? 0.1754 0.2761 0.5383 -0.0367 -0.0231 -0.0123 127 ASN A CB  
997  C CG  . ASN A 125 ? 0.2444 0.3431 0.6055 -0.0413 -0.0229 -0.0226 127 ASN A CG  
998  O OD1 . ASN A 125 ? 0.2584 0.3570 0.6324 -0.0441 -0.0231 -0.0258 127 ASN A OD1 
999  N ND2 . ASN A 125 ? 0.2605 0.3569 0.6057 -0.0423 -0.0226 -0.0281 127 ASN A ND2 
1000 N N   . ARG A 126 ? 0.1470 0.2530 0.4982 -0.0268 -0.0258 0.0079  128 ARG A N   
1001 C CA  . ARG A 126 ? 0.1325 0.2379 0.4803 -0.0224 -0.0261 0.0162  128 ARG A CA  
1002 C C   . ARG A 126 ? 0.1304 0.2343 0.4582 -0.0191 -0.0280 0.0172  128 ARG A C   
1003 O O   . ARG A 126 ? 0.1216 0.2213 0.4424 -0.0174 -0.0293 0.0184  128 ARG A O   
1004 C CB  . ARG A 126 ? 0.1289 0.2388 0.4867 -0.0207 -0.0249 0.0239  128 ARG A CB  
1005 C CG  . ARG A 126 ? 0.1797 0.2889 0.5299 -0.0156 -0.0249 0.0330  128 ARG A CG  
1006 C CD  . ARG A 126 ? 0.2343 0.3385 0.5857 -0.0152 -0.0263 0.0347  128 ARG A CD  
1007 N NE  . ARG A 126 ? 0.2214 0.3256 0.5936 -0.0183 -0.0251 0.0346  128 ARG A NE  
1008 C CZ  . ARG A 126 ? 0.2230 0.3235 0.6021 -0.0188 -0.0262 0.0352  128 ARG A CZ  
1009 N NH1 . ARG A 126 ? 0.1975 0.2941 0.5647 -0.0169 -0.0292 0.0361  128 ARG A NH1 
1010 N NH2 . ARG A 126 ? 0.1957 0.2962 0.5952 -0.0213 -0.0247 0.0352  128 ARG A NH2 
1011 N N   . PHE A 127 ? 0.1250 0.2322 0.4453 -0.0182 -0.0286 0.0169  129 PHE A N   
1012 C CA  . PHE A 127 ? 0.1589 0.2642 0.4617 -0.0146 -0.0301 0.0183  129 PHE A CA  
1013 C C   . PHE A 127 ? 0.1285 0.2291 0.4220 -0.0165 -0.0317 0.0125  129 PHE A C   
1014 O O   . PHE A 127 ? 0.1271 0.2237 0.4092 -0.0138 -0.0333 0.0140  129 PHE A O   
1015 C CB  . PHE A 127 ? 0.1668 0.2768 0.4660 -0.0133 -0.0303 0.0194  129 PHE A CB  
1016 C CG  . PHE A 127 ? 0.1963 0.3112 0.5012 -0.0099 -0.0281 0.0267  129 PHE A CG  
1017 C CD1 . PHE A 127 ? 0.2157 0.3314 0.5305 -0.0090 -0.0258 0.0320  129 PHE A CD1 
1018 C CD2 . PHE A 127 ? 0.2147 0.3337 0.5158 -0.0073 -0.0279 0.0290  129 PHE A CD2 
1019 C CE1 . PHE A 127 ? 0.2321 0.3526 0.5521 -0.0057 -0.0227 0.0396  129 PHE A CE1 
1020 C CE2 . PHE A 127 ? 0.2268 0.3508 0.5342 -0.0037 -0.0246 0.0363  129 PHE A CE2 
1021 C CZ  . PHE A 127 ? 0.2278 0.3527 0.5445 -0.0030 -0.0217 0.0416  129 PHE A CZ  
1022 N N   . TRP A 128 ? 0.1222 0.2228 0.4203 -0.0211 -0.0310 0.0059  130 TRP A N   
1023 C CA  . TRP A 128 ? 0.1334 0.2299 0.4236 -0.0229 -0.0311 0.0011  130 TRP A CA  
1024 C C   . TRP A 128 ? 0.1497 0.2420 0.4438 -0.0223 -0.0308 0.0025  130 TRP A C   
1025 O O   . TRP A 128 ? 0.1607 0.2494 0.4457 -0.0211 -0.0325 0.0029  130 TRP A O   
1026 C CB  . TRP A 128 ? 0.1197 0.2167 0.4125 -0.0277 -0.0295 -0.0064 130 TRP A CB  
1027 C CG  . TRP A 128 ? 0.1196 0.2129 0.4038 -0.0295 -0.0284 -0.0107 130 TRP A CG  
1028 C CD1 . TRP A 128 ? 0.1454 0.2362 0.4345 -0.0326 -0.0247 -0.0163 130 TRP A CD1 
1029 C CD2 . TRP A 128 ? 0.1381 0.2298 0.4076 -0.0283 -0.0303 -0.0098 130 TRP A CD2 
1030 N NE1 . TRP A 128 ? 0.1645 0.2527 0.4430 -0.0334 -0.0237 -0.0180 130 TRP A NE1 
1031 C CE2 . TRP A 128 ? 0.1472 0.2358 0.4138 -0.0310 -0.0275 -0.0140 130 TRP A CE2 
1032 C CE3 . TRP A 128 ? 0.1384 0.2306 0.3978 -0.0249 -0.0336 -0.0053 130 TRP A CE3 
1033 C CZ2 . TRP A 128 ? 0.1533 0.2397 0.4075 -0.0308 -0.0284 -0.0135 130 TRP A CZ2 
1034 C CZ3 . TRP A 128 ? 0.1272 0.2166 0.3747 -0.0247 -0.0349 -0.0054 130 TRP A CZ3 
1035 C CH2 . TRP A 128 ? 0.1438 0.2306 0.3889 -0.0278 -0.0325 -0.0091 130 TRP A CH2 
1036 N N   . LEU A 129 ? 0.1401 0.2327 0.4491 -0.0232 -0.0292 0.0035  131 LEU A N   
1037 C CA  . LEU A 129 ? 0.1486 0.2378 0.4636 -0.0225 -0.0299 0.0060  131 LEU A CA  
1038 C C   . LEU A 129 ? 0.1472 0.2340 0.4517 -0.0183 -0.0339 0.0123  131 LEU A C   
1039 O O   . LEU A 129 ? 0.1563 0.2391 0.4568 -0.0179 -0.0364 0.0128  131 LEU A O   
1040 C CB  . LEU A 129 ? 0.1555 0.2457 0.4895 -0.0237 -0.0280 0.0073  131 LEU A CB  
1041 C CG  . LEU A 129 ? 0.1815 0.2687 0.5240 -0.0228 -0.0297 0.0114  131 LEU A CG  
1042 C CD1 . LEU A 129 ? 0.1919 0.2763 0.5349 -0.0246 -0.0289 0.0074  131 LEU A CD1 
1043 C CD2 . LEU A 129 ? 0.1908 0.2793 0.5527 -0.0237 -0.0280 0.0137  131 LEU A CD2 
1044 N N   . GLU A 130 ? 0.1284 0.2176 0.4287 -0.0152 -0.0343 0.0171  132 GLU A N   
1045 C CA  . GLU A 130 ? 0.1455 0.2312 0.4334 -0.0108 -0.0375 0.0225  132 GLU A CA  
1046 C C   . GLU A 130 ? 0.1419 0.2236 0.4138 -0.0095 -0.0401 0.0200  132 GLU A C   
1047 O O   . GLU A 130 ? 0.1409 0.2171 0.4046 -0.0076 -0.0440 0.0218  132 GLU A O   
1048 C CB  . GLU A 130 ? 0.1753 0.2642 0.4606 -0.0074 -0.0360 0.0280  132 GLU A CB  
1049 C CG  . GLU A 130 ? 0.2013 0.2938 0.5027 -0.0083 -0.0337 0.0321  132 GLU A CG  
1050 C CD  . GLU A 130 ? 0.2298 0.3188 0.5370 -0.0083 -0.0363 0.0360  132 GLU A CD  
1051 O OE1 . GLU A 130 ? 0.2789 0.3625 0.5741 -0.0062 -0.0404 0.0374  132 GLU A OE1 
1052 O OE2 . GLU A 130 ? 0.2075 0.2987 0.5318 -0.0104 -0.0347 0.0378  132 GLU A OE2 
1053 N N   . THR A 131 ? 0.1423 0.2265 0.4105 -0.0107 -0.0385 0.0161  133 THR A N   
1054 C CA  . THR A 131 ? 0.1524 0.2332 0.4081 -0.0103 -0.0405 0.0136  133 THR A CA  
1055 C C   . THR A 131 ? 0.1514 0.2277 0.4093 -0.0130 -0.0422 0.0113  133 THR A C   
1056 O O   . THR A 131 ? 0.1212 0.1923 0.3705 -0.0114 -0.0458 0.0122  133 THR A O   
1057 C CB  . THR A 131 ? 0.1475 0.2322 0.4011 -0.0120 -0.0387 0.0104  133 THR A CB  
1058 O OG1 . THR A 131 ? 0.1557 0.2450 0.4097 -0.0094 -0.0376 0.0134  133 THR A OG1 
1059 C CG2 . THR A 131 ? 0.1360 0.2175 0.3779 -0.0116 -0.0407 0.0088  133 THR A CG2 
1060 N N   . LEU A 132 ? 0.1648 0.2431 0.4352 -0.0169 -0.0393 0.0082  134 LEU A N   
1061 C CA  . LEU A 132 ? 0.1549 0.2303 0.4309 -0.0194 -0.0394 0.0065  134 LEU A CA  
1062 C C   . LEU A 132 ? 0.1460 0.2173 0.4255 -0.0178 -0.0439 0.0107  134 LEU A C   
1063 O O   . LEU A 132 ? 0.1464 0.2139 0.4251 -0.0186 -0.0466 0.0108  134 LEU A O   
1064 C CB  . LEU A 132 ? 0.1496 0.2278 0.4395 -0.0231 -0.0342 0.0024  134 LEU A CB  
1065 C CG  . LEU A 132 ? 0.1451 0.2261 0.4308 -0.0255 -0.0303 -0.0029 134 LEU A CG  
1066 C CD1 . LEU A 132 ? 0.1247 0.2070 0.4233 -0.0287 -0.0252 -0.0075 134 LEU A CD1 
1067 C CD2 . LEU A 132 ? 0.1598 0.2389 0.4337 -0.0265 -0.0303 -0.0047 134 LEU A CD2 
1068 N N   . LEU A 133 ? 0.1475 0.2197 0.4312 -0.0159 -0.0451 0.0146  135 LEU A N   
1069 C CA  . LEU A 133 ? 0.1517 0.2198 0.4370 -0.0145 -0.0505 0.0192  135 LEU A CA  
1070 C C   . LEU A 133 ? 0.1424 0.2044 0.4097 -0.0113 -0.0562 0.0207  135 LEU A C   
1071 O O   . LEU A 133 ? 0.1509 0.2079 0.4182 -0.0116 -0.0618 0.0222  135 LEU A O   
1072 C CB  . LEU A 133 ? 0.1349 0.2053 0.4281 -0.0133 -0.0502 0.0238  135 LEU A CB  
1073 C CG  . LEU A 133 ? 0.1328 0.2078 0.4462 -0.0163 -0.0453 0.0223  135 LEU A CG  
1074 C CD1 . LEU A 133 ? 0.1226 0.1992 0.4450 -0.0150 -0.0459 0.0283  135 LEU A CD1 
1075 C CD2 . LEU A 133 ? 0.1423 0.2162 0.4701 -0.0193 -0.0451 0.0204  135 LEU A CD2 
1076 N N   . CYS A 134 ? 0.1360 0.1982 0.3897 -0.0085 -0.0549 0.0203  136 CYS A N   
1077 C CA  . CYS A 134 ? 0.1700 0.2260 0.4060 -0.0050 -0.0589 0.0206  136 CYS A CA  
1078 C C   . CYS A 134 ? 0.1668 0.2185 0.4009 -0.0070 -0.0618 0.0176  136 CYS A C   
1079 O O   . CYS A 134 ? 0.1825 0.2267 0.4073 -0.0054 -0.0678 0.0181  136 CYS A O   
1080 C CB  . CYS A 134 ? 0.1930 0.2517 0.4189 -0.0016 -0.0552 0.0205  136 CYS A CB  
1081 S SG  . CYS A 134 ? 0.2252 0.2867 0.4486 0.0024  -0.0526 0.0258  136 CYS A SG  
1082 N N   . LEU A 135 ? 0.1504 0.2065 0.3924 -0.0106 -0.0574 0.0145  137 LEU A N   
1083 C CA  . LEU A 135 ? 0.1668 0.2200 0.4084 -0.0129 -0.0585 0.0124  137 LEU A CA  
1084 C C   . LEU A 135 ? 0.1658 0.2163 0.4192 -0.0155 -0.0620 0.0136  137 LEU A C   
1085 O O   . LEU A 135 ? 0.1761 0.2201 0.4252 -0.0150 -0.0681 0.0146  137 LEU A O   
1086 C CB  . LEU A 135 ? 0.1478 0.2062 0.3922 -0.0158 -0.0525 0.0092  137 LEU A CB  
1087 C CG  . LEU A 135 ? 0.1371 0.1958 0.3688 -0.0141 -0.0517 0.0082  137 LEU A CG  
1088 C CD1 . LEU A 135 ? 0.1615 0.2210 0.3849 -0.0097 -0.0523 0.0099  137 LEU A CD1 
1089 C CD2 . LEU A 135 ? 0.1297 0.1938 0.3641 -0.0174 -0.0465 0.0054  137 LEU A CD2 
1090 N N   . ILE A 136 ? 0.1699 0.2250 0.4395 -0.0182 -0.0584 0.0136  138 ILE A N   
1091 C CA  . ILE A 136 ? 0.1634 0.2170 0.4480 -0.0208 -0.0609 0.0151  138 ILE A CA  
1092 C C   . ILE A 136 ? 0.1678 0.2163 0.4514 -0.0190 -0.0696 0.0191  138 ILE A C   
1093 O O   . ILE A 136 ? 0.1867 0.2316 0.4776 -0.0207 -0.0751 0.0208  138 ILE A O   
1094 C CB  . ILE A 136 ? 0.1540 0.2134 0.4579 -0.0237 -0.0540 0.0139  138 ILE A CB  
1095 C CG1 . ILE A 136 ? 0.1448 0.2068 0.4555 -0.0224 -0.0538 0.0159  138 ILE A CG1 
1096 C CG2 . ILE A 136 ? 0.1606 0.2237 0.4615 -0.0255 -0.0457 0.0091  138 ILE A CG2 
1097 C CD1 . ILE A 136 ? 0.1854 0.2519 0.5137 -0.0246 -0.0476 0.0143  138 ILE A CD1 
1098 N N   . GLY A 137 ? 0.1716 0.2200 0.4470 -0.0159 -0.0711 0.0211  139 GLY A N   
1099 C CA  . GLY A 137 ? 0.1930 0.2358 0.4633 -0.0139 -0.0796 0.0251  139 GLY A CA  
1100 C C   . GLY A 137 ? 0.2072 0.2413 0.4584 -0.0114 -0.0867 0.0245  139 GLY A C   
1101 O O   . GLY A 137 ? 0.2269 0.2551 0.4717 -0.0100 -0.0946 0.0272  139 GLY A O   
1102 N N   . GLU A 138 ? 0.2245 0.2569 0.4658 -0.0108 -0.0845 0.0210  140 GLU A N   
1103 C CA  . GLU A 138 ? 0.2265 0.2495 0.4492 -0.0078 -0.0906 0.0198  140 GLU A CA  
1104 C C   . GLU A 138 ? 0.2452 0.2641 0.4493 -0.0026 -0.0925 0.0210  140 GLU A C   
1105 O O   . GLU A 138 ? 0.2463 0.2561 0.4388 -0.0008 -0.1006 0.0215  140 GLU A O   
1106 C CB  . GLU A 138 ? 0.2250 0.2410 0.4527 -0.0104 -0.0998 0.0202  140 GLU A CB  
1107 C CG  . GLU A 138 ? 0.2511 0.2710 0.4969 -0.0152 -0.0970 0.0197  140 GLU A CG  
1108 C CD  . GLU A 138 ? 0.2975 0.3172 0.5381 -0.0155 -0.0927 0.0169  140 GLU A CD  
1109 O OE1 . GLU A 138 ? 0.2707 0.2824 0.4967 -0.0131 -0.0973 0.0154  140 GLU A OE1 
1110 O OE2 . GLU A 138 ? 0.2723 0.2990 0.5230 -0.0181 -0.0850 0.0163  140 GLU A OE2 
1111 N N   . SER A 139 ? 0.2462 0.2712 0.4472 -0.0002 -0.0849 0.0215  141 SER A N   
1112 C CA  . SER A 139 ? 0.2597 0.2837 0.4479 0.0044  -0.0838 0.0242  141 SER A CA  
1113 C C   . SER A 139 ? 0.2515 0.2677 0.4174 0.0097  -0.0846 0.0221  141 SER A C   
1114 O O   . SER A 139 ? 0.2216 0.2357 0.3748 0.0140  -0.0835 0.0242  141 SER A O   
1115 C CB  . SER A 139 ? 0.2860 0.3204 0.4837 0.0044  -0.0751 0.0260  141 SER A CB  
1116 O OG  . SER A 139 ? 0.2800 0.3204 0.4977 0.0000  -0.0739 0.0275  141 SER A OG  
1117 N N   . PHE A 140 ? 0.2743 0.2860 0.4359 0.0096  -0.0862 0.0182  142 PHE A N   
1118 C CA  . PHE A 140 ? 0.2983 0.3028 0.4411 0.0149  -0.0859 0.0157  142 PHE A CA  
1119 C C   . PHE A 140 ? 0.3095 0.3006 0.4401 0.0156  -0.0955 0.0131  142 PHE A C   
1120 O O   . PHE A 140 ? 0.2955 0.2793 0.4134 0.0191  -0.0960 0.0098  142 PHE A O   
1121 C CB  . PHE A 140 ? 0.2988 0.3081 0.4460 0.0148  -0.0801 0.0137  142 PHE A CB  
1122 C CG  . PHE A 140 ? 0.2527 0.2749 0.4128 0.0131  -0.0722 0.0158  142 PHE A CG  
1123 C CD1 . PHE A 140 ? 0.2523 0.2792 0.4093 0.0166  -0.0668 0.0186  142 PHE A CD1 
1124 C CD2 . PHE A 140 ? 0.2530 0.2819 0.4283 0.0079  -0.0703 0.0151  142 PHE A CD2 
1125 C CE1 . PHE A 140 ? 0.2568 0.2949 0.4271 0.0146  -0.0606 0.0203  142 PHE A CE1 
1126 C CE2 . PHE A 140 ? 0.2489 0.2881 0.4349 0.0061  -0.0639 0.0161  142 PHE A CE2 
1127 C CZ  . PHE A 140 ? 0.2482 0.2918 0.4323 0.0093  -0.0597 0.0186  142 PHE A CZ  
1128 N N   . ASP A 141 ? 0.3294 0.3168 0.4645 0.0124  -0.1038 0.0146  143 ASP A N   
1129 C CA  . ASP A 141 ? 0.3706 0.3443 0.4934 0.0128  -0.1147 0.0120  143 ASP A CA  
1130 C C   . ASP A 141 ? 0.3753 0.3444 0.5030 0.0106  -0.1175 0.0082  143 ASP A C   
1131 O O   . ASP A 141 ? 0.3811 0.3588 0.5276 0.0063  -0.1138 0.0095  143 ASP A O   
1132 C CB  . ASP A 141 ? 0.4548 0.4192 0.5508 0.0195  -0.1155 0.0108  143 ASP A CB  
1133 C CG  . ASP A 141 ? 0.6401 0.6073 0.7321 0.0205  -0.1156 0.0159  143 ASP A CG  
1134 O OD1 . ASP A 141 ? 0.6516 0.6223 0.7581 0.0158  -0.1212 0.0195  143 ASP A OD1 
1135 O OD2 . ASP A 141 ? 0.7278 0.6940 0.8032 0.0261  -0.1099 0.0169  143 ASP A OD2 
1136 N N   . ASP A 142 ? 0.3878 0.3438 0.5002 0.0131  -0.1234 0.0039  144 ASP A N   
1137 C CA  . ASP A 142 ? 0.4148 0.3675 0.5358 0.0103  -0.1258 0.0015  144 ASP A CA  
1138 C C   . ASP A 142 ? 0.3967 0.3584 0.5238 0.0112  -0.1152 0.0019  144 ASP A C   
1139 O O   . ASP A 142 ? 0.4022 0.3665 0.5422 0.0074  -0.1146 0.0023  144 ASP A O   
1140 C CB  . ASP A 142 ? 0.5031 0.4393 0.6082 0.0128  -0.1342 -0.0036 144 ASP A CB  
1141 C CG  . ASP A 142 ? 0.6375 0.5625 0.7377 0.0107  -0.1477 -0.0048 144 ASP A CG  
1142 O OD1 . ASP A 142 ? 0.6480 0.5783 0.7578 0.0073  -0.1512 -0.0008 144 ASP A OD1 
1143 O OD2 . ASP A 142 ? 0.7213 0.6317 0.8086 0.0123  -0.1553 -0.0097 144 ASP A OD2 
1144 N N   . TYR A 143 ? 0.3644 0.3311 0.4824 0.0161  -0.1069 0.0023  145 TYR A N   
1145 C CA  . TYR A 143 ? 0.3317 0.3065 0.4542 0.0173  -0.0981 0.0028  145 TYR A CA  
1146 C C   . TYR A 143 ? 0.2753 0.2636 0.4171 0.0119  -0.0930 0.0059  145 TYR A C   
1147 O O   . TYR A 143 ? 0.2504 0.2453 0.3965 0.0119  -0.0871 0.0063  145 TYR A O   
1148 C CB  . TYR A 143 ? 0.3450 0.3220 0.4551 0.0238  -0.0911 0.0032  145 TYR A CB  
1149 C CG  . TYR A 143 ? 0.3748 0.3383 0.4636 0.0300  -0.0940 -0.0003 145 TYR A CG  
1150 C CD1 . TYR A 143 ? 0.4121 0.3641 0.4943 0.0314  -0.0987 -0.0045 145 TYR A CD1 
1151 C CD2 . TYR A 143 ? 0.4077 0.3691 0.4827 0.0343  -0.0923 0.0005  145 TYR A CD2 
1152 C CE1 . TYR A 143 ? 0.4414 0.3798 0.5030 0.0374  -0.1009 -0.0088 145 TYR A CE1 
1153 C CE2 . TYR A 143 ? 0.4469 0.3950 0.4998 0.0403  -0.0943 -0.0033 145 TYR A CE2 
1154 C CZ  . TYR A 143 ? 0.4855 0.4219 0.5315 0.0420  -0.0984 -0.0085 145 TYR A CZ  
1155 O OH  . TYR A 143 ? 0.5729 0.4948 0.5957 0.0484  -0.0999 -0.0133 145 TYR A OH  
1156 N N   . SER A 144 ? 0.2723 0.2644 0.4257 0.0076  -0.0954 0.0079  146 SER A N   
1157 C CA  . SER A 144 ? 0.2450 0.2478 0.4165 0.0024  -0.0907 0.0097  146 SER A CA  
1158 C C   . SER A 144 ? 0.2134 0.2152 0.3921 -0.0010 -0.0914 0.0090  146 SER A C   
1159 O O   . SER A 144 ? 0.2106 0.2206 0.3986 -0.0038 -0.0855 0.0098  146 SER A O   
1160 C CB  . SER A 144 ? 0.2649 0.2711 0.4485 -0.0010 -0.0929 0.0120  146 SER A CB  
1161 O OG  . SER A 144 ? 0.2701 0.2801 0.4502 0.0016  -0.0902 0.0138  146 SER A OG  
1162 N N   . ASP A 145 ? 0.2218 0.2130 0.3958 -0.0008 -0.0983 0.0076  147 ASP A N   
1163 C CA  . ASP A 145 ? 0.2246 0.2146 0.4055 -0.0038 -0.0986 0.0080  147 ASP A CA  
1164 C C   . ASP A 145 ? 0.2123 0.2061 0.3876 -0.0015 -0.0922 0.0078  147 ASP A C   
1165 O O   . ASP A 145 ? 0.2025 0.1998 0.3853 -0.0047 -0.0894 0.0094  147 ASP A O   
1166 C CB  . ASP A 145 ? 0.2973 0.2742 0.4750 -0.0040 -0.1082 0.0065  147 ASP A CB  
1167 C CG  . ASP A 145 ? 0.3945 0.3686 0.5830 -0.0080 -0.1157 0.0076  147 ASP A CG  
1168 O OD1 . ASP A 145 ? 0.4016 0.3848 0.6058 -0.0120 -0.1123 0.0103  147 ASP A OD1 
1169 O OD2 . ASP A 145 ? 0.4755 0.4381 0.6571 -0.0071 -0.1252 0.0057  147 ASP A OD2 
1170 N N   . ASP A 146 ? 0.1950 0.1885 0.3578 0.0041  -0.0896 0.0066  148 ASP A N   
1171 C CA  . ASP A 146 ? 0.2016 0.1998 0.3616 0.0063  -0.0841 0.0072  148 ASP A CA  
1172 C C   . ASP A 146 ? 0.2014 0.2126 0.3699 0.0034  -0.0772 0.0090  148 ASP A C   
1173 O O   . ASP A 146 ? 0.1970 0.2129 0.3652 0.0037  -0.0738 0.0100  148 ASP A O   
1174 C CB  . ASP A 146 ? 0.2264 0.2203 0.3725 0.0134  -0.0830 0.0057  148 ASP A CB  
1175 C CG  . ASP A 146 ? 0.2962 0.2780 0.4345 0.0165  -0.0874 0.0037  148 ASP A CG  
1176 O OD1 . ASP A 146 ? 0.3216 0.2942 0.4598 0.0145  -0.0943 0.0021  148 ASP A OD1 
1177 O OD2 . ASP A 146 ? 0.2265 0.2082 0.3605 0.0206  -0.0843 0.0038  148 ASP A OD2 
1178 N N   . VAL A 147 ? 0.1867 0.2035 0.3628 0.0006  -0.0757 0.0093  149 VAL A N   
1179 C CA  . VAL A 147 ? 0.1879 0.2158 0.3718 -0.0021 -0.0694 0.0100  149 VAL A CA  
1180 C C   . VAL A 147 ? 0.1711 0.2015 0.3626 -0.0072 -0.0678 0.0105  149 VAL A C   
1181 O O   . VAL A 147 ? 0.1638 0.1903 0.3614 -0.0101 -0.0706 0.0109  149 VAL A O   
1182 C CB  . VAL A 147 ? 0.2056 0.2373 0.3961 -0.0031 -0.0684 0.0101  149 VAL A CB  
1183 C CG1 . VAL A 147 ? 0.2248 0.2665 0.4247 -0.0064 -0.0624 0.0099  149 VAL A CG1 
1184 C CG2 . VAL A 147 ? 0.2048 0.2341 0.3860 0.0022  -0.0692 0.0106  149 VAL A CG2 
1185 N N   . CYS A 148 ? 0.1660 0.2030 0.3571 -0.0084 -0.0634 0.0107  150 CYS A N   
1186 C CA  . CYS A 148 ? 0.1729 0.2134 0.3691 -0.0132 -0.0603 0.0113  150 CYS A CA  
1187 C C   . CYS A 148 ? 0.1694 0.2174 0.3731 -0.0164 -0.0551 0.0095  150 CYS A C   
1188 O O   . CYS A 148 ? 0.1633 0.2123 0.3748 -0.0202 -0.0526 0.0092  150 CYS A O   
1189 C CB  . CYS A 148 ? 0.1803 0.2221 0.3692 -0.0126 -0.0596 0.0127  150 CYS A CB  
1190 S SG  . CYS A 148 ? 0.2215 0.2535 0.4034 -0.0087 -0.0653 0.0146  150 CYS A SG  
1191 N N   . GLY A 149 ? 0.1722 0.2253 0.3746 -0.0148 -0.0533 0.0084  151 GLY A N   
1192 C CA  . GLY A 149 ? 0.1458 0.2053 0.3553 -0.0176 -0.0487 0.0062  151 GLY A CA  
1193 C C   . GLY A 149 ? 0.1371 0.2016 0.3452 -0.0154 -0.0479 0.0058  151 GLY A C   
1194 O O   . GLY A 149 ? 0.1353 0.1984 0.3377 -0.0112 -0.0502 0.0076  151 GLY A O   
1195 N N   . ALA A 150 ? 0.1207 0.1907 0.3350 -0.0183 -0.0442 0.0033  152 ALA A N   
1196 C CA  . ALA A 150 ? 0.1389 0.2144 0.3550 -0.0173 -0.0433 0.0029  152 ALA A CA  
1197 C C   . ALA A 150 ? 0.1373 0.2171 0.3534 -0.0214 -0.0409 -0.0003 152 ALA A C   
1198 O O   . ALA A 150 ? 0.1446 0.2234 0.3623 -0.0249 -0.0380 -0.0031 152 ALA A O   
1199 C CB  . ALA A 150 ? 0.1339 0.2104 0.3594 -0.0166 -0.0422 0.0032  152 ALA A CB  
1200 N N   . VAL A 151 ? 0.1485 0.2328 0.3626 -0.0209 -0.0421 0.0000  153 VAL A N   
1201 C CA  . VAL A 151 ? 0.1555 0.2436 0.3681 -0.0247 -0.0416 -0.0033 153 VAL A CA  
1202 C C   . VAL A 151 ? 0.1553 0.2486 0.3769 -0.0252 -0.0415 -0.0045 153 VAL A C   
1203 O O   . VAL A 151 ? 0.1427 0.2385 0.3684 -0.0217 -0.0429 -0.0008 153 VAL A O   
1204 C CB  . VAL A 151 ? 0.1879 0.2769 0.3901 -0.0245 -0.0450 -0.0012 153 VAL A CB  
1205 C CG1 . VAL A 151 ? 0.1976 0.2899 0.3963 -0.0290 -0.0457 -0.0047 153 VAL A CG1 
1206 C CG2 . VAL A 151 ? 0.2119 0.2957 0.4062 -0.0242 -0.0453 0.0008  153 VAL A CG2 
1207 N N   . VAL A 152 ? 0.1536 0.2481 0.3783 -0.0295 -0.0397 -0.0096 154 VAL A N   
1208 C CA  . VAL A 152 ? 0.1686 0.2677 0.4015 -0.0310 -0.0408 -0.0112 154 VAL A CA  
1209 C C   . VAL A 152 ? 0.1710 0.2718 0.3958 -0.0349 -0.0438 -0.0146 154 VAL A C   
1210 O O   . VAL A 152 ? 0.1395 0.2372 0.3566 -0.0384 -0.0419 -0.0196 154 VAL A O   
1211 C CB  . VAL A 152 ? 0.1874 0.2861 0.4335 -0.0324 -0.0372 -0.0142 154 VAL A CB  
1212 C CG1 . VAL A 152 ? 0.2302 0.3247 0.4748 -0.0357 -0.0329 -0.0200 154 VAL A CG1 
1213 C CG2 . VAL A 152 ? 0.1829 0.2859 0.4385 -0.0344 -0.0388 -0.0157 154 VAL A CG2 
1214 N N   . ASN A 153 ? 0.1926 0.2981 0.4189 -0.0341 -0.0484 -0.0117 155 ASN A N   
1215 C CA  . ASN A 153 ? 0.2248 0.3324 0.4455 -0.0380 -0.0530 -0.0146 155 ASN A CA  
1216 C C   . ASN A 153 ? 0.2355 0.3464 0.4691 -0.0408 -0.0545 -0.0179 155 ASN A C   
1217 O O   . ASN A 153 ? 0.2388 0.3545 0.4854 -0.0385 -0.0557 -0.0134 155 ASN A O   
1218 C CB  . ASN A 153 ? 0.2531 0.3639 0.4685 -0.0358 -0.0584 -0.0088 155 ASN A CB  
1219 C CG  . ASN A 153 ? 0.2696 0.3772 0.4764 -0.0320 -0.0573 -0.0042 155 ASN A CG  
1220 O OD1 . ASN A 153 ? 0.2772 0.3854 0.4886 -0.0270 -0.0567 0.0008  155 ASN A OD1 
1221 N ND2 . ASN A 153 ? 0.2885 0.3922 0.4824 -0.0341 -0.0571 -0.0057 155 ASN A ND2 
1222 N N   . VAL A 154 ? 0.2363 0.3439 0.4662 -0.0457 -0.0540 -0.0257 156 VAL A N   
1223 C CA  . VAL A 154 ? 0.2510 0.3599 0.4925 -0.0491 -0.0555 -0.0304 156 VAL A CA  
1224 C C   . VAL A 154 ? 0.2679 0.3800 0.5049 -0.0521 -0.0637 -0.0307 156 VAL A C   
1225 O O   . VAL A 154 ? 0.2552 0.3641 0.4754 -0.0548 -0.0660 -0.0343 156 VAL A O   
1226 C CB  . VAL A 154 ? 0.2708 0.3733 0.5095 -0.0527 -0.0507 -0.0395 156 VAL A CB  
1227 C CG1 . VAL A 154 ? 0.2650 0.3675 0.5176 -0.0560 -0.0522 -0.0448 156 VAL A CG1 
1228 C CG2 . VAL A 154 ? 0.2848 0.3842 0.5267 -0.0497 -0.0430 -0.0383 156 VAL A CG2 
1229 N N   . ARG A 155 ? 0.2768 0.3953 0.5289 -0.0515 -0.0683 -0.0261 157 ARG A N   
1230 C CA  . ARG A 155 ? 0.3023 0.4252 0.5533 -0.0541 -0.0776 -0.0249 157 ARG A CA  
1231 C C   . ARG A 155 ? 0.3167 0.4438 0.5869 -0.0571 -0.0821 -0.0258 157 ARG A C   
1232 O O   . ARG A 155 ? 0.3163 0.4450 0.6028 -0.0553 -0.0776 -0.0238 157 ARG A O   
1233 C CB  . ARG A 155 ? 0.2693 0.3974 0.5192 -0.0495 -0.0802 -0.0155 157 ARG A CB  
1234 C CG  . ARG A 155 ? 0.3118 0.4357 0.5439 -0.0470 -0.0773 -0.0140 157 ARG A CG  
1235 C CD  . ARG A 155 ? 0.3715 0.4928 0.5852 -0.0509 -0.0828 -0.0169 157 ARG A CD  
1236 N NE  . ARG A 155 ? 0.4160 0.5339 0.6151 -0.0482 -0.0799 -0.0137 157 ARG A NE  
1237 C CZ  . ARG A 155 ? 0.4323 0.5440 0.6222 -0.0479 -0.0728 -0.0168 157 ARG A CZ  
1238 N NH1 . ARG A 155 ? 0.3940 0.5023 0.5874 -0.0499 -0.0674 -0.0236 157 ARG A NH1 
1239 N NH2 . ARG A 155 ? 0.4422 0.5514 0.6212 -0.0457 -0.0712 -0.0129 157 ARG A NH2 
1240 N N   . ALA A 156 ? 0.3453 0.4743 0.6143 -0.0615 -0.0913 -0.0278 158 ALA A N   
1241 C CA  . ALA A 156 ? 0.3757 0.5082 0.6641 -0.0653 -0.0969 -0.0292 158 ALA A CA  
1242 C C   . ALA A 156 ? 0.3771 0.5193 0.6876 -0.0612 -0.0970 -0.0183 158 ALA A C   
1243 O O   . ALA A 156 ? 0.3802 0.5253 0.7112 -0.0615 -0.0952 -0.0168 158 ALA A O   
1244 C CB  . ALA A 156 ? 0.3971 0.5286 0.6766 -0.0714 -0.1084 -0.0342 158 ALA A CB  
1245 N N   . LYS A 157 ? 0.3804 0.5274 0.6868 -0.0572 -0.0986 -0.0107 159 LYS A N   
1246 C CA  . LYS A 157 ? 0.3826 0.5386 0.7069 -0.0522 -0.0975 -0.0001 159 LYS A CA  
1247 C C   . LYS A 157 ? 0.3735 0.5295 0.7050 -0.0465 -0.0865 0.0040  159 LYS A C   
1248 O O   . LYS A 157 ? 0.3747 0.5374 0.7252 -0.0434 -0.0839 0.0113  159 LYS A O   
1249 C CB  . LYS A 157 ? 0.4215 0.5801 0.7352 -0.0489 -0.1009 0.0057  159 LYS A CB  
1250 C CG  . LYS A 157 ? 0.4588 0.6260 0.7887 -0.0427 -0.0989 0.0164  159 LYS A CG  
1251 C CD  . LYS A 157 ? 0.5006 0.6693 0.8203 -0.0406 -0.1042 0.0208  159 LYS A CD  
1252 C CE  . LYS A 157 ? 0.5046 0.6756 0.8266 -0.0322 -0.0974 0.0288  159 LYS A CE  
1253 N NZ  . LYS A 157 ? 0.5028 0.6661 0.8111 -0.0285 -0.0878 0.0262  159 LYS A NZ  
1254 N N   . GLY A 158 ? 0.3583 0.5068 0.6749 -0.0450 -0.0801 0.0000  160 GLY A N   
1255 C CA  . GLY A 158 ? 0.3459 0.4935 0.6664 -0.0397 -0.0711 0.0040  160 GLY A CA  
1256 C C   . GLY A 158 ? 0.3331 0.4737 0.6340 -0.0370 -0.0667 0.0018  160 GLY A C   
1257 O O   . GLY A 158 ? 0.3499 0.4893 0.6369 -0.0361 -0.0693 0.0024  160 GLY A O   
1258 N N   . ASP A 159 ? 0.2818 0.4182 0.5835 -0.0360 -0.0606 0.0002  161 ASP A N   
1259 C CA  . ASP A 159 ? 0.2398 0.3692 0.5262 -0.0350 -0.0569 -0.0031 161 ASP A CA  
1260 C C   . ASP A 159 ? 0.2267 0.3559 0.5068 -0.0286 -0.0541 0.0033  161 ASP A C   
1261 O O   . ASP A 159 ? 0.2300 0.3635 0.5194 -0.0244 -0.0522 0.0097  161 ASP A O   
1262 C CB  . ASP A 159 ? 0.2083 0.3335 0.5007 -0.0366 -0.0521 -0.0072 161 ASP A CB  
1263 C CG  . ASP A 159 ? 0.2289 0.3524 0.5259 -0.0429 -0.0546 -0.0152 161 ASP A CG  
1264 O OD1 . ASP A 159 ? 0.2179 0.3398 0.5036 -0.0464 -0.0590 -0.0201 161 ASP A OD1 
1265 O OD2 . ASP A 159 ? 0.2379 0.3610 0.5489 -0.0442 -0.0523 -0.0165 161 ASP A OD2 
1266 N N   . LYS A 160 ? 0.2045 0.3282 0.4689 -0.0278 -0.0535 0.0015  162 LYS A N   
1267 C CA  . LYS A 160 ? 0.1845 0.3059 0.4416 -0.0220 -0.0513 0.0064  162 LYS A CA  
1268 C C   . LYS A 160 ? 0.1421 0.2569 0.3932 -0.0215 -0.0475 0.0041  162 LYS A C   
1269 O O   . LYS A 160 ? 0.1203 0.2314 0.3660 -0.0255 -0.0471 -0.0013 162 LYS A O   
1270 C CB  . LYS A 160 ? 0.2168 0.3381 0.4630 -0.0211 -0.0552 0.0081  162 LYS A CB  
1271 C CG  . LYS A 160 ? 0.2643 0.3928 0.5185 -0.0205 -0.0596 0.0121  162 LYS A CG  
1272 C CD  . LYS A 160 ? 0.3823 0.5102 0.6262 -0.0196 -0.0639 0.0144  162 LYS A CD  
1273 C CE  . LYS A 160 ? 0.4580 0.5875 0.6974 -0.0256 -0.0705 0.0112  162 LYS A CE  
1274 N NZ  . LYS A 160 ? 0.4731 0.6035 0.7051 -0.0245 -0.0757 0.0153  162 LYS A NZ  
1275 N N   . ILE A 161 ? 0.1201 0.2331 0.3718 -0.0166 -0.0446 0.0082  163 ILE A N   
1276 C CA  . ILE A 161 ? 0.1319 0.2384 0.3779 -0.0157 -0.0424 0.0071  163 ILE A CA  
1277 C C   . ILE A 161 ? 0.1345 0.2374 0.3709 -0.0102 -0.0429 0.0110  163 ILE A C   
1278 O O   . ILE A 161 ? 0.1082 0.2137 0.3468 -0.0058 -0.0421 0.0153  163 ILE A O   
1279 C CB  . ILE A 161 ? 0.1501 0.2564 0.4062 -0.0153 -0.0394 0.0079  163 ILE A CB  
1280 C CG1 . ILE A 161 ? 0.1653 0.2742 0.4325 -0.0205 -0.0387 0.0037  163 ILE A CG1 
1281 C CG2 . ILE A 161 ? 0.1683 0.2680 0.4190 -0.0140 -0.0385 0.0078  163 ILE A CG2 
1282 C CD1 . ILE A 161 ? 0.1909 0.3004 0.4707 -0.0200 -0.0360 0.0057  163 ILE A CD1 
1283 N N   . ALA A 162 ? 0.1326 0.2294 0.3595 -0.0103 -0.0438 0.0094  164 ALA A N   
1284 C CA  . ALA A 162 ? 0.1444 0.2365 0.3619 -0.0058 -0.0451 0.0120  164 ALA A CA  
1285 C C   . ALA A 162 ? 0.1543 0.2389 0.3663 -0.0060 -0.0456 0.0107  164 ALA A C   
1286 O O   . ALA A 162 ? 0.1788 0.2623 0.3922 -0.0104 -0.0452 0.0076  164 ALA A O   
