data_8QM8
# 
_entry.id   8QM8 
# 
_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   8QM8         pdb_00008qm8 10.2210/pdb8qm8/pdb 
WWPDB D_1292133486 ?            ?                   
# 
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                        8QM8 
_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'                                                25015.432 2   ? ? ? 
? 
2 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                                                      106.120   6   ? ? ? 
? 
3 non-polymer syn 'TRIETHYLENE GLYCOL'                                                                         150.173   1   ? ? ? 
? 
4 non-polymer syn '(2~{R})-2-[(1~{S})-1-[4-(2-fluorophenyl)-2-(2-hydroxyethylamino)phenyl]propoxy]propan-1-ol' 347.424   2   ? ? ? 
? 
5 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                         78.133    3   ? ? ? 
? 
6 water       nat water                                                                                        18.015    401 ? ? ? 
? 
# 
_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
SNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDK
IAIWTTECENREAVTHIGRVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MHHHHHHGARIIYDRAFLMACRGGGGENLYFQGKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLS
SNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDK
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 'DI(HYDROXYETHYL)ETHER'                                                                      PEG 
3 'TRIETHYLENE GLYCOL'                                                                         PGE 
4 '(2~{R})-2-[(1~{S})-1-[4-(2-fluorophenyl)-2-(2-hydroxyethylamino)phenyl]propoxy]propan-1-ol' W4K 
5 'DIMETHYL SULFOXIDE'                                                                         DMS 
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 ASP 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 
W4K non-polymer         . '(2~{R})-2-[(1~{S})-1-[4-(2-fluorophenyl)-2-(2-hydroxyethylamino)phenyl]propoxy]propan-1-ol' ? 
'C20 H26 F N O3' 347.424 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   3   ?   ?   ?   A . n 
A 1 2   HIS 2   4   ?   ?   ?   A . n 
A 1 3   HIS 3   5   ?   ?   ?   A . n 
A 1 4   HIS 4   6   ?   ?   ?   A . n 
A 1 5   HIS 5   7   ?   ?   ?   A . n 
A 1 6   HIS 6   8   ?   ?   ?   A . n 
A 1 7   HIS 7   9   ?   ?   ?   A . n 
A 1 8   GLY 8   10  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 ASP 125 127 127 ASP ASP 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 ?   ?   ?   A . n 
A 1 206 GLY 206 208 ?   ?   ?   A . n 
A 1 207 SER 207 209 ?   ?   ?   A . n 
A 1 208 THR 208 210 ?   ?   ?   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  10  GLY GLY 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  26  GLY GLY B . n 
B 1 25  GLY 25  27  27  GLY GLY B . n 
B 1 26  GLY 26  28  28  GLY GLY B . n 
B 1 27  GLU 27  29  29  GLU GLU B . n 
B 1 28  ASN 28  30  30  ASN ASN B . n 
B 1 29  LEU 29  31  31  LEU LEU B . n 
B 1 30  TYR 30  32  32  TYR TYR B . n 
B 1 31  PHE 31  33  33  PHE PHE B . n 
B 1 32  GLN 32  34  34  GLN GLN B . n 
B 1 33  GLY 33  35  35  GLY GLY 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 ASP 125 127 127 ASP ASP 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 ?   ?   ?   B . n 
B 1 206 GLY 206 208 ?   ?   ?   B . n 
B 1 207 SER 207 209 ?   ?   ?   B . n 
B 1 208 THR 208 210 ?   ?   ?   B . n 
B 1 209 THR 209 211 211 THR THR B . n 
B 1 210 LYS 210 212 212 LYS LYS B . n 
B 1 211 ASN 211 213 213 ASN ASN B . n 
B 1 212 ARG 212 214 214 ARG ARG B . n 
B 1 213 PHE 213 215 215 PHE PHE B . n 
B 1 214 VAL 214 216 216 VAL VAL B . n 
B 1 215 VAL 215 217 217 VAL VAL B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 W4K ? ? W4K ? ? 'SUBJECT OF INVESTIGATION' ? 
2 W4K ? ? W4K ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 PEG 1   401  401 PEG PEG A . 
D 2 PEG 1   402  501 PEG PEG A . 
E 2 PEG 1   403  834 PEG PEG A . 
F 3 PGE 1   404  839 PGE PGE A . 
G 2 PEG 1   405  866 PEG PEG A . 
H 4 W4K 1   406  1   W4K L01 A . 
I 5 DMS 1   301  301 DMS DMS B . 
J 5 DMS 1   302  401 DMS DMS B . 
K 5 DMS 1   303  601 DMS DMS B . 
L 2 PEG 1   304  701 PEG PEG B . 
M 2 PEG 1   305  830 PEG PEG B . 
N 4 W4K 1   306  1   W4K L02 B . 
O 6 HOH 1   901  901 HOH HOH A . 
O 6 HOH 2   902  541 HOH HOH A . 
O 6 HOH 3   903  509 HOH HOH A . 
O 6 HOH 4   904  26  HOH HOH A . 
O 6 HOH 5   905  500 HOH HOH A . 
O 6 HOH 6   906  559 HOH HOH A . 
O 6 HOH 7   907  689 HOH HOH A . 
O 6 HOH 8   908  16  HOH HOH A . 
O 6 HOH 9   909  784 HOH HOH A . 
O 6 HOH 10  910  528 HOH HOH A . 
O 6 HOH 11  911  836 HOH HOH A . 
O 6 HOH 12  912  560 HOH HOH A . 
O 6 HOH 13  913  753 HOH HOH A . 
O 6 HOH 14  914  656 HOH HOH A . 
O 6 HOH 15  915  616 HOH HOH A . 
O 6 HOH 16  916  503 HOH HOH A . 
O 6 HOH 17  917  683 HOH HOH A . 
O 6 HOH 18  918  455 HOH HOH A . 
O 6 HOH 19  919  489 HOH HOH A . 
O 6 HOH 20  920  553 HOH HOH A . 
O 6 HOH 21  921  496 HOH HOH A . 
O 6 HOH 22  922  4   HOH HOH A . 
O 6 HOH 23  923  484 HOH HOH A . 
O 6 HOH 24  924  755 HOH HOH A . 
O 6 HOH 25  925  639 HOH HOH A . 
O 6 HOH 26  926  537 HOH HOH A . 
O 6 HOH 27  927  483 HOH HOH A . 
O 6 HOH 28  928  731 HOH HOH A . 
O 6 HOH 29  929  778 HOH HOH A . 
O 6 HOH 30  930  741 HOH HOH A . 
O 6 HOH 31  931  701 HOH HOH A . 
O 6 HOH 32  932  556 HOH HOH A . 
O 6 HOH 33  933  582 HOH HOH A . 
O 6 HOH 34  934  462 HOH HOH A . 
O 6 HOH 35  935  659 HOH HOH A . 
O 6 HOH 36  936  522 HOH HOH A . 
O 6 HOH 37  937  614 HOH HOH A . 
O 6 HOH 38  938  864 HOH HOH A . 
O 6 HOH 39  939  409 HOH HOH A . 
O 6 HOH 40  940  903 HOH HOH A . 
O 6 HOH 41  941  881 HOH HOH A . 
O 6 HOH 42  942  506 HOH HOH A . 
O 6 HOH 43  943  687 HOH HOH A . 
O 6 HOH 44  944  696 HOH HOH A . 
O 6 HOH 45  945  495 HOH HOH A . 
O 6 HOH 46  946  655 HOH HOH A . 
O 6 HOH 47  947  402 HOH HOH A . 
O 6 HOH 48  948  672 HOH HOH A . 
O 6 HOH 49  949  396 HOH HOH A . 
O 6 HOH 50  950  425 HOH HOH A . 
O 6 HOH 51  951  589 HOH HOH A . 
O 6 HOH 52  952  463 HOH HOH A . 
O 6 HOH 53  953  423 HOH HOH A . 
O 6 HOH 54  954  459 HOH HOH A . 
O 6 HOH 55  955  404 HOH HOH A . 
O 6 HOH 56  956  535 HOH HOH A . 
O 6 HOH 57  957  698 HOH HOH A . 
O 6 HOH 58  958  389 HOH HOH A . 
O 6 HOH 59  959  648 HOH HOH A . 
O 6 HOH 60  960  669 HOH HOH A . 
O 6 HOH 61  961  398 HOH HOH A . 
O 6 HOH 62  962  403 HOH HOH A . 
O 6 HOH 63  963  420 HOH HOH A . 
O 6 HOH 64  964  448 HOH HOH A . 
O 6 HOH 65  965  756 HOH HOH A . 
O 6 HOH 66  966  401 HOH HOH A . 
O 6 HOH 67  967  394 HOH HOH A . 
O 6 HOH 68  968  13  HOH HOH A . 
O 6 HOH 69  969  782 HOH HOH A . 
O 6 HOH 70  970  781 HOH HOH A . 
O 6 HOH 71  971  750 HOH HOH A . 
O 6 HOH 72  972  18  HOH HOH A . 
O 6 HOH 73  973  438 HOH HOH A . 
O 6 HOH 74  974  754 HOH HOH A . 
O 6 HOH 75  975  439 HOH HOH A . 
O 6 HOH 76  976  539 HOH HOH A . 
O 6 HOH 77  977  510 HOH HOH A . 
O 6 HOH 78  978  486 HOH HOH A . 
O 6 HOH 79  979  617 HOH HOH A . 
O 6 HOH 80  980  479 HOH HOH A . 
O 6 HOH 81  981  533 HOH HOH A . 
O 6 HOH 82  982  837 HOH HOH A . 
O 6 HOH 83  983  502 HOH HOH A . 
O 6 HOH 84  984  447 HOH HOH A . 
O 6 HOH 85  985  605 HOH HOH A . 
O 6 HOH 86  986  635 HOH HOH A . 
O 6 HOH 87  987  450 HOH HOH A . 
O 6 HOH 88  988  513 HOH HOH A . 
O 6 HOH 89  989  467 HOH HOH A . 
O 6 HOH 90  990  417 HOH HOH A . 
O 6 HOH 91  991  827 HOH HOH A . 
O 6 HOH 92  992  663 HOH HOH A . 
O 6 HOH 93  993  411 HOH HOH A . 
O 6 HOH 94  994  395 HOH HOH A . 
O 6 HOH 95  995  493 HOH HOH A . 
O 6 HOH 96  996  676 HOH HOH A . 
O 6 HOH 97  997  452 HOH HOH A . 
O 6 HOH 98  998  637 HOH HOH A . 
O 6 HOH 99  999  799 HOH HOH A . 
O 6 HOH 100 1000 838 HOH HOH A . 
O 6 HOH 101 1001 703 HOH HOH A . 
O 6 HOH 102 1002 746 HOH HOH A . 
O 6 HOH 103 1003 473 HOH HOH A . 
O 6 HOH 104 1004 726 HOH HOH A . 
O 6 HOH 105 1005 413 HOH HOH A . 
O 6 HOH 106 1006 435 HOH HOH A . 
O 6 HOH 107 1007 757 HOH HOH A . 
O 6 HOH 108 1008 514 HOH HOH A . 
O 6 HOH 109 1009 875 HOH HOH A . 
O 6 HOH 110 1010 576 HOH HOH A . 
O 6 HOH 111 1011 727 HOH HOH A . 
O 6 HOH 112 1012 822 HOH HOH A . 
O 6 HOH 113 1013 461 HOH HOH A . 
O 6 HOH 114 1014 893 HOH HOH A . 
O 6 HOH 115 1015 645 HOH HOH A . 
O 6 HOH 116 1016 647 HOH HOH A . 
O 6 HOH 117 1017 440 HOH HOH A . 
O 6 HOH 118 1018 451 HOH HOH A . 
O 6 HOH 119 1019 631 HOH HOH A . 
O 6 HOH 120 1020 516 HOH HOH A . 
O 6 HOH 121 1021 588 HOH HOH A . 
O 6 HOH 122 1022 714 HOH HOH A . 
O 6 HOH 123 1023 412 HOH HOH A . 
O 6 HOH 124 1024 520 HOH HOH A . 
O 6 HOH 125 1025 507 HOH HOH A . 
O 6 HOH 126 1026 797 HOH HOH A . 
O 6 HOH 127 1027 517 HOH HOH A . 
O 6 HOH 128 1028 596 HOH HOH A . 
O 6 HOH 129 1029 419 HOH HOH A . 
O 6 HOH 130 1030 624 HOH HOH A . 
O 6 HOH 131 1031 597 HOH HOH A . 
O 6 HOH 132 1032 492 HOH HOH A . 
O 6 HOH 133 1033 826 HOH HOH A . 
O 6 HOH 134 1034 636 HOH HOH A . 
O 6 HOH 135 1035 469 HOH HOH A . 
O 6 HOH 136 1036 400 HOH HOH A . 
O 6 HOH 137 1037 482 HOH HOH A . 
O 6 HOH 138 1038 707 HOH HOH A . 
O 6 HOH 139 1039 874 HOH HOH A . 
O 6 HOH 140 1040 17  HOH HOH A . 
O 6 HOH 141 1041 532 HOH HOH A . 
O 6 HOH 142 1042 894 HOH HOH A . 
O 6 HOH 143 1043 445 HOH HOH A . 
O 6 HOH 144 1044 740 HOH HOH A . 
O 6 HOH 145 1045 550 HOH HOH A . 
O 6 HOH 146 1046 889 HOH HOH A . 
O 6 HOH 147 1047 498 HOH HOH A . 
O 6 HOH 148 1048 795 HOH HOH A . 
O 6 HOH 149 1049 629 HOH HOH A . 
O 6 HOH 150 1050 490 HOH HOH A . 
O 6 HOH 151 1051 591 HOH HOH A . 
O 6 HOH 152 1052 565 HOH HOH A . 
O 6 HOH 153 1053 602 HOH HOH A . 
O 6 HOH 154 1054 542 HOH HOH A . 
O 6 HOH 155 1055 734 HOH HOH A . 
O 6 HOH 156 1056 642 HOH HOH A . 
O 6 HOH 157 1057 793 HOH HOH A . 
O 6 HOH 158 1058 664 HOH HOH A . 
O 6 HOH 159 1059 824 HOH HOH A . 
O 6 HOH 160 1060 15  HOH HOH A . 
O 6 HOH 161 1061 505 HOH HOH A . 
O 6 HOH 162 1062 895 HOH HOH A . 
O 6 HOH 163 1063 622 HOH HOH A . 
O 6 HOH 164 1064 519 HOH HOH A . 
O 6 HOH 165 1065 544 HOH HOH A . 
O 6 HOH 166 1066 712 HOH HOH A . 
O 6 HOH 167 1067 765 HOH HOH A . 
O 6 HOH 168 1068 763 HOH HOH A . 
O 6 HOH 169 1069 671 HOH HOH A . 
O 6 HOH 170 1070 632 HOH HOH A . 
O 6 HOH 171 1071 529 HOH HOH A . 
O 6 HOH 172 1072 485 HOH HOH A . 
O 6 HOH 173 1073 662 HOH HOH A . 
O 6 HOH 174 1074 634 HOH HOH A . 
O 6 HOH 175 1075 764 HOH HOH A . 
O 6 HOH 176 1076 880 HOH HOH A . 
O 6 HOH 177 1077 751 HOH HOH A . 
O 6 HOH 178 1078 25  HOH HOH A . 
O 6 HOH 179 1079 692 HOH HOH A . 
O 6 HOH 180 1080 526 HOH HOH A . 
O 6 HOH 181 1081 833 HOH HOH A . 
O 6 HOH 182 1082 581 HOH HOH A . 
O 6 HOH 183 1083 525 HOH HOH A . 
O 6 HOH 184 1084 800 HOH HOH A . 
O 6 HOH 185 1085 721 HOH HOH A . 
O 6 HOH 186 1086 578 HOH HOH A . 
O 6 HOH 187 1087 870 HOH HOH A . 
O 6 HOH 188 1088 562 HOH HOH A . 
O 6 HOH 189 1089 745 HOH HOH A . 
O 6 HOH 190 1090 820 HOH HOH A . 
O 6 HOH 191 1091 10  HOH HOH A . 
O 6 HOH 192 1092 728 HOH HOH A . 
P 6 HOH 1   401  668 HOH HOH B . 
P 6 HOH 2   402  491 HOH HOH B . 
P 6 HOH 3   403  558 HOH HOH B . 
P 6 HOH 4   404  9   HOH HOH B . 
P 6 HOH 5   405  12  HOH HOH B . 
P 6 HOH 6   406  24  HOH HOH B . 
P 6 HOH 7   407  652 HOH HOH B . 
P 6 HOH 8   408  651 HOH HOH B . 
P 6 HOH 9   409  540 HOH HOH B . 
P 6 HOH 10  410  618 HOH HOH B . 
P 6 HOH 11  411  737 HOH HOH B . 
P 6 HOH 12  412  808 HOH HOH B . 
P 6 HOH 13  413  568 HOH HOH B . 
P 6 HOH 14  414  590 HOH HOH B . 
P 6 HOH 15  415  710 HOH HOH B . 
P 6 HOH 16  416  884 HOH HOH B . 
P 6 HOH 17  417  774 HOH HOH B . 
P 6 HOH 18  418  584 HOH HOH B . 
P 6 HOH 19  419  431 HOH HOH B . 
P 6 HOH 20  420  619 HOH HOH B . 
P 6 HOH 21  421  472 HOH HOH B . 
P 6 HOH 22  422  27  HOH HOH B . 
P 6 HOH 23  423  499 HOH HOH B . 
P 6 HOH 24  424  497 HOH HOH B . 
P 6 HOH 25  425  823 HOH HOH B . 
P 6 HOH 26  426  441 HOH HOH B . 
P 6 HOH 27  427  454 HOH HOH B . 
P 6 HOH 28  428  690 HOH HOH B . 
P 6 HOH 29  429  583 HOH HOH B . 
P 6 HOH 30  430  569 HOH HOH B . 
P 6 HOH 31  431  523 HOH HOH B . 
P 6 HOH 32  432  858 HOH HOH B . 
P 6 HOH 33  433  512 HOH HOH B . 
P 6 HOH 34  434  563 HOH HOH B . 
P 6 HOH 35  435  426 HOH HOH B . 
P 6 HOH 36  436  405 HOH HOH B . 
P 6 HOH 37  437  415 HOH HOH B . 
P 6 HOH 38  438  598 HOH HOH B . 
P 6 HOH 39  439  840 HOH HOH B . 
P 6 HOH 40  440  422 HOH HOH B . 
P 6 HOH 41  441  429 HOH HOH B . 
P 6 HOH 42  442  468 HOH HOH B . 
P 6 HOH 43  443  818 HOH HOH B . 
P 6 HOH 44  444  487 HOH HOH B . 
P 6 HOH 45  445  397 HOH HOH B . 
P 6 HOH 46  446  567 HOH HOH B . 
P 6 HOH 47  447  862 HOH HOH B . 
P 6 HOH 48  448  611 HOH HOH B . 
P 6 HOH 49  449  444 HOH HOH B . 
P 6 HOH 50  450  722 HOH HOH B . 
P 6 HOH 51  451  390 HOH HOH B . 
P 6 HOH 52  452  407 HOH HOH B . 
P 6 HOH 53  453  789 HOH HOH B . 
P 6 HOH 54  454  442 HOH HOH B . 
P 6 HOH 55  455  437 HOH HOH B . 
P 6 HOH 56  456  478 HOH HOH B . 
P 6 HOH 57  457  574 HOH HOH B . 
P 6 HOH 58  458  477 HOH HOH B . 
P 6 HOH 59  459  458 HOH HOH B . 
P 6 HOH 60  460  416 HOH HOH B . 
P 6 HOH 61  461  814 HOH HOH B . 
P 6 HOH 62  462  531 HOH HOH B . 
P 6 HOH 63  463  480 HOH HOH B . 
P 6 HOH 64  464  705 HOH HOH B . 
P 6 HOH 65  465  579 HOH HOH B . 
P 6 HOH 66  466  421 HOH HOH B . 
P 6 HOH 67  467  573 HOH HOH B . 
P 6 HOH 68  468  730 HOH HOH B . 
P 6 HOH 69  469  433 HOH HOH B . 
P 6 HOH 70  470  886 HOH HOH B . 
P 6 HOH 71  471  729 HOH HOH B . 
P 6 HOH 72  472  511 HOH HOH B . 
P 6 HOH 73  473  399 HOH HOH B . 
P 6 HOH 74  474  392 HOH HOH B . 
P 6 HOH 75  475  406 HOH HOH B . 
P 6 HOH 76  476  536 HOH HOH B . 
P 6 HOH 77  477  854 HOH HOH B . 
P 6 HOH 78  478  5   HOH HOH B . 
P 6 HOH 79  479  393 HOH HOH B . 
P 6 HOH 80  480  811 HOH HOH B . 
P 6 HOH 81  481  809 HOH HOH B . 
P 6 HOH 82  482  566 HOH HOH B . 
P 6 HOH 83  483  504 HOH HOH B . 
P 6 HOH 84  484  658 HOH HOH B . 
P 6 HOH 85  485  725 HOH HOH B . 
P 6 HOH 86  486  460 HOH HOH B . 
P 6 HOH 87  487  877 HOH HOH B . 
P 6 HOH 88  488  534 HOH HOH B . 
P 6 HOH 89  489  810 HOH HOH B . 
P 6 HOH 90  490  607 HOH HOH B . 
P 6 HOH 91  491  414 HOH HOH B . 
P 6 HOH 92  492  427 HOH HOH B . 
P 6 HOH 93  493  424 HOH HOH B . 
P 6 HOH 94  494  900 HOH HOH B . 
P 6 HOH 95  495  464 HOH HOH B . 
P 6 HOH 96  496  8   HOH HOH B . 
P 6 HOH 97  497  410 HOH HOH B . 
P 6 HOH 98  498  488 HOH HOH B . 
P 6 HOH 99  499  654 HOH HOH B . 
P 6 HOH 100 500  430 HOH HOH B . 
P 6 HOH 101 501  844 HOH HOH B . 
P 6 HOH 102 502  501 HOH HOH B . 
P 6 HOH 103 503  481 HOH HOH B . 
P 6 HOH 104 504  418 HOH HOH B . 
P 6 HOH 105 505  595 HOH HOH B . 
P 6 HOH 106 506  680 HOH HOH B . 
P 6 HOH 107 507  471 HOH HOH B . 
P 6 HOH 108 508  786 HOH HOH B . 
P 6 HOH 109 509  543 HOH HOH B . 
P 6 HOH 110 510  677 HOH HOH B . 
P 6 HOH 111 511  465 HOH HOH B . 
P 6 HOH 112 512  446 HOH HOH B . 
P 6 HOH 113 513  813 HOH HOH B . 
P 6 HOH 114 514  547 HOH HOH B . 
P 6 HOH 115 515  474 HOH HOH B . 
P 6 HOH 116 516  443 HOH HOH B . 
P 6 HOH 117 517  609 HOH HOH B . 
P 6 HOH 118 518  640 HOH HOH B . 
P 6 HOH 119 519  667 HOH HOH B . 
P 6 HOH 120 520  456 HOH HOH B . 
P 6 HOH 121 521  476 HOH HOH B . 
P 6 HOH 122 522  555 HOH HOH B . 
P 6 HOH 123 523  847 HOH HOH B . 
P 6 HOH 124 524  518 HOH HOH B . 
P 6 HOH 125 525  801 HOH HOH B . 
P 6 HOH 126 526  557 HOH HOH B . 
P 6 HOH 127 527  428 HOH HOH B . 
P 6 HOH 128 528  538 HOH HOH B . 
P 6 HOH 129 529  899 HOH HOH B . 
P 6 HOH 130 530  646 HOH HOH B . 
P 6 HOH 131 531  19  HOH HOH B . 
P 6 HOH 132 532  508 HOH HOH B . 
P 6 HOH 133 533  475 HOH HOH B . 
P 6 HOH 134 534  434 HOH HOH B . 
P 6 HOH 135 535  845 HOH HOH B . 
P 6 HOH 136 536  665 HOH HOH B . 
P 6 HOH 137 537  666 HOH HOH B . 
P 6 HOH 138 538  572 HOH HOH B . 
P 6 HOH 139 539  436 HOH HOH B . 
P 6 HOH 140 540  702 HOH HOH B . 
P 6 HOH 141 541  771 HOH HOH B . 
P 6 HOH 142 542  674 HOH HOH B . 
P 6 HOH 143 543  678 HOH HOH B . 
P 6 HOH 144 544  804 HOH HOH B . 
P 6 HOH 145 545  732 HOH HOH B . 
P 6 HOH 146 546  554 HOH HOH B . 
P 6 HOH 147 547  6   HOH HOH B . 
P 6 HOH 148 548  738 HOH HOH B . 
P 6 HOH 149 549  803 HOH HOH B . 
P 6 HOH 150 550  685 HOH HOH B . 
P 6 HOH 151 551  2   HOH HOH B . 
P 6 HOH 152 552  545 HOH HOH B . 
P 6 HOH 153 553  860 HOH HOH B . 
P 6 HOH 154 554  679 HOH HOH B . 
P 6 HOH 155 555  593 HOH HOH B . 
P 6 HOH 156 556  524 HOH HOH B . 
P 6 HOH 157 557  882 HOH HOH B . 
P 6 HOH 158 558  749 HOH HOH B . 
P 6 HOH 159 559  494 HOH HOH B . 
P 6 HOH 160 560  867 HOH HOH B . 
P 6 HOH 161 561  688 HOH HOH B . 
P 6 HOH 162 562  876 HOH HOH B . 
P 6 HOH 163 563  549 HOH HOH B . 
P 6 HOH 164 564  564 HOH HOH B . 
P 6 HOH 165 565  615 HOH HOH B . 
P 6 HOH 166 566  575 HOH HOH B . 
P 6 HOH 167 567  719 HOH HOH B . 
P 6 HOH 168 568  449 HOH HOH B . 
P 6 HOH 169 569  853 HOH HOH B . 
P 6 HOH 170 570  851 HOH HOH B . 
P 6 HOH 171 571  457 HOH HOH B . 
P 6 HOH 172 572  22  HOH HOH B . 
P 6 HOH 173 573  776 HOH HOH B . 
P 6 HOH 174 574  577 HOH HOH B . 
P 6 HOH 175 575  20  HOH HOH B . 
P 6 HOH 176 576  859 HOH HOH B . 
P 6 HOH 177 577  657 HOH HOH B . 
P 6 HOH 178 578  821 HOH HOH B . 
P 6 HOH 179 579  681 HOH HOH B . 
P 6 HOH 180 580  23  HOH HOH B . 
P 6 HOH 181 581  697 HOH HOH B . 
P 6 HOH 182 582  700 HOH HOH B . 
P 6 HOH 183 583  530 HOH HOH B . 
P 6 HOH 184 584  716 HOH HOH B . 
P 6 HOH 185 585  902 HOH HOH B . 
P 6 HOH 186 586  861 HOH HOH B . 
P 6 HOH 187 587  890 HOH HOH B . 
P 6 HOH 188 588  856 HOH HOH B . 
P 6 HOH 189 589  660 HOH HOH B . 
P 6 HOH 190 590  733 HOH HOH B . 
P 6 HOH 191 591  548 HOH HOH B . 
P 6 HOH 192 592  551 HOH HOH B . 
P 6 HOH 193 593  704 HOH HOH B . 
P 6 HOH 194 594  868 HOH HOH B . 
P 6 HOH 195 595  857 HOH HOH B . 
P 6 HOH 196 596  812 HOH HOH B . 
P 6 HOH 197 597  846 HOH HOH B . 
P 6 HOH 198 598  816 HOH HOH B . 
P 6 HOH 199 599  470 HOH HOH B . 
P 6 HOH 200 600  715 HOH HOH B . 
P 6 HOH 201 601  552 HOH HOH B . 
P 6 HOH 202 602  600 HOH HOH B . 
P 6 HOH 203 603  586 HOH HOH B . 
P 6 HOH 204 604  527 HOH HOH B . 
P 6 HOH 205 605  775 HOH HOH B . 
P 6 HOH 206 606  633 HOH HOH B . 
P 6 HOH 207 607  650 HOH HOH B . 
P 6 HOH 208 608  849 HOH HOH B . 
P 6 HOH 209 609  21  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                   90.01 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  117.22 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QM8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     40.418 
_cell.length_a_esd                 ? 
_cell.length_b                     42.035 
_cell.length_b_esd                 ? 
_cell.length_c                     64.728 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         8QM8 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 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                   8QM8 
_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             1.95 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          37.07 
_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 
_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    
;10% PEG 3350
0.1M pH=8 Bicine/NaOH
;
_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 EIGER R 1M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2016-10-18 
_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                                       8QM8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.585 
_reflns.d_resolution_low                               64.73 
_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                                     36074 
_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                           70.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.3 
_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                                0.06 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.585 
_reflns_shell.d_res_low                                     1.59 
_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                             23 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.155 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.41950 
_refine.aniso_B[1][2]                            0.36290 
_refine.aniso_B[1][3]                            -0.25030 
_refine.aniso_B[2][2]                            0.17380 
_refine.aniso_B[2][3]                            -0.21780 
_refine.aniso_B[3][3]                            -0.59330 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               23.671 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.954 
_refine.correlation_coeff_Fo_to_Fc_free          0.942 
_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                                 8QM8 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.585 
_refine.ls_d_res_low                             64.73 
_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                     36072 
_refine.ls_number_reflns_R_free                  1828 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    70.1 
_refine.ls_percent_reflns_R_free                 5.070 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1669 
_refine.ls_R_factor_R_free                       0.2017 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1651 
_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   0.118 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.119 
_refine.pdbx_overall_SU_R_Blow_DPI               0.133 
_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             0.219 
_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                        8QM8 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.19 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.585 
_refine_hist.d_res_low                        64.73 
_refine_hist.number_atoms_solvent             401 
_refine_hist.number_atoms_total               3859 
_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        3344 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         114 
_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' ? 0.014 ? 6951  ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 1.10  ? 12459 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1545  ? 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' ? ?     ? 1099  ? t_gen_planes              16.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 6951  ? t_it                      10.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 6.10  ? ?     ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 14.87 ? ?     ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 432   ? 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' ? ?     ? 5883  ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.585 
_refine_ls_shell.d_res_low                        1.67 
_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             674 
_refine_ls_shell.percent_reflns_obs               9.84 
_refine_ls_shell.percent_reflns_R_free            6.65 
_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                  0.2697 
_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                  0.2753 
# 
_struct.entry_id                     8QM8 
_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        8QM8 
_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 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
K N N 5 ? 
L N N 2 ? 
M N N 2 ? 
N N N 4 ? 
O N N 6 ? 
P 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 8QM8 A 34 ? 215 ? P06730 36 ? 217 ? 36 217 
2 1 8QM8 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 8QM8 MET A 1  ? UNP P06730 ? ? 'initiating methionine' 3  1  
1 8QM8 HIS A 2  ? UNP P06730 ? ? 'expression tag'        4  2  
1 8QM8 HIS A 3  ? UNP P06730 ? ? 'expression tag'        5  3  
1 8QM8 HIS A 4  ? UNP P06730 ? ? 'expression tag'        6  4  
1 8QM8 HIS A 5  ? UNP P06730 ? ? 'expression tag'        7  5  
1 8QM8 HIS A 6  ? UNP P06730 ? ? 'expression tag'        8  6  
1 8QM8 HIS A 7  ? UNP P06730 ? ? 'expression tag'        9  7  
1 8QM8 GLY A 8  ? UNP P06730 ? ? 'expression tag'        10 8  
1 8QM8 ALA A 9  ? UNP P06730 ? ? 'expression tag'        11 9  
1 8QM8 ARG A 10 ? UNP P06730 ? ? 'expression tag'        12 10 
1 8QM8 ILE A 11 ? UNP P06730 ? ? 'expression tag'        13 11 
1 8QM8 ILE A 12 ? UNP P06730 ? ? 'expression tag'        14 12 
1 8QM8 TYR A 13 ? UNP P06730 ? ? 'expression tag'        15 13 
1 8QM8 ASP A 14 ? UNP P06730 ? ? 'expression tag'        16 14 
1 8QM8 ARG A 15 ? UNP P06730 ? ? 'expression tag'        17 15 
1 8QM8 ALA A 16 ? UNP P06730 ? ? 'expression tag'        18 16 
1 8QM8 PHE A 17 ? UNP P06730 ? ? 'expression tag'        19 17 
1 8QM8 LEU A 18 ? UNP P06730 ? ? 'expression tag'        20 18 
1 8QM8 MET A 19 ? UNP P06730 ? ? 'expression tag'        21 19 
1 8QM8 ALA A 20 ? UNP P06730 ? ? 'expression tag'        22 20 
1 8QM8 CYS A 21 ? UNP P06730 ? ? 'expression tag'        23 21 
1 8QM8 ARG A 22 ? UNP P06730 ? ? 'expression tag'        24 22 
1 8QM8 GLY A 23 ? UNP P06730 ? ? 'expression tag'        25 23 
1 8QM8 GLY A 24 ? UNP P06730 ? ? 'expression tag'        26 24 
1 8QM8 GLY A 25 ? UNP P06730 ? ? 'expression tag'        27 25 
1 8QM8 GLY A 26 ? UNP P06730 ? ? 'expression tag'        28 26 
1 8QM8 GLU A 27 ? UNP P06730 ? ? 'expression tag'        29 27 
1 8QM8 ASN A 28 ? UNP P06730 ? ? 'expression tag'        30 28 
1 8QM8 LEU A 29 ? UNP P06730 ? ? 'expression tag'        31 29 
1 8QM8 TYR A 30 ? UNP P06730 ? ? 'expression tag'        32 30 
1 8QM8 PHE A 31 ? UNP P06730 ? ? 'expression tag'        33 31 
1 8QM8 GLN A 32 ? UNP P06730 ? ? 'expression tag'        34 32 
1 8QM8 GLY A 33 ? UNP P06730 ? ? 'expression tag'        35 33 
2 8QM8 MET B 1  ? UNP P06730 ? ? 'initiating methionine' 3  34 
2 8QM8 HIS B 2  ? UNP P06730 ? ? 'expression tag'        4  35 
2 8QM8 HIS B 3  ? UNP P06730 ? ? 'expression tag'        5  36 
2 8QM8 HIS B 4  ? UNP P06730 ? ? 'expression tag'        6  37 
2 8QM8 HIS B 5  ? UNP P06730 ? ? 'expression tag'        7  38 
2 8QM8 HIS B 6  ? UNP P06730 ? ? 'expression tag'        8  39 
2 8QM8 HIS B 7  ? UNP P06730 ? ? 'expression tag'        9  40 
2 8QM8 GLY B 8  ? UNP P06730 ? ? 'expression tag'        10 41 
2 8QM8 ALA B 9  ? UNP P06730 ? ? 'expression tag'        11 42 
2 8QM8 ARG B 10 ? UNP P06730 ? ? 'expression tag'        12 43 
2 8QM8 ILE B 11 ? UNP P06730 ? ? 'expression tag'        13 44 
2 8QM8 ILE B 12 ? UNP P06730 ? ? 'expression tag'        14 45 
2 8QM8 TYR B 13 ? UNP P06730 ? ? 'expression tag'        15 46 
2 8QM8 ASP B 14 ? UNP P06730 ? ? 'expression tag'        16 47 
2 8QM8 ARG B 15 ? UNP P06730 ? ? 'expression tag'        17 48 
2 8QM8 ALA B 16 ? UNP P06730 ? ? 'expression tag'        18 49 
2 8QM8 PHE B 17 ? UNP P06730 ? ? 'expression tag'        19 50 
2 8QM8 LEU B 18 ? UNP P06730 ? ? 'expression tag'        20 51 
2 8QM8 MET B 19 ? UNP P06730 ? ? 'expression tag'        21 52 
2 8QM8 ALA B 20 ? UNP P06730 ? ? 'expression tag'        22 53 
2 8QM8 CYS B 21 ? UNP P06730 ? ? 'expression tag'        23 54 
2 8QM8 ARG B 22 ? UNP P06730 ? ? 'expression tag'        24 55 
2 8QM8 GLY B 23 ? UNP P06730 ? ? 'expression tag'        25 56 
2 8QM8 GLY B 24 ? UNP P06730 ? ? 'expression tag'        26 57 
2 8QM8 GLY B 25 ? UNP P06730 ? ? 'expression tag'        27 58 
2 8QM8 GLY B 26 ? UNP P06730 ? ? 'expression tag'        28 59 
2 8QM8 GLU B 27 ? UNP P06730 ? ? 'expression tag'        29 60 
2 8QM8 ASN B 28 ? UNP P06730 ? ? 'expression tag'        30 61 
2 8QM8 LEU B 29 ? UNP P06730 ? ? 'expression tag'        31 62 
2 8QM8 TYR B 30 ? UNP P06730 ? ? 'expression tag'        32 63 
2 8QM8 PHE B 31 ? UNP P06730 ? ? 'expression tag'        33 64 
2 8QM8 GLN B 32 ? UNP P06730 ? ? 'expression tag'        34 65 
2 8QM8 GLY B 33 ? UNP P06730 ? ? 'expression tag'        35 66 
# 
_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)' 3520  ? 
1 MORE         22    ? 
1 'SSA (A^2)'  21160 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 14  ? GLY A 25  ? ASP A 16  GLY A 27  1 ? 12 
HELX_P HELX_P2  AA2 TYR A 30  ? LYS A 34  ? TYR A 32  LYS A 36  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 80  ? VAL A 69  SER A 82  1 ? 14 
HELX_P HELX_P5  AA5 LYS A 117 ? ASP A 123 ? LYS A 119 ASP A 125 1 ? 7  
HELX_P HELX_P6  AA6 ASP A 123 ? GLY A 137 ? ASP A 125 GLY A 139 1 ? 15 
HELX_P HELX_P7  AA7 PHE A 140 ? ASP A 145 ? PHE A 142 ASP A 147 5 ? 6  
HELX_P HELX_P8  AA8 ASN A 170 ? GLY A 186 ? ASN A 172 GLY A 188 1 ? 17 
HELX_P HELX_P9  AA9 HIS A 198 ? ALA A 202 ? HIS A 200 ALA A 204 1 ? 5  
HELX_P HELX_P10 AB1 ASP B 14  ? GLY B 24  ? ASP B 16  GLY B 26  1 ? 11 
HELX_P HELX_P11 AB2 TYR B 30  ? LYS B 34  ? TYR B 32  LYS B 36  5 ? 5  
HELX_P HELX_P12 AB3 THR B 53  ? ASN B 57  ? THR B 55  ASN B 59  1 ? 5  
HELX_P HELX_P13 AB4 VAL B 67  ? SER B 80  ? VAL B 69  SER B 82  1 ? 14 
HELX_P HELX_P14 AB5 LYS B 117 ? ASP B 123 ? LYS B 119 ASP B 125 1 ? 7  
HELX_P HELX_P15 AB6 ASP B 123 ? GLY B 137 ? ASP B 125 GLY B 139 1 ? 15 
HELX_P HELX_P16 AB7 PHE B 140 ? ASP B 145 ? PHE B 142 ASP B 147 5 ? 6  
HELX_P HELX_P17 AB8 ASN B 170 ? GLY B 186 ? ASN B 172 GLY B 188 1 ? 17 
HELX_P HELX_P18 AB9 HIS B 198 ? ALA B 202 ? HIS B 200 ALA B 204 1 ? 5  
# 
_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  ? LYS A 47  ? PRO A 38  LYS A 49  
AA1 3 CYS A 87  ? LYS A 93  ? CYS A 89  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 ILE A 61  ? O ILE A 63  N LEU A 43  ? N LEU A 45  
AA1 2 3 N ALA A 42  ? N ALA A 44  O PHE A 92  ? O PHE A 94  
AA1 3 4 N TYR A 89  ? N TYR A 91  O VAL A 152 ? O VAL A 154 
AA1 4 5 N 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 ARG A 110 ? N ARG A 112 O GLN A 196 ? O GLN A 198 
AA1 7 8 N TYR A 195 ? N TYR A 197 O PHE A 213 ? O PHE A 215 
AA2 1 2 O ILE B 61  ? O ILE B 63  N LEU B 43  ? N LEU B 45  
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 ARG B 110 ? N ARG B 112 O GLN B 196 ? O GLN B 198 
AA2 7 8 N TYR B 195 ? N TYR B 197 O PHE B 213 ? O PHE B 215 
# 
_pdbx_entry_details.entry_id                   8QM8 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 67  ? ? -146.43 17.67   
2 1 SER A 83  ? ? 175.24  153.65  
3 1 ASP A 143 ? ? 49.54   -130.58 
4 1 ASP B 67  ? ? -145.69 17.81   
5 1 ASP B 143 ? ? 49.42   -130.88 
# 
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 -5.1248 -23.4358 3.2559   -0.0152 ? 0.0146 ? -0.0130 ? -0.0036 ? -0.0109 ? -0.0172 ? 0.4186 ? 
0.4072 ? 0.1829  ? 0.8022 ? -0.2746 ? 0.7436 ? 0.0168 ? -0.0348 ? 0.0204  ? -0.0270 ? -0.0129 ? 0.0824  ? 0.0110  ? -0.0131 ? 
-0.0038 ? 
2 'X-RAY DIFFRACTION' ? refined 8.5434  -16.2339 -29.2716 -0.0130 ? 0.0150 ? 0.0111  ? -0.0030 ? 0.0027  ? -0.0174 ? 0.3988 ? 
0.3995 ? -0.2602 ? 0.7583 ? 0.1922  ? 0.7312 ? 0.0067 ? -0.0375 ? -0.0287 ? -0.0264 ? -0.0102 ? -0.0855 ? -0.0078 ? 0.0094  ? 
0.0034  ? 
# 
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|10 - B|217 }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 3   ? A MET 1   
2  1 Y 1 A HIS 4   ? A HIS 2   
3  1 Y 1 A HIS 5   ? A HIS 3   
4  1 Y 1 A HIS 6   ? A HIS 4   
5  1 Y 1 A HIS 7   ? A HIS 5   
6  1 Y 1 A HIS 8   ? A HIS 6   
7  1 Y 1 A HIS 9   ? A HIS 7   
8  1 Y 1 A SER 207 ? A SER 205 
9  1 Y 1 A GLY 208 ? A GLY 206 
10 1 Y 1 A SER 209 ? A SER 207 
11 1 Y 1 A THR 210 ? A THR 208 
12 1 Y 1 B MET 3   ? B MET 1   
13 1 Y 1 B HIS 4   ? B HIS 2   
14 1 Y 1 B HIS 5   ? B HIS 3   
15 1 Y 1 B HIS 6   ? B HIS 4   
16 1 Y 1 B HIS 7   ? B HIS 5   
17 1 Y 1 B HIS 8   ? B HIS 6   
18 1 Y 1 B HIS 9   ? B HIS 7   
19 1 Y 1 B SER 207 ? B SER 205 
20 1 Y 1 B GLY 208 ? B GLY 206 
21 1 Y 1 B SER 209 ? B SER 207 
22 1 Y 1 B THR 210 ? B THR 208 
# 
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 
W4K C1   C N N 442 
W4K C2   C N N 443 
W4K C3   C N S 444 
W4K C5   C N R 445 
W4K C6   C N N 446 
W4K C7   C N N 447 
W4K C10  C Y N 448 
W4K C11  C Y N 449 
W4K C12  C Y N 450 
W4K C13  C Y N 451 
W4K C14  C Y N 452 
W4K C16  C N N 453 
W4K C19  C Y N 454 
W4K C21  C Y N 455 
W4K C22  C Y N 456 
W4K C23  C Y N 457 
W4K C24  C Y N 458 
W4K O4   O N N 459 
W4K O8   O N N 460 
W4K C9   C Y N 461 
W4K N15  N N N 462 
W4K C17  C N N 463 
W4K O18  O N N 464 
W4K C20  C Y N 465 
W4K F25  F N N 466 
W4K H30  H N N 467 
W4K H29  H N N 468 
W4K H28  H N N 469 
W4K H32  H N N 470 
W4K H31  H N N 471 
W4K H26  H N N 472 
W4K H27  H N N 473 
W4K H35  H N N 474 
W4K H34  H N N 475 
W4K H33  H N N 476 
W4K H37  H N N 477 
W4K H36  H N N 478 
W4K H39  H N N 479 
W4K H40  H N N 480 
W4K H41  H N N 481 
W4K H44  H N N 482 
W4K H43  H N N 483 
W4K H49  H N N 484 
W4K H50  H N N 485 
W4K H51  H N N 486 
W4K H38  H N N 487 
W4K H42  H N N 488 
W4K H46  H N N 489 
W4K H45  H N N 490 
W4K H47  H N N 491 
W4K 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 
W4K C22 C21  doub Y N 424 
W4K C22 C23  sing Y N 425 
W4K C21 C20  sing Y N 426 
W4K C23 C24  doub Y N 427 
W4K C20 C19  doub Y N 428 
W4K C1  C2   sing N N 429 
W4K C24 C19  sing Y N 430 
W4K C24 F25  sing N N 431 
W4K C19 C12  sing N N 432 
W4K C11 C12  doub Y N 433 
W4K C11 C10  sing Y N 434 
W4K C12 C13  sing Y N 435 
W4K C10 C9   doub Y N 436 
W4K C2  C3   sing N N 437 
W4K C13 C14  doub Y N 438 
W4K C9  C14  sing Y N 439 
W4K C9  C3   sing N N 440 
W4K C14 N15  sing N N 441 
W4K C3  O4   sing N N 442 
W4K N15 C16  sing N N 443 
W4K C16 C17  sing N N 444 
W4K O4  C5   sing N N 445 
W4K C17 O18  sing N N 446 
W4K C6  C5   sing N N 447 
W4K C5  C7   sing N N 448 
W4K O8  C7   sing N N 449 
W4K C1  H30  sing N N 450 
W4K C1  H29  sing N N 451 
W4K C1  H28  sing N N 452 
W4K C2  H32  sing N N 453 
W4K C2  H31  sing N N 454 
W4K C3  H26  sing N N 455 
W4K C5  H27  sing N N 456 
W4K C6  H35  sing N N 457 
W4K C6  H34  sing N N 458 
W4K C6  H33  sing N N 459 
W4K C7  H37  sing N N 460 
W4K C7  H36  sing N N 461 
W4K C10 H39  sing N N 462 
W4K C11 H40  sing N N 463 
W4K C13 H41  sing N N 464 
W4K C16 H44  sing N N 465 
W4K C16 H43  sing N N 466 
W4K C21 H49  sing N N 467 
W4K C22 H50  sing N N 468 
W4K C23 H51  sing N N 469 
W4K O8  H38  sing N N 470 
W4K N15 H42  sing N N 471 
W4K C17 H46  sing N N 472 
W4K C17 H45  sing N N 473 
W4K O18 H47  sing N N 474 
W4K 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                    8QM8 
_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]   0.024741 
_atom_sites.fract_transf_matrix[1][2]   0.012726 
_atom_sites.fract_transf_matrix[1][3]   0.000005 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.026752 
_atom_sites.fract_transf_matrix[2][3]   0.000002 
_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]   0.015449 
_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   ? 16.987  -14.845 -3.234  1.00 36.19 ? 10   GLY A N   1 
ATOM   2    C CA  . GLY A 1 8   ? 17.546  -14.493 -1.938  1.00 35.12 ? 10   GLY A CA  1 
ATOM   3    C C   . GLY A 1 8   ? 17.105  -15.471 -0.873  1.00 33.26 ? 10   GLY A C   1 
ATOM   4    O O   . GLY A 1 8   ? 16.927  -16.659 -1.159  1.00 34.04 ? 10   GLY A O   1 
ATOM   5    N N   . ALA A 1 9   ? 16.947  -14.991 0.344   1.00 30.87 ? 11   ALA A N   1 
ATOM   6    C CA  . ALA A 1 9   ? 16.399  -15.803 1.391   1.00 29.35 ? 11   ALA A CA  1 
ATOM   7    C C   . ALA A 1 9   ? 14.872  -15.928 1.152   1.00 25.88 ? 11   ALA A C   1 
ATOM   8    O O   . ALA A 1 9   ? 14.251  -15.195 0.341   1.00 26.04 ? 11   ALA A O   1 
ATOM   9    C CB  . ALA A 1 9   ? 16.718  -15.197 2.751   1.00 30.94 ? 11   ALA A CB  1 
ATOM   10   N N   . ARG A 1 10  ? 14.243  -16.890 1.854   1.00 21.14 ? 12   ARG A N   1 
ATOM   11   C CA  . ARG A 1 10  ? 12.795  -17.026 1.782   1.00 17.46 ? 12   ARG A CA  1 
ATOM   12   C C   . ARG A 1 10  ? 12.118  -15.728 2.154   1.00 16.27 ? 12   ARG A C   1 
ATOM   13   O O   . ARG A 1 10  ? 12.516  -15.088 3.132   1.00 16.74 ? 12   ARG A O   1 
ATOM   14   C CB  . ARG A 1 10  ? 12.354  -18.054 2.778   1.00 16.05 ? 12   ARG A CB  1 
ATOM   15   C CG  . ARG A 1 10  ? 10.892  -18.427 2.702   1.00 16.32 ? 12   ARG A CG  1 
ATOM   16   C CD  . ARG A 1 10  ? 10.589  -19.501 3.749   1.00 16.49 ? 12   ARG A CD  1 
ATOM   17   N NE  . ARG A 1 10  ? 11.446  -20.668 3.564   1.00 16.03 ? 12   ARG A NE  1 
ATOM   18   C CZ  . ARG A 1 10  ? 11.185  -21.691 2.750   1.00 16.97 ? 12   ARG A CZ  1 
ATOM   19   N NH1 . ARG A 1 10  ? 10.055  -21.729 2.058   1.00 15.09 ? 12   ARG A NH1 1 
ATOM   20   N NH2 . ARG A 1 10  ? 12.051  -22.688 2.630   1.00 16.69 ? 12   ARG A NH2 1 
ATOM   21   N N   . ILE A 1 11  ? 11.089  -15.380 1.411   1.00 14.00 ? 13   ILE A N   1 
ATOM   22   C CA  . ILE A 1 11  ? 10.346  -14.196 1.639   1.00 12.90 ? 13   ILE A CA  1 
ATOM   23   C C   . ILE A 1 11  ? 9.294   -14.555 2.668   1.00 13.61 ? 13   ILE A C   1 
ATOM   24   O O   . ILE A 1 11  ? 8.371   -15.349 2.373   1.00 14.21 ? 13   ILE A O   1 
ATOM   25   C CB  . ILE A 1 11  ? 9.690   -13.676 0.336   1.00 12.99 ? 13   ILE A CB  1 
ATOM   26   C CG1 . ILE A 1 11  ? 10.779  -13.275 -0.726  1.00 16.21 ? 13   ILE A CG1 1 
ATOM   27   C CG2 . ILE A 1 11  ? 8.885   -12.452 0.684   1.00 12.72 ? 13   ILE A CG2 1 
ATOM   28   C CD1 . ILE A 1 11  ? 10.258  -12.898 -2.064  1.00 17.29 ? 13   ILE A CD1 1 
ATOM   29   N N   . ILE A 1 12  ? 9.439   -14.025 3.888   1.00 13.00 ? 14   ILE A N   1 
ATOM   30   C CA  . ILE A 1 12  ? 8.517   -14.355 4.978   1.00 11.81 ? 14   ILE A CA  1 
ATOM   31   C C   . ILE A 1 12  ? 7.862   -13.048 5.382   1.00 12.78 ? 14   ILE A C   1 
ATOM   32   O O   . ILE A 1 12  ? 8.569   -12.024 5.606   1.00 14.30 ? 14   ILE A O   1 
ATOM   33   C CB  . ILE A 1 12  ? 9.262   -14.971 6.175   1.00 14.33 ? 14   ILE A CB  1 
ATOM   34   C CG1 . ILE A 1 12  ? 9.935   -16.313 5.765   1.00 16.01 ? 14   ILE A CG1 1 
ATOM   35   C CG2 . ILE A 1 12  ? 8.351   -15.083 7.452   1.00 15.99 ? 14   ILE A CG2 1 
ATOM   36   C CD1 . ILE A 1 12  ? 10.956  -16.804 6.720   1.00 19.11 ? 14   ILE A CD1 1 
ATOM   37   N N   . TYR A 1 13  ? 6.532   -13.054 5.530   1.00 11.19 ? 15   TYR A N   1 
ATOM   38   C CA  . TYR A 1 13  ? 5.828   -11.879 6.042   1.00 9.74  ? 15   TYR A CA  1 
ATOM   39   C C   . TYR A 1 13  ? 5.008   -12.296 7.258   1.00 11.18 ? 15   TYR A C   1 
ATOM   40   O O   . TYR A 1 13  ? 4.297   -13.311 7.186   1.00 11.62 ? 15   TYR A O   1 
ATOM   41   C CB  . TYR A 1 13  ? 4.872   -11.382 5.000   1.00 9.86  ? 15   TYR A CB  1 
ATOM   42   C CG  . TYR A 1 13  ? 5.490   -10.914 3.716   1.00 11.31 ? 15   TYR A CG  1 
ATOM   43   C CD1 . TYR A 1 13  ? 6.227   -9.735  3.665   1.00 12.00 ? 15   TYR A CD1 1 
ATOM   44   C CD2 . TYR A 1 13  ? 5.289   -11.610 2.525   1.00 11.58 ? 15   TYR A CD2 1 
ATOM   45   C CE1 . TYR A 1 13  ? 6.703   -9.241  2.465   1.00 12.35 ? 15   TYR A CE1 1 
ATOM   46   C CE2 . TYR A 1 13  ? 5.812   -11.149 1.319   1.00 11.83 ? 15   TYR A CE2 1 
ATOM   47   C CZ  . TYR A 1 13  ? 6.497   -9.947  1.291   1.00 12.53 ? 15   TYR A CZ  1 
ATOM   48   O OH  . TYR A 1 13  ? 6.997   -9.448  0.107   1.00 13.57 ? 15   TYR A OH  1 
ATOM   49   N N   . ASP A 1 14  ? 5.102   -11.558 8.347   1.00 11.93 ? 16   ASP A N   1 
ATOM   50   C CA  . ASP A 1 14  ? 4.260   -11.863 9.503   1.00 12.28 ? 16   ASP A CA  1 
ATOM   51   C C   . ASP A 1 14  ? 2.861   -11.289 9.351   1.00 12.51 ? 16   ASP A C   1 
ATOM   52   O O   . ASP A 1 14  ? 2.585   -10.573 8.400   1.00 13.95 ? 16   ASP A O   1 
ATOM   53   C CB  . ASP A 1 14  ? 4.946   -11.469 10.816  1.00 15.03 ? 16   ASP A CB  1 
ATOM   54   C CG  . ASP A 1 14  ? 5.089   -10.000 11.152  1.00 20.90 ? 16   ASP A CG  1 
ATOM   55   O OD1 . ASP A 1 14  ? 4.467   -9.156  10.473  1.00 17.06 ? 16   ASP A OD1 1 
ATOM   56   O OD2 . ASP A 1 14  ? 5.841   -9.679  12.130  1.00 22.78 ? 16   ASP A OD2 1 
ATOM   57   N N   . ARG A 1 15  ? 1.961   -11.645 10.269  1.00 13.11 ? 17   ARG A N   1 
ATOM   58   C CA  . ARG A 1 15  ? 0.565   -11.254 10.187  1.00 13.23 ? 17   ARG A CA  1 
ATOM   59   C C   . ARG A 1 15  ? 0.400   -9.752  10.124  1.00 13.64 ? 17   ARG A C   1 
ATOM   60   O O   . ARG A 1 15  ? -0.337  -9.247  9.271   1.00 13.08 ? 17   ARG A O   1 
ATOM   61   C CB  . ARG A 1 15  ? -0.205  -11.807 11.390  1.00 13.57 ? 17   ARG A CB  1 
ATOM   62   C CG  . ARG A 1 15  ? -1.675  -11.536 11.287  1.00 14.82 ? 17   ARG A CG  1 
ATOM   63   C CD  . ARG A 1 15  ? -2.324  -11.892 12.598  1.00 21.22 ? 17   ARG A CD  1 
ATOM   64   N NE  . ARG A 1 15  ? -3.768  -11.941 12.469  1.00 25.11 ? 17   ARG A NE  1 
ATOM   65   C CZ  . ARG A 1 15  ? -4.628  -10.940 12.663  1.00 32.33 ? 17   ARG A CZ  1 
ATOM   66   N NH1 . ARG A 1 15  ? -4.192  -9.723  12.995  1.00 29.19 ? 17   ARG A NH1 1 
ATOM   67   N NH2 . ARG A 1 15  ? -5.932  -11.143 12.518  1.00 35.19 ? 17   ARG A NH2 1 
ATOM   68   N N   . ALA A 1 16  ? 1.106   -9.021  11.014  1.00 14.38 ? 18   ALA A N   1 
ATOM   69   C CA  . ALA A 1 16  ? 0.946   -7.571  11.065  1.00 16.81 ? 18   ALA A CA  1 
ATOM   70   C C   . ALA A 1 16  ? 1.366   -6.913  9.764   1.00 15.48 ? 18   ALA A C   1 
ATOM   71   O O   . ALA A 1 16  ? 0.681   -5.993  9.306   1.00 14.78 ? 18   ALA A O   1 
ATOM   72   C CB  . ALA A 1 16  ? 1.731   -6.991  12.237  1.00 17.48 ? 18   ALA A CB  1 
ATOM   73   N N   . PHE A 1 17  ? 2.443   -7.389  9.156   1.00 13.48 ? 19   PHE A N   1 
ATOM   74   C CA  . PHE A 1 17  ? 2.934   -6.841  7.884   1.00 14.11 ? 19   PHE A CA  1 
ATOM   75   C C   . PHE A 1 17  ? 1.897   -7.063  6.791   1.00 13.48 ? 19   PHE A C   1 
ATOM   76   O O   . PHE A 1 17  ? 1.528   -6.147  6.056   1.00 14.13 ? 19   PHE A O   1 
ATOM   77   C CB  . PHE A 1 17  ? 4.286   -7.495  7.504   1.00 14.66 ? 19   PHE A CB  1 
ATOM   78   C CG  . PHE A 1 17  ? 4.989   -6.802  6.358   1.00 16.73 ? 19   PHE A CG  1 
ATOM   79   C CD1 . PHE A 1 17  ? 4.633   -7.058  5.044   1.00 17.81 ? 19   PHE A CD1 1 
ATOM   80   C CD2 . PHE A 1 17  ? 5.975   -5.878  6.595   1.00 19.78 ? 19   PHE A CD2 1 
ATOM   81   C CE1 . PHE A 1 17  ? 5.270   -6.403  3.996   1.00 19.55 ? 19   PHE A CE1 1 
ATOM   82   C CE2 . PHE A 1 17  ? 6.584   -5.220  5.562   1.00 20.42 ? 19   PHE A CE2 1 
ATOM   83   C CZ  . PHE A 1 17  ? 6.247   -5.506  4.254   1.00 19.59 ? 19   PHE A CZ  1 
ATOM   84   N N   . LEU A 1 18  ? 1.395   -8.313  6.694   1.00 12.22 ? 20   LEU A N   1 
ATOM   85   C CA  . LEU A 1 18  ? 0.365   -8.581  5.687   1.00 11.87 ? 20   LEU A CA  1 
ATOM   86   C C   . LEU A 1 18  ? -0.887  -7.727  5.881   1.00 12.61 ? 20   LEU A C   1 
ATOM   87   O O   . LEU A 1 18  ? -1.433  -7.213  4.922   1.00 13.06 ? 20   LEU A O   1 
ATOM   88   C CB  . LEU A 1 18  ? 0.019   -10.069 5.657   1.00 11.56 ? 20   LEU A CB  1 
ATOM   89   C CG  . LEU A 1 18  ? 1.194   -10.917 5.209   1.00 10.66 ? 20   LEU A CG  1 
ATOM   90   C CD1 . LEU A 1 18  ? 0.917   -12.397 5.402   1.00 10.20 ? 20   LEU A CD1 1 
ATOM   91   C CD2 . LEU A 1 18  ? 1.502   -10.658 3.698   1.00 10.81 ? 20   LEU A CD2 1 
ATOM   92   N N   . MET A 1 19  ? -1.316  -7.569  7.106   1.00 13.63 ? 21   MET A N   1 
ATOM   93   C CA  . MET A 1 19  ? -2.535  -6.797  7.431   1.00 15.63 ? 21   MET A CA  1 
ATOM   94   C C   . MET A 1 19  ? -2.369  -5.321  7.067   1.00 19.30 ? 21   MET A C   1 
ATOM   95   O O   . MET A 1 19  ? -3.321  -4.693  6.553   1.00 20.55 ? 21   MET A O   1 
ATOM   96   C CB  . MET A 1 19  ? -2.869  -6.956  8.933   1.00 17.27 ? 21   MET A CB  1 
ATOM   97   C CG  . MET A 1 19  ? -3.354  -8.349  9.297   1.00 17.96 ? 21   MET A CG  1 
ATOM   98   S SD  . MET A 1 19  ? -4.729  -9.041  8.349   1.00 21.08 ? 21   MET A SD  1 
ATOM   99   C CE  . MET A 1 19  ? -5.236  -10.242 9.436   1.00 31.65 ? 21   MET A CE  1 
ATOM   100  N N   . ALA A 1 20  ? -1.165  -4.781  7.321   1.00 19.09 ? 22   ALA A N   1 
ATOM   101  C CA  . ALA A 1 20  ? -0.781  -3.407  6.999   1.00 20.54 ? 22   ALA A CA  1 
ATOM   102  C C   . ALA A 1 20  ? -0.784  -3.179  5.498   1.00 20.91 ? 22   ALA A C   1 
ATOM   103  O O   . ALA A 1 20  ? -1.076  -2.070  5.080   1.00 21.77 ? 22   ALA A O   1 
ATOM   104  C CB  . ALA A 1 20  ? 0.586   -3.077  7.596   1.00 20.95 ? 22   ALA A CB  1 
ATOM   105  N N   . CYS A 1 21  ? -0.501  -4.204  4.664   1.00 18.85 ? 23   CYS A N   1 
ATOM   106  C CA  . CYS A 1 21  ? -0.543  -4.062  3.219   1.00 18.98 ? 23   CYS A CA  1 
ATOM   107  C C   . CYS A 1 21  ? -1.948  -3.966  2.630   1.00 18.72 ? 23   CYS A C   1 
ATOM   108  O O   . CYS A 1 21  ? -2.053  -3.661  1.453   1.00 19.89 ? 23   CYS A O   1 
ATOM   109  C CB  . CYS A 1 21  ? 0.229   -5.170  2.520   1.00 18.95 ? 23   CYS A CB  1 
ATOM   110  S SG  . CYS A 1 21  ? 1.996   -5.193  2.830   1.00 19.51 ? 23   CYS A SG  1 
ATOM   111  N N   . ARG A 1 22  ? -2.993  -4.239  3.379   1.00 18.25 ? 24   ARG A N   1 
ATOM   112  C CA  . ARG A 1 22  ? -4.334  -4.213  2.859   1.00 18.97 ? 24   ARG A CA  1 
ATOM   113  C C   . ARG A 1 22  ? -4.756  -2.766  2.613   1.00 23.41 ? 24   ARG A C   1 
ATOM   114  O O   . ARG A 1 22  ? -5.210  -2.456  1.531   1.00 23.60 ? 24   ARG A O   1 
ATOM   115  C CB  . ARG A 1 22  ? -5.316  -4.889  3.798   1.00 17.89 ? 24   ARG A CB  1 
ATOM   116  C CG  . ARG A 1 22  ? -6.639  -5.112  3.111   1.00 17.05 ? 24   ARG A CG  1 
ATOM   117  C CD  . ARG A 1 22  ? -7.620  -5.705  4.027   1.00 18.82 ? 24   ARG A CD  1 
ATOM   118  N NE  . ARG A 1 22  ? -8.845  -6.100  3.322   1.00 20.79 ? 24   ARG A NE  1 
ATOM   119  C CZ  . ARG A 1 22  ? -9.968  -6.455  3.912   1.00 25.15 ? 24   ARG A CZ  1 
ATOM   120  N NH1 . ARG A 1 22  ? -10.058 -6.456  5.235   1.00 27.53 ? 24   ARG A NH1 1 
ATOM   121  N NH2 . ARG A 1 22  ? -11.019 -6.818  3.185   1.00 26.84 ? 24   ARG A NH2 1 
ATOM   122  N N   . GLY A 1 23  ? -4.585  -1.939  3.620   1.00 26.34 ? 25   GLY A N   1 
ATOM   123  C CA  . GLY A 1 23  ? -4.935  -0.525  3.538   1.00 30.66 ? 25   GLY A CA  1 
ATOM   124  C C   . GLY A 1 23  ? -3.751  0.383   3.264   1.00 33.82 ? 25   GLY A C   1 
ATOM   125  O O   . GLY A 1 23  ? -3.958  1.539   2.887   1.00 35.55 ? 25   GLY A O   1 
ATOM   126  N N   . GLY A 1 24  ? -2.529  -0.125  3.457   1.00 34.35 ? 26   GLY A N   1 
ATOM   127  C CA  . GLY A 1 24  ? -1.293  0.607   3.213   1.00 35.17 ? 26   GLY A CA  1 
ATOM   128  C C   . GLY A 1 24  ? -0.310  -0.165  2.360   1.00 34.84 ? 26   GLY A C   1 
ATOM   129  O O   . GLY A 1 24  ? 0.890   -0.159  2.617   1.00 34.48 ? 26   GLY A O   1 
ATOM   130  N N   . GLY A 1 25  ? -0.813  -0.835  1.357   1.00 35.57 ? 27   GLY A N   1 
ATOM   131  C CA  . GLY A 1 25  ? 0.009   -1.623  0.451   1.00 36.23 ? 27   GLY A CA  1 
ATOM   132  C C   . GLY A 1 25  ? 0.436   -0.792  -0.729  1.00 36.49 ? 27   GLY A C   1 
ATOM   133  O O   . GLY A 1 25  ? 0.049   0.374   -0.883  1.00 37.33 ? 27   GLY A O   1 
ATOM   134  N N   . GLY A 1 26  ? 1.251   -1.396  -1.557  1.00 34.81 ? 28   GLY A N   1 
ATOM   135  C CA  . GLY A 1 26  ? 1.691   -0.774  -2.788  1.00 34.39 ? 28   GLY A CA  1 
ATOM   136  C C   . GLY A 1 26  ? 2.795   0.241   -2.576  1.00 33.94 ? 28   GLY A C   1 
ATOM   137  O O   . GLY A 1 26  ? 3.093   0.985   -3.505  1.00 36.42 ? 28   GLY A O   1 
ATOM   138  N N   . GLU A 1 27  ? 3.413   0.290   -1.378  1.00 31.95 ? 29   GLU A N   1 
ATOM   139  C CA  . GLU A 1 27  ? 4.513   1.225   -1.119  1.00 32.50 ? 29   GLU A CA  1 
ATOM   140  C C   . GLU A 1 27  ? 5.842   0.479   -0.908  1.00 32.19 ? 29   GLU A C   1 
ATOM   141  O O   . GLU A 1 27  ? 6.755   1.001   -0.260  1.00 32.12 ? 29   GLU A O   1 
ATOM   142  C CB  . GLU A 1 27  ? 4.163   2.104   0.099   1.00 36.18 ? 29   GLU A CB  1 
ATOM   143  C CG  . GLU A 1 27  ? 3.299   3.312   -0.245  1.00 43.56 ? 29   GLU A CG  1 
ATOM   144  C CD  . GLU A 1 27  ? 2.483   3.800   0.929   1.00 50.10 ? 29   GLU A CD  1 
ATOM   145  O OE1 . GLU A 1 27  ? 1.292   4.132   0.732   1.00 53.62 ? 29   GLU A OE1 1 
ATOM   146  O OE2 . GLU A 1 27  ? 3.032   3.846   2.050   1.00 53.61 ? 29   GLU A OE2 1 
ATOM   147  N N   . ASN A 1 28  ? 5.977   -0.751  -1.481  1.00 30.23 ? 30   ASN A N   1 
ATOM   148  C CA  . ASN A 1 28  ? 7.264   -1.434  -1.493  1.00 30.85 ? 30   ASN A CA  1 
ATOM   149  C C   . ASN A 1 28  ? 8.285   -0.609  -2.253  1.00 32.27 ? 30   ASN A C   1 
ATOM   150  O O   . ASN A 1 28  ? 7.939   0.191   -3.129  1.00 31.97 ? 30   ASN A O   1 
ATOM   151  C CB  . ASN A 1 28  ? 7.182   -2.806  -2.156  1.00 31.76 ? 30   ASN A CB  1 
ATOM   152  C CG  . ASN A 1 28  ? 8.326   -3.733  -1.805  1.00 33.71 ? 30   ASN A CG  1 
ATOM   153  O OD1 . ASN A 1 28  ? 9.039   -3.541  -0.830  1.00 36.01 ? 30   ASN A OD1 1 
ATOM   154  N ND2 . ASN A 1 28  ? 8.517   -4.769  -2.589  1.00 34.63 ? 30   ASN A ND2 1 
ATOM   155  N N   . LEU A 1 29  ? 9.531   -0.805  -1.902  1.00 33.26 ? 31   LEU A N   1 
ATOM   156  C CA  . LEU A 1 29  ? 10.650  -0.093  -2.496  1.00 34.07 ? 31   LEU A CA  1 
ATOM   157  C C   . LEU A 1 29  ? 11.035  -0.617  -3.903  1.00 34.70 ? 31   LEU A C   1 
ATOM   158  O O   . LEU A 1 29  ? 11.885  -0.014  -4.570  1.00 34.26 ? 31   LEU A O   1 
ATOM   159  C CB  . LEU A 1 29  ? 11.859  -0.182  -1.543  1.00 34.99 ? 31   LEU A CB  1 
ATOM   160  C CG  . LEU A 1 29  ? 11.690  0.337   -0.092  1.00 38.44 ? 31   LEU A CG  1 
ATOM   161  C CD1 . LEU A 1 29  ? 12.945  0.154   0.668   1.00 40.01 ? 31   LEU A CD1 1 
ATOM   162  C CD2 . LEU A 1 29  ? 11.393  1.843   -0.033  1.00 39.71 ? 31   LEU A CD2 1 
ATOM   163  N N   . TYR A 1 30  ? 10.421  -1.717  -4.366  1.00 34.47 ? 32   TYR A N   1 
ATOM   164  C CA  . TYR A 1 30  ? 10.583  -2.138  -5.754  1.00 34.55 ? 32   TYR A CA  1 
ATOM   165  C C   . TYR A 1 30  ? 9.284   -2.740  -6.276  1.00 33.19 ? 32   TYR A C   1 
ATOM   166  O O   . TYR A 1 30  ? 8.269   -2.681  -5.566  1.00 33.49 ? 32   TYR A O   1 
ATOM   167  C CB  . TYR A 1 30  ? 11.811  -3.056  -5.911  1.00 35.40 ? 32   TYR A CB  1 
ATOM   168  C CG  . TYR A 1 30  ? 11.647  -4.471  -5.396  1.00 36.98 ? 32   TYR A CG  1 
ATOM   169  C CD1 . TYR A 1 30  ? 11.563  -4.732  -4.037  1.00 37.98 ? 32   TYR A CD1 1 
ATOM   170  C CD2 . TYR A 1 30  ? 11.629  -5.550  -6.267  1.00 38.18 ? 32   TYR A CD2 1 
ATOM   171  C CE1 . TYR A 1 30  ? 11.447  -6.033  -3.556  1.00 39.25 ? 32   TYR A CE1 1 
ATOM   172  C CE2 . TYR A 1 30  ? 11.494  -6.853  -5.800  1.00 39.12 ? 32   TYR A CE2 1 
ATOM   173  C CZ  . TYR A 1 30  ? 11.407  -7.092  -4.443  1.00 40.15 ? 32   TYR A CZ  1 
ATOM   174  O OH  . TYR A 1 30  ? 11.316  -8.396  -4.000  1.00 41.60 ? 32   TYR A OH  1 
ATOM   175  N N   . PHE A 1 31  ? 9.281   -3.276  -7.511  1.00 31.04 ? 33   PHE A N   1 
ATOM   176  C CA  . PHE A 1 31  ? 8.110   -3.931  -8.090  1.00 30.11 ? 33   PHE A CA  1 
ATOM   177  C C   . PHE A 1 31  ? 6.969   -2.935  -8.296  1.00 30.75 ? 33   PHE A C   1 
ATOM   178  O O   . PHE A 1 31  ? 5.781   -3.297  -8.254  1.00 30.43 ? 33   PHE A O   1 
ATOM   179  C CB  . PHE A 1 31  ? 7.645   -5.125  -7.253  1.00 29.56 ? 33   PHE A CB  1 
ATOM   180  C CG  . PHE A 1 31  ? 6.958   -6.264  -8.016  1.00 30.52 ? 33   PHE A CG  1 
ATOM   181  C CD1 . PHE A 1 31  ? 6.302   -6.027  -9.226  1.00 30.95 ? 33   PHE A CD1 1 
ATOM   182  C CD2 . PHE A 1 31  ? 6.979   -7.563  -7.525  1.00 30.42 ? 33   PHE A CD2 1 
ATOM   183  C CE1 . PHE A 1 31  ? 5.673   -7.078  -9.922  1.00 31.20 ? 33   PHE A CE1 1 
ATOM   184  C CE2 . PHE A 1 31  ? 6.328   -8.612  -8.217  1.00 30.12 ? 33   PHE A CE2 1 
ATOM   185  C CZ  . PHE A 1 31  ? 5.702   -8.349  -9.415  1.00 31.19 ? 33   PHE A CZ  1 
ATOM   186  N N   . GLN A 1 32  ? 7.321   -1.654  -8.559  1.00 30.06 ? 34   GLN A N   1 
ATOM   187  C CA  . GLN A 1 32  ? 6.368   -0.561  -8.611  1.00 29.12 ? 34   GLN A CA  1 
ATOM   188  C C   . GLN A 1 32  ? 5.427   -0.553  -7.396  1.00 28.78 ? 34   GLN A C   1 
ATOM   189  O O   . GLN A 1 32  ? 4.255   -0.228  -7.520  1.00 31.19 ? 34   GLN A O   1 
ATOM   190  C CB  . GLN A 1 32  ? 5.635   -0.585  -9.970  1.00 29.37 ? 34   GLN A CB  1 
ATOM   191  C CG  . GLN A 1 32  ? 6.608   -0.437  -11.140 1.00 32.62 ? 34   GLN A CG  1 
ATOM   192  C CD  . GLN A 1 32  ? 5.931   -0.210  -12.468 1.00 33.97 ? 34   GLN A CD  1 
ATOM   193  O OE1 . GLN A 1 32  ? 4.708   -0.094  -12.564 1.00 33.82 ? 34   GLN A OE1 1 
ATOM   194  N NE2 . GLN A 1 32  ? 6.720   -0.133  -13.532 1.00 36.78 ? 34   GLN A NE2 1 
ATOM   195  N N   . GLY A 1 33  ? 5.985   -0.902  -6.243  1.00 26.69 ? 35   GLY A N   1 
ATOM   196  C CA  . GLY A 1 33  ? 5.298   -0.884  -4.959  1.00 24.86 ? 35   GLY A CA  1 
ATOM   197  C C   . GLY A 1 33  ? 4.733   -2.206  -4.468  1.00 24.57 ? 35   GLY A C   1 
ATOM   198  O O   . GLY A 1 33  ? 4.354   -2.283  -3.287  1.00 23.78 ? 35   GLY A O   1 
ATOM   199  N N   . LYS A 1 34  ? 4.653   -3.263  -5.333  1.00 22.18 ? 36   LYS A N   1 
ATOM   200  C CA  . LYS A 1 34  ? 4.081   -4.542  -4.861  1.00 20.21 ? 36   LYS A CA  1 
ATOM   201  C C   . LYS A 1 34  ? 5.109   -5.388  -4.097  1.00 19.26 ? 36   LYS A C   1 
ATOM   202  O O   . LYS A 1 34  ? 6.279   -5.382  -4.421  1.00 21.74 ? 36   LYS A O   1 
ATOM   203  C CB  . LYS A 1 34  ? 3.410   -5.321  -6.003  1.00 21.11 ? 36   LYS A CB  1 
ATOM   204  C CG  . LYS A 1 34  ? 2.124   -4.636  -6.494  1.00 26.47 ? 36   LYS A CG  1 
ATOM   205  C CD  . LYS A 1 34  ? 1.434   -5.430  -7.519  1.00 30.55 ? 36   LYS A CD  1 
ATOM   206  C CE  . LYS A 1 34  ? 0.403   -4.621  -8.260  1.00 36.26 ? 36   LYS A CE  1 
ATOM   207  N NZ  . LYS A 1 34  ? -0.562  -3.956  -7.346  1.00 42.48 ? 36   LYS A NZ  1 
ATOM   208  N N   . HIS A 1 35  ? 4.664   -6.121  -3.086  1.00 14.14 ? 37   HIS A N   1 
ATOM   209  C CA  . HIS A 1 35  ? 5.489   -6.966  -2.262  1.00 13.08 ? 37   HIS A CA  1 
ATOM   210  C C   . HIS A 1 35  ? 5.349   -8.389  -2.835  1.00 12.67 ? 37   HIS A C   1 
ATOM   211  O O   . HIS A 1 35  ? 4.266   -8.969  -2.719  1.00 11.39 ? 37   HIS A O   1 
ATOM   212  C CB  . HIS A 1 35  ? 4.994   -6.936  -0.792  1.00 12.92 ? 37   HIS A CB  1 
ATOM   213  C CG  . HIS A 1 35  ? 5.198   -5.613  -0.144  1.00 15.30 ? 37   HIS A CG  1 
ATOM   214  N ND1 . HIS A 1 35  ? 4.292   -4.604  -0.278  1.00 16.18 ? 37   HIS A ND1 1 
ATOM   215  C CD2 . HIS A 1 35  ? 6.220   -5.187  0.643   1.00 16.93 ? 37   HIS A CD2 1 
ATOM   216  C CE1 . HIS A 1 35  ? 4.775   -3.566  0.395   1.00 17.88 ? 37   HIS A CE1 1 
ATOM   217  N NE2 . HIS A 1 35  ? 5.937   -3.850  0.959   1.00 18.37 ? 37   HIS A NE2 1 
ATOM   218  N N   . PRO A 1 36  ? 6.385   -8.933  -3.461  1.00 13.06 ? 38   PRO A N   1 
ATOM   219  C CA  . PRO A 1 36  ? 6.256   -10.300 -4.002  1.00 11.89 ? 38   PRO A CA  1 
ATOM   220  C C   . PRO A 1 36  ? 6.196   -11.359 -2.939  1.00 11.86 ? 38   PRO A C   1 
ATOM   221  O O   . PRO A 1 36  ? 6.781   -11.219 -1.904  1.00 10.85 ? 38   PRO A O   1 
ATOM   222  C CB  . PRO A 1 36  ? 7.515   -10.458 -4.799  1.00 14.07 ? 38   PRO A CB  1 
ATOM   223  C CG  . PRO A 1 36  ? 8.492   -9.593  -4.120  1.00 16.59 ? 38   PRO A CG  1 
ATOM   224  C CD  . PRO A 1 36  ? 7.727   -8.396  -3.721  1.00 14.16 ? 38   PRO A CD  1 
ATOM   225  N N   . LEU A 1 37  ? 5.479   -12.422 -3.210  1.00 10.81 ? 39   LEU A N   1 
ATOM   226  C CA  . LEU A 1 37  ? 5.421   -13.570 -2.324  1.00 10.79 ? 39   LEU A CA  1 
ATOM   227  C C   . LEU A 1 37  ? 6.513   -14.541 -2.668  1.00 11.72 ? 39   LEU A C   1 
ATOM   228  O O   . LEU A 1 37  ? 7.072   -14.494 -3.769  1.00 12.91 ? 39   LEU A O   1 
ATOM   229  C CB  . LEU A 1 37  ? 4.070   -14.238 -2.503  1.00 9.74  ? 39   LEU A CB  1 
ATOM   230  C CG  . LEU A 1 37  ? 2.801   -13.426 -2.137  1.00 11.01 ? 39   LEU A CG  1 
ATOM   231  C CD1 . LEU A 1 37  ? 1.583   -14.232 -2.449  1.00 12.05 ? 39   LEU A CD1 1 
ATOM   232  C CD2 . LEU A 1 37  ? 2.809   -13.014 -0.666  1.00 9.24  ? 39   LEU A CD2 1 
ATOM   233  N N   . GLN A 1 38  ? 6.823   -15.433 -1.753  1.00 11.09 ? 40   GLN A N   1 
ATOM   234  C CA  . GLN A 1 38  ? 7.730   -16.539 -2.042  1.00 11.73 ? 40   GLN A CA  1 
ATOM   235  C C   . GLN A 1 38  ? 7.261   -17.420 -3.150  1.00 11.35 ? 40   GLN A C   1 
ATOM   236  O O   . GLN A 1 38  ? 8.062   -17.875 -3.981  1.00 11.01 ? 40   GLN A O   1 
ATOM   237  C CB  . GLN A 1 38  ? 7.976   -17.337 -0.795  1.00 10.90 ? 40   GLN A CB  1 
ATOM   238  C CG  . GLN A 1 38  ? 8.871   -18.532 -0.979  1.00 12.87 ? 40   GLN A CG  1 
ATOM   239  C CD  . GLN A 1 38  ? 10.276  -18.149 -1.288  1.00 14.89 ? 40   GLN A CD  1 
ATOM   240  O OE1 . GLN A 1 38  ? 10.737  -17.041 -0.988  1.00 15.74 ? 40   GLN A OE1 1 
ATOM   241  N NE2 . GLN A 1 38  ? 10.980  -19.044 -1.922  1.00 18.55 ? 40   GLN A NE2 1 
ATOM   242  N N   . ASN A 1 39  ? 5.968   -17.704 -3.140  1.00 10.34 ? 41   ASN A N   1 
ATOM   243  C CA  . ASN A 1 39  ? 5.315   -18.594 -4.072  1.00 9.29  ? 41   ASN A CA  1 
ATOM   244  C C   . ASN A 1 39  ? 4.190   -17.916 -4.776  1.00 9.40  ? 41   ASN A C   1 
ATOM   245  O O   . ASN A 1 39  ? 3.600   -16.984 -4.280  1.00 9.92  ? 41   ASN A O   1 
ATOM   246  C CB  . ASN A 1 39  ? 4.763   -19.837 -3.384  1.00 12.04 ? 41   ASN A CB  1 
ATOM   247  C CG  . ASN A 1 39  ? 5.841   -20.769 -3.016  1.00 14.21 ? 41   ASN A CG  1 
ATOM   248  O OD1 . ASN A 1 39  ? 6.418   -21.395 -3.888  1.00 18.18 ? 41   ASN A OD1 1 
ATOM   249  N ND2 . ASN A 1 39  ? 6.204   -20.865 -1.746  1.00 12.06 ? 41   ASN A ND2 1 
ATOM   250  N N   . ARG A 1 40  ? 3.893   -18.402 -5.980  1.00 10.18 ? 42   ARG A N   1 
ATOM   251  C CA  . ARG A 1 40  ? 2.682   -18.090 -6.687  1.00 9.68  ? 42   ARG A CA  1 
ATOM   252  C C   . ARG A 1 40  ? 1.590   -19.069 -6.267  1.00 10.67 ? 42   ARG A C   1 
ATOM   253  O O   . ARG A 1 40  ? 1.837   -20.279 -6.114  1.00 9.06  ? 42   ARG A O   1 
ATOM   254  C CB  . ARG A 1 40  ? 2.945   -18.204 -8.205  1.00 11.19 ? 42   ARG A CB  1 
ATOM   255  C CG  . ARG A 1 40  ? 1.812   -17.882 -9.165  1.00 12.64 ? 42   ARG A CG  1 
ATOM   256  C CD  . ARG A 1 40  ? 2.330   -17.900 -10.662 1.00 18.71 ? 42   ARG A CD  1 
ATOM   257  N NE  . ARG A 1 40  ? 3.338   -16.880 -10.700 1.00 18.89 ? 42   ARG A NE  1 
ATOM   258  C CZ  . ARG A 1 40  ? 4.659   -17.036 -10.819 1.00 17.87 ? 42   ARG A CZ  1 
ATOM   259  N NH1 . ARG A 1 40  ? 5.184   -18.233 -11.041 1.00 19.44 ? 42   ARG A NH1 1 
ATOM   260  N NH2 . ARG A 1 40  ? 5.452   -16.000 -10.727 1.00 16.01 ? 42   ARG A NH2 1 
ATOM   261  N N   . TRP A 1 41  ? 0.376   -18.524 -6.107  1.00 10.00 ? 43   TRP A N   1 
ATOM   262  C CA  . TRP A 1 41  ? -0.745  -19.296 -5.605  1.00 9.64  ? 43   TRP A CA  1 
ATOM   263  C C   . TRP A 1 41  ? -1.936  -19.225 -6.546  1.00 9.52  ? 43   TRP A C   1 
ATOM   264  O O   . TRP A 1 41  ? -2.145  -18.214 -7.193  1.00 9.70  ? 43   TRP A O   1 
ATOM   265  C CB  . TRP A 1 41  ? -1.151  -18.795 -4.228  1.00 9.19  ? 43   TRP A CB  1 
ATOM   266  C CG  . TRP A 1 41  ? -0.044  -18.874 -3.198  1.00 8.71  ? 43   TRP A CG  1 
ATOM   267  C CD1 . TRP A 1 41  ? 0.901   -17.932 -2.934  1.00 9.41  ? 43   TRP A CD1 1 
ATOM   268  C CD2 . TRP A 1 41  ? 0.164   -19.918 -2.237  1.00 8.53  ? 43   TRP A CD2 1 
ATOM   269  N NE1 . TRP A 1 41  ? 1.764   -18.386 -1.967  1.00 8.89  ? 43   TRP A NE1 1 
ATOM   270  C CE2 . TRP A 1 41  ? 1.319   -19.590 -1.501  1.00 9.18  ? 43   TRP A CE2 1 
ATOM   271  C CE3 . TRP A 1 41  ? -0.425  -21.150 -2.021  1.00 9.16  ? 43   TRP A CE3 1 
ATOM   272  C CZ2 . TRP A 1 41  ? 1.825   -20.431 -0.496  1.00 8.60  ? 43   TRP A CZ2 1 
ATOM   273  C CZ3 . TRP A 1 41  ? 0.035   -21.957 -1.023  1.00 9.94  ? 43   TRP A CZ3 1 
ATOM   274  C CH2 . TRP A 1 41  ? 1.171   -21.631 -0.300  1.00 8.53  ? 43   TRP A CH2 1 
ATOM   275  N N   . ALA A 1 42  ? -2.689  -20.310 -6.600  1.00 10.04 ? 44   ALA A N   1 
ATOM   276  C CA  . ALA A 1 42  ? -3.923  -20.426 -7.368  1.00 10.92 ? 44   ALA A CA  1 
ATOM   277  C C   . ALA A 1 42  ? -5.091  -20.715 -6.454  1.00 11.03 ? 44   ALA A C   1 
ATOM   278  O O   . ALA A 1 42  ? -5.067  -21.633 -5.601  1.00 10.77 ? 44   ALA A O   1 
ATOM   279  C CB  . ALA A 1 42  ? -3.810  -21.527 -8.390  1.00 11.05 ? 44   ALA A CB  1 
ATOM   280  N N   . LEU A 1 43  ? -6.136  -19.918 -6.618  1.00 10.18 ? 45   LEU A N   1 
ATOM   281  C CA  . LEU A 1 43  ? -7.412  -20.138 -5.956  1.00 11.18 ? 45   LEU A CA  1 
ATOM   282  C C   . LEU A 1 43  ? -8.412  -20.889 -6.846  1.00 11.98 ? 45   LEU A C   1 
ATOM   283  O O   . LEU A 1 43  ? -8.680  -20.477 -7.998  1.00 13.49 ? 45   LEU A O   1 
ATOM   284  C CB  . LEU A 1 43  ? -8.020  -18.787 -5.576  1.00 11.52 ? 45   LEU A CB  1 
ATOM   285  C CG  . LEU A 1 43  ? -9.410  -18.867 -4.874  1.00 13.13 ? 45   LEU A CG  1 
ATOM   286  C CD1 . LEU A 1 43  ? -9.315  -19.584 -3.497  1.00 12.22 ? 45   LEU A CD1 1 
ATOM   287  C CD2 . LEU A 1 43  ? -9.982  -17.482 -4.679  1.00 13.98 ? 45   LEU A CD2 1 
ATOM   288  N N   . TRP A 1 44  ? -8.938  -21.952 -6.311  1.00 11.93 ? 46   TRP A N   1 
ATOM   289  C CA  . TRP A 1 44  ? -9.877  -22.868 -6.971  1.00 13.07 ? 46   TRP A CA  1 
ATOM   290  C C   . TRP A 1 44  ? -11.196 -22.874 -6.210  1.00 13.43 ? 46   TRP A C   1 
ATOM   291  O O   . TRP A 1 44  ? -11.271 -22.726 -4.971  1.00 11.46 ? 46   TRP A O   1 
ATOM   292  C CB  . TRP A 1 44  ? -9.333  -24.309 -6.946  1.00 13.24 ? 46   TRP A CB  1 
ATOM   293  C CG  . TRP A 1 44  ? -7.980  -24.428 -7.564  1.00 14.88 ? 46   TRP A CG  1 
ATOM   294  C CD1 . TRP A 1 44  ? -6.762  -24.278 -6.939  1.00 15.90 ? 46   TRP A CD1 1 
ATOM   295  C CD2 . TRP A 1 44  ? -7.699  -24.827 -8.905  1.00 17.65 ? 46   TRP A CD2 1 
ATOM   296  N NE1 . TRP A 1 44  ? -5.745  -24.512 -7.823  1.00 16.41 ? 46   TRP A NE1 1 
ATOM   297  C CE2 . TRP A 1 44  ? -6.290  -24.877 -9.042  1.00 18.91 ? 46   TRP A CE2 1 
ATOM   298  C CE3 . TRP A 1 44  ? -8.505  -25.133 -10.017 1.00 21.19 ? 46   TRP A CE3 1 
ATOM   299  C CZ2 . TRP A 1 44  ? -5.670  -25.158 -10.248 1.00 22.77 ? 46   TRP A CZ2 1 
ATOM   300  C CZ3 . TRP A 1 44  ? -7.885  -25.420 -11.218 1.00 24.29 ? 46   TRP A CZ3 1 
ATOM   301  C CH2 . TRP A 1 44  ? -6.488  -25.465 -11.328 1.00 24.19 ? 46   TRP A CH2 1 
ATOM   302  N N   . PHE A 1 45  ? -12.266 -23.094 -6.970  1.00 13.79 ? 47   PHE A N   1 
ATOM   303  C CA  . PHE A 1 45  ? -13.587 -23.292 -6.416  1.00 14.76 ? 47   PHE A CA  1 
ATOM   304  C C   . PHE A 1 45  ? -14.130 -24.608 -6.911  1.00 16.17 ? 47   PHE A C   1 
ATOM   305  O O   . PHE A 1 45  ? -13.914 -24.990 -8.073  1.00 16.29 ? 47   PHE A O   1 
ATOM   306  C CB  . PHE A 1 45  ? -14.481 -22.141 -6.866  1.00 17.87 ? 47   PHE A CB  1 
ATOM   307  C CG  . PHE A 1 45  ? -15.928 -22.326 -6.563  1.00 20.64 ? 47   PHE A CG  1 
ATOM   308  C CD1 . PHE A 1 45  ? -16.415 -22.123 -5.289  1.00 22.64 ? 47   PHE A CD1 1 
ATOM   309  C CD2 . PHE A 1 45  ? -16.810 -22.708 -7.552  1.00 24.01 ? 47   PHE A CD2 1 
ATOM   310  C CE1 . PHE A 1 45  ? -17.757 -22.298 -5.008  1.00 24.72 ? 47   PHE A CE1 1 
ATOM   311  C CE2 . PHE A 1 45  ? -18.157 -22.890 -7.266  1.00 25.84 ? 47   PHE A CE2 1 
ATOM   312  C CZ  . PHE A 1 45  ? -18.621 -22.691 -5.998  1.00 24.93 ? 47   PHE A CZ  1 
ATOM   313  N N   . PHE A 1 46  ? -14.844 -25.279 -6.040  1.00 15.27 ? 48   PHE A N   1 
ATOM   314  C CA  . PHE A 1 46  ? -15.521 -26.534 -6.426  1.00 18.82 ? 48   PHE A CA  1 
ATOM   315  C C   . PHE A 1 46  ? -16.886 -26.579 -5.790  1.00 20.84 ? 48   PHE A C   1 
ATOM   316  O O   . PHE A 1 46  ? -17.055 -26.278 -4.620  1.00 18.52 ? 48   PHE A O   1 
ATOM   317  C CB  . PHE A 1 46  ? -14.727 -27.738 -5.999  1.00 21.58 ? 48   PHE A CB  1 
ATOM   318  C CG  . PHE A 1 46  ? -15.328 -29.046 -6.493  1.00 26.33 ? 48   PHE A CG  1 
ATOM   319  C CD1 . PHE A 1 46  ? -15.088 -29.497 -7.778  1.00 28.60 ? 48   PHE A CD1 1 
ATOM   320  C CD2 . PHE A 1 46  ? -16.159 -29.787 -5.683  1.00 29.53 ? 48   PHE A CD2 1 
ATOM   321  C CE1 . PHE A 1 46  ? -15.684 -30.673 -8.250  1.00 31.06 ? 48   PHE A CE1 1 
ATOM   322  C CE2 . PHE A 1 46  ? -16.734 -30.986 -6.142  1.00 31.19 ? 48   PHE A CE2 1 
ATOM   323  C CZ  . PHE A 1 46  ? -16.492 -31.418 -7.412  1.00 30.92 ? 48   PHE A CZ  1 
ATOM   324  N N   . LYS A 1 47  ? -17.897 -26.975 -6.593  1.00 23.34 ? 49   LYS A N   1 
ATOM   325  C CA  . LYS A 1 47  ? -19.176 -27.367 -5.996  1.00 27.56 ? 49   LYS A CA  1 
ATOM   326  C C   . LYS A 1 47  ? -19.679 -28.584 -6.728  1.00 34.36 ? 49   LYS A C   1 
ATOM   327  O O   . LYS A 1 47  ? -19.797 -28.536 -7.944  1.00 35.26 ? 49   LYS A O   1 
ATOM   328  C CB  . LYS A 1 47  ? -20.156 -26.208 -6.034  1.00 29.38 ? 49   LYS A CB  1 
ATOM   329  C CG  . LYS A 1 47  ? -21.390 -26.409 -5.181  1.00 34.45 ? 49   LYS A CG  1 
ATOM   330  C CD  . LYS A 1 47  ? -22.212 -25.123 -5.108  1.00 39.85 ? 49   LYS A CD  1 
ATOM   331  C CE  . LYS A 1 47  ? -23.651 -25.351 -4.698  1.00 43.92 ? 49   LYS A CE  1 
ATOM   332  N NZ  . LYS A 1 47  ? -23.756 -26.009 -3.370  1.00 47.41 ? 49   LYS A NZ  1 
ATOM   333  N N   . ASN A 1 48  ? -19.924 -29.673 -5.996  1.00 38.11 ? 50   ASN A N   1 
ATOM   334  C CA  . ASN A 1 48  ? -20.370 -30.933 -6.579  1.00 42.63 ? 50   ASN A CA  1 
ATOM   335  C C   . ASN A 1 48  ? -21.814 -30.736 -6.994  1.00 46.70 ? 50   ASN A C   1 
ATOM   336  O O   . ASN A 1 48  ? -22.714 -30.742 -6.150  1.00 47.90 ? 50   ASN A O   1 
ATOM   337  C CB  . ASN A 1 48  ? -20.211 -32.095 -5.559  1.00 45.16 ? 50   ASN A CB  1 
ATOM   338  C CG  . ASN A 1 48  ? -19.919 -33.454 -6.144  1.00 49.06 ? 50   ASN A CG  1 
ATOM   339  O OD1 . ASN A 1 48  ? -19.870 -33.657 -7.368  1.00 49.71 ? 50   ASN A OD1 1 
ATOM   340  N ND2 . ASN A 1 48  ? -19.724 -34.420 -5.256  1.00 50.29 ? 50   ASN A ND2 1 
ATOM   341  N N   . ASP A 1 49  ? -22.017 -30.536 -8.304  1.00 48.75 ? 51   ASP A N   1 
ATOM   342  C CA  . ASP A 1 49  ? -23.303 -30.386 -8.970  1.00 50.84 ? 51   ASP A CA  1 
ATOM   343  C C   . ASP A 1 49  ? -23.393 -31.510 -10.000 1.00 52.53 ? 51   ASP A C   1 
ATOM   344  O O   . ASP A 1 49  ? -22.702 -31.472 -11.031 1.00 52.60 ? 51   ASP A O   1 
ATOM   345  C CB  . ASP A 1 49  ? -23.350 -29.012 -9.663  1.00 53.53 ? 51   ASP A CB  1 
ATOM   346  C CG  . ASP A 1 49  ? -24.555 -28.756 -10.544 1.00 58.53 ? 51   ASP A CG  1 
ATOM   347  O OD1 . ASP A 1 49  ? -25.351 -29.684 -10.739 1.00 58.71 ? 51   ASP A OD1 1 
ATOM   348  O OD2 . ASP A 1 49  ? -24.695 -27.616 -11.041 1.00 61.90 ? 51   ASP A OD2 1 
ATOM   349  N N   . LYS A 1 50  ? -24.260 -32.507 -9.724  1.00 53.39 ? 52   LYS A N   1 
ATOM   350  C CA  . LYS A 1 50  ? -24.436 -33.704 -10.563 1.00 54.09 ? 52   LYS A CA  1 
ATOM   351  C C   . LYS A 1 50  ? -24.942 -33.390 -11.992 1.00 54.02 ? 52   LYS A C   1 
ATOM   352  O O   . LYS A 1 50  ? -24.806 -34.244 -12.864 1.00 54.49 ? 52   LYS A O   1 
ATOM   353  C CB  . LYS A 1 50  ? -25.395 -34.690 -9.861  1.00 57.01 ? 52   LYS A CB  1 
ATOM   354  C CG  . LYS A 1 50  ? -25.348 -36.124 -10.399 1.00 62.41 ? 52   LYS A CG  1 
ATOM   355  C CD  . LYS A 1 50  ? -26.626 -36.906 -10.050 1.00 66.87 ? 52   LYS A CD  1 
ATOM   356  C CE  . LYS A 1 50  ? -26.654 -38.277 -10.669 1.00 70.16 ? 52   LYS A CE  1 
ATOM   357  N NZ  . LYS A 1 50  ? -28.000 -38.906 -10.562 1.00 72.67 ? 52   LYS A NZ  1 
ATOM   358  N N   . SER A 1 51  ? -25.521 -32.196 -12.246 1.00 53.40 ? 53   SER A N   1 
ATOM   359  C CA  . SER A 1 51  ? -25.969 -31.831 -13.598 1.00 53.54 ? 53   SER A CA  1 
ATOM   360  C C   . SER A 1 51  ? -24.796 -31.531 -14.573 1.00 52.94 ? 53   SER A C   1 
ATOM   361  O O   . SER A 1 51  ? -24.971 -31.677 -15.788 1.00 53.99 ? 53   SER A O   1 
ATOM   362  C CB  . SER A 1 51  ? -26.912 -30.625 -13.556 1.00 55.31 ? 53   SER A CB  1 
ATOM   363  O OG  . SER A 1 51  ? -26.243 -29.372 -13.507 1.00 57.25 ? 53   SER A OG  1 
ATOM   364  N N   . LYS A 1 52  ? -23.629 -31.085 -14.048 1.00 50.48 ? 54   LYS A N   1 
ATOM   365  C CA  . LYS A 1 52  ? -22.431 -30.820 -14.848 1.00 48.34 ? 54   LYS A CA  1 
ATOM   366  C C   . LYS A 1 52  ? -21.362 -31.909 -14.589 1.00 45.59 ? 54   LYS A C   1 
ATOM   367  O O   . LYS A 1 52  ? -21.457 -32.670 -13.627 1.00 43.87 ? 54   LYS A O   1 
ATOM   368  C CB  . LYS A 1 52  ? -21.839 -29.442 -14.493 1.00 50.24 ? 54   LYS A CB  1 
ATOM   369  C CG  . LYS A 1 52  ? -22.798 -28.286 -14.586 1.00 53.50 ? 54   LYS A CG  1 
ATOM   370  C CD  . LYS A 1 52  ? -22.106 -27.022 -14.125 1.00 57.12 ? 54   LYS A CD  1 
ATOM   371  C CE  . LYS A 1 52  ? -22.986 -25.796 -14.234 1.00 59.97 ? 54   LYS A CE  1 
ATOM   372  N NZ  . LYS A 1 52  ? -22.191 -24.528 -14.130 1.00 61.20 ? 54   LYS A NZ  1 
ATOM   373  N N   . THR A 1 53  ? -20.348 -31.972 -15.461 1.00 44.85 ? 55   THR A N   1 
ATOM   374  C CA  . THR A 1 53  ? -19.213 -32.869 -15.270 1.00 44.96 ? 55   THR A CA  1 
ATOM   375  C C   . THR A 1 53  ? -18.399 -32.398 -14.057 1.00 44.73 ? 55   THR A C   1 
ATOM   376  O O   . THR A 1 53  ? -18.510 -31.237 -13.642 1.00 44.71 ? 55   THR A O   1 
ATOM   377  C CB  . THR A 1 53  ? -18.294 -32.835 -16.518 1.00 46.75 ? 55   THR A CB  1 
ATOM   378  O OG1 . THR A 1 53  ? -17.871 -31.484 -16.762 1.00 48.65 ? 55   THR A OG1 1 
ATOM   379  C CG2 . THR A 1 53  ? -18.964 -33.391 -17.747 1.00 46.32 ? 55   THR A CG2 1 
ATOM   380  N N   . TRP A 1 54  ? -17.570 -33.296 -13.498 1.00 44.18 ? 56   TRP A N   1 
ATOM   381  C CA  . TRP A 1 54  ? -16.603 -32.951 -12.463 1.00 43.71 ? 56   TRP A CA  1 
ATOM   382  C C   . TRP A 1 54  ? -15.672 -31.816 -12.948 1.00 42.80 ? 56   TRP A C   1 
ATOM   383  O O   . TRP A 1 54  ? -15.371 -30.883 -12.185 1.00 42.77 ? 56   TRP A O   1 
ATOM   384  C CB  . TRP A 1 54  ? -15.777 -34.198 -12.078 1.00 44.45 ? 56   TRP A CB  1 
ATOM   385  C CG  . TRP A 1 54  ? -14.686 -33.909 -11.091 1.00 45.76 ? 56   TRP A CG  1 
ATOM   386  C CD1 . TRP A 1 54  ? -14.739 -34.061 -9.739  1.00 47.12 ? 56   TRP A CD1 1 
ATOM   387  C CD2 . TRP A 1 54  ? -13.385 -33.404 -11.390 1.00 46.56 ? 56   TRP A CD2 1 
ATOM   388  N NE1 . TRP A 1 54  ? -13.545 -33.673 -9.174  1.00 47.81 ? 56   TRP A NE1 1 
ATOM   389  C CE2 . TRP A 1 54  ? -12.701 -33.254 -10.168 1.00 47.77 ? 56   TRP A CE2 1 
ATOM   390  C CE3 . TRP A 1 54  ? -12.726 -33.070 -12.574 1.00 47.68 ? 56   TRP A CE3 1 
ATOM   391  C CZ2 . TRP A 1 54  ? -11.407 -32.755 -10.101 1.00 48.78 ? 56   TRP A CZ2 1 
ATOM   392  C CZ3 . TRP A 1 54  ? -11.454 -32.557 -12.506 1.00 49.13 ? 56   TRP A CZ3 1 
ATOM   393  C CH2 . TRP A 1 54  ? -10.798 -32.422 -11.286 1.00 49.18 ? 56   TRP A CH2 1 
ATOM   394  N N   . GLN A 1 55  ? -15.252 -31.902 -14.227 1.00 41.55 ? 57   GLN A N   1 
ATOM   395  C CA  . GLN A 1 55  ? -14.309 -30.988 -14.877 1.00 41.34 ? 57   GLN A CA  1 
ATOM   396  C C   . GLN A 1 55  ? -14.863 -29.574 -14.825 1.00 39.87 ? 57   GLN A C   1 
ATOM   397  O O   . GLN A 1 55  ? -14.129 -28.645 -14.483 1.00 39.79 ? 57   GLN A O   1 
ATOM   398  C CB  . GLN A 1 55  ? -14.090 -31.417 -16.364 1.00 44.21 ? 57   GLN A CB  1 
ATOM   399  C CG  . GLN A 1 55  ? -12.681 -31.222 -16.920 1.00 50.38 ? 57   GLN A CG  1 
ATOM   400  C CD  . GLN A 1 55  ? -12.494 -32.132 -18.118 1.00 57.36 ? 57   GLN A CD  1 
ATOM   401  O OE1 . GLN A 1 55  ? -11.756 -33.118 -18.074 1.00 58.50 ? 57   GLN A OE1 1 
ATOM   402  N NE2 . GLN A 1 55  ? -13.172 -31.830 -19.216 1.00 59.68 ? 57   GLN A NE2 1 
ATOM   403  N N   . ALA A 1 56  ? -16.151 -29.413 -15.167 1.00 38.73 ? 58   ALA A N   1 
ATOM   404  C CA  . ALA A 1 56  ? -16.825 -28.109 -15.169 1.00 38.18 ? 58   ALA A CA  1 
ATOM   405  C C   . ALA A 1 56  ? -17.238 -27.645 -13.763 1.00 35.26 ? 58   ALA A C   1 
ATOM   406  O O   . ALA A 1 56  ? -17.546 -26.457 -13.588 1.00 35.37 ? 58   ALA A O   1 
ATOM   407  C CB  . ALA A 1 56  ? -18.051 -28.170 -16.042 1.00 39.89 ? 58   ALA A CB  1 
ATOM   408  N N   . ASN A 1 57  ? -17.266 -28.555 -12.784 1.00 32.44 ? 59   ASN A N   1 
ATOM   409  C CA  . ASN A 1 57  ? -17.490 -28.176 -11.387 1.00 32.32 ? 59   ASN A CA  1 
ATOM   410  C C   . ASN A 1 57  ? -16.215 -27.578 -10.738 1.00 31.48 ? 59   ASN A C   1 
ATOM   411  O O   . ASN A 1 57  ? -16.401 -26.756 -9.845  1.00 31.93 ? 59   ASN A O   1 
ATOM   412  C CB  . ASN A 1 57  ? -17.979 -29.347 -10.528 1.00 33.29 ? 59   ASN A CB  1 
ATOM   413  C CG  . ASN A 1 57  ? -19.401 -29.779 -10.854 1.00 38.11 ? 59   ASN A CG  1 
ATOM   414  O OD1 . ASN A 1 57  ? -20.294 -28.958 -11.051 1.00 38.57 ? 59   ASN A OD1 1 
ATOM   415  N ND2 . ASN A 1 57  ? -19.642 -31.055 -10.910 1.00 39.78 ? 59   ASN A ND2 1 
ATOM   416  N N   . LEU A 1 58  ? -14.964 -27.995 -11.146 1.00 30.02 ? 60   LEU A N   1 
ATOM   417  C CA  . LEU A 1 58  ? -13.701 -27.392 -10.626 1.00 28.74 ? 60   LEU A CA  1 
ATOM   418  C C   . LEU A 1 58  ? -13.347 -26.185 -11.461 1.00 27.74 ? 60   LEU A C   1 
ATOM   419  O O   . LEU A 1 58  ? -13.221 -26.295 -12.689 1.00 29.17 ? 60   LEU A O   1 
ATOM   420  C CB  . LEU A 1 58  ? -12.543 -28.378 -10.664 1.00 28.72 ? 60   LEU A CB  1 
ATOM   421  C CG  . LEU A 1 58  ? -11.205 -27.875 -10.039 1.00 31.30 ? 60   LEU A CG  1 
ATOM   422  C CD1 . LEU A 1 58  ? -11.321 -27.770 -8.508  1.00 29.82 ? 60   LEU A CD1 1 
ATOM   423  C CD2 . LEU A 1 58  ? -10.055 -28.816 -10.351 1.00 33.51 ? 60   LEU A CD2 1 
ATOM   424  N N   . ARG A 1 59  ? -13.189 -25.022 -10.825 1.00 24.73 ? 61   ARG A N   1 
ATOM   425  C CA  . ARG A 1 59  ? -12.893 -23.800 -11.526 1.00 24.28 ? 61   ARG A CA  1 
ATOM   426  C C   . ARG A 1 59  ? -11.669 -23.160 -10.925 1.00 21.37 ? 61   ARG A C   1 
ATOM   427  O O   . ARG A 1 59  ? -11.623 -23.006 -9.698  1.00 20.50 ? 61   ARG A O   1 
ATOM   428  C CB  . ARG A 1 59  ? -14.045 -22.793 -11.425 1.00 28.60 ? 61   ARG A CB  1 
ATOM   429  C CG  . ARG A 1 59  ? -15.220 -23.209 -12.300 1.00 37.28 ? 61   ARG A CG  1 
ATOM   430  C CD  . ARG A 1 59  ? -16.577 -22.722 -11.835 1.00 44.34 ? 61   ARG A CD  1 
ATOM   431  N NE  . ARG A 1 59  ? -16.853 -21.337 -12.217 1.00 50.95 ? 61   ARG A NE  1 
ATOM   432  C CZ  . ARG A 1 59  ? -18.077 -20.818 -12.360 1.00 57.86 ? 61   ARG A CZ  1 
ATOM   433  N NH1 . ARG A 1 59  ? -18.229 -19.546 -12.711 1.00 59.29 ? 61   ARG A NH1 1 
ATOM   434  N NH2 . ARG A 1 59  ? -19.162 -21.570 -12.158 1.00 59.26 ? 61   ARG A NH2 1 
ATOM   435  N N   . LEU A 1 60  ? -10.695 -22.809 -11.772 1.00 20.91 ? 62   LEU A N   1 
ATOM   436  C CA  . LEU A 1 60  ? -9.583  -21.912 -11.395 1.00 22.09 ? 62   LEU A CA  1 
ATOM   437  C C   . LEU A 1 60  ? -10.144 -20.518 -11.365 1.00 22.76 ? 62   LEU A C   1 
ATOM   438  O O   . LEU A 1 60  ? -10.634 -20.021 -12.402 1.00 23.10 ? 62   LEU A O   1 
ATOM   439  C CB  . LEU A 1 60  ? -8.470  -21.967 -12.468 1.00 23.65 ? 62   LEU A CB  1 
ATOM   440  C CG  . LEU A 1 60  ? -7.314  -20.909 -12.317 1.00 25.98 ? 62   LEU A CG  1 
ATOM   441  C CD1 . LEU A 1 60  ? -6.640  -21.103 -11.005 1.00 24.09 ? 62   LEU A CD1 1 
ATOM   442  C CD2 . LEU A 1 60  ? -6.357  -21.027 -13.455 1.00 28.12 ? 62   LEU A CD2 1 
ATOM   443  N N   . ILE A 1 61  ? -10.123 -19.860 -10.216 1.00 19.59 ? 63   ILE A N   1 
ATOM   444  C CA  . ILE A 1 61  ? -10.639 -18.511 -10.087 1.00 20.26 ? 63   ILE A CA  1 
ATOM   445  C C   . ILE A 1 61  ? -9.587  -17.509 -10.495 1.00 20.14 ? 63   ILE A C   1 
ATOM   446  O O   . ILE A 1 61  ? -9.852  -16.597 -11.287 1.00 21.48 ? 63   ILE A O   1 
ATOM   447  C CB  . ILE A 1 61  ? -11.164 -18.218 -8.644  1.00 21.33 ? 63   ILE A CB  1 
ATOM   448  C CG1 . ILE A 1 61  ? -12.313 -19.179 -8.224  1.00 24.47 ? 63   ILE A CG1 1 
ATOM   449  C CG2 . ILE A 1 61  ? -11.618 -16.769 -8.517  1.00 23.10 ? 63   ILE A CG2 1 
ATOM   450  C CD1 . ILE A 1 61  ? -13.405 -19.406 -9.302  1.00 28.62 ? 63   ILE A CD1 1 
ATOM   451  N N   . SER A 1 62  ? -8.353  -17.646 -9.929  1.00 16.06 ? 64   SER A N   1 
ATOM   452  C CA  . SER A 1 62  ? -7.382  -16.613 -10.098 1.00 17.46 ? 64   SER A CA  1 
ATOM   453  C C   . SER A 1 62  ? -6.046  -17.090 -9.565  1.00 16.08 ? 64   SER A C   1 
ATOM   454  O O   . SER A 1 62  ? -6.011  -18.002 -8.749  1.00 14.80 ? 64   SER A O   1 
ATOM   455  C CB  . SER A 1 62  ? -7.828  -15.329 -9.385  1.00 23.21 ? 64   SER A CB  1 
ATOM   456  O OG  . SER A 1 62  ? -6.973  -14.261 -9.738  1.00 31.93 ? 64   SER A OG  1 
ATOM   457  N N   . LYS A 1 63  ? -4.989  -16.496 -10.049 1.00 15.17 ? 65   LYS A N   1 
ATOM   458  C CA  . LYS A 1 63  ? -3.652  -16.740 -9.560  1.00 12.97 ? 65   LYS A CA  1 
ATOM   459  C C   . LYS A 1 63  ? -3.023  -15.402 -9.148  1.00 13.51 ? 65   LYS A C   1 
ATOM   460  O O   . LYS A 1 63  ? -3.266  -14.383 -9.789  1.00 15.60 ? 65   LYS A O   1 
ATOM   461  C CB  . LYS A 1 63  ? -2.767  -17.421 -10.594 1.00 11.49 ? 65   LYS A CB  1 
ATOM   462  C CG  . LYS A 1 63  ? -3.224  -18.781 -11.040 1.00 14.83 ? 65   LYS A CG  1 
ATOM   463  C CD  . LYS A 1 63  ? -2.148  -19.536 -11.838 1.00 17.46 ? 65   LYS A CD  1 
ATOM   464  C CE  . LYS A 1 63  ? -2.730  -20.727 -12.564 1.00 20.38 ? 65   LYS A CE  1 
ATOM   465  N NZ  . LYS A 1 63  ? -1.704  -21.670 -13.039 1.00 26.63 ? 65   LYS A NZ  1 
ATOM   466  N N   . PHE A 1 64  ? -2.193  -15.425 -8.125  1.00 10.89 ? 66   PHE A N   1 
ATOM   467  C CA  . PHE A 1 64  ? -1.535  -14.217 -7.655  1.00 9.83  ? 66   PHE A CA  1 
ATOM   468  C C   . PHE A 1 64  ? -0.195  -14.527 -7.082  1.00 10.15 ? 66   PHE A C   1 
ATOM   469  O O   . PHE A 1 64  ? 0.054   -15.664 -6.695  1.00 11.02 ? 66   PHE A O   1 
ATOM   470  C CB  . PHE A 1 64  ? -2.382  -13.423 -6.627  1.00 11.49 ? 66   PHE A CB  1 
ATOM   471  C CG  . PHE A 1 64  ? -2.676  -14.244 -5.406  1.00 11.33 ? 66   PHE A CG  1 
ATOM   472  C CD1 . PHE A 1 64  ? -1.807  -14.246 -4.323  1.00 9.49  ? 66   PHE A CD1 1 
ATOM   473  C CD2 . PHE A 1 64  ? -3.805  -15.022 -5.341  1.00 13.43 ? 66   PHE A CD2 1 
ATOM   474  C CE1 . PHE A 1 64  ? -2.057  -15.038 -3.221  1.00 11.33 ? 66   PHE A CE1 1 
ATOM   475  C CE2 . PHE A 1 64  ? -4.042  -15.830 -4.244  1.00 13.47 ? 66   PHE A CE2 1 
ATOM   476  C CZ  . PHE A 1 64  ? -3.163  -15.821 -3.177  1.00 12.28 ? 66   PHE A CZ  1 
ATOM   477  N N   . ASP A 1 65  ? 0.667   -13.519 -7.037  1.00 9.45  ? 67   ASP A N   1 
ATOM   478  C CA  . ASP A 1 65  ? 2.015   -13.720 -6.505  1.00 10.37 ? 67   ASP A CA  1 
ATOM   479  C C   . ASP A 1 65  ? 2.581   -12.493 -5.772  1.00 9.81  ? 67   ASP A C   1 
ATOM   480  O O   . ASP A 1 65  ? 3.790   -12.430 -5.541  1.00 11.31 ? 67   ASP A O   1 
ATOM   481  C CB  . ASP A 1 65  ? 2.940   -14.219 -7.611  1.00 11.59 ? 67   ASP A CB  1 
ATOM   482  C CG  . ASP A 1 65  ? 3.253   -13.221 -8.714  1.00 15.80 ? 67   ASP A CG  1 
ATOM   483  O OD1 . ASP A 1 65  ? 2.787   -12.104 -8.627  1.00 14.49 ? 67   ASP A OD1 1 
ATOM   484  O OD2 . ASP A 1 65  ? 3.965   -13.599 -9.701  1.00 16.74 ? 67   ASP A OD2 1 
ATOM   485  N N   . THR A 1 66  ? 1.692   -11.535 -5.373  1.00 9.64  ? 68   THR A N   1 
ATOM   486  C CA  . THR A 1 66  ? 2.051   -10.444 -4.525  1.00 10.09 ? 68   THR A CA  1 
ATOM   487  C C   . THR A 1 66  ? 1.043   -10.301 -3.372  1.00 10.21 ? 68   THR A C   1 
ATOM   488  O O   . THR A 1 66  ? -0.116  -10.711 -3.461  1.00 9.76  ? 68   THR A O   1 
ATOM   489  C CB  . THR A 1 66  ? 2.148   -9.110  -5.302  1.00 10.51 ? 68   THR A CB  1 
ATOM   490  O OG1 . THR A 1 66  ? 0.875   -8.652  -5.652  1.00 11.18 ? 68   THR A OG1 1 
ATOM   491  C CG2 . THR A 1 66  ? 3.084   -9.186  -6.562  1.00 12.09 ? 68   THR A CG2 1 
ATOM   492  N N   . VAL A 1 67  ? 1.473   -9.651  -2.314  1.00 9.70  ? 69   VAL A N   1 
ATOM   493  C CA  . VAL A 1 67  ? 0.595   -9.330  -1.177  1.00 10.63 ? 69   VAL A CA  1 
ATOM   494  C C   . VAL A 1 67  ? -0.572  -8.476  -1.649  1.00 11.65 ? 69   VAL A C   1 
ATOM   495  O O   . VAL A 1 67  ? -1.720  -8.703  -1.264  1.00 11.78 ? 69   VAL A O   1 
ATOM   496  C CB  . VAL A 1 67  ? 1.370   -8.589  -0.077  1.00 12.72 ? 69   VAL A CB  1 
ATOM   497  C CG1 . VAL A 1 67  ? 0.417   -8.227  1.072   1.00 15.95 ? 69   VAL A CG1 1 
ATOM   498  C CG2 . VAL A 1 67  ? 2.510   -9.429  0.465   1.00 12.30 ? 69   VAL A CG2 1 
ATOM   499  N N   . GLU A 1 68  ? -0.270  -7.443  -2.516  1.00 11.19 ? 70   GLU A N   1 
ATOM   500  C CA  . GLU A 1 68  ? -1.325  -6.520  -2.914  1.00 13.62 ? 70   GLU A CA  1 
ATOM   501  C C   . GLU A 1 68  ? -2.346  -7.229  -3.768  1.00 13.41 ? 70   GLU A C   1 
ATOM   502  O O   . GLU A 1 68  ? -3.540  -6.951  -3.667  1.00 11.91 ? 70   GLU A O   1 
ATOM   503  C CB  . GLU A 1 68  ? -0.739  -5.293  -3.628  1.00 15.27 ? 70   GLU A CB  1 
ATOM   504  C CG  . GLU A 1 68  ? 0.068   -4.411  -2.728  1.00 16.12 ? 70   GLU A CG  1 
ATOM   505  C CD  . GLU A 1 68  ? 1.416   -4.853  -2.223  1.00 16.85 ? 70   GLU A CD  1 
ATOM   506  O OE1 . GLU A 1 68  ? 1.943   -5.897  -2.675  1.00 13.70 ? 70   GLU A OE1 1 
ATOM   507  O OE2 . GLU A 1 68  ? 1.960   -4.132  -1.360  1.00 18.71 ? 70   GLU A OE2 1 
ATOM   508  N N   . ASP A 1 69  ? -1.891  -8.159  -4.656  1.00 12.49 ? 71   ASP A N   1 
ATOM   509  C CA  . ASP A 1 69  ? -2.828  -8.899  -5.513  1.00 11.00 ? 71   ASP A CA  1 
ATOM   510  C C   . ASP A 1 69  ? -3.644  -9.927  -4.710  1.00 11.81 ? 71   ASP A C   1 
ATOM   511  O O   . ASP A 1 69  ? -4.807  -10.220 -5.030  1.00 11.48 ? 71   ASP A O   1 
ATOM   512  C CB  . ASP A 1 69  ? -2.080  -9.561  -6.638  1.00 12.24 ? 71   ASP A CB  1 
ATOM   513  C CG  . ASP A 1 69  ? -1.456  -8.577  -7.625  1.00 16.83 ? 71   ASP A CG  1 
ATOM   514  O OD1 . ASP A 1 69  ? -2.126  -7.564  -7.959  1.00 18.42 ? 71   ASP A OD1 1 
ATOM   515  O OD2 . ASP A 1 69  ? -0.290  -8.811  -8.035  1.00 16.61 ? 71   ASP A OD2 1 
ATOM   516  N N   . PHE A 1 70  ? -3.038  -10.472 -3.622  1.00 12.01 ? 72   PHE A N   1 
ATOM   517  C CA  . PHE A 1 70  ? -3.786  -11.324 -2.686  1.00 10.93 ? 72   PHE A CA  1 
ATOM   518  C C   . PHE A 1 70  ? -4.965  -10.487 -2.104  1.00 11.08 ? 72   PHE A C   1 
ATOM   519  O O   . PHE A 1 70  ? -6.118  -10.935 -2.138  1.00 12.03 ? 72   PHE A O   1 
ATOM   520  C CB  . PHE A 1 70  ? -2.868  -11.804 -1.569  1.00 9.61  ? 72   PHE A CB  1 
ATOM   521  C CG  . PHE A 1 70  ? -3.659  -12.303 -0.387  1.00 9.36  ? 72   PHE A CG  1 
ATOM   522  C CD1 . PHE A 1 70  ? -4.253  -13.559 -0.406  1.00 8.80  ? 72   PHE A CD1 1 
ATOM   523  C CD2 . PHE A 1 70  ? -3.854  -11.508 0.718   1.00 11.08 ? 72   PHE A CD2 1 
ATOM   524  C CE1 . PHE A 1 70  ? -4.993  -14.002 0.683   1.00 11.19 ? 72   PHE A CE1 1 
ATOM   525  C CE2 . PHE A 1 70  ? -4.595  -11.951 1.798   1.00 10.11 ? 72   PHE A CE2 1 
ATOM   526  C CZ  . PHE A 1 70  ? -5.187  -13.197 1.761   1.00 9.41  ? 72   PHE A CZ  1 
ATOM   527  N N   . TRP A 1 71  ? -4.660  -9.281  -1.606  1.00 12.17 ? 73   TRP A N   1 
ATOM   528  C CA  . TRP A 1 71  ? -5.721  -8.465  -0.992  1.00 13.31 ? 73   TRP A CA  1 
ATOM   529  C C   . TRP A 1 71  ? -6.735  -8.035  -2.024  1.00 13.89 ? 73   TRP A C   1 
ATOM   530  O O   . TRP A 1 71  ? -7.923  -8.003  -1.707  1.00 14.93 ? 73   TRP A O   1 
ATOM   531  C CB  . TRP A 1 71  ? -5.179  -7.298  -0.208  1.00 13.04 ? 73   TRP A CB  1 
ATOM   532  C CG  . TRP A 1 71  ? -4.546  -7.670  1.095   1.00 12.24 ? 73   TRP A CG  1 
ATOM   533  C CD1 . TRP A 1 71  ? -3.251  -7.463  1.463   1.00 13.89 ? 73   TRP A CD1 1 
ATOM   534  C CD2 . TRP A 1 71  ? -5.186  -8.301  2.211   1.00 12.70 ? 73   TRP A CD2 1 
ATOM   535  N NE1 . TRP A 1 71  ? -3.048  -7.917  2.751   1.00 13.61 ? 73   TRP A NE1 1 
ATOM   536  C CE2 . TRP A 1 71  ? -4.221  -8.440  3.228   1.00 13.50 ? 73   TRP A CE2 1 
ATOM   537  C CE3 . TRP A 1 71  ? -6.482  -8.800  2.444   1.00 13.76 ? 73   TRP A CE3 1 
ATOM   538  C CZ2 . TRP A 1 71  ? -4.524  -9.026  4.466   1.00 14.07 ? 73   TRP A CZ2 1 
ATOM   539  C CZ3 . TRP A 1 71  ? -6.787  -9.311  3.695   1.00 13.98 ? 73   TRP A CZ3 1 
ATOM   540  C CH2 . TRP A 1 71  ? -5.813  -9.428  4.675   1.00 14.85 ? 73   TRP A CH2 1 
ATOM   541  N N   . ALA A 1 72  ? -6.318  -7.719  -3.276  1.00 13.44 ? 74   ALA A N   1 
ATOM   542  C CA  . ALA A 1 72  ? -7.300  -7.340  -4.292  1.00 14.30 ? 74   ALA A CA  1 
ATOM   543  C C   . ALA A 1 72  ? -8.292  -8.478  -4.558  1.00 13.82 ? 74   ALA A C   1 
ATOM   544  O O   . ALA A 1 72  ? -9.504  -8.229  -4.712  1.00 14.84 ? 74   ALA A O   1 
ATOM   545  C CB  . ALA A 1 72  ? -6.603  -6.933  -5.577  1.00 14.60 ? 74   ALA A CB  1 
ATOM   546  N N   . LEU A 1 73  ? -7.792  -9.718  -4.604  1.00 13.09 ? 75   LEU A N   1 
ATOM   547  C CA  . LEU A 1 73  ? -8.611  -10.917 -4.756  1.00 12.97 ? 75   LEU A CA  1 
ATOM   548  C C   . LEU A 1 73  ? -9.498  -11.140 -3.535  1.00 11.70 ? 75   LEU A C   1 
ATOM   549  O O   . LEU A 1 73  ? -10.687 -11.331 -3.672  1.00 14.15 ? 75   LEU A O   1 
ATOM   550  C CB  . LEU A 1 73  ? -7.728  -12.116 -5.028  1.00 14.02 ? 75   LEU A CB  1 
ATOM   551  C CG  . LEU A 1 73  ? -8.494  -13.428 -5.273  1.00 14.51 ? 75   LEU A CG  1 
ATOM   552  C CD1 . LEU A 1 73  ? -9.453  -13.330 -6.560  1.00 14.24 ? 75   LEU A CD1 1 
ATOM   553  C CD2 . LEU A 1 73  ? -7.555  -14.601 -5.436  1.00 16.85 ? 75   LEU A CD2 1 
ATOM   554  N N   . TYR A 1 74  ? -8.952  -11.024 -2.348  1.00 12.52 ? 76   TYR A N   1 
ATOM   555  C CA  . TYR A 1 74  ? -9.672  -11.177 -1.091  1.00 12.56 ? 76   TYR A CA  1 
ATOM   556  C C   . TYR A 1 74  ? -10.839 -10.234 -1.030  1.00 15.01 ? 76   TYR A C   1 
ATOM   557  O O   . TYR A 1 74  ? -11.973 -10.638 -0.795  1.00 16.41 ? 76   TYR A O   1 
ATOM   558  C CB  . TYR A 1 74  ? -8.742  -10.970 0.092   1.00 11.70 ? 76   TYR A CB  1 
ATOM   559  C CG  . TYR A 1 74  ? -9.374  -11.343 1.411   1.00 13.02 ? 76   TYR A CG  1 
ATOM   560  C CD1 . TYR A 1 74  ? -9.301  -12.634 1.890   1.00 14.83 ? 76   TYR A CD1 1 
