data_8QM4
# 
_entry.id   8QM4 
# 
_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   8QM4         pdb_00008qm4 10.2210/pdb8qm4/pdb 
WWPDB D_1292133478 ?            ?                   
# 
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                        8QM4 
_pdbx_database_status.recvd_initial_deposition_date   2023-09-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              Andrew.Woodhead@astx.com 
_pdbx_contact_author.name_first         Andrew 
_pdbx_contact_author.name_last          Woodhead 
_pdbx_contact_author.name_mi            J. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0009-0005-1604-2904 
# 
_audit_author.name               'Cleasby, A.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0003-2619-9532 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                10037 
_citation.page_last                 10037 
_citation.title                     
'Integrating fragment-based screening with targeted protein degradation and genetic rescue to explore eIF4E function.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-024-54356-1 
_citation.pdbx_database_id_PubMed   40016190 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Sharp, S.Y.'          1  ? 
primary 'Martella, M.'         2  ? 
primary 
;D'Agostino, S.
;
3  ? 
primary 'Milton, C.I.'         4  ? 
primary 'Ward, G.'             5  ? 
primary 'Woodhead, A.J.'       6  ? 
primary 'Richardson, C.J.'     7  ? 
primary 'Carr, M.G.'           8  ? 
primary 'Chiarparin, E.'       9  ? 
primary 'Cons, B.D.'           10 ? 
primary 'Coyle, J.'            11 ? 
primary 'East, C.E.'           12 ? 
primary 'Hiscock, S.D.'        13 ? 
primary 'Martinez-Fleites, C.' 14 ? 
primary 'Mortenson, P.N.'      15 ? 
primary 'Palmer, N.'           16 ? 
primary 'Pathuri, P.'          17 ? 
primary 'Powers, M.V.'         18 ? 
primary 'Saalau, S.M.'         19 ? 
primary 'St Denis, J.D.'       20 ? 
primary 'Swabey, K.'           21 ? 
primary 'Vinkovic, M.'         22 ? 
primary 'Walton, H.'           23 ? 
primary 'Williams, G.'         24 ? 
primary 'Clarke, P.A.'         25 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Eukaryotic translation initiation factor 4E' 25014.445 2   ? ? ? ? 
2 non-polymer syn 'DIMETHYL SULFOXIDE'                          78.133    2   ? ? ? ? 
3 non-polymer syn 'TRIETHYLENE GLYCOL'                          150.173   2   ? ? ? ? 
4 non-polymer syn 3-phenylphenol                                170.207   2   ? ? ? ? 
5 water       nat water                                         18.015    120 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MHHHHHHGARIIYDRAFLMACRGGGGENLYFQGKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLS
SNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLNRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDK
IAIWTTECENREAVTHIGRVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MHHHHHHGARIIYDRAFLMACRGGGGENLYFQGKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLS
SNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLNRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDK
IAIWTTECENREAVTHIGRVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'DIMETHYL SULFOXIDE' DMS 
3 'TRIETHYLENE GLYCOL' PGE 
4 3-phenylphenol       W5B 
5 water                HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   GLY n 
1 9   ALA n 
1 10  ARG n 
1 11  ILE n 
1 12  ILE n 
1 13  TYR n 
1 14  ASP n 
1 15  ARG n 
1 16  ALA n 
1 17  PHE n 
1 18  LEU n 
1 19  MET n 
1 20  ALA n 
1 21  CYS n 
1 22  ARG n 
1 23  GLY n 
1 24  GLY n 
1 25  GLY n 
1 26  GLY n 
1 27  GLU n 
1 28  ASN n 
1 29  LEU n 
1 30  TYR n 
1 31  PHE n 
1 32  GLN n 
1 33  GLY n 
1 34  LYS n 
1 35  HIS n 
1 36  PRO n 
1 37  LEU n 
1 38  GLN n 
1 39  ASN n 
1 40  ARG n 
1 41  TRP n 
1 42  ALA n 
1 43  LEU n 
1 44  TRP n 
1 45  PHE n 
1 46  PHE n 
1 47  LYS n 
1 48  ASN n 
1 49  ASP n 
1 50  LYS n 
1 51  SER n 
1 52  LYS n 
1 53  THR n 
1 54  TRP n 
1 55  GLN n 
1 56  ALA n 
1 57  ASN n 
1 58  LEU n 
1 59  ARG n 
1 60  LEU n 
1 61  ILE n 
1 62  SER n 
1 63  LYS n 
1 64  PHE n 
1 65  ASP n 
1 66  THR n 
1 67  VAL n 
1 68  GLU n 
1 69  ASP n 
1 70  PHE n 
1 71  TRP n 
1 72  ALA n 
1 73  LEU n 
1 74  TYR n 
1 75  ASN n 
1 76  HIS n 
1 77  ILE n 
1 78  GLN n 
1 79  LEU n 
1 80  SER n 
1 81  SER n 
1 82  ASN n 
1 83  LEU n 
1 84  MET n 
1 85  PRO n 
1 86  GLY n 
1 87  CYS n 
1 88  ASP n 
1 89  TYR n 
1 90  SER n 
1 91  LEU n 
1 92  PHE n 
1 93  LYS n 
1 94  ASP n 
1 95  GLY n 
1 96  ILE n 
1 97  GLU n 
1 98  PRO n 
1 99  MET n 
1 100 TRP n 
1 101 GLU n 
1 102 ASP n 
1 103 GLU n 
1 104 LYS n 
1 105 ASN n 
1 106 LYS n 
1 107 ARG n 
1 108 GLY n 
1 109 GLY n 
1 110 ARG n 
1 111 TRP n 
1 112 LEU n 
1 113 ILE n 
1 114 THR n 
1 115 LEU n 
1 116 ASN n 
1 117 LYS n 
1 118 GLN n 
1 119 GLN n 
1 120 ARG n 
1 121 ARG n 
1 122 SER n 
1 123 ASP n 
1 124 LEU n 
1 125 ASN n 
1 126 ARG n 
1 127 PHE n 
1 128 TRP n 
1 129 LEU n 
1 130 GLU n 
1 131 THR n 
1 132 LEU n 
1 133 LEU n 
1 134 CYS n 
1 135 LEU n 
1 136 ILE n 
1 137 GLY n 
1 138 GLU n 
1 139 SER n 
1 140 PHE n 
1 141 ASP n 
1 142 ASP n 
1 143 TYR n 
1 144 SER n 
1 145 ASP n 
1 146 ASP n 
1 147 VAL n 
1 148 CYS n 
1 149 GLY n 
1 150 ALA n 
1 151 VAL n 
1 152 VAL n 
1 153 ASN n 
1 154 VAL n 
1 155 ARG n 
1 156 ALA n 
1 157 LYS n 
1 158 GLY n 
1 159 ASP n 
1 160 LYS n 
1 161 ILE n 
1 162 ALA n 
1 163 ILE n 
1 164 TRP n 
1 165 THR n 
1 166 THR n 
1 167 GLU n 
1 168 CYS n 
1 169 GLU n 
1 170 ASN n 
1 171 ARG n 
1 172 GLU n 
1 173 ALA n 
1 174 VAL n 
1 175 THR n 
1 176 HIS n 
1 177 ILE n 
1 178 GLY n 
1 179 ARG n 
1 180 VAL n 
1 181 TYR n 
1 182 LYS n 
1 183 GLU n 
1 184 ARG n 
1 185 LEU n 
1 186 GLY n 
1 187 LEU n 
1 188 PRO n 
1 189 PRO n 
1 190 LYS n 
1 191 ILE n 
1 192 VAL n 
1 193 ILE n 
1 194 GLY n 
1 195 TYR n 
1 196 GLN n 
1 197 SER n 
1 198 HIS n 
1 199 ALA n 
1 200 ASP n 
1 201 THR n 
1 202 ALA n 
1 203 THR n 
1 204 LYS n 
1 205 SER n 
1 206 GLY n 
1 207 SER n 
1 208 THR n 
1 209 THR n 
1 210 LYS n 
1 211 ASN n 
1 212 ARG n 
1 213 PHE n 
1 214 VAL n 
1 215 VAL n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   215 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 EIF4E 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21-Codon plus (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 
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 
W5B non-polymer         . 3-phenylphenol       ? 'C12 H10 O'      170.207 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   3   ?   ?   ?   A . n 
A 1 2   HIS 2   4   ?   ?   ?   A . n 
A 1 3   HIS 3   5   ?   ?   ?   A . n 
A 1 4   HIS 4   6   ?   ?   ?   A . n 
A 1 5   HIS 5   7   ?   ?   ?   A . n 
A 1 6   HIS 6   8   ?   ?   ?   A . n 
A 1 7   HIS 7   9   ?   ?   ?   A . n 
A 1 8   GLY 8   10  ?   ?   ?   A . n 
A 1 9   ALA 9   11  11  ALA ALA A . n 
A 1 10  ARG 10  12  12  ARG ARG A . n 
A 1 11  ILE 11  13  13  ILE ILE A . n 
A 1 12  ILE 12  14  14  ILE ILE A . n 
A 1 13  TYR 13  15  15  TYR TYR A . n 
A 1 14  ASP 14  16  16  ASP ASP A . n 
A 1 15  ARG 15  17  17  ARG ARG A . n 
A 1 16  ALA 16  18  18  ALA ALA A . n 
A 1 17  PHE 17  19  19  PHE PHE A . n 
A 1 18  LEU 18  20  20  LEU LEU A . n 
A 1 19  MET 19  21  21  MET MET A . n 
A 1 20  ALA 20  22  22  ALA ALA A . n 
A 1 21  CYS 21  23  23  CYS CYS A . n 
A 1 22  ARG 22  24  24  ARG ARG A . n 
A 1 23  GLY 23  25  25  GLY GLY A . n 
A 1 24  GLY 24  26  26  GLY GLY A . n 
A 1 25  GLY 25  27  27  GLY GLY A . n 
A 1 26  GLY 26  28  28  GLY GLY A . n 
A 1 27  GLU 27  29  29  GLU GLU A . n 
A 1 28  ASN 28  30  30  ASN ASN A . n 
A 1 29  LEU 29  31  31  LEU LEU A . n 
A 1 30  TYR 30  32  32  TYR TYR A . n 
A 1 31  PHE 31  33  33  PHE PHE A . n 
A 1 32  GLN 32  34  34  GLN GLN A . n 
A 1 33  GLY 33  35  35  GLY GLY A . n 
A 1 34  LYS 34  36  36  LYS LYS A . n 
A 1 35  HIS 35  37  37  HIS HIS A . n 
A 1 36  PRO 36  38  38  PRO PRO A . n 
A 1 37  LEU 37  39  39  LEU LEU A . n 
A 1 38  GLN 38  40  40  GLN GLN A . n 
A 1 39  ASN 39  41  41  ASN ASN A . n 
A 1 40  ARG 40  42  42  ARG ARG A . n 
A 1 41  TRP 41  43  43  TRP TRP A . n 
A 1 42  ALA 42  44  44  ALA ALA A . n 
A 1 43  LEU 43  45  45  LEU LEU A . n 
A 1 44  TRP 44  46  46  TRP TRP A . n 
A 1 45  PHE 45  47  47  PHE PHE A . n 
A 1 46  PHE 46  48  48  PHE PHE A . n 
A 1 47  LYS 47  49  49  LYS LYS A . n 
A 1 48  ASN 48  50  50  ASN ASN A . n 
A 1 49  ASP 49  51  51  ASP ASP A . n 
A 1 50  LYS 50  52  52  LYS LYS A . n 
A 1 51  SER 51  53  53  SER SER A . n 
A 1 52  LYS 52  54  54  LYS LYS A . n 
A 1 53  THR 53  55  55  THR THR A . n 
A 1 54  TRP 54  56  56  TRP TRP A . n 
A 1 55  GLN 55  57  57  GLN GLN A . n 
A 1 56  ALA 56  58  58  ALA ALA A . n 
A 1 57  ASN 57  59  59  ASN ASN A . n 
A 1 58  LEU 58  60  60  LEU LEU A . n 
A 1 59  ARG 59  61  61  ARG ARG A . n 
A 1 60  LEU 60  62  62  LEU LEU A . n 
A 1 61  ILE 61  63  63  ILE ILE A . n 
A 1 62  SER 62  64  64  SER SER A . n 
A 1 63  LYS 63  65  65  LYS LYS A . n 
A 1 64  PHE 64  66  66  PHE PHE A . n 
A 1 65  ASP 65  67  67  ASP ASP A . n 
A 1 66  THR 66  68  68  THR THR A . n 
A 1 67  VAL 67  69  69  VAL VAL A . n 
A 1 68  GLU 68  70  70  GLU GLU A . n 
A 1 69  ASP 69  71  71  ASP ASP A . n 
A 1 70  PHE 70  72  72  PHE PHE A . n 
A 1 71  TRP 71  73  73  TRP TRP A . n 
A 1 72  ALA 72  74  74  ALA ALA A . n 
A 1 73  LEU 73  75  75  LEU LEU A . n 
A 1 74  TYR 74  76  76  TYR TYR A . n 
A 1 75  ASN 75  77  77  ASN ASN A . n 
A 1 76  HIS 76  78  78  HIS HIS A . n 
A 1 77  ILE 77  79  79  ILE ILE A . n 
A 1 78  GLN 78  80  80  GLN GLN A . n 
A 1 79  LEU 79  81  81  LEU LEU A . n 
A 1 80  SER 80  82  82  SER SER A . n 
A 1 81  SER 81  83  83  SER SER A . n 
A 1 82  ASN 82  84  84  ASN ASN A . n 
A 1 83  LEU 83  85  85  LEU LEU A . n 
A 1 84  MET 84  86  86  MET MET A . n 
A 1 85  PRO 85  87  87  PRO PRO A . n 
A 1 86  GLY 86  88  88  GLY GLY A . n 
A 1 87  CYS 87  89  89  CYS CYS A . n 
A 1 88  ASP 88  90  90  ASP ASP A . n 
A 1 89  TYR 89  91  91  TYR TYR A . n 
A 1 90  SER 90  92  92  SER SER A . n 
A 1 91  LEU 91  93  93  LEU LEU A . n 
A 1 92  PHE 92  94  94  PHE PHE A . n 
A 1 93  LYS 93  95  95  LYS LYS A . n 
A 1 94  ASP 94  96  96  ASP ASP A . n 
A 1 95  GLY 95  97  97  GLY GLY A . n 
A 1 96  ILE 96  98  98  ILE ILE A . n 
A 1 97  GLU 97  99  99  GLU GLU A . n 
A 1 98  PRO 98  100 100 PRO PRO A . n 
A 1 99  MET 99  101 101 MET MET A . n 
A 1 100 TRP 100 102 102 TRP TRP A . n 
A 1 101 GLU 101 103 103 GLU GLU A . n 
A 1 102 ASP 102 104 104 ASP ASP A . n 
A 1 103 GLU 103 105 105 GLU GLU A . n 
A 1 104 LYS 104 106 106 LYS LYS A . n 
A 1 105 ASN 105 107 107 ASN ASN A . n 
A 1 106 LYS 106 108 108 LYS LYS A . n 
A 1 107 ARG 107 109 109 ARG ARG A . n 
A 1 108 GLY 108 110 110 GLY GLY A . n 
A 1 109 GLY 109 111 111 GLY GLY A . n 
A 1 110 ARG 110 112 112 ARG ARG A . n 
A 1 111 TRP 111 113 113 TRP TRP A . n 
A 1 112 LEU 112 114 114 LEU LEU A . n 
A 1 113 ILE 113 115 115 ILE ILE A . n 
A 1 114 THR 114 116 116 THR THR A . n 
A 1 115 LEU 115 117 117 LEU LEU A . n 
A 1 116 ASN 116 118 118 ASN ASN A . n 
A 1 117 LYS 117 119 119 LYS LYS A . n 
A 1 118 GLN 118 120 120 GLN GLN A . n 
A 1 119 GLN 119 121 121 GLN GLN A . n 
A 1 120 ARG 120 122 122 ARG ARG A . n 
A 1 121 ARG 121 123 123 ARG ARG A . n 
A 1 122 SER 122 124 124 SER SER A . n 
A 1 123 ASP 123 125 125 ASP ASP A . n 
A 1 124 LEU 124 126 126 LEU LEU A . n 
A 1 125 ASN 125 127 127 ASN ASN A . n 
A 1 126 ARG 126 128 128 ARG ARG A . n 
A 1 127 PHE 127 129 129 PHE PHE A . n 
A 1 128 TRP 128 130 130 TRP TRP A . n 
A 1 129 LEU 129 131 131 LEU LEU A . n 
A 1 130 GLU 130 132 132 GLU GLU A . n 
A 1 131 THR 131 133 133 THR THR A . n 
A 1 132 LEU 132 134 134 LEU LEU A . n 
A 1 133 LEU 133 135 135 LEU LEU A . n 
A 1 134 CYS 134 136 136 CYS CYS A . n 
A 1 135 LEU 135 137 137 LEU LEU A . n 
A 1 136 ILE 136 138 138 ILE ILE A . n 
A 1 137 GLY 137 139 139 GLY GLY A . n 
A 1 138 GLU 138 140 140 GLU GLU A . n 
A 1 139 SER 139 141 141 SER SER A . n 
A 1 140 PHE 140 142 142 PHE PHE A . n 
A 1 141 ASP 141 143 143 ASP ASP A . n 
A 1 142 ASP 142 144 144 ASP ASP A . n 
A 1 143 TYR 143 145 145 TYR TYR A . n 
A 1 144 SER 144 146 146 SER SER A . n 
A 1 145 ASP 145 147 147 ASP ASP A . n 
A 1 146 ASP 146 148 148 ASP ASP A . n 
A 1 147 VAL 147 149 149 VAL VAL A . n 
A 1 148 CYS 148 150 150 CYS CYS A . n 
A 1 149 GLY 149 151 151 GLY GLY A . n 
A 1 150 ALA 150 152 152 ALA ALA A . n 
A 1 151 VAL 151 153 153 VAL VAL A . n 
A 1 152 VAL 152 154 154 VAL VAL A . n 
A 1 153 ASN 153 155 155 ASN ASN A . n 
A 1 154 VAL 154 156 156 VAL VAL A . n 
A 1 155 ARG 155 157 157 ARG ARG A . n 
A 1 156 ALA 156 158 158 ALA ALA A . n 
A 1 157 LYS 157 159 159 LYS LYS A . n 
A 1 158 GLY 158 160 160 GLY GLY A . n 
A 1 159 ASP 159 161 161 ASP ASP A . n 
A 1 160 LYS 160 162 162 LYS LYS A . n 
A 1 161 ILE 161 163 163 ILE ILE A . n 
A 1 162 ALA 162 164 164 ALA ALA A . n 
A 1 163 ILE 163 165 165 ILE ILE A . n 
A 1 164 TRP 164 166 166 TRP TRP A . n 
A 1 165 THR 165 167 167 THR THR A . n 
A 1 166 THR 166 168 168 THR THR A . n 
A 1 167 GLU 167 169 169 GLU GLU A . n 
A 1 168 CYS 168 170 170 CYS CYS A . n 
A 1 169 GLU 169 171 171 GLU GLU A . n 
A 1 170 ASN 170 172 172 ASN ASN A . n 
A 1 171 ARG 171 173 173 ARG ARG A . n 
A 1 172 GLU 172 174 174 GLU GLU A . n 
A 1 173 ALA 173 175 175 ALA ALA A . n 
A 1 174 VAL 174 176 176 VAL VAL A . n 
A 1 175 THR 175 177 177 THR THR A . n 
A 1 176 HIS 176 178 178 HIS HIS A . n 
A 1 177 ILE 177 179 179 ILE ILE A . n 
A 1 178 GLY 178 180 180 GLY GLY A . n 
A 1 179 ARG 179 181 181 ARG ARG A . n 
A 1 180 VAL 180 182 182 VAL VAL A . n 
A 1 181 TYR 181 183 183 TYR TYR A . n 
A 1 182 LYS 182 184 184 LYS LYS A . n 
A 1 183 GLU 183 185 185 GLU GLU A . n 
A 1 184 ARG 184 186 186 ARG ARG A . n 
A 1 185 LEU 185 187 187 LEU LEU A . n 
A 1 186 GLY 186 188 188 GLY GLY A . n 
A 1 187 LEU 187 189 189 LEU LEU A . n 
A 1 188 PRO 188 190 190 PRO PRO A . n 
A 1 189 PRO 189 191 191 PRO PRO A . n 
A 1 190 LYS 190 192 192 LYS LYS A . n 
A 1 191 ILE 191 193 193 ILE ILE A . n 
A 1 192 VAL 192 194 194 VAL VAL A . n 
A 1 193 ILE 193 195 195 ILE ILE A . n 
A 1 194 GLY 194 196 196 GLY GLY A . n 
A 1 195 TYR 195 197 197 TYR TYR A . n 
A 1 196 GLN 196 198 198 GLN GLN A . n 
A 1 197 SER 197 199 199 SER SER A . n 
A 1 198 HIS 198 200 200 HIS HIS A . n 
A 1 199 ALA 199 201 201 ALA ALA A . n 
A 1 200 ASP 200 202 202 ASP ASP A . n 
A 1 201 THR 201 203 203 THR THR A . n 
A 1 202 ALA 202 204 204 ALA ALA A . n 
A 1 203 THR 203 205 205 THR THR A . n 
A 1 204 LYS 204 206 206 LYS LYS A . n 
A 1 205 SER 205 207 207 SER SER A . n 
A 1 206 GLY 206 208 208 GLY GLY A . n 
A 1 207 SER 207 209 ?   ?   ?   A . n 
A 1 208 THR 208 210 ?   ?   ?   A . n 
A 1 209 THR 209 211 ?   ?   ?   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   9   HIS HIS 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  ?   ?   ?   B . n 
B 1 24  GLY 24  26  ?   ?   ?   B . n 
B 1 25  GLY 25  27  ?   ?   ?   B . n 
B 1 26  GLY 26  28  ?   ?   ?   B . n 
B 1 27  GLU 27  29  ?   ?   ?   B . n 
B 1 28  ASN 28  30  ?   ?   ?   B . n 
B 1 29  LEU 29  31  ?   ?   ?   B . n 
B 1 30  TYR 30  32  ?   ?   ?   B . n 
B 1 31  PHE 31  33  ?   ?   ?   B . n 
B 1 32  GLN 32  34  ?   ?   ?   B . n 
B 1 33  GLY 33  35  ?   ?   ?   B . n 
B 1 34  LYS 34  36  36  LYS LYS B . n 
B 1 35  HIS 35  37  37  HIS HIS B . n 
B 1 36  PRO 36  38  38  PRO PRO B . n 
B 1 37  LEU 37  39  39  LEU LEU B . n 
B 1 38  GLN 38  40  40  GLN GLN B . n 
B 1 39  ASN 39  41  41  ASN ASN B . n 
B 1 40  ARG 40  42  42  ARG ARG B . n 
B 1 41  TRP 41  43  43  TRP TRP B . n 
B 1 42  ALA 42  44  44  ALA ALA B . n 
B 1 43  LEU 43  45  45  LEU LEU B . n 
B 1 44  TRP 44  46  46  TRP TRP B . n 
B 1 45  PHE 45  47  47  PHE PHE B . n 
B 1 46  PHE 46  48  48  PHE PHE B . n 
B 1 47  LYS 47  49  49  LYS LYS B . n 
B 1 48  ASN 48  50  50  ASN ASN B . n 
B 1 49  ASP 49  51  51  ASP ASP B . n 
B 1 50  LYS 50  52  52  LYS LYS B . n 
B 1 51  SER 51  53  53  SER SER B . n 
B 1 52  LYS 52  54  54  LYS LYS B . n 
B 1 53  THR 53  55  55  THR THR B . n 
B 1 54  TRP 54  56  56  TRP TRP B . n 
B 1 55  GLN 55  57  57  GLN GLN B . n 
B 1 56  ALA 56  58  58  ALA ALA B . n 
B 1 57  ASN 57  59  59  ASN ASN B . n 
B 1 58  LEU 58  60  60  LEU LEU B . n 
B 1 59  ARG 59  61  61  ARG ARG B . n 
B 1 60  LEU 60  62  62  LEU LEU B . n 
B 1 61  ILE 61  63  63  ILE ILE B . n 
B 1 62  SER 62  64  64  SER SER B . n 
B 1 63  LYS 63  65  65  LYS LYS B . n 
B 1 64  PHE 64  66  66  PHE PHE B . n 
B 1 65  ASP 65  67  67  ASP ASP B . n 
B 1 66  THR 66  68  68  THR THR B . n 
B 1 67  VAL 67  69  69  VAL VAL B . n 
B 1 68  GLU 68  70  70  GLU GLU B . n 
B 1 69  ASP 69  71  71  ASP ASP B . n 
B 1 70  PHE 70  72  72  PHE PHE B . n 
B 1 71  TRP 71  73  73  TRP TRP B . n 
B 1 72  ALA 72  74  74  ALA ALA B . n 
B 1 73  LEU 73  75  75  LEU LEU B . n 
B 1 74  TYR 74  76  76  TYR TYR B . n 
B 1 75  ASN 75  77  77  ASN ASN B . n 
B 1 76  HIS 76  78  78  HIS HIS B . n 
B 1 77  ILE 77  79  79  ILE ILE B . n 
B 1 78  GLN 78  80  80  GLN GLN B . n 
B 1 79  LEU 79  81  81  LEU LEU B . n 
B 1 80  SER 80  82  82  SER SER B . n 
B 1 81  SER 81  83  83  SER SER B . n 
B 1 82  ASN 82  84  84  ASN ASN B . n 
B 1 83  LEU 83  85  85  LEU LEU B . n 
B 1 84  MET 84  86  86  MET MET B . n 
B 1 85  PRO 85  87  87  PRO PRO B . n 
B 1 86  GLY 86  88  88  GLY GLY B . n 
B 1 87  CYS 87  89  89  CYS CYS B . n 
B 1 88  ASP 88  90  90  ASP ASP B . n 
B 1 89  TYR 89  91  91  TYR TYR B . n 
B 1 90  SER 90  92  92  SER SER B . n 
B 1 91  LEU 91  93  93  LEU LEU B . n 
B 1 92  PHE 92  94  94  PHE PHE B . n 
B 1 93  LYS 93  95  95  LYS LYS B . n 
B 1 94  ASP 94  96  96  ASP ASP B . n 
B 1 95  GLY 95  97  97  GLY GLY B . n 
B 1 96  ILE 96  98  98  ILE ILE B . n 
B 1 97  GLU 97  99  99  GLU GLU B . n 
B 1 98  PRO 98  100 100 PRO PRO B . n 
B 1 99  MET 99  101 101 MET MET B . n 
B 1 100 TRP 100 102 102 TRP TRP B . n 
B 1 101 GLU 101 103 103 GLU GLU B . n 
B 1 102 ASP 102 104 104 ASP ASP B . n 
B 1 103 GLU 103 105 105 GLU GLU B . n 
B 1 104 LYS 104 106 106 LYS LYS B . n 
B 1 105 ASN 105 107 107 ASN ASN B . n 
B 1 106 LYS 106 108 108 LYS LYS B . n 
B 1 107 ARG 107 109 109 ARG ARG B . n 
B 1 108 GLY 108 110 110 GLY GLY B . n 
B 1 109 GLY 109 111 111 GLY GLY B . n 
B 1 110 ARG 110 112 112 ARG ARG B . n 
B 1 111 TRP 111 113 113 TRP TRP B . n 
B 1 112 LEU 112 114 114 LEU LEU B . n 
B 1 113 ILE 113 115 115 ILE ILE B . n 
B 1 114 THR 114 116 116 THR THR B . n 
B 1 115 LEU 115 117 117 LEU LEU B . n 
B 1 116 ASN 116 118 118 ASN ASN B . n 
B 1 117 LYS 117 119 119 LYS LYS B . n 
B 1 118 GLN 118 120 120 GLN GLN B . n 
B 1 119 GLN 119 121 121 GLN GLN B . n 
B 1 120 ARG 120 122 122 ARG ARG B . n 
B 1 121 ARG 121 123 123 ARG ARG B . n 
B 1 122 SER 122 124 124 SER SER B . n 
B 1 123 ASP 123 125 125 ASP ASP B . n 
B 1 124 LEU 124 126 126 LEU LEU B . n 
B 1 125 ASN 125 127 127 ASN ASN B . n 
B 1 126 ARG 126 128 128 ARG ARG B . n 
B 1 127 PHE 127 129 129 PHE PHE B . n 
B 1 128 TRP 128 130 130 TRP TRP B . n 
B 1 129 LEU 129 131 131 LEU LEU B . n 
B 1 130 GLU 130 132 132 GLU GLU B . n 
B 1 131 THR 131 133 133 THR THR B . n 
B 1 132 LEU 132 134 134 LEU LEU B . n 
B 1 133 LEU 133 135 135 LEU LEU B . n 
B 1 134 CYS 134 136 136 CYS CYS B . n 
B 1 135 LEU 135 137 137 LEU LEU B . n 
B 1 136 ILE 136 138 138 ILE ILE B . n 
B 1 137 GLY 137 139 139 GLY GLY B . n 
B 1 138 GLU 138 140 140 GLU GLU B . n 
B 1 139 SER 139 141 141 SER SER B . n 
B 1 140 PHE 140 142 142 PHE PHE B . n 
B 1 141 ASP 141 143 143 ASP ASP B . n 
B 1 142 ASP 142 144 144 ASP ASP B . n 
B 1 143 TYR 143 145 145 TYR TYR B . n 
B 1 144 SER 144 146 146 SER SER B . n 
B 1 145 ASP 145 147 147 ASP ASP B . n 
B 1 146 ASP 146 148 148 ASP ASP B . n 
B 1 147 VAL 147 149 149 VAL VAL B . n 
B 1 148 CYS 148 150 150 CYS CYS B . n 
B 1 149 GLY 149 151 151 GLY GLY B . n 
B 1 150 ALA 150 152 152 ALA ALA B . n 
B 1 151 VAL 151 153 153 VAL VAL B . n 
B 1 152 VAL 152 154 154 VAL VAL B . n 
B 1 153 ASN 153 155 155 ASN ASN B . n 
B 1 154 VAL 154 156 156 VAL VAL B . n 
B 1 155 ARG 155 157 157 ARG ARG B . n 
B 1 156 ALA 156 158 158 ALA ALA B . n 
B 1 157 LYS 157 159 159 LYS LYS B . n 
B 1 158 GLY 158 160 160 GLY GLY B . n 
B 1 159 ASP 159 161 161 ASP ASP B . n 
B 1 160 LYS 160 162 162 LYS LYS B . n 
B 1 161 ILE 161 163 163 ILE ILE B . n 
B 1 162 ALA 162 164 164 ALA ALA B . n 
B 1 163 ILE 163 165 165 ILE ILE B . n 
B 1 164 TRP 164 166 166 TRP TRP B . n 
B 1 165 THR 165 167 167 THR THR B . n 
B 1 166 THR 166 168 168 THR THR B . n 
B 1 167 GLU 167 169 169 GLU GLU B . n 
B 1 168 CYS 168 170 170 CYS CYS B . n 
B 1 169 GLU 169 171 171 GLU GLU B . n 
B 1 170 ASN 170 172 172 ASN ASN B . n 
B 1 171 ARG 171 173 173 ARG ARG B . n 
B 1 172 GLU 172 174 174 GLU GLU B . n 
B 1 173 ALA 173 175 175 ALA ALA B . n 
B 1 174 VAL 174 176 176 VAL VAL B . n 
B 1 175 THR 175 177 177 THR THR B . n 
B 1 176 HIS 176 178 178 HIS HIS B . n 
B 1 177 ILE 177 179 179 ILE ILE B . n 
B 1 178 GLY 178 180 180 GLY GLY B . n 
B 1 179 ARG 179 181 181 ARG ARG B . n 
B 1 180 VAL 180 182 182 VAL VAL B . n 
B 1 181 TYR 181 183 183 TYR TYR B . n 
B 1 182 LYS 182 184 184 LYS LYS B . n 
B 1 183 GLU 183 185 185 GLU GLU B . n 
B 1 184 ARG 184 186 186 ARG ARG B . n 
B 1 185 LEU 185 187 187 LEU LEU B . n 
B 1 186 GLY 186 188 188 GLY GLY B . n 
B 1 187 LEU 187 189 189 LEU LEU B . n 
B 1 188 PRO 188 190 190 PRO PRO B . n 
B 1 189 PRO 189 191 191 PRO PRO B . n 
B 1 190 LYS 190 192 192 LYS LYS B . n 
B 1 191 ILE 191 193 193 ILE ILE B . n 
B 1 192 VAL 192 194 194 VAL VAL B . n 
B 1 193 ILE 193 195 195 ILE ILE B . n 
B 1 194 GLY 194 196 196 GLY GLY B . n 
B 1 195 TYR 195 197 197 TYR TYR B . n 
B 1 196 GLN 196 198 198 GLN GLN B . n 
B 1 197 SER 197 199 199 SER SER B . n 
B 1 198 HIS 198 200 200 HIS HIS B . n 
B 1 199 ALA 199 201 201 ALA ALA B . n 
B 1 200 ASP 200 202 202 ASP ASP B . n 
B 1 201 THR 201 203 203 THR THR B . n 
B 1 202 ALA 202 204 204 ALA ALA B . n 
B 1 203 THR 203 205 205 THR THR B . n 
B 1 204 LYS 204 206 206 LYS LYS B . n 
B 1 205 SER 205 207 207 SER SER B . n 
B 1 206 GLY 206 208 208 GLY GLY B . n 
B 1 207 SER 207 209 209 SER SER B . n 
B 1 208 THR 208 210 210 THR THR B . n 
B 1 209 THR 209 211 211 THR THR B . n 
B 1 210 LYS 210 212 212 LYS LYS B . n 
B 1 211 ASN 211 213 213 ASN ASN B . n 
B 1 212 ARG 212 214 214 ARG ARG B . n 
B 1 213 PHE 213 215 215 PHE PHE B . n 
B 1 214 VAL 214 216 216 VAL VAL B . n 
B 1 215 VAL 215 217 217 VAL VAL B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 W5B ? ? W5B ? ? 'SUBJECT OF INVESTIGATION' ? 