1287 C CB  . ALA A 162 ? 0.1443 0.2376 0.3563 -0.0061 -0.0479 0.0126  164 ALA A CB  
1288 N N   . ILE A 163 ? 0.1322 0.2113 0.3385 -0.0013 -0.0463 0.0128  165 ILE A N   
1289 C CA  . ILE A 163 ? 0.1321 0.2031 0.3324 -0.0013 -0.0486 0.0118  165 ILE A CA  
1290 C C   . ILE A 163 ? 0.1426 0.2094 0.3343 0.0008  -0.0511 0.0126  165 ILE A C   
1291 O O   . ILE A 163 ? 0.1317 0.1975 0.3190 0.0058  -0.0512 0.0145  165 ILE A O   
1292 C CB  . ILE A 163 ? 0.1412 0.2070 0.3391 0.0019  -0.0494 0.0130  165 ILE A CB  
1293 C CG1 . ILE A 163 ? 0.1355 0.2048 0.3436 -0.0008 -0.0476 0.0129  165 ILE A CG1 
1294 C CG2 . ILE A 163 ? 0.1454 0.2019 0.3366 0.0022  -0.0534 0.0121  165 ILE A CG2 
1295 C CD1 . ILE A 163 ? 0.1544 0.2194 0.3603 0.0020  -0.0488 0.0150  165 ILE A CD1 
1296 N N   . TRP A 164 ? 0.1523 0.2164 0.3427 -0.0029 -0.0525 0.0113  166 TRP A N   
1297 C CA  . TRP A 164 ? 0.1660 0.2257 0.3500 -0.0023 -0.0550 0.0124  166 TRP A CA  
1298 C C   . TRP A 164 ? 0.1646 0.2147 0.3446 0.0000  -0.0580 0.0123  166 TRP A C   
1299 O O   . TRP A 164 ? 0.1594 0.2067 0.3429 -0.0023 -0.0587 0.0111  166 TRP A O   
1300 C CB  . TRP A 164 ? 0.1735 0.2355 0.3585 -0.0078 -0.0542 0.0117  166 TRP A CB  
1301 C CG  . TRP A 164 ? 0.1854 0.2549 0.3706 -0.0098 -0.0532 0.0117  166 TRP A CG  
1302 C CD1 . TRP A 164 ? 0.1977 0.2737 0.3877 -0.0095 -0.0520 0.0111  166 TRP A CD1 
1303 C CD2 . TRP A 164 ? 0.1956 0.2666 0.3760 -0.0128 -0.0541 0.0127  166 TRP A CD2 
1304 N NE1 . TRP A 164 ? 0.2025 0.2836 0.3912 -0.0124 -0.0527 0.0109  166 TRP A NE1 
1305 C CE2 . TRP A 164 ? 0.2097 0.2879 0.3915 -0.0144 -0.0540 0.0119  166 TRP A CE2 
1306 C CE3 . TRP A 164 ? 0.2174 0.2843 0.3927 -0.0146 -0.0551 0.0145  166 TRP A CE3 
1307 C CZ2 . TRP A 164 ? 0.2248 0.3058 0.4011 -0.0174 -0.0558 0.0128  166 TRP A CZ2 
1308 C CZ3 . TRP A 164 ? 0.2387 0.3087 0.4085 -0.0175 -0.0557 0.0159  166 TRP A CZ3 
1309 C CH2 . TRP A 164 ? 0.2437 0.3205 0.4131 -0.0188 -0.0565 0.0149  166 TRP A CH2 
1310 N N   . THR A 165 ? 0.1717 0.2162 0.3450 0.0044  -0.0602 0.0133  167 THR A N   
1311 C CA  . THR A 165 ? 0.1923 0.2261 0.3605 0.0065  -0.0641 0.0126  167 THR A CA  
1312 C C   . THR A 165 ? 0.1928 0.2221 0.3587 0.0063  -0.0666 0.0139  167 THR A C   
1313 O O   . THR A 165 ? 0.1861 0.2205 0.3526 0.0059  -0.0652 0.0160  167 THR A O   
1314 C CB  . THR A 165 ? 0.2372 0.2659 0.3981 0.0127  -0.0645 0.0117  167 THR A CB  
1315 O OG1 . THR A 165 ? 0.2551 0.2821 0.4108 0.0180  -0.0636 0.0126  167 THR A OG1 
1316 C CG2 . THR A 165 ? 0.2614 0.2965 0.4254 0.0130  -0.0611 0.0120  167 THR A CG2 
1317 N N   . THR A 166 ? 0.1861 0.2056 0.3500 0.0062  -0.0708 0.0132  168 THR A N   
1318 C CA  . THR A 166 ? 0.2022 0.2168 0.3667 0.0047  -0.0734 0.0150  168 THR A CA  
1319 C C   . THR A 166 ? 0.2080 0.2166 0.3669 0.0100  -0.0751 0.0159  168 THR A C   
1320 O O   . THR A 166 ? 0.2040 0.2117 0.3647 0.0086  -0.0762 0.0189  168 THR A O   
1321 C CB  . THR A 166 ? 0.2473 0.2542 0.4154 0.0016  -0.0775 0.0142  168 THR A CB  
1322 O OG1 . THR A 166 ? 0.2847 0.2895 0.4567 -0.0017 -0.0786 0.0172  168 THR A OG1 
1323 C CG2 . THR A 166 ? 0.2570 0.2524 0.4184 0.0058  -0.0827 0.0112  168 THR A CG2 
1324 N N   . GLU A 167 ? 0.2008 0.2052 0.3532 0.0161  -0.0750 0.0137  169 GLU A N   
1325 C CA  . GLU A 167 ? 0.1994 0.1955 0.3467 0.0220  -0.0765 0.0133  169 GLU A CA  
1326 C C   . GLU A 167 ? 0.2184 0.2173 0.3614 0.0286  -0.0722 0.0127  169 GLU A C   
1327 O O   . GLU A 167 ? 0.2327 0.2273 0.3686 0.0319  -0.0715 0.0096  169 GLU A O   
1328 C CB  . GLU A 167 ? 0.2098 0.1912 0.3521 0.0230  -0.0822 0.0100  169 GLU A CB  
1329 C CG  . GLU A 167 ? 0.2448 0.2150 0.3814 0.0290  -0.0840 0.0083  169 GLU A CG  
1330 C CD  . GLU A 167 ? 0.2808 0.2542 0.4233 0.0296  -0.0830 0.0128  169 GLU A CD  
1331 O OE1 . GLU A 167 ? 0.2761 0.2483 0.4247 0.0248  -0.0860 0.0157  169 GLU A OE1 
1332 O OE2 . GLU A 167 ? 0.2927 0.2706 0.4349 0.0346  -0.0790 0.0140  169 GLU A OE2 
1333 N N   . CYS A 168 ? 0.2043 0.2105 0.3515 0.0306  -0.0693 0.0160  170 CYS A N   
1334 C CA  . CYS A 168 ? 0.2498 0.2601 0.3959 0.0368  -0.0644 0.0163  170 CYS A CA  
1335 C C   . CYS A 168 ? 0.2805 0.2792 0.4183 0.0445  -0.0638 0.0134  170 CYS A C   
1336 O O   . CYS A 168 ? 0.3146 0.3157 0.4499 0.0498  -0.0586 0.0132  170 CYS A O   
1337 C CB  . CYS A 168 ? 0.2875 0.3091 0.4426 0.0367  -0.0624 0.0210  170 CYS A CB  
1338 S SG  . CYS A 168 ? 0.3988 0.4155 0.5570 0.0386  -0.0657 0.0243  170 CYS A SG  
1339 N N   . GLU A 169 ? 0.2721 0.2577 0.4053 0.0454  -0.0684 0.0110  171 GLU A N   
1340 C CA  . GLU A 169 ? 0.2887 0.2614 0.4123 0.0530  -0.0678 0.0069  171 GLU A CA  
1341 C C   . GLU A 169 ? 0.3118 0.2742 0.4224 0.0536  -0.0702 0.0013  171 GLU A C   
1342 O O   . GLU A 169 ? 0.3302 0.2804 0.4297 0.0598  -0.0700 -0.0031 171 GLU A O   
1343 C CB  . GLU A 169 ? 0.2876 0.2498 0.4133 0.0542  -0.0721 0.0068  171 GLU A CB  
1344 C CG  . GLU A 169 ? 0.3417 0.3126 0.4794 0.0539  -0.0710 0.0130  171 GLU A CG  
1345 C CD  . GLU A 169 ? 0.3511 0.3298 0.4935 0.0603  -0.0647 0.0157  171 GLU A CD  
1346 O OE1 . GLU A 169 ? 0.3544 0.3285 0.4900 0.0674  -0.0598 0.0123  171 GLU A OE1 
1347 O OE2 . GLU A 169 ? 0.3244 0.3140 0.4775 0.0580  -0.0646 0.0216  171 GLU A OE2 
1348 N N   . ASN A 170 ? 0.3100 0.2769 0.4219 0.0473  -0.0727 0.0015  172 ASN A N   
1349 C CA  . ASN A 170 ? 0.2908 0.2501 0.3915 0.0475  -0.0755 -0.0025 172 ASN A CA  
1350 C C   . ASN A 170 ? 0.2773 0.2437 0.3730 0.0514  -0.0686 -0.0016 172 ASN A C   
1351 O O   . ASN A 170 ? 0.2400 0.2155 0.3402 0.0474  -0.0675 0.0007  172 ASN A O   
1352 C CB  . ASN A 170 ? 0.2741 0.2359 0.3815 0.0391  -0.0810 -0.0017 172 ASN A CB  
1353 C CG  . ASN A 170 ? 0.2511 0.2024 0.3608 0.0356  -0.0888 -0.0033 172 ASN A CG  
1354 O OD1 . ASN A 170 ? 0.2888 0.2284 0.3932 0.0392  -0.0915 -0.0060 172 ASN A OD1 
1355 N ND2 . ASN A 170 ? 0.1891 0.1442 0.3080 0.0285  -0.0923 -0.0016 172 ASN A ND2 
1356 N N   . ARG A 171 ? 0.3015 0.2632 0.3883 0.0597  -0.0633 -0.0031 173 ARG A N   
1357 C CA  . ARG A 171 ? 0.3082 0.2778 0.3924 0.0639  -0.0552 -0.0009 173 ARG A CA  
1358 C C   . ARG A 171 ? 0.3256 0.2930 0.3997 0.0624  -0.0568 -0.0020 173 ARG A C   
1359 O O   . ARG A 171 ? 0.2989 0.2776 0.3791 0.0605  -0.0529 0.0019  173 ARG A O   
1360 C CB  . ARG A 171 ? 0.3351 0.2987 0.4114 0.0735  -0.0486 -0.0025 173 ARG A CB  
1361 C CG  . ARG A 171 ? 0.4080 0.3789 0.4814 0.0792  -0.0386 0.0003  173 ARG A CG  
1362 C CD  . ARG A 171 ? 0.5002 0.4609 0.5526 0.0828  -0.0378 -0.0032 173 ARG A CD  
1363 N NE  . ARG A 171 ? 0.5449 0.4869 0.5799 0.0878  -0.0410 -0.0103 173 ARG A NE  
1364 C CZ  . ARG A 171 ? 0.6190 0.5475 0.6333 0.0891  -0.0450 -0.0153 173 ARG A CZ  
1365 N NH1 . ARG A 171 ? 0.6346 0.5668 0.6432 0.0861  -0.0463 -0.0132 173 ARG A NH1 
1366 N NH2 . ARG A 171 ? 0.6551 0.5658 0.6542 0.0935  -0.0485 -0.0225 173 ARG A NH2 
1367 N N   . GLU A 172 ? 0.3487 0.3012 0.4080 0.0631  -0.0633 -0.0071 174 GLU A N   
1368 C CA  . GLU A 172 ? 0.3822 0.3311 0.4300 0.0620  -0.0661 -0.0078 174 GLU A CA  
1369 C C   . GLU A 172 ? 0.3665 0.3261 0.4287 0.0536  -0.0697 -0.0040 174 GLU A C   
1370 O O   . GLU A 172 ? 0.3737 0.3388 0.4345 0.0529  -0.0676 -0.0012 174 GLU A O   
1371 C CB  . GLU A 172 ? 0.4375 0.3673 0.4676 0.0636  -0.0745 -0.0144 174 GLU A CB  
1372 C CG  . GLU A 172 ? 0.6291 0.5533 0.6448 0.0629  -0.0791 -0.0153 174 GLU A CG  
1373 C CD  . GLU A 172 ? 0.8085 0.7267 0.8023 0.0708  -0.0730 -0.0165 174 GLU A CD  
1374 O OE1 . GLU A 172 ? 0.8432 0.7493 0.8184 0.0714  -0.0795 -0.0198 174 GLU A OE1 
1375 O OE2 . GLU A 172 ? 0.8468 0.7722 0.8420 0.0764  -0.0617 -0.0140 174 GLU A OE2 
1376 N N   . ALA A 173 ? 0.3442 0.3064 0.4202 0.0473  -0.0745 -0.0036 175 ALA A N   
1377 C CA  . ALA A 173 ? 0.3306 0.3026 0.4212 0.0396  -0.0767 -0.0006 175 ALA A CA  
1378 C C   . ALA A 173 ? 0.3059 0.2937 0.4080 0.0388  -0.0687 0.0040  175 ALA A C   
1379 O O   . ALA A 173 ? 0.2638 0.2588 0.3715 0.0359  -0.0676 0.0064  175 ALA A O   
1380 C CB  . ALA A 173 ? 0.3261 0.2966 0.4275 0.0339  -0.0822 -0.0011 175 ALA A CB  
1381 N N   . VAL A 174 ? 0.2987 0.2913 0.4051 0.0415  -0.0638 0.0051  176 VAL A N   
1382 C CA  . VAL A 174 ? 0.2835 0.2903 0.4023 0.0402  -0.0578 0.0090  176 VAL A CA  
1383 C C   . VAL A 174 ? 0.2907 0.3026 0.4067 0.0440  -0.0517 0.0114  176 VAL A C   
1384 O O   . VAL A 174 ? 0.2785 0.3007 0.4048 0.0404  -0.0494 0.0143  176 VAL A O   
1385 C CB  . VAL A 174 ? 0.2647 0.2738 0.3882 0.0426  -0.0556 0.0099  176 VAL A CB  
1386 C CG1 . VAL A 174 ? 0.2640 0.2866 0.3981 0.0431  -0.0496 0.0139  176 VAL A CG1 
1387 C CG2 . VAL A 174 ? 0.2802 0.2877 0.4098 0.0371  -0.0610 0.0094  176 VAL A CG2 
1388 N N   . THR A 175 ? 0.2958 0.3001 0.3980 0.0513  -0.0487 0.0103  177 THR A N   
1389 C CA  . THR A 175 ? 0.3040 0.3130 0.4028 0.0556  -0.0416 0.0135  177 THR A CA  
1390 C C   . THR A 175 ? 0.3106 0.3190 0.4057 0.0526  -0.0442 0.0146  177 THR A C   
1391 O O   . THR A 175 ? 0.3028 0.3204 0.4045 0.0524  -0.0392 0.0191  177 THR A O   
1392 C CB  . THR A 175 ? 0.3426 0.3433 0.4266 0.0649  -0.0362 0.0119  177 THR A CB  
1393 O OG1 . THR A 175 ? 0.4044 0.3889 0.4700 0.0669  -0.0420 0.0064  177 THR A OG1 
1394 C CG2 . THR A 175 ? 0.3262 0.3297 0.4182 0.0681  -0.0328 0.0122  177 THR A CG2 
1395 N N   . HIS A 176 ? 0.3116 0.3094 0.3977 0.0502  -0.0523 0.0112  178 HIS A N   
1396 C CA  . HIS A 176 ? 0.3005 0.2977 0.3852 0.0467  -0.0566 0.0127  178 HIS A CA  
1397 C C   . HIS A 176 ? 0.2819 0.2912 0.3871 0.0396  -0.0568 0.0156  178 HIS A C   
1398 O O   . HIS A 176 ? 0.2771 0.2924 0.3872 0.0383  -0.0547 0.0195  178 HIS A O   
1399 C CB  . HIS A 176 ? 0.3201 0.3037 0.3941 0.0450  -0.0668 0.0083  178 HIS A CB  
1400 C CG  . HIS A 176 ? 0.3407 0.3227 0.4130 0.0417  -0.0724 0.0103  178 HIS A CG  
1401 N ND1 . HIS A 176 ? 0.3872 0.3591 0.4392 0.0459  -0.0749 0.0097  178 HIS A ND1 
1402 C CD2 . HIS A 176 ? 0.3718 0.3602 0.4595 0.0352  -0.0760 0.0128  178 HIS A CD2 
1403 C CE1 . HIS A 176 ? 0.3900 0.3630 0.4457 0.0418  -0.0805 0.0126  178 HIS A CE1 
1404 N NE2 . HIS A 176 ? 0.3784 0.3611 0.4563 0.0355  -0.0813 0.0145  178 HIS A NE2 
1405 N N   . ILE A 177 ? 0.2543 0.2669 0.3714 0.0350  -0.0589 0.0139  179 ILE A N   
1406 C CA  . ILE A 177 ? 0.2196 0.2434 0.3550 0.0287  -0.0578 0.0158  179 ILE A CA  
1407 C C   . ILE A 177 ? 0.2374 0.2726 0.3807 0.0302  -0.0500 0.0198  179 ILE A C   
1408 O O   . ILE A 177 ? 0.2498 0.2913 0.4027 0.0271  -0.0487 0.0222  179 ILE A O   
1409 C CB  . ILE A 177 ? 0.1735 0.1991 0.3173 0.0245  -0.0596 0.0137  179 ILE A CB  
1410 C CG1 . ILE A 177 ? 0.1900 0.2066 0.3322 0.0211  -0.0673 0.0110  179 ILE A CG1 
1411 C CG2 . ILE A 177 ? 0.1059 0.1434 0.2659 0.0192  -0.0565 0.0151  179 ILE A CG2 
1412 C CD1 . ILE A 177 ? 0.1760 0.1906 0.3208 0.0191  -0.0692 0.0095  179 ILE A CD1 
1413 N N   . GLY A 178 ? 0.2442 0.2814 0.3848 0.0349  -0.0453 0.0205  180 GLY A N   
1414 C CA  . GLY A 178 ? 0.2440 0.2921 0.3944 0.0362  -0.0384 0.0244  180 GLY A CA  
1415 C C   . GLY A 178 ? 0.2569 0.3066 0.4047 0.0388  -0.0344 0.0285  180 GLY A C   
1416 O O   . GLY A 178 ? 0.2511 0.3103 0.4123 0.0362  -0.0313 0.0319  180 GLY A O   
1417 N N   . ARG A 179 ? 0.2822 0.3219 0.4119 0.0440  -0.0347 0.0282  181 ARG A N   
1418 C CA  . ARG A 179 ? 0.3075 0.3469 0.4304 0.0470  -0.0312 0.0326  181 ARG A CA  
1419 C C   . ARG A 179 ? 0.2886 0.3309 0.4204 0.0412  -0.0352 0.0347  181 ARG A C   
1420 O O   . ARG A 179 ? 0.2901 0.3404 0.4318 0.0405  -0.0308 0.0399  181 ARG A O   
1421 C CB  . ARG A 179 ? 0.3616 0.3874 0.4596 0.0531  -0.0324 0.0307  181 ARG A CB  
1422 C CG  . ARG A 179 ? 0.4406 0.4624 0.5280 0.0606  -0.0264 0.0291  181 ARG A CG  
1423 C CD  . ARG A 179 ? 0.5447 0.5700 0.6266 0.0670  -0.0163 0.0345  181 ARG A CD  
1424 N NE  . ARG A 179 ? 0.6136 0.6359 0.6887 0.0743  -0.0096 0.0328  181 ARG A NE  
1425 C CZ  . ARG A 179 ? 0.6490 0.6776 0.7267 0.0803  0.0014  0.0376  181 ARG A CZ  
1426 N NH1 . ARG A 179 ? 0.6375 0.6759 0.7243 0.0795  0.0071  0.0449  181 ARG A NH1 
1427 N NH2 . ARG A 179 ? 0.6717 0.6968 0.7444 0.0870  0.0071  0.0355  181 ARG A NH2 
1428 N N   . VAL A 180 ? 0.2687 0.3047 0.3990 0.0371  -0.0433 0.0311  182 VAL A N   
1429 C CA  . VAL A 180 ? 0.2533 0.2909 0.3931 0.0318  -0.0478 0.0328  182 VAL A CA  
1430 C C   . VAL A 180 ? 0.2484 0.2977 0.4106 0.0265  -0.0448 0.0337  182 VAL A C   
1431 O O   . VAL A 180 ? 0.2554 0.3100 0.4285 0.0242  -0.0435 0.0376  182 VAL A O   
1432 C CB  . VAL A 180 ? 0.2638 0.2921 0.3986 0.0288  -0.0570 0.0286  182 VAL A CB  
1433 C CG1 . VAL A 180 ? 0.2678 0.2987 0.4164 0.0231  -0.0615 0.0303  182 VAL A CG1 
1434 C CG2 . VAL A 180 ? 0.2999 0.3152 0.4112 0.0338  -0.0612 0.0272  182 VAL A CG2 
1435 N N   . TYR A 181 ? 0.2197 0.2724 0.3883 0.0246  -0.0441 0.0303  183 TYR A N   
1436 C CA  . TYR A 181 ? 0.2107 0.2735 0.3977 0.0198  -0.0414 0.0302  183 TYR A CA  
1437 C C   . TYR A 181 ? 0.2229 0.2945 0.4188 0.0214  -0.0350 0.0350  183 TYR A C   
1438 O O   . TYR A 181 ? 0.2035 0.2812 0.4143 0.0175  -0.0339 0.0367  183 TYR A O   
1439 C CB  . TYR A 181 ? 0.1928 0.2567 0.3810 0.0183  -0.0421 0.0262  183 TYR A CB  
1440 C CG  . TYR A 181 ? 0.1863 0.2586 0.3898 0.0129  -0.0407 0.0247  183 TYR A CG  
1441 C CD1 . TYR A 181 ? 0.1951 0.2702 0.4105 0.0079  -0.0412 0.0241  183 TYR A CD1 
1442 C CD2 . TYR A 181 ? 0.1918 0.2685 0.3972 0.0127  -0.0395 0.0236  183 TYR A CD2 
1443 C CE1 . TYR A 181 ? 0.1775 0.2588 0.4046 0.0032  -0.0399 0.0216  183 TYR A CE1 
1444 C CE2 . TYR A 181 ? 0.1781 0.2615 0.3948 0.0077  -0.0390 0.0217  183 TYR A CE2 
1445 C CZ  . TYR A 181 ? 0.1715 0.2567 0.3982 0.0029  -0.0391 0.0202  183 TYR A CZ  
1446 O OH  . TYR A 181 ? 0.1607 0.2510 0.3961 -0.0020 -0.0387 0.0172  183 TYR A OH  
1447 N N   . LYS A 182 ? 0.2171 0.2894 0.4058 0.0270  -0.0304 0.0375  184 LYS A N   
1448 C CA  . LYS A 182 ? 0.2344 0.3156 0.4333 0.0287  -0.0239 0.0430  184 LYS A CA  
1449 C C   . LYS A 182 ? 0.2550 0.3358 0.4548 0.0289  -0.0227 0.0483  184 LYS A C   
1450 O O   . LYS A 182 ? 0.2656 0.3542 0.4813 0.0265  -0.0197 0.0522  184 LYS A O   
1451 C CB  . LYS A 182 ? 0.2419 0.3231 0.4323 0.0356  -0.0185 0.0451  184 LYS A CB  
1452 C CG  . LYS A 182 ? 0.3041 0.3948 0.5063 0.0377  -0.0111 0.0518  184 LYS A CG  
1453 C CD  . LYS A 182 ? 0.3395 0.4288 0.5315 0.0456  -0.0046 0.0545  184 LYS A CD  
1454 C CE  . LYS A 182 ? 0.3760 0.4768 0.5846 0.0472  0.0030  0.0613  184 LYS A CE  
1455 N NZ  . LYS A 182 ? 0.4230 0.5239 0.6257 0.0549  0.0102  0.0636  184 LYS A NZ  
1456 N N   . GLU A 183 ? 0.2524 0.3238 0.4353 0.0316  -0.0257 0.0485  185 GLU A N   
1457 C CA  . GLU A 183 ? 0.2523 0.3217 0.4333 0.0317  -0.0265 0.0538  185 GLU A CA  
1458 C C   . GLU A 183 ? 0.2473 0.3208 0.4475 0.0248  -0.0302 0.0537  185 GLU A C   
1459 O O   . GLU A 183 ? 0.2387 0.3173 0.4509 0.0235  -0.0276 0.0594  185 GLU A O   
1460 C CB  . GLU A 183 ? 0.2791 0.3361 0.4373 0.0347  -0.0320 0.0519  185 GLU A CB  
1461 C CG  . GLU A 183 ? 0.3709 0.4235 0.5198 0.0363  -0.0338 0.0576  185 GLU A CG  
1462 C CD  . GLU A 183 ? 0.4457 0.4861 0.5777 0.0362  -0.0431 0.0536  185 GLU A CD  
1463 O OE1 . GLU A 183 ? 0.4241 0.4631 0.5631 0.0319  -0.0499 0.0546  185 GLU A OE1 
1464 O OE2 . GLU A 183 ? 0.5033 0.5356 0.6169 0.0403  -0.0440 0.0492  185 GLU A OE2 
1465 N N   . ARG A 184 ? 0.2398 0.3108 0.4434 0.0206  -0.0355 0.0475  186 ARG A N   
1466 C CA  . ARG A 184 ? 0.2525 0.3259 0.4729 0.0146  -0.0383 0.0463  186 ARG A CA  
1467 C C   . ARG A 184 ? 0.2652 0.3480 0.5047 0.0112  -0.0339 0.0458  186 ARG A C   
1468 O O   . ARG A 184 ? 0.2562 0.3419 0.5114 0.0075  -0.0340 0.0470  186 ARG A O   
1469 C CB  . ARG A 184 ? 0.2665 0.3346 0.4848 0.0115  -0.0442 0.0400  186 ARG A CB  
1470 C CG  . ARG A 184 ? 0.2990 0.3573 0.5026 0.0134  -0.0508 0.0405  186 ARG A CG  
1471 C CD  . ARG A 184 ? 0.2880 0.3453 0.5001 0.0112  -0.0546 0.0445  186 ARG A CD  
1472 N NE  . ARG A 184 ? 0.2389 0.2989 0.4695 0.0056  -0.0562 0.0414  186 ARG A NE  
1473 C CZ  . ARG A 184 ? 0.2375 0.2928 0.4705 0.0030  -0.0623 0.0393  186 ARG A CZ  
1474 N NH1 . ARG A 184 ? 0.2326 0.2794 0.4504 0.0050  -0.0690 0.0395  186 ARG A NH1 
1475 N NH2 . ARG A 184 ? 0.2538 0.3126 0.5051 -0.0016 -0.0616 0.0368  186 ARG A NH2 
1476 N N   . LEU A 185 ? 0.2745 0.3617 0.5139 0.0123  -0.0306 0.0440  187 LEU A N   
1477 C CA  . LEU A 185 ? 0.2829 0.3788 0.5393 0.0095  -0.0270 0.0445  187 LEU A CA  
1478 C C   . LEU A 185 ? 0.3154 0.4165 0.5804 0.0115  -0.0222 0.0522  187 LEU A C   
1479 O O   . LEU A 185 ? 0.2962 0.4039 0.5785 0.0083  -0.0202 0.0530  187 LEU A O   
1480 C CB  . LEU A 185 ? 0.2775 0.3766 0.5317 0.0100  -0.0260 0.0412  187 LEU A CB  
1481 C CG  . LEU A 185 ? 0.2738 0.3699 0.5243 0.0065  -0.0302 0.0338  187 LEU A CG  
1482 C CD1 . LEU A 185 ? 0.2613 0.3599 0.5076 0.0079  -0.0298 0.0322  187 LEU A CD1 
1483 C CD2 . LEU A 185 ? 0.2739 0.3725 0.5383 0.0002  -0.0311 0.0299  187 LEU A CD2 
1484 N N   . GLY A 186 ? 0.3534 0.4511 0.6059 0.0166  -0.0204 0.0580  188 GLY A N   
1485 C CA  . GLY A 186 ? 0.3681 0.4708 0.6262 0.0195  -0.0145 0.0665  188 GLY A CA  
1486 C C   . GLY A 186 ? 0.3856 0.4964 0.6526 0.0208  -0.0091 0.0682  188 GLY A C   
1487 O O   . GLY A 186 ? 0.3971 0.5151 0.6813 0.0194  -0.0054 0.0735  188 GLY A O   
1488 N N   . LEU A 187 ? 0.3886 0.4985 0.6460 0.0233  -0.0090 0.0642  189 LEU A N   
1489 C CA  . LEU A 187 ? 0.3882 0.5061 0.6548 0.0251  -0.0043 0.0667  189 LEU A CA  
1490 C C   . LEU A 187 ? 0.4157 0.5344 0.6750 0.0321  0.0035  0.0748  189 LEU A C   
1491 O O   . LEU A 187 ? 0.4011 0.5115 0.6395 0.0367  0.0039  0.0751  189 LEU A O   
1492 C CB  . LEU A 187 ? 0.3691 0.4858 0.6289 0.0258  -0.0068 0.0606  189 LEU A CB  
1493 C CG  . LEU A 187 ? 0.3383 0.4552 0.6044 0.0193  -0.0132 0.0532  189 LEU A CG  
1494 C CD1 . LEU A 187 ? 0.3234 0.4373 0.5787 0.0208  -0.0159 0.0483  189 LEU A CD1 
1495 C CD2 . LEU A 187 ? 0.3385 0.4641 0.6252 0.0146  -0.0132 0.0537  189 LEU A CD2 
1496 N N   . PRO A 188 ? 0.4464 0.5747 0.7228 0.0329  0.0096  0.0816  190 PRO A N   
1497 C CA  . PRO A 188 ? 0.4765 0.6066 0.7464 0.0403  0.0188  0.0894  190 PRO A CA  
1498 C C   . PRO A 188 ? 0.5185 0.6431 0.7693 0.0466  0.0206  0.0857  190 PRO A C   
1499 O O   . PRO A 188 ? 0.5312 0.6569 0.7854 0.0450  0.0167  0.0799  190 PRO A O   
1500 C CB  . PRO A 188 ? 0.4737 0.6164 0.7701 0.0388  0.0236  0.0954  190 PRO A CB  
1501 C CG  . PRO A 188 ? 0.4666 0.6128 0.7823 0.0303  0.0168  0.0920  190 PRO A CG  
1502 C CD  . PRO A 188 ? 0.4414 0.5790 0.7441 0.0269  0.0085  0.0823  190 PRO A CD  
1503 N N   . PRO A 189 ? 0.5387 0.6570 0.7690 0.0539  0.0264  0.0888  191 PRO A N   
1504 C CA  . PRO A 189 ? 0.5543 0.6662 0.7667 0.0602  0.0282  0.0844  191 PRO A CA  
1505 C C   . PRO A 189 ? 0.5510 0.6712 0.7776 0.0629  0.0332  0.0857  191 PRO A C   
1506 O O   . PRO A 189 ? 0.5623 0.6775 0.7781 0.0671  0.0333  0.0811  191 PRO A O   
1507 C CB  . PRO A 189 ? 0.5765 0.6806 0.7658 0.0674  0.0349  0.0884  191 PRO A CB  
1508 C CG  . PRO A 189 ? 0.5739 0.6836 0.7726 0.0656  0.0385  0.0974  191 PRO A CG  
1509 C CD  . PRO A 189 ? 0.5442 0.6605 0.7664 0.0567  0.0315  0.0965  191 PRO A CD  
1510 N N   . LYS A 190 ? 0.5346 0.6674 0.7867 0.0605  0.0369  0.0921  192 LYS A N   
1511 C CA  . LYS A 190 ? 0.5134 0.6553 0.7828 0.0621  0.0400  0.0939  192 LYS A CA  
1512 C C   . LYS A 190 ? 0.4900 0.6356 0.7731 0.0549  0.0301  0.0879  192 LYS A C   
1513 O O   . LYS A 190 ? 0.4859 0.6373 0.7800 0.0561  0.0303  0.0882  192 LYS A O   
1514 C CB  . LYS A 190 ? 0.5360 0.6897 0.8267 0.0638  0.0495  0.1047  192 LYS A CB  
1515 C CG  . LYS A 190 ? 0.5849 0.7447 0.8833 0.0710  0.0584  0.1091  192 LYS A CG  
1516 C CD  . LYS A 190 ? 0.6461 0.7968 0.9186 0.0810  0.0679  0.1096  192 LYS A CD  
1517 C CE  . LYS A 190 ? 0.6860 0.8396 0.9631 0.0881  0.0745  0.1103  192 LYS A CE  
1518 N NZ  . LYS A 190 ? 0.7305 0.8808 1.0070 0.0857  0.0646  0.1018  192 LYS A NZ  
1519 N N   . ILE A 191 ? 0.4839 0.6263 0.7667 0.0475  0.0215  0.0828  193 ILE A N   
1520 C CA  . ILE A 191 ? 0.4777 0.6203 0.7653 0.0414  0.0122  0.0756  193 ILE A CA  
1521 C C   . ILE A 191 ? 0.4933 0.6254 0.7586 0.0446  0.0092  0.0692  193 ILE A C   
1522 O O   . ILE A 191 ? 0.5229 0.6455 0.7713 0.0447  0.0071  0.0659  193 ILE A O   
1523 C CB  . ILE A 191 ? 0.4751 0.6173 0.7697 0.0331  0.0058  0.0722  193 ILE A CB  
1524 C CG1 . ILE A 191 ? 0.4622 0.6142 0.7808 0.0298  0.0085  0.0786  193 ILE A CG1 
1525 C CG2 . ILE A 191 ? 0.4897 0.6305 0.7845 0.0273  -0.0031 0.0641  193 ILE A CG2 
1526 C CD1 . ILE A 191 ? 0.4563 0.6197 0.7971 0.0290  0.0093  0.0822  193 ILE A CD1 
1527 N N   . VAL A 192 ? 0.4730 0.6064 0.7391 0.0473  0.0088  0.0679  194 VAL A N   
1528 C CA  . VAL A 192 ? 0.4762 0.5993 0.7229 0.0507  0.0062  0.0623  194 VAL A CA  
1529 C C   . VAL A 192 ? 0.4590 0.5802 0.7060 0.0439  -0.0035 0.0559  194 VAL A C   
1530 O O   . VAL A 192 ? 0.4716 0.6010 0.7341 0.0397  -0.0069 0.0564  194 VAL A O   
1531 C CB  . VAL A 192 ? 0.4835 0.6075 0.7298 0.0586  0.0121  0.0649  194 VAL A CB  
1532 C CG1 . VAL A 192 ? 0.4837 0.6105 0.7307 0.0655  0.0234  0.0719  194 VAL A CG1 
1533 C CG2 . VAL A 192 ? 0.4750 0.6087 0.7408 0.0562  0.0090  0.0664  194 VAL A CG2 
1534 N N   . ILE A 193 ? 0.4162 0.5267 0.6461 0.0428  -0.0081 0.0502  195 ILE A N   
1535 C CA  . ILE A 193 ? 0.3632 0.4714 0.5918 0.0371  -0.0160 0.0446  195 ILE A CA  
1536 C C   . ILE A 193 ? 0.3140 0.4159 0.5323 0.0412  -0.0175 0.0424  195 ILE A C   
1537 O O   . ILE A 193 ? 0.3116 0.4070 0.5186 0.0481  -0.0134 0.0429  195 ILE A O   
1538 C CB  . ILE A 193 ? 0.3706 0.4732 0.5932 0.0316  -0.0205 0.0404  195 ILE A CB  
1539 C CG1 . ILE A 193 ? 0.3877 0.4787 0.5919 0.0353  -0.0207 0.0385  195 ILE A CG1 
1540 C CG2 . ILE A 193 ? 0.3715 0.4806 0.6073 0.0277  -0.0189 0.0429  195 ILE A CG2 
1541 C CD1 . ILE A 193 ? 0.3972 0.4824 0.5969 0.0301  -0.0262 0.0344  195 ILE A CD1 
1542 N N   . GLY A 194 ? 0.2596 0.3632 0.4818 0.0369  -0.0233 0.0400  196 GLY A N   
1543 C CA  . GLY A 194 ? 0.2285 0.3279 0.4452 0.0401  -0.0253 0.0391  196 GLY A CA  
1544 C C   . GLY A 194 ? 0.2013 0.2928 0.4079 0.0358  -0.0319 0.0341  196 GLY A C   
1545 O O   . GLY A 194 ? 0.1932 0.2868 0.4027 0.0289  -0.0356 0.0318  196 GLY A O   
1546 N N   . TYR A 195 ? 0.1982 0.2802 0.3936 0.0400  -0.0329 0.0323  197 TYR A N   
1547 C CA  . TYR A 195 ? 0.2041 0.2782 0.3912 0.0364  -0.0388 0.0285  197 TYR A CA  
1548 C C   . TYR A 195 ? 0.2386 0.3148 0.4300 0.0369  -0.0415 0.0304  197 TYR A C   
1549 O O   . TYR A 195 ? 0.2510 0.3262 0.4434 0.0434  -0.0387 0.0325  197 TYR A O   
1550 C CB  . TYR A 195 ? 0.2158 0.2768 0.3881 0.0402  -0.0392 0.0253  197 TYR A CB  
1551 C CG  . TYR A 195 ? 0.2171 0.2705 0.3837 0.0361  -0.0453 0.0222  197 TYR A CG  
1552 C CD1 . TYR A 195 ? 0.2311 0.2825 0.3964 0.0304  -0.0483 0.0198  197 TYR A CD1 
1553 C CD2 . TYR A 195 ? 0.2218 0.2701 0.3862 0.0382  -0.0478 0.0222  197 TYR A CD2 
1554 C CE1 . TYR A 195 ? 0.2249 0.2700 0.3870 0.0267  -0.0531 0.0177  197 TYR A CE1 
1555 C CE2 . TYR A 195 ? 0.2176 0.2591 0.3782 0.0343  -0.0531 0.0203  197 TYR A CE2 
1556 C CZ  . TYR A 195 ? 0.2417 0.2819 0.4013 0.0285  -0.0555 0.0182  197 TYR A CZ  
1557 O OH  . TYR A 195 ? 0.2645 0.2987 0.4223 0.0245  -0.0599 0.0171  197 TYR A OH  
1558 N N   . GLN A 196 ? 0.2340 0.3134 0.4283 0.0302  -0.0465 0.0299  198 GLN A N   
1559 C CA  . GLN A 196 ? 0.2357 0.3176 0.4334 0.0291  -0.0504 0.0323  198 GLN A CA  
1560 C C   . GLN A 196 ? 0.2124 0.2860 0.4013 0.0262  -0.0548 0.0304  198 GLN A C   
1561 O O   . GLN A 196 ? 0.1544 0.2266 0.3398 0.0205  -0.0563 0.0277  198 GLN A O   
1562 C CB  . GLN A 196 ? 0.2500 0.3425 0.4566 0.0228  -0.0530 0.0335  198 GLN A CB  
1563 C CG  . GLN A 196 ? 0.3223 0.4249 0.5420 0.0247  -0.0502 0.0367  198 GLN A CG  
1564 C CD  . GLN A 196 ? 0.4252 0.5358 0.6520 0.0177  -0.0525 0.0357  198 GLN A CD  
1565 O OE1 . GLN A 196 ? 0.4354 0.5437 0.6563 0.0118  -0.0548 0.0318  198 GLN A OE1 
1566 N NE2 . GLN A 196 ? 0.4544 0.5744 0.6951 0.0183  -0.0517 0.0392  198 GLN A NE2 
1567 N N   . SER A 197 ? 0.2185 0.2867 0.4055 0.0303  -0.0563 0.0322  199 SER A N   
1568 C CA  . SER A 197 ? 0.2463 0.3075 0.4276 0.0276  -0.0608 0.0321  199 SER A CA  
1569 C C   . SER A 197 ? 0.2221 0.2906 0.4057 0.0206  -0.0643 0.0340  199 SER A C   
1570 O O   . SER A 197 ? 0.2508 0.3285 0.4416 0.0199  -0.0655 0.0372  199 SER A O   
1571 C CB  . SER A 197 ? 0.3012 0.3569 0.4833 0.0336  -0.0617 0.0348  199 SER A CB  
1572 O OG  . SER A 197 ? 0.3812 0.4320 0.5607 0.0308  -0.0664 0.0366  199 SER A OG  
1573 N N   . HIS A 198 ? 0.1790 0.2436 0.3568 0.0154  -0.0660 0.0323  200 HIS A N   
1574 C CA  . HIS A 198 ? 0.2194 0.2892 0.3960 0.0089  -0.0687 0.0338  200 HIS A CA  
1575 C C   . HIS A 198 ? 0.2862 0.3580 0.4644 0.0100  -0.0729 0.0394  200 HIS A C   
1576 O O   . HIS A 198 ? 0.3125 0.3918 0.4918 0.0063  -0.0757 0.0415  200 HIS A O   
1577 C CB  . HIS A 198 ? 0.2136 0.2779 0.3839 0.0040  -0.0686 0.0317  200 HIS A CB  
1578 C CG  . HIS A 198 ? 0.2160 0.2809 0.3868 0.0012  -0.0652 0.0269  200 HIS A CG  