ATOM   561  C CD2 . TYR A 1 74  ? -10.111 -10.424 2.136   1.00 14.57 ? 76   TYR A CD2 1 
ATOM   562  C CE1 . TYR A 1 74  ? -9.920  -13.001 3.086   1.00 16.08 ? 76   TYR A CE1 1 
ATOM   563  C CE2 . TYR A 1 74  ? -10.696 -10.767 3.359   1.00 15.05 ? 76   TYR A CE2 1 
ATOM   564  C CZ  . TYR A 1 74  ? -10.619 -12.063 3.811   1.00 16.12 ? 76   TYR A CZ  1 
ATOM   565  O OH  . TYR A 1 74  ? -11.237 -12.432 4.973   1.00 19.16 ? 76   TYR A OH  1 
ATOM   566  N N   . ASN A 1 75  ? -10.539 -8.944  -1.315  1.00 15.60 ? 77   ASN A N   1 
ATOM   567  C CA  . ASN A 1 75  ? -11.585 -7.927  -1.321  1.00 17.08 ? 77   ASN A CA  1 
ATOM   568  C C   . ASN A 1 75  ? -12.709 -8.196  -2.305  1.00 18.87 ? 77   ASN A C   1 
ATOM   569  O O   . ASN A 1 75  ? -13.870 -7.935  -1.982  1.00 22.05 ? 77   ASN A O   1 
ATOM   570  C CB  . ASN A 1 75  ? -10.986 -6.552  -1.569  1.00 18.44 ? 77   ASN A CB  1 
ATOM   571  C CG  . ASN A 1 75  ? -10.025 -6.089  -0.524  1.00 23.13 ? 77   ASN A CG  1 
ATOM   572  O OD1 . ASN A 1 75  ? -9.994  -6.560  0.596   1.00 20.51 ? 77   ASN A OD1 1 
ATOM   573  N ND2 . ASN A 1 75  ? -9.173  -5.125  -0.874  1.00 25.86 ? 77   ASN A ND2 1 
ATOM   574  N N   . HIS A 1 76  ? -12.393 -8.665  -3.494  1.00 18.21 ? 78   HIS A N   1 
ATOM   575  C CA  . HIS A 1 76  ? -13.319 -9.009  -4.554  1.00 19.68 ? 78   HIS A CA  1 
ATOM   576  C C   . HIS A 1 76  ? -14.127 -10.202 -4.203  1.00 20.13 ? 78   HIS A C   1 
ATOM   577  O O   . HIS A 1 76  ? -15.340 -10.216 -4.459  1.00 21.40 ? 78   HIS A O   1 
ATOM   578  C CB  . HIS A 1 76  ? -12.551 -9.264  -5.869  1.00 22.22 ? 78   HIS A CB  1 
ATOM   579  C CG  . HIS A 1 76  ? -13.353 -9.848  -6.987  1.00 29.34 ? 78   HIS A CG  1 
ATOM   580  N ND1 . HIS A 1 76  ? -13.229 -11.179 -7.339  1.00 32.17 ? 78   HIS A ND1 1 
ATOM   581  C CD2 . HIS A 1 76  ? -14.249 -9.263  -7.811  1.00 32.34 ? 78   HIS A CD2 1 
ATOM   582  C CE1 . HIS A 1 76  ? -14.048 -11.362 -8.362  1.00 32.98 ? 78   HIS A CE1 1 
ATOM   583  N NE2 . HIS A 1 76  ? -14.700 -10.246 -8.658  1.00 32.91 ? 78   HIS A NE2 1 
ATOM   584  N N   . ILE A 1 77  ? -13.497 -11.240 -3.637  1.00 18.86 ? 79   ILE A N   1 
ATOM   585  C CA  . ILE A 1 77  ? -14.231 -12.444 -3.187  1.00 21.03 ? 79   ILE A CA  1 
ATOM   586  C C   . ILE A 1 77  ? -15.178 -12.078 -2.060  1.00 23.75 ? 79   ILE A C   1 
ATOM   587  O O   . ILE A 1 77  ? -16.314 -12.570 -1.999  1.00 25.06 ? 79   ILE A O   1 
ATOM   588  C CB  . ILE A 1 77  ? -13.262 -13.566 -2.730  1.00 20.43 ? 79   ILE A CB  1 
ATOM   589  C CG1 . ILE A 1 77  ? -12.395 -14.090 -3.884  1.00 22.78 ? 79   ILE A CG1 1 
ATOM   590  C CG2 . ILE A 1 77  ? -14.032 -14.714 -2.035  1.00 21.09 ? 79   ILE A CG2 1 
ATOM   591  C CD1 . ILE A 1 77  ? -13.116 -14.597 -5.071  1.00 26.37 ? 79   ILE A CD1 1 
ATOM   592  N N   . GLN A 1 78  ? -14.731 -11.221 -1.166  1.00 26.10 ? 80   GLN A N   1 
ATOM   593  C CA  . GLN A 1 78  ? -15.541 -10.771 -0.040  1.00 29.99 ? 80   GLN A CA  1 
ATOM   594  C C   . GLN A 1 78  ? -16.837 -10.091 -0.552  1.00 35.17 ? 80   GLN A C   1 
ATOM   595  O O   . GLN A 1 78  ? -17.828 -10.130 0.152   1.00 35.82 ? 80   GLN A O   1 
ATOM   596  C CB  . GLN A 1 78  ? -14.719 -9.859  0.894   1.00 31.40 ? 80   GLN A CB  1 
ATOM   597  C CG  . GLN A 1 78  ? -15.301 -9.606  2.302   1.00 34.16 ? 80   GLN A CG  1 
ATOM   598  C CD  . GLN A 1 78  ? -14.389 -8.724  3.134   1.00 35.83 ? 80   GLN A CD  1 
ATOM   599  O OE1 . GLN A 1 78  ? -13.544 -7.992  2.628   1.00 37.94 ? 80   GLN A OE1 1 
ATOM   600  N NE2 . GLN A 1 78  ? -14.523 -8.760  4.437   1.00 36.86 ? 80   GLN A NE2 1 
ATOM   601  N N   . LEU A 1 79  ? -16.819 -9.544  -1.804  1.00 38.53 ? 81   LEU A N   1 
ATOM   602  C CA  . LEU A 1 79  ? -17.917 -8.846  -2.473  1.00 42.24 ? 81   LEU A CA  1 
ATOM   603  C C   . LEU A 1 79  ? -18.697 -9.763  -3.413  1.00 44.45 ? 81   LEU A C   1 
ATOM   604  O O   . LEU A 1 79  ? -19.915 -9.615  -3.532  1.00 45.82 ? 81   LEU A O   1 
ATOM   605  C CB  . LEU A 1 79  ? -17.281 -7.707  -3.303  1.00 43.04 ? 81   LEU A CB  1 
ATOM   606  C CG  . LEU A 1 79  ? -17.958 -6.360  -3.443  1.00 44.93 ? 81   LEU A CG  1 
ATOM   607  C CD1 . LEU A 1 79  ? -18.448 -5.836  -2.103  1.00 45.35 ? 81   LEU A CD1 1 
ATOM   608  C CD2 . LEU A 1 79  ? -16.963 -5.401  -4.043  1.00 45.78 ? 81   LEU A CD2 1 
ATOM   609  N N   . SER A 1 80  ? -18.006 -10.701 -4.087  1.00 45.28 ? 82   SER A N   1 
ATOM   610  C CA  . SER A 1 80  ? -18.555 -11.562 -5.135  1.00 47.43 ? 82   SER A CA  1 
ATOM   611  C C   . SER A 1 80  ? -18.053 -12.989 -5.008  1.00 48.34 ? 82   SER A C   1 
ATOM   612  O O   . SER A 1 80  ? -16.936 -13.316 -5.449  1.00 49.99 ? 82   SER A O   1 
ATOM   613  C CB  . SER A 1 80  ? -18.218 -11.024 -6.520  1.00 51.00 ? 82   SER A CB  1 
ATOM   614  O OG  . SER A 1 80  ? -16.844 -11.133 -6.847  1.00 55.97 ? 82   SER A OG  1 
ATOM   615  N N   . SER A 1 81  ? -18.878 -13.847 -4.401  1.00 46.25 ? 83   SER A N   1 
ATOM   616  C CA  . SER A 1 81  ? -18.603 -15.280 -4.322  1.00 44.66 ? 83   SER A CA  1 
ATOM   617  C C   . SER A 1 81  ? -19.642 -16.002 -3.480  1.00 43.11 ? 83   SER A C   1 
ATOM   618  O O   . SER A 1 81  ? -20.221 -15.394 -2.582  1.00 43.83 ? 83   SER A O   1 
ATOM   619  C CB  . SER A 1 81  ? -17.252 -15.505 -3.677  1.00 46.95 ? 83   SER A CB  1 
ATOM   620  O OG  . SER A 1 81  ? -17.262 -14.855 -2.414  1.00 49.55 ? 83   SER A OG  1 
ATOM   621  N N   . ASN A 1 82  ? -19.852 -17.296 -3.742  1.00 41.14 ? 84   ASN A N   1 
ATOM   622  C CA  . ASN A 1 82  ? -20.915 -18.065 -3.106  1.00 40.26 ? 84   ASN A CA  1 
ATOM   623  C C   . ASN A 1 82  ? -20.373 -18.624 -1.800  1.00 36.70 ? 84   ASN A C   1 
ATOM   624  O O   . ASN A 1 82  ? -19.295 -19.243 -1.782  1.00 36.33 ? 84   ASN A O   1 
ATOM   625  C CB  . ASN A 1 82  ? -21.368 -19.196 -4.058  1.00 44.24 ? 84   ASN A CB  1 
ATOM   626  C CG  . ASN A 1 82  ? -22.774 -19.750 -3.863  1.00 51.71 ? 84   ASN A CG  1 
ATOM   627  O OD1 . ASN A 1 82  ? -22.985 -20.969 -3.821  1.00 54.22 ? 84   ASN A OD1 1 
ATOM   628  N ND2 . ASN A 1 82  ? -23.785 -18.890 -3.773  1.00 54.29 ? 84   ASN A ND2 1 
ATOM   629  N N   . LEU A 1 83  ? -21.089 -18.378 -0.713  1.00 33.58 ? 85   LEU A N   1 
ATOM   630  C CA  . LEU A 1 83  ? -20.819 -19.009 0.573   1.00 31.74 ? 85   LEU A CA  1 
ATOM   631  C C   . LEU A 1 83  ? -22.065 -19.800 0.853   1.00 30.62 ? 85   LEU A C   1 
ATOM   632  O O   . LEU A 1 83  ? -22.944 -19.332 1.574   1.00 32.06 ? 85   LEU A O   1 
ATOM   633  C CB  . LEU A 1 83  ? -20.567 -17.980 1.695   1.00 31.57 ? 85   LEU A CB  1 
ATOM   634  C CG  . LEU A 1 83  ? -20.269 -18.587 3.103   1.00 33.80 ? 85   LEU A CG  1 
ATOM   635  C CD1 . LEU A 1 83  ? -18.912 -19.113 3.169   1.00 33.36 ? 85   LEU A CD1 1 
ATOM   636  C CD2 . LEU A 1 83  ? -20.465 -17.576 4.206   1.00 35.43 ? 85   LEU A CD2 1 
ATOM   637  N N   . MET A 1 84  ? -22.160 -20.999 0.280   1.00 27.45 ? 86   MET A N   1 
ATOM   638  C CA  . MET A 1 84  ? -23.316 -21.856 0.527   1.00 25.76 ? 86   MET A CA  1 
ATOM   639  C C   . MET A 1 84  ? -22.837 -23.265 0.813   1.00 25.29 ? 86   MET A C   1 
ATOM   640  O O   . MET A 1 84  ? -21.725 -23.609 0.403   1.00 24.58 ? 86   MET A O   1 
ATOM   641  C CB  . MET A 1 84  ? -24.176 -21.878 -0.723  1.00 24.80 ? 86   MET A CB  1 
ATOM   642  C CG  . MET A 1 84  ? -24.898 -20.585 -0.970  1.00 27.33 ? 86   MET A CG  1 
ATOM   643  S SD  . MET A 1 84  ? -26.363 -20.333 0.075   1.00 29.48 ? 86   MET A SD  1 
ATOM   644  C CE  . MET A 1 84  ? -27.433 -21.445 -0.598  1.00 28.11 ? 86   MET A CE  1 
ATOM   645  N N   . PRO A 1 85  ? -23.666 -24.124 1.460   1.00 24.65 ? 87   PRO A N   1 
ATOM   646  C CA  . PRO A 1 85  ? -23.231 -25.506 1.711   1.00 25.23 ? 87   PRO A CA  1 
ATOM   647  C C   . PRO A 1 85  ? -22.918 -26.196 0.393   1.00 25.68 ? 87   PRO A C   1 
ATOM   648  O O   . PRO A 1 85  ? -23.613 -25.990 -0.615  1.00 24.80 ? 87   PRO A O   1 
ATOM   649  C CB  . PRO A 1 85  ? -24.436 -26.166 2.423   1.00 27.03 ? 87   PRO A CB  1 
ATOM   650  C CG  . PRO A 1 85  ? -25.234 -25.058 2.931   1.00 26.42 ? 87   PRO A CG  1 
ATOM   651  C CD  . PRO A 1 85  ? -25.042 -23.910 1.944   1.00 24.99 ? 87   PRO A CD  1 
ATOM   652  N N   . GLY A 1 86  ? -21.875 -27.009 0.429   1.00 24.96 ? 88   GLY A N   1 
ATOM   653  C CA  . GLY A 1 86  ? -21.365 -27.733 -0.721  1.00 25.48 ? 88   GLY A CA  1 
ATOM   654  C C   . GLY A 1 86  ? -20.236 -27.013 -1.449  1.00 25.29 ? 88   GLY A C   1 
ATOM   655  O O   . GLY A 1 86  ? -19.619 -27.604 -2.351  1.00 26.77 ? 88   GLY A O   1 
ATOM   656  N N   . CYS A 1 87  ? -19.935 -25.749 -1.090  1.00 22.90 ? 89   CYS A N   1 
ATOM   657  C CA  . CYS A 1 87  ? -18.823 -25.045 -1.728  1.00 22.25 ? 89   CYS A CA  1 
ATOM   658  C C   . CYS A 1 87  ? -17.504 -25.532 -1.071  1.00 22.04 ? 89   CYS A C   1 
ATOM   659  O O   . CYS A 1 87  ? -17.435 -25.750 0.142   1.00 21.04 ? 89   CYS A O   1 
ATOM   660  C CB  . CYS A 1 87  ? -18.979 -23.537 -1.612  1.00 23.69 ? 89   CYS A CB  1 
ATOM   661  S SG  . CYS A 1 87  ? -20.388 -22.884 -2.529  1.00 33.12 ? 89   CYS A SG  1 
ATOM   662  N N   . ASP A 1 88  ? -16.467 -25.717 -1.892  1.00 20.72 ? 90   ASP A N   1 
ATOM   663  C CA  . ASP A 1 88  ? -15.096 -25.872 -1.416  1.00 19.38 ? 90   ASP A CA  1 
ATOM   664  C C   . ASP A 1 88  ? -14.271 -24.755 -2.073  1.00 16.71 ? 90   ASP A C   1 
ATOM   665  O O   . ASP A 1 88  ? -14.441 -24.495 -3.241  1.00 15.93 ? 90   ASP A O   1 
ATOM   666  C CB  . ASP A 1 88  ? -14.511 -27.229 -1.768  1.00 19.55 ? 90   ASP A CB  1 
ATOM   667  C CG  . ASP A 1 88  ? -15.320 -28.438 -1.345  1.00 27.60 ? 90   ASP A CG  1 
ATOM   668  O OD1 . ASP A 1 88  ? -15.933 -28.392 -0.271  1.00 24.91 ? 90   ASP A OD1 1 
ATOM   669  O OD2 . ASP A 1 88  ? -15.325 -29.438 -2.099  1.00 32.96 ? 90   ASP A OD2 1 
ATOM   670  N N   . TYR A 1 89  ? -13.380 -24.083 -1.322  1.00 14.14 ? 91   TYR A N   1 
ATOM   671  C CA  . TYR A 1 89  ? -12.405 -23.190 -1.905  1.00 11.79 ? 91   TYR A CA  1 
ATOM   672  C C   . TYR A 1 89  ? -11.034 -23.692 -1.522  1.00 10.82 ? 91   TYR A C   1 
ATOM   673  O O   . TYR A 1 89  ? -10.861 -24.170 -0.417  1.00 10.18 ? 91   TYR A O   1 
ATOM   674  C CB  . TYR A 1 89  ? -12.564 -21.755 -1.398  1.00 11.02 ? 91   TYR A CB  1 
ATOM   675  C CG  . TYR A 1 89  ? -13.786 -21.054 -1.960  1.00 16.39 ? 91   TYR A CG  1 
ATOM   676  C CD1 . TYR A 1 89  ? -15.001 -21.158 -1.333  1.00 17.26 ? 91   TYR A CD1 1 
ATOM   677  C CD2 . TYR A 1 89  ? -13.696 -20.253 -3.086  1.00 18.05 ? 91   TYR A CD2 1 
ATOM   678  C CE1 . TYR A 1 89  ? -16.113 -20.443 -1.790  1.00 19.24 ? 91   TYR A CE1 1 
ATOM   679  C CE2 . TYR A 1 89  ? -14.788 -19.541 -3.556  1.00 19.31 ? 91   TYR A CE2 1 
ATOM   680  C CZ  . TYR A 1 89  ? -15.999 -19.649 -2.911  1.00 21.39 ? 91   TYR A CZ  1 
ATOM   681  O OH  . TYR A 1 89  ? -17.086 -18.966 -3.433  1.00 28.74 ? 91   TYR A OH  1 
ATOM   682  N N   . SER A 1 90  ? -10.094 -23.628 -2.417  1.00 9.85  ? 92   SER A N   1 
ATOM   683  C CA  . SER A 1 90  ? -8.761  -24.198 -2.184  1.00 10.33 ? 92   SER A CA  1 
ATOM   684  C C   . SER A 1 90  ? -7.715  -23.221 -2.659  1.00 11.10 ? 92   SER A C   1 
ATOM   685  O O   . SER A 1 90  ? -7.816  -22.728 -3.796  1.00 11.48 ? 92   SER A O   1 
ATOM   686  C CB  . SER A 1 90  ? -8.591  -25.490 -2.949  1.00 13.46 ? 92   SER A CB  1 
ATOM   687  O OG  . SER A 1 90  ? -9.576  -26.451 -2.629  1.00 16.31 ? 92   SER A OG  1 
ATOM   688  N N   . LEU A 1 91  ? -6.690  -22.944 -1.837  1.00 9.59  ? 93   LEU A N   1 
ATOM   689  C CA  . LEU A 1 91  ? -5.579  -22.123 -2.297  1.00 9.06  ? 93   LEU A CA  1 
ATOM   690  C C   . LEU A 1 91  ? -4.369  -23.021 -2.330  1.00 10.88 ? 93   LEU A C   1 
ATOM   691  O O   . LEU A 1 91  ? -3.972  -23.512 -1.265  1.00 9.71  ? 93   LEU A O   1 
ATOM   692  C CB  . LEU A 1 91  ? -5.279  -20.941 -1.369  1.00 10.28 ? 93   LEU A CB  1 
ATOM   693  C CG  . LEU A 1 91  ? -4.215  -19.983 -1.936  1.00 10.48 ? 93   LEU A CG  1 
ATOM   694  C CD1 . LEU A 1 91  ? -4.757  -19.192 -3.096  1.00 11.24 ? 93   LEU A CD1 1 
ATOM   695  C CD2 . LEU A 1 91  ? -3.651  -19.063 -0.846  1.00 11.66 ? 93   LEU A CD2 1 
ATOM   696  N N   . PHE A 1 92  ? -3.806  -23.296 -3.513  1.00 10.72 ? 94   PHE A N   1 
ATOM   697  C CA  . PHE A 1 92  ? -2.668  -24.216 -3.670  1.00 10.37 ? 94   PHE A CA  1 
ATOM   698  C C   . PHE A 1 92  ? -1.567  -23.513 -4.392  1.00 9.73  ? 94   PHE A C   1 
ATOM   699  O O   . PHE A 1 92  ? -1.789  -22.660 -5.229  1.00 10.50 ? 94   PHE A O   1 
ATOM   700  C CB  . PHE A 1 92  ? -3.042  -25.521 -4.426  1.00 10.82 ? 94   PHE A CB  1 
ATOM   701  C CG  . PHE A 1 92  ? -3.617  -26.538 -3.476  1.00 9.50  ? 94   PHE A CG  1 
ATOM   702  C CD1 . PHE A 1 92  ? -4.830  -26.308 -2.840  1.00 12.08 ? 94   PHE A CD1 1 
ATOM   703  C CD2 . PHE A 1 92  ? -2.944  -27.709 -3.201  1.00 9.59  ? 94   PHE A CD2 1 
ATOM   704  C CE1 . PHE A 1 92  ? -5.345  -27.213 -1.934  1.00 13.35 ? 94   PHE A CE1 1 
ATOM   705  C CE2 . PHE A 1 92  ? -3.465  -28.632 -2.300  1.00 11.21 ? 94   PHE A CE2 1 
ATOM   706  C CZ  . PHE A 1 92  ? -4.682  -28.397 -1.689  1.00 12.32 ? 94   PHE A CZ  1 
ATOM   707  N N   . LYS A 1 93  ? -0.320  -23.896 -4.101  1.00 6.12  ? 95   LYS A N   1 
ATOM   708  C CA  . LYS A 1 93  ? 0.831   -23.441 -4.846  1.00 8.61  ? 95   LYS A CA  1 
ATOM   709  C C   . LYS A 1 93  ? 0.644   -23.718 -6.316  1.00 10.20 ? 95   LYS A C   1 
ATOM   710  O O   . LYS A 1 93  ? 0.074   -24.771 -6.679  1.00 12.12 ? 95   LYS A O   1 
ATOM   711  C CB  . LYS A 1 93  ? 2.090   -24.134 -4.370  1.00 9.65  ? 95   LYS A CB  1 
ATOM   712  C CG  . LYS A 1 93  ? 2.478   -23.693 -2.958  1.00 10.77 ? 95   LYS A CG  1 
ATOM   713  C CD  . LYS A 1 93  ? 3.794   -24.329 -2.490  1.00 11.62 ? 95   LYS A CD  1 
ATOM   714  C CE  . LYS A 1 93  ? 4.200   -23.876 -1.084  1.00 10.16 ? 95   LYS A CE  1 
ATOM   715  N NZ  . LYS A 1 93  ? 5.262   -24.754 -0.500  1.00 10.56 ? 95   LYS A NZ  1 
ATOM   716  N N   . ASP A 1 94  ? 1.073   -22.786 -7.151  1.00 10.67 ? 96   ASP A N   1 
ATOM   717  C CA  . ASP A 1 94  ? 0.892   -22.968 -8.628  1.00 11.62 ? 96   ASP A CA  1 
ATOM   718  C C   . ASP A 1 94  ? 1.544   -24.255 -9.099  1.00 13.08 ? 96   ASP A C   1 
ATOM   719  O O   . ASP A 1 94  ? 2.656   -24.568 -8.679  1.00 14.15 ? 96   ASP A O   1 
ATOM   720  C CB  . ASP A 1 94  ? 1.471   -21.801 -9.403  1.00 14.17 ? 96   ASP A CB  1 
ATOM   721  C CG  . ASP A 1 94  ? 0.927   -21.800 -10.861 1.00 20.73 ? 96   ASP A CG  1 
ATOM   722  O OD1 . ASP A 1 94  ? -0.220  -22.167 -11.063 1.00 22.36 ? 96   ASP A OD1 1 
ATOM   723  O OD2 . ASP A 1 94  ? 1.650   -21.449 -11.737 1.00 25.59 ? 96   ASP A OD2 1 
ATOM   724  N N   . GLY A 1 95  ? 0.823   -25.021 -9.900  1.00 13.76 ? 97   GLY A N   1 
ATOM   725  C CA  . GLY A 1 95  ? 1.295   -26.321 -10.353 1.00 14.31 ? 97   GLY A CA  1 
ATOM   726  C C   . GLY A 1 95  ? 0.872   -27.502 -9.530  1.00 17.17 ? 97   GLY A C   1 
ATOM   727  O O   . GLY A 1 95  ? 1.131   -28.637 -9.932  1.00 19.84 ? 97   GLY A O   1 
ATOM   728  N N   . ILE A 1 96  ? 0.234   -27.282 -8.368  1.00 14.90 ? 98   ILE A N   1 
ATOM   729  C CA  . ILE A 1 96  ? -0.323  -28.362 -7.594  1.00 12.91 ? 98   ILE A CA  1 
ATOM   730  C C   . ILE A 1 96  ? -1.794  -28.283 -7.705  1.00 14.72 ? 98   ILE A C   1 
ATOM   731  O O   . ILE A 1 96  ? -2.400  -27.285 -7.275  1.00 15.80 ? 98   ILE A O   1 
ATOM   732  C CB  . ILE A 1 96  ? 0.093   -28.305 -6.102  1.00 10.49 ? 98   ILE A CB  1 
ATOM   733  C CG1 . ILE A 1 96  ? 1.600   -28.175 -5.901  1.00 12.17 ? 98   ILE A CG1 1 
ATOM   734  C CG2 . ILE A 1 96  ? -0.480  -29.577 -5.397  1.00 9.87  ? 98   ILE A CG2 1 
ATOM   735  C CD1 . ILE A 1 96  ? 2.047   -28.124 -4.474  1.00 14.25 ? 98   ILE A CD1 1 
ATOM   736  N N   . GLU A 1 97  ? -2.412  -29.297 -8.310  1.00 17.20 ? 99   GLU A N   1 
ATOM   737  C CA  . GLU A 1 97  ? -3.834  -29.326 -8.390  1.00 18.94 ? 99   GLU A CA  1 
ATOM   738  C C   . GLU A 1 97  ? -4.390  -29.679 -7.034  1.00 17.93 ? 99   GLU A C   1 
ATOM   739  O O   . GLU A 1 97  ? -3.779  -30.416 -6.248  1.00 17.08 ? 99   GLU A O   1 
ATOM   740  C CB  . GLU A 1 97  ? -4.322  -30.294 -9.456  1.00 21.59 ? 99   GLU A CB  1 
ATOM   741  C CG  . GLU A 1 97  ? -3.806  -29.965 -10.837 1.00 27.17 ? 99   GLU A CG  1 
ATOM   742  C CD  . GLU A 1 97  ? -4.530  -30.794 -11.877 1.00 39.88 ? 99   GLU A CD  1 
ATOM   743  O OE1 . GLU A 1 97  ? -3.880  -31.659 -12.506 1.00 42.45 ? 99   GLU A OE1 1 
ATOM   744  O OE2 . GLU A 1 97  ? -5.753  -30.588 -12.045 1.00 45.40 ? 99   GLU A OE2 1 
ATOM   745  N N   . PRO A 1 98  ? -5.573  -29.144 -6.723  1.00 18.17 ? 100  PRO A N   1 
ATOM   746  C CA  . PRO A 1 98  ? -6.144  -29.359 -5.414  1.00 17.36 ? 100  PRO A CA  1 
ATOM   747  C C   . PRO A 1 98  ? -6.842  -30.692 -5.205  1.00 17.41 ? 100  PRO A C   1 
ATOM   748  O O   . PRO A 1 98  ? -7.991  -30.770 -4.800  1.00 19.36 ? 100  PRO A O   1 
ATOM   749  C CB  . PRO A 1 98  ? -7.103  -28.165 -5.335  1.00 18.82 ? 100  PRO A CB  1 
ATOM   750  C CG  . PRO A 1 98  ? -7.590  -28.038 -6.645  1.00 19.68 ? 100  PRO A CG  1 
ATOM   751  C CD  . PRO A 1 98  ? -6.444  -28.241 -7.528  1.00 18.52 ? 100  PRO A CD  1 
ATOM   752  N N   . MET A 1 99  ? -6.103  -31.774 -5.472  1.00 15.73 ? 101  MET A N   1 
ATOM   753  C CA  . MET A 1 99  ? -6.668  -33.101 -5.457  1.00 14.97 ? 101  MET A CA  1 
ATOM   754  C C   . MET A 1 99  ? -5.574  -34.090 -4.990  1.00 15.04 ? 101  MET A C   1 
ATOM   755  O O   . MET A 1 99  ? -4.383  -33.907 -5.246  1.00 15.28 ? 101  MET A O   1 
ATOM   756  C CB  . MET A 1 99  ? -7.212  -33.453 -6.837  1.00 16.02 ? 101  MET A CB  1 
ATOM   757  C CG  . MET A 1 99  ? -6.239  -33.304 -7.946  1.00 21.93 ? 101  MET A CG  1 
ATOM   758  S SD  . MET A 1 99  ? -7.148  -33.527 -9.509  1.00 34.50 ? 101  MET A SD  1 
ATOM   759  C CE  . MET A 1 99  ? -7.905  -31.836 -9.656  1.00 35.75 ? 101  MET A CE  1 
ATOM   760  N N   . TRP A 1 100 ? -5.994  -35.114 -4.332  1.00 16.07 ? 102  TRP A N   1 
ATOM   761  C CA  . TRP A 1 100 ? -5.106  -36.181 -3.816  1.00 18.14 ? 102  TRP A CA  1 
ATOM   762  C C   . TRP A 1 100 ? -4.198  -36.759 -4.884  1.00 20.05 ? 102  TRP A C   1 
ATOM   763  O O   . TRP A 1 100 ? -3.014  -37.046 -4.609  1.00 20.49 ? 102  TRP A O   1 
ATOM   764  C CB  . TRP A 1 100 ? -5.931  -37.262 -3.138  1.00 18.79 ? 102  TRP A CB  1 
ATOM   765  C CG  . TRP A 1 100 ? -5.167  -38.376 -2.478  1.00 22.39 ? 102  TRP A CG  1 
ATOM   766  C CD1 . TRP A 1 100 ? -3.880  -38.339 -2.041  1.00 24.50 ? 102  TRP A CD1 1 
ATOM   767  C CD2 . TRP A 1 100 ? -5.663  -39.694 -2.146  1.00 24.14 ? 102  TRP A CD2 1 
ATOM   768  N NE1 . TRP A 1 100 ? -3.518  -39.564 -1.521  1.00 25.62 ? 102  TRP A NE1 1 
ATOM   769  C CE2 . TRP A 1 100 ? -4.596  -40.408 -1.566  1.00 25.57 ? 102  TRP A CE2 1 
ATOM   770  C CE3 . TRP A 1 100 ? -6.887  -40.357 -2.337  1.00 25.70 ? 102  TRP A CE3 1 
ATOM   771  C CZ2 . TRP A 1 100 ? -4.736  -41.725 -1.121  1.00 26.64 ? 102  TRP A CZ2 1 
ATOM   772  C CZ3 . TRP A 1 100 ? -7.016  -41.662 -1.889  1.00 26.56 ? 102  TRP A CZ3 1 
ATOM   773  C CH2 . TRP A 1 100 ? -5.948  -42.327 -1.296  1.00 26.67 ? 102  TRP A CH2 1 
ATOM   774  N N   . GLU A 1 101 ? -4.717  -36.921 -6.106  1.00 20.48 ? 103  GLU A N   1 
ATOM   775  C CA  . GLU A 1 101 ? -3.934  -37.562 -7.161  1.00 20.66 ? 103  GLU A CA  1 
ATOM   776  C C   . GLU A 1 101 ? -2.801  -36.791 -7.667  1.00 21.14 ? 103  GLU A C   1 
ATOM   777  O O   . GLU A 1 101 ? -1.925  -37.362 -8.326  1.00 21.21 ? 103  GLU A O   1 
ATOM   778  C CB  . GLU A 1 101 ? -4.820  -37.925 -8.335  1.00 24.91 ? 103  GLU A CB  1 
ATOM   779  C CG  . GLU A 1 101 ? -5.328  -36.759 -9.109  1.00 31.51 ? 103  GLU A CG  1 
ATOM   780  C CD  . GLU A 1 101 ? -5.881  -37.212 -10.437 1.00 42.13 ? 103  GLU A CD  1 
ATOM   781  O OE1 . GLU A 1 101 ? -6.511  -38.295 -10.493 1.00 42.84 ? 103  GLU A OE1 1 
ATOM   782  O OE2 . GLU A 1 101 ? -5.678  -36.474 -11.427 1.00 44.64 ? 103  GLU A OE2 1 
ATOM   783  N N   . ASP A 1 102 ? -2.724  -35.440 -7.394  1.00 19.00 ? 104  ASP A N   1 
ATOM   784  C CA  . ASP A 1 102 ? -1.534  -34.687 -7.795  1.00 17.98 ? 104  ASP A CA  1 
ATOM   785  C C   . ASP A 1 102 ? -0.290  -35.347 -7.200  1.00 17.74 ? 104  ASP A C   1 
ATOM   786  O O   . ASP A 1 102 ? -0.356  -35.800 -6.051  1.00 17.07 ? 104  ASP A O   1 
ATOM   787  C CB  . ASP A 1 102 ? -1.611  -33.246 -7.274  1.00 16.50 ? 104  ASP A CB  1 
ATOM   788  C CG  . ASP A 1 102 ? -0.585  -32.332 -7.877  1.00 18.25 ? 104  ASP A CG  1 
ATOM   789  O OD1 . ASP A 1 102 ? 0.596   -32.359 -7.433  1.00 15.73 ? 104  ASP A OD1 1 
ATOM   790  O OD2 . ASP A 1 102 ? -0.938  -31.590 -8.794  1.00 17.88 ? 104  ASP A OD2 1 
ATOM   791  N N   . GLU A 1 103 ? 0.794   -35.397 -7.956  1.00 18.54 ? 105  GLU A N   1 
ATOM   792  C CA  . GLU A 1 103 ? 2.048   -35.981 -7.481  1.00 20.06 ? 105  GLU A CA  1 
ATOM   793  C C   . GLU A 1 103 ? 2.488   -35.405 -6.128  1.00 18.67 ? 105  GLU A C   1 
ATOM   794  O O   . GLU A 1 103 ? 3.037   -36.134 -5.302  1.00 19.38 ? 105  GLU A O   1 
ATOM   795  C CB  . GLU A 1 103 ? 3.158   -35.713 -8.502  1.00 25.09 ? 105  GLU A CB  1 
ATOM   796  C CG  . GLU A 1 103 ? 4.374   -36.594 -8.301  1.00 38.01 ? 105  GLU A CG  1 
ATOM   797  C CD  . GLU A 1 103 ? 4.220   -38.011 -8.828  1.00 47.69 ? 105  GLU A CD  1 
ATOM   798  O OE1 . GLU A 1 103 ? 5.247   -38.720 -8.870  1.00 53.90 ? 105  GLU A OE1 1 
ATOM   799  O OE2 . GLU A 1 103 ? 3.089   -38.416 -9.195  1.00 48.24 ? 105  GLU A OE2 1 
ATOM   800  N N   . LYS A 1 104 ? 2.260   -34.085 -5.915  1.00 16.81 ? 106  LYS A N   1 
ATOM   801  C CA  . LYS A 1 104 ? 2.633   -33.453 -4.654  1.00 15.62 ? 106  LYS A CA  1 
ATOM   802  C C   . LYS A 1 104 ? 1.695   -33.708 -3.495  1.00 13.94 ? 106  LYS A C   1 
ATOM   803  O O   . LYS A 1 104 ? 2.068   -33.387 -2.360  1.00 13.10 ? 106  LYS A O   1 
ATOM   804  C CB  . LYS A 1 104 ? 2.810   -31.938 -4.852  1.00 16.54 ? 106  LYS A CB  1 
ATOM   805  C CG  . LYS A 1 104 ? 3.940   -31.568 -5.827  1.00 23.14 ? 106  LYS A CG  1 
ATOM   806  C CD  . LYS A 1 104 ? 5.291   -31.957 -5.296  1.00 31.85 ? 106  LYS A CD  1 
ATOM   807  C CE  . LYS A 1 104 ? 6.455   -31.383 -6.057  1.00 39.96 ? 106  LYS A CE  1 
ATOM   808  N NZ  . LYS A 1 104 ? 7.648   -32.264 -5.842  1.00 45.30 ? 106  LYS A NZ  1 
ATOM   809  N N   . ASN A 1 105 ? 0.499   -34.269 -3.732  1.00 13.15 ? 107  ASN A N   1 
ATOM   810  C CA  . ASN A 1 105 ? -0.441  -34.650 -2.676  1.00 11.99 ? 107  ASN A CA  1 
ATOM   811  C C   . ASN A 1 105 ? -0.599  -36.141 -2.412  1.00 14.58 ? 107  ASN A C   1 
ATOM   812  O O   . ASN A 1 105 ? -1.105  -36.512 -1.342  1.00 15.49 ? 107  ASN A O   1 
ATOM   813  C CB  . ASN A 1 105 ? -1.802  -34.115 -2.968  1.00 12.31 ? 107  ASN A CB  1 
ATOM   814  C CG  . ASN A 1 105 ? -1.846  -32.624 -3.066  1.00 11.83 ? 107  ASN A CG  1 
ATOM   815  O OD1 . ASN A 1 105 ? -1.232  -31.917 -2.268  1.00 10.21 ? 107  ASN A OD1 1 
ATOM   816  N ND2 . ASN A 1 105 ? -2.612  -32.077 -4.000  1.00 13.85 ? 107  ASN A ND2 1 
ATOM   817  N N   . LYS A 1 106 ? -0.175  -36.999 -3.338  1.00 15.46 ? 108  LYS A N   1 
ATOM   818  C CA  . LYS A 1 106 ? -0.482  -38.437 -3.193  1.00 16.82 ? 108  LYS A CA  1 
ATOM   819  C C   . LYS A 1 106 ? 0.031   -39.059 -1.901  1.00 15.25 ? 108  LYS A C   1 
ATOM   820  O O   . LYS A 1 106 ? -0.670  -39.912 -1.320  1.00 16.69 ? 108  LYS A O   1 
ATOM   821  C CB  . LYS A 1 106 ? -0.023  -39.257 -4.415  1.00 20.90 ? 108  LYS A CB  1 
ATOM   822  C CG  . LYS A 1 106 ? 1.395   -39.106 -4.874  1.00 29.30 ? 108  LYS A CG  1 
ATOM   823  C CD  . LYS A 1 106 ? 1.519   -39.879 -6.226  1.00 39.36 ? 108  LYS A CD  1 
ATOM   824  C CE  . LYS A 1 106 ? 2.944   -40.221 -6.570  1.00 45.66 ? 108  LYS A CE  1 
ATOM   825  N NZ  . LYS A 1 106 ? 3.065   -40.954 -7.863  1.00 49.02 ? 108  LYS A NZ  1 
ATOM   826  N N   . ARG A 1 107 ? 1.236   -38.666 -1.439  1.00 13.57 ? 109  ARG A N   1 
ATOM   827  C CA  A ARG A 1 107 ? 1.835   -39.162 -0.199  0.50 13.25 ? 109  ARG A CA  1 
ATOM   828  C CA  B ARG A 1 107 ? 1.802   -39.194 -0.217  0.50 12.78 ? 109  ARG A CA  1 
ATOM   829  C C   . ARG A 1 107 ? 1.477   -38.290 1.027   1.00 13.97 ? 109  ARG A C   1 
ATOM   830  O O   . ARG A 1 107 ? 1.996   -38.487 2.128   1.00 15.43 ? 109  ARG A O   1 
ATOM   831  C CB  A ARG A 1 107 ? 3.381   -39.213 -0.328  0.50 15.55 ? 109  ARG A CB  1 
ATOM   832  C CB  B ARG A 1 107 ? 3.322   -39.417 -0.431  0.50 13.95 ? 109  ARG A CB  1 
ATOM   833  C CG  A ARG A 1 107 ? 3.907   -40.009 -1.504  0.50 18.29 ? 109  ARG A CG  1 
ATOM   834  C CG  B ARG A 1 107 ? 3.691   -40.689 -1.261  0.50 15.48 ? 109  ARG A CG  1 
ATOM   835  C CD  A ARG A 1 107 ? 5.357   -40.529 -1.296  0.50 19.63 ? 109  ARG A CD  1 
ATOM   836  C CD  B ARG A 1 107 ? 5.205   -41.012 -1.113  0.50 14.89 ? 109  ARG A CD  1 
ATOM   837  N NE  A ARG A 1 107 ? 5.383   -41.925 -0.822  0.50 22.89 ? 109  ARG A NE  1 
ATOM   838  N NE  B ARG A 1 107 ? 5.562   -41.126 0.296   0.50 13.73 ? 109  ARG A NE  1 
ATOM   839  C CZ  A ARG A 1 107 ? 5.499   -42.340 0.440   0.50 26.35 ? 109  ARG A CZ  1 
ATOM   840  C CZ  B ARG A 1 107 ? 5.320   -42.182 1.071   0.50 15.94 ? 109  ARG A CZ  1 
ATOM   841  N NH1 A ARG A 1 107 ? 5.612   -41.467 1.431   0.50 26.62 ? 109  ARG A NH1 1 
ATOM   842  N NH1 B ARG A 1 107 ? 4.716   -43.257 0.575   0.50 18.58 ? 109  ARG A NH1 1 
ATOM   843  N NH2 A ARG A 1 107 ? 5.497   -43.633 0.719   0.50 29.17 ? 109  ARG A NH2 1 
ATOM   844  N NH2 B ARG A 1 107 ? 5.665   -42.164 2.353   0.50 15.29 ? 109  ARG A NH2 1 
ATOM   845  N N   . GLY A 1 108 ? 0.605   -37.324 0.853   1.00 13.85 ? 110  GLY A N   1 
ATOM   846  C CA  . GLY A 1 108 ? 0.406   -36.290 1.850   1.00 13.07 ? 110  GLY A CA  1 
ATOM   847  C C   . GLY A 1 108 ? -0.705  -36.528 2.837   1.00 11.18 ? 110  GLY A C   1 
ATOM   848  O O   . GLY A 1 108 ? -1.246  -37.625 3.030   1.00 10.87 ? 110  GLY A O   1 
ATOM   849  N N   . GLY A 1 109 ? -1.080  -35.440 3.431   1.00 10.90 ? 111  GLY A N   1 
ATOM   850  C CA  . GLY A 1 109 ? -2.077  -35.430 4.492   1.00 9.94  ? 111  GLY A CA  1 
ATOM   851  C C   . GLY A 1 109 ? -2.468  -34.022 4.852   1.00 11.03 ? 111  GLY A C   1 
ATOM   852  O O   . GLY A 1 109 ? -2.003  -33.064 4.194   1.00 10.41 ? 111  GLY A O   1 
ATOM   853  N N   . ARG A 1 110 ? -3.313  -33.867 5.887   1.00 10.86 ? 112  ARG A N   1 
ATOM   854  C CA  . ARG A 1 110 ? -3.802  -32.527 6.204   1.00 10.02 ? 112  ARG A CA  1 
ATOM   855  C C   . ARG A 1 110 ? -3.919  -32.354 7.720   1.00 10.45 ? 112  ARG A C   1 
ATOM   856  O O   . ARG A 1 110 ? -4.233  -33.322 8.433   1.00 11.83 ? 112  ARG A O   1 
ATOM   857  C CB  . ARG A 1 110 ? -5.122  -32.252 5.480   1.00 12.33 ? 112  ARG A CB  1 
ATOM   858  C CG  . ARG A 1 110 ? -6.300  -32.992 6.103   1.00 15.14 ? 112  ARG A CG  1 
ATOM   859  C CD  . ARG A 1 110 ? -7.565  -32.903 5.280   1.00 21.48 ? 112  ARG A CD  1 
ATOM   860  N NE  . ARG A 1 110 ? -8.574  -33.786 5.891   1.00 24.78 ? 112  ARG A NE  1 
ATOM   861  C CZ  . ARG A 1 110 ? -9.849  -33.857 5.517   1.00 26.78 ? 112  ARG A CZ  1 
ATOM   862  N NH1 . ARG A 1 110 ? -10.680 -34.690 6.130   1.00 25.77 ? 112  ARG A NH1 1 
ATOM   863  N NH2 . ARG A 1 110 ? -10.298 -33.107 4.533   1.00 23.96 ? 112  ARG A NH2 1 
ATOM   864  N N   . TRP A 1 111 ? -3.672  -31.122 8.189   1.00 9.72  ? 113  TRP A N   1 
ATOM   865  C CA  . TRP A 1 111 ? -4.052  -30.657 9.518   1.00 10.50 ? 113  TRP A CA  1 
ATOM   866  C C   . TRP A 1 111 ? -5.451  -30.125 9.401   1.00 12.41 ? 113  TRP A C   1 
ATOM   867  O O   . TRP A 1 111 ? -5.669  -29.196 8.620   1.00 12.13 ? 113  TRP A O   1 
ATOM   868  C CB  . TRP A 1 111 ? -3.147  -29.510 9.994   1.00 9.91  ? 113  TRP A CB  1 
ATOM   869  C CG  . TRP A 1 111 ? -1.841  -30.014 10.469  1.00 9.91  ? 113  TRP A CG  1 
ATOM   870  C CD1 . TRP A 1 111 ? -0.633  -29.910 9.833   1.00 11.08 ? 113  TRP A CD1 1 
ATOM   871  C CD2 . TRP A 1 111 ? -1.596  -30.718 11.692  1.00 10.20 ? 113  TRP A CD2 1 
ATOM   872  N NE1 . TRP A 1 111 ? 0.341   -30.519 10.572  1.00 10.65 ? 113  TRP A NE1 1 
ATOM   873  C CE2 . TRP A 1 111 ? -0.221  -31.024 11.731  1.00 10.33 ? 113  TRP A CE2 1 
ATOM   874  C CE3 . TRP A 1 111 ? -2.397  -31.076 12.790  1.00 10.92 ? 113  TRP A CE3 1 
ATOM   875  C CZ2 . TRP A 1 111 ? 0.366   -31.682 12.810  1.00 10.62 ? 113  TRP A CZ2 1 
ATOM   876  C CZ3 . TRP A 1 111 ? -1.802  -31.742 13.852  1.00 10.86 ? 113  TRP A CZ3 1 
ATOM   877  C CH2 . TRP A 1 111 ? -0.434  -31.997 13.865  1.00 11.00 ? 113  TRP A CH2 1 
ATOM   878  N N   . LEU A 1 112 ? -6.383  -30.679 10.191  1.00 11.15 ? 114  LEU A N   1 
ATOM   879  C CA  . LEU A 1 112 ? -7.794  -30.341 10.032  1.00 12.49 ? 114  LEU A CA  1 
ATOM   880  C C   . LEU A 1 112 ? -8.324  -29.598 11.241  1.00 16.15 ? 114  LEU A C   1 
ATOM   881  O O   . LEU A 1 112 ? -8.078  -30.009 12.400  1.00 15.82 ? 114  LEU A O   1 
ATOM   882  C CB  . LEU A 1 112 ? -8.572  -31.653 9.887   1.00 13.13 ? 114  LEU A CB  1 
ATOM   883  C CG  . LEU A 1 112 ? -10.087 -31.515 9.749   1.00 15.93 ? 114  LEU A CG  1 
ATOM   884  C CD1 . LEU A 1 112 ? -10.431 -30.929 8.454   1.00 15.81 ? 114  LEU A CD1 1 
ATOM   885  C CD2 . LEU A 1 112 ? -10.741 -32.863 9.909   1.00 17.96 ? 114  LEU A CD2 1 
ATOM   886  N N   . ILE A 1 113 ? -9.115  -28.530 10.942  1.00 15.73 ? 115  ILE A N   1 
ATOM   887  C CA  . ILE A 1 113 ? -9.878  -27.730 11.866  1.00 18.35 ? 115  ILE A CA  1 
ATOM   888  C C   . ILE A 1 113 ? -11.357 -28.031 11.558  1.00 19.22 ? 115  ILE A C   1 
ATOM   889  O O   . ILE A 1 113 ? -11.769 -27.824 10.434  1.00 17.20 ? 115  ILE A O   1 
ATOM   890  C CB  . ILE A 1 113 ? -9.562  -26.212 11.636  1.00 20.29 ? 115  ILE A CB  1 
ATOM   891  C CG1 . ILE A 1 113 ? -8.051  -25.914 11.540  1.00 23.58 ? 115  ILE A CG1 1 
ATOM   892  C CG2 . ILE A 1 113 ? -10.240 -25.365 12.715  1.00 22.43 ? 115  ILE A CG2 1 
ATOM   893  C CD1 . ILE A 1 113 ? -7.223  -26.433 12.658  1.00 23.92 ? 115  ILE A CD1 1 
ATOM   894  N N   . THR A 1 114 ? -12.148 -28.543 12.535  1.00 19.81 ? 116  THR A N   1 
ATOM   895  C CA  . THR A 1 114 ? -13.584 -28.720 12.299  1.00 21.73 ? 116  THR A CA  1 
ATOM   896  C C   . THR A 1 114 ? -14.368 -27.761 13.131  1.00 22.61 ? 116  THR A C   1 
ATOM   897  O O   . THR A 1 114 ? -14.144 -27.711 14.348  1.00 25.11 ? 116  THR A O   1 
ATOM   898  C CB  . THR A 1 114 ? -14.000 -30.135 12.614  1.00 26.73 ? 116  THR A CB  1 
ATOM   899  O OG1 . THR A 1 114 ? -13.709 -30.337 13.997  1.00 33.13 ? 116  THR A OG1 1 
ATOM   900  C CG2 . THR A 1 114 ? -13.269 -31.141 11.805  1.00 25.48 ? 116  THR A CG2 1 
ATOM   901  N N   . LEU A 1 115 ? -15.304 -27.036 12.525  1.00 21.81 ? 117  LEU A N   1 
ATOM   902  C CA  . LEU A 1 115 ? -16.043 -26.011 13.221  1.00 26.72 ? 117  LEU A CA  1 
ATOM   903  C C   . LEU A 1 115 ? -17.437 -26.567 13.572  1.00 30.57 ? 117  LEU A C   1 
ATOM   904  O O   . LEU A 1 115 ? -17.936 -27.503 12.921  1.00 31.22 ? 117  LEU A O   1 
ATOM   905  C CB  . LEU A 1 115 ? -16.173 -24.716 12.359  1.00 28.08 ? 117  LEU A CB  1 
ATOM   906  C CG  . LEU A 1 115 ? -14.888 -24.073 11.732  1.00 32.64 ? 117  LEU A CG  1 
ATOM   907  C CD1 . LEU A 1 115 ? -15.118 -22.612 11.408  1.00 33.81 ? 117  LEU A CD1 1 
ATOM   908  C CD2 . LEU A 1 115 ? -13.704 -24.133 12.612  1.00 35.34 ? 117  LEU A CD2 1 
ATOM   909  N N   . ASN A 1 116 ? -18.038 -25.991 14.595  1.00 33.26 ? 118  ASN A N   1 
ATOM   910  C CA  . ASN A 1 116 ? -19.481 -26.129 14.854  1.00 37.63 ? 118  ASN A CA  1 
ATOM   911  C C   . ASN A 1 116 ? -20.212 -25.072 13.984  1.00 40.77 ? 118  ASN A C   1 
ATOM   912  O O   . ASN A 1 116 ? -19.578 -24.168 13.429  1.00 42.07 ? 118  ASN A O   1 
ATOM   913  C CB  . ASN A 1 116 ? -19.828 -25.822 16.344  1.00 39.87 ? 118  ASN A CB  1 
ATOM   914  C CG  . ASN A 1 116 ? -18.934 -26.376 17.426  1.00 45.19 ? 118  ASN A CG  1 
ATOM   915  O OD1 . ASN A 1 116 ? -18.283 -27.420 17.303  1.00 48.09 ? 118  ASN A OD1 1 
ATOM   916  N ND2 . ASN A 1 116 ? -18.892 -25.678 18.534  1.00 46.06 ? 118  ASN A ND2 1 
ATOM   917  N N   . LYS A 1 117 ? -21.534 -25.155 13.892  1.00 42.83 ? 119  LYS A N   1 
ATOM   918  C CA  . LYS A 1 117 ? -22.332 -24.143 13.179  1.00 44.25 ? 119  LYS A CA  1 
ATOM   919  C C   . LYS A 1 117 ? -22.221 -22.774 13.843  1.00 44.13 ? 119  LYS A C   1 
ATOM   920  O O   . LYS A 1 117 ? -22.076 -21.780 13.130  1.00 44.14 ? 119  LYS A O   1 
ATOM   921  C CB  . LYS A 1 117 ? -23.805 -24.559 13.066  1.00 47.74 ? 119  LYS A CB  1 
ATOM   922  C CG  . LYS A 1 117 ? -24.004 -25.973 12.563  1.00 53.48 ? 119  LYS A CG  1 
ATOM   923  C CD  . LYS A 1 117 ? -24.553 -26.887 13.653  1.00 59.56 ? 119  LYS A CD  1 
ATOM   924  C CE  . LYS A 1 117 ? -24.491 -28.347 13.296  1.00 63.96 ? 119  LYS A CE  1 
ATOM   925  N NZ  . LYS A 1 117 ? -25.222 -29.173 14.295  1.00 67.20 ? 119  LYS A NZ  1 
ATOM   926  N N   . GLN A 1 118 ? -22.275 -22.690 15.190  1.00 44.48 ? 120  GLN A N   1 
ATOM   927  C CA  . GLN A 1 118 ? -22.107 -21.393 15.884  1.00 46.60 ? 120  GLN A CA  1 
ATOM   928  C C   . GLN A 1 118 ? -20.790 -20.704 15.486  1.00 47.14 ? 120  GLN A C   1 
ATOM   929  O O   . GLN A 1 118 ? -20.711 -19.473 15.444  1.00 47.54 ? 120  GLN A O   1 
ATOM   930  C CB  . GLN A 1 118 ? -22.152 -21.571 17.427  1.00 50.79 ? 120  GLN A CB  1 
ATOM   931  C CG  . GLN A 1 118 ? -23.584 -21.774 17.994  1.00 57.71 ? 120  GLN A CG  1 
ATOM   932  C CD  . GLN A 1 118 ? -23.645 -22.583 19.279  1.00 64.56 ? 120  GLN A CD  1 
ATOM   933  O OE1 . GLN A 1 118 ? -22.635 -22.829 19.963  1.00 67.84 ? 120  GLN A OE1 1 
ATOM   934  N NE2 . GLN A 1 118 ? -24.846 -23.020 19.639  1.00 64.58 ? 120  GLN A NE2 1 
ATOM   935  N N   . GLN A 1 119 ? -19.756 -21.523 15.180  1.00 46.32 ? 121  GLN A N   1 
ATOM   936  C CA  . GLN A 1 119 ? -18.473 -21.035 14.730  1.00 45.76 ? 121  GLN A CA  1 
ATOM   937  C C   . GLN A 1 119 ? -18.436 -20.529 13.279  1.00 46.77 ? 121  GLN A C   1 
ATOM   938  O O   . GLN A 1 119 ? -17.402 -19.972 12.905  1.00 47.26 ? 121  GLN A O   1 
ATOM   939  C CB  . GLN A 1 119 ? -17.409 -22.126 14.948  1.00 44.39 ? 121  GLN A CB  1 
ATOM   940  C CG  . GLN A 1 119 ? -16.916 -22.249 16.351  1.00 42.00 ? 121  GLN A CG  1 
ATOM   941  C CD  . GLN A 1 119 ? -15.753 -23.194 16.361  1.00 41.59 ? 121  GLN A CD  1 
ATOM   942  O OE1 . GLN A 1 119 ? -15.912 -24.385 16.059  1.00 42.95 ? 121  GLN A OE1 1 
ATOM   943  N NE2 . GLN A 1 119 ? -14.553 -22.685 16.698  1.00 37.79 ? 121  GLN A NE2 1 
ATOM   944  N N   . ARG A 1 120 ? -19.511 -20.692 12.459  1.00 46.54 ? 122  ARG A N   1 
ATOM   945  C CA  . ARG A 1 120 ? -19.503 -20.085 11.123  1.00 46.07 ? 122  ARG A CA  1 
ATOM   946  C C   . ARG A 1 120 ? -19.544 -18.572 11.199  1.00 46.11 ? 122  ARG A C   1 
ATOM   947  O O   . ARG A 1 120 ? -18.860 -17.908 10.394  1.00 46.80 ? 122  ARG A O   1 
ATOM   948  C CB  . ARG A 1 120 ? -20.630 -20.547 10.164  1.00 45.41 ? 122  ARG A CB  1 
ATOM   949  C CG  . ARG A 1 120 ? -20.327 -19.974 8.750   1.00 43.63 ? 122  ARG A CG  1 
ATOM   950  C CD  . ARG A 1 120 ? -21.281 -20.282 7.675   1.00 40.05 ? 122  ARG A CD  1 
ATOM   951  N NE  . ARG A 1 120 ? -21.271 -21.703 7.326   1.00 36.64 ? 122  ARG A NE  1 
ATOM   952  C CZ  . ARG A 1 120 ? -22.307 -22.351 6.803   1.00 32.78 ? 122  ARG A CZ  1 
ATOM   953  N NH1 . ARG A 1 120 ? -23.444 -21.712 6.552   1.00 27.53 ? 122  ARG A NH1 1 
ATOM   954  N NH2 . ARG A 1 120 ? -22.217 -23.640 6.528   1.00 30.83 ? 122  ARG A NH2 1 
ATOM   955  N N   . ARG A 1 121 ? -20.346 -18.020 12.115  1.00 44.76 ? 123  ARG A N   1 
ATOM   956  C CA  . ARG A 1 121 ? -20.437 -16.565 12.213  1.00 44.41 ? 123  ARG A CA  1 
ATOM   957  C C   . ARG A 1 121 ? -19.290 -15.977 13.039  1.00 42.65 ? 123  ARG A C   1 
ATOM   958  O O   . ARG A 1 121 ? -18.852 -14.869 12.734  1.00 42.97 ? 123  ARG A O   1 
ATOM   959  C CB  . ARG A 1 121 ? -21.796 -16.122 12.777  1.00 47.41 ? 123  ARG A CB  1 
ATOM   960  C CG  . ARG A 1 121 ? -22.126 -14.643 12.477  1.00 52.65 ? 123  ARG A CG  1 
ATOM   961  C CD  . ARG A 1 121 ? -23.331 -14.148 13.248  1.00 58.19 ? 123  ARG A CD  1 
ATOM   962  N NE  . ARG A 1 121 ? -23.015 -13.943 14.664  1.00 62.57 ? 123  ARG A NE  1 
ATOM   963  C CZ  . ARG A 1 121 ? -23.891 -13.559 15.588  1.00 63.89 ? 123  ARG A CZ  1 
ATOM   964  N NH1 . ARG A 1 121 ? -23.506 -13.403 16.849  1.00 62.25 ? 123  ARG A NH1 1 
ATOM   965  N NH2 . ARG A 1 121 ? -25.163 -13.336 15.260  1.00 64.73 ? 123  ARG A NH2 1 
ATOM   966  N N   . SER A 1 122 ? -18.810 -16.700 14.076  1.00 41.16 ? 124  SER A N   1 
ATOM   967  C CA  . SER A 1 122 ? -17.802 -16.185 15.008  1.00 41.23 ? 124  SER A CA  1 
ATOM   968  C C   . SER A 1 122 ? -16.384 -16.382 14.476  1.00 38.92 ? 124  SER A C   1 
ATOM   969  O O   . SER A 1 122 ? -15.530 -15.501 14.662  1.00 40.09 ? 124  SER A O   1 
ATOM   970  C CB  . SER A 1 122 ? -17.919 -16.917 16.341  1.00 44.99 ? 124  SER A CB  1 
ATOM   971  O OG  . SER A 1 122 ? -17.660 -18.302 16.158  1.00 48.92 ? 124  SER A OG  1 
ATOM   972  N N   . ASP A 1 123 ? -16.131 -17.521 13.801  1.00 35.29 ? 125  ASP A N   1 
ATOM   973  C CA  . ASP A 1 123 ? -14.773 -18.012 13.586  1.00 32.51 ? 125  ASP A CA  1 
ATOM   974  C C   . ASP A 1 123 ? -14.436 -18.361 12.126  1.00 26.26 ? 125  ASP A C   1 
ATOM   975  O O   . ASP A 1 123 ? -13.250 -18.391 11.862  1.00 23.02 ? 125  ASP A O   1 
ATOM   976  C CB  . ASP A 1 123 ? -14.503 -19.256 14.441  1.00 36.55 ? 125  ASP A CB  1 
ATOM   977  C CG  . ASP A 1 123 ? -14.302 -19.017 15.925  1.00 46.82 ? 125  ASP A CG  1 
ATOM   978  O OD1 . ASP A 1 123 ? -14.079 -17.857 16.315  1.00 49.06 ? 125  ASP A OD1 1 
ATOM   979  O OD2 . ASP A 1 123 ? -14.357 -20.000 16.694  1.00 51.43 ? 125  ASP A OD2 1 
ATOM   980  N N   . LEU A 1 124 ? -15.418 -18.633 11.194  1.00 23.22 ? 126  LEU A N   1 
ATOM   981  C CA  . LEU A 1 124 ? -15.010 -19.202 9.896   1.00 20.49 ? 126  LEU A CA  1 
ATOM   982  C C   . LEU A 1 124 ? -14.128 -18.222 9.116   1.00 17.61 ? 126  LEU A C   1 
ATOM   983  O O   . LEU A 1 124 ? -13.064 -18.608 8.637   1.00 16.11 ? 126  LEU A O   1 
ATOM   984  C CB  . LEU A 1 124 ? -16.166 -19.686 9.021   1.00 20.99 ? 126  LEU A CB  1 
ATOM   985  C CG  . LEU A 1 124 ? -15.783 -20.304 7.652   1.00 22.97 ? 126  LEU A CG  1 
ATOM   986  C CD1 . LEU A 1 124 ? -15.104 -21.700 7.797   1.00 23.95 ? 126  LEU A CD1 1 
ATOM   987  C CD2 . LEU A 1 124 ? -17.060 -20.474 6.760   1.00 25.58 ? 126  LEU A CD2 1 
ATOM   988  N N   . ASP A 1 125 ? -14.550 -16.983 8.998   1.00 16.48 ? 127  ASP A N   1 
ATOM   989  C CA  . ASP A 1 125 ? -13.823 -15.994 8.243   1.00 15.84 ? 127  ASP A CA  1 
ATOM   990  C C   . ASP A 1 125 ? -12.446 -15.743 8.889   1.00 14.51 ? 127  ASP A C   1 
ATOM   991  O O   . ASP A 1 125 ? -11.468 -15.680 8.155   1.00 14.71 ? 127  ASP A O   1 
ATOM   992  C CB  . ASP A 1 125 ? -14.614 -14.684 8.163   1.00 19.20 ? 127  ASP A CB  1 
ATOM   993  C CG  . ASP A 1 125 ? -15.876 -14.725 7.343   1.00 28.14 ? 127  ASP A CG  1 
ATOM   994  O OD1 . ASP A 1 125 ? -15.992 -15.600 6.448   1.00 28.40 ? 127  ASP A OD1 1 
ATOM   995  O OD2 . ASP A 1 125 ? -16.736 -13.874 7.561   1.00 33.37 ? 127  ASP A OD2 1 
ATOM   996  N N   . ARG A 1 126 ? -12.356 -15.641 10.242  1.00 14.41 ? 128  ARG A N   1 
ATOM   997  C CA  . ARG A 1 126 ? -11.101 -15.263 10.831  1.00 15.89 ? 128  ARG A CA  1 
ATOM   998  C C   . ARG A 1 126 ? -10.161 -16.464 10.736  1.00 14.38 ? 128  ARG A C   1 
ATOM   999  O O   . ARG A 1 126 ? -9.002  -16.260 10.441  1.00 14.60 ? 128  ARG A O   1 
ATOM   1000 C CB  . ARG A 1 126 ? -11.201 -14.690 12.264  1.00 21.48 ? 128  ARG A CB  1 
ATOM   1001 C CG  . ARG A 1 126 ? -11.462 -15.656 13.321  1.00 28.46 ? 128  ARG A CG  1 
ATOM   1002 C CD  . ARG A 1 126 ? -11.836 -14.905 14.625  1.00 35.21 ? 128  ARG A CD  1 
ATOM   1003 N NE  . ARG A 1 126 ? -12.075 -15.806 15.748  1.00 38.12 ? 128  ARG A NE  1 
ATOM   1004 C CZ  . ARG A 1 126 ? -11.118 -16.449 16.420  1.00 43.79 ? 128  ARG A CZ  1 
ATOM   1005 N NH1 . ARG A 1 126 ? -9.838  -16.293 16.090  1.00 44.71 ? 128  ARG A NH1 1 
ATOM   1006 N NH2 . ARG A 1 126 ? -11.432 -17.249 17.427  1.00 46.32 ? 128  ARG A NH2 1 
ATOM   1007 N N   . PHE A 1 127 ? -10.644 -17.687 10.959  1.00 13.66 ? 129  PHE A N   1 
ATOM   1008 C CA  . PHE A 1 127 ? -9.771  -18.871 10.819  1.00 13.77 ? 129  PHE A CA  1 
ATOM   1009 C C   . PHE A 1 127 ? -9.287  -19.076 9.382   1.00 11.71 ? 129  PHE A C   1 
ATOM   1010 O O   . PHE A 1 127 ? -8.096  -19.421 9.175   1.00 10.47 ? 129  PHE A O   1 
ATOM   1011 C CB  . PHE A 1 127 ? -10.459 -20.124 11.282  1.00 15.19 ? 129  PHE A CB  1 
ATOM   1012 C CG  . PHE A 1 127 ? -10.608 -20.358 12.776  1.00 19.65 ? 129  PHE A CG  1 
ATOM   1013 C CD1 . PHE A 1 127 ? -9.982  -19.540 13.695  1.00 22.39 ? 129  PHE A CD1 1 
ATOM   1014 C CD2 . PHE A 1 127 ? -11.387 -21.397 13.252  1.00 24.67 ? 129  PHE A CD2 1 
ATOM   1015 C CE1 . PHE A 1 127 ? -10.134 -19.761 15.070  1.00 25.49 ? 129  PHE A CE1 1 
ATOM   1016 C CE2 . PHE A 1 127 ? -11.532 -21.610 14.629  1.00 26.47 ? 129  PHE A CE2 1 
ATOM   1017 C CZ  . PHE A 1 127 ? -10.899 -20.800 15.510  1.00 26.17 ? 129  PHE A CZ  1 
ATOM   1018 N N   . TRP A 1 128 ? -10.166 -18.883 8.416   1.00 10.56 ? 130  TRP A N   1 
ATOM   1019 C CA  . TRP A 1 128 ? -9.745  -18.993 6.994   1.00 10.41 ? 130  TRP A CA  1 
ATOM   1020 C C   . TRP A 1 128 ? -8.710  -17.944 6.652   1.00 11.10 ? 130  TRP A C   1 
ATOM   1021 O O   . TRP A 1 128 ? -7.658  -18.257 6.061   1.00 10.26 ? 130  TRP A O   1 
ATOM   1022 C CB  . TRP A 1 128 ? -10.959 -18.979 6.074   1.00 9.94  ? 130  TRP A CB  1 
ATOM   1023 C CG  . TRP A 1 128 ? -10.657 -19.142 4.620   1.00 10.21 ? 130  TRP A CG  1 
ATOM   1024 C CD1 . TRP A 1 128 ? -10.981 -18.280 3.630   1.00 10.92 ? 130  TRP A CD1 1 
ATOM   1025 C CD2 . TRP A 1 128 ? -10.020 -20.267 3.985   1.00 9.93  ? 130  TRP A CD2 1 
ATOM   1026 N NE1 . TRP A 1 128 ? -10.619 -18.779 2.415   1.00 10.43 ? 130  TRP A NE1 1 
ATOM   1027 C CE2 . TRP A 1 128 ? -9.997  -19.995 2.599   1.00 10.51 ? 130  TRP A CE2 1 
ATOM   1028 C CE3 . TRP A 1 128 ? -9.393  -21.446 4.467   1.00 8.78  ? 130  TRP A CE3 1 
ATOM   1029 C CZ2 . TRP A 1 128 ? -9.405  -20.864 1.688   1.00 10.14 ? 130  TRP A CZ2 1 
ATOM   1030 C CZ3 . TRP A 1 128 ? -8.836  -22.314 3.552   1.00 10.29 ? 130  TRP A CZ3 1 
ATOM   1031 C CH2 . TRP A 1 128 ? -8.837  -22.023 2.180   1.00 9.80  ? 130  TRP A CH2 1 
ATOM   1032 N N   . LEU A 1 129 ? -8.951  -16.687 7.042   1.00 11.74 ? 131  LEU A N   1 
ATOM   1033 C CA  . LEU A 1 129 ? -7.959  -15.633 6.775   1.00 10.90 ? 131  LEU A CA  1 
ATOM   1034 C C   . LEU A 1 129 ? -6.611  -15.972 7.419   1.00 10.50 ? 131  LEU A C   1 
ATOM   1035 O O   . LEU A 1 129 ? -5.600  -15.901 6.752   1.00 10.24 ? 131  LEU A O   1 
ATOM   1036 C CB  . LEU A 1 129 ? -8.440  -14.279 7.231   1.00 10.37 ? 131  LEU A CB  1 
ATOM   1037 C CG  . LEU A 1 129 ? -7.465  -13.130 7.002   1.00 12.12 ? 131  LEU A CG  1 
ATOM   1038 C CD1 . LEU A 1 129 ? -6.955  -13.040 5.540   1.00 14.14 ? 131  LEU A CD1 1 
ATOM   1039 C CD2 . LEU A 1 129 ? -8.132  -11.824 7.492   1.00 13.82 ? 131  LEU A CD2 1 
ATOM   1040 N N   . GLU A 1 130 ? -6.581  -16.396 8.683   1.00 10.78 ? 132  GLU A N   1 
ATOM   1041 C CA  . GLU A 1 130 ? -5.322  -16.742 9.355   1.00 10.20 ? 132  GLU A CA  1 
ATOM   1042 C C   . GLU A 1 130 ? -4.592  -17.873 8.591   1.00 11.23 ? 132  GLU A C   1 
ATOM   1043 O O   . GLU A 1 130 ? -3.360  -17.835 8.420   1.00 12.26 ? 132  GLU A O   1 
ATOM   1044 C CB  . GLU A 1 130 ? -5.541  -17.133 10.818  1.00 12.50 ? 132  GLU A CB  1 
ATOM   1045 C CG  . GLU A 1 130 ? -6.221  -16.089 11.689  1.00 22.81 ? 132  GLU A CG  1 
ATOM   1046 C CD  . GLU A 1 130 ? -5.476  -14.774 11.803  1.00 25.09 ? 132  GLU A CD  1 
ATOM   1047 O OE1 . GLU A 1 130 ? -4.239  -14.764 11.655  1.00 17.75 ? 132  GLU A OE1 1 
ATOM   1048 O OE2 . GLU A 1 130 ? -6.148  -13.746 12.033  1.00 34.35 ? 132  GLU A OE2 1 
ATOM   1049 N N   . THR A 1 131 ? -5.360  -18.886 8.124   1.00 9.03  ? 133  THR A N   1 
ATOM   1050 C CA  . THR A 1 131 ? -4.813  -19.956 7.264   1.00 8.11  ? 133  THR A CA  1 
ATOM   1051 C C   . THR A 1 131 ? -4.160  -19.374 6.021   1.00 8.01  ? 133  THR A C   1 
ATOM   1052 O O   . THR A 1 131 ? -3.021  -19.710 5.696   1.00 7.70  ? 133  THR A O   1 
ATOM   1053 C CB  . THR A 1 131 ? -5.928  -20.961 6.901   1.00 9.64  ? 133  THR A CB  1 
ATOM   1054 O OG1 . THR A 1 131 ? -6.539  -21.427 8.118   1.00 10.59 ? 133  THR A OG1 1 
ATOM   1055 C CG2 . THR A 1 131 ? -5.391  -22.145 6.155   1.00 9.97  ? 133  THR A CG2 1 
ATOM   1056 N N   . LEU A 1 132 ? -4.878  -18.477 5.326   1.00 7.99  ? 134  LEU A N   1 
ATOM   1057 C CA  . LEU A 1 132 ? -4.328  -17.883 4.072   1.00 8.17  ? 134  LEU A CA  1 
ATOM   1058 C C   . LEU A 1 132 ? -3.031  -17.108 4.368   1.00 8.63  ? 134  LEU A C   1 
ATOM   1059 O O   . LEU A 1 132 ? -2.059  -17.210 3.604   1.00 8.95  ? 134  LEU A O   1 
ATOM   1060 C CB  . LEU A 1 132 ? -5.353  -16.961 3.460   1.00 9.54  ? 134  LEU A CB  1 
ATOM   1061 C CG  . LEU A 1 132 ? -6.668  -17.604 3.006   1.00 10.70 ? 134  LEU A CG  1 
ATOM   1062 C CD1 . LEU A 1 132 ? -7.633  -16.501 2.556   1.00 11.55 ? 134  LEU A CD1 1 
ATOM   1063 C CD2 . LEU A 1 132 ? -6.416  -18.580 1.888   1.00 12.53 ? 134  LEU A CD2 1 
ATOM   1064 N N   . LEU A 1 133 ? -3.002  -16.338 5.474   1.00 9.23  ? 135  LEU A N   1 
ATOM   1065 C CA  . LEU A 1 133 ? -1.806  -15.603 5.833   1.00 8.63  ? 135  LEU A CA  1 
ATOM   1066 C C   . LEU A 1 133 ? -0.628  -16.503 6.166   1.00 9.54  ? 135  LEU A C   1 
ATOM   1067 O O   . LEU A 1 133 ? 0.509   -16.162 5.844   1.00 10.30 ? 135  LEU A O   1 
ATOM   1068 C CB  . LEU A 1 133 ? -2.072  -14.626 6.966   1.00 8.61  ? 135  LEU A CB  1 
ATOM   1069 C CG  . LEU A 1 133 ? -3.175  -13.566 6.693   1.00 11.05 ? 135  LEU A CG  1 
ATOM   1070 C CD1 . LEU A 1 133 ? -3.260  -12.678 7.833   1.00 13.49 ? 135  LEU A CD1 1 
ATOM   1071 C CD2 . LEU A 1 133 ? -2.948  -12.817 5.375   1.00 11.79 ? 135  LEU A CD2 1 
ATOM   1072 N N   . CYS A 1 134 ? -0.881  -17.661 6.791   1.00 9.38  ? 136  CYS A N   1 
ATOM   1073 C CA  . CYS A 1 134 ? 0.194   -18.671 7.068   1.00 8.44  ? 136  CYS A CA  1 
ATOM   1074 C C   . CYS A 1 134 ? 0.819   -19.182 5.746   1.00 9.08  ? 136  CYS A C   1 
ATOM   1075 O O   . CYS A 1 134 ? 2.021   -19.387 5.663   1.00 9.96  ? 136  CYS A O   1 
ATOM   1076 C CB  . CYS A 1 134 ? -0.308  -19.818 7.909   1.00 9.90  ? 136  CYS A CB  1 
ATOM   1077 S SG  . CYS A 1 134 ? -0.558  -19.386 9.663   1.00 12.49 ? 136  CYS A SG  1 
ATOM   1078 N N   . LEU A 1 135 ? -0.030  -19.432 4.771   1.00 8.37  ? 137  LEU A N   1 
ATOM   1079 C CA  . LEU A 1 135 ? 0.370   -19.871 3.477   1.00 8.98  ? 137  LEU A CA  1 
ATOM   1080 C C   . LEU A 1 135 ? 1.187   -18.816 2.750   1.00 8.52  ? 137  LEU A C   1 
ATOM   1081 O O   . LEU A 1 135 ? 2.389   -19.021 2.501   1.00 8.25  ? 137  LEU A O   1 
ATOM   1082 C CB  . LEU A 1 135 ? -0.838  -20.306 2.631   1.00 8.42  ? 137  LEU A CB  1 
ATOM   1083 C CG  . LEU A 1 135 ? -1.203  -21.805 2.686   1.00 9.20  ? 137  LEU A CG  1 
ATOM   1084 C CD1 . LEU A 1 135 ? -1.414  -22.272 4.082   1.00 9.30  ? 137  LEU A CD1 1 
ATOM   1085 C CD2 . LEU A 1 135 ? -2.419  -22.084 1.836   1.00 10.20 ? 137  LEU A CD2 1 
ATOM   1086 N N   . ILE A 1 136 ? 0.554   -17.680 2.436   1.00 7.92  ? 138  ILE A N   1 
ATOM   1087 C CA  . ILE A 1 136 ? 1.231   -16.677 1.623   1.00 8.86  ? 138  ILE A CA  1 
ATOM   1088 C C   . ILE A 1 136 ? 2.449   -16.108 2.305   1.00 8.27  ? 138  ILE A C   1 
ATOM   1089 O O   . ILE A 1 136 ? 3.425   -15.750 1.616   1.00 9.62  ? 138  ILE A O   1 
ATOM   1090 C CB  . ILE A 1 136 ? 0.245   -15.629 1.076   1.00 9.02  ? 138  ILE A CB  1 
ATOM   1091 C CG1 . ILE A 1 136 ? -0.252  -14.670 2.188   1.00 9.70  ? 138  ILE A CG1 1 
ATOM   1092 C CG2 . ILE A 1 136 ? -0.911  -16.342 0.356   1.00 9.52  ? 138  ILE A CG2 1 
ATOM   1093 C CD1 . ILE A 1 136 ? -0.987  -13.444 1.638   1.00 10.06 ? 138  ILE A CD1 1 
ATOM   1094 N N   . GLY A 1 137 ? 2.403   -16.001 3.635   1.00 8.53  ? 139  GLY A N   1 
ATOM   1095 C CA  . GLY A 1 137 ? 3.538   -15.464 4.398   1.00 7.04  ? 139  GLY A CA  1 
ATOM   1096 C C   . GLY A 1 137 ? 4.660   -16.413 4.708   1.00 8.79  ? 139  GLY A C   1 
ATOM   1097 O O   . GLY A 1 137 ? 5.646   -15.979 5.325   1.00 10.29 ? 139  GLY A O   1 
ATOM   1098 N N   . GLU A 1 138 ? 4.526   -17.707 4.301   1.00 7.05  ? 140  GLU A N   1 
ATOM   1099 C CA  . GLU A 1 138 ? 5.563   -18.729 4.521   1.00 7.26  ? 140  GLU A CA  1 
ATOM   1100 C C   . GLU A 1 138 ? 5.896   -18.841 6.032   1.00 9.14  ? 140  GLU A C   1 
ATOM   1101 O O   . GLU A 1 138 ? 7.065   -18.809 6.474   1.00 8.46  ? 140  GLU A O   1 
ATOM   1102 C CB  . GLU A 1 138 ? 6.837   -18.419 3.773   1.00 8.83  ? 140  GLU A CB  1 
ATOM   1103 C CG  . GLU A 1 138 ? 6.633   -18.253 2.282   1.00 8.32  ? 140  GLU A CG  1 
ATOM   1104 C CD  . GLU A 1 138 ? 6.501   -19.562 1.566   1.00 11.83 ? 140  GLU A CD  1 
ATOM   1105 O OE1 . GLU A 1 138 ? 7.319   -20.470 1.820   1.00 12.90 ? 140  GLU A OE1 1 
ATOM   1106 O OE2 . GLU A 1 138 ? 5.558   -19.665 0.743   1.00 12.05 ? 140  GLU A OE2 1 
ATOM   1107 N N   . SER A 1 139 ? 4.849   -18.972 6.815   1.00 8.04  ? 141  SER A N   1 
ATOM   1108 C CA  . SER A 1 139 ? 4.942   -18.910 8.303   1.00 8.13  ? 141  SER A CA  1 
ATOM   1109 C C   . SER A 1 139 ? 5.558   -20.103 9.012   1.00 10.71 ? 141  SER A C   1 
ATOM   1110 O O   . SER A 1 139 ? 5.740   -20.059 10.252  1.00 12.47 ? 141  SER A O   1 
ATOM   1111 C CB  . SER A 1 139 ? 3.557   -18.704 8.890   1.00 10.36 ? 141  SER A CB  1 
ATOM   1112 O OG  . SER A 1 139 ? 2.981   -17.522 8.370   1.00 11.37 ? 141  SER A OG  1 
ATOM   1113 N N   . PHE A 1 140 ? 5.902   -21.124 8.275   1.00 8.02  ? 142  PHE A N   1 
ATOM   1114 C CA  . PHE A 1 140 ? 6.464   -22.388 8.832   1.00 9.84  ? 142  PHE A CA  1 
ATOM   1115 C C   . PHE A 1 140 ? 7.953   -22.538 8.588   1.00 12.45 ? 142  PHE A C   1 
ATOM   1116 O O   . PHE A 1 140 ? 8.474   -23.643 8.678   1.00 12.61 ? 142  PHE A O   1 
ATOM   1117 C CB  . PHE A 1 140 ? 5.674   -23.579 8.313   1.00 9.88  ? 142  PHE A CB  1 
ATOM   1118 C CG  . PHE A 1 140 ? 4.166   -23.381 8.448   1.00 9.69  ? 142  PHE A CG  1 
ATOM   1119 C CD1 . PHE A 1 140 ? 3.574   -23.259 9.696   1.00 9.57  ? 142  PHE A CD1 1 
ATOM   1120 C CD2 . PHE A 1 140 ? 3.357   -23.274 7.329   1.00 9.79  ? 142  PHE A CD2 1 
ATOM   1121 C CE1 . PHE A 1 140 ? 2.181   -23.054 9.815   1.00 10.69 ? 142  PHE A CE1 1 
ATOM   1122 C CE2 . PHE A 1 140 ? 1.970   -23.158 7.448   1.00 8.68  ? 142  PHE A CE2 1 
ATOM   1123 C CZ  . PHE A 1 140 ? 1.390   -23.028 8.688   1.00 9.31  ? 142  PHE A CZ  1 
ATOM   1124 N N   . ASP A 1 141 ? 8.602   -21.432 8.303   1.00 15.94 ? 143  ASP A N   1 
ATOM   1125 C CA  . ASP A 1 141 ? 10.048  -21.330 7.968   1.00 17.27 ? 143  ASP A CA  1 
ATOM   1126 C C   . ASP A 1 141 ? 10.416  -22.342 6.896   1.00 14.99 ? 143  ASP A C   1 
ATOM   1127 O O   . ASP A 1 141 ? 9.697   -22.375 5.907   1.00 14.98 ? 143  ASP A O   1 
ATOM   1128 C CB  . ASP A 1 141 ? 10.827  -21.436 9.248   1.00 21.82 ? 143  ASP A CB  1 
ATOM   1129 C CG  . ASP A 1 141 ? 10.683  -20.199 10.097  1.00 30.86 ? 143  ASP A CG  1 
ATOM   1130 O OD1 . ASP A 1 141 ? 10.930  -19.061 9.558   1.00 34.70 ? 143  ASP A OD1 1 
ATOM   1131 O OD2 . ASP A 1 141 ? 10.341  -20.344 11.259  1.00 30.31 ? 143  ASP A OD2 1 
ATOM   1132 N N   . ASP A 1 142 ? 11.488  -23.158 7.047   1.00 14.72 ? 144  ASP A N   1 
ATOM   1133 C CA  . ASP A 1 142 ? 11.862  -24.062 5.931   1.00 15.37 ? 144  ASP A CA  1 
ATOM   1134 C C   . ASP A 1 142 ? 10.764  -25.080 5.633   1.00 13.97 ? 144  ASP A C   1 
ATOM   1135 O O   . ASP A 1 142 ? 10.609  -25.539 4.488   1.00 15.15 ? 144  ASP A O   1 
ATOM   1136 C CB  . ASP A 1 142 ? 13.126  -24.797 6.268   1.00 17.52 ? 144  ASP A CB  1 
ATOM   1137 C CG  . ASP A 1 142 ? 14.384  -23.934 6.196   1.00 23.83 ? 144  ASP A CG  1 
ATOM   1138 O OD1 . ASP A 1 142 ? 14.341  -22.890 5.581   1.00 26.85 ? 144  ASP A OD1 1 
ATOM   1139 O OD2 . ASP A 1 142 ? 15.389  -24.338 6.750   1.00 27.75 ? 144  ASP A OD2 1 
ATOM   1140 N N   . TYR A 1 143 ? 9.998   -25.439 6.661   1.00 11.36 ? 145  TYR A N   1 
ATOM   1141 C CA  . TYR A 1 143 ? 8.915   -26.396 6.500   1.00 10.86 ? 145  TYR A CA  1 
ATOM   1142 C C   . TYR A 1 143 ? 7.737   -25.875 5.716   1.00 11.85 ? 145  TYR A C   1 
ATOM   1143 O O   . TYR A 1 143 ? 6.892   -26.695 5.337   1.00 11.81 ? 145  TYR A O   1 
ATOM   1144 C CB  . TYR A 1 143 ? 8.479   -26.914 7.846   1.00 12.15 ? 145  TYR A CB  1 
ATOM   1145 C CG  . TYR A 1 143 ? 9.619   -27.513 8.622   1.00 15.11 ? 145  TYR A CG  1 
ATOM   1146 C CD1 . TYR A 1 143 ? 10.440  -28.476 8.058   1.00 15.96 ? 145  TYR A CD1 1 
ATOM   1147 C CD2 . TYR A 1 143 ? 9.913   -27.076 9.890   1.00 19.57 ? 145  TYR A CD2 1 
ATOM   1148 C CE1 . TYR A 1 143 ? 11.474  -29.050 8.788   1.00 19.09 ? 145  TYR A CE1 1 
ATOM   1149 C CE2 . TYR A 1 143 ? 10.953  -27.628 10.618  1.00 22.90 ? 145  TYR A CE2 1 
ATOM   1150 C CZ  . TYR A 1 143 ? 11.721  -28.617 10.065  1.00 22.53 ? 145  TYR A CZ  1 
ATOM   1151 O OH  . TYR A 1 143 ? 12.730  -29.135 10.845  1.00 27.05 ? 145  TYR A OH  1 
ATOM   1152 N N   . SER A 1 144 ? 7.662   -24.585 5.452   1.00 10.25 ? 146  SER A N   1 
ATOM   1153 C CA  . SER A 1 144 ? 6.675   -24.079 4.489   1.00 10.65 ? 146  SER A CA  1 
ATOM   1154 C C   . SER A 1 144 ? 6.775   -24.735 3.114   1.00 11.74 ? 146  SER A C   1 
ATOM   1155 O O   . SER A 1 144 ? 5.771   -24.760 2.401   1.00 10.91 ? 146  SER A O   1 
ATOM   1156 C CB  . SER A 1 144 ? 6.766   -22.551 4.360   1.00 12.67 ? 146  SER A CB  1 
ATOM   1157 O OG  . SER A 1 144 ? 6.081   -21.917 5.434   1.00 13.65 ? 146  SER A OG  1 
ATOM   1158 N N   . ASP A 1 145 ? 7.945   -25.254 2.753   1.00 11.03 ? 147  ASP A N   1 
ATOM   1159 C CA  . ASP A 1 145 ? 8.092   -25.942 1.479   1.00 12.32 ? 147  ASP A CA  1 
ATOM   1160 C C   . ASP A 1 145 ? 7.248   -27.224 1.445   1.00 12.49 ? 147  ASP A C   1 
ATOM   1161 O O   . ASP A 1 145 ? 6.908   -27.700 0.341   1.00 13.34 ? 147  ASP A O   1 
ATOM   1162 C CB  . ASP A 1 145 ? 9.566   -26.280 1.216   1.00 13.84 ? 147  ASP A CB  1 
ATOM   1163 C CG  . ASP A 1 145 ? 10.404  -25.035 0.860   1.00 17.86 ? 147  ASP A CG  1 
ATOM   1164 O OD1 . ASP A 1 145 ? 9.818   -24.014 0.421   1.00 18.12 ? 147  ASP A OD1 1 
ATOM   1165 O OD2 . ASP A 1 145 ? 11.617  -25.079 1.029   1.00 19.83 ? 147  ASP A OD2 1 
ATOM   1166 N N   . ASP A 1 146 ? 6.906   -27.804 2.610   1.00 9.72  ? 148  ASP A N   1 
ATOM   1167 C CA  . ASP A 1 146 ? 6.054   -29.003 2.623   1.00 8.52  ? 148  ASP A CA  1 
ATOM   1168 C C   . ASP A 1 146 ? 4.557   -28.646 2.439   1.00 8.61  ? 148  ASP A C   1 
ATOM   1169 O O   . ASP A 1 146 ? 3.754   -29.561 2.214   1.00 9.46  ? 148  ASP A O   1 
ATOM   1170 C CB  . ASP A 1 146 ? 6.184   -29.797 3.904   1.00 8.43  ? 148  ASP A CB  1 
ATOM   1171 C CG  . ASP A 1 146 ? 7.300   -30.834 3.858   1.00 16.17 ? 148  ASP A CG  1 
ATOM   1172 O OD1 . ASP A 1 146 ? 8.410   -30.470 3.413   1.00 17.21 ? 148  ASP A OD1 1 
ATOM   1173 O OD2 . ASP A 1 146 ? 7.039   -32.012 4.247   1.00 15.50 ? 148  ASP A OD2 1 
ATOM   1174 N N   . VAL A 1 147 ? 4.194   -27.385 2.524   1.00 8.49  ? 149  VAL A N   1 
ATOM   1175 C CA  . VAL A 1 147 ? 2.824   -26.978 2.397   1.00 7.92  ? 149  VAL A CA  1 
ATOM   1176 C C   . VAL A 1 147 ? 2.477   -27.088 0.914   1.00 9.10  ? 149  VAL A C   1 
ATOM   1177 O O   . VAL A 1 147 ? 3.208   -26.601 0.049   1.00 9.90  ? 149  VAL A O   1 
ATOM   1178 C CB  . VAL A 1 147 ? 2.592   -25.572 2.961   1.00 8.27  ? 149  VAL A CB  1 
ATOM   1179 C CG1 . VAL A 1 147 ? 1.180   -25.103 2.626   1.00 8.87  ? 149  VAL A CG1 1 
ATOM   1180 C CG2 . VAL A 1 147 ? 2.826   -25.513 4.462   1.00 9.60  ? 149  VAL A CG2 1 
ATOM   1181 N N   . CYS A 1 148 ? 1.330   -27.741 0.620   1.00 9.28  ? 150  CYS A N   1 
ATOM   1182 C CA  . CYS A 1 148 ? 0.758   -27.753 -0.721  1.00 8.58  ? 150  CYS A CA  1 
ATOM   1183 C C   . CYS A 1 148 ? -0.292  -26.669 -0.897  1.00 9.04  ? 150  CYS A C   1 
ATOM   1184 O O   . CYS A 1 148 ? -0.319  -26.011 -1.942  1.00 10.01 ? 150  CYS A O   1 
ATOM   1185 C CB  . CYS A 1 148 ? 0.183   -29.110 -1.041  1.00 8.41  ? 150  CYS A CB  1 
ATOM   1186 S SG  . CYS A 1 148 ? 1.422   -30.400 -0.960  1.00 12.78 ? 150  CYS A SG  1 
ATOM   1187 N N   . GLY A 1 149 ? -1.129  -26.511 0.089   1.00 7.07  ? 151  GLY A N   1 
ATOM   1188 C CA  . GLY A 1 149 ? -2.308  -25.637 -0.008  1.00 7.18  ? 151  GLY A CA  1 
ATOM   1189 C C   . GLY A 1 149 ? -3.233  -25.740 1.173   1.00 7.00  ? 151  GLY A C   1 
ATOM   1190 O O   . GLY A 1 149 ? -2.898  -26.401 2.150   1.00 8.44  ? 151  GLY A O   1 
ATOM   1191 N N   . ALA A 1 150 ? -4.396  -25.101 1.078   1.00 8.11  ? 152  ALA A N   1 
ATOM   1192 C CA  . ALA A 1 150 ? -5.379  -25.171 2.122   1.00 8.18  ? 152  ALA A CA  1 
ATOM   1193 C C   . ALA A 1 150 ? -6.746  -25.247 1.502   1.00 9.61  ? 152  ALA A C   1 
ATOM   1194 O O   . ALA A 1 150 ? -6.946  -24.766 0.352   1.00 9.06  ? 152  ALA A O   1 
ATOM   1195 C CB  . ALA A 1 150 ? -5.256  -23.997 3.077   1.00 8.77  ? 152  ALA A CB  1 
ATOM   1196 N N   . VAL A 1 151 ? -7.676  -25.863 2.211   1.00 9.92  ? 153  VAL A N   1 
ATOM   1197 C CA  . VAL A 1 151 ? -9.042  -26.110 1.692   1.00 10.64 ? 153  VAL A CA  1 
ATOM   1198 C C   . VAL A 1 151 ? -10.027 -25.711 2.726   1.00 11.08 ? 153  VAL A C   1 
ATOM   1199 O O   . VAL A 1 151 ? -9.853  -26.039 3.905   1.00 9.78  ? 153  VAL A O   1 
ATOM   1200 C CB  . VAL A 1 151 ? -9.264  -27.616 1.283   1.00 12.08 ? 153  VAL A CB  1 
ATOM   1201 C CG1 . VAL A 1 151 ? -10.692 -27.841 0.708   1.00 12.60 ? 153  VAL A CG1 1 
ATOM   1202 C CG2 . VAL A 1 151 ? -8.217  -28.075 0.294   1.00 13.13 ? 153  VAL A CG2 1 
ATOM   1203 N N   . VAL A 1 152 ? -11.104 -25.020 2.304   1.00 11.22 ? 154  VAL A N   1 
ATOM   1204 C CA  . VAL A 1 152 ? -12.233 -24.765 3.211   1.00 12.31 ? 154  VAL A CA  1 
ATOM   1205 C C   . VAL A 1 152 ? -13.452 -25.487 2.576   1.00 13.02 ? 154  VAL A C   1 
ATOM   1206 O O   . VAL A 1 152 ? -13.727 -25.332 1.370   1.00 11.54 ? 154  VAL A O   1 
ATOM   1207 C CB  . VAL A 1 152 ? -12.499 -23.261 3.548   1.00 14.05 ? 154  VAL A CB  1 
ATOM   1208 C CG1 . VAL A 1 152 ? -12.685 -22.397 2.283   1.00 14.97 ? 154  VAL A CG1 1 
ATOM   1209 C CG2 . VAL A 1 152 ? -13.683 -23.146 4.504   1.00 13.99 ? 154  VAL A CG2 1 
ATOM   1210 N N   . ASN A 1 153 ? -14.120 -26.283 3.382   1.00 12.26 ? 155  ASN A N   1 
ATOM   1211 C CA  . ASN A 1 153 ? -15.360 -26.960 2.999   1.00 14.72 ? 155  ASN A CA  1 
ATOM   1212 C C   . ASN A 1 153 ? -16.487 -26.338 3.797   1.00 14.29 ? 155  ASN A C   1 
ATOM   1213 O O   . ASN A 1 153 ? -16.447 -26.361 5.016   1.00 14.85 ? 155  ASN A O   1 
ATOM   1214 C CB  . ASN A 1 153 ? -15.313 -28.447 3.354   1.00 15.29 ? 155  ASN A CB  1 
ATOM   1215 C CG  . ASN A 1 153 ? -14.068 -29.203 2.977   1.00 19.59 ? 155  ASN A CG  1 
ATOM   1216 O OD1 . ASN A 1 153 ? -13.307 -29.679 3.835   1.00 21.27 ? 155  ASN A OD1 1 
ATOM   1217 N ND2 . ASN A 1 153 ? -13.858 -29.363 1.704   1.00 20.82 ? 155  ASN A ND2 1 
ATOM   1218 N N   . VAL A 1 154 ? -17.439 -25.783 3.133   1.00 14.24 ? 156  VAL A N   1 
ATOM   1219 C CA  . VAL A 1 154 ? -18.629 -25.171 3.736   1.00 16.14 ? 156  VAL A CA  1 
ATOM   1220 C C   . VAL A 1 154 ? -19.744 -26.233 3.749   1.00 15.42 ? 156  VAL A C   1 
ATOM   1221 O O   . VAL A 1 154 ? -20.147 -26.684 2.686   1.00 16.31 ? 156  VAL A O   1 
ATOM   1222 C CB  . VAL A 1 154 ? -19.075 -23.938 2.952   1.00 17.29 ? 156  VAL A CB  1 
ATOM   1223 C CG1 . VAL A 1 154 ? -20.328 -23.335 3.582   1.00 18.67 ? 156  VAL A CG1 1 
ATOM   1224 C CG2 . VAL A 1 154 ? -17.963 -22.900 2.919   1.00 18.27 ? 156  VAL A CG2 1 
ATOM   1225 N N   . ARG A 1 155 ? -20.181 -26.620 4.936   1.00 15.44 ? 157  ARG A N   1 
ATOM   1226 C CA  . ARG A 1 155 ? -21.127 -27.733 5.122   1.00 19.35 ? 157  ARG A CA  1 
ATOM   1227 C C   . ARG A 1 155 ? -22.150 -27.434 6.212   1.00 22.42 ? 157  ARG A C   1 
ATOM   1228 O O   . ARG A 1 155 ? -21.791 -26.917 7.280   1.00 22.54 ? 157  ARG A O   1 
ATOM   1229 C CB  . ARG A 1 155 ? -20.399 -29.013 5.536   1.00 21.26 ? 157  ARG A CB  1 
ATOM   1230 C CG  . ARG A 1 155 ? -19.400 -29.547 4.490   1.00 21.50 ? 157  ARG A CG  1 
ATOM   1231 C CD  . ARG A 1 155 ? -20.035 -30.004 3.203   1.00 25.83 ? 157  ARG A CD  1 
ATOM   1232 N NE  . ARG A 1 155 ? -19.038 -30.611 2.302   1.00 25.64 ? 157  ARG A NE  1 
ATOM   1233 C CZ  . ARG A 1 155 ? -18.276 -29.954 1.435   1.00 23.72 ? 157  ARG A CZ  1 
ATOM   1234 N NH1 . ARG A 1 155 ? -18.362 -28.627 1.322   1.00 17.84 ? 157  ARG A NH1 1 
ATOM   1235 N NH2 . ARG A 1 155 ? -17.389 -30.606 0.699   1.00 24.00 ? 157  ARG A NH2 1 
ATOM   1236 N N   . ALA A 1 156 ? -23.414 -27.803 5.956   1.00 23.78 ? 158  ALA A N   1 
ATOM   1237 C CA  . ALA A 1 156 ? -24.455 -27.704 6.977   1.00 27.21 ? 158  ALA A CA  1 
ATOM   1238 C C   . ALA A 1 156 ? -24.094 -28.445 8.284   1.00 29.29 ? 158  ALA A C   1 
ATOM   1239 O O   . ALA A 1 156 ? -24.397 -27.949 9.362   1.00 30.57 ? 158  ALA A O   1 
ATOM   1240 C CB  . ALA A 1 156 ? -25.766 -28.224 6.424   1.00 26.47 ? 158  ALA A CB  1 
ATOM   1241 N N   . LYS A 1 157 ? -23.457 -29.606 8.204   1.00 30.49 ? 159  LYS A N   1 
ATOM   1242 C CA  . LYS A 1 157 ? -23.044 -30.392 9.394   1.00 31.74 ? 159  LYS A CA  1 
ATOM   1243 C C   . LYS A 1 157 ? -21.880 -29.774 10.186  1.00 31.98 ? 159  LYS A C   1 
ATOM   1244 O O   . LYS A 1 157 ? -21.661 -30.120 11.362  1.00 34.15 ? 159  LYS A O   1 
ATOM   1245 C CB  . LYS A 1 157 ? -22.677 -31.820 8.937   1.00 36.02 ? 159  LYS A CB  1 
ATOM   1246 C CG  . LYS A 1 157 ? -22.089 -32.761 9.984   1.00 44.44 ? 159  LYS A CG  1 
ATOM   1247 C CD  . LYS A 1 157 ? -21.710 -34.112 9.352   1.00 50.67 ? 159  LYS A CD  1 
ATOM   1248 C CE  . LYS A 1 157 ? -21.380 -35.176 10.389  1.00 55.85 ? 159  LYS A CE  1 
ATOM   1249 N NZ  . LYS A 1 157 ? -21.227 -36.545 9.789   1.00 60.27 ? 159  LYS A NZ  1 
ATOM   1250 N N   . GLY A 1 158 ? -21.123 -28.871 9.567   1.00 28.76 ? 160  GLY A N   1 
ATOM   1251 C CA  . GLY A 1 158 ? -20.029 -28.187 10.237  1.00 25.85 ? 160  GLY A CA  1 
ATOM   1252 C C   . GLY A 1 158 ? -18.908 -27.932 9.241   1.00 22.23 ? 160  GLY A C   1 
ATOM   1253 O O   . GLY A 1 158 ? -18.523 -28.837 8.519   1.00 22.83 ? 160  GLY A O   1 
ATOM   1254 N N   . ASP A 1 159 ? -18.416 -26.719 9.190   1.00 19.14 ? 161  ASP A N   1 
ATOM   1255 C CA  . ASP A 1 159 ? -17.413 -26.332 8.186   1.00 16.97 ? 161  ASP A CA  1 
ATOM   1256 C C   . ASP A 1 159 ? -16.051 -26.921 8.581   1.00 15.61 ? 161  ASP A C   1 
ATOM   1257 O O   . ASP A 1 159 ? -15.805 -27.223 9.742   1.00 17.05 ? 161  ASP A O   1 
ATOM   1258 C CB  . ASP A 1 159 ? -17.335 -24.808 8.079   1.00 15.50 ? 161  ASP A CB  1 
ATOM   1259 C CG  . ASP A 1 159 ? -18.660 -24.143 7.741   1.00 19.95 ? 161  ASP A CG  1 
ATOM   1260 O OD1 . ASP A 1 159 ? -19.437 -24.737 6.971   1.00 19.93 ? 161  ASP A OD1 1 
ATOM   1261 O OD2 . ASP A 1 159 ? -18.914 -23.015 8.248   1.00 23.16 ? 161  ASP A OD2 1 
ATOM   1262 N N   . LYS A 1 160 ? -15.162 -27.065 7.596   1.00 14.53 ? 162  LYS A N   1 
ATOM   1263 C CA  . LYS A 1 160 ? -13.831 -27.639 7.877   1.00 12.61 ? 162  LYS A CA  1 
ATOM   1264 C C   . LYS A 1 160 ? -12.811 -26.757 7.162   1.00 12.68 ? 162  LYS A C   1 
ATOM   1265 O O   . LYS A 1 160 ? -13.077 -26.271 6.042   1.00 13.54 ? 162  LYS A O   1 
ATOM   1266 C CB  . LYS A 1 160 ? -13.695 -29.046 7.341   1.00 14.78 ? 162  LYS A CB  1 
ATOM   1267 C CG  . LYS A 1 160 ? -14.610 -30.058 8.015   1.00 20.12 ? 162  LYS A CG  1 
ATOM   1268 C CD  . LYS A 1 160 ? -14.564 -31.408 7.306   1.00 27.74 ? 162  LYS A CD  1 
ATOM   1269 C CE  . LYS A 1 160 ? -15.551 -31.457 6.157   1.00 39.10 ? 162  LYS A CE  1 
ATOM   1270 N NZ  . LYS A 1 160 ? -15.696 -32.824 5.554   1.00 43.97 ? 162  LYS A NZ  1 
ATOM   1271 N N   . ILE A 1 161 ? -11.651 -26.560 7.814   1.00 11.61 ? 163  ILE A N   1 
ATOM   1272 C CA  . ILE A 1 161 ? -10.498 -25.909 7.169   1.00 10.70 ? 163  ILE A CA  1 
ATOM   1273 C C   . ILE A 1 161 ? -9.341  -26.837 7.325   1.00 10.59 ? 163  ILE A C   1 
ATOM   1274 O O   . ILE A 1 161 ? -9.159  -27.404 8.375   1.00 11.26 ? 163  ILE A O   1 
ATOM   1275 C CB  . ILE A 1 161 ? -10.165 -24.539 7.788   1.00 11.09 ? 163  ILE A CB  1 
ATOM   1276 C CG1 . ILE A 1 161 ? -11.365 -23.594 7.625   1.00 11.72 ? 163  ILE A CG1 1 
ATOM   1277 C CG2 . ILE A 1 161 ? -8.896  -23.965 7.235   1.00 9.78  ? 163  ILE A CG2 1 
ATOM   1278 C CD1 . ILE A 1 161 ? -11.236 -22.324 8.407   1.00 14.60 ? 163  ILE A CD1 1 
ATOM   1279 N N   . ALA A 1 162 ? -8.528  -26.977 6.276   1.00 10.64 ? 164  ALA A N   1 
ATOM   1280 C CA  . ALA A 1 162 ? -7.369  -27.843 6.398   1.00 11.09 ? 164  ALA A CA  1 
ATOM   1281 C C   . ALA A 1 162 ? -6.172  -27.283 5.672   1.00 9.43  ? 164  ALA A C   1 
ATOM   1282 O O   . ALA A 1 162 ? -6.336  -26.692 4.623   1.00 10.78 ? 164  ALA A O   1 
ATOM   1283 C CB  . ALA A 1 162 ? -7.680  -29.237 5.925   1.00 11.81 ? 164  ALA A CB  1 
ATOM   1284 N N   . ILE A 1 163 ? -4.976  -27.482 6.248   1.00 7.18  ? 165  ILE A N   1 
ATOM   1285 C CA  . ILE A 1 163 ? -3.723  -27.279 5.531   1.00 7.84  ? 165  ILE A CA  1 
ATOM   1286 C C   . ILE A 1 163 ? -3.197  -28.646 5.043   1.00 8.77  ? 165  ILE A C   1 
ATOM   1287 O O   . ILE A 1 163 ? -2.950  -29.556 5.876   1.00 8.86  ? 165  ILE A O   1 
ATOM   1288 C CB  . ILE A 1 163 ? -2.645  -26.525 6.381   1.00 8.05  ? 165  ILE A CB  1 
ATOM   1289 C CG1 . ILE A 1 163 ? -3.075  -25.051 6.600   1.00 9.28  ? 165  ILE A CG1 1 
ATOM   1290 C CG2 . ILE A 1 163 ? -1.268  -26.570 5.601   1.00 8.37  ? 165  ILE A CG2 1 
ATOM   1291 C CD1 . ILE A 1 163 ? -2.103  -24.243 7.454   1.00 8.83  ? 165  ILE A CD1 1 
ATOM   1292 N N   . TRP A 1 164 ? -3.013  -28.779 3.730   1.00 7.20  ? 166  TRP A N   1 
ATOM   1293 C CA  . TRP A 1 164 ? -2.499  -29.968 3.092   1.00 7.31  ? 166  TRP A CA  1 
ATOM   1294 C C   . TRP A 1 164 ? -0.981  -29.851 2.961   1.00 8.97  ? 166  TRP A C   1 
ATOM   1295 O O   . TRP A 1 164 ? -0.443  -28.822 2.504   1.00 9.79  ? 166  TRP A O   1 
ATOM   1296 C CB  . TRP A 1 164 ? -3.039  -30.150 1.699   1.00 7.53  ? 166  TRP A CB  1 
ATOM   1297 C CG  . TRP A 1 164 ? -4.494  -30.504 1.626   1.00 8.95  ? 166  TRP A CG  1 
ATOM   1298 C CD1 . TRP A 1 164 ? -5.482  -30.238 2.529   1.00 10.41 ? 166  TRP A CD1 1 
ATOM   1299 C CD2 . TRP A 1 164 ? -5.105  -31.254 0.566   1.00 8.64  ? 166  TRP A CD2 1 
ATOM   1300 N NE1 . TRP A 1 164 ? -6.697  -30.732 2.057   1.00 11.09 ? 166  TRP A NE1 1 
ATOM   1301 C CE2 . TRP A 1 164 ? -6.489  -31.340 0.855   1.00 9.96  ? 166  TRP A CE2 1 
ATOM   1302 C CE3 . TRP A 1 164 ? -4.631  -31.784 -0.645  1.00 9.41  ? 166  TRP A CE3 1 
ATOM   1303 C CZ2 . TRP A 1 164 ? -7.376  -31.991 0.006   1.00 11.94 ? 166  TRP A CZ2 1 
ATOM   1304 C CZ3 . TRP A 1 164 ? -5.522  -32.449 -1.475  1.00 13.32 ? 166  TRP A CZ3 1 
ATOM   1305 C CH2 . TRP A 1 164 ? -6.867  -32.543 -1.146  1.00 12.94 ? 166  TRP A CH2 1 
ATOM   1306 N N   . THR A 1 165 ? -0.318  -30.920 3.316   1.00 7.65  ? 167  THR A N   1 
ATOM   1307 C CA  . THR A 1 165 ? 1.150   -31.002 3.184   1.00 8.39  ? 167  THR A CA  1 
ATOM   1308 C C   . THR A 1 165 ? 1.525   -32.254 2.315   1.00 10.48 ? 167  THR A C   1 
ATOM   1309 O O   . THR A 1 165 ? 0.691   -33.126 2.107   1.00 11.17 ? 167  THR A O   1 
ATOM   1310 C CB  . THR A 1 165 ? 1.892   -31.024 4.559   1.00 9.40  ? 167  THR A CB  1 
ATOM   1311 O OG1 . THR A 1 165 ? 1.981   -32.364 5.110   1.00 10.49 ? 167  THR A OG1 1 
ATOM   1312 C CG2 . THR A 1 165 ? 1.308   -30.116 5.593   1.00 8.55  ? 167  THR A CG2 1 
ATOM   1313 N N   . THR A 1 166 ? 2.766   -32.278 1.824   1.00 10.54 ? 168  THR A N   1 
ATOM   1314 C CA  . THR A 1 166 ? 3.170   -33.119 0.707   1.00 11.19 ? 168  THR A CA  1 
ATOM   1315 C C   . THR A 1 166 ? 3.515   -34.549 1.120   1.00 12.31 ? 168  THR A C   1 
ATOM   1316 O O   . THR A 1 166 ? 3.438   -35.428 0.283   1.00 13.84 ? 168  THR A O   1 
ATOM   1317 C CB  . THR A 1 166 ? 4.336   -32.476 -0.035  1.00 12.68 ? 168  THR A CB  1 
ATOM   1318 O OG1 . THR A 1 166 ? 4.548   -33.099 -1.302  1.00 15.44 ? 168  THR A OG1 1 
ATOM   1319 C CG2 . THR A 1 166 ? 5.661   -32.518 0.753   1.00 11.06 ? 168  THR A CG2 1 
ATOM   1320 N N   . GLU A 1 167 ? 3.924   -34.772 2.385   1.00 12.77 ? 169  GLU A N   1 
ATOM   1321 C CA  . GLU A 1 167 ? 4.541   -36.030 2.786   1.00 13.39 ? 169  GLU A CA  1 
ATOM   1322 C C   . GLU A 1 167 ? 4.150   -36.368 4.191   1.00 13.40 ? 169  GLU A C   1 
ATOM   1323 O O   . GLU A 1 167 ? 4.683   -35.774 5.115   1.00 15.17 ? 169  GLU A O   1 
ATOM   1324 C CB  . GLU A 1 167 ? 6.077   -35.927 2.635   1.00 14.77 ? 169  GLU A CB  1 
ATOM   1325 C CG  . GLU A 1 167 ? 6.857   -37.173 3.059   1.00 15.37 ? 169  GLU A CG  1 
ATOM   1326 C CD  . GLU A 1 167 ? 6.328   -38.477 2.495   1.00 18.03 ? 169  GLU A CD  1 
ATOM   1327 O OE1 . GLU A 1 167 ? 6.458   -38.713 1.274   1.00 18.84 ? 169  GLU A OE1 1 
ATOM   1328 O OE2 . GLU A 1 167 ? 5.752   -39.250 3.286   1.00 19.90 ? 169  GLU A OE2 1 
ATOM   1329 N N   . CYS A 1 168 ? 3.230   -37.299 4.371   1.00 13.06 ? 170  CYS A N   1 
ATOM   1330 C CA  . CYS A 1 168 ? 2.701   -37.595 5.712   1.00 16.00 ? 170  CYS A CA  1 
ATOM   1331 C C   . CYS A 1 168 ? 3.761   -38.202 6.635   1.00 17.33 ? 170  CYS A C   1 
ATOM   1332 O O   . CYS A 1 168 ? 3.529   -38.192 7.859   1.00 18.11 ? 170  CYS A O   1 
ATOM   1333 C CB  . CYS A 1 168 ? 1.451   -38.465 5.602   1.00 16.58 ? 170  CYS A CB  1 
ATOM   1334 S SG  . CYS A 1 168 ? 1.769   -40.104 4.909   1.00 21.73 ? 170  CYS A SG  1 
ATOM   1335 N N   . GLU A 1 169 ? 4.919   -38.716 6.095   1.00 17.25 ? 171  GLU A N   1 
ATOM   1336 C CA  A GLU A 1 169 ? 6.018   -39.323 6.866   0.50 18.33 ? 171  GLU A CA  1 
ATOM   1337 C CA  B GLU A 1 169 ? 5.957   -39.280 6.959   0.50 17.98 ? 171  GLU A CA  1 
ATOM   1338 C C   . GLU A 1 169 ? 7.132   -38.336 7.237   1.00 19.01 ? 171  GLU A C   1 
ATOM   1339 O O   . GLU A 1 169 ? 8.117   -38.747 7.887   1.00 21.13 ? 171  GLU A O   1 
ATOM   1340 C CB  A GLU A 1 169 ? 6.663   -40.485 6.066   0.50 21.44 ? 171  GLU A CB  1 
ATOM   1341 C CB  B GLU A 1 169 ? 6.448   -40.622 6.406   0.50 19.95 ? 171  GLU A CB  1 
ATOM   1342 C CG  A GLU A 1 169 ? 5.713   -41.625 5.728   0.50 25.49 ? 171  GLU A CG  1 
ATOM   1343 C CG  B GLU A 1 169 ? 5.324   -41.626 6.241   0.50 19.95 ? 171  GLU A CG  1 
ATOM   1344 C CD  A GLU A 1 169 ? 5.560   -42.729 6.762   0.50 28.99 ? 171  GLU A CD  1 
ATOM   1345 C CD  B GLU A 1 169 ? 5.850   -42.936 5.694   0.50 24.28 ? 171  GLU A CD  1 
ATOM   1346 O OE1 A GLU A 1 169 ? 6.286   -42.710 7.780   0.50 30.63 ? 171  GLU A OE1 1 
ATOM   1347 O OE1 B GLU A 1 169 ? 6.648   -43.570 6.409   0.50 26.53 ? 171  GLU A OE1 1 
ATOM   1348 O OE2 A GLU A 1 169 ? 4.710   -43.622 6.546   0.50 26.91 ? 171  GLU A OE2 1 
ATOM   1349 O OE2 B GLU A 1 169 ? 5.489   -43.322 4.560   0.50 24.06 ? 171  GLU A OE2 1 
ATOM   1350 N N   . ASN A 1 170 ? 7.039   -37.062 6.795   1.00 16.14 ? 172  ASN A N   1 
ATOM   1351 C CA  . ASN A 1 170 ? 7.949   -36.018 7.234   1.00 16.10 ? 172  ASN A CA  1 
ATOM   1352 C C   . ASN A 1 170 ? 7.529   -35.478 8.615   1.00 17.48 ? 172  ASN A C   1 
ATOM   1353 O O   . ASN A 1 170 ? 6.935   -34.386 8.753   1.00 16.59 ? 172  ASN A O   1 
ATOM   1354 C CB  . ASN A 1 170 ? 8.067   -34.878 6.214   1.00 19.71 ? 172  ASN A CB  1 
ATOM   1355 C CG  . ASN A 1 170 ? 8.835   -35.141 4.949   1.00 26.04 ? 172  ASN A CG  1 
ATOM   1356 O OD1 . ASN A 1 170 ? 9.630   -36.108 4.865   1.00 29.21 ? 172  ASN A OD1 1 
ATOM   1357 N ND2 . ASN A 1 170 ? 8.635   -34.272 3.918   1.00 24.35 ? 172  ASN A ND2 1 
ATOM   1358 N N   . ARG A 1 171 ? 7.872   -36.236 9.660   1.00 18.07 ? 173  ARG A N   1 
ATOM   1359 C CA  . ARG A 1 171 ? 7.410   -35.982 11.032  1.00 19.20 ? 173  ARG A CA  1 
ATOM   1360 C C   . ARG A 1 171 ? 7.738   -34.593 11.533  1.00 17.22 ? 173  ARG A C   1 
ATOM   1361 O O   . ARG A 1 171 ? 6.849   -33.910 12.070  1.00 17.36 ? 173  ARG A O   1 
ATOM   1362 C CB  . ARG A 1 171 ? 8.015   -37.030 12.007  1.00 23.26 ? 173  ARG A CB  1 
ATOM   1363 C CG  . ARG A 1 171 ? 7.712   -36.705 13.482  1.00 32.10 ? 173  ARG A CG  1 
ATOM   1364 C CD  . ARG A 1 171 ? 8.163   -37.813 14.421  1.00 41.84 ? 173  ARG A CD  1 
ATOM   1365 N NE  . ARG A 1 171 ? 9.627   -37.972 14.494  1.00 51.07 ? 173  ARG A NE  1 
ATOM   1366 C CZ  . ARG A 1 171 ? 10.454  -37.209 15.206  1.00 59.11 ? 173  ARG A CZ  1 
ATOM   1367 N NH1 . ARG A 1 171 ? 9.981   -36.203 15.941  1.00 61.91 ? 173  ARG A NH1 1 
ATOM   1368 N NH2 . ARG A 1 171 ? 11.762  -37.449 15.196  1.00 60.67 ? 173  ARG A NH2 1 
ATOM   1369 N N   . GLU A 1 172 ? 9.005   -34.164 11.382  1.00 16.78 ? 174  GLU A N   1 
ATOM   1370 C CA  . GLU A 1 172 ? 9.432   -32.854 11.886  1.00 16.91 ? 174  GLU A CA  1 
ATOM   1371 C C   . GLU A 1 172 ? 8.707   -31.716 11.165  1.00 15.49 ? 174  GLU A C   1 
ATOM   1372 O O   . GLU A 1 172 ? 8.197   -30.792 11.812  1.00 14.60 ? 174  GLU A O   1 
ATOM   1373 C CB  . GLU A 1 172 ? 10.945  -32.662 11.765  1.00 21.32 ? 174  GLU A CB  1 
ATOM   1374 C CG  . GLU A 1 172 ? 11.707  -33.442 12.831  1.00 32.83 ? 174  GLU A CG  1 
ATOM   1375 C CD  . GLU A 1 172 ? 12.963  -34.143 12.355  1.00 50.92 ? 174  GLU A CD  1 
ATOM   1376 O OE1 . GLU A 1 172 ? 12.973  -35.398 12.384  1.00 55.21 ? 174  GLU A OE1 1 
ATOM   1377 O OE2 . GLU A 1 172 ? 13.929  -33.452 11.949  1.00 56.54 ? 174  GLU A OE2 1 
ATOM   1378 N N   . ALA A 1 173 ? 8.631   -31.793 9.832   1.00 13.39 ? 175  ALA A N   1 
ATOM   1379 C CA  . ALA A 1 173 ? 7.907   -30.764 9.065   1.00 14.18 ? 175  ALA A CA  1 
ATOM   1380 C C   . ALA A 1 173 ? 6.435   -30.724 9.461   1.00 13.70 ? 175  ALA A C   1 
ATOM   1381 O O   . ALA A 1 173 ? 5.883   -29.641 9.770   1.00 11.95 ? 175  ALA A O   1 
ATOM   1382 C CB  . ALA A 1 173 ? 8.067   -31.051 7.575   1.00 13.92 ? 175  ALA A CB  1 
ATOM   1383 N N   . VAL A 1 174 ? 5.757   -31.878 9.461   1.00 11.98 ? 176  VAL A N   1 
ATOM   1384 C CA  . VAL A 1 174 ? 4.332   -31.925 9.698   1.00 11.91 ? 176  VAL A CA  1 
ATOM   1385 C C   . VAL A 1 174 ? 4.026   -31.390 11.114  1.00 11.02 ? 176  VAL A C   1 
ATOM   1386 O O   . VAL A 1 174 ? 3.070   -30.614 11.282  1.00 11.11 ? 176  VAL A O   1 
ATOM   1387 C CB  . VAL A 1 174 ? 3.797   -33.371 9.528   1.00 12.19 ? 176  VAL A CB  1 
ATOM   1388 C CG1 . VAL A 1 174 ? 2.409   -33.497 10.092  1.00 15.43 ? 176  VAL A CG1 1 
ATOM   1389 C CG2 . VAL A 1 174 ? 3.837   -33.811 8.051   1.00 12.89 ? 176  VAL A CG2 1 
ATOM   1390 N N   . THR A 1 175 ? 4.846   -31.794 12.108  1.00 11.70 ? 177  THR A N   1 
ATOM   1391 C CA  A THR A 1 175 ? 4.513   -31.392 13.479  0.50 11.89 ? 177  THR A CA  1 
ATOM   1392 C CA  B THR A 1 175 ? 4.592   -31.386 13.489  0.50 11.94 ? 177  THR A CA  1 
ATOM   1393 C C   . THR A 1 175 ? 4.793   -29.894 13.644  1.00 11.93 ? 177  THR A C   1 
ATOM   1394 O O   . THR A 1 175 ? 3.996   -29.215 14.293  1.00 12.48 ? 177  THR A O   1 
ATOM   1395 C CB  A THR A 1 175 ? 5.157   -32.310 14.521  0.50 12.91 ? 177  THR A CB  1 
ATOM   1396 C CB  B THR A 1 175 ? 5.495   -32.178 14.418  0.50 13.00 ? 177  THR A CB  1 
ATOM   1397 O OG1 A THR A 1 175 ? 6.572   -32.342 14.362  0.50 14.44 ? 177  THR A OG1 1 
ATOM   1398 O OG1 B THR A 1 175 ? 5.220   -33.573 14.243  0.50 12.83 ? 177  THR A OG1 1 
ATOM   1399 C CG2 A THR A 1 175 ? 4.566   -33.720 14.507  0.50 11.85 ? 177  THR A CG2 1 
ATOM   1400 C CG2 B THR A 1 175 ? 5.300   -31.793 15.866  0.50 13.64 ? 177  THR A CG2 1 
ATOM   1401 N N   . HIS A 1 176 ? 5.882   -29.349 13.065  1.00 12.86 ? 178  HIS A N   1 
ATOM   1402 C CA  . HIS A 1 176 ? 6.126   -27.900 13.128  1.00 11.83 ? 178  HIS A CA  1 
ATOM   1403 C C   . HIS A 1 176 ? 4.990   -27.110 12.515  1.00 10.74 ? 178  HIS A C   1 
ATOM   1404 O O   . HIS A 1 176 ? 4.513   -26.142 13.094  1.00 10.56 ? 178  HIS A O   1 
ATOM   1405 C CB  . HIS A 1 176 ? 7.441   -27.513 12.460  1.00 14.37 ? 178  HIS A CB  1 
ATOM   1406 C CG  . HIS A 1 176 ? 7.720   -26.051 12.565  1.00 15.71 ? 178  HIS A CG  1 
ATOM   1407 N ND1 . HIS A 1 176 ? 8.146   -25.472 13.783  1.00 18.75 ? 178  HIS A ND1 1 
ATOM   1408 C CD2 . HIS A 1 176 ? 7.626   -25.073 11.641  1.00 16.52 ? 178  HIS A CD2 1 
ATOM   1409 C CE1 . HIS A 1 176 ? 8.279   -24.177 13.533  1.00 18.73 ? 178  HIS A CE1 1 
ATOM   1410 N NE2 . HIS A 1 176 ? 8.011   -23.895 12.248  1.00 16.91 ? 178  HIS A NE2 1 
ATOM   1411 N N   . ILE A 1 177 ? 4.517   -27.523 11.327  1.00 11.00 ? 179  ILE A N   1 
ATOM   1412 C CA  . ILE A 1 177 ? 3.407   -26.858 10.704  1.00 9.29  ? 179  ILE A CA  1 
ATOM   1413 C C   . ILE A 1 177 ? 2.180   -26.859 11.643  1.00 9.84  ? 179  ILE A C   1 
ATOM   1414 O O   . ILE A 1 177 ? 1.545   -25.845 11.827  1.00 10.87 ? 179  ILE A O   1 
ATOM   1415 C CB  . ILE A 1 177 ? 3.085   -27.522 9.353   1.00 10.62 ? 179  ILE A CB  1 
ATOM   1416 C CG1 . ILE A 1 177 ? 4.237   -27.271 8.352   1.00 10.35 ? 179  ILE A CG1 1 
ATOM   1417 C CG2 . ILE A 1 177 ? 1.759   -26.998 8.780   1.00 9.70  ? 179  ILE A CG2 1 
ATOM   1418 C CD1 . ILE A 1 177 ? 4.205   -28.156 7.130   1.00 12.43 ? 179  ILE A CD1 1 
ATOM   1419 N N   . GLY A 1 178 ? 1.827   -28.004 12.201  1.00 9.53  ? 180  GLY A N   1 
ATOM   1420 C CA  . GLY A 1 178 ? 0.666   -28.090 13.089  1.00 9.51  ? 180  GLY A CA  1 
ATOM   1421 C C   . GLY A 1 178 ? 0.777   -27.161 14.292  1.00 11.17 ? 180  GLY A C   1 
ATOM   1422 O O   . GLY A 1 178 ? -0.177  -26.430 14.615  1.00 10.69 ? 180  GLY A O   1 
ATOM   1423 N N   . ARG A 1 179 ? 1.950   -27.179 14.954  1.00 10.61 ? 181  ARG A N   1 
ATOM   1424 C CA  . ARG A 1 179 ? 2.127   -26.335 16.149  1.00 10.70 ? 181  ARG A CA  1 
ATOM   1425 C C   . ARG A 1 179 ? 1.961   -24.840 15.843  1.00 11.92 ? 181  ARG A C   1 
ATOM   1426 O O   . ARG A 1 179 ? 1.233   -24.104 16.516  1.00 12.96 ? 181  ARG A O   1 
ATOM   1427 C CB  . ARG A 1 179 ? 3.449   -26.656 16.791  1.00 14.40 ? 181  ARG A CB  1 
ATOM   1428 C CG  . ARG A 1 179 ? 3.509   -28.023 17.400  1.00 18.19 ? 181  ARG A CG  1 
ATOM   1429 C CD  . ARG A 1 179 ? 4.704   -28.081 18.282  1.00 22.76 ? 181  ARG A CD  1 
ATOM   1430 N NE  . ARG A 1 179 ? 5.126   -29.433 18.646  1.00 28.59 ? 181  ARG A NE  1 
ATOM   1431 C CZ  . ARG A 1 179 ? 4.505   -30.245 19.512  1.00 33.12 ? 181  ARG A CZ  1 
ATOM   1432 N NH1 . ARG A 1 179 ? 5.005   -31.440 19.780  1.00 35.20 ? 181  ARG A NH1 1 
ATOM   1433 N NH2 . ARG A 1 179 ? 3.368   -29.869 20.101  1.00 28.24 ? 181  ARG A NH2 1 
ATOM   1434 N N   . VAL A 1 180 ? 2.642   -24.379 14.795  1.00 11.54 ? 182  VAL A N   1 
ATOM   1435 C CA  . VAL A 1 180 ? 2.578   -22.975 14.386  1.00 11.11 ? 182  VAL A CA  1 
ATOM   1436 C C   . VAL A 1 180 ? 1.182   -22.622 13.909  1.00 10.38 ? 182  VAL A C   1 
ATOM   1437 O O   . VAL A 1 180 ? 0.707   -21.541 14.210  1.00 10.75 ? 182  VAL A O   1 
ATOM   1438 C CB  . VAL A 1 180 ? 3.662   -22.657 13.348  1.00 11.73 ? 182  VAL A CB  1 
ATOM   1439 C CG1 . VAL A 1 180 ? 3.514   -21.230 12.854  1.00 14.00 ? 182  VAL A CG1 1 
ATOM   1440 C CG2 . VAL A 1 180 ? 5.036   -22.878 13.915  1.00 12.83 ? 182  VAL A CG2 1 
ATOM   1441 N N   . TYR A 1 181 ? 0.511   -23.521 13.205  1.00 10.46 ? 183  TYR A N   1 
ATOM   1442 C CA  . TYR A 1 181 ? -0.848  -23.263 12.718  1.00 10.65 ? 183  TYR A CA  1 
ATOM   1443 C C   . TYR A 1 181 ? -1.820  -23.064 13.880  1.00 11.45 ? 183  TYR A C   1 
ATOM   1444 O O   . TYR A 1 181 ? -2.573  -22.078 13.940  1.00 10.80 ? 183  TYR A O   1 
ATOM   1445 C CB  . TYR A 1 181 ? -1.278  -24.393 11.819  1.00 10.03 ? 183  TYR A CB  1 
ATOM   1446 C CG  . TYR A 1 181 ? -2.619  -24.249 11.152  1.00 8.90  ? 183  TYR A CG  1 
ATOM   1447 C CD1 . TYR A 1 181 ? -3.087  -23.006 10.732  1.00 9.37  ? 183  TYR A CD1 1 
ATOM   1448 C CD2 . TYR A 1 181 ? -3.401  -25.355 10.889  1.00 8.28  ? 183  TYR A CD2 1 
ATOM   1449 C CE1 . TYR A 1 181 ? -4.285  -22.888 10.029  1.00 9.34  ? 183  TYR A CE1 1 
ATOM   1450 C CE2 . TYR A 1 181 ? -4.566  -25.254 10.167  1.00 8.28  ? 183  TYR A CE2 1 
ATOM   1451 C CZ  . TYR A 1 181 ? -5.048  -24.020 9.802   1.00 10.87 ? 183  TYR A CZ  1 
ATOM   1452 O OH  . TYR A 1 181 ? -6.219  -24.002 9.092   1.00 12.50 ? 183  TYR A OH  1 
ATOM   1453 N N   . LYS A 1 182 ? -1.757  -23.990 14.822  1.00 11.96 ? 184  LYS A N   1 
ATOM   1454 C CA  . LYS A 1 182 ? -2.541  -23.882 16.060  1.00 11.58 ? 184  LYS A CA  1 
ATOM   1455 C C   . LYS A 1 182 ? -2.238  -22.539 16.795  1.00 13.26 ? 184  LYS A C   1 
ATOM   1456 O O   . LYS A 1 182 ? -3.168  -21.853 17.175  1.00 12.14 ? 184  LYS A O   1 
ATOM   1457 C CB  . LYS A 1 182 ? -2.244  -25.055 16.950  1.00 12.17 ? 184  LYS A CB  1 
ATOM   1458 C CG  . LYS A 1 182 ? -3.039  -25.029 18.247  1.00 13.23 ? 184  LYS A CG  1 
ATOM   1459 C CD  . LYS A 1 182 ? -3.169  -26.365 18.875  1.00 13.79 ? 184  LYS A CD  1 
ATOM   1460 C CE  . LYS A 1 182 ? -3.595  -26.244 20.347  1.00 12.85 ? 184  LYS A CE  1 
ATOM   1461 N NZ  . LYS A 1 182 ? -3.737  -27.566 20.963  1.00 13.73 ? 184  LYS A NZ  1 
ATOM   1462 N N   . GLU A 1 183 ? -0.964  -22.177 16.963  1.00 13.71 ? 185  GLU A N   1 
ATOM   1463 C CA  . GLU A 1 183 ? -0.532  -20.918 17.595  1.00 15.20 ? 185  GLU A CA  1 
ATOM   1464 C C   . GLU A 1 183 ? -1.101  -19.723 16.864  1.00 15.88 ? 185  GLU A C   1 
ATOM   1465 O O   . GLU A 1 183 ? -1.673  -18.812 17.473  1.00 16.92 ? 185  GLU A O   1 
ATOM   1466 C CB  . GLU A 1 183 ? 1.006   -20.974 17.641  1.00 18.79 ? 185  GLU A CB  1 
ATOM   1467 C CG  . GLU A 1 183 ? 1.807   -19.780 17.945  1.00 27.16 ? 185  GLU A CG  1 
ATOM   1468 C CD  . GLU A 1 183 ? 3.238   -20.110 17.530  1.00 26.78 ? 185  GLU A CD  1 
ATOM   1469 O OE1 . GLU A 1 183 ? 3.881   -19.177 17.031  1.00 29.32 ? 185  GLU A OE1 1 
ATOM   1470 O OE2 . GLU A 1 183 ? 3.714   -21.258 17.701  1.00 24.94 ? 185  GLU A OE2 1 
ATOM   1471 N N   . ARG A 1 184 ? -0.991  -19.719 15.529  1.00 12.89 ? 186  ARG A N   1 
ATOM   1472 C CA  . ARG A 1 184 ? -1.526  -18.624 14.699  1.00 13.31 ? 186  ARG A CA  1 
ATOM   1473 C C   . ARG A 1 184 ? -3.045  -18.507 14.658  1.00 14.70 ? 186  ARG A C   1 
ATOM   1474 O O   . ARG A 1 184 ? -3.575  -17.386 14.572  1.00 16.01 ? 186  ARG A O   1 
ATOM   1475 C CB  . ARG A 1 184 ? -0.947  -18.744 13.272  1.00 13.21 ? 186  ARG A CB  1 
ATOM   1476 C CG  . ARG A 1 184 ? 0.531   -18.405 13.239  1.00 16.70 ? 186  ARG A CG  1 
ATOM   1477 C CD  . ARG A 1 184 ? 0.861   -16.926 13.348  1.00 17.94 ? 186  ARG A CD  1 
ATOM   1478 N NE  . ARG A 1 184 ? 0.297   -16.222 12.218  1.00 14.70 ? 186  ARG A NE  1 
ATOM   1479 C CZ  . ARG A 1 184 ? 0.957   -15.822 11.129  1.00 13.89 ? 186  ARG A CZ  1 
ATOM   1480 N NH1 . ARG A 1 184 ? 2.259   -16.051 11.006  1.00 13.71 ? 186  ARG A NH1 1 
ATOM   1481 N NH2 . ARG A 1 184 ? 0.320   -15.208 10.165  1.00 14.17 ? 186  ARG A NH2 1 
ATOM   1482 N N   . LEU A 1 185 ? -3.766  -19.640 14.726  1.00 14.65 ? 187  LEU A N   1 
ATOM   1483 C CA  . LEU A 1 185 ? -5.191  -19.636 14.935  1.00 14.01 ? 187  LEU A CA  1 
ATOM   1484 C C   . LEU A 1 185 ? -5.604  -19.122 16.317  1.00 16.51 ? 187  LEU A C   1 
ATOM   1485 O O   . LEU A 1 185 ? -6.765  -18.698 16.482  1.00 18.29 ? 187  LEU A O   1 
ATOM   1486 C CB  . LEU A 1 185 ? -5.766  -21.042 14.722  1.00 13.18 ? 187  LEU A CB  1 
ATOM   1487 C CG  . LEU A 1 185 ? -5.742  -21.648 13.318  1.00 13.61 ? 187  LEU A CG  1 
ATOM   1488 C CD1 . LEU A 1 185 ? -6.040  -23.135 13.353  1.00 13.88 ? 187  LEU A CD1 1 
ATOM   1489 C CD2 . LEU A 1 185 ? -6.636  -20.890 12.354  1.00 14.81 ? 187  LEU A CD2 1 
ATOM   1490 N N   . GLY A 1 186 ? -4.701  -19.186 17.300  1.00 15.24 ? 188  GLY A N   1 
ATOM   1491 C CA  . GLY A 1 186 ? -5.015  -18.714 18.629  1.00 16.09 ? 188  GLY A CA  1 
ATOM   1492 C C   . GLY A 1 186 ? -5.864  -19.682 19.399  1.00 15.43 ? 188  GLY A C   1 
ATOM   1493 O O   . GLY A 1 186 ? -6.584  -19.255 20.285  1.00 16.28 ? 188  GLY A O   1 
ATOM   1494 N N   . LEU A 1 187 ? -5.788  -20.988 19.083  1.00 14.01 ? 189  LEU A N   1 
ATOM   1495 C CA  . LEU A 1 187 ? -6.663  -21.952 19.723  1.00 14.08 ? 189  LEU A CA  1 
ATOM   1496 C C   . LEU A 1 187 ? -6.127  -22.181 21.125  1.00 16.07 ? 189  LEU A C   1 
ATOM   1497 O O   . LEU A 1 187 ? -4.900  -22.260 21.328  1.00 16.90 ? 189  LEU A O   1 
ATOM   1498 C CB  . LEU A 1 187 ? -6.661  -23.306 19.034  1.00 15.14 ? 189  LEU A CB  1 
ATOM   1499 C CG  . LEU A 1 187 ? -7.129  -23.324 17.575  1.00 16.42 ? 189  LEU A CG  1 
ATOM   1500 C CD1 . LEU A 1 187 ? -7.076  -24.754 16.980  1.00 16.25 ? 189  LEU A CD1 1 
ATOM   1501 C CD2 . LEU A 1 187 ? -8.533  -22.843 17.431  1.00 18.65 ? 189  LEU A CD2 1 
ATOM   1502 N N   . PRO A 1 188 ? -7.022  -22.290 22.093  1.00 17.29 ? 190  PRO A N   1 
ATOM   1503 C CA  . PRO A 1 188 ? -6.590  -22.699 23.426  1.00 16.41 ? 190  PRO A CA  1 
ATOM   1504 C C   . PRO A 1 188 ? -5.812  -24.025 23.389  1.00 12.90 ? 190  PRO A C   1 
