data_8QM7
# 
_entry.id   8QM7 
# 
_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   8QM7         pdb_00008qm7 10.2210/pdb8qm7/pdb 
WWPDB D_1292133485 ?            ?                   
# 
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                        8QM7 
_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 'DIMETHYL SULFOXIDE'                                                                         78.133    3   ? ? ? 
? 
3 non-polymer syn 'TRIETHYLENE GLYCOL'                                                                         150.173   1   ? ? ? 
? 
4 non-polymer syn '(2~{R})-2-[(1~{R})-1-[4-(2-fluorophenyl)-2-(2-hydroxyethylamino)phenyl]propoxy]propan-1-ol' 347.424   2   ? ? ? 
? 
5 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                                                      106.120   1   ? ? ? 
? 
6 water       nat water                                                                                        18.015    197 ? ? ? 
? 
# 
_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 'DIMETHYL SULFOXIDE'                                                                         DMS 
3 'TRIETHYLENE GLYCOL'                                                                         PGE 
4 '(2~{R})-2-[(1~{R})-1-[4-(2-fluorophenyl)-2-(2-hydroxyethylamino)phenyl]propoxy]propan-1-ol' W5K 
5 'DI(HYDROXYETHYL)ETHER'                                                                      PEG 
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  
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 
PGE non-polymer         . 'TRIETHYLENE GLYCOL'                                                                         ? 
'C6 H14 O4'      150.173 
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 
W5K non-polymer         . '(2~{R})-2-[(1~{R})-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  10  GLY GLY 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 W5K ? ? W5K ? ? 'SUBJECT OF INVESTIGATION' ? 
2 W5K ? ? W5K ? ? '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 DMS 1   301 301 DMS DMS A . 
D 2 DMS 1   302 401 DMS DMS A . 
E 3 PGE 1   303 501 PGE PGE A . 
F 4 W5K 1   304 1   W5K L01 A . 
G 2 DMS 1   401 401 DMS DMS B . 
H 5 PEG 1   402 208 PEG PEG B . 
I 4 W5K 1   403 1   W5K L02 B . 
J 6 HOH 1   401 187 HOH HOH A . 
J 6 HOH 2   402 220 HOH HOH A . 
J 6 HOH 3   403 79  HOH HOH A . 
J 6 HOH 4   404 161 HOH HOH A . 
J 6 HOH 5   405 138 HOH HOH A . 
J 6 HOH 6   406 170 HOH HOH A . 
J 6 HOH 7   407 56  HOH HOH A . 
J 6 HOH 8   408 12  HOH HOH A . 
J 6 HOH 9   409 2   HOH HOH A . 
J 6 HOH 10  410 121 HOH HOH A . 
J 6 HOH 11  411 63  HOH HOH A . 
J 6 HOH 12  412 4   HOH HOH A . 
J 6 HOH 13  413 156 HOH HOH A . 
J 6 HOH 14  414 6   HOH HOH A . 
J 6 HOH 15  415 55  HOH HOH A . 
J 6 HOH 16  416 23  HOH HOH A . 
J 6 HOH 17  417 44  HOH HOH A . 
J 6 HOH 18  418 186 HOH HOH A . 
J 6 HOH 19  419 10  HOH HOH A . 
J 6 HOH 20  420 181 HOH HOH A . 
J 6 HOH 21  421 102 HOH HOH A . 
J 6 HOH 22  422 139 HOH HOH A . 
J 6 HOH 23  423 201 HOH HOH A . 
J 6 HOH 24  424 179 HOH HOH A . 
J 6 HOH 25  425 42  HOH HOH A . 
J 6 HOH 26  426 85  HOH HOH A . 
J 6 HOH 27  427 11  HOH HOH A . 
J 6 HOH 28  428 18  HOH HOH A . 
J 6 HOH 29  429 7   HOH HOH A . 
J 6 HOH 30  430 29  HOH HOH A . 
J 6 HOH 31  431 46  HOH HOH A . 
J 6 HOH 32  432 153 HOH HOH A . 
J 6 HOH 33  433 174 HOH HOH A . 
J 6 HOH 34  434 59  HOH HOH A . 
J 6 HOH 35  435 52  HOH HOH A . 
J 6 HOH 36  436 81  HOH HOH A . 
J 6 HOH 37  437 3   HOH HOH A . 
J 6 HOH 38  438 131 HOH HOH A . 
J 6 HOH 39  439 9   HOH HOH A . 
J 6 HOH 40  440 45  HOH HOH A . 
J 6 HOH 41  441 8   HOH HOH A . 
J 6 HOH 42  442 203 HOH HOH A . 
J 6 HOH 43  443 130 HOH HOH A . 
J 6 HOH 44  444 200 HOH HOH A . 
J 6 HOH 45  445 152 HOH HOH A . 
J 6 HOH 46  446 16  HOH HOH A . 
J 6 HOH 47  447 105 HOH HOH A . 
J 6 HOH 48  448 24  HOH HOH A . 
J 6 HOH 49  449 49  HOH HOH A . 
J 6 HOH 50  450 169 HOH HOH A . 
J 6 HOH 51  451 70  HOH HOH A . 
J 6 HOH 52  452 61  HOH HOH A . 
J 6 HOH 53  453 17  HOH HOH A . 
J 6 HOH 54  454 50  HOH HOH A . 
J 6 HOH 55  455 123 HOH HOH A . 
J 6 HOH 56  456 6   HOH HOH A . 
J 6 HOH 57  457 111 HOH HOH A . 
J 6 HOH 58  458 73  HOH HOH A . 
J 6 HOH 59  459 31  HOH HOH A . 
J 6 HOH 60  460 25  HOH HOH A . 
J 6 HOH 61  461 33  HOH HOH A . 
J 6 HOH 62  462 206 HOH HOH A . 
J 6 HOH 63  463 175 HOH HOH A . 
J 6 HOH 64  464 20  HOH HOH A . 
J 6 HOH 65  465 94  HOH HOH A . 
J 6 HOH 66  466 221 HOH HOH A . 
J 6 HOH 67  467 127 HOH HOH A . 
J 6 HOH 68  468 119 HOH HOH A . 
J 6 HOH 69  469 38  HOH HOH A . 
J 6 HOH 70  470 191 HOH HOH A . 
J 6 HOH 71  471 64  HOH HOH A . 
J 6 HOH 72  472 47  HOH HOH A . 
J 6 HOH 73  473 67  HOH HOH A . 
J 6 HOH 74  474 103 HOH HOH A . 
J 6 HOH 75  475 51  HOH HOH A . 
J 6 HOH 76  476 26  HOH HOH A . 
J 6 HOH 77  477 15  HOH HOH A . 
J 6 HOH 78  478 69  HOH HOH A . 
J 6 HOH 79  479 171 HOH HOH A . 
J 6 HOH 80  480 93  HOH HOH A . 
J 6 HOH 81  481 71  HOH HOH A . 
J 6 HOH 82  482 98  HOH HOH A . 
J 6 HOH 83  483 167 HOH HOH A . 
J 6 HOH 84  484 116 HOH HOH A . 
J 6 HOH 85  485 154 HOH HOH A . 
J 6 HOH 86  486 65  HOH HOH A . 
J 6 HOH 87  487 145 HOH HOH A . 
J 6 HOH 88  488 100 HOH HOH A . 
J 6 HOH 89  489 132 HOH HOH A . 
J 6 HOH 90  490 135 HOH HOH A . 
J 6 HOH 91  491 140 HOH HOH A . 
J 6 HOH 92  492 114 HOH HOH A . 
J 6 HOH 93  493 96  HOH HOH A . 
J 6 HOH 94  494 226 HOH HOH A . 
J 6 HOH 95  495 113 HOH HOH A . 
J 6 HOH 96  496 91  HOH HOH A . 
J 6 HOH 97  497 223 HOH HOH A . 
J 6 HOH 98  498 68  HOH HOH A . 
J 6 HOH 99  499 104 HOH HOH A . 
J 6 HOH 100 500 183 HOH HOH A . 
J 6 HOH 101 501 90  HOH HOH A . 
J 6 HOH 102 502 160 HOH HOH A . 
J 6 HOH 103 503 84  HOH HOH A . 
J 6 HOH 104 504 192 HOH HOH A . 
J 6 HOH 105 505 57  HOH HOH A . 
J 6 HOH 106 506 133 HOH HOH A . 
J 6 HOH 107 507 224 HOH HOH A . 
J 6 HOH 108 508 137 HOH HOH A . 
J 6 HOH 109 509 218 HOH HOH A . 
J 6 HOH 110 510 225 HOH HOH A . 
J 6 HOH 111 511 120 HOH HOH A . 
J 6 HOH 112 512 106 HOH HOH A . 
J 6 HOH 113 513 157 HOH HOH A . 
J 6 HOH 114 514 193 HOH HOH A . 
K 6 HOH 1   501 34  HOH HOH B . 
K 6 HOH 2   502 37  HOH HOH B . 
K 6 HOH 3   503 125 HOH HOH B . 
K 6 HOH 4   504 178 HOH HOH B . 
K 6 HOH 5   505 107 HOH HOH B . 
K 6 HOH 6   506 13  HOH HOH B . 
K 6 HOH 7   507 76  HOH HOH B . 
K 6 HOH 8   508 109 HOH HOH B . 
K 6 HOH 9   509 149 HOH HOH B . 
K 6 HOH 10  510 110 HOH HOH B . 
K 6 HOH 11  511 112 HOH HOH B . 
K 6 HOH 12  512 199 HOH HOH B . 
K 6 HOH 13  513 32  HOH HOH B . 
K 6 HOH 14  514 87  HOH HOH B . 
K 6 HOH 15  515 75  HOH HOH B . 
K 6 HOH 16  516 83  HOH HOH B . 
K 6 HOH 17  517 43  HOH HOH B . 
K 6 HOH 18  518 202 HOH HOH B . 
K 6 HOH 19  519 41  HOH HOH B . 
K 6 HOH 20  520 14  HOH HOH B . 
K 6 HOH 21  521 28  HOH HOH B . 
K 6 HOH 22  522 129 HOH HOH B . 
K 6 HOH 23  523 185 HOH HOH B . 
K 6 HOH 24  524 108 HOH HOH B . 
K 6 HOH 25  525 30  HOH HOH B . 
K 6 HOH 26  526 58  HOH HOH B . 
K 6 HOH 27  527 162 HOH HOH B . 
K 6 HOH 28  528 134 HOH HOH B . 
K 6 HOH 29  529 205 HOH HOH B . 
K 6 HOH 30  530 158 HOH HOH B . 
K 6 HOH 31  531 19  HOH HOH B . 
K 6 HOH 32  532 164 HOH HOH B . 
K 6 HOH 33  533 177 HOH HOH B . 
K 6 HOH 34  534 1   HOH HOH B . 
K 6 HOH 35  535 150 HOH HOH B . 
K 6 HOH 36  536 39  HOH HOH B . 
K 6 HOH 37  537 40  HOH HOH B . 
K 6 HOH 38  538 101 HOH HOH B . 
K 6 HOH 39  539 48  HOH HOH B . 
K 6 HOH 40  540 136 HOH HOH B . 
K 6 HOH 41  541 194 HOH HOH B . 
K 6 HOH 42  542 92  HOH HOH B . 
K 6 HOH 43  543 60  HOH HOH B . 
K 6 HOH 44  544 72  HOH HOH B . 
K 6 HOH 45  545 207 HOH HOH B . 
K 6 HOH 46  546 165 HOH HOH B . 
K 6 HOH 47  547 74  HOH HOH B . 
K 6 HOH 48  548 53  HOH HOH B . 
K 6 HOH 49  549 78  HOH HOH B . 
K 6 HOH 50  550 173 HOH HOH B . 
K 6 HOH 51  551 66  HOH HOH B . 
K 6 HOH 52  552 141 HOH HOH B . 
K 6 HOH 53  553 172 HOH HOH B . 
K 6 HOH 54  554 115 HOH HOH B . 
K 6 HOH 55  555 155 HOH HOH B . 
K 6 HOH 56  556 86  HOH HOH B . 
K 6 HOH 57  557 195 HOH HOH B . 
K 6 HOH 58  558 54  HOH HOH B . 
K 6 HOH 59  559 89  HOH HOH B . 
K 6 HOH 60  560 117 HOH HOH B . 
K 6 HOH 61  561 27  HOH HOH B . 
K 6 HOH 62  562 36  HOH HOH B . 
K 6 HOH 63  563 189 HOH HOH B . 
K 6 HOH 64  564 82  HOH HOH B . 
K 6 HOH 65  565 99  HOH HOH B . 
K 6 HOH 66  566 126 HOH HOH B . 
K 6 HOH 67  567 21  HOH HOH B . 
K 6 HOH 68  568 118 HOH HOH B . 
K 6 HOH 69  569 182 HOH HOH B . 
K 6 HOH 70  570 197 HOH HOH B . 
K 6 HOH 71  571 3   HOH HOH B . 
K 6 HOH 72  572 198 HOH HOH B . 
K 6 HOH 73  573 122 HOH HOH B . 
K 6 HOH 74  574 188 HOH HOH B . 
K 6 HOH 75  575 144 HOH HOH B . 
K 6 HOH 76  576 142 HOH HOH B . 
K 6 HOH 77  577 176 HOH HOH B . 
K 6 HOH 78  578 128 HOH HOH B . 
K 6 HOH 79  579 4   HOH HOH B . 
K 6 HOH 80  580 97  HOH HOH B . 
K 6 HOH 81  581 5   HOH HOH B . 
K 6 HOH 82  582 95  HOH HOH B . 
K 6 HOH 83  583 211 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                   95.67 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QM7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     47.157 
_cell.length_a_esd                 ? 
_cell.length_b                     69.122 
_cell.length_b_esd                 ? 
_cell.length_c                     64.435 
_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                         8QM7 
_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                   8QM7 
_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             2.09 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.12 
_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                                       8QM7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.19 
_reflns.d_resolution_low                               64.12 
_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                                     20450 
_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                           95.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.6 
_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                                0.19 
_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                                    2.19 
_reflns_shell.d_res_low                                     2.27 
_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                             1900 
_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                               ? 
_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                                  1.88 
_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]                            -1.77810 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -1.81960 
_refine.aniso_B[2][2]                            9.83640 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            -8.05820 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               47.574 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.940 
_refine.correlation_coeff_Fo_to_Fc_free          0.912 
_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                                 8QM7 
_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                            2.191 
_refine.ls_d_res_low                             64.12 
_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                     20450 
_refine.ls_number_reflns_R_free                  1027 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.9 
_refine.ls_percent_reflns_R_free                 5.020 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1945 
_refine.ls_R_factor_R_free                       0.2401 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1920 
_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          0.222 
_refine.pdbx_overall_SU_R_Blow_DPI               0.334 
_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                        8QM7 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.27 
_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                       2.191 
_refine_hist.d_res_low                        64.12 
_refine_hist.number_atoms_solvent             197 
_refine_hist.number_atoms_total               3589 
_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        3313 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         79 
_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 ? 6799  ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 1.00  ? 12202 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1489  ? 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' ? ?     ? 1077  ? t_gen_planes              16.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 6799  ? t_it                      10.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 6.85  ? ?     ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 15.35 ? ?     ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 427   ? 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' ? ?     ? 5230  ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.191 
_refine_ls_shell.d_res_low                        2.21 
_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             391 
_refine_ls_shell.percent_reflns_obs               93.84 
_refine_ls_shell.percent_reflns_R_free            4.40 
_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                  0.2933 
_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                  0.3123 
# 
_struct.entry_id                     8QM7 
_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        8QM7 
_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 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 2 ? 
H N N 5 ? 
I N N 4 ? 
J N N 6 ? 
K 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 8QM7 A 34 ? 215 ? P06730 36 ? 217 ? 36 217 
2 1 8QM7 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 8QM7 MET A 1   ? UNP P06730 ?   ?   'initiating methionine' 3   1  
1 8QM7 HIS A 2   ? UNP P06730 ?   ?   'expression tag'        4   2  
1 8QM7 HIS A 3   ? UNP P06730 ?   ?   'expression tag'        5   3  
1 8QM7 HIS A 4   ? UNP P06730 ?   ?   'expression tag'        6   4  
1 8QM7 HIS A 5   ? UNP P06730 ?   ?   'expression tag'        7   5  
1 8QM7 HIS A 6   ? UNP P06730 ?   ?   'expression tag'        8   6  
1 8QM7 HIS A 7   ? UNP P06730 ?   ?   'expression tag'        9   7  
1 8QM7 GLY A 8   ? UNP P06730 ?   ?   'expression tag'        10  8  
1 8QM7 ALA A 9   ? UNP P06730 ?   ?   'expression tag'        11  9  
1 8QM7 ARG A 10  ? UNP P06730 ?   ?   'expression tag'        12  10 
1 8QM7 ILE A 11  ? UNP P06730 ?   ?   'expression tag'        13  11 
1 8QM7 ILE A 12  ? UNP P06730 ?   ?   'expression tag'        14  12 
1 8QM7 TYR A 13  ? UNP P06730 ?   ?   'expression tag'        15  13 
1 8QM7 ASP A 14  ? UNP P06730 ?   ?   'expression tag'        16  14 
1 8QM7 ARG A 15  ? UNP P06730 ?   ?   'expression tag'        17  15 
1 8QM7 ALA A 16  ? UNP P06730 ?   ?   'expression tag'        18  16 
1 8QM7 PHE A 17  ? UNP P06730 ?   ?   'expression tag'        19  17 
1 8QM7 LEU A 18  ? UNP P06730 ?   ?   'expression tag'        20  18 
1 8QM7 MET A 19  ? UNP P06730 ?   ?   'expression tag'        21  19 
1 8QM7 ALA A 20  ? UNP P06730 ?   ?   'expression tag'        22  20 
1 8QM7 CYS A 21  ? UNP P06730 ?   ?   'expression tag'        23  21 
1 8QM7 ARG A 22  ? UNP P06730 ?   ?   'expression tag'        24  22 
1 8QM7 GLY A 23  ? UNP P06730 ?   ?   'expression tag'        25  23 
1 8QM7 GLY A 24  ? UNP P06730 ?   ?   'expression tag'        26  24 
1 8QM7 GLY A 25  ? UNP P06730 ?   ?   'expression tag'        27  25 
1 8QM7 GLY A 26  ? UNP P06730 ?   ?   'expression tag'        28  26 
1 8QM7 GLU A 27  ? UNP P06730 ?   ?   'expression tag'        29  27 
1 8QM7 ASN A 28  ? UNP P06730 ?   ?   'expression tag'        30  28 
1 8QM7 LEU A 29  ? UNP P06730 ?   ?   'expression tag'        31  29 
1 8QM7 TYR A 30  ? UNP P06730 ?   ?   'expression tag'        32  30 
1 8QM7 PHE A 31  ? UNP P06730 ?   ?   'expression tag'        33  31 
1 8QM7 GLN A 32  ? UNP P06730 ?   ?   'expression tag'        34  32 
1 8QM7 GLY A 33  ? UNP P06730 ?   ?   'expression tag'        35  33 
1 8QM7 ASN A 125 ? UNP P06730 ASP 127 conflict                127 34 
2 8QM7 MET B 1   ? UNP P06730 ?   ?   'initiating methionine' 3   35 
2 8QM7 HIS B 2   ? UNP P06730 ?   ?   'expression tag'        4   36 
2 8QM7 HIS B 3   ? UNP P06730 ?   ?   'expression tag'        5   37 
2 8QM7 HIS B 4   ? UNP P06730 ?   ?   'expression tag'        6   38 
2 8QM7 HIS B 5   ? UNP P06730 ?   ?   'expression tag'        7   39 
2 8QM7 HIS B 6   ? UNP P06730 ?   ?   'expression tag'        8   40 
2 8QM7 HIS B 7   ? UNP P06730 ?   ?   'expression tag'        9   41 
2 8QM7 GLY B 8   ? UNP P06730 ?   ?   'expression tag'        10  42 
2 8QM7 ALA B 9   ? UNP P06730 ?   ?   'expression tag'        11  43 
2 8QM7 ARG B 10  ? UNP P06730 ?   ?   'expression tag'        12  44 
2 8QM7 ILE B 11  ? UNP P06730 ?   ?   'expression tag'        13  45 
2 8QM7 ILE B 12  ? UNP P06730 ?   ?   'expression tag'        14  46 
2 8QM7 TYR B 13  ? UNP P06730 ?   ?   'expression tag'        15  47 
2 8QM7 ASP B 14  ? UNP P06730 ?   ?   'expression tag'        16  48 
2 8QM7 ARG B 15  ? UNP P06730 ?   ?   'expression tag'        17  49 
2 8QM7 ALA B 16  ? UNP P06730 ?   ?   'expression tag'        18  50 
2 8QM7 PHE B 17  ? UNP P06730 ?   ?   'expression tag'        19  51 
2 8QM7 LEU B 18  ? UNP P06730 ?   ?   'expression tag'        20  52 
2 8QM7 MET B 19  ? UNP P06730 ?   ?   'expression tag'        21  53 
2 8QM7 ALA B 20  ? UNP P06730 ?   ?   'expression tag'        22  54 
2 8QM7 CYS B 21  ? UNP P06730 ?   ?   'expression tag'        23  55 
2 8QM7 ARG B 22  ? UNP P06730 ?   ?   'expression tag'        24  56 
2 8QM7 GLY B 23  ? UNP P06730 ?   ?   'expression tag'        25  57 
2 8QM7 GLY B 24  ? UNP P06730 ?   ?   'expression tag'        26  58 
2 8QM7 GLY B 25  ? UNP P06730 ?   ?   'expression tag'        27  59 
2 8QM7 GLY B 26  ? UNP P06730 ?   ?   'expression tag'        28  60 
2 8QM7 GLU B 27  ? UNP P06730 ?   ?   'expression tag'        29  61 
2 8QM7 ASN B 28  ? UNP P06730 ?   ?   'expression tag'        30  62 
2 8QM7 LEU B 29  ? UNP P06730 ?   ?   'expression tag'        31  63 
2 8QM7 TYR B 30  ? UNP P06730 ?   ?   'expression tag'        32  64 
2 8QM7 PHE B 31  ? UNP P06730 ?   ?   'expression tag'        33  65 
2 8QM7 GLN B 32  ? UNP P06730 ?   ?   'expression tag'        34  66 
2 8QM7 GLY B 33  ? UNP P06730 ?   ?   'expression tag'        35  67 
2 8QM7 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)' 2370  ? 
1 MORE         18    ? 
1 'SSA (A^2)'  20340 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'mass spectrometry' 
_pdbx_struct_assembly_auth_evidence.details                'the molecule is a 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]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 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 ? LEU A 185 ? ASN A 172 LEU A 187 1 ? 16 
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 LYS B 52  ? ASN B 57  ? LYS B 54  ASN B 59  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 ASN B 116 ? GLY B 137 ? ASN B 118 GLY B 139 1 ? 22 
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 LEU B 58  ? THR B 66  ? LEU B 60  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 TRP A 44  ? N TRP A 46  O SER A 90  ? O SER A 92  
AA1 3 4 N TYR A 89  ? N TYR A 91  O VAL A 152 ? O VAL A 154 
AA1 4 5 N CYS A 148 ? N CYS A 150 O TRP A 164 ? O TRP A 166 
AA1 5 6 O ILE A 161 ? O ILE A 163 N ILE A 113 ? N ILE A 115 
AA1 6 7 N LEU A 112 ? N LEU A 114 O GLY A 194 ? O GLY A 196 
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 ALA B 42  ? N ALA B 44  O PHE B 92  ? O PHE B 94  
AA2 3 4 N TYR B 89  ? N TYR B 91  O VAL B 152 ? O VAL B 154 
AA2 4 5 N CYS B 148 ? N CYS B 150 O TRP B 164 ? O TRP B 166 
AA2 5 6 O ILE B 161 ? O ILE B 163 N ILE B 113 ? N ILE B 115 
AA2 6 7 N LEU B 112 ? N LEU B 114 O GLY B 194 ? O GLY B 196 
AA2 7 8 N TYR B 195 ? N TYR B 197 O PHE B 213 ? O PHE B 215 
# 
_pdbx_entry_details.entry_id                   8QM7 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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  ? ? 57.76   17.86   
2 1 LYS A 52  ? ? 85.50   26.81   
3 1 ASP A 67  ? ? -145.56 23.05   
4 1 PRO A 100 ? ? -79.26  49.75   
5 1 ASP A 143 ? ? 57.24   -140.00 
6 1 THR B 55  ? ? 62.19   158.75  
7 1 ASP B 67  ? ? -145.97 23.46   
8 1 PRO B 100 ? ? -79.16  49.80   
9 1 ASP B 143 ? ? 60.05   -141.69 
# 
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 20.5784 -13.6990 4.1621  -0.0722 ? -0.0257 ? 0.0322 ? -0.0429 ? 0.0036 ? 0.0665  ? 1.5625 ? 0.0214 
? -0.0272 ? 1.7232 ? -0.2626 ? 0.2716 ? 0.0877  ? -0.0356 ? 0.1874  ? 0.0855  ? -0.0432 ? 0.1371 ? 0.1090 ? 0.1167 ? -0.0445 ? 
2 'X-RAY DIFFRACTION' ? refined 1.6918  -21.4124 32.2396 0.0323  ? 0.0017  ? 0.0161 ? -0.0608 ? 0.0351 ? -0.0723 ? 1.0609 ? 0.5279 
? -0.6300 ? 2.8630 ? 0.8100  ? 1.9105 ? -0.1580 ? -0.2556 ? -0.0926 ? -0.0868 ? -0.0820 ? 0.1079 ? 0.0056 ? 0.1325 ? 0.2400  ? 
# 
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|10 - 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 B MET 3  ? B MET 1  
9  1 Y 1 B HIS 4  ? B HIS 2  
10 1 Y 1 B HIS 5  ? B HIS 3  
11 1 Y 1 B HIS 6  ? B HIS 4  
12 1 Y 1 B HIS 7  ? B HIS 5  
13 1 Y 1 B HIS 8  ? B HIS 6  
14 1 Y 1 B HIS 9  ? B HIS 7  
15 1 Y 1 B GLY 10 ? B GLY 8  
16 1 Y 1 B GLY 26 ? B GLY 24 
17 1 Y 1 B GLY 27 ? B GLY 25 
18 1 Y 1 B GLY 28 ? B GLY 26 
19 1 Y 1 B GLU 29 ? B GLU 27 
20 1 Y 1 B ASN 30 ? B ASN 28 
21 1 Y 1 B LEU 31 ? B LEU 29 
22 1 Y 1 B TYR 32 ? B TYR 30 
23 1 Y 1 B PHE 33 ? B PHE 31 
24 1 Y 1 B GLN 34 ? B GLN 32 
25 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  
GLN N    N N N 98  
GLN CA   C N S 99  
GLN C    C N N 100 
GLN O    O N N 101 
GLN CB   C N N 102 
GLN CG   C N N 103 
GLN CD   C N N 104 
GLN OE1  O N N 105 
GLN NE2  N N N 106 
GLN OXT  O N N 107 
GLN H    H N N 108 
GLN H2   H N N 109 
GLN HA   H N N 110 
GLN HB2  H N N 111 
GLN HB3  H N N 112 
GLN HG2  H N N 113 
GLN HG3  H N N 114 
GLN HE21 H N N 115 
GLN HE22 H N N 116 
GLN HXT  H N N 117 
GLU N    N N N 118 
GLU CA   C N S 119 
GLU C    C N N 120 
GLU O    O N N 121 
GLU CB   C N N 122 
GLU CG   C N N 123 
GLU CD   C N N 124 
GLU OE1  O N N 125 
GLU OE2  O N N 126 
GLU OXT  O N N 127 
GLU H    H N N 128 
GLU H2   H N N 129 
GLU HA   H N N 130 
GLU HB2  H N N 131 
GLU HB3  H N N 132 
GLU HG2  H N N 133 
GLU HG3  H N N 134 
GLU HE2  H N N 135 
GLU HXT  H N N 136 
GLY N    N N N 137 
GLY CA   C N N 138 
GLY C    C N N 139 
GLY O    O N N 140 
GLY OXT  O N N 141 
GLY H    H N N 142 
GLY H2   H N N 143 
GLY HA2  H N N 144 
GLY HA3  H N N 145 
GLY HXT  H N N 146 
HIS N    N N N 147 
HIS CA   C N S 148 
HIS C    C N N 149 
HIS O    O N N 150 
HIS CB   C N N 151 
HIS CG   C Y N 152 
HIS ND1  N Y N 153 
HIS CD2  C Y N 154 
HIS CE1  C Y N 155 
HIS NE2  N Y N 156 
HIS OXT  O N N 157 
HIS H    H N N 158 
HIS H2   H N N 159 
HIS HA   H N N 160 
HIS HB2  H N N 161 
HIS HB3  H N N 162 
HIS HD1  H N N 163 
HIS HD2  H N N 164 
HIS HE1  H N N 165 
HIS HE2  H N N 166 
HIS HXT  H N N 167 
HOH O    O N N 168 
HOH H1   H N N 169 
HOH H2   H N N 170 
ILE N    N N N 171 
ILE CA   C N S 172 
ILE C    C N N 173 
ILE O    O N N 174 
ILE CB   C N S 175 
ILE CG1  C N N 176 
ILE CG2  C N N 177 
ILE CD1  C N N 178 
ILE OXT  O N N 179 
ILE H    H N N 180 
ILE H2   H N N 181 
ILE HA   H N N 182 
ILE HB   H N N 183 
ILE HG12 H N N 184 
ILE HG13 H N N 185 
ILE HG21 H N N 186 
ILE HG22 H N N 187 
ILE HG23 H N N 188 
ILE HD11 H N N 189 
ILE HD12 H N N 190 
ILE HD13 H N N 191 
ILE HXT  H N N 192 
LEU N    N N N 193 
LEU CA   C N S 194 
LEU C    C N N 195 
LEU O    O N N 196 
LEU CB   C N N 197 
LEU CG   C N N 198 
LEU CD1  C N N 199 
LEU CD2  C N N 200 
LEU OXT  O N N 201 
LEU H    H N N 202 
LEU H2   H N N 203 
LEU HA   H N N 204 
LEU HB2  H N N 205 
LEU HB3  H N N 206 
LEU HG   H N N 207 
LEU HD11 H N N 208 
LEU HD12 H N N 209 
LEU HD13 H N N 210 
LEU HD21 H N N 211 
LEU HD22 H N N 212 
LEU HD23 H N N 213 
LEU HXT  H N N 214 
LYS N    N N N 215 
LYS CA   C N S 216 
LYS C    C N N 217 
LYS O    O N N 218 
LYS CB   C N N 219 
LYS CG   C N N 220 
LYS CD   C N N 221 
LYS CE   C N N 222 
LYS NZ   N N N 223 
LYS OXT  O N N 224 
LYS H    H N N 225 
LYS H2   H N N 226 
LYS HA   H N N 227 
LYS HB2  H N N 228 
LYS HB3  H N N 229 
LYS HG2  H N N 230 
LYS HG3  H N N 231 
LYS HD2  H N N 232 
LYS HD3  H N N 233 
LYS HE2  H N N 234 
LYS HE3  H N N 235 
LYS HZ1  H N N 236 
LYS HZ2  H N N 237 
LYS HZ3  H N N 238 
LYS HXT  H N N 239 
MET N    N N N 240 
MET CA   C N S 241 
MET C    C N N 242 
MET O    O N N 243 
MET CB   C N N 244 
MET CG   C N N 245 
MET SD   S N N 246 
MET CE   C N N 247 
MET OXT  O N N 248 
MET H    H N N 249 
MET H2   H N N 250 
MET HA   H N N 251 
MET HB2  H N N 252 
MET HB3  H N N 253 
MET HG2  H N N 254 
MET HG3  H N N 255 
MET HE1  H N N 256 
MET HE2  H N N 257 
MET HE3  H N N 258 
MET HXT  H N N 259 
PEG C1   C N N 260 
PEG O1   O N N 261 
PEG C2   C N N 262 
PEG O2   O N N 263 
PEG C3   C N N 264 
PEG C4   C N N 265 
PEG O4   O N N 266 
PEG H11  H N N 267 
PEG H12  H N N 268 
PEG HO1  H N N 269 
PEG H21  H N N 270 
PEG H22  H N N 271 
PEG H31  H N N 272 
PEG H32  H N N 273 
PEG H41  H N N 274 
PEG H42  H N N 275 
PEG HO4  H N N 276 
PGE C1   C N N 277 
PGE O1   O N N 278 
PGE C2   C N N 279 
PGE O2   O N N 280 
PGE C3   C N N 281 
PGE C4   C N N 282 
PGE O4   O N N 283 
PGE C6   C N N 284 
PGE C5   C N N 285 
PGE O3   O N N 286 
PGE H1   H N N 287 
PGE H12  H N N 288 
PGE HO1  H N N 289 
PGE H2   H N N 290 
PGE H22  H N N 291 
PGE H3   H N N 292 
PGE H32  H N N 293 
PGE H4   H N N 294 
PGE H42  H N N 295 
PGE HO4  H N N 296 
PGE H6   H N N 297 
PGE H62  H N N 298 
PGE H5   H N N 299 
PGE H52  H N N 300 
PHE N    N N N 301 
PHE CA   C N S 302 
PHE C    C N N 303 
PHE O    O N N 304 
PHE CB   C N N 305 
PHE CG   C Y N 306 
PHE CD1  C Y N 307 
PHE CD2  C Y N 308 
PHE CE1  C Y N 309 
PHE CE2  C Y N 310 
PHE CZ   C Y N 311 
PHE OXT  O N N 312 
PHE H    H N N 313 
PHE H2   H N N 314 
PHE HA   H N N 315 
PHE HB2  H N N 316 
PHE HB3  H N N 317 
PHE HD1  H N N 318 
PHE HD2  H N N 319 
PHE HE1  H N N 320 
PHE HE2  H N N 321 
PHE HZ   H N N 322 
PHE HXT  H N N 323 
PRO N    N N N 324 
PRO CA   C N S 325 
PRO C    C N N 326 
PRO O    O N N 327 
PRO CB   C N N 328 
PRO CG   C N N 329 
PRO CD   C N N 330 
PRO OXT  O N N 331 
PRO H    H N N 332 
PRO HA   H N N 333 
PRO HB2  H N N 334 
PRO HB3  H N N 335 
PRO HG2  H N N 336 
PRO HG3  H N N 337 
PRO HD2  H N N 338 
PRO HD3  H N N 339 
PRO HXT  H N N 340 
SER N    N N N 341 
SER CA   C N S 342 
SER C    C N N 343 
SER O    O N N 344 
SER CB   C N N 345 
SER OG   O N N 346 
SER OXT  O N N 347 
SER H    H N N 348 
SER H2   H N N 349 
SER HA   H N N 350 
SER HB2  H N N 351 
SER HB3  H N N 352 
SER HG   H N N 353 
SER HXT  H N N 354 
THR N    N N N 355 
THR CA   C N S 356 
THR C    C N N 357 
THR O    O N N 358 
THR CB   C N R 359 
THR OG1  O N N 360 
THR CG2  C N N 361 
THR OXT  O N N 362 
THR H    H N N 363 
THR H2   H N N 364 
THR HA   H N N 365 
THR HB   H N N 366 
THR HG1  H N N 367 
THR HG21 H N N 368 
THR HG22 H N N 369 
THR HG23 H N N 370 
THR HXT  H N N 371 
TRP N    N N N 372 
TRP CA   C N S 373 
TRP C    C N N 374 
TRP O    O N N 375 
TRP CB   C N N 376 
TRP CG   C Y N 377 
TRP CD1  C Y N 378 
TRP CD2  C Y N 379 
TRP NE1  N Y N 380 
TRP CE2  C Y N 381 
TRP CE3  C Y N 382 
TRP CZ2  C Y N 383 
TRP CZ3  C Y N 384 
TRP CH2  C Y N 385 
TRP OXT  O N N 386 
TRP H    H N N 387 
TRP H2   H N N 388 
TRP HA   H N N 389 
TRP HB2  H N N 390 
TRP HB3  H N N 391 
TRP HD1  H N N 392 
TRP HE1  H N N 393 
TRP HE3  H N N 394 
TRP HZ2  H N N 395 
TRP HZ3  H N N 396 
TRP HH2  H N N 397 
TRP HXT  H N N 398 
TYR N    N N N 399 
TYR CA   C N S 400 
TYR C    C N N 401 
TYR O    O N N 402 
TYR CB   C N N 403 
TYR CG   C Y N 404 
TYR CD1  C Y N 405 
TYR CD2  C Y N 406 
TYR CE1  C Y N 407 
TYR CE2  C Y N 408 
TYR CZ   C Y N 409 
TYR OH   O N N 410 
TYR OXT  O N N 411 
TYR H    H N N 412 
TYR H2   H N N 413 
TYR HA   H N N 414 
TYR HB2  H N N 415 
TYR HB3  H N N 416 
TYR HD1  H N N 417 
TYR HD2  H N N 418 
TYR HE1  H N N 419 
TYR HE2  H N N 420 
TYR HH   H N N 421 
TYR HXT  H N N 422 
VAL N    N N N 423 
VAL CA   C N S 424 
VAL C    C N N 425 
VAL O    O N N 426 
VAL CB   C N N 427 
VAL CG1  C N N 428 
VAL CG2  C N N 429 
VAL OXT  O N N 430 
VAL H    H N N 431 
VAL H2   H N N 432 
VAL HA   H N N 433 
VAL HB   H N N 434 
VAL HG11 H N N 435 
VAL HG12 H N N 436 
VAL HG13 H N N 437 
VAL HG21 H N N 438 
VAL HG22 H N N 439 
VAL HG23 H N N 440 
VAL HXT  H N N 441 
W5K C1   C N N 442 
W5K C2   C N N 443 
W5K C3   C N R 444 
W5K C5   C N R 445 
W5K C6   C N N 446 
W5K C7   C N N 447 
W5K C10  C Y N 448 
W5K C11  C Y N 449 
W5K C12  C Y N 450 
W5K C13  C Y N 451 
W5K C14  C Y N 452 
W5K C16  C N N 453 
W5K C19  C Y N 454 
W5K C21  C Y N 455 
W5K C22  C Y N 456 
W5K C23  C Y N 457 
W5K C24  C Y N 458 
W5K O4   O N N 459 
W5K O8   O N N 460 
W5K C9   C Y N 461 
W5K N15  N N N 462 
W5K C17  C N N 463 
W5K O18  O N N 464 
W5K C20  C Y N 465 
W5K F25  F N N 466 
W5K H29  H N N 467 
W5K H28  H N N 468 
W5K H30  H N N 469 
W5K H32  H N N 470 
W5K H31  H N N 471 
W5K H26  H N N 472 
W5K H27  H N N 473 
W5K H35  H N N 474 
W5K H34  H N N 475 
W5K H33  H N N 476 
W5K H37  H N N 477 
W5K H36  H N N 478 
W5K H39  H N N 479 
W5K H40  H N N 480 
W5K H41  H N N 481 
W5K H43  H N N 482 
W5K H44  H N N 483 
W5K H49  H N N 484 
W5K H50  H N N 485 
W5K H51  H N N 486 
W5K H38  H N N 487 
W5K H42  H N N 488 
W5K H46  H N N 489 
W5K H45  H N N 490 
W5K H47  H N N 491 
W5K H48  H N N 492 
# 
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  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PEG C1  O1   sing N N 246 
PEG C1  C2   sing N N 247 
PEG C1  H11  sing N N 248 
PEG C1  H12  sing N N 249 
PEG O1  HO1  sing N N 250 
PEG C2  O2   sing N N 251 
PEG C2  H21  sing N N 252 
PEG C2  H22  sing N N 253 
PEG O2  C3   sing N N 254 
PEG C3  C4   sing N N 255 
PEG C3  H31  sing N N 256 
PEG C3  H32  sing N N 257 
PEG C4  O4   sing N N 258 
PEG C4  H41  sing N N 259 
PEG C4  H42  sing N N 260 
PEG O4  HO4  sing N N 261 
PGE C1  O1   sing N N 262 
PGE C1  C2   sing N N 263 
PGE C1  H1   sing N N 264 
PGE C1  H12  sing N N 265 
PGE O1  HO1  sing N N 266 
PGE C2  O2   sing N N 267 
PGE C2  H2   sing N N 268 
PGE C2  H22  sing N N 269 
PGE O2  C3   sing N N 270 
PGE C3  C4   sing N N 271 
PGE C3  H3   sing N N 272 
PGE C3  H32  sing N N 273 
PGE C4  O3   sing N N 274 
PGE C4  H4   sing N N 275 
PGE C4  H42  sing N N 276 
PGE O4  C6   sing N N 277 
PGE O4  HO4  sing N N 278 
PGE C6  C5   sing N N 279 
PGE C6  H6   sing N N 280 
PGE C6  H62  sing N N 281 
PGE C5  O3   sing N N 282 
PGE C5  H5   sing N N 283 
PGE C5  H52  sing N N 284 
PHE N   CA   sing N N 285 
PHE N   H    sing N N 286 
PHE N   H2   sing N N 287 
PHE CA  C    sing N N 288 
PHE CA  CB   sing N N 289 
PHE CA  HA   sing N N 290 
PHE C   O    doub N N 291 
PHE C   OXT  sing N N 292 
PHE CB  CG   sing N N 293 
PHE CB  HB2  sing N N 294 
PHE CB  HB3  sing N N 295 
PHE CG  CD1  doub Y N 296 
PHE CG  CD2  sing Y N 297 
PHE CD1 CE1  sing Y N 298 
PHE CD1 HD1  sing N N 299 
PHE CD2 CE2  doub Y N 300 
PHE CD2 HD2  sing N N 301 
PHE CE1 CZ   doub Y N 302 
PHE CE1 HE1  sing N N 303 
PHE CE2 CZ   sing Y N 304 
PHE CE2 HE2  sing N N 305 
PHE CZ  HZ   sing N N 306 
PHE OXT HXT  sing N N 307 
PRO N   CA   sing N N 308 
PRO N   CD   sing N N 309 
PRO N   H    sing N N 310 
PRO CA  C    sing N N 311 
PRO CA  CB   sing N N 312 
PRO CA  HA   sing N N 313 
PRO C   O    doub N N 314 
PRO C   OXT  sing N N 315 
PRO CB  CG   sing N N 316 
PRO CB  HB2  sing N N 317 
PRO CB  HB3  sing N N 318 
PRO CG  CD   sing N N 319 
PRO CG  HG2  sing N N 320 
PRO CG  HG3  sing N N 321 
PRO CD  HD2  sing N N 322 
PRO CD  HD3  sing N N 323 
PRO OXT HXT  sing N N 324 
SER N   CA   sing N N 325 
SER N   H    sing N N 326 
SER N   H2   sing N N 327 
SER CA  C    sing N N 328 
SER CA  CB   sing N N 329 
SER CA  HA   sing N N 330 
SER C   O    doub N N 331 
SER C   OXT  sing N N 332 
SER CB  OG   sing N N 333 
SER CB  HB2  sing N N 334 
SER CB  HB3  sing N N 335 
SER OG  HG   sing N N 336 
SER OXT HXT  sing N N 337 
THR N   CA   sing N N 338 
THR N   H    sing N N 339 
THR N   H2   sing N N 340 
THR CA  C    sing N N 341 
THR CA  CB   sing N N 342 
THR CA  HA   sing N N 343 
THR C   O    doub N N 344 
THR C   OXT  sing N N 345 
THR CB  OG1  sing N N 346 
THR CB  CG2  sing N N 347 
THR CB  HB   sing N N 348 
THR OG1 HG1  sing N N 349 
THR CG2 HG21 sing N N 350 
THR CG2 HG22 sing N N 351 
THR CG2 HG23 sing N N 352 
THR OXT HXT  sing N N 353 
TRP N   CA   sing N N 354 
TRP N   H    sing N N 355 
TRP N   H2   sing N N 356 
TRP CA  C    sing N N 357 
TRP CA  CB   sing N N 358 
TRP CA  HA   sing N N 359 
TRP C   O    doub N N 360 
TRP C   OXT  sing N N 361 
TRP CB  CG   sing N N 362 
TRP CB  HB2  sing N N 363 
TRP CB  HB3  sing N N 364 
TRP CG  CD1  doub Y N 365 
TRP CG  CD2  sing Y N 366 
TRP CD1 NE1  sing Y N 367 
TRP CD1 HD1  sing N N 368 
TRP CD2 CE2  doub Y N 369 
TRP CD2 CE3  sing Y N 370 
TRP NE1 CE2  sing Y N 371 
TRP NE1 HE1  sing N N 372 
TRP CE2 CZ2  sing Y N 373 
TRP CE3 CZ3  doub Y N 374 
TRP CE3 HE3  sing N N 375 
TRP CZ2 CH2  doub Y N 376 
TRP CZ2 HZ2  sing N N 377 
TRP CZ3 CH2  sing Y N 378 
TRP CZ3 HZ3  sing N N 379 
TRP CH2 HH2  sing N N 380 
TRP OXT HXT  sing N N 381 
TYR N   CA   sing N N 382 
TYR N   H    sing N N 383 
TYR N   H2   sing N N 384 
TYR CA  C    sing N N 385 
TYR CA  CB   sing N N 386 
TYR CA  HA   sing N N 387 
TYR C   O    doub N N 388 
TYR C   OXT  sing N N 389 
TYR CB  CG   sing N N 390 
TYR CB  HB2  sing N N 391 
TYR CB  HB3  sing N N 392 
TYR CG  CD1  doub Y N 393 
TYR CG  CD2  sing Y N 394 
TYR CD1 CE1  sing Y N 395 
TYR CD1 HD1  sing N N 396 
TYR CD2 CE2  doub Y N 397 
TYR CD2 HD2  sing N N 398 
TYR CE1 CZ   doub Y N 399 
TYR CE1 HE1  sing N N 400 
TYR CE2 CZ   sing Y N 401 
TYR CE2 HE2  sing N N 402 
TYR CZ  OH   sing N N 403 
TYR OH  HH   sing N N 404 
TYR OXT HXT  sing N N 405 
VAL N   CA   sing N N 406 
VAL N   H    sing N N 407 
VAL N   H2   sing N N 408 
VAL CA  C    sing N N 409 
VAL CA  CB   sing N N 410 
VAL CA  HA   sing N N 411 
VAL C   O    doub N N 412 
VAL C   OXT  sing N N 413 
VAL CB  CG1  sing N N 414 
VAL CB  CG2  sing N N 415 
VAL CB  HB   sing N N 416 
VAL CG1 HG11 sing N N 417 
VAL CG1 HG12 sing N N 418 
VAL CG1 HG13 sing N N 419 
VAL CG2 HG21 sing N N 420 
VAL CG2 HG22 sing N N 421 
VAL CG2 HG23 sing N N 422 
VAL OXT HXT  sing N N 423 
W5K C17 C16  sing N N 424 
W5K C17 O18  sing N N 425 
W5K C16 N15  sing N N 426 
W5K C22 C23  doub Y N 427 
W5K C22 C21  sing Y N 428 
W5K C23 C24  sing Y N 429 
W5K C21 C20  doub Y N 430 
W5K C24 F25  sing N N 431 
W5K C24 C19  doub Y N 432 
W5K N15 C14  sing N N 433 
W5K C20 C19  sing Y N 434 
W5K C13 C14  doub Y N 435 
W5K C13 C12  sing Y N 436 
W5K C19 C12  sing N N 437 
W5K C14 C9   sing Y N 438 
W5K C12 C11  doub Y N 439 
W5K C2  C1   sing N N 440 
W5K C2  C3   sing N N 441 
W5K C9  C3   sing N N 442 
W5K C9  C10  doub Y N 443 
W5K C11 C10  sing Y N 444 
W5K C3  O4   sing N N 445 
W5K O4  C5   sing N N 446 
W5K C6  C5   sing N N 447 
W5K C5  C7   sing N N 448 
W5K O8  C7   sing N N 449 
W5K C1  H29  sing N N 450 
W5K C1  H28  sing N N 451 
W5K C1  H30  sing N N 452 
W5K C2  H32  sing N N 453 
W5K C2  H31  sing N N 454 
W5K C3  H26  sing N N 455 
W5K C5  H27  sing N N 456 
W5K C6  H35  sing N N 457 
W5K C6  H34  sing N N 458 
W5K C6  H33  sing N N 459 
W5K C7  H37  sing N N 460 
W5K C7  H36  sing N N 461 
W5K C10 H39  sing N N 462 
W5K C11 H40  sing N N 463 
W5K C13 H41  sing N N 464 
W5K C16 H43  sing N N 465 
W5K C16 H44  sing N N 466 
W5K C21 H49  sing N N 467 
W5K C22 H50  sing N N 468 
W5K C23 H51  sing N N 469 
W5K O8  H38  sing N N 470 
W5K N15 H42  sing N N 471 
W5K C17 H46  sing N N 472 
W5K C17 H45  sing N N 473 
W5K O18 H47  sing N N 474 
W5K C20 H48  sing N N 475 
# 
_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                    8QM7 
_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]   0.021206 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002105 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014467 
_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]   0.015596 
_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   . GLY A 1 8   ? 0.547   -23.466 -11.439 1.00 58.94  ? 10  GLY A N   1 
ATOM   2    C CA  . GLY A 1 8   ? 0.811   -23.624 -10.011 1.00 59.68  ? 10  GLY A CA  1 
ATOM   3    C C   . GLY A 1 8   ? 2.276   -23.377 -9.714  1.00 59.62  ? 10  GLY A C   1 
ATOM   4    O O   . GLY A 1 8   ? 2.997   -24.285 -9.269  1.00 60.98  ? 10  GLY A O   1 
ATOM   5    N N   . ALA A 1 9   ? 2.718   -22.131 -9.951  1.00 56.78  ? 11  ALA A N   1 
ATOM   6    C CA  . ALA A 1 9   ? 4.126   -21.870 -10.233 1.00 54.17  ? 11  ALA A CA  1 
ATOM   7    C C   . ALA A 1 9   ? 4.813   -21.095 -9.093  1.00 51.53  ? 11  ALA A C   1 
ATOM   8    O O   . ALA A 1 9   ? 4.146   -20.449 -8.285  1.00 51.82  ? 11  ALA A O   1 
ATOM   9    C CB  . ALA A 1 9   ? 4.238   -21.094 -11.539 1.00 53.55  ? 11  ALA A CB  1 
ATOM   10   N N   . ARG A 1 10  ? 6.164   -21.157 -9.041  1.00 48.21  ? 12  ARG A N   1 
ATOM   11   C CA  . ARG A 1 10  ? 6.945   -20.398 -8.065  1.00 45.33  ? 12  ARG A CA  1 
ATOM   12   C C   . ARG A 1 10  ? 6.647   -18.897 -8.199  1.00 41.48  ? 12  ARG A C   1 
ATOM   13   O O   . ARG A 1 10  ? 6.507   -18.399 -9.308  1.00 40.88  ? 12  ARG A O   1 
ATOM   14   C CB  . ARG A 1 10  ? 8.449   -20.679 -8.252  1.00 46.72  ? 12  ARG A CB  1 
ATOM   15   C CG  . ARG A 1 10  ? 9.350   -20.135 -7.119  1.00 50.64  ? 12  ARG A CG  1 
ATOM   16   C CD  . ARG A 1 10  ? 10.811  -20.413 -7.377  1.00 55.35  ? 12  ARG A CD  1 
ATOM   17   N NE  . ARG A 1 10  ? 11.044  -21.844 -7.497  1.00 60.57  ? 12  ARG A NE  1 
ATOM   18   C CZ  . ARG A 1 10  ? 11.191  -22.684 -6.475  1.00 61.58  ? 12  ARG A CZ  1 
ATOM   19   N NH1 . ARG A 1 10  ? 11.136  -22.235 -5.217  1.00 58.64  ? 12  ARG A NH1 1 
ATOM   20   N NH2 . ARG A 1 10  ? 11.388  -23.977 -6.700  1.00 61.45  ? 12  ARG A NH2 1 
ATOM   21   N N   . ILE A 1 11  ? 6.518   -18.209 -7.075  1.00 39.13  ? 13  ILE A N   1 
ATOM   22   C CA  . ILE A 1 11  ? 6.384   -16.755 -7.022  1.00 37.82  ? 13  ILE A CA  1 
ATOM   23   C C   . ILE A 1 11  ? 7.780   -16.115 -7.017  1.00 36.63  ? 13  ILE A C   1 
ATOM   24   O O   . ILE A 1 11  ? 8.549   -16.246 -6.058  1.00 36.75  ? 13  ILE A O   1 
ATOM   25   C CB  . ILE A 1 11  ? 5.572   -16.316 -5.793  1.00 37.62  ? 13  ILE A CB  1 
ATOM   26   C CG1 . ILE A 1 11  ? 4.252   -17.117 -5.684  1.00 38.17  ? 13  ILE A CG1 1 
ATOM   27   C CG2 . ILE A 1 11  ? 5.305   -14.837 -5.857  1.00 36.61  ? 13  ILE A CG2 1 
ATOM   28   C CD1 . ILE A 1 11  ? 3.387   -16.694 -4.515  1.00 38.31  ? 13  ILE A CD1 1 
ATOM   29   N N   . ILE A 1 12  ? 8.092   -15.407 -8.098  1.00 35.31  ? 14  ILE A N   1 
ATOM   30   C CA  . ILE A 1 12  ? 9.389   -14.833 -8.303  1.00 35.15  ? 14  ILE A CA  1 
ATOM   31   C C   . ILE A 1 12  ? 9.218   -13.356 -8.512  1.00 35.12  ? 14  ILE A C   1 
ATOM   32   O O   . ILE A 1 12  ? 8.430   -12.932 -9.358  1.00 34.22  ? 14  ILE A O   1 
ATOM   33   C CB  . ILE A 1 12  ? 10.070  -15.516 -9.518  1.00 36.21  ? 14  ILE A CB  1 
ATOM   34   C CG1 . ILE A 1 12  ? 10.109  -17.077 -9.320  1.00 37.32  ? 14  ILE A CG1 1 
ATOM   35   C CG2 . ILE A 1 12  ? 11.481  -14.902 -9.752  1.00 36.59  ? 14  ILE A CG2 1 
ATOM   36   C CD1 . ILE A 1 12  ? 10.746  -17.784 -10.320 1.00 39.46  ? 14  ILE A CD1 1 
ATOM   37   N N   . TYR A 1 13  ? 9.969   -12.556 -7.751  1.00 35.87  ? 15  TYR A N   1 
ATOM   38   C CA  . TYR A 1 13  ? 10.008  -11.120 -7.936  1.00 36.60  ? 15  TYR A CA  1 
ATOM   39   C C   . TYR A 1 13  ? 11.405  -10.703 -8.289  1.00 38.11  ? 15  TYR A C   1 
ATOM   40   O O   . TYR A 1 13  ? 12.353  -11.050 -7.561  1.00 39.43  ? 15  TYR A O   1 
ATOM   41   C CB  . TYR A 1 13  ? 9.627   -10.418 -6.660  1.00 36.70  ? 15  TYR A CB  1 
ATOM   42   C CG  . TYR A 1 13  ? 8.245   -10.747 -6.196  1.00 38.58  ? 15  TYR A CG  1 
ATOM   43   C CD1 . TYR A 1 13  ? 7.137   -10.224 -6.840  1.00 40.79  ? 15  TYR A CD1 1 
ATOM   44   C CD2 . TYR A 1 13  ? 8.036   -11.567 -5.104  1.00 39.58  ? 15  TYR A CD2 1 
ATOM   45   C CE1 . TYR A 1 13  ? 5.854   -10.486 -6.395  1.00 41.06  ? 15  TYR A CE1 1 
ATOM   46   C CE2 . TYR A 1 13  ? 6.760   -11.848 -4.654  1.00 40.10  ? 15  TYR A CE2 1 
ATOM   47   C CZ  . TYR A 1 13  ? 5.667   -11.302 -5.307  1.00 40.62  ? 15  TYR A CZ  1 
ATOM   48   O OH  . TYR A 1 13  ? 4.395   -11.576 -4.915  1.00 39.52  ? 15  TYR A OH  1 
ATOM   49   N N   . ASP A 1 14  ? 11.556  -9.985  -9.390  1.00 37.38  ? 16  ASP A N   1 
ATOM   50   C CA  . ASP A 1 14  ? 12.824  -9.341  -9.669  1.00 38.65  ? 16  ASP A CA  1 
ATOM   51   C C   . ASP A 1 14  ? 13.020  -8.119  -8.761  1.00 37.49  ? 16  ASP A C   1 
ATOM   52   O O   . ASP A 1 14  ? 12.106  -7.663  -8.071  1.00 36.45  ? 16  ASP A O   1 
ATOM   53   C CB  . ASP A 1 14  ? 13.015  -9.020  -11.179 1.00 41.99  ? 16  ASP A CB  1 
ATOM   54   C CG  . ASP A 1 14  ? 12.076  -7.982  -11.736 1.00 46.63  ? 16  ASP A CG  1 
ATOM   55   O OD1 . ASP A 1 14  ? 11.570  -7.168  -10.951 1.00 48.16  ? 16  ASP A OD1 1 
ATOM   56   O OD2 . ASP A 1 14  ? 11.848  -7.991  -12.960 1.00 49.27  ? 16  ASP A OD2 1 
ATOM   57   N N   . ARG A 1 15  ? 14.239  -7.611  -8.770  1.00 37.45  ? 17  ARG A N   1 
ATOM   58   C CA  . ARG A 1 15  ? 14.635  -6.463  -7.966  1.00 37.95  ? 17  ARG A CA  1 
ATOM   59   C C   . ARG A 1 15  ? 13.743  -5.249  -8.204  1.00 40.12  ? 17  ARG A C   1 
ATOM   60   O O   . ARG A 1 15  ? 13.296  -4.642  -7.237  1.00 40.49  ? 17  ARG A O   1 
ATOM   61   C CB  . ARG A 1 15  ? 16.084  -6.102  -8.272  1.00 36.67  ? 17  ARG A CB  1 
ATOM   62   C CG  . ARG A 1 15  ? 16.622  -5.046  -7.354  1.00 37.42  ? 17  ARG A CG  1 
ATOM   63   C CD  . ARG A 1 15  ? 18.058  -4.778  -7.709  1.00 38.78  ? 17  ARG A CD  1 
ATOM   64   N NE  . ARG A 1 15  ? 18.639  -3.715  -6.899  1.00 44.82  ? 17  ARG A NE  1 
ATOM   65   C CZ  . ARG A 1 15  ? 18.433  -2.416  -7.076  1.00 48.28  ? 17  ARG A CZ  1 
ATOM   66   N NH1 . ARG A 1 15  ? 17.620  -1.988  -8.046  1.00 47.20  ? 17  ARG A NH1 1 
ATOM   67   N NH2 . ARG A 1 15  ? 19.023  -1.532  -6.278  1.00 49.75  ? 17  ARG A NH2 1 
ATOM   68   N N   . ALA A 1 16  ? 13.471  -4.914  -9.484  1.00 41.16  ? 18  ALA A N   1 
ATOM   69   C CA  . ALA A 1 16  ? 12.657  -3.760  -9.825  1.00 42.86  ? 18  ALA A CA  1 
ATOM   70   C C   . ALA A 1 16  ? 11.258  -3.817  -9.249  1.00 44.55  ? 18  ALA A C   1 
ATOM   71   O O   . ALA A 1 16  ? 10.769  -2.800  -8.770  1.00 46.56  ? 18  ALA A O   1 
ATOM   72   C CB  . ALA A 1 16  ? 12.573  -3.619  -11.323 1.00 43.36  ? 18  ALA A CB  1 
ATOM   73   N N   . PHE A 1 17  ? 10.601  -4.986  -9.292  1.00 44.24  ? 19  PHE A N   1 
ATOM   74   C CA  . PHE A 1 17  ? 9.267   -5.126  -8.755  1.00 45.06  ? 19  PHE A CA  1 
ATOM   75   C C   . PHE A 1 17  ? 9.260   -4.922  -7.239  1.00 44.35  ? 19  PHE A C   1 
ATOM   76   O O   . PHE A 1 17  ? 8.393   -4.227  -6.732  1.00 44.31  ? 19  PHE A O   1 
ATOM   77   C CB  . PHE A 1 17  ? 8.683   -6.486  -9.147  1.00 46.41  ? 19  PHE A CB  1 
ATOM   78   C CG  . PHE A 1 17  ? 7.223   -6.581  -8.826  1.00 49.40  ? 19  PHE A CG  1 
ATOM   79   C CD1 . PHE A 1 17  ? 6.797   -7.019  -7.585  1.00 50.02  ? 19  PHE A CD1 1 
ATOM   80   C CD2 . PHE A 1 17  ? 6.269   -6.154  -9.733  1.00 51.57  ? 19  PHE A CD2 1 
ATOM   81   C CE1 . PHE A 1 17  ? 5.455   -7.033  -7.261  1.00 50.65  ? 19  PHE A CE1 1 
ATOM   82   C CE2 . PHE A 1 17  ? 4.924   -6.204  -9.409  1.00 51.71  ? 19  PHE A CE2 1 
ATOM   83   C CZ  . PHE A 1 17  ? 4.533   -6.648  -8.178  1.00 50.70  ? 19  PHE A CZ  1 
ATOM   84   N N   . LEU A 1 18  ? 10.218  -5.520  -6.508  1.00 43.31  ? 20  LEU A N   1 
ATOM   85   C CA  . LEU A 1 18  ? 10.275  -5.380  -5.052  1.00 42.09  ? 20  LEU A CA  1 
ATOM   86   C C   . LEU A 1 18  ? 10.517  -3.931  -4.630  1.00 42.36  ? 20  LEU A C   1 
ATOM   87   O O   . LEU A 1 18  ? 9.932   -3.479  -3.660  1.00 42.32  ? 20  LEU A O   1 
ATOM   88   C CB  . LEU A 1 18  ? 11.347  -6.311  -4.436  1.00 40.70  ? 20  LEU A CB  1 
ATOM   89   C CG  . LEU A 1 18  ? 11.127  -7.824  -4.604  1.00 40.83  ? 20  LEU A CG  1 
ATOM   90   C CD1 . LEU A 1 18  ? 12.332  -8.628  -4.118  1.00 41.18  ? 20  LEU A CD1 1 
ATOM   91   C CD2 . LEU A 1 18  ? 9.913   -8.277  -3.903  1.00 40.89  ? 20  LEU A CD2 1 
ATOM   92   N N   . MET A 1 19  ? 11.380  -3.215  -5.330  1.00 43.61  ? 21  MET A N   1 
ATOM   93   C CA  . MET A 1 19  ? 11.616  -1.789  -5.042  1.00 45.62  ? 21  MET A CA  1 
ATOM   94   C C   . MET A 1 19  ? 10.373  -0.914  -5.287  1.00 49.21  ? 21  MET A C   1 
ATOM   95   O O   . MET A 1 19  ? 10.090  -0.040  -4.492  1.00 49.08  ? 21  MET A O   1 
ATOM   96   C CB  . MET A 1 19  ? 12.754  -1.264  -5.882  1.00 43.93  ? 21  MET A CB  1 
ATOM   97   C CG  . MET A 1 19  ? 14.067  -1.860  -5.580  1.00 44.99  ? 21  MET A CG  1 
ATOM   98   S SD  . MET A 1 19  ? 14.610  -1.676  -3.873  1.00 48.98  ? 21  MET A SD  1 
ATOM   99   C CE  . MET A 1 19  ? 16.344  -1.943  -4.090  1.00 52.94  ? 21  MET A CE  1 
ATOM   100  N N   . ALA A 1 20  ? 9.640   -1.155  -6.379  1.00 51.73  ? 22  ALA A N   1 
ATOM   101  C CA  . ALA A 1 20  ? 8.356   -0.492  -6.651  1.00 53.09  ? 22  ALA A CA  1 
ATOM   102  C C   . ALA A 1 20  ? 7.314   -0.715  -5.540  1.00 55.05  ? 22  ALA A C   1 
ATOM   103  O O   . ALA A 1 20  ? 6.531   0.186   -5.255  1.00 55.65  ? 22  ALA A O   1 
ATOM   104  C CB  . ALA A 1 20  ? 7.798   -1.001  -7.971  1.00 52.72  ? 22  ALA A CB  1 
ATOM   105  N N   . CYS A 1 21  ? 7.292   -1.926  -4.909  1.00 55.57  ? 23  CYS A N   1 
ATOM   106  C CA  . CYS A 1 21  ? 6.370   -2.264  -3.805  1.00 55.59  ? 23  CYS A CA  1 
ATOM   107  C C   . CYS A 1 21  ? 6.764   -1.626  -2.429  1.00 55.39  ? 23  CYS A C   1 
ATOM   108  O O   . CYS A 1 21  ? 6.220   -2.038  -1.389  1.00 56.19  ? 23  CYS A O   1 
ATOM   109  C CB  . CYS A 1 21  ? 6.251   -3.780  -3.665  1.00 56.41  ? 23  CYS A CB  1 
ATOM   110  S SG  . CYS A 1 21  ? 5.598   -4.652  -5.116  1.00 61.02  ? 23  CYS A SG  1 
ATOM   111  N N   . ARG A 1 22  ? 7.684   -0.665  -2.413  1.00 54.89  ? 24  ARG A N   1 
ATOM   112  C CA  . ARG A 1 22  ? 8.257   -0.115  -1.190  1.00 56.10  ? 24  ARG A CA  1 
ATOM   113  C C   . ARG A 1 22  ? 7.646   1.247   -0.867  1.00 61.51  ? 24  ARG A C   1 
ATOM   114  O O   . ARG A 1 22  ? 7.456   2.071   -1.790  1.00 61.58  ? 24  ARG A O   1 
ATOM   115  C CB  . ARG A 1 22  ? 9.777   0.116   -1.365  1.00 51.95  ? 24  ARG A CB  1 
ATOM   116  C CG  . ARG A 1 22  ? 10.441  0.603   -0.133  1.00 48.80  ? 24  ARG A CG  1 
ATOM   117  C CD  . ARG A 1 22  ? 11.870  0.948   -0.411  1.00 50.15  ? 24  ARG A CD  1 
ATOM   118  N NE  . ARG A 1 22  ? 12.587  1.327   0.819   1.00 48.66  ? 24  ARG A NE  1 
ATOM   119  C CZ  . ARG A 1 22  ? 13.905  1.248   0.998   1.00 47.56  ? 24  ARG A CZ  1 
ATOM   120  N NH1 . ARG A 1 22  ? 14.697  0.810   0.021   1.00 44.54  ? 24  ARG A NH1 1 
ATOM   121  N NH2 . ARG A 1 22  ? 14.444  1.607   2.151   1.00 50.84  ? 24  ARG A NH2 1 
ATOM   122  N N   . GLY A 1 23  ? 7.400   1.477   0.434   1.00 64.58  ? 25  GLY A N   1 
ATOM   123  C CA  . GLY A 1 23  ? 7.039   2.793   0.957   1.00 67.79  ? 25  GLY A CA  1 
ATOM   124  C C   . GLY A 1 23  ? 5.540   2.917   1.185   1.00 70.64  ? 25  GLY A C   1 
ATOM   125  O O   . GLY A 1 23  ? 4.940   3.950   0.849   1.00 71.34  ? 25  GLY A O   1 
ATOM   126  N N   . GLY A 1 24  ? 4.949   1.866   1.765   1.00 71.86  ? 26  GLY A N   1 
ATOM   127  C CA  . GLY A 1 24  ? 3.518   1.789   2.032   1.00 73.54  ? 26  GLY A CA  1 
ATOM   128  C C   . GLY A 1 24  ? 2.689   1.897   0.772   1.00 75.41  ? 26  GLY A C   1 
ATOM   129  O O   . GLY A 1 24  ? 3.124   1.471   -0.306  1.00 75.77  ? 26  GLY A O   1 
ATOM   130  N N   . GLY A 1 25  ? 1.496   2.462   0.926   1.00 76.54  ? 27  GLY A N   1 
ATOM   131  C CA  . GLY A 1 25  ? 0.658   2.901   -0.186  1.00 77.49  ? 27  GLY A CA  1 
ATOM   132  C C   . GLY A 1 25  ? -0.563  2.041   -0.362  1.00 78.26  ? 27  GLY A C   1 
ATOM   133  O O   . GLY A 1 25  ? -1.687  2.547   -0.385  1.00 79.36  ? 27  GLY A O   1 
ATOM   134  N N   . GLY A 1 26  ? -0.337  0.739   -0.479  1.00 77.98  ? 28  GLY A N   1 
ATOM   135  C CA  . GLY A 1 26  ? -1.385  -0.240  -0.732  1.00 78.00  ? 28  GLY A CA  1 
ATOM   136  C C   . GLY A 1 26  ? -2.515  -0.210  0.275   1.00 77.73  ? 28  GLY A C   1 
ATOM   137  O O   . GLY A 1 26  ? -2.288  -0.375  1.479   1.00 78.34  ? 28  GLY A O   1 
ATOM   138  N N   . GLU A 1 27  ? -3.745  0.015   -0.215  1.00 76.38  ? 29  GLU A N   1 
ATOM   139  C CA  . GLU A 1 27  ? -4.954  -0.065  0.606   1.00 74.59  ? 29  GLU A CA  1 
ATOM   140  C C   . GLU A 1 27  ? -5.129  -1.480  1.196   1.00 71.55  ? 29  GLU A C   1 
ATOM   141  O O   . GLU A 1 27  ? -5.610  -1.609  2.318   1.00 72.48  ? 29  GLU A O   1 
ATOM   142  C CB  . GLU A 1 27  ? -6.200  0.326   -0.232  1.00 78.17  ? 29  GLU A CB  1 
ATOM   143  C CG  . GLU A 1 27  ? -6.359  1.819   -0.510  1.00 84.01  ? 29  GLU A CG  1 
ATOM   144  C CD  . GLU A 1 27  ? -7.728  2.248   -1.036  1.00 92.86  ? 29  GLU A CD  1 
ATOM   145  O OE1 . GLU A 1 27  ? -8.742  2.009   -0.337  1.00 94.49  ? 29  GLU A OE1 1 
ATOM   146  O OE2 . GLU A 1 27  ? -7.790  2.834   -2.145  1.00 95.41  ? 29  GLU A OE2 1 
ATOM   147  N N   . ASN A 1 28  ? -4.722  -2.535  0.444   1.00 67.63  ? 30  ASN A N   1 
ATOM   148  C CA  . ASN A 1 28  ? -4.920  -3.953  0.770   1.00 63.14  ? 30  ASN A CA  1 
ATOM   149  C C   . ASN A 1 28  ? -6.387  -4.309  0.916   1.00 61.58  ? 30  ASN A C   1 
ATOM   150  O O   . ASN A 1 28  ? -6.811  -4.951  1.897   1.00 61.41  ? 30  ASN A O   1 
ATOM   151  C CB  . ASN A 1 28  ? -4.102  -4.434  1.981   1.00 60.09  ? 30  ASN A CB  1 
ATOM   152  C CG  . ASN A 1 28  ? -4.080  -5.959  2.118   1.00 57.43  ? 30  ASN A CG  1 
ATOM   153  O OD1 . ASN A 1 28  ? -4.096  -6.716  1.129   1.00 54.64  ? 30  ASN A OD1 1 
ATOM   154  N ND2 . ASN A 1 28  ? -4.048  -6.453  3.345   1.00 57.92  ? 30  ASN A ND2 1 
ATOM   155  N N   . LEU A 1 29  ? -7.167  -3.924  -0.092  1.00 60.28  ? 31  LEU A N   1 
ATOM   156  C CA  . LEU A 1 29  ? -8.591  -4.256  -0.115  1.00 59.02  ? 31  LEU A CA  1 
ATOM   157  C C   . LEU A 1 29  ? -8.781  -5.753  -0.190  1.00 57.42  ? 31  LEU A C   1 
ATOM   158  O O   . LEU A 1 29  ? -8.012  -6.450  -0.871  1.00 57.79  ? 31  LEU A O   1 
ATOM   159  C CB  . LEU A 1 29  ? -9.331  -3.577  -1.282  1.00 59.81  ? 31  LEU A CB  1 
ATOM   160  C CG  . LEU A 1 29  ? -9.175  -2.083  -1.433  1.00 62.57  ? 31  LEU A CG  1 
ATOM   161  C CD1 . LEU A 1 29  ? -10.030 -1.594  -2.588  1.00 64.21  ? 31  LEU A CD1 1 
ATOM   162  C CD2 . LEU A 1 29  ? -9.547  -1.360  -0.161  1.00 63.12  ? 31  LEU A CD2 1 
ATOM   163  N N   . TYR A 1 30  ? -9.817  -6.243  0.526   1.00 55.37  ? 32  TYR A N   1 
ATOM   164  C CA  . TYR A 1 30  ? -10.180 -7.649  0.673   1.00 53.89  ? 32  TYR A CA  1 
ATOM   165  C C   . TYR A 1 30  ? -9.052  -8.511  1.255   1.00 52.69  ? 32  TYR A C   1 
ATOM   166  O O   . TYR A 1 30  ? -9.152  -9.684  1.112   1.00 51.64  ? 32  TYR A O   1 
ATOM   167  C CB  . TYR A 1 30  ? -10.714 -8.233  -0.669  1.00 53.55  ? 32  TYR A CB  1 
ATOM   168  C CG  . TYR A 1 30  ? -11.715 -7.307  -1.336  1.00 53.32  ? 32  TYR A CG  1 
ATOM   169  C CD1 . TYR A 1 30  ? -13.060 -7.352  -1.006  1.00 53.87  ? 32  TYR A CD1 1 
ATOM   170  C CD2 . TYR A 1 30  ? -11.302 -6.338  -2.239  1.00 53.59  ? 32  TYR A CD2 1 
ATOM   171  C CE1 . TYR A 1 30  ? -13.977 -6.491  -1.596  1.00 54.10  ? 32  TYR A CE1 1 
ATOM   172  C CE2 . TYR A 1 30  ? -12.206 -5.462  -2.823  1.00 54.68  ? 32  TYR A CE2 1 
ATOM   173  C CZ  . TYR A 1 30  ? -13.546 -5.532  -2.487  1.00 55.14  ? 32  TYR A CZ  1 
ATOM   174  O OH  . TYR A 1 30  ? -14.452 -4.656  -3.049  1.00 56.99  ? 32  TYR A OH  1 
ATOM   175  N N   . PHE A 1 31  ? -7.993  -7.939  1.918   1.00 53.00  ? 33  PHE A N   1 
ATOM   176  C CA  . PHE A 1 31  ? -6.753  -8.660  2.303   1.00 53.88  ? 33  PHE A CA  1 
ATOM   177  C C   . PHE A 1 31  ? -6.150  -9.385  1.091   1.00 54.59  ? 33  PHE A C   1 
ATOM   178  O O   . PHE A 1 31  ? -5.592  -10.476 1.231   1.00 54.38  ? 33  PHE A O   1 
ATOM   179  C CB  . PHE A 1 31  ? -6.980  -9.621  3.493   1.00 53.97  ? 33  PHE A CB  1 
ATOM   180  C CG  . PHE A 1 31  ? -7.423  -8.873  4.727   1.00 54.67  ? 33  PHE A CG  1 
ATOM   181  C CD1 . PHE A 1 31  ? -6.518  -8.134  5.473   1.00 54.67  ? 33  PHE A CD1 1 
ATOM   182  C CD2 . PHE A 1 31  ? -8.754  -8.857  5.107   1.00 54.97  ? 33  PHE A CD2 1 
ATOM   183  C CE1 . PHE A 1 31  ? -6.935  -7.416  6.580   1.00 54.77  ? 33  PHE A CE1 1 
ATOM   184  C CE2 . PHE A 1 31  ? -9.163  -8.121  6.203   1.00 55.29  ? 33  PHE A CE2 1 
ATOM   185  C CZ  . PHE A 1 31  ? -8.249  -7.422  6.941   1.00 55.09  ? 33  PHE A CZ  1 
ATOM   186  N N   . GLN A 1 32  ? -6.283  -8.760  -0.112  1.00 54.78  ? 34  GLN A N   1 
ATOM   187  C CA  . GLN A 1 32  ? -5.888  -9.358  -1.400  1.00 54.20  ? 34  GLN A CA  1 
ATOM   188  C C   . GLN A 1 32  ? -5.060  -8.464  -2.274  1.00 52.36  ? 34  GLN A C   1 
ATOM   189  O O   . GLN A 1 32  ? -4.824  -8.832  -3.417  1.00 52.64  ? 34  GLN A O   1 
ATOM   190  C CB  . GLN A 1 32  ? -7.146  -9.808  -2.190  1.00 55.09  ? 34  GLN A CB  1 
ATOM   191  C CG  . GLN A 1 32  ? -7.821  -11.005 -1.577  1.00 56.59  ? 34  GLN A CG  1 
ATOM   192  C CD  . GLN A 1 32  ? -8.880  -11.559 -2.481  1.00 63.63  ? 34  GLN A CD  1 
ATOM   193  O OE1 . GLN A 1 32  ? -8.600  -12.024 -3.595  1.00 66.14  ? 34  GLN A OE1 1 
ATOM   194  N NE2 . GLN A 1 32  ? -10.128 -11.539 -2.026  1.00 65.03  ? 34  GLN A NE2 1 
ATOM   195  N N   . GLY A 1 33  ? -4.618  -7.326  -1.758  1.00 51.09  ? 35  GLY A N   1 
ATOM   196  C CA  . GLY A 1 33  ? -3.828  -6.367  -2.511  1.00 50.50  ? 35  GLY A CA  1 
ATOM   197  C C   . GLY A 1 33  ? -2.335  -6.406  -2.193  1.00 50.09  ? 35  GLY A C   1 
ATOM   198  O O   . GLY A 1 33  ? -1.559  -5.690  -2.827  1.00 50.39  ? 35  GLY A O   1 
ATOM   199  N N   . LYS A 1 34  ? -1.930  -7.211  -1.211  1.00 48.07  ? 36  LYS A N   1 
ATOM   200  C CA  . LYS A 1 34  ? -0.536  -7.450  -0.863  1.00 47.06  ? 36  LYS A CA  1 
ATOM   201  C C   . LYS A 1 34  ? 0.029   -8.582  -1.728  1.00 46.76  ? 36  LYS A C   1 
ATOM   202  O O   . LYS A 1 34  ? -0.723  -9.476  -2.163  1.00 47.07  ? 36  LYS A O   1 
ATOM   203  C CB  . LYS A 1 34  ? -0.401  -7.851  0.628   1.00 47.13  ? 36  LYS A CB  1 
ATOM   204  C CG  . LYS A 1 34  ? -0.409  -6.657  1.574   1.00 46.11  ? 36  LYS A CG  1 
ATOM   205  C CD  . LYS A 1 34  ? -0.377  -7.107  3.029   1.00 48.67  ? 36  LYS A CD  1 
ATOM   206  C CE  . LYS A 1 34  ? -0.153  -5.936  3.965   1.00 50.35  ? 36  LYS A CE  1 
ATOM   207  N NZ  . LYS A 1 34  ? -0.268  -6.320  5.392   1.00 50.96  ? 36  LYS A NZ  1 
ATOM   208  N N   . HIS A 1 35  ? 1.358   -8.546  -1.962  1.00 44.60  ? 37  HIS A N   1 
ATOM   209  C CA  . HIS A 1 35  ? 2.044   -9.446  -2.887  1.00 43.76  ? 37  HIS A CA  1 
ATOM   210  C C   . HIS A 1 35  ? 2.677   -10.600 -2.149  1.00 41.58  ? 37  HIS A C   1 
ATOM   211  O O   . HIS A 1 35  ? 3.692   -10.408 -1.482  1.00 41.55  ? 37  HIS A O   1 
ATOM   212  C CB  . HIS A 1 35  ? 3.092   -8.687  -3.690  1.00 45.45  ? 37  HIS A CB  1 
ATOM   213  C CG  . HIS A 1 35  ? 2.461   -7.745  -4.665  1.00 48.59  ? 37  HIS A CG  1 
ATOM   214  N ND1 . HIS A 1 35  ? 2.162   -6.444  -4.317  1.00 50.51  ? 37  HIS A ND1 1 
ATOM   215  C CD2 . HIS A 1 35  ? 2.066   -7.957  -5.940  1.00 49.40  ? 37  HIS A CD2 1 
ATOM   216  C CE1 . HIS A 1 35  ? 1.611   -5.911  -5.385  1.00 51.20  ? 37  HIS A CE1 1 
ATOM   217  N NE2 . HIS A 1 35  ? 1.531   -6.785  -6.384  1.00 50.29  ? 37  HIS A NE2 1 
ATOM   218  N N   . PRO A 1 36  ? 2.099   -11.810 -2.261  1.00 40.15  ? 38  PRO A N   1 
ATOM   219  C CA  . PRO A 1 36  ? 2.594   -12.930 -1.460  1.00 38.60  ? 38  PRO A CA  1 
ATOM   220  C C   . PRO A 1 36  ? 3.991   -13.381 -1.841  1.00 36.89  ? 38  PRO A C   1 
ATOM   221  O O   . PRO A 1 36  ? 4.357   -13.397 -3.017  1.00 35.35  ? 38  PRO A O   1 
ATOM   222  C CB  . PRO A 1 36  ? 1.610   -14.050 -1.756  1.00 39.78  ? 38  PRO A CB  1 
ATOM   223  C CG  . PRO A 1 36  ? 0.977   -13.713 -3.028  1.00 40.10  ? 38  PRO A CG  1 
ATOM   224  C CD  . PRO A 1 36  ? 0.982   -12.224 -3.135  1.00 39.85  ? 38  PRO A CD  1 
ATOM   225  N N   . LEU A 1 37  ? 4.771   -13.742 -0.828  1.00 35.90  ? 39  LEU A N   1 
ATOM   226  C CA  . LEU A 1 37  ? 6.072   -14.365 -1.046  1.00 34.50  ? 39  LEU A CA  1 
ATOM   227  C C   . LEU A 1 37  ? 5.902   -15.882 -1.227  1.00 33.83  ? 39  LEU A C   1 
ATOM   228  O O   . LEU A 1 37  ? 4.972   -16.457 -0.741  1.00 33.89  ? 39  LEU A O   1 
ATOM   229  C CB  . LEU A 1 37  ? 7.000   -14.036 0.139   1.00 32.78  ? 39  LEU A CB  1 
ATOM   230  C CG  . LEU A 1 37  ? 7.302   -12.540 0.340   1.00 32.24  ? 39  LEU A CG  1 
ATOM   231  C CD1 . LEU A 1 37  ? 8.198   -12.295 1.591   1.00 32.73  ? 39  LEU A CD1 1 
ATOM   232  C CD2 . LEU A 1 37  ? 7.956   -11.921 -0.899  1.00 32.30  ? 39  LEU A CD2 1 
ATOM   233  N N   . GLN A 1 38  ? 6.818   -16.509 -1.942  1.00 33.81  ? 40  GLN A N   1 
ATOM   234  C CA  . GLN A 1 38  ? 6.870   -17.963 -2.088  1.00 32.60  ? 40  GLN A CA  1 
ATOM   235  C C   . GLN A 1 38  ? 7.009   -18.648 -0.750  1.00 31.01  ? 40  GLN A C   1 
ATOM   236  O O   . GLN A 1 38  ? 6.372   -19.663 -0.530  1.00 30.42  ? 40  GLN A O   1 
ATOM   237  C CB  . GLN A 1 38  ? 8.063   -18.339 -2.983  1.00 32.66  ? 40  GLN A CB  1 
ATOM   238  C CG  . GLN A 1 38  ? 8.261   -19.822 -3.191  1.00 32.84  ? 40  GLN A CG  1 
ATOM   239  C CD  . GLN A 1 38  ? 7.197   -20.425 -4.068  1.00 38.75  ? 40  GLN A CD  1 
ATOM   240  O OE1 . GLN A 1 38  ? 6.397   -19.726 -4.724  1.00 40.22  ? 40  GLN A OE1 1 
ATOM   241  N NE2 . GLN A 1 38  ? 7.179   -21.751 -4.124  1.00 37.06  ? 40  GLN A NE2 1 
ATOM   242  N N   . ASN A 1 39  ? 7.845   -18.101 0.137   1.00 30.25  ? 41  ASN A N   1 
ATOM   243  C CA  . ASN A 1 39  ? 8.075   -18.617 1.487   1.00 29.71  ? 41  ASN A CA  1 
ATOM   244  C C   . ASN A 1 39  ? 7.747   -17.586 2.544   1.00 28.88  ? 41  ASN A C   1 
ATOM   245  O O   . ASN A 1 39  ? 7.777   -16.417 2.248   1.00 30.43  ? 41  ASN A O   1 
ATOM   246  C CB  . ASN A 1 39  ? 9.541   -19.002 1.615   1.00 29.29  ? 41  ASN A CB  1 
ATOM   247  C CG  . ASN A 1 39  ? 9.801   -20.227 0.861   1.00 30.84  ? 41  ASN A CG  1 
ATOM   248  O OD1 . ASN A 1 39  ? 9.466   -21.287 1.340   1.00 33.46  ? 41  ASN A OD1 1 
ATOM   249  N ND2 . ASN A 1 39  ? 10.357  -20.133 -0.338  1.00 30.56  ? 41  ASN A ND2 1 
ATOM   250  N N   . ARG A 1 40  ? 7.429   -18.023 3.750   1.00 27.41  ? 42  ARG A N   1 
ATOM   251  C CA  . ARG A 1 40  ? 7.387   -17.204 4.947   1.00 29.08  ? 42  ARG A CA  1 
ATOM   252  C C   . ARG A 1 40  ? 8.815   -17.152 5.526   1.00 28.85  ? 42  ARG A C   1 
ATOM   253  O O   . ARG A 1 40  ? 9.546   -18.150 5.503   1.00 28.60  ? 42  ARG A O   1 
ATOM   254  C CB  . ARG A 1 40  ? 6.404   -17.821 5.946   1.00 32.85  ? 42  ARG A CB  1 
ATOM   255  C CG  . ARG A 1 40  ? 6.188   -17.076 7.276   1.00 39.86  ? 42  ARG A CG  1 
ATOM   256  C CD  . ARG A 1 40  ? 4.736   -17.239 7.690   1.00 46.90  ? 42  ARG A CD  1 
ATOM   257  N NE  . ARG A 1 40  ? 4.527   -17.115 9.135   1.00 55.72  ? 42  ARG A NE  1 
ATOM   258  C CZ  . ARG A 1 40  ? 4.108   -16.029 9.794   1.00 60.00  ? 42  ARG A CZ  1 
ATOM   259  N NH1 . ARG A 1 40  ? 3.836   -14.899 9.137   1.00 58.97  ? 42  ARG A NH1 1 
ATOM   260  N NH2 . ARG A 1 40  ? 3.961   -16.064 11.122  1.00 61.38  ? 42  ARG A NH2 1 
ATOM   261  N N   . TRP A 1 41  ? 9.212   -15.979 6.014   1.00 28.39  ? 43  TRP A N   1 
ATOM   262  C CA  . TRP A 1 41  ? 10.593  -15.706 6.455   1.00 27.95  ? 43  TRP A CA  1 
ATOM   263  C C   . TRP A 1 41  ? 10.580  -15.223 7.874   1.00 28.04  ? 43  TRP A C   1 
ATOM   264  O O   . TRP A 1 41  ? 9.672   -14.531 8.252   1.00 28.02  ? 43  TRP A O   1 
ATOM   265  C CB  . TRP A 1 41  ? 11.314  -14.670 5.556   1.00 26.35  ? 43  TRP A CB  1 
ATOM   266  C CG  . TRP A 1 41  ? 11.434  -15.121 4.149   1.00 26.42  ? 43  TRP A CG  1 
ATOM   267  C CD1 . TRP A 1 41  ? 10.498  -14.993 3.161   1.00 26.91  ? 43  TRP A CD1 1 
ATOM   268  C CD2 . TRP A 1 41  ? 12.537  -15.860 3.574   1.00 25.81  ? 43  TRP A CD2 1 
ATOM   269  N NE1 . TRP A 1 41  ? 10.953  -15.593 2.003   1.00 27.33  ? 43  TRP A NE1 1 
ATOM   270  C CE2 . TRP A 1 41  ? 12.206  -16.120 2.231   1.00 26.82  ? 43  TRP A CE2 1 
ATOM   271  C CE3 . TRP A 1 41  ? 13.788  -16.282 4.057   1.00 25.73  ? 43  TRP A CE3 1 
ATOM   272  C CZ2 . TRP A 1 41  ? 13.063  -16.806 1.381   1.00 28.09  ? 43  TRP A CZ2 1 
ATOM   273  C CZ3 . TRP A 1 41  ? 14.637  -16.946 3.210   1.00 27.14  ? 43  TRP A CZ3 1 
ATOM   274  C CH2 . TRP A 1 41  ? 14.268  -17.225 1.893   1.00 28.23  ? 43  TRP A CH2 1 
ATOM   275  N N   . ALA A 1 42  ? 11.611  -15.576 8.661   1.00 27.96  ? 44  ALA A N   1 
ATOM   276  C CA  . ALA A 1 42  ? 11.726  -15.120 10.017  1.00 26.98  ? 44  ALA A CA  1 
ATOM   277  C C   . ALA A 1 42  ? 13.062  -14.436 10.204  1.00 27.66  ? 44  ALA A C   1 
ATOM   278  O O   . ALA A 1 42  ? 14.119  -14.932 9.795   1.00 27.62  ? 44  ALA A O   1 
ATOM   279  C CB  . ALA A 1 42  ? 11.597  -16.306 10.948  1.00 27.14  ? 44  ALA A CB  1 
ATOM   280  N N   . LEU A 1 43  ? 12.999  -13.270 10.843  1.00 28.93  ? 45  LEU A N   1 
ATOM   281  C CA  . LEU A 1 43  ? 14.120  -12.448 11.194  1.00 28.94  ? 45  LEU A CA  1 
ATOM   282  C C   . LEU A 1 43  ? 14.530  -12.738 12.606  1.00 28.95  ? 45  LEU A C   1 
ATOM   283  O O   . LEU A 1 43  ? 13.700  -12.668 13.509  1.00 28.75  ? 45  LEU A O   1 
ATOM   284  C CB  . LEU A 1 43  ? 13.762  -10.964 11.044  1.00 28.87  ? 45  LEU A CB  1 
ATOM   285  C CG  . LEU A 1 43  ? 14.852  -9.974  11.491  1.00 30.67  ? 45  LEU A CG  1 
ATOM   286  C CD1 . LEU A 1 43  ? 16.132  -10.159 10.689  1.00 29.16  ? 45  LEU A CD1 1 
ATOM   287  C CD2 . LEU A 1 43  ? 14.314  -8.548  11.452  1.00 31.35  ? 45  LEU A CD2 1 
ATOM   288  N N   . TRP A 1 44  ? 15.810  -13.059 12.781  1.00 29.41  ? 46  TRP A N   1 
ATOM   289  C CA  . TRP A 1 44  ? 16.451  -13.409 14.032  1.00 30.47  ? 46  TRP A CA  1 
ATOM   290  C C   . TRP A 1 44  ? 17.540  -12.423 14.371  1.00 31.40  ? 46  TRP A C   1 
ATOM   291  O O   . TRP A 1 44  ? 18.190  -11.870 13.496  1.00 30.12  ? 46  TRP A O   1 
ATOM   292  C CB  . TRP A 1 44  ? 17.087  -14.804 13.952  1.00 30.01  ? 46  TRP A CB  1 
ATOM   293  C CG  . TRP A 1 44  ? 16.184  -15.882 13.506  1.00 30.72  ? 46  TRP A CG  1 
ATOM   294  C CD1 . TRP A 1 44  ? 15.822  -16.182 12.236  1.00 31.28  ? 46  TRP A CD1 1 
ATOM   295  C CD2 . TRP A 1 44  ? 15.520  -16.829 14.350  1.00 31.36  ? 46  TRP A CD2 1 
ATOM   296  N NE1 . TRP A 1 44  ? 14.939  -17.237 12.234  1.00 31.93  ? 46  TRP A NE1 1 
ATOM   297  C CE2 . TRP A 1 44  ? 14.754  -17.667 13.520  1.00 31.84  ? 46  TRP A CE2 1 
ATOM   298  C CE3 . TRP A 1 44  ? 15.509  -17.059 15.724  1.00 32.83  ? 46  TRP A CE3 1 
ATOM   299  C CZ2 . TRP A 1 44  ? 13.984  -18.721 14.025  1.00 31.85  ? 46  TRP A CZ2 1 
ATOM   300  C CZ3 . TRP A 1 44  ? 14.740  -18.097 16.216  1.00 33.80  ? 46  TRP A CZ3 1 
ATOM   301  C CH2 . TRP A 1 44  ? 14.011  -18.927 15.371  1.00 32.34  ? 46  TRP A CH2 1 
ATOM   302  N N   . PHE A 1 45  ? 17.737  -12.224 15.660  1.00 35.18  ? 47  PHE A N   1 
ATOM   303  C CA  . PHE A 1 45  ? 18.795  -11.405 16.248  1.00 39.51  ? 47  PHE A CA  1 
ATOM   304  C C   . PHE A 1 45  ? 19.553  -12.298 17.201  1.00 41.68  ? 47  PHE A C   1 
ATOM   305  O O   . PHE A 1 45  ? 18.935  -13.086 17.926  1.00 40.82  ? 47  PHE A O   1 
ATOM   306  C CB  . PHE A 1 45  ? 18.162  -10.236 17.015  1.00 41.75  ? 47  PHE A CB  1 
ATOM   307  C CG  . PHE A 1 45  ? 19.149  -9.324  17.672  1.00 45.23  ? 47  PHE A CG  1 
ATOM   308  C CD1 . PHE A 1 45  ? 20.033  -8.573  16.914  1.00 47.75  ? 47  PHE A CD1 1 
ATOM   309  C CD2 . PHE A 1 45  ? 19.188  -9.199  19.049  1.00 47.50  ? 47  PHE A CD2 1 
ATOM   310  C CE1 . PHE A 1 45  ? 20.958  -7.738  17.520  1.00 48.57  ? 47  PHE A CE1 1 
ATOM   311  C CE2 . PHE A 1 45  ? 20.109  -8.350  19.659  1.00 49.22  ? 47  PHE A CE2 1 
ATOM   312  C CZ  . PHE A 1 45  ? 20.992  -7.634  18.888  1.00 49.12  ? 47  PHE A CZ  1 
ATOM   313  N N   . PHE A 1 46  ? 20.865  -12.208 17.197  1.00 45.08  ? 48  PHE A N   1 
ATOM   314  C CA  . PHE A 1 46  ? 21.687  -12.978 18.112  1.00 50.99  ? 48  PHE A CA  1 
ATOM   315  C C   . PHE A 1 46  ? 22.630  -12.001 18.759  1.00 55.81  ? 48  PHE A C   1 
ATOM   316  O O   . PHE A 1 46  ? 23.547  -11.510 18.108  1.00 55.46  ? 48  PHE A O   1 
ATOM   317  C CB  . PHE A 1 46  ? 22.414  -14.068 17.361  1.00 52.56  ? 48  PHE A CB  1 
ATOM   318  C CG  . PHE A 1 46  ? 23.312  -14.978 18.147  1.00 55.44  ? 48  PHE A CG  1 
ATOM   319  C CD1 . PHE A 1 46  ? 24.683  -14.776 18.169  1.00 57.62  ? 48  PHE A CD1 1 
ATOM   320  C CD2 . PHE A 1 46  ? 22.800  -16.079 18.809  1.00 56.98  ? 48  PHE A CD2 1 
ATOM   321  C CE1 . PHE A 1 46  ? 25.520  -15.653 18.853  1.00 58.87  ? 48  PHE A CE1 1 
ATOM   322  C CE2 . PHE A 1 46  ? 23.636  -16.941 19.513  1.00 58.24  ? 48  PHE A CE2 1 
ATOM   323  C CZ  . PHE A 1 46  ? 24.990  -16.726 19.526  1.00 58.56  ? 48  PHE A CZ  1 
ATOM   324  N N   . LYS A 1 47  ? 22.378  -11.693 20.045  1.00 59.93  ? 49  LYS A N   1 
ATOM   325  C CA  . LYS A 1 47  ? 23.132  -10.687 20.790  1.00 64.72  ? 49  LYS A CA  1 
ATOM   326  C C   . LYS A 1 47  ? 24.409  -11.313 21.392  1.00 68.36  ? 49  LYS A C   1 
ATOM   327  O O   . LYS A 1 47  ? 24.556  -12.541 21.410  1.00 67.90  ? 49  LYS A O   1 
ATOM   328  C CB  . LYS A 1 47  ? 22.226  -10.084 21.891  1.00 68.48  ? 49  LYS A CB  1 
ATOM   329  C CG  . LYS A 1 47  ? 22.698  -8.697  22.428  1.00 75.64  ? 49  LYS A CG  1 
ATOM   330  C CD  . LYS A 1 47  ? 21.616  -7.968  23.282  1.00 81.37  ? 49  LYS A CD  1 
ATOM   331  C CE  . LYS A 1 47  ? 21.826  -6.458  23.414  1.00 87.35  ? 49  LYS A CE  1 
ATOM   332  N NZ  . LYS A 1 47  ? 22.421  -6.052  24.734  1.00 90.52  ? 49  LYS A NZ  1 
ATOM   333  N N   . ASN A 1 48  ? 25.330  -10.475 21.884  1.00 71.87  ? 50  ASN A N   1 
ATOM   334  C CA  . ASN A 1 48  ? 26.581  -10.995 22.440  1.00 76.03  ? 50  ASN A CA  1 
ATOM   335  C C   . ASN A 1 48  ? 26.921  -10.349 23.772  1.00 78.47  ? 50  ASN A C   1 
ATOM   336  O O   . ASN A 1 48  ? 27.841  -9.519  23.840  1.00 78.73  ? 50  ASN A O   1 
ATOM   337  C CB  . ASN A 1 48  ? 27.732  -10.840 21.414  1.00 78.90  ? 50  ASN A CB  1 
ATOM   338  C CG  . ASN A 1 48  ? 28.916  -11.745 21.707  1.00 83.54  ? 50  ASN A CG  1 
ATOM   339  O OD1 . ASN A 1 48  ? 28.779  -12.986 21.733  1.00 85.33  ? 50  ASN A OD1 1 
ATOM   340  N ND2 . ASN A 1 48  ? 30.096  -11.159 21.938  1.00 83.91  ? 50  ASN A ND2 1 
ATOM   341  N N   . ASP A 1 49  ? 26.183  -10.729 24.842  1.00 79.89  ? 51  ASP A N   1 
ATOM   342  C CA  . ASP A 1 49  ? 26.505  -10.200 26.167  1.00 82.03  ? 51  ASP A CA  1 
ATOM   343  C C   . ASP A 1 49  ? 25.775  -10.920 27.340  1.00 82.66  ? 51  ASP A C   1 
ATOM   344  O O   . ASP A 1 49  ? 24.775  -11.601 27.162  1.00 82.35  ? 51  ASP A O   1 
ATOM   345  C CB  . ASP A 1 49  ? 26.274  -8.652  26.212  1.00 85.50  ? 51  ASP A CB  1 
ATOM   346  C CG  . ASP A 1 49  ? 25.084  -8.104  25.401  1.00 92.85  ? 51  ASP A CG  1 
ATOM   347  O OD1 . ASP A 1 49  ? 23.921  -8.506  25.690  1.00 94.61  ? 51  ASP A OD1 1 
ATOM   348  O OD2 . ASP A 1 49  ? 25.316  -7.269  24.485  1.00 94.87  ? 51  ASP A OD2 1 
ATOM   349  N N   . LYS A 1 50  ? 26.338  -10.748 28.542  1.00 83.58  ? 52  LYS A N   1 
ATOM   350  C CA  . LYS A 1 50  ? 25.747  -11.025 29.864  1.00 84.53  ? 52  LYS A CA  1 
ATOM   351  C C   . LYS A 1 50  ? 25.927  -12.498 30.295  1.00 83.75  ? 52  LYS A C   1 
ATOM   352  O O   . LYS A 1 50  ? 25.125  -13.011 31.085  1.00 83.90  ? 52  LYS A O   1 
ATOM   353  C CB  . LYS A 1 50  ? 24.263  -10.556 29.974  1.00 87.40  ? 52  LYS A CB  1 
ATOM   354  C CG  . LYS A 1 50  ? 24.060  -9.041  29.986  1.00 92.46  ? 52  LYS A CG  1 
ATOM   355  C CD  . LYS A 1 50  ? 22.596  -8.710  30.288  1.00 98.12  ? 52  LYS A CD  1 
ATOM   356  C CE  . LYS A 1 50  ? 22.224  -7.266  30.020  1.00 102.09 ? 52  LYS A CE  1 
ATOM   357  N NZ  . LYS A 1 50  ? 20.759  -7.113  29.778  1.00 104.14 ? 52  LYS A NZ  1 
ATOM   358  N N   . SER A 1 51  ? 26.983  -13.173 29.793  1.00 82.59  ? 53  SER A N   1 
ATOM   359  C CA  . SER A 1 51  ? 27.359  -14.510 30.253  1.00 82.15  ? 53  SER A CA  1 
ATOM   360  C C   . SER A 1 51  ? 26.196  -15.489 30.137  1.00 80.42  ? 53  SER A C   1 
ATOM   361  O O   . SER A 1 51  ? 25.803  -16.129 31.112  1.00 80.20  ? 53  SER A O   1 
ATOM   362  C CB  . SER A 1 51  ? 27.931  -14.448 31.673  1.00 85.35  ? 53  SER A CB  1 
ATOM   363  O OG  . SER A 1 51  ? 27.217  -13.650 32.609  1.00 89.18  ? 53  SER A OG  1 
ATOM   364  N N   . LYS A 1 52  ? 25.650  -15.582 28.910  1.00 79.01  ? 54  LYS A N   1 
ATOM   365  C CA  . LYS A 1 52  ? 24.417  -16.298 28.604  1.00 77.62  ? 54  LYS A CA  1 
ATOM   366  C C   . LYS A 1 52  ? 24.662  -17.447 27.641  1.00 77.14  ? 54  LYS A C   1 
ATOM   367  O O   . LYS A 1 52  ? 25.627  -17.435 26.869  1.00 76.82  ? 54  LYS A O   1 
ATOM   368  C CB  . LYS A 1 52  ? 23.390  -15.337 27.995  1.00 77.83  ? 54  LYS A CB  1 
ATOM   369  C CG  . LYS A 1 52  ? 22.813  -14.332 28.964  1.00 79.12  ? 54  LYS A CG  1 
ATOM   370  C CD  . LYS A 1 52  ? 21.855  -13.392 28.265  1.00 81.89  ? 54  LYS A CD  1 
ATOM   371  C CE  . LYS A 1 52  ? 20.581  -13.129 29.037  1.00 86.28  ? 54  LYS A CE  1 
ATOM   372  N NZ  . LYS A 1 52  ? 20.793  -12.844 30.489  1.00 88.52  ? 54  LYS A NZ  1 
ATOM   373  N N   . THR A 1 53  ? 23.772  -18.444 27.690  1.00 76.98  ? 55  THR A N   1 
ATOM   374  C CA  . THR A 1 53  ? 23.813  -19.592 26.781  1.00 77.57  ? 55  THR A CA  1 
ATOM   375  C C   . THR A 1 53  ? 23.465  -19.175 25.336  1.00 77.44  ? 55  THR A C   1 
ATOM   376  O O   . THR A 1 53  ? 22.743  -18.200 25.124  1.00 77.78  ? 55  THR A O   1 
ATOM   377  C CB  . THR A 1 53  ? 22.859  -20.675 27.280  1.00 79.98  ? 55  THR A CB  1 
ATOM   378  O OG1 . THR A 1 53  ? 21.567  -20.083 27.413  1.00 82.34  ? 55  THR A OG1 1 
ATOM   379  C CG2 . THR A 1 53  ? 23.289  -21.273 28.638  1.00 79.87  ? 55  THR A CG2 1 
ATOM   380  N N   . TRP A 1 54  ? 23.990  -19.912 24.340  1.00 76.80  ? 56  TRP A N   1 
ATOM   381  C CA  . TRP A 1 54  ? 23.707  -19.703 22.905  1.00 76.07  ? 56  TRP A CA  1 
ATOM   382  C C   . TRP A 1 54  ? 22.204  -19.507 22.620  1.00 71.64  ? 56  TRP A C   1 
ATOM   383  O O   . TRP A 1 54  ? 21.832  -18.610 21.863  1.00 71.35  ? 56  TRP A O   1 
ATOM   384  C CB  . TRP A 1 54  ? 24.265  -20.879 22.064  1.00 78.10  ? 56  TRP A CB  1 
ATOM   385  C CG  . TRP A 1 54  ? 23.693  -22.232 22.423  1.00 81.81  ? 56  TRP A CG  1 
ATOM   386  C CD1 . TRP A 1 54  ? 23.908  -22.948 23.572  1.00 83.68  ? 56  TRP A CD1 1 
ATOM   387  C CD2 . TRP A 1 54  ? 22.798  -23.022 21.622  1.00 83.12  ? 56  TRP A CD2 1 
ATOM   388  N NE1 . TRP A 1 54  ? 23.189  -24.126 23.539  1.00 84.32  ? 56  TRP A NE1 1 
ATOM   389  C CE2 . TRP A 1 54  ? 22.521  -24.207 22.342  1.00 84.18  ? 56  TRP A CE2 1 
ATOM   390  C CE3 . TRP A 1 54  ? 22.214  -22.846 20.364  1.00 84.12  ? 56  TRP A CE3 1 
ATOM   391  C CZ2 . TRP A 1 54  ? 21.685  -25.204 21.842  1.00 85.11  ? 56  TRP A CZ2 1 
ATOM   392  C CZ3 . TRP A 1 54  ? 21.388  -23.837 19.870  1.00 85.36  ? 56  TRP A CZ3 1 
ATOM   393  C CH2 . TRP A 1 54  ? 21.124  -24.995 20.610  1.00 85.39  ? 56  TRP A CH2 1 
ATOM   394  N N   . GLN A 1 55  ? 21.358  -20.354 23.239  1.00 68.18  ? 57  GLN A N   1 
ATOM   395  C CA  . GLN A 1 55  ? 19.908  -20.294 23.128  1.00 64.64  ? 57  GLN A CA  1 
ATOM   396  C C   . GLN A 1 55  ? 19.352  -18.984 23.676  1.00 58.75  ? 57  GLN A C   1 
ATOM   397  O O   . GLN A 1 55  ? 18.465  -18.398 23.057  1.00 57.95  ? 57  GLN A O   1 
ATOM   398  C CB  . GLN A 1 55  ? 19.254  -21.478 23.866  1.00 68.80  ? 57  GLN A CB  1 
ATOM   399  C CG  . GLN A 1 55  ? 19.514  -22.840 23.231  1.00 75.24  ? 57  GLN A CG  1 
ATOM   400  C CD  . GLN A 1 55  ? 18.274  -23.573 22.715  1.00 81.24  ? 57  GLN A CD  1 
ATOM   401  O OE1 . GLN A 1 55  ? 17.441  -23.030 21.969  1.00 82.85  ? 57  GLN A OE1 1 
ATOM   402  N NE2 . GLN A 1 55  ? 18.123  -24.843 23.084  1.00 81.84  ? 57  GLN A NE2 1 
ATOM   403  N N   . ALA A 1 56  ? 19.870  -18.513 24.819  1.00 54.79  ? 58  ALA A N   1 
ATOM   404  C CA  . ALA A 1 56  ? 19.369  -17.284 25.416  1.00 51.99  ? 58  ALA A CA  1 
ATOM   405  C C   . ALA A 1 56  ? 19.648  -16.058 24.580  1.00 48.28  ? 58  ALA A C   1 
ATOM   406  O O   . ALA A 1 56  ? 18.862  -15.121 24.625  1.00 47.33  ? 58  ALA A O   1 
ATOM   407  C CB  . ALA A 1 56  ? 19.916  -17.111 26.812  1.00 52.39  ? 58  ALA A CB  1 
ATOM   408  N N   . ASN A 1 57  ? 20.747  -16.056 23.813  1.00 46.25  ? 59  ASN A N   1 
ATOM   409  C CA  . ASN A 1 57  ? 21.115  -14.918 22.972  1.00 45.30  ? 59  ASN A CA  1 
ATOM   410  C C   . ASN A 1 57  ? 20.414  -14.873 21.627  1.00 41.28  ? 59  ASN A C   1 
ATOM   411  O O   . ASN A 1 57  ? 20.370  -13.814 21.021  1.00 39.53  ? 59  ASN A O   1 
ATOM   412  C CB  . ASN A 1 57  ? 22.624  -14.897 22.770  1.00 49.02  ? 59  ASN A CB  1 
ATOM   413  C CG  . ASN A 1 57  ? 23.340  -14.663 24.084  1.00 54.35  ? 59  ASN A CG  1 
ATOM   414  O OD1 . ASN A 1 57  ? 22.988  -13.752 24.863  1.00 55.00  ? 59  ASN A OD1 1 
ATOM   415  N ND2 . ASN A 1 57  ? 24.350  -15.480 24.362  1.00 57.03  ? 59  ASN A ND2 1 
ATOM   416  N N   . LEU A 1 58  ? 19.880  -16.006 21.164  1.00 39.91  ? 60  LEU A N   1 
ATOM   417  C CA  . LEU A 1 58  ? 19.102  -16.055 19.954  1.00 39.34  ? 60  LEU A CA  1 
ATOM   418  C C   . LEU A 1 58  ? 17.670  -15.702 20.223  1.00 39.27  ? 60  LEU A C   1 
ATOM   419  O O   . LEU A 1 58  ? 17.017  -16.369 21.013  1.00 39.38  ? 60  LEU A O   1 
ATOM   420  C CB  . LEU A 1 58  ? 19.169  -17.460 19.340  1.00 39.71  ? 60  LEU A CB  1 
ATOM   421  C CG  . LEU A 1 58  ? 18.448  -17.631 17.990  1.00 42.35  ? 60  LEU A CG  1 
ATOM   422  C CD1 . LEU A 1 58  ? 18.954  -16.604 16.933  1.00 42.54  ? 60  LEU A CD1 1 
ATOM   423  C CD2 . LEU A 1 58  ? 18.554  -19.072 17.492  1.00 43.15  ? 60  LEU A CD2 1 
ATOM   424  N N   . ARG A 1 59  ? 17.168  -14.701 19.527  1.00 39.36  ? 61  ARG A N   1 
ATOM   425  C CA  . ARG A 1 59  ? 15.811  -14.220 19.674  1.00 39.84  ? 61  ARG A CA  1 
ATOM   426  C C   . ARG A 1 59  ? 15.169  -14.106 18.277  1.00 38.75  ? 61  ARG A C   1 
ATOM   427  O O   . ARG A 1 59  ? 15.803  -13.632 17.345  1.00 38.67  ? 61  ARG A O   1 
ATOM   428  C CB  . ARG A 1 59  ? 15.867  -12.875 20.419  1.00 44.24  ? 61  ARG A CB  1 
ATOM   429  C CG  . ARG A 1 59  ? 14.623  -12.010 20.329  1.00 53.02  ? 61  ARG A CG  1 
ATOM   430  C CD  . ARG A 1 59  ? 14.026  -11.687 21.709  1.00 60.75  ? 61  ARG A CD  1 
ATOM   431  N NE  . ARG A 1 59  ? 13.109  -10.541 21.683  1.00 65.95  ? 61  ARG A NE  1 
ATOM   432  C CZ  . ARG A 1 59  ? 11.883  -10.561 21.162  1.00 70.69  ? 61  ARG A CZ  1 
ATOM   433  N NH1 . ARG A 1 59  ? 11.129  -9.472  21.186  1.00 72.43  ? 61  ARG A NH1 1 
ATOM   434  N NH2 . ARG A 1 59  ? 11.404  -11.673 20.607  1.00 70.87  ? 61  ARG A NH2 1 
ATOM   435  N N   . LEU A 1 60  ? 13.921  -14.575 18.128  1.00 37.40  ? 62  LEU A N   1 
ATOM   436  C CA  . LEU A 1 60  ? 13.130  -14.324 16.934  1.00 36.85  ? 62  LEU A CA  1 
ATOM   437  C C   . LEU A 1 60  ? 12.515  -12.941 17.090  1.00 38.10  ? 62  LEU A C   1 
ATOM   438  O O   . LEU A 1 60  ? 11.864  -12.709 18.077  1.00 38.89  ? 62  LEU A O   1 
ATOM   439  C CB  . LEU A 1 60  ? 12.035  -15.382 16.800  1.00 36.11  ? 62  LEU A CB  1 
ATOM   440  C CG  . LEU A 1 60  ? 10.873  -15.074 15.856  1.00 37.19  ? 62  LEU A CG  1 
ATOM   441  C CD1 . LEU A 1 60  ? 11.261  -15.313 14.447  1.00 37.78  ? 62  LEU A CD1 1 
ATOM   442  C CD2 . LEU A 1 60  ? 9.623   -15.857 16.249  1.00 37.54  ? 62  LEU A CD2 1 
ATOM   443  N N   . ILE A 1 61  ? 12.716  -12.049 16.137  1.00 38.64  ? 63  ILE A N   1 
ATOM   444  C CA  . ILE A 1 61  ? 12.116  -10.732 16.089  1.00 39.37  ? 63  ILE A CA  1 
ATOM   445  C C   . ILE A 1 61  ? 10.700  -10.840 15.489  1.00 40.50  ? 63  ILE A C   1 
ATOM   446  O O   . ILE A 1 61  ? 9.735   -10.461 16.136  1.00 41.97  ? 63  ILE A O   1 
ATOM   447  C CB  . ILE A 1 61  ? 13.039  -9.766  15.265  1.00 40.30  ? 63  ILE A CB  1 
ATOM   448  C CG1 . ILE A 1 61  ? 14.473  -9.674  15.837  1.00 41.86  ? 63  ILE A CG1 1 
ATOM   449  C CG2 . ILE A 1 61  ? 12.426  -8.340  15.119  1.00 40.75  ? 63  ILE A CG2 1 
ATOM   450  C CD1 . ILE A 1 61  ? 14.604  -9.717  17.305  1.00 43.86  ? 63  ILE A CD1 1 
ATOM   451  N N   . SER A 1 62  ? 10.559  -11.376 14.283  1.00 40.15  ? 64  SER A N   1 
ATOM   452  C CA  . SER A 1 62  ? 9.358   -11.173 13.486  1.00 40.11  ? 64  SER A CA  1 
ATOM   453  C C   . SER A 1 62  ? 9.342   -12.097 12.277  1.00 39.31  ? 64  SER A C   1 
ATOM   454  O O   . SER A 1 62  ? 10.415  -12.478 11.774  1.00 40.01  ? 64  SER A O   1 
ATOM   455  C CB  . SER A 1 62  ? 9.341   -9.724  13.011  1.00 43.19  ? 64  SER A CB  1 
ATOM   456  O OG  . SER A 1 62  ? 8.201   -9.370  12.246  1.00 46.37  ? 64  SER A OG  1 
ATOM   457  N N   . LYS A 1 63  ? 8.147   -12.457 11.811  1.00 37.73  ? 65  LYS A N   1 
ATOM   458  C CA  . LYS A 1 63  ? 7.939   -13.218 10.584  1.00 37.71  ? 65  LYS A CA  1 
ATOM   459  C C   . LYS A 1 63  ? 7.058   -12.483 9.576   1.00 37.99  ? 65  LYS A C   1 
ATOM   460  O O   . LYS A 1 63  ? 6.302   -11.602 9.951   1.00 39.68  ? 65  LYS A O   1 
ATOM   461  C CB  . LYS A 1 63  ? 7.383   -14.618 10.871  1.00 38.90  ? 65  LYS A CB  1 
ATOM   462  C CG  . LYS A 1 63  ? 8.100   -15.347 11.982  1.00 40.37  ? 65  LYS A CG  1 
ATOM   463  C CD  . LYS A 1 63  ? 7.821   -16.819 11.928  1.00 42.88  ? 65  LYS A CD  1 
ATOM   464  C CE  . LYS A 1 63  ? 8.529   -17.562 13.016  1.00 46.76  ? 65  LYS A CE  1 
ATOM   465  N NZ  . LYS A 1 63  ? 8.073   -18.972 13.062  1.00 46.84  ? 65  LYS A NZ  1 
ATOM   466  N N   . PHE A 1 64  ? 7.173   -12.823 8.291   1.00 36.65  ? 66  PHE A N   1 
ATOM   467  C CA  . PHE A 1 64  ? 6.465   -12.136 7.202   1.00 36.12  ? 66  PHE A CA  1 
ATOM   468  C C   . PHE A 1 64  ? 6.399   -13.021 5.979   1.00 35.93  ? 66  PHE A C   1 
ATOM   469  O O   . PHE A 1 64  ? 7.234   -13.876 5.798   1.00 36.07  ? 66  PHE A O   1 
ATOM   470  C CB  . PHE A 1 64  ? 7.049   -10.750 6.868   1.00 36.89  ? 66  PHE A CB  1 
ATOM   471  C CG  . PHE A 1 64  ? 8.496   -10.783 6.381   1.00 37.24  ? 66  PHE A CG  1 
ATOM   472  C CD1 . PHE A 1 64  ? 8.792   -11.001 5.044   1.00 37.98  ? 66  PHE A CD1 1 
ATOM   473  C CD2 . PHE A 1 64  ? 9.542   -10.663 7.268   1.00 37.88  ? 66  PHE A CD2 1 
ATOM   474  C CE1 . PHE A 1 64  ? 10.111  -11.104 4.612   1.00 39.15  ? 66  PHE A CE1 1 
ATOM   475  C CE2 . PHE A 1 64  ? 10.859  -10.742 6.828   1.00 38.67  ? 66  PHE A CE2 1 
ATOM   476  C CZ  . PHE A 1 64  ? 11.133  -10.974 5.503   1.00 38.70  ? 66  PHE A CZ  1 
ATOM   477  N N   . ASP A 1 65  ? 5.387   -12.841 5.158   1.00 36.25  ? 67  ASP A N   1 
ATOM   478  C CA  . ASP A 1 65  ? 5.195   -13.605 3.938   1.00 36.60  ? 67  ASP A CA  1 
ATOM   479  C C   . ASP A 1 65  ? 4.563   -12.766 2.807   1.00 36.79  ? 67  ASP A C   1 
ATOM   480  O O   . ASP A 1 65  ? 3.970   -13.340 1.885   1.00 37.39  ? 67  ASP A O   1 
ATOM   481  C CB  . ASP A 1 65  ? 4.426   -14.904 4.202   1.00 38.68  ? 67  ASP A CB  1 
ATOM   482  C CG  . ASP A 1 65  ? 3.005   -14.728 4.682   1.00 48.06  ? 67  ASP A CG  1 
ATOM   483  O OD1 . ASP A 1 65  ? 2.746   -13.781 5.429   1.00 49.86  ? 67  ASP A OD1 1 
ATOM   484  O OD2 . ASP A 1 65  ? 2.159   -15.552 4.323   1.00 54.04  ? 67  ASP A OD2 1 
ATOM   485  N N   . THR A 1 66  ? 4.699   -11.422 2.860   1.00 35.41  ? 68  THR A N   1 
ATOM   486  C CA  . THR A 1 66  ? 4.379   -10.543 1.737   1.00 35.40  ? 68  THR A CA  1 
ATOM   487  C C   . THR A 1 66  ? 5.512   -9.551  1.533   1.00 34.38  ? 68  THR A C   1 
ATOM   488  O O   . THR A 1 66  ? 6.298   -9.315  2.459   1.00 33.37  ? 68  THR A O   1 
ATOM   489  C CB  . THR A 1 66  ? 3.017   -9.810  1.927   1.00 36.63  ? 68  THR A CB  1 
ATOM   490  O OG1 . THR A 1 66  ? 3.156   -8.748  2.849   1.00 37.59  ? 68  THR A OG1 1 
ATOM   491  C CG2 . THR A 1 66  ? 1.922   -10.740 2.393   1.00 34.88  ? 68  THR A CG2 1 
ATOM   492  N N   . VAL A 1 67  ? 5.570   -8.969  0.318   1.00 34.30  ? 69  VAL A N   1 
ATOM   493  C CA  . VAL A 1 67  ? 6.524   -7.924  -0.043  1.00 35.19  ? 69  VAL A CA  1 
ATOM   494  C C   . VAL A 1 67  ? 6.339   -6.695  0.824   1.00 34.66  ? 69  VAL A C   1 
ATOM   495  O O   . VAL A 1 67  ? 7.315   -6.136  1.306   1.00 34.61  ? 69  VAL A O   1 
ATOM   496  C CB  . VAL A 1 67  ? 6.425   -7.539  -1.531  1.00 36.19  ? 69  VAL A CB  1 
ATOM   497  C CG1 . VAL A 1 67  ? 7.406   -6.420  -1.859  1.00 38.14  ? 69  VAL A CG1 1 