1579 N ND1 . HIS A 198 ? 0.2341 0.2920 0.4029 0.0000  -0.0643 0.0246  200 HIS A ND1 
1580 C CD2 . HIS A 198 ? 0.1968 0.2686 0.3716 -0.0004 -0.0631 0.0245  200 HIS A CD2 
1581 C CE1 . HIS A 198 ? 0.2224 0.2834 0.3939 -0.0021 -0.0615 0.0211  200 HIS A CE1 
1582 N NE2 . HIS A 198 ? 0.2115 0.2805 0.3865 -0.0024 -0.0605 0.0208  200 HIS A NE2 
1583 N N   . ALA A 199 ? 0.3129 0.3774 0.4914 0.0151  -0.0737 0.0417  201 ALA A N   
1584 C CA  . ALA A 199 ? 0.3580 0.4235 0.5399 0.0171  -0.0777 0.0478  201 ALA A CA  
1585 C C   . ALA A 199 ? 0.3817 0.4571 0.5735 0.0198  -0.0786 0.0511  201 ALA A C   
1586 O O   . ALA A 199 ? 0.3763 0.4566 0.5711 0.0182  -0.0834 0.0563  201 ALA A O   
1587 C CB  . ALA A 199 ? 0.3680 0.4228 0.5500 0.0228  -0.0776 0.0485  201 ALA A CB  
1588 N N   . ASP A 200 ? 0.3932 0.4717 0.5907 0.0237  -0.0741 0.0486  202 ASP A N   
1589 C CA  . ASP A 200 ? 0.3977 0.4866 0.6070 0.0257  -0.0743 0.0518  202 ASP A CA  
1590 C C   . ASP A 200 ? 0.4197 0.5177 0.6299 0.0185  -0.0770 0.0509  202 ASP A C   
1591 O O   . ASP A 200 ? 0.4025 0.5085 0.6199 0.0167  -0.0819 0.0552  202 ASP A O   
1592 C CB  . ASP A 200 ? 0.4024 0.4910 0.6173 0.0326  -0.0674 0.0501  202 ASP A CB  
1593 C CG  . ASP A 200 ? 0.4398 0.5183 0.6525 0.0403  -0.0645 0.0499  202 ASP A CG  
1594 O OD1 . ASP A 200 ? 0.4630 0.5367 0.6751 0.0411  -0.0684 0.0528  202 ASP A OD1 
1595 O OD2 . ASP A 200 ? 0.4378 0.5127 0.6490 0.0457  -0.0584 0.0470  202 ASP A OD2 
1596 N N   . THR A 201 ? 0.4291 0.5256 0.6328 0.0143  -0.0743 0.0453  203 THR A N   
1597 C CA  . THR A 201 ? 0.4383 0.5417 0.6420 0.0074  -0.0762 0.0431  203 THR A CA  
1598 C C   . THR A 201 ? 0.4610 0.5655 0.6575 0.0016  -0.0824 0.0449  203 THR A C   
1599 O O   . THR A 201 ? 0.4549 0.5661 0.6530 -0.0030 -0.0861 0.0445  203 THR A O   
1600 C CB  . THR A 201 ? 0.4652 0.5651 0.6636 0.0047  -0.0717 0.0369  203 THR A CB  
1601 O OG1 . THR A 201 ? 0.4741 0.5725 0.6773 0.0103  -0.0665 0.0360  203 THR A OG1 
1602 C CG2 . THR A 201 ? 0.4818 0.5880 0.6818 -0.0016 -0.0727 0.0337  203 THR A CG2 
1603 N N   . ALA A 202 ? 0.4787 0.5762 0.6667 0.0016  -0.0837 0.0469  204 ALA A N   
1604 C CA  . ALA A 202 ? 0.4998 0.5980 0.6796 -0.0033 -0.0892 0.0501  204 ALA A CA  
1605 C C   . ALA A 202 ? 0.5212 0.6256 0.7085 -0.0018 -0.0959 0.0567  204 ALA A C   
1606 O O   . ALA A 202 ? 0.5417 0.6500 0.7236 -0.0069 -0.1017 0.0587  204 ALA A O   
1607 C CB  . ALA A 202 ? 0.5085 0.5977 0.6796 -0.0034 -0.0884 0.0517  204 ALA A CB  
1608 N N   . THR A 203 ? 0.5204 0.6259 0.7201 0.0051  -0.0951 0.0603  205 THR A N   
1609 C CA  . THR A 203 ? 0.5150 0.6271 0.7253 0.0071  -0.1013 0.0674  205 THR A CA  
1610 C C   . THR A 203 ? 0.5280 0.6501 0.7497 0.0059  -0.1024 0.0665  205 THR A C   
1611 O O   . THR A 203 ? 0.5260 0.6493 0.7549 0.0090  -0.0961 0.0632  205 THR A O   
1612 C CB  . THR A 203 ? 0.5176 0.6257 0.7374 0.0154  -0.0996 0.0722  205 THR A CB  
1613 O OG1 . THR A 203 ? 0.5156 0.6263 0.7477 0.0217  -0.0936 0.0708  205 THR A OG1 
1614 C CG2 . THR A 203 ? 0.5206 0.6171 0.7306 0.0170  -0.0970 0.0712  205 THR A CG2 
1615 N N   . LYS A 204 ? 0.5327 0.6618 0.7562 0.0012  -0.1108 0.0698  206 LYS A N   
1616 C CA  . LYS A 204 ? 0.5322 0.6713 0.7700 0.0001  -0.1134 0.0701  206 LYS A CA  
1617 C C   . LYS A 204 ? 0.5413 0.6860 0.7979 0.0063  -0.1159 0.0784  206 LYS A C   
1618 O O   . LYS A 204 ? 0.5241 0.6699 0.7814 0.0060  -0.1234 0.0849  206 LYS A O   
1619 C CB  . LYS A 204 ? 0.5444 0.6872 0.7738 -0.0086 -0.1217 0.0682  206 LYS A CB  
1620 C CG  . LYS A 204 ? 0.5957 0.7348 0.8124 -0.0139 -0.1174 0.0590  206 LYS A CG  
1621 C CD  . LYS A 204 ? 0.6336 0.7627 0.8341 -0.0138 -0.1107 0.0552  206 LYS A CD  
1622 C CE  . LYS A 204 ? 0.7228 0.8499 0.9213 -0.0156 -0.1036 0.0470  206 LYS A CE  
1623 N NZ  . LYS A 204 ? 0.7944 0.9128 0.9775 -0.0175 -0.0983 0.0427  206 LYS A NZ  
1624 N N   . SER A 205 ? 0.5617 0.7098 0.8338 0.0123  -0.1089 0.0785  207 SER A N   
1625 C CA  . SER A 205 ? 0.5783 0.7311 0.8701 0.0200  -0.1079 0.0857  207 SER A CA  
1626 C C   . SER A 205 ? 0.5683 0.7333 0.8820 0.0203  -0.1086 0.0886  207 SER A C   
1627 O O   . SER A 205 ? 0.5612 0.7310 0.8937 0.0273  -0.1051 0.0942  207 SER A O   
1628 C CB  . SER A 205 ? 0.6203 0.7650 0.9108 0.0284  -0.0970 0.0837  207 SER A CB  
1629 O OG  . SER A 205 ? 0.6899 0.8239 0.9658 0.0291  -0.0976 0.0831  207 SER A OG  
1630 N N   . GLY A 206 ? 0.5632 0.7331 0.8758 0.0129  -0.1128 0.0851  208 GLY A N   
1631 C CA  . GLY A 206 ? 0.5602 0.7415 0.8948 0.0121  -0.1144 0.0879  208 GLY A CA  
1632 C C   . GLY A 206 ? 0.5662 0.7474 0.8996 0.0100  -0.1074 0.0813  208 GLY A C   
1633 O O   . GLY A 206 ? 0.5597 0.7352 0.8754 0.0042  -0.1081 0.0741  208 GLY A O   
1634 N N   . SER A 207 ? 0.5707 0.7585 0.9239 0.0152  -0.1001 0.0845  209 SER A N   
1635 C CA  . SER A 207 ? 0.5854 0.7746 0.9425 0.0144  -0.0928 0.0806  209 SER A CA  
1636 C C   . SER A 207 ? 0.6133 0.7927 0.9558 0.0201  -0.0808 0.0763  209 SER A C   
1637 O O   . SER A 207 ? 0.6252 0.8026 0.9709 0.0285  -0.0735 0.0795  209 SER A O   
1638 C CB  . SER A 207 ? 0.5797 0.7810 0.9657 0.0174  -0.0903 0.0875  209 SER A CB  
1639 O OG  . SER A 207 ? 0.5974 0.8023 0.9906 0.0137  -0.0873 0.0848  209 SER A OG  
1640 N N   . THR A 208 ? 0.6101 0.7830 0.9364 0.0154  -0.0794 0.0688  210 THR A N   
1641 C CA  . THR A 208 ? 0.6169 0.7802 0.9283 0.0191  -0.0703 0.0642  210 THR A CA  
1642 C C   . THR A 208 ? 0.6038 0.7572 0.8989 0.0223  -0.0707 0.0633  210 THR A C   
1643 O O   . THR A 208 ? 0.5997 0.7540 0.8968 0.0230  -0.0765 0.0672  210 THR A O   
1644 C CB  . THR A 208 ? 0.6401 0.8065 0.9631 0.0259  -0.0597 0.0671  210 THR A CB  
1645 O OG1 . THR A 208 ? 0.6394 0.8158 0.9804 0.0224  -0.0604 0.0693  210 THR A OG1 
1646 C CG2 . THR A 208 ? 0.6560 0.8131 0.9634 0.0281  -0.0520 0.0620  210 THR A CG2 
1647 N N   . THR A 209 ? 0.5916 0.7353 0.8715 0.0238  -0.0651 0.0582  211 THR A N   
1648 C CA  . THR A 209 ? 0.5795 0.7124 0.8450 0.0275  -0.0639 0.0567  211 THR A CA  
1649 C C   . THR A 209 ? 0.5519 0.6800 0.8171 0.0362  -0.0545 0.0568  211 THR A C   
1650 O O   . THR A 209 ? 0.5504 0.6818 0.8210 0.0380  -0.0484 0.0567  211 THR A O   
1651 C CB  . THR A 209 ? 0.6092 0.7346 0.8577 0.0213  -0.0659 0.0505  211 THR A CB  
1652 O OG1 . THR A 209 ? 0.6274 0.7572 0.8750 0.0140  -0.0736 0.0504  211 THR A OG1 
1653 C CG2 . THR A 209 ? 0.6207 0.7345 0.8553 0.0242  -0.0648 0.0487  211 THR A CG2 
1654 N N   . LYS A 210 ? 0.5299 0.6496 0.7883 0.0417  -0.0533 0.0571  212 LYS A N   
1655 C CA  . LYS A 210 ? 0.5201 0.6327 0.7740 0.0499  -0.0450 0.0559  212 LYS A CA  
1656 C C   . LYS A 210 ? 0.4881 0.5927 0.7266 0.0481  -0.0420 0.0497  212 LYS A C   
1657 O O   . LYS A 210 ? 0.4862 0.5865 0.7151 0.0420  -0.0467 0.0460  212 LYS A O   
1658 C CB  . LYS A 210 ? 0.5704 0.6740 0.8195 0.0552  -0.0459 0.0564  212 LYS A CB  
1659 C CG  . LYS A 210 ? 0.6388 0.7350 0.8850 0.0651  -0.0373 0.0554  212 LYS A CG  
1660 C CD  . LYS A 210 ? 0.6898 0.7716 0.9228 0.0680  -0.0389 0.0518  212 LYS A CD  
1661 C CE  . LYS A 210 ? 0.7395 0.8111 0.9635 0.0766  -0.0307 0.0482  212 LYS A CE  
1662 N NZ  . LYS A 210 ? 0.7748 0.8306 0.9840 0.0778  -0.0337 0.0431  212 LYS A NZ  
1663 N N   . ASN A 211 ? 0.4516 0.5547 0.6886 0.0533  -0.0342 0.0491  213 ASN A N   
1664 C CA  . ASN A 211 ? 0.4262 0.5197 0.6475 0.0535  -0.0317 0.0440  213 ASN A CA  
1665 C C   . ASN A 211 ? 0.4262 0.5067 0.6348 0.0606  -0.0292 0.0413  213 ASN A C   
1666 O O   . ASN A 211 ? 0.4374 0.5172 0.6485 0.0685  -0.0226 0.0432  213 ASN A O   
1667 C CB  . ASN A 211 ? 0.4126 0.5113 0.6377 0.0549  -0.0251 0.0453  213 ASN A CB  
1668 C CG  . ASN A 211 ? 0.4063 0.5157 0.6431 0.0474  -0.0279 0.0467  213 ASN A CG  
1669 O OD1 . ASN A 211 ? 0.4103 0.5198 0.6451 0.0401  -0.0344 0.0440  213 ASN A OD1 
1670 N ND2 . ASN A 211 ? 0.3845 0.5024 0.6333 0.0489  -0.0228 0.0507  213 ASN A ND2 
1671 N N   . ARG A 212 ? 0.4100 0.4800 0.6059 0.0579  -0.0341 0.0368  214 ARG A N   
1672 C CA  . ARG A 212 ? 0.4249 0.4806 0.6067 0.0637  -0.0325 0.0328  214 ARG A CA  
1673 C C   . ARG A 212 ? 0.4177 0.4692 0.5896 0.0682  -0.0259 0.0307  214 ARG A C   
1674 O O   . ARG A 212 ? 0.4241 0.4683 0.5891 0.0762  -0.0207 0.0295  214 ARG A O   
1675 C CB  . ARG A 212 ? 0.4666 0.5122 0.6383 0.0587  -0.0397 0.0286  214 ARG A CB  
1676 C CG  . ARG A 212 ? 0.5435 0.5760 0.7081 0.0637  -0.0413 0.0264  214 ARG A CG  
1677 C CD  . ARG A 212 ? 0.5868 0.6226 0.7614 0.0623  -0.0454 0.0303  214 ARG A CD  
1678 N NE  . ARG A 212 ? 0.6374 0.6671 0.8077 0.0564  -0.0524 0.0290  214 ARG A NE  
1679 C CZ  . ARG A 212 ? 0.6752 0.7080 0.8520 0.0529  -0.0571 0.0330  214 ARG A CZ  
1680 N NH1 . ARG A 212 ? 0.6947 0.7369 0.8830 0.0546  -0.0567 0.0384  214 ARG A NH1 
1681 N NH2 . ARG A 212 ? 0.6853 0.7123 0.8578 0.0477  -0.0623 0.0322  214 ARG A NH2 
1682 N N   . PHE A 213 ? 0.4086 0.4644 0.5795 0.0634  -0.0259 0.0304  215 PHE A N   
1683 C CA  . PHE A 213 ? 0.4123 0.4650 0.5738 0.0669  -0.0204 0.0296  215 PHE A CA  
1684 C C   . PHE A 213 ? 0.4015 0.4674 0.5753 0.0634  -0.0172 0.0339  215 PHE A C   
1685 O O   . PHE A 213 ? 0.3842 0.4591 0.5705 0.0570  -0.0210 0.0355  215 PHE A O   
1686 C CB  . PHE A 213 ? 0.4107 0.4512 0.5557 0.0644  -0.0254 0.0243  215 PHE A CB  
1687 C CG  . PHE A 213 ? 0.4213 0.4494 0.5576 0.0651  -0.0309 0.0199  215 PHE A CG  
1688 C CD1 . PHE A 213 ? 0.4516 0.4690 0.5776 0.0731  -0.0279 0.0174  215 PHE A CD1 
1689 C CD2 . PHE A 213 ? 0.4256 0.4527 0.5651 0.0581  -0.0384 0.0186  215 PHE A CD2 
1690 C CE1 . PHE A 213 ? 0.4634 0.4687 0.5832 0.0736  -0.0335 0.0134  215 PHE A CE1 
1691 C CE2 . PHE A 213 ? 0.4398 0.4556 0.5732 0.0586  -0.0435 0.0154  215 PHE A CE2 
1692 C CZ  . PHE A 213 ? 0.4538 0.4588 0.5780 0.0661  -0.0414 0.0128  215 PHE A CZ  
1693 N N   . VAL A 214 ? 0.4083 0.4743 0.5776 0.0679  -0.0102 0.0358  216 VAL A N   
1694 C CA  . VAL A 214 ? 0.4107 0.4880 0.5915 0.0657  -0.0060 0.0407  216 VAL A CA  
1695 C C   . VAL A 214 ? 0.4003 0.4705 0.5658 0.0676  -0.0032 0.0400  216 VAL A C   
1696 O O   . VAL A 214 ? 0.4162 0.4759 0.5647 0.0739  -0.0003 0.0377  216 VAL A O   
1697 C CB  . VAL A 214 ? 0.4322 0.5198 0.6282 0.0710  0.0021  0.0469  216 VAL A CB  
1698 C CG1 . VAL A 214 ? 0.4395 0.5380 0.6480 0.0692  0.0070  0.0526  216 VAL A CG1 
1699 C CG2 . VAL A 214 ? 0.4347 0.5294 0.6462 0.0689  -0.0021 0.0483  216 VAL A CG2 
1700 N N   . VAL A 215 ? 0.3777 0.4531 0.5487 0.0621  -0.0045 0.0418  217 VAL A N   
1701 C CA  . VAL A 215 ? 0.3736 0.4446 0.5332 0.0638  -0.0016 0.0432  217 VAL A CA  
1702 C C   . VAL A 215 ? 0.3717 0.4548 0.5478 0.0610  0.0025  0.0496  217 VAL A C   
1703 O O   . VAL A 215 ? 0.3945 0.4760 0.5634 0.0635  0.0070  0.0531  217 VAL A O   
1704 C CB  . VAL A 215 ? 0.3754 0.4361 0.5217 0.0597  -0.0097 0.0384  217 VAL A CB  
1705 C CG1 . VAL A 215 ? 0.3899 0.4383 0.5218 0.0617  -0.0147 0.0322  217 VAL A CG1 
1706 C CG2 . VAL A 215 ? 0.3671 0.4341 0.5275 0.0508  -0.0156 0.0377  217 VAL A CG2 
1707 O OXT . VAL A 215 ? 0.2891 0.3825 0.4846 0.0561  0.0009  0.0511  217 VAL A OXT 
1708 N N   . ALA B 9   ? 1.0154 0.5260 0.5760 -0.1030 -0.2226 0.0351  11  ALA B N   
1709 C CA  . ALA B 9   ? 0.9979 0.5338 0.5953 -0.0914 -0.2313 0.0284  11  ALA B CA  
1710 C C   . ALA B 9   ? 0.9649 0.5408 0.6061 -0.0852 -0.2105 0.0230  11  ALA B C   
1711 O O   . ALA B 9   ? 0.9770 0.5597 0.6138 -0.0921 -0.1881 0.0227  11  ALA B O   
1712 C CB  . ALA B 9   ? 1.0086 0.5325 0.5836 -0.0974 -0.2360 0.0253  11  ALA B CB  
1713 N N   . ARG B 10  ? 0.9131 0.5146 0.5960 -0.0725 -0.2181 0.0185  12  ARG B N   
1714 C CA  . ARG B 10  ? 0.8656 0.5022 0.5878 -0.0662 -0.2008 0.0146  12  ARG B CA  
1715 C C   . ARG B 10  ? 0.8104 0.4639 0.5449 -0.0670 -0.1875 0.0091  12  ARG B C   
1716 O O   . ARG B 10  ? 0.8067 0.4570 0.5410 -0.0662 -0.1980 0.0051  12  ARG B O   
1717 C CB  . ARG B 10  ? 0.8737 0.5292 0.6333 -0.0536 -0.2123 0.0114  12  ARG B CB  
1718 C CG  . ARG B 10  ? 0.9489 0.5850 0.6991 -0.0508 -0.2301 0.0155  12  ARG B CG  
1719 C CD  . ARG B 10  ? 0.9890 0.6458 0.7734 -0.0416 -0.2290 0.0129  12  ARG B CD  
1720 N NE  . ARG B 10  ? 1.0689 0.7044 0.8438 -0.0388 -0.2458 0.0163  12  ARG B NE  
1721 C CZ  . ARG B 10  ? 1.1102 0.7545 0.9047 -0.0333 -0.2450 0.0152  12  ARG B CZ  
1722 N NH1 . ARG B 10  ? 1.1047 0.7793 0.9278 -0.0305 -0.2288 0.0109  12  ARG B NH1 
1723 N NH2 . ARG B 10  ? 1.1054 0.7264 0.8894 -0.0308 -0.2608 0.0183  12  ARG B NH2 
1724 N N   . ILE B 11  ? 0.7563 0.4274 0.5025 -0.0684 -0.1654 0.0088  13  ILE B N   
1725 C CA  . ILE B 11  ? 0.7203 0.4039 0.4754 -0.0696 -0.1502 0.0046  13  ILE B CA  
1726 C C   . ILE B 11  ? 0.6879 0.4013 0.4846 -0.0594 -0.1471 0.0005  13  ILE B C   
1727 O O   . ILE B 11  ? 0.6612 0.3944 0.4790 -0.0550 -0.1359 0.0018  13  ILE B O   
1728 C CB  . ILE B 11  ? 0.7073 0.3916 0.4513 -0.0766 -0.1279 0.0066  13  ILE B CB  
1729 C CG1 . ILE B 11  ? 0.7377 0.3922 0.4401 -0.0882 -0.1292 0.0105  13  ILE B CG1 
1730 C CG2 . ILE B 11  ? 0.6900 0.3822 0.4404 -0.0778 -0.1131 0.0020  13  ILE B CG2 
1731 C CD1 . ILE B 11  ? 0.7553 0.4067 0.4426 -0.0977 -0.1065 0.0102  13  ILE B CD1 
1732 N N   . ILE B 12  ? 0.6787 0.3944 0.4855 -0.0566 -0.1570 -0.0047 14  ILE B N   
1733 C CA  . ILE B 12  ? 0.6453 0.3859 0.4890 -0.0485 -0.1553 -0.0093 14  ILE B CA  
1734 C C   . ILE B 12  ? 0.6437 0.3886 0.4917 -0.0511 -0.1449 -0.0138 14  ILE B C   
1735 O O   . ILE B 12  ? 0.6743 0.4041 0.5052 -0.0564 -0.1524 -0.0171 14  ILE B O   
1736 C CB  . ILE B 12  ? 0.6357 0.3776 0.4940 -0.0428 -0.1767 -0.0132 14  ILE B CB  
1737 C CG1 . ILE B 12  ? 0.6284 0.3604 0.4793 -0.0402 -0.1891 -0.0088 14  ILE B CG1 
1738 C CG2 . ILE B 12  ? 0.6153 0.3840 0.5125 -0.0360 -0.1718 -0.0193 14  ILE B CG2 
1739 C CD1 . ILE B 12  ? 0.6345 0.3647 0.4975 -0.0344 -0.2099 -0.0125 14  ILE B CD1 
1740 N N   . TYR B 13  ? 0.6066 0.3706 0.4761 -0.0476 -0.1281 -0.0140 15  TYR B N   
1741 C CA  . TYR B 13  ? 0.5939 0.3625 0.4715 -0.0490 -0.1172 -0.0182 15  TYR B CA  
1742 C C   . TYR B 13  ? 0.5906 0.3794 0.5008 -0.0428 -0.1176 -0.0222 15  TYR B C   
1743 O O   . TYR B 13  ? 0.5925 0.3963 0.5192 -0.0375 -0.1125 -0.0193 15  TYR B O   
1744 C CB  . TYR B 13  ? 0.5762 0.3482 0.4514 -0.0497 -0.0965 -0.0144 15  TYR B CB  
1745 C CG  . TYR B 13  ? 0.5674 0.3213 0.4127 -0.0569 -0.0921 -0.0119 15  TYR B CG  
1746 C CD1 . TYR B 13  ? 0.5866 0.3215 0.4085 -0.0647 -0.0916 -0.0158 15  TYR B CD1 
1747 C CD2 . TYR B 13  ? 0.5741 0.3297 0.4139 -0.0570 -0.0873 -0.0065 15  TYR B CD2 
1748 C CE1 . TYR B 13  ? 0.5946 0.3120 0.3872 -0.0727 -0.0853 -0.0144 15  TYR B CE1 
1749 C CE2 . TYR B 13  ? 0.5852 0.3246 0.3980 -0.0650 -0.0810 -0.0051 15  TYR B CE2 
1750 C CZ  . TYR B 13  ? 0.6053 0.3250 0.3938 -0.0729 -0.0796 -0.0090 15  TYR B CZ  
1751 O OH  . TYR B 13  ? 0.6339 0.3363 0.3938 -0.0821 -0.0719 -0.0084 15  TYR B OH  
1752 N N   . ASP B 14  ? 0.5719 0.3611 0.4910 -0.0444 -0.1234 -0.0294 16  ASP B N   
1753 C CA  . ASP B 14  ? 0.5466 0.3545 0.4960 -0.0408 -0.1181 -0.0339 16  ASP B CA  
1754 C C   . ASP B 14  ? 0.5361 0.3491 0.4906 -0.0409 -0.0969 -0.0314 16  ASP B C   
1755 O O   . ASP B 14  ? 0.5433 0.3458 0.4806 -0.0436 -0.0863 -0.0278 16  ASP B O   
1756 C CB  . ASP B 14  ? 0.5425 0.3512 0.5033 -0.0432 -0.1309 -0.0434 16  ASP B CB  
1757 C CG  . ASP B 14  ? 0.5637 0.3580 0.5084 -0.0507 -0.1307 -0.0478 16  ASP B CG  
1758 O OD1 . ASP B 14  ? 0.5820 0.3693 0.5149 -0.0538 -0.1147 -0.0453 16  ASP B OD1 
1759 O OD2 . ASP B 14  ? 0.5625 0.3529 0.5075 -0.0533 -0.1468 -0.0542 16  ASP B OD2 
1760 N N   . ARG B 15  ? 0.5062 0.3346 0.4849 -0.0379 -0.0905 -0.0336 17  ARG B N   
1761 C CA  . ARG B 15  ? 0.4912 0.3238 0.4761 -0.0369 -0.0721 -0.0302 17  ARG B CA  
1762 C C   . ARG B 15  ? 0.5246 0.3435 0.4989 -0.0421 -0.0635 -0.0328 17  ARG B C   
1763 O O   . ARG B 15  ? 0.5343 0.3489 0.5025 -0.0408 -0.0498 -0.0276 17  ARG B O   
1764 C CB  . ARG B 15  ? 0.4673 0.3158 0.4769 -0.0347 -0.0683 -0.0331 17  ARG B CB  
1765 C CG  . ARG B 15  ? 0.4979 0.3484 0.5109 -0.0332 -0.0504 -0.0277 17  ARG B CG  
1766 C CD  . ARG B 15  ? 0.5161 0.3788 0.5496 -0.0336 -0.0460 -0.0316 17  ARG B CD  
1767 N NE  . ARG B 15  ? 0.5618 0.4230 0.5955 -0.0326 -0.0299 -0.0256 17  ARG B NE  
1768 C CZ  . ARG B 15  ? 0.5987 0.4491 0.6300 -0.0359 -0.0197 -0.0262 17  ARG B CZ  
1769 N NH1 . ARG B 15  ? 0.6113 0.4524 0.6396 -0.0412 -0.0233 -0.0336 17  ARG B NH1 
1770 N NH2 . ARG B 15  ? 0.6050 0.4524 0.6357 -0.0339 -0.0063 -0.0194 17  ARG B NH2 
1771 N N   . ALA B 16  ? 0.5436 0.3555 0.5162 -0.0478 -0.0717 -0.0411 18  ALA B N   
1772 C CA  . ALA B 16  ? 0.5578 0.3551 0.5187 -0.0539 -0.0638 -0.0450 18  ALA B CA  
1773 C C   . ALA B 16  ? 0.5882 0.3694 0.5223 -0.0562 -0.0598 -0.0414 18  ALA B C   
1774 O O   . ALA B 16  ? 0.5964 0.3695 0.5247 -0.0572 -0.0446 -0.0405 18  ALA B O   
1775 C CB  . ALA B 16  ? 0.5435 0.3379 0.5076 -0.0602 -0.0762 -0.0553 18  ALA B CB  
1776 N N   . PHE B 17  ? 0.6083 0.3837 0.5259 -0.0572 -0.0724 -0.0397 19  PHE B N   
1777 C CA  . PHE B 17  ? 0.6415 0.4013 0.5321 -0.0608 -0.0676 -0.0368 19  PHE B CA  
1778 C C   . PHE B 17  ? 0.6319 0.3980 0.5275 -0.0556 -0.0503 -0.0296 19  PHE B C   
1779 O O   . PHE B 17  ? 0.6363 0.3933 0.5233 -0.0577 -0.0363 -0.0302 19  PHE B O   
1780 C CB  . PHE B 17  ? 0.6764 0.4287 0.5489 -0.0628 -0.0850 -0.0350 19  PHE B CB  
1781 C CG  . PHE B 17  ? 0.7295 0.4612 0.5690 -0.0701 -0.0813 -0.0344 19  PHE B CG  
1782 C CD1 . PHE B 17  ? 0.7478 0.4790 0.5795 -0.0692 -0.0692 -0.0286 19  PHE B CD1 
1783 C CD2 . PHE B 17  ? 0.7763 0.4895 0.5929 -0.0787 -0.0881 -0.0405 19  PHE B CD2 
1784 C CE1 . PHE B 17  ? 0.7813 0.4937 0.5830 -0.0772 -0.0632 -0.0292 19  PHE B CE1 
1785 C CE2 . PHE B 17  ? 0.8075 0.5002 0.5909 -0.0868 -0.0826 -0.0406 19  PHE B CE2 
1786 C CZ  . PHE B 17  ? 0.8035 0.4959 0.5799 -0.0862 -0.0694 -0.0350 19  PHE B CZ  
1787 N N   . LEU B 18  ? 0.6117 0.3936 0.5225 -0.0487 -0.0513 -0.0236 20  LEU B N   
1788 C CA  . LEU B 18  ? 0.6123 0.4019 0.5288 -0.0434 -0.0377 -0.0167 20  LEU B CA  
1789 C C   . LEU B 18  ? 0.6200 0.4101 0.5478 -0.0407 -0.0218 -0.0165 20  LEU B C   
1790 O O   . LEU B 18  ? 0.6386 0.4263 0.5643 -0.0387 -0.0094 -0.0137 20  LEU B O   
1791 C CB  . LEU B 18  ? 0.5972 0.4044 0.5288 -0.0370 -0.0430 -0.0112 20  LEU B CB  
1792 C CG  . LEU B 18  ? 0.5946 0.4008 0.5165 -0.0384 -0.0569 -0.0103 20  LEU B CG  
1793 C CD1 . LEU B 18  ? 0.5697 0.3926 0.5082 -0.0326 -0.0616 -0.0070 20  LEU B CD1 
1794 C CD2 . LEU B 18  ? 0.6121 0.4094 0.5150 -0.0419 -0.0525 -0.0073 20  LEU B CD2 
1795 N N   . MET B 19  ? 0.6065 0.3993 0.5471 -0.0407 -0.0222 -0.0198 21  MET B N   
1796 C CA  . MET B 19  ? 0.6132 0.4018 0.5619 -0.0393 -0.0082 -0.0200 21  MET B CA  
1797 C C   . MET B 19  ? 0.6430 0.4132 0.5772 -0.0449 0.0004  -0.0256 21  MET B C   
1798 O O   . MET B 19  ? 0.6457 0.4108 0.5838 -0.0417 0.0148  -0.0237 21  MET B O   
1799 C CB  . MET B 19  ? 0.6084 0.4025 0.5724 -0.0404 -0.0104 -0.0235 21  MET B CB  
1800 C CG  . MET B 19  ? 0.5932 0.4045 0.5723 -0.0353 -0.0145 -0.0189 21  MET B CG  
1801 S SD  . MET B 19  ? 0.6373 0.4568 0.6215 -0.0263 -0.0042 -0.0071 21  MET B SD  
1802 C CE  . MET B 19  ? 0.6168 0.4493 0.6174 -0.0249 -0.0048 -0.0059 21  MET B CE  
1803 N N   . ALA B 20  ? 0.6659 0.4249 0.5829 -0.0529 -0.0082 -0.0326 22  ALA B N   
1804 C CA  . ALA B 20  ? 0.6919 0.4319 0.5914 -0.0596 0.0001  -0.0390 22  ALA B CA  
1805 C C   . ALA B 20  ? 0.7246 0.4589 0.6107 -0.0591 0.0098  -0.0363 22  ALA B C   
1806 O O   . ALA B 20  ? 0.7340 0.4556 0.6125 -0.0617 0.0234  -0.0404 22  ALA B O   
1807 C CB  . ALA B 20  ? 0.6919 0.4216 0.5750 -0.0690 -0.0142 -0.0471 22  ALA B CB  
1808 N N   . CYS B 21  ? 0.7232 0.4670 0.6074 -0.0563 0.0037  -0.0303 23  CYS B N   
1809 C CA  . CYS B 21  ? 0.7404 0.4827 0.6167 -0.0558 0.0139  -0.0278 23  CYS B CA  
1810 C C   . CYS B 21  ? 0.7298 0.4835 0.6283 -0.0461 0.0285  -0.0225 23  CYS B C   
1811 O O   . CYS B 21  ? 0.7414 0.4975 0.6391 -0.0448 0.0375  -0.0211 23  CYS B O   
1812 C CB  . CYS B 21  ? 0.7614 0.5091 0.6285 -0.0571 0.0024  -0.0235 23  CYS B CB  
1813 S SG  . CYS B 21  ? 0.8450 0.5764 0.6836 -0.0673 -0.0169 -0.0280 23  CYS B SG  
1814 N N   . ARG B 22  ? 0.7058 0.4659 0.6235 -0.0396 0.0307  -0.0197 24  ARG B N   
1815 C CA  . ARG B 22  ? 0.6934 0.4633 0.6313 -0.0292 0.0412  -0.0130 24  ARG B CA  
1816 C C   . ARG B 22  ? 0.7360 0.4924 0.6767 -0.0279 0.0573  -0.0169 24  ARG B C   
1817 O O   . ARG B 22  ? 0.7632 0.5036 0.6927 -0.0350 0.0597  -0.0247 24  ARG B O   
1818 C CB  . ARG B 22  ? 0.6559 0.4369 0.6094 -0.0236 0.0350  -0.0071 24  ARG B CB  
1819 C CG  . ARG B 22  ? 0.6302 0.4171 0.6013 -0.0135 0.0437  0.0006  24  ARG B CG  
1820 C CD  . ARG B 22  ? 0.6254 0.4186 0.6050 -0.0117 0.0379  0.0047  24  ARG B CD  
1821 N NE  . ARG B 22  ? 0.6242 0.4258 0.6164 -0.0021 0.0414  0.0146  24  ARG B NE  
1822 C CZ  . ARG B 22  ? 0.6572 0.4660 0.6550 0.0000  0.0372  0.0199  24  ARG B CZ  
1823 N NH1 . ARG B 22  ? 0.6934 0.5042 0.6892 -0.0064 0.0304  0.0153  24  ARG B NH1 
1824 N NH2 . ARG B 22  ? 0.6506 0.4649 0.6562 0.0085  0.0397  0.0295  24  ARG B NH2 
1825 N N   . GLY B 23  ? 0.7326 0.4955 0.6891 -0.0185 0.0673  -0.0118 25  GLY B N   
1826 C CA  . GLY B 23  ? 0.7438 0.4946 0.7077 -0.0143 0.0827  -0.0144 25  GLY B CA  
1827 C C   . GLY B 23  ? 0.7577 0.5118 0.7401 -0.0040 0.0845  -0.0059 25  GLY B C   
1828 O O   . GLY B 23  ? 0.7643 0.5160 0.7464 -0.0056 0.0788  -0.0038 25  GLY B O   
1829 N N   . LYS B 34  ? 0.8427 0.5117 0.5545 -0.1177 0.0538  -0.0379 36  LYS B N   
1830 C CA  . LYS B 34  ? 0.8250 0.5179 0.5705 -0.1041 0.0420  -0.0304 36  LYS B CA  
1831 C C   . LYS B 34  ? 0.8076 0.4937 0.5385 -0.1052 0.0185  -0.0247 36  LYS B C   
1832 O O   . LYS B 34  ? 0.8363 0.5029 0.5344 -0.1157 0.0123  -0.0240 36  LYS B O   
1833 C CB  . LYS B 34  ? 0.8530 0.5695 0.6259 -0.0981 0.0520  -0.0270 36  LYS B CB  
1834 C CG  . LYS B 34  ? 0.9118 0.6425 0.7129 -0.0911 0.0715  -0.0311 36  LYS B CG  
1835 C CD  . LYS B 34  ? 0.9657 0.7195 0.7925 -0.0865 0.0800  -0.0286 36  LYS B CD  
1836 C CE  . LYS B 34  ? 1.0047 0.7752 0.8657 -0.0759 0.0953  -0.0313 36  LYS B CE  
1837 N NZ  . LYS B 34  ? 1.0165 0.8117 0.9048 -0.0713 0.1020  -0.0293 36  LYS B NZ  
1838 N N   . HIS B 35  ? 0.7657 0.4669 0.5209 -0.0945 0.0056  -0.0207 37  HIS B N   
1839 C CA  . HIS B 35  ? 0.7503 0.4467 0.4972 -0.0939 -0.0170 -0.0168 37  HIS B CA  
1840 C C   . HIS B 35  ? 0.7229 0.4332 0.4823 -0.0897 -0.0220 -0.0102 37  HIS B C   
1841 O O   . HIS B 35  ? 0.7058 0.4396 0.4968 -0.0799 -0.0183 -0.0076 37  HIS B O   
1842 C CB  . HIS B 35  ? 0.7372 0.4424 0.5043 -0.0859 -0.0265 -0.0180 37  HIS B CB  
1843 C CG  . HIS B 35  ? 0.7582 0.4477 0.5108 -0.0916 -0.0238 -0.0252 37  HIS B CG  
1844 N ND1 . HIS B 35  ? 0.7782 0.4718 0.5442 -0.0894 -0.0065 -0.0296 37  HIS B ND1 
1845 C CD2 . HIS B 35  ? 0.7819 0.4512 0.5078 -0.0993 -0.0371 -0.0287 37  HIS B CD2 
1846 C CE1 . HIS B 35  ? 0.7903 0.4662 0.5372 -0.0965 -0.0085 -0.0363 37  HIS B CE1 
1847 N NE2 . HIS B 35  ? 0.8061 0.4677 0.5283 -0.1029 -0.0273 -0.0361 37  HIS B NE2 
1848 N N   . PRO B 36  ? 0.7158 0.4110 0.4497 -0.0973 -0.0302 -0.0074 38  PRO B N   
1849 C CA  . PRO B 36  ? 0.6887 0.3959 0.4337 -0.0946 -0.0331 -0.0019 38  PRO B CA  
1850 C C   . PRO B 36  ? 0.6622 0.3834 0.4290 -0.0844 -0.0493 0.0016  38  PRO B C   
1851 O O   . PRO B 36  ? 0.6634 0.3766 0.4258 -0.0826 -0.0641 0.0006  38  PRO B O   
1852 C CB  . PRO B 36  ? 0.7236 0.4045 0.4305 -0.1067 -0.0386 -0.0002 38  PRO B CB  
1853 C CG  . PRO B 36  ? 0.7516 0.4087 0.4310 -0.1117 -0.0496 -0.0027 38  PRO B CG  
1854 C CD  . PRO B 36  ? 0.7319 0.3963 0.4235 -0.1094 -0.0375 -0.0087 38  PRO B CD  
1855 N N   . LEU B 37  ? 0.6291 0.3719 0.4204 -0.0782 -0.0465 0.0049  39  LEU B N   
1856 C CA  . LEU B 37  ? 0.5913 0.3464 0.4009 -0.0700 -0.0604 0.0077  39  LEU B CA  
1857 C C   . LEU B 37  ? 0.6073 0.3482 0.3986 -0.0748 -0.0726 0.0107  39  LEU B C   
1858 O O   . LEU B 37  ? 0.6194 0.3483 0.3906 -0.0837 -0.0664 0.0119  39  LEU B O   
1859 C CB  . LEU B 37  ? 0.5503 0.3336 0.3917 -0.0617 -0.0518 0.0095  39  LEU B CB  
1860 C CG  . LEU B 37  ? 0.5196 0.3162 0.3805 -0.0557 -0.0398 0.0079  39  LEU B CG  
1861 C CD1 . LEU B 37  ? 0.4895 0.3122 0.3788 -0.0473 -0.0345 0.0114  39  LEU B CD1 
1862 C CD2 . LEU B 37  ? 0.5133 0.3054 0.3771 -0.0525 -0.0467 0.0052  39  LEU B CD2 
1863 N N   . GLN B 38  ? 0.5941 0.3349 0.3921 -0.0692 -0.0894 0.0114  40  GLN B N   
1864 C CA  . GLN B 38  ? 0.5840 0.3121 0.3695 -0.0714 -0.1021 0.0144  40  GLN B CA  
1865 C C   . GLN B 38  ? 0.5596 0.2993 0.3528 -0.0731 -0.0931 0.0169  40  GLN B C   
1866 O O   . GLN B 38  ? 0.5845 0.3081 0.3578 -0.0803 -0.0959 0.0194  40  GLN B O   
1867 C CB  . GLN B 38  ? 0.6024 0.3365 0.4057 -0.0622 -0.1191 0.0132  40  GLN B CB  
1868 C CG  . GLN B 38  ? 0.6258 0.3470 0.4208 -0.0621 -0.1335 0.0157  40  GLN B CG  
1869 C CD  . GLN B 38  ? 0.7009 0.3893 0.4608 -0.0691 -0.1458 0.0180  40  GLN B CD  