2 W5B ? ? W5B ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 DMS 1  301 301 DMS DMS A . 
D 3 PGE 1  302 401 PGE PGE A . 
E 3 PGE 1  303 401 PGE PGE A . 
F 4 W5B 1  304 1   W5B L01 A . 
G 2 DMS 1  301 301 DMS DMS B . 
H 4 W5B 1  302 1   W5B L02 B . 
I 5 HOH 1  401 121 HOH HOH A . 
I 5 HOH 2  402 37  HOH HOH A . 
I 5 HOH 3  403 312 HOH HOH A . 
I 5 HOH 4  404 386 HOH HOH A . 
I 5 HOH 5  405 118 HOH HOH A . 
I 5 HOH 6  406 80  HOH HOH A . 
I 5 HOH 7  407 232 HOH HOH A . 
I 5 HOH 8  408 311 HOH HOH A . 
I 5 HOH 9  409 117 HOH HOH A . 
I 5 HOH 10 410 39  HOH HOH A . 
I 5 HOH 11 411 411 HOH HOH A . 
I 5 HOH 12 412 336 HOH HOH A . 
I 5 HOH 13 413 316 HOH HOH A . 
I 5 HOH 14 414 35  HOH HOH A . 
I 5 HOH 15 415 322 HOH HOH A . 
I 5 HOH 16 416 1   HOH HOH A . 
I 5 HOH 17 417 122 HOH HOH A . 
I 5 HOH 18 418 112 HOH HOH A . 
I 5 HOH 19 419 45  HOH HOH A . 
I 5 HOH 20 420 61  HOH HOH A . 
I 5 HOH 21 421 7   HOH HOH A . 
I 5 HOH 22 422 334 HOH HOH A . 
I 5 HOH 23 423 418 HOH HOH A . 
I 5 HOH 24 424 29  HOH HOH A . 
I 5 HOH 25 425 4   HOH HOH A . 
I 5 HOH 26 426 12  HOH HOH A . 
I 5 HOH 27 427 310 HOH HOH A . 
I 5 HOH 28 428 130 HOH HOH A . 
I 5 HOH 29 429 362 HOH HOH A . 
I 5 HOH 30 430 341 HOH HOH A . 
I 5 HOH 31 431 116 HOH HOH A . 
I 5 HOH 32 432 114 HOH HOH A . 
I 5 HOH 33 433 363 HOH HOH A . 
I 5 HOH 34 434 34  HOH HOH A . 
I 5 HOH 35 435 385 HOH HOH A . 
I 5 HOH 36 436 41  HOH HOH A . 
I 5 HOH 37 437 23  HOH HOH A . 
I 5 HOH 38 438 3   HOH HOH A . 
I 5 HOH 39 439 48  HOH HOH A . 
I 5 HOH 40 440 405 HOH HOH A . 
I 5 HOH 41 441 17  HOH HOH A . 
I 5 HOH 42 442 313 HOH HOH A . 
I 5 HOH 43 443 33  HOH HOH A . 
I 5 HOH 44 444 379 HOH HOH A . 
I 5 HOH 45 445 395 HOH HOH A . 
I 5 HOH 46 446 412 HOH HOH A . 
I 5 HOH 47 447 88  HOH HOH A . 
I 5 HOH 48 448 417 HOH HOH A . 
I 5 HOH 49 449 71  HOH HOH A . 
I 5 HOH 50 450 376 HOH HOH A . 
I 5 HOH 51 451 261 HOH HOH A . 
I 5 HOH 52 452 60  HOH HOH A . 
I 5 HOH 53 453 21  HOH HOH A . 
I 5 HOH 54 454 375 HOH HOH A . 
I 5 HOH 55 455 19  HOH HOH A . 
I 5 HOH 56 456 408 HOH HOH A . 
I 5 HOH 57 457 36  HOH HOH A . 
I 5 HOH 58 458 355 HOH HOH A . 
I 5 HOH 59 459 364 HOH HOH A . 
I 5 HOH 60 460 419 HOH HOH A . 
I 5 HOH 61 461 205 HOH HOH A . 
I 5 HOH 62 462 398 HOH HOH A . 
I 5 HOH 63 463 413 HOH HOH A . 
I 5 HOH 64 464 378 HOH HOH A . 
I 5 HOH 65 465 360 HOH HOH A . 
I 5 HOH 66 466 414 HOH HOH A . 
I 5 HOH 67 467 350 HOH HOH A . 
I 5 HOH 68 468 135 HOH HOH A . 
I 5 HOH 69 469 220 HOH HOH A . 
I 5 HOH 70 470 235 HOH HOH A . 
I 5 HOH 71 471 390 HOH HOH A . 
J 5 HOH 1  401 387 HOH HOH B . 
J 5 HOH 2  402 20  HOH HOH B . 
J 5 HOH 3  403 89  HOH HOH B . 
J 5 HOH 4  404 72  HOH HOH B . 
J 5 HOH 5  405 177 HOH HOH B . 
J 5 HOH 6  406 318 HOH HOH B . 
J 5 HOH 7  407 38  HOH HOH B . 
J 5 HOH 8  408 352 HOH HOH B . 
J 5 HOH 9  409 410 HOH HOH B . 
J 5 HOH 10 410 406 HOH HOH B . 
J 5 HOH 11 411 369 HOH HOH B . 
J 5 HOH 12 412 10  HOH HOH B . 
J 5 HOH 13 413 382 HOH HOH B . 
J 5 HOH 14 414 315 HOH HOH B . 
J 5 HOH 15 415 407 HOH HOH B . 
J 5 HOH 16 416 40  HOH HOH B . 
J 5 HOH 17 417 366 HOH HOH B . 
J 5 HOH 18 418 123 HOH HOH B . 
J 5 HOH 19 419 340 HOH HOH B . 
J 5 HOH 20 420 2   HOH HOH B . 
J 5 HOH 21 421 105 HOH HOH B . 
J 5 HOH 22 422 26  HOH HOH B . 
J 5 HOH 23 423 6   HOH HOH B . 
J 5 HOH 24 424 325 HOH HOH B . 
J 5 HOH 25 425 14  HOH HOH B . 
J 5 HOH 26 426 32  HOH HOH B . 
J 5 HOH 27 427 82  HOH HOH B . 
J 5 HOH 28 428 15  HOH HOH B . 
J 5 HOH 29 429 182 HOH HOH B . 
J 5 HOH 30 430 59  HOH HOH B . 
J 5 HOH 31 431 79  HOH HOH B . 
J 5 HOH 32 432 93  HOH HOH B . 
J 5 HOH 33 433 337 HOH HOH B . 
J 5 HOH 34 434 94  HOH HOH B . 
J 5 HOH 35 435 54  HOH HOH B . 
J 5 HOH 36 436 409 HOH HOH B . 
J 5 HOH 37 437 28  HOH HOH B . 
J 5 HOH 38 438 9   HOH HOH B . 
J 5 HOH 39 439 370 HOH HOH B . 
J 5 HOH 40 440 391 HOH HOH B . 
J 5 HOH 41 441 92  HOH HOH B . 
J 5 HOH 42 442 30  HOH HOH B . 
J 5 HOH 43 443 356 HOH HOH B . 
J 5 HOH 44 444 374 HOH HOH B . 
J 5 HOH 45 445 367 HOH HOH B . 
J 5 HOH 46 446 346 HOH HOH B . 
J 5 HOH 47 447 415 HOH HOH B . 
J 5 HOH 48 448 383 HOH HOH B . 
J 5 HOH 49 449 416 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'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .                      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? BUSTER ? ? ? .                      4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   95.92 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QM4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     47.152 
_cell.length_a_esd                 ? 
_cell.length_b                     69.427 
_cell.length_b_esd                 ? 
_cell.length_c                     63.818 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8QM4 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8QM4 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.08 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.77 
_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              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.002M DTT, 40% PEG 400, 0.1M pH=7.5 HEPES/NaOH' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            273 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2011-09-25 
_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   0.97625 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE ID29' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97625 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID29 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8QM4 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.84 
_reflns.d_resolution_low                               69.427 
_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                                     35127 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.7 
_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                                0.048 
_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                                    1.85 
_reflns_shell.d_res_low                                     1.86 
_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                             694 
_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                               0.714 
_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                          99.29 
_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]                            -2.42840 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.23740 
_refine.aniso_B[2][2]                            5.08270 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            -2.65430 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               47.324 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.955 
_refine.correlation_coeff_Fo_to_Fc_free          0.953 
_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                                 8QM4 
_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                            1.849 
_refine.ls_d_res_low                             63.48 
_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                     34696 
_refine.ls_number_reflns_R_free                  1734 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.8 
_refine.ls_percent_reflns_R_free                 5.000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1945 
_refine.ls_R_factor_R_free                       0.2169 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1933 
_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   0.127 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.124 
_refine.pdbx_overall_SU_R_Blow_DPI               0.143 
_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             0.242 
_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                        8QM4 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.22 
_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                       1.849 
_refine_hist.d_res_low                        63.48 
_refine_hist.number_atoms_solvent             120 
_refine_hist.number_atoms_total               3473 
_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        3299 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         54 
_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' ? 0.013 ? 6722  ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 1.07  ? 12059 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1474  ? 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' ? ?     ? 1073  ? t_gen_planes              16.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 6722  ? t_it                      10.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 6.63  ? ?     ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 16.42 ? ?     ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 420   ? 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' ? ?     ? 5081  ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.85 
_refine_ls_shell.d_res_low                        1.86 
_refine_ls_shell.number_reflns_all                694 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             ? 
_refine_ls_shell.number_reflns_R_work             652 
_refine_ls_shell.percent_reflns_obs               99.29 
_refine_ls_shell.percent_reflns_R_free            6.05 
_refine_ls_shell.R_factor_all                     0.2577 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2552 
_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   51 
_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                  0.3007 
# 
_struct.entry_id                     8QM4 
_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        8QM4 
_struct_keywords.text            
'translation initiation factor, translation regulator, protein biosynthesis, RNA binding, TRANSLATION' 
_struct_keywords.pdbx_keywords   TRANSLATION 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 2 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
# 
_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 8QM4 A 34 ? 215 ? P06730 36 ? 217 ? 36 217 
2 1 8QM4 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 8QM4 MET A 1   ? UNP P06730 ?   ?   'initiating methionine' 3   1  
1 8QM4 HIS A 2   ? UNP P06730 ?   ?   'expression tag'        4   2  
1 8QM4 HIS A 3   ? UNP P06730 ?   ?   'expression tag'        5   3  
1 8QM4 HIS A 4   ? UNP P06730 ?   ?   'expression tag'        6   4  
1 8QM4 HIS A 5   ? UNP P06730 ?   ?   'expression tag'        7   5  
1 8QM4 HIS A 6   ? UNP P06730 ?   ?   'expression tag'        8   6  
1 8QM4 HIS A 7   ? UNP P06730 ?   ?   'expression tag'        9   7  
1 8QM4 GLY A 8   ? UNP P06730 ?   ?   'expression tag'        10  8  
1 8QM4 ALA A 9   ? UNP P06730 ?   ?   'expression tag'        11  9  
1 8QM4 ARG A 10  ? UNP P06730 ?   ?   'expression tag'        12  10 
1 8QM4 ILE A 11  ? UNP P06730 ?   ?   'expression tag'        13  11 
1 8QM4 ILE A 12  ? UNP P06730 ?   ?   'expression tag'        14  12 
1 8QM4 TYR A 13  ? UNP P06730 ?   ?   'expression tag'        15  13 
1 8QM4 ASP A 14  ? UNP P06730 ?   ?   'expression tag'        16  14 
1 8QM4 ARG A 15  ? UNP P06730 ?   ?   'expression tag'        17  15 
1 8QM4 ALA A 16  ? UNP P06730 ?   ?   'expression tag'        18  16 
1 8QM4 PHE A 17  ? UNP P06730 ?   ?   'expression tag'        19  17 
1 8QM4 LEU A 18  ? UNP P06730 ?   ?   'expression tag'        20  18 
1 8QM4 MET A 19  ? UNP P06730 ?   ?   'expression tag'        21  19 
1 8QM4 ALA A 20  ? UNP P06730 ?   ?   'expression tag'        22  20 
1 8QM4 CYS A 21  ? UNP P06730 ?   ?   'expression tag'        23  21 
1 8QM4 ARG A 22  ? UNP P06730 ?   ?   'expression tag'        24  22 
1 8QM4 GLY A 23  ? UNP P06730 ?   ?   'expression tag'        25  23 
1 8QM4 GLY A 24  ? UNP P06730 ?   ?   'expression tag'        26  24 
1 8QM4 GLY A 25  ? UNP P06730 ?   ?   'expression tag'        27  25 
1 8QM4 GLY A 26  ? UNP P06730 ?   ?   'expression tag'        28  26 
1 8QM4 GLU A 27  ? UNP P06730 ?   ?   'expression tag'        29  27 
1 8QM4 ASN A 28  ? UNP P06730 ?   ?   'expression tag'        30  28 
1 8QM4 LEU A 29  ? UNP P06730 ?   ?   'expression tag'        31  29 
1 8QM4 TYR A 30  ? UNP P06730 ?   ?   'expression tag'        32  30 
1 8QM4 PHE A 31  ? UNP P06730 ?   ?   'expression tag'        33  31 
1 8QM4 GLN A 32  ? UNP P06730 ?   ?   'expression tag'        34  32 
1 8QM4 GLY A 33  ? UNP P06730 ?   ?   'expression tag'        35  33 
1 8QM4 ASN A 125 ? UNP P06730 ASP 127 conflict                127 34 
2 8QM4 MET B 1   ? UNP P06730 ?   ?   'initiating methionine' 3   35 
2 8QM4 HIS B 2   ? UNP P06730 ?   ?   'expression tag'        4   36 
2 8QM4 HIS B 3   ? UNP P06730 ?   ?   'expression tag'        5   37 
2 8QM4 HIS B 4   ? UNP P06730 ?   ?   'expression tag'        6   38 
2 8QM4 HIS B 5   ? UNP P06730 ?   ?   'expression tag'        7   39 
2 8QM4 HIS B 6   ? UNP P06730 ?   ?   'expression tag'        8   40 
2 8QM4 HIS B 7   ? UNP P06730 ?   ?   'expression tag'        9   41 
2 8QM4 GLY B 8   ? UNP P06730 ?   ?   'expression tag'        10  42 
2 8QM4 ALA B 9   ? UNP P06730 ?   ?   'expression tag'        11  43 
2 8QM4 ARG B 10  ? UNP P06730 ?   ?   'expression tag'        12  44 
2 8QM4 ILE B 11  ? UNP P06730 ?   ?   'expression tag'        13  45 
2 8QM4 ILE B 12  ? UNP P06730 ?   ?   'expression tag'        14  46 
2 8QM4 TYR B 13  ? UNP P06730 ?   ?   'expression tag'        15  47 
2 8QM4 ASP B 14  ? UNP P06730 ?   ?   'expression tag'        16  48 
2 8QM4 ARG B 15  ? UNP P06730 ?   ?   'expression tag'        17  49 
2 8QM4 ALA B 16  ? UNP P06730 ?   ?   'expression tag'        18  50 
2 8QM4 PHE B 17  ? UNP P06730 ?   ?   'expression tag'        19  51 
2 8QM4 LEU B 18  ? UNP P06730 ?   ?   'expression tag'        20  52 
2 8QM4 MET B 19  ? UNP P06730 ?   ?   'expression tag'        21  53 
2 8QM4 ALA B 20  ? UNP P06730 ?   ?   'expression tag'        22  54 
2 8QM4 CYS B 21  ? UNP P06730 ?   ?   'expression tag'        23  55 
2 8QM4 ARG B 22  ? UNP P06730 ?   ?   'expression tag'        24  56 
2 8QM4 GLY B 23  ? UNP P06730 ?   ?   'expression tag'        25  57 
2 8QM4 GLY B 24  ? UNP P06730 ?   ?   'expression tag'        26  58 
2 8QM4 GLY B 25  ? UNP P06730 ?   ?   'expression tag'        27  59 
2 8QM4 GLY B 26  ? UNP P06730 ?   ?   'expression tag'        28  60 
2 8QM4 GLU B 27  ? UNP P06730 ?   ?   'expression tag'        29  61 
2 8QM4 ASN B 28  ? UNP P06730 ?   ?   'expression tag'        30  62 
2 8QM4 LEU B 29  ? UNP P06730 ?   ?   'expression tag'        31  63 
2 8QM4 TYR B 30  ? UNP P06730 ?   ?   'expression tag'        32  64 
2 8QM4 PHE B 31  ? UNP P06730 ?   ?   'expression tag'        33  65 
2 8QM4 GLN B 32  ? UNP P06730 ?   ?   'expression tag'        34  66 
2 8QM4 GLY B 33  ? UNP P06730 ?   ?   'expression tag'        35  67 
2 8QM4 ASN B 125 ? UNP P06730 ASP 127 conflict                127 68 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2440  ? 
1 MORE         13    ? 
1 'SSA (A^2)'  20160 ? 
# 
_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 
# 
_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  ? CYS A 21  ? ASP A 16  CYS A 23  1 ? 8  
HELX_P HELX_P2  AA2 ASN A 28  ? GLN A 32  ? ASN A 30  GLN A 34  5 ? 5  
HELX_P HELX_P3  AA3 THR A 53  ? ASN A 57  ? THR A 55  ASN A 59  1 ? 5  
HELX_P HELX_P4  AA4 VAL A 67  ? ILE A 77  ? VAL A 69  ILE A 79  1 ? 11 
HELX_P HELX_P5  AA5 LEU A 79  ? LEU A 83  ? LEU A 81  LEU A 85  5 ? 5  
HELX_P HELX_P6  AA6 GLN A 118 ? ASP A 123 ? GLN A 120 ASP A 125 1 ? 6  
HELX_P HELX_P7  AA7 ASP A 123 ? GLY A 137 ? ASP A 125 GLY A 139 1 ? 15 
HELX_P HELX_P8  AA8 PHE A 140 ? ASP A 145 ? PHE A 142 ASP A 147 5 ? 6  
HELX_P HELX_P9  AA9 ASN A 170 ? GLY A 186 ? ASN A 172 GLY A 188 1 ? 17 
HELX_P HELX_P10 AB1 HIS A 198 ? ALA A 202 ? HIS A 200 ALA A 204 1 ? 5  
HELX_P HELX_P11 AB2 ASP B 14  ? CYS B 21  ? ASP B 16  CYS B 23  1 ? 8  
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  ? LEU B 79  ? VAL B 69  LEU B 81  1 ? 13 
HELX_P HELX_P14 AB5 GLN B 118 ? ASP B 123 ? GLN B 120 ASP B 125 1 ? 6  
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  ? PHE A 46  ? PRO A 38  PHE A 48  
AA1 3 ASP A 88  ? LYS A 93  ? ASP A 90  LYS A 95  
AA1 4 VAL A 147 ? ASN A 153 ? VAL A 149 ASN A 155 
AA1 5 ASP A 159 ? THR A 165 ? ASP A 161 THR A 167 
AA1 6 GLY A 109 ? LEU A 115 ? GLY A 111 LEU A 117 
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  ? PHE B 46  ? PRO B 38  PHE B 48  
AA2 3 ASP B 88  ? LYS B 93  ? ASP B 90  LYS B 95  
AA2 4 VAL B 147 ? ASN B 153 ? VAL B 149 ASN B 155 
AA2 5 ASP B 159 ? THR B 165 ? ASP B 161 THR B 167 
AA2 6 GLY B 109 ? LEU B 115 ? GLY B 111 LEU B 117 
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 ARG A 59  ? O ARG A 61  N PHE A 45  ? N PHE A 47  
AA1 2 3 N TRP A 44  ? N TRP A 46  O SER A 90  ? O SER A 92  
AA1 3 4 N TYR A 89  ? N TYR A 91  O VAL A 152 ? O VAL A 154 
AA1 4 5 N CYS A 148 ? N CYS A 150 O TRP A 164 ? O TRP A 166 
AA1 5 6 O ASP A 159 ? O ASP A 161 N LEU A 115 ? N LEU A 117 
AA1 6 7 N LEU A 112 ? N LEU A 114 O GLY A 194 ? O GLY A 196 
AA1 7 8 N TYR A 195 ? N TYR A 197 O PHE A 213 ? O PHE A 215 
AA2 1 2 O ARG B 59  ? O ARG B 61  N PHE B 45  ? N PHE B 47  
AA2 2 3 N TRP B 44  ? N TRP B 46  O SER B 90  ? O SER B 92  
AA2 3 4 N TYR B 89  ? N TYR B 91  O VAL B 152 ? O VAL B 154 
AA2 4 5 N 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                   8QM4 
_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  ? ? -146.13 22.45   
2 1 ASP A 143 ? ? 58.18   -136.82 
3 1 ASP B 67  ? ? -146.11 23.39   
4 1 SER B 82  ? ? -159.99 35.03   
5 1 ASN B 84  ? ? -39.92  155.41  
6 1 PRO B 100 ? ? -80.20  49.94   
7 1 ASP B 143 ? ? 58.09   -135.48 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 20.7907 -13.8189 4.5374  -0.0463 ? -0.0157 ? 0.0093 ? -0.0343 ? 0.0051 ? 0.0584  ? 1.4071 ? 0.0696 
? 0.0272  ? 1.3399 ? -0.2474 ? 0.4407 ? 0.0713  ? -0.0481 ? 0.1455  ? 0.0262  ? -0.0243 ? 0.0706 ? 0.0909  ? 0.0499 ? -0.0470 ? 