ATOM   498  C CG2 . VAL A 1 67  ? 6.660   -8.748  -2.418  1.00 35.61  ? 69  VAL A CG2 1 
ATOM   499  N N   . GLU A 1 68  ? 5.102   -6.275  1.029   1.00 34.64  ? 70  GLU A N   1 
ATOM   500  C CA  . GLU A 1 68  ? 4.767   -5.078  1.828   1.00 34.61  ? 70  GLU A CA  1 
ATOM   501  C C   . GLU A 1 68  ? 5.131   -5.240  3.310   1.00 33.65  ? 70  GLU A C   1 
ATOM   502  O O   . GLU A 1 68  ? 5.616   -4.291  3.922   1.00 33.32  ? 70  GLU A O   1 
ATOM   503  C CB  . GLU A 1 68  ? 3.243   -4.787  1.718   1.00 38.81  ? 70  GLU A CB  1 
ATOM   504  C CG  . GLU A 1 68  ? 2.802   -4.337  0.323   1.00 44.26  ? 70  GLU A CG  1 
ATOM   505  C CD  . GLU A 1 68  ? 2.730   -5.417  -0.747  1.00 47.67  ? 70  GLU A CD  1 
ATOM   506  O OE1 . GLU A 1 68  ? 2.678   -6.611  -0.380  1.00 47.47  ? 70  GLU A OE1 1 
ATOM   507  O OE2 . GLU A 1 68  ? 2.722   -5.076  -1.950  1.00 51.31  ? 70  GLU A OE2 1 
ATOM   508  N N   . ASP A 1 69  ? 4.889   -6.428  3.891   1.00 33.73  ? 71  ASP A N   1 
ATOM   509  C CA  . ASP A 1 69  ? 5.263   -6.675  5.294   1.00 35.04  ? 71  ASP A CA  1 
ATOM   510  C C   . ASP A 1 69  ? 6.791   -6.772  5.465   1.00 35.45  ? 71  ASP A C   1 
ATOM   511  O O   . ASP A 1 69  ? 7.315   -6.365  6.516   1.00 36.09  ? 71  ASP A O   1 
ATOM   512  C CB  . ASP A 1 69  ? 4.599   -7.944  5.817   1.00 36.59  ? 71  ASP A CB  1 
ATOM   513  C CG  . ASP A 1 69  ? 3.083   -7.838  5.816   1.00 37.59  ? 71  ASP A CG  1 
ATOM   514  O OD1 . ASP A 1 69  ? 2.570   -6.761  6.185   1.00 39.84  ? 71  ASP A OD1 1 
ATOM   515  O OD2 . ASP A 1 69  ? 2.422   -8.824  5.430   1.00 35.19  ? 71  ASP A OD2 1 
ATOM   516  N N   . PHE A 1 70  ? 7.510   -7.292  4.423   1.00 33.68  ? 72  PHE A N   1 
ATOM   517  C CA  . PHE A 1 70  ? 8.980   -7.210  4.381   1.00 32.52  ? 72  PHE A CA  1 
ATOM   518  C C   . PHE A 1 70  ? 9.414   -5.757  4.459   1.00 31.71  ? 72  PHE A C   1 
ATOM   519  O O   . PHE A 1 70  ? 10.219  -5.419  5.304   1.00 30.63  ? 72  PHE A O   1 
ATOM   520  C CB  . PHE A 1 70  ? 9.558   -7.868  3.100   1.00 32.03  ? 72  PHE A CB  1 
ATOM   521  C CG  . PHE A 1 70  ? 10.968  -7.402  2.832   1.00 31.86  ? 72  PHE A CG  1 
ATOM   522  C CD1 . PHE A 1 70  ? 12.028  -7.875  3.588   1.00 31.73  ? 72  PHE A CD1 1 
ATOM   523  C CD2 . PHE A 1 70  ? 11.229  -6.453  1.850   1.00 32.10  ? 72  PHE A CD2 1 
ATOM   524  C CE1 . PHE A 1 70  ? 13.324  -7.434  3.332   1.00 32.47  ? 72  PHE A CE1 1 
ATOM   525  C CE2 . PHE A 1 70  ? 12.516  -6.007  1.614   1.00 32.04  ? 72  PHE A CE2 1 
ATOM   526  C CZ  . PHE A 1 70  ? 13.550  -6.481  2.364   1.00 32.41  ? 72  PHE A CZ  1 
ATOM   527  N N   . TRP A 1 71  ? 8.867   -4.893  3.577   1.00 32.72  ? 73  TRP A N   1 
ATOM   528  C CA  . TRP A 1 71  ? 9.246   -3.488  3.583   1.00 33.68  ? 73  TRP A CA  1 
ATOM   529  C C   . TRP A 1 71  ? 8.847   -2.747  4.828   1.00 34.37  ? 73  TRP A C   1 
ATOM   530  O O   . TRP A 1 71  ? 9.597   -1.899  5.256   1.00 36.33  ? 73  TRP A O   1 
ATOM   531  C CB  . TRP A 1 71  ? 8.686   -2.749  2.386   1.00 33.51  ? 73  TRP A CB  1 
ATOM   532  C CG  . TRP A 1 71  ? 9.424   -3.056  1.117   1.00 33.48  ? 73  TRP A CG  1 
ATOM   533  C CD1 . TRP A 1 71  ? 8.907   -3.596  -0.021  1.00 33.52  ? 73  TRP A CD1 1 
ATOM   534  C CD2 . TRP A 1 71  ? 10.810  -2.800  0.850   1.00 32.35  ? 73  TRP A CD2 1 
ATOM   535  N NE1 . TRP A 1 71  ? 9.875   -3.680  -0.987  1.00 33.00  ? 73  TRP A NE1 1 
ATOM   536  C CE2 . TRP A 1 71  ? 11.060  -3.219  -0.474  1.00 32.65  ? 73  TRP A CE2 1 
ATOM   537  C CE3 . TRP A 1 71  ? 11.870  -2.298  1.622   1.00 31.73  ? 73  TRP A CE3 1 
ATOM   538  C CZ2 . TRP A 1 71  ? 12.321  -3.161  -1.044  1.00 32.21  ? 73  TRP A CZ2 1 
ATOM   539  C CZ3 . TRP A 1 71  ? 13.121  -2.223  1.053   1.00 31.66  ? 73  TRP A CZ3 1 
ATOM   540  C CH2 . TRP A 1 71  ? 13.341  -2.639  -0.268  1.00 32.18  ? 73  TRP A CH2 1 
ATOM   541  N N   . ALA A 1 72  ? 7.695   -3.031  5.417   1.00 33.45  ? 74  ALA A N   1 
ATOM   542  C CA  . ALA A 1 72  ? 7.322   -2.450  6.721   1.00 34.88  ? 74  ALA A CA  1 
ATOM   543  C C   . ALA A 1 72  ? 8.384   -2.770  7.798   1.00 36.01  ? 74  ALA A C   1 
ATOM   544  O O   . ALA A 1 72  ? 8.814   -1.876  8.503   1.00 37.33  ? 74  ALA A O   1 
ATOM   545  C CB  . ALA A 1 72  ? 5.943   -2.985  7.161   1.00 35.46  ? 74  ALA A CB  1 
ATOM   546  N N   . LEU A 1 73  ? 8.796   -4.033  7.914   1.00 36.68  ? 75  LEU A N   1 
ATOM   547  C CA  . LEU A 1 73  ? 9.806   -4.480  8.875   1.00 37.16  ? 75  LEU A CA  1 
ATOM   548  C C   . LEU A 1 73  ? 11.144  -3.869  8.554   1.00 36.67  ? 75  LEU A C   1 
ATOM   549  O O   . LEU A 1 73  ? 11.838  -3.404  9.461   1.00 37.07  ? 75  LEU A O   1 
ATOM   550  C CB  . LEU A 1 73  ? 9.892   -6.022  8.846   1.00 37.98  ? 75  LEU A CB  1 
ATOM   551  C CG  . LEU A 1 73  ? 10.938  -6.660  9.753   1.00 40.60  ? 75  LEU A CG  1 
ATOM   552  C CD1 . LEU A 1 73  ? 10.641  -6.360  11.202  1.00 41.49  ? 75  LEU A CD1 1 
ATOM   553  C CD2 . LEU A 1 73  ? 10.991  -8.150  9.524   1.00 41.38  ? 75  LEU A CD2 1 
ATOM   554  N N   . TYR A 1 74  ? 11.520  -3.851  7.262   1.00 35.67  ? 76  TYR A N   1 
ATOM   555  C CA  . TYR A 1 74  ? 12.772  -3.251  6.832   1.00 36.27  ? 76  TYR A CA  1 
ATOM   556  C C   . TYR A 1 74  ? 12.842  -1.771  7.207   1.00 39.05  ? 76  TYR A C   1 
ATOM   557  O O   . TYR A 1 74  ? 13.834  -1.323  7.810   1.00 38.92  ? 76  TYR A O   1 
ATOM   558  C CB  . TYR A 1 74  ? 12.954  -3.423  5.311   1.00 34.51  ? 76  TYR A CB  1 
ATOM   559  C CG  . TYR A 1 74  ? 14.293  -2.915  4.826   1.00 32.98  ? 76  TYR A CG  1 
ATOM   560  C CD1 . TYR A 1 74  ? 14.464  -1.582  4.449   1.00 33.26  ? 76  TYR A CD1 1 
ATOM   561  C CD2 . TYR A 1 74  ? 15.386  -3.771  4.720   1.00 32.73  ? 76  TYR A CD2 1 
ATOM   562  C CE1 . TYR A 1 74  ? 15.691  -1.111  4.018   1.00 33.80  ? 76  TYR A CE1 1 
ATOM   563  C CE2 . TYR A 1 74  ? 16.611  -3.317  4.275   1.00 32.98  ? 76  TYR A CE2 1 
ATOM   564  C CZ  . TYR A 1 74  ? 16.762  -1.985  3.933   1.00 35.09  ? 76  TYR A CZ  1 
ATOM   565  O OH  . TYR A 1 74  ? 17.969  -1.523  3.511   1.00 39.30  ? 76  TYR A OH  1 
ATOM   566  N N   . ASN A 1 75  ? 11.796  -1.005  6.840   1.00 40.74  ? 77  ASN A N   1 
ATOM   567  C CA  . ASN A 1 75  ? 11.723  0.421   7.156   1.00 42.89  ? 77  ASN A CA  1 
ATOM   568  C C   . ASN A 1 75  ? 11.736  0.626   8.680   1.00 44.05  ? 77  ASN A C   1 
ATOM   569  O O   . ASN A 1 75  ? 12.460  1.477   9.168   1.00 45.14  ? 77  ASN A O   1 
ATOM   570  C CB  . ASN A 1 75  ? 10.482  1.057   6.517   1.00 44.56  ? 77  ASN A CB  1 
ATOM   571  C CG  . ASN A 1 75  ? 10.527  1.133   4.998   1.00 49.51  ? 77  ASN A CG  1 
ATOM   572  O OD1 . ASN A 1 75  ? 11.607  1.116   4.369   1.00 52.47  ? 77  ASN A OD1 1 
ATOM   573  N ND2 . ASN A 1 75  ? 9.367   1.228   4.361   1.00 50.30  ? 77  ASN A ND2 1 
ATOM   574  N N   . HIS A 1 76  ? 10.965  -0.156  9.424   1.00 44.63  ? 78  HIS A N   1 
ATOM   575  C CA  . HIS A 1 76  ? 11.012  -0.106  10.887  1.00 45.77  ? 78  HIS A CA  1 
ATOM   576  C C   . HIS A 1 76  ? 12.445  -0.334  11.449  1.00 45.59  ? 78  HIS A C   1 
ATOM   577  O O   . HIS A 1 76  ? 12.925  0.534   12.125  1.00 46.32  ? 78  HIS A O   1 
ATOM   578  C CB  . HIS A 1 76  ? 10.019  -1.101  11.498  1.00 47.05  ? 78  HIS A CB  1 
ATOM   579  C CG  . HIS A 1 76  ? 10.034  -1.056  12.988  1.00 55.10  ? 78  HIS A CG  1 
ATOM   580  N ND1 . HIS A 1 76  ? 10.368  -2.173  13.746  1.00 58.93  ? 78  HIS A ND1 1 
ATOM   581  C CD2 . HIS A 1 76  ? 9.784   -0.016  13.823  1.00 58.14  ? 78  HIS A CD2 1 
ATOM   582  C CE1 . HIS A 1 76  ? 10.291  -1.783  15.011  1.00 60.58  ? 78  HIS A CE1 1 
ATOM   583  N NE2 . HIS A 1 76  ? 9.950   -0.488  15.103  1.00 60.55  ? 78  HIS A NE2 1 
ATOM   584  N N   . ILE A 1 77  ? 13.129  -1.486  11.168  1.00 44.93  ? 79  ILE A N   1 
ATOM   585  C CA  . ILE A 1 77  ? 14.499  -1.751  11.638  1.00 44.77  ? 79  ILE A CA  1 
ATOM   586  C C   . ILE A 1 77  ? 15.449  -0.588  11.218  1.00 45.19  ? 79  ILE A C   1 
ATOM   587  O O   . ILE A 1 77  ? 16.244  -0.122  12.019  1.00 43.80  ? 79  ILE A O   1 
ATOM   588  C CB  . ILE A 1 77  ? 15.054  -3.106  11.073  1.00 44.50  ? 79  ILE A CB  1 
ATOM   589  C CG1 . ILE A 1 77  ? 14.240  -4.355  11.546  1.00 46.16  ? 79  ILE A CG1 1 
ATOM   590  C CG2 . ILE A 1 77  ? 16.521  -3.261  11.413  1.00 43.61  ? 79  ILE A CG2 1 
ATOM   591  C CD1 . ILE A 1 77  ? 14.501  -4.823  13.041  1.00 48.36  ? 79  ILE A CD1 1 
ATOM   592  N N   . GLN A 1 78  ? 15.355  -0.148  9.955   1.00 47.15  ? 80  GLN A N   1 
ATOM   593  C CA  . GLN A 1 78  ? 16.227  0.884   9.390   1.00 50.00  ? 80  GLN A CA  1 
ATOM   594  C C   . GLN A 1 78  ? 16.120  2.197   10.190  1.00 54.65  ? 80  GLN A C   1 
ATOM   595  O O   . GLN A 1 78  ? 17.128  2.879   10.360  1.00 55.22  ? 80  GLN A O   1 
ATOM   596  C CB  . GLN A 1 78  ? 15.857  1.142   7.908   1.00 50.26  ? 80  GLN A CB  1 
ATOM   597  C CG  . GLN A 1 78  ? 16.964  1.740   7.027   1.00 52.54  ? 80  GLN A CG  1 
ATOM   598  C CD  . GLN A 1 78  ? 16.462  2.115   5.643   1.00 56.48  ? 80  GLN A CD  1 
ATOM   599  O OE1 . GLN A 1 78  ? 15.260  2.330   5.401   1.00 58.04  ? 80  GLN A OE1 1 
ATOM   600  N NE2 . GLN A 1 78  ? 17.365  2.188   4.685   1.00 56.64  ? 80  GLN A NE2 1 
ATOM   601  N N   . LEU A 1 79  ? 14.919  2.548   10.683  1.00 58.11  ? 81  LEU A N   1 
ATOM   602  C CA  . LEU A 1 79  ? 14.702  3.753   11.497  1.00 61.65  ? 81  LEU A CA  1 
ATOM   603  C C   . LEU A 1 79  ? 14.858  3.530   13.021  1.00 64.80  ? 81  LEU A C   1 
ATOM   604  O O   . LEU A 1 79  ? 15.291  4.444   13.713  1.00 65.30  ? 81  LEU A O   1 
ATOM   605  C CB  . LEU A 1 79  ? 13.321  4.335   11.209  1.00 62.14  ? 81  LEU A CB  1 
ATOM   606  C CG  . LEU A 1 79  ? 13.025  4.668   9.744   1.00 65.34  ? 81  LEU A CG  1 
ATOM   607  C CD1 . LEU A 1 79  ? 11.516  4.734   9.500   1.00 65.54  ? 81  LEU A CD1 1 
ATOM   608  C CD2 . LEU A 1 79  ? 13.739  5.987   9.295   1.00 67.46  ? 81  LEU A CD2 1 
ATOM   609  N N   . SER A 1 80  ? 14.509  2.357   13.545  1.00 66.74  ? 82  SER A N   1 
ATOM   610  C CA  . SER A 1 80  ? 14.499  2.113   14.984  1.00 69.59  ? 82  SER A CA  1 
ATOM   611  C C   . SER A 1 80  ? 15.763  1.455   15.555  1.00 71.20  ? 82  SER A C   1 
ATOM   612  O O   . SER A 1 80  ? 15.854  1.319   16.779  1.00 72.06  ? 82  SER A O   1 
ATOM   613  C CB  . SER A 1 80  ? 13.288  1.256   15.349  1.00 72.88  ? 82  SER A CB  1 
ATOM   614  O OG  . SER A 1 80  ? 13.501  -0.144  15.189  1.00 77.50  ? 82  SER A OG  1 
ATOM   615  N N   . SER A 1 81  ? 16.722  1.045   14.712  1.00 71.19  ? 83  SER A N   1 
ATOM   616  C CA  . SER A 1 81  ? 17.829  0.220   15.187  1.00 71.61  ? 83  SER A CA  1 
ATOM   617  C C   . SER A 1 81  ? 19.135  0.854   14.817  1.00 72.18  ? 83  SER A C   1 
ATOM   618  O O   . SER A 1 81  ? 19.247  1.445   13.743  1.00 71.76  ? 83  SER A O   1 
ATOM   619  C CB  . SER A 1 81  ? 17.748  -1.200  14.617  1.00 72.14  ? 83  SER A CB  1 
ATOM   620  O OG  . SER A 1 81  ? 16.557  -1.882  14.977  1.00 74.25  ? 83  SER A OG  1 
ATOM   621  N N   . ASN A 1 82  ? 20.127  0.725   15.717  1.00 73.37  ? 84  ASN A N   1 
ATOM   622  C CA  . ASN A 1 82  ? 21.501  1.175   15.486  1.00 75.54  ? 84  ASN A CA  1 
ATOM   623  C C   . ASN A 1 82  ? 22.467  -0.023  15.493  1.00 75.94  ? 84  ASN A C   1 
ATOM   624  O O   . ASN A 1 82  ? 22.193  -1.062  16.095  1.00 75.84  ? 84  ASN A O   1 
ATOM   625  C CB  . ASN A 1 82  ? 21.935  2.223   16.552  1.00 78.14  ? 84  ASN A CB  1 
ATOM   626  C CG  . ASN A 1 82  ? 21.792  3.682   16.149  1.00 83.57  ? 84  ASN A CG  1 
ATOM   627  O OD1 . ASN A 1 82  ? 21.275  4.042   15.067  1.00 84.76  ? 84  ASN A OD1 1 
ATOM   628  N ND2 . ASN A 1 82  ? 22.244  4.573   17.033  1.00 85.22  ? 84  ASN A ND2 1 
ATOM   629  N N   . LEU A 1 83  ? 23.611  0.155   14.827  1.00 76.04  ? 85  LEU A N   1 
ATOM   630  C CA  . LEU A 1 83  ? 24.532  -0.927  14.520  1.00 76.41  ? 85  LEU A CA  1 
ATOM   631  C C   . LEU A 1 83  ? 25.505  -1.234  15.677  1.00 76.47  ? 85  LEU A C   1 
ATOM   632  O O   . LEU A 1 83  ? 26.323  -0.378  16.038  1.00 76.48  ? 85  LEU A O   1 
ATOM   633  C CB  . LEU A 1 83  ? 25.307  -0.531  13.264  1.00 76.72  ? 85  LEU A CB  1 
ATOM   634  C CG  . LEU A 1 83  ? 26.172  -1.597  12.628  1.00 77.66  ? 85  LEU A CG  1 
ATOM   635  C CD1 . LEU A 1 83  ? 25.323  -2.671  11.955  1.00 77.87  ? 85  LEU A CD1 1 
ATOM   636  C CD2 . LEU A 1 83  ? 27.103  -0.965  11.645  1.00 78.45  ? 85  LEU A CD2 1 
ATOM   637  N N   . MET A 1 84  ? 25.416  -2.462  16.241  1.00 75.69  ? 86  MET A N   1 
ATOM   638  C CA  . MET A 1 84  ? 26.239  -2.905  17.377  1.00 75.25  ? 86  MET A CA  1 
ATOM   639  C C   . MET A 1 84  ? 27.100  -4.073  16.942  1.00 72.82  ? 86  MET A C   1 
ATOM   640  O O   . MET A 1 84  ? 26.529  -5.091  16.554  1.00 73.00  ? 86  MET A O   1 
ATOM   641  C CB  . MET A 1 84  ? 25.341  -3.412  18.527  1.00 77.28  ? 86  MET A CB  1 
ATOM   642  C CG  . MET A 1 84  ? 24.766  -2.317  19.428  1.00 81.78  ? 86  MET A CG  1 
ATOM   643  S SD  . MET A 1 84  ? 23.690  -2.999  20.728  1.00 90.82  ? 86  MET A SD  1 
ATOM   644  C CE  . MET A 1 84  ? 22.284  -3.688  19.705  1.00 86.43  ? 86  MET A CE  1 
ATOM   645  N N   . PRO A 1 85  ? 28.439  -3.991  16.976  1.00 70.58  ? 87  PRO A N   1 
ATOM   646  C CA  . PRO A 1 85  ? 29.237  -5.214  16.767  1.00 69.03  ? 87  PRO A CA  1 
ATOM   647  C C   . PRO A 1 85  ? 28.968  -6.297  17.814  1.00 66.61  ? 87  PRO A C   1 
ATOM   648  O O   . PRO A 1 85  ? 28.355  -6.033  18.856  1.00 66.70  ? 87  PRO A O   1 
ATOM   649  C CB  . PRO A 1 85  ? 30.698  -4.721  16.736  1.00 70.38  ? 87  PRO A CB  1 
ATOM   650  C CG  . PRO A 1 85  ? 30.613  -3.223  16.550  1.00 71.23  ? 87  PRO A CG  1 
ATOM   651  C CD  . PRO A 1 85  ? 29.297  -2.806  17.174  1.00 70.14  ? 87  PRO A CD  1 
ATOM   652  N N   . GLY A 1 86  ? 29.412  -7.516  17.511  1.00 64.39  ? 88  GLY A N   1 
ATOM   653  C CA  . GLY A 1 86  ? 29.065  -8.710  18.270  1.00 62.94  ? 88  GLY A CA  1 
ATOM   654  C C   . GLY A 1 86  ? 27.703  -9.290  17.914  1.00 60.75  ? 88  GLY A C   1 
ATOM   655  O O   . GLY A 1 86  ? 27.450  -10.481 18.139  1.00 60.82  ? 88  GLY A O   1 
ATOM   656  N N   . CYS A 1 87  ? 26.811  -8.458  17.357  1.00 58.64  ? 89  CYS A N   1 
ATOM   657  C CA  . CYS A 1 87  ? 25.482  -8.883  16.966  1.00 57.42  ? 89  CYS A CA  1 
ATOM   658  C C   . CYS A 1 87  ? 25.463  -9.615  15.588  1.00 53.14  ? 89  CYS A C   1 
ATOM   659  O O   . CYS A 1 87  ? 26.391  -9.527  14.767  1.00 52.33  ? 89  CYS A O   1 
ATOM   660  C CB  . CYS A 1 87  ? 24.536  -7.688  16.973  1.00 59.75  ? 89  CYS A CB  1 
ATOM   661  S SG  . CYS A 1 87  ? 24.327  -6.936  18.610  1.00 70.20  ? 89  CYS A SG  1 
ATOM   662  N N   . ASP A 1 88  ? 24.396  -10.358 15.373  1.00 49.63  ? 90  ASP A N   1 
ATOM   663  C CA  . ASP A 1 88  ? 24.118  -10.971 14.106  1.00 46.02  ? 90  ASP A CA  1 
ATOM   664  C C   . ASP A 1 88  ? 22.654  -10.826 13.840  1.00 41.25  ? 90  ASP A C   1 
ATOM   665  O O   . ASP A 1 88  ? 21.840  -10.926 14.752  1.00 41.65  ? 90  ASP A O   1 
ATOM   666  C CB  . ASP A 1 88  ? 24.494  -12.445 14.079  1.00 49.05  ? 90  ASP A CB  1 
ATOM   667  C CG  . ASP A 1 88  ? 25.847  -12.841 14.669  1.00 56.36  ? 90  ASP A CG  1 
ATOM   668  O OD1 . ASP A 1 88  ? 26.806  -12.067 14.524  1.00 56.26  ? 90  ASP A OD1 1 
ATOM   669  O OD2 . ASP A 1 88  ? 25.941  -13.949 15.254  1.00 60.49  ? 90  ASP A OD2 1 
ATOM   670  N N   . TYR A 1 89  ? 22.316  -10.572 12.587  1.00 37.02  ? 91  TYR A N   1 
ATOM   671  C CA  . TYR A 1 89  ? 20.966  -10.709 12.081  1.00 33.93  ? 91  TYR A CA  1 
ATOM   672  C C   . TYR A 1 89  ? 20.943  -11.822 11.038  1.00 28.94  ? 91  TYR A C   1 
ATOM   673  O O   . TYR A 1 89  ? 21.909  -12.017 10.286  1.00 27.96  ? 91  TYR A O   1 
ATOM   674  C CB  . TYR A 1 89  ? 20.493  -9.396  11.461  1.00 35.71  ? 91  TYR A CB  1 
ATOM   675  C CG  . TYR A 1 89  ? 20.258  -8.284  12.460  1.00 38.82  ? 91  TYR A CG  1 
ATOM   676  C CD1 . TYR A 1 89  ? 21.308  -7.518  12.931  1.00 41.16  ? 91  TYR A CD1 1 
ATOM   677  C CD2 . TYR A 1 89  ? 18.975  -7.977  12.903  1.00 42.34  ? 91  TYR A CD2 1 
ATOM   678  C CE1 . TYR A 1 89  ? 21.093  -6.488  13.840  1.00 43.94  ? 91  TYR A CE1 1 
ATOM   679  C CE2 . TYR A 1 89  ? 18.746  -6.947  13.803  1.00 44.26  ? 91  TYR A CE2 1 
ATOM   680  C CZ  . TYR A 1 89  ? 19.811  -6.194  14.262  1.00 46.65  ? 91  TYR A CZ  1 
ATOM   681  O OH  . TYR A 1 89  ? 19.604  -5.149  15.136  1.00 52.29  ? 91  TYR A OH  1 
ATOM   682  N N   . SER A 1 90  ? 19.849  -12.550 11.004  1.00 26.72  ? 92  SER A N   1 
ATOM   683  C CA  . SER A 1 90  ? 19.635  -13.679 10.104  1.00 24.08  ? 92  SER A CA  1 
ATOM   684  C C   . SER A 1 90  ? 18.208  -13.640 9.621   1.00 22.21  ? 92  SER A C   1 
ATOM   685  O O   . SER A 1 90  ? 17.313  -13.476 10.441  1.00 20.75  ? 92  SER A O   1 
ATOM   686  C CB  . SER A 1 90  ? 19.816  -14.997 10.834  1.00 25.51  ? 92  SER A CB  1 
ATOM   687  O OG  . SER A 1 90  ? 21.115  -15.127 11.356  1.00 32.92  ? 92  SER A OG  1 
ATOM   688  N N   . LEU A 1 91  ? 17.992  -13.783 8.292   1.00 21.40  ? 93  LEU A N   1 
ATOM   689  C CA  . LEU A 1 91  ? 16.696  -14.063 7.739   1.00 21.87  ? 93  LEU A CA  1 
ATOM   690  C C   . LEU A 1 91  ? 16.669  -15.467 7.229   1.00 21.68  ? 93  LEU A C   1 
ATOM   691  O O   . LEU A 1 91  ? 17.371  -15.750 6.278   1.00 21.51  ? 93  LEU A O   1 
ATOM   692  C CB  . LEU A 1 91  ? 16.351  -13.098 6.617   1.00 22.23  ? 93  LEU A CB  1 
ATOM   693  C CG  . LEU A 1 91  ? 14.886  -13.196 6.099   1.00 22.02  ? 93  LEU A CG  1 
ATOM   694  C CD1 . LEU A 1 91  ? 13.911  -12.563 7.106   1.00 23.44  ? 93  LEU A CD1 1 
ATOM   695  C CD2 . LEU A 1 91  ? 14.715  -12.556 4.741   1.00 22.37  ? 93  LEU A CD2 1 
ATOM   696  N N   . PHE A 1 92  ? 15.848  -16.361 7.845   1.00 21.32  ? 94  PHE A N   1 
ATOM   697  C CA  . PHE A 1 92  ? 15.745  -17.754 7.431   1.00 22.70  ? 94  PHE A CA  1 
ATOM   698  C C   . PHE A 1 92  ? 14.321  -18.110 7.100   1.00 24.04  ? 94  PHE A C   1 
ATOM   699  O O   . PHE A 1 92  ? 13.378  -17.536 7.641   1.00 24.96  ? 94  PHE A O   1 
ATOM   700  C CB  . PHE A 1 92  ? 16.276  -18.711 8.514   1.00 22.31  ? 94  PHE A CB  1 
ATOM   701  C CG  . PHE A 1 92  ? 17.777  -18.884 8.485   1.00 22.40  ? 94  PHE A CG  1 
ATOM   702  C CD1 . PHE A 1 92  ? 18.611  -17.839 8.811   1.00 23.47  ? 94  PHE A CD1 1 
ATOM   703  C CD2 . PHE A 1 92  ? 18.342  -20.065 8.063   1.00 22.78  ? 94  PHE A CD2 1 
ATOM   704  C CE1 . PHE A 1 92  ? 19.981  -17.983 8.712   1.00 24.34  ? 94  PHE A CE1 1 
ATOM   705  C CE2 . PHE A 1 92  ? 19.715  -20.214 8.004   1.00 23.85  ? 94  PHE A CE2 1 
ATOM   706  C CZ  . PHE A 1 92  ? 20.516  -19.177 8.325   1.00 24.27  ? 94  PHE A CZ  1 
ATOM   707  N N   . LYS A 1 93  ? 14.134  -19.077 6.209   1.00 23.54  ? 95  LYS A N   1 
ATOM   708  C CA  . LYS A 1 93  ? 12.800  -19.623 5.945   1.00 25.31  ? 95  LYS A CA  1 
ATOM   709  C C   . LYS A 1 93  ? 12.153  -20.095 7.251   1.00 27.16  ? 95  LYS A C   1 
ATOM   710  O O   . LYS A 1 93  ? 12.823  -20.550 8.186   1.00 26.65  ? 95  LYS A O   1 
ATOM   711  C CB  . LYS A 1 93  ? 12.863  -20.756 4.941   1.00 26.94  ? 95  LYS A CB  1 
ATOM   712  C CG  . LYS A 1 93  ? 13.178  -20.269 3.542   1.00 25.56  ? 95  LYS A CG  1 
ATOM   713  C CD  . LYS A 1 93  ? 13.348  -21.416 2.628   1.00 25.68  ? 95  LYS A CD  1 
ATOM   714  C CE  . LYS A 1 93  ? 13.551  -20.883 1.253   1.00 27.16  ? 95  LYS A CE  1 
ATOM   715  N NZ  . LYS A 1 93  ? 13.972  -21.908 0.285   1.00 27.80  ? 95  LYS A NZ  1 
ATOM   716  N N   . ASP A 1 94  ? 10.864  -19.927 7.330   1.00 29.78  ? 96  ASP A N   1 
ATOM   717  C CA  . ASP A 1 94  ? 10.083  -20.339 8.500   1.00 32.23  ? 96  ASP A CA  1 
ATOM   718  C C   . ASP A 1 94  ? 10.335  -21.839 8.777   1.00 31.14  ? 96  ASP A C   1 
ATOM   719  O O   . ASP A 1 94  ? 10.241  -22.623 7.844   1.00 31.40  ? 96  ASP A O   1 
ATOM   720  C CB  . ASP A 1 94  ? 8.597   -20.060 8.224   1.00 35.98  ? 96  ASP A CB  1 
ATOM   721  C CG  . ASP A 1 94  ? 7.684   -20.115 9.416   1.00 40.09  ? 96  ASP A CG  1 
ATOM   722  O OD1 . ASP A 1 94  ? 8.180   -19.946 10.552  1.00 41.95  ? 96  ASP A OD1 1 
ATOM   723  O OD2 . ASP A 1 94  ? 6.480   -20.308 9.214   1.00 41.65  ? 96  ASP A OD2 1 
ATOM   724  N N   . GLY A 1 95  ? 10.744  -22.159 10.009  1.00 30.01  ? 97  GLY A N   1 
ATOM   725  C CA  . GLY A 1 95  ? 11.012  -23.503 10.460  1.00 29.97  ? 97  GLY A CA  1 
ATOM   726  C C   . GLY A 1 95  ? 12.457  -23.945 10.466  1.00 31.24  ? 97  GLY A C   1 
ATOM   727  O O   . GLY A 1 95  ? 12.743  -25.083 10.825  1.00 32.12  ? 97  GLY A O   1 
ATOM   728  N N   . ILE A 1 96  ? 13.383  -23.080 10.048  1.00 31.32  ? 98  ILE A N   1 
ATOM   729  C CA  . ILE A 1 96  ? 14.824  -23.340 10.058  1.00 30.24  ? 98  ILE A CA  1 
ATOM   730  C C   . ILE A 1 96  ? 15.416  -22.355 11.055  1.00 30.38  ? 98  ILE A C   1 
ATOM   731  O O   . ILE A 1 96  ? 15.360  -21.139 10.837  1.00 28.99  ? 98  ILE A O   1 
ATOM   732  C CB  . ILE A 1 96  ? 15.458  -23.118 8.655   1.00 29.53  ? 98  ILE A CB  1 
ATOM   733  C CG1 . ILE A 1 96  ? 14.762  -23.972 7.552   1.00 29.82  ? 98  ILE A CG1 1 
ATOM   734  C CG2 . ILE A 1 96  ? 16.949  -23.364 8.720   1.00 29.60  ? 98  ILE A CG2 1 
ATOM   735  C CD1 . ILE A 1 96  ? 15.313  -23.749 6.155   1.00 30.90  ? 98  ILE A CD1 1 
ATOM   736  N N   . GLU A 1 97  ? 15.979  -22.874 12.139  1.00 31.89  ? 99  GLU A N   1 
ATOM   737  C CA  . GLU A 1 97  ? 16.753  -22.027 13.050  1.00 33.95  ? 99  GLU A CA  1 
ATOM   738  C C   . GLU A 1 97  ? 18.069  -21.587 12.393  1.00 32.54  ? 99  GLU A C   1 
ATOM   739  O O   . GLU A 1 97  ? 18.665  -22.335 11.602  1.00 31.45  ? 99  GLU A O   1 
ATOM   740  C CB  . GLU A 1 97  ? 17.041  -22.746 14.367  1.00 40.30  ? 99  GLU A CB  1 
ATOM   741  C CG  . GLU A 1 97  ? 15.796  -23.047 15.189  1.00 51.18  ? 99  GLU A CG  1 
ATOM   742  C CD  . GLU A 1 97  ? 16.078  -23.572 16.582  1.00 65.32  ? 99  GLU A CD  1 
ATOM   743  O OE1 . GLU A 1 97  ? 15.096  -23.887 17.294  1.00 71.17  ? 99  GLU A OE1 1 
ATOM   744  O OE2 . GLU A 1 97  ? 17.269  -23.666 16.966  1.00 67.58  ? 99  GLU A OE2 1 
ATOM   745  N N   . PRO A 1 98  ? 18.532  -20.363 12.707  1.00 32.56  ? 100 PRO A N   1 
ATOM   746  C CA  . PRO A 1 98  ? 19.777  -19.870 12.107  1.00 33.57  ? 100 PRO A CA  1 
ATOM   747  C C   . PRO A 1 98  ? 21.034  -20.424 12.765  1.00 34.13  ? 100 PRO A C   1 
ATOM   748  O O   . PRO A 1 98  ? 21.921  -19.668 13.085  1.00 33.93  ? 100 PRO A O   1 
ATOM   749  C CB  . PRO A 1 98  ? 19.630  -18.351 12.280  1.00 34.44  ? 100 PRO A CB  1 
ATOM   750  C CG  . PRO A 1 98  ? 18.938  -18.218 13.572  1.00 34.16  ? 100 PRO A CG  1 
ATOM   751  C CD  . PRO A 1 98  ? 17.939  -19.343 13.602  1.00 31.11  ? 100 PRO A CD  1 
ATOM   752  N N   . MET A 1 99  ? 21.109  -21.741 12.940  1.00 35.51  ? 101 MET A N   1 
ATOM   753  C CA  . MET A 1 99  ? 22.224  -22.464 13.527  1.00 38.14  ? 101 MET A CA  1 
ATOM   754  C C   . MET A 1 99  ? 22.548  -23.661 12.614  1.00 37.91  ? 101 MET A C   1 
ATOM   755  O O   . MET A 1 99  ? 21.644  -24.320 12.075  1.00 37.25  ? 101 MET A O   1 
ATOM   756  C CB  . MET A 1 99  ? 21.831  -23.015 14.911  1.00 42.99  ? 101 MET A CB  1 
ATOM   757  C CG  . MET A 1 99  ? 21.442  -21.936 15.945  1.00 50.71  ? 101 MET A CG  1 
ATOM   758  S SD  . MET A 1 99  ? 22.842  -20.872 16.465  1.00 71.42  ? 101 MET A SD  1 
ATOM   759  C CE  . MET A 1 99  ? 22.097  -20.108 17.992  1.00 73.45  ? 101 MET A CE  1 
ATOM   760  N N   . TRP A 1 100 ? 23.828  -23.944 12.446  1.00 38.89  ? 102 TRP A N   1 
ATOM   761  C CA  . TRP A 1 100 ? 24.271  -24.982 11.514  1.00 41.05  ? 102 TRP A CA  1 
ATOM   762  C C   . TRP A 1 100 ? 23.829  -26.388 11.971  1.00 41.50  ? 102 TRP A C   1 
ATOM   763  O O   . TRP A 1 100 ? 23.737  -27.268 11.135  1.00 42.68  ? 102 TRP A O   1 
ATOM   764  C CB  . TRP A 1 100 ? 25.808  -24.881 11.224  1.00 41.82  ? 102 TRP A CB  1 
ATOM   765  C CG  . TRP A 1 100 ? 26.724  -25.668 12.126  1.00 43.68  ? 102 TRP A CG  1 
ATOM   766  C CD1 . TRP A 1 100 ? 27.256  -25.259 13.317  1.00 45.19  ? 102 TRP A CD1 1 
ATOM   767  C CD2 . TRP A 1 100 ? 27.250  -26.998 11.885  1.00 43.57  ? 102 TRP A CD2 1 
ATOM   768  N NE1 . TRP A 1 100 ? 28.044  -26.271 13.856  1.00 45.43  ? 102 TRP A NE1 1 
ATOM   769  C CE2 . TRP A 1 100 ? 28.067  -27.336 12.988  1.00 44.51  ? 102 TRP A CE2 1 
ATOM   770  C CE3 . TRP A 1 100 ? 27.108  -27.927 10.842  1.00 43.41  ? 102 TRP A CE3 1 
ATOM   771  C CZ2 . TRP A 1 100 ? 28.753  -28.559 13.066  1.00 44.73  ? 102 TRP A CZ2 1 
ATOM   772  C CZ3 . TRP A 1 100 ? 27.792  -29.127 10.915  1.00 44.01  ? 102 TRP A CZ3 1 
ATOM   773  C CH2 . TRP A 1 100 ? 28.606  -29.436 12.016  1.00 44.15  ? 102 TRP A CH2 1 
ATOM   774  N N   . GLU A 1 101 ? 23.539  -26.591 13.278  1.00 40.64  ? 103 GLU A N   1 
ATOM   775  C CA  . GLU A 1 101 ? 23.052  -27.854 13.834  1.00 40.42  ? 103 GLU A CA  1 
ATOM   776  C C   . GLU A 1 101 ? 21.650  -28.231 13.362  1.00 37.96  ? 103 GLU A C   1 
ATOM   777  O O   . GLU A 1 101 ? 21.286  -29.401 13.453  1.00 37.28  ? 103 GLU A O   1 
ATOM   778  C CB  . GLU A 1 101 ? 23.061  -27.805 15.368  1.00 46.14  ? 103 GLU A CB  1 
ATOM   779  C CG  . GLU A 1 101 ? 24.453  -27.623 15.987  1.00 54.03  ? 103 GLU A CG  1 
ATOM   780  C CD  . GLU A 1 101 ? 24.919  -26.193 16.247  1.00 62.02  ? 103 GLU A CD  1 
ATOM   781  O OE1 . GLU A 1 101 ? 24.430  -25.249 15.580  1.00 57.93  ? 103 GLU A OE1 1 
ATOM   782  O OE2 . GLU A 1 101 ? 25.794  -26.025 17.131  1.00 68.41  ? 103 GLU A OE2 1 
ATOM   783  N N   . ASP A 1 102 ? 20.859  -27.269 12.841  1.00 36.29  ? 104 ASP A N   1 
ATOM   784  C CA  . ASP A 1 102 ? 19.530  -27.529 12.303  1.00 34.89  ? 104 ASP A CA  1 
ATOM   785  C C   . ASP A 1 102 ? 19.605  -28.545 11.189  1.00 36.05  ? 104 ASP A C   1 
ATOM   786  O O   . ASP A 1 102 ? 20.550  -28.516 10.393  1.00 36.70  ? 104 ASP A O   1 
ATOM   787  C CB  . ASP A 1 102 ? 18.890  -26.221 11.795  1.00 34.23  ? 104 ASP A CB  1 
ATOM   788  C CG  . ASP A 1 102 ? 17.435  -26.251 11.347  1.00 34.85  ? 104 ASP A CG  1 
ATOM   789  O OD1 . ASP A 1 102 ? 17.142  -26.849 10.298  1.00 35.61  ? 104 ASP A OD1 1 
ATOM   790  O OD2 . ASP A 1 102 ? 16.605  -25.647 12.022  1.00 36.68  ? 104 ASP A OD2 1 
ATOM   791  N N   . GLU A 1 103 ? 18.615  -29.465 11.137  1.00 36.51  ? 105 GLU A N   1 
ATOM   792  C CA  . GLU A 1 103 ? 18.499  -30.469 10.079  1.00 36.51  ? 105 GLU A CA  1 
ATOM   793  C C   . GLU A 1 103 ? 18.649  -29.891 8.658   1.00 34.62  ? 105 GLU A C   1 
ATOM   794  O O   . GLU A 1 103 ? 19.235  -30.559 7.808   1.00 34.18  ? 105 GLU A O   1 
ATOM   795  C CB  . GLU A 1 103 ? 17.159  -31.212 10.174  1.00 41.58  ? 105 GLU A CB  1 
ATOM   796  C CG  . GLU A 1 103 ? 17.274  -32.739 10.085  1.00 53.63  ? 105 GLU A CG  1 
ATOM   797  C CD  . GLU A 1 103 ? 18.060  -33.395 11.207  1.00 65.41  ? 105 GLU A CD  1 
ATOM   798  O OE1 . GLU A 1 103 ? 18.365  -34.602 11.076  1.00 70.94  ? 105 GLU A OE1 1 
ATOM   799  O OE2 . GLU A 1 103 ? 18.374  -32.714 12.212  1.00 68.18  ? 105 GLU A OE2 1 
ATOM   800  N N   . LYS A 1 104 ? 18.137  -28.663 8.407   1.00 33.10  ? 106 LYS A N   1 
ATOM   801  C CA  . LYS A 1 104 ? 18.258  -28.014 7.095   1.00 32.14  ? 106 LYS A CA  1 
ATOM   802  C C   . LYS A 1 104 ? 19.560  -27.299 6.840   1.00 31.07  ? 106 LYS A C   1 
ATOM   803  O O   . LYS A 1 104 ? 19.749  -26.855 5.710   1.00 30.97  ? 106 LYS A O   1 
ATOM   804  C CB  . LYS A 1 104 ? 17.112  -27.060 6.860   1.00 33.62  ? 106 LYS A CB  1 
ATOM   805  C CG  . LYS A 1 104 ? 15.755  -27.742 6.912   1.00 39.59  ? 106 LYS A CG  1 
ATOM   806  C CD  . LYS A 1 104 ? 15.533  -28.745 5.816   1.00 46.22  ? 106 LYS A CD  1 
ATOM   807  C CE  . LYS A 1 104 ? 14.072  -28.705 5.403   1.00 53.47  ? 106 LYS A CE  1 
ATOM   808  N NZ  . LYS A 1 104 ? 13.703  -29.831 4.516   1.00 58.17  ? 106 LYS A NZ  1 
ATOM   809  N N   . ASN A 1 105 ? 20.465  -27.177 7.840   1.00 29.96  ? 107 ASN A N   1 
ATOM   810  C CA  . ASN A 1 105 ? 21.752  -26.520 7.646   1.00 29.65  ? 107 ASN A CA  1 
ATOM   811  C C   . ASN A 1 105 ? 22.966  -27.464 7.852   1.00 30.51  ? 107 ASN A C   1 
ATOM   812  O O   . ASN A 1 105 ? 24.053  -27.180 7.321   1.00 28.25  ? 107 ASN A O   1 
ATOM   813  C CB  . ASN A 1 105 ? 21.862  -25.378 8.609   1.00 29.77  ? 107 ASN A CB  1 
ATOM   814  C CG  . ASN A 1 105 ? 20.853  -24.273 8.383   1.00 31.37  ? 107 ASN A CG  1 
ATOM   815  O OD1 . ASN A 1 105 ? 20.526  -23.940 7.243   1.00 30.05  ? 107 ASN A OD1 1 
ATOM   816  N ND2 . ASN A 1 105 ? 20.355  -23.677 9.473   1.00 32.97  ? 107 ASN A ND2 1 
ATOM   817  N N   . LYS A 1 106 ? 22.798  -28.568 8.629   1.00 31.44  ? 108 LYS A N   1 
ATOM   818  C CA  . LYS A 1 106 ? 23.966  -29.363 9.025   1.00 33.53  ? 108 LYS A CA  1 
ATOM   819  C C   . LYS A 1 106 ? 24.698  -29.962 7.847   1.00 32.36  ? 108 LYS A C   1 
ATOM   820  O O   . LYS A 1 106 ? 25.923  -30.020 7.881   1.00 32.59  ? 108 LYS A O   1 
ATOM   821  C CB  . LYS A 1 106 ? 23.658  -30.424 10.103  1.00 38.06  ? 108 LYS A CB  1 
ATOM   822  C CG  . LYS A 1 106 ? 22.613  -31.467 9.764   1.00 47.43  ? 108 LYS A CG  1 
ATOM   823  C CD  . LYS A 1 106 ? 22.179  -32.137 11.067  1.00 57.52  ? 108 LYS A CD  1 
ATOM   824  C CE  . LYS A 1 106 ? 21.360  -33.385 10.838  1.00 66.97  ? 108 LYS A CE  1 
ATOM   825  N NZ  . LYS A 1 106 ? 20.791  -33.917 12.117  1.00 71.22  ? 108 LYS A NZ  1 
ATOM   826  N N   . ARG A 1 107 ? 23.991  -30.349 6.790   1.00 31.14  ? 109 ARG A N   1 
ATOM   827  C CA  . ARG A 1 107 ? 24.642  -30.849 5.564   1.00 30.54  ? 109 ARG A CA  1 
ATOM   828  C C   . ARG A 1 107 ? 24.990  -29.764 4.523   1.00 28.98  ? 109 ARG A C   1 
ATOM   829  O O   . ARG A 1 107 ? 25.347  -30.084 3.384   1.00 26.88  ? 109 ARG A O   1 
ATOM   830  C CB  . ARG A 1 107 ? 23.716  -31.907 4.950   1.00 33.62  ? 109 ARG A CB  1 
ATOM   831  C CG  . ARG A 1 107 ? 23.559  -33.147 5.873   1.00 39.13  ? 109 ARG A CG  1 
ATOM   832  C CD  . ARG A 1 107 ? 22.554  -34.145 5.335   1.00 45.58  ? 109 ARG A CD  1 
ATOM   833  N NE  . ARG A 1 107 ? 21.225  -33.546 5.152   1.00 53.81  ? 109 ARG A NE  1 
ATOM   834  C CZ  . ARG A 1 107 ? 20.337  -33.348 6.126   1.00 57.99  ? 109 ARG A CZ  1 
ATOM   835  N NH1 . ARG A 1 107 ? 20.621  -33.705 7.386   1.00 56.73  ? 109 ARG A NH1 1 
ATOM   836  N NH2 . ARG A 1 107 ? 19.164  -32.785 5.854   1.00 58.86  ? 109 ARG A NH2 1 
ATOM   837  N N   . GLY A 1 108 ? 24.889  -28.483 4.922   1.00 28.63  ? 110 GLY A N   1 
ATOM   838  C CA  . GLY A 1 108 ? 24.880  -27.346 4.011   1.00 27.15  ? 110 GLY A CA  1 
ATOM   839  C C   . GLY A 1 108 ? 26.107  -26.499 4.146   1.00 27.05  ? 110 GLY A C   1 
ATOM   840  O O   . GLY A 1 108 ? 27.134  -26.947 4.664   1.00 27.80  ? 110 GLY A O   1 
ATOM   841  N N   . GLY A 1 109 ? 25.995  -25.269 3.672   1.00 25.73  ? 111 GLY A N   1 
ATOM   842  C CA  . GLY A 1 109 ? 27.050  -24.282 3.806   1.00 24.41  ? 111 GLY A CA  1 
ATOM   843  C C   . GLY A 1 109 ? 26.629  -22.903 3.369   1.00 23.74  ? 111 GLY A C   1 
ATOM   844  O O   . GLY A 1 109 ? 25.443  -22.624 3.257   1.00 22.89  ? 111 GLY A O   1 
ATOM   845  N N   . ARG A 1 110 ? 27.607  -22.039 3.108   1.00 23.32  ? 112 ARG A N   1 
ATOM   846  C CA  . ARG A 1 110 ? 27.372  -20.654 2.872   1.00 22.84  ? 112 ARG A CA  1 
ATOM   847  C C   . ARG A 1 110 ? 28.251  -20.104 1.761   1.00 23.65  ? 112 ARG A C   1 
ATOM   848  O O   . ARG A 1 110 ? 29.463  -20.398 1.715   1.00 24.24  ? 112 ARG A O   1 
ATOM   849  C CB  . ARG A 1 110 ? 27.565  -19.866 4.160   1.00 23.96  ? 112 ARG A CB  1 
ATOM   850  C CG  . ARG A 1 110 ? 29.005  -19.715 4.630   1.00 27.26  ? 112 ARG A CG  1 
ATOM   851  C CD  . ARG A 1 110 ? 29.066  -18.998 5.943   1.00 27.78  ? 112 ARG A CD  1 
ATOM   852  N NE  . ARG A 1 110 ? 30.455  -18.837 6.390   1.00 30.47  ? 112 ARG A NE  1 
ATOM   853  C CZ  . ARG A 1 110 ? 30.827  -18.224 7.511   1.00 34.73  ? 112 ARG A CZ  1 
ATOM   854  N NH1 . ARG A 1 110 ? 32.117  -18.136 7.834   1.00 39.49  ? 112 ARG A NH1 1 
ATOM   855  N NH2 . ARG A 1 110 ? 29.920  -17.696 8.319   1.00 32.80  ? 112 ARG A NH2 1 
ATOM   856  N N   . TRP A 1 111 ? 27.641  -19.305 0.887   1.00 22.80  ? 113 TRP A N   1 
ATOM   857  C CA  . TRP A 1 111 ? 28.363  -18.286 0.102   1.00 23.07  ? 113 TRP A CA  1 
ATOM   858  C C   . TRP A 1 111 ? 28.733  -17.088 0.952   1.00 22.17  ? 113 TRP A C   1 
ATOM   859  O O   . TRP A 1 111 ? 27.850  -16.405 1.454   1.00 21.09  ? 113 TRP A O   1 
ATOM   860  C CB  . TRP A 1 111 ? 27.564  -17.867 -1.109  1.00 23.00  ? 113 TRP A CB  1 
ATOM   861  C CG  . TRP A 1 111 ? 27.556  -18.935 -2.138  1.00 24.12  ? 113 TRP A CG  1 
ATOM   862  C CD1 . TRP A 1 111 ? 26.511  -19.741 -2.503  1.00 25.09  ? 113 TRP A CD1 1 
ATOM   863  C CD2 . TRP A 1 111 ? 28.634  -19.255 -3.013  1.00 24.74  ? 113 TRP A CD2 1 
ATOM   864  N NE1 . TRP A 1 111 ? 26.901  -20.562 -3.542  1.00 25.34  ? 113 TRP A NE1 1 
ATOM   865  C CE2 . TRP A 1 111 ? 28.218  -20.340 -3.814  1.00 24.98  ? 113 TRP A CE2 1 
ATOM   866  C CE3 . TRP A 1 111 ? 29.961  -18.814 -3.115  1.00 24.37  ? 113 TRP A CE3 1 
ATOM   867  C CZ2 . TRP A 1 111 ? 29.044  -20.900 -4.777  1.00 25.47  ? 113 TRP A CZ2 1 
ATOM   868  C CZ3 . TRP A 1 111 ? 30.779  -19.409 -4.050  1.00 24.85  ? 113 TRP A CZ3 1 
ATOM   869  C CH2 . TRP A 1 111 ? 30.308  -20.403 -4.886  1.00 25.50  ? 113 TRP A CH2 1 
ATOM   870  N N   . LEU A 1 112 ? 30.040  -16.823 1.131   1.00 23.37  ? 114 LEU A N   1 
ATOM   871  C CA  . LEU A 1 112 ? 30.491  -15.768 2.037   1.00 24.80  ? 114 LEU A CA  1 
ATOM   872  C C   . LEU A 1 112 ? 31.063  -14.515 1.344   1.00 26.54  ? 114 LEU A C   1 
ATOM   873  O O   . LEU A 1 112 ? 31.922  -14.598 0.454   1.00 27.56  ? 114 LEU A O   1 
ATOM   874  C CB  . LEU A 1 112 ? 31.479  -16.341 3.034   1.00 24.26  ? 114 LEU A CB  1 
ATOM   875  C CG  . LEU A 1 112 ? 32.069  -15.367 4.099   1.00 26.41  ? 114 LEU A CG  1 
ATOM   876  C CD1 . LEU A 1 112 ? 31.105  -14.972 5.108   1.00 25.02  ? 114 LEU A CD1 1 
ATOM   877  C CD2 . LEU A 1 112 ? 33.205  -16.031 4.845   1.00 28.31  ? 114 LEU A CD2 1 
ATOM   878  N N   . ILE A 1 113 ? 30.567  -13.328 1.758   1.00 26.41  ? 115 ILE A N   1 
ATOM   879  C CA  . ILE A 1 113 ? 31.140  -12.019 1.421   1.00 28.23  ? 115 ILE A CA  1 
ATOM   880  C C   . ILE A 1 113 ? 31.836  -11.473 2.721   1.00 26.74  ? 115 ILE A C   1 
ATOM   881  O O   . ILE A 1 113 ? 31.146  -11.301 3.731   1.00 24.95  ? 115 ILE A O   1 
ATOM   882  C CB  . ILE A 1 113 ? 29.969  -10.995 1.019   1.00 33.76  ? 115 ILE A CB  1 
ATOM   883  C CG1 . ILE A 1 113 ? 28.872  -11.602 0.140   1.00 36.21  ? 115 ILE A CG1 1 
ATOM   884  C CG2 . ILE A 1 113 ? 30.503  -9.778  0.407   1.00 36.32  ? 115 ILE A CG2 1 
ATOM   885  C CD1 . ILE A 1 113 ? 29.409  -12.418 -1.158  1.00 39.97  ? 115 ILE A CD1 1 
ATOM   886  N N   . THR A 1 114 ? 33.113  -11.154 2.714   1.00 28.11  ? 116 THR A N   1 
ATOM   887  C CA  . THR A 1 114 ? 33.742  -10.478 3.862   1.00 32.23  ? 116 THR A CA  1 
ATOM   888  C C   . THR A 1 114 ? 34.021  -9.024  3.516   1.00 35.12  ? 116 THR A C   1 
ATOM   889  O O   . THR A 1 114 ? 34.691  -8.749  2.519   1.00 36.20  ? 116 THR A O   1 
ATOM   890  C CB  . THR A 1 114 ? 35.007  -11.198 4.360   1.00 36.77  ? 116 THR A CB  1 
ATOM   891  O OG1 . THR A 1 114 ? 34.754  -12.606 4.462   1.00 38.74  ? 116 THR A OG1 1 
ATOM   892  C CG2 . THR A 1 114 ? 35.462  -10.699 5.773   1.00 38.55  ? 116 THR A CG2 1 
ATOM   893  N N   . LEU A 1 115 ? 33.497  -8.095  4.329   1.00 35.62  ? 117 LEU A N   1 
ATOM   894  C CA  . LEU A 1 115 ? 33.725  -6.668  4.197   1.00 37.34  ? 117 LEU A CA  1 
ATOM   895  C C   . LEU A 1 115 ? 34.861  -6.194  5.137   1.00 39.66  ? 117 LEU A C   1 
ATOM   896  O O   . LEU A 1 115 ? 34.902  -6.513  6.320   1.00 38.53  ? 117 LEU A O   1 
ATOM   897  C CB  . LEU A 1 115 ? 32.459  -5.888  4.554   1.00 37.18  ? 117 LEU A CB  1 
ATOM   898  C CG  . LEU A 1 115 ? 31.197  -6.196  3.739   1.00 38.21  ? 117 LEU A CG  1 
ATOM   899  C CD1 . LEU A 1 115 ? 30.102  -5.324  4.107   1.00 36.86  ? 117 LEU A CD1 1 
ATOM   900  C CD2 . LEU A 1 115 ? 31.426  -6.021  2.269   1.00 39.59  ? 117 LEU A CD2 1 
ATOM   901  N N   . ASN A 1 116 ? 35.748  -5.408  4.591   1.00 42.74  ? 118 ASN A N   1 
ATOM   902  C CA  . ASN A 1 116 ? 36.745  -4.673  5.365   1.00 46.74  ? 118 ASN A CA  1 
ATOM   903  C C   . ASN A 1 116 ? 36.080  -3.518  6.211   1.00 46.80  ? 118 ASN A C   1 
ATOM   904  O O   . ASN A 1 116 ? 34.921  -3.161  5.994   1.00 44.83  ? 118 ASN A O   1 
ATOM   905  C CB  . ASN A 1 116 ? 37.828  -4.162  4.407   1.00 51.38  ? 118 ASN A CB  1 
ATOM   906  C CG  . ASN A 1 116 ? 38.765  -3.216  5.050   1.00 62.36  ? 118 ASN A CG  1 
ATOM   907  O OD1 . ASN A 1 116 ? 38.593  -1.985  4.909   1.00 67.04  ? 118 ASN A OD1 1 
ATOM   908  N ND2 . ASN A 1 116 ? 39.750  -3.768  5.797   1.00 64.07  ? 118 ASN A ND2 1 
ATOM   909  N N   . LYS A 1 117 ? 36.847  -2.960  7.161   1.00 49.03  ? 119 LYS A N   1 
ATOM   910  C CA  . LYS A 1 117 ? 36.421  -1.933  8.125   1.00 51.70  ? 119 LYS A CA  1 
ATOM   911  C C   . LYS A 1 117 ? 35.824  -0.712  7.425   1.00 51.55  ? 119 LYS A C   1 
ATOM   912  O O   . LYS A 1 117 ? 34.790  -0.203  7.858   1.00 51.90  ? 119 LYS A O   1 
ATOM   913  C CB  . LYS A 1 117 ? 37.626  -1.494  9.002   1.00 56.40  ? 119 LYS A CB  1 
ATOM   914  C CG  . LYS A 1 117 ? 38.234  -2.594  9.895   1.00 63.25  ? 119 LYS A CG  1 
ATOM   915  C CD  . LYS A 1 117 ? 39.402  -3.393  9.213   1.00 70.35  ? 119 LYS A CD  1 
ATOM   916  C CE  . LYS A 1 117 ? 40.401  -3.974  10.200  1.00 74.76  ? 119 LYS A CE  1 
ATOM   917  N NZ  . LYS A 1 117 ? 40.919  -5.306  9.743   1.00 76.46  ? 119 LYS A NZ  1 
ATOM   918  N N   . GLN A 1 118 ? 36.476  -0.262  6.344   1.00 51.70  ? 120 GLN A N   1 
ATOM   919  C CA  . GLN A 1 118 ? 35.974  0.791   5.451   1.00 53.51  ? 120 GLN A CA  1 
ATOM   920  C C   . GLN A 1 118 ? 34.589  0.473   4.888   1.00 53.44  ? 120 GLN A C   1 
ATOM   921  O O   . GLN A 1 118 ? 33.689  1.314   4.929   1.00 53.32  ? 120 GLN A O   1 
ATOM   922  C CB  . GLN A 1 118 ? 36.951  0.983   4.269   1.00 57.49  ? 120 GLN A CB  1 
ATOM   923  C CG  . GLN A 1 118 ? 38.184  1.763   4.641   1.00 66.19  ? 120 GLN A CG  1 
ATOM   924  C CD  . GLN A 1 118 ? 39.387  1.538   3.745   1.00 75.29  ? 120 GLN A CD  1 
ATOM   925  O OE1 . GLN A 1 118 ? 39.977  2.534   3.309   1.00 76.80  ? 120 GLN A OE1 1 
ATOM   926  N NE2 . GLN A 1 118 ? 39.823  0.283   3.424   1.00 76.29  ? 120 GLN A NE2 1 
ATOM   927  N N   . GLN A 1 119 ? 34.424  -0.756  4.366   1.00 53.03  ? 121 GLN A N   1 
ATOM   928  C CA  . GLN A 1 119 ? 33.230  -1.159  3.646   1.00 51.76  ? 121 GLN A CA  1 
ATOM   929  C C   . GLN A 1 119 ? 32.016  -1.329  4.518   1.00 50.66  ? 121 GLN A C   1 
ATOM   930  O O   . GLN A 1 119 ? 30.958  -1.595  3.981   1.00 50.60  ? 121 GLN A O   1 
ATOM   931  C CB  . GLN A 1 119 ? 33.491  -2.426  2.858   1.00 51.93  ? 121 GLN A CB  1 
ATOM   932  C CG  . GLN A 1 119 ? 34.588  -2.336  1.841   1.00 51.91  ? 121 GLN A CG  1 
ATOM   933  C CD  . GLN A 1 119 ? 34.800  -3.717  1.340   1.00 57.00  ? 121 GLN A CD  1 
ATOM   934  O OE1 . GLN A 1 119 ? 35.556  -4.482  1.906   1.00 55.93  ? 121 GLN A OE1 1 
ATOM   935  N NE2 . GLN A 1 119 ? 34.100  -4.098  0.284   1.00 61.76  ? 121 GLN A NE2 1 
ATOM   936  N N   . ARG A 1 120 ? 32.117  -1.146  5.850   1.00 50.02  ? 122 ARG A N   1 
ATOM   937  C CA  . ARG A 1 120 ? 30.930  -1.119  6.705   1.00 50.29  ? 122 ARG A CA  1 
ATOM   938  C C   . ARG A 1 120 ? 30.074  0.053   6.299   1.00 50.02  ? 122 ARG A C   1 
ATOM   939  O O   . ARG A 1 120 ? 28.892  -0.094  5.947   1.00 50.34  ? 122 ARG A O   1 
ATOM   940  C CB  . ARG A 1 120 ? 31.295  -1.023  8.192   1.00 51.41  ? 122 ARG A CB  1 
ATOM   941  C CG  . ARG A 1 120 ? 30.086  -0.956  9.078   1.00 55.42  ? 122 ARG A CG  1 
ATOM   942  C CD  . ARG A 1 120 ? 30.498  -1.012  10.511  1.00 60.57  ? 122 ARG A CD  1 
ATOM   943  N NE  . ARG A 1 120 ? 30.725  -2.366  11.019  1.00 62.40  ? 122 ARG A NE  1 
ATOM   944  C CZ  . ARG A 1 120 ? 31.145  -2.641  12.256  1.00 64.31  ? 122 ARG A CZ  1 
ATOM   945  N NH1 . ARG A 1 120 ? 31.321  -3.895  12.636  1.00 64.88  ? 122 ARG A NH1 1 
ATOM   946  N NH2 . ARG A 1 120 ? 31.388  -1.658  13.124  1.00 63.41  ? 122 ARG A NH2 1 
ATOM   947  N N   . ARG A 1 121 ? 30.704  1.217   6.309   1.00 48.86  ? 123 ARG A N   1 
ATOM   948  C CA  . ARG A 1 121 ? 29.995  2.428   6.020   1.00 48.47  ? 123 ARG A CA  1 
ATOM   949  C C   . ARG A 1 121 ? 29.530  2.469   4.542   1.00 46.29  ? 123 ARG A C   1 
ATOM   950  O O   . ARG A 1 121 ? 28.396  2.843   4.284   1.00 46.45  ? 123 ARG A O   1 
ATOM   951  C CB  . ARG A 1 121 ? 30.844  3.625   6.426   1.00 51.68  ? 123 ARG A CB  1 
ATOM   952  C CG  . ARG A 1 121 ? 30.941  3.850   7.976   1.00 56.90  ? 123 ARG A CG  1 
ATOM   953  C CD  . ARG A 1 121 ? 31.451  5.245   8.393   1.00 62.89  ? 123 ARG A CD  1 
ATOM   954  N NE  . ARG A 1 121 ? 30.755  6.217   7.545   1.00 67.42  ? 123 ARG A NE  1 
ATOM   955  C CZ  . ARG A 1 121 ? 31.308  7.050   6.665   1.00 71.65  ? 123 ARG A CZ  1 
ATOM   956  N NH1 . ARG A 1 121 ? 30.538  7.850   5.931   1.00 70.40  ? 123 ARG A NH1 1 
ATOM   957  N NH2 . ARG A 1 121 ? 32.642  7.100   6.517   1.00 71.96  ? 123 ARG A NH2 1 
ATOM   958  N N   . SER A 1 122 ? 30.376  2.064   3.602   1.00 44.45  ? 124 SER A N   1 
ATOM   959  C CA  . SER A 1 122 ? 30.037  2.045   2.183   1.00 43.39  ? 124 SER A CA  1 
ATOM   960  C C   . SER A 1 122 ? 29.097  0.900   1.685   1.00 40.54  ? 124 SER A C   1 
ATOM   961  O O   . SER A 1 122 ? 28.165  1.191   0.935   1.00 41.29  ? 124 SER A O   1 
ATOM   962  C CB  . SER A 1 122 ? 31.314  2.016   1.361   1.00 46.92  ? 124 SER A CB  1 
ATOM   963  O OG  . SER A 1 122 ? 32.084  0.883   1.738   1.00 52.54  ? 124 SER A OG  1 
ATOM   964  N N   . ASP A 1 123 ? 29.321  -0.386  2.080   1.00 36.93  ? 125 ASP A N   1 
ATOM   965  C CA  . ASP A 1 123 ? 28.661  -1.532  1.437   1.00 34.34  ? 125 ASP A CA  1 
ATOM   966  C C   . ASP A 1 123 ? 27.769  -2.405  2.309   1.00 30.84  ? 125 ASP A C   1 
ATOM   967  O O   . ASP A 1 123 ? 27.040  -3.193  1.744   1.00 30.15  ? 125 ASP A O   1 
ATOM   968  C CB  . ASP A 1 123 ? 29.665  -2.455  0.763   1.00 38.16  ? 125 ASP A CB  1 
ATOM   969  C CG  . ASP A 1 123 ? 30.537  -1.816  -0.283  1.00 44.57  ? 125 ASP A CG  1 
ATOM   970  O OD1 . ASP A 1 123 ? 29.988  -1.179  -1.197  1.00 46.50  ? 125 ASP A OD1 1 
ATOM   971  O OD2 . ASP A 1 123 ? 31.773  -1.965  -0.190  1.00 46.36  ? 125 ASP A OD2 1 
ATOM   972  N N   . LEU A 1 124 ? 27.808  -2.311  3.641   1.00 29.78  ? 126 LEU A N   1 
ATOM   973  C CA  . LEU A 1 124 ? 27.048  -3.210  4.507   1.00 28.08  ? 126 LEU A CA  1 
ATOM   974  C C   . LEU A 1 124 ? 25.546  -3.130  4.216   1.00 26.15  ? 126 LEU A C   1 
ATOM   975  O O   . LEU A 1 124 ? 24.954  -4.142  3.931   1.00 25.78  ? 126 LEU A O   1 
ATOM   976  C CB  . LEU A 1 124 ? 27.310  -2.883  5.962   1.00 28.29  ? 126 LEU A CB  1 
ATOM   977  C CG  . LEU A 1 124 ? 26.651  -3.800  7.040   1.00 30.49  ? 126 LEU A CG  1 
ATOM   978  C CD1 . LEU A 1 124 ? 27.134  -5.244  6.922   1.00 29.69  ? 126 LEU A CD1 1 
ATOM   979  C CD2 . LEU A 1 124 ? 26.967  -3.300  8.464   1.00 31.65  ? 126 LEU A CD2 1 
ATOM   980  N N   . ASN A 1 125 ? 24.930  -1.938  4.274   1.00 25.26  ? 127 ASN A N   1 
ATOM   981  C CA  . ASN A 1 125 ? 23.496  -1.820  4.118   1.00 24.90  ? 127 ASN A CA  1 
ATOM   982  C C   . ASN A 1 125 ? 23.072  -2.191  2.712   1.00 24.11  ? 127 ASN A C   1 
ATOM   983  O O   . ASN A 1 125 ? 22.111  -2.890  2.526   1.00 23.51  ? 127 ASN A O   1 
ATOM   984  C CB  . ASN A 1 125 ? 23.037  -0.441  4.519   1.00 28.29  ? 127 ASN A CB  1 
ATOM   985  C CG  . ASN A 1 125 ? 23.261  -0.180  6.001   1.00 35.07  ? 127 ASN A CG  1 
ATOM   986  O OD1 . ASN A 1 125 ? 22.998  -1.022  6.854   1.00 38.90  ? 127 ASN A OD1 1 
ATOM   987  N ND2 . ASN A 1 125 ? 23.739  0.974   6.361   1.00 36.16  ? 127 ASN A ND2 1 
ATOM   988  N N   . ARG A 1 126 ? 23.798  -1.720  1.716   1.00 25.03  ? 128 ARG A N   1 
ATOM   989  C CA  . ARG A 1 126 ? 23.532  -2.054  0.299   1.00 23.56  ? 128 ARG A CA  1 
ATOM   990  C C   . ARG A 1 126 ? 23.622  -3.592  0.059   1.00 23.16  ? 128 ARG A C   1 
ATOM   991  O O   . ARG A 1 126 ? 22.706  -4.177  -0.473  1.00 21.97  ? 128 ARG A O   1 
ATOM   992  C CB  . ARG A 1 126 ? 24.559  -1.299  -0.606  1.00 22.10  ? 128 ARG A CB  1 
ATOM   993  C CG  . ARG A 1 126 ? 24.523  -1.648  -2.087  1.00 24.61  ? 128 ARG A CG  1 
ATOM   994  C CD  . ARG A 1 126 ? 23.119  -1.573  -2.694  1.00 30.29  ? 128 ARG A CD  1 
ATOM   995  N NE  . ARG A 1 126 ? 22.589  -0.213  -2.607  1.00 34.59  ? 128 ARG A NE  1 
ATOM   996  C CZ  . ARG A 1 126 ? 21.338  0.143   -2.812  1.00 31.47  ? 128 ARG A CZ  1 
ATOM   997  N NH1 . ARG A 1 126 ? 20.431  -0.760  -3.120  1.00 30.37  ? 128 ARG A NH1 1 
ATOM   998  N NH2 . ARG A 1 126 ? 20.983  1.418   -2.718  1.00 30.38  ? 128 ARG A NH2 1 
ATOM   999  N N   . PHE A 1 127 ? 24.725  -4.213  0.436   1.00 23.47  ? 129 PHE A N   1 
ATOM   1000 C CA  . PHE A 1 127 ? 24.918  -5.648  0.195   1.00 25.14  ? 129 PHE A CA  1 
ATOM   1001 C C   . PHE A 1 127 ? 23.926  -6.489  0.942   1.00 23.69  ? 129 PHE A C   1 
ATOM   1002 O O   . PHE A 1 127 ? 23.494  -7.506  0.423   1.00 22.95  ? 129 PHE A O   1 
ATOM   1003 C CB  . PHE A 1 127 ? 26.304  -6.107  0.567   1.00 26.49  ? 129 PHE A CB  1 
ATOM   1004 C CG  . PHE A 1 127 ? 27.383  -5.833  -0.445  1.00 29.17  ? 129 PHE A CG  1 
ATOM   1005 C CD1 . PHE A 1 127 ? 27.317  -4.733  -1.280  1.00 31.33  ? 129 PHE A CD1 1 
ATOM   1006 C CD2 . PHE A 1 127 ? 28.486  -6.647  -0.527  1.00 31.56  ? 129 PHE A CD2 1 
ATOM   1007 C CE1 . PHE A 1 127 ? 28.350  -4.468  -2.194  1.00 31.56  ? 129 PHE A CE1 1 
ATOM   1008 C CE2 . PHE A 1 127 ? 29.513  -6.378  -1.413  1.00 32.81  ? 129 PHE A CE2 1 
ATOM   1009 C CZ  . PHE A 1 127 ? 29.436  -5.295  -2.248  1.00 32.03  ? 129 PHE A CZ  1 
ATOM   1010 N N   . TRP A 1 128 ? 23.553  -6.059  2.151   1.00 23.11  ? 130 TRP A N   1 
ATOM   1011 C CA  . TRP A 1 128 ? 22.602  -6.788  2.945   1.00 23.28  ? 130 TRP A CA  1 
ATOM   1012 C C   . TRP A 1 128 ? 21.204  -6.708  2.339   1.00 23.70  ? 130 TRP A C   1 
ATOM   1013 O O   . TRP A 1 128 ? 20.535  -7.735  2.244   1.00 23.40  ? 130 TRP A O   1 
ATOM   1014 C CB  . TRP A 1 128 ? 22.603  -6.265  4.390   1.00 21.15  ? 130 TRP A CB  1 
ATOM   1015 C CG  . TRP A 1 128 ? 21.644  -6.980  5.302   1.00 19.10  ? 130 TRP A CG  1 
ATOM   1016 C CD1 . TRP A 1 128 ? 20.665  -6.416  6.061   1.00 19.29  ? 130 TRP A CD1 1 
ATOM   1017 C CD2 . TRP A 1 128 ? 21.612  -8.380  5.578   1.00 18.63  ? 130 TRP A CD2 1 
ATOM   1018 N NE1 . TRP A 1 128 ? 20.042  -7.368  6.817   1.00 19.97  ? 130 TRP A NE1 1 
ATOM   1019 C CE2 . TRP A 1 128 ? 20.604  -8.591  6.546   1.00 19.33  ? 130 TRP A CE2 1 
ATOM   1020 C CE3 . TRP A 1 128 ? 22.367  -9.478  5.137   1.00 17.98  ? 130 TRP A CE3 1 
ATOM   1021 C CZ2 . TRP A 1 128 ? 20.304  -9.851  7.038   1.00 18.75  ? 130 TRP A CZ2 1 
ATOM   1022 C CZ3 . TRP A 1 128 ? 22.036  -10.729 5.597   1.00 18.59  ? 130 TRP A CZ3 1 
ATOM   1023 C CH2 . TRP A 1 128 ? 21.047  -10.906 6.557   1.00 18.94  ? 130 TRP A CH2 1 
ATOM   1024 N N   . LEU A 1 129 ? 20.752  -5.496  1.936   1.00 22.56  ? 131 LEU A N   1 
ATOM   1025 C CA  . LEU A 1 129 ? 19.488  -5.343  1.231   1.00 22.92  ? 131 LEU A CA  1 
ATOM   1026 C C   . LEU A 1 129 ? 19.470  -6.218  -0.047  1.00 22.90  ? 131 LEU A C   1 
ATOM   1027 O O   . LEU A 1 129 ? 18.516  -6.950  -0.260  1.00 22.01  ? 131 LEU A O   1 
ATOM   1028 C CB  . LEU A 1 129 ? 19.231  -3.887  0.843   1.00 24.06  ? 131 LEU A CB  1 
ATOM   1029 C CG  . LEU A 1 129 ? 17.935  -3.641  0.001   1.00 25.96  ? 131 LEU A CG  1 
ATOM   1030 C CD1 . LEU A 1 129 ? 16.750  -4.043  0.735   1.00 26.09  ? 131 LEU A CD1 1 
ATOM   1031 C CD2 . LEU A 1 129 ? 17.808  -2.216  -0.349  1.00 28.09  ? 131 LEU A CD2 1 
ATOM   1032 N N   . GLU A 1 130 ? 20.538  -6.154  -0.879  1.00 22.72  ? 132 GLU A N   1 
ATOM   1033 C CA  . GLU A 1 130 ? 20.550  -6.945  -2.105  1.00 23.00  ? 132 GLU A CA  1 
ATOM   1034 C C   . GLU A 1 130 ? 20.418  -8.456  -1.783  1.00 23.40  ? 132 GLU A C   1 
ATOM   1035 O O   . GLU A 1 130 ? 19.710  -9.164  -2.491  1.00 22.34  ? 132 GLU A O   1 
ATOM   1036 C CB  . GLU A 1 130 ? 21.740  -6.653  -3.009  1.00 24.35  ? 132 GLU A CB  1 
ATOM   1037 C CG  . GLU A 1 130 ? 21.912  -5.190  -3.413  1.00 28.37  ? 132 GLU A CG  1 
ATOM   1038 C CD  . GLU A 1 130 ? 20.752  -4.604  -4.193  1.00 30.22  ? 132 GLU A CD  1 
ATOM   1039 O OE1 . GLU A 1 130 ? 19.998  -5.367  -4.851  1.00 27.83  ? 132 GLU A OE1 1 
ATOM   1040 O OE2 . GLU A 1 130 ? 20.597  -3.367  -4.130  1.00 33.23  ? 132 GLU A OE2 1 
ATOM   1041 N N   . THR A 1 131 ? 21.087  -8.924  -0.710  1.00 24.29  ? 133 THR A N   1 
ATOM   1042 C CA  . THR A 1 131 ? 20.956  -10.310 -0.215  1.00 24.22  ? 133 THR A CA  1 
ATOM   1043 C C   . THR A 1 131 ? 19.494  -10.632 0.146   1.00 23.53  ? 133 THR A C   1 
ATOM   1044 O O   . THR A 1 131 ? 18.962  -11.644 -0.301  1.00 21.73  ? 133 THR A O   1 
ATOM   1045 C CB  . THR A 1 131 ? 21.863  -10.528 0.975   1.00 25.61  ? 133 THR A CB  1 
ATOM   1046 O OG1 . THR A 1 131 ? 23.184  -10.260 0.571   1.00 24.84  ? 133 THR A OG1 1 
ATOM   1047 C CG2 . THR A 1 131 ? 21.784  -11.903 1.509   1.00 26.68  ? 133 THR A CG2 1 
ATOM   1048 N N   . LEU A 1 132 ? 18.849  -9.756  0.947   1.00 24.60  ? 134 LEU A N   1 
ATOM   1049 C CA  . LEU A 1 132 ? 17.458  -9.907  1.350   1.00 24.45  ? 134 LEU A CA  1 
ATOM   1050 C C   . LEU A 1 132 ? 16.528  -10.030 0.137   1.00 23.09  ? 134 LEU A C   1 
ATOM   1051 O O   . LEU A 1 132 ? 15.659  -10.892 0.138   1.00 23.33  ? 134 LEU A O   1 
ATOM   1052 C CB  . LEU A 1 132 ? 17.023  -8.731  2.219   1.00 24.76  ? 134 LEU A CB  1 
ATOM   1053 C CG  . LEU A 1 132 ? 17.727  -8.550  3.564   1.00 25.22  ? 134 LEU A CG  1 
ATOM   1054 C CD1 . LEU A 1 132 ? 17.201  -7.341  4.285   1.00 25.62  ? 134 LEU A CD1 1 
ATOM   1055 C CD2 . LEU A 1 132 ? 17.665  -9.781  4.423   1.00 26.26  ? 134 LEU A CD2 1 
ATOM   1056 N N   . LEU A 1 133 ? 16.732  -9.225  -0.880  1.00 22.17  ? 135 LEU A N   1 
ATOM   1057 C CA  . LEU A 1 133 ? 15.872  -9.291  -2.074  1.00 25.23  ? 135 LEU A CA  1 
ATOM   1058 C C   . LEU A 1 133 ? 16.056  -10.563 -2.866  1.00 25.68  ? 135 LEU A C   1 
ATOM   1059 O O   . LEU A 1 133 ? 15.096  -11.060 -3.442  1.00 27.23  ? 135 LEU A O   1 
ATOM   1060 C CB  . LEU A 1 133 ? 16.051  -8.060  -2.980  1.00 25.18  ? 135 LEU A CB  1 
ATOM   1061 C CG  . LEU A 1 133 ? 15.888  -6.707  -2.319  1.00 25.36  ? 135 LEU A CG  1 
ATOM   1062 C CD1 . LEU A 1 133 ? 16.147  -5.598  -3.331  1.00 26.76  ? 135 LEU A CD1 1 
ATOM   1063 C CD2 . LEU A 1 133 ? 14.527  -6.517  -1.676  1.00 26.11  ? 135 LEU A CD2 1 
ATOM   1064 N N   . CYS A 1 134 ? 17.257  -11.103 -2.882  1.00 24.94  ? 136 CYS A N   1 
ATOM   1065 C CA  . CYS A 1 134 ? 17.541  -12.367 -3.545  1.00 24.82  ? 136 CYS A CA  1 
ATOM   1066 C C   . CYS A 1 134 ? 16.770  -13.499 -2.856  1.00 25.13  ? 136 CYS A C   1 
ATOM   1067 O O   . CYS A 1 134 ? 16.306  -14.432 -3.530  1.00 26.25  ? 136 CYS A O   1 
ATOM   1068 C CB  . CYS A 1 134 ? 19.039  -12.656 -3.542  1.00 23.89  ? 136 CYS A CB  1 
ATOM   1069 S SG  . CYS A 1 134 ? 19.994  -11.764 -4.794  1.00 28.41  ? 136 CYS A SG  1 
ATOM   1070 N N   . LEU A 1 135 ? 16.657  -13.439 -1.516  1.00 23.93  ? 137 LEU A N   1 
ATOM   1071 C CA  . LEU A 1 135 ? 15.930  -14.451 -0.759  1.00 24.43  ? 137 LEU A CA  1 
ATOM   1072 C C   . LEU A 1 135 ? 14.417  -14.341 -0.979  1.00 26.24  ? 137 LEU A C   1 
ATOM   1073 O O   . LEU A 1 135 ? 13.793  -15.283 -1.484  1.00 26.92  ? 137 LEU A O   1 
ATOM   1074 C CB  . LEU A 1 135 ? 16.250  -14.366 0.744   1.00 23.07  ? 137 LEU A CB  1 
ATOM   1075 C CG  . LEU A 1 135 ? 17.367  -15.209 1.318   1.00 23.46  ? 137 LEU A CG  1 
ATOM   1076 C CD1 . LEU A 1 135 ? 18.636  -15.163 0.480   1.00 24.39  ? 137 LEU A CD1 1 
ATOM   1077 C CD2 . LEU A 1 135 ? 17.614  -14.798 2.771   1.00 23.22  ? 137 LEU A CD2 1 
ATOM   1078 N N   . ILE A 1 136 ? 13.823  -13.210 -0.592  1.00 28.13  ? 138 ILE A N   1 
ATOM   1079 C CA  . ILE A 1 136 ? 12.364  -13.070 -0.640  1.00 28.67  ? 138 ILE A CA  1 
ATOM   1080 C C   . ILE A 1 136 ? 11.857  -13.145 -2.082  1.00 28.99  ? 138 ILE A C   1 
ATOM   1081 O O   . ILE A 1 136 ? 10.746  -13.622 -2.272  1.00 29.37  ? 138 ILE A O   1 
ATOM   1082 C CB  . ILE A 1 136 ? 11.814  -11.820 0.131   1.00 28.24  ? 138 ILE A CB  1 
ATOM   1083 C CG1 . ILE A 1 136 ? 12.232  -10.505 -0.554  1.00 29.26  ? 138 ILE A CG1 1 
ATOM   1084 C CG2 . ILE A 1 136 ? 12.264  -11.876 1.599   1.00 28.52  ? 138 ILE A CG2 1 
ATOM   1085 C CD1 . ILE A 1 136 ? 11.651  -9.356  -0.086  1.00 28.19  ? 138 ILE A CD1 1 
ATOM   1086 N N   . GLY A 1 137 ? 12.649  -12.700 -3.054  1.00 29.01  ? 139 GLY A N   1 
ATOM   1087 C CA  . GLY A 1 137 ? 12.235  -12.726 -4.461  1.00 30.36  ? 139 GLY A CA  1 
ATOM   1088 C C   . GLY A 1 137 ? 12.413  -14.057 -5.176  1.00 30.48  ? 139 GLY A C   1 
ATOM   1089 O O   . GLY A 1 137 ? 12.003  -14.189 -6.330  1.00 31.84  ? 139 GLY A O   1 
ATOM   1090 N N   . GLU A 1 138 ? 13.037  -15.047 -4.529  1.00 28.80  ? 140 GLU A N   1 
ATOM   1091 C CA  . GLU A 1 138 ? 13.316  -16.351 -5.119  1.00 27.06  ? 140 GLU A CA  1 
ATOM   1092 C C   . GLU A 1 138 ? 14.168  -16.246 -6.401  1.00 26.04  ? 140 GLU A C   1 
ATOM   1093 O O   . GLU A 1 138 ? 13.799  -16.761 -7.464  1.00 24.20  ? 140 GLU A O   1 
ATOM   1094 C CB  . GLU A 1 138 ? 12.028  -17.137 -5.389  1.00 27.48  ? 140 GLU A CB  1 
ATOM   1095 C CG  . GLU A 1 138 ? 11.127  -17.283 -4.171  1.00 32.15  ? 140 GLU A CG  1 
ATOM   1096 C CD  . GLU A 1 138 ? 11.560  -18.279 -3.118  1.00 33.81  ? 140 GLU A CD  1 
ATOM   1097 O OE1 . GLU A 1 138 ? 11.953  -19.404 -3.504  1.00 36.36  ? 140 GLU A OE1 1 
ATOM   1098 O OE2 . GLU A 1 138 ? 11.478  -17.950 -1.913  1.00 31.86  ? 140 GLU A OE2 1 
ATOM   1099 N N   . SER A 1 139 ? 15.305  -15.609 -6.273  1.00 26.20  ? 141 SER A N   1 
ATOM   1100 C CA  . SER A 1 139 ? 16.123  -15.213 -7.385  1.00 27.68  ? 141 SER A CA  1 
ATOM   1101 C C   . SER A 1 139 ? 16.987  -16.290 -8.010  1.00 28.67  ? 141 SER A C   1 
ATOM   1102 O O   . SER A 1 139 ? 17.668  -16.025 -9.022  1.00 29.06  ? 141 SER A O   1 
ATOM   1103 C CB  . SER A 1 139 ? 16.974  -14.017 -6.974  1.00 30.23  ? 141 SER A CB  1 
ATOM   1104 O OG  . SER A 1 139 ? 16.147  -12.985 -6.459  1.00 30.75  ? 141 SER A OG  1 
ATOM   1105 N N   . PHE A 1 140 ? 16.963  -17.505 -7.464  1.00 28.91  ? 142 PHE A N   1 
ATOM   1106 C CA  . PHE A 1 140 ? 17.812  -18.571 -7.959  1.00 30.21  ? 142 PHE A CA  1 
ATOM   1107 C C   . PHE A 1 140 ? 17.018  -19.623 -8.696  1.00 32.82  ? 142 PHE A C   1 
ATOM   1108 O O   . PHE A 1 140 ? 17.494  -20.744 -8.828  1.00 31.78  ? 142 PHE A O   1 
ATOM   1109 C CB  . PHE A 1 140 ? 18.629  -19.145 -6.788  1.00 29.47  ? 142 PHE A CB  1 
ATOM   1110 C CG  . PHE A 1 140 ? 19.323  -18.050 -5.998  1.00 27.59  ? 142 PHE A CG  1 
ATOM   1111 C CD1 . PHE A 1 140 ? 20.302  -17.285 -6.573  1.00 26.81  ? 142 PHE A CD1 1 
ATOM   1112 C CD2 . PHE A 1 140 ? 18.921  -17.739 -4.718  1.00 28.36  ? 142 PHE A CD2 1 
ATOM   1113 C CE1 . PHE A 1 140 ? 20.931  -16.274 -5.857  1.00 27.80  ? 142 PHE A CE1 1 
ATOM   1114 C CE2 . PHE A 1 140 ? 19.521  -16.687 -4.011  1.00 27.80  ? 142 PHE A CE2 1 
ATOM   1115 C CZ  . PHE A 1 140 ? 20.526  -15.984 -4.570  1.00 27.99  ? 142 PHE A CZ  1 
ATOM   1116 N N   . ASP A 1 141 ? 15.781  -19.281 -9.205  1.00 35.94  ? 143 ASP A N   1 
ATOM   1117 C CA  . ASP A 1 141 ? 14.971  -20.175 -10.008 1.00 39.14  ? 143 ASP A CA  1 
ATOM   1118 C C   . ASP A 1 141 ? 14.720  -21.465 -9.192  1.00 38.88  ? 143 ASP A C   1 
ATOM   1119 O O   . ASP A 1 141 ? 14.509  -21.309 -7.985  1.00 39.23  ? 143 ASP A O   1 
ATOM   1120 C CB  . ASP A 1 141 ? 15.596  -20.336 -11.440 1.00 45.79  ? 143 ASP A CB  1 
ATOM   1121 C CG  . ASP A 1 141 ? 15.570  -19.016 -12.241 1.00 56.85  ? 143 ASP A CG  1 
ATOM   1122 O OD1 . ASP A 1 141 ? 14.455  -18.403 -12.375 1.00 56.96  ? 143 ASP A OD1 1 
ATOM   1123 O OD2 . ASP A 1 141 ? 16.661  -18.582 -12.724 1.00 62.27  ? 143 ASP A OD2 1 
ATOM   1124 N N   . ASP A 1 142 ? 14.743  -22.682 -9.751  1.00 38.99  ? 144 ASP A N   1 
ATOM   1125 C CA  . ASP A 1 142 ? 14.403  -23.853 -8.916  1.00 39.96  ? 144 ASP A CA  1 
ATOM   1126 C C   . ASP A 1 142 ? 15.379  -24.034 -7.747  1.00 37.77  ? 144 ASP A C   1 
ATOM   1127 O O   . ASP A 1 142 ? 14.991  -24.572 -6.710  1.00 36.56  ? 144 ASP A O   1 
ATOM   1128 C CB  . ASP A 1 142 ? 14.273  -25.120 -9.741  1.00 45.01  ? 144 ASP A CB  1 
ATOM   1129 C CG  . ASP A 1 142 ? 12.999  -25.206 -10.556 1.00 54.84  ? 144 ASP A CG  1 
ATOM   1130 O OD1 . ASP A 1 142 ? 12.028  -24.485 -10.228 1.00 55.98  ? 144 ASP A OD1 1 
ATOM   1131 O OD2 . ASP A 1 142 ? 12.966  -26.003 -11.513 1.00 60.70  ? 144 ASP A OD2 1 
ATOM   1132 N N   . TYR A 1 143 ? 16.631  -23.538 -7.908  1.00 36.18  ? 145 TYR A N   1 
ATOM   1133 C CA  . TYR A 1 143 ? 17.648  -23.674 -6.882  1.00 33.54  ? 145 TYR A CA  1 
ATOM   1134 C C   . TYR A 1 143 ? 17.420  -22.773 -5.644  1.00 29.79  ? 145 TYR A C   1 
ATOM   1135 O O   . TYR A 1 143 ? 18.130  -22.902 -4.663  1.00 28.72  ? 145 TYR A O   1 
ATOM   1136 C CB  . TYR A 1 143 ? 19.001  -23.473 -7.516  1.00 34.21  ? 145 TYR A CB  1 
ATOM   1137 C CG  . TYR A 1 143 ? 19.321  -24.433 -8.655  1.00 35.89  ? 145 TYR A CG  1 
ATOM   1138 C CD1 . TYR A 1 143 ? 19.313  -25.797 -8.458  1.00 37.96  ? 145 TYR A CD1 1 
ATOM   1139 C CD2 . TYR A 1 143 ? 19.668  -23.963 -9.913  1.00 37.42  ? 145 TYR A CD2 1 
ATOM   1140 C CE1 . TYR A 1 143 ? 19.678  -26.678 -9.465  1.00 39.52  ? 145 TYR A CE1 1 
ATOM   1141 C CE2 . TYR A 1 143 ? 19.999  -24.832 -10.943 1.00 38.50  ? 145 TYR A CE2 1 
ATOM   1142 C CZ  . TYR A 1 143 ? 20.011  -26.194 -10.713 1.00 41.39  ? 145 TYR A CZ  1 
ATOM   1143 O OH  . TYR A 1 143 ? 20.336  -27.095 -11.709 1.00 45.71  ? 145 TYR A OH  1 
ATOM   1144 N N   . SER A 1 144 ? 16.440  -21.869 -5.674  1.00 29.34  ? 146 SER A N   1 
ATOM   1145 C CA  . SER A 1 144 ? 16.024  -21.112 -4.492  1.00 28.71  ? 146 SER A CA  1 
ATOM   1146 C C   . SER A 1 144 ? 15.527  -21.999 -3.339  1.00 28.15  ? 146 SER A C   1 
ATOM   1147 O O   . SER A 1 144 ? 15.588  -21.585 -2.195  1.00 29.55  ? 146 SER A O   1 
ATOM   1148 C CB  . SER A 1 144 ? 14.934  -20.105 -4.854  1.00 30.45  ? 146 SER A CB  1 
ATOM   1149 O OG  . SER A 1 144 ? 15.446  -18.888 -5.344  1.00 33.74  ? 146 SER A OG  1 
ATOM   1150 N N   . ASP A 1 145 ? 15.050  -23.187 -3.635  1.00 26.83  ? 147 ASP A N   1 
ATOM   1151 C CA  . ASP A 1 145 ? 14.682  -24.162 -2.627  1.00 26.60  ? 147 ASP A CA  1 
ATOM   1152 C C   . ASP A 1 145 ? 15.857  -24.658 -1.798  1.00 25.78  ? 147 ASP A C   1 
ATOM   1153 O O   . ASP A 1 145 ? 15.637  -25.094 -0.661  1.00 26.70  ? 147 ASP A O   1 
ATOM   1154 C CB  . ASP A 1 145 ? 13.980  -25.347 -3.273  1.00 29.60  ? 147 ASP A CB  1 
ATOM   1155 C CG  . ASP A 1 145 ? 12.571  -25.071 -3.772  1.00 36.97  ? 147 ASP A CG  1 
ATOM   1156 O OD1 . ASP A 1 145 ? 11.972  -24.049 -3.336  1.00 35.61  ? 147 ASP A OD1 1 
ATOM   1157 O OD2 . ASP A 1 145 ? 12.067  -25.871 -4.621  1.00 39.80  ? 147 ASP A OD2 1 
ATOM   1158 N N   . ASP A 1 146 ? 17.060  -24.646 -2.339  1.00 23.10  ? 148 ASP A N   1 
ATOM   1159 C CA  . ASP A 1 146 ? 18.272  -24.883 -1.569  1.00 22.62  ? 148 ASP A CA  1 
ATOM   1160 C C   . ASP A 1 146 ? 18.650  -23.802 -0.590  1.00 20.74  ? 148 ASP A C   1 
ATOM   1161 O O   . ASP A 1 146 ? 19.462  -24.063 0.258   1.00 20.55  ? 148 ASP A O   1 
ATOM   1162 C CB  . ASP A 1 146 ? 19.463  -25.066 -2.503  1.00 23.04  ? 148 ASP A CB  1 
ATOM   1163 C CG  . ASP A 1 146 ? 19.507  -26.510 -2.972  1.00 27.24  ? 148 ASP A CG  1 
ATOM   1164 O OD1 . ASP A 1 146 ? 18.522  -26.948 -3.551  1.00 30.01  ? 148 ASP A OD1 1 
ATOM   1165 O OD2 . ASP A 1 146 ? 20.540  -27.185 -2.728  1.00 21.38  ? 148 ASP A OD2 1 
ATOM   1166 N N   . VAL A 1 147 ? 18.116  -22.616 -0.728  1.00 20.37  ? 149 VAL A N   1 
ATOM   1167 C CA  . VAL A 1 147 ? 18.397  -21.505 0.154   1.00 21.44  ? 149 VAL A CA  1 
ATOM   1168 C C   . VAL A 1 147 ? 17.682  -21.708 1.483   1.00 23.42  ? 149 VAL A C   1 
ATOM   1169 O O   . VAL A 1 147 ? 16.475  -21.992 1.522   1.00 23.44  ? 149 VAL A O   1 
ATOM   1170 C CB  . VAL A 1 147 ? 18.004  -20.192 -0.508  1.00 22.04  ? 149 VAL A CB  1 
ATOM   1171 C CG1 . VAL A 1 147 ? 18.205  -19.026 0.441   1.00 22.77  ? 149 VAL A CG1 1 
ATOM   1172 C CG2 . VAL A 1 147 ? 18.767  -19.974 -1.801  1.00 22.70  ? 149 VAL A CG2 1 
ATOM   1173 N N   . CYS A 1 148 ? 18.449  -21.571 2.568   1.00 23.01  ? 150 CYS A N   1 
ATOM   1174 C CA  . CYS A 1 148 ? 17.942  -21.621 3.931   1.00 23.60  ? 150 CYS A CA  1 
ATOM   1175 C C   . CYS A 1 148 ? 17.695  -20.225 4.497   1.00 23.11  ? 150 CYS A C   1 
ATOM   1176 O O   . CYS A 1 148 ? 16.684  -19.991 5.157   1.00 24.08  ? 150 CYS A O   1 
ATOM   1177 C CB  . CYS A 1 148 ? 18.913  -22.404 4.806   1.00 22.22  ? 150 CYS A CB  1 
ATOM   1178 S SG  . CYS A 1 148 ? 19.050  -24.128 4.333   1.00 24.92  ? 150 CYS A SG  1 
ATOM   1179 N N   . GLY A 1 149 ? 18.623  -19.329 4.231   1.00 21.25  ? 151 GLY A N   1 
ATOM   1180 C CA  . GLY A 1 149 ? 18.609  -17.989 4.766   1.00 21.56  ? 151 GLY A CA  1 
ATOM   1181 C C   . GLY A 1 149 ? 19.893  -17.257 4.507   1.00 21.23  ? 151 GLY A C   1 
ATOM   1182 O O   . GLY A 1 149 ? 20.709  -17.697 3.719   1.00 20.53  ? 151 GLY A O   1 
ATOM   1183 N N   . ALA A 1 150 ? 20.050  -16.123 5.195   1.00 22.04  ? 152 ALA A N   1 
ATOM   1184 C CA  . ALA A 1 150 ? 21.185  -15.233 5.099   1.00 23.35  ? 152 ALA A CA  1 
ATOM   1185 C C   . ALA A 1 150 ? 21.565  -14.710 6.471   1.00 23.67  ? 152 ALA A C   1 
ATOM   1186 O O   . ALA A 1 150 ? 20.684  -14.475 7.294   1.00 23.08  ? 152 ALA A O   1 
ATOM   1187 C CB  . ALA A 1 150 ? 20.862  -14.085 4.171   1.00 24.33  ? 152 ALA A CB  1 
ATOM   1188 N N   . VAL A 1 151 ? 22.880  -14.538 6.717   1.00 23.54  ? 153 VAL A N   1 
ATOM   1189 C CA  . VAL A 1 151 ? 23.396  -14.070 7.987   1.00 24.19  ? 153 VAL A CA  1 
ATOM   1190 C C   . VAL A 1 151 ? 24.312  -12.878 7.758   1.00 24.02  ? 153 VAL A C   1 
ATOM   1191 O O   . VAL A 1 151 ? 25.130  -12.884 6.835   1.00 22.78  ? 153 VAL A O   1 
ATOM   1192 C CB  . VAL A 1 151 ? 24.155  -15.200 8.753   1.00 25.85  ? 153 VAL A CB  1 
ATOM   1193 C CG1 . VAL A 1 151 ? 24.616  -14.734 10.128  1.00 26.83  ? 153 VAL A CG1 1 
ATOM   1194 C CG2 . VAL A 1 151 ? 23.288  -16.423 8.906   1.00 28.02  ? 153 VAL A CG2 1 
ATOM   1195 N N   . VAL A 1 152 ? 24.166  -11.857 8.607   1.00 25.13  ? 154 VAL A N   1 
ATOM   1196 C CA  . VAL A 1 152 ? 25.103  -10.770 8.692   1.00 26.51  ? 154 VAL A CA  1 
ATOM   1197 C C   . VAL A 1 152 ? 25.718  -10.786 10.088  1.00 25.88  ? 154 VAL A C   1 
ATOM   1198 O O   . VAL A 1 152 ? 25.032  -10.678 11.064  1.00 24.51  ? 154 VAL A O   1 
ATOM   1199 C CB  . VAL A 1 152 ? 24.534  -9.388  8.259   1.00 28.98  ? 154 VAL A CB  1 
ATOM   1200 C CG1 . VAL A 1 152 ? 23.297  -9.003  9.069   1.00 31.53  ? 154 VAL A CG1 1 
ATOM   1201 C CG2 . VAL A 1 152 ? 25.603  -8.320  8.376   1.00 29.68  ? 154 VAL A CG2 1 
ATOM   1202 N N   . ASN A 1 153 ? 27.017  -10.944 10.157  1.00 28.61  ? 155 ASN A N   1 
ATOM   1203 C CA  . ASN A 1 153 ? 27.825  -10.815 11.378  1.00 30.84  ? 155 ASN A CA  1 
ATOM   1204 C C   . ASN A 1 153 ? 28.491  -9.433  11.379  1.00 33.27  ? 155 ASN A C   1 
ATOM   1205 O O   . ASN A 1 153 ? 29.367  -9.153  10.540  1.00 32.78  ? 155 ASN A O   1 
ATOM   1206 C CB  . ASN A 1 153 ? 28.896  -11.920 11.453  1.00 29.56  ? 155 ASN A CB  1 
ATOM   1207 C CG  . ASN A 1 153 ? 28.392  -13.310 11.113  1.00 30.85  ? 155 ASN A CG  1 
ATOM   1208 O OD1 . ASN A 1 153 ? 28.565  -13.879 10.003  1.00 29.35  ? 155 ASN A OD1 1 
ATOM   1209 N ND2 . ASN A 1 153 ? 27.732  -13.879 12.062  1.00 32.30  ? 155 ASN A ND2 1 
ATOM   1210 N N   . VAL A 1 154 ? 28.065  -8.581  12.322  1.00 36.04  ? 156 VAL A N   1 
ATOM   1211 C CA  . VAL A 1 154 ? 28.628  -7.239  12.503  1.00 40.77  ? 156 VAL A CA  1 
ATOM   1212 C C   . VAL A 1 154 ? 29.805  -7.385  13.454  1.00 43.47  ? 156 VAL A C   1 
ATOM   1213 O O   . VAL A 1 154 ? 29.592  -7.815  14.588  1.00 44.30  ? 156 VAL A O   1 
ATOM   1214 C CB  . VAL A 1 154 ? 27.566  -6.268  13.052  1.00 41.92  ? 156 VAL A CB  1 
ATOM   1215 C CG1 . VAL A 1 154 ? 28.128  -4.867  13.186  1.00 42.97  ? 156 VAL A CG1 1 
ATOM   1216 C CG2 . VAL A 1 154 ? 26.359  -6.250  12.130  1.00 42.22  ? 156 VAL A CG2 1 
ATOM   1217 N N   . ARG A 1 155 ? 31.024  -7.061  12.987  1.00 44.17  ? 157 ARG A N   1 
ATOM   1218 C CA  . ARG A 1 155 ? 32.269  -7.273  13.762  1.00 46.18  ? 157 ARG A CA  1 
ATOM   1219 C C   . ARG A 1 155 ? 33.277  -6.109  13.598  1.00 49.62  ? 157 ARG A C   1 
ATOM   1220 O O   . ARG A 1 155 ? 33.247  -5.397  12.600  1.00 50.38  ? 157 ARG A O   1 
ATOM   1221 C CB  . ARG A 1 155 ? 32.942  -8.573  13.325  1.00 45.48  ? 157 ARG A CB  1 
ATOM   1222 C CG  . ARG A 1 155 ? 32.125  -9.777  13.598  1.00 46.60  ? 157 ARG A CG  1 
ATOM   1223 C CD  . ARG A 1 155 ? 32.124  -10.193 15.058  1.00 47.76  ? 157 ARG A CD  1 
ATOM   1224 N NE  . ARG A 1 155 ? 31.541  -11.536 15.197  1.00 50.78  ? 157 ARG A NE  1 
ATOM   1225 C CZ  . ARG A 1 155 ? 30.235  -11.822 15.199  1.00 50.63  ? 157 ARG A CZ  1 
ATOM   1226 N NH1 . ARG A 1 155 ? 29.328  -10.850 15.080  1.00 45.88  ? 157 ARG A NH1 1 
ATOM   1227 N NH2 . ARG A 1 155 ? 29.827  -13.077 15.318  1.00 54.14  ? 157 ARG A NH2 1 
ATOM   1228 N N   . ALA A 1 156 ? 34.159  -5.925  14.574  1.00 51.53  ? 158 ALA A N   1 
ATOM   1229 C CA  . ALA A 1 156 ? 35.158  -4.847  14.548  1.00 52.79  ? 158 ALA A CA  1 
ATOM   1230 C C   . ALA A 1 156 ? 36.218  -5.098  13.468  1.00 52.86  ? 158 ALA A C   1 
ATOM   1231 O O   . ALA A 1 156 ? 36.526  -4.189  12.720  1.00 53.27  ? 158 ALA A O   1 
ATOM   1232 C CB  . ALA A 1 156 ? 35.817  -4.722  15.915  1.00 53.74  ? 158 ALA A CB  1 
ATOM   1233 N N   . LYS A 1 157 ? 36.761  -6.308  13.376  1.00 53.03  ? 159 LYS A N   1 
ATOM   1234 C CA  . LYS A 1 157 ? 37.668  -6.691  12.290  1.00 53.90  ? 159 LYS A CA  1 
ATOM   1235 C C   . LYS A 1 157 ? 37.044  -6.447  10.873  1.00 52.74  ? 159 LYS A C   1 
ATOM   1236 O O   . LYS A 1 157 ? 37.770  -6.109  9.921   1.00 54.00  ? 159 LYS A O   1 
ATOM   1237 C CB  . LYS A 1 157 ? 38.067  -8.182  12.455  1.00 58.85  ? 159 LYS A CB  1 
ATOM   1238 C CG  . LYS A 1 157 ? 38.856  -8.773  11.272  1.00 67.69  ? 159 LYS A CG  1 
ATOM   1239 C CD  . LYS A 1 157 ? 39.723  -10.008 11.647  1.00 76.12  ? 159 LYS A CD  1 
ATOM   1240 C CE  . LYS A 1 157 ? 41.050  -9.674  12.327  1.00 84.00  ? 159 LYS A CE  1 
ATOM   1241 N NZ  . LYS A 1 157 ? 42.027  -8.980  11.415  1.00 88.35  ? 159 LYS A NZ  1 
ATOM   1242 N N   . GLY A 1 158 ? 35.725  -6.614  10.742  1.00 49.05  ? 160 GLY A N   1 
ATOM   1243 C CA  . GLY A 1 158 ? 35.075  -6.488  9.452   1.00 46.48  ? 160 GLY A CA  1 
ATOM   1244 C C   . GLY A 1 158 ? 33.935  -7.465  9.274   1.00 43.47  ? 160 GLY A C   1 
ATOM   1245 O O   . GLY A 1 158 ? 33.980  -8.588  9.755   1.00 44.26  ? 160 GLY A O   1 
ATOM   1246 N N   . ASP A 1 159 ? 32.931  -7.049  8.532   1.00 39.06  ? 161 ASP A N   1 
ATOM   1247 C CA  . ASP A 1 159 ? 31.628  -7.648  8.611   1.00 35.03  ? 161 ASP A CA  1 
ATOM   1248 C C   . ASP A 1 159 ? 31.467  -8.790  7.659   1.00 33.27  ? 161 ASP A C   1 
ATOM   1249 O O   . ASP A 1 159 ? 32.045  -8.765  6.583   1.00 34.21  ? 161 ASP A O   1 
ATOM   1250 C CB  . ASP A 1 159 ? 30.571  -6.593  8.322   1.00 33.45  ? 161 ASP A CB  1 
ATOM   1251 C CG  . ASP A 1 159 ? 30.568  -5.452  9.338   1.00 33.62  ? 161 ASP A CG  1 
ATOM   1252 O OD1 . ASP A 1 159 ? 30.632  -5.734  10.560  1.00 34.87  ? 161 ASP A OD1 1 
ATOM   1253 O OD2 . ASP A 1 159 ? 30.486  -4.304  8.923   1.00 33.13  ? 161 ASP A OD2 1 
ATOM   1254 N N   . LYS A 1 160 ? 30.666  -9.800  8.034   1.00 30.50  ? 162 LYS A N   1 
ATOM   1255 C CA  . LYS A 1 160 ? 30.431  -10.931 7.136   1.00 27.73  ? 162 LYS A CA  1 
ATOM   1256 C C   . LYS A 1 160 ? 29.016  -10.996 6.700   1.00 23.22  ? 162 LYS A C   1 
ATOM   1257 O O   . LYS A 1 160 ? 28.135  -10.856 7.565   1.00 23.20  ? 162 LYS A O   1 
ATOM   1258 C CB  . LYS A 1 160 ? 30.887  -12.234 7.826   1.00 31.60  ? 162 LYS A CB  1 
ATOM   1259 C CG  . LYS A 1 160 ? 32.408  -12.352 7.920   1.00 36.24  ? 162 LYS A CG  1 
ATOM   1260 C CD  . LYS A 1 160 ? 32.814  -13.411 8.907   1.00 47.19  ? 162 LYS A CD  1 
ATOM   1261 C CE  . LYS A 1 160 ? 32.337  -14.816 8.634   1.00 56.03  ? 162 LYS A CE  1 
ATOM   1262 N NZ  . LYS A 1 160 ? 32.903  -15.759 9.645   1.00 62.40  ? 162 LYS A NZ  1 
ATOM   1263 N N   . ILE A 1 161 ? 28.755  -11.192 5.367   1.00 21.01  ? 163 ILE A N   1 
ATOM   1264 C CA  . ILE A 1 161 ? 27.404  -11.468 4.823   1.00 21.24  ? 163 ILE A CA  1 
ATOM   1265 C C   . ILE A 1 161 ? 27.452  -12.793 4.066   1.00 20.63  ? 163 ILE A C   1 
ATOM   1266 O O   . ILE A 1 161 ? 28.346  -12.982 3.252   1.00 19.55  ? 163 ILE A O   1 
ATOM   1267 C CB  . ILE A 1 161 ? 26.883  -10.351 3.920   1.00 23.02  ? 163 ILE A CB  1 
ATOM   1268 C CG1 . ILE A 1 161 ? 26.867  -8.988  4.668   1.00 25.49  ? 163 ILE A CG1 1 
ATOM   1269 C CG2 . ILE A 1 161 ? 25.509  -10.709 3.343   1.00 23.11  ? 163 ILE A CG2 1 
ATOM   1270 C CD1 . ILE A 1 161 ? 26.474  -7.836  3.847   1.00 26.69  ? 163 ILE A CD1 1 
ATOM   1271 N N   . ALA A 1 162 ? 26.482  -13.712 4.342   1.00 20.06  ? 164 ALA A N   1 
ATOM   1272 C CA  . ALA A 1 162 ? 26.487  -15.042 3.780   1.00 20.77  ? 164 ALA A CA  1 
ATOM   1273 C C   . ALA A 1 162 ? 25.096  -15.507 3.464   1.00 20.67  ? 164 ALA A C   1 
ATOM   1274 O O   . ALA A 1 162 ? 24.191  -15.271 4.257   1.00 20.05  ? 164 ALA A O   1 
ATOM   1275 C CB  . ALA A 1 162 ? 27.165  -16.019 4.727   1.00 21.06  ? 164 ALA A CB  1 
ATOM   1276 N N   . ILE A 1 163 ? 24.907  -16.145 2.281   1.00 20.60  ? 165 ILE A N   1 
ATOM   1277 C CA  . ILE A 1 163 ? 23.741  -16.966 1.991   1.00 19.92  ? 165 ILE A CA  1 
ATOM   1278 C C   . ILE A 1 163 ? 24.012  -18.392 2.354   1.00 20.49  ? 165 ILE A C   1 
ATOM   1279 O O   . ILE A 1 163 ? 24.961  -19.004 1.821   1.00 20.07  ? 165 ILE A O   1 
ATOM   1280 C CB  . ILE A 1 163 ? 23.308  -16.864 0.510   1.00 19.10  ? 165 ILE A CB  1 
ATOM   1281 C CG1 . ILE A 1 163 ? 22.813  -15.458 0.234   1.00 18.85  ? 165 ILE A CG1 1 
ATOM   1282 C CG2 . ILE A 1 163 ? 22.215  -17.922 0.182   1.00 18.87  ? 165 ILE A CG2 1 
ATOM   1283 C CD1 . ILE A 1 163 ? 22.271  -15.186 -1.136  1.00 21.19  ? 165 ILE A CD1 1 
ATOM   1284 N N   . TRP A 1 164 ? 23.170  -18.941 3.256   1.00 20.38  ? 166 TRP A N   1 
ATOM   1285 C CA  . TRP A 1 164 ? 23.209  -20.335 3.718   1.00 20.68  ? 166 TRP A CA  1 
ATOM   1286 C C   . TRP A 1 164 ? 22.309  -21.211 2.846   1.00 20.56  ? 166 TRP A C   1 
ATOM   1287 O O   . TRP A 1 164 ? 21.147  -20.871 2.573   1.00 19.45  ? 166 TRP A O   1 
ATOM   1288 C CB  . TRP A 1 164 ? 22.746  -20.455 5.180   1.00 22.01  ? 166 TRP A CB  1 
ATOM   1289 C CG  . TRP A 1 164 ? 23.703  -19.957 6.230   1.00 22.91  ? 166 TRP A CG  1 
ATOM   1290 C CD1 . TRP A 1 164 ? 24.604  -18.920 6.126   1.00 22.67  ? 166 TRP A CD1 1 
ATOM   1291 C CD2 . TRP A 1 164 ? 23.823  -20.462 7.573   1.00 22.90  ? 166 TRP A CD2 1 
ATOM   1292 N NE1 . TRP A 1 164 ? 25.279  -18.766 7.322   1.00 21.98  ? 166 TRP A NE1 1 
ATOM   1293 C CE2 . TRP A 1 164 ? 24.801  -19.686 8.230   1.00 22.47  ? 166 TRP A CE2 1 
ATOM   1294 C CE3 . TRP A 1 164 ? 23.187  -21.495 8.285   1.00 25.31  ? 166 TRP A CE3 1 
ATOM   1295 C CZ2 . TRP A 1 164 ? 25.180  -19.936 9.541   1.00 24.18  ? 166 TRP A CZ2 1 
ATOM   1296 C CZ3 . TRP A 1 164 ? 23.537  -21.713 9.608   1.00 25.61  ? 166 TRP A CZ3 1 
ATOM   1297 C CH2 . TRP A 1 164 ? 24.524  -20.940 10.219  1.00 24.67  ? 166 TRP A CH2 1 
ATOM   1298 N N   . THR A 1 165 ? 22.860  -22.344 2.395   1.00 20.94  ? 167 THR A N   1 
ATOM   1299 C CA  . THR A 1 165 ? 22.134  -23.326 1.574   1.00 22.94  ? 167 THR A CA  1 
ATOM   1300 C C   . THR A 1 165 ? 22.158  -24.699 2.300   1.00 23.88  ? 167 THR A C   1 
ATOM   1301 O O   . THR A 1 165 ? 22.956  -24.949 3.225   1.00 22.86  ? 167 THR A O   1 
ATOM   1302 C CB  . THR A 1 165 ? 22.645  -23.344 0.109   1.00 25.59  ? 167 THR A CB  1 
ATOM   1303 O OG1 . THR A 1 165 ? 23.834  -24.119 0.024   1.00 27.40  ? 167 THR A OG1 1 
ATOM   1304 C CG2 . THR A 1 165 ? 22.906  -21.942 -0.447  1.00 27.89  ? 167 THR A CG2 1 
ATOM   1305 N N   . THR A 1 166 ? 21.252  -25.555 1.883   1.00 25.39  ? 168 THR A N   1 
ATOM   1306 C CA  . THR A 1 166 ? 20.881  -26.751 2.626   1.00 25.91  ? 168 THR A CA  1 
ATOM   1307 C C   . THR A 1 166 ? 21.801  -27.950 2.415   1.00 24.94  ? 168 THR A C   1 
ATOM   1308 O O   . THR A 1 166 ? 21.874  -28.798 3.299   1.00 24.39  ? 168 THR A O   1 
ATOM   1309 C CB  . THR A 1 166 ? 19.405  -27.121 2.316   1.00 27.11  ? 168 THR A CB  1 
ATOM   1310 O OG1 . THR A 1 166 ? 18.916  -27.992 3.332   1.00 28.36  ? 168 THR A OG1 1 
ATOM   1311 C CG2 . THR A 1 166 ? 19.217  -27.747 0.953   1.00 28.55  ? 168 THR A CG2 1 
ATOM   1312 N N   . GLU A 1 167 ? 22.486  -28.020 1.275   1.00 24.70  ? 169 GLU A N   1 
ATOM   1313 C CA  . GLU A 1 167 ? 23.219  -29.217 0.892   1.00 25.41  ? 169 GLU A CA  1 
ATOM   1314 C C   . GLU A 1 167 ? 24.503  -28.897 0.097   1.00 26.54  ? 169 GLU A C   1 
ATOM   1315 O O   . GLU A 1 167 ? 24.423  -28.575 -1.083  1.00 27.32  ? 169 GLU A O   1 
ATOM   1316 C CB  . GLU A 1 167 ? 22.280  -30.135 0.055   1.00 25.45  ? 169 GLU A CB  1 
ATOM   1317 C CG  . GLU A 1 167 ? 22.872  -31.437 -0.423  1.00 26.48  ? 169 GLU A CG  1 
ATOM   1318 C CD  . GLU A 1 167 ? 23.637  -32.192 0.632   1.00 24.80  ? 169 GLU A CD  1 
ATOM   1319 O OE1 . GLU A 1 167 ? 22.995  -32.797 1.506   1.00 29.15  ? 169 GLU A OE1 1 
ATOM   1320 O OE2 . GLU A 1 167 ? 24.881  -32.146 0.606   1.00 26.10  ? 169 GLU A OE2 1 
ATOM   1321 N N   . CYS A 1 168 ? 25.663  -29.003 0.728   1.00 27.31  ? 170 CYS A N   1 
ATOM   1322 C CA  . CYS A 1 168 ? 26.929  -28.675 0.062   1.00 29.74  ? 170 CYS A CA  1 
ATOM   1323 C C   . CYS A 1 168 ? 27.282  -29.603 -1.131  1.00 29.79  ? 170 CYS A C   1 
ATOM   1324 O O   . CYS A 1 168 ? 28.049  -29.155 -1.969  1.00 29.22  ? 170 CYS A O   1 
ATOM   1325 C CB  . CYS A 1 168 ? 28.073  -28.606 1.068   1.00 31.04  ? 170 CYS A CB  1 
ATOM   1326 S SG  . CYS A 1 168 ? 28.374  -30.155 1.931   1.00 36.19  ? 170 CYS A SG  1 
ATOM   1327 N N   . GLU A 1 169 ? 26.719  -30.849 -1.229  1.00 29.59  ? 171 GLU A N   1 
ATOM   1328 C CA  . GLU A 1 169 ? 26.948  -31.760 -2.362  1.00 28.47  ? 171 GLU A CA  1 
ATOM   1329 C C   . GLU A 1 169 ? 26.078  -31.503 -3.598  1.00 27.86  ? 171 GLU A C   1 
ATOM   1330 O O   . GLU A 1 169 ? 26.250  -32.169 -4.613  1.00 28.14  ? 171 GLU A O   1 
ATOM   1331 C CB  . GLU A 1 169 ? 26.765  -33.237 -1.933  1.00 29.15  ? 171 GLU A CB  1 
ATOM   1332 C CG  . GLU A 1 169 ? 27.629  -33.648 -0.769  1.00 31.62  ? 171 GLU A CG  1 
ATOM   1333 C CD  . GLU A 1 169 ? 29.117  -33.452 -0.906  1.00 35.74  ? 171 GLU A CD  1 
ATOM   1334 O OE1 . GLU A 1 169 ? 29.630  -33.546 -2.046  1.00 38.39  ? 171 GLU A OE1 1 
ATOM   1335 O OE2 . GLU A 1 169 ? 29.778  -33.227 0.137   1.00 33.55  ? 171 GLU A OE2 1 
ATOM   1336 N N   . ASN A 1 170 ? 25.132  -30.577 -3.525  1.00 27.38  ? 172 ASN A N   1 
ATOM   1337 C CA  . ASN A 1 170 ? 24.414  -30.089 -4.713  1.00 27.55  ? 172 ASN A CA  1 
ATOM   1338 C C   . ASN A 1 170 ? 25.219  -29.000 -5.449  1.00 27.45  ? 172 ASN A C   1 
ATOM   1339 O O   . ASN A 1 170 ? 24.879  -27.809 -5.364  1.00 25.04  ? 172 ASN A O   1 
ATOM   1340 C CB  . ASN A 1 170 ? 23.029  -29.517 -4.290  1.00 29.04  ? 172 ASN A CB  1 
ATOM   1341 C CG  . ASN A 1 170 ? 22.029  -30.539 -3.864  1.00 28.52  ? 172 ASN A CG  1 
ATOM   1342 O OD1 . ASN A 1 170 ? 22.200  -31.761 -4.055  1.00 33.43  ? 172 ASN A OD1 1 
ATOM   1343 N ND2 . ASN A 1 170 ? 20.960  -30.081 -3.286  1.00 22.63  ? 172 ASN A ND2 1 
ATOM   1344 N N   . ARG A 1 171 ? 26.301  -29.397 -6.151  1.00 29.58  ? 173 ARG A N   1 
ATOM   1345 C CA  . ARG A 1 171 ? 27.195  -28.451 -6.838  1.00 32.49  ? 173 ARG A CA  1 
ATOM   1346 C C   . ARG A 1 171 ? 26.413  -27.561 -7.832  1.00 33.28  ? 173 ARG A C   1 
ATOM   1347 O O   . ARG A 1 171 ? 26.605  -26.372 -7.807  1.00 32.75  ? 173 ARG A O   1 
ATOM   1348 C CB  . ARG A 1 171 ? 28.354  -29.204 -7.527  1.00 37.04  ? 173 ARG A CB  1 
ATOM   1349 C CG  . ARG A 1 171 ? 29.432  -28.345 -8.274  1.00 45.37  ? 173 ARG A CG  1 
ATOM   1350 C CD  . ARG A 1 171 ? 29.095  -27.986 -9.741  1.00 53.60  ? 173 ARG A CD  1 
ATOM   1351 N NE  . ARG A 1 171 ? 28.645  -29.149 -10.527 1.00 61.72  ? 173 ARG A NE  1 
ATOM   1352 C CZ  . ARG A 1 171 ? 27.884  -29.109 -11.629 1.00 68.16  ? 173 ARG A CZ  1 
ATOM   1353 N NH1 . ARG A 1 171 ? 27.457  -27.942 -12.117 1.00 69.21  ? 173 ARG A NH1 1 
ATOM   1354 N NH2 . ARG A 1 171 ? 27.542  -30.237 -12.250 1.00 69.82  ? 173 ARG A NH2 1 
ATOM   1355 N N   . GLU A 1 172 ? 25.526  -28.120 -8.672  1.00 33.52  ? 174 GLU A N   1 
ATOM   1356 C CA  . GLU A 1 172 ? 24.766  -27.320 -9.642  1.00 33.95  ? 174 GLU A CA  1 
ATOM   1357 C C   . GLU A 1 172 ? 23.940  -26.218 -8.976  1.00 32.57  ? 174 GLU A C   1 
ATOM   1358 O O   . GLU A 1 172 ? 23.979  -25.068 -9.426  1.00 32.22  ? 174 GLU A O   1 
ATOM   1359 C CB  . GLU A 1 172 ? 23.818  -28.199 -10.464 1.00 37.20  ? 174 GLU A CB  1 
ATOM   1360 C CG  . GLU A 1 172 ? 24.503  -29.189 -11.351 1.00 50.82  ? 174 GLU A CG  1 
ATOM   1361 C CD  . GLU A 1 172 ? 23.553  -30.180 -12.006 1.00 65.18  ? 174 GLU A CD  1 
ATOM   1362 O OE1 . GLU A 1 172 ? 22.973  -29.826 -13.058 1.00 70.34  ? 174 GLU A OE1 1 
ATOM   1363 O OE2 . GLU A 1 172 ? 23.389  -31.303 -11.471 1.00 66.84  ? 174 GLU A OE2 1 
ATOM   1364 N N   . ALA A 1 173 ? 23.184  -26.581 -7.909  1.00 30.83  ? 175 ALA A N   1 
ATOM   1365 C CA  . ALA A 1 173 ? 22.406  -25.617 -7.152  1.00 29.68  ? 175 ALA A CA  1 
ATOM   1366 C C   . ALA A 1 173 ? 23.298  -24.546 -6.507  1.00 27.33  ? 175 ALA A C   1 
ATOM   1367 O O   . ALA A 1 173 ? 23.015  -23.359 -6.653  1.00 25.29  ? 175 ALA A O   1 
ATOM   1368 C CB  . ALA A 1 173 ? 21.578  -26.319 -6.090  1.00 30.64  ? 175 ALA A CB  1 
ATOM   1369 N N   . VAL A 1 174 ? 24.356  -24.984 -5.768  1.00 26.47  ? 176 VAL A N   1 
ATOM   1370 C CA  . VAL A 1 174 ? 25.239  -24.133 -4.998  1.00 26.50  ? 176 VAL A CA  1 
ATOM   1371 C C   . VAL A 1 174 ? 25.925  -23.148 -5.952  1.00 27.95  ? 176 VAL A C   1 
ATOM   1372 O O   . VAL A 1 174 ? 25.956  -21.954 -5.652  1.00 27.90  ? 176 VAL A O   1 
ATOM   1373 C CB  . VAL A 1 174 ? 26.243  -24.988 -4.174  1.00 27.10  ? 176 VAL A CB  1 
ATOM   1374 C CG1 . VAL A 1 174 ? 27.425  -24.160 -3.679  1.00 28.35  ? 176 VAL A CG1 1 
ATOM   1375 C CG2 . VAL A 1 174 ? 25.529  -25.675 -3.011  1.00 28.09  ? 176 VAL A CG2 1 
ATOM   1376 N N   . THR A 1 175 ? 26.445  -23.627 -7.108  1.00 27.64  ? 177 THR A N   1 
ATOM   1377 C CA  . THR A 1 175 ? 27.221  -22.758 -7.968  1.00 29.50  ? 177 THR A CA  1 
ATOM   1378 C C   . THR A 1 175 ? 26.321  -21.775 -8.718  1.00 28.93  ? 177 THR A C   1 
ATOM   1379 O O   . THR A 1 175 ? 26.711  -20.639 -8.916  1.00 28.13  ? 177 THR A O   1 
ATOM   1380 C CB  . THR A 1 175 ? 28.217  -23.522 -8.905  1.00 31.31  ? 177 THR A CB  1 
ATOM   1381 O OG1 . THR A 1 175 ? 27.484  -24.280 -9.812  1.00 35.74  ? 177 THR A OG1 1 
ATOM   1382 C CG2 . THR A 1 175 ? 29.180  -24.413 -8.162  1.00 29.58  ? 177 THR A CG2 1 
ATOM   1383 N N   . HIS A 1 176 ? 25.127  -22.184 -9.122  1.00 29.21  ? 178 HIS A N   1 
ATOM   1384 C CA  . HIS A 1 176 ? 24.137  -21.231 -9.689  1.00 27.92  ? 178 HIS A CA  1 
ATOM   1385 C C   . HIS A 1 176 ? 23.756  -20.175 -8.652  1.00 28.51  ? 178 HIS A C   1 
ATOM   1386 O O   . HIS A 1 176 ? 23.667  -18.995 -9.010  1.00 30.47  ? 178 HIS A O   1 
ATOM   1387 C CB  . HIS A 1 176 ? 22.888  -21.963 -10.213 1.00 27.08  ? 178 HIS A CB  1 
ATOM   1388 C CG  . HIS A 1 176 ? 21.812  -21.073 -10.779 1.00 31.56  ? 178 HIS A CG  1 
ATOM   1389 N ND1 . HIS A 1 176 ? 21.734  -20.822 -12.139 1.00 34.43  ? 178 HIS A ND1 1 
ATOM   1390 C CD2 . HIS A 1 176 ? 20.794  -20.415 -10.166 1.00 33.80  ? 178 HIS A CD2 1 
ATOM   1391 C CE1 . HIS A 1 176 ? 20.686  -20.027 -12.320 1.00 34.57  ? 178 HIS A CE1 1 
ATOM   1392 N NE2 . HIS A 1 176 ? 20.086  -19.738 -11.168 1.00 34.62  ? 178 HIS A NE2 1 
ATOM   1393 N N   . ILE A 1 177 ? 23.537  -20.552 -7.362  1.00 26.29  ? 179 ILE A N   1 
ATOM   1394 C CA  . ILE A 1 177 ? 23.219  -19.553 -6.322  1.00 25.80  ? 179 ILE A CA  1 
ATOM   1395 C C   . ILE A 1 177 ? 24.371  -18.541 -6.226  1.00 27.44  ? 179 ILE A C   1 
ATOM   1396 O O   . ILE A 1 177 ? 24.129  -17.342 -6.209  1.00 28.10  ? 179 ILE A O   1 
ATOM   1397 C CB  . ILE A 1 177 ? 22.894  -20.181 -4.921  1.00 23.67  ? 179 ILE A CB  1 
ATOM   1398 C CG1 . ILE A 1 177 ? 21.537  -20.940 -4.966  1.00 24.26  ? 179 ILE A CG1 1 
ATOM   1399 C CG2 . ILE A 1 177 ? 22.924  -19.149 -3.777  1.00 22.73  ? 179 ILE A CG2 1 
ATOM   1400 C CD1 . ILE A 1 177 ? 21.359  -22.019 -3.926  1.00 22.80  ? 179 ILE A CD1 1 