ATOM   1505 O O   . PRO A 1 188 ? -6.126  -24.868 22.604  1.00 12.74 ? 190  PRO A O   1 
ATOM   1506 C CB  . PRO A 1 188 ? -7.909  -22.853 24.167  1.00 19.16 ? 190  PRO A CB  1 
ATOM   1507 C CG  . PRO A 1 188 ? -8.863  -21.904 23.446  1.00 21.16 ? 190  PRO A CG  1 
ATOM   1508 C CD  . PRO A 1 188 ? -8.478  -22.027 22.046  1.00 18.99 ? 190  PRO A CD  1 
ATOM   1509 N N   . PRO A 1 189 ? -4.797  -24.199 24.252  1.00 12.35 ? 191  PRO A N   1 
ATOM   1510 C CA  . PRO A 1 189 ? -4.072  -25.491 24.298  1.00 12.11 ? 191  PRO A CA  1 
ATOM   1511 C C   . PRO A 1 189 ? -4.943  -26.727 24.323  1.00 12.73 ? 191  PRO A C   1 
ATOM   1512 O O   . PRO A 1 189 ? -4.602  -27.739 23.672  1.00 13.10 ? 191  PRO A O   1 
ATOM   1513 C CB  . PRO A 1 189 ? -3.220  -25.341 25.552  1.00 12.72 ? 191  PRO A CB  1 
ATOM   1514 C CG  . PRO A 1 189 ? -2.956  -23.843 25.627  1.00 13.18 ? 191  PRO A CG  1 
ATOM   1515 C CD  . PRO A 1 189 ? -4.247  -23.232 25.213  1.00 12.41 ? 191  PRO A CD  1 
ATOM   1516 N N   . LYS A 1 190 ? -6.067  -26.689 25.058  1.00 13.02 ? 192  LYS A N   1 
ATOM   1517 C CA  . LYS A 1 190 ? -6.918  -27.870 25.199  1.00 13.94 ? 192  LYS A CA  1 
ATOM   1518 C C   . LYS A 1 190 ? -7.686  -28.298 23.937  1.00 15.41 ? 192  LYS A C   1 
ATOM   1519 O O   . LYS A 1 190 ? -8.193  -29.414 23.892  1.00 16.72 ? 192  LYS A O   1 
ATOM   1520 C CB  . LYS A 1 190 ? -7.920  -27.667 26.352  1.00 17.45 ? 192  LYS A CB  1 
ATOM   1521 C CG  . LYS A 1 190 ? -8.979  -26.612 26.023  1.00 23.91 ? 192  LYS A CG  1 
ATOM   1522 C CD  . LYS A 1 190 ? -9.964  -26.310 27.160  1.00 30.77 ? 192  LYS A CD  1 
ATOM   1523 C CE  . LYS A 1 190 ? -10.824 -27.486 27.473  1.00 37.93 ? 192  LYS A CE  1 
ATOM   1524 N NZ  . LYS A 1 190 ? -11.924 -27.168 28.451  1.00 44.82 ? 192  LYS A NZ  1 
ATOM   1525 N N   . ILE A 1 191 ? -7.771  -27.431 22.962  1.00 14.32 ? 193  ILE A N   1 
ATOM   1526 C CA  . ILE A 1 191 ? -8.413  -27.729 21.676  1.00 16.10 ? 193  ILE A CA  1 
ATOM   1527 C C   . ILE A 1 191 ? -7.428  -28.398 20.783  1.00 16.85 ? 193  ILE A C   1 
ATOM   1528 O O   . ILE A 1 191 ? -6.605  -27.735 20.178  1.00 17.17 ? 193  ILE A O   1 
ATOM   1529 C CB  . ILE A 1 191 ? -9.001  -26.456 21.021  1.00 17.67 ? 193  ILE A CB  1 
ATOM   1530 C CG1 . ILE A 1 191 ? -10.014 -25.737 21.965  1.00 20.28 ? 193  ILE A CG1 1 
ATOM   1531 C CG2 . ILE A 1 191 ? -9.706  -26.823 19.670  1.00 18.96 ? 193  ILE A CG2 1 
ATOM   1532 C CD1 . ILE A 1 191 ? -11.113 -26.524 22.424  1.00 22.72 ? 193  ILE A CD1 1 
ATOM   1533 N N   . VAL A 1 192 ? -7.496  -29.729 20.694  1.00 17.86 ? 194  VAL A N   1 
ATOM   1534 C CA  . VAL A 1 192 ? -6.506  -30.492 19.970  1.00 19.30 ? 194  VAL A CA  1 
ATOM   1535 C C   . VAL A 1 192 ? -6.850  -30.490 18.505  1.00 19.66 ? 194  VAL A C   1 
ATOM   1536 O O   . VAL A 1 192 ? -8.016  -30.660 18.167  1.00 20.60 ? 194  VAL A O   1 
ATOM   1537 C CB  . VAL A 1 192 ? -6.379  -31.947 20.498  1.00 23.98 ? 194  VAL A CB  1 
ATOM   1538 C CG1 . VAL A 1 192 ? -6.207  -31.999 22.027  1.00 26.28 ? 194  VAL A CG1 1 
ATOM   1539 C CG2 . VAL A 1 192 ? -7.503  -32.829 20.025  1.00 28.79 ? 194  VAL A CG2 1 
ATOM   1540 N N   . ILE A 1 193 ? -5.851  -30.290 17.636  1.00 17.54 ? 195  ILE A N   1 
ATOM   1541 C CA  . ILE A 1 193 ? -6.026  -30.537 16.199  1.00 15.88 ? 195  ILE A CA  1 
ATOM   1542 C C   . ILE A 1 193 ? -5.204  -31.745 15.751  1.00 13.60 ? 195  ILE A C   1 
ATOM   1543 O O   . ILE A 1 193 ? -4.185  -32.067 16.323  1.00 13.55 ? 195  ILE A O   1 
ATOM   1544 C CB  . ILE A 1 193 ? -5.741  -29.274 15.404  1.00 16.46 ? 195  ILE A CB  1 
ATOM   1545 C CG1 . ILE A 1 193 ? -4.244  -28.922 15.407  1.00 15.78 ? 195  ILE A CG1 1 
ATOM   1546 C CG2 . ILE A 1 193 ? -6.589  -28.113 15.944  1.00 18.68 ? 195  ILE A CG2 1 
ATOM   1547 C CD1 . ILE A 1 193 ? -3.798  -27.892 14.404  1.00 16.11 ? 195  ILE A CD1 1 
ATOM   1548 N N   . GLY A 1 194 ? -5.681  -32.418 14.700  1.00 12.77 ? 196  GLY A N   1 
ATOM   1549 C CA  . GLY A 1 194 ? -5.107  -33.661 14.243  1.00 12.46 ? 196  GLY A CA  1 
ATOM   1550 C C   . GLY A 1 194 ? -4.676  -33.648 12.787  1.00 12.86 ? 196  GLY A C   1 
ATOM   1551 O O   . GLY A 1 194 ? -5.276  -32.941 11.959  1.00 13.11 ? 196  GLY A O   1 
ATOM   1552 N N   . TYR A 1 195 ? -3.663  -34.430 12.495  1.00 12.76 ? 197  TYR A N   1 
ATOM   1553 C CA  . TYR A 1 195 ? -3.164  -34.659 11.132  1.00 12.83 ? 197  TYR A CA  1 
ATOM   1554 C C   . TYR A 1 195 ? -3.492  -36.054 10.694  1.00 15.91 ? 197  TYR A C   1 
ATOM   1555 O O   . TYR A 1 195 ? -3.258  -37.014 11.438  1.00 16.97 ? 197  TYR A O   1 
ATOM   1556 C CB  . TYR A 1 195 ? -1.665  -34.444 11.072  1.00 11.75 ? 197  TYR A CB  1 
ATOM   1557 C CG  . TYR A 1 195 ? -1.052  -34.500 9.698   1.00 12.22 ? 197  TYR A CG  1 
ATOM   1558 C CD1 . TYR A 1 195 ? -0.627  -35.699 9.161   1.00 12.77 ? 197  TYR A CD1 1 
ATOM   1559 C CD2 . TYR A 1 195 ? -0.883  -33.342 8.937   1.00 9.56  ? 197  TYR A CD2 1 
ATOM   1560 C CE1 . TYR A 1 195 ? -0.030  -35.754 7.915   1.00 12.87 ? 197  TYR A CE1 1 
ATOM   1561 C CE2 . TYR A 1 195 ? -0.315  -33.392 7.665   1.00 8.61  ? 197  TYR A CE2 1 
ATOM   1562 C CZ  . TYR A 1 195 ? 0.126   -34.596 7.173   1.00 11.04 ? 197  TYR A CZ  1 
ATOM   1563 O OH  . TYR A 1 195 ? 0.694   -34.706 5.950   1.00 12.82 ? 197  TYR A OH  1 
ATOM   1564 N N   . GLN A 1 196 ? -4.048  -36.157 9.494   1.00 15.62 ? 198  GLN A N   1 
ATOM   1565 C CA  A GLN A 1 196 ? -4.388  -37.445 8.918   0.50 17.11 ? 198  GLN A CA  1 
ATOM   1566 C CA  B GLN A 1 196 ? -4.407  -37.437 8.899   0.50 17.37 ? 198  GLN A CA  1 
ATOM   1567 C C   . GLN A 1 196 ? -3.855  -37.509 7.490   1.00 15.54 ? 198  GLN A C   1 
ATOM   1568 O O   . GLN A 1 196 ? -3.984  -36.537 6.760   1.00 12.98 ? 198  GLN A O   1 
ATOM   1569 C CB  A GLN A 1 196 ? -5.902  -37.634 8.933   0.50 20.60 ? 198  GLN A CB  1 
ATOM   1570 C CB  B GLN A 1 196 ? -5.921  -37.526 8.815   0.50 21.59 ? 198  GLN A CB  1 
ATOM   1571 C CG  A GLN A 1 196 ? -6.672  -36.667 8.034   0.50 24.42 ? 198  GLN A CG  1 
ATOM   1572 C CG  B GLN A 1 196 ? -6.464  -38.918 8.554   0.50 27.38 ? 198  GLN A CG  1 
ATOM   1573 C CD  A GLN A 1 196 ? -7.422  -35.537 8.707   0.50 24.04 ? 198  GLN A CD  1 
ATOM   1574 C CD  B GLN A 1 196 ? -7.976  -38.959 8.682   0.50 33.32 ? 198  GLN A CD  1 
ATOM   1575 O OE1 A GLN A 1 196 ? -8.576  -35.320 8.380   0.50 23.04 ? 198  GLN A OE1 1 
ATOM   1576 O OE1 B GLN A 1 196 ? -8.680  -37.922 8.657   0.50 36.73 ? 198  GLN A OE1 1 
ATOM   1577 N NE2 A GLN A 1 196 ? -6.799  -34.782 9.657   0.50 18.81 ? 198  GLN A NE2 1 
ATOM   1578 N NE2 B GLN A 1 196 ? -8.523  -40.166 8.816   0.50 33.12 ? 198  GLN A NE2 1 
ATOM   1579 N N   . SER A 1 197 ? -3.254  -38.675 7.094   1.00 14.62 ? 199  SER A N   1 
ATOM   1580 C CA  . SER A 1 197 ? -2.869  -38.876 5.715   1.00 15.20 ? 199  SER A CA  1 
ATOM   1581 C C   . SER A 1 197 ? -4.116  -38.906 4.851   1.00 15.18 ? 199  SER A C   1 
ATOM   1582 O O   . SER A 1 197 ? -5.211  -39.287 5.299   1.00 16.58 ? 199  SER A O   1 
ATOM   1583 C CB  . SER A 1 197 ? -2.081  -40.168 5.543   1.00 17.59 ? 199  SER A CB  1 
ATOM   1584 O OG  . SER A 1 197 ? -2.960  -41.236 5.809   1.00 17.38 ? 199  SER A OG  1 
ATOM   1585 N N   . HIS A 1 198 ? -3.968  -38.533 3.587   1.00 13.53 ? 200  HIS A N   1 
ATOM   1586 C CA  . HIS A 1 198 ? -5.091  -38.583 2.658   1.00 13.98 ? 200  HIS A CA  1 
ATOM   1587 C C   . HIS A 1 198 ? -5.547  -40.056 2.499   1.00 15.69 ? 200  HIS A C   1 
ATOM   1588 O O   . HIS A 1 198 ? -6.749  -40.283 2.396   1.00 16.27 ? 200  HIS A O   1 
ATOM   1589 C CB  . HIS A 1 198 ? -4.691  -38.007 1.308   1.00 13.19 ? 200  HIS A CB  1 
ATOM   1590 C CG  . HIS A 1 198 ? -4.384  -36.530 1.384   1.00 13.32 ? 200  HIS A CG  1 
ATOM   1591 N ND1 . HIS A 1 198 ? -5.176  -35.679 2.091   1.00 13.47 ? 200  HIS A ND1 1 
ATOM   1592 C CD2 . HIS A 1 198 ? -3.365  -35.831 0.832   1.00 13.30 ? 200  HIS A CD2 1 
ATOM   1593 C CE1 . HIS A 1 198 ? -4.630  -34.469 1.961   1.00 14.34 ? 200  HIS A CE1 1 
ATOM   1594 N NE2 . HIS A 1 198 ? -3.540  -34.511 1.195   1.00 13.34 ? 200  HIS A NE2 1 
ATOM   1595 N N   . ALA A 1 199 ? -4.607  -41.009 2.514   1.00 17.40 ? 201  ALA A N   1 
ATOM   1596 C CA  . ALA A 1 199 ? -4.971  -42.438 2.396   1.00 21.08 ? 201  ALA A CA  1 
ATOM   1597 C C   . ALA A 1 199 ? -5.941  -42.845 3.516   1.00 23.22 ? 201  ALA A C   1 
ATOM   1598 O O   . ALA A 1 199 ? -6.931  -43.566 3.277   1.00 24.58 ? 201  ALA A O   1 
ATOM   1599 C CB  . ALA A 1 199 ? -3.713  -43.278 2.452   1.00 22.41 ? 201  ALA A CB  1 
ATOM   1600 N N   . ASP A 1 200 ? -5.678  -42.375 4.745   1.00 21.99 ? 202  ASP A N   1 
ATOM   1601 C CA  . ASP A 1 200 ? -6.553  -42.682 5.866   1.00 22.92 ? 202  ASP A CA  1 
ATOM   1602 C C   . ASP A 1 200 ? -7.930  -41.960 5.759   1.00 23.87 ? 202  ASP A C   1 
ATOM   1603 O O   . ASP A 1 200 ? -8.961  -42.581 6.059   1.00 26.39 ? 202  ASP A O   1 
ATOM   1604 C CB  . ASP A 1 200 ? -5.807  -42.413 7.181   1.00 25.49 ? 202  ASP A CB  1 
ATOM   1605 C CG  . ASP A 1 200 ? -4.723  -43.456 7.479   1.00 30.92 ? 202  ASP A CG  1 
ATOM   1606 O OD1 . ASP A 1 200 ? -4.787  -44.579 6.907   1.00 34.02 ? 202  ASP A OD1 1 
ATOM   1607 O OD2 . ASP A 1 200 ? -3.807  -43.155 8.257   1.00 27.83 ? 202  ASP A OD2 1 
ATOM   1608 N N   . THR A 1 201 ? -7.975  -40.705 5.314   1.00 20.15 ? 203  THR A N   1 
ATOM   1609 C CA  . THR A 1 201 ? -9.235  -39.971 5.082   1.00 20.93 ? 203  THR A CA  1 
ATOM   1610 C C   . THR A 1 201 ? -10.117 -40.703 4.051   1.00 22.39 ? 203  THR A C   1 
ATOM   1611 O O   . THR A 1 201 ? -11.330 -40.557 4.111   1.00 24.63 ? 203  THR A O   1 
ATOM   1612 C CB  . THR A 1 201 ? -8.944  -38.577 4.573   1.00 24.05 ? 203  THR A CB  1 
ATOM   1613 O OG1 . THR A 1 201 ? -8.146  -37.943 5.559   1.00 25.65 ? 203  THR A OG1 1 
ATOM   1614 C CG2 . THR A 1 201 ? -10.162 -37.771 4.315   1.00 25.01 ? 203  THR A CG2 1 
ATOM   1615 N N   . ALA A 1 202 ? -9.529  -41.467 3.147   1.00 22.63 ? 204  ALA A N   1 
ATOM   1616 C CA  . ALA A 1 202 ? -10.315 -42.135 2.096   1.00 22.85 ? 204  ALA A CA  1 
ATOM   1617 C C   . ALA A 1 202 ? -11.253 -43.238 2.693   1.00 22.33 ? 204  ALA A C   1 
ATOM   1618 O O   . ALA A 1 202 ? -12.239 -43.582 2.040   1.00 20.68 ? 204  ALA A O   1 
ATOM   1619 C CB  . ALA A 1 202 ? -9.380  -42.759 1.071   1.00 24.75 ? 204  ALA A CB  1 
ATOM   1620 N N   . THR A 1 203 ? -10.933 -43.792 3.897   1.00 22.19 ? 205  THR A N   1 
ATOM   1621 C CA  . THR A 1 203 ? -11.684 -44.932 4.444   1.00 24.43 ? 205  THR A CA  1 
ATOM   1622 C C   . THR A 1 203 ? -11.967 -44.844 5.939   1.00 25.33 ? 205  THR A C   1 
ATOM   1623 O O   . THR A 1 203 ? -12.641 -45.722 6.436   1.00 24.93 ? 205  THR A O   1 
ATOM   1624 C CB  . THR A 1 203 ? -11.000 -46.305 4.144   1.00 26.45 ? 205  THR A CB  1 
ATOM   1625 O OG1 . THR A 1 203 ? -9.853  -46.457 4.962   1.00 28.53 ? 205  THR A OG1 1 
ATOM   1626 C CG2 . THR A 1 203 ? -10.573 -46.477 2.698   1.00 26.07 ? 205  THR A CG2 1 
ATOM   1627 N N   . LYS A 1 204 ? -11.482 -43.801 6.655   1.00 24.91 ? 206  LYS A N   1 
ATOM   1628 C CA  . LYS A 1 204 ? -11.614 -43.731 8.127   1.00 26.44 ? 206  LYS A CA  1 
ATOM   1629 C C   . LYS A 1 204 ? -12.117 -42.389 8.524   1.00 26.57 ? 206  LYS A C   1 
ATOM   1630 O O   . LYS A 1 204 ? -11.691 -41.432 7.879   1.00 28.34 ? 206  LYS A O   1 
ATOM   1631 C CB  . LYS A 1 204 ? -10.275 -43.995 8.836   1.00 29.86 ? 206  LYS A CB  1 
ATOM   1632 C CG  . LYS A 1 204 ? -9.542  -45.198 8.318   1.00 36.08 ? 206  LYS A CG  1 
ATOM   1633 C CD  . LYS A 1 204 ? -8.273  -45.499 9.053   1.00 42.61 ? 206  LYS A CD  1 
ATOM   1634 C CE  . LYS A 1 204 ? -7.685  -46.807 8.567   1.00 46.14 ? 206  LYS A CE  1 
ATOM   1635 N NZ  . LYS A 1 204 ? -6.248  -46.906 8.910   1.00 49.04 ? 206  LYS A NZ  1 
ATOM   1636 N N   . THR A 1 209 ? -8.896  -36.961 17.162  1.00 40.86 ? 211  THR A N   1 
ATOM   1637 C CA  . THR A 1 209 ? -8.284  -37.198 18.468  1.00 41.47 ? 211  THR A CA  1 
ATOM   1638 C C   . THR A 1 209 ? -7.361  -38.417 18.468  1.00 41.00 ? 211  THR A C   1 
ATOM   1639 O O   . THR A 1 209 ? -6.338  -38.386 19.153  1.00 39.60 ? 211  THR A O   1 
ATOM   1640 C CB  . THR A 1 209 ? -9.346  -37.266 19.583  1.00 44.09 ? 211  THR A CB  1 
ATOM   1641 O OG1 . THR A 1 209 ? -10.250 -38.356 19.355  1.00 45.77 ? 211  THR A OG1 1 
ATOM   1642 C CG2 . THR A 1 209 ? -10.122 -35.953 19.728  1.00 44.99 ? 211  THR A CG2 1 
ATOM   1643 N N   . LYS A 1 210 ? -7.717  -39.491 17.708  1.00 40.84 ? 212  LYS A N   1 
ATOM   1644 C CA  . LYS A 1 210 ? -6.843  -40.650 17.525  1.00 41.36 ? 212  LYS A CA  1 
ATOM   1645 C C   . LYS A 1 210 ? -5.890  -40.535 16.308  1.00 41.07 ? 212  LYS A C   1 
ATOM   1646 O O   . LYS A 1 210 ? -5.195  -41.504 15.988  1.00 42.97 ? 212  LYS A O   1 
ATOM   1647 C CB  . LYS A 1 210 ? -7.680  -41.937 17.410  1.00 44.27 ? 212  LYS A CB  1 
ATOM   1648 C CG  . LYS A 1 210 ? -8.421  -42.163 16.105  1.00 50.70 ? 212  LYS A CG  1 
ATOM   1649 C CD  . LYS A 1 210 ? -9.433  -43.299 16.308  1.00 57.74 ? 212  LYS A CD  1 
ATOM   1650 C CE  . LYS A 1 210 ? -9.819  -44.019 15.030  1.00 63.99 ? 212  LYS A CE  1 
ATOM   1651 N NZ  . LYS A 1 210 ? -10.654 -45.227 15.313  1.00 67.20 ? 212  LYS A NZ  1 
ATOM   1652 N N   . ASN A 1 211 ? -5.868  -39.375 15.644  1.00 36.99 ? 213  ASN A N   1 
ATOM   1653 C CA  . ASN A 1 211 ? -5.037  -39.085 14.456  1.00 33.26 ? 213  ASN A CA  1 
ATOM   1654 C C   . ASN A 1 211 ? -3.553  -39.362 14.635  1.00 31.50 ? 213  ASN A C   1 
ATOM   1655 O O   . ASN A 1 211 ? -3.045  -39.460 15.763  1.00 30.91 ? 213  ASN A O   1 
ATOM   1656 C CB  . ASN A 1 211 ? -5.257  -37.611 14.052  1.00 30.88 ? 213  ASN A CB  1 
ATOM   1657 C CG  . ASN A 1 211 ? -6.570  -37.266 13.376  1.00 33.51 ? 213  ASN A CG  1 
ATOM   1658 O OD1 . ASN A 1 211 ? -6.815  -36.115 13.054  1.00 34.86 ? 213  ASN A OD1 1 
ATOM   1659 N ND2 . ASN A 1 211 ? -7.496  -38.216 13.122  1.00 34.38 ? 213  ASN A ND2 1 
ATOM   1660 N N   . ARG A 1 212 ? -2.864  -39.469 13.480  1.00 28.95 ? 214  ARG A N   1 
ATOM   1661 C CA  . ARG A 1 212 ? -1.427  -39.782 13.355  1.00 28.85 ? 214  ARG A CA  1 
ATOM   1662 C C   . ARG A 1 212 ? -0.569  -38.838 14.216  1.00 26.32 ? 214  ARG A C   1 
ATOM   1663 O O   . ARG A 1 212 ? 0.262   -39.277 15.022  1.00 26.94 ? 214  ARG A O   1 
ATOM   1664 C CB  . ARG A 1 212 ? -1.059  -39.618 11.849  1.00 32.39 ? 214  ARG A CB  1 
ATOM   1665 C CG  . ARG A 1 212 ? 0.344   -39.956 11.392  1.00 38.25 ? 214  ARG A CG  1 
ATOM   1666 C CD  . ARG A 1 212 ? 0.460   -39.681 9.908   1.00 43.83 ? 214  ARG A CD  1 
ATOM   1667 N NE  . ARG A 1 212 ? -0.090  -40.765 9.084   1.00 48.22 ? 214  ARG A NE  1 
ATOM   1668 C CZ  . ARG A 1 212 ? 0.613   -41.695 8.418   1.00 49.63 ? 214  ARG A CZ  1 
ATOM   1669 N NH1 . ARG A 1 212 ? -0.012  -42.623 7.710   1.00 47.31 ? 214  ARG A NH1 1 
ATOM   1670 N NH2 . ARG A 1 212 ? 1.945   -41.701 8.459   1.00 50.79 ? 214  ARG A NH2 1 
ATOM   1671 N N   . PHE A 1 213 ? -0.799  -37.532 14.029  1.00 20.93 ? 215  PHE A N   1 
ATOM   1672 C CA  . PHE A 1 213 ? -0.177  -36.516 14.883  1.00 19.19 ? 215  PHE A CA  1 
ATOM   1673 C C   . PHE A 1 213 ? -1.298  -35.640 15.473  1.00 16.07 ? 215  PHE A C   1 
ATOM   1674 O O   . PHE A 1 213 ? -2.300  -35.337 14.824  1.00 16.09 ? 215  PHE A O   1 
ATOM   1675 C CB  . PHE A 1 213 ? 0.814   -35.634 14.105  1.00 19.93 ? 215  PHE A CB  1 
ATOM   1676 C CG  . PHE A 1 213 ? 1.864   -36.383 13.303  1.00 22.82 ? 215  PHE A CG  1 
ATOM   1677 C CD1 . PHE A 1 213 ? 2.924   -36.997 13.934  1.00 25.81 ? 215  PHE A CD1 1 
ATOM   1678 C CD2 . PHE A 1 213 ? 1.788   -36.458 11.924  1.00 24.43 ? 215  PHE A CD2 1 
ATOM   1679 C CE1 . PHE A 1 213 ? 3.871   -37.714 13.203  1.00 27.02 ? 215  PHE A CE1 1 
ATOM   1680 C CE2 . PHE A 1 213 ? 2.777   -37.114 11.186  1.00 25.78 ? 215  PHE A CE2 1 
ATOM   1681 C CZ  . PHE A 1 213 ? 3.812   -37.736 11.838  1.00 26.06 ? 215  PHE A CZ  1 
ATOM   1682 N N   . VAL A 1 214 ? -1.108  -35.231 16.715  1.00 15.92 ? 216  VAL A N   1 
ATOM   1683 C CA  A VAL A 1 214 ? -2.035  -34.339 17.409  0.50 15.02 ? 216  VAL A CA  1 
ATOM   1684 C CA  B VAL A 1 214 ? -2.018  -34.298 17.351  0.50 14.99 ? 216  VAL A CA  1 
ATOM   1685 C C   . VAL A 1 214 ? -1.179  -33.238 18.065  1.00 15.71 ? 216  VAL A C   1 
ATOM   1686 O O   . VAL A 1 214 ? -0.117  -33.559 18.638  1.00 18.37 ? 216  VAL A O   1 
ATOM   1687 C CB  A VAL A 1 214 ? -2.895  -35.132 18.456  0.50 15.37 ? 216  VAL A CB  1 
ATOM   1688 C CB  B VAL A 1 214 ? -3.001  -35.070 18.276  0.50 15.24 ? 216  VAL A CB  1 
ATOM   1689 C CG1 A VAL A 1 214 ? -3.444  -34.192 19.524  0.50 16.70 ? 216  VAL A CG1 1 
ATOM   1690 C CG1 B VAL A 1 214 ? -2.312  -35.543 19.543  0.50 14.12 ? 216  VAL A CG1 1 
ATOM   1691 C CG2 A VAL A 1 214 ? -4.030  -35.923 17.767  0.50 13.83 ? 216  VAL A CG2 1 
ATOM   1692 C CG2 B VAL A 1 214 ? -4.211  -34.230 18.598  0.50 15.74 ? 216  VAL A CG2 1 
ATOM   1693 N N   . VAL A 1 215 ? -1.630  -31.989 18.026  1.00 14.74 ? 217  VAL A N   1 
ATOM   1694 C CA  . VAL A 1 215 ? -1.005  -30.890 18.772  1.00 13.95 ? 217  VAL A CA  1 
ATOM   1695 C C   . VAL A 1 215 ? -2.071  -29.999 19.398  1.00 14.46 ? 217  VAL A C   1 
ATOM   1696 O O   . VAL A 1 215 ? -1.681  -29.170 20.246  1.00 15.94 ? 217  VAL A O   1 
ATOM   1697 C CB  . VAL A 1 215 ? -0.075  -29.990 17.909  1.00 15.40 ? 217  VAL A CB  1 
ATOM   1698 C CG1 . VAL A 1 215 ? 1.065   -30.818 17.323  1.00 16.74 ? 217  VAL A CG1 1 
ATOM   1699 C CG2 . VAL A 1 215 ? -0.865  -29.238 16.830  1.00 13.99 ? 217  VAL A CG2 1 
ATOM   1700 O OXT . VAL A 1 215 ? -3.238  -30.108 19.008  1.00 13.46 ? 217  VAL A OXT 1 
ATOM   1701 N N   . GLY B 1 8   ? -13.675 -24.277 -35.715 1.00 35.18 ? 10   GLY B N   1 
ATOM   1702 C CA  . GLY B 1 8   ? -14.230 -24.711 -34.436 1.00 33.88 ? 10   GLY B CA  1 
ATOM   1703 C C   . GLY B 1 8   ? -13.806 -23.779 -33.325 1.00 31.84 ? 10   GLY B C   1 
ATOM   1704 O O   . GLY B 1 8   ? -13.627 -22.584 -33.568 1.00 33.36 ? 10   GLY B O   1 
ATOM   1705 N N   . ALA B 1 9   ? -13.667 -24.291 -32.129 1.00 28.58 ? 11   ALA B N   1 
ATOM   1706 C CA  . ALA B 1 9   ? -13.149 -23.513 -31.034 1.00 27.50 ? 11   ALA B CA  1 
ATOM   1707 C C   . ALA B 1 9   ? -11.618 -23.406 -31.232 1.00 25.09 ? 11   ALA B C   1 
ATOM   1708 O O   . ALA B 1 9   ? -11.002 -24.151 -32.026 1.00 26.03 ? 11   ALA B O   1 
ATOM   1709 C CB  . ALA B 1 9   ? -13.486 -24.158 -29.703 1.00 28.47 ? 11   ALA B CB  1 
ATOM   1710 N N   . ARG B 1 10  ? -10.987 -22.462 -30.510 1.00 21.28 ? 12   ARG B N   1 
ATOM   1711 C CA  . ARG B 1 10  ? -9.550  -22.320 -30.580 1.00 17.72 ? 12   ARG B CA  1 
ATOM   1712 C C   . ARG B 1 10  ? -8.871  -23.613 -30.210 1.00 17.08 ? 12   ARG B C   1 
ATOM   1713 O O   . ARG B 1 10  ? -9.268  -24.258 -29.249 1.00 17.23 ? 12   ARG B O   1 
ATOM   1714 C CB  . ARG B 1 10  ? -9.107  -21.288 -29.586 1.00 17.36 ? 12   ARG B CB  1 
ATOM   1715 C CG  . ARG B 1 10  ? -7.642  -20.922 -29.668 1.00 15.94 ? 12   ARG B CG  1 
ATOM   1716 C CD  . ARG B 1 10  ? -7.336  -19.853 -28.620 1.00 15.72 ? 12   ARG B CD  1 
ATOM   1717 N NE  . ARG B 1 10  ? -8.186  -18.680 -28.807 1.00 17.40 ? 12   ARG B NE  1 
ATOM   1718 C CZ  . ARG B 1 10  ? -7.934  -17.661 -29.621 1.00 17.25 ? 12   ARG B CZ  1 
ATOM   1719 N NH1 . ARG B 1 10  ? -6.807  -17.623 -30.320 1.00 15.97 ? 12   ARG B NH1 1 
ATOM   1720 N NH2 . ARG B 1 10  ? -8.810  -16.663 -29.738 1.00 18.12 ? 12   ARG B NH2 1 
ATOM   1721 N N   . ILE B 1 11  ? -7.850  -23.962 -30.967 1.00 14.54 ? 13   ILE B N   1 
ATOM   1722 C CA  . ILE B 1 11  ? -7.094  -25.152 -30.735 1.00 13.07 ? 13   ILE B CA  1 
ATOM   1723 C C   . ILE B 1 11  ? -6.058  -24.795 -29.702 1.00 13.42 ? 13   ILE B C   1 
ATOM   1724 O O   . ILE B 1 11  ? -5.136  -24.011 -29.995 1.00 13.88 ? 13   ILE B O   1 
ATOM   1725 C CB  . ILE B 1 11  ? -6.449  -25.676 -32.039 1.00 13.33 ? 13   ILE B CB  1 
ATOM   1726 C CG1 . ILE B 1 11  ? -7.539  -26.076 -33.078 1.00 16.69 ? 13   ILE B CG1 1 
ATOM   1727 C CG2 . ILE B 1 11  ? -5.635  -26.894 -31.680 1.00 13.16 ? 13   ILE B CG2 1 
ATOM   1728 C CD1 . ILE B 1 11  ? -7.015  -26.453 -34.432 1.00 17.75 ? 13   ILE B CD1 1 
ATOM   1729 N N   . ILE B 1 12  ? -6.202  -25.328 -28.484 1.00 13.26 ? 14   ILE B N   1 
ATOM   1730 C CA  . ILE B 1 12  ? -5.271  -25.007 -27.394 1.00 12.30 ? 14   ILE B CA  1 
ATOM   1731 C C   . ILE B 1 12  ? -4.610  -26.317 -26.973 1.00 13.03 ? 14   ILE B C   1 
ATOM   1732 O O   . ILE B 1 12  ? -5.317  -27.335 -26.744 1.00 14.00 ? 14   ILE B O   1 
ATOM   1733 C CB  . ILE B 1 12  ? -6.009  -24.386 -26.197 1.00 14.37 ? 14   ILE B CB  1 
ATOM   1734 C CG1 . ILE B 1 12  ? -6.686  -23.034 -26.607 1.00 16.81 ? 14   ILE B CG1 1 
ATOM   1735 C CG2 . ILE B 1 12  ? -5.102  -24.261 -24.927 1.00 16.78 ? 14   ILE B CG2 1 
ATOM   1736 C CD1 . ILE B 1 12  ? -7.708  -22.542 -25.652 1.00 20.86 ? 14   ILE B CD1 1 
ATOM   1737 N N   . TYR B 1 13  ? -3.287  -26.313 -26.820 1.00 12.10 ? 15   TYR B N   1 
ATOM   1738 C CA  . TYR B 1 13  ? -2.578  -27.473 -26.331 1.00 11.33 ? 15   TYR B CA  1 
ATOM   1739 C C   . TYR B 1 13  ? -1.749  -27.058 -25.120 1.00 12.11 ? 15   TYR B C   1 
ATOM   1740 O O   . TYR B 1 13  ? -1.049  -26.027 -25.187 1.00 11.60 ? 15   TYR B O   1 
ATOM   1741 C CB  . TYR B 1 13  ? -1.632  -27.962 -27.381 1.00 10.89 ? 15   TYR B CB  1 
ATOM   1742 C CG  . TYR B 1 13  ? -2.242  -28.429 -28.663 1.00 10.68 ? 15   TYR B CG  1 
ATOM   1743 C CD1 . TYR B 1 13  ? -2.981  -29.615 -28.715 1.00 11.91 ? 15   TYR B CD1 1 
ATOM   1744 C CD2 . TYR B 1 13  ? -2.032  -27.739 -29.854 1.00 10.08 ? 15   TYR B CD2 1 
ATOM   1745 C CE1 . TYR B 1 13  ? -3.454  -30.108 -29.914 1.00 12.54 ? 15   TYR B CE1 1 
ATOM   1746 C CE2 . TYR B 1 13  ? -2.550  -28.205 -31.053 1.00 10.83 ? 15   TYR B CE2 1 
ATOM   1747 C CZ  . TYR B 1 13  ? -3.254  -29.399 -31.080 1.00 12.84 ? 15   TYR B CZ  1 
ATOM   1748 O OH  . TYR B 1 13  ? -3.742  -29.898 -32.268 1.00 13.82 ? 15   TYR B OH  1 
ATOM   1749 N N   . ASP B 1 14  ? -1.840  -27.794 -24.027 1.00 12.61 ? 16   ASP B N   1 
ATOM   1750 C CA  . ASP B 1 14  ? -1.019  -27.486 -22.863 1.00 13.07 ? 16   ASP B CA  1 
ATOM   1751 C C   . ASP B 1 14  ? 0.386   -28.049 -23.030 1.00 12.65 ? 16   ASP B C   1 
ATOM   1752 O O   . ASP B 1 14  ? 0.666   -28.772 -23.972 1.00 14.64 ? 16   ASP B O   1 
ATOM   1753 C CB  . ASP B 1 14  ? -1.701  -27.889 -21.548 1.00 13.74 ? 16   ASP B CB  1 
ATOM   1754 C CG  . ASP B 1 14  ? -1.861  -29.338 -21.224 1.00 19.91 ? 16   ASP B CG  1 
ATOM   1755 O OD1 . ASP B 1 14  ? -1.252  -30.201 -21.919 1.00 17.79 ? 16   ASP B OD1 1 
ATOM   1756 O OD2 . ASP B 1 14  ? -2.641  -29.649 -20.269 1.00 24.04 ? 16   ASP B OD2 1 
ATOM   1757 N N   . ARG B 1 15  ? 1.285   -27.698 -22.119 1.00 12.68 ? 17   ARG B N   1 
ATOM   1758 C CA  . ARG B 1 15  ? 2.673   -28.085 -22.185 1.00 12.96 ? 17   ARG B CA  1 
ATOM   1759 C C   . ARG B 1 15  ? 2.840   -29.588 -22.252 1.00 13.84 ? 17   ARG B C   1 
ATOM   1760 O O   . ARG B 1 15  ? 3.566   -30.104 -23.104 1.00 13.30 ? 17   ARG B O   1 
ATOM   1761 C CB  . ARG B 1 15  ? 3.442   -27.536 -20.987 1.00 13.46 ? 17   ARG B CB  1 
ATOM   1762 C CG  . ARG B 1 15  ? 4.916   -27.800 -21.095 1.00 15.73 ? 17   ARG B CG  1 
ATOM   1763 C CD  . ARG B 1 15  ? 5.561   -27.447 -19.783 1.00 19.81 ? 17   ARG B CD  1 
ATOM   1764 N NE  . ARG B 1 15  ? 7.007   -27.396 -19.910 1.00 23.57 ? 17   ARG B NE  1 
ATOM   1765 C CZ  . ARG B 1 15  ? 7.871   -28.398 -19.715 1.00 32.09 ? 17   ARG B CZ  1 
ATOM   1766 N NH1 . ARG B 1 15  ? 7.439   -29.616 -19.390 1.00 28.17 ? 17   ARG B NH1 1 
ATOM   1767 N NH2 . ARG B 1 15  ? 9.173   -28.192 -19.853 1.00 34.19 ? 17   ARG B NH2 1 
ATOM   1768 N N   . ALA B 1 16  ? 2.139   -30.310 -21.366 1.00 13.73 ? 18   ALA B N   1 
ATOM   1769 C CA  . ALA B 1 16  ? 2.286   -31.761 -21.314 1.00 15.47 ? 18   ALA B CA  1 
ATOM   1770 C C   . ALA B 1 16  ? 1.872   -32.431 -22.609 1.00 14.70 ? 18   ALA B C   1 
ATOM   1771 O O   . ALA B 1 16  ? 2.558   -33.342 -23.056 1.00 16.01 ? 18   ALA B O   1 
ATOM   1772 C CB  . ALA B 1 16  ? 1.497   -32.329 -20.134 1.00 17.05 ? 18   ALA B CB  1 
ATOM   1773 N N   . PHE B 1 17  ? 0.794   -31.965 -23.223 1.00 12.58 ? 19   PHE B N   1 
ATOM   1774 C CA  . PHE B 1 17  ? 0.310   -32.514 -24.492 1.00 14.07 ? 19   PHE B CA  1 
ATOM   1775 C C   . PHE B 1 17  ? 1.344   -32.294 -25.581 1.00 13.98 ? 19   PHE B C   1 
ATOM   1776 O O   . PHE B 1 17  ? 1.714   -33.213 -26.321 1.00 14.18 ? 19   PHE B O   1 
ATOM   1777 C CB  . PHE B 1 17  ? -1.041  -31.861 -24.877 1.00 14.50 ? 19   PHE B CB  1 
ATOM   1778 C CG  . PHE B 1 17  ? -1.736  -32.557 -26.027 1.00 16.90 ? 19   PHE B CG  1 
ATOM   1779 C CD1 . PHE B 1 17  ? -1.388  -32.292 -27.333 1.00 18.79 ? 19   PHE B CD1 1 
ATOM   1780 C CD2 . PHE B 1 17  ? -2.724  -33.490 -25.790 1.00 18.61 ? 19   PHE B CD2 1 
ATOM   1781 C CE1 . PHE B 1 17  ? -2.009  -32.958 -28.381 1.00 20.51 ? 19   PHE B CE1 1 
ATOM   1782 C CE2 . PHE B 1 17  ? -3.338  -34.132 -26.820 1.00 19.83 ? 19   PHE B CE2 1 
ATOM   1783 C CZ  . PHE B 1 17  ? -2.988  -33.858 -28.120 1.00 19.91 ? 19   PHE B CZ  1 
ATOM   1784 N N   . LEU B 1 18  ? 1.844   -31.030 -25.678 1.00 11.89 ? 20   LEU B N   1 
ATOM   1785 C CA  . LEU B 1 18  ? 2.872   -30.763 -26.689 1.00 11.26 ? 20   LEU B CA  1 
ATOM   1786 C C   . LEU B 1 18  ? 4.126   -31.622 -26.493 1.00 13.45 ? 20   LEU B C   1 
ATOM   1787 O O   . LEU B 1 18  ? 4.672   -32.139 -27.454 1.00 13.39 ? 20   LEU B O   1 
ATOM   1788 C CB  . LEU B 1 18  ? 3.222   -29.280 -26.716 1.00 12.02 ? 20   LEU B CB  1 
ATOM   1789 C CG  . LEU B 1 18  ? 2.053   -28.431 -27.157 1.00 11.89 ? 20   LEU B CG  1 
ATOM   1790 C CD1 . LEU B 1 18  ? 2.323   -26.955 -26.978 1.00 11.45 ? 20   LEU B CD1 1 
ATOM   1791 C CD2 . LEU B 1 18  ? 1.742   -28.696 -28.672 1.00 10.64 ? 20   LEU B CD2 1 
ATOM   1792 N N   . MET B 1 19  ? 4.552   -31.775 -25.272 1.00 14.48 ? 21   MET B N   1 
ATOM   1793 C CA  . MET B 1 19  ? 5.776   -32.546 -24.941 1.00 15.14 ? 21   MET B CA  1 
ATOM   1794 C C   . MET B 1 19  ? 5.614   -34.020 -25.307 1.00 18.69 ? 21   MET B C   1 
ATOM   1795 O O   . MET B 1 19  ? 6.561   -34.636 -25.825 1.00 19.30 ? 21   MET B O   1 
ATOM   1796 C CB  . MET B 1 19  ? 6.103   -32.379 -23.440 1.00 15.11 ? 21   MET B CB  1 
ATOM   1797 C CG  . MET B 1 19  ? 6.597   -30.998 -23.086 1.00 17.60 ? 21   MET B CG  1 
ATOM   1798 S SD  . MET B 1 19  ? 7.981   -30.319 -24.029 1.00 21.32 ? 21   MET B SD  1 
ATOM   1799 C CE  . MET B 1 19  ? 8.481   -29.099 -22.938 1.00 28.63 ? 21   MET B CE  1 
ATOM   1800 N N   . ALA B 1 20  ? 4.416   -34.560 -25.054 1.00 18.66 ? 22   ALA B N   1 
ATOM   1801 C CA  . ALA B 1 20  ? 4.039   -35.938 -25.370 1.00 20.05 ? 22   ALA B CA  1 
ATOM   1802 C C   . ALA B 1 20  ? 4.038   -36.166 -26.872 1.00 21.37 ? 22   ALA B C   1 
ATOM   1803 O O   . ALA B 1 20  ? 4.332   -37.275 -27.294 1.00 23.48 ? 22   ALA B O   1 
ATOM   1804 C CB  . ALA B 1 20  ? 2.680   -36.273 -24.761 1.00 20.13 ? 22   ALA B CB  1 
ATOM   1805 N N   . CYS B 1 21  ? 3.755   -35.143 -27.707 1.00 19.86 ? 23   CYS B N   1 
ATOM   1806 C CA  . CYS B 1 21  ? 3.799   -35.288 -29.161 1.00 20.10 ? 23   CYS B CA  1 
ATOM   1807 C C   . CYS B 1 21  ? 5.205   -35.378 -29.746 1.00 19.30 ? 23   CYS B C   1 
ATOM   1808 O O   . CYS B 1 21  ? 5.317   -35.677 -30.924 1.00 20.81 ? 23   CYS B O   1 
ATOM   1809 C CB  . CYS B 1 21  ? 3.026   -34.182 -29.857 1.00 19.42 ? 23   CYS B CB  1 
ATOM   1810 S SG  . CYS B 1 21  ? 1.264   -34.153 -29.540 1.00 20.26 ? 23   CYS B SG  1 
ATOM   1811 N N   . ARG B 1 22  ? 6.243   -35.101 -28.990 1.00 18.51 ? 24   ARG B N   1 
ATOM   1812 C CA  . ARG B 1 22  ? 7.588   -35.132 -29.509 1.00 18.88 ? 24   ARG B CA  1 
ATOM   1813 C C   . ARG B 1 22  ? 8.014   -36.582 -29.756 1.00 23.54 ? 24   ARG B C   1 
ATOM   1814 O O   . ARG B 1 22  ? 8.481   -36.893 -30.837 1.00 24.73 ? 24   ARG B O   1 
ATOM   1815 C CB  . ARG B 1 22  ? 8.568   -34.453 -28.570 1.00 17.47 ? 24   ARG B CB  1 
ATOM   1816 C CG  . ARG B 1 22  ? 9.890   -34.227 -29.255 1.00 16.44 ? 24   ARG B CG  1 
ATOM   1817 C CD  . ARG B 1 22  ? 10.870  -33.635 -28.342 1.00 18.45 ? 24   ARG B CD  1 
ATOM   1818 N NE  . ARG B 1 22  ? 12.096  -33.249 -29.050 1.00 20.25 ? 24   ARG B NE  1 
ATOM   1819 C CZ  . ARG B 1 22  ? 13.224  -32.898 -28.460 1.00 25.20 ? 24   ARG B CZ  1 
ATOM   1820 N NH1 . ARG B 1 22  ? 13.316  -32.893 -27.137 1.00 29.06 ? 24   ARG B NH1 1 
ATOM   1821 N NH2 . ARG B 1 22  ? 14.272  -32.538 -29.185 1.00 25.91 ? 24   ARG B NH2 1 
ATOM   1822 N N   . GLY B 1 23  ? 7.838   -37.410 -28.760 1.00 26.59 ? 25   GLY B N   1 
ATOM   1823 C CA  . GLY B 1 23  ? 8.188   -38.824 -28.822 1.00 31.10 ? 25   GLY B CA  1 
ATOM   1824 C C   . GLY B 1 23  ? 7.004   -39.735 -29.078 1.00 34.38 ? 25   GLY B C   1 
ATOM   1825 O O   . GLY B 1 23  ? 7.211   -40.903 -29.415 1.00 35.70 ? 25   GLY B O   1 
ATOM   1826 N N   . GLY B 1 24  ? 5.782   -39.219 -28.909 1.00 35.48 ? 26   GLY B N   1 
ATOM   1827 C CA  . GLY B 1 24  ? 4.546   -39.954 -29.153 1.00 37.15 ? 26   GLY B CA  1 
ATOM   1828 C C   . GLY B 1 24  ? 3.581   -39.192 -30.037 1.00 37.86 ? 26   GLY B C   1 
ATOM   1829 O O   . GLY B 1 24  ? 2.372   -39.178 -29.785 1.00 38.07 ? 26   GLY B O   1 
ATOM   1830 N N   . GLY B 1 25  ? 4.128   -38.580 -31.070 1.00 38.35 ? 27   GLY B N   1 
ATOM   1831 C CA  . GLY B 1 25  ? 3.366   -37.763 -32.002 1.00 38.69 ? 27   GLY B CA  1 
ATOM   1832 C C   . GLY B 1 25  ? 2.820   -38.593 -33.133 1.00 38.93 ? 27   GLY B C   1 
ATOM   1833 O O   . GLY B 1 25  ? 3.126   -39.789 -33.262 1.00 39.90 ? 27   GLY B O   1 
ATOM   1834 N N   . GLY B 1 26  ? 1.998   -37.962 -33.945 1.00 37.71 ? 28   GLY B N   1 
ATOM   1835 C CA  . GLY B 1 26  ? 1.545   -38.574 -35.178 1.00 37.64 ? 28   GLY B CA  1 
ATOM   1836 C C   . GLY B 1 26  ? 0.437   -39.587 -34.969 1.00 37.65 ? 28   GLY B C   1 
ATOM   1837 O O   . GLY B 1 26  ? 0.127   -40.330 -35.895 1.00 38.95 ? 28   GLY B O   1 
ATOM   1838 N N   . GLU B 1 27  ? -0.179  -39.638 -33.766 1.00 36.32 ? 29   GLU B N   1 
ATOM   1839 C CA  . GLU B 1 27  ? -1.277  -40.569 -33.506 1.00 36.93 ? 29   GLU B CA  1 
ATOM   1840 C C   . GLU B 1 27  ? -2.615  -39.834 -33.306 1.00 35.91 ? 29   GLU B C   1 
ATOM   1841 O O   . GLU B 1 27  ? -3.523  -40.362 -32.645 1.00 36.37 ? 29   GLU B O   1 
ATOM   1842 C CB  . GLU B 1 27  ? -0.923  -41.448 -32.289 1.00 40.82 ? 29   GLU B CB  1 
ATOM   1843 C CG  . GLU B 1 27  ? -0.055  -42.655 -32.634 1.00 48.43 ? 29   GLU B CG  1 
ATOM   1844 C CD  . GLU B 1 27  ? 0.767   -43.139 -31.459 1.00 56.11 ? 29   GLU B CD  1 
ATOM   1845 O OE1 . GLU B 1 27  ? 1.957   -43.467 -31.660 1.00 58.31 ? 29   GLU B OE1 1 
ATOM   1846 O OE2 . GLU B 1 27  ? 0.220   -43.188 -30.334 1.00 60.03 ? 29   GLU B OE2 1 
ATOM   1847 N N   . ASN B 1 28  ? -2.768  -38.627 -33.890 1.00 33.20 ? 30   ASN B N   1 
ATOM   1848 C CA  . ASN B 1 28  ? -4.048  -37.948 -33.881 1.00 33.40 ? 30   ASN B CA  1 
ATOM   1849 C C   . ASN B 1 28  ? -5.065  -38.741 -34.664 1.00 34.39 ? 30   ASN B C   1 
ATOM   1850 O O   . ASN B 1 28  ? -4.732  -39.522 -35.555 1.00 34.00 ? 30   ASN B O   1 
ATOM   1851 C CB  . ASN B 1 28  ? -3.985  -36.553 -34.484 1.00 33.80 ? 30   ASN B CB  1 
ATOM   1852 C CG  . ASN B 1 28  ? -5.127  -35.664 -34.059 1.00 35.56 ? 30   ASN B CG  1 
ATOM   1853 O OD1 . ASN B 1 28  ? -5.828  -35.941 -33.078 1.00 37.29 ? 30   ASN B OD1 1 
ATOM   1854 N ND2 . ASN B 1 28  ? -5.329  -34.566 -34.769 1.00 35.69 ? 30   ASN B ND2 1 
ATOM   1855 N N   . LEU B 1 29  ? -6.303  -38.527 -34.314 1.00 34.70 ? 31   LEU B N   1 
ATOM   1856 C CA  . LEU B 1 29  ? -7.425  -39.231 -34.907 1.00 34.78 ? 31   LEU B CA  1 
ATOM   1857 C C   . LEU B 1 29  ? -7.812  -38.706 -36.312 1.00 34.14 ? 31   LEU B C   1 
ATOM   1858 O O   . LEU B 1 29  ? -8.676  -39.301 -36.975 1.00 33.85 ? 31   LEU B O   1 
ATOM   1859 C CB  . LEU B 1 29  ? -8.624  -39.136 -33.949 1.00 35.86 ? 31   LEU B CB  1 
ATOM   1860 C CG  . LEU B 1 29  ? -8.451  -39.651 -32.496 1.00 39.26 ? 31   LEU B CG  1 
ATOM   1861 C CD1 . LEU B 1 29  ? -9.710  -39.462 -31.732 1.00 40.91 ? 31   LEU B CD1 1 
ATOM   1862 C CD2 . LEU B 1 29  ? -8.168  -41.159 -32.435 1.00 40.36 ? 31   LEU B CD2 1 
ATOM   1863 N N   . TYR B 1 30  ? -7.188  -37.610 -36.776 1.00 32.88 ? 32   TYR B N   1 
ATOM   1864 C CA  . TYR B 1 30  ? -7.347  -37.193 -38.163 1.00 33.07 ? 32   TYR B CA  1 
ATOM   1865 C C   . TYR B 1 30  ? -6.052  -36.593 -38.677 1.00 32.31 ? 32   TYR B C   1 
ATOM   1866 O O   . TYR B 1 30  ? -5.034  -36.656 -37.975 1.00 32.92 ? 32   TYR B O   1 
ATOM   1867 C CB  . TYR B 1 30  ? -8.584  -36.268 -38.320 1.00 33.28 ? 32   TYR B CB  1 
ATOM   1868 C CG  . TYR B 1 30  ? -8.417  -34.857 -37.803 1.00 34.26 ? 32   TYR B CG  1 
ATOM   1869 C CD1 . TYR B 1 30  ? -8.334  -34.598 -36.444 1.00 34.97 ? 32   TYR B CD1 1 
ATOM   1870 C CD2 . TYR B 1 30  ? -8.388  -33.775 -38.674 1.00 36.29 ? 32   TYR B CD2 1 
ATOM   1871 C CE1 . TYR B 1 30  ? -8.215  -33.297 -35.960 1.00 36.34 ? 32   TYR B CE1 1 
ATOM   1872 C CE2 . TYR B 1 30  ? -8.243  -32.471 -38.204 1.00 37.07 ? 32   TYR B CE2 1 
ATOM   1873 C CZ  . TYR B 1 30  ? -8.170  -32.236 -36.845 1.00 37.56 ? 32   TYR B CZ  1 
ATOM   1874 O OH  . TYR B 1 30  ? -8.069  -30.938 -36.391 1.00 38.66 ? 32   TYR B OH  1 
ATOM   1875 N N   . PHE B 1 31  ? -6.064  -36.058 -39.911 1.00 31.03 ? 33   PHE B N   1 
ATOM   1876 C CA  . PHE B 1 31  ? -4.907  -35.409 -40.515 1.00 30.82 ? 33   PHE B CA  1 
ATOM   1877 C C   . PHE B 1 31  ? -3.744  -36.400 -40.662 1.00 31.60 ? 33   PHE B C   1 
ATOM   1878 O O   . PHE B 1 31  ? -2.565  -36.040 -40.523 1.00 30.14 ? 33   PHE B O   1 
ATOM   1879 C CB  . PHE B 1 31  ? -4.476  -34.182 -39.691 1.00 29.50 ? 33   PHE B CB  1 
ATOM   1880 C CG  . PHE B 1 31  ? -3.754  -33.051 -40.432 1.00 30.00 ? 33   PHE B CG  1 
ATOM   1881 C CD1 . PHE B 1 31  ? -3.034  -33.300 -41.594 1.00 30.46 ? 33   PHE B CD1 1 
ATOM   1882 C CD2 . PHE B 1 31  ? -3.781  -31.752 -39.942 1.00 29.93 ? 33   PHE B CD2 1 
ATOM   1883 C CE1 . PHE B 1 31  ? -2.344  -32.269 -42.252 1.00 31.65 ? 33   PHE B CE1 1 
ATOM   1884 C CE2 . PHE B 1 31  ? -3.069  -30.707 -40.594 1.00 30.10 ? 33   PHE B CE2 1 
ATOM   1885 C CZ  . PHE B 1 31  ? -2.378  -30.985 -41.752 1.00 31.65 ? 33   PHE B CZ  1 
ATOM   1886 N N   . GLN B 1 32  ? -4.078  -37.682 -40.956 1.00 30.96 ? 34   GLN B N   1 
ATOM   1887 C CA  . GLN B 1 32  ? -3.117  -38.775 -41.004 1.00 30.29 ? 34   GLN B CA  1 
ATOM   1888 C C   . GLN B 1 32  ? -2.185  -38.775 -39.784 1.00 29.63 ? 34   GLN B C   1 
ATOM   1889 O O   . GLN B 1 32  ? -1.020  -39.106 -39.895 1.00 31.84 ? 34   GLN B O   1 
ATOM   1890 C CB  . GLN B 1 32  ? -2.378  -38.757 -42.358 1.00 31.57 ? 34   GLN B CB  1 
ATOM   1891 C CG  . GLN B 1 32  ? -3.336  -38.924 -43.537 1.00 31.85 ? 34   GLN B CG  1 
ATOM   1892 C CD  . GLN B 1 32  ? -2.626  -39.148 -44.864 1.00 36.49 ? 34   GLN B CD  1 
ATOM   1893 O OE1 . GLN B 1 32  ? -1.402  -39.272 -44.940 1.00 36.32 ? 34   GLN B OE1 1 
ATOM   1894 N NE2 . GLN B 1 32  ? -3.384  -39.212 -45.944 1.00 36.58 ? 34   GLN B NE2 1 
ATOM   1895 N N   . GLY B 1 33  ? -2.747  -38.423 -38.634 1.00 28.22 ? 35   GLY B N   1 
ATOM   1896 C CA  . GLY B 1 33  ? -2.063  -38.447 -37.345 1.00 26.52 ? 35   GLY B CA  1 
ATOM   1897 C C   . GLY B 1 33  ? -1.492  -37.131 -36.853 1.00 25.89 ? 35   GLY B C   1 
ATOM   1898 O O   . GLY B 1 33  ? -1.116  -37.054 -35.674 1.00 25.05 ? 35   GLY B O   1 
ATOM   1899 N N   . LYS B 1 34  ? -1.405  -36.078 -37.726 1.00 23.51 ? 36   LYS B N   1 
ATOM   1900 C CA  . LYS B 1 34  ? -0.827  -34.793 -37.239 1.00 20.48 ? 36   LYS B CA  1 
ATOM   1901 C C   . LYS B 1 34  ? -1.856  -33.950 -36.472 1.00 19.18 ? 36   LYS B C   1 
ATOM   1902 O O   . LYS B 1 34  ? -3.039  -33.956 -36.784 1.00 21.45 ? 36   LYS B O   1 
ATOM   1903 C CB  . LYS B 1 34  ? -0.157  -34.016 -38.386 1.00 21.13 ? 36   LYS B CB  1 
ATOM   1904 C CG  . LYS B 1 34  ? 1.127   -34.699 -38.870 1.00 27.42 ? 36   LYS B CG  1 
ATOM   1905 C CD  . LYS B 1 34  ? 1.820   -33.899 -39.900 1.00 32.96 ? 36   LYS B CD  1 
ATOM   1906 C CE  . LYS B 1 34  ? 2.850   -34.706 -40.636 1.00 39.07 ? 36   LYS B CE  1 
ATOM   1907 N NZ  . LYS B 1 34  ? 3.815   -35.372 -39.722 1.00 45.22 ? 36   LYS B NZ  1 
ATOM   1908 N N   . HIS B 1 35  ? -1.408  -33.217 -35.471 1.00 14.74 ? 37   HIS B N   1 
ATOM   1909 C CA  . HIS B 1 35  ? -2.243  -32.376 -34.641 1.00 14.68 ? 37   HIS B CA  1 
ATOM   1910 C C   . HIS B 1 35  ? -2.102  -30.955 -35.212 1.00 14.25 ? 37   HIS B C   1 
ATOM   1911 O O   . HIS B 1 35  ? -1.023  -30.372 -35.112 1.00 12.65 ? 37   HIS B O   1 
ATOM   1912 C CB  . HIS B 1 35  ? -1.745  -32.407 -33.174 1.00 14.87 ? 37   HIS B CB  1 
ATOM   1913 C CG  . HIS B 1 35  ? -1.949  -33.736 -32.515 1.00 16.73 ? 37   HIS B CG  1 
ATOM   1914 N ND1 . HIS B 1 35  ? -1.041  -34.748 -32.660 1.00 17.19 ? 37   HIS B ND1 1 
ATOM   1915 C CD2 . HIS B 1 35  ? -2.966  -34.174 -31.730 1.00 18.49 ? 37   HIS B CD2 1 
ATOM   1916 C CE1 . HIS B 1 35  ? -1.521  -35.791 -31.984 1.00 19.09 ? 37   HIS B CE1 1 
ATOM   1917 N NE2 . HIS B 1 35  ? -2.676  -35.503 -31.412 1.00 19.24 ? 37   HIS B NE2 1 
ATOM   1918 N N   . PRO B 1 36  ? -3.142  -30.406 -35.826 1.00 15.06 ? 38   PRO B N   1 
ATOM   1919 C CA  . PRO B 1 36  ? -3.008  -29.038 -36.370 1.00 13.50 ? 38   PRO B CA  1 
ATOM   1920 C C   . PRO B 1 36  ? -2.950  -27.986 -35.310 1.00 11.69 ? 38   PRO B C   1 
ATOM   1921 O O   . PRO B 1 36  ? -3.542  -28.136 -34.268 1.00 11.07 ? 38   PRO B O   1 
ATOM   1922 C CB  . PRO B 1 36  ? -4.267  -28.880 -37.171 1.00 14.80 ? 38   PRO B CB  1 
ATOM   1923 C CG  . PRO B 1 36  ? -5.248  -29.745 -36.506 1.00 17.12 ? 38   PRO B CG  1 
ATOM   1924 C CD  . PRO B 1 36  ? -4.486  -30.948 -36.081 1.00 15.44 ? 38   PRO B CD  1 
ATOM   1925 N N   . LEU B 1 37  ? -2.246  -26.916 -35.579 1.00 10.93 ? 39   LEU B N   1 
ATOM   1926 C CA  . LEU B 1 37  ? -2.181  -25.770 -34.693 1.00 10.85 ? 39   LEU B CA  1 
ATOM   1927 C C   . LEU B 1 37  ? -3.271  -24.805 -35.034 1.00 11.69 ? 39   LEU B C   1 
ATOM   1928 O O   . LEU B 1 37  ? -3.827  -24.843 -36.130 1.00 13.00 ? 39   LEU B O   1 
ATOM   1929 C CB  . LEU B 1 37  ? -0.829  -25.099 -34.861 1.00 10.91 ? 39   LEU B CB  1 
ATOM   1930 C CG  . LEU B 1 37  ? 0.446   -25.910 -34.497 1.00 11.52 ? 39   LEU B CG  1 
ATOM   1931 C CD1 . LEU B 1 37  ? 1.661   -25.101 -34.823 1.00 11.99 ? 39   LEU B CD1 1 
ATOM   1932 C CD2 . LEU B 1 37  ? 0.435   -26.325 -33.045 1.00 10.50 ? 39   LEU B CD2 1 
ATOM   1933 N N   . GLN B 1 38  ? -3.591  -23.914 -34.120 1.00 10.63 ? 40   GLN B N   1 
ATOM   1934 C CA  . GLN B 1 38  ? -4.495  -22.798 -34.412 1.00 9.86  ? 40   GLN B CA  1 
ATOM   1935 C C   . GLN B 1 38  ? -4.015  -21.917 -35.518 1.00 11.96 ? 40   GLN B C   1 
ATOM   1936 O O   . GLN B 1 38  ? -4.823  -21.483 -36.379 1.00 10.84 ? 40   GLN B O   1 
ATOM   1937 C CB  . GLN B 1 38  ? -4.741  -22.005 -33.165 1.00 9.40  ? 40   GLN B CB  1 
ATOM   1938 C CG  . GLN B 1 38  ? -5.644  -20.816 -33.356 1.00 11.25 ? 40   GLN B CG  1 
ATOM   1939 C CD  . GLN B 1 38  ? -7.037  -21.201 -33.665 1.00 13.26 ? 40   GLN B CD  1 
ATOM   1940 O OE1 . GLN B 1 38  ? -7.498  -22.304 -33.351 1.00 15.15 ? 40   GLN B OE1 1 
ATOM   1941 N NE2 . GLN B 1 38  ? -7.745  -20.305 -34.292 1.00 18.59 ? 40   GLN B NE2 1 
ATOM   1942 N N   . ASN B 1 39  ? -2.728  -21.626 -35.494 1.00 11.93 ? 41   ASN B N   1 
ATOM   1943 C CA  . ASN B 1 39  ? -2.070  -20.738 -36.434 1.00 10.43 ? 41   ASN B CA  1 
ATOM   1944 C C   . ASN B 1 39  ? -0.946  -21.426 -37.141 1.00 9.64  ? 41   ASN B C   1 
ATOM   1945 O O   . ASN B 1 39  ? -0.351  -22.357 -36.633 1.00 11.10 ? 41   ASN B O   1 
ATOM   1946 C CB  . ASN B 1 39  ? -1.511  -19.508 -35.747 1.00 11.97 ? 41   ASN B CB  1 
ATOM   1947 C CG  . ASN B 1 39  ? -2.599  -18.575 -35.372 1.00 14.05 ? 41   ASN B CG  1 
ATOM   1948 O OD1 . ASN B 1 39  ? -3.173  -17.945 -36.261 1.00 15.76 ? 41   ASN B OD1 1 
ATOM   1949 N ND2 . ASN B 1 39  ? -2.957  -18.469 -34.119 1.00 11.93 ? 41   ASN B ND2 1 
ATOM   1950 N N   . ARG B 1 40  ? -0.651  -20.945 -38.347 1.00 10.55 ? 42   ARG B N   1 
ATOM   1951 C CA  . ARG B 1 40  ? 0.573   -21.254 -39.057 1.00 10.13 ? 42   ARG B CA  1 
ATOM   1952 C C   . ARG B 1 40  ? 1.650   -20.274 -38.640 1.00 10.75 ? 42   ARG B C   1 
ATOM   1953 O O   . ARG B 1 40  ? 1.393   -19.054 -38.465 1.00 10.02 ? 42   ARG B O   1 
ATOM   1954 C CB  . ARG B 1 40  ? 0.310   -21.141 -40.570 1.00 10.68 ? 42   ARG B CB  1 
ATOM   1955 C CG  . ARG B 1 40  ? 1.431   -21.458 -41.528 1.00 13.07 ? 42   ARG B CG  1 
ATOM   1956 C CD  . ARG B 1 40  ? 0.920   -21.441 -43.023 1.00 18.71 ? 42   ARG B CD  1 
ATOM   1957 N NE  . ARG B 1 40  ? -0.095  -22.460 -43.070 1.00 19.49 ? 42   ARG B NE  1 
ATOM   1958 C CZ  . ARG B 1 40  ? -1.419  -22.308 -43.179 1.00 18.87 ? 42   ARG B CZ  1 
ATOM   1959 N NH1 . ARG B 1 40  ? -1.957  -21.103 -43.375 1.00 19.43 ? 42   ARG B NH1 1 
ATOM   1960 N NH2 . ARG B 1 40  ? -2.206  -23.351 -43.105 1.00 15.39 ? 42   ARG B NH2 1 
ATOM   1961 N N   . TRP B 1 41  ? 2.874   -20.812 -38.477 1.00 10.23 ? 43   TRP B N   1 
ATOM   1962 C CA  . TRP B 1 41  ? 3.998   -20.044 -37.976 1.00 11.85 ? 43   TRP B CA  1 
ATOM   1963 C C   . TRP B 1 41  ? 5.192   -20.115 -38.902 1.00 10.99 ? 43   TRP B C   1 
ATOM   1964 O O   . TRP B 1 41  ? 5.411   -21.121 -39.548 1.00 11.25 ? 43   TRP B O   1 
ATOM   1965 C CB  . TRP B 1 41  ? 4.404   -20.543 -36.592 1.00 10.36 ? 43   TRP B CB  1 
ATOM   1966 C CG  . TRP B 1 41  ? 3.295   -20.464 -35.559 1.00 9.93  ? 43   TRP B CG  1 
ATOM   1967 C CD1 . TRP B 1 41  ? 2.345   -21.403 -35.300 1.00 10.13 ? 43   TRP B CD1 1 
ATOM   1968 C CD2 . TRP B 1 41  ? 3.087   -19.417 -34.596 1.00 8.21  ? 43   TRP B CD2 1 
ATOM   1969 N NE1 . TRP B 1 41  ? 1.480   -20.959 -34.329 1.00 10.42 ? 43   TRP B NE1 1 
ATOM   1970 C CE2 . TRP B 1 41  ? 1.925   -19.740 -33.867 1.00 10.19 ? 43   TRP B CE2 1 
ATOM   1971 C CE3 . TRP B 1 41  ? 3.675   -18.190 -34.387 1.00 9.38  ? 43   TRP B CE3 1 
ATOM   1972 C CZ2 . TRP B 1 41  ? 1.415   -18.900 -32.864 1.00 9.70  ? 43   TRP B CZ2 1 
ATOM   1973 C CZ3 . TRP B 1 41  ? 3.210   -17.382 -33.387 1.00 9.53  ? 43   TRP B CZ3 1 
ATOM   1974 C CH2 . TRP B 1 41  ? 2.064   -17.709 -32.665 1.00 9.42  ? 43   TRP B CH2 1 
ATOM   1975 N N   . ALA B 1 42  ? 5.945   -19.021 -38.956 1.00 11.62 ? 44   ALA B N   1 
ATOM   1976 C CA  . ALA B 1 42  ? 7.182   -18.897 -39.737 1.00 11.85 ? 44   ALA B CA  1 
ATOM   1977 C C   . ALA B 1 42  ? 8.344   -18.607 -38.827 1.00 11.63 ? 44   ALA B C   1 
ATOM   1978 O O   . ALA B 1 42  ? 8.306   -17.683 -37.992 1.00 11.21 ? 44   ALA B O   1 
ATOM   1979 C CB  . ALA B 1 42  ? 7.057   -17.794 -40.748 1.00 11.86 ? 44   ALA B CB  1 
ATOM   1980 N N   . LEU B 1 43  ? 9.390   -19.407 -38.981 1.00 10.45 ? 45   LEU B N   1 
ATOM   1981 C CA  . LEU B 1 43  ? 10.666  -19.197 -38.309 1.00 10.57 ? 45   LEU B CA  1 
ATOM   1982 C C   . LEU B 1 43  ? 11.669  -18.443 -39.211 1.00 11.34 ? 45   LEU B C   1 
ATOM   1983 O O   . LEU B 1 43  ? 11.922  -18.853 -40.359 1.00 12.34 ? 45   LEU B O   1 
ATOM   1984 C CB  . LEU B 1 43  ? 11.276  -20.550 -37.945 1.00 9.94  ? 45   LEU B CB  1 
ATOM   1985 C CG  . LEU B 1 43  ? 12.664  -20.470 -37.250 1.00 12.52 ? 45   LEU B CG  1 
ATOM   1986 C CD1 . LEU B 1 43  ? 12.562  -19.741 -35.860 1.00 12.30 ? 45   LEU B CD1 1 
ATOM   1987 C CD2 . LEU B 1 43  ? 13.238  -21.855 -37.039 1.00 16.87 ? 45   LEU B CD2 1 
ATOM   1988 N N   . TRP B 1 44  ? 12.187  -17.371 -38.672 1.00 11.35 ? 46   TRP B N   1 
ATOM   1989 C CA  . TRP B 1 44  ? 13.126  -16.459 -39.334 1.00 12.89 ? 46   TRP B CA  1 
ATOM   1990 C C   . TRP B 1 44  ? 14.449  -16.453 -38.567 1.00 14.28 ? 46   TRP B C   1 
ATOM   1991 O O   . TRP B 1 44  ? 14.521  -16.605 -37.337 1.00 13.17 ? 46   TRP B O   1 
ATOM   1992 C CB  . TRP B 1 44  ? 12.584  -15.019 -39.314 1.00 13.31 ? 46   TRP B CB  1 
ATOM   1993 C CG  . TRP B 1 44  ? 11.227  -14.899 -39.928 1.00 14.85 ? 46   TRP B CG  1 
ATOM   1994 C CD1 . TRP B 1 44  ? 10.015  -15.047 -39.302 1.00 16.49 ? 46   TRP B CD1 1 
ATOM   1995 C CD2 . TRP B 1 44  ? 10.945  -14.500 -41.260 1.00 18.91 ? 46   TRP B CD2 1 
ATOM   1996 N NE1 . TRP B 1 44  ? 8.998   -14.808 -40.185 1.00 16.96 ? 46   TRP B NE1 1 
ATOM   1997 C CE2 . TRP B 1 44  ? 9.542   -14.448 -41.398 1.00 19.68 ? 46   TRP B CE2 1 
ATOM   1998 C CE3 . TRP B 1 44  ? 11.749  -14.202 -42.373 1.00 22.10 ? 46   TRP B CE3 1 
ATOM   1999 C CZ2 . TRP B 1 44  ? 8.923   -14.166 -42.611 1.00 23.32 ? 46   TRP B CZ2 1 
ATOM   2000 C CZ3 . TRP B 1 44  ? 11.133  -13.902 -43.578 1.00 24.90 ? 46   TRP B CZ3 1 
ATOM   2001 C CH2 . TRP B 1 44  ? 9.740   -13.859 -43.689 1.00 25.03 ? 46   TRP B CH2 1 
ATOM   2002 N N   . PHE B 1 45  ? 15.519  -16.229 -39.328 1.00 15.14 ? 47   PHE B N   1 
ATOM   2003 C CA  . PHE B 1 45  ? 16.840  -16.033 -38.786 1.00 15.85 ? 47   PHE B CA  1 
ATOM   2004 C C   . PHE B 1 45  ? 17.372  -14.708 -39.279 1.00 16.30 ? 47   PHE B C   1 
ATOM   2005 O O   . PHE B 1 45  ? 17.157  -14.324 -40.433 1.00 17.30 ? 47   PHE B O   1 
ATOM   2006 C CB  . PHE B 1 45  ? 17.739  -17.165 -39.227 1.00 18.41 ? 47   PHE B CB  1 
ATOM   2007 C CG  . PHE B 1 45  ? 19.187  -16.982 -38.922 1.00 20.88 ? 47   PHE B CG  1 
ATOM   2008 C CD1 . PHE B 1 45  ? 19.676  -17.198 -37.653 1.00 21.75 ? 47   PHE B CD1 1 
ATOM   2009 C CD2 . PHE B 1 45  ? 20.069  -16.590 -39.912 1.00 23.94 ? 47   PHE B CD2 1 
ATOM   2010 C CE1 . PHE B 1 45  ? 21.028  -17.051 -37.380 1.00 24.04 ? 47   PHE B CE1 1 
ATOM   2011 C CE2 . PHE B 1 45  ? 21.415  -16.424 -39.630 1.00 25.19 ? 47   PHE B CE2 1 
ATOM   2012 C CZ  . PHE B 1 45  ? 21.884  -16.655 -38.366 1.00 23.79 ? 47   PHE B CZ  1 
ATOM   2013 N N   . PHE B 1 46  ? 18.064  -14.024 -38.411 1.00 14.60 ? 48   PHE B N   1 
ATOM   2014 C CA  . PHE B 1 46  ? 18.761  -12.791 -38.803 1.00 18.70 ? 48   PHE B CA  1 
ATOM   2015 C C   . PHE B 1 46  ? 20.123  -12.762 -38.183 1.00 20.52 ? 48   PHE B C   1 
ATOM   2016 O O   . PHE B 1 46  ? 20.303  -13.065 -37.001 1.00 18.26 ? 48   PHE B O   1 
ATOM   2017 C CB  . PHE B 1 46  ? 17.978  -11.577 -38.384 1.00 21.46 ? 48   PHE B CB  1 
ATOM   2018 C CG  . PHE B 1 46  ? 18.597  -10.284 -38.887 1.00 25.92 ? 48   PHE B CG  1 
ATOM   2019 C CD1 . PHE B 1 46  ? 18.433  -9.883  -40.201 1.00 27.72 ? 48   PHE B CD1 1 
ATOM   2020 C CD2 . PHE B 1 46  ? 19.380  -9.508  -38.058 1.00 29.85 ? 48   PHE B CD2 1 
ATOM   2021 C CE1 . PHE B 1 46  ? 19.027  -8.704  -40.670 1.00 29.51 ? 48   PHE B CE1 1 
ATOM   2022 C CE2 . PHE B 1 46  ? 19.938  -8.306  -38.518 1.00 30.77 ? 48   PHE B CE2 1 
ATOM   2023 C CZ  . PHE B 1 46  ? 19.776  -7.930  -39.820 1.00 30.09 ? 48   PHE B CZ  1 
ATOM   2024 N N   . LYS B 1 47  ? 21.124  -12.387 -38.993 1.00 23.60 ? 49   LYS B N   1 
ATOM   2025 C CA  . LYS B 1 47  ? 22.405  -11.968 -38.395 1.00 28.30 ? 49   LYS B CA  1 
ATOM   2026 C C   . LYS B 1 47  ? 22.897  -10.726 -39.096 1.00 34.29 ? 49   LYS B C   1 
ATOM   2027 O O   . LYS B 1 47  ? 22.990  -10.731 -40.316 1.00 34.25 ? 49   LYS B O   1 
ATOM   2028 C CB  . LYS B 1 47  ? 23.418  -13.085 -38.485 1.00 29.91 ? 49   LYS B CB  1 
ATOM   2029 C CG  . LYS B 1 47  ? 24.636  -12.889 -37.604 1.00 36.17 ? 49   LYS B CG  1 
ATOM   2030 C CD  . LYS B 1 47  ? 25.540  -14.117 -37.676 1.00 40.33 ? 49   LYS B CD  1 
ATOM   2031 C CE  . LYS B 1 47  ? 26.895  -13.851 -37.087 1.00 45.47 ? 49   LYS B CE  1 
ATOM   2032 N NZ  . LYS B 1 47  ? 26.799  -13.307 -35.708 1.00 49.79 ? 49   LYS B NZ  1 
ATOM   2033 N N   . ASN B 1 48  ? 23.168  -9.661  -38.339 1.00 38.62 ? 50   ASN B N   1 
ATOM   2034 C CA  . ASN B 1 48  ? 23.645  -8.405  -38.912 1.00 42.84 ? 50   ASN B CA  1 
ATOM   2035 C C   . ASN B 1 48  ? 25.089  -8.624  -39.344 1.00 46.25 ? 50   ASN B C   1 
ATOM   2036 O O   . ASN B 1 48  ? 26.000  -8.618  -38.510 1.00 46.95 ? 50   ASN B O   1 
ATOM   2037 C CB  . ASN B 1 48  ? 23.509  -7.249  -37.890 1.00 45.75 ? 50   ASN B CB  1 
ATOM   2038 C CG  . ASN B 1 48  ? 23.235  -5.883  -38.485 1.00 51.07 ? 50   ASN B CG  1 
ATOM   2039 O OD1 . ASN B 1 48  ? 23.176  -5.686  -39.715 1.00 52.86 ? 50   ASN B OD1 1 
ATOM   2040 N ND2 . ASN B 1 48  ? 23.068  -4.904  -37.602 1.00 52.75 ? 50   ASN B ND2 1 
ATOM   2041 N N   . ASP B 1 49  ? 25.271  -8.848  -40.657 1.00 48.23 ? 51   ASP B N   1 
ATOM   2042 C CA  . ASP B 1 49  ? 26.548  -8.989  -41.351 1.00 50.23 ? 51   ASP B CA  1 
ATOM   2043 C C   . ASP B 1 49  ? 26.667  -7.853  -42.368 1.00 51.40 ? 51   ASP B C   1 
ATOM   2044 O O   . ASP B 1 49  ? 25.971  -7.849  -43.403 1.00 51.51 ? 51   ASP B O   1 
ATOM   2045 C CB  . ASP B 1 49  ? 26.580  -10.345 -42.074 1.00 52.85 ? 51   ASP B CB  1 
ATOM   2046 C CG  . ASP B 1 49  ? 27.804  -10.612 -42.927 1.00 58.34 ? 51   ASP B CG  1 
ATOM   2047 O OD1 . ASP B 1 49  ? 28.662  -9.720  -43.029 1.00 59.17 ? 51   ASP B OD1 1 
ATOM   2048 O OD2 . ASP B 1 49  ? 27.899  -11.720 -43.494 1.00 60.92 ? 51   ASP B OD2 1 
ATOM   2049 N N   . LYS B 1 50  ? 27.569  -6.897  -42.083 1.00 51.73 ? 52   LYS B N   1 
ATOM   2050 C CA  . LYS B 1 50  ? 27.776  -5.699  -42.910 1.00 52.10 ? 52   LYS B CA  1 
ATOM   2051 C C   . LYS B 1 50  ? 28.262  -6.009  -44.345 1.00 52.12 ? 52   LYS B C   1 
ATOM   2052 O O   . LYS B 1 50  ? 28.128  -5.146  -45.205 1.00 52.98 ? 52   LYS B O   1 
ATOM   2053 C CB  . LYS B 1 50  ? 28.761  -4.743  -42.204 1.00 54.27 ? 52   LYS B CB  1 
ATOM   2054 C CG  . LYS B 1 50  ? 28.744  -3.301  -42.726 1.00 58.44 ? 52   LYS B CG  1 
ATOM   2055 C CD  . LYS B 1 50  ? 30.041  -2.554  -42.372 1.00 62.53 ? 52   LYS B CD  1 
ATOM   2056 C CE  . LYS B 1 50  ? 30.098  -1.176  -42.978 1.00 66.03 ? 52   LYS B CE  1 
ATOM   2057 N NZ  . LYS B 1 50  ? 31.459  -0.578  -42.867 1.00 68.33 ? 52   LYS B NZ  1 
ATOM   2058 N N   . SER B 1 51  ? 28.819  -7.208  -44.615 1.00 51.14 ? 53   SER B N   1 
ATOM   2059 C CA  . SER B 1 51  ? 29.251  -7.567  -45.975 1.00 51.20 ? 53   SER B CA  1 
ATOM   2060 C C   . SER B 1 51  ? 28.072  -7.841  -46.942 1.00 51.36 ? 53   SER B C   1 
ATOM   2061 O O   . SER B 1 51  ? 28.242  -7.684  -48.152 1.00 52.18 ? 53   SER B O   1 
ATOM   2062 C CB  . SER B 1 51  ? 30.182  -8.784  -45.952 1.00 52.10 ? 53   SER B CB  1 
ATOM   2063 O OG  . SER B 1 51  ? 29.502  -10.028 -45.910 1.00 52.58 ? 53   SER B OG  1 
ATOM   2064 N N   . LYS B 1 52  ? 26.897  -8.278  -46.410 1.00 49.68 ? 54   LYS B N   1 
ATOM   2065 C CA  . LYS B 1 52  ? 25.690  -8.520  -47.199 1.00 47.43 ? 54   LYS B CA  1 
ATOM   2066 C C   . LYS B 1 52  ? 24.632  -7.426  -46.922 1.00 44.37 ? 54   LYS B C   1 
ATOM   2067 O O   . LYS B 1 52  ? 24.735  -6.673  -45.949 1.00 43.28 ? 54   LYS B O   1 
ATOM   2068 C CB  . LYS B 1 52  ? 25.089  -9.896  -46.857 1.00 49.28 ? 54   LYS B CB  1 
ATOM   2069 C CG  . LYS B 1 52  ? 26.036  -11.063 -46.973 1.00 53.21 ? 54   LYS B CG  1 
ATOM   2070 C CD  . LYS B 1 52  ? 25.336  -12.326 -46.519 1.00 57.60 ? 54   LYS B CD  1 
ATOM   2071 C CE  . LYS B 1 52  ? 26.207  -13.557 -46.659 1.00 61.57 ? 54   LYS B CE  1 
ATOM   2072 N NZ  . LYS B 1 52  ? 25.408  -14.820 -46.565 1.00 63.93 ? 54   LYS B NZ  1 
ATOM   2073 N N   . THR B 1 53  ? 23.617  -7.345  -47.794 1.00 42.76 ? 55   THR B N   1 
ATOM   2074 C CA  . THR B 1 53  ? 22.489  -6.446  -47.590 1.00 42.72 ? 55   THR B CA  1 
ATOM   2075 C C   . THR B 1 53  ? 21.674  -6.921  -46.377 1.00 43.23 ? 55   THR B C   1 
ATOM   2076 O O   . THR B 1 53  ? 21.777  -8.086  -45.975 1.00 43.81 ? 55   THR B O   1 
ATOM   2077 C CB  . THR B 1 53  ? 21.569  -6.456  -48.835 1.00 43.71 ? 55   THR B CB  1 
ATOM   2078 O OG1 . THR B 1 53  ? 21.130  -7.799  -49.093 1.00 44.66 ? 55   THR B OG1 1 
ATOM   2079 C CG2 . THR B 1 53  ? 22.238  -5.885  -50.055 1.00 43.44 ? 55   THR B CG2 1 
ATOM   2080 N N   . TRP B 1 54  ? 20.853  -6.025  -45.810 1.00 42.75 ? 56   TRP B N   1 
ATOM   2081 C CA  . TRP B 1 54  ? 19.880  -6.366  -44.782 1.00 42.76 ? 56   TRP B CA  1 
ATOM   2082 C C   . TRP B 1 54  ? 18.955  -7.506  -45.261 1.00 42.35 ? 56   TRP B C   1 
ATOM   2083 O O   . TRP B 1 54  ? 18.661  -8.427  -44.481 1.00 42.89 ? 56   TRP B O   1 
ATOM   2084 C CB  . TRP B 1 54  ? 19.055  -5.110  -44.397 1.00 43.66 ? 56   TRP B CB  1 
ATOM   2085 C CG  . TRP B 1 54  ? 17.960  -5.394  -43.416 1.00 45.10 ? 56   TRP B CG  1 
ATOM   2086 C CD1 . TRP B 1 54  ? 18.008  -5.248  -42.063 1.00 46.34 ? 56   TRP B CD1 1 
ATOM   2087 C CD2 . TRP B 1 54  ? 16.659  -5.905  -43.722 1.00 45.79 ? 56   TRP B CD2 1 
ATOM   2088 N NE1 . TRP B 1 54  ? 16.810  -5.643  -41.503 1.00 46.87 ? 56   TRP B NE1 1 
ATOM   2089 C CE2 . TRP B 1 54  ? 15.973  -6.068  -42.503 1.00 46.69 ? 56   TRP B CE2 1 
ATOM   2090 C CE3 . TRP B 1 54  ? 16.006  -6.243  -44.910 1.00 46.60 ? 56   TRP B CE3 1 
ATOM   2091 C CZ2 . TRP B 1 54  ? 14.677  -6.567  -42.445 1.00 47.20 ? 56   TRP B CZ2 1 
ATOM   2092 C CZ3 . TRP B 1 54  ? 14.736  -6.762  -44.850 1.00 47.74 ? 56   TRP B CZ3 1 
ATOM   2093 C CH2 . TRP B 1 54  ? 14.072  -6.898  -43.634 1.00 47.51 ? 56   TRP B CH2 1 
ATOM   2094 N N   . GLN B 1 55  ? 18.518  -7.475  -46.532 1.00 40.53 ? 57   GLN B N   1 
ATOM   2095 C CA  . GLN B 1 55  ? 17.553  -8.455  -47.024 1.00 40.47 ? 57   GLN B CA  1 
ATOM   2096 C C   . GLN B 1 55  ? 18.173  -9.831  -47.126 1.00 39.16 ? 57   GLN B C   1 
ATOM   2097 O O   . GLN B 1 55  ? 17.512  -10.827 -46.846 1.00 38.94 ? 57   GLN B O   1 
ATOM   2098 C CB  . GLN B 1 55  ? 16.991  -8.044  -48.414 1.00 44.07 ? 57   GLN B CB  1 
ATOM   2099 C CG  . GLN B 1 55  ? 15.641  -8.698  -48.723 1.00 51.54 ? 57   GLN B CG  1 
ATOM   2100 C CD  . GLN B 1 55  ? 15.253  -8.554  -50.149 1.00 60.30 ? 57   GLN B CD  1 
ATOM   2101 O OE1 . GLN B 1 55  ? 15.128  -9.549  -50.881 1.00 64.16 ? 57   GLN B OE1 1 
ATOM   2102 N NE2 . GLN B 1 55  ? 15.048  -7.310  -50.577 1.00 61.79 ? 57   GLN B NE2 1 
ATOM   2103 N N   . ALA B 1 56  ? 19.438  -9.899  -47.546 1.00 38.53 ? 58   ALA B N   1 
ATOM   2104 C CA  . ALA B 1 56  ? 20.165  -11.157 -47.577 1.00 37.96 ? 58   ALA B CA  1 
ATOM   2105 C C   . ALA B 1 56  ? 20.512  -11.640 -46.140 1.00 35.10 ? 58   ALA B C   1 
ATOM   2106 O O   . ALA B 1 56  ? 20.742  -12.834 -45.956 1.00 34.98 ? 58   ALA B O   1 
ATOM   2107 C CB  . ALA B 1 56  ? 21.419  -11.002 -48.415 1.00 39.23 ? 58   ALA B CB  1 
ATOM   2108 N N   . ASN B 1 57  ? 20.539  -10.737 -45.145 1.00 32.37 ? 59   ASN B N   1 
ATOM   2109 C CA  . ASN B 1 57  ? 20.735  -11.129 -43.746 1.00 32.32 ? 59   ASN B CA  1 
ATOM   2110 C C   . ASN B 1 57  ? 19.460  -11.711 -43.079 1.00 30.75 ? 59   ASN B C   1 
ATOM   2111 O O   . ASN B 1 57  ? 19.648  -12.505 -42.160 1.00 30.62 ? 59   ASN B O   1 
ATOM   2112 C CB  . ASN B 1 57  ? 21.259  -9.980  -42.886 1.00 34.36 ? 59   ASN B CB  1 
ATOM   2113 C CG  . ASN B 1 57  ? 22.689  -9.600  -43.212 1.00 40.16 ? 59   ASN B CG  1 
ATOM   2114 O OD1 . ASN B 1 57  ? 23.533  -10.461 -43.486 1.00 41.30 ? 59   ASN B OD1 1 
ATOM   2115 N ND2 . ASN B 1 57  ? 22.991  -8.323  -43.175 1.00 42.17 ? 59   ASN B ND2 1 
ATOM   2116 N N   . LEU B 1 58  ? 18.207  -11.308 -43.503 1.00 29.25 ? 60   LEU B N   1 
ATOM   2117 C CA  . LEU B 1 58  ? 16.955  -11.919 -42.995 1.00 28.07 ? 60   LEU B CA  1 
ATOM   2118 C C   . LEU B 1 58  ? 16.593  -13.118 -43.833 1.00 26.94 ? 60   LEU B C   1 
ATOM   2119 O O   . LEU B 1 58  ? 16.466  -13.010 -45.074 1.00 27.71 ? 60   LEU B O   1 
ATOM   2120 C CB  . LEU B 1 58  ? 15.784  -10.923 -42.952 1.00 28.65 ? 60   LEU B CB  1 
ATOM   2121 C CG  . LEU B 1 58  ? 14.474  -11.477 -42.296 1.00 28.84 ? 60   LEU B CG  1 
ATOM   2122 C CD1 . LEU B 1 58  ? 14.595  -11.476 -40.801 1.00 27.39 ? 60   LEU B CD1 1 
ATOM   2123 C CD2 . LEU B 1 58  ? 13.281  -10.706 -42.727 1.00 30.38 ? 60   LEU B CD2 1 
ATOM   2124 N N   . ARG B 1 59  ? 16.433  -14.282 -43.188 1.00 23.05 ? 61   ARG B N   1 
ATOM   2125 C CA  . ARG B 1 59  ? 16.137  -15.512 -43.881 1.00 22.87 ? 61   ARG B CA  1 
ATOM   2126 C C   . ARG B 1 59  ? 14.919  -16.153 -43.278 1.00 22.15 ? 61   ARG B C   1 
ATOM   2127 O O   . ARG B 1 59  ? 14.867  -16.306 -42.062 1.00 22.50 ? 61   ARG B O   1 
ATOM   2128 C CB  . ARG B 1 59  ? 17.293  -16.509 -43.787 1.00 25.30 ? 61   ARG B CB  1 
ATOM   2129 C CG  . ARG B 1 59  ? 18.469  -16.091 -44.668 1.00 34.04 ? 61   ARG B CG  1 
ATOM   2130 C CD  . ARG B 1 59  ? 19.823  -16.587 -44.199 1.00 39.56 ? 61   ARG B CD  1 
ATOM   2131 N NE  . ARG B 1 59  ? 20.090  -17.977 -44.577 1.00 44.07 ? 61   ARG B NE  1 
ATOM   2132 C CZ  . ARG B 1 59  ? 21.309  -18.503 -44.722 1.00 50.91 ? 61   ARG B CZ  1 
ATOM   2133 N NH1 . ARG B 1 59  ? 21.452  -19.778 -45.067 1.00 51.65 ? 61   ARG B NH1 1 
ATOM   2134 N NH2 . ARG B 1 59  ? 22.400  -17.755 -44.526 1.00 52.91 ? 61   ARG B NH2 1 
ATOM   2135 N N   . LEU B 1 60  ? 13.945  -16.514 -44.126 1.00 21.56 ? 62   LEU B N   1 
ATOM   2136 C CA  . LEU B 1 60  ? 12.834  -17.412 -43.757 1.00 21.92 ? 62   LEU B CA  1 
ATOM   2137 C C   . LEU B 1 60  ? 13.399  -18.811 -43.735 1.00 21.98 ? 62   LEU B C   1 
ATOM   2138 O O   . LEU B 1 60  ? 13.892  -19.296 -44.777 1.00 23.32 ? 62   LEU B O   1 
ATOM   2139 C CB  . LEU B 1 60  ? 11.721  -17.355 -44.828 1.00 22.49 ? 62   LEU B CB  1 
ATOM   2140 C CG  . LEU B 1 60  ? 10.571  -18.412 -44.676 1.00 26.03 ? 62   LEU B CG  1 
ATOM   2141 C CD1 . LEU B 1 60  ? 9.891   -18.218 -43.368 1.00 25.48 ? 62   LEU B CD1 1 
ATOM   2142 C CD2 . LEU B 1 60  ? 9.605   -18.291 -45.820 1.00 27.81 ? 62   LEU B CD2 1 
ATOM   2143 N N   . ILE B 1 61  ? 13.378  -19.467 -42.589 1.00 19.05 ? 63   ILE B N   1 
ATOM   2144 C CA  A ILE B 1 61  ? 13.886  -20.824 -42.469 0.50 19.70 ? 63   ILE B CA  1 
ATOM   2145 C CA  B ILE B 1 61  ? 13.890  -20.836 -42.485 0.50 19.77 ? 63   ILE B CA  1 
ATOM   2146 C C   . ILE B 1 61  ? 12.836  -21.837 -42.871 1.00 20.33 ? 63   ILE B C   1 
ATOM   2147 O O   . ILE B 1 61  ? 13.100  -22.737 -43.669 1.00 22.58 ? 63   ILE B O   1 
ATOM   2148 C CB  A ILE B 1 61  ? 14.396  -21.059 -41.020 0.50 19.67 ? 63   ILE B CB  1 
ATOM   2149 C CB  B ILE B 1 61  ? 14.453  -21.154 -41.073 0.50 19.90 ? 63   ILE B CB  1 
ATOM   2150 C CG1 A ILE B 1 61  ? 15.475  -20.025 -40.621 0.50 21.29 ? 63   ILE B CG1 1 
ATOM   2151 C CG1 B ILE B 1 61  ? 15.714  -20.296 -40.805 0.50 21.21 ? 63   ILE B CG1 1 
ATOM   2152 C CG2 A ILE B 1 61  ? 14.923  -22.459 -40.852 0.50 19.81 ? 63   ILE B CG2 1 
ATOM   2153 C CG2 B ILE B 1 61  ? 14.771  -22.654 -40.929 0.50 20.52 ? 63   ILE B CG2 1 
ATOM   2154 C CD1 A ILE B 1 61  ? 16.672  -19.930 -41.632 0.50 21.96 ? 63   ILE B CD1 1 
ATOM   2155 C CD1 B ILE B 1 61  ? 16.498  -20.610 -39.542 0.50 21.27 ? 63   ILE B CD1 1 
ATOM   2156 N N   . SER B 1 62  ? 11.609  -21.717 -42.293 1.00 17.67 ? 64   SER B N   1 
ATOM   2157 C CA  . SER B 1 62  ? 10.621  -22.723 -42.506 1.00 18.05 ? 64   SER B CA  1 
ATOM   2158 C C   . SER B 1 62  ? 9.299   -22.243 -41.938 1.00 16.64 ? 64   SER B C   1 
ATOM   2159 O O   . SER B 1 62  ? 9.283   -21.373 -41.096 1.00 16.06 ? 64   SER B O   1 
ATOM   2160 C CB  . SER B 1 62  ? 11.019  -24.039 -41.818 1.00 23.63 ? 64   SER B CB  1 
ATOM   2161 O OG  . SER B 1 62  ? 10.078  -25.030 -42.164 1.00 33.29 ? 64   SER B OG  1 
ATOM   2162 N N   . LYS B 1 63  ? 8.239   -22.825 -42.420 1.00 15.71 ? 65   LYS B N   1 
ATOM   2163 C CA  . LYS B 1 63  ? 6.896   -22.588 -41.921 1.00 14.04 ? 65   LYS B CA  1 
ATOM   2164 C C   . LYS B 1 63  ? 6.272   -23.924 -41.520 1.00 14.44 ? 65   LYS B C   1 
ATOM   2165 O O   . LYS B 1 63  ? 6.504   -24.955 -42.159 1.00 16.14 ? 65   LYS B O   1 
ATOM   2166 C CB  . LYS B 1 63  ? 6.020   -21.906 -42.946 1.00 12.45 ? 65   LYS B CB  1 
ATOM   2167 C CG  . LYS B 1 63  ? 6.479   -20.534 -43.397 1.00 14.02 ? 65   LYS B CG  1 
ATOM   2168 C CD  . LYS B 1 63  ? 5.404   -19.782 -44.198 1.00 15.92 ? 65   LYS B CD  1 
ATOM   2169 C CE  . LYS B 1 63  ? 5.981   -18.599 -44.921 1.00 17.21 ? 65   LYS B CE  1 
ATOM   2170 N NZ  . LYS B 1 63  ? 4.951   -17.653 -45.417 1.00 21.12 ? 65   LYS B NZ  1 
ATOM   2171 N N   . PHE B 1 64  ? 5.449   -23.906 -40.483 1.00 12.69 ? 66   PHE B N   1 
ATOM   2172 C CA  . PHE B 1 64  ? 4.794   -25.122 -40.000 1.00 12.22 ? 66   PHE B CA  1 
ATOM   2173 C C   . PHE B 1 64  ? 3.458   -24.810 -39.440 1.00 11.71 ? 66   PHE B C   1 
ATOM   2174 O O   . PHE B 1 64  ? 3.202   -23.671 -39.063 1.00 11.97 ? 66   PHE B O   1 
ATOM   2175 C CB  . PHE B 1 64  ? 5.639   -25.913 -38.994 1.00 13.16 ? 66   PHE B CB  1 
ATOM   2176 C CG  . PHE B 1 64  ? 5.929   -25.092 -37.772 1.00 13.06 ? 66   PHE B CG  1 
ATOM   2177 C CD1 . PHE B 1 64  ? 5.060   -25.096 -36.688 1.00 10.93 ? 66   PHE B CD1 1 
ATOM   2178 C CD2 . PHE B 1 64  ? 7.057   -24.310 -37.712 1.00 13.55 ? 66   PHE B CD2 1 
ATOM   2179 C CE1 . PHE B 1 64  ? 5.306   -24.295 -35.590 1.00 12.34 ? 66   PHE B CE1 1 
ATOM   2180 C CE2 . PHE B 1 64  ? 7.287   -23.499 -36.613 1.00 12.63 ? 66   PHE B CE2 1 
ATOM   2181 C CZ  . PHE B 1 64  ? 6.402   -23.512 -35.554 1.00 12.57 ? 66   PHE B CZ  1 
ATOM   2182 N N   . ASP B 1 65  ? 2.587   -25.812 -39.408 1.00 10.77 ? 67   ASP B N   1 
ATOM   2183 C CA  . ASP B 1 65  ? 1.248   -25.614 -38.872 1.00 11.30 ? 67   ASP B CA  1 
ATOM   2184 C C   . ASP B 1 65  ? 0.673   -26.849 -38.136 1.00 10.64 ? 67   ASP B C   1 
ATOM   2185 O O   . ASP B 1 65  ? -0.525  -26.918 -37.929 1.00 11.20 ? 67   ASP B O   1 
ATOM   2186 C CB  . ASP B 1 65  ? 0.322   -25.121 -39.976 1.00 12.26 ? 67   ASP B CB  1 
ATOM   2187 C CG  . ASP B 1 65  ? 0.000   -26.115 -41.074 1.00 16.93 ? 67   ASP B CG  1 
ATOM   2188 O OD1 . ASP B 1 65  ? 0.498   -27.241 -41.006 1.00 15.20 ? 67   ASP B OD1 1 
ATOM   2189 O OD2 . ASP B 1 65  ? -0.747  -25.738 -42.034 1.00 18.38 ? 67   ASP B OD2 1 
ATOM   2190 N N   . THR B 1 66  ? 1.555   -27.804 -37.743 1.00 11.67 ? 68   THR B N   1 
ATOM   2191 C CA  . THR B 1 66  ? 1.201   -28.894 -36.897 1.00 11.35 ? 68   THR B CA  1 
ATOM   2192 C C   . THR B 1 66  ? 2.207   -29.032 -35.748 1.00 10.80 ? 68   THR B C   1 
ATOM   2193 O O   . THR B 1 66  ? 3.351   -28.617 -35.853 1.00 10.73 ? 68   THR B O   1 
ATOM   2194 C CB  . THR B 1 66  ? 1.115   -30.229 -37.670 1.00 12.48 ? 68   THR B CB  1 
ATOM   2195 O OG1 . THR B 1 66  ? 2.394   -30.686 -38.006 1.00 11.71 ? 68   THR B OG1 1 
ATOM   2196 C CG2 . THR B 1 66  ? 0.178   -30.151 -38.924 1.00 15.73 ? 68   THR B CG2 1 
ATOM   2197 N N   . VAL B 1 67  ? 1.773   -29.695 -34.681 1.00 11.23 ? 69   VAL B N   1 
ATOM   2198 C CA  . VAL B 1 67  ? 2.654   -30.013 -33.549 1.00 10.83 ? 69   VAL B CA  1 
ATOM   2199 C C   . VAL B 1 67  ? 3.818   -30.870 -34.019 1.00 11.44 ? 69   VAL B C   1 
ATOM   2200 O O   . VAL B 1 67  ? 4.968   -30.641 -33.634 1.00 12.37 ? 69   VAL B O   1 
ATOM   2201 C CB  . VAL B 1 67  ? 1.876   -30.750 -32.450 1.00 12.05 ? 69   VAL B CB  1 
ATOM   2202 C CG1 . VAL B 1 67  ? 2.830   -31.115 -31.308 1.00 14.02 ? 69   VAL B CG1 1 
ATOM   2203 C CG2 . VAL B 1 67  ? 0.735   -29.915 -31.910 1.00 13.01 ? 69   VAL B CG2 1 
ATOM   2204 N N   . GLU B 1 68  ? 3.514   -31.905 -34.889 1.00 11.65 ? 70   GLU B N   1 
ATOM   2205 C CA  . GLU B 1 68  ? 4.565   -32.824 -35.281 1.00 13.85 ? 70   GLU B CA  1 
ATOM   2206 C C   . GLU B 1 68  ? 5.595   -32.115 -36.146 1.00 13.62 ? 70   GLU B C   1 
ATOM   2207 O O   . GLU B 1 68  ? 6.786   -32.391 -36.031 1.00 13.46 ? 70   GLU B O   1 
ATOM   2208 C CB  . GLU B 1 68  ? 3.986   -34.050 -36.009 1.00 14.16 ? 70   GLU B CB  1 
ATOM   2209 C CG  . GLU B 1 68  ? 3.180   -34.939 -35.102 1.00 17.38 ? 70   GLU B CG  1 
ATOM   2210 C CD  . GLU B 1 68  ? 1.829   -34.492 -34.594 1.00 18.17 ? 70   GLU B CD  1 
ATOM   2211 O OE1 . GLU B 1 68  ? 1.289   -33.455 -35.047 1.00 12.44 ? 70   GLU B OE1 1 
ATOM   2212 O OE2 . GLU B 1 68  ? 1.291   -35.216 -33.726 1.00 22.30 ? 70   GLU B OE2 1 
ATOM   2213 N N   . ASP B 1 69  ? 5.149   -31.179 -37.024 1.00 11.90 ? 71   ASP B N   1 
ATOM   2214 C CA  . ASP B 1 69  ? 6.084   -30.438 -37.880 1.00 10.83 ? 71   ASP B CA  1 
ATOM   2215 C C   . ASP B 1 69  ? 6.888   -29.398 -37.075 1.00 11.33 ? 71   ASP B C   1 
ATOM   2216 O O   . ASP B 1 69  ? 8.056   -29.109 -37.387 1.00 12.44 ? 71   ASP B O   1 
ATOM   2217 C CB  . ASP B 1 69  ? 5.334   -29.765 -39.009 1.00 13.01 ? 71   ASP B CB  1 
ATOM   2218 C CG  . ASP B 1 69  ? 4.720   -30.751 -40.008 1.00 17.39 ? 71   ASP B CG  1 
ATOM   2219 O OD1 . ASP B 1 69  ? 5.394   -31.762 -40.328 1.00 18.29 ? 71   ASP B OD1 1 
ATOM   2220 O OD2 . ASP B 1 69  ? 3.545   -30.506 -40.443 1.00 16.94 ? 71   ASP B OD2 1 
ATOM   2221 N N   . PHE B 1 70  ? 6.282   -28.871 -35.992 1.00 11.35 ? 72   PHE B N   1 
ATOM   2222 C CA  . PHE B 1 70  ? 7.037   -28.012 -35.055 1.00 10.71 ? 72   PHE B CA  1 
ATOM   2223 C C   . PHE B 1 70  ? 8.211   -28.842 -34.471 1.00 10.25 ? 72   PHE B C   1 
ATOM   2224 O O   . PHE B 1 70  ? 9.360   -28.392 -34.490 1.00 11.63 ? 72   PHE B O   1 
ATOM   2225 C CB  . PHE B 1 70  ? 6.119   -27.528 -33.942 1.00 9.64  ? 72   PHE B CB  1 
ATOM   2226 C CG  . PHE B 1 70  ? 6.912   -27.031 -32.759 1.00 10.39 ? 72   PHE B CG  1 
ATOM   2227 C CD1 . PHE B 1 70  ? 7.501   -25.782 -32.783 1.00 10.97 ? 72   PHE B CD1 1 
ATOM   2228 C CD2 . PHE B 1 70  ? 7.102   -27.829 -31.653 1.00 11.42 ? 72   PHE B CD2 1 
ATOM   2229 C CE1 . PHE B 1 70  ? 8.251   -25.337 -31.686 1.00 11.98 ? 72   PHE B CE1 1 
ATOM   2230 C CE2 . PHE B 1 70  ? 7.851   -27.390 -30.577 1.00 10.57 ? 72   PHE B CE2 1 
ATOM   2231 C CZ  . PHE B 1 70  ? 8.431   -26.143 -30.613 1.00 10.86 ? 72   PHE B CZ  1 
ATOM   2232 N N   . TRP B 1 71  ? 7.907   -30.061 -33.975 1.00 10.35 ? 73   TRP B N   1 
ATOM   2233 C CA  . TRP B 1 71  ? 8.967   -30.881 -33.363 1.00 12.00 ? 73   TRP B CA  1 
ATOM   2234 C C   . TRP B 1 71  ? 9.984   -31.308 -34.389 1.00 13.37 ? 73   TRP B C   1 
ATOM   2235 O O   . TRP B 1 71  ? 11.166  -31.345 -34.064 1.00 13.69 ? 73   TRP B O   1 
ATOM   2236 C CB  . TRP B 1 71  ? 8.424   -32.048 -32.577 1.00 13.11 ? 73   TRP B CB  1 
ATOM   2237 C CG  . TRP B 1 71  ? 7.796   -31.680 -31.275 1.00 13.25 ? 73   TRP B CG  1 
ATOM   2238 C CD1 . TRP B 1 71  ? 6.496   -31.879 -30.908 1.00 13.18 ? 73   TRP B CD1 1 
ATOM   2239 C CD2 . TRP B 1 71  ? 8.430   -31.039 -30.163 1.00 12.91 ? 73   TRP B CD2 1 
ATOM   2240 N NE1 . TRP B 1 71  ? 6.295   -31.418 -29.626 1.00 13.10 ? 73   TRP B NE1 1 
ATOM   2241 C CE2 . TRP B 1 71  ? 7.464   -30.912 -29.146 1.00 13.41 ? 73   TRP B CE2 1 
ATOM   2242 C CE3 . TRP B 1 71  ? 9.727   -30.540 -29.928 1.00 13.22 ? 73   TRP B CE3 1 
ATOM   2243 C CZ2 . TRP B 1 71  ? 7.759   -30.314 -27.913 1.00 14.15 ? 73   TRP B CZ2 1 
ATOM   2244 C CZ3 . TRP B 1 71  ? 10.029  -30.026 -28.676 1.00 13.39 ? 73   TRP B CZ3 1 
ATOM   2245 C CH2 . TRP B 1 71  ? 9.061   -29.919 -27.695 1.00 14.48 ? 73   TRP B CH2 1 
ATOM   2246 N N   . ALA B 1 72  ? 9.568   -31.622 -35.640 1.00 13.09 ? 74   ALA B N   1 
ATOM   2247 C CA  . ALA B 1 72  ? 10.551  -31.982 -36.669 1.00 14.92 ? 74   ALA B CA  1 
ATOM   2248 C C   . ALA B 1 72  ? 11.536  -30.864 -36.935 1.00 14.79 ? 74   ALA B C   1 
ATOM   2249 O O   . ALA B 1 72  ? 12.744  -31.101 -37.082 1.00 14.73 ? 74   ALA B O   1 
ATOM   2250 C CB  . ALA B 1 72  ? 9.846   -32.402 -37.945 1.00 15.23 ? 74   ALA B CB  1 
ATOM   2251 N N   . LEU B 1 73  ? 11.036  -29.620 -36.982 1.00 14.05 ? 75   LEU B N   1 
ATOM   2252 C CA  . LEU B 1 73  ? 11.850  -28.426 -37.129 1.00 13.50 ? 75   LEU B CA  1 
ATOM   2253 C C   . LEU B 1 73  ? 12.743  -28.210 -35.904 1.00 13.43 ? 75   LEU B C   1 
ATOM   2254 O O   . LEU B 1 73  ? 13.932  -28.026 -36.035 1.00 15.07 ? 75   LEU B O   1 
ATOM   2255 C CB  . LEU B 1 73  ? 10.973  -27.223 -37.384 1.00 13.95 ? 75   LEU B CB  1 
ATOM   2256 C CG  . LEU B 1 73  ? 11.741  -25.901 -37.632 1.00 14.32 ? 75   LEU B CG  1 
ATOM   2257 C CD1 . LEU B 1 73  ? 12.699  -25.996 -38.916 1.00 14.66 ? 75   LEU B CD1 1 
ATOM   2258 C CD2 . LEU B 1 73  ? 10.793  -24.732 -37.788 1.00 15.26 ? 75   LEU B CD2 1 
ATOM   2259 N N   . TYR B 1 74  ? 12.190  -28.320 -34.714 1.00 13.72 ? 76   TYR B N   1 
ATOM   2260 C CA  . TYR B 1 74  ? 12.916  -28.165 -33.457 1.00 13.67 ? 76   TYR B CA  1 
ATOM   2261 C C   . TYR B 1 74  ? 14.080  -29.109 -33.399 1.00 16.50 ? 76   TYR B C   1 
ATOM   2262 O O   . TYR B 1 74  ? 15.205  -28.707 -33.152 1.00 17.79 ? 76   TYR B O   1 
ATOM   2263 C CB  . TYR B 1 74  ? 11.990  -28.383 -32.266 1.00 13.87 ? 76   TYR B CB  1 
ATOM   2264 C CG  . TYR B 1 74  ? 12.624  -28.006 -30.952 1.00 13.43 ? 76   TYR B CG  1 
ATOM   2265 C CD1 . TYR B 1 74  ? 12.542  -26.714 -30.469 1.00 14.71 ? 76   TYR B CD1 1 
ATOM   2266 C CD2 . TYR B 1 74  ? 13.355  -28.925 -30.222 1.00 14.55 ? 76   TYR B CD2 1 
ATOM   2267 C CE1 . TYR B 1 74  ? 13.158  -26.347 -29.275 1.00 16.67 ? 76   TYR B CE1 1 
ATOM   2268 C CE2 . TYR B 1 74  ? 13.941  -28.581 -29.000 1.00 15.37 ? 76   TYR B CE2 1 
ATOM   2269 C CZ  . TYR B 1 74  ? 13.870  -27.287 -28.551 1.00 17.50 ? 76   TYR B CZ  1 
ATOM   2270 O OH  . TYR B 1 74  ? 14.491  -26.920 -27.381 1.00 19.61 ? 76   TYR B OH  1 
ATOM   2271 N N   . ASN B 1 75  ? 13.785  -30.395 -33.680 1.00 16.82 ? 77   ASN B N   1 
ATOM   2272 C CA  . ASN B 1 75  ? 14.831  -31.418 -33.688 1.00 17.20 ? 77   ASN B CA  1 
ATOM   2273 C C   . ASN B 1 75  ? 15.955  -31.154 -34.676 1.00 19.51 ? 77   ASN B C   1 
ATOM   2274 O O   . ASN B 1 75  ? 17.111  -31.425 -34.341 1.00 21.84 ? 77   ASN B O   1 
ATOM   2275 C CB  . ASN B 1 75  ? 14.233  -32.795 -33.946 1.00 17.40 ? 77   ASN B CB  1 
ATOM   2276 C CG  . ASN B 1 75  ? 13.276  -33.259 -32.890 1.00 22.85 ? 77   ASN B CG  1 
ATOM   2277 O OD1 . ASN B 1 75  ? 13.251  -32.780 -31.775 1.00 20.83 ? 77   ASN B OD1 1 
ATOM   2278 N ND2 . ASN B 1 75  ? 12.424  -34.230 -33.233 1.00 26.22 ? 77   ASN B ND2 1 
ATOM   2279 N N   . HIS B 1 76  ? 15.635  -30.681 -35.862 1.00 18.48 ? 78   HIS B N   1 
ATOM   2280 C CA  . HIS B 1 76  ? 16.563  -30.333 -36.918 1.00 20.43 ? 78   HIS B CA  1 
ATOM   2281 C C   . HIS B 1 76  ? 17.374  -29.141 -36.572 1.00 21.46 ? 78   HIS B C   1 
ATOM   2282 O O   . HIS B 1 76  ? 18.589  -29.138 -36.799 1.00 23.42 ? 78   HIS B O   1 
ATOM   2283 C CB  . HIS B 1 76  ? 15.797  -30.072 -38.231 1.00 23.16 ? 78   HIS B CB  1 
ATOM   2284 C CG  . HIS B 1 76  ? 16.601  -29.490 -39.350 1.00 30.78 ? 78   HIS B CG  1 
ATOM   2285 N ND1 . HIS B 1 76  ? 16.483  -28.153 -39.693 1.00 34.60 ? 78   HIS B ND1 1 
ATOM   2286 C CD2 . HIS B 1 76  ? 17.496  -30.074 -40.175 1.00 33.69 ? 78   HIS B CD2 1 
ATOM   2287 C CE1 . HIS B 1 76  ? 17.301  -27.968 -40.716 1.00 35.22 ? 78   HIS B CE1 1 
ATOM   2288 N NE2 . HIS B 1 76  ? 17.946  -29.092 -41.024 1.00 35.45 ? 78   HIS B NE2 1 
ATOM   2289 N N   . ILE B 1 77  ? 16.747  -28.085 -36.059 1.00 19.18 ? 79   ILE B N   1 
ATOM   2290 C CA  . ILE B 1 77  ? 17.501  -26.869 -35.645 1.00 20.87 ? 79   ILE B CA  1 
ATOM   2291 C C   . ILE B 1 77  ? 18.446  -27.246 -34.515 1.00 21.90 ? 79   ILE B C   1 
ATOM   2292 O O   . ILE B 1 77  ? 19.579  -26.786 -34.471 1.00 23.20 ? 79   ILE B O   1 
ATOM   2293 C CB  . ILE B 1 77  ? 16.526  -25.748 -35.195 1.00 20.90 ? 79   ILE B CB  1 
ATOM   2294 C CG1 . ILE B 1 77  ? 15.693  -25.206 -36.366 1.00 22.78 ? 79   ILE B CG1 1 
ATOM   2295 C CG2 . ILE B 1 77  ? 17.231  -24.628 -34.422 1.00 22.50 ? 79   ILE B CG2 1 
ATOM   2296 C CD1 . ILE B 1 77  ? 16.406  -24.583 -37.492 1.00 25.63 ? 79   ILE B CD1 1 
ATOM   2297 N N   . GLN B 1 78  ? 17.981  -28.066 -33.593 1.00 24.23 ? 80   GLN B N   1 
ATOM   2298 C CA  . GLN B 1 78  ? 18.797  -28.526 -32.461 1.00 28.22 ? 80   GLN B CA  1 
ATOM   2299 C C   . GLN B 1 78  ? 20.101  -29.222 -32.962 1.00 33.67 ? 80   GLN B C   1 
ATOM   2300 O O   . GLN B 1 78  ? 21.106  -29.180 -32.281 1.00 33.71 ? 80   GLN B O   1 
ATOM   2301 C CB  . GLN B 1 78  ? 17.951  -29.464 -31.599 1.00 29.13 ? 80   GLN B CB  1 
ATOM   2302 C CG  . GLN B 1 78  ? 18.446  -29.758 -30.176 1.00 32.00 ? 80   GLN B CG  1 
ATOM   2303 C CD  . GLN B 1 78  ? 17.520  -30.740 -29.495 1.00 33.02 ? 80   GLN B CD  1 
ATOM   2304 O OE1 . GLN B 1 78  ? 16.810  -31.509 -30.139 1.00 36.54 ? 80   GLN B OE1 1 
ATOM   2305 N NE2 . GLN B 1 78  ? 17.490  -30.731 -28.189 1.00 32.13 ? 80   GLN B NE2 1 
ATOM   2306 N N   . LEU B 1 79  ? 20.065  -29.800 -34.179 1.00 38.19 ? 81   LEU B N   1 
ATOM   2307 C CA  . LEU B 1 79  ? 21.166  -30.511 -34.841 1.00 42.51 ? 81   LEU B CA  1 
ATOM   2308 C C   . LEU B 1 79  ? 21.958  -29.619 -35.803 1.00 44.96 ? 81   LEU B C   1 
ATOM   2309 O O   . LEU B 1 79  ? 23.181  -29.755 -35.891 1.00 45.83 ? 81   LEU B O   1 
ATOM   2310 C CB  . LEU B 1 79  ? 20.521  -31.655 -35.661 1.00 43.87 ? 81   LEU B CB  1 
ATOM   2311 C CG  . LEU B 1 79  ? 21.191  -33.003 -35.792 1.00 46.49 ? 81   LEU B CG  1 
ATOM   2312 C CD1 . LEU B 1 79  ? 21.674  -33.524 -34.450 1.00 47.07 ? 81   LEU B CD1 1 
ATOM   2313 C CD2 . LEU B 1 79  ? 20.197  -33.957 -36.396 1.00 47.93 ? 81   LEU B CD2 1 
ATOM   2314 N N   . SER B 1 80  ? 21.273  -28.735 -36.537 1.00 46.05 ? 82   SER B N   1 
ATOM   2315 C CA  . SER B 1 80  ? 21.822  -27.889 -37.593 1.00 47.84 ? 82   SER B CA  1 
ATOM   2316 C C   . SER B 1 80  ? 21.262  -26.497 -37.461 1.00 48.09 ? 82   SER B C   1 
ATOM   2317 O O   . SER B 1 80  ? 20.166  -26.213 -37.987 1.00 49.54 ? 82   SER B O   1 
ATOM   2318 C CB  . SER B 1 80  ? 21.457  -28.436 -38.967 1.00 52.16 ? 82   SER B CB  1 
ATOM   2319 O OG  . SER B 1 80  ? 20.071  -28.727 -39.069 1.00 57.17 ? 82   SER B OG  1 
ATOM   2320 N N   . SER B 1 81  ? 22.004  -25.629 -36.744 1.00 46.14 ? 83   SER B N   1 
ATOM   2321 C CA  . SER B 1 81  ? 21.760  -24.181 -36.690 1.00 44.83 ? 83   SER B CA  1 
ATOM   2322 C C   . SER B 1 81  ? 22.815  -23.475 -35.840 1.00 43.81 ? 83   SER B C   1 
ATOM   2323 O O   . SER B 1 81  ? 23.412  -24.105 -34.971 1.00 45.03 ? 83   SER B O   1 
ATOM   2324 C CB  . SER B 1 81  ? 20.408  -23.899 -36.061 1.00 47.05 ? 83   SER B CB  1 
ATOM   2325 O OG  . SER B 1 81  ? 20.431  -24.445 -34.750 1.00 49.46 ? 83   SER B OG  1 
ATOM   2326 N N   . ASN B 1 82  ? 23.012  -22.182 -36.059 1.00 42.04 ? 84   ASN B N   1 
ATOM   2327 C CA  . ASN B 1 82  ? 24.080  -21.436 -35.422 1.00 41.16 ? 84   ASN B CA  1 
ATOM   2328 C C   . ASN B 1 82  ? 23.604  -20.764 -34.136 1.00 38.12 ? 84   ASN B C   1 
ATOM   2329 O O   . ASN B 1 82  ? 22.569  -20.090 -34.127 1.00 37.89 ? 84   ASN B O   1 
ATOM   2330 C CB  . ASN B 1 82  ? 24.599  -20.396 -36.405 1.00 44.46 ? 84   ASN B CB  1 
ATOM   2331 C CG  . ASN B 1 82  ? 25.922  -19.826 -36.004 1.00 51.16 ? 84   ASN B CG  1 
ATOM   2332 O OD1 . ASN B 1 82  ? 26.022  -18.646 -35.702 1.00 53.74 ? 84   ASN B OD1 1 
ATOM   2333 N ND2 . ASN B 1 82  ? 26.967  -20.660 -35.998 1.00 53.48 ? 84   ASN B ND2 1 
ATOM   2334 N N   . LEU B 1 83  ? 24.348  -20.967 -33.054 1.00 35.03 ? 85   LEU B N   1 
ATOM   2335 C CA  . LEU B 1 83  ? 24.088  -20.324 -31.779 1.00 32.83 ? 85   LEU B CA  1 
ATOM   2336 C C   . LEU B 1 83  ? 25.332  -19.532 -31.491 1.00 31.10 ? 85   LEU B C   1 
ATOM   2337 O O   . LEU B 1 83  ? 26.209  -19.994 -30.756 1.00 32.69 ? 85   LEU B O   1 
ATOM   2338 C CB  . LEU B 1 83  ? 23.832  -21.346 -30.649 1.00 32.80 ? 85   LEU B CB  1 
ATOM   2339 C CG  . LEU B 1 83  ? 23.531  -20.742 -29.246 1.00 35.42 ? 85   LEU B CG  1 
ATOM   2340 C CD1 . LEU B 1 83  ? 22.170  -20.209 -29.181 1.00 36.10 ? 85   LEU B CD1 1 
ATOM   2341 C CD2 . LEU B 1 83  ? 23.721  -21.754 -28.143 1.00 37.07 ? 85   LEU B CD2 1 
ATOM   2342 N N   . MET B 1 84  ? 25.429  -18.341 -32.074 1.00 28.42 ? 86   MET B N   1 
ATOM   2343 C CA  . MET B 1 84  ? 26.593  -17.481 -31.840 1.00 26.68 ? 86   MET B CA  1 
ATOM   2344 C C   . MET B 1 84  ? 26.111  -16.068 -31.558 1.00 25.46 ? 86   MET B C   1 
ATOM   2345 O O   . MET B 1 84  ? 24.995  -15.722 -31.973 1.00 23.84 ? 86   MET B O   1 
ATOM   2346 C CB  . MET B 1 84  ? 27.451  -17.464 -33.088 1.00 27.05 ? 86   MET B CB  1 
ATOM   2347 C CG  . MET B 1 84  ? 28.175  -18.751 -33.319 1.00 29.11 ? 86   MET B CG  1 
ATOM   2348 S SD  . MET B 1 84  ? 29.637  -18.981 -32.252 1.00 29.79 ? 86   MET B SD  1 
ATOM   2349 C CE  . MET B 1 84  ? 30.708  -17.887 -32.951 1.00 27.21 ? 86   MET B CE  1 
ATOM   2350 N N   . PRO B 1 85  ? 26.933  -15.211 -30.902 1.00 24.97 ? 87   PRO B N   1 
ATOM   2351 C CA  . PRO B 1 85  ? 26.494  -13.833 -30.653 1.00 24.34 ? 87   PRO B CA  1 
ATOM   2352 C C   . PRO B 1 85  ? 26.182  -13.141 -31.973 1.00 24.92 ? 87   PRO B C   1 
ATOM   2353 O O   . PRO B 1 85  ? 26.884  -13.337 -32.981 1.00 24.72 ? 87   PRO B O   1 
ATOM   2354 C CB  . PRO B 1 85  ? 27.690  -13.164 -29.938 1.00 26.25 ? 87   PRO B CB  1 
ATOM   2355 C CG  . PRO B 1 85  ? 28.508  -14.274 -29.432 1.00 26.97 ? 87   PRO B CG  1 
ATOM   2356 C CD  . PRO B 1 85  ? 28.318  -15.422 -30.423 1.00 25.47 ? 87   PRO B CD  1 
ATOM   2357 N N   . GLY B 1 86  ? 25.140  -12.325 -31.937 1.00 23.98 ? 88   GLY B N   1 
ATOM   2358 C CA  . GLY B 1 86  ? 24.625  -11.605 -33.082 1.00 24.80 ? 88   GLY B CA  1 
ATOM   2359 C C   . GLY B 1 86  ? 23.499  -12.325 -33.809 1.00 24.73 ? 88   GLY B C   1 
ATOM   2360 O O   . GLY B 1 86  ? 22.870  -11.733 -34.706 1.00 26.02 ? 88   GLY B O   1 
ATOM   2361 N N   . CYS B 1 87  ? 23.203  -13.597 -33.458 1.00 22.27 ? 89   CYS B N   1 
ATOM   2362 C CA  . CYS B 1 87  ? 22.105  -14.303 -34.101 1.00 21.82 ? 89   CYS B CA  1 
ATOM   2363 C C   . CYS B 1 87  ? 20.785  -13.821 -33.442 1.00 20.36 ? 89   CYS B C   1 
ATOM   2364 O O   . CYS B 1 87  ? 20.705  -13.594 -32.233 1.00 18.64 ? 89   CYS B O   1 
ATOM   2365 C CB  . CYS B 1 87  ? 22.259  -15.812 -33.986 1.00 24.18 ? 89   CYS B CB  1 
ATOM   2366 S SG  . CYS B 1 87  ? 23.672  -16.476 -34.898 1.00 34.88 ? 89   CYS B SG  1 
ATOM   2367 N N   . ASP B 1 88  ? 19.758  -13.671 -34.277 1.00 19.59 ? 90   ASP B N   1 
ATOM   2368 C CA  . ASP B 1 88  ? 18.406  -13.489 -33.792 1.00 17.74 ? 90   ASP B CA  1 
ATOM   2369 C C   . ASP B 1 88  ? 17.548  -14.579 -34.453 1.00 16.85 ? 90   ASP B C   1 
ATOM   2370 O O   . ASP B 1 88  ? 17.660  -14.776 -35.655 1.00 16.64 ? 90   ASP B O   1 
ATOM   2371 C CB  . ASP B 1 88  ? 17.822  -12.135 -34.150 1.00 20.56 ? 90   ASP B CB  1 
ATOM   2372 C CG  . ASP B 1 88  ? 18.540  -10.908 -33.647 1.00 29.07 ? 90   ASP B CG  1 
ATOM   2373 O OD1 . ASP B 1 88  ? 19.191  -10.992 -32.573 1.00 25.86 ? 90   ASP B OD1 1 
ATOM   2374 O OD2 . ASP B 1 88  ? 18.430  -9.855  -34.311 1.00 33.85 ? 90   ASP B OD2 1 
ATOM   2375 N N   . TYR B 1 89  ? 16.651  -15.249 -33.690 1.00 14.45 ? 91   TYR B N   1 
ATOM   2376 C CA  . TYR B 1 89  ? 15.660  -16.141 -34.272 1.00 12.20 ? 91   TYR B CA  1 
ATOM   2377 C C   . TYR B 1 89  ? 14.284  -15.632 -33.886 1.00 10.18 ? 91   TYR B C   1 
ATOM   2378 O O   . TYR B 1 89  ? 14.110  -15.159 -32.777 1.00 10.77 ? 91   TYR B O   1 
ATOM   2379 C CB  . TYR B 1 89  ? 15.816  -17.571 -33.773 1.00 13.16 ? 91   TYR B CB  1 
ATOM   2380 C CG  . TYR B 1 89  ? 17.045  -18.274 -34.330 1.00 16.74 ? 91   TYR B CG  1 
ATOM   2381 C CD1 . TYR B 1 89  ? 18.256  -18.172 -33.697 1.00 17.72 ? 91   TYR B CD1 1 
ATOM   2382 C CD2 . TYR B 1 89  ? 16.958  -19.076 -35.457 1.00 18.80 ? 91   TYR B CD2 1 
ATOM   2383 C CE1 . TYR B 1 89  ? 19.371  -18.888 -34.154 1.00 20.14 ? 91   TYR B CE1 1 
ATOM   2384 C CE2 . TYR B 1 89  ? 18.044  -19.789 -35.918 1.00 20.17 ? 91   TYR B CE2 1 
ATOM   2385 C CZ  . TYR B 1 89  ? 19.255  -19.681 -35.273 1.00 22.65 ? 91   TYR B CZ  1 
ATOM   2386 O OH  . TYR B 1 89  ? 20.329  -20.370 -35.790 1.00 27.62 ? 91   TYR B OH  1 
ATOM   2387 N N   . SER B 1 90  ? 13.345  -15.705 -34.774 1.00 9.64  ? 92   SER B N   1 
ATOM   2388 C CA  . SER B 1 90  ? 12.008  -15.143 -34.548 1.00 9.08  ? 92   SER B CA  1 
ATOM   2389 C C   . SER B 1 90  ? 10.970  -16.118 -35.022 1.00 10.67 ? 92   SER B C   1 
ATOM   2390 O O   . SER B 1 90  ? 11.087  -16.617 -36.155 1.00 12.39 ? 92   SER B O   1 
ATOM   2391 C CB  . SER B 1 90  ? 11.835  -13.849 -35.303 1.00 12.53 ? 92   SER B CB  1 
ATOM   2392 O OG  . SER B 1 90  ? 12.814  -12.883 -34.974 1.00 15.65 ? 92   SER B OG  1 
ATOM   2393 N N   . LEU B 1 91  ? 9.943   -16.397 -34.203 1.00 8.84  ? 93   LEU B N   1 
ATOM   2394 C CA  . LEU B 1 91  ? 8.824   -17.226 -34.657 1.00 8.40  ? 93   LEU B CA  1 
ATOM   2395 C C   . LEU B 1 91  ? 7.617   -16.321 -34.692 1.00 9.11  ? 93   LEU B C   1 
ATOM   2396 O O   . LEU B 1 91  ? 7.224   -15.832 -33.622 1.00 8.42  ? 93   LEU B O   1 
ATOM   2397 C CB  . LEU B 1 91  ? 8.525   -18.397 -33.737 1.00 9.82  ? 93   LEU B CB  1 
ATOM   2398 C CG  . LEU B 1 91  ? 7.464   -19.360 -34.306 1.00 9.58  ? 93   LEU B CG  1 
ATOM   2399 C CD1 . LEU B 1 91  ? 8.004   -20.138 -35.464 1.00 10.01 ? 93   LEU B CD1 1 
ATOM   2400 C CD2 . LEU B 1 91  ? 6.898   -20.278 -33.209 1.00 10.85 ? 93   LEU B CD2 1 
ATOM   2401 N N   . PHE B 1 92  ? 7.048   -16.053 -35.871 1.00 9.87  ? 94   PHE B N   1 
ATOM   2402 C CA  . PHE B 1 92  ? 5.913   -15.121 -36.033 1.00 10.36 ? 94   PHE B CA  1 
ATOM   2403 C C   . PHE B 1 92  ? 4.816   -15.820 -36.757 1.00 9.81  ? 94   PHE B C   1 
ATOM   2404 O O   . PHE B 1 92  ? 5.031   -16.673 -37.608 1.00 9.70  ? 94   PHE B O   1 
ATOM   2405 C CB  . PHE B 1 92  ? 6.286   -13.815 -36.787 1.00 10.72 ? 94   PHE B CB  1 
ATOM   2406 C CG  . PHE B 1 92  ? 6.862   -12.797 -35.840 1.00 10.18 ? 94   PHE B CG  1 
ATOM   2407 C CD1 . PHE B 1 92  ? 8.075   -13.026 -35.205 1.00 11.25 ? 94   PHE B CD1 1 
ATOM   2408 C CD2 . PHE B 1 92  ? 6.188   -11.629 -35.568 1.00 9.38  ? 94   PHE B CD2 1 
ATOM   2409 C CE1 . PHE B 1 92  ? 8.587   -12.132 -34.289 1.00 13.37 ? 94   PHE B CE1 1 
ATOM   2410 C CE2 . PHE B 1 92  ? 6.711   -10.700 -34.668 1.00 10.51 ? 94   PHE B CE2 1 
ATOM   2411 C CZ  . PHE B 1 92  ? 7.929   -10.937 -34.048 1.00 11.43 ? 94   PHE B CZ  1 
ATOM   2412 N N   . LYS B 1 93  ? 3.579   -15.437 -36.458 1.00 8.88  ? 95   LYS B N   1 
ATOM   2413 C CA  . LYS B 1 93  ? 2.418   -15.902 -37.210 1.00 8.64  ? 95   LYS B CA  1 
ATOM   2414 C C   . LYS B 1 93  ? 2.596   -15.624 -38.684 1.00 10.33 ? 95   LYS B C   1 
ATOM   2415 O O   . LYS B 1 93  ? 3.169   -14.565 -39.058 1.00 11.36 ? 95   LYS B O   1 
ATOM   2416 C CB  . LYS B 1 93  ? 1.163   -15.206 -36.730 1.00 8.97  ? 95   LYS B CB  1 
ATOM   2417 C CG  . LYS B 1 93  ? 0.761   -15.644 -35.312 1.00 9.80  ? 95   LYS B CG  1 
ATOM   2418 C CD  . LYS B 1 93  ? -0.541  -15.012 -34.852 1.00 11.24 ? 95   LYS B CD  1 
ATOM   2419 C CE  . LYS B 1 93  ? -0.953  -15.460 -33.437 1.00 10.95 ? 95   LYS B CE  1 
ATOM   2420 N NZ  . LYS B 1 93  ? -2.037  -14.575 -32.867 1.00 9.69  ? 95   LYS B NZ  1 
ATOM   2421 N N   . ASP B 1 94  ? 2.174   -16.552 -39.509 1.00 10.16 ? 96   ASP B N   1 
ATOM   2422 C CA  . ASP B 1 94  ? 2.352   -16.379 -40.990 1.00 11.82 ? 96   ASP B CA  1 
ATOM   2423 C C   . ASP B 1 94  ? 1.709   -15.093 -41.460 1.00 14.20 ? 96   ASP B C   1 
ATOM   2424 O O   . ASP B 1 94  ? 0.597   -14.786 -41.045 1.00 14.75 ? 96   ASP B O   1 
ATOM   2425 C CB  . ASP B 1 94  ? 1.767   -17.535 -41.765 1.00 13.73 ? 96   ASP B CB  1 
ATOM   2426 C CG  . ASP B 1 94  ? 2.320   -17.541 -43.223 1.00 19.89 ? 96   ASP B CG  1 
ATOM   2427 O OD1 . ASP B 1 94  ? 3.488   -17.183 -43.419 1.00 22.75 ? 96   ASP B OD1 1 
ATOM   2428 O OD2 . ASP B 1 94  ? 1.599   -17.886 -44.104 1.00 24.61 ? 96   ASP B OD2 1 
ATOM   2429 N N   . GLY B 1 95  ? 2.438   -14.326 -42.272 1.00 14.87 ? 97   GLY B N   1 
ATOM   2430 C CA  . GLY B 1 95  ? 1.976   -13.032 -42.732 1.00 15.45 ? 97   GLY B CA  1 
ATOM   2431 C C   . GLY B 1 95  ? 2.396   -11.848 -41.911 1.00 16.74 ? 97   GLY B C   1 
ATOM   2432 O O   . GLY B 1 95  ? 2.133   -10.717 -42.315 1.00 19.26 ? 97   GLY B O   1 
ATOM   2433 N N   . ILE B 1 96  ? 3.031   -12.068 -40.743 1.00 14.80 ? 98   ILE B N   1 
ATOM   2434 C CA  . ILE B 1 96  ? 3.588   -10.985 -39.969 1.00 13.54 ? 98   ILE B CA  1 
ATOM   2435 C C   . ILE B 1 96  ? 5.059   -11.061 -40.078 1.00 15.96 ? 98   ILE B C   1 
ATOM   2436 O O   . ILE B 1 96  ? 5.654   -12.054 -39.655 1.00 15.38 ? 98   ILE B O   1 
ATOM   2437 C CB  . ILE B 1 96  ? 3.161   -11.043 -38.470 1.00 11.48 ? 98   ILE B CB  1 
ATOM   2438 C CG1 . ILE B 1 96  ? 1.656   -11.177 -38.267 1.00 14.34 ? 98   ILE B CG1 1 
ATOM   2439 C CG2 . ILE B 1 96  ? 3.735   -9.763  -37.762 1.00 10.51 ? 98   ILE B CG2 1 
ATOM   2440 C CD1 . ILE B 1 96  ? 1.206   -11.226 -36.841 1.00 14.85 ? 98   ILE B CD1 1 
ATOM   2441 N N   . GLU B 1 97  ? 5.675   -10.048 -40.685 1.00 17.72 ? 99   GLU B N   1 
ATOM   2442 C CA  . GLU B 1 97  ? 7.094   -10.011 -40.756 1.00 19.44 ? 99   GLU B CA  1 
ATOM   2443 C C   . GLU B 1 97  ? 7.651   -9.660  -39.396 1.00 18.55 ? 99   GLU B C   1 
ATOM   2444 O O   . GLU B 1 97  ? 7.038   -8.917  -38.619 1.00 18.43 ? 99   GLU B O   1 
ATOM   2445 C CB  . GLU B 1 97  ? 7.586   -9.041  -41.824 1.00 21.78 ? 99   GLU B CB  1 
ATOM   2446 C CG  . GLU B 1 97  ? 7.065   -9.365  -43.205 1.00 28.75 ? 99   GLU B CG  1 
ATOM   2447 C CD  . GLU B 1 97  ? 7.795   -8.540  -44.243 1.00 38.52 ? 99   GLU B CD  1 
ATOM   2448 O OE1 . GLU B 1 97  ? 7.145   -7.679  -44.875 1.00 42.28 ? 99   GLU B OE1 1 