2 'X-RAY DIFFRACTION' ? refined 1.8603  -21.2982 31.9892 0.0880  ? -0.0057 ? 0.0050 ? -0.0778 ? 0.0242 ? -0.0552 ? 0.8630 ? 
-0.3666 ? -0.6985 ? 1.7138 ? 0.4853  ? 1.5575 ? -0.0594 ? -0.1913 ? -0.0870 ? -0.1465 ? 0.0174  ? 0.2241 ? -0.0606 ? 0.1941 ? 
0.0420  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? '{ A|11 - A|217 }' 
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? '{ B|9 - B|217 }'  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 3   ? A MET 1   
2  1 Y 1 A HIS 4   ? A HIS 2   
3  1 Y 1 A HIS 5   ? A HIS 3   
4  1 Y 1 A HIS 6   ? A HIS 4   
5  1 Y 1 A HIS 7   ? A HIS 5   
6  1 Y 1 A HIS 8   ? A HIS 6   
7  1 Y 1 A HIS 9   ? A HIS 7   
8  1 Y 1 A GLY 10  ? A GLY 8   
9  1 Y 1 A SER 209 ? A SER 207 
10 1 Y 1 A THR 210 ? A THR 208 
11 1 Y 1 A THR 211 ? A THR 209 
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 GLY 25  ? B GLY 23  
19 1 Y 1 B GLY 26  ? B GLY 24  
20 1 Y 1 B GLY 27  ? B GLY 25  
21 1 Y 1 B GLY 28  ? B GLY 26  
22 1 Y 1 B GLU 29  ? B GLU 27  
23 1 Y 1 B ASN 30  ? B ASN 28  
24 1 Y 1 B LEU 31  ? B LEU 29  
25 1 Y 1 B TYR 32  ? B TYR 30  
26 1 Y 1 B PHE 33  ? B PHE 31  
27 1 Y 1 B GLN 34  ? B GLN 32  
28 1 Y 1 B GLY 35  ? B GLY 33  
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
DMS S    S N N 88  
DMS O    O N N 89  
DMS C1   C N N 90  
DMS C2   C N N 91  
DMS H11  H N N 92  
DMS H12  H N N 93  
DMS H13  H N N 94  
DMS H21  H N N 95  
DMS H22  H N N 96  
DMS H23  H N N 97  
GLN N    N N N 98  
GLN CA   C N S 99  
GLN C    C N N 100 
GLN O    O N N 101 
GLN CB   C N N 102 
GLN CG   C N N 103 
GLN CD   C N N 104 
GLN OE1  O N N 105 
GLN NE2  N N N 106 
GLN OXT  O N N 107 
GLN H    H N N 108 
GLN H2   H N N 109 
GLN HA   H N N 110 
GLN HB2  H N N 111 
GLN HB3  H N N 112 
GLN HG2  H N N 113 
GLN HG3  H N N 114 
GLN HE21 H N N 115 
GLN HE22 H N N 116 
GLN HXT  H N N 117 
GLU N    N N N 118 
GLU CA   C N S 119 
GLU C    C N N 120 
GLU O    O N N 121 
GLU CB   C N N 122 
GLU CG   C N N 123 
GLU CD   C N N 124 
GLU OE1  O N N 125 
GLU OE2  O N N 126 
GLU OXT  O N N 127 
GLU H    H N N 128 
GLU H2   H N N 129 
GLU HA   H N N 130 
GLU HB2  H N N 131 
GLU HB3  H N N 132 
GLU HG2  H N N 133 
GLU HG3  H N N 134 
GLU HE2  H N N 135 
GLU HXT  H N N 136 
GLY N    N N N 137 
GLY CA   C N N 138 
GLY C    C N N 139 
GLY O    O N N 140 
GLY OXT  O N N 141 
GLY H    H N N 142 
GLY H2   H N N 143 
GLY HA2  H N N 144 
GLY HA3  H N N 145 
GLY HXT  H N N 146 
HIS N    N N N 147 
HIS CA   C N S 148 
HIS C    C N N 149 
HIS O    O N N 150 
HIS CB   C N N 151 
HIS CG   C Y N 152 
HIS ND1  N Y N 153 
HIS CD2  C Y N 154 
HIS CE1  C Y N 155 
HIS NE2  N Y N 156 
HIS OXT  O N N 157 
HIS H    H N N 158 
HIS H2   H N N 159 
HIS HA   H N N 160 
HIS HB2  H N N 161 
HIS HB3  H N N 162 
HIS HD1  H N N 163 
HIS HD2  H N N 164 
HIS HE1  H N N 165 
HIS HE2  H N N 166 
HIS HXT  H N N 167 
HOH O    O N N 168 
HOH H1   H N N 169 
HOH H2   H N N 170 
ILE N    N N N 171 
ILE CA   C N S 172 
ILE C    C N N 173 
ILE O    O N N 174 
ILE CB   C N S 175 
ILE CG1  C N N 176 
ILE CG2  C N N 177 
ILE CD1  C N N 178 
ILE OXT  O N N 179 
ILE H    H N N 180 
ILE H2   H N N 181 
ILE HA   H N N 182 
ILE HB   H N N 183 
ILE HG12 H N N 184 
ILE HG13 H N N 185 
ILE HG21 H N N 186 
ILE HG22 H N N 187 
ILE HG23 H N N 188 
ILE HD11 H N N 189 
ILE HD12 H N N 190 
ILE HD13 H N N 191 
ILE HXT  H N N 192 
LEU N    N N N 193 
LEU CA   C N S 194 
LEU C    C N N 195 
LEU O    O N N 196 
LEU CB   C N N 197 
LEU CG   C N N 198 
LEU CD1  C N N 199 
LEU CD2  C N N 200 
LEU OXT  O N N 201 
LEU H    H N N 202 
LEU H2   H N N 203 
LEU HA   H N N 204 
LEU HB2  H N N 205 
LEU HB3  H N N 206 
LEU HG   H N N 207 
LEU HD11 H N N 208 
LEU HD12 H N N 209 
LEU HD13 H N N 210 
LEU HD21 H N N 211 
LEU HD22 H N N 212 
LEU HD23 H N N 213 
LEU HXT  H N N 214 
LYS N    N N N 215 
LYS CA   C N S 216 
LYS C    C N N 217 
LYS O    O N N 218 
LYS CB   C N N 219 
LYS CG   C N N 220 
LYS CD   C N N 221 
LYS CE   C N N 222 
LYS NZ   N N N 223 
LYS OXT  O N N 224 
LYS H    H N N 225 
LYS H2   H N N 226 
LYS HA   H N N 227 
LYS HB2  H N N 228 
LYS HB3  H N N 229 
LYS HG2  H N N 230 
LYS HG3  H N N 231 
LYS HD2  H N N 232 
LYS HD3  H N N 233 
LYS HE2  H N N 234 
LYS HE3  H N N 235 
LYS HZ1  H N N 236 
LYS HZ2  H N N 237 
LYS HZ3  H N N 238 
LYS HXT  H N N 239 
MET N    N N N 240 
MET CA   C N S 241 
MET C    C N N 242 
MET O    O N N 243 
MET CB   C N N 244 
MET CG   C N N 245 
MET SD   S N N 246 
MET CE   C N N 247 
MET OXT  O N N 248 
MET H    H N N 249 
MET H2   H N N 250 
MET HA   H N N 251 
MET HB2  H N N 252 
MET HB3  H N N 253 
MET HG2  H N N 254 
MET HG3  H N N 255 
MET HE1  H N N 256 
MET HE2  H N N 257 
MET HE3  H N N 258 
MET HXT  H N N 259 
PGE C1   C N N 260 
PGE O1   O N N 261 
PGE C2   C N N 262 
PGE O2   O N N 263 
PGE C3   C N N 264 
PGE C4   C N N 265 
PGE O4   O N N 266 
PGE C6   C N N 267 
PGE C5   C N N 268 
PGE O3   O N N 269 
PGE H1   H N N 270 
PGE H12  H N N 271 
PGE HO1  H N N 272 
PGE H2   H N N 273 
PGE H22  H N N 274 
PGE H3   H N N 275 
PGE H32  H N N 276 
PGE H4   H N N 277 
PGE H42  H N N 278 
PGE HO4  H N N 279 
PGE H6   H N N 280 
PGE H62  H N N 281 
PGE H5   H N N 282 
PGE H52  H N N 283 
PHE N    N N N 284 
PHE CA   C N S 285 
PHE C    C N N 286 
PHE O    O N N 287 
PHE CB   C N N 288 
PHE CG   C Y N 289 
PHE CD1  C Y N 290 
PHE CD2  C Y N 291 
PHE CE1  C Y N 292 
PHE CE2  C Y N 293 
PHE CZ   C Y N 294 
PHE OXT  O N N 295 
PHE H    H N N 296 
PHE H2   H N N 297 
PHE HA   H N N 298 
PHE HB2  H N N 299 
PHE HB3  H N N 300 
PHE HD1  H N N 301 
PHE HD2  H N N 302 
PHE HE1  H N N 303 
PHE HE2  H N N 304 
PHE HZ   H N N 305 
PHE HXT  H N N 306 
PRO N    N N N 307 
PRO CA   C N S 308 
PRO C    C N N 309 
PRO O    O N N 310 
PRO CB   C N N 311 
PRO CG   C N N 312 
PRO CD   C N N 313 
PRO OXT  O N N 314 
PRO H    H N N 315 
PRO HA   H N N 316 
PRO HB2  H N N 317 
PRO HB3  H N N 318 
PRO HG2  H N N 319 
PRO HG3  H N N 320 
PRO HD2  H N N 321 
PRO HD3  H N N 322 
PRO HXT  H N N 323 
SER N    N N N 324 
SER CA   C N S 325 
SER C    C N N 326 
SER O    O N N 327 
SER CB   C N N 328 
SER OG   O N N 329 
SER OXT  O N N 330 
SER H    H N N 331 
SER H2   H N N 332 
SER HA   H N N 333 
SER HB2  H N N 334 
SER HB3  H N N 335 
SER HG   H N N 336 
SER HXT  H N N 337 
THR N    N N N 338 
THR CA   C N S 339 
THR C    C N N 340 
THR O    O N N 341 
THR CB   C N R 342 
THR OG1  O N N 343 
THR CG2  C N N 344 
THR OXT  O N N 345 
THR H    H N N 346 
THR H2   H N N 347 
THR HA   H N N 348 
THR HB   H N N 349 
THR HG1  H N N 350 
THR HG21 H N N 351 
THR HG22 H N N 352 
THR HG23 H N N 353 
THR HXT  H N N 354 
TRP N    N N N 355 
TRP CA   C N S 356 
TRP C    C N N 357 
TRP O    O N N 358 
TRP CB   C N N 359 
TRP CG   C Y N 360 
TRP CD1  C Y N 361 
TRP CD2  C Y N 362 
TRP NE1  N Y N 363 
TRP CE2  C Y N 364 
TRP CE3  C Y N 365 
TRP CZ2  C Y N 366 
TRP CZ3  C Y N 367 
TRP CH2  C Y N 368 
TRP OXT  O N N 369 
TRP H    H N N 370 
TRP H2   H N N 371 
TRP HA   H N N 372 
TRP HB2  H N N 373 
TRP HB3  H N N 374 
TRP HD1  H N N 375 
TRP HE1  H N N 376 
TRP HE3  H N N 377 
TRP HZ2  H N N 378 
TRP HZ3  H N N 379 
TRP HH2  H N N 380 
TRP HXT  H N N 381 
TYR N    N N N 382 
TYR CA   C N S 383 
TYR C    C N N 384 
TYR O    O N N 385 
TYR CB   C N N 386 
TYR CG   C Y N 387 
TYR CD1  C Y N 388 
TYR CD2  C Y N 389 
TYR CE1  C Y N 390 
TYR CE2  C Y N 391 
TYR CZ   C Y N 392 
TYR OH   O N N 393 
TYR OXT  O N N 394 
TYR H    H N N 395 
TYR H2   H N N 396 
TYR HA   H N N 397 
TYR HB2  H N N 398 
TYR HB3  H N N 399 
TYR HD1  H N N 400 
TYR HD2  H N N 401 
TYR HE1  H N N 402 
TYR HE2  H N N 403 
TYR HH   H N N 404 
TYR HXT  H N N 405 
VAL N    N N N 406 
VAL CA   C N S 407 
VAL C    C N N 408 
VAL O    O N N 409 
VAL CB   C N N 410 
VAL CG1  C N N 411 
VAL CG2  C N N 412 
VAL OXT  O N N 413 
VAL H    H N N 414 
VAL H2   H N N 415 
VAL HA   H N N 416 
VAL HB   H N N 417 
VAL HG11 H N N 418 
VAL HG12 H N N 419 
VAL HG13 H N N 420 
VAL HG21 H N N 421 
VAL HG22 H N N 422 
VAL HG23 H N N 423 
VAL HXT  H N N 424 
W5B C2   C Y N 425 
W5B C3   C Y N 426 
W5B C5   C Y N 427 
W5B C6   C Y N 428 
W5B C7   C Y N 429 
W5B C8   C Y N 430 
W5B C10  C Y N 431 
W5B C11  C Y N 432 
W5B C12  C Y N 433 
W5B C13  C Y N 434 
W5B O1   O N N 435 
W5B C4   C Y N 436 
W5B C9   C Y N 437 
W5B H15  H N N 438 
W5B H17  H N N 439 
W5B H18  H N N 440 
W5B H20  H N N 441 
W5B H21  H N N 442 
W5B H22  H N N 443 
W5B H23  H N N 444 
W5B H14  H N N 445 
W5B H16  H N N 446 
W5B H19  H N N 447 
# 
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 
PGE C1  O1   sing N N 246 
PGE C1  C2   sing N N 247 
PGE C1  H1   sing N N 248 
PGE C1  H12  sing N N 249 
PGE O1  HO1  sing N N 250 
PGE C2  O2   sing N N 251 
PGE C2  H2   sing N N 252 
PGE C2  H22  sing N N 253 
PGE O2  C3   sing N N 254 
PGE C3  C4   sing N N 255 
PGE C3  H3   sing N N 256 
PGE C3  H32  sing N N 257 
PGE C4  O3   sing N N 258 
PGE C4  H4   sing N N 259 
PGE C4  H42  sing N N 260 
PGE O4  C6   sing N N 261 
PGE O4  HO4  sing N N 262 
PGE C6  C5   sing N N 263 
PGE C6  H6   sing N N 264 
PGE C6  H62  sing N N 265 
PGE C5  O3   sing N N 266 
PGE C5  H5   sing N N 267 
PGE C5  H52  sing N N 268 
PHE N   CA   sing N N 269 
PHE N   H    sing N N 270 
PHE N   H2   sing N N 271 
PHE CA  C    sing N N 272 
PHE CA  CB   sing N N 273 
PHE CA  HA   sing N N 274 
PHE C   O    doub N N 275 
PHE C   OXT  sing N N 276 
PHE CB  CG   sing N N 277 
PHE CB  HB2  sing N N 278 
PHE CB  HB3  sing N N 279 
PHE CG  CD1  doub Y N 280 
PHE CG  CD2  sing Y N 281 
PHE CD1 CE1  sing Y N 282 
PHE CD1 HD1  sing N N 283 
PHE CD2 CE2  doub Y N 284 
PHE CD2 HD2  sing N N 285 
PHE CE1 CZ   doub Y N 286 
PHE CE1 HE1  sing N N 287 
PHE CE2 CZ   sing Y N 288 
PHE CE2 HE2  sing N N 289 
PHE CZ  HZ   sing N N 290 
PHE OXT HXT  sing N N 291 
PRO N   CA   sing N N 292 
PRO N   CD   sing N N 293 
PRO N   H    sing N N 294 
PRO CA  C    sing N N 295 
PRO CA  CB   sing N N 296 
PRO CA  HA   sing N N 297 
PRO C   O    doub N N 298 
PRO C   OXT  sing N N 299 
PRO CB  CG   sing N N 300 
PRO CB  HB2  sing N N 301 
PRO CB  HB3  sing N N 302 
PRO CG  CD   sing N N 303 
PRO CG  HG2  sing N N 304 
PRO CG  HG3  sing N N 305 
PRO CD  HD2  sing N N 306 
PRO CD  HD3  sing N N 307 
PRO OXT HXT  sing N N 308 
SER N   CA   sing N N 309 
SER N   H    sing N N 310 
SER N   H2   sing N N 311 
SER CA  C    sing N N 312 
SER CA  CB   sing N N 313 
SER CA  HA   sing N N 314 
SER C   O    doub N N 315 
SER C   OXT  sing N N 316 
SER CB  OG   sing N N 317 
SER CB  HB2  sing N N 318 
SER CB  HB3  sing N N 319 
SER OG  HG   sing N N 320 
SER OXT HXT  sing N N 321 
THR N   CA   sing N N 322 
THR N   H    sing N N 323 
THR N   H2   sing N N 324 
THR CA  C    sing N N 325 
THR CA  CB   sing N N 326 
THR CA  HA   sing N N 327 
THR C   O    doub N N 328 
THR C   OXT  sing N N 329 
THR CB  OG1  sing N N 330 
THR CB  CG2  sing N N 331 
THR CB  HB   sing N N 332 
THR OG1 HG1  sing N N 333 
THR CG2 HG21 sing N N 334 
THR CG2 HG22 sing N N 335 
THR CG2 HG23 sing N N 336 
THR OXT HXT  sing N N 337 
TRP N   CA   sing N N 338 
TRP N   H    sing N N 339 
TRP N   H2   sing N N 340 
TRP CA  C    sing N N 341 
TRP CA  CB   sing N N 342 
TRP CA  HA   sing N N 343 
TRP C   O    doub N N 344 
TRP C   OXT  sing N N 345 
TRP CB  CG   sing N N 346 
TRP CB  HB2  sing N N 347 
TRP CB  HB3  sing N N 348 
TRP CG  CD1  doub Y N 349 
TRP CG  CD2  sing Y N 350 
TRP CD1 NE1  sing Y N 351 
TRP CD1 HD1  sing N N 352 
TRP CD2 CE2  doub Y N 353 
TRP CD2 CE3  sing Y N 354 
TRP NE1 CE2  sing Y N 355 
TRP NE1 HE1  sing N N 356 
TRP CE2 CZ2  sing Y N 357 
TRP CE3 CZ3  doub Y N 358 
TRP CE3 HE3  sing N N 359 
TRP CZ2 CH2  doub Y N 360 
TRP CZ2 HZ2  sing N N 361 
TRP CZ3 CH2  sing Y N 362 
TRP CZ3 HZ3  sing N N 363 
TRP CH2 HH2  sing N N 364 
TRP OXT HXT  sing N N 365 
TYR N   CA   sing N N 366 
TYR N   H    sing N N 367 
TYR N   H2   sing N N 368 
TYR CA  C    sing N N 369 
TYR CA  CB   sing N N 370 
TYR CA  HA   sing N N 371 
TYR C   O    doub N N 372 
TYR C   OXT  sing N N 373 
TYR CB  CG   sing N N 374 
TYR CB  HB2  sing N N 375 
TYR CB  HB3  sing N N 376 
TYR CG  CD1  doub Y N 377 
TYR CG  CD2  sing Y N 378 
TYR CD1 CE1  sing Y N 379 
TYR CD1 HD1  sing N N 380 
TYR CD2 CE2  doub Y N 381 
TYR CD2 HD2  sing N N 382 
TYR CE1 CZ   doub Y N 383 
TYR CE1 HE1  sing N N 384 
TYR CE2 CZ   sing Y N 385 
TYR CE2 HE2  sing N N 386 
TYR CZ  OH   sing N N 387 
TYR OH  HH   sing N N 388 
TYR OXT HXT  sing N N 389 
VAL N   CA   sing N N 390 
VAL N   H    sing N N 391 
VAL N   H2   sing N N 392 
VAL CA  C    sing N N 393 
VAL CA  CB   sing N N 394 
VAL CA  HA   sing N N 395 
VAL C   O    doub N N 396 
VAL C   OXT  sing N N 397 
VAL CB  CG1  sing N N 398 
VAL CB  CG2  sing N N 399 
VAL CB  HB   sing N N 400 
VAL CG1 HG11 sing N N 401 
VAL CG1 HG12 sing N N 402 
VAL CG1 HG13 sing N N 403 
VAL CG2 HG21 sing N N 404 
VAL CG2 HG22 sing N N 405 
VAL CG2 HG23 sing N N 406 
VAL OXT HXT  sing N N 407 
W5B C12 C11  doub Y N 408 
W5B C12 C13  sing Y N 409 
W5B C11 C10  sing Y N 410 
W5B C13 C8   doub Y N 411 
W5B C10 C9   doub Y N 412 
W5B C8  C9   sing Y N 413 
W5B C8  C6   sing N N 414 
W5B C7  C6   doub Y N 415 
W5B C7  C2   sing Y N 416 
W5B C6  C5   sing Y N 417 
W5B O1  C2   sing N N 418 
W5B C2  C3   doub Y N 419 
W5B C5  C4   doub Y N 420 
W5B C3  C4   sing Y N 421 
W5B C3  H15  sing N N 422 
W5B C5  H17  sing N N 423 
W5B C7  H18  sing N N 424 
W5B C10 H20  sing N N 425 
W5B C11 H21  sing N N 426 
W5B C12 H22  sing N N 427 
W5B C13 H23  sing N N 428 
W5B O1  H14  sing N N 429 
W5B C4  H16  sing N N 430 
W5B C9  H19  sing N N 431 
# 
_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                    8QM4 
_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]   0.021208 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002199 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014404 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.015754 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ALA A 1 9   ? 3.305   -22.352 -9.970  1.00 52.99 ? 11  ALA A N   1 
ATOM   2    C CA  . ALA A 1 9   ? 4.468   -21.620 -10.464 1.00 52.00 ? 11  ALA A CA  1 
ATOM   3    C C   . ALA A 1 9   ? 5.169   -20.938 -9.271  1.00 51.39 ? 11  ALA A C   1 
ATOM   4    O O   . ALA A 1 9   ? 4.506   -20.470 -8.345  1.00 52.35 ? 11  ALA A O   1 
ATOM   5    C CB  . ALA A 1 9   ? 4.034   -20.541 -11.453 1.00 52.47 ? 11  ALA A CB  1 
ATOM   6    N N   . ARG A 1 10  ? 6.507   -20.864 -9.309  1.00 48.87 ? 12  ARG A N   1 
ATOM   7    C CA  . ARG A 1 10  ? 7.270   -20.189 -8.250  1.00 45.52 ? 12  ARG A CA  1 
ATOM   8    C C   . ARG A 1 10  ? 7.010   -18.693 -8.242  1.00 44.08 ? 12  ARG A C   1 
ATOM   9    O O   . ARG A 1 10  ? 7.017   -18.062 -9.304  1.00 45.73 ? 12  ARG A O   1 
ATOM   10   C CB  . ARG A 1 10  ? 8.773   -20.471 -8.424  1.00 44.70 ? 12  ARG A CB  1 
ATOM   11   C CG  . ARG A 1 10  ? 9.671   -19.987 -7.243  1.00 47.10 ? 12  ARG A CG  1 
ATOM   12   C CD  . ARG A 1 10  ? 11.144  -20.335 -7.463  1.00 49.05 ? 12  ARG A CD  1 
ATOM   13   N NE  . ARG A 1 10  ? 11.289  -21.774 -7.619  1.00 50.16 ? 12  ARG A NE  1 
ATOM   14   C CZ  . ARG A 1 10  ? 11.347  -22.647 -6.617  1.00 50.28 ? 12  ARG A CZ  1 
ATOM   15   N NH1 . ARG A 1 10  ? 11.299  -22.229 -5.352  1.00 52.02 ? 12  ARG A NH1 1 
ATOM   16   N NH2 . ARG A 1 10  ? 11.456  -23.939 -6.867  1.00 46.44 ? 12  ARG A NH2 1 
ATOM   17   N N   . ILE A 1 11  ? 6.791   -18.111 -7.042  1.00 40.73 ? 13  ILE A N   1 
ATOM   18   C CA  . ILE A 1 11  ? 6.643   -16.681 -6.893  1.00 38.97 ? 13  ILE A CA  1 
ATOM   19   C C   . ILE A 1 11  ? 8.046   -16.032 -6.855  1.00 39.71 ? 13  ILE A C   1 
ATOM   20   O O   . ILE A 1 11  ? 8.773   -16.201 -5.851  1.00 39.89 ? 13  ILE A O   1 
ATOM   21   C CB  . ILE A 1 11  ? 5.839   -16.330 -5.620  1.00 38.64 ? 13  ILE A CB  1 
ATOM   22   C CG1 . ILE A 1 11  ? 4.475   -17.089 -5.552  1.00 39.60 ? 13  ILE A CG1 1 
ATOM   23   C CG2 . ILE A 1 11  ? 5.622   -14.839 -5.536  1.00 39.80 ? 13  ILE A CG2 1 
ATOM   24   C CD1 . ILE A 1 11  ? 3.757   -16.915 -4.235  1.00 40.43 ? 13  ILE A CD1 1 
ATOM   25   N N   . ILE A 1 12  ? 8.401   -15.283 -7.914  1.00 38.72 ? 14  ILE A N   1 
ATOM   26   C CA  . ILE A 1 12  ? 9.708   -14.684 -8.096  1.00 40.34 ? 14  ILE A CA  1 
ATOM   27   C C   . ILE A 1 12  ? 9.517   -13.203 -8.268  1.00 40.51 ? 14  ILE A C   1 
ATOM   28   O O   . ILE A 1 12  ? 8.695   -12.771 -9.105  1.00 41.16 ? 14  ILE A O   1 
ATOM   29   C CB  . ILE A 1 12  ? 10.446  -15.274 -9.323  1.00 42.05 ? 14  ILE A CB  1 