ATOM   1401 N N   . GLY A 1 178 ? 25.582  -19.063 -6.157  1.00 27.70  ? 180 GLY A N   1 
ATOM   1402 C CA  . GLY A 1 178 ? 26.813  -18.297 -6.094  1.00 27.94  ? 180 GLY A CA  1 
ATOM   1403 C C   . GLY A 1 178 ? 26.972  -17.274 -7.191  1.00 27.94  ? 180 GLY A C   1 
ATOM   1404 O O   . GLY A 1 178 ? 27.284  -16.112 -6.917  1.00 27.36  ? 180 GLY A O   1 
ATOM   1405 N N   . ARG A 1 179 ? 26.751  -17.702 -8.433  1.00 28.39  ? 181 ARG A N   1 
ATOM   1406 C CA  . ARG A 1 179 ? 26.942  -16.864 -9.622  1.00 28.96  ? 181 ARG A CA  1 
ATOM   1407 C C   . ARG A 1 179 ? 25.906  -15.767 -9.696  1.00 28.28  ? 181 ARG A C   1 
ATOM   1408 O O   . ARG A 1 179 ? 26.252  -14.633 -10.030 1.00 28.78  ? 181 ARG A O   1 
ATOM   1409 C CB  . ARG A 1 179 ? 26.872  -17.691 -10.930 1.00 31.48  ? 181 ARG A CB  1 
ATOM   1410 C CG  . ARG A 1 179 ? 27.996  -18.712 -10.986 1.00 39.94  ? 181 ARG A CG  1 
ATOM   1411 C CD  . ARG A 1 179 ? 28.346  -19.192 -12.372 1.00 48.08  ? 181 ARG A CD  1 
ATOM   1412 N NE  . ARG A 1 179 ? 29.424  -20.190 -12.283 1.00 56.21  ? 181 ARG A NE  1 
ATOM   1413 C CZ  . ARG A 1 179 ? 30.731  -19.951 -12.399 1.00 59.86  ? 181 ARG A CZ  1 
ATOM   1414 N NH1 . ARG A 1 179 ? 31.176  -18.712 -12.652 1.00 58.30  ? 181 ARG A NH1 1 
ATOM   1415 N NH2 . ARG A 1 179 ? 31.604  -20.946 -12.276 1.00 60.69  ? 181 ARG A NH2 1 
ATOM   1416 N N   . VAL A 1 180 ? 24.653  -16.096 -9.429  1.00 27.45  ? 182 VAL A N   1 
ATOM   1417 C CA  . VAL A 1 180 ? 23.600  -15.113 -9.429  1.00 28.22  ? 182 VAL A CA  1 
ATOM   1418 C C   . VAL A 1 180 ? 23.767  -14.115 -8.290  1.00 28.58  ? 182 VAL A C   1 
ATOM   1419 O O   . VAL A 1 180 ? 23.578  -12.910 -8.494  1.00 30.94  ? 182 VAL A O   1 
ATOM   1420 C CB  . VAL A 1 180 ? 22.238  -15.790 -9.385  1.00 29.57  ? 182 VAL A CB  1 
ATOM   1421 C CG1 . VAL A 1 180 ? 21.125  -14.770 -9.221  1.00 30.18  ? 182 VAL A CG1 1 
ATOM   1422 C CG2 . VAL A 1 180 ? 22.024  -16.642 -10.655 1.00 30.98  ? 182 VAL A CG2 1 
ATOM   1423 N N   . TYR A 1 181 ? 24.097  -14.595 -7.099  1.00 25.44  ? 183 TYR A N   1 
ATOM   1424 C CA  . TYR A 1 181 ? 24.311  -13.726 -5.949  1.00 25.21  ? 183 TYR A CA  1 
ATOM   1425 C C   . TYR A 1 181 ? 25.427  -12.700 -6.224  1.00 27.74  ? 183 TYR A C   1 
ATOM   1426 O O   . TYR A 1 181 ? 25.231  -11.536 -5.941  1.00 27.57  ? 183 TYR A O   1 
ATOM   1427 C CB  . TYR A 1 181 ? 24.676  -14.588 -4.743  1.00 23.32  ? 183 TYR A CB  1 
ATOM   1428 C CG  . TYR A 1 181 ? 24.875  -13.888 -3.429  1.00 23.08  ? 183 TYR A CG  1 
ATOM   1429 C CD1 . TYR A 1 181 ? 24.067  -12.820 -3.055  1.00 23.69  ? 183 TYR A CD1 1 
ATOM   1430 C CD2 . TYR A 1 181 ? 25.816  -14.337 -2.517  1.00 22.40  ? 183 TYR A CD2 1 
ATOM   1431 C CE1 . TYR A 1 181 ? 24.187  -12.232 -1.815  1.00 22.63  ? 183 TYR A CE1 1 
ATOM   1432 C CE2 . TYR A 1 181 ? 25.955  -13.741 -1.278  1.00 22.19  ? 183 TYR A CE2 1 
ATOM   1433 C CZ  . TYR A 1 181 ? 25.125  -12.695 -0.924  1.00 22.10  ? 183 TYR A CZ  1 
ATOM   1434 O OH  . TYR A 1 181 ? 25.246  -12.088 0.285   1.00 21.10  ? 183 TYR A OH  1 
ATOM   1435 N N   . LYS A 1 182 ? 26.580  -13.149 -6.775  1.00 28.19  ? 184 LYS A N   1 
ATOM   1436 C CA  . LYS A 1 182 ? 27.735  -12.284 -7.056  1.00 30.09  ? 184 LYS A CA  1 
ATOM   1437 C C   . LYS A 1 182 ? 27.343  -11.194 -8.097  1.00 31.16  ? 184 LYS A C   1 
ATOM   1438 O O   . LYS A 1 182 ? 27.787  -10.057 -7.992  1.00 31.79  ? 184 LYS A O   1 
ATOM   1439 C CB  . LYS A 1 182 ? 28.893  -13.133 -7.612  1.00 31.77  ? 184 LYS A CB  1 
ATOM   1440 C CG  . LYS A 1 182 ? 30.159  -12.377 -7.852  1.00 35.17  ? 184 LYS A CG  1 
ATOM   1441 C CD  . LYS A 1 182 ? 31.260  -13.267 -8.339  1.00 37.51  ? 184 LYS A CD  1 
ATOM   1442 C CE  . LYS A 1 182 ? 32.418  -12.427 -8.824  1.00 40.38  ? 184 LYS A CE  1 
ATOM   1443 N NZ  . LYS A 1 182 ? 33.588  -13.245 -9.171  1.00 40.79  ? 184 LYS A NZ  1 
ATOM   1444 N N   . GLU A 1 183 ? 26.525  -11.584 -9.092  1.00 30.04  ? 185 GLU A N   1 
ATOM   1445 C CA  . GLU A 1 183 ? 25.985  -10.695 -10.114 1.00 30.33  ? 185 GLU A CA  1 
ATOM   1446 C C   . GLU A 1 183 ? 25.105  -9.598  -9.429  1.00 30.97  ? 185 GLU A C   1 
ATOM   1447 O O   . GLU A 1 183 ? 25.254  -8.391  -9.698  1.00 30.27  ? 185 GLU A O   1 
ATOM   1448 C CB  . GLU A 1 183 ? 25.209  -11.544 -11.113 1.00 32.49  ? 185 GLU A CB  1 
ATOM   1449 C CG  . GLU A 1 183 ? 24.609  -10.951 -12.368 1.00 42.11  ? 185 GLU A CG  1 
ATOM   1450 C CD  . GLU A 1 183 ? 23.652  -12.015 -12.906 1.00 55.59  ? 185 GLU A CD  1 
ATOM   1451 O OE1 . GLU A 1 183 ? 24.122  -13.131 -13.246 1.00 57.80  ? 185 GLU A OE1 1 
ATOM   1452 O OE2 . GLU A 1 183 ? 22.426  -11.745 -12.948 1.00 59.35  ? 185 GLU A OE2 1 
ATOM   1453 N N   . ARG A 1 184 ? 24.221  -10.023 -8.523  1.00 31.02  ? 186 ARG A N   1 
ATOM   1454 C CA  . ARG A 1 184 ? 23.303  -9.143  -7.846  1.00 31.57  ? 186 ARG A CA  1 
ATOM   1455 C C   . ARG A 1 184 ? 23.967  -8.246  -6.826  1.00 32.49  ? 186 ARG A C   1 
ATOM   1456 O O   . ARG A 1 184 ? 23.473  -7.146  -6.584  1.00 33.13  ? 186 ARG A O   1 
ATOM   1457 C CB  . ARG A 1 184 ? 22.167  -9.946  -7.211  1.00 34.00  ? 186 ARG A CB  1 
ATOM   1458 C CG  . ARG A 1 184 ? 21.216  -10.582 -8.232  1.00 34.94  ? 186 ARG A CG  1 
ATOM   1459 C CD  . ARG A 1 184 ? 20.204  -9.609  -8.764  1.00 35.51  ? 186 ARG A CD  1 
ATOM   1460 N NE  . ARG A 1 184 ? 19.220  -9.206  -7.761  1.00 35.29  ? 186 ARG A NE  1 
ATOM   1461 C CZ  . ARG A 1 184 ? 17.975  -9.658  -7.652  1.00 33.09  ? 186 ARG A CZ  1 
ATOM   1462 N NH1 . ARG A 1 184 ? 17.510  -10.569 -8.499  1.00 33.31  ? 186 ARG A NH1 1 
ATOM   1463 N NH2 . ARG A 1 184 ? 17.178  -9.193  -6.700  1.00 31.86  ? 186 ARG A NH2 1 
ATOM   1464 N N   . LEU A 1 185 ? 25.078  -8.673  -6.238  1.00 33.03  ? 187 LEU A N   1 
ATOM   1465 C CA  . LEU A 1 185 ? 25.906  -7.790  -5.424  1.00 33.65  ? 187 LEU A CA  1 
ATOM   1466 C C   . LEU A 1 185 ? 26.719  -6.774  -6.287  1.00 36.62  ? 187 LEU A C   1 
ATOM   1467 O O   . LEU A 1 185 ? 27.303  -5.860  -5.732  1.00 35.72  ? 187 LEU A O   1 
ATOM   1468 C CB  . LEU A 1 185 ? 26.868  -8.604  -4.535  1.00 32.12  ? 187 LEU A CB  1 
ATOM   1469 C CG  . LEU A 1 185 ? 26.238  -9.439  -3.400  1.00 31.88  ? 187 LEU A CG  1 
ATOM   1470 C CD1 . LEU A 1 185 ? 27.219  -10.459 -2.849  1.00 30.83  ? 187 LEU A CD1 1 
ATOM   1471 C CD2 . LEU A 1 185 ? 25.718  -8.576  -2.258  1.00 32.34  ? 187 LEU A CD2 1 
ATOM   1472 N N   . GLY A 1 186 ? 26.741  -6.948  -7.609  1.00 39.41  ? 188 GLY A N   1 
ATOM   1473 C CA  . GLY A 1 186 ? 27.547  -6.151  -8.516  1.00 42.67  ? 188 GLY A CA  1 
ATOM   1474 C C   . GLY A 1 186 ? 29.016  -6.237  -8.193  1.00 45.23  ? 188 GLY A C   1 
ATOM   1475 O O   . GLY A 1 186 ? 29.695  -5.217  -8.190  1.00 46.14  ? 188 GLY A O   1 
ATOM   1476 N N   . LEU A 1 187 ? 29.505  -7.433  -7.897  1.00 46.60  ? 189 LEU A N   1 
ATOM   1477 C CA  . LEU A 1 187 ? 30.900  -7.611  -7.537  1.00 48.54  ? 189 LEU A CA  1 
ATOM   1478 C C   . LEU A 1 187 ? 31.739  -7.786  -8.804  1.00 52.29  ? 189 LEU A C   1 
ATOM   1479 O O   . LEU A 1 187 ? 31.291  -8.472  -9.721  1.00 52.56  ? 189 LEU A O   1 
ATOM   1480 C CB  . LEU A 1 187 ? 31.096  -8.836  -6.609  1.00 47.64  ? 189 LEU A CB  1 
ATOM   1481 C CG  . LEU A 1 187 ? 30.672  -8.711  -5.159  1.00 46.91  ? 189 LEU A CG  1 
ATOM   1482 C CD1 . LEU A 1 187 ? 30.995  -9.948  -4.405  1.00 45.27  ? 189 LEU A CD1 1 
ATOM   1483 C CD2 . LEU A 1 187 ? 31.338  -7.563  -4.486  1.00 48.22  ? 189 LEU A CD2 1 
ATOM   1484 N N   . PRO A 1 188 ? 32.948  -7.175  -8.880  1.00 55.01  ? 190 PRO A N   1 
ATOM   1485 C CA  . PRO A 1 188 ? 33.818  -7.434  -10.037 1.00 56.86  ? 190 PRO A CA  1 
ATOM   1486 C C   . PRO A 1 188 ? 34.201  -8.909  -10.181 1.00 58.96  ? 190 PRO A C   1 
ATOM   1487 O O   . PRO A 1 188 ? 34.396  -9.565  -9.167  1.00 59.84  ? 190 PRO A O   1 
ATOM   1488 C CB  . PRO A 1 188 ? 35.087  -6.605  -9.749  1.00 58.05  ? 190 PRO A CB  1 
ATOM   1489 C CG  . PRO A 1 188 ? 34.785  -5.731  -8.598  1.00 58.09  ? 190 PRO A CG  1 
ATOM   1490 C CD  . PRO A 1 188 ? 33.554  -6.219  -7.923  1.00 55.45  ? 190 PRO A CD  1 
ATOM   1491 N N   . PRO A 1 189 ? 34.330  -9.455  -11.407 1.00 60.12  ? 191 PRO A N   1 
ATOM   1492 C CA  . PRO A 1 189 ? 34.833  -10.841 -11.560 1.00 60.56  ? 191 PRO A CA  1 
ATOM   1493 C C   . PRO A 1 189 ? 36.184  -11.167 -10.921 1.00 60.07  ? 191 PRO A C   1 
ATOM   1494 O O   . PRO A 1 189 ? 36.486  -12.343 -10.687 1.00 60.11  ? 191 PRO A O   1 
ATOM   1495 C CB  . PRO A 1 189 ? 34.943  -11.010 -13.079 1.00 62.03  ? 191 PRO A CB  1 
ATOM   1496 C CG  . PRO A 1 189 ? 34.014  -10.010 -13.657 1.00 62.64  ? 191 PRO A CG  1 
ATOM   1497 C CD  . PRO A 1 189 ? 34.006  -8.845  -12.715 1.00 60.37  ? 191 PRO A CD  1 
ATOM   1498 N N   . LYS A 1 190 ? 37.003  -10.145 -10.675 1.00 59.49  ? 192 LYS A N   1 
ATOM   1499 C CA  . LYS A 1 190 ? 38.257  -10.293 -9.939  1.00 59.64  ? 192 LYS A CA  1 
ATOM   1500 C C   . LYS A 1 190 ? 37.982  -10.724 -8.495  1.00 57.83  ? 192 LYS A C   1 
ATOM   1501 O O   . LYS A 1 190 ? 38.726  -11.524 -7.932  1.00 57.95  ? 192 LYS A O   1 
ATOM   1502 C CB  . LYS A 1 190 ? 39.021  -8.955  -9.924  1.00 63.82  ? 192 LYS A CB  1 
ATOM   1503 C CG  . LYS A 1 190 ? 39.581  -8.546  -11.282 1.00 72.50  ? 192 LYS A CG  1 
ATOM   1504 C CD  . LYS A 1 190 ? 39.965  -7.043  -11.324 1.00 79.09  ? 192 LYS A CD  1 
ATOM   1505 C CE  . LYS A 1 190 ? 40.888  -6.713  -12.481 1.00 84.05  ? 192 LYS A CE  1 
ATOM   1506 N NZ  . LYS A 1 190 ? 41.546  -5.389  -12.291 1.00 86.81  ? 192 LYS A NZ  1 
ATOM   1507 N N   . ILE A 1 191 ? 36.922  -10.174 -7.889  1.00 56.40  ? 193 ILE A N   1 
ATOM   1508 C CA  . ILE A 1 191 ? 36.567  -10.488 -6.511  1.00 55.64  ? 193 ILE A CA  1 
ATOM   1509 C C   . ILE A 1 191 ? 35.896  -11.845 -6.569  1.00 54.68  ? 193 ILE A C   1 
ATOM   1510 O O   . ILE A 1 191 ? 34.790  -11.944 -7.077  1.00 54.86  ? 193 ILE A O   1 
ATOM   1511 C CB  . ILE A 1 191 ? 35.629  -9.420  -5.902  1.00 55.07  ? 193 ILE A CB  1 
ATOM   1512 C CG1 . ILE A 1 191 ? 36.255  -8.009  -5.960  1.00 55.80  ? 193 ILE A CG1 1 
ATOM   1513 C CG2 . ILE A 1 191 ? 35.266  -9.796  -4.468  1.00 55.17  ? 193 ILE A CG2 1 
ATOM   1514 C CD1 . ILE A 1 191 ? 37.640  -7.803  -5.197  1.00 55.95  ? 193 ILE A CD1 1 
ATOM   1515 N N   . VAL A 1 192 ? 36.567  -12.875 -6.089  1.00 53.44  ? 194 VAL A N   1 
ATOM   1516 C CA  . VAL A 1 192 ? 35.997  -14.215 -6.045  1.00 52.61  ? 194 VAL A CA  1 
ATOM   1517 C C   . VAL A 1 192 ? 35.371  -14.453 -4.679  1.00 50.57  ? 194 VAL A C   1 
ATOM   1518 O O   . VAL A 1 192 ? 35.983  -14.141 -3.663  1.00 51.68  ? 194 VAL A O   1 
ATOM   1519 C CB  . VAL A 1 192 ? 37.041  -15.291 -6.392  1.00 54.18  ? 194 VAL A CB  1 
ATOM   1520 C CG1 . VAL A 1 192 ? 37.784  -14.953 -7.700  1.00 54.75  ? 194 VAL A CG1 1 
ATOM   1521 C CG2 . VAL A 1 192 ? 38.020  -15.511 -5.247  1.00 54.90  ? 194 VAL A CG2 1 
ATOM   1522 N N   . ILE A 1 193 ? 34.134  -15.002 -4.649  1.00 46.81  ? 195 ILE A N   1 
ATOM   1523 C CA  . ILE A 1 193 ? 33.444  -15.379 -3.400  1.00 41.84  ? 195 ILE A CA  1 
ATOM   1524 C C   . ILE A 1 193 ? 33.570  -16.890 -3.221  1.00 36.99  ? 195 ILE A C   1 
ATOM   1525 O O   . ILE A 1 193 ? 33.680  -17.627 -4.202  1.00 36.91  ? 195 ILE A O   1 
ATOM   1526 C CB  . ILE A 1 193 ? 31.995  -14.852 -3.321  1.00 41.14  ? 195 ILE A CB  1 
ATOM   1527 C CG1 . ILE A 1 193 ? 31.076  -15.488 -4.381  1.00 39.88  ? 195 ILE A CG1 1 
ATOM   1528 C CG2 . ILE A 1 193 ? 32.002  -13.357 -3.480  1.00 42.22  ? 195 ILE A CG2 1 
ATOM   1529 C CD1 . ILE A 1 193 ? 29.589  -15.125 -4.236  1.00 38.93  ? 195 ILE A CD1 1 
ATOM   1530 N N   . GLY A 1 194 ? 33.612  -17.329 -1.975  1.00 33.36  ? 196 GLY A N   1 
ATOM   1531 C CA  . GLY A 1 194 ? 33.813  -18.744 -1.675  1.00 31.49  ? 196 GLY A CA  1 
ATOM   1532 C C   . GLY A 1 194 ? 32.640  -19.350 -0.934  1.00 29.89  ? 196 GLY A C   1 
ATOM   1533 O O   . GLY A 1 194 ? 31.998  -18.668 -0.119  1.00 29.40  ? 196 GLY A O   1 
ATOM   1534 N N   . TYR A 1 195 ? 32.350  -20.655 -1.227  1.00 29.46  ? 197 TYR A N   1 
ATOM   1535 C CA  . TYR A 1 195 ? 31.345  -21.457 -0.575  1.00 29.20  ? 197 TYR A CA  1 
ATOM   1536 C C   . TYR A 1 195 ? 32.057  -22.390 0.369   1.00 30.23  ? 197 TYR A C   1 
ATOM   1537 O O   . TYR A 1 195 ? 32.935  -23.133 -0.057  1.00 30.68  ? 197 TYR A O   1 
ATOM   1538 C CB  . TYR A 1 195 ? 30.518  -22.287 -1.569  1.00 29.75  ? 197 TYR A CB  1 
ATOM   1539 C CG  . TYR A 1 195 ? 29.370  -23.065 -0.929  1.00 30.94  ? 197 TYR A CG  1 
ATOM   1540 C CD1 . TYR A 1 195 ? 28.119  -22.504 -0.803  1.00 32.10  ? 197 TYR A CD1 1 
ATOM   1541 C CD2 . TYR A 1 195 ? 29.548  -24.370 -0.462  1.00 32.34  ? 197 TYR A CD2 1 
ATOM   1542 C CE1 . TYR A 1 195 ? 27.067  -23.198 -0.221  1.00 32.41  ? 197 TYR A CE1 1 
ATOM   1543 C CE2 . TYR A 1 195 ? 28.500  -25.078 0.126   1.00 32.10  ? 197 TYR A CE2 1 
ATOM   1544 C CZ  . TYR A 1 195 ? 27.257  -24.488 0.232   1.00 32.39  ? 197 TYR A CZ  1 
ATOM   1545 O OH  . TYR A 1 195 ? 26.193  -25.137 0.804   1.00 32.70  ? 197 TYR A OH  1 
ATOM   1546 N N   . GLN A 1 196 ? 31.657  -22.368 1.629   1.00 29.48  ? 198 GLN A N   1 
ATOM   1547 C CA  . GLN A 1 196 ? 32.215  -23.152 2.701   1.00 29.69  ? 198 GLN A CA  1 
ATOM   1548 C C   . GLN A 1 196 ? 31.128  -24.030 3.289   1.00 29.75  ? 198 GLN A C   1 
ATOM   1549 O O   . GLN A 1 196 ? 30.061  -23.534 3.694   1.00 28.74  ? 198 GLN A O   1 
ATOM   1550 C CB  . GLN A 1 196 ? 32.716  -22.234 3.831   1.00 30.79  ? 198 GLN A CB  1 
ATOM   1551 C CG  . GLN A 1 196 ? 33.646  -21.123 3.403   1.00 39.73  ? 198 GLN A CG  1 
ATOM   1552 C CD  . GLN A 1 196 ? 33.807  -20.063 4.479   1.00 50.60  ? 198 GLN A CD  1 
ATOM   1553 O OE1 . GLN A 1 196 ? 32.827  -19.555 5.043   1.00 51.88  ? 198 GLN A OE1 1 
ATOM   1554 N NE2 . GLN A 1 196 ? 35.051  -19.700 4.793   1.00 54.64  ? 198 GLN A NE2 1 
ATOM   1555 N N   . SER A 1 197 ? 31.405  -25.333 3.361   1.00 29.96  ? 199 SER A N   1 
ATOM   1556 C CA  . SER A 1 197 ? 30.614  -26.310 4.125   1.00 30.76  ? 199 SER A CA  1 
ATOM   1557 C C   . SER A 1 197 ? 30.544  -25.863 5.568   1.00 30.92  ? 199 SER A C   1 
ATOM   1558 O O   . SER A 1 197 ? 31.563  -25.414 6.104   1.00 31.30  ? 199 SER A O   1 
ATOM   1559 C CB  . SER A 1 197 ? 31.311  -27.665 4.077   1.00 34.70  ? 199 SER A CB  1 
ATOM   1560 O OG  . SER A 1 197 ? 30.556  -28.683 4.705   1.00 42.87  ? 199 SER A OG  1 
ATOM   1561 N N   . HIS A 1 198 ? 29.391  -25.955 6.192   1.00 30.87  ? 200 HIS A N   1 
ATOM   1562 C CA  . HIS A 1 198 ? 29.296  -25.643 7.617   1.00 31.43  ? 200 HIS A CA  1 
ATOM   1563 C C   . HIS A 1 198 ? 30.161  -26.622 8.463   1.00 34.90  ? 200 HIS A C   1 
ATOM   1564 O O   . HIS A 1 198 ? 30.727  -26.218 9.479   1.00 34.34  ? 200 HIS A O   1 
ATOM   1565 C CB  . HIS A 1 198 ? 27.853  -25.679 8.094   1.00 29.13  ? 200 HIS A CB  1 
ATOM   1566 C CG  . HIS A 1 198 ? 26.997  -24.577 7.562   1.00 29.11  ? 200 HIS A CG  1 
ATOM   1567 N ND1 . HIS A 1 198 ? 27.485  -23.285 7.378   1.00 30.16  ? 200 HIS A ND1 1 
ATOM   1568 C CD2 . HIS A 1 198 ? 25.700  -24.606 7.186   1.00 29.56  ? 200 HIS A CD2 1 
ATOM   1569 C CE1 . HIS A 1 198 ? 26.476  -22.594 6.885   1.00 30.93  ? 200 HIS A CE1 1 
ATOM   1570 N NE2 . HIS A 1 198 ? 25.378  -23.354 6.758   1.00 31.15  ? 200 HIS A NE2 1 
ATOM   1571 N N   . ALA A 1 199 ? 30.239  -27.898 8.042   1.00 37.39  ? 201 ALA A N   1 
ATOM   1572 C CA  . ALA A 1 199 ? 31.107  -28.875 8.714   1.00 40.81  ? 201 ALA A CA  1 
ATOM   1573 C C   . ALA A 1 199 ? 32.615  -28.479 8.684   1.00 42.98  ? 201 ALA A C   1 
ATOM   1574 O O   . ALA A 1 199 ? 33.310  -28.781 9.638   1.00 42.58  ? 201 ALA A O   1 
ATOM   1575 C CB  . ALA A 1 199 ? 30.897  -30.249 8.096   1.00 40.98  ? 201 ALA A CB  1 
ATOM   1576 N N   . ASP A 1 200 ? 33.109  -27.798 7.614   1.00 44.84  ? 202 ASP A N   1 
ATOM   1577 C CA  . ASP A 1 200 ? 34.476  -27.249 7.628   1.00 46.68  ? 202 ASP A CA  1 
ATOM   1578 C C   . ASP A 1 200 ? 34.569  -25.977 8.497   1.00 49.12  ? 202 ASP A C   1 
ATOM   1579 O O   . ASP A 1 200 ? 35.488  -25.869 9.312   1.00 49.86  ? 202 ASP A O   1 
ATOM   1580 C CB  . ASP A 1 200 ? 35.003  -26.935 6.204   1.00 47.34  ? 202 ASP A CB  1 
ATOM   1581 C CG  . ASP A 1 200 ? 34.968  -28.109 5.254   1.00 50.47  ? 202 ASP A CG  1 
ATOM   1582 O OD1 . ASP A 1 200 ? 34.949  -29.253 5.731   1.00 51.49  ? 202 ASP A OD1 1 
ATOM   1583 O OD2 . ASP A 1 200 ? 34.953  -27.878 4.022   1.00 52.17  ? 202 ASP A OD2 1 
ATOM   1584 N N   . THR A 1 201 ? 33.646  -25.017 8.322   1.00 49.68  ? 203 THR A N   1 
ATOM   1585 C CA  . THR A 1 201 ? 33.633  -23.821 9.155   1.00 51.71  ? 203 THR A CA  1 
ATOM   1586 C C   . THR A 1 201 ? 33.551  -24.100 10.656  1.00 53.89  ? 203 THR A C   1 
ATOM   1587 O O   . THR A 1 201 ? 34.075  -23.304 11.440  1.00 54.13  ? 203 THR A O   1 
ATOM   1588 C CB  . THR A 1 201 ? 32.507  -22.884 8.753   1.00 52.64  ? 203 THR A CB  1 
ATOM   1589 O OG1 . THR A 1 201 ? 32.554  -22.668 7.344   1.00 52.51  ? 203 THR A OG1 1 
ATOM   1590 C CG2 . THR A 1 201 ? 32.615  -21.532 9.458   1.00 54.66  ? 203 THR A CG2 1 
ATOM   1591 N N   . ALA A 1 202 ? 32.900  -25.209 11.066  1.00 55.04  ? 204 ALA A N   1 
ATOM   1592 C CA  . ALA A 1 202 ? 32.768  -25.537 12.485  1.00 56.26  ? 204 ALA A CA  1 
ATOM   1593 C C   . ALA A 1 202 ? 34.110  -25.912 13.091  1.00 57.78  ? 204 ALA A C   1 
ATOM   1594 O O   . ALA A 1 202 ? 34.353  -25.605 14.256  1.00 58.54  ? 204 ALA A O   1 
ATOM   1595 C CB  . ALA A 1 202 ? 31.773  -26.669 12.672  1.00 56.15  ? 204 ALA A CB  1 
ATOM   1596 N N   . THR A 1 203 ? 34.984  -26.561 12.313  1.00 58.49  ? 205 THR A N   1 
ATOM   1597 C CA  . THR A 1 203 ? 36.278  -26.995 12.800  1.00 59.68  ? 205 THR A CA  1 
ATOM   1598 C C   . THR A 1 203 ? 37.277  -25.890 12.554  1.00 62.00  ? 205 THR A C   1 
ATOM   1599 O O   . THR A 1 203 ? 37.504  -25.497 11.412  1.00 61.88  ? 205 THR A O   1 
ATOM   1600 C CB  . THR A 1 203 ? 36.729  -28.316 12.147  1.00 60.63  ? 205 THR A CB  1 
ATOM   1601 O OG1 . THR A 1 203 ? 37.217  -28.088 10.821  1.00 61.17  ? 205 THR A OG1 1 
ATOM   1602 C CG2 . THR A 1 203 ? 35.633  -29.374 12.128  1.00 60.87  ? 205 THR A CG2 1 
ATOM   1603 N N   . LYS A 1 204 ? 37.876  -25.382 13.626  1.00 63.90  ? 206 LYS A N   1 
ATOM   1604 C CA  . LYS A 1 204 ? 38.957  -24.411 13.509  1.00 65.04  ? 206 LYS A CA  1 
ATOM   1605 C C   . LYS A 1 204 ? 40.243  -25.205 13.261  1.00 66.03  ? 206 LYS A C   1 
ATOM   1606 O O   . LYS A 1 204 ? 40.625  -26.018 14.098  1.00 65.76  ? 206 LYS A O   1 
ATOM   1607 C CB  . LYS A 1 204 ? 39.026  -23.564 14.791  1.00 67.33  ? 206 LYS A CB  1 
ATOM   1608 C CG  . LYS A 1 204 ? 38.092  -22.334 14.835  1.00 71.50  ? 206 LYS A CG  1 
ATOM   1609 C CD  . LYS A 1 204 ? 36.633  -22.536 14.417  1.00 75.59  ? 206 LYS A CD  1 
ATOM   1610 C CE  . LYS A 1 204 ? 35.997  -21.183 14.140  1.00 81.13  ? 206 LYS A CE  1 
ATOM   1611 N NZ  . LYS A 1 204 ? 34.523  -21.260 13.872  1.00 84.92  ? 206 LYS A NZ  1 
ATOM   1612 N N   . SER A 1 205 ? 40.910  -24.972 12.108  1.00 67.02  ? 207 SER A N   1 
ATOM   1613 C CA  . SER A 1 205 ? 42.114  -25.722 11.683  1.00 67.96  ? 207 SER A CA  1 
ATOM   1614 C C   . SER A 1 205 ? 43.270  -24.832 11.217  1.00 68.24  ? 207 SER A C   1 
ATOM   1615 O O   . SER A 1 205 ? 44.196  -25.344 10.593  1.00 68.27  ? 207 SER A O   1 
ATOM   1616 C CB  . SER A 1 205 ? 41.768  -26.654 10.521  1.00 70.28  ? 207 SER A CB  1 
ATOM   1617 O OG  . SER A 1 205 ? 40.606  -27.420 10.779  1.00 74.76  ? 207 SER A OG  1 
ATOM   1618 N N   . GLY A 1 206 ? 43.227  -23.536 11.499  1.00 68.64  ? 208 GLY A N   1 
ATOM   1619 C CA  . GLY A 1 206 ? 44.248  -22.614 11.007  1.00 69.16  ? 208 GLY A CA  1 
ATOM   1620 C C   . GLY A 1 206 ? 43.704  -21.226 10.765  1.00 69.64  ? 208 GLY A C   1 
ATOM   1621 O O   . GLY A 1 206 ? 42.671  -20.856 11.337  1.00 69.03  ? 208 GLY A O   1 
ATOM   1622 N N   . SER A 1 207 ? 44.410  -20.440 9.912   1.00 70.63  ? 209 SER A N   1 
ATOM   1623 C CA  . SER A 1 207 ? 43.999  -19.068 9.540   1.00 71.51  ? 209 SER A CA  1 
ATOM   1624 C C   . SER A 1 207 ? 42.848  -19.036 8.506   1.00 72.73  ? 209 SER A C   1 
ATOM   1625 O O   . SER A 1 207 ? 42.303  -17.954 8.252   1.00 73.88  ? 209 SER A O   1 
ATOM   1626 C CB  . SER A 1 207 ? 45.186  -18.240 9.024   1.00 72.38  ? 209 SER A CB  1 
ATOM   1627 O OG  . SER A 1 207 ? 46.211  -18.975 8.368   1.00 73.70  ? 209 SER A OG  1 
ATOM   1628 N N   . THR A 1 208 ? 42.469  -20.195 7.913   1.00 72.00  ? 210 THR A N   1 
ATOM   1629 C CA  . THR A 1 208 ? 41.441  -20.240 6.865   1.00 71.42  ? 210 THR A CA  1 
ATOM   1630 C C   . THR A 1 208 ? 40.579  -21.492 6.970   1.00 70.59  ? 210 THR A C   1 
ATOM   1631 O O   . THR A 1 208 ? 41.006  -22.521 7.539   1.00 71.24  ? 210 THR A O   1 
ATOM   1632 C CB  . THR A 1 208 ? 42.095  -20.201 5.448   1.00 72.30  ? 210 THR A CB  1 
ATOM   1633 O OG1 . THR A 1 208 ? 43.209  -21.112 5.410   1.00 72.20  ? 210 THR A OG1 1 
ATOM   1634 C CG2 . THR A 1 208 ? 42.507  -18.766 5.008   1.00 72.98  ? 210 THR A CG2 1 
ATOM   1635 N N   . THR A 1 209 ? 39.352  -21.380 6.412   1.00 68.32  ? 211 THR A N   1 
ATOM   1636 C CA  . THR A 1 209 ? 38.494  -22.520 6.130   1.00 66.41  ? 211 THR A CA  1 
ATOM   1637 C C   . THR A 1 209 ? 38.621  -22.850 4.624   1.00 62.63  ? 211 THR A C   1 
ATOM   1638 O O   . THR A 1 209 ? 38.736  -21.942 3.792   1.00 62.52  ? 211 THR A O   1 
ATOM   1639 C CB  . THR A 1 209 ? 37.048  -22.180 6.510   1.00 69.23  ? 211 THR A CB  1 
ATOM   1640 O OG1 . THR A 1 209 ? 37.027  -21.734 7.875   1.00 71.38  ? 211 THR A OG1 1 
ATOM   1641 C CG2 . THR A 1 209 ? 36.102  -23.369 6.297   1.00 69.69  ? 211 THR A CG2 1 
ATOM   1642 N N   . LYS A 1 210 ? 38.632  -24.137 4.292   1.00 59.21  ? 212 LYS A N   1 
ATOM   1643 C CA  . LYS A 1 210 ? 38.546  -24.604 2.912   1.00 56.91  ? 212 LYS A CA  1 
ATOM   1644 C C   . LYS A 1 210 ? 37.201  -24.121 2.211   1.00 53.58  ? 212 LYS A C   1 
ATOM   1645 O O   . LYS A 1 210 ? 36.110  -24.208 2.764   1.00 52.88  ? 212 LYS A O   1 
ATOM   1646 C CB  . LYS A 1 210 ? 38.652  -26.154 2.892   1.00 59.45  ? 212 LYS A CB  1 
ATOM   1647 C CG  . LYS A 1 210 ? 38.797  -26.808 1.518   1.00 64.71  ? 212 LYS A CG  1 
ATOM   1648 C CD  . LYS A 1 210 ? 37.529  -27.583 1.122   1.00 69.88  ? 212 LYS A CD  1 
ATOM   1649 C CE  . LYS A 1 210 ? 37.714  -28.350 -0.175  1.00 73.52  ? 212 LYS A CE  1 
ATOM   1650 N NZ  . LYS A 1 210 ? 36.864  -29.579 -0.241  1.00 73.63  ? 212 LYS A NZ  1 
ATOM   1651 N N   . ASN A 1 211 ? 37.326  -23.599 0.996   1.00 51.25  ? 213 ASN A N   1 
ATOM   1652 C CA  . ASN A 1 211 ? 36.208  -23.331 0.116   1.00 47.75  ? 213 ASN A CA  1 
ATOM   1653 C C   . ASN A 1 211 ? 35.925  -24.560 -0.757  1.00 46.35  ? 213 ASN A C   1 
ATOM   1654 O O   . ASN A 1 211 ? 36.730  -24.884 -1.610  1.00 46.17  ? 213 ASN A O   1 
ATOM   1655 C CB  . ASN A 1 211 ? 36.559  -22.163 -0.793  1.00 46.03  ? 213 ASN A CB  1 
ATOM   1656 C CG  . ASN A 1 211 ? 36.569  -20.811 -0.129  1.00 49.41  ? 213 ASN A CG  1 
ATOM   1657 O OD1 . ASN A 1 211 ? 35.888  -20.578 0.878   1.00 50.81  ? 213 ASN A OD1 1 
ATOM   1658 N ND2 . ASN A 1 211 ? 37.275  -19.856 -0.644  1.00 49.88  ? 213 ASN A ND2 1 
ATOM   1659 N N   . ARG A 1 212 ? 34.792  -25.231 -0.568  1.00 46.37  ? 214 ARG A N   1 
ATOM   1660 C CA  . ARG A 1 212 ? 34.365  -26.299 -1.472  1.00 47.22  ? 214 ARG A CA  1 
ATOM   1661 C C   . ARG A 1 212 ? 34.131  -25.791 -2.941  1.00 47.30  ? 214 ARG A C   1 
ATOM   1662 O O   . ARG A 1 212 ? 34.411  -26.526 -3.870  1.00 48.94  ? 214 ARG A O   1 
ATOM   1663 C CB  . ARG A 1 212 ? 33.119  -27.028 -0.917  1.00 50.54  ? 214 ARG A CB  1 
ATOM   1664 C CG  . ARG A 1 212 ? 32.939  -28.448 -1.492  1.00 57.86  ? 214 ARG A CG  1 
ATOM   1665 C CD  . ARG A 1 212 ? 32.159  -29.365 -0.570  1.00 62.84  ? 214 ARG A CD  1 
ATOM   1666 N NE  . ARG A 1 212 ? 32.917  -29.692 0.641   1.00 65.77  ? 214 ARG A NE  1 
ATOM   1667 C CZ  . ARG A 1 212 ? 32.413  -30.335 1.697   1.00 66.85  ? 214 ARG A CZ  1 
ATOM   1668 N NH1 . ARG A 1 212 ? 33.176  -30.594 2.755   1.00 64.56  ? 214 ARG A NH1 1 
ATOM   1669 N NH2 . ARG A 1 212 ? 31.144  -30.723 1.704   1.00 67.82  ? 214 ARG A NH2 1 
ATOM   1670 N N   . PHE A 1 213 ? 33.649  -24.551 -3.147  1.00 45.52  ? 215 PHE A N   1 
ATOM   1671 C CA  . PHE A 1 213 ? 33.482  -23.940 -4.467  1.00 44.62  ? 215 PHE A CA  1 
ATOM   1672 C C   . PHE A 1 213 ? 33.845  -22.422 -4.411  1.00 45.06  ? 215 PHE A C   1 
ATOM   1673 O O   . PHE A 1 213 ? 33.894  -21.803 -3.333  1.00 45.10  ? 215 PHE A O   1 
ATOM   1674 C CB  . PHE A 1 213 ? 32.032  -24.132 -5.042  1.00 43.68  ? 215 PHE A CB  1 
ATOM   1675 C CG  . PHE A 1 213 ? 31.404  -25.497 -4.860  1.00 44.31  ? 215 PHE A CG  1 
ATOM   1676 C CD1 . PHE A 1 213 ? 31.794  -26.577 -5.655  1.00 45.05  ? 215 PHE A CD1 1 
ATOM   1677 C CD2 . PHE A 1 213 ? 30.468  -25.726 -3.854  1.00 44.46  ? 215 PHE A CD2 1 
ATOM   1678 C CE1 . PHE A 1 213 ? 31.230  -27.847 -5.466  1.00 45.27  ? 215 PHE A CE1 1 
ATOM   1679 C CE2 . PHE A 1 213 ? 29.903  -26.990 -3.674  1.00 44.55  ? 215 PHE A CE2 1 
ATOM   1680 C CZ  . PHE A 1 213 ? 30.274  -28.040 -4.485  1.00 44.90  ? 215 PHE A CZ  1 
ATOM   1681 N N   . VAL A 1 214 ? 34.098  -21.829 -5.595  1.00 44.92  ? 216 VAL A N   1 
ATOM   1682 C CA  . VAL A 1 214 ? 34.477  -20.408 -5.743  1.00 45.27  ? 216 VAL A CA  1 
ATOM   1683 C C   . VAL A 1 214 ? 33.852  -19.870 -7.082  1.00 44.36  ? 216 VAL A C   1 
ATOM   1684 O O   . VAL A 1 214 ? 33.821  -20.594 -8.063  1.00 45.64  ? 216 VAL A O   1 
ATOM   1685 C CB  . VAL A 1 214 ? 36.029  -20.243 -5.730  1.00 46.58  ? 216 VAL A CB  1 
ATOM   1686 C CG1 . VAL A 1 214 ? 36.458  -18.792 -5.948  1.00 47.69  ? 216 VAL A CG1 1 
ATOM   1687 C CG2 . VAL A 1 214 ? 36.627  -20.759 -4.436  1.00 47.08  ? 216 VAL A CG2 1 
ATOM   1688 N N   . VAL A 1 215 ? 33.366  -18.637 -7.109  1.00 42.35  ? 217 VAL A N   1 
ATOM   1689 C CA  . VAL A 1 215 ? 32.810  -17.987 -8.309  1.00 41.93  ? 217 VAL A CA  1 
ATOM   1690 C C   . VAL A 1 215 ? 33.265  -16.514 -8.328  1.00 42.08  ? 217 VAL A C   1 
ATOM   1691 O O   . VAL A 1 215 ? 33.240  -15.896 -9.411  1.00 42.98  ? 217 VAL A O   1 
ATOM   1692 C CB  . VAL A 1 215 ? 31.251  -18.063 -8.428  1.00 42.62  ? 217 VAL A CB  1 
ATOM   1693 C CG1 . VAL A 1 215 ? 30.757  -19.503 -8.518  1.00 44.24  ? 217 VAL A CG1 1 
ATOM   1694 C CG2 . VAL A 1 215 ? 30.555  -17.338 -7.299  1.00 41.96  ? 217 VAL A CG2 1 
ATOM   1695 O OXT . VAL A 1 215 ? 33.627  -15.968 -7.272  1.00 39.01  ? 217 VAL A OXT 1 
ATOM   1696 N N   . ALA B 1 9   ? -1.834  -13.334 8.833   1.00 60.38  ? 11  ALA B N   1 
ATOM   1697 C CA  . ALA B 1 9   ? -2.932  -14.004 9.545   1.00 60.27  ? 11  ALA B CA  1 
ATOM   1698 C C   . ALA B 1 9   ? -2.412  -14.860 10.740  1.00 59.99  ? 11  ALA B C   1 
ATOM   1699 O O   . ALA B 1 9   ? -1.326  -15.442 10.653  1.00 60.35  ? 11  ALA B O   1 
ATOM   1700 C CB  . ALA B 1 9   ? -3.710  -14.854 8.557   1.00 60.07  ? 11  ALA B CB  1 
ATOM   1701 N N   . ARG B 1 10  ? -3.179  -14.918 11.856  1.00 58.52  ? 12  ARG B N   1 
ATOM   1702 C CA  . ARG B 1 10  ? -2.708  -15.555 13.093  1.00 56.55  ? 12  ARG B CA  1 
ATOM   1703 C C   . ARG B 1 10  ? -2.722  -17.066 12.944  1.00 54.16  ? 12  ARG B C   1 
ATOM   1704 O O   . ARG B 1 10  ? -3.691  -17.622 12.436  1.00 54.54  ? 12  ARG B O   1 
ATOM   1705 C CB  . ARG B 1 10  ? -3.547  -15.148 14.334  1.00 57.38  ? 12  ARG B CB  1 
ATOM   1706 C CG  . ARG B 1 10  ? -2.943  -15.689 15.669  1.00 60.99  ? 12  ARG B CG  1 
ATOM   1707 C CD  . ARG B 1 10  ? -3.792  -15.391 16.882  1.00 64.80  ? 12  ARG B CD  1 
ATOM   1708 N NE  . ARG B 1 10  ? -4.005  -13.952 17.037  1.00 69.59  ? 12  ARG B NE  1 
ATOM   1709 C CZ  . ARG B 1 10  ? -3.292  -13.128 17.806  1.00 70.81  ? 12  ARG B CZ  1 
ATOM   1710 N NH1 . ARG B 1 10  ? -2.277  -13.592 18.536  1.00 70.51  ? 12  ARG B NH1 1 
ATOM   1711 N NH2 . ARG B 1 10  ? -3.587  -11.834 17.851  1.00 69.36  ? 12  ARG B NH2 1 
ATOM   1712 N N   . ILE B 1 11  ? -1.654  -17.725 13.388  1.00 51.30  ? 13  ILE B N   1 
ATOM   1713 C CA  . ILE B 1 11  ? -1.572  -19.186 13.343  1.00 49.41  ? 13  ILE B CA  1 
ATOM   1714 C C   . ILE B 1 11  ? -2.213  -19.782 14.612  1.00 47.21  ? 13  ILE B C   1 
ATOM   1715 O O   . ILE B 1 11  ? -1.706  -19.621 15.733  1.00 45.77  ? 13  ILE B O   1 
ATOM   1716 C CB  . ILE B 1 11  ? -0.127  -19.664 13.182  1.00 49.50  ? 13  ILE B CB  1 
ATOM   1717 C CG1 . ILE B 1 11  ? 0.595   -18.899 12.039  1.00 51.00  ? 13  ILE B CG1 1 
ATOM   1718 C CG2 . ILE B 1 11  ? -0.091  -21.152 12.941  1.00 49.68  ? 13  ILE B CG2 1 
ATOM   1719 C CD1 . ILE B 1 11  ? 2.011   -19.370 11.793  1.00 52.84  ? 13  ILE B CD1 1 
ATOM   1720 N N   . ILE B 1 12  ? -3.329  -20.474 14.417  1.00 46.40  ? 14  ILE B N   1 
ATOM   1721 C CA  . ILE B 1 12  ? -4.112  -21.006 15.507  1.00 46.69  ? 14  ILE B CA  1 
ATOM   1722 C C   . ILE B 1 12  ? -4.257  -22.494 15.293  1.00 46.37  ? 14  ILE B C   1 
ATOM   1723 O O   . ILE B 1 12  ? -4.667  -22.936 14.221  1.00 46.64  ? 14  ILE B O   1 
ATOM   1724 C CB  . ILE B 1 12  ? -5.485  -20.294 15.559  1.00 47.47  ? 14  ILE B CB  1 
ATOM   1725 C CG1 . ILE B 1 12  ? -5.297  -18.743 15.628  1.00 47.98  ? 14  ILE B CG1 1 
ATOM   1726 C CG2 . ILE B 1 12  ? -6.341  -20.862 16.716  1.00 48.08  ? 14  ILE B CG2 1 
ATOM   1727 C CD1 . ILE B 1 12  ? -6.480  -18.010 15.723  1.00 50.13  ? 14  ILE B CD1 1 
ATOM   1728 N N   . TYR B 1 13  ? -3.925  -23.271 16.315  1.00 45.62  ? 15  TYR B N   1 
ATOM   1729 C CA  . TYR B 1 13  ? -4.139  -24.705 16.303  1.00 44.90  ? 15  TYR B CA  1 
ATOM   1730 C C   . TYR B 1 13  ? -5.091  -25.079 17.397  1.00 46.08  ? 15  TYR B C   1 
ATOM   1731 O O   . TYR B 1 13  ? -4.867  -24.713 18.555  1.00 47.37  ? 15  TYR B O   1 
ATOM   1732 C CB  . TYR B 1 13  ? -2.849  -25.426 16.554  1.00 43.89  ? 15  TYR B CB  1 
ATOM   1733 C CG  . TYR B 1 13  ? -1.804  -25.144 15.518  1.00 43.39  ? 15  TYR B CG  1 
ATOM   1734 C CD1 . TYR B 1 13  ? -1.890  -25.703 14.251  1.00 44.69  ? 15  TYR B CD1 1 
ATOM   1735 C CD2 . TYR B 1 13  ? -0.717  -24.350 15.805  1.00 44.14  ? 15  TYR B CD2 1 
ATOM   1736 C CE1 . TYR B 1 13  ? -0.909  -25.491 13.299  1.00 45.07  ? 15  TYR B CE1 1 
ATOM   1737 C CE2 . TYR B 1 13  ? 0.261   -24.109 14.855  1.00 45.58  ? 15  TYR B CE2 1 
ATOM   1738 C CZ  . TYR B 1 13  ? 0.163   -24.691 13.599  1.00 46.52  ? 15  TYR B CZ  1 
ATOM   1739 O OH  . TYR B 1 13  ? 1.102   -24.470 12.633  1.00 48.06  ? 15  TYR B OH  1 
ATOM   1740 N N   . ASP B 1 14  ? -6.168  -25.788 17.048  1.00 45.34  ? 16  ASP B N   1 
ATOM   1741 C CA  . ASP B 1 14  ? -7.004  -26.381 18.071  1.00 44.93  ? 16  ASP B CA  1 
ATOM   1742 C C   . ASP B 1 14  ? -6.294  -27.600 18.696  1.00 44.18  ? 16  ASP B C   1 
ATOM   1743 O O   . ASP B 1 14  ? -5.270  -28.096 18.207  1.00 42.91  ? 16  ASP B O   1 
ATOM   1744 C CB  . ASP B 1 14  ? -8.444  -26.702 17.579  1.00 45.96  ? 16  ASP B CB  1 
ATOM   1745 C CG  . ASP B 1 14  ? -8.546  -27.760 16.526  1.00 49.47  ? 16  ASP B CG  1 
ATOM   1746 O OD1 . ASP B 1 14  ? -7.620  -28.598 16.431  1.00 50.45  ? 16  ASP B OD1 1 
ATOM   1747 O OD2 . ASP B 1 14  ? -9.550  -27.759 15.791  1.00 51.67  ? 16  ASP B OD2 1 
ATOM   1748 N N   . ARG B 1 15  ? -6.865  -28.067 19.792  1.00 44.21  ? 17  ARG B N   1 
ATOM   1749 C CA  . ARG B 1 15  ? -6.350  -29.190 20.539  1.00 44.73  ? 17  ARG B CA  1 
ATOM   1750 C C   . ARG B 1 15  ? -6.183  -30.434 19.678  1.00 45.54  ? 17  ARG B C   1 
ATOM   1751 O O   . ARG B 1 15  ? -5.134  -31.061 19.737  1.00 45.67  ? 17  ARG B O   1 
ATOM   1752 C CB  . ARG B 1 15  ? -7.282  -29.485 21.711  1.00 45.58  ? 17  ARG B CB  1 
ATOM   1753 C CG  . ARG B 1 15  ? -6.729  -30.529 22.634  1.00 48.40  ? 17  ARG B CG  1 
ATOM   1754 C CD  . ARG B 1 15  ? -7.707  -30.740 23.765  1.00 51.33  ? 17  ARG B CD  1 
ATOM   1755 N NE  . ARG B 1 15  ? -7.268  -31.790 24.671  1.00 57.66  ? 17  ARG B NE  1 
ATOM   1756 C CZ  . ARG B 1 15  ? -7.362  -33.101 24.434  1.00 63.53  ? 17  ARG B CZ  1 
ATOM   1757 N NH1 . ARG B 1 15  ? -7.876  -33.545 23.290  1.00 64.62  ? 17  ARG B NH1 1 
ATOM   1758 N NH2 . ARG B 1 15  ? -6.938  -33.975 25.334  1.00 64.82  ? 17  ARG B NH2 1 
ATOM   1759 N N   . ALA B 1 16  ? -7.205  -30.776 18.868  1.00 46.10  ? 18  ALA B N   1 
ATOM   1760 C CA  . ALA B 1 16  ? -7.166  -31.962 18.030  1.00 46.82  ? 18  ALA B CA  1 
ATOM   1761 C C   . ALA B 1 16  ? -6.022  -31.954 17.037  1.00 47.80  ? 18  ALA B C   1 
ATOM   1762 O O   . ALA B 1 16  ? -5.389  -32.991 16.845  1.00 48.46  ? 18  ALA B O   1 
ATOM   1763 C CB  . ALA B 1 16  ? -8.472  -32.112 17.284  1.00 47.41  ? 18  ALA B CB  1 
ATOM   1764 N N   . PHE B 1 17  ? -5.750  -30.810 16.392  1.00 47.85  ? 19  PHE B N   1 
ATOM   1765 C CA  . PHE B 1 17  ? -4.661  -30.725 15.433  1.00 48.94  ? 19  PHE B CA  1 
ATOM   1766 C C   . PHE B 1 17  ? -3.304  -30.938 16.118  1.00 47.62  ? 19  PHE B C   1 
ATOM   1767 O O   . PHE B 1 17  ? -2.478  -31.670 15.600  1.00 46.64  ? 19  PHE B O   1 
ATOM   1768 C CB  . PHE B 1 17  ? -4.717  -29.379 14.698  1.00 50.59  ? 19  PHE B CB  1 
ATOM   1769 C CG  . PHE B 1 17  ? -3.767  -29.340 13.534  1.00 52.88  ? 19  PHE B CG  1 
ATOM   1770 C CD1 . PHE B 1 17  ? -2.460  -28.930 13.703  1.00 54.25  ? 19  PHE B CD1 1 
ATOM   1771 C CD2 . PHE B 1 17  ? -4.159  -29.785 12.287  1.00 54.75  ? 19  PHE B CD2 1 
ATOM   1772 C CE1 . PHE B 1 17  ? -1.572  -28.938 12.646  1.00 55.09  ? 19  PHE B CE1 1 
ATOM   1773 C CE2 . PHE B 1 17  ? -3.268  -29.790 11.228  1.00 55.86  ? 19  PHE B CE2 1 
ATOM   1774 C CZ  . PHE B 1 17  ? -1.980  -29.351 11.418  1.00 55.67  ? 19  PHE B CZ  1 
ATOM   1775 N N   . LEU B 1 18  ? -3.074  -30.303 17.287  1.00 47.20  ? 20  LEU B N   1 
ATOM   1776 C CA  . LEU B 1 18  ? -1.802  -30.449 17.998  1.00 46.53  ? 20  LEU B CA  1 
ATOM   1777 C C   . LEU B 1 18  ? -1.566  -31.887 18.448  1.00 47.35  ? 20  LEU B C   1 
ATOM   1778 O O   . LEU B 1 18  ? -0.438  -32.369 18.356  1.00 48.36  ? 20  LEU B O   1 
ATOM   1779 C CB  . LEU B 1 18  ? -1.719  -29.486 19.207  1.00 45.30  ? 20  LEU B CB  1 
ATOM   1780 C CG  . LEU B 1 18  ? -1.741  -27.972 18.894  1.00 44.40  ? 20  LEU B CG  1 
ATOM   1781 C CD1 . LEU B 1 18  ? -1.834  -27.134 20.159  1.00 42.40  ? 20  LEU B CD1 1 
ATOM   1782 C CD2 . LEU B 1 18  ? -0.557  -27.573 18.107  1.00 45.35  ? 20  LEU B CD2 1 
ATOM   1783 N N   . MET B 1 19  ? -2.597  -32.567 18.930  1.00 46.72  ? 21  MET B N   1 
ATOM   1784 C CA  . MET B 1 19  ? -2.471  -33.979 19.309  1.00 47.56  ? 21  MET B CA  1 
ATOM   1785 C C   . MET B 1 19  ? -2.154  -34.893 18.122  1.00 49.87  ? 21  MET B C   1 
ATOM   1786 O O   . MET B 1 19  ? -1.340  -35.783 18.256  1.00 50.51  ? 21  MET B O   1 
ATOM   1787 C CB  . MET B 1 19  ? -3.746  -34.465 19.970  1.00 46.76  ? 21  MET B CB  1 
ATOM   1788 C CG  . MET B 1 19  ? -4.061  -33.818 21.250  1.00 47.68  ? 21  MET B CG  1 
ATOM   1789 S SD  . MET B 1 19  ? -2.773  -33.973 22.496  1.00 47.21  ? 21  MET B SD  1 
ATOM   1790 C CE  . MET B 1 19  ? -3.766  -33.664 23.944  1.00 52.76  ? 21  MET B CE  1 
ATOM   1791 N N   . ALA B 1 20  ? -2.800  -34.686 16.973  1.00 51.31  ? 22  ALA B N   1 
ATOM   1792 C CA  . ALA B 1 20  ? -2.502  -35.419 15.744  1.00 52.86  ? 22  ALA B CA  1 
ATOM   1793 C C   . ALA B 1 20  ? -1.022  -35.309 15.340  1.00 55.31  ? 22  ALA B C   1 
ATOM   1794 O O   . ALA B 1 20  ? -0.465  -36.305 14.863  1.00 56.46  ? 22  ALA B O   1 
ATOM   1795 C CB  . ALA B 1 20  ? -3.390  -34.912 14.620  1.00 52.63  ? 22  ALA B CB  1 
ATOM   1796 N N   . CYS B 1 21  ? -0.382  -34.131 15.537  1.00 55.70  ? 23  CYS B N   1 
ATOM   1797 C CA  . CYS B 1 21  ? 1.045   -33.924 15.245  1.00 56.85  ? 23  CYS B CA  1 
ATOM   1798 C C   . CYS B 1 21  ? 2.037   -34.627 16.230  1.00 57.25  ? 23  CYS B C   1 
ATOM   1799 O O   . CYS B 1 21  ? 3.239   -34.603 15.992  1.00 57.10  ? 23  CYS B O   1 
ATOM   1800 C CB  . CYS B 1 21  ? 1.332   -32.431 15.162  1.00 58.42  ? 23  CYS B CB  1 
ATOM   1801 S SG  . CYS B 1 21  ? 0.322   -31.527 13.949  1.00 62.93  ? 23  CYS B SG  1 
ATOM   1802 N N   . ARG B 1 22  ? 1.552   -35.237 17.313  1.00 57.95  ? 24  ARG B N   1 
ATOM   1803 C CA  . ARG B 1 22  ? 2.388   -35.908 18.320  1.00 59.53  ? 24  ARG B CA  1 
ATOM   1804 C C   . ARG B 1 22  ? 2.717   -37.333 17.875  1.00 63.68  ? 24  ARG B C   1 
ATOM   1805 O O   . ARG B 1 22  ? 1.836   -38.012 17.340  1.00 64.87  ? 24  ARG B O   1 
ATOM   1806 C CB  . ARG B 1 22  ? 1.606   -35.963 19.634  1.00 58.32  ? 24  ARG B CB  1 
ATOM   1807 C CG  . ARG B 1 22  ? 2.212   -36.760 20.753  1.00 58.28  ? 24  ARG B CG  1 
ATOM   1808 C CD  . ARG B 1 22  ? 1.150   -36.888 21.814  1.00 58.88  ? 24  ARG B CD  1 
ATOM   1809 N NE  . ARG B 1 22  ? 1.751   -37.044 23.127  1.00 59.58  ? 24  ARG B NE  1 
ATOM   1810 C CZ  . ARG B 1 22  ? 1.166   -36.735 24.278  1.00 61.65  ? 24  ARG B CZ  1 
ATOM   1811 N NH1 . ARG B 1 22  ? -0.070  -36.242 24.297  1.00 61.89  ? 24  ARG B NH1 1 
ATOM   1812 N NH2 . ARG B 1 22  ? 1.813   -36.915 25.425  1.00 61.80  ? 24  ARG B NH2 1 
ATOM   1813 N N   . GLY B 1 23  ? 3.949   -37.790 18.118  1.00 65.11  ? 25  GLY B N   1 
ATOM   1814 C CA  . GLY B 1 23  ? 4.351   -39.152 17.754  1.00 66.54  ? 25  GLY B CA  1 
ATOM   1815 C C   . GLY B 1 23  ? 3.739   -40.229 18.632  1.00 68.13  ? 25  GLY B C   1 
ATOM   1816 O O   . GLY B 1 23  ? 3.517   -40.043 19.840  1.00 68.92  ? 25  GLY B O   1 
ATOM   1817 N N   . LYS B 1 34  ? 7.179   -29.123 8.795   1.00 61.71  ? 36  LYS B N   1 
ATOM   1818 C CA  . LYS B 1 34  ? 6.865   -28.772 10.187  1.00 61.40  ? 36  LYS B CA  1 
ATOM   1819 C C   . LYS B 1 34  ? 5.857   -27.640 10.260  1.00 59.48  ? 36  LYS B C   1 
ATOM   1820 O O   . LYS B 1 34  ? 5.814   -26.797 9.357   1.00 59.81  ? 36  LYS B O   1 
ATOM   1821 C CB  . LYS B 1 34  ? 8.137   -28.384 10.969  1.00 63.71  ? 36  LYS B CB  1 
ATOM   1822 C CG  . LYS B 1 34  ? 8.966   -29.570 11.424  1.00 69.89  ? 36  LYS B CG  1 
ATOM   1823 C CD  . LYS B 1 34  ? 10.257  -29.129 12.097  1.00 75.27  ? 36  LYS B CD  1 
ATOM   1824 C CE  . LYS B 1 34  ? 10.965  -30.301 12.752  1.00 80.75  ? 36  LYS B CE  1 
ATOM   1825 N NZ  . LYS B 1 34  ? 12.303  -29.915 13.280  1.00 84.31  ? 36  LYS B NZ  1 
ATOM   1826 N N   . HIS B 1 35  ? 5.050   -27.624 11.339  1.00 58.32  ? 37  HIS B N   1 
ATOM   1827 C CA  . HIS B 1 35  ? 3.931   -26.691 11.512  1.00 57.73  ? 37  HIS B CA  1 
ATOM   1828 C C   . HIS B 1 35  ? 4.328   -25.522 12.378  1.00 56.58  ? 37  HIS B C   1 
ATOM   1829 O O   . HIS B 1 35  ? 4.464   -25.682 13.597  1.00 56.62  ? 37  HIS B O   1 
ATOM   1830 C CB  . HIS B 1 35  ? 2.722   -27.407 12.108  1.00 58.99  ? 37  HIS B CB  1 
ATOM   1831 C CG  . HIS B 1 35  ? 2.118   -28.365 11.131  1.00 62.86  ? 37  HIS B CG  1 
ATOM   1832 N ND1 . HIS B 1 35  ? 2.540   -29.675 11.054  1.00 65.48  ? 37  HIS B ND1 1 
ATOM   1833 C CD2 . HIS B 1 35  ? 1.163   -28.160 10.196  1.00 64.30  ? 37  HIS B CD2 1 
ATOM   1834 C CE1 . HIS B 1 35  ? 1.824   -30.230 10.095  1.00 65.83  ? 37  HIS B CE1 1 
ATOM   1835 N NE2 . HIS B 1 35  ? 0.988   -29.353 9.544   1.00 65.71  ? 37  HIS B NE2 1 
ATOM   1836 N N   . PRO B 1 36  ? 4.506   -24.331 11.783  1.00 54.69  ? 38  PRO B N   1 
ATOM   1837 C CA  . PRO B 1 36  ? 5.011   -23.203 12.563  1.00 52.40  ? 38  PRO B CA  1 
ATOM   1838 C C   . PRO B 1 36  ? 4.053   -22.700 13.616  1.00 49.84  ? 38  PRO B C   1 
ATOM   1839 O O   . PRO B 1 36  ? 2.843   -22.653 13.401  1.00 50.21  ? 38  PRO B O   1 
ATOM   1840 C CB  . PRO B 1 36  ? 5.221   -22.103 11.524  1.00 54.05  ? 38  PRO B CB  1 
ATOM   1841 C CG  . PRO B 1 36  ? 4.354   -22.466 10.388  1.00 55.07  ? 38  PRO B CG  1 
ATOM   1842 C CD  . PRO B 1 36  ? 4.241   -23.951 10.381  1.00 54.59  ? 38  PRO B CD  1 
ATOM   1843 N N   . LEU B 1 37  ? 4.607   -22.316 14.769  1.00 46.71  ? 39  LEU B N   1 
ATOM   1844 C CA  . LEU B 1 37  ? 3.841   -21.652 15.809  1.00 43.70  ? 39  LEU B CA  1 
ATOM   1845 C C   . LEU B 1 37  ? 3.786   -20.134 15.536  1.00 43.16  ? 39  LEU B C   1 
ATOM   1846 O O   . LEU B 1 37  ? 4.666   -19.588 14.885  1.00 43.78  ? 39  LEU B O   1 
ATOM   1847 C CB  . LEU B 1 37  ? 4.469   -21.961 17.174  1.00 41.71  ? 39  LEU B CB  1 
ATOM   1848 C CG  . LEU B 1 37  ? 4.486   -23.433 17.576  1.00 40.20  ? 39  LEU B CG  1 
ATOM   1849 C CD1 . LEU B 1 37  ? 5.197   -23.655 18.946  1.00 40.50  ? 39  LEU B CD1 1 
ATOM   1850 C CD2 . LEU B 1 37  ? 3.075   -24.026 17.614  1.00 39.75  ? 39  LEU B CD2 1 
ATOM   1851 N N   . GLN B 1 38  ? 2.742   -19.470 16.019  1.00 41.65  ? 40  GLN B N   1 
ATOM   1852 C CA  . GLN B 1 38  ? 2.616   -18.016 15.970  1.00 40.48  ? 40  GLN B CA  1 
ATOM   1853 C C   . GLN B 1 38  ? 3.760   -17.343 16.681  1.00 39.46  ? 40  GLN B C   1 
ATOM   1854 O O   . GLN B 1 38  ? 4.249   -16.330 16.217  1.00 40.67  ? 40  GLN B O   1 
ATOM   1855 C CB  . GLN B 1 38  ? 1.296   -17.599 16.627  1.00 42.83  ? 40  GLN B CB  1 
ATOM   1856 C CG  . GLN B 1 38  ? 1.042   -16.097 16.685  1.00 46.48  ? 40  GLN B CG  1 
ATOM   1857 C CD  . GLN B 1 38  ? 0.740   -15.520 15.340  1.00 50.89  ? 40  GLN B CD  1 
ATOM   1858 O OE1 . GLN B 1 38  ? 0.530   -16.230 14.330  1.00 50.48  ? 40  GLN B OE1 1 
ATOM   1859 N NE2 . GLN B 1 38  ? 0.719   -14.190 15.304  1.00 50.96  ? 40  GLN B NE2 1 
ATOM   1860 N N   . ASN B 1 39  ? 4.193   -17.912 17.800  1.00 37.41  ? 41  ASN B N   1 
ATOM   1861 C CA  . ASN B 1 39  ? 5.288   -17.402 18.593  1.00 35.02  ? 41  ASN B CA  1 
ATOM   1862 C C   . ASN B 1 39  ? 6.376   -18.467 18.823  1.00 33.41  ? 41  ASN B C   1 
ATOM   1863 O O   . ASN B 1 39  ? 6.117   -19.668 18.784  1.00 33.40  ? 41  ASN B O   1 
ATOM   1864 C CB  . ASN B 1 39  ? 4.732   -16.993 19.926  1.00 35.51  ? 41  ASN B CB  1 
ATOM   1865 C CG  . ASN B 1 39  ? 4.062   -15.654 19.917  1.00 38.51  ? 41  ASN B CG  1 
ATOM   1866 O OD1 . ASN B 1 39  ? 4.715   -14.643 19.727  1.00 40.86  ? 41  ASN B OD1 1 
ATOM   1867 N ND2 . ASN B 1 39  ? 2.762   -15.604 20.112  1.00 38.79  ? 41  ASN B ND2 1 
ATOM   1868 N N   . ARG B 1 40  ? 7.598   -18.002 19.052  1.00 31.70  ? 42  ARG B N   1 
ATOM   1869 C CA  A ARG B 1 40  ? 8.657   -18.827 19.623  0.50 31.43  ? 42  ARG B CA  1 
ATOM   1870 C CA  B ARG B 1 40  ? 8.638   -18.849 19.618  0.50 31.82  ? 42  ARG B CA  1 
ATOM   1871 C C   . ARG B 1 40  ? 8.519   -18.820 21.141  1.00 30.38  ? 42  ARG B C   1 
ATOM   1872 O O   . ARG B 1 40  ? 8.193   -17.778 21.720  1.00 30.13  ? 42  ARG B O   1 
ATOM   1873 C CB  A ARG B 1 40  ? 10.014  -18.269 19.200  0.50 32.29  ? 42  ARG B CB  1 
ATOM   1874 C CB  B ARG B 1 40  ? 10.006  -18.365 19.157  0.50 33.76  ? 42  ARG B CB  1 
ATOM   1875 C CG  A ARG B 1 40  ? 11.209  -19.102 19.624  0.50 32.78  ? 42  ARG B CG  1 
ATOM   1876 C CG  B ARG B 1 40  ? 11.149  -19.278 19.536  0.50 36.47  ? 42  ARG B CG  1 
ATOM   1877 C CD  A ARG B 1 40  ? 12.262  -18.949 18.537  0.50 32.72  ? 42  ARG B CD  1 
ATOM   1878 C CD  B ARG B 1 40  ? 12.255  -19.085 18.514  0.50 39.21  ? 42  ARG B CD  1 
ATOM   1879 N NE  A ARG B 1 40  ? 13.499  -19.692 18.805  0.50 30.94  ? 42  ARG B NE  1 
ATOM   1880 N NE  B ARG B 1 40  ? 13.496  -19.763 18.898  0.50 40.55  ? 42  ARG B NE  1 
ATOM   1881 C CZ  A ARG B 1 40  ? 14.606  -19.211 19.370  0.50 26.45  ? 42  ARG B CZ  1 
ATOM   1882 C CZ  B ARG B 1 40  ? 13.860  -21.003 18.567  0.50 39.70  ? 42  ARG B CZ  1 
ATOM   1883 N NH1 A ARG B 1 40  ? 14.677  -17.938 19.744  0.50 20.53  ? 42  ARG B NH1 1 
ATOM   1884 N NH1 B ARG B 1 40  ? 13.067  -21.767 17.808  0.50 35.12  ? 42  ARG B NH1 1 
ATOM   1885 N NH2 A ARG B 1 40  ? 15.656  -19.991 19.542  0.50 26.16  ? 42  ARG B NH2 1 
ATOM   1886 N NH2 B ARG B 1 40  ? 15.018  -21.493 18.991  0.50 40.74  ? 42  ARG B NH2 1 
ATOM   1887 N N   . TRP B 1 41  ? 8.757   -19.964 21.779  1.00 28.92  ? 43  TRP B N   1 
ATOM   1888 C CA  . TRP B 1 41  ? 8.569   -20.162 23.217  1.00 28.53  ? 43  TRP B CA  1 
ATOM   1889 C C   . TRP B 1 41  ? 9.881   -20.648 23.845  1.00 30.27  ? 43  TRP B C   1 
ATOM   1890 O O   . TRP B 1 41  ? 10.661  -21.339 23.210  1.00 29.95  ? 43  TRP B O   1 
ATOM   1891 C CB  . TRP B 1 41  ? 7.396   -21.156 23.494  1.00 26.80  ? 43  TRP B CB  1 
ATOM   1892 C CG  . TRP B 1 41  ? 6.080   -20.683 22.979  1.00 26.27  ? 43  TRP B CG  1 
ATOM   1893 C CD1 . TRP B 1 41  ? 5.589   -20.864 21.730  1.00 27.52  ? 43  TRP B CD1 1 
ATOM   1894 C CD2 . TRP B 1 41  ? 5.112   -19.867 23.676  1.00 26.36  ? 43  TRP B CD2 1 
ATOM   1895 N NE1 . TRP B 1 41  ? 4.386   -20.193 21.586  1.00 27.44  ? 43  TRP B NE1 1 
ATOM   1896 C CE2 . TRP B 1 41  ? 4.064   -19.599 22.776  1.00 27.11  ? 43  TRP B CE2 1 
ATOM   1897 C CE3 . TRP B 1 41  ? 5.000   -19.393 24.999  1.00 26.32  ? 43  TRP B CE3 1 
ATOM   1898 C CZ2 . TRP B 1 41  ? 2.943   -18.834 23.138  1.00 28.54  ? 43  TRP B CZ2 1 
ATOM   1899 C CZ3 . TRP B 1 41  ? 3.901   -18.648 25.347  1.00 27.13  ? 43  TRP B CZ3 1 
ATOM   1900 C CH2 . TRP B 1 41  ? 2.889   -18.361 24.419  1.00 27.75  ? 43  TRP B CH2 1 
ATOM   1901 N N   . ALA B 1 42  ? 10.124  -20.272 25.107  1.00 31.97  ? 44  ALA B N   1 
ATOM   1902 C CA  . ALA B 1 42  ? 11.308  -20.678 25.849  1.00 33.59  ? 44  ALA B CA  1 
ATOM   1903 C C   . ALA B 1 42  ? 10.875  -21.389 27.118  1.00 34.00  ? 44  ALA B C   1 
ATOM   1904 O O   . ALA B 1 42  ? 10.078  -20.849 27.864  1.00 33.82  ? 44  ALA B O   1 
ATOM   1905 C CB  . ALA B 1 42  ? 12.140  -19.450 26.183  1.00 34.41  ? 44  ALA B CB  1 
ATOM   1906 N N   . LEU B 1 43  ? 11.386  -22.606 27.345  1.00 34.65  ? 45  LEU B N   1 
ATOM   1907 C CA  . LEU B 1 43  ? 11.153  -23.400 28.523  1.00 35.42  ? 45  LEU B CA  1 
ATOM   1908 C C   . LEU B 1 43  ? 12.252  -23.130 29.520  1.00 37.63  ? 45  LEU B C   1 
ATOM   1909 O O   . LEU B 1 43  ? 13.421  -23.255 29.191  1.00 37.90  ? 45  LEU B O   1 
ATOM   1910 C CB  . LEU B 1 43  ? 11.135  -24.895 28.186  1.00 34.97  ? 45  LEU B CB  1 
ATOM   1911 C CG  . LEU B 1 43  ? 11.013  -25.858 29.390  1.00 33.85  ? 45  LEU B CG  1 
ATOM   1912 C CD1 . LEU B 1 43  ? 9.750   -25.613 30.154  1.00 33.73  ? 45  LEU B CD1 1 
ATOM   1913 C CD2 . LEU B 1 43  ? 11.166  -27.286 28.921  1.00 34.69  ? 45  LEU B CD2 1 
ATOM   1914 N N   . TRP B 1 44  ? 11.853  -22.763 30.733  1.00 39.54  ? 46  TRP B N   1 
ATOM   1915 C CA  . TRP B 1 44  ? 12.700  -22.411 31.849  1.00 41.75  ? 46  TRP B CA  1 
ATOM   1916 C C   . TRP B 1 44  ? 12.465  -23.352 33.015  1.00 45.21  ? 46  TRP B C   1 
ATOM   1917 O O   . TRP B 1 44  ? 11.366  -23.853 33.215  1.00 43.92  ? 46  TRP B O   1 
ATOM   1918 C CB  . TRP B 1 44  ? 12.394  -20.996 32.333  1.00 41.37  ? 46  TRP B CB  1 
ATOM   1919 C CG  . TRP B 1 44  ? 12.427  -19.942 31.279  1.00 42.25  ? 46  TRP B CG  1 
ATOM   1920 C CD1 . TRP B 1 44  ? 11.446  -19.635 30.383  1.00 43.27  ? 46  TRP B CD1 1 
ATOM   1921 C CD2 . TRP B 1 44  ? 13.506  -19.047 31.015  1.00 43.02  ? 46  TRP B CD2 1 
ATOM   1922 N NE1 . TRP B 1 44  ? 11.861  -18.615 29.558  1.00 43.60  ? 46  TRP B NE1 1 
ATOM   1923 C CE2 . TRP B 1 44  ? 13.117  -18.223 29.935  1.00 43.64  ? 46  TRP B CE2 1 
ATOM   1924 C CE3 . TRP B 1 44  ? 14.762  -18.845 31.601  1.00 44.45  ? 46  TRP B CE3 1 
ATOM   1925 C CZ2 . TRP B 1 44  ? 13.935  -17.211 29.430  1.00 45.10  ? 46  TRP B CZ2 1 
ATOM   1926 C CZ3 . TRP B 1 44  ? 15.587  -17.858 31.077  1.00 46.35  ? 46  TRP B CZ3 1 
ATOM   1927 C CH2 . TRP B 1 44  ? 15.162  -17.040 30.020  1.00 46.23  ? 46  TRP B CH2 1 
ATOM   1928 N N   . PHE B 1 45  ? 13.523  -23.576 33.791  1.00 49.27  ? 47  PHE B N   1 
ATOM   1929 C CA  . PHE B 1 45  ? 13.539  -24.356 35.023  1.00 53.29  ? 47  PHE B CA  1 
ATOM   1930 C C   . PHE B 1 45  ? 14.079  -23.445 36.098  1.00 56.49  ? 47  PHE B C   1 
ATOM   1931 O O   . PHE B 1 45  ? 15.035  -22.697 35.846  1.00 55.20  ? 47  PHE B O   1 
ATOM   1932 C CB  . PHE B 1 45  ? 14.460  -25.560 34.851  1.00 55.14  ? 47  PHE B CB  1 
ATOM   1933 C CG  . PHE B 1 45  ? 14.571  -26.457 36.054  1.00 57.89  ? 47  PHE B CG  1 
ATOM   1934 C CD1 . PHE B 1 45  ? 13.478  -27.174 36.504  1.00 60.13  ? 47  PHE B CD1 1 
ATOM   1935 C CD2 . PHE B 1 45  ? 15.772  -26.604 36.724  1.00 59.41  ? 47  PHE B CD2 1 
ATOM   1936 C CE1 . PHE B 1 45  ? 13.575  -28.009 37.618  1.00 61.00  ? 47  PHE B CE1 1 
ATOM   1937 C CE2 . PHE B 1 45  ? 15.869  -27.447 37.834  1.00 60.69  ? 47  PHE B CE2 1 
ATOM   1938 C CZ  . PHE B 1 45  ? 14.768  -28.137 38.279  1.00 60.79  ? 47  PHE B CZ  1 
ATOM   1939 N N   . PHE B 1 46  ? 13.480  -23.502 37.295  1.00 60.87  ? 48  PHE B N   1 
ATOM   1940 C CA  . PHE B 1 46  ? 13.912  -22.701 38.442  1.00 66.54  ? 48  PHE B CA  1 
ATOM   1941 C C   . PHE B 1 46  ? 13.769  -23.486 39.749  1.00 71.04  ? 48  PHE B C   1 
ATOM   1942 O O   . PHE B 1 46  ? 12.648  -23.787 40.155  1.00 71.00  ? 48  PHE B O   1 
ATOM   1943 C CB  . PHE B 1 46  ? 13.067  -21.427 38.523  1.00 67.90  ? 48  PHE B CB  1 
ATOM   1944 C CG  . PHE B 1 46  ? 13.488  -20.434 39.576  1.00 70.90  ? 48  PHE B CG  1 
ATOM   1945 C CD1 . PHE B 1 46  ? 12.918  -20.452 40.842  1.00 73.29  ? 48  PHE B CD1 1 
ATOM   1946 C CD2 . PHE B 1 46  ? 14.407  -19.449 39.285  1.00 72.39  ? 48  PHE B CD2 1 
ATOM   1947 C CE1 . PHE B 1 46  ? 13.286  -19.507 41.803  1.00 74.49  ? 48  PHE B CE1 1 
ATOM   1948 C CE2 . PHE B 1 46  ? 14.787  -18.515 40.244  1.00 73.84  ? 48  PHE B CE2 1 
ATOM   1949 C CZ  . PHE B 1 46  ? 14.217  -18.543 41.495  1.00 74.10  ? 48  PHE B CZ  1 
ATOM   1950 N N   . LYS B 1 47  ? 14.893  -23.815 40.413  1.00 74.73  ? 49  LYS B N   1 
ATOM   1951 C CA  . LYS B 1 47  ? 14.867  -24.398 41.777  1.00 78.23  ? 49  LYS B CA  1 
ATOM   1952 C C   . LYS B 1 47  ? 15.017  -23.281 42.843  1.00 81.64  ? 49  LYS B C   1 
ATOM   1953 O O   . LYS B 1 47  ? 15.849  -22.403 42.656  1.00 81.89  ? 49  LYS B O   1 
ATOM   1954 C CB  . LYS B 1 47  ? 15.992  -25.424 41.916  1.00 79.55  ? 49  LYS B CB  1 
ATOM   1955 C CG  . LYS B 1 47  ? 15.953  -26.219 43.213  1.00 85.02  ? 49  LYS B CG  1 
ATOM   1956 C CD  . LYS B 1 47  ? 16.822  -27.519 43.145  1.00 89.91  ? 49  LYS B CD  1 
ATOM   1957 C CE  . LYS B 1 47  ? 18.332  -27.306 43.164  1.00 92.85  ? 49  LYS B CE  1 
ATOM   1958 N NZ  . LYS B 1 47  ? 18.889  -27.193 44.549  1.00 94.17  ? 49  LYS B NZ  1 
ATOM   1959 N N   . ASN B 1 48  ? 14.222  -23.296 43.946  1.00 83.82  ? 50  ASN B N   1 
ATOM   1960 C CA  . ASN B 1 48  ? 14.431  -22.338 45.054  1.00 85.99  ? 50  ASN B CA  1 
ATOM   1961 C C   . ASN B 1 48  ? 15.693  -22.702 45.879  1.00 87.63  ? 50  ASN B C   1 
ATOM   1962 O O   . ASN B 1 48  ? 15.600  -23.513 46.800  1.00 87.90  ? 50  ASN B O   1 
ATOM   1963 C CB  . ASN B 1 48  ? 13.196  -22.257 45.997  1.00 87.11  ? 50  ASN B CB  1 
ATOM   1964 C CG  . ASN B 1 48  ? 13.388  -21.300 47.187  1.00 90.19  ? 50  ASN B CG  1 
ATOM   1965 O OD1 . ASN B 1 48  ? 14.122  -20.294 47.104  1.00 90.72  ? 50  ASN B OD1 1 
ATOM   1966 N ND2 . ASN B 1 48  ? 12.733  -21.584 48.327  1.00 90.88  ? 50  ASN B ND2 1 
ATOM   1967 N N   . ASP B 1 49  ? 16.856  -22.099 45.552  1.00 88.44  ? 51  ASP B N   1 
ATOM   1968 C CA  . ASP B 1 49  ? 18.099  -22.296 46.319  1.00 89.59  ? 51  ASP B CA  1 
ATOM   1969 C C   . ASP B 1 49  ? 18.819  -20.953 46.646  1.00 90.50  ? 51  ASP B C   1 
ATOM   1970 O O   . ASP B 1 49  ? 19.198  -20.191 45.757  1.00 89.45  ? 51  ASP B O   1 
ATOM   1971 C CB  . ASP B 1 49  ? 19.040  -23.268 45.593  1.00 90.77  ? 51  ASP B CB  1 
ATOM   1972 C CG  . ASP B 1 49  ? 20.257  -23.690 46.393  1.00 93.78  ? 51  ASP B CG  1 
ATOM   1973 O OD1 . ASP B 1 49  ? 20.298  -23.406 47.624  1.00 93.41  ? 51  ASP B OD1 1 
ATOM   1974 O OD2 . ASP B 1 49  ? 21.169  -24.301 45.797  1.00 96.00  ? 51  ASP B OD2 1 
ATOM   1975 N N   . LYS B 1 50  ? 19.007  -20.694 47.954  1.00 92.04  ? 52  LYS B N   1 
ATOM   1976 C CA  . LYS B 1 50  ? 19.501  -19.408 48.463  1.00 93.54  ? 52  LYS B CA  1 
ATOM   1977 C C   . LYS B 1 50  ? 21.043  -19.315 48.406  1.00 94.84  ? 52  LYS B C   1 
ATOM   1978 O O   . LYS B 1 50  ? 21.586  -18.202 48.307  1.00 94.80  ? 52  LYS B O   1 
ATOM   1979 C CB  . LYS B 1 50  ? 18.953  -19.142 49.898  1.00 94.62  ? 52  LYS B CB  1 
ATOM   1980 C CG  . LYS B 1 50  ? 17.504  -18.651 49.939  1.00 97.12  ? 52  LYS B CG  1 
ATOM   1981 C CD  . LYS B 1 50  ? 17.444  -17.150 49.741  1.00 100.79 ? 52  LYS B CD  1 
ATOM   1982 C CE  . LYS B 1 50  ? 16.043  -16.626 49.722  1.00 104.36 ? 52  LYS B CE  1 
ATOM   1983 N NZ  . LYS B 1 50  ? 16.024  -15.147 49.903  1.00 107.00 ? 52  LYS B NZ  1 
ATOM   1984 N N   . SER B 1 51  ? 21.753  -20.475 48.454  1.00 95.61  ? 53  SER B N   1 
ATOM   1985 C CA  . SER B 1 51  ? 23.207  -20.488 48.237  1.00 96.78  ? 53  SER B CA  1 
ATOM   1986 C C   . SER B 1 51  ? 23.603  -20.189 46.772  1.00 98.43  ? 53  SER B C   1 
ATOM   1987 O O   . SER B 1 51  ? 24.797  -20.205 46.467  1.00 98.57  ? 53  SER B O   1 
ATOM   1988 C CB  . SER B 1 51  ? 23.810  -21.823 48.677  1.00 97.54  ? 53  SER B CB  1 
ATOM   1989 O OG  . SER B 1 51  ? 23.502  -22.897 47.805  1.00 99.29  ? 53  SER B OG  1 
ATOM   1990 N N   . LYS B 1 52  ? 22.618  -19.923 45.869  1.00 99.33  ? 54  LYS B N   1 
ATOM   1991 C CA  . LYS B 1 52  ? 22.871  -19.651 44.458  1.00 100.56 ? 54  LYS B CA  1 
ATOM   1992 C C   . LYS B 1 52  ? 22.176  -18.360 43.941  1.00 101.25 ? 54  LYS B C   1 
ATOM   1993 O O   . LYS B 1 52  ? 22.664  -17.776 42.975  1.00 101.73 ? 54  LYS B O   1 
ATOM   1994 C CB  . LYS B 1 52  ? 22.470  -20.897 43.640  1.00 102.89 ? 54  LYS B CB  1 
ATOM   1995 C CG  . LYS B 1 52  ? 23.469  -22.054 43.761  1.00 107.70 ? 54  LYS B CG  1 
ATOM   1996 C CD  . LYS B 1 52  ? 22.949  -23.361 43.192  1.00 112.91 ? 54  LYS B CD  1 
ATOM   1997 C CE  . LYS B 1 52  ? 23.049  -23.434 41.688  1.00 118.21 ? 54  LYS B CE  1 
ATOM   1998 N NZ  . LYS B 1 52  ? 22.506  -24.720 41.170  1.00 121.76 ? 54  LYS B NZ  1 
ATOM   1999 N N   . THR B 1 53  ? 21.060  -17.901 44.565  1.00 101.02 ? 55  THR B N   1 
ATOM   2000 C CA  . THR B 1 53  ? 20.314  -16.676 44.179  1.00 101.22 ? 55  THR B CA  1 
ATOM   2001 C C   . THR B 1 53  ? 19.719  -16.747 42.737  1.00 101.17 ? 55  THR B C   1 
ATOM   2002 O O   . THR B 1 53  ? 20.188  -17.522 41.896  1.00 101.38 ? 55  THR B O   1 
ATOM   2003 C CB  . THR B 1 53  ? 21.140  -15.367 44.399  1.00 102.47 ? 55  THR B CB  1 
ATOM   2004 O OG1 . THR B 1 53  ? 21.926  -15.069 43.240  1.00 103.42 ? 55  THR B OG1 1 
ATOM   2005 C CG2 . THR B 1 53  ? 22.022  -15.421 45.659  1.00 102.74 ? 55  THR B CG2 1 
ATOM   2006 N N   . TRP B 1 54  ? 18.688  -15.909 42.481  1.00 100.56 ? 56  TRP B N   1 
ATOM   2007 C CA  . TRP B 1 54  ? 17.808  -15.960 41.300  1.00 100.37 ? 56  TRP B CA  1 
ATOM   2008 C C   . TRP B 1 54  ? 18.498  -16.040 39.929  1.00 97.72  ? 56  TRP B C   1 
ATOM   2009 O O   . TRP B 1 54  ? 17.860  -16.486 38.980  1.00 97.77  ? 56  TRP B O   1 
ATOM   2010 C CB  . TRP B 1 54  ? 16.847  -14.751 41.292  1.00 101.77 ? 56  TRP B CB  1 
ATOM   2011 C CG  . TRP B 1 54  ? 17.538  -13.435 41.086  1.00 104.24 ? 56  TRP B CG  1 
ATOM   2012 C CD1 . TRP B 1 54  ? 18.060  -12.621 42.050  1.00 105.87 ? 56  TRP B CD1 1 
ATOM   2013 C CD2 . TRP B 1 54  ? 17.811  -12.797 39.829  1.00 105.11 ? 56  TRP B CD2 1 
ATOM   2014 N NE1 . TRP B 1 54  ? 18.640  -11.512 41.470  1.00 106.45 ? 56  TRP B NE1 1 
ATOM   2015 C CE2 . TRP B 1 54  ? 18.503  -11.599 40.108  1.00 106.23 ? 56  TRP B CE2 1 
ATOM   2016 C CE3 . TRP B 1 54  ? 17.551  -13.131 38.493  1.00 105.91 ? 56  TRP B CE3 1 
ATOM   2017 C CZ2 . TRP B 1 54  ? 18.927  -10.734 39.102  1.00 107.09 ? 56  TRP B CZ2 1 
ATOM   2018 C CZ3 . TRP B 1 54  ? 17.969  -12.273 37.499  1.00 106.98 ? 56  TRP B CZ3 1 
ATOM   2019 C CH2 . TRP B 1 54  ? 18.645  -11.087 37.806  1.00 107.29 ? 56  TRP B CH2 1 
ATOM   2020 N N   . GLN B 1 55  ? 19.761  -15.595 39.806  1.00 95.27  ? 57  GLN B N   1 
ATOM   2021 C CA  . GLN B 1 55  ? 20.491  -15.677 38.535  1.00 93.38  ? 57  GLN B CA  1 
ATOM   2022 C C   . GLN B 1 55  ? 20.924  -17.120 38.241  1.00 90.02  ? 57  GLN B C   1 
ATOM   2023 O O   . GLN B 1 55  ? 20.756  -17.599 37.119  1.00 89.79  ? 57  GLN B O   1 
ATOM   2024 C CB  . GLN B 1 55  ? 21.730  -14.744 38.543  1.00 95.83  ? 57  GLN B CB  1 
ATOM   2025 C CG  . GLN B 1 55  ? 22.672  -14.935 37.327  1.00 100.36 ? 57  GLN B CG  1 
ATOM   2026 C CD  . GLN B 1 55  ? 23.743  -13.876 37.224  1.00 105.07 ? 57  GLN B CD  1 
ATOM   2027 O OE1 . GLN B 1 55  ? 24.941  -14.140 37.451  1.00 105.63 ? 57  GLN B OE1 1 
ATOM   2028 N NE2 . GLN B 1 55  ? 23.327  -12.657 36.872  1.00 106.08 ? 57  GLN B NE2 1 
ATOM   2029 N N   . ALA B 1 56  ? 21.495  -17.799 39.238  1.00 87.25  ? 58  ALA B N   1 
ATOM   2030 C CA  . ALA B 1 56  ? 22.005  -19.156 39.044  1.00 84.99  ? 58  ALA B CA  1 
ATOM   2031 C C   . ALA B 1 56  ? 20.902  -20.206 39.102  1.00 81.92  ? 58  ALA B C   1 
ATOM   2032 O O   . ALA B 1 56  ? 21.078  -21.279 38.528  1.00 82.17  ? 58  ALA B O   1 
ATOM   2033 C CB  . ALA B 1 56  ? 23.081  -19.473 40.071  1.00 85.19  ? 58  ALA B CB  1 
ATOM   2034 N N   . ASN B 1 57  ? 19.778  -19.913 39.790  1.00 78.63  ? 59  ASN B N   1 
ATOM   2035 C CA  . ASN B 1 57  ? 18.671  -20.857 39.893  1.00 76.23  ? 59  ASN B CA  1 
ATOM   2036 C C   . ASN B 1 57  ? 17.884  -20.927 38.604  1.00 73.17  ? 59  ASN B C   1 
ATOM   2037 O O   . ASN B 1 57  ? 17.435  -22.011 38.238  1.00 74.02  ? 59  ASN B O   1 
ATOM   2038 C CB  . ASN B 1 57  ? 17.719  -20.464 41.020  1.00 76.79  ? 59  ASN B CB  1 
ATOM   2039 C CG  . ASN B 1 57  ? 18.312  -20.609 42.391  1.00 78.91  ? 59  ASN B CG  1 
ATOM   2040 O OD1 . ASN B 1 57  ? 19.260  -21.375 42.611  1.00 79.21  ? 59  ASN B OD1 1 
ATOM   2041 N ND2 . ASN B 1 57  ? 17.748  -19.886 43.351  1.00 79.52  ? 59  ASN B ND2 1 
ATOM   2042 N N   . LEU B 1 58  ? 17.697  -19.785 37.927  1.00 69.69  ? 60  LEU B N   1 
ATOM   2043 C CA  . LEU B 1 58  ? 16.929  -19.749 36.710  1.00 67.18  ? 60  LEU B CA  1 
ATOM   2044 C C   . LEU B 1 58  ? 17.800  -20.244 35.603  1.00 64.55  ? 60  LEU B C   1 
ATOM   2045 O O   . LEU B 1 58  ? 18.777  -19.594 35.284  1.00 64.67  ? 60  LEU B O   1 
ATOM   2046 C CB  . LEU B 1 58  ? 16.409  -18.331 36.432  1.00 67.26  ? 60  LEU B CB  1 
ATOM   2047 C CG  . LEU B 1 58  ? 15.517  -18.174 35.203  1.00 68.61  ? 60  LEU B CG  1 
ATOM   2048 C CD1 . LEU B 1 58  ? 14.313  -19.151 35.236  1.00 69.41  ? 60  LEU B CD1 1 
ATOM   2049 C CD2 . LEU B 1 58  ? 15.065  -16.719 35.028  1.00 69.55  ? 60  LEU B CD2 1 
ATOM   2050 N N   . ARG B 1 59  ? 17.491  -21.441 35.047  1.00 62.39  ? 61  ARG B N   1 
ATOM   2051 C CA  . ARG B 1 59  ? 18.179  -22.011 33.888  1.00 60.72  ? 61  ARG B CA  1 
ATOM   2052 C C   . ARG B 1 59  ? 17.208  -22.171 32.704  1.00 56.95  ? 61  ARG B C   1 
ATOM   2053 O O   . ARG B 1 59  ? 16.124  -22.746 32.847  1.00 56.14  ? 61  ARG B O   1 
ATOM   2054 C CB  . ARG B 1 59  ? 18.798  -23.384 34.234  1.00 65.04  ? 61  ARG B CB  1 
ATOM   2055 C CG  . ARG B 1 59  ? 20.165  -23.302 34.959  1.00 74.09  ? 61  ARG B CG  1 
ATOM   2056 C CD  . ARG B 1 59  ? 20.728  -24.680 35.323  1.00 81.30  ? 61  ARG B CD  1 
ATOM   2057 N NE  . ARG B 1 59  ? 20.158  -25.212 36.568  1.00 86.64  ? 61  ARG B NE  1 
ATOM   2058 C CZ  . ARG B 1 59  ? 20.530  -24.848 37.795  1.00 90.42  ? 61  ARG B CZ  1 
ATOM   2059 N NH1 . ARG B 1 59  ? 19.952  -25.396 38.860  1.00 90.46  ? 61  ARG B NH1 1 
ATOM   2060 N NH2 . ARG B 1 59  ? 21.480  -23.931 37.967  1.00 91.27  ? 61  ARG B NH2 1 
ATOM   2061 N N   . LEU B 1 60  ? 17.607  -21.651 31.530  1.00 54.18  ? 62  LEU B N   1 
ATOM   2062 C CA  . LEU B 1 60  ? 16.919  -21.899 30.265  1.00 51.84  ? 62  LEU B CA  1 
ATOM   2063 C C   . LEU B 1 60  ? 17.232  -23.318 29.788  1.00 50.24  ? 62  LEU B C   1 
ATOM   2064 O O   . LEU B 1 60  ? 18.395  -23.731 29.826  1.00 50.96  ? 62  LEU B O   1 
ATOM   2065 C CB  . LEU B 1 60  ? 17.358  -20.875 29.219  1.00 50.77  ? 62  LEU B CB  1 
ATOM   2066 C CG  . LEU B 1 60  ? 16.813  -21.059 27.826  1.00 51.70  ? 62  LEU B CG  1 
ATOM   2067 C CD1 . LEU B 1 60  ? 15.329  -20.770 27.763  1.00 51.28  ? 62  LEU B CD1 1 
ATOM   2068 C CD2 . LEU B 1 60  ? 17.565  -20.194 26.846  1.00 53.01  ? 62  LEU B CD2 1 
ATOM   2069 N N   . ILE B 1 61  ? 16.192  -24.059 29.339  1.00 48.12  ? 63  ILE B N   1 
ATOM   2070 C CA  . ILE B 1 61  ? 16.285  -25.474 28.985  1.00 46.65  ? 63  ILE B CA  1 
ATOM   2071 C C   . ILE B 1 61  ? 16.323  -25.555 27.468  1.00 44.53  ? 63  ILE B C   1 
ATOM   2072 O O   . ILE B 1 61  ? 17.202  -26.212 26.909  1.00 44.41  ? 63  ILE B O   1 
ATOM   2073 C CB  . ILE B 1 61  ? 15.108  -26.316 29.567  1.00 47.68  ? 63  ILE B CB  1 
ATOM   2074 C CG1 . ILE B 1 61  ? 15.024  -26.267 31.128  1.00 49.91  ? 63  ILE B CG1 1 
ATOM   2075 C CG2 . ILE B 1 61  ? 15.135  -27.781 29.038  1.00 47.94  ? 63  ILE B CG2 1 
ATOM   2076 C CD1 . ILE B 1 61  ? 16.321  -26.341 31.896  1.00 52.21  ? 63  ILE B CD1 1 
ATOM   2077 N N   . SER B 1 62  ? 15.370  -24.894 26.788  1.00 42.91  ? 64  SER B N   1 
ATOM   2078 C CA  . SER B 1 62  ? 15.294  -24.972 25.324  1.00 41.64  ? 64  SER B CA  1 
ATOM   2079 C C   . SER B 1 62  ? 14.229  -24.023 24.749  1.00 38.45  ? 64  SER B C   1 
ATOM   2080 O O   . SER B 1 62  ? 13.305  -23.685 25.465  1.00 38.66  ? 64  SER B O   1 
ATOM   2081 C CB  . SER B 1 62  ? 14.979  -26.407 24.906  1.00 43.59  ? 64  SER B CB  1 
ATOM   2082 O OG  . SER B 1 62  ? 14.845  -26.557 23.507  1.00 47.03  ? 64  SER B OG  1 
ATOM   2083 N N   . LYS B 1 63  ? 14.371  -23.612 23.483  1.00 35.73  ? 65  LYS B N   1 
ATOM   2084 C CA  . LYS B 1 63  ? 13.384  -22.825 22.734  1.00 35.08  ? 65  LYS B CA  1 
ATOM   2085 C C   . LYS B 1 63  ? 12.852  -23.593 21.520  1.00 36.54  ? 65  LYS B C   1 
ATOM   2086 O O   . LYS B 1 63  ? 13.500  -24.523 21.055  1.00 38.34  ? 65  LYS B O   1 
ATOM   2087 C CB  . LYS B 1 63  ? 13.925  -21.452 22.314  1.00 31.72  ? 65  LYS B CB  1 
ATOM   2088 C CG  . LYS B 1 63  ? 14.605  -20.705 23.428  1.00 32.02  ? 65  LYS B CG  1 
ATOM   2089 C CD  . LYS B 1 63  ? 14.739  -19.234 23.089  1.00 34.88  ? 65  LYS B CD  1 
ATOM   2090 C CE  . LYS B 1 63  ? 15.421  -18.472 24.168  1.00 36.16  ? 65  LYS B CE  1 
ATOM   2091 N NZ  . LYS B 1 63  ? 15.702  -17.090 23.708  1.00 39.44  ? 65  LYS B NZ  1 
ATOM   2092 N N   . PHE B 1 64  ? 11.659  -23.212 21.022  1.00 35.81  ? 66  PHE B N   1 
ATOM   2093 C CA  . PHE B 1 64  ? 10.990  -23.904 19.926  1.00 35.48  ? 66  PHE B CA  1 
ATOM   2094 C C   . PHE B 1 64  ? 9.950   -23.022 19.300  1.00 36.26  ? 66  PHE B C   1 
ATOM   2095 O O   . PHE B 1 64  ? 9.412   -22.147 19.947  1.00 37.12  ? 66  PHE B O   1 
ATOM   2096 C CB  . PHE B 1 64  ? 10.401  -25.274 20.339  1.00 35.21  ? 66  PHE B CB  1 
ATOM   2097 C CG  . PHE B 1 64  ? 9.316   -25.188 21.409  1.00 34.97  ? 66  PHE B CG  1 
ATOM   2098 C CD1 . PHE B 1 64  ? 7.989   -24.955 21.065  1.00 35.30  ? 66  PHE B CD1 1 
ATOM   2099 C CD2 . PHE B 1 64  ? 9.634   -25.282 22.742  1.00 34.77  ? 66  PHE B CD2 1 
ATOM   2100 C CE1 . PHE B 1 64  ? 7.015   -24.799 22.043  1.00 35.28  ? 66  PHE B CE1 1 
ATOM   2101 C CE2 . PHE B 1 64  ? 8.656   -25.156 23.709  1.00 36.16  ? 66  PHE B CE2 1 
ATOM   2102 C CZ  . PHE B 1 64  ? 7.348   -24.900 23.348  1.00 35.24  ? 66  PHE B CZ  1 
ATOM   2103 N N   . ASP B 1 65  ? 9.663   -23.240 18.026  1.00 37.07  ? 67  ASP B N   1 
ATOM   2104 C CA  . ASP B 1 65  ? 8.665   -22.474 17.290  1.00 37.84  ? 67  ASP B CA  1 
ATOM   2105 C C   . ASP B 1 65  ? 7.932   -23.333 16.247  1.00 37.15  ? 67  ASP B C   1 
ATOM   2106 O O   . ASP B 1 65  ? 7.385   -22.808 15.301  1.00 37.50  ? 67  ASP B O   1 
ATOM   2107 C CB  . ASP B 1 65  ? 9.264   -21.188 16.693  1.00 42.15  ? 67  ASP B CB  1 
ATOM   2108 C CG  . ASP B 1 65  ? 10.305  -21.393 15.637  1.00 49.71  ? 67  ASP B CG  1 
ATOM   2109 O OD1 . ASP B 1 65  ? 11.104  -22.331 15.780  1.00 51.97  ? 67  ASP B OD1 1 
ATOM   2110 O OD2 . ASP B 1 65  ? 10.318  -20.609 14.670  1.00 53.00  ? 67  ASP B OD2 1 
ATOM   2111 N N   . THR B 1 66  ? 7.895   -24.652 16.426  1.00 38.32  ? 68  THR B N   1 
ATOM   2112 C CA  . THR B 1 66  ? 7.021   -25.545 15.655  1.00 38.51  ? 68  THR B CA  1 
ATOM   2113 C C   . THR B 1 66  ? 6.311   -26.495 16.600  1.00 39.31  ? 68  THR B C   1 
ATOM   2114 O O   . THR B 1 66  ? 6.774   -26.700 17.725  1.00 39.95  ? 68  THR B O   1 
ATOM   2115 C CB  . THR B 1 66  ? 7.789   -26.319 14.550  1.00 37.59  ? 68  THR B CB  1 
ATOM   2116 O OG1 . THR B 1 66  ? 8.529   -27.377 15.124  1.00 39.27  ? 68  THR B OG1 1 
ATOM   2117 C CG2 . THR B 1 66  ? 8.723   -25.427 13.760  1.00 36.47  ? 68  THR B CG2 1 
ATOM   2118 N N   . VAL B 1 67  ? 5.185   -27.076 16.121  1.00 39.09  ? 69  VAL B N   1 
ATOM   2119 C CA  . VAL B 1 67  ? 4.407   -28.069 16.838  1.00 40.12  ? 69  VAL B CA  1 
ATOM   2120 C C   . VAL B 1 67  ? 5.240   -29.314 17.097  1.00 42.81  ? 69  VAL B C   1 
ATOM   2121 O O   . VAL B 1 67  ? 5.214   -29.847 18.193  1.00 43.00  ? 69  VAL B O   1 
ATOM   2122 C CB  . VAL B 1 67  ? 3.117   -28.444 16.088  1.00 40.04  ? 69  VAL B CB  1 
ATOM   2123 C CG1 . VAL B 1 67  ? 2.360   -29.526 16.839  1.00 40.97  ? 69  VAL B CG1 1 
ATOM   2124 C CG2 . VAL B 1 67  ? 2.245   -27.226 15.859  1.00 39.10  ? 69  VAL B CG2 1 
ATOM   2125 N N   . GLU B 1 68  ? 5.983   -29.777 16.088  1.00 44.12  ? 70  GLU B N   1 
ATOM   2126 C CA  . GLU B 1 68  ? 6.821   -30.983 16.185  1.00 45.21  ? 70  GLU B CA  1 
ATOM   2127 C C   . GLU B 1 68  ? 7.982   -30.826 17.179  1.00 44.62  ? 70  GLU B C   1 
ATOM   2128 O O   . GLU B 1 68  ? 8.294   -31.762 17.917  1.00 45.12  ? 70  GLU B O   1 
ATOM   2129 C CB  . GLU B 1 68  ? 7.397   -31.326 14.793  1.00 49.56  ? 70  GLU B CB  1 
ATOM   2130 C CG  . GLU B 1 68  ? 6.347   -31.785 13.776  1.00 54.55  ? 70  GLU B CG  1 
ATOM   2131 C CD  . GLU B 1 68  ? 5.442   -30.712 13.210  1.00 62.30  ? 70  GLU B CD  1 
ATOM   2132 O OE1 . GLU B 1 68  ? 5.813   -29.519 13.296  1.00 64.68  ? 70  GLU B OE1 1 
ATOM   2133 O OE2 . GLU B 1 68  ? 4.363   -31.058 12.677  1.00 63.96  ? 70  GLU B OE2 1 
ATOM   2134 N N   . ASP B 1 69  ? 8.631   -29.653 17.195  1.00 43.80  ? 71  ASP B N   1 
ATOM   2135 C CA  . ASP B 1 69  ? 9.716   -29.393 18.162  1.00 42.78  ? 71  ASP B CA  1 
ATOM   2136 C C   . ASP B 1 69  ? 9.178   -29.241 19.595  1.00 40.89  ? 71  ASP B C   1 
ATOM   2137 O O   . ASP B 1 69  ? 9.866   -29.632 20.551  1.00 41.04  ? 71  ASP B O   1 
ATOM   2138 C CB  . ASP B 1 69  ? 10.508  -28.155 17.768  1.00 44.21  ? 71  ASP B CB  1 
ATOM   2139 C CG  . ASP B 1 69  ? 11.190  -28.316 16.428  1.00 48.20  ? 71  ASP B CG  1 
ATOM   2140 O OD1 . ASP B 1 69  ? 11.730  -29.417 16.171  1.00 50.25  ? 71  ASP B OD1 1 
ATOM   2141 O OD2 . ASP B 1 69  ? 11.169  -27.343 15.622  1.00 48.33  ? 71  ASP B OD2 1 
ATOM   2142 N N   . PHE B 1 70  ? 7.939   -28.696 19.748  1.00 38.86  ? 72  PHE B N   1 
ATOM   2143 C CA  . PHE B 1 70  ? 7.227   -28.726 21.034  1.00 36.95  ? 72  PHE B CA  1 
ATOM   2144 C C   . PHE B 1 70  ? 7.069   -30.167 21.501  1.00 36.49  ? 72  PHE B C   1 
ATOM   2145 O O   . PHE B 1 70  ? 7.454   -30.478 22.622  1.00 35.44  ? 72  PHE B O   1 
ATOM   2146 C CB  . PHE B 1 70  ? 5.842   -28.039 20.959  1.00 34.82  ? 72  PHE B CB  1 
ATOM   2147 C CG  . PHE B 1 70  ? 4.951   -28.446 22.104  1.00 34.12  ? 72  PHE B CG  1 
ATOM   2148 C CD1 . PHE B 1 70  ? 5.158   -27.948 23.376  1.00 34.43  ? 72  PHE B CD1 1 
ATOM   2149 C CD2 . PHE B 1 70  ? 3.942   -29.377 21.923  1.00 34.12  ? 72  PHE B CD2 1 
ATOM   2150 C CE1 . PHE B 1 70  ? 4.342   -28.340 24.425  1.00 34.67  ? 72  PHE B CE1 1 
ATOM   2151 C CE2 . PHE B 1 70  ? 3.145   -29.774 22.979  1.00 34.20  ? 72  PHE B CE2 1 
ATOM   2152 C CZ  . PHE B 1 70  ? 3.353   -29.273 24.220  1.00 33.70  ? 72  PHE B CZ  1 
ATOM   2153 N N   . TRP B 1 71  ? 6.508   -31.042 20.642  1.00 37.80  ? 73  TRP B N   1 
ATOM   2154 C CA  . TRP B 1 71  ? 6.319   -32.426 21.021  1.00 39.77  ? 73  TRP B CA  1 
ATOM   2155 C C   . TRP B 1 71  ? 7.591   -33.191 21.253  1.00 42.01  ? 73  TRP B C   1 
ATOM   2156 O O   . TRP B 1 71  ? 7.617   -34.014 22.134  1.00 44.38  ? 73  TRP B O   1 
ATOM   2157 C CB  . TRP B 1 71  ? 5.484   -33.175 19.999  1.00 39.66  ? 73  TRP B CB  1 
ATOM   2158 C CG  . TRP B 1 71  ? 4.027   -32.848 20.074  1.00 38.29  ? 73  TRP B CG  1 
ATOM   2159 C CD1 . TRP B 1 71  ? 3.261   -32.310 19.089  1.00 38.32  ? 73  TRP B CD1 1 
ATOM   2160 C CD2 . TRP B 1 71  ? 3.160   -33.045 21.202  1.00 36.97  ? 73  TRP B CD2 1 
ATOM   2161 N NE1 . TRP B 1 71  ? 1.963   -32.183 19.521  1.00 38.32  ? 73  TRP B NE1 1 
ATOM   2162 C CE2 . TRP B 1 71  ? 1.878   -32.611 20.821  1.00 37.65  ? 73  TRP B CE2 1 
ATOM   2163 C CE3 . TRP B 1 71  ? 3.361   -33.495 22.508  1.00 37.03  ? 73  TRP B CE3 1 
ATOM   2164 C CZ2 . TRP B 1 71  ? 0.800   -32.614 21.697  1.00 38.80  ? 73  TRP B CZ2 1 
ATOM   2165 C CZ3 . TRP B 1 71  ? 2.290   -33.515 23.371  1.00 38.82  ? 73  TRP B CZ3 1 
ATOM   2166 C CH2 . TRP B 1 71  ? 1.023   -33.078 22.964  1.00 39.26  ? 73  TRP B CH2 1 
ATOM   2167 N N   . ALA B 1 72  ? 8.645   -32.957 20.483  1.00 42.40  ? 74  ALA B N   1 
ATOM   2168 C CA  . ALA B 1 72  ? 9.963   -33.565 20.754  1.00 42.20  ? 74  ALA B CA  1 
ATOM   2169 C C   . ALA B 1 72  ? 10.454  -33.221 22.171  1.00 41.42  ? 74  ALA B C   1 
ATOM   2170 O O   . ALA B 1 72  ? 10.880  -34.101 22.892  1.00 41.55  ? 74  ALA B O   1 
ATOM   2171 C CB  . ALA B 1 72  ? 10.991  -33.078 19.708  1.00 43.10  ? 74  ALA B CB  1 
ATOM   2172 N N   . LEU B 1 73  ? 10.386  -31.940 22.562  1.00 41.01  ? 75  LEU B N   1 
ATOM   2173 C CA  . LEU B 1 73  ? 10.804  -31.466 23.883  1.00 40.91  ? 75  LEU B CA  1 
ATOM   2174 C C   . LEU B 1 73  ? 9.901   -32.013 24.954  1.00 40.52  ? 75  LEU B C   1 
ATOM   2175 O O   . LEU B 1 73  ? 10.380  -32.452 26.002  1.00 39.67  ? 75  LEU B O   1 
ATOM   2176 C CB  . LEU B 1 73  ? 10.781  -29.919 23.901  1.00 41.48  ? 75  LEU B CB  1 
ATOM   2177 C CG  . LEU B 1 73  ? 11.147  -29.252 25.205  1.00 42.08  ? 75  LEU B CG  1 
ATOM   2178 C CD1 . LEU B 1 73  ? 12.586  -29.585 25.599  1.00 42.12  ? 75  LEU B CD1 1 
ATOM   2179 C CD2 . LEU B 1 73  ? 10.949  -27.773 25.112  1.00 41.89  ? 75  LEU B CD2 1 
ATOM   2180 N N   . TYR B 1 74  ? 8.584   -32.004 24.701  1.00 41.43  ? 76  TYR B N   1 
ATOM   2181 C CA  . TYR B 1 74  ? 7.616   -32.567 25.633  1.00 42.58  ? 76  TYR B CA  1 
ATOM   2182 C C   . TYR B 1 74  ? 7.885   -34.048 25.902  1.00 43.90  ? 76  TYR B C   1 
ATOM   2183 O O   . TYR B 1 74  ? 7.975   -34.451 27.064  1.00 43.87  ? 76  TYR B O   1 
ATOM   2184 C CB  . TYR B 1 74  ? 6.178   -32.376 25.104  1.00 41.82  ? 76  TYR B CB  1 
ATOM   2185 C CG  . TYR B 1 74  ? 5.129   -32.828 26.096  1.00 41.56  ? 76  TYR B CG  1 
ATOM   2186 C CD1 . TYR B 1 74  ? 4.690   -34.152 26.125  1.00 41.80  ? 76  TYR B CD1 1 
ATOM   2187 C CD2 . TYR B 1 74  ? 4.570   -31.935 27.001  1.00 41.96  ? 76  TYR B CD2 1 
ATOM   2188 C CE1 . TYR B 1 74  ? 3.739   -34.574 27.041  1.00 42.23  ? 76  TYR B CE1 1 
ATOM   2189 C CE2 . TYR B 1 74  ? 3.605   -32.337 27.901  1.00 43.08  ? 76  TYR B CE2 1 
ATOM   2190 C CZ  . TYR B 1 74  ? 3.199   -33.668 27.930  1.00 44.53  ? 76  TYR B CZ  1 
ATOM   2191 O OH  . TYR B 1 74  ? 2.244   -34.082 28.821  1.00 46.84  ? 76  TYR B OH  1 
ATOM   2192 N N   . ASN B 1 75  ? 8.008   -34.847 24.836  1.00 45.15  ? 77  ASN B N   1 
ATOM   2193 C CA  . ASN B 1 75  ? 8.285   -36.277 24.955  1.00 47.91  ? 77  ASN B CA  1 
ATOM   2194 C C   . ASN B 1 75  ? 9.628   -36.497 25.662  1.00 49.88  ? 77  ASN B C   1 
ATOM   2195 O O   . ASN B 1 75  ? 9.710   -37.321 26.568  1.00 50.55  ? 77  ASN B O   1 
ATOM   2196 C CB  . ASN B 1 75  ? 8.267   -36.953 23.580  1.00 50.19  ? 77  ASN B CB  1 
ATOM   2197 C CG  . ASN B 1 75  ? 6.895   -37.010 22.924  1.00 55.71  ? 77  ASN B CG  1 
ATOM   2198 O OD1 . ASN B 1 75  ? 5.846   -36.951 23.596  1.00 60.50  ? 77  ASN B OD1 1 
ATOM   2199 N ND2 . ASN B 1 75  ? 6.855   -37.138 21.597  1.00 53.60  ? 77  ASN B ND2 1 
ATOM   2200 N N   . HIS B 1 76  ? 10.674  -35.746 25.280  1.00 50.54  ? 78  HIS B N   1 
ATOM   2201 C CA  . HIS B 1 76  ? 11.953  -35.812 25.979  1.00 51.85  ? 78  HIS B CA  1 
ATOM   2202 C C   . HIS B 1 76  ? 11.802  -35.546 27.509  1.00 52.07  ? 78  HIS B C   1 
ATOM   2203 O O   . HIS B 1 76  ? 12.149  -36.419 28.277  1.00 51.53  ? 78  HIS B O   1 
ATOM   2204 C CB  . HIS B 1 76  ? 12.965  -34.860 25.357  1.00 55.09  ? 78  HIS B CB  1 
ATOM   2205 C CG  . HIS B 1 76  ? 14.286  -34.927 26.051  1.00 62.58  ? 78  HIS B CG  1 
ATOM   2206 N ND1 . HIS B 1 76  ? 14.837  -33.815 26.673  1.00 65.42  ? 78  HIS B ND1 1 
ATOM   2207 C CD2 . HIS B 1 76  ? 15.119  -35.989 26.220  1.00 64.97  ? 78  HIS B CD2 1 
ATOM   2208 C CE1 . HIS B 1 76  ? 15.989  -34.229 27.187  1.00 66.52  ? 78  HIS B CE1 1 
ATOM   2209 N NE2 . HIS B 1 76  ? 16.198  -35.532 26.941  1.00 66.33  ? 78  HIS B NE2 1 
ATOM   2210 N N   . ILE B 1 77  ? 11.269  -34.352 27.935  1.00 51.81  ? 79  ILE B N   1 
ATOM   2211 C CA  . ILE B 1 77  ? 11.071  -34.002 29.353  1.00 51.61  ? 79  ILE B CA  1 
ATOM   2212 C C   . ILE B 1 77  ? 10.209  -35.060 30.094  1.00 53.63  ? 79  ILE B C   1 
ATOM   2213 O O   . ILE B 1 77  ? 10.503  -35.401 31.231  1.00 52.42  ? 79  ILE B O   1 
ATOM   2214 C CB  . ILE B 1 77  ? 10.447  -32.568 29.489  1.00 50.04  ? 79  ILE B CB  1 
ATOM   2215 C CG1 . ILE B 1 77  ? 11.406  -31.436 28.937  1.00 50.58  ? 79  ILE B CG1 1 
ATOM   2216 C CG2 . ILE B 1 77  ? 9.998   -32.273 30.921  1.00 48.43  ? 79  ILE B CG2 1 
ATOM   2217 C CD1 . ILE B 1 77  ? 12.607  -31.049 29.851  1.00 51.90  ? 79  ILE B CD1 1 
ATOM   2218 N N   . GLN B 1 78  ? 9.149   -35.555 29.447  1.00 56.64  ? 80  GLN B N   1 
ATOM   2219 C CA  . GLN B 1 78  ? 8.216   -36.542 30.009  1.00 59.96  ? 80  GLN B CA  1 
ATOM   2220 C C   . GLN B 1 78  ? 8.916   -37.861 30.317  1.00 64.14  ? 80  GLN B C   1 
ATOM   2221 O O   . GLN B 1 78  ? 8.586   -38.501 31.323  1.00 64.74  ? 80  GLN B O   1 
ATOM   2222 C CB  . GLN B 1 78  ? 7.065   -36.813 29.021  1.00 60.93  ? 80  GLN B CB  1 
ATOM   2223 C CG  . GLN B 1 78  ? 5.765   -37.361 29.621  1.00 61.80  ? 80  GLN B CG  1 
ATOM   2224 C CD  . GLN B 1 78  ? 4.756   -37.760 28.554  1.00 65.21  ? 80  GLN B CD  1 
ATOM   2225 O OE1 . GLN B 1 78  ? 5.084   -38.025 27.381  1.00 66.98  ? 80  GLN B OE1 1 
ATOM   2226 N NE2 . GLN B 1 78  ? 3.493   -37.810 28.926  1.00 66.62  ? 80  GLN B NE2 1 
ATOM   2227 N N   . LEU B 1 79  ? 9.867   -38.267 29.452  1.00 67.01  ? 81  LEU B N   1 
ATOM   2228 C CA  . LEU B 1 79  ? 10.653  -39.497 29.644  1.00 69.81  ? 81  LEU B CA  1 
ATOM   2229 C C   . LEU B 1 79  ? 11.798  -39.236 30.643  1.00 70.94  ? 81  LEU B C   1 
ATOM   2230 O O   . LEU B 1 79  ? 11.893  -39.932 31.642  1.00 70.98  ? 81  LEU B O   1 
ATOM   2231 C CB  . LEU B 1 79  ? 11.206  -39.993 28.274  1.00 71.39  ? 81  LEU B CB  1 
ATOM   2232 C CG  . LEU B 1 79  ? 12.120  -41.241 28.301  1.00 75.61  ? 81  LEU B CG  1 
ATOM   2233 C CD1 . LEU B 1 79  ? 11.454  -42.436 29.042  1.00 76.96  ? 81  LEU B CD1 1 
ATOM   2234 C CD2 . LEU B 1 79  ? 12.537  -41.660 26.890  1.00 77.10  ? 81  LEU B CD2 1 
ATOM   2235 N N   . SER B 1 80  ? 12.623  -38.210 30.386  1.00 71.79  ? 82  SER B N   1 
ATOM   2236 C CA  . SER B 1 80  ? 13.942  -38.025 30.986  1.00 73.03  ? 82  SER B CA  1 
ATOM   2237 C C   . SER B 1 80  ? 13.920  -37.331 32.350  1.00 73.02  ? 82  SER B C   1 
ATOM   2238 O O   . SER B 1 80  ? 14.977  -37.225 32.976  1.00 72.84  ? 82  SER B O   1 
ATOM   2239 C CB  . SER B 1 80  ? 14.845  -37.214 30.043  1.00 75.92  ? 82  SER B CB  1 
ATOM   2240 O OG  . SER B 1 80  ? 14.660  -35.801 30.137  1.00 78.92  ? 82  SER B OG  1 
ATOM   2241 N N   . SER B 1 81  ? 12.764  -36.849 32.812  1.00 73.28  ? 83  SER B N   1 
ATOM   2242 C CA  . SER B 1 81  ? 12.725  -35.995 33.998  1.00 74.21  ? 83  SER B CA  1 
ATOM   2243 C C   . SER B 1 81  ? 11.760  -36.573 34.995  1.00 75.09  ? 83  SER B C   1 
ATOM   2244 O O   . SER B 1 81  ? 10.720  -37.111 34.613  1.00 74.48  ? 83  SER B O   1 
ATOM   2245 C CB  . SER B 1 81  ? 12.309  -34.565 33.635  1.00 75.73  ? 83  SER B CB  1 
ATOM   2246 O OG  . SER B 1 81  ? 13.196  -33.936 32.721  1.00 77.81  ? 83  SER B OG  1 
ATOM   2247 N N   . ASN B 1 82  ? 12.108  -36.461 36.279  1.00 76.50  ? 84  ASN B N   1 
ATOM   2248 C CA  . ASN B 1 82  ? 11.257  -36.883 37.391  1.00 77.95  ? 84  ASN B CA  1 
ATOM   2249 C C   . ASN B 1 82  ? 10.849  -35.665 38.233  1.00 78.20  ? 84  ASN B C   1 
ATOM   2250 O O   . ASN B 1 82  ? 11.532  -34.632 38.244  1.00 78.19  ? 84  ASN B O   1 
ATOM   2251 C CB  . ASN B 1 82  ? 11.969  -37.937 38.271  1.00 80.66  ? 84  ASN B CB  1 
ATOM   2252 C CG  . ASN B 1 82  ? 11.641  -39.397 37.964  1.00 85.09  ? 84  ASN B CG  1 
ATOM   2253 O OD1 . ASN B 1 82  ? 10.901  -39.740 37.023  1.00 85.87  ? 84  ASN B OD1 1 
ATOM   2254 N ND2 . ASN B 1 82  ? 12.206  -40.294 38.772  1.00 86.73  ? 84  ASN B ND2 1 
ATOM   2255 N N   . LEU B 1 83  ? 9.724   -35.807 38.948  1.00 77.91  ? 85  LEU B N   1 
ATOM   2256 C CA  . LEU B 1 83  ? 9.057   -34.691 39.590  1.00 78.09  ? 85  LEU B CA  1 
ATOM   2257 C C   . LEU B 1 83  ? 9.648   -34.355 40.969  1.00 78.51  ? 85  LEU B C   1 
ATOM   2258 O O   . LEU B 1 83  ? 9.573   -35.177 41.875  1.00 78.58  ? 85  LEU B O   1 
ATOM   2259 C CB  . LEU B 1 83  ? 7.575   -35.051 39.711  1.00 77.81  ? 85  LEU B CB  1 
ATOM   2260 C CG  . LEU B 1 83  ? 6.639   -33.946 40.148  1.00 78.49  ? 85  LEU B CG  1 
ATOM   2261 C CD1 . LEU B 1 83  ? 6.468   -32.891 39.044  1.00 78.77  ? 85  LEU B CD1 1 
ATOM   2262 C CD2 . LEU B 1 83  ? 5.331   -34.520 40.547  1.00 78.48  ? 85  LEU B CD2 1 
ATOM   2263 N N   . MET B 1 84  ? 10.222  -33.137 41.119  1.00 78.85  ? 86  MET B N   1 
ATOM   2264 C CA  . MET B 1 84  ? 10.863  -32.682 42.363  1.00 79.67  ? 86  MET B CA  1 
ATOM   2265 C C   . MET B 1 84  ? 10.110  -31.482 42.892  1.00 79.11  ? 86  MET B C   1 
ATOM   2266 O O   . MET B 1 84  ? 10.061  -30.477 42.182  1.00 79.91  ? 86  MET B O   1 
ATOM   2267 C CB  . MET B 1 84  ? 12.308  -32.215 42.086  1.00 81.67  ? 86  MET B CB  1 
ATOM   2268 C CG  . MET B 1 84  ? 13.348  -33.346 42.024  1.00 85.96  ? 86  MET B CG  1 
ATOM   2269 S SD  . MET B 1 84  ? 15.021  -32.733 41.645  1.00 94.59  ? 86  MET B SD  1 
ATOM   2270 C CE  . MET B 1 84  ? 14.772  -32.050 39.910  1.00 89.34  ? 86  MET B CE  1 
ATOM   2271 N N   . PRO B 1 85  ? 9.512   -31.520 44.097  1.00 77.72  ? 87  PRO B N   1 
ATOM   2272 C CA  . PRO B 1 85  ? 8.988   -30.270 44.676  1.00 76.68  ? 87  PRO B CA  1 
ATOM   2273 C C   . PRO B 1 85  ? 10.077  -29.215 44.899  1.00 75.29  ? 87  PRO B C   1 
ATOM   2274 O O   . PRO B 1 85  ? 11.272  -29.509 44.840  1.00 75.54  ? 87  PRO B O   1 
ATOM   2275 C CB  . PRO B 1 85  ? 8.273   -30.714 45.966  1.00 77.90  ? 87  PRO B CB  1 
ATOM   2276 C CG  . PRO B 1 85  ? 8.103   -32.210 45.840  1.00 78.86  ? 87  PRO B CG  1 
ATOM   2277 C CD  . PRO B 1 85  ? 9.258   -32.677 44.978  1.00 77.52  ? 87  PRO B CD  1 
ATOM   2278 N N   . GLY B 1 86  ? 9.644   -27.981 45.131  1.00 73.63  ? 88  GLY B N   1 
ATOM   2279 C CA  . GLY B 1 86  ? 10.524  -26.817 45.157  1.00 72.32  ? 88  GLY B CA  1 
ATOM   2280 C C   . GLY B 1 86  ? 10.861  -26.270 43.774  1.00 70.00  ? 88  GLY B C   1 
ATOM   2281 O O   . GLY B 1 86  ? 11.230  -25.098 43.636  1.00 69.60  ? 88  GLY B O   1 
ATOM   2282 N N   . CYS B 1 87  ? 10.747  -27.113 42.737  1.00 68.28  ? 89  CYS B N   1 
ATOM   2283 C CA  . CYS B 1 87  ? 11.032  -26.723 41.371  1.00 67.33  ? 89  CYS B CA  1 
ATOM   2284 C C   . CYS B 1 87  ? 9.858   -25.964 40.707  1.00 63.84  ? 89  CYS B C   1 
ATOM   2285 O O   . CYS B 1 87  ? 8.702   -26.009 41.155  1.00 64.22  ? 89  CYS B O   1 
ATOM   2286 C CB  . CYS B 1 87  ? 11.436  -27.943 40.556  1.00 70.14  ? 89  CYS B CB  1 
ATOM   2287 S SG  . CYS B 1 87  ? 12.956  -28.723 41.136  1.00 82.10  ? 89  CYS B SG  1 
ATOM   2288 N N   . ASP B 1 88  ? 10.188  -25.243 39.647  1.00 59.48  ? 90  ASP B N   1 
ATOM   2289 C CA  . ASP B 1 88  ? 9.214   -24.609 38.811  1.00 56.20  ? 90  ASP B CA  1 
ATOM   2290 C C   . ASP B 1 88  ? 9.637   -24.782 37.384  1.00 52.21  ? 90  ASP B C   1 
ATOM   2291 O O   . ASP B 1 88  ? 10.822  -24.718 37.071  1.00 52.51  ? 90  ASP B O   1 
ATOM   2292 C CB  . ASP B 1 88  ? 9.065   -23.111 39.108  1.00 57.87  ? 90  ASP B CB  1 
ATOM   2293 C CG  . ASP B 1 88  ? 8.990   -22.700 40.577  1.00 60.51  ? 90  ASP B CG  1 
ATOM   2294 O OD1 . ASP B 1 88  ? 8.386   -23.450 41.376  1.00 60.96  ? 90  ASP B OD1 1 
ATOM   2295 O OD2 . ASP B 1 88  ? 9.516   -21.617 40.920  1.00 61.17  ? 90  ASP B OD2 1 
ATOM   2296 N N   . TYR B 1 89  ? 8.667   -25.023 36.519  1.00 48.19  ? 91  TYR B N   1 
ATOM   2297 C CA  . TYR B 1 89  ? 8.833   -24.917 35.081  1.00 44.87  ? 91  TYR B CA  1 
ATOM   2298 C C   . TYR B 1 89  ? 7.947   -23.790 34.562  1.00 39.08  ? 91  TYR B C   1 
ATOM   2299 O O   . TYR B 1 89  ? 6.846   -23.560 35.077  1.00 37.45  ? 91  TYR B O   1 
ATOM   2300 C CB  . TYR B 1 89  ? 8.457   -26.231 34.409  1.00 46.74  ? 91  TYR B CB  1 
ATOM   2301 C CG  . TYR B 1 89  ? 9.422   -27.367 34.678  1.00 49.24  ? 91  TYR B CG  1 
ATOM   2302 C CD1 . TYR B 1 89  ? 9.337   -28.114 35.843  1.00 50.79  ? 91  TYR B CD1 1 
ATOM   2303 C CD2 . TYR B 1 89  ? 10.387  -27.722 33.746  1.00 51.08  ? 91  TYR B CD2 1 
ATOM   2304 C CE1 . TYR B 1 89  ? 10.196  -29.178 36.085  1.00 52.40  ? 91  TYR B CE1 1 