ATOM   2449 O OE2 . GLU B 1 97  ? 9.020   -8.747  -44.404 1.00 43.18 ? 99   GLU B OE2 1 
ATOM   2450 N N   . PRO B 1 98  ? 8.825   -10.189 -39.076 1.00 18.05 ? 100  PRO B N   1 
ATOM   2451 C CA  . PRO B 1 98  ? 9.402   -9.970  -37.777 1.00 17.82 ? 100  PRO B CA  1 
ATOM   2452 C C   . PRO B 1 98  ? 10.103  -8.636  -37.576 1.00 18.50 ? 100  PRO B C   1 
ATOM   2453 O O   . PRO B 1 98  ? 11.249  -8.554  -37.153 1.00 19.48 ? 100  PRO B O   1 
ATOM   2454 C CB  . PRO B 1 98  ? 10.353  -11.161 -37.688 1.00 20.16 ? 100  PRO B CB  1 
ATOM   2455 C CG  . PRO B 1 98  ? 10.846  -11.291 -39.001 1.00 20.86 ? 100  PRO B CG  1 
ATOM   2456 C CD  . PRO B 1 98  ? 9.704   -11.087 -39.886 1.00 19.21 ? 100  PRO B CD  1 
ATOM   2457 N N   . MET B 1 99  ? 9.364   -7.554  -37.847 1.00 16.88 ? 101  MET B N   1 
ATOM   2458 C CA  . MET B 1 99  ? 9.917   -6.223  -37.828 1.00 15.27 ? 101  MET B CA  1 
ATOM   2459 C C   . MET B 1 99  ? 8.831   -5.241  -37.364 1.00 14.71 ? 101  MET B C   1 
ATOM   2460 O O   . MET B 1 99  ? 7.635   -5.426  -37.629 1.00 15.00 ? 101  MET B O   1 
ATOM   2461 C CB  . MET B 1 99  ? 10.469  -5.873  -39.211 1.00 17.24 ? 101  MET B CB  1 
ATOM   2462 C CG  . MET B 1 99  ? 9.496   -6.030  -40.318 1.00 21.39 ? 101  MET B CG  1 
ATOM   2463 S SD  . MET B 1 99  ? 10.397  -5.814  -41.891 1.00 37.94 ? 101  MET B SD  1 
ATOM   2464 C CE  . MET B 1 99  ? 11.175  -7.503  -42.021 1.00 38.29 ? 101  MET B CE  1 
ATOM   2465 N N   . TRP B 1 100 ? 9.244   -4.228  -36.710 1.00 16.08 ? 102  TRP B N   1 
ATOM   2466 C CA  . TRP B 1 100 ? 8.355   -3.153  -36.188 1.00 18.66 ? 102  TRP B CA  1 
ATOM   2467 C C   . TRP B 1 100 ? 7.447   -2.577  -37.248 1.00 20.86 ? 102  TRP B C   1 
ATOM   2468 O O   . TRP B 1 100 ? 6.271   -2.292  -36.983 1.00 20.58 ? 102  TRP B O   1 
ATOM   2469 C CB  . TRP B 1 100 ? 9.189   -2.077  -35.507 1.00 20.09 ? 102  TRP B CB  1 
ATOM   2470 C CG  . TRP B 1 100 ? 8.415   -0.958  -34.853 1.00 23.73 ? 102  TRP B CG  1 
ATOM   2471 C CD1 . TRP B 1 100 ? 7.126   -1.001  -34.413 1.00 26.40 ? 102  TRP B CD1 1 
ATOM   2472 C CD2 . TRP B 1 100 ? 8.911   0.351   -34.498 1.00 24.98 ? 102  TRP B CD2 1 
ATOM   2473 N NE1 . TRP B 1 100 ? 6.763   0.222   -33.885 1.00 26.87 ? 102  TRP B NE1 1 
ATOM   2474 C CE2 . TRP B 1 100 ? 7.841   1.063   -33.919 1.00 26.22 ? 102  TRP B CE2 1 
ATOM   2475 C CE3 . TRP B 1 100 ? 10.126  1.022   -34.692 1.00 26.65 ? 102  TRP B CE3 1 
ATOM   2476 C CZ2 . TRP B 1 100 ? 7.972   2.386   -33.478 1.00 26.43 ? 102  TRP B CZ2 1 
ATOM   2477 C CZ3 . TRP B 1 100 ? 10.252  2.327   -34.236 1.00 26.94 ? 102  TRP B CZ3 1 
ATOM   2478 C CH2 . TRP B 1 100 ? 9.184   2.991   -33.644 1.00 26.90 ? 102  TRP B CH2 1 
ATOM   2479 N N   . GLU B 1 101 ? 7.962   -2.416  -38.472 1.00 21.43 ? 103  GLU B N   1 
ATOM   2480 C CA  . GLU B 1 101 ? 7.189   -1.774  -39.544 1.00 20.21 ? 103  GLU B CA  1 
ATOM   2481 C C   . GLU B 1 101 ? 6.062   -2.551  -40.052 1.00 20.09 ? 103  GLU B C   1 
ATOM   2482 O O   . GLU B 1 101 ? 5.179   -1.984  -40.716 1.00 19.36 ? 103  GLU B O   1 
ATOM   2483 C CB  . GLU B 1 101 ? 8.082   -1.493  -40.759 1.00 23.88 ? 103  GLU B CB  1 
ATOM   2484 C CG  . GLU B 1 101 ? 9.203   -0.537  -40.538 1.00 33.28 ? 103  GLU B CG  1 
ATOM   2485 C CD  . GLU B 1 101 ? 10.233  -0.656  -41.645 1.00 40.77 ? 103  GLU B CD  1 
ATOM   2486 O OE1 . GLU B 1 101 ? 9.846   -0.962  -42.805 1.00 41.18 ? 103  GLU B OE1 1 
ATOM   2487 O OE2 . GLU B 1 101 ? 11.432  -0.475  -41.322 1.00 41.33 ? 103  GLU B OE2 1 
ATOM   2488 N N   . ASP B 1 102 ? 5.980   -3.900  -39.771 1.00 18.68 ? 104  ASP B N   1 
ATOM   2489 C CA  . ASP B 1 102 ? 4.781   -4.655  -40.168 1.00 18.01 ? 104  ASP B CA  1 
ATOM   2490 C C   . ASP B 1 102 ? 3.545   -4.001  -39.570 1.00 16.14 ? 104  ASP B C   1 
ATOM   2491 O O   . ASP B 1 102 ? 3.603   -3.552  -38.411 1.00 14.77 ? 104  ASP B O   1 
ATOM   2492 C CB  . ASP B 1 102 ? 4.866   -6.095  -39.646 1.00 16.43 ? 104  ASP B CB  1 
ATOM   2493 C CG  . ASP B 1 102 ? 3.841   -7.011  -40.245 1.00 18.96 ? 104  ASP B CG  1 
ATOM   2494 O OD1 . ASP B 1 102 ? 2.656   -6.986  -39.790 1.00 16.12 ? 104  ASP B OD1 1 
ATOM   2495 O OD2 . ASP B 1 102 ? 4.192   -7.753  -41.161 1.00 20.19 ? 104  ASP B OD2 1 
ATOM   2496 N N   . GLU B 1 103 ? 2.458   -3.949  -40.328 1.00 17.34 ? 105  GLU B N   1 
ATOM   2497 C CA  . GLU B 1 103 ? 1.198   -3.356  -39.849 1.00 19.31 ? 105  GLU B CA  1 
ATOM   2498 C C   . GLU B 1 103 ? 0.768   -3.938  -38.494 1.00 18.72 ? 105  GLU B C   1 
ATOM   2499 O O   . GLU B 1 103 ? 0.224   -3.213  -37.674 1.00 17.89 ? 105  GLU B O   1 
ATOM   2500 C CB  . GLU B 1 103 ? 0.094   -3.628  -40.868 1.00 23.87 ? 105  GLU B CB  1 
ATOM   2501 C CG  . GLU B 1 103 ? -1.127  -2.756  -40.661 1.00 39.31 ? 105  GLU B CG  1 
ATOM   2502 C CD  . GLU B 1 103 ? -0.982  -1.335  -41.177 1.00 47.52 ? 105  GLU B CD  1 
ATOM   2503 O OE1 . GLU B 1 103 ? -2.015  -0.631  -41.208 1.00 53.47 ? 105  GLU B OE1 1 
ATOM   2504 O OE2 . GLU B 1 103 ? 0.145   -0.920  -41.542 1.00 47.98 ? 105  GLU B OE2 1 
ATOM   2505 N N   . LYS B 1 104 ? 1.001   -5.266  -38.281 1.00 17.00 ? 106  LYS B N   1 
ATOM   2506 C CA  . LYS B 1 104 ? 0.624   -5.896  -37.023 1.00 15.03 ? 106  LYS B CA  1 
ATOM   2507 C C   . LYS B 1 104 ? 1.558   -5.635  -35.861 1.00 14.95 ? 106  LYS B C   1 
ATOM   2508 O O   . LYS B 1 104 ? 1.175   -5.954  -34.727 1.00 14.53 ? 106  LYS B O   1 
ATOM   2509 C CB  . LYS B 1 104 ? 0.446   -7.417  -37.220 1.00 15.52 ? 106  LYS B CB  1 
ATOM   2510 C CG  . LYS B 1 104 ? -0.677  -7.785  -38.204 1.00 22.36 ? 106  LYS B CG  1 
ATOM   2511 C CD  . LYS B 1 104 ? -2.034  -7.390  -37.669 1.00 32.63 ? 106  LYS B CD  1 
ATOM   2512 C CE  . LYS B 1 104 ? -3.196  -7.965  -38.434 1.00 40.55 ? 106  LYS B CE  1 
ATOM   2513 N NZ  . LYS B 1 104 ? -4.391  -7.098  -38.220 1.00 46.59 ? 106  LYS B NZ  1 
ATOM   2514 N N   . ASN B 1 105 ? 2.767   -5.081  -36.102 1.00 13.19 ? 107  ASN B N   1 
ATOM   2515 C CA  . ASN B 1 105 ? 3.701   -4.701  -35.041 1.00 13.00 ? 107  ASN B CA  1 
ATOM   2516 C C   . ASN B 1 105 ? 3.850   -3.204  -34.773 1.00 14.66 ? 107  ASN B C   1 
ATOM   2517 O O   . ASN B 1 105 ? 4.351   -2.834  -33.702 1.00 14.55 ? 107  ASN B O   1 
ATOM   2518 C CB  . ASN B 1 105 ? 5.060   -5.231  -35.334 1.00 11.98 ? 107  ASN B CB  1 
ATOM   2519 C CG  . ASN B 1 105 ? 5.100   -6.712  -35.422 1.00 10.91 ? 107  ASN B CG  1 
ATOM   2520 O OD1 . ASN B 1 105 ? 4.477   -7.415  -34.618 1.00 10.96 ? 107  ASN B OD1 1 
ATOM   2521 N ND2 . ASN B 1 105 ? 5.869   -7.266  -36.368 1.00 12.53 ? 107  ASN B ND2 1 
ATOM   2522 N N   . LYS B 1 106 ? 3.425   -2.352  -35.694 1.00 16.04 ? 108  LYS B N   1 
ATOM   2523 C CA  . LYS B 1 106 ? 3.729   -0.912  -35.556 1.00 16.59 ? 108  LYS B CA  1 
ATOM   2524 C C   . LYS B 1 106 ? 3.216   -0.290  -34.258 1.00 15.92 ? 108  LYS B C   1 
ATOM   2525 O O   . LYS B 1 106 ? 3.926   0.554   -33.684 1.00 16.25 ? 108  LYS B O   1 
ATOM   2526 C CB  . LYS B 1 106 ? 3.271   -0.095  -36.779 1.00 18.63 ? 108  LYS B CB  1 
ATOM   2527 C CG  . LYS B 1 106 ? 1.857   -0.248  -37.233 1.00 27.41 ? 108  LYS B CG  1 
ATOM   2528 C CD  . LYS B 1 106 ? 1.724   0.530   -38.583 1.00 37.45 ? 108  LYS B CD  1 
ATOM   2529 C CE  . LYS B 1 106 ? 0.294   0.871   -38.914 1.00 43.95 ? 108  LYS B CE  1 
ATOM   2530 N NZ  . LYS B 1 106 ? 0.155   1.610   -40.197 1.00 47.39 ? 108  LYS B NZ  1 
ATOM   2531 N N   . ARG B 1 107 ? 2.007   -0.683  -33.792 1.00 14.32 ? 109  ARG B N   1 
ATOM   2532 C CA  . ARG B 1 107 ? 1.432   -0.143  -32.570 1.00 13.39 ? 109  ARG B CA  1 
ATOM   2533 C C   . ARG B 1 107 ? 1.770   -1.053  -31.331 1.00 13.96 ? 109  ARG B C   1 
ATOM   2534 O O   . ARG B 1 107 ? 1.243   -0.856  -30.221 1.00 16.07 ? 109  ARG B O   1 
ATOM   2535 C CB  . ARG B 1 107 ? -0.090  0.035   -32.747 1.00 14.36 ? 109  ARG B CB  1 
ATOM   2536 C CG  . ARG B 1 107 ? -0.521  1.181   -33.680 1.00 20.60 ? 109  ARG B CG  1 
ATOM   2537 C CD  . ARG B 1 107 ? -2.018  1.559   -33.516 1.00 20.99 ? 109  ARG B CD  1 
ATOM   2538 N NE  . ARG B 1 107 ? -2.337  1.714   -32.101 1.00 24.40 ? 109  ARG B NE  1 
ATOM   2539 C CZ  . ARG B 1 107 ? -2.194  2.812   -31.381 1.00 27.11 ? 109  ARG B CZ  1 
ATOM   2540 N NH1 . ARG B 1 107 ? -1.750  3.924   -31.938 1.00 29.20 ? 109  ARG B NH1 1 
ATOM   2541 N NH2 . ARG B 1 107 ? -2.487  2.804   -30.083 1.00 29.74 ? 109  ARG B NH2 1 
ATOM   2542 N N   . GLY B 1 108 ? 2.648   -2.028  -31.509 1.00 13.58 ? 110  GLY B N   1 
ATOM   2543 C CA  . GLY B 1 108 ? 2.842   -3.055  -30.514 1.00 12.83 ? 110  GLY B CA  1 
ATOM   2544 C C   . GLY B 1 108 ? 3.958   -2.823  -29.533 1.00 11.09 ? 110  GLY B C   1 
ATOM   2545 O O   . GLY B 1 108 ? 4.483   -1.730  -29.343 1.00 12.30 ? 110  GLY B O   1 
ATOM   2546 N N   . GLY B 1 109 ? 4.330   -3.909  -28.941 1.00 10.49 ? 111  GLY B N   1 
ATOM   2547 C CA  . GLY B 1 109 ? 5.323   -3.926  -27.878 1.00 9.89  ? 111  GLY B CA  1 
ATOM   2548 C C   . GLY B 1 109 ? 5.724   -5.331  -27.520 1.00 10.59 ? 111  GLY B C   1 
ATOM   2549 O O   . GLY B 1 109 ? 5.255   -6.292  -28.157 1.00 9.59  ? 111  GLY B O   1 
ATOM   2550 N N   . ARG B 1 110 ? 6.580   -5.490  -26.495 1.00 11.41 ? 112  ARG B N   1 
ATOM   2551 C CA  . ARG B 1 110 ? 7.063   -6.814  -26.169 1.00 11.10 ? 112  ARG B CA  1 
ATOM   2552 C C   . ARG B 1 110 ? 7.174   -6.993  -24.646 1.00 11.95 ? 112  ARG B C   1 
ATOM   2553 O O   . ARG B 1 110 ? 7.473   -6.024  -23.919 1.00 13.28 ? 112  ARG B O   1 
ATOM   2554 C CB  . ARG B 1 110 ? 8.379   -7.092  -26.888 1.00 12.40 ? 112  ARG B CB  1 
ATOM   2555 C CG  . ARG B 1 110 ? 9.559   -6.353  -26.261 1.00 15.83 ? 112  ARG B CG  1 
ATOM   2556 C CD  . ARG B 1 110 ? 10.822  -6.442  -27.087 1.00 23.74 ? 112  ARG B CD  1 
ATOM   2557 N NE  . ARG B 1 110 ? 11.827  -5.560  -26.473 1.00 24.91 ? 112  ARG B NE  1 
ATOM   2558 C CZ  . ARG B 1 110 ? 13.104  -5.490  -26.847 1.00 26.30 ? 112  ARG B CZ  1 
ATOM   2559 N NH1 . ARG B 1 110 ? 13.936  -4.653  -26.237 1.00 25.47 ? 112  ARG B NH1 1 
ATOM   2560 N NH2 . ARG B 1 110 ? 13.551  -6.239  -27.838 1.00 23.03 ? 112  ARG B NH2 1 
ATOM   2561 N N   . TRP B 1 111 ? 6.927   -8.222  -24.187 1.00 10.37 ? 113  TRP B N   1 
ATOM   2562 C CA  . TRP B 1 111 ? 7.306   -8.697  -22.847 1.00 10.90 ? 113  TRP B CA  1 
ATOM   2563 C C   . TRP B 1 111 ? 8.705   -9.220  -22.973 1.00 11.99 ? 113  TRP B C   1 
ATOM   2564 O O   . TRP B 1 111 ? 8.927   -10.137 -23.766 1.00 11.83 ? 113  TRP B O   1 
ATOM   2565 C CB  . TRP B 1 111 ? 6.413   -9.839  -22.366 1.00 10.67 ? 113  TRP B CB  1 
ATOM   2566 C CG  . TRP B 1 111 ? 5.093   -9.341  -21.897 1.00 9.35  ? 113  TRP B CG  1 
ATOM   2567 C CD1 . TRP B 1 111 ? 3.890   -9.429  -22.539 1.00 10.88 ? 113  TRP B CD1 1 
ATOM   2568 C CD2 . TRP B 1 111 ? 4.850   -8.630  -20.668 1.00 9.73  ? 113  TRP B CD2 1 
ATOM   2569 N NE1 . TRP B 1 111 ? 2.914   -8.831  -21.795 1.00 11.40 ? 113  TRP B NE1 1 
ATOM   2570 C CE2 . TRP B 1 111 ? 3.483   -8.317  -20.637 1.00 11.28 ? 113  TRP B CE2 1 
ATOM   2571 C CE3 . TRP B 1 111 ? 5.652   -8.283  -19.571 1.00 10.13 ? 113  TRP B CE3 1 
ATOM   2572 C CZ2 . TRP B 1 111 ? 2.898   -7.667  -19.556 1.00 11.76 ? 113  TRP B CZ2 1 
ATOM   2573 C CZ3 . TRP B 1 111 ? 5.067   -7.608  -18.516 1.00 10.70 ? 113  TRP B CZ3 1 
ATOM   2574 C CH2 . TRP B 1 111 ? 3.705   -7.361  -18.498 1.00 10.26 ? 113  TRP B CH2 1 
ATOM   2575 N N   . LEU B 1 112 ? 9.629   -8.676  -22.180 1.00 12.09 ? 114  LEU B N   1 
ATOM   2576 C CA  . LEU B 1 112 ? 11.044  -9.009  -22.337 1.00 13.32 ? 114  LEU B CA  1 
ATOM   2577 C C   . LEU B 1 112 ? 11.588  -9.748  -21.133 1.00 14.79 ? 114  LEU B C   1 
ATOM   2578 O O   . LEU B 1 112 ? 11.352  -9.342  -19.970 1.00 14.92 ? 114  LEU B O   1 
ATOM   2579 C CB  . LEU B 1 112 ? 11.826  -7.693  -22.488 1.00 15.77 ? 114  LEU B CB  1 
ATOM   2580 C CG  . LEU B 1 112 ? 13.346  -7.837  -22.620 1.00 17.05 ? 114  LEU B CG  1 
ATOM   2581 C CD1 . LEU B 1 112 ? 13.687  -8.419  -23.921 1.00 18.66 ? 114  LEU B CD1 1 
ATOM   2582 C CD2 . LEU B 1 112 ? 14.002  -6.481  -22.466 1.00 18.56 ? 114  LEU B CD2 1 
ATOM   2583 N N   . ILE B 1 113 ? 12.397  -10.813 -21.424 1.00 15.57 ? 115  ILE B N   1 
ATOM   2584 C CA  . ILE B 1 113 ? 13.133  -11.599 -20.456 1.00 18.14 ? 115  ILE B CA  1 
ATOM   2585 C C   . ILE B 1 113 ? 14.623  -11.313 -20.797 1.00 18.96 ? 115  ILE B C   1 
ATOM   2586 O O   . ILE B 1 113 ? 15.035  -11.538 -21.940 1.00 16.11 ? 115  ILE B O   1 
ATOM   2587 C CB  . ILE B 1 113 ? 12.829  -13.122 -20.654 1.00 20.83 ? 115  ILE B CB  1 
ATOM   2588 C CG1 . ILE B 1 113 ? 11.357  -13.443 -20.746 1.00 23.94 ? 115  ILE B CG1 1 
ATOM   2589 C CG2 . ILE B 1 113 ? 13.485  -13.933 -19.597 1.00 22.92 ? 115  ILE B CG2 1 
ATOM   2590 C CD1 . ILE B 1 113 ? 10.519  -12.894 -19.662 1.00 23.88 ? 115  ILE B CD1 1 
ATOM   2591 N N   . THR B 1 114 ? 15.416  -10.803 -19.831 1.00 20.59 ? 116  THR B N   1 
ATOM   2592 C CA  . THR B 1 114 ? 16.840  -10.624 -20.062 1.00 22.99 ? 116  THR B CA  1 
ATOM   2593 C C   . THR B 1 114 ? 17.623  -11.574 -19.222 1.00 25.35 ? 116  THR B C   1 
ATOM   2594 O O   . THR B 1 114 ? 17.443  -11.576 -17.985 1.00 28.20 ? 116  THR B O   1 
ATOM   2595 C CB  . THR B 1 114 ? 17.255  -9.198  -19.750 1.00 26.69 ? 116  THR B CB  1 
ATOM   2596 O OG1 . THR B 1 114 ? 16.966  -8.977  -18.357 1.00 32.41 ? 116  THR B OG1 1 
ATOM   2597 C CG2 . THR B 1 114 ? 16.521  -8.205  -20.562 1.00 24.84 ? 116  THR B CG2 1 
ATOM   2598 N N   . LEU B 1 115 ? 18.523  -12.334 -19.842 1.00 23.90 ? 117  LEU B N   1 
ATOM   2599 C CA  . LEU B 1 115 ? 19.285  -13.343 -19.157 1.00 27.61 ? 117  LEU B CA  1 
ATOM   2600 C C   . LEU B 1 115 ? 20.676  -12.733 -18.862 1.00 31.01 ? 117  LEU B C   1 
ATOM   2601 O O   . LEU B 1 115 ? 21.148  -11.826 -19.570 1.00 31.21 ? 117  LEU B O   1 
ATOM   2602 C CB  . LEU B 1 115 ? 19.391  -14.637 -20.020 1.00 27.17 ? 117  LEU B CB  1 
ATOM   2603 C CG  . LEU B 1 115 ? 18.104  -15.469 -20.161 1.00 29.89 ? 117  LEU B CG  1 
ATOM   2604 C CD1 . LEU B 1 115 ? 17.073  -14.796 -21.064 1.00 31.19 ? 117  LEU B CD1 1 
ATOM   2605 C CD2 . LEU B 1 115 ? 18.407  -16.833 -20.752 1.00 31.92 ? 117  LEU B CD2 1 
ATOM   2606 N N   . ASN B 1 116 ? 21.318  -13.208 -17.807 1.00 34.02 ? 118  ASN B N   1 
ATOM   2607 C CA  . ASN B 1 116 ? 22.764  -12.993 -17.679 1.00 37.83 ? 118  ASN B CA  1 
ATOM   2608 C C   . ASN B 1 116 ? 23.472  -14.203 -18.349 1.00 40.79 ? 118  ASN B C   1 
ATOM   2609 O O   . ASN B 1 116 ? 22.820  -15.151 -18.795 1.00 41.41 ? 118  ASN B O   1 
ATOM   2610 C CB  . ASN B 1 116 ? 23.168  -12.739 -16.212 1.00 40.05 ? 118  ASN B CB  1 
ATOM   2611 C CG  . ASN B 1 116 ? 22.624  -13.717 -15.218 1.00 44.61 ? 118  ASN B CG  1 
ATOM   2612 O OD1 . ASN B 1 116 ? 22.787  -14.932 -15.363 1.00 46.93 ? 118  ASN B OD1 1 
ATOM   2613 N ND2 . ASN B 1 116 ? 21.965  -13.219 -14.183 1.00 45.52 ? 118  ASN B ND2 1 
ATOM   2614 N N   . LYS B 1 117 ? 24.788  -14.175 -18.422 1.00 42.76 ? 119  LYS B N   1 
ATOM   2615 C CA  . LYS B 1 117 ? 25.571  -15.210 -19.115 1.00 43.93 ? 119  LYS B CA  1 
ATOM   2616 C C   . LYS B 1 117 ? 25.454  -16.569 -18.409 1.00 43.26 ? 119  LYS B C   1 
ATOM   2617 O O   . LYS B 1 117 ? 25.357  -17.585 -19.084 1.00 43.30 ? 119  LYS B O   1 
ATOM   2618 C CB  . LYS B 1 117 ? 27.046  -14.797 -19.252 1.00 47.94 ? 119  LYS B CB  1 
ATOM   2619 C CG  . LYS B 1 117 ? 27.243  -13.388 -19.776 1.00 54.85 ? 119  LYS B CG  1 
ATOM   2620 C CD  . LYS B 1 117 ? 27.809  -12.466 -18.693 1.00 61.52 ? 119  LYS B CD  1 
ATOM   2621 C CE  . LYS B 1 117 ? 27.745  -11.009 -19.058 1.00 66.45 ? 119  LYS B CE  1 
ATOM   2622 N NZ  . LYS B 1 117 ? 28.493  -10.180 -18.073 1.00 70.81 ? 119  LYS B NZ  1 
ATOM   2623 N N   . GLN B 1 118 ? 25.433  -16.611 -17.063 1.00 43.28 ? 120  GLN B N   1 
ATOM   2624 C CA  . GLN B 1 118 ? 25.224  -17.882 -16.334 1.00 44.52 ? 120  GLN B CA  1 
ATOM   2625 C C   . GLN B 1 118 ? 23.940  -18.605 -16.778 1.00 44.22 ? 120  GLN B C   1 
ATOM   2626 O O   . GLN B 1 118 ? 23.859  -19.829 -16.687 1.00 44.57 ? 120  GLN B O   1 
ATOM   2627 C CB  . GLN B 1 118 ? 25.156  -17.640 -14.814 1.00 47.81 ? 120  GLN B CB  1 
ATOM   2628 C CG  . GLN B 1 118 ? 25.252  -18.917 -13.959 1.00 54.40 ? 120  GLN B CG  1 
ATOM   2629 C CD  . GLN B 1 118 ? 26.584  -19.611 -14.073 1.00 60.47 ? 120  GLN B CD  1 
ATOM   2630 O OE1 . GLN B 1 118 ? 27.488  -19.418 -13.247 1.00 60.72 ? 120  GLN B OE1 1 
ATOM   2631 N NE2 . GLN B 1 118 ? 26.732  -20.433 -15.109 1.00 62.28 ? 120  GLN B NE2 1 
ATOM   2632 N N   . GLN B 1 119 ? 22.944  -17.840 -17.261 1.00 42.82 ? 121  GLN B N   1 
ATOM   2633 C CA  . GLN B 1 119 ? 21.706  -18.395 -17.750 1.00 42.19 ? 121  GLN B CA  1 
ATOM   2634 C C   . GLN B 1 119 ? 21.777  -18.904 -19.216 1.00 43.80 ? 121  GLN B C   1 
ATOM   2635 O O   . GLN B 1 119 ? 20.866  -19.601 -19.635 1.00 45.01 ? 121  GLN B O   1 
ATOM   2636 C CB  . GLN B 1 119 ? 20.598  -17.349 -17.543 1.00 40.62 ? 121  GLN B CB  1 
ATOM   2637 C CG  . GLN B 1 119 ? 20.132  -17.208 -16.117 1.00 38.34 ? 121  GLN B CG  1 
ATOM   2638 C CD  . GLN B 1 119 ? 19.073  -16.148 -16.004 1.00 40.60 ? 121  GLN B CD  1 
ATOM   2639 O OE1 . GLN B 1 119 ? 19.336  -14.941 -16.210 1.00 41.96 ? 121  GLN B OE1 1 
ATOM   2640 N NE2 . GLN B 1 119 ? 17.834  -16.567 -15.676 1.00 37.47 ? 121  GLN B NE2 1 
ATOM   2641 N N   . ARG B 1 120 ? 22.826  -18.591 -19.987 1.00 43.52 ? 122  ARG B N   1 
ATOM   2642 C CA  . ARG B 1 120 ? 23.036  -19.165 -21.346 1.00 42.51 ? 122  ARG B CA  1 
ATOM   2643 C C   . ARG B 1 120 ? 23.008  -20.719 -21.289 1.00 42.56 ? 122  ARG B C   1 
ATOM   2644 O O   . ARG B 1 120 ? 22.390  -21.359 -22.150 1.00 43.09 ? 122  ARG B O   1 
ATOM   2645 C CB  . ARG B 1 120 ? 24.360  -18.609 -21.970 1.00 40.73 ? 122  ARG B CB  1 
ATOM   2646 C CG  . ARG B 1 120 ? 24.927  -19.307 -23.235 1.00 39.79 ? 122  ARG B CG  1 
ATOM   2647 C CD  . ARG B 1 120 ? 24.287  -19.008 -24.596 1.00 36.99 ? 122  ARG B CD  1 
ATOM   2648 N NE  . ARG B 1 120 ? 24.402  -17.602 -24.999 1.00 32.73 ? 122  ARG B NE  1 
ATOM   2649 C CZ  . ARG B 1 120 ? 25.487  -17.012 -25.504 1.00 31.93 ? 122  ARG B CZ  1 
ATOM   2650 N NH1 . ARG B 1 120 ? 26.605  -17.700 -25.688 1.00 26.34 ? 122  ARG B NH1 1 
ATOM   2651 N NH2 . ARG B 1 120 ? 25.467  -15.724 -25.807 1.00 31.13 ? 122  ARG B NH2 1 
ATOM   2652 N N   . ARG B 1 121 ? 23.651  -21.316 -20.284 1.00 41.52 ? 123  ARG B N   1 
ATOM   2653 C CA  . ARG B 1 121 ? 23.692  -22.776 -20.155 1.00 41.66 ? 123  ARG B CA  1 
ATOM   2654 C C   . ARG B 1 121 ? 22.540  -23.361 -19.329 1.00 40.02 ? 123  ARG B C   1 
ATOM   2655 O O   . ARG B 1 121 ? 22.096  -24.473 -19.639 1.00 40.58 ? 123  ARG B O   1 
ATOM   2656 C CB  . ARG B 1 121 ? 25.049  -23.239 -19.575 1.00 44.96 ? 123  ARG B CB  1 
ATOM   2657 C CG  . ARG B 1 121 ? 25.365  -24.721 -19.869 1.00 50.50 ? 123  ARG B CG  1 
ATOM   2658 C CD  . ARG B 1 121 ? 26.553  -25.235 -19.082 1.00 57.00 ? 123  ARG B CD  1 
ATOM   2659 N NE  . ARG B 1 121 ? 26.215  -25.437 -17.671 1.00 62.41 ? 123  ARG B NE  1 
ATOM   2660 C CZ  . ARG B 1 121 ? 27.071  -25.834 -16.735 1.00 65.48 ? 123  ARG B CZ  1 
ATOM   2661 N NH1 . ARG B 1 121 ? 26.667  -25.985 -15.480 1.00 64.23 ? 123  ARG B NH1 1 
ATOM   2662 N NH2 . ARG B 1 121 ? 28.341  -26.080 -17.045 1.00 67.35 ? 123  ARG B NH2 1 
ATOM   2663 N N   . SER B 1 122 ? 22.055  -22.631 -18.295 1.00 38.70 ? 124  SER B N   1 
ATOM   2664 C CA  . SER B 1 122 ? 21.063  -23.132 -17.341 1.00 38.87 ? 124  SER B CA  1 
ATOM   2665 C C   . SER B 1 122 ? 19.627  -22.928 -17.812 1.00 37.05 ? 124  SER B C   1 
ATOM   2666 O O   . SER B 1 122 ? 18.761  -23.758 -17.505 1.00 37.81 ? 124  SER B O   1 
ATOM   2667 C CB  . SER B 1 122 ? 21.225  -22.399 -16.015 1.00 42.17 ? 124  SER B CB  1 
ATOM   2668 O OG  . SER B 1 122 ? 20.884  -21.032 -16.207 1.00 45.30 ? 124  SER B OG  1 
ATOM   2669 N N   . ASP B 1 123 ? 19.372  -21.821 -18.553 1.00 33.82 ? 125  ASP B N   1 
ATOM   2670 C CA  . ASP B 1 123 ? 18.014  -21.340 -18.772 1.00 31.04 ? 125  ASP B CA  1 
ATOM   2671 C C   . ASP B 1 123 ? 17.682  -20.986 -20.234 1.00 24.99 ? 125  ASP B C   1 
ATOM   2672 O O   . ASP B 1 123 ? 16.489  -20.959 -20.494 1.00 23.80 ? 125  ASP B O   1 
ATOM   2673 C CB  . ASP B 1 123 ? 17.741  -20.101 -17.920 1.00 34.91 ? 125  ASP B CB  1 
ATOM   2674 C CG  . ASP B 1 123 ? 17.542  -20.331 -16.433 1.00 43.70 ? 125  ASP B CG  1 
ATOM   2675 O OD1 . ASP B 1 123 ? 17.313  -21.491 -16.033 1.00 45.91 ? 125  ASP B OD1 1 
ATOM   2676 O OD2 . ASP B 1 123 ? 17.599  -19.342 -15.672 1.00 47.05 ? 125  ASP B OD2 1 
ATOM   2677 N N   . LEU B 1 124 ? 18.667  -20.715 -21.167 1.00 22.29 ? 126  LEU B N   1 
ATOM   2678 C CA  . LEU B 1 124 ? 18.255  -20.151 -22.460 1.00 20.80 ? 126  LEU B CA  1 
ATOM   2679 C C   . LEU B 1 124 ? 17.371  -21.126 -23.242 1.00 18.40 ? 126  LEU B C   1 
ATOM   2680 O O   . LEU B 1 124 ? 16.306  -20.739 -23.733 1.00 17.57 ? 126  LEU B O   1 
ATOM   2681 C CB  . LEU B 1 124 ? 19.404  -19.668 -23.346 1.00 21.35 ? 126  LEU B CB  1 
ATOM   2682 C CG  . LEU B 1 124 ? 19.021  -19.050 -24.712 1.00 22.40 ? 126  LEU B CG  1 
ATOM   2683 C CD1 . LEU B 1 124 ? 18.342  -17.646 -24.565 1.00 23.25 ? 126  LEU B CD1 1 
ATOM   2684 C CD2 . LEU B 1 124 ? 20.303  -18.874 -25.593 1.00 24.37 ? 126  LEU B CD2 1 
ATOM   2685 N N   . ASP B 1 125 ? 17.802  -22.376 -23.357 1.00 16.94 ? 127  ASP B N   1 
ATOM   2686 C CA  . ASP B 1 125 ? 17.065  -23.352 -24.118 1.00 17.09 ? 127  ASP B CA  1 
ATOM   2687 C C   . ASP B 1 125 ? 15.682  -23.599 -23.470 1.00 16.50 ? 127  ASP B C   1 
ATOM   2688 O O   . ASP B 1 125 ? 14.696  -23.658 -24.198 1.00 16.44 ? 127  ASP B O   1 
ATOM   2689 C CB  . ASP B 1 125 ? 17.845  -24.667 -24.191 1.00 20.28 ? 127  ASP B CB  1 
ATOM   2690 C CG  . ASP B 1 125 ? 19.112  -24.643 -25.011 1.00 27.50 ? 127  ASP B CG  1 
ATOM   2691 O OD1 . ASP B 1 125 ? 19.245  -23.771 -25.908 1.00 26.10 ? 127  ASP B OD1 1 
ATOM   2692 O OD2 . ASP B 1 125 ? 19.948  -25.503 -24.793 1.00 32.09 ? 127  ASP B OD2 1 
ATOM   2693 N N   . ARG B 1 126 ? 15.595  -23.705 -22.118 1.00 15.37 ? 128  ARG B N   1 
ATOM   2694 C CA  . ARG B 1 126 ? 14.332  -24.079 -21.527 1.00 16.60 ? 128  ARG B CA  1 
ATOM   2695 C C   . ARG B 1 126 ? 13.396  -22.879 -21.624 1.00 13.91 ? 128  ARG B C   1 
ATOM   2696 O O   . ARG B 1 126 ? 12.243  -23.067 -21.929 1.00 13.53 ? 128  ARG B O   1 
ATOM   2697 C CB  . ARG B 1 126 ? 14.434  -24.654 -20.096 1.00 22.54 ? 128  ARG B CB  1 
ATOM   2698 C CG  . ARG B 1 126 ? 14.693  -23.691 -19.039 1.00 30.99 ? 128  ARG B CG  1 
ATOM   2699 C CD  . ARG B 1 126 ? 15.064  -24.439 -17.735 1.00 36.37 ? 128  ARG B CD  1 
ATOM   2700 N NE  . ARG B 1 126 ? 15.304  -23.536 -16.611 1.00 38.92 ? 128  ARG B NE  1 
ATOM   2701 C CZ  . ARG B 1 126 ? 14.348  -22.894 -15.939 1.00 43.68 ? 128  ARG B CZ  1 
ATOM   2702 N NH1 . ARG B 1 126 ? 13.070  -23.044 -16.275 1.00 44.96 ? 128  ARG B NH1 1 
ATOM   2703 N NH2 . ARG B 1 126 ? 14.662  -22.093 -14.933 1.00 46.56 ? 128  ARG B NH2 1 
ATOM   2704 N N   . PHE B 1 127 ? 13.884  -21.635 -21.408 1.00 13.42 ? 129  PHE B N   1 
ATOM   2705 C CA  . PHE B 1 127 ? 13.012  -20.467 -21.540 1.00 13.72 ? 129  PHE B CA  1 
ATOM   2706 C C   . PHE B 1 127 ? 12.530  -20.267 -22.985 1.00 10.62 ? 129  PHE B C   1 
ATOM   2707 O O   . PHE B 1 127 ? 11.346  -19.920 -23.197 1.00 10.69 ? 129  PHE B O   1 
ATOM   2708 C CB  . PHE B 1 127 ? 13.706  -19.205 -21.081 1.00 14.84 ? 129  PHE B CB  1 
ATOM   2709 C CG  . PHE B 1 127 ? 13.858  -18.981 -19.589 1.00 19.12 ? 129  PHE B CG  1 
ATOM   2710 C CD1 . PHE B 1 127 ? 13.225  -19.797 -18.672 1.00 21.36 ? 129  PHE B CD1 1 
ATOM   2711 C CD2 . PHE B 1 127 ? 14.628  -17.940 -19.111 1.00 24.53 ? 129  PHE B CD2 1 
ATOM   2712 C CE1 . PHE B 1 127 ? 13.375  -19.574 -17.286 1.00 24.82 ? 129  PHE B CE1 1 
ATOM   2713 C CE2 . PHE B 1 127 ? 14.781  -17.735 -17.728 1.00 26.81 ? 129  PHE B CE2 1 
ATOM   2714 C CZ  . PHE B 1 127 ? 14.140  -18.541 -16.843 1.00 25.18 ? 129  PHE B CZ  1 
ATOM   2715 N N   . TRP B 1 128 ? 13.412  -20.468 -23.951 1.00 9.67  ? 130  TRP B N   1 
ATOM   2716 C CA  . TRP B 1 128 ? 12.987  -20.355 -25.371 1.00 10.03 ? 130  TRP B CA  1 
ATOM   2717 C C   . TRP B 1 128 ? 11.959  -21.401 -25.717 1.00 10.58 ? 130  TRP B C   1 
ATOM   2718 O O   . TRP B 1 128 ? 10.904  -21.093 -26.296 1.00 10.35 ? 130  TRP B O   1 
ATOM   2719 C CB  . TRP B 1 128 ? 14.210  -20.365 -26.284 1.00 10.19 ? 130  TRP B CB  1 
ATOM   2720 C CG  . TRP B 1 128 ? 13.903  -20.204 -27.740 1.00 10.79 ? 130  TRP B CG  1 
ATOM   2721 C CD1 . TRP B 1 128 ? 14.240  -21.068 -28.737 1.00 11.27 ? 130  TRP B CD1 1 
ATOM   2722 C CD2 . TRP B 1 128 ? 13.259  -19.081 -28.377 1.00 10.45 ? 130  TRP B CD2 1 
ATOM   2723 N NE1 . TRP B 1 128 ? 13.858  -20.569 -29.952 1.00 10.95 ? 130  TRP B NE1 1 
ATOM   2724 C CE2 . TRP B 1 128 ? 13.244  -19.347 -29.765 1.00 10.76 ? 130  TRP B CE2 1 
ATOM   2725 C CE3 . TRP B 1 128 ? 12.637  -17.902 -27.899 1.00 10.28 ? 130  TRP B CE3 1 
ATOM   2726 C CZ2 . TRP B 1 128 ? 12.664  -18.472 -30.676 1.00 10.34 ? 130  TRP B CZ2 1 
ATOM   2727 C CZ3 . TRP B 1 128 ? 12.092  -17.022 -28.811 1.00 10.21 ? 130  TRP B CZ3 1 
ATOM   2728 C CH2 . TRP B 1 128 ? 12.088  -17.326 -30.191 1.00 9.64  ? 130  TRP B CH2 1 
ATOM   2729 N N   . LEU B 1 129 ? 12.204  -22.664 -25.323 1.00 11.09 ? 131  LEU B N   1 
ATOM   2730 C CA  . LEU B 1 129 ? 11.204  -23.715 -25.590 1.00 10.96 ? 131  LEU B CA  1 
ATOM   2731 C C   . LEU B 1 129 ? 9.850   -23.374 -24.944 1.00 10.86 ? 131  LEU B C   1 
ATOM   2732 O O   . LEU B 1 129 ? 8.841   -23.445 -25.608 1.00 10.32 ? 131  LEU B O   1 
ATOM   2733 C CB  . LEU B 1 129 ? 11.677  -25.066 -25.138 1.00 11.08 ? 131  LEU B CB  1 
ATOM   2734 C CG  . LEU B 1 129 ? 10.709  -26.217 -25.374 1.00 13.67 ? 131  LEU B CG  1 
ATOM   2735 C CD1 . LEU B 1 129 ? 10.200  -26.300 -26.835 1.00 16.12 ? 131  LEU B CD1 1 
ATOM   2736 C CD2 . LEU B 1 129 ? 11.370  -27.524 -24.877 1.00 16.20 ? 131  LEU B CD2 1 
ATOM   2737 N N   . GLU B 1 130 ? 9.828   -22.954 -23.684 1.00 11.23 ? 132  GLU B N   1 
ATOM   2738 C CA  . GLU B 1 130 ? 8.558   -22.603 -23.016 1.00 11.35 ? 132  GLU B CA  1 
ATOM   2739 C C   . GLU B 1 130 ? 7.831   -21.469 -23.771 1.00 12.36 ? 132  GLU B C   1 
ATOM   2740 O O   . GLU B 1 130 ? 6.582   -21.499 -23.936 1.00 12.77 ? 132  GLU B O   1 
ATOM   2741 C CB  . GLU B 1 130 ? 8.787   -22.198 -21.557 1.00 12.34 ? 132  GLU B CB  1 
ATOM   2742 C CG  . GLU B 1 130 ? 9.460   -23.252 -20.681 1.00 22.40 ? 132  GLU B CG  1 
ATOM   2743 C CD  . GLU B 1 130 ? 8.715   -24.566 -20.572 1.00 24.81 ? 132  GLU B CD  1 
ATOM   2744 O OE1 . GLU B 1 130 ? 7.479   -24.580 -20.740 1.00 17.55 ? 132  GLU B OE1 1 
ATOM   2745 O OE2 . GLU B 1 130 ? 9.390   -25.588 -20.325 1.00 34.06 ? 132  GLU B OE2 1 
ATOM   2746 N N   . THR B 1 131 ? 8.600   -20.461 -24.237 1.00 10.08 ? 133  THR B N   1 
ATOM   2747 C CA  . THR B 1 131 ? 8.057   -19.390 -25.108 1.00 8.12  ? 133  THR B CA  1 
ATOM   2748 C C   . THR B 1 131 ? 7.406   -19.968 -26.344 1.00 7.32  ? 133  THR B C   1 
ATOM   2749 O O   . THR B 1 131 ? 6.261   -19.622 -26.672 1.00 8.42  ? 133  THR B O   1 
ATOM   2750 C CB  . THR B 1 131 ? 9.175   -18.383 -25.463 1.00 10.89 ? 133  THR B CB  1 
ATOM   2751 O OG1 . THR B 1 131 ? 9.790   -17.913 -24.255 1.00 10.29 ? 133  THR B OG1 1 
ATOM   2752 C CG2 . THR B 1 131 ? 8.639   -17.204 -26.211 1.00 11.21 ? 133  THR B CG2 1 
ATOM   2753 N N   . LEU B 1 132 ? 8.115   -20.870 -27.042 1.00 8.16  ? 134  LEU B N   1 
ATOM   2754 C CA  . LEU B 1 132 ? 7.568   -21.458 -28.293 1.00 8.61  ? 134  LEU B CA  1 
ATOM   2755 C C   . LEU B 1 132 ? 6.273   -22.232 -28.003 1.00 9.15  ? 134  LEU B C   1 
ATOM   2756 O O   . LEU B 1 132 ? 5.316   -22.138 -28.773 1.00 8.69  ? 134  LEU B O   1 
ATOM   2757 C CB  . LEU B 1 132 ? 8.587   -22.378 -28.911 1.00 9.40  ? 134  LEU B CB  1 
ATOM   2758 C CG  . LEU B 1 132 ? 9.917   -21.730 -29.374 1.00 10.25 ? 134  LEU B CG  1 
ATOM   2759 C CD1 . LEU B 1 132 ? 10.888  -22.839 -29.819 1.00 11.29 ? 134  LEU B CD1 1 
ATOM   2760 C CD2 . LEU B 1 132 ? 9.673   -20.760 -30.476 1.00 12.29 ? 134  LEU B CD2 1 
ATOM   2761 N N   . LEU B 1 133 ? 6.242   -22.994 -26.893 1.00 9.23  ? 135  LEU B N   1 
ATOM   2762 C CA  . LEU B 1 133 ? 5.043   -23.741 -26.530 1.00 8.86  ? 135  LEU B CA  1 
ATOM   2763 C C   . LEU B 1 133 ? 3.864   -22.854 -26.203 1.00 9.83  ? 135  LEU B C   1 
ATOM   2764 O O   . LEU B 1 133 ? 2.723   -23.184 -26.550 1.00 9.60  ? 135  LEU B O   1 
ATOM   2765 C CB  . LEU B 1 133 ? 5.325   -24.723 -25.416 1.00 8.52  ? 135  LEU B CB  1 
ATOM   2766 C CG  . LEU B 1 133 ? 6.416   -25.773 -25.688 1.00 11.02 ? 135  LEU B CG  1 
ATOM   2767 C CD1 . LEU B 1 133 ? 6.503   -26.666 -24.538 1.00 12.51 ? 135  LEU B CD1 1 
ATOM   2768 C CD2 . LEU B 1 133 ? 6.195   -26.527 -27.000 1.00 11.05 ? 135  LEU B CD2 1 
ATOM   2769 N N   . CYS B 1 134 ? 4.110   -21.681 -25.572 1.00 8.29  ? 136  CYS B N   1 
ATOM   2770 C CA  . CYS B 1 134 ? 3.056   -20.683 -25.311 1.00 7.82  ? 136  CYS B CA  1 
ATOM   2771 C C   . CYS B 1 134 ? 2.432   -20.162 -26.613 1.00 8.06  ? 136  CYS B C   1 
ATOM   2772 O O   . CYS B 1 134 ? 1.226   -19.950 -26.691 1.00 9.24  ? 136  CYS B O   1 
ATOM   2773 C CB  . CYS B 1 134 ? 3.560   -19.534 -24.460 1.00 8.53  ? 136  CYS B CB  1 
ATOM   2774 S SG  . CYS B 1 134 ? 3.804   -19.963 -22.701 1.00 12.22 ? 136  CYS B SG  1 
ATOM   2775 N N   . LEU B 1 135 ? 3.283   -19.901 -27.606 1.00 6.20  ? 137  LEU B N   1 
ATOM   2776 C CA  . LEU B 1 135 ? 2.879   -19.472 -28.898 1.00 8.25  ? 137  LEU B CA  1 
ATOM   2777 C C   . LEU B 1 135 ? 2.066   -20.529 -29.620 1.00 8.08  ? 137  LEU B C   1 
ATOM   2778 O O   . LEU B 1 135 ? 0.853   -20.327 -29.878 1.00 7.26  ? 137  LEU B O   1 
ATOM   2779 C CB  . LEU B 1 135 ? 4.073   -19.041 -29.740 1.00 8.83  ? 137  LEU B CB  1 
ATOM   2780 C CG  . LEU B 1 135 ? 4.443   -17.532 -29.692 1.00 10.05 ? 137  LEU B CG  1 
ATOM   2781 C CD1 . LEU B 1 135 ? 4.666   -17.074 -28.289 1.00 7.69  ? 137  LEU B CD1 1 
ATOM   2782 C CD2 . LEU B 1 135 ? 5.660   -17.253 -30.528 1.00 10.84 ? 137  LEU B CD2 1 
ATOM   2783 N N   . ILE B 1 136 ? 2.697   -21.658 -29.918 1.00 8.37  ? 138  ILE B N   1 
ATOM   2784 C CA  . ILE B 1 136 ? 2.014   -22.660 -30.752 1.00 9.76  ? 138  ILE B CA  1 
ATOM   2785 C C   . ILE B 1 136 ? 0.799   -23.244 -30.069 1.00 9.40  ? 138  ILE B C   1 
ATOM   2786 O O   . ILE B 1 136 ? -0.178  -23.601 -30.752 1.00 8.76  ? 138  ILE B O   1 
ATOM   2787 C CB  . ILE B 1 136 ? 3.005   -23.721 -31.293 1.00 11.40 ? 138  ILE B CB  1 
ATOM   2788 C CG1 . ILE B 1 136 ? 3.496   -24.672 -30.201 1.00 11.66 ? 138  ILE B CG1 1 
ATOM   2789 C CG2 . ILE B 1 136 ? 4.168   -23.000 -32.031 1.00 11.39 ? 138  ILE B CG2 1 
ATOM   2790 C CD1 . ILE B 1 136 ? 4.230   -25.898 -30.735 1.00 11.75 ? 138  ILE B CD1 1 
ATOM   2791 N N   . GLY B 1 137 ? 0.843   -23.350 -28.741 1.00 8.55  ? 139  GLY B N   1 
ATOM   2792 C CA  . GLY B 1 137 ? -0.293  -23.883 -27.988 1.00 7.85  ? 139  GLY B CA  1 
ATOM   2793 C C   . GLY B 1 137 ? -1.422  -22.928 -27.665 1.00 8.63  ? 139  GLY B C   1 
ATOM   2794 O O   . GLY B 1 137 ? -2.405  -23.350 -27.049 1.00 9.63  ? 139  GLY B O   1 
ATOM   2795 N N   . GLU B 1 138 ? -1.285  -21.649 -28.056 1.00 7.28  ? 140  GLU B N   1 
ATOM   2796 C CA  . GLU B 1 138 ? -2.307  -20.625 -27.839 1.00 7.96  ? 140  GLU B CA  1 
ATOM   2797 C C   . GLU B 1 138 ? -2.648  -20.503 -26.340 1.00 9.63  ? 140  GLU B C   1 
ATOM   2798 O O   . GLU B 1 138 ? -3.814  -20.523 -25.878 1.00 9.28  ? 140  GLU B O   1 
ATOM   2799 C CB  . GLU B 1 138 ? -3.588  -20.927 -28.601 1.00 7.18  ? 140  GLU B CB  1 
ATOM   2800 C CG  . GLU B 1 138 ? -3.390  -21.097 -30.089 1.00 8.20  ? 140  GLU B CG  1 
ATOM   2801 C CD  . GLU B 1 138 ? -3.265  -19.789 -30.798 1.00 13.34 ? 140  GLU B CD  1 
ATOM   2802 O OE1 . GLU B 1 138 ? -4.083  -18.871 -30.545 1.00 13.25 ? 140  GLU B OE1 1 
ATOM   2803 O OE2 . GLU B 1 138 ? -2.330  -19.692 -31.616 1.00 13.27 ? 140  GLU B OE2 1 
ATOM   2804 N N   . SER B 1 139 ? -1.583  -20.347 -25.533 1.00 9.40  ? 141  SER B N   1 
ATOM   2805 C CA  . SER B 1 139 ? -1.733  -20.436 -24.068 1.00 9.08  ? 141  SER B CA  1 
ATOM   2806 C C   . SER B 1 139 ? -2.321  -19.237 -23.353 1.00 10.60 ? 141  SER B C   1 
ATOM   2807 O O   . SER B 1 139 ? -2.527  -19.273 -22.099 1.00 12.11 ? 141  SER B O   1 
ATOM   2808 C CB  . SER B 1 139 ? -0.387  -20.731 -23.437 1.00 9.71  ? 141  SER B CB  1 
ATOM   2809 O OG  . SER B 1 139 ? 0.274   -21.821 -24.062 1.00 10.71 ? 141  SER B OG  1 
ATOM   2810 N N   . PHE B 1 140 ? -2.644  -18.212 -24.089 1.00 8.22  ? 142  PHE B N   1 
ATOM   2811 C CA  . PHE B 1 140 ? -3.208  -16.958 -23.523 1.00 9.38  ? 142  PHE B CA  1 
ATOM   2812 C C   . PHE B 1 140 ? -4.695  -16.805 -23.776 1.00 12.99 ? 142  PHE B C   1 
ATOM   2813 O O   . PHE B 1 140 ? -5.218  -15.709 -23.680 1.00 13.25 ? 142  PHE B O   1 
ATOM   2814 C CB  . PHE B 1 140 ? -2.424  -15.771 -24.045 1.00 9.52  ? 142  PHE B CB  1 
ATOM   2815 C CG  . PHE B 1 140 ? -0.916  -15.953 -23.915 1.00 10.17 ? 142  PHE B CG  1 
ATOM   2816 C CD1 . PHE B 1 140 ? -0.326  -16.081 -22.671 1.00 9.97  ? 142  PHE B CD1 1 
ATOM   2817 C CD2 . PHE B 1 140 ? -0.105  -16.053 -25.039 1.00 9.49  ? 142  PHE B CD2 1 
ATOM   2818 C CE1 . PHE B 1 140 ? 1.064   -16.295 -22.554 1.00 10.08 ? 142  PHE B CE1 1 
ATOM   2819 C CE2 . PHE B 1 140 ? 1.284   -16.184 -24.916 1.00 7.92  ? 142  PHE B CE2 1 
ATOM   2820 C CZ  . PHE B 1 140 ? 1.851   -16.317 -23.689 1.00 9.13  ? 142  PHE B CZ  1 
ATOM   2821 N N   . ASP B 1 141 ? -5.347  -17.921 -24.070 1.00 15.25 ? 143  ASP B N   1 
ATOM   2822 C CA  . ASP B 1 141 ? -6.786  -18.019 -24.405 1.00 16.63 ? 143  ASP B CA  1 
ATOM   2823 C C   . ASP B 1 141 ? -7.156  -17.003 -25.466 1.00 14.92 ? 143  ASP B C   1 
ATOM   2824 O O   . ASP B 1 141 ? -6.431  -16.968 -26.471 1.00 14.66 ? 143  ASP B O   1 
ATOM   2825 C CB  . ASP B 1 141 ? -7.572  -17.913 -23.111 1.00 20.29 ? 143  ASP B CB  1 
ATOM   2826 C CG  . ASP B 1 141 ? -7.426  -19.149 -22.268 1.00 29.38 ? 143  ASP B CG  1 
ATOM   2827 O OD1 . ASP B 1 141 ? -7.666  -20.291 -22.810 1.00 35.22 ? 143  ASP B OD1 1 
ATOM   2828 O OD2 . ASP B 1 141 ? -7.082  -19.010 -21.117 1.00 27.83 ? 143  ASP B OD2 1 
ATOM   2829 N N   . ASP B 1 142 ? -8.237  -16.193 -25.306 1.00 15.13 ? 144  ASP B N   1 
ATOM   2830 C CA  . ASP B 1 142 ? -8.611  -15.293 -26.416 1.00 15.79 ? 144  ASP B CA  1 
ATOM   2831 C C   . ASP B 1 142 ? -7.521  -14.266 -26.721 1.00 15.83 ? 144  ASP B C   1 
ATOM   2832 O O   . ASP B 1 142 ? -7.369  -13.812 -27.848 1.00 16.21 ? 144  ASP B O   1 
ATOM   2833 C CB  . ASP B 1 142 ? -9.889  -14.556 -26.079 1.00 18.28 ? 144  ASP B CB  1 
ATOM   2834 C CG  . ASP B 1 142 ? -11.135 -15.412 -26.181 1.00 25.49 ? 144  ASP B CG  1 
ATOM   2835 O OD1 . ASP B 1 142 ? -11.083 -16.455 -26.818 1.00 27.46 ? 144  ASP B OD1 1 
ATOM   2836 O OD2 . ASP B 1 142 ? -12.142 -15.018 -25.645 1.00 27.55 ? 144  ASP B OD2 1 
ATOM   2837 N N   . TYR B 1 143 ? -6.745  -13.902 -25.686 1.00 12.86 ? 145  TYR B N   1 
ATOM   2838 C CA  . TYR B 1 143 ? -5.662  -12.948 -25.863 1.00 11.74 ? 145  TYR B CA  1 
ATOM   2839 C C   . TYR B 1 143 ? -4.485  -13.473 -26.646 1.00 11.71 ? 145  TYR B C   1 
ATOM   2840 O O   . TYR B 1 143 ? -3.646  -12.658 -27.018 1.00 11.72 ? 145  TYR B O   1 
ATOM   2841 C CB  . TYR B 1 143 ? -5.222  -12.426 -24.518 1.00 12.95 ? 145  TYR B CB  1 
ATOM   2842 C CG  . TYR B 1 143 ? -6.370  -11.831 -23.744 1.00 17.24 ? 145  TYR B CG  1 
ATOM   2843 C CD1 . TYR B 1 143 ? -7.183  -10.869 -24.306 1.00 18.61 ? 145  TYR B CD1 1 
ATOM   2844 C CD2 . TYR B 1 143 ? -6.659  -12.262 -22.466 1.00 21.82 ? 145  TYR B CD2 1 
ATOM   2845 C CE1 . TYR B 1 143 ? -8.217  -10.292 -23.585 1.00 21.37 ? 145  TYR B CE1 1 
ATOM   2846 C CE2 . TYR B 1 143 ? -7.704  -11.707 -21.738 1.00 24.28 ? 145  TYR B CE2 1 
ATOM   2847 C CZ  . TYR B 1 143 ? -8.476  -10.722 -22.302 1.00 23.85 ? 145  TYR B CZ  1 
ATOM   2848 O OH  . TYR B 1 143 ? -9.495  -10.190 -21.564 1.00 28.27 ? 145  TYR B OH  1 
ATOM   2849 N N   . SER B 1 144 ? -4.411  -14.758 -26.914 1.00 9.29  ? 146  SER B N   1 
ATOM   2850 C CA  . SER B 1 144 ? -3.428  -15.267 -27.875 1.00 9.98  ? 146  SER B CA  1 
ATOM   2851 C C   . SER B 1 144 ? -3.525  -14.612 -29.251 1.00 11.01 ? 146  SER B C   1 
ATOM   2852 O O   . SER B 1 144 ? -2.546  -14.584 -29.961 1.00 10.07 ? 146  SER B O   1 
ATOM   2853 C CB  . SER B 1 144 ? -3.516  -16.798 -28.004 1.00 11.74 ? 146  SER B CB  1 
ATOM   2854 O OG  . SER B 1 144 ? -2.824  -17.428 -26.932 1.00 13.65 ? 146  SER B OG  1 
ATOM   2855 N N   . ASP B 1 145 ? -4.702  -14.094 -29.609 1.00 11.06 ? 147  ASP B N   1 
ATOM   2856 C CA  . ASP B 1 145 ? -4.860  -13.408 -30.882 1.00 11.83 ? 147  ASP B CA  1 
ATOM   2857 C C   . ASP B 1 145 ? -4.013  -12.117 -30.912 1.00 12.17 ? 147  ASP B C   1 
ATOM   2858 O O   . ASP B 1 145 ? -3.665  -11.646 -32.000 1.00 13.45 ? 147  ASP B O   1 
ATOM   2859 C CB  . ASP B 1 145 ? -6.317  -13.065 -31.132 1.00 10.88 ? 147  ASP B CB  1 
ATOM   2860 C CG  . ASP B 1 145 ? -7.167  -14.305 -31.476 1.00 18.88 ? 147  ASP B CG  1 
ATOM   2861 O OD1 . ASP B 1 145 ? -6.585  -15.335 -31.927 1.00 19.21 ? 147  ASP B OD1 1 
ATOM   2862 O OD2 . ASP B 1 145 ? -8.378  -14.242 -31.297 1.00 19.58 ? 147  ASP B OD2 1 
ATOM   2863 N N   . ASP B 1 146 ? -3.672  -11.536 -29.738 1.00 9.75  ? 148  ASP B N   1 
ATOM   2864 C CA  . ASP B 1 146 ? -2.811  -10.335 -29.748 1.00 9.12  ? 148  ASP B CA  1 
ATOM   2865 C C   . ASP B 1 146 ? -1.314  -10.694 -29.912 1.00 9.43  ? 148  ASP B C   1 
ATOM   2866 O O   . ASP B 1 146 ? -0.506  -9.782  -30.139 1.00 9.55  ? 148  ASP B O   1 
ATOM   2867 C CB  . ASP B 1 146 ? -2.950  -9.538  -28.468 1.00 8.89  ? 148  ASP B CB  1 
ATOM   2868 C CG  . ASP B 1 146 ? -4.061  -8.505  -28.509 1.00 16.88 ? 148  ASP B CG  1 
ATOM   2869 O OD1 . ASP B 1 146 ? -5.174  -8.867  -28.956 1.00 17.40 ? 148  ASP B OD1 1 
ATOM   2870 O OD2 . ASP B 1 146 ? -3.794  -7.332  -28.123 1.00 15.53 ? 148  ASP B OD2 1 
ATOM   2871 N N   . VAL B 1 147 ? -0.954  -11.949 -29.823 1.00 8.54  ? 149  VAL B N   1 
ATOM   2872 C CA  . VAL B 1 147 ? 0.420   -12.361 -29.962 1.00 7.68  ? 149  VAL B CA  1 
ATOM   2873 C C   . VAL B 1 147 ? 0.770   -12.256 -31.431 1.00 8.92  ? 149  VAL B C   1 
ATOM   2874 O O   . VAL B 1 147 ? 0.039   -12.749 -32.292 1.00 10.02 ? 149  VAL B O   1 
ATOM   2875 C CB  . VAL B 1 147 ? 0.652   -13.773 -29.399 1.00 7.97  ? 149  VAL B CB  1 
ATOM   2876 C CG1 . VAL B 1 147 ? 2.070   -14.233 -29.737 1.00 7.12  ? 149  VAL B CG1 1 
ATOM   2877 C CG2 . VAL B 1 147 ? 0.420   -13.830 -27.904 1.00 8.34  ? 149  VAL B CG2 1 
ATOM   2878 N N   . CYS B 1 148 ? 1.912   -11.594 -31.729 1.00 8.61  ? 150  CYS B N   1 
ATOM   2879 C CA  . CYS B 1 148 ? 2.491   -11.581 -33.087 1.00 7.81  ? 150  CYS B CA  1 
ATOM   2880 C C   . CYS B 1 148 ? 3.530   -12.664 -33.262 1.00 7.78  ? 150  CYS B C   1 
ATOM   2881 O O   . CYS B 1 148 ? 3.573   -13.320 -34.289 1.00 9.29  ? 150  CYS B O   1 
ATOM   2882 C CB  . CYS B 1 148 ? 3.069   -10.225 -33.393 1.00 7.59  ? 150  CYS B CB  1 
ATOM   2883 S SG  . CYS B 1 148 ? 1.806   -8.941  -33.329 1.00 11.75 ? 150  CYS B SG  1 
ATOM   2884 N N   . GLY B 1 149 ? 4.379   -12.823 -32.268 1.00 7.15  ? 151  GLY B N   1 
ATOM   2885 C CA  . GLY B 1 149 ? 5.556   -13.700 -32.375 1.00 8.86  ? 151  GLY B CA  1 
ATOM   2886 C C   . GLY B 1 149 ? 6.475   -13.609 -31.195 1.00 7.21  ? 151  GLY B C   1 
ATOM   2887 O O   . GLY B 1 149 ? 6.152   -12.954 -30.217 1.00 7.75  ? 151  GLY B O   1 
ATOM   2888 N N   . ALA B 1 150 ? 7.642   -14.254 -31.291 1.00 8.97  ? 152  ALA B N   1 
ATOM   2889 C CA  . ALA B 1 150 ? 8.622   -14.176 -30.240 1.00 7.79  ? 152  ALA B CA  1 
ATOM   2890 C C   . ALA B 1 150 ? 9.993   -14.103 -30.860 1.00 8.13  ? 152  ALA B C   1 
ATOM   2891 O O   . ALA B 1 150 ? 10.196  -14.572 -32.011 1.00 8.99  ? 152  ALA B O   1 
ATOM   2892 C CB  . ALA B 1 150 ? 8.504   -15.347 -29.283 1.00 8.12  ? 152  ALA B CB  1 
ATOM   2893 N N   . VAL B 1 151 ? 10.932  -13.480 -30.153 1.00 9.50  ? 153  VAL B N   1 
ATOM   2894 C CA  . VAL B 1 151 ? 12.294  -13.235 -30.663 1.00 9.39  ? 153  VAL B CA  1 
ATOM   2895 C C   . VAL B 1 151 ? 13.275  -13.635 -29.636 1.00 10.25 ? 153  VAL B C   1 
ATOM   2896 O O   . VAL B 1 151 ? 13.092  -13.317 -28.460 1.00 10.14 ? 153  VAL B O   1 
ATOM   2897 C CB  . VAL B 1 151 ? 12.511  -11.731 -31.074 1.00 11.60 ? 153  VAL B CB  1 
ATOM   2898 C CG1 . VAL B 1 151 ? 13.940  -11.495 -31.641 1.00 12.08 ? 153  VAL B CG1 1 
ATOM   2899 C CG2 . VAL B 1 151 ? 11.460  -11.263 -32.068 1.00 12.88 ? 153  VAL B CG2 1 
ATOM   2900 N N   . VAL B 1 152 ? 14.355  -14.334 -30.058 1.00 10.94 ? 154  VAL B N   1 
ATOM   2901 C CA  . VAL B 1 152 ? 15.473  -14.584 -29.151 1.00 11.15 ? 154  VAL B CA  1 
ATOM   2902 C C   . VAL B 1 152 ? 16.705  -13.851 -29.796 1.00 11.61 ? 154  VAL B C   1 
ATOM   2903 O O   . VAL B 1 152 ? 17.008  -14.024 -30.995 1.00 12.16 ? 154  VAL B O   1 
ATOM   2904 C CB  . VAL B 1 152 ? 15.752  -16.080 -28.823 1.00 13.30 ? 154  VAL B CB  1 
ATOM   2905 C CG1 . VAL B 1 152 ? 15.933  -16.941 -30.077 1.00 14.51 ? 154  VAL B CG1 1 
ATOM   2906 C CG2 . VAL B 1 152 ? 16.927  -16.202 -27.865 1.00 13.55 ? 154  VAL B CG2 1 
ATOM   2907 N N   . ASN B 1 153 ? 17.371  -13.070 -28.996 1.00 12.09 ? 155  ASN B N   1 
ATOM   2908 C CA  . ASN B 1 153 ? 18.606  -12.395 -29.366 1.00 14.37 ? 155  ASN B CA  1 
ATOM   2909 C C   . ASN B 1 153 ? 19.750  -13.020 -28.565 1.00 15.34 ? 155  ASN B C   1 
ATOM   2910 O O   . ASN B 1 153 ? 19.705  -12.993 -27.360 1.00 15.77 ? 155  ASN B O   1 
ATOM   2911 C CB  . ASN B 1 153 ? 18.560  -10.900 -29.013 1.00 16.23 ? 155  ASN B CB  1 
ATOM   2912 C CG  . ASN B 1 153 ? 17.326  -10.140 -29.388 1.00 20.42 ? 155  ASN B CG  1 
ATOM   2913 O OD1 . ASN B 1 153 ? 16.585  -9.657  -28.532 1.00 20.45 ? 155  ASN B OD1 1 
ATOM   2914 N ND2 . ASN B 1 153 ? 17.110  -9.984  -30.654 1.00 22.41 ? 155  ASN B ND2 1 
ATOM   2915 N N   . VAL B 1 154 ? 20.716  -13.572 -29.234 1.00 14.92 ? 156  VAL B N   1 
ATOM   2916 C CA  . VAL B 1 154 ? 21.918  -14.189 -28.642 1.00 16.41 ? 156  VAL B CA  1 
ATOM   2917 C C   . VAL B 1 154 ? 22.994  -13.094 -28.616 1.00 15.75 ? 156  VAL B C   1 
ATOM   2918 O O   . VAL B 1 154 ? 23.346  -12.607 -29.677 1.00 15.81 ? 156  VAL B O   1 
ATOM   2919 C CB  . VAL B 1 154 ? 22.407  -15.409 -29.429 1.00 15.59 ? 156  VAL B CB  1 
ATOM   2920 C CG1 . VAL B 1 154 ? 23.646  -16.013 -28.759 1.00 16.61 ? 156  VAL B CG1 1 
ATOM   2921 C CG2 . VAL B 1 154 ? 21.279  -16.446 -29.520 1.00 17.12 ? 156  VAL B CG2 1 
ATOM   2922 N N   . ARG B 1 155 ? 23.435  -12.722 -27.428 1.00 15.60 ? 157  ARG B N   1 
ATOM   2923 C CA  . ARG B 1 155 ? 24.380  -11.617 -27.237 1.00 19.00 ? 157  ARG B CA  1 
ATOM   2924 C C   . ARG B 1 155 ? 25.405  -11.918 -26.150 1.00 21.78 ? 157  ARG B C   1 
ATOM   2925 O O   . ARG B 1 155 ? 25.057  -12.450 -25.079 1.00 22.99 ? 157  ARG B O   1 
ATOM   2926 C CB  . ARG B 1 155 ? 23.652  -10.335 -26.828 1.00 22.61 ? 157  ARG B CB  1 
ATOM   2927 C CG  . ARG B 1 155 ? 22.652  -9.808  -27.869 1.00 22.67 ? 157  ARG B CG  1 
ATOM   2928 C CD  . ARG B 1 155 ? 23.289  -9.348  -29.154 1.00 22.99 ? 157  ARG B CD  1 
ATOM   2929 N NE  . ARG B 1 155 ? 22.295  -8.740  -30.060 1.00 23.33 ? 157  ARG B NE  1 
ATOM   2930 C CZ  . ARG B 1 155 ? 21.532  -9.397  -30.926 1.00 23.13 ? 157  ARG B CZ  1 
ATOM   2931 N NH1 . ARG B 1 155 ? 21.618  -10.721 -31.037 1.00 19.53 ? 157  ARG B NH1 1 
ATOM   2932 N NH2 . ARG B 1 155 ? 20.647  -8.743  -31.671 1.00 23.24 ? 157  ARG B NH2 1 
ATOM   2933 N N   . ALA B 1 156 ? 26.665  -11.543 -26.402 1.00 21.82 ? 158  ALA B N   1 
ATOM   2934 C CA  . ALA B 1 156 ? 27.698  -11.657 -25.367 1.00 24.83 ? 158  ALA B CA  1 
ATOM   2935 C C   . ALA B 1 156 ? 27.331  -10.919 -24.061 1.00 27.09 ? 158  ALA B C   1 
ATOM   2936 O O   . ALA B 1 156 ? 27.629  -11.417 -22.983 1.00 27.75 ? 158  ALA B O   1 
ATOM   2937 C CB  . ALA B 1 156 ? 29.006  -11.127 -25.912 1.00 25.15 ? 158  ALA B CB  1 
ATOM   2938 N N   . LYS B 1 157 ? 26.697  -9.749  -24.147 1.00 29.05 ? 159  LYS B N   1 
ATOM   2939 C CA  . LYS B 1 157 ? 26.285  -8.963  -22.956 1.00 30.54 ? 159  LYS B CA  1 
ATOM   2940 C C   . LYS B 1 157 ? 25.121  -9.583  -22.166 1.00 30.69 ? 159  LYS B C   1 
ATOM   2941 O O   . LYS B 1 157 ? 24.904  -9.252  -20.986 1.00 32.77 ? 159  LYS B O   1 
ATOM   2942 C CB  . LYS B 1 157 ? 25.916  -7.534  -23.411 1.00 35.22 ? 159  LYS B CB  1 
ATOM   2943 C CG  . LYS B 1 157 ? 25.330  -6.600  -22.355 1.00 44.36 ? 159  LYS B CG  1 
ATOM   2944 C CD  . LYS B 1 157 ? 24.943  -5.249  -22.978 1.00 51.20 ? 159  LYS B CD  1 
ATOM   2945 C CE  . LYS B 1 157 ? 24.620  -4.188  -21.939 1.00 56.86 ? 159  LYS B CE  1 
ATOM   2946 N NZ  . LYS B 1 157 ? 24.469  -2.814  -22.535 1.00 61.12 ? 159  LYS B NZ  1 
ATOM   2947 N N   . GLY B 1 158 ? 24.368  -10.483 -22.788 1.00 28.18 ? 160  GLY B N   1 
ATOM   2948 C CA  . GLY B 1 158 ? 23.279  -11.180 -22.119 1.00 24.83 ? 160  GLY B CA  1 
ATOM   2949 C C   . GLY B 1 158 ? 22.163  -11.424 -23.122 1.00 21.72 ? 160  GLY B C   1 
ATOM   2950 O O   . GLY B 1 158 ? 21.775  -10.511 -23.845 1.00 22.35 ? 160  GLY B O   1 
ATOM   2951 N N   . ASP B 1 159 ? 21.669  -12.641 -23.179 1.00 19.13 ? 161  ASP B N   1 
ATOM   2952 C CA  . ASP B 1 159 ? 20.671  -13.017 -24.182 1.00 16.93 ? 161  ASP B CA  1 
ATOM   2953 C C   . ASP B 1 159 ? 19.308  -12.422 -23.783 1.00 14.44 ? 161  ASP B C   1 
ATOM   2954 O O   . ASP B 1 159 ? 19.059  -12.123 -22.611 1.00 15.54 ? 161  ASP B O   1 
ATOM   2955 C CB  . ASP B 1 159 ? 20.583  -14.541 -24.287 1.00 16.85 ? 161  ASP B CB  1 
ATOM   2956 C CG  . ASP B 1 159 ? 21.900  -15.213 -24.616 1.00 19.86 ? 161  ASP B CG  1 
ATOM   2957 O OD1 . ASP B 1 159 ? 22.693  -14.620 -25.381 1.00 19.17 ? 161  ASP B OD1 1 
ATOM   2958 O OD2 . ASP B 1 159 ? 22.144  -16.346 -24.085 1.00 23.90 ? 161  ASP B OD2 1 
ATOM   2959 N N   . LYS B 1 160 ? 18.416  -12.280 -24.772 1.00 14.00 ? 162  LYS B N   1 
ATOM   2960 C CA  . LYS B 1 160 ? 17.091  -11.709 -24.491 1.00 12.75 ? 162  LYS B CA  1 
ATOM   2961 C C   . LYS B 1 160 ? 16.067  -12.582 -25.203 1.00 12.02 ? 162  LYS B C   1 
ATOM   2962 O O   . LYS B 1 160 ? 16.336  -13.067 -26.318 1.00 13.45 ? 162  LYS B O   1 
ATOM   2963 C CB  . LYS B 1 160 ? 16.957  -10.301 -25.032 1.00 14.94 ? 162  LYS B CB  1 
ATOM   2964 C CG  . LYS B 1 160 ? 17.869  -9.288  -24.352 1.00 21.93 ? 162  LYS B CG  1 
ATOM   2965 C CD  . LYS B 1 160 ? 17.823  -7.937  -25.055 1.00 31.32 ? 162  LYS B CD  1 
ATOM   2966 C CE  . LYS B 1 160 ? 18.808  -7.887  -26.209 1.00 41.23 ? 162  LYS B CE  1 
ATOM   2967 N NZ  . LYS B 1 160 ? 18.954  -6.519  -26.809 1.00 46.31 ? 162  LYS B NZ  1 
ATOM   2968 N N   . ILE B 1 161 ? 14.906  -12.778 -24.547 1.00 12.16 ? 163  ILE B N   1 
ATOM   2969 C CA  . ILE B 1 161 ? 13.741  -13.434 -25.195 1.00 9.94  ? 163  ILE B CA  1 
ATOM   2970 C C   . ILE B 1 161 ? 12.590  -12.502 -25.046 1.00 9.72  ? 163  ILE B C   1 
ATOM   2971 O O   . ILE B 1 161 ? 12.417  -11.925 -23.982 1.00 11.15 ? 163  ILE B O   1 
ATOM   2972 C CB  . ILE B 1 161 ? 13.418  -14.806 -24.577 1.00 11.89 ? 163  ILE B CB  1 
ATOM   2973 C CG1 . ILE B 1 161 ? 14.617  -15.748 -24.742 1.00 11.38 ? 163  ILE B CG1 1 
ATOM   2974 C CG2 . ILE B 1 161 ? 12.144  -15.378 -25.127 1.00 11.00 ? 163  ILE B CG2 1 
ATOM   2975 C CD1 . ILE B 1 161 ? 14.489  -17.021 -23.962 1.00 12.85 ? 163  ILE B CD1 1 
ATOM   2976 N N   . ALA B 1 162 ? 11.781  -12.363 -26.080 1.00 10.19 ? 164  ALA B N   1 
ATOM   2977 C CA  . ALA B 1 162 ? 10.614  -11.517 -25.972 1.00 9.25  ? 164  ALA B CA  1 
ATOM   2978 C C   . ALA B 1 162 ? 9.428   -12.052 -26.700 1.00 9.69  ? 164  ALA B C   1 
ATOM   2979 O O   . ALA B 1 162 ? 9.583   -12.651 -27.742 1.00 12.50 ? 164  ALA B O   1 
ATOM   2980 C CB  . ALA B 1 162 ? 10.926  -10.098 -26.440 1.00 9.89  ? 164  ALA B CB  1 
ATOM   2981 N N   . ILE B 1 163 ? 8.234   -11.859 -26.125 1.00 7.91  ? 165  ILE B N   1 
ATOM   2982 C CA  . ILE B 1 163 ? 6.972   -12.072 -26.831 1.00 7.93  ? 165  ILE B CA  1 
ATOM   2983 C C   . ILE B 1 163 ? 6.456   -10.701 -27.316 1.00 8.98  ? 165  ILE B C   1 
ATOM   2984 O O   . ILE B 1 163 ? 6.219   -9.792  -26.486 1.00 8.85  ? 165  ILE B O   1 
ATOM   2985 C CB  . ILE B 1 163 ? 5.898   -12.822 -25.992 1.00 8.60  ? 165  ILE B CB  1 
ATOM   2986 C CG1 . ILE B 1 163 ? 6.316   -14.300 -25.772 1.00 8.14  ? 165  ILE B CG1 1 
ATOM   2987 C CG2 . ILE B 1 163 ? 4.516   -12.769 -26.768 1.00 8.21  ? 165  ILE B CG2 1 
ATOM   2988 C CD1 . ILE B 1 163 ? 5.339   -15.097 -24.925 1.00 8.75  ? 165  ILE B CD1 1 
ATOM   2989 N N   . TRP B 1 164 ? 6.259   -10.571 -28.633 1.00 7.18  ? 166  TRP B N   1 
ATOM   2990 C CA  . TRP B 1 164 ? 5.756   -9.377  -29.257 1.00 6.90  ? 166  TRP B CA  1 
ATOM   2991 C C   . TRP B 1 164 ? 4.233   -9.497  -29.399 1.00 9.16  ? 166  TRP B C   1 
ATOM   2992 O O   . TRP B 1 164 ? 3.697   -10.511 -29.852 1.00 10.23 ? 166  TRP B O   1 
ATOM   2993 C CB  . TRP B 1 164 ? 6.295   -9.194  -30.665 1.00 6.93  ? 166  TRP B CB  1 
ATOM   2994 C CG  . TRP B 1 164 ? 7.751   -8.840  -30.743 1.00 9.20  ? 166  TRP B CG  1 
ATOM   2995 C CD1 . TRP B 1 164 ? 8.728   -9.109  -29.843 1.00 10.70 ? 166  TRP B CD1 1 
ATOM   2996 C CD2 . TRP B 1 164 ? 8.365   -8.089  -31.803 1.00 9.98  ? 166  TRP B CD2 1 
ATOM   2997 N NE1 . TRP B 1 164 ? 9.955   -8.620  -30.315 1.00 11.12 ? 166  TRP B NE1 1 
ATOM   2998 C CE2 . TRP B 1 164 ? 9.747   -8.001  -31.512 1.00 10.74 ? 166  TRP B CE2 1 
ATOM   2999 C CE3 . TRP B 1 164 ? 7.897   -7.554  -33.007 1.00 10.23 ? 166  TRP B CE3 1 
ATOM   3000 C CZ2 . TRP B 1 164 ? 10.631  -7.350  -32.365 1.00 12.31 ? 166  TRP B CZ2 1 
ATOM   3001 C CZ3 . TRP B 1 164 ? 8.789   -6.901  -33.857 1.00 12.96 ? 166  TRP B CZ3 1 
ATOM   3002 C CH2 . TRP B 1 164 ? 10.126  -6.795  -33.518 1.00 13.08 ? 166  TRP B CH2 1 
ATOM   3003 N N   . THR B 1 165 ? 3.571   -8.423  -29.049 1.00 8.33  ? 167  THR B N   1 
ATOM   3004 C CA  . THR B 1 165 ? 2.096   -8.350  -29.171 1.00 7.31  ? 167  THR B CA  1 
ATOM   3005 C C   . THR B 1 165 ? 1.721   -7.082  -30.043 1.00 10.04 ? 167  THR B C   1 
ATOM   3006 O O   . THR B 1 165 ? 2.544   -6.204  -30.262 1.00 11.91 ? 167  THR B O   1 
ATOM   3007 C CB  . THR B 1 165 ? 1.352   -8.321  -27.786 1.00 8.96  ? 167  THR B CB  1 
ATOM   3008 O OG1 . THR B 1 165 ? 1.262   -6.990  -27.253 1.00 9.43  ? 167  THR B OG1 1 
ATOM   3009 C CG2 . THR B 1 165 ? 1.948   -9.226  -26.764 1.00 6.04  ? 167  THR B CG2 1 
ATOM   3010 N N   . THR B 1 166 ? 0.495   -7.058  -30.535 1.00 10.27 ? 168  THR B N   1 
ATOM   3011 C CA  . THR B 1 166 ? 0.088   -6.223  -31.643 1.00 11.47 ? 168  THR B CA  1 
ATOM   3012 C C   . THR B 1 166 ? -0.268  -4.794  -31.244 1.00 12.48 ? 168  THR B C   1 
ATOM   3013 O O   . THR B 1 166 ? -0.194  -3.915  -32.084 1.00 13.48 ? 168  THR B O   1 
ATOM   3014 C CB  . THR B 1 166 ? -1.080  -6.871  -32.394 1.00 11.29 ? 168  THR B CB  1 
ATOM   3015 O OG1 . THR B 1 166 ? -1.276  -6.248  -33.667 1.00 13.70 ? 168  THR B OG1 1 
ATOM   3016 C CG2 . THR B 1 166 ? -2.406  -6.816  -31.617 1.00 10.23 ? 168  THR B CG2 1 
ATOM   3017 N N   . GLU B 1 167 ? -0.677  -4.569  -29.971 1.00 13.02 ? 169  GLU B N   1 
ATOM   3018 C CA  . GLU B 1 167 ? -1.286  -3.314  -29.573 1.00 13.56 ? 169  GLU B CA  1 
ATOM   3019 C C   . GLU B 1 167 ? -0.903  -2.978  -28.178 1.00 13.29 ? 169  GLU B C   1 
ATOM   3020 O O   . GLU B 1 167 ? -1.433  -3.577  -27.245 1.00 14.15 ? 169  GLU B O   1 
ATOM   3021 C CB  . GLU B 1 167 ? -2.821  -3.411  -29.726 1.00 13.70 ? 169  GLU B CB  1 
ATOM   3022 C CG  . GLU B 1 167 ? -3.602  -2.169  -29.306 1.00 17.42 ? 169  GLU B CG  1 
ATOM   3023 C CD  . GLU B 1 167 ? -3.079  -0.861  -29.864 1.00 20.20 ? 169  GLU B CD  1 
ATOM   3024 O OE1 . GLU B 1 167 ? -3.197  -0.619  -31.084 1.00 20.73 ? 169  GLU B OE1 1 
ATOM   3025 O OE2 . GLU B 1 167 ? -2.510  -0.093  -29.070 1.00 18.86 ? 169  GLU B OE2 1 
ATOM   3026 N N   . CYS B 1 168 ? 0.011   -2.035  -27.993 1.00 13.45 ? 170  CYS B N   1 
ATOM   3027 C CA  . CYS B 1 168 ? 0.546   -1.755  -26.651 1.00 16.02 ? 170  CYS B CA  1 
ATOM   3028 C C   . CYS B 1 168 ? -0.520  -1.139  -25.720 1.00 18.49 ? 170  CYS B C   1 
ATOM   3029 O O   . CYS B 1 168 ? -0.294  -1.137  -24.500 1.00 19.29 ? 170  CYS B O   1 
ATOM   3030 C CB  . CYS B 1 168 ? 1.799   -0.885  -26.763 1.00 16.45 ? 170  CYS B CB  1 
ATOM   3031 S SG  . CYS B 1 168 ? 1.460   0.754   -27.445 1.00 21.94 ? 170  CYS B SG  1 
ATOM   3032 N N   . GLU B 1 169 ? -1.664  -0.615  -26.261 1.00 18.18 ? 171  GLU B N   1 
ATOM   3033 C CA  . GLU B 1 169 ? -2.734  -0.069  -25.416 1.00 19.07 ? 171  GLU B CA  1 
ATOM   3034 C C   . GLU B 1 169 ? -3.888  -1.014  -25.121 1.00 20.40 ? 171  GLU B C   1 
ATOM   3035 O O   . GLU B 1 169 ? -4.868  -0.611  -24.473 1.00 22.22 ? 171  GLU B O   1 
ATOM   3036 C CB  . GLU B 1 169 ? -3.245  1.235   -26.044 1.00 23.74 ? 171  GLU B CB  1 
ATOM   3037 C CG  . GLU B 1 169 ? -2.056  2.151   -26.156 1.00 28.20 ? 171  GLU B CG  1 
ATOM   3038 C CD  . GLU B 1 169 ? -2.402  3.579   -26.416 1.00 39.01 ? 171  GLU B CD  1 
ATOM   3039 O OE1 . GLU B 1 169 ? -2.879  3.874   -27.531 1.00 39.20 ? 171  GLU B OE1 1 
ATOM   3040 O OE2 . GLU B 1 169 ? -2.185  4.401   -25.505 1.00 41.35 ? 171  GLU B OE2 1 
ATOM   3041 N N   . ASN B 1 170 ? -3.784  -2.288  -25.564 1.00 17.43 ? 172  ASN B N   1 
ATOM   3042 C CA  . ASN B 1 170 ? -4.709  -3.330  -25.118 1.00 16.38 ? 172  ASN B CA  1 
ATOM   3043 C C   . ASN B 1 170 ? -4.284  -3.870  -23.737 1.00 17.27 ? 172  ASN B C   1 
ATOM   3044 O O   . ASN B 1 170 ? -3.694  -4.962  -23.612 1.00 16.37 ? 172  ASN B O   1 
ATOM   3045 C CB  . ASN B 1 170 ? -4.814  -4.468  -26.146 1.00 19.19 ? 172  ASN B CB  1 
ATOM   3046 C CG  . ASN B 1 170 ? -5.576  -4.199  -27.417 1.00 24.23 ? 172  ASN B CG  1 
ATOM   3047 O OD1 . ASN B 1 170 ? -6.369  -3.227  -27.498 1.00 26.54 ? 172  ASN B OD1 1 
ATOM   3048 N ND2 . ASN B 1 170 ? -5.388  -5.070  -28.443 1.00 24.04 ? 172  ASN B ND2 1 
ATOM   3049 N N   . ARG B 1 171 ? -4.621  -3.108  -22.684 1.00 18.13 ? 173  ARG B N   1 
ATOM   3050 C CA  . ARG B 1 171 ? -4.164  -3.367  -21.318 1.00 20.26 ? 173  ARG B CA  1 
ATOM   3051 C C   . ARG B 1 171 ? -4.494  -4.748  -20.817 1.00 18.36 ? 173  ARG B C   1 
ATOM   3052 O O   . ARG B 1 171 ? -3.612  -5.425  -20.271 1.00 19.54 ? 173  ARG B O   1 
ATOM   3053 C CB  . ARG B 1 171 ? -4.774  -2.317  -20.334 1.00 25.61 ? 173  ARG B CB  1 
ATOM   3054 C CG  . ARG B 1 171 ? -4.492  -2.644  -18.865 1.00 34.50 ? 173  ARG B CG  1 
ATOM   3055 C CD  . ARG B 1 171 ? -4.993  -1.551  -17.932 1.00 42.30 ? 173  ARG B CD  1 
ATOM   3056 N NE  . ARG B 1 171 ? -4.108  -0.398  -17.940 1.00 49.42 ? 173  ARG B NE  1 
ATOM   3057 C CZ  . ARG B 1 171 ? -2.986  -0.295  -17.230 1.00 53.32 ? 173  ARG B CZ  1 
ATOM   3058 N NH1 . ARG B 1 171 ? -2.581  -1.304  -16.461 1.00 52.54 ? 173  ARG B NH1 1 
ATOM   3059 N NH2 . ARG B 1 171 ? -2.243  0.813   -17.304 1.00 54.19 ? 173  ARG B NH2 1 
ATOM   3060 N N   . GLU B 1 172 ? -5.777  -5.184  -20.974 1.00 17.33 ? 174  GLU B N   1 
ATOM   3061 C CA  . GLU B 1 172 ? -6.197  -6.480  -20.478 1.00 17.85 ? 174  GLU B CA  1 
ATOM   3062 C C   . GLU B 1 172 ? -5.455  -7.626  -21.191 1.00 15.71 ? 174  GLU B C   1 
ATOM   3063 O O   . GLU B 1 172 ? -4.948  -8.552  -20.531 1.00 14.74 ? 174  GLU B O   1 
ATOM   3064 C CB  . GLU B 1 172 ? -7.705  -6.681  -20.599 1.00 23.40 ? 174  GLU B CB  1 
ATOM   3065 C CG  . GLU B 1 172 ? -8.486  -5.889  -19.557 1.00 33.58 ? 174  GLU B CG  1 
ATOM   3066 C CD  . GLU B 1 172 ? -9.739  -5.193  -20.062 1.00 49.05 ? 174  GLU B CD  1 
ATOM   3067 O OE1 . GLU B 1 172 ? -9.742  -3.938  -20.092 1.00 51.21 ? 174  GLU B OE1 1 
ATOM   3068 O OE2 . GLU B 1 172 ? -10.709 -5.894  -20.439 1.00 52.96 ? 174  GLU B OE2 1 
ATOM   3069 N N   . ALA B 1 173 ? -5.373  -7.560  -22.523 1.00 14.94 ? 175  ALA B N   1 
ATOM   3070 C CA  . ALA B 1 173 ? -4.654  -8.578  -23.289 1.00 15.17 ? 175  ALA B CA  1 
ATOM   3071 C C   . ALA B 1 173 ? -3.183  -8.616  -22.896 1.00 13.59 ? 175  ALA B C   1 
ATOM   3072 O O   . ALA B 1 173 ? -2.629  -9.685  -22.588 1.00 13.60 ? 175  ALA B O   1 
ATOM   3073 C CB  . ALA B 1 173 ? -4.818  -8.293  -24.789 1.00 15.41 ? 175  ALA B CB  1 
ATOM   3074 N N   . VAL B 1 174 ? -2.516  -7.459  -22.887 1.00 10.76 ? 176  VAL B N   1 
ATOM   3075 C CA  . VAL B 1 174 ? -1.082  -7.411  -22.650 1.00 10.84 ? 176  VAL B CA  1 
ATOM   3076 C C   . VAL B 1 174 ? -0.775  -7.951  -21.238 1.00 11.36 ? 176  VAL B C   1 
ATOM   3077 O O   . VAL B 1 174 ? 0.181   -8.720  -21.073 1.00 10.61 ? 176  VAL B O   1 
ATOM   3078 C CB  . VAL B 1 174 ? -0.550  -5.963  -22.832 1.00 11.79 ? 176  VAL B CB  1 
ATOM   3079 C CG1 . VAL B 1 174 ? 0.841   -5.847  -22.262 1.00 14.25 ? 176  VAL B CG1 1 
ATOM   3080 C CG2 . VAL B 1 174 ? -0.587  -5.540  -24.312 1.00 10.65 ? 176  VAL B CG2 1 
ATOM   3081 N N   . THR B 1 175 ? -1.586  -7.547  -20.264 1.00 12.27 ? 177  THR B N   1 
ATOM   3082 C CA  . THR B 1 175 ? -1.308  -7.947  -18.885 1.00 13.95 ? 177  THR B CA  1 
ATOM   3083 C C   . THR B 1 175 ? -1.549  -9.453  -18.721 1.00 13.19 ? 177  THR B C   1 
ATOM   3084 O O   . THR B 1 175 ? -0.749  -10.143 -18.074 1.00 12.64 ? 177  THR B O   1 
ATOM   3085 C CB  . THR B 1 175 ? -2.025  -7.058  -17.888 1.00 17.52 ? 177  THR B CB  1 
ATOM   3086 O OG1 . THR B 1 175 ? -3.416  -7.187  -18.009 1.00 26.67 ? 177  THR B OG1 1 
ATOM   3087 C CG2 . THR B 1 175 ? -1.659  -5.637  -18.010 1.00 14.01 ? 177  THR B CG2 1 
ATOM   3088 N N   . HIS B 1 176 ? -2.633  -9.997  -19.303 1.00 13.78 ? 178  HIS B N   1 
ATOM   3089 C CA  . HIS B 1 176 ? -2.880  -11.453 -19.238 1.00 12.61 ? 178  HIS B CA  1 
ATOM   3090 C C   . HIS B 1 176 ? -1.742  -12.234 -19.846 1.00 11.30 ? 178  HIS B C   1 
ATOM   3091 O O   . HIS B 1 176 ? -1.246  -13.205 -19.267 1.00 10.36 ? 178  HIS B O   1 
ATOM   3092 C CB  . HIS B 1 176 ? -4.191  -11.827 -19.901 1.00 14.27 ? 178  HIS B CB  1 
ATOM   3093 C CG  . HIS B 1 176 ? -4.476  -13.300 -19.800 1.00 16.74 ? 178  HIS B CG  1 
ATOM   3094 N ND1 . HIS B 1 176 ? -4.885  -13.881 -18.588 1.00 20.70 ? 178  HIS B ND1 1 
ATOM   3095 C CD2 . HIS B 1 176 ? -4.371  -14.273 -20.721 1.00 17.15 ? 178  HIS B CD2 1 
ATOM   3096 C CE1 . HIS B 1 176 ? -5.025  -15.170 -18.832 1.00 19.01 ? 178  HIS B CE1 1 
ATOM   3097 N NE2 . HIS B 1 176 ? -4.765  -15.453 -20.113 1.00 16.25 ? 178  HIS B NE2 1 
ATOM   3098 N N   . ILE B 1 177 ? -1.261  -11.825 -21.038 1.00 10.88 ? 179  ILE B N   1 
ATOM   3099 C CA  . ILE B 1 177 ? -0.153  -12.484 -21.660 1.00 9.20  ? 179  ILE B CA  1 
ATOM   3100 C C   . ILE B 1 177 ? 1.063   -12.474 -20.730 1.00 10.03 ? 179  ILE B C   1 
ATOM   3101 O O   . ILE B 1 177 ? 1.690   -13.493 -20.549 1.00 10.77 ? 179  ILE B O   1 
ATOM   3102 C CB  . ILE B 1 177 ? 0.168   -11.821 -23.019 1.00 9.16  ? 179  ILE B CB  1 
ATOM   3103 C CG1 . ILE B 1 177 ? -0.981  -12.070 -24.014 1.00 8.56  ? 179  ILE B CG1 1 
ATOM   3104 C CG2 . ILE B 1 177 ? 1.494   -12.343 -23.597 1.00 8.86  ? 179  ILE B CG2 1 
ATOM   3105 C CD1 . ILE B 1 177 ? -0.962  -11.187 -25.225 1.00 10.61 ? 179  ILE B CD1 1 
ATOM   3106 N N   . GLY B 1 178 ? 1.378   -11.341 -20.140 1.00 9.55  ? 180  GLY B N   1 
ATOM   3107 C CA  . GLY B 1 178 ? 2.580   -11.262 -19.292 1.00 9.45  ? 180  GLY B CA  1 
ATOM   3108 C C   . GLY B 1 178 ? 2.479   -12.165 -18.072 1.00 10.76 ? 180  GLY B C   1 
ATOM   3109 O O   . GLY B 1 178 ? 3.436   -12.858 -17.719 1.00 11.12 ? 180  GLY B O   1 
ATOM   3110 N N   . ARG B 1 179 ? 1.294   -12.155 -17.401 1.00 10.06 ? 181  ARG B N   1 
ATOM   3111 C CA  . ARG B 1 179 ? 1.120   -13.007 -16.211 1.00 11.68 ? 181  ARG B CA  1 
ATOM   3112 C C   . ARG B 1 179 ? 1.284   -14.502 -16.520 1.00 11.35 ? 181  ARG B C   1 
ATOM   3113 O O   . ARG B 1 179 ? 2.034   -15.232 -15.861 1.00 11.93 ? 181  ARG B O   1 
ATOM   3114 C CB  . ARG B 1 179 ? -0.212  -12.689 -15.566 1.00 14.47 ? 181  ARG B CB  1 
ATOM   3115 C CG  . ARG B 1 179 ? -0.266  -11.321 -14.956 1.00 19.54 ? 181  ARG B CG  1 
ATOM   3116 C CD  . ARG B 1 179 ? -1.455  -11.259 -14.081 1.00 25.03 ? 181  ARG B CD  1 
ATOM   3117 N NE  . ARG B 1 179 ? -1.894  -9.904  -13.728 1.00 29.37 ? 181  ARG B NE  1 
ATOM   3118 C CZ  . ARG B 1 179 ? -1.287  -9.085  -12.873 1.00 31.48 ? 181  ARG B CZ  1 
ATOM   3119 N NH1 . ARG B 1 179 ? -1.798  -7.892  -12.616 1.00 33.46 ? 181  ARG B NH1 1 
ATOM   3120 N NH2 . ARG B 1 179 ? -0.148  -9.441  -12.287 1.00 26.87 ? 181  ARG B NH2 1 
ATOM   3121 N N   . VAL B 1 180 ? 0.606   -14.969 -17.575 1.00 11.30 ? 182  VAL B N   1 
ATOM   3122 C CA  . VAL B 1 180 ? 0.666   -16.363 -17.985 1.00 10.63 ? 182  VAL B CA  1 
ATOM   3123 C C   . VAL B 1 180 ? 2.062   -16.718 -18.463 1.00 10.14 ? 182  VAL B C   1 
ATOM   3124 O O   . VAL B 1 180 ? 2.532   -17.801 -18.147 1.00 10.28 ? 182  VAL B O   1 
ATOM   3125 C CB  . VAL B 1 180 ? -0.416  -16.690 -19.009 1.00 12.71 ? 182  VAL B CB  1 
ATOM   3126 C CG1 . VAL B 1 180 ? -0.267  -18.113 -19.512 1.00 15.15 ? 182  VAL B CG1 1 
ATOM   3127 C CG2 . VAL B 1 180 ? -1.791  -16.467 -18.449 1.00 12.81 ? 182  VAL B CG2 1 
ATOM   3128 N N   . TYR B 1 181 ? 2.735   -15.824 -19.177 1.00 8.98  ? 183  TYR B N   1 
ATOM   3129 C CA  . TYR B 1 181 ? 4.089   -16.082 -19.648 1.00 10.05 ? 183  TYR B CA  1 
ATOM   3130 C C   . TYR B 1 181 ? 5.066   -16.279 -18.485 1.00 11.22 ? 183  TYR B C   1 
ATOM   3131 O O   . TYR B 1 181 ? 5.810   -17.274 -18.441 1.00 9.52  ? 183  TYR B O   1 
ATOM   3132 C CB  . TYR B 1 181 ? 4.525   -14.953 -20.550 1.00 10.00 ? 183  TYR B CB  1 
ATOM   3133 C CG  . TYR B 1 181 ? 5.859   -15.095 -21.226 1.00 9.17  ? 183  TYR B CG  1 
ATOM   3134 C CD1 . TYR B 1 181 ? 6.323   -16.334 -21.653 1.00 10.50 ? 183  TYR B CD1 1 
ATOM   3135 C CD2 . TYR B 1 181 ? 6.643   -13.991 -21.485 1.00 9.78  ? 183  TYR B CD2 1 
ATOM   3136 C CE1 . TYR B 1 181 ? 7.531   -16.449 -22.347 1.00 10.33 ? 183  TYR B CE1 1 
ATOM   3137 C CE2 . TYR B 1 181 ? 7.814   -14.089 -22.199 1.00 9.27  ? 183  TYR B CE2 1 
ATOM   3138 C CZ  . TYR B 1 181 ? 8.302   -15.322 -22.562 1.00 11.14 ? 183  TYR B CZ  1 
ATOM   3139 O OH  . TYR B 1 181 ? 9.461   -15.351 -23.285 1.00 12.15 ? 183  TYR B OH  1 
ATOM   3140 N N   . LYS B 1 182 ? 5.022   -15.344 -17.527 1.00 11.11 ? 184  LYS B N   1 
ATOM   3141 C CA  . LYS B 1 182 ? 5.805   -15.463 -16.288 1.00 11.14 ? 184  LYS B CA  1 
ATOM   3142 C C   . LYS B 1 182 ? 5.499   -16.808 -15.570 1.00 12.69 ? 184  LYS B C   1 
ATOM   3143 O O   . LYS B 1 182 ? 6.434   -17.484 -15.131 1.00 12.30 ? 184  LYS B O   1 
ATOM   3144 C CB  . LYS B 1 182 ? 5.525   -14.290 -15.388 1.00 12.59 ? 184  LYS B CB  1 
ATOM   3145 C CG  . LYS B 1 182 ? 6.298   -14.314 -14.095 1.00 12.90 ? 184  LYS B CG  1 
ATOM   3146 C CD  . LYS B 1 182 ? 6.423   -12.995 -13.467 1.00 13.63 ? 184  LYS B CD  1 
ATOM   3147 C CE  . LYS B 1 182 ? 6.857   -13.122 -12.004 1.00 13.91 ? 184  LYS B CE  1 
ATOM   3148 N NZ  . LYS B 1 182 ? 7.025   -11.786 -11.405 1.00 14.69 ? 184  LYS B NZ  1 
ATOM   3149 N N   . GLU B 1 183 ? 4.228   -17.158 -15.424 1.00 12.37 ? 185  GLU B N   1 
ATOM   3150 C CA  . GLU B 1 183 ? 3.786   -18.426 -14.786 1.00 14.27 ? 185  GLU B CA  1 
ATOM   3151 C C   . GLU B 1 183 ? 4.350   -19.625 -15.513 1.00 14.72 ? 185  GLU B C   1 
ATOM   3152 O O   . GLU B 1 183 ? 4.910   -20.525 -14.910 1.00 15.24 ? 185  GLU B O   1 
ATOM   3153 C CB  . GLU B 1 183 ? 2.248   -18.364 -14.733 1.00 17.43 ? 185  GLU B CB  1 
ATOM   3154 C CG  . GLU B 1 183 ? 1.452   -19.556 -14.422 1.00 26.69 ? 185  GLU B CG  1 
ATOM   3155 C CD  . GLU B 1 183 ? 0.018   -19.239 -14.840 1.00 24.30 ? 185  GLU B CD  1 
ATOM   3156 O OE1 . GLU B 1 183 ? -0.611  -20.185 -15.336 1.00 27.07 ? 185  GLU B OE1 1 
ATOM   3157 O OE2 . GLU B 1 183 ? -0.470  -18.098 -14.662 1.00 25.89 ? 185  GLU B OE2 1 
ATOM   3158 N N   . ARG B 1 184 ? 4.248   -19.633 -16.864 1.00 13.50 ? 186  ARG B N   1 
ATOM   3159 C CA  . ARG B 1 184 ? 4.774   -20.714 -17.674 1.00 13.30 ? 186  ARG B CA  1 
ATOM   3160 C C   . ARG B 1 184 ? 6.295   -20.827 -17.721 1.00 14.86 ? 186  ARG B C   1 
ATOM   3161 O O   . ARG B 1 184 ? 6.843   -21.928 -17.837 1.00 16.71 ? 186  ARG B O   1 
ATOM   3162 C CB  . ARG B 1 184 ? 4.196   -20.602 -19.108 1.00 12.35 ? 186  ARG B CB  1 
ATOM   3163 C CG  . ARG B 1 184 ? 2.708   -20.944 -19.133 1.00 16.45 ? 186  ARG B CG  1 
ATOM   3164 C CD  . ARG B 1 184 ? 2.390   -22.429 -19.023 1.00 17.29 ? 186  ARG B CD  1 
ATOM   3165 N NE  . ARG B 1 184 ? 2.945   -23.131 -20.148 1.00 14.44 ? 186  ARG B NE  1 
ATOM   3166 C CZ  . ARG B 1 184 ? 2.280   -23.531 -21.244 1.00 12.74 ? 186  ARG B CZ  1 
ATOM   3167 N NH1 . ARG B 1 184 ? 0.983   -23.294 -21.372 1.00 13.04 ? 186  ARG B NH1 1 
ATOM   3168 N NH2 . ARG B 1 184 ? 2.916   -24.138 -22.215 1.00 14.99 ? 186  ARG B NH2 1 
ATOM   3169 N N   . LEU B 1 185 ? 7.010   -19.693 -17.641 1.00 13.91 ? 187  LEU B N   1 
ATOM   3170 C CA  . LEU B 1 185 ? 8.436   -19.696 -17.442 1.00 12.68 ? 187  LEU B CA  1 
ATOM   3171 C C   . LEU B 1 185 ? 8.848   -20.213 -16.061 1.00 16.71 ? 187  LEU B C   1 
ATOM   3172 O O   . LEU B 1 185 ? 10.010  -20.634 -15.886 1.00 18.71 ? 187  LEU B O   1 
ATOM   3173 C CB  . LEU B 1 185 ? 9.009   -18.283 -17.652 1.00 12.18 ? 187  LEU B CB  1 
ATOM   3174 C CG  . LEU B 1 185 ? 8.991   -17.680 -19.058 1.00 13.70 ? 187  LEU B CG  1 
ATOM   3175 C CD1 . LEU B 1 185 ? 9.283   -16.199 -19.019 1.00 14.96 ? 187  LEU B CD1 1 
ATOM   3176 C CD2 . LEU B 1 185 ? 9.888   -18.443 -20.021 1.00 14.38 ? 187  LEU B CD2 1 
ATOM   3177 N N   . GLY B 1 186 ? 7.955   -20.152 -15.088 1.00 16.87 ? 188  GLY B N   1 
ATOM   3178 C CA  . GLY B 1 186 ? 8.257   -20.620 -13.749 1.00 16.57 ? 188  GLY B CA  1 
ATOM   3179 C C   . GLY B 1 186 ? 9.096   -19.647 -12.975 1.00 15.97 ? 188  GLY B C   1 
ATOM   3180 O O   . GLY B 1 186 ? 9.825   -20.073 -12.085 1.00 16.22 ? 188  GLY B O   1 
ATOM   3181 N N   . LEU B 1 187 ? 9.024   -18.351 -13.297 1.00 15.21 ? 189  LEU B N   1 
ATOM   3182 C CA  . LEU B 1 187 ? 9.879   -17.370 -12.647 1.00 15.14 ? 189  LEU B CA  1 
ATOM   3183 C C   . LEU B 1 187 ? 9.343   -17.150 -11.247 1.00 16.86 ? 189  LEU B C   1 
ATOM   3184 O O   . LEU B 1 187 ? 8.131   -17.069 -11.046 1.00 17.07 ? 189  LEU B O   1 
ATOM   3185 C CB  . LEU B 1 187 ? 9.891   -16.023 -13.341 1.00 15.87 ? 189  LEU B CB  1 
ATOM   3186 C CG  . LEU B 1 187 ? 10.356  -15.997 -14.807 1.00 17.54 ? 189  LEU B CG  1 
ATOM   3187 C CD1 . LEU B 1 187 ? 10.303  -14.574 -15.395 1.00 18.23 ? 189  LEU B CD1 1 
ATOM   3188 C CD2 . LEU B 1 187 ? 11.771  -16.482 -14.945 1.00 18.99 ? 189  LEU B CD2 1 
ATOM   3189 N N   . PRO B 1 188 ? 10.235  -17.044 -10.280 1.00 16.78 ? 190  PRO B N   1 
ATOM   3190 C CA  . PRO B 1 188 ? 9.809   -16.638 -8.948  1.00 16.45 ? 190  PRO B CA  1 
ATOM   3191 C C   . PRO B 1 188 ? 9.030   -15.312 -8.973  1.00 13.32 ? 190  PRO B C   1 
ATOM   3192 O O   . PRO B 1 188 ? 9.342   -14.456 -9.770  1.00 13.55 ? 190  PRO B O   1 
ATOM   3193 C CB  . PRO B 1 188 ? 11.136  -16.483 -8.204  1.00 18.90 ? 190  PRO B CB  1 
ATOM   3194 C CG  . PRO B 1 188 ? 12.087  -17.420 -8.914  1.00 19.72 ? 190  PRO B CG  1 
ATOM   3195 C CD  . PRO B 1 188 ? 11.696  -17.303 -10.335 1.00 18.57 ? 190  PRO B CD  1 
ATOM   3196 N N   . PRO B 1 189 ? 8.026   -15.148 -8.112  1.00 13.64 ? 191  PRO B N   1 
ATOM   3197 C CA  . PRO B 1 189 ? 7.300   -13.845 -8.063  1.00 12.37 ? 191  PRO B CA  1 
ATOM   3198 C C   . PRO B 1 189 ? 8.166   -12.608 -8.023  1.00 12.10 ? 191  PRO B C   1 
ATOM   3199 O O   . PRO B 1 189 ? 7.834   -11.597 -8.671  1.00 13.92 ? 191  PRO B O   1 
ATOM   3200 C CB  . PRO B 1 189 ? 6.448   -13.996 -6.816  1.00 12.20 ? 191  PRO B CB  1 
ATOM   3201 C CG  . PRO B 1 189 ? 6.182   -15.498 -6.746  1.00 12.81 ? 191  PRO B CG  1 
ATOM   3202 C CD  . PRO B 1 189 ? 7.474   -16.100 -7.133  1.00 13.49 ? 191  PRO B CD  1 
ATOM   3203 N N   . LYS B 1 190 ? 9.292   -12.646 -7.292  1.00 12.27 ? 192  LYS B N   1 
ATOM   3204 C CA  . LYS B 1 190 ? 10.129  -11.471 -7.146  1.00 12.85 ? 192  LYS B CA  1 
ATOM   3205 C C   . LYS B 1 190 ? 10.905  -11.034 -8.406  1.00 14.07 ? 192  LYS B C   1 
ATOM   3206 O O   . LYS B 1 190 ? 11.414  -9.910  -8.438  1.00 16.00 ? 192  LYS B O   1 
ATOM   3207 C CB  . LYS B 1 190 ? 11.133  -11.667 -6.002  1.00 14.74 ? 192  LYS B CB  1 
ATOM   3208 C CG  . LYS B 1 190 ? 12.193  -12.725 -6.342  1.00 17.61 ? 192  LYS B CG  1 
ATOM   3209 C CD  . LYS B 1 190 ? 13.186  -13.027 -5.197  1.00 24.19 ? 192  LYS B CD  1 
ATOM   3210 C CE  . LYS B 1 190 ? 14.037  -11.852 -4.881  1.00 30.74 ? 192  LYS B CE  1 
ATOM   3211 N NZ  . LYS B 1 190 ? 15.130  -12.169 -3.889  1.00 36.41 ? 192  LYS B NZ  1 
ATOM   3212 N N   . ILE B 1 191 ? 10.988  -11.901 -9.404  1.00 14.11 ? 193  ILE B N   1 
ATOM   3213 C CA  . ILE B 1 191 ? 11.634  -11.606 -10.676 1.00 15.33 ? 193  ILE B CA  1 
ATOM   3214 C C   . ILE B 1 191 ? 10.642  -10.940 -11.576 1.00 14.59 ? 193  ILE B C   1 
ATOM   3215 O O   . ILE B 1 191 ? 9.836   -11.594 -12.186 1.00 15.33 ? 193  ILE B O   1 
ATOM   3216 C CB  . ILE B 1 191 ? 12.225  -12.872 -11.335 1.00 17.76 ? 193  ILE B CB  1 
ATOM   3217 C CG1 . ILE B 1 191 ? 13.231  -13.589 -10.401 1.00 20.55 ? 193  ILE B CG1 1 
ATOM   3218 C CG2 . ILE B 1 191 ? 12.923  -12.502 -12.694 1.00 18.11 ? 193  ILE B CG2 1 
ATOM   3219 C CD1 . ILE B 1 191 ? 14.328  -12.801 -9.935  1.00 23.22 ? 193  ILE B CD1 1 
ATOM   3220 N N   . VAL B 1 192 ? 10.701  -9.634  -11.638 1.00 15.52 ? 194  VAL B N   1 
ATOM   3221 C CA  . VAL B 1 192 ? 9.756   -8.787  -12.359 1.00 18.62 ? 194  VAL B CA  1 
ATOM   3222 C C   . VAL B 1 192 ? 10.112  -8.808  -13.843 1.00 18.30 ? 194  VAL B C   1 
ATOM   3223 O O   . VAL B 1 192 ? 11.281  -8.696  -14.184 1.00 18.52 ? 194  VAL B O   1 
ATOM   3224 C CB  . VAL B 1 192 ? 9.827   -7.350  -11.766 1.00 23.12 ? 194  VAL B CB  1 
ATOM   3225 C CG1 . VAL B 1 192 ? 9.030   -6.370  -12.588 1.00 26.46 ? 194  VAL B CG1 1 
ATOM   3226 C CG2 . VAL B 1 192 ? 9.357   -7.354  -10.308 1.00 24.86 ? 194  VAL B CG2 1 
ATOM   3227 N N   . ILE B 1 193 ? 9.117   -8.986  -14.717 1.00 16.07 ? 195  ILE B N   1 
ATOM   3228 C CA  . ILE B 1 193 ? 9.308   -8.816  -16.153 1.00 15.43 ? 195  ILE B CA  1 
ATOM   3229 C C   . ILE B 1 193 ? 8.480   -7.617  -16.620 1.00 13.60 ? 195  ILE B C   1 
ATOM   3230 O O   . ILE B 1 193 ? 7.455   -7.335  -16.059 1.00 13.40 ? 195  ILE B O   1 
ATOM   3231 C CB  . ILE B 1 193 ? 8.981   -10.084 -16.943 1.00 15.77 ? 195  ILE B CB  1 
ATOM   3232 C CG1 . ILE B 1 193 ? 7.451   -10.403 -16.998 1.00 15.11 ? 195  ILE B CG1 1 
ATOM   3233 C CG2 . ILE B 1 193 ? 9.798   -11.241 -16.401 1.00 16.90 ? 195  ILE B CG2 1 
ATOM   3234 C CD1 . ILE B 1 193 ? 7.053   -11.390 -17.912 1.00 16.97 ? 195  ILE B CD1 1 
ATOM   3235 N N   . GLY B 1 194 ? 8.945   -6.935  -17.670 1.00 13.35 ? 196  GLY B N   1 
ATOM   3236 C CA  . GLY B 1 194 ? 8.357   -5.695  -18.128 1.00 12.73 ? 196  GLY B CA  1 
ATOM   3237 C C   . GLY B 1 194 ? 7.939   -5.699  -19.578 1.00 13.51 ? 196  GLY B C   1 
ATOM   3238 O O   . GLY B 1 194 ? 8.547   -6.409  -20.398 1.00 14.04 ? 196  GLY B O   1 
ATOM   3239 N N   . TYR B 1 195 ? 6.931   -4.910  -19.870 1.00 13.21 ? 197  TYR B N   1 
ATOM   3240 C CA  . TYR B 1 195 ? 6.431   -4.688  -21.234 1.00 13.43 ? 197  TYR B CA  1 
ATOM   3241 C C   . TYR B 1 195 ? 6.753   -3.290  -21.667 1.00 15.32 ? 197  TYR B C   1 
ATOM   3242 O O   . TYR B 1 195 ? 6.506   -2.319  -20.934 1.00 15.61 ? 197  TYR B O   1 
ATOM   3243 C CB  . TYR B 1 195 ? 4.917   -4.910  -21.285 1.00 13.08 ? 197  TYR B CB  1 
ATOM   3244 C CG  . TYR B 1 195 ? 4.311   -4.852  -22.669 1.00 12.58 ? 197  TYR B CG  1 
ATOM   3245 C CD1 . TYR B 1 195 ? 3.863   -3.651  -23.199 1.00 13.69 ? 197  TYR B CD1 1 
ATOM   3246 C CD2 . TYR B 1 195 ? 4.136   -6.010  -23.426 1.00 10.16 ? 197  TYR B CD2 1 
ATOM   3247 C CE1 . TYR B 1 195 ? 3.268   -3.593  -24.449 1.00 13.41 ? 197  TYR B CE1 1 
ATOM   3248 C CE2 . TYR B 1 195 ? 3.561   -5.959  -24.699 1.00 8.64  ? 197  TYR B CE2 1 
ATOM   3249 C CZ  . TYR B 1 195 ? 3.117   -4.751  -25.190 1.00 11.34 ? 197  TYR B CZ  1 
ATOM   3250 O OH  . TYR B 1 195 ? 2.558   -4.648  -26.424 1.00 13.38 ? 197  TYR B OH  1 
ATOM   3251 N N   . GLN B 1 196 ? 7.291   -3.181  -22.870 1.00 15.48 ? 198  GLN B N   1 
ATOM   3252 C CA  . GLN B 1 196 ? 7.591   -1.893  -23.436 1.00 18.29 ? 198  GLN B CA  1 
ATOM   3253 C C   . GLN B 1 196 ? 7.094   -1.843  -24.862 1.00 16.79 ? 198  GLN B C   1 
ATOM   3254 O O   . GLN B 1 196 ? 7.235   -2.816  -25.588 1.00 13.11 ? 198  GLN B O   1 
ATOM   3255 C CB  . GLN B 1 196 ? 9.090   -1.622  -23.328 1.00 23.22 ? 198  GLN B CB  1 
ATOM   3256 C CG  . GLN B 1 196 ? 9.439   -0.151  -23.529 1.00 33.17 ? 198  GLN B CG  1 
ATOM   3257 C CD  . GLN B 1 196 ? 9.607   0.681   -22.262 1.00 43.10 ? 198  GLN B CD  1 
ATOM   3258 O OE1 . GLN B 1 196 ? 8.739   0.699   -21.359 1.00 44.83 ? 198  GLN B OE1 1 
ATOM   3259 N NE2 . GLN B 1 196 ? 10.722  1.409   -22.172 1.00 46.50 ? 198  GLN B NE2 1 
ATOM   3260 N N   . SER B 1 197 ? 6.508   -0.671  -25.269 1.00 16.33 ? 199  SER B N   1 
ATOM   3261 C CA  . SER B 1 197 ? 6.151   -0.464  -26.644 1.00 15.93 ? 199  SER B CA  1 
ATOM   3262 C C   . SER B 1 197 ? 7.368   -0.432  -27.505 1.00 15.03 ? 199  SER B C   1 
ATOM   3263 O O   . SER B 1 197 ? 8.440   -0.084  -27.037 1.00 14.78 ? 199  SER B O   1 
ATOM   3264 C CB  . SER B 1 197 ? 5.303   0.791   -26.840 1.00 16.71 ? 199  SER B CB  1 
ATOM   3265 O OG  . SER B 1 197 ? 6.137   1.912   -26.648 1.00 17.76 ? 199  SER B OG  1 
ATOM   3266 N N   . HIS B 1 198 ? 7.220   -0.817  -28.777 1.00 13.58 ? 200  HIS B N   1 
ATOM   3267 C CA  . HIS B 1 198 ? 8.337   -0.757  -29.709 1.00 14.77 ? 200  HIS B CA  1 
ATOM   3268 C C   . HIS B 1 198 ? 8.791   0.706   -29.865 1.00 17.32 ? 200  HIS B C   1 
ATOM   3269 O O   . HIS B 1 198 ? 9.997   0.940   -29.948 1.00 16.37 ? 200  HIS B O   1 
ATOM   3270 C CB  . HIS B 1 198 ? 7.931   -1.339  -31.052 1.00 14.96 ? 200  HIS B CB  1 
ATOM   3271 C CG  . HIS B 1 198 ? 7.630   -2.811  -30.975 1.00 15.31 ? 200  HIS B CG  1 
ATOM   3272 N ND1 . HIS B 1 198 ? 8.425   -3.660  -30.275 1.00 15.40 ? 200  HIS B ND1 1 
ATOM   3273 C CD2 . HIS B 1 198 ? 6.618   -3.512  -31.534 1.00 15.22 ? 200  HIS B CD2 1 
ATOM   3274 C CE1 . HIS B 1 198 ? 7.888   -4.879  -30.417 1.00 15.69 ? 200  HIS B CE1 1 
ATOM   3275 N NE2 . HIS B 1 198 ? 6.804   -4.840  -31.185 1.00 13.93 ? 200  HIS B NE2 1 
ATOM   3276 N N   . ALA B 1 199 ? 7.849   1.663   -29.847 1.00 20.46 ? 201  ALA B N   1 
ATOM   3277 C CA  . ALA B 1 199 ? 8.202   3.089   -29.949 1.00 23.35 ? 201  ALA B CA  1 
ATOM   3278 C C   . ALA B 1 199 ? 9.171   3.492   -28.831 1.00 24.48 ? 201  ALA B C   1 
ATOM   3279 O O   . ALA B 1 199 ? 10.156  4.212   -29.071 1.00 25.08 ? 201  ALA B O   1 
ATOM   3280 C CB  . ALA B 1 199 ? 6.943   3.921   -29.897 1.00 24.36 ? 201  ALA B CB  1 
ATOM   3281 N N   . ASP B 1 200 ? 8.917   3.018   -27.602 1.00 24.29 ? 202  ASP B N   1 
ATOM   3282 C CA  . ASP B 1 200 ? 9.787   3.327   -26.482 1.00 24.67 ? 202  ASP B CA  1 
ATOM   3283 C C   . ASP B 1 200 ? 11.163  2.608   -26.582 1.00 24.93 ? 202  ASP B C   1 
ATOM   3284 O O   . ASP B 1 200 ? 12.192  3.222   -26.274 1.00 26.76 ? 202  ASP B O   1 
ATOM   3285 C CB  . ASP B 1 200 ? 9.035   3.058   -25.164 1.00 26.39 ? 202  ASP B CB  1 
ATOM   3286 C CG  . ASP B 1 200 ? 7.950   4.092   -24.865 1.00 29.22 ? 202  ASP B CG  1 
ATOM   3287 O OD1 . ASP B 1 200 ? 8.006   5.199   -25.431 1.00 31.69 ? 202  ASP B OD1 1 
ATOM   3288 O OD2 . ASP B 1 200 ? 7.040   3.788   -24.083 1.00 29.49 ? 202  ASP B OD2 1 
ATOM   3289 N N   . THR B 1 201 ? 11.212  1.351   -27.035 1.00 21.70 ? 203  THR B N   1 
ATOM   3290 C CA  . THR B 1 201 ? 12.474  0.626   -27.269 1.00 21.11 ? 203  THR B CA  1 
ATOM   3291 C C   . THR B 1 201 ? 13.358  1.358   -28.297 1.00 21.83 ? 203  THR B C   1 
ATOM   3292 O O   . THR B 1 201 ? 14.573  1.224   -28.227 1.00 21.84 ? 203  THR B O   1 
ATOM   3293 C CB  . THR B 1 201 ? 12.185  -0.768  -27.786 1.00 24.25 ? 203  THR B CB  1 
ATOM   3294 O OG1 . THR B 1 201 ? 11.376  -1.409  -26.785 1.00 26.60 ? 203  THR B OG1 1 
ATOM   3295 C CG2 . THR B 1 201 ? 13.413  -1.569  -28.048 1.00 24.81 ? 203  THR B CG2 1 
ATOM   3296 N N   . ALA B 1 202 ? 12.759  2.124   -29.199 1.00 20.46 ? 204  ALA B N   1 
ATOM   3297 C CA  . ALA B 1 202 ? 13.548  2.797   -30.255 1.00 20.36 ? 204  ALA B CA  1 
ATOM   3298 C C   . ALA B 1 202 ? 14.466  3.896   -29.652 1.00 19.57 ? 204  ALA B C   1 
ATOM   3299 O O   . ALA B 1 202 ? 15.460  4.231   -30.290 1.00 17.93 ? 204  ALA B O   1 
ATOM   3300 C CB  . ALA B 1 202 ? 12.609  3.416   -31.278 1.00 21.25 ? 204  ALA B CB  1 
ATOM   3301 N N   . THR B 1 203 ? 14.148  4.450   -28.451 1.00 19.54 ? 205  THR B N   1 
ATOM   3302 C CA  . THR B 1 203 ? 14.900  5.592   -27.897 1.00 22.47 ? 205  THR B CA  1 
ATOM   3303 C C   . THR B 1 203 ? 15.185  5.497   -26.395 1.00 22.37 ? 205  THR B C   1 
ATOM   3304 O O   . THR B 1 203 ? 15.855  6.381   -25.893 1.00 20.73 ? 205  THR B O   1 
ATOM   3305 C CB  . THR B 1 203 ? 14.218  6.951   -28.189 1.00 26.01 ? 205  THR B CB  1 
ATOM   3306 O OG1 . THR B 1 203 ? 13.076  7.109   -27.364 1.00 29.40 ? 205  THR B OG1 1 
ATOM   3307 C CG2 . THR B 1 203 ? 13.789  7.131   -29.636 1.00 26.03 ? 205  THR B CG2 1 
ATOM   3308 N N   . LYS B 1 204 ? 14.703  4.458   -25.690 1.00 22.78 ? 206  LYS B N   1 
ATOM   3309 C CA  . LYS B 1 204 ? 14.835  4.381   -24.219 1.00 26.27 ? 206  LYS B CA  1 
ATOM   3310 C C   . LYS B 1 204 ? 15.362  3.044   -23.834 1.00 27.66 ? 206  LYS B C   1 
ATOM   3311 O O   . LYS B 1 204 ? 14.906  2.081   -24.459 1.00 30.84 ? 206  LYS B O   1 
ATOM   3312 C CB  . LYS B 1 204 ? 13.494  4.641   -23.505 1.00 29.80 ? 206  LYS B CB  1 
ATOM   3313 C CG  . LYS B 1 204 ? 12.759  5.840   -24.016 1.00 36.19 ? 206  LYS B CG  1 
ATOM   3314 C CD  . LYS B 1 204 ? 11.492  6.143   -23.284 1.00 42.87 ? 206  LYS B CD  1 
ATOM   3315 C CE  . LYS B 1 204 ? 10.900  7.450   -23.774 1.00 47.10 ? 206  LYS B CE  1 
ATOM   3316 N NZ  . LYS B 1 204 ? 9.457   7.549   -23.435 1.00 50.93 ? 206  LYS B NZ  1 
ATOM   3317 N N   . THR B 1 209 ? 12.069  -2.448  -15.190 1.00 38.51 ? 211  THR B N   1 
ATOM   3318 C CA  . THR B 1 209 ? 11.615  -2.131  -13.838 1.00 39.61 ? 211  THR B CA  1 
ATOM   3319 C C   . THR B 1 209 ? 10.654  -0.941  -13.847 1.00 39.84 ? 211  THR B C   1 
ATOM   3320 O O   . THR B 1 209 ? 9.639   -0.975  -13.150 1.00 39.38 ? 211  THR B O   1 
ATOM   3321 C CB  . THR B 1 209 ? 12.810  -1.937  -12.908 1.00 42.74 ? 211  THR B CB  1 
ATOM   3322 O OG1 . THR B 1 209 ? 12.330  -1.623  -11.583 1.00 44.40 ? 211  THR B OG1 1 
ATOM   3323 C CG2 . THR B 1 209 ? 13.770  -0.855  -13.395 1.00 43.64 ? 211  THR B CG2 1 
ATOM   3324 N N   . LYS B 1 210 ? 10.978  0.116   -14.641 1.00 39.45 ? 212  LYS B N   1 
ATOM   3325 C CA  . LYS B 1 210 ? 10.112  1.272   -14.829 1.00 39.51 ? 212  LYS B CA  1 
ATOM   3326 C C   . LYS B 1 210 ? 9.163   1.169   -16.048 1.00 38.37 ? 212  LYS B C   1 
ATOM   3327 O O   . LYS B 1 210 ? 8.466   2.137   -16.349 1.00 40.01 ? 212  LYS B O   1 
ATOM   3328 C CB  . LYS B 1 210 ? 10.953  2.558   -14.931 1.00 43.36 ? 212  LYS B CB  1 
ATOM   3329 C CG  . LYS B 1 210 ? 11.699  2.787   -16.239 1.00 49.79 ? 212  LYS B CG  1 
ATOM   3330 C CD  . LYS B 1 210 ? 12.718  3.915   -16.030 1.00 55.43 ? 212  LYS B CD  1 
ATOM   3331 C CE  . LYS B 1 210 ? 13.096  4.646   -17.307 1.00 61.37 ? 212  LYS B CE  1 
ATOM   3332 N NZ  . LYS B 1 210 ? 13.930  5.854   -17.018 1.00 64.63 ? 212  LYS B NZ  1 
ATOM   3333 N N   . ASN B 1 211 ? 9.138   0.017   -16.725 1.00 34.17 ? 213  ASN B N   1 
ATOM   3334 C CA  . ASN B 1 211 ? 8.300   -0.264  -17.909 1.00 31.24 ? 213  ASN B CA  1 
ATOM   3335 C C   . ASN B 1 211 ? 6.821   0.005   -17.726 1.00 29.54 ? 213  ASN B C   1 
ATOM   3336 O O   . ASN B 1 211 ? 6.313   0.112   -16.588 1.00 29.94 ? 213  ASN B O   1 
ATOM   3337 C CB  . ASN B 1 211 ? 8.518   -1.735  -18.326 1.00 29.78 ? 213  ASN B CB  1 
ATOM   3338 C CG  . ASN B 1 211 ? 9.833   -2.077  -19.003 1.00 32.87 ? 213  ASN B CG  1 
ATOM   3339 O OD1 . ASN B 1 211 ? 10.085  -3.228  -19.337 1.00 34.25 ? 213  ASN B OD1 1 
ATOM   3340 N ND2 . ASN B 1 211 ? 10.753  -1.133  -19.246 1.00 35.66 ? 213  ASN B ND2 1 
ATOM   3341 N N   . ARG B 1 212 ? 6.112   0.089   -18.875 1.00 26.83 ? 214  ARG B N   1 
ATOM   3342 C CA  . ARG B 1 212 ? 4.681   0.451   -18.944 1.00 27.37 ? 214  ARG B CA  1 
ATOM   3343 C C   . ARG B 1 212 ? 3.761   -0.492  -18.125 1.00 25.72 ? 214  ARG B C   1 
ATOM   3344 O O   . ARG B 1 212 ? 2.895   -0.045  -17.349 1.00 26.51 ? 214  ARG B O   1 
ATOM   3345 C CB  . ARG B 1 212 ? 4.275   0.381   -20.417 1.00 30.82 ? 214  ARG B CB  1 
ATOM   3346 C CG  . ARG B 1 212 ? 2.836   0.668   -20.782 1.00 36.89 ? 214  ARG B CG  1 
ATOM   3347 C CD  . ARG B 1 212 ? 2.687   0.434   -22.261 1.00 41.12 ? 214  ARG B CD  1 
ATOM   3348 N NE  . ARG B 1 212 ? 3.226   1.540   -23.068 1.00 45.42 ? 214  ARG B NE  1 
ATOM   3349 C CZ  . ARG B 1 212 ? 2.526   2.386   -23.844 1.00 45.03 ? 214  ARG B CZ  1 
ATOM   3350 N NH1 . ARG B 1 212 ? 3.146   3.338   -24.525 1.00 42.58 ? 214  ARG B NH1 1 
ATOM   3351 N NH2 . ARG B 1 212 ? 1.201   2.282   -23.941 1.00 45.55 ? 214  ARG B NH2 1 
ATOM   3352 N N   . PHE B 1 213 ? 3.962   -1.792  -18.319 1.00 20.54 ? 215  PHE B N   1 
ATOM   3353 C CA  . PHE B 1 213 ? 3.387   -2.798  -17.414 1.00 20.03 ? 215  PHE B CA  1 
ATOM   3354 C C   . PHE B 1 213 ? 4.528   -3.677  -16.852 1.00 18.06 ? 215  PHE B C   1 
ATOM   3355 O O   . PHE B 1 213 ? 5.502   -3.965  -17.514 1.00 17.79 ? 215  PHE B O   1 
ATOM   3356 C CB  . PHE B 1 213 ? 2.404   -3.688  -18.172 1.00 19.99 ? 215  PHE B CB  1 
ATOM   3357 C CG  . PHE B 1 213 ? 1.388   -2.982  -19.025 1.00 22.77 ? 215  PHE B CG  1 
ATOM   3358 C CD1 . PHE B 1 213 ? 0.246   -2.445  -18.465 1.00 26.20 ? 215  PHE B CD1 1 
ATOM   3359 C CD2 . PHE B 1 213 ? 1.548   -2.898  -20.396 1.00 24.25 ? 215  PHE B CD2 1 
ATOM   3360 C CE1 . PHE B 1 213 ? -0.704  -1.807  -19.271 1.00 27.24 ? 215  PHE B CE1 1 
ATOM   3361 C CE2 . PHE B 1 213 ? 0.582   -2.290  -21.195 1.00 25.25 ? 215  PHE B CE2 1 
ATOM   3362 C CZ  . PHE B 1 213 ? -0.527  -1.740  -20.627 1.00 26.00 ? 215  PHE B CZ  1 
ATOM   3363 N N   . VAL B 1 214 ? 4.393   -4.108  -15.615 1.00 18.89 ? 216  VAL B N   1 
ATOM   3364 C CA  . VAL B 1 214 ? 5.284   -5.057  -14.986 1.00 18.12 ? 216  VAL B CA  1 
ATOM   3365 C C   . VAL B 1 214 ? 4.435   -6.119  -14.307 1.00 16.58 ? 216  VAL B C   1 
ATOM   3366 O O   . VAL B 1 214 ? 3.361   -5.793  -13.774 1.00 17.85 ? 216  VAL B O   1 
ATOM   3367 C CB  . VAL B 1 214 ? 6.264   -4.393  -13.989 1.00 20.26 ? 216  VAL B CB  1 
ATOM   3368 C CG1 . VAL B 1 214 ? 7.165   -3.362  -14.683 1.00 21.24 ? 216  VAL B CG1 1 
ATOM   3369 C CG2 . VAL B 1 214 ? 5.537   -3.791  -12.816 1.00 23.95 ? 216  VAL B CG2 1 
ATOM   3370 N N   . VAL B 1 215 ? 4.893   -7.362  -14.322 1.00 15.14 ? 217  VAL B N   1 
ATOM   3371 C CA  . VAL B 1 215 ? 4.285   -8.474  -13.599 1.00 14.97 ? 217  VAL B CA  1 
ATOM   3372 C C   . VAL B 1 215 ? 5.340   -9.359  -12.984 1.00 14.97 ? 217  VAL B C   1 
ATOM   3373 O O   . VAL B 1 215 ? 4.958   -10.240 -12.162 1.00 16.19 ? 217  VAL B O   1 
ATOM   3374 C CB  . VAL B 1 215 ? 3.332   -9.350  -14.453 1.00 14.96 ? 217  VAL B CB  1 
ATOM   3375 C CG1 . VAL B 1 215 ? 2.169   -8.516  -14.974 1.00 15.93 ? 217  VAL B CG1 1 
ATOM   3376 C CG2 . VAL B 1 215 ? 4.093   -10.040 -15.598 1.00 14.39 ? 217  VAL B CG2 1 
ATOM   3377 O OXT . VAL B 1 215 ? 6.509   -9.188  -13.346 1.00 13.76 ? 217  VAL B OXT 1 
HETATM 3378 C C1  . PEG C 2 .   ? -1.804  -14.882 15.183  0.50 18.90 ? 401  PEG A C1  1 
HETATM 3379 O O1  . PEG C 2 .   ? -2.049  -15.244 13.827  0.50 18.95 ? 401  PEG A O1  1 
HETATM 3380 C C2  . PEG C 2 .   ? -0.882  -13.723 15.372  0.50 18.87 ? 401  PEG A C2  1 
HETATM 3381 O O2  . PEG C 2 .   ? 0.241   -13.833 14.510  0.50 17.83 ? 401  PEG A O2  1 
HETATM 3382 C C3  . PEG C 2 .   ? 1.492   -13.663 15.131  0.50 15.24 ? 401  PEG A C3  1 
HETATM 3383 C C4  . PEG C 2 .   ? 2.591   -13.925 14.136  0.50 13.52 ? 401  PEG A C4  1 
HETATM 3384 O O4  . PEG C 2 .   ? 2.569   -13.057 12.990  0.50 10.18 ? 401  PEG A O4  1 
HETATM 3385 C C1  . PEG D 2 .   ? -8.970  -2.431  0.602   1.00 46.84 ? 402  PEG A C1  1 
HETATM 3386 O O1  . PEG D 2 .   ? -8.343  -1.714  -0.470  1.00 47.71 ? 402  PEG A O1  1 
HETATM 3387 C C2  . PEG D 2 .   ? -9.261  -1.549  1.750   1.00 45.43 ? 402  PEG A C2  1 
HETATM 3388 O O2  . PEG D 2 .   ? -9.450  -2.318  2.924   1.00 44.11 ? 402  PEG A O2  1 
HETATM 3389 C C3  . PEG D 2 .   ? -8.468  -1.985  3.898   1.00 43.49 ? 402  PEG A C3  1 
HETATM 3390 C C4  . PEG D 2 .   ? -9.021  -2.083  5.270   1.00 43.51 ? 402  PEG A C4  1 
HETATM 3391 O O4  . PEG D 2 .   ? -7.991  -2.291  6.254   1.00 43.61 ? 402  PEG A O4  1 
HETATM 3392 C C1  . PEG E 2 .   ? -11.527 -10.515 -12.065 1.00 70.16 ? 403  PEG A C1  1 
HETATM 3393 O O1  . PEG E 2 .   ? -12.725 -10.294 -12.793 1.00 70.19 ? 403  PEG A O1  1 