ATOM   30   C CG1 . ILE A 1 12  ? 10.644  -16.806 -9.169  1.00 44.92 ? 14  ILE A CG1 1 
ATOM   31   C CG2 . ILE A 1 12  ? 11.779  -14.582 -9.578  1.00 42.07 ? 14  ILE A CG2 1 
ATOM   32   C CD1 . ILE A 1 12  ? 11.142  -17.476 -10.367 1.00 47.22 ? 14  ILE A CD1 1 
ATOM   33   N N   . TYR A 1 13  ? 10.248  -12.414 -7.500  1.00 37.15 ? 15  TYR A N   1 
ATOM   34   C CA  . TYR A 1 13  ? 10.266  -10.957 -7.638  1.00 36.44 ? 15  TYR A CA  1 
ATOM   35   C C   . TYR A 1 13  ? 11.661  -10.469 -7.918  1.00 40.55 ? 15  TYR A C   1 
ATOM   36   O O   . TYR A 1 13  ? 12.610  -10.855 -7.199  1.00 39.52 ? 15  TYR A O   1 
ATOM   37   C CB  . TYR A 1 13  ? 9.822   -10.298 -6.359  1.00 36.33 ? 15  TYR A CB  1 
ATOM   38   C CG  . TYR A 1 13  ? 8.429   -10.646 -5.916  1.00 37.60 ? 15  TYR A CG  1 
ATOM   39   C CD1 . TYR A 1 13  ? 7.320   -10.106 -6.561  1.00 39.08 ? 15  TYR A CD1 1 
ATOM   40   C CD2 . TYR A 1 13  ? 8.212   -11.486 -4.843  1.00 37.74 ? 15  TYR A CD2 1 
ATOM   41   C CE1 . TYR A 1 13  ? 6.039   -10.395 -6.149  1.00 38.54 ? 15  TYR A CE1 1 
ATOM   42   C CE2 . TYR A 1 13  ? 6.924   -11.796 -4.418  1.00 37.79 ? 15  TYR A CE2 1 
ATOM   43   C CZ  . TYR A 1 13  ? 5.838   -11.254 -5.089  1.00 38.65 ? 15  TYR A CZ  1 
ATOM   44   O OH  . TYR A 1 13  ? 4.579   -11.570 -4.680  1.00 38.02 ? 15  TYR A OH  1 
ATOM   45   N N   . ASP A 1 14  ? 11.810  -9.621  -8.914  1.00 41.23 ? 16  ASP A N   1 
ATOM   46   C CA  . ASP A 1 14  ? 13.095  -8.986  -9.134  1.00 42.17 ? 16  ASP A CA  1 
ATOM   47   C C   . ASP A 1 14  ? 13.283  -7.792  -8.194  1.00 40.32 ? 16  ASP A C   1 
ATOM   48   O O   . ASP A 1 14  ? 12.369  -7.341  -7.493  1.00 38.79 ? 16  ASP A O   1 
ATOM   49   C CB  . ASP A 1 14  ? 13.349  -8.655  -10.610 1.00 45.91 ? 16  ASP A CB  1 
ATOM   50   C CG  . ASP A 1 14  ? 12.446  -7.641  -11.248 1.00 53.53 ? 16  ASP A CG  1 
ATOM   51   O OD1 . ASP A 1 14  ? 11.835  -6.844  -10.508 1.00 55.75 ? 16  ASP A OD1 1 
ATOM   52   O OD2 . ASP A 1 14  ? 12.352  -7.644  -12.491 1.00 55.84 ? 16  ASP A OD2 1 
ATOM   53   N N   . ARG A 1 15  ? 14.499  -7.293  -8.189  1.00 40.04 ? 17  ARG A N   1 
ATOM   54   C CA  . ARG A 1 15  ? 14.908  -6.216  -7.315  1.00 39.99 ? 17  ARG A CA  1 
ATOM   55   C C   . ARG A 1 15  ? 14.038  -4.965  -7.521  1.00 41.54 ? 17  ARG A C   1 
ATOM   56   O O   . ARG A 1 15  ? 13.615  -4.358  -6.554  1.00 40.24 ? 17  ARG A O   1 
ATOM   57   C CB  . ARG A 1 15  ? 16.376  -5.882  -7.594  1.00 40.14 ? 17  ARG A CB  1 
ATOM   58   C CG  . ARG A 1 15  ? 16.981  -5.030  -6.586  1.00 43.07 ? 17  ARG A CG  1 
ATOM   59   C CD  . ARG A 1 15  ? 18.346  -4.544  -7.059  1.00 46.93 ? 17  ARG A CD  1 
ATOM   60   N NE  . ARG A 1 15  ? 18.917  -3.610  -6.108  1.00 50.66 ? 17  ARG A NE  1 
ATOM   61   C CZ  . ARG A 1 15  ? 18.590  -2.327  -5.990  1.00 57.33 ? 17  ARG A CZ  1 
ATOM   62   N NH1 . ARG A 1 15  ? 17.665  -1.792  -6.776  1.00 60.02 ? 17  ARG A NH1 1 
ATOM   63   N NH2 . ARG A 1 15  ? 19.177  -1.572  -5.077  1.00 60.28 ? 17  ARG A NH2 1 
ATOM   64   N N   . ALA A 1 16  ? 13.791  -4.597  -8.785  1.00 44.01 ? 18  ALA A N   1 
ATOM   65   C CA  . ALA A 1 16  ? 13.004  -3.381  -9.108  1.00 44.14 ? 18  ALA A CA  1 
ATOM   66   C C   . ALA A 1 16  ? 11.580  -3.488  -8.539  1.00 44.16 ? 18  ALA A C   1 
ATOM   67   O O   . ALA A 1 16  ? 11.110  -2.534  -7.933  1.00 46.37 ? 18  ALA A O   1 
ATOM   68   C CB  . ALA A 1 16  ? 12.972  -3.194  -10.610 1.00 44.83 ? 18  ALA A CB  1 
ATOM   69   N N   . PHE A 1 17  ? 10.920  -4.618  -8.699  1.00 44.35 ? 19  PHE A N   1 
ATOM   70   C CA  . PHE A 1 17  ? 9.597   -4.853  -8.130  1.00 44.92 ? 19  PHE A CA  1 
ATOM   71   C C   . PHE A 1 17  ? 9.600   -4.724  -6.613  1.00 44.63 ? 19  PHE A C   1 
ATOM   72   O O   . PHE A 1 17  ? 8.783   -4.005  -6.060  1.00 45.14 ? 19  PHE A O   1 
ATOM   73   C CB  . PHE A 1 17  ? 9.070   -6.223  -8.512  1.00 46.15 ? 19  PHE A CB  1 
ATOM   74   C CG  . PHE A 1 17  ? 7.585   -6.354  -8.289  1.00 47.82 ? 19  PHE A CG  1 
ATOM   75   C CD1 . PHE A 1 17  ? 6.684   -5.908  -9.242  1.00 50.11 ? 19  PHE A CD1 1 
ATOM   76   C CD2 . PHE A 1 17  ? 7.084   -6.831  -7.095  1.00 49.41 ? 19  PHE A CD2 1 
ATOM   77   C CE1 . PHE A 1 17  ? 5.318   -6.027  -9.042  1.00 51.09 ? 19  PHE A CE1 1 
ATOM   78   C CE2 . PHE A 1 17  ? 5.710   -6.944  -6.896  1.00 51.04 ? 19  PHE A CE2 1 
ATOM   79   C CZ  . PHE A 1 17  ? 4.837   -6.564  -7.881  1.00 51.12 ? 19  PHE A CZ  1 
ATOM   80   N N   . LEU A 1 18  ? 10.539  -5.417  -5.901  1.00 41.11 ? 20  LEU A N   1 
ATOM   81   C CA  . LEU A 1 18  ? 10.564  -5.338  -4.441  1.00 38.79 ? 20  LEU A CA  1 
ATOM   82   C C   . LEU A 1 18  ? 10.760  -3.909  -3.953  1.00 40.00 ? 20  LEU A C   1 
ATOM   83   O O   . LEU A 1 18  ? 10.103  -3.488  -2.998  1.00 41.31 ? 20  LEU A O   1 
ATOM   84   C CB  . LEU A 1 18  ? 11.661  -6.289  -3.913  1.00 36.97 ? 20  LEU A CB  1 
ATOM   85   C CG  . LEU A 1 18  ? 11.397  -7.783  -4.163  1.00 34.49 ? 20  LEU A CG  1 
ATOM   86   C CD1 . LEU A 1 18  ? 12.633  -8.643  -3.800  1.00 31.93 ? 20  LEU A CD1 1 
ATOM   87   C CD2 . LEU A 1 18  ? 10.207  -8.308  -3.431  1.00 38.72 ? 20  LEU A CD2 1 
ATOM   88   N N   . MET A 1 19  ? 11.632  -3.168  -4.614  1.00 40.72 ? 21  MET A N   1 
ATOM   89   C CA  . MET A 1 19  ? 11.950  -1.807  -4.270  1.00 44.66 ? 21  MET A CA  1 
ATOM   90   C C   . MET A 1 19  ? 10.753  -0.881  -4.536  1.00 49.11 ? 21  MET A C   1 
ATOM   91   O O   . MET A 1 19  ? 10.667  0.133   -3.865  1.00 51.76 ? 21  MET A O   1 
ATOM   92   C CB  . MET A 1 19  ? 13.177  -1.296  -5.054  1.00 46.14 ? 21  MET A CB  1 
ATOM   93   C CG  . MET A 1 19  ? 14.491  -1.975  -4.716  1.00 48.80 ? 21  MET A CG  1 
ATOM   94   S SD  . MET A 1 19  ? 15.026  -1.904  -2.973  1.00 49.79 ? 21  MET A SD  1 
ATOM   95   C CE  . MET A 1 19  ? 15.026  -0.101  -2.747  1.00 58.30 ? 21  MET A CE  1 
ATOM   96   N N   . ALA A 1 20  ? 9.855   -1.208  -5.482  1.00 51.66 ? 22  ALA A N   1 
ATOM   97   C CA  . ALA A 1 20  ? 8.619   -0.419  -5.762  1.00 53.04 ? 22  ALA A CA  1 
ATOM   98   C C   . ALA A 1 20  ? 7.553   -0.651  -4.661  1.00 55.74 ? 22  ALA A C   1 
ATOM   99   O O   . ALA A 1 20  ? 6.754   0.239   -4.398  1.00 57.66 ? 22  ALA A O   1 
ATOM   100  C CB  . ALA A 1 20  ? 8.034   -0.832  -7.118  1.00 52.56 ? 22  ALA A CB  1 
ATOM   101  N N   . CYS A 1 21  ? 7.530   -1.859  -4.028  1.00 54.14 ? 23  CYS A N   1 
ATOM   102  C CA  . CYS A 1 21  ? 6.597   -2.185  -2.930  1.00 53.23 ? 23  CYS A CA  1 
ATOM   103  C C   . CYS A 1 21  ? 6.978   -1.604  -1.593  1.00 54.16 ? 23  CYS A C   1 
ATOM   104  O O   . CYS A 1 21  ? 6.273   -1.867  -0.603  1.00 55.45 ? 23  CYS A O   1 
ATOM   105  C CB  . CYS A 1 21  ? 6.446   -3.685  -2.773  1.00 52.87 ? 23  CYS A CB  1 
ATOM   106  S SG  . CYS A 1 21  ? 5.876   -4.557  -4.233  1.00 56.85 ? 23  CYS A SG  1 
ATOM   107  N N   . ARG A 1 22  ? 8.068   -0.900  -1.521  1.00 54.21 ? 24  ARG A N   1 
ATOM   108  C CA  . ARG A 1 22  ? 8.577   -0.385  -0.273  1.00 57.62 ? 24  ARG A CA  1 
ATOM   109  C C   . ARG A 1 22  ? 7.874   0.959   0.067   1.00 63.02 ? 24  ARG A C   1 
ATOM   110  O O   . ARG A 1 22  ? 7.560   1.742   -0.842  1.00 63.18 ? 24  ARG A O   1 
ATOM   111  C CB  . ARG A 1 22  ? 10.062  -0.169  -0.411  1.00 57.10 ? 24  ARG A CB  1 
ATOM   112  C CG  . ARG A 1 22  ? 10.687  0.400   0.809   1.00 58.96 ? 24  ARG A CG  1 
ATOM   113  C CD  . ARG A 1 22  ? 12.072  0.805   0.482   1.00 58.26 ? 24  ARG A CD  1 
ATOM   114  N NE  . ARG A 1 22  ? 12.820  1.054   1.708   1.00 57.95 ? 24  ARG A NE  1 
ATOM   115  C CZ  . ARG A 1 22  ? 14.143  1.121   1.795   1.00 55.99 ? 24  ARG A CZ  1 
ATOM   116  N NH1 . ARG A 1 22  ? 14.897  0.955   0.720   1.00 55.90 ? 24  ARG A NH1 1 
ATOM   117  N NH2 . ARG A 1 22  ? 14.722  1.339   2.958   1.00 56.60 ? 24  ARG A NH2 1 
ATOM   118  N N   . GLY A 1 23  ? 7.664   1.203   1.361   1.00 66.43 ? 25  GLY A N   1 
ATOM   119  C CA  . GLY A 1 23  ? 7.084   2.453   1.850   1.00 70.51 ? 25  GLY A CA  1 
ATOM   120  C C   . GLY A 1 23  ? 5.774   2.826   1.187   1.00 74.14 ? 25  GLY A C   1 
ATOM   121  O O   . GLY A 1 23  ? 5.490   4.016   0.983   1.00 74.83 ? 25  GLY A O   1 
ATOM   122  N N   . GLY A 1 24  ? 4.983   1.801   0.868   1.00 75.75 ? 26  GLY A N   1 
ATOM   123  C CA  . GLY A 1 24  ? 3.871   1.921   -0.066  1.00 77.53 ? 26  GLY A CA  1 
ATOM   124  C C   . GLY A 1 24  ? 2.678   2.681   0.461   1.00 79.03 ? 26  GLY A C   1 
ATOM   125  O O   . GLY A 1 24  ? 2.187   3.601   -0.199  1.00 79.66 ? 26  GLY A O   1 
ATOM   126  N N   . GLY A 1 25  ? 2.208   2.308   1.648   1.00 79.38 ? 27  GLY A N   1 
ATOM   127  C CA  . GLY A 1 25  ? 0.944   2.830   2.164   1.00 79.51 ? 27  GLY A CA  1 
ATOM   128  C C   . GLY A 1 25  ? -0.280  2.328   1.408   1.00 79.28 ? 27  GLY A C   1 
ATOM   129  O O   . GLY A 1 25  ? -1.349  2.962   1.435   1.00 79.41 ? 27  GLY A O   1 
ATOM   130  N N   . GLY A 1 26  ? -0.137  1.185   0.733   1.00 78.19 ? 28  GLY A N   1 
ATOM   131  C CA  . GLY A 1 26  ? -1.236  0.620   -0.034  1.00 77.34 ? 28  GLY A CA  1 
ATOM   132  C C   . GLY A 1 26  ? -2.378  0.184   0.859   1.00 75.04 ? 28  GLY A C   1 
ATOM   133  O O   . GLY A 1 26  ? -2.163  -0.242  2.001   1.00 75.48 ? 28  GLY A O   1 
ATOM   134  N N   . GLU A 1 27  ? -3.604  0.301   0.351   1.00 72.32 ? 29  GLU A N   1 
ATOM   135  C CA  . GLU A 1 27  ? -4.760  -0.176  1.067   1.00 69.08 ? 29  GLU A CA  1 
ATOM   136  C C   . GLU A 1 27  ? -4.782  -1.697  0.830   1.00 66.06 ? 29  GLU A C   1 
ATOM   137  O O   . GLU A 1 27  ? -4.937  -2.160  -0.326  1.00 68.45 ? 29  GLU A O   1 
ATOM   138  C CB  . GLU A 1 27  ? -6.033  0.490   0.540   1.00 72.49 ? 29  GLU A CB  1 
ATOM   139  C CG  . GLU A 1 27  ? -6.085  2.001   0.694   1.00 78.41 ? 29  GLU A CG  1 
ATOM   140  C CD  . GLU A 1 27  ? -6.812  2.420   1.958   1.00 85.31 ? 29  GLU A CD  1 
ATOM   141  O OE1 . GLU A 1 27  ? -8.068  2.397   1.964   1.00 84.91 ? 29  GLU A OE1 1 
ATOM   142  O OE2 . GLU A 1 27  ? -6.120  2.768   2.945   1.00 87.68 ? 29  GLU A OE2 1 
ATOM   143  N N   . ASN A 1 28  ? -4.623  -2.486  1.902   1.00 59.21 ? 30  ASN A N   1 
ATOM   144  C CA  . ASN A 1 28  ? -4.652  -3.931  1.771   1.00 52.36 ? 30  ASN A CA  1 
ATOM   145  C C   . ASN A 1 28  ? -6.153  -4.314  1.726   1.00 46.90 ? 30  ASN A C   1 
ATOM   146  O O   . ASN A 1 28  ? -6.608  -5.047  2.604   1.00 44.39 ? 30  ASN A O   1 
ATOM   147  C CB  . ASN A 1 28  ? -3.932  -4.570  2.945   1.00 50.24 ? 30  ASN A CB  1 
ATOM   148  C CG  . ASN A 1 28  ? -3.834  -6.052  2.856   1.00 49.25 ? 30  ASN A CG  1 
ATOM   149  O OD1 . ASN A 1 28  ? -3.951  -6.637  1.797   1.00 49.05 ? 30  ASN A OD1 1 
ATOM   150  N ND2 . ASN A 1 28  ? -3.619  -6.705  3.969   1.00 51.03 ? 30  ASN A ND2 1 
ATOM   151  N N   . LEU A 1 29  ? -6.892  -3.807  0.693   1.00 45.06 ? 31  LEU A N   1 
ATOM   152  C CA  . LEU A 1 29  ? -8.324  -4.073  0.445   1.00 46.79 ? 31  LEU A CA  1 
ATOM   153  C C   . LEU A 1 29  ? -8.548  -5.558  0.413   1.00 43.83 ? 31  LEU A C   1 
ATOM   154  O O   . LEU A 1 29  ? -7.858  -6.278  -0.287  1.00 43.31 ? 31  LEU A O   1 
ATOM   155  C CB  . LEU A 1 29  ? -8.798  -3.499  -0.935  1.00 50.46 ? 31  LEU A CB  1 
ATOM   156  C CG  . LEU A 1 29  ? -9.453  -2.123  -1.020  1.00 58.24 ? 31  LEU A CG  1 
ATOM   157  C CD1 . LEU A 1 29  ? -8.785  -1.185  -0.160  1.00 59.73 ? 31  LEU A CD1 1 
ATOM   158  C CD2 . LEU A 1 29  ? -9.410  -1.565  -2.458  1.00 60.13 ? 31  LEU A CD2 1 
ATOM   159  N N   . TYR A 1 30  ? -9.532  -6.012  1.162   1.00 42.70 ? 32  TYR A N   1 
ATOM   160  C CA  . TYR A 1 30  ? -9.970  -7.376  1.198   1.00 43.17 ? 32  TYR A CA  1 
ATOM   161  C C   . TYR A 1 30  ? -8.883  -8.333  1.760   1.00 42.03 ? 32  TYR A C   1 
ATOM   162  O O   . TYR A 1 30  ? -9.039  -9.549  1.581   1.00 41.34 ? 32  TYR A O   1 
ATOM   163  C CB  . TYR A 1 30  ? -10.417 -7.818  -0.185  1.00 44.42 ? 32  TYR A CB  1 
ATOM   164  C CG  . TYR A 1 30  ? -11.463 -6.947  -0.823  1.00 46.35 ? 32  TYR A CG  1 
ATOM   165  C CD1 . TYR A 1 30  ? -12.774 -6.982  -0.391  1.00 47.72 ? 32  TYR A CD1 1 
ATOM   166  C CD2 . TYR A 1 30  ? -11.140 -6.077  -1.864  1.00 47.45 ? 32  TYR A CD2 1 
ATOM   167  C CE1 . TYR A 1 30  ? -13.743 -6.222  -0.995  1.00 49.84 ? 32  TYR A CE1 1 
ATOM   168  C CE2 . TYR A 1 30  ? -12.119 -5.295  -2.475  1.00 49.81 ? 32  TYR A CE2 1 
ATOM   169  C CZ  . TYR A 1 30  ? -13.414 -5.349  -2.006  1.00 51.04 ? 32  TYR A CZ  1 
ATOM   170  O OH  . TYR A 1 30  ? -14.477 -4.652  -2.552  1.00 56.48 ? 32  TYR A OH  1 
ATOM   171  N N   . PHE A 1 31  ? -7.839  -7.803  2.438   1.00 42.95 ? 33  PHE A N   1 
ATOM   172  C CA  . PHE A 1 31  ? -6.610  -8.554  2.793   1.00 44.82 ? 33  PHE A CA  1 
ATOM   173  C C   . PHE A 1 31  ? -5.986  -9.251  1.597   1.00 45.17 ? 33  PHE A C   1 
ATOM   174  O O   . PHE A 1 31  ? -5.338  -10.283 1.765   1.00 45.05 ? 33  PHE A O   1 
ATOM   175  C CB  . PHE A 1 31  ? -6.899  -9.569  3.897   1.00 46.08 ? 33  PHE A CB  1 
ATOM   176  C CG  . PHE A 1 31  ? -7.261  -8.905  5.190   1.00 48.30 ? 33  PHE A CG  1 
ATOM   177  C CD1 . PHE A 1 31  ? -6.280  -8.423  6.037   1.00 50.20 ? 33  PHE A CD1 1 
ATOM   178  C CD2 . PHE A 1 31  ? -8.577  -8.758  5.558   1.00 50.07 ? 33  PHE A CD2 1 
ATOM   179  C CE1 . PHE A 1 31  ? -6.622  -7.827  7.240   1.00 51.96 ? 33  PHE A CE1 1 
ATOM   180  C CE2 . PHE A 1 31  ? -8.911  -8.162  6.758   1.00 51.82 ? 33  PHE A CE2 1 
ATOM   181  C CZ  . PHE A 1 31  ? -7.941  -7.685  7.577   1.00 51.81 ? 33  PHE A CZ  1 
ATOM   182  N N   . GLN A 1 32  ? -6.161  -8.690  0.383   1.00 44.73 ? 34  GLN A N   1 
ATOM   183  C CA  . GLN A 1 32  ? -5.658  -9.291  -0.863  1.00 45.53 ? 34  GLN A CA  1 
ATOM   184  C C   . GLN A 1 32  ? -4.710  -8.318  -1.625  1.00 45.71 ? 34  GLN A C   1 
ATOM   185  O O   . GLN A 1 32  ? -4.430  -8.557  -2.776  1.00 48.19 ? 34  GLN A O   1 
ATOM   186  C CB  . GLN A 1 32  ? -6.814  -9.729  -1.773  1.00 45.39 ? 34  GLN A CB  1 
ATOM   187  C CG  . GLN A 1 32  ? -7.684  -10.826 -1.145  1.00 47.85 ? 34  GLN A CG  1 
ATOM   188  C CD  . GLN A 1 32  ? -8.765  -11.329 -2.058  1.00 50.50 ? 34  GLN A CD  1 
ATOM   189  O OE1 . GLN A 1 32  ? -8.564  -11.540 -3.242  1.00 48.53 ? 34  GLN A OE1 1 
ATOM   190  N NE2 . GLN A 1 32  ? -9.980  -11.574 -1.526  1.00 51.42 ? 34  GLN A NE2 1 
ATOM   191  N N   . GLY A 1 33  ? -4.259  -7.264  -0.982  1.00 43.49 ? 35  GLY A N   1 
ATOM   192  C CA  . GLY A 1 33  ? -3.510  -6.186  -1.594  1.00 43.75 ? 35  GLY A CA  1 
ATOM   193  C C   . GLY A 1 33  ? -1.998  -6.369  -1.340  1.00 45.96 ? 35  GLY A C   1 
ATOM   194  O O   . GLY A 1 33  ? -1.189  -5.633  -1.902  1.00 48.76 ? 35  GLY A O   1 
ATOM   195  N N   . LYS A 1 34  ? -1.596  -7.324  -0.490  1.00 45.20 ? 36  LYS A N   1 
ATOM   196  C CA  . LYS A 1 34  ? -0.162  -7.569  -0.246  1.00 45.41 ? 36  LYS A CA  1 
ATOM   197  C C   . LYS A 1 34  ? 0.363   -8.601  -1.209  1.00 45.83 ? 36  LYS A C   1 
ATOM   198  O O   . LYS A 1 34  ? -0.398  -9.446  -1.723  1.00 47.23 ? 36  LYS A O   1 
ATOM   199  C CB  . LYS A 1 34  ? 0.071   -7.999  1.207   1.00 45.96 ? 36  LYS A CB  1 
ATOM   200  C CG  . LYS A 1 34  ? -0.030  -6.824  2.164   1.00 46.10 ? 36  LYS A CG  1 
ATOM   201  C CD  . LYS A 1 34  ? 0.113   -7.272  3.582   1.00 48.85 ? 36  LYS A CD  1 
ATOM   202  C CE  . LYS A 1 34  ? 0.123   -6.093  4.512   1.00 51.66 ? 36  LYS A CE  1 
ATOM   203  N NZ  . LYS A 1 34  ? 0.200   -6.548  5.913   1.00 55.81 ? 36  LYS A NZ  1 
ATOM   204  N N   . HIS A 1 35  ? 1.661   -8.554  -1.458  1.00 43.45 ? 37  HIS A N   1 
ATOM   205  C CA  . HIS A 1 35  ? 2.278   -9.412  -2.434  1.00 43.64 ? 37  HIS A CA  1 
ATOM   206  C C   . HIS A 1 35  ? 2.879   -10.605 -1.718  1.00 42.63 ? 37  HIS A C   1 
ATOM   207  O O   . HIS A 1 35  ? 3.826   -10.423 -0.962  1.00 41.46 ? 37  HIS A O   1 
ATOM   208  C CB  . HIS A 1 35  ? 3.335   -8.640  -3.219  1.00 46.06 ? 37  HIS A CB  1 
ATOM   209  C CG  . HIS A 1 35  ? 2.736   -7.630  -4.129  1.00 49.78 ? 37  HIS A CG  1 
ATOM   210  N ND1 . HIS A 1 35  ? 2.608   -6.299  -3.753  1.00 53.21 ? 37  HIS A ND1 1 
ATOM   211  C CD2 . HIS A 1 35  ? 2.232   -7.783  -5.377  1.00 50.86 ? 37  HIS A CD2 1 
ATOM   212  C CE1 . HIS A 1 35  ? 2.030   -5.695  -4.777  1.00 53.18 ? 37  HIS A CE1 1 
ATOM   213  N NE2 . HIS A 1 35  ? 1.790   -6.556  -5.776  1.00 52.17 ? 37  HIS A NE2 1 
ATOM   214  N N   . PRO A 1 36  ? 2.336   -11.816 -1.922  1.00 41.71 ? 38  PRO A N   1 
ATOM   215  C CA  . PRO A 1 36  ? 2.808   -12.970 -1.149  1.00 39.94 ? 38  PRO A CA  1 
ATOM   216  C C   . PRO A 1 36  ? 4.209   -13.396 -1.546  1.00 38.90 ? 38  PRO A C   1 