ATOM   2305 C CE2 . TYR B 1 89  ? 11.255  -28.783 33.974  1.00 52.17  ? 91  TYR B CE2 1 
ATOM   2306 C CZ  . TYR B 1 89  ? 11.152  -29.513 35.145  1.00 53.84  ? 91  TYR B CZ  1 
ATOM   2307 O OH  . TYR B 1 89  ? 11.989  -30.580 35.393  1.00 57.43  ? 91  TYR B OH  1 
ATOM   2308 N N   . SER B 1 90  ? 8.437   -23.096 33.555  1.00 36.07  ? 92  SER B N   1 
ATOM   2309 C CA  . SER B 1 90  ? 7.766   -21.961 32.926  1.00 35.28  ? 92  SER B CA  1 
ATOM   2310 C C   . SER B 1 90  ? 7.960   -22.047 31.437  1.00 34.31  ? 92  SER B C   1 
ATOM   2311 O O   . SER B 1 90  ? 9.086   -22.248 30.999  1.00 34.82  ? 92  SER B O   1 
ATOM   2312 C CB  . SER B 1 90  ? 8.377   -20.643 33.383  1.00 36.69  ? 92  SER B CB  1 
ATOM   2313 O OG  . SER B 1 90  ? 8.277   -20.480 34.785  1.00 40.94  ? 92  SER B OG  1 
ATOM   2314 N N   . LEU B 1 91  ? 6.875   -21.896 30.654  1.00 32.57  ? 93  LEU B N   1 
ATOM   2315 C CA  . LEU B 1 91  ? 6.973   -21.657 29.227  1.00 30.22  ? 93  LEU B CA  1 
ATOM   2316 C C   . LEU B 1 91  ? 6.557   -20.230 28.935  1.00 29.08  ? 93  LEU B C   1 
ATOM   2317 O O   . LEU B 1 91  ? 5.401   -19.914 29.124  1.00 27.34  ? 93  LEU B O   1 
ATOM   2318 C CB  . LEU B 1 91  ? 6.084   -22.623 28.448  1.00 28.75  ? 93  LEU B CB  1 
ATOM   2319 C CG  . LEU B 1 91  ? 6.278   -22.560 26.910  1.00 28.53  ? 93  LEU B CG  1 
ATOM   2320 C CD1 . LEU B 1 91  ? 7.592   -23.238 26.503  1.00 27.90  ? 93  LEU B CD1 1 
ATOM   2321 C CD2 . LEU B 1 91  ? 5.106   -23.197 26.161  1.00 28.04  ? 93  LEU B CD2 1 
ATOM   2322 N N   . PHE B 1 92  ? 7.502   -19.375 28.459  1.00 28.78  ? 94  PHE B N   1 
ATOM   2323 C CA  . PHE B 1 92  ? 7.206   -17.981 28.138  1.00 29.85  ? 94  PHE B CA  1 
ATOM   2324 C C   . PHE B 1 92  ? 7.557   -17.665 26.704  1.00 27.97  ? 94  PHE B C   1 
ATOM   2325 O O   . PHE B 1 92  ? 8.442   -18.277 26.124  1.00 27.35  ? 94  PHE B O   1 
ATOM   2326 C CB  . PHE B 1 92  ? 7.974   -17.021 29.061  1.00 31.51  ? 94  PHE B CB  1 
ATOM   2327 C CG  . PHE B 1 92  ? 7.282   -16.800 30.387  1.00 33.40  ? 94  PHE B CG  1 
ATOM   2328 C CD1 . PHE B 1 92  ? 7.179   -17.827 31.316  1.00 33.53  ? 94  PHE B CD1 1 
ATOM   2329 C CD2 . PHE B 1 92  ? 6.677   -15.591 30.675  1.00 34.17  ? 94  PHE B CD2 1 
ATOM   2330 C CE1 . PHE B 1 92  ? 6.497   -17.633 32.500  1.00 34.48  ? 94  PHE B CE1 1 
ATOM   2331 C CE2 . PHE B 1 92  ? 6.024   -15.400 31.878  1.00 34.89  ? 94  PHE B CE2 1 
ATOM   2332 C CZ  . PHE B 1 92  ? 5.940   -16.417 32.777  1.00 34.67  ? 94  PHE B CZ  1 
ATOM   2333 N N   . LYS B 1 93  ? 6.869   -16.690 26.117  1.00 27.70  ? 95  LYS B N   1 
ATOM   2334 C CA  . LYS B 1 93  ? 7.227   -16.180 24.795  1.00 28.75  ? 95  LYS B CA  1 
ATOM   2335 C C   . LYS B 1 93  ? 8.697   -15.743 24.767  1.00 29.92  ? 95  LYS B C   1 
ATOM   2336 O O   . LYS B 1 93  ? 9.251   -15.272 25.766  1.00 29.26  ? 95  LYS B O   1 
ATOM   2337 C CB  . LYS B 1 93  ? 6.322   -15.033 24.372  1.00 30.45  ? 95  LYS B CB  1 
ATOM   2338 C CG  . LYS B 1 93  ? 4.909   -15.489 24.065  1.00 32.01  ? 95  LYS B CG  1 
ATOM   2339 C CD  . LYS B 1 93  ? 4.036   -14.349 23.801  1.00 31.76  ? 95  LYS B CD  1 
ATOM   2340 C CE  . LYS B 1 93  ? 2.706   -14.840 23.365  1.00 34.80  ? 95  LYS B CE  1 
ATOM   2341 N NZ  . LYS B 1 93  ? 1.669   -13.772 23.284  1.00 31.78  ? 95  LYS B NZ  1 
ATOM   2342 N N   . ASP B 1 94  ? 9.330   -15.952 23.646  1.00 31.44  ? 96  ASP B N   1 
ATOM   2343 C CA  . ASP B 1 94  ? 10.737  -15.611 23.456  1.00 33.93  ? 96  ASP B CA  1 
ATOM   2344 C C   . ASP B 1 94  ? 10.936  -14.115 23.745  1.00 35.62  ? 96  ASP B C   1 
ATOM   2345 O O   . ASP B 1 94  ? 10.204  -13.305 23.178  1.00 36.15  ? 96  ASP B O   1 
ATOM   2346 C CB  . ASP B 1 94  ? 11.143  -15.972 22.015  1.00 34.89  ? 96  ASP B CB  1 
ATOM   2347 C CG  . ASP B 1 94  ? 12.634  -15.947 21.714  1.00 39.26  ? 96  ASP B CG  1 
ATOM   2348 O OD1 . ASP B 1 94  ? 13.433  -16.090 22.650  1.00 39.59  ? 96  ASP B OD1 1 
ATOM   2349 O OD2 . ASP B 1 94  ? 12.992  -15.796 20.548  1.00 41.76  ? 96  ASP B OD2 1 
ATOM   2350 N N   . GLY B 1 95  ? 11.860  -13.800 24.665  1.00 36.27  ? 97  GLY B N   1 
ATOM   2351 C CA  . GLY B 1 95  ? 12.176  -12.439 25.067  1.00 37.12  ? 97  GLY B CA  1 
ATOM   2352 C C   . GLY B 1 95  ? 11.538  -11.935 26.350  1.00 37.69  ? 97  GLY B C   1 
ATOM   2353 O O   . GLY B 1 95  ? 11.769  -10.788 26.738  1.00 38.96  ? 97  GLY B O   1 
ATOM   2354 N N   . ILE B 1 96  ? 10.745  -12.755 27.010  1.00 37.12  ? 98  ILE B N   1 
ATOM   2355 C CA  . ILE B 1 96  ? 10.123  -12.458 28.305  1.00 36.58  ? 98  ILE B CA  1 
ATOM   2356 C C   . ILE B 1 96  ? 10.736  -13.445 29.293  1.00 38.32  ? 98  ILE B C   1 
ATOM   2357 O O   . ILE B 1 96  ? 10.543  -14.663 29.176  1.00 36.68  ? 98  ILE B O   1 
ATOM   2358 C CB  . ILE B 1 96  ? 8.573   -12.647 28.270  1.00 35.32  ? 98  ILE B CB  1 
ATOM   2359 C CG1 . ILE B 1 96  ? 7.899   -11.793 27.144  1.00 34.24  ? 98  ILE B CG1 1 
ATOM   2360 C CG2 . ILE B 1 96  ? 7.970   -12.351 29.638  1.00 34.56  ? 98  ILE B CG2 1 
ATOM   2361 C CD1 . ILE B 1 96  ? 6.407   -11.992 27.033  1.00 33.21  ? 98  ILE B CD1 1 
ATOM   2362 N N   . GLU B 1 97  ? 11.477  -12.921 30.267  1.00 42.10  ? 99  GLU B N   1 
ATOM   2363 C CA  . GLU B 1 97  ? 11.934  -13.762 31.380  1.00 46.18  ? 99  GLU B CA  1 
ATOM   2364 C C   . GLU B 1 97  ? 10.745  -14.148 32.286  1.00 47.17  ? 99  GLU B C   1 
ATOM   2365 O O   . GLU B 1 97  ? 9.787   -13.358 32.448  1.00 47.06  ? 99  GLU B O   1 
ATOM   2366 C CB  . GLU B 1 97  ? 13.004  -13.044 32.200  1.00 51.06  ? 99  GLU B CB  1 
ATOM   2367 C CG  . GLU B 1 97  ? 14.295  -12.813 31.429  1.00 60.89  ? 99  GLU B CG  1 
ATOM   2368 C CD  . GLU B 1 97  ? 15.442  -12.302 32.283  1.00 75.48  ? 99  GLU B CD  1 
ATOM   2369 O OE1 . GLU B 1 97  ? 16.533  -12.052 31.715  1.00 79.22  ? 99  GLU B OE1 1 
ATOM   2370 O OE2 . GLU B 1 97  ? 15.257  -12.154 33.517  1.00 79.84  ? 99  GLU B OE2 1 
ATOM   2371 N N   . PRO B 1 98  ? 10.795  -15.364 32.874  1.00 47.43  ? 100 PRO B N   1 
ATOM   2372 C CA  . PRO B 1 98  ? 9.694   -15.804 33.739  1.00 48.29  ? 100 PRO B CA  1 
ATOM   2373 C C   . PRO B 1 98  ? 9.742   -15.208 35.147  1.00 50.13  ? 100 PRO B C   1 
ATOM   2374 O O   . PRO B 1 98  ? 9.624   -15.939 36.122  1.00 51.59  ? 100 PRO B O   1 
ATOM   2375 C CB  . PRO B 1 98  ? 9.872   -17.320 33.738  1.00 48.37  ? 100 PRO B CB  1 
ATOM   2376 C CG  . PRO B 1 98  ? 11.337  -17.494 33.688  1.00 48.98  ? 100 PRO B CG  1 
ATOM   2377 C CD  . PRO B 1 98  ? 11.837  -16.408 32.773  1.00 47.20  ? 100 PRO B CD  1 
ATOM   2378 N N   . MET B 1 99  ? 9.898   -13.892 35.249  1.00 49.85  ? 101 MET B N   1 
ATOM   2379 C CA  . MET B 1 99  ? 9.954   -13.144 36.491  1.00 50.94  ? 101 MET B CA  1 
ATOM   2380 C C   . MET B 1 99  ? 9.003   -11.944 36.354  1.00 51.29  ? 101 MET B C   1 
ATOM   2381 O O   . MET B 1 99  ? 8.923   -11.306 35.294  1.00 49.85  ? 101 MET B O   1 
ATOM   2382 C CB  . MET B 1 99  ? 11.378  -12.619 36.732  1.00 53.37  ? 101 MET B CB  1 
ATOM   2383 C CG  . MET B 1 99  ? 12.463  -13.712 36.861  1.00 59.47  ? 101 MET B CG  1 
ATOM   2384 S SD  . MET B 1 99  ? 12.335  -14.708 38.377  1.00 74.79  ? 101 MET B SD  1 
ATOM   2385 C CE  . MET B 1 99  ? 13.991  -15.517 38.383  1.00 77.90  ? 101 MET B CE  1 
ATOM   2386 N N   . TRP B 1 100 ? 8.288   -11.628 37.431  1.00 53.05  ? 102 TRP B N   1 
ATOM   2387 C CA  . TRP B 1 100 ? 7.275   -10.564 37.394  1.00 54.86  ? 102 TRP B CA  1 
ATOM   2388 C C   . TRP B 1 100 ? 7.912   -9.172  37.172  1.00 54.33  ? 102 TRP B C   1 
ATOM   2389 O O   . TRP B 1 100 ? 7.221   -8.285  36.704  1.00 54.48  ? 102 TRP B O   1 
ATOM   2390 C CB  . TRP B 1 100 ? 6.333   -10.615 38.642  1.00 55.88  ? 102 TRP B CB  1 
ATOM   2391 C CG  . TRP B 1 100 ? 6.760   -9.822  39.845  1.00 57.30  ? 102 TRP B CG  1 
ATOM   2392 C CD1 . TRP B 1 100 ? 7.590   -10.233 40.847  1.00 58.88  ? 102 TRP B CD1 1 
ATOM   2393 C CD2 . TRP B 1 100 ? 6.334   -8.490  40.195  1.00 57.33  ? 102 TRP B CD2 1 
ATOM   2394 N NE1 . TRP B 1 100 ? 7.744   -9.223  41.778  1.00 59.41  ? 102 TRP B NE1 1 
ATOM   2395 C CE2 . TRP B 1 100 ? 6.975   -8.147  41.402  1.00 58.55  ? 102 TRP B CE2 1 
ATOM   2396 C CE3 . TRP B 1 100 ? 5.476   -7.555  39.599  1.00 57.74  ? 102 TRP B CE3 1 
ATOM   2397 C CZ2 . TRP B 1 100 ? 6.774   -6.917  42.029  1.00 59.07  ? 102 TRP B CZ2 1 
ATOM   2398 C CZ3 . TRP B 1 100 ? 5.266   -6.345  40.229  1.00 58.68  ? 102 TRP B CZ3 1 
ATOM   2399 C CH2 . TRP B 1 100 ? 5.906   -6.038  41.433  1.00 58.99  ? 102 TRP B CH2 1 
ATOM   2400 N N   . GLU B 1 101 ? 9.216   -8.994  37.482  1.00 53.36  ? 103 GLU B N   1 
ATOM   2401 C CA  . GLU B 1 101 ? 9.950   -7.752  37.266  1.00 52.85  ? 103 GLU B CA  1 
ATOM   2402 C C   . GLU B 1 101 ? 10.150  -7.410  35.789  1.00 51.51  ? 103 GLU B C   1 
ATOM   2403 O O   . GLU B 1 101 ? 10.431  -6.253  35.480  1.00 51.80  ? 103 GLU B O   1 
ATOM   2404 C CB  . GLU B 1 101 ? 11.328  -7.815  37.951  1.00 56.03  ? 103 GLU B CB  1 
ATOM   2405 C CG  . GLU B 1 101 ? 11.268  -7.966  39.473  1.00 61.97  ? 103 GLU B CG  1 
ATOM   2406 C CD  . GLU B 1 101 ? 11.264  -9.384  40.039  1.00 67.32  ? 103 GLU B CD  1 
ATOM   2407 O OE1 . GLU B 1 101 ? 10.865  -10.333 39.326  1.00 64.32  ? 103 GLU B OE1 1 
ATOM   2408 O OE2 . GLU B 1 101 ? 11.665  -9.539  41.216  1.00 71.97  ? 103 GLU B OE2 1 
ATOM   2409 N N   . ASP B 1 102 ? 10.010  -8.391  34.868  1.00 49.70  ? 104 ASP B N   1 
ATOM   2410 C CA  . ASP B 1 102 ? 10.126  -8.161  33.428  1.00 48.56  ? 104 ASP B CA  1 
ATOM   2411 C C   . ASP B 1 102 ? 9.113   -7.130  32.986  1.00 48.44  ? 104 ASP B C   1 
ATOM   2412 O O   . ASP B 1 102 ? 7.985   -7.123  33.484  1.00 47.86  ? 104 ASP B O   1 
ATOM   2413 C CB  . ASP B 1 102 ? 9.931   -9.482  32.660  1.00 49.40  ? 104 ASP B CB  1 
ATOM   2414 C CG  . ASP B 1 102 ? 10.178  -9.484  31.145  1.00 50.10  ? 104 ASP B CG  1 
ATOM   2415 O OD1 . ASP B 1 102 ? 9.379   -8.875  30.404  1.00 49.80  ? 104 ASP B OD1 1 
ATOM   2416 O OD2 . ASP B 1 102 ? 11.145  -10.116 30.707  1.00 50.34  ? 104 ASP B OD2 1 
ATOM   2417 N N   . GLU B 1 103 ? 9.523   -6.243  32.054  1.00 49.01  ? 105 GLU B N   1 
ATOM   2418 C CA  . GLU B 1 103 ? 8.644   -5.223  31.466  1.00 48.95  ? 105 GLU B CA  1 
ATOM   2419 C C   . GLU B 1 103 ? 7.284   -5.780  30.991  1.00 47.60  ? 105 GLU B C   1 
ATOM   2420 O O   . GLU B 1 103 ? 6.270   -5.088  31.139  1.00 47.72  ? 105 GLU B O   1 
ATOM   2421 C CB  . GLU B 1 103 ? 9.337   -4.520  30.285  1.00 51.90  ? 105 GLU B CB  1 
ATOM   2422 C CG  . GLU B 1 103 ? 9.235   -2.992  30.316  1.00 63.18  ? 105 GLU B CG  1 
ATOM   2423 C CD  . GLU B 1 103 ? 9.921   -2.325  31.498  1.00 75.91  ? 105 GLU B CD  1 
ATOM   2424 O OE1 . GLU B 1 103 ? 9.705   -1.105  31.689  1.00 79.23  ? 105 GLU B OE1 1 
ATOM   2425 O OE2 . GLU B 1 103 ? 10.667  -3.014  32.233  1.00 78.75  ? 105 GLU B OE2 1 
ATOM   2426 N N   . LYS B 1 104 ? 7.260   -7.018  30.442  1.00 45.03  ? 106 LYS B N   1 
ATOM   2427 C CA  . LYS B 1 104 ? 6.016   -7.647  29.990  1.00 43.41  ? 106 LYS B CA  1 
ATOM   2428 C C   . LYS B 1 104 ? 5.201   -8.320  31.066  1.00 41.89  ? 106 LYS B C   1 
ATOM   2429 O O   . LYS B 1 104 ? 4.098   -8.741  30.753  1.00 42.43  ? 106 LYS B O   1 
ATOM   2430 C CB  . LYS B 1 104 ? 6.297   -8.641  28.875  1.00 45.38  ? 106 LYS B CB  1 
ATOM   2431 C CG  . LYS B 1 104 ? 6.953   -7.999  27.671  1.00 51.37  ? 106 LYS B CG  1 
ATOM   2432 C CD  . LYS B 1 104 ? 6.087   -6.982  26.964  1.00 58.54  ? 106 LYS B CD  1 
ATOM   2433 C CE  . LYS B 1 104 ? 6.378   -7.052  25.482  1.00 65.36  ? 106 LYS B CE  1 
ATOM   2434 N NZ  . LYS B 1 104 ? 5.770   -5.936  24.731  1.00 69.96  ? 106 LYS B NZ  1 
ATOM   2435 N N   . ASN B 1 105 ? 5.692   -8.426  32.320  1.00 40.20  ? 107 ASN B N   1 
ATOM   2436 C CA  . ASN B 1 105 ? 4.942   -9.040  33.402  1.00 39.65  ? 107 ASN B CA  1 
ATOM   2437 C C   . ASN B 1 105 ? 4.613   -8.073  34.563  1.00 41.64  ? 107 ASN B C   1 
ATOM   2438 O O   . ASN B 1 105 ? 3.642   -8.318  35.315  1.00 40.84  ? 107 ASN B O   1 
ATOM   2439 C CB  . ASN B 1 105 ? 5.733   -10.196 33.951  1.00 39.17  ? 107 ASN B CB  1 
ATOM   2440 C CG  . ASN B 1 105 ? 5.962   -11.329 32.958  1.00 40.16  ? 107 ASN B CG  1 
ATOM   2441 O OD1 . ASN B 1 105 ? 5.085   -11.655 32.143  1.00 39.06  ? 107 ASN B OD1 1 
ATOM   2442 N ND2 . ASN B 1 105 ? 7.146   -11.952 33.008  1.00 39.49  ? 107 ASN B ND2 1 
ATOM   2443 N N   . LYS B 1 106 ? 5.410   -6.985  34.734  1.00 43.00  ? 108 LYS B N   1 
ATOM   2444 C CA  . LYS B 1 106 ? 5.275   -6.168  35.951  1.00 44.43  ? 108 LYS B CA  1 
ATOM   2445 C C   . LYS B 1 106 ? 3.902   -5.532  36.092  1.00 42.56  ? 108 LYS B C   1 
ATOM   2446 O O   . LYS B 1 106 ? 3.401   -5.463  37.198  1.00 41.93  ? 108 LYS B O   1 
ATOM   2447 C CB  . LYS B 1 106 ? 6.401   -5.132  36.124  1.00 49.94  ? 108 LYS B CB  1 
ATOM   2448 C CG  . LYS B 1 106 ? 6.583   -4.111  35.007  1.00 58.08  ? 108 LYS B CG  1 
ATOM   2449 C CD  . LYS B 1 106 ? 7.959   -3.468  35.171  1.00 64.90  ? 108 LYS B CD  1 
ATOM   2450 C CE  . LYS B 1 106 ? 8.143   -2.245  34.309  1.00 71.86  ? 108 LYS B CE  1 
ATOM   2451 N NZ  . LYS B 1 106 ? 9.547   -1.740  34.343  1.00 75.91  ? 108 LYS B NZ  1 
ATOM   2452 N N   . ARG B 1 107 ? 3.269   -5.139  34.984  1.00 41.84  ? 109 ARG B N   1 
ATOM   2453 C CA  . ARG B 1 107 ? 1.898   -4.612  35.023  1.00 42.01  ? 109 ARG B CA  1 
ATOM   2454 C C   . ARG B 1 107 ? 0.777   -5.687  34.902  1.00 40.69  ? 109 ARG B C   1 
ATOM   2455 O O   . ARG B 1 107 ? -0.402  -5.350  34.731  1.00 40.43  ? 109 ARG B O   1 
ATOM   2456 C CB  . ARG B 1 107 ? 1.767   -3.570  33.908  1.00 46.22  ? 109 ARG B CB  1 
ATOM   2457 C CG  . ARG B 1 107 ? 2.707   -2.351  34.145  1.00 52.88  ? 109 ARG B CG  1 
ATOM   2458 C CD  . ARG B 1 107 ? 2.681   -1.379  32.981  1.00 60.78  ? 109 ARG B CD  1 
ATOM   2459 N NE  . ARG B 1 107 ? 3.084   -2.010  31.721  1.00 69.98  ? 109 ARG B NE  1 
ATOM   2460 C CZ  . ARG B 1 107 ? 4.346   -2.244  31.347  1.00 75.96  ? 109 ARG B CZ  1 
ATOM   2461 N NH1 . ARG B 1 107 ? 5.363   -1.898  32.140  1.00 75.48  ? 109 ARG B NH1 1 
ATOM   2462 N NH2 . ARG B 1 107 ? 4.603   -2.829  30.177  1.00 77.71  ? 109 ARG B NH2 1 
ATOM   2463 N N   . GLY B 1 108 ? 1.153   -6.965  35.003  1.00 39.16  ? 110 GLY B N   1 
ATOM   2464 C CA  . GLY B 1 108 ? 0.313   -8.087  34.611  1.00 37.80  ? 110 GLY B CA  1 
ATOM   2465 C C   . GLY B 1 108 ? -0.131  -8.905  35.788  1.00 35.59  ? 110 GLY B C   1 
ATOM   2466 O O   . GLY B 1 108 ? -0.118  -8.426  36.930  1.00 35.60  ? 110 GLY B O   1 
ATOM   2467 N N   . GLY B 1 109 ? -0.532  -10.125 35.496  1.00 33.71  ? 111 GLY B N   1 
ATOM   2468 C CA  . GLY B 1 109 ? -0.913  -11.087 36.520  1.00 33.45  ? 111 GLY B CA  1 
ATOM   2469 C C   . GLY B 1 109 ? -1.159  -12.478 35.966  1.00 32.52  ? 111 GLY B C   1 
ATOM   2470 O O   . GLY B 1 109 ? -0.759  -12.778 34.848  1.00 31.80  ? 111 GLY B O   1 
ATOM   2471 N N   . ARG B 1 110 ? -1.847  -13.314 36.741  1.00 31.39  ? 112 ARG B N   1 
ATOM   2472 C CA  . ARG B 1 110 ? -1.995  -14.694 36.448  1.00 31.31  ? 112 ARG B CA  1 
ATOM   2473 C C   . ARG B 1 110 ? -3.388  -15.229 36.756  1.00 31.90  ? 112 ARG B C   1 
ATOM   2474 O O   . ARG B 1 110 ? -3.954  -14.896 37.805  1.00 32.53  ? 112 ARG B O   1 
ATOM   2475 C CB  . ARG B 1 110 ? -0.927  -15.489 37.208  1.00 32.23  ? 112 ARG B CB  1 
ATOM   2476 C CG  . ARG B 1 110 ? -1.147  -15.616 38.694  1.00 34.26  ? 112 ARG B CG  1 
ATOM   2477 C CD  . ARG B 1 110 ? -0.012  -16.344 39.348  1.00 39.63  ? 112 ARG B CD  1 
ATOM   2478 N NE  . ARG B 1 110 ? -0.218  -16.498 40.786  1.00 43.36  ? 112 ARG B NE  1 
ATOM   2479 C CZ  . ARG B 1 110 ? 0.605   -17.137 41.620  1.00 45.95  ? 112 ARG B CZ  1 
ATOM   2480 N NH1 . ARG B 1 110 ? 0.324   -17.211 42.911  1.00 46.28  ? 112 ARG B NH1 1 
ATOM   2481 N NH2 . ARG B 1 110 ? 1.713   -17.698 41.172  1.00 46.91  ? 112 ARG B NH2 1 
ATOM   2482 N N   . TRP B 1 111 ? -3.942  -16.081 35.842  1.00 31.65  ? 113 TRP B N   1 
ATOM   2483 C CA  . TRP B 1 111 ? -5.044  -16.986 36.171  1.00 33.44  ? 113 TRP B CA  1 
ATOM   2484 C C   . TRP B 1 111 ? -4.470  -18.152 36.916  1.00 34.29  ? 113 TRP B C   1 
ATOM   2485 O O   . TRP B 1 111 ? -3.624  -18.822 36.362  1.00 34.83  ? 113 TRP B O   1 
ATOM   2486 C CB  . TRP B 1 111 ? -5.819  -17.470 34.927  1.00 33.30  ? 113 TRP B CB  1 
ATOM   2487 C CG  . TRP B 1 111 ? -6.778  -16.447 34.441  1.00 33.66  ? 113 TRP B CG  1 
ATOM   2488 C CD1 . TRP B 1 111 ? -6.655  -15.642 33.343  1.00 34.47  ? 113 TRP B CD1 1 
ATOM   2489 C CD2 . TRP B 1 111 ? -7.969  -16.033 35.111  1.00 34.61  ? 113 TRP B CD2 1 
ATOM   2490 N NE1 . TRP B 1 111 ? -7.721  -14.772 33.276  1.00 34.83  ? 113 TRP B NE1 1 
ATOM   2491 C CE2 . TRP B 1 111 ? -8.552  -15.010 34.339  1.00 35.00  ? 113 TRP B CE2 1 
ATOM   2492 C CE3 . TRP B 1 111 ? -8.636  -16.474 36.268  1.00 35.89  ? 113 TRP B CE3 1 
ATOM   2493 C CZ2 . TRP B 1 111 ? -9.740  -14.404 34.699  1.00 36.74  ? 113 TRP B CZ2 1 
ATOM   2494 C CZ3 . TRP B 1 111 ? -9.824  -15.863 36.612  1.00 37.01  ? 113 TRP B CZ3 1 
ATOM   2495 C CH2 . TRP B 1 111 ? -10.348 -14.834 35.844  1.00 37.46  ? 113 TRP B CH2 1 
ATOM   2496 N N   . LEU B 1 112 ? -4.888  -18.405 38.161  1.00 35.46  ? 114 LEU B N   1 
ATOM   2497 C CA  . LEU B 1 112 ? -4.238  -19.442 38.978  1.00 37.65  ? 114 LEU B CA  1 
ATOM   2498 C C   . LEU B 1 112 ? -5.156  -20.648 39.219  1.00 39.05  ? 114 LEU B C   1 
ATOM   2499 O O   . LEU B 1 112 ? -6.321  -20.485 39.585  1.00 40.09  ? 114 LEU B O   1 
ATOM   2500 C CB  . LEU B 1 112 ? -3.702  -18.866 40.292  1.00 37.77  ? 114 LEU B CB  1 
ATOM   2501 C CG  . LEU B 1 112 ? -3.233  -19.861 41.366  1.00 38.43  ? 114 LEU B CG  1 
ATOM   2502 C CD1 . LEU B 1 112 ? -1.914  -20.430 41.029  1.00 38.47  ? 114 LEU B CD1 1 
ATOM   2503 C CD2 . LEU B 1 112 ? -3.089  -19.173 42.710  1.00 38.64  ? 114 LEU B CD2 1 
ATOM   2504 N N   . ILE B 1 113 ? -4.600  -21.853 39.006  1.00 38.40  ? 115 ILE B N   1 
ATOM   2505 C CA  . ILE B 1 113 ? -5.203  -23.140 39.278  1.00 39.41  ? 115 ILE B CA  1 
ATOM   2506 C C   . ILE B 1 113 ? -4.419  -23.762 40.412  1.00 41.25  ? 115 ILE B C   1 
ATOM   2507 O O   . ILE B 1 113 ? -3.264  -24.063 40.219  1.00 39.55  ? 115 ILE B O   1 
ATOM   2508 C CB  . ILE B 1 113 ? -5.070  -24.070 38.020  1.00 40.21  ? 115 ILE B CB  1 
ATOM   2509 C CG1 . ILE B 1 113 ? -5.458  -23.352 36.685  1.00 39.69  ? 115 ILE B CG1 1 
ATOM   2510 C CG2 . ILE B 1 113 ? -5.805  -25.375 38.209  1.00 41.14  ? 115 ILE B CG2 1 
ATOM   2511 C CD1 . ILE B 1 113 ? -6.756  -22.721 36.652  1.00 38.94  ? 115 ILE B CD1 1 
ATOM   2512 N N   . THR B 1 114 ? -5.029  -23.972 41.580  1.00 45.28  ? 116 THR B N   1 
ATOM   2513 C CA  . THR B 1 114 ? -4.342  -24.607 42.704  1.00 48.46  ? 116 THR B CA  1 
ATOM   2514 C C   . THR B 1 114 ? -4.829  -26.014 42.837  1.00 51.53  ? 116 THR B C   1 
ATOM   2515 O O   . THR B 1 114 ? -6.032  -26.240 42.920  1.00 52.01  ? 116 THR B O   1 
ATOM   2516 C CB  . THR B 1 114 ? -4.514  -23.844 44.027  1.00 50.59  ? 116 THR B CB  1 
ATOM   2517 O OG1 . THR B 1 114 ? -4.348  -22.437 43.801  1.00 51.39  ? 116 THR B OG1 1 
ATOM   2518 C CG2 . THR B 1 114 ? -3.471  -24.327 45.117  1.00 52.62  ? 116 THR B CG2 1 
ATOM   2519 N N   . LEU B 1 115 ? -3.897  -26.961 42.876  1.00 53.58  ? 117 LEU B N   1 
ATOM   2520 C CA  . LEU B 1 115 ? -4.204  -28.369 42.936  1.00 55.93  ? 117 LEU B CA  1 
ATOM   2521 C C   . LEU B 1 115 ? -3.883  -28.895 44.346  1.00 59.48  ? 117 LEU B C   1 
ATOM   2522 O O   . LEU B 1 115 ? -2.792  -28.634 44.854  1.00 60.57  ? 117 LEU B O   1 
ATOM   2523 C CB  . LEU B 1 115 ? -3.370  -29.104 41.887  1.00 55.50  ? 117 LEU B CB  1 
ATOM   2524 C CG  . LEU B 1 115 ? -3.498  -28.641 40.433  1.00 57.07  ? 117 LEU B CG  1 
ATOM   2525 C CD1 . LEU B 1 115 ? -2.771  -29.603 39.515  1.00 57.81  ? 117 LEU B CD1 1 
ATOM   2526 C CD2 . LEU B 1 115 ? -4.951  -28.564 39.984  1.00 57.54  ? 117 LEU B CD2 1 
ATOM   2527 N N   . ASN B 1 116 ? -4.815  -29.624 44.970  1.00 60.73  ? 118 ASN B N   1 
ATOM   2528 C CA  . ASN B 1 116 ? -4.543  -30.244 46.267  1.00 63.77  ? 118 ASN B CA  1 
ATOM   2529 C C   . ASN B 1 116 ? -3.546  -31.432 46.137  1.00 65.80  ? 118 ASN B C   1 
ATOM   2530 O O   . ASN B 1 116 ? -3.136  -31.789 45.034  1.00 66.45  ? 118 ASN B O   1 
ATOM   2531 C CB  . ASN B 1 116 ? -5.857  -30.620 47.017  1.00 65.31  ? 118 ASN B CB  1 
ATOM   2532 C CG  . ASN B 1 116 ? -6.694  -31.734 46.442  1.00 70.32  ? 118 ASN B CG  1 
ATOM   2533 O OD1 . ASN B 1 116 ? -6.219  -32.602 45.701  1.00 70.35  ? 118 ASN B OD1 1 
ATOM   2534 N ND2 . ASN B 1 116 ? -7.991  -31.737 46.798  1.00 72.92  ? 118 ASN B ND2 1 
ATOM   2535 N N   . LYS B 1 117 ? -3.155  -32.007 47.259  1.00 66.86  ? 119 LYS B N   1 
ATOM   2536 C CA  . LYS B 1 117 ? -2.170  -33.083 47.339  1.00 68.58  ? 119 LYS B CA  1 
ATOM   2537 C C   . LYS B 1 117 ? -2.608  -34.305 46.537  1.00 69.31  ? 119 LYS B C   1 
ATOM   2538 O O   . LYS B 1 117 ? -1.786  -34.906 45.860  1.00 69.03  ? 119 LYS B O   1 
ATOM   2539 C CB  . LYS B 1 117 ? -1.942  -33.489 48.812  1.00 71.78  ? 119 LYS B CB  1 
ATOM   2540 C CG  . LYS B 1 117 ? -1.344  -32.390 49.719  1.00 78.53  ? 119 LYS B CG  1 
ATOM   2541 C CD  . LYS B 1 117 ? -2.424  -31.516 50.445  1.00 84.23  ? 119 LYS B CD  1 
ATOM   2542 C CE  . LYS B 1 117 ? -1.945  -30.925 51.762  1.00 88.25  ? 119 LYS B CE  1 
ATOM   2543 N NZ  . LYS B 1 117 ? -2.518  -29.562 51.995  1.00 90.66  ? 119 LYS B NZ  1 
ATOM   2544 N N   . GLN B 1 118 ? -3.893  -34.668 46.633  1.00 70.05  ? 120 GLN B N   1 
ATOM   2545 C CA  . GLN B 1 118 ? -4.525  -35.725 45.828  1.00 71.30  ? 120 GLN B CA  1 
ATOM   2546 C C   . GLN B 1 118 ? -4.359  -35.480 44.330  1.00 71.29  ? 120 GLN B C   1 
ATOM   2547 O O   . GLN B 1 118 ? -3.952  -36.379 43.593  1.00 71.36  ? 120 GLN B O   1 
ATOM   2548 C CB  . GLN B 1 118 ? -6.031  -35.813 46.152  1.00 74.58  ? 120 GLN B CB  1 
ATOM   2549 C CG  . GLN B 1 118 ? -6.325  -36.499 47.472  1.00 81.58  ? 120 GLN B CG  1 
ATOM   2550 C CD  . GLN B 1 118 ? -7.625  -36.047 48.110  1.00 89.78  ? 120 GLN B CD  1 
ATOM   2551 O OE1 . GLN B 1 118 ? -7.837  -34.864 48.475  1.00 91.95  ? 120 GLN B OE1 1 
ATOM   2552 N NE2 . GLN B 1 118 ? -8.509  -36.992 48.260  1.00 91.50  ? 120 GLN B NE2 1 
ATOM   2553 N N   . GLN B 1 119 ? -4.669  -34.251 43.886  1.00 70.82  ? 121 GLN B N   1 
ATOM   2554 C CA  . GLN B 1 119 ? -4.716  -33.907 42.475  1.00 70.49  ? 121 GLN B CA  1 
ATOM   2555 C C   . GLN B 1 119 ? -3.360  -33.801 41.812  1.00 69.56  ? 121 GLN B C   1 
ATOM   2556 O O   . GLN B 1 119 ? -3.323  -33.614 40.617  1.00 69.76  ? 121 GLN B O   1 
ATOM   2557 C CB  . GLN B 1 119 ? -5.464  -32.604 42.277  1.00 72.37  ? 121 GLN B CB  1 
ATOM   2558 C CG  . GLN B 1 119 ? -6.882  -32.616 42.755  1.00 76.97  ? 121 GLN B CG  1 
ATOM   2559 C CD  . GLN B 1 119 ? -7.363  -31.206 42.649  1.00 82.95  ? 121 GLN B CD  1 
ATOM   2560 O OE1 . GLN B 1 119 ? -7.179  -30.389 43.548  1.00 83.82  ? 121 GLN B OE1 1 
ATOM   2561 N NE2 . GLN B 1 119 ? -7.963  -30.871 41.548  1.00 84.75  ? 121 GLN B NE2 1 
ATOM   2562 N N   . ARG B 1 120 ? -2.248  -33.891 42.559  1.00 68.41  ? 122 ARG B N   1 
ATOM   2563 C CA  . ARG B 1 120 ? -0.905  -34.046 41.991  1.00 67.26  ? 122 ARG B CA  1 
ATOM   2564 C C   . ARG B 1 120 ? -0.865  -35.298 41.087  1.00 66.68  ? 122 ARG B C   1 
ATOM   2565 O O   . ARG B 1 120 ? -0.498  -35.231 39.917  1.00 66.80  ? 122 ARG B O   1 
ATOM   2566 C CB  . ARG B 1 120 ? 0.121   -34.104 43.147  1.00 68.10  ? 122 ARG B CB  1 
ATOM   2567 C CG  . ARG B 1 120 ? 1.346   -34.992 42.997  1.00 70.05  ? 122 ARG B CG  1 
ATOM   2568 C CD  . ARG B 1 120 ? 2.445   -34.314 42.260  1.00 71.86  ? 122 ARG B CD  1 
ATOM   2569 N NE  . ARG B 1 120 ? 2.910   -33.097 42.931  1.00 74.17  ? 122 ARG B NE  1 
ATOM   2570 C CZ  . ARG B 1 120 ? 3.686   -33.054 44.012  1.00 76.36  ? 122 ARG B CZ  1 
ATOM   2571 N NH1 . ARG B 1 120 ? 4.041   -31.889 44.532  1.00 75.49  ? 122 ARG B NH1 1 
ATOM   2572 N NH2 . ARG B 1 120 ? 4.109   -34.179 44.585  1.00 77.57  ? 122 ARG B NH2 1 
ATOM   2573 N N   . ARG B 1 121 ? -1.260  -36.433 41.649  1.00 66.10  ? 123 ARG B N   1 
ATOM   2574 C CA  . ARG B 1 121 ? -1.234  -37.704 40.947  1.00 66.40  ? 123 ARG B CA  1 
ATOM   2575 C C   . ARG B 1 121 ? -2.296  -37.743 39.823  1.00 63.73  ? 123 ARG B C   1 
ATOM   2576 O O   . ARG B 1 121 ? -1.981  -38.168 38.711  1.00 64.32  ? 123 ARG B O   1 
ATOM   2577 C CB  . ARG B 1 121 ? -1.354  -38.866 41.945  1.00 70.15  ? 123 ARG B CB  1 
ATOM   2578 C CG  . ARG B 1 121 ? -0.084  -39.097 42.814  1.00 76.75  ? 123 ARG B CG  1 
ATOM   2579 C CD  . ARG B 1 121 ? -0.133  -40.378 43.687  1.00 84.31  ? 123 ARG B CD  1 
ATOM   2580 N NE  . ARG B 1 121 ? -1.192  -41.283 43.237  1.00 89.53  ? 123 ARG B NE  1 
ATOM   2581 C CZ  . ARG B 1 121 ? -1.049  -42.336 42.448  1.00 92.28  ? 123 ARG B CZ  1 
ATOM   2582 N NH1 . ARG B 1 121 ? -2.105  -43.054 42.103  1.00 91.93  ? 123 ARG B NH1 1 
ATOM   2583 N NH2 . ARG B 1 121 ? 0.151   -42.688 42.005  1.00 92.39  ? 123 ARG B NH2 1 
ATOM   2584 N N   . SER B 1 122 ? -3.512  -37.269 40.086  1.00 60.54  ? 124 SER B N   1 
ATOM   2585 C CA  . SER B 1 122 ? -4.590  -37.252 39.097  1.00 59.11  ? 124 SER B CA  1 
ATOM   2586 C C   . SER B 1 122 ? -4.532  -36.157 37.984  1.00 56.11  ? 124 SER B C   1 
ATOM   2587 O O   . SER B 1 122 ? -4.750  -36.490 36.817  1.00 55.73  ? 124 SER B O   1 
ATOM   2588 C CB  . SER B 1 122 ? -5.927  -37.143 39.822  1.00 61.76  ? 124 SER B CB  1 
ATOM   2589 O OG  . SER B 1 122 ? -5.928  -35.981 40.632  1.00 66.04  ? 124 SER B OG  1 
ATOM   2590 N N   . ASP B 1 123 ? -4.257  -34.870 38.322  1.00 53.67  ? 125 ASP B N   1 
ATOM   2591 C CA  . ASP B 1 123 ? -4.479  -33.732 37.392  1.00 51.24  ? 125 ASP B CA  1 
ATOM   2592 C C   . ASP B 1 123 ? -3.249  -32.898 36.983  1.00 47.14  ? 125 ASP B C   1 
ATOM   2593 O O   . ASP B 1 123 ? -3.392  -32.118 36.056  1.00 46.49  ? 125 ASP B O   1 
ATOM   2594 C CB  . ASP B 1 123 ? -5.513  -32.760 37.934  1.00 53.61  ? 125 ASP B CB  1 
ATOM   2595 C CG  . ASP B 1 123 ? -6.867  -33.353 38.223  1.00 59.64  ? 125 ASP B CG  1 
ATOM   2596 O OD1 . ASP B 1 123 ? -7.425  -34.016 37.323  1.00 60.39  ? 125 ASP B OD1 1 
ATOM   2597 O OD2 . ASP B 1 123 ? -7.382  -33.137 39.350  1.00 62.49  ? 125 ASP B OD2 1 
ATOM   2598 N N   . LEU B 1 124 ? -2.067  -33.033 37.632  1.00 43.68  ? 126 LEU B N   1 
ATOM   2599 C CA  . LEU B 1 124 ? -0.922  -32.168 37.339  1.00 40.76  ? 126 LEU B CA  1 
ATOM   2600 C C   . LEU B 1 124 ? -0.526  -32.234 35.856  1.00 39.04  ? 126 LEU B C   1 
ATOM   2601 O O   . LEU B 1 124 ? -0.509  -31.195 35.159  1.00 37.04  ? 126 LEU B O   1 
ATOM   2602 C CB  . LEU B 1 124 ? 0.262   -32.543 38.248  1.00 40.05  ? 126 LEU B CB  1 
ATOM   2603 C CG  . LEU B 1 124 ? 1.554   -31.677 38.215  1.00 41.84  ? 126 LEU B CG  1 
ATOM   2604 C CD1 . LEU B 1 124 ? 1.286   -30.254 38.462  1.00 41.21  ? 126 LEU B CD1 1 
ATOM   2605 C CD2 . LEU B 1 124 ? 2.534   -32.121 39.310  1.00 44.45  ? 126 LEU B CD2 1 
ATOM   2606 N N   . ASN B 1 125 ? -0.223  -33.460 35.369  1.00 38.04  ? 127 ASN B N   1 
ATOM   2607 C CA  . ASN B 1 125 ? 0.296   -33.630 34.019  1.00 37.16  ? 127 ASN B CA  1 
ATOM   2608 C C   . ASN B 1 125 ? -0.754  -33.257 32.987  1.00 35.36  ? 127 ASN B C   1 
ATOM   2609 O O   . ASN B 1 125 ? -0.450  -32.582 32.019  1.00 35.86  ? 127 ASN B O   1 
ATOM   2610 C CB  . ASN B 1 125 ? 0.792   -35.059 33.824  1.00 40.10  ? 127 ASN B CB  1 
ATOM   2611 C CG  . ASN B 1 125 ? 1.958   -35.378 34.725  1.00 47.48  ? 127 ASN B CG  1 
ATOM   2612 O OD1 . ASN B 1 125 ? 2.884   -34.569 34.860  1.00 52.61  ? 127 ASN B OD1 1 
ATOM   2613 N ND2 . ASN B 1 125 ? 1.968   -36.530 35.370  1.00 47.16  ? 127 ASN B ND2 1 
ATOM   2614 N N   . ARG B 1 126 ? -1.984  -33.690 33.185  1.00 33.90  ? 128 ARG B N   1 
ATOM   2615 C CA  . ARG B 1 126 ? -3.108  -33.351 32.299  1.00 33.13  ? 128 ARG B CA  1 
ATOM   2616 C C   . ARG B 1 126 ? -3.328  -31.809 32.236  1.00 30.76  ? 128 ARG B C   1 
ATOM   2617 O O   . ARG B 1 126 ? -3.369  -31.253 31.165  1.00 30.30  ? 128 ARG B O   1 
ATOM   2618 C CB  . ARG B 1 126 ? -4.408  -34.073 32.820  1.00 34.99  ? 128 ARG B CB  1 
ATOM   2619 C CG  . ARG B 1 126 ? -5.707  -33.684 32.110  1.00 38.21  ? 128 ARG B CG  1 
ATOM   2620 C CD  . ARG B 1 126 ? -5.615  -33.812 30.603  1.00 40.53  ? 128 ARG B CD  1 
ATOM   2621 N NE  . ARG B 1 126 ? -5.368  -35.194 30.213  1.00 43.52  ? 128 ARG B NE  1 
ATOM   2622 C CZ  . ARG B 1 126 ? -4.978  -35.599 29.006  1.00 44.49  ? 128 ARG B CZ  1 
ATOM   2623 N NH1 . ARG B 1 126 ? -4.779  -34.716 28.033  1.00 44.17  ? 128 ARG B NH1 1 
ATOM   2624 N NH2 . ARG B 1 126 ? -4.782  -36.896 28.764  1.00 41.16  ? 128 ARG B NH2 1 
ATOM   2625 N N   . PHE B 1 127 ? -3.471  -31.151 33.367  1.00 30.93  ? 129 PHE B N   1 
ATOM   2626 C CA  . PHE B 1 127 ? -3.730  -29.707 33.406  1.00 32.27  ? 129 PHE B CA  1 
ATOM   2627 C C   . PHE B 1 127 ? -2.594  -28.914 32.835  1.00 31.58  ? 129 PHE B C   1 
ATOM   2628 O O   . PHE B 1 127 ? -2.833  -27.907 32.181  1.00 31.35  ? 129 PHE B O   1 
ATOM   2629 C CB  . PHE B 1 127 ? -4.011  -29.207 34.799  1.00 33.45  ? 129 PHE B CB  1 
ATOM   2630 C CG  . PHE B 1 127 ? -5.416  -29.433 35.306  1.00 37.51  ? 129 PHE B CG  1 
ATOM   2631 C CD1 . PHE B 1 127 ? -6.168  -30.518 34.878  1.00 39.15  ? 129 PHE B CD1 1 
ATOM   2632 C CD2 . PHE B 1 127 ? -5.979  -28.575 36.228  1.00 39.76  ? 129 PHE B CD2 1 
ATOM   2633 C CE1 . PHE B 1 127 ? -7.459  -30.726 35.365  1.00 40.09  ? 129 PHE B CE1 1 
ATOM   2634 C CE2 . PHE B 1 127 ? -7.259  -28.800 36.728  1.00 40.59  ? 129 PHE B CE2 1 
ATOM   2635 C CZ  . PHE B 1 127 ? -7.993  -29.869 36.290  1.00 40.40  ? 129 PHE B CZ  1 
ATOM   2636 N N   . TRP B 1 128 ? -1.354  -29.366 33.066  1.00 30.09  ? 130 TRP B N   1 
ATOM   2637 C CA  . TRP B 1 128 ? -0.194  -28.680 32.549  1.00 28.69  ? 130 TRP B CA  1 
ATOM   2638 C C   . TRP B 1 128 ? -0.107  -28.793 31.043  1.00 27.43  ? 130 TRP B C   1 
ATOM   2639 O O   . TRP B 1 128 ? 0.135   -27.787 30.380  1.00 26.68  ? 130 TRP B O   1 
ATOM   2640 C CB  . TRP B 1 128 ? 1.094   -29.229 33.200  1.00 27.55  ? 130 TRP B CB  1 
ATOM   2641 C CG  . TRP B 1 128 ? 2.363   -28.558 32.750  1.00 25.31  ? 130 TRP B CG  1 
ATOM   2642 C CD1 . TRP B 1 128 ? 3.469   -29.166 32.235  1.00 25.50  ? 130 TRP B CD1 1 
ATOM   2643 C CD2 . TRP B 1 128 ? 2.669   -27.161 32.819  1.00 24.77  ? 130 TRP B CD2 1 
ATOM   2644 N NE1 . TRP B 1 128 ? 4.447   -28.244 31.987  1.00 25.61  ? 130 TRP B NE1 1 
ATOM   2645 C CE2 . TRP B 1 128 ? 3.980   -26.994 32.331  1.00 25.63  ? 130 TRP B CE2 1 
ATOM   2646 C CE3 . TRP B 1 128 ? 1.961   -26.025 33.249  1.00 25.25  ? 130 TRP B CE3 1 
ATOM   2647 C CZ2 . TRP B 1 128 ? 4.596   -25.732 32.246  1.00 26.03  ? 130 TRP B CZ2 1 
ATOM   2648 C CZ3 . TRP B 1 128 ? 2.553   -24.789 33.127  1.00 25.92  ? 130 TRP B CZ3 1 
ATOM   2649 C CH2 . TRP B 1 128 ? 3.870   -24.648 32.657  1.00 25.92  ? 130 TRP B CH2 1 
ATOM   2650 N N   . LEU B 1 129 ? -0.304  -30.009 30.485  1.00 27.49  ? 131 LEU B N   1 
ATOM   2651 C CA  . LEU B 1 129 ? -0.373  -30.196 29.039  1.00 27.66  ? 131 LEU B CA  1 
ATOM   2652 C C   . LEU B 1 129 ? -1.470  -29.318 28.435  1.00 28.04  ? 131 LEU B C   1 
ATOM   2653 O O   . LEU B 1 129 ? -1.208  -28.612 27.463  1.00 28.90  ? 131 LEU B O   1 
ATOM   2654 C CB  . LEU B 1 129 ? -0.635  -31.664 28.670  1.00 29.18  ? 131 LEU B CB  1 
ATOM   2655 C CG  . LEU B 1 129 ? -0.808  -31.954 27.161  1.00 30.55  ? 131 LEU B CG  1 
ATOM   2656 C CD1 . LEU B 1 129 ? 0.402   -31.582 26.421  1.00 32.95  ? 131 LEU B CD1 1 
ATOM   2657 C CD2 . LEU B 1 129 ? -1.094  -33.349 26.921  1.00 31.21  ? 131 LEU B CD2 1 
ATOM   2658 N N   . GLU B 1 130 ? -2.687  -29.332 29.009  1.00 28.52  ? 132 GLU B N   1 
ATOM   2659 C CA  . GLU B 1 130 ? -3.776  -28.524 28.442  1.00 29.28  ? 132 GLU B CA  1 
ATOM   2660 C C   . GLU B 1 130 ? -3.396  -27.030 28.430  1.00 30.29  ? 132 GLU B C   1 
ATOM   2661 O O   . GLU B 1 130 ? -3.693  -26.344 27.457  1.00 31.15  ? 132 GLU B O   1 
ATOM   2662 C CB  . GLU B 1 130 ? -5.136  -28.772 29.119  1.00 30.90  ? 132 GLU B CB  1 
ATOM   2663 C CG  . GLU B 1 130 ? -5.606  -30.222 29.114  1.00 36.55  ? 132 GLU B CG  1 
ATOM   2664 C CD  . GLU B 1 130 ? -5.786  -30.849 27.741  1.00 39.78  ? 132 GLU B CD  1 
ATOM   2665 O OE1 . GLU B 1 130 ? -6.019  -30.106 26.756  1.00 36.51  ? 132 GLU B OE1 1 
ATOM   2666 O OE2 . GLU B 1 130 ? -5.681  -32.094 27.658  1.00 39.99  ? 132 GLU B OE2 1 
ATOM   2667 N N   . THR B 1 131 ? -2.714  -26.548 29.499  1.00 30.33  ? 133 THR B N   1 
ATOM   2668 C CA  . THR B 1 131 ? -2.174  -25.170 29.569  1.00 30.25  ? 133 THR B CA  1 
ATOM   2669 C C   . THR B 1 131 ? -1.193  -24.904 28.428  1.00 29.67  ? 133 THR B C   1 
ATOM   2670 O O   . THR B 1 131 ? -1.317  -23.906 27.729  1.00 29.78  ? 133 THR B O   1 
ATOM   2671 C CB  . THR B 1 131 ? -1.516  -24.934 30.919  1.00 29.81  ? 133 THR B CB  1 
ATOM   2672 O OG1 . THR B 1 131 ? -2.483  -25.162 31.923  1.00 30.42  ? 133 THR B OG1 1 
ATOM   2673 C CG2 . THR B 1 131 ? -0.970  -23.580 31.047  1.00 28.85  ? 133 THR B CG2 1 
ATOM   2674 N N   . LEU B 1 132 ? -0.222  -25.807 28.235  1.00 30.14  ? 134 LEU B N   1 
ATOM   2675 C CA  . LEU B 1 132 ? 0.774   -25.706 27.166  1.00 29.76  ? 134 LEU B CA  1 
ATOM   2676 C C   . LEU B 1 132 ? 0.103   -25.594 25.789  1.00 28.99  ? 134 LEU B C   1 
ATOM   2677 O O   . LEU B 1 132 ? 0.510   -24.767 24.988  1.00 27.10  ? 134 LEU B O   1 
ATOM   2678 C CB  . LEU B 1 132 ? 1.712   -26.910 27.191  1.00 29.90  ? 134 LEU B CB  1 
ATOM   2679 C CG  . LEU B 1 132 ? 2.592   -27.086 28.439  1.00 30.14  ? 134 LEU B CG  1 
ATOM   2680 C CD1 . LEU B 1 132 ? 3.442   -28.319 28.323  1.00 29.01  ? 134 LEU B CD1 1 
ATOM   2681 C CD2 . LEU B 1 132 ? 3.426   -25.862 28.726  1.00 30.48  ? 134 LEU B CD2 1 
ATOM   2682 N N   . LEU B 1 133 ? -0.921  -26.394 25.528  1.00 29.53  ? 135 LEU B N   1 
ATOM   2683 C CA  . LEU B 1 133 ? -1.592  -26.355 24.218  1.00 30.34  ? 135 LEU B CA  1 
ATOM   2684 C C   . LEU B 1 133 ? -2.356  -25.055 23.994  1.00 31.44  ? 135 LEU B C   1 
ATOM   2685 O O   . LEU B 1 133 ? -2.433  -24.587 22.873  1.00 32.34  ? 135 LEU B O   1 
ATOM   2686 C CB  . LEU B 1 133 ? -2.504  -27.554 24.011  1.00 30.44  ? 135 LEU B CB  1 
ATOM   2687 C CG  . LEU B 1 133 ? -1.871  -28.931 24.201  1.00 32.18  ? 135 LEU B CG  1 
ATOM   2688 C CD1 . LEU B 1 133 ? -2.917  -30.014 24.006  1.00 32.78  ? 135 LEU B CD1 1 
ATOM   2689 C CD2 . LEU B 1 133 ? -0.693  -29.171 23.280  1.00 32.04  ? 135 LEU B CD2 1 
ATOM   2690 N N   . CYS B 1 134 ? -2.901  -24.468 25.050  1.00 30.98  ? 136 CYS B N   1 
ATOM   2691 C CA  . CYS B 1 134 ? -3.579  -23.201 24.977  1.00 31.16  ? 136 CYS B CA  1 
ATOM   2692 C C   . CYS B 1 134 ? -2.589  -22.101 24.574  1.00 30.48  ? 136 CYS B C   1 
ATOM   2693 O O   . CYS B 1 134 ? -2.970  -21.187 23.842  1.00 31.00  ? 136 CYS B O   1 
ATOM   2694 C CB  . CYS B 1 134 ? -4.236  -22.853 26.313  1.00 33.76  ? 136 CYS B CB  1 
ATOM   2695 S SG  . CYS B 1 134 ? -5.799  -23.694 26.625  1.00 36.85  ? 136 CYS B SG  1 
ATOM   2696 N N   . LEU B 1 135 ? -1.335  -22.172 25.073  1.00 27.90  ? 137 LEU B N   1 
ATOM   2697 C CA  . LEU B 1 135 ? -0.316  -21.202 24.738  1.00 26.68  ? 137 LEU B CA  1 
ATOM   2698 C C   . LEU B 1 135 ? 0.161   -21.368 23.287  1.00 28.44  ? 137 LEU B C   1 
ATOM   2699 O O   . LEU B 1 135 ? 0.019   -20.432 22.478  1.00 28.03  ? 137 LEU B O   1 
ATOM   2700 C CB  . LEU B 1 135 ? 0.894   -21.293 25.700  1.00 24.91  ? 137 LEU B CB  1 
ATOM   2701 C CG  . LEU B 1 135 ? 0.932   -20.411 26.935  1.00 25.25  ? 137 LEU B CG  1 
ATOM   2702 C CD1 . LEU B 1 135 ? -0.377  -20.401 27.692  1.00 25.74  ? 137 LEU B CD1 1 
ATOM   2703 C CD2 . LEU B 1 135 ? 2.117   -20.832 27.806  1.00 26.82  ? 137 LEU B CD2 1 
ATOM   2704 N N   . ILE B 1 136 ? 0.741   -22.534 22.957  1.00 29.77  ? 138 ILE B N   1 
ATOM   2705 C CA  . ILE B 1 136 ? 1.346   -22.727 21.635  1.00 31.62  ? 138 ILE B CA  1 
ATOM   2706 C C   . ILE B 1 136 ? 0.293   -22.659 20.536  1.00 33.61  ? 138 ILE B C   1 
ATOM   2707 O O   . ILE B 1 136 ? 0.618   -22.217 19.447  1.00 33.57  ? 138 ILE B O   1 
ATOM   2708 C CB  . ILE B 1 136 ? 2.250   -23.983 21.526  1.00 32.03  ? 138 ILE B CB  1 
ATOM   2709 C CG1 . ILE B 1 136 ? 1.432   -25.284 21.628  1.00 33.62  ? 138 ILE B CG1 1 
ATOM   2710 C CG2 . ILE B 1 136 ? 3.379   -23.916 22.590  1.00 31.54  ? 138 ILE B CG2 1 
ATOM   2711 C CD1 . ILE B 1 136 ? 2.080   -26.443 21.353  1.00 33.94  ? 138 ILE B CD1 1 
ATOM   2712 N N   . GLY B 1 137 ? -0.937  -23.070 20.816  1.00 35.59  ? 139 GLY B N   1 
ATOM   2713 C CA  . GLY B 1 137 ? -2.009  -23.047 19.814  1.00 38.12  ? 139 GLY B CA  1 
ATOM   2714 C C   . GLY B 1 137 ? -2.711  -21.705 19.627  1.00 38.56  ? 139 GLY B C   1 
ATOM   2715 O O   . GLY B 1 137 ? -3.553  -21.584 18.735  1.00 39.12  ? 139 GLY B O   1 
ATOM   2716 N N   . GLU B 1 138 ? -2.386  -20.695 20.455  1.00 37.58  ? 140 GLU B N   1 
ATOM   2717 C CA  . GLU B 1 138 ? -3.012  -19.368 20.411  1.00 37.41  ? 140 GLU B CA  1 
ATOM   2718 C C   . GLU B 1 138 ? -4.523  -19.432 20.602  1.00 38.06  ? 140 GLU B C   1 
ATOM   2719 O O   . GLU B 1 138 ? -5.304  -18.920 19.787  1.00 38.95  ? 140 GLU B O   1 
ATOM   2720 C CB  . GLU B 1 138 ? -2.659  -18.625 19.122  1.00 36.90  ? 140 GLU B CB  1 
ATOM   2721 C CG  . GLU B 1 138 ? -1.164  -18.514 18.865  1.00 39.16  ? 140 GLU B CG  1 
ATOM   2722 C CD  . GLU B 1 138 ? -0.389  -17.517 19.705  1.00 39.96  ? 140 GLU B CD  1 
ATOM   2723 O OE1 . GLU B 1 138 ? -0.880  -16.383 19.882  1.00 39.26  ? 140 GLU B OE1 1 
ATOM   2724 O OE2 . GLU B 1 138 ? 0.723   -17.857 20.167  1.00 40.69  ? 140 GLU B OE2 1 
ATOM   2725 N N   . SER B 1 139 ? -4.910  -20.057 21.711  1.00 37.45  ? 141 SER B N   1 
ATOM   2726 C CA  . SER B 1 139 ? -6.284  -20.430 21.993  1.00 37.78  ? 141 SER B CA  1 
ATOM   2727 C C   . SER B 1 139 ? -7.189  -19.315 22.465  1.00 39.24  ? 141 SER B C   1 
ATOM   2728 O O   . SER B 1 139 ? -8.381  -19.582 22.646  1.00 40.91  ? 141 SER B O   1 
ATOM   2729 C CB  . SER B 1 139 ? -6.300  -21.548 23.031  1.00 39.01  ? 141 SER B CB  1 
ATOM   2730 O OG  . SER B 1 139 ? -5.610  -22.680 22.514  1.00 40.97  ? 141 SER B OG  1 
ATOM   2731 N N   . PHE B 1 140 ? -6.677  -18.083 22.661  1.00 38.07  ? 142 PHE B N   1 
ATOM   2732 C CA  . PHE B 1 140 ? -7.502  -17.025 23.222  1.00 38.93  ? 142 PHE B CA  1 
ATOM   2733 C C   . PHE B 1 140 ? -7.870  -15.979 22.178  1.00 40.61  ? 142 PHE B C   1 
ATOM   2734 O O   . PHE B 1 140 ? -8.162  -14.855 22.544  1.00 40.15  ? 142 PHE B O   1 
ATOM   2735 C CB  . PHE B 1 140 ? -6.803  -16.413 24.458  1.00 37.65  ? 142 PHE B CB  1 
ATOM   2736 C CG  . PHE B 1 140 ? -6.389  -17.488 25.434  1.00 36.35  ? 142 PHE B CG  1 
ATOM   2737 C CD1 . PHE B 1 140 ? -7.331  -18.258 26.078  1.00 36.26  ? 142 PHE B CD1 1 
ATOM   2738 C CD2 . PHE B 1 140 ? -5.063  -17.789 25.634  1.00 36.08  ? 142 PHE B CD2 1 
ATOM   2739 C CE1 . PHE B 1 140 ? -6.955  -19.278 26.927  1.00 35.27  ? 142 PHE B CE1 1 
ATOM   2740 C CE2 . PHE B 1 140 ? -4.696  -18.807 26.494  1.00 35.31  ? 142 PHE B CE2 1 
ATOM   2741 C CZ  . PHE B 1 140 ? -5.642  -19.521 27.150  1.00 34.46  ? 142 PHE B CZ  1 
ATOM   2742 N N   . ASP B 1 141 ? -7.866  -16.341 20.881  1.00 42.78  ? 143 ASP B N   1 
ATOM   2743 C CA  . ASP B 1 141 ? -8.236  -15.425 19.802  1.00 45.72  ? 143 ASP B CA  1 
ATOM   2744 C C   . ASP B 1 141 ? -7.270  -14.191 19.812  1.00 46.59  ? 143 ASP B C   1 
ATOM   2745 O O   . ASP B 1 141 ? -6.081  -14.417 20.048  1.00 47.82  ? 143 ASP B O   1 
ATOM   2746 C CB  . ASP B 1 141 ? -9.773  -15.120 19.861  1.00 49.45  ? 143 ASP B CB  1 
ATOM   2747 C CG  . ASP B 1 141 ? -10.583 -16.415 19.812  1.00 58.22  ? 143 ASP B CG  1 
ATOM   2748 O OD1 . ASP B 1 141 ? -10.723 -16.991 18.701  1.00 58.99  ? 143 ASP B OD1 1 
ATOM   2749 O OD2 . ASP B 1 141 ? -11.058 -16.873 20.897  1.00 62.87  ? 143 ASP B OD2 1 
ATOM   2750 N N   . ASP B 1 142 ? -7.706  -12.953 19.554  1.00 46.83  ? 144 ASP B N   1 
ATOM   2751 C CA  . ASP B 1 142 ? -6.770  -11.805 19.576  1.00 48.55  ? 144 ASP B CA  1 
ATOM   2752 C C   . ASP B 1 142 ? -6.140  -11.579 20.958  1.00 47.09  ? 144 ASP B C   1 
ATOM   2753 O O   . ASP B 1 142 ? -5.037  -11.043 21.052  1.00 47.45  ? 144 ASP B O   1 
ATOM   2754 C CB  . ASP B 1 142 ? -7.428  -10.527 19.054  1.00 53.34  ? 144 ASP B CB  1 
ATOM   2755 C CG  . ASP B 1 142 ? -7.606  -10.534 17.532  1.00 64.18  ? 144 ASP B CG  1 
ATOM   2756 O OD1 . ASP B 1 142 ? -6.877  -11.322 16.838  1.00 65.17  ? 144 ASP B OD1 1 
ATOM   2757 O OD2 . ASP B 1 142 ? -8.458  -9.757  17.031  1.00 68.59  ? 144 ASP B OD2 1 
ATOM   2758 N N   . TYR B 1 143 ? -6.823  -12.023 22.018  1.00 45.09  ? 145 TYR B N   1 
ATOM   2759 C CA  . TYR B 1 143 ? -6.345  -11.864 23.371  1.00 43.01  ? 145 TYR B CA  1 
ATOM   2760 C C   . TYR B 1 143 ? -5.160  -12.799 23.729  1.00 40.85  ? 145 TYR B C   1 
ATOM   2761 O O   . TYR B 1 143 ? -4.596  -12.672 24.803  1.00 39.86  ? 145 TYR B O   1 
ATOM   2762 C CB  . TYR B 1 143 ? -7.509  -12.022 24.324  1.00 43.99  ? 145 TYR B CB  1 
ATOM   2763 C CG  . TYR B 1 143 ? -8.652  -11.045 24.087  1.00 46.63  ? 145 TYR B CG  1 
ATOM   2764 C CD1 . TYR B 1 143 ? -8.440  -9.672  24.126  1.00 47.67  ? 145 TYR B CD1 1 
ATOM   2765 C CD2 . TYR B 1 143 ? -9.949  -11.497 23.852  1.00 47.65  ? 145 TYR B CD2 1 
ATOM   2766 C CE1 . TYR B 1 143 ? -9.491  -8.775  23.993  1.00 48.59  ? 145 TYR B CE1 1 
ATOM   2767 C CE2 . TYR B 1 143 ? -11.001 -10.605 23.675  1.00 48.38  ? 145 TYR B CE2 1 
ATOM   2768 C CZ  . TYR B 1 143 ? -10.769 -9.243  23.764  1.00 50.23  ? 145 TYR B CZ  1 
ATOM   2769 O OH  . TYR B 1 143 ? -11.780 -8.318  23.616  1.00 54.73  ? 145 TYR B OH  1 
ATOM   2770 N N   . SER B 1 144 ? -4.777  -13.734 22.842  1.00 40.03  ? 146 SER B N   1 
ATOM   2771 C CA  . SER B 1 144 ? -3.539  -14.507 23.009  1.00 39.37  ? 146 SER B CA  1 
ATOM   2772 C C   . SER B 1 144 ? -2.277  -13.655 23.064  1.00 37.59  ? 146 SER B C   1 
ATOM   2773 O O   . SER B 1 144 ? -1.271  -14.091 23.626  1.00 37.24  ? 146 SER B O   1 
ATOM   2774 C CB  . SER B 1 144 ? -3.400  -15.551 21.898  1.00 40.58  ? 146 SER B CB  1 
ATOM   2775 O OG  . SER B 1 144 ? -4.102  -16.750 22.190  1.00 42.33  ? 146 SER B OG  1 
ATOM   2776 N N   . ASP B 1 145 ? -2.314  -12.469 22.485  1.00 36.64  ? 147 ASP B N   1 
ATOM   2777 C CA  . ASP B 1 145 ? -1.230  -11.504 22.579  1.00 36.28  ? 147 ASP B CA  1 
ATOM   2778 C C   . ASP B 1 145 ? -1.014  -10.979 23.983  1.00 35.14  ? 147 ASP B C   1 
ATOM   2779 O O   . ASP B 1 145 ? 0.096   -10.563 24.279  1.00 36.72  ? 147 ASP B O   1 
ATOM   2780 C CB  . ASP B 1 145 ? -1.481  -10.333 21.626  1.00 38.52  ? 147 ASP B CB  1 
ATOM   2781 C CG  . ASP B 1 145 ? -1.324  -10.652 20.152  1.00 44.55  ? 147 ASP B CG  1 
ATOM   2782 O OD1 . ASP B 1 145 ? -0.687  -11.701 19.830  1.00 44.76  ? 147 ASP B OD1 1 
ATOM   2783 O OD2 . ASP B 1 145 ? -1.846  -9.859  19.312  1.00 46.95  ? 147 ASP B OD2 1 
ATOM   2784 N N   . ASP B 1 146 ? -2.053  -10.961 24.833  1.00 32.87  ? 148 ASP B N   1 
ATOM   2785 C CA  . ASP B 1 146 ? -1.876  -10.654 26.261  1.00 32.47  ? 148 ASP B CA  1 
ATOM   2786 C C   . ASP B 1 146 ? -1.211  -11.753 27.059  1.00 31.16  ? 148 ASP B C   1 
ATOM   2787 O O   . ASP B 1 146 ? -0.811  -11.496 28.166  1.00 31.58  ? 148 ASP B O   1 
ATOM   2788 C CB  . ASP B 1 146 ? -3.215  -10.296 26.948  1.00 34.94  ? 148 ASP B CB  1 
ATOM   2789 C CG  . ASP B 1 146 ? -3.550  -8.806  26.819  1.00 39.18  ? 148 ASP B CG  1 
ATOM   2790 O OD1 . ASP B 1 146 ? -3.406  -8.276  25.720  1.00 41.31  ? 148 ASP B OD1 1 
ATOM   2791 O OD2 . ASP B 1 146 ? -3.933  -8.184  27.845  1.00 38.54  ? 148 ASP B OD2 1 
ATOM   2792 N N   . VAL B 1 147 ? -1.087  -12.957 26.525  1.00 29.82  ? 149 VAL B N   1 
ATOM   2793 C CA  . VAL B 1 147 ? -0.415  -14.067 27.194  1.00 28.08  ? 149 VAL B CA  1 
ATOM   2794 C C   . VAL B 1 147 ? 1.091   -13.883 27.138  1.00 25.59  ? 149 VAL B C   1 
ATOM   2795 O O   . VAL B 1 147 ? 1.661   -13.638 26.080  1.00 24.88  ? 149 VAL B O   1 
ATOM   2796 C CB  . VAL B 1 147 ? -0.856  -15.388 26.576  1.00 28.56  ? 149 VAL B CB  1 
ATOM   2797 C CG1 . VAL B 1 147 ? -0.118  -16.555 27.207  1.00 29.34  ? 149 VAL B CG1 1 
ATOM   2798 C CG2 . VAL B 1 147 ? -2.365  -15.569 26.694  1.00 28.25  ? 149 VAL B CG2 1 
ATOM   2799 N N   . CYS B 1 148 ? 1.727   -13.998 28.306  1.00 24.88  ? 150 CYS B N   1 
ATOM   2800 C CA  . CYS B 1 148 ? 3.185   -13.990 28.456  1.00 24.74  ? 150 CYS B CA  1 
ATOM   2801 C C   . CYS B 1 148 ? 3.771   -15.405 28.522  1.00 24.53  ? 150 CYS B C   1 
ATOM   2802 O O   . CYS B 1 148 ? 4.805   -15.671 27.915  1.00 24.87  ? 150 CYS B O   1 
ATOM   2803 C CB  . CYS B 1 148 ? 3.551   -13.198 29.691  1.00 25.58  ? 150 CYS B CB  1 
ATOM   2804 S SG  . CYS B 1 148 ? 3.106   -11.477 29.562  1.00 32.79  ? 150 CYS B SG  1 
ATOM   2805 N N   . GLY B 1 149 ? 3.096   -16.274 29.250  1.00 24.11  ? 151 GLY B N   1 
ATOM   2806 C CA  . GLY B 1 149 ? 3.559   -17.626 29.511  1.00 25.22  ? 151 GLY B CA  1 
ATOM   2807 C C   . GLY B 1 149 ? 2.732   -18.315 30.563  1.00 24.48  ? 151 GLY B C   1 
ATOM   2808 O O   . GLY B 1 149 ? 1.662   -17.839 30.927  1.00 22.72  ? 151 GLY B O   1 
ATOM   2809 N N   . ALA B 1 150 ? 3.244   -19.450 31.029  1.00 24.88  ? 152 ALA B N   1 
ATOM   2810 C CA  . ALA B 1 150 ? 2.627   -20.313 32.022  1.00 25.29  ? 152 ALA B CA  1 
ATOM   2811 C C   . ALA B 1 150 ? 3.670   -20.835 32.985  1.00 26.06  ? 152 ALA B C   1 
ATOM   2812 O O   . ALA B 1 150 ? 4.798   -21.093 32.581  1.00 25.75  ? 152 ALA B O   1 
ATOM   2813 C CB  . ALA B 1 150 ? 1.900   -21.458 31.351  1.00 24.87  ? 152 ALA B CB  1 
ATOM   2814 N N   . VAL B 1 151 ? 3.289   -20.975 34.289  1.00 27.00  ? 153 VAL B N   1 
ATOM   2815 C CA  . VAL B 1 151 ? 4.186   -21.443 35.334  1.00 27.52  ? 153 VAL B CA  1 
ATOM   2816 C C   . VAL B 1 151 ? 3.544   -22.597 36.076  1.00 28.98  ? 153 VAL B C   1 
ATOM   2817 O O   . VAL B 1 151 ? 2.358   -22.562 36.392  1.00 29.87  ? 153 VAL B O   1 
ATOM   2818 C CB  . VAL B 1 151 ? 4.572   -20.295 36.305  1.00 28.55  ? 153 VAL B CB  1 
ATOM   2819 C CG1 . VAL B 1 151 ? 5.573   -20.759 37.356  1.00 29.49  ? 153 VAL B CG1 1 
ATOM   2820 C CG2 . VAL B 1 151 ? 5.130   -19.095 35.565  1.00 28.99  ? 153 VAL B CG2 1 
ATOM   2821 N N   . VAL B 1 152 ? 4.330   -23.630 36.357  1.00 29.15  ? 154 VAL B N   1 
ATOM   2822 C CA  . VAL B 1 152 ? 3.949   -24.694 37.251  1.00 29.94  ? 154 VAL B CA  1 
ATOM   2823 C C   . VAL B 1 152 ? 4.910   -24.703 38.431  1.00 30.80  ? 154 VAL B C   1 
ATOM   2824 O O   . VAL B 1 152 ? 6.100   -24.829 38.245  1.00 28.64  ? 154 VAL B O   1 
ATOM   2825 C CB  . VAL B 1 152 ? 3.778   -26.091 36.581  1.00 31.71  ? 154 VAL B CB  1 
ATOM   2826 C CG1 . VAL B 1 152 ? 5.042   -26.523 35.847  1.00 33.84  ? 154 VAL B CG1 1 
ATOM   2827 C CG2 . VAL B 1 152 ? 3.372   -27.129 37.617  1.00 33.60  ? 154 VAL B CG2 1 
ATOM   2828 N N   . ASN B 1 153 ? 4.382   -24.559 39.646  1.00 33.55  ? 155 ASN B N   1 
ATOM   2829 C CA  . ASN B 1 153 ? 5.169   -24.683 40.884  1.00 36.96  ? 155 ASN B CA  1 
ATOM   2830 C C   . ASN B 1 153 ? 4.790   -26.060 41.499  1.00 40.14  ? 155 ASN B C   1 
ATOM   2831 O O   . ASN B 1 153 ? 3.653   -26.257 41.919  1.00 40.01  ? 155 ASN B O   1 
ATOM   2832 C CB  . ASN B 1 153 ? 4.862   -23.517 41.880  1.00 37.38  ? 155 ASN B CB  1 
ATOM   2833 C CG  . ASN B 1 153 ? 4.755   -22.123 41.242  1.00 41.95  ? 155 ASN B CG  1 
ATOM   2834 O OD1 . ASN B 1 153 ? 3.671   -21.591 40.953  1.00 42.15  ? 155 ASN B OD1 1 
ATOM   2835 N ND2 . ASN B 1 153 ? 5.886   -21.474 41.002  1.00 42.86  ? 155 ASN B ND2 1 
ATOM   2836 N N   . VAL B 1 154 ? 5.732   -26.996 41.528  1.00 43.34  ? 156 VAL B N   1 
ATOM   2837 C CA  . VAL B 1 154 ? 5.557   -28.320 42.143  1.00 47.26  ? 156 VAL B CA  1 
ATOM   2838 C C   . VAL B 1 154 ? 5.855   -28.148 43.645  1.00 50.39  ? 156 VAL B C   1 
ATOM   2839 O O   . VAL B 1 154 ? 6.988   -27.855 43.988  1.00 50.35  ? 156 VAL B O   1 
ATOM   2840 C CB  . VAL B 1 154 ? 6.530   -29.337 41.491  1.00 48.88  ? 156 VAL B CB  1 
ATOM   2841 C CG1 . VAL B 1 154 ? 6.400   -30.739 42.085  1.00 49.47  ? 156 VAL B CG1 1 
ATOM   2842 C CG2 . VAL B 1 154 ? 6.278   -29.392 40.008  1.00 49.75  ? 156 VAL B CG2 1 
ATOM   2843 N N   . ARG B 1 155 ? 4.855   -28.317 44.512  1.00 53.06  ? 157 ARG B N   1 
ATOM   2844 C CA  . ARG B 1 155 ? 4.986   -28.067 45.963  1.00 56.35  ? 157 ARG B CA  1 
ATOM   2845 C C   . ARG B 1 155 ? 4.350   -29.192 46.816  1.00 58.91  ? 157 ARG B C   1 
ATOM   2846 O O   . ARG B 1 155 ? 3.439   -29.890 46.359  1.00 59.36  ? 157 ARG B O   1 
ATOM   2847 C CB  . ARG B 1 155 ? 4.346   -26.737 46.336  1.00 56.97  ? 157 ARG B CB  1 
ATOM   2848 C CG  . ARG B 1 155 ? 5.000   -25.561 45.695  1.00 59.80  ? 157 ARG B CG  1 
ATOM   2849 C CD  . ARG B 1 155 ? 6.306   -25.177 46.352  1.00 63.49  ? 157 ARG B CD  1 
ATOM   2850 N NE  . ARG B 1 155 ? 6.745   -23.860 45.878  1.00 67.81  ? 157 ARG B NE  1 
ATOM   2851 C CZ  . ARG B 1 155 ? 7.366   -23.617 44.724  1.00 68.72  ? 157 ARG B CZ  1 
ATOM   2852 N NH1 . ARG B 1 155 ? 7.648   -24.614 43.885  1.00 67.23  ? 157 ARG B NH1 1 
ATOM   2853 N NH2 . ARG B 1 155 ? 7.710   -22.378 44.400  1.00 69.42  ? 157 ARG B NH2 1 
ATOM   2854 N N   . ALA B 1 156 ? 4.827   -29.357 48.052  1.00 60.39  ? 158 ALA B N   1 
ATOM   2855 C CA  . ALA B 1 156 ? 4.318   -30.402 48.962  1.00 61.66  ? 158 ALA B CA  1 
ATOM   2856 C C   . ALA B 1 156 ? 2.881   -30.087 49.429  1.00 61.89  ? 158 ALA B C   1 
ATOM   2857 O O   . ALA B 1 156 ? 2.037   -30.966 49.403  1.00 62.03  ? 158 ALA B O   1 
ATOM   2858 C CB  . ALA B 1 156 ? 5.243   -30.534 50.167  1.00 61.91  ? 158 ALA B CB  1 
ATOM   2859 N N   . LYS B 1 157 ? 2.611   -28.848 49.836  1.00 62.19  ? 159 LYS B N   1 
ATOM   2860 C CA  . LYS B 1 157 ? 1.251   -28.392 50.143  1.00 62.90  ? 159 LYS B CA  1 
ATOM   2861 C C   . LYS B 1 157 ? 0.250   -28.636 48.971  1.00 61.47  ? 159 LYS B C   1 
ATOM   2862 O O   . LYS B 1 157 ? -0.931  -28.914 49.211  1.00 61.93  ? 159 LYS B O   1 
ATOM   2863 C CB  . LYS B 1 157 ? 1.282   -26.885 50.530  1.00 66.14  ? 159 LYS B CB  1 
ATOM   2864 C CG  . LYS B 1 157 ? -0.106  -26.230 50.693  1.00 72.28  ? 159 LYS B CG  1 
ATOM   2865 C CD  . LYS B 1 157 ? -0.100  -24.963 51.599  1.00 77.76  ? 159 LYS B CD  1 
ATOM   2866 C CE  . LYS B 1 157 ? -0.082  -25.251 53.097  1.00 82.76  ? 159 LYS B CE  1 
ATOM   2867 N NZ  . LYS B 1 157 ? -1.352  -25.877 53.598  1.00 86.14  ? 159 LYS B NZ  1 
ATOM   2868 N N   . GLY B 1 158 ? 0.720   -28.524 47.735  1.00 59.47  ? 160 GLY B N   1 
ATOM   2869 C CA  . GLY B 1 158 ? -0.155  -28.644 46.578  1.00 58.00  ? 160 GLY B CA  1 
ATOM   2870 C C   . GLY B 1 158 ? 0.256   -27.723 45.457  1.00 55.45  ? 160 GLY B C   1 
ATOM   2871 O O   . GLY B 1 158 ? 0.680   -26.581 45.687  1.00 56.11  ? 160 GLY B O   1 
ATOM   2872 N N   . ASP B 1 159 ? 0.137   -28.234 44.232  1.00 51.81  ? 161 ASP B N   1 
ATOM   2873 C CA  . ASP B 1 159 ? 0.796   -27.624 43.094  1.00 47.71  ? 161 ASP B CA  1 
ATOM   2874 C C   . ASP B 1 159 ? 0.050   -26.381 42.625  1.00 44.63  ? 161 ASP B C   1 
ATOM   2875 O O   . ASP B 1 159 ? -1.099  -26.139 43.011  1.00 44.98  ? 161 ASP B O   1 
ATOM   2876 C CB  . ASP B 1 159 ? 0.944   -28.658 41.989  1.00 47.29  ? 161 ASP B CB  1 
ATOM   2877 C CG  . ASP B 1 159 ? 1.699   -29.882 42.477  1.00 48.46  ? 161 ASP B CG  1 
ATOM   2878 O OD1 . ASP B 1 159 ? 2.754   -29.713 43.093  1.00 48.82  ? 161 ASP B OD1 1 
ATOM   2879 O OD2 . ASP B 1 159 ? 1.225   -30.997 42.246  1.00 48.95  ? 161 ASP B OD2 1 
ATOM   2880 N N   . LYS B 1 160 ? 0.712   -25.573 41.810  1.00 41.97  ? 162 LYS B N   1 
ATOM   2881 C CA  . LYS B 1 160 ? 0.102   -24.365 41.256  1.00 39.12  ? 162 LYS B CA  1 
ATOM   2882 C C   . LYS B 1 160 ? 0.389   -24.378 39.777  1.00 35.84  ? 162 LYS B C   1 
ATOM   2883 O O   . LYS B 1 160 ? 1.534   -24.638 39.358  1.00 35.35  ? 162 LYS B O   1 
ATOM   2884 C CB  . LYS B 1 160 ? 0.712   -23.111 41.905  1.00 42.65  ? 162 LYS B CB  1 
ATOM   2885 C CG  . LYS B 1 160 ? 0.367   -22.972 43.385  1.00 50.50  ? 162 LYS B CG  1 
ATOM   2886 C CD  . LYS B 1 160 ? 0.424   -21.516 43.885  1.00 60.03  ? 162 LYS B CD  1 
ATOM   2887 C CE  . LYS B 1 160 ? 1.823   -20.934 44.051  1.00 67.84  ? 162 LYS B CE  1 
ATOM   2888 N NZ  . LYS B 1 160 ? 2.336   -21.031 45.475  1.00 71.03  ? 162 LYS B NZ  1 
ATOM   2889 N N   . ILE B 1 161 ? -0.649  -24.121 38.982  1.00 33.78  ? 163 ILE B N   1 
ATOM   2890 C CA  . ILE B 1 161 ? -0.509  -23.874 37.553  1.00 32.29  ? 163 ILE B CA  1 
ATOM   2891 C C   . ILE B 1 161 ? -1.146  -22.542 37.239  1.00 30.83  ? 163 ILE B C   1 
ATOM   2892 O O   . ILE B 1 161 ? -2.264  -22.303 37.679  1.00 30.36  ? 163 ILE B O   1 
ATOM   2893 C CB  . ILE B 1 161 ? -1.124  -25.002 36.713  1.00 32.56  ? 163 ILE B CB  1 
ATOM   2894 C CG1 . ILE B 1 161 ? -0.482  -26.360 37.056  1.00 34.07  ? 163 ILE B CG1 1 
ATOM   2895 C CG2 . ILE B 1 161 ? -1.009  -24.672 35.211  1.00 32.63  ? 163 ILE B CG2 1 
ATOM   2896 C CD1 . ILE B 1 161 ? -1.094  -27.518 36.372  1.00 36.91  ? 163 ILE B CD1 1 
ATOM   2897 N N   . ALA B 1 162 ? -0.445  -21.666 36.466  1.00 28.48  ? 164 ALA B N   1 
ATOM   2898 C CA  . ALA B 1 162 ? -0.931  -20.324 36.181  1.00 28.71  ? 164 ALA B CA  1 
ATOM   2899 C C   . ALA B 1 162 ? -0.577  -19.902 34.783  1.00 27.83  ? 164 ALA B C   1 
ATOM   2900 O O   . ALA B 1 162 ? 0.543   -20.168 34.344  1.00 27.18  ? 164 ALA B O   1 
ATOM   2901 C CB  . ALA B 1 162 ? -0.346  -19.343 37.167  1.00 30.13  ? 164 ALA B CB  1 
ATOM   2902 N N   . ILE B 1 163 ? -1.536  -19.269 34.066  1.00 27.40  ? 165 ILE B N   1 
ATOM   2903 C CA  . ILE B 1 163 ? -1.245  -18.475 32.874  1.00 26.28  ? 165 ILE B CA  1 
ATOM   2904 C C   . ILE B 1 163 ? -0.996  -17.035 33.251  1.00 26.16  ? 165 ILE B C   1 
ATOM   2905 O O   . ILE B 1 163 ? -1.875  -16.396 33.829  1.00 26.01  ? 165 ILE B O   1 
ATOM   2906 C CB  . ILE B 1 163 ? -2.390  -18.571 31.850  1.00 26.65  ? 165 ILE B CB  1 
ATOM   2907 C CG1 . ILE B 1 163 ? -2.466  -19.982 31.310  1.00 26.28  ? 165 ILE B CG1 1 
ATOM   2908 C CG2 . ILE B 1 163 ? -2.167  -17.523 30.694  1.00 28.11  ? 165 ILE B CG2 1 
ATOM   2909 C CD1 . ILE B 1 163 ? -3.461  -20.253 30.224  1.00 27.94  ? 165 ILE B CD1 1 
ATOM   2910 N N   . TRP B 1 164 ? 0.181   -16.525 32.896  1.00 26.38  ? 166 TRP B N   1 
ATOM   2911 C CA  . TRP B 1 164 ? 0.618   -15.129 33.098  1.00 26.97  ? 166 TRP B CA  1 
ATOM   2912 C C   . TRP B 1 164 ? 0.247   -14.275 31.894  1.00 27.55  ? 166 TRP B C   1 
ATOM   2913 O O   . TRP B 1 164 ? 0.508   -14.638 30.750  1.00 26.05  ? 166 TRP B O   1 
ATOM   2914 C CB  . TRP B 1 164 ? 2.141   -15.037 33.332  1.00 27.23  ? 166 TRP B CB  1 
ATOM   2915 C CG  . TRP B 1 164 ? 2.642   -15.522 34.665  1.00 29.19  ? 166 TRP B CG  1 
ATOM   2916 C CD1 . TRP B 1 164 ? 2.129   -16.526 35.442  1.00 30.04  ? 166 TRP B CD1 1 
ATOM   2917 C CD2 . TRP B 1 164 ? 3.805   -15.021 35.364  1.00 30.42  ? 166 TRP B CD2 1 
ATOM   2918 N NE1 . TRP B 1 164 ? 2.891   -16.673 36.589  1.00 29.92  ? 166 TRP B NE1 1 
ATOM   2919 C CE2 . TRP B 1 164 ? 3.940   -15.777 36.550  1.00 30.66  ? 166 TRP B CE2 1 
ATOM   2920 C CE3 . TRP B 1 164 ? 4.768   -14.018 35.077  1.00 31.75  ? 166 TRP B CE3 1 
ATOM   2921 C CZ2 . TRP B 1 164 ? 4.982   -15.553 37.457  1.00 31.83  ? 166 TRP B CZ2 1 
ATOM   2922 C CZ3 . TRP B 1 164 ? 5.809   -13.807 35.968  1.00 32.30  ? 166 TRP B CZ3 1 
ATOM   2923 C CH2 . TRP B 1 164 ? 5.905   -14.565 37.145  1.00 33.01  ? 166 TRP B CH2 1 
ATOM   2924 N N   . THR B 1 165 ? -0.359  -13.124 32.164  1.00 29.47  ? 167 THR B N   1 
ATOM   2925 C CA  . THR B 1 165 ? -0.739  -12.144 31.140  1.00 31.12  ? 167 THR B CA  1 
ATOM   2926 C C   . THR B 1 165 ? -0.074  -10.796 31.453  1.00 31.19  ? 167 THR B C   1 
ATOM   2927 O O   . THR B 1 165 ? 0.399   -10.540 32.577  1.00 29.56  ? 167 THR B O   1 
ATOM   2928 C CB  . THR B 1 165 ? -2.302  -12.083 30.946  1.00 32.91  ? 167 THR B CB  1 
ATOM   2929 O OG1 . THR B 1 165 ? -2.868  -11.274 31.962  1.00 32.30  ? 167 THR B OG1 1 
ATOM   2930 C CG2 . THR B 1 165 ? -2.951  -13.476 30.955  1.00 35.38  ? 167 THR B CG2 1 
ATOM   2931 N N   . THR B 1 166 ? -0.038  -9.943  30.429  1.00 31.91  ? 168 THR B N   1 
ATOM   2932 C CA  . THR B 1 166 ? 0.821   -8.764  30.422  1.00 33.12  ? 168 THR B CA  1 
ATOM   2933 C C   . THR B 1 166 ? 0.253   -7.549  31.131  1.00 33.98  ? 168 THR B C   1 
ATOM   2934 O O   . THR B 1 166 ? 1.029   -6.697  31.578  1.00 33.23  ? 168 THR B O   1 
ATOM   2935 C CB  . THR B 1 166 ? 1.203   -8.428  28.948  1.00 35.63  ? 168 THR B CB  1 
ATOM   2936 O OG1 . THR B 1 166 ? 2.364   -7.585  28.936  1.00 37.55  ? 168 THR B OG1 1 
ATOM   2937 C CG2 . THR B 1 166 ? 0.065   -7.779  28.171  1.00 35.30  ? 168 THR B CG2 1 
ATOM   2938 N N   . GLU B 1 167 ? -1.088  -7.458  31.250  1.00 34.62  ? 169 GLU B N   1 
ATOM   2939 C CA  . GLU B 1 167 ? -1.724  -6.229  31.729  1.00 35.83  ? 169 GLU B CA  1 
ATOM   2940 C C   . GLU B 1 167 ? -3.013  -6.513  32.531  1.00 36.60  ? 169 GLU B C   1 
ATOM   2941 O O   . GLU B 1 167 ? -4.040  -6.830  31.943  1.00 36.01  ? 169 GLU B O   1 
ATOM   2942 C CB  . GLU B 1 167 ? -2.048  -5.316  30.504  1.00 36.27  ? 169 GLU B CB  1 
ATOM   2943 C CG  . GLU B 1 167 ? -2.721  -3.998  30.817  1.00 36.70  ? 169 GLU B CG  1 
ATOM   2944 C CD  . GLU B 1 167 ? -2.083  -3.249  31.962  1.00 42.21  ? 169 GLU B CD  1 
ATOM   2945 O OE1 . GLU B 1 167 ? -0.988  -2.676  31.769  1.00 41.88  ? 169 GLU B OE1 1 
ATOM   2946 O OE2 . GLU B 1 167 ? -2.668  -3.262  33.069  1.00 45.04  ? 169 GLU B OE2 1 
ATOM   2947 N N   . CYS B 1 168 ? -2.955  -6.381  33.861  1.00 37.75  ? 170 CYS B N   1 
ATOM   2948 C CA  . CYS B 1 168 ? -4.111  -6.672  34.706  1.00 39.55  ? 170 CYS B CA  1 
ATOM   2949 C C   . CYS B 1 168 ? -5.322  -5.733  34.489  1.00 38.82  ? 170 CYS B C   1 
ATOM   2950 O O   . CYS B 1 168 ? -6.417  -6.131  34.853  1.00 38.12  ? 170 CYS B O   1 
ATOM   2951 C CB  . CYS B 1 168 ? -3.714  -6.717  36.179  1.00 43.08  ? 170 CYS B CB  1 
ATOM   2952 S SG  . CYS B 1 168 ? -3.031  -5.170  36.802  1.00 51.89  ? 170 CYS B SG  1 
ATOM   2953 N N   . GLU B 1 169 ? -5.143  -4.509  33.911  1.00 38.88  ? 171 GLU B N   1 
ATOM   2954 C CA  . GLU B 1 169 ? -6.257  -3.588  33.611  1.00 38.08  ? 171 GLU B CA  1 
ATOM   2955 C C   . GLU B 1 169 ? -7.000  -3.885  32.304  1.00 38.08  ? 171 GLU B C   1 
ATOM   2956 O O   . GLU B 1 169 ? -8.004  -3.249  32.033  1.00 38.25  ? 171 GLU B O   1 
ATOM   2957 C CB  . GLU B 1 169 ? -5.771  -2.122  33.612  1.00 39.04  ? 171 GLU B CB  1 
ATOM   2958 C CG  . GLU B 1 169 ? -5.092  -1.695  34.887  1.00 42.65  ? 171 GLU B CG  1 
ATOM   2959 C CD  . GLU B 1 169 ? -5.888  -1.864  36.168  1.00 47.23  ? 171 GLU B CD  1 
ATOM   2960 O OE1 . GLU B 1 169 ? -7.137  -1.794  36.113  1.00 47.83  ? 171 GLU B OE1 1 
ATOM   2961 O OE2 . GLU B 1 169 ? -5.256  -2.049  37.234  1.00 48.04  ? 171 GLU B OE2 1 
ATOM   2962 N N   . ASN B 1 170 ? -6.524  -4.819  31.494  1.00 38.70  ? 172 ASN B N   1 
ATOM   2963 C CA  . ASN B 1 170 ? -7.273  -5.304  30.324  1.00 39.67  ? 172 ASN B CA  1 
ATOM   2964 C C   . ASN B 1 170 ? -8.317  -6.365  30.718  1.00 41.32  ? 172 ASN B C   1 
ATOM   2965 O O   . ASN B 1 170 ? -8.101  -7.572  30.478  1.00 39.37  ? 172 ASN B O   1 
ATOM   2966 C CB  . ASN B 1 170 ? -6.296  -5.889  29.268  1.00 39.67  ? 172 ASN B CB  1 
ATOM   2967 C CG  . ASN B 1 170 ? -5.450  -4.864  28.556  1.00 39.83  ? 172 ASN B CG  1 
ATOM   2968 O OD1 . ASN B 1 170 ? -5.691  -3.657  28.598  1.00 39.17  ? 172 ASN B OD1 1 
ATOM   2969 N ND2 . ASN B 1 170 ? -4.448  -5.331  27.860  1.00 39.87  ? 172 ASN B ND2 1 
ATOM   2970 N N   . ARG B 1 171 ? -9.477  -5.910  31.307  1.00 43.06  ? 173 ARG B N   1 
ATOM   2971 C CA  . ARG B 1 171 ? -10.451 -6.870  31.842  1.00 45.45  ? 173 ARG B CA  1 
ATOM   2972 C C   . ARG B 1 171 ? -10.988 -7.798  30.757  1.00 45.48  ? 173 ARG B C   1 
ATOM   2973 O O   . ARG B 1 171 ? -11.095 -8.984  30.997  1.00 45.25  ? 173 ARG B O   1 
ATOM   2974 C CB  . ARG B 1 171 ? -11.633 -6.209  32.590  1.00 48.81  ? 173 ARG B CB  1 
ATOM   2975 C CG  . ARG B 1 171 ? -12.519 -7.235  33.317  1.00 56.61  ? 173 ARG B CG  1 
ATOM   2976 C CD  . ARG B 1 171 ? -13.866 -6.767  33.840  1.00 63.88  ? 173 ARG B CD  1 
ATOM   2977 N NE  . ARG B 1 171 ? -13.842 -5.963  35.083  1.00 70.89  ? 173 ARG B NE  1 
ATOM   2978 C CZ  . ARG B 1 171 ? -14.161 -6.371  36.323  1.00 74.53  ? 173 ARG B CZ  1 
ATOM   2979 N NH1 . ARG B 1 171 ? -14.532 -7.633  36.549  1.00 74.00  ? 173 ARG B NH1 1 
ATOM   2980 N NH2 . ARG B 1 171 ? -14.106 -5.515  37.347  1.00 74.23  ? 173 ARG B NH2 1 
ATOM   2981 N N   . GLU B 1 172 ? -11.340 -7.254  29.583  1.00 45.22  ? 174 GLU B N   1 
ATOM   2982 C CA  . GLU B 1 172 ? -11.884 -8.053  28.482  1.00 44.35  ? 174 GLU B CA  1 
ATOM   2983 C C   . GLU B 1 172 ? -10.930 -9.161  28.049  1.00 43.37  ? 174 GLU B C   1 
ATOM   2984 O O   . GLU B 1 172 ? -11.355 -10.315 27.913  1.00 43.83  ? 174 GLU B O   1 
ATOM   2985 C CB  . GLU B 1 172 ? -12.185 -7.181  27.275  1.00 47.29  ? 174 GLU B CB  1 
ATOM   2986 C CG  . GLU B 1 172 ? -13.287 -6.172  27.495  1.00 58.54  ? 174 GLU B CG  1 
ATOM   2987 C CD  . GLU B 1 172 ? -13.431 -5.196  26.339  1.00 70.18  ? 174 GLU B CD  1 
ATOM   2988 O OE1 . GLU B 1 172 ? -14.134 -5.553  25.365  1.00 73.11  ? 174 GLU B OE1 1 
ATOM   2989 O OE2 . GLU B 1 172 ? -12.838 -4.089  26.399  1.00 72.72  ? 174 GLU B OE2 1 
ATOM   2990 N N   . ALA B 1 173 ? -9.633  -8.811  27.826  1.00 41.27  ? 175 ALA B N   1 
ATOM   2991 C CA  . ALA B 1 173 ? -8.626  -9.781  27.476  1.00 39.20  ? 175 ALA B CA  1 
ATOM   2992 C C   . ALA B 1 173 ? -8.475  -10.849 28.575  1.00 36.96  ? 175 ALA B C   1 
ATOM   2993 O O   . ALA B 1 173 ? -8.474  -12.050 28.277  1.00 35.16  ? 175 ALA B O   1 
ATOM   2994 C CB  . ALA B 1 173 ? -7.293  -9.094  27.195  1.00 39.47  ? 175 ALA B CB  1 
ATOM   2995 N N   . VAL B 1 174 ? -8.392  -10.387 29.818  1.00 36.07  ? 176 VAL B N   1 
ATOM   2996 C CA  . VAL B 1 174 ? -8.114  -11.212 30.946  1.00 36.28  ? 176 VAL B CA  1 
ATOM   2997 C C   . VAL B 1 174 ? -9.239  -12.214 31.214  1.00 37.91  ? 176 VAL B C   1 
ATOM   2998 O O   . VAL B 1 174 ? -8.949  -13.396 31.460  1.00 37.85  ? 176 VAL B O   1 
ATOM   2999 C CB  . VAL B 1 174 ? -7.751  -10.343 32.186  1.00 35.11  ? 176 VAL B CB  1 
ATOM   3000 C CG1 . VAL B 1 174 ? -7.738  -11.186 33.462  1.00 35.53  ? 176 VAL B CG1 1 
ATOM   3001 C CG2 . VAL B 1 174 ? -6.400  -9.620  31.974  1.00 34.16  ? 176 VAL B CG2 1 
ATOM   3002 N N   . THR B 1 175 ? -10.496 -11.778 31.166  1.00 39.28  ? 177 THR B N   1 
ATOM   3003 C CA  . THR B 1 175 ? -11.603 -12.663 31.553  1.00 41.46  ? 177 THR B CA  1 
ATOM   3004 C C   . THR B 1 175 ? -11.966 -13.604 30.387  1.00 42.13  ? 177 THR B C   1 
ATOM   3005 O O   . THR B 1 175 ? -12.454 -14.705 30.649  1.00 42.66  ? 177 THR B O   1 
ATOM   3006 C CB  . THR B 1 175 ? -12.792 -11.885 32.160  1.00 43.70  ? 177 THR B CB  1 
ATOM   3007 O OG1 . THR B 1 175 ? -13.452 -11.168 31.136  1.00 46.57  ? 177 THR B OG1 1 
ATOM   3008 C CG2 . THR B 1 175 ? -12.371 -10.930 33.270  1.00 43.09  ? 177 THR B CG2 1 
ATOM   3009 N N   . HIS B 1 176 ? -11.736 -13.202 29.120  1.00 42.06  ? 178 HIS B N   1 
ATOM   3010 C CA  . HIS B 1 176 ? -11.864 -14.151 27.992  1.00 41.70  ? 178 HIS B CA  1 
ATOM   3011 C C   . HIS B 1 176 ? -10.850 -15.297 28.134  1.00 40.28  ? 178 HIS B C   1 
ATOM   3012 O O   . HIS B 1 176 ? -11.197 -16.470 27.965  1.00 39.66  ? 178 HIS B O   1 
ATOM   3013 C CB  . HIS B 1 176 ? -11.666 -13.442 26.641  1.00 43.76  ? 178 HIS B CB  1 
ATOM   3014 C CG  . HIS B 1 176 ? -11.708 -14.380 25.470  1.00 50.69  ? 178 HIS B CG  1 
ATOM   3015 N ND1 . HIS B 1 176 ? -12.882 -14.624 24.777  1.00 53.81  ? 178 HIS B ND1 1 
ATOM   3016 C CD2 . HIS B 1 176 ? -10.718 -15.129 24.924  1.00 53.26  ? 178 HIS B CD2 1 
ATOM   3017 C CE1 . HIS B 1 176 ? -12.572 -15.506 23.836  1.00 55.12  ? 178 HIS B CE1 1 
ATOM   3018 N NE2 . HIS B 1 176 ? -11.278 -15.828 23.877  1.00 55.20  ? 178 HIS B NE2 1 
ATOM   3019 N N   . ILE B 1 177 ? -9.585  -14.957 28.469  1.00 38.78  ? 179 ILE B N   1 
ATOM   3020 C CA  . ILE B 1 177 ? -8.529  -15.944 28.652  1.00 36.87  ? 179 ILE B CA  1 
ATOM   3021 C C   . ILE B 1 177 ? -8.930  -16.908 29.761  1.00 37.09  ? 179 ILE B C   1 
ATOM   3022 O O   . ILE B 1 177 ? -8.805  -18.118 29.581  1.00 37.41  ? 179 ILE B O   1 
ATOM   3023 C CB  . ILE B 1 177 ? -7.143  -15.297 28.966  1.00 35.75  ? 179 ILE B CB  1 
ATOM   3024 C CG1 . ILE B 1 177 ? -6.532  -14.656 27.717  1.00 35.40  ? 179 ILE B CG1 1 
ATOM   3025 C CG2 . ILE B 1 177 ? -6.140  -16.326 29.626  1.00 34.44  ? 179 ILE B CG2 1 
ATOM   3026 C CD1 . ILE B 1 177 ? -5.393  -13.546 28.019  1.00 33.71  ? 179 ILE B CD1 1 
ATOM   3027 N N   . GLY B 1 178 ? -9.401  -16.363 30.872  1.00 36.07  ? 180 GLY B N   1 
ATOM   3028 C CA  . GLY B 1 178 ? -9.798  -17.183 32.000  1.00 36.85  ? 180 GLY B CA  1 
ATOM   3029 C C   . GLY B 1 178 ? -10.948 -18.111 31.708  1.00 37.57  ? 180 GLY B C   1 
ATOM   3030 O O   . GLY B 1 178 ? -10.916 -19.263 32.136  1.00 36.86  ? 180 GLY B O   1 
ATOM   3031 N N   . ARG B 1 179 ? -11.992 -17.613 30.988  1.00 39.17  ? 181 ARG B N   1 
ATOM   3032 C CA  . ARG B 1 179 ? -13.155 -18.441 30.624  1.00 39.10  ? 181 ARG B CA  1 
ATOM   3033 C C   . ARG B 1 179 ? -12.759 -19.526 29.657  1.00 39.27  ? 181 ARG B C   1 
ATOM   3034 O O   . ARG B 1 179 ? -13.217 -20.663 29.821  1.00 39.56  ? 181 ARG B O   1 
ATOM   3035 C CB  . ARG B 1 179 ? -14.281 -17.624 29.980  1.00 40.13  ? 181 ARG B CB  1 
ATOM   3036 C CG  . ARG B 1 179 ? -15.137 -16.797 30.942  1.00 46.33  ? 181 ARG B CG  1 
ATOM   3037 C CD  . ARG B 1 179 ? -15.830 -15.672 30.219  1.00 50.91  ? 181 ARG B CD  1 
ATOM   3038 N NE  . ARG B 1 179 ? -16.106 -14.531 31.095  1.00 57.26  ? 181 ARG B NE  1 
ATOM   3039 C CZ  . ARG B 1 179 ? -16.072 -13.247 30.726  1.00 64.56  ? 181 ARG B CZ  1 
ATOM   3040 N NH1 . ARG B 1 179 ? -15.769 -12.906 29.468  1.00 64.62  ? 181 ARG B NH1 1 
ATOM   3041 N NH2 . ARG B 1 179 ? -16.341 -12.288 31.610  1.00 68.38  ? 181 ARG B NH2 1 
ATOM   3042 N N   . VAL B 1 180 ? -11.931 -19.197 28.622  1.00 39.07  ? 182 VAL B N   1 
ATOM   3043 C CA  . VAL B 1 180 ? -11.473 -20.232 27.652  1.00 38.73  ? 182 VAL B CA  1 
ATOM   3044 C C   . VAL B 1 180 ? -10.559 -21.197 28.355  1.00 39.90  ? 182 VAL B C   1 
ATOM   3045 O O   . VAL B 1 180 ? -10.690 -22.403 28.203  1.00 42.17  ? 182 VAL B O   1 
ATOM   3046 C CB  . VAL B 1 180 ? -10.802 -19.629 26.401  1.00 38.97  ? 182 VAL B CB  1 
ATOM   3047 C CG1 . VAL B 1 180 ? -10.123 -20.688 25.560  1.00 38.95  ? 182 VAL B CG1 1 
ATOM   3048 C CG2 . VAL B 1 180 ? -11.810 -18.845 25.533  1.00 39.84  ? 182 VAL B CG2 1 
ATOM   3049 N N   . TYR B 1 181 ? -9.627  -20.700 29.149  1.00 39.06  ? 183 TYR B N   1 
ATOM   3050 C CA  . TYR B 1 181 ? -8.717  -21.576 29.902  1.00 37.89  ? 183 TYR B CA  1 
ATOM   3051 C C   . TYR B 1 181 ? -9.496  -22.560 30.794  1.00 38.22  ? 183 TYR B C   1 
ATOM   3052 O O   . TYR B 1 181 ? -9.196  -23.730 30.777  1.00 36.37  ? 183 TYR B O   1 
ATOM   3053 C CB  . TYR B 1 181 ? -7.783  -20.708 30.762  1.00 35.00  ? 183 TYR B CB  1 
ATOM   3054 C CG  . TYR B 1 181 ? -6.719  -21.429 31.544  1.00 33.41  ? 183 TYR B CG  1 
ATOM   3055 C CD1 . TYR B 1 181 ? -6.055  -22.523 31.009  1.00 34.09  ? 183 TYR B CD1 1 
ATOM   3056 C CD2 . TYR B 1 181 ? -6.310  -20.964 32.783  1.00 32.65  ? 183 TYR B CD2 1 
ATOM   3057 C CE1 . TYR B 1 181 ? -5.022  -23.136 31.695  1.00 33.96  ? 183 TYR B CE1 1 
ATOM   3058 C CE2 . TYR B 1 181 ? -5.280  -21.570 33.475  1.00 32.57  ? 183 TYR B CE2 1 
ATOM   3059 C CZ  . TYR B 1 181 ? -4.627  -22.647 32.924  1.00 32.61  ? 183 TYR B CZ  1 
ATOM   3060 O OH  . TYR B 1 181 ? -3.606  -23.270 33.600  1.00 32.20  ? 183 TYR B OH  1 
ATOM   3061 N N   . LYS B 1 182 ? -10.487 -22.064 31.560  1.00 40.29  ? 184 LYS B N   1 
ATOM   3062 C CA  . LYS B 1 182 ? -11.298 -22.881 32.466  1.00 42.93  ? 184 LYS B CA  1 
ATOM   3063 C C   . LYS B 1 182 ? -12.073 -23.957 31.661  1.00 45.46  ? 184 LYS B C   1 
ATOM   3064 O O   . LYS B 1 182 ? -12.219 -25.096 32.118  1.00 46.83  ? 184 LYS B O   1 
ATOM   3065 C CB  . LYS B 1 182 ? -12.296 -21.971 33.225  1.00 45.72  ? 184 LYS B CB  1 
ATOM   3066 C CG  . LYS B 1 182 ? -13.116 -22.675 34.258  1.00 49.18  ? 184 LYS B CG  1 
ATOM   3067 C CD  . LYS B 1 182 ? -14.015 -21.738 34.986  1.00 56.15  ? 184 LYS B CD  1 
ATOM   3068 C CE  . LYS B 1 182 ? -15.010 -22.515 35.800  1.00 62.44  ? 184 LYS B CE  1 
ATOM   3069 N NZ  . LYS B 1 182 ? -15.837 -21.637 36.666  1.00 66.65  ? 184 LYS B NZ  1 
ATOM   3070 N N   . GLU B 1 183 ? -12.576 -23.577 30.479  1.00 45.46  ? 185 GLU B N   1 
ATOM   3071 C CA  . GLU B 1 183 ? -13.277 -24.484 29.550  1.00 46.30  ? 185 GLU B CA  1 
ATOM   3072 C C   . GLU B 1 183 ? -12.306 -25.608 29.107  1.00 45.66  ? 185 GLU B C   1 
ATOM   3073 O O   . GLU B 1 183 ? -12.649 -26.803 29.145  1.00 46.06  ? 185 GLU B O   1 
ATOM   3074 C CB  . GLU B 1 183 ? -13.793 -23.640 28.380  1.00 51.54  ? 185 GLU B CB  1 
ATOM   3075 C CG  . GLU B 1 183 ? -14.652 -24.236 27.293  1.00 63.44  ? 185 GLU B CG  1 
ATOM   3076 C CD  . GLU B 1 183 ? -14.684 -23.202 26.178  1.00 76.43  ? 185 GLU B CD  1 
ATOM   3077 O OE1 . GLU B 1 183 ? -15.227 -22.096 26.416  1.00 78.44  ? 185 GLU B OE1 1 
ATOM   3078 O OE2 . GLU B 1 183 ? -14.148 -23.482 25.080  1.00 80.44  ? 185 GLU B OE2 1 
ATOM   3079 N N   . ARG B 1 184 ? -11.092 -25.232 28.720  1.00 44.49  ? 186 ARG B N   1 
ATOM   3080 C CA  . ARG B 1 184 ? -10.092 -26.163 28.229  1.00 43.25  ? 186 ARG B CA  1 
ATOM   3081 C C   . ARG B 1 184 ? -9.511  -27.053 29.312  1.00 43.04  ? 186 ARG B C   1 
ATOM   3082 O O   . ARG B 1 184 ? -9.098  -28.172 29.013  1.00 43.46  ? 186 ARG B O   1 
ATOM   3083 C CB  . ARG B 1 184 ? -8.985  -25.403 27.490  1.00 43.49  ? 186 ARG B CB  1 
ATOM   3084 C CG  . ARG B 1 184 ? -9.448  -24.801 26.172  1.00 44.10  ? 186 ARG B CG  1 
ATOM   3085 C CD  . ARG B 1 184 ? -9.500  -25.826 25.042  1.00 44.41  ? 186 ARG B CD  1 
ATOM   3086 N NE  . ARG B 1 184 ? -8.176  -26.282 24.626  1.00 41.71  ? 186 ARG B NE  1 
ATOM   3087 C CZ  . ARG B 1 184 ? -7.499  -25.867 23.562  1.00 42.13  ? 186 ARG B CZ  1 
ATOM   3088 N NH1 . ARG B 1 184 ? -8.014  -24.954 22.742  1.00 43.39  ? 186 ARG B NH1 1 
ATOM   3089 N NH2 . ARG B 1 184 ? -6.302  -26.364 23.300  1.00 40.78  ? 186 ARG B NH2 1 
ATOM   3090 N N   . LEU B 1 185 ? -9.474  -26.589 30.557  1.00 43.27  ? 187 LEU B N   1 
ATOM   3091 C CA  . LEU B 1 185 ? -9.150  -27.457 31.681  1.00 45.21  ? 187 LEU B CA  1 
ATOM   3092 C C   . LEU B 1 185 ? -10.320 -28.439 32.030  1.00 48.96  ? 187 LEU B C   1 
ATOM   3093 O O   . LEU B 1 185 ? -10.120 -29.345 32.820  1.00 48.35  ? 187 LEU B O   1 
ATOM   3094 C CB  . LEU B 1 185 ? -8.777  -26.633 32.922  1.00 44.77  ? 187 LEU B CB  1 
ATOM   3095 C CG  . LEU B 1 185 ? -7.442  -25.830 32.860  1.00 45.23  ? 187 LEU B CG  1 
ATOM   3096 C CD1 . LEU B 1 185 ? -7.374  -24.790 33.958  1.00 44.87  ? 187 LEU B CD1 1 
ATOM   3097 C CD2 . LEU B 1 185 ? -6.213  -26.720 32.932  1.00 45.06  ? 187 LEU B CD2 1 
ATOM   3098 N N   . GLY B 1 186 ? -11.503 -28.249 31.436  1.00 52.25  ? 188 GLY B N   1 
ATOM   3099 C CA  . GLY B 1 186 ? -12.706 -28.998 31.744  1.00 54.71  ? 188 GLY B CA  1 
ATOM   3100 C C   . GLY B 1 186 ? -13.100 -28.854 33.187  1.00 57.96  ? 188 GLY B C   1 
ATOM   3101 O O   . GLY B 1 186 ? -13.474 -29.840 33.809  1.00 58.62  ? 188 GLY B O   1 
ATOM   3102 N N   . LEU B 1 187 ? -13.016 -27.638 33.734  1.00 60.01  ? 189 LEU B N   1 
ATOM   3103 C CA  . LEU B 1 187 ? -13.344 -27.417 35.129  1.00 62.88  ? 189 LEU B CA  1 
ATOM   3104 C C   . LEU B 1 187 ? -14.853 -27.174 35.264  1.00 66.99  ? 189 LEU B C   1 
ATOM   3105 O O   . LEU B 1 187 ? -15.424 -26.467 34.429  1.00 67.82  ? 189 LEU B O   1 
ATOM   3106 C CB  . LEU B 1 187 ? -12.574 -26.222 35.708  1.00 62.50  ? 189 LEU B CB  1 
ATOM   3107 C CG  . LEU B 1 187 ? -11.086 -26.400 36.008  1.00 62.44  ? 189 LEU B CG  1 
ATOM   3108 C CD1 . LEU B 1 187 ? -10.523 -25.160 36.626  1.00 62.21  ? 189 LEU B CD1 1 
ATOM   3109 C CD2 . LEU B 1 187 ? -10.839 -27.538 36.930  1.00 62.61  ? 189 LEU B CD2 1 
ATOM   3110 N N   . PRO B 1 188 ? -15.519 -27.743 36.296  1.00 69.05  ? 190 PRO B N   1 
ATOM   3111 C CA  . PRO B 1 188 ? -16.944 -27.416 36.514  1.00 70.63  ? 190 PRO B CA  1 
ATOM   3112 C C   . PRO B 1 188 ? -17.190 -25.927 36.769  1.00 73.13  ? 190 PRO B C   1 
ATOM   3113 O O   . PRO B 1 188 ? -16.361 -25.295 37.416  1.00 73.85  ? 190 PRO B O   1 
ATOM   3114 C CB  . PRO B 1 188 ? -17.324 -28.212 37.768  1.00 71.06  ? 190 PRO B CB  1 
ATOM   3115 C CG  . PRO B 1 188 ? -16.203 -29.133 38.057  1.00 71.28  ? 190 PRO B CG  1 
ATOM   3116 C CD  . PRO B 1 188 ? -14.999 -28.706 37.292  1.00 69.15  ? 190 PRO B CD  1 
ATOM   3117 N N   . PRO B 1 189 ? -18.303 -25.334 36.294  1.00 74.62  ? 191 PRO B N   1 
ATOM   3118 C CA  . PRO B 1 189 ? -18.622 -23.926 36.659  1.00 75.20  ? 191 PRO B CA  1 
ATOM   3119 C C   . PRO B 1 189 ? -18.689 -23.581 38.152  1.00 75.21  ? 191 PRO B C   1 
ATOM   3120 O O   . PRO B 1 189 ? -18.580 -22.410 38.519  1.00 75.58  ? 191 PRO B O   1 
ATOM   3121 C CB  . PRO B 1 189 ? -20.009 -23.700 36.035  1.00 76.06  ? 191 PRO B CB  1 
ATOM   3122 C CG  . PRO B 1 189 ? -20.119 -24.705 34.949  1.00 76.40  ? 191 PRO B CG  1 
ATOM   3123 C CD  . PRO B 1 189 ? -19.327 -25.902 35.397  1.00 75.00  ? 191 PRO B CD  1 
ATOM   3124 N N   . LYS B 1 190 ? -18.895 -24.589 39.002  1.00 74.60  ? 192 LYS B N   1 
ATOM   3125 C CA  . LYS B 1 190 ? -18.826 -24.439 40.453  1.00 74.12  ? 192 LYS B CA  1 
ATOM   3126 C C   . LYS B 1 190 ? -17.410 -24.066 40.892  1.00 72.82  ? 192 LYS B C   1 
ATOM   3127 O O   . LYS B 1 190 ? -17.238 -23.261 41.812  1.00 73.46  ? 192 LYS B O   1 
ATOM   3128 C CB  . LYS B 1 190 ? -19.229 -25.760 41.138  1.00 76.83  ? 192 LYS B CB  1 
ATOM   3129 C CG  . LYS B 1 190 ? -20.705 -26.104 40.991  1.00 83.47  ? 192 LYS B CG  1 
ATOM   3130 C CD  . LYS B 1 190 ? -20.990 -27.596 41.312  1.00 89.36  ? 192 LYS B CD  1 
ATOM   3131 C CE  . LYS B 1 190 ? -22.462 -27.868 41.550  1.00 92.83  ? 192 LYS B CE  1 
ATOM   3132 N NZ  . LYS B 1 190 ? -22.666 -29.182 42.206  1.00 95.94  ? 192 LYS B NZ  1 
ATOM   3133 N N   . ILE B 1 191 ? -16.393 -24.662 40.237  1.00 70.73  ? 193 ILE B N   1 
ATOM   3134 C CA  . ILE B 1 191 ? -15.000 -24.394 40.565  1.00 68.52  ? 193 ILE B CA  1 
ATOM   3135 C C   . ILE B 1 191 ? -14.693 -23.055 39.935  1.00 66.01  ? 193 ILE B C   1 
ATOM   3136 O O   . ILE B 1 191 ? -14.614 -22.971 38.721  1.00 66.94  ? 193 ILE B O   1 
ATOM   3137 C CB  . ILE B 1 191 ? -14.063 -25.510 40.028  1.00 68.50  ? 193 ILE B CB  1 
ATOM   3138 C CG1 . ILE B 1 191 ? -14.468 -26.902 40.569  1.00 69.20  ? 193 ILE B CG1 1 
ATOM   3139 C CG2 . ILE B 1 191 ? -12.607 -25.191 40.372  1.00 68.65  ? 193 ILE B CG2 1 
ATOM   3140 C CD1 . ILE B 1 191 ? -14.451 -27.094 42.145  1.00 70.52  ? 193 ILE B CD1 1 
ATOM   3141 N N   . VAL B 1 192 ? -14.535 -22.025 40.741  1.00 63.17  ? 194 VAL B N   1 
ATOM   3142 C CA  . VAL B 1 192 ? -14.165 -20.704 40.249  1.00 61.06  ? 194 VAL B CA  1 
ATOM   3143 C C   . VAL B 1 192 ? -12.649 -20.524 40.328  1.00 57.23  ? 194 VAL B C   1 
ATOM   3144 O O   . VAL B 1 192 ? -12.057 -20.873 41.345  1.00 57.54  ? 194 VAL B O   1 
ATOM   3145 C CB  . VAL B 1 192 ? -14.916 -19.582 41.006  1.00 62.21  ? 194 VAL B CB  1 
ATOM   3146 C CG1 . VAL B 1 192 ? -16.420 -19.858 41.053  1.00 62.34  ? 194 VAL B CG1 1 
ATOM   3147 C CG2 . VAL B 1 192 ? -14.342 -19.377 42.405  1.00 63.48  ? 194 VAL B CG2 1 
ATOM   3148 N N   . ILE B 1 193 ? -12.026 -20.003 39.248  1.00 53.50  ? 195 ILE B N   1 
ATOM   3149 C CA  . ILE B 1 193 ? -10.585 -19.694 39.219  1.00 50.36  ? 195 ILE B CA  1 
ATOM   3150 C C   . ILE B 1 193 ? -10.411 -18.188 39.420  1.00 47.63  ? 195 ILE B C   1 
ATOM   3151 O O   . ILE B 1 193 ? -11.305 -17.420 39.073  1.00 47.44  ? 195 ILE B O   1 
ATOM   3152 C CB  . ILE B 1 193 ? -9.870  -20.263 37.958  1.00 49.63  ? 195 ILE B CB  1 
ATOM   3153 C CG1 . ILE B 1 193 ? -10.360 -19.627 36.645  1.00 49.13  ? 195 ILE B CG1 1 
ATOM   3154 C CG2 . ILE B 1 193 ? -10.069 -21.749 37.904  1.00 50.67  ? 195 ILE B CG2 1 
ATOM   3155 C CD1 . ILE B 1 193 ? -9.549  -20.036 35.390  1.00 49.82  ? 195 ILE B CD1 1 
ATOM   3156 N N   . GLY B 1 194 ? -9.288  -17.778 39.983  1.00 45.07  ? 196 GLY B N   1 
ATOM   3157 C CA  . GLY B 1 194 ? -9.027  -16.371 40.237  1.00 42.82  ? 196 GLY B CA  1 
ATOM   3158 C C   . GLY B 1 194 ? -7.808  -15.812 39.503  1.00 41.33  ? 196 GLY B C   1 
ATOM   3159 O O   . GLY B 1 194 ? -6.812  -16.517 39.297  1.00 41.72  ? 196 GLY B O   1 
ATOM   3160 N N   . TYR B 1 195 ? -7.896  -14.510 39.097  1.00 38.75  ? 197 TYR B N   1 
ATOM   3161 C CA  . TYR B 1 195 ? -6.828  -13.745 38.472  1.00 36.27  ? 197 TYR B CA  1 
ATOM   3162 C C   . TYR B 1 195 ? -6.261  -12.807 39.510  1.00 36.20  ? 197 TYR B C   1 
ATOM   3163 O O   . TYR B 1 195 ? -6.996  -12.035 40.097  1.00 35.51  ? 197 TYR B O   1 
ATOM   3164 C CB  . TYR B 1 195 ? -7.325  -12.917 37.293  1.00 34.47  ? 197 TYR B CB  1 
ATOM   3165 C CG  . TYR B 1 195 ? -6.220  -12.180 36.536  1.00 33.68  ? 197 TYR B CG  1 
ATOM   3166 C CD1 . TYR B 1 195 ? -5.566  -12.778 35.470  1.00 33.28  ? 197 TYR B CD1 1 
ATOM   3167 C CD2 . TYR B 1 195 ? -5.852  -10.875 36.880  1.00 33.61  ? 197 TYR B CD2 1 
ATOM   3168 C CE1 . TYR B 1 195 ? -4.560  -12.127 34.775  1.00 34.37  ? 197 TYR B CE1 1 
ATOM   3169 C CE2 . TYR B 1 195 ? -4.839  -10.207 36.193  1.00 34.92  ? 197 TYR B CE2 1 
ATOM   3170 C CZ  . TYR B 1 195 ? -4.197  -10.837 35.126  1.00 35.39  ? 197 TYR B CZ  1 
ATOM   3171 O OH  . TYR B 1 195 ? -3.199  -10.213 34.399  1.00 33.24  ? 197 TYR B OH  1 
ATOM   3172 N N   . GLN B 1 196 ? -4.955  -12.876 39.716  1.00 36.58  ? 198 GLN B N   1 
ATOM   3173 C CA  . GLN B 1 196 ? -4.216  -12.103 40.682  1.00 37.00  ? 198 GLN B CA  1 
ATOM   3174 C C   . GLN B 1 196 ? -3.184  -11.252 39.947  1.00 37.17  ? 198 GLN B C   1 
ATOM   3175 O O   . GLN B 1 196 ? -2.377  -11.772 39.174  1.00 36.12  ? 198 GLN B O   1 
ATOM   3176 C CB  . GLN B 1 196 ? -3.446  -13.029 41.638  1.00 38.61  ? 198 GLN B CB  1 
ATOM   3177 C CG  . GLN B 1 196 ? -4.264  -14.114 42.288  1.00 45.42  ? 198 GLN B CG  1 
ATOM   3178 C CD  . GLN B 1 196 ? -3.392  -15.201 42.908  1.00 54.20  ? 198 GLN B CD  1 
ATOM   3179 O OE1 . GLN B 1 196 ? -2.482  -15.750 42.281  1.00 58.00  ? 198 GLN B OE1 1 
ATOM   3180 N NE2 . GLN B 1 196 ? -3.649  -15.558 44.152  1.00 55.57  ? 198 GLN B NE2 1 
ATOM   3181 N N   . SER B 1 197 ? -3.196  -9.946  40.218  1.00 38.26  ? 199 SER B N   1 
ATOM   3182 C CA  . SER B 1 197 ? -2.142  -9.004  39.836  1.00 40.20  ? 199 SER B CA  1 
ATOM   3183 C C   . SER B 1 197 ? -0.818  -9.480  40.409  1.00 40.95  ? 199 SER B C   1 
ATOM   3184 O O   . SER B 1 197 ? -0.785  -9.931  41.554  1.00 41.84  ? 199 SER B O   1 
ATOM   3185 C CB  . SER B 1 197 ? -2.450  -7.632  40.426  1.00 45.23  ? 199 SER B CB  1 
ATOM   3186 O OG  . SER B 1 197 ? -1.519  -6.645  40.012  1.00 53.04  ? 199 SER B OG  1 
ATOM   3187 N N   . HIS B 1 198 ? 0.250   -9.407  39.642  1.00 40.86  ? 200 HIS B N   1 
ATOM   3188 C CA  . HIS B 1 198 ? 1.569   -9.735  40.180  1.00 41.76  ? 200 HIS B CA  1 
ATOM   3189 C C   . HIS B 1 198 ? 1.973   -8.772  41.320  1.00 44.74  ? 200 HIS B C   1 
ATOM   3190 O O   . HIS B 1 198 ? 2.632   -9.192  42.273  1.00 44.00  ? 200 HIS B O   1 
ATOM   3191 C CB  . HIS B 1 198 ? 2.630   -9.735  39.094  1.00 39.21  ? 200 HIS B CB  1 
ATOM   3192 C CG  . HIS B 1 198 ? 2.492   -10.849 38.101  1.00 37.92  ? 200 HIS B CG  1 
ATOM   3193 N ND1 . HIS B 1 198 ? 2.077   -12.115 38.466  1.00 38.52  ? 200 HIS B ND1 1 
ATOM   3194 C CD2 . HIS B 1 198 ? 2.735   -10.847 36.778  1.00 38.30  ? 200 HIS B CD2 1 
ATOM   3195 C CE1 . HIS B 1 198 ? 2.068   -12.822 37.363  1.00 38.94  ? 200 HIS B CE1 1 
ATOM   3196 N NE2 . HIS B 1 198 ? 2.459   -12.104 36.322  1.00 38.47  ? 200 HIS B NE2 1 
ATOM   3197 N N   . ALA B 1 199 ? 1.591   -7.491  41.209  1.00 47.05  ? 201 ALA B N   1 
ATOM   3198 C CA  . ALA B 1 199 ? 1.834   -6.516  42.280  1.00 49.10  ? 201 ALA B CA  1 
ATOM   3199 C C   . ALA B 1 199 ? 1.140   -6.902  43.628  1.00 51.54  ? 201 ALA B C   1 
ATOM   3200 O O   . ALA B 1 199 ? 1.696   -6.606  44.684  1.00 52.65  ? 201 ALA B O   1 
ATOM   3201 C CB  . ALA B 1 199 ? 1.404   -5.133  41.818  1.00 48.83  ? 201 ALA B CB  1 
ATOM   3202 N N   . ASP B 1 200 ? -0.049  -7.560  43.603  1.00 51.86  ? 202 ASP B N   1 
ATOM   3203 C CA  . ASP B 1 200 ? -0.647  -8.091  44.841  1.00 53.23  ? 202 ASP B CA  1 
ATOM   3204 C C   . ASP B 1 200 ? 0.064   -9.375  45.305  1.00 55.81  ? 202 ASP B C   1 
ATOM   3205 O O   . ASP B 1 200 ? 0.409   -9.493  46.486  1.00 56.97  ? 202 ASP B O   1 
ATOM   3206 C CB  . ASP B 1 200 ? -2.167  -8.367  44.694  1.00 54.24  ? 202 ASP B CB  1 
ATOM   3207 C CG  . ASP B 1 200 ? -2.982  -7.171  44.244  1.00 58.08  ? 202 ASP B CG  1 