HETATM 3394 C C2  . PEG E 2 .   ? -11.682 -11.628 -11.069 1.00 70.29 ? 403  PEG A C2  1 
HETATM 3395 O O2  . PEG E 2 .   ? -10.457 -11.864 -10.384 1.00 70.26 ? 403  PEG A O2  1 
HETATM 3396 C C3  . PEG E 2 .   ? -10.244 -10.975 -9.298  1.00 70.15 ? 403  PEG A C3  1 
HETATM 3397 C C4  . PEG E 2 .   ? -8.899  -10.338 -9.412  1.00 70.16 ? 403  PEG A C4  1 
HETATM 3398 O O4  . PEG E 2 .   ? -8.560  -9.615  -8.242  1.00 70.01 ? 403  PEG A O4  1 
HETATM 3399 C C1  . PGE F 3 .   ? 4.240   -27.941 -8.502  1.00 47.29 ? 404  PGE A C1  1 
HETATM 3400 O O1  . PGE F 3 .   ? 5.124   -29.065 -8.486  1.00 47.67 ? 404  PGE A O1  1 
HETATM 3401 C C2  . PGE F 3 .   ? 4.955   -26.667 -8.239  1.00 46.71 ? 404  PGE A C2  1 
HETATM 3402 O O2  . PGE F 3 .   ? 4.930   -26.345 -6.855  1.00 46.78 ? 404  PGE A O2  1 
HETATM 3403 C C3  . PGE F 3 .   ? 5.808   -27.126 -6.037  1.00 45.81 ? 404  PGE A C3  1 
HETATM 3404 C C4  . PGE F 3 .   ? 5.420   -26.979 -4.601  1.00 44.77 ? 404  PGE A C4  1 
HETATM 3405 O O4  . PGE F 3 .   ? 6.142   -30.208 -1.981  1.00 45.77 ? 404  PGE A O4  1 
HETATM 3406 C C6  . PGE F 3 .   ? 5.035   -29.297 -1.922  1.00 44.56 ? 404  PGE A C6  1 
HETATM 3407 C C5  . PGE F 3 .   ? 5.431   -27.975 -2.471  1.00 44.00 ? 404  PGE A C5  1 
HETATM 3408 O O3  . PGE F 3 .   ? 5.805   -28.108 -3.825  1.00 43.86 ? 404  PGE A O3  1 
HETATM 3409 C C1  . PEG G 2 .   ? -11.656 -24.473 17.339  1.00 46.47 ? 405  PEG A C1  1 
HETATM 3410 O O1  . PEG G 2 .   ? -12.582 -23.795 18.177  1.00 46.59 ? 405  PEG A O1  1 
HETATM 3411 C C2  . PEG G 2 .   ? -12.233 -25.698 16.718  1.00 46.22 ? 405  PEG A C2  1 
HETATM 3412 O O2  . PEG G 2 .   ? -11.376 -26.171 15.687  1.00 46.48 ? 405  PEG A O2  1 
HETATM 3413 C C3  . PEG G 2 .   ? -10.238 -26.912 16.127  1.00 45.97 ? 405  PEG A C3  1 
HETATM 3414 C C4  . PEG G 2 .   ? -10.595 -28.338 16.379  1.00 45.38 ? 405  PEG A C4  1 
HETATM 3415 O O4  . PEG G 2 .   ? -10.863 -29.054 15.179  1.00 44.82 ? 405  PEG A O4  1 
HETATM 3416 C C1  . W4K H 4 .   ? -16.216 -17.062 -1.069  1.00 21.42 ? 406  W4K A C1  1 
HETATM 3417 C C2  . W4K H 4 .   ? -16.066 -16.744 0.333   1.00 18.72 ? 406  W4K A C2  1 
HETATM 3418 C C3  . W4K H 4 .   ? -15.074 -17.655 1.036   1.00 15.70 ? 406  W4K A C3  1 
HETATM 3419 C C5  . W4K H 4 .   ? -14.643 -18.438 3.314   1.00 16.80 ? 406  W4K A C5  1 
HETATM 3420 C C6  . W4K H 4 .   ? -15.363 -19.771 3.254   1.00 18.60 ? 406  W4K A C6  1 
HETATM 3421 C C7  . W4K H 4 .   ? -14.583 -17.848 4.730   1.00 16.72 ? 406  W4K A C7  1 
HETATM 3422 C C10 . W4K H 4 .   ? -12.955 -18.099 -0.256  1.00 12.70 ? 406  W4K A C10 1 
HETATM 3423 C C11 . W4K H 4 .   ? -11.682 -17.767 -0.691  1.00 11.72 ? 406  W4K A C11 1 
HETATM 3424 C C12 . W4K H 4 .   ? -11.060 -16.596 -0.266  1.00 11.34 ? 406  W4K A C12 1 
HETATM 3425 C C13 . W4K H 4 .   ? -11.768 -15.770 0.600   1.00 12.33 ? 406  W4K A C13 1 
HETATM 3426 C C14 . W4K H 4 .   ? -13.062 -16.053 1.008   1.00 14.30 ? 406  W4K A C14 1 
HETATM 3427 C C16 . W4K H 4 .   ? -13.287 -13.895 2.279   1.00 18.61 ? 406  W4K A C16 1 
HETATM 3428 C C19 . W4K H 4 .   ? -9.696  -16.227 -0.744  1.00 12.30 ? 406  W4K A C19 1 
HETATM 3429 C C21 . W4K H 4 .   ? -8.217  -14.555 -1.676  1.00 13.23 ? 406  W4K A C21 1 
HETATM 3430 C C22 . W4K H 4 .   ? -7.192  -15.480 -1.743  1.00 12.66 ? 406  W4K A C22 1 
HETATM 3431 C C23 . W4K H 4 .   ? -7.412  -16.759 -1.325  1.00 11.37 ? 406  W4K A C23 1 
HETATM 3432 C C24 . W4K H 4 .   ? -8.643  -17.122 -0.843  1.00 11.19 ? 406  W4K A C24 1 
HETATM 3433 O O4  . W4K H 4 .   ? -15.328 -17.506 2.475   1.00 14.50 ? 406  W4K A O4  1 
HETATM 3434 O O8  . W4K H 4 .   ? -14.002 -16.541 4.712   1.00 19.17 ? 406  W4K A O8  1 
HETATM 3435 C C9  . W4K H 4 .   ? -13.653 -17.285 0.635   1.00 14.06 ? 406  W4K A C9  1 
HETATM 3436 N N15 . W4K H 4 .   ? -13.745 -15.211 1.858   1.00 16.63 ? 406  W4K A N15 1 
HETATM 3437 C C17 . W4K H 4 .   ? -14.297 -13.230 3.210   1.00 21.49 ? 406  W4K A C17 1 
HETATM 3438 O O18 . W4K H 4 .   ? -14.342 -13.889 4.475   1.00 26.08 ? 406  W4K A O18 1 
HETATM 3439 C C20 . W4K H 4 .   ? -9.457  -14.928 -1.188  1.00 12.77 ? 406  W4K A C20 1 
HETATM 3440 F F25 . W4K H 4 .   ? -8.853  -18.394 -0.449  1.00 13.22 ? 406  W4K A F25 1 
HETATM 3441 H H30 . W4K H 4 .   ? -16.147 -16.247 -1.597  1.00 21.41 ? 406  W4K A H30 1 
HETATM 3442 H H29 . W4K H 4 .   ? -17.093 -17.473 -1.219  1.00 21.47 ? 406  W4K A H29 1 
HETATM 3443 H H28 . W4K H 4 .   ? -15.512 -17.687 -1.342  1.00 21.41 ? 406  W4K A H28 1 
HETATM 3444 H H32 . W4K H 4 .   ? -16.945 -16.823 0.776   1.00 18.70 ? 406  W4K A H32 1 
HETATM 3445 H H31 . W4K H 4 .   ? -15.763 -15.815 0.419   1.00 18.65 ? 406  W4K A H31 1 
HETATM 3446 H H26 . W4K H 4 .   ? -15.253 -18.589 0.770   1.00 15.70 ? 406  W4K A H26 1 
HETATM 3447 H H27 . W4K H 4 .   ? -13.720 -18.557 2.982   1.00 16.82 ? 406  W4K A H27 1 
HETATM 3448 H H35 . W4K H 4 .   ? -16.330 -19.621 3.297   1.00 18.66 ? 406  W4K A H35 1 
HETATM 3449 H H34 . W4K H 4 .   ? -15.086 -20.325 4.010   1.00 18.58 ? 406  W4K A H34 1 
HETATM 3450 H H33 . W4K H 4 .   ? -15.140 -20.225 2.417   1.00 18.58 ? 406  W4K A H33 1 
HETATM 3451 H H37 . W4K H 4 .   ? -14.049 -18.434 5.302   1.00 16.75 ? 406  W4K A H37 1 
HETATM 3452 H H36 . W4K H 4 .   ? -15.492 -17.800 5.104   1.00 16.75 ? 406  W4K A H36 1 
HETATM 3453 H H39 . W4K H 4 .   ? -13.351 -18.918 -0.549  1.00 12.72 ? 406  W4K A H39 1 
HETATM 3454 H H40 . W4K H 4 .   ? -11.212 -18.367 -1.267  1.00 11.69 ? 406  W4K A H40 1 
HETATM 3455 H H41 . W4K H 4 .   ? -11.371 -14.946 0.871   1.00 12.43 ? 406  W4K A H41 1 
HETATM 3456 H H44 . W4K H 4 .   ? -13.151 -13.327 1.486   1.00 18.56 ? 406  W4K A H44 1 
HETATM 3457 H H43 . W4K H 4 .   ? -12.425 -13.984 2.744   1.00 18.60 ? 406  W4K A H43 1 
HETATM 3458 H H49 . W4K H 4 .   ? -8.068  -13.656 -1.961  1.00 13.18 ? 406  W4K A H49 1 
HETATM 3459 H H50 . W4K H 4 .   ? -6.335  -15.222 -2.069  1.00 12.69 ? 406  W4K A H50 1 
HETATM 3460 H H51 . W4K H 4 .   ? -6.709  -17.405 -1.371  1.00 11.40 ? 406  W4K A H51 1 
HETATM 3461 H H38 . W4K H 4 .   ? -14.539 -15.984 5.099   1.00 19.19 ? 406  W4K A H38 1 
HETATM 3462 H H42 . W4K H 4 .   ? -14.310 -15.600 2.402   1.00 16.59 ? 406  W4K A H42 1 
HETATM 3463 H H46 . W4K H 4 .   ? -15.194 -13.252 2.794   1.00 21.35 ? 406  W4K A H46 1 
HETATM 3464 H H45 . W4K H 4 .   ? -14.046 -12.289 3.343   1.00 21.54 ? 406  W4K A H45 1 
HETATM 3465 H H47 . W4K H 4 .   ? -13.599 -14.306 4.604   1.00 26.11 ? 406  W4K A H47 1 
HETATM 3466 H H48 . W4K H 4 .   ? -10.160 -14.284 -1.150  1.00 12.79 ? 406  W4K A H48 1 
HETATM 3467 S S   . DMS I 5 .   ? -6.658  -40.308 -41.462 1.00 43.95 ? 301  DMS B S   1 
HETATM 3468 O O   . DMS I 5 .   ? -6.755  -38.864 -41.025 1.00 43.44 ? 301  DMS B O   1 
HETATM 3469 C C1  . DMS I 5 .   ? -7.680  -41.228 -40.334 1.00 43.48 ? 301  DMS B C1  1 
HETATM 3470 C C2  . DMS I 5 .   ? -7.683  -40.450 -42.907 1.00 43.46 ? 301  DMS B C2  1 
HETATM 3471 S S   . DMS J 5 .   ? -0.132  -37.040 -27.360 1.00 74.56 ? 302  DMS B S   1 
HETATM 3472 O O   . DMS J 5 .   ? -0.327  -35.910 -26.384 1.00 74.51 ? 302  DMS B O   1 
HETATM 3473 C C1  . DMS J 5 .   ? 0.207   -38.479 -26.375 1.00 74.70 ? 302  DMS B C1  1 
HETATM 3474 C C2  . DMS J 5 .   ? -1.758  -37.493 -27.910 1.00 74.28 ? 302  DMS B C2  1 
HETATM 3475 S S   . DMS K 5 .   ? -2.668  -11.074 -35.255 1.00 47.36 ? 303  DMS B S   1 
HETATM 3476 O O   . DMS K 5 .   ? -2.158  -11.269 -36.654 1.00 46.87 ? 303  DMS B O   1 
HETATM 3477 C C1  . DMS K 5 .   ? -1.413  -10.177 -34.375 1.00 46.42 ? 303  DMS B C1  1 
HETATM 3478 C C2  . DMS K 5 .   ? -3.874  -9.772  -35.347 1.00 47.76 ? 303  DMS B C2  1 
HETATM 3479 C C1  . PEG L 2 .   ? 5.708   -23.540 -14.575 1.00 53.94 ? 304  PEG B C1  1 
HETATM 3480 O O1  . PEG L 2 .   ? 4.389   -23.388 -15.082 1.00 53.91 ? 304  PEG B O1  1 
HETATM 3481 C C2  . PEG L 2 .   ? 6.601   -24.231 -15.540 1.00 53.95 ? 304  PEG B C2  1 
HETATM 3482 O O2  . PEG L 2 .   ? 7.937   -24.205 -15.062 1.00 54.03 ? 304  PEG B O2  1 
HETATM 3483 C C3  . PEG L 2 .   ? 8.884   -23.776 -16.031 1.00 53.66 ? 304  PEG B C3  1 
HETATM 3484 C C4  . PEG L 2 .   ? 9.233   -24.891 -16.969 1.00 53.28 ? 304  PEG B C4  1 
HETATM 3485 O O4  . PEG L 2 .   ? 10.435  -24.607 -17.680 1.00 52.73 ? 304  PEG B O4  1 
HETATM 3486 C C1  . PEG M 2 .   ? 13.533  -10.795 -16.209 1.00 42.80 ? 305  PEG B C1  1 
HETATM 3487 O O1  . PEG M 2 .   ? 14.226  -10.047 -17.204 1.00 43.05 ? 305  PEG B O1  1 
HETATM 3488 C C2  . PEG M 2 .   ? 13.841  -12.242 -16.296 1.00 43.13 ? 305  PEG B C2  1 
HETATM 3489 O O2  . PEG M 2 .   ? 15.162  -12.492 -15.823 1.00 43.91 ? 305  PEG B O2  1 
HETATM 3490 C C3  . PEG M 2 .   ? 15.533  -13.864 -15.917 1.00 43.77 ? 305  PEG B C3  1 
HETATM 3491 C C4  . PEG M 2 .   ? 14.959  -14.633 -14.770 1.00 43.92 ? 305  PEG B C4  1 
HETATM 3492 O O4  . PEG M 2 .   ? 15.836  -15.631 -14.280 1.00 44.17 ? 305  PEG B O4  1 
HETATM 3493 C C1  . W4K N 4 .   ? 20.691  -22.212 -31.912 1.00 23.55 ? 306  W4K B C1  1 
HETATM 3494 C C2  . W4K N 4 .   ? 19.289  -22.563 -32.147 1.00 20.47 ? 306  W4K B C2  1 
HETATM 3495 C C3  . W4K N 4 .   ? 18.309  -21.678 -31.378 1.00 16.33 ? 306  W4K B C3  1 
HETATM 3496 C C5  . W4K N 4 .   ? 17.903  -20.857 -29.112 1.00 14.67 ? 306  W4K B C5  1 
HETATM 3497 C C6  . W4K N 4 .   ? 18.603  -19.513 -29.181 1.00 15.81 ? 306  W4K B C6  1 
HETATM 3498 C C7  . W4K N 4 .   ? 17.886  -21.421 -27.688 1.00 16.88 ? 306  W4K B C7  1 
HETATM 3499 C C10 . W4K N 4 .   ? 16.196  -21.278 -32.636 1.00 13.49 ? 306  W4K B C10 1 
HETATM 3500 C C11 . W4K N 4 .   ? 14.929  -21.610 -33.054 1.00 13.71 ? 306  W4K B C11 1 
HETATM 3501 C C12 . W4K N 4 .   ? 14.296  -22.767 -32.600 1.00 12.54 ? 306  W4K B C12 1 
HETATM 3502 C C13 . W4K N 4 .   ? 14.998  -23.602 -31.732 1.00 14.35 ? 306  W4K B C13 1 
HETATM 3503 C C14 . W4K N 4 .   ? 16.294  -23.304 -31.322 1.00 15.19 ? 306  W4K B C14 1 
HETATM 3504 C C16 . W4K N 4 .   ? 16.437  -25.419 -30.058 1.00 17.92 ? 306  W4K B C16 1 
HETATM 3505 C C19 . W4K N 4 .   ? 12.940  -23.132 -33.092 1.00 13.31 ? 306  W4K B C19 1 
HETATM 3506 C C21 . W4K N 4 .   ? 11.492  -24.809 -34.053 1.00 12.27 ? 306  W4K B C21 1 
HETATM 3507 C C22 . W4K N 4 .   ? 10.462  -23.883 -34.137 1.00 12.21 ? 306  W4K B C22 1 
HETATM 3508 C C23 . W4K N 4 .   ? 10.673  -22.602 -33.704 1.00 11.09 ? 306  W4K B C23 1 
HETATM 3509 C C24 . W4K N 4 .   ? 11.897  -22.233 -33.204 1.00 11.90 ? 306  W4K B C24 1 
HETATM 3510 O O4  . W4K N 4 .   ? 18.573  -21.827 -29.970 1.00 14.61 ? 306  W4K B O4  1 
HETATM 3511 O O8  . W4K N 4 .   ? 17.265  -22.702 -27.624 1.00 17.95 ? 306  W4K B O8  1 
HETATM 3512 C C9  . W4K N 4 .   ? 16.895  -22.086 -31.749 1.00 14.25 ? 306  W4K B C9  1 
HETATM 3513 N N15 . W4K N 4 .   ? 16.942  -24.119 -30.455 1.00 16.38 ? 306  W4K B N15 1 
HETATM 3514 C C17 . W4K N 4 .   ? 17.330  -26.088 -29.042 1.00 20.69 ? 306  W4K B C17 1 
HETATM 3515 O O18 . W4K N 4 .   ? 18.592  -26.389 -29.633 1.00 24.11 ? 306  W4K B O18 1 
HETATM 3516 C C20 . W4K N 4 .   ? 12.709  -24.437 -33.531 1.00 13.30 ? 306  W4K B C20 1 
HETATM 3517 F F25 . W4K N 4 .   ? 12.106  -20.969 -32.771 1.00 14.59 ? 306  W4K B F25 1 
HETATM 3518 H H30 . W4K N 4 .   ? 20.792  -21.236 -31.918 1.00 23.54 ? 306  W4K B H30 1 
HETATM 3519 H H29 . W4K N 4 .   ? 21.250  -22.602 -32.617 1.00 23.56 ? 306  W4K B H29 1 
HETATM 3520 H H28 . W4K N 4 .   ? 20.972  -22.562 -31.044 1.00 23.59 ? 306  W4K B H28 1 
HETATM 3521 H H32 . W4K N 4 .   ? 19.146  -23.499 -31.886 1.00 20.42 ? 306  W4K B H32 1 
HETATM 3522 H H31 . W4K N 4 .   ? 19.099  -22.485 -33.112 1.00 20.41 ? 306  W4K B H31 1 
HETATM 3523 H H26 . W4K N 4 .   ? 18.455  -20.737 -31.638 1.00 16.33 ? 306  W4K B H26 1 
HETATM 3524 H H27 . W4K N 4 .   ? 16.973  -20.743 -29.417 1.00 14.66 ? 306  W4K B H27 1 
HETATM 3525 H H35 . W4K N 4 .   ? 18.590  -19.185 -30.103 1.00 15.79 ? 306  W4K B H35 1 
HETATM 3526 H H34 . W4K N 4 .   ? 19.531  -19.613 -28.884 1.00 15.82 ? 306  W4K B H34 1 
HETATM 3527 H H33 . W4K N 4 .   ? 18.142  -18.876 -28.602 1.00 15.78 ? 306  W4K B H33 1 
HETATM 3528 H H37 . W4K N 4 .   ? 17.400  -20.800 -27.103 1.00 16.91 ? 306  W4K B H37 1 
HETATM 3529 H H36 . W4K N 4 .   ? 18.812  -21.491 -27.356 1.00 16.88 ? 306  W4K B H36 1 
HETATM 3530 H H39 . W4K N 4 .   ? 16.600  -20.475 -32.957 1.00 13.55 ? 306  W4K B H39 1 
HETATM 3531 H H40 . W4K N 4 .   ? 14.467  -21.025 -33.651 1.00 13.72 ? 306  W4K B H40 1 
HETATM 3532 H H41 . W4K N 4 .   ? 14.586  -24.408 -31.429 1.00 14.35 ? 306  W4K B H41 1 
HETATM 3533 H H44 . W4K N 4 .   ? 16.364  -25.994 -30.854 1.00 17.91 ? 306  W4K B H44 1 
HETATM 3534 H H43 . W4K N 4 .   ? 15.536  -25.312 -29.676 1.00 17.95 ? 306  W4K B H43 1 
HETATM 3535 H H49 . W4K N 4 .   ? 11.352  -25.706 -34.348 1.00 12.21 ? 306  W4K B H49 1 
HETATM 3536 H H50 . W4K N 4 .   ? 9.608   -24.144 -34.473 1.00 12.12 ? 306  W4K B H50 1 
HETATM 3537 H H51 . W4K N 4 .   ? 9.966   -21.960 -33.753 1.00 11.11 ? 306  W4K B H51 1 
HETATM 3538 H H38 . W4K N 4 .   ? 17.719  -23.209 -27.100 1.00 17.95 ? 306  W4K B H38 1 
HETATM 3539 H H42 . W4K N 4 .   ? 17.455  -23.711 -29.872 1.00 16.35 ? 306  W4K B H42 1 
HETATM 3540 H H46 . W4K N 4 .   ? 16.907  -26.916 -28.728 1.00 20.71 ? 306  W4K B H46 1 
HETATM 3541 H H45 . W4K N 4 .   ? 17.458  -25.489 -28.263 1.00 20.58 ? 306  W4K B H45 1 
HETATM 3542 H H47 . W4K N 4 .   ? 19.158  -25.747 -29.435 1.00 24.09 ? 306  W4K B H47 1 
HETATM 3543 H H48 . W4K N 4 .   ? 13.419  -25.072 -33.497 1.00 13.39 ? 306  W4K B H48 1 
HETATM 3544 O O   . HOH O 6 .   ? -3.027  -42.204 16.633  1.00 36.23 ? 901  HOH A O   1 
HETATM 3545 O O   . HOH O 6 .   ? 10.502  -11.281 6.787   1.00 45.93 ? 902  HOH A O   1 
HETATM 3546 O O   . HOH O 6 .   ? 7.214   -45.931 6.510   1.00 38.45 ? 903  HOH A O   1 
HETATM 3547 O O   . HOH O 6 .   ? 3.377   -17.349 15.486  1.00 34.05 ? 904  HOH A O   1 
HETATM 3548 O O   . HOH O 6 .   ? 7.501   -37.263 -0.414  1.00 31.93 ? 905  HOH A O   1 
HETATM 3549 O O   . HOH O 6 .   ? -11.718 -28.048 -14.562 1.00 43.60 ? 906  HOH A O   1 
HETATM 3550 O O   . HOH O 6 .   ? 13.882  -20.498 5.070   1.00 39.22 ? 907  HOH A O   1 
HETATM 3551 O O   . HOH O 6 .   ? -3.309  -40.833 9.003   1.00 23.18 ? 908  HOH A O   1 
HETATM 3552 O O   . HOH O 6 .   ? -18.156 -24.997 -10.123 1.00 51.12 ? 909  HOH A O   1 
HETATM 3553 O O   . HOH O 6 .   ? -18.840 -31.301 8.190   1.00 39.75 ? 910  HOH A O   1 
HETATM 3554 O O   . HOH O 6 .   ? 14.031  -31.108 9.936   1.00 30.08 ? 911  HOH A O   1 
HETATM 3555 O O   . HOH O 6 .   ? -0.429  -31.080 -11.228 1.00 51.55 ? 912  HOH A O   1 
HETATM 3556 O O   . HOH O 6 .   ? -8.438  -32.098 13.842  1.00 23.63 ? 913  HOH A O   1 
HETATM 3557 O O   . HOH O 6 .   ? 13.513  0.054   -6.587  1.00 27.55 ? 914  HOH A O   1 
HETATM 3558 O O   . HOH O 6 .   ? -2.982  -3.826  -0.978  1.00 45.45 ? 915  HOH A O   1 
HETATM 3559 O O   . HOH O 6 .   ? -5.470  -12.521 -8.507  1.00 32.34 ? 916  HOH A O   1 
HETATM 3560 O O   . HOH O 6 .   ? 3.098   -0.874  1.425   1.00 33.22 ? 917  HOH A O   1 
HETATM 3561 O O   . HOH O 6 .   ? 0.097   -29.356 22.150  1.00 29.22 ? 918  HOH A O   1 
HETATM 3562 O O   . HOH O 6 .   ? -10.545 -5.895  -5.279  1.00 27.71 ? 919  HOH A O   1 
HETATM 3563 O O   . HOH O 6 .   ? 14.054  -15.438 5.223   1.00 27.51 ? 920  HOH A O   1 
HETATM 3564 O O   . HOH O 6 .   ? 10.083  -23.522 -2.138  0.50 27.52 ? 921  HOH A O   1 
HETATM 3565 O O   . HOH O 6 .   ? -19.335 -14.192 -0.426  1.00 47.86 ? 922  HOH A O   1 
HETATM 3566 O O   . HOH O 6 .   ? 3.270   -12.537 -12.001 1.00 15.83 ? 923  HOH A O   1 
HETATM 3567 O O   . HOH O 6 .   ? -25.463 -25.546 9.503   1.00 44.11 ? 924  HOH A O   1 
HETATM 3568 O O   . HOH O 6 .   ? -7.333  -46.040 4.104   1.00 36.54 ? 925  HOH A O   1 
HETATM 3569 O O   . HOH O 6 .   ? -1.800  -6.337  -10.274 1.00 32.52 ? 926  HOH A O   1 
HETATM 3570 O O   . HOH O 6 .   ? 9.088   -30.398 14.266  1.00 22.37 ? 927  HOH A O   1 
HETATM 3571 O O   . HOH O 6 .   ? -2.220  -16.043 10.524  1.00 26.85 ? 928  HOH A O   1 
HETATM 3572 O O   . HOH O 6 .   ? -8.337  -38.943 -8.689  1.00 40.44 ? 929  HOH A O   1 
HETATM 3573 O O   . HOH O 6 .   ? 11.602  -22.280 12.561  1.00 46.50 ? 930  HOH A O   1 
HETATM 3574 O O   . HOH O 6 .   ? -3.462  -0.974  0.185   1.00 47.58 ? 931  HOH A O   1 
HETATM 3575 O O   . HOH O 6 .   ? -20.540 -26.307 -11.165 1.00 48.89 ? 932  HOH A O   1 
HETATM 3576 O O   . HOH O 6 .   ? 11.069  -8.834  -1.382  1.00 35.26 ? 933  HOH A O   1 
HETATM 3577 O O   . HOH O 6 .   ? -19.693 -24.588 10.798  1.00 26.70 ? 934  HOH A O   1 
HETATM 3578 O O   . HOH O 6 .   ? 12.426  2.492   -3.822  1.00 24.35 ? 935  HOH A O   1 
HETATM 3579 O O   . HOH O 6 .   ? 8.860   -40.918 9.256   1.00 40.83 ? 936  HOH A O   1 
HETATM 3580 O O   . HOH O 6 .   ? -4.349  -2.228  6.469   1.00 35.23 ? 937  HOH A O   1 
HETATM 3581 O O   . HOH O 6 .   ? 0.662   -24.459 19.103  1.00 16.57 ? 938  HOH A O   1 
HETATM 3582 O O   . HOH O 6 .   ? -10.881 -28.815 4.555   1.00 13.80 ? 939  HOH A O   1 
HETATM 3583 O O   . HOH O 6 .   ? -1.375  -39.979 -8.393  1.00 39.91 ? 940  HOH A O   1 
HETATM 3584 O O   . HOH O 6 .   ? -20.074 -30.105 -3.188  0.50 26.05 ? 941  HOH A O   1 
HETATM 3585 O O   . HOH O 6 .   ? 7.215   -22.706 0.347   1.00 14.34 ? 942  HOH A O   1 
HETATM 3586 O O   . HOH O 6 .   ? -18.101 -29.811 -2.251  0.50 28.40 ? 943  HOH A O   1 
HETATM 3587 O O   . HOH O 6 .   ? 8.006   3.181   -1.202  1.00 50.86 ? 944  HOH A O   1 
HETATM 3588 O O   . HOH O 6 .   ? -0.802  -4.452  10.933  1.00 18.24 ? 945  HOH A O   1 
HETATM 3589 O O   . HOH O 6 .   ? -24.767 -18.806 3.478   1.00 29.13 ? 946  HOH A O   1 
HETATM 3590 O O   . HOH O 6 .   ? -2.734  -24.649 -7.690  1.00 12.36 ? 947  HOH A O   1 
HETATM 3591 O O   . HOH O 6 .   ? 6.252   -35.115 -1.856  0.50 25.13 ? 948  HOH A O   1 
HETATM 3592 O O   . HOH O 6 .   ? 4.575   -33.031 4.787   1.00 12.43 ? 949  HOH A O   1 
HETATM 3593 O O   . HOH O 6 .   ? -13.357 -39.872 2.461   1.00 24.74 ? 950  HOH A O   1 
HETATM 3594 O O   . HOH O 6 .   ? -13.924 -47.033 8.426   1.00 18.28 ? 951  HOH A O   1 
HETATM 3595 O O   . HOH O 6 .   ? -4.603  -4.584  -2.897  1.00 25.82 ? 952  HOH A O   1 
HETATM 3596 O O   . HOH O 6 .   ? -11.795 -26.096 -4.139  1.00 15.23 ? 953  HOH A O   1 
HETATM 3597 O O   . HOH O 6 .   ? 2.306   -30.853 -8.907  1.00 23.75 ? 954  HOH A O   1 
HETATM 3598 O O   . HOH O 6 .   ? -1.379  -32.846 0.381   1.00 12.74 ? 955  HOH A O   1 
HETATM 3599 O O   . HOH O 6 .   ? 7.805   -21.151 11.841  1.00 18.89 ? 956  HOH A O   1 
HETATM 3600 O O   . HOH O 6 .   ? -2.310  -33.007 -10.734 1.00 56.64 ? 957  HOH A O   1 
HETATM 3601 O O   . HOH O 6 .   ? -11.686 -15.072 5.508   1.00 16.05 ? 958  HOH A O   1 
HETATM 3602 O O   . HOH O 6 .   ? -1.315  -43.349 5.301   1.00 40.16 ? 959  HOH A O   1 
HETATM 3603 O O   . HOH O 6 .   ? -6.171  -36.212 4.811   0.50 14.86 ? 960  HOH A O   1 
HETATM 3604 O O   . HOH O 6 .   ? -0.319  -11.415 -8.861  1.00 12.44 ? 961  HOH A O   1 
HETATM 3605 O O   . HOH O 6 .   ? 2.935   -36.397 -2.223  1.00 19.01 ? 962  HOH A O   1 
HETATM 3606 O O   . HOH O 6 .   ? -1.643  -40.064 1.860   1.00 17.41 ? 963  HOH A O   1 
HETATM 3607 O O   . HOH O 6 .   ? 7.823   -26.452 16.318  1.00 27.16 ? 964  HOH A O   1 
HETATM 3608 O O   . HOH O 6 .   ? 11.737  -36.527 6.565   1.00 50.04 ? 965  HOH A O   1 
HETATM 3609 O O   . HOH O 6 .   ? 1.781   -14.581 7.927   1.00 12.36 ? 966  HOH A O   1 
HETATM 3610 O O   . HOH O 6 .   ? 4.212   -17.595 -0.457  1.00 10.12 ? 967  HOH A O   1 
HETATM 3611 O O   . HOH O 6 .   ? -23.454 -16.738 -5.449  1.00 50.65 ? 968  HOH A O   1 
HETATM 3612 O O   . HOH O 6 .   ? 9.680   -31.695 1.305   0.50 30.40 ? 969  HOH A O   1 
HETATM 3613 O O   . HOH O 6 .   ? 11.233  -35.746 10.283  1.00 34.61 ? 970  HOH A O   1 
HETATM 3614 O O   . HOH O 6 .   ? -12.177 -44.794 -0.428  1.00 19.31 ? 971  HOH A O   1 
HETATM 3615 O O   . HOH O 6 .   ? 8.328   -18.443 8.903   1.00 19.77 ? 972  HOH A O   1 
HETATM 3616 O O   . HOH O 6 .   ? 4.761   -15.491 8.911   1.00 15.58 ? 973  HOH A O   1 
HETATM 3617 O O   . HOH O 6 .   ? -5.919  -36.818 21.380  1.00 39.95 ? 974  HOH A O   1 
HETATM 3618 O O   . HOH O 6 .   ? 7.278   -25.062 -2.357  0.50 8.53  ? 975  HOH A O   1 
HETATM 3619 O O   . HOH O 6 .   ? -20.176 -17.602 -12.508 1.00 60.91 ? 976  HOH A O   1 
HETATM 3620 O O   . HOH O 6 .   ? 4.752   -22.959 -7.861  1.00 27.68 ? 977  HOH A O   1 
HETATM 3621 O O   . HOH O 6 .   ? -13.123 -32.438 3.944   1.00 31.24 ? 978  HOH A O   1 
HETATM 3622 O O   . HOH O 6 .   ? 12.740  -27.610 0.972   1.00 44.50 ? 979  HOH A O   1 
HETATM 3623 O O   . HOH O 6 .   ? -1.702  -8.510  13.048  1.00 32.26 ? 980  HOH A O   1 
HETATM 3624 O O   . HOH O 6 .   ? -6.319  -3.954  -0.534  1.00 28.68 ? 981  HOH A O   1 
HETATM 3625 O O   . HOH O 6 .   ? 10.351  -28.869 4.613   1.00 30.40 ? 982  HOH A O   1 
HETATM 3626 O O   . HOH O 6 .   ? 2.615   -27.292 20.854  1.00 19.30 ? 983  HOH A O   1 
HETATM 3627 O O   . HOH O 6 .   ? -5.705  -10.339 -7.668  1.00 21.69 ? 984  HOH A O   1 
HETATM 3628 O O   . HOH O 6 .   ? -3.053  -5.127  -6.848  1.00 33.63 ? 985  HOH A O   1 
HETATM 3629 O O   . HOH O 6 .   ? -6.469  2.745   3.149   1.00 44.24 ? 986  HOH A O   1 
HETATM 3630 O O   . HOH O 6 .   ? 1.244   -7.991  -10.228 1.00 21.72 ? 987  HOH A O   1 
HETATM 3631 O O   . HOH O 6 .   ? 4.605   -8.818  14.494  1.00 39.25 ? 988  HOH A O   1 
HETATM 3632 O O   . HOH O 6 .   ? -9.640  -29.315 -3.051  1.00 33.26 ? 989  HOH A O   1 
HETATM 3633 O O   . HOH O 6 .   ? 9.541   -14.504 -5.111  1.00 12.42 ? 990  HOH A O   1 
HETATM 3634 O O   . HOH O 6 .   ? 10.671  -17.214 -4.819  0.50 20.35 ? 991  HOH A O   1 
HETATM 3635 O O   . HOH O 6 .   ? 0.906   -33.699 21.264  1.00 26.53 ? 992  HOH A O   1 
HETATM 3636 O O   . HOH O 6 .   ? -1.958  -24.286 -10.381 1.00 15.23 ? 993  HOH A O   1 
HETATM 3637 O O   . HOH O 6 .   ? 6.011   -14.831 0.910   1.00 9.20  ? 994  HOH A O   1 
HETATM 3638 O O   . HOH O 6 .   ? -5.392  -15.139 -12.495 1.00 26.79 ? 995  HOH A O   1 
HETATM 3639 O O   . HOH O 6 .   ? -23.641 -38.006 9.486   1.00 42.70 ? 996  HOH A O   1 
HETATM 3640 O O   . HOH O 6 .   ? -9.452  -30.803 3.106   1.00 12.09 ? 997  HOH A O   1 
HETATM 3641 O O   . HOH O 6 .   ? -8.724  -17.657 18.319  1.00 37.25 ? 998  HOH A O   1 
HETATM 3642 O O   . HOH O 6 .   ? 13.099  -17.238 9.784   1.00 42.99 ? 999  HOH A O   1 
HETATM 3643 O O   . HOH O 6 .   ? 12.237  -27.631 3.437   1.00 35.04 ? 1000 HOH A O   1 
HETATM 3644 O O   . HOH O 6 .   ? 10.706  -26.168 14.839  1.00 47.85 ? 1001 HOH A O   1 
HETATM 3645 O O   . HOH O 6 .   ? 6.497   -21.429 17.017  1.00 38.89 ? 1002 HOH A O   1 
HETATM 3646 O O   . HOH O 6 .   ? 0.442   -34.695 -10.718 1.00 33.55 ? 1003 HOH A O   1 
HETATM 3647 O O   . HOH O 6 .   ? 2.491   -1.570  -11.484 1.00 43.67 ? 1004 HOH A O   1 
HETATM 3648 O O   . HOH O 6 .   ? 3.428   -21.668 4.356   1.00 10.97 ? 1005 HOH A O   1 
HETATM 3649 O O   . HOH O 6 .   ? 4.054   -21.876 1.806   1.00 15.07 ? 1006 HOH A O   1 
HETATM 3650 O O   . HOH O 6 .   ? -9.486  -41.036 11.387  1.00 53.89 ? 1007 HOH A O   1 
HETATM 3651 O O   . HOH O 6 .   ? -23.455 -31.073 5.718   1.00 32.90 ? 1008 HOH A O   1 
HETATM 3652 O O   . HOH O 6 .   ? 3.181   -23.265 19.708  1.00 26.22 ? 1009 HOH A O   1 
HETATM 3653 O O   . HOH O 6 .   ? -1.931  0.033   6.882   1.00 37.31 ? 1010 HOH A O   1 
HETATM 3654 O O   . HOH O 6 .   ? -13.415 -34.946 5.189   1.00 47.40 ? 1011 HOH A O   1 
HETATM 3655 O O   . HOH O 6 .   ? -3.091  -11.491 -10.001 1.00 41.22 ? 1012 HOH A O   1 
HETATM 3656 O O   . HOH O 6 .   ? -22.088 -25.348 9.720   1.00 36.52 ? 1013 HOH A O   1 
HETATM 3657 O O   . HOH O 6 .   ? 5.142   -6.381  11.068  1.00 33.57 ? 1014 HOH A O   1 
HETATM 3658 O O   . HOH O 6 .   ? -17.071 -15.416 3.742   1.00 35.93 ? 1015 HOH A O   1 
HETATM 3659 O O   . HOH O 6 .   ? -11.549 -22.942 -14.562 1.00 40.00 ? 1016 HOH A O   1 
HETATM 3660 O O   . HOH O 6 .   ? 11.751  -12.363 4.559   1.00 26.71 ? 1017 HOH A O   1 
HETATM 3661 O O   . HOH O 6 .   ? 9.773   -21.278 -3.377  0.50 16.38 ? 1018 HOH A O   1 
HETATM 3662 O O   . HOH O 6 .   ? -3.184  -23.831 -14.346 1.00 43.82 ? 1019 HOH A O   1 
HETATM 3663 O O   . HOH O 6 .   ? -1.341  -14.099 -11.981 1.00 31.32 ? 1020 HOH A O   1 
HETATM 3664 O O   . HOH O 6 .   ? -12.557 -10.986 7.159   1.00 37.42 ? 1021 HOH A O   1 
HETATM 3665 O O   . HOH O 6 .   ? -12.870 -39.254 6.259   1.00 45.35 ? 1022 HOH A O   1 
HETATM 3666 O O   . HOH O 6 .   ? 5.472   -20.844 -6.625  1.00 20.20 ? 1023 HOH A O   1 
HETATM 3667 O O   . HOH O 6 .   ? -9.413  -4.104  -3.643  1.00 33.04 ? 1024 HOH A O   1 
HETATM 3668 O O   . HOH O 6 .   ? 2.501   -10.134 13.470  1.00 17.92 ? 1025 HOH A O   1 
HETATM 3669 O O   . HOH O 6 .   ? -8.046  -9.406  11.347  1.00 47.26 ? 1026 HOH A O   1 
HETATM 3670 O O   . HOH O 6 .   ? -14.900 -15.075 11.784  0.50 13.07 ? 1027 HOH A O   1 
HETATM 3671 O O   . HOH O 6 .   ? 7.098   -35.188 -6.138  1.00 51.56 ? 1028 HOH A O   1 
HETATM 3672 O O   . HOH O 6 .   ? 10.090  -33.855 8.204   1.00 24.91 ? 1029 HOH A O   1 
HETATM 3673 O O   . HOH O 6 .   ? 7.628   -32.230 18.523  1.00 43.72 ? 1030 HOH A O   1 
HETATM 3674 O O   . HOH O 6 .   ? 9.500   -19.464 -6.107  1.00 39.85 ? 1031 HOH A O   1 
HETATM 3675 O O   . HOH O 6 .   ? -23.802 -29.526 3.499   0.50 13.99 ? 1032 HOH A O   1 
HETATM 3676 O O   . HOH O 6 .   ? 11.699  -15.743 -3.597  0.50 23.81 ? 1033 HOH A O   1 
HETATM 3677 O O   . HOH O 6 .   ? -4.889  -8.344  -9.119  1.00 39.23 ? 1034 HOH A O   1 
HETATM 3678 O O   . HOH O 6 .   ? -9.904  -31.202 22.015  1.00 34.73 ? 1035 HOH A O   1 
HETATM 3679 O O   . HOH O 6 .   ? 7.199   -29.921 21.383  0.50 34.23 ? 1036 HOH A O   1 
HETATM 3680 O O   . HOH O 6 .   ? 11.866  -29.083 13.845  1.00 38.10 ? 1037 HOH A O   1 
HETATM 3681 O O   . HOH O 6 .   ? 3.194   -3.297  -10.043 1.00 40.47 ? 1038 HOH A O   1 
HETATM 3682 O O   . HOH O 6 .   ? 5.089   -41.209 10.303  1.00 56.35 ? 1039 HOH A O   1 
HETATM 3683 O O   . HOH O 6 .   ? -4.887  -40.356 11.127  1.00 41.49 ? 1040 HOH A O   1 
HETATM 3684 O O   . HOH O 6 .   ? 1.514   -36.552 18.078  1.00 29.67 ? 1041 HOH A O   1 
HETATM 3685 O O   . HOH O 6 .   ? 7.501   -7.447  10.474  1.00 44.15 ? 1042 HOH A O   1 
HETATM 3686 O O   . HOH O 6 .   ? 8.919   -30.304 0.215   0.50 18.42 ? 1043 HOH A O   1 
HETATM 3687 O O   . HOH O 6 .   ? 0.855   4.019   4.462   1.00 45.83 ? 1044 HOH A O   1 
HETATM 3688 O O   . HOH O 6 .   ? 9.191   -11.612 8.834   1.00 32.90 ? 1045 HOH A O   1 
HETATM 3689 O O   . HOH O 6 .   ? -14.850 -34.810 -6.333  1.00 45.04 ? 1046 HOH A O   1 
HETATM 3690 O O   . HOH O 6 .   ? -11.277 -31.423 1.245   1.00 21.37 ? 1047 HOH A O   1 
HETATM 3691 O O   . HOH O 6 .   ? -2.541  -46.164 4.993   1.00 64.58 ? 1048 HOH A O   1 
HETATM 3692 O O   . HOH O 6 .   ? 0.684   -14.772 -10.518 1.00 50.93 ? 1049 HOH A O   1 
HETATM 3693 O O   . HOH O 6 .   ? 7.707   -28.899 16.458  1.00 31.54 ? 1050 HOH A O   1 
HETATM 3694 O O   . HOH O 6 .   ? -23.046 -30.104 1.444   0.50 25.84 ? 1051 HOH A O   1 
HETATM 3695 O O   . HOH O 6 .   ? -2.743  -3.126  9.929   1.00 32.26 ? 1052 HOH A O   1 
HETATM 3696 O O   . HOH O 6 .   ? -17.424 -6.873  4.714   1.00 62.58 ? 1053 HOH A O   1 
HETATM 3697 O O   . HOH O 6 .   ? 13.468  -11.899 2.049   1.00 39.80 ? 1054 HOH A O   1 
HETATM 3698 O O   . HOH O 6 .   ? 3.524   -4.026  9.928   1.00 38.18 ? 1055 HOH A O   1 
HETATM 3699 O O   . HOH O 6 .   ? 9.497   -32.513 16.309  1.00 42.95 ? 1056 HOH A O   1 
HETATM 3700 O O   . HOH O 6 .   ? -19.906 -15.439 7.637   1.00 51.41 ? 1057 HOH A O   1 
HETATM 3701 O O   . HOH O 6 .   ? 8.069   3.777   1.517   1.00 50.03 ? 1058 HOH A O   1 
HETATM 3702 O O   . HOH O 6 .   ? -11.350 -36.514 -9.142  1.00 30.83 ? 1059 HOH A O   1 
HETATM 3703 O O   . HOH O 6 .   ? 0.422   1.084   6.097   1.00 62.19 ? 1060 HOH A O   1 
HETATM 3704 O O   . HOH O 6 .   ? -11.608 -28.835 -4.520  1.00 38.22 ? 1061 HOH A O   1 
HETATM 3705 O O   . HOH O 6 .   ? 5.508   -6.549  14.030  1.00 45.83 ? 1062 HOH A O   1 
HETATM 3706 O O   . HOH O 6 .   ? -9.191  -11.781 10.938  1.00 40.48 ? 1063 HOH A O   1 
HETATM 3707 O O   . HOH O 6 .   ? -11.799 -12.057 9.415   1.00 32.08 ? 1064 HOH A O   1 
HETATM 3708 O O   . HOH O 6 .   ? -13.184 -5.112  -4.575  1.00 32.04 ? 1065 HOH A O   1 
HETATM 3709 O O   . HOH O 6 .   ? 6.470   -23.939 17.524  1.00 47.30 ? 1066 HOH A O   1 
HETATM 3710 O O   . HOH O 6 .   ? 3.116   -41.550 12.155  1.00 61.27 ? 1067 HOH A O   1 
HETATM 3711 O O   . HOH O 6 .   ? -23.574 -17.284 10.042  1.00 48.77 ? 1068 HOH A O   1 
HETATM 3712 O O   . HOH O 6 .   ? -22.897 -30.776 -2.226  1.00 58.64 ? 1069 HOH A O   1 
HETATM 3713 O O   . HOH O 6 .   ? 0.051   -25.286 -13.778 1.00 36.93 ? 1070 HOH A O   1 
HETATM 3714 O O   . HOH O 6 .   ? 0.171   -9.678  14.939  1.00 30.54 ? 1071 HOH A O   1 
HETATM 3715 O O   . HOH O 6 .   ? 7.466   -19.778 -7.970  1.00 38.13 ? 1072 HOH A O   1 
HETATM 3716 O O   . HOH O 6 .   ? 1.136   -2.875  11.999  1.00 42.08 ? 1073 HOH A O   1 
HETATM 3717 O O   . HOH O 6 .   ? 11.299  -14.984 10.362  1.00 43.92 ? 1074 HOH A O   1 
HETATM 3718 O O   . HOH O 6 .   ? 0.087   -42.181 2.533   0.50 23.37 ? 1075 HOH A O   1 
HETATM 3719 O O   . HOH O 6 .   ? -10.484 -33.415 -2.722  1.00 42.41 ? 1076 HOH A O   1 
HETATM 3720 O O   . HOH O 6 .   ? -5.543  -5.915  11.880  1.00 46.32 ? 1077 HOH A O   1 
HETATM 3721 O O   . HOH O 6 .   ? 3.667   -2.598  5.356   1.00 47.00 ? 1078 HOH A O   1 
HETATM 3722 O O   . HOH O 6 .   ? -6.508  -6.134  -9.501  1.00 43.64 ? 1079 HOH A O   1 
HETATM 3723 O O   . HOH O 6 .   ? -10.788 -31.041 -1.635  1.00 29.34 ? 1080 HOH A O   1 
HETATM 3724 O O   . HOH O 6 .   ? -4.733  -41.250 -5.601  1.00 46.65 ? 1081 HOH A O   1 
HETATM 3725 O O   . HOH O 6 .   ? 12.612  -13.025 7.089   1.00 45.65 ? 1082 HOH A O   1 
HETATM 3726 O O   . HOH O 6 .   ? -2.074  -5.819  12.925  1.00 33.79 ? 1083 HOH A O   1 
HETATM 3727 O O   . HOH O 6 .   ? 15.169  -20.050 10.520  1.00 48.77 ? 1084 HOH A O   1 
HETATM 3728 O O   . HOH O 6 .   ? -6.635  -3.244  -4.299  0.50 23.60 ? 1085 HOH A O   1 
HETATM 3729 O O   . HOH O 6 .   ? -5.547  -3.945  10.362  1.00 39.06 ? 1086 HOH A O   1 
HETATM 3730 O O   . HOH O 6 .   ? 21.104  -14.152 1.908   1.00 54.52 ? 1087 HOH A O   1 
HETATM 3731 O O   . HOH O 6 .   ? 5.570   -10.824 16.608  1.00 46.10 ? 1088 HOH A O   1 
HETATM 3732 O O   . HOH O 6 .   ? 13.085  -9.956  0.201   1.00 42.65 ? 1089 HOH A O   1 
HETATM 3733 O O   . HOH O 6 .   ? -7.120  -9.503  -13.405 1.00 61.37 ? 1090 HOH A O   1 
HETATM 3734 O O   . HOH O 6 .   ? -29.793 -14.023 17.364  1.00 61.34 ? 1091 HOH A O   1 
HETATM 3735 O O   . HOH O 6 .   ? 10.316  -29.072 18.614  1.00 45.90 ? 1092 HOH A O   1 
HETATM 3736 O O   . HOH P 6 .   ? -0.040  -21.914 -16.872 1.00 35.42 ? 401  HOH B O   1 
HETATM 3737 O O   . HOH P 6 .   ? -4.259  -2.005  -32.748 1.00 34.67 ? 402  HOH B O   1 
HETATM 3738 O O   . HOH P 6 .   ? -7.316  -28.138 -25.651 1.00 36.52 ? 403  HOH B O   1 
HETATM 3739 O O   . HOH P 6 .   ? -4.126  -15.770 -36.761 1.00 44.31 ? 404  HOH B O   1 
HETATM 3740 O O   . HOH P 6 .   ? 6.294   2.687   -15.385 1.00 37.81 ? 405  HOH B O   1 
HETATM 3741 O O   . HOH P 6 .   ? -10.282 -39.430 -38.837 1.00 26.37 ? 406  HOH B O   1 
HETATM 3742 O O   . HOH P 6 .   ? 6.466   1.514   -23.333 1.00 20.56 ? 407  HOH B O   1 
HETATM 3743 O O   . HOH P 6 .   ? 0.274   -38.469 -30.932 1.00 31.57 ? 408  HOH B O   1 
HETATM 3744 O O   . HOH P 6 .   ? 21.931  -8.027  -24.055 1.00 36.88 ? 409  HOH B O   1 
HETATM 3745 O O   . HOH P 6 .   ? -10.675 -18.777 -27.673 1.00 43.73 ? 410  HOH B O   1 
HETATM 3746 O O   . HOH P 6 .   ? 6.895   -38.312 -32.173 1.00 46.64 ? 411  HOH B O   1 
HETATM 3747 O O   . HOH P 6 .   ? -10.704 -8.146  -22.436 1.00 35.10 ? 412  HOH B O   1 
HETATM 3748 O O   . HOH P 6 .   ? 23.797  -12.988 -43.451 1.00 53.14 ? 413  HOH B O   1 
HETATM 3749 O O   . HOH P 6 .   ? 6.327   -35.587 -33.286 1.00 39.23 ? 414  HOH B O   1 
HETATM 3750 O O   . HOH P 6 .   ? 26.640  -1.444  -22.866 1.00 43.44 ? 415  HOH B O   1 
HETATM 3751 O O   . HOH P 6 .   ? 22.502  -25.121 -32.767 1.00 42.42 ? 416  HOH B O   1 
HETATM 3752 O O   . HOH P 6 .   ? 28.962  -13.617 -22.601 1.00 49.06 ? 417  HOH B O   1 
HETATM 3753 O O   . HOH P 6 .   ? 21.529  -14.289 -42.393 1.00 57.33 ? 418  HOH B O   1 
HETATM 3754 O O   . HOH P 6 .   ? 8.762   -26.854 -40.837 1.00 36.94 ? 419  HOH B O   1 
HETATM 3755 O O   . HOH P 6 .   ? 10.548  6.662   -28.233 1.00 34.39 ? 420  HOH B O   1 
HETATM 3756 O O   . HOH P 6 .   ? -6.990  -15.778 -34.478 1.00 41.36 ? 421  HOH B O   1 
HETATM 3757 O O   . HOH P 6 .   ? 1.543   -16.203 -46.123 1.00 34.10 ? 422  HOH B O   1 
HETATM 3758 O O   . HOH P 6 .   ? -2.728  -21.088 -20.198 0.50 16.44 ? 423  HOH B O   1 
HETATM 3759 O O   . HOH P 6 .   ? 13.756  -33.477 -37.618 1.00 29.49 ? 424  HOH B O   1 
HETATM 3760 O O   . HOH P 6 .   ? 3.214   -9.971  -10.176 1.00 29.20 ? 425  HOH B O   1 
HETATM 3761 O O   . HOH P 6 .   ? -9.157  -41.789 -36.163 0.50 12.07 ? 426  HOH B O   1 
HETATM 3762 O O   . HOH P 6 .   ? 0.934   -8.421  -41.230 1.00 21.89 ? 427  HOH B O   1 
HETATM 3763 O O   . HOH P 6 .   ? 17.239  7.578   -23.948 1.00 18.42 ? 428  HOH B O   1 
HETATM 3764 O O   . HOH P 6 .   ? -7.809  -30.521 -33.765 1.00 31.57 ? 429  HOH B O   1 
HETATM 3765 O O   . HOH P 6 .   ? -10.794 -23.844 -27.092 1.00 29.47 ? 430  HOH B O   1 
HETATM 3766 O O   . HOH P 6 .   ? 5.493   -24.137 -18.511 1.00 35.39 ? 431  HOH B O   1 
HETATM 3767 O O   . HOH P 6 .   ? 3.564   -27.942 -41.223 1.00 14.75 ? 432  HOH B O   1 
HETATM 3768 O O   . HOH P 6 .   ? -3.681  6.592   -25.902 1.00 36.10 ? 433  HOH B O   1 
HETATM 3769 O O   . HOH P 6 .   ? 6.209   -34.261 -39.239 1.00 32.88 ? 434  HOH B O   1 
HETATM 3770 O O   . HOH P 6 .   ? 16.594  0.574   -29.868 1.00 22.84 ? 435  HOH B O   1 
HETATM 3771 O O   . HOH P 6 .   ? 5.970   -14.685 -40.080 1.00 12.10 ? 436  HOH B O   1 
HETATM 3772 O O   . HOH P 6 .   ? 0.325   -2.937  -34.529 1.00 17.59 ? 437  HOH B O   1 
HETATM 3773 O O   . HOH P 6 .   ? 27.959  -20.521 -28.790 1.00 28.00 ? 438  HOH B O   1 
HETATM 3774 O O   . HOH P 6 .   ? 5.495   -23.302 -22.020 1.00 25.39 ? 439  HOH B O   1 
HETATM 3775 O O   . HOH P 6 .   ? -4.023  -16.619 -32.008 1.00 14.29 ? 440  HOH B O   1 
HETATM 3776 O O   . HOH P 6 .   ? -4.029  -14.389 -34.661 1.00 22.78 ? 441  HOH B O   1 
HETATM 3777 O O   . HOH P 6 .   ? -5.935  -8.999  -18.070 1.00 22.93 ? 442  HOH B O   1 
HETATM 3778 O O   . HOH P 6 .   ? -6.255  -19.010 -18.558 1.00 59.91 ? 443  HOH B O   1 
HETATM 3779 O O   . HOH P 6 .   ? 11.677  -7.057  -18.586 1.00 21.40 ? 444  HOH B O   1 
HETATM 3780 O O   . HOH P 6 .   ? -1.353  -6.297  -27.652 1.00 12.99 ? 445  HOH B O   1 
HETATM 3781 O O   . HOH P 6 .   ? 5.171   -33.094 -42.659 1.00 31.75 ? 446  HOH B O   1 
HETATM 3782 O O   . HOH P 6 .   ? -1.076  -12.713 -40.599 1.00 43.61 ? 447  HOH B O   1 
HETATM 3783 O O   . HOH P 6 .   ? 7.557   -37.144 -25.955 1.00 30.22 ? 448  HOH B O   1 
HETATM 3784 O O   . HOH P 6 .   ? 14.967  -13.258 -36.563 1.00 18.78 ? 449  HOH B O   1 
HETATM 3785 O O   . HOH P 6 .   ? -8.385  -2.651  -25.789 1.00 51.77 ? 450  HOH B O   1 
HETATM 3786 O O   . HOH P 6 .   ? 14.862  -24.289 -26.859 1.00 16.43 ? 451  HOH B O   1 
HETATM 3787 O O   . HOH P 6 .   ? 1.474   -24.714 -24.438 1.00 13.61 ? 452  HOH B O   1 
HETATM 3788 O O   . HOH P 6 .   ? -5.431  -41.512 -37.261 1.00 47.34 ? 453  HOH B O   1 
HETATM 3789 O O   . HOH P 6 .   ? 16.318  -6.961  -28.366 1.00 28.39 ? 454  HOH B O   1 
HETATM 3790 O O   . HOH P 6 .   ? 2.601   -14.809 -13.239 1.00 16.44 ? 455  HOH B O   1 
HETATM 3791 O O   . HOH P 6 .   ? 4.089   -34.817 -21.361 1.00 22.25 ? 456  HOH B O   1 
HETATM 3792 O O   . HOH P 6 .   ? 3.790   -8.181  -43.816 1.00 59.48 ? 457  HOH B O   1 
HETATM 3793 O O   . HOH P 6 .   ? -0.002  -26.813 -44.419 1.00 17.25 ? 458  HOH B O   1 
HETATM 3794 O O   . HOH P 6 .   ? 7.808   -34.793 -35.256 1.00 25.28 ? 459  HOH B O   1 
HETATM 3795 O O   . HOH P 6 .   ? 4.919   0.676   -30.542 1.00 17.73 ? 460  HOH B O   1 
HETATM 3796 O O   . HOH P 6 .   ? -5.044  -20.922 -23.470 1.00 17.91 ? 461  HOH B O   1 
HETATM 3797 O O   . HOH P 6 .   ? 15.418  -28.311 -25.212 1.00 43.60 ? 462  HOH B O   1 
HETATM 3798 O O   . HOH P 6 .   ? 5.059   -30.969 -19.506 1.00 31.19 ? 463  HOH B O   1 
HETATM 3799 O O   . HOH P 6 .   ? 1.599   -38.911 -39.104 1.00 39.08 ? 464  HOH B O   1 
HETATM 3800 O O   . HOH P 6 .   ? -4.494  -18.221 -20.503 1.00 18.49 ? 465  HOH B O   1 
HETATM 3801 O O   . HOH P 6 .   ? -1.412  -23.958 -23.416 1.00 17.96 ? 466  HOH B O   1 
HETATM 3802 O O   . HOH P 6 .   ? -1.563  -30.379 -17.845 1.00 46.95 ? 467  HOH B O   1 
HETATM 3803 O O   . HOH P 6 .   ? 20.867  -4.422  -40.525 1.00 48.60 ? 468  HOH B O   1 
HETATM 3804 O O   . HOH P 6 .   ? 22.860  -14.786 -21.528 1.00 24.60 ? 469  HOH B O   1 
HETATM 3805 O O   . HOH P 6 .   ? 9.404   -3.148  -27.626 0.50 11.00 ? 470  HOH B O   1 
HETATM 3806 O O   . HOH P 6 .   ? 4.530   0.701   -40.758 1.00 44.78 ? 471  HOH B O   1 
HETATM 3807 O O   . HOH P 6 .   ? -1.560  -16.345 -40.264 0.50 12.91 ? 472  HOH B O   1 
HETATM 3808 O O   . HOH P 6 .   ? 4.684   -6.499  -32.002 1.00 11.76 ? 473  HOH B O   1 
HETATM 3809 O O   . HOH P 6 .   ? -0.962  -21.772 -32.841 1.00 8.68  ? 474  HOH B O   1 
HETATM 3810 O O   . HOH P 6 .   ? 14.080  -10.575 -27.766 1.00 13.85 ? 475  HOH B O   1 
HETATM 3811 O O   . HOH P 6 .   ? -1.288  -18.648 -44.492 1.00 20.83 ? 476  HOH B O   1 
HETATM 3812 O O   . HOH P 6 .   ? 15.444  5.520   -32.753 1.00 18.47 ? 477  HOH B O   1 
HETATM 3813 O O   . HOH P 6 .   ? 13.637  -0.895  -16.885 1.00 39.65 ? 478  HOH B O   1 
HETATM 3814 O O   . HOH P 6 .   ? -2.802  -24.509 -31.438 1.00 9.39  ? 479  HOH B O   1 
HETATM 3815 O O   . HOH P 6 .   ? -7.158  -10.424 -27.759 0.50 17.22 ? 480  HOH B O   1 
HETATM 3816 O O   . HOH P 6 .   ? -7.962  -3.708  -22.234 0.50 19.48 ? 481  HOH B O   1 
HETATM 3817 O O   . HOH P 6 .   ? -7.381  -22.147 -37.288 1.00 42.42 ? 482  HOH B O   1 
HETATM 3818 O O   . HOH P 6 .   ? 4.541   -20.745 -12.146 1.00 17.94 ? 483  HOH B O   1 
HETATM 3819 O O   . HOH P 6 .   ? 10.943  -3.653  -29.053 0.50 23.89 ? 484  HOH B O   1 
HETATM 3820 O O   . HOH P 6 .   ? -7.251  -21.509 -19.865 1.00 53.48 ? 485  HOH B O   1 
HETATM 3821 O O   . HOH P 6 .   ? 9.039   -29.098 -40.012 1.00 23.02 ? 486  HOH B O   1 
HETATM 3822 O O   . HOH P 6 .   ? 6.445   -27.751 -42.398 1.00 42.59 ? 487  HOH B O   1 
HETATM 3823 O O   . HOH P 6 .   ? 9.704   -35.286 -32.796 1.00 31.41 ? 488  HOH B O   1 
HETATM 3824 O O   . HOH P 6 .   ? -8.869  -11.586 -28.714 0.50 21.30 ? 489  HOH B O   1 
HETATM 3825 O O   . HOH P 6 .   ? -6.236  -19.907 -38.247 1.00 38.79 ? 490  HOH B O   1 
HETATM 3826 O O   . HOH P 6 .   ? -0.208  -17.718 -27.956 1.00 10.91 ? 491  HOH B O   1 
HETATM 3827 O O   . HOH P 6 .   ? 5.188   -15.048 -42.690 1.00 15.86 ? 492  HOH B O   1 
HETATM 3828 O O   . HOH P 6 .   ? 12.625  -8.532  -29.208 1.00 12.13 ? 493  HOH B O   1 
HETATM 3829 O O   . HOH P 6 .   ? 11.600  -3.784  -24.283 1.00 34.55 ? 494  HOH B O   1 
HETATM 3830 O O   . HOH P 6 .   ? -4.425  -12.948 -15.954 1.00 31.57 ? 495  HOH B O   1 
HETATM 3831 O O   . HOH P 6 .   ? -1.817  -32.912 -21.326 1.00 38.59 ? 496  HOH B O   1 
HETATM 3832 O O   . HOH P 6 .   ? -6.328  -24.788 -37.469 1.00 13.57 ? 497  HOH B O   1 
HETATM 3833 O O   . HOH P 6 .   ? 25.405  -13.981 -22.714 1.00 28.94 ? 498  HOH B O   1 
HETATM 3834 O O   . HOH P 6 .   ? 21.517  -9.258  -35.033 1.00 52.28 ? 499  HOH B O   1 
HETATM 3835 O O   . HOH P 6 .   ? -5.959  -8.761  -31.684 1.00 36.74 ? 500  HOH B O   1 
HETATM 3836 O O   . HOH P 6 .   ? 12.024  -21.608 -13.982 1.00 46.80 ? 501  HOH B O   1 
HETATM 3837 O O   . HOH P 6 .   ? 0.578   -12.086 -11.518 1.00 18.73 ? 502  HOH B O   1 
HETATM 3838 O O   . HOH P 6 .   ? 2.637   -4.662  -43.081 1.00 31.41 ? 503  HOH B O   1 
HETATM 3839 O O   . HOH P 6 .   ? -2.229  -18.530 -38.887 0.50 6.64  ? 504  HOH B O   1 
HETATM 3840 O O   . HOH P 6 .   ? 6.551   -15.741 -46.803 1.00 41.12 ? 505  HOH B O   1 
HETATM 3841 O O   . HOH P 6 .   ? 5.064   -39.407 -25.540 1.00 32.53 ? 506  HOH B O   1 
HETATM 3842 O O   . HOH P 6 .   ? -3.774  -5.823  -34.990 0.50 25.44 ? 507  HOH B O   1 
HETATM 3843 O O   . HOH P 6 .   ? 14.530  -16.113 -46.902 0.50 26.62 ? 508  HOH B O   1 
HETATM 3844 O O   . HOH P 6 .   ? 12.996  -9.932  -35.338 1.00 31.27 ? 509  HOH B O   1 
HETATM 3845 O O   . HOH P 6 .   ? 9.256   -2.723  -10.903 1.00 42.68 ? 510  HOH B O   1 
HETATM 3846 O O   . HOH P 6 .   ? 1.941   -31.428 -42.643 1.00 23.29 ? 511  HOH B O   1 
HETATM 3847 O O   . HOH P 6 .   ? -8.510  -26.959 -27.925 1.00 28.01 ? 512  HOH B O   1 
HETATM 3848 O O   . HOH P 6 .   ? -3.147  -17.114 -15.069 1.00 43.33 ? 513  HOH B O   1 
HETATM 3849 O O   . HOH P 6 .   ? -6.503  -18.029 -35.549 1.00 30.96 ? 514  HOH B O   1 
HETATM 3850 O O   . HOH P 6 .   ? 8.619   -24.229 -44.913 1.00 28.02 ? 515  HOH B O   1 
HETATM 3851 O O   . HOH P 6 .   ? -0.850  -17.431 -30.596 1.00 14.31 ? 516  HOH B O   1 
HETATM 3852 O O   . HOH P 6 .   ? -9.442  -11.578 -31.646 1.00 45.78 ? 517  HOH B O   1 
HETATM 3853 O O   . HOH P 6 .   ? -4.365  -7.278  -13.806 1.00 46.59 ? 518  HOH B O   1 
HETATM 3854 O O   . HOH P 6 .   ? 20.281  -23.859 -28.793 1.00 36.35 ? 519  HOH B O   1 
HETATM 3855 O O   . HOH P 6 .   ? 2.286   -5.603  -11.083 1.00 27.39 ? 520  HOH B O   1 
HETATM 3856 O O   . HOH P 6 .   ? 26.690  -8.383  -26.723 1.00 31.28 ? 521  HOH B O   1 
HETATM 3857 O O   . HOH P 6 .   ? 0.040   -16.067 -12.620 1.00 27.02 ? 522  HOH B O   1 
HETATM 3858 O O   . HOH P 6 .   ? 10.965  -30.360 -20.694 1.00 43.22 ? 523  HOH B O   1 
HETATM 3859 O O   . HOH P 6 .   ? 12.647  -35.197 -35.999 1.00 35.70 ? 524  HOH B O   1 
HETATM 3860 O O   . HOH P 6 .   ? 11.233  -3.653  -9.743  1.00 34.55 ? 525  HOH B O   1 
HETATM 3861 O O   . HOH P 6 .   ? 4.647   -25.261 -44.449 1.00 33.45 ? 526  HOH B O   1 
HETATM 3862 O O   . HOH P 6 .   ? -6.899  -5.512  -24.061 1.00 24.39 ? 527  HOH B O   1 
HETATM 3863 O O   . HOH P 6 .   ? -1.936  -1.916  -36.046 1.00 47.64 ? 528  HOH B O   1 
HETATM 3864 O O   . HOH P 6 .   ? 16.144  -8.307  -32.950 1.00 41.66 ? 529  HOH B O   1 
HETATM 3865 O O   . HOH P 6 .   ? -8.558  -23.623 -35.838 0.50 19.39 ? 530  HOH B O   1 
HETATM 3866 O O   . HOH P 6 .   ? 9.965   -4.854  -22.601 1.00 38.06 ? 531  HOH B O   1 
HETATM 3867 O O   . HOH P 6 .   ? 0.830   -29.208 -18.838 1.00 17.58 ? 532  HOH B O   1 
HETATM 3868 O O   . HOH P 6 .   ? 18.213  -24.226 -20.610 0.50 13.28 ? 533  HOH B O   1 
HETATM 3869 O O   . HOH P 6 .   ? 27.006  -9.804  -28.909 0.50 18.91 ? 534  HOH B O   1 
HETATM 3870 O O   . HOH P 6 .   ? 11.202  -32.421 -24.926 1.00 51.50 ? 535  HOH B O   1 
HETATM 3871 O O   . HOH P 6 .   ? -0.982  -22.286 -19.172 0.50 18.73 ? 536  HOH B O   1 
HETATM 3872 O O   . HOH P 6 .   ? 1.859   -2.794  -14.296 1.00 30.51 ? 537  HOH B O   1 
HETATM 3873 O O   . HOH P 6 .   ? -5.844  -27.855 -23.658 1.00 32.22 ? 538  HOH B O   1 
HETATM 3874 O O   . HOH P 6 .   ? 0.601   -26.238 -19.365 1.00 17.24 ? 539  HOH B O   1 
HETATM 3875 O O   . HOH P 6 .   ? 12.032  -28.072 -21.273 1.00 40.96 ? 540  HOH B O   1 
HETATM 3876 O O   . HOH P 6 .   ? 13.541  -8.443  -10.779 0.50 25.73 ? 541  HOH B O   1 
HETATM 3877 O O   . HOH P 6 .   ? 22.268  -8.864  -19.116 1.00 45.10 ? 542  HOH B O   1 
HETATM 3878 O O   . HOH P 6 .   ? -1.528  1.883   -22.280 1.00 52.33 ? 543  HOH B O   1 
HETATM 3879 O O   . HOH P 6 .   ? -3.774  -43.375 -31.538 0.50 36.94 ? 544  HOH B O   1 
HETATM 3880 O O   . HOH P 6 .   ? 18.214  -4.441  -38.849 1.00 43.32 ? 545  HOH B O   1 
HETATM 3881 O O   . HOH P 6 .   ? 8.298   -31.006 -41.556 1.00 45.33 ? 546  HOH B O   1 
HETATM 3882 O O   . HOH P 6 .   ? -4.087  -32.072 -21.912 1.00 37.26 ? 547  HOH B O   1 
HETATM 3883 O O   . HOH P 6 .   ? 6.812   7.003   -27.879 0.50 41.33 ? 548  HOH B O   1 
HETATM 3884 O O   . HOH P 6 .   ? 23.160  -24.806 -24.559 1.00 48.61 ? 549  HOH B O   1 
HETATM 3885 O O   . HOH P 6 .   ? 26.932  -20.967 -25.988 1.00 43.22 ? 550  HOH B O   1 
HETATM 3886 O O   . HOH P 6 .   ? 18.608  -28.331 -25.836 1.00 59.23 ? 551  HOH B O   1 
HETATM 3887 O O   . HOH P 6 .   ? -4.385  -10.391 -15.860 1.00 31.14 ? 552  HOH B O   1 
HETATM 3888 O O   . HOH P 6 .   ? -2.639  -14.134 -38.285 1.00 58.89 ? 553  HOH B O   1 
HETATM 3889 O O   . HOH P 6 .   ? 9.713   -34.448 -24.692 1.00 51.28 ? 554  HOH B O   1 
HETATM 3890 O O   . HOH P 6 .   ? 26.250  -9.325  -30.918 0.50 20.95 ? 555  HOH B O   1 
HETATM 3891 O O   . HOH P 6 .   ? 14.494  -7.947  -31.202 1.00 21.34 ? 556  HOH B O   1 
HETATM 3892 O O   . HOH P 6 .   ? 4.172   -24.963 -12.092 1.00 46.32 ? 557  HOH B O   1 
HETATM 3893 O O   . HOH P 6 .   ? 30.371  -25.693 -14.293 1.00 42.59 ? 558  HOH B O   1 
HETATM 3894 O O   . HOH P 6 .   ? -10.264 -27.383 -30.361 1.00 46.81 ? 559  HOH B O   1 
HETATM 3895 O O   . HOH P 6 .   ? 13.300  -13.591 -46.417 1.00 48.81 ? 560  HOH B O   1 
HETATM 3896 O O   . HOH P 6 .   ? 9.734   6.214   -31.904 1.00 39.64 ? 561  HOH B O   1 
HETATM 3897 O O   . HOH P 6 .   ? 2.631   -24.636 -42.836 1.00 46.68 ? 562  HOH B O   1 
HETATM 3898 O O   . HOH P 6 .   ? 28.958  -10.774 -49.629 1.00 52.75 ? 563  HOH B O   1 
HETATM 3899 O O   . HOH P 6 .   ? -0.295  -35.284 -22.479 0.50 18.99 ? 564  HOH B O   1 
HETATM 3900 O O   . HOH P 6 .   ? 6.092   -36.269 -22.418 1.00 33.06 ? 565  HOH B O   1 
HETATM 3901 O O   . HOH P 6 .   ? 2.737   -25.628 -17.552 1.00 37.60 ? 566  HOH B O   1 
HETATM 3902 O O   . HOH P 6 .   ? -3.337  -3.853  -37.008 1.00 50.37 ? 567  HOH B O   1 
HETATM 3903 O O   . HOH P 6 .   ? 15.122  -27.202 -22.946 1.00 31.18 ? 568  HOH B O   1 
HETATM 3904 O O   . HOH P 6 .   ? 14.903  -10.554 -36.825 1.00 37.54 ? 569  HOH B O   1 
HETATM 3905 O O   . HOH P 6 .   ? -6.482  0.500   -29.825 1.00 36.21 ? 570  HOH B O   1 
HETATM 3906 O O   . HOH P 6 .   ? 16.491  -34.187 -36.825 1.00 32.65 ? 571  HOH B O   1 
HETATM 3907 O O   . HOH P 6 .   ? 3.038   -14.039 -46.027 1.00 36.80 ? 572  HOH B O   1 
HETATM 3908 O O   . HOH P 6 .   ? -4.583  -7.937  -41.936 1.00 56.56 ? 573  HOH B O   1 
HETATM 3909 O O   . HOH P 6 .   ? 4.676   -37.896 -36.672 1.00 49.17 ? 574  HOH B O   1 
HETATM 3910 O O   . HOH P 6 .   ? 13.753  -19.073 -12.763 1.00 45.98 ? 575  HOH B O   1 
HETATM 3911 O O   . HOH P 6 .   ? -3.820  -19.487 -40.446 1.00 34.37 ? 576  HOH B O   1 
HETATM 3912 O O   . HOH P 6 .   ? -1.627  -25.004 -19.103 1.00 36.44 ? 577  HOH B O   1 
HETATM 3913 O O   . HOH P 6 .   ? -4.930  -11.031 -11.576 1.00 50.34 ? 578  HOH B O   1 
HETATM 3914 O O   . HOH P 6 .   ? -2.930  -17.311 -43.009 1.00 45.63 ? 579  HOH B O   1 
HETATM 3915 O O   . HOH P 6 .   ? -1.190  -14.429 -44.535 1.00 47.02 ? 580  HOH B O   1 
HETATM 3916 O O   . HOH P 6 .   ? 30.441  -21.000 -16.374 1.00 56.16 ? 581  HOH B O   1 
HETATM 3917 O O   . HOH P 6 .   ? -8.708  -7.090  -29.476 1.00 45.41 ? 582  HOH B O   1 
HETATM 3918 O O   . HOH P 6 .   ? 2.918   -29.644 -17.439 1.00 30.47 ? 583  HOH B O   1 
HETATM 3919 O O   . HOH P 6 .   ? 1.891   3.158   -30.310 1.00 47.32 ? 584  HOH B O   1 
HETATM 3920 O O   . HOH P 6 .   ? -2.904  -5.345  -41.615 1.00 62.35 ? 585  HOH B O   1 
HETATM 3921 O O   . HOH P 6 .   ? -1.628  -10.246 -40.694 1.00 48.88 ? 586  HOH B O   1 
HETATM 3922 O O   . HOH P 6 .   ? -3.300  -43.351 -36.088 1.00 52.65 ? 587  HOH B O   1 
HETATM 3923 O O   . HOH P 6 .   ? 7.937   1.791   -38.096 1.00 42.25 ? 588  HOH B O   1 
HETATM 3924 O O   . HOH P 6 .   ? 12.608  -29.424 -40.965 1.00 45.35 ? 589  HOH B O   1 
HETATM 3925 O O   . HOH P 6 .   ? 23.659  0.745   -20.356 0.50 24.21 ? 590  HOH B O   1 
HETATM 3926 O O   . HOH P 6 .   ? 14.080  -8.271  -33.993 1.00 26.61 ? 591  HOH B O   1 
HETATM 3927 O O   . HOH P 6 .   ? 5.755   -13.342 -44.790 1.00 41.06 ? 592  HOH B O   1 
HETATM 3928 O O   . HOH P 6 .   ? -8.082  -24.568 -22.224 1.00 39.81 ? 593  HOH B O   1 
HETATM 3929 O O   . HOH P 6 .   ? 22.563  -24.739 -30.311 1.00 48.83 ? 594  HOH B O   1 
HETATM 3930 O O   . HOH P 6 .   ? 13.715  -5.884  -34.735 1.00 43.81 ? 595  HOH B O   1 
HETATM 3931 O O   . HOH P 6 .   ? -3.181  -14.681 -14.407 1.00 36.70 ? 596  HOH B O   1 
HETATM 3932 O O   . HOH P 6 .   ? 12.663  -30.707 -23.351 1.00 52.22 ? 597  HOH B O   1 
HETATM 3933 O O   . HOH P 6 .   ? -3.487  -24.288 -21.855 1.00 29.95 ? 598  HOH B O   1 
HETATM 3934 O O   . HOH P 6 .   ? -5.387  -26.221 -21.864 1.00 37.50 ? 599  HOH B O   1 
HETATM 3935 O O   . HOH P 6 .   ? 14.344  -37.553 -35.491 1.00 50.01 ? 600  HOH B O   1 
HETATM 3936 O O   . HOH P 6 .   ? -9.765  -26.007 -25.170 1.00 39.97 ? 601  HOH B O   1 
HETATM 3937 O O   . HOH P 6 .   ? 3.982   -27.665 -16.340 1.00 32.04 ? 602  HOH B O   1 
HETATM 3938 O O   . HOH P 6 .   ? -2.132  -28.297 -16.008 1.00 48.72 ? 603  HOH B O   1 
HETATM 3939 O O   . HOH P 6 .   ? 5.358   -33.616 -19.439 1.00 32.82 ? 604  HOH B O   1 
HETATM 3940 O O   . HOH P 6 .   ? 9.652   -33.250 -41.673 1.00 41.36 ? 605  HOH B O   1 
HETATM 3941 O O   . HOH P 6 .   ? -9.873  -29.260 -32.111 1.00 50.43 ? 606  HOH B O   1 
HETATM 3942 O O   . HOH P 6 .   ? 4.386   7.981   -27.325 1.00 46.89 ? 607  HOH B O   1 
HETATM 3943 O O   . HOH P 6 .   ? 9.203   -34.051 -20.919 1.00 45.86 ? 608  HOH B O   1 
HETATM 3944 O O   . HOH P 6 .   ? 15.837  0.670   -17.869 1.00 51.02 ? 609  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   ? 0.4227 0.5279 0.4245 -0.0152 -0.0007 0.0305  10  GLY A N   
2    C CA  . GLY A 8   ? 0.4062 0.5157 0.4125 -0.0183 -0.0050 0.0347  10  GLY A CA  
3    C C   . GLY A 8   ? 0.3820 0.4889 0.3928 -0.0135 -0.0056 0.0332  10  GLY A C   
4    O O   . GLY A 8   ? 0.3901 0.4980 0.4053 -0.0071 -0.0015 0.0308  10  GLY A O   
5    N N   . ALA A 9   ? 0.3537 0.4567 0.3625 -0.0170 -0.0106 0.0348  11  ALA A N   
6    C CA  . ALA A 9   ? 0.3351 0.4340 0.3460 -0.0136 -0.0117 0.0333  11  ALA A CA  
7    C C   . ALA A 9   ? 0.2982 0.3837 0.3014 -0.0107 -0.0113 0.0270  11  ALA A C   
8    O O   . ALA A 9   ? 0.3050 0.3836 0.3009 -0.0121 -0.0114 0.0245  11  ALA A O   
9    C CB  . ALA A 9   ? 0.3559 0.4542 0.3655 -0.0192 -0.0171 0.0368  11  ALA A CB  
10   N N   . ARG A 10  ? 0.2387 0.3206 0.2439 -0.0067 -0.0110 0.0249  12  ARG A N   
11   C CA  . ARG A 10  ? 0.1980 0.2684 0.1970 -0.0043 -0.0110 0.0197  12  ARG A CA  
12   C C   . ARG A 10  ? 0.1886 0.2502 0.1794 -0.0089 -0.0145 0.0185  12  ARG A C   
13   O O   . ARG A 10  ? 0.1951 0.2567 0.1842 -0.0133 -0.0176 0.0209  12  ARG A O   
14   C CB  . ARG A 10  ? 0.1797 0.2484 0.1817 -0.0013 -0.0113 0.0188  12  ARG A CB  
15   C CG  . ARG A 10  ? 0.1879 0.2467 0.1855 0.0015  -0.0107 0.0140  12  ARG A CG  
16   C CD  . ARG A 10  ? 0.1892 0.2474 0.1899 0.0037  -0.0112 0.0138  12  ARG A CD  
17   N NE  . ARG A 10  ? 0.1784 0.2439 0.1868 0.0075  -0.0092 0.0160  12  ARG A NE  
18   C CZ  . ARG A 10  ? 0.1901 0.2544 0.2003 0.0126  -0.0061 0.0137  12  ARG A CZ  
19   N NH1 . ARG A 10  ? 0.1707 0.2272 0.1754 0.0139  -0.0051 0.0096  12  ARG A NH1 
20   N NH2 . ARG A 10  ? 0.1820 0.2526 0.1996 0.0163  -0.0041 0.0157  12  ARG A NH2 
21   N N   . ILE A 11  ? 0.1643 0.2179 0.1498 -0.0078 -0.0142 0.0149  13  ILE A N   
22   C CA  . ILE A 11  ? 0.1557 0.2002 0.1343 -0.0109 -0.0172 0.0133  13  ILE A CA  
23   C C   . ILE A 11  ? 0.1671 0.2052 0.1448 -0.0089 -0.0175 0.0103  13  ILE A C   
24   O O   . ILE A 11  ? 0.1751 0.2106 0.1543 -0.0047 -0.0157 0.0074  13  ILE A O   
25   C CB  . ILE A 11  ? 0.1601 0.1991 0.1344 -0.0106 -0.0171 0.0112  13  ILE A CB  
26   C CG1 . ILE A 11  ? 0.1988 0.2443 0.1728 -0.0135 -0.0164 0.0143  13  ILE A CG1 
27   C CG2 . ILE A 11  ? 0.1620 0.1910 0.1303 -0.0131 -0.0204 0.0097  13  ILE A CG2 
28   C CD1 . ILE A 11  ? 0.2156 0.2564 0.1850 -0.0138 -0.0163 0.0128  13  ILE A CD1 
29   N N   . ILE A 12  ? 0.1610 0.1969 0.1360 -0.0123 -0.0197 0.0112  14  ILE A N   
30   C CA  . ILE A 12  ? 0.1482 0.1787 0.1218 -0.0111 -0.0196 0.0085  14  ILE A CA  
31   C C   . ILE A 12  ? 0.1662 0.1869 0.1325 -0.0138 -0.0214 0.0063  14  ILE A C   
32   O O   . ILE A 12  ? 0.1875 0.2066 0.1492 -0.0187 -0.0239 0.0084  14  ILE A O   
33   C CB  . ILE A 12  ? 0.1778 0.2132 0.1535 -0.0130 -0.0203 0.0113  14  ILE A CB  
34   C CG1 . ILE A 12  ? 0.1931 0.2379 0.1772 -0.0094 -0.0185 0.0136  14  ILE A CG1 
35   C CG2 . ILE A 12  ? 0.2023 0.2311 0.1741 -0.0135 -0.0204 0.0087  14  ILE A CG2 
36   C CD1 . ILE A 12  ? 0.2289 0.2804 0.2168 -0.0116 -0.0202 0.0179  14  ILE A CD1 
37   N N   . TYR A 13  ? 0.1486 0.1626 0.1139 -0.0109 -0.0202 0.0022  15  TYR A N   
38   C CA  . TYR A 13  ? 0.1355 0.1398 0.0947 -0.0125 -0.0211 -0.0004 15  TYR A CA  
39   C C   . TYR A 13  ? 0.1551 0.1563 0.1134 -0.0114 -0.0192 -0.0033 15  TYR A C   
40   O O   . TYR A 13  ? 0.1581 0.1621 0.1213 -0.0077 -0.0171 -0.0047 15  TYR A O   
41   C CB  . TYR A 13  ? 0.1384 0.1378 0.0984 -0.0096 -0.0213 -0.0027 15  TYR A CB  
42   C CG  . TYR A 13  ? 0.1564 0.1574 0.1160 -0.0110 -0.0231 -0.0003 15  TYR A CG  
43   C CD1 . TYR A 13  ? 0.1680 0.1658 0.1221 -0.0156 -0.0260 0.0017  15  TYR A CD1 
44   C CD2 . TYR A 13  ? 0.1571 0.1620 0.1208 -0.0081 -0.0222 -0.0001 15  TYR A CD2 
45   C CE1 . TYR A 13  ? 0.1724 0.1713 0.1255 -0.0174 -0.0278 0.0039  15  TYR A CE1 
46   C CE2 . TYR A 13  ? 0.1605 0.1664 0.1226 -0.0099 -0.0236 0.0019  15  TYR A CE2 
47   C CZ  . TYR A 13  ? 0.1720 0.1751 0.1290 -0.0146 -0.0264 0.0040  15  TYR A CZ  
48   O OH  . TYR A 13  ? 0.1855 0.1896 0.1405 -0.0171 -0.0280 0.0062  15  TYR A OH  
49   N N   . ASP A 14  ? 0.1689 0.1641 0.1203 -0.0151 -0.0198 -0.0041 16  ASP A N   
50   C CA  . ASP A 14  ? 0.1752 0.1669 0.1245 -0.0145 -0.0173 -0.0072 16  ASP A CA  
51   C C   . ASP A 14  ? 0.1804 0.1650 0.1299 -0.0108 -0.0151 -0.0119 16  ASP A C   
52   O O   . ASP A 14  ? 0.1992 0.1808 0.1500 -0.0090 -0.0163 -0.0124 16  ASP A O   
53   C CB  . ASP A 14  ? 0.2140 0.2022 0.1549 -0.0204 -0.0185 -0.0062 16  ASP A CB  
54   C CG  . ASP A 14  ? 0.2950 0.2728 0.2263 -0.0241 -0.0201 -0.0074 16  ASP A CG  
55   O OD1 . ASP A 14  ? 0.2484 0.2202 0.1796 -0.0216 -0.0199 -0.0099 16  ASP A OD1 
56   O OD2 . ASP A 14  ? 0.3224 0.2973 0.2458 -0.0300 -0.0219 -0.0057 16  ASP A OD2 
57   N N   . ARG A 15  ? 0.1888 0.1715 0.1378 -0.0096 -0.0119 -0.0150 17  ARG A N   
58   C CA  . ARG A 15  ? 0.1909 0.1691 0.1426 -0.0054 -0.0092 -0.0192 17  ARG A CA  
59   C C   . ARG A 15  ? 0.2012 0.1694 0.1477 -0.0057 -0.0099 -0.0213 17  ARG A C   
60   O O   . ARG A 15  ? 0.1934 0.1591 0.1445 -0.0019 -0.0103 -0.0225 17  ARG A O   
61   C CB  . ARG A 15  ? 0.1956 0.1738 0.1462 -0.0053 -0.0051 -0.0220 17  ARG A CB  
62   C CG  . ARG A 15  ? 0.2105 0.1864 0.1662 -0.0005 -0.0018 -0.0259 17  ARG A CG  
63   C CD  . ARG A 15  ? 0.2927 0.2681 0.2455 -0.0014 0.0028  -0.0288 17  ARG A CD  
64   N NE  . ARG A 15  ? 0.3390 0.3157 0.2994 0.0035  0.0065  -0.0319 17  ARG A NE  
65   C CZ  . ARG A 15  ? 0.4323 0.4029 0.3932 0.0065  0.0095  -0.0358 17  ARG A CZ  
66   N NH1 . ARG A 15  ? 0.3987 0.3593 0.3511 0.0049  0.0092  -0.0377 17  ARG A NH1 
67   N NH2 . ARG A 15  ? 0.4642 0.4385 0.4344 0.0110  0.0127  -0.0377 17  ARG A NH2 
68   N N   . ALA A 16  ? 0.2161 0.1777 0.1525 -0.0106 -0.0107 -0.0215 18  ALA A N   
69   C CA  . ALA A 16  ? 0.2530 0.2029 0.1828 -0.0111 -0.0115 -0.0238 18  ALA A CA  
70   C C   . ALA A 16  ? 0.2357 0.1848 0.1676 -0.0108 -0.0158 -0.0212 18  ALA A C   
71   O O   . ALA A 16  ? 0.2292 0.1707 0.1617 -0.0080 -0.0162 -0.0234 18  ALA A O   
72   C CB  . ALA A 16  ? 0.2682 0.2107 0.1853 -0.0174 -0.0121 -0.0240 18  ALA A CB  
73   N N   . PHE A 17  ? 0.2073 0.1641 0.1407 -0.0136 -0.0188 -0.0165 19  PHE A N   
74   C CA  . PHE A 17  ? 0.2148 0.1719 0.1495 -0.0142 -0.0227 -0.0136 19  PHE A CA  
75   C C   . PHE A 17  ? 0.2033 0.1622 0.1467 -0.0086 -0.0221 -0.0148 19  PHE A C   
76   O O   . PHE A 17  ? 0.2138 0.1662 0.1569 -0.0075 -0.0244 -0.0151 19  PHE A O   
77   C CB  . PHE A 17  ? 0.2180 0.1852 0.1539 -0.0179 -0.0248 -0.0085 19  PHE A CB  
78   C CG  . PHE A 17  ? 0.2445 0.2118 0.1794 -0.0203 -0.0285 -0.0053 19  PHE A CG  
79   C CD1 . PHE A 17  ? 0.2550 0.2258 0.1959 -0.0171 -0.0289 -0.0047 19  PHE A CD1 
80   C CD2 . PHE A 17  ? 0.2870 0.2503 0.2142 -0.0263 -0.0319 -0.0027 19  PHE A CD2 
81   C CE1 . PHE A 17  ? 0.2777 0.2484 0.2167 -0.0200 -0.0322 -0.0016 19  PHE A CE1 
82   C CE2 . PHE A 17  ? 0.2955 0.2590 0.2214 -0.0291 -0.0353 0.0004  19  PHE A CE2 
83   C CZ  . PHE A 17  ? 0.2817 0.2492 0.2135 -0.0259 -0.0352 0.0009  19  PHE A CZ  
84   N N   . LEU A 18  ? 0.1822 0.1492 0.1329 -0.0053 -0.0195 -0.0151 20  LEU A N   
85   C CA  . LEU A 18  ? 0.1746 0.1432 0.1332 -0.0005 -0.0194 -0.0158 20  LEU A CA  
86   C C   . LEU A 18  ? 0.1861 0.1466 0.1464 0.0031  -0.0185 -0.0194 20  LEU A C   
87   O O   . LEU A 18  ? 0.1915 0.1492 0.1555 0.0052  -0.0208 -0.0190 20  LEU A O   
88   C CB  . LEU A 18  ? 0.1655 0.1432 0.1306 0.0019  -0.0170 -0.0156 20  LEU A CB  
89   C CG  . LEU A 18  ? 0.1516 0.1369 0.1165 -0.0004 -0.0180 -0.0120 20  LEU A CG  
90   C CD1 . LEU A 18  ? 0.1417 0.1341 0.1117 0.0017  -0.0157 -0.0121 20  LEU A CD1 
91   C CD2 . LEU A 18  ? 0.1529 0.1390 0.1188 -0.0006 -0.0208 -0.0097 20  LEU A CD2 
92   N N   . MET A 19  ? 0.2010 0.1580 0.1589 0.0036  -0.0150 -0.0227 21  MET A N   
93   C CA  . MET A 19  ? 0.2279 0.1777 0.1883 0.0078  -0.0128 -0.0266 21  MET A CA  
94   C C   . MET A 19  ? 0.2798 0.2183 0.2352 0.0072  -0.0161 -0.0269 21  MET A C   
95   O O   . MET A 19  ? 0.2952 0.2292 0.2563 0.0115  -0.0168 -0.0282 21  MET A O   
96   C CB  . MET A 19  ? 0.2506 0.1985 0.2071 0.0076  -0.0076 -0.0304 21  MET A CB  
97   C CG  . MET A 19  ? 0.2539 0.2120 0.2165 0.0089  -0.0043 -0.0305 21  MET A CG  
98   S SD  . MET A 19  ? 0.2862 0.2517 0.2631 0.0147  -0.0037 -0.0302 21  MET A SD  
99   C CE  . MET A 19  ? 0.4171 0.3897 0.3958 0.0146  0.0013  -0.0317 21  MET A CE  
100  N N   . ALA A 20  ? 0.2820 0.2161 0.2272 0.0016  -0.0186 -0.0253 22  ALA A N   
101  C CA  . ALA A 20  ? 0.3064 0.2292 0.2448 -0.0006 -0.0226 -0.0248 22  ALA A CA  
102  C C   . ALA A 20  ? 0.3090 0.2333 0.2522 0.0001  -0.0274 -0.0214 22  ALA A C   
103  O O   . ALA A 20  ? 0.3237 0.2382 0.2652 0.0009  -0.0304 -0.0218 22  ALA A O   
104  C CB  . ALA A 20  ? 0.3165 0.2364 0.2432 -0.0077 -0.0246 -0.0229 22  ALA A CB  
105  N N   . CYS A 21  ? 0.2774 0.2128 0.2260 -0.0003 -0.0281 -0.0183 23  CYS A N   
106  C CA  . CYS A 21  ? 0.2774 0.2142 0.2295 -0.0002 -0.0323 -0.0152 23  CYS A CA  
107  C C   . CYS A 21  ? 0.2717 0.2066 0.2329 0.0054  -0.0327 -0.0164 23  CYS A C   
108  O O   . CYS A 21  ? 0.2864 0.2201 0.2492 0.0050  -0.0369 -0.0138 23  CYS A O   
109  C CB  . CYS A 21  ? 0.2727 0.2208 0.2265 -0.0025 -0.0324 -0.0118 23  CYS A CB  
110  S SG  . CYS A 21  ? 0.2812 0.2333 0.2268 -0.0093 -0.0333 -0.0086 23  CYS A SG  
111  N N   . ARG A 22  ? 0.2636 0.1990 0.2307 0.0102  -0.0286 -0.0199 24  ARG A N   
112  C CA  . ARG A 22  ? 0.2693 0.2048 0.2467 0.0155  -0.0290 -0.0205 24  ARG A CA  
113  C C   . ARG A 22  ? 0.3297 0.2531 0.3066 0.0172  -0.0323 -0.0211 24  ARG A C   
114  O O   . ARG A 22  ? 0.3310 0.2529 0.3128 0.0183  -0.0368 -0.0185 24  ARG A O   
115  C CB  . ARG A 22  ? 0.2516 0.1920 0.2361 0.0199  -0.0232 -0.0239 24  ARG A CB  
116  C CG  . ARG A 22  ? 0.2357 0.1796 0.2326 0.0247  -0.0241 -0.0232 24  ARG A CG  
117  C CD  . ARG A 22  ? 0.2538 0.2031 0.2581 0.0286  -0.0183 -0.0263 24  ARG A CD  
118  N NE  . ARG A 22  ? 0.2726 0.2276 0.2898 0.0325  -0.0195 -0.0246 24  ARG A NE  
119  C CZ  . ARG A 22  ? 0.3229 0.2831 0.3497 0.0367  -0.0152 -0.0266 24  ARG A CZ  
120  N NH1 . ARG A 22  ? 0.3540 0.3138 0.3782 0.0377  -0.0088 -0.0308 24  ARG A NH1 
121  N NH2 . ARG A 22  ? 0.3384 0.3043 0.3771 0.0394  -0.0173 -0.0242 24  ARG A NH2 
122  N N   . GLY A 23  ? 0.3720 0.2864 0.3424 0.0172  -0.0302 -0.0243 25  GLY A N   
123  C CA  . GLY A 23  ? 0.4318 0.3327 0.4005 0.0191  -0.0330 -0.0255 25  GLY A CA  
124  C C   . GLY A 23  ? 0.4789 0.3709 0.4352 0.0129  -0.0381 -0.0232 25  GLY A C   
125  O O   . GLY A 23  ? 0.5053 0.3857 0.4598 0.0136  -0.0422 -0.0229 25  GLY A O   
126  N N   . GLY A 24  ? 0.4865 0.3839 0.4348 0.0068  -0.0379 -0.0213 26  GLY A N   
127  C CA  . GLY A 24  ? 0.5026 0.3942 0.4396 -0.0001 -0.0426 -0.0184 26  GLY A CA  
128  C C   . GLY A 24  ? 0.4948 0.3977 0.4312 -0.0050 -0.0447 -0.0137 26  GLY A C   
129  O O   . GLY A 24  ? 0.4923 0.3970 0.4208 -0.0109 -0.0455 -0.0116 26  GLY A O   
130  N N   . GLY A 25  ? 0.4988 0.4092 0.4435 -0.0026 -0.0455 -0.0118 27  GLY A N   
131  C CA  . GLY A 25  ? 0.5038 0.4245 0.4482 -0.0065 -0.0467 -0.0079 27  GLY A CA  
132  C C   . GLY A 25  ? 0.5103 0.4260 0.4501 -0.0108 -0.0528 -0.0040 27  GLY A C   
133  O O   . GLY A 25  ? 0.5256 0.4296 0.4631 -0.0105 -0.0568 -0.0041 27  GLY A O   
134  N N   . GLY A 26  ? 0.4866 0.4110 0.4250 -0.0147 -0.0534 -0.0006 28  GLY A N   
135  C CA  . GLY A 26  ? 0.4838 0.4054 0.4175 -0.0195 -0.0587 0.0034  28  GLY A CA  
136  C C   . GLY A 26  ? 0.4833 0.3993 0.4070 -0.0260 -0.0619 0.0056  28  GLY A C   
137  O O   . GLY A 26  ? 0.5179 0.4292 0.4367 -0.0304 -0.0669 0.0090  28  GLY A O   
138  N N   . GLU A 27  ? 0.4593 0.3754 0.3793 -0.0273 -0.0593 0.0042  29  GLU A N   
139  C CA  . GLU A 27  ? 0.4712 0.3823 0.3813 -0.0343 -0.0627 0.0067  29  GLU A CA  
140  C C   . GLU A 27  ? 0.4633 0.3875 0.3722 -0.0390 -0.0602 0.0095  29  GLU A C   
141  O O   . GLU A 27  ? 0.4654 0.3876 0.3674 -0.0443 -0.0616 0.0111  29  GLU A O   
142  C CB  . GLU A 27  ? 0.5240 0.4217 0.4290 -0.0331 -0.0630 0.0032  29  GLU A CB  
143  C CG  . GLU A 27  ? 0.6233 0.5053 0.5264 -0.0312 -0.0675 0.0022  29  GLU A CG  
144  C CD  . GLU A 27  ? 0.7102 0.5808 0.6126 -0.0262 -0.0651 -0.0031 29  GLU A CD  
145  O OE1 . GLU A 27  ? 0.7551 0.6188 0.6635 -0.0199 -0.0655 -0.0056 29  GLU A OE1 
146  O OE2 . GLU A 27  ? 0.7575 0.6261 0.6533 -0.0286 -0.0628 -0.0048 29  GLU A OE2 
147  N N   . ASN A 28  ? 0.4318 0.3694 0.3474 -0.0370 -0.0566 0.0103  30  ASN A N   
148  C CA  . ASN A 28  ? 0.4352 0.3858 0.3511 -0.0410 -0.0544 0.0134  30  ASN A CA  
149  C C   . ASN A 28  ? 0.4553 0.4061 0.3646 -0.0487 -0.0585 0.0183  30  ASN A C   
150  O O   . ASN A 28  ? 0.4555 0.3984 0.3609 -0.0506 -0.0627 0.0194  30  ASN A O   
151  C CB  . ASN A 28  ? 0.4401 0.4029 0.3637 -0.0373 -0.0501 0.0132  30  ASN A CB  
152  C CG  . ASN A 28  ? 0.4593 0.4357 0.3859 -0.0388 -0.0464 0.0152  30  ASN A CG  
153  O OD1 . ASN A 28  ? 0.4886 0.4664 0.4132 -0.0416 -0.0466 0.0164  30  ASN A OD1 
154  N ND2 . ASN A 28  ? 0.4660 0.4523 0.3974 -0.0368 -0.0430 0.0158  30  ASN A ND2 
155  N N   . LEU A 29  ? 0.4652 0.4251 0.3735 -0.0533 -0.0576 0.0214  31  LEU A N   
156  C CA  . LEU A 29  ? 0.4764 0.4390 0.3791 -0.0615 -0.0610 0.0266  31  LEU A CA  
157  C C   . LEU A 29  ? 0.4800 0.4530 0.3854 -0.0627 -0.0593 0.0292  31  LEU A C   
158  O O   . LEU A 29  ? 0.4752 0.4507 0.3758 -0.0696 -0.0619 0.0336  31  LEU A O   
159  C CB  . LEU A 29  ? 0.4857 0.4560 0.3878 -0.0661 -0.0606 0.0296  31  LEU A CB  
160  C CG  . LEU A 29  ? 0.5344 0.4946 0.4315 -0.0667 -0.0623 0.0276  31  LEU A CG  
161  C CD1 . LEU A 29  ? 0.5513 0.5207 0.4483 -0.0721 -0.0625 0.0316  31  LEU A CD1 
162  C CD2 . LEU A 29  ? 0.5601 0.5025 0.4463 -0.0708 -0.0684 0.0275  31  LEU A CD2 
163  N N   . TYR A 30  ? 0.4731 0.4515 0.3851 -0.0565 -0.0549 0.0265  32  TYR A N   
164  C CA  . TYR A 30  ? 0.4719 0.4566 0.3842 -0.0575 -0.0533 0.0280  32  TYR A CA  
165  C C   . TYR A 30  ? 0.4552 0.4353 0.3706 -0.0513 -0.0522 0.0243  32  TYR A C   
166  O O   . TYR A 30  ? 0.4608 0.4330 0.3786 -0.0464 -0.0530 0.0209  32  TYR A O   
167  C CB  . TYR A 30  ? 0.4755 0.4770 0.3925 -0.0588 -0.0481 0.0304  32  TYR A CB  
168  C CG  . TYR A 30  ? 0.4899 0.4995 0.4156 -0.0517 -0.0422 0.0275  32  TYR A CG  
169  C CD1 . TYR A 30  ? 0.5014 0.5108 0.4308 -0.0489 -0.0416 0.0259  32  TYR A CD1 
170  C CD2 . TYR A 30  ? 0.5014 0.5185 0.4308 -0.0484 -0.0374 0.0264  32  TYR A CD2 
171  C CE1 . TYR A 30  ? 0.5126 0.5292 0.4496 -0.0430 -0.0368 0.0237  32  TYR A CE1 
172  C CE2 . TYR A 30  ? 0.5087 0.5321 0.4455 -0.0421 -0.0324 0.0238  32  TYR A CE2 
173  C CZ  . TYR A 30  ? 0.5204 0.5438 0.4614 -0.0394 -0.0324 0.0227  32  TYR A CZ  
174  O OH  . TYR A 30  ? 0.5343 0.5639 0.4824 -0.0337 -0.0279 0.0206  32  TYR A OH  
175  N N   . PHE A 31  ? 0.4266 0.4112 0.3416 -0.0517 -0.0504 0.0249  33  PHE A N   
176  C CA  . PHE A 31  ? 0.4153 0.3961 0.3326 -0.0467 -0.0496 0.0220  33  PHE A CA  
177  C C   . PHE A 31  ? 0.4291 0.3957 0.3436 -0.0466 -0.0559 0.0216  33  PHE A C   
178  O O   . PHE A 31  ? 0.4252 0.3871 0.3439 -0.0413 -0.0562 0.0189  33  PHE A O   
179  C CB  . PHE A 31  ? 0.4042 0.3895 0.3295 -0.0395 -0.0448 0.0183  33  PHE A CB  
180  C CG  . PHE A 31  ? 0.4148 0.4022 0.3426 -0.0355 -0.0418 0.0161  33  PHE A CG  
181  C CD1 . PHE A 31  ? 0.4239 0.4050 0.3471 -0.0373 -0.0449 0.0168  33  PHE A CD1 
182  C CD2 . PHE A 31  ? 0.4091 0.4037 0.3430 -0.0304 -0.0365 0.0138  33  PHE A CD2 
183  C CE1 . PHE A 31  ? 0.4264 0.4084 0.3507 -0.0344 -0.0426 0.0150  33  PHE A CE1 
184  C CE2 . PHE A 31  ? 0.4048 0.3998 0.3398 -0.0271 -0.0342 0.0118  33  PHE A CE2 
185  C CZ  . PHE A 31  ? 0.4222 0.4108 0.3520 -0.0294 -0.0372 0.0124  33  PHE A CZ  
186  N N   . GLN A 32  ? 0.4250 0.3846 0.3325 -0.0527 -0.0614 0.0247  34  GLN A N   
187  C CA  . GLN A 32  ? 0.4188 0.3638 0.3238 -0.0525 -0.0679 0.0246  34  GLN A CA  
188  C C   . GLN A 32  ? 0.4144 0.3536 0.3256 -0.0456 -0.0672 0.0206  34  GLN A C   
189  O O   . GLN A 32  ? 0.4469 0.3773 0.3608 -0.0419 -0.0702 0.0192  34  GLN A O   
190  C CB  . GLN A 32  ? 0.4240 0.3649 0.3271 -0.0536 -0.0711 0.0259  34  GLN A CB  
191  C CG  . GLN A 32  ? 0.4664 0.4117 0.3613 -0.0616 -0.0717 0.0299  34  GLN A CG  
192  C CD  . GLN A 32  ? 0.4873 0.4259 0.3775 -0.0645 -0.0764 0.0319  34  GLN A CD  
193  O OE1 . GLN A 32  ? 0.4870 0.4173 0.3807 -0.0606 -0.0800 0.0308  34  GLN A OE1 
194  N NE2 . GLN A 32  ? 0.5243 0.4666 0.4066 -0.0717 -0.0764 0.0351  34  GLN A NE2 
195  N N   . GLY A 33  ? 0.3854 0.3300 0.2987 -0.0442 -0.0633 0.0190  35  GLY A N   
196  C CA  . GLY A 33  ? 0.3625 0.3023 0.2798 -0.0388 -0.0618 0.0152  35  GLY A CA  
197  C C   . GLY A 33  ? 0.3535 0.3009 0.2792 -0.0322 -0.0561 0.0118  35  GLY A C   
198  O O   . GLY A 33  ? 0.3433 0.2886 0.2716 -0.0286 -0.0540 0.0087  35  GLY A O   
199  N N   . LYS A 34  ? 0.3194 0.2749 0.2484 -0.0309 -0.0536 0.0121  36  LYS A N   
200  C CA  . LYS A 34  ? 0.2899 0.2517 0.2263 -0.0250 -0.0487 0.0090  36  LYS A CA  
201  C C   . LYS A 34  ? 0.2739 0.2461 0.2118 -0.0251 -0.0439 0.0090  36  LYS A C   
202  O O   . LYS A 34  ? 0.3042 0.2826 0.2392 -0.0294 -0.0433 0.0118  36  LYS A O   
203  C CB  . LYS A 34  ? 0.2999 0.2636 0.2386 -0.0232 -0.0485 0.0090  36  LYS A CB  
204  C CG  . LYS A 34  ? 0.3706 0.3244 0.3107 -0.0216 -0.0534 0.0089  36  LYS A CG  
205  C CD  . LYS A 34  ? 0.4212 0.3765 0.3631 -0.0205 -0.0536 0.0092  36  LYS A CD  
206  C CE  . LYS A 34  ? 0.4964 0.4425 0.4388 -0.0208 -0.0599 0.0107  36  LYS A CE  
207  N NZ  . LYS A 34  ? 0.5752 0.5149 0.5240 -0.0161 -0.0614 0.0088  36  LYS A NZ  
208  N N   . HIS A 35  ? 0.2066 0.1810 0.1496 -0.0206 -0.0406 0.0061  37  HIS A N   
209  C CA  . HIS A 35  ? 0.1894 0.1728 0.1348 -0.0203 -0.0367 0.0062  37  HIS A CA  
210  C C   . HIS A 35  ? 0.1800 0.1712 0.1302 -0.0169 -0.0330 0.0055  37  HIS A C   
211  O O   . HIS A 35  ? 0.1632 0.1523 0.1173 -0.0125 -0.0320 0.0029  37  HIS A O   
212  C CB  . HIS A 35  ? 0.1880 0.1679 0.1350 -0.0177 -0.0355 0.0034  37  HIS A CB  
213  C CG  . HIS A 35  ? 0.2231 0.1943 0.1640 -0.0211 -0.0386 0.0036  37  HIS A CG  
214  N ND1 . HIS A 35  ? 0.2386 0.1987 0.1775 -0.0201 -0.0416 0.0021  37  HIS A ND1 
215  C CD2 . HIS A 35  ? 0.2450 0.2170 0.1813 -0.0256 -0.0394 0.0054  37  HIS A CD2 
216  C CE1 . HIS A 35  ? 0.2647 0.2177 0.1969 -0.0238 -0.0439 0.0025  37  HIS A CE1 
217  N NE2 . HIS A 35  ? 0.2695 0.2291 0.1994 -0.0277 -0.0429 0.0047  37  HIS A NE2 
218  N N   . PRO A 36  ? 0.1823 0.1817 0.1322 -0.0188 -0.0309 0.0077  38  PRO A N   
219  C CA  . PRO A 36  ? 0.1644 0.1695 0.1178 -0.0152 -0.0271 0.0066  38  PRO A CA  
220  C C   . PRO A 36  ? 0.1607 0.1703 0.1197 -0.0113 -0.0239 0.0049  38  PRO A C   
221  O O   . PRO A 36  ? 0.1466 0.1589 0.1067 -0.0123 -0.0237 0.0058  38  PRO A O   
222  C CB  . PRO A 36  ? 0.1901 0.2028 0.1417 -0.0183 -0.0251 0.0093  38  PRO A CB  
223  C CG  . PRO A 36  ? 0.2215 0.2368 0.1720 -0.0225 -0.0268 0.0120  38  PRO A CG  
224  C CD  . PRO A 36  ? 0.1956 0.2001 0.1423 -0.0240 -0.0314 0.0113  38  PRO A CD  
225  N N   . LEU A 37  ? 0.1465 0.1561 0.1081 -0.0074 -0.0219 0.0029  39  LEU A N   
226  C CA  . LEU A 37  ? 0.1432 0.1570 0.1098 -0.0038 -0.0191 0.0016  39  LEU A CA  
227  C C   . LEU A 37  ? 0.1516 0.1736 0.1201 -0.0030 -0.0156 0.0029  39  LEU A C   
228  O O   . LEU A 37  ? 0.1668 0.1910 0.1327 -0.0045 -0.0146 0.0040  39  LEU A O   
229  C CB  . LEU A 37  ? 0.1308 0.1402 0.0991 -0.0003 -0.0190 -0.0010 39  LEU A CB  
230  C CG  . LEU A 37  ? 0.1492 0.1513 0.1179 0.0002  -0.0219 -0.0026 39  LEU A CG  
231  C CD1 . LEU A 37  ? 0.1621 0.1621 0.1336 0.0032  -0.0218 -0.0043 39  LEU A CD1 
232  C CD2 . LEU A 37  ? 0.1264 0.1281 0.0965 0.0002  -0.0216 -0.0034 39  LEU A CD2 
233  N N   . GLN A 38  ? 0.1405 0.1672 0.1136 -0.0007 -0.0136 0.0029  40  GLN A N   
234  C CA  . GLN A 38  ? 0.1450 0.1791 0.1216 0.0015  -0.0100 0.0038  40  GLN A CA  
235  C C   . GLN A 38  ? 0.1417 0.1731 0.1164 0.0042  -0.0078 0.0017  40  GLN A C   
236  O O   . GLN A 38  ? 0.1360 0.1718 0.1105 0.0048  -0.0047 0.0023  40  GLN A O   
237  C CB  . GLN A 38  ? 0.1315 0.1693 0.1133 0.0035  -0.0093 0.0043  40  GLN A CB  
238  C CG  . GLN A 38  ? 0.1525 0.1973 0.1392 0.0066  -0.0059 0.0053  40  GLN A CG  
239  C CD  . GLN A 38  ? 0.1743 0.2279 0.1635 0.0046  -0.0046 0.0087  40  GLN A CD  
240  O OE1 . GLN A 38  ? 0.1850 0.2403 0.1728 0.0002  -0.0070 0.0110  40  GLN A OE1 
241  N NE2 . GLN A 38  ? 0.2176 0.2767 0.2104 0.0077  -0.0007 0.0090  40  GLN A NE2 
242  N N   . ASN A 39  ? 0.1316 0.1562 0.1051 0.0058  -0.0093 -0.0007 41  ASN A N   
243  C CA  . ASN A 39  ? 0.1205 0.1410 0.0915 0.0078  -0.0081 -0.0026 41  ASN A CA  
244  C C   . ASN A 39  ? 0.1258 0.1389 0.0925 0.0060  -0.0114 -0.0034 41  ASN A C   
245  O O   . ASN A 39  ? 0.1329 0.1434 0.1006 0.0047  -0.0144 -0.0032 41  ASN A O   
246  C CB  . ASN A 39  ? 0.1546 0.1741 0.1288 0.0114  -0.0072 -0.0041 41  ASN A CB  
247  C CG  . ASN A 39  ? 0.1788 0.2043 0.1568 0.0139  -0.0040 -0.0033 41  ASN A CG  
248  O OD1 . ASN A 39  ? 0.2292 0.2558 0.2058 0.0154  -0.0010 -0.0037 41  ASN A OD1 
249  N ND2 . ASN A 39  ? 0.1485 0.1782 0.1315 0.0143  -0.0045 -0.0019 41  ASN A ND2 
250  N N   . ARG A 40  ? 0.1385 0.1478 0.1005 0.0058  -0.0108 -0.0043 42  ARG A N   
251  C CA  . ARG A 40  ? 0.1358 0.1377 0.0943 0.0043  -0.0144 -0.0048 42  ARG A CA  
252  C C   . ARG A 40  ? 0.1484 0.1474 0.1096 0.0070  -0.0150 -0.0063 42  ARG A C   
253  O O   . ARG A 40  ? 0.1275 0.1276 0.0891 0.0095  -0.0122 -0.0074 42  ARG A O   
254  C CB  . ARG A 40  ? 0.1587 0.1574 0.1091 0.0018  -0.0137 -0.0048 42  ARG A CB  
255  C CG  . ARG A 40  ? 0.1814 0.1721 0.1268 -0.0009 -0.0180 -0.0045 42  ARG A CG  
256  C CD  . ARG A 40  ? 0.2626 0.2503 0.1980 -0.0045 -0.0169 -0.0042 42  ARG A CD  
257  N NE  . ARG A 40  ? 0.2635 0.2558 0.1984 -0.0070 -0.0162 -0.0025 42  ARG A NE  
258  C CZ  . ARG A 40  ? 0.2487 0.2476 0.1827 -0.0070 -0.0114 -0.0023 42  ARG A CZ  
259  N NH1 . ARG A 40  ? 0.2682 0.2692 0.2013 -0.0041 -0.0060 -0.0043 42  ARG A NH1 
260  N NH2 . ARG A 40  ? 0.2235 0.2268 0.1580 -0.0099 -0.0119 -0.0001 42  ARG A NH2 
261  N N   . TRP A 41  ? 0.1404 0.1358 0.1037 0.0064  -0.0188 -0.0062 43  TRP A N   
262  C CA  . TRP A 41  ? 0.1351 0.1290 0.1022 0.0083  -0.0197 -0.0071 43  TRP A CA  
263  C C   . TRP A 41  ? 0.1362 0.1243 0.1012 0.0066  -0.0237 -0.0065 43  TRP A C   
264  O O   . TRP A 41  ? 0.1399 0.1253 0.1033 0.0043  -0.0267 -0.0052 43  TRP A O   
265  C CB  . TRP A 41  ? 0.1262 0.1229 0.1001 0.0097  -0.0200 -0.0073 43  TRP A CB  
266  C CG  . TRP A 41  ? 0.1178 0.1198 0.0934 0.0106  -0.0170 -0.0074 43  TRP A CG  
267  C CD1 . TRP A 41  ? 0.1261 0.1305 0.1010 0.0092  -0.0166 -0.0065 43  TRP A CD1 
268  C CD2 . TRP A 41  ? 0.1135 0.1187 0.0919 0.0127  -0.0147 -0.0080 43  TRP A CD2 
269  N NE1 . TRP A 41  ? 0.1172 0.1265 0.0941 0.0101  -0.0143 -0.0062 43  TRP A NE1 
270  C CE2 . TRP A 41  ? 0.1199 0.1297 0.0992 0.0123  -0.0131 -0.0071 43  TRP A CE2 
271  C CE3 . TRP A 41  ? 0.1214 0.1257 0.1009 0.0143  -0.0142 -0.0088 43  TRP A CE3 
272  C CZ2 . TRP A 41  ? 0.1104 0.1240 0.0924 0.0136  -0.0113 -0.0069 43  TRP A CZ2 
273  C CZ3 . TRP A 41  ? 0.1295 0.1370 0.1112 0.0156  -0.0123 -0.0087 43  TRP A CZ3 
274  C CH2 . TRP A 41  ? 0.1097 0.1217 0.0927 0.0154  -0.0110 -0.0078 43  TRP A CH2 
275  N N   . ALA A 42  ? 0.1434 0.1295 0.1086 0.0074  -0.0240 -0.0070 44  ALA A N   
276  C CA  . ALA A 42  ? 0.1565 0.1377 0.1207 0.0055  -0.0283 -0.0059 44  ALA A CA  
277  C C   . ALA A 42  ? 0.1544 0.1379 0.1268 0.0071  -0.0296 -0.0058 44  ALA A C   
278  O O   . ALA A 42  ? 0.1495 0.1355 0.1242 0.0090  -0.0271 -0.0069 44  ALA A O   
279  C CB  . ALA A 42  ? 0.1629 0.1387 0.1183 0.0040  -0.0279 -0.0065 44  ALA A CB  
280  N N   . LEU A 43  ? 0.1422 0.1250 0.1196 0.0063  -0.0335 -0.0041 45  LEU A N   
281  C CA  . LEU A 43  ? 0.1511 0.1367 0.1370 0.0074  -0.0350 -0.0035 45  LEU A CA  
282  C C   . LEU A 43  ? 0.1630 0.1450 0.1472 0.0048  -0.0391 -0.0015 45  LEU A C   
283  O O   . LEU A 43  ? 0.1850 0.1623 0.1653 0.0019  -0.0433 0.0004  45  LEU A O   
284  C CB  . LEU A 43  ? 0.1520 0.1396 0.1462 0.0086  -0.0368 -0.0027 45  LEU A CB  
285  C CG  . LEU A 43  ? 0.1674 0.1592 0.1724 0.0103  -0.0377 -0.0020 45  LEU A CG  
286  C CD1 . LEU A 43  ? 0.1531 0.1501 0.1611 0.0124  -0.0329 -0.0041 45  LEU A CD1 
287  C CD2 . LEU A 43  ? 0.1752 0.1678 0.1882 0.0120  -0.0394 -0.0013 45  LEU A CD2 
288  N N   . TRP A 44  ? 0.1611 0.1448 0.1474 0.0053  -0.0383 -0.0018 46  TRP A N   
289  C CA  . TRP A 44  ? 0.1774 0.1577 0.1616 0.0024  -0.0421 0.0002  46  TRP A CA  
290  C C   . TRP A 44  ? 0.1759 0.1624 0.1719 0.0030  -0.0437 0.0019  46  TRP A C   
291  O O   . TRP A 44  ? 0.1464 0.1392 0.1498 0.0059  -0.0402 0.0006  46  TRP A O   
292  C CB  . TRP A 44  ? 0.1835 0.1601 0.1595 0.0020  -0.0397 -0.0015 46  TRP A CB  
293  C CG  . TRP A 44  ? 0.2093 0.1811 0.1750 0.0023  -0.0368 -0.0036 46  TRP A CG  
294  C CD1 . TRP A 44  ? 0.2212 0.1962 0.1868 0.0053  -0.0319 -0.0057 46  TRP A CD1 
295  C CD2 . TRP A 44  ? 0.2511 0.2145 0.2050 -0.0007 -0.0382 -0.0036 46  TRP A CD2 
296  N NE1 . TRP A 44  ? 0.2324 0.2027 0.1884 0.0047  -0.0299 -0.0070 46  TRP A NE1 
297  C CE2 . TRP A 44  ? 0.2693 0.2319 0.2173 0.0011  -0.0333 -0.0061 46  TRP A CE2 
298  C CE3 . TRP A 44  ? 0.3004 0.2568 0.2480 -0.0052 -0.0431 -0.0017 46  TRP A CE3 
299  C CZ2 . TRP A 44  ? 0.3246 0.2800 0.2606 -0.0011 -0.0325 -0.0071 46  TRP A CZ2 
300  C CZ3 . TRP A 44  ? 0.3469 0.2949 0.2811 -0.0078 -0.0427 -0.0027 46  TRP A CZ3 
301  C CH2 . TRP A 44  ? 0.3478 0.2952 0.2761 -0.0056 -0.0370 -0.0057 46  TRP A CH2 
302  N N   . PHE A 45  ? 0.1806 0.1653 0.1780 -0.0001 -0.0490 0.0050  47  PHE A N   
303  C CA  . PHE A 45  ? 0.1871 0.1781 0.1956 -0.0002 -0.0509 0.0074  47  PHE A CA  
304  C C   . PHE A 45  ? 0.2081 0.1953 0.2110 -0.0043 -0.0541 0.0092  47  PHE A C   
305  O O   . PHE A 45  ? 0.2162 0.1947 0.2080 -0.0079 -0.0574 0.0100  47  PHE A O   
306  C CB  . PHE A 45  ? 0.2224 0.2160 0.2406 -0.0003 -0.0553 0.0105  47  PHE A CB  
307  C CG  . PHE A 45  ? 0.2510 0.2516 0.2816 -0.0009 -0.0581 0.0139  47  PHE A CG  
308  C CD1 . PHE A 45  ? 0.2693 0.2792 0.3118 0.0028  -0.0540 0.0128  47  PHE A CD1 
309  C CD2 . PHE A 45  ? 0.2945 0.2928 0.3249 -0.0054 -0.0649 0.0183  47  PHE A CD2 
310  C CE1 . PHE A 45  ? 0.2888 0.3066 0.3439 0.0022  -0.0560 0.0161  47  PHE A CE1 
311  C CE2 . PHE A 45  ? 0.3108 0.3170 0.3541 -0.0062 -0.0677 0.0220  47  PHE A CE2 
312  C CZ  . PHE A 45  ? 0.2916 0.3080 0.3476 -0.0022 -0.0630 0.0209  47  PHE A CZ  
313  N N   . PHE A 46  ? 0.1926 0.1855 0.2021 -0.0042 -0.0533 0.0099  48  PHE A N   
314  C CA  . PHE A 46  ? 0.2402 0.2296 0.2452 -0.0088 -0.0570 0.0123  48  PHE A CA  
315  C C   . PHE A 46  ? 0.2580 0.2571 0.2767 -0.0095 -0.0588 0.0156  48  PHE A C   
316  O O   . PHE A 46  ? 0.2224 0.2304 0.2509 -0.0062 -0.0544 0.0144  48  PHE A O   
317  C CB  . PHE A 46  ? 0.2801 0.2646 0.2752 -0.0086 -0.0537 0.0095  48  PHE A CB  
318  C CG  . PHE A 46  ? 0.3448 0.3230 0.3326 -0.0136 -0.0579 0.0116  48  PHE A CG  
319  C CD1 . PHE A 46  ? 0.3819 0.3485 0.3563 -0.0172 -0.0614 0.0119  48  PHE A CD1 
320  C CD2 . PHE A 46  ? 0.3816 0.3651 0.3753 -0.0152 -0.0585 0.0135  48  PHE A CD2 
321  C CE1 . PHE A 46  ? 0.4181 0.3774 0.3846 -0.0224 -0.0658 0.0140  48  PHE A CE1 
322  C CE2 . PHE A 46  ? 0.4072 0.3842 0.3936 -0.0205 -0.0631 0.0159  48  PHE A CE2 
323  C CZ  . PHE A 46  ? 0.4126 0.3771 0.3852 -0.0239 -0.0668 0.0160  48  PHE A CZ  
324  N N   . LYS A 47  ? 0.2899 0.2876 0.3093 -0.0144 -0.0654 0.0201  49  LYS A N   
325  C CA  . LYS A 47  ? 0.3362 0.3434 0.3676 -0.0162 -0.0671 0.0237  49  LYS A CA  
326  C C   . LYS A 47  ? 0.4276 0.4279 0.4500 -0.0228 -0.0730 0.0269  49  LYS A C   
327  O O   . LYS A 47  ? 0.4440 0.4365 0.4593 -0.0267 -0.0786 0.0292  49  LYS A O   
328  C CB  . LYS A 47  ? 0.3504 0.3673 0.3986 -0.0145 -0.0693 0.0270  49  LYS A CB  
329  C CG  . LYS A 47  ? 0.4051 0.4349 0.4689 -0.0147 -0.0688 0.0300  49  LYS A CG  
330  C CD  . LYS A 47  ? 0.4642 0.5039 0.5460 -0.0111 -0.0694 0.0324  49  LYS A CD  
331  C CE  . LYS A 47  ? 0.5059 0.5586 0.6043 -0.0126 -0.0712 0.0372  49  LYS A CE  
332  N NZ  . LYS A 47  ? 0.5466 0.6069 0.6479 -0.0118 -0.0647 0.0349  49  LYS A NZ  
333  N N   . ASN A 48  ? 0.4750 0.4769 0.4962 -0.0246 -0.0717 0.0269  50  ASN A N   
334  C CA  . ASN A 48  ? 0.5381 0.5322 0.5494 -0.0313 -0.0772 0.0298  50  ASN A CA  
335  C C   . ASN A 48  ? 0.5834 0.5849 0.6061 -0.0357 -0.0839 0.0363  50  ASN A C   
336  O O   . ASN A 48  ? 0.5896 0.6038 0.6266 -0.0357 -0.0831 0.0389  50  ASN A O   
337  C CB  . ASN A 48  ? 0.5714 0.5655 0.5790 -0.0318 -0.0740 0.0282  50  ASN A CB  
338  C CG  . ASN A 48  ? 0.6315 0.6110 0.6216 -0.0366 -0.0774 0.0280  50  ASN A CG  
339  O OD1 . ASN A 48  ? 0.6472 0.6155 0.6261 -0.0403 -0.0822 0.0289  50  ASN A OD1 
340  N ND2 . ASN A 48  ? 0.6484 0.6271 0.6353 -0.0368 -0.0750 0.0268  50  ASN A ND2 
341  N N   . ASP A 49  ? 0.6140 0.6078 0.6305 -0.0398 -0.0905 0.0392  51  ASP A N   
342  C CA  . ASP A 49  ? 0.6361 0.6344 0.6611 -0.0452 -0.0987 0.0462  51  ASP A CA  
343  C C   . ASP A 49  ? 0.6685 0.6521 0.6753 -0.0534 -0.1055 0.0484  51  ASP A C   
344  O O   . ASP A 49  ? 0.6791 0.6491 0.6703 -0.0551 -0.1073 0.0465  51  ASP A O   
345  C CB  . ASP A 49  ? 0.6671 0.6675 0.6993 -0.0429 -0.1010 0.0477  51  ASP A CB  
346  C CG  . ASP A 49  ? 0.7268 0.7302 0.7669 -0.0486 -0.1106 0.0554  51  ASP A CG  
347  O OD1 . ASP A 49  ? 0.7298 0.7328 0.7682 -0.0552 -0.1160 0.0599  51  ASP A OD1 
348  O OD2 . ASP A 49  ? 0.7661 0.7719 0.8139 -0.0467 -0.1131 0.0573  51  ASP A OD2 
349  N N   . LYS A 50  ? 0.6781 0.6642 0.6863 -0.0589 -0.1092 0.0523  52  LYS A N   
350  C CA  . LYS A 50  ? 0.6978 0.6693 0.6881 -0.0673 -0.1158 0.0545  52  LYS A CA  
351  C C   . LYS A 50  ? 0.7012 0.6654 0.6859 -0.0739 -0.1249 0.0594  52  LYS A C   
352  O O   . LYS A 50  ? 0.7190 0.6671 0.6843 -0.0805 -0.1296 0.0597  52  LYS A O   
353  C CB  . LYS A 50  ? 0.7306 0.7088 0.7267 -0.0721 -0.1183 0.0587  52  LYS A CB  
354  C CG  . LYS A 50  ? 0.8117 0.7728 0.7868 -0.0798 -0.1232 0.0592  52  LYS A CG  
355  C CD  . LYS A 50  ? 0.8632 0.8319 0.8457 -0.0872 -0.1291 0.0661  52  LYS A CD  
356  C CE  . LYS A 50  ? 0.9183 0.8684 0.8790 -0.0957 -0.1352 0.0671  52  LYS A CE  
357  N NZ  . LYS A 50  ? 0.9453 0.9027 0.9131 -0.1045 -0.1429 0.0753  52  LYS A NZ  
358  N N   . SER A 51  ? 0.6844 0.6594 0.6852 -0.0724 -0.1277 0.0634  53  SER A N   
359  C CA  . SER A 51  ? 0.6902 0.6582 0.6858 -0.0790 -0.1370 0.0686  53  SER A CA  
360  C C   . SER A 51  ? 0.6948 0.6463 0.6704 -0.0786 -0.1356 0.0636  53  SER A C   
361  O O   . SER A 51  ? 0.7166 0.6561 0.6787 -0.0861 -0.1431 0.0667  53  SER A O   
362  C CB  . SER A 51  ? 0.6992 0.6835 0.7189 -0.0770 -0.1405 0.0745  53  SER A CB  
363  O OG  . SER A 51  ? 0.7209 0.7079 0.7464 -0.0694 -0.1358 0.0709  53  SER A OG  
364  N N   . LYS A 52  ? 0.6642 0.6155 0.6382 -0.0703 -0.1263 0.0564  54  LYS A N   
365  C CA  . LYS A 52  ? 0.6476 0.5852 0.6039 -0.0694 -0.1236 0.0513  54  LYS A CA  
366  C C   . LYS A 52  ? 0.6225 0.5485 0.5612 -0.0677 -0.1169 0.0444  54  LYS A C   
367  O O   . LYS A 52  ? 0.5981 0.5282 0.5406 -0.0658 -0.1137 0.0432  54  LYS A O   
368  C CB  . LYS A 52  ? 0.6650 0.6111 0.6328 -0.0615 -0.1182 0.0486  54  LYS A CB  
369  C CG  . LYS A 52  ? 0.6959 0.6538 0.6830 -0.0611 -0.1235 0.0546  54  LYS A CG  
370  C CD  . LYS A 52  ? 0.7366 0.7008 0.7329 -0.0530 -0.1175 0.0510  54  LYS A CD  
371  C CE  . LYS A 52  ? 0.7628 0.7374 0.7784 -0.0516 -0.1225 0.0565  54  LYS A CE  
372  N NZ  . LYS A 52  ? 0.7769 0.7526 0.7958 -0.0454 -0.1182 0.0531  54  LYS A NZ  
373  N N   . THR A 53  ? 0.6243 0.5358 0.5440 -0.0684 -0.1149 0.0402  55  THR A N   
374  C CA  . THR A 53  ? 0.6344 0.5352 0.5387 -0.0654 -0.1079 0.0333  55  THR A CA  
375  C C   . THR A 53  ? 0.6237 0.5357 0.5401 -0.0557 -0.0987 0.0287  55  THR A C   
376  O O   . THR A 53  ? 0.6141 0.5385 0.5461 -0.0516 -0.0975 0.0298  55  THR A O   
377  C CB  . THR A 53  ? 0.6694 0.5542 0.5526 -0.0678 -0.1069 0.0298  55  THR A CB  
378  O OG1 . THR A 53  ? 0.6892 0.5802 0.5791 -0.0646 -0.1053 0.0295  55  THR A OG1 
379  C CG2 . THR A 53  ? 0.6740 0.5448 0.5411 -0.0780 -0.1155 0.0335  55  THR A CG2 
380  N N   . TRP A 54  ? 0.6210 0.5278 0.5298 -0.0522 -0.0927 0.0237  56  TRP A N   
381  C CA  . TRP A 54  ? 0.6099 0.5245 0.5264 -0.0438 -0.0842 0.0191  56  TRP A CA  
382  C C   . TRP A 54  ? 0.5986 0.5137 0.5139 -0.0403 -0.0805 0.0164  56  TRP A C   
383  O O   . TRP A 54  ? 0.5900 0.5166 0.5185 -0.0348 -0.0766 0.0155  56  TRP A O   
384  C CB  . TRP A 54  ? 0.6261 0.5315 0.5312 -0.0416 -0.0794 0.0145  56  TRP A CB  
385  C CG  . TRP A 54  ? 0.6382 0.5506 0.5499 -0.0335 -0.0713 0.0101  56  TRP A CG  
386  C CD1 . TRP A 54  ? 0.6481 0.5706 0.5716 -0.0298 -0.0683 0.0100  56  TRP A CD1 
387  C CD2 . TRP A 54  ? 0.6508 0.5608 0.5574 -0.0289 -0.0654 0.0058  56  TRP A CD2 
388  N NE1 . TRP A 54  ? 0.6549 0.5809 0.5807 -0.0233 -0.0614 0.0059  56  TRP A NE1 
389  C CE2 . TRP A 54  ? 0.6599 0.5789 0.5762 -0.0225 -0.0595 0.0034  56  TRP A CE2 
390  C CE3 . TRP A 54  ? 0.6720 0.5731 0.5664 -0.0301 -0.0646 0.0038  56  TRP A CE3 
391  C CZ2 . TRP A 54  ? 0.6726 0.5929 0.5879 -0.0173 -0.0533 -0.0004 56  TRP A CZ2 
392  C CZ3 . TRP A 54  ? 0.6900 0.5930 0.5838 -0.0248 -0.0580 -0.0001 56  TRP A CZ3 
393  C CH2 . TRP A 54  ? 0.6839 0.5965 0.5883 -0.0184 -0.0525 -0.0021 56  TRP A CH2 
394  N N   . GLN A 55  ? 0.5927 0.4947 0.4913 -0.0441 -0.0820 0.0153  57  GLN A N   
395  C CA  . GLN A 55  ? 0.5924 0.4924 0.4859 -0.0423 -0.0788 0.0128  57  GLN A CA  
396  C C   . GLN A 55  ? 0.5651 0.4763 0.4735 -0.0419 -0.0822 0.0167  57  GLN A C   
397  O O   . GLN A 55  ? 0.5599 0.4775 0.4745 -0.0370 -0.0776 0.0146  57  GLN A O   
398  C CB  . GLN A 55  ? 0.6415 0.5248 0.5134 -0.0487 -0.0814 0.0121  57  GLN A CB  
399  C CG  . GLN A 55  ? 0.7258 0.6027 0.5856 -0.0460 -0.0745 0.0068  57  GLN A CG  
400  C CD  . GLN A 55  ? 0.8280 0.6867 0.6647 -0.0517 -0.0754 0.0048  57  GLN A CD  
401  O OE1 . GLN A 55  ? 0.8488 0.6990 0.6750 -0.0491 -0.0698 0.0000  57  GLN A OE1 
402  N NE2 . GLN A 55  ? 0.8627 0.7143 0.6906 -0.0598 -0.0825 0.0085  57  GLN A NE2 
403  N N   . ALA A 56  ? 0.5480 0.4613 0.4623 -0.0472 -0.0903 0.0226  58  ALA A N   
404  C CA  . ALA A 56  ? 0.5326 0.4560 0.4621 -0.0469 -0.0945 0.0269  58  ALA A CA  
405  C C   . ALA A 56  ? 0.4832 0.4224 0.4341 -0.0406 -0.0914 0.0274  58  ALA A C   
406  O O   . ALA A 56  ? 0.4773 0.4250 0.4415 -0.0381 -0.0926 0.0294  58  ALA A O   
407  C CB  . ALA A 56  ? 0.5555 0.4757 0.4844 -0.0548 -0.1045 0.0335  58  ALA A CB  
408  N N   . ASN A 57  ? 0.4455 0.3880 0.3991 -0.0383 -0.0877 0.0255  59  ASN A N   
409  C CA  . ASN A 57  ? 0.4334 0.3900 0.4046 -0.0324 -0.0834 0.0249  59  ASN A CA  
410  C C   . ASN A 57  ? 0.4218 0.3808 0.3934 -0.0257 -0.0754 0.0196  59  ASN A C   
411  O O   . ASN A 57  ? 0.4192 0.3889 0.4051 -0.0212 -0.0728 0.0195  59  ASN A O   