ATOM   217  O O   . PRO A 1 36  ? 4.593   -13.285 -2.707  1.00 37.05 ? 38  PRO A O   1 
ATOM   218  C CB  . PRO A 1 36  ? 1.778   -14.058 -1.479  1.00 42.43 ? 38  PRO A CB  1 
ATOM   219  C CG  . PRO A 1 36  ? 1.276   -13.690 -2.804  1.00 43.78 ? 38  PRO A CG  1 
ATOM   220  C CD  . PRO A 1 36  ? 1.222   -12.212 -2.833  1.00 42.20 ? 38  PRO A CD  1 
ATOM   221  N N   . LEU A 1 37  ? 4.972   -13.881 -0.553  1.00 37.21 ? 39  LEU A N   1 
ATOM   222  C CA  . LEU A 1 37  ? 6.257   -14.521 -0.828  1.00 35.41 ? 39  LEU A CA  1 
ATOM   223  C C   . LEU A 1 37  ? 6.072   -15.991 -1.044  1.00 34.90 ? 39  LEU A C   1 
ATOM   224  O O   . LEU A 1 37  ? 5.123   -16.572 -0.517  1.00 35.39 ? 39  LEU A O   1 
ATOM   225  C CB  . LEU A 1 37  ? 7.211   -14.262 0.372   1.00 34.18 ? 39  LEU A CB  1 
ATOM   226  C CG  . LEU A 1 37  ? 7.590   -12.812 0.658   1.00 34.69 ? 39  LEU A CG  1 
ATOM   227  C CD1 . LEU A 1 37  ? 8.518   -12.716 1.876   1.00 35.16 ? 39  LEU A CD1 1 
ATOM   228  C CD2 . LEU A 1 37  ? 8.154   -12.126 -0.550  1.00 34.32 ? 39  LEU A CD2 1 
ATOM   229  N N   . GLN A 1 38  ? 7.011   -16.612 -1.794  1.00 34.84 ? 40  GLN A N   1 
ATOM   230  C CA  . GLN A 1 38  ? 7.075   -18.054 -2.011  1.00 35.57 ? 40  GLN A CA  1 
ATOM   231  C C   . GLN A 1 38  ? 7.186   -18.799 -0.691  1.00 35.93 ? 40  GLN A C   1 
ATOM   232  O O   . GLN A 1 38  ? 6.540   -19.832 -0.481  1.00 37.10 ? 40  GLN A O   1 
ATOM   233  C CB  . GLN A 1 38  ? 8.289   -18.376 -2.893  1.00 36.44 ? 40  GLN A CB  1 
ATOM   234  C CG  . GLN A 1 38  ? 8.527   -19.865 -3.187  1.00 38.16 ? 40  GLN A CG  1 
ATOM   235  C CD  . GLN A 1 38  ? 7.405   -20.498 -4.000  1.00 43.82 ? 40  GLN A CD  1 
ATOM   236  O OE1 . GLN A 1 38  ? 6.656   -19.801 -4.706  1.00 41.83 ? 40  GLN A OE1 1 
ATOM   237  N NE2 . GLN A 1 38  ? 7.292   -21.808 -3.922  1.00 45.31 ? 40  GLN A NE2 1 
ATOM   238  N N   . ASN A 1 39  ? 8.022   -18.254 0.236   1.00 34.10 ? 41  ASN A N   1 
ATOM   239  C CA  . ASN A 1 39  ? 8.289   -18.829 1.536   1.00 34.06 ? 41  ASN A CA  1 
ATOM   240  C C   . ASN A 1 39  ? 7.937   -17.876 2.646   1.00 31.79 ? 41  ASN A C   1 
ATOM   241  O O   . ASN A 1 39  ? 7.961   -16.672 2.447   1.00 32.92 ? 41  ASN A O   1 
ATOM   242  C CB  . ASN A 1 39  ? 9.787   -19.191 1.607   1.00 36.02 ? 41  ASN A CB  1 
ATOM   243  C CG  . ASN A 1 39  ? 10.109  -20.408 0.789   1.00 41.48 ? 41  ASN A CG  1 
ATOM   244  O OD1 . ASN A 1 39  ? 9.760   -21.503 1.174   1.00 42.96 ? 41  ASN A OD1 1 
ATOM   245  N ND2 . ASN A 1 39  ? 10.776  -20.256 -0.339  1.00 42.89 ? 41  ASN A ND2 1 
ATOM   246  N N   . ARG A 1 40  ? 7.641   -18.412 3.838   1.00 31.11 ? 42  ARG A N   1 
ATOM   247  C CA  . ARG A 1 40  ? 7.596   -17.622 5.058   1.00 32.04 ? 42  ARG A CA  1 
ATOM   248  C C   . ARG A 1 40  ? 9.057   -17.617 5.625   1.00 30.36 ? 42  ARG A C   1 
ATOM   249  O O   . ARG A 1 40  ? 9.767   -18.626 5.541   1.00 30.39 ? 42  ARG A O   1 
ATOM   250  C CB  . ARG A 1 40  ? 6.657   -18.228 6.088   1.00 36.30 ? 42  ARG A CB  1 
ATOM   251  C CG  . ARG A 1 40  ? 6.535   -17.435 7.350   1.00 44.79 ? 42  ARG A CG  1 
ATOM   252  C CD  . ARG A 1 40  ? 5.136   -17.695 7.901   1.00 55.98 ? 42  ARG A CD  1 
ATOM   253  N NE  . ARG A 1 40  ? 4.804   -16.915 9.087   1.00 67.20 ? 42  ARG A NE  1 
ATOM   254  C CZ  . ARG A 1 40  ? 3.578   -16.565 9.437   1.00 77.55 ? 42  ARG A CZ  1 
ATOM   255  N NH1 . ARG A 1 40  ? 2.531   -16.933 8.695   1.00 79.97 ? 42  ARG A NH1 1 
ATOM   256  N NH2 . ARG A 1 40  ? 3.376   -15.845 10.535  1.00 80.76 ? 42  ARG A NH2 1 
ATOM   257  N N   . TRP A 1 41  ? 9.461   -16.483 6.133   1.00 30.34 ? 43  TRP A N   1 
ATOM   258  C CA  . TRP A 1 41  ? 10.837  -16.205 6.595   1.00 30.67 ? 43  TRP A CA  1 
ATOM   259  C C   . TRP A 1 41  ? 10.796  -15.754 8.049   1.00 31.39 ? 43  TRP A C   1 
ATOM   260  O O   . TRP A 1 41  ? 9.814   -15.120 8.472   1.00 32.58 ? 43  TRP A O   1 
ATOM   261  C CB  . TRP A 1 41  ? 11.493  -15.089 5.711   1.00 29.28 ? 43  TRP A CB  1 
ATOM   262  C CG  . TRP A 1 41  ? 11.709  -15.524 4.290   1.00 29.42 ? 43  TRP A CG  1 
ATOM   263  C CD1 . TRP A 1 41  ? 10.835  -15.361 3.266   1.00 29.52 ? 43  TRP A CD1 1 
ATOM   264  C CD2 . TRP A 1 41  ? 12.855  -16.210 3.726   1.00 27.52 ? 43  TRP A CD2 1 
ATOM   265  N NE1 . TRP A 1 41  ? 11.346  -15.894 2.123   1.00 30.12 ? 43  TRP A NE1 1 
ATOM   266  C CE2 . TRP A 1 41  ? 12.571  -16.445 2.376   1.00 27.86 ? 43  TRP A CE2 1 
ATOM   267  C CE3 . TRP A 1 41  ? 14.067  -16.652 4.231   1.00 26.35 ? 43  TRP A CE3 1 
ATOM   268  C CZ2 . TRP A 1 41  ? 13.468  -17.070 1.517   1.00 28.92 ? 43  TRP A CZ2 1 
ATOM   269  C CZ3 . TRP A 1 41  ? 14.963  -17.274 3.380   1.00 26.75 ? 43  TRP A CZ3 1 
ATOM   270  C CH2 . TRP A 1 41  ? 14.660  -17.492 2.048   1.00 27.85 ? 43  TRP A CH2 1 
ATOM   271  N N   . ALA A 1 42  ? 11.855  -16.043 8.803   1.00 28.03 ? 44  ALA A N   1 
ATOM   272  C CA  . ALA A 1 42  ? 11.995  -15.672 10.179  1.00 28.38 ? 44  ALA A CA  1 
ATOM   273  C C   . ALA A 1 42  ? 13.276  -14.881 10.327  1.00 27.59 ? 44  ALA A C   1 
ATOM   274  O O   . ALA A 1 42  ? 14.346  -15.341 9.830   1.00 28.52 ? 44  ALA A O   1 
ATOM   275  C CB  . ALA A 1 42  ? 12.053  -16.909 11.058  1.00 27.85 ? 44  ALA A CB  1 
ATOM   276  N N   . LEU A 1 43  ? 13.203  -13.734 10.984  1.00 27.19 ? 45  LEU A N   1 
ATOM   277  C CA  . LEU A 1 43  ? 14.365  -12.911 11.315  1.00 27.87 ? 45  LEU A CA  1 
ATOM   278  C C   . LEU A 1 43  ? 14.797  -13.224 12.722  1.00 28.92 ? 45  LEU A C   1 
ATOM   279  O O   . LEU A 1 43  ? 13.982  -13.152 13.633  1.00 28.80 ? 45  LEU A O   1 
ATOM   280  C CB  . LEU A 1 43  ? 14.060  -11.414 11.234  1.00 28.96 ? 45  LEU A CB  1 
ATOM   281  C CG  . LEU A 1 43  ? 15.215  -10.487 11.620  1.00 30.97 ? 45  LEU A CG  1 
ATOM   282  C CD1 . LEU A 1 43  ? 16.354  -10.619 10.652  1.00 32.07 ? 45  LEU A CD1 1 
ATOM   283  C CD2 . LEU A 1 43  ? 14.758  -9.098  11.694  1.00 36.17 ? 45  LEU A CD2 1 
ATOM   284  N N   . TRP A 1 44  ? 16.060  -13.527 12.887  1.00 28.44 ? 46  TRP A N   1 
ATOM   285  C CA  . TRP A 1 44  ? 16.704  -13.865 14.138  1.00 28.37 ? 46  TRP A CA  1 
ATOM   286  C C   . TRP A 1 44  ? 17.779  -12.895 14.484  1.00 30.01 ? 46  TRP A C   1 
ATOM   287  O O   . TRP A 1 44  ? 18.422  -12.258 13.590  1.00 29.25 ? 46  TRP A O   1 
ATOM   288  C CB  . TRP A 1 44  ? 17.372  -15.250 14.028  1.00 28.50 ? 46  TRP A CB  1 
ATOM   289  C CG  . TRP A 1 44  ? 16.509  -16.376 13.622  1.00 30.14 ? 46  TRP A CG  1 
ATOM   290  C CD1 . TRP A 1 44  ? 16.058  -16.700 12.377  1.00 29.29 ? 46  TRP A CD1 1 
ATOM   291  C CD2 . TRP A 1 44  ? 15.951  -17.343 14.510  1.00 32.56 ? 46  TRP A CD2 1 
ATOM   292  N NE1 . TRP A 1 44  ? 15.265  -17.812 12.438  1.00 30.80 ? 46  TRP A NE1 1 
ATOM   293  C CE2 . TRP A 1 44  ? 15.168  -18.222 13.736  1.00 31.96 ? 46  TRP A CE2 1 
ATOM   294  C CE3 . TRP A 1 44  ? 16.034  -17.536 15.895  1.00 35.35 ? 46  TRP A CE3 1 
ATOM   295  C CZ2 . TRP A 1 44  ? 14.506  -19.311 14.285  1.00 34.36 ? 46  TRP A CZ2 1 
ATOM   296  C CZ3 . TRP A 1 44  ? 15.359  -18.609 16.435  1.00 39.25 ? 46  TRP A CZ3 1 
ATOM   297  C CH2 . TRP A 1 44  ? 14.599  -19.473 15.634  1.00 38.01 ? 46  TRP A CH2 1 
ATOM   298  N N   . PHE A 1 45  ? 18.052  -12.778 15.783  1.00 30.07 ? 47  PHE A N   1 
ATOM   299  C CA  . PHE A 1 45  ? 19.060  -11.857 16.303  1.00 33.53 ? 47  PHE A CA  1 
ATOM   300  C C   . PHE A 1 45  ? 19.850  -12.616 17.357  1.00 36.07 ? 47  PHE A C   1 
ATOM   301  O O   . PHE A 1 45  ? 19.264  -13.306 18.191  1.00 37.36 ? 47  PHE A O   1 
ATOM   302  C CB  . PHE A 1 45  ? 18.382  -10.623 16.902  1.00 35.94 ? 47  PHE A CB  1 
ATOM   303  C CG  . PHE A 1 45  ? 19.302  -9.698  17.650  1.00 40.08 ? 47  PHE A CG  1 
ATOM   304  C CD1 . PHE A 1 45  ? 20.235  -8.925  16.973  1.00 41.61 ? 47  PHE A CD1 1 
ATOM   305  C CD2 . PHE A 1 45  ? 19.221  -9.581  19.021  1.00 44.13 ? 47  PHE A CD2 1 
ATOM   306  C CE1 . PHE A 1 45  ? 21.067  -8.056  17.654  1.00 43.30 ? 47  PHE A CE1 1 
ATOM   307  C CE2 . PHE A 1 45  ? 20.048  -8.713  19.700  1.00 46.15 ? 47  PHE A CE2 1 
ATOM   308  C CZ  . PHE A 1 45  ? 20.981  -7.972  19.018  1.00 45.40 ? 47  PHE A CZ  1 
ATOM   309  N N   . PHE A 1 46  ? 21.133  -12.479 17.336  1.00 36.32 ? 48  PHE A N   1 
ATOM   310  C CA  . PHE A 1 46  ? 22.000  -13.034 18.327  1.00 41.91 ? 48  PHE A CA  1 
ATOM   311  C C   . PHE A 1 46  ? 22.742  -11.880 18.990  1.00 46.87 ? 48  PHE A C   1 
ATOM   312  O O   . PHE A 1 46  ? 23.436  -11.138 18.303  1.00 46.19 ? 48  PHE A O   1 
ATOM   313  C CB  . PHE A 1 46  ? 22.907  -14.038 17.705  1.00 43.97 ? 48  PHE A CB  1 
ATOM   314  C CG  . PHE A 1 46  ? 23.780  -14.785 18.661  1.00 48.57 ? 48  PHE A CG  1 
ATOM   315  C CD1 . PHE A 1 46  ? 23.404  -16.028 19.140  1.00 50.77 ? 48  PHE A CD1 1 
ATOM   316  C CD2 . PHE A 1 46  ? 24.998  -14.258 19.064  1.00 51.69 ? 48  PHE A CD2 1 
ATOM   317  C CE1 . PHE A 1 46  ? 24.235  -16.733 20.005  1.00 52.89 ? 48  PHE A CE1 1 
ATOM   318  C CE2 . PHE A 1 46  ? 25.830  -14.960 19.938  1.00 53.07 ? 48  PHE A CE2 1 
ATOM   319  C CZ  . PHE A 1 46  ? 25.450  -16.189 20.398  1.00 52.74 ? 48  PHE A CZ  1 
ATOM   320  N N   . LYS A 1 47  ? 22.552  -11.707 20.314  1.00 51.21 ? 49  LYS A N   1 
ATOM   321  C CA  . LYS A 1 47  ? 23.204  -10.644 21.100  1.00 56.00 ? 49  LYS A CA  1 
ATOM   322  C C   . LYS A 1 47  ? 24.520  -11.143 21.670  1.00 60.93 ? 49  LYS A C   1 
ATOM   323  O O   . LYS A 1 47  ? 24.654  -12.323 22.051  1.00 61.25 ? 49  LYS A O   1 
ATOM   324  C CB  . LYS A 1 47  ? 22.298  -10.195 22.250  1.00 60.35 ? 49  LYS A CB  1 
ATOM   325  C CG  . LYS A 1 47  ? 22.878  -9.085  23.146  1.00 66.37 ? 49  LYS A CG  1 
ATOM   326  C CD  . LYS A 1 47  ? 23.003  -7.722  22.443  1.00 73.41 ? 49  LYS A CD  1 
ATOM   327  C CE  . LYS A 1 47  ? 22.149  -6.669  23.118  1.00 78.60 ? 49  LYS A CE  1 
ATOM   328  N NZ  . LYS A 1 47  ? 22.583  -6.370  24.524  1.00 78.69 ? 49  LYS A NZ  1 
ATOM   329  N N   . ASN A 1 48  ? 25.499  -10.226 21.706  1.00 64.61 ? 50  ASN A N   1 
ATOM   330  C CA  . ASN A 1 48  ? 26.750  -10.364 22.453  1.00 68.39 ? 50  ASN A CA  1 
ATOM   331  C C   . ASN A 1 48  ? 26.503  -10.008 23.936  1.00 70.52 ? 50  ASN A C   1 
ATOM   332  O O   . ASN A 1 48  ? 26.641  -8.859  24.345  1.00 70.62 ? 50  ASN A O   1 
ATOM   333  C CB  . ASN A 1 48  ? 27.807  -9.431  21.860  1.00 71.44 ? 50  ASN A CB  1 
ATOM   334  C CG  . ASN A 1 48  ? 29.180  -9.628  22.453  1.00 76.79 ? 50  ASN A CG  1 
ATOM   335  O OD1 . ASN A 1 48  ? 29.715  -10.742 22.466  1.00 78.88 ? 50  ASN A OD1 1 
ATOM   336  N ND2 . ASN A 1 48  ? 29.793  -8.560  22.951  1.00 78.44 ? 50  ASN A ND2 1 
ATOM   337  N N   . ASP A 1 49  ? 26.118  -11.007 24.718  1.00 71.85 ? 51  ASP A N   1 
ATOM   338  C CA  . ASP A 1 49  ? 25.962  -10.890 26.167  1.00 72.90 ? 51  ASP A CA  1 
ATOM   339  C C   . ASP A 1 49  ? 26.516  -12.186 26.740  1.00 73.57 ? 51  ASP A C   1 
ATOM   340  O O   . ASP A 1 49  ? 25.772  -13.121 26.998  1.00 74.05 ? 51  ASP A O   1 
ATOM   341  C CB  . ASP A 1 49  ? 24.486  -10.666 26.539  1.00 74.63 ? 51  ASP A CB  1 
ATOM   342  C CG  . ASP A 1 49  ? 24.229  -10.398 28.005  1.00 78.85 ? 51  ASP A CG  1 
ATOM   343  O OD1 . ASP A 1 49  ? 25.173  -10.561 28.816  1.00 79.08 ? 51  ASP A OD1 1 
ATOM   344  O OD2 . ASP A 1 49  ? 23.080  -10.019 28.347  1.00 80.49 ? 51  ASP A OD2 1 
ATOM   345  N N   . LYS A 1 50  ? 27.840  -12.230 26.922  1.00 73.51 ? 52  LYS A N   1 
ATOM   346  C CA  . LYS A 1 50  ? 28.564  -13.455 27.286  1.00 74.07 ? 52  LYS A CA  1 
ATOM   347  C C   . LYS A 1 50  ? 28.214  -13.966 28.715  1.00 73.41 ? 52  LYS A C   1 
ATOM   348  O O   . LYS A 1 50  ? 28.503  -15.130 29.021  1.00 73.37 ? 52  LYS A O   1 
ATOM   349  C CB  . LYS A 1 50  ? 30.106  -13.242 27.151  1.00 76.43 ? 52  LYS A CB  1 
ATOM   350  C CG  . LYS A 1 50  ? 30.766  -13.883 25.917  1.00 80.46 ? 52  LYS A CG  1 
ATOM   351  C CD  . LYS A 1 50  ? 30.708  -15.430 26.013  1.00 84.62 ? 52  LYS A CD  1 
ATOM   352  C CE  . LYS A 1 50  ? 31.958  -16.135 25.550  1.00 87.22 ? 52  LYS A CE  1 
ATOM   353  N NZ  . LYS A 1 50  ? 32.138  -16.068 24.082  1.00 89.14 ? 52  LYS A NZ  1 
ATOM   354  N N   . SER A 1 51  ? 27.589  -13.104 29.569  1.00 72.71 ? 53  SER A N   1 
ATOM   355  C CA  . SER A 1 51  ? 27.001  -13.492 30.872  1.00 71.72 ? 53  SER A CA  1 
ATOM   356  C C   . SER A 1 51  ? 25.870  -14.522 30.712  1.00 71.22 ? 53  SER A C   1 
ATOM   357  O O   . SER A 1 51  ? 25.624  -15.311 31.626  1.00 71.77 ? 53  SER A O   1 
ATOM   358  C CB  . SER A 1 51  ? 26.492  -12.261 31.634  1.00 71.90 ? 53  SER A CB  1 
ATOM   359  O OG  . SER A 1 51  ? 25.232  -11.777 31.182  1.00 72.37 ? 53  SER A OG  1 
ATOM   360  N N   . LYS A 1 52  ? 25.177  -14.519 29.555  1.00 70.23 ? 54  LYS A N   1 
ATOM   361  C CA  . LYS A 1 52  ? 24.167  -15.526 29.226  1.00 68.46 ? 54  LYS A CA  1 
ATOM   362  C C   . LYS A 1 52  ? 24.770  -16.595 28.340  1.00 66.51 ? 54  LYS A C   1 
ATOM   363  O O   . LYS A 1 52  ? 25.783  -16.347 27.663  1.00 67.04 ? 54  LYS A O   1 
ATOM   364  C CB  . LYS A 1 52  ? 22.965  -14.853 28.561  1.00 70.54 ? 54  LYS A CB  1 
ATOM   365  C CG  . LYS A 1 52  ? 22.366  -13.726 29.402  1.00 76.33 ? 54  LYS A CG  1 
ATOM   366  C CD  . LYS A 1 52  ? 21.168  -13.079 28.710  1.00 82.40 ? 54  LYS A CD  1 
ATOM   367  C CE  . LYS A 1 52  ? 20.440  -12.118 29.625  1.00 87.32 ? 54  LYS A CE  1 
ATOM   368  N NZ  . LYS A 1 52  ? 19.147  -11.663 29.042  1.00 90.92 ? 54  LYS A NZ  1 
ATOM   369  N N   . THR A 1 53  ? 24.179  -17.788 28.339  1.00 64.55 ? 55  THR A N   1 
ATOM   370  C CA  . THR A 1 53  ? 24.581  -18.813 27.359  1.00 64.00 ? 55  THR A CA  1 
ATOM   371  C C   . THR A 1 53  ? 24.204  -18.338 25.941  1.00 63.40 ? 55  THR A C   1 
ATOM   372  O O   . THR A 1 53  ? 23.319  -17.480 25.799  1.00 63.13 ? 55  THR A O   1 
ATOM   373  C CB  . THR A 1 53  ? 23.880  -20.150 27.626  1.00 64.34 ? 55  THR A CB  1 
ATOM   374  O OG1 . THR A 1 53  ? 22.473  -19.956 27.561  1.00 65.56 ? 55  THR A OG1 1 
ATOM   375  C CG2 . THR A 1 53  ? 24.242  -20.770 28.973  1.00 64.91 ? 55  THR A CG2 1 
ATOM   376  N N   . TRP A 1 54  ? 24.866  -18.891 24.899  1.00 62.46 ? 56  TRP A N   1 
ATOM   377  C CA  . TRP A 1 54  ? 24.542  -18.530 23.522  1.00 61.35 ? 56  TRP A CA  1 
ATOM   378  C C   . TRP A 1 54  ? 23.050  -18.893 23.202  1.00 57.48 ? 56  TRP A C   1 
ATOM   379  O O   . TRP A 1 54  ? 22.409  -18.188 22.438  1.00 56.69 ? 56  TRP A O   1 
ATOM   380  C CB  . TRP A 1 54  ? 25.538  -19.174 22.509  1.00 62.69 ? 56  TRP A CB  1 
ATOM   381  C CG  . TRP A 1 54  ? 25.363  -20.645 22.256  1.00 64.23 ? 56  TRP A CG  1 
ATOM   382  C CD1 . TRP A 1 54  ? 26.132  -21.655 22.759  1.00 65.65 ? 56  TRP A CD1 1 
ATOM   383  C CD2 . TRP A 1 54  ? 24.389  -21.269 21.399  1.00 64.68 ? 56  TRP A CD2 1 
ATOM   384  N NE1 . TRP A 1 54  ? 25.685  -22.869 22.287  1.00 66.28 ? 56  TRP A NE1 1 
ATOM   385  C CE2 . TRP A 1 54  ? 24.619  -22.659 21.448  1.00 65.87 ? 56  TRP A CE2 1 
ATOM   386  C CE3 . TRP A 1 54  ? 23.355  -20.788 20.581  1.00 65.19 ? 56  TRP A CE3 1 
ATOM   387  C CZ2 . TRP A 1 54  ? 23.825  -23.571 20.751  1.00 66.75 ? 56  TRP A CZ2 1 
ATOM   388  C CZ3 . TRP A 1 54  ? 22.558  -21.691 19.911  1.00 66.25 ? 56  TRP A CZ3 1 
ATOM   389  C CH2 . TRP A 1 54  ? 22.809  -23.063 19.977  1.00 66.67 ? 56  TRP A CH2 1 
ATOM   390  N N   . GLN A 1 55  ? 22.507  -19.968 23.802  1.00 54.85 ? 57  GLN A N   1 
ATOM   391  C CA  . GLN A 1 55  ? 21.092  -20.377 23.587  1.00 52.73 ? 57  GLN A CA  1 
ATOM   392  C C   . GLN A 1 55  ? 20.036  -19.318 24.046  1.00 48.54 ? 57  GLN A C   1 
ATOM   393  O O   . GLN A 1 55  ? 19.016  -19.103 23.401  1.00 46.83 ? 57  GLN A O   1 
ATOM   394  C CB  . GLN A 1 55  ? 20.819  -21.712 24.283  1.00 55.85 ? 57  GLN A CB  1 
ATOM   395  C CG  . GLN A 1 55  ? 21.530  -22.930 23.627  1.00 62.94 ? 57  GLN A CG  1 
ATOM   396  C CD  . GLN A 1 55  ? 22.862  -23.277 24.253  1.00 71.45 ? 57  GLN A CD  1 
ATOM   397  O OE1 . GLN A 1 55  ? 23.537  -22.449 24.880  1.00 73.04 ? 57  GLN A OE1 1 
ATOM   398  N NE2 . GLN A 1 55  ? 23.276  -24.527 24.085  1.00 74.47 ? 57  GLN A NE2 1 
ATOM   399  N N   . ALA A 1 56  ? 20.306  -18.691 25.144  1.00 46.91 ? 58  ALA A N   1 
ATOM   400  C CA  . ALA A 1 56  ? 19.534  -17.560 25.648  1.00 45.60 ? 58  ALA A CA  1 
ATOM   401  C C   . ALA A 1 56  ? 19.750  -16.310 24.808  1.00 43.99 ? 58  ALA A C   1 
ATOM   402  O O   . ALA A 1 56  ? 18.860  -15.484 24.721  1.00 43.69 ? 58  ALA A O   1 
ATOM   403  C CB  . ALA A 1 56  ? 19.945  -17.283 27.082  1.00 45.27 ? 58  ALA A CB  1 