ATOM   3208 O OD1 . ASP B 1 200 ? -2.517  -6.033  44.439  1.00 59.02  ? 202 ASP B OD1 1 
ATOM   3209 O OD2 . ASP B 1 200 ? -4.083  -7.377  43.688  1.00 59.49  ? 202 ASP B OD2 1 
ATOM   3210 N N   . THR B 1 201 ? 0.284   -10.337 44.405  1.00 56.48  ? 203 THR B N   1 
ATOM   3211 C CA  . THR B 1 201 ? 1.017   -11.550 44.756  1.00 58.07  ? 203 THR B CA  1 
ATOM   3212 C C   . THR B 1 201 ? 2.428   -11.307 45.310  1.00 58.82  ? 203 THR B C   1 
ATOM   3213 O O   . THR B 1 201 ? 2.914   -12.130 46.095  1.00 58.67  ? 203 THR B O   1 
ATOM   3214 C CB  . THR B 1 201 ? 1.113   -12.484 43.578  1.00 60.76  ? 203 THR B CB  1 
ATOM   3215 O OG1 . THR B 1 201 ? -0.193  -12.664 43.020  1.00 62.66  ? 203 THR B OG1 1 
ATOM   3216 C CG2 . THR B 1 201 ? 1.675   -13.841 43.981  1.00 61.60  ? 203 THR B CG2 1 
ATOM   3217 N N   . ALA B 1 202 ? 3.095   -10.210 44.908  1.00 59.58  ? 204 ALA B N   1 
ATOM   3218 C CA  . ALA B 1 202 ? 4.440   -9.904  45.400  1.00 61.05  ? 204 ALA B CA  1 
ATOM   3219 C C   . ALA B 1 202 ? 4.417   -9.546  46.873  1.00 62.28  ? 204 ALA B C   1 
ATOM   3220 O O   . ALA B 1 202 ? 5.367   -9.870  47.584  1.00 62.96  ? 204 ALA B O   1 
ATOM   3221 C CB  . ALA B 1 202 ? 5.060   -8.768  44.606  1.00 61.34  ? 204 ALA B CB  1 
ATOM   3222 N N   . THR B 1 203 ? 3.340   -8.888  47.337  1.00 62.34  ? 205 THR B N   1 
ATOM   3223 C CA  . THR B 1 203 ? 3.231   -8.475  48.719  1.00 62.59  ? 205 THR B CA  1 
ATOM   3224 C C   . THR B 1 203 ? 2.587   -9.595  49.495  1.00 62.35  ? 205 THR B C   1 
ATOM   3225 O O   . THR B 1 203 ? 1.457   -9.975  49.207  1.00 62.58  ? 205 THR B O   1 
ATOM   3226 C CB  . THR B 1 203 ? 2.451   -7.149  48.866  1.00 64.63  ? 205 THR B CB  1 
ATOM   3227 O OG1 . THR B 1 203 ? 1.048   -7.369  48.737  1.00 66.14  ? 205 THR B OG1 1 
ATOM   3228 C CG2 . THR B 1 203 ? 2.913   -6.079  47.881  1.00 65.51  ? 205 THR B CG2 1 
ATOM   3229 N N   . LYS B 1 204 ? 3.302   -10.124 50.478  1.00 61.82  ? 206 LYS B N   1 
ATOM   3230 C CA  . LYS B 1 204 ? 2.741   -11.106 51.395  1.00 61.47  ? 206 LYS B CA  1 
ATOM   3231 C C   . LYS B 1 204 ? 1.946   -10.344 52.459  1.00 60.95  ? 206 LYS B C   1 
ATOM   3232 O O   . LYS B 1 204 ? 2.522   -9.526  53.167  1.00 59.98  ? 206 LYS B O   1 
ATOM   3233 C CB  . LYS B 1 204 ? 3.874   -11.961 51.992  1.00 62.27  ? 206 LYS B CB  1 
ATOM   3234 C CG  . LYS B 1 204 ? 4.317   -13.172 51.149  1.00 65.74  ? 206 LYS B CG  1 
ATOM   3235 C CD  . LYS B 1 204 ? 4.531   -12.969 49.664  1.00 70.63  ? 206 LYS B CD  1 
ATOM   3236 C CE  . LYS B 1 204 ? 4.541   -14.312 48.951  1.00 73.87  ? 206 LYS B CE  1 
ATOM   3237 N NZ  . LYS B 1 204 ? 4.917   -14.215 47.494  1.00 73.99  ? 206 LYS B NZ  1 
ATOM   3238 N N   . SER B 1 205 ? 0.620   -10.605 52.551  1.00 61.99  ? 207 SER B N   1 
ATOM   3239 C CA  . SER B 1 205 ? -0.295  -9.896  53.461  1.00 64.22  ? 207 SER B CA  1 
ATOM   3240 C C   . SER B 1 205 ? -1.203  -10.820 54.287  1.00 65.22  ? 207 SER B C   1 
ATOM   3241 O O   . SER B 1 205 ? -2.171  -10.339 54.869  1.00 64.95  ? 207 SER B O   1 
ATOM   3242 C CB  . SER B 1 205 ? -1.200  -8.959  52.664  1.00 66.83  ? 207 SER B CB  1 
ATOM   3243 O OG  . SER B 1 205 ? -0.490  -8.169  51.725  1.00 71.46  ? 207 SER B OG  1 
ATOM   3244 N N   . GLY B 1 206 ? -0.900  -12.109 54.344  1.00 66.66  ? 208 GLY B N   1 
ATOM   3245 C CA  . GLY B 1 206 ? -1.739  -13.080 55.038  1.00 68.91  ? 208 GLY B CA  1 
ATOM   3246 C C   . GLY B 1 206 ? -1.713  -14.444 54.378  1.00 71.27  ? 208 GLY B C   1 
ATOM   3247 O O   . GLY B 1 206 ? -0.775  -14.761 53.636  1.00 71.00  ? 208 GLY B O   1 
ATOM   3248 N N   . SER B 1 207 ? -2.754  -15.270 54.646  1.00 73.13  ? 209 SER B N   1 
ATOM   3249 C CA  . SER B 1 207 ? -2.889  -16.616 54.035  1.00 74.59  ? 209 SER B CA  1 
ATOM   3250 C C   . SER B 1 207 ? -3.386  -16.576 52.572  1.00 75.76  ? 209 SER B C   1 
ATOM   3251 O O   . SER B 1 207 ? -3.377  -17.621 51.909  1.00 76.35  ? 209 SER B O   1 
ATOM   3252 C CB  . SER B 1 207 ? -3.802  -17.530 54.866  1.00 76.02  ? 209 SER B CB  1 
ATOM   3253 O OG  . SER B 1 207 ? -4.822  -16.868 55.599  1.00 78.31  ? 209 SER B OG  1 
ATOM   3254 N N   . THR B 1 208 ? -3.812  -15.391 52.063  1.00 75.70  ? 210 THR B N   1 
ATOM   3255 C CA  . THR B 1 208 ? -4.364  -15.277 50.704  1.00 76.08  ? 210 THR B CA  1 
ATOM   3256 C C   . THR B 1 208 ? -3.944  -13.967 50.028  1.00 74.12  ? 210 THR B C   1 
ATOM   3257 O O   . THR B 1 208 ? -3.609  -12.983 50.698  1.00 74.95  ? 210 THR B O   1 
ATOM   3258 C CB  . THR B 1 208 ? -5.914  -15.344 50.727  1.00 78.45  ? 210 THR B CB  1 
ATOM   3259 O OG1 . THR B 1 208 ? -6.408  -14.504 51.788  1.00 80.06  ? 210 THR B OG1 1 
ATOM   3260 C CG2 . THR B 1 208 ? -6.454  -16.804 50.854  1.00 78.42  ? 210 THR B CG2 1 
ATOM   3261 N N   . THR B 1 209 ? -3.959  -13.982 48.697  1.00 70.75  ? 211 THR B N   1 
ATOM   3262 C CA  . THR B 1 209 ? -3.847  -12.799 47.841  1.00 68.21  ? 211 THR B CA  1 
ATOM   3263 C C   . THR B 1 209 ? -5.245  -12.433 47.315  1.00 65.82  ? 211 THR B C   1 
ATOM   3264 O O   . THR B 1 209 ? -6.074  -13.327 47.087  1.00 66.32  ? 211 THR B O   1 
ATOM   3265 C CB  . THR B 1 209 ? -2.878  -13.109 46.689  1.00 67.88  ? 211 THR B CB  1 
ATOM   3266 O OG1 . THR B 1 209 ? -1.641  -13.573 47.253  1.00 68.92  ? 211 THR B OG1 1 
ATOM   3267 C CG2 . THR B 1 209 ? -2.650  -11.920 45.757  1.00 66.88  ? 211 THR B CG2 1 
ATOM   3268 N N   . LYS B 1 210 ? -5.505  -11.127 47.111  1.00 62.84  ? 212 LYS B N   1 
ATOM   3269 C CA  . LYS B 1 210 ? -6.768  -10.721 46.498  1.00 60.99  ? 212 LYS B CA  1 
ATOM   3270 C C   . LYS B 1 210 ? -6.799  -11.112 45.010  1.00 57.57  ? 212 LYS B C   1 
ATOM   3271 O O   . LYS B 1 210 ? -5.794  -11.034 44.316  1.00 58.13  ? 212 LYS B O   1 
ATOM   3272 C CB  . LYS B 1 210 ? -7.081  -9.220  46.696  1.00 64.29  ? 212 LYS B CB  1 
ATOM   3273 C CG  . LYS B 1 210 ? -6.025  -8.257  46.137  1.00 69.18  ? 212 LYS B CG  1 
ATOM   3274 C CD  . LYS B 1 210 ? -6.516  -6.799  46.117  1.00 73.14  ? 212 LYS B CD  1 
ATOM   3275 C CE  . LYS B 1 210 ? -5.728  -5.882  47.044  1.00 76.26  ? 212 LYS B CE  1 
ATOM   3276 N NZ  . LYS B 1 210 ? -5.671  -4.485  46.534  1.00 77.88  ? 212 LYS B NZ  1 
ATOM   3277 N N   . ASN B 1 211 ? -7.945  -11.541 44.551  1.00 54.37  ? 213 ASN B N   1 
ATOM   3278 C CA  . ASN B 1 211 ? -8.262  -11.786 43.154  1.00 52.59  ? 213 ASN B CA  1 
ATOM   3279 C C   . ASN B 1 211 ? -8.884  -10.552 42.502  1.00 52.70  ? 213 ASN B C   1 
ATOM   3280 O O   . ASN B 1 211 ? -9.974  -10.179 42.876  1.00 54.04  ? 213 ASN B O   1 
ATOM   3281 C CB  . ASN B 1 211 ? -9.269  -12.922 43.067  1.00 52.12  ? 213 ASN B CB  1 
ATOM   3282 C CG  . ASN B 1 211 ? -8.762  -14.305 43.396  1.00 55.29  ? 213 ASN B CG  1 
ATOM   3283 O OD1 . ASN B 1 211 ? -9.514  -15.091 43.959  1.00 57.21  ? 213 ASN B OD1 1 
ATOM   3284 N ND2 . ASN B 1 211 ? -7.542  -14.701 43.065  1.00 55.28  ? 213 ASN B ND2 1 
ATOM   3285 N N   . ARG B 1 212 ? -8.217  -9.916  41.552  1.00 52.28  ? 214 ARG B N   1 
ATOM   3286 C CA  . ARG B 1 212 ? -8.811  -8.827  40.781  1.00 52.82  ? 214 ARG B CA  1 
ATOM   3287 C C   . ARG B 1 212 ? -10.055 -9.290  39.963  1.00 51.98  ? 214 ARG B C   1 
ATOM   3288 O O   . ARG B 1 212 ? -11.001 -8.513  39.838  1.00 52.55  ? 214 ARG B O   1 
ATOM   3289 C CB  . ARG B 1 212 ? -7.753  -8.139  39.880  1.00 55.46  ? 214 ARG B CB  1 
ATOM   3290 C CG  . ARG B 1 212 ? -8.155  -6.717  39.451  1.00 61.85  ? 214 ARG B CG  1 
ATOM   3291 C CD  . ARG B 1 212 ? -6.955  -5.841  39.143  1.00 68.11  ? 214 ARG B CD  1 
ATOM   3292 N NE  . ARG B 1 212 ? -6.187  -5.519  40.350  1.00 72.02  ? 214 ARG B NE  1 
ATOM   3293 C CZ  . ARG B 1 212 ? -5.004  -4.905  40.347  1.00 75.70  ? 214 ARG B CZ  1 
ATOM   3294 N NH1 . ARG B 1 212 ? -4.375  -4.653  41.495  1.00 75.89  ? 214 ARG B NH1 1 
ATOM   3295 N NH2 . ARG B 1 212 ? -4.437  -4.539  39.196  1.00 75.35  ? 214 ARG B NH2 1 
ATOM   3296 N N   . PHE B 1 213 ? -10.066 -10.517 39.423  1.00 49.92  ? 215 PHE B N   1 
ATOM   3297 C CA  . PHE B 1 213 ? -11.240 -11.081 38.752  1.00 49.06  ? 215 PHE B CA  1 
ATOM   3298 C C   . PHE B 1 213 ? -11.366 -12.585 39.077  1.00 50.07  ? 215 PHE B C   1 
ATOM   3299 O O   . PHE B 1 213 ? -10.431 -13.217 39.601  1.00 49.73  ? 215 PHE B O   1 
ATOM   3300 C CB  . PHE B 1 213 ? -11.213 -10.871 37.210  1.00 48.53  ? 215 PHE B CB  1 
ATOM   3301 C CG  . PHE B 1 213 ? -10.589 -9.620  36.670  1.00 49.68  ? 215 PHE B CG  1 
ATOM   3302 C CD1 . PHE B 1 213 ? -11.289 -8.423  36.658  1.00 51.31  ? 215 PHE B CD1 1 
ATOM   3303 C CD2 . PHE B 1 213 ? -9.298  -9.629  36.174  1.00 50.58  ? 215 PHE B CD2 1 
ATOM   3304 C CE1 . PHE B 1 213 ? -10.690 -7.249  36.192  1.00 52.14  ? 215 PHE B CE1 1 
ATOM   3305 C CE2 . PHE B 1 213 ? -8.720  -8.464  35.665  1.00 51.45  ? 215 PHE B CE2 1 
ATOM   3306 C CZ  . PHE B 1 213 ? -9.431  -7.287  35.658  1.00 51.64  ? 215 PHE B CZ  1 
ATOM   3307 N N   . VAL B 1 214 ? -12.531 -13.147 38.764  1.00 51.47  ? 216 VAL B N   1 
ATOM   3308 C CA  . VAL B 1 214 ? -12.890 -14.549 39.035  1.00 53.42  ? 216 VAL B CA  1 
ATOM   3309 C C   . VAL B 1 214 ? -13.789 -15.038 37.872  1.00 53.97  ? 216 VAL B C   1 
ATOM   3310 O O   . VAL B 1 214 ? -14.623 -14.284 37.407  1.00 53.92  ? 216 VAL B O   1 
ATOM   3311 C CB  . VAL B 1 214 ? -13.587 -14.679 40.439  1.00 54.96  ? 216 VAL B CB  1 
ATOM   3312 C CG1 . VAL B 1 214 ? -14.052 -16.115 40.711  1.00 56.66  ? 216 VAL B CG1 1 
ATOM   3313 C CG2 . VAL B 1 214 ? -12.662 -14.213 41.557  1.00 54.62  ? 216 VAL B CG2 1 
ATOM   3314 N N   . VAL B 1 215 ? -13.590 -16.289 37.395  1.00 55.19  ? 217 VAL B N   1 
ATOM   3315 C CA  . VAL B 1 215 ? -14.455 -16.936 36.384  1.00 55.92  ? 217 VAL B CA  1 
ATOM   3316 C C   . VAL B 1 215 ? -14.753 -18.391 36.721  1.00 56.75  ? 217 VAL B C   1 
ATOM   3317 O O   . VAL B 1 215 ? -15.677 -18.966 36.104  1.00 57.45  ? 217 VAL B O   1 
ATOM   3318 C CB  . VAL B 1 215 ? -13.876 -16.845 34.961  1.00 56.66  ? 217 VAL B CB  1 
ATOM   3319 C CG1 . VAL B 1 215 ? -13.759 -15.396 34.497  1.00 57.09  ? 217 VAL B CG1 1 
ATOM   3320 C CG2 . VAL B 1 215 ? -12.540 -17.549 34.868  1.00 57.74  ? 217 VAL B CG2 1 
ATOM   3321 O OXT . VAL B 1 215 ? -14.065 -18.969 37.580  1.00 56.64  ? 217 VAL B OXT 1 
HETATM 3322 S S   . DMS C 2 .   ? 28.323  -21.884 10.901  1.00 83.36  ? 301 DMS A S   1 
HETATM 3323 O O   . DMS C 2 .   ? 29.080  -23.021 11.558  1.00 83.20  ? 301 DMS A O   1 
HETATM 3324 C C1  . DMS C 2 .   ? 28.747  -20.415 11.809  1.00 83.37  ? 301 DMS A C1  1 
HETATM 3325 C C2  . DMS C 2 .   ? 29.210  -21.500 9.409   1.00 82.86  ? 301 DMS A C2  1 
HETATM 3326 S S   . DMS D 2 .   ? 23.190  -2.963  -7.641  1.00 91.58  ? 302 DMS A S   1 
HETATM 3327 O O   . DMS D 2 .   ? 22.937  -1.494  -7.405  1.00 91.55  ? 302 DMS A O   1 
HETATM 3328 C C1  . DMS D 2 .   ? 23.966  -3.576  -6.165  1.00 91.07  ? 302 DMS A C1  1 
HETATM 3329 C C2  . DMS D 2 .   ? 21.616  -3.755  -7.452  1.00 91.80  ? 302 DMS A C2  1 
HETATM 3330 C C1  . PGE E 3 .   ? -0.425  -2.694  -4.024  1.00 91.03  ? 303 PGE A C1  1 
HETATM 3331 O O1  . PGE E 3 .   ? 0.712   -3.287  -3.397  1.00 90.80  ? 303 PGE A O1  1 
HETATM 3332 C C2  . PGE E 3 .   ? -0.496  -2.993  -5.496  1.00 91.06  ? 303 PGE A C2  1 
HETATM 3333 O O2  . PGE E 3 .   ? 0.575   -2.358  -6.181  1.00 90.92  ? 303 PGE A O2  1 
HETATM 3334 C C3  . PGE E 3 .   ? 0.895   -2.972  -7.426  1.00 90.39  ? 303 PGE A C3  1 
HETATM 3335 C C4  . PGE E 3 .   ? 2.360   -3.250  -7.505  1.00 89.82  ? 303 PGE A C4  1 
HETATM 3336 O O4  . PGE E 3 .   ? 5.359   -2.039  -10.380 1.00 88.56  ? 303 PGE A O4  1 
HETATM 3337 C C6  . PGE E 3 .   ? 4.142   -2.111  -9.650  1.00 88.68  ? 303 PGE A C6  1 
HETATM 3338 C C5  . PGE E 3 .   ? 4.364   -2.163  -8.158  1.00 88.80  ? 303 PGE A C5  1 
HETATM 3339 O O3  . PGE E 3 .   ? 3.129   -2.055  -7.464  1.00 89.19  ? 303 PGE A O3  1 
HETATM 3340 C C1  . W5K F 4 .   ? 23.162  -5.347  9.466   0.94 36.88  ? 304 W5K A C1  1 
HETATM 3341 C C2  . W5K F 4 .   ? 22.103  -4.380  9.058   0.94 36.15  ? 304 W5K A C2  1 
HETATM 3342 C C3  . W5K F 4 .   ? 20.989  -4.203  10.101  0.94 36.28  ? 304 W5K A C3  1 
HETATM 3343 C C5  . W5K F 4 .   ? 19.941  -2.282  11.301  0.94 41.59  ? 304 W5K A C5  1 
HETATM 3344 C C6  . W5K F 4 .   ? 19.487  -0.884  10.895  0.94 42.16  ? 304 W5K A C6  1 
HETATM 3345 C C7  . W5K F 4 .   ? 20.681  -2.282  12.619  0.94 43.60  ? 304 W5K A C7  1 
HETATM 3346 C C10 . W5K F 4 .   ? 19.249  -6.016  10.218  0.94 31.61  ? 304 W5K A C10 1 
HETATM 3347 C C11 . W5K F 4 .   ? 18.105  -6.663  9.781   0.94 30.65  ? 304 W5K A C11 1 
HETATM 3348 C C12 . W5K F 4 .   ? 17.332  -6.117  8.768   0.94 29.51  ? 304 W5K A C12 1 
HETATM 3349 C C13 . W5K F 4 .   ? 17.790  -4.959  8.149   0.94 31.14  ? 304 W5K A C13 1 
HETATM 3350 C C14 . W5K F 4 .   ? 18.942  -4.310  8.561   0.94 32.46  ? 304 W5K A C14 1 
HETATM 3351 C C16 . W5K F 4 .   ? 18.700  -2.528  6.828   0.94 36.70  ? 304 W5K A C16 1 
HETATM 3352 C C19 . W5K F 4 .   ? 16.133  -6.811  8.224   0.94 28.18  ? 304 W5K A C19 1 
HETATM 3353 C C21 . W5K F 4 .   ? 13.866  -6.682  7.431   0.94 28.04  ? 304 W5K A C21 1 
HETATM 3354 C C22 . W5K F 4 .   ? 13.923  -8.006  7.024   0.94 27.98  ? 304 W5K A C22 1 
HETATM 3355 C C23 . W5K F 4 .   ? 15.079  -8.725  7.204   0.94 27.60  ? 304 W5K A C23 1 
HETATM 3356 C C24 . W5K F 4 .   ? 16.166  -8.123  7.779   0.94 27.40  ? 304 W5K A C24 1 
HETATM 3357 O O4  . W5K F 4 .   ? 20.874  -2.783  10.297  0.94 38.92  ? 304 W5K A O4  1 
HETATM 3358 O O8  . W5K F 4 .   ? 21.972  -1.733  12.436  0.94 45.65  ? 304 W5K A O8  1 
HETATM 3359 C C9  . W5K F 4 .   ? 19.689  -4.839  9.621   0.94 33.02  ? 304 W5K A C9  1 
HETATM 3360 N N15 . W5K F 4 .   ? 19.365  -3.161  7.951   0.94 34.44  ? 304 W5K A N15 1 
HETATM 3361 C C17 . W5K F 4 .   ? 19.425  -1.277  6.379   0.94 38.73  ? 304 W5K A C17 1 
HETATM 3362 O O18 . W5K F 4 .   ? 19.784  -0.481  7.504   0.94 40.18  ? 304 W5K A O18 1 
HETATM 3363 C C20 . W5K F 4 .   ? 14.966  -6.086  7.999   0.94 28.19  ? 304 W5K A C20 1 
HETATM 3364 F F25 . W5K F 4 .   ? 17.288  -8.848  7.969   0.94 25.70  ? 304 W5K A F25 1 
HETATM 3365 H H29 . W5K F 4 .   ? 23.724  -5.558  8.697   0.94 36.90  ? 304 W5K A H29 1 
HETATM 3366 H H28 . W5K F 4 .   ? 22.745  -6.167  9.799   0.94 36.88  ? 304 W5K A H28 1 
HETATM 3367 H H30 . W5K F 4 .   ? 23.711  -4.952  10.172  0.94 36.88  ? 304 W5K A H30 1 
HETATM 3368 H H32 . W5K F 4 .   ? 21.703  -4.688  8.216   0.94 36.14  ? 304 W5K A H32 1 
HETATM 3369 H H31 . W5K F 4 .   ? 22.520  -3.507  8.889   0.94 36.14  ? 304 W5K A H31 1 
HETATM 3370 H H26 . W5K F 4 .   ? 21.267  -4.630  10.951  0.94 36.28  ? 304 W5K A H26 1 
HETATM 3371 H H27 . W5K F 4 .   ? 19.162  -2.885  11.365  0.94 41.59  ? 304 W5K A H27 1 
HETATM 3372 H H35 . W5K F 4 .   ? 20.262  -0.287  10.860  0.94 42.16  ? 304 W5K A H35 1 
HETATM 3373 H H34 . W5K F 4 .   ? 18.845  -0.546  11.549  0.94 42.18  ? 304 W5K A H34 1 
HETATM 3374 H H33 . W5K F 4 .   ? 19.065  -0.921  10.012  0.94 42.16  ? 304 W5K A H33 1 
HETATM 3375 H H37 . W5K F 4 .   ? 20.757  -3.204  12.955  0.94 43.61  ? 304 W5K A H37 1 
HETATM 3376 H H36 . W5K F 4 .   ? 20.184  -1.748  13.278  0.94 43.60  ? 304 W5K A H36 1 
HETATM 3377 H H39 . W5K F 4 .   ? 19.755  -6.394  10.933  0.94 31.61  ? 304 W5K A H39 1 
HETATM 3378 H H40 . W5K F 4 .   ? 17.821  -7.467  10.211  0.94 30.65  ? 304 W5K A H40 1 
HETATM 3379 H H41 . W5K F 4 .   ? 17.288  -4.599  7.420   0.94 31.14  ? 304 W5K A H41 1 
HETATM 3380 H H43 . W5K F 4 .   ? 18.654  -3.164  6.079   0.94 36.71  ? 304 W5K A H43 1 
HETATM 3381 H H44 . W5K F 4 .   ? 17.780  -2.294  7.086   0.94 36.70  ? 304 W5K A H44 1 
HETATM 3382 H H49 . W5K F 4 .   ? 13.067  -6.177  7.299   0.94 28.04  ? 304 W5K A H49 1 
HETATM 3383 H H50 . W5K F 4 .   ? 13.157  -8.421  6.632   0.94 27.98  ? 304 W5K A H50 1 
HETATM 3384 H H51 . W5K F 4 .   ? 15.120  -9.642  6.946   0.94 27.61  ? 304 W5K A H51 1 
HETATM 3385 H H38 . W5K F 4 .   ? 22.510  -2.362  12.198  0.94 45.67  ? 304 W5K A H38 1 
HETATM 3386 H H42 . W5K F 4 .   ? 19.874  -2.637  8.426   0.94 34.44  ? 304 W5K A H42 1 
HETATM 3387 H H46 . W5K F 4 .   ? 18.842  -0.756  5.778   0.94 38.73  ? 304 W5K A H46 1 
HETATM 3388 H H45 . W5K F 4 .   ? 20.237  -1.526  5.879   0.94 38.72  ? 304 W5K A H45 1 
HETATM 3389 H H47 . W5K F 4 .   ? 19.776  0.349   7.274   0.94 40.20  ? 304 W5K A H47 1 
HETATM 3390 H H48 . W5K F 4 .   ? 14.924  -5.170  8.260   0.94 28.22  ? 304 W5K A H48 1 
HETATM 3391 S S   . DMS G 2 .   ? 4.863   -13.556 41.481  1.00 83.18  ? 401 DMS B S   1 
HETATM 3392 O O   . DMS G 2 .   ? 6.018   -13.466 40.519  1.00 83.72  ? 401 DMS B O   1 
HETATM 3393 C C1  . DMS G 2 .   ? 4.245   -11.899 41.647  1.00 82.90  ? 401 DMS B C1  1 
HETATM 3394 C C2  . DMS G 2 .   ? 3.511   -14.247 40.562  1.00 82.65  ? 401 DMS B C2  1 
HETATM 3395 C C1  . PEG H 5 .   ? 3.914   -9.536  24.202  1.00 65.74  ? 402 PEG B C1  1 
HETATM 3396 O O1  . PEG H 5 .   ? 3.196   -10.031 25.321  1.00 65.13  ? 402 PEG B O1  1 
HETATM 3397 C C2  . PEG H 5 .   ? 5.189   -10.300 23.945  1.00 66.26  ? 402 PEG B C2  1 
HETATM 3398 O O2  . PEG H 5 .   ? 6.141   -9.479  23.259  1.00 66.88  ? 402 PEG B O2  1 
HETATM 3399 C C3  . PEG H 5 .   ? 7.297   -10.179 22.810  1.00 67.04  ? 402 PEG B C3  1 
HETATM 3400 C C4  . PEG H 5 .   ? 8.401   -10.070 23.812  1.00 67.04  ? 402 PEG B C4  1 
HETATM 3401 O O4  . PEG H 5 .   ? 8.900   -8.751  23.896  1.00 67.50  ? 402 PEG B O4  1 
HETATM 3402 C C1  . W5K I 4 .   ? 4.361   -31.303 35.028  0.89 42.96  ? 403 W5K B C1  1 
HETATM 3403 C C2  . W5K I 4 .   ? 5.670   -30.625 35.259  0.89 42.27  ? 403 W5K B C2  1 
HETATM 3404 C C3  . W5K I 4 .   ? 6.855   -31.256 34.512  0.89 42.17  ? 403 W5K B C3  1 
HETATM 3405 C C5  . W5K I 4 .   ? 7.819   -33.535 34.685  0.89 47.76  ? 403 W5K B C5  1 
HETATM 3406 C C6  . W5K I 4 .   ? 7.377   -34.802 35.412  0.89 48.71  ? 403 W5K B C6  1 
HETATM 3407 C C7  . W5K I 4 .   ? 8.926   -32.823 35.447  0.89 49.68  ? 403 W5K B C7  1 
HETATM 3408 C C10 . W5K I 4 .   ? 7.732   -29.589 32.887  0.89 36.99  ? 403 W5K B C10 1 
HETATM 3409 C C11 . W5K I 4 .   ? 7.856   -29.022 31.637  0.89 35.83  ? 403 W5K B C11 1 
HETATM 3410 C C12 . W5K I 4 .   ? 7.250   -29.603 30.532  0.89 34.44  ? 403 W5K B C12 1 
HETATM 3411 C C13 . W5K I 4 .   ? 6.484   -30.742 30.721  0.89 35.92  ? 403 W5K B C13 1 
HETATM 3412 C C14 . W5K I 4 .   ? 6.330   -31.330 31.962  0.89 37.60  ? 403 W5K B C14 1 
HETATM 3413 C C16 . W5K I 4 .   ? 5.051   -33.217 30.928  0.89 39.79  ? 403 W5K B C16 1 
HETATM 3414 C C19 . W5K I 4 .   ? 7.352   -28.990 29.179  0.89 32.61  ? 403 W5K B C19 1 
HETATM 3415 C C21 . W5K I 4 .   ? 7.848   -29.203 26.830  0.89 29.95  ? 403 W5K B C21 1 
HETATM 3416 C C22 . W5K I 4 .   ? 7.517   -27.873 26.633  0.89 29.05  ? 403 W5K B C22 1 
HETATM 3417 C C23 . W5K I 4 .   ? 7.111   -27.106 27.694  0.89 29.73  ? 403 W5K B C23 1 
HETATM 3418 C C24 . W5K I 4 .   ? 7.014   -27.666 28.940  0.89 31.28  ? 403 W5K B C24 1 
HETATM 3419 O O4  . W5K I 4 .   ? 6.661   -32.666 34.559  0.89 44.99  ? 403 W5K B O4  1 
HETATM 3420 O O8  . W5K I 4 .   ? 10.045  -33.673 35.626  0.89 51.52  ? 403 W5K B O8  1 
HETATM 3421 C C9  . W5K I 4 .   ? 6.969   -30.736 33.086  0.89 38.96  ? 403 W5K B C9  1 
HETATM 3422 N N15 . W5K I 4 .   ? 5.555   -32.457 32.060  0.89 38.48  ? 403 W5K B N15 1 
HETATM 3423 C C17 . W5K I 4 .   ? 3.877   -34.107 31.313  0.89 41.21  ? 403 W5K B C17 1 
HETATM 3424 O O18 . W5K I 4 .   ? 4.102   -34.745 32.560  0.89 41.74  ? 403 W5K B O18 1 
HETATM 3425 C C20 . W5K I 4 .   ? 7.756   -29.765 28.093  0.89 30.93  ? 403 W5K B C20 1 
HETATM 3426 F F25 . W5K I 4 .   ? 6.628   -26.895 29.985  0.89 30.59  ? 403 W5K B F25 1 
HETATM 3427 H H29 . W5K I 4 .   ? 3.632   -30.694 35.260  0.89 42.97  ? 403 W5K B H29 1 
HETATM 3428 H H28 . W5K I 4 .   ? 4.304   -32.102 35.585  0.89 42.99  ? 403 W5K B H28 1 
HETATM 3429 H H30 . W5K I 4 .   ? 4.285   -31.556 34.087  0.89 42.95  ? 403 W5K B H30 1 
HETATM 3430 H H32 . W5K I 4 .   ? 5.864   -30.637 36.225  0.89 42.25  ? 403 W5K B H32 1 
HETATM 3431 H H31 . W5K I 4 .   ? 5.590   -29.683 34.984  0.89 42.26  ? 403 W5K B H31 1 
HETATM 3432 H H26 . W5K I 4 .   ? 7.674   -31.028 34.993  0.89 42.18  ? 403 W5K B H26 1 
HETATM 3433 H H27 . W5K I 4 .   ? 8.148   -33.769 33.782  0.89 47.76  ? 403 W5K B H27 1 
HETATM 3434 H H35 . W5K I 4 .   ? 7.217   -34.597 36.354  0.89 48.72  ? 403 W5K B H35 1 
HETATM 3435 H H34 . W5K I 4 .   ? 8.078   -35.482 35.341  0.89 48.71  ? 403 W5K B H34 1 
HETATM 3436 H H33 . W5K I 4 .   ? 6.552   -35.140 35.007  0.89 48.71  ? 403 W5K B H33 1 
HETATM 3437 H H37 . W5K I 4 .   ? 8.587   -32.536 36.327  0.89 49.68  ? 403 W5K B H37 1 
HETATM 3438 H H36 . W5K I 4 .   ? 9.212   -32.028 34.948  0.89 49.69  ? 403 W5K B H36 1 
HETATM 3439 H H39 . W5K I 4 .   ? 8.158   -29.177 33.634  0.89 36.95  ? 403 W5K B H39 1 
HETATM 3440 H H40 . W5K I 4 .   ? 8.382   -28.234 31.527  0.89 35.84  ? 403 W5K B H40 1 
HETATM 3441 H H41 . W5K I 4 .   ? 6.051   -31.131 29.965  0.89 35.93  ? 403 W5K B H41 1 
HETATM 3442 H H43 . W5K I 4 .   ? 4.764   -32.596 30.224  0.89 39.78  ? 403 W5K B H43 1 
HETATM 3443 H H44 . W5K I 4 .   ? 5.776   -33.776 30.564  0.89 39.78  ? 403 W5K B H44 1 
HETATM 3444 H H49 . W5K I 4 .   ? 8.124   -29.738 26.090  0.89 29.96  ? 403 W5K B H49 1 
HETATM 3445 H H50 . W5K I 4 .   ? 7.576   -27.490 25.762  0.89 29.06  ? 403 W5K B H50 1 
HETATM 3446 H H51 . W5K I 4 .   ? 6.886   -26.188 27.564  0.89 29.73  ? 403 W5K B H51 1 
HETATM 3447 H H38 . W5K I 4 .   ? 10.154  -34.133 34.918  0.89 51.53  ? 403 W5K B H38 1 
HETATM 3448 H H42 . W5K I 4 .   ? 5.329   -32.727 32.860  0.89 38.47  ? 403 W5K B H42 1 
HETATM 3449 H H46 . W5K I 4 .   ? 3.745   -34.790 30.617  0.89 41.22  ? 403 W5K B H46 1 
HETATM 3450 H H45 . W5K I 4 .   ? 3.056   -33.562 31.367  0.89 41.21  ? 403 W5K B H45 1 
HETATM 3451 H H47 . W5K I 4 .   ? 3.829   -34.225 33.190  0.89 41.73  ? 403 W5K B H47 1 
HETATM 3452 H H48 . W5K I 4 .   ? 7.981   -30.682 28.222  0.89 30.90  ? 403 W5K B H48 1 
HETATM 3453 O O   . HOH J 6 .   ? 40.689  -16.736 7.044   1.00 58.92  ? 401 HOH A O   1 
HETATM 3454 O O   . HOH J 6 .   ? 17.061  5.509   14.964  1.00 63.85  ? 402 HOH A O   1 
HETATM 3455 O O   . HOH J 6 .   ? 27.727  -0.496  -1.803  1.00 53.26  ? 403 HOH A O   1 
HETATM 3456 O O   . HOH J 6 .   ? 18.889  -27.148 22.615  1.00 61.00  ? 404 HOH A O   1 
HETATM 3457 O O   . HOH J 6 .   ? 34.047  -26.157 2.474   1.00 33.25  ? 405 HOH A O   1 
HETATM 3458 O O   . HOH J 6 .   ? 23.009  -0.883  9.339   1.00 45.07  ? 406 HOH A O   1 
HETATM 3459 O O   . HOH J 6 .   ? 26.579  0.684   5.414   1.00 39.74  ? 407 HOH A O   1 
HETATM 3460 O O   . HOH J 6 .   ? 10.121  -16.076 -0.962  1.00 25.22  ? 408 HOH A O   1 
HETATM 3461 O O   . HOH J 6 .   ? 13.650  -19.324 10.600  1.00 21.00  ? 409 HOH A O   1 
HETATM 3462 O O   . HOH J 6 .   ? -5.654  -9.475  -5.731  1.00 51.60  ? 410 HOH A O   1 
HETATM 3463 O O   . HOH J 6 .   ? 19.001  4.696   15.996  1.00 60.88  ? 411 HOH A O   1 
HETATM 3464 O O   . HOH J 6 .   ? 22.529  -26.550 -1.264  1.00 18.13  ? 412 HOH A O   1 
HETATM 3465 O O   . HOH J 6 .   ? 16.257  -24.103 19.959  1.00 47.04  ? 413 HOH A O   1 
HETATM 3466 O O   . HOH J 6 .   ? 25.938  0.451   1.986   1.00 26.39  ? 414 HOH A O   1 
HETATM 3467 O O   . HOH J 6 .   ? 5.207   -1.807  3.390   1.00 48.60  ? 415 HOH A O   1 
HETATM 3468 O O   . HOH J 6 .   ? 27.868  -29.048 6.495   1.00 30.65  ? 416 HOH A O   1 
HETATM 3469 O O   . HOH J 6 .   ? 7.081   -9.062  9.929   1.00 53.08  ? 417 HOH A O   1 
HETATM 3470 O O   . HOH J 6 .   ? 24.976  -24.499 -11.750 1.00 46.38  ? 418 HOH A O   1 
HETATM 3471 O O   . HOH J 6 .   ? 27.714  -14.235 7.572   1.00 22.49  ? 419 HOH A O   1 
HETATM 3472 O O   . HOH J 6 .   ? 35.446  -13.880 2.288   1.00 52.96  ? 420 HOH A O   1 
HETATM 3473 O O   . HOH J 6 .   ? 5.597   -21.274 6.948   1.00 52.66  ? 421 HOH A O   1 
HETATM 3474 O O   . HOH J 6 .   ? 11.737  -0.405  -9.242  1.00 49.82  ? 422 HOH A O   1 
HETATM 3475 O O   . HOH J 6 .   ? 11.488  -21.920 -10.511 1.00 52.24  ? 423 HOH A O   1 
HETATM 3476 O O   . HOH J 6 .   ? 23.302  -17.493 12.462  1.00 46.47  ? 424 HOH A O   1 
HETATM 3477 O O   . HOH J 6 .   ? 21.046  -14.218 13.859  1.00 37.67  ? 425 HOH A O   1 
HETATM 3478 O O   . HOH J 6 .   ? 29.286  -33.916 2.668   1.00 56.21  ? 426 HOH A O   1 
HETATM 3479 O O   . HOH J 6 .   ? 30.131  -22.439 6.235   1.00 35.87  ? 427 HOH A O   1 
HETATM 3480 O O   . HOH J 6 .   ? 12.398  -21.538 -1.950  1.00 27.26  ? 428 HOH A O   1 
HETATM 3481 O O   . HOH J 6 .   ? 22.723  -23.853 5.665   1.00 25.00  ? 429 HOH A O   1 
HETATM 3482 O O   . HOH J 6 .   ? 20.971  -6.550  -7.404  1.00 28.97  ? 430 HOH A O   1 
HETATM 3483 O O   . HOH J 6 .   ? 27.340  -16.895 8.220   1.00 21.95  ? 431 HOH A O   1 
HETATM 3484 O O   . HOH J 6 .   ? 28.668  -14.150 -11.145 1.00 32.17  ? 432 HOH A O   1 
HETATM 3485 O O   . HOH J 6 .   ? 33.074  -4.265  7.638   1.00 50.39  ? 433 HOH A O   1 
HETATM 3486 O O   . HOH J 6 .   ? 14.691  -12.542 -8.708  1.00 38.68  ? 434 HOH A O   1 
HETATM 3487 O O   . HOH J 6 .   ? 14.475  -16.840 -10.151 1.00 42.78  ? 435 HOH A O   1 
HETATM 3488 O O   . HOH J 6 .   ? 14.443  -27.143 10.144  1.00 41.70  ? 436 HOH A O   1 
HETATM 3489 O O   . HOH J 6 .   ? 19.248  -7.997  -5.015  1.00 23.41  ? 437 HOH A O   1 
HETATM 3490 O O   . HOH J 6 .   ? 3.176   -11.099 6.762   1.00 39.60  ? 438 HOH A O   1 
HETATM 3491 O O   . HOH J 6 .   ? 14.678  -10.231 -6.094  1.00 32.78  ? 439 HOH A O   1 
HETATM 3492 O O   . HOH J 6 .   ? 7.380   -18.616 -11.940 1.00 53.80  ? 440 HOH A O   1 
HETATM 3493 O O   . HOH J 6 .   ? 21.232  -29.771 5.980   1.00 27.08  ? 441 HOH A O   1 
HETATM 3494 O O   . HOH J 6 .   ? 18.483  -30.752 2.921   1.00 42.61  ? 442 HOH A O   1 
HETATM 3495 O O   . HOH J 6 .   ? 37.495  -22.611 10.519  1.00 55.10  ? 443 HOH A O   1 
HETATM 3496 O O   . HOH J 6 .   ? 33.762  1.106   -0.543  1.00 67.78  ? 444 HOH A O   1 
HETATM 3497 O O   . HOH J 6 .   ? 39.999  -22.880 10.398  1.00 49.26  ? 445 HOH A O   1 
HETATM 3498 O O   . HOH J 6 .   ? 8.493   -14.683 -3.672  1.00 27.72  ? 446 HOH A O   1 
HETATM 3499 O O   . HOH J 6 .   ? 2.881   -1.471  -3.794  1.00 74.51  ? 447 HOH A O   1 
HETATM 3500 O O   . HOH J 6 .   ? 16.134  -17.328 -3.039  1.00 31.71  ? 448 HOH A O   1 
HETATM 3501 O O   . HOH J 6 .   ? 1.815   -1.159  -0.509  1.00 54.09  ? 449 HOH A O   1 
HETATM 3502 O O   . HOH J 6 .   ? 32.086  -20.086 12.893  1.00 55.26  ? 450 HOH A O   1 
HETATM 3503 O O   . HOH J 6 .   ? 29.409  -3.636  -5.794  1.00 65.52  ? 451 HOH A O   1 
HETATM 3504 O O   . HOH J 6 .   ? 18.777  1.324   -6.669  1.00 52.96  ? 452 HOH A O   1 
HETATM 3505 O O   . HOH J 6 .   ? 16.333  -2.987  -10.438 1.00 51.36  ? 453 HOH A O   1 
HETATM 3506 O O   . HOH J 6 .   ? 11.944  -23.976 0.322   1.00 33.54  ? 454 HOH A O   1 
HETATM 3507 O O   . HOH J 6 .   ? 34.260  -21.149 -10.874 1.00 68.50  ? 455 HOH A O   1 
HETATM 3508 O O   . HOH J 6 .   ? 15.677  -25.542 2.218   1.00 41.59  ? 456 HOH A O   1 
HETATM 3509 O O   . HOH J 6 .   ? 16.702  -29.605 13.347  1.00 63.46  ? 457 HOH A O   1 
HETATM 3510 O O   . HOH J 6 .   ? 18.634  -12.130 -10.731 1.00 44.22  ? 458 HOH A O   1 
HETATM 3511 O O   . HOH J 6 .   ? 16.327  -8.524  -10.666 1.00 37.74  ? 459 HOH A O   1 
HETATM 3512 O O   . HOH J 6 .   ? 34.668  -15.808 0.495   1.00 45.65  ? 460 HOH A O   1 
HETATM 3513 O O   . HOH J 6 .   ? 14.877  -6.235  -11.783 1.00 47.85  ? 461 HOH A O   1 
HETATM 3514 O O   . HOH J 6 .   ? 12.073  -5.358  -14.416 1.00 62.75  ? 462 HOH A O   1 
HETATM 3515 O O   . HOH J 6 .   ? 17.256  -14.040 -11.260 1.00 49.91  ? 463 HOH A O   1 
HETATM 3516 O O   . HOH J 6 .   ? 13.522  -26.706 -14.397 0.50 29.79  ? 464 HOH A O   1 
HETATM 3517 O O   . HOH J 6 .   ? 9.479   -22.657 4.916   1.00 41.24  ? 465 HOH A O   1 
HETATM 3518 O O   . HOH J 6 .   ? 23.587  -4.676  15.211  1.00 67.96  ? 466 HOH A O   1 
HETATM 3519 O O   . HOH J 6 .   ? 35.535  -14.184 6.970   1.00 51.19  ? 467 HOH A O   1 
HETATM 3520 O O   . HOH J 6 .   ? 7.740   -21.070 3.920   1.00 36.19  ? 468 HOH A O   1 
HETATM 3521 O O   . HOH J 6 .   ? 24.335  -31.207 -8.554  1.00 33.28  ? 469 HOH A O   1 
HETATM 3522 O O   . HOH J 6 .   ? 11.363  -28.148 3.453   1.00 62.63  ? 470 HOH A O   1 
HETATM 3523 O O   . HOH J 6 .   ? 13.839  -25.306 13.712  1.00 69.46  ? 471 HOH A O   1 
HETATM 3524 O O   . HOH J 6 .   ? 27.299  -7.368  -11.786 1.00 48.23  ? 472 HOH A O   1 
HETATM 3525 O O   . HOH J 6 .   ? 14.509  -18.605 -1.376  1.00 29.27  ? 473 HOH A O   1 
HETATM 3526 O O   . HOH J 6 .   ? 10.498  1.507   17.495  1.00 63.53  ? 474 HOH A O   1 
HETATM 3527 O O   . HOH J 6 .   ? 22.568  -29.651 -7.448  1.00 36.18  ? 475 HOH A O   1 
HETATM 3528 O O   . HOH J 6 .   ? 5.120   -11.348 12.920  1.00 53.02  ? 476 HOH A O   1 
HETATM 3529 O O   . HOH J 6 .   ? 25.776  -22.338 14.469  1.00 45.14  ? 477 HOH A O   1 
HETATM 3530 O O   . HOH J 6 .   ? 45.960  -19.407 4.907   1.00 60.31  ? 478 HOH A O   1 
HETATM 3531 O O   . HOH J 6 .   ? 43.432  -5.527  7.619   1.00 71.94  ? 479 HOH A O   1 
HETATM 3532 O O   . HOH J 6 .   ? 32.292  -13.118 -12.238 1.00 50.02  ? 480 HOH A O   1 
HETATM 3533 O O   . HOH J 6 .   ? 27.099  1.239   8.439   1.00 50.08  ? 481 HOH A O   1 
HETATM 3534 O O   . HOH J 6 .   ? 37.959  -16.577 -0.955  1.00 66.49  ? 482 HOH A O   1 
HETATM 3535 O O   . HOH J 6 .   ? 3.216   -19.851 -1.799  1.00 50.42  ? 483 HOH A O   1 
HETATM 3536 O O   . HOH J 6 .   ? 34.032  -24.334 -7.933  1.00 50.28  ? 484 HOH A O   1 
HETATM 3537 O O   . HOH J 6 .   ? -1.661  -10.462 -5.337  1.00 51.22  ? 485 HOH A O   1 
HETATM 3538 O O   . HOH J 6 .   ? 8.172   -25.064 6.540   1.00 52.25  ? 486 HOH A O   1 
HETATM 3539 O O   . HOH J 6 .   ? 6.076   -3.060  -13.611 1.00 61.81  ? 487 HOH A O   1 
HETATM 3540 O O   . HOH J 6 .   ? 41.379  -21.380 1.608   1.00 51.38  ? 488 HOH A O   1 
HETATM 3541 O O   . HOH J 6 .   ? 43.266  -9.626  8.228   1.00 52.82  ? 489 HOH A O   1 
HETATM 3542 O O   . HOH J 6 .   ? -6.782  -5.645  -4.050  1.00 47.70  ? 490 HOH A O   1 
HETATM 3543 O O   . HOH J 6 .   ? -1.697  -3.106  5.300   1.00 69.28  ? 491 HOH A O   1 
HETATM 3544 O O   . HOH J 6 .   ? 28.488  -31.512 5.219   1.00 43.19  ? 492 HOH A O   1 
HETATM 3545 O O   . HOH J 6 .   ? 39.891  -21.477 -2.410  1.00 62.21  ? 493 HOH A O   1 
HETATM 3546 O O   . HOH J 6 .   ? 9.589   -5.186  15.530  1.00 62.92  ? 494 HOH A O   1 
HETATM 3547 O O   . HOH J 6 .   ? 29.934  -11.147 -11.702 1.00 59.32  ? 495 HOH A O   1 
HETATM 3548 O O   . HOH J 6 .   ? 27.279  -17.295 11.026  1.00 33.43  ? 496 HOH A O   1 
HETATM 3549 O O   . HOH J 6 .   ? 27.065  -19.592 29.388  1.00 50.88  ? 497 HOH A O   1 
HETATM 3550 O O   . HOH J 6 .   ? 32.640  5.496   3.253   1.00 54.78  ? 498 HOH A O   1 
HETATM 3551 O O   . HOH J 6 .   ? 21.643  -8.341  -11.853 1.00 53.30  ? 499 HOH A O   1 
HETATM 3552 O O   . HOH J 6 .   ? 32.994  -32.386 6.039   1.00 59.32  ? 500 HOH A O   1 
HETATM 3553 O O   . HOH J 6 .   ? 18.457  -7.813  -11.131 1.00 48.01  ? 501 HOH A O   1 
HETATM 3554 O O   . HOH J 6 .   ? 16.827  -24.606 -12.175 1.00 48.92  ? 502 HOH A O   1 
HETATM 3555 O O   . HOH J 6 .   ? 27.211  3.892   7.666   1.00 42.01  ? 503 HOH A O   1 
HETATM 3556 O O   . HOH J 6 .   ? 18.172  -26.208 19.582  1.00 57.13  ? 504 HOH A O   1 
HETATM 3557 O O   . HOH J 6 .   ? 38.414  -29.933 4.425   1.00 54.19  ? 505 HOH A O   1 
HETATM 3558 O O   . HOH J 6 .   ? 22.456  -16.279 14.856  1.00 46.97  ? 506 HOH A O   1 
HETATM 3559 O O   . HOH J 6 .   ? 36.024  -16.742 7.411   1.00 60.71  ? 507 HOH A O   1 
HETATM 3560 O O   . HOH J 6 .   ? 20.949  -6.240  -10.252 1.00 44.47  ? 508 HOH A O   1 
HETATM 3561 O O   . HOH J 6 .   ? 12.945  -25.613 4.228   1.00 52.42  ? 509 HOH A O   1 
HETATM 3562 O O   . HOH J 6 .   ? 6.868   -4.840  11.749  1.00 47.10  ? 510 HOH A O   1 
HETATM 3563 O O   . HOH J 6 .   ? 14.728  -13.363 -10.899 1.00 53.85  ? 511 HOH A O   1 
HETATM 3564 O O   . HOH J 6 .   ? 12.666  -29.172 -1.553  1.00 48.32  ? 512 HOH A O   1 
HETATM 3565 O O   . HOH J 6 .   ? 38.042  -11.186 8.831   1.00 70.24  ? 513 HOH A O   1 
HETATM 3566 O O   . HOH J 6 .   ? -5.235  -4.867  -6.461  1.00 66.88  ? 514 HOH A O   1 
HETATM 3567 O O   . HOH K 6 .   ? 0.627   -2.771  30.016  1.00 52.77  ? 501 HOH B O   1 
HETATM 3568 O O   . HOH K 6 .   ? -4.938  -9.204  42.370  1.00 38.70  ? 502 HOH B O   1 
HETATM 3569 O O   . HOH K 6 .   ? -2.949  -2.023  38.106  1.00 49.31  ? 503 HOH B O   1 
HETATM 3570 O O   . HOH K 6 .   ? 17.573  -20.403 21.062  1.00 40.56  ? 504 HOH B O   1 
HETATM 3571 O O   . HOH K 6 .   ? -2.223  -3.748  43.486  1.00 58.41  ? 505 HOH B O   1 
HETATM 3572 O O   . HOH K 6 .   ? 11.120  -16.439 27.516  1.00 32.66  ? 506 HOH B O   1 
HETATM 3573 O O   . HOH K 6 .   ? -3.486  -8.921  30.193  1.00 31.25  ? 507 HOH B O   1 
HETATM 3574 O O   . HOH K 6 .   ? 4.890   -18.479 12.654  1.00 51.64  ? 508 HOH B O   1 
HETATM 3575 O O   . HOH K 6 .   ? -15.817 -24.776 32.620  1.00 54.81  ? 509 HOH B O   1 
HETATM 3576 O O   . HOH K 6 .   ? 8.441   -13.264 21.391  1.00 49.13  ? 510 HOH B O   1 
HETATM 3577 O O   . HOH K 6 .   ? 2.171   -21.190 38.959  1.00 27.60  ? 511 HOH B O   1 
HETATM 3578 O O   . HOH K 6 .   ? -5.919  -13.148 53.890  1.00 71.10  ? 512 HOH B O   1 
HETATM 3579 O O   . HOH K 6 .   ? 2.529   -11.655 33.580  1.00 28.65  ? 513 HOH B O   1 
HETATM 3580 O O   . HOH K 6 .   ? -7.860  -19.845 41.600  1.00 49.91  ? 514 HOH B O   1 
HETATM 3581 O O   . HOH K 6 .   ? 2.686   -18.568 38.892  1.00 26.73  ? 515 HOH B O   1 
HETATM 3582 O O   . HOH K 6 .   ? 13.150  -27.086 21.557  1.00 52.38  ? 516 HOH B O   1 
HETATM 3583 O O   . HOH K 6 .   ? -9.138  -29.147 26.564  1.00 48.00  ? 517 HOH B O   1 
HETATM 3584 O O   . HOH K 6 .   ? 2.585   -11.978 21.566  1.00 56.09  ? 518 HOH B O   1 
HETATM 3585 O O   . HOH K 6 .   ? 0.094   -14.092 20.823  1.00 39.01  ? 519 HOH B O   1 
HETATM 3586 O O   . HOH K 6 .   ? -2.587  -35.908 35.372  1.00 36.97  ? 520 HOH B O   1 
HETATM 3587 O O   . HOH K 6 .   ? 3.520   -5.864  32.058  1.00 39.08  ? 521 HOH B O   1 
HETATM 3588 O O   . HOH K 6 .   ? 10.386  -21.351 36.185  1.00 56.37  ? 522 HOH B O   1 
HETATM 3589 O O   . HOH K 6 .   ? 4.004   -38.837 23.103  1.00 73.11  ? 523 HOH B O   1 
HETATM 3590 O O   . HOH K 6 .   ? 10.214  -8.578  27.871  1.00 50.20  ? 524 HOH B O   1 
HETATM 3591 O O   . HOH K 6 .   ? -6.672  -23.415 20.064  1.00 43.71  ? 525 HOH B O   1 
HETATM 3592 O O   . HOH K 6 .   ? 11.582  -24.972 16.818  1.00 35.17  ? 526 HOH B O   1 
HETATM 3593 O O   . HOH K 6 .   ? -5.802  -1.554  26.914  1.00 61.74  ? 527 HOH B O   1 
HETATM 3594 O O   . HOH K 6 .   ? 2.357   -19.861 19.397  1.00 26.83  ? 528 HOH B O   1 
HETATM 3595 O O   . HOH K 6 .   ? -6.090  -14.931 56.987  1.00 60.22  ? 529 HOH B O   1 
HETATM 3596 O O   . HOH K 6 .   ? -7.371  -34.697 34.706  1.00 70.58  ? 530 HOH B O   1 
HETATM 3597 O O   . HOH K 6 .   ? -4.748  -25.307 21.193  1.00 33.73  ? 531 HOH B O   1 
HETATM 3598 O O   . HOH K 6 .   ? 0.486   -13.113 40.419  1.00 45.41  ? 532 HOH B O   1 
HETATM 3599 O O   . HOH K 6 .   ? 1.086   -6.274  38.423  1.00 40.88  ? 533 HOH B O   1 
HETATM 3600 O O   . HOH K 6 .   ? -5.754  -27.511 25.903  1.00 31.86  ? 534 HOH B O   1 
HETATM 3601 O O   . HOH K 6 .   ? 8.196   -18.125 37.099  1.00 47.06  ? 535 HOH B O   1 
HETATM 3602 O O   . HOH K 6 .   ? -2.420  -18.454 23.938  1.00 30.81  ? 536 HOH B O   1 
HETATM 3603 O O   . HOH K 6 .   ? 0.504   -21.149 16.839  1.00 29.83  ? 537 HOH B O   1 
HETATM 3604 O O   . HOH K 6 .   ? -1.921  -3.505  40.559  1.00 58.79  ? 538 HOH B O   1 
HETATM 3605 O O   . HOH K 6 .   ? 11.369  -20.159 12.033  1.00 33.93  ? 539 HOH B O   1 
HETATM 3606 O O   . HOH K 6 .   ? 8.776   -13.717 39.747  1.00 57.66  ? 540 HOH B O   1 
HETATM 3607 O O   . HOH K 6 .   ? -8.146  -18.860 19.354  1.00 44.35  ? 541 HOH B O   1 
HETATM 3608 O O   . HOH K 6 .   ? 5.628   -5.935  21.833  1.00 58.75  ? 542 HOH B O   1 
HETATM 3609 O O   . HOH K 6 .   ? 7.537   -14.908 19.075  1.00 46.24  ? 543 HOH B O   1 
HETATM 3610 O O   . HOH K 6 .   ? 0.164   -11.346 8.088   1.00 53.58  ? 544 HOH B O   1 
HETATM 3611 O O   . HOH K 6 .   ? 16.289  -15.483 26.077  1.00 48.90  ? 545 HOH B O   1 
HETATM 3612 O O   . HOH K 6 .   ? 13.482  -15.556 26.359  1.00 49.16  ? 546 HOH B O   1 
HETATM 3613 O O   . HOH K 6 .   ? -6.386  -35.563 17.896  1.00 47.96  ? 547 HOH B O   1 
HETATM 3614 O O   . HOH K 6 .   ? -0.724  -12.411 50.333  1.00 48.54  ? 548 HOH B O   1 
HETATM 3615 O O   . HOH K 6 .   ? -9.569  -27.097 20.663  1.00 37.83  ? 549 HOH B O   1 
HETATM 3616 O O   . HOH K 6 .   ? 9.276   0.103   36.706  1.00 66.50  ? 550 HOH B O   1 
HETATM 3617 O O   . HOH K 6 .   ? -0.185  -17.235 23.034  1.00 41.00  ? 551 HOH B O   1 
HETATM 3618 O O   . HOH K 6 .   ? -10.816 -8.886  15.223  1.00 49.73  ? 552 HOH B O   1 
HETATM 3619 O O   . HOH K 6 .   ? 4.107   -38.749 35.691  1.00 42.51  ? 553 HOH B O   1 
HETATM 3620 O O   . HOH K 6 .   ? -8.589  -33.910 27.983  1.00 64.47  ? 554 HOH B O   1 
HETATM 3621 O O   . HOH K 6 .   ? -9.265  -21.157 20.052  1.00 66.30  ? 555 HOH B O   1 
HETATM 3622 O O   . HOH K 6 .   ? -10.787 -23.419 22.887  1.00 57.26  ? 556 HOH B O   1 
HETATM 3623 O O   . HOH K 6 .   ? 20.495  -20.453 30.879  1.00 57.87  ? 557 HOH B O   1 
HETATM 3624 O O   . HOH K 6 .   ? -10.254 -29.995 19.486  1.00 61.19  ? 558 HOH B O   1 
HETATM 3625 O O   . HOH K 6 .   ? -15.578 -27.685 30.144  1.00 45.60  ? 559 HOH B O   1 
HETATM 3626 O O   . HOH K 6 .   ? 5.118   -18.412 40.227  1.00 36.01  ? 560 HOH B O   1 
HETATM 3627 O O   . HOH K 6 .   ? 12.578  -5.896  30.983  1.00 55.64  ? 561 HOH B O   1 
HETATM 3628 O O   . HOH K 6 .   ? -14.676 -10.812 38.024  1.00 44.50  ? 562 HOH B O   1 
HETATM 3629 O O   . HOH K 6 .   ? 5.064   -8.209  20.452  1.00 72.59  ? 563 HOH B O   1 
HETATM 3630 O O   . HOH K 6 .   ? 0.834   -24.209 47.928  1.00 62.30  ? 564 HOH B O   1 
HETATM 3631 O O   . HOH K 6 .   ? -8.639  -5.688  27.413  1.00 36.79  ? 565 HOH B O   1 
HETATM 3632 O O   . HOH K 6 .   ? -4.493  -37.285 18.166  1.00 54.66  ? 566 HOH B O   1 
HETATM 3633 O O   . HOH K 6 .   ? -10.174 -32.214 21.282  1.00 40.31  ? 567 HOH B O   1 
HETATM 3634 O O   . HOH K 6 .   ? 7.831   -20.764 47.312  1.00 55.67  ? 568 HOH B O   1 
HETATM 3635 O O   . HOH K 6 .   ? -23.349 -31.839 44.290  1.00 55.16  ? 569 HOH B O   1 
HETATM 3636 O O   . HOH K 6 .   ? 2.169   -12.588 18.113  1.00 59.26  ? 570 HOH B O   1 
HETATM 3637 O O   . HOH K 6 .   ? 8.478   -41.456 33.177  1.00 54.36  ? 571 HOH B O   1 
HETATM 3638 O O   . HOH K 6 .   ? 0.738   -28.737 53.529  1.00 66.95  ? 572 HOH B O   1 
HETATM 3639 O O   . HOH K 6 .   ? -0.210  -3.784  38.369  1.00 50.14  ? 573 HOH B O   1 
HETATM 3640 O O   . HOH K 6 .   ? 6.295   -23.834 7.437   1.00 58.86  ? 574 HOH B O   1 
HETATM 3641 O O   . HOH K 6 .   ? -8.696  -14.734 16.556  1.00 55.44  ? 575 HOH B O   1 
HETATM 3642 O O   . HOH K 6 .   ? 2.917   -36.524 38.931  1.00 42.66  ? 576 HOH B O   1 
HETATM 3643 O O   . HOH K 6 .   ? -10.988 -27.953 22.756  1.00 45.38  ? 577 HOH B O   1 
HETATM 3644 O O   . HOH K 6 .   ? 10.198  -19.295 37.944  1.00 62.38  ? 578 HOH B O   1 
HETATM 3645 O O   . HOH K 6 .   ? -9.389  -32.064 29.436  1.00 55.76  ? 579 HOH B O   1 
HETATM 3646 O O   . HOH K 6 .   ? -18.591 -30.031 43.393  1.00 68.72  ? 580 HOH B O   1 
HETATM 3647 O O   . HOH K 6 .   ? -10.982 -34.553 26.858  1.00 61.47  ? 581 HOH B O   1 
HETATM 3648 O O   . HOH K 6 .   ? -11.221 -29.343 25.335  1.00 49.09  ? 582 HOH B O   1 
HETATM 3649 O O   . HOH K 6 .   ? -0.283  -33.929 10.788  1.00 50.31  ? 583 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   . GLY A 8   ? 0.6780 0.6099 0.9515 -0.0523 -0.1757 0.0211  10  GLY A N   
2    C CA  . GLY A 8   ? 0.6830 0.6152 0.9693 -0.0518 -0.1561 0.0211  10  GLY A CA  
3    C C   . GLY A 8   ? 0.6915 0.6269 0.9469 -0.0464 -0.1419 0.0185  10  GLY A C   
4    O O   . GLY A 8   ? 0.7159 0.6453 0.9557 -0.0435 -0.1351 0.0116  10  GLY A O   
5    N N   . ALA A 9   ? 0.6545 0.5995 0.9034 -0.0452 -0.1374 0.0247  11  ALA A N   
6    C CA  . ALA A 9   ? 0.6318 0.5799 0.8466 -0.0399 -0.1303 0.0222  11  ALA A CA  
7    C C   . ALA A 9   ? 0.5943 0.5496 0.8140 -0.0387 -0.1110 0.0255  11  ALA A C   
8    O O   . ALA A 9   ? 0.5872 0.5465 0.8353 -0.0420 -0.1039 0.0309  11  ALA A O   
9    C CB  . ALA A 9   ? 0.6274 0.5805 0.8267 -0.0389 -0.1412 0.0267  11  ALA A CB  
10   N N   . ARG A 10  ? 0.5610 0.5176 0.7532 -0.0338 -0.1025 0.0218  12  ARG A N   
11   C CA  . ARG A 10  ? 0.5217 0.4853 0.7153 -0.0326 -0.0861 0.0243  12  ARG A CA  
12   C C   . ARG A 10  ? 0.4644 0.4376 0.6740 -0.0347 -0.0841 0.0330  12  ARG A C   
13   O O   . ARG A 10  ? 0.4577 0.4339 0.6617 -0.0345 -0.0941 0.0373  12  ARG A O   
14   C CB  . ARG A 10  ? 0.5496 0.5138 0.7117 -0.0270 -0.0804 0.0196  12  ARG A CB  
15   C CG  . ARG A 10  ? 0.5972 0.5671 0.7598 -0.0257 -0.0643 0.0205  12  ARG A CG  
16   C CD  . ARG A 10  ? 0.6656 0.6368 0.8007 -0.0202 -0.0599 0.0167  12  ARG A CD  
17   N NE  . ARG A 10  ? 0.7395 0.7013 0.8606 -0.0176 -0.0637 0.0092  12  ARG A NE  
18   C CZ  . ARG A 10  ? 0.7528 0.7096 0.8774 -0.0175 -0.0578 0.0057  12  ARG A CZ  
19   N NH1 . ARG A 10  ? 0.7096 0.6700 0.8485 -0.0198 -0.0477 0.0087  12  ARG A NH1 
20   N NH2 . ARG A 10  ? 0.7578 0.7057 0.8714 -0.0149 -0.0621 -0.0008 12  ARG A NH2 
21   N N   . ILE A 11  ? 0.4266 0.4041 0.6561 -0.0367 -0.0716 0.0357  13  ILE A N   
22   C CA  . ILE A 11  ? 0.4015 0.3878 0.6477 -0.0383 -0.0669 0.0429  13  ILE A CA  
23   C C   . ILE A 11  ? 0.3910 0.3835 0.6173 -0.0346 -0.0584 0.0429  13  ILE A C   
24   O O   . ILE A 11  ? 0.3947 0.3873 0.6143 -0.0333 -0.0469 0.0386  13  ILE A O   
25   C CB  . ILE A 11  ? 0.3883 0.3754 0.6657 -0.0422 -0.0566 0.0444  13  ILE A CB  
26   C CG1 . ILE A 11  ? 0.3905 0.3710 0.6888 -0.0457 -0.0634 0.0442  13  ILE A CG1 
27   C CG2 . ILE A 11  ? 0.3659 0.3611 0.6640 -0.0440 -0.0532 0.0515  13  ILE A CG2 
28   C CD1 . ILE A 11  ? 0.3814 0.3627 0.7116 -0.0494 -0.0520 0.0460  13  ILE A CD1 
29   N N   . ILE A 12  ? 0.3753 0.3731 0.5932 -0.0331 -0.0643 0.0484  14  ILE A N   
30   C CA  . ILE A 12  ? 0.3773 0.3811 0.5772 -0.0295 -0.0577 0.0494  14  ILE A CA  
31   C C   . ILE A 12  ? 0.3678 0.3801 0.5865 -0.0313 -0.0557 0.0585  14  ILE A C   
32   O O   . ILE A 12  ? 0.3526 0.3664 0.5812 -0.0330 -0.0658 0.0655  14  ILE A O   
33   C CB  . ILE A 12  ? 0.4022 0.4037 0.5700 -0.0252 -0.0658 0.0475  14  ILE A CB  
34   C CG1 . ILE A 12  ? 0.4245 0.4161 0.5774 -0.0237 -0.0688 0.0378  14  ILE A CG1 
35   C CG2 . ILE A 12  ? 0.4103 0.4188 0.5612 -0.0212 -0.0575 0.0495  14  ILE A CG2 
36   C CD1 . ILE A 12  ? 0.4624 0.4506 0.5863 -0.0196 -0.0746 0.0339  14  ILE A CD1 
37   N N   . TYR A 13  ? 0.3736 0.3913 0.5979 -0.0309 -0.0433 0.0585  15  TYR A N   
38   C CA  . TYR A 13  ? 0.3743 0.4001 0.6162 -0.0321 -0.0401 0.0667  15  TYR A CA  
39   C C   . TYR A 13  ? 0.3977 0.4292 0.6211 -0.0284 -0.0349 0.0681  15  TYR A C   
40   O O   . TYR A 13  ? 0.4184 0.4495 0.6302 -0.0265 -0.0265 0.0615  15  TYR A O   
41   C CB  . TYR A 13  ? 0.3661 0.3930 0.6353 -0.0355 -0.0293 0.0648  15  TYR A CB  
42   C CG  . TYR A 13  ? 0.3841 0.4061 0.6756 -0.0392 -0.0316 0.0638  15  TYR A CG  
43   C CD1 . TYR A 13  ? 0.4039 0.4274 0.7185 -0.0417 -0.0401 0.0717  15  TYR A CD1 
44   C CD2 . TYR A 13  ? 0.3989 0.4149 0.6901 -0.0402 -0.0253 0.0558  15  TYR A CD2 
45   C CE1 . TYR A 13  ? 0.4004 0.4200 0.7397 -0.0451 -0.0416 0.0714  15  TYR A CE1 
46   C CE2 . TYR A 13  ? 0.3993 0.4110 0.7133 -0.0436 -0.0260 0.0556  15  TYR A CE2 
47   C CZ  . TYR A 13  ? 0.3969 0.4105 0.7360 -0.0461 -0.0340 0.0632  15  TYR A CZ  
48   O OH  . TYR A 13  ? 0.3756 0.3856 0.7403 -0.0494 -0.0349 0.0637  15  TYR A OH  
49   N N   . ASP A 14  ? 0.3874 0.4244 0.6084 -0.0273 -0.0399 0.0774  16  ASP A N   
50   C CA  . ASP A 14  ? 0.4046 0.4484 0.6155 -0.0243 -0.0331 0.0808  16  ASP A CA  
51   C C   . ASP A 14  ? 0.3791 0.4285 0.6169 -0.0267 -0.0227 0.0825  16  ASP A C   
52   O O   . ASP A 14  ? 0.3575 0.4057 0.6217 -0.0306 -0.0210 0.0820  16  ASP A O   
53   C CB  . ASP A 14  ? 0.4505 0.4983 0.6466 -0.0219 -0.0408 0.0908  16  ASP A CB  
54   C CG  . ASP A 14  ? 0.5002 0.5520 0.7195 -0.0249 -0.0474 0.1026  16  ASP A CG  
55   O OD1 . ASP A 14  ? 0.5085 0.5623 0.7590 -0.0283 -0.0425 0.1040  16  ASP A OD1 
56   O OD2 . ASP A 14  ? 0.5378 0.5905 0.7437 -0.0238 -0.0574 0.1103  16  ASP A OD2 
57   N N   . ARG A 15  ? 0.3787 0.4339 0.6103 -0.0244 -0.0154 0.0838  17  ARG A N   
58   C CA  . ARG A 15  ? 0.3756 0.4360 0.6303 -0.0265 -0.0058 0.0843  17  ARG A CA  
59   C C   . ARG A 15  ? 0.3917 0.4554 0.6772 -0.0298 -0.0075 0.0935  17  ARG A C   
60   O O   . ARG A 15  ? 0.3883 0.4514 0.6988 -0.0331 -0.0016 0.0899  17  ARG A O   
61   C CB  . ARG A 15  ? 0.3609 0.4278 0.6045 -0.0232 -0.0001 0.0869  17  ARG A CB  
62   C CG  . ARG A 15  ? 0.3615 0.4329 0.6274 -0.0254 0.0093  0.0852  17  ARG A CG  
63   C CD  . ARG A 15  ? 0.3796 0.4578 0.6360 -0.0221 0.0142  0.0882  17  ARG A CD  
64   N NE  . ARG A 15  ? 0.4470 0.5298 0.7262 -0.0245 0.0221  0.0868  17  ARG A NE  
65   C CZ  . ARG A 15  ? 0.4803 0.5677 0.7864 -0.0268 0.0241  0.0945  17  ARG A CZ  
66   N NH1 . ARG A 15  ? 0.4636 0.5522 0.7776 -0.0271 0.0184  0.1056  17  ARG A NH1 
67   N NH2 . ARG A 15  ? 0.4912 0.5819 0.8172 -0.0290 0.0310  0.0911  17  ARG A NH2 
68   N N   . ALA A 16  ? 0.4045 0.4715 0.6879 -0.0288 -0.0156 0.1052  18  ALA A N   
69   C CA  . ALA A 16  ? 0.4147 0.4855 0.7283 -0.0315 -0.0185 0.1159  18  ALA A CA  
70   C C   . ALA A 16  ? 0.4298 0.4956 0.7673 -0.0354 -0.0215 0.1131  18  ALA A C   
71   O O   . ALA A 16  ? 0.4436 0.5115 0.8140 -0.0382 -0.0169 0.1158  18  ALA A O   
72   C CB  . ALA A 16  ? 0.4240 0.4982 0.7253 -0.0296 -0.0284 0.1291  18  ALA A CB  
73   N N   . PHE A 17  ? 0.4326 0.4919 0.7564 -0.0354 -0.0286 0.1078  19  PHE A N   
74   C CA  . PHE A 17  ? 0.4366 0.4914 0.7841 -0.0390 -0.0311 0.1055  19  PHE A CA  
75   C C   . PHE A 17  ? 0.4228 0.4752 0.7871 -0.0412 -0.0177 0.0952  19  PHE A C   
76   O O   . PHE A 17  ? 0.4116 0.4640 0.8080 -0.0443 -0.0142 0.0964  19  PHE A O   
77   C CB  . PHE A 17  ? 0.4623 0.5105 0.7905 -0.0385 -0.0417 0.1017  19  PHE A CB  
78   C CG  . PHE A 17  ? 0.4921 0.5367 0.8482 -0.0423 -0.0462 0.1022  19  PHE A CG  
79   C CD1 . PHE A 17  ? 0.4979 0.5374 0.8653 -0.0443 -0.0377 0.0925  19  PHE A CD1 
80   C CD2 . PHE A 17  ? 0.5131 0.5598 0.8865 -0.0439 -0.0582 0.1132  19  PHE A CD2 
81   C CE1 . PHE A 17  ? 0.4970 0.5338 0.8937 -0.0476 -0.0399 0.0937  19  PHE A CE1 
82   C CE2 . PHE A 17  ? 0.5057 0.5498 0.9092 -0.0474 -0.0619 0.1141  19  PHE A CE2 
83   C CZ  . PHE A 17  ? 0.4906 0.5298 0.9060 -0.0491 -0.0522 0.1042  19  PHE A CZ  
84   N N   . LEU A 18  ? 0.4175 0.4679 0.7602 -0.0395 -0.0103 0.0852  20  LEU A N   
85   C CA  . LEU A 18  ? 0.3994 0.4471 0.7527 -0.0416 0.0018  0.0751  20  LEU A CA  
86   C C   . LEU A 18  ? 0.3925 0.4452 0.7718 -0.0434 0.0104  0.0769  20  LEU A C   
87   O O   . LEU A 18  ? 0.3854 0.4358 0.7868 -0.0463 0.0183  0.0716  20  LEU A O   
88   C CB  . LEU A 18  ? 0.3926 0.4378 0.7160 -0.0393 0.0063  0.0655  20  LEU A CB  
89   C CG  . LEU A 18  ? 0.4042 0.4430 0.7042 -0.0377 -0.0002 0.0615  20  LEU A CG  
90   C CD1 . LEU A 18  ? 0.4183 0.4557 0.6907 -0.0349 0.0038  0.0539  20  LEU A CD1 
91   C CD2 . LEU A 18  ? 0.4020 0.4348 0.7168 -0.0408 0.0008  0.0578  20  LEU A CD2 
92   N N   . MET A 19  ? 0.4069 0.4661 0.7840 -0.0416 0.0095  0.0838  21  MET A N   
93   C CA  . MET A 19  ? 0.4216 0.4854 0.8263 -0.0434 0.0167  0.0865  21  MET A CA  
94   C C   . MET A 19  ? 0.4547 0.5192 0.8958 -0.0461 0.0147  0.0943  21  MET A C   
95   O O   . MET A 19  ? 0.4441 0.5081 0.9127 -0.0486 0.0232  0.0905  21  MET A O   
96   C CB  . MET A 19  ? 0.4008 0.4716 0.7968 -0.0408 0.0155  0.0946  21  MET A CB  
97   C CG  . MET A 19  ? 0.4231 0.4947 0.7916 -0.0383 0.0192  0.0876  21  MET A CG  
98   S SD  . MET A 19  ? 0.4728 0.5416 0.8465 -0.0407 0.0308  0.0723  21  MET A SD  
99   C CE  . MET A 19  ? 0.5294 0.6033 0.8788 -0.0372 0.0321  0.0716  21  MET A CE  
100  N N   . ALA A 20  ? 0.4862 0.5515 0.9278 -0.0455 0.0031  0.1049  22  ALA A N   
101  C CA  . ALA A 20  ? 0.4915 0.5574 0.9682 -0.0479 -0.0009 0.1132  22  ALA A CA  
102  C C   . ALA A 20  ? 0.5116 0.5714 1.0087 -0.0508 0.0055  0.1039  22  ALA A C   
103  O O   . ALA A 20  ? 0.5067 0.5671 1.0407 -0.0531 0.0096  0.1066  22  ALA A O   
104  C CB  . ALA A 20  ? 0.4901 0.5569 0.9561 -0.0468 -0.0165 0.1244  22  ALA A CB  
105  N N   . CYS A 21  ? 0.5277 0.5817 1.0020 -0.0506 0.0072  0.0933  23  CYS A N   
106  C CA  . CYS A 21  ? 0.5249 0.5729 1.0144 -0.0531 0.0148  0.0845  23  CYS A CA  
107  C C   . CYS A 21  ? 0.5198 0.5661 1.0188 -0.0546 0.0311  0.0731  23  CYS A C   
108  O O   . CYS A 21  ? 0.5305 0.5713 1.0332 -0.0563 0.0395  0.0640  23  CYS A O   
109  C CB  . CYS A 21  ? 0.5464 0.5888 1.0082 -0.0522 0.0105  0.0786  23  CYS A CB  
110  S SG  . CYS A 21  ? 0.6082 0.6504 1.0599 -0.0512 -0.0088 0.0886  23  CYS A SG  
111  N N   . ARG A 22  ? 0.5110 0.5615 1.0131 -0.0542 0.0356  0.0733  24  ARG A N   
112  C CA  . ARG A 22  ? 0.5259 0.5746 1.0311 -0.0556 0.0490  0.0615  24  ARG A CA  
113  C C   . ARG A 22  ? 0.5802 0.6296 1.1273 -0.0580 0.0566  0.0622  24  ARG A C   
114  O O   . ARG A 22  ? 0.5719 0.6263 1.1416 -0.0578 0.0509  0.0742  24  ARG A O   
115  C CB  . ARG A 22  ? 0.4789 0.5319 0.9631 -0.0538 0.0487  0.0606  24  ARG A CB  
116  C CG  . ARG A 22  ? 0.4395 0.4907 0.9240 -0.0554 0.0601  0.0479  24  ARG A CG  
117  C CD  . ARG A 22  ? 0.4593 0.5157 0.9304 -0.0539 0.0587  0.0489  24  ARG A CD  
118  N NE  . ARG A 22  ? 0.4421 0.4963 0.9105 -0.0557 0.0679  0.0356  24  ARG A NE  
119  C CZ  . ARG A 22  ? 0.4335 0.4906 0.8830 -0.0547 0.0675  0.0318  24  ARG A CZ  
120  N NH1 . ARG A 22  ? 0.3993 0.4617 0.8313 -0.0515 0.0599  0.0405  24  ARG A NH1 
121  N NH2 . ARG A 22  ? 0.4762 0.5309 0.9245 -0.0569 0.0746  0.0193  24  ARG A NH2 
122  N N   . GLY A 23  ? 0.6178 0.6621 1.1738 -0.0602 0.0697  0.0495  25  GLY A N   
123  C CA  . GLY A 23  ? 0.6464 0.6902 1.2392 -0.0624 0.0798  0.0461  25  GLY A CA  
124  C C   . GLY A 23  ? 0.6727 0.7133 1.2980 -0.0639 0.0843  0.0474  25  GLY A C   
125  O O   . GLY A 23  ? 0.6680 0.7106 1.3320 -0.0647 0.0854  0.0538  25  GLY A O   
126  N N   . GLY A 24  ? 0.6945 0.7300 1.3058 -0.0643 0.0873  0.0417  26  GLY A N   
127  C CA  . GLY A 24  ? 0.7072 0.7395 1.3475 -0.0656 0.0921  0.0427  26  GLY A CA  
128  C C   . GLY A 24  ? 0.7209 0.7579 1.3864 -0.0652 0.0789  0.0589  26  GLY A C   
129  O O   . GLY A 24  ? 0.7304 0.7714 1.3771 -0.0635 0.0643  0.0685  26  GLY A O   
130  N N   . GLY A 25  ? 0.7215 0.7576 1.4291 -0.0666 0.0843  0.0616  27  GLY A N   
131  C CA  . GLY A 25  ? 0.7206 0.7616 1.4620 -0.0666 0.0726  0.0774  27  GLY A CA  
132  C C   . GLY A 25  ? 0.7270 0.7664 1.4802 -0.0673 0.0672  0.0821  27  GLY A C   
133  O O   . GLY A 25  ? 0.7262 0.7662 1.5228 -0.0685 0.0695  0.0874  27  GLY A O   
134  N N   . GLY A 26  ? 0.7362 0.7735 1.4532 -0.0667 0.0601  0.0803  28  GLY A N   
135  C CA  . GLY A 26  ? 0.7347 0.7703 1.4586 -0.0675 0.0526  0.0848  28  GLY A CA  
136  C C   . GLY A 26  ? 0.7218 0.7533 1.4782 -0.0693 0.0674  0.0792  28  GLY A C   
137  O O   . GLY A 26  ? 0.7353 0.7618 1.4795 -0.0697 0.0840  0.0664  28  GLY A O   
138  N N   . GLU A 27  ? 0.6899 0.7238 1.4884 -0.0705 0.0616  0.0893  29  GLU A N   
139  C CA  . GLU A 27  ? 0.6567 0.6872 1.4902 -0.0721 0.0747  0.0860  29  GLU A CA  
140  C C   . GLU A 27  ? 0.6285 0.6537 1.4364 -0.0726 0.0778  0.0795  29  GLU A C   
141  O O   . GLU A 27  ? 0.6384 0.6591 1.4564 -0.0734 0.0958  0.0711  29  GLU A O   
142  C CB  . GLU A 27  ? 0.6838 0.7190 1.5673 -0.0731 0.0635  0.1004  29  GLU A CB  
143  C CG  . GLU A 27  ? 0.7431 0.7826 1.6664 -0.0729 0.0659  0.1067  29  GLU A CG  
144  C CD  . GLU A 27  ? 0.8349 0.8782 1.8151 -0.0741 0.0592  0.1196  29  GLU A CD  
145  O OE1 . GLU A 27  ? 0.8465 0.8872 1.8565 -0.0752 0.0706  0.1163  29  GLU A OE1 
146  O OE2 . GLU A 27  ? 0.8599 0.9092 1.8561 -0.0738 0.0428  0.1337  29  GLU A OE2 
147  N N   . ASN A 28  ? 0.5899 0.6153 1.3644 -0.0720 0.0608  0.0833  30  ASN A N   
148  C CA  . ASN A 28  ? 0.5419 0.5624 1.2947 -0.0725 0.0597  0.0796  30  ASN A CA  
149  C C   . ASN A 28  ? 0.5089 0.5284 1.3025 -0.0746 0.0612  0.0843  30  ASN A C   
150  O O   . ASN A 28  ? 0.5080 0.5227 1.3026 -0.0755 0.0749  0.0780  30  ASN A O   
151  C CB  . ASN A 28  ? 0.5173 0.5323 1.2336 -0.0718 0.0758  0.0661  30  ASN A CB  
152  C CG  . ASN A 28  ? 0.4944 0.5048 1.1829 -0.0718 0.0712  0.0641  30  ASN A CG  
153  O OD1 . ASN A 28  ? 0.4624 0.4736 1.1401 -0.0716 0.0526  0.0704  30  ASN A OD1 
154  N ND2 . ASN A 28  ? 0.5066 0.5116 1.1825 -0.0722 0.0878  0.0553  30  ASN A ND2 
155  N N   . LEU A 29  ? 0.4794 0.5038 1.3071 -0.0755 0.0462  0.0965  31  LEU A N   
156  C CA  . LEU A 29  ? 0.4490 0.4735 1.3199 -0.0776 0.0443  0.1028  31  LEU A CA  
157  C C   . LEU A 29  ? 0.4370 0.4573 1.2873 -0.0786 0.0358  0.1017  31  LEU A C   
158  O O   . LEU A 29  ? 0.4553 0.4747 1.2658 -0.0776 0.0208  0.1016  31  LEU A O   
159  C CB  . LEU A 29  ? 0.4439 0.4749 1.3537 -0.0785 0.0264  0.1172  31  LEU A CB  
160  C CG  . LEU A 29  ? 0.4691 0.5049 1.4033 -0.0776 0.0310  0.1211  31  LEU A CG  
161  C CD1 . LEU A 29  ? 0.4745 0.5166 1.4485 -0.0787 0.0115  0.1371  31  LEU A CD1 
162  C CD2 . LEU A 29  ? 0.4672 0.5006 1.4305 -0.0776 0.0576  0.1127  31  LEU A CD2 
163  N N   . TYR A 30  ? 0.4023 0.4199 1.2816 -0.0804 0.0465  0.1010  32  TYR A N   
164  C CA  . TYR A 30  ? 0.3884 0.4014 1.2578 -0.0817 0.0424  0.0999  32  TYR A CA  
165  C C   . TYR A 30  ? 0.3935 0.4007 1.2078 -0.0801 0.0486  0.0898  32  TYR A C   
166  O O   . TYR A 30  ? 0.3860 0.3896 1.1865 -0.0808 0.0405  0.0899  32  TYR A O   
167  C CB  . TYR A 30  ? 0.3800 0.3952 1.2594 -0.0832 0.0144  0.1100  32  TYR A CB  
168  C CG  . TYR A 30  ? 0.3575 0.3792 1.2892 -0.0846 0.0054  0.1214  32  TYR A CG  
169  C CD1 . TYR A 30  ? 0.3466 0.3691 1.3312 -0.0870 0.0106  0.1264  32  TYR A CD1 
170  C CD2 . TYR A 30  ? 0.3595 0.3867 1.2900 -0.0835 -0.0068 0.1277  32  TYR A CD2 
171  C CE1 . TYR A 30  ? 0.3304 0.3592 1.3659 -0.0881 0.0023  0.1374  32  TYR A CE1 
172  C CE2 . TYR A 30  ? 0.3549 0.3881 1.3346 -0.0847 -0.0150 0.1392  32  TYR A CE2 
173  C CZ  . TYR A 30  ? 0.3427 0.3767 1.3756 -0.0870 -0.0106 0.1438  32  TYR A CZ  
174  O OH  . TYR A 30  ? 0.3467 0.3871 1.4316 -0.0881 -0.0189 0.1558  32  TYR A OH  
175  N N   . PHE A 31  ? 0.4075 0.4139 1.1923 -0.0781 0.0625  0.0812  33  PHE A N   
176  C CA  . PHE A 31  ? 0.4381 0.4403 1.1688 -0.0763 0.0647  0.0729  33  PHE A CA  
177  C C   . PHE A 31  ? 0.4567 0.4594 1.1581 -0.0753 0.0409  0.0765  33  PHE A C   
178  O O   . PHE A 31  ? 0.4667 0.4650 1.1345 -0.0745 0.0382  0.0723  33  PHE A O   
179  C CB  . PHE A 31  ? 0.4444 0.4403 1.1660 -0.0771 0.0806  0.0670  33  PHE A CB  
180  C CG  . PHE A 31  ? 0.4465 0.4413 1.1894 -0.0777 0.1058  0.0618  33  PHE A CG  
181  C CD1 . PHE A 31  ? 0.4545 0.4487 1.1740 -0.0763 0.1196  0.0527  33  PHE A CD1 
182  C CD2 . PHE A 31  ? 0.4354 0.4300 1.2232 -0.0796 0.1155  0.0658  33  PHE A CD2 
183  C CE1 . PHE A 31  ? 0.4503 0.4427 1.1880 -0.0769 0.1427  0.0467  33  PHE A CE1 
184  C CE2 . PHE A 31  ? 0.4333 0.4267 1.2407 -0.0798 0.1398  0.0605  33  PHE A CE2 
185  C CZ  . PHE A 31  ? 0.4402 0.4322 1.2208 -0.0785 0.1533  0.0504  33  PHE A CZ  
186  N N   . GLN A 32  ? 0.4528 0.4609 1.1677 -0.0752 0.0239  0.0847  34  GLN A N   
187  C CA  . GLN A 32  ? 0.4531 0.4620 1.1442 -0.0745 0.0003  0.0891  34  GLN A CA  
188  C C   . GLN A 32  ? 0.4331 0.4473 1.1091 -0.0725 -0.0087 0.0928  34  GLN A C   
189  O O   . GLN A 32  ? 0.4421 0.4573 1.1007 -0.0719 -0.0280 0.0974  34  GLN A O   
190  C CB  . GLN A 32  ? 0.4532 0.4626 1.1774 -0.0771 -0.0165 0.0979  34  GLN A CB  
191  C CG  . GLN A 32  ? 0.4715 0.4751 1.2035 -0.0789 -0.0124 0.0949  34  GLN A CG  
192  C CD  . GLN A 32  ? 0.5517 0.5554 1.3106 -0.0815 -0.0325 0.1026  34  GLN A CD  
193  O OE1 . GLN A 32  ? 0.5905 0.5940 1.3285 -0.0812 -0.0539 0.1048  34  GLN A OE1 
194  N NE2 . GLN A 32  ? 0.5535 0.5577 1.3596 -0.0842 -0.0263 0.1068  34  GLN A NE2 
195  N N   . GLY A 33  ? 0.4141 0.4312 1.0959 -0.0717 0.0050  0.0906  35  GLY A N   
196  C CA  . GLY A 33  ? 0.4081 0.4307 1.0800 -0.0699 -0.0015 0.0949  35  GLY A CA  
197  C C   . GLY A 33  ? 0.4179 0.4396 1.0456 -0.0673 0.0051  0.0868  35  GLY A C   
198  O O   . GLY A 33  ? 0.4240 0.4501 1.0405 -0.0657 0.0001  0.0903  35  GLY A O   
199  N N   . LYS A 34  ? 0.4019 0.4182 1.0063 -0.0670 0.0162  0.0768  36  LYS A N   
200  C CA  . LYS A 34  ? 0.4036 0.4186 0.9659 -0.0646 0.0211  0.0690  36  LYS A CA  
201  C C   . LYS A 34  ? 0.4120 0.4252 0.9395 -0.0627 0.0055  0.0699  36  LYS A C   
202  O O   . LYS A 34  ? 0.4151 0.4253 0.9480 -0.0637 -0.0050 0.0728  36  LYS A O   
203  C CB  . LYS A 34  ? 0.4093 0.4191 0.9623 -0.0651 0.0396  0.0585  36  LYS A CB  
204  C CG  . LYS A 34  ? 0.3898 0.4007 0.9615 -0.0661 0.0572  0.0537  36  LYS A CG  
205  C CD  . LYS A 34  ? 0.4278 0.4331 0.9883 -0.0668 0.0749  0.0437  36  LYS A CD  
206  C CE  . LYS A 34  ? 0.4457 0.4513 1.0161 -0.0675 0.0918  0.0364  36  LYS A CE  
207  N NZ  . LYS A 34  ? 0.4587 0.4585 1.0191 -0.0685 0.1096  0.0270  36  LYS A NZ  
208  N N   . HIS A 35  ? 0.3955 0.4103 0.8888 -0.0600 0.0043  0.0670  37  HIS A N   
209  C CA  . HIS A 35  ? 0.3965 0.4102 0.8561 -0.0575 -0.0095 0.0677  37  HIS A CA  
210  C C   . HIS A 35  ? 0.3806 0.3885 0.8108 -0.0562 -0.0040 0.0589  37  HIS A C   
211  O O   . HIS A 35  ? 0.3863 0.3948 0.7976 -0.0547 0.0059  0.0531  37  HIS A O   
212  C CB  . HIS A 35  ? 0.4214 0.4410 0.8645 -0.0550 -0.0140 0.0714  37  HIS A CB  
213  C CG  . HIS A 35  ? 0.4509 0.4759 0.9194 -0.0561 -0.0235 0.0824  37  HIS A CG  
214  N ND1 . HIS A 35  ? 0.4634 0.4926 0.9631 -0.0575 -0.0151 0.0858  37  HIS A ND1 
215  C CD2 . HIS A 35  ? 0.4613 0.4876 0.9281 -0.0559 -0.0409 0.0906  37  HIS A CD2 
216  C CE1 . HIS A 35  ? 0.4649 0.4984 0.9821 -0.0581 -0.0276 0.0970  37  HIS A CE1 
217  N NE2 . HIS A 35  ? 0.4606 0.4926 0.9577 -0.0572 -0.0436 0.1004  37  HIS A NE2 
218  N N   . PRO A 36  ? 0.3653 0.3676 0.7926 -0.0568 -0.0108 0.0580  38  PRO A N   
219  C CA  . PRO A 36  ? 0.3555 0.3518 0.7593 -0.0557 -0.0046 0.0506  38  PRO A CA  
220  C C   . PRO A 36  ? 0.3467 0.3430 0.7119 -0.0519 -0.0085 0.0470  38  PRO A C   
221  O O   . PRO A 36  ? 0.3308 0.3292 0.6832 -0.0500 -0.0208 0.0501  38  PRO A O   
222  C CB  . PRO A 36  ? 0.3691 0.3597 0.7827 -0.0573 -0.0139 0.0521  38  PRO A CB  
223  C CG  . PRO A 36  ? 0.3673 0.3608 0.7956 -0.0582 -0.0298 0.0592  38  PRO A CG  
224  C CD  . PRO A 36  ? 0.3557 0.3566 0.8018 -0.0586 -0.0254 0.0640  38  PRO A CD  
225  N N   . LEU A 37  ? 0.3410 0.3352 0.6879 -0.0508 0.0023  0.0407  39  LEU A N   
226  C CA  . LEU A 37  ? 0.3350 0.3284 0.6474 -0.0471 -0.0006 0.0370  39  LEU A CA  
227  C C   . LEU A 37  ? 0.3332 0.3192 0.6330 -0.0461 -0.0078 0.0348  39  LEU A C   
228  O O   . LEU A 37  ? 0.3305 0.3117 0.6455 -0.0485 -0.0061 0.0349  39  LEU A O   
229  C CB  . LEU A 37  ? 0.3168 0.3116 0.6170 -0.0465 0.0130  0.0317  39  LEU A CB  
230  C CG  . LEU A 37  ? 0.3038 0.3054 0.6157 -0.0474 0.0201  0.0323  39  LEU A CG  
231  C CD1 . LEU A 37  ? 0.3143 0.3163 0.6130 -0.0474 0.0324  0.0257  39  LEU A CD1 
232  C CD2 . LEU A 37  ? 0.3046 0.3122 0.6104 -0.0451 0.0113  0.0370  39  LEU A CD2 
233  N N   . GLN A 38  ? 0.3421 0.3271 0.6155 -0.0425 -0.0154 0.0328  40  GLN A N   
234  C CA  . GLN A 38  ? 0.3340 0.3115 0.5931 -0.0410 -0.0215 0.0294  40  GLN A CA  
235  C C   . GLN A 38  ? 0.3164 0.2894 0.5724 -0.0415 -0.0107 0.0261  40  GLN A C   
236  O O   . GLN A 38  ? 0.3093 0.2755 0.5711 -0.0426 -0.0129 0.0255  40  GLN A O   
237  C CB  . GLN A 38  ? 0.3444 0.3224 0.5741 -0.0363 -0.0281 0.0270  40  GLN A CB  
238  C CG  . GLN A 38  ? 0.3547 0.3244 0.5687 -0.0341 -0.0341 0.0224  40  GLN A CG  
239  C CD  . GLN A 38  ? 0.4281 0.3923 0.6520 -0.0358 -0.0473 0.0229  40  GLN A CD  
240  O OE1 . GLN A 38  ? 0.4405 0.4078 0.6799 -0.0382 -0.0541 0.0274  40  GLN A OE1 
241  N NE2 . GLN A 38  ? 0.4121 0.3680 0.6280 -0.0347 -0.0521 0.0184  40  GLN A NE2 
242  N N   . ASN A 39  ? 0.3086 0.2853 0.5554 -0.0408 0.0003  0.0242  41  ASN A N   
243  C CA  . ASN A 39  ? 0.3050 0.2783 0.5455 -0.0413 0.0109  0.0216  41  ASN A CA  
244  C C   . ASN A 39  ? 0.2889 0.2655 0.5429 -0.0444 0.0238  0.0215  41  ASN A C   
245  O O   . ASN A 39  ? 0.3035 0.2860 0.5668 -0.0451 0.0249  0.0223  41  ASN A O   
246  C CB  . ASN A 39  ? 0.3085 0.2829 0.5215 -0.0373 0.0112  0.0185  41  ASN A CB  
247  C CG  . ASN A 39  ? 0.3342 0.3032 0.5344 -0.0343 0.0015  0.0174  41  ASN A CG  
248  O OD1 . ASN A 39  ? 0.3695 0.3317 0.5701 -0.0347 0.0019  0.0170  41  ASN A OD1 
249  N ND2 . ASN A 39  ? 0.3334 0.3048 0.5229 -0.0313 -0.0070 0.0169  41  ASN A ND2 
250  N N   . ARG A 40  ? 0.2713 0.2438 0.5264 -0.0461 0.0336  0.0205  42  ARG A N   
251  C CA  . ARG A 40  ? 0.2905 0.2650 0.5494 -0.0484 0.0475  0.0183  42  ARG A CA  
252  C C   . ARG A 40  ? 0.2959 0.2726 0.5277 -0.0462 0.0503  0.0144  42  ARG A C   
253  O O   . ARG A 40  ? 0.3000 0.2742 0.5125 -0.0435 0.0456  0.0143  42  ARG A O   
254  C CB  . ARG A 40  ? 0.3367 0.3053 0.6062 -0.0511 0.0568  0.0196  42  ARG A CB  
255  C CG  . ARG A 40  ? 0.4243 0.3934 0.6968 -0.0537 0.0730  0.0167  42  ARG A CG  
256  C CD  . ARG A 40  ? 0.5060 0.4713 0.8047 -0.0568 0.0810  0.0198  42  ARG A CD  
257  N NE  . ARG A 40  ? 0.6200 0.5828 0.9142 -0.0588 0.0977  0.0175  42  ARG A NE  
258  C CZ  . ARG A 40  ? 0.6697 0.6342 0.9758 -0.0610 0.1105  0.0140  42  ARG A CZ  
259  N NH1 . ARG A 40  ? 0.6481 0.6174 0.9751 -0.0616 0.1084  0.0130  42  ARG A NH1 
260  N NH2 . ARG A 40  ? 0.6914 0.6526 0.9882 -0.0626 0.1257  0.0115  42  ARG A NH2 
261  N N   . TRP A 41  ? 0.2883 0.2698 0.5206 -0.0474 0.0573  0.0112  43  TRP A N   
262  C CA  . TRP A 41  ? 0.2888 0.2738 0.4993 -0.0457 0.0584  0.0074  43  TRP A CA  
263  C C   . TRP A 41  ? 0.2916 0.2756 0.4982 -0.0484 0.0707  0.0030  43  TRP A C   
264  O O   . TRP A 41  ? 0.2856 0.2690 0.5101 -0.0514 0.0790  0.0018  43  TRP A O   
265  C CB  . TRP A 41  ? 0.2652 0.2575 0.4785 -0.0442 0.0532  0.0072  43  TRP A CB  
266  C CG  . TRP A 41  ? 0.2660 0.2595 0.4783 -0.0413 0.0414  0.0113  43  TRP A CG  
267  C CD1 . TRP A 41  ? 0.2665 0.2598 0.4962 -0.0419 0.0355  0.0154  43  TRP A CD1 
268  C CD2 . TRP A 41  ? 0.2649 0.2591 0.4567 -0.0371 0.0340  0.0115  43  TRP A CD2 
269  N NE1 . TRP A 41  ? 0.2755 0.2690 0.4939 -0.0385 0.0247  0.0175  43  TRP A NE1 
270  C CE2 . TRP A 41  ? 0.2765 0.2705 0.4721 -0.0353 0.0245  0.0149  43  TRP A CE2 
271  C CE3 . TRP A 41  ? 0.2704 0.2656 0.4417 -0.0346 0.0344  0.0091  43  TRP A CE3 
272  C CZ2 . TRP A 41  ? 0.2982 0.2924 0.4767 -0.0310 0.0169  0.0151  43  TRP A CZ2 
273  C CZ3 . TRP A 41  ? 0.2925 0.2885 0.4503 -0.0303 0.0269  0.0101  43  TRP A CZ3 
274  C CH2 . TRP A 41  ? 0.3056 0.3007 0.4663 -0.0284 0.0189  0.0126  43  TRP A CH2 
275  N N   . ALA A 42  ? 0.2985 0.2824 0.4814 -0.0474 0.0718  0.0003  44  ALA A N   
276  C CA  . ALA A 42  ? 0.2895 0.2722 0.4635 -0.0501 0.0823  -0.0047 44  ALA A CA  
277  C C   . ALA A 42  ? 0.3008 0.2890 0.4612 -0.0493 0.0795  -0.0092 44  ALA A C   
278  O O   . ALA A 42  ? 0.3039 0.2947 0.4508 -0.0462 0.0709  -0.0076 44  ALA A O   
279  C CB  . ALA A 42  ? 0.2989 0.2756 0.4567 -0.0502 0.0859  -0.0025 44  ALA A CB  
280  N N   . LEU A 43  ? 0.3146 0.3042 0.4804 -0.0523 0.0873  -0.0154 45  LEU A N   
281  C CA  . LEU A 43  ? 0.3162 0.3104 0.4730 -0.0527 0.0861  -0.0211 45  LEU A CA  
282  C C   . LEU A 43  ? 0.3252 0.3162 0.4586 -0.0544 0.0910  -0.0257 45  LEU A C   
283  O O   . LEU A 43  ? 0.3247 0.3106 0.4571 -0.0572 0.1016  -0.0286 45  LEU A O   
284  C CB  . LEU A 43  ? 0.3070 0.3041 0.4858 -0.0551 0.0914  -0.0258 45  LEU A CB  
285  C CG  . LEU A 43  ? 0.3303 0.3316 0.5035 -0.0564 0.0909  -0.0330 45  LEU A CG  
286  C CD1 . LEU A 43  ? 0.3112 0.3189 0.4778 -0.0531 0.0794  -0.0293 45  LEU A CD1 
287  C CD2 . LEU A 43  ? 0.3303 0.3327 0.5281 -0.0591 0.0979  -0.0381 45  LEU A CD2 
288  N N   . TRP A 44  ? 0.3363 0.3302 0.4510 -0.0528 0.0833  -0.0259 46  TRP A N   
289  C CA  . TRP A 44  ? 0.3588 0.3507 0.4482 -0.0540 0.0841  -0.0290 46  TRP A CA  
290  C C   . TRP A 44  ? 0.3705 0.3674 0.4552 -0.0554 0.0808  -0.0361 46  TRP A C   
291  O O   . TRP A 44  ? 0.3481 0.3512 0.4452 -0.0539 0.0745  -0.0358 46  TRP A O   
292  C CB  . TRP A 44  ? 0.3587 0.3499 0.4317 -0.0506 0.0759  -0.0218 46  TRP A CB  
293  C CG  . TRP A 44  ? 0.3674 0.3538 0.4460 -0.0489 0.0768  -0.0146 46  TRP A CG  
294  C CD1 . TRP A 44  ? 0.3688 0.3560 0.4637 -0.0463 0.0720  -0.0102 46  TRP A CD1 
295  C CD2 . TRP A 44  ? 0.3814 0.3609 0.4492 -0.0498 0.0826  -0.0109 46  TRP A CD2 
296  N NE1 . TRP A 44  ? 0.3785 0.3595 0.4752 -0.0459 0.0740  -0.0048 46  TRP A NE1 
297  C CE2 . TRP A 44  ? 0.3840 0.3605 0.4653 -0.0479 0.0808  -0.0046 46  TRP A CE2 
298  C CE3 . TRP A 44  ? 0.4081 0.3837 0.4556 -0.0522 0.0889  -0.0120 46  TRP A CE3 
299  C CZ2 . TRP A 44  ? 0.3875 0.3572 0.4655 -0.0483 0.0854  0.0010  46  TRP A CZ2 
300  C CZ3 . TRP A 44  ? 0.4242 0.3934 0.4667 -0.0524 0.0943  -0.0057 46  TRP A CZ3 
301  C CH2 . TRP A 44  ? 0.4011 0.3676 0.4601 -0.0504 0.0925  0.0009  46  TRP A CH2 
302  N N   . PHE A 45  ? 0.4254 0.4195 0.4917 -0.0584 0.0850  -0.0425 47  PHE A N   
303  C CA  . PHE A 45  ? 0.4820 0.4796 0.5396 -0.0605 0.0809  -0.0504 47  PHE A CA  
304  C C   . PHE A 45  ? 0.5197 0.5159 0.5481 -0.0604 0.0754  -0.0486 47  PHE A C   
305  O O   . PHE A 45  ? 0.5161 0.5062 0.5287 -0.0609 0.0810  -0.0457 47  PHE A O   
306  C CB  . PHE A 45  ? 0.5102 0.5042 0.5720 -0.0650 0.0919  -0.0614 47  PHE A CB  
307  C CG  . PHE A 45  ? 0.5561 0.5525 0.6100 -0.0678 0.0879  -0.0713 47  PHE A CG  
308  C CD1 . PHE A 45  ? 0.5799 0.5836 0.6509 -0.0671 0.0799  -0.0724 47  PHE A CD1 
309  C CD2 . PHE A 45  ? 0.5946 0.5860 0.6241 -0.0713 0.0922  -0.0797 47  PHE A CD2 
310  C CE1 . PHE A 45  ? 0.5911 0.5970 0.6574 -0.0701 0.0753  -0.0817 47  PHE A CE1 
311  C CE2 . PHE A 45  ? 0.6183 0.6115 0.6404 -0.0744 0.0871  -0.0899 47  PHE A CE2 
312  C CZ  . PHE A 45  ? 0.6079 0.6085 0.6499 -0.0738 0.0783  -0.0908 47  PHE A CZ  
313  N N   . PHE A 46  ? 0.5628 0.5647 0.5853 -0.0596 0.0646  -0.0492 48  PHE A N   
314  C CA  . PHE A 46  ? 0.6465 0.6480 0.6429 -0.0596 0.0575  -0.0471 48  PHE A CA  
315  C C   . PHE A 46  ? 0.7084 0.7133 0.6988 -0.0629 0.0522  -0.0565 48  PHE A C   
316  O O   . PHE A 46  ? 0.6967 0.7088 0.7017 -0.0617 0.0442  -0.0571 48  PHE A O   
317  C CB  . PHE A 46  ? 0.6646 0.6699 0.6625 -0.0546 0.0475  -0.0366 48  PHE A CB  
318  C CG  . PHE A 46  ? 0.7085 0.7141 0.6839 -0.0537 0.0387  -0.0320 48  PHE A CG  
319  C CD1 . PHE A 46  ? 0.7339 0.7465 0.7088 -0.0531 0.0272  -0.0327 48  PHE A CD1 
320  C CD2 . PHE A 46  ? 0.7360 0.7354 0.6936 -0.0534 0.0416  -0.0256 48  PHE A CD2 
321  C CE1 . PHE A 46  ? 0.7556 0.7689 0.7123 -0.0521 0.0180  -0.0272 48  PHE A CE1 
322  C CE2 . PHE A 46  ? 0.7583 0.7581 0.6965 -0.0524 0.0328  -0.0198 48  PHE A CE2 
323  C CZ  . PHE A 46  ? 0.7601 0.7669 0.6980 -0.0517 0.0207  -0.0206 48  PHE A CZ  
324  N N   . LYS A 47  ? 0.7694 0.7690 0.7386 -0.0671 0.0571  -0.0644 49  LYS A N   
325  C CA  . LYS A 47  ? 0.8321 0.8332 0.7938 -0.0712 0.0526  -0.0758 49  LYS A CA  
326  C C   . LYS A 47  ? 0.8839 0.8886 0.8249 -0.0709 0.0382  -0.0724 49  LYS A C   
327  O O   . LYS A 47  ? 0.8820 0.8864 0.8115 -0.0679 0.0340  -0.0615 49  LYS A O   
328  C CB  . LYS A 47  ? 0.8875 0.8804 0.8341 -0.0758 0.0652  -0.0868 49  LYS A CB  
329  C CG  . LYS A 47  ? 0.9776 0.9707 0.9257 -0.0805 0.0639  -0.1023 49  LYS A CG  
330  C CD  . LYS A 47  ? 1.0558 1.0401 0.9958 -0.0845 0.0797  -0.1145 49  LYS A CD  
331  C CE  . LYS A 47  ? 1.1267 1.1108 1.0814 -0.0883 0.0811  -0.1300 49  LYS A CE  
332  N NZ  . LYS A 47  ? 1.1781 1.1583 1.1030 -0.0930 0.0768  -0.1430 49  LYS A NZ  
333  N N   . ASN A 48  ? 0.9282 0.9362 0.8664 -0.0742 0.0300  -0.0814 50  ASN A N   
334  C CA  . ASN A 48  ? 0.9850 0.9971 0.9067 -0.0743 0.0147  -0.0781 50  ASN A CA  
335  C C   . ASN A 48  ? 1.0251 1.0339 0.9225 -0.0800 0.0109  -0.0902 50  ASN A C   
336  O O   . ASN A 48  ? 1.0238 1.0375 0.9300 -0.0825 0.0013  -0.0978 50  ASN A O   
337  C CB  . ASN A 48  ? 1.0091 1.0315 0.9573 -0.0712 0.0034  -0.0735 50  ASN A CB  
338  C CG  . ASN A 48  ? 1.0698 1.0972 1.0071 -0.0692 -0.0116 -0.0651 50  ASN A CG  
339  O OD1 . ASN A 48  ? 1.0969 1.1225 1.0227 -0.0658 -0.0124 -0.0542 50  ASN A OD1 
340  N ND2 . ASN A 48  ? 1.0704 1.1043 1.0135 -0.0713 -0.0240 -0.0697 50  ASN A ND2 
341  N N   . ASP A 49  ? 1.0562 1.0567 0.9225 -0.0823 0.0185  -0.0921 51  ASP A N   
342  C CA  . ASP A 49  ? 1.0943 1.0908 0.9317 -0.0878 0.0146  -0.1038 51  ASP A CA  
343  C C   . ASP A 49  ? 1.1183 1.1060 0.9164 -0.0893 0.0224  -0.1019 51  ASP A C   
344  O O   . ASP A 49  ? 1.1161 1.0995 0.9133 -0.0868 0.0348  -0.0940 51  ASP A O   
345  C CB  . ASP A 49  ? 1.1343 1.1286 0.9858 -0.0920 0.0208  -0.1216 51  ASP A CB  
346  C CG  . ASP A 49  ? 1.2193 1.2108 1.0978 -0.0907 0.0380  -0.1240 51  ASP A CG  
347  O OD1 . ASP A 49  ? 1.2477 1.2322 1.1149 -0.0902 0.0525  -0.1221 51  ASP A OD1 
348  O OD2 . ASP A 49  ? 1.2321 1.2286 1.1439 -0.0902 0.0368  -0.1270 51  ASP A OD2 
349  N N   . LYS A 50  ? 1.1415 1.1267 0.9075 -0.0936 0.0142  -0.1089 52  LYS A N   
350  C CA  . LYS A 50  ? 1.1706 1.1468 0.8944 -0.0967 0.0218  -0.1121 52  LYS A CA  
351  C C   . LYS A 50  ? 1.1688 1.1450 0.8683 -0.0941 0.0159  -0.0945 52  LYS A C   
352  O O   . LYS A 50  ? 1.1826 1.1514 0.8538 -0.0949 0.0270  -0.0914 52  LYS A O   
353  C CB  . LYS A 50  ? 1.2095 1.1771 0.9342 -0.0976 0.0455  -0.1199 52  LYS A CB  
354  C CG  . LYS A 50  ? 1.2698 1.2349 1.0084 -0.1014 0.0520  -0.1397 52  LYS A CG  
355  C CD  . LYS A 50  ? 1.3456 1.3015 1.0810 -0.1023 0.0758  -0.1464 52  LYS A CD  
356  C CE  . LYS A 50  ? 1.3884 1.3420 1.1486 -0.1048 0.0847  -0.1638 52  LYS A CE  
357  N NZ  . LYS A 50  ? 1.4113 1.3591 1.1864 -0.1034 0.1074  -0.1646 52  LYS A NZ  
358  N N   . SER A 51  ? 1.1473 1.1318 0.8589 -0.0909 -0.0012 -0.0828 53  SER A N   
359  C CA  . SER A 51  ? 1.1486 1.1337 0.8391 -0.0887 -0.0099 -0.0664 53  SER A CA  
360  C C   . SER A 51  ? 1.1298 1.1091 0.8168 -0.0856 0.0058  -0.0547 53  SER A C   
361  O O   . SER A 51  ? 1.1399 1.1133 0.7941 -0.0868 0.0100  -0.0488 53  SER A O   
362  C CB  . SER A 51  ? 1.2040 1.1865 0.8524 -0.0935 -0.0205 -0.0706 53  SER A CB  
363  O OG  . SER A 51  ? 1.2646 1.2385 0.8853 -0.0986 -0.0087 -0.0855 53  SER A OG  
364  N N   . LYS A 52  ? 1.0996 1.0807 0.8217 -0.0816 0.0141  -0.0512 54  LYS A N   
365  C CA  . LYS A 52  ? 1.0820 1.0576 0.8096 -0.0790 0.0302  -0.0427 54  LYS A CA  
366  C C   . LYS A 52  ? 1.0673 1.0469 0.8168 -0.0732 0.0241  -0.0270 54  LYS A C   
367  O O   . LYS A 52  ? 1.0538 1.0411 0.8239 -0.0706 0.0113  -0.0251 54  LYS A O   
368  C CB  . LYS A 52  ? 1.0779 1.0509 0.8284 -0.0798 0.0462  -0.0537 54  LYS A CB  
369  C CG  . LYS A 52  ? 1.1033 1.0698 0.8331 -0.0850 0.0577  -0.0689 54  LYS A CG  
370  C CD  . LYS A 52  ? 1.1294 1.0941 0.8880 -0.0853 0.0725  -0.0786 54  LYS A CD  
371  C CE  . LYS A 52  ? 1.1931 1.1487 0.9365 -0.0878 0.0931  -0.0849 54  LYS A CE  
372  N NZ  . LYS A 52  ? 1.2375 1.1876 0.9383 -0.0924 0.0940  -0.0937 54  LYS A NZ  
373  N N   . THR A 53  ? 1.0683 1.0425 0.8141 -0.0712 0.0340  -0.0159 55  THR A N   
374  C CA  . THR A 53  ? 1.0681 1.0442 0.8350 -0.0657 0.0304  -0.0019 55  THR A CA  
375  C C   . THR A 53  ? 1.0529 1.0320 0.8575 -0.0630 0.0346  -0.0059 55  THR A C   
376  O O   . THR A 53  ? 1.0545 1.0320 0.8687 -0.0652 0.0453  -0.0166 55  THR A O   
377  C CB  . THR A 53  ? 1.1054 1.0741 0.8594 -0.0650 0.0410  0.0099  55  THR A CB  
378  O OG1 . THR A 53  ? 1.1368 1.0997 0.8920 -0.0675 0.0594  0.0024  55  THR A OG1 
379  C CG2 . THR A 53  ? 1.1174 1.0836 0.8336 -0.0670 0.0353  0.0176  55  THR A CG2 
380  N N   . TRP A 54  ? 1.0363 1.0197 0.8620 -0.0580 0.0261  0.0026  56  TRP A N   
381  C CA  . TRP A 54  ? 1.0151 1.0013 0.8739 -0.0548 0.0288  0.0008  56  TRP A CA  
382  C C   . TRP A 54  ? 0.9577 0.9378 0.8265 -0.0559 0.0451  -0.0017 56  TRP A C   
383  O O   . TRP A 54  ? 0.9467 0.9287 0.8356 -0.0563 0.0498  -0.0096 56  TRP A O   
384  C CB  . TRP A 54  ? 1.0351 1.0238 0.9086 -0.0491 0.0200  0.0123  56  TRP A CB  
385  C CG  . TRP A 54  ? 1.0871 1.0692 0.9521 -0.0473 0.0234  0.0246  56  TRP A CG  
386  C CD1 . TRP A 54  ? 1.1201 1.0992 0.9601 -0.0485 0.0204  0.0328  56  TRP A CD1 
387  C CD2 . TRP A 54  ? 1.0994 1.0768 0.9820 -0.0444 0.0301  0.0305  56  TRP A CD2 
388  N NE1 . TRP A 54  ? 1.1295 1.1024 0.9719 -0.0463 0.0258  0.0439  56  TRP A NE1 
389  C CE2 . TRP A 54  ? 1.1192 1.0909 0.9884 -0.0438 0.0313  0.0422  56  TRP A CE2 
390  C CE3 . TRP A 54  ? 1.1034 1.0810 1.0117 -0.0423 0.0344  0.0273  56  TRP A CE3 
391  C CZ2 . TRP A 54  ? 1.1283 1.0943 1.0112 -0.0414 0.0368  0.0500  56  TRP A CZ2 
392  C CZ3 . TRP A 54  ? 1.1172 1.0890 1.0371 -0.0400 0.0390  0.0345  56  TRP A CZ3 
393  C CH2 . TRP A 54  ? 1.1234 1.0894 1.0317 -0.0397 0.0403  0.0454  56  TRP A CH2 
394  N N   . GLN A 55  ? 0.9204 0.8935 0.7767 -0.0563 0.0535  0.0059  57  GLN A N   
395  C CA  . GLN A 55  ? 0.8745 0.8415 0.7400 -0.0575 0.0692  0.0051  57  GLN A CA  
396  C C   . GLN A 55  ? 0.8023 0.7677 0.6622 -0.0621 0.0801  -0.0079 57  GLN A C   
397  O O   . GLN A 55  ? 0.7853 0.7498 0.6668 -0.0625 0.0895  -0.0130 57  GLN A O   
398  C CB  . GLN A 55  ? 0.9343 0.8945 0.7853 -0.0574 0.0758  0.0169  57  GLN A CB  
399  C CG  . GLN A 55  ? 1.0121 0.9720 0.8747 -0.0528 0.0678  0.0298  57  GLN A CG  
400  C CD  . GLN A 55  ? 1.0836 1.0378 0.9653 -0.0515 0.0775  0.0363  57  GLN A CD  
401  O OE1 . GLN A 55  ? 1.0970 1.0507 1.0002 -0.0520 0.0846  0.0305  57  GLN A OE1 
402  N NE2 . GLN A 55  ? 1.0946 1.0442 0.9707 -0.0500 0.0773  0.0490  57  GLN A NE2 
403  N N   . ALA A 56  ? 0.7616 0.7266 0.5935 -0.0655 0.0785  -0.0137 58  ALA A N   
404  C CA  . ALA A 56  ? 0.7294 0.6918 0.5542 -0.0699 0.0893  -0.0275 58  ALA A CA  
405  C C   . ALA A 56  ? 0.6725 0.6401 0.5218 -0.0703 0.0865  -0.0388 58  ALA A C   
406  O O   . ALA A 56  ? 0.6584 0.6233 0.5167 -0.0727 0.0985  -0.0486 58  ALA A O   
407  C CB  . ALA A 56  ? 0.7478 0.7081 0.5347 -0.0734 0.0868  -0.0316 58  ALA A CB  
408  N N   . ASN A 57  ? 0.6402 0.6151 0.5020 -0.0678 0.0716  -0.0371 59  ASN A N   
409  C CA  . ASN A 57  ? 0.6182 0.5987 0.5043 -0.0680 0.0682  -0.0462 59  ASN A CA  
410  C C   . ASN A 57  ? 0.5559 0.5378 0.4748 -0.0651 0.0729  -0.0430 59  ASN A C   
411  O O   . ASN A 57  ? 0.5259 0.5109 0.4652 -0.0659 0.0744  -0.0506 59  ASN A O   
412  C CB  . ASN A 57  ? 0.6629 0.6511 0.5485 -0.0668 0.0510  -0.0454 59  ASN A CB  
413  C CG  . ASN A 57  ? 0.7409 0.7281 0.5961 -0.0706 0.0447  -0.0509 59  ASN A CG  
414  O OD1 . ASN A 57  ? 0.7544 0.7378 0.5975 -0.0751 0.0518  -0.0628 59  ASN A OD1 
415  N ND2 . ASN A 57  ? 0.7780 0.7686 0.6203 -0.0689 0.0311  -0.0426 59  ASN A ND2 
416  N N   . LEU A 58  ? 0.5375 0.5171 0.4618 -0.0619 0.0745  -0.0319 60  LEU A N   
417  C CA  . LEU A 58  ? 0.5208 0.5006 0.4733 -0.0595 0.0785  -0.0289 60  LEU A CA  
418  C C   . LEU A 58  ? 0.5195 0.4935 0.4791 -0.0620 0.0942  -0.0320 60  LEU A C   
419  O O   . LEU A 58  ? 0.5276 0.4957 0.4729 -0.0630 0.1022  -0.0278 60  LEU A O   
420  C CB  . LEU A 58  ? 0.5245 0.5038 0.4805 -0.0552 0.0725  -0.0165 60  LEU A CB  
421  C CG  . LEU A 58  ? 0.5487 0.5282 0.5323 -0.0525 0.0740  -0.0132 60  LEU A CG  
422  C CD1 . LEU A 58  ? 0.5422 0.5287 0.5455 -0.0515 0.0688  -0.0186 60  LEU A CD1 
423  C CD2 . LEU A 58  ? 0.5591 0.5368 0.5437 -0.0484 0.0678  -0.0025 60  LEU A CD2 
424  N N   . ARG A 59  ? 0.5120 0.4877 0.4958 -0.0628 0.0989  -0.0381 61  ARG A N   
425  C CA  . ARG A 59  ? 0.5153 0.4863 0.5121 -0.0649 0.1138  -0.0415 61  ARG A CA  
426  C C   . ARG A 59  ? 0.4896 0.4631 0.5196 -0.0627 0.1130  -0.0376 61  ARG A C   
427  O O   . ARG A 59  ? 0.4821 0.4615 0.5257 -0.0611 0.1041  -0.0385 61  ARG A O   
428  C CB  . ARG A 59  ? 0.5727 0.5431 0.5651 -0.0689 0.1206  -0.0550 61  ARG A CB  
429  C CG  . ARG A 59  ? 0.6775 0.6448 0.6922 -0.0708 0.1352  -0.0609 61  ARG A CG  
430  C CD  . ARG A 59  ? 0.7841 0.7444 0.7797 -0.0744 0.1503  -0.0689 61  ARG A CD  
431  N NE  . ARG A 59  ? 0.8431 0.8012 0.8615 -0.0764 0.1636  -0.0780 61  ARG A NE  
432  C CZ  . ARG A 59  ? 0.8946 0.8511 0.9403 -0.0757 0.1733  -0.0738 61  ARG A CZ  
433  N NH1 . ARG A 59  ? 0.9099 0.8646 0.9775 -0.0775 0.1850  -0.0823 61  ARG A NH1 
434  N NH2 . ARG A 59  ? 0.8943 0.8509 0.9476 -0.0733 0.1708  -0.0612 61  ARG A NH2 
435  N N   . LEU A 60  ? 0.4697 0.4387 0.5126 -0.0627 0.1218  -0.0327 62  LEU A N   
436  C CA  . LEU A 60  ? 0.4516 0.4222 0.5263 -0.0615 0.1219  -0.0300 62  LEU A CA  
437  C C   . LEU A 60  ? 0.4618 0.4324 0.5534 -0.0644 0.1322  -0.0391 62  LEU A C   
438  O O   . LEU A 60  ? 0.4754 0.4412 0.5610 -0.0670 0.1452  -0.0435 62  LEU A O   
439  C CB  . LEU A 60  ? 0.4410 0.4067 0.5243 -0.0608 0.1267  -0.0214 62  LEU A CB  
440  C CG  . LEU A 60  ? 0.4435 0.4093 0.5603 -0.0609 0.1299  -0.0192 62  LEU A CG  
441  C CD1 . LEU A 60  ? 0.4453 0.4154 0.5747 -0.0578 0.1160  -0.0147 62  LEU A CD1 
442  C CD2 . LEU A 60  ? 0.4473 0.4071 0.5720 -0.0619 0.1400  -0.0134 62  LEU A CD2 
443  N N   . ILE A 61  ? 0.4598 0.4356 0.5727 -0.0639 0.1270  -0.0414 63  ILE A N   
444  C CA  . ILE A 61  ? 0.4614 0.4377 0.5968 -0.0662 0.1355  -0.0486 63  ILE A CA  
445  C C   . ILE A 61  ? 0.4668 0.4411 0.6309 -0.0660 0.1419  -0.0431 63  ILE A C   
446  O O   . ILE A 61  ? 0.4838 0.4539 0.6570 -0.0682 0.1558  -0.0469 63  ILE A O   
447  C CB  . ILE A 61  ? 0.4670 0.4502 0.6140 -0.0654 0.1258  -0.0515 63  ILE A CB  
448  C CG1 . ILE A 61  ? 0.4943 0.4800 0.6162 -0.0657 0.1184  -0.0566 63  ILE A CG1 
449  C CG2 . ILE A 61  ? 0.4633 0.4470 0.6380 -0.0677 0.1340  -0.0582 63  ILE A CG2 
450  C CD1 . ILE A 61  ? 0.5301 0.5108 0.6256 -0.0685 0.1253  -0.0641 63  ILE A CD1 
451  N N   . SER A 62  ? 0.4568 0.4339 0.6349 -0.0634 0.1320  -0.0343 64  SER A N   
452  C CA  . SER A 62  ? 0.4455 0.4226 0.6558 -0.0635 0.1345  -0.0298 64  SER A CA  
453  C C   . SER A 62  ? 0.4330 0.4119 0.6487 -0.0606 0.1215  -0.0202 64  SER A C   
454  O O   . SER A 62  ? 0.4459 0.4280 0.6462 -0.0582 0.1101  -0.0184 64  SER A O   
455  C CB  . SER A 62  ? 0.4754 0.4567 0.7090 -0.0645 0.1354  -0.0345 64  SER A CB  
456  O OG  . SER A 62  ? 0.5042 0.4862 0.7714 -0.0648 0.1372  -0.0299 64  SER A OG  
457  N N   . LYS A 63  ? 0.4063 0.3831 0.6442 -0.0609 0.1231  -0.0146 65  LYS A N   
458  C CA  . LYS A 63  ? 0.4027 0.3805 0.6496 -0.0587 0.1107  -0.0066 65  LYS A CA  
459  C C   . LYS A 63  ? 0.3942 0.3749 0.6743 -0.0593 0.1079  -0.0034 65  LYS A C   
460  O O   . LYS A 63  ? 0.4087 0.3893 0.7097 -0.0616 0.1181  -0.0061 65  LYS A O   
461  C CB  . LYS A 63  ? 0.4216 0.3936 0.6628 -0.0584 0.1113  -0.0013 65  LYS A CB  
462  C CG  . LYS A 63  ? 0.4516 0.4202 0.6621 -0.0581 0.1152  -0.0029 65  LYS A CG  
463  C CD  . LYS A 63  ? 0.4867 0.4506 0.6920 -0.0569 0.1114  0.0040  65  LYS A CD  
464  C CE  . LYS A 63  ? 0.5467 0.5075 0.7225 -0.0565 0.1146  0.0041  65  LYS A CE  
465  N NZ  . LYS A 63  ? 0.5497 0.5049 0.7252 -0.0558 0.1131  0.0116  65  LYS A NZ  
466  N N   . PHE A 64  ? 0.3748 0.3581 0.6596 -0.0572 0.0941  0.0022  66  PHE A N   
467  C CA  . PHE A 64  ? 0.3573 0.3442 0.6709 -0.0575 0.0885  0.0066  66  PHE A CA  
468  C C   . PHE A 64  ? 0.3554 0.3422 0.6675 -0.0554 0.0736  0.0130  66  PHE A C   
469  O O   . PHE A 64  ? 0.3656 0.3513 0.6536 -0.0529 0.0669  0.0129  66  PHE A O   
470  C CB  . PHE A 64  ? 0.3627 0.3555 0.6834 -0.0575 0.0882  0.0042  66  PHE A CB  
471  C CG  . PHE A 64  ? 0.3737 0.3707 0.6706 -0.0547 0.0793  0.0035  66  PHE A CG  
472  C CD1 . PHE A 64  ? 0.3823 0.3826 0.6781 -0.0522 0.0662  0.0095  66  PHE A CD1 
473  C CD2 . PHE A 64  ? 0.3890 0.3862 0.6641 -0.0546 0.0839  -0.0029 66  PHE A CD2 
474  C CE1 . PHE A 64  ? 0.4030 0.4070 0.6775 -0.0493 0.0596  0.0092  66  PHE A CE1 
475  C CE2 . PHE A 64  ? 0.4039 0.4053 0.6601 -0.0520 0.0759  -0.0029 66  PHE A CE2 
476  C CZ  . PHE A 64  ? 0.4030 0.4078 0.6597 -0.0492 0.0646  0.0033  66  PHE A CZ  
477  N N   . ASP A 65  ? 0.3505 0.3381 0.6888 -0.0563 0.0682  0.0182  67  ASP A N   
478  C CA  . ASP A 65  ? 0.3551 0.3422 0.6933 -0.0548 0.0531  0.0236  67  ASP A CA  
479  C C   . ASP A 65  ? 0.3476 0.3392 0.7111 -0.0555 0.0448  0.0292  67  ASP A C   
480  O O   . ASP A 65  ? 0.3531 0.3434 0.7241 -0.0554 0.0330  0.0340  67  ASP A O   
481  C CB  . ASP A 65  ? 0.3829 0.3632 0.7236 -0.0556 0.0524  0.0253  67  ASP A CB  
482  C CG  . ASP A 65  ? 0.4917 0.4699 0.8645 -0.0590 0.0606  0.0277  67  ASP A CG  
483  O OD1 . ASP A 65  ? 0.5097 0.4897 0.8951 -0.0607 0.0734  0.0252  67  ASP A OD1 