412  C CB  . ASN A 57  ? 0.4440 0.4034 0.4175 -0.0331 -0.0825 0.0252  59  ASN A CB  
413  C CG  . ASN A 57  ? 0.5026 0.4642 0.4812 -0.0393 -0.0902 0.0314  59  ASN A CG  
414  O OD1 . ASN A 57  ? 0.5016 0.4710 0.4929 -0.0403 -0.0947 0.0359  59  ASN A OD1 
415  N ND2 . ASN A 57  ? 0.5291 0.4840 0.4984 -0.0437 -0.0923 0.0320  59  ASN A ND2 
416  N N   . LEU A 58  ? 0.4115 0.3610 0.3681 -0.0249 -0.0714 0.0153  60  LEU A N   
417  C CA  . LEU A 58  ? 0.3943 0.3465 0.3512 -0.0192 -0.0644 0.0109  60  LEU A CA  
418  C C   . LEU A 58  ? 0.3827 0.3333 0.3380 -0.0198 -0.0659 0.0115  60  LEU A C   
419  O O   . LEU A 58  ? 0.4081 0.3492 0.3510 -0.0244 -0.0691 0.0122  60  LEU A O   
420  C CB  . LEU A 58  ? 0.4010 0.3453 0.3449 -0.0179 -0.0594 0.0066  60  LEU A CB  
421  C CG  . LEU A 58  ? 0.4318 0.3802 0.3772 -0.0122 -0.0524 0.0027  60  LEU A CG  
422  C CD1 . LEU A 58  ? 0.4052 0.3642 0.3637 -0.0080 -0.0492 0.0022  60  LEU A CD1 
423  C CD2 . LEU A 58  ? 0.4669 0.4069 0.3994 -0.0110 -0.0480 -0.0011 60  LEU A CD2 
424  N N   . ARG A 59  ? 0.3381 0.2970 0.3046 -0.0158 -0.0638 0.0112  61  ARG A N   
425  C CA  . ARG A 59  ? 0.3331 0.2906 0.2988 -0.0164 -0.0657 0.0121  61  ARG A CA  
426  C C   . ARG A 59  ? 0.2951 0.2557 0.2612 -0.0118 -0.0594 0.0084  61  ARG A C   
427  O O   . ARG A 59  ? 0.2783 0.2465 0.2541 -0.0074 -0.0556 0.0070  61  ARG A O   
428  C CB  . ARG A 59  ? 0.3808 0.3448 0.3611 -0.0163 -0.0708 0.0163  61  ARG A CB  
429  C CG  . ARG A 59  ? 0.4921 0.4527 0.4716 -0.0221 -0.0787 0.0212  61  ARG A CG  
430  C CD  . ARG A 59  ? 0.5723 0.5424 0.5700 -0.0211 -0.0828 0.0256  61  ARG A CD  
431  N NE  . ARG A 59  ? 0.6528 0.6246 0.6585 -0.0203 -0.0866 0.0283  61  ARG A NE  
432  C CZ  . ARG A 59  ? 0.7340 0.7111 0.7534 -0.0210 -0.0927 0.0335  61  ARG A CZ  
433  N NH1 . ARG A 59  ? 0.7497 0.7271 0.7759 -0.0198 -0.0961 0.0358  61  ARG A NH1 
434  N NH2 . ARG A 59  ? 0.7475 0.7297 0.7744 -0.0229 -0.0956 0.0368  61  ARG A NH2 
435  N N   . LEU A 60  ? 0.2948 0.2496 0.2501 -0.0133 -0.0584 0.0072  62  LEU A N   
436  C CA  . LEU A 60  ? 0.3084 0.2663 0.2646 -0.0101 -0.0539 0.0049  62  LEU A CA  
437  C C   . LEU A 60  ? 0.3126 0.2738 0.2783 -0.0098 -0.0578 0.0076  62  LEU A C   
438  O O   . LEU A 60  ? 0.3194 0.2760 0.2822 -0.0139 -0.0637 0.0107  62  LEU A O   
439  C CB  . LEU A 60  ? 0.3354 0.2863 0.2770 -0.0128 -0.0521 0.0034  62  LEU A CB  
440  C CG  . LEU A 60  ? 0.3638 0.3179 0.3054 -0.0110 -0.0486 0.0021  62  LEU A CG  
441  C CD1 . LEU A 60  ? 0.3353 0.2964 0.2836 -0.0059 -0.0428 -0.0006 62  LEU A CD1 
442  C CD2 . LEU A 60  ? 0.3977 0.3456 0.3252 -0.0144 -0.0468 0.0010  62  LEU A CD2 
443  N N   . ILE A 61  ? 0.2665 0.2348 0.2431 -0.0053 -0.0551 0.0065  63  ILE A N   
444  C CA  . ILE A 61  ? 0.2711 0.2417 0.2570 -0.0042 -0.0582 0.0085  63  ILE A CA  
445  C C   . ILE A 61  ? 0.2727 0.2402 0.2524 -0.0049 -0.0576 0.0079  63  ILE A C   
446  O O   . ILE A 61  ? 0.2911 0.2548 0.2703 -0.0074 -0.0627 0.0107  63  ILE A O   
447  C CB  . ILE A 61  ? 0.2774 0.2560 0.2771 0.0009  -0.0552 0.0073  63  ILE A CB  
448  C CG1 . ILE A 61  ? 0.3133 0.2962 0.3202 0.0011  -0.0560 0.0086  63  ILE A CG1 
449  C CG2 . ILE A 61  ? 0.2964 0.2761 0.3052 0.0028  -0.0579 0.0088  63  ILE A CG2 
450  C CD1 . ILE A 61  ? 0.3665 0.3467 0.3743 -0.0031 -0.0633 0.0130  63  ILE A CD1 
451  N N   . SER A 62  ? 0.2218 0.1912 0.1972 -0.0030 -0.0516 0.0046  64  SER A N   
452  C CA  . SER A 62  ? 0.2413 0.2094 0.2128 -0.0036 -0.0508 0.0043  64  SER A CA  
453  C C   . SER A 62  ? 0.2245 0.1954 0.1911 -0.0021 -0.0443 0.0013  64  SER A C   
454  O O   . SER A 62  ? 0.2061 0.1807 0.1755 0.0006  -0.0407 -0.0006 64  SER A O   
455  C CB  . SER A 62  ? 0.3101 0.2802 0.2916 -0.0009 -0.0524 0.0049  64  SER A CB  
456  O OG  . SER A 62  ? 0.4232 0.3903 0.3997 -0.0027 -0.0532 0.0054  64  SER A OG  
457  N N   . LYS A 63  ? 0.2157 0.1852 0.1755 -0.0041 -0.0433 0.0012  65  LYS A N   
458  C CA  . LYS A 63  ? 0.1875 0.1609 0.1444 -0.0028 -0.0377 -0.0008 65  LYS A CA  
459  C C   . LYS A 63  ? 0.1932 0.1682 0.1519 -0.0030 -0.0379 -0.0002 65  LYS A C   
460  O O   . LYS A 63  ? 0.2216 0.1925 0.1786 -0.0057 -0.0423 0.0018  65  LYS A O   
461  C CB  . LYS A 63  ? 0.1731 0.1443 0.1192 -0.0053 -0.0352 -0.0014 65  LYS A CB  
462  C CG  . LYS A 63  ? 0.2179 0.1858 0.1598 -0.0053 -0.0345 -0.0024 65  LYS A CG  
463  C CD  . LYS A 63  ? 0.2553 0.2213 0.1868 -0.0065 -0.0300 -0.0041 65  LYS A CD  
464  C CE  . LYS A 63  ? 0.2970 0.2562 0.2212 -0.0079 -0.0307 -0.0049 65  LYS A CE  
465  N NZ  . LYS A 63  ? 0.3795 0.3370 0.2953 -0.0071 -0.0248 -0.0076 65  LYS A NZ  
466  N N   . PHE A 64  ? 0.1575 0.1376 0.1187 -0.0008 -0.0338 -0.0017 66  PHE A N   
467  C CA  . PHE A 64  ? 0.1436 0.1245 0.1054 -0.0015 -0.0341 -0.0012 66  PHE A CA  
468  C C   . PHE A 64  ? 0.1462 0.1328 0.1066 -0.0011 -0.0294 -0.0020 66  PHE A C   
469  O O   . PHE A 64  ? 0.1556 0.1459 0.1172 0.0011  -0.0258 -0.0033 66  PHE A O   
470  C CB  . PHE A 64  ? 0.1623 0.1424 0.1319 0.0010  -0.0358 -0.0016 66  PHE A CB  
471  C CG  . PHE A 64  ? 0.1569 0.1413 0.1323 0.0046  -0.0323 -0.0037 66  PHE A CG  
472  C CD1 . PHE A 64  ? 0.1321 0.1205 0.1079 0.0055  -0.0288 -0.0049 66  PHE A CD1 
473  C CD2 . PHE A 64  ? 0.1818 0.1666 0.1619 0.0065  -0.0328 -0.0042 66  PHE A CD2 
474  C CE1 . PHE A 64  ? 0.1528 0.1448 0.1329 0.0081  -0.0258 -0.0065 66  PHE A CE1 
475  C CE2 . PHE A 64  ? 0.1795 0.1684 0.1640 0.0091  -0.0295 -0.0059 66  PHE A CE2 
476  C CZ  . PHE A 64  ? 0.1634 0.1556 0.1476 0.0099  -0.0260 -0.0071 66  PHE A CZ  
477  N N   . ASP A 65  ? 0.1380 0.1252 0.0959 -0.0035 -0.0299 -0.0007 67  ASP A N   
478  C CA  . ASP A 65  ? 0.1476 0.1413 0.1050 -0.0037 -0.0260 -0.0006 67  ASP A CA  
479  C C   . ASP A 65  ? 0.1404 0.1343 0.0981 -0.0056 -0.0274 0.0005  67  ASP A C   
480  O O   . ASP A 65  ? 0.1580 0.1572 0.1145 -0.0073 -0.0253 0.0017  67  ASP A O   
481  C CB  . ASP A 65  ? 0.1642 0.1604 0.1158 -0.0058 -0.0235 0.0001  67  ASP A CB  
482  C CG  . ASP A 65  ? 0.2208 0.2138 0.1657 -0.0108 -0.0262 0.0023  67  ASP A CG  
483  O OD1 . ASP A 65  ? 0.2058 0.1941 0.1506 -0.0126 -0.0306 0.0034  67  ASP A OD1 
484  O OD2 . ASP A 65  ? 0.2340 0.2289 0.1732 -0.0130 -0.0237 0.0027  67  ASP A OD2 
485  N N   . THR A 66  ? 0.1396 0.1275 0.0991 -0.0053 -0.0309 0.0002  68  THR A N   
486  C CA  . THR A 66  ? 0.1461 0.1321 0.1052 -0.0066 -0.0322 0.0006  68  THR A CA  
487  C C   . THR A 66  ? 0.1468 0.1299 0.1112 -0.0030 -0.0321 -0.0018 68  THR A C   
488  O O   . THR A 66  ? 0.1402 0.1217 0.1090 0.0000  -0.0324 -0.0031 68  THR A O   
489  C CB  . THR A 66  ? 0.1552 0.1349 0.1093 -0.0106 -0.0369 0.0027  68  THR A CB  
490  O OG1 . THR A 66  ? 0.1653 0.1379 0.1216 -0.0091 -0.0405 0.0024  68  THR A OG1 
491  C CG2 . THR A 66  ? 0.1763 0.1588 0.1242 -0.0150 -0.0369 0.0052  68  THR A CG2 
492  N N   . VAL A 67  ? 0.1411 0.1230 0.1045 -0.0037 -0.0317 -0.0023 69  VAL A N   
493  C CA  . VAL A 67  ? 0.1530 0.1312 0.1198 -0.0009 -0.0310 -0.0049 69  VAL A CA  
494  C C   . VAL A 67  ? 0.1676 0.1383 0.1367 0.0008  -0.0343 -0.0054 69  VAL A C   
495  O O   . VAL A 67  ? 0.1675 0.1374 0.1427 0.0046  -0.0334 -0.0074 69  VAL A O   
496  C CB  . VAL A 67  ? 0.1815 0.1577 0.1441 -0.0032 -0.0306 -0.0052 69  VAL A CB  
497  C CG1 . VAL A 67  ? 0.2234 0.1945 0.1881 -0.0002 -0.0291 -0.0085 69  VAL A CG1 
498  C CG2 . VAL A 67  ? 0.1738 0.1580 0.1355 -0.0049 -0.0279 -0.0040 69  VAL A CG2 
499  N N   . GLU A 68  ? 0.1651 0.1303 0.1297 -0.0023 -0.0386 -0.0032 70  GLU A N   
500  C CA  . GLU A 68  ? 0.1977 0.1548 0.1649 -0.0007 -0.0425 -0.0032 70  GLU A CA  
501  C C   . GLU A 68  ? 0.1925 0.1516 0.1654 0.0014  -0.0437 -0.0026 70  GLU A C   
502  O O   . GLU A 68  ? 0.1723 0.1283 0.1519 0.0050  -0.0451 -0.0033 70  GLU A O   
503  C CB  . GLU A 68  ? 0.2232 0.1734 0.1836 -0.0052 -0.0474 -0.0006 70  GLU A CB  
504  C CG  . GLU A 68  ? 0.2372 0.1833 0.1920 -0.0075 -0.0472 -0.0011 70  GLU A CG  
505  C CD  . GLU A 68  ? 0.2457 0.1986 0.1959 -0.0110 -0.0444 -0.0003 70  GLU A CD  
506  O OE1 . GLU A 68  ? 0.2025 0.1644 0.1536 -0.0117 -0.0420 0.0008  70  GLU A OE1 
507  O OE2 . GLU A 68  ? 0.2722 0.2210 0.2177 -0.0131 -0.0446 -0.0007 70  GLU A OE2 
508  N N   . ASP A 69  ? 0.1801 0.1443 0.1502 -0.0007 -0.0432 -0.0010 71  ASP A N   
509  C CA  . ASP A 69  ? 0.1597 0.1248 0.1334 0.0004  -0.0447 -0.0002 71  ASP A CA  
510  C C   . ASP A 69  ? 0.1659 0.1359 0.1469 0.0047  -0.0412 -0.0025 71  ASP A C   
511  O O   . ASP A 69  ? 0.1598 0.1295 0.1468 0.0066  -0.0430 -0.0020 71  ASP A O   
512  C CB  . ASP A 69  ? 0.1769 0.1444 0.1438 -0.0034 -0.0447 0.0016  71  ASP A CB  
513  C CG  . ASP A 69  ? 0.2390 0.2019 0.1985 -0.0084 -0.0487 0.0044  71  ASP A CG  
514  O OD1 . ASP A 69  ? 0.2611 0.2170 0.2218 -0.0089 -0.0539 0.0059  71  ASP A OD1 
515  O OD2 . ASP A 69  ? 0.2373 0.2036 0.1902 -0.0117 -0.0466 0.0052  71  ASP A OD2 
516  N N   . PHE A 70  ? 0.1669 0.1416 0.1477 0.0058  -0.0364 -0.0045 72  PHE A N   
517  C CA  . PHE A 70  ? 0.1498 0.1286 0.1369 0.0093  -0.0331 -0.0067 72  PHE A CA  
518  C C   . PHE A 70  ? 0.1505 0.1258 0.1447 0.0125  -0.0339 -0.0080 72  PHE A C   
519  O O   . PHE A 70  ? 0.1594 0.1367 0.1609 0.0151  -0.0340 -0.0081 72  PHE A O   
520  C CB  . PHE A 70  ? 0.1325 0.1155 0.1172 0.0091  -0.0287 -0.0082 72  PHE A CB  
521  C CG  . PHE A 70  ? 0.1266 0.1122 0.1169 0.0122  -0.0255 -0.0105 72  PHE A CG  
522  C CD1 . PHE A 70  ? 0.1168 0.1068 0.1108 0.0136  -0.0241 -0.0107 72  PHE A CD1 
523  C CD2 . PHE A 70  ? 0.1490 0.1319 0.1401 0.0132  -0.0239 -0.0126 72  PHE A CD2 
524  C CE1 . PHE A 70  ? 0.1445 0.1373 0.1434 0.0157  -0.0212 -0.0126 72  PHE A CE1 
525  C CE2 . PHE A 70  ? 0.1344 0.1199 0.1299 0.0156  -0.0204 -0.0149 72  PHE A CE2 
526  C CZ  . PHE A 70  ? 0.1223 0.1132 0.1221 0.0167  -0.0192 -0.0147 72  PHE A CZ  
527  N N   . TRP A 71  ? 0.1668 0.1368 0.1587 0.0124  -0.0344 -0.0088 73  TRP A N   
528  C CA  . TRP A 71  ? 0.1804 0.1464 0.1789 0.0161  -0.0342 -0.0106 73  TRP A CA  
529  C C   . TRP A 71  ? 0.1867 0.1498 0.1913 0.0175  -0.0391 -0.0084 73  TRP A C   
530  O O   . TRP A 71  ? 0.1963 0.1606 0.2104 0.0215  -0.0384 -0.0092 73  TRP A O   
531  C CB  . TRP A 71  ? 0.1809 0.1402 0.1743 0.0157  -0.0336 -0.0124 73  TRP A CB  
532  C CG  . TRP A 71  ? 0.1713 0.1331 0.1607 0.0150  -0.0287 -0.0149 73  TRP A CG  
533  C CD1 . TRP A 71  ? 0.1954 0.1563 0.1761 0.0110  -0.0284 -0.0145 73  TRP A CD1 
534  C CD2 . TRP A 71  ? 0.1743 0.1402 0.1681 0.0178  -0.0237 -0.0178 73  TRP A CD2 
535  N NE1 . TRP A 71  ? 0.1916 0.1549 0.1706 0.0111  -0.0240 -0.0168 73  TRP A NE1 
536  C CE2 . TRP A 71  ? 0.1868 0.1530 0.1732 0.0151  -0.0209 -0.0190 73  TRP A CE2 
537  C CE3 . TRP A 71  ? 0.1833 0.1531 0.1865 0.0218  -0.0215 -0.0190 73  TRP A CE3 
538  C CZ2 . TRP A 71  ? 0.1926 0.1620 0.1800 0.0162  -0.0161 -0.0216 73  TRP A CZ2 
539  C CZ3 . TRP A 71  ? 0.1846 0.1577 0.1889 0.0230  -0.0163 -0.0219 73  TRP A CZ3 
540  C CH2 . TRP A 71  ? 0.1986 0.1711 0.1945 0.0201  -0.0136 -0.0232 73  TRP A CH2 
541  N N   . ALA A 72  ? 0.1837 0.1435 0.1835 0.0139  -0.0441 -0.0052 74  ALA A N   
542  C CA  . ALA A 72  ? 0.1937 0.1505 0.1991 0.0145  -0.0497 -0.0024 74  ALA A CA  
543  C C   . ALA A 72  ? 0.1830 0.1462 0.1959 0.0160  -0.0494 -0.0015 74  ALA A C   
544  O O   . ALA A 72  ? 0.1926 0.1558 0.2154 0.0189  -0.0519 -0.0003 74  ALA A O   
545  C CB  . ALA A 72  ? 0.2019 0.1540 0.1988 0.0093  -0.0548 0.0010  74  ALA A CB  
546  N N   . LEU A 73  ? 0.1734 0.1420 0.1819 0.0142  -0.0465 -0.0019 75  LEU A N   
547  C CA  . LEU A 73  ? 0.1684 0.1425 0.1819 0.0149  -0.0460 -0.0014 75  LEU A CA  
548  C C   . LEU A 73  ? 0.1474 0.1264 0.1708 0.0194  -0.0419 -0.0037 75  LEU A C   
549  O O   . LEU A 73  ? 0.1743 0.1561 0.2071 0.0213  -0.0436 -0.0023 75  LEU A O   
550  C CB  . LEU A 73  ? 0.1835 0.1605 0.1887 0.0121  -0.0436 -0.0017 75  LEU A CB  
551  C CG  . LEU A 73  ? 0.1873 0.1684 0.1957 0.0121  -0.0436 -0.0010 75  LEU A CG  
552  C CD1 . LEU A 73  ? 0.1841 0.1621 0.1948 0.0100  -0.0502 0.0028  75  LEU A CD1 
553  C CD2 . LEU A 73  ? 0.2192 0.2019 0.2191 0.0101  -0.0407 -0.0018 75  LEU A CD2 
554  N N   . TYR A 74  ? 0.1581 0.1381 0.1795 0.0208  -0.0369 -0.0069 76  TYR A N   
555  C CA  . TYR A 74  ? 0.1548 0.1389 0.1835 0.0244  -0.0321 -0.0096 76  TYR A CA  
556  C C   . TYR A 74  ? 0.1828 0.1654 0.2221 0.0284  -0.0335 -0.0095 76  TYR A C   
557  O O   . TYR A 74  ? 0.1953 0.1834 0.2448 0.0309  -0.0324 -0.0092 76  TYR A O   
558  C CB  . TYR A 74  ? 0.1464 0.1295 0.1686 0.0242  -0.0273 -0.0129 76  TYR A CB  
559  C CG  . TYR A 74  ? 0.1599 0.1475 0.1872 0.0268  -0.0218 -0.0158 76  TYR A CG  
560  C CD1 . TYR A 74  ? 0.1810 0.1749 0.2075 0.0257  -0.0190 -0.0161 76  TYR A CD1 
561  C CD2 . TYR A 74  ? 0.1784 0.1638 0.2115 0.0305  -0.0194 -0.0182 76  TYR A CD2 
562  C CE1 . TYR A 74  ? 0.1941 0.1922 0.2247 0.0273  -0.0140 -0.0185 76  TYR A CE1 
563  C CE2 . TYR A 74  ? 0.1817 0.1714 0.2187 0.0325  -0.0136 -0.0211 76  TYR A CE2 
564  C CZ  . TYR A 74  ? 0.1934 0.1899 0.2292 0.0306  -0.0111 -0.0210 76  TYR A CZ  
565  O OH  . TYR A 74  ? 0.2293 0.2303 0.2685 0.0319  -0.0056 -0.0235 76  TYR A OH  
566  N N   . ASN A 75  ? 0.1937 0.1684 0.2306 0.0287  -0.0363 -0.0093 77  ASN A N   
567  C CA  . ASN A 75  ? 0.2100 0.1817 0.2573 0.0329  -0.0381 -0.0091 77  ASN A CA  
568  C C   . ASN A 75  ? 0.2280 0.2033 0.2857 0.0336  -0.0432 -0.0050 77  ASN A C   
569  O O   . ASN A 75  ? 0.2629 0.2413 0.3335 0.0381  -0.0424 -0.0049 77  ASN A O   
570  C CB  . ASN A 75  ? 0.2326 0.1939 0.2741 0.0325  -0.0412 -0.0091 77  ASN A CB  
571  C CG  . ASN A 75  ? 0.2966 0.2535 0.3288 0.0319  -0.0368 -0.0129 77  ASN A CG  
572  O OD1 . ASN A 75  ? 0.2623 0.2230 0.2940 0.0331  -0.0307 -0.0162 77  ASN A OD1 
573  N ND2 . ASN A 75  ? 0.3370 0.2851 0.3605 0.0292  -0.0402 -0.0122 77  ASN A ND2 
574  N N   . HIS A 76  ? 0.2217 0.1962 0.2740 0.0291  -0.0483 -0.0014 78  HIS A N   
575  C CA  . HIS A 76  ? 0.2373 0.2140 0.2964 0.0280  -0.0542 0.0032  78  HIS A CA  
576  C C   . HIS A 76  ? 0.2375 0.2235 0.3038 0.0287  -0.0516 0.0034  78  HIS A C   
577  O O   . HIS A 76  ? 0.2481 0.2381 0.3269 0.0306  -0.0545 0.0062  78  HIS A O   
578  C CB  . HIS A 76  ? 0.2750 0.2471 0.3222 0.0218  -0.0595 0.0062  78  HIS A CB  
579  C CG  . HIS A 76  ? 0.3635 0.3372 0.4141 0.0189  -0.0655 0.0108  78  HIS A CG  
580  N ND1 . HIS A 76  ? 0.4001 0.3772 0.4450 0.0155  -0.0648 0.0113  78  HIS A ND1 
581  C CD2 . HIS A 76  ? 0.3997 0.3711 0.4579 0.0187  -0.0726 0.0153  78  HIS A CD2 
582  C CE1 . HIS A 76  ? 0.4095 0.3859 0.4577 0.0128  -0.0714 0.0159  78  HIS A CE1 
583  N NE2 . HIS A 76  ? 0.4066 0.3803 0.4635 0.0147  -0.0764 0.0186  78  HIS A NE2 
584  N N   . ILE A 77  ? 0.2226 0.2122 0.2818 0.0271  -0.0467 0.0009  79  ILE A N   
585  C CA  . ILE A 77  ? 0.2454 0.2433 0.3104 0.0274  -0.0441 0.0010  79  ILE A CA  
586  C C   . ILE A 77  ? 0.2737 0.2773 0.3515 0.0325  -0.0395 -0.0011 79  ILE A C   
587  O O   . ILE A 77  ? 0.2841 0.2950 0.3731 0.0337  -0.0398 0.0009  79  ILE A O   
588  C CB  . ILE A 77  ? 0.2409 0.2403 0.2951 0.0248  -0.0398 -0.0014 79  ILE A CB  
589  C CG1 . ILE A 77  ? 0.2762 0.2709 0.3184 0.0200  -0.0435 0.0004  79  ILE A CG1 
590  C CG2 . ILE A 77  ? 0.2445 0.2521 0.3047 0.0252  -0.0366 -0.0017 79  ILE A CG2 
591  C CD1 . ILE A 77  ? 0.3214 0.3156 0.3650 0.0171  -0.0494 0.0045  79  ILE A CD1 
592  N N   . GLN A 78  ? 0.3051 0.3054 0.3811 0.0354  -0.0351 -0.0049 80  GLN A N   
593  C CA  . GLN A 78  ? 0.3496 0.3539 0.4360 0.0405  -0.0295 -0.0077 80  GLN A CA  
594  C C   . GLN A 78  ? 0.4092 0.4156 0.5115 0.0444  -0.0332 -0.0047 80  GLN A C   
595  O O   . GLN A 78  ? 0.4109 0.4246 0.5255 0.0483  -0.0291 -0.0056 80  GLN A O   
596  C CB  . GLN A 78  ? 0.3723 0.3697 0.4511 0.0422  -0.0249 -0.0125 80  GLN A CB  
597  C CG  . GLN A 78  ? 0.4042 0.4048 0.4890 0.0465  -0.0171 -0.0169 80  GLN A CG  
598  C CD  . GLN A 78  ? 0.4318 0.4236 0.5061 0.0469  -0.0134 -0.0213 80  GLN A CD  
599  O OE1 . GLN A 78  ? 0.4642 0.4472 0.5302 0.0453  -0.0172 -0.0208 80  GLN A OE1 
600  N NE2 . GLN A 78  ? 0.4445 0.4380 0.5180 0.0485  -0.0060 -0.0256 80  GLN A NE2 
601  N N   . LEU A 79  ? 0.4536 0.4545 0.5559 0.0429  -0.0411 -0.0007 81  LEU A N   
602  C CA  . LEU A 79  ? 0.4956 0.4971 0.6122 0.0459  -0.0465 0.0033  81  LEU A CA  
603  C C   . LEU A 79  ? 0.5194 0.5274 0.6421 0.0424  -0.0524 0.0090  81  LEU A C   
604  O O   . LEU A 79  ? 0.5292 0.5436 0.6682 0.0454  -0.0545 0.0121  81  LEU A O   
605  C CB  . LEU A 79  ? 0.5119 0.5017 0.6217 0.0448  -0.0525 0.0047  81  LEU A CB  
606  C CG  . LEU A 79  ? 0.5336 0.5187 0.6548 0.0500  -0.0556 0.0059  81  LEU A CG  
607  C CD1 . LEU A 79  ? 0.5352 0.5226 0.6654 0.0572  -0.0474 0.0009  81  LEU A CD1 
608  C CD2 . LEU A 79  ? 0.5527 0.5251 0.6616 0.0474  -0.0603 0.0062  81  LEU A CD2 
609  N N   . SER A 80  ? 0.5348 0.5410 0.6446 0.0362  -0.0551 0.0104  82  SER A N   
610  C CA  . SER A 80  ? 0.5607 0.5698 0.6716 0.0315  -0.0615 0.0157  82  SER A CA  
611  C C   . SER A 80  ? 0.5751 0.5864 0.6752 0.0272  -0.0588 0.0144  82  SER A C   
612  O O   . SER A 80  ? 0.6033 0.6082 0.6879 0.0233  -0.0592 0.0132  82  SER A O   
613  C CB  . SER A 80  ? 0.6112 0.6113 0.7152 0.0275  -0.0701 0.0196  82  SER A CB  
614  O OG  . SER A 80  ? 0.6828 0.6752 0.7687 0.0236  -0.0693 0.0174  82  SER A OG  
615  N N   . SER A 81  ? 0.5426 0.5634 0.6513 0.0278  -0.0560 0.0147  83  SER A N   
616  C CA  . SER A 81  ? 0.5247 0.5476 0.6246 0.0236  -0.0544 0.0143  83  SER A CA  
617  C C   . SER A 81  ? 0.4975 0.5314 0.6091 0.0249  -0.0510 0.0148  83  SER A C   
618  O O   . SER A 81  ? 0.5006 0.5406 0.6242 0.0299  -0.0464 0.0131  83  SER A O   
619  C CB  . SER A 81  ? 0.5598 0.5783 0.6458 0.0234  -0.0486 0.0092  83  SER A CB  
620  O OG  . SER A 81  ? 0.5898 0.6114 0.6816 0.0283  -0.0420 0.0053  83  SER A OG  
621  N N   . ASN A 82  ? 0.4732 0.5094 0.5806 0.0202  -0.0528 0.0169  84  ASN A N   
622  C CA  . ASN A 82  ? 0.4549 0.5017 0.5731 0.0200  -0.0509 0.0186  84  ASN A CA  
623  C C   . ASN A 82  ? 0.4107 0.4601 0.5236 0.0210  -0.0427 0.0136  84  ASN A C   
624  O O   . ASN A 82  ? 0.4131 0.4561 0.5111 0.0186  -0.0415 0.0112  84  ASN A O   
625  C CB  . ASN A 82  ? 0.5068 0.5530 0.6211 0.0135  -0.0578 0.0235  84  ASN A CB  
626  C CG  . ASN A 82  ? 0.5927 0.6504 0.7217 0.0122  -0.0595 0.0280  84  ASN A CG  
627  O OD1 . ASN A 82  ? 0.6255 0.6848 0.7498 0.0076  -0.0604 0.0294  84  ASN A OD1 
628  N ND2 . ASN A 82  ? 0.6165 0.6824 0.7639 0.0160  -0.0603 0.0307  84  ASN A ND2 
629  N N   . LEU A 83  ? 0.3641 0.4227 0.4891 0.0247  -0.0370 0.0122  85  LEU A N   
630  C CA  . LEU A 83  ? 0.3408 0.4033 0.4619 0.0247  -0.0297 0.0084  85  LEU A CA  
631  C C   . LEU A 83  ? 0.3190 0.3928 0.4516 0.0228  -0.0297 0.0118  85  LEU A C   
632  O O   . LEU A 83  ? 0.3294 0.4127 0.4761 0.0263  -0.0253 0.0115  85  LEU A O   
633  C CB  . LEU A 83  ? 0.3375 0.4006 0.4615 0.0300  -0.0221 0.0032  85  LEU A CB  
634  C CG  . LEU A 83  ? 0.3663 0.4329 0.4851 0.0293  -0.0144 -0.0007 85  LEU A CG  
635  C CD1 . LEU A 83  ? 0.3692 0.4273 0.4710 0.0264  -0.0145 -0.0029 85  LEU A CD1 
636  C CD2 . LEU A 83  ? 0.3842 0.4532 0.5088 0.0343  -0.0069 -0.0050 85  LEU A CD2 
637  N N   . MET A 84  ? 0.2812 0.3540 0.4077 0.0171  -0.0346 0.0152  86  MET A N   
638  C CA  . MET A 84  ? 0.2531 0.3364 0.3892 0.0141  -0.0353 0.0190  86  MET A CA  
639  C C   . MET A 84  ? 0.2527 0.3328 0.3755 0.0088  -0.0352 0.0186  86  MET A C   
640  O O   . MET A 84  ? 0.2525 0.3216 0.3599 0.0073  -0.0367 0.0166  86  MET A O   
641  C CB  . MET A 84  ? 0.2379 0.3227 0.3817 0.0114  -0.0441 0.0255  86  MET A CB  
642  C CG  . MET A 84  ? 0.2627 0.3526 0.4231 0.0165  -0.0450 0.0272  86  MET A CG  
643  S SD  . MET A 84  ? 0.2757 0.3843 0.4600 0.0204  -0.0392 0.0287  86  MET A SD  
644  C CE  . MET A 84  ? 0.2538 0.3698 0.4444 0.0134  -0.0468 0.0366  86  MET A CE  
645  N N   . PRO A 85  ? 0.2395 0.3289 0.3682 0.0058  -0.0336 0.0207  87  PRO A N   
646  C CA  . PRO A 85  ? 0.2526 0.3377 0.3683 0.0005  -0.0343 0.0206  87  PRO A CA  
647  C C   . PRO A 85  ? 0.2655 0.3401 0.3701 -0.0039 -0.0425 0.0235  87  PRO A C   
648  O O   . PRO A 85  ? 0.2521 0.3274 0.3627 -0.0055 -0.0488 0.0280  87  PRO A O   
649  C CB  . PRO A 85  ? 0.2675 0.3656 0.3940 -0.0025 -0.0328 0.0239  87  PRO A CB  
650  C CG  . PRO A 85  ? 0.2500 0.3597 0.3941 0.0026  -0.0279 0.0234  87  PRO A CG  
651  C CD  . PRO A 85  ? 0.2325 0.3368 0.3801 0.0068  -0.0316 0.0236  87  PRO A CD  
652  N N   . GLY A 86  ? 0.2651 0.3297 0.3535 -0.0059 -0.0423 0.0210  88  GLY A N   
653  C CA  . GLY A 86  ? 0.2803 0.3327 0.3551 -0.0097 -0.0485 0.0224  88  GLY A CA  
654  C C   . GLY A 86  ? 0.2841 0.3266 0.3501 -0.0067 -0.0487 0.0194  88  GLY A C   
655  O O   . GLY A 86  ? 0.3109 0.3425 0.3638 -0.0093 -0.0524 0.0194  88  GLY A O   
656  N N   . CYS A 87  ? 0.2508 0.2963 0.3230 -0.0014 -0.0447 0.0167  89  CYS A N   
657  C CA  . CYS A 87  ? 0.2484 0.2850 0.3120 0.0008  -0.0449 0.0141  89  CYS A CA  
658  C C   . CYS A 87  ? 0.2515 0.2827 0.3032 0.0018  -0.0402 0.0097  89  CYS A C   
659  O O   . CYS A 87  ? 0.2365 0.2726 0.2903 0.0029  -0.0353 0.0078  89  CYS A O   
660  C CB  . CYS A 87  ? 0.2619 0.3024 0.3358 0.0056  -0.0431 0.0132  89  CYS A CB  
661  S SG  . CYS A 87  ? 0.3747 0.4205 0.4631 0.0050  -0.0496 0.0188  89  CYS A SG  
662  N N   . ASP A 88  ? 0.2422 0.2634 0.2816 0.0012  -0.0418 0.0085  90  ASP A N   
663  C CA  . ASP A 88  ? 0.2299 0.2466 0.2599 0.0031  -0.0376 0.0047  90  ASP A CA  
664  C C   . ASP A 88  ? 0.1985 0.2109 0.2255 0.0054  -0.0376 0.0032  90  ASP A C   
665  O O   . ASP A 88  ? 0.1909 0.1989 0.2155 0.0038  -0.0419 0.0050  90  ASP A O   
666  C CB  . ASP A 88  ? 0.2386 0.2475 0.2566 0.0005  -0.0390 0.0045  90  ASP A CB  
667  C CG  . ASP A 88  ? 0.3397 0.3505 0.3585 -0.0029 -0.0405 0.0066  90  ASP A CG  
668  O OD1 . ASP A 88  ? 0.3000 0.3193 0.3272 -0.0027 -0.0380 0.0069  90  ASP A OD1 
669  O OD2 . ASP A 88  ? 0.4131 0.4161 0.4231 -0.0062 -0.0442 0.0078  90  ASP A OD2 
670  N N   . TYR A 89  ? 0.1658 0.1792 0.1922 0.0084  -0.0330 0.0001  91  TYR A N   
671  C CA  . TYR A 89  ? 0.1392 0.1480 0.1607 0.0098  -0.0330 -0.0012 91  TYR A CA  
672  C C   . TYR A 89  ? 0.1309 0.1367 0.1435 0.0104  -0.0296 -0.0036 91  TYR A C   
673  O O   . TYR A 89  ? 0.1215 0.1304 0.1349 0.0110  -0.0264 -0.0048 91  TYR A O   
674  C CB  . TYR A 89  ? 0.1257 0.1381 0.1549 0.0128  -0.0311 -0.0022 91  TYR A CB  
675  C CG  . TYR A 89  ? 0.1897 0.2045 0.2286 0.0130  -0.0349 0.0005  91  TYR A CG  
676  C CD1 . TYR A 89  ? 0.1945 0.2167 0.2446 0.0137  -0.0342 0.0017  91  TYR A CD1 
677  C CD2 . TYR A 89  ? 0.2128 0.2228 0.2502 0.0125  -0.0391 0.0020  91  TYR A CD2 
678  C CE1 . TYR A 89  ? 0.2147 0.2403 0.2760 0.0146  -0.0375 0.0044  91  TYR A CE1 
679  C CE2 . TYR A 89  ? 0.2247 0.2369 0.2721 0.0130  -0.0430 0.0049  91  TYR A CE2 
680  C CZ  . TYR A 89  ? 0.2442 0.2644 0.3041 0.0143  -0.0423 0.0062  91  TYR A CZ  
681  O OH  . TYR A 89  ? 0.3325 0.3556 0.4038 0.0150  -0.0465 0.0096  91  TYR A OH  
682  N N   . SER A 90  ? 0.1232 0.1233 0.1277 0.0100  -0.0304 -0.0041 92  SER A N   
683  C CA  . SER A 90  ? 0.1326 0.1303 0.1296 0.0108  -0.0274 -0.0059 92  SER A CA  
684  C C   . SER A 90  ? 0.1441 0.1401 0.1376 0.0117  -0.0265 -0.0067 92  SER A C   
685  O O   . SER A 90  ? 0.1510 0.1434 0.1418 0.0103  -0.0293 -0.0058 92  SER A O   
686  C CB  . SER A 90  ? 0.1769 0.1686 0.1659 0.0092  -0.0288 -0.0055 92  SER A CB  
687  O OG  . SER A 90  ? 0.2121 0.2044 0.2032 0.0076  -0.0305 -0.0043 92  SER A OG  
688  N N   . LEU A 91  ? 0.1243 0.1228 0.1173 0.0132  -0.0231 -0.0082 93  LEU A N   
689  C CA  . LEU A 91  ? 0.1192 0.1166 0.1085 0.0134  -0.0223 -0.0086 93  LEU A CA  
690  C C   . LEU A 91  ? 0.1443 0.1410 0.1281 0.0140  -0.0198 -0.0092 93  LEU A C   
691  O O   . LEU A 91  ? 0.1279 0.1276 0.1135 0.0151  -0.0177 -0.0096 93  LEU A O   
692  C CB  . LEU A 91  ? 0.1323 0.1329 0.1253 0.0143  -0.0207 -0.0093 93  LEU A CB  
693  C CG  . LEU A 91  ? 0.1367 0.1359 0.1256 0.0136  -0.0208 -0.0091 93  LEU A CG  
694  C CD1 . LEU A 91  ? 0.1479 0.1432 0.1360 0.0123  -0.0243 -0.0079 93  LEU A CD1 
695  C CD2 . LEU A 91  ? 0.1503 0.1519 0.1409 0.0140  -0.0190 -0.0098 93  LEU A CD2 
696  N N   . PHE A 92  ? 0.1458 0.1384 0.1231 0.0134  -0.0200 -0.0092 94  PHE A N   
697  C CA  . PHE A 92  ? 0.1431 0.1350 0.1159 0.0147  -0.0171 -0.0100 94  PHE A CA  
698  C C   . PHE A 92  ? 0.1360 0.1284 0.1053 0.0143  -0.0156 -0.0100 94  PHE A C   
699  O O   . PHE A 92  ? 0.1473 0.1376 0.1141 0.0123  -0.0175 -0.0094 94  PHE A O   
700  C CB  . PHE A 92  ? 0.1528 0.1383 0.1199 0.0144  -0.0178 -0.0105 94  PHE A CB  
701  C CG  . PHE A 92  ? 0.1350 0.1209 0.1051 0.0151  -0.0182 -0.0104 94  PHE A CG  
702  C CD1 . PHE A 92  ? 0.1650 0.1533 0.1407 0.0139  -0.0204 -0.0094 94  PHE A CD1 
703  C CD2 . PHE A 92  ? 0.1375 0.1216 0.1053 0.0170  -0.0162 -0.0110 94  PHE A CD2 
704  C CE1 . PHE A 92  ? 0.1799 0.1692 0.1581 0.0139  -0.0206 -0.0091 94  PHE A CE1 
705  C CE2 . PHE A 92  ? 0.1573 0.1413 0.1274 0.0171  -0.0170 -0.0106 94  PHE A CE2 
706  C CZ  . PHE A 92  ? 0.1689 0.1555 0.1436 0.0151  -0.0193 -0.0096 94  PHE A CZ  
707  N N   . LYS A 93  ? 0.0893 0.0849 0.0584 0.0162  -0.0123 -0.0103 95  LYS A N   
708  C CA  . LYS A 93  ? 0.1214 0.1185 0.0872 0.0158  -0.0100 -0.0101 95  LYS A CA  
709  C C   . LYS A 93  ? 0.1464 0.1371 0.1041 0.0144  -0.0102 -0.0109 95  LYS A C   
710  O O   . LYS A 93  ? 0.1738 0.1588 0.1279 0.0148  -0.0106 -0.0120 95  LYS A O   
711  C CB  . LYS A 93  ? 0.1323 0.1340 0.1004 0.0186  -0.0063 -0.0101 95  LYS A CB  
712  C CG  . LYS A 93  ? 0.1420 0.1502 0.1169 0.0189  -0.0065 -0.0087 95  LYS A CG  
713  C CD  . LYS A 93  ? 0.1498 0.1635 0.1282 0.0214  -0.0036 -0.0077 95  LYS A CD  
714  C CE  . LYS A 93  ? 0.1276 0.1470 0.1115 0.0206  -0.0045 -0.0058 95  LYS A CE  
715  N NZ  . LYS A 93  ? 0.1295 0.1537 0.1180 0.0231  -0.0028 -0.0043 95  LYS A NZ  
716  N N   . ASP A 94  ? 0.1535 0.1443 0.1076 0.0120  -0.0102 -0.0103 96  ASP A N   
717  C CA  . ASP A 94  ? 0.1710 0.1549 0.1156 0.0095  -0.0106 -0.0110 96  ASP A CA  
718  C C   . ASP A 94  ? 0.1921 0.1733 0.1316 0.0119  -0.0061 -0.0131 96  ASP A C   
719  O O   . ASP A 94  ? 0.2027 0.1894 0.1456 0.0149  -0.0019 -0.0134 96  ASP A O   
720  C CB  . ASP A 94  ? 0.2041 0.1893 0.1450 0.0063  -0.0107 -0.0098 96  ASP A CB  
721  C CG  . ASP A 94  ? 0.2935 0.2703 0.2239 0.0024  -0.0128 -0.0100 96  ASP A CG  
722  O OD1 . ASP A 94  ? 0.3166 0.2875 0.2455 0.0013  -0.0165 -0.0098 96  ASP A OD1 
723  O OD2 . ASP A 94  ? 0.3572 0.3337 0.2813 0.0000  -0.0109 -0.0099 96  ASP A OD2 
724  N N   . GLY A 95  ? 0.2063 0.1786 0.1380 0.0106  -0.0073 -0.0143 97  GLY A N   
725  C CA  . GLY A 95  ? 0.2170 0.1842 0.1426 0.0129  -0.0033 -0.0167 97  GLY A CA  
726  C C   . GLY A 95  ? 0.2529 0.2178 0.1817 0.0160  -0.0037 -0.0174 97  GLY A C   
727  O O   . GLY A 95  ? 0.2908 0.2493 0.2137 0.0180  -0.0010 -0.0196 97  GLY A O   
728  N N   . ILE A 96  ? 0.2197 0.1891 0.1573 0.0164  -0.0069 -0.0158 98  ILE A N   
729  C CA  . ILE A 96  ? 0.1945 0.1615 0.1345 0.0181  -0.0081 -0.0160 98  ILE A CA  
730  C C   . ILE A 96  ? 0.2192 0.1821 0.1581 0.0146  -0.0134 -0.0148 98  ILE A C   
731  O O   . ILE A 96  ? 0.2291 0.1970 0.1742 0.0130  -0.0162 -0.0131 98  ILE A O   
732  C CB  . ILE A 96  ? 0.1575 0.1331 0.1080 0.0209  -0.0074 -0.0148 98  ILE A CB  
733  C CG1 . ILE A 96  ? 0.1756 0.1575 0.1294 0.0239  -0.0029 -0.0149 98  ILE A CG1 
734  C CG2 . ILE A 96  ? 0.1507 0.1224 0.1019 0.0221  -0.0088 -0.0149 98  ILE A CG2 
735  C CD1 . ILE A 96  ? 0.1963 0.1859 0.1593 0.0258  -0.0028 -0.0132 98  ILE A CD1 
736  N N   . GLU A 97  ? 0.2563 0.2098 0.1874 0.0132  -0.0150 -0.0156 99  GLU A N   
737  C CA  . GLU A 97  ? 0.2793 0.2298 0.2104 0.0095  -0.0204 -0.0139 99  GLU A CA  
738  C C   . GLU A 97  ? 0.2618 0.2175 0.2019 0.0108  -0.0217 -0.0127 99  GLU A C   
739  O O   . GLU A 97  ? 0.2499 0.2069 0.1922 0.0139  -0.0191 -0.0135 99  GLU A O   
740  C CB  . GLU A 97  ? 0.3210 0.2593 0.2400 0.0067  -0.0222 -0.0147 99  GLU A CB  
741  C CG  . GLU A 97  ? 0.3973 0.3296 0.3055 0.0047  -0.0207 -0.0161 99  GLU A CG  
742  C CD  . GLU A 97  ? 0.5669 0.4862 0.4621 0.0004  -0.0238 -0.0165 99  GLU A CD  
743  O OE1 . GLU A 97  ? 0.6060 0.5164 0.4904 0.0015  -0.0201 -0.0195 99  GLU A OE1 
744  O OE2 . GLU A 97  ? 0.6370 0.5549 0.5330 -0.0040 -0.0299 -0.0137 99  GLU A OE2 
745  N N   . PRO A 98  ? 0.2618 0.2209 0.2077 0.0082  -0.0257 -0.0105 100 PRO A N   
746  C CA  . PRO A 98  ? 0.2467 0.2117 0.2013 0.0090  -0.0263 -0.0094 100 PRO A CA  
747  C C   . PRO A 98  ? 0.2500 0.2098 0.2017 0.0075  -0.0285 -0.0088 100 PRO A C   
748  O O   . PRO A 98  ? 0.2723 0.2347 0.2286 0.0051  -0.0317 -0.0068 100 PRO A O   
749  C CB  . PRO A 98  ? 0.2608 0.2315 0.2228 0.0072  -0.0291 -0.0075 100 PRO A CB  
750  C CG  . PRO A 98  ? 0.2759 0.2403 0.2316 0.0040  -0.0325 -0.0066 100 PRO A CG  
751  C CD  . PRO A 98  ? 0.2665 0.2249 0.2123 0.0047  -0.0297 -0.0087 100 PRO A CD  
752  N N   . MET A 99  ? 0.2337 0.1862 0.1777 0.0091  -0.0266 -0.0106 101 MET A N   
753  C CA  . MET A 99  ? 0.2285 0.1732 0.1671 0.0074  -0.0290 -0.0102 101 MET A CA  
754  C C   . MET A 99  ? 0.2314 0.1726 0.1675 0.0114  -0.0257 -0.0120 101 MET A C   
755  O O   . MET A 99  ? 0.2347 0.1762 0.1697 0.0150  -0.0215 -0.0139 101 MET A O   
756  C CB  . MET A 99  ? 0.2490 0.1830 0.1767 0.0036  -0.0321 -0.0103 101 MET A CB  
757  C CG  . MET A 99  ? 0.3289 0.2568 0.2475 0.0050  -0.0289 -0.0129 101 MET A CG  
758  S SD  . MET A 99  ? 0.4967 0.4122 0.4019 -0.0013 -0.0337 -0.0123 101 MET A SD  
759  C CE  . MET A 99  ? 0.5059 0.4318 0.4207 -0.0041 -0.0371 -0.0091 101 MET A CE  
760  N N   . TRP A 100 ? 0.2455 0.1837 0.1814 0.0106  -0.0276 -0.0111 102 TRP A N   
761  C CA  . TRP A 100 ? 0.2738 0.2076 0.2078 0.0142  -0.0256 -0.0122 102 TRP A CA  
762  C C   . TRP A 100 ? 0.3046 0.2281 0.2291 0.0172  -0.0226 -0.0151 102 TRP A C   
763  O O   . TRP A 100 ? 0.3093 0.2335 0.2357 0.0222  -0.0188 -0.0164 102 TRP A O   
764  C CB  . TRP A 100 ? 0.2838 0.2134 0.2167 0.0115  -0.0294 -0.0103 102 TRP A CB  
765  C CG  . TRP A 100 ? 0.3314 0.2562 0.2631 0.0147  -0.0286 -0.0106 102 TRP A CG  
766  C CD1 . TRP A 100 ? 0.3556 0.2837 0.2916 0.0198  -0.0248 -0.0116 102 TRP A CD1 
767  C CD2 . TRP A 100 ? 0.3583 0.2740 0.2849 0.0126  -0.0322 -0.0095 102 TRP A CD2 
768  N NE1 . TRP A 100 ? 0.3727 0.2940 0.3067 0.0217  -0.0258 -0.0112 102 TRP A NE1 
769  C CE2 . TRP A 100 ? 0.3769 0.2900 0.3046 0.0172  -0.0303 -0.0100 102 TRP A CE2 
770  C CE3 . TRP A 100 ? 0.3822 0.2913 0.3030 0.0071  -0.0371 -0.0078 102 TRP A CE3 
771  C CZ2 . TRP A 100 ? 0.3950 0.2988 0.3184 0.0166  -0.0334 -0.0090 102 TRP A CZ2 
772  C CZ3 . TRP A 100 ? 0.3977 0.2978 0.3136 0.0061  -0.0400 -0.0068 102 TRP A CZ3 
773  C CH2 . TRP A 100 ? 0.3998 0.2968 0.3167 0.0109  -0.0382 -0.0075 102 TRP A CH2 
774  N N   . GLU A 101 ? 0.3167 0.2307 0.2308 0.0142  -0.0242 -0.0162 103 GLU A N   
775  C CA  . GLU A 101 ? 0.3266 0.2289 0.2295 0.0166  -0.0210 -0.0195 103 GLU A CA  
776  C C   . GLU A 101 ? 0.3306 0.2378 0.2348 0.0201  -0.0155 -0.0216 103 GLU A C   
777  O O   . GLU A 101 ? 0.3363 0.2360 0.2335 0.0236  -0.0112 -0.0246 103 GLU A O   
778  C CB  . GLU A 101 ? 0.3889 0.2789 0.2787 0.0113  -0.0244 -0.0200 103 GLU A CB  
779  C CG  . GLU A 101 ? 0.4714 0.3654 0.3605 0.0073  -0.0260 -0.0190 103 GLU A CG  
780  C CD  . GLU A 101 ? 0.6158 0.4955 0.4894 0.0024  -0.0286 -0.0199 103 GLU A CD  
781  O OE1 . GLU A 101 ? 0.6310 0.4999 0.4969 -0.0003 -0.0321 -0.0196 103 GLU A OE1 
782  O OE2 . GLU A 101 ? 0.6498 0.5284 0.5180 0.0007  -0.0274 -0.0208 103 GLU A OE2 
783  N N   . ASP A 102 ? 0.2963 0.2161 0.2094 0.0196  -0.0150 -0.0200 104 ASP A N   
784  C CA  . ASP A 102 ? 0.2809 0.2063 0.1959 0.0227  -0.0098 -0.0215 104 ASP A CA  
785  C C   . ASP A 102 ? 0.2757 0.2031 0.1953 0.0289  -0.0053 -0.0226 104 ASP A C   
786  O O   . ASP A 102 ? 0.2638 0.1945 0.1904 0.0302  -0.0071 -0.0209 104 ASP A O   
787  C CB  . ASP A 102 ? 0.2546 0.1929 0.1794 0.0214  -0.0107 -0.0193 104 ASP A CB  
788  C CG  . ASP A 102 ? 0.2750 0.2184 0.2000 0.0227  -0.0065 -0.0202 104 ASP A CG  
789  O OD1 . ASP A 102 ? 0.2392 0.1886 0.1698 0.0270  -0.0023 -0.0206 104 ASP A OD1 
790  O OD2 . ASP A 102 ? 0.2726 0.2143 0.1925 0.0192  -0.0076 -0.0202 104 ASP A OD2 
791  N N   . GLU A 103 ? 0.2875 0.2134 0.2036 0.0323  0.0001  -0.0251 105 GLU A N   
792  C CA  . GLU A 103 ? 0.3037 0.2326 0.2258 0.0387  0.0047  -0.0258 105 GLU A CA  
793  C C   . GLU A 103 ? 0.2767 0.2195 0.2131 0.0401  0.0038  -0.0225 105 GLU A C   
794  O O   . GLU A 103 ? 0.2832 0.2274 0.2257 0.0440  0.0042  -0.0216 105 GLU A O   
795  C CB  . GLU A 103 ? 0.3683 0.2980 0.2871 0.0416  0.0114  -0.0284 105 GLU A CB  
796  C CG  . GLU A 103 ? 0.5304 0.4601 0.4536 0.0488  0.0166  -0.0297 105 GLU A CG  
797  C CD  . GLU A 103 ? 0.6620 0.5754 0.5747 0.0513  0.0178  -0.0330 105 GLU A CD  
798  O OE1 . GLU A 103 ? 0.7401 0.6522 0.6556 0.0579  0.0229  -0.0347 105 GLU A OE1 
799  O OE2 . GLU A 103 ? 0.6764 0.5782 0.5783 0.0468  0.0135  -0.0338 105 GLU A OE2 
800  N N   . LYS A 104 ? 0.2484 0.2008 0.1895 0.0368  0.0024  -0.0207 106 LYS A N   
801  C CA  . LYS A 104 ? 0.2255 0.1898 0.1782 0.0373  0.0014  -0.0178 106 LYS A CA  
802  C C   . LYS A 104 ? 0.2028 0.1677 0.1592 0.0350  -0.0034 -0.0158 106 LYS A C   
803  O O   . LYS A 104 ? 0.1867 0.1598 0.1513 0.0354  -0.0040 -0.0135 106 LYS A O   
804  C CB  . LYS A 104 ? 0.2333 0.2063 0.1889 0.0347  0.0019  -0.0169 106 LYS A CB  
805  C CG  . LYS A 104 ? 0.3166 0.2922 0.2704 0.0367  0.0070  -0.0182 106 LYS A CG  
806  C CD  . LYS A 104 ? 0.4219 0.4044 0.3839 0.0416  0.0107  -0.0173 106 LYS A CD  
807  C CE  . LYS A 104 ? 0.5222 0.5109 0.4852 0.0431  0.0159  -0.0177 106 LYS A CE  
808  N NZ  . LYS A 104 ? 0.5866 0.5785 0.5561 0.0492  0.0202  -0.0176 106 LYS A NZ  
809  N N   . ASN A 105 ? 0.1978 0.1541 0.1477 0.0321  -0.0068 -0.0162 107 ASN A N   
810  C CA  . ASN A 105 ? 0.1820 0.1387 0.1349 0.0296  -0.0109 -0.0143 107 ASN A CA  
811  C C   . ASN A 105 ? 0.2191 0.1667 0.1682 0.0307  -0.0126 -0.0143 107 ASN A C   
812  O O   . ASN A 105 ? 0.2289 0.1782 0.1815 0.0289  -0.0156 -0.0122 107 ASN A O   
813  C CB  . ASN A 105 ? 0.1871 0.1430 0.1376 0.0247  -0.0143 -0.0138 107 ASN A CB  
814  C CG  . ASN A 105 ? 0.1768 0.1410 0.1316 0.0232  -0.0138 -0.0133 107 ASN A CG  
815  O OD1 . ASN A 105 ? 0.1511 0.1239 0.1129 0.0244  -0.0124 -0.0124 107 ASN A OD1 
816  N ND2 . ASN A 105 ? 0.2047 0.1661 0.1554 0.0203  -0.0155 -0.0136 107 ASN A ND2 
817  N N   . LYS A 106 ? 0.2362 0.1735 0.1777 0.0334  -0.0106 -0.0167 108 LYS A N   
818  C CA  . LYS A 106 ? 0.2590 0.1850 0.1951 0.0339  -0.0129 -0.0169 108 LYS A CA  
819  C C   . LYS A 106 ? 0.2356 0.1648 0.1791 0.0364  -0.0140 -0.0146 108 LYS A C   
820  O O   . LYS A 106 ? 0.2564 0.1800 0.1977 0.0340  -0.0181 -0.0131 108 LYS A O   
821  C CB  . LYS A 106 ? 0.3185 0.2315 0.2441 0.0370  -0.0099 -0.0204 108 LYS A CB  
822  C CG  . LYS A 106 ? 0.4230 0.3389 0.3514 0.0430  -0.0037 -0.0224 108 LYS A CG  
823  C CD  . LYS A 106 ? 0.5598 0.4608 0.4748 0.0446  -0.0006 -0.0266 108 LYS A CD  
824  C CE  . LYS A 106 ? 0.6387 0.5399 0.5563 0.0519  0.0061  -0.0289 108 LYS A CE  
825  N NZ  . LYS A 106 ? 0.6910 0.5769 0.5946 0.0536  0.0099  -0.0335 108 LYS A NZ  
826  N N   . ARG A 107 ? 0.2084 0.1466 0.1606 0.0405  -0.0109 -0.0138 109 ARG A N   
827  C CA  A ARG A 107 ? 0.2005 0.1425 0.1604 0.0425  -0.0124 -0.0110 109 ARG A CA  
828  C CA  B ARG A 107 ? 0.1948 0.1364 0.1544 0.0424  -0.0125 -0.0110 109 ARG A CA  
829  C C   . ARG A 107 ? 0.2034 0.1569 0.1704 0.0383  -0.0148 -0.0079 109 ARG A C   
830  O O   . ARG A 107 ? 0.2182 0.1764 0.1916 0.0388  -0.0163 -0.0051 109 ARG A O   
831  C CB  A ARG A 107 ? 0.2260 0.1723 0.1926 0.0490  -0.0080 -0.0111 109 ARG A CB  
832  C CB  B ARG A 107 ? 0.2070 0.1509 0.1721 0.0493  -0.0081 -0.0115 109 ARG A CB  
833  C CG  A ARG A 107 ? 0.2661 0.2022 0.2266 0.0541  -0.0041 -0.0146 109 ARG A CG  
834  C CG  B ARG A 107 ? 0.2330 0.1634 0.1917 0.0543  -0.0060 -0.0143 109 ARG A CG  
835  C CD  A ARG A 107 ? 0.2792 0.2182 0.2484 0.0614  -0.0008 -0.0139 109 ARG A CD  
836  C CD  B ARG A 107 ? 0.2210 0.1558 0.1889 0.0616  -0.0022 -0.0136 109 ARG A CD  
837  N NE  A ARG A 107 ? 0.3242 0.2529 0.2926 0.0642  -0.0036 -0.0131 109 ARG A NE  
838  N NE  B ARG A 107 ? 0.2005 0.1427 0.1785 0.0614  -0.0060 -0.0090 109 ARG A NE  
839  C CZ  A ARG A 107 ? 0.3648 0.2963 0.3401 0.0638  -0.0081 -0.0090 109 ARG A CZ  
840  C CZ  B ARG A 107 ? 0.2309 0.1661 0.2087 0.0614  -0.0105 -0.0069 109 ARG A CZ  
841  N NH1 A ARG A 107 ? 0.3612 0.3058 0.3445 0.0604  -0.0101 -0.0054 109 ARG A NH1 
842  N NH1 B ARG A 107 ? 0.2727 0.1926 0.2407 0.0618  -0.0119 -0.0092 109 ARG A NH1 
843  N NH2 A ARG A 107 ? 0.4049 0.3253 0.3781 0.0662  -0.0108 -0.0085 109 ARG A NH2 
844  N NH2 B ARG A 107 ? 0.2173 0.1599 0.2037 0.0603  -0.0141 -0.0024 109 ARG A NH2 
845  N N   . GLY A 108 ? 0.2010 0.1585 0.1667 0.0341  -0.0154 -0.0084 110 GLY A N   
846  C CA  . GLY A 108 ? 0.1855 0.1537 0.1574 0.0310  -0.0162 -0.0064 110 GLY A CA  
847  C C   . GLY A 108 ? 0.1615 0.1300 0.1333 0.0262  -0.0198 -0.0046 110 GLY A C   
848  O O   . GLY A 108 ? 0.1613 0.1225 0.1292 0.0249  -0.0226 -0.0039 110 GLY A O   
849  N N   . GLY A 109 ? 0.1539 0.1308 0.1294 0.0234  -0.0196 -0.0040 111 GLY A N   
850  C CA  . GLY A 109 ? 0.1405 0.1202 0.1170 0.0188  -0.0218 -0.0025 111 GLY A CA  
851  C C   . GLY A 109 ? 0.1503 0.1384 0.1304 0.0166  -0.0203 -0.0029 111 GLY A C   
852  O O   . GLY A 109 ? 0.1411 0.1319 0.1225 0.0185  -0.0181 -0.0042 111 GLY A O   
853  N N   . ARG A 110 ? 0.1465 0.1383 0.1279 0.0127  -0.0212 -0.0019 112 ARG A N   
854  C CA  . ARG A 110 ? 0.1325 0.1311 0.1171 0.0111  -0.0193 -0.0028 112 ARG A CA  
855  C C   . ARG A 110 ? 0.1359 0.1392 0.1219 0.0078  -0.0190 -0.0016 112 ARG A C   
856  O O   . ARG A 110 ? 0.1546 0.1561 0.1388 0.0053  -0.0209 0.0001  112 ARG A O   
857  C CB  . ARG A 110 ? 0.1619 0.1600 0.1467 0.0097  -0.0197 -0.0038 112 ARG A CB  
858  C CG  . ARG A 110 ? 0.1975 0.1957 0.1821 0.0059  -0.0215 -0.0025 112 ARG A CG  
859  C CD  . ARG A 110 ? 0.2776 0.2754 0.2632 0.0045  -0.0228 -0.0026 112 ARG A CD  
860  N NE  . ARG A 110 ? 0.3194 0.3174 0.3047 0.0005  -0.0247 -0.0008 112 ARG A NE  
861  C CZ  . ARG A 110 ? 0.3435 0.3431 0.3309 -0.0021 -0.0262 0.0002  112 ARG A CZ  
862  N NH1 . ARG A 110 ? 0.3305 0.3310 0.3177 -0.0062 -0.0279 0.0022  112 ARG A NH1 
863  N NH2 . ARG A 110 ? 0.3066 0.3071 0.2966 -0.0009 -0.0264 -0.0005 112 ARG A NH2 
864  N N   . TRP A 111 ? 0.1243 0.1328 0.1122 0.0074  -0.0168 -0.0025 113 TRP A N   
865  C CA  . TRP A 111 ? 0.1328 0.1454 0.1208 0.0037  -0.0156 -0.0023 113 TRP A CA  
866  C C   . TRP A 111 ? 0.1555 0.1705 0.1456 0.0025  -0.0140 -0.0040 113 TRP A C   
867  O O   . TRP A 111 ? 0.1508 0.1667 0.1433 0.0046  -0.0129 -0.0056 113 TRP A O   
868  C CB  . TRP A 111 ? 0.1243 0.1398 0.1124 0.0038  -0.0140 -0.0028 113 TRP A CB  
869  C CG  . TRP A 111 ? 0.1248 0.1398 0.1119 0.0038  -0.0157 -0.0003 113 TRP A CG  
870  C CD1 . TRP A 111 ? 0.1391 0.1542 0.1278 0.0070  -0.0162 0.0006  113 TRP A CD1 
871  C CD2 . TRP A 111 ? 0.1293 0.1441 0.1142 0.0003  -0.0175 0.0022  113 TRP A CD2 
872  N NE1 . TRP A 111 ? 0.1334 0.1489 0.1223 0.0061  -0.0182 0.0036  113 TRP A NE1 
873  C CE2 . TRP A 111 ? 0.1305 0.1453 0.1167 0.0019  -0.0195 0.0048  113 TRP A CE2 
874  C CE3 . TRP A 111 ? 0.1393 0.1544 0.1212 -0.0044 -0.0177 0.0027  113 TRP A CE3 
875  C CZ2 . TRP A 111 ? 0.1347 0.1493 0.1196 -0.0010 -0.0222 0.0081  113 TRP A CZ2 
876  C CZ3 . TRP A 111 ? 0.1397 0.1540 0.1190 -0.0077 -0.0203 0.0059  113 TRP A CZ3 
877  C CH2 . TRP A 111 ? 0.1410 0.1550 0.1219 -0.0060 -0.0228 0.0086  113 TRP A CH2 
878  N N   . LEU A 112 ? 0.1391 0.1557 0.1289 -0.0010 -0.0140 -0.0032 114 LEU A N   
879  C CA  . LEU A 112 ? 0.1536 0.1737 0.1472 -0.0020 -0.0126 -0.0042 114 LEU A CA  
880  C C   . LEU A 112 ? 0.1980 0.2232 0.1924 -0.0045 -0.0089 -0.0054 114 LEU A C   
881  O O   . LEU A 112 ? 0.1950 0.2206 0.1855 -0.0081 -0.0085 -0.0045 114 LEU A O   
882  C CB  . LEU A 112 ? 0.1626 0.1809 0.1554 -0.0044 -0.0154 -0.0021 114 LEU A CB  
883  C CG  . LEU A 112 ? 0.1949 0.2179 0.1925 -0.0061 -0.0145 -0.0021 114 LEU A CG  
884  C CD1 . LEU A 112 ? 0.1923 0.2148 0.1936 -0.0030 -0.0153 -0.0029 114 LEU A CD1 
885  C CD2 . LEU A 112 ? 0.2218 0.2432 0.2174 -0.0099 -0.0175 0.0005  114 LEU A CD2 
886  N N   . ILE A 113 ? 0.1898 0.2186 0.1893 -0.0029 -0.0062 -0.0075 115 ILE A N   
887  C CA  . ILE A 113 ? 0.2206 0.2543 0.2224 -0.0042 -0.0017 -0.0094 115 ILE A CA  
888  C C   . ILE A 113 ? 0.2277 0.2664 0.2362 -0.0048 -0.0013 -0.0088 115 ILE A C   
889  O O   . ILE A 113 ? 0.2005 0.2391 0.2139 -0.0022 -0.0032 -0.0084 115 ILE A O   
890  C CB  . ILE A 113 ? 0.2448 0.2780 0.2481 -0.0009 0.0007  -0.0122 115 ILE A CB  
891  C CG1 . ILE A 113 ? 0.2899 0.3184 0.2877 -0.0001 -0.0009 -0.0121 115 ILE A CG1 
892  C CG2 . ILE A 113 ? 0.2704 0.3071 0.2747 -0.0020 0.0060  -0.0148 115 ILE A CG2 
893  C CD1 . ILE A 113 ? 0.2968 0.3240 0.2881 -0.0037 -0.0013 -0.0109 115 ILE A CD1 
894  N N   . THR A 114 ? 0.2335 0.2768 0.2423 -0.0087 0.0008  -0.0081 116 THR A N   
895  C CA  . THR A 114 ? 0.2530 0.3028 0.2698 -0.0095 0.0016  -0.0072 116 THR A CA  
896  C C   . THR A 114 ? 0.2603 0.3168 0.2819 -0.0092 0.0079  -0.0097 116 THR A C   
897  O O   . THR A 114 ? 0.2937 0.3507 0.3097 -0.0121 0.0115  -0.0111 116 THR A O   
898  C CB  . THR A 114 ? 0.3170 0.3675 0.3312 -0.0144 -0.0011 -0.0040 116 THR A CB  
899  O OG1 . THR A 114 ? 0.3999 0.4510 0.4079 -0.0183 0.0016  -0.0044 116 THR A OG1 
900  C CG2 . THR A 114 ? 0.3055 0.3481 0.3145 -0.0143 -0.0070 -0.0017 116 THR A CG2 
901  N N   . LEU A 115 ? 0.2452 0.3067 0.2768 -0.0059 0.0094  -0.0104 117 LEU A N   
902  C CA  . LEU A 115 ? 0.3034 0.3709 0.3409 -0.0043 0.0159  -0.0133 117 LEU A CA  
903  C C   . LEU A 115 ? 0.3461 0.4236 0.3917 -0.0069 0.0182  -0.0114 117 LEU A C   
904  O O   . LEU A 115 ? 0.3526 0.4322 0.4014 -0.0090 0.0135  -0.0076 117 LEU A O   
905  C CB  . LEU A 115 ? 0.3185 0.3851 0.3633 0.0017  0.0163  -0.0151 117 LEU A CB  
906  C CG  . LEU A 115 ? 0.3815 0.4388 0.4199 0.0045  0.0134  -0.0163 117 LEU A CG  
907  C CD1 . LEU A 115 ? 0.3945 0.4512 0.4389 0.0095  0.0157  -0.0189 117 LEU A CD1 
908  C CD2 . LEU A 115 ? 0.4214 0.4732 0.4482 0.0021  0.0144  -0.0178 117 LEU A CD2 
909  N N   . ASN A 116 ? 0.3773 0.4607 0.4257 -0.0071 0.0254  -0.0141 118 ASN A N   
910  C CA  . ASN A 116 ? 0.4249 0.5202 0.4846 -0.0080 0.0291  -0.0129 118 ASN A CA  
911  C C   . ASN A 116 ? 0.4586 0.5581 0.5324 -0.0015 0.0299  -0.0135 118 ASN A C   
912  O O   . ASN A 116 ? 0.4777 0.5703 0.5504 0.0030  0.0286  -0.0156 118 ASN A O   
913  C CB  . ASN A 116 ? 0.4527 0.5526 0.5096 -0.0104 0.0379  -0.0163 118 ASN A CB  
914  C CG  . ASN A 116 ? 0.5272 0.6211 0.5687 -0.0161 0.0386  -0.0171 118 ASN A CG  
915  O OD1 . ASN A 116 ? 0.5682 0.6571 0.6018 -0.0201 0.0325  -0.0139 118 ASN A OD1 
916  N ND2 . ASN A 116 ? 0.5400 0.6337 0.5764 -0.0167 0.0460  -0.0213 118 ASN A ND2 
917  N N   . LYS A 117 ? 0.4764 0.5874 0.5636 -0.0013 0.0318  -0.0114 119 LYS A N   
918  C CA  . LYS A 117 ? 0.4875 0.6038 0.5900 0.0049  0.0327  -0.0115 119 LYS A CA  
919  C C   . LYS A 117 ? 0.4862 0.6008 0.5897 0.0102  0.0404  -0.0173 119 LYS A C   
920  O O   . LYS A 117 ? 0.4862 0.5965 0.5944 0.0158  0.0389  -0.0185 119 LYS A O   
921  C CB  . LYS A 117 ? 0.5217 0.6524 0.6398 0.0037  0.0335  -0.0076 119 LYS A CB  
922  C CG  . LYS A 117 ? 0.5948 0.7268 0.7104 -0.0026 0.0262  -0.0019 119 LYS A CG  
923  C CD  . LYS A 117 ? 0.6696 0.8099 0.7835 -0.0090 0.0302  -0.0007 119 LYS A CD  
924  C CE  . LYS A 117 ? 0.7284 0.8663 0.8355 -0.0160 0.0226  0.0043  119 LYS A CE  
925  N NZ  . LYS A 117 ? 0.7661 0.9136 0.8736 -0.0225 0.0262  0.0063  119 LYS A NZ  
926  N N   . GLN A 118 ? 0.4918 0.6084 0.5899 0.0081  0.0485  -0.0209 120 GLN A N   
927  C CA  . GLN A 118 ? 0.5205 0.6332 0.6169 0.0127  0.0562  -0.0270 120 GLN A CA  
928  C C   . GLN A 118 ? 0.5358 0.6342 0.6211 0.0149  0.0523  -0.0293 120 GLN A C   
929  O O   . GLN A 118 ? 0.5417 0.6355 0.6291 0.0203  0.0553  -0.0329 120 GLN A O   
930  C CB  . GLN A 118 ? 0.5760 0.6905 0.6633 0.0084  0.0647  -0.0306 120 GLN A CB  
931  C CG  . GLN A 118 ? 0.6542 0.7841 0.7544 0.0079  0.0720  -0.0301 120 GLN A CG  
932  C CD  . GLN A 118 ? 0.7433 0.8765 0.8332 0.0002  0.0771  -0.0308 120 GLN A CD  
933  O OE1 . GLN A 118 ? 0.7939 0.9174 0.8663 -0.0045 0.0766  -0.0325 120 GLN A OE1 
934  N NE2 . GLN A 118 ? 0.7350 0.8827 0.8360 -0.0016 0.0819  -0.0290 120 GLN A NE2 
935  N N   . GLN A 119 ? 0.5316 0.6230 0.6053 0.0106  0.0455  -0.0268 121 GLN A N   
936  C CA  . GLN A 119 ? 0.5317 0.6112 0.5957 0.0119  0.0413  -0.0279 121 GLN A CA  
937  C C   . GLN A 119 ? 0.5429 0.6198 0.6144 0.0166  0.0352  -0.0259 121 GLN A C   
938  O O   . GLN A 119 ? 0.5547 0.6222 0.6188 0.0179  0.0323  -0.0271 121 GLN A O   
939  C CB  . GLN A 119 ? 0.5206 0.5948 0.5711 0.0060  0.0367  -0.0258 121 GLN A CB  
940  C CG  . GLN A 119 ? 0.4953 0.5668 0.5337 0.0015  0.0415  -0.0284 121 GLN A CG  
941  C CD  . GLN A 119 ? 0.4960 0.5613 0.5229 -0.0031 0.0356  -0.0258 121 GLN A CD  
942  O OE1 . GLN A 119 ? 0.5120 0.5802 0.5398 -0.0061 0.0313  -0.0219 121 GLN A OE1 
943  N NE2 . GLN A 119 ? 0.4544 0.5109 0.4706 -0.0037 0.0349  -0.0276 121 GLN A NE2 
944  N N   . ARG A 120 ? 0.5326 0.6174 0.6183 0.0186  0.0328  -0.0226 122 ARG A N   
945  C CA  . ARG A 120 ? 0.5255 0.6072 0.6178 0.0227  0.0271  -0.0208 122 ARG A CA  
946  C C   . ARG A 120 ? 0.5259 0.6038 0.6222 0.0286  0.0307  -0.0246 122 ARG A C   
947  O O   . ARG A 120 ? 0.5385 0.6081 0.6316 0.0308  0.0263  -0.0246 122 ARG A O   
948  C CB  . ARG A 120 ? 0.5096 0.5999 0.6159 0.0230  0.0226  -0.0158 122 ARG A CB  
949  C CG  . ARG A 120 ? 0.4884 0.5724 0.5969 0.0258  0.0155  -0.0137 122 ARG A CG  
950  C CD  . ARG A 120 ? 0.4371 0.5271 0.5575 0.0258  0.0098  -0.0086 122 ARG A CD  
951  N NE  . ARG A 120 ? 0.3953 0.4863 0.5106 0.0200  0.0050  -0.0047 122 ARG A NE  
952  C CZ  . ARG A 120 ? 0.3406 0.4394 0.4655 0.0177  0.0013  0.0001  122 ARG A CZ  
953  N NH1 . ARG A 120 ? 0.2656 0.3732 0.4072 0.0209  0.0017  0.0021  122 ARG A NH1 
954  N NH2 . ARG A 120 ? 0.3186 0.4162 0.4366 0.0121  -0.0031 0.0032  122 ARG A NH2 
955  N N   . ARG A 121 ? 0.5047 0.5882 0.6078 0.0312  0.0387  -0.0278 123 ARG A N   
956  C CA  . ARG A 121 ? 0.5007 0.5792 0.6075 0.0374  0.0425  -0.0318 123 ARG A CA  
957  C C   . ARG A 121 ? 0.4878 0.5547 0.5780 0.0362  0.0457  -0.0367 123 ARG A C   
958  O O   . ARG A 121 ? 0.4955 0.5535 0.5837 0.0399  0.0449  -0.0389 123 ARG A O   
959  C CB  . ARG A 121 ? 0.5302 0.6190 0.6522 0.0417  0.0501  -0.0335 123 ARG A CB  
960  C CG  . ARG A 121 ? 0.5950 0.6796 0.7259 0.0495  0.0520  -0.0361 123 ARG A CG  
961  C CD  . ARG A 121 ? 0.6576 0.7513 0.8021 0.0544  0.0615  -0.0391 123 ARG A CD  
962  N NE  . ARG A 121 ? 0.7186 0.8081 0.8507 0.0529  0.0709  -0.0454 123 ARG A NE  
963  C CZ  . ARG A 121 ? 0.7308 0.8267 0.8701 0.0561  0.0812  -0.0493 123 ARG A CZ  
964  N NH1 . ARG A 121 ? 0.7166 0.8070 0.8417 0.0537  0.0893  -0.0551 123 ARG A NH1 
965  N NH2 . ARG A 121 ? 0.7302 0.8383 0.8910 0.0617  0.0835  -0.0474 123 ARG A NH2 
966  N N   . SER A 122 ? 0.4730 0.5396 0.5513 0.0307  0.0490  -0.0381 124 SER A N   
967  C CA  . SER A 122 ? 0.4827 0.5389 0.5450 0.0286  0.0523  -0.0425 124 SER A CA  
968  C C   . SER A 122 ? 0.4604 0.5076 0.5108 0.0256  0.0449  -0.0405 124 SER A C   
969  O O   . SER A 122 ? 0.4816 0.5188 0.5228 0.0260  0.0450  -0.0432 124 SER A O   
970  C CB  . SER A 122 ? 0.5316 0.5916 0.5862 0.0233  0.0582  -0.0441 124 SER A CB  
971  O OG  . SER A 122 ? 0.5809 0.6451 0.6327 0.0178  0.0532  -0.0395 124 SER A OG  
972  N N   . ASP A 123 ? 0.4131 0.4638 0.4639 0.0225  0.0387  -0.0358 125 ASP A N   
973  C CA  . ASP A 123 ? 0.3841 0.4282 0.4229 0.0187  0.0333  -0.0340 125 ASP A CA  
974  C C   . ASP A 123 ? 0.3041 0.3473 0.3464 0.0197  0.0255  -0.0300 125 ASP A C   
975  O O   . ASP A 123 ? 0.2681 0.3050 0.3015 0.0181  0.0219  -0.0293 125 ASP A O   
976  C CB  . ASP A 123 ? 0.4369 0.4837 0.4681 0.0127  0.0339  -0.0327 125 ASP A CB  
977  C CG  . ASP A 123 ? 0.5711 0.6154 0.5924 0.0094  0.0402  -0.0363 125 ASP A CG  
978  O OD1 . ASP A 123 ? 0.6029 0.6410 0.6202 0.0114  0.0436  -0.0402 125 ASP A OD1 
979  O OD2 . ASP A 123 ? 0.6299 0.6777 0.6466 0.0044  0.0413  -0.0351 125 ASP A OD2 
980  N N   . LEU A 124 ? 0.2595 0.3089 0.3139 0.0219  0.0228  -0.0271 126 LEU A N   
981  C CA  . LEU A 124 ? 0.2255 0.2731 0.2799 0.0213  0.0154  -0.0233 126 LEU A CA  
982  C C   . LEU A 124 ? 0.1931 0.2324 0.2435 0.0235  0.0122  -0.0238 126 LEU A C   
983  O O   . LEU A 124 ? 0.1783 0.2131 0.2207 0.0215  0.0083  -0.0225 126 LEU A O   
984  C CB  . LEU A 124 ? 0.2256 0.2801 0.2918 0.0221  0.0124  -0.0197 126 LEU A CB  
985  C CG  . LEU A 124 ? 0.2524 0.3037 0.3167 0.0208  0.0048  -0.0160 126 LEU A CG  
986  C CD1 . LEU A 124 ? 0.2684 0.3183 0.3233 0.0163  0.0028  -0.0144 126 LEU A CD1 
987  C CD2 . LEU A 124 ? 0.2792 0.3367 0.3560 0.0217  0.0015  -0.0124 126 LEU A CD2 
988  N N   . ASP A 125 ? 0.1776 0.2150 0.2336 0.0276  0.0137  -0.0257 127 ASP A N   
989  C CA  . ASP A 125 ? 0.1732 0.2027 0.2259 0.0293  0.0103  -0.0260 127 ASP A CA  
990  C C   . ASP A 125 ? 0.1633 0.1857 0.2023 0.0267  0.0113  -0.0280 127 ASP A C   
991  O O   . ASP A 125 ? 0.1693 0.1871 0.2025 0.0255  0.0069  -0.0264 127 ASP A O   
992  C CB  . ASP A 125 ? 0.2133 0.2414 0.2748 0.0343  0.0121  -0.0278 127 ASP A CB  
993  C CG  . ASP A 125 ? 0.3194 0.3541 0.3957 0.0372  0.0097  -0.0249 127 ASP A CG  
994  O OD1 . ASP A 125 ? 0.3211 0.3589 0.3991 0.0350  0.0046  -0.0209 127 ASP A OD1 
995  O OD2 . ASP A 125 ? 0.3819 0.4181 0.4679 0.0416  0.0127  -0.0264 127 ASP A OD2 
996  N N   . ARG A 126 ? 0.1640 0.1859 0.1976 0.0253  0.0169  -0.0312 128 ARG A N   
997  C CA  . ARG A 126 ? 0.1893 0.2040 0.2104 0.0226  0.0171  -0.0327 128 ARG A CA  
998  C C   . ARG A 126 ? 0.1717 0.1881 0.1866 0.0184  0.0138  -0.0297 128 ARG A C   
999  O O   . ARG A 126 ? 0.1783 0.1901 0.1863 0.0169  0.0108  -0.0287 128 ARG A O   
1000 C CB  . ARG A 126 ? 0.2631 0.2748 0.2783 0.0217  0.0236  -0.0371 128 ARG A CB  
1001 C CG  . ARG A 126 ? 0.3507 0.3675 0.3632 0.0182  0.0274  -0.0375 128 ARG A CG  
1002 C CD  . ARG A 126 ? 0.4390 0.4523 0.4465 0.0181  0.0347  -0.0424 128 ARG A CD  
1003 N NE  . ARG A 126 ? 0.4757 0.4937 0.4790 0.0138  0.0387  -0.0429 128 ARG A NE  
1004 C CZ  . ARG A 126 ? 0.5521 0.5677 0.5440 0.0079  0.0371  -0.0416 128 ARG A CZ  
1005 N NH1 . ARG A 126 ? 0.5681 0.5779 0.5527 0.0060  0.0319  -0.0398 128 ARG A NH1 
1006 N NH2 . ARG A 126 ? 0.5841 0.6037 0.5722 0.0037  0.0405  -0.0418 128 ARG A NH2 
1007 N N   . PHE A 127 ? 0.1596 0.1823 0.1771 0.0167  0.0142  -0.0281 129 PHE A N   
1008 C CA  . PHE A 127 ? 0.1625 0.1859 0.1747 0.0134  0.0108  -0.0252 129 PHE A CA  
1009 C C   . PHE A 127 ? 0.1364 0.1584 0.1501 0.0147  0.0054  -0.0225 129 PHE A C   
1010 O O   . PHE A 127 ? 0.1236 0.1431 0.1311 0.0130  0.0029  -0.0211 129 PHE A O   
1011 C CB  . PHE A 127 ? 0.1777 0.2071 0.1923 0.0112  0.0119  -0.0239 129 PHE A CB  
1012 C CG  . PHE A 127 ? 0.2354 0.2662 0.2450 0.0079  0.0165  -0.0257 129 PHE A CG  
1013 C CD1 . PHE A 127 ? 0.2744 0.3003 0.2760 0.0064  0.0193  -0.0283 129 PHE A CD1 
1014 C CD2 . PHE A 127 ? 0.2962 0.3328 0.3084 0.0056  0.0178  -0.0245 129 PHE A CD2 
1015 C CE1 . PHE A 127 ? 0.3155 0.3419 0.3111 0.0026  0.0236  -0.0299 129 PHE A CE1 
1016 C CE2 . PHE A 127 ? 0.3204 0.3582 0.3271 0.0017  0.0222  -0.0260 129 PHE A CE2 
1017 C CZ  . PHE A 127 ? 0.3212 0.3538 0.3194 0.0003  0.0250  -0.0287 129 PHE A CZ  
1018 N N   . TRP A 128 ? 0.1186 0.1423 0.1404 0.0174  0.0037  -0.0217 130 TRP A N   
1019 C CA  . TRP A 128 ? 0.1174 0.1388 0.1393 0.0181  -0.0013 -0.0193 130 TRP A CA  
1020 C C   . TRP A 128 ? 0.1298 0.1455 0.1465 0.0185  -0.0026 -0.0199 130 TRP A C   
1021 O O   . TRP A 128 ? 0.1216 0.1352 0.1330 0.0172  -0.0051 -0.0184 130 TRP A O   
1022 C CB  . TRP A 128 ? 0.1075 0.1316 0.1386 0.0200  -0.0034 -0.0178 130 TRP A CB  
1023 C CG  . TRP A 128 ? 0.1123 0.1334 0.1423 0.0199  -0.0086 -0.0153 130 TRP A CG  
1024 C CD1 . TRP A 128 ? 0.1208 0.1395 0.1546 0.0216  -0.0115 -0.0144 130 TRP A CD1 
1025 C CD2 . TRP A 128 ? 0.1110 0.1308 0.1355 0.0179  -0.0112 -0.0135 130 TRP A CD2 
1026 N NE1 . TRP A 128 ? 0.1167 0.1328 0.1469 0.0201  -0.0158 -0.0121 130 TRP A NE1 
1027 C CE2 . TRP A 128 ? 0.1196 0.1360 0.1438 0.0181  -0.0153 -0.0118 130 TRP A CE2 
1028 C CE3 . TRP A 128 ? 0.0981 0.1183 0.1171 0.0159  -0.0105 -0.0131 130 TRP A CE3 
1029 C CZ2 . TRP A 128 ? 0.1178 0.1313 0.1361 0.0166  -0.0179 -0.0103 130 TRP A CZ2 
1030 C CZ3 . TRP A 128 ? 0.1198 0.1370 0.1342 0.0150  -0.0133 -0.0115 130 TRP A CZ3 
1031 C CH2 . TRP A 128 ? 0.1149 0.1288 0.1286 0.0154  -0.0166 -0.0104 130 TRP A CH2 
1032 N N   . LEU A 129 ? 0.1385 0.1513 0.1562 0.0202  -0.0006 -0.0222 131 LEU A N   
1033 C CA  . LEU A 129 ? 0.1319 0.1385 0.1437 0.0199  -0.0022 -0.0226 131 LEU A CA  
1034 C C   . LEU A 129 ? 0.1303 0.1357 0.1330 0.0165  -0.0018 -0.0223 131 LEU A C   
1035 O O   . LEU A 129 ? 0.1288 0.1326 0.1277 0.0153  -0.0047 -0.0205 131 LEU A O   
1036 C CB  . LEU A 129 ? 0.1262 0.1284 0.1394 0.0220  0.0001  -0.0254 131 LEU A CB  
1037 C CG  . LEU A 129 ? 0.1531 0.1479 0.1596 0.0212  -0.0020 -0.0258 131 LEU A CG  
1038 C CD1 . LEU A 129 ? 0.1791 0.1726 0.1855 0.0208  -0.0073 -0.0226 131 LEU A CD1 
1039 C CD2 . LEU A 129 ? 0.1759 0.1651 0.1842 0.0240  0.0005  -0.0290 131 LEU A CD2 
1040 N N   . GLU A 130 ? 0.1343 0.1413 0.1339 0.0146  0.0014  -0.0236 132 GLU A N   
1041 C CA  . GLU A 130 ? 0.1299 0.1361 0.1215 0.0110  0.0011  -0.0226 132 GLU A CA  
1042 C C   . GLU A 130 ? 0.1418 0.1512 0.1337 0.0104  -0.0021 -0.0193 132 GLU A C   
1043 O O   . GLU A 130 ? 0.1564 0.1652 0.1442 0.0088  -0.0039 -0.0176 132 GLU A O   
1044 C CB  . GLU A 130 ? 0.1599 0.1671 0.1479 0.0085  0.0046  -0.0241 132 GLU A CB  
1045 C CG  . GLU A 130 ? 0.2923 0.2958 0.2786 0.0089  0.0089  -0.0279 132 GLU A CG  
1046 C CD  . GLU A 130 ? 0.3259 0.3219 0.3056 0.0081  0.0082  -0.0292 132 GLU A CD  
1047 O OE1 . GLU A 130 ? 0.2352 0.2297 0.2095 0.0053  0.0050  -0.0269 132 GLU A OE1 
1048 O OE2 . GLU A 130 ? 0.4445 0.4360 0.4247 0.0102  0.0110  -0.0325 132 GLU A OE2 
1049 N N   . THR A 131 ? 0.1111 0.1240 0.1080 0.0117  -0.0025 -0.0185 133 THR A N   
1050 C CA  . THR A 131 ? 0.0989 0.1133 0.0959 0.0118  -0.0052 -0.0159 133 THR A CA  
1051 C C   . THR A 131 ? 0.0987 0.1108 0.0949 0.0128  -0.0076 -0.0150 133 THR A C   
1052 O O   . THR A 131 ? 0.0957 0.1081 0.0888 0.0122  -0.0087 -0.0134 133 THR A O   
1053 C CB  . THR A 131 ? 0.1159 0.1327 0.1177 0.0127  -0.0056 -0.0154 133 THR A CB  
1054 O OG1 . THR A 131 ? 0.1269 0.1463 0.1291 0.0111  -0.0030 -0.0162 133 THR A OG1 
1055 C CG2 . THR A 131 ? 0.1207 0.1373 0.1209 0.0126  -0.0079 -0.0133 133 THR A CG2 
1056 N N   . LEU A 132 ? 0.0981 0.1081 0.0973 0.0144  -0.0084 -0.0158 134 LEU A N   
1057 C CA  . LEU A 132 ? 0.1018 0.1092 0.0994 0.0147  -0.0111 -0.0146 134 LEU A CA  
1058 C C   . LEU A 132 ? 0.1099 0.1157 0.1022 0.0129  -0.0112 -0.0143 134 LEU A C   
1059 O O   . LEU A 132 ? 0.1147 0.1209 0.1044 0.0121  -0.0126 -0.0126 134 LEU A O   
1060 C CB  . LEU A 132 ? 0.1185 0.1235 0.1205 0.0163  -0.0125 -0.0152 134 LEU A CB  
1061 C CG  . LEU A 132 ? 0.1304 0.1375 0.1387 0.0177  -0.0134 -0.0147 134 LEU A CG  
1062 C CD1 . LEU A 132 ? 0.1400 0.1450 0.1539 0.0195  -0.0149 -0.0149 134 LEU A CD1 
1063 C CD2 . LEU A 132 ? 0.1544 0.1612 0.1604 0.0168  -0.0159 -0.0127 134 LEU A CD2 
1064 N N   . LEU A 133 ? 0.1188 0.1228 0.1091 0.0119  -0.0095 -0.0159 135 LEU A N   
1065 C CA  . LEU A 133 ? 0.1137 0.1158 0.0983 0.0094  -0.0101 -0.0152 135 LEU A CA  
1066 C C   . LEU A 133 ? 0.1246 0.1309 0.1070 0.0075  -0.0102 -0.0130 135 LEU A C   
1067 O O   . LEU A 133 ? 0.1348 0.1419 0.1146 0.0057  -0.0116 -0.0110 135 LEU A O   
1068 C CB  . LEU A 133 ? 0.1160 0.1137 0.0974 0.0084  -0.0083 -0.0176 135 LEU A CB  
1069 C CG  . LEU A 133 ? 0.1475 0.1404 0.1319 0.0110  -0.0080 -0.0199 135 LEU A CG  
1070 C CD1 . LEU A 133 ? 0.1817 0.1694 0.1615 0.0099  -0.0058 -0.0226 135 LEU A CD1 
1071 C CD2 . LEU A 133 ? 0.1577 0.1477 0.1425 0.0114  -0.0116 -0.0184 135 LEU A CD2 
1072 N N   . CYS A 134 ? 0.1210 0.1305 0.1050 0.0077  -0.0089 -0.0129 136 CYS A N   
1073 C CA  . CYS A 134 ? 0.1080 0.1215 0.0913 0.0065  -0.0094 -0.0103 136 CYS A CA  
1074 C C   . CYS A 134 ? 0.1147 0.1304 0.0999 0.0083  -0.0105 -0.0086 136 CYS A C   
1075 O O   . CYS A 134 ? 0.1250 0.1437 0.1098 0.0075  -0.0110 -0.0063 136 CYS A O   
1076 C CB  . CYS A 134 ? 0.1255 0.1408 0.1099 0.0064  -0.0083 -0.0105 136 CYS A CB  
1077 S SG  . CYS A 134 ? 0.1604 0.1739 0.1403 0.0028  -0.0066 -0.0118 136 CYS A SG  
1078 N N   . LEU A 135 ? 0.1055 0.1197 0.0928 0.0105  -0.0107 -0.0096 137 LEU A N   
1079 C CA  . LEU A 135 ? 0.1131 0.1277 0.1005 0.0119  -0.0114 -0.0086 137 LEU A CA  
1080 C C   . LEU A 135 ? 0.1081 0.1224 0.0932 0.0106  -0.0122 -0.0077 137 LEU A C   
1081 O O   . LEU A 135 ? 0.1037 0.1214 0.0883 0.0101  -0.0118 -0.0058 137 LEU A O   
1082 C CB  . LEU A 135 ? 0.1063 0.1183 0.0953 0.0135  -0.0120 -0.0097 137 LEU A CB  
1083 C CG  . LEU A 135 ? 0.1157 0.1282 0.1057 0.0147  -0.0116 -0.0096 137 LEU A CG  
1084 C CD1 . LEU A 135 ? 0.1159 0.1303 0.1071 0.0139  -0.0107 -0.0097 137 LEU A CD1 
1085 C CD2 . LEU A 135 ? 0.1290 0.1386 0.1199 0.0153  -0.0130 -0.0102 137 LEU A CD2 
1086 N N   . ILE A 136 ? 0.1020 0.1125 0.0864 0.0101  -0.0135 -0.0087 138 ILE A N   
1087 C CA  . ILE A 136 ? 0.1153 0.1246 0.0968 0.0084  -0.0149 -0.0075 138 ILE A CA  
1088 C C   . ILE A 136 ? 0.1078 0.1194 0.0870 0.0058  -0.0149 -0.0059 138 ILE A C   
1089 O O   . ILE A 136 ? 0.1248 0.1384 0.1023 0.0041  -0.0155 -0.0040 138 ILE A O   
1090 C CB  . ILE A 136 ? 0.1192 0.1230 0.1006 0.0085  -0.0169 -0.0086 138 ILE A CB  
1091 C CG1 . ILE A 136 ? 0.1289 0.1293 0.1104 0.0082  -0.0168 -0.0102 138 ILE A CG1 
1092 C CG2 . ILE A 136 ? 0.1250 0.1275 0.1092 0.0106  -0.0175 -0.0093 138 ILE A CG2 
1093 C CD1 . ILE A 136 ? 0.1354 0.1298 0.1170 0.0085  -0.0192 -0.0108 138 ILE A CD1 
1094 N N   . GLY A 137 ? 0.1113 0.1226 0.0901 0.0048  -0.0143 -0.0065 139 GLY A N   
1095 C CA  . GLY A 137 ? 0.0928 0.1058 0.0688 0.0014  -0.0150 -0.0046 139 GLY A CA  
1096 C C   . GLY A 137 ? 0.1120 0.1319 0.0901 0.0009  -0.0145 -0.0018 139 GLY A C   
1097 O O   . GLY A 137 ? 0.1308 0.1529 0.1072 -0.0024 -0.0156 0.0005  139 GLY A O   
1098 N N   . GLU A 138 ? 0.0876 0.1106 0.0696 0.0041  -0.0131 -0.0019 140 GLU A N   
1099 C CA  . GLU A 138 ? 0.0870 0.1164 0.0725 0.0047  -0.0125 0.0007  140 GLU A CA  
1100 C C   . GLU A 138 ? 0.1106 0.1412 0.0955 0.0021  -0.0135 0.0022  140 GLU A C   
1101 O O   . GLU A 138 ? 0.0999 0.1354 0.0861 -0.0002 -0.0146 0.0056  140 GLU A O   
1102 C CB  . GLU A 138 ? 0.1047 0.1394 0.0914 0.0038  -0.0124 0.0035  140 GLU A CB  
1103 C CG  . GLU A 138 ? 0.0991 0.1324 0.0846 0.0053  -0.0114 0.0023  140 GLU A CG  
1104 C CD  . GLU A 138 ? 0.1424 0.1767 0.1304 0.0093  -0.0092 0.0014  140 GLU A CD  
1105 O OE1 . GLU A 138 ? 0.1528 0.1923 0.1450 0.0111  -0.0079 0.0031  140 GLU A OE1 
1106 O OE2 . GLU A 138 ? 0.1477 0.1769 0.1333 0.0106  -0.0090 -0.0009 140 GLU A OE2 
1107 N N   . SER A 139 ? 0.0987 0.1250 0.0818 0.0020  -0.0131 -0.0001 141 SER A N   
1108 C CA  . SER A 139 ? 0.1011 0.1266 0.0812 -0.0015 -0.0139 0.0005  141 SER A CA  
1109 C C   . SER A 139 ? 0.1314 0.1612 0.1144 -0.0018 -0.0147 0.0034  141 SER A C   
1110 O O   . SER A 139 ? 0.1550 0.1840 0.1348 -0.0056 -0.0159 0.0046  141 SER A O   
1111 C CB  . SER A 139 ? 0.1321 0.1521 0.1094 -0.0014 -0.0124 -0.0032 141 SER A CB  
1112 O OG  . SER A 139 ? 0.1471 0.1625 0.1224 -0.0010 -0.0120 -0.0056 141 SER A OG  
1113 N N   . PHE A 140 ? 0.0943 0.1278 0.0826 0.0018  -0.0143 0.0046  142 PHE A N   
1114 C CA  . PHE A 140 ? 0.1149 0.1520 0.1071 0.0025  -0.0153 0.0075  142 PHE A CA  
1115 C C   . PHE A 140 ? 0.1438 0.1880 0.1413 0.0028  -0.0163 0.0117  142 PHE A C   
1116 O O   . PHE A 140 ? 0.1430 0.1904 0.1457 0.0051  -0.0168 0.0140  142 PHE A O   
1117 C CB  . PHE A 140 ? 0.1154 0.1503 0.1097 0.0066  -0.0140 0.0056  142 PHE A CB  
1118 C CG  . PHE A 140 ? 0.1160 0.1456 0.1066 0.0062  -0.0129 0.0019  142 PHE A CG  
1119 C CD1 . PHE A 140 ? 0.1164 0.1438 0.1034 0.0029  -0.0133 0.0013  142 PHE A CD1 
1120 C CD2 . PHE A 140 ? 0.1181 0.1451 0.1088 0.0089  -0.0116 -0.0008 142 PHE A CD2 
1121 C CE1 . PHE A 140 ? 0.1325 0.1563 0.1174 0.0029  -0.0116 -0.0021 142 PHE A CE1 
1122 C CE2 . PHE A 140 ? 0.1058 0.1291 0.0949 0.0088  -0.0108 -0.0036 142 PHE A CE2 
1123 C CZ  . PHE A 140 ? 0.1148 0.1371 0.1018 0.0060  -0.0106 -0.0043 142 PHE A CZ  
1124 N N   . ASP A 141 ? 0.1876 0.2340 0.1840 0.0005  -0.0167 0.0128  143 ASP A N   
1125 C CA  . ASP A 141 ? 0.1999 0.2545 0.2018 0.0001  -0.0175 0.0172  143 ASP A CA  
1126 C C   . ASP A 141 ? 0.1674 0.2261 0.1761 0.0059  -0.0149 0.0172  143 ASP A C   
1127 O O   . ASP A 141 ? 0.1693 0.2241 0.1758 0.0088  -0.0125 0.0136  143 ASP A O   
1128 C CB  . ASP A 141 ? 0.2560 0.3139 0.2591 -0.0040 -0.0209 0.0216  143 ASP A CB  
1129 C CG  . ASP A 141 ? 0.3748 0.4282 0.3695 -0.0104 -0.0231 0.0215  143 ASP A CG  
1130 O OD1 . ASP A 141 ? 0.4245 0.4775 0.4164 -0.0123 -0.0230 0.0212  143 ASP A OD1 
1131 O OD2 . ASP A 141 ? 0.3706 0.4202 0.3609 -0.0136 -0.0248 0.0217  143 ASP A OD2 
1132 N N   . ASP A 142 ? 0.1589 0.2248 0.1756 0.0079  -0.0153 0.0212  144 ASP A N   
1133 C CA  . ASP A 142 ? 0.1641 0.2331 0.1867 0.0140  -0.0118 0.0206  144 ASP A CA  
1134 C C   . ASP A 142 ? 0.1499 0.2111 0.1698 0.0179  -0.0104 0.0166  144 ASP A C   
1135 O O   . ASP A 142 ? 0.1654 0.2249 0.1854 0.0220  -0.0071 0.0140  144 ASP A O   
1136 C CB  . ASP A 142 ? 0.1851 0.2628 0.2178 0.0159  -0.0125 0.0255  144 ASP A CB  
1137 C CG  . ASP A 142 ? 0.2600 0.3478 0.2976 0.0130  -0.0132 0.0300  144 ASP A CG  
1138 O OD1 . ASP A 142 ? 0.2997 0.3875 0.3329 0.0105  -0.0121 0.0287  144 ASP A OD1 
1139 O OD2 . ASP A 142 ? 0.3042 0.3998 0.3504 0.0130  -0.0150 0.0351  144 ASP A OD2 
1140 N N   . TYR A 143 ? 0.1195 0.1757 0.1364 0.0160  -0.0128 0.0162  145 TYR A N   
1141 C CA  . TYR A 143 ? 0.1165 0.1655 0.1306 0.0187  -0.0121 0.0130  145 TYR A CA  
1142 C C   . TYR A 143 ? 0.1332 0.1761 0.1409 0.0186  -0.0105 0.0085  145 TYR A C   
1143 O O   . TYR A 143 ? 0.1351 0.1726 0.1410 0.0209  -0.0098 0.0061  145 TYR A O   
1144 C CB  . TYR A 143 ? 0.1342 0.1806 0.1469 0.0160  -0.0152 0.0143  145 TYR A CB  
1145 C CG  . TYR A 143 ? 0.1677 0.2195 0.1869 0.0159  -0.0178 0.0194  145 TYR A CG  
1146 C CD1 . TYR A 143 ? 0.1749 0.2299 0.2016 0.0213  -0.0167 0.0211  145 TYR A CD1 
1147 C CD2 . TYR A 143 ? 0.2240 0.2777 0.2419 0.0105  -0.0212 0.0226  145 TYR A CD2 
1148 C CE1 . TYR A 143 ? 0.2102 0.2706 0.2445 0.0215  -0.0195 0.0264  145 TYR A CE1 
1149 C CE2 . TYR A 143 ? 0.2624 0.3211 0.2866 0.0098  -0.0244 0.0280  145 TYR A CE2 
1150 C CZ  . TYR A 143 ? 0.2534 0.3159 0.2866 0.0156  -0.0237 0.0301  145 TYR A CZ  
1151 O OH  . TYR A 143 ? 0.3064 0.3743 0.3471 0.0150  -0.0275 0.0360  145 TYR A OH  
1152 N N   . SER A 144 ? 0.1137 0.1572 0.1185 0.0159  -0.0103 0.0077  146 SER A N   
1153 C CA  . SER A 144 ? 0.1220 0.1604 0.1222 0.0163  -0.0089 0.0040  146 SER A CA  
1154 C C   . SER A 144 ? 0.1361 0.1733 0.1366 0.0203  -0.0064 0.0026  146 SER A C   
1155 O O   . SER A 144 ? 0.1289 0.1604 0.1253 0.0209  -0.0060 -0.0003 146 SER A O   
1156 C CB  . SER A 144 ? 0.1484 0.1874 0.1456 0.0129  -0.0095 0.0040  146 SER A CB  
1157 O OG  . SER A 144 ? 0.1629 0.1988 0.1569 0.0097  -0.0111 0.0032  146 SER A OG  
1158 N N   . ASP A 145 ? 0.1239 0.1662 0.1289 0.0229  -0.0047 0.0045  147 ASP A N   
1159 C CA  . ASP A 145 ? 0.1411 0.1815 0.1455 0.0268  -0.0015 0.0026  147 ASP A CA  
1160 C C   . ASP A 145 ? 0.1465 0.1794 0.1487 0.0295  -0.0017 0.0005  147 ASP A C   
1161 O O   . ASP A 145 ? 0.1604 0.1880 0.1585 0.0316  0.0003  -0.0021 147 ASP A O   
1162 C CB  . ASP A 145 ? 0.1555 0.2038 0.1665 0.0296  0.0010  0.0051  147 ASP A CB  
1163 C CG  . ASP A 145 ? 0.2036 0.2592 0.2157 0.0267  0.0018  0.0070  147 ASP A CG  
1164 O OD1 . ASP A 145 ? 0.2100 0.2624 0.2161 0.0234  0.0010  0.0055  147 ASP A OD1 
1165 O OD2 . ASP A 145 ? 0.2233 0.2877 0.2425 0.0275  0.0028  0.0103  147 ASP A OD2 
1166 N N   . ASP A 146 ? 0.1112 0.1430 0.1151 0.0289  -0.0043 0.0017  148 ASP A N   
1167 C CA  . ASP A 146 ? 0.0993 0.1237 0.1007 0.0306  -0.0050 0.0001  148 ASP A CA  
1168 C C   . ASP A 146 ? 0.1043 0.1229 0.0999 0.0279  -0.0063 -0.0024 148 ASP A C   
1169 O O   . ASP A 146 ? 0.1183 0.1304 0.1108 0.0288  -0.0070 -0.0038 148 ASP A O   
1170 C CB  . ASP A 146 ? 0.0968 0.1218 0.1016 0.0304  -0.0076 0.0026  148 ASP A CB  
1171 C CG  . ASP A 146 ? 0.1924 0.2192 0.2028 0.0349  -0.0067 0.0046  148 ASP A CG  
1172 O OD1 . ASP A 146 ? 0.2018 0.2351 0.2170 0.0368  -0.0044 0.0059  148 ASP A OD1 
1173 O OD2 . ASP A 146 ? 0.1856 0.2073 0.1961 0.0365  -0.0083 0.0050  148 ASP A OD2 
1174 N N   . VAL A 147 ? 0.1025 0.1231 0.0969 0.0249  -0.0069 -0.0028 149 VAL A N   
1175 C CA  . VAL A 147 ? 0.0979 0.1143 0.0888 0.0228  -0.0081 -0.0047 149 VAL A CA  
1176 C C   . VAL A 147 ? 0.1158 0.1274 0.1026 0.0240  -0.0071 -0.0067 149 VAL A C   
1177 O O   . VAL A 147 ? 0.1257 0.1389 0.1116 0.0246  -0.0054 -0.0068 149 VAL A O   
1178 C CB  . VAL A 147 ? 0.1013 0.1205 0.0925 0.0197  -0.0088 -0.0046 149 VAL A CB  
1179 C CG1 . VAL A 147 ? 0.1108 0.1261 0.1000 0.0185  -0.0097 -0.0066 149 VAL A CG1 
1180 C CG2 . VAL A 147 ? 0.1164 0.1387 0.1096 0.0176  -0.0098 -0.0029 149 VAL A CG2 
1181 N N   . CYS A 148 ? 0.1210 0.1267 0.1049 0.0237  -0.0084 -0.0080 150 CYS A N   
1182 C CA  . CYS A 148 ? 0.1157 0.1159 0.0945 0.0235  -0.0086 -0.0095 150 CYS A CA  
1183 C C   . CYS A 148 ? 0.1216 0.1216 0.1003 0.0208  -0.0106 -0.0098 150 CYS A C   
1184 O O   . CYS A 148 ? 0.1354 0.1338 0.1111 0.0199  -0.0107 -0.0103 150 CYS A O   
1185 C CB  . CYS A 148 ? 0.1171 0.1102 0.0922 0.0243  -0.0094 -0.0103 150 CYS A CB  
1186 S SG  . CYS A 148 ? 0.1729 0.1645 0.1482 0.0285  -0.0070 -0.0103 150 CYS A SG  
1187 N N   . GLY A 149 ? 0.0949 0.0967 0.0770 0.0194  -0.0120 -0.0094 151 GLY A N   
1188 C CA  . GLY A 149 ? 0.0958 0.0975 0.0794 0.0176  -0.0138 -0.0097 151 GLY A CA  
1189 C C   . GLY A 149 ? 0.0914 0.0955 0.0790 0.0166  -0.0143 -0.0095 151 GLY A C   
1190 O O   . GLY A 149 ? 0.1088 0.1146 0.0973 0.0167  -0.0135 -0.0090 151 GLY A O   
1191 N N   . ALA A 150 ? 0.1044 0.1089 0.0948 0.0155  -0.0156 -0.0097 152 ALA A N   
1192 C CA  . ALA A 150 ? 0.1029 0.1103 0.0976 0.0146  -0.0154 -0.0097 152 ALA A CA  
1193 C C   . ALA A 150 ? 0.1204 0.1269 0.1178 0.0137  -0.0177 -0.0091 152 ALA A C   
1194 O O   . ALA A 150 ? 0.1147 0.1185 0.1111 0.0136  -0.0196 -0.0088 152 ALA A O   
1195 C CB  . ALA A 150 ? 0.1082 0.1192 0.1058 0.0145  -0.0135 -0.0105 152 ALA A CB  
1196 N N   . VAL A 151 ? 0.1225 0.1314 0.1230 0.0125  -0.0178 -0.0086 153 VAL A N   
1197 C CA  . VAL A 151 ? 0.1304 0.1395 0.1344 0.0111  -0.0203 -0.0072 153 VAL A CA  
1198 C C   . VAL A 151 ? 0.1313 0.1469 0.1428 0.0107  -0.0186 -0.0073 153 VAL A C   
1199 O O   . VAL A 151 ? 0.1140 0.1323 0.1253 0.0101  -0.0161 -0.0079 153 VAL A O   
1200 C CB  . VAL A 151 ? 0.1516 0.1564 0.1509 0.0092  -0.0227 -0.0060 153 VAL A CB  
1201 C CG1 . VAL A 151 ? 0.1568 0.1622 0.1597 0.0069  -0.0261 -0.0039 153 VAL A CG1 
1202 C CG2 . VAL A 151 ? 0.1700 0.1677 0.1612 0.0101  -0.0233 -0.0065 153 VAL A CG2 
1203 N N   . VAL A 152 ? 0.1300 0.1482 0.1482 0.0109  -0.0199 -0.0065 154 VAL A N   
1204 C CA  . VAL A 152 ? 0.1386 0.1638 0.1653 0.0108  -0.0179 -0.0064 154 VAL A CA  
1205 C C   . VAL A 152 ? 0.1456 0.1726 0.1766 0.0086  -0.0215 -0.0034 154 VAL A C   
1206 O O   . VAL A 152 ? 0.1278 0.1517 0.1589 0.0082  -0.0255 -0.0018 154 VAL A O   
1207 C CB  . VAL A 152 ? 0.1575 0.1857 0.1907 0.0135  -0.0154 -0.0081 154 VAL A CB  
1208 C CG1 . VAL A 152 ? 0.1693 0.1946 0.2050 0.0149  -0.0189 -0.0070 154 VAL A CG1 
1209 C CG2 . VAL A 152 ? 0.1512 0.1870 0.1934 0.0137  -0.0123 -0.0082 154 VAL A CG2 
1210 N N   . ASN A 153 ? 0.1336 0.1651 0.1671 0.0064  -0.0204 -0.0025 155 ASN A N   
1211 C CA  . ASN A 153 ? 0.1620 0.1968 0.2005 0.0036  -0.0237 0.0007  155 ASN A CA  
1212 C C   . ASN A 153 ? 0.1490 0.1941 0.1998 0.0044  -0.0205 0.0010  155 ASN A C   
1213 O O   . ASN A 153 ? 0.1545 0.2038 0.2059 0.0043  -0.0159 -0.0008 155 ASN A O   
1214 C CB  . ASN A 153 ? 0.1721 0.2046 0.2043 -0.0001 -0.0250 0.0020  155 ASN A CB  
1215 C CG  . ASN A 153 ? 0.2337 0.2566 0.2540 -0.0001 -0.0263 0.0010  155 ASN A CG  
1216 O OD1 . ASN A 153 ? 0.2570 0.2786 0.2726 -0.0001 -0.0240 -0.0003 155 ASN A OD1 
1217 N ND2 . ASN A 153 ? 0.2533 0.2692 0.2686 -0.0003 -0.0299 0.0017  155 ASN A ND2 
1218 N N   . VAL A 154 ? 0.1440 0.1930 0.2040 0.0051  -0.0229 0.0031  156 VAL A N   
1219 C CA  . VAL A 154 ? 0.1599 0.2195 0.2338 0.0065  -0.0199 0.0037  156 VAL A CA  
1220 C C   . VAL A 154 ? 0.1470 0.2129 0.2259 0.0021  -0.0225 0.0078  156 VAL A C   
1221 O O   . VAL A 154 ? 0.1592 0.2226 0.2379 -0.0004 -0.0286 0.0113  156 VAL A O   
1222 C CB  . VAL A 154 ? 0.1711 0.2317 0.2541 0.0100  -0.0218 0.0045  156 VAL A CB  
1223 C CG1 . VAL A 154 ? 0.1794 0.2516 0.2784 0.0123  -0.0183 0.0052  156 VAL A CG1 
1224 C CG2 . VAL A 154 ? 0.1878 0.2415 0.2649 0.0136  -0.0199 0.0008  156 VAL A CG2 
1225 N N   . ARG A 155 ? 0.1437 0.2171 0.2258 0.0007  -0.0179 0.0072  157 ARG A N   
1226 C CA  . ARG A 155 ? 0.1902 0.2696 0.2754 -0.0044 -0.0199 0.0111  157 ARG A CA  
1227 C C   . ARG A 155 ? 0.2205 0.3133 0.3181 -0.0041 -0.0140 0.0111  157 ARG A C   
1228 O O   . ARG A 155 ? 0.2217 0.3164 0.3183 -0.0018 -0.0072 0.0071  157 ARG A O   
1229 C CB  . ARG A 155 ? 0.2212 0.2938 0.2928 -0.0085 -0.0209 0.0108  157 ARG A CB  
1230 C CG  . ARG A 155 ? 0.2329 0.2921 0.2918 -0.0091 -0.0262 0.0108  157 ARG A CG  
1231 C CD  . ARG A 155 ? 0.2886 0.3448 0.3480 -0.0120 -0.0332 0.0149  157 ARG A CD  
1232 N NE  . ARG A 155 ? 0.2954 0.3380 0.3408 -0.0127 -0.0371 0.0141  157 ARG A NE  
1233 C CZ  . ARG A 155 ? 0.2749 0.3106 0.3158 -0.0096 -0.0381 0.0123  157 ARG A CZ  
1234 N NH1 . ARG A 155 ? 0.1962 0.2363 0.2453 -0.0057 -0.0362 0.0112  157 ARG A NH1 
1235 N NH2 . ARG A 155 ? 0.2866 0.3106 0.3147 -0.0104 -0.0407 0.0115  157 ARG A NH2 
1236 N N   . ALA A 156 ? 0.2309 0.3331 0.3395 -0.0068 -0.0165 0.0157  158 ALA A N   
1237 C CA  . ALA A 156 ? 0.2656 0.3820 0.3863 -0.0073 -0.0106 0.0163  158 ALA A CA  
1238 C C   . ALA A 156 ? 0.2948 0.4117 0.4065 -0.0109 -0.0057 0.0141  158 ALA A C   
1239 O O   . ALA A 156 ? 0.3066 0.4314 0.4235 -0.0093 0.0020  0.0115  158 ALA A O   
1240 C CB  . ALA A 156 ? 0.2491 0.3751 0.3816 -0.0111 -0.0153 0.0226  158 ALA A CB  
1241 N N   . LYS A 157 ? 0.3174 0.4256 0.4155 -0.0157 -0.0100 0.0153  159 LYS A N   
1242 C CA  . LYS A 157 ? 0.3368 0.4440 0.4252 -0.0197 -0.0067 0.0139  159 LYS A CA  
1243 C C   . LYS A 157 ? 0.3448 0.4458 0.4245 -0.0164 -0.0014 0.0084  159 LYS A C   
1244 O O   . LYS A 157 ? 0.3738 0.4760 0.4477 -0.0193 0.0028  0.0070  159 LYS A O   
1245 C CB  . LYS A 157 ? 0.3981 0.4959 0.4746 -0.0253 -0.0139 0.0171  159 LYS A CB  
1246 C CG  . LYS A 157 ? 0.5100 0.6037 0.5748 -0.0297 -0.0127 0.0164  159 LYS A CG  
1247 C CD  . LYS A 157 ? 0.5964 0.6789 0.6499 -0.0341 -0.0204 0.0194  159 LYS A CD  
1248 C CE  . LYS A 157 ? 0.6663 0.7458 0.7100 -0.0394 -0.0203 0.0202  159 LYS A CE  
1249 N NZ  . LYS A 157 ? 0.7290 0.7979 0.7630 -0.0440 -0.0281 0.0235  159 LYS A NZ  
1250 N N   . GLY A 158 ? 0.3069 0.4009 0.3849 -0.0111 -0.0019 0.0057  160 GLY A N   
1251 C CA  . GLY A 158 ? 0.2745 0.3628 0.3449 -0.0082 0.0024  0.0010  160 GLY A CA  
1252 C C   . GLY A 158 ? 0.2348 0.3119 0.2980 -0.0053 -0.0020 0.0001  160 GLY A C   
1253 O O   . GLY A 158 ? 0.2468 0.3172 0.3034 -0.0074 -0.0077 0.0023  160 GLY A O   
1254 N N   . ASP A 159 ? 0.1961 0.2708 0.2603 -0.0005 0.0007  -0.0032 161 ASP A N   
1255 C CA  . ASP A 159 ? 0.1736 0.2390 0.2321 0.0022  -0.0032 -0.0039 161 ASP A CA  
1256 C C   . ASP A 159 ? 0.1635 0.2208 0.2088 0.0006  -0.0037 -0.0051 161 ASP A C   
1257 O O   . ASP A 159 ? 0.1828 0.2413 0.2237 -0.0016 -0.0004 -0.0063 161 ASP A O   
1258 C CB  . ASP A 159 ? 0.1533 0.2187 0.2170 0.0073  -0.0002 -0.0068 161 ASP A CB  
1259 C CG  . ASP A 159 ? 0.2020 0.2756 0.2804 0.0098  0.0004  -0.0055 161 ASP A CG  
1260 O OD1 . ASP A 159 ? 0.1988 0.2756 0.2828 0.0079  -0.0041 -0.0015 161 ASP A OD1 
1261 O OD2 . ASP A 159 ? 0.2398 0.3161 0.3241 0.0136  0.0054  -0.0083 161 ASP A OD2 
1262 N N   . LYS A 160 ? 0.1545 0.2038 0.1938 0.0018  -0.0079 -0.0048 162 LYS A N   
1263 C CA  . LYS A 160 ? 0.1361 0.1784 0.1646 0.0009  -0.0086 -0.0055 162 LYS A CA  
1264 C C   . LYS A 160 ? 0.1398 0.1766 0.1654 0.0045  -0.0092 -0.0072 162 LYS A C   
1265 O O   . LYS A 160 ? 0.1500 0.1856 0.1789 0.0063  -0.0117 -0.0066 162 LYS A O   
1266 C CB  . LYS A 160 ? 0.1670 0.2045 0.1900 -0.0018 -0.0133 -0.0029 162 LYS A CB  
1267 C CG  . LYS A 160 ? 0.2328 0.2746 0.2571 -0.0062 -0.0136 -0.0006 162 LYS A CG  
1268 C CD  . LYS A 160 ? 0.3335 0.3686 0.3519 -0.0088 -0.0190 0.0020  162 LYS A CD  
1269 C CE  . LYS A 160 ? 0.4755 0.5114 0.4987 -0.0095 -0.0227 0.0043  162 LYS A CE  
1270 N NZ  . LYS A 160 ? 0.5418 0.5706 0.5583 -0.0131 -0.0280 0.0069  162 LYS A NZ  
1271 N N   . ILE A 161 ? 0.1293 0.1632 0.1486 0.0048  -0.0074 -0.0088 163 ILE A N   
1272 C CA  . ILE A 161 ? 0.1207 0.1496 0.1362 0.0073  -0.0083 -0.0099 163 ILE A CA  
1273 C C   . ILE A 161 ? 0.1232 0.1479 0.1313 0.0063  -0.0097 -0.0090 163 ILE A C   
1274 O O   . ILE A 161 ? 0.1322 0.1579 0.1377 0.0040  -0.0087 -0.0087 163 ILE A O   
1275 C CB  . ILE A 161 ? 0.1252 0.1549 0.1413 0.0089  -0.0048 -0.0124 163 ILE A CB  
1276 C CG1 . ILE A 161 ? 0.1290 0.1626 0.1537 0.0108  -0.0032 -0.0133 163 ILE A CG1 
1277 C CG2 . ILE A 161 ? 0.1117 0.1367 0.1232 0.0104  -0.0060 -0.0129 163 ILE A CG2 
1278 C CD1 . ILE A 161 ? 0.1654 0.1990 0.1903 0.0122  0.0008  -0.0163 163 ILE A CD1 
1279 N N   . ALA A 162 ? 0.1265 0.1464 0.1314 0.0080  -0.0121 -0.0086 164 ALA A N   
1280 C CA  . ALA A 162 ? 0.1352 0.1516 0.1346 0.0079  -0.0130 -0.0078 164 ALA A CA  
1281 C C   . ALA A 162 ? 0.1158 0.1297 0.1128 0.0103  -0.0131 -0.0084 164 ALA A C   
1282 O O   . ALA A 162 ? 0.1331 0.1456 0.1309 0.0117  -0.0138 -0.0089 164 ALA A O   
1283 C CB  . ALA A 162 ? 0.1464 0.1590 0.1433 0.0069  -0.0158 -0.0062 164 ALA A CB  
1284 N N   . ILE A 163 ? 0.0883 0.1019 0.0826 0.0105  -0.0126 -0.0079 165 ILE A N   
1285 C CA  . ILE A 163 ? 0.0978 0.1098 0.0903 0.0126  -0.0127 -0.0078 165 ILE A CA  
1286 C C   . ILE A 163 ? 0.1117 0.1198 0.1017 0.0139  -0.0141 -0.0067 165 ILE A C   
1287 O O   . ILE A 163 ? 0.1132 0.1210 0.1025 0.0131  -0.0148 -0.0054 165 ILE A O   
1288 C CB  . ILE A 163 ? 0.0996 0.1145 0.0917 0.0121  -0.0114 -0.0075 165 ILE A CB  
1289 C CG1 . ILE A 163 ? 0.1143 0.1308 0.1075 0.0114  -0.0100 -0.0091 165 ILE A CG1 
1290 C CG2 . ILE A 163 ? 0.1041 0.1185 0.0954 0.0143  -0.0116 -0.0066 165 ILE A CG2 
1291 C CD1 . ILE A 163 ? 0.1087 0.1267 0.1001 0.0099  -0.0092 -0.0088 165 ILE A CD1 
1292 N N   . TRP A 164 ? 0.0937 0.0982 0.0817 0.0158  -0.0145 -0.0073 166 TRP A N   
1293 C CA  . TRP A 164 ? 0.0979 0.0972 0.0826 0.0177  -0.0151 -0.0070 166 TRP A CA  
1294 C C   . TRP A 164 ? 0.1182 0.1192 0.1034 0.0203  -0.0133 -0.0067 166 TRP A C   
1295 O O   . TRP A 164 ? 0.1274 0.1313 0.1133 0.0208  -0.0120 -0.0071 166 TRP A O   
1296 C CB  . TRP A 164 ? 0.1038 0.0976 0.0847 0.0180  -0.0159 -0.0081 166 TRP A CB  
1297 C CG  . TRP A 164 ? 0.1226 0.1143 0.1032 0.0154  -0.0183 -0.0077 166 TRP A CG  
1298 C CD1 . TRP A 164 ? 0.1382 0.1344 0.1230 0.0130  -0.0189 -0.0070 166 TRP A CD1 
1299 C CD2 . TRP A 164 ? 0.1227 0.1073 0.0983 0.0145  -0.0205 -0.0079 166 TRP A CD2 
1300 N NE1 . TRP A 164 ? 0.1479 0.1415 0.1320 0.0108  -0.0214 -0.0063 166 TRP A NE1 
1301 C CE2 . TRP A 164 ? 0.1381 0.1242 0.1161 0.0114  -0.0228 -0.0067 166 TRP A CE2 
1302 C CE3 . TRP A 164 ? 0.1373 0.1143 0.1060 0.0158  -0.0204 -0.0090 166 TRP A CE3 
1303 C CZ2 . TRP A 164 ? 0.1665 0.1467 0.1405 0.0092  -0.0259 -0.0060 166 TRP A CZ2 
1304 C CZ3 . TRP A 164 ? 0.1910 0.1608 0.1543 0.0135  -0.0232 -0.0088 166 TRP A CZ3 
1305 C CH2 . TRP A 164 ? 0.1847 0.1562 0.1507 0.0101  -0.0263 -0.0071 166 TRP A CH2 
1306 N N   . THR A 165 ? 0.1021 0.1013 0.0872 0.0219  -0.0136 -0.0056 167 THR A N   
1307 C CA  . THR A 165 ? 0.1100 0.1116 0.0972 0.0249  -0.0119 -0.0048 167 THR A CA  
1308 C C   . THR A 165 ? 0.1397 0.1344 0.1241 0.0285  -0.0113 -0.0056 167 THR A C   
1309 O O   . THR A 165 ? 0.1521 0.1399 0.1324 0.0279  -0.0129 -0.0063 167 THR A O   
1310 C CB  . THR A 165 ? 0.1196 0.1264 0.1111 0.0241  -0.0128 -0.0021 167 THR A CB  
1311 O OG1 . THR A 165 ? 0.1346 0.1378 0.1262 0.0249  -0.0146 -0.0006 167 THR A OG1 
1312 C CG2 . THR A 165 ? 0.1074 0.1181 0.0994 0.0200  -0.0135 -0.0017 167 THR A CG2 
1313 N N   . THR A 166 ? 0.1391 0.1359 0.1255 0.0320  -0.0087 -0.0055 168 THR A N   
1314 C CA  . THR A 166 ? 0.1506 0.1410 0.1335 0.0358  -0.0065 -0.0073 168 THR A CA  
1315 C C   . THR A 166 ? 0.1663 0.1515 0.1500 0.0389  -0.0074 -0.0065 168 THR A C   
1316 O O   . THR A 166 ? 0.1903 0.1668 0.1687 0.0413  -0.0064 -0.0085 168 THR A O   
1317 C CB  . THR A 166 ? 0.1670 0.1627 0.1521 0.0383  -0.0026 -0.0077 168 THR A CB  
1318 O OG1 . THR A 166 ? 0.2061 0.1949 0.1857 0.0413  0.0004  -0.0104 168 THR A OG1 
1319 C CG2 . THR A 166 ? 0.1408 0.1447 0.1347 0.0408  -0.0018 -0.0048 168 THR A CG2 
1320 N N   . GLU A 167 ? 0.1686 0.1584 0.1582 0.0385  -0.0095 -0.0034 169 GLU A N   
1321 C CA  . GLU A 167 ? 0.1768 0.1629 0.1691 0.0421  -0.0105 -0.0019 169 GLU A CA  
1322 C C   . GLU A 167 ? 0.1760 0.1630 0.1701 0.0386  -0.0149 0.0012  169 GLU A C   
1323 O O   . GLU A 167 ? 0.1939 0.1890 0.1934 0.0369  -0.0158 0.0040  169 GLU A O   
1324 C CB  . GLU A 167 ? 0.1894 0.1823 0.1895 0.0469  -0.0075 -0.0005 169 GLU A CB  
1325 C CG  . GLU A 167 ? 0.1963 0.1863 0.2014 0.0515  -0.0084 0.0016  169 GLU A CG  
1326 C CD  . GLU A 167 ? 0.2368 0.2132 0.2350 0.0541  -0.0088 -0.0009 169 GLU A CD  
1327 O OE1 . GLU A 167 ? 0.2505 0.2212 0.2441 0.0576  -0.0047 -0.0044 169 GLU A OE1 
1328 O OE2 . GLU A 167 ? 0.2630 0.2338 0.2593 0.0520  -0.0132 0.0008  169 GLU A OE2 
1329 N N   . CYS A 168 ? 0.1763 0.1548 0.1651 0.0369  -0.0177 0.0009  170 CYS A N   
1330 C CA  . CYS A 168 ? 0.2131 0.1924 0.2024 0.0324  -0.0218 0.0038  170 CYS A CA  
1331 C C   . CYS A 168 ? 0.2273 0.2086 0.2226 0.0342  -0.0240 0.0076  170 CYS A C   
1332 O O   . CYS A 168 ? 0.2361 0.2201 0.2320 0.0297  -0.0272 0.0105  170 CYS A O   
1333 C CB  . CYS A 168 ? 0.2259 0.1960 0.2080 0.0297  -0.0244 0.0029  170 CYS A CB  
1334 S SG  . CYS A 168 ? 0.2971 0.2535 0.2751 0.0345  -0.0255 0.0022  170 CYS A SG  
1335 N N   . GLU A 169 ? 0.2250 0.2054 0.2250 0.0405  -0.0222 0.0079  171 GLU A N   
1336 C CA  A GLU A 169 ? 0.2354 0.2181 0.2430 0.0432  -0.0245 0.0120  171 GLU A CA  
1337 C CA  B GLU A 169 ? 0.2309 0.2139 0.2383 0.0426  -0.0248 0.0122  171 GLU A CA  
1338 C C   . GLU A 169 ? 0.2369 0.2322 0.2532 0.0435  -0.0233 0.0147  171 GLU A C   
1339 O O   . GLU A 169 ? 0.2600 0.2588 0.2841 0.0454  -0.0255 0.0189  171 GLU A O   
1340 C CB  A GLU A 169 ? 0.2769 0.2517 0.2861 0.0506  -0.0230 0.0110  171 GLU A CB  
1341 C CB  B GLU A 169 ? 0.2586 0.2324 0.2669 0.0490  -0.0247 0.0118  171 GLU A CB  
1342 C CG  A GLU A 169 ? 0.3360 0.2965 0.3361 0.0504  -0.0250 0.0089  171 GLU A CG  
1343 C CG  B GLU A 169 ? 0.2662 0.2268 0.2650 0.0472  -0.0272 0.0101  171 GLU A CG  
1344 C CD  A GLU A 169 ? 0.3825 0.3366 0.3824 0.0487  -0.0309 0.0126  171 GLU A CD  
1345 C CD  B GLU A 169 ? 0.3247 0.2745 0.3234 0.0538  -0.0271 0.0093  171 GLU A CD  
1346 O OE1 A GLU A 169 ? 0.3986 0.3591 0.4061 0.0481  -0.0338 0.0171  171 GLU A OE1 
1347 O OE1 B GLU A 169 ? 0.3507 0.3009 0.3565 0.0564  -0.0299 0.0131  171 GLU A OE1 
1348 O OE2 A GLU A 169 ? 0.3628 0.3051 0.3545 0.0474  -0.0332 0.0112  171 GLU A OE2 
1349 O OE2 B GLU A 169 ? 0.3274 0.2678 0.3189 0.0564  -0.0243 0.0051  171 GLU A OE2 
1350 N N   . ASN A 170 ? 0.1987 0.2004 0.2141 0.0417  -0.0201 0.0127  172 ASN A N   
1351 C CA  . ASN A 170 ? 0.1923 0.2053 0.2141 0.0403  -0.0196 0.0153  172 ASN A CA  
1352 C C   . ASN A 170 ? 0.2094 0.2255 0.2292 0.0332  -0.0236 0.0180  172 ASN A C   
1353 O O   . ASN A 170 ? 0.1987 0.2174 0.2143 0.0288  -0.0227 0.0164  172 ASN A O   
1354 C CB  . ASN A 170 ? 0.2368 0.2544 0.2577 0.0409  -0.0151 0.0124  172 ASN A CB  
1355 C CG  . ASN A 170 ? 0.3159 0.3337 0.3397 0.0473  -0.0104 0.0105  172 ASN A CG  
1356 O OD1 . ASN A 170 ? 0.3544 0.3713 0.3841 0.0526  -0.0099 0.0119  172 ASN A OD1 
1357 N ND2 . ASN A 170 ? 0.2954 0.3144 0.3153 0.0470  -0.0067 0.0072  172 ASN A ND2 
1358 N N   . ARG A 171 ? 0.2162 0.2315 0.2388 0.0319  -0.0280 0.0223  173 ARG A N   
1359 C CA  . ARG A 171 ? 0.2315 0.2476 0.2504 0.0246  -0.0320 0.0248  173 ARG A CA  
1360 C C   . ARG A 171 ? 0.2037 0.2279 0.2227 0.0202  -0.0315 0.0258  173 ARG A C   
1361 O O   . ARG A 171 ? 0.2080 0.2314 0.2202 0.0147  -0.0313 0.0241  173 ARG A O   
1362 C CB  . ARG A 171 ? 0.2821 0.2967 0.3050 0.0242  -0.0373 0.0302  173 ARG A CB  
1363 C CG  . ARG A 171 ? 0.3951 0.4111 0.4135 0.0158  -0.0415 0.0334  173 ARG A CG  
1364 C CD  . ARG A 171 ? 0.5186 0.5316 0.5396 0.0145  -0.0476 0.0389  173 ARG A CD  
1365 N NE  . ARG A 171 ? 0.6297 0.6488 0.6619 0.0182  -0.0497 0.0439  173 ARG A NE  
1366 C CZ  . ARG A 171 ? 0.7277 0.7548 0.7634 0.0144  -0.0520 0.0481  173 ARG A CZ  
1367 N NH1 . ARG A 171 ? 0.7652 0.7941 0.7930 0.0067  -0.0521 0.0475  173 ARG A NH1 
1368 N NH2 . ARG A 171 ? 0.7415 0.7747 0.7889 0.0182  -0.0541 0.0530  173 ARG A NH2 
1369 N N   . GLU A 172 ? 0.1930 0.2248 0.2197 0.0223  -0.0311 0.0286  174 GLU A N   
1370 C CA  . GLU A 172 ? 0.1925 0.2312 0.2188 0.0175  -0.0314 0.0301  174 GLU A CA  
1371 C C   . GLU A 172 ? 0.1765 0.2149 0.1971 0.0166  -0.0272 0.0250  174 GLU A C   
1372 O O   . GLU A 172 ? 0.1672 0.2056 0.1819 0.0111  -0.0276 0.0242  174 GLU A O   
1373 C CB  . GLU A 172 ? 0.2419 0.2896 0.2785 0.0200  -0.0320 0.0345  174 GLU A CB  
1374 C CG  . GLU A 172 ? 0.3852 0.4347 0.4275 0.0185  -0.0377 0.0409  174 GLU A CG  
1375 C CD  . GLU A 172 ? 0.6080 0.6632 0.6635 0.0253  -0.0377 0.0446  174 GLU A CD  
1376 O OE1 . GLU A 172 ? 0.6628 0.7132 0.7217 0.0294  -0.0394 0.0457  174 GLU A OE1 
1377 O OE2 . GLU A 172 ? 0.6737 0.7383 0.7363 0.0266  -0.0360 0.0465  174 GLU A OE2 
1378 N N   . ALA A 173 ? 0.1498 0.1872 0.1718 0.0220  -0.0233 0.0216  175 ALA A N   
1379 C CA  . ALA A 173 ? 0.1619 0.1983 0.1786 0.0212  -0.0199 0.0172  175 ALA A CA  
1380 C C   . ALA A 173 ? 0.1604 0.1906 0.1695 0.0177  -0.0203 0.0143  175 ALA A C   
1381 O O   . ALA A 173 ? 0.1395 0.1703 0.1443 0.0139  -0.0197 0.0127  175 ALA A O   
1382 C CB  . ALA A 173 ? 0.1584 0.1936 0.1768 0.0270  -0.0162 0.0145  175 ALA A CB  
1383 N N   . VAL A 174 ? 0.1412 0.1654 0.1485 0.0190  -0.0213 0.0136  176 VAL A N   
1384 C CA  . VAL A 174 ? 0.1440 0.1633 0.1452 0.0160  -0.0213 0.0110  176 VAL A CA  
1385 C C   . VAL A 174 ? 0.1332 0.1544 0.1312 0.0098  -0.0230 0.0124  176 VAL A C   
1386 O O   . VAL A 174 ? 0.1358 0.1566 0.1297 0.0070  -0.0214 0.0097  176 VAL A O   
1387 C CB  . VAL A 174 ? 0.1503 0.1628 0.1501 0.0178  -0.0229 0.0109  176 VAL A CB  
1388 C CG1 . VAL A 174 ? 0.1942 0.2034 0.1887 0.0134  -0.0237 0.0096  176 VAL A CG1 
1389 C CG2 . VAL A 174 ? 0.1604 0.1689 0.1605 0.0233  -0.0205 0.0083  176 VAL A CG2 
1390 N N   . THR A 175 ? 0.1406 0.1636 0.1404 0.0077  -0.0263 0.0166  177 THR A N   
1391 C CA  A THR A 175 ? 0.1446 0.1679 0.1393 0.0010  -0.0279 0.0179  177 THR A CA  
1392 C CA  B THR A 175 ? 0.1450 0.1686 0.1400 0.0010  -0.0280 0.0181  177 THR A CA  
1393 C C   . THR A 175 ? 0.1445 0.1715 0.1373 -0.0016 -0.0262 0.0169  177 THR A C   
1394 O O   . THR A 175 ? 0.1539 0.1795 0.1408 -0.0058 -0.0249 0.0148  177 THR A O   
1395 C CB  A THR A 175 ? 0.1573 0.1802 0.1530 -0.0016 -0.0326 0.0230  177 THR A CB  
1396 C CB  B THR A 175 ? 0.1575 0.1817 0.1548 -0.0009 -0.0327 0.0235  177 THR A CB  
1397 O OG1 A THR A 175 ? 0.1728 0.2002 0.1757 0.0010  -0.0345 0.0268  177 THR A OG1 
1398 O OG1 B THR A 175 ? 0.1565 0.1760 0.1551 0.0016  -0.0345 0.0244  177 THR A OG1 
1399 C CG2 A THR A 175 ? 0.1460 0.1632 0.1411 -0.0004 -0.0345 0.0234  177 THR A CG2 
1400 C CG2 B THR A 175 ? 0.1678 0.1918 0.1586 -0.0087 -0.0348 0.0253  177 THR A CG2 