1870 O OE1 . GLN B 38  ? 0.6938 0.3690 0.4357 -0.0735 -0.1466 0.0169  40  GLN B OE1 
1871 N NE2 . GLN B 38  ? 0.7311 0.4039 0.4790 -0.0706 -0.1559 0.0214  40  GLN B NE2 
1872 N N   . ASN B 39  ? 0.5194 0.2866 0.3411 -0.0668 -0.0831 0.0162  41  ASN B N   
1873 C CA  . ASN B 39  ? 0.4980 0.2823 0.3333 -0.0670 -0.0753 0.0178  41  ASN B CA  
1874 C C   . ASN B 39  ? 0.4805 0.2821 0.3290 -0.0669 -0.0578 0.0171  41  ASN B C   
1875 O O   . ASN B 39  ? 0.4512 0.2572 0.3072 -0.0627 -0.0523 0.0156  41  ASN B O   
1876 C CB  . ASN B 39  ? 0.4944 0.2967 0.3534 -0.0581 -0.0828 0.0177  41  ASN B CB  
1877 C CG  . ASN B 39  ? 0.5784 0.3661 0.4287 -0.0579 -0.0985 0.0178  41  ASN B CG  
1878 O OD1 . ASN B 39  ? 0.6065 0.3805 0.4409 -0.0645 -0.1008 0.0195  41  ASN B OD1 
1879 N ND2 . ASN B 39  ? 0.5905 0.3798 0.4514 -0.0508 -0.1091 0.0156  41  ASN B ND2 
1880 N N   . ARG B 40  ? 0.4668 0.2774 0.3189 -0.0715 -0.0491 0.0177  42  ARG B N   
1881 C CA  . ARG B 40  ? 0.4459 0.2802 0.3203 -0.0684 -0.0355 0.0171  42  ARG B CA  
1882 C C   . ARG B 40  ? 0.4020 0.2606 0.3025 -0.0588 -0.0403 0.0191  42  ARG B C   
1883 O O   . ARG B 40  ? 0.3975 0.2569 0.2982 -0.0587 -0.0500 0.0199  42  ARG B O   
1884 C CB  . ARG B 40  ? 0.4783 0.3136 0.3476 -0.0783 -0.0247 0.0159  42  ARG B CB  
1885 C CG  . ARG B 40  ? 0.5152 0.3744 0.4088 -0.0754 -0.0099 0.0141  42  ARG B CG  
1886 C CD  . ARG B 40  ? 0.5633 0.4141 0.4444 -0.0876 0.0045  0.0102  42  ARG B CD  
1887 N NE  . ARG B 40  ? 0.5593 0.4341 0.4671 -0.0848 0.0190  0.0072  42  ARG B NE  
1888 C CZ  . ARG B 40  ? 0.5723 0.4690 0.5003 -0.0864 0.0236  0.0059  42  ARG B CZ  
1889 N NH1 . ARG B 40  ? 0.5352 0.4318 0.4578 -0.0922 0.0160  0.0073  42  ARG B NH1 
1890 N NH2 . ARG B 40  ? 0.5735 0.4920 0.5280 -0.0825 0.0357  0.0028  42  ARG B NH2 
1891 N N   . TRP B 41  ? 0.3688 0.2455 0.2900 -0.0511 -0.0332 0.0197  43  TRP B N   
1892 C CA  . TRP B 41  ? 0.3702 0.2666 0.3120 -0.0419 -0.0376 0.0222  43  TRP B CA  
1893 C C   . TRP B 41  ? 0.3832 0.3013 0.3447 -0.0386 -0.0288 0.0236  43  TRP B C   
1894 O O   . TRP B 41  ? 0.3941 0.3128 0.3590 -0.0395 -0.0178 0.0222  43  TRP B O   
1895 C CB  . TRP B 41  ? 0.3540 0.2480 0.3004 -0.0345 -0.0396 0.0226  43  TRP B CB  
1896 C CG  . TRP B 41  ? 0.3585 0.2344 0.2905 -0.0365 -0.0497 0.0205  43  TRP B CG  
1897 C CD1 . TRP B 41  ? 0.3839 0.2391 0.2976 -0.0416 -0.0506 0.0181  43  TRP B CD1 
1898 C CD2 . TRP B 41  ? 0.3633 0.2400 0.2979 -0.0340 -0.0614 0.0198  43  TRP B CD2 
1899 N NE1 . TRP B 41  ? 0.3871 0.2307 0.2929 -0.0417 -0.0637 0.0166  43  TRP B NE1 
1900 C CE2 . TRP B 41  ? 0.3828 0.2399 0.3032 -0.0366 -0.0698 0.0171  43  TRP B CE2 
1901 C CE3 . TRP B 41  ? 0.3613 0.2529 0.3086 -0.0301 -0.0655 0.0205  43  TRP B CE3 
1902 C CZ2 . TRP B 41  ? 0.3881 0.2420 0.3107 -0.0342 -0.0820 0.0149  43  TRP B CZ2 
1903 C CZ3 . TRP B 41  ? 0.3718 0.2593 0.3196 -0.0285 -0.0757 0.0178  43  TRP B CZ3 
1904 C CH2 . TRP B 41  ? 0.3826 0.2520 0.3199 -0.0301 -0.0838 0.0149  43  TRP B CH2 
1905 N N   . ALA B 42  ? 0.3626 0.2989 0.3378 -0.0347 -0.0340 0.0258  44  ALA B N   
1906 C CA  . ALA B 42  ? 0.3436 0.3028 0.3393 -0.0305 -0.0292 0.0276  44  ALA B CA  
1907 C C   . ALA B 42  ? 0.3385 0.3094 0.3461 -0.0205 -0.0337 0.0320  44  ALA B C   
1908 O O   . ALA B 42  ? 0.3236 0.2934 0.3268 -0.0194 -0.0420 0.0327  44  ALA B O   
1909 C CB  . ALA B 42  ? 0.3314 0.3014 0.3299 -0.0370 -0.0317 0.0261  44  ALA B CB  
1910 N N   . LEU B 43  ? 0.3434 0.3238 0.3656 -0.0132 -0.0277 0.0348  45  LEU B N   
1911 C CA  . LEU B 43  ? 0.3418 0.3322 0.3740 -0.0038 -0.0313 0.0403  45  LEU B CA  
1912 C C   . LEU B 43  ? 0.3442 0.3574 0.3915 -0.0012 -0.0351 0.0430  45  LEU B C   
1913 O O   . LEU B 43  ? 0.3445 0.3689 0.4059 -0.0009 -0.0297 0.0417  45  LEU B O   
1914 C CB  . LEU B 43  ? 0.3410 0.3261 0.3800 0.0036  -0.0234 0.0427  45  LEU B CB  
1915 C CG  . LEU B 43  ? 0.3445 0.3363 0.3914 0.0133  -0.0268 0.0499  45  LEU B CG  
1916 C CD1 . LEU B 43  ? 0.3573 0.3419 0.3916 0.0120  -0.0334 0.0509  45  LEU B CD1 
1917 C CD2 . LEU B 43  ? 0.3366 0.3208 0.3902 0.0201  -0.0185 0.0520  45  LEU B CD2 
1918 N N   . TRP B 44  ? 0.3493 0.3699 0.3945 0.0005  -0.0442 0.0459  46  TRP B N   
1919 C CA  . TRP B 44  ? 0.3581 0.3996 0.4141 0.0025  -0.0507 0.0486  46  TRP B CA  
1920 C C   . TRP B 44  ? 0.4123 0.4583 0.4706 0.0117  -0.0550 0.0561  46  TRP B C   
1921 O O   . TRP B 44  ? 0.4142 0.4468 0.4616 0.0136  -0.0544 0.0580  46  TRP B O   
1922 C CB  . TRP B 44  ? 0.3506 0.3941 0.3968 -0.0051 -0.0581 0.0450  46  TRP B CB  
1923 C CG  . TRP B 44  ? 0.3737 0.4080 0.4125 -0.0149 -0.0555 0.0386  46  TRP B CG  
1924 C CD1 . TRP B 44  ? 0.3930 0.4061 0.4167 -0.0191 -0.0538 0.0354  46  TRP B CD1 
1925 C CD2 . TRP B 44  ? 0.3764 0.4212 0.4216 -0.0221 -0.0547 0.0349  46  TRP B CD2 
1926 N NE1 . TRP B 44  ? 0.3988 0.4063 0.4164 -0.0283 -0.0526 0.0310  46  TRP B NE1 
1927 C CE2 . TRP B 44  ? 0.3928 0.4194 0.4234 -0.0309 -0.0521 0.0302  46  TRP B CE2 
1928 C CE3 . TRP B 44  ? 0.3761 0.4440 0.4379 -0.0225 -0.0570 0.0348  46  TRP B CE3 
1929 C CZ2 . TRP B 44  ? 0.4118 0.4405 0.4422 -0.0408 -0.0497 0.0259  46  TRP B CZ2 
1930 C CZ3 . TRP B 44  ? 0.3896 0.4626 0.4545 -0.0324 -0.0544 0.0293  46  TRP B CZ3 
1931 C CH2 . TRP B 44  ? 0.4059 0.4584 0.4541 -0.0418 -0.0502 0.0250  46  TRP B CH2 
1932 N N   . PHE B 45  ? 0.4401 0.5051 0.5127 0.0169  -0.0599 0.0603  47  PHE B N   
1933 C CA  . PHE B 45  ? 0.4925 0.5627 0.5649 0.0248  -0.0668 0.0685  47  PHE B CA  
1934 C C   . PHE B 45  ? 0.5074 0.5952 0.5795 0.0213  -0.0777 0.0685  47  PHE B C   
1935 O O   . PHE B 45  ? 0.4903 0.5935 0.5751 0.0173  -0.0793 0.0640  47  PHE B O   
1936 C CB  . PHE B 45  ? 0.5132 0.5898 0.6045 0.0354  -0.0645 0.0738  47  PHE B CB  
1937 C CG  . PHE B 45  ? 0.5542 0.6350 0.6456 0.0447  -0.0730 0.0838  47  PHE B CG  
1938 C CD1 . PHE B 45  ? 0.5955 0.6582 0.6700 0.0476  -0.0720 0.0897  47  PHE B CD1 
1939 C CD2 . PHE B 45  ? 0.5661 0.6682 0.6742 0.0500  -0.0823 0.0873  47  PHE B CD2 
1940 C CE1 . PHE B 45  ? 0.6168 0.6798 0.6871 0.0553  -0.0798 0.0999  47  PHE B CE1 
1941 C CE2 . PHE B 45  ? 0.5840 0.6876 0.6893 0.0588  -0.0920 0.0976  47  PHE B CE2 
1942 C CZ  . PHE B 45  ? 0.6020 0.6845 0.6866 0.0612  -0.0905 0.1043  47  PHE B CZ  
1943 N N   . PHE B 46  ? 0.5416 0.6268 0.5984 0.0215  -0.0845 0.0725  48  PHE B N   
1944 C CA  . PHE B 46  ? 0.5912 0.6908 0.6433 0.0174  -0.0952 0.0721  48  PHE B CA  
1945 C C   . PHE B 46  ? 0.6430 0.7412 0.6831 0.0233  -0.1025 0.0814  48  PHE B C   
1946 O O   . PHE B 46  ? 0.6438 0.7259 0.6748 0.0279  -0.0976 0.0866  48  PHE B O   
1947 C CB  . PHE B 46  ? 0.6113 0.7042 0.6492 0.0067  -0.0945 0.0636  48  PHE B CB  
1948 C CG  . PHE B 46  ? 0.6542 0.7588 0.6843 0.0008  -0.1040 0.0614  48  PHE B CG  
1949 C CD1 . PHE B 46  ? 0.6600 0.7810 0.7009 -0.0049 -0.1085 0.0563  48  PHE B CD1 
1950 C CD2 . PHE B 46  ? 0.6925 0.7911 0.7035 -0.0001 -0.1075 0.0636  48  PHE B CD2 
1951 C CE1 . PHE B 46  ? 0.6745 0.8060 0.7077 -0.0109 -0.1174 0.0536  48  PHE B CE1 
1952 C CE2 . PHE B 46  ? 0.6998 0.8081 0.7015 -0.0063 -0.1157 0.0607  48  PHE B CE2 
1953 C CZ  . PHE B 46  ? 0.6833 0.8079 0.6962 -0.0116 -0.1211 0.0556  48  PHE B CZ  
1954 N N   . LYS B 47  ? 0.6714 0.7855 0.7096 0.0222  -0.1144 0.0835  49  LYS B N   
1955 C CA  . LYS B 47  ? 0.7027 0.8150 0.7259 0.0267  -0.1232 0.0930  49  LYS B CA  
1956 C C   . LYS B 47  ? 0.7389 0.8640 0.7510 0.0194  -0.1344 0.0904  49  LYS B C   
1957 O O   . LYS B 47  ? 0.7295 0.8727 0.7561 0.0153  -0.1391 0.0844  49  LYS B O   
1958 C CB  . LYS B 47  ? 0.6969 0.8166 0.7366 0.0393  -0.1291 0.1030  49  LYS B CB  
1959 C CG  . LYS B 47  ? 0.7392 0.8467 0.7588 0.0453  -0.1354 0.1150  49  LYS B CG  
1960 C CD  . LYS B 47  ? 0.7832 0.8989 0.8187 0.0584  -0.1453 0.1254  49  LYS B CD  
1961 C CE  . LYS B 47  ? 0.8037 0.9449 0.8492 0.0593  -0.1626 0.1265  49  LYS B CE  
1962 N NZ  . LYS B 47  ? 0.7830 0.9300 0.8415 0.0737  -0.1751 0.1383  49  LYS B NZ  
1963 N N   . ASN B 48  ? 0.7796 0.8949 0.7652 0.0168  -0.1379 0.0942  50  ASN B N   
1964 C CA  . ASN B 48  ? 0.8146 0.9387 0.7848 0.0081  -0.1469 0.0902  50  ASN B CA  
1965 C C   . ASN B 48  ? 0.8331 0.9762 0.8078 0.0121  -0.1639 0.0968  50  ASN B C   
1966 O O   . ASN B 48  ? 0.8453 0.9881 0.7970 0.0077  -0.1728 0.0992  50  ASN B O   
1967 C CB  . ASN B 48  ? 0.8528 0.9584 0.7911 0.0022  -0.1424 0.0902  50  ASN B CB  
1968 C CG  . ASN B 48  ? 0.9127 1.0250 0.8352 -0.0089 -0.1479 0.0820  50  ASN B CG  
1969 O OD1 . ASN B 48  ? 0.9201 1.0406 0.8532 -0.0155 -0.1464 0.0714  50  ASN B OD1 
1970 N ND2 . ASN B 48  ? 0.9310 1.0386 0.8262 -0.0120 -0.1541 0.0866  50  ASN B ND2 
1971 N N   . ASP B 49  ? 0.8291 0.9895 0.8338 0.0200  -0.1689 0.0992  51  ASP B N   
1972 C CA  . ASP B 49  ? 0.8363 1.0175 0.8499 0.0245  -0.1867 0.1048  51  ASP B CA  
1973 C C   . ASP B 49  ? 0.8395 1.0391 0.8533 0.0130  -0.1945 0.0949  51  ASP B C   
1974 O O   . ASP B 49  ? 0.8305 1.0349 0.8559 0.0051  -0.1861 0.0838  51  ASP B O   
1975 C CB  . ASP B 49  ? 0.8475 1.0444 0.8977 0.0361  -0.1890 0.1080  51  ASP B CB  
1976 C CG  . ASP B 49  ? 0.9109 1.1269 0.9722 0.0445  -0.2089 0.1162  51  ASP B CG  
1977 O OD1 . ASP B 49  ? 0.9319 1.1455 0.9672 0.0419  -0.2218 0.1215  51  ASP B OD1 
1978 O OD2 . ASP B 49  ? 0.9265 1.1598 1.0224 0.0537  -0.2117 0.1168  51  ASP B OD2 
1979 N N   . LYS B 50  ? 0.8475 1.0557 0.8466 0.0116  -0.2108 0.0992  52  LYS B N   
1980 C CA  . LYS B 50  ? 0.8511 1.0756 0.8465 -0.0004 -0.2192 0.0896  52  LYS B CA  
1981 C C   . LYS B 50  ? 0.8354 1.0917 0.8652 0.0023  -0.2319 0.0875  52  LYS B C   
1982 O O   . LYS B 50  ? 0.8191 1.0908 0.8614 -0.0080 -0.2315 0.0758  52  LYS B O   
1983 C CB  . LYS B 50  ? 0.8704 1.0855 0.8268 -0.0061 -0.2291 0.0934  52  LYS B CB  
1984 C CG  . LYS B 50  ? 0.9285 1.1203 0.8552 -0.0164 -0.2146 0.0865  52  LYS B CG  
1985 C CD  . LYS B 50  ? 0.9678 1.1682 0.8969 -0.0300 -0.2117 0.0710  52  LYS B CD  
1986 C CE  . LYS B 50  ? 1.0025 1.1834 0.9225 -0.0364 -0.1938 0.0619  52  LYS B CE  
1987 N NZ  . LYS B 50  ? 1.0146 1.2022 0.9358 -0.0491 -0.1928 0.0476  52  LYS B NZ  
1988 N N   . SER B 51  ? 0.8367 1.1024 0.8832 0.0162  -0.2428 0.0984  53  SER B N   
1989 C CA  . SER B 51  ? 0.8266 1.1244 0.9131 0.0215  -0.2542 0.0965  53  SER B CA  
1990 C C   . SER B 51  ? 0.8231 1.1344 0.9420 0.0154  -0.2401 0.0835  53  SER B C   
1991 O O   . SER B 51  ? 0.8026 1.1426 0.9504 0.0123  -0.2474 0.0765  53  SER B O   
1992 C CB  . SER B 51  ? 0.8319 1.1307 0.9356 0.0398  -0.2613 0.1096  53  SER B CB  
1993 O OG  . SER B 51  ? 0.8305 1.1608 0.9792 0.0463  -0.2692 0.1064  53  SER B OG  
1994 N N   . LYS B 52  ? 0.8377 1.1274 0.9503 0.0132  -0.2201 0.0803  54  LYS B N   
1995 C CA  . LYS B 52  ? 0.8416 1.1361 0.9772 0.0074  -0.2048 0.0696  54  LYS B CA  
1996 C C   . LYS B 52  ? 0.8721 1.1492 0.9834 -0.0070 -0.1941 0.0605  54  LYS B C   
1997 O O   . LYS B 52  ? 0.8939 1.1484 0.9741 -0.0083 -0.1915 0.0637  54  LYS B O   
1998 C CB  . LYS B 52  ? 0.8542 1.1359 1.0028 0.0185  -0.1917 0.0745  54  LYS B CB  
1999 C CG  . LYS B 52  ? 0.8831 1.1732 1.0491 0.0352  -0.2018 0.0857  54  LYS B CG  
2000 C CD  . LYS B 52  ? 0.9396 1.2191 1.1226 0.0449  -0.1872 0.0878  54  LYS B CD  
2001 C CE  . LYS B 52  ? 0.9817 1.2563 1.1698 0.0620  -0.1951 0.1010  54  LYS B CE  
2002 N NZ  . LYS B 52  ? 1.0075 1.2642 1.2034 0.0696  -0.1787 0.1026  54  LYS B NZ  
2003 N N   . THR B 53  ? 0.8719 1.1585 0.9975 -0.0180 -0.1877 0.0490  55  THR B N   
2004 C CA  . THR B 53  ? 0.8999 1.1674 1.0050 -0.0304 -0.1771 0.0406  55  THR B CA  
2005 C C   . THR B 53  ? 0.9187 1.1594 1.0143 -0.0260 -0.1617 0.0431  55  THR B C   
2006 O O   . THR B 53  ? 0.9194 1.1593 1.0297 -0.0160 -0.1567 0.0487  55  THR B O   
2007 C CB  . THR B 53  ? 0.9167 1.1982 1.0380 -0.0437 -0.1741 0.0283  55  THR B CB  
2008 O OG1 . THR B 53  ? 0.9199 1.2238 1.0769 -0.0401 -0.1726 0.0271  55  THR B OG1 
2009 C CG2 . THR B 53  ? 0.9185 1.2137 1.0313 -0.0543 -0.1869 0.0222  55  THR B CG2 
2010 N N   . TRP B 54  ? 0.9287 1.1473 1.0009 -0.0334 -0.1545 0.0384  56  TRP B N   
2011 C CA  . TRP B 54  ? 0.9387 1.1321 1.0007 -0.0295 -0.1421 0.0405  56  TRP B CA  
2012 C C   . TRP B 54  ? 0.9147 1.1075 0.9966 -0.0277 -0.1316 0.0391  56  TRP B C   
2013 O O   . TRP B 54  ? 0.9199 1.1014 1.0031 -0.0193 -0.1249 0.0445  56  TRP B O   
2014 C CB  . TRP B 54  ? 0.9617 1.1347 1.0010 -0.0382 -0.1370 0.0335  56  TRP B CB  
2015 C CG  . TRP B 54  ? 0.9855 1.1558 1.0290 -0.0493 -0.1321 0.0236  56  TRP B CG  
2016 C CD1 . TRP B 54  ? 1.0013 1.1798 1.0428 -0.0601 -0.1371 0.0158  56  TRP B CD1 
2017 C CD2 . TRP B 54  ? 0.9985 1.1535 1.0453 -0.0513 -0.1212 0.0208  56  TRP B CD2 
2018 N NE1 . TRP B 54  ? 1.0084 1.1772 1.0527 -0.0686 -0.1296 0.0086  56  TRP B NE1 
2019 C CE2 . TRP B 54  ? 1.0107 1.1648 1.0572 -0.0633 -0.1202 0.0119  56  TRP B CE2 
2020 C CE3 . TRP B 54  ? 1.0134 1.1543 1.0618 -0.0447 -0.1125 0.0247  56  TRP B CE3 
2021 C CZ2 . TRP B 54  ? 1.0280 1.1659 1.0737 -0.0687 -0.1113 0.0081  56  TRP B CZ2 
2022 C CZ3 . TRP B 54  ? 1.0323 1.1589 1.0802 -0.0502 -0.1041 0.0203  56  TRP B CZ3 
2023 C CH2 . TRP B 54  ? 1.0361 1.1607 1.0818 -0.0620 -0.1038 0.0126  56  TRP B CH2 
2024 N N   . GLN B 55  ? 0.8848 1.0890 0.9811 -0.0365 -0.1294 0.0313  57  GLN B N   
2025 C CA  . GLN B 55  ? 0.8609 1.0641 0.9737 -0.0376 -0.1180 0.0285  57  GLN B CA  
2026 C C   . GLN B 55  ? 0.8099 1.0298 0.9480 -0.0260 -0.1182 0.0341  57  GLN B C   
2027 O O   . GLN B 55  ? 0.8137 1.0260 0.9601 -0.0228 -0.1071 0.0343  57  GLN B O   
2028 C CB  . GLN B 55  ? 0.8852 1.0971 1.0061 -0.0515 -0.1156 0.0186  57  GLN B CB  
2029 C CG  . GLN B 55  ? 0.9434 1.1474 1.0728 -0.0563 -0.1015 0.0145  57  GLN B CG  
2030 C CD  . GLN B 55  ? 1.0067 1.2161 1.1409 -0.0716 -0.0980 0.0051  57  GLN B CD  
2031 O OE1 . GLN B 55  ? 1.0194 1.2509 1.1657 -0.0770 -0.1058 0.0009  57  GLN B OE1 
2032 N NE2 . GLN B 55  ? 1.0251 1.2131 1.1487 -0.0796 -0.0864 0.0015  57  GLN B NE2 
2033 N N   . ALA B 56  ? 0.7622 1.0036 0.9121 -0.0196 -0.1310 0.0385  58  ALA B N   
2034 C CA  . ALA B 56  ? 0.7196 0.9742 0.8929 -0.0062 -0.1331 0.0450  58  ALA B CA  
2035 C C   . ALA B 56  ? 0.6951 0.9277 0.8534 0.0052  -0.1301 0.0546  58  ALA B C   
2036 O O   . ALA B 56  ? 0.6926 0.9262 0.8680 0.0152  -0.1251 0.0583  58  ALA B O   
2037 C CB  . ALA B 56  ? 0.6989 0.9810 0.8875 -0.0020 -0.1503 0.0477  58  ALA B CB  
2038 N N   . ASN B 57  ? 0.6729 0.8858 0.8008 0.0033  -0.1320 0.0577  59  ASN B N   
2039 C CA  . ASN B 57  ? 0.6712 0.8621 0.7836 0.0119  -0.1279 0.0657  59  ASN B CA  
2040 C C   . ASN B 57  ? 0.6538 0.8227 0.7599 0.0098  -0.1128 0.0623  59  ASN B C   
2041 O O   . ASN B 57  ? 0.6634 0.8182 0.7659 0.0177  -0.1076 0.0680  59  ASN B O   
2042 C CB  . ASN B 57  ? 0.7003 0.8801 0.7837 0.0099  -0.1350 0.0695  59  ASN B CB  
2043 C CG  . ASN B 57  ? 0.7100 0.9052 0.7926 0.0142  -0.1508 0.0761  59  ASN B CG  
2044 O OD1 . ASN B 57  ? 0.7125 0.9216 0.8151 0.0241  -0.1574 0.0820  59  ASN B OD1 
2045 N ND2 . ASN B 57  ? 0.7172 0.9095 0.7765 0.0072  -0.1575 0.0749  59  ASN B ND2 
2046 N N   . LEU B 58  ? 0.6361 0.8004 0.7387 -0.0011 -0.1065 0.0535  60  LEU B N   
2047 C CA  . LEU B 58  ? 0.6273 0.7710 0.7230 -0.0037 -0.0942 0.0503  60  LEU B CA  
2048 C C   . LEU B 58  ? 0.6056 0.7555 0.7229 -0.0010 -0.0853 0.0486  60  LEU B C   
2049 O O   . LEU B 58  ? 0.5920 0.7568 0.7242 -0.0072 -0.0838 0.0428  60  LEU B O   
2050 C CB  . LEU B 58  ? 0.6389 0.7736 0.7213 -0.0161 -0.0926 0.0423  60  LEU B CB  
2051 C CG  . LEU B 58  ? 0.6795 0.7910 0.7511 -0.0199 -0.0826 0.0389  60  LEU B CG  
2052 C CD1 . LEU B 58  ? 0.6971 0.7903 0.7562 -0.0128 -0.0801 0.0436  60  LEU B CD1 
2053 C CD2 . LEU B 58  ? 0.6958 0.7977 0.7539 -0.0313 -0.0836 0.0319  60  LEU B CD2 
2054 N N   . ARG B 59  ? 0.5992 0.7374 0.7183 0.0077  -0.0785 0.0531  61  ARG B N   
2055 C CA  . ARG B 59  ? 0.5764 0.7166 0.7139 0.0107  -0.0677 0.0508  61  ARG B CA  
2056 C C   . ARG B 59  ? 0.5684 0.6831 0.6897 0.0062  -0.0562 0.0475  61  ARG B C   
2057 O O   . ARG B 59  ? 0.5817 0.6781 0.6847 0.0082  -0.0570 0.0507  61  ARG B O   
2058 C CB  . ARG B 59  ? 0.5912 0.7367 0.7437 0.0251  -0.0695 0.0583  61  ARG B CB  
2059 C CG  . ARG B 59  ? 0.6378 0.7958 0.8187 0.0294  -0.0610 0.0548  61  ARG B CG  
2060 C CD  . ARG B 59  ? 0.6861 0.8496 0.8846 0.0450  -0.0644 0.0624  61  ARG B CD  
2061 N NE  . ARG B 59  ? 0.7412 0.8946 0.9502 0.0492  -0.0498 0.0594  61  ARG B NE  
2062 C CZ  . ARG B 59  ? 0.7979 0.9336 1.0027 0.0585  -0.0455 0.0648  61  ARG B CZ  
2063 N NH1 . ARG B 59  ? 0.8160 0.9410 1.0056 0.0650  -0.0546 0.0746  61  ARG B NH1 
2064 N NH2 . ARG B 59  ? 0.8050 0.9325 1.0198 0.0604  -0.0312 0.0599  61  ARG B NH2 
2065 N N   . LEU B 60  ? 0.5392 0.6525 0.6666 -0.0004 -0.0457 0.0408  62  LEU B N   
2066 C CA  . LEU B 60  ? 0.5388 0.6277 0.6498 -0.0053 -0.0354 0.0376  62  LEU B CA  
2067 C C   . LEU B 60  ? 0.5096 0.5961 0.6337 0.0036  -0.0260 0.0389  62  LEU B C   
2068 O O   . LEU B 60  ? 0.5009 0.6049 0.6496 0.0072  -0.0214 0.0369  62  LEU B O   
2069 C CB  . LEU B 60  ? 0.5565 0.6422 0.6620 -0.0189 -0.0291 0.0298  62  LEU B CB  
2070 C CG  . LEU B 60  ? 0.6123 0.6722 0.6977 -0.0267 -0.0192 0.0259  62  LEU B CG  
2071 C CD1 . LEU B 60  ? 0.6273 0.6891 0.7255 -0.0264 -0.0053 0.0221  62  LEU B CD1 
2072 C CD2 . LEU B 60  ? 0.6340 0.6706 0.6978 -0.0238 -0.0229 0.0291  62  LEU B CD2 
2073 N N   . ILE B 61  ? 0.4849 0.5500 0.5940 0.0071  -0.0232 0.0415  63  ILE B N   
2074 C CA  . ILE B 61  ? 0.4644 0.5236 0.5828 0.0159  -0.0152 0.0432  63  ILE B CA  
2075 C C   . ILE B 61  ? 0.4600 0.5047 0.5718 0.0087  -0.0015 0.0359  63  ILE B C   
2076 O O   . ILE B 61  ? 0.4554 0.5059 0.5847 0.0119  0.0088  0.0326  63  ILE B O   
2077 C CB  . ILE B 61  ? 0.4706 0.5146 0.5764 0.0230  -0.0194 0.0500  63  ILE B CB  
2078 C CG1 . ILE B 61  ? 0.4840 0.5399 0.5921 0.0294  -0.0323 0.0577  63  ILE B CG1 
2079 C CG2 . ILE B 61  ? 0.4690 0.5026 0.5820 0.0306  -0.0098 0.0508  63  ILE B CG2 
2080 C CD1 . ILE B 61  ? 0.5061 0.5896 0.6392 0.0356  -0.0389 0.0604  63  ILE B CD1 
2081 N N   . SER B 62  ? 0.4617 0.4867 0.5482 -0.0009 -0.0012 0.0330  64  SER B N   
2082 C CA  . SER B 62  ? 0.4705 0.4768 0.5441 -0.0080 0.0104  0.0271  64  SER B CA  
2083 C C   . SER B 62  ? 0.4622 0.4483 0.5072 -0.0184 0.0059  0.0252  64  SER B C   
2084 O O   . SER B 62  ? 0.4710 0.4546 0.5072 -0.0175 -0.0053 0.0286  64  SER B O   
2085 C CB  . SER B 62  ? 0.5086 0.5026 0.5831 0.0000  0.0163  0.0286  64  SER B CB  
2086 O OG  . SER B 62  ? 0.5705 0.5531 0.6417 -0.0046 0.0303  0.0219  64  SER B OG  
2087 N N   . LYS B 63  ? 0.4423 0.4131 0.4722 -0.0283 0.0147  0.0195  65  LYS B N   
2088 C CA  . LYS B 63  ? 0.4434 0.3907 0.4441 -0.0373 0.0098  0.0183  65  LYS B CA  
2089 C C   . LYS B 63  ? 0.4580 0.3828 0.4419 -0.0402 0.0173  0.0151  65  LYS B C   
2090 O O   . LYS B 63  ? 0.4630 0.3897 0.4559 -0.0389 0.0298  0.0118  65  LYS B O   
2091 C CB  . LYS B 63  ? 0.4501 0.3954 0.4406 -0.0495 0.0107  0.0151  65  LYS B CB  
2092 C CG  . LYS B 63  ? 0.4422 0.4088 0.4477 -0.0486 0.0032  0.0170  65  LYS B CG  
2093 C CD  . LYS B 63  ? 0.4224 0.3802 0.4117 -0.0614 0.0012  0.0145  65  LYS B CD  
2094 C CE  . LYS B 63  ? 0.4394 0.4189 0.4446 -0.0616 -0.0049 0.0150  65  LYS B CE  
2095 N NZ  . LYS B 63  ? 0.5087 0.4804 0.5011 -0.0754 -0.0029 0.0115  65  LYS B NZ  
2096 N N   . PHE B 64  ? 0.4668 0.3705 0.4269 -0.0443 0.0094  0.0153  66  PHE B N   
2097 C CA  . PHE B 64  ? 0.4744 0.3559 0.4160 -0.0479 0.0141  0.0120  66  PHE B CA  
2098 C C   . PHE B 64  ? 0.5033 0.3628 0.4170 -0.0552 0.0029  0.0119  66  PHE B C   
2099 O O   . PHE B 64  ? 0.5012 0.3630 0.4139 -0.0543 -0.0093 0.0147  66  PHE B O   
2100 C CB  . PHE B 64  ? 0.4535 0.3365 0.4069 -0.0378 0.0156  0.0132  66  PHE B CB  
2101 C CG  . PHE B 64  ? 0.4283 0.3157 0.3867 -0.0310 0.0025  0.0178  66  PHE B CG  
2102 C CD1 . PHE B 64  ? 0.4426 0.3138 0.3845 -0.0336 -0.0068 0.0168  66  PHE B CD1 
2103 C CD2 . PHE B 64  ? 0.4145 0.3223 0.3936 -0.0226 -0.0006 0.0225  66  PHE B CD2 
2104 C CE1 . PHE B 64  ? 0.4363 0.3129 0.3849 -0.0281 -0.0170 0.0195  66  PHE B CE1 
2105 C CE2 . PHE B 64  ? 0.4240 0.3349 0.4053 -0.0180 -0.0109 0.0258  66  PHE B CE2 
2106 C CZ  . PHE B 64  ? 0.4229 0.3187 0.3903 -0.0208 -0.0180 0.0238  66  PHE B CZ  
2107 N N   . ASP B 65  ? 0.5398 0.3768 0.4303 -0.0624 0.0067  0.0083  67  ASP B N   
2108 C CA  . ASP B 65  ? 0.5659 0.3795 0.4282 -0.0690 -0.0054 0.0084  67  ASP B CA  
2109 C C   . ASP B 65  ? 0.5791 0.3722 0.4227 -0.0721 -0.0046 0.0049  67  ASP B C   
2110 O O   . ASP B 65  ? 0.6069 0.3771 0.4218 -0.0802 -0.0121 0.0042  67  ASP B O   
2111 C CB  . ASP B 65  ? 0.6188 0.4213 0.4611 -0.0803 -0.0053 0.0085  67  ASP B CB  
2112 C CG  . ASP B 65  ? 0.7479 0.5432 0.5784 -0.0905 0.0119  0.0041  67  ASP B CG  
2113 O OD1 . ASP B 65  ? 0.7715 0.5741 0.6142 -0.0877 0.0250  0.0005  67  ASP B OD1 
2114 O OD2 . ASP B 65  ? 0.8266 0.6081 0.6357 -0.1017 0.0128  0.0040  67  ASP B OD2 
2115 N N   . THR B 66  ? 0.5732 0.3731 0.4318 -0.0657 0.0036  0.0029  68  THR B N   
2116 C CA  . THR B 66  ? 0.5773 0.3605 0.4228 -0.0673 0.0031  -0.0008 68  THR B CA  
2117 C C   . THR B 66  ? 0.5553 0.3513 0.4248 -0.0562 0.0006  0.0006  68  THR B C   
2118 O O   . THR B 66  ? 0.5193 0.3357 0.4141 -0.0477 0.0040  0.0041  68  THR B O   
2119 C CB  . THR B 66  ? 0.6026 0.3745 0.4363 -0.0741 0.0203  -0.0067 68  THR B CB  
2120 O OG1 . THR B 66  ? 0.6174 0.4067 0.4794 -0.0657 0.0339  -0.0076 68  THR B OG1 
2121 C CG2 . THR B 66  ? 0.6118 0.3730 0.4237 -0.0860 0.0270  -0.0084 68  THR B CG2 
2122 N N   . VAL B 67  ? 0.5670 0.3497 0.4268 -0.0574 -0.0055 -0.0025 69  VAL B N   
2123 C CA  . VAL B 67  ? 0.5638 0.3539 0.4421 -0.0497 -0.0063 -0.0025 69  VAL B CA  
2124 C C   . VAL B 67  ? 0.5721 0.3691 0.4666 -0.0446 0.0107  -0.0031 69  VAL B C   
2125 O O   . VAL B 67  ? 0.5634 0.3743 0.4799 -0.0357 0.0122  0.0007  69  VAL B O   
2126 C CB  . VAL B 67  ? 0.5717 0.3447 0.4348 -0.0544 -0.0147 -0.0075 69  VAL B CB  
2127 C CG1 . VAL B 67  ? 0.5753 0.3544 0.4571 -0.0483 -0.0122 -0.0087 69  VAL B CG1 
2128 C CG2 . VAL B 67  ? 0.5678 0.3347 0.4189 -0.0573 -0.0337 -0.0067 69  VAL B CG2 
2129 N N   . GLU B 68  ? 0.5864 0.3723 0.4692 -0.0504 0.0236  -0.0079 70  GLU B N   
2130 C CA  . GLU B 68  ? 0.5852 0.3751 0.4835 -0.0455 0.0404  -0.0100 70  GLU B CA  
2131 C C   . GLU B 68  ? 0.5680 0.3805 0.4919 -0.0371 0.0458  -0.0049 70  GLU B C   
2132 O O   . GLU B 68  ? 0.5625 0.3841 0.5082 -0.0275 0.0522  -0.0027 70  GLU B O   
2133 C CB  . GLU B 68  ? 0.6473 0.4196 0.5255 -0.0551 0.0538  -0.0181 70  GLU B CB  
2134 C CG  . GLU B 68  ? 0.7264 0.4761 0.5813 -0.0626 0.0506  -0.0241 70  GLU B CG  
2135 C CD  . GLU B 68  ? 0.8376 0.5745 0.6655 -0.0712 0.0336  -0.0238 70  GLU B CD  
2136 O OE1 . GLU B 68  ? 0.8337 0.5750 0.6560 -0.0732 0.0266  -0.0195 70  GLU B OE1 
2137 O OE2 . GLU B 68  ? 0.8608 0.5828 0.6739 -0.0757 0.0267  -0.0279 70  GLU B OE2 
2138 N N   . ASP B 69  ? 0.5554 0.3759 0.4764 -0.0407 0.0427  -0.0031 71  ASP B N   
2139 C CA  . ASP B 69  ? 0.5325 0.3764 0.4784 -0.0335 0.0456  0.0012  71  ASP B CA  
2140 C C   . ASP B 69  ? 0.4949 0.3537 0.4566 -0.0243 0.0334  0.0088  71  ASP B C   
2141 O O   . ASP B 69  ? 0.4709 0.3471 0.4556 -0.0153 0.0358  0.0130  71  ASP B O   
2142 C CB  . ASP B 69  ? 0.5582 0.4055 0.4958 -0.0419 0.0469  -0.0001 71  ASP B CB  
2143 C CG  . ASP B 69  ? 0.6178 0.4510 0.5404 -0.0515 0.0620  -0.0080 71  ASP B CG  
2144 O OD1 . ASP B 69  ? 0.6224 0.4555 0.5567 -0.0475 0.0754  -0.0122 71  ASP B OD1 
2145 O OD2 . ASP B 69  ? 0.6510 0.4715 0.5489 -0.0632 0.0608  -0.0101 71  ASP B OD2 
2146 N N   . PHE B 70  ? 0.4850 0.3368 0.4346 -0.0266 0.0203  0.0101  72  PHE B N   
2147 C CA  . PHE B 70  ? 0.4557 0.3182 0.4184 -0.0188 0.0114  0.0155  72  PHE B CA  
2148 C C   . PHE B 70  ? 0.4500 0.3124 0.4261 -0.0110 0.0185  0.0171  72  PHE B C   
2149 O O   . PHE B 70  ? 0.4491 0.3251 0.4421 -0.0027 0.0185  0.0229  72  PHE B O   
2150 C CB  . PHE B 70  ? 0.4377 0.2916 0.3874 -0.0229 -0.0019 0.0143  72  PHE B CB  
2151 C CG  . PHE B 70  ? 0.4131 0.2751 0.3756 -0.0162 -0.0071 0.0177  72  PHE B CG  
2152 C CD1 . PHE B 70  ? 0.3994 0.2776 0.3728 -0.0118 -0.0125 0.0225  72  PHE B CD1 
2153 C CD2 . PHE B 70  ? 0.4193 0.2721 0.3820 -0.0155 -0.0056 0.0154  72  PHE B CD2 
2154 C CE1 . PHE B 70  ? 0.3990 0.2831 0.3814 -0.0070 -0.0156 0.0252  72  PHE B CE1 
2155 C CE2 . PHE B 70  ? 0.4190 0.2785 0.3926 -0.0109 -0.0085 0.0180  72  PHE B CE2 
2156 C CZ  . PHE B 70  ? 0.4012 0.2758 0.3838 -0.0067 -0.0130 0.0231  72  PHE B CZ  
2157 N N   . TRP B 71  ? 0.4635 0.3089 0.4305 -0.0141 0.0241  0.0121  73  TRP B N   
2158 C CA  . TRP B 71  ? 0.4753 0.3168 0.4530 -0.0078 0.0312  0.0132  73  TRP B CA  
2159 C C   . TRP B 71  ? 0.4772 0.3260 0.4719 -0.0002 0.0429  0.0153  73  TRP B C   
2160 O O   . TRP B 71  ? 0.4696 0.3223 0.4783 0.0085  0.0445  0.0206  73  TRP B O   