ATOM   404  N N   . ASN A 1 57  ? 20.938  -16.174 24.205  1.00 42.97 ? 59  ASN A N   1 
ATOM   405  C CA  . ASN A 1 57  ? 21.278  -15.044 23.348  1.00 43.52 ? 59  ASN A CA  1 
ATOM   406  C C   . ASN A 1 57  ? 20.731  -15.080 21.883  1.00 41.83 ? 59  ASN A C   1 
ATOM   407  O O   . ASN A 1 57  ? 20.822  -14.052 21.216  1.00 42.45 ? 59  ASN A O   1 
ATOM   408  C CB  . ASN A 1 57  ? 22.773  -14.859 23.312  1.00 45.28 ? 59  ASN A CB  1 
ATOM   409  C CG  . ASN A 1 57  ? 23.382  -14.282 24.572  1.00 49.93 ? 59  ASN A CG  1 
ATOM   410  O OD1 . ASN A 1 57  ? 22.857  -13.352 25.199  1.00 52.55 ? 59  ASN A OD1 1 
ATOM   411  N ND2 . ASN A 1 57  ? 24.525  -14.805 24.952  1.00 50.98 ? 59  ASN A ND2 1 
ATOM   412  N N   . LEU A 1 58  ? 20.171  -16.197 21.409  1.00 41.18 ? 60  LEU A N   1 
ATOM   413  C CA  . LEU A 1 58  ? 19.505  -16.310 20.116  1.00 40.15 ? 60  LEU A CA  1 
ATOM   414  C C   . LEU A 1 58  ? 18.045  -16.037 20.282  1.00 39.44 ? 60  LEU A C   1 
ATOM   415  O O   . LEU A 1 58  ? 17.377  -16.760 21.031  1.00 41.19 ? 60  LEU A O   1 
ATOM   416  C CB  . LEU A 1 58  ? 19.725  -17.713 19.505  1.00 40.72 ? 60  LEU A CB  1 
ATOM   417  C CG  . LEU A 1 58  ? 19.038  -17.950 18.135  1.00 42.76 ? 60  LEU A CG  1 
ATOM   418  C CD1 . LEU A 1 58  ? 19.575  -17.022 17.057  1.00 41.76 ? 60  LEU A CD1 1 
ATOM   419  C CD2 . LEU A 1 58  ? 19.163  -19.424 17.724  1.00 44.33 ? 60  LEU A CD2 1 
ATOM   420  N N   . ARG A 1 59  ? 17.525  -15.016 19.591  1.00 37.76 ? 61  ARG A N   1 
ATOM   421  C CA  A ARG A 1 59  ? 16.135  -14.595 19.707  0.50 38.37 ? 61  ARG A CA  1 
ATOM   422  C CA  B ARG A 1 59  ? 16.131  -14.563 19.717  0.50 38.40 ? 61  ARG A CA  1 
ATOM   423  C C   . ARG A 1 59  ? 15.476  -14.540 18.334  1.00 38.24 ? 61  ARG A C   1 
ATOM   424  O O   . ARG A 1 59  ? 16.073  -14.035 17.369  1.00 36.79 ? 61  ARG A O   1 
ATOM   425  C CB  A ARG A 1 59  ? 16.093  -13.185 20.356  0.50 41.42 ? 61  ARG A CB  1 
ATOM   426  C CB  B ARG A 1 59  ? 16.101  -13.129 20.355  0.50 41.39 ? 61  ARG A CB  1 
ATOM   427  C CG  A ARG A 1 59  ? 15.485  -13.076 21.769  0.50 48.88 ? 61  ARG A CG  1 
ATOM   428  C CG  B ARG A 1 59  ? 14.773  -12.652 21.001  0.50 48.79 ? 61  ARG A CG  1 
ATOM   429  C CD  A ARG A 1 59  ? 15.161  -11.607 22.032  0.50 53.73 ? 61  ARG A CD  1 
ATOM   430  C CD  B ARG A 1 59  ? 14.713  -11.111 21.060  0.50 54.76 ? 61  ARG A CD  1 
ATOM   431  N NE  A ARG A 1 59  ? 13.783  -11.051 21.938  0.50 57.53 ? 61  ARG A NE  1 
ATOM   432  N NE  B ARG A 1 59  ? 14.127  -10.503 22.275  0.50 57.72 ? 61  ARG A NE  1 
ATOM   433  C CZ  A ARG A 1 59  ? 12.728  -11.451 21.214  0.50 59.60 ? 61  ARG A CZ  1 
ATOM   434  C CZ  B ARG A 1 59  ? 14.759  -10.317 23.440  0.50 57.36 ? 61  ARG A CZ  1 
ATOM   435  N NH1 A ARG A 1 59  ? 11.585  -10.785 21.276  0.50 61.23 ? 61  ARG A NH1 1 
ATOM   436  N NH1 B ARG A 1 59  ? 14.130  -9.743  24.459  0.50 55.75 ? 61  ARG A NH1 1 
ATOM   437  N NH2 A ARG A 1 59  ? 12.802  -12.522 20.437  0.50 59.21 ? 61  ARG A NH2 1 
ATOM   438  N NH2 B ARG A 1 59  ? 16.019  -10.712 23.596  0.50 56.31 ? 61  ARG A NH2 1 
ATOM   439  N N   . LEU A 1 60  ? 14.269  -15.072 18.217  1.00 38.66 ? 62  LEU A N   1 
ATOM   440  C CA  . LEU A 1 60  ? 13.427  -14.871 17.054  1.00 41.07 ? 62  LEU A CA  1 
ATOM   441  C C   . LEU A 1 60  ? 12.767  -13.515 17.155  1.00 42.11 ? 62  LEU A C   1 
ATOM   442  O O   . LEU A 1 60  ? 12.019  -13.296 18.099  1.00 43.47 ? 62  LEU A O   1 
ATOM   443  C CB  . LEU A 1 60  ? 12.352  -15.950 16.960  1.00 43.35 ? 62  LEU A CB  1 
ATOM   444  C CG  . LEU A 1 60  ? 11.236  -15.675 15.904  1.00 45.30 ? 62  LEU A CG  1 
ATOM   445  C CD1 . LEU A 1 60  ? 11.762  -15.882 14.572  1.00 42.95 ? 62  LEU A CD1 1 
ATOM   446  C CD2 . LEU A 1 60  ? 10.031  -16.522 16.150  1.00 48.07 ? 62  LEU A CD2 1 
ATOM   447  N N   . ILE A 1 61  ? 13.009  -12.607 16.210  1.00 40.06 ? 63  ILE A N   1 
ATOM   448  C CA  . ILE A 1 61  ? 12.402  -11.274 16.201  1.00 41.41 ? 63  ILE A CA  1 
ATOM   449  C C   . ILE A 1 61  ? 10.988  -11.337 15.618  1.00 41.86 ? 63  ILE A C   1 
ATOM   450  O O   . ILE A 1 61  ? 10.017  -10.909 16.268  1.00 42.39 ? 63  ILE A O   1 
ATOM   451  C CB  . ILE A 1 61  ? 13.287  -10.250 15.448  1.00 41.68 ? 63  ILE A CB  1 
ATOM   452  C CG1 . ILE A 1 61  ? 14.666  -10.192 16.055  1.00 42.01 ? 63  ILE A CG1 1 
ATOM   453  C CG2 . ILE A 1 61  ? 12.621  -8.866  15.404  1.00 43.36 ? 63  ILE A CG2 1 
ATOM   454  C CD1 . ILE A 1 61  ? 14.704  -10.066 17.572  1.00 45.04 ? 63  ILE A CD1 1 
ATOM   455  N N   . SER A 1 62  ? 10.846  -11.928 14.436  1.00 39.94 ? 64  SER A N   1 
ATOM   456  C CA  . SER A 1 62  ? 9.609   -11.819 13.690  1.00 39.29 ? 64  SER A CA  1 
ATOM   457  C C   . SER A 1 62  ? 9.583   -12.737 12.512  1.00 37.73 ? 64  SER A C   1 
ATOM   458  O O   . SER A 1 62  ? 10.621  -13.218 12.031  1.00 36.09 ? 64  SER A O   1 
ATOM   459  C CB  . SER A 1 62  ? 9.400   -10.348 13.257  1.00 45.01 ? 64  SER A CB  1 
ATOM   460  O OG  . SER A 1 62  ? 8.112   -10.168 12.673  1.00 52.22 ? 64  SER A OG  1 
ATOM   461  N N   . LYS A 1 63  ? 8.391   -13.003 12.019  1.00 38.02 ? 65  LYS A N   1 
ATOM   462  C CA  . LYS A 1 63  ? 8.165   -13.833 10.834  1.00 38.36 ? 65  LYS A CA  1 
ATOM   463  C C   . LYS A 1 63  ? 7.297   -13.044 9.873   1.00 40.41 ? 65  LYS A C   1 
ATOM   464  O O   . LYS A 1 63  ? 6.518   -12.174 10.316  1.00 41.06 ? 65  LYS A O   1 
ATOM   465  C CB  . LYS A 1 63  ? 7.561   -15.204 11.163  1.00 41.24 ? 65  LYS A CB  1 
ATOM   466  C CG  . LYS A 1 63  ? 8.407   -16.020 12.139  1.00 45.15 ? 65  LYS A CG  1 
ATOM   467  C CD  . LYS A 1 63  ? 7.885   -17.412 12.278  1.00 48.02 ? 65  LYS A CD  1 
ATOM   468  C CE  . LYS A 1 63  ? 8.713   -18.327 13.152  1.00 49.46 ? 65  LYS A CE  1 
ATOM   469  N NZ  . LYS A 1 63  ? 8.151   -19.740 13.171  1.00 50.61 ? 65  LYS A NZ  1 
ATOM   470  N N   . PHE A 1 64  ? 7.440   -13.312 8.566   1.00 36.65 ? 66  PHE A N   1 
ATOM   471  C CA  . PHE A 1 64  ? 6.693   -12.628 7.539   1.00 35.67 ? 66  PHE A CA  1 
ATOM   472  C C   . PHE A 1 64  ? 6.622   -13.484 6.310   1.00 35.99 ? 66  PHE A C   1 
ATOM   473  O O   . PHE A 1 64  ? 7.445   -14.389 6.110   1.00 33.85 ? 66  PHE A O   1 
ATOM   474  C CB  . PHE A 1 64  ? 7.209   -11.206 7.225   1.00 34.58 ? 66  PHE A CB  1 
ATOM   475  C CG  . PHE A 1 64  ? 8.644   -11.223 6.697   1.00 31.66 ? 66  PHE A CG  1 
ATOM   476  C CD1 . PHE A 1 64  ? 8.903   -11.396 5.348   1.00 31.57 ? 66  PHE A CD1 1 
ATOM   477  C CD2 . PHE A 1 64  ? 9.710   -11.207 7.566   1.00 32.69 ? 66  PHE A CD2 1 
ATOM   478  C CE1 . PHE A 1 64  ? 10.223  -11.507 4.878   1.00 32.97 ? 66  PHE A CE1 1 
ATOM   479  C CE2 . PHE A 1 64  ? 11.005  -11.277 7.092   1.00 32.62 ? 66  PHE A CE2 1 
ATOM   480  C CZ  . PHE A 1 64  ? 11.253  -11.442 5.758   1.00 31.10 ? 66  PHE A CZ  1 
ATOM   481  N N   . ASP A 1 65  ? 5.604   -13.225 5.486   1.00 36.02 ? 67  ASP A N   1 
ATOM   482  C CA  . ASP A 1 65  ? 5.422   -13.952 4.236   1.00 37.14 ? 67  ASP A CA  1 
ATOM   483  C C   . ASP A 1 65  ? 4.828   -13.103 3.113   1.00 35.61 ? 67  ASP A C   1 
ATOM   484  O O   . ASP A 1 65  ? 4.287   -13.683 2.172   1.00 36.73 ? 67  ASP A O   1 
ATOM   485  C CB  . ASP A 1 65  ? 4.609   -15.220 4.487   1.00 40.09 ? 67  ASP A CB  1 
ATOM   486  C CG  . ASP A 1 65  ? 3.233   -14.938 5.112   1.00 43.48 ? 67  ASP A CG  1 
ATOM   487  O OD1 . ASP A 1 65  ? 2.774   -13.794 5.051   1.00 44.15 ? 67  ASP A OD1 1 
ATOM   488  O OD2 . ASP A 1 65  ? 2.638   -15.854 5.667   1.00 47.30 ? 67  ASP A OD2 1 
ATOM   489  N N   . THR A 1 66  ? 4.956   -11.792 3.184   1.00 34.26 ? 68  THR A N   1 
ATOM   490  C CA  . THR A 1 66  ? 4.667   -10.882 2.093   1.00 35.22 ? 68  THR A CA  1 
ATOM   491  C C   . THR A 1 66  ? 5.757   -9.829  1.973   1.00 34.90 ? 68  THR A C   1 
ATOM   492  O O   . THR A 1 66  ? 6.453   -9.555  2.946   1.00 35.67 ? 68  THR A O   1 
ATOM   493  C CB  . THR A 1 66  ? 3.290   -10.161 2.279   1.00 38.15 ? 68  THR A CB  1 
ATOM   494  O OG1 . THR A 1 66  ? 3.390   -9.156  3.266   1.00 39.83 ? 68  THR A OG1 1 
ATOM   495  C CG2 . THR A 1 66  ? 2.149   -11.100 2.560   1.00 38.34 ? 68  THR A CG2 1 
ATOM   496  N N   . VAL A 1 67  ? 5.865   -9.224  0.817   1.00 34.18 ? 69  VAL A N   1 
ATOM   497  C CA  . VAL A 1 67  ? 6.793   -8.134  0.529   1.00 36.34 ? 69  VAL A CA  1 
ATOM   498  C C   . VAL A 1 67  ? 6.579   -6.960  1.441   1.00 36.85 ? 69  VAL A C   1 
ATOM   499  O O   . VAL A 1 67  ? 7.523   -6.395  1.982   1.00 34.65 ? 69  VAL A O   1 
ATOM   500  C CB  . VAL A 1 67  ? 6.696   -7.695  -0.937  1.00 35.91 ? 69  VAL A CB  1 
ATOM   501  C CG1 . VAL A 1 67  ? 7.666   -6.556  -1.213  1.00 37.01 ? 69  VAL A CG1 1 
ATOM   502  C CG2 . VAL A 1 67  ? 6.923   -8.860  -1.871  1.00 36.26 ? 69  VAL A CG2 1 
ATOM   503  N N   . GLU A 1 68  ? 5.283   -6.555  1.625   1.00 35.66 ? 70  GLU A N   1 
ATOM   504  C CA  . GLU A 1 68  ? 5.001   -5.382  2.433   1.00 36.37 ? 70  GLU A CA  1 
ATOM   505  C C   . GLU A 1 68  ? 5.340   -5.599  3.911   1.00 35.73 ? 70  GLU A C   1 
ATOM   506  O O   . GLU A 1 68  ? 5.790   -4.644  4.564   1.00 36.93 ? 70  GLU A O   1 
ATOM   507  C CB  . GLU A 1 68  ? 3.524   -4.930  2.268   1.00 40.56 ? 70  GLU A CB  1 
ATOM   508  C CG  . GLU A 1 68  ? 3.238   -4.393  0.861   1.00 42.82 ? 70  GLU A CG  1 
ATOM   509  C CD  . GLU A 1 68  ? 3.098   -5.416  -0.254  1.00 45.49 ? 70  GLU A CD  1 
ATOM   510  O OE1 . GLU A 1 68  ? 3.019   -6.635  0.035   1.00 40.92 ? 70  GLU A OE1 1 
ATOM   511  O OE2 . GLU A 1 68  ? 3.077   -4.996  -1.432  1.00 51.10 ? 70  GLU A OE2 1 
ATOM   512  N N   . ASP A 1 69  ? 5.145   -6.779  4.411   1.00 35.89 ? 71  ASP A N   1 
ATOM   513  C CA  . ASP A 1 69  ? 5.477   -7.103  5.803   1.00 35.52 ? 71  ASP A CA  1 
ATOM   514  C C   . ASP A 1 69  ? 7.026   -7.164  5.971   1.00 34.35 ? 71  ASP A C   1 
ATOM   515  O O   . ASP A 1 69  ? 7.547   -6.725  7.013   1.00 32.70 ? 71  ASP A O   1 
ATOM   516  C CB  . ASP A 1 69  ? 4.806   -8.400  6.220   1.00 37.65 ? 71  ASP A CB  1 
ATOM   517  C CG  . ASP A 1 69  ? 3.270   -8.268  6.308   1.00 44.49 ? 71  ASP A CG  1 
ATOM   518  O OD1 . ASP A 1 69  ? 2.783   -7.155  6.649   1.00 45.72 ? 71  ASP A OD1 1 
ATOM   519  O OD2 . ASP A 1 69  ? 2.577   -9.257  6.016   1.00 45.79 ? 71  ASP A OD2 1 
ATOM   520  N N   . PHE A 1 70  ? 7.729   -7.653  4.951   1.00 32.80 ? 72  PHE A N   1 
ATOM   521  C CA  . PHE A 1 70  ? 9.236   -7.554  4.912   1.00 31.10 ? 72  PHE A CA  1 
ATOM   522  C C   . PHE A 1 70  ? 9.644   -6.111  5.106   1.00 31.74 ? 72  PHE A C   1 
ATOM   523  O O   . PHE A 1 70  ? 10.417  -5.801  6.023   1.00 32.95 ? 72  PHE A O   1 
ATOM   524  C CB  . PHE A 1 70  ? 9.812   -8.101  3.584   1.00 30.09 ? 72  PHE A CB  1 
ATOM   525  C CG  . PHE A 1 70  ? 11.278  -7.714  3.407   1.00 28.41 ? 72  PHE A CG  1 
ATOM   526  C CD1 . PHE A 1 70  ? 12.266  -8.317  4.180   1.00 30.11 ? 72  PHE A CD1 1 
ATOM   527  C CD2 . PHE A 1 70  ? 11.651  -6.696  2.542   1.00 29.40 ? 72  PHE A CD2 1 
ATOM   528  C CE1 . PHE A 1 70  ? 13.584  -7.928  4.056   1.00 28.97 ? 72  PHE A CE1 1 
ATOM   529  C CE2 . PHE A 1 70  ? 12.976  -6.318  2.415   1.00 30.09 ? 72  PHE A CE2 1 
ATOM   530  C CZ  . PHE A 1 70  ? 13.932  -6.919  3.200   1.00 29.19 ? 72  PHE A CZ  1 
ATOM   531  N N   . TRP A 1 71  ? 9.138   -5.218  4.242   1.00 31.56 ? 73  TRP A N   1 
ATOM   532  C CA  . TRP A 1 71  ? 9.523   -3.825  4.303   1.00 34.44 ? 73  TRP A CA  1 
ATOM   533  C C   . TRP A 1 71  ? 9.157   -3.116  5.618   1.00 37.38 ? 73  TRP A C   1 
ATOM   534  O O   . TRP A 1 71  ? 9.928   -2.274  6.069   1.00 36.85 ? 73  TRP A O   1 
ATOM   535  C CB  . TRP A 1 71  ? 9.004   -3.041  3.113   1.00 34.19 ? 73  TRP A CB  1 
ATOM   536  C CG  . TRP A 1 71  ? 9.699   -3.335  1.826   1.00 34.03 ? 73  TRP A CG  1 
ATOM   537  C CD1 . TRP A 1 71  ? 9.125   -3.789  0.682   1.00 36.44 ? 73  TRP A CD1 1 
ATOM   538  C CD2 . TRP A 1 71  ? 11.081  -3.075  1.508   1.00 34.29 ? 73  TRP A CD2 1 
ATOM   539  N NE1 . TRP A 1 71  ? 10.088  -3.938  -0.299  1.00 37.19 ? 73  TRP A NE1 1 
ATOM   540  C CE2 . TRP A 1 71  ? 11.287  -3.469  0.173   1.00 35.54 ? 73  TRP A CE2 1 
ATOM   541  C CE3 . TRP A 1 71  ? 12.187  -2.622  2.248   1.00 34.47 ? 73  TRP A CE3 1 
ATOM   542  C CZ2 . TRP A 1 71  ? 12.544  -3.383  -0.450  1.00 35.45 ? 73  TRP A CZ2 1 
ATOM   543  C CZ3 . TRP A 1 71  ? 13.436  -2.535  1.631   1.00 35.43 ? 73  TRP A CZ3 1 
ATOM   544  C CH2 . TRP A 1 71  ? 13.602  -2.887  0.293   1.00 34.65 ? 73  TRP A CH2 1 
ATOM   545  N N   . ALA A 1 72  ? 8.024   -3.460  6.240   1.00 40.11 ? 74  ALA A N   1 
ATOM   546  C CA  . ALA A 1 72  ? 7.593   -2.862  7.516   1.00 40.13 ? 74  ALA A CA  1 
ATOM   547  C C   . ALA A 1 72  ? 8.557   -3.290  8.632   1.00 40.68 ? 74  ALA A C   1 
ATOM   548  O O   . ALA A 1 72  ? 8.928   -2.479  9.495   1.00 41.65 ? 74  ALA A O   1 
ATOM   549  C CB  . ALA A 1 72  ? 6.183   -3.302  7.838   1.00 41.13 ? 74  ALA A CB  1 
ATOM   550  N N   . LEU A 1 73  ? 9.000   -4.550  8.593   1.00 37.68 ? 75  LEU A N   1 
ATOM   551  C CA  . LEU A 1 73  ? 9.972   -5.041  9.557   1.00 37.47 ? 75  LEU A CA  1 
ATOM   552  C C   . LEU A 1 73  ? 11.328  -4.414  9.318   1.00 36.26 ? 75  LEU A C   1 
ATOM   553  O O   . LEU A 1 73  ? 11.968  -3.966  10.267  1.00 37.73 ? 75  LEU A O   1 
ATOM   554  C CB  . LEU A 1 73  ? 10.065  -6.571  9.471   1.00 37.47 ? 75  LEU A CB  1 
ATOM   555  C CG  . LEU A 1 73  ? 11.083  -7.234  10.383  1.00 40.04 ? 75  LEU A CG  1 
ATOM   556  C CD1 . LEU A 1 73  ? 10.821  -6.928  11.860  1.00 42.73 ? 75  LEU A CD1 1 
ATOM   557  C CD2 . LEU A 1 73  ? 11.078  -8.742  10.184  1.00 39.98 ? 75  LEU A CD2 1 
ATOM   558  N N   . TYR A 1 74  ? 11.790  -4.395  8.050   1.00 33.73 ? 76  TYR A N   1 
ATOM   559  C CA  . TYR A 1 74  ? 13.091  -3.817  7.670   1.00 33.31 ? 76  TYR A CA  1 
ATOM   560  C C   . TYR A 1 74  ? 13.186  -2.357  8.097   1.00 35.06 ? 76  TYR A C   1 
ATOM   561  O O   . TYR A 1 74  ? 14.151  -1.945  8.716   1.00 34.53 ? 76  TYR A O   1 
ATOM   562  C CB  . TYR A 1 74  ? 13.328  -3.985  6.158   1.00 32.63 ? 76  TYR A CB  1 
ATOM   563  C CG  . TYR A 1 74  ? 14.689  -3.461  5.717   1.00 32.49 ? 76  TYR A CG  1 
ATOM   564  C CD1 . TYR A 1 74  ? 15.817  -4.260  5.787   1.00 33.60 ? 76  TYR A CD1 1 
ATOM   565  C CD2 . TYR A 1 74  ? 14.842  -2.161  5.269   1.00 33.20 ? 76  TYR A CD2 1 
ATOM   566  C CE1 . TYR A 1 74  ? 17.083  -3.769  5.412   1.00 34.99 ? 76  TYR A CE1 1 
ATOM   567  C CE2 . TYR A 1 74  ? 16.080  -1.668  4.878   1.00 34.05 ? 76  TYR A CE2 1 
ATOM   568  C CZ  . TYR A 1 74  ? 17.196  -2.480  4.938   1.00 35.56 ? 76  TYR A CZ  1 
ATOM   569  O OH  . TYR A 1 74  ? 18.402  -1.998  4.552   1.00 37.91 ? 76  TYR A OH  1 
ATOM   570  N N   . ASN A 1 75  ? 12.159  -1.583  7.779   1.00 38.70 ? 77  ASN A N   1 
ATOM   571  C CA  . ASN A 1 75  ? 12.108  -0.158  8.145   1.00 43.28 ? 77  ASN A CA  1 
ATOM   572  C C   . ASN A 1 75  ? 12.145  0.090   9.673   1.00 45.82 ? 77  ASN A C   1 
ATOM   573  O O   . ASN A 1 75  ? 12.760  1.065   10.134  1.00 47.30 ? 77  ASN A O   1 
ATOM   574  C CB  . ASN A 1 75  ? 10.893  0.491   7.481   1.00 46.23 ? 77  ASN A CB  1 
ATOM   575  C CG  . ASN A 1 75  ? 11.009  0.547   5.957   1.00 53.02 ? 77  ASN A CG  1 
ATOM   576  O OD1 . ASN A 1 75  ? 12.098  0.648   5.381   1.00 58.32 ? 77  ASN A OD1 1 
ATOM   577  N ND2 . ASN A 1 75  ? 9.913   0.492   5.252   1.00 55.10 ? 77  ASN A ND2 1 
ATOM   578  N N   . HIS A 1 76  ? 11.519  -0.767  10.427  1.00 46.97 ? 78  HIS A N   1 
ATOM   579  C CA  . HIS A 1 76  ? 11.471  -0.667  11.878  1.00 50.01 ? 78  HIS A CA  1 
ATOM   580  C C   . HIS A 1 76  ? 12.791  -0.963  12.542  1.00 49.93 ? 78  HIS A C   1 
ATOM   581  O O   . HIS A 1 76  ? 13.184  -0.267  13.488  1.00 51.22 ? 78  HIS A O   1 
ATOM   582  C CB  . HIS A 1 76  ? 10.362  -1.572  12.419  1.00 53.52 ? 78  HIS A CB  1 
ATOM   583  C CG  . HIS A 1 76  ? 10.352  -1.715  13.903  1.00 63.49 ? 78  HIS A CG  1 
ATOM   584  N ND1 . HIS A 1 76  ? 10.728  -2.909  14.518  1.00 67.55 ? 78  HIS A ND1 1 
ATOM   585  C CD2 . HIS A 1 76  ? 10.001  -0.819  14.856  1.00 66.91 ? 78  HIS A CD2 1 
ATOM   586  C CE1 . HIS A 1 76  ? 10.599  -2.696  15.816  1.00 68.82 ? 78  HIS A CE1 1 
ATOM   587  N NE2 . HIS A 1 76  ? 10.166  -1.452  16.066  1.00 69.27 ? 78  HIS A NE2 1 
ATOM   588  N N   . ILE A 1 77  ? 13.509  -1.944  12.056  1.00 48.51 ? 79  ILE A N   1 
ATOM   589  C CA  . ILE A 1 77  ? 14.670  -2.495  12.776  1.00 48.19 ? 79  ILE A CA  1 
ATOM   590  C C   . ILE A 1 77  ? 15.918  -1.662  12.662  1.00 47.99 ? 79  ILE A C   1 
ATOM   591  O O   . ILE A 1 77  ? 16.077  -0.884  11.732  1.00 47.26 ? 79  ILE A O   1 