1401 N N   . HIS A 176 ? 0.1532 0.1846 0.1508 0.0008  -0.0259 0.0182  178 HIS A N   
1402 C CA  . HIS A 176 ? 0.1402 0.1740 0.1352 -0.0018 -0.0246 0.0173  178 HIS A CA  
1403 C C   . HIS A 176 ? 0.1286 0.1595 0.1199 -0.0010 -0.0210 0.0121  178 HIS A C   
1404 O O   . HIS A 176 ? 0.1287 0.1580 0.1145 -0.0048 -0.0200 0.0102  178 HIS A O   
1405 C CB  . HIS A 176 ? 0.1684 0.2080 0.1696 0.0006  -0.0249 0.0198  178 HIS A CB  
1406 C CG  . HIS A 176 ? 0.1859 0.2272 0.1838 -0.0029 -0.0243 0.0193  178 HIS A CG  
1407 N ND1 . HIS A 176 ? 0.2259 0.2673 0.2192 -0.0093 -0.0271 0.0220  178 HIS A ND1 
1408 C CD2 . HIS A 176 ? 0.1963 0.2379 0.1935 -0.0014 -0.0218 0.0166  178 HIS A CD2 
1409 C CE1 . HIS A 176 ? 0.2267 0.2682 0.2168 -0.0111 -0.0260 0.0205  178 HIS A CE1 
1410 N NE2 . HIS A 176 ? 0.2026 0.2445 0.1954 -0.0064 -0.0229 0.0175  178 HIS A NE2 
1411 N N   . ILE A 177 ? 0.1315 0.1611 0.1254 0.0038  -0.0191 0.0097  179 ILE A N   
1412 C CA  . ILE A 177 ? 0.1116 0.1385 0.1029 0.0046  -0.0164 0.0055  179 ILE A CA  
1413 C C   . ILE A 177 ? 0.1209 0.1452 0.1078 0.0011  -0.0158 0.0037  179 ILE A C   
1414 O O   . ILE A 177 ? 0.1352 0.1586 0.1192 -0.0005 -0.0139 0.0011  179 ILE A O   
1415 C CB  . ILE A 177 ? 0.1282 0.1533 0.1220 0.0095  -0.0153 0.0039  179 ILE A CB  
1416 C CG1 . ILE A 177 ? 0.1225 0.1508 0.1200 0.0127  -0.0145 0.0048  179 ILE A CG1 
1417 C CG2 . ILE A 177 ? 0.1182 0.1405 0.1099 0.0097  -0.0135 0.0002  179 ILE A CG2 
1418 C CD1 . ILE A 177 ? 0.1491 0.1750 0.1482 0.0174  -0.0134 0.0037  179 ILE A CD1 
1419 N N   . GLY A 178 ? 0.1177 0.1404 0.1040 0.0000  -0.0173 0.0050  180 GLY A N   
1420 C CA  . GLY A 178 ? 0.1193 0.1404 0.1016 -0.0037 -0.0164 0.0035  180 GLY A CA  
1421 C C   . GLY A 178 ? 0.1420 0.1634 0.1190 -0.0087 -0.0156 0.0034  180 GLY A C   
1422 O O   . GLY A 178 ? 0.1372 0.1577 0.1113 -0.0103 -0.0126 0.0002  180 GLY A O   
1423 N N   . ARG A 179 ? 0.1349 0.1574 0.1108 -0.0113 -0.0184 0.0069  181 ARG A N   
1424 C CA  . ARG A 179 ? 0.1387 0.1601 0.1077 -0.0171 -0.0183 0.0070  181 ARG A CA  
1425 C C   . ARG A 179 ? 0.1553 0.1757 0.1220 -0.0167 -0.0153 0.0035  181 ARG A C   
1426 O O   . ARG A 179 ? 0.1713 0.1889 0.1322 -0.0196 -0.0125 0.0005  181 ARG A O   
1427 C CB  . ARG A 179 ? 0.1851 0.2080 0.1540 -0.0201 -0.0227 0.0121  181 ARG A CB  
1428 C CG  . ARG A 179 ? 0.2331 0.2555 0.2025 -0.0218 -0.0260 0.0157  181 ARG A CG  
1429 C CD  . ARG A 179 ? 0.2910 0.3146 0.2591 -0.0263 -0.0306 0.0209  181 ARG A CD  
1430 N NE  . ARG A 179 ? 0.3638 0.3874 0.3351 -0.0266 -0.0351 0.0256  181 ARG A NE  
1431 C CZ  . ARG A 179 ? 0.4239 0.4442 0.3903 -0.0307 -0.0366 0.0266  181 ARG A CZ  
1432 N NH1 . ARG A 179 ? 0.4492 0.4691 0.4191 -0.0307 -0.0415 0.0314  181 ARG A NH1 
1433 N NH2 . ARG A 179 ? 0.3657 0.3833 0.3240 -0.0348 -0.0332 0.0229  181 ARG A NH2 
1434 N N   . VAL A 180 ? 0.1483 0.1706 0.1196 -0.0131 -0.0158 0.0039  182 VAL A N   
1435 C CA  . VAL A 180 ? 0.1440 0.1648 0.1133 -0.0126 -0.0138 0.0012  182 VAL A CA  
1436 C C   . VAL A 180 ? 0.1352 0.1539 0.1052 -0.0099 -0.0102 -0.0034 182 VAL A C   
1437 O O   . VAL A 180 ? 0.1423 0.1578 0.1083 -0.0111 -0.0080 -0.0063 182 VAL A O   
1438 C CB  . VAL A 180 ? 0.1493 0.1732 0.1233 -0.0099 -0.0154 0.0033  182 VAL A CB  
1439 C CG1 . VAL A 180 ? 0.1796 0.2011 0.1512 -0.0097 -0.0138 0.0006  182 VAL A CG1 
1440 C CG2 . VAL A 180 ? 0.1620 0.1891 0.1364 -0.0130 -0.0189 0.0082  182 VAL A CG2 
1441 N N   . TYR A 181 ? 0.1342 0.1542 0.1091 -0.0064 -0.0098 -0.0038 183 TYR A N   
1442 C CA  . TYR A 181 ? 0.1362 0.1552 0.1132 -0.0040 -0.0071 -0.0073 183 TYR A CA  
1443 C C   . TYR A 181 ? 0.1481 0.1659 0.1211 -0.0072 -0.0042 -0.0096 183 TYR A C   
1444 O O   . TYR A 181 ? 0.1405 0.1568 0.1130 -0.0066 -0.0012 -0.0129 183 TYR A O   
1445 C CB  . TYR A 181 ? 0.1263 0.1466 0.1082 -0.0008 -0.0080 -0.0066 183 TYR A CB  
1446 C CG  . TYR A 181 ? 0.1110 0.1310 0.0961 0.0015  -0.0063 -0.0091 183 TYR A CG  
1447 C CD1 . TYR A 181 ? 0.1169 0.1360 0.1031 0.0030  -0.0045 -0.0116 183 TYR A CD1 
1448 C CD2 . TYR A 181 ? 0.1022 0.1227 0.0897 0.0021  -0.0069 -0.0086 183 TYR A CD2 
1449 C CE1 . TYR A 181 ? 0.1149 0.1344 0.1056 0.0053  -0.0037 -0.0132 183 TYR A CE1 
1450 C CE2 . TYR A 181 ? 0.1008 0.1217 0.0921 0.0040  -0.0061 -0.0101 183 TYR A CE2 
1451 C CZ  . TYR A 181 ? 0.1329 0.1538 0.1263 0.0055  -0.0044 -0.0123 183 TYR A CZ  
1452 O OH  . TYR A 181 ? 0.1515 0.1735 0.1499 0.0072  -0.0042 -0.0130 183 TYR A OH  
1453 N N   . LYS A 182 ? 0.1553 0.1737 0.1255 -0.0107 -0.0052 -0.0077 184 LYS A N   
1454 C CA  . LYS A 182 ? 0.1525 0.1700 0.1175 -0.0148 -0.0022 -0.0095 184 LYS A CA  
1455 C C   . LYS A 182 ? 0.1774 0.1911 0.1353 -0.0176 -0.0002 -0.0117 184 LYS A C   
1456 O O   . LYS A 182 ? 0.1643 0.1766 0.1204 -0.0177 0.0042  -0.0154 184 LYS A O   
1457 C CB  . LYS A 182 ? 0.1610 0.1788 0.1226 -0.0191 -0.0047 -0.0062 184 LYS A CB  
1458 C CG  . LYS A 182 ? 0.1768 0.1939 0.1319 -0.0242 -0.0015 -0.0078 184 LYS A CG  
1459 C CD  . LYS A 182 ? 0.1842 0.2021 0.1376 -0.0279 -0.0038 -0.0048 184 LYS A CD  
1460 C CE  . LYS A 182 ? 0.1759 0.1923 0.1200 -0.0347 -0.0011 -0.0057 184 LYS A CE  
1461 N NZ  . LYS A 182 ? 0.1876 0.2046 0.1295 -0.0390 -0.0039 -0.0023 184 LYS A NZ  
1462 N N   . GLU A 183 ? 0.1848 0.1969 0.1391 -0.0197 -0.0032 -0.0093 185 GLU A N   
1463 C CA  . GLU A 183 ? 0.2079 0.2153 0.1544 -0.0230 -0.0022 -0.0108 185 GLU A CA  
1464 C C   . GLU A 183 ? 0.2167 0.2216 0.1652 -0.0190 0.0007  -0.0148 185 GLU A C   
1465 O O   . GLU A 183 ? 0.2332 0.2335 0.1762 -0.0202 0.0044  -0.0186 185 GLU A O   
1466 C CB  . GLU A 183 ? 0.2537 0.2616 0.1986 -0.0256 -0.0073 -0.0061 185 GLU A CB  
1467 C CG  . GLU A 183 ? 0.3633 0.3671 0.3016 -0.0289 -0.0084 -0.0060 185 GLU A CG  
1468 C CD  . GLU A 183 ? 0.3557 0.3638 0.2981 -0.0293 -0.0136 -0.0005 185 GLU A CD  
1469 O OE1 . GLU A 183 ? 0.3882 0.3955 0.3303 -0.0292 -0.0147 -0.0001 185 GLU A OE1 
1470 O OE2 . GLU A 183 ? 0.3297 0.3420 0.2759 -0.0299 -0.0164 0.0035  185 GLU A OE2 
1471 N N   . ARG A 184 ? 0.1753 0.1828 0.1316 -0.0140 -0.0009 -0.0141 186 ARG A N   
1472 C CA  . ARG A 184 ? 0.1805 0.1856 0.1396 -0.0101 0.0009  -0.0172 186 ARG A CA  
1473 C C   . ARG A 184 ? 0.1967 0.2021 0.1598 -0.0071 0.0051  -0.0209 186 ARG A C   
1474 O O   . ARG A 184 ? 0.2147 0.2162 0.1774 -0.0052 0.0076  -0.0242 186 ARG A O   
1475 C CB  . ARG A 184 ? 0.1762 0.1840 0.1416 -0.0065 -0.0022 -0.0149 186 ARG A CB  
1476 C CG  . ARG A 184 ? 0.2216 0.2292 0.1837 -0.0091 -0.0055 -0.0118 186 ARG A CG  
1477 C CD  . ARG A 184 ? 0.2411 0.2431 0.1975 -0.0108 -0.0055 -0.0132 186 ARG A CD  
1478 N NE  . ARG A 184 ? 0.1991 0.1996 0.1598 -0.0066 -0.0050 -0.0152 186 ARG A NE  
1479 C CZ  . ARG A 184 ? 0.1878 0.1892 0.1507 -0.0054 -0.0074 -0.0134 186 ARG A CZ  
1480 N NH1 . ARG A 184 ? 0.1846 0.1894 0.1469 -0.0077 -0.0102 -0.0096 186 ARG A NH1 
1481 N NH2 . ARG A 184 ? 0.1910 0.1903 0.1571 -0.0021 -0.0072 -0.0151 186 ARG A NH2 
1482 N N   . LEU A 185 ? 0.1931 0.2030 0.1605 -0.0066 0.0059  -0.0203 187 LEU A N   
1483 C CA  . LEU A 185 ? 0.1831 0.1949 0.1544 -0.0049 0.0100  -0.0231 187 LEU A CA  
1484 C C   . LEU A 185 ? 0.2181 0.2270 0.1822 -0.0083 0.0148  -0.0263 187 LEU A C   
1485 O O   . LEU A 185 ? 0.2392 0.2490 0.2067 -0.0061 0.0194  -0.0296 187 LEU A O   
1486 C CB  . LEU A 185 ? 0.1690 0.1862 0.1455 -0.0047 0.0091  -0.0210 187 LEU A CB  
1487 C CG  . LEU A 185 ? 0.1714 0.1909 0.1549 -0.0011 0.0055  -0.0188 187 LEU A CG  
1488 C CD1 . LEU A 185 ? 0.1731 0.1958 0.1584 -0.0024 0.0039  -0.0163 187 LEU A CD1 
1489 C CD2 . LEU A 185 ? 0.1841 0.2040 0.1746 0.0032  0.0065  -0.0206 187 LEU A CD2 
1490 N N   . GLY A 186 ? 0.2064 0.2120 0.1607 -0.0137 0.0137  -0.0252 188 GLY A N   
1491 C CA  . GLY A 186 ? 0.2216 0.2231 0.1667 -0.0178 0.0182  -0.0282 188 GLY A CA  
1492 C C   . GLY A 186 ? 0.2118 0.2177 0.1568 -0.0204 0.0211  -0.0284 188 GLY A C   
1493 O O   . GLY A 186 ? 0.2247 0.2288 0.1651 -0.0221 0.0268  -0.0321 188 GLY A O   
1494 N N   . LEU A 187 ? 0.1905 0.2016 0.1402 -0.0208 0.0175  -0.0244 189 LEU A N   
1495 C CA  . LEU A 187 ? 0.1898 0.2053 0.1399 -0.0235 0.0198  -0.0241 189 LEU A CA  
1496 C C   . LEU A 187 ? 0.2203 0.2322 0.1580 -0.0311 0.0199  -0.0232 189 LEU A C   
1497 O O   . LEU A 187 ? 0.2338 0.2423 0.1660 -0.0342 0.0151  -0.0202 189 LEU A O   
1498 C CB  . LEU A 187 ? 0.1994 0.2196 0.1563 -0.0225 0.0152  -0.0199 189 LEU A CB  
1499 C CG  . LEU A 187 ? 0.2108 0.2342 0.1789 -0.0161 0.0139  -0.0198 189 LEU A CG  
1500 C CD1 . LEU A 187 ? 0.2064 0.2324 0.1786 -0.0159 0.0093  -0.0158 189 LEU A CD1 
1501 C CD2 . LEU A 187 ? 0.2357 0.2627 0.2103 -0.0132 0.0190  -0.0230 189 LEU A CD2 
1502 N N   . PRO A 188 ? 0.2368 0.2498 0.1703 -0.0346 0.0251  -0.0256 190 PRO A N   
1503 C CA  . PRO A 188 ? 0.2310 0.2407 0.1518 -0.0429 0.0247  -0.0242 190 PRO A CA  
1504 C C   . PRO A 188 ? 0.1859 0.1972 0.1071 -0.0460 0.0173  -0.0180 190 PRO A C   
1505 O O   . PRO A 188 ? 0.1792 0.1953 0.1096 -0.0426 0.0149  -0.0158 190 PRO A O   
1506 C CB  . PRO A 188 ? 0.2650 0.2782 0.1847 -0.0450 0.0318  -0.0274 190 PRO A CB  
1507 C CG  . PRO A 188 ? 0.2863 0.3020 0.2156 -0.0375 0.0375  -0.0321 190 PRO A CG  
1508 C CD  . PRO A 188 ? 0.2547 0.2723 0.1946 -0.0314 0.0319  -0.0295 190 PRO A CD  
1509 N N   . PRO A 189 ? 0.1838 0.1906 0.0948 -0.0525 0.0134  -0.0150 191 PRO A N   
1510 C CA  . PRO A 189 ? 0.1800 0.1881 0.0920 -0.0553 0.0062  -0.0087 191 PRO A CA  
1511 C C   . PRO A 189 ? 0.1851 0.1976 0.1010 -0.0561 0.0061  -0.0071 191 PRO A C   
1512 O O   . PRO A 189 ? 0.1869 0.2013 0.1095 -0.0538 0.0007  -0.0030 191 PRO A O   
1513 C CB  . PRO A 189 ? 0.1941 0.1965 0.0926 -0.0638 0.0037  -0.0066 191 PRO A CB  
1514 C CG  . PRO A 189 ? 0.2035 0.2009 0.0965 -0.0631 0.0071  -0.0108 191 PRO A CG  
1515 C CD  . PRO A 189 ? 0.1913 0.1909 0.0893 -0.0578 0.0149  -0.0168 191 PRO A CD  
1516 N N   . LYS A 190 ? 0.1896 0.2038 0.1014 -0.0595 0.0121  -0.0101 192 LYS A N   
1517 C CA  . LYS A 190 ? 0.1988 0.2175 0.1133 -0.0618 0.0119  -0.0081 192 LYS A CA  
1518 C C   . LYS A 190 ? 0.2110 0.2354 0.1390 -0.0548 0.0119  -0.0082 192 LYS A C   
1519 O O   . LYS A 190 ? 0.2259 0.2531 0.1564 -0.0566 0.0097  -0.0054 192 LYS A O   
1520 C CB  . LYS A 190 ? 0.2455 0.2656 0.1519 -0.0678 0.0190  -0.0112 192 LYS A CB  
1521 C CG  . LYS A 190 ? 0.3242 0.3479 0.2363 -0.0624 0.0277  -0.0174 192 LYS A CG  
1522 C CD  . LYS A 190 ? 0.4131 0.4384 0.3177 -0.0676 0.0362  -0.0213 192 LYS A CD  
1523 C CE  . LYS A 190 ? 0.5010 0.5328 0.4074 -0.0719 0.0364  -0.0186 192 LYS A CE  
1524 N NZ  . LYS A 190 ? 0.5886 0.6242 0.4901 -0.0760 0.0460  -0.0226 192 LYS A NZ  
1525 N N   . ILE A 191 ? 0.1944 0.2197 0.1300 -0.0476 0.0139  -0.0112 193 ILE A N   
1526 C CA  . ILE A 191 ? 0.2114 0.2412 0.1591 -0.0412 0.0132  -0.0111 193 ILE A CA  
1527 C C   . ILE A 191 ? 0.2206 0.2479 0.1718 -0.0382 0.0061  -0.0073 193 ILE A C   
1528 O O   . ILE A 191 ? 0.2249 0.2498 0.1777 -0.0344 0.0046  -0.0078 193 ILE A O   
1529 C CB  . ILE A 191 ? 0.2285 0.2601 0.1828 -0.0351 0.0183  -0.0158 193 ILE A CB  
1530 C CG1 . ILE A 191 ? 0.2617 0.2957 0.2131 -0.0373 0.0265  -0.0202 193 ILE A CG1 
1531 C CG2 . ILE A 191 ? 0.2392 0.2754 0.2058 -0.0293 0.0168  -0.0150 193 ILE A CG2 
1532 C CD1 . ILE A 191 ? 0.2899 0.3302 0.2432 -0.0407 0.0293  -0.0194 193 ILE A CD1 
1533 N N   . VAL A 192 ? 0.2329 0.2606 0.1851 -0.0401 0.0017  -0.0035 194 VAL A N   
1534 C CA  . VAL A 192 ? 0.2514 0.2758 0.2060 -0.0374 -0.0047 0.0001  194 VAL A CA  
1535 C C   . VAL A 192 ? 0.2526 0.2783 0.2161 -0.0306 -0.0051 -0.0009 194 VAL A C   
1536 O O   . VAL A 192 ? 0.2619 0.2911 0.2297 -0.0300 -0.0030 -0.0020 194 VAL A O   
1537 C CB  . VAL A 192 ? 0.3126 0.3349 0.2636 -0.0422 -0.0097 0.0047  194 VAL A CB  
1538 C CG1 . VAL A 192 ? 0.3455 0.3665 0.2865 -0.0504 -0.0094 0.0060  194 VAL A CG1 
1539 C CG2 . VAL A 192 ? 0.3714 0.3959 0.3265 -0.0421 -0.0100 0.0053  194 VAL A CG2 
1540 N N   . ILE A 193 ? 0.2256 0.2489 0.1919 -0.0260 -0.0078 -0.0004 195 ILE A N   
1541 C CA  . ILE A 193 ? 0.2024 0.2255 0.1755 -0.0203 -0.0093 -0.0006 195 ILE A CA  
1542 C C   . ILE A 193 ? 0.1749 0.1939 0.1480 -0.0190 -0.0146 0.0028  195 ILE A C   
1543 O O   . ILE A 193 ? 0.1759 0.1928 0.1461 -0.0206 -0.0173 0.0054  195 ILE A O   
1544 C CB  . ILE A 193 ? 0.2084 0.2321 0.1849 -0.0156 -0.0071 -0.0034 195 ILE A CB  
1545 C CG1 . ILE A 193 ? 0.2013 0.2226 0.1757 -0.0146 -0.0092 -0.0021 195 ILE A CG1 
1546 C CG2 . ILE A 193 ? 0.2356 0.2622 0.2119 -0.0166 -0.0017 -0.0070 195 ILE A CG2 
1547 C CD1 . ILE A 193 ? 0.2044 0.2257 0.1820 -0.0100 -0.0083 -0.0040 195 ILE A CD1 
1548 N N   . GLY A 194 ? 0.1637 0.1812 0.1403 -0.0161 -0.0162 0.0030  196 GLY A N   
1549 C CA  . GLY A 194 ? 0.1617 0.1740 0.1377 -0.0146 -0.0207 0.0057  196 GLY A CA  
1550 C C   . GLY A 194 ? 0.1665 0.1762 0.1460 -0.0086 -0.0213 0.0047  196 GLY A C   
1551 O O   . GLY A 194 ? 0.1681 0.1796 0.1504 -0.0063 -0.0191 0.0022  196 GLY A O   
1552 N N   . TYR A 195 ? 0.1668 0.1721 0.1459 -0.0062 -0.0243 0.0066  197 TYR A N   
1553 C CA  . TYR A 195 ? 0.1683 0.1698 0.1493 -0.0006 -0.0247 0.0057  197 TYR A CA  
1554 C C   . TYR A 195 ? 0.2105 0.2049 0.1891 -0.0003 -0.0278 0.0069  197 TYR A C   
1555 O O   . TYR A 195 ? 0.2256 0.2169 0.2022 -0.0024 -0.0309 0.0097  197 TYR A O   
1556 C CB  . TYR A 195 ? 0.1537 0.1559 0.1369 0.0027  -0.0250 0.0068  197 TYR A CB  
1557 C CG  . TYR A 195 ? 0.1599 0.1594 0.1450 0.0084  -0.0241 0.0054  197 TYR A CG  
1558 C CD1 . TYR A 195 ? 0.1692 0.1623 0.1537 0.0115  -0.0261 0.0063  197 TYR A CD1 
1559 C CD2 . TYR A 195 ? 0.1245 0.1274 0.1114 0.0106  -0.0212 0.0031  197 TYR A CD2 
1560 C CE1 . TYR A 195 ? 0.1710 0.1615 0.1564 0.0167  -0.0245 0.0047  197 TYR A CE1 
1561 C CE2 . TYR A 195 ? 0.1129 0.1135 0.1007 0.0152  -0.0201 0.0018  197 TYR A CE2 
1562 C CZ  . TYR A 195 ? 0.1460 0.1406 0.1329 0.0182  -0.0214 0.0025  197 TYR A CZ  
1563 O OH  . TYR A 195 ? 0.1695 0.1613 0.1562 0.0227  -0.0196 0.0009  197 TYR A OH  
1564 N N   . GLN A 196 ? 0.2080 0.1993 0.1863 0.0020  -0.0275 0.0051  198 GLN A N   
1565 C CA  A GLN A 196 ? 0.2309 0.2137 0.2055 0.0022  -0.0305 0.0058  198 GLN A CA  
1566 C CA  B GLN A 196 ? 0.2342 0.2170 0.2088 0.0022  -0.0305 0.0058  198 GLN A CA  
1567 C C   . GLN A 196 ? 0.2131 0.1906 0.1868 0.0075  -0.0296 0.0037  198 GLN A C   
1568 O O   . GLN A 196 ? 0.1790 0.1598 0.1544 0.0090  -0.0271 0.0016  198 GLN A O   
1569 C CB  A GLN A 196 ? 0.2754 0.2588 0.2485 -0.0024 -0.0314 0.0060  198 GLN A CB  
1570 C CB  B GLN A 196 ? 0.2878 0.2715 0.2611 -0.0020 -0.0311 0.0057  198 GLN A CB  
1571 C CG  A GLN A 196 ? 0.3217 0.3088 0.2973 -0.0016 -0.0291 0.0037  198 GLN A CG  
1572 C CG  B GLN A 196 ? 0.3657 0.3407 0.3340 -0.0041 -0.0351 0.0073  198 GLN A CG  
1573 C CD  A GLN A 196 ? 0.3122 0.3089 0.2923 -0.0040 -0.0262 0.0030  198 GLN A CD  
1574 C CD  B GLN A 196 ? 0.4398 0.4181 0.4081 -0.0094 -0.0359 0.0081  198 GLN A CD  
1575 O OE1 A GLN A 196 ? 0.2979 0.2974 0.2802 -0.0059 -0.0261 0.0028  198 GLN A OE1 
1576 O OE1 B GLN A 196 ? 0.4787 0.4652 0.4517 -0.0102 -0.0332 0.0069  198 GLN A OE1 
1577 N NE2 A GLN A 196 ? 0.2437 0.2455 0.2255 -0.0042 -0.0238 0.0027  198 GLN A NE2 
1578 N NE2 B GLN A 196 ? 0.4409 0.4129 0.4046 -0.0131 -0.0399 0.0104  198 GLN A NE2 
1579 N N   . SER A 197 ? 0.2054 0.1740 0.1761 0.0103  -0.0317 0.0043  199 SER A N   
1580 C CA  . SER A 197 ? 0.2158 0.1779 0.1838 0.0148  -0.0304 0.0020  199 SER A CA  
1581 C C   . SER A 197 ? 0.2183 0.1766 0.1819 0.0121  -0.0313 0.0006  199 SER A C   
1582 O O   . SER A 197 ? 0.2367 0.1947 0.1986 0.0073  -0.0339 0.0022  199 SER A O   
1583 C CB  . SER A 197 ? 0.2502 0.2026 0.2156 0.0183  -0.0321 0.0026  199 SER A CB  
1584 O OG  . SER A 197 ? 0.2518 0.1966 0.2119 0.0145  -0.0362 0.0041  199 SER A OG  
1585 N N   . HIS A 198 ? 0.1991 0.1545 0.1604 0.0148  -0.0294 -0.0018 200 HIS A N   
1586 C CA  . HIS A 198 ? 0.2079 0.1588 0.1644 0.0120  -0.0309 -0.0027 200 HIS A CA  
1587 C C   . HIS A 198 ? 0.2360 0.1751 0.1850 0.0101  -0.0348 -0.0018 200 HIS A C   
1588 O O   . HIS A 198 ? 0.2447 0.1823 0.1912 0.0053  -0.0377 -0.0005 200 HIS A O   
1589 C CB  . HIS A 198 ? 0.1996 0.1481 0.1535 0.0150  -0.0284 -0.0053 200 HIS A CB  
1590 C CG  . HIS A 198 ? 0.1955 0.1547 0.1559 0.0160  -0.0254 -0.0060 200 HIS A CG  
1591 N ND1 . HIS A 198 ? 0.1927 0.1606 0.1586 0.0129  -0.0258 -0.0048 200 HIS A ND1 
1592 C CD2 . HIS A 198 ? 0.1941 0.1556 0.1557 0.0196  -0.0221 -0.0075 200 HIS A CD2 
1593 C CE1 . HIS A 198 ? 0.2002 0.1746 0.1701 0.0147  -0.0230 -0.0058 200 HIS A CE1 
1594 N NE2 . HIS A 198 ? 0.1895 0.1605 0.1568 0.0184  -0.0210 -0.0073 200 HIS A NE2 
1595 N N   . ALA A 199 ? 0.2614 0.1923 0.2074 0.0138  -0.0349 -0.0021 201 ALA A N   
1596 C CA  . ALA A 199 ? 0.3151 0.2328 0.2530 0.0122  -0.0388 -0.0013 201 ALA A CA  
1597 C C   . ALA A 199 ? 0.3408 0.2616 0.2799 0.0060  -0.0429 0.0022  201 ALA A C   
1598 O O   . ALA A 199 ? 0.3624 0.2762 0.2953 0.0014  -0.0468 0.0034  201 ALA A O   
1599 C CB  . ALA A 199 ? 0.3347 0.2450 0.2718 0.0180  -0.0380 -0.0019 201 ALA A CB  
1600 N N   . ASP A 200 ? 0.3193 0.2505 0.2657 0.0052  -0.0421 0.0041  202 ASP A N   
1601 C CA  . ASP A 200 ? 0.3295 0.2646 0.2767 -0.0010 -0.0451 0.0073  202 ASP A CA  
1602 C C   . ASP A 200 ? 0.3382 0.2812 0.2876 -0.0060 -0.0449 0.0076  202 ASP A C   
1603 O O   . ASP A 200 ? 0.3714 0.3130 0.3183 -0.0117 -0.0483 0.0100  202 ASP A O   
1604 C CB  . ASP A 200 ? 0.3577 0.3003 0.3105 -0.0007 -0.0443 0.0090  202 ASP A CB  
1605 C CG  . ASP A 200 ? 0.4299 0.3639 0.3810 0.0027  -0.0465 0.0104  202 ASP A CG  
1606 O OD1 . ASP A 200 ? 0.4756 0.3968 0.4201 0.0035  -0.0494 0.0103  202 ASP A OD1 
1607 O OD2 . ASP A 200 ? 0.3873 0.3267 0.3434 0.0045  -0.0456 0.0116  202 ASP A OD2 
1608 N N   . THR A 201 ? 0.2867 0.2378 0.2411 -0.0041 -0.0413 0.0056  203 THR A N   
1609 C CA  . THR A 201 ? 0.2930 0.2514 0.2508 -0.0078 -0.0411 0.0060  203 THR A CA  
1610 C C   . THR A 201 ? 0.3165 0.2662 0.2680 -0.0108 -0.0450 0.0067  203 THR A C   
1611 O O   . THR A 201 ? 0.3422 0.2972 0.2964 -0.0155 -0.0466 0.0086  203 THR A O   
1612 C CB  . THR A 201 ? 0.3284 0.2939 0.2915 -0.0043 -0.0372 0.0036  203 THR A CB  
1613 O OG1 . THR A 201 ? 0.3448 0.3173 0.3125 -0.0024 -0.0342 0.0032  203 THR A OG1 
1614 C CG2 . THR A 201 ? 0.3365 0.3094 0.3044 -0.0071 -0.0371 0.0041  203 THR A CG2 
1615 N N   . ALA A 202 ? 0.3266 0.2634 0.2699 -0.0082 -0.0464 0.0053  204 ALA A N   
1616 C CA  . ALA A 202 ? 0.3354 0.2621 0.2707 -0.0115 -0.0502 0.0057  204 ALA A CA  
1617 C C   . ALA A 202 ? 0.3313 0.2542 0.2630 -0.0180 -0.0553 0.0093  204 ALA A C   
1618 O O   . ALA A 202 ? 0.3132 0.2320 0.2406 -0.0227 -0.0591 0.0108  204 ALA A O   
1619 C CB  . ALA A 202 ? 0.3674 0.2797 0.2933 -0.0071 -0.0498 0.0028  204 ALA A CB  
1620 N N   . THR A 203 ? 0.3287 0.2528 0.2616 -0.0187 -0.0559 0.0109  205 THR A N   
1621 C CA  . THR A 203 ? 0.3604 0.2793 0.2885 -0.0251 -0.0610 0.0144  205 THR A CA  
1622 C C   . THR A 203 ? 0.3661 0.2960 0.3004 -0.0287 -0.0605 0.0172  205 THR A C   
1623 O O   . THR A 203 ? 0.3632 0.2902 0.2939 -0.0347 -0.0647 0.0205  205 THR A O   
1624 C CB  . THR A 203 ? 0.3957 0.2964 0.3129 -0.0234 -0.0644 0.0141  205 THR A CB  
1625 O OG1 . THR A 203 ? 0.4211 0.3219 0.3410 -0.0190 -0.0626 0.0137  205 THR A OG1 
1626 C CG2 . THR A 203 ? 0.3978 0.2858 0.3070 -0.0194 -0.0639 0.0107  205 THR A CG2 
1627 N N   . LYS A 204 ? 0.3540 0.2959 0.2966 -0.0258 -0.0557 0.0160  206 LYS A N   
1628 C CA  . LYS A 204 ? 0.3691 0.3199 0.3157 -0.0294 -0.0549 0.0182  206 LYS A CA  
1629 C C   . LYS A 204 ? 0.3626 0.3287 0.3183 -0.0297 -0.0500 0.0173  206 LYS A C   
1630 O O   . LYS A 204 ? 0.3828 0.3517 0.3422 -0.0247 -0.0468 0.0144  206 LYS A O   
1631 C CB  . LYS A 204 ? 0.4140 0.3611 0.3595 -0.0258 -0.0544 0.0180  206 LYS A CB  
1632 C CG  . LYS A 204 ? 0.5006 0.4319 0.4384 -0.0231 -0.0583 0.0181  206 LYS A CG  
1633 C CD  . LYS A 204 ? 0.5840 0.5125 0.5225 -0.0196 -0.0585 0.0187  206 LYS A CD  
1634 C CE  . LYS A 204 ? 0.6366 0.5486 0.5679 -0.0168 -0.0625 0.0190  206 LYS A CE  
1635 N NZ  . LYS A 204 ? 0.6730 0.5829 0.6074 -0.0107 -0.0617 0.0189  206 LYS A NZ  
1636 N N   . THR A 209 ? 0.5246 0.5392 0.4887 -0.0381 -0.0246 0.0133  211 THR A N   
1637 C CA  . THR A 209 ? 0.5349 0.5482 0.4926 -0.0432 -0.0260 0.0155  211 THR A CA  
1638 C C   . THR A 209 ? 0.5328 0.5376 0.4874 -0.0433 -0.0329 0.0196  211 THR A C   
1639 O O   . THR A 209 ? 0.5167 0.5195 0.4685 -0.0444 -0.0348 0.0214  211 THR A O   
1640 C CB  . THR A 209 ? 0.5676 0.5861 0.5215 -0.0509 -0.0232 0.0160  211 THR A CB  
1641 O OG1 . THR A 209 ? 0.5892 0.6068 0.5430 -0.0541 -0.0261 0.0185  211 THR A OG1 
1642 C CG2 . THR A 209 ? 0.5751 0.6018 0.5325 -0.0502 -0.0156 0.0117  211 THR A CG2 
1643 N N   . LYS A 210 ? 0.5324 0.5319 0.4874 -0.0422 -0.0367 0.0211  212 LYS A N   
1644 C CA  . LYS A 210 ? 0.5428 0.5330 0.4957 -0.0407 -0.0430 0.0244  212 LYS A CA  
1645 C C   . LYS A 210 ? 0.5390 0.5250 0.4964 -0.0319 -0.0434 0.0227  212 LYS A C   
1646 O O   . LYS A 210 ? 0.5661 0.5439 0.5227 -0.0293 -0.0479 0.0248  212 LYS A O   
1647 C CB  . LYS A 210 ? 0.5827 0.5673 0.5320 -0.0446 -0.0472 0.0270  212 LYS A CB  
1648 C CG  . LYS A 210 ? 0.6641 0.6465 0.6157 -0.0413 -0.0470 0.0252  212 LYS A CG  
1649 C CD  . LYS A 210 ? 0.7561 0.7348 0.7030 -0.0478 -0.0510 0.0282  212 LYS A CD  
1650 C CE  . LYS A 210 ? 0.8381 0.8089 0.7843 -0.0451 -0.0540 0.0279  212 LYS A CE  
1651 N NZ  . LYS A 210 ? 0.8825 0.8480 0.8228 -0.0521 -0.0590 0.0317  212 LYS A NZ  
1652 N N   . ASN A 211 ? 0.4841 0.4753 0.4460 -0.0276 -0.0387 0.0190  213 ASN A N   
1653 C CA  . ASN A 211 ? 0.4363 0.4251 0.4023 -0.0199 -0.0380 0.0170  213 ASN A CA  
1654 C C   . ASN A 211 ? 0.4147 0.4003 0.3818 -0.0166 -0.0405 0.0191  213 ASN A C   
1655 O O   . ASN A 211 ? 0.4074 0.3941 0.3729 -0.0203 -0.0426 0.0220  213 ASN A O   
1656 C CB  . ASN A 211 ? 0.4025 0.3986 0.3722 -0.0176 -0.0326 0.0133  213 ASN A CB  
1657 C CG  . ASN A 211 ? 0.4342 0.4332 0.4058 -0.0179 -0.0302 0.0110  213 ASN A CG  
1658 O OD1 . ASN A 211 ? 0.4484 0.4527 0.4234 -0.0160 -0.0264 0.0083  213 ASN A OD1 
1659 N ND2 . ASN A 211 ? 0.4470 0.4427 0.4166 -0.0205 -0.0327 0.0123  213 ASN A ND2 
1660 N N   . ARG A 212 ? 0.3826 0.3646 0.3528 -0.0098 -0.0403 0.0177  214 ARG A N   
1661 C CA  . ARG A 212 ? 0.3810 0.3606 0.3546 -0.0049 -0.0421 0.0195  214 ARG A CA  
1662 C C   . ARG A 212 ? 0.3457 0.3325 0.3219 -0.0063 -0.0411 0.0208  214 ARG A C   
1663 O O   . ARG A 212 ? 0.3535 0.3396 0.3305 -0.0076 -0.0447 0.0247  214 ARG A O   
1664 C CB  . ARG A 212 ? 0.4257 0.4029 0.4020 0.0023  -0.0394 0.0163  214 ARG A CB  
1665 C CG  . ARG A 212 ? 0.4991 0.4742 0.4800 0.0087  -0.0399 0.0172  214 ARG A CG  
1666 C CD  . ARG A 212 ? 0.5702 0.5434 0.5518 0.0144  -0.0363 0.0134  214 ARG A CD  
1667 N NE  . ARG A 212 ? 0.6309 0.5935 0.6077 0.0161  -0.0376 0.0121  214 ARG A NE  
1668 C CZ  . ARG A 212 ? 0.6516 0.6060 0.6282 0.0215  -0.0382 0.0119  214 ARG A CZ  
1669 N NH1 . ARG A 212 ? 0.6280 0.5714 0.5982 0.0220  -0.0396 0.0104  214 ARG A NH1 
1670 N NH2 . ARG A 212 ? 0.6633 0.6202 0.6463 0.0266  -0.0373 0.0131  214 ARG A NH2 
1671 N N   . PHE A 213 ? 0.2749 0.2682 0.2522 -0.0063 -0.0368 0.0178  215 PHE A N   
1672 C CA  . PHE A 213 ? 0.2506 0.2500 0.2285 -0.0089 -0.0357 0.0187  215 PHE A CA  
1673 C C   . PHE A 213 ? 0.2111 0.2145 0.1851 -0.0139 -0.0323 0.0162  215 PHE A C   
1674 O O   . PHE A 213 ? 0.2109 0.2151 0.1853 -0.0130 -0.0295 0.0131  215 PHE A O   
1675 C CB  . PHE A 213 ? 0.2570 0.2601 0.2401 -0.0036 -0.0334 0.0174  215 PHE A CB  
1676 C CG  . PHE A 213 ? 0.2929 0.2932 0.2809 0.0026  -0.0350 0.0188  215 PHE A CG  
1677 C CD1 . PHE A 213 ? 0.3298 0.3299 0.3209 0.0028  -0.0388 0.0233  215 PHE A CD1 
1678 C CD2 . PHE A 213 ? 0.3135 0.3115 0.3033 0.0082  -0.0325 0.0158  215 PHE A CD2 
1679 C CE1 . PHE A 213 ? 0.3440 0.3418 0.3409 0.0093  -0.0397 0.0245  215 PHE A CE1 
1680 C CE2 . PHE A 213 ? 0.3300 0.3254 0.3241 0.0143  -0.0330 0.0166  215 PHE A CE2 
1681 C CZ  . PHE A 213 ? 0.3321 0.3278 0.3303 0.0152  -0.0363 0.0209  215 PHE A CZ  
1682 N N   . VAL A 214 ? 0.2096 0.2153 0.1800 -0.0194 -0.0327 0.0178  216 VAL A N   
1683 C CA  A VAL A 214 ? 0.1984 0.2077 0.1647 -0.0241 -0.0288 0.0152  216 VAL A CA  
1684 C CA  B VAL A 214 ? 0.1979 0.2073 0.1644 -0.0238 -0.0286 0.0150  216 VAL A CA  
1685 C C   . VAL A 214 ? 0.2069 0.2187 0.1713 -0.0260 -0.0278 0.0153  216 VAL A C   
1686 O O   . VAL A 214 ? 0.2411 0.2520 0.2049 -0.0277 -0.0318 0.0192  216 VAL A O   
1687 C CB  A VAL A 214 ? 0.2052 0.2131 0.1657 -0.0310 -0.0301 0.0170  216 VAL A CB  
1688 C CB  B VAL A 214 ? 0.2032 0.2114 0.1644 -0.0302 -0.0295 0.0164  216 VAL A CB  
1689 C CG1 A VAL A 214 ? 0.2227 0.2342 0.1777 -0.0367 -0.0260 0.0150  216 VAL A CG1 
1690 C CG1 B VAL A 214 ? 0.1914 0.1977 0.1474 -0.0361 -0.0336 0.0207  216 VAL A CG1 
1691 C CG2 A VAL A 214 ? 0.1857 0.1922 0.1476 -0.0300 -0.0300 0.0161  216 VAL A CG2 
1692 C CG2 B VAL A 214 ? 0.2087 0.2213 0.1680 -0.0330 -0.0240 0.0127  216 VAL A CG2 
1693 N N   . VAL A 215 ? 0.1940 0.2086 0.1574 -0.0260 -0.0231 0.0115  217 VAL A N   
1694 C CA  . VAL A 215 ? 0.1850 0.2007 0.1444 -0.0291 -0.0219 0.0111  217 VAL A CA  
1695 C C   . VAL A 215 ? 0.1928 0.2095 0.1471 -0.0325 -0.0166 0.0071  217 VAL A C   
1696 O O   . VAL A 215 ? 0.2139 0.2297 0.1620 -0.0365 -0.0156 0.0066  217 VAL A O   
1697 C CB  . VAL A 215 ? 0.2014 0.2185 0.1652 -0.0242 -0.0215 0.0104  217 VAL A CB  
1698 C CG1 . VAL A 215 ? 0.2164 0.2336 0.1861 -0.0205 -0.0259 0.0142  217 VAL A CG1 
1699 C CG2 . VAL A 215 ? 0.1819 0.2003 0.1494 -0.0194 -0.0173 0.0058  217 VAL A CG2 
1700 O OXT . VAL A 215 ? 0.1789 0.1970 0.1355 -0.0310 -0.0136 0.0045  217 VAL A OXT 
1701 N N   . GLY B 8   ? 0.4108 0.5211 0.4048 -0.0193 -0.0011 -0.0325 10  GLY B N   
1702 C CA  . GLY B 8   ? 0.3918 0.5055 0.3900 -0.0218 0.0030  -0.0365 10  GLY B CA  
1703 C C   . GLY B 8   ? 0.3654 0.4758 0.3685 -0.0162 0.0036  -0.0350 10  GLY B C   
1704 O O   . GLY B 8   ? 0.3827 0.4944 0.3904 -0.0099 -0.0003 -0.0323 10  GLY B O   
1705 N N   . ALA B 9   ? 0.3262 0.4320 0.3277 -0.0188 0.0084  -0.0369 11  ALA B N   
1706 C CA  . ALA B 9   ? 0.3132 0.4143 0.3174 -0.0147 0.0095  -0.0356 11  ALA B CA  
1707 C C   . ALA B 9   ? 0.2896 0.3771 0.2866 -0.0120 0.0095  -0.0306 11  ALA B C   
1708 O O   . ALA B 9   ? 0.3061 0.3870 0.2959 -0.0142 0.0100  -0.0289 11  ALA B O   
1709 C CB  . ALA B 9   ? 0.3262 0.4262 0.3294 -0.0192 0.0146  -0.0391 11  ALA B CB  
1710 N N   . ARG B 10  ? 0.2420 0.3254 0.2412 -0.0074 0.0091  -0.0285 12  ARG B N   
1711 C CA  . ARG B 10  ? 0.2025 0.2745 0.1963 -0.0051 0.0093  -0.0243 12  ARG B CA  
1712 C C   . ARG B 10  ? 0.2000 0.2629 0.1860 -0.0095 0.0130  -0.0239 12  ARG B C   
1713 O O   . ARG B 10  ? 0.2025 0.2651 0.1871 -0.0131 0.0160  -0.0262 12  ARG B O   
1714 C CB  . ARG B 10  ? 0.1977 0.2673 0.1946 -0.0014 0.0093  -0.0232 12  ARG B CB  
1715 C CG  . ARG B 10  ? 0.1843 0.2441 0.1772 0.0014  0.0089  -0.0191 12  ARG B CG  
1716 C CD  . ARG B 10  ? 0.1809 0.2394 0.1769 0.0043  0.0091  -0.0187 12  ARG B CD  
1717 N NE  . ARG B 10  ? 0.1974 0.2632 0.2005 0.0080  0.0071  -0.0199 12  ARG B NE  
1718 C CZ  . ARG B 10  ? 0.1952 0.2603 0.1999 0.0126  0.0042  -0.0176 12  ARG B CZ  
1719 N NH1 . ARG B 10  ? 0.1832 0.2409 0.1827 0.0136  0.0034  -0.0143 12  ARG B NH1 
1720 N NH2 . ARG B 10  ? 0.2017 0.2734 0.2133 0.0163  0.0024  -0.0187 12  ARG B NH2 
1721 N N   . ILE B 11  ? 0.1721 0.2272 0.1531 -0.0090 0.0130  -0.0210 13  ILE B N   
1722 C CA  . ILE B 11  ? 0.1588 0.2045 0.1333 -0.0120 0.0164  -0.0201 13  ILE B CA  
1723 C C   . ILE B 11  ? 0.1655 0.2046 0.1398 -0.0093 0.0167  -0.0175 13  ILE B C   
1724 O O   . ILE B 11  ? 0.1717 0.2081 0.1475 -0.0053 0.0149  -0.0147 13  ILE B O   
1725 C CB  . ILE B 11  ? 0.1653 0.2058 0.1354 -0.0127 0.0167  -0.0186 13  ILE B CB  
1726 C CG1 . ILE B 11  ? 0.2059 0.2533 0.1750 -0.0165 0.0162  -0.0214 13  ILE B CG1 
1727 C CG2 . ILE B 11  ? 0.1685 0.1986 0.1329 -0.0150 0.0207  -0.0176 13  ILE B CG2 
1728 C CD1 . ILE B 11  ? 0.2225 0.2653 0.1866 -0.0178 0.0165  -0.0203 13  ILE B CD1 
1729 N N   . ILE B 12  ? 0.1650 0.2017 0.1371 -0.0118 0.0188  -0.0184 14  ILE B N   
1730 C CA  . ILE B 12  ? 0.1550 0.1860 0.1263 -0.0099 0.0186  -0.0159 14  ILE B CA  
1731 C C   . ILE B 12  ? 0.1697 0.1910 0.1344 -0.0124 0.0210  -0.0142 14  ILE B C   
1732 O O   . ILE B 12  ? 0.1839 0.2038 0.1443 -0.0169 0.0238  -0.0164 14  ILE B O   
1733 C CB  . ILE B 12  ? 0.1789 0.2145 0.1525 -0.0108 0.0188  -0.0181 14  ILE B CB  
1734 C CG1 . ILE B 12  ? 0.2042 0.2491 0.1854 -0.0075 0.0166  -0.0197 14  ILE B CG1 
1735 C CG2 . ILE B 12  ? 0.2127 0.2417 0.1832 -0.0105 0.0189  -0.0157 14  ILE B CG2 
1736 C CD1 . ILE B 12  ? 0.2523 0.3033 0.2371 -0.0089 0.0178  -0.0232 14  ILE B CD1 
1737 N N   . TYR B 13  ? 0.1603 0.1750 0.1244 -0.0095 0.0202  -0.0105 15  TYR B N   
1738 C CA  . TYR B 13  ? 0.1554 0.1608 0.1143 -0.0107 0.0218  -0.0082 15  TYR B CA  
1739 C C   . TYR B 13  ? 0.1663 0.1687 0.1251 -0.0089 0.0198  -0.0054 15  TYR B C   
1740 O O   . TYR B 13  ? 0.1575 0.1625 0.1208 -0.0054 0.0173  -0.0039 15  TYR B O   
1741 C CB  . TYR B 13  ? 0.1513 0.1518 0.1107 -0.0086 0.0226  -0.0063 15  TYR B CB  
1742 C CG  . TYR B 13  ? 0.1485 0.1505 0.1068 -0.0108 0.0246  -0.0087 15  TYR B CG  
1743 C CD1 . TYR B 13  ? 0.1669 0.1658 0.1198 -0.0156 0.0280  -0.0109 15  TYR B CD1 
1744 C CD2 . TYR B 13  ? 0.1386 0.1441 0.1003 -0.0088 0.0235  -0.0088 15  TYR B CD2 
1745 C CE1 . TYR B 13  ? 0.1752 0.1750 0.1263 -0.0183 0.0301  -0.0132 15  TYR B CE1 
1746 C CE2 . TYR B 13  ? 0.1485 0.1550 0.1080 -0.0115 0.0251  -0.0109 15  TYR B CE2 
1747 C CZ  . TYR B 13  ? 0.1765 0.1804 0.1309 -0.0163 0.0284  -0.0132 15  TYR B CZ  
1748 O OH  . TYR B 13  ? 0.1897 0.1944 0.1411 -0.0198 0.0303  -0.0154 15  TYR B OH  
1749 N N   . ASP B 14  ? 0.1764 0.1734 0.1293 -0.0117 0.0207  -0.0047 16  ASP B N   
1750 C CA  . ASP B 14  ? 0.1838 0.1775 0.1353 -0.0106 0.0182  -0.0016 16  ASP B CA  
1751 C C   . ASP B 14  ? 0.1804 0.1676 0.1326 -0.0071 0.0169  0.0028  16  ASP B C   
1752 O O   . ASP B 14  ? 0.2064 0.1904 0.1595 -0.0060 0.0187  0.0032  16  ASP B O   
1753 C CB  . ASP B 14  ? 0.1958 0.1863 0.1399 -0.0153 0.0193  -0.0026 16  ASP B CB  
1754 C CG  . ASP B 14  ? 0.2798 0.2611 0.2156 -0.0186 0.0217  -0.0017 16  ASP B CG  
1755 O OD1 . ASP B 14  ? 0.2550 0.2305 0.1905 -0.0167 0.0224  0.0004  16  ASP B OD1 
1756 O OD2 . ASP B 14  ? 0.3352 0.3141 0.2641 -0.0235 0.0234  -0.0035 16  ASP B OD2 
1757 N N   . ARG B 15  ? 0.1812 0.1670 0.1336 -0.0055 0.0137  0.0060  17  ARG B N   
1758 C CA  . ARG B 15  ? 0.1853 0.1668 0.1403 -0.0017 0.0118  0.0102  17  ARG B CA  
1759 C C   . ARG B 15  ? 0.2010 0.1732 0.1516 -0.0020 0.0137  0.0122  17  ARG B C   
1760 O O   . ARG B 15  ? 0.1937 0.1632 0.1484 0.0011  0.0148  0.0134  17  ARG B O   
1761 C CB  . ARG B 15  ? 0.1916 0.1736 0.1462 -0.0011 0.0076  0.0132  17  ARG B CB  
1762 C CG  . ARG B 15  ? 0.2192 0.1994 0.1790 0.0033  0.0050  0.0173  17  ARG B CG  
1763 C CD  . ARG B 15  ? 0.2715 0.2520 0.2292 0.0028  0.0005  0.0204  17  ARG B CD  
1764 N NE  . ARG B 15  ? 0.3161 0.2982 0.2813 0.0072  -0.0027 0.0238  17  ARG B NE  
1765 C CZ  . ARG B 15  ? 0.4253 0.4023 0.3917 0.0102  -0.0046 0.0280  17  ARG B CZ  
1766 N NH1 . ARG B 15  ? 0.3812 0.3490 0.3402 0.0091  -0.0034 0.0296  17  ARG B NH1 
1767 N NH2 . ARG B 15  ? 0.4477 0.4285 0.4229 0.0143  -0.0075 0.0304  17  ARG B NH2 
1768 N N   . ALA B 16  ? 0.2045 0.1710 0.1462 -0.0060 0.0147  0.0122  18  ALA B N   
1769 C CA  . ALA B 16  ? 0.2321 0.1877 0.1680 -0.0064 0.0167  0.0143  18  ALA B CA  
1770 C C   . ALA B 16  ? 0.2225 0.1765 0.1595 -0.0069 0.0214  0.0116  18  ALA B C   
1771 O O   . ALA B 16  ? 0.2413 0.1881 0.1789 -0.0045 0.0230  0.0138  18  ALA B O   
1772 C CB  . ALA B 16  ? 0.2580 0.2072 0.1826 -0.0116 0.0175  0.0143  18  ALA B CB  
1773 N N   . PHE B 17  ? 0.1931 0.1541 0.1308 -0.0100 0.0236  0.0068  19  PHE B N   
1774 C CA  . PHE B 17  ? 0.2120 0.1726 0.1500 -0.0114 0.0277  0.0039  19  PHE B CA  
1775 C C   . PHE B 17  ? 0.2080 0.1697 0.1536 -0.0067 0.0275  0.0051  19  PHE B C   
1776 O O   . PHE B 17  ? 0.2129 0.1680 0.1579 -0.0063 0.0308  0.0054  19  PHE B O   
1777 C CB  . PHE B 17  ? 0.2141 0.1842 0.1526 -0.0152 0.0288  -0.0012 19  PHE B CB  
1778 C CG  . PHE B 17  ? 0.2452 0.2151 0.1819 -0.0183 0.0328  -0.0046 19  PHE B CG  
1779 C CD1 . PHE B 17  ? 0.2665 0.2394 0.2081 -0.0162 0.0332  -0.0052 19  PHE B CD1 
1780 C CD2 . PHE B 17  ? 0.2706 0.2367 0.1998 -0.0240 0.0365  -0.0073 19  PHE B CD2 
1781 C CE1 . PHE B 17  ? 0.2894 0.2617 0.2282 -0.0199 0.0368  -0.0083 19  PHE B CE1 
1782 C CE2 . PHE B 17  ? 0.2867 0.2529 0.2138 -0.0275 0.0402  -0.0105 19  PHE B CE2 
1783 C CZ  . PHE B 17  ? 0.2851 0.2545 0.2169 -0.0255 0.0402  -0.0110 19  PHE B CZ  
1784 N N   . LEU B 18  ? 0.1765 0.1461 0.1291 -0.0036 0.0241  0.0056  20  LEU B N   
1785 C CA  . LEU B 18  ? 0.1659 0.1364 0.1255 0.0003  0.0242  0.0065  20  LEU B CA  
1786 C C   . LEU B 18  ? 0.1955 0.1582 0.1573 0.0039  0.0244  0.0103  20  LEU B C   
1787 O O   . LEU B 18  ? 0.1949 0.1542 0.1596 0.0054  0.0275  0.0100  20  LEU B O   
1788 C CB  . LEU B 18  ? 0.1706 0.1498 0.1363 0.0027  0.0207  0.0065  20  LEU B CB  
1789 C CG  . LEU B 18  ? 0.1667 0.1532 0.1318 0.0003  0.0207  0.0029  20  LEU B CG  
1790 C CD1 . LEU B 18  ? 0.1573 0.1506 0.1271 0.0025  0.0175  0.0031  20  LEU B CD1 
1791 C CD2 . LEU B 18  ? 0.1508 0.1375 0.1159 -0.0008 0.0237  0.0005  20  LEU B CD2 
1792 N N   . MET B 19  ? 0.2099 0.1700 0.1703 0.0051  0.0213  0.0137  21  MET B N   
1793 C CA  . MET B 19  ? 0.2195 0.1729 0.1828 0.0093  0.0204  0.0180  21  MET B CA  
1794 C C   . MET B 19  ? 0.2697 0.2121 0.2283 0.0085  0.0251  0.0181  21  MET B C   
1795 O O   . MET B 19  ? 0.2773 0.2149 0.2411 0.0123  0.0269  0.0197  21  MET B O   
1796 C CB  . MET B 19  ? 0.2202 0.1730 0.1809 0.0100  0.0152  0.0218  21  MET B CB  
1797 C CG  . MET B 19  ? 0.2465 0.2092 0.2131 0.0113  0.0108  0.0221  21  MET B CG  
1798 S SD  . MET B 19  ? 0.2871 0.2562 0.2668 0.0164  0.0101  0.0224  21  MET B SD  
1799 C CE  . MET B 19  ? 0.3764 0.3531 0.3583 0.0166  0.0042  0.0241  21  MET B CE  
1800 N N   . ALA B 20  ? 0.2739 0.2122 0.2228 0.0034  0.0275  0.0161  22  ALA B N   
1801 C CA  . ALA B 20  ? 0.2975 0.2247 0.2396 0.0011  0.0328  0.0155  22  ALA B CA  
1802 C C   . ALA B 20  ? 0.3130 0.2404 0.2585 0.0006  0.0378  0.0121  22  ALA B C   
1803 O O   . ALA B 20  ? 0.3437 0.2612 0.2873 0.0010  0.0422  0.0124  22  ALA B O   
1804 C CB  . ALA B 20  ? 0.3030 0.2278 0.2341 -0.0053 0.0344  0.0131  22  ALA B CB  
1805 N N   . CYS B 21  ? 0.2890 0.2266 0.2389 -0.0003 0.0373  0.0089  23  CYS B N   
1806 C CA  . CYS B 21  ? 0.2913 0.2290 0.2433 -0.0013 0.0416  0.0058  23  CYS B CA  
1807 C C   . CYS B 21  ? 0.2792 0.2144 0.2397 0.0038  0.0427  0.0076  23  CYS B C   
1808 O O   . CYS B 21  ? 0.2988 0.2318 0.2600 0.0026  0.0473  0.0050  23  CYS B O   
1809 C CB  . CYS B 21  ? 0.2788 0.2273 0.2317 -0.0039 0.0403  0.0023  23  CYS B CB  
1810 S SG  . CYS B 21  ? 0.2906 0.2436 0.2356 -0.0103 0.0404  -0.0012 23  CYS B SG  
1811 N N   . ARG B 22  ? 0.2667 0.2029 0.2337 0.0090  0.0388  0.0115  24  ARG B N   
1812 C CA  . ARG B 22  ? 0.2684 0.2039 0.2451 0.0139  0.0398  0.0127  24  ARG B CA  
1813 C C   . ARG B 22  ? 0.3317 0.2550 0.3078 0.0154  0.0450  0.0136  24  ARG B C   
1814 O O   . ARG B 22  ? 0.3464 0.2669 0.3263 0.0157  0.0501  0.0114  24  ARG B O   
1815 C CB  . ARG B 22  ? 0.2461 0.1872 0.2305 0.0188  0.0338  0.0166  24  ARG B CB  
1816 C CG  . ARG B 22  ? 0.2283 0.1720 0.2244 0.0232  0.0349  0.0167  24  ARG B CG  
1817 C CD  . ARG B 22  ? 0.2491 0.1988 0.2531 0.0276  0.0290  0.0202  24  ARG B CD  
1818 N NE  . ARG B 22  ? 0.2664 0.2207 0.2823 0.0310  0.0302  0.0194  24  ARG B NE  
1819 C CZ  . ARG B 22  ? 0.3240 0.2838 0.3497 0.0354  0.0260  0.0221  24  ARG B CZ  
1820 N NH1 . ARG B 22  ? 0.3729 0.3340 0.3972 0.0370  0.0198  0.0263  24  ARG B NH1 
1821 N NH2 . ARG B 22  ? 0.3277 0.2922 0.3645 0.0378  0.0280  0.0205  24  ARG B NH2 
1822 N N   . GLY B 23  ? 0.3747 0.2902 0.3454 0.0159  0.0440  0.0167  25  GLY B N   
1823 C CA  . GLY B 23  ? 0.4369 0.3390 0.4058 0.0176  0.0487  0.0182  25  GLY B CA  
1824 C C   . GLY B 23  ? 0.4855 0.3788 0.4419 0.0113  0.0542  0.0153  25  GLY B C   
1825 O O   . GLY B 23  ? 0.5070 0.3883 0.4611 0.0117  0.0599  0.0153  25  GLY B O   
1826 N N   . GLY B 24  ? 0.5001 0.3991 0.4489 0.0055  0.0528  0.0127  26  GLY B N   
1827 C CA  . GLY B 24  ? 0.5270 0.4202 0.4643 -0.0015 0.0577  0.0092  26  GLY B CA  
1828 C C   . GLY B 24  ? 0.5330 0.4366 0.4689 -0.0069 0.0584  0.0040  26  GLY B C   
1829 O O   . GLY B 24  ? 0.5373 0.4435 0.4656 -0.0126 0.0585  0.0015  26  GLY B O   
1830 N N   . GLY B 25  ? 0.5349 0.4442 0.4780 -0.0053 0.0589  0.0025  27  GLY B N   
1831 C CA  . GLY B 25  ? 0.5362 0.4553 0.4785 -0.0095 0.0587  -0.0016 27  GLY B CA  
1832 C C   . GLY B 25  ? 0.5432 0.4568 0.4792 -0.0153 0.0655  -0.0058 27  GLY B C   
1833 O O   . GLY B 25  ? 0.5607 0.4620 0.4933 -0.0158 0.0711  -0.0058 27  GLY B O   
1834 N N   . GLY B 26  ? 0.5257 0.4477 0.4594 -0.0198 0.0649  -0.0094 28  GLY B N   
1835 C CA  . GLY B 26  ? 0.5279 0.4465 0.4558 -0.0257 0.0707  -0.0136 28  GLY B CA  
1836 C C   . GLY B 26  ? 0.5331 0.4466 0.4509 -0.0323 0.0744  -0.0162 28  GLY B C   
1837 O O   . GLY B 26  ? 0.5533 0.4615 0.4651 -0.0378 0.0802  -0.0197 28  GLY B O   
1838 N N   . GLU B 27  ? 0.5166 0.4314 0.4320 -0.0326 0.0716  -0.0150 29  GLU B N   
1839 C CA  . GLU B 27  ? 0.5292 0.4394 0.4346 -0.0396 0.0754  -0.0179 29  GLU B CA  
1840 C C   . GLU B 27  ? 0.5121 0.4360 0.4164 -0.0440 0.0714  -0.0208 29  GLU B C   
1841 O O   . GLU B 27  ? 0.5205 0.4430 0.4184 -0.0487 0.0729  -0.0226 29  GLU B O   
1842 C CB  . GLU B 27  ? 0.5838 0.4816 0.4855 -0.0373 0.0769  -0.0145 29  GLU B CB  
1843 C CG  . GLU B 27  ? 0.6864 0.5680 0.5858 -0.0358 0.0834  -0.0134 29  GLU B CG  
1844 C CD  . GLU B 27  ? 0.7868 0.6580 0.6870 -0.0297 0.0821  -0.0078 29  GLU B CD  
1845 O OE1 . GLU B 27  ? 0.8152 0.6791 0.7212 -0.0238 0.0837  -0.0050 29  GLU B OE1 
1846 O OE2 . GLU B 27  ? 0.8384 0.7089 0.7335 -0.0310 0.0795  -0.0064 29  GLU B OE2 
1847 N N   . ASN B 28  ? 0.4714 0.4083 0.3818 -0.0426 0.0666  -0.0214 30  ASN B N   
1848 C CA  . ASN B 28  ? 0.4694 0.4197 0.3799 -0.0464 0.0631  -0.0245 30  ASN B CA  
1849 C C   . ASN B 28  ? 0.4843 0.4350 0.3874 -0.0549 0.0675  -0.0295 30  ASN B C   
1850 O O   . ASN B 28  ? 0.4837 0.4261 0.3821 -0.0579 0.0727  -0.0308 30  ASN B O   
1851 C CB  . ASN B 28  ? 0.4679 0.4305 0.3858 -0.0430 0.0574  -0.0239 30  ASN B CB  
1852 C CG  . ASN B 28  ? 0.4846 0.4610 0.4056 -0.0440 0.0525  -0.0256 30  ASN B CG  
1853 O OD1 . ASN B 28  ? 0.5067 0.4842 0.4259 -0.0463 0.0529  -0.0267 30  ASN B OD1 
1854 N ND2 . ASN B 28  ? 0.4812 0.4679 0.4070 -0.0423 0.0481  -0.0258 30  ASN B ND2 
1855 N N   . LEU B 29  ? 0.4852 0.4458 0.3875 -0.0592 0.0657  -0.0325 31  LEU B N   
1856 C CA  . LEU B 29  ? 0.4874 0.4508 0.3833 -0.0681 0.0693  -0.0377 31  LEU B CA  
1857 C C   . LEU B 29  ? 0.4755 0.4490 0.3727 -0.0707 0.0670  -0.0400 31  LEU B C   
1858 O O   . LEU B 29  ? 0.4728 0.4491 0.3643 -0.0786 0.0698  -0.0445 31  LEU B O   
1859 C CB  . LEU B 29  ? 0.4982 0.4701 0.3942 -0.0716 0.0680  -0.0404 31  LEU B CB  
1860 C CG  . LEU B 29  ? 0.5457 0.5079 0.4382 -0.0706 0.0701  -0.0386 31  LEU B CG  
1861 C CD1 . LEU B 29  ? 0.5632 0.5352 0.4560 -0.0751 0.0692  -0.0423 31  LEU B CD1 
1862 C CD2 . LEU B 29  ? 0.5691 0.5137 0.4508 -0.0749 0.0777  -0.0391 31  LEU B CD2 
1863 N N   . TYR B 30  ? 0.4556 0.4342 0.3594 -0.0647 0.0620  -0.0371 32  TYR B N   
1864 C CA  . TYR B 30  ? 0.4563 0.4409 0.3593 -0.0671 0.0602  -0.0385 32  TYR B CA  
1865 C C   . TYR B 30  ? 0.4473 0.4267 0.3536 -0.0610 0.0591  -0.0348 32  TYR B C   
1866 O O   . TYR B 30  ? 0.4568 0.4279 0.3661 -0.0554 0.0603  -0.0315 32  TYR B O   
1867 C CB  . TYR B 30  ? 0.4515 0.4539 0.3591 -0.0684 0.0538  -0.0403 32  TYR B CB  
1868 C CG  . TYR B 30  ? 0.4579 0.4688 0.3750 -0.0605 0.0469  -0.0370 32  TYR B CG  
1869 C CD1 . TYR B 30  ? 0.4654 0.4762 0.3872 -0.0562 0.0459  -0.0354 32  TYR B CD1 
1870 C CD2 . TYR B 30  ? 0.4800 0.4984 0.4004 -0.0577 0.0414  -0.0356 32  TYR B CD2 
1871 C CE1 . TYR B 30  ? 0.4775 0.4957 0.4075 -0.0496 0.0402  -0.0328 32  TYR B CE1 
1872 C CE2 . TYR B 30  ? 0.4850 0.5100 0.4135 -0.0506 0.0357  -0.0326 32  TYR B CE2 
1873 C CZ  . TYR B 30  ? 0.4895 0.5146 0.4230 -0.0466 0.0353  -0.0315 32  TYR B CZ  
1874 O OH  . TYR B 30  ? 0.4988 0.5302 0.4399 -0.0402 0.0301  -0.0291 32  TYR B OH  
1875 N N   . PHE B 31  ? 0.4301 0.4139 0.3351 -0.0625 0.0570  -0.0353 33  PHE B N   
1876 C CA  . PHE B 31  ? 0.4281 0.4076 0.3354 -0.0578 0.0562  -0.0324 33  PHE B CA  
1877 C C   . PHE B 31  ? 0.4441 0.4081 0.3485 -0.0577 0.0637  -0.0321 33  PHE B C   
1878 O O   . PHE B 31  ? 0.4257 0.3845 0.3351 -0.0517 0.0639  -0.0292 33  PHE B O   
1879 C CB  . PHE B 31  ? 0.4065 0.3914 0.3230 -0.0493 0.0503  -0.0285 33  PHE B CB  
1880 C CG  . PHE B 31  ? 0.4114 0.3978 0.3306 -0.0453 0.0468  -0.0262 33  PHE B CG  
1881 C CD1 . PHE B 31  ? 0.4213 0.4003 0.3357 -0.0478 0.0505  -0.0268 33  PHE B CD1 
1882 C CD2 . PHE B 31  ? 0.4056 0.4000 0.3316 -0.0395 0.0405  -0.0236 33  PHE B CD2 
1883 C CE1 . PHE B 31  ? 0.4358 0.4151 0.3517 -0.0447 0.0478  -0.0248 33  PHE B CE1 
1884 C CE2 . PHE B 31  ? 0.4073 0.4015 0.3348 -0.0360 0.0379  -0.0214 33  PHE B CE2 
1885 C CZ  . PHE B 31  ? 0.4312 0.4180 0.3534 -0.0389 0.0415  -0.0220 33  PHE B CZ  
1886 N N   . GLN B 32  ? 0.4411 0.3975 0.3377 -0.0645 0.0703  -0.0354 34  GLN B N   
1887 C CA  . GLN B 32  ? 0.4387 0.3796 0.3326 -0.0645 0.0782  -0.0355 34  GLN B CA  
1888 C C   . GLN B 32  ? 0.4298 0.3650 0.3310 -0.0562 0.0778  -0.0313 34  GLN B C   
1889 O O   . GLN B 32  ? 0.4602 0.3856 0.3639 -0.0526 0.0816  -0.0298 34  GLN B O   
1890 C CB  . GLN B 32  ? 0.4578 0.3931 0.3487 -0.0666 0.0818  -0.0366 34  GLN B CB  
1891 C CG  . GLN B 32  ? 0.4629 0.4026 0.3446 -0.0760 0.0825  -0.0408 34  GLN B CG  
1892 C CD  . GLN B 32  ? 0.5263 0.4577 0.4024 -0.0798 0.0878  -0.0426 34  GLN B CD  
1893 O OE1 . GLN B 32  ? 0.5261 0.4481 0.4058 -0.0756 0.0920  -0.0413 34  GLN B OE1 
1894 N NE2 . GLN B 32  ? 0.5291 0.4643 0.3964 -0.0883 0.0878  -0.0459 34  GLN B NE2 
1895 N N   . GLY B 33  ? 0.4088 0.3504 0.3130 -0.0538 0.0732  -0.0299 35  GLY B N   
1896 C CA  . GLY B 33  ? 0.3870 0.3242 0.2965 -0.0471 0.0720  -0.0260 35  GLY B CA  
1897 C C   . GLY B 33  ? 0.3734 0.3184 0.2920 -0.0398 0.0652  -0.0223 35  GLY B C   
1898 O O   . GLY B 33  ? 0.3621 0.3054 0.2843 -0.0351 0.0631  -0.0193 35  GLY B O   
1899 N N   . LYS B 34  ? 0.3397 0.2924 0.2612 -0.0389 0.0618  -0.0225 36  LYS B N   
1900 C CA  . LYS B 34  ? 0.2964 0.2557 0.2261 -0.0321 0.0559  -0.0192 36  LYS B CA  
1901 C C   . LYS B 34  ? 0.2754 0.2461 0.2072 -0.0316 0.0500  -0.0191 36  LYS B C   
1902 O O   . LYS B 34  ? 0.3030 0.2804 0.2315 -0.0363 0.0490  -0.0219 36  LYS B O   
1903 C CB  . LYS B 34  ? 0.3036 0.2641 0.2351 -0.0310 0.0552  -0.0190 36  LYS B CB  
1904 C CG  . LYS B 34  ? 0.3866 0.3361 0.3191 -0.0297 0.0611  -0.0187 36  LYS B CG  
1905 C CD  . LYS B 34  ? 0.4560 0.4064 0.3900 -0.0290 0.0609  -0.0188 36  LYS B CD  
1906 C CE  . LYS B 34  ? 0.5370 0.4767 0.4708 -0.0298 0.0682  -0.0201 36  LYS B CE  
1907 N NZ  . LYS B 34  ? 0.6149 0.5479 0.5554 -0.0245 0.0707  -0.0179 36  LYS B NZ  
1908 N N   . HIS B 35  ? 0.2163 0.1896 0.1541 -0.0261 0.0461  -0.0161 37  HIS B N   
1909 C CA  . HIS B 35  ? 0.2114 0.1943 0.1520 -0.0251 0.0413  -0.0161 37  HIS B CA  
1910 C C   . HIS B 35  ? 0.2018 0.1925 0.1471 -0.0218 0.0366  -0.0152 37  HIS B C   
1911 O O   . HIS B 35  ? 0.1810 0.1693 0.1304 -0.0172 0.0355  -0.0126 37  HIS B O   
1912 C CB  . HIS B 35  ? 0.2140 0.1937 0.1573 -0.0214 0.0402  -0.0133 37  HIS B CB  
1913 C CG  . HIS B 35  ? 0.2423 0.2136 0.1798 -0.0244 0.0442  -0.0137 37  HIS B CG  
1914 N ND1 . HIS B 35  ? 0.2527 0.2123 0.1881 -0.0237 0.0484  -0.0123 37  HIS B ND1 
1915 C CD2 . HIS B 35  ? 0.2656 0.2380 0.1989 -0.0283 0.0449  -0.0156 37  HIS B CD2 
1916 C CE1 . HIS B 35  ? 0.2810 0.2341 0.2103 -0.0270 0.0514  -0.0129 37  HIS B CE1 
1917 N NE2 . HIS B 35  ? 0.2811 0.2414 0.2085 -0.0303 0.0496  -0.0150 37  HIS B NE2 
1918 N N   . PRO B 36  ? 0.2094 0.2088 0.1540 -0.0241 0.0339  -0.0172 38  PRO B N   
1919 C CA  . PRO B 36  ? 0.1865 0.1917 0.1347 -0.0207 0.0294  -0.0158 38  PRO B CA  
1920 C C   . PRO B 36  ? 0.1600 0.1699 0.1142 -0.0158 0.0256  -0.0140 38  PRO B C   
1921 O O   . PRO B 36  ? 0.1507 0.1636 0.1063 -0.0162 0.0253  -0.0147 38  PRO B O   
1922 C CB  . PRO B 36  ? 0.2010 0.2145 0.1468 -0.0245 0.0272  -0.0183 38  PRO B CB  
1923 C CG  . PRO B 36  ? 0.2299 0.2462 0.1744 -0.0286 0.0290  -0.0210 38  PRO B CG  
1924 C CD  . PRO B 36  ? 0.2137 0.2185 0.1545 -0.0299 0.0345  -0.0207 38  PRO B CD  
1925 N N   . LEU B 37  ? 0.1493 0.1595 0.1065 -0.0118 0.0232  -0.0119 39  LEU B N   
1926 C CA  . LEU B 37  ? 0.1451 0.1595 0.1076 -0.0074 0.0198  -0.0104 39  LEU B CA  
1927 C C   . LEU B 37  ? 0.1522 0.1755 0.1164 -0.0068 0.0158  -0.0113 39  LEU B C   
1928 O O   . LEU B 37  ? 0.1690 0.1947 0.1303 -0.0090 0.0149  -0.0123 39  LEU B O   
1929 C CB  . LEU B 37  ? 0.1468 0.1564 0.1113 -0.0038 0.0197  -0.0079 39  LEU B CB  
1930 C CG  . LEU B 37  ? 0.1569 0.1587 0.1221 -0.0031 0.0230  -0.0066 39  LEU B CG  
1931 C CD1 . LEU B 37  ? 0.1628 0.1620 0.1308 0.0000  0.0227  -0.0049 39  LEU B CD1 
1932 C CD2 . LEU B 37  ? 0.1436 0.1449 0.1105 -0.0023 0.0229  -0.0058 39  LEU B CD2 
1933 N N   . GLN B 38  ? 0.1356 0.1637 0.1046 -0.0038 0.0134  -0.0110 40  GLN B N   
1934 C CA  . GLN B 38  ? 0.1221 0.1581 0.0944 -0.0017 0.0094  -0.0114 40  GLN B CA  
1935 C C   . GLN B 38  ? 0.1500 0.1838 0.1206 0.0006  0.0073  -0.0094 40  GLN B C   
1936 O O   . GLN B 38  ? 0.1344 0.1731 0.1043 0.0006  0.0041  -0.0096 40  GLN B O   
1937 C CB  . GLN B 38  ? 0.1133 0.1529 0.0909 0.0012  0.0084  -0.0115 40  GLN B CB  
1938 C CG  . GLN B 38  ? 0.1327 0.1799 0.1149 0.0043  0.0048  -0.0119 40  GLN B CG  
1939 C CD  . GLN B 38  ? 0.1544 0.2107 0.1386 0.0019  0.0035  -0.0146 40  GLN B CD  
1940 O OE1 . GLN B 38  ? 0.1783 0.2362 0.1611 -0.0025 0.0060  -0.0170 40  GLN B OE1 
1941 N NE2 . GLN B 38  ? 0.2187 0.2813 0.2063 0.0047  -0.0003 -0.0144 40  GLN B NE2 
1942 N N   . ASN B 39  ? 0.1524 0.1789 0.1220 0.0025  0.0086  -0.0074 41  ASN B N   
1943 C CA  . ASN B 39  ? 0.1355 0.1580 0.1028 0.0043  0.0074  -0.0055 41  ASN B CA  
1944 C C   . ASN B 39  ? 0.1295 0.1441 0.0927 0.0021  0.0109  -0.0052 41  ASN B C   
1945 O O   . ASN B 39  ? 0.1488 0.1601 0.1128 0.0009  0.0142  -0.0056 41  ASN B O   
1946 C CB  . ASN B 39  ? 0.1542 0.1756 0.1250 0.0085  0.0063  -0.0040 41  ASN B CB  
1947 C CG  . ASN B 39  ? 0.1770 0.2052 0.1516 0.0112  0.0029  -0.0043 41  ASN B CG  
1948 O OD1 . ASN B 39  ? 0.1986 0.2286 0.1716 0.0124  0.0000  -0.0036 41  ASN B OD1 
1949 N ND2 . ASN B 39  ? 0.1474 0.1793 0.1267 0.0122  0.0033  -0.0053 41  ASN B ND2 
1950 N N   . ARG B 40  ? 0.1437 0.1549 0.1023 0.0015  0.0104  -0.0044 42  ARG B N   
1951 C CA  . ARG B 40  ? 0.1422 0.1453 0.0974 -0.0001 0.0141  -0.0042 42  ARG B CA  
1952 C C   . ARG B 40  ? 0.1501 0.1500 0.1083 0.0033  0.0143  -0.0027 42  ARG B C   
1953 O O   . ARG B 40  ? 0.1400 0.1417 0.0990 0.0062  0.0111  -0.0015 42  ARG B O   
1954 C CB  . ARG B 40  ? 0.1527 0.1531 0.1000 -0.0032 0.0134  -0.0043 42  ARG B CB  
1955 C CG  . ARG B 40  ? 0.1875 0.1793 0.1299 -0.0061 0.0178  -0.0048 42  ARG B CG  
1956 C CD  . ARG B 40  ? 0.2630 0.2524 0.1955 -0.0104 0.0168  -0.0051 42  ARG B CD  
1957 N NE  . ARG B 40  ? 0.2717 0.2658 0.2030 -0.0137 0.0165  -0.0068 42  ARG B NE  
1958 C CZ  . ARG B 40  ? 0.2615 0.2635 0.1920 -0.0141 0.0117  -0.0067 42  ARG B CZ  
1959 N NH1 . ARG B 40  ? 0.2675 0.2730 0.1977 -0.0110 0.0061  -0.0045 42  ARG B NH1 
1960 N NH2 . ARG B 40  ? 0.2162 0.2223 0.1463 -0.0177 0.0125  -0.0088 42  ARG B NH2 
1961 N N   . TRP B 41  ? 0.1443 0.1396 0.1047 0.0029  0.0182  -0.0030 43  TRP B N   
1962 C CA  . TRP B 41  ? 0.1642 0.1575 0.1285 0.0054  0.0188  -0.0020 43  TRP B CA  
1963 C C   . TRP B 41  ? 0.1560 0.1430 0.1186 0.0037  0.0228  -0.0027 43  TRP B C   
1964 O O   . TRP B 41  ? 0.1611 0.1447 0.1217 0.0009  0.0262  -0.0040 43  TRP B O   
1965 C CB  . TRP B 41  ? 0.1423 0.1381 0.1133 0.0072  0.0192  -0.0017 43  TRP B CB  
1966 C CG  . TRP B 41  ? 0.1344 0.1359 0.1070 0.0083  0.0162  -0.0015 43  TRP B CG  
1967 C CD1 . TRP B 41  ? 0.1363 0.1405 0.1081 0.0066  0.0161  -0.0024 43  TRP B CD1 
1968 C CD2 . TRP B 41  ? 0.1105 0.1155 0.0860 0.0109  0.0135  -0.0008 43  TRP B CD2 
1969 N NE1 . TRP B 41  ? 0.1375 0.1470 0.1114 0.0079  0.0135  -0.0026 43  TRP B NE1 
1970 C CE2 . TRP B 41  ? 0.1336 0.1436 0.1100 0.0106  0.0120  -0.0015 43  TRP B CE2 
1971 C CE3 . TRP B 41  ? 0.1251 0.1294 0.1019 0.0129  0.0127  -0.0001 43  TRP B CE3 
1972 C CZ2 . TRP B 41  ? 0.1252 0.1391 0.1042 0.0124  0.0100  -0.0016 43  TRP B CZ2 
1973 C CZ3 . TRP B 41  ? 0.1252 0.1328 0.1041 0.0146  0.0107  0.0001  43  TRP B CZ3 
1974 C CH2 . TRP B 41  ? 0.1218 0.1342 0.1019 0.0145  0.0094  -0.0007 43  TRP B CH2 
1975 N N   . ALA B 42  ? 0.1645 0.1495 0.1275 0.0050  0.0227  -0.0021 44  ALA B N   
1976 C CA  . ALA B 42  ? 0.1696 0.1489 0.1317 0.0032  0.0268  -0.0032 44  ALA B CA  
1977 C C   . ALA B 42  ? 0.1636 0.1446 0.1337 0.0053  0.0279  -0.0031 44  ALA B C   
1978 O O   . ALA B 42  ? 0.1566 0.1405 0.1289 0.0076  0.0252  -0.0021 44  ALA B O   
1979 C CB  . ALA B 42  ? 0.1740 0.1487 0.1280 0.0019  0.0260  -0.0028 44  ALA B CB  
1980 N N   . LEU B 43  ? 0.1476 0.1270 0.1225 0.0045  0.0321  -0.0045 45  LEU B N   
1981 C CA  . LEU B 43  ? 0.1456 0.1271 0.1289 0.0061  0.0334  -0.0047 45  LEU B CA  
1982 C C   . LEU B 43  ? 0.1572 0.1346 0.1390 0.0038  0.0371  -0.0066 45  LEU B C   
1983 O O   . LEU B 43  ? 0.1730 0.1451 0.1509 0.0008  0.0413  -0.0084 45  LEU B O   
1984 C CB  . LEU B 43  ? 0.1347 0.1173 0.1257 0.0070  0.0359  -0.0051 45  LEU B CB  
1985 C CG  . LEU B 43  ? 0.1626 0.1489 0.1642 0.0090  0.0368  -0.0053 45  LEU B CG  
1986 C CD1 . LEU B 43  ? 0.1569 0.1490 0.1614 0.0114  0.0317  -0.0032 45  LEU B CD1 
1987 C CD2 . LEU B 43  ? 0.2152 0.2015 0.2243 0.0105  0.0392  -0.0053 45  LEU B CD2 
1988 N N   . TRP B 44  ? 0.1560 0.1353 0.1400 0.0048  0.0358  -0.0063 46  TRP B N   
1989 C CA  . TRP B 44  ? 0.1773 0.1529 0.1595 0.0024  0.0391  -0.0081 46  TRP B CA  
1990 C C   . TRP B 44  ? 0.1893 0.1704 0.1829 0.0034  0.0405  -0.0093 46  TRP B C   
1991 O O   . TRP B 44  ? 0.1707 0.1583 0.1713 0.0061  0.0373  -0.0078 46  TRP B O   
1992 C CB  . TRP B 44  ? 0.1861 0.1591 0.1606 0.0024  0.0363  -0.0070 46  TRP B CB  
1993 C CG  . TRP B 44  ? 0.2100 0.1794 0.1748 0.0024  0.0335  -0.0053 46  TRP B CG  
1994 C CD1 . TRP B 44  ? 0.2296 0.2028 0.1941 0.0050  0.0290  -0.0034 46  TRP B CD1 
1995 C CD2 . TRP B 44  ? 0.2677 0.2292 0.2216 -0.0005 0.0348  -0.0055 46  TRP B CD2 
1996 N NE1 . TRP B 44  ? 0.2399 0.2092 0.1953 0.0042  0.0271  -0.0024 46  TRP B NE1 
1997 C CE2 . TRP B 44  ? 0.2793 0.2410 0.2274 0.0009  0.0303  -0.0033 46  TRP B CE2 
1998 C CE3 . TRP B 44  ? 0.3125 0.2666 0.2606 -0.0046 0.0394  -0.0074 46  TRP B CE3 
1999 C CZ2 . TRP B 44  ? 0.3313 0.2866 0.2681 -0.0014 0.0295  -0.0026 46  TRP B CZ2 
2000 C CZ3 . TRP B 44  ? 0.3547 0.3011 0.2902 -0.0073 0.0391  -0.0067 46  TRP B CZ3 
2001 C CH2 . TRP B 44  ? 0.3580 0.3051 0.2879 -0.0055 0.0337  -0.0040 46  TRP B CH2 
2002 N N   . PHE B 45  ? 0.2006 0.1791 0.1956 0.0006  0.0455  -0.0121 47  PHE B N   
2003 C CA  . PHE B 45  ? 0.2041 0.1883 0.2098 0.0008  0.0472  -0.0137 47  PHE B CA  
2004 C C   . PHE B 45  ? 0.2129 0.1932 0.2133 -0.0027 0.0497  -0.0157 47  PHE B C   
2005 O O   . PHE B 45  ? 0.2318 0.2036 0.2219 -0.0060 0.0527  -0.0168 47  PHE B O   
2006 C CB  . PHE B 45  ? 0.2331 0.2185 0.2479 0.0006  0.0520  -0.0160 47  PHE B CB  
2007 C CG  . PHE B 45  ? 0.2583 0.2499 0.2851 0.0004  0.0545  -0.0185 47  PHE B CG  
2008 C CD1 . PHE B 45  ? 0.2624 0.2635 0.3006 0.0039  0.0507  -0.0169 47  PHE B CD1 
2009 C CD2 . PHE B 45  ? 0.2982 0.2865 0.3248 -0.0037 0.0608  -0.0225 47  PHE B CD2 
2010 C CE1 . PHE B 45  ? 0.2849 0.2932 0.3353 0.0036  0.0526  -0.0193 47  PHE B CE1 
2011 C CE2 . PHE B 45  ? 0.3076 0.3030 0.3466 -0.0041 0.0634  -0.0253 47  PHE B CE2 
2012 C CZ  . PHE B 45  ? 0.2822 0.2882 0.3336 -0.0003 0.0590  -0.0236 47  PHE B CZ  
2013 N N   . PHE B 46  ? 0.1875 0.1734 0.1939 -0.0023 0.0485  -0.0162 48  PHE B N   
2014 C CA  . PHE B 46  ? 0.2418 0.2244 0.2443 -0.0061 0.0517  -0.0187 48  PHE B CA  
2015 C C   . PHE B 46  ? 0.2576 0.2490 0.2731 -0.0067 0.0533  -0.0211 48  PHE B C   
2016 O O   . PHE B 46  ? 0.2229 0.2234 0.2476 -0.0038 0.0492  -0.0196 48  PHE B O   
2017 C CB  . PHE B 46  ? 0.2812 0.2600 0.2742 -0.0059 0.0483  -0.0167 48  PHE B CB  
2018 C CG  . PHE B 46  ? 0.3419 0.3147 0.3283 -0.0102 0.0521  -0.0191 48  PHE B CG  
2019 C CD1 . PHE B 46  ? 0.3724 0.3340 0.3468 -0.0135 0.0557  -0.0200 48  PHE B CD1 
2020 C CD2 . PHE B 46  ? 0.3884 0.3661 0.3797 -0.0115 0.0522  -0.0206 48  PHE B CD2 
2021 C CE1 . PHE B 46  ? 0.3998 0.3544 0.3670 -0.0179 0.0596  -0.0222 48  PHE B CE1 
2022 C CE2 . PHE B 46  ? 0.4045 0.3758 0.3888 -0.0160 0.0563  -0.0231 48  PHE B CE2 
2023 C CZ  . PHE B 46  ? 0.4038 0.3633 0.3762 -0.0191 0.0601  -0.0239 48  PHE B CZ  
2024 N N   . LYS B 47  ? 0.2970 0.2863 0.3134 -0.0110 0.0593  -0.0251 49  LYS B N   
2025 C CA  . LYS B 47  ? 0.3499 0.3480 0.3774 -0.0125 0.0607  -0.0279 49  LYS B CA  
2026 C C   . LYS B 47  ? 0.4309 0.4221 0.4499 -0.0183 0.0657  -0.0313 49  LYS B C   
2027 O O   . LYS B 47  ? 0.4356 0.4182 0.4476 -0.0217 0.0711  -0.0335 49  LYS B O   
2028 C CB  . LYS B 47  ? 0.3624 0.3685 0.4056 -0.0113 0.0635  -0.0302 49  LYS B CB  
2029 C CG  . LYS B 47  ? 0.4325 0.4513 0.4905 -0.0114 0.0628  -0.0322 49  LYS B CG  
2030 C CD  . LYS B 47  ? 0.4767 0.5039 0.5517 -0.0087 0.0649  -0.0338 49  LYS B CD  
2031 C CE  . LYS B 47  ? 0.5324 0.5725 0.6228 -0.0097 0.0652  -0.0368 49  LYS B CE  
2032 N NZ  . LYS B 47  ? 0.5841 0.6319 0.6758 -0.0084 0.0579  -0.0338 49  LYS B NZ  
2033 N N   . ASN B 48  ? 0.4851 0.4789 0.5033 -0.0199 0.0642  -0.0317 50  ASN B N   
2034 C CA  . ASN B 48  ? 0.5440 0.5304 0.5533 -0.0257 0.0691  -0.0349 50  ASN B CA  
2035 C C   . ASN B 48  ? 0.5815 0.5740 0.6018 -0.0296 0.0753  -0.0403 50  ASN B C   
2036 O O   . ASN B 48  ? 0.5818 0.5866 0.6155 -0.0298 0.0744  -0.0422 50  ASN B O   
2037 C CB  . ASN B 48  ? 0.5818 0.5693 0.5873 -0.0264 0.0660  -0.0340 50  ASN B CB  
2038 C CG  . ASN B 48  ? 0.6592 0.6330 0.6482 -0.0305 0.0693  -0.0348 50  ASN B CG  
2039 O OD1 . ASN B 48  ? 0.6891 0.6516 0.6678 -0.0335 0.0738  -0.0359 50  ASN B OD1 
2040 N ND2 . ASN B 48  ? 0.6817 0.6554 0.6672 -0.0311 0.0671  -0.0341 50  ASN B ND2 
2041 N N   . ASP B 49  ? 0.6112 0.5952 0.6261 -0.0329 0.0815  -0.0430 51  ASP B N   
2042 C CA  . ASP B 49  ? 0.6330 0.6198 0.6558 -0.0377 0.0892  -0.0489 51  ASP B CA  
2043 C C   . ASP B 49  ? 0.6580 0.6307 0.6643 -0.0449 0.0954  -0.0518 51  ASP B C   
2044 O O   . ASP B 49  ? 0.6689 0.6280 0.6603 -0.0465 0.0973  -0.0506 51  ASP B O   
2045 C CB  . ASP B 49  ? 0.6639 0.6510 0.6931 -0.0358 0.0920  -0.0497 51  ASP B CB  
2046 C CG  . ASP B 49  ? 0.7301 0.7190 0.7676 -0.0406 0.1009  -0.0562 51  ASP B CG  
2047 O OD1 . ASP B 49  ? 0.7402 0.7300 0.7780 -0.0461 0.1053  -0.0605 51  ASP B OD1 
2048 O OD2 . ASP B 49  ? 0.7607 0.7497 0.8042 -0.0393 0.1040  -0.0573 51  ASP B OD2 
2049 N N   . LYS B 50  ? 0.6605 0.6362 0.6688 -0.0497 0.0986  -0.0557 52  LYS B N   
2050 C CA  . LYS B 50  ? 0.6752 0.6371 0.6673 -0.0571 0.1047  -0.0586 52  LYS B CA  
2051 C C   . LYS B 50  ? 0.6799 0.6333 0.6671 -0.0627 0.1132  -0.0630 52  LYS B C   
2052 O O   . LYS B 50  ? 0.7019 0.6399 0.6712 -0.0683 0.1176  -0.0640 52  LYS B O   
2053 C CB  . LYS B 50  ? 0.6983 0.6675 0.6962 -0.0615 0.1067  -0.0626 52  LYS B CB  
2054 C CG  . LYS B 50  ? 0.7628 0.7163 0.7414 -0.0682 0.1114  -0.0642 52  LYS B CG  
2055 C CD  . LYS B 50  ? 0.8097 0.7706 0.7955 -0.0750 0.1166  -0.0705 52  LYS B CD  
2056 C CE  . LYS B 50  ? 0.8664 0.8102 0.8323 -0.0825 0.1224  -0.0727 52  LYS B CE  
2057 N NZ  . LYS B 50  ? 0.8908 0.8416 0.8639 -0.0905 0.1293  -0.0801 52  LYS B NZ  
2058 N N   . SER B 51  ? 0.6597 0.6217 0.6617 -0.0614 0.1160  -0.0657 53  SER B N   
2059 C CA  . SER B 51  ? 0.6648 0.6184 0.6621 -0.0670 0.1248  -0.0702 53  SER B CA  
2060 C C   . SER B 51  ? 0.6784 0.6161 0.6569 -0.0668 0.1238  -0.0663 53  SER B C   
2061 O O   . SER B 51  ? 0.6971 0.6224 0.6632 -0.0734 0.1307  -0.0694 53  SER B O   
2062 C CB  . SER B 51  ? 0.6641 0.6316 0.6839 -0.0653 0.1285  -0.0744 53  SER B CB  
2063 O OG  . SER B 51  ? 0.6678 0.6374 0.6926 -0.0589 0.1246  -0.0706 53  SER B OG  
2064 N N   . LYS B 52  ? 0.6575 0.5961 0.6340 -0.0596 0.1152  -0.0597 54  LYS B N   
2065 C CA  . LYS B 52  ? 0.6389 0.5646 0.5986 -0.0589 0.1128  -0.0555 54  LYS B CA  
2066 C C   . LYS B 52  ? 0.6086 0.5252 0.5520 -0.0572 0.1065  -0.0501 54  LYS B C   
2067 O O   . LYS B 52  ? 0.5919 0.5135 0.5390 -0.0554 0.1033  -0.0492 54  LYS B O   
2068 C CB  . LYS B 52  ? 0.6564 0.5898 0.6262 -0.0523 0.1083  -0.0525 54  LYS B CB  
2069 C CG  . LYS B 52  ? 0.6970 0.6399 0.6848 -0.0522 0.1137  -0.0570 54  LYS B CG  
2070 C CD  . LYS B 52  ? 0.7479 0.6969 0.7438 -0.0453 0.1085  -0.0533 54  LYS B CD  
2071 C CE  . LYS B 52  ? 0.7897 0.7466 0.8031 -0.0443 0.1139  -0.0573 54  LYS B CE  
2072 N NZ  . LYS B 52  ? 0.8185 0.7761 0.8344 -0.0393 0.1107  -0.0539 54  LYS B NZ  
2073 N N   . THR B 53  ? 0.5987 0.5018 0.5242 -0.0579 0.1047  -0.0467 55  THR B N   
2074 C CA  . THR B 53  ? 0.6057 0.5005 0.5170 -0.0551 0.0982  -0.0411 55  THR B CA  
2075 C C   . THR B 53  ? 0.6046 0.5110 0.5268 -0.0466 0.0897  -0.0366 55  THR B C   
2076 O O   . THR B 53  ? 0.6035 0.5211 0.5400 -0.0433 0.0887  -0.0370 55  THR B O   
2077 C CB  . THR B 53  ? 0.6298 0.5095 0.5215 -0.0573 0.0975  -0.0382 55  THR B CB  
2078 O OG1 . THR B 53  ? 0.6382 0.5231 0.5356 -0.0551 0.0961  -0.0375 55  THR B OG1 
2079 C CG2 . THR B 53  ? 0.6359 0.5015 0.5131 -0.0662 0.1054  -0.0419 55  THR B CG2 
2080 N N   . TRP B 54  ? 0.6021 0.5050 0.5171 -0.0433 0.0841  -0.0324 56  TRP B N   
2081 C CA  . TRP B 54  ? 0.5973 0.5085 0.5189 -0.0359 0.0763  -0.0280 56  TRP B CA  
2082 C C   . TRP B 54  ? 0.5922 0.5040 0.5128 -0.0332 0.0731  -0.0254 56  TRP B C   
2083 O O   . TRP B 54  ? 0.5913 0.5142 0.5241 -0.0285 0.0694  -0.0242 56  TRP B O   
2084 C CB  . TRP B 54  ? 0.6148 0.5185 0.5256 -0.0337 0.0720  -0.0243 56  TRP B CB  
2085 C CG  . TRP B 54  ? 0.6287 0.5398 0.5451 -0.0266 0.0645  -0.0201 56  TRP B CG  
2086 C CD1 . TRP B 54  ? 0.6375 0.5586 0.5645 -0.0233 0.0617  -0.0198 56  TRP B CD1 
2087 C CD2 . TRP B 54  ? 0.6395 0.5491 0.5512 -0.0227 0.0593  -0.0160 56  TRP B CD2 
2088 N NE1 . TRP B 54  ? 0.6422 0.5675 0.5711 -0.0176 0.0554  -0.0159 56  TRP B NE1 
2089 C CE2 . TRP B 54  ? 0.6449 0.5638 0.5653 -0.0170 0.0538  -0.0136 56  TRP B CE2 
2090 C CE3 . TRP B 54  ? 0.6562 0.5576 0.5568 -0.0239 0.0587  -0.0143 56  TRP B CE3 
2091 C CZ2 . TRP B 54  ? 0.6511 0.5719 0.5703 -0.0125 0.0482  -0.0100 56  TRP B CZ2 
2092 C CZ3 . TRP B 54  ? 0.6700 0.5741 0.5698 -0.0194 0.0526  -0.0105 56  TRP B CZ3 
2093 C CH2 . TRP B 54  ? 0.6607 0.5745 0.5700 -0.0137 0.0476  -0.0085 56  TRP B CH2 
2094 N N   . GLN B 55  ? 0.5781 0.4780 0.4839 -0.0365 0.0745  -0.0246 57  GLN B N   
2095 C CA  . GLN B 55  ? 0.5784 0.4782 0.4812 -0.0346 0.0712  -0.0221 57  GLN B CA  
2096 C C   . GLN B 55  ? 0.5551 0.4627 0.4701 -0.0356 0.0752  -0.0255 57  GLN B C   
2097 O O   . GLN B 55  ? 0.5484 0.4621 0.4690 -0.0320 0.0718  -0.0237 57  GLN B O   
2098 C CB  . GLN B 55  ? 0.6357 0.5204 0.5183 -0.0389 0.0717  -0.0205 57  GLN B CB  
2099 C CG  . GLN B 55  ? 0.7319 0.6169 0.6095 -0.0359 0.0655  -0.0165 57  GLN B CG  
2100 C CD  . GLN B 55  ? 0.8535 0.7252 0.7125 -0.0410 0.0663  -0.0155 57  GLN B CD  
2101 O OE1 . GLN B 55  ? 0.9032 0.7745 0.7601 -0.0441 0.0682  -0.0167 57  GLN B OE1 
2102 N NE2 . GLN B 55  ? 0.8811 0.7410 0.7256 -0.0423 0.0650  -0.0131 57  GLN B NE2 
2103 N N   . ALA B 56  ? 0.5460 0.4529 0.4651 -0.0406 0.0829  -0.0306 58  ALA B N   
2104 C CA  . ALA B 56  ? 0.5316 0.4462 0.4645 -0.0410 0.0874  -0.0342 58  ALA B CA  
2105 C C   . ALA B 56  ? 0.4836 0.4137 0.4363 -0.0350 0.0841  -0.0338 58  ALA B C   
2106 O O   . ALA B 56  ? 0.4759 0.4129 0.4403 -0.0328 0.0853  -0.0348 58  ALA B O   
2107 C CB  . ALA B 56  ? 0.5494 0.4594 0.4818 -0.0481 0.0968  -0.0401 58  ALA B CB  
2108 N N   . ASN B 57  ? 0.4467 0.3811 0.4022 -0.0324 0.0802  -0.0322 59  ASN B N   
2109 C CA  . ASN B 57  ? 0.4361 0.3842 0.4077 -0.0271 0.0761  -0.0311 59  ASN B CA  
2110 C C   . ASN B 57  ? 0.4150 0.3665 0.3868 -0.0212 0.0687  -0.0262 59  ASN B C   
2111 O O   . ASN B 57  ? 0.4055 0.3673 0.3906 -0.0173 0.0664  -0.0256 59  ASN B O   
2112 C CB  . ASN B 57  ? 0.4598 0.4115 0.4341 -0.0274 0.0750  -0.0317 59  ASN B CB  
2113 C CG  . ASN B 57  ? 0.5310 0.4841 0.5107 -0.0327 0.0821  -0.0372 59  ASN B CG  
2114 O OD1 . ASN B 57  ? 0.5398 0.4986 0.5309 -0.0336 0.0865  -0.0406 59  ASN B OD1 
2115 N ND2 . ASN B 57  ? 0.5606 0.5088 0.5329 -0.0362 0.0836  -0.0384 59  ASN B ND2 
2116 N N   . LEU B 58  ? 0.4035 0.3468 0.3611 -0.0207 0.0650  -0.0228 60  LEU B N   
2117 C CA  . LEU B 58  ? 0.3874 0.3341 0.3451 -0.0159 0.0588  -0.0189 60  LEU B CA  
2118 C C   . LEU B 58  ? 0.3744 0.3189 0.3303 -0.0170 0.0605  -0.0192 60  LEU B C   
2119 O O   . LEU B 58  ? 0.3912 0.3262 0.3354 -0.0213 0.0636  -0.0202 60  LEU B O   
2120 C CB  . LEU B 58  ? 0.4005 0.3416 0.3465 -0.0142 0.0537  -0.0152 60  LEU B CB  
2121 C CG  . LEU B 58  ? 0.4006 0.3469 0.3483 -0.0093 0.0473  -0.0117 60  LEU B CG  
2122 C CD1 . LEU B 58  ? 0.3752 0.3313 0.3342 -0.0055 0.0443  -0.0110 60  LEU B CD1 
2123 C CD2 . LEU B 58  ? 0.4264 0.3660 0.3619 -0.0083 0.0433  -0.0086 60  LEU B CD2 
2124 N N   . ARG B 59  ? 0.3191 0.2714 0.2853 -0.0136 0.0589  -0.0186 61  ARG B N   
2125 C CA  . ARG B 59  ? 0.3178 0.2681 0.2831 -0.0147 0.0611  -0.0193 61  ARG B CA  
2126 C C   . ARG B 59  ? 0.3074 0.2615 0.2728 -0.0109 0.0555  -0.0160 61  ARG B C   
2127 O O   . ARG B 59  ? 0.3062 0.2680 0.2806 -0.0067 0.0519  -0.0144 61  ARG B O   
2128 C CB  . ARG B 59  ? 0.3426 0.2974 0.3213 -0.0147 0.0665  -0.0225 61  ARG B CB  
2129 C CG  . ARG B 59  ? 0.4549 0.4053 0.4332 -0.0198 0.0738  -0.0269 61  ARG B CG  
2130 C CD  . ARG B 59  ? 0.5164 0.4748 0.5119 -0.0186 0.0779  -0.0301 61  ARG B CD  
2131 N NE  . ARG B 59  ? 0.5711 0.5297 0.5737 -0.0183 0.0823  -0.0320 61  ARG B NE  
2132 C CZ  . ARG B 59  ? 0.6522 0.6144 0.6677 -0.0187 0.0884  -0.0360 61  ARG B CZ  
2133 N NH1 . ARG B 59  ? 0.6600 0.6212 0.6813 -0.0181 0.0926  -0.0375 61  ARG B NH1 
2134 N NH2 . ARG B 59  ? 0.6735 0.6404 0.6965 -0.0200 0.0908  -0.0387 61  ARG B NH2 
2135 N N   . LEU B 60  ? 0.3051 0.2539 0.2601 -0.0129 0.0547  -0.0151 62  LEU B N   
2136 C CA  . LEU B 60  ? 0.3084 0.2607 0.2638 -0.0105 0.0509  -0.0131 62  LEU B CA  
2137 C C   . LEU B 60  ? 0.3057 0.2598 0.2696 -0.0107 0.0553  -0.0152 62  LEU B C   
2138 O O   . LEU B 60  ? 0.3256 0.2740 0.2865 -0.0149 0.0613  -0.0180 62  LEU B O   
2139 C CB  . LEU B 60  ? 0.3223 0.2686 0.2637 -0.0136 0.0491  -0.0120 62  LEU B CB  
2140 C CG  . LEU B 60  ? 0.3661 0.3159 0.3070 -0.0128 0.0463  -0.0109 62  LEU B CG  
2141 C CD1 . LEU B 60  ? 0.3544 0.3120 0.3017 -0.0076 0.0406  -0.0083 62  LEU B CD1 
2142 C CD2 . LEU B 60  ? 0.3950 0.3395 0.3222 -0.0165 0.0446  -0.0102 62  LEU B CD2 
2143 N N   . ILE B 61  ? 0.2629 0.2239 0.2370 -0.0065 0.0530  -0.0139 63  ILE B N   
2144 C CA  A ILE B 61  ? 0.2680 0.2300 0.2505 -0.0057 0.0569  -0.0153 63  ILE B CA  
2145 C CA  B ILE B 61  ? 0.2689 0.2309 0.2514 -0.0058 0.0570  -0.0153 63  ILE B CA  
2146 C C   . ILE B 61  ? 0.2791 0.2382 0.2552 -0.0073 0.0569  -0.0150 63  ILE B C   
2147 O O   . ILE B 61  ? 0.3096 0.2638 0.2846 -0.0102 0.0625  -0.0174 63  ILE B O   
2148 C CB  A ILE B 61  ? 0.2606 0.2307 0.2561 -0.0006 0.0540  -0.0136 63  ILE B CB  
2149 C CB  B ILE B 61  ? 0.2634 0.2333 0.2594 -0.0007 0.0546  -0.0139 63  ILE B CB  
2150 C CG1 A ILE B 61  ? 0.2777 0.2516 0.2796 0.0002  0.0540  -0.0144 63  ILE B CG1 
2151 C CG1 B ILE B 61  ? 0.2763 0.2496 0.2799 -0.0002 0.0558  -0.0152 63  ILE B CG1 
2152 C CG2 A ILE B 61  ? 0.2592 0.2297 0.2638 0.0011  0.0576  -0.0145 63  ILE B CG2 
2153 C CG2 B ILE B 61  ? 0.2688 0.2385 0.2724 0.0008  0.0578  -0.0145 63  ILE B CG2 
2154 C CD1 A ILE B 61  ? 0.2865 0.2570 0.2909 -0.0033 0.0612  -0.0184 63  ILE B CD1 
2155 C CD1 B ILE B 61  ? 0.2697 0.2512 0.2872 0.0042  0.0537  -0.0140 63  ILE B CD1 
2156 N N   . SER B 62  ? 0.2456 0.2080 0.2178 -0.0056 0.0509  -0.0123 64  SER B N   
2157 C CA  . SER B 62  ? 0.2524 0.2135 0.2199 -0.0070 0.0508  -0.0121 64  SER B CA  
2158 C C   . SER B 62  ? 0.2345 0.2000 0.1977 -0.0055 0.0441  -0.0096 64  SER B C   
2159 O O   . SER B 62  ? 0.2245 0.1945 0.1912 -0.0023 0.0401  -0.0079 64  SER B O   
2160 C CB  . SER B 62  ? 0.3198 0.2818 0.2962 -0.0048 0.0533  -0.0124 64  SER B CB  
2161 O OG  . SER B 62  ? 0.4450 0.4044 0.4154 -0.0073 0.0543  -0.0129 64  SER B OG  
2162 N N   . LYS B 63  ? 0.2253 0.1899 0.1817 -0.0081 0.0434  -0.0099 65  LYS B N   
2163 C CA  . LYS B 63  ? 0.2034 0.1731 0.1569 -0.0070 0.0376  -0.0081 65  LYS B CA  
2164 C C   . LYS B 63  ? 0.2077 0.1787 0.1623 -0.0078 0.0386  -0.0087 65  LYS B C   
2165 O O   . LYS B 63  ? 0.2316 0.1976 0.1840 -0.0110 0.0436  -0.0106 65  LYS B O   
2166 C CB  . LYS B 63  ? 0.1871 0.1556 0.1304 -0.0098 0.0349  -0.0078 65  LYS B CB  
2167 C CG  . LYS B 63  ? 0.2090 0.1747 0.1489 -0.0092 0.0336  -0.0068 65  LYS B CG  
2168 C CD  . LYS B 63  ? 0.2365 0.2018 0.1666 -0.0106 0.0290  -0.0054 65  LYS B CD  
2169 C CE  . LYS B 63  ? 0.2570 0.2160 0.1808 -0.0114 0.0292  -0.0047 65  LYS B CE  
2170 N NZ  . LYS B 63  ? 0.3092 0.2682 0.2250 -0.0108 0.0233  -0.0022 65  LYS B NZ  
2171 N N   . PHE B 64  ? 0.1826 0.1595 0.1400 -0.0054 0.0345  -0.0073 66  PHE B N   
2172 C CA  . PHE B 64  ? 0.1763 0.1541 0.1339 -0.0065 0.0354  -0.0079 66  PHE B CA  
2173 C C   . PHE B 64  ? 0.1681 0.1525 0.1243 -0.0061 0.0305  -0.0073 66  PHE B C   
2174 O O   . PHE B 64  ? 0.1694 0.1582 0.1272 -0.0034 0.0263  -0.0059 66  PHE B O   
2175 C CB  . PHE B 64  ? 0.1863 0.1624 0.1514 -0.0037 0.0377  -0.0072 66  PHE B CB  
2176 C CG  . PHE B 64  ? 0.1813 0.1623 0.1526 0.0007  0.0337  -0.0051 66  PHE B CG  
2177 C CD1 . PHE B 64  ? 0.1525 0.1382 0.1245 0.0018  0.0301  -0.0040 66  PHE B CD1 
2178 C CD2 . PHE B 64  ? 0.1859 0.1669 0.1621 0.0030  0.0338  -0.0044 66  PHE B CD2 
2179 C CE1 . PHE B 64  ? 0.1675 0.1572 0.1441 0.0051  0.0267  -0.0023 66  PHE B CE1 
2180 C CE2 . PHE B 64  ? 0.1711 0.1567 0.1521 0.0062  0.0301  -0.0027 66  PHE B CE2 
2181 C CZ  . PHE B 64  ? 0.1690 0.1587 0.1499 0.0072  0.0266  -0.0016 66  PHE B CZ  
2182 N N   . ASP B 65  ? 0.1569 0.1421 0.1102 -0.0090 0.0314  -0.0086 67  ASP B N   
2183 C CA  . ASP B 65  ? 0.1613 0.1538 0.1142 -0.0091 0.0273  -0.0087 67  ASP B CA  
2184 C C   . ASP B 65  ? 0.1529 0.1456 0.1058 -0.0111 0.0293  -0.0099 67  ASP B C   
2185 O O   . ASP B 65  ? 0.1585 0.1571 0.1100 -0.0129 0.0271  -0.0110 67  ASP B O   
2186 C CB  . ASP B 65  ? 0.1743 0.1702 0.1213 -0.0119 0.0246  -0.0094 67  ASP B CB  
2187 C CG  . ASP B 65  ? 0.2370 0.2295 0.1767 -0.0178 0.0278  -0.0116 67  ASP B CG  
2188 O OD1 . ASP B 65  ? 0.2172 0.2038 0.1565 -0.0198 0.0330  -0.0129 67  ASP B OD1 
2189 O OD2 . ASP B 65  ? 0.2563 0.2516 0.1904 -0.0206 0.0250  -0.0121 67  ASP B OD2 
2190 N N   . THR B 66  ? 0.1676 0.1536 0.1222 -0.0107 0.0335  -0.0096 68  THR B N   
2191 C CA  . THR B 66  ? 0.1643 0.1484 0.1185 -0.0118 0.0354  -0.0100 68  THR B CA  
2192 C C   . THR B 66  ? 0.1564 0.1375 0.1164 -0.0075 0.0355  -0.0075 68  THR B C   
2193 O O   . THR B 66  ? 0.1547 0.1338 0.1191 -0.0044 0.0358  -0.0062 68  THR B O   
2194 C CB  . THR B 66  ? 0.1828 0.1600 0.1314 -0.0166 0.0409  -0.0123 68  THR B CB  
2195 O OG1 . THR B 66  ? 0.1750 0.1443 0.1257 -0.0152 0.0452  -0.0117 68  THR B OG1 
2196 C CG2 . THR B 66  ? 0.2252 0.2054 0.1671 -0.0219 0.0407  -0.0148 68  THR B CG2 
2197 N N   . VAL B 67  ? 0.1623 0.1427 0.1217 -0.0078 0.0354  -0.0071 69  VAL B N   
2198 C CA  . VAL B 67  ? 0.1572 0.1338 0.1205 -0.0042 0.0352  -0.0044 69  VAL B CA  
2199 C C   . VAL B 67  ? 0.1670 0.1353 0.1323 -0.0029 0.0395  -0.0037 69  VAL B C   
2200 O O   . VAL B 67  ? 0.1770 0.1444 0.1486 0.0013  0.0387  -0.0015 69  VAL B O   
2201 C CB  . VAL B 67  ? 0.1743 0.1496 0.1340 -0.0060 0.0350  -0.0043 69  VAL B CB  
2202 C CG1 . VAL B 67  ? 0.1998 0.1704 0.1625 -0.0023 0.0342  -0.0009 69  VAL B CG1 
2203 C CG2 . VAL B 67  ? 0.1838 0.1677 0.1428 -0.0072 0.0314  -0.0054 69  VAL B CG2 
2204 N N   . GLU B 68  ? 0.1734 0.1357 0.1336 -0.0068 0.0446  -0.0060 70  GLU B N   
2205 C CA  . GLU B 68  ? 0.2034 0.1570 0.1658 -0.0056 0.0496  -0.0058 70  GLU B CA  
2206 C C   . GLU B 68  ? 0.1984 0.1530 0.1661 -0.0036 0.0504  -0.0061 70  GLU B C   
2207 O O   . GLU B 68  ? 0.1954 0.1463 0.1697 0.0000  0.0524  -0.0048 70  GLU B O   
2208 C CB  . GLU B 68  ? 0.2123 0.1585 0.1672 -0.0108 0.0555  -0.0086 70  GLU B CB  
2209 C CG  . GLU B 68  ? 0.2559 0.1987 0.2057 -0.0128 0.0559  -0.0083 70  GLU B CG  
2210 C CD  . GLU B 68  ? 0.2647 0.2154 0.2103 -0.0159 0.0521  -0.0094 70  GLU B CD  
2211 O OE1 . GLU B 68  ? 0.1889 0.1486 0.1351 -0.0168 0.0487  -0.0106 70  GLU B OE1 
2212 O OE2 . GLU B 68  ? 0.3195 0.2667 0.2611 -0.0175 0.0528  -0.0092 70  GLU B OE2 
2213 N N   . ASP B 69  ? 0.1759 0.1356 0.1407 -0.0061 0.0490  -0.0078 71  ASP B N   
2214 C CA  . ASP B 69  ? 0.1612 0.1210 0.1293 -0.0050 0.0500  -0.0083 71  ASP B CA  
2215 C C   . ASP B 69  ? 0.1631 0.1282 0.1391 0.0000  0.0458  -0.0058 71  ASP B C   
2216 O O   . ASP B 69  ? 0.1756 0.1396 0.1574 0.0021  0.0476  -0.0058 71  ASP B O   
2217 C CB  . ASP B 69  ? 0.1903 0.1527 0.1514 -0.0093 0.0493  -0.0103 71  ASP B CB  
2218 C CG  . ASP B 69  ? 0.2502 0.2074 0.2031 -0.0153 0.0540  -0.0133 71  ASP B CG  
2219 O OD1 . ASP B 69  ? 0.2640 0.2133 0.2176 -0.0161 0.0601  -0.0145 71  ASP B OD1 
2220 O OD2 . ASP B 69  ? 0.2454 0.2067 0.1916 -0.0191 0.0515  -0.0144 71  ASP B OD2 
2221 N N   . PHE B 70  ? 0.1614 0.1321 0.1377 0.0017  0.0405  -0.0040 72  PHE B N   
2222 C CA  . PHE B 70  ? 0.1495 0.1247 0.1327 0.0059  0.0367  -0.0016 72  PHE B CA  
2223 C C   . PHE B 70  ? 0.1426 0.1140 0.1329 0.0093  0.0384  0.0002  72  PHE B C   
2224 O O   . PHE B 70  ? 0.1572 0.1301 0.1546 0.0120  0.0384  0.0008  72  PHE B O   
2225 C CB  . PHE B 70  ? 0.1349 0.1152 0.1162 0.0063  0.0318  -0.0004 72  PHE B CB  
2226 C CG  . PHE B 70  ? 0.1414 0.1246 0.1288 0.0100  0.0285  0.0022  72  PHE B CG  
2227 C CD1 . PHE B 70  ? 0.1461 0.1336 0.1372 0.0116  0.0264  0.0025  72  PHE B CD1 
2228 C CD2 . PHE B 70  ? 0.1548 0.1358 0.1434 0.0114  0.0275  0.0044  72  PHE B CD2 
2229 C CE1 . PHE B 70  ? 0.1561 0.1467 0.1524 0.0142  0.0233  0.0046  72  PHE B CE1 
2230 C CE2 . PHE B 70  ? 0.1414 0.1253 0.1349 0.0143  0.0240  0.0069  72  PHE B CE2 
2231 C CZ  . PHE B 70  ? 0.1420 0.1311 0.1395 0.0155  0.0219  0.0068  72  PHE B CZ  
2232 N N   . TRP B 71  ? 0.1463 0.1125 0.1344 0.0091  0.0399  0.0010  73  TRP B N   
2233 C CA  . TRP B 71  ? 0.1663 0.1285 0.1611 0.0130  0.0409  0.0033  73  TRP B CA  
2234 C C   . TRP B 71  ? 0.1833 0.1413 0.1834 0.0139  0.0464  0.0017  73  TRP B C   
2235 O O   . TRP B 71  ? 0.1839 0.1428 0.1934 0.0181  0.0461  0.0032  73  TRP B O   
2236 C CB  . TRP B 71  ? 0.1839 0.1401 0.1741 0.0127  0.0413  0.0049  73  TRP B CB  
2237 C CG  . TRP B 71  ? 0.1855 0.1454 0.1726 0.0128  0.0359  0.0071  73  TRP B CG  
2238 C CD1 . TRP B 71  ? 0.1875 0.1471 0.1662 0.0090  0.0353  0.0061  73  TRP B CD1 
2239 C CD2 . TRP B 71  ? 0.1779 0.1426 0.1700 0.0162  0.0306  0.0102  73  TRP B CD2 
2240 N NE1 . TRP B 71  ? 0.1855 0.1487 0.1636 0.0099  0.0305  0.0084  73  TRP B NE1 
2241 C CE2 . TRP B 71  ? 0.1860 0.1520 0.1716 0.0141  0.0274  0.0110  73  TRP B CE2 
2242 C CE3 . TRP B 71  ? 0.1774 0.1459 0.1789 0.0203  0.0284  0.0120  73  TRP B CE3 
2243 C CZ2 . TRP B 71  ? 0.1935 0.1635 0.1807 0.0158  0.0222  0.0137  73  TRP B CZ2 
2244 C CZ3 . TRP B 71  ? 0.1775 0.1504 0.1809 0.0221  0.0228  0.0150  73  TRP B CZ3 
2245 C CH2 . TRP B 71  ? 0.1938 0.1669 0.1895 0.0197  0.0198  0.0158  73  TRP B CH2 
2246 N N   . ALA B 72  ? 0.1830 0.1368 0.1776 0.0097  0.0515  -0.0017 74  ALA B N   
2247 C CA  . ALA B 72  ? 0.2060 0.1554 0.2054 0.0098  0.0576  -0.0039 74  ALA B CA  
2248 C C   . ALA B 72  ? 0.2000 0.1552 0.2067 0.0116  0.0564  -0.0043 74  ALA B C   
2249 O O   . ALA B 72  ? 0.1963 0.1507 0.2126 0.0145  0.0594  -0.0047 74  ALA B O   
2250 C CB  . ALA B 72  ? 0.2148 0.1588 0.2050 0.0038  0.0629  -0.0076 74  ALA B CB  
2251 N N   . LEU B 73  ? 0.1899 0.1512 0.1927 0.0100  0.0523  -0.0044 75  LEU B N   
2252 C CA  . LEU B 73  ? 0.1795 0.1460 0.1875 0.0112  0.0507  -0.0047 75  LEU B CA  
2253 C C   . LEU B 73  ? 0.1734 0.1453 0.1916 0.0163  0.0468  -0.0019 75  LEU B C   
2254 O O   . LEU B 73  ? 0.1904 0.1644 0.2178 0.0183  0.0484  -0.0025 75  LEU B O   
2255 C CB  . LEU B 73  ? 0.1865 0.1567 0.1868 0.0086  0.0471  -0.0050 75  LEU B CB  
2256 C CG  . LEU B 73  ? 0.1888 0.1629 0.1923 0.0090  0.0461  -0.0056 75  LEU B CG  
2257 C CD1 . LEU B 73  ? 0.1940 0.1636 0.1993 0.0068  0.0528  -0.0089 75  LEU B CD1 
2258 C CD2 . LEU B 73  ? 0.2026 0.1792 0.1981 0.0072  0.0422  -0.0054 75  LEU B CD2 
2259 N N   . TYR B 74  ? 0.1768 0.1509 0.1936 0.0179  0.0418  0.0011  76  TYR B N   
2260 C CA  . TYR B 74  ? 0.1720 0.1509 0.1965 0.0221  0.0372  0.0042  76  TYR B CA  
2261 C C   . TYR B 74  ? 0.2052 0.1819 0.2398 0.0258  0.0398  0.0050  76  TYR B C   
2262 O O   . TYR B 74  ? 0.2164 0.1985 0.2611 0.0286  0.0386  0.0055  76  TYR B O   
2263 C CB  . TYR B 74  ? 0.1763 0.1555 0.1951 0.0222  0.0325  0.0069  76  TYR B CB  
2264 C CG  . TYR B 74  ? 0.1671 0.1517 0.1915 0.0253  0.0270  0.0101  76  TYR B CG  
2265 C CD1 . TYR B 74  ? 0.1814 0.1725 0.2051 0.0244  0.0230  0.0102  76  TYR B CD1 
2266 C CD2 . TYR B 74  ? 0.1799 0.1627 0.2103 0.0290  0.0257  0.0131  76  TYR B CD2 
2267 C CE1 . TYR B 74  ? 0.2030 0.1992 0.2312 0.0264  0.0180  0.0129  76  TYR B CE1 
2268 C CE2 . TYR B 74  ? 0.1870 0.1751 0.2218 0.0314  0.0199  0.0164  76  TYR B CE2 
2269 C CZ  . TYR B 74  ? 0.2120 0.2071 0.2457 0.0298  0.0162  0.0160  76  TYR B CZ  
2270 O OH  . TYR B 74  ? 0.2356 0.2362 0.2732 0.0314  0.0107  0.0189  76  TYR B OH  
2271 N N   . ASN B 75  ? 0.2127 0.1815 0.2449 0.0258  0.0438  0.0049  77  ASN B N   
2272 C CA  . ASN B 75  ? 0.2155 0.1806 0.2575 0.0299  0.0470  0.0057  77  ASN B CA  
2273 C C   . ASN B 75  ? 0.2409 0.2079 0.2924 0.0304  0.0520  0.0024  77  ASN B C   
2274 O O   . ASN B 75  ? 0.2652 0.2351 0.3294 0.0350  0.0518  0.0035  77  ASN B O   
2275 C CB  . ASN B 75  ? 0.2235 0.1780 0.2596 0.0290  0.0516  0.0055  77  ASN B CB  
2276 C CG  . ASN B 75  ? 0.2963 0.2479 0.3240 0.0287  0.0474  0.0087  77  ASN B CG  
2277 O OD1 . ASN B 75  ? 0.2688 0.2256 0.2970 0.0304  0.0410  0.0118  77  ASN B OD1 
2278 N ND2 . ASN B 75  ? 0.3449 0.2876 0.3637 0.0257  0.0516  0.0075  77  ASN B ND2 
2279 N N   . HIS B 76  ? 0.2304 0.1957 0.2761 0.0256  0.0563  -0.0015 78  HIS B N   
2280 C CA  . HIS B 76  ? 0.2528 0.2188 0.3046 0.0244  0.0618  -0.0053 78  HIS B CA  
2281 C C   . HIS B 76  ? 0.2602 0.2356 0.3195 0.0257  0.0582  -0.0052 78  HIS B C   
2282 O O   . HIS B 76  ? 0.2800 0.2586 0.3513 0.0278  0.0611  -0.0069 78  HIS B O   
2283 C CB  . HIS B 76  ? 0.2932 0.2538 0.3330 0.0179  0.0664  -0.0091 78  HIS B CB  
2284 C CG  . HIS B 76  ? 0.3887 0.3494 0.4313 0.0151  0.0718  -0.0132 78  HIS B CG  
2285 N ND1 . HIS B 76  ? 0.4375 0.4021 0.4751 0.0121  0.0696  -0.0142 78  HIS B ND1 
2286 C CD2 . HIS B 76  ? 0.4246 0.3814 0.4740 0.0147  0.0796  -0.0166 78  HIS B CD2 
2287 C CE1 . HIS B 76  ? 0.4451 0.4076 0.4855 0.0095  0.0759  -0.0181 78  HIS B CE1 
2288 N NE2 . HIS B 76  ? 0.4468 0.4051 0.4950 0.0110  0.0822  -0.0199 78  HIS B NE2 
2289 N N   . ILE B 77  ? 0.2320 0.2120 0.2847 0.0242  0.0524  -0.0038 79  ILE B N   
2290 C CA  . ILE B 77  ? 0.2485 0.2372 0.3073 0.0250  0.0490  -0.0037 79  ILE B CA  
2291 C C   . ILE B 77  ? 0.2552 0.2501 0.3269 0.0303  0.0451  -0.0008 79  ILE B C   
2292 O O   . ILE B 77  ? 0.2658 0.2674 0.3483 0.0317  0.0453  -0.0019 79  ILE B O   
2293 C CB  . ILE B 77  ? 0.2514 0.2427 0.3000 0.0226  0.0436  -0.0024 79  ILE B CB  
2294 C CG1 . ILE B 77  ? 0.2808 0.2671 0.3177 0.0177  0.0466  -0.0051 79  ILE B CG1 
2295 C CG2 . ILE B 77  ? 0.2669 0.2667 0.3213 0.0237  0.0392  -0.0016 79  ILE B CG2 
2296 C CD1 . ILE B 77  ? 0.3170 0.3021 0.3547 0.0149  0.0515  -0.0087 79  ILE B CD1 
2297 N N   . GLN B 78  ? 0.2859 0.2787 0.3560 0.0331  0.0414  0.0030  80  GLN B N   
2298 C CA  . GLN B 78  ? 0.3313 0.3289 0.4121 0.0384  0.0368  0.0067  80  GLN B CA  
2299 C C   . GLN B 78  ? 0.3949 0.3935 0.4909 0.0421  0.0415  0.0052  80  GLN B C   
2300 O O   . GLN B 78  ? 0.3887 0.3950 0.4971 0.0461  0.0379  0.0070  80  GLN B O   
2301 C CB  . GLN B 78  ? 0.3471 0.3389 0.4209 0.0399  0.0336  0.0107  80  GLN B CB  
2302 C CG  . GLN B 78  ? 0.3801 0.3761 0.4597 0.0444  0.0265  0.0158  80  GLN B CG  
2303 C CD  . GLN B 78  ? 0.3990 0.3865 0.4690 0.0448  0.0247  0.0192  80  GLN B CD  
2304 O OE1 . GLN B 78  ? 0.4489 0.4274 0.5121 0.0432  0.0297  0.0178  80  GLN B OE1 
2305 N NE2 . GLN B 78  ? 0.3875 0.3774 0.4559 0.0464  0.0177  0.0235  80  GLN B NE2 
2306 N N   . LEU B 79  ? 0.4549 0.4462 0.5500 0.0404  0.0496  0.0015  81  LEU B N   
2307 C CA  . LEU B 79  ? 0.5054 0.4959 0.6139 0.0432  0.0560  -0.0010 81  LEU B CA  
2308 C C   . LEU B 79  ? 0.5329 0.5283 0.6471 0.0400  0.0608  -0.0062 81  LEU B C   
2309 O O   . LEU B 79  ? 0.5368 0.5378 0.6667 0.0432  0.0631  -0.0078 81  LEU B O   
2310 C CB  . LEU B 79  ? 0.5293 0.5071 0.6305 0.0417  0.0630  -0.0026 81  LEU B CB  
2311 C CG  . LEU B 79  ? 0.5608 0.5330 0.6726 0.0465  0.0679  -0.0024 81  LEU B CG  
2312 C CD1 . LEU B 79  ? 0.5637 0.5398 0.6849 0.0538  0.0609  0.0033  81  LEU B CD1 
2313 C CD2 . LEU B 79  ? 0.5876 0.5467 0.6869 0.0434  0.0735  -0.0035 81  LEU B CD2 
2314 N N   . SER B 80  ? 0.5517 0.5446 0.6533 0.0339  0.0626  -0.0089 82  SER B N   
2315 C CA  . SER B 80  ? 0.5737 0.5679 0.6761 0.0294  0.0680  -0.0140 82  SER B CA  
2316 C C   . SER B 80  ? 0.5793 0.5766 0.6713 0.0255  0.0636  -0.0137 82  SER B C   
2317 O O   . SER B 80  ? 0.6048 0.5956 0.6818 0.0214  0.0640  -0.0140 82  SER B O   
2318 C CB  . SER B 80  ? 0.6345 0.6181 0.7292 0.0251  0.0767  -0.0180 82  SER B CB  
2319 O OG  . SER B 80  ? 0.7057 0.6818 0.7847 0.0225  0.0753  -0.0163 82  SER B OG  
2320 N N   . SER B 81  ? 0.5487 0.5559 0.6486 0.0268  0.0593  -0.0130 83  SER B N   
2321 C CA  . SER B 81  ? 0.5337 0.5438 0.6258 0.0230  0.0565  -0.0136 83  SER B CA  
2322 C C   . SER B 81  ? 0.5130 0.5347 0.6169 0.0247  0.0526  -0.0134 83  SER B C   
2323 O O   . SER B 81  ? 0.5224 0.5504 0.6382 0.0295  0.0491  -0.0109 83  SER B O   
2324 C CB  . SER B 81  ? 0.5672 0.5746 0.6459 0.0225  0.0505  -0.0100 83  SER B CB  
2325 O OG  . SER B 81  ? 0.5943 0.6063 0.6787 0.0271  0.0444  -0.0058 83  SER B OG  
2326 N N   . ASN B 82  ? 0.4911 0.5152 0.5910 0.0206  0.0529  -0.0156 84  ASN B N   
2327 C CA  . ASN B 82  ? 0.4728 0.5077 0.5834 0.0208  0.0505  -0.0165 84  ASN B CA  
2328 C C   . ASN B 82  ? 0.4343 0.4739 0.5402 0.0214  0.0423  -0.0126 84  ASN B C   
2329 O O   . ASN B 82  ? 0.4379 0.4721 0.5297 0.0189  0.0406  -0.0116 84  ASN B O   
2330 C CB  . ASN B 82  ? 0.5158 0.5496 0.6238 0.0152  0.0564  -0.0217 84  ASN B CB  
2331 C CG  . ASN B 82  ? 0.5922 0.6376 0.7141 0.0148  0.0563  -0.0241 84  ASN B CG  
2332 O OD1 . ASN B 82  ? 0.6254 0.6737 0.7428 0.0115  0.0545  -0.0249 84  ASN B OD1 
2333 N ND2 . ASN B 82  ? 0.6134 0.6658 0.7528 0.0182  0.0584  -0.0255 84  ASN B ND2 
2334 N N   . LEU B 83  ? 0.3878 0.4376 0.5056 0.0247  0.0371  -0.0105 85  LEU B N   
2335 C CA  . LEU B 83  ? 0.3594 0.4144 0.4736 0.0246  0.0296  -0.0073 85  LEU B CA  
2336 C C   . LEU B 83  ? 0.3301 0.3963 0.4552 0.0229  0.0291  -0.0098 85  LEU B C   
2337 O O   . LEU B 83  ? 0.3424 0.4185 0.4811 0.0262  0.0252  -0.0082 85  LEU B O   
2338 C CB  . LEU B 83  ? 0.3574 0.4142 0.4746 0.0296  0.0231  -0.0019 85  LEU B CB  
2339 C CG  . LEU B 83  ? 0.3906 0.4523 0.5029 0.0288  0.0153  0.0015  85  LEU B CG  
2340 C CD1 . LEU B 83  ? 0.4073 0.4611 0.5032 0.0259  0.0148  0.0022  85  LEU B CD1 
2341 C CD2 . LEU B 83  ? 0.4082 0.4736 0.5267 0.0335  0.0089  0.0065  85  LEU B CD2 
2342 N N   . MET B 84  ? 0.2987 0.3634 0.4177 0.0176  0.0329  -0.0136 86  MET B N   
2343 C CA  . MET B 84  ? 0.2702 0.3452 0.3983 0.0147  0.0331  -0.0168 86  MET B CA  
2344 C C   . MET B 84  ? 0.2600 0.3324 0.3750 0.0096  0.0320  -0.0175 86  MET B C   
2345 O O   . MET B 84  ? 0.2481 0.3095 0.3482 0.0082  0.0334  -0.0168 86  MET B O   
2346 C CB  . MET B 84  ? 0.2725 0.3474 0.4079 0.0126  0.0414  -0.0223 86  MET B CB  
2347 C CG  . MET B 84  ? 0.2917 0.3711 0.4432 0.0175  0.0432  -0.0225 86  MET B CG  
2348 S SD  . MET B 84  ? 0.2864 0.3848 0.4607 0.0210  0.0378  -0.0221 86  MET B SD  
2349 C CE  . MET B 84  ? 0.2497 0.3543 0.4299 0.0146  0.0444  -0.0293 86  MET B CE  
2350 N N   . PRO B 85  ? 0.2488 0.3308 0.3691 0.0067  0.0300  -0.0191 87  PRO B N   
2351 C CA  . PRO B 85  ? 0.2464 0.3246 0.3538 0.0015  0.0299  -0.0202 87  PRO B CA  
2352 C C   . PRO B 85  ? 0.2611 0.3279 0.3579 -0.0023 0.0374  -0.0238 87  PRO B C   
2353 O O   . PRO B 85  ? 0.2567 0.3232 0.3594 -0.0035 0.0434  -0.0275 87  PRO B O   
2354 C CB  . PRO B 85  ? 0.2630 0.3542 0.3803 -0.0016 0.0280  -0.0225 87  PRO B CB  
2355 C CG  . PRO B 85  ? 0.2623 0.3654 0.3970 0.0031  0.0239  -0.0207 87  PRO B CG  
2356 C CD  . PRO B 85  ? 0.2442 0.3410 0.3826 0.0075  0.0281  -0.0205 87  PRO B CD  
2357 N N   . GLY B 86  ? 0.2575 0.3149 0.3387 -0.0042 0.0369  -0.0226 88  GLY B N   
2358 C CA  . GLY B 86  ? 0.2764 0.3213 0.3446 -0.0074 0.0425  -0.0247 88  GLY B CA  
2359 C C   . GLY B 86  ? 0.2815 0.3165 0.3416 -0.0044 0.0431  -0.0224 88  GLY B C   
2360 O O   . GLY B 86  ? 0.3056 0.3298 0.3532 -0.0067 0.0465  -0.0232 88  GLY B O   
2361 N N   . CYS B 87  ? 0.2472 0.2854 0.3136 0.0003  0.0399  -0.0194 89  CYS B N   
2362 C CA  . CYS B 87  ? 0.2471 0.2764 0.3055 0.0025  0.0405  -0.0174 89  CYS B CA  
2363 C C   . CYS B 87  ? 0.2339 0.2589 0.2808 0.0033  0.0359  -0.0141 89  CYS B C   
2364 O O   . CYS B 87  ? 0.2098 0.2402 0.2583 0.0041  0.0311  -0.0122 89  CYS B O   
2365 C CB  . CYS B 87  ? 0.2725 0.3053 0.3408 0.0068  0.0395  -0.0158 89  CYS B CB  
2366 S SG  . CYS B 87  ? 0.4021 0.4387 0.4845 0.0065  0.0461  -0.0200 89  CYS B SG  
2367 N N   . ASP B 88  ? 0.2313 0.2465 0.2666 0.0028  0.0375  -0.0137 90  ASP B N   
2368 C CA  . ASP B 88  ? 0.2120 0.2237 0.2383 0.0044  0.0335  -0.0108 90  ASP B CA  
2369 C C   . ASP B 88  ? 0.2033 0.2104 0.2265 0.0064  0.0339  -0.0094 90  ASP B C   
2370 O O   . ASP B 88  ? 0.2034 0.2051 0.2238 0.0048  0.0382  -0.0111 90  ASP B O   
2371 C CB  . ASP B 88  ? 0.2541 0.2584 0.2687 0.0021  0.0345  -0.0113 90  ASP B CB  
2372 C CG  . ASP B 88  ? 0.3612 0.3674 0.3759 -0.0008 0.0352  -0.0131 90  ASP B CG  
2373 O OD1 . ASP B 88  ? 0.3149 0.3299 0.3378 -0.0008 0.0327  -0.0131 90  ASP B OD1 
2374 O OD2 . ASP B 88  ? 0.4273 0.4258 0.4331 -0.0034 0.0380  -0.0145 90  ASP B OD2 
2375 N N   . TYR B 89  ? 0.1726 0.1812 0.1952 0.0091  0.0298  -0.0065 91  TYR B N   
2376 C CA  . TYR B 89  ? 0.1472 0.1512 0.1651 0.0103  0.0300  -0.0055 91  TYR B CA  
2377 C C   . TYR B 89  ? 0.1253 0.1271 0.1345 0.0108  0.0267  -0.0037 91  TYR B C   
2378 O O   . TYR B 89  ? 0.1313 0.1368 0.1412 0.0114  0.0234  -0.0026 91  TYR B O   
2379 C CB  . TYR B 89  ? 0.1558 0.1632 0.1811 0.0129  0.0290  -0.0040 91  TYR B CB  
2380 C CG  . TYR B 89  ? 0.1975 0.2063 0.2322 0.0131  0.0330  -0.0058 91  TYR B CG  
2381 C CD1 . TYR B 89  ? 0.2039 0.2200 0.2494 0.0139  0.0322  -0.0062 91  TYR B CD1 
2382 C CD2 . TYR B 89  ? 0.2259 0.2293 0.2591 0.0124  0.0375  -0.0072 91  TYR B CD2 
2383 C CE1 . TYR B 89  ? 0.2302 0.2487 0.2864 0.0148  0.0359  -0.0080 91  TYR B CE1 
2384 C CE2 . TYR B 89  ? 0.2397 0.2442 0.2824 0.0128  0.0417  -0.0092 91  TYR B CE2 
2385 C CZ  . TYR B 89  ? 0.2645 0.2768 0.3193 0.0143  0.0409  -0.0096 91  TYR B CZ  
2386 O OH  . TYR B 89  ? 0.3233 0.3372 0.3889 0.0150  0.0456  -0.0119 91  TYR B OH  
2387 N N   . SER B 90  ? 0.1228 0.1192 0.1243 0.0103  0.0275  -0.0037 92  SER B N   
2388 C CA  . SER B 90  ? 0.1186 0.1135 0.1129 0.0111  0.0245  -0.0024 92  SER B CA  