2161 C CB  . TRP B 71  ? 0.4889 0.3099 0.4528 -0.0139 0.0346  0.0063  73  TRP B CB  
2162 C CG  . TRP B 71  ? 0.4810 0.2975 0.4370 -0.0181 0.0227  0.0048  73  TRP B CG  
2163 C CD1 . TRP B 71  ? 0.4960 0.3008 0.4339 -0.0269 0.0152  -0.0011 73  TRP B CD1 
2164 C CD2 . TRP B 71  ? 0.4602 0.2837 0.4272 -0.0137 0.0171  0.0087  73  TRP B CD2 
2165 N NE1 . TRP B 71  ? 0.4918 0.2977 0.4325 -0.0274 0.0052  -0.0019 73  TRP B NE1 
2166 C CE2 . TRP B 71  ? 0.4688 0.2864 0.4271 -0.0201 0.0072  0.0037  73  TRP B CE2 
2167 C CE3 . TRP B 71  ? 0.4450 0.2783 0.4272 -0.0055 0.0197  0.0158  73  TRP B CE3 
2168 C CZ2 . TRP B 71  ? 0.4695 0.2926 0.4366 -0.0188 0.0014  0.0042  73  TRP B CZ2 
2169 C CZ3 . TRP B 71  ? 0.4604 0.2968 0.4469 -0.0053 0.0142  0.0171  73  TRP B CZ3 
2170 C CH2 . TRP B 71  ? 0.4591 0.2914 0.4395 -0.0120 0.0061  0.0108  73  TRP B CH2 
2171 N N   . ALA B 72  ? 0.4878 0.3381 0.4822 -0.0033 0.0511  0.0110  74  ALA B N   
2172 C CA  . ALA B 72  ? 0.4934 0.3544 0.5101 0.0054  0.0617  0.0122  74  ALA B CA  
2173 C C   . ALA B 72  ? 0.4663 0.3492 0.5018 0.0145  0.0533  0.0212  74  ALA B C   
2174 O O   . ALA B 72  ? 0.4559 0.3449 0.5100 0.0254  0.0557  0.0262  74  ALA B O   
2175 C CB  . ALA B 72  ? 0.5176 0.3792 0.5322 -0.0009 0.0724  0.0049  74  ALA B CB  
2176 N N   . LEU B 73  ? 0.4417 0.3349 0.4712 0.0101  0.0427  0.0232  75  LEU B N   
2177 C CA  . LEU B 73  ? 0.4237 0.3367 0.4669 0.0166  0.0335  0.0308  75  LEU B CA  
2178 C C   . LEU B 73  ? 0.4164 0.3273 0.4604 0.0230  0.0265  0.0379  75  LEU B C   
2179 O O   . LEU B 73  ? 0.3920 0.3134 0.4504 0.0322  0.0243  0.0449  75  LEU B O   
2180 C CB  . LEU B 73  ? 0.4245 0.3451 0.4577 0.0085  0.0245  0.0299  75  LEU B CB  
2181 C CG  . LEU B 73  ? 0.4303 0.3713 0.4750 0.0131  0.0148  0.0361  75  LEU B CG  
2182 C CD1 . LEU B 73  ? 0.4323 0.3916 0.5010 0.0206  0.0192  0.0380  75  LEU B CD1 
2183 C CD2 . LEU B 73  ? 0.4376 0.3821 0.4710 0.0044  0.0071  0.0340  75  LEU B CD2 
2184 N N   . TYR B 74  ? 0.4252 0.3222 0.4533 0.0175  0.0229  0.0359  76  TYR B N   
2185 C CA  . TYR B 74  ? 0.4262 0.3189 0.4537 0.0213  0.0190  0.0409  76  TYR B CA  
2186 C C   . TYR B 74  ? 0.4396 0.3236 0.4763 0.0293  0.0278  0.0443  76  TYR B C   
2187 O O   . TYR B 74  ? 0.4162 0.3038 0.4590 0.0364  0.0250  0.0522  76  TYR B O   
2188 C CB  . TYR B 74  ? 0.4311 0.3111 0.4436 0.0131  0.0152  0.0355  76  TYR B CB  
2189 C CG  . TYR B 74  ? 0.4386 0.3163 0.4515 0.0152  0.0123  0.0393  76  TYR B CG  
2190 C CD1 . TYR B 74  ? 0.4413 0.3299 0.4537 0.0148  0.0034  0.0423  76  TYR B CD1 
2191 C CD2 . TYR B 74  ? 0.4477 0.3115 0.4613 0.0168  0.0197  0.0395  76  TYR B CD2 
2192 C CE1 . TYR B 74  ? 0.4554 0.3415 0.4672 0.0153  0.0027  0.0449  76  TYR B CE1 
2193 C CE2 . TYR B 74  ? 0.4592 0.3200 0.4724 0.0175  0.0188  0.0430  76  TYR B CE2 
2194 C CZ  . TYR B 74  ? 0.4774 0.3496 0.4895 0.0164  0.0107  0.0454  76  TYR B CZ  
2195 O OH  . TYR B 74  ? 0.5111 0.3794 0.5217 0.0157  0.0119  0.0479  76  TYR B OH  
2196 N N   . ASN B 75  ? 0.4805 0.3510 0.5162 0.0277  0.0384  0.0382  77  ASN B N   
2197 C CA  . ASN B 75  ? 0.5177 0.3766 0.5620 0.0351  0.0479  0.0401  77  ASN B CA  
2198 C C   . ASN B 75  ? 0.5287 0.4012 0.5930 0.0466  0.0485  0.0467  77  ASN B C   
2199 O O   . ASN B 75  ? 0.5554 0.4243 0.6267 0.0555  0.0479  0.0546  77  ASN B O   
2200 C CB  . ASN B 75  ? 0.5507 0.3931 0.5896 0.0302  0.0597  0.0305  77  ASN B CB  
2201 C CG  . ASN B 75  ? 0.6309 0.4571 0.6515 0.0201  0.0586  0.0244  77  ASN B CG  
2202 O OD1 . ASN B 75  ? 0.6713 0.4955 0.6878 0.0188  0.0521  0.0275  77  ASN B OD1 
2203 N ND2 . ASN B 75  ? 0.6388 0.4533 0.6481 0.0122  0.0649  0.0148  77  ASN B ND2 
2204 N N   . HIS B 76  ? 0.5166 0.4046 0.5903 0.0464  0.0492  0.0437  78  HIS B N   
2205 C CA  . HIS B 76  ? 0.5079 0.4138 0.6038 0.0572  0.0472  0.0493  78  HIS B CA  
2206 C C   . HIS B 76  ? 0.4976 0.4139 0.5947 0.0630  0.0340  0.0605  78  HIS B C   
2207 O O   . HIS B 76  ? 0.4871 0.4003 0.5932 0.0734  0.0329  0.0683  78  HIS B O   
2208 C CB  . HIS B 76  ? 0.5237 0.4467 0.6289 0.0533  0.0495  0.0431  78  HIS B CB  
2209 C CG  . HIS B 76  ? 0.5763 0.5203 0.7086 0.0642  0.0473  0.0474  78  HIS B CG  
2210 N ND1 . HIS B 76  ? 0.6025 0.5684 0.7410 0.0644  0.0359  0.0515  78  HIS B ND1 
2211 C CD2 . HIS B 76  ? 0.5966 0.5424 0.7520 0.0756  0.0542  0.0478  78  HIS B CD2 
2212 C CE1 . HIS B 76  ? 0.5968 0.5786 0.7624 0.0756  0.0353  0.0543  78  HIS B CE1 
2213 N NE2 . HIS B 76  ? 0.6024 0.5729 0.7799 0.0832  0.0460  0.0523  78  HIS B NE2 
2214 N N   . ILE B 77  ? 0.5033 0.4293 0.5892 0.0560  0.0240  0.0612  79  ILE B N   
2215 C CA  . ILE B 77  ? 0.5124 0.4477 0.5962 0.0596  0.0123  0.0703  79  ILE B CA  
2216 C C   . ILE B 77  ? 0.5470 0.4649 0.6219 0.0634  0.0128  0.0772  79  ILE B C   
2217 O O   . ILE B 77  ? 0.5328 0.4540 0.6101 0.0709  0.0065  0.0869  79  ILE B O   
2218 C CB  . ILE B 77  ? 0.5116 0.4552 0.5823 0.0497  0.0041  0.0674  79  ILE B CB  
2219 C CG1 . ILE B 77  ? 0.5161 0.4762 0.5944 0.0452  0.0032  0.0616  79  ILE B CG1 
2220 C CG2 . ILE B 77  ? 0.5115 0.4612 0.5761 0.0518  -0.0062 0.0754  79  ILE B CG2 
2221 C CD1 . ILE B 77  ? 0.5268 0.5101 0.6170 0.0488  -0.0061 0.0661  79  ILE B CD1 
2222 N N   . GLN B 78  ? 0.5791 0.4778 0.6426 0.0574  0.0202  0.0721  80  GLN B N   
2223 C CA  . GLN B 78  ? 0.5992 0.4803 0.6539 0.0587  0.0224  0.0772  80  GLN B CA  
2224 C C   . GLN B 78  ? 0.6453 0.5169 0.7107 0.0702  0.0272  0.0841  80  GLN B C   
2225 O O   . GLN B 78  ? 0.6428 0.5058 0.7025 0.0745  0.0246  0.0933  80  GLN B O   
2226 C CB  . GLN B 78  ? 0.5915 0.4558 0.6348 0.0493  0.0292  0.0688  80  GLN B CB  
2227 C CG  . GLN B 78  ? 0.5781 0.4250 0.6125 0.0483  0.0324  0.0729  80  GLN B CG  
2228 C CD  . GLN B 78  ? 0.5541 0.3897 0.5794 0.0376  0.0366  0.0632  80  GLN B CD  
2229 O OE1 . GLN B 78  ? 0.5652 0.3933 0.5913 0.0345  0.0425  0.0553  80  GLN B OE1 
2230 N NE2 . GLN B 78  ? 0.5280 0.3628 0.5451 0.0312  0.0335  0.0628  80  GLN B NE2 
2231 N N   . LEU B 79  ? 0.6875 0.5591 0.7676 0.0750  0.0347  0.0795  81  LEU B N   
2232 C CA  . LEU B 79  ? 0.7294 0.5920 0.8238 0.0875  0.0395  0.0850  81  LEU B CA  
2233 C C   . LEU B 79  ? 0.7579 0.6387 0.8679 0.0991  0.0292  0.0942  81  LEU B C   
2234 O O   . LEU B 79  ? 0.7638 0.6355 0.8777 0.1096  0.0264  0.1043  81  LEU B O   
2235 C CB  . LEU B 79  ? 0.7351 0.5919 0.8410 0.0878  0.0526  0.0745  81  LEU B CB  
2236 C CG  . LEU B 79  ? 0.7740 0.6103 0.8643 0.0768  0.0627  0.0649  81  LEU B CG  
2237 C CD1 . LEU B 79  ? 0.7741 0.6065 0.8733 0.0758  0.0754  0.0537  81  LEU B CD1 
2238 C CD2 . LEU B 79  ? 0.8019 0.6139 0.8825 0.0780  0.0661  0.0701  81  LEU B CD2 
2239 N N   . SER B 80  ? 0.7705 0.6760 0.8887 0.0968  0.0230  0.0911  82  SER B N   
2240 C CA  . SER B 80  ? 0.7808 0.7072 0.9198 0.1074  0.0143  0.0967  82  SER B CA  
2241 C C   . SER B 80  ? 0.7968 0.7351 0.9269 0.1081  -0.0013 0.1064  82  SER B C   
2242 O O   . SER B 80  ? 0.7959 0.7424 0.9383 0.1194  -0.0104 0.1153  82  SER B O   
2243 C CB  . SER B 80  ? 0.7986 0.7459 0.9552 0.1041  0.0182  0.0863  82  SER B CB  
2244 O OG  . SER B 80  ? 0.8585 0.8140 1.0001 0.0909  0.0153  0.0807  82  SER B OG  
2245 N N   . SER B 81  ? 0.8162 0.7554 0.9255 0.0966  -0.0051 0.1046  83  SER B N   
2246 C CA  . SER B 81  ? 0.8339 0.7895 0.9371 0.0953  -0.0189 0.1104  83  SER B CA  
2247 C C   . SER B 81  ? 0.8515 0.7936 0.9352 0.0972  -0.0252 0.1216  83  SER B C   
2248 O O   . SER B 81  ? 0.8636 0.7833 0.9330 0.0941  -0.0178 0.1225  83  SER B O   
2249 C CB  . SER B 81  ? 0.8612 0.8271 0.9546 0.0822  -0.0200 0.1016  83  SER B CB  
2250 O OG  . SER B 81  ? 0.8967 0.8758 1.0060 0.0799  -0.0154 0.0925  83  SER B OG  
2251 N N   . ASN B 82  ? 0.8506 0.8057 0.9327 0.1013  -0.0387 0.1298  84  ASN B N   
2252 C CA  . ASN B 82  ? 0.8737 0.8166 0.9326 0.1011  -0.0455 0.1406  84  ASN B CA  
2253 C C   . ASN B 82  ? 0.8697 0.8199 0.9096 0.0887  -0.0493 0.1367  84  ASN B C   
2254 O O   . ASN B 82  ? 0.8709 0.8413 0.9187 0.0838  -0.0529 0.1292  84  ASN B O   
2255 C CB  . ASN B 82  ? 0.8989 0.8496 0.9640 0.1131  -0.0597 0.1527  84  ASN B CB  
2256 C CG  . ASN B 82  ? 0.9602 0.8990 1.0414 0.1276  -0.0581 0.1597  84  ASN B CG  
2257 O OD1 . ASN B 82  ? 0.9947 0.9164 1.0636 0.1347  -0.0640 0.1725  84  ASN B OD1 
2258 N ND2 . ASN B 82  ? 0.9545 0.9002 1.0623 0.1322  -0.0499 0.1515  84  ASN B ND2 
2259 N N   . LEU B 83  ? 0.8648 0.7980 0.8799 0.0834  -0.0478 0.1414  85  LEU B N   
2260 C CA  . LEU B 83  ? 0.8620 0.7990 0.8588 0.0717  -0.0491 0.1369  85  LEU B CA  
2261 C C   . LEU B 83  ? 0.8522 0.7958 0.8339 0.0724  -0.0617 0.1458  85  LEU B C   
2262 O O   . LEU B 83  ? 0.8640 0.7902 0.8242 0.0718  -0.0616 0.1544  85  LEU B O   
2263 C CB  . LEU B 83  ? 0.8740 0.7887 0.8545 0.0641  -0.0374 0.1348  85  LEU B CB  
2264 C CG  . LEU B 83  ? 0.8810 0.7980 0.8454 0.0519  -0.0359 0.1281  85  LEU B CG  
2265 C CD1 . LEU B 83  ? 0.8780 0.8091 0.8548 0.0457  -0.0344 0.1145  85  LEU B CD1 
2266 C CD2 . LEU B 83  ? 0.8901 0.7852 0.8389 0.0457  -0.0252 0.1286  85  LEU B CD2 
2267 N N   . MET B 84  ? 0.8386 0.8057 0.8292 0.0726  -0.0723 0.1434  86  MET B N   
2268 C CA  . MET B 84  ? 0.8479 0.8224 0.8242 0.0733  -0.0860 0.1514  86  MET B CA  
2269 C C   . MET B 84  ? 0.8435 0.8222 0.8014 0.0601  -0.0851 0.1438  86  MET B C   
2270 O O   . MET B 84  ? 0.8418 0.8332 0.8106 0.0541  -0.0822 0.1322  86  MET B O   
2271 C CB  . MET B 84  ? 0.8492 0.8486 0.8472 0.0810  -0.0993 0.1529  86  MET B CB  
2272 C CG  . MET B 84  ? 0.8842 0.8881 0.9124 0.0924  -0.0968 0.1532  86  MET B CG  
2273 S SD  . MET B 84  ? 0.9608 0.9966 1.0169 0.1012  -0.1132 0.1547  86  MET B SD  
2274 C CE  . MET B 84  ? 0.9093 0.9592 0.9975 0.1000  -0.1012 0.1408  86  MET B CE  
2275 N N   . PRO B 85  ? 0.8374 0.8044 0.7671 0.0551  -0.0869 0.1495  87  PRO B N   
2276 C CA  . PRO B 85  ? 0.8252 0.8002 0.7399 0.0434  -0.0878 0.1415  87  PRO B CA  
2277 C C   . PRO B 85  ? 0.7957 0.7958 0.7198 0.0434  -0.1010 0.1385  87  PRO B C   
2278 O O   . PRO B 85  ? 0.7775 0.7893 0.7160 0.0524  -0.1117 0.1448  87  PRO B O   
2279 C CB  . PRO B 85  ? 0.8607 0.8172 0.7421 0.0386  -0.0869 0.1495  87  PRO B CB  
2280 C CG  . PRO B 85  ? 0.8802 0.8144 0.7584 0.0465  -0.0824 0.1609  87  PRO B CG  
2281 C CD  . PRO B 85  ? 0.8484 0.7926 0.7569 0.0590  -0.0872 0.1630  87  PRO B CD  
2282 N N   . GLY B 86  ? 0.7849 0.7931 0.7025 0.0330  -0.0997 0.1281  88  GLY B N   
2283 C CA  . GLY B 86  ? 0.7636 0.7944 0.6906 0.0302  -0.1096 0.1221  88  GLY B CA  
2284 C C   . GLY B 86  ? 0.7306 0.7736 0.6851 0.0307  -0.1059 0.1127  88  GLY B C   
2285 O O   . GLY B 86  ? 0.7235 0.7823 0.6846 0.0254  -0.1107 0.1051  88  GLY B O   
2286 N N   . CYS B 87  ? 0.7041 0.7383 0.6729 0.0360  -0.0969 0.1129  89  CYS B N   
2287 C CA  . CYS B 87  ? 0.6881 0.7308 0.6800 0.0365  -0.0927 0.1052  89  CYS B CA  
2288 C C   . CYS B 87  ? 0.6579 0.6913 0.6466 0.0282  -0.0827 0.0944  89  CYS B C   
2289 O O   . CYS B 87  ? 0.6744 0.6938 0.6485 0.0244  -0.0766 0.0931  89  CYS B O   
2290 C CB  . CYS B 87  ? 0.7252 0.7642 0.7342 0.0469  -0.0894 0.1109  89  CYS B CB  
2291 S SG  . CYS B 87  ? 0.8777 0.9300 0.8976 0.0587  -0.1031 0.1227  89  CYS B SG  
2292 N N   . ASP B 88  ? 0.6028 0.6441 0.6054 0.0253  -0.0813 0.0864  90  ASP B N   
2293 C CA  . ASP B 88  ? 0.5623 0.5951 0.5630 0.0186  -0.0746 0.0768  90  ASP B CA  
2294 C C   . ASP B 88  ? 0.5057 0.5376 0.5216 0.0204  -0.0696 0.0738  90  ASP B C   
2295 O O   . ASP B 88  ? 0.4728 0.5175 0.5025 0.0231  -0.0722 0.0749  90  ASP B O   
2296 C CB  . ASP B 88  ? 0.5898 0.6307 0.5858 0.0103  -0.0793 0.0688  90  ASP B CB  
2297 C CG  . ASP B 88  ? 0.6445 0.6901 0.6255 0.0072  -0.0853 0.0704  90  ASP B CG  
2298 O OD1 . ASP B 88  ? 0.6788 0.7150 0.6469 0.0085  -0.0828 0.0753  90  ASP B OD1 
2299 O OD2 . ASP B 88  ? 0.6343 0.6919 0.6150 0.0024  -0.0919 0.0663  90  ASP B OD2 
2300 N N   . TYR B 89  ? 0.4781 0.4951 0.4916 0.0185  -0.0620 0.0695  91  TYR B N   
2301 C CA  . TYR B 89  ? 0.4460 0.4585 0.4680 0.0175  -0.0569 0.0648  91  TYR B CA  
2302 C C   . TYR B 89  ? 0.3986 0.4039 0.4138 0.0097  -0.0571 0.0561  91  TYR B C   
2303 O O   . TYR B 89  ? 0.3870 0.3865 0.3938 0.0070  -0.0578 0.0534  91  TYR B O   
2304 C CB  . TYR B 89  ? 0.4707 0.4693 0.4947 0.0222  -0.0488 0.0673  91  TYR B CB  
2305 C CG  . TYR B 89  ? 0.4984 0.5011 0.5325 0.0311  -0.0476 0.0752  91  TYR B CG  
2306 C CD1 . TYR B 89  ? 0.5107 0.5111 0.5395 0.0365  -0.0501 0.0837  91  TYR B CD1 
2307 C CD2 . TYR B 89  ? 0.5225 0.5302 0.5711 0.0341  -0.0439 0.0740  91  TYR B CD2 
2308 C CE1 . TYR B 89  ? 0.5340 0.5364 0.5725 0.0460  -0.0506 0.0916  91  TYR B CE1 
2309 C CE2 . TYR B 89  ? 0.5288 0.5406 0.5902 0.0436  -0.0430 0.0805  91  TYR B CE2 
2310 C CZ  . TYR B 89  ? 0.5480 0.5570 0.6048 0.0502  -0.0473 0.0897  91  TYR B CZ  
2311 O OH  . TYR B 89  ? 0.5736 0.5850 0.6435 0.0610  -0.0481 0.0970  91  TYR B OH  
2312 N N   . SER B 90  ? 0.3723 0.3774 0.3913 0.0062  -0.0561 0.0517  92  SER B N   
2313 C CA  . SER B 90  ? 0.3646 0.3612 0.3764 -0.0008 -0.0581 0.0444  92  SER B CA  
2314 C C   . SER B 90  ? 0.3483 0.3351 0.3599 -0.0033 -0.0537 0.0416  92  SER B C   
2315 O O   . SER B 90  ? 0.3295 0.3230 0.3483 -0.0030 -0.0503 0.0428  92  SER B O   
2316 C CB  . SER B 90  ? 0.3833 0.3899 0.3941 -0.0059 -0.0644 0.0415  92  SER B CB  
2317 O OG  . SER B 90  ? 0.4443 0.4595 0.4523 -0.0053 -0.0689 0.0428  92  SER B OG  
2318 N N   . LEU B 91  ? 0.3370 0.3084 0.3406 -0.0062 -0.0540 0.0372  93  LEU B N   
2319 C CA  . LEU B 91  ? 0.3316 0.2904 0.3291 -0.0105 -0.0517 0.0339  93  LEU B CA  
2320 C C   . LEU B 91  ? 0.3361 0.2877 0.3246 -0.0165 -0.0589 0.0293  93  LEU B C   
2321 O O   . LEU B 91  ? 0.3319 0.2780 0.3179 -0.0161 -0.0641 0.0264  93  LEU B O   
2322 C CB  . LEU B 91  ? 0.3395 0.2839 0.3333 -0.0090 -0.0479 0.0327  93  LEU B CB  
2323 C CG  . LEU B 91  ? 0.3638 0.2940 0.3483 -0.0140 -0.0446 0.0298  93  LEU B CG  
2324 C CD1 . LEU B 91  ? 0.3714 0.3075 0.3626 -0.0127 -0.0350 0.0319  93  LEU B CD1 
2325 C CD2 . LEU B 91  ? 0.3665 0.2805 0.3439 -0.0145 -0.0448 0.0268  93  LEU B CD2 
2326 N N   . PHE B 92  ? 0.3359 0.2873 0.3206 -0.0222 -0.0589 0.0282  94  PHE B N   
2327 C CA  . PHE B 92  ? 0.3511 0.2931 0.3258 -0.0283 -0.0658 0.0245  94  PHE B CA  
2328 C C   . PHE B 92  ? 0.3611 0.2875 0.3232 -0.0350 -0.0635 0.0233  94  PHE B C   
2329 O O   . PHE B 92  ? 0.3578 0.2868 0.3216 -0.0364 -0.0550 0.0245  94  PHE B O   
2330 C CB  . PHE B 92  ? 0.3557 0.3120 0.3354 -0.0309 -0.0687 0.0242  94  PHE B CB  
2331 C CG  . PHE B 92  ? 0.3583 0.3223 0.3422 -0.0274 -0.0740 0.0231  94  PHE B CG  
2332 C CD1 . PHE B 92  ? 0.3533 0.3287 0.3450 -0.0211 -0.0717 0.0264  94  PHE B CD1 
2333 C CD2 . PHE B 92  ? 0.3749 0.3326 0.3537 -0.0306 -0.0806 0.0185  94  PHE B CD2 
2334 C CE1 . PHE B 92  ? 0.3636 0.3441 0.3561 -0.0192 -0.0749 0.0248  94  PHE B CE1 
2335 C CE2 . PHE B 92  ? 0.3736 0.3379 0.3561 -0.0279 -0.0837 0.0161  94  PHE B CE2 
2336 C CZ  . PHE B 92  ? 0.3635 0.3392 0.3520 -0.0228 -0.0804 0.0191  94  PHE B CZ  
2337 N N   . LYS B 93  ? 0.3881 0.2964 0.3364 -0.0392 -0.0708 0.0208  95  LYS B N   
2338 C CA  . LYS B 93  ? 0.3897 0.2793 0.3204 -0.0473 -0.0695 0.0203  95  LYS B CA  
2339 C C   . LYS B 93  ? 0.4068 0.3054 0.3391 -0.0541 -0.0624 0.0205  95  LYS B C   
2340 O O   . LYS B 93  ? 0.3919 0.3065 0.3351 -0.0542 -0.0636 0.0202  95  LYS B O   
2341 C CB  . LYS B 93  ? 0.3726 0.2406 0.2881 -0.0500 -0.0808 0.0185  95  LYS B CB  
2342 C CG  . LYS B 93  ? 0.3612 0.2201 0.2763 -0.0444 -0.0880 0.0171  95  LYS B CG  
2343 C CD  . LYS B 93  ? 0.3983 0.2399 0.3045 -0.0448 -0.1011 0.0150  95  LYS B CD  
2344 C CE  . LYS B 93  ? 0.4398 0.2721 0.3463 -0.0400 -0.1090 0.0129  95  LYS B CE  
2345 N NZ  . LYS B 93  ? 0.4077 0.2264 0.3116 -0.0381 -0.1231 0.0103  95  LYS B NZ  
2346 N N   . ASP B 94  ? 0.4320 0.3205 0.3535 -0.0606 -0.0545 0.0203  96  ASP B N   
2347 C CA  . ASP B 94  ? 0.4549 0.3510 0.3785 -0.0686 -0.0455 0.0193  96  ASP B CA  
2348 C C   . ASP B 94  ? 0.4810 0.3723 0.3976 -0.0757 -0.0516 0.0181  96  ASP B C   
2349 O O   . ASP B 94  ? 0.4906 0.3580 0.3875 -0.0794 -0.0593 0.0183  96  ASP B O   
2350 C CB  . ASP B 94  ? 0.4988 0.3775 0.4053 -0.0763 -0.0359 0.0181  96  ASP B CB  
2351 C CG  . ASP B 94  ? 0.5781 0.4683 0.4921 -0.0837 -0.0219 0.0155  96  ASP B CG  
2352 O OD1 . ASP B 94  ? 0.5587 0.4753 0.4968 -0.0806 -0.0195 0.0150  96  ASP B OD1 
2353 O OD2 . ASP B 94  ? 0.6362 0.5094 0.5322 -0.0929 -0.0133 0.0136  96  ASP B OD2 
2354 N N   . GLY B 95  ? 0.4834 0.3974 0.4172 -0.0766 -0.0493 0.0171  97  GLY B N   
2355 C CA  . GLY B 95  ? 0.4991 0.4121 0.4296 -0.0840 -0.0534 0.0151  97  GLY B CA  
2356 C C   . GLY B 95  ? 0.5034 0.4233 0.4408 -0.0781 -0.0642 0.0145  97  GLY B C   
2357 O O   . GLY B 95  ? 0.5192 0.4352 0.4523 -0.0843 -0.0682 0.0122  97  GLY B O   
2358 N N   . ILE B 96  ? 0.4897 0.4184 0.4366 -0.0673 -0.0680 0.0161  98  ILE B N   
2359 C CA  . ILE B 96  ? 0.4913 0.4301 0.4464 -0.0618 -0.0756 0.0149  98  ILE B CA  
2360 C C   . ILE B 96  ? 0.5022 0.4686 0.4761 -0.0556 -0.0724 0.0171  98  ILE B C   
2361 O O   . ILE B 96  ? 0.5033 0.4739 0.4830 -0.0488 -0.0686 0.0202  98  ILE B O   
2362 C CB  . ILE B 96  ? 0.4926 0.4176 0.4425 -0.0548 -0.0824 0.0146  98  ILE B CB  
2363 C CG1 . ILE B 96  ? 0.5202 0.4161 0.4514 -0.0592 -0.0875 0.0136  98  ILE B CG1 
2364 C CG2 . ILE B 96  ? 0.4803 0.4160 0.4385 -0.0505 -0.0880 0.0119  98  ILE B CG2 
2365 C CD1 . ILE B 96  ? 0.5424 0.4263 0.4724 -0.0518 -0.0959 0.0122  98  ILE B CD1 
2366 N N   . GLU B 97  ? 0.5123 0.4958 0.4946 -0.0581 -0.0746 0.0155  99  GLU B N   
2367 C CA  . GLU B 97  ? 0.5400 0.5477 0.5374 -0.0518 -0.0751 0.0180  99  GLU B CA  
2368 C C   . GLU B 97  ? 0.5513 0.5579 0.5466 -0.0442 -0.0799 0.0191  99  GLU B C   
2369 O O   . GLU B 97  ? 0.5564 0.5501 0.5429 -0.0455 -0.0842 0.0154  99  GLU B O   
2370 C CB  . GLU B 97  ? 0.5879 0.6147 0.5939 -0.0577 -0.0775 0.0155  99  GLU B CB  
2371 C CG  . GLU B 97  ? 0.6773 0.7124 0.6921 -0.0642 -0.0707 0.0144  99  GLU B CG  
2372 C CD  . GLU B 97  ? 0.7979 0.8574 0.8269 -0.0689 -0.0733 0.0118  99  GLU B CD  
2373 O OE1 . GLU B 97  ? 0.8245 0.9040 0.8718 -0.0670 -0.0696 0.0129  99  GLU B OE1 
2374 O OE2 . GLU B 97  ? 0.8305 0.8894 0.8535 -0.0744 -0.0793 0.0080  99  GLU B OE2 
2375 N N   . PRO B 98  ? 0.5470 0.5663 0.5509 -0.0365 -0.0784 0.0238  100 PRO B N   
2376 C CA  . PRO B 98  ? 0.5620 0.5793 0.5628 -0.0306 -0.0808 0.0249  100 PRO B CA  
2377 C C   . PRO B 98  ? 0.5584 0.5871 0.5578 -0.0323 -0.0863 0.0229  100 PRO B C   
2378 O O   . PRO B 98  ? 0.5592 0.5976 0.5598 -0.0277 -0.0873 0.0267  100 PRO B O   
2379 C CB  . PRO B 98  ? 0.5785 0.6025 0.5870 -0.0228 -0.0764 0.0314  100 PRO B CB  
2380 C CG  . PRO B 98  ? 0.5766 0.6174 0.5966 -0.0236 -0.0757 0.0335  100 PRO B CG  
2381 C CD  . PRO B 98  ? 0.5497 0.5844 0.5669 -0.0326 -0.0742 0.0282  100 PRO B CD  
2382 N N   . MET B 99  ? 0.5619 0.5873 0.5565 -0.0394 -0.0898 0.0170  101 MET B N   
2383 C CA  . MET B 99  ? 0.5628 0.5977 0.5546 -0.0428 -0.0946 0.0135  101 MET B CA  
2384 C C   . MET B 99  ? 0.5739 0.5924 0.5576 -0.0469 -0.0965 0.0058  101 MET B C   
2385 O O   . MET B 99  ? 0.5708 0.5747 0.5518 -0.0505 -0.0963 0.0034  101 MET B O   
2386 C CB  . MET B 99  ? 0.5649 0.6171 0.5635 -0.0483 -0.0972 0.0134  101 MET B CB  
2387 C CG  . MET B 99  ? 0.6065 0.6785 0.6164 -0.0424 -0.0977 0.0207  101 MET B CG  
2388 S SD  . MET B 99  ? 0.8144 0.8983 0.8190 -0.0370 -0.1034 0.0251  101 MET B SD  
2389 C CE  . MET B 99  ? 0.8160 0.9132 0.8351 -0.0276 -0.1028 0.0350  101 MET B CE  
2390 N N   . TRP B 100 ? 0.5827 0.6024 0.5620 -0.0464 -0.0981 0.0018  102 TRP B N   
2391 C CA  . TRP B 100 ? 0.6064 0.6106 0.5814 -0.0482 -0.0992 -0.0063 102 TRP B CA  
2392 C C   . TRP B 100 ? 0.5986 0.5966 0.5705 -0.0563 -0.1025 -0.0117 102 TRP B C   
2393 O O   . TRP B 100 ? 0.6116 0.5922 0.5809 -0.0571 -0.1041 -0.0172 102 TRP B O   
2394 C CB  . TRP B 100 ? 0.6182 0.6256 0.5903 -0.0463 -0.0979 -0.0108 102 TRP B CB  
2395 C CG  . TRP B 100 ? 0.6391 0.6549 0.6050 -0.0525 -0.1000 -0.0164 102 TRP B CG  
2396 C CD1 . TRP B 100 ? 0.6553 0.6876 0.6166 -0.0544 -0.1016 -0.0129 102 TRP B CD1 
2397 C CD2 . TRP B 100 ? 0.6507 0.6576 0.6135 -0.0576 -0.1014 -0.0267 102 TRP B CD2 
2398 N NE1 . TRP B 100 ? 0.6604 0.6954 0.6146 -0.0615 -0.1040 -0.0207 102 TRP B NE1 
2399 C CE2 . TRP B 100 ? 0.6618 0.6811 0.6173 -0.0636 -0.1030 -0.0296 102 TRP B CE2 
2400 C CE3 . TRP B 100 ? 0.6660 0.6548 0.6314 -0.0575 -0.1022 -0.0336 102 TRP B CE3 
2401 C CZ2 . TRP B 100 ? 0.6748 0.6888 0.6254 -0.0699 -0.1038 -0.0402 102 TRP B CZ2 
2402 C CZ3 . TRP B 100 ? 0.6821 0.6651 0.6441 -0.0627 -0.1033 -0.0435 102 TRP B CZ3 
2403 C CH2 . TRP B 100 ? 0.6811 0.6767 0.6358 -0.0692 -0.1033 -0.0472 102 TRP B CH2 
2404 N N   . GLU B 101 ? 0.5772 0.5890 0.5505 -0.0622 -0.1037 -0.0103 103 GLU B N   
2405 C CA  . GLU B 101 ? 0.5664 0.5739 0.5371 -0.0716 -0.1057 -0.0154 103 GLU B CA  
2406 C C   . GLU B 101 ? 0.5504 0.5420 0.5194 -0.0746 -0.1039 -0.0134 103 GLU B C   
2407 O O   . GLU B 101 ? 0.5531 0.5313 0.5163 -0.0818 -0.1052 -0.0180 103 GLU B O   
2408 C CB  . GLU B 101 ? 0.5808 0.6112 0.5561 -0.0774 -0.1077 -0.0149 103 GLU B CB  
2409 C CG  . GLU B 101 ? 0.6349 0.6803 0.6074 -0.0760 -0.1108 -0.0162 103 GLU B CG  
2410 C CD  . GLU B 101 ? 0.6755 0.7358 0.6519 -0.0680 -0.1109 -0.0078 103 GLU B CD  
2411 O OE1 . GLU B 101 ? 0.6512 0.7072 0.6329 -0.0614 -0.1073 -0.0016 103 GLU B OE1 
2412 O OE2 . GLU B 101 ? 0.6996 0.7741 0.6723 -0.0685 -0.1149 -0.0072 103 GLU B OE2 
2413 N N   . ASP B 102 ? 0.5356 0.5261 0.5075 -0.0698 -0.1005 -0.0067 104 ASP B N   
2414 C CA  . ASP B 102 ? 0.5385 0.5097 0.5043 -0.0728 -0.0982 -0.0048 104 ASP B CA  
2415 C C   . ASP B 102 ? 0.5494 0.4942 0.5044 -0.0743 -0.1026 -0.0093 104 ASP B C   
2416 O O   . ASP B 102 ? 0.5373 0.4785 0.4934 -0.0688 -0.1060 -0.0130 104 ASP B O   
2417 C CB  . ASP B 102 ? 0.5427 0.5111 0.5101 -0.0653 -0.0948 0.0012  104 ASP B CB  
2418 C CG  . ASP B 102 ? 0.5987 0.5511 0.5582 -0.0696 -0.0910 0.0038  104 ASP B CG  
2419 O OD1 . ASP B 102 ? 0.6107 0.5744 0.5756 -0.0731 -0.0850 0.0061  104 ASP B OD1 
2420 O OD2 . ASP B 102 ? 0.5935 0.5218 0.5413 -0.0693 -0.0942 0.0033  104 ASP B OD2 
2421 N N   . GLU B 103 ? 0.5677 0.4939 0.5126 -0.0817 -0.1023 -0.0091 105 GLU B N   
2422 C CA  . GLU B 103 ? 0.5967 0.4939 0.5299 -0.0828 -0.1077 -0.0119 105 GLU B CA  
2423 C C   . GLU B 103 ? 0.5837 0.4677 0.5159 -0.0726 -0.1121 -0.0102 105 GLU B C   
2424 O O   . GLU B 103 ? 0.6010 0.4684 0.5310 -0.0693 -0.1186 -0.0142 105 GLU B O   
2425 C CB  . GLU B 103 ? 0.6710 0.5488 0.5899 -0.0937 -0.1058 -0.0102 105 GLU B CB  
2426 C CG  . GLU B 103 ? 0.7896 0.6608 0.7013 -0.0946 -0.1011 -0.0038 105 GLU B CG  
2427 C CD  . GLU B 103 ? 0.9592 0.8126 0.8552 -0.1074 -0.0965 -0.0024 105 GLU B CD  
2428 O OE1 . GLU B 103 ? 0.9864 0.8273 0.8752 -0.1155 -0.0982 -0.0058 105 GLU B OE1 
2429 O OE2 . GLU B 103 ? 1.0023 0.8530 0.8925 -0.1100 -0.0902 0.0016  105 GLU B OE2 
2430 N N   . LYS B 104 ? 0.5502 0.4418 0.4856 -0.0676 -0.1087 -0.0051 106 LYS B N   
2431 C CA  . LYS B 104 ? 0.5340 0.4155 0.4701 -0.0589 -0.1128 -0.0042 106 LYS B CA  
2432 C C   . LYS B 104 ? 0.4968 0.3952 0.4473 -0.0506 -0.1125 -0.0072 106 LYS B C   
2433 O O   . LYS B 104 ? 0.5014 0.3927 0.4555 -0.0439 -0.1160 -0.0084 106 LYS B O   
2434 C CB  . LYS B 104 ? 0.5708 0.4475 0.5004 -0.0590 -0.1091 0.0019  106 LYS B CB  
2435 C CG  . LYS B 104 ? 0.6530 0.5055 0.5634 -0.0675 -0.1099 0.0044  106 LYS B CG  
2436 C CD  . LYS B 104 ? 0.7575 0.5813 0.6563 -0.0643 -0.1208 0.0040  106 LYS B CD  
2437 C CE  . LYS B 104 ? 0.8501 0.6451 0.7245 -0.0732 -0.1227 0.0075  106 LYS B CE  
2438 N NZ  . LYS B 104 ? 0.9308 0.7025 0.7969 -0.0744 -0.1325 0.0052  106 LYS B NZ  
2439 N N   . ASN B 105 ? 0.4592 0.3791 0.4174 -0.0514 -0.1086 -0.0088 107 ASN B N   
2440 C CA  . ASN B 105 ? 0.4457 0.3788 0.4134 -0.0453 -0.1073 -0.0117 107 ASN B CA  
2441 C C   . ASN B 105 ? 0.4721 0.4074 0.4416 -0.0473 -0.1092 -0.0199 107 ASN B C   
2442 O O   . ASN B 105 ? 0.4641 0.4034 0.4400 -0.0428 -0.1083 -0.0247 107 ASN B O   
2443 C CB  . ASN B 105 ? 0.4332 0.3876 0.4053 -0.0441 -0.1017 -0.0063 107 ASN B CB  
2444 C CG  . ASN B 105 ? 0.4414 0.3954 0.4136 -0.0418 -0.0981 0.0007  107 ASN B CG  
2445 O OD1 . ASN B 105 ? 0.4402 0.3809 0.4107 -0.0385 -0.0992 0.0013  107 ASN B OD1 
2446 N ND2 . ASN B 105 ? 0.4245 0.3939 0.3998 -0.0433 -0.0942 0.0054  107 ASN B ND2 
2447 N N   . LYS B 106 ? 0.5021 0.4345 0.4659 -0.0548 -0.1107 -0.0223 108 LYS B N   
2448 C CA  . LYS B 106 ? 0.5279 0.4644 0.4925 -0.0578 -0.1112 -0.0307 108 LYS B CA  
2449 C C   . LYS B 106 ? 0.5088 0.4322 0.4785 -0.0525 -0.1138 -0.0388 108 LYS B C   
2450 O O   . LYS B 106 ? 0.5069 0.4389 0.4802 -0.0522 -0.1112 -0.0458 108 LYS B O   
2451 C CB  . LYS B 106 ? 0.5990 0.5332 0.5571 -0.0677 -0.1124 -0.0331 108 LYS B CB  