ATOM   592  C CB  . ILE A 1 77  ? 14.900  -3.988  12.302  1.00 50.14 ? 79  ILE A CB  1 
ATOM   593  C CG1 . ILE A 1 77  ? 14.135  -4.918  13.271  1.00 51.69 ? 79  ILE A CG1 1 
ATOM   594  C CG2 . ILE A 1 77  ? 16.376  -4.375  12.173  1.00 52.04 ? 79  ILE A CG2 1 
ATOM   595  C CD1 . ILE A 1 77  ? 14.092  -6.197  12.990  1.00 56.05 ? 79  ILE A CD1 1 
ATOM   596  N N   . GLN A 1 78  ? 16.835  -1.880  13.632  1.00 48.19 ? 80  GLN A N   1 
ATOM   597  C CA  . GLN A 1 78  ? 18.141  -1.276  13.642  1.00 50.49 ? 80  GLN A CA  1 
ATOM   598  C C   . GLN A 1 78  ? 19.030  -1.825  12.495  1.00 50.38 ? 80  GLN A C   1 
ATOM   599  O O   . GLN A 1 78  ? 19.038  -3.011  12.243  1.00 49.66 ? 80  GLN A O   1 
ATOM   600  C CB  . GLN A 1 78  ? 18.818  -1.486  15.012  1.00 54.96 ? 80  GLN A CB  1 
ATOM   601  C CG  . GLN A 1 78  ? 20.135  -0.701  15.150  1.00 63.96 ? 80  GLN A CG  1 
ATOM   602  C CD  . GLN A 1 78  ? 19.957  0.797   14.951  1.00 73.78 ? 80  GLN A CD  1 
ATOM   603  O OE1 . GLN A 1 78  ? 19.960  1.308   13.814  1.00 76.12 ? 80  GLN A OE1 1 
ATOM   604  N NE2 . GLN A 1 78  ? 19.798  1.528   16.032  1.00 76.13 ? 80  GLN A NE2 1 
ATOM   605  N N   . LEU A 1 79  ? 19.765  -0.962  11.821  1.00 50.11 ? 81  LEU A N   1 
ATOM   606  C CA  . LEU A 1 79  ? 20.665  -1.351  10.743  1.00 48.25 ? 81  LEU A CA  1 
ATOM   607  C C   . LEU A 1 79  ? 21.886  -2.104  11.262  1.00 47.19 ? 81  LEU A C   1 
ATOM   608  O O   . LEU A 1 79  ? 22.389  -1.859  12.372  1.00 45.19 ? 81  LEU A O   1 
ATOM   609  C CB  . LEU A 1 79  ? 21.140  -0.120  9.995   1.00 49.16 ? 81  LEU A CB  1 
ATOM   610  C CG  . LEU A 1 79  ? 20.179  0.523   8.993   1.00 52.85 ? 81  LEU A CG  1 
ATOM   611  C CD1 . LEU A 1 79  ? 20.695  1.897   8.591   1.00 53.07 ? 81  LEU A CD1 1 
ATOM   612  C CD2 . LEU A 1 79  ? 19.964  -0.399  7.762   1.00 54.68 ? 81  LEU A CD2 1 
ATOM   613  N N   . SER A 1 80  ? 22.406  -3.011  10.391  1.00 46.99 ? 82  SER A N   1 
ATOM   614  C CA  A SER A 1 80  ? 23.542  -3.859  10.732  0.50 46.97 ? 82  SER A CA  1 
ATOM   615  C CA  B SER A 1 80  ? 23.520  -3.850  10.769  0.50 46.45 ? 82  SER A CA  1 
ATOM   616  C C   . SER A 1 80  ? 24.762  -3.043  11.109  1.00 48.60 ? 82  SER A C   1 
ATOM   617  O O   . SER A 1 80  ? 25.436  -3.340  12.108  1.00 50.01 ? 82  SER A O   1 
ATOM   618  C CB  A SER A 1 80  ? 23.864  -4.781  9.564   0.50 47.50 ? 82  SER A CB  1 
ATOM   619  C CB  B SER A 1 80  ? 23.775  -4.872  9.672   0.50 45.54 ? 82  SER A CB  1 
ATOM   620  O OG  A SER A 1 80  ? 24.004  -4.034  8.371   0.50 48.59 ? 82  SER A OG  1 
ATOM   621  O OG  B SER A 1 80  ? 22.645  -5.733  9.607   0.50 43.67 ? 82  SER A OG  1 
ATOM   622  N N   . SER A 1 81  ? 25.083  -1.997  10.297  1.00 49.98 ? 83  SER A N   1 
ATOM   623  C CA  . SER A 1 81  ? 26.156  -1.019  10.582  1.00 52.57 ? 83  SER A CA  1 
ATOM   624  C C   . SER A 1 81  ? 26.117  -0.494  12.022  1.00 55.43 ? 83  SER A C   1 
ATOM   625  O O   . SER A 1 81  ? 27.188  -0.272  12.606  1.00 56.40 ? 83  SER A O   1 
ATOM   626  C CB  . SER A 1 81  ? 26.091  0.153   9.600   1.00 52.69 ? 83  SER A CB  1 
ATOM   627  O OG  . SER A 1 81  ? 24.907  0.916   9.771   1.00 54.52 ? 83  SER A OG  1 
ATOM   628  N N   . ASN A 1 82  ? 24.871  -0.302  12.593  1.00 56.12 ? 84  ASN A N   1 
ATOM   629  C CA  . ASN A 1 82  ? 24.660  0.176   13.962  1.00 58.22 ? 84  ASN A CA  1 
ATOM   630  C C   . ASN A 1 82  ? 24.629  -0.908  15.056  1.00 59.88 ? 84  ASN A C   1 
ATOM   631  O O   . ASN A 1 82  ? 24.470  -0.547  16.231  1.00 60.14 ? 84  ASN A O   1 
ATOM   632  C CB  . ASN A 1 82  ? 23.375  1.009   14.029  1.00 60.75 ? 84  ASN A CB  1 
ATOM   633  C CG  . ASN A 1 82  ? 23.451  2.245   13.166  1.00 66.87 ? 84  ASN A CG  1 
ATOM   634  O OD1 . ASN A 1 82  ? 24.491  2.940   13.099  1.00 70.26 ? 84  ASN A OD1 1 
ATOM   635  N ND2 . ASN A 1 82  ? 22.371  2.559   12.487  1.00 67.06 ? 84  ASN A ND2 1 
ATOM   636  N N   . LEU A 1 83  ? 24.783  -2.221  14.704  1.00 59.87 ? 85  LEU A N   1 
ATOM   637  C CA  . LEU A 1 83  ? 24.859  -3.271  15.726  1.00 60.72 ? 85  LEU A CA  1 
ATOM   638  C C   . LEU A 1 83  ? 26.191  -3.259  16.447  1.00 61.73 ? 85  LEU A C   1 
ATOM   639  O O   . LEU A 1 83  ? 27.230  -3.155  15.795  1.00 61.23 ? 85  LEU A O   1 
ATOM   640  C CB  . LEU A 1 83  ? 24.788  -4.632  15.088  1.00 60.71 ? 85  LEU A CB  1 
ATOM   641  C CG  . LEU A 1 83  ? 23.456  -5.214  14.689  1.00 61.60 ? 85  LEU A CG  1 
ATOM   642  C CD1 . LEU A 1 83  ? 23.655  -6.651  14.124  1.00 60.58 ? 85  LEU A CD1 1 
ATOM   643  C CD2 . LEU A 1 83  ? 22.445  -5.224  15.827  1.00 62.47 ? 85  LEU A CD2 1 
ATOM   644  N N   . MET A 1 84  ? 26.186  -3.411  17.785  1.00 63.55 ? 86  MET A N   1 
ATOM   645  C CA  . MET A 1 84  ? 27.452  -3.573  18.526  1.00 66.18 ? 86  MET A CA  1 
ATOM   646  C C   . MET A 1 84  ? 28.173  -4.828  18.061  1.00 65.63 ? 86  MET A C   1 
ATOM   647  O O   . MET A 1 84  ? 27.528  -5.840  17.854  1.00 65.70 ? 86  MET A O   1 
ATOM   648  C CB  . MET A 1 84  ? 27.205  -3.684  20.041  1.00 69.65 ? 86  MET A CB  1 
ATOM   649  C CG  . MET A 1 84  ? 26.834  -2.372  20.691  1.00 76.01 ? 86  MET A CG  1 
ATOM   650  S SD  . MET A 1 84  ? 27.147  -2.373  22.473  1.00 92.79 ? 86  MET A SD  1 
ATOM   651  C CE  . MET A 1 84  ? 25.419  -2.500  23.111  1.00 92.88 ? 86  MET A CE  1 
ATOM   652  N N   . PRO A 1 85  ? 29.497  -4.795  17.864  1.00 65.24 ? 87  PRO A N   1 
ATOM   653  C CA  . PRO A 1 85  ? 30.226  -6.038  17.554  1.00 63.88 ? 87  PRO A CA  1 
ATOM   654  C C   . PRO A 1 85  ? 29.851  -7.240  18.417  1.00 61.01 ? 87  PRO A C   1 
ATOM   655  O O   . PRO A 1 85  ? 29.534  -7.120  19.614  1.00 61.99 ? 87  PRO A O   1 
ATOM   656  C CB  . PRO A 1 85  ? 31.680  -5.652  17.773  1.00 65.45 ? 87  PRO A CB  1 
ATOM   657  C CG  . PRO A 1 85  ? 31.718  -4.215  17.394  1.00 66.81 ? 87  PRO A CG  1 
ATOM   658  C CD  . PRO A 1 85  ? 30.404  -3.631  17.886  1.00 64.97 ? 87  PRO A CD  1 
ATOM   659  N N   . GLY A 1 86  ? 29.893  -8.385  17.785  1.00 56.62 ? 88  GLY A N   1 
ATOM   660  C CA  . GLY A 1 86  ? 29.480  -9.623  18.402  1.00 53.43 ? 88  GLY A CA  1 
ATOM   661  C C   . GLY A 1 86  ? 28.031  -9.945  18.136  1.00 49.04 ? 88  GLY A C   1 
ATOM   662  O O   . GLY A 1 86  ? 27.629  -11.064 18.463  1.00 50.98 ? 88  GLY A O   1 
ATOM   663  N N   . CYS A 1 87  ? 27.216  -9.003  17.522  1.00 44.36 ? 89  CYS A N   1 
ATOM   664  C CA  . CYS A 1 87  ? 25.821  -9.327  17.138  1.00 41.81 ? 89  CYS A CA  1 
ATOM   665  C C   . CYS A 1 87  ? 25.706  -9.956  15.709  1.00 37.12 ? 89  CYS A C   1 
ATOM   666  O O   . CYS A 1 87  ? 26.536  -9.721  14.827  1.00 35.35 ? 89  CYS A O   1 
ATOM   667  C CB  . CYS A 1 87  ? 24.947  -8.088  17.258  1.00 43.84 ? 89  CYS A CB  1 
ATOM   668  S SG  . CYS A 1 87  ? 24.755  -7.485  18.956  1.00 51.65 ? 89  CYS A SG  1 
ATOM   669  N N   . ASP A 1 88  ? 24.692  -10.765 15.519  1.00 35.12 ? 90  ASP A N   1 
ATOM   670  C CA  . ASP A 1 88  ? 24.400  -11.448 14.260  1.00 34.59 ? 90  ASP A CA  1 
ATOM   671  C C   . ASP A 1 88  ? 22.943  -11.198 13.960  1.00 34.16 ? 90  ASP A C   1 
ATOM   672  O O   . ASP A 1 88  ? 22.093  -11.232 14.873  1.00 35.55 ? 90  ASP A O   1 
ATOM   673  C CB  . ASP A 1 88  ? 24.657  -12.944 14.314  1.00 36.69 ? 90  ASP A CB  1 
ATOM   674  C CG  . ASP A 1 88  ? 25.960  -13.443 14.837  1.00 45.67 ? 90  ASP A CG  1 
ATOM   675  O OD1 . ASP A 1 88  ? 26.999  -12.813 14.548  1.00 42.34 ? 90  ASP A OD1 1 
ATOM   676  O OD2 . ASP A 1 88  ? 25.957  -14.499 15.505  1.00 53.79 ? 90  ASP A OD2 1 
ATOM   677  N N   . TYR A 1 89  ? 22.603  -10.954 12.681  1.00 29.87 ? 91  TYR A N   1 
ATOM   678  C CA  . TYR A 1 89  ? 21.225  -11.059 12.242  1.00 28.49 ? 91  TYR A CA  1 
ATOM   679  C C   . TYR A 1 89  ? 21.155  -12.181 11.239  1.00 25.47 ? 91  TYR A C   1 
ATOM   680  O O   . TYR A 1 89  ? 22.087  -12.327 10.390  1.00 24.82 ? 91  TYR A O   1 
ATOM   681  C CB  . TYR A 1 89  ? 20.755  -9.817  11.511  1.00 31.96 ? 91  TYR A CB  1 
ATOM   682  C CG  . TYR A 1 89  ? 20.251  -8.665  12.345  1.00 40.86 ? 91  TYR A CG  1 
ATOM   683  C CD1 . TYR A 1 89  ? 20.976  -7.504  12.453  1.00 48.84 ? 91  TYR A CD1 1 
ATOM   684  C CD2 . TYR A 1 89  ? 18.998  -8.700  12.928  1.00 44.50 ? 91  TYR A CD2 1 
ATOM   685  C CE1 . TYR A 1 89  ? 20.465  -6.383  13.132  1.00 51.06 ? 91  TYR A CE1 1 
ATOM   686  C CE2 . TYR A 1 89  ? 18.488  -7.607  13.624  1.00 47.41 ? 91  TYR A CE2 1 
ATOM   687  C CZ  . TYR A 1 89  ? 19.219  -6.442  13.709  1.00 51.06 ? 91  TYR A CZ  1 
ATOM   688  O OH  . TYR A 1 89  ? 18.709  -5.336  14.370  1.00 54.86 ? 91  TYR A OH  1 
ATOM   689  N N   . SER A 1 90  ? 20.073  -12.963 11.272  1.00 23.70 ? 92  SER A N   1 
ATOM   690  C CA  . SER A 1 90  ? 19.898  -14.072 10.331  1.00 24.86 ? 92  SER A CA  1 
ATOM   691  C C   . SER A 1 90  ? 18.492  -14.077 9.765   1.00 28.05 ? 92  SER A C   1 
ATOM   692  O O   . SER A 1 90  ? 17.544  -13.879 10.531  1.00 29.88 ? 92  SER A O   1 
ATOM   693  C CB  . SER A 1 90  ? 20.177  -15.404 11.009  1.00 25.58 ? 92  SER A CB  1 
ATOM   694  O OG  . SER A 1 90  ? 21.403  -15.480 11.711  1.00 30.34 ? 92  SER A OG  1 
ATOM   695  N N   . LEU A 1 91  ? 18.305  -14.320 8.457   1.00 24.69 ? 93  LEU A N   1 
ATOM   696  C CA  . LEU A 1 91  ? 16.978  -14.514 7.901   1.00 23.04 ? 93  LEU A CA  1 
ATOM   697  C C   . LEU A 1 91  ? 16.920  -15.921 7.342   1.00 22.97 ? 93  LEU A C   1 
ATOM   698  O O   . LEU A 1 91  ? 17.689  -16.224 6.410   1.00 21.82 ? 93  LEU A O   1 
ATOM   699  C CB  . LEU A 1 91  ? 16.668  -13.506 6.800   1.00 22.96 ? 93  LEU A CB  1 
ATOM   700  C CG  . LEU A 1 91  ? 15.200  -13.574 6.301   1.00 26.59 ? 93  LEU A CG  1 
ATOM   701  C CD1 . LEU A 1 91  ? 14.270  -12.892 7.267   1.00 28.35 ? 93  LEU A CD1 1 
ATOM   702  C CD2 . LEU A 1 91  ? 15.016  -12.987 4.954   1.00 28.02 ? 93  LEU A CD2 1 
ATOM   703  N N   . PHE A 1 92  ? 16.048  -16.787 7.877   1.00 22.81 ? 94  PHE A N   1 
ATOM   704  C CA  . PHE A 1 92  ? 15.975  -18.158 7.494   1.00 22.82 ? 94  PHE A CA  1 
ATOM   705  C C   . PHE A 1 92  ? 14.538  -18.546 7.168   1.00 25.37 ? 94  PHE A C   1 
ATOM   706  O O   . PHE A 1 92  ? 13.589  -17.984 7.710   1.00 25.75 ? 94  PHE A O   1 
ATOM   707  C CB  . PHE A 1 92  ? 16.524  -19.092 8.603   1.00 24.26 ? 94  PHE A CB  1 
ATOM   708  C CG  . PHE A 1 92  ? 18.024  -19.273 8.474   1.00 24.49 ? 94  PHE A CG  1 
ATOM   709  C CD1 . PHE A 1 92  ? 18.882  -18.238 8.763   1.00 24.34 ? 94  PHE A CD1 1 
ATOM   710  C CD2 . PHE A 1 92  ? 18.567  -20.479 8.055   1.00 25.35 ? 94  PHE A CD2 1 
ATOM   711  C CE1 . PHE A 1 92  ? 20.274  -18.401 8.609   1.00 24.09 ? 94  PHE A CE1 1 
ATOM   712  C CE2 . PHE A 1 92  ? 19.925  -20.632 7.878   1.00 25.99 ? 94  PHE A CE2 1 
ATOM   713  C CZ  . PHE A 1 92  ? 20.791  -19.598 8.197   1.00 24.82 ? 94  PHE A CZ  1 
ATOM   714  N N   . LYS A 1 93  ? 14.394  -19.515 6.285   1.00 25.17 ? 95  LYS A N   1 
ATOM   715  C CA  . LYS A 1 93  ? 13.066  -20.056 5.970   1.00 25.54 ? 95  LYS A CA  1 
ATOM   716  C C   . LYS A 1 93  ? 12.439  -20.585 7.264   1.00 28.20 ? 95  LYS A C   1 
ATOM   717  O O   . LYS A 1 93  ? 13.119  -21.133 8.141   1.00 27.92 ? 95  LYS A O   1 
ATOM   718  C CB  . LYS A 1 93  ? 13.161  -21.142 4.928   1.00 25.31 ? 95  LYS A CB  1 
ATOM   719  C CG  . LYS A 1 93  ? 13.502  -20.642 3.533   1.00 28.40 ? 95  LYS A CG  1 
ATOM   720  C CD  . LYS A 1 93  ? 13.716  -21.703 2.565   1.00 32.78 ? 95  LYS A CD  1 
ATOM   721  C CE  . LYS A 1 93  ? 13.952  -21.101 1.192   1.00 34.82 ? 95  LYS A CE  1 
ATOM   722  N NZ  . LYS A 1 93  ? 14.299  -22.136 0.212   1.00 34.17 ? 95  LYS A NZ  1 
ATOM   723  N N   . ASP A 1 94  ? 11.155  -20.393 7.384   1.00 31.04 ? 96  ASP A N   1 
ATOM   724  C CA  . ASP A 1 94  ? 10.411  -20.837 8.581   1.00 34.52 ? 96  ASP A CA  1 
ATOM   725  C C   . ASP A 1 94  ? 10.676  -22.332 8.809   1.00 35.45 ? 96  ASP A C   1 
ATOM   726  O O   . ASP A 1 94  ? 10.595  -23.114 7.858   1.00 36.51 ? 96  ASP A O   1 
ATOM   727  C CB  . ASP A 1 94  ? 8.919   -20.502 8.335   1.00 39.77 ? 96  ASP A CB  1 
ATOM   728  C CG  . ASP A 1 94  ? 8.021   -20.565 9.537   1.00 49.81 ? 96  ASP A CG  1 
ATOM   729  O OD1 . ASP A 1 94  ? 8.546   -20.566 10.670  1.00 48.92 ? 96  ASP A OD1 1 
ATOM   730  O OD2 . ASP A 1 94  ? 6.805   -20.578 9.344   1.00 55.80 ? 96  ASP A OD2 1 
ATOM   731  N N   . GLY A 1 95  ? 11.079  -22.684 10.031  1.00 36.35 ? 97  GLY A N   1 
ATOM   732  C CA  . GLY A 1 95  ? 11.345  -24.054 10.408  1.00 35.51 ? 97  GLY A CA  1 
ATOM   733  C C   . GLY A 1 95  ? 12.813  -24.461 10.359  1.00 35.53 ? 97  GLY A C   1 
ATOM   734  O O   . GLY A 1 95  ? 13.130  -25.605 10.647  1.00 38.47 ? 97  GLY A O   1 
ATOM   735  N N   . ILE A 1 96  ? 13.731  -23.533 9.969   1.00 31.45 ? 98  ILE A N   1 
ATOM   736  C CA  . ILE A 1 96  ? 15.156  -23.776 9.992   1.00 30.41 ? 98  ILE A CA  1 
ATOM   737  C C   . ILE A 1 96  ? 15.776  -22.815 11.020  1.00 32.27 ? 98  ILE A C   1 
ATOM   738  O O   . ILE A 1 96  ? 15.659  -21.587 10.901  1.00 32.16 ? 98  ILE A O   1 
ATOM   739  C CB  . ILE A 1 96  ? 15.825  -23.520 8.614   1.00 30.25 ? 98  ILE A CB  1 
ATOM   740  C CG1 . ILE A 1 96  ? 15.126  -24.251 7.473   1.00 30.90 ? 98  ILE A CG1 1 
ATOM   741  C CG2 . ILE A 1 96  ? 17.324  -23.820 8.689   1.00 29.78 ? 98  ILE A CG2 1 
ATOM   742  C CD1 . ILE A 1 96  ? 15.732  -24.083 6.082   1.00 30.94 ? 98  ILE A CD1 1 
ATOM   743  N N   . GLU A 1 97  ? 16.430  -23.373 12.027  1.00 34.37 ? 99  GLU A N   1 
ATOM   744  C CA  . GLU A 1 97  ? 17.251  -22.599 12.934  1.00 34.67 ? 99  GLU A CA  1 
ATOM   745  C C   . GLU A 1 97  ? 18.545  -22.114 12.284  1.00 33.21 ? 99  GLU A C   1 
ATOM   746  O O   . GLU A 1 97  ? 19.131  -22.842 11.477  1.00 31.96 ? 99  GLU A O   1 
ATOM   747  C CB  . GLU A 1 97  ? 17.516  -23.359 14.209  1.00 38.55 ? 99  GLU A CB  1 
ATOM   748  C CG  . GLU A 1 97  ? 16.219  -23.706 14.918  1.00 46.44 ? 99  GLU A CG  1 
ATOM   749  C CD  . GLU A 1 97  ? 16.345  -24.142 16.362  1.00 58.32 ? 99  GLU A CD  1 
ATOM   750  O OE1 . GLU A 1 97  ? 17.406  -24.689 16.733  1.00 57.07 ? 99  GLU A OE1 1 
ATOM   751  O OE2 . GLU A 1 97  ? 15.373  -23.926 17.126  1.00 66.68 ? 99  GLU A OE2 1 
ATOM   752  N N   . PRO A 1 98  ? 19.005  -20.874 12.589  1.00 30.48 ? 100 PRO A N   1 
ATOM   753  C CA  . PRO A 1 98  ? 20.235  -20.389 11.996  1.00 30.35 ? 100 PRO A CA  1 
ATOM   754  C C   . PRO A 1 98  ? 21.496  -20.927 12.670  1.00 31.01 ? 100 PRO A C   1 
ATOM   755  O O   . PRO A 1 98  ? 22.360  -20.187 13.075  1.00 30.83 ? 100 PRO A O   1 
ATOM   756  C CB  . PRO A 1 98  ? 20.078  -18.851 12.156  1.00 31.45 ? 100 PRO A CB  1 
ATOM   757  C CG  . PRO A 1 98  ? 19.340  -18.697 13.441  1.00 31.94 ? 100 PRO A CG  1 
ATOM   758  C CD  . PRO A 1 98  ? 18.386  -19.837 13.469  1.00 30.83 ? 100 PRO A CD  1 
ATOM   759  N N   . MET A 1 99  ? 21.617  -22.248 12.769  1.00 31.52 ? 101 MET A N   1 
ATOM   760  C CA  . MET A 1 99  ? 22.750  -22.918 13.358  1.00 32.59 ? 101 MET A CA  1 
ATOM   761  C C   . MET A 1 99  ? 23.060  -24.125 12.504  1.00 31.13 ? 101 MET A C   1 
ATOM   762  O O   . MET A 1 99  ? 22.144  -24.790 12.009  1.00 29.48 ? 101 MET A O   1 
ATOM   763  C CB  . MET A 1 99  ? 22.365  -23.423 14.756  1.00 37.87 ? 101 MET A CB  1 
ATOM   764  C CG  . MET A 1 99  ? 22.107  -22.295 15.777  1.00 48.47 ? 101 MET A CG  1 
ATOM   765  S SD  . MET A 1 99  ? 20.911  -22.651 17.115  1.00 72.24 ? 101 MET A SD  1 
ATOM   766  C CE  . MET A 1 99  ? 20.881  -24.498 17.181  1.00 69.83 ? 101 MET A CE  1 
ATOM   767  N N   . TRP A 1 100 ? 24.312  -24.437 12.339  1.00 32.80 ? 102 TRP A N   1 
ATOM   768  C CA  . TRP A 1 100 ? 24.706  -25.387 11.311  1.00 36.39 ? 102 TRP A CA  1 
ATOM   769  C C   . TRP A 1 100 ? 24.237  -26.796 11.628  1.00 38.19 ? 102 TRP A C   1 
ATOM   770  O O   . TRP A 1 100 ? 24.094  -27.563 10.702  1.00 37.77 ? 102 TRP A O   1 
ATOM   771  C CB  . TRP A 1 100 ? 26.195  -25.345 10.998  1.00 38.27 ? 102 TRP A CB  1 
ATOM   772  C CG  . TRP A 1 100 ? 27.086  -26.113 11.936  1.00 40.90 ? 102 TRP A CG  1 
ATOM   773  C CD1 . TRP A 1 100 ? 27.603  -25.677 13.119  1.00 43.46 ? 102 TRP A CD1 1 
ATOM   774  C CD2 . TRP A 1 100 ? 27.589  -27.460 11.749  1.00 41.12 ? 102 TRP A CD2 1 
ATOM   775  N NE1 . TRP A 1 100 ? 28.354  -26.679 13.706  1.00 43.93 ? 102 TRP A NE1 1 
ATOM   776  C CE2 . TRP A 1 100 ? 28.394  -27.763 12.865  1.00 42.81 ? 102 TRP A CE2 1 
ATOM   777  C CE3 . TRP A 1 100 ? 27.427  -28.428 10.756  1.00 41.52 ? 102 TRP A CE3 1 
ATOM   778  C CZ2 . TRP A 1 100 ? 29.058  -28.981 12.993  1.00 43.44 ? 102 TRP A CZ2 1 