484  O OD2 . ASP A 65  ? 0.5641 0.5388 0.9503 -0.0599 0.0546  0.0316  67  ASP A OD2 
485  N N   . THR A 66  ? 0.3240 0.3207 0.7006 -0.0562 0.0501  0.0288  68  THR A N   
486  C CA  . THR A 66  ? 0.3155 0.3175 0.7121 -0.0563 0.0414  0.0353  68  THR A CA  
487  C C   . THR A 66  ? 0.3041 0.3118 0.6905 -0.0548 0.0422  0.0341  68  THR A C   
488  O O   . THR A 66  ? 0.2959 0.3035 0.6685 -0.0546 0.0519  0.0273  68  THR A O   
489  C CB  . THR A 66  ? 0.3174 0.3199 0.7545 -0.0594 0.0470  0.0385  68  THR A CB  
490  O OG1 . THR A 66  ? 0.3256 0.3295 0.7731 -0.0606 0.0615  0.0335  68  THR A OG1 
491  C CG2 . THR A 66  ? 0.2928 0.2897 0.7427 -0.0612 0.0498  0.0390  68  THR A CG2 
492  N N   . VAL A 67  ? 0.2988 0.3116 0.6929 -0.0538 0.0318  0.0412  69  VAL A N   
493  C CA  . VAL A 67  ? 0.3091 0.3281 0.6999 -0.0525 0.0320  0.0425  69  VAL A CA  
494  C C   . VAL A 67  ? 0.2941 0.3145 0.7083 -0.0549 0.0449  0.0390  69  VAL A C   
495  O O   . VAL A 67  ? 0.2961 0.3186 0.7003 -0.0544 0.0511  0.0340  69  VAL A O   
496  C CB  . VAL A 67  ? 0.3181 0.3419 0.7151 -0.0513 0.0187  0.0527  69  VAL A CB  
497  C CG1 . VAL A 67  ? 0.3409 0.3712 0.7370 -0.0501 0.0204  0.0551  69  VAL A CG1 
498  C CG2 . VAL A 67  ? 0.3202 0.3417 0.6911 -0.0489 0.0061  0.0545  69  VAL A CG2 
499  N N   . GLU A 68  ? 0.2835 0.3028 0.7299 -0.0573 0.0490  0.0411  70  GLU A N   
500  C CA  . GLU A 68  ? 0.2740 0.2939 0.7471 -0.0595 0.0621  0.0372  70  GLU A CA  
501  C C   . GLU A 68  ? 0.2683 0.2835 0.7268 -0.0606 0.0768  0.0252  70  GLU A C   
502  O O   . GLU A 68  ? 0.2623 0.2785 0.7252 -0.0614 0.0858  0.0191  70  GLU A O   
503  C CB  . GLU A 68  ? 0.3144 0.3334 0.8269 -0.0617 0.0634  0.0424  70  GLU A CB  
504  C CG  . GLU A 68  ? 0.3749 0.3992 0.9076 -0.0613 0.0491  0.0550  70  GLU A CG  
505  C CD  . GLU A 68  ? 0.4242 0.4483 0.9387 -0.0599 0.0323  0.0615  70  GLU A CD  
506  O OE1 . GLU A 68  ? 0.4298 0.4489 0.9250 -0.0597 0.0321  0.0570  70  GLU A OE1 
507  O OE2 . GLU A 68  ? 0.4673 0.4959 0.9863 -0.0591 0.0194  0.0712  70  GLU A OE2 
508  N N   . ASP A 69  ? 0.2767 0.2866 0.7183 -0.0606 0.0791  0.0219  71  ASP A N   
509  C CA  . ASP A 69  ? 0.3009 0.3063 0.7242 -0.0615 0.0921  0.0116  71  ASP A CA  
510  C C   . ASP A 69  ? 0.3166 0.3237 0.7066 -0.0598 0.0894  0.0069  71  ASP A C   
511  O O   . ASP A 69  ? 0.3285 0.3341 0.7086 -0.0609 0.0993  -0.0019 71  ASP A O   
512  C CB  . ASP A 69  ? 0.3252 0.3247 0.7403 -0.0620 0.0949  0.0115  71  ASP A CB  
513  C CG  . ASP A 69  ? 0.3266 0.3244 0.7773 -0.0640 0.0995  0.0155  71  ASP A CG  
514  O OD1 . ASP A 69  ? 0.3460 0.3446 0.8231 -0.0656 0.1095  0.0131  71  ASP A OD1 
515  O OD2 . ASP A 69  ? 0.2959 0.2914 0.7498 -0.0640 0.0930  0.0208  71  ASP A OD2 
516  N N   . PHE A 70  ? 0.2987 0.3090 0.6720 -0.0570 0.0759  0.0126  72  PHE A N   
517  C CA  . PHE A 70  ? 0.2911 0.3048 0.6397 -0.0551 0.0727  0.0098  72  PHE A CA  
518  C C   . PHE A 70  ? 0.2741 0.2923 0.6385 -0.0562 0.0773  0.0075  72  PHE A C   
519  O O   . PHE A 70  ? 0.2643 0.2824 0.6171 -0.0569 0.0832  -0.0003 72  PHE A O   
520  C CB  . PHE A 70  ? 0.2890 0.3058 0.6223 -0.0517 0.0588  0.0170  72  PHE A CB  
521  C CG  . PHE A 70  ? 0.2897 0.3120 0.6088 -0.0497 0.0563  0.0162  72  PHE A CG  
522  C CD1 . PHE A 70  ? 0.2966 0.3181 0.5909 -0.0488 0.0587  0.0099  72  PHE A CD1 
523  C CD2 . PHE A 70  ? 0.2862 0.3147 0.6188 -0.0490 0.0517  0.0225  72  PHE A CD2 
524  C CE1 . PHE A 70  ? 0.3073 0.3343 0.5921 -0.0470 0.0563  0.0097  72  PHE A CE1 
525  C CE2 . PHE A 70  ? 0.2871 0.3209 0.6095 -0.0473 0.0504  0.0225  72  PHE A CE2 
526  C CZ  . PHE A 70  ? 0.2995 0.3326 0.5993 -0.0464 0.0528  0.0158  72  PHE A CZ  
527  N N   . TRP A 71  ? 0.2764 0.2984 0.6685 -0.0566 0.0739  0.0146  73  TRP A N   
528  C CA  . TRP A 71  ? 0.2809 0.3069 0.6919 -0.0576 0.0779  0.0135  73  TRP A CA  
529  C C   . TRP A 71  ? 0.2860 0.3081 0.7118 -0.0607 0.0920  0.0034  73  TRP A C   
530  O O   . TRP A 71  ? 0.3099 0.3335 0.7370 -0.0616 0.0963  -0.0026 73  TRP A O   
531  C CB  . TRP A 71  ? 0.2679 0.2986 0.7067 -0.0573 0.0712  0.0247  73  TRP A CB  
532  C CG  . TRP A 71  ? 0.2711 0.3069 0.6941 -0.0543 0.0585  0.0338  73  TRP A CG  
533  C CD1 . TRP A 71  ? 0.2714 0.3084 0.6937 -0.0528 0.0473  0.0436  73  TRP A CD1 
534  C CD2 . TRP A 71  ? 0.2608 0.3013 0.6671 -0.0525 0.0563  0.0338  73  TRP A CD2 
535  N NE1 . TRP A 71  ? 0.2692 0.3111 0.6735 -0.0500 0.0391  0.0494  73  TRP A NE1 
536  C CE2 . TRP A 71  ? 0.2671 0.3114 0.6621 -0.0496 0.0449  0.0440  73  TRP A CE2 
537  C CE3 . TRP A 71  ? 0.2548 0.2966 0.6542 -0.0530 0.0626  0.0258  73  TRP A CE3 
538  C CZ2 . TRP A 71  ? 0.2655 0.3149 0.6434 -0.0469 0.0413  0.0468  73  TRP A CZ2 
539  C CZ3 . TRP A 71  ? 0.2568 0.3042 0.6420 -0.0507 0.0579  0.0291  73  TRP A CZ3 
540  C CH2 . TRP A 71  ? 0.2654 0.3167 0.6406 -0.0475 0.0482  0.0398  73  TRP A CH2 
541  N N   . ALA A 72  ? 0.2721 0.2891 0.7098 -0.0623 0.0996  0.0011  74  ALA A N   
542  C CA  . ALA A 72  ? 0.2888 0.3010 0.7355 -0.0649 0.1150  -0.0101 74  ALA A CA  
543  C C   . ALA A 72  ? 0.3153 0.3249 0.7281 -0.0653 0.1195  -0.0210 74  ALA A C   
544  O O   . ALA A 72  ? 0.3313 0.3400 0.7470 -0.0670 0.1268  -0.0302 74  ALA A O   
545  C CB  . ALA A 72  ? 0.2933 0.3004 0.7537 -0.0661 0.1227  -0.0097 74  ALA A CB  
546  N N   . LEU A 73  ? 0.3346 0.3427 0.7164 -0.0638 0.1144  -0.0199 75  LEU A N   
547  C CA  . LEU A 73  ? 0.3524 0.3584 0.7010 -0.0640 0.1164  -0.0282 75  LEU A CA  
548  C C   . LEU A 73  ? 0.3468 0.3583 0.6882 -0.0632 0.1097  -0.0296 75  LEU A C   
549  O O   . LEU A 73  ? 0.3558 0.3661 0.6865 -0.0649 0.1144  -0.0393 75  LEU A O   
550  C CB  . LEU A 73  ? 0.3724 0.3761 0.6946 -0.0620 0.1106  -0.0239 75  LEU A CB  
551  C CG  . LEU A 73  ? 0.4177 0.4197 0.7052 -0.0618 0.1106  -0.0299 75  LEU A CG  
552  C CD1 . LEU A 73  ? 0.4331 0.4294 0.7139 -0.0648 0.1241  -0.0403 75  LEU A CD1 
553  C CD2 . LEU A 73  ? 0.4350 0.4351 0.7022 -0.0594 0.1038  -0.0239 75  LEU A CD2 
554  N N   . TYR A 74  ? 0.3302 0.3477 0.6774 -0.0608 0.0987  -0.0199 76  TYR A N   
555  C CA  . TYR A 74  ? 0.3369 0.3603 0.6809 -0.0598 0.0929  -0.0193 76  TYR A CA  
556  C C   . TYR A 74  ? 0.3638 0.3882 0.7317 -0.0625 0.0997  -0.0255 76  TYR A C   
557  O O   . TYR A 74  ? 0.3648 0.3901 0.7239 -0.0637 0.1007  -0.0332 76  TYR A O   
558  C CB  . TYR A 74  ? 0.3111 0.3404 0.6597 -0.0567 0.0819  -0.0067 76  TYR A CB  
559  C CG  . TYR A 74  ? 0.2909 0.3269 0.6353 -0.0553 0.0767  -0.0048 76  TYR A CG  
560  C CD1 . TYR A 74  ? 0.2844 0.3247 0.6546 -0.0564 0.0781  -0.0028 76  TYR A CD1 
561  C CD2 . TYR A 74  ? 0.2961 0.3342 0.6133 -0.0526 0.0707  -0.0043 76  TYR A CD2 
562  C CE1 . TYR A 74  ? 0.2896 0.3363 0.6583 -0.0553 0.0740  -0.0004 76  TYR A CE1 
563  C CE2 . TYR A 74  ? 0.2976 0.3422 0.6133 -0.0512 0.0668  -0.0021 76  TYR A CE2 
564  C CZ  . TYR A 74  ? 0.3143 0.3633 0.6557 -0.0526 0.0686  0.0000  76  TYR A CZ  
565  O OH  . TYR A 74  ? 0.3650 0.4207 0.7075 -0.0514 0.0655  0.0028  76  TYR A OH  
566  N N   . ASN A 75  ? 0.3746 0.3986 0.7748 -0.0636 0.1038  -0.0221 77  ASN A N   
567  C CA  . ASN A 75  ? 0.3925 0.4166 0.8205 -0.0661 0.1110  -0.0277 77  ASN A CA  
568  C C   . ASN A 75  ? 0.4127 0.4301 0.8308 -0.0690 0.1225  -0.0436 77  ASN A C   
569  O O   . ASN A 75  ? 0.4255 0.4431 0.8466 -0.0708 0.1249  -0.0521 77  ASN A O   
570  C CB  . ASN A 75  ? 0.4011 0.4255 0.8664 -0.0664 0.1134  -0.0203 77  ASN A CB  
571  C CG  . ASN A 75  ? 0.4576 0.4890 0.9345 -0.0640 0.1017  -0.0048 77  ASN A CG  
572  O OD1 . ASN A 75  ? 0.4976 0.5343 0.9617 -0.0623 0.0937  0.0000  77  ASN A OD1 
573  N ND2 . ASN A 75  ? 0.4594 0.4909 0.9609 -0.0639 0.1003  0.0039  77  ASN A ND2 
574  N N   . HIS A 76  ? 0.4263 0.4377 0.8318 -0.0695 0.1293  -0.0476 78  HIS A N   
575  C CA  . HIS A 76  ? 0.4484 0.4531 0.8375 -0.0721 0.1402  -0.0622 78  HIS A CA  
576  C C   . HIS A 76  ? 0.4564 0.4623 0.8135 -0.0725 0.1345  -0.0689 78  HIS A C   
577  O O   . HIS A 76  ? 0.4655 0.4697 0.8247 -0.0749 0.1386  -0.0799 78  HIS A O   
578  C CB  . HIS A 76  ? 0.4705 0.4693 0.8478 -0.0721 0.1478  -0.0625 78  HIS A CB  
579  C CG  . HIS A 76  ? 0.5813 0.5731 0.9391 -0.0746 0.1598  -0.0766 78  HIS A CG  
580  N ND1 . HIS A 76  ? 0.6432 0.6319 0.9640 -0.0744 0.1596  -0.0786 78  HIS A ND1 
581  C CD2 . HIS A 76  ? 0.6174 0.6046 0.9870 -0.0773 0.1720  -0.0893 78  HIS A CD2 
582  C CE1 . HIS A 76  ? 0.6700 0.6525 0.9793 -0.0771 0.1714  -0.0918 78  HIS A CE1 
583  N NE2 . HIS A 76  ? 0.6607 0.6419 0.9981 -0.0789 0.1794  -0.0995 78  HIS A NE2 
584  N N   . ILE A 77  ? 0.4564 0.4649 0.7858 -0.0701 0.1247  -0.0626 79  ILE A N   
585  C CA  . ILE A 77  ? 0.4629 0.4733 0.7648 -0.0701 0.1182  -0.0674 79  ILE A CA  
586  C C   . ILE A 77  ? 0.4606 0.4767 0.7798 -0.0709 0.1134  -0.0691 79  ILE A C   
587  O O   . ILE A 77  ? 0.4463 0.4615 0.7564 -0.0732 0.1136  -0.0794 79  ILE A O   
588  C CB  . ILE A 77  ? 0.4663 0.4799 0.7445 -0.0666 0.1076  -0.0576 79  ILE A CB  
589  C CG1 . ILE A 77  ? 0.4953 0.5031 0.7555 -0.0659 0.1114  -0.0557 79  ILE A CG1 
590  C CG2 . ILE A 77  ? 0.4610 0.4781 0.7179 -0.0664 0.0999  -0.0611 79  ILE A CG2 
591  C CD1 . ILE A 77  ? 0.5351 0.5371 0.7653 -0.0680 0.1168  -0.0653 79  ILE A CD1 
592  N N   . GLN A 78  ? 0.4752 0.4971 0.8191 -0.0691 0.1087  -0.0584 80  GLN A N   
593  C CA  . GLN A 78  ? 0.5030 0.5310 0.8657 -0.0694 0.1041  -0.0569 80  GLN A CA  
594  C C   . GLN A 78  ? 0.5564 0.5807 0.9393 -0.0733 0.1124  -0.0695 80  GLN A C   
595  O O   . GLN A 78  ? 0.5614 0.5885 0.9481 -0.0748 0.1092  -0.0745 80  GLN A O   
596  C CB  . GLN A 78  ? 0.4964 0.5302 0.8831 -0.0668 0.0995  -0.0420 80  GLN A CB  
597  C CG  . GLN A 78  ? 0.5190 0.5611 0.9162 -0.0655 0.0922  -0.0349 80  GLN A CG  
598  C CD  . GLN A 78  ? 0.5594 0.6063 0.9802 -0.0635 0.0890  -0.0203 80  GLN A CD  
599  O OE1 . GLN A 78  ? 0.5739 0.6181 1.0132 -0.0639 0.0926  -0.0168 80  GLN A OE1 
600  N NE2 . GLN A 78  ? 0.5590 0.6133 0.9797 -0.0611 0.0820  -0.0106 80  GLN A NE2 
601  N N   . LEU A 79  ? 0.5977 0.6156 0.9947 -0.0751 0.1233  -0.0750 81  LEU A N   
602  C CA  . LEU A 79  ? 0.6379 0.6507 1.0539 -0.0787 0.1330  -0.0887 81  LEU A CA  
603  C C   . LEU A 79  ? 0.6898 0.6950 1.0773 -0.0815 0.1396  -0.1055 81  LEU A C   
604  O O   . LEU A 79  ? 0.6953 0.6975 1.0883 -0.0846 0.1428  -0.1186 81  LEU A O   
605  C CB  . LEU A 79  ? 0.6338 0.6437 1.0836 -0.0788 0.1423  -0.0860 81  LEU A CB  
606  C CG  . LEU A 79  ? 0.6620 0.6788 1.1418 -0.0764 0.1359  -0.0693 81  LEU A CG  
607  C CD1 . LEU A 79  ? 0.6571 0.6710 1.1621 -0.0760 0.1432  -0.0643 81  LEU A CD1 
608  C CD2 . LEU A 79  ? 0.6778 0.6990 1.1863 -0.0776 0.1332  -0.0687 81  LEU A CD2 
609  N N   . SER A 80  ? 0.7255 0.7272 1.0831 -0.0806 0.1416  -0.1052 82  SER A N   
610  C CA  . SER A 80  ? 0.7736 0.7676 1.1028 -0.0832 0.1491  -0.1196 82  SER A CA  
611  C C   . SER A 80  ? 0.8058 0.8014 1.0980 -0.0836 0.1393  -0.1230 82  SER A C   
612  O O   . SER A 80  ? 0.8274 0.8167 1.0939 -0.0861 0.1442  -0.1351 82  SER A O   
613  C CB  . SER A 80  ? 0.8202 0.8089 1.1400 -0.0822 0.1588  -0.1171 82  SER A CB  
614  O OG  . SER A 80  ? 0.8874 0.8780 1.1793 -0.0798 0.1516  -0.1076 82  SER A OG  
615  N N   . SER A 81  ? 0.8041 0.8077 1.0931 -0.0812 0.1259  -0.1126 83  SER A N   
616  C CA  . SER A 81  ? 0.8200 0.8255 1.0753 -0.0809 0.1164  -0.1134 83  SER A CA  
617  C C   . SER A 81  ? 0.8219 0.8341 1.0865 -0.0815 0.1059  -0.1138 83  SER A C   
618  O O   . SER A 81  ? 0.8051 0.8232 1.0983 -0.0801 0.1032  -0.1059 83  SER A O   
619  C CB  . SER A 81  ? 0.8316 0.8397 1.0697 -0.0769 0.1108  -0.0998 83  SER A CB  
620  O OG  . SER A 81  ? 0.8630 0.8650 1.0931 -0.0765 0.1200  -0.0984 83  SER A OG  
621  N N   . ASN A 82  ? 0.8450 0.8568 1.0859 -0.0836 0.0999  -0.1224 84  ASN A N   
622  C CA  . ASN A 82  ? 0.8680 0.8867 1.1154 -0.0843 0.0886  -0.1228 84  ASN A CA  
623  C C   . ASN A 82  ? 0.8806 0.9040 1.1008 -0.0818 0.0773  -0.1155 84  ASN A C   
624  O O   . ASN A 82  ? 0.8903 0.9097 1.0815 -0.0810 0.0781  -0.1149 84  ASN A O   
625  C CB  . ASN A 82  ? 0.9022 0.9164 1.1504 -0.0896 0.0894  -0.1407 84  ASN A CB  
626  C CG  . ASN A 82  ? 0.9578 0.9723 1.2452 -0.0918 0.0937  -0.1456 84  ASN A CG  
627  O OD1 . ASN A 82  ? 0.9619 0.9799 1.2787 -0.0894 0.0971  -0.1352 84  ASN A OD1 
628  N ND2 . ASN A 82  ? 0.9795 0.9899 1.2686 -0.0964 0.0933  -0.1617 84  ASN A ND2 
629  N N   . LEU A 83  ? 0.8750 0.9070 1.1071 -0.0805 0.0674  -0.1097 85  LEU A N   
630  C CA  . LEU A 83  ? 0.8833 0.9213 1.0986 -0.0771 0.0572  -0.1002 85  LEU A CA  
631  C C   . LEU A 83  ? 0.8926 0.9300 1.0828 -0.0797 0.0487  -0.1084 85  LEU A C   
632  O O   . LEU A 83  ? 0.8886 0.9283 1.0890 -0.0831 0.0433  -0.1165 85  LEU A O   
633  C CB  . LEU A 83  ? 0.8752 0.9230 1.1168 -0.0744 0.0520  -0.0900 85  LEU A CB  
634  C CG  . LEU A 83  ? 0.8883 0.9431 1.1193 -0.0698 0.0436  -0.0783 85  LEU A CG  
635  C CD1 . LEU A 83  ? 0.8953 0.9480 1.1154 -0.0653 0.0472  -0.0681 85  LEU A CD1 
636  C CD2 . LEU A 83  ? 0.8864 0.9506 1.1437 -0.0683 0.0394  -0.0713 85  LEU A CD2 
637  N N   . MET A 84  ? 0.8943 0.9286 1.0530 -0.0782 0.0467  -0.1058 86  MET A N   
638  C CA  . MET A 84  ? 0.8982 0.9315 1.0294 -0.0805 0.0380  -0.1118 86  MET A CA  
639  C C   . MET A 84  ? 0.8685 0.9083 0.9900 -0.0760 0.0281  -0.0995 86  MET A C   
640  O O   . MET A 84  ? 0.8746 0.9128 0.9863 -0.0722 0.0313  -0.0903 86  MET A O   
641  C CB  . MET A 84  ? 0.9375 0.9609 1.0379 -0.0825 0.0452  -0.1184 86  MET A CB  
642  C CG  . MET A 84  ? 0.9971 1.0128 1.0974 -0.0878 0.0536  -0.1348 86  MET A CG  
643  S SD  . MET A 84  ? 1.1281 1.1323 1.1904 -0.0896 0.0643  -0.1408 86  MET A SD  
644  C CE  . MET A 84  ? 1.0681 1.0710 1.1448 -0.0848 0.0765  -0.1273 86  MET A CE  
645  N N   . PRO A 85  ? 0.8363 0.8833 0.9620 -0.0763 0.0161  -0.0988 87  PRO A N   
646  C CA  . PRO A 85  ? 0.8190 0.8711 0.9327 -0.0720 0.0071  -0.0879 87  PRO A CA  
647  C C   . PRO A 85  ? 0.8023 0.8481 0.8804 -0.0724 0.0055  -0.0881 87  PRO A C   
648  O O   . PRO A 85  ? 0.8122 0.8502 0.8719 -0.0765 0.0099  -0.0979 87  PRO A O   
649  C CB  . PRO A 85  ? 0.8281 0.8890 0.9570 -0.0731 -0.0048 -0.0888 87  PRO A CB  
650  C CG  . PRO A 85  ? 0.8298 0.8913 0.9853 -0.0770 -0.0009 -0.0974 87  PRO A CG  
651  C CD  . PRO A 85  ? 0.8231 0.8741 0.9677 -0.0802 0.0102  -0.1074 87  PRO A CD  
652  N N   . GLY A 86  ? 0.7762 0.8251 0.8453 -0.0678 -0.0002 -0.0768 88  GLY A N   
653  C CA  . GLY A 86  ? 0.7698 0.8129 0.8087 -0.0669 -0.0008 -0.0731 88  GLY A CA  
654  C C   . GLY A 86  ? 0.7459 0.7823 0.7800 -0.0647 0.0113  -0.0687 88  GLY A C   
655  O O   . GLY A 86  ? 0.7539 0.7869 0.7701 -0.0623 0.0110  -0.0615 88  GLY A O   
656  N N   . CYS A 87  ? 0.7139 0.7483 0.7659 -0.0657 0.0215  -0.0725 89  CYS A N   
657  C CA  . CYS A 87  ? 0.7003 0.7288 0.7526 -0.0640 0.0324  -0.0686 89  CYS A CA  
658  C C   . CYS A 87  ? 0.6401 0.6726 0.7064 -0.0582 0.0312  -0.0565 89  CYS A C   
659  O O   . CYS A 87  ? 0.6225 0.6627 0.7031 -0.0554 0.0247  -0.0520 89  CYS A O   
660  C CB  . CYS A 87  ? 0.7260 0.7508 0.7934 -0.0674 0.0431  -0.0774 89  CYS A CB  
661  S SG  . CYS A 87  ? 0.8674 0.8850 0.9149 -0.0740 0.0473  -0.0932 89  CYS A SG  
662  N N   . ASP A 88  ? 0.5991 0.6260 0.6606 -0.0565 0.0379  -0.0517 90  ASP A N   
663  C CA  . ASP A 88  ? 0.5488 0.5774 0.6223 -0.0517 0.0380  -0.0425 90  ASP A CA  
664  C C   . ASP A 88  ? 0.4877 0.5105 0.5691 -0.0527 0.0481  -0.0427 90  ASP A C   
665  O O   . ASP A 88  ? 0.4988 0.5149 0.5688 -0.0555 0.0550  -0.0466 90  ASP A O   
666  C CB  . ASP A 88  ? 0.5925 0.6203 0.6509 -0.0477 0.0323  -0.0342 90  ASP A CB  
667  C CG  . ASP A 88  ? 0.6877 0.7197 0.7341 -0.0470 0.0221  -0.0332 90  ASP A CG  
668  O OD1 . ASP A 88  ? 0.6805 0.7195 0.7376 -0.0477 0.0169  -0.0361 90  ASP A OD1 
669  O OD2 . ASP A 88  ? 0.7471 0.7758 0.7755 -0.0458 0.0190  -0.0286 90  ASP A OD2 
670  N N   . TYR A 89  ? 0.4265 0.4521 0.5280 -0.0503 0.0491  -0.0382 91  TYR A N   
671  C CA  . TYR A 89  ? 0.3857 0.4067 0.4968 -0.0501 0.0560  -0.0354 91  TYR A CA  
672  C C   . TYR A 89  ? 0.3226 0.3439 0.4330 -0.0452 0.0512  -0.0262 91  TYR A C   
673  O O   . TYR A 89  ? 0.3077 0.3347 0.4199 -0.0418 0.0444  -0.0222 91  TYR A O   
674  C CB  . TYR A 89  ? 0.3991 0.4225 0.5352 -0.0518 0.0604  -0.0379 91  TYR A CB  
675  C CG  . TYR A 89  ? 0.4380 0.4592 0.5778 -0.0568 0.0671  -0.0483 91  TYR A CG  
676  C CD1 . TYR A 89  ? 0.4665 0.4916 0.6057 -0.0588 0.0633  -0.0547 91  TYR A CD1 
677  C CD2 . TYR A 89  ? 0.4827 0.4976 0.6284 -0.0594 0.0774  -0.0521 91  TYR A CD2 
678  C CE1 . TYR A 89  ? 0.5018 0.5238 0.6439 -0.0634 0.0692  -0.0657 91  TYR A CE1 
679  C CE2 . TYR A 89  ? 0.5068 0.5188 0.6560 -0.0637 0.0846  -0.0628 91  TYR A CE2 
680  C CZ  . TYR A 89  ? 0.5368 0.5521 0.6836 -0.0657 0.0803  -0.0701 91  TYR A CZ  
681  O OH  . TYR A 89  ? 0.6083 0.6200 0.7585 -0.0701 0.0871  -0.0822 91  TYR A OH  
682  N N   . SER A 90  ? 0.2972 0.3123 0.4058 -0.0450 0.0551  -0.0232 92  SER A N   
683  C CA  . SER A 90  ? 0.2646 0.2781 0.3722 -0.0409 0.0508  -0.0158 92  SER A CA  
684  C C   . SER A 90  ? 0.2377 0.2468 0.3593 -0.0420 0.0557  -0.0140 92  SER A C   
685  O O   . SER A 90  ? 0.2205 0.2248 0.3431 -0.0453 0.0634  -0.0169 92  SER A O   
686  C CB  . SER A 90  ? 0.2909 0.2995 0.3789 -0.0396 0.0489  -0.0133 92  SER A CB  
687  O OG  . SER A 90  ? 0.3876 0.4002 0.4630 -0.0387 0.0433  -0.0141 92  SER A OG  
688  N N   . LEU A 91  ? 0.2233 0.2341 0.3557 -0.0392 0.0513  -0.0092 93  LEU A N   
689  C CA  . LEU A 91  ? 0.2267 0.2332 0.3710 -0.0396 0.0529  -0.0061 93  LEU A CA  
690  C C   . LEU A 91  ? 0.2287 0.2312 0.3638 -0.0362 0.0470  -0.0016 93  LEU A C   
691  O O   . LEU A 91  ? 0.2266 0.2322 0.3584 -0.0325 0.0404  0.0008  93  LEU A O   
692  C CB  . LEU A 91  ? 0.2233 0.2341 0.3873 -0.0396 0.0514  -0.0040 93  LEU A CB  
693  C CG  . LEU A 91  ? 0.2165 0.2233 0.3969 -0.0409 0.0525  -0.0008 93  LEU A CG  
694  C CD1 . LEU A 91  ? 0.2315 0.2351 0.4240 -0.0453 0.0628  -0.0047 93  LEU A CD1 
695  C CD2 . LEU A 91  ? 0.2145 0.2258 0.4097 -0.0397 0.0473  0.0036  93  LEU A CD2 
696  N N   . PHE A 92  ? 0.2277 0.2231 0.3593 -0.0373 0.0501  -0.0004 94  PHE A N   
697  C CA  . PHE A 92  ? 0.2490 0.2394 0.3741 -0.0344 0.0447  0.0034  94  PHE A CA  
698  C C   . PHE A 92  ? 0.2630 0.2479 0.4026 -0.0361 0.0459  0.0058  94  PHE A C   
699  O O   . PHE A 92  ? 0.2711 0.2546 0.4226 -0.0398 0.0534  0.0049  94  PHE A O   
700  C CB  . PHE A 92  ? 0.2512 0.2380 0.3585 -0.0338 0.0456  0.0041  94  PHE A CB  
701  C CG  . PHE A 92  ? 0.2552 0.2468 0.3491 -0.0305 0.0400  0.0038  94  PHE A CG  
702  C CD1 . PHE A 92  ? 0.2672 0.2655 0.3591 -0.0316 0.0409  0.0004  94  PHE A CD1 
703  C CD2 . PHE A 92  ? 0.2633 0.2526 0.3496 -0.0263 0.0338  0.0069  94  PHE A CD2 
704  C CE1 . PHE A 92  ? 0.2794 0.2827 0.3627 -0.0285 0.0353  0.0007  94  PHE A CE1 
705  C CE2 . PHE A 92  ? 0.2783 0.2724 0.3555 -0.0229 0.0291  0.0070  94  PHE A CE2 
706  C CZ  . PHE A 92  ? 0.2815 0.2828 0.3578 -0.0241 0.0298  0.0042  94  PHE A CZ  
707  N N   . LYS A 93  ? 0.2576 0.2390 0.3977 -0.0334 0.0386  0.0086  95  LYS A N   
708  C CA  . LYS A 93  ? 0.2773 0.2527 0.4316 -0.0351 0.0382  0.0110  95  LYS A CA  
709  C C   . LYS A 93  ? 0.3025 0.2725 0.4569 -0.0380 0.0470  0.0121  95  LYS A C   
710  O O   . LYS A 93  ? 0.3019 0.2707 0.4400 -0.0375 0.0499  0.0122  95  LYS A O   
711  C CB  . LYS A 93  ? 0.3005 0.2717 0.4514 -0.0318 0.0285  0.0125  95  LYS A CB  
712  C CG  . LYS A 93  ? 0.2811 0.2567 0.4333 -0.0294 0.0207  0.0119  95  LYS A CG  
713  C CD  . LYS A 93  ? 0.2867 0.2574 0.4317 -0.0258 0.0118  0.0117  95  LYS A CD  
714  C CE  . LYS A 93  ? 0.3042 0.2790 0.4487 -0.0238 0.0049  0.0115  95  LYS A CE  
715  N NZ  . LYS A 93  ? 0.3177 0.2882 0.4504 -0.0196 -0.0032 0.0096  95  LYS A NZ  
716  N N   . ASP A 94  ? 0.3304 0.2976 0.5035 -0.0412 0.0514  0.0136  96  ASP A N   
717  C CA  . ASP A 94  ? 0.3621 0.3242 0.5383 -0.0441 0.0614  0.0154  96  ASP A CA  
718  C C   . ASP A 94  ? 0.3542 0.3102 0.5188 -0.0421 0.0582  0.0191  96  ASP A C   
719  O O   . ASP A 94  ? 0.3569 0.3100 0.5261 -0.0400 0.0489  0.0205  96  ASP A O   
720  C CB  . ASP A 94  ? 0.4010 0.3613 0.6048 -0.0471 0.0647  0.0174  96  ASP A CB  
721  C CG  . ASP A 94  ? 0.4517 0.4082 0.6633 -0.0505 0.0783  0.0189  96  ASP A CG  
722  O OD1 . ASP A 94  ? 0.4810 0.4375 0.6754 -0.0512 0.0870  0.0170  96  ASP A OD1 
723  O OD2 . ASP A 94  ? 0.4646 0.4183 0.6996 -0.0525 0.0802  0.0221  96  ASP A OD2 
724  N N   . GLY A 95  ? 0.3458 0.3000 0.4944 -0.0426 0.0651  0.0202  97  GLY A N   
725  C CA  . GLY A 95  ? 0.3507 0.2993 0.4886 -0.0410 0.0634  0.0248  97  GLY A CA  
726  C C   . GLY A 95  ? 0.3731 0.3237 0.4902 -0.0372 0.0564  0.0245  97  GLY A C   
727  O O   . GLY A 95  ? 0.3884 0.3343 0.4978 -0.0355 0.0544  0.0290  97  GLY A O   
728  N N   . ILE A 96  ? 0.3742 0.3316 0.4842 -0.0357 0.0526  0.0199  98  ILE A N   
729  C CA  . ILE A 96  ? 0.3651 0.3259 0.4580 -0.0321 0.0464  0.0195  98  ILE A CA  
730  C C   . ILE A 96  ? 0.3692 0.3352 0.4499 -0.0343 0.0518  0.0165  98  ILE A C   
731  O O   . ILE A 96  ? 0.3479 0.3188 0.4348 -0.0360 0.0541  0.0118  98  ILE A O   
732  C CB  . ILE A 96  ? 0.3535 0.3185 0.4500 -0.0285 0.0375  0.0166  98  ILE A CB  
733  C CG1 . ILE A 96  ? 0.3552 0.3145 0.4633 -0.0267 0.0315  0.0177  98  ILE A CG1 
734  C CG2 . ILE A 96  ? 0.3580 0.3269 0.4398 -0.0247 0.0326  0.0164  98  ILE A CG2 
735  C CD1 . ILE A 96  ? 0.3675 0.3304 0.4762 -0.0232 0.0236  0.0147  98  ILE A CD1 
736  N N   . GLU A 97  ? 0.3944 0.3589 0.4583 -0.0344 0.0531  0.0193  99  GLU A N   
737  C CA  . GLU A 97  ? 0.4238 0.3932 0.4730 -0.0361 0.0554  0.0157  99  GLU A CA  
738  C C   . GLU A 97  ? 0.4042 0.3811 0.4511 -0.0331 0.0468  0.0127  99  GLU A C   
739  O O   . GLU A 97  ? 0.3897 0.3669 0.4383 -0.0288 0.0393  0.0153  99  GLU A O   
740  C CB  . GLU A 97  ? 0.5117 0.4778 0.5417 -0.0370 0.0575  0.0204  99  GLU A CB  
741  C CG  . GLU A 97  ? 0.6516 0.6110 0.6820 -0.0404 0.0683  0.0236  99  GLU A CG  
742  C CD  . GLU A 97  ? 0.8391 0.7956 0.8471 -0.0417 0.0716  0.0285  99  GLU A CD  
743  O OE1 . GLU A 97  ? 0.9154 0.8663 0.9224 -0.0443 0.0816  0.0323  99  GLU A OE1 
744  O OE2 . GLU A 97  ? 0.8719 0.8319 0.8639 -0.0403 0.0644  0.0291  99  GLU A OE2 
745  N N   . PRO A 98  ? 0.4034 0.3860 0.4477 -0.0353 0.0484  0.0070  100 PRO A N   
746  C CA  . PRO A 98  ? 0.4134 0.4037 0.4584 -0.0327 0.0411  0.0048  100 PRO A CA  
747  C C   . PRO A 98  ? 0.4249 0.4174 0.4545 -0.0309 0.0348  0.0072  100 PRO A C   
748  O O   . PRO A 98  ? 0.4217 0.4202 0.4473 -0.0317 0.0321  0.0037  100 PRO A O   
749  C CB  . PRO A 98  ? 0.4209 0.4155 0.4722 -0.0364 0.0459  -0.0021 100 PRO A CB  
750  C CG  . PRO A 98  ? 0.4223 0.4120 0.4636 -0.0407 0.0541  -0.0040 100 PRO A CG  
751  C CD  . PRO A 98  ? 0.3857 0.3681 0.4282 -0.0402 0.0575  0.0019  100 PRO A CD  
752  N N   . MET A 99  ? 0.4460 0.4339 0.4693 -0.0283 0.0318  0.0136  101 MET A N   
753  C CA  . MET A 99  ? 0.4829 0.4722 0.4940 -0.0260 0.0251  0.0179  101 MET A CA  
754  C C   . MET A 99  ? 0.4784 0.4654 0.4966 -0.0204 0.0196  0.0228  101 MET A C   
755  O O   . MET A 99  ? 0.4696 0.4503 0.4954 -0.0196 0.0219  0.0245  101 MET A O   
756  C CB  . MET A 99  ? 0.5516 0.5354 0.5464 -0.0289 0.0285  0.0222  101 MET A CB  
757  C CG  . MET A 99  ? 0.6528 0.6371 0.6368 -0.0345 0.0353  0.0165  101 MET A CG  
758  S SD  . MET A 99  ? 0.9153 0.9084 0.8900 -0.0360 0.0282  0.0105  101 MET A SD  
759  C CE  . MET A 99  ? 0.9489 0.9379 0.9040 -0.0427 0.0378  0.0049  101 MET A CE  
760  N N   . TRP A 100 ? 0.4895 0.4815 0.5067 -0.0167 0.0124  0.0245  102 TRP A N   
761  C CA  . TRP A 100 ? 0.5148 0.5051 0.5398 -0.0109 0.0078  0.0276  102 TRP A CA  
762  C C   . TRP A 100 ? 0.5245 0.5060 0.5463 -0.0097 0.0074  0.0344  102 TRP A C   
763  O O   . TRP A 100 ? 0.5381 0.5152 0.5683 -0.0057 0.0056  0.0355  102 TRP A O   
764  C CB  . TRP A 100 ? 0.5209 0.5194 0.5486 -0.0069 0.0013  0.0278  102 TRP A CB  
765  C CG  . TRP A 100 ? 0.5466 0.5457 0.5673 -0.0053 -0.0048 0.0342  102 TRP A CG  
766  C CD1 . TRP A 100 ? 0.5681 0.5711 0.5778 -0.0085 -0.0080 0.0357  102 TRP A CD1 
767  C CD2 . TRP A 100 ? 0.5448 0.5406 0.5701 0.0001  -0.0091 0.0400  102 TRP A CD2 
768  N NE1 . TRP A 100 ? 0.5722 0.5749 0.5790 -0.0057 -0.0147 0.0433  102 TRP A NE1 
769  C CE2 . TRP A 100 ? 0.5584 0.5567 0.5761 -0.0002 -0.0151 0.0461  102 TRP A CE2 
770  C CE3 . TRP A 100 ? 0.5411 0.5318 0.5764 0.0051  -0.0088 0.0401  102 TRP A CE3 
771  C CZ2 . TRP A 100 ? 0.5603 0.5566 0.5826 0.0046  -0.0205 0.0533  102 TRP A CZ2 
772  C CZ3 . TRP A 100 ? 0.5482 0.5363 0.5877 0.0099  -0.0134 0.0459  102 TRP A CZ3 
773  C CH2 . TRP A 100 ? 0.5507 0.5418 0.5850 0.0097  -0.0190 0.0529  102 TRP A CH2 
774  N N   . GLU A 101 ? 0.5187 0.4972 0.5282 -0.0132 0.0093  0.0389  103 GLU A N   
775  C CA  . GLU A 101 ? 0.5196 0.4899 0.5264 -0.0128 0.0100  0.0468  103 GLU A CA  
776  C C   . GLU A 101 ? 0.4878 0.4502 0.5044 -0.0140 0.0160  0.0464  103 GLU A C   
777  O O   . GLU A 101 ? 0.4803 0.4354 0.5008 -0.0126 0.0157  0.0526  103 GLU A O   
778  C CB  . GLU A 101 ? 0.5982 0.5680 0.5869 -0.0167 0.0116  0.0519  103 GLU A CB  
779  C CG  . GLU A 101 ? 0.6991 0.6761 0.6777 -0.0157 0.0034  0.0538  103 GLU A CG  
780  C CD  . GLU A 101 ? 0.7998 0.7847 0.7719 -0.0190 0.0029  0.0459  103 GLU A CD  
781  O OE1 . GLU A 101 ? 0.7447 0.7315 0.7249 -0.0205 0.0078  0.0380  103 GLU A OE1 
782  O OE2 . GLU A 101 ? 0.8835 0.8727 0.8431 -0.0202 -0.0031 0.0480  103 GLU A OE2 
783  N N   . ASP A 102 ? 0.4641 0.4278 0.4870 -0.0167 0.0210  0.0397  104 ASP A N   
784  C CA  . ASP A 102 ? 0.4445 0.4016 0.4796 -0.0181 0.0255  0.0391  104 ASP A CA  
785  C C   . ASP A 102 ? 0.4569 0.4095 0.5034 -0.0135 0.0198  0.0394  104 ASP A C   
786  O O   . ASP A 102 ? 0.4634 0.4200 0.5110 -0.0093 0.0142  0.0364  104 ASP A O   
787  C CB  . ASP A 102 ? 0.4325 0.3935 0.4746 -0.0212 0.0298  0.0319  104 ASP A CB  
788  C CG  . ASP A 102 ? 0.4374 0.3929 0.4938 -0.0236 0.0345  0.0312  104 ASP A CG  
789  O OD1 . ASP A 102 ? 0.4445 0.3965 0.5120 -0.0211 0.0300  0.0306  104 ASP A OD1 
790  O OD2 . ASP A 102 ? 0.4606 0.4155 0.5176 -0.0279 0.0425  0.0308  104 ASP A OD2 
791  N N   . GLU A 103 ? 0.4626 0.4065 0.5182 -0.0141 0.0215  0.0429  105 GLU A N   
792  C CA  . GLU A 103 ? 0.4607 0.3985 0.5281 -0.0103 0.0161  0.0419  105 GLU A CA  
793  C C   . GLU A 103 ? 0.4339 0.3750 0.5065 -0.0081 0.0122  0.0336  105 GLU A C   
794  O O   . GLU A 103 ? 0.4282 0.3672 0.5033 -0.0033 0.0067  0.0314  105 GLU A O   
795  C CB  . GLU A 103 ? 0.5238 0.4524 0.6036 -0.0129 0.0191  0.0453  105 GLU A CB  
796  C CG  . GLU A 103 ? 0.6769 0.5969 0.7639 -0.0097 0.0149  0.0500  105 GLU A CG  
797  C CD  . GLU A 103 ? 0.8294 0.7491 0.9067 -0.0083 0.0150  0.0589  105 GLU A CD  
798  O OE1 . GLU A 103 ? 0.8992 0.8127 0.9834 -0.0048 0.0108  0.0627  105 GLU A OE1 
799  O OE2 . GLU A 103 ? 0.8673 0.7928 0.9305 -0.0108 0.0188  0.0619  105 GLU A OE2 
800  N N   . LYS A 104 ? 0.4124 0.3585 0.4867 -0.0113 0.0154  0.0294  106 LYS A N   
801  C CA  . LYS A 104 ? 0.3977 0.3476 0.4758 -0.0096 0.0120  0.0230  106 LYS A CA  
802  C C   . LYS A 104 ? 0.3838 0.3428 0.4539 -0.0067 0.0104  0.0206  106 LYS A C   
803  O O   . LYS A 104 ? 0.3808 0.3429 0.4530 -0.0047 0.0079  0.0164  106 LYS A O   
804  C CB  . LYS A 104 ? 0.4131 0.3643 0.5000 -0.0141 0.0154  0.0208  106 LYS A CB  
805  C CG  . LYS A 104 ? 0.4874 0.4300 0.5868 -0.0168 0.0165  0.0230  106 LYS A CG  
806  C CD  . LYS A 104 ? 0.5714 0.5071 0.6776 -0.0139 0.0090  0.0209  106 LYS A CD  
807  C CE  . LYS A 104 ? 0.6593 0.5905 0.7818 -0.0176 0.0084  0.0204  106 LYS A CE  
808  N NZ  . LYS A 104 ? 0.7192 0.6417 0.8493 -0.0157 0.0006  0.0182  106 LYS A NZ  
809  N N   . ASN A 105 ? 0.3713 0.3347 0.4324 -0.0066 0.0114  0.0235  107 ASN A N   
810  C CA  . ASN A 105 ? 0.3659 0.3383 0.4223 -0.0041 0.0093  0.0217  107 ASN A CA  
811  C C   . ASN A 105 ? 0.3780 0.3506 0.4307 0.0008  0.0049  0.0250  107 ASN A C   
812  O O   . ASN A 105 ? 0.3470 0.3262 0.4002 0.0044  0.0027  0.0233  107 ASN A O   
813  C CB  . ASN A 105 ? 0.3671 0.3458 0.4182 -0.0085 0.0130  0.0213  107 ASN A CB  
814  C CG  . ASN A 105 ? 0.3849 0.3648 0.4422 -0.0129 0.0178  0.0176  107 ASN A CG  
815  O OD1 . ASN A 105 ? 0.3653 0.3460 0.4304 -0.0118 0.0167  0.0149  107 ASN A OD1 
816  N ND2 . ASN A 105 ? 0.4064 0.3864 0.4599 -0.0178 0.0231  0.0176  107 ASN A ND2 
817  N N   . LYS A 106 ? 0.3925 0.3585 0.4436 0.0010  0.0041  0.0305  108 LYS A N   
818  C CA  . LYS A 106 ? 0.4194 0.3864 0.4683 0.0051  -0.0002 0.0351  108 LYS A CA  
819  C C   . LYS A 106 ? 0.4024 0.3688 0.4583 0.0116  -0.0035 0.0321  108 LYS A C   
820  O O   . LYS A 106 ? 0.4032 0.3754 0.4597 0.0153  -0.0062 0.0335  108 LYS A O   
821  C CB  . LYS A 106 ? 0.4800 0.4400 0.5262 0.0040  -0.0006 0.0431  108 LYS A CB  
822  C CG  . LYS A 106 ? 0.5995 0.5485 0.6541 0.0043  0.0004  0.0444  108 LYS A CG  
823  C CD  . LYS A 106 ? 0.7304 0.6743 0.7808 0.0014  0.0023  0.0536  108 LYS A CD  
824  C CE  . LYS A 106 ? 0.8499 0.7828 0.9118 0.0023  0.0024  0.0567  108 LYS A CE  
825  N NZ  . LYS A 106 ? 0.9066 0.8348 0.9647 -0.0011 0.0061  0.0667  108 LYS A NZ  
826  N N   . ARG A 107 ? 0.3872 0.3473 0.4487 0.0130  -0.0032 0.0276  109 ARG A N   
827  C CA  . ARG A 107 ? 0.3786 0.3376 0.4442 0.0193  -0.0052 0.0230  109 ARG A CA  
828  C C   . ARG A 107 ? 0.3569 0.3236 0.4206 0.0204  -0.0037 0.0172  109 ARG A C   
829  O O   . ARG A 107 ? 0.3304 0.2957 0.3952 0.0252  -0.0041 0.0126  109 ARG A O   
830  C CB  . ARG A 107 ? 0.4197 0.3668 0.4909 0.0202  -0.0067 0.0204  109 ARG A CB  
831  C CG  . ARG A 107 ? 0.4905 0.4297 0.5666 0.0203  -0.0081 0.0271  109 ARG A CG  
832  C CD  . ARG A 107 ? 0.5735 0.5006 0.6578 0.0204  -0.0098 0.0245  109 ARG A CD  
833  N NE  . ARG A 107 ? 0.6780 0.6033 0.7632 0.0149  -0.0084 0.0222  109 ARG A NE  
834  C CZ  . ARG A 107 ? 0.7308 0.6550 0.8175 0.0093  -0.0053 0.0277  109 ARG A CZ  
835  N NH1 . ARG A 107 ? 0.7156 0.6401 0.7998 0.0083  -0.0034 0.0362  109 ARG A NH1 
836  N NH2 . ARG A 107 ? 0.7410 0.6639 0.8315 0.0048  -0.0038 0.0252  109 ARG A NH2 
837  N N   . GLY A 108 ? 0.3508 0.3254 0.4117 0.0160  -0.0014 0.0176  110 GLY A N   
838  C CA  . GLY A 108 ? 0.3300 0.3109 0.3907 0.0155  0.0005  0.0135  110 GLY A CA  
839  C C   . GLY A 108 ? 0.3248 0.3169 0.3860 0.0168  0.0014  0.0144  110 GLY A C   
840  O O   . GLY A 108 ? 0.3330 0.3279 0.3954 0.0196  -0.0003 0.0174  110 GLY A O   
841  N N   . GLY A 109 ? 0.3056 0.3041 0.3679 0.0146  0.0038  0.0124  111 GLY A N   
842  C CA  . GLY A 109 ? 0.2841 0.2937 0.3497 0.0148  0.0049  0.0133  111 GLY A CA  
843  C C   . GLY A 109 ? 0.2728 0.2878 0.3414 0.0113  0.0078  0.0117  111 GLY A C   
844  O O   . GLY A 109 ? 0.2635 0.2742 0.3319 0.0077  0.0087  0.0104  111 GLY A O   
845  N N   . ARG A 110 ? 0.2624 0.2872 0.3364 0.0124  0.0092  0.0123  112 ARG A N   
846  C CA  . ARG A 110 ? 0.2524 0.2833 0.3321 0.0089  0.0118  0.0117  112 ARG A CA  
847  C C   . ARG A 110 ? 0.2582 0.2970 0.3433 0.0128  0.0143  0.0129  112 ARG A C   
848  O O   . ARG A 110 ? 0.2630 0.3068 0.3512 0.0169  0.0143  0.0144  112 ARG A O   
849  C CB  . ARG A 110 ? 0.2642 0.2994 0.3468 0.0037  0.0113  0.0115  112 ARG A CB  
850  C CG  . ARG A 110 ? 0.3017 0.3450 0.3890 0.0054  0.0091  0.0131  112 ARG A CG  
851  C CD  . ARG A 110 ? 0.3075 0.3533 0.3947 -0.0003 0.0074  0.0116  112 ARG A CD  
852  N NE  . ARG A 110 ? 0.3369 0.3908 0.4300 0.0010  0.0036  0.0131  112 ARG A NE  
853  C CZ  . ARG A 110 ? 0.3897 0.4471 0.4828 -0.0035 0.0002  0.0114  112 ARG A CZ  
854  N NH1 . ARG A 110 ? 0.4450 0.5100 0.5454 -0.0022 -0.0046 0.0132  112 ARG A NH1 
855  N NH2 . ARG A 110 ? 0.3689 0.4221 0.4553 -0.0093 0.0016  0.0077  112 ARG A NH2 
856  N N   . TRP A 111 ? 0.2463 0.2865 0.3335 0.0115  0.0166  0.0131  113 TRP A N   
857  C CA  . TRP A 111 ? 0.2440 0.2936 0.3390 0.0129  0.0200  0.0156  113 TRP A CA  
858  C C   . TRP A 111 ? 0.2261 0.2832 0.3330 0.0083  0.0206  0.0162  113 TRP A C   
859  O O   . TRP A 111 ? 0.2121 0.2673 0.3219 0.0029  0.0206  0.0148  113 TRP A O   
860  C CB  . TRP A 111 ? 0.2444 0.2926 0.3370 0.0131  0.0215  0.0167  113 TRP A CB  
861  C CG  . TRP A 111 ? 0.2644 0.3070 0.3450 0.0186  0.0211  0.0155  113 TRP A CG  
862  C CD1 . TRP A 111 ? 0.2831 0.3158 0.3543 0.0186  0.0176  0.0127  113 TRP A CD1 
863  C CD2 . TRP A 111 ? 0.2720 0.3185 0.3495 0.0250  0.0246  0.0165  113 TRP A CD2 
864  N NE1 . TRP A 111 ? 0.2908 0.3204 0.3517 0.0246  0.0183  0.0110  113 TRP A NE1 
865  C CE2 . TRP A 111 ? 0.2825 0.3201 0.3465 0.0288  0.0231  0.0131  113 TRP A CE2 
866  C CE3 . TRP A 111 ? 0.2613 0.3174 0.3472 0.0280  0.0291  0.0196  113 TRP A CE3 
867  C CZ2 . TRP A 111 ? 0.2909 0.3290 0.3478 0.0355  0.0270  0.0122  113 TRP A CZ2 
868  C CZ3 . TRP A 111 ? 0.2688 0.3260 0.3494 0.0348  0.0334  0.0197  113 TRP A CZ3 
869  C CH2 . TRP A 111 ? 0.2851 0.3333 0.3505 0.0385  0.0328  0.0158  113 TRP A CH2 
870  N N   . LEU A 112 ? 0.2358 0.3012 0.3509 0.0102  0.0212  0.0180  114 LEU A N   
871  C CA  . LEU A 112 ? 0.2479 0.3199 0.3745 0.0055  0.0203  0.0174  114 LEU A CA  
872  C C   . LEU A 112 ? 0.2616 0.3432 0.4036 0.0053  0.0241  0.0207  114 LEU A C   
873  O O   . LEU A 112 ? 0.2712 0.3584 0.4176 0.0103  0.0272  0.0245  114 LEU A O   
874  C CB  . LEU A 112 ? 0.2402 0.3144 0.3672 0.0063  0.0160  0.0169  114 LEU A CB  
875  C CG  . LEU A 112 ? 0.2619 0.3424 0.3992 0.0013  0.0130  0.0152  114 LEU A CG  
876  C CD1 . LEU A 112 ? 0.2482 0.3232 0.3792 -0.0049 0.0117  0.0107  114 LEU A CD1 
877  C CD2 . LEU A 112 ? 0.2845 0.3683 0.4228 0.0033  0.0075  0.0163  114 LEU A CD2 
878  N N   . ILE A 113 ? 0.2563 0.3395 0.4077 -0.0004 0.0247  0.0192  115 ILE A N   
879  C CA  . ILE A 113 ? 0.2701 0.3625 0.4400 -0.0019 0.0275  0.0221  115 ILE A CA  
880  C C   . ILE A 113 ? 0.2466 0.3430 0.4264 -0.0063 0.0236  0.0180  115 ILE A C   
881  O O   . ILE A 113 ? 0.2274 0.3184 0.4022 -0.0112 0.0213  0.0125  115 ILE A O   
882  C CB  . ILE A 113 ? 0.3387 0.4291 0.5149 -0.0059 0.0304  0.0227  115 ILE A CB  
883  C CG1 . ILE A 113 ? 0.3764 0.4598 0.5396 -0.0038 0.0311  0.0244  115 ILE A CG1 
884  C CG2 . ILE A 113 ? 0.3619 0.4610 0.5571 -0.0064 0.0339  0.0275  115 ILE A CG2 
885  C CD1 . ILE A 113 ? 0.4269 0.5116 0.5802 0.0033  0.0330  0.0291  115 ILE A CD1 
886  N N   . THR A 114 ? 0.2565 0.3617 0.4499 -0.0049 0.0229  0.0204  116 THR A N   
887  C CA  . THR A 114 ? 0.3036 0.4129 0.5081 -0.0097 0.0180  0.0162  116 THR A CA  
888  C C   . THR A 114 ? 0.3301 0.4466 0.5577 -0.0127 0.0211  0.0178  116 THR A C   
889  O O   . THR A 114 ? 0.3371 0.4608 0.5775 -0.0091 0.0254  0.0247  116 THR A O   
890  C CB  . THR A 114 ? 0.3590 0.4729 0.5651 -0.0070 0.0126  0.0172  116 THR A CB  
891  O OG1 . THR A 114 ? 0.3926 0.4998 0.5795 -0.0033 0.0108  0.0174  116 THR A OG1 
892  C CG2 . THR A 114 ? 0.3794 0.4951 0.5902 -0.0128 0.0047  0.0113  116 THR A CG2 
893  N N   . LEU A 115 ? 0.3354 0.4494 0.5686 -0.0191 0.0196  0.0116  117 LEU A N   
894  C CA  . LEU A 115 ? 0.3472 0.4670 0.6046 -0.0228 0.0217  0.0118  117 LEU A CA  
895  C C   . LEU A 115 ? 0.3700 0.4956 0.6413 -0.0261 0.0152  0.0075  117 LEU A C   
896  O O   . LEU A 115 ? 0.3608 0.4825 0.6206 -0.0292 0.0086  0.0001  117 LEU A O   
897  C CB  . LEU A 115 ? 0.3473 0.4603 0.6051 -0.0280 0.0241  0.0063  117 LEU A CB  
898  C CG  . LEU A 115 ? 0.3658 0.4727 0.6133 -0.0260 0.0291  0.0099  117 LEU A CG  
899  C CD1 . LEU A 115 ? 0.3482 0.4500 0.6023 -0.0311 0.0317  0.0052  117 LEU A CD1 
900  C CD2 . LEU A 115 ? 0.3785 0.4911 0.6346 -0.0215 0.0337  0.0203  117 LEU A CD2 
901  N N   . ASN A 116 ? 0.3977 0.5325 0.6938 -0.0257 0.0168  0.0124  118 ASN A N   
902  C CA  . ASN A 116 ? 0.4397 0.5805 0.7557 -0.0298 0.0106  0.0083  118 ASN A CA  
903  C C   . ASN A 116 ? 0.4397 0.5757 0.7628 -0.0374 0.0092  -0.0016 118 ASN A C   
904  O O   . ASN A 116 ? 0.4184 0.5481 0.7369 -0.0389 0.0147  -0.0031 118 ASN A O   
905  C CB  . ASN A 116 ? 0.4855 0.6377 0.8290 -0.0268 0.0144  0.0178  118 ASN A CB  
906  C CG  . ASN A 116 ? 0.6136 0.7723 0.9835 -0.0316 0.0086  0.0143  118 ASN A CG  
907  O OD1 . ASN A 116 ? 0.6652 0.8255 1.0565 -0.0356 0.0114  0.0136  118 ASN A OD1 
908  N ND2 . ASN A 116 ? 0.6340 0.7964 1.0040 -0.0316 -0.0003 0.0119  118 ASN A ND2 
909  N N   . LYS A 117 ? 0.4630 0.6018 0.7981 -0.0422 0.0015  -0.0085 119 LYS A N   
910  C CA  . LYS A 117 ? 0.4966 0.6304 0.8374 -0.0495 -0.0012 -0.0203 119 LYS A CA  
911  C C   . LYS A 117 ? 0.4870 0.6209 0.8507 -0.0514 0.0069  -0.0184 119 LYS A C   
912  O O   . LYS A 117 ? 0.4956 0.6215 0.8549 -0.0552 0.0099  -0.0260 119 LYS A O   
913  C CB  . LYS A 117 ? 0.5494 0.6886 0.9050 -0.0536 -0.0118 -0.0263 119 LYS A CB  
914  C CG  . LYS A 117 ? 0.6434 0.7823 0.9775 -0.0529 -0.0222 -0.0288 119 LYS A CG  
915  C CD  . LYS A 117 ? 0.7268 0.8757 1.0705 -0.0467 -0.0242 -0.0172 119 LYS A CD  
916  C CE  . LYS A 117 ? 0.7832 0.9352 1.1221 -0.0478 -0.0376 -0.0200 119 LYS A CE  
917  N NZ  . LYS A 117 ? 0.8064 0.9620 1.1367 -0.0406 -0.0378 -0.0102 119 LYS A NZ  
918  N N   . GLN A 118 ? 0.4775 0.6205 0.8663 -0.0485 0.0111  -0.0075 120 GLN A N   
919  C CA  . GLN A 118 ? 0.4925 0.6369 0.9038 -0.0491 0.0193  -0.0016 120 GLN A CA  
920  C C   . GLN A 118 ? 0.4999 0.6371 0.8935 -0.0469 0.0262  0.0013  120 GLN A C   
921  O O   . GLN A 118 ? 0.4968 0.6292 0.8999 -0.0503 0.0300  -0.0018 120 GLN A O   
922  C CB  . GLN A 118 ? 0.5315 0.6873 0.9655 -0.0447 0.0235  0.0125  120 GLN A CB  
923  C CG  . GLN A 118 ? 0.6287 0.7926 1.0936 -0.0481 0.0186  0.0111  120 GLN A CG  
924  C CD  . GLN A 118 ? 0.7345 0.9100 1.2162 -0.0430 0.0214  0.0240  120 GLN A CD  
925  O OE1 . GLN A 118 ? 0.7400 0.9228 1.2552 -0.0445 0.0243  0.0298  120 GLN A OE1 
926  N NE2 . GLN A 118 ? 0.7527 0.9307 1.2153 -0.0369 0.0215  0.0291  120 GLN A NE2 
927  N N   . GLN A 119 ? 0.5031 0.6393 0.8725 -0.0413 0.0275  0.0072  121 GLN A N   
928  C CA  . GLN A 119 ? 0.4940 0.6246 0.8481 -0.0385 0.0330  0.0117  121 GLN A CA  
929  C C   . GLN A 119 ? 0.4893 0.6092 0.8264 -0.0420 0.0324  0.0017  121 GLN A C   
930  O O   . GLN A 119 ? 0.4933 0.6083 0.8209 -0.0404 0.0363  0.0050  121 GLN A O   
931  C CB  . GLN A 119 ? 0.5021 0.6344 0.8366 -0.0317 0.0340  0.0196  121 GLN A CB  
932  C CG  . GLN A 119 ? 0.4935 0.6361 0.8427 -0.0273 0.0372  0.0305  121 GLN A CG  
933  C CD  . GLN A 119 ? 0.5658 0.7079 0.8920 -0.0209 0.0376  0.0345  121 GLN A CD  
934  O OE1 . GLN A 119 ? 0.5542 0.6976 0.8733 -0.0194 0.0330  0.0314  121 GLN A OE1 
935  N NE2 . GLN A 119 ? 0.6312 0.7707 0.9447 -0.0170 0.0426  0.0409  121 GLN A NE2 
936  N N   . ARG A 120 ? 0.4837 0.5996 0.8171 -0.0469 0.0276  -0.0105 122 ARG A N   
937  C CA  . ARG A 120 ? 0.4950 0.6007 0.8150 -0.0506 0.0291  -0.0203 122 ARG A CA  
938  C C   . ARG A 120 ? 0.4849 0.5887 0.8269 -0.0532 0.0355  -0.0199 122 ARG A C   
939  O O   . ARG A 120 ? 0.4926 0.5911 0.8290 -0.0524 0.0403  -0.0177 122 ARG A O   
940  C CB  . ARG A 120 ? 0.5132 0.6154 0.8248 -0.0556 0.0232  -0.0337 122 ARG A CB  
941  C CG  . ARG A 120 ? 0.5723 0.6638 0.8696 -0.0592 0.0267  -0.0439 122 ARG A CG  
942  C CD  . ARG A 120 ? 0.6436 0.7315 0.9264 -0.0636 0.0206  -0.0564 122 ARG A CD  
943  N NE  . ARG A 120 ? 0.6773 0.7634 0.9302 -0.0612 0.0155  -0.0553 122 ARG A NE  
944  C CZ  . ARG A 120 ? 0.7084 0.7918 0.9433 -0.0643 0.0087  -0.0641 122 ARG A CZ  
945  N NH1 . ARG A 120 ? 0.7246 0.8065 0.9340 -0.0617 0.0042  -0.0610 122 ARG A NH1 
946  N NH2 . ARG A 120 ? 0.6952 0.7768 0.9372 -0.0701 0.0059  -0.0759 122 ARG A NH2 
947  N N   . ARG A 121 ? 0.4593 0.5679 0.8292 -0.0563 0.0352  -0.0211 123 ARG A N   
948  C CA  . ARG A 121 ? 0.4465 0.5534 0.8417 -0.0591 0.0408  -0.0210 123 ARG A CA  
949  C C   . ARG A 121 ? 0.4147 0.5254 0.8186 -0.0548 0.0459  -0.0056 123 ARG A C   
950  O O   . ARG A 121 ? 0.4164 0.5224 0.8261 -0.0556 0.0504  -0.0044 123 ARG A O   
951  C CB  . ARG A 121 ? 0.4762 0.5871 0.9003 -0.0636 0.0386  -0.0264 123 ARG A CB  
952  C CG  . ARG A 121 ? 0.5472 0.6515 0.9633 -0.0693 0.0340  -0.0445 123 ARG A CG  
953  C CD  . ARG A 121 ? 0.6119 0.7174 1.0602 -0.0748 0.0327  -0.0524 123 ARG A CD  
954  N NE  . ARG A 121 ? 0.6597 0.7653 1.1366 -0.0748 0.0405  -0.0453 123 ARG A NE  
955  C CZ  . ARG A 121 ? 0.6998 0.8131 1.2095 -0.0743 0.0421  -0.0349 123 ARG A CZ  
956  N NH1 . ARG A 121 ? 0.6765 0.7891 1.2093 -0.0742 0.0490  -0.0277 123 ARG A NH1 
957  N NH2 . ARG A 121 ? 0.6968 0.8189 1.2184 -0.0740 0.0367  -0.0309 123 ARG A NH2 
958  N N   . SER A 122 ? 0.3887 0.5076 0.7926 -0.0502 0.0451  0.0060  124 SER A N   
959  C CA  . SER A 122 ? 0.3728 0.4954 0.7805 -0.0458 0.0494  0.0207  124 SER A CA  
960  C C   . SER A 122 ? 0.3479 0.4653 0.7271 -0.0419 0.0499  0.0243  124 SER A C   
961  O O   . SER A 122 ? 0.3563 0.4720 0.7405 -0.0413 0.0529  0.0311  124 SER A O   
962  C CB  . SER A 122 ? 0.4111 0.5440 0.8277 -0.0421 0.0498  0.0313  124 SER A CB  
963  O OG  . SER A 122 ? 0.4890 0.6231 0.8842 -0.0394 0.0456  0.0280  124 SER A OG  
964  N N   . ASP A 123 ? 0.3124 0.4271 0.6636 -0.0394 0.0464  0.0202  125 ASP A N   
965  C CA  . ASP A 123 ? 0.2890 0.4000 0.6157 -0.0350 0.0464  0.0248  125 ASP A CA  
966  C C   . ASP A 123 ? 0.2553 0.3568 0.5597 -0.0363 0.0445  0.0158  125 ASP A C   
967  O O   . ASP A 123 ? 0.2529 0.3506 0.5421 -0.0335 0.0445  0.0196  125 ASP A O   
968  C CB  . ASP A 123 ? 0.3400 0.4564 0.6535 -0.0293 0.0453  0.0313  125 ASP A CB  
969  C CG  . ASP A 123 ? 0.4120 0.5381 0.7434 -0.0267 0.0487  0.0423  125 ASP A CG  
970  O OD1 . ASP A 123 ? 0.4326 0.5601 0.7741 -0.0264 0.0521  0.0508  125 ASP A OD1 
971  O OD2 . ASP A 123 ? 0.4310 0.5635 0.7669 -0.0250 0.0480  0.0432  125 ASP A OD2 
972  N N   . LEU A 124 ? 0.2441 0.3416 0.5458 -0.0404 0.0429  0.0044  126 LEU A N   
973  C CA  . LEU A 124 ? 0.2331 0.3218 0.5120 -0.0414 0.0419  -0.0031 126 LEU A CA  
974  C C   . LEU A 124 ? 0.2103 0.2927 0.4905 -0.0423 0.0459  -0.0020 126 LEU A C   
975  O O   . LEU A 124 ? 0.2127 0.2910 0.4758 -0.0397 0.0451  0.0005  126 LEU A O   
976  C CB  . LEU A 124 ? 0.2374 0.3231 0.5144 -0.0462 0.0403  -0.0153 126 LEU A CB  
977  C CG  . LEU A 124 ? 0.2766 0.3536 0.5283 -0.0475 0.0399  -0.0231 126 LEU A CG  
978  C CD1 . LEU A 124 ? 0.2740 0.3512 0.5028 -0.0430 0.0353  -0.0188 126 LEU A CD1 
979  C CD2 . LEU A 124 ? 0.2931 0.3673 0.5422 -0.0527 0.0384  -0.0355 126 LEU A CD2 
980  N N   . ASN A 125 ? 0.1919 0.2734 0.4945 -0.0459 0.0499  -0.0037 127 ASN A N   
981  C CA  . ASN A 125 ? 0.1877 0.2633 0.4951 -0.0471 0.0536  -0.0031 127 ASN A CA  
982  C C   . ASN A 125 ? 0.1772 0.2550 0.4839 -0.0430 0.0522  0.0093  127 ASN A C   
983  O O   . ASN A 125 ? 0.1747 0.2474 0.4712 -0.0421 0.0518  0.0107  127 ASN A O   
984  C CB  . ASN A 125 ? 0.2222 0.2965 0.5562 -0.0516 0.0584  -0.0079 127 ASN A CB  
985  C CG  . ASN A 125 ? 0.3110 0.3809 0.6407 -0.0560 0.0600  -0.0224 127 ASN A CG  
986  O OD1 . ASN A 125 ? 0.3690 0.4332 0.6758 -0.0565 0.0600  -0.0291 127 ASN A OD1 
987  N ND2 . ASN A 125 ? 0.3172 0.3891 0.6676 -0.0593 0.0612  -0.0277 127 ASN A ND2 
988  N N   . ARG A 126 ? 0.1827 0.2682 0.5001 -0.0407 0.0512  0.0185  128 ARG A N   
989  C CA  . ARG A 126 ? 0.1645 0.2527 0.4779 -0.0366 0.0495  0.0307  128 ARG A CA  
990  C C   . ARG A 126 ? 0.1705 0.2557 0.4538 -0.0324 0.0458  0.0308  128 ARG A C   
991  O O   . ARG A 126 ? 0.1598 0.2408 0.4342 -0.0311 0.0439  0.0339  128 ARG A O   
992  C CB  . ARG A 126 ? 0.1381 0.2357 0.4659 -0.0347 0.0504  0.0403  128 ARG A CB  
993  C CG  . ARG A 126 ? 0.1715 0.2726 0.4909 -0.0301 0.0490  0.0530  128 ARG A CG  
994  C CD  . ARG A 126 ? 0.2441 0.3409 0.5660 -0.0307 0.0473  0.0582  128 ARG A CD  
995  N NE  . ARG A 126 ? 0.2879 0.3859 0.6405 -0.0346 0.0500  0.0608  128 ARG A NE  
996  C CZ  . ARG A 126 ? 0.2456 0.3400 0.6101 -0.0365 0.0492  0.0637  128 ARG A CZ  
997  N NH1 . ARG A 126 ? 0.2388 0.3281 0.5870 -0.0352 0.0452  0.0643  128 ARG A NH1 
998  N NH2 . ARG A 126 ? 0.2210 0.3169 0.6164 -0.0397 0.0522  0.0661  128 ARG A NH2 
999  N N   . PHE A 127 ? 0.1780 0.2654 0.4484 -0.0304 0.0445  0.0276  129 PHE A N   
1000 C CA  . PHE A 127 ? 0.2085 0.2933 0.4534 -0.0261 0.0414  0.0278  129 PHE A CA  
1001 C C   . PHE A 127 ? 0.1978 0.2734 0.4289 -0.0277 0.0401  0.0213  129 PHE A C   
1002 O O   . PHE A 127 ? 0.1949 0.2665 0.4106 -0.0247 0.0376  0.0234  129 PHE A O   
1003 C CB  . PHE A 127 ? 0.2266 0.3157 0.4641 -0.0239 0.0402  0.0256  129 PHE A CB  
1004 C CG  . PHE A 127 ? 0.2555 0.3534 0.4994 -0.0200 0.0416  0.0339  129 PHE A CG  
1005 C CD1 . PHE A 127 ? 0.2749 0.3781 0.5373 -0.0206 0.0446  0.0418  129 PHE A CD1 
1006 C CD2 . PHE A 127 ? 0.2883 0.3894 0.5215 -0.0158 0.0407  0.0344  129 PHE A CD2 
1007 C CE1 . PHE A 127 ? 0.2730 0.3847 0.5414 -0.0170 0.0472  0.0503  129 PHE A CE1 
1008 C CE2 . PHE A 127 ? 0.2988 0.4084 0.5394 -0.0122 0.0435  0.0420  129 PHE A CE2 
1009 C CZ  . PHE A 127 ? 0.2816 0.3964 0.5390 -0.0128 0.0471  0.0501  129 PHE A CZ  
1010 N N   . TRP A 128 ? 0.1896 0.2617 0.4268 -0.0323 0.0423  0.0132  130 TRP A N   
1011 C CA  . TRP A 128 ? 0.1985 0.2621 0.4240 -0.0340 0.0427  0.0074  130 TRP A CA  
1012 C C   . TRP A 128 ? 0.2026 0.2621 0.4358 -0.0348 0.0436  0.0113  130 TRP A C   
1013 O O   . TRP A 128 ? 0.2050 0.2589 0.4252 -0.0335 0.0416  0.0116  130 TRP A O   
1014 C CB  . TRP A 128 ? 0.1713 0.2323 0.4000 -0.0388 0.0459  -0.0024 130 TRP A CB  
1015 C CG  . TRP A 128 ? 0.1524 0.2048 0.3685 -0.0407 0.0481  -0.0079 130 TRP A CG  
1016 C CD1 . TRP A 128 ? 0.1536 0.2009 0.3784 -0.0449 0.0538  -0.0137 130 TRP A CD1 
1017 C CD2 . TRP A 128 ? 0.1554 0.2031 0.3493 -0.0384 0.0454  -0.0079 130 TRP A CD2 
1018 N NE1 . TRP A 128 ? 0.1700 0.2103 0.3785 -0.0455 0.0554  -0.0170 130 TRP A NE1 
1019 C CE2 . TRP A 128 ? 0.1682 0.2085 0.3578 -0.0417 0.0499  -0.0132 130 TRP A CE2 
1020 C CE3 . TRP A 128 ? 0.1519 0.2010 0.3303 -0.0339 0.0403  -0.0040 130 TRP A CE3 
1021 C CZ2 . TRP A 128 ? 0.1690 0.2034 0.3400 -0.0406 0.0491  -0.0134 130 TRP A CZ2 
1022 C CZ3 . TRP A 128 ? 0.1676 0.2103 0.3285 -0.0328 0.0390  -0.0049 130 TRP A CZ3 
1023 C CH2 . TRP A 128 ? 0.1755 0.2113 0.3328 -0.0363 0.0431  -0.0091 130 TRP A CH2 
1024 N N   . LEU A 129 ? 0.1796 0.2418 0.4358 -0.0370 0.0461  0.0145  131 LEU A N   
1025 C CA  . LEU A 129 ? 0.1815 0.2411 0.4482 -0.0375 0.0456  0.0199  131 LEU A CA  
1026 C C   . LEU A 129 ? 0.1858 0.2461 0.4382 -0.0330 0.0395  0.0279  131 LEU A C   
1027 O O   . LEU A 129 ? 0.1783 0.2332 0.4248 -0.0327 0.0368  0.0286  131 LEU A O   
1028 C CB  . LEU A 129 ? 0.1851 0.2490 0.4801 -0.0397 0.0482  0.0242  131 LEU A CB  
1029 C CG  . LEU A 129 ? 0.2049 0.2672 0.5142 -0.0402 0.0463  0.0318  131 LEU A CG  
1030 C CD1 . LEU A 129 ? 0.2084 0.2633 0.5196 -0.0426 0.0486  0.0262  131 LEU A CD1 
1031 C CD2 . LEU A 129 ? 0.2208 0.2876 0.5589 -0.0421 0.0488  0.0369  131 LEU A CD2 
1032 N N   . GLU A 130 ? 0.1831 0.2499 0.4303 -0.0295 0.0377  0.0335  132 GLU A N   
1033 C CA  . GLU A 130 ? 0.1918 0.2587 0.4233 -0.0251 0.0329  0.0401  132 GLU A CA  
1034 C C   . GLU A 130 ? 0.2068 0.2668 0.4155 -0.0231 0.0299  0.0346  132 GLU A C   
1035 O O   . GLU A 130 ? 0.1978 0.2535 0.3975 -0.0216 0.0253  0.0371  132 GLU A O   
1036 C CB  . GLU A 130 ? 0.2073 0.2820 0.4359 -0.0214 0.0334  0.0467  132 GLU A CB  
1037 C CG  . GLU A 130 ? 0.2479 0.3297 0.5003 -0.0232 0.0363  0.0537  132 GLU A CG  
1038 C CD  . GLU A 130 ? 0.2674 0.3485 0.5324 -0.0246 0.0338  0.0614  132 GLU A CD  
1039 O OE1 . GLU A 130 ? 0.2431 0.3198 0.4946 -0.0231 0.0285  0.0638  132 GLU A OE1 
1040 O OE2 . GLU A 130 ? 0.2960 0.3807 0.5859 -0.0275 0.0366  0.0651  132 GLU A OE2 
1041 N N   . THR A 131 ? 0.2212 0.2799 0.4218 -0.0233 0.0319  0.0276  133 THR A N   
1042 C CA  . THR A 131 ? 0.2288 0.2807 0.4107 -0.0219 0.0297  0.0229  133 THR A CA  
1043 C C   . THR A 131 ? 0.2215 0.2656 0.4070 -0.0249 0.0293  0.0209  133 THR A C   
1044 O O   . THR A 131 ? 0.2039 0.2427 0.3790 -0.0231 0.0251  0.0216  133 THR A O   
1045 C CB  . THR A 131 ? 0.2482 0.3007 0.4241 -0.0224 0.0318  0.0169  133 THR A CB  
1046 O OG1 . THR A 131 ? 0.2360 0.2960 0.4118 -0.0195 0.0319  0.0194  133 THR A OG1 
1047 C CG2 . THR A 131 ? 0.2698 0.3157 0.4283 -0.0209 0.0297  0.0135  133 THR A CG2 
1048 N N   . LEU A 132 ? 0.2298 0.2733 0.4316 -0.0295 0.0339  0.0181  134 LEU A N   
1049 C CA  . LEU A 132 ? 0.2274 0.2644 0.4372 -0.0326 0.0353  0.0165  134 LEU A CA  
1050 C C   . LEU A 132 ? 0.2085 0.2443 0.4245 -0.0317 0.0297  0.0231  134 LEU A C   
1051 O O   . LEU A 132 ? 0.2147 0.2444 0.4273 -0.0320 0.0271  0.0227  134 LEU A O   
1052 C CB  . LEU A 132 ? 0.2247 0.2623 0.4538 -0.0372 0.0422  0.0127  134 LEU A CB  
1053 C CG  . LEU A 132 ? 0.2328 0.2701 0.4554 -0.0391 0.0474  0.0047  134 LEU A CG  
1054 C CD1 . LEU A 132 ? 0.2314 0.2684 0.4737 -0.0436 0.0545  0.0000  134 LEU A CD1 
1055 C CD2 . LEU A 132 ? 0.2546 0.2857 0.4574 -0.0388 0.0477  0.0007  134 LEU A CD2 
1056 N N   . LEU A 133 ? 0.1920 0.2337 0.4166 -0.0307 0.0274  0.0296  135 LEU A N   
1057 C CA  . LEU A 133 ? 0.2296 0.2705 0.4585 -0.0300 0.0207  0.0366  135 LEU A CA  
1058 C C   . LEU A 133 ? 0.2440 0.2816 0.4502 -0.0261 0.0138  0.0372  135 LEU A C   
1059 O O   . LEU A 133 ? 0.2650 0.2982 0.4715 -0.0265 0.0075  0.0393  135 LEU A O   
1060 C CB  . LEU A 133 ? 0.2217 0.2700 0.4650 -0.0300 0.0199  0.0448  135 LEU A CB  
1061 C CG  . LEU A 133 ? 0.2143 0.2658 0.4835 -0.0337 0.0266  0.0444  135 LEU A CG  
1062 C CD1 . LEU A 133 ? 0.2250 0.2838 0.5079 -0.0331 0.0252  0.0542  135 LEU A CD1 
1063 C CD2 . LEU A 133 ? 0.2191 0.2656 0.5074 -0.0376 0.0289  0.0418  135 LEU A CD2 
1064 N N   . CYS A 134 ? 0.2402 0.2793 0.4281 -0.0225 0.0146  0.0349  136 CYS A N   
1065 C CA  . CYS A 134 ? 0.2473 0.2824 0.4133 -0.0184 0.0093  0.0339  136 CYS A CA  
1066 C C   . CYS A 134 ? 0.2556 0.2818 0.4175 -0.0197 0.0076  0.0285  136 CYS A C   
1067 O O   . CYS A 134 ? 0.2748 0.2955 0.4271 -0.0181 0.0010  0.0283  136 CYS A O   
1068 C CB  . CYS A 134 ? 0.2390 0.2781 0.3907 -0.0143 0.0123  0.0323  136 CYS A CB  
1069 S SG  . CYS A 134 ? 0.2934 0.3420 0.4440 -0.0110 0.0134  0.0400  136 CYS A SG  
1070 N N   . LEU A 135 ? 0.2387 0.2632 0.4073 -0.0226 0.0134  0.0242  137 LEU A N   
1071 C CA  . LEU A 135 ? 0.2486 0.2650 0.4146 -0.0241 0.0134  0.0204  137 LEU A CA  
1072 C C   . LEU A 135 ? 0.2673 0.2798 0.4498 -0.0274 0.0107  0.0226  137 LEU A C   
1073 O O   . LEU A 135 ? 0.2792 0.2859 0.4577 -0.0267 0.0043  0.0228  137 LEU A O   
1074 C CB  . LEU A 135 ? 0.2315 0.2474 0.3977 -0.0263 0.0210  0.0158  137 LEU A CB  
1075 C CG  . LEU A 135 ? 0.2427 0.2578 0.3909 -0.0235 0.0216  0.0127  137 LEU A CG  
1076 C CD1 . LEU A 135 ? 0.2557 0.2767 0.3943 -0.0189 0.0190  0.0144  137 LEU A CD1 
1077 C CD2 . LEU A 135 ? 0.2390 0.2548 0.3884 -0.0265 0.0284  0.0089  137 LEU A CD2 
1078 N N   . ILE A 136 ? 0.2835 0.2990 0.4864 -0.0311 0.0154  0.0240  138 ILE A N   
1079 C CA  . ILE A 136 ? 0.2848 0.2969 0.5076 -0.0345 0.0141  0.0262  138 ILE A CA  
1080 C C   . ILE A 136 ? 0.2880 0.3005 0.5130 -0.0333 0.0033  0.0320  138 ILE A C   
1081 O O   . ILE A 136 ? 0.2911 0.2989 0.5259 -0.0351 -0.0015 0.0332  138 ILE A O   
1082 C CB  . ILE A 136 ? 0.2705 0.2853 0.5172 -0.0385 0.0227  0.0259  138 ILE A CB  
1083 C CG1 . ILE A 136 ? 0.2773 0.2998 0.5347 -0.0383 0.0222  0.0304  138 ILE A CG1 
1084 C CG2 . ILE A 136 ? 0.2768 0.2899 0.5169 -0.0398 0.0327  0.0191  138 ILE A CG2 
1085 C CD1 . ILE A 136 ? 0.2547 0.2793 0.5370 -0.0416 0.0286  0.0307  138 ILE A CD1 
1086 N N   . GLY A 137 ? 0.2895 0.3075 0.5053 -0.0305 -0.0004 0.0357  139 GLY A N   
1087 C CA  . GLY A 137 ? 0.3071 0.3257 0.5208 -0.0294 -0.0109 0.0415  139 GLY A CA  
1088 C C   . GLY A 137 ? 0.3182 0.3311 0.5088 -0.0261 -0.0190 0.0388  139 GLY A C   
1089 O O   . GLY A 137 ? 0.3372 0.3493 0.5232 -0.0254 -0.0288 0.0424  139 GLY A O   
1090 N N   . GLU A 138 ? 0.3033 0.3120 0.4790 -0.0241 -0.0156 0.0324  140 GLU A N   
1091 C CA  . GLU A 138 ? 0.2903 0.2928 0.4450 -0.0207 -0.0220 0.0286  140 GLU A CA  
1092 C C   . GLU A 138 ? 0.2826 0.2887 0.4182 -0.0163 -0.0260 0.0307  140 GLU A C   
1093 O O   . GLU A 138 ? 0.2640 0.2663 0.3891 -0.0150 -0.0353 0.0308  140 GLU A O   
1094 C CB  . GLU A 138 ? 0.2958 0.2905 0.4578 -0.0230 -0.0307 0.0277  140 GLU A CB  
1095 C CG  . GLU A 138 ? 0.3495 0.3406 0.5315 -0.0271 -0.0257 0.0265  140 GLU A CG  
1096 C CD  . GLU A 138 ? 0.3751 0.3610 0.5485 -0.0262 -0.0197 0.0212  140 GLU A CD  
1097 O OE1 . GLU A 138 ? 0.4146 0.3951 0.5718 -0.0231 -0.0245 0.0176  140 GLU A OE1 
1098 O OE2 . GLU A 138 ? 0.3469 0.3338 0.5298 -0.0286 -0.0104 0.0207  140 GLU A OE2 
1099 N N   . SER A 139 ? 0.2838 0.2969 0.4147 -0.0141 -0.0188 0.0321  141 SER A N   
1100 C CA  . SER A 139 ? 0.3053 0.3238 0.4226 -0.0104 -0.0197 0.0360  141 SER A CA  
1101 C C   . SER A 139 ? 0.3275 0.3425 0.4194 -0.0049 -0.0210 0.0313  141 SER A C   
1102 O O   . SER A 139 ? 0.3356 0.3547 0.4139 -0.0014 -0.0208 0.0345  141 SER A O   
1103 C CB  . SER A 139 ? 0.3312 0.3591 0.4583 -0.0106 -0.0109 0.0399  141 SER A CB  
1104 O OG  . SER A 139 ? 0.3288 0.3593 0.4803 -0.0155 -0.0095 0.0435  141 SER A OG  
1105 N N   . PHE A 140 ? 0.3352 0.3424 0.4209 -0.0040 -0.0218 0.0242  142 PHE A N   
1106 C CA  . PHE A 140 ? 0.3601 0.3633 0.4244 0.0014  -0.0220 0.0189  142 PHE A CA  
1107 C C   . PHE A 140 ? 0.3999 0.3932 0.4539 0.0019  -0.0319 0.0143  142 PHE A C   
1108 O O   . PHE A 140 ? 0.3934 0.3804 0.4337 0.0056  -0.0323 0.0078  142 PHE A O   
1109 C CB  . PHE A 140 ? 0.3506 0.3531 0.4160 0.0028  -0.0151 0.0148  142 PHE A CB  
1110 C CG  . PHE A 140 ? 0.3198 0.3318 0.3967 0.0015  -0.0070 0.0187  142 PHE A CG  
1111 C CD1 . PHE A 140 ? 0.3083 0.3287 0.3817 0.0042  -0.0026 0.0226  142 PHE A CD1 
1112 C CD2 . PHE A 140 ? 0.3245 0.3366 0.4164 -0.0029 -0.0038 0.0184  142 PHE A CD2 
1113 C CE1 . PHE A 140 ? 0.3138 0.3425 0.3999 0.0026  0.0039  0.0257  142 PHE A CE1 
1114 C CE2 . PHE A 140 ? 0.3113 0.3314 0.4136 -0.0045 0.0028  0.0207  142 PHE A CE2 
1115 C CZ  . PHE A 140 ? 0.3117 0.3399 0.4119 -0.0019 0.0060  0.0241  142 PHE A CZ  
1116 N N   . ASP A 141 ? 0.4373 0.4288 0.4994 -0.0020 -0.0406 0.0174  143 ASP A N   
1117 C CA  . ASP A 141 ? 0.4838 0.4663 0.5371 -0.0022 -0.0519 0.0132  143 ASP A CA  
1118 C C   . ASP A 141 ? 0.4824 0.4553 0.5396 -0.0026 -0.0525 0.0058  143 ASP A C   
1119 O O   . ASP A 141 ? 0.4806 0.4548 0.5551 -0.0054 -0.0467 0.0072  143 ASP A O   
1120 C CB  . ASP A 141 ? 0.5772 0.5594 0.6032 0.0026  -0.0554 0.0118  143 ASP A CB  
1121 C CG  . ASP A 141 ? 0.7145 0.7057 0.7399 0.0018  -0.0563 0.0215  143 ASP A CG  
1122 O OD1 . ASP A 141 ? 0.7104 0.7028 0.7511 -0.0029 -0.0639 0.0271  143 ASP A OD1 
1123 O OD2 . ASP A 141 ? 0.7856 0.7831 0.7973 0.0060  -0.0491 0.0242  143 ASP A OD2 
1124 N N   . ASP A 142 ? 0.4918 0.4554 0.5343 0.0002  -0.0584 -0.0018 144 ASP A N   
1125 C CA  . ASP A 142 ? 0.5042 0.4589 0.5552 -0.0008 -0.0590 -0.0073 144 ASP A CA  
1126 C C   . ASP A 142 ? 0.4747 0.4321 0.5283 0.0013  -0.0475 -0.0074 144 ASP A C   
1127 O O   . ASP A 142 ? 0.4565 0.4097 0.5230 -0.0010 -0.0456 -0.0078 144 ASP A O   
1128 C CB  . ASP A 142 ? 0.5767 0.5202 0.6133 0.0018  -0.0677 -0.0161 144 ASP A CB  
1129 C CG  . ASP A 142 ? 0.7018 0.6400 0.7419 -0.0020 -0.0816 -0.0169 144 ASP A CG  
1130 O OD1 . ASP A 142 ? 0.7082 0.6502 0.7686 -0.0072 -0.0843 -0.0104 144 ASP A OD1 
1131 O OD2 . ASP A 142 ? 0.7842 0.7144 0.8077 0.0002  -0.0900 -0.0245 144 ASP A OD2 
1132 N N   . TYR A 143 ? 0.4559 0.4207 0.4980 0.0054  -0.0400 -0.0060 145 TYR A N   
1133 C CA  . TYR A 143 ? 0.4207 0.3888 0.4648 0.0076  -0.0307 -0.0058 145 TYR A CA  
1134 C C   . TYR A 143 ? 0.3652 0.3398 0.4269 0.0030  -0.0248 -0.0002 145 TYR A C   
1135 O O   . TYR A 143 ? 0.3502 0.3270 0.4140 0.0038  -0.0184 0.0000  145 TYR A O   
1136 C CB  . TYR A 143 ? 0.4324 0.4061 0.4612 0.0133  -0.0253 -0.0062 145 TYR A CB  
1137 C CG  . TYR A 143 ? 0.4625 0.4290 0.4721 0.0184  -0.0290 -0.0131 145 TYR A CG  
1138 C CD1 . TYR A 143 ? 0.4929 0.4491 0.5003 0.0205  -0.0314 -0.0201 145 TYR A CD1 
1139 C CD2 . TYR A 143 ? 0.4862 0.4560 0.4797 0.0213  -0.0295 -0.0127 145 TYR A CD2 
1140 C CE1 . TYR A 143 ? 0.5208 0.4698 0.5110 0.0255  -0.0338 -0.0279 145 TYR A CE1 
1141 C CE2 . TYR A 143 ? 0.5089 0.4716 0.4824 0.0263  -0.0318 -0.0201 145 TYR A CE2 
1142 C CZ  . TYR A 143 ? 0.5495 0.5015 0.5216 0.0284  -0.0339 -0.0284 145 TYR A CZ  
1143 O OH  . TYR A 143 ? 0.6133 0.5572 0.5663 0.0334  -0.0357 -0.0374 145 TYR A OH  
1144 N N   . SER A 144 ? 0.3543 0.3317 0.4288 -0.0018 -0.0270 0.0040  146 SER A N   
1145 C CA  . SER A 144 ? 0.3391 0.3206 0.4312 -0.0065 -0.0213 0.0077  146 SER A CA  
1146 C C   . SER A 144 ? 0.3317 0.3063 0.4316 -0.0086 -0.0196 0.0057  146 SER A C   
1147 O O   . SER A 144 ? 0.3458 0.3233 0.4536 -0.0111 -0.0127 0.0074  146 SER A O   
1148 C CB  . SER A 144 ? 0.3552 0.3397 0.4620 -0.0109 -0.0246 0.0123  146 SER A CB  
1149 O OG  . SER A 144 ? 0.3939 0.3875 0.5006 -0.0103 -0.0221 0.0168  146 SER A OG  
1150 N N   . ASP A 145 ? 0.3190 0.2842 0.4162 -0.0079 -0.0257 0.0022  147 ASP A N   
1151 C CA  . ASP A 145 ? 0.3162 0.2744 0.4201 -0.0093 -0.0240 0.0012  147 ASP A CA  
1152 C C   . ASP A 145 ? 0.3086 0.2675 0.4034 -0.0060 -0.0178 0.0005  147 ASP A C   
1153 O O   . ASP A 145 ? 0.3192 0.2751 0.4202 -0.0080 -0.0138 0.0021  147 ASP A O   
1154 C CB  . ASP A 145 ? 0.3576 0.3052 0.4619 -0.0089 -0.0328 -0.0027 147 ASP A CB  
1155 C CG  . ASP A 145 ? 0.4468 0.3922 0.5657 -0.0134 -0.0400 -0.0014 147 ASP A CG  
1156 O OD1 . ASP A 145 ? 0.4229 0.3740 0.5560 -0.0174 -0.0364 0.0034  147 ASP A OD1 
1157 O OD2 . ASP A 145 ? 0.4858 0.4235 0.6029 -0.0130 -0.0498 -0.0054 147 ASP A OD2 
1158 N N   . ASP A 146 ? 0.2779 0.2406 0.3592 -0.0011 -0.0170 -0.0013 148 ASP A N   
1159 C CA  . ASP A 146 ? 0.2728 0.2386 0.3481 0.0018  -0.0114 -0.0009 148 ASP A CA  
1160 C C   . ASP A 146 ? 0.2445 0.2191 0.3244 -0.0008 -0.0048 0.0028  148 ASP A C   
1161 O O   . ASP A 146 ? 0.2426 0.2188 0.3194 0.0005  -0.0014 0.0036  148 ASP A O   
1162 C CB  . ASP A 146 ? 0.2816 0.2500 0.3438 0.0080  -0.0117 -0.0035 148 ASP A CB  
1163 C CG  . ASP A 146 ? 0.3402 0.2984 0.3964 0.0118  -0.0160 -0.0086 148 ASP A CG  
1164 O OD1 . ASP A 146 ? 0.3772 0.3280 0.4350 0.0102  -0.0221 -0.0113 148 ASP A OD1 
1165 O OD2 . ASP A 146 ? 0.2677 0.2253 0.3193 0.0163  -0.0134 -0.0097 148 ASP A OD2 
1166 N N   . VAL A 147 ? 0.2356 0.2154 0.3230 -0.0043 -0.0035 0.0048  149 VAL A N   
1167 C CA  . VAL A 147 ? 0.2447 0.2321 0.3378 -0.0073 0.0026  0.0070  149 VAL A CA  
1168 C C   . VAL A 147 ? 0.2689 0.2523 0.3687 -0.0115 0.0064  0.0077  149 VAL A C   
1169 O O   . VAL A 147 ? 0.2681 0.2458 0.3768 -0.0145 0.0052  0.0082  149 VAL A O   
1170 C CB  . VAL A 147 ? 0.2475 0.2411 0.3488 -0.0094 0.0028  0.0090  149 VAL A CB  
1171 C CG1 . VAL A 147 ? 0.2518 0.2520 0.3613 -0.0129 0.0093  0.0101  149 VAL A CG1 
1172 C CG2 . VAL A 147 ? 0.2573 0.2552 0.3500 -0.0051 0.0001  0.0095  149 VAL A CG2 
1173 N N   . CYS A 148 ? 0.2641 0.2507 0.3595 -0.0119 0.0109  0.0080  150 CYS A N   
1174 C CA  . CYS A 148 ? 0.2717 0.2556 0.3694 -0.0158 0.0158  0.0089  150 CYS A CA  
1175 C C   . CYS A 148 ? 0.2611 0.2507 0.3662 -0.0201 0.0216  0.0082  150 CYS A C   
1176 O O   . CYS A 148 ? 0.2718 0.2584 0.3847 -0.0242 0.0262  0.0083  150 CYS A O   
1177 C CB  . CYS A 148 ? 0.2582 0.2413 0.3447 -0.0137 0.0161  0.0097  150 CYS A CB  
1178 S SG  . CYS A 148 ? 0.2969 0.2714 0.3785 -0.0090 0.0106  0.0105  150 CYS A SG  
1179 N N   . GLY A 149 ? 0.2353 0.2328 0.3393 -0.0190 0.0217  0.0073  151 GLY A N   
1180 C CA  . GLY A 149 ? 0.2349 0.2380 0.3462 -0.0227 0.0268  0.0058  151 GLY A CA  
1181 C C   . GLY A 149 ? 0.2285 0.2401 0.3380 -0.0207 0.0259  0.0053  151 GLY A C   
1182 O O   . GLY A 149 ? 0.2208 0.2346 0.3247 -0.0163 0.0219  0.0067  151 GLY A O   
1183 N N   . ALA A 150 ? 0.2354 0.2514 0.3507 -0.0242 0.0301  0.0029  152 ALA A N   
1184 C CA  . ALA A 150 ? 0.2483 0.2726 0.3663 -0.0235 0.0298  0.0022  152 ALA A CA  
1185 C C   . ALA A 150 ? 0.2529 0.2785 0.3680 -0.0272 0.0328  -0.0021 152 ALA A C   
1186 O O   . ALA A 150 ? 0.2465 0.2677 0.3628 -0.0311 0.0376  -0.0050 152 ALA A O   
1187 C CB  . ALA A 150 ? 0.2540 0.2830 0.3874 -0.0244 0.0309  0.0038  152 ALA A CB  
1188 N N   . VAL A 151 ? 0.2505 0.2820 0.3619 -0.0258 0.0300  -0.0028 153 VAL A N   
1189 C CA  . VAL A 151 ? 0.2598 0.2928 0.3665 -0.0292 0.0307  -0.0074 153 VAL A CA  
1190 C C   . VAL A 151 ? 0.2507 0.2923 0.3696 -0.0299 0.0299  -0.0090 153 VAL A C   
1191 O O   . VAL A 151 ? 0.2312 0.2787 0.3556 -0.0262 0.0270  -0.0051 153 VAL A O   
1192 C CB  . VAL A 151 ? 0.2869 0.3183 0.3770 -0.0273 0.0262  -0.0061 153 VAL A CB  
1193 C CG1 . VAL A 151 ? 0.3016 0.3340 0.3838 -0.0313 0.0257  -0.0109 153 VAL A CG1 
1194 C CG2 . VAL A 151 ? 0.3204 0.3433 0.4009 -0.0263 0.0270  -0.0034 153 VAL A CG2 
1195 N N   . VAL A 152 ? 0.2631 0.3050 0.3867 -0.0348 0.0329  -0.0150 154 VAL A N   
1196 C CA  . VAL A 152 ? 0.2744 0.3236 0.4093 -0.0364 0.0314  -0.0178 154 VAL A CA  
1197 C C   . VAL A 152 ? 0.2708 0.3193 0.3932 -0.0394 0.0284  -0.0237 154 VAL A C   
1198 O O   . VAL A 152 ? 0.2584 0.3010 0.3719 -0.0432 0.0320  -0.0292 154 VAL A O   
1199 C CB  . VAL A 152 ? 0.2981 0.3491 0.4539 -0.0393 0.0364  -0.0198 154 VAL A CB  
1200 C CG1 . VAL A 152 ? 0.3328 0.3767 0.4885 -0.0438 0.0430  -0.0258 154 VAL A CG1 
1201 C CG2 . VAL A 152 ? 0.3001 0.3585 0.4691 -0.0410 0.0343  -0.0225 154 VAL A CG2 
1202 N N   . ASN A 153 ? 0.3036 0.3583 0.4252 -0.0377 0.0218  -0.0223 155 ASN A N   
1203 C CA  . ASN A 153 ? 0.3346 0.3904 0.4468 -0.0407 0.0164  -0.0275 155 ASN A CA  
1204 C C   . ASN A 153 ? 0.3570 0.4193 0.4878 -0.0438 0.0152  -0.0324 155 ASN A C   
1205 O O   . ASN A 153 ? 0.3428 0.4131 0.4896 -0.0411 0.0126  -0.0279 155 ASN A O   
1206 C CB  . ASN A 153 ? 0.3204 0.3794 0.4233 -0.0367 0.0084  -0.0219 155 ASN A CB  
1207 C CG  . ASN A 153 ? 0.3426 0.3962 0.4334 -0.0324 0.0093  -0.0156 155 ASN A CG  
1208 O OD1 . ASN A 153 ? 0.3209 0.3764 0.4179 -0.0273 0.0095  -0.0097 155 ASN A OD1 
1209 N ND2 . ASN A 153 ? 0.3692 0.4155 0.4426 -0.0346 0.0104  -0.0171 155 ASN A ND2 
1210 N N   . VAL A 154 ? 0.3939 0.4525 0.5230 -0.0494 0.0177  -0.0418 156 VAL A N   
1211 C CA  . VAL A 154 ? 0.4464 0.5095 0.5931 -0.0532 0.0163  -0.0483 156 VAL A CA  
1212 C C   . VAL A 154 ? 0.4828 0.5491 0.6198 -0.0550 0.0063  -0.0520 156 VAL A C   
1213 O O   . VAL A 154 ? 0.5029 0.5634 0.6169 -0.0575 0.0044  -0.0569 156 VAL A O   
1214 C CB  . VAL A 154 ? 0.4620 0.5186 0.6122 -0.0582 0.0243  -0.0578 156 VAL A CB  
1215 C CG1 . VAL A 154 ? 0.4669 0.5275 0.6382 -0.0621 0.0230  -0.0651 156 VAL A CG1 
1216 C CG2 . VAL A 154 ? 0.4634 0.5171 0.6237 -0.0562 0.0331  -0.0529 156 VAL A CG2 
1217 N N   . ARG A 155 ? 0.4828 0.5582 0.6373 -0.0536 -0.0001 -0.0488 157 ARG A N   
1218 C CA  . ARG A 155 ? 0.5084 0.5884 0.6578 -0.0548 -0.0116 -0.0504 157 ARG A CA  
1219 C C   . ARG A 155 ? 0.5403 0.6285 0.7165 -0.0573 -0.0163 -0.0535 157 ARG A C   
1220 O O   . ARG A 155 ? 0.5405 0.6330 0.7407 -0.0561 -0.0109 -0.0501 157 ARG A O   
1221 C CB  . ARG A 155 ? 0.5002 0.5842 0.6436 -0.0488 -0.0165 -0.0397 157 ARG A CB  
1222 C CG  . ARG A 155 ? 0.5253 0.6014 0.6439 -0.0466 -0.0138 -0.0366 157 ARG A CG  
1223 C CD  . ARG A 155 ? 0.5502 0.6211 0.6433 -0.0503 -0.0198 -0.0415 157 ARG A CD  
1224 N NE  . ARG A 155 ? 0.5974 0.6621 0.6699 -0.0471 -0.0180 -0.0352 157 ARG A NE  
1225 C CZ  . ARG A 155 ? 0.6018 0.6583 0.6636 -0.0474 -0.0087 -0.0357 157 ARG A CZ  
1226 N NH1 . ARG A 155 ? 0.5403 0.5935 0.6095 -0.0505 0.0000  -0.0423 157 ARG A NH1 
1227 N NH2 . ARG A 155 ? 0.6532 0.7046 0.6993 -0.0445 -0.0080 -0.0293 157 ARG A NH2 
1228 N N   . ALA A 156 ? 0.5650 0.6554 0.7374 -0.0609 -0.0269 -0.0593 158 ALA A N   
1229 C CA  . ALA A 156 ? 0.5697 0.6676 0.7686 -0.0640 -0.0328 -0.0630 158 ALA A CA  
1230 C C   . ALA A 156 ? 0.5590 0.6680 0.7815 -0.0587 -0.0350 -0.0512 158 ALA A C   
1231 O O   . ALA A 156 ? 0.5528 0.6676 0.8037 -0.0589 -0.0317 -0.0494 158 ALA A O   
1232 C CB  . ALA A 156 ? 0.5863 0.6833 0.7723 -0.0693 -0.0453 -0.0724 158 ALA A CB  
1233 N N   . LYS A 157 ? 0.5636 0.6755 0.7758 -0.0540 -0.0398 -0.0430 159 LYS A N   
1234 C CA  . LYS A 157 ? 0.5647 0.6862 0.7971 -0.0480 -0.0394 -0.0316 159 LYS A CA  
1235 C C   . LYS A 157 ? 0.5456 0.6678 0.7905 -0.0439 -0.0264 -0.0250 159 LYS A C   
1236 O O   . LYS A 157 ? 0.5505 0.6814 0.8199 -0.0409 -0.0238 -0.0179 159 LYS A O   
1237 C CB  . LYS A 157 ? 0.6331 0.7547 0.8483 -0.0430 -0.0446 -0.0245 159 LYS A CB  
1238 C CG  . LYS A 157 ? 0.7365 0.8663 0.9691 -0.0357 -0.0417 -0.0130 159 LYS A CG  
1239 C CD  . LYS A 157 ? 0.8445 0.9772 1.0705 -0.0318 -0.0505 -0.0071 159 LYS A CD  
1240 C CE  . LYS A 157 ? 0.9357 1.0771 1.1788 -0.0345 -0.0635 -0.0078 159 LYS A CE  
1241 N NZ  . LYS A 157 ? 0.9750 1.1278 1.2541 -0.0325 -0.0609 -0.0029 159 LYS A NZ  
1242 N N   . GLY A 158 ? 0.5073 0.6207 0.7357 -0.0439 -0.0185 -0.0267 160 GLY A N   
1243 C CA  . GLY A 158 ? 0.4719 0.5854 0.7087 -0.0402 -0.0081 -0.0202 160 GLY A CA  
1244 C C   . GLY A 158 ? 0.4446 0.5494 0.6576 -0.0375 -0.0031 -0.0184 160 GLY A C   
1245 O O   . GLY A 158 ? 0.4623 0.5637 0.6557 -0.0355 -0.0070 -0.0175 160 GLY A O   
1246 N N   . ASP A 159 ? 0.3885 0.4901 0.6056 -0.0372 0.0052  -0.0171 161 ASP A N   
1247 C CA  . ASP A 159 ? 0.3469 0.4391 0.5450 -0.0370 0.0096  -0.0182 161 ASP A CA  
1248 C C   . ASP A 159 ? 0.3280 0.4193 0.5168 -0.0307 0.0117  -0.0100 161 ASP A C   
1249 O O   . ASP A 159 ? 0.3339 0.4316 0.5344 -0.0265 0.0134  -0.0031 161 ASP A O   
1250 C CB  . ASP A 159 ? 0.3241 0.4131 0.5337 -0.0402 0.0167  -0.0210 161 ASP A CB  
1251 C CG  . ASP A 159 ? 0.3239 0.4116 0.5419 -0.0468 0.0158  -0.0314 161 ASP A CG  
1252 O OD1 . ASP A 159 ? 0.3467 0.4302 0.5480 -0.0499 0.0116  -0.0389 161 ASP A OD1 
1253 O OD2 . ASP A 159 ? 0.3094 0.3998 0.5496 -0.0489 0.0193  -0.0319 161 ASP A OD2 
1254 N N   . LYS A 160 ? 0.3026 0.3858 0.4704 -0.0299 0.0120  -0.0108 162 LYS A N   
1255 C CA  . LYS A 160 ? 0.2712 0.3522 0.4302 -0.0241 0.0136  -0.0043 162 LYS A CA  
1256 C C   . LYS A 160 ? 0.2181 0.2919 0.3723 -0.0247 0.0190  -0.0042 162 LYS A C   
1257 O O   . LYS A 160 ? 0.2224 0.2897 0.3694 -0.0289 0.0205  -0.0095 162 LYS A O   
1258 C CB  . LYS A 160 ? 0.3268 0.4050 0.4689 -0.0218 0.0080  -0.0035 162 LYS A CB  
1259 C CG  . LYS A 160 ? 0.3799 0.4666 0.5304 -0.0195 0.0021  -0.0009 162 LYS A CG  
1260 C CD  . LYS A 160 ? 0.5245 0.6085 0.6600 -0.0189 -0.0048 -0.0007 162 LYS A CD  
1261 C CE  . LYS A 160 ? 0.6435 0.7207 0.7646 -0.0145 -0.0038 0.0033  162 LYS A CE  
1262 N NZ  . LYS A 160 ? 0.7284 0.8042 0.8382 -0.0140 -0.0113 0.0048  162 LYS A NZ  
1263 N N   . ILE A 161 ? 0.1886 0.2632 0.3465 -0.0205 0.0219  0.0017  163 ILE A N   
1264 C CA  . ILE A 161 ? 0.1955 0.2632 0.3484 -0.0204 0.0252  0.0028  163 ILE A CA  
1265 C C   . ILE A 161 ? 0.1929 0.2576 0.3334 -0.0147 0.0237  0.0070  163 ILE A C   
1266 O O   . ILE A 161 ? 0.1765 0.2467 0.3196 -0.0102 0.0234  0.0110  163 ILE A O   
1267 C CB  . ILE A 161 ? 0.2117 0.2823 0.3807 -0.0216 0.0291  0.0055  163 ILE A CB  
1268 C CG1 . ILE A 161 ? 0.2370 0.3101 0.4214 -0.0272 0.0311  0.0007  163 ILE A CG1 
1269 C CG2 . ILE A 161 ? 0.2166 0.2803 0.3812 -0.0214 0.0308  0.0073  163 ILE A CG2 
1270 C CD1 . ILE A 161 ? 0.2447 0.3211 0.4483 -0.0284 0.0347  0.0042  163 ILE A CD1 
1271 N N   . ALA A 162 ? 0.1927 0.2486 0.3208 -0.0149 0.0232  0.0057  164 ALA A N   
1272 C CA  . ALA A 162 ? 0.2070 0.2585 0.3236 -0.0100 0.0212  0.0081  164 ALA A CA  
1273 C C   . ALA A 162 ? 0.2100 0.2532 0.3221 -0.0109 0.0220  0.0080  164 ALA A C   
1274 O O   . ALA A 162 ? 0.2034 0.2422 0.3162 -0.0154 0.0237  0.0053  164 ALA A O   
1275 C CB  . ALA A 162 ? 0.2146 0.2643 0.3212 -0.0088 0.0177  0.0073  164 ALA A CB  
1276 N N   . ILE A 163 ? 0.2113 0.2522 0.3193 -0.0067 0.0208  0.0105  165 ILE A N   
1277 C CA  . ILE A 163 ? 0.2076 0.2396 0.3098 -0.0068 0.0193  0.0101  165 ILE A CA  
1278 C C   . ILE A 163 ? 0.2204 0.2466 0.3115 -0.0037 0.0167  0.0093  165 ILE A C   
1279 O O   . ILE A 163 ? 0.2161 0.2440 0.3025 0.0014  0.0154  0.0102  165 ILE A O   
1280 C CB  . ILE A 163 ? 0.1970 0.2288 0.2999 -0.0044 0.0182  0.0126  165 ILE A CB  
1281 C CG1 . ILE A 163 ? 0.1878 0.2245 0.3040 -0.0080 0.0204  0.0146  165 ILE A CG1 
1282 C CG2 . ILE A 163 ? 0.1995 0.2215 0.2960 -0.0040 0.0147  0.0114  165 ILE A CG2 
1283 C CD1 . ILE A 163 ? 0.2169 0.2539 0.3343 -0.0067 0.0185  0.0183  165 ILE A CD1 
1284 N N   . TRP A 164 ? 0.2224 0.2414 0.3105 -0.0068 0.0166  0.0081  166 TRP A N   
1285 C CA  . TRP A 164 ? 0.2315 0.2434 0.3108 -0.0047 0.0143  0.0084  166 TRP A CA  
1286 C C   . TRP A 164 ? 0.2331 0.2370 0.3111 -0.0029 0.0119  0.0082  166 TRP A C   
1287 O O   . TRP A 164 ? 0.2181 0.2190 0.3019 -0.0061 0.0123  0.0079  166 TRP A O   
1288 C CB  . TRP A 164 ? 0.2505 0.2588 0.3270 -0.0091 0.0162  0.0082  166 TRP A CB  
1289 C CG  . TRP A 164 ? 0.2610 0.2751 0.3344 -0.0106 0.0165  0.0078  166 TRP A CG  
1290 C CD1 . TRP A 164 ? 0.2532 0.2763 0.3319 -0.0107 0.0165  0.0067  166 TRP A CD1 
1291 C CD2 . TRP A 164 ? 0.2648 0.2761 0.3292 -0.0125 0.0161  0.0086  166 TRP A CD2 
1292 N NE1 . TRP A 164 ? 0.2453 0.2709 0.3189 -0.0128 0.0153  0.0060  166 TRP A NE1 
1293 C CE2 . TRP A 164 ? 0.2573 0.2758 0.3207 -0.0140 0.0150  0.0073  166 TRP A CE2 
1294 C CE3 . TRP A 164 ? 0.3005 0.3036 0.3577 -0.0133 0.0165  0.0110  166 TRP A CE3 
1295 C CZ2 . TRP A 164 ? 0.2826 0.3004 0.3357 -0.0160 0.0132  0.0078  166 TRP A CZ2 
1296 C CZ3 . TRP A 164 ? 0.3078 0.3104 0.3548 -0.0153 0.0160  0.0125  166 TRP A CZ3 
1297 C CH2 . TRP A 164 ? 0.2946 0.3044 0.3383 -0.0167 0.0140  0.0107  166 TRP A CH2 
1298 N N   . THR A 165 ? 0.2411 0.2415 0.3130 0.0021  0.0090  0.0080  167 THR A N   
1299 C CA  . THR A 165 ? 0.2701 0.2617 0.3398 0.0041  0.0057  0.0064  167 THR A CA  
1300 C C   . THR A 165 ? 0.2855 0.2694 0.3524 0.0054  0.0041  0.0071  167 THR A C   
1301 O O   . THR A 165 ? 0.2726 0.2587 0.3373 0.0062  0.0049  0.0092  167 THR A O   
1302 C CB  . THR A 165 ? 0.3045 0.2980 0.3698 0.0090  0.0042  0.0046  167 THR A CB  
1303 O OG1 . THR A 165 ? 0.3288 0.3229 0.3893 0.0146  0.0044  0.0041  167 THR A OG1 
1304 C CG2 . THR A 165 ? 0.3294 0.3323 0.3980 0.0080  0.0067  0.0062  167 THR A CG2 
1305 N N   . THR A 166 ? 0.3073 0.2820 0.3755 0.0055  0.0012  0.0056  168 THR A N   
1306 C CA  . THR A 166 ? 0.3163 0.2824 0.3857 0.0052  0.0001  0.0072  168 THR A CA  
1307 C C   . THR A 166 ? 0.3065 0.2687 0.3724 0.0110  -0.0023 0.0065  168 THR A C   
1308 O O   . THR A 166 ? 0.3006 0.2584 0.3678 0.0111  -0.0025 0.0099  168 THR A O   
1309 C CB  . THR A 166 ? 0.3319 0.2897 0.4085 0.0019  -0.0022 0.0062  168 THR A CB  
1310 O OG1 . THR A 166 ? 0.3487 0.2997 0.4292 0.0000  -0.0011 0.0096  168 THR A OG1 
1311 C CG2 . THR A 166 ? 0.3525 0.3046 0.4277 0.0053  -0.0078 0.0014  168 THR A CG2 
1312 N N   . GLU A 167 ? 0.3042 0.2681 0.3662 0.0160  -0.0036 0.0027  169 GLU A N   
1313 C CA  . GLU A 167 ? 0.3155 0.2741 0.3759 0.0220  -0.0052 0.0006  169 GLU A CA  
1314 C C   . GLU A 167 ? 0.3289 0.2947 0.3848 0.0276  -0.0030 -0.0015 169 GLU A C   
1315 O O   . GLU A 167 ? 0.3404 0.3066 0.3910 0.0294  -0.0029 -0.0057 169 GLU A O   
1316 C CB  . GLU A 167 ? 0.3196 0.2666 0.3808 0.0226  -0.0095 -0.0045 169 GLU A CB  
1317 C CG  . GLU A 167 ? 0.3353 0.2746 0.3962 0.0287  -0.0112 -0.0085 169 GLU A CG  
1318 C CD  . GLU A 167 ? 0.3124 0.2512 0.3788 0.0308  -0.0100 -0.0034 169 GLU A CD  
1319 O OE1 . GLU A 167 ? 0.3673 0.3002 0.4401 0.0277  -0.0114 0.0008  169 GLU A OE1 
1320 O OE2 . GLU A 167 ? 0.3272 0.2720 0.3925 0.0353  -0.0077 -0.0026 169 GLU A OE2 
1321 N N   . CYS A 168 ? 0.3360 0.3073 0.3944 0.0303  -0.0012 0.0018  170 CYS A N   
1322 C CA  . CYS A 168 ? 0.3645 0.3435 0.4220 0.0356  0.0019  0.0008  170 CYS A CA  
1323 C C   . CYS A 168 ? 0.3684 0.3410 0.4225 0.0423  0.0026  -0.0052 170 CYS A C   
1324 O O   . CYS A 168 ? 0.3601 0.3388 0.4113 0.0462  0.0066  -0.0069 170 CYS A O   
1325 C CB  . CYS A 168 ? 0.3764 0.3629 0.4401 0.0366  0.0025  0.0061  170 CYS A CB  
1326 S SG  . CYS A 168 ? 0.4424 0.4209 0.5117 0.0394  -0.0009 0.0093  170 CYS A SG  
1327 N N   . GLU A 169 ? 0.3697 0.3302 0.4244 0.0436  -0.0006 -0.0086 171 GLU A N   
1328 C CA  . GLU A 169 ? 0.3595 0.3121 0.4102 0.0497  -0.0001 -0.0161 171 GLU A CA  
1329 C C   . GLU A 169 ? 0.3570 0.3050 0.3965 0.0487  -0.0019 -0.0229 171 GLU A C   
1330 O O   . GLU A 169 ? 0.3651 0.3064 0.3978 0.0536  -0.0015 -0.0304 171 GLU A O   
1331 C CB  . GLU A 169 ? 0.3694 0.3103 0.4278 0.0516  -0.0033 -0.0173 171 GLU A CB  
1332 C CG  . GLU A 169 ? 0.3959 0.3403 0.4651 0.0531  -0.0027 -0.0099 171 GLU A CG  
1333 C CD  . GLU A 169 ? 0.4438 0.3973 0.5168 0.0588  0.0018  -0.0084 171 GLU A CD  
1334 O OE1 . GLU A 169 ? 0.4789 0.4320 0.5478 0.0642  0.0060  -0.0149 171 GLU A OE1 
1335 O OE2 . GLU A 169 ? 0.4112 0.3721 0.4915 0.0578  0.0013  -0.0007 171 GLU A OE2 
1336 N N   . ASN A 170 ? 0.3507 0.3016 0.3880 0.0426  -0.0042 -0.0206 172 ASN A N   
1337 C CA  . ASN A 170 ? 0.3569 0.3062 0.3837 0.0415  -0.0065 -0.0250 172 ASN A CA  
1338 C C   . ASN A 170 ? 0.3545 0.3148 0.3736 0.0439  -0.0010 -0.0235 172 ASN A C   
1339 O O   . ASN A 170 ? 0.3210 0.2892 0.3412 0.0396  -0.0007 -0.0188 172 ASN A O   
1340 C CB  . ASN A 170 ? 0.3744 0.3228 0.4061 0.0338  -0.0113 -0.0220 172 ASN A CB  
1341 C CG  . ASN A 170 ? 0.3693 0.3061 0.4082 0.0311  -0.0167 -0.0238 172 ASN A CG  
1342 O OD1 . ASN A 170 ? 0.4344 0.3619 0.4739 0.0348  -0.0185 -0.0286 172 ASN A OD1 
1343 N ND2 . ASN A 170 ? 0.2921 0.2291 0.3387 0.0248  -0.0190 -0.0199 172 ASN A ND2 
1344 N N   . ARG A 171 ? 0.3832 0.3443 0.3964 0.0508  0.0040  -0.0271 173 ARG A N   
1345 C CA  . ARG A 171 ? 0.4184 0.3902 0.4259 0.0538  0.0108  -0.0248 173 ARG A CA  
1346 C C   . ARG A 171 ? 0.4319 0.4052 0.4274 0.0510  0.0087  -0.0249 173 ARG A C   
1347 O O   . ARG A 171 ? 0.4208 0.4045 0.4190 0.0488  0.0116  -0.0186 173 ARG A O   
1348 C CB  . ARG A 171 ? 0.4780 0.4483 0.4811 0.0622  0.0174  -0.0297 173 ARG A CB  
1349 C CG  . ARG A 171 ? 0.5812 0.5627 0.5800 0.0664  0.0266  -0.0269 173 ARG A CG  
1350 C CD  . ARG A 171 ? 0.6928 0.6726 0.6711 0.0680  0.0281  -0.0307 173 ARG A CD  
1351 N NE  . ARG A 171 ? 0.8051 0.7708 0.7692 0.0712  0.0250  -0.0415 173 ARG A NE  
1352 C CZ  . ARG A 171 ? 0.8952 0.8549 0.8397 0.0706  0.0211  -0.0467 173 ARG A CZ  
1353 N NH1 . ARG A 171 ? 0.9088 0.8755 0.8454 0.0670  0.0199  -0.0410 173 ARG A NH1 
1354 N NH2 . ARG A 171 ? 0.9246 0.8708 0.8575 0.0734  0.0176  -0.0577 173 ARG A NH2 
1355 N N   . GLU A 172 ? 0.4423 0.4054 0.4259 0.0508  0.0028  -0.0315 174 GLU A N   
1356 C CA  . GLU A 172 ? 0.4513 0.4156 0.4230 0.0481  -0.0008 -0.0309 174 GLU A CA  
1357 C C   . GLU A 172 ? 0.4278 0.3985 0.4113 0.0407  -0.0042 -0.0230 174 GLU A C   
1358 O O   . GLU A 172 ? 0.4213 0.4006 0.4024 0.0394  -0.0022 -0.0176 174 GLU A O   
1359 C CB  . GLU A 172 ? 0.5010 0.4521 0.4604 0.0479  -0.0093 -0.0396 174 GLU A CB  
1360 C CG  . GLU A 172 ? 0.6810 0.6245 0.6254 0.0551  -0.0061 -0.0492 174 GLU A CG  
1361 C CD  . GLU A 172 ? 0.8711 0.8000 0.8055 0.0545  -0.0158 -0.0594 174 GLU A CD  
1362 O OE1 . GLU A 172 ? 0.9427 0.8697 0.8602 0.0533  -0.0211 -0.0618 174 GLU A OE1 
1363 O OE2 . GLU A 172 ? 0.8921 0.8114 0.8362 0.0550  -0.0186 -0.0646 174 GLU A OE2 
1364 N N   . ALA A 173 ? 0.4028 0.3690 0.3996 0.0361  -0.0087 -0.0224 175 ALA A N   
1365 C CA  . ALA A 173 ? 0.3822 0.3537 0.3918 0.0294  -0.0104 -0.0159 175 ALA A CA  
1366 C C   . ALA A 173 ? 0.3456 0.3296 0.3632 0.0290  -0.0031 -0.0093 175 ALA A C   
1367 O O   . ALA A 173 ? 0.3161 0.3073 0.3375 0.0257  -0.0024 -0.0043 175 ALA A O   
1368 C CB  . ALA A 173 ? 0.3929 0.3570 0.4143 0.0254  -0.0144 -0.0165 175 ALA A CB  
1369 N N   . VAL A 174 ? 0.3325 0.3188 0.3544 0.0321  0.0016  -0.0091 176 VAL A N   
1370 C CA  . VAL A 174 ? 0.3261 0.3233 0.3574 0.0314  0.0071  -0.0037 176 VAL A CA  
1371 C C   . VAL A 174 ? 0.3427 0.3492 0.3700 0.0339  0.0120  -0.0007 176 VAL A C   
1372 O O   . VAL A 174 ? 0.3364 0.3515 0.3722 0.0304  0.0140  0.0045  176 VAL A O   
1373 C CB  . VAL A 174 ? 0.3323 0.3291 0.3682 0.0350  0.0093  -0.0043 176 VAL A CB  
1374 C CG1 . VAL A 174 ? 0.3413 0.3502 0.3856 0.0357  0.0144  0.0005  176 VAL A CG1 
1375 C CG2 . VAL A 174 ? 0.3453 0.3350 0.3871 0.0312  0.0051  -0.0043 176 VAL A CG2 
1376 N N   . THR A 175 ? 0.3437 0.3482 0.3583 0.0398  0.0145  -0.0040 177 THR A N   
1377 C CA  . THR A 175 ? 0.3654 0.3792 0.3762 0.0427  0.0209  0.0000  177 THR A CA  
1378 C C   . THR A 175 ? 0.3592 0.3749 0.3651 0.0389  0.0179  0.0036  177 THR A C   
1379 O O   . THR A 175 ? 0.3439 0.3695 0.3554 0.0381  0.0222  0.0102  177 THR A O   
1380 C CB  . THR A 175 ? 0.3929 0.4050 0.3918 0.0507  0.0269  -0.0042 177 THR A CB  
1381 O OG1 . THR A 175 ? 0.4583 0.4597 0.4400 0.0522  0.0224  -0.0109 177 THR A OG1 
1382 C CG2 . THR A 175 ? 0.3683 0.3796 0.3760 0.0547  0.0300  -0.0065 177 THR A CG2 
1383 N N   . HIS A 176 ? 0.3684 0.3752 0.3662 0.0365  0.0102  0.0002  178 HIS A N   
1384 C CA  . HIS A 176 ? 0.3517 0.3604 0.3487 0.0321  0.0055  0.0048  178 HIS A CA  
1385 C C   . HIS A 176 ? 0.3502 0.3655 0.3675 0.0260  0.0058  0.0107  178 HIS A C   
1386 O O   . HIS A 176 ? 0.3708 0.3936 0.3933 0.0240  0.0072  0.0173  178 HIS A O   
1387 C CB  . HIS A 176 ? 0.3480 0.3454 0.3355 0.0303  -0.0044 -0.0005 178 HIS A CB  
1388 C CG  . HIS A 176 ? 0.4038 0.4029 0.3924 0.0257  -0.0108 0.0047  178 HIS A CG  
1389 N ND1 . HIS A 176 ? 0.4460 0.4453 0.4168 0.0277  -0.0132 0.0061  178 HIS A ND1 
1390 C CD2 . HIS A 176 ? 0.4261 0.4265 0.4317 0.0194  -0.0152 0.0088  178 HIS A CD2 
1391 C CE1 . HIS A 176 ? 0.4447 0.4457 0.4231 0.0226  -0.0200 0.0118  178 HIS A CE1 
1392 N NE2 . HIS A 176 ? 0.4377 0.4395 0.4382 0.0175  -0.0210 0.0135  178 HIS A NE2 
1393 N N   . ILE A 177 ? 0.3191 0.3316 0.3481 0.0231  0.0048  0.0085  179 ILE A N   
1394 C CA  . ILE A 177 ? 0.3052 0.3233 0.3518 0.0175  0.0061  0.0128  179 ILE A CA  
1395 C C   . ILE A 177 ? 0.3197 0.3494 0.3735 0.0187  0.0132  0.0176  179 ILE A C   
1396 O O   . ILE A 177 ? 0.3224 0.3584 0.3869 0.0152  0.0144  0.0226  179 ILE A O   
1397 C CB  . ILE A 177 ? 0.2773 0.2903 0.3317 0.0146  0.0050  0.0097  179 ILE A CB  
1398 C CG1 . ILE A 177 ? 0.2887 0.2911 0.3420 0.0119  -0.0018 0.0065  179 ILE A CG1 
1399 C CG2 . ILE A 177 ? 0.2582 0.2778 0.3277 0.0098  0.0085  0.0127  179 ILE A CG2 
1400 C CD1 . ILE A 177 ? 0.2719 0.2670 0.3274 0.0113  -0.0027 0.0032  179 ILE A CD1 
1401 N N   . GLY A 178 ? 0.3234 0.3555 0.3736 0.0235  0.0175  0.0161  180 GLY A N   
1402 C CA  . GLY A 178 ? 0.3202 0.3630 0.3784 0.0254  0.0241  0.0203  180 GLY A CA  
1403 C C   . GLY A 178 ? 0.3180 0.3679 0.3757 0.0262  0.0275  0.0265  180 GLY A C   
1404 O O   . GLY A 178 ? 0.3030 0.3615 0.3751 0.0235  0.0306  0.0317  180 GLY A O   
1405 N N   . ARG A 179 ? 0.3307 0.3766 0.3714 0.0298  0.0269  0.0259  181 ARG A N   
1406 C CA  . ARG A 179 ? 0.3377 0.3896 0.3730 0.0314  0.0304  0.0326  181 ARG A CA  
1407 C C   . ARG A 179 ? 0.3253 0.3794 0.3698 0.0256  0.0262  0.0383  181 ARG A C   
1408 O O   . ARG A 179 ? 0.3257 0.3885 0.3794 0.0249  0.0304  0.0463  181 ARG A O   
1409 C CB  . ARG A 179 ? 0.3800 0.4256 0.3905 0.0366  0.0299  0.0294  181 ARG A CB  
1410 C CG  . ARG A 179 ? 0.4901 0.5342 0.4933 0.0432  0.0360  0.0239  181 ARG A CG  
1411 C CD  . ARG A 179 ? 0.6018 0.6431 0.5819 0.0493  0.0400  0.0220  181 ARG A CD  
1412 N NE  . ARG A 179 ? 0.7062 0.7457 0.6838 0.0557  0.0467  0.0162  181 ARG A NE  
1413 C CZ  . ARG A 179 ? 0.7472 0.7954 0.7318 0.0602  0.0573  0.0198  181 ARG A CZ  
1414 N NH1 . ARG A 179 ? 0.7205 0.7801 0.7145 0.0592  0.0631  0.0296  181 ARG A NH1 
1415 N NH2 . ARG A 179 ? 0.7585 0.8042 0.7432 0.0660  0.0624  0.0141  181 ARG A NH2 
1416 N N   . VAL A 180 ? 0.3176 0.3638 0.3615 0.0217  0.0182  0.0350  182 VAL A N   
1417 C CA  . VAL A 180 ? 0.3229 0.3706 0.3787 0.0163  0.0139  0.0402  182 VAL A CA  
1418 C C   . VAL A 180 ? 0.3174 0.3716 0.3969 0.0119  0.0177  0.0426  182 VAL A C   
1419 O O   . VAL A 180 ? 0.3408 0.4012 0.4336 0.0092  0.0189  0.0496  182 VAL A O   
1420 C CB  . VAL A 180 ? 0.3446 0.3823 0.3965 0.0133  0.0048  0.0358  182 VAL A CB  
1421 C CG1 . VAL A 180 ? 0.3460 0.3855 0.4152 0.0074  0.0009  0.0412  182 VAL A CG1 
1422 C CG2 . VAL A 180 ? 0.3727 0.4039 0.4006 0.0172  -0.0003 0.0332  182 VAL A CG2 
1423 N N   . TYR A 181 ? 0.2765 0.3288 0.3613 0.0111  0.0191  0.0369  183 TYR A N   
1424 C CA  . TYR A 181 ? 0.2653 0.3228 0.3697 0.0069  0.0222  0.0373  183 TYR A CA  
1425 C C   . TYR A 181 ? 0.2904 0.3587 0.4049 0.0082  0.0284  0.0433  183 TYR A C   
1426 O O   . TYR A 181 ? 0.2808 0.3540 0.4127 0.0043  0.0298  0.0469  183 TYR A O   
1427 C CB  . TYR A 181 ? 0.2432 0.2969 0.3460 0.0069  0.0222  0.0306  183 TYR A CB  
1428 C CG  . TYR A 181 ? 0.2339 0.2911 0.3519 0.0025  0.0244  0.0290  183 TYR A CG  
1429 C CD1 . TYR A 181 ? 0.2362 0.2947 0.3692 -0.0029 0.0247  0.0304  183 TYR A CD1 