2452 C CG  . LYS B 106 ? 0.7256 0.6359 0.6755 -0.0724 -0.1156 -0.0319 108 LYS B CG  
2453 C CD  . LYS B 106 ? 0.8342 0.7453 0.7785 -0.0840 -0.1149 -0.0348 108 LYS B CD  
2454 C CE  . LYS B 106 ? 0.9285 0.8100 0.8627 -0.0890 -0.1185 -0.0374 108 LYS B CE  
2455 N NZ  . LYS B 106 ? 0.9833 0.8647 0.9135 -0.1004 -0.1175 -0.0432 108 LYS B NZ  
2456 N N   . ARG B 107 ? 0.4914 0.3944 0.4615 -0.0484 -0.1190 -0.0383 109 ARG B N   
2457 C CA  . ARG B 107 ? 0.4810 0.3727 0.4602 -0.0421 -0.1227 -0.0466 109 ARG B CA  
2458 C C   . ARG B 107 ? 0.4431 0.3419 0.4343 -0.0337 -0.1214 -0.0468 109 ARG B C   
2459 O O   . ARG B 107 ? 0.4305 0.3201 0.4325 -0.0276 -0.1256 -0.0531 109 ARG B O   
2460 C CB  . ARG B 107 ? 0.5417 0.4059 0.5149 -0.0420 -0.1314 -0.0463 109 ARG B CB  
2461 C CG  . ARG B 107 ? 0.6164 0.4708 0.5785 -0.0513 -0.1318 -0.0481 109 ARG B CG  
2462 C CD  . ARG B 107 ? 0.7121 0.5356 0.6643 -0.0520 -0.1402 -0.0460 109 ARG B CD  
2463 N NE  . ARG B 107 ? 0.8380 0.6531 0.7788 -0.0532 -0.1420 -0.0356 109 ARG B NE  
2464 C CZ  . ARG B 107 ? 0.9030 0.7199 0.8312 -0.0625 -0.1374 -0.0291 109 ARG B CZ  
2465 N NH1 . ARG B 107 ? 0.8967 0.7249 0.8233 -0.0713 -0.1318 -0.0315 109 ARG B NH1 
2466 N NH2 . ARG B 107 ? 0.9129 0.7209 0.8306 -0.0634 -0.1380 -0.0210 109 ARG B NH2 
2467 N N   . GLY B 108 ? 0.4176 0.3324 0.4081 -0.0336 -0.1157 -0.0404 110 GLY B N   
2468 C CA  . GLY B 108 ? 0.4261 0.3443 0.4245 -0.0275 -0.1145 -0.0381 110 GLY B CA  
2469 C C   . GLY B 108 ? 0.4117 0.3470 0.4181 -0.0258 -0.1065 -0.0419 110 GLY B C   
2470 O O   . GLY B 108 ? 0.4035 0.3455 0.4107 -0.0283 -0.1029 -0.0489 110 GLY B O   
2471 N N   . GLY B 109 ? 0.4024 0.3428 0.4130 -0.0223 -0.1035 -0.0378 111 GLY B N   
2472 C CA  . GLY B 109 ? 0.3954 0.3504 0.4096 -0.0219 -0.0947 -0.0386 111 GLY B CA  
2473 C C   . GLY B 109 ? 0.3783 0.3355 0.3945 -0.0190 -0.0918 -0.0319 111 GLY B C   
2474 O O   . GLY B 109 ? 0.3621 0.3121 0.3741 -0.0181 -0.0957 -0.0253 111 GLY B O   
2475 N N   . ARG B 110 ? 0.3719 0.3377 0.3935 -0.0182 -0.0841 -0.0342 112 ARG B N   
2476 C CA  . ARG B 110 ? 0.3471 0.3155 0.3687 -0.0166 -0.0793 -0.0276 112 ARG B CA  
2477 C C   . ARG B 110 ? 0.3395 0.3110 0.3738 -0.0154 -0.0731 -0.0348 112 ARG B C   
2478 O O   . ARG B 110 ? 0.3376 0.3150 0.3751 -0.0175 -0.0675 -0.0425 112 ARG B O   
2479 C CB  . ARG B 110 ? 0.3507 0.3277 0.3596 -0.0188 -0.0745 -0.0183 112 ARG B CB  
2480 C CG  . ARG B 110 ? 0.3686 0.3541 0.3727 -0.0219 -0.0680 -0.0215 112 ARG B CG  
2481 C CD  . ARG B 110 ? 0.4013 0.3937 0.3927 -0.0230 -0.0659 -0.0114 112 ARG B CD  
2482 N NE  . ARG B 110 ? 0.4876 0.4855 0.4700 -0.0267 -0.0597 -0.0138 112 ARG B NE  
2483 C CZ  . ARG B 110 ? 0.5327 0.5362 0.5010 -0.0282 -0.0587 -0.0055 112 ARG B CZ  
2484 N NH1 . ARG B 110 ? 0.5696 0.5757 0.5261 -0.0327 -0.0532 -0.0081 112 ARG B NH1 
2485 N NH2 . ARG B 110 ? 0.5260 0.5323 0.4919 -0.0251 -0.0632 0.0052  112 ARG B NH2 
2486 N N   . TRP B 111 ? 0.3364 0.3039 0.3780 -0.0128 -0.0734 -0.0334 113 TRP B N   
2487 C CA  . TRP B 111 ? 0.3425 0.3145 0.3947 -0.0131 -0.0653 -0.0379 113 TRP B CA  
2488 C C   . TRP B 111 ? 0.3338 0.3096 0.3734 -0.0155 -0.0559 -0.0289 113 TRP B C   
2489 O O   . TRP B 111 ? 0.3452 0.3174 0.3762 -0.0141 -0.0576 -0.0191 113 TRP B O   
2490 C CB  . TRP B 111 ? 0.3490 0.3149 0.4121 -0.0103 -0.0700 -0.0392 113 TRP B CB  
2491 C CG  . TRP B 111 ? 0.3624 0.3247 0.4410 -0.0073 -0.0796 -0.0490 113 TRP B CG  
2492 C CD1 . TRP B 111 ? 0.3816 0.3326 0.4580 -0.0044 -0.0925 -0.0476 113 TRP B CD1 
2493 C CD2 . TRP B 111 ? 0.3599 0.3291 0.4589 -0.0065 -0.0772 -0.0620 113 TRP B CD2 
2494 N NE1 . TRP B 111 ? 0.3716 0.3212 0.4657 -0.0009 -0.1000 -0.0582 113 TRP B NE1 
2495 C CE2 . TRP B 111 ? 0.3634 0.3256 0.4740 -0.0018 -0.0905 -0.0679 113 TRP B CE2 
2496 C CE3 . TRP B 111 ? 0.3627 0.3429 0.4712 -0.0097 -0.0645 -0.0697 113 TRP B CE3 
2497 C CZ2 . TRP B 111 ? 0.3756 0.3430 0.5102 0.0011  -0.0921 -0.0815 113 TRP B CZ2 
2498 C CZ3 . TRP B 111 ? 0.3609 0.3470 0.4931 -0.0081 -0.0643 -0.0841 113 TRP B CZ3 
2499 C CH2 . TRP B 111 ? 0.3720 0.3527 0.5189 -0.0021 -0.0783 -0.0901 113 TRP B CH2 
2500 N N   . LEU B 112 ? 0.3315 0.3131 0.3695 -0.0189 -0.0463 -0.0322 114 LEU B N   
2501 C CA  . LEU B 112 ? 0.3577 0.3407 0.3795 -0.0213 -0.0386 -0.0226 114 LEU B CA  
2502 C C   . LEU B 112 ? 0.3696 0.3508 0.3948 -0.0236 -0.0279 -0.0235 114 LEU B C   
2503 O O   . LEU B 112 ? 0.3911 0.3755 0.4290 -0.0264 -0.0220 -0.0347 114 LEU B O   
2504 C CB  . LEU B 112 ? 0.3661 0.3545 0.3751 -0.0254 -0.0356 -0.0241 114 LEU B CB  
2505 C CG  . LEU B 112 ? 0.4055 0.3942 0.3938 -0.0276 -0.0307 -0.0129 114 LEU B CG  
2506 C CD1 . LEU B 112 ? 0.4041 0.3928 0.3852 -0.0234 -0.0387 -0.0006 114 LEU B CD1 
2507 C CD2 . LEU B 112 ? 0.4185 0.4118 0.3928 -0.0333 -0.0274 -0.0168 114 LEU B CD2 
2508 N N   . ILE B 113 ? 0.3522 0.3284 0.3673 -0.0226 -0.0250 -0.0121 115 ILE B N   
2509 C CA  . ILE B 113 ? 0.3768 0.3480 0.3900 -0.0254 -0.0142 -0.0098 115 ILE B CA  
2510 C C   . ILE B 113 ? 0.3867 0.3552 0.3774 -0.0268 -0.0100 0.0016  115 ILE B C   
2511 O O   . ILE B 113 ? 0.3388 0.3052 0.3207 -0.0223 -0.0157 0.0128  115 ILE B O   
2512 C CB  . ILE B 113 ? 0.4097 0.3733 0.4295 -0.0222 -0.0154 -0.0055 115 ILE B CB  
2513 C CG1 . ILE B 113 ? 0.4313 0.3953 0.4664 -0.0190 -0.0256 -0.0121 115 ILE B CG1 
2514 C CG2 . ILE B 113 ? 0.4208 0.3793 0.4435 -0.0266 -0.0037 -0.0075 115 ILE B CG2 
2515 C CD1 . ILE B 113 ? 0.4400 0.4093 0.4950 -0.0208 -0.0264 -0.0268 115 ILE B CD1 
2516 N N   . THR B 114 ? 0.4227 0.3910 0.4040 -0.0331 -0.0002 -0.0014 116 THR B N   
2517 C CA  . THR B 114 ? 0.4862 0.4491 0.4436 -0.0351 0.0035  0.0094  116 THR B CA  
2518 C C   . THR B 114 ? 0.5521 0.5035 0.5060 -0.0374 0.0139  0.0141  116 THR B C   
2519 O O   . THR B 114 ? 0.5650 0.5153 0.5280 -0.0434 0.0243  0.0045  116 THR B O   
2520 C CB  . THR B 114 ? 0.5323 0.4993 0.4772 -0.0420 0.0082  0.0032  116 THR B CB  
2521 O OG1 . THR B 114 ? 0.5679 0.5344 0.5221 -0.0487 0.0211  -0.0088 116 THR B OG1 
2522 C CG2 . THR B 114 ? 0.5175 0.4950 0.4675 -0.0403 -0.0017 -0.0032 116 THR B CG2 
2523 N N   . LEU B 115 ? 0.5811 0.5237 0.5237 -0.0328 0.0113  0.0281  117 LEU B N   
2524 C CA  . LEU B 115 ? 0.6164 0.5445 0.5504 -0.0351 0.0211  0.0347  117 LEU B CA  
2525 C C   . LEU B 115 ? 0.6606 0.5803 0.5658 -0.0395 0.0254  0.0438  117 LEU B C   
2526 O O   . LEU B 115 ? 0.6686 0.5914 0.5599 -0.0357 0.0159  0.0523  117 LEU B O   
2527 C CB  . LEU B 115 ? 0.6151 0.5366 0.5536 -0.0269 0.0158  0.0446  117 LEU B CB  
2528 C CG  . LEU B 115 ? 0.6286 0.5557 0.5905 -0.0231 0.0107  0.0370  117 LEU B CG  
2529 C CD1 . LEU B 115 ? 0.6469 0.5648 0.6101 -0.0167 0.0091  0.0460  117 LEU B CD1 
2530 C CD2 . LEU B 115 ? 0.6312 0.5588 0.6090 -0.0293 0.0184  0.0236  117 LEU B CD2 
2531 N N   . ASN B 116 ? 0.6858 0.5945 0.5811 -0.0481 0.0394  0.0419  118 ASN B N   
2532 C CA  . ASN B 116 ? 0.7383 0.6335 0.6013 -0.0529 0.0441  0.0525  118 ASN B CA  
2533 C C   . ASN B 116 ? 0.7746 0.6531 0.6252 -0.0459 0.0404  0.0701  118 ASN B C   
2534 O O   . ASN B 116 ? 0.7690 0.6470 0.6376 -0.0386 0.0368  0.0719  118 ASN B O   
2535 C CB  . ASN B 116 ? 0.7684 0.6570 0.6221 -0.0664 0.0619  0.0434  118 ASN B CB  
2536 C CG  . ASN B 116 ? 0.8290 0.7079 0.6938 -0.0720 0.0759  0.0387  118 ASN B CG  
2537 O OD1 . ASN B 116 ? 0.8430 0.7120 0.7134 -0.0667 0.0744  0.0462  118 ASN B OD1 
2538 N ND2 . ASN B 116 ? 0.8523 0.7341 0.7214 -0.0837 0.0909  0.0247  118 ASN B ND2 
2539 N N   . LYS B 117 ? 0.8105 0.6744 0.6299 -0.0481 0.0408  0.0827  119 LYS B N   
2540 C CA  . LYS B 117 ? 0.8438 0.6917 0.6492 -0.0399 0.0342  0.1008  119 LYS B CA  
2541 C C   . LYS B 117 ? 0.8581 0.6915 0.6754 -0.0375 0.0420  0.1032  119 LYS B C   
2542 O O   . LYS B 117 ? 0.8525 0.6833 0.6793 -0.0265 0.0339  0.1115  119 LYS B O   
2543 C CB  . LYS B 117 ? 0.9029 0.7326 0.6685 -0.0458 0.0363  0.1127  119 LYS B CB  
2544 C CG  . LYS B 117 ? 0.9780 0.8189 0.7267 -0.0456 0.0242  0.1151  119 LYS B CG  
2545 C CD  . LYS B 117 ? 1.0431 0.8966 0.7899 -0.0573 0.0320  0.0989  119 LYS B CD  
2546 C CE  . LYS B 117 ? 1.1047 0.9590 0.8206 -0.0608 0.0236  0.1041  119 LYS B CE  
2547 N NZ  . LYS B 117 ? 1.1098 0.9821 0.8319 -0.0682 0.0263  0.0872  119 LYS B NZ  
2548 N N   . GLN B 118 ? 0.8765 0.7007 0.6942 -0.0482 0.0582  0.0951  120 GLN B N   
2549 C CA  . GLN B 118 ? 0.8923 0.7011 0.7194 -0.0482 0.0669  0.0962  120 GLN B CA  
2550 C C   . GLN B 118 ? 0.8687 0.6930 0.7309 -0.0425 0.0629  0.0854  120 GLN B C   
2551 O O   . GLN B 118 ? 0.8694 0.6835 0.7401 -0.0370 0.0631  0.0898  120 GLN B O   
2552 C CB  . GLN B 118 ? 0.9324 0.7274 0.7488 -0.0632 0.0862  0.0900  120 GLN B CB  
2553 C CG  . GLN B 118 ? 0.9784 0.7926 0.8173 -0.0726 0.0949  0.0692  120 GLN B CG  
2554 C CD  . GLN B 118 ? 1.0566 0.8655 0.8767 -0.0877 0.1105  0.0631  120 GLN B CD  
2555 O OE1 . GLN B 118 ? 1.0880 0.8736 0.8763 -0.0943 0.1188  0.0739  120 GLN B OE1 
2556 N NE2 . GLN B 118 ? 1.0618 0.8913 0.9011 -0.0937 0.1150  0.0452  120 GLN B NE2 
2557 N N   . GLN B 119 ? 0.8398 0.6868 0.7204 -0.0442 0.0593  0.0714  121 GLN B N   
2558 C CA  . GLN B 119 ? 0.8108 0.6719 0.7206 -0.0391 0.0531  0.0618  121 GLN B CA  
2559 C C   . GLN B 119 ? 0.7917 0.6557 0.7058 -0.0266 0.0399  0.0709  121 GLN B C   
2560 O O   . GLN B 119 ? 0.7916 0.6617 0.7253 -0.0229 0.0363  0.0649  121 GLN B O   
2561 C CB  . GLN B 119 ? 0.8178 0.7000 0.7432 -0.0424 0.0501  0.0468  121 GLN B CB  
2562 C CG  . GLN B 119 ? 0.8514 0.7366 0.7867 -0.0536 0.0630  0.0323  121 GLN B CG  
2563 C CD  . GLN B 119 ? 0.8858 0.7914 0.8400 -0.0538 0.0574  0.0182  121 GLN B CD  
2564 O OE1 . GLN B 119 ? 0.8987 0.8116 0.8438 -0.0562 0.0567  0.0157  121 GLN B OE1 
2565 N NE2 . GLN B 119 ? 0.8932 0.8074 0.8732 -0.0511 0.0526  0.0086  121 GLN B NE2 
2566 N N   . ARG B 120 ? 0.7813 0.6418 0.6784 -0.0203 0.0322  0.0845  122 ARG B N   
2567 C CA  . ARG B 120 ? 0.7761 0.6403 0.6814 -0.0084 0.0212  0.0923  122 ARG B CA  
2568 C C   . ARG B 120 ? 0.7979 0.6464 0.7111 -0.0046 0.0269  0.0954  122 ARG B C   
2569 O O   . ARG B 120 ? 0.8059 0.6600 0.7378 -0.0012 0.0250  0.0892  122 ARG B O   
2570 C CB  . ARG B 120 ? 0.7820 0.6453 0.6696 -0.0022 0.0116  0.1063  122 ARG B CB  
2571 C CG  . ARG B 120 ? 0.7897 0.6549 0.6881 0.0106  0.0021  0.1150  122 ARG B CG  
2572 C CD  . ARG B 120 ? 0.8194 0.6849 0.7026 0.0168  -0.0086 0.1284  122 ARG B CD  
2573 N NE  . ARG B 120 ? 0.8459 0.7327 0.7296 0.0152  -0.0182 0.1238  122 ARG B NE  
2574 C CZ  . ARG B 120 ? 0.8789 0.7733 0.7540 0.0201  -0.0305 0.1324  122 ARG B CZ  
2575 N NH1 . ARG B 120 ? 0.8903 0.7728 0.7556 0.0281  -0.0361 0.1471  122 ARG B NH1 
2576 N NH2 . ARG B 120 ? 0.8610 0.7744 0.7374 0.0171  -0.0381 0.1264  122 ARG B NH2 
2577 N N   . ARG B 121 ? 0.7996 0.6265 0.6963 -0.0061 0.0343  0.1048  123 ARG B N   
2578 C CA  . ARG B 121 ? 0.8087 0.6166 0.7092 -0.0021 0.0402  0.1096  123 ARG B CA  
2579 C C   . ARG B 121 ? 0.7813 0.5915 0.7013 -0.0079 0.0477  0.0951  123 ARG B C   
2580 O O   . ARG B 121 ? 0.7830 0.5907 0.7161 -0.0023 0.0467  0.0938  123 ARG B O   
2581 C CB  . ARG B 121 ? 0.8598 0.6405 0.7362 -0.0057 0.0490  0.1209  123 ARG B CB  
2582 C CG  . ARG B 121 ? 0.9358 0.7136 0.7853 -0.0105 0.0474  0.1283  123 ARG B CG  
2583 C CD  . ARG B 121 ? 1.0122 0.7595 0.8340 -0.0131 0.0544  0.1420  123 ARG B CD  
2584 N NE  . ARG B 121 ? 1.0691 0.8107 0.8707 -0.0281 0.0656  0.1377  123 ARG B NE  
2585 C CZ  . ARG B 121 ? 1.1064 0.8420 0.9123 -0.0407 0.0817  0.1266  123 ARG B CZ  
2586 N NH1 . ARG B 121 ? 1.1066 0.8386 0.8947 -0.0544 0.0925  0.1223  123 ARG B NH1 
2587 N NH2 . ARG B 121 ? 1.1062 0.8397 0.9346 -0.0404 0.0876  0.1191  123 ARG B NH2 
2588 N N   . SER B 122 ? 0.7533 0.5695 0.6757 -0.0191 0.0546  0.0837  124 SER B N   
2589 C CA  . SER B 122 ? 0.7318 0.5514 0.6725 -0.0260 0.0608  0.0691  124 SER B CA  
2590 C C   . SER B 122 ? 0.6828 0.5236 0.6440 -0.0238 0.0511  0.0576  124 SER B C   
2591 O O   . SER B 122 ? 0.6866 0.5264 0.6617 -0.0242 0.0514  0.0503  124 SER B O   
2592 C CB  . SER B 122 ? 0.7646 0.5823 0.7011 -0.0390 0.0726  0.0615  124 SER B CB  
2593 O OG  . SER B 122 ? 0.7885 0.6210 0.7194 -0.0412 0.0689  0.0592  124 SER B OG  
2594 N N   . ASP B 123 ? 0.6338 0.4918 0.5952 -0.0218 0.0424  0.0560  125 ASP B N   
2595 C CA  . ASP B 123 ? 0.5832 0.4585 0.5617 -0.0216 0.0342  0.0444  125 ASP B CA  
2596 C C   . ASP B 123 ? 0.5236 0.4090 0.5036 -0.0131 0.0219  0.0487  125 ASP B C   
2597 O O   . ASP B 123 ? 0.5039 0.3978 0.4961 -0.0125 0.0157  0.0407  125 ASP B O   
2598 C CB  . ASP B 123 ? 0.6112 0.4990 0.5946 -0.0289 0.0359  0.0337  125 ASP B CB  
2599 C CG  . ASP B 123 ? 0.6629 0.5456 0.6514 -0.0388 0.0485  0.0252  125 ASP B CG  
2600 O OD1 . ASP B 123 ? 0.6718 0.5509 0.6736 -0.0411 0.0510  0.0186  125 ASP B OD1 
2601 O OD2 . ASP B 123 ? 0.6954 0.5781 0.6745 -0.0452 0.0563  0.0244  125 ASP B OD2 
2602 N N   . LEU B 124 ? 0.5007 0.3854 0.4689 -0.0069 0.0179  0.0607  126 LEU B N   
2603 C CA  . LEU B 124 ? 0.4663 0.3635 0.4381 -0.0003 0.0067  0.0632  126 LEU B CA  
2604 C C   . LEU B 124 ? 0.4236 0.3197 0.4073 0.0039  0.0043  0.0605  126 LEU B C   
2605 O O   . LEU B 124 ? 0.4015 0.3076 0.3928 0.0035  -0.0023 0.0539  126 LEU B O   
2606 C CB  . LEU B 124 ? 0.4686 0.3647 0.4281 0.0060  0.0028  0.0766  126 LEU B CB  
2607 C CG  . LEU B 124 ? 0.4553 0.3666 0.4195 0.0121  -0.0084 0.0794  126 LEU B CG  
2608 C CD1 . LEU B 124 ? 0.4364 0.3621 0.3999 0.0073  -0.0139 0.0723  126 LEU B CD1 
2609 C CD2 . LEU B 124 ? 0.4952 0.4049 0.4503 0.0191  -0.0130 0.0928  126 LEU B CD2 
2610 N N   . ASN B 125 ? 0.4169 0.2994 0.4008 0.0073  0.0099  0.0655  127 ASN B N   
2611 C CA  . ASN B 125 ? 0.4183 0.2983 0.4111 0.0107  0.0092  0.0629  127 ASN B CA  
2612 C C   . ASN B 125 ? 0.4094 0.2899 0.4094 0.0042  0.0090  0.0504  127 ASN B C   
2613 O O   . ASN B 125 ? 0.4075 0.2931 0.4119 0.0048  0.0034  0.0458  127 ASN B O   
2614 C CB  . ASN B 125 ? 0.4495 0.3134 0.4411 0.0156  0.0163  0.0698  127 ASN B CB  
2615 C CG  . ASN B 125 ? 0.4982 0.3622 0.4854 0.0245  0.0135  0.0829  127 ASN B CG  
2616 O OD1 . ASN B 125 ? 0.5098 0.3591 0.4898 0.0272  0.0184  0.0911  127 ASN B OD1 
2617 N ND2 . ASN B 125 ? 0.5165 0.3959 0.5079 0.0294  0.0049  0.0853  127 ASN B ND2 
2618 N N   . ARG B 126 ? 0.3984 0.2732 0.3991 -0.0023 0.0147  0.0450  128 ARG B N   
2619 C CA  . ARG B 126 ? 0.3909 0.2669 0.4004 -0.0085 0.0134  0.0328  128 ARG B CA  
2620 C C   . ARG B 126 ? 0.3772 0.2683 0.3914 -0.0095 0.0032  0.0264  128 ARG B C   
2621 O O   . ARG B 126 ? 0.3796 0.2718 0.3976 -0.0097 -0.0034 0.0209  128 ARG B O   
2622 C CB  . ARG B 126 ? 0.4134 0.2832 0.4254 -0.0158 0.0224  0.0279  128 ARG B CB  
2623 C CG  . ARG B 126 ? 0.4459 0.3207 0.4709 -0.0224 0.0196  0.0140  128 ARG B CG  
2624 C CD  . ARG B 126 ? 0.4672 0.3356 0.4951 -0.0222 0.0157  0.0095  128 ARG B CD  
2625 N NE  . ARG B 126 ? 0.5004 0.3519 0.5231 -0.0220 0.0250  0.0137  128 ARG B NE  
2626 C CZ  . ARG B 126 ? 0.5278 0.3703 0.5492 -0.0216 0.0242  0.0111  128 ARG B CZ  
2627 N NH1 . ARG B 126 ? 0.5470 0.3949 0.5696 -0.0220 0.0141  0.0052  128 ARG B NH1 
2628 N NH2 . ARG B 126 ? 0.5154 0.3418 0.5326 -0.0213 0.0338  0.0144  128 ARG B NH2 
2629 N N   . PHE B 127 ? 0.3764 0.2768 0.3886 -0.0103 0.0019  0.0273  129 PHE B N   
2630 C CA  . PHE B 127 ? 0.3955 0.3085 0.4131 -0.0112 -0.0070 0.0204  129 PHE B CA  
2631 C C   . PHE B 127 ? 0.3663 0.2834 0.3804 -0.0065 -0.0155 0.0244  129 PHE B C   
2632 O O   . PHE B 127 ? 0.3582 0.2791 0.3764 -0.0074 -0.0234 0.0182  129 PHE B O   
2633 C CB  . PHE B 127 ? 0.4234 0.3445 0.4384 -0.0136 -0.0050 0.0197  129 PHE B CB  
2634 C CG  . PHE B 127 ? 0.4734 0.3947 0.4948 -0.0202 0.0030  0.0118  129 PHE B CG  
2635 C CD1 . PHE B 127 ? 0.4995 0.4128 0.5278 -0.0240 0.0096  0.0076  129 PHE B CD1 
2636 C CD2 . PHE B 127 ? 0.5071 0.4372 0.5284 -0.0236 0.0049  0.0074  129 PHE B CD2 
2637 C CE1 . PHE B 127 ? 0.5121 0.4272 0.5486 -0.0312 0.0181  -0.0009 129 PHE B CE1 
2638 C CE2 . PHE B 127 ? 0.5146 0.4460 0.5433 -0.0305 0.0142  -0.0012 129 PHE B CE2 
2639 C CZ  . PHE B 127 ? 0.5066 0.4311 0.5438 -0.0344 0.0208  -0.0053 129 PHE B CZ  
2640 N N   . TRP B 128 ? 0.3477 0.2638 0.3548 -0.0017 -0.0140 0.0345  130 TRP B N   
2641 C CA  . TRP B 128 ? 0.3226 0.2439 0.3287 0.0019  -0.0204 0.0373  130 TRP B CA  
2642 C C   . TRP B 128 ? 0.3022 0.2161 0.3104 0.0011  -0.0215 0.0331  130 TRP B C   
2643 O O   . TRP B 128 ? 0.3067 0.2234 0.3142 -0.0002 -0.0283 0.0296  130 TRP B O   
2644 C CB  . TRP B 128 ? 0.3168 0.2407 0.3191 0.0077  -0.0188 0.0482  130 TRP B CB  
2645 C CG  . TRP B 128 ? 0.2900 0.2222 0.2944 0.0106  -0.0243 0.0501  130 TRP B CG  
2646 C CD1 . TRP B 128 ? 0.2989 0.2303 0.3067 0.0155  -0.0220 0.0551  130 TRP B CD1 
2647 C CD2 . TRP B 128 ? 0.2858 0.2288 0.2899 0.0083  -0.0321 0.0469  130 TRP B CD2 
2648 N NE1 . TRP B 128 ? 0.2996 0.2415 0.3101 0.0155  -0.0272 0.0544  130 TRP B NE1 
2649 C CE2 . TRP B 128 ? 0.2957 0.2439 0.3028 0.0108  -0.0337 0.0498  130 TRP B CE2 
2650 C CE3 . TRP B 128 ? 0.2832 0.2311 0.2859 0.0040  -0.0372 0.0409  130 TRP B CE3 
2651 C CZ2 . TRP B 128 ? 0.3045 0.2623 0.3117 0.0084  -0.0401 0.0476  130 TRP B CZ2 
2652 C CZ3 . TRP B 128 ? 0.2896 0.2454 0.2919 0.0024  -0.0440 0.0388  130 TRP B CZ3 
2653 C CH2 . TRP B 128 ? 0.3008 0.2612 0.3046 0.0042  -0.0454 0.0424  130 TRP B CH2 
2654 N N   . LEU B 129 ? 0.3102 0.2123 0.3187 0.0011  -0.0145 0.0333  131 LEU B N   
2655 C CA  . LEU B 129 ? 0.3222 0.2153 0.3299 -0.0010 -0.0150 0.0282  131 LEU B CA  
2656 C C   . LEU B 129 ? 0.3307 0.2238 0.3400 -0.0062 -0.0229 0.0187  131 LEU B C   
2657 O O   . LEU B 129 ? 0.3238 0.2139 0.3283 -0.0078 -0.0291 0.0158  131 LEU B O   
2658 C CB  . LEU B 129 ? 0.3228 0.2023 0.3305 -0.0010 -0.0054 0.0286  131 LEU B CB  
2659 C CG  . LEU B 129 ? 0.3307 0.1992 0.3352 -0.0047 -0.0053 0.0220  131 LEU B CG  
2660 C CD1 . LEU B 129 ? 0.3323 0.2016 0.3316 -0.0031 -0.0071 0.0235  131 LEU B CD1 
2661 C CD2 . LEU B 129 ? 0.3496 0.2045 0.3544 -0.0054 0.0045  0.0214  131 LEU B CD2 
2662 N N   . GLU B 130 ? 0.3245 0.2205 0.3407 -0.0090 -0.0228 0.0138  132 GLU B N   
2663 C CA  . GLU B 130 ? 0.3228 0.2200 0.3447 -0.0126 -0.0314 0.0042  132 GLU B CA  
2664 C C   . GLU B 130 ? 0.3371 0.2409 0.3571 -0.0114 -0.0419 0.0034  132 GLU B C   
2665 O O   . GLU B 130 ? 0.3233 0.2226 0.3417 -0.0130 -0.0516 -0.0015 132 GLU B O   
2666 C CB  . GLU B 130 ? 0.3265 0.2285 0.3603 -0.0158 -0.0284 -0.0022 132 GLU B CB  
2667 C CG  . GLU B 130 ? 0.3918 0.2855 0.4276 -0.0187 -0.0181 -0.0028 132 GLU B CG  
2668 C CD  . GLU B 130 ? 0.4652 0.3479 0.4996 -0.0215 -0.0201 -0.0075 132 GLU B CD  
2669 O OE1 . GLU B 130 ? 0.4250 0.3077 0.4592 -0.0224 -0.0314 -0.0128 132 GLU B OE1 
2670 O OE2 . GLU B 130 ? 0.4823 0.3548 0.5140 -0.0230 -0.0108 -0.0058 132 GLU B OE2 
2671 N N   . THR B 131 ? 0.3392 0.2522 0.3581 -0.0090 -0.0406 0.0085  133 THR B N   
2672 C CA  . THR B 131 ? 0.3471 0.2655 0.3627 -0.0082 -0.0487 0.0087  133 THR B CA  
2673 C C   . THR B 131 ? 0.3639 0.2752 0.3697 -0.0084 -0.0523 0.0115  133 THR B C   
2674 O O   . THR B 131 ? 0.3618 0.2693 0.3639 -0.0102 -0.0612 0.0081  133 THR B O   
2675 C CB  . THR B 131 ? 0.3350 0.2640 0.3494 -0.0062 -0.0456 0.0141  133 THR B CB  
2676 O OG1 . THR B 131 ? 0.3365 0.2701 0.3570 -0.0076 -0.0414 0.0107  133 THR B OG1 
2677 C CG2 . THR B 131 ? 0.3296 0.2640 0.3411 -0.0064 -0.0532 0.0137  133 THR B CG2 
2678 N N   . LEU B 132 ? 0.3689 0.2774 0.3705 -0.0069 -0.0448 0.0174  134 LEU B N   
2679 C CA  . LEU B 132 ? 0.3774 0.2797 0.3703 -0.0080 -0.0451 0.0191  134 LEU B CA  
2680 C C   . LEU B 132 ? 0.3837 0.2719 0.3692 -0.0123 -0.0495 0.0134  134 LEU B C   
2681 O O   . LEU B 132 ? 0.4029 0.2845 0.3780 -0.0153 -0.0542 0.0128  134 LEU B O   
2682 C CB  . LEU B 132 ? 0.3760 0.2785 0.3699 -0.0048 -0.0349 0.0249  134 LEU B CB  
2683 C CG  . LEU B 132 ? 0.3865 0.3021 0.3864 0.0001  -0.0322 0.0318  134 LEU B CG  
2684 C CD1 . LEU B 132 ? 0.3929 0.3069 0.3964 0.0046  -0.0235 0.0370  134 LEU B CD1 
2685 C CD2 . LEU B 132 ? 0.3967 0.3223 0.3954 -0.0009 -0.0377 0.0330  134 LEU B CD2 
2686 N N   . LEU B 133 ? 0.3712 0.2539 0.3605 -0.0133 -0.0484 0.0092  135 LEU B N   
2687 C CA  . LEU B 133 ? 0.3786 0.2482 0.3604 -0.0176 -0.0545 0.0034  135 LEU B CA  
2688 C C   . LEU B 133 ? 0.3532 0.2215 0.3338 -0.0190 -0.0688 -0.0010 135 LEU B C   
2689 O O   . LEU B 133 ? 0.3812 0.2368 0.3482 -0.0224 -0.0761 -0.0026 135 LEU B O   
2690 C CB  . LEU B 133 ? 0.3852 0.2506 0.3734 -0.0189 -0.0499 -0.0008 135 LEU B CB  
2691 C CG  . LEU B 133 ? 0.3869 0.2486 0.3749 -0.0175 -0.0358 0.0032  135 LEU B CG  
2692 C CD1 . LEU B 133 ? 0.3846 0.2392 0.3773 -0.0205 -0.0317 -0.0021 135 LEU B CD1 
2693 C CD2 . LEU B 133 ? 0.4034 0.2554 0.3785 -0.0188 -0.0314 0.0050  135 LEU B CD2 
2694 N N   . CYS B 134 ? 0.3189 0.1984 0.3122 -0.0164 -0.0726 -0.0029 136 CYS B N   
2695 C CA  . CYS B 134 ? 0.3117 0.1916 0.3080 -0.0160 -0.0851 -0.0070 136 CYS B CA  
2696 C C   . CYS B 134 ? 0.3371 0.2106 0.3186 -0.0172 -0.0902 -0.0029 136 CYS B C   
2697 O O   . CYS B 134 ? 0.3389 0.2017 0.3132 -0.0185 -0.1024 -0.0053 136 CYS B O   
2698 C CB  . CYS B 134 ? 0.3441 0.2389 0.3575 -0.0131 -0.0838 -0.0099 136 CYS B CB  
2699 S SG  . CYS B 134 ? 0.3346 0.2358 0.3676 -0.0136 -0.0813 -0.0184 136 CYS B SG  
2700 N N   . LEU B 135 ? 0.3307 0.2105 0.3087 -0.0168 -0.0814 0.0032  137 LEU B N   
2701 C CA  . LEU B 135 ? 0.3455 0.2214 0.3115 -0.0191 -0.0835 0.0067  137 LEU B CA  
2702 C C   . LEU B 135 ? 0.3687 0.2278 0.3162 -0.0241 -0.0835 0.0077  137 LEU B C   
2703 O O   . LEU B 135 ? 0.3860 0.2314 0.3203 -0.0275 -0.0931 0.0066  137 LEU B O   
2704 C CB  . LEU B 135 ? 0.3297 0.2196 0.3002 -0.0175 -0.0746 0.0120  137 LEU B CB  
2705 C CG  . LEU B 135 ? 0.3425 0.2446 0.3209 -0.0157 -0.0779 0.0116  137 LEU B CG  
2706 C CD1 . LEU B 135 ? 0.3188 0.2262 0.3095 -0.0129 -0.0807 0.0065  137 LEU B CD1 
2707 C CD2 . LEU B 135 ? 0.3423 0.2585 0.3247 -0.0141 -0.0700 0.0170  137 LEU B CD2 
2708 N N   . ILE B 136 ? 0.3833 0.2412 0.3284 -0.0249 -0.0728 0.0094  138 ILE B N   
2709 C CA  . ILE B 136 ? 0.4037 0.2457 0.3297 -0.0307 -0.0701 0.0095  138 ILE B CA  
2710 C C   . ILE B 136 ? 0.4307 0.2554 0.3440 -0.0342 -0.0801 0.0052  138 ILE B C   
2711 O O   . ILE B 136 ? 0.4615 0.2690 0.3531 -0.0404 -0.0836 0.0053  138 ILE B O   
2712 C CB  . ILE B 136 ? 0.4090 0.2539 0.3371 -0.0303 -0.0548 0.0112  138 ILE B CB  
2713 C CG1 . ILE B 136 ? 0.3957 0.2388 0.3309 -0.0281 -0.0511 0.0085  138 ILE B CG1 
2714 C CG2 . ILE B 136 ? 0.3935 0.2571 0.3358 -0.0259 -0.0475 0.0159  138 ILE B CG2 
2715 C CD1 . ILE B 136 ? 0.4175 0.2617 0.3566 -0.0265 -0.0377 0.0098  138 ILE B CD1 
2716 N N   . GLY B 137 ? 0.4337 0.2622 0.3596 -0.0311 -0.0849 0.0012  139 GLY B N   
2717 C CA  . GLY B 137 ? 0.4667 0.2815 0.3845 -0.0338 -0.0969 -0.0037 139 GLY B CA  
2718 C C   . GLY B 137 ? 0.4837 0.2919 0.3981 -0.0332 -0.1143 -0.0050 139 GLY B C   
2719 O O   . GLY B 137 ? 0.4727 0.2690 0.3799 -0.0349 -0.1266 -0.0086 139 GLY B O   
2720 N N   . GLU B 138 ? 0.4872 0.3021 0.4068 -0.0306 -0.1164 -0.0025 140 GLU B N   
2721 C CA  . GLU B 138 ? 0.4832 0.2912 0.4023 -0.0287 -0.1328 -0.0040 140 GLU B CA  
2722 C C   . GLU B 138 ? 0.4797 0.2942 0.4196 -0.0237 -0.1440 -0.0111 140 GLU B C   
2723 O O   . GLU B 138 ? 0.4846 0.2860 0.4186 -0.0236 -0.1601 -0.0137 140 GLU B O   
2724 C CB  . GLU B 138 ? 0.5169 0.2996 0.4062 -0.0347 -0.1420 -0.0011 140 GLU B CB  
2725 C CG  . GLU B 138 ? 0.5576 0.3347 0.4284 -0.0408 -0.1301 0.0045  140 GLU B CG  
2726 C CD  . GLU B 138 ? 0.5670 0.3521 0.4431 -0.0399 -0.1272 0.0074  140 GLU B CD  
2727 O OE1 . GLU B 138 ? 0.5133 0.2924 0.3901 -0.0377 -0.1394 0.0069  140 GLU B OE1 
2728 O OE2 . GLU B 138 ? 0.5623 0.3596 0.4425 -0.0412 -0.1129 0.0098  140 GLU B OE2 
2729 N N   . SER B 139 ? 0.4652 0.3003 0.4298 -0.0198 -0.1352 -0.0143 141 SER B N   
2730 C CA  . SER B 139 ? 0.4628 0.3076 0.4497 -0.0169 -0.1397 -0.0221 141 SER B CA  
2731 C C   . SER B 139 ? 0.4589 0.3087 0.4635 -0.0117 -0.1525 -0.0278 141 SER B C   
2732 O O   . SER B 139 ? 0.4443 0.3036 0.4710 -0.0092 -0.1569 -0.0358 141 SER B O   
2733 C CB  . SER B 139 ? 0.4762 0.3376 0.4784 -0.0164 -0.1232 -0.0228 141 SER B CB  
2734 O OG  . SER B 139 ? 0.4817 0.3369 0.4710 -0.0202 -0.1129 -0.0192 141 SER B OG  
2735 N N   . PHE B 140 ? 0.4664 0.3100 0.4634 -0.0102 -0.1580 -0.0247 142 PHE B N   
2736 C CA  . PHE B 140 ? 0.4813 0.3294 0.4963 -0.0045 -0.1683 -0.0304 142 PHE B CA  
2737 C C   . PHE B 140 ? 0.4924 0.3200 0.4955 -0.0030 -0.1880 -0.0298 142 PHE B C   
2738 O O   . PHE B 140 ? 0.4655 0.2918 0.4783 0.0018  -0.1965 -0.0325 142 PHE B O   
2739 C CB  . PHE B 140 ? 0.4781 0.3363 0.4968 -0.0036 -0.1583 -0.0285 142 PHE B CB  
2740 C CG  . PHE B 140 ? 0.4695 0.3451 0.4954 -0.0053 -0.1401 -0.0275 142 PHE B CG  
2741 C CD1 . PHE B 140 ? 0.4520 0.3425 0.5000 -0.0038 -0.1345 -0.0343 142 PHE B CD1 
2742 C CD2 . PHE B 140 ? 0.4804 0.3564 0.4907 -0.0087 -0.1291 -0.0195 142 PHE B CD2 
2743 C CE1 . PHE B 140 ? 0.4499 0.3524 0.5009 -0.0057 -0.1186 -0.0322 142 PHE B CE1 