2389 C C   . SER B 90  ? 0.1404 0.1337 0.1313 0.0115  0.0240  -0.0017 92  SER B C   
2390 O O   . SER B 90  ? 0.1643 0.1537 0.1528 0.0100  0.0268  -0.0026 92  SER B O   
2391 C CB  . SER B 90  ? 0.1667 0.1560 0.1534 0.0097  0.0255  -0.0030 92  SER B CB  
2392 O OG  . SER B 90  ? 0.2054 0.1951 0.1941 0.0085  0.0268  -0.0042 92  SER B OG  
2393 N N   . LEU B 91  ? 0.1164 0.1127 0.1068 0.0129  0.0208  -0.0004 93  LEU B N   
2394 C CA  . LEU B 91  ? 0.1124 0.1077 0.0990 0.0127  0.0203  -0.0001 93  LEU B CA  
2395 C C   . LEU B 91  ? 0.1231 0.1185 0.1045 0.0134  0.0177  0.0003  93  LEU B C   
2396 O O   . LEU B 91  ? 0.1127 0.1114 0.0958 0.0147  0.0154  0.0008  93  LEU B O   
2397 C CB  . LEU B 91  ? 0.1281 0.1267 0.1183 0.0135  0.0192  0.0007  93  LEU B CB  
2398 C CG  . LEU B 91  ? 0.1268 0.1241 0.1130 0.0124  0.0196  0.0004  93  LEU B CG  
2399 C CD1 . LEU B 91  ? 0.1341 0.1270 0.1193 0.0107  0.0234  -0.0007 93  LEU B CD1 
2400 C CD2 . LEU B 91  ? 0.1415 0.1414 0.1293 0.0128  0.0181  0.0011  93  LEU B CD2 
2401 N N   . PHE B 92  ? 0.1360 0.1279 0.1112 0.0126  0.0178  0.0002  94  PHE B N   
2402 C CA  . PHE B 92  ? 0.1436 0.1356 0.1145 0.0139  0.0149  0.0009  94  PHE B CA  
2403 C C   . PHE B 92  ? 0.1375 0.1304 0.1048 0.0131  0.0137  0.0009  94  PHE B C   
2404 O O   . PHE B 92  ? 0.1377 0.1283 0.1026 0.0106  0.0157  0.0002  94  PHE B O   
2405 C CB  . PHE B 92  ? 0.1519 0.1379 0.1175 0.0139  0.0154  0.0012  94  PHE B CB  
2406 C CG  . PHE B 92  ? 0.1440 0.1303 0.1125 0.0151  0.0156  0.0011  94  PHE B CG  
2407 C CD1 . PHE B 92  ? 0.1553 0.1432 0.1290 0.0140  0.0177  0.0003  94  PHE B CD1 
2408 C CD2 . PHE B 92  ? 0.1351 0.1201 0.1012 0.0172  0.0138  0.0018  94  PHE B CD2 
2409 C CE1 . PHE B 92  ? 0.1811 0.1699 0.1570 0.0143  0.0177  0.0000  94  PHE B CE1 
2410 C CE2 . PHE B 92  ? 0.1489 0.1335 0.1169 0.0176  0.0145  0.0014  94  PHE B CE2 
2411 C CZ  . PHE B 92  ? 0.1584 0.1450 0.1309 0.0157  0.0165  0.0004  94  PHE B CZ  
2412 N N   . LYS B 93  ? 0.1245 0.1213 0.0916 0.0148  0.0105  0.0013  95  LYS B N   
2413 C CA  . LYS B 93  ? 0.1218 0.1208 0.0857 0.0140  0.0085  0.0012  95  LYS B CA  
2414 C C   . LYS B 93  ? 0.1477 0.1409 0.1040 0.0122  0.0086  0.0019  95  LYS B C   
2415 O O   . LYS B 93  ? 0.1637 0.1514 0.1166 0.0131  0.0089  0.0028  95  LYS B O   
2416 C CB  . LYS B 93  ? 0.1235 0.1278 0.0895 0.0168  0.0049  0.0016  95  LYS B CB  
2417 C CG  . LYS B 93  ? 0.1299 0.1402 0.1022 0.0174  0.0050  0.0004  95  LYS B CG  
2418 C CD  . LYS B 93  ? 0.1452 0.1613 0.1206 0.0199  0.0022  0.0000  95  LYS B CD  
2419 C CE  . LYS B 93  ? 0.1380 0.1594 0.1186 0.0195  0.0031  -0.0017 95  LYS B CE  
2420 N NZ  . LYS B 93  ? 0.1190 0.1453 0.1038 0.0223  0.0014  -0.0025 95  LYS B NZ  
2421 N N   . ASP B 94  ? 0.1467 0.1401 0.0993 0.0093  0.0089  0.0013  96  ASP B N   
2422 C CA  . ASP B 94  ? 0.1728 0.1599 0.1164 0.0065  0.0092  0.0018  96  ASP B CA  
2423 C C   . ASP B 94  ? 0.2049 0.1906 0.1440 0.0090  0.0049  0.0039  96  ASP B C   
2424 O O   . ASP B 94  ? 0.2087 0.2007 0.1510 0.0118  0.0009  0.0046  96  ASP B O   
2425 C CB  . ASP B 94  ? 0.1979 0.1862 0.1375 0.0025  0.0096  0.0006  96  ASP B CB  
2426 C CG  . ASP B 94  ? 0.2820 0.2620 0.2118 -0.0017 0.0118  0.0005  96  ASP B CG  
2427 O OD1 . ASP B 94  ? 0.3207 0.2943 0.2494 -0.0023 0.0153  0.0002  96  ASP B OD1 
2428 O OD2 . ASP B 94  ? 0.3438 0.3241 0.2672 -0.0046 0.0100  0.0005  96  ASP B OD2 
2429 N N   . GLY B 95  ? 0.2186 0.1957 0.1507 0.0080  0.0060  0.0049  97  GLY B N   
2430 C CA  . GLY B 95  ? 0.2290 0.2024 0.1557 0.0106  0.0023  0.0074  97  GLY B CA  
2431 C C   . GLY B 95  ? 0.2450 0.2161 0.1750 0.0144  0.0026  0.0081  97  GLY B C   
2432 O O   . GLY B 95  ? 0.2804 0.2463 0.2051 0.0166  0.0002  0.0103  97  GLY B O   
2433 N N   . ILE B 96  ? 0.2166 0.1910 0.1547 0.0150  0.0055  0.0065  98  ILE B N   
2434 C CA  . ILE B 96  ? 0.2008 0.1725 0.1412 0.0174  0.0067  0.0066  98  ILE B CA  
2435 C C   . ILE B 96  ? 0.2334 0.2001 0.1730 0.0143  0.0115  0.0052  98  ILE B C   
2436 O O   . ILE B 96  ? 0.2229 0.1935 0.1681 0.0125  0.0140  0.0035  98  ILE B O   
2437 C CB  . ILE B 96  ? 0.1688 0.1485 0.1189 0.0202  0.0059  0.0058  98  ILE B CB  
2438 C CG1 . ILE B 96  ? 0.2016 0.1884 0.1548 0.0229  0.0018  0.0063  98  ILE B CG1 
2439 C CG2 . ILE B 96  ? 0.1576 0.1333 0.1084 0.0220  0.0073  0.0058  98  ILE B CG2 
2440 C CD1 . ILE B 96  ? 0.2030 0.1968 0.1645 0.0249  0.0017  0.0050  98  ILE B CD1 
2441 N N   . GLU B 97  ? 0.2609 0.2188 0.1936 0.0134  0.0130  0.0057  99  GLU B N   
2442 C CA  . GLU B 97  ? 0.2840 0.2379 0.2167 0.0102  0.0179  0.0038  99  GLU B CA  
2443 C C   . GLU B 97  ? 0.2685 0.2268 0.2095 0.0117  0.0191  0.0027  99  GLU B C   
2444 O O   . GLU B 97  ? 0.2659 0.2258 0.2086 0.0148  0.0168  0.0036  99  GLU B O   
2445 C CB  . GLU B 97  ? 0.3211 0.2636 0.2428 0.0079  0.0197  0.0044  99  GLU B CB  
2446 C CG  . GLU B 97  ? 0.4144 0.3518 0.3262 0.0056  0.0183  0.0057  99  GLU B CG  
2447 C CD  . GLU B 97  ? 0.5462 0.4711 0.4462 0.0020  0.0213  0.0058  99  GLU B CD  
2448 O OE1 . GLU B 97  ? 0.5995 0.5172 0.4897 0.0033  0.0180  0.0087  99  GLU B OE1 
2449 O OE2 . GLU B 97  ? 0.6058 0.5282 0.5067 -0.0019 0.0268  0.0029  99  GLU B OE2 
2450 N N   . PRO B 98  ? 0.2596 0.2202 0.2061 0.0093  0.0226  0.0006  100 PRO B N   
2451 C CA  . PRO B 98  ? 0.2524 0.2181 0.2066 0.0102  0.0232  -0.0003 100 PRO B CA  
2452 C C   . PRO B 98  ? 0.2636 0.2242 0.2151 0.0092  0.0252  -0.0011 100 PRO B C   
2453 O O   . PRO B 98  ? 0.2740 0.2364 0.2298 0.0071  0.0280  -0.0029 100 PRO B O   
2454 C CB  . PRO B 98  ? 0.2781 0.2484 0.2395 0.0082  0.0257  -0.0020 100 PRO B CB  
2455 C CG  . PRO B 98  ? 0.2910 0.2549 0.2467 0.0052  0.0289  -0.0030 100 PRO B CG  
2456 C CD  . PRO B 98  ? 0.2748 0.2338 0.2213 0.0057  0.0264  -0.0011 100 PRO B CD  
2457 N N   . MET B 99  ? 0.2476 0.2019 0.1918 0.0109  0.0237  0.0005  101 MET B N   
2458 C CA  . MET B 99  ? 0.2314 0.1783 0.1705 0.0098  0.0261  0.0000  101 MET B CA  
2459 C C   . MET B 99  ? 0.2261 0.1703 0.1625 0.0138  0.0234  0.0018  101 MET B C   
2460 O O   . MET B 99  ? 0.2297 0.1750 0.1652 0.0171  0.0197  0.0038  101 MET B O   
2461 C CB  . MET B 99  ? 0.2631 0.1997 0.1923 0.0065  0.0290  -0.0002 101 MET B CB  
2462 C CG  . MET B 99  ? 0.3200 0.2516 0.2411 0.0078  0.0261  0.0023  101 MET B CG  
2463 S SD  . MET B 99  ? 0.5376 0.4572 0.4467 0.0021  0.0305  0.0014  101 MET B SD  
2464 C CE  . MET B 99  ? 0.5360 0.4645 0.4543 -0.0011 0.0334  -0.0016 101 MET B CE  
2465 N N   . TRP B 100 ? 0.2447 0.1858 0.1805 0.0133  0.0254  0.0008  102 TRP B N   
2466 C CA  . TRP B 100 ? 0.2794 0.2166 0.2130 0.0169  0.0242  0.0020  102 TRP B CA  
2467 C C   . TRP B 100 ? 0.3130 0.2415 0.2381 0.0200  0.0219  0.0049  102 TRP B C   
2468 O O   . TRP B 100 ? 0.3084 0.2382 0.2353 0.0247  0.0188  0.0066  102 TRP B O   
2469 C CB  . TRP B 100 ? 0.2996 0.2322 0.2316 0.0144  0.0281  0.0000  102 TRP B CB  
2470 C CG  . TRP B 100 ? 0.3478 0.2758 0.2780 0.0176  0.0281  0.0005  102 TRP B CG  
2471 C CD1 . TRP B 100 ? 0.3790 0.3108 0.3132 0.0224  0.0249  0.0018  102 TRP B CD1 
2472 C CD2 . TRP B 100 ? 0.3683 0.2876 0.2933 0.0158  0.0320  -0.0009 102 TRP B CD2 
2473 N NE1 . TRP B 100 ? 0.3880 0.3132 0.3197 0.0243  0.0267  0.0016  102 TRP B NE1 
2474 C CE2 . TRP B 100 ? 0.3846 0.3015 0.3102 0.0203  0.0311  0.0000  102 TRP B CE2 
2475 C CE3 . TRP B 100 ? 0.3936 0.3060 0.3130 0.0108  0.0367  -0.0029 102 TRP B CE3 
2476 C CZ2 . TRP B 100 ? 0.3920 0.2995 0.3126 0.0198  0.0349  -0.0011 102 TRP B CZ2 
2477 C CZ3 . TRP B 100 ? 0.4020 0.3055 0.3161 0.0099  0.0402  -0.0040 102 TRP B CZ3 
2478 C CH2 . TRP B 100 ? 0.4024 0.3030 0.3168 0.0145  0.0394  -0.0030 102 TRP B CH2 
2479 N N   . GLU B 101 ? 0.3261 0.2459 0.2422 0.0174  0.0233  0.0056  103 GLU B N   
2480 C CA  . GLU B 101 ? 0.3174 0.2272 0.2233 0.0200  0.0207  0.0089  103 GLU B CA  
2481 C C   . GLU B 101 ? 0.3135 0.2288 0.2210 0.0230  0.0155  0.0113  103 GLU B C   
2482 O O   . GLU B 101 ? 0.3083 0.2178 0.2095 0.0264  0.0120  0.0145  103 GLU B O   
2483 C CB  . GLU B 101 ? 0.3716 0.2700 0.2658 0.0152  0.0238  0.0089  103 GLU B CB  
2484 C CG  . GLU B 101 ? 0.4948 0.3851 0.3846 0.0115  0.0294  0.0067  103 GLU B CG  
2485 C CD  . GLU B 101 ? 0.5951 0.4777 0.4762 0.0054  0.0334  0.0053  103 GLU B CD  
2486 O OE1 . GLU B 101 ? 0.6047 0.4822 0.4777 0.0049  0.0313  0.0075  103 GLU B OE1 
2487 O OE2 . GLU B 101 ? 0.6016 0.4842 0.4845 0.0008  0.0386  0.0018  103 GLU B OE2 
2488 N N   . ASP B 102 ? 0.2890 0.2160 0.2047 0.0219  0.0145  0.0099  104 ASP B N   
2489 C CA  . ASP B 102 ? 0.2778 0.2111 0.1954 0.0245  0.0095  0.0117  104 ASP B CA  
2490 C C   . ASP B 102 ? 0.2518 0.1879 0.1736 0.0304  0.0059  0.0133  104 ASP B C   
2491 O O   . ASP B 102 ? 0.2315 0.1701 0.1595 0.0319  0.0077  0.0118  104 ASP B O   
2492 C CB  . ASP B 102 ? 0.2509 0.1958 0.1776 0.0227  0.0098  0.0096  104 ASP B CB  
2493 C CG  . ASP B 102 ? 0.2809 0.2315 0.2080 0.0234  0.0058  0.0108  104 ASP B CG  
2494 O OD1 . ASP B 102 ? 0.2411 0.1981 0.1733 0.0274  0.0020  0.0116  104 ASP B OD1 
2495 O OD2 . ASP B 102 ? 0.2986 0.2475 0.2211 0.0197  0.0066  0.0105  104 ASP B OD2 
2496 N N   . GLU B 103 ? 0.2680 0.2040 0.1869 0.0336  0.0010  0.0161  105 GLU B N   
2497 C CA  . GLU B 103 ? 0.2899 0.2295 0.2143 0.0398  -0.0027 0.0176  105 GLU B CA  
2498 C C   . GLU B 103 ? 0.2740 0.2261 0.2112 0.0409  -0.0020 0.0147  105 GLU B C   
2499 O O   . GLU B 103 ? 0.2614 0.2145 0.2039 0.0448  -0.0018 0.0143  105 GLU B O   
2500 C CB  . GLU B 103 ? 0.3477 0.2898 0.2695 0.0422  -0.0088 0.0206  105 GLU B CB  
2501 C CG  . GLU B 103 ? 0.5414 0.4848 0.4674 0.0493  -0.0130 0.0228  105 GLU B CG  
2502 C CD  . GLU B 103 ? 0.6534 0.5821 0.5701 0.0524  -0.0132 0.0260  105 GLU B CD  
2503 O OE1 . GLU B 103 ? 0.7277 0.6565 0.6474 0.0589  -0.0172 0.0285  105 GLU B OE1 
2504 O OE2 . GLU B 103 ? 0.6664 0.5834 0.5732 0.0485  -0.0092 0.0260  105 GLU B OE2 
2505 N N   . LYS B 104 ? 0.2479 0.2085 0.1895 0.0372  -0.0013 0.0127  106 LYS B N   
2506 C CA  . LYS B 104 ? 0.2160 0.1872 0.1679 0.0375  -0.0007 0.0102  106 LYS B CA  
2507 C C   . LYS B 104 ? 0.2143 0.1846 0.1692 0.0356  0.0037  0.0079  106 LYS B C   
2508 O O   . LYS B 104 ? 0.2040 0.1817 0.1663 0.0360  0.0043  0.0060  106 LYS B O   
2509 C CB  . LYS B 104 ? 0.2185 0.1980 0.1732 0.0345  -0.0017 0.0092  106 LYS B CB  
2510 C CG  . LYS B 104 ? 0.3044 0.2876 0.2576 0.0359  -0.0065 0.0109  106 LYS B CG  
2511 C CD  . LYS B 104 ? 0.4295 0.4201 0.3902 0.0408  -0.0096 0.0109  106 LYS B CD  
2512 C CE  . LYS B 104 ? 0.5270 0.5249 0.4888 0.0417  -0.0145 0.0118  106 LYS B CE  
2513 N NZ  . LYS B 104 ? 0.6001 0.6021 0.5681 0.0477  -0.0180 0.0127  106 LYS B NZ  
2514 N N   . ASN B 105 ? 0.1968 0.1586 0.1458 0.0330  0.0070  0.0078  107 ASN B N   
2515 C CA  . ASN B 105 ? 0.1939 0.1549 0.1451 0.0308  0.0108  0.0056  107 ASN B CA  
2516 C C   . ASN B 105 ? 0.2192 0.1713 0.1665 0.0323  0.0131  0.0057  107 ASN B C   
2517 O O   . ASN B 105 ? 0.2167 0.1695 0.1667 0.0306  0.0160  0.0036  107 ASN B O   
2518 C CB  . ASN B 105 ? 0.1821 0.1417 0.1313 0.0260  0.0135  0.0046  107 ASN B CB  
2519 C CG  . ASN B 105 ? 0.1646 0.1319 0.1180 0.0243  0.0125  0.0042  107 ASN B CG  
2520 O OD1 . ASN B 105 ? 0.1604 0.1359 0.1202 0.0252  0.0110  0.0035  107 ASN B OD1 
2521 N ND2 . ASN B 105 ? 0.1872 0.1518 0.1371 0.0214  0.0138  0.0042  107 ASN B ND2 
2522 N N   . LYS B 106 ? 0.2418 0.1852 0.1824 0.0351  0.0118  0.0081  108 LYS B N   
2523 C CA  . LYS B 106 ? 0.2543 0.1866 0.1894 0.0360  0.0147  0.0082  108 LYS B CA  
2524 C C   . LYS B 106 ? 0.2430 0.1777 0.1842 0.0383  0.0163  0.0065  108 LYS B C   
2525 O O   . LYS B 106 ? 0.2502 0.1786 0.1886 0.0361  0.0206  0.0048  108 LYS B O   
2526 C CB  . LYS B 106 ? 0.2869 0.2081 0.2128 0.0393  0.0126  0.0118  108 LYS B CB  
2527 C CG  . LYS B 106 ? 0.3958 0.3211 0.3246 0.0449  0.0070  0.0144  108 LYS B CG  
2528 C CD  . LYS B 106 ? 0.5311 0.4436 0.4482 0.0469  0.0047  0.0185  108 LYS B CD  
2529 C CE  . LYS B 106 ? 0.6119 0.5261 0.5319 0.0540  -0.0009 0.0216  108 LYS B CE  
2530 N NZ  . LYS B 106 ? 0.6638 0.5652 0.5716 0.0561  -0.0039 0.0261  108 LYS B NZ  
2531 N N   . ARG B 107 ? 0.2171 0.1605 0.1664 0.0421  0.0135  0.0064  109 ARG B N   
2532 C CA  . ARG B 107 ? 0.2025 0.1483 0.1579 0.0440  0.0156  0.0042  109 ARG B CA  
2533 C C   . ARG B 107 ? 0.2042 0.1602 0.1660 0.0397  0.0171  0.0011  109 ARG B C   
2534 O O   . ARG B 107 ? 0.2279 0.1877 0.1950 0.0402  0.0188  -0.0012 109 ARG B O   
2535 C CB  . ARG B 107 ? 0.2117 0.1611 0.1728 0.0506  0.0122  0.0055  109 ARG B CB  
2536 C CG  . ARG B 107 ? 0.2963 0.2347 0.2518 0.0559  0.0107  0.0088  109 ARG B CG  
2537 C CD  . ARG B 107 ? 0.2969 0.2398 0.2609 0.0630  0.0081  0.0094  109 ARG B CD  
2538 N NE  . ARG B 107 ? 0.3357 0.2836 0.3078 0.0627  0.0121  0.0054  109 ARG B NE  
2539 C CZ  . ARG B 107 ? 0.3730 0.3128 0.3443 0.0635  0.0170  0.0037  109 ARG B CZ  
2540 N NH1 . ARG B 107 ? 0.4071 0.3326 0.3697 0.0651  0.0186  0.0058  109 ARG B NH1 
2541 N NH2 . ARG B 107 ? 0.4022 0.3474 0.3804 0.0621  0.0208  -0.0003 109 ARG B NH2 
2542 N N   . GLY B 108 ? 0.1984 0.1582 0.1593 0.0355  0.0167  0.0009  110 GLY B N   
2543 C CA  . GLY B 108 ? 0.1838 0.1532 0.1504 0.0322  0.0168  -0.0010 110 GLY B CA  
2544 C C   . GLY B 108 ? 0.1623 0.1310 0.1281 0.0275  0.0201  -0.0031 110 GLY B C   
2545 O O   . GLY B 108 ? 0.1815 0.1428 0.1431 0.0264  0.0232  -0.0039 110 GLY B O   
2546 N N   . GLY B 109 ? 0.1509 0.1273 0.1204 0.0246  0.0192  -0.0038 111 GLY B N   
2547 C CA  . GLY B 109 ? 0.1425 0.1209 0.1124 0.0200  0.0210  -0.0055 111 GLY B CA  
2548 C C   . GLY B 109 ? 0.1474 0.1338 0.1211 0.0177  0.0189  -0.0052 111 GLY B C   
2549 O O   . GLY B 109 ? 0.1330 0.1227 0.1086 0.0195  0.0166  -0.0039 111 GLY B O   
2550 N N   . ARG B 110 ? 0.1564 0.1460 0.1311 0.0138  0.0195  -0.0063 112 ARG B N   
2551 C CA  . ARG B 110 ? 0.1491 0.1454 0.1273 0.0121  0.0171  -0.0054 112 ARG B CA  
2552 C C   . ARG B 110 ? 0.1582 0.1586 0.1372 0.0088  0.0168  -0.0064 112 ARG B C   
2553 O O   . ARG B 110 ? 0.1766 0.1748 0.1531 0.0062  0.0188  -0.0081 112 ARG B O   
2554 C CB  . ARG B 110 ? 0.1654 0.1615 0.1442 0.0107  0.0173  -0.0047 112 ARG B CB  
2555 C CG  . ARG B 110 ? 0.2092 0.2050 0.1873 0.0068  0.0189  -0.0061 112 ARG B CG  
2556 C CD  . ARG B 110 ? 0.3090 0.3046 0.2884 0.0055  0.0198  -0.0061 112 ARG B CD  
2557 N NE  . ARG B 110 ? 0.3241 0.3197 0.3026 0.0014  0.0216  -0.0080 112 ARG B NE  
2558 C CZ  . ARG B 110 ? 0.3405 0.3376 0.3212 -0.0011 0.0228  -0.0089 112 ARG B CZ  
2559 N NH1 . ARG B 110 ? 0.3301 0.3278 0.3098 -0.0054 0.0245  -0.0110 112 ARG B NH1 
2560 N NH2 . ARG B 110 ? 0.2977 0.2958 0.2816 0.0001  0.0228  -0.0082 112 ARG B NH2 
2561 N N   . TRP B 111 ? 0.1357 0.1413 0.1170 0.0084  0.0144  -0.0055 113 TRP B N   
2562 C CA  . TRP B 111 ? 0.1412 0.1506 0.1224 0.0048  0.0130  -0.0055 113 TRP B CA  
2563 C C   . TRP B 111 ? 0.1532 0.1654 0.1369 0.0034  0.0113  -0.0040 113 TRP B C   
2564 O O   . TRP B 111 ? 0.1498 0.1632 0.1365 0.0056  0.0101  -0.0025 113 TRP B O   
2565 C CB  . TRP B 111 ? 0.1370 0.1495 0.1189 0.0051  0.0114  -0.0049 113 TRP B CB  
2566 C CG  . TRP B 111 ? 0.1211 0.1326 0.1016 0.0053  0.0133  -0.0070 113 TRP B CG  
2567 C CD1 . TRP B 111 ? 0.1399 0.1515 0.1220 0.0086  0.0139  -0.0076 113 TRP B CD1 
2568 C CD2 . TRP B 111 ? 0.1272 0.1378 0.1047 0.0019  0.0152  -0.0092 113 TRP B CD2 
2569 N NE1 . TRP B 111 ? 0.1467 0.1580 0.1284 0.0080  0.0161  -0.0101 113 TRP B NE1 
2570 C CE2 . TRP B 111 ? 0.1467 0.1568 0.1251 0.0037  0.0174  -0.0113 113 TRP B CE2 
2571 C CE3 . TRP B 111 ? 0.1334 0.1440 0.1076 -0.0029 0.0153  -0.0098 113 TRP B CE3 
2572 C CZ2 . TRP B 111 ? 0.1538 0.1628 0.1302 0.0010  0.0203  -0.0142 113 TRP B CZ2 
2573 C CZ3 . TRP B 111 ? 0.1423 0.1512 0.1131 -0.0061 0.0180  -0.0125 113 TRP B CZ3 
2574 C CH2 . TRP B 111 ? 0.1366 0.1445 0.1087 -0.0042 0.0207  -0.0148 113 TRP B CH2 
2575 N N   . LEU B 112 ? 0.1543 0.1679 0.1372 -0.0002 0.0112  -0.0047 114 LEU B N   
2576 C CA  . LEU B 112 ? 0.1673 0.1847 0.1541 -0.0014 0.0096  -0.0037 114 LEU B CA  
2577 C C   . LEU B 112 ? 0.1837 0.2066 0.1716 -0.0041 0.0059  -0.0022 114 LEU B C   
2578 O O   . LEU B 112 ? 0.1867 0.2099 0.1703 -0.0076 0.0056  -0.0031 114 LEU B O   
2579 C CB  . LEU B 112 ? 0.1996 0.2149 0.1848 -0.0040 0.0123  -0.0059 114 LEU B CB  
2580 C CG  . LEU B 112 ? 0.2125 0.2328 0.2025 -0.0059 0.0112  -0.0058 114 LEU B CG  
2581 C CD1 . LEU B 112 ? 0.2316 0.2515 0.2259 -0.0027 0.0118  -0.0050 114 LEU B CD1 
2582 C CD2 . LEU B 112 ? 0.2332 0.2516 0.2203 -0.0099 0.0142  -0.0085 114 LEU B CD2 
2583 N N   . ILE B 113 ? 0.1903 0.2174 0.1839 -0.0025 0.0032  0.0000  115 ILE B N   
2584 C CA  . ILE B 113 ? 0.2203 0.2528 0.2162 -0.0041 -0.0011 0.0022  115 ILE B CA  
2585 C C   . ILE B 113 ? 0.2268 0.2644 0.2292 -0.0048 -0.0016 0.0018  115 ILE B C   
2586 O O   . ILE B 113 ? 0.1891 0.2265 0.1965 -0.0021 0.0001  0.0016  115 ILE B O   
2587 C CB  . ILE B 113 ? 0.2535 0.2861 0.2519 -0.0006 -0.0033 0.0051  115 ILE B CB  
2588 C CG1 . ILE B 113 ? 0.2961 0.3240 0.2895 0.0006  -0.0017 0.0048  115 ILE B CG1 
2589 C CG2 . ILE B 113 ? 0.2781 0.3149 0.2778 -0.0018 -0.0082 0.0080  115 ILE B CG2 
2590 C CD1 . ILE B 113 ? 0.2981 0.3244 0.2848 -0.0028 -0.0014 0.0035  115 ILE B CD1 
2591 N N   . THR B 114 ? 0.2460 0.2883 0.2481 -0.0090 -0.0037 0.0015  116 THR B N   
2592 C CA  . THR B 114 ? 0.2717 0.3206 0.2812 -0.0101 -0.0046 0.0009  116 THR B CA  
2593 C C   . THR B 114 ? 0.2973 0.3538 0.3120 -0.0100 -0.0106 0.0041  116 THR B C   
2594 O O   . THR B 114 ? 0.3348 0.3925 0.3441 -0.0133 -0.0140 0.0053  116 THR B O   
2595 C CB  . THR B 114 ? 0.3197 0.3688 0.3256 -0.0153 -0.0022 -0.0024 116 THR B CB  
2596 O OG1 . THR B 114 ? 0.3940 0.4440 0.3935 -0.0196 -0.0047 -0.0020 116 THR B OG1 
2597 C CG2 . THR B 114 ? 0.3009 0.3415 0.3014 -0.0149 0.0035  -0.0051 116 THR B CG2 
2598 N N   . LEU B 115 ? 0.2739 0.3354 0.2988 -0.0067 -0.0119 0.0053  117 LEU B N   
2599 C CA  . LEU B 115 ? 0.3164 0.3850 0.3477 -0.0052 -0.0179 0.0089  117 LEU B CA  
2600 C C   . LEU B 115 ? 0.3536 0.4324 0.3922 -0.0084 -0.0199 0.0075  117 LEU B C   
2601 O O   . LEU B 115 ? 0.3550 0.4348 0.3961 -0.0104 -0.0156 0.0037  117 LEU B O   
2602 C CB  . LEU B 115 ? 0.3085 0.3762 0.3476 0.0010  -0.0178 0.0110  117 LEU B CB  
2603 C CG  . LEU B 115 ? 0.3481 0.4071 0.3805 0.0037  -0.0168 0.0129  117 LEU B CG  
2604 C CD1 . LEU B 115 ? 0.3691 0.4207 0.3953 0.0034  -0.0110 0.0098  117 LEU B CD1 
2605 C CD2 . LEU B 115 ? 0.3713 0.4301 0.4115 0.0091  -0.0175 0.0153  117 LEU B CD2 
2606 N N   . ASN B 116 ? 0.3883 0.4745 0.4298 -0.0094 -0.0266 0.0105  118 ASN B N   
2607 C CA  . ASN B 116 ? 0.4289 0.5271 0.4813 -0.0108 -0.0294 0.0098  118 ASN B CA  
2608 C C   . ASN B 116 ? 0.4602 0.5630 0.5266 -0.0041 -0.0311 0.0121  118 ASN B C   
2609 O O   . ASN B 116 ? 0.4706 0.5665 0.5363 0.0008  -0.0301 0.0143  118 ASN B O   
2610 C CB  . ASN B 116 ? 0.4561 0.5610 0.5046 -0.0160 -0.0361 0.0116  118 ASN B CB  
2611 C CG  . ASN B 116 ? 0.5169 0.6188 0.5593 -0.0146 -0.0421 0.0168  118 ASN B CG  
2612 O OD1 . ASN B 116 ? 0.5439 0.6464 0.5928 -0.0088 -0.0454 0.0208  118 ASN B OD1 
2613 N ND2 . ASN B 116 ? 0.5341 0.6320 0.5634 -0.0202 -0.0432 0.0169  118 ASN B ND2 
2614 N N   . LYS B 117 ? 0.4770 0.5915 0.5563 -0.0040 -0.0332 0.0113  119 LYS B N   
2615 C CA  . LYS B 117 ? 0.4850 0.6046 0.5795 0.0024  -0.0337 0.0126  119 LYS B CA  
2616 C C   . LYS B 117 ? 0.4760 0.5954 0.5723 0.0075  -0.0405 0.0189  119 LYS B C   
2617 O O   . LYS B 117 ? 0.4760 0.5913 0.5779 0.0135  -0.0389 0.0205  119 LYS B O   
2618 C CB  . LYS B 117 ? 0.5262 0.6601 0.6353 0.0009  -0.0346 0.0099  119 LYS B CB  
2619 C CG  . LYS B 117 ? 0.6147 0.7488 0.7206 -0.0054 -0.0283 0.0037  119 LYS B CG  
2620 C CD  . LYS B 117 ? 0.6970 0.8401 0.8004 -0.0124 -0.0324 0.0026  119 LYS B CD  
2621 C CE  . LYS B 117 ? 0.7631 0.9027 0.8589 -0.0193 -0.0258 -0.0032 119 LYS B CE  
2622 N NZ  . LYS B 117 ? 0.8150 0.9650 0.9105 -0.0265 -0.0295 -0.0048 119 LYS B NZ  
2623 N N   . GLN B 118 ? 0.4773 0.5996 0.5675 0.0049  -0.0479 0.0226  120 GLN B N   
2624 C CA  . GLN B 118 ? 0.4944 0.6139 0.5833 0.0093  -0.0545 0.0290  120 GLN B CA  
2625 C C   . GLN B 118 ? 0.4985 0.6035 0.5781 0.0124  -0.0503 0.0302  120 GLN B C   
2626 O O   . GLN B 118 ? 0.5034 0.6048 0.5853 0.0177  -0.0530 0.0346  120 GLN B O   
2627 C CB  . GLN B 118 ? 0.5386 0.6605 0.6175 0.0041  -0.0621 0.0322  120 GLN B CB  
2628 C CG  . GLN B 118 ? 0.6224 0.7434 0.7011 0.0083  -0.0704 0.0395  120 GLN B CG  
2629 C CD  . GLN B 118 ? 0.6892 0.8220 0.7864 0.0142  -0.0757 0.0422  120 GLN B CD  
2630 O OE1 . GLN B 118 ? 0.6868 0.8313 0.7890 0.0122  -0.0833 0.0443  120 GLN B OE1 
2631 N NE2 . GLN B 118 ? 0.7093 0.8396 0.8175 0.0214  -0.0717 0.0421  120 GLN B NE2 
2632 N N   . GLN B 119 ? 0.4869 0.5838 0.5563 0.0090  -0.0437 0.0263  121 GLN B N   
2633 C CA  . GLN B 119 ? 0.4857 0.5705 0.5469 0.0112  -0.0395 0.0266  121 GLN B CA  
2634 C C   . GLN B 119 ? 0.5043 0.5861 0.5739 0.0162  -0.0335 0.0247  121 GLN B C   
2635 O O   . GLN B 119 ? 0.5244 0.5970 0.5887 0.0185  -0.0307 0.0255  121 GLN B O   
2636 C CB  . GLN B 119 ? 0.4726 0.5509 0.5198 0.0057  -0.0358 0.0235  121 GLN B CB  
2637 C CG  . GLN B 119 ? 0.4481 0.5249 0.4838 0.0011  -0.0406 0.0258  121 GLN B CG  
2638 C CD  . GLN B 119 ? 0.4826 0.5534 0.5066 -0.0039 -0.0359 0.0221  121 GLN B CD  
2639 O OE1 . GLN B 119 ? 0.4989 0.5724 0.5230 -0.0075 -0.0329 0.0182  121 GLN B OE1 
2640 N NE2 . GLN B 119 ? 0.4493 0.5113 0.4631 -0.0043 -0.0348 0.0231  121 GLN B NE2 
2641 N N   . ARG B 120 ? 0.4941 0.5833 0.5761 0.0172  -0.0311 0.0218  122 ARG B N   
2642 C CA  . ARG B 120 ? 0.4793 0.5660 0.5699 0.0216  -0.0254 0.0199  122 ARG B CA  
2643 C C   . ARG B 120 ? 0.4797 0.5627 0.5747 0.0277  -0.0276 0.0244  122 ARG B C   
2644 O O   . ARG B 120 ? 0.4899 0.5644 0.5829 0.0302  -0.0227 0.0238  122 ARG B O   
2645 C CB  . ARG B 120 ? 0.4487 0.5457 0.5532 0.0211  -0.0232 0.0162  122 ARG B CB  
2646 C CG  . ARG B 120 ? 0.4328 0.5296 0.5494 0.0255  -0.0178 0.0142  122 ARG B CG  
2647 C CD  . ARG B 120 ? 0.4023 0.4899 0.5133 0.0243  -0.0093 0.0101  122 ARG B CD  
2648 N NE  . ARG B 120 ? 0.3493 0.4381 0.4562 0.0188  -0.0055 0.0055  122 ARG B NE  
2649 C CZ  . ARG B 120 ? 0.3335 0.4297 0.4500 0.0169  -0.0026 0.0015  122 ARG B CZ  
2650 N NH1 . ARG B 120 ? 0.2545 0.3592 0.3871 0.0203  -0.0030 0.0013  122 ARG B NH1 
2651 N NH2 . ARG B 120 ? 0.3259 0.4209 0.4360 0.0115  0.0010  -0.0024 122 ARG B NH2 
2652 N N   . ARG B 121 ? 0.4628 0.5516 0.5631 0.0300  -0.0350 0.0289  123 ARG B N   
2653 C CA  . ARG B 121 ? 0.4648 0.5492 0.5689 0.0361  -0.0375 0.0336  123 ARG B CA  
2654 C C   . ARG B 121 ? 0.4526 0.5265 0.5415 0.0353  -0.0403 0.0377  123 ARG B C   
2655 O O   . ARG B 121 ? 0.4631 0.5283 0.5505 0.0392  -0.0385 0.0398  123 ARG B O   
2656 C CB  . ARG B 121 ? 0.4978 0.5936 0.6169 0.0401  -0.0443 0.0370  123 ARG B CB  
2657 C CG  . ARG B 121 ? 0.5662 0.6580 0.6945 0.0480  -0.0446 0.0407  123 ARG B CG  
2658 C CD  . ARG B 121 ? 0.6406 0.7429 0.7823 0.0525  -0.0529 0.0453  123 ARG B CD  
2659 N NE  . ARG B 121 ? 0.7136 0.8137 0.8439 0.0510  -0.0617 0.0513  123 ARG B NE  
2660 C CZ  . ARG B 121 ? 0.7474 0.8555 0.8850 0.0540  -0.0710 0.0566  123 ARG B CZ  
2661 N NH1 . ARG B 121 ? 0.7372 0.8416 0.8616 0.0516  -0.0786 0.0619  123 ARG B NH1 
2662 N NH2 . ARG B 121 ? 0.7603 0.8804 0.9183 0.0593  -0.0729 0.0566  123 ARG B NH2 
2663 N N   . SER B 122 ? 0.4396 0.5139 0.5168 0.0298  -0.0440 0.0384  124 SER B N   
2664 C CA  . SER B 122 ? 0.4496 0.5150 0.5123 0.0281  -0.0471 0.0420  124 SER B CA  
2665 C C   . SER B 122 ? 0.4341 0.4892 0.4844 0.0253  -0.0407 0.0389  124 SER B C   
2666 O O   . SER B 122 ? 0.4498 0.4957 0.4911 0.0257  -0.0407 0.0413  124 SER B O   
2667 C CB  . SER B 122 ? 0.4920 0.5626 0.5477 0.0227  -0.0535 0.0436  124 SER B CB  
2668 O OG  . SER B 122 ? 0.5324 0.6052 0.5835 0.0171  -0.0495 0.0383  124 SER B OG  
2669 N N   . ASP B 123 ? 0.3927 0.4496 0.4427 0.0223  -0.0354 0.0336  125 ASP B N   
2670 C CA  . ASP B 123 ? 0.3639 0.4134 0.4021 0.0189  -0.0307 0.0308  125 ASP B CA  
2671 C C   . ASP B 123 ? 0.2871 0.3343 0.3281 0.0198  -0.0235 0.0263  125 ASP B C   
2672 O O   . ASP B 123 ? 0.2772 0.3176 0.3095 0.0185  -0.0202 0.0249  125 ASP B O   
2673 C CB  . ASP B 123 ? 0.4147 0.4669 0.4449 0.0129  -0.0322 0.0290  125 ASP B CB  
2674 C CG  . ASP B 123 ? 0.5293 0.5805 0.5506 0.0097  -0.0381 0.0326  125 ASP B CG  
2675 O OD1 . ASP B 123 ? 0.5601 0.6060 0.5783 0.0120  -0.0407 0.0366  125 ASP B OD1 
2676 O OD2 . ASP B 123 ? 0.5723 0.6269 0.5885 0.0046  -0.0397 0.0313  125 ASP B OD2 
2677 N N   . LEU B 124 ? 0.2474 0.2999 0.2996 0.0218  -0.0210 0.0241  126 LEU B N   
2678 C CA  . LEU B 124 ? 0.2298 0.2791 0.2813 0.0211  -0.0143 0.0198  126 LEU B CA  
2679 C C   . LEU B 124 ? 0.2035 0.2442 0.2515 0.0235  -0.0106 0.0200  126 LEU B C   
2680 O O   . LEU B 124 ? 0.1973 0.2329 0.2373 0.0216  -0.0072 0.0178  126 LEU B O   
2681 C CB  . LEU B 124 ? 0.2311 0.2865 0.2936 0.0218  -0.0115 0.0169  126 LEU B CB  
2682 C CG  . LEU B 124 ? 0.2467 0.2976 0.3068 0.0205  -0.0047 0.0126  126 LEU B CG  
2683 C CD1 . LEU B 124 ? 0.2613 0.3104 0.3117 0.0161  -0.0036 0.0102  126 LEU B CD1 
2684 C CD2 . LEU B 124 ? 0.2659 0.3222 0.3379 0.0213  -0.0016 0.0099  126 LEU B CD2 
2685 N N   . ASP B 125 ? 0.1835 0.2227 0.2375 0.0275  -0.0112 0.0225  127 ASP B N   
2686 C CA  . ASP B 125 ? 0.1892 0.2201 0.2400 0.0292  -0.0072 0.0223  127 ASP B CA  
2687 C C   . ASP B 125 ? 0.1882 0.2126 0.2261 0.0270  -0.0082 0.0235  127 ASP B C   
2688 O O   . ASP B 125 ? 0.1911 0.2104 0.2232 0.0257  -0.0042 0.0214  127 ASP B O   
2689 C CB  . ASP B 125 ? 0.2270 0.2568 0.2867 0.0341  -0.0078 0.0251  127 ASP B CB  
2690 C CG  . ASP B 125 ? 0.3120 0.3473 0.3856 0.0367  -0.0052 0.0232  127 ASP B CG  
2691 O OD1 . ASP B 125 ? 0.2931 0.3305 0.3681 0.0345  -0.0010 0.0190  127 ASP B OD1 
2692 O OD2 . ASP B 125 ? 0.3663 0.4035 0.4495 0.0410  -0.0071 0.0258  127 ASP B OD2 
2693 N N   . ARG B 126 ? 0.1752 0.2003 0.2085 0.0259  -0.0136 0.0268  128 ARG B N   
2694 C CA  . ARG B 126 ? 0.1969 0.2154 0.2185 0.0235  -0.0138 0.0276  128 ARG B CA  
2695 C C   . ARG B 126 ? 0.1647 0.1841 0.1797 0.0194  -0.0116 0.0239  128 ARG B C   
2696 O O   . ARG B 126 ? 0.1637 0.1783 0.1721 0.0181  -0.0087 0.0223  128 ARG B O   
2697 C CB  . ARG B 126 ? 0.2742 0.2912 0.2910 0.0230  -0.0195 0.0321  128 ARG B CB  
2698 C CG  . ARG B 126 ? 0.3803 0.4028 0.3944 0.0196  -0.0239 0.0325  128 ARG B CG  
2699 C CD  . ARG B 126 ? 0.4502 0.4711 0.4606 0.0197  -0.0303 0.0378  128 ARG B CD  
2700 N NE  . ARG B 126 ? 0.4823 0.5082 0.4883 0.0154  -0.0348 0.0383  128 ARG B NE  
2701 C CZ  . ARG B 126 ? 0.5471 0.5706 0.5420 0.0099  -0.0339 0.0364  128 ARG B CZ  
2702 N NH1 . ARG B 126 ? 0.5678 0.5848 0.5557 0.0084  -0.0291 0.0339  128 ARG B NH1 
2703 N NH2 . ARG B 126 ? 0.5834 0.6112 0.5745 0.0057  -0.0377 0.0367  128 ARG B NH2 
2704 N N   . PHE B 127 ? 0.1558 0.1813 0.1728 0.0176  -0.0127 0.0223  129 PHE B N   
2705 C CA  . PHE B 127 ? 0.1616 0.1870 0.1728 0.0144  -0.0103 0.0189  129 PHE B CA  
2706 C C   . PHE B 127 ? 0.1227 0.1458 0.1350 0.0155  -0.0052 0.0159  129 PHE B C   
2707 O O   . PHE B 127 ? 0.1266 0.1469 0.1327 0.0140  -0.0031 0.0140  129 PHE B O   
2708 C CB  . PHE B 127 ? 0.1732 0.2045 0.1862 0.0120  -0.0118 0.0177  129 PHE B CB  
2709 C CG  . PHE B 127 ? 0.2282 0.2617 0.2366 0.0088  -0.0164 0.0196  129 PHE B CG  
2710 C CD1 . PHE B 127 ? 0.2603 0.2896 0.2616 0.0078  -0.0188 0.0221  129 PHE B CD1 
2711 C CD2 . PHE B 127 ? 0.2942 0.3334 0.3044 0.0062  -0.0181 0.0186  129 PHE B CD2 
2712 C CE1 . PHE B 127 ? 0.3056 0.3363 0.3012 0.0040  -0.0231 0.0239  129 PHE B CE1 
2713 C CE2 . PHE B 127 ? 0.3242 0.3653 0.3292 0.0025  -0.0224 0.0203  129 PHE B CE2 
2714 C CZ  . PHE B 127 ? 0.3075 0.3442 0.3050 0.0014  -0.0249 0.0229  129 PHE B CZ  
2715 N N   . TRP B 128 ? 0.1077 0.1320 0.1277 0.0179  -0.0033 0.0154  130 TRP B N   
2716 C CA  . TRP B 128 ? 0.1135 0.1346 0.1331 0.0184  0.0014  0.0128  130 TRP B CA  
2717 C C   . TRP B 128 ? 0.1239 0.1394 0.1387 0.0189  0.0031  0.0131  130 TRP B C   
2718 O O   . TRP B 128 ? 0.1235 0.1367 0.1330 0.0176  0.0053  0.0111  130 TRP B O   
2719 C CB  . TRP B 128 ? 0.1118 0.1351 0.1402 0.0201  0.0036  0.0118  130 TRP B CB  
2720 C CG  . TRP B 128 ? 0.1212 0.1406 0.1482 0.0199  0.0084  0.0091  130 TRP B CG  
2721 C CD1 . TRP B 128 ? 0.1270 0.1435 0.1577 0.0213  0.0119  0.0085  130 TRP B CD1 
2722 C CD2 . TRP B 128 ? 0.1194 0.1371 0.1406 0.0179  0.0104  0.0067  130 TRP B CD2 
2723 N NE1 . TRP B 128 ? 0.1253 0.1386 0.1522 0.0198  0.0157  0.0058  130 TRP B NE1 
2724 C CE2 . TRP B 128 ? 0.1247 0.1385 0.1456 0.0180  0.0145  0.0050  130 TRP B CE2 
2725 C CE3 . TRP B 128 ? 0.1188 0.1372 0.1346 0.0161  0.0091  0.0060  130 TRP B CE3 
2726 C CZ2 . TRP B 128 ? 0.1224 0.1331 0.1374 0.0164  0.0165  0.0031  130 TRP B CZ2 
2727 C CZ3 . TRP B 128 ? 0.1205 0.1358 0.1316 0.0152  0.0115  0.0040  130 TRP B CZ3 
2728 C CH2 . TRP B 128 ? 0.1148 0.1263 0.1252 0.0155  0.0148  0.0029  130 TRP B CH2 
2729 N N   . LEU B 129 ? 0.1306 0.1437 0.1470 0.0206  0.0020  0.0157  131 LEU B N   
2730 C CA  . LEU B 129 ? 0.1328 0.1399 0.1437 0.0203  0.0041  0.0158  131 LEU B CA  
2731 C C   . LEU B 129 ? 0.1347 0.1410 0.1369 0.0173  0.0033  0.0149  131 LEU B C   
2732 O O   . LEU B 129 ? 0.1299 0.1342 0.1280 0.0161  0.0059  0.0128  131 LEU B O   
2733 C CB  . LEU B 129 ? 0.1349 0.1383 0.1478 0.0225  0.0030  0.0189  131 LEU B CB  
2734 C CG  . LEU B 129 ? 0.1722 0.1683 0.1788 0.0217  0.0057  0.0189  131 LEU B CG  
2735 C CD1 . LEU B 129 ? 0.2043 0.1981 0.2101 0.0209  0.0108  0.0155  131 LEU B CD1 
2736 C CD2 . LEU B 129 ? 0.2051 0.1964 0.2140 0.0246  0.0045  0.0226  131 LEU B CD2 
2737 N N   . GLU B 130 ? 0.1396 0.1480 0.1391 0.0158  -0.0002 0.0162  132 GLU B N   
2738 C CA  . GLU B 130 ? 0.1439 0.1517 0.1357 0.0126  -0.0002 0.0149  132 GLU B CA  
2739 C C   . GLU B 130 ? 0.1561 0.1662 0.1473 0.0119  0.0021  0.0114  132 GLU B C   
2740 O O   . GLU B 130 ? 0.1629 0.1722 0.1500 0.0104  0.0037  0.0094  132 GLU B O   
2741 C CB  . GLU B 130 ? 0.1569 0.1663 0.1456 0.0105  -0.0039 0.0165  132 GLU B CB  
2742 C CG  . GLU B 130 ? 0.2855 0.2922 0.2734 0.0112  -0.0073 0.0206  132 GLU B CG  
2743 C CD  . GLU B 130 ? 0.3203 0.3200 0.3024 0.0107  -0.0060 0.0217  132 GLU B CD  
2744 O OE1 . GLU B 130 ? 0.2307 0.2286 0.2075 0.0083  -0.0031 0.0190  132 GLU B OE1 
2745 O OE2 . GLU B 130 ? 0.4383 0.4344 0.4215 0.0129  -0.0078 0.0252  132 GLU B OE2 
2746 N N   . THR B 131 ? 0.1247 0.1379 0.1204 0.0129  0.0021  0.0106  133 THR B N   
2747 C CA  . THR B 131 ? 0.0998 0.1138 0.0949 0.0128  0.0042  0.0079  133 THR B CA  
2748 C C   . THR B 131 ? 0.0908 0.1024 0.0850 0.0136  0.0068  0.0068  133 THR B C   
2749 O O   . THR B 131 ? 0.1057 0.1175 0.0967 0.0129  0.0076  0.0051  133 THR B O   
2750 C CB  . THR B 131 ? 0.1327 0.1489 0.1321 0.0135  0.0043  0.0075  133 THR B CB  
2751 O OG1 . THR B 131 ? 0.1240 0.1431 0.1239 0.0121  0.0017  0.0085  133 THR B OG1 
2752 C CG2 . THR B 131 ? 0.1377 0.1532 0.1350 0.0134  0.0062  0.0053  133 THR B CG2 
2753 N N   . LEU B 132 ? 0.1011 0.1105 0.0984 0.0149  0.0081  0.0077  134 LEU B N   
2754 C CA  . LEU B 132 ? 0.1083 0.1149 0.1040 0.0148  0.0110  0.0064  134 LEU B CA  
2755 C C   . LEU B 132 ? 0.1172 0.1226 0.1078 0.0131  0.0112  0.0059  134 LEU B C   
2756 O O   . LEU B 132 ? 0.1123 0.1179 0.1001 0.0121  0.0124  0.0041  134 LEU B O   
2757 C CB  . LEU B 132 ? 0.1178 0.1216 0.1177 0.0161  0.0129  0.0072  134 LEU B CB  
2758 C CG  . LEU B 132 ? 0.1260 0.1315 0.1319 0.0174  0.0136  0.0070  134 LEU B CG  
2759 C CD1 . LEU B 132 ? 0.1381 0.1412 0.1496 0.0190  0.0159  0.0076  134 LEU B CD1 
2760 C CD2 . LEU B 132 ? 0.1529 0.1578 0.1563 0.0164  0.0155  0.0048  134 LEU B CD2 
2761 N N   . LEU B 133 ? 0.1192 0.1232 0.1083 0.0125  0.0100  0.0075  135 LEU B N   
2762 C CA  . LEU B 133 ? 0.1168 0.1192 0.1006 0.0102  0.0107  0.0067  135 LEU B CA  
2763 C C   . LEU B 133 ? 0.1285 0.1351 0.1099 0.0085  0.0101  0.0044  135 LEU B C   
2764 O O   . LEU B 133 ? 0.1262 0.1335 0.1050 0.0068  0.0115  0.0024  135 LEU B O   
2765 C CB  . LEU B 133 ? 0.1145 0.1132 0.0960 0.0097  0.0096  0.0091  135 LEU B CB  
2766 C CG  . LEU B 133 ? 0.1467 0.1407 0.1313 0.0120  0.0102  0.0116  135 LEU B CG  
2767 C CD1 . LEU B 133 ? 0.1682 0.1579 0.1492 0.0115  0.0086  0.0143  135 LEU B CD1 
2768 C CD2 . LEU B 133 ? 0.1482 0.1388 0.1328 0.0119  0.0143  0.0100  135 LEU B CD2 
2769 N N   . CYS B 134 ? 0.1075 0.1171 0.0904 0.0090  0.0083  0.0044  136 CYS B N   
2770 C CA  . CYS B 134 ? 0.1006 0.1140 0.0825 0.0081  0.0083  0.0021  136 CYS B CA  
2771 C C   . CYS B 134 ? 0.1026 0.1179 0.0858 0.0094  0.0092  0.0003  136 CYS B C   
2772 O O   . CYS B 134 ? 0.1167 0.1351 0.0993 0.0086  0.0096  -0.0017 136 CYS B O   
2773 C CB  . CYS B 134 ? 0.1088 0.1237 0.0916 0.0082  0.0069  0.0023  136 CYS B CB  
2774 S SG  . CYS B 134 ? 0.1573 0.1708 0.1362 0.0052  0.0053  0.0038  136 CYS B SG  
2775 N N   . LEU B 135 ? 0.0789 0.0927 0.0640 0.0112  0.0095  0.0012  137 LEU B N   
2776 C CA  . LEU B 135 ? 0.1048 0.1190 0.0897 0.0121  0.0100  0.0002  137 LEU B CA  
2777 C C   . LEU B 135 ? 0.1035 0.1175 0.0861 0.0105  0.0111  -0.0008 137 LEU B C   
2778 O O   . LEU B 135 ? 0.0921 0.1098 0.0739 0.0099  0.0106  -0.0025 137 LEU B O   
2779 C CB  . LEU B 135 ? 0.1126 0.1240 0.0989 0.0134  0.0106  0.0012  137 LEU B CB  
2780 C CG  . LEU B 135 ? 0.1277 0.1394 0.1147 0.0147  0.0099  0.0011  137 LEU B CG  
2781 C CD1 . LEU B 135 ? 0.0968 0.1103 0.0851 0.0144  0.0088  0.0013  137 LEU B CD1 
2782 C CD2 . LEU B 135 ? 0.1384 0.1471 0.1264 0.0152  0.0112  0.0016  137 LEU B CD2 
2783 N N   . ILE B 136 ? 0.1086 0.1188 0.0906 0.0097  0.0128  0.0000  138 ILE B N   
2784 C CA  . ILE B 136 ? 0.1276 0.1366 0.1066 0.0076  0.0146  -0.0012 138 ILE B CA  
2785 C C   . ILE B 136 ? 0.1229 0.1345 0.0998 0.0052  0.0147  -0.0027 138 ILE B C   
2786 O O   . ILE B 136 ? 0.1148 0.1285 0.0896 0.0031  0.0153  -0.0046 138 ILE B O   
2787 C CB  . ILE B 136 ? 0.1504 0.1535 0.1293 0.0073  0.0173  -0.0003 138 ILE B CB  
2788 C CG1 . ILE B 136 ? 0.1545 0.1545 0.1340 0.0074  0.0177  0.0013  138 ILE B CG1 
2789 C CG2 . ILE B 136 ? 0.1499 0.1514 0.1315 0.0092  0.0177  0.0004  138 ILE B CG2 
2790 C CD1 . ILE B 136 ? 0.1577 0.1514 0.1373 0.0073  0.0209  0.0019  138 ILE B CD1 
2791 N N   . GLY B 137 ? 0.1122 0.1236 0.0891 0.0049  0.0141  -0.0021 139 GLY B N   
2792 C CA  . GLY B 137 ? 0.1036 0.1168 0.0779 0.0019  0.0147  -0.0039 139 GLY B CA  
2793 C C   . GLY B 137 ? 0.1105 0.1307 0.0867 0.0017  0.0136  -0.0062 139 GLY B C   
2794 O O   . GLY B 137 ? 0.1229 0.1454 0.0976 -0.0011 0.0146  -0.0084 139 GLY B O   
2795 N N   . GLU B 138 ? 0.0913 0.1144 0.0709 0.0047  0.0119  -0.0060 140 GLU B N   
2796 C CA  . GLU B 138 ? 0.0968 0.1262 0.0794 0.0055  0.0109  -0.0081 140 GLU B CA  
2797 C C   . GLU B 138 ? 0.1178 0.1480 0.1001 0.0037  0.0116  -0.0093 140 GLU B C   
2798 O O   . GLU B 138 ? 0.1114 0.1464 0.0948 0.0019  0.0126  -0.0122 140 GLU B O   
2799 C CB  . GLU B 138 ? 0.0848 0.1198 0.0682 0.0043  0.0108  -0.0105 140 GLU B CB  
2800 C CG  . GLU B 138 ? 0.0985 0.1325 0.0806 0.0049  0.0101  -0.0096 140 GLU B CG  
2801 C CD  . GLU B 138 ? 0.1625 0.1976 0.1468 0.0086  0.0077  -0.0085 140 GLU B CD  
2802 O OE1 . GLU B 138 ? 0.1583 0.1987 0.1464 0.0106  0.0062  -0.0097 140 GLU B OE1 
2803 O OE2 . GLU B 138 ? 0.1640 0.1942 0.1460 0.0095  0.0076  -0.0066 140 GLU B OE2 
2804 N N   . SER B 139 ? 0.1168 0.1427 0.0977 0.0040  0.0113  -0.0072 141 SER B N   
2805 C CA  . SER B 139 ? 0.1139 0.1389 0.0923 0.0012  0.0120  -0.0079 141 SER B CA  
2806 C C   . SER B 139 ? 0.1311 0.1598 0.1118 0.0013  0.0124  -0.0101 141 SER B C   
2807 O O   . SER B 139 ? 0.1516 0.1792 0.1293 -0.0018 0.0135  -0.0112 141 SER B O   
2808 C CB  . SER B 139 ? 0.1246 0.1441 0.1003 0.0012  0.0108  -0.0046 141 SER B CB  
2809 O OG  . SER B 139 ? 0.1390 0.1545 0.1135 0.0017  0.0108  -0.0024 141 SER B OG  
2810 N N   . PHE B 140 ? 0.0983 0.1304 0.0836 0.0045  0.0119  -0.0110 142 PHE B N   
2811 C CA  . PHE B 140 ? 0.1110 0.1460 0.0994 0.0055  0.0127  -0.0132 142 PHE B CA  
2812 C C   . PHE B 140 ? 0.1529 0.1947 0.1460 0.0059  0.0137  -0.0167 142 PHE B C   
2813 O O   . PHE B 140 ? 0.1537 0.1984 0.1513 0.0082  0.0142  -0.0184 142 PHE B O   
2814 C CB  . PHE B 140 ? 0.1129 0.1458 0.1030 0.0091  0.0115  -0.0115 142 PHE B CB  
2815 C CG  . PHE B 140 ? 0.1240 0.1517 0.1108 0.0087  0.0105  -0.0084 142 PHE B CG  
2816 C CD1 . PHE B 140 ? 0.1233 0.1487 0.1069 0.0057  0.0107  -0.0080 142 PHE B CD1 
2817 C CD2 . PHE B 140 ? 0.1160 0.1415 0.1031 0.0109  0.0093  -0.0062 142 PHE B CD2 
2818 C CE1 . PHE B 140 ? 0.1264 0.1484 0.1082 0.0055  0.0092  -0.0051 142 PHE B CE1 
2819 C CE2 . PHE B 140 ? 0.0977 0.1197 0.0835 0.0106  0.0086  -0.0038 142 PHE B CE2 
2820 C CZ  . PHE B 140 ? 0.1141 0.1349 0.0979 0.0082  0.0083  -0.0032 142 PHE B CZ  
2821 N N   . ASP B 141 ? 0.1809 0.2253 0.1733 0.0036  0.0141  -0.0178 143 ASP B N   
2822 C CA  . ASP B 141 ? 0.1940 0.2465 0.1914 0.0033  0.0147  -0.0213 143 ASP B CA  
2823 C C   . ASP B 141 ? 0.1688 0.2257 0.1723 0.0084  0.0123  -0.0209 143 ASP B C   
2824 O O   . ASP B 141 ? 0.1673 0.2209 0.1688 0.0106  0.0101  -0.0179 143 ASP B O   
2825 C CB  . ASP B 141 ? 0.2391 0.2942 0.2376 0.0000  0.0179  -0.0251 143 ASP B CB  
2826 C CG  . ASP B 141 ? 0.3582 0.4088 0.3493 -0.0057 0.0199  -0.0255 143 ASP B CG  
2827 O OD1 . ASP B 141 ? 0.4329 0.4837 0.4216 -0.0078 0.0199  -0.0254 143 ASP B OD1 
2828 O OD2 . ASP B 141 ? 0.3413 0.3877 0.3284 -0.0082 0.0214  -0.0256 143 ASP B OD2 
2829 N N   . ASP B 142 ? 0.1668 0.2306 0.1775 0.0104  0.0128  -0.0239 144 ASP B N   
2830 C CA  . ASP B 142 ? 0.1721 0.2396 0.1882 0.0159  0.0098  -0.0228 144 ASP B CA  
2831 C C   . ASP B 142 ? 0.1760 0.2359 0.1895 0.0196  0.0085  -0.0194 144 ASP B C   
2832 O O   . ASP B 142 ? 0.1811 0.2401 0.1947 0.0231  0.0056  -0.0169 144 ASP B O   
2833 C CB  . ASP B 142 ? 0.1978 0.2736 0.2232 0.0181  0.0106  -0.0265 144 ASP B CB  
2834 C CG  . ASP B 142 ? 0.2842 0.3701 0.3142 0.0153  0.0109  -0.0301 144 ASP B CG  
2835 O OD1 . ASP B 142 ? 0.3103 0.3968 0.3363 0.0125  0.0097  -0.0293 144 ASP B OD1 
2836 O OD2 . ASP B 142 ? 0.3052 0.3984 0.3432 0.0158  0.0127  -0.0339 144 ASP B OD2 
2837 N N   . TYR B 143 ? 0.1414 0.1954 0.1518 0.0181  0.0109  -0.0192 145 TYR B N   
2838 C CA  . TYR B 143 ? 0.1305 0.1774 0.1381 0.0206  0.0103  -0.0165 145 TYR B CA  
2839 C C   . TYR B 143 ? 0.1338 0.1754 0.1358 0.0201  0.0086  -0.0130 145 TYR B C   
2840 O O   . TYR B 143 ? 0.1363 0.1726 0.1364 0.0223  0.0081  -0.0110 145 TYR B O   
2841 C CB  . TYR B 143 ? 0.1476 0.1909 0.1536 0.0185  0.0133  -0.0178 145 TYR B CB  
2842 C CG  . TYR B 143 ? 0.1985 0.2464 0.2102 0.0188  0.0159  -0.0218 145 TYR B CG  
2843 C CD1 . TYR B 143 ? 0.2124 0.2636 0.2310 0.0239  0.0154  -0.0226 145 TYR B CD1 
2844 C CD2 . TYR B 143 ? 0.2566 0.3054 0.2670 0.0140  0.0191  -0.0247 145 TYR B CD2 
2845 C CE1 . TYR B 143 ? 0.2437 0.2993 0.2690 0.0246  0.0183  -0.0266 145 TYR B CE1 
2846 C CE2 . TYR B 143 ? 0.2846 0.3374 0.3005 0.0139  0.0224  -0.0290 145 TYR B CE2 
2847 C CZ  . TYR B 143 ? 0.2752 0.3317 0.2993 0.0194  0.0222  -0.0301 145 TYR B CZ  
2848 O OH  . TYR B 143 ? 0.3275 0.3883 0.3583 0.0194  0.0259  -0.0347 145 TYR B OH  
2849 N N   . SER B 144 ? 0.1037 0.1461 0.1032 0.0173  0.0082  -0.0126 146 SER B N   
2850 C CA  . SER B 144 ? 0.1153 0.1532 0.1107 0.0173  0.0070  -0.0098 146 SER B CA  
2851 C C   . SER B 144 ? 0.1284 0.1659 0.1241 0.0207  0.0047  -0.0082 146 SER B C   
2852 O O   . SER B 144 ? 0.1194 0.1516 0.1115 0.0210  0.0044  -0.0061 146 SER B O   
2853 C CB  . SER B 144 ? 0.1382 0.1768 0.1311 0.0138  0.0075  -0.0100 146 SER B CB  
2854 O OG  . SER B 144 ? 0.1644 0.1996 0.1546 0.0110  0.0090  -0.0096 146 SER B OG  
2855 N N   . ASP B 145 ? 0.1258 0.1688 0.1257 0.0232  0.0032  -0.0094 147 ASP B N   
2856 C CA  . ASP B 145 ? 0.1360 0.1781 0.1353 0.0266  0.0004  -0.0075 147 ASP B CA  
2857 C C   . ASP B 145 ? 0.1435 0.1781 0.1408 0.0294  0.0007  -0.0056 147 ASP B C   
2858 O O   . ASP B 145 ? 0.1624 0.1926 0.1560 0.0312  -0.0010 -0.0033 147 ASP B O   
2859 C CB  . ASP B 145 ? 0.1192 0.1696 0.1246 0.0292  -0.0019 -0.0090 147 ASP B CB  
2860 C CG  . ASP B 145 ? 0.2176 0.2756 0.2242 0.0260  -0.0027 -0.0107 147 ASP B CG  
2861 O OD1 . ASP B 145 ? 0.2246 0.2796 0.2257 0.0224  -0.0022 -0.0100 147 ASP B OD1 
2862 O OD2 . ASP B 145 ? 0.2213 0.2881 0.2345 0.0269  -0.0036 -0.0131 147 ASP B OD2 
2863 N N   . ASP B 146 ? 0.1131 0.1457 0.1117 0.0293  0.0032  -0.0068 148 ASP B N   
2864 C CA  . ASP B 146 ? 0.1085 0.1336 0.1044 0.0311  0.0042  -0.0054 148 ASP B CA  
2865 C C   . ASP B 146 ? 0.1162 0.1353 0.1068 0.0284  0.0052  -0.0038 148 ASP B C   
2866 O O   . ASP B 146 ? 0.1208 0.1336 0.1085 0.0292  0.0060  -0.0027 148 ASP B O   
2867 C CB  . ASP B 146 ? 0.1048 0.1295 0.1035 0.0313  0.0068  -0.0074 148 ASP B CB  
2868 C CG  . ASP B 146 ? 0.2037 0.2303 0.2074 0.0358  0.0066  -0.0085 148 ASP B CG  
2869 O OD1 . ASP B 146 ? 0.2064 0.2400 0.2148 0.0376  0.0044  -0.0091 148 ASP B OD1 
2870 O OD2 . ASP B 146 ? 0.1886 0.2097 0.1918 0.0375  0.0086  -0.0087 148 ASP B OD2 
2871 N N   . VAL B 147 ? 0.1046 0.1256 0.0944 0.0253  0.0054  -0.0038 149 VAL B N   
2872 C CA  . VAL B 147 ? 0.0961 0.1128 0.0829 0.0232  0.0063  -0.0025 149 VAL B CA  
2873 C C   . VAL B 147 ? 0.1144 0.1270 0.0975 0.0240  0.0055  -0.0008 149 VAL B C   
2874 O O   . VAL B 147 ? 0.1279 0.1426 0.1102 0.0243  0.0039  -0.0006 149 VAL B O   
2875 C CB  . VAL B 147 ? 0.0988 0.1179 0.0861 0.0201  0.0069  -0.0028 149 VAL B CB  
2876 C CG1 . VAL B 147 ? 0.0900 0.1050 0.0755 0.0188  0.0077  -0.0013 149 VAL B CG1 
2877 C CG2 . VAL B 147 ? 0.1021 0.1237 0.0911 0.0185  0.0077  -0.0042 149 VAL B CG2 
2878 N N   . CYS B 148 ? 0.1134 0.1200 0.0937 0.0238  0.0067  0.0001  150 CYS B N   
2879 C CA  . CYS B 148 ? 0.1065 0.1080 0.0822 0.0234  0.0068  0.0014  150 CYS B CA  
2880 C C   . CYS B 148 ? 0.1062 0.1072 0.0822 0.0206  0.0086  0.0013  150 CYS B C   
2881 O O   . CYS B 148 ? 0.1267 0.1262 0.1000 0.0195  0.0087  0.0016  150 CYS B O   
2882 C CB  . CYS B 148 ? 0.1071 0.1019 0.0794 0.0245  0.0078  0.0020  150 CYS B CB  
2883 S SG  . CYS B 148 ? 0.1600 0.1541 0.1323 0.0288  0.0059  0.0024  150 CYS B SG  
2884 N N   . GLY B 149 ? 0.0968 0.0989 0.0759 0.0195  0.0098  0.0008  151 GLY B N   
2885 C CA  . GLY B 149 ? 0.1182 0.1196 0.0989 0.0176  0.0115  0.0009  151 GLY B CA  
2886 C C   . GLY B 149 ? 0.0954 0.0987 0.0798 0.0168  0.0119  0.0008  151 GLY B C   
2887 O O   . GLY B 149 ? 0.1015 0.1065 0.0865 0.0171  0.0111  0.0004  151 GLY B O   
2888 N N   . ALA B 150 ? 0.1167 0.1201 0.1041 0.0157  0.0131  0.0010  152 ALA B N   
2889 C CA  . ALA B 150 ? 0.0995 0.1055 0.0909 0.0149  0.0128  0.0011  152 ALA B CA  
2890 C C   . ALA B 150 ? 0.1034 0.1081 0.0974 0.0141  0.0149  0.0006  152 ALA B C   
2891 O O   . ALA B 150 ? 0.1155 0.1174 0.1088 0.0139  0.0169  0.0003  152 ALA B O   
2892 C CB  . ALA B 150 ? 0.1016 0.1111 0.0958 0.0149  0.0112  0.0021  152 ALA B CB  
2893 N N   . VAL B 151 ? 0.1190 0.1260 0.1159 0.0130  0.0148  0.0002  153 VAL B N   
2894 C CA  . VAL B 151 ? 0.1165 0.1234 0.1169 0.0117  0.0171  -0.0009 153 VAL B CA  
2895 C C   . VAL B 151 ? 0.1230 0.1361 0.1304 0.0113  0.0155  -0.0004 153 VAL B C   
2896 O O   . VAL B 151 ? 0.1207 0.1368 0.1278 0.0107  0.0130  0.0002  153 VAL B O   
2897 C CB  . VAL B 151 ? 0.1475 0.1501 0.1431 0.0101  0.0192  -0.0024 153 VAL B CB  
2898 C CG1 . VAL B 151 ? 0.1524 0.1551 0.1515 0.0079  0.0223  -0.0042 153 VAL B CG1 
2899 C CG2 . VAL B 151 ? 0.1685 0.1645 0.1564 0.0111  0.0199  -0.0022 153 VAL B CG2 
2900 N N   . VAL B 152 ? 0.1287 0.1441 0.1429 0.0114  0.0169  -0.0008 154 VAL B N   
2901 C CA  . VAL B 152 ? 0.1263 0.1487 0.1487 0.0112  0.0149  -0.0003 154 VAL B CA  
2902 C C   . VAL B 152 ? 0.1304 0.1540 0.1567 0.0091  0.0182  -0.0030 154 VAL B C   
2903 O O   . VAL B 152 ? 0.1384 0.1585 0.1652 0.0089  0.0221  -0.0046 154 VAL B O   
2904 C CB  . VAL B 152 ? 0.1503 0.1757 0.1793 0.0138  0.0131  0.0018  154 VAL B CB  
2905 C CG1 . VAL B 152 ? 0.1659 0.1879 0.1975 0.0150  0.0168  0.0009  154 VAL B CG1 
2906 C CG2 . VAL B 152 ? 0.1480 0.1812 0.1856 0.0138  0.0102  0.0027  154 VAL B CG2 
2907 N N   . ASN B 153 ? 0.1342 0.1625 0.1627 0.0070  0.0169  -0.0037 155 ASN B N   
2908 C CA  . ASN B 153 ? 0.1606 0.1917 0.1937 0.0044  0.0197  -0.0065 155 ASN B CA  
2909 C C   . ASN B 153 ? 0.1655 0.2070 0.2104 0.0049  0.0168  -0.0059 155 ASN B C   
2910 O O   . ASN B 153 ? 0.1692 0.2154 0.2146 0.0046  0.0123  -0.0041 155 ASN B O   
2911 C CB  . ASN B 153 ? 0.1871 0.2161 0.2135 0.0008  0.0206  -0.0082 155 ASN B CB  
2912 C CG  . ASN B 153 ? 0.2471 0.2667 0.2620 0.0009  0.0219  -0.0080 155 ASN B CG  
2913 O OD1 . ASN B 153 ? 0.2494 0.2681 0.2594 0.0007  0.0198  -0.0072 155 ASN B OD1 
2914 N ND2 . ASN B 153 ? 0.2762 0.2887 0.2866 0.0010  0.0254  -0.0090 155 ASN B ND2 
2915 N N   . VAL B 154 ? 0.1559 0.2008 0.2101 0.0057  0.0192  -0.0073 156 VAL B N   
2916 C CA  . VAL B 154 ? 0.1667 0.2223 0.2345 0.0069  0.0166  -0.0069 156 VAL B CA  
2917 C C   . VAL B 154 ? 0.1551 0.2165 0.2268 0.0026  0.0185  -0.0105 156 VAL B C   
2918 O O   . VAL B 154 ? 0.1574 0.2151 0.2282 0.0003  0.0241  -0.0140 156 VAL B O   
2919 C CB  . VAL B 154 ? 0.1529 0.2092 0.2302 0.0104  0.0190  -0.0070 156 VAL B CB  
2920 C CG1 . VAL B 154 ? 0.1568 0.2248 0.2495 0.0124  0.0157  -0.0063 156 VAL B CG1 
2921 C CG2 . VAL B 154 ? 0.1765 0.2258 0.2482 0.0138  0.0179  -0.0039 156 VAL B CG2 
2922 N N   . ARG B 155 ? 0.1496 0.2190 0.2241 0.0009  0.0139  -0.0097 157 ARG B N   
2923 C CA  . ARG B 155 ? 0.1899 0.2652 0.2668 -0.0042 0.0153  -0.0132 157 ARG B CA  
2924 C C   . ARG B 155 ? 0.2165 0.3058 0.3052 -0.0043 0.0097  -0.0122 157 ARG B C   
2925 O O   . ARG B 155 ? 0.2311 0.3233 0.3191 -0.0024 0.0034  -0.0081 157 ARG B O   
2926 C CB  . ARG B 155 ? 0.2423 0.3111 0.3056 -0.0083 0.0159  -0.0140 157 ARG B CB  
2927 C CG  . ARG B 155 ? 0.2517 0.3068 0.3028 -0.0084 0.0210  -0.0150 157 ARG B CG  
2928 C CD  . ARG B 155 ? 0.2568 0.3082 0.3085 -0.0108 0.0275  -0.0189 157 ARG B CD  
2929 N NE  . ARG B 155 ? 0.2700 0.3079 0.3085 -0.0111 0.0313  -0.0192 157 ARG B NE  
2930 C CZ  . ARG B 155 ? 0.2711 0.3019 0.3059 -0.0079 0.0324  -0.0177 157 ARG B CZ  
2931 N NH1 . ARG B 155 ? 0.2214 0.2564 0.2643 -0.0042 0.0308  -0.0160 157 ARG B NH1 
2932 N NH2 . ARG B 155 ? 0.2803 0.2997 0.3030 -0.0083 0.0350  -0.0176 157 ARG B NH2 
2933 N N   . ALA B 156 ? 0.2106 0.3089 0.3096 -0.0070 0.0118  -0.0159 158 ALA B N   
2934 C CA  . ALA B 156 ? 0.2400 0.3531 0.3504 -0.0079 0.0060  -0.0153 158 ALA B CA  
2935 C C   . ALA B 156 ? 0.2713 0.3857 0.3723 -0.0120 0.0011  -0.0137 158 ALA B C   
2936 O O   . ALA B 156 ? 0.2750 0.3982 0.3811 -0.0109 -0.0060 -0.0104 158 ALA B O   
2937 C CB  . ALA B 156 ? 0.2374 0.3594 0.3588 -0.0116 0.0102  -0.0206 158 ALA B CB  
2938 N N   . LYS B 157 ? 0.3037 0.4091 0.3910 -0.0167 0.0050  -0.0160 159 LYS B N   
2939 C CA  . LYS B 157 ? 0.3260 0.4311 0.4033 -0.0211 0.0017  -0.0152 159 LYS B CA  
2940 C C   . LYS B 157 ? 0.3325 0.4320 0.4016 -0.0180 -0.0030 -0.0104 159 LYS B C   
2941 O O   . LYS B 157 ? 0.3602 0.4616 0.4233 -0.0213 -0.0071 -0.0091 159 LYS B O   
2942 C CB  . LYS B 157 ? 0.3927 0.4878 0.4577 -0.0264 0.0084  -0.0194 159 LYS B CB  
2943 C CG  . LYS B 157 ? 0.5137 0.6051 0.5666 -0.0312 0.0072  -0.0194 159 LYS B CG  
2944 C CD  . LYS B 157 ? 0.6081 0.6877 0.6495 -0.0353 0.0146  -0.0233 159 LYS B CD  
2945 C CE  . LYS B 157 ? 0.6843 0.7610 0.7151 -0.0411 0.0146  -0.0245 159 LYS B CE  
2946 N NZ  . LYS B 157 ? 0.7453 0.8109 0.7660 -0.0454 0.0221  -0.0286 159 LYS B NZ  
2947 N N   . GLY B 158 ? 0.3032 0.3958 0.3717 -0.0123 -0.0022 -0.0080 160 GLY B N   
2948 C CA  . GLY B 158 ? 0.2648 0.3522 0.3264 -0.0095 -0.0061 -0.0037 160 GLY B CA  
2949 C C   . GLY B 158 ? 0.2315 0.3072 0.2866 -0.0061 -0.0016 -0.0036 160 GLY B C   
2950 O O   . GLY B 158 ? 0.2442 0.3125 0.2925 -0.0080 0.0036  -0.0065 160 GLY B O   
2951 N N   . ASP B 159 ? 0.1988 0.2724 0.2556 -0.0012 -0.0038 -0.0002 161 ASP B N   
2952 C CA  . ASP B 159 ? 0.1759 0.2397 0.2277 0.0018  0.0001  -0.0001 161 ASP B CA  
2953 C C   . ASP B 159 ? 0.1514 0.2072 0.1901 0.0003  0.0005  0.0001  161 ASP B C   
2954 O O   . ASP B 159 ? 0.1663 0.2238 0.2004 -0.0022 -0.0027 0.0012  161 ASP B O   
2955 C CB  . ASP B 159 ? 0.1729 0.2369 0.2304 0.0069  -0.0021 0.0031  161 ASP B CB  
2956 C CG  . ASP B 159 ? 0.2036 0.2756 0.2754 0.0092  -0.0025 0.0030  161 ASP B CG  
2957 O OD1 . ASP B 159 ? 0.1922 0.2669 0.2692 0.0075  0.0015  -0.0006 161 ASP B OD1 
2958 O OD2 . ASP B 159 ? 0.2516 0.3270 0.3295 0.0129  -0.0068 0.0066  161 ASP B OD2 
2959 N N   . LYS B 160 ? 0.1505 0.1979 0.1835 0.0017  0.0046  -0.0008 162 LYS B N   
2960 C CA  . LYS B 160 ? 0.1405 0.1810 0.1629 0.0010  0.0052  -0.0008 162 LYS B CA  
2961 C C   . LYS B 160 ? 0.1339 0.1688 0.1540 0.0047  0.0061  0.0006  162 LYS B C   
2962 O O   . LYS B 160 ? 0.1513 0.1847 0.1750 0.0066  0.0085  0.0001  162 LYS B O   
2963 C CB  . LYS B 160 ? 0.1720 0.2072 0.1885 -0.0016 0.0095  -0.0039 162 LYS B CB  
2964 C CG  . LYS B 160 ? 0.2590 0.2984 0.2759 -0.0063 0.0096  -0.0059 162 LYS B CG  
2965 C CD  . LYS B 160 ? 0.3823 0.4147 0.3931 -0.0087 0.0147  -0.0090 162 LYS B CD  
2966 C CE  . LYS B 160 ? 0.5060 0.5388 0.5217 -0.0091 0.0181  -0.0110 162 LYS B CE  
2967 N NZ  . LYS B 160 ? 0.5751 0.6006 0.5839 -0.0124 0.0232  -0.0141 162 LYS B NZ  
2968 N N   . ILE B 161 ? 0.1386 0.1708 0.1526 0.0050  0.0045  0.0019  163 ILE B N   
2969 C CA  . ILE B 161 ? 0.1133 0.1404 0.1240 0.0077  0.0055  0.0026  163 ILE B CA  
2970 C C   . ILE B 161 ? 0.1144 0.1373 0.1176 0.0068  0.0068  0.0014  163 ILE B C   
2971 O O   . ILE B 161 ? 0.1331 0.1571 0.1334 0.0045  0.0057  0.0010  163 ILE B O   
2972 C CB  . ILE B 161 ? 0.1371 0.1656 0.1490 0.0093  0.0025  0.0053  163 ILE B CB  
2973 C CG1 . ILE B 161 ? 0.1264 0.1589 0.1470 0.0110  0.0013  0.0068  163 ILE B CG1 
2974 C CG2 . ILE B 161 ? 0.1288 0.1526 0.1365 0.0110  0.0038  0.0055  163 ILE B CG2 
2975 C CD1 . ILE B 161 ? 0.1445 0.1777 0.1660 0.0125  -0.0022 0.0099  163 ILE B CD1 
2976 N N   . ALA B 162 ? 0.1230 0.1410 0.1232 0.0086  0.0091  0.0007  164 ALA B N   
2977 C CA  . ALA B 162 ? 0.1142 0.1286 0.1086 0.0086  0.0100  -0.0003 164 ALA B CA  
2978 C C   . ALA B 162 ? 0.1212 0.1333 0.1137 0.0111  0.0103  0.0001  164 ALA B C   
2979 O O   . ALA B 162 ? 0.1568 0.1676 0.1505 0.0124  0.0110  0.0005  164 ALA B O   
2980 C CB  . ALA B 162 ? 0.1245 0.1351 0.1162 0.0076  0.0127  -0.0021 164 ALA B CB  
2981 N N   . ILE B 163 ? 0.0996 0.1115 0.0894 0.0113  0.0098  -0.0004 165 ILE B N   
2982 C CA  . ILE B 163 ? 0.1009 0.1114 0.0890 0.0135  0.0101  -0.0005 165 ILE B CA  
2983 C C   . ILE B 163 ? 0.1165 0.1230 0.1017 0.0148  0.0115  -0.0016 165 ILE B C   
2984 O O   . ILE B 163 ? 0.1155 0.1213 0.0995 0.0140  0.0123  -0.0028 165 ILE B O   
2985 C CB  . ILE B 163 ? 0.1086 0.1218 0.0964 0.0131  0.0089  -0.0006 165 ILE B CB  
2986 C CG1 . ILE B 163 ? 0.1016 0.1166 0.0911 0.0124  0.0076  0.0009  165 ILE B CG1 
2987 C CG2 . ILE B 163 ? 0.1040 0.1170 0.0910 0.0153  0.0092  -0.0014 165 ILE B CG2 
2988 C CD1 . ILE B 163 ? 0.1093 0.1259 0.0972 0.0113  0.0069  0.0008  165 ILE B CD1 
2989 N N   . TRP B 164 ? 0.0953 0.0986 0.0789 0.0167  0.0120  -0.0011 166 TRP B N   
2990 C CA  . TRP B 164 ? 0.0945 0.0930 0.0747 0.0185  0.0128  -0.0014 166 TRP B CA  
2991 C C   . TRP B 164 ? 0.1223 0.1228 0.1030 0.0211  0.0113  -0.0014 166 TRP B C   
2992 O O   . TRP B 164 ? 0.1345 0.1380 0.1162 0.0215  0.0100  -0.0009 166 TRP B O   
2993 C CB  . TRP B 164 ? 0.0976 0.0911 0.0746 0.0188  0.0136  -0.0006 166 TRP B CB  
2994 C CG  . TRP B 164 ? 0.1273 0.1183 0.1040 0.0163  0.0157  -0.0012 166 TRP B CG  
2995 C CD1 . TRP B 164 ? 0.1437 0.1387 0.1242 0.0140  0.0161  -0.0018 166 TRP B CD1 
2996 C CD2 . TRP B 164 ? 0.1409 0.1252 0.1130 0.0156  0.0178  -0.0013 166 TRP B CD2 
2997 N NE1 . TRP B 164 ? 0.1501 0.1424 0.1300 0.0119  0.0183  -0.0027 166 TRP B NE1 
2998 C CE2 . TRP B 164 ? 0.1495 0.1347 0.1239 0.0126  0.0198  -0.0025 166 TRP B CE2 
2999 C CE3 . TRP B 164 ? 0.1484 0.1259 0.1144 0.0170  0.0180  -0.0004 166 TRP B CE3 
3000 C CZ2 . TRP B 164 ? 0.1725 0.1520 0.1432 0.0107  0.0227  -0.0033 166 TRP B CZ2 
3001 C CZ3 . TRP B 164 ? 0.1870 0.1574 0.1480 0.0150  0.0207  -0.0008 166 TRP B CZ3 
3002 C CH2 . TRP B 164 ? 0.1874 0.1588 0.1508 0.0118  0.0233  -0.0025 166 TRP B CH2 
3003 N N   . THR B 165 ? 0.1125 0.1112 0.0927 0.0228  0.0119  -0.0022 167 THR B N   
3004 C CA  . THR B 165 ? 0.0981 0.0994 0.0802 0.0258  0.0106  -0.0025 167 THR B CA  
3005 C C   . THR B 165 ? 0.1356 0.1308 0.1150 0.0294  0.0105  -0.0016 167 THR B C   
3006 O O   . THR B 165 ? 0.1629 0.1513 0.1383 0.0289  0.0122  -0.0012 167 THR B O   
3007 C CB  . THR B 165 ? 0.1163 0.1221 0.1020 0.0251  0.0115  -0.0047 167 THR B CB  
3008 O OG1 . THR B 165 ? 0.1238 0.1256 0.1090 0.0260  0.0137  -0.0059 167 THR B OG1 
3009 C CG2 . THR B 165 ? 0.0781 0.0871 0.0643 0.0212  0.0119  -0.0052 167 THR B CG2 
3010 N N   . THR B 166 ? 0.1370 0.1348 0.1184 0.0327  0.0084  -0.0012 168 THR B N   
3011 C CA  . THR B 166 ? 0.1550 0.1476 0.1333 0.0364  0.0068  0.0008  168 THR B CA  
3012 C C   . THR B 166 ? 0.1694 0.1568 0.1480 0.0397  0.0083  0.0004  168 THR B C   
3013 O O   . THR B 166 ? 0.1862 0.1659 0.1600 0.0422  0.0078  0.0024  168 THR B O   
3014 C CB  . THR B 166 ? 0.1498 0.1485 0.1307 0.0387  0.0030  0.0016  168 THR B CB  
3015 O OG1 . THR B 166 ? 0.1838 0.1769 0.1598 0.0415  0.0005  0.0043  168 THR B OG1 
3016 C CG2 . THR B 166 ? 0.1312 0.1376 0.1199 0.0412  0.0025  -0.0003 168 THR B CG2 
3017 N N   . GLU B 167 ? 0.1734 0.1643 0.1570 0.0395  0.0106  -0.0022 169 GLU B N   
3018 C CA  . GLU B 167 ? 0.1810 0.1679 0.1663 0.0431  0.0124  -0.0030 169 GLU B CA  
3019 C C   . GLU B 167 ? 0.1774 0.1638 0.1637 0.0398  0.0166  -0.0060 169 GLU B C   
3020 O O   . GLU B 167 ? 0.1843 0.1779 0.1754 0.0381  0.0173  -0.0083 169 GLU B O   
3021 C CB  . GLU B 167 ? 0.1779 0.1719 0.1707 0.0478  0.0099  -0.0033 169 GLU B CB  
3022 C CG  . GLU B 167 ? 0.2247 0.2156 0.2216 0.0525  0.0119  -0.0044 169 GLU B CG  
3023 C CD  . GLU B 167 ? 0.2663 0.2444 0.2567 0.0551  0.0131  -0.0022 169 GLU B CD  
3024 O OE1 . GLU B 167 ? 0.2757 0.2496 0.2624 0.0585  0.0095  0.0013  169 GLU B OE1 
3025 O OE2 . GLU B 167 ? 0.2524 0.2240 0.2402 0.0531  0.0177  -0.0041 169 GLU B OE2 
3026 N N   . CYS B 168 ? 0.1842 0.1619 0.1650 0.0382  0.0197  -0.0062 170 CYS B N   
3027 C CA  . CYS B 168 ? 0.2171 0.1943 0.1974 0.0337  0.0236  -0.0091 170 CYS B CA  
3028 C C   . CYS B 168 ? 0.2464 0.2246 0.2316 0.0355  0.0265  -0.0120 170 CYS B C   
3029 O O   . CYS B 168 ? 0.2561 0.2357 0.2411 0.0311  0.0295  -0.0148 170 CYS B O   
3030 C CB  . CYS B 168 ? 0.2280 0.1960 0.2011 0.0309  0.0263  -0.0089 170 CYS B CB  
3031 S SG  . CYS B 168 ? 0.3031 0.2584 0.2721 0.0358  0.0287  -0.0079 170 CYS B SG  
3032 N N   . GLU B 169 ? 0.2412 0.2188 0.2308 0.0418  0.0256  -0.0114 171 GLU B N   
3033 C CA  . GLU B 169 ? 0.2497 0.2291 0.2458 0.0441  0.0287  -0.0145 171 GLU B CA  
3034 C C   . GLU B 169 ? 0.2598 0.2509 0.2644 0.0450  0.0269  -0.0162 171 GLU B C   
3035 O O   . GLU B 169 ? 0.2797 0.2735 0.2911 0.0470  0.0297  -0.0192 171 GLU B O   
3036 C CB  . GLU B 169 ? 0.3115 0.2824 0.3081 0.0507  0.0296  -0.0132 171 GLU B CB  
3037 C CG  . GLU B 169 ? 0.3753 0.3339 0.3623 0.0483  0.0326  -0.0124 171 GLU B CG  
3038 C CD  . GLU B 169 ? 0.5163 0.4638 0.5021 0.0534  0.0354  -0.0120 171 GLU B CD  
3039 O OE1 . GLU B 169 ? 0.5197 0.4640 0.5057 0.0596  0.0318  -0.0084 171 GLU B OE1 
3040 O OE2 . GLU B 169 ? 0.5487 0.4899 0.5326 0.0510  0.0413  -0.0150 171 GLU B OE2 
3041 N N   . ASN B 170 ? 0.2198 0.2181 0.2244 0.0431  0.0229  -0.0146 172 ASN B N   
3042 C CA  . ASN B 170 ? 0.2007 0.2098 0.2118 0.0420  0.0219  -0.0168 172 ASN B CA  
3043 C C   . ASN B 170 ? 0.2122 0.2230 0.2210 0.0351  0.0252  -0.0197 172 ASN B C   
3044 O O   . ASN B 170 ? 0.2010 0.2146 0.2063 0.0309  0.0234  -0.0188 172 ASN B O   
3045 C CB  . ASN B 170 ? 0.2344 0.2493 0.2455 0.0424  0.0168  -0.0142 172 ASN B CB  
3046 C CG  . ASN B 170 ? 0.2966 0.3130 0.3110 0.0485  0.0128  -0.0117 172 ASN B CG  
3047 O OD1 . ASN B 170 ? 0.3244 0.3400 0.3440 0.0538  0.0133  -0.0122 172 ASN B OD1 
3048 N ND2 . ASN B 170 ? 0.2943 0.3132 0.3059 0.0480  0.0086  -0.0091 172 ASN B ND2 
3049 N N   . ARG B 171 ? 0.2233 0.2319 0.2337 0.0340  0.0300  -0.0232 173 ARG B N   
3050 C CA  . ARG B 171 ? 0.2518 0.2600 0.2581 0.0270  0.0334  -0.0260 173 ARG B CA  
3051 C C   . ARG B 171 ? 0.2248 0.2408 0.2319 0.0229  0.0321  -0.0270 173 ARG B C   
3052 O O   . ARG B 171 ? 0.2421 0.2573 0.2429 0.0175  0.0314  -0.0261 173 ARG B O   
3053 C CB  . ARG B 171 ? 0.3197 0.3248 0.3286 0.0266  0.0395  -0.0304 173 ARG B CB  
3054 C CG  . ARG B 171 ? 0.4338 0.4390 0.4380 0.0186  0.0431  -0.0337 173 ARG B CG  
3055 C CD  . ARG B 171 ? 0.5336 0.5344 0.5392 0.0175  0.0499  -0.0383 173 ARG B CD  
3056 N NE  . ARG B 171 ? 0.6290 0.6199 0.6288 0.0172  0.0523  -0.0378 173 ARG B NE  
3057 C CZ  . ARG B 171 ? 0.6830 0.6693 0.6736 0.0103  0.0535  -0.0379 173 ARG B CZ  
3058 N NH1 . ARG B 171 ? 0.6732 0.6638 0.6593 0.0038  0.0518  -0.0380 173 ARG B NH1 
3059 N NH2 . ARG B 171 ? 0.6986 0.6760 0.6843 0.0099  0.0561  -0.0378 173 ARG B NH2 
3060 N N   . GLU B 172 ? 0.2067 0.2303 0.2215 0.0253  0.0318  -0.0289 174 GLU B N   
3061 C CA  . GLU B 172 ? 0.2109 0.2413 0.2260 0.0210  0.0312  -0.0303 174 GLU B CA  
3062 C C   . GLU B 172 ? 0.1851 0.2163 0.1955 0.0199  0.0265  -0.0264 174 GLU B C   
3063 O O   . GLU B 172 ? 0.1746 0.2058 0.1797 0.0146  0.0263  -0.0261 174 GLU B O   
3064 C CB  . GLU B 172 ? 0.2751 0.3141 0.2999 0.0237  0.0320  -0.0335 174 GLU B CB  
3065 C CG  . GLU B 172 ? 0.4024 0.4416 0.4319 0.0229  0.0379  -0.0386 174 GLU B CG  
3066 C CD  . GLU B 172 ? 0.5924 0.6371 0.6341 0.0297  0.0387  -0.0407 174 GLU B CD  
3067 O OE1 . GLU B 172 ? 0.6207 0.6600 0.6650 0.0338  0.0410  -0.0410 174 GLU B OE1 
3068 O OE2 . GLU B 172 ? 0.6362 0.6907 0.6853 0.0310  0.0368  -0.0420 174 GLU B OE2 
3069 N N   . ALA B 173 ? 0.1747 0.2062 0.1868 0.0247  0.0228  -0.0232 175 ALA B N   
3070 C CA  . ALA B 173 ? 0.1789 0.2105 0.1869 0.0237  0.0191  -0.0198 175 ALA B CA  
3071 C C   . ALA B 173 ? 0.1634 0.1888 0.1641 0.0202  0.0192  -0.0179 175 ALA B C   
3072 O O   . ALA B 173 ? 0.1645 0.1906 0.1617 0.0165  0.0180  -0.0168 175 ALA B O   
3073 C CB  . ALA B 173 ? 0.1813 0.2130 0.1912 0.0291  0.0157  -0.0171 175 ALA B CB  
3074 N N   . VAL B 174 ? 0.1304 0.1496 0.1289 0.0213  0.0205  -0.0174 176 VAL B N   
3075 C CA  . VAL B 174 ? 0.1349 0.1494 0.1276 0.0181  0.0203  -0.0156 176 VAL B CA  
3076 C C   . VAL B 174 ? 0.1422 0.1578 0.1316 0.0122  0.0216  -0.0171 176 VAL B C   
3077 O O   . VAL B 174 ? 0.1339 0.1494 0.1199 0.0094  0.0196  -0.0151 176 VAL B O   
3078 C CB  . VAL B 174 ? 0.1500 0.1574 0.1406 0.0197  0.0223  -0.0156 176 VAL B CB  
3079 C CG1 . VAL B 174 ? 0.1840 0.1881 0.1693 0.0152  0.0229  -0.0150 176 VAL B CG1 
3080 C CG2 . VAL B 174 ? 0.1363 0.1409 0.1275 0.0249  0.0204  -0.0131 176 VAL B CG2 
3081 N N   . THR B 175 ? 0.1531 0.1694 0.1436 0.0105  0.0249  -0.0205 177 THR B N   
3082 C CA  . THR B 175 ? 0.1761 0.1921 0.1618 0.0042  0.0263  -0.0220 177 THR B CA  
3083 C C   . THR B 175 ? 0.1654 0.1856 0.1502 0.0019  0.0240  -0.0211 177 THR B C   
3084 O O   . THR B 175 ? 0.1606 0.1796 0.1400 -0.0022 0.0224  -0.0194 177 THR B O   
3085 C CB  . THR B 175 ? 0.2217 0.2362 0.2077 0.0021  0.0313  -0.0263 177 THR B CB  
3086 O OG1 . THR B 175 ? 0.3339 0.3530 0.3264 0.0045  0.0330  -0.0290 177 THR B OG1 
3087 C CG2 . THR B 175 ? 0.1792 0.1882 0.1649 0.0038  0.0338  -0.0270 177 THR B CG2 
3088 N N   . HIS B 176 ? 0.1697 0.1945 0.1594 0.0045  0.0237  -0.0220 178 HIS B N   
3089 C CA  . HIS B 176 ? 0.1544 0.1821 0.1426 0.0022  0.0221  -0.0212 178 HIS B CA  
3090 C C   . HIS B 176 ? 0.1394 0.1653 0.1246 0.0027  0.0184  -0.0170 178 HIS B C   
3091 O O   . HIS B 176 ? 0.1295 0.1541 0.1101 -0.0008 0.0171  -0.0155 178 HIS B O   
3092 C CB  . HIS B 176 ? 0.1714 0.2050 0.1657 0.0048  0.0223  -0.0231 178 HIS B CB  
3093 C CG  . HIS B 176 ? 0.2028 0.2386 0.1947 0.0017  0.0214  -0.0229 178 HIS B CG  
3094 N ND1 . HIS B 176 ? 0.2545 0.2899 0.2422 -0.0040 0.0239  -0.0253 178 HIS B ND1 
3095 C CD2 . HIS B 176 ? 0.2076 0.2446 0.1994 0.0029  0.0189  -0.0206 178 HIS B CD2 
3096 C CE1 . HIS B 176 ? 0.2336 0.2698 0.2190 -0.0056 0.0226  -0.0242 178 HIS B CE1 
3097 N NE2 . HIS B 176 ? 0.1973 0.2347 0.1854 -0.0016 0.0198  -0.0217 178 HIS B NE2 
3098 N N   . ILE B 177 ? 0.1336 0.1586 0.1212 0.0070  0.0166  -0.0148 179 ILE B N   
3099 C CA  . ILE B 177 ? 0.1135 0.1368 0.0993 0.0074  0.0139  -0.0114 179 ILE B CA  
3100 C C   . ILE B 177 ? 0.1263 0.1469 0.1079 0.0040  0.0133  -0.0100 179 ILE B C   
3101 O O   . ILE B 177 ? 0.1365 0.1567 0.1160 0.0024  0.0113  -0.0078 179 ILE B O   
3102 C CB  . ILE B 177 ? 0.1126 0.1346 0.1008 0.0118  0.0130  -0.0100 179 ILE B CB  
3103 C CG1 . ILE B 177 ? 0.1027 0.1281 0.0944 0.0149  0.0124  -0.0106 179 ILE B CG1 
3104 C CG2 . ILE B 177 ? 0.1101 0.1298 0.0967 0.0117  0.0111  -0.0070 179 ILE B CG2 
3105 C CD1 . ILE B 177 ? 0.1288 0.1523 0.1220 0.0191  0.0115  -0.0095 179 ILE B CD1 
3106 N N   . GLY B 178 ? 0.1213 0.1399 0.1017 0.0028  0.0148  -0.0113 180 GLY B N   
3107 C CA  . GLY B 178 ? 0.1219 0.1388 0.0983 -0.0009 0.0137  -0.0100 180 GLY B CA  
3108 C C   . GLY B 178 ? 0.1399 0.1571 0.1118 -0.0055 0.0129  -0.0098 180 GLY B C   
3109 O O   . GLY B 178 ? 0.1453 0.1624 0.1148 -0.0072 0.0100  -0.0070 180 GLY B O   
3110 N N   . ARG B 179 ? 0.1314 0.1490 0.1019 -0.0076 0.0156  -0.0128 181 ARG B N   
3111 C CA  . ARG B 179 ? 0.1542 0.1709 0.1186 -0.0128 0.0153  -0.0129 181 ARG B CA  
3112 C C   . ARG B 179 ? 0.1504 0.1671 0.1138 -0.0122 0.0124  -0.0098 181 ARG B C   
3113 O O   . ARG B 179 ? 0.1600 0.1747 0.1185 -0.0148 0.0096  -0.0070 181 ARG B O   
3114 C CB  . ARG B 179 ? 0.1896 0.2067 0.1535 -0.0153 0.0196  -0.0174 181 ARG B CB  
3115 C CG  . ARG B 179 ? 0.2546 0.2700 0.2178 -0.0171 0.0230  -0.0205 181 ARG B CG  
3116 C CD  . ARG B 179 ? 0.3246 0.3401 0.2863 -0.0208 0.0274  -0.0249 181 ARG B CD  
3117 N NE  . ARG B 179 ? 0.3794 0.3936 0.3430 -0.0212 0.0322  -0.0290 181 ARG B NE  
3118 C CZ  . ARG B 179 ? 0.4092 0.4195 0.3674 -0.0255 0.0339  -0.0301 181 ARG B CZ  
3119 N NH1 . ARG B 179 ? 0.4342 0.4426 0.3945 -0.0255 0.0391  -0.0342 181 ARG B NH1 
3120 N NH2 . ARG B 179 ? 0.3540 0.3623 0.3047 -0.0297 0.0305  -0.0270 181 ARG B NH2 
3121 N N   . VAL B 180 ? 0.1475 0.1663 0.1155 -0.0086 0.0128  -0.0102 182 VAL B N   
3122 C CA  . VAL B 180 ? 0.1395 0.1577 0.1067 -0.0081 0.0110  -0.0078 182 VAL B CA  
3123 C C   . VAL B 180 ? 0.1334 0.1503 0.1016 -0.0058 0.0077  -0.0037 182 VAL B C   
3124 O O   . VAL B 180 ? 0.1370 0.1516 0.1021 -0.0069 0.0057  -0.0010 182 VAL B O   
3125 C CB  . VAL B 180 ? 0.1634 0.1846 0.1349 -0.0055 0.0126  -0.0096 182 VAL B CB  
3126 C CG1 . VAL B 180 ? 0.1953 0.2150 0.1654 -0.0052 0.0113  -0.0074 182 VAL B CG1 
3127 C CG2 . VAL B 180 ? 0.1637 0.1875 0.1355 -0.0079 0.0158  -0.0139 182 VAL B CG2 
3128 N N   . TYR B 181 ? 0.1169 0.1350 0.0893 -0.0029 0.0073  -0.0033 183 TYR B N   
3129 C CA  . TYR B 181 ? 0.1299 0.1475 0.1044 -0.0010 0.0047  -0.0001 183 TYR B CA  
3130 C C   . TYR B 181 ? 0.1461 0.1630 0.1172 -0.0041 0.0020  0.0021  183 TYR B C   
3131 O O   . TYR B 181 ? 0.1248 0.1409 0.0960 -0.0034 -0.0007 0.0053  183 TYR B O   
3132 C CB  . TYR B 181 ? 0.1276 0.1461 0.1062 0.0017  0.0056  -0.0009 183 TYR B CB  
3133 C CG  . TYR B 181 ? 0.1159 0.1346 0.0979 0.0036  0.0039  0.0014  183 TYR B CG  
3134 C CD1 . TYR B 181 ? 0.1323 0.1506 0.1160 0.0050  0.0025  0.0038  183 TYR B CD1 
3135 C CD2 . TYR B 181 ? 0.1230 0.1419 0.1067 0.0039  0.0044  0.0009  183 TYR B CD2 
3136 C CE1 . TYR B 181 ? 0.1285 0.1473 0.1167 0.0070  0.0017  0.0053  183 TYR B CE1 
3137 C CE2 . TYR B 181 ? 0.1151 0.1346 0.1025 0.0054  0.0036  0.0023  183 TYR B CE2 
3138 C CZ  . TYR B 181 ? 0.1377 0.1577 0.1279 0.0069  0.0022  0.0045  183 TYR B CZ  
3139 O OH  . TYR B 181 ? 0.1486 0.1695 0.1435 0.0083  0.0021  0.0053  183 TYR B OH  
3140 N N   . LYS B 182 ? 0.1458 0.1628 0.1135 -0.0075 0.0027  0.0004  184 LYS B N   
3141 C CA  . LYS B 182 ? 0.1480 0.1645 0.1108 -0.0115 -0.0001 0.0022  184 LYS B CA  
3142 C C   . LYS B 182 ? 0.1704 0.1840 0.1277 -0.0136 -0.0020 0.0044  184 LYS B C   
3143 O O   . LYS B 182 ? 0.1661 0.1792 0.1220 -0.0139 -0.0060 0.0081  184 LYS B O   
3144 C CB  . LYS B 182 ? 0.1679 0.1839 0.1266 -0.0157 0.0020  -0.0008 184 LYS B CB  
3145 C CG  . LYS B 182 ? 0.1740 0.1897 0.1265 -0.0209 -0.0010 0.0009  184 LYS B CG  
3146 C CD  . LYS B 182 ? 0.1842 0.1999 0.1338 -0.0248 0.0011  -0.0020 184 LYS B CD  
3147 C CE  . LYS B 182 ? 0.1910 0.2056 0.1319 -0.0315 -0.0015 -0.0009 184 LYS B CE  
3148 N NZ  . LYS B 182 ? 0.2021 0.2164 0.1397 -0.0360 0.0011  -0.0042 184 LYS B NZ  
3149 N N   . GLU B 183 ? 0.1681 0.1798 0.1222 -0.0151 0.0009  0.0021  185 GLU B N   
3150 C CA  . GLU B 183 ? 0.1956 0.2033 0.1432 -0.0176 0.0002  0.0036  185 GLU B CA  
3151 C C   . GLU B 183 ? 0.2009 0.2072 0.1512 -0.0138 -0.0022 0.0073  185 GLU B C   
3152 O O   . GLU B 183 ? 0.2101 0.2129 0.1561 -0.0148 -0.0053 0.0110  185 GLU B O   
3153 C CB  . GLU B 183 ? 0.2363 0.2438 0.1822 -0.0197 0.0049  -0.0009 185 GLU B CB  
3154 C CG  . GLU B 183 ? 0.3566 0.3604 0.2970 -0.0222 0.0061  -0.0010 185 GLU B CG  
3155 C CD  . GLU B 183 ? 0.3242 0.3312 0.2679 -0.0224 0.0108  -0.0061 185 GLU B CD  
3156 O OE1 . GLU B 183 ? 0.3594 0.3658 0.3033 -0.0220 0.0120  -0.0065 185 GLU B OE1 
3157 O OE2 . GLU B 183 ? 0.3424 0.3525 0.2888 -0.0230 0.0134  -0.0097 185 GLU B OE2 
3158 N N   . ARG B 184 ? 0.1823 0.1908 0.1399 -0.0093 -0.0006 0.0065  186 ARG B N   
3159 C CA  . ARG B 184 ? 0.1793 0.1861 0.1400 -0.0057 -0.0018 0.0094  186 ARG B CA  
3160 C C   . ARG B 184 ? 0.1973 0.2051 0.1622 -0.0032 -0.0056 0.0131  186 ARG B C   
3161 O O   . ARG B 184 ? 0.2215 0.2264 0.1870 -0.0013 -0.0074 0.0164  186 ARG B O   
3162 C CB  . ARG B 184 ? 0.1647 0.1736 0.1310 -0.0026 0.0011  0.0070  186 ARG B CB  
3163 C CG  . ARG B 184 ? 0.2178 0.2262 0.1810 -0.0047 0.0042  0.0039  186 ARG B CG  
3164 C CD  . ARG B 184 ? 0.2317 0.2351 0.1901 -0.0061 0.0047  0.0052  186 ARG B CD  
3165 N NE  . ARG B 184 ? 0.1946 0.1968 0.1572 -0.0025 0.0047  0.0070  186 ARG B NE  
3166 C CZ  . ARG B 184 ? 0.1723 0.1751 0.1367 -0.0016 0.0072  0.0051  186 ARG B CZ  
3167 N NH1 . ARG B 184 ? 0.1754 0.1812 0.1389 -0.0037 0.0095  0.0014  186 ARG B NH1 
3168 N NH2 . ARG B 184 ? 0.2004 0.2013 0.1679 0.0011  0.0075  0.0066  186 ARG B NH2 
3169 N N   . LEU B 185 ? 0.1828 0.1947 0.1510 -0.0032 -0.0067 0.0126  187 LEU B N   
3170 C CA  . LEU B 185 ? 0.1651 0.1794 0.1373 -0.0018 -0.0105 0.0157  187 LEU B CA  
3171 C C   . LEU B 185 ? 0.2188 0.2313 0.1848 -0.0049 -0.0148 0.0190  187 LEU B C   
3172 O O   . LEU B 185 ? 0.2423 0.2566 0.2120 -0.0030 -0.0190 0.0226  187 LEU B O   
3173 C CB  . LEU B 185 ? 0.1559 0.1749 0.1320 -0.0022 -0.0100 0.0136  187 LEU B CB  
3174 C CG  . LEU B 185 ? 0.1726 0.1930 0.1549 0.0011  -0.0067 0.0113  187 LEU B CG  
3175 C CD1 . LEU B 185 ? 0.1875 0.2104 0.1705 -0.0005 -0.0056 0.0088  187 LEU B CD1 
3176 C CD2 . LEU B 185 ? 0.1786 0.1998 0.1680 0.0050  -0.0074 0.0132  187 LEU B CD2 
3177 N N   . GLY B 186 ? 0.2249 0.2342 0.1818 -0.0095 -0.0140 0.0178  188 GLY B N   
3178 C CA  . GLY B 186 ? 0.2248 0.2312 0.1736 -0.0133 -0.0181 0.0209  188 GLY B CA  
3179 C C   . GLY B 186 ? 0.2160 0.2267 0.1641 -0.0163 -0.0212 0.0212  188 GLY B C   
3180 O O   . GLY B 186 ? 0.2206 0.2309 0.1648 -0.0179 -0.0264 0.0251  188 GLY B O   
3181 N N   . LEU B 187 ? 0.2039 0.2187 0.1553 -0.0171 -0.0182 0.0173  189 LEU B N   
3182 C CA  . LEU B 187 ? 0.2018 0.2208 0.1527 -0.0204 -0.0206 0.0171  189 LEU B CA  
3183 C C   . LEU B 187 ? 0.2287 0.2442 0.1677 -0.0275 -0.0208 0.0163  189 LEU B C   
3184 O O   . LEU B 187 ? 0.2346 0.2458 0.1682 -0.0299 -0.0164 0.0132  189 LEU B O   
3185 C CB  . LEU B 187 ? 0.2082 0.2305 0.1643 -0.0199 -0.0166 0.0129  189 LEU B CB  
3186 C CG  . LEU B 187 ? 0.2248 0.2500 0.1916 -0.0138 -0.0152 0.0128  189 LEU B CG  
3187 C CD1 . LEU B 187 ? 0.2322 0.2588 0.2017 -0.0141 -0.0112 0.0087  189 LEU B CD1 
3188 C CD2 . LEU B 187 ? 0.2394 0.2692 0.2129 -0.0114 -0.0200 0.0163  189 LEU B CD2 
3189 N N   . PRO B 188 ? 0.2284 0.2458 0.1634 -0.0312 -0.0258 0.0189  190 PRO B N   
3190 C CA  . PRO B 188 ? 0.2294 0.2435 0.1521 -0.0391 -0.0256 0.0175  190 PRO B CA  
3191 C C   . PRO B 188 ? 0.1903 0.2040 0.1118 -0.0424 -0.0188 0.0113  190 PRO B C   
3192 O O   . PRO B 188 ? 0.1893 0.2069 0.1187 -0.0396 -0.0166 0.0090  190 PRO B O   
3193 C CB  . PRO B 188 ? 0.2592 0.2780 0.1809 -0.0418 -0.0324 0.0210  190 PRO B CB  
3194 C CG  . PRO B 188 ? 0.2650 0.2876 0.1967 -0.0347 -0.0374 0.0258  190 PRO B CG  
3195 C CD  . PRO B 188 ? 0.2469 0.2702 0.1885 -0.0286 -0.0321 0.0230  190 PRO B CD  
3196 N N   . PRO B 189 ? 0.1994 0.2079 0.1109 -0.0482 -0.0153 0.0084  191 PRO B N   
3197 C CA  . PRO B 189 ? 0.1838 0.1916 0.0947 -0.0511 -0.0085 0.0022  191 PRO B CA  
3198 C C   . PRO B 189 ? 0.1783 0.1900 0.0915 -0.0530 -0.0084 0.0006  191 PRO B C   
3199 O O   . PRO B 189 ? 0.1994 0.2116 0.1179 -0.0511 -0.0032 -0.0033 191 PRO B O   
3200 C CB  . PRO B 189 ? 0.1878 0.1897 0.0861 -0.0588 -0.0061 0.0003  191 PRO B CB  
3201 C CG  . PRO B 189 ? 0.1979 0.1962 0.0926 -0.0572 -0.0093 0.0043  191 PRO B CG  
3202 C CD  . PRO B 189 ? 0.2034 0.2056 0.1035 -0.0526 -0.0166 0.0101  191 PRO B CD  
3203 N N   . LYS B 190 ? 0.1808 0.1953 0.0901 -0.0569 -0.0142 0.0037  192 LYS B N   
3204 C CA  . LYS B 190 ? 0.1865 0.2049 0.0969 -0.0601 -0.0140 0.0018  192 LYS B CA  
3205 C C   . LYS B 190 ? 0.1959 0.2199 0.1188 -0.0538 -0.0140 0.0018  192 LYS B C   
3206 O O   . LYS B 190 ? 0.2193 0.2453 0.1433 -0.0564 -0.0119 -0.0010 192 LYS B O   
3207 C CB  . LYS B 190 ? 0.2120 0.2331 0.1149 -0.0664 -0.0208 0.0051  192 LYS B CB  
3208 C CG  . LYS B 190 ? 0.2442 0.2709 0.1540 -0.0611 -0.0291 0.0114  192 LYS B CG  
3209 C CD  . LYS B 190 ? 0.3286 0.3588 0.2317 -0.0667 -0.0372 0.0156  192 LYS B CD  
3210 C CE  . LYS B 190 ? 0.4096 0.4457 0.3127 -0.0720 -0.0375 0.0130  192 LYS B CE  
3211 N NZ  . LYS B 190 ? 0.4811 0.5227 0.3796 -0.0768 -0.0467 0.0175  192 LYS B NZ  
3212 N N   . ILE B 191 ? 0.1930 0.2186 0.1245 -0.0463 -0.0158 0.0047  193 ILE B N   
3213 C CA  . ILE B 191 ? 0.2032 0.2332 0.1461 -0.0404 -0.0152 0.0046  193 ILE B CA  
3214 C C   . ILE B 191 ? 0.1943 0.2203 0.1398 -0.0372 -0.0083 0.0006  193 ILE B C   
3215 O O   . ILE B 191 ? 0.2036 0.2273 0.1515 -0.0328 -0.0069 0.0010  193 ILE B O   
3216 C CB  . ILE B 191 ? 0.2304 0.2635 0.1809 -0.0342 -0.0201 0.0093  193 ILE B CB  
3217 C CG1 . ILE B 191 ? 0.2650 0.3022 0.2136 -0.0365 -0.0278 0.0140  193 ILE B CG1 
3218 C CG2 . ILE B 191 ? 0.2296 0.2669 0.1916 -0.0288 -0.0186 0.0085  193 ILE B CG2 
3219 C CD1 . ILE B 191 ? 0.2965 0.3399 0.2459 -0.0407 -0.0306 0.0135  193 ILE B CD1 
3220 N N   . VAL B 192 ? 0.2065 0.2317 0.1514 -0.0396 -0.0042 -0.0032 194 VAL B N   
3221 C CA  . VAL B 192 ? 0.2467 0.2675 0.1933 -0.0370 0.0024  -0.0070 194 VAL B CA  
3222 C C   . VAL B 192 ? 0.2391 0.2615 0.1947 -0.0302 0.0026  -0.0061 194 VAL B C   
3223 O O   . VAL B 192 ? 0.2392 0.2656 0.1989 -0.0300 0.0003  -0.0049 194 VAL B O   
3224 C CB  . VAL B 192 ? 0.3064 0.3244 0.2477 -0.0426 0.0067  -0.0112 194 VAL B CB  
3225 C CG1 . VAL B 192 ? 0.3494 0.3626 0.2933 -0.0391 0.0131  -0.0147 194 VAL B CG1 
3226 C CG2 . VAL B 192 ? 0.3326 0.3481 0.2639 -0.0500 0.0073  -0.0126 194 VAL B CG2 
3227 N N   . ILE B 193 ? 0.2108 0.2303 0.1695 -0.0251 0.0054  -0.0068 195 ILE B N   
3228 C CA  . ILE B 193 ? 0.2005 0.2200 0.1658 -0.0195 0.0065  -0.0065 195 ILE B CA  
3229 C C   . ILE B 193 ? 0.1793 0.1937 0.1438 -0.0182 0.0120  -0.0099 195 ILE B C   
3230 O O   . ILE B 193 ? 0.1787 0.1904 0.1400 -0.0195 0.0147  -0.0121 195 ILE B O   
3231 C CB  . ILE B 193 ? 0.2029 0.2236 0.1727 -0.0145 0.0044  -0.0038 195 ILE B CB  
3232 C CG1 . ILE B 193 ? 0.1960 0.2139 0.1642 -0.0128 0.0067  -0.0051 195 ILE B CG1 
3233 C CG2 . ILE B 193 ? 0.2157 0.2402 0.1862 -0.0155 -0.0008 -0.0003 195 ILE B CG2 
3234 C CD1 . ILE B 193 ? 0.2181 0.2366 0.1901 -0.0084 0.0058  -0.0034 195 ILE B CD1 
3235 N N   . GLY B 194 ? 0.1756 0.1885 0.1432 -0.0155 0.0136  -0.0103 196 GLY B N   
3236 C CA  . GLY B 194 ? 0.1702 0.1772 0.1363 -0.0141 0.0184  -0.0130 196 GLY B CA  
3237 C C   . GLY B 194 ? 0.1796 0.1842 0.1495 -0.0080 0.0191  -0.0121 196 GLY B C   
3238 O O   . GLY B 194 ? 0.1842 0.1915 0.1578 -0.0057 0.0167  -0.0099 196 GLY B O   
3239 N N   . TYR B 195 ? 0.1777 0.1774 0.1468 -0.0054 0.0225  -0.0139 197 TYR B N   
3240 C CA  . TYR B 195 ? 0.1808 0.1773 0.1522 0.0002  0.0231  -0.0130 197 TYR B CA  
3241 C C   . TYR B 195 ? 0.2082 0.1974 0.1765 0.0004  0.0267  -0.0144 197 TYR B C   
3242 O O   . TYR B 195 ? 0.2142 0.1994 0.1795 -0.0018 0.0302  -0.0169 197 TYR B O   
3243 C CB  . TYR B 195 ? 0.1755 0.1724 0.1491 0.0038  0.0236  -0.0136 197 TYR B CB  
3244 C CG  . TYR B 195 ? 0.1690 0.1640 0.1450 0.0096  0.0230  -0.0122 197 TYR B CG  
3245 C CD1 . TYR B 195 ? 0.1855 0.1741 0.1605 0.0127  0.0255  -0.0130 197 TYR B CD1 
3246 C CD2 . TYR B 195 ? 0.1361 0.1351 0.1149 0.0118  0.0198  -0.0101 197 TYR B CD2 
3247 C CE1 . TYR B 195 ? 0.1821 0.1689 0.1585 0.0179  0.0242  -0.0113 197 TYR B CE1 
3248 C CE2 . TYR B 195 ? 0.1170 0.1143 0.0970 0.0164  0.0189  -0.0088 197 TYR B CE2 
3249 C CZ  . TYR B 195 ? 0.1535 0.1451 0.1323 0.0195  0.0208  -0.0092 197 TYR B CZ  
3250 O OH  . TYR B 195 ? 0.1799 0.1695 0.1590 0.0239  0.0193  -0.0076 197 TYR B OH  
3251 N N   . GLN B 196 ? 0.2110 0.1977 0.1795 0.0027  0.0263  -0.0129 198 GLN B N   
3252 C CA  . GLN B 196 ? 0.2507 0.2291 0.2152 0.0030  0.0297  -0.0138 198 GLN B CA  
3253 C C   . GLN B 196 ? 0.2331 0.2072 0.1976 0.0084  0.0290  -0.0118 198 GLN B C   
3254 O O   . GLN B 196 ? 0.1844 0.1623 0.1514 0.0099  0.0261  -0.0098 198 GLN B O   
3255 C CB  . GLN B 196 ? 0.3136 0.2924 0.2762 -0.0020 0.0305  -0.0146 198 GLN B CB  
3256 C CG  . GLN B 196 ? 0.4447 0.4141 0.4015 -0.0037 0.0352  -0.0165 198 GLN B CG  
3257 C CD  . GLN B 196 ? 0.5723 0.5399 0.5254 -0.0089 0.0385  -0.0196 198 GLN B CD  
3258 O OE1 . GLN B 196 ? 0.5939 0.5622 0.5472 -0.0090 0.0392  -0.0207 198 GLN B OE1 
3259 N NE2 . GLN B 196 ? 0.6174 0.5825 0.5668 -0.0140 0.0411  -0.0214 198 GLN B NE2 
3260 N N   . SER B 197 ? 0.2314 0.1966 0.1925 0.0112  0.0319  -0.0123 199 SER B N   
3261 C CA  . SER B 197 ? 0.2287 0.1885 0.1881 0.0159  0.0310  -0.0100 199 SER B CA  
3262 C C   . SER B 197 ? 0.2196 0.1762 0.1753 0.0135  0.0314  -0.0093 199 SER B C   
3263 O O   . SER B 197 ? 0.2172 0.1733 0.1711 0.0086  0.0336  -0.0111 199 SER B O   
3264 C CB  . SER B 197 ? 0.2427 0.1931 0.1991 0.0198  0.0335  -0.0102 199 SER B CB  
3265 O OG  . SER B 197 ? 0.2609 0.2028 0.2112 0.0163  0.0379  -0.0119 199 SER B OG  
3266 N N   . HIS B 198 ? 0.2022 0.1569 0.1568 0.0164  0.0293  -0.0070 200 HIS B N   
3267 C CA  . HIS B 198 ? 0.2200 0.1706 0.1706 0.0138  0.0305  -0.0066 200 HIS B CA  
3268 C C   . HIS B 198 ? 0.2587 0.1977 0.2016 0.0122  0.0348  -0.0078 200 HIS B C   
3269 O O   . HIS B 198 ? 0.2480 0.1855 0.1885 0.0074  0.0374  -0.0093 200 HIS B O   
3270 C CB  . HIS B 198 ? 0.2234 0.1725 0.1725 0.0170  0.0279  -0.0040 200 HIS B CB  
3271 C CG  . HIS B 198 ? 0.2221 0.1817 0.1779 0.0177  0.0244  -0.0033 200 HIS B CG  
3272 N ND1 . HIS B 198 ? 0.2189 0.1864 0.1798 0.0145  0.0241  -0.0044 200 HIS B ND1 
3273 C CD2 . HIS B 198 ? 0.2195 0.1819 0.1769 0.0212  0.0212  -0.0015 200 HIS B CD2 
3274 C CE1 . HIS B 198 ? 0.2190 0.1930 0.1842 0.0161  0.0212  -0.0032 200 HIS B CE1 
3275 N NE2 . HIS B 198 ? 0.1983 0.1697 0.1614 0.0198  0.0195  -0.0017 200 HIS B NE2 
3276 N N   . ALA B 199 ? 0.3022 0.2334 0.2418 0.0159  0.0360  -0.0072 201 ALA B N   
3277 C CA  . ALA B 199 ? 0.3457 0.2642 0.2773 0.0145  0.0406  -0.0082 201 ALA B CA  
3278 C C   . ALA B 199 ? 0.3595 0.2798 0.2909 0.0081  0.0444  -0.0119 201 ALA B C   
3279 O O   . ALA B 199 ? 0.3714 0.2848 0.2967 0.0037  0.0482  -0.0134 201 ALA B O   
3280 C CB  . ALA B 199 ? 0.3613 0.2726 0.2916 0.0203  0.0410  -0.0071 201 ALA B CB  
3281 N N   . ASP B 200 ? 0.3519 0.2815 0.2895 0.0068  0.0434  -0.0134 202 ASP B N   
3282 C CA  . ASP B 200 ? 0.3559 0.2884 0.2931 0.0003  0.0462  -0.0166 202 ASP B CA  
3283 C C   . ASP B 200 ? 0.3557 0.2961 0.2954 -0.0047 0.0449  -0.0173 202 ASP B C   
3284 O O   . ASP B 200 ? 0.3804 0.3192 0.3171 -0.0105 0.0481  -0.0198 202 ASP B O   
3285 C CB  . ASP B 200 ? 0.3740 0.3130 0.3157 0.0002  0.0455  -0.0179 202 ASP B CB  
3286 C CG  . ASP B 200 ? 0.4136 0.3438 0.3528 0.0035  0.0489  -0.0188 202 ASP B CG  
3287 O OD1 . ASP B 200 ? 0.4511 0.3691 0.3839 0.0045  0.0525  -0.0189 202 ASP B OD1 
3288 O OD2 . ASP B 200 ? 0.4140 0.3488 0.3576 0.0051  0.0482  -0.0195 202 ASP B OD2 
3289 N N   . THR B 201 ? 0.3100 0.2588 0.2556 -0.0027 0.0406  -0.0152 203 THR B N   
3290 C CA  . THR B 201 ? 0.2989 0.2549 0.2483 -0.0064 0.0396  -0.0157 203 THR B CA  
3291 C C   . THR B 201 ? 0.3127 0.2605 0.2563 -0.0089 0.0433  -0.0168 203 THR B C   
3292 O O   . THR B 201 ? 0.3103 0.2631 0.2564 -0.0136 0.0444  -0.0187 203 THR B O   
3293 C CB  . THR B 201 ? 0.3342 0.2975 0.2897 -0.0028 0.0352  -0.0132 203 THR B CB  
3294 O OG1 . THR B 201 ? 0.3603 0.3303 0.3200 -0.0012 0.0323  -0.0125 203 THR B OG1 
3295 C CG2 . THR B 201 ? 0.3371 0.3077 0.2978 -0.0056 0.0344  -0.0136 203 THR B CG2 
3296 N N   . ALA B 202 ? 0.3019 0.2375 0.2380 -0.0059 0.0453  -0.0156 204 ALA B N   
3297 C CA  . ALA B 202 ? 0.3062 0.2323 0.2351 -0.0086 0.0491  -0.0164 204 ALA B CA  
3298 C C   . ALA B 202 ? 0.2991 0.2210 0.2235 -0.0151 0.0542  -0.0201 204 ALA B C   
3299 O O   . ALA B 202 ? 0.2808 0.1989 0.2015 -0.0194 0.0575  -0.0219 204 ALA B O   
3300 C CB  . ALA B 202 ? 0.3247 0.2375 0.2452 -0.0038 0.0494  -0.0137 204 ALA B CB  
3301 N N   . THR B 203 ? 0.2986 0.2210 0.2229 -0.0164 0.0553  -0.0216 205 THR B N   
3302 C CA  . THR B 203 ? 0.3395 0.2563 0.2579 -0.0229 0.0607  -0.0253 205 THR B CA  
3303 C C   . THR B 203 ? 0.3334 0.2601 0.2564 -0.0273 0.0602  -0.0278 205 THR B C   
3304 O O   . THR B 203 ? 0.3153 0.2387 0.2337 -0.0335 0.0645  -0.0312 205 THR B O   
3305 C CB  . THR B 203 ? 0.3938 0.2930 0.3015 -0.0210 0.0653  -0.0252 205 THR B CB  
3306 O OG1 . THR B 203 ? 0.4363 0.3351 0.3457 -0.0170 0.0645  -0.0245 205 THR B OG1 
3307 C CG2 . THR B 203 ? 0.4000 0.2877 0.3013 -0.0162 0.0652  -0.0220 205 THR B CG2 
3308 N N   . LYS B 204 ? 0.3321 0.2703 0.2631 -0.0248 0.0551  -0.0262 206 LYS B N   
3309 C CA  . LYS B 204 ? 0.3727 0.3191 0.3063 -0.0291 0.0542  -0.0281 206 LYS B CA  
3310 C C   . LYS B 204 ? 0.3821 0.3437 0.3251 -0.0297 0.0485  -0.0269 206 LYS B C   
3311 O O   . LYS B 204 ? 0.4198 0.3846 0.3675 -0.0243 0.0449  -0.0239 206 LYS B O   
3312 C CB  . LYS B 204 ? 0.4194 0.3616 0.3513 -0.0257 0.0546  -0.0277 206 LYS B CB  
3313 C CG  . LYS B 204 ? 0.5081 0.4347 0.4323 -0.0227 0.0595  -0.0279 206 LYS B CG  
3314 C CD  . LYS B 204 ? 0.5939 0.5171 0.5179 -0.0195 0.0606  -0.0281 206 LYS B CD  
3315 C CE  . LYS B 204 ? 0.6553 0.5622 0.5720 -0.0165 0.0659  -0.0285 206 LYS B CE  
3316 N NZ  . LYS B 204 ? 0.7038 0.6082 0.6232 -0.0104 0.0659  -0.0277 206 LYS B NZ  
3317 N N   . THR B 209 ? 0.5016 0.5097 0.4519 -0.0393 0.0225  -0.0205 211 THR B N   
3318 C CA  . THR B 209 ? 0.5186 0.5249 0.4616 -0.0454 0.0241  -0.0227 211 THR B CA  
3319 C C   . THR B 209 ? 0.5261 0.5227 0.4649 -0.0453 0.0315  -0.0266 211 THR B C   
3320 O O   . THR B 209 ? 0.5223 0.5160 0.4580 -0.0462 0.0337  -0.0281 211 THR B O   
3321 C CB  . THR B 209 ? 0.5576 0.5693 0.4970 -0.0534 0.0216  -0.0233 211 THR B CB  
3322 O OG1 . THR B 209 ? 0.5824 0.5914 0.5132 -0.0601 0.0234  -0.0256 211 THR B OG1 
3323 C CG2 . THR B 209 ? 0.5694 0.5799 0.5088 -0.0560 0.0247  -0.0257 211 THR B CG2 
3324 N N   . LYS B 210 ? 0.5231 0.5141 0.4618 -0.0441 0.0357  -0.0283 212 LYS B N   
3325 C CA  . LYS B 210 ? 0.5283 0.5089 0.4639 -0.0426 0.0427  -0.0314 212 LYS B CA  
3326 C C   . LYS B 210 ? 0.5135 0.4901 0.4543 -0.0333 0.0434  -0.0298 212 LYS B C   
3327 O O   . LYS B 210 ? 0.5376 0.5056 0.4769 -0.0307 0.0486  -0.0317 212 LYS B O   
3328 C CB  . LYS B 210 ? 0.5807 0.5555 0.5113 -0.0471 0.0473  -0.0343 212 LYS B CB  
3329 C CG  . LYS B 210 ? 0.6615 0.6351 0.5952 -0.0437 0.0470  -0.0329 212 LYS B CG  
3330 C CD  . LYS B 210 ? 0.7362 0.7059 0.6640 -0.0508 0.0512  -0.0362 212 LYS B CD  
3331 C CE  . LYS B 210 ? 0.8141 0.7763 0.7414 -0.0478 0.0545  -0.0364 212 LYS B CE  
3332 N NZ  . LYS B 210 ? 0.8596 0.8162 0.7798 -0.0553 0.0599  -0.0403 212 LYS B NZ  
3333 N N   . ASN B 211 ? 0.4562 0.4391 0.4030 -0.0285 0.0381  -0.0262 213 ASN B N   
3334 C CA  . ASN B 211 ? 0.4182 0.3990 0.3698 -0.0203 0.0376  -0.0242 213 ASN B CA  
3335 C C   . ASN B 211 ? 0.3977 0.3746 0.3501 -0.0169 0.0407  -0.0257 213 ASN B C   
3336 O O   . ASN B 211 ? 0.4036 0.3805 0.3535 -0.0207 0.0429  -0.0282 213 ASN B O   
3337 C CB  . ASN B 211 ? 0.3952 0.3843 0.3521 -0.0177 0.0316  -0.0206 213 ASN B CB  
3338 C CG  . ASN B 211 ? 0.4323 0.4251 0.3915 -0.0182 0.0287  -0.0187 213 ASN B CG  
3339 O OD1 . ASN B 211 ? 0.4463 0.4450 0.4100 -0.0161 0.0245  -0.0160 213 ASN B OD1 
3340 N ND2 . ASN B 211 ? 0.4696 0.4591 0.4262 -0.0211 0.0313  -0.0203 213 ASN B ND2 
3341 N N   . ARG B 212 ? 0.3631 0.3371 0.3192 -0.0097 0.0407  -0.0242 214 ARG B N   
3342 C CA  . ARG B 212 ? 0.3701 0.3409 0.3289 -0.0049 0.0433  -0.0255 214 ARG B CA  
3343 C C   . ARG B 212 ? 0.3460 0.3234 0.3079 -0.0056 0.0420  -0.0263 214 ARG B C   
3344 O O   . ARG B 212 ? 0.3566 0.3320 0.3186 -0.0066 0.0461  -0.0295 214 ARG B O   
3345 C CB  . ARG B 212 ? 0.4132 0.3822 0.3756 0.0026  0.0412  -0.0227 214 ARG B CB  
3346 C CG  . ARG B 212 ? 0.4891 0.4564 0.4562 0.0090  0.0424  -0.0231 214 ARG B CG  
3347 C CD  . ARG B 212 ? 0.5421 0.5089 0.5114 0.0151  0.0389  -0.0196 214 ARG B CD  
3348 N NE  . ARG B 212 ? 0.6016 0.5582 0.5659 0.0167  0.0409  -0.0187 214 ARG B NE  
3349 C CZ  . ARG B 212 ? 0.5990 0.5484 0.5635 0.0226  0.0420  -0.0177 214 ARG B CZ  
3350 N NH1 . ARG B 212 ? 0.5735 0.5125 0.5318 0.0230  0.0440  -0.0168 214 ARG B NH1 
3351 N NH2 . ARG B 212 ? 0.6025 0.5548 0.5733 0.0281  0.0411  -0.0176 214 ARG B NH2 
3352 N N   . PHE B 213 ? 0.2772 0.2618 0.2414 -0.0053 0.0369  -0.0237 215 PHE B N   
3353 C CA  . PHE B 213 ? 0.2686 0.2590 0.2335 -0.0079 0.0355  -0.0242 215 PHE B CA  
3354 C C   . PHE B 213 ? 0.2432 0.2381 0.2049 -0.0130 0.0315  -0.0222 215 PHE B C   
3355 O O   . PHE B 213 ? 0.2389 0.2354 0.2016 -0.0121 0.0284  -0.0196 215 PHE B O   
3356 C CB  . PHE B 213 ? 0.2647 0.2593 0.2355 -0.0024 0.0331  -0.0227 215 PHE B CB  
3357 C CG  . PHE B 213 ? 0.2992 0.2912 0.2748 0.0041  0.0351  -0.0235 215 PHE B CG  
3358 C CD1 . PHE B 213 ? 0.3421 0.3331 0.3203 0.0049  0.0391  -0.0269 215 PHE B CD1 
3359 C CD2 . PHE B 213 ? 0.3178 0.3083 0.2953 0.0093  0.0328  -0.0207 215 PHE B CD2 
3360 C CE1 . PHE B 213 ? 0.3540 0.3433 0.3377 0.0116  0.0403  -0.0272 215 PHE B CE1 
3361 C CE2 . PHE B 213 ? 0.3298 0.3181 0.3114 0.0155  0.0336  -0.0207 215 PHE B CE2 
3362 C CZ  . PHE B 213 ? 0.3383 0.3262 0.3234 0.0170  0.0371  -0.0238 215 PHE B CZ  
3363 N N   . VAL B 214 ? 0.2543 0.2512 0.2123 -0.0184 0.0314  -0.0234 216 VAL B N   
3364 C CA  . VAL B 214 ? 0.2441 0.2453 0.1991 -0.0227 0.0269  -0.0210 216 VAL B CA  
3365 C C   . VAL B 214 ? 0.2241 0.2278 0.1780 -0.0241 0.0257  -0.0210 216 VAL B C   
3366 O O   . VAL B 214 ? 0.2412 0.2429 0.1941 -0.0253 0.0299  -0.0243 216 VAL B O   
3367 C CB  . VAL B 214 ? 0.2737 0.2738 0.2223 -0.0299 0.0275  -0.0223 216 VAL B CB  
3368 C CG1 . VAL B 214 ? 0.2867 0.2843 0.2360 -0.0292 0.0290  -0.0227 216 VAL B CG1 
3369 C CG2 . VAL B 214 ? 0.3236 0.3199 0.2665 -0.0352 0.0323  -0.0264 216 VAL B CG2 
3370 N N   . VAL B 215 ? 0.2045 0.2121 0.1586 -0.0241 0.0207  -0.0175 217 VAL B N   
3371 C CA  . VAL B 215 ? 0.2030 0.2118 0.1540 -0.0264 0.0192  -0.0169 217 VAL B CA  
3372 C C   . VAL B 215 ? 0.2036 0.2145 0.1507 -0.0298 0.0138  -0.0132 217 VAL B C   
3373 O O   . VAL B 215 ? 0.2209 0.2314 0.1629 -0.0331 0.0125  -0.0125 217 VAL B O   
3374 C CB  . VAL B 215 ? 0.2005 0.2111 0.1568 -0.0211 0.0189  -0.0162 217 VAL B CB  
3375 C CG1 . VAL B 215 ? 0.2116 0.2212 0.1725 -0.0176 0.0236  -0.0197 217 VAL B CG1 
3376 C CG2 . VAL B 215 ? 0.1909 0.2039 0.1520 -0.0163 0.0148  -0.0122 217 VAL B CG2 
3377 O OXT . VAL B 215 ? 0.1869 0.1999 0.1361 -0.0290 0.0110  -0.0111 217 VAL B OXT 
# 