1430 C CD2 . TYR A 181 ? 0.2250 0.2836 0.3425 0.0036  0.0256  0.0257  183 TYR A CD2 
1431 C CE1 . TYR A 181 ? 0.2183 0.2785 0.3630 -0.0070 0.0268  0.0272  183 TYR A CE1 
1432 C CE2 . TYR A 181 ? 0.2179 0.2789 0.3463 -0.0008 0.0264  0.0233  183 TYR A CE2 
1433 C CZ  . TYR A 181 ? 0.2125 0.2738 0.3534 -0.0061 0.0273  0.0234  183 TYR A CZ  
1434 O OH  . TYR A 181 ? 0.1963 0.2590 0.3464 -0.0105 0.0286  0.0197  183 TYR A OH  
1435 N N   . LYS A 182 ? 0.2979 0.3698 0.4034 0.0138  0.0325  0.0442  184 LYS A N   
1436 C CA  . LYS A 182 ? 0.3147 0.3972 0.4313 0.0156  0.0392  0.0503  184 LYS A CA  
1437 C C   . LYS A 182 ? 0.3252 0.4124 0.4463 0.0146  0.0406  0.0596  184 LYS A C   
1438 O O   . LYS A 182 ? 0.3242 0.4195 0.4641 0.0126  0.0445  0.0654  184 LYS A O   
1439 C CB  . LYS A 182 ? 0.3395 0.4236 0.4440 0.0225  0.0439  0.0496  184 LYS A CB  
1440 C CG  . LYS A 182 ? 0.3744 0.4697 0.4922 0.0246  0.0515  0.0559  184 LYS A CG  
1441 C CD  . LYS A 182 ? 0.4068 0.5035 0.5149 0.0316  0.0570  0.0548  184 LYS A CD  
1442 C CE  . LYS A 182 ? 0.4346 0.5429 0.5567 0.0340  0.0658  0.0630  184 LYS A CE  
1443 N NZ  . LYS A 182 ? 0.4406 0.5512 0.5580 0.0409  0.0725  0.0619  184 LYS A NZ  
1444 N N   . GLU A 183 ? 0.3185 0.4003 0.4226 0.0159  0.0367  0.0611  185 GLU A N   
1445 C CA  . GLU A 183 ? 0.3208 0.4057 0.4259 0.0149  0.0359  0.0704  185 GLU A CA  
1446 C C   . GLU A 183 ? 0.3205 0.4067 0.4496 0.0083  0.0330  0.0730  185 GLU A C   
1447 O O   . GLU A 183 ? 0.3036 0.3971 0.4494 0.0065  0.0361  0.0817  185 GLU A O   
1448 C CB  . GLU A 183 ? 0.3591 0.4361 0.4393 0.0172  0.0299  0.0690  185 GLU A CB  
1449 C CG  . GLU A 183 ? 0.4830 0.5615 0.5554 0.0171  0.0268  0.0783  185 GLU A CG  
1450 C CD  . GLU A 183 ? 0.6647 0.7327 0.7148 0.0178  0.0176  0.0724  185 GLU A CD  
1451 O OE1 . GLU A 183 ? 0.7015 0.7644 0.7302 0.0225  0.0187  0.0654  185 GLU A OE1 
1452 O OE2 . GLU A 183 ? 0.7115 0.7760 0.7675 0.0135  0.0091  0.0743  185 GLU A OE2 
1453 N N   . ARG A 184 ? 0.3224 0.4015 0.4547 0.0046  0.0279  0.0656  186 ARG A N   
1454 C CA  . ARG A 184 ? 0.3224 0.4011 0.4760 -0.0013 0.0259  0.0663  186 ARG A CA  
1455 C C   . ARG A 184 ? 0.3248 0.4094 0.5002 -0.0041 0.0314  0.0651  186 ARG A C   
1456 O O   . ARG A 184 ? 0.3251 0.4121 0.5215 -0.0082 0.0320  0.0684  186 ARG A O   
1457 C CB  . ARG A 184 ? 0.3577 0.4268 0.5073 -0.0039 0.0201  0.0588  186 ARG A CB  
1458 C CG  . ARG A 184 ? 0.3767 0.4398 0.5111 -0.0027 0.0126  0.0605  186 ARG A CG  
1459 C CD  . ARG A 184 ? 0.3785 0.4434 0.5273 -0.0061 0.0086  0.0686  186 ARG A CD  
1460 N NE  . ARG A 184 ? 0.3696 0.4315 0.5398 -0.0115 0.0079  0.0656  186 ARG A NE  
1461 C CZ  . ARG A 184 ? 0.3431 0.3983 0.5158 -0.0140 0.0017  0.0633  186 ARG A CZ  
1462 N NH1 . ARG A 184 ? 0.3537 0.4036 0.5084 -0.0120 -0.0061 0.0631  186 ARG A NH1 
1463 N NH2 . ARG A 184 ? 0.3210 0.3744 0.5151 -0.0186 0.0034  0.0610  186 ARG A NH2 
1464 N N   . LEU A 185 ? 0.3321 0.4188 0.5041 -0.0020 0.0348  0.0604  187 LEU A N   
1465 C CA  . LEU A 185 ? 0.3311 0.4244 0.5231 -0.0043 0.0392  0.0598  187 LEU A CA  
1466 C C   . LEU A 185 ? 0.3612 0.4644 0.5657 -0.0027 0.0442  0.0700  187 LEU A C   
1467 O O   . LEU A 185 ? 0.3410 0.4499 0.5663 -0.0053 0.0473  0.0706  187 LEU A O   
1468 C CB  . LEU A 185 ? 0.3140 0.4071 0.4993 -0.0026 0.0398  0.0524  187 LEU A CB  
1469 C CG  . LEU A 185 ? 0.3166 0.4011 0.4936 -0.0050 0.0360  0.0430  187 LEU A CG  
1470 C CD1 . LEU A 185 ? 0.3070 0.3912 0.4732 -0.0018 0.0356  0.0382  187 LEU A CD1 
1471 C CD2 . LEU A 185 ? 0.3171 0.4008 0.5109 -0.0112 0.0362  0.0386  187 LEU A CD2 
1472 N N   . GLY A 186 ? 0.4004 0.5051 0.5919 0.0013  0.0450  0.0778  188 GLY A N   
1473 C CA  . GLY A 186 ? 0.4360 0.5498 0.6355 0.0036  0.0509  0.0886  188 GLY A CA  
1474 C C   . GLY A 186 ? 0.4642 0.5846 0.6697 0.0063  0.0568  0.0876  188 GLY A C   
1475 O O   . GLY A 186 ? 0.4658 0.5943 0.6930 0.0051  0.0614  0.0937  188 GLY A O   
1476 N N   . LEU A 187 ? 0.4882 0.6052 0.6772 0.0097  0.0563  0.0801  189 LEU A N   
1477 C CA  . LEU A 187 ? 0.5082 0.6315 0.7046 0.0124  0.0611  0.0790  189 LEU A CA  
1478 C C   . LEU A 187 ? 0.5568 0.6857 0.7443 0.0188  0.0686  0.0870  189 LEU A C   
1479 O O   . LEU A 187 ? 0.5698 0.6938 0.7335 0.0224  0.0684  0.0878  189 LEU A O   
1480 C CB  . LEU A 187 ? 0.5026 0.6200 0.6876 0.0135  0.0572  0.0682  189 LEU A CB  
1481 C CG  . LEU A 187 ? 0.4915 0.6051 0.6858 0.0078  0.0516  0.0600  189 LEU A CG  
1482 C CD1 . LEU A 187 ? 0.4765 0.5853 0.6583 0.0097  0.0484  0.0521  189 LEU A CD1 
1483 C CD2 . LEU A 187 ? 0.4968 0.6181 0.7172 0.0040  0.0531  0.0612  189 LEU A CD2 
1484 N N   . PRO A 188 ? 0.5816 0.7206 0.7879 0.0202  0.0756  0.0929  190 PRO A N   
1485 C CA  . PRO A 188 ? 0.6063 0.7506 0.8036 0.0268  0.0847  0.1003  190 PRO A CA  
1486 C C   . PRO A 188 ? 0.6422 0.7813 0.8167 0.0327  0.0857  0.0930  190 PRO A C   
1487 O O   . PRO A 188 ? 0.6536 0.7896 0.8305 0.0319  0.0811  0.0841  190 PRO A O   
1488 C CB  . PRO A 188 ? 0.6075 0.7633 0.8348 0.0264  0.0911  0.1060  190 PRO A CB  
1489 C CG  . PRO A 188 ? 0.5997 0.7562 0.8512 0.0192  0.0848  0.1025  190 PRO A CG  
1490 C CD  . PRO A 188 ? 0.5747 0.7204 0.8117 0.0157  0.0756  0.0929  190 PRO A CD  
1491 N N   . PRO A 189 ? 0.6647 0.8026 0.8169 0.0387  0.0917  0.0963  191 PRO A N   
1492 C CA  . PRO A 189 ? 0.6780 0.8112 0.8118 0.0448  0.0941  0.0888  191 PRO A CA  
1493 C C   . PRO A 189 ? 0.6637 0.8032 0.8155 0.0477  0.0989  0.0868  191 PRO A C   
1494 O O   . PRO A 189 ? 0.6693 0.8037 0.8109 0.0516  0.0982  0.0791  191 PRO A O   
1495 C CB  . PRO A 189 ? 0.7041 0.8374 0.8154 0.0506  0.1024  0.0946  191 PRO A CB  
1496 C CG  . PRO A 189 ? 0.7124 0.8463 0.8214 0.0466  0.0994  0.1030  191 PRO A CG  
1497 C CD  . PRO A 189 ? 0.6706 0.8109 0.8123 0.0401  0.0964  0.1069  191 PRO A CD  
1498 N N   . LYS A 190 ? 0.6433 0.7938 0.8232 0.0459  0.1034  0.0942  192 LYS A N   
1499 C CA  . LYS A 190 ? 0.6353 0.7929 0.8379 0.0473  0.1058  0.0929  192 LYS A CA  
1500 C C   . LYS A 190 ? 0.6124 0.7648 0.8201 0.0429  0.0941  0.0830  192 LYS A C   
1501 O O   . LYS A 190 ? 0.6123 0.7651 0.8244 0.0456  0.0931  0.0785  192 LYS A O   
1502 C CB  . LYS A 190 ? 0.6735 0.8435 0.9079 0.0447  0.1110  0.1029  192 LYS A CB  
1503 C CG  . LYS A 190 ? 0.7814 0.9585 1.0148 0.0497  0.1247  0.1145  192 LYS A CG  
1504 C CD  . LYS A 190 ? 0.8509 1.0387 1.1155 0.0456  0.1285  0.1258  192 LYS A CD  
1505 C CE  . LYS A 190 ? 0.9086 1.1058 1.1791 0.0512  0.1439  0.1382  192 LYS A CE  
1506 N NZ  . LYS A 190 ? 0.9270 1.1355 1.2359 0.0474  0.1475  0.1483  192 LYS A NZ  
1507 N N   . ILE A 191 ? 0.5958 0.7436 0.8036 0.0361  0.0857  0.0803  193 ILE A N   
1508 C CA  . ILE A 191 ? 0.5870 0.7296 0.7975 0.0315  0.0755  0.0714  193 ILE A CA  
1509 C C   . ILE A 191 ? 0.5876 0.7190 0.7711 0.0344  0.0719  0.0641  193 ILE A C   
1510 O O   . ILE A 191 ? 0.5980 0.7222 0.7642 0.0335  0.0699  0.0632  193 ILE A O   
1511 C CB  . ILE A 191 ? 0.5771 0.7182 0.7971 0.0237  0.0698  0.0706  193 ILE A CB  
1512 C CG1 . ILE A 191 ? 0.5732 0.7249 0.8220 0.0208  0.0738  0.0781  193 ILE A CG1 
1513 C CG2 . ILE A 191 ? 0.5805 0.7158 0.7999 0.0192  0.0605  0.0611  193 ILE A CG2 
1514 C CD1 . ILE A 191 ? 0.5637 0.7244 0.8377 0.0205  0.0736  0.0778  193 ILE A CD1 
1515 N N   . VAL A 192 ? 0.5729 0.7029 0.7547 0.0379  0.0706  0.0595  194 VAL A N   
1516 C CA  . VAL A 192 ? 0.5735 0.6925 0.7330 0.0405  0.0669  0.0525  194 VAL A CA  
1517 C C   . VAL A 192 ? 0.5496 0.6627 0.7092 0.0350  0.0568  0.0462  194 VAL A C   
1518 O O   . VAL A 192 ? 0.5566 0.6746 0.7324 0.0322  0.0533  0.0457  194 VAL A O   
1519 C CB  . VAL A 192 ? 0.5938 0.7137 0.7512 0.0482  0.0721  0.0515  194 VAL A CB  
1520 C CG1 . VAL A 192 ? 0.5981 0.7251 0.7570 0.0538  0.0842  0.0582  194 VAL A CG1 
1521 C CG2 . VAL A 192 ? 0.5947 0.7197 0.7715 0.0477  0.0683  0.0505  194 VAL A CG2 
1522 N N   . ILE A 193 ? 0.5116 0.6140 0.6530 0.0333  0.0521  0.0415  195 ILE A N   
1523 C CA  . ILE A 193 ? 0.4519 0.5474 0.5904 0.0286  0.0439  0.0358  195 ILE A CA  
1524 C C   . ILE A 193 ? 0.3970 0.4851 0.5233 0.0329  0.0417  0.0314  195 ILE A C   
1525 O O   . ILE A 193 ? 0.4008 0.4856 0.5160 0.0386  0.0456  0.0309  195 ILE A O   
1526 C CB  . ILE A 193 ? 0.4469 0.5365 0.5797 0.0230  0.0406  0.0344  195 ILE A CB  
1527 C CG1 . ILE A 193 ? 0.4399 0.5214 0.5540 0.0256  0.0407  0.0335  195 ILE A CG1 
1528 C CG2 . ILE A 193 ? 0.4527 0.5501 0.6014 0.0191  0.0432  0.0392  195 ILE A CG2 
1529 C CD1 . ILE A 193 ? 0.4312 0.5063 0.5417 0.0201  0.0362  0.0322  195 ILE A CD1 
1530 N N   . GLY A 194 ? 0.3511 0.4366 0.4798 0.0304  0.0357  0.0285  196 GLY A N   
1531 C CA  . GLY A 194 ? 0.3323 0.4112 0.4531 0.0343  0.0331  0.0256  196 GLY A CA  
1532 C C   . GLY A 194 ? 0.3194 0.3877 0.4287 0.0305  0.0271  0.0216  196 GLY A C   
1533 O O   . GLY A 194 ? 0.3126 0.3806 0.4239 0.0242  0.0240  0.0209  196 GLY A O   
1534 N N   . TYR A 195 ? 0.3207 0.3799 0.4188 0.0345  0.0262  0.0188  197 TYR A N   
1535 C CA  . TYR A 195 ? 0.3239 0.3726 0.4129 0.0319  0.0211  0.0158  197 TYR A CA  
1536 C C   . TYR A 195 ? 0.3362 0.3837 0.4287 0.0339  0.0176  0.0165  197 TYR A C   
1537 O O   . TYR A 195 ? 0.3406 0.3889 0.4361 0.0400  0.0196  0.0169  197 TYR A O   
1538 C CB  . TYR A 195 ? 0.3385 0.3772 0.4147 0.0348  0.0215  0.0123  197 TYR A CB  
1539 C CG  . TYR A 195 ? 0.3593 0.3871 0.4291 0.0316  0.0164  0.0097  197 TYR A CG  
1540 C CD1 . TYR A 195 ? 0.3758 0.4004 0.4434 0.0259  0.0146  0.0092  197 TYR A CD1 
1541 C CD2 . TYR A 195 ? 0.3799 0.4008 0.4482 0.0344  0.0138  0.0086  197 TYR A CD2 
1542 C CE1 . TYR A 195 ? 0.3841 0.3992 0.4481 0.0229  0.0110  0.0076  197 TYR A CE1 
1543 C CE2 . TYR A 195 ? 0.3814 0.3925 0.4457 0.0313  0.0098  0.0074  197 TYR A CE2 
1544 C CZ  . TYR A 195 ? 0.3867 0.3951 0.4488 0.0256  0.0087  0.0068  197 TYR A CZ  
1545 O OH  . TYR A 195 ? 0.3943 0.3936 0.4546 0.0224  0.0058  0.0062  197 TYR A OH  
1546 N N   . GLN A 196 ? 0.3276 0.3731 0.4195 0.0288  0.0128  0.0170  198 GLN A N   
1547 C CA  . GLN A 196 ? 0.3299 0.3744 0.4238 0.0294  0.0081  0.0190  198 GLN A CA  
1548 C C   . GLN A 196 ? 0.3377 0.3710 0.4216 0.0271  0.0050  0.0181  198 GLN A C   
1549 O O   . GLN A 196 ? 0.3278 0.3578 0.4064 0.0215  0.0049  0.0168  198 GLN A O   
1550 C CB  . GLN A 196 ? 0.3391 0.3916 0.4392 0.0244  0.0046  0.0210  198 GLN A CB  
1551 C CG  . GLN A 196 ? 0.4442 0.5082 0.5572 0.0248  0.0072  0.0221  198 GLN A CG  
1552 C CD  . GLN A 196 ? 0.5783 0.6482 0.6960 0.0184  0.0034  0.0219  198 GLN A CD  
1553 O OE1 . GLN A 196 ? 0.5983 0.6642 0.7087 0.0126  0.0028  0.0192  198 GLN A OE1 
1554 N NE2 . GLN A 196 ? 0.6219 0.7013 0.7530 0.0191  0.0007  0.0243  198 GLN A NE2 
1555 N N   . SER A 197 ? 0.3425 0.3699 0.4260 0.0315  0.0031  0.0191  199 SER A N   
1556 C CA  . SER A 197 ? 0.3580 0.3754 0.4353 0.0297  -0.0003 0.0202  199 SER A CA  
1557 C C   . SER A 197 ? 0.3601 0.3801 0.4346 0.0239  -0.0039 0.0235  199 SER A C   
1558 O O   . SER A 197 ? 0.3603 0.3888 0.4401 0.0237  -0.0065 0.0260  199 SER A O   
1559 C CB  . SER A 197 ? 0.4077 0.4210 0.4898 0.0358  -0.0022 0.0222  199 SER A CB  
1560 O OG  . SER A 197 ? 0.5160 0.5190 0.5939 0.0346  -0.0050 0.0240  199 SER A OG  
1561 N N   . HIS A 198 ? 0.3644 0.3775 0.4311 0.0191  -0.0040 0.0234  200 HIS A N   
1562 C CA  . HIS A 198 ? 0.3730 0.3874 0.4338 0.0138  -0.0067 0.0263  200 HIS A CA  
1563 C C   . HIS A 198 ? 0.4170 0.4311 0.4780 0.0163  -0.0123 0.0324  200 HIS A C   
1564 O O   . HIS A 198 ? 0.4091 0.4286 0.4670 0.0135  -0.0164 0.0351  200 HIS A O   
1565 C CB  . HIS A 198 ? 0.3492 0.3555 0.4022 0.0088  -0.0040 0.0256  200 HIS A CB  
1566 C CG  . HIS A 198 ? 0.3481 0.3556 0.4023 0.0052  0.0005  0.0207  200 HIS A CG  
1567 N ND1 . HIS A 198 ? 0.3570 0.3735 0.4154 0.0035  0.0017  0.0181  200 HIS A ND1 
1568 C CD2 . HIS A 198 ? 0.3561 0.3569 0.4102 0.0029  0.0037  0.0187  200 HIS A CD2 
1569 C CE1 . HIS A 198 ? 0.3667 0.3815 0.4270 0.0006  0.0057  0.0149  200 HIS A CE1 
1570 N NE2 . HIS A 198 ? 0.3733 0.3790 0.4312 0.0002  0.0067  0.0152  200 HIS A NE2 
1571 N N   . ALA A 199 ? 0.4494 0.4570 0.5143 0.0214  -0.0131 0.0346  201 ALA A N   
1572 C CA  . ALA A 199 ? 0.4915 0.4989 0.5602 0.0247  -0.0186 0.0413  201 ALA A CA  
1573 C C   . ALA A 199 ? 0.5118 0.5305 0.5907 0.0278  -0.0220 0.0429  201 ALA A C   
1574 O O   . ALA A 199 ? 0.5054 0.5271 0.5853 0.0275  -0.0284 0.0491  201 ALA A O   
1575 C CB  . ALA A 199 ? 0.4949 0.4929 0.5693 0.0300  -0.0178 0.0420  201 ALA A CB  
1576 N N   . ASP A 200 ? 0.5305 0.5557 0.6175 0.0305  -0.0180 0.0383  202 ASP A N   
1577 C CA  . ASP A 200 ? 0.5460 0.5828 0.6449 0.0325  -0.0205 0.0400  202 ASP A CA  
1578 C C   . ASP A 200 ? 0.5758 0.6201 0.6705 0.0257  -0.0238 0.0395  202 ASP A C   
1579 O O   . ASP A 200 ? 0.5814 0.6323 0.6808 0.0249  -0.0308 0.0436  202 ASP A O   
1580 C CB  . ASP A 200 ? 0.5493 0.5908 0.6587 0.0377  -0.0139 0.0361  202 ASP A CB  
1581 C CG  . ASP A 200 ? 0.5904 0.6243 0.7029 0.0446  -0.0100 0.0345  202 ASP A CG  
1582 O OD1 . ASP A 200 ? 0.6053 0.6324 0.7187 0.0466  -0.0135 0.0379  202 ASP A OD1 
1583 O OD2 . ASP A 200 ? 0.6115 0.6458 0.7250 0.0479  -0.0033 0.0298  202 ASP A OD2 
1584 N N   . THR A 201 ? 0.5857 0.6291 0.6728 0.0209  -0.0194 0.0344  203 THR A N   
1585 C CA  . THR A 201 ? 0.6109 0.6598 0.6940 0.0143  -0.0218 0.0325  203 THR A CA  
1586 C C   . THR A 201 ? 0.6434 0.6898 0.7144 0.0100  -0.0286 0.0358  203 THR A C   
1587 O O   . THR A 201 ? 0.6447 0.6974 0.7146 0.0060  -0.0336 0.0350  203 THR A O   
1588 C CB  . THR A 201 ? 0.6253 0.6716 0.7031 0.0101  -0.0154 0.0267  203 THR A CB  
1589 O OG1 . THR A 201 ? 0.6201 0.6684 0.7067 0.0141  -0.0097 0.0247  203 THR A OG1 
1590 C CG2 . THR A 201 ? 0.6489 0.7014 0.7265 0.0039  -0.0168 0.0234  203 THR A CG2 
1591 N N   . ALA A 202 ? 0.6643 0.7013 0.7257 0.0107  -0.0290 0.0396  204 ALA A N   
1592 C CA  . ALA A 202 ? 0.6853 0.7195 0.7328 0.0068  -0.0346 0.0441  204 ALA A CA  
1593 C C   . ALA A 202 ? 0.7004 0.7411 0.7538 0.0089  -0.0445 0.0504  204 ALA A C   
1594 O O   . ALA A 202 ? 0.7128 0.7559 0.7555 0.0045  -0.0511 0.0523  204 ALA A O   
1595 C CB  . ALA A 202 ? 0.6905 0.7134 0.7295 0.0074  -0.0318 0.0480  204 ALA A CB  
1596 N N   . THR A 203 ? 0.7026 0.7464 0.7733 0.0157  -0.0456 0.0534  205 THR A N   
1597 C CA  . THR A 203 ? 0.7121 0.7624 0.7931 0.0184  -0.0550 0.0602  205 THR A CA  
1598 C C   . THR A 203 ? 0.7330 0.7953 0.8274 0.0177  -0.0575 0.0569  205 THR A C   
1599 O O   . THR A 203 ? 0.7258 0.7918 0.8336 0.0210  -0.0508 0.0529  205 THR A O   
1600 C CB  . THR A 203 ? 0.7203 0.7675 0.8159 0.0263  -0.0543 0.0654  205 THR A CB  
1601 O OG1 . THR A 203 ? 0.7201 0.7716 0.8324 0.0315  -0.0478 0.0608  205 THR A OG1 
1602 C CG2 . THR A 203 ? 0.7308 0.7652 0.8168 0.0272  -0.0502 0.0672  205 THR A CG2 
1603 N N   . LYS A 204 ? 0.7563 0.8246 0.8471 0.0133  -0.0673 0.0588  206 LYS A N   
1604 C CA  . LYS A 204 ? 0.7613 0.8415 0.8685 0.0125  -0.0717 0.0567  206 LYS A CA  
1605 C C   . LYS A 204 ? 0.7642 0.8507 0.8939 0.0191  -0.0773 0.0643  206 LYS A C   
1606 O O   . LYS A 204 ? 0.7619 0.8475 0.8892 0.0197  -0.0867 0.0721  206 LYS A O   
1607 C CB  . LYS A 204 ? 0.7940 0.8770 0.8873 0.0047  -0.0809 0.0545  206 LYS A CB  
1608 C CG  . LYS A 204 ? 0.8517 0.9324 0.9326 -0.0016 -0.0743 0.0445  206 LYS A CG  
1609 C CD  . LYS A 204 ? 0.9116 0.9818 0.9786 -0.0020 -0.0626 0.0412  206 LYS A CD  
1610 C CE  . LYS A 204 ? 0.9820 1.0529 1.0477 -0.0067 -0.0557 0.0318  206 LYS A CE  
1611 N NZ  . LYS A 204 ? 1.0375 1.0986 1.0904 -0.0081 -0.0455 0.0285  206 LYS A NZ  
1612 N N   . SER A 205 ? 0.7671 0.8601 0.9193 0.0242  -0.0711 0.0628  207 SER A N   
1613 C CA  . SER A 205 ? 0.7687 0.8676 0.9459 0.0314  -0.0734 0.0693  207 SER A CA  
1614 C C   . SER A 205 ? 0.7593 0.8715 0.9619 0.0324  -0.0738 0.0686  207 SER A C   
1615 O O   . SER A 205 ? 0.7502 0.8676 0.9762 0.0392  -0.0716 0.0728  207 SER A O   
1616 C CB  . SER A 205 ? 0.7990 0.8909 0.9805 0.0388  -0.0620 0.0686  207 SER A CB  
1617 O OG  . SER A 205 ? 0.8668 0.9461 1.0276 0.0378  -0.0601 0.0685  207 SER A OG  
1618 N N   . GLY A 206 ? 0.7635 0.8809 0.9636 0.0260  -0.0758 0.0635  208 GLY A N   
1619 C CA  . GLY A 206 ? 0.7573 0.8871 0.9833 0.0265  -0.0752 0.0629  208 GLY A CA  
1620 C C   . GLY A 206 ? 0.7647 0.8959 0.9854 0.0209  -0.0700 0.0550  208 GLY A C   
1621 O O   . GLY A 206 ? 0.7672 0.8913 0.9643 0.0150  -0.0706 0.0499  208 GLY A O   
1622 N N   . SER A 207 ? 0.7660 0.9068 1.0107 0.0227  -0.0641 0.0545  209 SER A N   
1623 C CA  . SER A 207 ? 0.7762 0.9194 1.0215 0.0179  -0.0583 0.0483  209 SER A CA  
1624 C C   . SER A 207 ? 0.7991 0.9343 1.0299 0.0198  -0.0441 0.0445  209 SER A C   
1625 O O   . SER A 207 ? 0.8144 0.9498 1.0429 0.0155  -0.0395 0.0398  209 SER A O   
1626 C CB  . SER A 207 ? 0.7719 0.9284 1.0498 0.0190  -0.0572 0.0506  209 SER A CB  
1627 O OG  . SER A 207 ? 0.7789 0.9417 1.0796 0.0268  -0.0538 0.0575  209 SER A OG  
1628 N N   . THR A 208 ? 0.7952 0.9232 1.0173 0.0259  -0.0380 0.0465  210 THR A N   
1629 C CA  . THR A 208 ? 0.7946 0.9152 1.0038 0.0280  -0.0260 0.0431  210 THR A CA  
1630 C C   . THR A 208 ? 0.7948 0.9032 0.9841 0.0303  -0.0256 0.0429  210 THR A C   
1631 O O   . THR A 208 ? 0.8033 0.9098 0.9937 0.0330  -0.0319 0.0471  210 THR A O   
1632 C CB  . THR A 208 ? 0.7980 0.9245 1.0246 0.0350  -0.0149 0.0453  210 THR A CB  
1633 O OG1 . THR A 208 ? 0.7897 0.9205 1.0330 0.0413  -0.0167 0.0506  210 THR A OG1 
1634 C CG2 . THR A 208 ? 0.7978 0.9343 1.0409 0.0321  -0.0109 0.0450  210 THR A CG2 
1635 N N   . THR A 209 ? 0.7743 0.8744 0.9471 0.0292  -0.0184 0.0385  211 THR A N   
1636 C CA  . THR A 209 ? 0.7590 0.8476 0.9167 0.0322  -0.0155 0.0377  211 THR A CA  
1637 C C   . THR A 209 ? 0.7096 0.7976 0.8724 0.0392  -0.0052 0.0368  211 THR A C   
1638 O O   . THR A 209 ? 0.7044 0.7980 0.8732 0.0394  0.0013  0.0356  211 THR A O   
1639 C CB  . THR A 209 ? 0.8041 0.8842 0.9421 0.0261  -0.0150 0.0334  211 THR A CB  
1640 O OG1 . THR A 209 ? 0.8328 0.9142 0.9652 0.0197  -0.0231 0.0334  211 THR A OG1 
1641 C CG2 . THR A 209 ? 0.8186 0.8865 0.9428 0.0286  -0.0129 0.0328  211 THR A CG2 
1642 N N   . LYS A 210 ? 0.6694 0.7505 0.8299 0.0450  -0.0038 0.0375  212 LYS A N   
1643 C CA  . LYS A 210 ? 0.6418 0.7193 0.8012 0.0514  0.0058  0.0349  212 LYS A CA  
1644 C C   . LYS A 210 ? 0.6077 0.6784 0.7496 0.0483  0.0106  0.0297  212 LYS A C   
1645 O O   . LYS A 210 ? 0.6058 0.6689 0.7345 0.0436  0.0069  0.0279  212 LYS A O   
1646 C CB  . LYS A 210 ? 0.6769 0.7459 0.8361 0.0573  0.0049  0.0354  212 LYS A CB  
1647 C CG  . LYS A 210 ? 0.7448 0.8096 0.9043 0.0650  0.0145  0.0317  212 LYS A CG  
1648 C CD  . LYS A 210 ? 0.8211 0.8717 0.9622 0.0650  0.0153  0.0263  212 LYS A CD  
1649 C CE  . LYS A 210 ? 0.8695 0.9146 1.0093 0.0727  0.0237  0.0213  212 LYS A CE  
1650 N NZ  . LYS A 210 ? 0.8790 0.9096 1.0090 0.0741  0.0216  0.0171  212 LYS A NZ  
1651 N N   . ASN A 211 ? 0.5767 0.6507 0.7199 0.0512  0.0189  0.0283  213 ASN A N   
1652 C CA  . ASN A 211 ? 0.5394 0.6073 0.6676 0.0500  0.0232  0.0243  213 ASN A CA  
1653 C C   . ASN A 211 ? 0.5283 0.5861 0.6468 0.0561  0.0268  0.0204  213 ASN A C   
1654 O O   . ASN A 211 ? 0.5235 0.5838 0.6470 0.0626  0.0333  0.0201  213 ASN A O   
1655 C CB  . ASN A 211 ? 0.5128 0.5896 0.6466 0.0503  0.0302  0.0258  213 ASN A CB  
1656 C CG  . ASN A 211 ? 0.5500 0.6349 0.6924 0.0435  0.0274  0.0281  213 ASN A CG  
1657 O OD1 . ASN A 211 ? 0.5703 0.6521 0.7081 0.0374  0.0210  0.0268  213 ASN A OD1 
1658 N ND2 . ASN A 211 ? 0.5484 0.6433 0.7035 0.0441  0.0324  0.0313  213 ASN A ND2 
1659 N N   . ARG A 212 ? 0.5367 0.5830 0.6422 0.0540  0.0229  0.0170  214 ARG A N   
1660 C CA  . ARG A 212 ? 0.5543 0.5900 0.6499 0.0589  0.0255  0.0119  214 ARG A CA  
1661 C C   . ARG A 212 ? 0.5584 0.5946 0.6442 0.0612  0.0325  0.0086  214 ARG A C   
1662 O O   . ARG A 212 ? 0.5824 0.6139 0.6632 0.0674  0.0373  0.0045  214 ARG A O   
1663 C CB  . ARG A 212 ? 0.6035 0.6272 0.6896 0.0551  0.0193  0.0095  214 ARG A CB  
1664 C CG  . ARG A 212 ? 0.7015 0.7135 0.7834 0.0605  0.0198  0.0046  214 ARG A CG  
1665 C CD  . ARG A 212 ? 0.7682 0.7702 0.8492 0.0577  0.0132  0.0051  214 ARG A CD  
1666 N NE  . ARG A 212 ? 0.8003 0.8062 0.8925 0.0576  0.0095  0.0115  214 ARG A NE  
1667 C CZ  . ARG A 212 ? 0.8159 0.8157 0.9084 0.0546  0.0039  0.0149  214 ARG A CZ  
1668 N NH1 . ARG A 212 ? 0.7825 0.7866 0.8838 0.0547  -0.0001 0.0214  214 ARG A NH1 
1669 N NH2 . ARG A 212 ? 0.8343 0.8239 0.9186 0.0513  0.0020  0.0123  214 ARG A NH2 
1670 N N   . PHE A 213 ? 0.5351 0.5766 0.6179 0.0563  0.0332  0.0104  215 PHE A N   
1671 C CA  . PHE A 213 ? 0.5260 0.5694 0.5999 0.0580  0.0391  0.0095  215 PHE A CA  
1672 C C   . PHE A 213 ? 0.5241 0.5800 0.6079 0.0545  0.0418  0.0155  215 PHE A C   
1673 O O   . PHE A 213 ? 0.5194 0.5803 0.6140 0.0493  0.0377  0.0184  215 PHE A O   
1674 C CB  . PHE A 213 ? 0.5233 0.5562 0.5801 0.0553  0.0354  0.0050  215 PHE A CB  
1675 C CG  . PHE A 213 ? 0.5380 0.5577 0.5879 0.0565  0.0306  -0.0007 215 PHE A CG  
1676 C CD1 . PHE A 213 ? 0.5518 0.5648 0.5952 0.0634  0.0338  -0.0062 215 PHE A CD1 
1677 C CD2 . PHE A 213 ? 0.5413 0.5553 0.5927 0.0509  0.0235  -0.0005 215 PHE A CD2 
1678 C CE1 . PHE A 213 ? 0.5599 0.5603 0.5998 0.0643  0.0291  -0.0115 215 PHE A CE1 
1679 C CE2 . PHE A 213 ? 0.5476 0.5497 0.5954 0.0518  0.0193  -0.0048 215 PHE A CE2 
1680 C CZ  . PHE A 213 ? 0.5561 0.5512 0.5987 0.0584  0.0216  -0.0103 215 PHE A CZ  
1681 N N   . VAL A 214 ? 0.5222 0.5827 0.6019 0.0572  0.0490  0.0172  216 VAL A N   
1682 C CA  . VAL A 214 ? 0.5191 0.5913 0.6096 0.0546  0.0528  0.0235  216 VAL A CA  
1683 C C   . VAL A 214 ? 0.5128 0.5839 0.5887 0.0551  0.0569  0.0247  216 VAL A C   
1684 O O   . VAL A 214 ? 0.5361 0.6015 0.5966 0.0603  0.0605  0.0212  216 VAL A O   
1685 C CB  . VAL A 214 ? 0.5261 0.6092 0.6345 0.0590  0.0595  0.0278  216 VAL A CB  
1686 C CG1 . VAL A 214 ? 0.5317 0.6267 0.6536 0.0564  0.0639  0.0348  216 VAL A CG1 
1687 C CG2 . VAL A 214 ? 0.5274 0.6118 0.6497 0.0583  0.0537  0.0275  216 VAL A CG2 
1688 N N   . VAL A 215 ? 0.4841 0.5603 0.5648 0.0499  0.0560  0.0294  217 VAL A N   
1689 C CA  . VAL A 215 ? 0.4824 0.5591 0.5517 0.0499  0.0590  0.0327  217 VAL A CA  
1690 C C   . VAL A 215 ? 0.4745 0.5633 0.5611 0.0470  0.0632  0.0413  217 VAL A C   
1691 O O   . VAL A 215 ? 0.4866 0.5790 0.5674 0.0485  0.0684  0.0468  217 VAL A O   
1692 C CB  . VAL A 215 ? 0.4988 0.5659 0.5547 0.0454  0.0509  0.0297  217 VAL A CB  
1693 C CG1 . VAL A 215 ? 0.5287 0.5835 0.5687 0.0480  0.0465  0.0214  217 VAL A CG1 
1694 C CG2 . VAL A 215 ? 0.4854 0.5536 0.5552 0.0378  0.0448  0.0308  217 VAL A CG2 
1695 O OXT . VAL A 215 ? 0.4273 0.5217 0.5332 0.0432  0.0610  0.0427  217 VAL A OXT 
1696 N N   . ALA B 9   ? 1.2766 0.4958 0.5218 -0.0632 -0.1863 0.0182  11  ALA B N   
1697 C CA  . ALA B 9   ? 1.2381 0.5089 0.5430 -0.0507 -0.2016 0.0119  11  ALA B CA  
1698 C C   . ALA B 9   ? 1.1954 0.5231 0.5608 -0.0522 -0.1741 0.0088  11  ALA B C   
1699 O O   . ALA B 9   ? 1.2030 0.5293 0.5608 -0.0647 -0.1457 0.0100  11  ALA B O   
1700 C CB  . ALA B 9   ? 1.2472 0.5039 0.5312 -0.0536 -0.2193 0.0076  11  ALA B CB  
1701 N N   . ARG B 10  ? 1.1410 0.5170 0.5655 -0.0393 -0.1824 0.0048  12  ARG B N   
1702 C CA  . ARG B 10  ? 1.0818 0.5077 0.5592 -0.0393 -0.1586 0.0033  12  ARG B CA  
1703 C C   . ARG B 10  ? 1.0404 0.4844 0.5330 -0.0460 -0.1460 -0.0006 12  ARG B C   
1704 O O   . ARG B 10  ? 1.0453 0.4884 0.5385 -0.0443 -0.1630 -0.0059 12  ARG B O   
1705 C CB  . ARG B 10  ? 1.0604 0.5281 0.5917 -0.0248 -0.1695 -0.0004 12  ARG B CB  
1706 C CG  . ARG B 10  ? 1.0752 0.5891 0.6530 -0.0255 -0.1444 -0.0005 12  ARG B CG  
1707 C CD  . ARG B 10  ? 1.0940 0.6468 0.7214 -0.0133 -0.1525 -0.0051 12  ARG B CD  
1708 N NE  . ARG B 10  ? 1.1629 0.7001 0.7811 -0.0056 -0.1666 -0.0040 12  ARG B NE  
1709 C CZ  . ARG B 10  ? 1.1757 0.7174 0.7974 -0.0059 -0.1552 -0.0012 12  ARG B CZ  
1710 N NH1 . ARG B 10  ? 1.1593 0.7241 0.7956 -0.0131 -0.1306 0.0012  12  ARG B NH1 
1711 N NH2 . ARG B 10  ? 1.1673 0.6900 0.7781 0.0013  -0.1688 -0.0010 12  ARG B NH2 
1712 N N   . ILE B 11  ? 0.9944 0.4547 0.5001 -0.0532 -0.1167 0.0016  13  ILE B N   
1713 C CA  . ILE B 11  ? 0.9596 0.4362 0.4815 -0.0587 -0.1013 -0.0014 13  ILE B CA  
1714 C C   . ILE B 11  ? 0.8950 0.4225 0.4763 -0.0496 -0.1000 -0.0048 13  ILE B C   
1715 O O   . ILE B 11  ? 0.8570 0.4134 0.4687 -0.0454 -0.0871 -0.0018 13  ILE B O   
1716 C CB  . ILE B 11  ? 0.9677 0.4363 0.4768 -0.0694 -0.0705 0.0024  13  ILE B CB  
1717 C CG1 . ILE B 11  ? 1.0235 0.4408 0.4735 -0.0798 -0.0680 0.0053  13  ILE B CG1 
1718 C CG2 . ILE B 11  ? 0.9643 0.4405 0.4828 -0.0748 -0.0557 -0.0008 13  ILE B CG2 
1719 C CD1 . ILE B 11  ? 1.0529 0.4623 0.4925 -0.0913 -0.0362 0.0070  13  ILE B CD1 
1720 N N   . ILE B 12  ? 0.8769 0.4137 0.4724 -0.0477 -0.1133 -0.0116 14  ILE B N   
1721 C CA  . ILE B 12  ? 0.8487 0.4286 0.4966 -0.0404 -0.1134 -0.0164 14  ILE B CA  
1722 C C   . ILE B 12  ? 0.8395 0.4261 0.4963 -0.0474 -0.1005 -0.0206 14  ILE B C   
1723 O O   . ILE B 12  ? 0.8592 0.4225 0.4905 -0.0541 -0.1096 -0.0252 14  ILE B O   
1724 C CB  . ILE B 12  ? 0.8507 0.4385 0.5145 -0.0307 -0.1431 -0.0231 14  ILE B CB  
1725 C CG1 . ILE B 12  ? 0.8678 0.4399 0.5153 -0.0236 -0.1559 -0.0184 14  ILE B CG1 
1726 C CG2 . ILE B 12  ? 0.8245 0.4576 0.5447 -0.0247 -0.1403 -0.0298 14  ILE B CG2 
1727 C CD1 . ILE B 12  ? 0.8872 0.4660 0.5515 -0.0125 -0.1824 -0.0240 14  ILE B CD1 
1728 N N   . TYR B 13  ? 0.8088 0.4251 0.4995 -0.0461 -0.0795 -0.0189 15  TYR B N   
1729 C CA  . TYR B 13  ? 0.7925 0.4169 0.4966 -0.0516 -0.0657 -0.0228 15  TYR B CA  
1730 C C   . TYR B 13  ? 0.7798 0.4407 0.5303 -0.0457 -0.0670 -0.0282 15  TYR B C   
1731 O O   . TYR B 13  ? 0.7798 0.4648 0.5552 -0.0387 -0.0603 -0.0241 15  TYR B O   
1732 C CB  . TYR B 13  ? 0.7808 0.4044 0.4824 -0.0549 -0.0368 -0.0153 15  TYR B CB  
1733 C CG  . TYR B 13  ? 0.8002 0.3891 0.4593 -0.0623 -0.0298 -0.0112 15  TYR B CG  
1734 C CD1 . TYR B 13  ? 0.8389 0.3954 0.4637 -0.0725 -0.0299 -0.0157 15  TYR B CD1 
1735 C CD2 . TYR B 13  ? 0.8123 0.4001 0.4647 -0.0606 -0.0215 -0.0039 15  TYR B CD2 
1736 C CE1 . TYR B 13  ? 0.8689 0.3910 0.4526 -0.0808 -0.0199 -0.0127 15  TYR B CE1 
1737 C CE2 . TYR B 13  ? 0.8539 0.4096 0.4684 -0.0690 -0.0119 -0.0014 15  TYR B CE2 
1738 C CZ  . TYR B 13  ? 0.8888 0.4106 0.4682 -0.0791 -0.0103 -0.0057 15  TYR B CZ  
1739 O OH  . TYR B 13  ? 0.9333 0.4203 0.4724 -0.0888 0.0013  -0.0042 15  TYR B OH  
1740 N N   . ASP B 14  ? 0.7654 0.4303 0.5270 -0.0495 -0.0753 -0.0382 16  ASP B N   
1741 C CA  . ASP B 14  ? 0.7346 0.4324 0.5402 -0.0470 -0.0700 -0.0444 16  ASP B CA  
1742 C C   . ASP B 14  ? 0.7201 0.4240 0.5345 -0.0504 -0.0398 -0.0390 16  ASP B C   
1743 O O   . ASP B 14  ? 0.7190 0.4026 0.5087 -0.0548 -0.0245 -0.0324 16  ASP B O   
1744 C CB  . ASP B 14  ? 0.7402 0.4448 0.5613 -0.0505 -0.0886 -0.0588 16  ASP B CB  
1745 C CG  . ASP B 14  ? 0.7989 0.4823 0.5984 -0.0624 -0.0854 -0.0642 16  ASP B CG  
1746 O OD1 . ASP B 14  ? 0.8215 0.4907 0.6047 -0.0682 -0.0616 -0.0580 16  ASP B OD1 
1747 O OD2 . ASP B 14  ? 0.8275 0.5086 0.6271 -0.0660 -0.1070 -0.0752 16  ASP B OD2 
1748 N N   . ARG B 15  ? 0.6997 0.4305 0.5496 -0.0479 -0.0311 -0.0421 17  ARG B N   
1749 C CA  . ARG B 15  ? 0.7010 0.4376 0.5610 -0.0493 -0.0045 -0.0365 17  ARG B CA  
1750 C C   . ARG B 15  ? 0.7243 0.4389 0.5672 -0.0589 0.0083  -0.0389 17  ARG B C   
1751 O O   . ARG B 15  ? 0.7336 0.4370 0.5647 -0.0588 0.0283  -0.0298 17  ARG B O   
1752 C CB  . ARG B 15  ? 0.6901 0.4544 0.5873 -0.0475 0.0004  -0.0424 17  ARG B CB  
1753 C CG  . ARG B 15  ? 0.7223 0.4902 0.6264 -0.0471 0.0270  -0.0346 17  ARG B CG  
1754 C CD  . ARG B 15  ? 0.7410 0.5322 0.6771 -0.0470 0.0323  -0.0412 17  ARG B CD  
1755 N NE  . ARG B 15  ? 0.8206 0.6109 0.7593 -0.0469 0.0575  -0.0333 17  ARG B NE  
1756 C CZ  . ARG B 15  ? 0.9007 0.6771 0.8361 -0.0540 0.0742  -0.0349 17  ARG B CZ  
1757 N NH1 . ARG B 15  ? 0.9209 0.6843 0.8502 -0.0632 0.0687  -0.0452 17  ARG B NH1 
1758 N NH2 . ARG B 15  ? 0.9181 0.6911 0.8537 -0.0520 0.0963  -0.0262 17  ARG B NH2 
1759 N N   . ALA B 16  ? 0.7336 0.4421 0.5759 -0.0672 -0.0038 -0.0516 18  ALA B N   
1760 C CA  . ALA B 16  ? 0.7558 0.4422 0.5810 -0.0782 0.0080  -0.0561 18  ALA B CA  
1761 C C   . ALA B 16  ? 0.7922 0.4469 0.5771 -0.0812 0.0139  -0.0490 18  ALA B C   
1762 O O   . ALA B 16  ? 0.8093 0.4481 0.5839 -0.0858 0.0364  -0.0461 18  ALA B O   
1763 C CB  . ALA B 16  ? 0.7613 0.4484 0.5916 -0.0868 -0.0112 -0.0721 18  ALA B CB  
1764 N N   . PHE B 17  ? 0.8046 0.4475 0.5660 -0.0789 -0.0044 -0.0467 19  PHE B N   
1765 C CA  . PHE B 17  ? 0.8424 0.4534 0.5637 -0.0832 0.0028  -0.0409 19  PHE B CA  
1766 C C   . PHE B 17  ? 0.8227 0.4376 0.5490 -0.0772 0.0279  -0.0285 19  PHE B C   
1767 O O   . PHE B 17  ? 0.8229 0.4174 0.5317 -0.0821 0.0474  -0.0260 19  PHE B O   
1768 C CB  . PHE B 17  ? 0.8773 0.4735 0.5714 -0.0820 -0.0221 -0.0407 19  PHE B CB  
1769 C CG  . PHE B 17  ? 0.9348 0.4924 0.5820 -0.0900 -0.0148 -0.0376 19  PHE B CG  
1770 C CD1 . PHE B 17  ? 0.9575 0.5090 0.5947 -0.0871 0.0010  -0.0276 19  PHE B CD1 
1771 C CD2 . PHE B 17  ? 0.9797 0.5073 0.5933 -0.1018 -0.0216 -0.0457 19  PHE B CD2 
1772 C CE1 . PHE B 17  ? 0.9938 0.5097 0.5896 -0.0958 0.0114  -0.0260 19  PHE B CE1 
1773 C CE2 . PHE B 17  ? 1.0219 0.5110 0.5895 -0.1105 -0.0116 -0.0435 19  PHE B CE2 
1774 C CZ  . PHE B 17  ? 1.0239 0.5075 0.5837 -0.1075 0.0057  -0.0338 19  PHE B CZ  
1775 N N   . LEU B 18  ? 0.8001 0.4419 0.5514 -0.0666 0.0273  -0.0214 20  LEU B N   
1776 C CA  . LEU B 18  ? 0.7865 0.4361 0.5453 -0.0600 0.0475  -0.0099 20  LEU B CA  
1777 C C   . LEU B 18  ? 0.7916 0.4430 0.5646 -0.0598 0.0715  -0.0074 20  LEU B C   
1778 O O   . LEU B 18  ? 0.8094 0.4517 0.5764 -0.0581 0.0903  -0.0004 20  LEU B O   
1779 C CB  . LEU B 18  ? 0.7538 0.4321 0.5353 -0.0498 0.0399  -0.0041 20  LEU B CB  
1780 C CG  . LEU B 18  ? 0.7481 0.4232 0.5157 -0.0484 0.0193  -0.0047 20  LEU B CG  
1781 C CD1 . LEU B 18  ? 0.7051 0.4087 0.4972 -0.0394 0.0130  -0.0011 20  LEU B CD1 
1782 C CD2 . LEU B 18  ? 0.7772 0.4300 0.5159 -0.0521 0.0259  0.0002  20  LEU B CD2 
1783 N N   . MET B 19  ? 0.7736 0.4356 0.5659 -0.0613 0.0718  -0.0133 21  MET B N   
1784 C CA  . MET B 19  ? 0.7824 0.4403 0.5843 -0.0620 0.0951  -0.0113 21  MET B CA  
1785 C C   . MET B 19  ? 0.8305 0.4565 0.6079 -0.0716 0.1082  -0.0156 21  MET B C   
1786 O O   . MET B 19  ? 0.8419 0.4581 0.6192 -0.0688 0.1307  -0.0092 21  MET B O   
1787 C CB  . MET B 19  ? 0.7597 0.4323 0.5847 -0.0647 0.0932  -0.0190 21  MET B CB  
1788 C CG  . MET B 19  ? 0.7536 0.4550 0.6030 -0.0563 0.0868  -0.0154 21  MET B CG  
1789 S SD  . MET B 19  ? 0.7416 0.4537 0.5985 -0.0433 0.1041  0.0021  21  MET B SD  
1790 C CE  . MET B 19  ? 0.7937 0.5335 0.6775 -0.0398 0.0995  -0.0001 21  MET B CE  
1791 N N   . ALA B 20  ? 0.8617 0.4703 0.6176 -0.0824 0.0941  -0.0265 22  ALA B N   
1792 C CA  . ALA B 20  ? 0.9025 0.4773 0.6286 -0.0934 0.1049  -0.0318 22  ALA B CA  
1793 C C   . ALA B 20  ? 0.9452 0.5034 0.6529 -0.0905 0.1208  -0.0230 22  ALA B C   
1794 O O   . ALA B 20  ? 0.9707 0.5070 0.6675 -0.0948 0.1430  -0.0236 22  ALA B O   
1795 C CB  . ALA B 20  ? 0.9124 0.4728 0.6145 -0.1044 0.0811  -0.0437 22  ALA B CB  
1796 N N   . CYS B 21  ? 0.9472 0.5158 0.6534 -0.0837 0.1114  -0.0160 23  CYS B N   
1797 C CA  . CYS B 21  ? 0.9691 0.5272 0.6637 -0.0812 0.1267  -0.0088 23  CYS B CA  
1798 C C   . CYS B 21  ? 0.9592 0.5338 0.6822 -0.0695 0.1495  0.0017  23  CYS B C   
1799 O O   . CYS B 21  ? 0.9605 0.5291 0.6800 -0.0671 0.1642  0.0064  23  CYS B O   
1800 C CB  . CYS B 21  ? 0.9906 0.5541 0.6750 -0.0793 0.1091  -0.0060 23  CYS B CB  
1801 S SG  . CYS B 21  ? 1.0687 0.6075 0.7148 -0.0905 0.0808  -0.0159 23  CYS B SG  
1802 N N   . ARG B 22  ? 0.9525 0.5467 0.7026 -0.0622 0.1523  0.0051  24  ARG B N   
1803 C CA  . ARG B 22  ? 0.9597 0.5681 0.7342 -0.0496 0.1704  0.0162  24  ARG B CA  
1804 C C   . ARG B 22  ? 1.0219 0.6058 0.7918 -0.0516 0.1954  0.0153  24  ARG B C   
1805 O O   . ARG B 22  ? 1.0472 0.6124 0.8052 -0.0620 0.1975  0.0061  24  ARG B O   
1806 C CB  . ARG B 22  ? 0.9280 0.5615 0.7264 -0.0426 0.1628  0.0198  24  ARG B CB  
1807 C CG  . ARG B 22  ? 0.9170 0.5614 0.7360 -0.0299 0.1787  0.0315  24  ARG B CG  
1808 C CD  . ARG B 22  ? 0.9147 0.5744 0.7480 -0.0283 0.1722  0.0313  24  ARG B CD  
1809 N NE  . ARG B 22  ? 0.9121 0.5896 0.7621 -0.0145 0.1777  0.0445  24  ARG B NE  
1810 C CZ  . ARG B 22  ? 0.9280 0.6248 0.7896 -0.0107 0.1698  0.0473  24  ARG B CZ  
1811 N NH1 . ARG B 22  ? 0.9281 0.6318 0.7916 -0.0192 0.1569  0.0369  24  ARG B NH1 
1812 N NH2 . ARG B 22  ? 0.9224 0.6319 0.7938 0.0017  0.1745  0.0600  24  ARG B NH2 
1813 N N   . GLY B 23  ? 1.0361 0.6207 0.8171 -0.0417 0.2140  0.0240  25  GLY B N   
1814 C CA  . GLY B 23  ? 1.0629 0.6233 0.8420 -0.0413 0.2397  0.0238  25  GLY B CA  
1815 C C   . GLY B 23  ? 1.0784 0.6389 0.8713 -0.0360 0.2482  0.0277  25  GLY B C   
1816 O O   . GLY B 23  ? 1.0743 0.6586 0.8857 -0.0263 0.2400  0.0358  25  GLY B O   
1817 N N   . LYS B 34  ? 1.1706 0.5421 0.6320 -0.1412 0.1761  -0.0160 36  LYS B N   
1818 C CA  . LYS B 34  ? 1.1349 0.5541 0.6439 -0.1254 0.1601  -0.0087 36  LYS B CA  
1819 C C   . LYS B 34  ? 1.1171 0.5341 0.6088 -0.1241 0.1272  -0.0075 36  LYS B C   
1820 O O   . LYS B 34  ? 1.1485 0.5301 0.5940 -0.1340 0.1188  -0.0096 36  LYS B O   
1821 C CB  . LYS B 34  ? 1.1423 0.5915 0.6869 -0.1187 0.1759  -0.0035 36  LYS B CB  
1822 C CG  . LYS B 34  ? 1.2006 0.6707 0.7842 -0.1114 0.2021  -0.0022 36  LYS B CG  
1823 C CD  . LYS B 34  ? 1.2472 0.7473 0.8654 -0.1055 0.2153  0.0017  36  LYS B CD  
1824 C CE  . LYS B 34  ? 1.2925 0.8194 0.9563 -0.0936 0.2355  0.0049  36  LYS B CE  
1825 N NZ  . LYS B 34  ? 1.3163 0.8725 1.0147 -0.0886 0.2485  0.0071  36  LYS B NZ  
1826 N N   . HIS B 35  ? 1.0784 0.5312 0.6063 -0.1117 0.1093  -0.0041 37  HIS B N   
1827 C CA  . HIS B 35  ? 1.0725 0.5280 0.5930 -0.1080 0.0776  -0.0041 37  HIS B CA  
1828 C C   . HIS B 35  ? 1.0439 0.5227 0.5831 -0.1006 0.0706  0.0017  37  HIS B C   
1829 O O   . HIS B 35  ? 1.0164 0.5350 0.5998 -0.0899 0.0733  0.0059  37  HIS B O   
1830 C CB  . HIS B 35  ? 1.0714 0.5501 0.6198 -0.1009 0.0643  -0.0063 37  HIS B CB  
1831 C CG  . HIS B 35  ? 1.1378 0.5894 0.6612 -0.1105 0.0653  -0.0140 37  HIS B CG  
1832 N ND1 . HIS B 35  ? 1.1683 0.6181 0.7016 -0.1133 0.0901  -0.0158 37  HIS B ND1 
1833 C CD2 . HIS B 35  ? 1.1769 0.6013 0.6649 -0.1179 0.0440  -0.0203 37  HIS B CD2 
1834 C CE1 . HIS B 35  ? 1.1919 0.6138 0.6955 -0.1236 0.0844  -0.0240 37  HIS B CE1 
1835 N NE2 . HIS B 35  ? 1.2048 0.6116 0.6803 -0.1268 0.0560  -0.0270 37  HIS B NE2 
1836 N N   . PRO B 36  ? 1.0408 0.4929 0.5443 -0.1066 0.0615  0.0019  38  PRO B N   
1837 C CA  . PRO B 36  ? 1.0003 0.4713 0.5194 -0.1016 0.0583  0.0065  38  PRO B CA  
1838 C C   . PRO B 36  ? 0.9477 0.4495 0.4965 -0.0893 0.0353  0.0084  38  PRO B C   
1839 O O   . PRO B 36  ? 0.9572 0.4523 0.4982 -0.0864 0.0136  0.0056  38  PRO B O   
1840 C CB  . PRO B 36  ? 1.0540 0.4799 0.5198 -0.1122 0.0528  0.0055  38  PRO B CB  
1841 C CG  . PRO B 36  ? 1.0934 0.4816 0.5175 -0.1185 0.0403  0.0014  38  PRO B CG  
1842 C CD  . PRO B 36  ? 1.0765 0.4772 0.5205 -0.1186 0.0536  -0.0018 38  PRO B CD  
1843 N N   . LEU B 37  ? 0.8848 0.4213 0.4687 -0.0822 0.0404  0.0124  39  LEU B N   
1844 C CA  . LEU B 37  ? 0.8294 0.3927 0.4383 -0.0719 0.0214  0.0137  39  LEU B CA  
1845 C C   . LEU B 37  ? 0.8388 0.3805 0.4205 -0.0742 0.0070  0.0139  39  LEU B C   
1846 O O   . LEU B 37  ? 0.8648 0.3809 0.4177 -0.0835 0.0172  0.0143  39  LEU B O   
1847 C CB  . LEU B 37  ? 0.7744 0.3817 0.4286 -0.0643 0.0332  0.0178  39  LEU B CB  
1848 C CG  . LEU B 37  ? 0.7397 0.3669 0.4209 -0.0599 0.0466  0.0191  39  LEU B CG  
1849 C CD1 . LEU B 37  ? 0.7166 0.3844 0.4378 -0.0515 0.0564  0.0247  39  LEU B CD1 
1850 C CD2 . LEU B 37  ? 0.7314 0.3602 0.4186 -0.0561 0.0330  0.0155  39  LEU B CD2 
1851 N N   . GLN B 38  ? 0.8139 0.3641 0.4046 -0.0659 -0.0153 0.0129  40  GLN B N   
1852 C CA  . GLN B 38  ? 0.8114 0.3443 0.3824 -0.0651 -0.0295 0.0135  40  GLN B CA  
1853 C C   . GLN B 38  ? 0.7897 0.3374 0.3722 -0.0678 -0.0152 0.0160  40  GLN B C   
1854 O O   . GLN B 38  ? 0.8242 0.3443 0.3767 -0.0744 -0.0147 0.0165  40  GLN B O   
1855 C CB  . GLN B 38  ? 0.8281 0.3782 0.4210 -0.0532 -0.0529 0.0111  40  GLN B CB  
1856 C CG  . GLN B 38  ? 0.8853 0.4184 0.4623 -0.0498 -0.0686 0.0115  40  GLN B CG  
1857 C CD  . GLN B 38  ? 0.9754 0.4576 0.5006 -0.0540 -0.0829 0.0118  40  GLN B CD  
1858 O OE1 . GLN B 38  ? 0.9860 0.4457 0.4864 -0.0593 -0.0848 0.0107  40  GLN B OE1 
1859 N NE2 . GLN B 38  ? 0.9904 0.4505 0.4953 -0.0521 -0.0932 0.0133  40  GLN B NE2 
1860 N N   . ASN B 39  ? 0.7358 0.3256 0.3601 -0.0631 -0.0037 0.0175  41  ASN B N   
1861 C CA  . ASN B 39  ? 0.6926 0.3039 0.3340 -0.0653 0.0086  0.0192  41  ASN B CA  
1862 C C   . ASN B 39  ? 0.6571 0.2911 0.3212 -0.0673 0.0310  0.0212  41  ASN B C   
1863 O O   . ASN B 39  ? 0.6498 0.2925 0.3268 -0.0635 0.0360  0.0221  41  ASN B O   
1864 C CB  . ASN B 39  ? 0.6774 0.3216 0.3502 -0.0556 -0.0022 0.0193  41  ASN B CB  
1865 C CG  . ASN B 39  ? 0.7270 0.3531 0.3831 -0.0537 -0.0197 0.0170  41  ASN B CG  
1866 O OD1 . ASN B 39  ? 0.7689 0.3779 0.4056 -0.0604 -0.0167 0.0168  41  ASN B OD1 
1867 N ND2 . ASN B 39  ? 0.7270 0.3556 0.3912 -0.0447 -0.0375 0.0148  41  ASN B ND2 
1868 N N   . ARG B 40  ? 0.6304 0.2737 0.3003 -0.0734 0.0444  0.0213  42  ARG B N   
1869 C CA  A ARG B 40  ? 0.6051 0.2811 0.3080 -0.0718 0.0621  0.0233  42  ARG B CA  
1870 C CA  B ARG B 40  ? 0.6101 0.2859 0.3130 -0.0717 0.0620  0.0233  42  ARG B CA  
1871 C C   . ARG B 40  ? 0.5653 0.2839 0.3051 -0.0616 0.0546  0.0262  42  ARG B C   
1872 O O   . ARG B 40  ? 0.5611 0.2841 0.2996 -0.0611 0.0428  0.0248  42  ARG B O   
1873 C CB  A ARG B 40  ? 0.6205 0.2900 0.3164 -0.0835 0.0787  0.0205  42  ARG B CB  
1874 C CB  B ARG B 40  ? 0.6392 0.3083 0.3352 -0.0833 0.0794  0.0206  42  ARG B CB  
1875 C CG  A ARG B 40  ? 0.6038 0.3062 0.3355 -0.0819 0.0972  0.0214  42  ARG B CG  
1876 C CG  B ARG B 40  ? 0.6514 0.3519 0.3824 -0.0813 0.0979  0.0217  42  ARG B CG  
1877 C CD  A ARG B 40  ? 0.6170 0.2956 0.3306 -0.0957 0.1177  0.0164  42  ARG B CD  
1878 C CD  B ARG B 40  ? 0.6986 0.3777 0.4135 -0.0951 0.1185  0.0167  42  ARG B CD  
1879 N NE  A ARG B 40  ? 0.5719 0.2812 0.3224 -0.0945 0.1369  0.0157  42  ARG B NE  
1880 N NE  B ARG B 40  ? 0.6913 0.4041 0.4453 -0.0932 0.1365  0.0162  42  ARG B NE  
1881 C CZ  A ARG B 40  ? 0.4962 0.2350 0.2739 -0.0979 0.1445  0.0129  42  ARG B CZ  
1882 C CZ  B ARG B 40  ? 0.6744 0.3911 0.4430 -0.0891 0.1514  0.0171  42  ARG B CZ  
1883 N NH1 A ARG B 40  ? 0.4234 0.1634 0.1933 -0.1047 0.1361  0.0101  42  ARG B NH1 
1884 N NH1 B ARG B 40  ? 0.6340 0.3214 0.3789 -0.0881 0.1516  0.0181  42  ARG B NH1 
1885 N NH2 A ARG B 40  ? 0.4712 0.2380 0.2848 -0.0948 0.1605  0.0121  42  ARG B NH2 
1886 N NH2 B ARG B 40  ? 0.6633 0.4133 0.4713 -0.0858 0.1658  0.0166  42  ARG B NH2 
1887 N N   . TRP B 41  ? 0.5275 0.2743 0.2970 -0.0537 0.0620  0.0302  43  TRP B N   
1888 C CA  . TRP B 41  ? 0.5002 0.2838 0.3000 -0.0437 0.0556  0.0339  43  TRP B CA  
1889 C C   . TRP B 41  ? 0.5022 0.3172 0.3307 -0.0411 0.0680  0.0374  43  TRP B C   
1890 O O   . TRP B 41  ? 0.4981 0.3092 0.3306 -0.0429 0.0829  0.0378  43  TRP B O   
1891 C CB  . TRP B 41  ? 0.4754 0.2608 0.2821 -0.0350 0.0500  0.0363  43  TRP B CB  
1892 C CG  . TRP B 41  ? 0.4835 0.2450 0.2696 -0.0362 0.0355  0.0318  43  TRP B CG  
1893 C CD1 . TRP B 41  ? 0.5187 0.2476 0.2793 -0.0411 0.0338  0.0287  43  TRP B CD1 
1894 C CD2 . TRP B 41  ? 0.4814 0.2495 0.2707 -0.0325 0.0196  0.0293  43  TRP B CD2 
1895 N NE1 . TRP B 41  ? 0.5260 0.2419 0.2747 -0.0397 0.0157  0.0247  43  TRP B NE1 
1896 C CE2 . TRP B 41  ? 0.5071 0.2474 0.2755 -0.0340 0.0078  0.0248  43  TRP B CE2 
1897 C CE3 . TRP B 41  ? 0.4656 0.2605 0.2739 -0.0277 0.0144  0.0299  43  TRP B CE3 
1898 C CZ2 . TRP B 41  ? 0.5248 0.2648 0.2948 -0.0297 -0.0088 0.0207  43  TRP B CZ2 
1899 C CZ3 . TRP B 41  ? 0.4771 0.2694 0.2843 -0.0249 0.0005  0.0254  43  TRP B CZ3 
1900 C CH2 . TRP B 41  ? 0.4993 0.2653 0.2898 -0.0253 -0.0110 0.0207  43  TRP B CH2 
1901 N N   . ALA B 42  ? 0.5065 0.3530 0.3553 -0.0366 0.0613  0.0394  44  ALA B N   
1902 C CA  . ALA B 42  ? 0.5060 0.3863 0.3839 -0.0325 0.0682  0.0430  44  ALA B CA  
1903 C C   . ALA B 42  ? 0.4971 0.4018 0.3929 -0.0202 0.0613  0.0500  44  ALA B C   
1904 O O   . ALA B 42  ? 0.4953 0.4037 0.3860 -0.0190 0.0495  0.0493  44  ALA B O   
1905 C CB  . ALA B 42  ? 0.5106 0.4048 0.3921 -0.0410 0.0660  0.0381  44  ALA B CB  
1906 N N   . LEU B 43  ? 0.4944 0.4128 0.4094 -0.0110 0.0696  0.0565  45  LEU B N   
1907 C CA  . LEU B 43  ? 0.4928 0.4310 0.4220 0.0009  0.0652  0.0646  45  LEU B CA  
1908 C C   . LEU B 43  ? 0.5019 0.4752 0.4527 0.0045  0.0608  0.0676  45  LEU B C   
1909 O O   . LEU B 43  ? 0.4951 0.4815 0.4634 0.0042  0.0683  0.0669  45  LEU B O   
1910 C CB  . LEU B 43  ? 0.4877 0.4173 0.4237 0.0096  0.0768  0.0707  45  LEU B CB  
1911 C CG  . LEU B 43  ? 0.4640 0.4098 0.4123 0.0229  0.0745  0.0809  45  LEU B CG  
1912 C CD1 . LEU B 43  ? 0.4684 0.4098 0.4034 0.0226  0.0647  0.0807  45  LEU B CD1 
1913 C CD2 . LEU B 43  ? 0.4766 0.4101 0.4313 0.0309  0.0884  0.0864  45  LEU B CD2 
1914 N N   . TRP B 44  ? 0.5214 0.5099 0.4711 0.0073  0.0487  0.0698  46  TRP B N   
1915 C CA  . TRP B 44  ? 0.5334 0.5547 0.4982 0.0098  0.0403  0.0722  46  TRP B CA  
1916 C C   . TRP B 44  ? 0.5720 0.6051 0.5407 0.0227  0.0354  0.0828  46  TRP B C   
1917 O O   . TRP B 44  ? 0.5660 0.5818 0.5210 0.0260  0.0363  0.0857  46  TRP B O   
1918 C CB  . TRP B 44  ? 0.5316 0.5561 0.4841 -0.0004 0.0299  0.0646  46  TRP B CB  
1919 C CG  . TRP B 44  ? 0.5528 0.5588 0.4937 -0.0135 0.0334  0.0547  46  TRP B CG  
1920 C CD1 . TRP B 44  ? 0.5837 0.5570 0.5033 -0.0184 0.0352  0.0503  46  TRP B CD1 
1921 C CD2 . TRP B 44  ? 0.5562 0.5737 0.5047 -0.0238 0.0354  0.0478  46  TRP B CD2 
1922 N NE1 . TRP B 44  ? 0.5957 0.5557 0.5052 -0.0303 0.0381  0.0425  46  TRP B NE1 
1923 C CE2 . TRP B 44  ? 0.5817 0.5679 0.5086 -0.0348 0.0396  0.0403  46  TRP B CE2 
1924 C CE3 . TRP B 44  ? 0.5552 0.6068 0.5270 -0.0251 0.0334  0.0467  46  TRP B CE3 
1925 C CZ2 . TRP B 44  ? 0.6014 0.5858 0.5264 -0.0480 0.0444  0.0320  46  TRP B CZ2 
1926 C CZ3 . TRP B 44  ? 0.5774 0.6314 0.5522 -0.0389 0.0383  0.0371  46  TRP B CZ3 
1927 C CH2 . TRP B 44  ? 0.5959 0.6149 0.5458 -0.0506 0.0447  0.0300  46  TRP B CH2 
1928 N N   . PHE B 45  ? 0.6073 0.6699 0.5948 0.0296  0.0300  0.0882  47  PHE B N   
1929 C CA  . PHE B 45  ? 0.6536 0.7289 0.6423 0.0421  0.0227  0.0993  47  PHE B CA  
1930 C C   . PHE B 45  ? 0.6842 0.7873 0.6748 0.0383  0.0079  0.0972  47  PHE B C   
1931 O O   . PHE B 45  ? 0.6558 0.7790 0.6625 0.0314  0.0054  0.0902  47  PHE B O   
1932 C CB  . PHE B 45  ? 0.6663 0.7512 0.6776 0.0560  0.0286  0.1084  47  PHE B CB  
1933 C CG  . PHE B 45  ? 0.6983 0.7924 0.7088 0.0710  0.0208  0.1218  47  PHE B CG  
1934 C CD1 . PHE B 45  ? 0.7423 0.8123 0.7301 0.0755  0.0238  0.1287  47  PHE B CD1 
1935 C CD2 . PHE B 45  ? 0.6997 0.8257 0.7319 0.0804  0.0103  0.1274  47  PHE B CD2 
1936 C CE1 . PHE B 45  ? 0.7545 0.8274 0.7358 0.0888  0.0176  0.1419  47  PHE B CE1 
1937 C CE2 . PHE B 45  ? 0.7162 0.8468 0.7429 0.0953  0.0013  0.1412  47  PHE B CE2 
1938 C CZ  . PHE B 45  ? 0.7364 0.8381 0.7352 0.0991  0.0056  0.1489  47  PHE B CZ  
1939 N N   . PHE B 46  ? 0.7454 0.8488 0.7186 0.0413  -0.0009 0.1023  48  PHE B N   
1940 C CA  . PHE B 46  ? 0.8105 0.9378 0.7800 0.0373  -0.0157 0.1005  48  PHE B CA  
1941 C C   . PHE B 46  ? 0.8708 1.0014 0.8270 0.0485  -0.0240 0.1128  48  PHE B C   
1942 O O   . PHE B 46  ? 0.8856 0.9935 0.8186 0.0488  -0.0199 0.1155  48  PHE B O   
1943 C CB  . PHE B 46  ? 0.8381 0.9537 0.7881 0.0226  -0.0171 0.0889  48  PHE B CB  
1944 C CG  . PHE B 46  ? 0.8709 1.0079 0.8151 0.0149  -0.0303 0.0839  48  PHE B CG  
1945 C CD1 . PHE B 46  ? 0.9092 1.0443 0.8312 0.0161  -0.0374 0.0875  48  PHE B CD1 
1946 C CD2 . PHE B 46  ? 0.8787 1.0348 0.8371 0.0047  -0.0340 0.0744  48  PHE B CD2 
1947 C CE1 . PHE B 46  ? 0.9214 1.0741 0.8348 0.0074  -0.0492 0.0817  48  PHE B CE1 
1948 C CE2 . PHE B 46  ? 0.8927 1.0678 0.8450 -0.0041 -0.0458 0.0685  48  PHE B CE2 
1949 C CZ  . PHE B 46  ? 0.9044 1.0775 0.8335 -0.0026 -0.0538 0.0721  48  PHE B CZ  
1950 N N   . LYS B 47  ? 0.9035 1.0618 0.8740 0.0575  -0.0358 0.1200  49  LYS B N   
1951 C CA  . LYS B 47  ? 0.9530 1.1143 0.9051 0.0673  -0.0474 0.1320  49  LYS B CA  
1952 C C   . LYS B 47  ? 0.9953 1.1742 0.9324 0.0565  -0.0626 0.1256  49  LYS B C   
1953 O O   . LYS B 47  ? 0.9836 1.1883 0.9396 0.0483  -0.0695 0.1162  49  LYS B O   
1954 C CB  . LYS B 47  ? 0.9559 1.1360 0.9307 0.0851  -0.0541 0.1443  49  LYS B CB  
1955 C CG  . LYS B 47  ? 1.0342 1.2101 0.9861 0.0980  -0.0657 0.1596  49  LYS B CG  
1956 C CD  . LYS B 47  ? 1.0868 1.2695 1.0599 0.1199  -0.0683 0.1743  49  LYS B CD  
1957 C CE  . LYS B 47  ? 1.0964 1.3231 1.1083 0.1265  -0.0836 0.1731  49  LYS B CE  
1958 N NZ  . LYS B 47  ? 1.1102 1.3582 1.1096 0.1325  -0.1087 0.1806  49  LYS B NZ  
1959 N N   . ASN B 48  ? 1.0394 1.2033 0.9420 0.0549  -0.0664 0.1293  50  ASN B N   
1960 C CA  . ASN B 48  ? 1.0676 1.2470 0.9527 0.0451  -0.0811 0.1238  50  ASN B CA  
1961 C C   . ASN B 48  ? 1.0754 1.2854 0.9687 0.0552  -0.1016 0.1331  50  ASN B C   
1962 O O   . ASN B 48  ? 1.0894 1.2905 0.9599 0.0660  -0.1087 0.1465  50  ASN B O   
1963 C CB  . ASN B 48  ? 1.1046 1.2567 0.9485 0.0395  -0.0769 0.1242  50  ASN B CB  
1964 C CG  . ASN B 48  ? 1.1470 1.3116 0.9682 0.0285  -0.0907 0.1181  50  ASN B CG  
1965 O OD1 . ASN B 48  ? 1.1407 1.3299 0.9763 0.0188  -0.0996 0.1075  50  ASN B OD1 
1966 N ND2 . ASN B 48  ? 1.1747 1.3206 0.9577 0.0284  -0.0915 0.1237  50  ASN B ND2 
1967 N N   . ASP B 49  ? 1.0632 1.3085 0.9886 0.0516  -0.1111 0.1256  51  ASP B N   
1968 C CA  . ASP B 49  ? 1.0613 1.3422 1.0005 0.0600  -0.1333 0.1315  51  ASP B CA  
1969 C C   . ASP B 49  ? 1.0590 1.3720 1.0076 0.0431  -0.1462 0.1162  51  ASP B C   
1970 O O   . ASP B 49  ? 1.0325 1.3583 1.0080 0.0319  -0.1386 0.1029  51  ASP B O   
1971 C CB  . ASP B 49  ? 1.0567 1.3550 1.0371 0.0774  -0.1329 0.1396  51  ASP B CB  
1972 C CG  . ASP B 49  ? 1.0772 1.4113 1.0747 0.0910  -0.1571 0.1482  51  ASP B CG  
1973 O OD1 . ASP B 49  ? 1.0798 1.4202 1.0491 0.0886  -0.1759 0.1511  51  ASP B OD1 
1974 O OD2 . ASP B 49  ? 1.0843 1.4398 1.1234 0.1041  -0.1577 0.1517  51  ASP B OD2 
1975 N N   . LYS B 50  ? 1.0835 1.4070 1.0066 0.0406  -0.1654 0.1183  52  LYS B N   
1976 C CA  . LYS B 50  ? 1.0946 1.4429 1.0166 0.0223  -0.1775 0.1033  52  LYS B CA  
1977 C C   . LYS B 50  ? 1.0795 1.4782 1.0458 0.0252  -0.1952 0.0998  52  LYS B C   
1978 O O   . LYS B 50  ? 1.0660 1.4883 1.0477 0.0078  -0.1985 0.0834  52  LYS B O   
1979 C CB  . LYS B 50  ? 1.1301 1.4643 1.0008 0.0161  -0.1890 0.1055  52  LYS B CB  
1980 C CG  . LYS B 50  ? 1.1878 1.4805 1.0218 0.0042  -0.1698 0.0994  52  LYS B CG  
1981 C CD  . LYS B 50  ? 1.2318 1.5299 1.0678 -0.0180 -0.1651 0.0790  52  LYS B CD  
1982 C CE  . LYS B 50  ? 1.2999 1.5594 1.1060 -0.0281 -0.1465 0.0720  52  LYS B CE  
1983 N NZ  . LYS B 50  ? 1.3348 1.5975 1.1333 -0.0492 -0.1457 0.0533  52  LYS B NZ  
1984 N N   . SER B 51  ? 1.0761 1.4915 1.0651 0.0471  -0.2059 0.1144  53  SER B N   
1985 C CA  . SER B 51  ? 1.0568 1.5224 1.0980 0.0522  -0.2203 0.1103  53  SER B CA  
1986 C C   . SER B 51  ? 1.0589 1.5346 1.1464 0.0459  -0.1998 0.0981  53  SER B C   
1987 O O   . SER B 51  ? 1.0306 1.5480 1.1666 0.0491  -0.2073 0.0928  53  SER B O   
1988 C CB  . SER B 51  ? 1.0581 1.5362 1.1118 0.0795  -0.2370 0.1295  53  SER B CB  
1989 O OG  . SER B 51  ? 1.0836 1.5385 1.1505 0.0960  -0.2186 0.1404  53  SER B OG  
1990 N N   . LYS B 52  ? 1.0878 1.5258 1.1605 0.0368  -0.1742 0.0934  54  LYS B N   
1991 C CA  . LYS B 52  ? 1.0921 1.5305 1.1982 0.0299  -0.1535 0.0828  54  LYS B CA  
1992 C C   . LYS B 52  ? 1.1152 1.5305 1.2013 0.0060  -0.1381 0.0670  54  LYS B C   
1993 O O   . LYS B 52  ? 1.1098 1.5334 1.2221 -0.0053 -0.1259 0.0545  54  LYS B O   
1994 C CB  . LYS B 52  ? 1.1279 1.5408 1.2406 0.0478  -0.1375 0.0956  54  LYS B CB  
1995 C CG  . LYS B 52  ? 1.1675 1.6083 1.3163 0.0707  -0.1481 0.1074  54  LYS B CG  
1996 C CD  . LYS B 52  ? 1.2450 1.6544 1.3907 0.0892  -0.1335 0.1217  54  LYS B CD  
1997 C CE  . LYS B 52  ? 1.3060 1.7063 1.4791 0.0852  -0.1086 0.1138  54  LYS B CE  
1998 N NZ  . LYS B 52  ? 1.3637 1.7317 1.5309 0.1020  -0.0943 0.1270  54  LYS B NZ  
1999 N N   . THR B 53  ? 1.1377 1.5229 1.1778 -0.0016 -0.1378 0.0670  55  THR B N   
2000 C CA  . THR B 53  ? 1.1555 1.5159 1.1744 -0.0218 -0.1248 0.0529  55  THR B CA  
2001 C C   . THR B 53  ? 1.1635 1.4930 1.1875 -0.0228 -0.1015 0.0508  55  THR B C   
2002 O O   . THR B 53  ? 1.1552 1.4900 1.2069 -0.0127 -0.0938 0.0557  55  THR B O   
2003 C CB  . THR B 53  ? 1.1582 1.5463 1.1888 -0.0422 -0.1319 0.0355  55  THR B CB  
2004 O OG1 . THR B 53  ? 1.1535 1.5550 1.2210 -0.0490 -0.1201 0.0259  55  THR B OG1 
2005 C CG2 . THR B 53  ? 1.1467 1.5744 1.1826 -0.0403 -0.1575 0.0368  55  THR B CG2 
2006 N N   . TRP B 54  ? 1.1761 1.4726 1.1721 -0.0350 -0.0909 0.0432  56  TRP B N   
2007 C CA  . TRP B 54  ? 1.1882 1.4482 1.1772 -0.0351 -0.0723 0.0426  56  TRP B CA  
2008 C C   . TRP B 54  ? 1.1442 1.4069 1.1619 -0.0370 -0.0595 0.0384  56  TRP B C   
2009 O O   . TRP B 54  ? 1.1558 1.3903 1.1687 -0.0323 -0.0463 0.0419  56  TRP B O   
2010 C CB  . TRP B 54  ? 1.2250 1.4567 1.1851 -0.0499 -0.0667 0.0317  56  TRP B CB  
2011 C CG  . TRP B 54  ? 1.2506 1.4928 1.2173 -0.0686 -0.0662 0.0164  56  TRP B CG  
2012 C CD1 . TRP B 54  ? 1.2653 1.5292 1.2281 -0.0802 -0.0775 0.0080  56  TRP B CD1 
2013 C CD2 . TRP B 54  ? 1.2627 1.4921 1.2389 -0.0790 -0.0527 0.0073  56  TRP B CD2 
2014 N NE1 . TRP B 54  ? 1.2690 1.5351 1.2405 -0.0976 -0.0711 -0.0064 56  TRP B NE1 
2015 C CE2 . TRP B 54  ? 1.2712 1.5151 1.2499 -0.0971 -0.0555 -0.0066 56  TRP B CE2 
2016 C CE3 . TRP B 54  ? 1.2795 1.4848 1.2598 -0.0758 -0.0382 0.0093  56  TRP B CE3 
2017 C CZ2 . TRP B 54  ? 1.2839 1.5168 1.2682 -0.1118 -0.0431 -0.0179 56  TRP B CZ2 
2018 C CZ3 . TRP B 54  ? 1.2958 1.4896 1.2793 -0.0900 -0.0270 -0.0014 56  TRP B CZ3 
2019 C CH2 . TRP B 54  ? 1.2949 1.5016 1.2801 -0.1077 -0.0289 -0.0146 56  TRP B CH2 
2020 N N   . GLN B 55  ? 1.0927 1.3878 1.1393 -0.0450 -0.0624 0.0300  57  GLN B N   
2021 C CA  . GLN B 55  ? 1.0584 1.3566 1.1329 -0.0482 -0.0479 0.0248  57  GLN B CA  
2022 C C   . GLN B 55  ? 1.0032 1.3134 1.1038 -0.0287 -0.0459 0.0369  57  GLN B C   
2023 O O   . GLN B 55  ? 1.0059 1.2949 1.1109 -0.0255 -0.0297 0.0384  57  GLN B O   
2024 C CB  . GLN B 55  ? 1.0697 1.4011 1.1703 -0.0645 -0.0499 0.0102  57  GLN B CB  
2025 C CG  . GLN B 55  ? 1.1124 1.4532 1.2476 -0.0677 -0.0337 0.0042  57  GLN B CG  
2026 C CD  . GLN B 55  ? 1.1560 1.5229 1.3133 -0.0878 -0.0314 -0.0129 57  GLN B CD  
2027 O OE1 . GLN B 55  ? 1.1338 1.5460 1.3337 -0.0861 -0.0371 -0.0168 57  GLN B OE1 
2028 N NE2 . GLN B 55  ? 1.1873 1.5258 1.3174 -0.1070 -0.0227 -0.0237 57  GLN B NE2 
2029 N N   . ALA B 56  ? 0.9521 1.2944 1.0686 -0.0156 -0.0625 0.0452  58  ALA B N   
2030 C CA  . ALA B 56  ? 0.9102 1.2652 1.0538 0.0045  -0.0618 0.0568  58  ALA B CA  
2031 C C   . ALA B 56  ? 0.8915 1.2123 1.0087 0.0198  -0.0579 0.0718  58  ALA B C   
2032 O O   . ALA B 56  ? 0.8907 1.2067 1.0246 0.0337  -0.0492 0.0797  58  ALA B O   
2033 C CB  . ALA B 56  ? 0.8878 1.2898 1.0592 0.0141  -0.0829 0.0605  58  ALA B CB  
2034 N N   . ASN B 57  ? 0.8711 1.1679 0.9485 0.0166  -0.0628 0.0746  59  ASN B N   
2035 C CA  . ASN B 57  ? 0.8599 1.1243 0.9122 0.0286  -0.0579 0.0870  59  ASN B CA  
2036 C C   . ASN B 57  ? 0.8355 1.0647 0.8800 0.0243  -0.0381 0.0836  59  ASN B C   
2037 O O   . ASN B 57  ? 0.8534 1.0635 0.8955 0.0363  -0.0298 0.0929  59  ASN B O   
2038 C CB  . ASN B 57  ? 0.8841 1.1350 0.8986 0.0246  -0.0671 0.0888  59  ASN B CB  
2039 C CG  . ASN B 57  ? 0.9029 1.1807 0.9146 0.0307  -0.0876 0.0951  59  ASN B CG  
2040 O OD1 . ASN B 57  ? 0.8903 1.1931 0.9262 0.0443  -0.0967 0.1033  59  ASN B OD1 
2041 N ND2 . ASN B 57  ? 0.9228 1.1948 0.9038 0.0211  -0.0956 0.0914  59  ASN B ND2 
2042 N N   . LEU B 58  ? 0.7971 1.0156 0.8352 0.0074  -0.0312 0.0704  60  LEU B N   
2043 C CA  . LEU B 58  ? 0.7809 0.9644 0.8073 0.0027  -0.0154 0.0669  60  LEU B CA  
2044 C C   . LEU B 58  ? 0.7369 0.9255 0.7902 0.0049  -0.0030 0.0657  60  LEU B C   
2045 O O   . LEU B 58  ? 0.7253 0.9335 0.7984 -0.0046 -0.0011 0.0565  60  LEU B O   
2046 C CB  . LEU B 58  ? 0.7942 0.9609 0.8005 -0.0149 -0.0138 0.0544  60  LEU B CB  
2047 C CG  . LEU B 58  ? 0.8300 0.9577 0.8192 -0.0197 -0.0010 0.0509  60  LEU B CG  
2048 C CD1 . LEU B 58  ? 0.8530 0.9572 0.8270 -0.0083 0.0013  0.0599  60  LEU B CD1 
2049 C CD2 . LEU B 58  ? 0.8543 0.9650 0.8233 -0.0352 -0.0017 0.0394  60  LEU B CD2 
2050 N N   . ARG B 59  ? 0.7146 0.8860 0.7700 0.0170  0.0067  0.0742  61  ARG B N   
2051 C CA  . ARG B 59  ? 0.6868 0.8560 0.7642 0.0191  0.0221  0.0726  61  ARG B CA  
2052 C C   . ARG B 59  ? 0.6612 0.7875 0.7151 0.0142  0.0366  0.0706  61  ARG B C   
2053 O O   . ARG B 59  ? 0.6653 0.7689 0.6989 0.0205  0.0362  0.0771  61  ARG B O   
2054 C CB  . ARG B 59  ? 0.7274 0.9138 0.8300 0.0387  0.0215  0.0843  61  ARG B CB  
2055 C CG  . ARG B 59  ? 0.8142 1.0479 0.9530 0.0440  0.0098  0.0840  61  ARG B CG  
2056 C CD  . ARG B 59  ? 0.8926 1.1408 1.0556 0.0663  0.0073  0.0969  61  ARG B CD  
2057 N NE  . ARG B 59  ? 0.9680 1.2136 1.1103 0.0787  -0.0083 0.1103  61  ARG B NE  
2058 C CZ  . ARG B 59  ? 1.0066 1.2798 1.1492 0.0810  -0.0291 0.1131  61  ARG B CZ  
2059 N NH1 . ARG B 59  ? 1.0185 1.2824 1.1362 0.0917  -0.0407 0.1258  61  ARG B NH1 
2060 N NH2 . ARG B 59  ? 0.9976 1.3066 1.1637 0.0715  -0.0379 0.1026  61  ARG B NH2 
2061 N N   . LEU B 60  ? 0.6293 0.7442 0.6851 0.0022  0.0495  0.0608  62  LEU B N   
2062 C CA  . LEU B 60  ? 0.6198 0.6950 0.6549 -0.0022 0.0634  0.0587  62  LEU B CA  
2063 C C   . LEU B 60  ? 0.5952 0.6671 0.6467 0.0103  0.0756  0.0654  62  LEU B C   
2064 O O   . LEU B 60  ? 0.5846 0.6828 0.6689 0.0161  0.0805  0.0657  62  LEU B O   
2065 C CB  . LEU B 60  ? 0.6130 0.6750 0.6411 -0.0197 0.0736  0.0466  62  LEU B CB  
2066 C CG  . LEU B 60  ? 0.6468 0.6669 0.6507 -0.0259 0.0875  0.0437  62  LEU B CG  
2067 C CD1 . LEU B 60  ? 0.6636 0.6523 0.6325 -0.0272 0.0789  0.0452  62  LEU B CD1 
2068 C CD2 . LEU B 60  ? 0.6681 0.6779 0.6682 -0.0425 0.1002  0.0326  62  LEU B CD2 
2069 N N   . ILE B 61  ? 0.5860 0.6260 0.6163 0.0145  0.0808  0.0700  63  ILE B N   
2070 C CA  . ILE B 61  ? 0.5668 0.5983 0.6075 0.0267  0.0924  0.0769  63  ILE B CA  
2071 C C   . ILE B 61  ? 0.5534 0.5551 0.5834 0.0170  0.1105  0.0693  63  ILE B C   
2072 O O   . ILE B 61  ? 0.5435 0.5494 0.5945 0.0207  0.1252  0.0684  63  ILE B O   
2073 C CB  . ILE B 61  ? 0.5907 0.6063 0.6146 0.0366  0.0872  0.0863  63  ILE B CB  
2074 C CG1 . ILE B 61  ? 0.6094 0.6497 0.6373 0.0455  0.0703  0.0943  63  ILE B CG1 
2075 C CG2 . ILE B 61  ? 0.5974 0.5965 0.6276 0.0471  0.1021  0.0922  63  ILE B CG2 
2076 C CD1 . ILE B 61  ? 0.6155 0.6942 0.6740 0.0544  0.0634  0.0984  63  ILE B CD1 
2077 N N   . SER B 62  ? 0.5544 0.5249 0.5511 0.0048  0.1094  0.0635  64  SER B N   
2078 C CA  . SER B 62  ? 0.5558 0.4924 0.5339 -0.0054 0.1249  0.0568  64  SER B CA  
2079 C C   . SER B 62  ? 0.5386 0.4438 0.4786 -0.0179 0.1174  0.0512  64  SER B C   
2080 O O   . SER B 62  ? 0.5439 0.4508 0.4743 -0.0153 0.1023  0.0537  64  SER B O   
2081 C CB  . SER B 62  ? 0.5863 0.5054 0.5646 0.0037  0.1364  0.0619  64  SER B CB  
2082 O OG  . SER B 62  ? 0.6489 0.5327 0.6053 -0.0065 0.1511  0.0552  64  SER B OG  
2083 N N   . LYS B 63  ? 0.5211 0.3971 0.4394 -0.0308 0.1281  0.0436  65  LYS B N   
2084 C CA  . LYS B 63  ? 0.5381 0.3780 0.4168 -0.0414 0.1211  0.0390  65  LYS B CA  
2085 C C   . LYS B 63  ? 0.5774 0.3796 0.4314 -0.0447 0.1310  0.0374  65  LYS B C   
2086 O O   . LYS B 63  ? 0.5969 0.3975 0.4624 -0.0428 0.1481  0.0374  65  LYS B O   
2087 C CB  . LYS B 63  ? 0.5032 0.3346 0.3675 -0.0558 0.1221  0.0315  65  LYS B CB  
2088 C CG  . LYS B 63  ? 0.4861 0.3549 0.3756 -0.0550 0.1147  0.0311  65  LYS B CG  
2089 C CD  . LYS B 63  ? 0.5351 0.3880 0.4022 -0.0698 0.1123  0.0237  65  LYS B CD  
2090 C CE  . LYS B 63  ? 0.5313 0.4204 0.4222 -0.0712 0.1057  0.0217  65  LYS B CE  
2091 N NZ  . LYS B 63  ? 0.5866 0.4565 0.4554 -0.0876 0.1081  0.0134  65  LYS B NZ  
2092 N N   . PHE B 64  ? 0.5890 0.3615 0.4101 -0.0493 0.1195  0.0354  66  PHE B N   
2093 C CA  . PHE B 64  ? 0.6055 0.3424 0.4002 -0.0530 0.1246  0.0334  66  PHE B CA  
2094 C C   . PHE B 64  ? 0.6382 0.3439 0.3956 -0.0605 0.1092  0.0296  66  PHE B C   
2095 O O   . PHE B 64  ? 0.6459 0.3609 0.4036 -0.0583 0.0927  0.0301  66  PHE B O   
2096 C CB  . PHE B 64  ? 0.5942 0.3390 0.4047 -0.0419 0.1261  0.0383  66  PHE B CB  
2097 C CG  . PHE B 64  ? 0.5825 0.3441 0.4020 -0.0335 0.1077  0.0420  66  PHE B CG  
2098 C CD1 . PHE B 64  ? 0.6007 0.3422 0.3984 -0.0364 0.0938  0.0386  66  PHE B CD1 
2099 C CD2 . PHE B 64  ? 0.5584 0.3554 0.4073 -0.0235 0.1041  0.0480  66  PHE B CD2 
2100 C CE1 . PHE B 64  ? 0.5913 0.3492 0.3999 -0.0297 0.0791  0.0402  66  PHE B CE1 
2101 C CE2 . PHE B 64  ? 0.5701 0.3796 0.4242 -0.0176 0.0898  0.0503  66  PHE B CE2 
2102 C CZ  . PHE B 64  ? 0.5712 0.3614 0.4064 -0.0211 0.0785  0.0459  66  PHE B CZ  
2103 N N   . ASP B 65  ? 0.6726 0.3396 0.3963 -0.0691 0.1141  0.0256  67  ASP B N   
2104 C CA  . ASP B 65  ? 0.7067 0.3398 0.3912 -0.0754 0.0977  0.0224  67  ASP B CA  
2105 C C   . ASP B 65  ? 0.7174 0.3186 0.3756 -0.0791 0.0985  0.0196  67  ASP B C   
2106 O O   . ASP B 65  ? 0.7469 0.3123 0.3656 -0.0868 0.0888  0.0163  67  ASP B O   
2107 C CB  . ASP B 65  ? 0.7785 0.3884 0.4346 -0.0869 0.0993  0.0193  67  ASP B CB  
2108 C CG  . ASP B 65  ? 0.8890 0.4741 0.5257 -0.0992 0.1225  0.0154  67  ASP B CG  
2109 O OD1 . ASP B 65  ? 0.9023 0.5062 0.5662 -0.0967 0.1413  0.0155  67  ASP B OD1 
2110 O OD2 . ASP B 65  ? 0.9583 0.5036 0.5519 -0.1110 0.1222  0.0121  67  ASP B OD2 
2111 N N   . THR B 66  ? 0.7216 0.3342 0.4001 -0.0737 0.1091  0.0209  68  THR B N   
2112 C CA  . THR B 66  ? 0.7387 0.3267 0.3977 -0.0766 0.1076  0.0175  68  THR B CA  
2113 C C   . THR B 66  ? 0.7291 0.3440 0.4205 -0.0656 0.1039  0.0204  68  THR B C   
2114 O O   . THR B 66  ? 0.7143 0.3629 0.4407 -0.0560 0.1086  0.0259  68  THR B O   
2115 C CB  . THR B 66  ? 0.7429 0.3029 0.3824 -0.0860 0.1314  0.0138  68  THR B CB  
2116 O OG1 . THR B 66  ? 0.7442 0.3282 0.4197 -0.0784 0.1509  0.0170  68  THR B OG1 
2117 C CG2 . THR B 66  ? 0.7458 0.2822 0.3577 -0.0976 0.1412  0.0110  68  THR B CG2 
2118 N N   . VAL B 67  ? 0.7363 0.3349 0.4141 -0.0679 0.0954  0.0162  69  VAL B N   
2119 C CA  . VAL B 67  ? 0.7348 0.3517 0.4380 -0.0607 0.0944  0.0170  69  VAL B CA  
2120 C C   . VAL B 67  ? 0.7597 0.3841 0.4828 -0.0565 0.1190  0.0208  69  VAL B C   
2121 O O   . VAL B 67  ? 0.7432 0.3938 0.4967 -0.0465 0.1221  0.0262  69  VAL B O   
2122 C CB  . VAL B 67  ? 0.7476 0.3430 0.4307 -0.0669 0.0820  0.0094  69  VAL B CB  
2123 C CG1 . VAL B 67  ? 0.7440 0.3578 0.4548 -0.0614 0.0848  0.0091  69  VAL B CG1 
2124 C CG2 . VAL B 67  ? 0.7432 0.3324 0.4100 -0.0683 0.0554  0.0060  69  VAL B CG2 
2125 N N   . GLU B 68  ? 0.7910 0.3900 0.4954 -0.0641 0.1370  0.0180  70  GLU B N   
2126 C CA  . GLU B 68  ? 0.7979 0.3995 0.5204 -0.0596 0.1621  0.0207  70  GLU B CA  
2127 C C   . GLU B 68  ? 0.7677 0.4024 0.5252 -0.0485 0.1705  0.0287  70  GLU B C   
2128 O O   . GLU B 68  ? 0.7593 0.4108 0.5443 -0.0377 0.1810  0.0345  70  GLU B O   
2129 C CB  . GLU B 68  ? 0.8754 0.4400 0.5676 -0.0717 0.1803  0.0141  70  GLU B CB  
2130 C CG  . GLU B 68  ? 0.9618 0.4919 0.6190 -0.0830 0.1749  0.0059  70  GLU B CG  
2131 C CD  . GLU B 68  ? 1.0762 0.5902 0.7007 -0.0912 0.1492  0.0015  70  GLU B CD  
2132 O OE1 . GLU B 68  ? 1.1069 0.6253 0.7253 -0.0913 0.1401  0.0038  70  GLU B OE1 
2133 O OE2 . GLU B 68  ? 1.1095 0.6060 0.7146 -0.0973 0.1377  -0.0047 70  GLU B OE2 
2134 N N   . ASP B 69  ? 0.7553 0.3983 0.5106 -0.0512 0.1654  0.0288  71  ASP B N   
2135 C CA  . ASP B 69  ? 0.7193 0.3972 0.5089 -0.0418 0.1702  0.0350  71  ASP B CA  
2136 C C   . ASP B 69  ? 0.6764 0.3869 0.4903 -0.0302 0.1538  0.0419  71  ASP B C   
2137 O O   . ASP B 69  ? 0.6586 0.3973 0.5034 -0.0189 0.1587  0.0488  71  ASP B O   
2138 C CB  . ASP B 69  ? 0.7413 0.4177 0.5208 -0.0503 0.1701  0.0315  71  ASP B CB  
2139 C CG  . ASP B 69  ? 0.8104 0.4546 0.5663 -0.0624 0.1902  0.0246  71  ASP B CG  
2140 O OD1 . ASP B 69  ? 0.8332 0.4741 0.6019 -0.0594 0.2105  0.0243  71  ASP B OD1 
2141 O OD2 . ASP B 69  ? 0.8315 0.4509 0.5540 -0.0752 0.1864  0.0194  71  ASP B OD2 
2142 N N   . PHE B 70  ? 0.6568 0.3630 0.4567 -0.0327 0.1343  0.0397  72  PHE B N   
2143 C CA  . PHE B 70  ? 0.6176 0.3491 0.4372 -0.0234 0.1217  0.0445  72  PHE B CA  
2144 C C   . PHE B 70  ? 0.6054 0.3402 0.4409 -0.0152 0.1334  0.0493  72  PHE B C   
2145 O O   . PHE B 70  ? 0.5761 0.3354 0.4350 -0.0044 0.1349  0.0571  72  PHE B O   
2146 C CB  . PHE B 70  ? 0.5985 0.3220 0.4026 -0.0279 0.1017  0.0391  72  PHE B CB  
2147 C CG  . PHE B 70  ? 0.5768 0.3197 0.3999 -0.0202 0.0949  0.0418  72  PHE B CG  
2148 C CD1 . PHE B 70  ? 0.5648 0.3364 0.4070 -0.0128 0.0888  0.0471  72  PHE B CD1 
2149 C CD2 . PHE B 70  ? 0.5811 0.3128 0.4025 -0.0215 0.0966  0.0385  72  PHE B CD2 
2150 C CE1 . PHE B 70  ? 0.5586 0.3444 0.4144 -0.0070 0.0850  0.0492  72  PHE B CE1 
2151 C CE2 . PHE B 70  ? 0.5711 0.3189 0.4094 -0.0160 0.0936  0.0402  72  PHE B CE2 
2152 C CZ  . PHE B 70  ? 0.5509 0.3244 0.4052 -0.0087 0.0885  0.0459  72  PHE B CZ  
2153 N N   . TRP B 71  ? 0.6360 0.3440 0.4563 -0.0208 0.1415  0.0445  73  TRP B N   
2154 C CA  . TRP B 71  ? 0.6576 0.3635 0.4899 -0.0144 0.1543  0.0483  73  TRP B CA  
2155 C C   . TRP B 71  ? 0.6774 0.3903 0.5285 -0.0049 0.1730  0.0555  73  TRP B C   
2156 O O   . TRP B 71  ? 0.6984 0.4213 0.5665 0.0058  0.1783  0.0632  73  TRP B O   
2157 C CB  . TRP B 71  ? 0.6737 0.3483 0.4849 -0.0242 0.1597  0.0401  73  TRP B CB  
2158 C CG  . TRP B 71  ? 0.6592 0.3329 0.4628 -0.0297 0.1418  0.0338  73  TRP B CG  
2159 C CD1 . TRP B 71  ? 0.6738 0.3288 0.4533 -0.0408 0.1290  0.0243  73  TRP B CD1 
2160 C CD2 . TRP B 71  ? 0.6304 0.3227 0.4516 -0.0242 0.1349  0.0361  73  TRP B CD2 
2161 N NE1 . TRP B 71  ? 0.6686 0.3327 0.4547 -0.0417 0.1140  0.0198  73  TRP B NE1 
2162 C CE2 . TRP B 71  ? 0.6440 0.3308 0.4557 -0.0323 0.1186  0.0264  73  TRP B CE2 
2163 C CE3 . TRP B 71  ? 0.6172 0.3296 0.4601 -0.0132 0.1403  0.0452  73  TRP B CE3 
2164 C CZ2 . TRP B 71  ? 0.6480 0.3509 0.4752 -0.0305 0.1100  0.0243  73  TRP B CZ2 
2165 C CZ3 . TRP B 71  ? 0.6329 0.3570 0.4851 -0.0124 0.1326  0.0439  73  TRP B CZ3 
2166 C CH2 . TRP B 71  ? 0.6417 0.3620 0.4880 -0.0213 0.1187  0.0328  73  TRP B CH2 
2167 N N   . ALA B 72  ? 0.6853 0.3919 0.5339 -0.0082 0.1836  0.0531  74  ALA B N   
2168 C CA  . ALA B 72  ? 0.6700 0.3894 0.5440 0.0024  0.2003  0.0593  74  ALA B CA  
2169 C C   . ALA B 72  ? 0.6380 0.3955 0.5402 0.0158  0.1897  0.0691  74  ALA B C   
2170 O O   . ALA B 72  ? 0.6292 0.3975 0.5520 0.0294  0.1967  0.0776  74  ALA B O   
2171 C CB  . ALA B 72  ? 0.6864 0.3966 0.5545 -0.0060 0.2121  0.0526  74  ALA B CB  
2172 N N   . LEU B 73  ? 0.6274 0.4028 0.5280 0.0120  0.1726  0.0677  75  LEU B N   
2173 C CA  . LEU B 73  ? 0.6071 0.4177 0.5296 0.0219  0.1607  0.0754  75  LEU B CA  
2174 C C   . LEU B 73  ? 0.6000 0.4155 0.5241 0.0299  0.1531  0.0822  75  LEU B C   
2175 O O   . LEU B 73  ? 0.5765 0.4117 0.5190 0.0428  0.1523  0.0919  75  LEU B O   
2176 C CB  . LEU B 73  ? 0.6135 0.4348 0.5278 0.0127  0.1456  0.0700  75  LEU B CB  
2177 C CG  . LEU B 73  ? 0.6036 0.4594 0.5358 0.0196  0.1320  0.0755  75  LEU B CG  
2178 C CD1 . LEU B 73  ? 0.5856 0.4669 0.5478 0.0293  0.1395  0.0807  75  LEU B CD1 
2179 C CD2 . LEU B 73  ? 0.6044 0.4632 0.5240 0.0090  0.1190  0.0689  75  LEU B CD2 
2180 N N   . TYR B 74  ? 0.6241 0.4214 0.5286 0.0221  0.1476  0.0770  76  TYR B N   
2181 C CA  . TYR B 74  ? 0.6381 0.4367 0.5430 0.0270  0.1437  0.0814  76  TYR B CA  
2182 C C   . TYR B 74  ? 0.6553 0.4444 0.5683 0.0372  0.1598  0.0894  76  TYR B C   
2183 O O   . TYR B 74  ? 0.6476 0.4493 0.5700 0.0480  0.1581  0.0992  76  TYR B O   
2184 C CB  . TYR B 74  ? 0.6407 0.4210 0.5273 0.0156  0.1370  0.0717  76  TYR B CB  
2185 C CG  . TYR B 74  ? 0.6352 0.4192 0.5246 0.0184  0.1341  0.0740  76  TYR B CG  
2186 C CD1 . TYR B 74  ? 0.6444 0.4112 0.5326 0.0201  0.1479  0.0759  76  TYR B CD1 
2187 C CD2 . TYR B 74  ? 0.6333 0.4355 0.5255 0.0183  0.1195  0.0733  76  TYR B CD2 
2188 C CE1 . TYR B 74  ? 0.6489 0.4171 0.5385 0.0210  0.1477  0.0772  76  TYR B CE1 
2189 C CE2 . TYR B 74  ? 0.6461 0.4504 0.5403 0.0194  0.1193  0.0740  76  TYR B CE2 
2190 C CZ  . TYR B 74  ? 0.6706 0.4579 0.5634 0.0205  0.1338  0.0761  76  TYR B CZ  
2191 O OH  . TYR B 74  ? 0.6997 0.4868 0.5933 0.0199  0.1362  0.0762  76  TYR B OH  
2192 N N   . ASN B 75  ? 0.6815 0.4458 0.5882 0.0335  0.1755  0.0853  77  ASN B N   
2193 C CA  . ASN B 75  ? 0.7191 0.4691 0.6321 0.0429  0.1931  0.0921  77  ASN B CA  
2194 C C   . ASN B 75  ? 0.7289 0.5003 0.6660 0.0594  0.1961  0.1033  77  ASN B C   
2195 O O   . ASN B 75  ? 0.7345 0.5072 0.6789 0.0723  0.1993  0.1141  77  ASN B O   
2196 C CB  . ASN B 75  ? 0.7625 0.4813 0.6632 0.0343  0.2101  0.0837  77  ASN B CB  
2197 C CG  . ASN B 75  ? 0.8476 0.5438 0.7253 0.0194  0.2071  0.0730  77  ASN B CG  
2198 O OD1 . ASN B 75  ? 0.9076 0.6084 0.7828 0.0175  0.1974  0.0727  77  ASN B OD1 
2199 N ND2 . ASN B 75  ? 0.8348 0.5063 0.6955 0.0078  0.2154  0.0632  77  ASN B ND2 
2200 N N   . HIS B 76  ? 0.7274 0.5159 0.6770 0.0591  0.1944  0.1008  78  HIS B N   
2201 C CA  . HIS B 76  ? 0.7256 0.5413 0.7031 0.0742  0.1937  0.1098  78  HIS B CA  
2202 C C   . HIS B 76  ? 0.7186 0.5585 0.7014 0.0840  0.1762  0.1202  78  HIS B C   
2203 O O   . HIS B 76  ? 0.7076 0.5500 0.7004 0.0993  0.1789  0.1317  78  HIS B O   
2204 C CB  . HIS B 76  ? 0.7568 0.5895 0.7469 0.0685  0.1935  0.1027  78  HIS B CB  
2205 C CG  . HIS B 76  ? 0.8296 0.6945 0.8536 0.0836  0.1919  0.1101  78  HIS B CG  
2206 N ND1 . HIS B 76  ? 0.8499 0.7487 0.8870 0.0829  0.1759  0.1099  78  HIS B ND1 
2207 C CD2 . HIS B 76  ? 0.8510 0.7188 0.8987 0.1000  0.2034  0.1176  78  HIS B CD2 
2208 C CE1 . HIS B 76  ? 0.8447 0.7684 0.9143 0.0983  0.1770  0.1166  78  HIS B CE1 
2209 N NE2 . HIS B 76  ? 0.8454 0.7517 0.9232 0.1101  0.1930  0.1219  78  HIS B NE2 
2210 N N   . ILE B 77  ? 0.7135 0.5681 0.6869 0.0751  0.1589  0.1162  79  ILE B N   
2211 C CA  . ILE B 77  ? 0.7039 0.5792 0.6778 0.0816  0.1431  0.1242  79  ILE B CA  
2212 C C   . ILE B 77  ? 0.7399 0.5967 0.7011 0.0880  0.1475  0.1324  79  ILE B C   
2213 O O   . ILE B 77  ? 0.7200 0.5872 0.6845 0.1002  0.1419  0.1439  79  ILE B O   
2214 C CB  . ILE B 77  ? 0.6842 0.5704 0.6467 0.0685  0.1274  0.1157  79  ILE B CB  
2215 C CG1 . ILE B 77  ? 0.6811 0.5860 0.6548 0.0621  0.1228  0.1086  79  ILE B CG1 
2216 C CG2 . ILE B 77  ? 0.6607 0.5615 0.6180 0.0726  0.1139  0.1220  79  ILE B CG2 
2217 C CD1 . ILE B 77  ? 0.6784 0.6188 0.6748 0.0713  0.1134  0.1147  79  ILE B CD1 
2218 N N   . GLN B 78  ? 0.7928 0.6213 0.7380 0.0788  0.1573  0.1260  80  GLN B N   
2219 C CA  . GLN B 78  ? 0.8463 0.6537 0.7783 0.0809  0.1646  0.1308  80  GLN B CA  
2220 C C   . GLN B 78  ? 0.9011 0.6964 0.8395 0.0970  0.1775  0.1434  80  GLN B C   
2221 O O   . GLN B 78  ? 0.9145 0.7015 0.8438 0.1045  0.1785  0.1534  80  GLN B O   
2222 C CB  . GLN B 78  ? 0.8720 0.6531 0.7900 0.0663  0.1733  0.1188  80  GLN B CB  
2223 C CG  . GLN B 78  ? 0.8926 0.6583 0.7973 0.0616  0.1769  0.1181  80  GLN B CG  
2224 C CD  . GLN B 78  ? 0.9469 0.6886 0.8422 0.0475  0.1858  0.1053  80  GLN B CD  
2225 O OE1 . GLN B 78  ? 0.9742 0.7021 0.8686 0.0434  0.1939  0.0997  80  GLN B OE1 
2226 N NE2 . GLN B 78  ? 0.9689 0.7052 0.8572 0.0389  0.1847  0.0994  80  GLN B NE2 
2227 N N   . LEU B 79  ? 0.9338 0.7256 0.8866 0.1021  0.1883  0.1428  81  LEU B N   
2228 C CA  . LEU B 79  ? 0.9694 0.7501 0.9329 0.1194  0.2010  0.1543  81  LEU B CA  
2229 C C   . LEU B 79  ? 0.9667 0.7788 0.9499 0.1368  0.1874  0.1664  81  LEU B C   
2230 O O   . LEU B 79  ? 0.9701 0.7773 0.9494 0.1510  0.1854  0.1801  81  LEU B O   
2231 C CB  . LEU B 79  ? 0.9915 0.7564 0.9646 0.1172  0.2195  0.1468  81  LEU B CB  
2232 C CG  . LEU B 79  ? 1.0436 0.7966 1.0326 0.1361  0.2350  0.1568  81  LEU B CG  
2233 C CD1 . LEU B 79  ? 1.0763 0.7998 1.0480 0.1442  0.2431  0.1677  81  LEU B CD1 
2234 C CD2 . LEU B 79  ? 1.0665 0.8010 1.0619 0.1306  0.2556  0.1465  81  LEU B CD2 
2235 N N   . SER B 80  ? 0.9608 0.8039 0.9630 0.1345  0.1774  0.1609  82  SER B N   
2236 C CA  . SER B 80  ? 0.9565 0.8321 0.9862 0.1500  0.1672  0.1689  82  SER B CA  
2237 C C   . SER B 80  ? 0.9497 0.8505 0.9742 0.1538  0.1446  0.1763  82  SER B C   
2238 O O   . SER B 80  ? 0.9308 0.8598 0.9770 0.1674  0.1332  0.1836  82  SER B O   
2239 C CB  . SER B 80  ? 0.9781 0.8752 1.0313 0.1430  0.1691  0.1573  82  SER B CB  
2240 O OG  . SER B 80  ? 1.0107 0.9291 1.0588 0.1288  0.1541  0.1489  82  SER B OG  
2241 N N   . SER B 81  ? 0.9646 0.8571 0.9625 0.1419  0.1378  0.1735  83  SER B N   
2242 C CA  . SER B 81  ? 0.9708 0.8871 0.9618 0.1417  0.1175  0.1772  83  SER B CA  
2243 C C   . SER B 81  ? 0.9986 0.8932 0.9613 0.1439  0.1174  0.1860  83  SER B C   
2244 O O   . SER B 81  ? 1.0064 0.8712 0.9523 0.1360  0.1309  0.1823  83  SER B O   
2245 C CB  . SER B 81  ? 0.9865 0.9171 0.9738 0.1231  0.1090  0.1630  83  SER B CB  
2246 O OG  . SER B 81  ? 0.9996 0.9477 1.0091 0.1188  0.1102  0.1542  83  SER B OG  
2247 N N   . ASN B 82  ? 1.0138 0.9228 0.9701 0.1535  0.1023  0.1970  84  ASN B N   
2248 C CA  . ASN B 82  ? 1.0494 0.9380 0.9743 0.1545  0.1014  0.2057  84  ASN B CA  
2249 C C   . ASN B 82  ? 1.0507 0.9585 0.9621 0.1436  0.0854  0.2006  84  ASN B C   
2250 O O   . ASN B 82  ? 1.0346 0.9746 0.9617 0.1409  0.0713  0.1953  84  ASN B O   
2251 C CB  . ASN B 82  ? 1.0880 0.9685 1.0083 0.1763  0.0982  0.2250  84  ASN B CB  
2252 C CG  . ASN B 82  ? 1.1607 1.0010 1.0714 0.1845  0.1186  0.2328  84  ASN B CG  
2253 O OD1 . ASN B 82  ? 1.1786 0.9966 1.0875 0.1736  0.1367  0.2232  84  ASN B OD1 
2254 N ND2 . ASN B 82  ? 1.1879 1.0167 1.0907 0.2043  0.1152  0.2507  84  ASN B ND2 
2255 N N   . LEU B 83  ? 1.0638 0.9505 0.9459 0.1365  0.0896  0.2014  85  LEU B N   
2256 C CA  . LEU B 83  ? 1.0669 0.9651 0.9350 0.1232  0.0801  0.1932  85  LEU B CA  
2257 C C   . LEU B 83  ? 1.0717 0.9856 0.9257 0.1305  0.0625  0.2035  85  LEU B C   
2258 O O   . LEU B 83  ? 1.0870 0.9814 0.9173 0.1395  0.0638  0.2169  85  LEU B O   
2259 C CB  . LEU B 83  ? 1.0806 0.9491 0.9267 0.1118  0.0950  0.1879  85  LEU B CB  
2260 C CG  . LEU B 83  ? 1.0900 0.9664 0.9259 0.0964  0.0903  0.1758  85  LEU B CG  
2261 C CD1 . LEU B 83  ? 1.0808 0.9740 0.9382 0.0852  0.0867  0.1595  85  LEU B CD1 
2262 C CD2 . LEU B 83  ? 1.1062 0.9543 0.9214 0.0884  0.1056  0.1734  85  LEU B CD2 
2263 N N   . MET B 84  ? 1.0611 1.0080 0.9268 0.1256  0.0461  0.1968  86  MET B N   
2264 C CA  . MET B 84  ? 1.0690 1.0352 0.9228 0.1306  0.0269  0.2042  86  MET B CA  
2265 C C   . MET B 84  ? 1.0652 1.0379 0.9027 0.1137  0.0219  0.1924  86  MET B C   
2266 O O   . MET B 84  ? 1.0641 1.0529 0.9192 0.1027  0.0205  0.1784  86  MET B O   
2267 C CB  . MET B 84  ? 1.0711 1.0748 0.9571 0.1381  0.0116  0.2043  86  MET B CB  
2268 C CG  . MET B 84  ? 1.1194 1.1246 1.0221 0.1595  0.0098  0.2189  86  MET B CG  
2269 S SD  . MET B 84  ? 1.1969 1.2515 1.1456 0.1666  -0.0065 0.2154  86  MET B SD  
2270 C CE  . MET B 84  ? 1.1210 1.1777 1.0958 0.1497  0.0110  0.1955  86  MET B CE  
2271 N N   . PRO B 85  ? 1.0639 1.0221 0.8670 0.1108  0.0204  0.1970  87  PRO B N   
2272 C CA  . PRO B 85  ? 1.0516 1.0201 0.8418 0.0957  0.0144  0.1852  87  PRO B CA  
2273 C C   . PRO B 85  ? 1.0172 1.0222 0.8212 0.0948  -0.0061 0.1817  87  PRO B C   
2274 O O   . PRO B 85  ? 1.0082 1.0325 0.8295 0.1070  -0.0177 0.1900  87  PRO B O   
2275 C CB  . PRO B 85  ? 1.0897 1.0323 0.8379 0.0942  0.0187  0.1926  87  PRO B CB  
2276 C CG  . PRO B 85  ? 1.1148 1.0273 0.8542 0.1056  0.0321  0.2059  87  PRO B CG  
2277 C CD  . PRO B 85  ? 1.0817 1.0102 0.8535 0.1202  0.0260  0.2126  87  PRO B CD  
2278 N N   . GLY B 86  ? 0.9949 1.0094 0.7934 0.0800  -0.0096 0.1682  88  GLY B N   
2279 C CA  . GLY B 86  ? 0.9624 1.0096 0.7759 0.0747  -0.0255 0.1605  88  GLY B CA  
2280 C C   . GLY B 86  ? 0.9166 0.9780 0.7651 0.0705  -0.0223 0.1499  88  GLY B C   
2281 O O   . GLY B 86  ? 0.9016 0.9829 0.7600 0.0607  -0.0300 0.1389  88  GLY B O   
2282 N N   . CYS B 87  ? 0.8938 0.9422 0.7583 0.0770  -0.0098 0.1527  89  CYS B N   
2283 C CA  . CYS B 87  ? 0.8702 0.9258 0.7623 0.0728  -0.0047 0.1434  89  CYS B CA  
2284 C C   . CYS B 87  ? 0.8328 0.8727 0.7201 0.0588  0.0043  0.1292  89  CYS B C   
2285 O O   . CYS B 87  ? 0.8502 0.8716 0.7183 0.0541  0.0104  0.1268  89  CYS B O   
2286 C CB  . CYS B 87  ? 0.9031 0.9500 0.8119 0.0851  0.0050  0.1518  89  CYS B CB  
2287 S SG  . CYS B 87  ? 1.0418 1.1114 0.9662 0.1039  -0.0072 0.1670  89  CYS B SG  
2288 N N   . ASP B 88  ? 0.7691 0.8166 0.6743 0.0523  0.0049  0.1196  90  ASP B N   
2289 C CA  . ASP B 88  ? 0.7336 0.7651 0.6367 0.0418  0.0116  0.1076  90  ASP B CA  
2290 C C   . ASP B 88  ? 0.6787 0.7059 0.5991 0.0418  0.0184  0.1048  90  ASP B C   
2291 O O   . ASP B 88  ? 0.6712 0.7158 0.6082 0.0444  0.0156  0.1064  90  ASP B O   
2292 C CB  . ASP B 88  ? 0.7536 0.7941 0.6510 0.0299  0.0034  0.0961  90  ASP B CB  
2293 C CG  . ASP B 88  ? 0.7896 0.8396 0.6698 0.0278  -0.0050 0.0972  90  ASP B CG  
2294 O OD1 . ASP B 88  ? 0.8043 0.8431 0.6688 0.0324  -0.0013 0.1040  90  ASP B OD1 
2295 O OD2 . ASP B 88  ? 0.7926 0.8588 0.6728 0.0204  -0.0142 0.0907  90  ASP B OD2 
2296 N N   . TYR B 89  ? 0.6368 0.6409 0.5534 0.0385  0.0276  0.0999  91  TYR B N   
2297 C CA  . TYR B 89  ? 0.5952 0.5894 0.5203 0.0345  0.0335  0.0942  91  TYR B CA  
2298 C C   . TYR B 89  ? 0.5288 0.5112 0.4449 0.0233  0.0303  0.0819  91  TYR B C   
2299 O O   . TYR B 89  ? 0.5137 0.4889 0.4203 0.0209  0.0286  0.0781  91  TYR B O   
2300 C CB  . TYR B 89  ? 0.6252 0.5993 0.5514 0.0402  0.0458  0.0988  91  TYR B CB  
2301 C CG  . TYR B 89  ? 0.6507 0.6323 0.5879 0.0527  0.0504  0.1109  91  TYR B CG  
2302 C CD1 . TYR B 89  ? 0.6720 0.6554 0.6024 0.0619  0.0491  0.1214  91  TYR B CD1 
2303 C CD2 . TYR B 89  ? 0.6680 0.6518 0.6210 0.0558  0.0571  0.1116  91  TYR B CD2 
2304 C CE1 . TYR B 89  ? 0.6880 0.6753 0.6276 0.0754  0.0521  0.1335  91  TYR B CE1 
2305 C CE2 . TYR B 89  ? 0.6751 0.6655 0.6416 0.0691  0.0616  0.1223  91  TYR B CE2 
2306 C CZ  . TYR B 89  ? 0.6979 0.6899 0.6578 0.0798  0.0581  0.1337  91  TYR B CZ  
2307 O OH  . TYR B 89  ? 0.7380 0.7339 0.7101 0.0950  0.0612  0.1455  91  TYR B OH  
2308 N N   . SER B 90  ? 0.4906 0.4703 0.4097 0.0169  0.0301  0.0757  92  SER B N   
2309 C CA  . SER B 90  ? 0.4887 0.4542 0.3975 0.0074  0.0259  0.0651  92  SER B CA  
2310 C C   . SER B 90  ? 0.4835 0.4303 0.3899 0.0036  0.0321  0.0620  92  SER B C   
2311 O O   . SER B 90  ? 0.4848 0.4384 0.3998 0.0036  0.0375  0.0643  92  SER B O   
2312 C CB  . SER B 90  ? 0.5021 0.4820 0.4099 0.0006  0.0179  0.0600  92  SER B CB  
2313 O OG  . SER B 90  ? 0.5507 0.5475 0.4573 0.0026  0.0118  0.0621  92  SER B OG  
2314 N N   . LEU B 91  ? 0.4731 0.3963 0.3680 0.0001  0.0310  0.0561  93  LEU B N   
2315 C CA  . LEU B 91  ? 0.4544 0.3551 0.3387 -0.0060 0.0338  0.0516  93  LEU B CA  
2316 C C   . LEU B 91  ? 0.4485 0.3375 0.3189 -0.0133 0.0241  0.0436  93  LEU B C   
2317 O O   . LEU B 91  ? 0.4303 0.3120 0.2966 -0.0123 0.0166  0.0394  93  LEU B O   
2318 C CB  . LEU B 91  ? 0.4445 0.3245 0.3234 -0.0043 0.0383  0.0512  93  LEU B CB  
2319 C CG  . LEU B 91  ? 0.4556 0.3093 0.3190 -0.0110 0.0422  0.0473  93  LEU B CG  
2320 C CD1 . LEU B 91  ? 0.4439 0.3016 0.3146 -0.0105 0.0561  0.0518  93  LEU B CD1 
2321 C CD2 . LEU B 91  ? 0.4599 0.2916 0.3139 -0.0115 0.0412  0.0439  93  LEU B CD2 
2322 N N   . PHE B 92  ? 0.4477 0.3339 0.3119 -0.0206 0.0253  0.0409  94  PHE B N   
2323 C CA  . PHE B 92  ? 0.4722 0.3422 0.3197 -0.0277 0.0173  0.0339  94  PHE B CA  
2324 C C   . PHE B 92  ? 0.4648 0.3057 0.2923 -0.0355 0.0216  0.0312  94  PHE B C   
2325 O O   . PHE B 92  ? 0.4561 0.2967 0.2863 -0.0378 0.0331  0.0334  94  PHE B O   
2326 C CB  . PHE B 92  ? 0.4844 0.3748 0.3380 -0.0320 0.0148  0.0319  94  PHE B CB  
2327 C CG  . PHE B 92  ? 0.5003 0.4075 0.3612 -0.0274 0.0071  0.0314  94  PHE B CG  
2328 C CD1 . PHE B 92  ? 0.4903 0.4182 0.3655 -0.0195 0.0090  0.0375  94  PHE B CD1 
2329 C CD2 . PHE B 92  ? 0.5163 0.4146 0.3674 -0.0308 -0.0007 0.0246  94  PHE B CD2 
2330 C CE1 . PHE B 92  ? 0.4978 0.4368 0.3754 -0.0167 0.0039  0.0364  94  PHE B CE1 
2331 C CE2 . PHE B 92  ? 0.5189 0.4308 0.3760 -0.0274 -0.0054 0.0229  94  PHE B CE2 
2332 C CZ  . PHE B 92  ? 0.5053 0.4373 0.3747 -0.0211 -0.0027 0.0285  94  PHE B CZ  
2333 N N   . LYS B 93  ? 0.4775 0.2917 0.2833 -0.0394 0.0129  0.0262  95  LYS B N   
2334 C CA  . LYS B 93  ? 0.5108 0.2918 0.2897 -0.0482 0.0162  0.0237  95  LYS B CA  
2335 C C   . LYS B 93  ? 0.5221 0.3114 0.3033 -0.0575 0.0281  0.0226  95  LYS B C   
2336 O O   . LYS B 93  ? 0.4995 0.3151 0.2971 -0.0585 0.0277  0.0217  95  LYS B O   
2337 C CB  . LYS B 93  ? 0.5502 0.3018 0.3049 -0.0495 0.0028  0.0194  95  LYS B CB  
2338 C CG  . LYS B 93  ? 0.5746 0.3148 0.3268 -0.0416 -0.0090 0.0188  95  LYS B CG  
2339 C CD  . LYS B 93  ? 0.5853 0.3016 0.3199 -0.0401 -0.0240 0.0147  95  LYS B CD  
2340 C CE  . LYS B 93  ? 0.6269 0.3337 0.3617 -0.0327 -0.0363 0.0130  95  LYS B CE  
2341 N NZ  . LYS B 93  ? 0.5972 0.2867 0.3236 -0.0275 -0.0539 0.0086  95  LYS B NZ  
2342 N N   . ASP B 94  ? 0.5534 0.3217 0.3196 -0.0649 0.0393  0.0220  96  ASP B N   
2343 C CA  . ASP B 94  ? 0.5813 0.3562 0.3517 -0.0753 0.0535  0.0193  96  ASP B CA  
2344 C C   . ASP B 94  ? 0.6091 0.3770 0.3673 -0.0839 0.0488  0.0141  96  ASP B C   
2345 O O   . ASP B 94  ? 0.6379 0.3704 0.3653 -0.0865 0.0407  0.0123  96  ASP B O   
2346 C CB  . ASP B 94  ? 0.6120 0.3543 0.3594 -0.0834 0.0671  0.0179  96  ASP B CB  
2347 C CG  . ASP B 94  ? 0.6606 0.4123 0.4188 -0.0938 0.0866  0.0143  96  ASP B CG  
2348 O OD1 . ASP B 94  ? 0.6395 0.4319 0.4328 -0.0913 0.0897  0.0142  96  ASP B OD1 
2349 O OD2 . ASP B 94  ? 0.7123 0.4306 0.4438 -0.1046 0.0986  0.0109  96  ASP B OD2 
2350 N N   . GLY B 95  ? 0.5978 0.3996 0.3806 -0.0872 0.0525  0.0119  97  GLY B N   
2351 C CA  . GLY B 95  ? 0.6119 0.4115 0.3870 -0.0968 0.0500  0.0059  97  GLY B CA  
2352 C C   . GLY B 95  ? 0.6092 0.4284 0.3944 -0.0905 0.0360  0.0055  97  GLY B C   
2353 O O   . GLY B 95  ? 0.6285 0.4450 0.4067 -0.0988 0.0342  -0.0002 97  GLY B O   
2354 N N   . ILE B 96  ? 0.5913 0.4279 0.3912 -0.0774 0.0276  0.0107  98  ILE B N   
2355 C CA  . ILE B 96  ? 0.5742 0.4309 0.3848 -0.0713 0.0165  0.0102  98  ILE B CA  
2356 C C   . ILE B 96  ? 0.5720 0.4712 0.4128 -0.0652 0.0183  0.0149  98  ILE B C   
2357 O O   . ILE B 96  ? 0.5455 0.4514 0.3967 -0.0561 0.0207  0.0213  98  ILE B O   
2358 C CB  . ILE B 96  ? 0.5668 0.4064 0.3688 -0.0609 0.0060  0.0118  98  ILE B CB  
2359 C CG1 . ILE B 96  ? 0.5785 0.3730 0.3495 -0.0640 0.0013  0.0086  98  ILE B CG1 
2360 C CG2 . ILE B 96  ? 0.5464 0.4066 0.3601 -0.0558 -0.0020 0.0101  98  ILE B CG2 
2361 C CD1 . ILE B 96  ? 0.5711 0.3522 0.3386 -0.0534 -0.0105 0.0091  98  ILE B CD1 
2362 N N   . GLU B 97  ? 0.6067 0.5329 0.4600 -0.0701 0.0167  0.0118  99  GLU B N   
2363 C CA  . GLU B 97  ? 0.6370 0.6024 0.5152 -0.0628 0.0140  0.0169  99  GLU B CA  
2364 C C   . GLU B 97  ? 0.6493 0.6174 0.5255 -0.0524 0.0055  0.0208  99  GLU B C   
2365 O O   . GLU B 97  ? 0.6589 0.6091 0.5201 -0.0537 0.0001  0.0160  99  GLU B O   
2366 C CB  . GLU B 97  ? 0.6854 0.6791 0.5755 -0.0717 0.0122  0.0116  99  GLU B CB  
2367 C CG  . GLU B 97  ? 0.8049 0.8038 0.7048 -0.0824 0.0227  0.0069  99  GLU B CG  
2368 C CD  . GLU B 97  ? 0.9712 1.0061 0.8906 -0.0908 0.0201  0.0011  99  GLU B CD  
2369 O OE1 . GLU B 97  ? 1.0119 1.0546 0.9435 -0.1011 0.0297  -0.0048 99  GLU B OE1 
2370 O OE2 . GLU B 97  ? 1.0186 1.0741 0.9409 -0.0880 0.0090  0.0016  99  GLU B OE2 
2371 N N   . PRO B 98  ? 0.6407 0.6293 0.5320 -0.0420 0.0053  0.0290  100 PRO B N   
2372 C CA  . PRO B 98  ? 0.6524 0.6418 0.5406 -0.0336 0.0001  0.0323  100 PRO B CA  
2373 C C   . PRO B 98  ? 0.6697 0.6783 0.5567 -0.0361 -0.0071 0.0297  100 PRO B C   
2374 O O   . PRO B 98  ? 0.6816 0.7059 0.5727 -0.0292 -0.0096 0.0358  100 PRO B O   
2375 C CB  . PRO B 98  ? 0.6459 0.6450 0.5469 -0.0230 0.0047  0.0423  100 PRO B CB  