2744 C CE2 . PHE B 140 ? 0.4645 0.3543 0.4806 -0.0092 -0.1144 -0.0175 142 PHE B CE2 
2745 C CZ  . PHE B 140 ? 0.4457 0.3471 0.4801 -0.0078 -0.1095 -0.0233 142 PHE B CZ  
2746 N N   . ASP B 141 ? 0.5299 0.3396 0.5109 -0.0071 -0.1959 -0.0263 143 ASP B N   
2747 C CA  . ASP B 141 ? 0.5750 0.3620 0.5413 -0.0058 -0.2172 -0.0250 143 ASP B CA  
2748 C C   . ASP B 141 ? 0.5862 0.3575 0.5328 -0.0070 -0.2185 -0.0182 143 ASP B C   
2749 O O   . ASP B 141 ? 0.5974 0.3696 0.5293 -0.0127 -0.2033 -0.0127 143 ASP B O   
2750 C CB  . ASP B 141 ? 0.6219 0.4170 0.6181 0.0021  -0.2335 -0.0345 143 ASP B CB  
2751 C CG  . ASP B 141 ? 0.7785 0.5824 0.7858 0.0004  -0.2349 -0.0404 143 ASP B CG  
2752 O OD1 . ASP B 141 ? 0.8226 0.6145 0.8047 -0.0065 -0.2324 -0.0360 143 ASP B OD1 
2753 O OD2 . ASP B 141 ? 0.8209 0.6440 0.8627 0.0054  -0.2375 -0.0502 143 ASP B OD2 
2754 N N   . ASP B 142 ? 0.5964 0.3538 0.5431 -0.0022 -0.2352 -0.0185 144 ASP B N   
2755 C CA  . ASP B 142 ? 0.6254 0.3663 0.5513 -0.0051 -0.2342 -0.0119 144 ASP B CA  
2756 C C   . ASP B 142 ? 0.6000 0.3623 0.5423 -0.0048 -0.2167 -0.0137 144 ASP B C   
2757 O O   . ASP B 142 ? 0.6011 0.3562 0.5260 -0.0102 -0.2090 -0.0083 144 ASP B O   
2758 C CB  . ASP B 142 ? 0.6833 0.4030 0.6064 0.0005  -0.2550 -0.0117 144 ASP B CB  
2759 C CG  . ASP B 142 ? 0.8251 0.5162 0.7234 -0.0004 -0.2756 -0.0073 144 ASP B CG  
2760 O OD1 . ASP B 142 ? 0.8256 0.5133 0.7079 -0.0061 -0.2743 -0.0054 144 ASP B OD1 
2761 O OD2 . ASP B 142 ? 0.8892 0.5595 0.7828 0.0047  -0.2937 -0.0057 144 ASP B OD2 
2762 N N   . TYR B 143 ? 0.5681 0.3562 0.5427 0.0005  -0.2103 -0.0217 145 TYR B N   
2763 C CA  . TYR B 143 ? 0.5428 0.3491 0.5314 0.0010  -0.1964 -0.0240 145 TYR B CA  
2764 C C   . TYR B 143 ? 0.4915 0.3092 0.4703 -0.0053 -0.1780 -0.0188 145 TYR B C   
2765 O O   . TYR B 143 ? 0.4539 0.2865 0.4416 -0.0055 -0.1673 -0.0198 145 TYR B O   
2766 C CB  . TYR B 143 ? 0.5547 0.3824 0.5786 0.0079  -0.1953 -0.0347 145 TYR B CB  
2767 C CG  . TYR B 143 ? 0.5825 0.4033 0.6237 0.0156  -0.2140 -0.0416 145 TYR B CG  
2768 C CD1 . TYR B 143 ? 0.6113 0.4160 0.6502 0.0197  -0.2261 -0.0420 145 TYR B CD1 
2769 C CD2 . TYR B 143 ? 0.5986 0.4281 0.6588 0.0189  -0.2203 -0.0479 145 TYR B CD2 
2770 C CE1 . TYR B 143 ? 0.6330 0.4314 0.6905 0.0283  -0.2444 -0.0484 145 TYR B CE1 
2771 C CE2 . TYR B 143 ? 0.6179 0.4430 0.6972 0.0268  -0.2390 -0.0548 145 TYR B CE2 
2772 C CZ  . TYR B 143 ? 0.6562 0.4659 0.7348 0.0322  -0.2513 -0.0549 145 TYR B CZ  
2773 O OH  . TYR B 143 ? 0.7296 0.5348 0.8295 0.0414  -0.2711 -0.0617 145 TYR B OH  
2774 N N   . SER B 144 ? 0.4828 0.2933 0.4436 -0.0104 -0.1745 -0.0135 146 SER B N   
2775 C CA  . SER B 144 ? 0.4570 0.2748 0.4073 -0.0159 -0.1582 -0.0081 146 SER B CA  
2776 C C   . SER B 144 ? 0.4595 0.2678 0.3917 -0.0210 -0.1554 -0.0026 146 SER B C   
2777 O O   . SER B 144 ? 0.4630 0.2831 0.3941 -0.0242 -0.1421 0.0005  146 SER B O   
2778 C CB  . SER B 144 ? 0.4657 0.2759 0.4017 -0.0200 -0.1550 -0.0053 146 SER B CB  
2779 O OG  . SER B 144 ? 0.4698 0.2941 0.4231 -0.0174 -0.1500 -0.0095 146 SER B OG  
2780 N N   . ASP B 145 ? 0.4553 0.2422 0.3733 -0.0222 -0.1678 -0.0013 147 ASP B N   
2781 C CA  . ASP B 145 ? 0.4770 0.2552 0.3799 -0.0279 -0.1644 0.0028  147 ASP B CA  
2782 C C   . ASP B 145 ? 0.4535 0.2509 0.3754 -0.0253 -0.1583 -0.0008 147 ASP B C   
2783 O O   . ASP B 145 ? 0.4909 0.2911 0.4054 -0.0309 -0.1503 0.0020  147 ASP B O   
2784 C CB  . ASP B 145 ? 0.5575 0.3047 0.4391 -0.0299 -0.1796 0.0053  147 ASP B CB  
2785 C CG  . ASP B 145 ? 0.6887 0.4133 0.5421 -0.0357 -0.1841 0.0103  147 ASP B CG  
2786 O OD1 . ASP B 145 ? 0.7022 0.4329 0.5473 -0.0413 -0.1712 0.0126  147 ASP B OD1 
2787 O OD2 . ASP B 145 ? 0.7678 0.4679 0.6071 -0.0345 -0.2006 0.0117  147 ASP B OD2 
2788 N N   . ASP B 146 ? 0.3913 0.2022 0.3374 -0.0178 -0.1612 -0.0076 148 ASP B N   
2789 C CA  . ASP B 146 ? 0.3938 0.2228 0.3553 -0.0164 -0.1540 -0.0116 148 ASP B CA  
2790 C C   . ASP B 146 ? 0.3755 0.2270 0.3428 -0.0182 -0.1391 -0.0096 148 ASP B C   
2791 O O   . ASP B 146 ? 0.3684 0.2333 0.3422 -0.0189 -0.1330 -0.0112 148 ASP B O   
2792 C CB  . ASP B 146 ? 0.4292 0.2643 0.4140 -0.0087 -0.1605 -0.0208 148 ASP B CB  
2793 C CG  . ASP B 146 ? 0.4854 0.3034 0.4685 -0.0068 -0.1717 -0.0237 148 ASP B CG  
2794 O OD1 . ASP B 146 ? 0.5279 0.3221 0.4928 -0.0086 -0.1820 -0.0190 148 ASP B OD1 
2795 O OD2 . ASP B 146 ? 0.4767 0.3038 0.4748 -0.0042 -0.1694 -0.0305 148 ASP B OD2 
2796 N N   . VAL B 147 ? 0.3675 0.2223 0.3316 -0.0189 -0.1338 -0.0061 149 VAL B N   
2797 C CA  . VAL B 147 ? 0.3405 0.2144 0.3102 -0.0194 -0.1206 -0.0033 149 VAL B CA  
2798 C C   . VAL B 147 ? 0.3364 0.2115 0.2941 -0.0251 -0.1143 0.0022  149 VAL B C   
2799 O O   . VAL B 147 ? 0.3451 0.2053 0.2870 -0.0299 -0.1160 0.0054  149 VAL B O   
2800 C CB  . VAL B 147 ? 0.3296 0.2038 0.3006 -0.0181 -0.1171 -0.0021 149 VAL B CB  
2801 C CG1 . VAL B 147 ? 0.3169 0.2069 0.2920 -0.0181 -0.1040 0.0020  149 VAL B CG1 
2802 C CG2 . VAL B 147 ? 0.3282 0.2042 0.3148 -0.0132 -0.1229 -0.0089 149 VAL B CG2 
2803 N N   . CYS B 148 ? 0.3253 0.2185 0.2906 -0.0252 -0.1072 0.0029  150 CYS B N   
2804 C CA  . CYS B 148 ? 0.3261 0.2264 0.2858 -0.0300 -0.1008 0.0073  150 CYS B CA  
2805 C C   . CYS B 148 ? 0.3248 0.2373 0.2893 -0.0280 -0.0915 0.0118  150 CYS B C   
2806 O O   . CYS B 148 ? 0.3307 0.2417 0.2893 -0.0313 -0.0866 0.0152  150 CYS B O   
2807 C CB  . CYS B 148 ? 0.3331 0.2456 0.2982 -0.0313 -0.1009 0.0050  150 CYS B CB  
2808 S SG  . CYS B 148 ? 0.4010 0.2969 0.3610 -0.0336 -0.1108 -0.0007 150 CYS B SG  
2809 N N   . GLY B 149 ? 0.3090 0.2322 0.2841 -0.0228 -0.0888 0.0112  151 GLY B N   
2810 C CA  . GLY B 149 ? 0.2969 0.2299 0.2769 -0.0199 -0.0806 0.0158  151 GLY B CA  
2811 C C   . GLY B 149 ? 0.2886 0.2302 0.2775 -0.0154 -0.0782 0.0149  151 GLY B C   
2812 O O   . GLY B 149 ? 0.2710 0.2113 0.2639 -0.0148 -0.0821 0.0094  151 GLY B O   
2813 N N   . ALA B 150 ? 0.2845 0.2342 0.2769 -0.0125 -0.0711 0.0200  152 ALA B N   
2814 C CA  . ALA B 150 ? 0.2886 0.2448 0.2861 -0.0093 -0.0671 0.0208  152 ALA B CA  
2815 C C   . ALA B 150 ? 0.3114 0.2800 0.3095 -0.0071 -0.0635 0.0278  152 ALA B C   
2816 O O   . ALA B 150 ? 0.3166 0.2881 0.3155 -0.0063 -0.0619 0.0321  152 ALA B O   
2817 C CB  . ALA B 150 ? 0.2665 0.2141 0.2663 -0.0075 -0.0628 0.0206  152 ALA B CB  
2818 N N   . VAL B 151 ? 0.3160 0.2918 0.3136 -0.0064 -0.0626 0.0284  153 VAL B N   
2819 C CA  . VAL B 151 ? 0.3258 0.3120 0.3216 -0.0040 -0.0614 0.0355  153 VAL B CA  
2820 C C   . VAL B 151 ? 0.3120 0.2953 0.3053 -0.0014 -0.0555 0.0395  153 VAL B C   
2821 O O   . VAL B 151 ? 0.2940 0.2725 0.2861 -0.0035 -0.0527 0.0345  153 VAL B O   
2822 C CB  . VAL B 151 ? 0.3549 0.3514 0.3465 -0.0073 -0.0666 0.0335  153 VAL B CB  
2823 C CG1 . VAL B 151 ? 0.3609 0.3684 0.3494 -0.0048 -0.0676 0.0414  153 VAL B CG1 
2824 C CG2 . VAL B 151 ? 0.3852 0.3832 0.3783 -0.0111 -0.0717 0.0294  153 VAL B CG2 
2825 N N   . VAL B 152 ? 0.3076 0.2934 0.3006 0.0032  -0.0536 0.0483  154 VAL B N   
2826 C CA  . VAL B 152 ? 0.3216 0.3034 0.3082 0.0053  -0.0492 0.0540  154 VAL B CA  
2827 C C   . VAL B 152 ? 0.3460 0.3379 0.3257 0.0070  -0.0543 0.0612  154 VAL B C   
2828 O O   . VAL B 152 ? 0.3178 0.3180 0.3031 0.0112  -0.0587 0.0666  154 VAL B O   
2829 C CB  . VAL B 152 ? 0.3284 0.2988 0.3185 0.0095  -0.0423 0.0583  154 VAL B CB  
2830 C CG1 . VAL B 152 ? 0.3428 0.3164 0.3412 0.0148  -0.0433 0.0631  154 VAL B CG1 
2831 C CG2 . VAL B 152 ? 0.3372 0.3008 0.3183 0.0109  -0.0376 0.0651  154 VAL B CG2 
2832 N N   . ASN B 153 ? 0.3888 0.3806 0.3565 0.0033  -0.0539 0.0607  155 ASN B N   
2833 C CA  . ASN B 153 ? 0.4214 0.4195 0.3776 0.0043  -0.0591 0.0683  155 ASN B CA  
2834 C C   . ASN B 153 ? 0.4740 0.4599 0.4191 0.0071  -0.0539 0.0774  155 ASN B C   
2835 O O   . ASN B 153 ? 0.4944 0.4703 0.4305 0.0024  -0.0461 0.0745  155 ASN B O   
2836 C CB  . ASN B 153 ? 0.4298 0.4344 0.3760 -0.0027 -0.0621 0.0616  155 ASN B CB  
2837 C CG  . ASN B 153 ? 0.4588 0.4698 0.4141 -0.0068 -0.0651 0.0510  155 ASN B CG  
2838 O OD1 . ASN B 153 ? 0.4514 0.4573 0.4094 -0.0106 -0.0610 0.0417  155 ASN B OD1 
2839 N ND2 . ASN B 153 ? 0.4733 0.4953 0.4342 -0.0061 -0.0726 0.0521  155 ASN B ND2 
2840 N N   . VAL B 154 ? 0.4945 0.4805 0.4415 0.0147  -0.0578 0.0882  156 VAL B N   
2841 C CA  . VAL B 154 ? 0.5365 0.5083 0.4720 0.0185  -0.0544 0.0987  156 VAL B CA  
2842 C C   . VAL B 154 ? 0.5627 0.5367 0.4774 0.0166  -0.0615 0.1056  156 VAL B C   
2843 O O   . VAL B 154 ? 0.5441 0.5319 0.4617 0.0200  -0.0728 0.1092  156 VAL B O   
2844 C CB  . VAL B 154 ? 0.5361 0.5059 0.4854 0.0287  -0.0558 0.1065  156 VAL B CB  
2845 C CG1 . VAL B 154 ? 0.5510 0.5030 0.4890 0.0333  -0.0523 0.1177  156 VAL B CG1 
2846 C CG2 . VAL B 154 ? 0.5481 0.5156 0.5143 0.0286  -0.0487 0.0984  156 VAL B CG2 
2847 N N   . ARG B 155 ? 0.5951 0.5558 0.4890 0.0105  -0.0549 0.1065  157 ARG B N   
2848 C CA  . ARG B 155 ? 0.6476 0.6085 0.5167 0.0057  -0.0602 0.1106  157 ARG B CA  
2849 C C   . ARG B 155 ? 0.7036 0.6429 0.5484 0.0037  -0.0536 0.1199  157 ARG B C   
2850 O O   . ARG B 155 ? 0.7227 0.6480 0.5713 0.0036  -0.0426 0.1197  157 ARG B O   
2851 C CB  . ARG B 155 ? 0.6489 0.6178 0.5131 -0.0047 -0.0572 0.0972  157 ARG B CB  
2852 C CG  . ARG B 155 ? 0.6783 0.6653 0.5615 -0.0043 -0.0639 0.0884  157 ARG B CG  
2853 C CD  . ARG B 155 ? 0.7120 0.7128 0.5924 -0.0014 -0.0782 0.0943  157 ARG B CD  
2854 N NE  . ARG B 155 ? 0.7563 0.7736 0.6526 -0.0033 -0.0835 0.0850  157 ARG B NE  
2855 C CZ  . ARG B 155 ? 0.7768 0.8015 0.6965 0.0014  -0.0847 0.0828  157 ARG B CZ  
2856 N NH1 . ARG B 155 ? 0.7609 0.7789 0.6921 0.0088  -0.0809 0.0885  157 ARG B NH1 
2857 N NH2 . ARG B 155 ? 0.7629 0.8000 0.6932 -0.0020 -0.0889 0.0746  157 ARG B NH2 
2858 N N   . ALA B 156 ? 0.7262 0.6616 0.5446 0.0012  -0.0603 0.1279  158 ALA B N   
2859 C CA  . ALA B 156 ? 0.7703 0.6818 0.5602 -0.0016 -0.0546 0.1384  158 ALA B CA  
2860 C C   . ALA B 156 ? 0.7903 0.6922 0.5662 -0.0149 -0.0382 0.1281  158 ALA B C   
2861 O O   . ALA B 156 ? 0.8042 0.6870 0.5716 -0.0181 -0.0262 0.1308  158 ALA B O   
2862 C CB  . ALA B 156 ? 0.7864 0.6959 0.5497 -0.0002 -0.0688 0.1507  158 ALA B CB  
2863 N N   . LYS B 157 ? 0.7888 0.7044 0.5638 -0.0229 -0.0376 0.1156  159 LYS B N   
2864 C CA  . LYS B 157 ? 0.7954 0.7069 0.5621 -0.0355 -0.0224 0.1026  159 LYS B CA  
2865 C C   . LYS B 157 ? 0.7731 0.6848 0.5669 -0.0359 -0.0100 0.0918  159 LYS B C   
2866 O O   . LYS B 157 ? 0.8045 0.7070 0.5926 -0.0449 0.0049  0.0847  159 LYS B O   
2867 C CB  . LYS B 157 ? 0.8167 0.7451 0.5822 -0.0413 -0.0270 0.0911  159 LYS B CB  
2868 C CG  . LYS B 157 ? 0.8780 0.8054 0.6389 -0.0535 -0.0119 0.0755  159 LYS B CG  
2869 C CD  . LYS B 157 ? 0.9429 0.8844 0.6979 -0.0585 -0.0184 0.0662  159 LYS B CD  
2870 C CE  . LYS B 157 ? 0.9919 0.9430 0.7666 -0.0639 -0.0090 0.0466  159 LYS B CE  
2871 N NZ  . LYS B 157 ? 1.0012 0.9618 0.8130 -0.0557 -0.0115 0.0412  159 LYS B NZ  
2872 N N   . GLY B 158 ? 0.7278 0.6499 0.5503 -0.0272 -0.0159 0.0900  160 GLY B N   
2873 C CA  . GLY B 158 ? 0.6895 0.6124 0.5367 -0.0276 -0.0068 0.0797  160 GLY B CA  
2874 C C   . GLY B 158 ? 0.6453 0.5840 0.5186 -0.0213 -0.0155 0.0737  160 GLY B C   
2875 O O   . GLY B 158 ? 0.6394 0.5916 0.5146 -0.0217 -0.0236 0.0692  160 GLY B O   
2876 N N   . ASP B 159 ? 0.6013 0.5367 0.4931 -0.0165 -0.0131 0.0731  161 ASP B N   
2877 C CA  . ASP B 159 ? 0.5504 0.4968 0.4631 -0.0101 -0.0212 0.0704  161 ASP B CA  
2878 C C   . ASP B 159 ? 0.4973 0.4528 0.4242 -0.0145 -0.0204 0.0555  161 ASP B C   
2879 O O   . ASP B 159 ? 0.4793 0.4316 0.4079 -0.0208 -0.0115 0.0466  161 ASP B O   
2880 C CB  . ASP B 159 ? 0.5570 0.4940 0.4805 -0.0040 -0.0183 0.0754  161 ASP B CB  
2881 C CG  . ASP B 159 ? 0.5853 0.5128 0.4973 0.0024  -0.0208 0.0906  161 ASP B CG  
2882 O OD1 . ASP B 159 ? 0.5718 0.5064 0.4755 0.0056  -0.0303 0.0977  161 ASP B OD1 
2883 O OD2 . ASP B 159 ? 0.6382 0.5511 0.5502 0.0042  -0.0139 0.0950  161 ASP B OD2 
2884 N N   . LYS B 160 ? 0.4661 0.4329 0.4042 -0.0113 -0.0296 0.0526  162 LYS B N   
2885 C CA  . LYS B 160 ? 0.4261 0.3991 0.3777 -0.0141 -0.0309 0.0396  162 LYS B CA  
2886 C C   . LYS B 160 ? 0.3992 0.3718 0.3662 -0.0096 -0.0348 0.0387  162 LYS B C   
2887 O O   . LYS B 160 ? 0.3780 0.3529 0.3462 -0.0046 -0.0398 0.0464  162 LYS B O   
2888 C CB  . LYS B 160 ? 0.4560 0.4394 0.4029 -0.0168 -0.0377 0.0355  162 LYS B CB  
2889 C CG  . LYS B 160 ? 0.5394 0.5226 0.4693 -0.0233 -0.0330 0.0333  162 LYS B CG  
2890 C CD  . LYS B 160 ? 0.6317 0.6247 0.5564 -0.0266 -0.0397 0.0282  162 LYS B CD  
2891 C CE  . LYS B 160 ? 0.7215 0.7186 0.6280 -0.0262 -0.0467 0.0387  162 LYS B CE  
2892 N NZ  . LYS B 160 ? 0.7764 0.7822 0.6751 -0.0315 -0.0521 0.0323  162 LYS B NZ  
2893 N N   . ILE B 161 ? 0.3699 0.3395 0.3492 -0.0114 -0.0325 0.0289  163 ILE B N   
2894 C CA  . ILE B 161 ? 0.3530 0.3206 0.3436 -0.0086 -0.0372 0.0266  163 ILE B CA  
2895 C C   . ILE B 161 ? 0.3401 0.3110 0.3391 -0.0112 -0.0419 0.0153  163 ILE B C   
2896 O O   . ILE B 161 ? 0.3201 0.2916 0.3237 -0.0144 -0.0380 0.0070  163 ILE B O   
2897 C CB  . ILE B 161 ? 0.3704 0.3281 0.3669 -0.0078 -0.0313 0.0266  163 ILE B CB  
2898 C CG1 . ILE B 161 ? 0.3939 0.3454 0.3827 -0.0047 -0.0260 0.0376  163 ILE B CG1 
2899 C CG2 . ILE B 161 ? 0.3784 0.3326 0.3836 -0.0063 -0.0368 0.0227  163 ILE B CG2 
2900 C CD1 . ILE B 161 ? 0.4104 0.3506 0.4039 -0.0052 -0.0186 0.0366  163 ILE B CD1 
2901 N N   . ALA B 162 ? 0.3171 0.2889 0.3185 -0.0099 -0.0499 0.0146  164 ALA B N   
2902 C CA  . ALA B 162 ? 0.3109 0.2834 0.3180 -0.0117 -0.0559 0.0054  164 ALA B CA  
2903 C C   . ALA B 162 ? 0.3167 0.2823 0.3262 -0.0104 -0.0629 0.0052  164 ALA B C   
2904 O O   . ALA B 162 ? 0.3309 0.2961 0.3354 -0.0093 -0.0636 0.0124  164 ALA B O   
2905 C CB  . ALA B 162 ? 0.3029 0.2831 0.3032 -0.0139 -0.0586 0.0046  164 ALA B CB  
2906 N N   . ILE B 163 ? 0.2954 0.2552 0.3127 -0.0106 -0.0679 -0.0029 165 ILE B N   
2907 C CA  . ILE B 163 ? 0.2870 0.2379 0.3019 -0.0106 -0.0766 -0.0034 165 ILE B CA  
2908 C C   . ILE B 163 ? 0.2795 0.2310 0.2931 -0.0121 -0.0826 -0.0077 165 ILE B C   
2909 O O   . ILE B 163 ? 0.2669 0.2202 0.2888 -0.0119 -0.0838 -0.0159 165 ILE B O   
2910 C CB  . ILE B 163 ? 0.2829 0.2239 0.3048 -0.0094 -0.0812 -0.0086 165 ILE B CB  
2911 C CG1 . ILE B 163 ? 0.2940 0.2319 0.3149 -0.0089 -0.0754 -0.0043 165 ILE B CG1 
2912 C CG2 . ILE B 163 ? 0.3023 0.2311 0.3177 -0.0101 -0.0917 -0.0091 165 ILE B CG2 
2913 C CD1 . ILE B 163 ? 0.3079 0.2376 0.3352 -0.0087 -0.0799 -0.0096 165 ILE B CD1 
2914 N N   . TRP B 164 ? 0.2986 0.2482 0.3031 -0.0141 -0.0856 -0.0029 166 TRP B N   
2915 C CA  . TRP B 164 ? 0.3062 0.2545 0.3067 -0.0169 -0.0907 -0.0054 166 TRP B CA  
2916 C C   . TRP B 164 ? 0.3303 0.2619 0.3289 -0.0171 -0.0994 -0.0084 166 TRP B C   
2917 O O   . TRP B 164 ? 0.3251 0.2470 0.3177 -0.0174 -0.1010 -0.0045 166 TRP B O   
2918 C CB  . TRP B 164 ? 0.3172 0.2726 0.3099 -0.0199 -0.0888 0.0013  166 TRP B CB  
2919 C CG  . TRP B 164 ? 0.3345 0.3055 0.3274 -0.0199 -0.0842 0.0039  166 TRP B CG  
2920 C CD1 . TRP B 164 ? 0.3423 0.3192 0.3374 -0.0174 -0.0786 0.0052  166 TRP B CD1 
2921 C CD2 . TRP B 164 ? 0.3461 0.3275 0.3348 -0.0233 -0.0852 0.0059  166 TRP B CD2 
2922 N NE1 . TRP B 164 ? 0.3423 0.3311 0.3327 -0.0185 -0.0770 0.0088  166 TRP B NE1 
2923 C CE2 . TRP B 164 ? 0.3548 0.3478 0.3423 -0.0218 -0.0815 0.0090  166 TRP B CE2 
2924 C CE3 . TRP B 164 ? 0.3636 0.3452 0.3490 -0.0280 -0.0891 0.0053  166 TRP B CE3 
2925 C CZ2 . TRP B 164 ? 0.3657 0.3713 0.3489 -0.0244 -0.0833 0.0113  166 TRP B CZ2 
2926 C CZ3 . TRP B 164 ? 0.3699 0.3657 0.3537 -0.0310 -0.0897 0.0069  166 TRP B CZ3 
2927 C CH2 . TRP B 164 ? 0.3813 0.3894 0.3642 -0.0288 -0.0877 0.0099  166 TRP B CH2 
2928 N N   . THR B 165 ? 0.3455 0.2720 0.3480 -0.0169 -0.1051 -0.0155 167 THR B N   
2929 C CA  . THR B 165 ? 0.3633 0.2717 0.3624 -0.0166 -0.1152 -0.0177 167 THR B CA  
2930 C C   . THR B 165 ? 0.3681 0.2714 0.3605 -0.0204 -0.1183 -0.0192 167 THR B C   
2931 O O   . THR B 165 ? 0.3673 0.2830 0.3608 -0.0228 -0.1133 -0.0209 167 THR B O   
2932 C CB  . THR B 165 ? 0.4008 0.3045 0.4144 -0.0111 -0.1213 -0.0254 167 THR B CB  
2933 O OG1 . THR B 165 ? 0.4084 0.3165 0.4335 -0.0094 -0.1218 -0.0343 167 THR B OG1 
2934 C CG2 . THR B 165 ? 0.4000 0.3129 0.4228 -0.0087 -0.1156 -0.0255 167 THR B CG2 
2935 N N   . THR B 166 ? 0.3740 0.2574 0.3572 -0.0218 -0.1269 -0.0184 168 THR B N   
2936 C CA  . THR B 166 ? 0.4049 0.2792 0.3775 -0.0274 -0.1292 -0.0181 168 THR B CA  
2937 C C   . THR B 166 ? 0.4015 0.2712 0.3813 -0.0259 -0.1336 -0.0266 168 THR B C   
2938 O O   . THR B 166 ? 0.3930 0.2610 0.3661 -0.0315 -0.1325 -0.0276 168 THR B O   
2939 C CB  . THR B 166 ? 0.4692 0.3204 0.4243 -0.0310 -0.1353 -0.0125 168 THR B CB  
2940 O OG1 . THR B 166 ? 0.5158 0.3606 0.4588 -0.0388 -0.1338 -0.0107 168 THR B OG1 
2941 C CG2 . THR B 166 ? 0.4816 0.3115 0.4368 -0.0257 -0.1481 -0.0152 168 THR B CG2 
2942 N N   . GLU B 167 ? 0.3952 0.2629 0.3898 -0.0188 -0.1384 -0.0337 169 GLU B N   
2943 C CA  . GLU B 167 ? 0.4008 0.2597 0.4041 -0.0160 -0.1439 -0.0427 169 GLU B CA  
2944 C C   . GLU B 167 ? 0.4130 0.2854 0.4389 -0.0095 -0.1411 -0.0526 169 GLU B C   
2945 O O   . GLU B 167 ? 0.3979 0.2673 0.4359 -0.0032 -0.1470 -0.0550 169 GLU B O   
2946 C CB  . GLU B 167 ? 0.3760 0.2069 0.3719 -0.0136 -0.1575 -0.0409 169 GLU B CB  
2947 C CG  . GLU B 167 ? 0.4002 0.2174 0.4052 -0.0093 -0.1650 -0.0496 169 GLU B CG  
2948 C CD  . GLU B 167 ? 0.5011 0.3242 0.5049 -0.0148 -0.1575 -0.0549 169 GLU B CD  
2949 O OE1 . GLU B 167 ? 0.5623 0.3757 0.5480 -0.0228 -0.1567 -0.0498 169 GLU B OE1 
2950 O OE2 . GLU B 167 ? 0.5343 0.3723 0.5547 -0.0120 -0.1517 -0.0646 169 GLU B OE2 
2951 N N   . CYS B 168 ? 0.4381 0.3255 0.4697 -0.0118 -0.1320 -0.0591 170 CYS B N   
2952 C CA  . CYS B 168 ? 0.4730 0.3737 0.5249 -0.0074 -0.1265 -0.0693 170 CYS B CA  
2953 C C   . CYS B 168 ? 0.4753 0.3655 0.5460 -0.0002 -0.1344 -0.0800 170 CYS B C   
2954 O O   . CYS B 168 ? 0.4918 0.3931 0.5829 0.0040  -0.1306 -0.0886 170 CYS B O   
2955 C CB  . CYS B 168 ? 0.5141 0.4311 0.5632 -0.0127 -0.1145 -0.0735 170 CYS B CB  
2956 S SG  . CYS B 168 ? 0.6228 0.5315 0.6656 -0.0172 -0.1153 -0.0810 170 CYS B SG  
2957 N N   . GLU B 169 ? 0.4629 0.3316 0.5285 0.0013  -0.1453 -0.0798 171 GLU B N   
2958 C CA  . GLU B 169 ? 0.4470 0.3042 0.5323 0.0098  -0.1548 -0.0895 171 GLU B CA  
2959 C C   . GLU B 169 ? 0.4498 0.2949 0.5410 0.0171  -0.1691 -0.0855 171 GLU B C   
2960 O O   . GLU B 169 ? 0.4444 0.2798 0.5539 0.0256  -0.1797 -0.0929 171 GLU B O   
2961 C CB  . GLU B 169 ? 0.4503 0.2874 0.5276 0.0085  -0.1598 -0.0925 171 GLU B CB  
2962 C CG  . GLU B 169 ? 0.4183 0.2655 0.4892 0.0007  -0.1473 -0.0979 171 GLU B CG  
2963 C CD  . GLU B 169 ? 0.4528 0.3194 0.5432 0.0020  -0.1356 -0.1118 171 GLU B CD  
2964 O OE1 . GLU B 169 ? 0.4448 0.3149 0.5606 0.0103  -0.1373 -0.1214 171 GLU B OE1 
2965 O OE2 . GLU B 169 ? 0.5114 0.3898 0.5912 -0.0060 -0.1246 -0.1136 171 GLU B OE2 
2966 N N   . ASN B 170 ? 0.4549 0.2999 0.5309 0.0140  -0.1703 -0.0743 172 ASN B N   
2967 C CA  . ASN B 170 ? 0.4570 0.2929 0.5366 0.0195  -0.1830 -0.0708 172 ASN B CA  
2968 C C   . ASN B 170 ? 0.4278 0.2861 0.5327 0.0234  -0.1775 -0.0781 172 ASN B C   
2969 O O   . ASN B 170 ? 0.4041 0.2723 0.5033 0.0200  -0.1718 -0.0726 172 ASN B O   
2970 C CB  . ASN B 170 ? 0.4922 0.3175 0.5433 0.0132  -0.1848 -0.0568 172 ASN B CB  
2971 C CG  . ASN B 170 ? 0.5240 0.3212 0.5504 0.0099  -0.1941 -0.0494 172 ASN B CG  
2972 O OD1 . ASN B 170 ? 0.5442 0.3252 0.5738 0.0135  -0.2026 -0.0534 172 ASN B OD1 
2973 N ND2 . ASN B 170 ? 0.5085 0.2984 0.5097 0.0025  -0.1918 -0.0386 172 ASN B ND2 
2974 N N   . ARG B 171 ? 0.4275 0.2935 0.5620 0.0303  -0.1787 -0.0916 173 ARG B N   
2975 C CA  . ARG B 171 ? 0.4353 0.3245 0.5959 0.0323  -0.1703 -0.1008 173 ARG B CA  
2976 C C   . ARG B 171 ? 0.4257 0.3149 0.5904 0.0347  -0.1793 -0.0967 173 ARG B C   
2977 O O   . ARG B 171 ? 0.4040 0.3088 0.5710 0.0307  -0.1689 -0.0960 173 ARG B O   
2978 C CB  . ARG B 171 ? 0.4637 0.3602 0.6576 0.0392  -0.1702 -0.1174 173 ARG B CB  
2979 C CG  . ARG B 171 ? 0.4853 0.4064 0.7109 0.0408  -0.1604 -0.1297 173 ARG B CG  
2980 C CD  . ARG B 171 ? 0.5493 0.4712 0.7987 0.0486  -0.1753 -0.1333 173 ARG B CD  
2981 N NE  . ARG B 171 ? 0.5993 0.5050 0.8627 0.0589  -0.1942 -0.1377 173 ARG B NE  
2982 C CZ  . ARG B 171 ? 0.6439 0.5406 0.9182 0.0667  -0.2144 -0.1366 173 ARG B CZ  
2983 N NH1 . ARG B 171 ? 0.6503 0.5534 0.9233 0.0646  -0.2180 -0.1321 173 ARG B NH1 
2984 N NH2 . ARG B 171 ? 0.6561 0.5359 0.9418 0.0766  -0.2319 -0.1400 173 ARG B NH2 
2985 N N   . GLU B 172 ? 0.4358 0.3060 0.5995 0.0407  -0.1990 -0.0939 174 GLU B N   
2986 C CA  . GLU B 172 ? 0.4344 0.3033 0.6016 0.0429  -0.2102 -0.0912 174 GLU B CA  
2987 C C   . GLU B 172 ? 0.4232 0.2906 0.5612 0.0342  -0.2030 -0.0786 174 GLU B C   
2988 O O   . GLU B 172 ? 0.3936 0.2715 0.5386 0.0329  -0.2008 -0.0793 174 GLU B O   
2989 C CB  . GLU B 172 ? 0.4896 0.3341 0.6547 0.0504  -0.2342 -0.0890 174 GLU B CB  
2990 C CG  . GLU B 172 ? 0.6951 0.5360 0.8628 0.0531  -0.2492 -0.0868 174 GLU B CG  
2991 C CD  . GLU B 172 ? 0.9267 0.7846 1.1369 0.0617  -0.2575 -0.1006 174 GLU B CD  
2992 O OE1 . GLU B 172 ? 0.9772 0.8247 1.1902 0.0667  -0.2780 -0.0994 174 GLU B OE1 
2993 O OE2 . GLU B 172 ? 0.9884 0.8702 1.2289 0.0628  -0.2436 -0.1130 174 GLU B OE2 
2994 N N   . ALA B 173 ? 0.4313 0.2860 0.5384 0.0280  -0.1987 -0.0682 175 ALA B N   
2995 C CA  . ALA B 173 ? 0.4306 0.2847 0.5123 0.0202  -0.1905 -0.0572 175 ALA B CA  
2996 C C   . ALA B 173 ? 0.3997 0.2780 0.4899 0.0163  -0.1713 -0.0594 175 ALA B C   
2997 O O   . ALA B 173 ? 0.3749 0.2598 0.4623 0.0136  -0.1657 -0.0561 175 ALA B O   
2998 C CB  . ALA B 173 ? 0.4377 0.2743 0.4891 0.0146  -0.1902 -0.0474 175 ALA B CB  
2999 N N   . VAL B 174 ? 0.3927 0.2821 0.4917 0.0159  -0.1616 -0.0649 176 VAL B N   
3000 C CA  . VAL B 174 ? 0.3849 0.2930 0.4856 0.0115  -0.1443 -0.0657 176 VAL B CA  
3001 C C   . VAL B 174 ? 0.3797 0.3031 0.5030 0.0130  -0.1388 -0.0732 176 VAL B C   
3002 O O   . VAL B 174 ? 0.3808 0.3123 0.4981 0.0090  -0.1285 -0.0686 176 VAL B O   
3003 C CB  . VAL B 174 ? 0.3738 0.2870 0.4760 0.0102  -0.1373 -0.0709 176 VAL B CB  
3004 C CG1 . VAL B 174 ? 0.3751 0.3078 0.4832 0.0065  -0.1208 -0.0748 176 VAL B CG1 
3005 C CG2 . VAL B 174 ? 0.3799 0.2814 0.4569 0.0057  -0.1389 -0.0619 176 VAL B CG2 
3006 N N   . THR B 175 ? 0.3693 0.2966 0.5192 0.0187  -0.1451 -0.0850 177 THR B N   
3007 C CA  . THR B 175 ? 0.3690 0.3133 0.5446 0.0191  -0.1381 -0.0946 177 THR B CA  
3008 C C   . THR B 175 ? 0.3776 0.3186 0.5508 0.0186  -0.1446 -0.0898 177 THR B C   
3009 O O   . THR B 175 ? 0.3833 0.3362 0.5632 0.0147  -0.1337 -0.0915 177 THR B O   
3010 C CB  . THR B 175 ? 0.4039 0.3559 0.6126 0.0253  -0.1416 -0.1103 177 THR B CB  
3011 O OG1 . THR B 175 ? 0.4470 0.3852 0.6637 0.0331  -0.1624 -0.1116 177 THR B OG1 
3012 C CG2 . THR B 175 ? 0.4004 0.3549 0.6080 0.0243  -0.1326 -0.1155 177 THR B CG2 
3013 N N   . HIS B 176 ? 0.3912 0.3147 0.5526 0.0214  -0.1615 -0.0839 178 HIS B N   
3014 C CA  . HIS B 176 ? 0.4040 0.3219 0.5579 0.0197  -0.1677 -0.0791 178 HIS B CA  
3015 C C   . HIS B 176 ? 0.3886 0.3069 0.5191 0.0125  -0.1538 -0.0689 178 HIS B C   
3016 O O   . HIS B 176 ? 0.3834 0.3081 0.5180 0.0096  -0.1478 -0.0695 178 HIS B O   
3017 C CB  . HIS B 176 ? 0.4627 0.3580 0.6012 0.0229  -0.1884 -0.0735 178 HIS B CB  
3018 C CG  . HIS B 176 ? 0.5645 0.4508 0.6880 0.0196  -0.1945 -0.0678 178 HIS B CG  
3019 N ND1 . HIS B 176 ? 0.6282 0.5007 0.7181 0.0137  -0.1902 -0.0559 178 HIS B ND1 
3020 C CD2 . HIS B 176 ? 0.5889 0.4785 0.7261 0.0206  -0.2031 -0.0731 178 HIS B CD2 
3021 C CE1 . HIS B 176 ? 0.6557 0.5220 0.7381 0.0113  -0.1959 -0.0544 178 HIS B CE1 
3022 N NE2 . HIS B 176 ? 0.6326 0.5083 0.7413 0.0149  -0.2043 -0.0641 178 HIS B NE2 
3023 N N   . ILE B 177 ? 0.3819 0.2935 0.4891 0.0098  -0.1484 -0.0599 179 ILE B N   
3024 C CA  . ILE B 177 ? 0.3735 0.2880 0.4628 0.0043  -0.1346 -0.0510 179 ILE B CA  
3025 C C   . ILE B 177 ? 0.3695 0.3018 0.4731 0.0022  -0.1190 -0.0554 179 ILE B C   
3026 O O   . ILE B 177 ? 0.3925 0.3264 0.4913 -0.0009 -0.1114 -0.0516 179 ILE B O   
3027 C CB  . ILE B 177 ? 0.3602 0.2700 0.4290 0.0019  -0.1306 -0.0430 179 ILE B CB  
3028 C CG1 . ILE B 177 ? 0.3540 0.2437 0.4023 0.0012  -0.1423 -0.0364 179 ILE B CG1 
3029 C CG2 . ILE B 177 ? 0.3475 0.2656 0.4052 -0.0022 -0.1157 -0.0355 179 ILE B CG2 
3030 C CD1 . ILE B 177 ? 0.3666 0.2513 0.4022 -0.0007 -0.1419 -0.0326 179 ILE B CD1 
3031 N N   . GLY B 178 ? 0.3385 0.2817 0.4574 0.0033  -0.1141 -0.0634 180 GLY B N   
3032 C CA  . GLY B 178 ? 0.3374 0.2953 0.4658 0.0000  -0.0982 -0.0677 180 GLY B CA  
3033 C C   . GLY B 178 ? 0.3369 0.3013 0.4838 -0.0010 -0.0958 -0.0744 180 GLY B C   
3034 O O   . GLY B 178 ? 0.3315 0.3007 0.4754 -0.0055 -0.0830 -0.0720 180 GLY B O   
3035 N N   . ARG B 179 ? 0.3495 0.3134 0.5157 0.0030  -0.1085 -0.0827 181 ARG B N   
3036 C CA  . ARG B 179 ? 0.3519 0.3241 0.5410 0.0021  -0.1087 -0.0916 181 ARG B CA  
3037 C C   . ARG B 179 ? 0.3563 0.3203 0.5306 -0.0015 -0.1088 -0.0838 181 ARG B C   
3038 O O   . ARG B 179 ? 0.3420 0.3129 0.5241 -0.0062 -0.0982 -0.0867 181 ARG B O   
3039 C CB  . ARG B 179 ? 0.3758 0.3477 0.5877 0.0088  -0.1269 -0.1010 181 ARG B CB  
3040 C CG  . ARG B 179 ? 0.4895 0.4768 0.7359 0.0088  -0.1264 -0.1151 181 ARG B CG  
3041 C CD  . ARG B 179 ? 0.5395 0.5424 0.8102 0.0095  -0.1156 -0.1273 181 ARG B CD  
3042 N NE  . ARG B 179 ? 0.5850 0.5839 0.8646 0.0174  -0.1280 -0.1316 181 ARG B NE  
3043 C CZ  . ARG B 179 ? 0.6010 0.6113 0.9036 0.0197  -0.1217 -0.1439 181 ARG B CZ  
3044 N NH1 . ARG B 179 ? 0.5620 0.5894 0.8810 0.0137  -0.1023 -0.1536 181 ARG B NH1 
3045 N NH2 . ARG B 179 ? 0.6017 0.6050 0.9104 0.0274  -0.1337 -0.1469 181 ARG B NH2 
3046 N N   . VAL B 180 ? 0.3694 0.3173 0.5219 0.0001  -0.1204 -0.0747 182 VAL B N   
3047 C CA  . VAL B 180 ? 0.3805 0.3179 0.5152 -0.0034 -0.1205 -0.0673 182 VAL B CA  
3048 C C   . VAL B 180 ? 0.3709 0.3093 0.4897 -0.0076 -0.1029 -0.0587 182 VAL B C   
3049 O O   . VAL B 180 ? 0.3826 0.3201 0.4995 -0.0114 -0.0951 -0.0575 182 VAL B O   
3050 C CB  . VAL B 180 ? 0.4193 0.3384 0.5323 -0.0015 -0.1357 -0.0602 182 VAL B CB  
3051 C CG1 . VAL B 180 ? 0.4484 0.3556 0.5395 -0.0058 -0.1332 -0.0526 182 VAL B CG1 
3052 C CG2 . VAL B 180 ? 0.4363 0.3519 0.5641 0.0032  -0.1555 -0.0679 182 VAL B CG2 
3053 N N   . TYR B 181 ? 0.3450 0.2845 0.4526 -0.0068 -0.0972 -0.0530 183 TYR B N   
3054 C CA  . TYR B 181 ? 0.3567 0.2981 0.4508 -0.0096 -0.0822 -0.0446 183 TYR B CA  
3055 C C   . TYR B 181 ? 0.3787 0.3300 0.4852 -0.0132 -0.0683 -0.0493 183 TYR B C   
3056 O O   . TYR B 181 ? 0.4073 0.3549 0.5053 -0.0160 -0.0588 -0.0436 183 TYR B O   
3057 C CB  . TYR B 181 ? 0.3368 0.2800 0.4198 -0.0083 -0.0810 -0.0394 183 TYR B CB  
3058 C CG  . TYR B 181 ? 0.3228 0.2677 0.3906 -0.0099 -0.0695 -0.0296 183 TYR B CG  
3059 C CD1 . TYR B 181 ? 0.3281 0.2663 0.3848 -0.0108 -0.0648 -0.0217 183 TYR B CD1 
3060 C CD2 . TYR B 181 ? 0.3218 0.2742 0.3858 -0.0103 -0.0644 -0.0283 183 TYR B CD2 
3061 C CE1 . TYR B 181 ? 0.3207 0.2604 0.3658 -0.0109 -0.0558 -0.0126 183 TYR B CE1 
3062 C CE2 . TYR B 181 ? 0.3112 0.2651 0.3614 -0.0112 -0.0564 -0.0190 183 TYR B CE2 
3063 C CZ  . TYR B 181 ? 0.3263 0.2741 0.3681 -0.0109 -0.0526 -0.0109 183 TYR B CZ  
3064 O OH  . TYR B 181 ? 0.3514 0.3009 0.3815 -0.0103 -0.0465 -0.0013 183 TYR B OH  
3065 N N   . LYS B 182 ? 0.3736 0.3362 0.4996 -0.0135 -0.0660 -0.0597 184 LYS B N   
3066 C CA  . LYS B 182 ? 0.4011 0.3725 0.5384 -0.0185 -0.0513 -0.0653 184 LYS B CA  
3067 C C   . LYS B 182 ? 0.4331 0.4026 0.5807 -0.0217 -0.0506 -0.0693 184 LYS B C   
3068 O O   . LYS B 182 ? 0.4566 0.4247 0.6002 -0.0268 -0.0373 -0.0669 184 LYS B O   
3069 C CB  . LYS B 182 ? 0.4189 0.4034 0.5782 -0.0185 -0.0492 -0.0784 184 LYS B CB  
3070 C CG  . LYS B 182 ? 0.4456 0.4390 0.6167 -0.0253 -0.0324 -0.0857 184 LYS B CG  
3071 C CD  . LYS B 182 ? 0.4908 0.4981 0.6897 -0.0252 -0.0313 -0.1015 184 LYS B CD  
3072 C CE  . LYS B 182 ? 0.5224 0.5378 0.7279 -0.0336 -0.0114 -0.1084 184 LYS B CE  
3073 N NZ  . LYS B 182 ? 0.5373 0.5667 0.7676 -0.0338 -0.0072 -0.1242 184 LYS B NZ  
3074 N N   . GLU B 183 ? 0.4228 0.3907 0.5820 -0.0189 -0.0656 -0.0750 185 GLU B N   
3075 C CA  . GLU B 183 ? 0.4180 0.3833 0.5856 -0.0220 -0.0687 -0.0793 185 GLU B CA  
3076 C C   . GLU B 183 ? 0.4217 0.3728 0.5646 -0.0247 -0.0624 -0.0678 185 GLU B C   
3077 O O   . GLU B 183 ? 0.3974 0.3468 0.5427 -0.0300 -0.0525 -0.0691 185 GLU B O   
3078 C CB  . GLU B 183 ? 0.4659 0.4288 0.6426 -0.0173 -0.0896 -0.0845 185 GLU B CB  
3079 C CG  . GLU B 183 ? 0.5715 0.5343 0.7613 -0.0199 -0.0979 -0.0919 185 GLU B CG  
3080 C CD  . GLU B 183 ? 0.6779 0.6296 0.8594 -0.0152 -0.1197 -0.0903 185 GLU B CD  
3081 O OE1 . GLU B 183 ? 0.6785 0.6163 0.8402 -0.0179 -0.1237 -0.0847 185 GLU B OE1 
3082 O OE2 . GLU B 183 ? 0.7256 0.6805 0.9185 -0.0092 -0.1324 -0.0944 185 GLU B OE2 
3083 N N   . ARG B 184 ? 0.4198 0.3606 0.5403 -0.0212 -0.0675 -0.0572 186 ARG B N   
3084 C CA  . ARG B 184 ? 0.4147 0.3426 0.5140 -0.0224 -0.0624 -0.0473 186 ARG B CA  
3085 C C   . ARG B 184 ? 0.4408 0.3691 0.5324 -0.0242 -0.0457 -0.0403 186 ARG B C   
3086 O O   . ARG B 184 ? 0.4499 0.3691 0.5325 -0.0263 -0.0382 -0.0355 186 ARG B O   
3087 C CB  . ARG B 184 ? 0.4179 0.3365 0.4979 -0.0188 -0.0717 -0.0394 186 ARG B CB  
3088 C CG  . ARG B 184 ? 0.4052 0.3164 0.4847 -0.0180 -0.0887 -0.0439 186 ARG B CG  
3089 C CD  . ARG B 184 ? 0.4278 0.3276 0.4988 -0.0219 -0.0895 -0.0443 186 ARG B CD  
3090 N NE  . ARG B 184 ? 0.4250 0.3131 0.4729 -0.0226 -0.0827 -0.0345 186 ARG B NE  
3091 C CZ  . ARG B 184 ? 0.4500 0.3250 0.4785 -0.0231 -0.0899 -0.0307 186 ARG B CZ  
3092 N NH1 . ARG B 184 ? 0.4595 0.3284 0.4850 -0.0230 -0.1062 -0.0343 186 ARG B NH1 
3093 N NH2 . ARG B 184 ? 0.4598 0.3269 0.4717 -0.0239 -0.0807 -0.0233 186 ARG B NH2 
3094 N N   . LEU B 185 ? 0.4550 0.3922 0.5487 -0.0234 -0.0400 -0.0395 187 LEU B N   
3095 C CA  . LEU B 185 ? 0.4815 0.4184 0.5678 -0.0259 -0.0250 -0.0337 187 LEU B CA  
3096 C C   . LEU B 185 ? 0.5304 0.4690 0.6294 -0.0325 -0.0138 -0.0410 187 LEU B C   
3097 O O   . LEU B 185 ? 0.5430 0.4761 0.6322 -0.0354 -0.0011 -0.0348 187 LEU B O   
3098 C CB  . LEU B 185 ? 0.4719 0.4167 0.5533 -0.0243 -0.0231 -0.0312 187 LEU B CB  
3099 C CG  . LEU B 185 ? 0.4901 0.4325 0.5558 -0.0192 -0.0305 -0.0218 187 LEU B CG  
3100 C CD1 . LEU B 185 ? 0.4974 0.4471 0.5570 -0.0190 -0.0273 -0.0196 187 LEU B CD1 
3101 C CD2 . LEU B 185 ? 0.4894 0.4221 0.5396 -0.0174 -0.0266 -0.0102 187 LEU B CD2 
3102 N N   . GLY B 186 ? 0.5529 0.4985 0.6736 -0.0350 -0.0188 -0.0537 188 GLY B N   
3103 C CA  . GLY B 186 ? 0.5784 0.5292 0.7161 -0.0424 -0.0083 -0.0633 188 GLY B CA  
3104 C C   . GLY B 186 ? 0.6251 0.5834 0.7653 -0.0464 0.0053  -0.0656 188 GLY B C   
3105 O O   . GLY B 186 ? 0.6347 0.5912 0.7775 -0.0539 0.0196  -0.0681 188 GLY B O   
3106 N N   . LEU B 187 ? 0.6543 0.6197 0.7922 -0.0425 0.0017  -0.0652 189 LEU B N   
3107 C CA  . LEU B 187 ? 0.6753 0.6486 0.8160 -0.0470 0.0140  -0.0700 189 LEU B CA  
3108 C C   . LEU B 187 ? 0.6972 0.6849 0.8703 -0.0516 0.0169  -0.0879 189 LEU B C   
3109 O O   . LEU B 187 ? 0.6921 0.6872 0.8860 -0.0472 0.0029  -0.0964 189 LEU B O   
3110 C CB  . LEU B 187 ? 0.6698 0.6477 0.8023 -0.0419 0.0079  -0.0674 189 LEU B CB  
3111 C CG  . LEU B 187 ? 0.6890 0.6569 0.7933 -0.0373 0.0042  -0.0513 189 LEU B CG  
3112 C CD1 . LEU B 187 ? 0.6897 0.6638 0.7898 -0.0336 -0.0023 -0.0517 189 LEU B CD1 
3113 C CD2 . LEU B 187 ? 0.6949 0.6532 0.7781 -0.0416 0.0178  -0.0408 189 LEU B CD2 
3114 N N   . PRO B 188 ? 0.7128 0.7044 0.8910 -0.0606 0.0347  -0.0941 190 PRO B N   
3115 C CA  . PRO B 188 ? 0.7062 0.7147 0.9193 -0.0652 0.0386  -0.1131 190 PRO B CA  
3116 C C   . PRO B 188 ? 0.7163 0.7384 0.9455 -0.0596 0.0315  -0.1225 190 PRO B C   
3117 O O   . PRO B 188 ? 0.7273 0.7456 0.9368 -0.0563 0.0309  -0.1153 190 PRO B O   
3118 C CB  . PRO B 188 ? 0.7182 0.7250 0.9266 -0.0773 0.0620  -0.1158 190 PRO B CB  
3119 C CG  . PRO B 188 ? 0.7433 0.7309 0.9127 -0.0783 0.0685  -0.0974 190 PRO B CG  
3120 C CD  . PRO B 188 ? 0.7262 0.7064 0.8783 -0.0672 0.0516  -0.0843 190 PRO B CD  
3121 N N   . PRO B 189 ? 0.7079 0.7462 0.9746 -0.0584 0.0258  -0.1393 191 PRO B N   
3122 C CA  . PRO B 189 ? 0.7003 0.7498 0.9846 -0.0513 0.0171  -0.1486 191 PRO B CA  
3123 C C   . PRO B 189 ? 0.6978 0.7525 0.9776 -0.0560 0.0335  -0.1539 191 PRO B C   
3124 O O   . PRO B 189 ? 0.6847 0.7445 0.9713 -0.0500 0.0270  -0.1589 191 PRO B O   
3125 C CB  . PRO B 189 ? 0.6874 0.7531 1.0155 -0.0492 0.0079  -0.1658 191 PRO B CB  
3126 C CG  . PRO B 189 ? 0.6917 0.7588 1.0279 -0.0586 0.0179  -0.1691 191 PRO B CG  
3127 C CD  . PRO B 189 ? 0.6942 0.7413 0.9901 -0.0631 0.0262  -0.1510 191 PRO B CD  
3128 N N   . LYS B 190 ? 0.7114 0.7630 0.9778 -0.0675 0.0552  -0.1528 192 LYS B N   
3129 C CA  . LYS B 190 ? 0.7206 0.7733 0.9743 -0.0752 0.0740  -0.1564 192 LYS B CA  
3130 C C   . LYS B 190 ? 0.7322 0.7706 0.9452 -0.0721 0.0708  -0.1395 192 LYS B C   
3131 O O   . LYS B 190 ? 0.7448 0.7856 0.9491 -0.0741 0.0777  -0.1434 192 LYS B O   
3132 C CB  . LYS B 190 ? 0.7571 0.8051 1.0017 -0.0894 0.0969  -0.1570 192 LYS B CB  
3133 C CG  . LYS B 190 ? 0.8009 0.8610 1.0813 -0.0961 0.1040  -0.1719 192 LYS B CG  
3134 C CD  . LYS B 190 ? 0.8633 0.9095 1.1217 -0.1095 0.1237  -0.1650 192 LYS B CD  
3135 C CE  . LYS B 190 ? 0.8735 0.9297 1.1643 -0.1181 0.1319  -0.1787 192 LYS B CE  
3136 N NZ  . LYS B 190 ? 0.8804 0.9494 1.1901 -0.1309 0.1551  -0.1964 192 LYS B NZ  
3137 N N   . ILE B 191 ? 0.7242 0.7481 0.9126 -0.0678 0.0610  -0.1216 193 ILE B N   
3138 C CA  . ILE B 191 ? 0.7191 0.7313 0.8726 -0.0638 0.0554  -0.1054 193 ILE B CA  
3139 C C   . ILE B 191 ? 0.6847 0.7023 0.8486 -0.0537 0.0375  -0.1080 193 ILE B C   
3140 O O   . ILE B 191 ? 0.6877 0.7044 0.8626 -0.0468 0.0226  -0.1063 193 ILE B O   
3141 C CB  . ILE B 191 ? 0.7385 0.7352 0.8688 -0.0623 0.0519  -0.0877 193 ILE B CB  
3142 C CG1 . ILE B 191 ? 0.7575 0.7455 0.8770 -0.0728 0.0703  -0.0850 193 ILE B CG1 
3143 C CG2 . ILE B 191 ? 0.7555 0.7433 0.8557 -0.0568 0.0437  -0.0719 193 ILE B CG2 
3144 C CD1 . ILE B 191 ? 0.7855 0.7701 0.8841 -0.0823 0.0878  -0.0850 193 ILE B CD1 
3145 N N   . VAL B 192 ? 0.6557 0.6772 0.8146 -0.0534 0.0391  -0.1123 194 VAL B N   
3146 C CA  . VAL B 192 ? 0.6242 0.6488 0.7924 -0.0445 0.0232  -0.1155 194 VAL B CA  
3147 C C   . VAL B 192 ? 0.5932 0.6074 0.7303 -0.0408 0.0142  -0.0992 194 VAL B C   
3148 O O   . VAL B 192 ? 0.6027 0.6125 0.7138 -0.0457 0.0228  -0.0919 194 VAL B O   
3149 C CB  . VAL B 192 ? 0.6303 0.6658 0.8168 -0.0458 0.0295  -0.1325 194 VAL B CB  
3150 C CG1 . VAL B 192 ? 0.6143 0.6629 0.8349 -0.0503 0.0406  -0.1500 194 VAL B CG1 
3151 C CG2 . VAL B 192 ? 0.6581 0.6901 0.8160 -0.0525 0.0415  -0.1294 194 VAL B CG2 
3152 N N   . ILE B 193 ? 0.5538 0.5637 0.6930 -0.0326 -0.0032 -0.0937 195 ILE B N   
3153 C CA  . ILE B 193 ? 0.5213 0.5233 0.6352 -0.0295 -0.0117 -0.0803 195 ILE B CA  
3154 C C   . ILE B 193 ? 0.4876 0.4919 0.6064 -0.0260 -0.0195 -0.0870 195 ILE B C   
3155 O O   . ILE B 193 ? 0.4664 0.4756 0.6104 -0.0229 -0.0237 -0.0999 195 ILE B O   
3156 C CB  . ILE B 193 ? 0.5132 0.5063 0.6189 -0.0250 -0.0223 -0.0679 195 ILE B CB  
3157 C CG1 . ILE B 193 ? 0.5007 0.4925 0.6257 -0.0191 -0.0367 -0.0735 195 ILE B CG1 
3158 C CG2 . ILE B 193 ? 0.5289 0.5183 0.6288 -0.0289 -0.0128 -0.0619 195 ILE B CG2 
3159 C CD1 . ILE B 193 ? 0.5138 0.4953 0.6266 -0.0155 -0.0474 -0.0622 195 ILE B CD1 
3160 N N   . GLY B 194 ? 0.4708 0.4713 0.5663 -0.0266 -0.0218 -0.0785 196 GLY B N   
3161 C CA  . GLY B 194 ? 0.4516 0.4529 0.5474 -0.0251 -0.0270 -0.0845 196 GLY B CA  
3162 C C   . GLY B 194 ? 0.4485 0.4422 0.5318 -0.0210 -0.0409 -0.0745 196 GLY B C   
3163 O O   . GLY B 194 ? 0.4556 0.4459 0.5214 -0.0213 -0.0426 -0.0611 196 GLY B O   
3164 N N   . TYR B 195 ? 0.4334 0.4240 0.5264 -0.0172 -0.0504 -0.0812 197 TYR B N   
3165 C CA  . TYR B 195 ? 0.4086 0.3905 0.4898 -0.0147 -0.0626 -0.0734 197 TYR B CA  
3166 C C   . TYR B 195 ? 0.3944 0.3778 0.4642 -0.0184 -0.0603 -0.0764 197 TYR B C   
3167 O O   . TYR B 195 ? 0.3900 0.3757 0.4718 -0.0187 -0.0569 -0.0892 197 TYR B O   
3168 C CB  . TYR B 195 ? 0.3876 0.3608 0.4842 -0.0085 -0.0759 -0.0777 197 TYR B CB  
3169 C CG  . TYR B 195 ? 0.3919 0.3534 0.4733 -0.0076 -0.0870 -0.0694 197 TYR B CG  
3170 C CD1 . TYR B 195 ? 0.3980 0.3527 0.4682 -0.0071 -0.0925 -0.0580 197 TYR B CD1 
3171 C CD2 . TYR B 195 ? 0.3874 0.3440 0.4658 -0.0082 -0.0909 -0.0738 197 TYR B CD2 
3172 C CE1 . TYR B 195 ? 0.4137 0.3575 0.4697 -0.0078 -0.1007 -0.0511 197 TYR B CE1 
3173 C CE2 . TYR B 195 ? 0.3960 0.3414 0.4598 -0.0090 -0.0996 -0.0665 197 TYR B CE2 
3174 C CZ  . TYR B 195 ? 0.4002 0.3394 0.4530 -0.0090 -0.1043 -0.0552 197 TYR B CZ  
3175 O OH  . TYR B 195 ? 0.3890 0.3167 0.4273 -0.0112 -0.1112 -0.0488 197 TYR B OH  
3176 N N   . GLN B 196 ? 0.3867 0.3697 0.4351 -0.0214 -0.0619 -0.0656 198 GLN B N   
3177 C CA  . GLN B 196 ? 0.3937 0.3790 0.4283 -0.0262 -0.0605 -0.0672 198 GLN B CA  
3178 C C   . GLN B 196 ? 0.4083 0.3865 0.4360 -0.0256 -0.0715 -0.0623 198 GLN B C   
3179 O O   . GLN B 196 ? 0.4109 0.3877 0.4306 -0.0249 -0.0759 -0.0510 198 GLN B O   
3180 C CB  . GLN B 196 ? 0.3964 0.3890 0.4111 -0.0311 -0.0536 -0.0585 198 GLN B CB  
3181 C CG  . GLN B 196 ? 0.4862 0.4831 0.5014 -0.0332 -0.0417 -0.0600 198 GLN B CG  
3182 C CD  . GLN B 196 ? 0.5918 0.5916 0.5850 -0.0365 -0.0381 -0.0476 198 GLN B CD  
3183 O OE1 . GLN B 196 ? 0.6304 0.6293 0.6177 -0.0336 -0.0436 -0.0354 198 GLN B OE1 
3184 N NE2 . GLN B 196 ? 0.6184 0.6208 0.5986 -0.0426 -0.0287 -0.0507 198 GLN B NE2 
3185 N N   . SER B 197 ? 0.4263 0.3994 0.4570 -0.0265 -0.0748 -0.0712 199 SER B N   
3186 C CA  . SER B 197 ? 0.4379 0.4040 0.4587 -0.0287 -0.0830 -0.0676 199 SER B CA  
3187 C C   . SER B 197 ? 0.4157 0.3913 0.4180 -0.0343 -0.0813 -0.0581 199 SER B C   
3188 O O   . SER B 197 ? 0.4345 0.4199 0.4287 -0.0378 -0.0742 -0.0586 199 SER B O   
3189 C CB  . SER B 197 ? 0.4947 0.4545 0.5208 -0.0299 -0.0839 -0.0804 199 SER B CB  
3190 O OG  . SER B 197 ? 0.5838 0.5364 0.5991 -0.0339 -0.0902 -0.0781 199 SER B OG  
3191 N N   . HIS B 198 ? 0.4032 0.3760 0.3991 -0.0352 -0.0876 -0.0497 200 HIS B N   
3192 C CA  . HIS B 198 ? 0.4352 0.4186 0.4180 -0.0399 -0.0878 -0.0416 200 HIS B CA  
3193 C C   . HIS B 198 ? 0.4675 0.4552 0.4418 -0.0466 -0.0873 -0.0488 200 HIS B C   
3194 O O   . HIS B 198 ? 0.4770 0.4765 0.4405 -0.0504 -0.0857 -0.0452 200 HIS B O   
3195 C CB  . HIS B 198 ? 0.4275 0.4070 0.4084 -0.0403 -0.0938 -0.0335 200 HIS B CB  
3196 C CG  . HIS B 198 ? 0.4324 0.4100 0.4171 -0.0354 -0.0934 -0.0251 200 HIS B CG  
3197 N ND1 . HIS B 198 ? 0.4407 0.4261 0.4261 -0.0321 -0.0882 -0.0198 200 HIS B ND1 
3198 C CD2 . HIS B 198 ? 0.4398 0.4059 0.4260 -0.0339 -0.0974 -0.0218 200 HIS B CD2 
3199 C CE1 . HIS B 198 ? 0.4471 0.4266 0.4360 -0.0286 -0.0891 -0.0142 200 HIS B CE1 
3200 N NE2 . HIS B 198 ? 0.4378 0.4060 0.4264 -0.0298 -0.0944 -0.0152 200 HIS B NE2 
3201 N N   . ALA B 199 ? 0.4938 0.4709 0.4726 -0.0478 -0.0892 -0.0591 201 ALA B N   
3202 C CA  . ALA B 199 ? 0.5150 0.4936 0.4861 -0.0547 -0.0880 -0.0683 201 ALA B CA  
3203 C C   . ALA B 199 ? 0.5380 0.5256 0.5033 -0.0571 -0.0794 -0.0743 201 ALA B C   
3204 O O   . ALA B 199 ? 0.5359 0.5303 0.4875 -0.0642 -0.0784 -0.0769 201 ALA B O   
3205 C CB  . ALA B 199 ? 0.5180 0.4806 0.4974 -0.0539 -0.0909 -0.0784 201 ALA B CB  
3206 N N   . ASP B 200 ? 0.5429 0.5303 0.5173 -0.0523 -0.0730 -0.0770 202 ASP B N   
3207 C CA  . ASP B 200 ? 0.5566 0.5511 0.5235 -0.0557 -0.0629 -0.0819 202 ASP B CA  
3208 C C   . ASP B 200 ? 0.5885 0.5928 0.5399 -0.0572 -0.0623 -0.0686 202 ASP B C   
3209 O O   . ASP B 200 ? 0.5931 0.6033 0.5267 -0.0635 -0.0590 -0.0689 202 ASP B O   
3210 C CB  . ASP B 200 ? 0.5543 0.5456 0.5392 -0.0508 -0.0554 -0.0905 202 ASP B CB  
3211 C CG  . ASP B 200 ? 0.5963 0.5780 0.5990 -0.0478 -0.0570 -0.1043 202 ASP B CG  
3212 O OD1 . ASP B 200 ? 0.6289 0.6056 0.6257 -0.0517 -0.0603 -0.1097 202 ASP B OD1 
3213 O OD2 . ASP B 200 ? 0.5805 0.5594 0.6040 -0.0414 -0.0554 -0.1099 202 ASP B OD2 
3214 N N   . THR B 201 ? 0.6013 0.6062 0.5586 -0.0515 -0.0659 -0.0569 203 THR B N   
3215 C CA  . THR B 201 ? 0.6229 0.6354 0.5685 -0.0511 -0.0661 -0.0436 203 THR B CA  
3216 C C   . THR B 201 ? 0.6372 0.6580 0.5688 -0.0556 -0.0734 -0.0377 203 THR B C   
3217 O O   . THR B 201 ? 0.6429 0.6704 0.5607 -0.0568 -0.0736 -0.0296 203 THR B O   
3218 C CB  . THR B 201 ? 0.6536 0.6637 0.6102 -0.0441 -0.0685 -0.0342 203 THR B CB  
3219 O OG1 . THR B 201 ? 0.6820 0.6853 0.6526 -0.0405 -0.0632 -0.0408 203 THR B OG1 
3220 C CG2 . THR B 201 ? 0.6732 0.6890 0.6204 -0.0423 -0.0677 -0.0211 203 THR B CG2 
3221 N N   . ALA B 202 ? 0.6464 0.6664 0.5817 -0.0581 -0.0799 -0.0415 204 ALA B N   
3222 C CA  . ALA B 202 ? 0.6549 0.6847 0.5795 -0.0637 -0.0868 -0.0384 204 ALA B CA  
3223 C C   . ALA B 202 ? 0.6700 0.7029 0.5774 -0.0714 -0.0844 -0.0458 204 ALA B C   
3224 O O   . ALA B 202 ? 0.6778 0.7209 0.5721 -0.0752 -0.0898 -0.0405 204 ALA B O   
3225 C CB  . ALA B 202 ? 0.6552 0.6816 0.5880 -0.0660 -0.0927 -0.0418 204 ALA B CB  
3226 N N   . THR B 203 ? 0.6724 0.6970 0.5798 -0.0737 -0.0765 -0.0586 205 THR B N   
3227 C CA  . THR B 203 ? 0.6722 0.6982 0.5614 -0.0821 -0.0722 -0.0673 205 THR B CA  
3228 C C   . THR B 203 ? 0.6666 0.6940 0.5422 -0.0821 -0.0650 -0.0623 205 THR B C   
3229 O O   . THR B 203 ? 0.6493 0.6717 0.5351 -0.0773 -0.0573 -0.0627 205 THR B O   
3230 C CB  . THR B 203 ? 0.6863 0.7025 0.5824 -0.0852 -0.0659 -0.0850 205 THR B CB  
3231 O OG1 . THR B 203 ? 0.6879 0.6984 0.5929 -0.0818 -0.0549 -0.0920 205 THR B OG1 
3232 C CG2 . THR B 203 ? 0.6876 0.6968 0.5997 -0.0829 -0.0723 -0.0883 205 THR B CG2 
3233 N N   . LYS B 204 ? 0.6743 0.7076 0.5259 -0.0882 -0.0681 -0.0576 206 LYS B N   
3234 C CA  . LYS B 204 ? 0.6788 0.7097 0.5113 -0.0903 -0.0606 -0.0534 206 LYS B CA  
3235 C C   . LYS B 204 ? 0.6776 0.7026 0.4972 -0.0995 -0.0495 -0.0696 206 LYS B C   
3236 O O   . LYS B 204 ? 0.6597 0.6866 0.4642 -0.1076 -0.0528 -0.0763 206 LYS B O   
3237 C CB  . LYS B 204 ? 0.6922 0.7304 0.5045 -0.0911 -0.0710 -0.0385 206 LYS B CB  
3238 C CG  . LYS B 204 ? 0.7347 0.7766 0.5606 -0.0809 -0.0772 -0.0228 206 LYS B CG  
3239 C CD  . LYS B 204 ? 0.7723 0.8188 0.6252 -0.0748 -0.0833 -0.0222 206 LYS B CD  
3240 C CE  . LYS B 204 ? 0.8292 0.8731 0.6968 -0.0651 -0.0815 -0.0118 206 LYS B CE  
3241 N NZ  . LYS B 204 ? 0.8527 0.9012 0.7417 -0.0597 -0.0883 -0.0083 206 LYS B NZ  
3242 N N   . SER B 205 ? 0.6956 0.7138 0.5233 -0.0985 -0.0356 -0.0770 207 SER B N   
3243 C CA  . SER B 205 ? 0.7280 0.7407 0.5508 -0.1060 -0.0215 -0.0947 207 SER B CA  
3244 C C   . SER B 205 ? 0.7365 0.7445 0.5399 -0.1115 -0.0077 -0.0941 207 SER B C   
3245 O O   . SER B 205 ? 0.7343 0.7382 0.5394 -0.1168 0.0073  -0.1094 207 SER B O   
3246 C CB  . SER B 205 ? 0.7578 0.7673 0.6145 -0.0997 -0.0161 -0.1075 207 SER B CB  
3247 O OG  . SER B 205 ? 0.8134 0.8228 0.6830 -0.0972 -0.0266 -0.1108 207 SER B OG  
3248 N N   . GLY B 206 ? 0.7461 0.7538 0.5318 -0.1105 -0.0120 -0.0772 208 GLY B N   
3249 C CA  . GLY B 206 ? 0.7775 0.7777 0.5413 -0.1164 0.0008  -0.0745 208 GLY B CA  
3250 C C   . GLY B 206 ? 0.7929 0.7909 0.5664 -0.1084 0.0008  -0.0603 208 GLY B C   
3251 O O   . GLY B 206 ? 0.7859 0.7881 0.5660 -0.1002 -0.0131 -0.0462 208 GLY B O   
3252 N N   . SER B 207 ? 0.8057 0.7970 0.5806 -0.1114 0.0173  -0.0645 209 SER B N   
3253 C CA  . SER B 207 ? 0.8098 0.7962 0.5859 -0.1061 0.0181  -0.0497 209 SER B CA  
3254 C C   . SER B 207 ? 0.7972 0.7886 0.6115 -0.0944 0.0137  -0.0483 209 SER B C   
3255 O O   . SER B 207 ? 0.8159 0.8056 0.6313 -0.0876 0.0064  -0.0329 209 SER B O   
3256 C CB  . SER B 207 ? 0.8279 0.8036 0.5871 -0.1151 0.0371  -0.0526 209 SER B CB  
3257 O OG  . SER B 207 ? 0.8433 0.8194 0.6060 -0.1240 0.0535  -0.0729 209 SER B OG  
3258 N N   . THR B 208 ? 0.7665 0.7630 0.6115 -0.0918 0.0175  -0.0638 210 THR B N   
3259 C CA  . THR B 208 ? 0.7445 0.7446 0.6223 -0.0809 0.0106  -0.0616 210 THR B CA  
3260 C C   . THR B 208 ? 0.7100 0.7153 0.6078 -0.0767 0.0013  -0.0712 210 THR B C   
3261 O O   . THR B 208 ? 0.7105 0.7170 0.5958 -0.0818 -0.0009 -0.0773 210 THR B O   
3262 C CB  . THR B 208 ? 0.7667 0.7644 0.6638 -0.0801 0.0237  -0.0669 210 THR B CB  
3263 O OG1 . THR B 208 ? 0.7804 0.7767 0.6724 -0.0897 0.0410  -0.0809 210 THR B OG1 
3264 C CG2 . THR B 208 ? 0.7872 0.7786 0.6741 -0.0782 0.0243  -0.0505 210 THR B CG2 
3265 N N   . THR B 209 ? 0.6781 0.6845 0.6040 -0.0680 -0.0046 -0.0717 211 THR B N   
3266 C CA  . THR B 209 ? 0.6578 0.6652 0.6027 -0.0634 -0.0136 -0.0792 211 THR B CA  
3267 C C   . THR B 209 ? 0.6226 0.6293 0.5977 -0.0597 -0.0077 -0.0940 211 THR B C   
3268 O O   . THR B 209 ? 0.6173 0.6248 0.6030 -0.0589 0.0004  -0.0952 211 THR B O   
3269 C CB  . THR B 209 ? 0.6654 0.6730 0.6135 -0.0566 -0.0277 -0.0653 211 THR B CB  
3270 O OG1 . THR B 209 ? 0.7019 0.7125 0.6259 -0.0598 -0.0330 -0.0535 211 THR B OG1 
3271 C CG2 . THR B 209 ? 0.6491 0.6543 0.6138 -0.0523 -0.0374 -0.0706 211 THR B CG2 
3272 N N   . LYS B 210 ? 0.5919 0.5971 0.5816 -0.0575 -0.0121 -0.1052 212 LYS B N   
3273 C CA  . LYS B 210 ? 0.5723 0.5770 0.5928 -0.0524 -0.0096 -0.1190 212 LYS B CA  
3274 C C   . LYS B 210 ? 0.5453 0.5476 0.5838 -0.0434 -0.0200 -0.1112 212 LYS B C   
3275 O O   . LYS B 210 ? 0.5539 0.5526 0.5839 -0.0406 -0.0314 -0.0990 212 LYS B O   
3276 C CB  . LYS B 210 ? 0.6236 0.6241 0.6532 -0.0512 -0.0140 -0.1312 212 LYS B CB  
3277 C CG  . LYS B 210 ? 0.7104 0.7125 0.7334 -0.0590 -0.0012 -0.1466 212 LYS B CG  
3278 C CD  . LYS B 210 ? 0.7776 0.7745 0.8231 -0.0547 -0.0040 -0.1624 212 LYS B CD  
3279 C CE  . LYS B 210 ? 0.8277 0.8154 0.8718 -0.0501 -0.0206 -0.1557 212 LYS B CE  
3280 N NZ  . LYS B 210 ? 0.8333 0.8164 0.8960 -0.0400 -0.0331 -0.1475 212 LYS B NZ  
3281 N N   . ASN B 211 ? 0.5189 0.5238 0.5820 -0.0397 -0.0157 -0.1189 213 ASN B N   
3282 C CA  . ASN B 211 ? 0.5137 0.5157 0.5968 -0.0313 -0.0262 -0.1153 213 ASN B CA  
3283 C C   . ASN B 211 ? 0.5154 0.5129 0.6226 -0.0246 -0.0351 -0.1267 213 ASN B C   
3284 O O   . ASN B 211 ? 0.5198 0.5217 0.6478 -0.0239 -0.0281 -0.1427 213 ASN B O   
3285 C CB  . ASN B 211 ? 0.5313 0.5392 0.6287 -0.0315 -0.0179 -0.1175 213 ASN B CB  
3286 C CG  . ASN B 211 ? 0.6039 0.6126 0.6787 -0.0369 -0.0104 -0.1048 213 ASN B CG  
3287 O OD1 . ASN B 211 ? 0.6244 0.6373 0.7007 -0.0421 0.0032  -0.1090 213 ASN B OD1 
3288 N ND2 . ASN B 211 ? 0.6278 0.6320 0.6821 -0.0361 -0.0182 -0.0892 213 ASN B ND2 
3289 N N   . ARG B 212 ? 0.5144 0.5023 0.6190 -0.0195 -0.0499 -0.1189 214 ARG B N   
3290 C CA  . ARG B 212 ? 0.5230 0.5023 0.6484 -0.0119 -0.0613 -0.1265 214 ARG B CA  
3291 C C   . ARG B 212 ? 0.5152 0.4984 0.6693 -0.0054 -0.0641 -0.1322 214 ARG B C   
3292 O O   . ARG B 212 ? 0.5073 0.4909 0.6877 0.0000  -0.0665 -0.1458 214 ARG B O   
3293 C CB  . ARG B 212 ? 0.5580 0.5236 0.6677 -0.0099 -0.0758 -0.1145 214 ARG B CB  
3294 C CG  . ARG B 212 ? 0.6016 0.5531 0.7234 -0.0037 -0.0882 -0.1202 214 ARG B CG  
3295 C CD  . ARG B 212 ? 0.6384 0.5863 0.7594 -0.0061 -0.0846 -0.1310 214 ARG B CD  
3296 N NE  . ARG B 212 ? 0.6883 0.6353 0.7818 -0.0144 -0.0818 -0.1244 214 ARG B NE  
3297 C CZ  . ARG B 212 ? 0.7362 0.6718 0.8132 -0.0161 -0.0913 -0.1144 214 ARG B CZ  
3298 N NH1 . ARG B 212 ? 0.7200 0.6583 0.7761 -0.0241 -0.0882 -0.1103 214 ARG B NH1 
3299 N NH2 . ARG B 212 ? 0.7625 0.6839 0.8436 -0.0104 -0.1039 -0.1088 214 ARG B NH2 
3300 N N   . PHE B 213 ? 0.5114 0.4979 0.6622 -0.0059 -0.0639 -0.1228 215 PHE B N   
3301 C CA  . PHE B 213 ? 0.5071 0.4987 0.6835 -0.0014 -0.0662 -0.1279 215 PHE B CA  
3302 C C   . PHE B 213 ? 0.5225 0.5238 0.6936 -0.0076 -0.0528 -0.1241 215 PHE B C   
3303 O O   . PHE B 213 ? 0.5310 0.5316 0.6758 -0.0133 -0.0461 -0.1134 215 PHE B O   
3304 C CB  . PHE B 213 ? 0.5063 0.4859 0.6835 0.0052  -0.0847 -0.1194 215 PHE B CB  
3305 C CG  . PHE B 213 ? 0.5186 0.4833 0.6908 0.0097  -0.0981 -0.1184 215 PHE B CG  
3306 C CD1 . PHE B 213 ? 0.5237 0.4856 0.7199 0.0162  -0.1046 -0.1312 215 PHE B CD1 
3307 C CD2 . PHE B 213 ? 0.5459 0.4991 0.6899 0.0070  -0.1035 -0.1050 215 PHE B CD2 
3308 C CE1 . PHE B 213 ? 0.5464 0.4914 0.7362 0.0200  -0.1167 -0.1297 215 PHE B CE1 
3309 C CE2 . PHE B 213 ? 0.5630 0.5006 0.7009 0.0096  -0.1147 -0.1041 215 PHE B CE2 
3310 C CZ  . PHE B 213 ? 0.5630 0.4954 0.7224 0.0161  -0.1213 -0.1160 215 PHE B CZ  
3311 N N   . VAL B 214 ? 0.5161 0.5260 0.7132 -0.0063 -0.0496 -0.1330 216 VAL B N   
3312 C CA  . VAL B 214 ? 0.5176 0.5353 0.7140 -0.0124 -0.0366 -0.1314 216 VAL B CA  
3313 C C   . VAL B 214 ? 0.5091 0.5287 0.7290 -0.0078 -0.0459 -0.1337 216 VAL B C   
3314 O O   . VAL B 214 ? 0.4950 0.5168 0.7417 -0.0010 -0.0565 -0.1438 216 VAL B O   
3315 C CB  . VAL B 214 ? 0.5331 0.5626 0.7402 -0.0192 -0.0171 -0.1457 216 VAL B CB  
3316 C CG1 . VAL B 214 ? 0.5499 0.5858 0.7584 -0.0264 -0.0028 -0.1456 216 VAL B CG1 
3317 C CG2 . VAL B 214 ? 0.5435 0.5699 0.7236 -0.0248 -0.0088 -0.1434 216 VAL B CG2 
3318 N N   . VAL B 215 ? 0.5178 0.5357 0.7273 -0.0112 -0.0431 -0.1243 217 VAL B N   
3319 C CA  . VAL B 215 ? 0.5234 0.5447 0.7542 -0.0093 -0.0489 -0.1281 217 VAL B CA  
3320 C C   . VAL B 215 ? 0.5240 0.5503 0.7518 -0.0176 -0.0327 -0.1269 217 VAL B C   
3321 O O   . VAL B 215 ? 0.5181 0.5508 0.7685 -0.0182 -0.0337 -0.1340 217 VAL B O   
3322 C CB  . VAL B 215 ? 0.5518 0.5603 0.7728 -0.0038 -0.0675 -0.1174 217 VAL B CB  
3323 C CG1 . VAL B 215 ? 0.5785 0.5781 0.7987 0.0036  -0.0837 -0.1172 217 VAL B CG1 
3324 C CG2 . VAL B 215 ? 0.5722 0.5710 0.7607 -0.0075 -0.0638 -0.1008 217 VAL B CG2 
3325 O OXT . VAL B 215 ? 0.5158 0.5389 0.7186 -0.0237 -0.0199 -0.1188 217 VAL B OXT 
# 