2376 C CG  . PRO B 98  ? 0.6406 0.6624 0.5581 -0.0245 0.0072  0.0444  100 PRO B CG  
2377 C CD  . PRO B 98  ? 0.6240 0.6337 0.5356 -0.0369 0.0108  0.0355  100 PRO B CD  
2378 N N   . MET B 99  ? 0.6705 0.6748 0.5488 -0.0465 -0.0099 0.0207  101 MET B N   
2379 C CA  . MET B 99  ? 0.6812 0.6996 0.5547 -0.0517 -0.0158 0.0159  101 MET B CA  
2380 C C   . MET B 99  ? 0.6998 0.6920 0.5570 -0.0571 -0.0165 0.0064  101 MET B C   
2381 O O   . MET B 99  ? 0.6921 0.6605 0.5415 -0.0614 -0.0141 0.0022  101 MET B O   
2382 C CB  . MET B 99  ? 0.7013 0.7431 0.5834 -0.0614 -0.0176 0.0123  101 MET B CB  
2383 C CG  . MET B 99  ? 0.7615 0.8330 0.6651 -0.0552 -0.0182 0.0207  101 MET B CG  
2384 S SD  . MET B 99  ? 0.9471 1.0423 0.8523 -0.0440 -0.0269 0.0305  101 MET B SD  
2385 C CE  . MET B 99  ? 0.9644 1.0967 0.8987 -0.0392 -0.0302 0.0371  101 MET B CE  
2386 N N   . TRP B 100 ? 0.7236 0.7180 0.5741 -0.0566 -0.0195 0.0029  102 TRP B N   
2387 C CA  . TRP B 100 ? 0.7585 0.7287 0.5972 -0.0592 -0.0197 -0.0063 102 TRP B CA  
2388 C C   . TRP B 100 ? 0.7583 0.7189 0.5871 -0.0717 -0.0197 -0.0153 102 TRP B C   
2389 O O   . TRP B 100 ? 0.7727 0.7061 0.5912 -0.0728 -0.0194 -0.0216 102 TRP B O   
2390 C CB  . TRP B 100 ? 0.7710 0.7457 0.6064 -0.0560 -0.0199 -0.0091 102 TRP B CB  
2391 C CG  . TRP B 100 ? 0.7881 0.7749 0.6141 -0.0654 -0.0216 -0.0157 102 TRP B CG  
2392 C CD1 . TRP B 100 ? 0.7997 0.8128 0.6247 -0.0684 -0.0250 -0.0119 102 TRP B CD1 
2393 C CD2 . TRP B 100 ? 0.7974 0.7689 0.6120 -0.0729 -0.0205 -0.0277 102 TRP B CD2 
2394 N NE1 . TRP B 100 ? 0.8098 0.8255 0.6221 -0.0789 -0.0264 -0.0213 102 TRP B NE1 
2395 C CE2 . TRP B 100 ? 0.8096 0.7994 0.6156 -0.0820 -0.0224 -0.0314 102 TRP B CE2 
2396 C CE3 . TRP B 100 ? 0.8135 0.7564 0.6239 -0.0721 -0.0187 -0.0356 102 TRP B CE3 
2397 C CZ2 . TRP B 100 ? 0.8240 0.8035 0.6168 -0.0916 -0.0205 -0.0435 102 TRP B CZ2 
2398 C CZ3 . TRP B 100 ? 0.8326 0.7651 0.6318 -0.0799 -0.0168 -0.0469 102 TRP B CZ3 
2399 C CH2 . TRP B 100 ? 0.8336 0.7839 0.6238 -0.0901 -0.0167 -0.0512 102 TRP B CH2 
2400 N N   . GLU B 101 ? 0.7375 0.7197 0.5703 -0.0809 -0.0202 -0.0161 103 GLU B N   
2401 C CA  . GLU B 101 ? 0.7361 0.7110 0.5609 -0.0951 -0.0183 -0.0253 103 GLU B CA  
2402 C C   . GLU B 101 ? 0.7301 0.6780 0.5490 -0.0982 -0.0130 -0.0257 103 GLU B C   
2403 O O   . GLU B 101 ? 0.7444 0.6735 0.5503 -0.1094 -0.0099 -0.0338 103 GLU B O   
2404 C CB  . GLU B 101 ? 0.7608 0.7712 0.5968 -0.1041 -0.0207 -0.0265 103 GLU B CB  
2405 C CG  . GLU B 101 ? 0.8286 0.8629 0.6631 -0.1038 -0.0275 -0.0270 103 GLU B CG  
2406 C CD  . GLU B 101 ? 0.8851 0.9425 0.7302 -0.0912 -0.0321 -0.0152 103 GLU B CD  
2407 O OE1 . GLU B 101 ? 0.8472 0.8970 0.6997 -0.0799 -0.0291 -0.0065 103 GLU B OE1 
2408 O OE2 . GLU B 101 ? 0.9366 1.0178 0.7801 -0.0931 -0.0390 -0.0146 103 GLU B OE2 
2409 N N   . ASP B 102 ? 0.7070 0.6494 0.5320 -0.0894 -0.0111 -0.0174 104 ASP B N   
2410 C CA  . ASP B 102 ? 0.7060 0.6188 0.5202 -0.0924 -0.0059 -0.0172 104 ASP B CA  
2411 C C   . ASP B 102 ? 0.7250 0.5983 0.5172 -0.0921 -0.0083 -0.0222 104 ASP B C   
2412 O O   . ASP B 102 ? 0.7191 0.5879 0.5114 -0.0831 -0.0139 -0.0228 104 ASP B O   
2413 C CB  . ASP B 102 ? 0.7139 0.6267 0.5364 -0.0819 -0.0041 -0.0078 104 ASP B CB  
2414 C CG  . ASP B 102 ? 0.7366 0.6205 0.5465 -0.0854 0.0023  -0.0067 104 ASP B CG  
2415 O OD1 . ASP B 102 ? 0.7522 0.5994 0.5406 -0.0847 -0.0002 -0.0085 104 ASP B OD1 
2416 O OD2 . ASP B 102 ? 0.7317 0.6285 0.5525 -0.0883 0.0098  -0.0039 104 ASP B OD2 
2417 N N   . GLU B 103 ? 0.7483 0.5920 0.5219 -0.1018 -0.0035 -0.0261 105 GLU B N   
2418 C CA  . GLU B 103 ? 0.7703 0.5702 0.5194 -0.1006 -0.0065 -0.0296 105 GLU B CA  
2419 C C   . GLU B 103 ? 0.7590 0.5427 0.5070 -0.0847 -0.0150 -0.0245 105 GLU B C   
2420 O O   . GLU B 103 ? 0.7696 0.5334 0.5102 -0.0785 -0.0213 -0.0283 105 GLU B O   
2421 C CB  . GLU B 103 ? 0.8269 0.5929 0.5522 -0.1123 0.0010  -0.0314 105 GLU B CB  
2422 C CG  . GLU B 103 ? 0.9887 0.7216 0.6903 -0.1210 0.0023  -0.0394 105 GLU B CG  
2423 C CD  . GLU B 103 ? 1.1386 0.8961 0.8495 -0.1329 0.0063  -0.0483 105 GLU B CD  
2424 O OE1 . GLU B 103 ? 1.1953 0.9267 0.8884 -0.1389 0.0075  -0.0555 105 GLU B OE1 
2425 O OE2 . GLU B 103 ? 1.1517 0.9535 0.8869 -0.1361 0.0076  -0.0481 105 GLU B OE2 
2426 N N   . LYS B 104 ? 0.7202 0.5132 0.4775 -0.0781 -0.0147 -0.0170 106 LYS B N   
2427 C CA  . LYS B 104 ? 0.7030 0.4845 0.4619 -0.0646 -0.0227 -0.0132 106 LYS B CA  
2428 C C   . LYS B 104 ? 0.6669 0.4761 0.4486 -0.0548 -0.0264 -0.0130 106 LYS B C   
2429 O O   . LYS B 104 ? 0.6752 0.4760 0.4610 -0.0447 -0.0326 -0.0121 106 LYS B O   
2430 C CB  . LYS B 104 ? 0.7314 0.5060 0.4868 -0.0635 -0.0196 -0.0066 106 LYS B CB  
2431 C CG  . LYS B 104 ? 0.8282 0.5679 0.5557 -0.0735 -0.0147 -0.0070 106 LYS B CG  
2432 C CD  . LYS B 104 ? 0.9431 0.6384 0.6428 -0.0707 -0.0238 -0.0092 106 LYS B CD  
2433 C CE  . LYS B 104 ? 1.0517 0.7099 0.7218 -0.0757 -0.0211 -0.0056 106 LYS B CE  
2434 N NZ  . LYS B 104 ? 1.1376 0.7469 0.7736 -0.0747 -0.0298 -0.0067 106 LYS B NZ  
2435 N N   . ASN B 105 ? 0.6305 0.4712 0.4257 -0.0582 -0.0228 -0.0144 107 ASN B N   
2436 C CA  . ASN B 105 ? 0.6106 0.4737 0.4223 -0.0505 -0.0244 -0.0143 107 ASN B CA  
2437 C C   . ASN B 105 ? 0.6349 0.5020 0.4452 -0.0536 -0.0249 -0.0227 107 ASN B C   
2438 O O   . ASN B 105 ? 0.6190 0.4937 0.4390 -0.0469 -0.0257 -0.0253 107 ASN B O   
2439 C CB  . ASN B 105 ? 0.5893 0.4843 0.4146 -0.0504 -0.0201 -0.0073 107 ASN B CB  
2440 C CG  . ASN B 105 ? 0.6010 0.4941 0.4308 -0.0460 -0.0175 0.0007  107 ASN B CG  
2441 O OD1 . ASN B 105 ? 0.5944 0.4684 0.4213 -0.0398 -0.0201 0.0015  107 ASN B OD1 
2442 N ND2 . ASN B 105 ? 0.5832 0.4964 0.4209 -0.0491 -0.0125 0.0059  107 ASN B ND2 
2443 N N   . LYS B 106 ? 0.6580 0.5195 0.4564 -0.0648 -0.0229 -0.0282 108 LYS B N   
2444 C CA  . LYS B 106 ? 0.6745 0.5430 0.4707 -0.0699 -0.0218 -0.0366 108 LYS B CA  
2445 C C   . LYS B 106 ? 0.6580 0.5056 0.4535 -0.0622 -0.0241 -0.0434 108 LYS B C   
2446 O O   . LYS B 106 ? 0.6441 0.5038 0.4452 -0.0613 -0.0219 -0.0486 108 LYS B O   
2447 C CB  . LYS B 106 ? 0.7488 0.6157 0.5330 -0.0850 -0.0185 -0.0425 108 LYS B CB  
2448 C CG  . LYS B 106 ? 0.8702 0.7005 0.6361 -0.0905 -0.0172 -0.0456 108 LYS B CG  
2449 C CD  . LYS B 106 ? 0.9561 0.7943 0.7155 -0.1077 -0.0116 -0.0503 108 LYS B CD  
2450 C CE  . LYS B 106 ? 1.0653 0.8633 0.8018 -0.1162 -0.0076 -0.0555 108 LYS B CE  
2451 N NZ  . LYS B 106 ? 1.1147 0.9219 0.8476 -0.1347 0.0000  -0.0607 108 LYS B NZ  
2452 N N   . ARG B 107 ? 0.6612 0.4782 0.4504 -0.0558 -0.0288 -0.0435 109 ARG B N   
2453 C CA  . ARG B 107 ? 0.6676 0.4668 0.4618 -0.0455 -0.0330 -0.0499 109 ARG B CA  
2454 C C   . ARG B 107 ? 0.6404 0.4503 0.4553 -0.0326 -0.0367 -0.0473 109 ARG B C   
2455 O O   . ARG B 107 ? 0.6383 0.4352 0.4626 -0.0227 -0.0418 -0.0527 109 ARG B O   
2456 C CB  . ARG B 107 ? 0.7407 0.4993 0.5161 -0.0443 -0.0385 -0.0512 109 ARG B CB  
2457 C CG  . ARG B 107 ? 0.8368 0.5807 0.5917 -0.0581 -0.0325 -0.0565 109 ARG B CG  
2458 C CD  . ARG B 107 ? 0.9601 0.6586 0.6906 -0.0578 -0.0365 -0.0562 109 ARG B CD  
2459 N NE  . ARG B 107 ? 1.0838 0.7714 0.8038 -0.0577 -0.0396 -0.0470 109 ARG B NE  
2460 C CZ  . ARG B 107 ? 1.1611 0.8539 0.8712 -0.0706 -0.0323 -0.0433 109 ARG B CZ  
2461 N NH1 . ARG B 107 ? 1.1484 0.8600 0.8596 -0.0846 -0.0233 -0.0480 109 ARG B NH1 
2462 N NH2 . ARG B 107 ? 1.1910 0.8708 0.8908 -0.0700 -0.0338 -0.0358 109 ARG B NH2 
2463 N N   . GLY B 108 ? 0.6101 0.4440 0.4338 -0.0328 -0.0340 -0.0396 110 GLY B N   
2464 C CA  . GLY B 108 ? 0.5854 0.4259 0.4250 -0.0232 -0.0366 -0.0359 110 GLY B CA  
2465 C C   . GLY B 108 ? 0.5433 0.4100 0.3990 -0.0216 -0.0297 -0.0370 110 GLY B C   
2466 O O   . GLY B 108 ? 0.5408 0.4164 0.3954 -0.0259 -0.0243 -0.0428 110 GLY B O   
2467 N N   . GLY B 109 ? 0.5124 0.3884 0.3800 -0.0162 -0.0291 -0.0319 111 GLY B N   
2468 C CA  . GLY B 109 ? 0.4980 0.3954 0.3776 -0.0153 -0.0209 -0.0313 111 GLY B CA  
2469 C C   . GLY B 109 ? 0.4811 0.3841 0.3704 -0.0107 -0.0196 -0.0243 111 GLY B C   
2470 O O   . GLY B 109 ? 0.4769 0.3703 0.3611 -0.0097 -0.0244 -0.0187 111 GLY B O   
2471 N N   . ARG B 110 ? 0.4585 0.3743 0.3598 -0.0089 -0.0118 -0.0256 112 ARG B N   
2472 C CA  . ARG B 110 ? 0.4533 0.3747 0.3616 -0.0063 -0.0076 -0.0190 112 ARG B CA  
2473 C C   . ARG B 110 ? 0.4529 0.3781 0.3811 -0.0031 -0.0020 -0.0268 112 ARG B C   
2474 O O   . ARG B 110 ? 0.4572 0.3884 0.3904 -0.0048 0.0051  -0.0343 112 ARG B O   
2475 C CB  . ARG B 110 ? 0.4642 0.3990 0.3614 -0.0095 -0.0007 -0.0083 112 ARG B CB  
2476 C CG  . ARG B 110 ? 0.4874 0.4331 0.3812 -0.0122 0.0081  -0.0101 112 ARG B CG  
2477 C CD  . ARG B 110 ? 0.5561 0.5132 0.4364 -0.0138 0.0109  0.0018  112 ARG B CD  
2478 N NE  . ARG B 110 ? 0.6044 0.5681 0.4750 -0.0169 0.0185  0.0010  112 ARG B NE  
2479 C CZ  . ARG B 110 ? 0.6392 0.6117 0.4950 -0.0175 0.0201  0.0111  112 ARG B CZ  
2480 N NH1 . ARG B 110 ? 0.6476 0.6214 0.4895 -0.0212 0.0268  0.0097  112 ARG B NH1 
2481 N NH2 . ARG B 110 ? 0.6497 0.6288 0.5040 -0.0142 0.0150  0.0224  112 ARG B NH2 
2482 N N   . TRP B 111 ? 0.4472 0.3686 0.3867 0.0003  -0.0039 -0.0261 113 TRP B N   
2483 C CA  . TRP B 111 ? 0.4612 0.3897 0.4196 0.0010  0.0048  -0.0315 113 TRP B CA  
2484 C C   . TRP B 111 ? 0.4731 0.4084 0.4213 -0.0021 0.0176  -0.0216 113 TRP B C   
2485 O O   . TRP B 111 ? 0.4845 0.4166 0.4223 -0.0015 0.0165  -0.0110 113 TRP B O   
2486 C CB  . TRP B 111 ? 0.4565 0.3788 0.4300 0.0045  -0.0026 -0.0353 113 TRP B CB  
2487 C CG  . TRP B 111 ? 0.4571 0.3750 0.4468 0.0093  -0.0147 -0.0473 113 TRP B CG  
2488 C CD1 . TRP B 111 ? 0.4749 0.3776 0.4572 0.0133  -0.0310 -0.0473 113 TRP B CD1 
2489 C CD2 . TRP B 111 ? 0.4574 0.3849 0.4726 0.0112  -0.0111 -0.0611 113 TRP B CD2 
2490 N NE1 . TRP B 111 ? 0.4730 0.3751 0.4753 0.0193  -0.0397 -0.0594 113 TRP B NE1 
2491 C CE2 . TRP B 111 ? 0.4617 0.3807 0.4874 0.0183  -0.0273 -0.0687 113 TRP B CE2 
2492 C CE3 . TRP B 111 ? 0.4641 0.4052 0.4944 0.0076  0.0053  -0.0681 113 TRP B CE3 
2493 C CZ2 . TRP B 111 ? 0.4715 0.3981 0.5264 0.0230  -0.0283 -0.0834 113 TRP B CZ2 
2494 C CZ3 . TRP B 111 ? 0.4664 0.4148 0.5251 0.0106  0.0063  -0.0837 113 TRP B CZ3 
2495 C CH2 . TRP B 111 ? 0.4693 0.4120 0.5420 0.0188  -0.0106 -0.0913 113 TRP B CH2 
2496 N N   . LEU B 112 ? 0.4853 0.4277 0.4343 -0.0052 0.0301  -0.0246 114 LEU B N   
2497 C CA  . LEU B 112 ? 0.5177 0.4626 0.4502 -0.0074 0.0410  -0.0133 114 LEU B CA  
2498 C C   . LEU B 112 ? 0.5326 0.4759 0.4752 -0.0091 0.0549  -0.0155 114 LEU B C   
2499 O O   . LEU B 112 ? 0.5393 0.4851 0.4988 -0.0117 0.0621  -0.0283 114 LEU B O   
2500 C CB  . LEU B 112 ? 0.5238 0.4735 0.4378 -0.0111 0.0444  -0.0117 114 LEU B CB  
2501 C CG  . LEU B 112 ? 0.5386 0.4888 0.4328 -0.0130 0.0551  -0.0011 114 LEU B CG  
2502 C CD1 . LEU B 112 ? 0.5426 0.4948 0.4243 -0.0091 0.0487  0.0142  114 LEU B CD1 
2503 C CD2 . LEU B 112 ? 0.5463 0.4992 0.4227 -0.0183 0.0588  -0.0040 114 LEU B CD2 
2504 N N   . ILE B 113 ? 0.5291 0.4677 0.4622 -0.0078 0.0597  -0.0035 115 ILE B N   
2505 C CA  . ILE B 113 ? 0.5430 0.4759 0.4786 -0.0102 0.0748  -0.0025 115 ILE B CA  
2506 C C   . ILE B 113 ? 0.5764 0.5054 0.4855 -0.0104 0.0836  0.0107  115 ILE B C   
2507 O O   . ILE B 113 ? 0.5595 0.4880 0.4552 -0.0057 0.0777  0.0239  115 ILE B O   
2508 C CB  . ILE B 113 ? 0.5533 0.4791 0.4953 -0.0077 0.0726  0.0022  115 ILE B CB  
2509 C CG1 . ILE B 113 ? 0.5406 0.4675 0.5000 -0.0061 0.0576  -0.0068 115 ILE B CG1 
2510 C CG2 . ILE B 113 ? 0.5663 0.4842 0.5127 -0.0115 0.0891  0.0012  115 ILE B CG2 
2511 C CD1 . ILE B 113 ? 0.5212 0.4542 0.5042 -0.0079 0.0553  -0.0233 115 ILE B CD1 
2512 N N   . THR B 114 ? 0.6312 0.5569 0.5323 -0.0156 0.0977  0.0070  116 THR B N   
2513 C CA  . THR B 114 ? 0.6843 0.6022 0.5548 -0.0156 0.1053  0.0203  116 THR B CA  
2514 C C   . THR B 114 ? 0.7297 0.6324 0.5957 -0.0175 0.1220  0.0245  116 THR B C   
2515 O O   . THR B 114 ? 0.7321 0.6314 0.6127 -0.0242 0.1354  0.0120  116 THR B O   
2516 C CB  . THR B 114 ? 0.7164 0.6355 0.5702 -0.0213 0.1098  0.0152  116 THR B CB  
2517 O OG1 . THR B 114 ? 0.7192 0.6507 0.5826 -0.0212 0.0966  0.0068  116 THR B OG1 
2518 C CG2 . THR B 114 ? 0.7572 0.6691 0.5730 -0.0196 0.1101  0.0319  116 THR B CG2 
2519 N N   . LEU B 115 ? 0.7651 0.6585 0.6122 -0.0115 0.1221  0.0415  117 LEU B N   
2520 C CA  . LEU B 115 ? 0.8038 0.6782 0.6430 -0.0121 0.1381  0.0477  117 LEU B CA  
2521 C C   . LEU B 115 ? 0.8662 0.7250 0.6687 -0.0126 0.1478  0.0595  117 LEU B C   
2522 O O   . LEU B 115 ? 0.8854 0.7483 0.6677 -0.0062 0.1359  0.0717  117 LEU B O   
2523 C CB  . LEU B 115 ? 0.7979 0.6692 0.6417 -0.0036 0.1316  0.0589  117 LEU B CB  
2524 C CG  . LEU B 115 ? 0.8048 0.6870 0.6766 -0.0030 0.1207  0.0499  117 LEU B CG  
2525 C CD1 . LEU B 115 ? 0.8172 0.6904 0.6890 0.0035  0.1206  0.0604  117 LEU B CD1 
2526 C CD2 . LEU B 115 ? 0.8024 0.6856 0.6983 -0.0115 0.1278  0.0318  117 LEU B CD2 
2527 N N   . ASN B 116 ? 0.8914 0.7318 0.6842 -0.0206 0.1688  0.0555  118 ASN B N   
2528 C CA  . ASN B 116 ? 0.9510 0.7695 0.7025 -0.0214 0.1793  0.0679  118 ASN B CA  
2529 C C   . ASN B 116 ? 0.9889 0.7906 0.7205 -0.0100 0.1772  0.0893  118 ASN B C   
2530 O O   . ASN B 116 ? 0.9885 0.7958 0.7405 -0.0030 0.1705  0.0925  118 ASN B O   
2531 C CB  . ASN B 116 ? 0.9788 0.7796 0.7231 -0.0351 0.2053  0.0563  118 ASN B CB  
2532 C CG  . ASN B 116 ? 1.0423 0.8283 0.8013 -0.0405 0.2239  0.0512  118 ASN B CG  
2533 O OD1 . ASN B 116 ? 1.0446 0.8225 0.8059 -0.0334 0.2217  0.0614  118 ASN B OD1 
2534 N ND2 . ASN B 116 ? 1.0728 0.8548 0.8431 -0.0543 0.2445  0.0339  118 ASN B ND2 
2535 N N   . LYS B 117 ? 1.0231 0.8031 0.7141 -0.0079 0.1827  0.1035  119 LYS B N   
2536 C CA  . LYS B 117 ? 1.0583 0.8205 0.7269 0.0049  0.1795  0.1251  119 LYS B CA  
2537 C C   . LYS B 117 ? 1.0702 0.8129 0.7503 0.0051  0.1956  0.1260  119 LYS B C   
2538 O O   . LYS B 117 ? 1.0650 0.8063 0.7516 0.0171  0.1885  0.1376  119 LYS B O   
2539 C CB  . LYS B 117 ? 1.1247 0.8606 0.7420 0.0051  0.1848  0.1387  119 LYS B CB  
2540 C CG  . LYS B 117 ? 1.2112 0.9633 0.8093 0.0052  0.1674  0.1401  119 LYS B CG  
2541 C CD  . LYS B 117 ? 1.2853 1.0378 0.8772 -0.0119 0.1800  0.1217  119 LYS B CD  
2542 C CE  . LYS B 117 ? 1.3515 1.1000 0.9016 -0.0141 0.1714  0.1273  119 LYS B CE  
2543 N NZ  . LYS B 117 ? 1.3711 1.1391 0.9344 -0.0260 0.1714  0.1074  119 LYS B NZ  
2544 N N   . GLN B 118 ? 1.0835 0.8112 0.7669 -0.0087 0.2182  0.1129  120 GLN B N   
2545 C CA  . GLN B 118 ? 1.0998 0.8110 0.7983 -0.0128 0.2354  0.1086  120 GLN B CA  
2546 C C   . GLN B 118 ? 1.0782 0.8128 0.8177 -0.0088 0.2229  0.1012  120 GLN B C   
2547 O O   . GLN B 118 ? 1.0820 0.8045 0.8249 -0.0023 0.2253  0.1090  120 GLN B O   
2548 C CB  . GLN B 118 ? 1.1420 0.8443 0.8473 -0.0312 0.2594  0.0898  120 GLN B CB  
2549 C CG  . GLN B 118 ? 1.2578 0.9240 0.9178 -0.0377 0.2805  0.0975  120 GLN B CG  
2550 C CD  . GLN B 118 ? 1.3597 1.0266 1.0249 -0.0561 0.2999  0.0774  120 GLN B CD  
2551 O OE1 . GLN B 118 ? 1.3763 1.0662 1.0511 -0.0598 0.2918  0.0665  120 GLN B OE1 
2552 N NE2 . GLN B 118 ? 1.3921 1.0328 1.0516 -0.0682 0.3272  0.0714  120 GLN B NE2 
2553 N N   . GLN B 119 ? 1.0526 0.8177 0.8205 -0.0127 0.2099  0.0862  121 GLN B N   
2554 C CA  . GLN B 119 ? 1.0301 0.8145 0.8337 -0.0115 0.1988  0.0767  121 GLN B CA  
2555 C C   . GLN B 119 ? 1.0148 0.8084 0.8198 0.0022  0.1805  0.0897  121 GLN B C   
2556 O O   . GLN B 119 ? 1.0058 0.8102 0.8346 0.0029  0.1729  0.0832  121 GLN B O   
2557 C CB  . GLN B 119 ? 1.0365 0.8467 0.8665 -0.0188 0.1903  0.0578  121 GLN B CB  
2558 C CG  . GLN B 119 ? 1.0926 0.8996 0.9323 -0.0326 0.2082  0.0409  121 GLN B CG  
2559 C CD  . GLN B 119 ? 1.1514 0.9848 1.0155 -0.0355 0.1961  0.0253  121 GLN B CD  
2560 O OE1 . GLN B 119 ? 1.1648 1.0042 1.0157 -0.0356 0.1926  0.0255  121 GLN B OE1 
2561 N NE2 . GLN B 119 ? 1.1578 1.0061 1.0562 -0.0374 0.1886  0.0116  121 GLN B NE2 
2562 N N   . ARG B 120 ? 1.0095 0.7999 0.7899 0.0128  0.1730  0.1071  122 ARG B N   
2563 C CA  . ARG B 120 ? 0.9916 0.7889 0.7750 0.0266  0.1593  0.1204  122 ARG B CA  
2564 C C   . ARG B 120 ? 0.9889 0.7663 0.7784 0.0300  0.1711  0.1246  122 ARG B C   
2565 O O   . ARG B 120 ? 0.9805 0.7669 0.7907 0.0327  0.1649  0.1214  122 ARG B O   
2566 C CB  . ARG B 120 ? 1.0125 0.8075 0.7674 0.0370  0.1509  0.1381  122 ARG B CB  
2567 C CG  . ARG B 120 ? 1.0421 0.8290 0.7905 0.0531  0.1465  0.1568  122 ARG B CG  
2568 C CD  . ARG B 120 ? 1.0480 0.8631 0.8193 0.0611  0.1279  0.1578  122 ARG B CD  
2569 N NE  . ARG B 120 ? 1.0701 0.9101 0.8380 0.0601  0.1105  0.1562  122 ARG B NE  
2570 C CZ  . ARG B 120 ? 1.1039 0.9472 0.8502 0.0678  0.0999  0.1688  122 ARG B CZ  
2571 N NH1 . ARG B 120 ? 1.0857 0.9523 0.8303 0.0643  0.0847  0.1645  122 ARG B NH1 
2572 N NH2 . ARG B 120 ? 1.1337 0.9554 0.8583 0.0789  0.1040  0.1858  122 ARG B NH2 
2573 N N   . ARG B 121 ? 0.9984 0.7460 0.7671 0.0289  0.1894  0.1313  123 ARG B N   
2574 C CA  . ARG B 121 ? 1.0100 0.7333 0.7796 0.0316  0.2033  0.1359  123 ARG B CA  
2575 C C   . ARG B 121 ? 0.9667 0.6924 0.7623 0.0183  0.2115  0.1165  123 ARG B C   
2576 O O   . ARG B 121 ? 0.9707 0.6935 0.7797 0.0211  0.2115  0.1157  123 ARG B O   
2577 C CB  . ARG B 121 ? 1.0809 0.7678 0.8166 0.0338  0.2211  0.1490  123 ARG B CB  
2578 C CG  . ARG B 121 ? 1.1753 0.8558 0.8850 0.0514  0.2102  0.1717  123 ARG B CG  
2579 C CD  . ARG B 121 ? 1.2982 0.9353 0.9700 0.0559  0.2275  0.1873  123 ARG B CD  
2580 N NE  . ARG B 121 ? 1.3729 0.9827 1.0462 0.0433  0.2529  0.1778  123 ARG B NE  
2581 C CZ  . ARG B 121 ? 1.4130 1.0014 1.0918 0.0473  0.2647  0.1812  123 ARG B CZ  
2582 N NH1 . ARG B 121 ? 1.4157 0.9814 1.0958 0.0327  0.2877  0.1699  123 ARG B NH1 
2583 N NH2 . ARG B 121 ? 1.4122 1.0019 1.0963 0.0655  0.2546  0.1950  123 ARG B NH2 
2584 N N   . SER B 122 ? 0.9214 0.6535 0.7253 0.0041  0.2174  0.1004  124 SER B N   
2585 C CA  . SER B 122 ? 0.8925 0.6302 0.7233 -0.0084 0.2223  0.0809  124 SER B CA  
2586 C C   . SER B 122 ? 0.8357 0.6020 0.6942 -0.0085 0.2018  0.0696  124 SER B C   
2587 O O   . SER B 122 ? 0.8268 0.5907 0.7000 -0.0119 0.2019  0.0622  124 SER B O   
2588 C CB  . SER B 122 ? 0.9254 0.6618 0.7593 -0.0230 0.2364  0.0666  124 SER B CB  
2589 O OG  . SER B 122 ? 0.9738 0.7296 0.8058 -0.0225 0.2258  0.0644  124 SER B OG  
2590 N N   . ASP B 123 ? 0.7955 0.5855 0.6582 -0.0055 0.1849  0.0681  125 ASP B N   
2591 C CA  . ASP B 123 ? 0.7490 0.5622 0.6357 -0.0078 0.1674  0.0551  125 ASP B CA  
2592 C C   . ASP B 123 ? 0.6926 0.5203 0.5782 0.0021  0.1483  0.0632  125 ASP B C   
2593 O O   . ASP B 123 ? 0.6752 0.5149 0.5763 0.0001  0.1357  0.0537  125 ASP B O   
2594 C CB  . ASP B 123 ? 0.7693 0.5986 0.6691 -0.0157 0.1650  0.0402  125 ASP B CB  
2595 C CG  . ASP B 123 ? 0.8449 0.6665 0.7546 -0.0277 0.1831  0.0271  125 ASP B CG  
2596 O OD1 . ASP B 123 ? 0.8518 0.6672 0.7755 -0.0335 0.1884  0.0190  125 ASP B OD1 
2597 O OD2 . ASP B 123 ? 0.8830 0.7049 0.7865 -0.0326 0.1927  0.0237  125 ASP B OD2 
2598 N N   . LEU B 124 ? 0.6549 0.4816 0.5231 0.0123  0.1456  0.0797  126 LEU B N   
2599 C CA  . LEU B 124 ? 0.6114 0.4553 0.4820 0.0198  0.1284  0.0851  126 LEU B CA  
2600 C C   . LEU B 124 ? 0.5858 0.4287 0.4689 0.0208  0.1238  0.0823  126 LEU B C   
2601 O O   . LEU B 124 ? 0.5528 0.4084 0.4461 0.0180  0.1109  0.0740  126 LEU B O   
2602 C CB  . LEU B 124 ? 0.6086 0.4515 0.4615 0.0309  0.1270  0.1031  126 LEU B CB  
2603 C CG  . LEU B 124 ? 0.6232 0.4873 0.4792 0.0384  0.1099  0.1092  126 LEU B CG  
2604 C CD1 . LEU B 124 ? 0.6075 0.4904 0.4679 0.0320  0.0979  0.0990  126 LEU B CD1 
2605 C CD2 . LEU B 124 ? 0.6618 0.5262 0.5009 0.0491  0.1075  0.1260  126 LEU B CD2 
2606 N N   . ASN B 125 ? 0.5804 0.4048 0.4601 0.0243  0.1355  0.0890  127 ASN B N   
2607 C CA  . ASN B 125 ? 0.5682 0.3883 0.4554 0.0253  0.1337  0.0875  127 ASN B CA  
2608 C C   . ASN B 125 ? 0.5424 0.3611 0.4400 0.0141  0.1303  0.0709  127 ASN B C   
2609 O O   . ASN B 125 ? 0.5457 0.3693 0.4476 0.0127  0.1199  0.0661  127 ASN B O   
2610 C CB  . ASN B 125 ? 0.6148 0.4133 0.4955 0.0315  0.1491  0.0977  127 ASN B CB  
2611 C CG  . ASN B 125 ? 0.7100 0.5114 0.5826 0.0453  0.1485  0.1149  127 ASN B CG  
2612 O OD1 . ASN B 125 ? 0.7667 0.5883 0.6440 0.0511  0.1353  0.1190  127 ASN B OD1 
2613 N ND2 . ASN B 125 ? 0.7168 0.4981 0.5769 0.0510  0.1619  0.1254  127 ASN B ND2 
2614 N N   . ARG B 126 ? 0.5252 0.3366 0.4263 0.0059  0.1388  0.0619  128 ARG B N   
2615 C CA  . ARG B 126 ? 0.5105 0.3235 0.4248 -0.0044 0.1335  0.0450  128 ARG B CA  
2616 C C   . ARG B 126 ? 0.4707 0.3041 0.3939 -0.0051 0.1143  0.0370  128 ARG B C   
2617 O O   . ARG B 126 ? 0.4636 0.2975 0.3901 -0.0073 0.1026  0.0304  128 ARG B O   
2618 C CB  . ARG B 126 ? 0.5341 0.3405 0.4549 -0.0133 0.1476  0.0360  128 ARG B CB  
2619 C CG  . ARG B 126 ? 0.5657 0.3798 0.5062 -0.0237 0.1406  0.0168  128 ARG B CG  
2620 C CD  . ARG B 126 ? 0.5977 0.4036 0.5387 -0.0266 0.1328  0.0115  128 ARG B CD  
2621 N NE  . ARG B 126 ? 0.6466 0.4294 0.5775 -0.0289 0.1498  0.0159  128 ARG B NE  
2622 C CZ  . ARG B 126 ? 0.6661 0.4346 0.5897 -0.0307 0.1490  0.0152  128 ARG B CZ  
2623 N NH1 . ARG B 126 ? 0.6606 0.4344 0.5832 -0.0307 0.1313  0.0107  128 ARG B NH1 
2624 N NH2 . ARG B 126 ? 0.6345 0.3803 0.5491 -0.0328 0.1671  0.0188  128 ARG B NH2 
2625 N N   . PHE B 127 ? 0.4683 0.3148 0.3921 -0.0036 0.1120  0.0377  129 PHE B N   
2626 C CA  . PHE B 127 ? 0.4770 0.3402 0.4089 -0.0042 0.0960  0.0297  129 PHE B CA  
2627 C C   . PHE B 127 ? 0.4693 0.3366 0.3940 0.0009  0.0831  0.0358  129 PHE B C   
2628 O O   . PHE B 127 ? 0.4633 0.3349 0.3929 -0.0009 0.0694  0.0278  129 PHE B O   
2629 C CB  . PHE B 127 ? 0.4886 0.3627 0.4197 -0.0041 0.0986  0.0295  129 PHE B CB  
2630 C CG  . PHE B 127 ? 0.5351 0.4105 0.4796 -0.0117 0.1083  0.0169  129 PHE B CG  
2631 C CD1 . PHE B 127 ? 0.5570 0.4214 0.5091 -0.0178 0.1202  0.0113  129 PHE B CD1 
2632 C CD2 . PHE B 127 ? 0.5576 0.4451 0.5081 -0.0138 0.1072  0.0096  129 PHE B CD2 
2633 C CE1 . PHE B 127 ? 0.5626 0.4302 0.5305 -0.0262 0.1308  -0.0019 129 PHE B CE1 
2634 C CE2 . PHE B 127 ? 0.5623 0.4520 0.5280 -0.0214 0.1188  -0.0032 129 PHE B CE2 
2635 C CZ  . PHE B 127 ? 0.5595 0.4404 0.5351 -0.0277 0.1304  -0.0092 129 PHE B CZ  
2636 N N   . TRP B 128 ? 0.4548 0.3200 0.3685 0.0073  0.0875  0.0496  130 TRP B N   
2637 C CA  . TRP B 128 ? 0.4368 0.3072 0.3461 0.0110  0.0780  0.0545  130 TRP B CA  
2638 C C   . TRP B 128 ? 0.4254 0.2828 0.3340 0.0079  0.0757  0.0501  130 TRP B C   
2639 O O   . TRP B 128 ? 0.4161 0.2752 0.3224 0.0059  0.0641  0.0459  130 TRP B O   
2640 C CB  . TRP B 128 ? 0.4232 0.2975 0.3260 0.0194  0.0835  0.0695  130 TRP B CB  
2641 C CG  . TRP B 128 ? 0.3918 0.2752 0.2946 0.0225  0.0754  0.0736  130 TRP B CG  
2642 C CD1 . TRP B 128 ? 0.3949 0.2753 0.2987 0.0278  0.0808  0.0815  130 TRP B CD1 
2643 C CD2 . TRP B 128 ? 0.3804 0.2773 0.2835 0.0199  0.0625  0.0692  130 TRP B CD2 
2644 N NE1 . TRP B 128 ? 0.3912 0.2843 0.2976 0.0279  0.0725  0.0817  130 TRP B NE1 
2645 C CE2 . TRP B 128 ? 0.3891 0.2913 0.2934 0.0225  0.0611  0.0744  130 TRP B CE2 
2646 C CE3 . TRP B 128 ? 0.3840 0.2882 0.2872 0.0153  0.0532  0.0606  130 TRP B CE3 
2647 C CZ2 . TRP B 128 ? 0.3904 0.3040 0.2946 0.0193  0.0510  0.0710  130 TRP B CZ2 
2648 C CZ3 . TRP B 128 ? 0.3901 0.3031 0.2917 0.0131  0.0429  0.0579  130 TRP B CZ3 
2649 C CH2 . TRP B 128 ? 0.3887 0.3063 0.2899 0.0145  0.0419  0.0632  130 TRP B CH2 
2650 N N   . LEU B 129 ? 0.4319 0.2733 0.3392 0.0065  0.0873  0.0508  131 LEU B N   
2651 C CA  . LEU B 129 ? 0.4407 0.2665 0.3437 0.0016  0.0860  0.0450  131 LEU B CA  
2652 C C   . LEU B 129 ? 0.4442 0.2704 0.3507 -0.0051 0.0716  0.0314  131 LEU B C   
2653 O O   . LEU B 129 ? 0.4602 0.2797 0.3582 -0.0073 0.0613  0.0282  131 LEU B O   
2654 C CB  . LEU B 129 ? 0.4666 0.2743 0.3679 -0.0005 0.1018  0.0456  131 LEU B CB  
2655 C CG  . LEU B 129 ? 0.4928 0.2815 0.3864 -0.0075 0.1013  0.0380  131 LEU B CG  
2656 C CD1 . LEU B 129 ? 0.5282 0.3119 0.4119 -0.0052 0.0999  0.0430  131 LEU B CD1 
2657 C CD2 . LEU B 129 ? 0.5076 0.2788 0.3995 -0.0105 0.1176  0.0377  131 LEU B CD2 
2658 N N   . GLU B 130 ? 0.4437 0.2772 0.3627 -0.0080 0.0708  0.0232  132 GLU B N   
2659 C CA  . GLU B 130 ? 0.4497 0.2858 0.3770 -0.0124 0.0556  0.0097  132 GLU B CA  
2660 C C   . GLU B 130 ? 0.4614 0.3049 0.3846 -0.0092 0.0399  0.0097  132 GLU B C   
2661 O O   . GLU B 130 ? 0.4766 0.3121 0.3949 -0.0111 0.0257  0.0034  132 GLU B O   
2662 C CB  . GLU B 130 ? 0.4601 0.3065 0.4075 -0.0160 0.0589  -0.0006 132 GLU B CB  
2663 C CG  . GLU B 130 ? 0.5336 0.3705 0.4846 -0.0214 0.0756  -0.0024 132 GLU B CG  
2664 C CD  . GLU B 130 ? 0.5821 0.4023 0.5270 -0.0273 0.0738  -0.0077 132 GLU B CD  
2665 O OE1 . GLU B 130 ? 0.5424 0.3602 0.4846 -0.0288 0.0563  -0.0145 132 GLU B OE1 
2666 O OE2 . GLU B 130 ? 0.5908 0.3976 0.5310 -0.0307 0.0902  -0.0050 132 GLU B OE2 
2667 N N   . THR B 131 ? 0.4579 0.3141 0.3804 -0.0046 0.0423  0.0171  133 THR B N   
2668 C CA  . THR B 131 ? 0.4569 0.3188 0.3737 -0.0025 0.0302  0.0178  133 THR B CA  
2669 C C   . THR B 131 ? 0.4598 0.3077 0.3599 -0.0036 0.0262  0.0218  133 THR B C   
2670 O O   . THR B 131 ? 0.4665 0.3063 0.3588 -0.0053 0.0134  0.0169  133 THR B O   
2671 C CB  . THR B 131 ? 0.4461 0.3234 0.3632 0.0011  0.0354  0.0251  133 THR B CB  
2672 O OG1 . THR B 131 ? 0.4471 0.3331 0.3756 0.0005  0.0408  0.0204  133 THR B OG1 
2673 C CG2 . THR B 131 ? 0.4339 0.3169 0.3454 0.0016  0.0249  0.0247  133 THR B CG2 
2674 N N   . LEU B 132 ? 0.4694 0.3124 0.3634 -0.0026 0.0381  0.0305  134 LEU B N   
2675 C CA  . LEU B 132 ? 0.4740 0.3033 0.3535 -0.0047 0.0389  0.0336  134 LEU B CA  
2676 C C   . LEU B 132 ? 0.4757 0.2830 0.3428 -0.0105 0.0310  0.0254  134 LEU B C   
2677 O O   . LEU B 132 ? 0.4612 0.2560 0.3125 -0.0136 0.0235  0.0241  134 LEU B O   
2678 C CB  . LEU B 132 ? 0.4760 0.3037 0.3564 -0.0017 0.0551  0.0426  134 LEU B CB  
2679 C CG  . LEU B 132 ? 0.4692 0.3169 0.3590 0.0055  0.0611  0.0526  134 LEU B CG  
2680 C CD1 . LEU B 132 ? 0.4557 0.2988 0.3478 0.0103  0.0759  0.0611  134 LEU B CD1 
2681 C CD2 . LEU B 132 ? 0.4695 0.3304 0.3582 0.0055  0.0527  0.0537  134 LEU B CD2 
2682 N N   . LEU B 133 ? 0.4826 0.2842 0.3552 -0.0128 0.0322  0.0196  135 LEU B N   
2683 C CA  . LEU B 133 ? 0.5039 0.2852 0.3637 -0.0187 0.0224  0.0114  135 LEU B CA  
2684 C C   . LEU B 133 ? 0.5184 0.2994 0.3768 -0.0183 0.0016  0.0041  135 LEU B C   
2685 O O   . LEU B 133 ? 0.5433 0.3039 0.3816 -0.0217 -0.0095 0.0008  135 LEU B O   
2686 C CB  . LEU B 133 ? 0.5037 0.2810 0.3718 -0.0225 0.0285  0.0055  135 LEU B CB  
2687 C CG  . LEU B 133 ? 0.5271 0.2998 0.3957 -0.0224 0.0500  0.0124  135 LEU B CG  
2688 C CD1 . LEU B 133 ? 0.5340 0.3011 0.4104 -0.0280 0.0556  0.0046  135 LEU B CD1 
2689 C CD2 . LEU B 133 ? 0.5383 0.2923 0.3868 -0.0242 0.0582  0.0178  135 LEU B CD2 
2690 N N   . CYS B 134 ? 0.4995 0.3006 0.3769 -0.0138 -0.0032 0.0016  136 CYS B N   
2691 C CA  . CYS B 134 ? 0.5009 0.3027 0.3803 -0.0113 -0.0215 -0.0050 136 CYS B CA  
2692 C C   . CYS B 134 ? 0.5043 0.2929 0.3609 -0.0114 -0.0270 0.0002  136 CYS B C   
2693 O O   . CYS B 134 ? 0.5204 0.2934 0.3641 -0.0111 -0.0430 -0.0039 136 CYS B O   
2694 C CB  . CYS B 134 ? 0.5172 0.3432 0.4223 -0.0070 -0.0208 -0.0088 136 CYS B CB  
2695 S SG  . CYS B 134 ? 0.5421 0.3816 0.4765 -0.0083 -0.0194 -0.0204 136 CYS B SG  
2696 N N   . LEU B 135 ? 0.4709 0.2658 0.3233 -0.0116 -0.0141 0.0089  137 LEU B N   
2697 C CA  . LEU B 135 ? 0.4653 0.2497 0.2987 -0.0137 -0.0160 0.0128  137 LEU B CA  
2698 C C   . LEU B 135 ? 0.5065 0.2617 0.3124 -0.0198 -0.0154 0.0136  137 LEU B C   
2699 O O   . LEU B 135 ? 0.5160 0.2490 0.3000 -0.0222 -0.0276 0.0109  137 LEU B O   
2700 C CB  . LEU B 135 ? 0.4339 0.2375 0.2750 -0.0127 -0.0029 0.0205  137 LEU B CB  
2701 C CG  . LEU B 135 ? 0.4278 0.2512 0.2803 -0.0098 -0.0064 0.0202  137 LEU B CG  
2702 C CD1 . LEU B 135 ? 0.4243 0.2593 0.2944 -0.0058 -0.0119 0.0140  137 LEU B CD1 
2703 C CD2 . LEU B 135 ? 0.4386 0.2817 0.2988 -0.0088 0.0057  0.0282  137 LEU B CD2 
2704 N N   . ILE B 136 ? 0.5248 0.2772 0.3292 -0.0224 -0.0005 0.0174  138 ILE B N   
2705 C CA  . ILE B 136 ? 0.5669 0.2908 0.3438 -0.0295 0.0042  0.0178  138 ILE B CA  
2706 C C   . ILE B 136 ? 0.6069 0.3057 0.3644 -0.0329 -0.0106 0.0110  138 ILE B C   
2707 O O   . ILE B 136 ? 0.6266 0.2963 0.3526 -0.0389 -0.0140 0.0104  138 ILE B O   
2708 C CB  . ILE B 136 ? 0.5701 0.2956 0.3512 -0.0309 0.0252  0.0227  138 ILE B CB  
2709 C CG1 . ILE B 136 ? 0.5849 0.3138 0.3788 -0.0293 0.0299  0.0207  138 ILE B CG1 
2710 C CG2 . ILE B 136 ? 0.5489 0.3003 0.3492 -0.0263 0.0361  0.0298  138 ILE B CG2 
2711 C CD1 . ILE B 136 ? 0.5907 0.3140 0.3848 -0.0305 0.0480  0.0241  138 ILE B CD1 
2712 N N   . GLY B 137 ? 0.6225 0.3321 0.3977 -0.0296 -0.0194 0.0054  139 GLY B N   
2713 C CA  . GLY B 137 ? 0.6656 0.3559 0.4269 -0.0323 -0.0364 -0.0022 139 GLY B CA  
2714 C C   . GLY B 137 ? 0.6760 0.3588 0.4303 -0.0281 -0.0598 -0.0060 139 GLY B C   
2715 O O   . GLY B 137 ? 0.6935 0.3589 0.4340 -0.0291 -0.0773 -0.0118 139 GLY B O   
2716 N N   . GLU B 138 ? 0.6567 0.3515 0.4196 -0.0231 -0.0611 -0.0031 140 GLU B N   
2717 C CA  . GLU B 138 ? 0.6586 0.3458 0.4170 -0.0177 -0.0815 -0.0064 140 GLU B CA  
2718 C C   . GLU B 138 ? 0.6532 0.3549 0.4379 -0.0113 -0.0981 -0.0156 140 GLU B C   
2719 O O   . GLU B 138 ? 0.6744 0.3585 0.4470 -0.0086 -0.1193 -0.0202 140 GLU B O   
2720 C CB  . GLU B 138 ? 0.6806 0.3270 0.3944 -0.0221 -0.0917 -0.0043 140 GLU B CB  
2721 C CG  . GLU B 138 ? 0.7223 0.3539 0.4116 -0.0301 -0.0735 0.0028  140 GLU B CG  
2722 C CD  . GLU B 138 ? 0.7273 0.3689 0.4221 -0.0289 -0.0674 0.0062  140 GLU B CD  
2723 O OE1 . GLU B 138 ? 0.7216 0.3567 0.4135 -0.0238 -0.0821 0.0043  140 GLU B OE1 
2724 O OE2 . GLU B 138 ? 0.7296 0.3849 0.4316 -0.0329 -0.0483 0.0105  140 GLU B OE2 
2725 N N   . SER B 139 ? 0.6227 0.3566 0.4436 -0.0088 -0.0879 -0.0183 141 SER B N   
2726 C CA  . SER B 139 ? 0.6100 0.3629 0.4626 -0.0052 -0.0967 -0.0285 141 SER B CA  
2727 C C   . SER B 139 ? 0.6181 0.3816 0.4912 0.0038  -0.1131 -0.0353 141 SER B C   
2728 O O   . SER B 139 ? 0.6234 0.4044 0.5267 0.0069  -0.1209 -0.0455 141 SER B O   
2729 C CB  . SER B 139 ? 0.6076 0.3869 0.4876 -0.0073 -0.0761 -0.0286 141 SER B CB  
2730 O OG  . SER B 139 ? 0.6415 0.4097 0.5055 -0.0144 -0.0618 -0.0235 141 SER B OG  
2731 N N   . PHE B 140 ? 0.6113 0.3646 0.4705 0.0078  -0.1175 -0.0310 142 PHE B N   
2732 C CA  . PHE B 140 ? 0.6118 0.3749 0.4925 0.0171  -0.1302 -0.0377 142 PHE B CA  
2733 C C   . PHE B 140 ? 0.6504 0.3843 0.5083 0.0230  -0.1549 -0.0386 142 PHE B C   
2734 O O   . PHE B 140 ? 0.6431 0.3750 0.5073 0.0310  -0.1639 -0.0408 142 PHE B O   
2735 C CB  . PHE B 140 ? 0.5893 0.3652 0.4760 0.0177  -0.1157 -0.0340 142 PHE B CB  
2736 C CG  . PHE B 140 ? 0.5593 0.3597 0.4621 0.0125  -0.0933 -0.0314 142 PHE B CG  
2737 C CD1 . PHE B 140 ? 0.5390 0.3637 0.4750 0.0133  -0.0878 -0.0390 142 PHE B CD1 
2738 C CD2 . PHE B 140 ? 0.5630 0.3607 0.4472 0.0067  -0.0780 -0.0214 142 PHE B CD2 
2739 C CE1 . PHE B 140 ? 0.5179 0.3591 0.4631 0.0086  -0.0674 -0.0355 142 PHE B CE1 
2740 C CE2 . PHE B 140 ? 0.5423 0.3599 0.4394 0.0037  -0.0597 -0.0178 142 PHE B CE2 
2741 C CZ  . PHE B 140 ? 0.5158 0.3529 0.4407 0.0048  -0.0546 -0.0243 142 PHE B CZ  
2742 N N   . ASP B 141 ? 0.6959 0.4044 0.5251 0.0193  -0.1660 -0.0368 143 ASP B N   
2743 C CA  . ASP B 141 ? 0.7535 0.4292 0.5545 0.0249  -0.1914 -0.0365 143 ASP B CA  
2744 C C   . ASP B 141 ? 0.7846 0.4330 0.5526 0.0252  -0.1886 -0.0280 143 ASP B C   
2745 O O   . ASP B 141 ? 0.8062 0.4522 0.5585 0.0161  -0.1676 -0.0212 143 ASP B O   
2746 C CB  . ASP B 141 ? 0.7830 0.4755 0.6204 0.0369  -0.2148 -0.0480 143 ASP B CB  
2747 C CG  . ASP B 141 ? 0.8750 0.5939 0.7432 0.0329  -0.2140 -0.0571 143 ASP B CG  
2748 O OD1 . ASP B 141 ? 0.8983 0.5995 0.7436 0.0277  -0.2249 -0.0574 143 ASP B OD1 
2749 O OD2 . ASP B 141 ? 0.9069 0.6622 0.8196 0.0335  -0.2008 -0.0642 143 ASP B OD2 
2750 N N   . ASP B 142 ? 0.7981 0.4258 0.5555 0.0348  -0.2079 -0.0286 144 ASP B N   
2751 C CA  . ASP B 142 ? 0.8403 0.4396 0.5648 0.0332  -0.2027 -0.0213 144 ASP B CA  
2752 C C   . ASP B 142 ? 0.8048 0.4313 0.5531 0.0307  -0.1807 -0.0213 144 ASP B C   
2753 O O   . ASP B 142 ? 0.8230 0.4338 0.5461 0.0235  -0.1681 -0.0152 144 ASP B O   
2754 C CB  . ASP B 142 ? 0.9167 0.4853 0.6248 0.0452  -0.2279 -0.0218 144 ASP B CB  
2755 C CG  . ASP B 142 ? 1.0832 0.6097 0.7457 0.0446  -0.2485 -0.0177 144 ASP B CG  
2756 O OD1 . ASP B 142 ? 1.1105 0.6229 0.7428 0.0317  -0.2379 -0.0130 144 ASP B OD1 
2757 O OD2 . ASP B 142 ? 1.1481 0.6542 0.8038 0.0573  -0.2751 -0.0191 144 ASP B OD2 
2758 N N   . TYR B 143 ? 0.7503 0.4170 0.5459 0.0352  -0.1754 -0.0287 145 TYR B N   
2759 C CA  . TYR B 143 ? 0.7083 0.4008 0.5251 0.0329  -0.1563 -0.0294 145 TYR B CA  
2760 C C   . TYR B 143 ? 0.6786 0.3843 0.4892 0.0210  -0.1331 -0.0228 145 TYR B C   
2761 O O   . TYR B 143 ? 0.6559 0.3806 0.4780 0.0181  -0.1183 -0.0219 145 TYR B O   
2762 C CB  . TYR B 143 ? 0.6933 0.4197 0.5584 0.0410  -0.1578 -0.0399 145 TYR B CB  
2763 C CG  . TYR B 143 ? 0.7252 0.4428 0.6037 0.0546  -0.1799 -0.0474 145 TYR B CG  
2764 C CD1 . TYR B 143 ? 0.7523 0.4456 0.6133 0.0600  -0.1860 -0.0458 145 TYR B CD1 
2765 C CD2 . TYR B 143 ? 0.7217 0.4559 0.6329 0.0624  -0.1943 -0.0568 145 TYR B CD2 
2766 C CE1 . TYR B 143 ? 0.7613 0.4469 0.6379 0.0745  -0.2056 -0.0527 145 TYR B CE1 
2767 C CE2 . TYR B 143 ? 0.7265 0.4560 0.6557 0.0767  -0.2155 -0.0643 145 TYR B CE2 
2768 C CZ  . TYR B 143 ? 0.7639 0.4687 0.6759 0.0836  -0.2210 -0.0618 145 TYR B CZ  
2769 O OH  . TYR B 143 ? 0.8171 0.5150 0.7474 0.0997  -0.2416 -0.0687 145 TYR B OH  
2770 N N   . SER B 144 ? 0.6777 0.3731 0.4702 0.0144  -0.1303 -0.0184 146 SER B N   
2771 C CA  . SER B 144 ? 0.6700 0.3723 0.4536 0.0044  -0.1093 -0.0115 146 SER B CA  
2772 C C   . SER B 144 ? 0.6609 0.3480 0.4194 -0.0018 -0.1003 -0.0058 146 SER B C   
2773 O O   . SER B 144 ? 0.6494 0.3530 0.4126 -0.0079 -0.0829 -0.0017 146 SER B O   
2774 C CB  . SER B 144 ? 0.6962 0.3838 0.4618 -0.0013 -0.1082 -0.0090 146 SER B CB  
2775 O OG  . SER B 144 ? 0.7010 0.4126 0.4948 -0.0001 -0.1048 -0.0131 146 SER B OG  
2776 N N   . ASP B 145 ? 0.6679 0.3239 0.4004 -0.0004 -0.1121 -0.0057 147 ASP B N   
2777 C CA  . ASP B 145 ? 0.6762 0.3163 0.3860 -0.0071 -0.1037 -0.0022 147 ASP B CA  
2778 C C   . ASP B 145 ? 0.6445 0.3118 0.3788 -0.0061 -0.0954 -0.0050 147 ASP B C   
2779 O O   . ASP B 145 ? 0.6682 0.3351 0.3919 -0.0145 -0.0833 -0.0025 147 ASP B O   
2780 C CB  . ASP B 145 ? 0.7317 0.3267 0.4052 -0.0051 -0.1191 -0.0016 147 ASP B CB  
2781 C CG  . ASP B 145 ? 0.8335 0.3915 0.4677 -0.0102 -0.1245 0.0025  147 ASP B CG  
2782 O OD1 . ASP B 145 ? 0.8347 0.3999 0.4661 -0.0184 -0.1111 0.0051  147 ASP B OD1 
2783 O OD2 . ASP B 145 ? 0.8865 0.4064 0.4910 -0.0057 -0.1422 0.0032  147 ASP B OD2 
2784 N N   . ASP B 146 ? 0.5977 0.2877 0.3635 0.0030  -0.1015 -0.0110 148 ASP B N   
2785 C CA  . ASP B 146 ? 0.5757 0.2936 0.3644 0.0027  -0.0915 -0.0142 148 ASP B CA  
2786 C C   . ASP B 146 ? 0.5427 0.2931 0.3481 -0.0025 -0.0753 -0.0108 148 ASP B C   
2787 O O   . ASP B 146 ? 0.5380 0.3079 0.3540 -0.0048 -0.0669 -0.0119 148 ASP B O   
2788 C CB  . ASP B 146 ? 0.5932 0.3240 0.4104 0.0134  -0.1004 -0.0229 148 ASP B CB  
2789 C CG  . ASP B 146 ? 0.6595 0.3644 0.4647 0.0187  -0.1112 -0.0268 148 ASP B CG  
2790 O OD1 . ASP B 146 ? 0.7082 0.3780 0.4834 0.0189  -0.1213 -0.0232 148 ASP B OD1 
2791 O OD2 . ASP B 146 ? 0.6409 0.3587 0.4647 0.0222  -0.1083 -0.0334 148 ASP B OD2 
2792 N N   . VAL B 147 ? 0.5240 0.2786 0.3304 -0.0041 -0.0713 -0.0067 149 VAL B N   
2793 C CA  . VAL B 147 ? 0.4885 0.2698 0.3086 -0.0075 -0.0563 -0.0021 149 VAL B CA  
2794 C C   . VAL B 147 ? 0.4626 0.2424 0.2674 -0.0160 -0.0458 0.0036  149 VAL B C   
2795 O O   . VAL B 147 ? 0.4698 0.2249 0.2507 -0.0212 -0.0459 0.0058  149 VAL B O   
2796 C CB  . VAL B 147 ? 0.4923 0.2746 0.3182 -0.0061 -0.0552 -0.0006 149 VAL B CB  
2797 C CG1 . VAL B 147 ? 0.4907 0.2957 0.3283 -0.0084 -0.0394 0.0054  149 VAL B CG1 
2798 C CG2 . VAL B 147 ? 0.4795 0.2679 0.3259 0.0011  -0.0652 -0.0082 149 VAL B CG2 
2799 N N   . CYS B 148 ? 0.4400 0.2466 0.2587 -0.0177 -0.0367 0.0052  150 CYS B N   
2800 C CA  . CYS B 148 ? 0.4370 0.2524 0.2506 -0.0251 -0.0266 0.0098  150 CYS B CA  
2801 C C   . CYS B 148 ? 0.4245 0.2577 0.2499 -0.0240 -0.0163 0.0165  150 CYS B C   
2802 O O   . CYS B 148 ? 0.4322 0.2617 0.2510 -0.0290 -0.0087 0.0200  150 CYS B O   
2803 C CB  . CYS B 148 ? 0.4393 0.2730 0.2597 -0.0276 -0.0255 0.0070  150 CYS B CB  
2804 S SG  . CYS B 148 ? 0.5444 0.3530 0.3485 -0.0298 -0.0344 -0.0008 150 CYS B SG  
2805 N N   . GLY B 149 ? 0.4077 0.2580 0.2503 -0.0177 -0.0151 0.0177  151 GLY B N   
2806 C CA  . GLY B 149 ? 0.4127 0.2789 0.2667 -0.0151 -0.0052 0.0246  151 GLY B CA  
2807 C C   . GLY B 149 ? 0.3927 0.2753 0.2621 -0.0093 -0.0037 0.0249  151 GLY B C   
2808 O O   . GLY B 149 ? 0.3695 0.2506 0.2431 -0.0076 -0.0096 0.0184  151 GLY B O   
2809 N N   . ALA B 150 ? 0.3904 0.2869 0.2680 -0.0063 0.0053  0.0324  152 ALA B N   
2810 C CA  . ALA B 150 ? 0.3882 0.2966 0.2761 -0.0016 0.0101  0.0347  152 ALA B CA  
2811 C C   . ALA B 150 ? 0.3905 0.3181 0.2816 0.0011  0.0156  0.0438  152 ALA B C   
2812 O O   . ALA B 150 ? 0.3851 0.3164 0.2769 0.0014  0.0186  0.0492  152 ALA B O   
2813 C CB  . ALA B 150 ? 0.3856 0.2824 0.2770 0.0005  0.0152  0.0350  152 ALA B CB  
2814 N N   . VAL B 151 ? 0.3977 0.3374 0.2907 0.0031  0.0168  0.0449  153 VAL B N   
2815 C CA  . VAL B 151 ? 0.3988 0.3555 0.2913 0.0065  0.0192  0.0540  153 VAL B CA  
2816 C C   . VAL B 151 ? 0.4182 0.3729 0.3101 0.0112  0.0272  0.0592  153 VAL B C   
2817 O O   . VAL B 151 ? 0.4316 0.3798 0.3235 0.0092  0.0298  0.0527  153 VAL B O   
2818 C CB  . VAL B 151 ? 0.4089 0.3797 0.2961 0.0023  0.0119  0.0506  153 VAL B CB  
2819 C CG1 . VAL B 151 ? 0.4152 0.4048 0.3005 0.0059  0.0110  0.0602  153 VAL B CG1 
2820 C CG2 . VAL B 151 ? 0.4155 0.3844 0.3015 -0.0040 0.0057  0.0444  153 VAL B CG2 
2821 N N   . VAL B 152 ? 0.4187 0.3781 0.3108 0.0177  0.0318  0.0706  154 VAL B N   
2822 C CA  . VAL B 152 ? 0.4319 0.3877 0.3180 0.0224  0.0395  0.0778  154 VAL B CA  
2823 C C   . VAL B 152 ? 0.4402 0.4116 0.3184 0.0267  0.0343  0.0871  154 VAL B C   
2824 O O   . VAL B 152 ? 0.4068 0.3900 0.2914 0.0314  0.0300  0.0938  154 VAL B O   
2825 C CB  . VAL B 152 ? 0.4582 0.3987 0.3479 0.0273  0.0506  0.0835  154 VAL B CB  
2826 C CG1 . VAL B 152 ? 0.4814 0.4256 0.3787 0.0330  0.0508  0.0910  154 VAL B CG1 
2827 C CG2 . VAL B 152 ? 0.4881 0.4210 0.3675 0.0313  0.0596  0.0913  154 VAL B CG2 
2828 N N   . ASN B 153 ? 0.4795 0.4513 0.3439 0.0246  0.0347  0.0868  155 ASN B N   
2829 C CA  . ASN B 153 ? 0.5235 0.5065 0.3743 0.0285  0.0289  0.0964  155 ASN B CA  
2830 C C   . ASN B 153 ? 0.5737 0.5404 0.4110 0.0350  0.0392  0.1071  155 ASN B C   
2831 O O   . ASN B 153 ? 0.5802 0.5322 0.4078 0.0301  0.0490  0.1025  155 ASN B O   
2832 C CB  . ASN B 153 ? 0.5307 0.5211 0.3685 0.0200  0.0230  0.0882  155 ASN B CB  
2833 C CG  . ASN B 153 ? 0.5830 0.5797 0.4312 0.0119  0.0171  0.0746  155 ASN B CG  
2834 O OD1 . ASN B 153 ? 0.5878 0.5744 0.4393 0.0064  0.0214  0.0635  155 ASN B OD1 
2835 N ND2 . ASN B 153 ? 0.5870 0.5999 0.4415 0.0109  0.0072  0.0749  155 ASN B ND2 
2836 N N   . VAL B 154 ? 0.6135 0.5818 0.4514 0.0458  0.0378  0.1208  156 VAL B N   
2837 C CA  . VAL B 154 ? 0.6747 0.6245 0.4965 0.0535  0.0468  0.1333  156 VAL B CA  
2838 C C   . VAL B 154 ? 0.7217 0.6754 0.5175 0.0547  0.0387  0.1405  156 VAL B C   
2839 O O   . VAL B 154 ? 0.7140 0.6875 0.5116 0.0602  0.0241  0.1467  156 VAL B O   
2840 C CB  . VAL B 154 ? 0.6910 0.6404 0.5259 0.0664  0.0477  0.1451  156 VAL B CB  
2841 C CG1 . VAL B 154 ? 0.7122 0.6383 0.5291 0.0758  0.0572  0.1592  156 VAL B CG1 
2842 C CG2 . VAL B 154 ? 0.6965 0.6410 0.5528 0.0632  0.0553  0.1366  156 VAL B CG2 
2843 N N   . ARG B 155 ? 0.7696 0.7049 0.5415 0.0486  0.0482  0.1389  157 ARG B N   
2844 C CA  . ARG B 155 ? 0.8221 0.7564 0.5626 0.0468  0.0421  0.1438  157 ARG B CA  
2845 C C   . ARG B 155 ? 0.8754 0.7785 0.5845 0.0485  0.0561  0.1534  157 ARG B C   
2846 O O   . ARG B 155 ? 0.8864 0.7694 0.5996 0.0458  0.0736  0.1503  157 ARG B O   
2847 C CB  . ARG B 155 ? 0.8283 0.7707 0.5656 0.0329  0.0409  0.1278  157 ARG B CB  
2848 C CG  . ARG B 155 ? 0.8477 0.8164 0.6081 0.0300  0.0274  0.1191  157 ARG B CG  
2849 C CD  . ARG B 155 ? 0.8899 0.8797 0.6427 0.0339  0.0089  0.1264  157 ARG B CD  
2850 N NE  . ARG B 155 ? 0.9311 0.9431 0.7022 0.0266  -0.0009 0.1144  157 ARG B NE  
2851 C CZ  . ARG B 155 ? 0.9284 0.9543 0.7283 0.0289  -0.0048 0.1117  157 ARG B CZ  
2852 N NH1 . ARG B 155 ? 0.9057 0.9272 0.7215 0.0387  0.0001  0.1198  157 ARG B NH1 
2853 N NH2 . ARG B 155 ? 0.9284 0.9699 0.7393 0.0206  -0.0121 0.1006  157 ARG B NH2 
2854 N N   . ALA B 156 ? 0.9070 0.8046 0.5829 0.0520  0.0483  0.1646  158 ALA B N   
2855 C CA  . ALA B 156 ? 0.9471 0.8104 0.5852 0.0534  0.0612  0.1755  158 ALA B CA  
2856 C C   . ALA B 156 ? 0.9610 0.8063 0.5842 0.0368  0.0806  0.1614  158 ALA B C   
2857 O O   . ALA B 156 ? 0.9746 0.7929 0.5894 0.0341  0.1005  0.1619  158 ALA B O   
2858 C CB  . ALA B 156 ? 0.9624 0.8245 0.5654 0.0612  0.0448  0.1909  158 ALA B CB  
2859 N N   . LYS B 157 ? 0.9604 0.8204 0.5822 0.0256  0.0761  0.1479  159 LYS B N   
2860 C CA  . LYS B 157 ? 0.9745 0.8231 0.5924 0.0102  0.0945  0.1312  159 LYS B CA  
2861 C C   . LYS B 157 ? 0.9446 0.7917 0.5993 0.0066  0.1098  0.1189  159 LYS B C   
2862 O O   . LYS B 157 ? 0.9577 0.7871 0.6083 -0.0030 0.1302  0.1098  159 LYS B O   
2863 C CB  . LYS B 157 ? 1.0081 0.8774 0.6276 0.0008  0.0847  0.1174  159 LYS B CB  
2864 C CG  . LYS B 157 ? 1.0858 0.9488 0.7117 -0.0138 0.1028  0.0972  159 LYS B CG  
2865 C CD  . LYS B 157 ? 1.1585 1.0293 0.7668 -0.0239 0.0977  0.0868  159 LYS B CD  
2866 C CE  . LYS B 157 ? 1.2473 1.0952 0.8020 -0.0296 0.1033  0.0938  159 LYS B CE  
2867 N NZ  . LYS B 157 ? 1.3052 1.1238 0.8440 -0.0389 0.1313  0.0879  159 LYS B NZ  
2868 N N   . GLY B 158 ? 0.9016 0.7670 0.5910 0.0134  0.1000  0.1180  160 GLY B N   
2869 C CA  . GLY B 158 ? 0.8719 0.7376 0.5943 0.0098  0.1103  0.1060  160 GLY B CA  
2870 C C   . GLY B 158 ? 0.8204 0.7110 0.5754 0.0116  0.0957  0.0982  160 GLY B C   
2871 O O   . GLY B 158 ? 0.8226 0.7308 0.5785 0.0092  0.0829  0.0932  160 GLY B O   
2872 N N   . ASP B 159 ? 0.7666 0.6562 0.5458 0.0150  0.0984  0.0970  161 ASP B N   
2873 C CA  . ASP B 159 ? 0.7006 0.6082 0.5040 0.0187  0.0847  0.0943  161 ASP B CA  
2874 C C   . ASP B 159 ? 0.6518 0.5702 0.4737 0.0104  0.0810  0.0765  161 ASP B C   
2875 O O   . ASP B 159 ? 0.6576 0.5705 0.4809 0.0027  0.0906  0.0651  161 ASP B O   
2876 C CB  . ASP B 159 ? 0.6937 0.5922 0.5109 0.0246  0.0901  0.0995  161 ASP B CB  
2877 C CG  . ASP B 159 ? 0.7188 0.6044 0.5181 0.0347  0.0940  0.1175  161 ASP B CG  
2878 O OD1 . ASP B 159 ? 0.7236 0.6194 0.5119 0.0417  0.0823  0.1280  161 ASP B OD1 
2879 O OD2 . ASP B 159 ? 0.7326 0.5977 0.5296 0.0356  0.1082  0.1207  161 ASP B OD2 
2880 N N   . LYS B 160 ? 0.6085 0.5414 0.4448 0.0121  0.0676  0.0740  162 LYS B N   
2881 C CA  . LYS B 160 ? 0.5648 0.5047 0.4169 0.0061  0.0622  0.0587  162 LYS B CA  
2882 C C   . LYS B 160 ? 0.5173 0.4576 0.3869 0.0089  0.0565  0.0577  162 LYS B C   
2883 O O   . LYS B 160 ? 0.5097 0.4547 0.3787 0.0143  0.0511  0.0672  162 LYS B O   
2884 C CB  . LYS B 160 ? 0.6079 0.5613 0.4514 0.0032  0.0512  0.0560  162 LYS B CB  
2885 C CG  . LYS B 160 ? 0.7152 0.6661 0.5375 -0.0015 0.0570  0.0550  162 LYS B CG  
2886 C CD  . LYS B 160 ? 0.8341 0.7945 0.6523 -0.0080 0.0495  0.0449  162 LYS B CD  
2887 C CE  . LYS B 160 ? 0.9306 0.9061 0.7409 -0.0069 0.0348  0.0512  162 LYS B CE  
2888 N NZ  . LYS B 160 ? 0.9797 0.9576 0.7616 -0.0087 0.0328  0.0580  162 LYS B NZ  
2889 N N   . ILE B 161 ? 0.4878 0.4228 0.3729 0.0053  0.0579  0.0457  163 ILE B N   
2890 C CA  . ILE B 161 ? 0.4657 0.3983 0.3628 0.0062  0.0505  0.0424  163 ILE B CA  
2891 C C   . ILE B 161 ? 0.4435 0.3788 0.3492 0.0024  0.0416  0.0292  163 ILE B C   
2892 O O   . ILE B 161 ? 0.4349 0.3701 0.3485 -0.0006 0.0455  0.0192  163 ILE B O   
2893 C CB  . ILE B 161 ? 0.4706 0.3906 0.3760 0.0065  0.0586  0.0418  163 ILE B CB  
2894 C CG1 . ILE B 161 ? 0.4952 0.4086 0.3907 0.0113  0.0689  0.0555  163 ILE B CG1 
2895 C CG2 . ILE B 161 ? 0.4708 0.3854 0.3836 0.0063  0.0499  0.0376  163 ILE B CG2 
2896 C CD1 . ILE B 161 ? 0.5341 0.4329 0.4354 0.0104  0.0794  0.0545  163 ILE B CD1 
2897 N N   . ALA B 162 ? 0.4137 0.3500 0.3184 0.0025  0.0304  0.0287  164 ALA B N   
2898 C CA  . ALA B 162 ? 0.4156 0.3506 0.3247 -0.0001 0.0212  0.0177  164 ALA B CA  
2899 C C   . ALA B 162 ? 0.4081 0.3330 0.3164 0.0002  0.0122  0.0169  164 ALA B C   
2900 O O   . ALA B 162 ? 0.4023 0.3271 0.3033 0.0005  0.0122  0.0252  164 ALA B O   
2901 C CB  . ALA B 162 ? 0.4336 0.3781 0.3331 -0.0026 0.0181  0.0173  164 ALA B CB  
2902 N N   . ILE B 163 ? 0.4033 0.3187 0.3190 0.0001  0.0047  0.0069  165 ILE B N   
2903 C CA  . ILE B 163 ? 0.3963 0.2978 0.3044 -0.0004 -0.0061 0.0051  165 ILE B CA  
2904 C C   . ILE B 163 ? 0.3971 0.2981 0.2988 -0.0022 -0.0126 0.0007  165 ILE B C   
2905 O O   . ILE B 163 ? 0.3914 0.2949 0.3019 -0.0011 -0.0145 -0.0079 165 ILE B O   
2906 C CB  . ILE B 163 ? 0.4024 0.2913 0.3189 0.0015  -0.0134 -0.0024 165 ILE B CB  
2907 C CG1 . ILE B 163 ? 0.3978 0.2839 0.3168 0.0013  -0.0065 0.0018  165 ILE B CG1 
2908 C CG2 . ILE B 163 ? 0.4322 0.3014 0.3345 0.0013  -0.0266 -0.0043 165 ILE B CG2 
2909 C CD1 . ILE B 163 ? 0.4206 0.2951 0.3458 0.0017  -0.0142 -0.0053 165 ILE B CD1 
2910 N N   . TRP B 164 ? 0.4059 0.3030 0.2935 -0.0055 -0.0148 0.0055  166 TRP B N   
2911 C CA  . TRP B 164 ? 0.4179 0.3109 0.2959 -0.0093 -0.0200 0.0015  166 TRP B CA  
2912 C C   . TRP B 164 ? 0.4367 0.3046 0.3054 -0.0088 -0.0299 -0.0031 166 TRP B C   
2913 O O   . TRP B 164 ? 0.4255 0.2790 0.2853 -0.0094 -0.0319 0.0006  166 TRP B O   
2914 C CB  . TRP B 164 ? 0.4210 0.3238 0.2898 -0.0146 -0.0162 0.0082  166 TRP B CB  
2915 C CG  . TRP B 164 ? 0.4365 0.3629 0.3097 -0.0150 -0.0105 0.0125  166 TRP B CG  
2916 C CD1 . TRP B 164 ? 0.4412 0.3782 0.3219 -0.0109 -0.0047 0.0156  166 TRP B CD1 
2917 C CD2 . TRP B 164 ? 0.4490 0.3901 0.3168 -0.0204 -0.0106 0.0144  166 TRP B CD2 
2918 N NE1 . TRP B 164 ? 0.4350 0.3899 0.3119 -0.0124 -0.0023 0.0205  166 TRP B NE1 
2919 C CE2 . TRP B 164 ? 0.4448 0.4046 0.3155 -0.0180 -0.0068 0.0196  166 TRP B CE2 
2920 C CE3 . TRP B 164 ? 0.4689 0.4084 0.3290 -0.0277 -0.0134 0.0119  166 TRP B CE3 
2921 C CZ2 . TRP B 164 ? 0.4547 0.4333 0.3214 -0.0218 -0.0085 0.0224  166 TRP B CZ2 
2922 C CZ3 . TRP B 164 ? 0.4690 0.4295 0.3287 -0.0327 -0.0135 0.0134  166 TRP B CZ3 
2923 C CH2 . TRP B 164 ? 0.4701 0.4508 0.3333 -0.0292 -0.0124 0.0187  166 TRP B CH2 
2924 N N   . THR B 165 ? 0.4635 0.3239 0.3323 -0.0077 -0.0360 -0.0111 167 THR B N   
2925 C CA  . THR B 165 ? 0.4974 0.3305 0.3545 -0.0059 -0.0471 -0.0151 167 THR B CA  
2926 C C   . THR B 165 ? 0.5063 0.3300 0.3487 -0.0113 -0.0474 -0.0177 167 THR B C   
2927 O O   . THR B 165 ? 0.4790 0.3198 0.3243 -0.0158 -0.0406 -0.0191 167 THR B O   
2928 C CB  . THR B 165 ? 0.5159 0.3444 0.3901 0.0030  -0.0561 -0.0231 167 THR B CB  
2929 O OG1 . THR B 165 ? 0.5019 0.3377 0.3877 0.0052  -0.0550 -0.0313 167 THR B OG1 
2930 C CG2 . THR B 165 ? 0.5359 0.3797 0.4287 0.0058  -0.0523 -0.0225 167 THR B CG2 
2931 N N   . THR B 166 ? 0.5317 0.3256 0.3552 -0.0116 -0.0553 -0.0184 168 THR B N   
2932 C CA  . THR B 166 ? 0.5589 0.3373 0.3622 -0.0194 -0.0536 -0.0195 168 THR B CA  
2933 C C   . THR B 166 ? 0.5715 0.3429 0.3767 -0.0172 -0.0564 -0.0281 168 THR B C   
2934 O O   . THR B 166 ? 0.5670 0.3351 0.3605 -0.0257 -0.0512 -0.0304 168 THR B O   
2935 C CB  . THR B 166 ? 0.6115 0.3549 0.3874 -0.0222 -0.0585 -0.0157 168 THR B CB  
2936 O OG1 . THR B 166 ? 0.6457 0.3786 0.4025 -0.0335 -0.0516 -0.0156 168 THR B OG1 
2937 C CG2 . THR B 166 ? 0.6204 0.3332 0.3877 -0.0129 -0.0732 -0.0188 168 THR B CG2 
2938 N N   . GLU B 167 ? 0.5746 0.3445 0.3963 -0.0064 -0.0637 -0.0339 169 GLU B N   
2939 C CA  . GLU B 167 ? 0.5934 0.3507 0.4172 -0.0024 -0.0668 -0.0428 169 GLU B CA  
2940 C C   . GLU B 167 ? 0.5862 0.3630 0.4414 0.0068  -0.0668 -0.0510 169 GLU B C   
2941 O O   . GLU B 167 ? 0.5749 0.3484 0.4450 0.0169  -0.0764 -0.0530 169 GLU B O   
2942 C CB  . GLU B 167 ? 0.6194 0.3358 0.4229 0.0033  -0.0799 -0.0424 169 GLU B CB  
2943 C CG  . GLU B 167 ? 0.6312 0.3280 0.4352 0.0098  -0.0845 -0.0507 169 GLU B CG  
2944 C CD  . GLU B 167 ? 0.6999 0.4038 0.5001 0.0001  -0.0716 -0.0562 169 GLU B CD  
2945 O OE1 . GLU B 167 ? 0.7095 0.3980 0.4837 -0.0113 -0.0665 -0.0534 169 GLU B OE1 
2946 O OE2 . GLU B 167 ? 0.7211 0.4463 0.5439 0.0026  -0.0658 -0.0640 169 GLU B OE2 
2947 N N   . CYS B 168 ? 0.5910 0.3875 0.4558 0.0023  -0.0557 -0.0565 170 CYS B N   
2948 C CA  . CYS B 168 ? 0.5983 0.4129 0.4915 0.0086  -0.0515 -0.0652 170 CYS B CA  
2949 C C   . CYS B 168 ? 0.5893 0.3878 0.4979 0.0203  -0.0597 -0.0756 170 CYS B C   
2950 O O   . CYS B 168 ? 0.5655 0.3793 0.5035 0.0272  -0.0583 -0.0832 170 CYS B O   
2951 C CB  . CYS B 168 ? 0.6362 0.4712 0.5294 -0.0002 -0.0370 -0.0686 170 CYS B CB  
2952 S SG  . CYS B 168 ? 0.7602 0.5793 0.6321 -0.0085 -0.0329 -0.0747 170 CYS B SG  
2953 N N   . GLU B 169 ? 0.6065 0.3740 0.4968 0.0227  -0.0677 -0.0763 171 GLU B N   
2954 C CA  . GLU B 169 ? 0.5980 0.3467 0.5022 0.0363  -0.0777 -0.0849 171 GLU B CA  
2955 C C   . GLU B 169 ? 0.5998 0.3362 0.5108 0.0487  -0.0967 -0.0817 171 GLU B C   
2956 O O   . GLU B 169 ? 0.6004 0.3251 0.5279 0.0622  -0.1076 -0.0886 171 GLU B O   
2957 C CB  . GLU B 169 ? 0.6293 0.3458 0.5083 0.0341  -0.0775 -0.0870 171 GLU B CB  
2958 C CG  . GLU B 169 ? 0.6742 0.4008 0.5455 0.0212  -0.0605 -0.0921 171 GLU B CG  
2959 C CD  . GLU B 169 ? 0.7144 0.4660 0.6141 0.0226  -0.0487 -0.1037 171 GLU B CD  
2960 O OE1 . GLU B 169 ? 0.7114 0.4651 0.6407 0.0360  -0.0531 -0.1118 171 GLU B OE1 
2961 O OE2 . GLU B 169 ? 0.7214 0.4903 0.6136 0.0100  -0.0350 -0.1052 171 GLU B OE2 
2962 N N   . ASN B 170 ? 0.6112 0.3494 0.5098 0.0447  -0.1011 -0.0718 172 ASN B N   
2963 C CA  . ASN B 170 ? 0.6237 0.3545 0.5291 0.0546  -0.1188 -0.0696 172 ASN B CA  
2964 C C   . ASN B 170 ? 0.6194 0.3845 0.5661 0.0593  -0.1171 -0.0767 172 ASN B C   
2965 O O   . ASN B 170 ? 0.5892 0.3697 0.5370 0.0537  -0.1138 -0.0715 172 ASN B O   
2966 C CB  . ASN B 170 ? 0.6398 0.3557 0.5118 0.0465  -0.1219 -0.0571 172 ASN B CB  
2967 C CG  . ASN B 170 ? 0.6689 0.3449 0.4995 0.0426  -0.1260 -0.0508 172 ASN B CG  
2968 O OD1 . ASN B 170 ? 0.6711 0.3232 0.4940 0.0483  -0.1310 -0.0546 172 ASN B OD1 
2969 N ND2 . ASN B 170 ? 0.6822 0.3479 0.4848 0.0326  -0.1227 -0.0415 172 ASN B ND2 
2970 N N   . ARG B 171 ? 0.6260 0.4022 0.6079 0.0695  -0.1183 -0.0895 173 ARG B N   
2971 C CA  . ARG B 171 ? 0.6310 0.4415 0.6544 0.0714  -0.1122 -0.0985 173 ARG B CA  
2972 C C   . ARG B 171 ? 0.6266 0.4416 0.6598 0.0756  -0.1271 -0.0963 173 ARG B C   
2973 O O   . ARG B 171 ? 0.6114 0.4496 0.6582 0.0692  -0.1179 -0.0965 173 ARG B O   
2974 C CB  . ARG B 171 ? 0.6565 0.4785 0.7196 0.0814  -0.1097 -0.1144 173 ARG B CB  
2975 C CG  . ARG B 171 ? 0.7293 0.5877 0.8339 0.0793  -0.0972 -0.1248 173 ARG B CG  
2976 C CD  . ARG B 171 ? 0.8003 0.6739 0.9529 0.0900  -0.0958 -0.1427 173 ARG B CD  
2977 N NE  . ARG B 171 ? 0.8878 0.7617 1.0439 0.0873  -0.0772 -0.1513 173 ARG B NE  
2978 C CZ  . ARG B 171 ? 0.9202 0.8165 1.0951 0.0791  -0.0538 -0.1610 173 ARG B CZ  
2979 N NH1 . ARG B 171 ? 0.8992 0.8202 1.0923 0.0724  -0.0443 -0.1631 173 ARG B NH1 
2980 N NH2 . ARG B 171 ? 0.9190 0.8099 1.0914 0.0766  -0.0387 -0.1689 173 ARG B NH2 
2981 N N   . GLU B 172 ? 0.6344 0.4251 0.6587 0.0862  -0.1503 -0.0944 174 GLU B N   
2982 C CA  . GLU B 172 ? 0.6208 0.4131 0.6512 0.0900  -0.1674 -0.0931 174 GLU B CA  
2983 C C   . GLU B 172 ? 0.6180 0.4096 0.6203 0.0766  -0.1598 -0.0818 174 GLU B C   
2984 O O   . GLU B 172 ? 0.6108 0.4229 0.6316 0.0734  -0.1579 -0.0843 174 GLU B O   
2985 C CB  . GLU B 172 ? 0.6754 0.4338 0.6875 0.1024  -0.1944 -0.0901 174 GLU B CB  
2986 C CG  . GLU B 172 ? 0.8070 0.5655 0.8518 0.1193  -0.2068 -0.1015 174 GLU B CG  
2987 C CD  . GLU B 172 ? 0.9770 0.6946 0.9949 0.1324  -0.2338 -0.0959 174 GLU B CD  
2988 O OE1 . GLU B 172 ? 1.0123 0.7283 1.0373 0.1406  -0.2571 -0.0966 174 GLU B OE1 
2989 O OE2 . GLU B 172 ? 1.0300 0.7154 1.0176 0.1338  -0.2320 -0.0907 174 GLU B OE2 
2990 N N   . ALA B 173 ? 0.6140 0.3815 0.5726 0.0685  -0.1542 -0.0701 175 ALA B N   
2991 C CA  . ALA B 173 ? 0.5963 0.3631 0.5301 0.0564  -0.1447 -0.0599 175 ALA B CA  
2992 C C   . ALA B 173 ? 0.5492 0.3504 0.5047 0.0484  -0.1234 -0.0615 175 ALA B C   
2993 O O   . ALA B 173 ? 0.5215 0.3335 0.4808 0.0437  -0.1196 -0.0590 175 ALA B O   
2994 C CB  . ALA B 173 ? 0.6235 0.3623 0.5139 0.0491  -0.1403 -0.0498 175 ALA B CB  
2995 N N   . VAL B 174 ? 0.5295 0.3443 0.4967 0.0469  -0.1100 -0.0659 176 VAL B N   
2996 C CA  . VAL B 174 ? 0.5197 0.3606 0.4982 0.0390  -0.0899 -0.0658 176 VAL B CA  
2997 C C   . VAL B 174 ? 0.5202 0.3854 0.5348 0.0409  -0.0862 -0.0744 176 VAL B C   
2998 O O   . VAL B 174 ? 0.5151 0.3933 0.5298 0.0339  -0.0741 -0.0699 176 VAL B O   
2999 C CB  . VAL B 174 ? 0.5041 0.3493 0.4806 0.0362  -0.0780 -0.0691 176 VAL B CB  
3000 C CG1 . VAL B 174 ? 0.4961 0.3678 0.4860 0.0294  -0.0586 -0.0709 176 VAL B CG1 
3001 C CG2 . VAL B 174 ? 0.5111 0.3362 0.4506 0.0299  -0.0778 -0.0599 176 VAL B CG2 
3002 N N   . THR B 175 ? 0.5251 0.3964 0.5710 0.0502  -0.0955 -0.0868 177 THR B N   
3003 C CA  . THR B 175 ? 0.5309 0.4284 0.6161 0.0503  -0.0890 -0.0976 177 THR B CA  
3004 C C   . THR B 175 ? 0.5384 0.4353 0.6270 0.0504  -0.1013 -0.0963 177 THR B C   
3005 O O   . THR B 175 ? 0.5318 0.4478 0.6412 0.0451  -0.0910 -0.1010 177 THR B O   
3006 C CB  . THR B 175 ? 0.5420 0.4522 0.6662 0.0589  -0.0899 -0.1138 177 THR B CB  
3007 O OG1 . THR B 175 ? 0.5790 0.4773 0.7131 0.0714  -0.1146 -0.1180 177 THR B OG1 
3008 C CG2 . THR B 175 ? 0.5384 0.4449 0.6539 0.0574  -0.0770 -0.1154 177 THR B CG2 
3009 N N   . HIS B 176 ? 0.5532 0.4261 0.6189 0.0551  -0.1221 -0.0904 178 HIS B N   
3010 C CA  . HIS B 176 ? 0.5525 0.4206 0.6113 0.0525  -0.1322 -0.0876 178 HIS B CA  
3011 C C   . HIS B 176 ? 0.5416 0.4105 0.5783 0.0403  -0.1138 -0.0770 178 HIS B C   
3012 O O   . HIS B 176 ? 0.5260 0.4063 0.5746 0.0351  -0.1083 -0.0794 178 HIS B O   
3013 C CB  . HIS B 176 ? 0.5993 0.4354 0.6279 0.0585  -0.1565 -0.0817 178 HIS B CB  
3014 C CG  . HIS B 176 ? 0.6947 0.5220 0.7093 0.0541  -0.1663 -0.0788 178 HIS B CG  
3015 N ND1 . HIS B 176 ? 0.7238 0.5584 0.7624 0.0599  -0.1858 -0.0887 178 HIS B ND1 
3016 C CD2 . HIS B 176 ? 0.7434 0.5561 0.7241 0.0442  -0.1584 -0.0681 178 HIS B CD2 
3017 C CE1 . HIS B 176 ? 0.7522 0.5747 0.7674 0.0523  -0.1890 -0.0837 178 HIS B CE1 
3018 N NE2 . HIS B 176 ? 0.7698 0.5778 0.7497 0.0431  -0.1721 -0.0713 178 HIS B NE2 
3019 N N   . ILE B 177 ? 0.5368 0.3940 0.5427 0.0359  -0.1039 -0.0659 179 ILE B N   
3020 C CA  . ILE B 177 ? 0.5185 0.3770 0.5054 0.0266  -0.0873 -0.0553 179 ILE B CA  
3021 C C   . ILE B 177 ? 0.5044 0.3885 0.5163 0.0225  -0.0686 -0.0595 179 ILE B C   
3022 O O   . ILE B 177 ? 0.5077 0.3952 0.5185 0.0171  -0.0599 -0.0561 179 ILE B O   
3023 C CB  . ILE B 177 ? 0.5182 0.3653 0.4749 0.0230  -0.0805 -0.0449 179 ILE B CB  
3024 C CG1 . ILE B 177 ? 0.5346 0.3515 0.4589 0.0234  -0.0941 -0.0387 179 ILE B CG1 
3025 C CG2 . ILE B 177 ? 0.5004 0.3591 0.4491 0.0154  -0.0609 -0.0357 179 ILE B CG2 
3026 C CD1 . ILE B 177 ? 0.5260 0.3297 0.4251 0.0205  -0.0905 -0.0328 179 ILE B CD1 
3027 N N   . GLY B 178 ? 0.4802 0.3786 0.5116 0.0245  -0.0616 -0.0669 180 GLY B N   
3028 C CA  . GLY B 178 ? 0.4769 0.3956 0.5276 0.0196  -0.0423 -0.0712 180 GLY B CA  
3029 C C   . GLY B 178 ? 0.4721 0.4030 0.5523 0.0184  -0.0413 -0.0813 180 GLY B C   
3030 O O   . GLY B 178 ? 0.4602 0.3981 0.5422 0.0115  -0.0251 -0.0792 180 GLY B O   
3031 N N   . ARG B 179 ? 0.4836 0.4169 0.5878 0.0251  -0.0591 -0.0927 181 ARG B N   
3032 C CA  . ARG B 179 ? 0.4669 0.4149 0.6038 0.0233  -0.0610 -0.1047 181 ARG B CA  
3033 C C   . ARG B 179 ? 0.4789 0.4162 0.5969 0.0174  -0.0631 -0.0974 181 ARG B C   
3034 O O   . ARG B 179 ? 0.4740 0.4219 0.6072 0.0101  -0.0506 -0.1023 181 ARG B O   
3035 C CB  . ARG B 179 ? 0.4681 0.4218 0.6349 0.0333  -0.0837 -0.1180 181 ARG B CB  
3036 C CG  . ARG B 179 ? 0.5287 0.5001 0.7316 0.0391  -0.0790 -0.1317 181 ARG B CG  
3037 C CD  . ARG B 179 ? 0.5821 0.5500 0.8022 0.0529  -0.1054 -0.1393 181 ARG B CD  
3038 N NE  . ARG B 179 ? 0.6556 0.6279 0.8921 0.0601  -0.1010 -0.1463 181 ARG B NE  
3039 C CZ  . ARG B 179 ? 0.7558 0.7119 0.9853 0.0721  -0.1188 -0.1453 181 ARG B CZ  
3040 N NH1 . ARG B 179 ? 0.7730 0.7057 0.9765 0.0783  -0.1434 -0.1368 181 ARG B NH1 
3041 N NH2 . ARG B 179 ? 0.7976 0.7574 1.0431 0.0776  -0.1112 -0.1529 181 ARG B NH2 
3042 N N   . VAL B 180 ? 0.4955 0.4095 0.5794 0.0196  -0.0775 -0.0867 182 VAL B N   
3043 C CA  . VAL B 180 ? 0.5030 0.4034 0.5652 0.0132  -0.0778 -0.0799 182 VAL B CA  
3044 C C   . VAL B 180 ? 0.5227 0.4234 0.5699 0.0059  -0.0536 -0.0696 182 VAL B C   
3045 O O   . VAL B 180 ? 0.5500 0.4521 0.6001 -0.0008 -0.0431 -0.0700 182 VAL B O   
3046 C CB  . VAL B 180 ? 0.5270 0.3998 0.5539 0.0161  -0.0964 -0.0717 182 VAL B CB  
3047 C CG1 . VAL B 180 ? 0.5408 0.3977 0.5414 0.0082  -0.0910 -0.0639 182 VAL B CG1 
3048 C CG2 . VAL B 180 ? 0.5354 0.4040 0.5743 0.0241  -0.1238 -0.0813 182 VAL B CG2 
3049 N N   . TYR B 181 ? 0.5179 0.4170 0.5492 0.0071  -0.0446 -0.0604 183 TYR B N   
3050 C CA  . TYR B 181 ? 0.5073 0.4077 0.5247 0.0020  -0.0237 -0.0497 183 TYR B CA  
3051 C C   . TYR B 181 ? 0.4987 0.4144 0.5391 -0.0028 -0.0060 -0.0563 183 TYR B C   
3052 O O   . TYR B 181 ? 0.4794 0.3905 0.5121 -0.0077 0.0069  -0.0507 183 TYR B O   
3053 C CB  . TYR B 181 ? 0.4754 0.3766 0.4778 0.0044  -0.0199 -0.0420 183 TYR B CB  
3054 C CG  . TYR B 181 ? 0.4601 0.3629 0.4464 0.0013  -0.0029 -0.0298 183 TYR B CG  
3055 C CD1 . TYR B 181 ? 0.4762 0.3700 0.4490 -0.0013 0.0040  -0.0208 183 TYR B CD1 
3056 C CD2 . TYR B 181 ? 0.4487 0.3606 0.4313 0.0015  0.0049  -0.0269 183 TYR B CD2 
3057 C CE1 . TYR B 181 ? 0.4786 0.3738 0.4379 -0.0018 0.0173  -0.0089 183 TYR B CE1 
3058 C CE2 . TYR B 181 ? 0.4525 0.3660 0.4190 0.0000  0.0167  -0.0149 183 TYR B CE2 
3059 C CZ  . TYR B 181 ? 0.4591 0.3647 0.4152 -0.0007 0.0222  -0.0056 183 TYR B CZ  
3060 O OH  . TYR B 181 ? 0.4577 0.3653 0.4004 0.0000  0.0325  0.0067  183 TYR B OH  
3061 N N   . LYS B 182 ? 0.5105 0.4421 0.5782 -0.0016 -0.0042 -0.0685 184 LYS B N   
3062 C CA  . LYS B 182 ? 0.5322 0.4770 0.6219 -0.0076 0.0147  -0.0766 184 LYS B CA  
3063 C C   . LYS B 182 ? 0.5585 0.5044 0.6644 -0.0133 0.0150  -0.0845 184 LYS B C   
3064 O O   . LYS B 182 ? 0.5753 0.5212 0.6828 -0.0208 0.0342  -0.0843 184 LYS B O   
3065 C CB  . LYS B 182 ? 0.5520 0.5135 0.6717 -0.0051 0.0146  -0.0912 184 LYS B CB  
3066 C CG  . LYS B 182 ? 0.5845 0.5585 0.7256 -0.0126 0.0368  -0.1009 184 LYS B CG  
3067 C CD  . LYS B 182 ? 0.6579 0.6473 0.8282 -0.0101 0.0385  -0.1158 184 LYS B CD  
3068 C CE  . LYS B 182 ? 0.7247 0.7266 0.9212 -0.0193 0.0612  -0.1287 184 LYS B CE  
3069 N NZ  . LYS B 182 ? 0.7638 0.7802 0.9884 -0.0180 0.0679  -0.1440 184 LYS B NZ  
3070 N N   . GLU B 183 ? 0.5554 0.5004 0.6714 -0.0100 -0.0066 -0.0916 185 GLU B N   
3071 C CA  . GLU B 183 ? 0.5616 0.5070 0.6905 -0.0158 -0.0109 -0.1000 185 GLU B CA  
3072 C C   . GLU B 183 ? 0.5708 0.4965 0.6676 -0.0216 -0.0001 -0.0867 185 GLU B C   
3073 O O   . GLU B 183 ? 0.5738 0.4991 0.6771 -0.0301 0.0146  -0.0903 185 GLU B O   
3074 C CB  . GLU B 183 ? 0.6257 0.5701 0.7625 -0.0092 -0.0404 -0.1072 185 GLU B CB  
3075 C CG  . GLU B 183 ? 0.7704 0.7174 0.9226 -0.0135 -0.0537 -0.1184 185 GLU B CG  
3076 C CD  . GLU B 183 ? 0.9424 0.8782 1.0834 -0.0044 -0.0847 -0.1181 185 GLU B CD  
3077 O OE1 . GLU B 183 ? 0.9574 0.9038 1.1192 0.0053  -0.0981 -0.1246 185 GLU B OE1 
3078 O OE2 . GLU B 183 ? 1.0110 0.9249 1.1204 -0.0067 -0.0946 -0.1110 185 GLU B OE2 
3079 N N   . ARG B 184 ? 0.5728 0.4815 0.6362 -0.0173 -0.0056 -0.0722 186 ARG B N   
3080 C CA  . ARG B 184 ? 0.5729 0.4628 0.6076 -0.0209 0.0037  -0.0600 186 ARG B CA  
3081 C C   . ARG B 184 ? 0.5728 0.4623 0.6002 -0.0235 0.0285  -0.0506 186 ARG B C   
3082 O O   . ARG B 184 ? 0.5866 0.4633 0.6013 -0.0277 0.0405  -0.0448 186 ARG B O   
3083 C CB  . ARG B 184 ? 0.5914 0.4649 0.5961 -0.0160 -0.0089 -0.0491 186 ARG B CB  
3084 C CG  . ARG B 184 ? 0.6039 0.4675 0.6043 -0.0148 -0.0328 -0.0558 186 ARG B CG  
3085 C CD  . ARG B 184 ? 0.6172 0.4651 0.6051 -0.0220 -0.0330 -0.0574 186 ARG B CD  
3086 N NE  . ARG B 184 ? 0.6006 0.4281 0.5560 -0.0240 -0.0225 -0.0441 186 ARG B NE  
3087 C CZ  . ARG B 184 ? 0.6230 0.4288 0.5490 -0.0241 -0.0327 -0.0391 186 ARG B CZ  
3088 N NH1 . ARG B 184 ? 0.6437 0.4415 0.5634 -0.0219 -0.0560 -0.0449 186 ARG B NH1 
3089 N NH2 . ARG B 184 ? 0.6189 0.4094 0.5212 -0.0262 -0.0192 -0.0284 186 ARG B NH2 
3090 N N   . LEU B 185 ? 0.5700 0.4710 0.6031 -0.0208 0.0364  -0.0489 187 LEU B N   
3091 C CA  . LEU B 185 ? 0.5972 0.4971 0.6235 -0.0235 0.0591  -0.0415 187 LEU B CA  
3092 C C   . LEU B 185 ? 0.6360 0.5404 0.6839 -0.0323 0.0747  -0.0533 187 LEU B C   
3093 O O   . LEU B 185 ? 0.6338 0.5310 0.6723 -0.0357 0.0948  -0.0470 187 LEU B O   
3094 C CB  . LEU B 185 ? 0.5902 0.4990 0.6118 -0.0193 0.0622  -0.0369 187 LEU B CB  
3095 C CG  . LEU B 185 ? 0.6052 0.5099 0.6034 -0.0126 0.0523  -0.0239 187 LEU B CG  
3096 C CD1 . LEU B 185 ? 0.5969 0.5125 0.5954 -0.0101 0.0515  -0.0248 187 LEU B CD1 
3097 C CD2 . LEU B 185 ? 0.6146 0.5080 0.5895 -0.0110 0.0622  -0.0077 187 LEU B CD2 
3098 N N   . GLY B 186 ? 0.6645 0.5800 0.7408 -0.0359 0.0650  -0.0702 188 GLY B N   
3099 C CA  . GLY B 186 ? 0.6835 0.6081 0.7871 -0.0454 0.0784  -0.0850 188 GLY B CA  
3100 C C   . GLY B 186 ? 0.7182 0.6523 0.8316 -0.0476 0.0960  -0.0884 188 GLY B C   
3101 O O   . GLY B 186 ? 0.7275 0.6569 0.8428 -0.0563 0.1184  -0.0908 188 GLY B O   
3102 N N   . LEU B 187 ? 0.7395 0.6841 0.8564 -0.0406 0.0876  -0.0888 189 LEU B N   
3103 C CA  . LEU B 187 ? 0.7719 0.7234 0.8939 -0.0433 0.1048  -0.0924 189 LEU B CA  
3104 C C   . LEU B 187 ? 0.8018 0.7744 0.9691 -0.0485 0.1075  -0.1155 189 LEU B C   
3105 O O   . LEU B 187 ? 0.7992 0.7852 0.9924 -0.0436 0.0866  -0.1263 189 LEU B O   
3106 C CB  . LEU B 187 ? 0.7724 0.7250 0.8773 -0.0348 0.0963  -0.0840 189 LEU B CB  
3107 C CG  . LEU B 187 ? 0.7906 0.7274 0.8545 -0.0307 0.0980  -0.0626 189 LEU B CG  
3108 C CD1 . LEU B 187 ? 0.7897 0.7313 0.8427 -0.0248 0.0900  -0.0586 189 LEU B CD1 
3109 C CD2 . LEU B 187 ? 0.8033 0.7278 0.8478 -0.0363 0.1213  -0.0541 189 LEU B CD2 
3110 N N   . PRO B 188 ? 0.8236 0.7987 1.0013 -0.0583 0.1330  -0.1238 190 PRO B N   
3111 C CA  . PRO B 188 ? 0.8198 0.8183 1.0455 -0.0633 0.1375  -0.1476 190 PRO B CA  
3112 C C   . PRO B 188 ? 0.8400 0.8543 1.0843 -0.0538 0.1236  -0.1550 190 PRO B C   
3113 O O   . PRO B 188 ? 0.8619 0.8668 1.0773 -0.0485 0.1239  -0.1431 190 PRO B O   
3114 C CB  . PRO B 188 ? 0.8291 0.8207 1.0502 -0.0760 0.1714  -0.1513 190 PRO B CB  
3115 C CG  . PRO B 188 ? 0.8579 0.8210 1.0295 -0.0774 0.1827  -0.1294 190 PRO B CG  
3116 C CD  . PRO B 188 ? 0.8423 0.7975 0.9876 -0.0650 0.1589  -0.1118 190 PRO B CD  
3117 N N   . PRO B 189 ? 0.8351 0.8729 1.1273 -0.0510 0.1111  -0.1748 191 PRO B N   
3118 C CA  . PRO B 189 ? 0.8313 0.8824 1.1436 -0.0415 0.1014  -0.1832 191 PRO B CA  
3119 C C   . PRO B 189 ? 0.8336 0.8837 1.1403 -0.0460 0.1263  -0.1864 191 PRO B C   
3120 O O   . PRO B 189 ? 0.8369 0.8899 1.1449 -0.0380 0.1193  -0.1880 191 PRO B O   
3121 C CB  . PRO B 189 ? 0.8131 0.8917 1.1852 -0.0400 0.0900  -0.2067 191 PRO B CB  
3122 C CG  . PRO B 189 ? 0.8172 0.8944 1.1912 -0.0451 0.0809  -0.2062 191 PRO B CG  
3123 C CD  . PRO B 189 ? 0.8213 0.8753 1.1531 -0.0560 0.1041  -0.1911 191 PRO B CD  
3124 N N   . LYS B 190 ? 0.8308 0.8743 1.1294 -0.0596 0.1557  -0.1881 192 LYS B N   
3125 C CA  . LYS B 190 ? 0.8335 0.8688 1.1140 -0.0662 0.1816  -0.1883 192 LYS B CA  
3126 C C   . LYS B 190 ? 0.8426 0.8565 1.0677 -0.0605 0.1762  -0.1653 192 LYS B C   
3127 O O   . LYS B 190 ? 0.8556 0.8669 1.0686 -0.0596 0.1828  -0.1661 192 LYS B O   
3128 C CB  . LYS B 190 ? 0.8734 0.8987 1.1471 -0.0827 0.2136  -0.1916 192 LYS B CB  
3129 C CG  . LYS B 190 ? 0.9305 0.9791 1.2619 -0.0920 0.2257  -0.2179 192 LYS B CG  
3130 C CD  . LYS B 190 ? 1.0132 1.0477 1.3345 -0.1091 0.2542  -0.2189 192 LYS B CD  
3131 C CE  . LYS B 190 ? 1.0311 1.0881 1.4079 -0.1220 0.2748  -0.2474 192 LYS B CE  
3132 N NZ  . LYS B 190 ? 1.0841 1.1201 1.4411 -0.1406 0.3095  -0.2477 192 LYS B NZ  
3133 N N   . ILE B 191 ? 0.8320 0.8309 1.0246 -0.0571 0.1648  -0.1460 193 ILE B N   
3134 C CA  . ILE B 191 ? 0.8257 0.8076 0.9702 -0.0516 0.1584  -0.1246 193 ILE B CA  
3135 C C   . ILE B 191 ? 0.7885 0.7788 0.9408 -0.0398 0.1323  -0.1248 193 ILE B C   
3136 O O   . ILE B 191 ? 0.7958 0.7892 0.9584 -0.0334 0.1117  -0.1233 193 ILE B O   
3137 C CB  . ILE B 191 ? 0.8414 0.8063 0.9549 -0.0515 0.1564  -0.1056 193 ILE B CB  
3138 C CG1 . ILE B 191 ? 0.8567 0.8094 0.9632 -0.0634 0.1831  -0.1061 193 ILE B CG1 
3139 C CG2 . ILE B 191 ? 0.8623 0.8141 0.9320 -0.0450 0.1485  -0.0848 193 ILE B CG2 
3140 C CD1 . ILE B 191 ? 0.8868 0.8262 0.9664 -0.0714 0.2090  -0.1037 193 ILE B CD1 
3141 N N   . VAL B 192 ? 0.7547 0.7459 0.8996 -0.0376 0.1338  -0.1270 194 VAL B N   
3142 C CA  . VAL B 192 ? 0.7263 0.7206 0.8731 -0.0271 0.1112  -0.1264 194 VAL B CA  
3143 C C   . VAL B 192 ? 0.6979 0.6777 0.7989 -0.0241 0.1028  -0.1057 194 VAL B C   
3144 O O   . VAL B 192 ? 0.7150 0.6859 0.7854 -0.0297 0.1169  -0.0968 194 VAL B O   
3145 C CB  . VAL B 192 ? 0.7302 0.7339 0.8996 -0.0262 0.1174  -0.1431 194 VAL B CB  
3146 C CG1 . VAL B 192 ? 0.7095 0.7306 0.9286 -0.0301 0.1294  -0.1650 194 VAL B CG1 
3147 C CG2 . VAL B 192 ? 0.7617 0.7545 0.8958 -0.0329 0.1350  -0.1377 194 VAL B CG2 
3148 N N   . ILE B 193 ? 0.6533 0.6302 0.7492 -0.0159 0.0798  -0.0983 195 ILE B N   
3149 C CA  . ILE B 193 ? 0.6296 0.5958 0.6881 -0.0132 0.0707  -0.0811 195 ILE B CA  
3150 C C   . ILE B 193 ? 0.5955 0.5618 0.6525 -0.0089 0.0608  -0.0858 195 ILE B C   
3151 O O   . ILE B 193 ? 0.5816 0.5537 0.6672 -0.0042 0.0536  -0.0995 195 ILE B O   
3152 C CB  . ILE B 193 ? 0.6263 0.5852 0.6743 -0.0096 0.0571  -0.0690 195 ILE B CB  
3153 C CG1 . ILE B 193 ? 0.6129 0.5725 0.6813 -0.0030 0.0366  -0.0763 195 ILE B CG1 
3154 C CG2 . ILE B 193 ? 0.6402 0.5966 0.6884 -0.0147 0.0701  -0.0653 195 ILE B CG2 
3155 C CD1 . ILE B 193 ? 0.6311 0.5795 0.6824 -0.0006 0.0236  -0.0644 195 ILE B CD1 
3156 N N   . GLY B 194 ? 0.5756 0.5358 0.6010 -0.0103 0.0602  -0.0752 196 GLY B N   
3157 C CA  . GLY B 194 ? 0.5498 0.5076 0.5696 -0.0081 0.0527  -0.0795 196 GLY B CA  
3158 C C   . GLY B 194 ? 0.5409 0.4906 0.5388 -0.0049 0.0361  -0.0678 196 GLY B C   
3159 O O   . GLY B 194 ? 0.5532 0.5009 0.5310 -0.0063 0.0347  -0.0538 196 GLY B O   
3160 N N   . TYR B 195 ? 0.5085 0.4525 0.5113 -0.0005 0.0243  -0.0743 197 TYR B N   
3161 C CA  . TYR B 195 ? 0.4876 0.4210 0.4695 0.0009  0.0108  -0.0663 197 TYR B CA  
3162 C C   . TYR B 195 ? 0.4931 0.4252 0.4571 -0.0043 0.0158  -0.0682 197 TYR B C   
3163 O O   . TYR B 195 ? 0.4808 0.4123 0.4561 -0.0039 0.0208  -0.0806 197 TYR B O   
3164 C CB  . TYR B 195 ? 0.4643 0.3865 0.4589 0.0089  -0.0055 -0.0719 197 TYR B CB  
3165 C CG  . TYR B 195 ? 0.4678 0.3745 0.4375 0.0088  -0.0176 -0.0633 197 TYR B CG  
3166 C CD1 . TYR B 195 ? 0.4689 0.3689 0.4267 0.0090  -0.0250 -0.0527 197 TYR B CD1 
3167 C CD2 . TYR B 195 ? 0.4741 0.3711 0.4318 0.0075  -0.0197 -0.0670 197 TYR B CD2 
3168 C CE1 . TYR B 195 ? 0.4954 0.3801 0.4303 0.0073  -0.0333 -0.0460 197 TYR B CE1 
3169 C CE2 . TYR B 195 ? 0.5037 0.3850 0.4381 0.0056  -0.0285 -0.0601 197 TYR B CE2 
3170 C CZ  . TYR B 195 ? 0.5153 0.3906 0.4387 0.0053  -0.0350 -0.0497 197 TYR B CZ  
3171 O OH  . TYR B 195 ? 0.5014 0.3599 0.4016 0.0021  -0.0414 -0.0438 197 TYR B OH  
3172 N N   . GLN B 196 ? 0.5066 0.4388 0.4444 -0.0093 0.0144  -0.0569 198 GLN B N   
3173 C CA  . GLN B 196 ? 0.5186 0.4513 0.4359 -0.0161 0.0176  -0.0575 198 GLN B CA  
3174 C C   . GLN B 196 ? 0.5285 0.4523 0.4315 -0.0171 0.0056  -0.0529 198 GLN B C   
3175 O O   . GLN B 196 ? 0.5172 0.4414 0.4138 -0.0165 -0.0005 -0.0423 198 GLN B O   
3176 C CB  . GLN B 196 ? 0.5418 0.4852 0.4401 -0.0219 0.0254  -0.0475 198 GLN B CB  
3177 C CG  . GLN B 196 ? 0.6240 0.5723 0.5294 -0.0222 0.0388  -0.0484 198 GLN B CG  
3178 C CD  . GLN B 196 ? 0.7404 0.6945 0.6245 -0.0250 0.0429  -0.0344 198 GLN B CD  
3179 O OE1 . GLN B 196 ? 0.7893 0.7461 0.6683 -0.0222 0.0354  -0.0223 198 GLN B OE1 
3180 N NE2 . GLN B 196 ? 0.7621 0.7166 0.6327 -0.0303 0.0553  -0.0356 198 GLN B NE2 
3181 N N   . SER B 197 ? 0.5472 0.4617 0.4448 -0.0195 0.0042  -0.0616 199 SER B N   
3182 C CA  . SER B 197 ? 0.5809 0.4859 0.4606 -0.0242 -0.0032 -0.0592 199 SER B CA  
3183 C C   . SER B 197 ? 0.5916 0.5112 0.4531 -0.0324 -0.0017 -0.0496 199 SER B C   
3184 O O   . SER B 197 ? 0.6007 0.5328 0.4562 -0.0364 0.0057  -0.0493 199 SER B O   
3185 C CB  . SER B 197 ? 0.6499 0.5435 0.5252 -0.0273 -0.0004 -0.0716 199 SER B CB  
3186 O OG  . SER B 197 ? 0.7588 0.6397 0.6168 -0.0328 -0.0063 -0.0708 199 SER B OG  
3187 N N   . HIS B 198 ? 0.5938 0.5119 0.4468 -0.0348 -0.0086 -0.0422 200 HIS B N   
3188 C CA  . HIS B 198 ? 0.6038 0.5387 0.4442 -0.0421 -0.0087 -0.0347 200 HIS B CA  
3189 C C   . HIS B 198 ? 0.6452 0.5838 0.4709 -0.0522 -0.0064 -0.0424 200 HIS B C   
3190 O O   . HIS B 198 ? 0.6332 0.5892 0.4494 -0.0572 -0.0055 -0.0384 200 HIS B O   
3191 C CB  . HIS B 198 ? 0.5731 0.5059 0.4108 -0.0438 -0.0146 -0.0278 200 HIS B CB  
3192 C CG  . HIS B 198 ? 0.5538 0.4855 0.4015 -0.0360 -0.0157 -0.0191 200 HIS B CG  
3193 N ND1 . HIS B 198 ? 0.5549 0.4978 0.4109 -0.0303 -0.0115 -0.0132 200 HIS B ND1 
3194 C CD2 . HIS B 198 ? 0.5633 0.4812 0.4107 -0.0344 -0.0194 -0.0160 200 HIS B CD2 
3195 C CE1 . HIS B 198 ? 0.5602 0.4969 0.4224 -0.0254 -0.0130 -0.0074 200 HIS B CE1 
3196 N NE2 . HIS B 198 ? 0.5611 0.4829 0.4177 -0.0277 -0.0179 -0.0088 200 HIS B NE2 
3197 N N   . ALA B 199 ? 0.6815 0.6022 0.5040 -0.0549 -0.0062 -0.0533 201 ALA B N   
3198 C CA  . ALA B 199 ? 0.7125 0.6328 0.5203 -0.0652 -0.0023 -0.0628 201 ALA B CA  
3199 C C   . ALA B 199 ? 0.7416 0.6704 0.5463 -0.0663 0.0064  -0.0673 201 ALA B C   
3200 O O   . ALA B 199 ? 0.7588 0.6957 0.5460 -0.0763 0.0084  -0.0704 201 ALA B O   
3201 C CB  . ALA B 199 ? 0.7182 0.6128 0.5242 -0.0659 -0.0022 -0.0736 201 ALA B CB  
3202 N N   . ASP B 200 ? 0.7412 0.6679 0.5613 -0.0573 0.0121  -0.0683 202 ASP B N   
3203 C CA  . ASP B 200 ? 0.7579 0.6915 0.5731 -0.0595 0.0228  -0.0715 202 ASP B CA  
3204 C C   . ASP B 200 ? 0.7884 0.7393 0.5928 -0.0604 0.0214  -0.0578 202 ASP B C   
3205 O O   . ASP B 200 ? 0.8079 0.7652 0.5915 -0.0679 0.0249  -0.0575 202 ASP B O   
3206 C CB  . ASP B 200 ? 0.7654 0.6920 0.6035 -0.0510 0.0314  -0.0789 202 ASP B CB  
3207 C CG  . ASP B 200 ? 0.8147 0.7246 0.6675 -0.0469 0.0316  -0.0922 202 ASP B CG  
3208 O OD1 . ASP B 200 ? 0.8343 0.7344 0.6737 -0.0530 0.0302  -0.0983 202 ASP B OD1 
3209 O OD2 . ASP B 200 ? 0.8252 0.7317 0.7035 -0.0372 0.0327  -0.0967 202 ASP B OD2 
3210 N N   . THR B 201 ? 0.7911 0.7475 0.6074 -0.0527 0.0162  -0.0464 203 THR B N   
3211 C CA  . THR B 201 ? 0.8094 0.7800 0.6170 -0.0517 0.0144  -0.0325 203 THR B CA  
3212 C C   . THR B 201 ? 0.8203 0.8048 0.6097 -0.0590 0.0059  -0.0274 203 THR B C   
3213 O O   . THR B 201 ? 0.8193 0.8146 0.5953 -0.0592 0.0048  -0.0184 203 THR B O   
3214 C CB  . THR B 201 ? 0.8375 0.8096 0.6615 -0.0427 0.0106  -0.0225 203 THR B CB  
3215 O OG1 . THR B 201 ? 0.8591 0.8203 0.7014 -0.0366 0.0163  -0.0286 203 THR B OG1 
3216 C CG2 . THR B 201 ? 0.8467 0.8301 0.6636 -0.0394 0.0110  -0.0085 203 THR B CG2 
3217 N N   . ALA B 202 ? 0.8304 0.8143 0.6191 -0.0651 -0.0005 -0.0330 204 ALA B N   
3218 C CA  . ALA B 202 ? 0.8479 0.8480 0.6237 -0.0736 -0.0089 -0.0306 204 ALA B CA  
3219 C C   . ALA B 202 ? 0.8706 0.8731 0.6226 -0.0828 -0.0065 -0.0366 204 ALA B C   
3220 O O   . ALA B 202 ? 0.8779 0.8976 0.6166 -0.0869 -0.0143 -0.0306 204 ALA B O   
3221 C CB  . ALA B 202 ? 0.8516 0.8471 0.6320 -0.0799 -0.0133 -0.0372 204 ALA B CB  
3222 N N   . THR B 203 ? 0.8789 0.8643 0.6254 -0.0859 0.0039  -0.0488 205 THR B N   
3223 C CA  . THR B 203 ? 0.8913 0.8746 0.6122 -0.0961 0.0088  -0.0566 205 THR B CA  
3224 C C   . THR B 203 ? 0.8922 0.8741 0.6027 -0.0920 0.0166  -0.0503 205 THR B C   
3225 O O   . THR B 203 ? 0.8940 0.8650 0.6187 -0.0852 0.0274  -0.0527 205 THR B O   
3226 C CB  . THR B 203 ? 0.9239 0.8879 0.6438 -0.1023 0.0183  -0.0742 205 THR B CB  
3227 O OG1 . THR B 203 ? 0.9428 0.8930 0.6772 -0.0945 0.0308  -0.0795 205 THR B OG1 
3228 C CG2 . THR B 203 ? 0.9334 0.8913 0.6644 -0.1044 0.0125  -0.0796 205 THR B CG2 
3229 N N   . LYS B 204 ? 0.8905 0.8826 0.5757 -0.0964 0.0109  -0.0427 206 LYS B N   
3230 C CA  . LYS B 204 ? 0.8949 0.8802 0.5605 -0.0948 0.0194  -0.0369 206 LYS B CA  
3231 C C   . LYS B 204 ? 0.9013 0.8699 0.5447 -0.1061 0.0334  -0.0522 206 LYS B C   
3232 O O   . LYS B 204 ? 0.8958 0.8662 0.5170 -0.1176 0.0286  -0.0591 206 LYS B O   
3233 C CB  . LYS B 204 ? 0.9071 0.9073 0.5517 -0.0937 0.0056  -0.0214 206 LYS B CB  
3234 C CG  . LYS B 204 ? 0.9409 0.9517 0.6052 -0.0798 -0.0014 -0.0046 206 LYS B CG  
3235 C CD  . LYS B 204 ? 0.9883 1.0064 0.6889 -0.0732 -0.0053 -0.0046 206 LYS B CD  
3236 C CE  . LYS B 204 ? 1.0235 1.0436 0.7397 -0.0600 -0.0052 0.0099  206 LYS B CE  
3237 N NZ  . LYS B 204 ? 1.0125 1.0393 0.7595 -0.0543 -0.0099 0.0112  206 LYS B NZ  
3238 N N   . SER B 205 ? 0.9170 0.8701 0.5682 -0.1036 0.0515  -0.0588 207 SER B N   
3239 C CA  . SER B 205 ? 0.9559 0.8918 0.5924 -0.1134 0.0689  -0.0755 207 SER B CA  
3240 C C   . SER B 205 ? 0.9784 0.9009 0.5988 -0.1147 0.0868  -0.0747 207 SER B C   
3241 O O   . SER B 205 ? 0.9809 0.8889 0.5979 -0.1214 0.1055  -0.0899 207 SER B O   
3242 C CB  . SER B 205 ? 0.9800 0.9085 0.6508 -0.1098 0.0770  -0.0905 207 SER B CB  
3243 O OG  . SER B 205 ? 1.0310 0.9665 0.7177 -0.1075 0.0626  -0.0906 207 SER B OG  
3244 N N   . GLY B 206 ? 0.9989 0.9246 0.6093 -0.1089 0.0829  -0.0579 208 GLY B N   
3245 C CA  . GLY B 206 ? 1.0381 0.9481 0.6321 -0.1104 0.1010  -0.0559 208 GLY B CA  
3246 C C   . GLY B 206 ? 1.0621 0.9758 0.6701 -0.0986 0.0982  -0.0396 208 GLY B C   
3247 O O   . GLY B 206 ? 1.0498 0.9787 0.6692 -0.0899 0.0798  -0.0267 208 GLY B O   
3248 N N   . SER B 207 ? 1.0906 0.9896 0.6984 -0.0990 0.1184  -0.0412 209 SER B N   
3249 C CA  . SER B 207 ? 1.1049 1.0034 0.7258 -0.0892 0.1198  -0.0276 209 SER B CA  
3250 C C   . SER B 207 ? 1.0980 1.0087 0.7718 -0.0795 0.1174  -0.0322 209 SER B C   
3251 O O   . SER B 207 ? 1.1007 1.0127 0.7875 -0.0714 0.1161  -0.0213 209 SER B O   
3252 C CB  . SER B 207 ? 1.1378 1.0139 0.7368 -0.0952 0.1436  -0.0283 209 SER B CB  
3253 O OG  . SER B 207 ? 1.1723 1.0363 0.7669 -0.1069 0.1651  -0.0476 209 SER B OG  
3254 N N   . THR B 208 ? 1.0857 1.0031 0.7875 -0.0802 0.1164  -0.0479 210 THR B N   
3255 C CA  . THR B 208 ? 1.0721 0.9982 0.8204 -0.0711 0.1129  -0.0530 210 THR B CA  
3256 C C   . THR B 208 ? 1.0393 0.9736 0.8034 -0.0691 0.0984  -0.0597 210 THR B C   
3257 O O   . THR B 208 ? 1.0567 0.9885 0.8025 -0.0766 0.0972  -0.0668 210 THR B O   
3258 C CB  . THR B 208 ? 1.0954 1.0153 0.8701 -0.0729 0.1336  -0.0691 210 THR B CB  
3259 O OG1 . THR B 208 ? 1.1235 1.0345 0.8839 -0.0830 0.1478  -0.0842 210 THR B OG1 
3260 C CG2 . THR B 208 ? 1.0979 1.0107 0.8710 -0.0728 0.1476  -0.0624 210 THR B CG2 
3261 N N   . THR B 209 ? 0.9839 0.9252 0.7791 -0.0597 0.0879  -0.0575 211 THR B N   
3262 C CA  . THR B 209 ? 0.9446 0.8882 0.7589 -0.0566 0.0767  -0.0650 211 THR B CA  
3263 C C   . THR B 209 ? 0.9038 0.8436 0.7535 -0.0518 0.0847  -0.0801 211 THR B C   
3264 O O   . THR B 209 ? 0.9036 0.8447 0.7716 -0.0485 0.0930  -0.0808 211 THR B O   
3265 C CB  . THR B 209 ? 0.9356 0.8870 0.7565 -0.0496 0.0595  -0.0515 211 THR B CB  
3266 O OG1 . THR B 209 ? 0.9557 0.9140 0.7490 -0.0528 0.0528  -0.0381 211 THR B OG1 
3267 C CG2 . THR B 209 ? 0.9192 0.8685 0.7534 -0.0472 0.0480  -0.0574 211 THR B CG2 
3268 N N   . LYS B 210 ? 0.8641 0.7990 0.7246 -0.0513 0.0817  -0.0924 212 LYS B N   
3269 C CA  . LYS B 210 ? 0.8289 0.7617 0.7268 -0.0440 0.0852  -0.1061 212 LYS B CA  
3270 C C   . LYS B 210 ? 0.7767 0.7130 0.6977 -0.0333 0.0702  -0.0989 212 LYS B C   
3271 O O   . LYS B 210 ? 0.7879 0.7236 0.6972 -0.0316 0.0559  -0.0877 212 LYS B O   
3272 C CB  . LYS B 210 ? 0.8721 0.7955 0.7751 -0.0447 0.0864  -0.1210 212 LYS B CB  
3273 C CG  . LYS B 210 ? 0.9412 0.8580 0.8294 -0.0446 0.0703  -0.1160 212 LYS B CG  
3274 C CD  . LYS B 210 ? 0.9925 0.8958 0.8907 -0.0427 0.0716  -0.1312 212 LYS B CD  
3275 C CE  . LYS B 210 ? 1.0454 0.9407 0.9114 -0.0547 0.0755  -0.1354 212 LYS B CE  
3276 N NZ  . LYS B 210 ? 1.0703 0.9490 0.9398 -0.0519 0.0692  -0.1433 212 LYS B NZ  
3277 N N   . ASN B 211 ? 0.7242 0.6642 0.6774 -0.0273 0.0744  -0.1062 213 ASN B N   
3278 C CA  . ASN B 211 ? 0.6929 0.6345 0.6708 -0.0174 0.0605  -0.1036 213 ASN B CA  
3279 C C   . ASN B 211 ? 0.6891 0.6238 0.6895 -0.0091 0.0508  -0.1152 213 ASN B C   
3280 O O   . ASN B 211 ? 0.6967 0.6340 0.7226 -0.0068 0.0597  -0.1304 213 ASN B O   
3281 C CB  . ASN B 211 ? 0.6756 0.6263 0.6785 -0.0163 0.0701  -0.1075 213 ASN B CB  
3282 C CG  . ASN B 211 ? 0.7212 0.6747 0.7049 -0.0217 0.0777  -0.0944 213 ASN B CG  
3283 O OD1 . ASN B 211 ? 0.7414 0.6983 0.7340 -0.0260 0.0939  -0.0996 213 ASN B OD1 
3284 N ND2 . ASN B 211 ? 0.7300 0.6815 0.6889 -0.0217 0.0681  -0.0779 213 ASN B ND2 
3285 N N   . ARG B 212 ? 0.6902 0.6148 0.6814 -0.0045 0.0337  -0.1086 214 ARG B N   
3286 C CA  . ARG B 212 ? 0.6946 0.6080 0.7043 0.0053  0.0222  -0.1173 214 ARG B CA  
3287 C C   . ARG B 212 ? 0.6686 0.5893 0.7171 0.0157  0.0159  -0.1241 214 ARG B C   
3288 O O   . ARG B 212 ? 0.6678 0.5859 0.7430 0.0241  0.0130  -0.1370 214 ARG B O   
3289 C CB  . ARG B 212 ? 0.7416 0.6385 0.7271 0.0065  0.0061  -0.1072 214 ARG B CB  
3290 C CG  . ARG B 212 ? 0.8268 0.7045 0.8187 0.0143  -0.0026 -0.1160 214 ARG B CG  
3291 C CD  . ARG B 212 ? 0.9234 0.7822 0.8822 0.0093  -0.0095 -0.1087 214 ARG B CD  
3292 N NE  . ARG B 212 ? 0.9791 0.8417 0.9157 -0.0033 0.0031  -0.1102 214 ARG B NE  
3293 C CZ  . ARG B 212 ? 1.0386 0.8912 0.9465 -0.0117 0.0004  -0.1049 214 ARG B CZ  
3294 N NH1 . ARG B 212 ? 1.0452 0.9038 0.9345 -0.0236 0.0107  -0.1075 214 ARG B NH1 
3295 N NH2 . ARG B 212 ? 1.0435 0.8796 0.9398 -0.0093 -0.0121 -0.0976 214 ARG B NH2 
3296 N N   . PHE B 213 ? 0.6380 0.5677 0.6910 0.0153  0.0135  -0.1164 215 PHE B N   
3297 C CA  . PHE B 213 ? 0.6115 0.5512 0.7013 0.0224  0.0088  -0.1240 215 PHE B CA  
3298 C C   . PHE B 213 ? 0.6185 0.5722 0.7117 0.0150  0.0220  -0.1204 215 PHE B C   
3299 O O   . PHE B 213 ? 0.6244 0.5770 0.6881 0.0068  0.0306  -0.1087 215 PHE B O   
3300 C CB  . PHE B 213 ? 0.6079 0.5365 0.6995 0.0320  -0.0152 -0.1186 215 PHE B CB  
3301 C CG  . PHE B 213 ? 0.6371 0.5434 0.7071 0.0368  -0.0293 -0.1144 215 PHE B CG  
3302 C CD1 . PHE B 213 ? 0.6549 0.5526 0.7420 0.0461  -0.0354 -0.1256 215 PHE B CD1 
3303 C CD2 . PHE B 213 ? 0.6653 0.5579 0.6986 0.0319  -0.0351 -0.0998 215 PHE B CD2 
3304 C CE1 . PHE B 213 ? 0.6818 0.5542 0.7450 0.0497  -0.0467 -0.1214 215 PHE B CE1 
3305 C CE2 . PHE B 213 ? 0.6912 0.5607 0.7030 0.0345  -0.0460 -0.0966 215 PHE B CE2 
3306 C CZ  . PHE B 213 ? 0.6930 0.5508 0.7182 0.0434  -0.0520 -0.1070 215 PHE B CZ  
3307 N N   . VAL B 214 ? 0.6199 0.5862 0.7496 0.0182  0.0231  -0.1309 216 VAL B N   
3308 C CA  . VAL B 214 ? 0.6378 0.6158 0.7761 0.0108  0.0374  -0.1307 216 VAL B CA  
3309 C C   . VAL B 214 ? 0.6308 0.6173 0.8025 0.0168  0.0242  -0.1371 216 VAL B C   
3310 O O   . VAL B 214 ? 0.6185 0.6096 0.8206 0.0260  0.0121  -0.1489 216 VAL B O   
3311 C CB  . VAL B 214 ? 0.6500 0.6373 0.8009 0.0031  0.0631  -0.1434 216 VAL B CB  
3312 C CG1 . VAL B 214 ? 0.6658 0.6617 0.8254 -0.0054 0.0797  -0.1444 216 VAL B CG1 
3313 C CG2 . VAL B 214 ? 0.6618 0.6390 0.7745 -0.0037 0.0738  -0.1368 216 VAL B CG2 
3314 N N   . VAL B 215 ? 0.6481 0.6358 0.8131 0.0120  0.0257  -0.1291 217 VAL B N   
3315 C CA  . VAL B 215 ? 0.6444 0.6411 0.8392 0.0145  0.0157  -0.1361 217 VAL B CA  
3316 C C   . VAL B 215 ? 0.6505 0.6549 0.8509 0.0040  0.0346  -0.1370 217 VAL B C   
3317 O O   . VAL B 215 ? 0.6450 0.6610 0.8769 0.0034  0.0308  -0.1473 217 VAL B O   
3318 C CB  . VAL B 215 ? 0.6643 0.6473 0.8412 0.0206  -0.0087 -0.1254 217 VAL B CB  
3319 C CG1 . VAL B 215 ? 0.6747 0.6467 0.8478 0.0313  -0.0282 -0.1260 217 VAL B CG1 
3320 C CG2 . VAL B 215 ? 0.6966 0.6659 0.8313 0.0146  -0.0038 -0.1066 217 VAL B CG2 
3321 O OXT . VAL B 215 ? 0.6606 0.6584 0.8330 -0.0039 0.0524  -0.1273 217 VAL B OXT 
# 