ATOM   779  C CZ3 . TRP A 1 100 ? 28.090  -29.632 10.887  1.00 42.60 ? 102 TRP A CZ3 1 
ATOM   780  C CH2 . TRP A 1 100 ? 28.885  -29.895 11.994  1.00 43.20 ? 102 TRP A CH2 1 
ATOM   781  N N   . GLU A 1 101 ? 23.970  -27.119 12.880  1.00 38.57 ? 103 GLU A N   1 
ATOM   782  C CA  . GLU A 1 101 ? 23.619  -28.459 13.259  1.00 41.33 ? 103 GLU A CA  1 
ATOM   783  C C   . GLU A 1 101 ? 22.124  -28.725 13.037  1.00 40.05 ? 103 GLU A C   1 
ATOM   784  O O   . GLU A 1 101 ? 21.723  -29.888 13.180  1.00 38.87 ? 103 GLU A O   1 
ATOM   785  C CB  . GLU A 1 101 ? 24.134  -28.785 14.687  1.00 46.34 ? 103 GLU A CB  1 
ATOM   786  C CG  . GLU A 1 101 ? 23.483  -28.001 15.833  1.00 56.94 ? 103 GLU A CG  1 
ATOM   787  C CD  . GLU A 1 101 ? 24.025  -26.627 16.248  1.00 63.00 ? 103 GLU A CD  1 
ATOM   788  O OE1 . GLU A 1 101 ? 24.757  -25.975 15.464  1.00 51.16 ? 103 GLU A OE1 1 
ATOM   789  O OE2 . GLU A 1 101 ? 23.697  -26.207 17.388  1.00 70.27 ? 103 GLU A OE2 1 
ATOM   790  N N   . ASP A 1 102 ? 21.267  -27.702 12.640  1.00 36.03 ? 104 ASP A N   1 
ATOM   791  C CA  . ASP A 1 102 ? 19.900  -27.945 12.138  1.00 34.13 ? 104 ASP A CA  1 
ATOM   792  C C   . ASP A 1 102 ? 19.942  -28.979 11.002  1.00 35.65 ? 104 ASP A C   1 
ATOM   793  O O   . ASP A 1 102 ? 20.897  -28.979 10.216  1.00 35.47 ? 104 ASP A O   1 
ATOM   794  C CB  . ASP A 1 102 ? 19.238  -26.636 11.618  1.00 33.59 ? 104 ASP A CB  1 
ATOM   795  C CG  . ASP A 1 102 ? 17.757  -26.709 11.269  1.00 37.42 ? 104 ASP A CG  1 
ATOM   796  O OD1 . ASP A 1 102 ? 17.408  -27.294 10.202  1.00 38.32 ? 104 ASP A OD1 1 
ATOM   797  O OD2 . ASP A 1 102 ? 16.929  -26.156 12.043  1.00 38.39 ? 104 ASP A OD2 1 
ATOM   798  N N   . GLU A 1 103 ? 18.932  -29.876 10.927  1.00 36.47 ? 105 GLU A N   1 
ATOM   799  C CA  . GLU A 1 103 ? 18.846  -30.907 9.891   1.00 38.67 ? 105 GLU A CA  1 
ATOM   800  C C   . GLU A 1 103 ? 18.996  -30.328 8.473   1.00 36.23 ? 105 GLU A C   1 
ATOM   801  O O   . GLU A 1 103 ? 19.621  -30.951 7.626   1.00 36.66 ? 105 GLU A O   1 
ATOM   802  C CB  . GLU A 1 103 ? 17.471  -31.633 9.980   1.00 44.56 ? 105 GLU A CB  1 
ATOM   803  C CG  . GLU A 1 103 ? 17.318  -32.824 9.049   1.00 57.58 ? 105 GLU A CG  1 
ATOM   804  C CD  . GLU A 1 103 ? 18.024  -34.090 9.497   1.00 72.65 ? 105 GLU A CD  1 
ATOM   805  O OE1 . GLU A 1 103 ? 18.774  -34.046 10.500  1.00 75.63 ? 105 GLU A OE1 1 
ATOM   806  O OE2 . GLU A 1 103 ? 17.819  -35.135 8.838   1.00 78.63 ? 105 GLU A OE2 1 
ATOM   807  N N   . LYS A 1 104 ? 18.433  -29.150 8.228   1.00 34.68 ? 106 LYS A N   1 
ATOM   808  C CA  . LYS A 1 104 ? 18.486  -28.483 6.933   1.00 31.91 ? 106 LYS A CA  1 
ATOM   809  C C   . LYS A 1 104 ? 19.815  -27.757 6.647   1.00 31.43 ? 106 LYS A C   1 
ATOM   810  O O   . LYS A 1 104 ? 20.042  -27.364 5.500   1.00 31.75 ? 106 LYS A O   1 
ATOM   811  C CB  . LYS A 1 104 ? 17.283  -27.518 6.783   1.00 32.92 ? 106 LYS A CB  1 
ATOM   812  C CG  . LYS A 1 104 ? 15.904  -28.166 6.629   1.00 40.01 ? 106 LYS A CG  1 
ATOM   813  C CD  . LYS A 1 104 ? 15.780  -28.915 5.303   1.00 50.67 ? 106 LYS A CD  1 
ATOM   814  C CE  . LYS A 1 104 ? 14.373  -29.362 4.943   1.00 55.12 ? 106 LYS A CE  1 
ATOM   815  N NZ  . LYS A 1 104 ? 14.435  -30.450 3.918   1.00 61.59 ? 106 LYS A NZ  1 
ATOM   816  N N   . ASN A 1 105 ? 20.697  -27.597 7.638   1.00 29.95 ? 107 ASN A N   1 
ATOM   817  C CA  . ASN A 1 105 ? 22.012  -26.975 7.446   1.00 28.54 ? 107 ASN A CA  1 
ATOM   818  C C   . ASN A 1 105 ? 23.193  -27.945 7.601   1.00 30.21 ? 107 ASN A C   1 
ATOM   819  O O   . ASN A 1 105 ? 24.256  -27.715 6.994   1.00 30.86 ? 107 ASN A O   1 
ATOM   820  C CB  . ASN A 1 105 ? 22.200  -25.860 8.449   1.00 28.02 ? 107 ASN A CB  1 
ATOM   821  C CG  . ASN A 1 105 ? 21.186  -24.744 8.324   1.00 29.72 ? 107 ASN A CG  1 
ATOM   822  O OD1 . ASN A 1 105 ? 20.810  -24.363 7.232   1.00 30.82 ? 107 ASN A OD1 1 
ATOM   823  N ND2 . ASN A 1 105 ? 20.734  -24.206 9.410   1.00 28.75 ? 107 ASN A ND2 1 
ATOM   824  N N   . LYS A 1 106 ? 23.043  -29.013 8.382   1.00 31.40 ? 108 LYS A N   1 
ATOM   825  C CA  . LYS A 1 106 ? 24.211  -29.864 8.717   1.00 32.13 ? 108 LYS A CA  1 
ATOM   826  C C   . LYS A 1 106 ? 24.925  -30.480 7.520   1.00 31.31 ? 108 LYS A C   1 
ATOM   827  O O   . LYS A 1 106 ? 26.128  -30.687 7.634   1.00 32.05 ? 108 LYS A O   1 
ATOM   828  C CB  . LYS A 1 106 ? 23.878  -30.962 9.732   1.00 36.16 ? 108 LYS A CB  1 
ATOM   829  C CG  . LYS A 1 106 ? 22.791  -31.918 9.288   1.00 44.67 ? 108 LYS A CG  1 
ATOM   830  C CD  . LYS A 1 106 ? 22.619  -33.043 10.349  1.00 50.81 ? 108 LYS A CD  1 
ATOM   831  C CE  . LYS A 1 106 ? 21.956  -34.268 9.770   1.00 60.81 ? 108 LYS A CE  1 
ATOM   832  N NZ  . LYS A 1 106 ? 21.351  -35.159 10.816  1.00 67.35 ? 108 LYS A NZ  1 
ATOM   833  N N   . ARG A 1 107 ? 24.228  -30.754 6.414   1.00 29.68 ? 109 ARG A N   1 
ATOM   834  C CA  . ARG A 1 107 ? 24.916  -31.272 5.225   1.00 31.91 ? 109 ARG A CA  1 
ATOM   835  C C   . ARG A 1 107 ? 25.225  -30.211 4.191   1.00 32.42 ? 109 ARG A C   1 
ATOM   836  O O   . ARG A 1 107 ? 25.603  -30.549 3.077   1.00 32.22 ? 109 ARG A O   1 
ATOM   837  C CB  . ARG A 1 107 ? 24.033  -32.337 4.554   1.00 36.76 ? 109 ARG A CB  1 
ATOM   838  C CG  . ARG A 1 107 ? 23.719  -33.548 5.418   1.00 44.06 ? 109 ARG A CG  1 
ATOM   839  C CD  . ARG A 1 107 ? 22.533  -34.254 4.789   1.00 52.29 ? 109 ARG A CD  1 
ATOM   840  N NE  . ARG A 1 107 ? 21.968  -35.257 5.687   1.00 62.64 ? 109 ARG A NE  1 
ATOM   841  C CZ  . ARG A 1 107 ? 21.011  -35.054 6.597   1.00 66.97 ? 109 ARG A CZ  1 
ATOM   842  N NH1 . ARG A 1 107 ? 20.580  -36.067 7.351   1.00 67.66 ? 109 ARG A NH1 1 
ATOM   843  N NH2 . ARG A 1 107 ? 20.476  -33.839 6.760   1.00 63.84 ? 109 ARG A NH2 1 
ATOM   844  N N   . GLY A 1 108 ? 25.098  -28.939 4.564   1.00 30.66 ? 110 GLY A N   1 
ATOM   845  C CA  . GLY A 1 108 ? 25.239  -27.820 3.666   1.00 28.05 ? 110 GLY A CA  1 
ATOM   846  C C   . GLY A 1 108 ? 26.445  -26.975 3.946   1.00 28.78 ? 110 GLY A C   1 
ATOM   847  O O   . GLY A 1 108 ? 27.467  -27.418 4.497   1.00 27.42 ? 110 GLY A O   1 
ATOM   848  N N   . GLY A 1 109 ? 26.329  -25.698 3.566   1.00 26.27 ? 111 GLY A N   1 
ATOM   849  C CA  . GLY A 1 109 ? 27.466  -24.805 3.598   1.00 25.91 ? 111 GLY A CA  1 
ATOM   850  C C   . GLY A 1 109 ? 27.019  -23.389 3.312   1.00 25.32 ? 111 GLY A C   1 
ATOM   851  O O   . GLY A 1 109 ? 25.812  -23.104 3.308   1.00 24.43 ? 111 GLY A O   1 
ATOM   852  N N   . ARG A 1 110 ? 27.961  -22.510 3.095   1.00 24.38 ? 112 ARG A N   1 
ATOM   853  C CA  . ARG A 1 110 ? 27.653  -21.112 2.842   1.00 23.80 ? 112 ARG A CA  1 
ATOM   854  C C   . ARG A 1 110 ? 28.574  -20.473 1.845   1.00 24.89 ? 112 ARG A C   1 
ATOM   855  O O   . ARG A 1 110 ? 29.724  -20.833 1.806   1.00 27.07 ? 112 ARG A O   1 
ATOM   856  C CB  . ARG A 1 110 ? 27.683  -20.340 4.139   1.00 25.88 ? 112 ARG A CB  1 
ATOM   857  C CG  . ARG A 1 110 ? 29.065  -20.206 4.767   1.00 31.25 ? 112 ARG A CG  1 
ATOM   858  C CD  . ARG A 1 110 ? 29.104  -19.556 6.132   1.00 37.64 ? 112 ARG A CD  1 
ATOM   859  N NE  . ARG A 1 110 ? 30.514  -19.512 6.568   1.00 43.63 ? 112 ARG A NE  1 
ATOM   860  C CZ  . ARG A 1 110 ? 30.987  -18.876 7.637   1.00 45.07 ? 112 ARG A CZ  1 
ATOM   861  N NH1 . ARG A 1 110 ? 32.298  -18.917 7.924   1.00 45.51 ? 112 ARG A NH1 1 
ATOM   862  N NH2 . ARG A 1 110 ? 30.174  -18.195 8.423   1.00 42.08 ? 112 ARG A NH2 1 
ATOM   863  N N   . TRP A 1 111 ? 28.038  -19.492 1.083   1.00 23.38 ? 113 TRP A N   1 
ATOM   864  C CA  . TRP A 1 111 ? 28.793  -18.532 0.257   1.00 22.98 ? 113 TRP A CA  1 
ATOM   865  C C   . TRP A 1 111 ? 29.072  -17.342 1.104   1.00 26.07 ? 113 TRP A C   1 
ATOM   866  O O   . TRP A 1 111 ? 28.115  -16.713 1.590   1.00 26.02 ? 113 TRP A O   1 
ATOM   867  C CB  . TRP A 1 111 ? 27.948  -18.161 -0.941  1.00 23.19 ? 113 TRP A CB  1 
ATOM   868  C CG  . TRP A 1 111 ? 27.961  -19.174 -2.022  1.00 24.12 ? 113 TRP A CG  1 
ATOM   869  C CD1 . TRP A 1 111 ? 26.920  -19.958 -2.408  1.00 26.28 ? 113 TRP A CD1 1 
ATOM   870  C CD2 . TRP A 1 111 ? 29.059  -19.487 -2.905  1.00 26.45 ? 113 TRP A CD2 1 
ATOM   871  N NE1 . TRP A 1 111 ? 27.296  -20.746 -3.492  1.00 27.85 ? 113 TRP A NE1 1 
ATOM   872  C CE2 . TRP A 1 111 ? 28.623  -20.513 -3.770  1.00 28.57 ? 113 TRP A CE2 1 
ATOM   873  C CE3 . TRP A 1 111 ? 30.396  -19.050 -3.005  1.00 28.52 ? 113 TRP A CE3 1 
ATOM   874  C CZ2 . TRP A 1 111 ? 29.448  -21.054 -4.752  1.00 30.21 ? 113 TRP A CZ2 1 
ATOM   875  C CZ3 . TRP A 1 111 ? 31.204  -19.608 -3.976  1.00 30.46 ? 113 TRP A CZ3 1 
ATOM   876  C CH2 . TRP A 1 111 ? 30.725  -20.605 -4.824  1.00 30.89 ? 113 TRP A CH2 1 
ATOM   877  N N   . LEU A 1 112 ? 30.369  -17.012 1.329   1.00 25.59 ? 114 LEU A N   1 
ATOM   878  C CA  . LEU A 1 112 ? 30.785  -16.011 2.305   1.00 27.38 ? 114 LEU A CA  1 
ATOM   879  C C   . LEU A 1 112 ? 31.498  -14.849 1.635   1.00 28.13 ? 114 LEU A C   1 
ATOM   880  O O   . LEU A 1 112 ? 32.414  -15.074 0.817   1.00 26.88 ? 114 LEU A O   1 
ATOM   881  C CB  . LEU A 1 112 ? 31.751  -16.656 3.313   1.00 31.03 ? 114 LEU A CB  1 
ATOM   882  C CG  . LEU A 1 112 ? 32.375  -15.737 4.362   1.00 36.45 ? 114 LEU A CG  1 
ATOM   883  C CD1 . LEU A 1 112 ? 31.342  -15.362 5.357   1.00 38.36 ? 114 LEU A CD1 1 
ATOM   884  C CD2 . LEU A 1 112 ? 33.601  -16.434 5.028   1.00 39.14 ? 114 LEU A CD2 1 
ATOM   885  N N   . ILE A 1 113 ? 31.140  -13.624 2.018   1.00 27.37 ? 115 ILE A N   1 
ATOM   886  C CA  . ILE A 1 113 ? 31.960  -12.426 1.708   1.00 31.78 ? 115 ILE A CA  1 
ATOM   887  C C   . ILE A 1 113 ? 32.356  -11.778 3.026   1.00 30.53 ? 115 ILE A C   1 
ATOM   888  O O   . ILE A 1 113 ? 31.570  -11.750 4.010   1.00 27.11 ? 115 ILE A O   1 
ATOM   889  C CB  . ILE A 1 113 ? 31.250  -11.480 0.671   1.00 35.47 ? 115 ILE A CB  1 
ATOM   890  C CG1 . ILE A 1 113 ? 32.190  -10.304 0.117   1.00 38.21 ? 115 ILE A CG1 1 
ATOM   891  C CG2 . ILE A 1 113 ? 30.013  -10.820 1.299   1.00 38.03 ? 115 ILE A CG2 1 
ATOM   892  C CD1 . ILE A 1 113 ? 33.341  -10.658 -0.839  1.00 41.57 ? 115 ILE A CD1 1 
ATOM   893  N N   . THR A 1 114 ? 33.600  -11.297 3.092   1.00 31.89 ? 116 THR A N   1 
ATOM   894  C CA  . THR A 1 114 ? 34.089  -10.628 4.286   1.00 32.43 ? 116 THR A CA  1 
ATOM   895  C C   . THR A 1 114 ? 34.373  -9.197  3.872   1.00 33.37 ? 116 THR A C   1 
ATOM   896  O O   . THR A 1 114 ? 34.977  -8.948  2.836   1.00 34.75 ? 116 THR A O   1 
ATOM   897  C CB  . THR A 1 114 ? 35.324  -11.279 4.886   1.00 38.05 ? 116 THR A CB  1 
ATOM   898  O OG1 . THR A 1 114 ? 35.054  -12.677 5.129   1.00 42.49 ? 116 THR A OG1 1 
ATOM   899  C CG2 . THR A 1 114 ? 35.715  -10.634 6.242   1.00 40.79 ? 116 THR A CG2 1 
ATOM   900  N N   . LEU A 1 115 ? 33.942  -8.303  4.684   1.00 32.44 ? 117 LEU A N   1 
ATOM   901  C CA  . LEU A 1 115 ? 34.132  -6.852  4.517   1.00 34.14 ? 117 LEU A CA  1 
ATOM   902  C C   . LEU A 1 115 ? 35.176  -6.322  5.550   1.00 38.23 ? 117 LEU A C   1 
ATOM   903  O O   . LEU A 1 115 ? 35.099  -6.659  6.731   1.00 39.02 ? 117 LEU A O   1 
ATOM   904  C CB  . LEU A 1 115 ? 32.818  -6.121  4.755   1.00 34.26 ? 117 LEU A CB  1 
ATOM   905  C CG  . LEU A 1 115 ? 31.661  -6.420  3.802   1.00 38.03 ? 117 LEU A CG  1 
ATOM   906  C CD1 . LEU A 1 115 ? 30.486  -5.487  4.106   1.00 38.63 ? 117 LEU A CD1 1 
ATOM   907  C CD2 . LEU A 1 115 ? 32.048  -6.181  2.360   1.00 39.22 ? 117 LEU A CD2 1 
ATOM   908  N N   . ASN A 1 116 ? 36.098  -5.440  5.129   1.00 40.21 ? 118 ASN A N   1 
ATOM   909  C CA  . ASN A 1 116 ? 37.045  -4.843  6.084   1.00 42.62 ? 118 ASN A CA  1 
ATOM   910  C C   . ASN A 1 116 ? 36.331  -3.739  6.962   1.00 44.46 ? 118 ASN A C   1 
ATOM   911  O O   . ASN A 1 116 ? 35.200  -3.312  6.697   1.00 41.75 ? 118 ASN A O   1 
ATOM   912  C CB  . ASN A 1 116 ? 38.290  -4.335  5.347   1.00 44.75 ? 118 ASN A CB  1 
ATOM   913  C CG  . ASN A 1 116 ? 39.582  -4.273  6.186   1.00 52.54 ? 118 ASN A CG  1 
ATOM   914  O OD1 . ASN A 1 116 ? 39.596  -4.120  7.431   1.00 52.95 ? 118 ASN A OD1 1 
ATOM   915  N ND2 . ASN A 1 116 ? 40.697  -4.392  5.500   1.00 54.67 ? 118 ASN A ND2 1 
ATOM   916  N N   . LYS A 1 117 ? 37.018  -3.305  8.012   1.00 47.26 ? 119 LYS A N   1 
ATOM   917  C CA  . LYS A 1 117 ? 36.497  -2.402  9.040   1.00 50.78 ? 119 LYS A CA  1 
ATOM   918  C C   . LYS A 1 117 ? 35.876  -1.104  8.428   1.00 51.31 ? 119 LYS A C   1 
ATOM   919  O O   . LYS A 1 117 ? 34.818  -0.695  8.900   1.00 52.60 ? 119 LYS A O   1 
ATOM   920  C CB  . LYS A 1 117 ? 37.631  -2.019  10.019  1.00 55.47 ? 119 LYS A CB  1 
ATOM   921  C CG  . LYS A 1 117 ? 38.164  -3.197  10.866  1.00 62.74 ? 119 LYS A CG  1 
ATOM   922  C CD  . LYS A 1 117 ? 39.650  -2.993  11.290  1.00 67.63 ? 119 LYS A CD  1 
ATOM   923  C CE  . LYS A 1 117 ? 40.458  -4.280  11.387  1.00 72.31 ? 119 LYS A CE  1 
ATOM   924  N NZ  . LYS A 1 117 ? 40.639  -5.001  10.086  1.00 74.42 ? 119 LYS A NZ  1 
ATOM   925  N N   . GLN A 1 118 ? 36.498  -0.527  7.375   1.00 50.88 ? 120 GLN A N   1 
ATOM   926  C CA  . GLN A 1 118 ? 36.039  0.699   6.693   1.00 52.77 ? 120 GLN A CA  1 
ATOM   927  C C   . GLN A 1 118 ? 34.786  0.455   5.802   1.00 50.85 ? 120 GLN A C   1 
ATOM   928  O O   . GLN A 1 118 ? 33.918  1.341   5.667   1.00 50.56 ? 120 GLN A O   1 
ATOM   929  C CB  . GLN A 1 118 ? 37.194  1.354   5.874   1.00 58.30 ? 120 GLN A CB  1 
ATOM   930  C CG  . GLN A 1 118 ? 37.361  2.884   6.096   1.00 66.58 ? 120 GLN A CG  1 
ATOM   931  C CD  . GLN A 1 118 ? 38.761  3.447   5.820   1.00 75.67 ? 120 GLN A CD  1 
ATOM   932  O OE1 . GLN A 1 118 ? 39.785  2.918   6.297   1.00 79.41 ? 120 GLN A OE1 1 
ATOM   933  N NE2 . GLN A 1 118 ? 38.858  4.551   5.057   1.00 76.15 ? 120 GLN A NE2 1 
ATOM   934  N N   . GLN A 1 119 ? 34.642  -0.770  5.244   1.00 47.56 ? 121 GLN A N   1 
ATOM   935  C CA  . GLN A 1 119 ? 33.438  -1.148  4.489   1.00 44.67 ? 121 GLN A CA  1 
ATOM   936  C C   . GLN A 1 119 ? 32.218  -1.247  5.323   1.00 43.27 ? 121 GLN A C   1 
ATOM   937  O O   . GLN A 1 119 ? 31.118  -1.346  4.746   1.00 42.92 ? 121 GLN A O   1 
ATOM   938  C CB  . GLN A 1 119 ? 33.707  -2.450  3.730   1.00 44.43 ? 121 GLN A CB  1 
ATOM   939  C CG  . GLN A 1 119 ? 34.724  -2.237  2.650   1.00 45.46 ? 121 GLN A CG  1 
ATOM   940  C CD  . GLN A 1 119 ? 34.989  -3.519  1.964   1.00 43.63 ? 121 GLN A CD  1 
ATOM   941  O OE1 . GLN A 1 119 ? 35.758  -4.376  2.467   1.00 42.50 ? 121 GLN A OE1 1 
ATOM   942  N NE2 . GLN A 1 119 ? 34.372  -3.695  0.827   1.00 44.10 ? 121 GLN A NE2 1 
ATOM   943  N N   . ARG A 1 120 ? 32.327  -1.181  6.691   1.00 42.92 ? 122 ARG A N   1 
ATOM   944  C CA  . ARG A 1 120 ? 31.143  -1.150  7.511   1.00 43.87 ? 122 ARG A CA  1 
ATOM   945  C C   . ARG A 1 120 ? 30.249  0.047   7.165   1.00 43.19 ? 122 ARG A C   1 
ATOM   946  O O   . ARG A 1 120 ? 29.036  -0.105  6.992   1.00 40.99 ? 122 ARG A O   1 
ATOM   947  C CB  . ARG A 1 120 ? 31.464  -1.136  9.001   1.00 46.64 ? 122 ARG A CB  1 
ATOM   948  C CG  . ARG A 1 120 ? 30.169  -1.158  9.826   1.00 53.42 ? 122 ARG A CG  1 
ATOM   949  C CD  . ARG A 1 120 ? 30.412  -1.329  11.291  1.00 59.59 ? 122 ARG A CD  1 
ATOM   950  N NE  . ARG A 1 120 ? 30.912  -2.662  11.630  1.00 61.46 ? 122 ARG A NE  1 
ATOM   951  C CZ  . ARG A 1 120 ? 31.542  -2.954  12.765  1.00 64.65 ? 122 ARG A CZ  1 
ATOM   952  N NH1 . ARG A 1 120 ? 31.970  -4.187  12.994  1.00 62.62 ? 122 ARG A NH1 1 
ATOM   953  N NH2 . ARG A 1 120 ? 31.765  -2.006  13.680  1.00 65.40 ? 122 ARG A NH2 1 
ATOM   954  N N   . ARG A 1 121 ? 30.875  1.254   7.049   1.00 44.16 ? 123 ARG A N   1 
ATOM   955  C CA  . ARG A 1 121 ? 30.081  2.431   6.815   1.00 46.20 ? 123 ARG A CA  1 
ATOM   956  C C   . ARG A 1 121 ? 29.626  2.447   5.379   1.00 46.62 ? 123 ARG A C   1 
ATOM   957  O O   . ARG A 1 121 ? 28.497  2.861   5.160   1.00 49.85 ? 123 ARG A O   1 
ATOM   958  C CB  . ARG A 1 121 ? 30.855  3.711   7.101   1.00 51.60 ? 123 ARG A CB  1 
ATOM   959  C CG  . ARG A 1 121 ? 31.360  3.868   8.525   1.00 60.76 ? 123 ARG A CG  1 
ATOM   960  C CD  . ARG A 1 121 ? 30.412  4.641   9.436   1.00 70.73 ? 123 ARG A CD  1 
ATOM   961  N NE  . ARG A 1 121 ? 29.316  3.830   9.987   1.00 78.95 ? 123 ARG A NE  1 
ATOM   962  C CZ  . ARG A 1 121 ? 29.458  2.841   10.876  1.00 83.61 ? 123 ARG A CZ  1 
ATOM   963  N NH1 . ARG A 1 121 ? 30.667  2.510   11.334  1.00 85.17 ? 123 ARG A NH1 1 
ATOM   964  N NH2 . ARG A 1 121 ? 28.398  2.174   11.306  1.00 82.78 ? 123 ARG A NH2 1 
ATOM   965  N N   . SER A 1 122 ? 30.440  2.019   4.404   1.00 45.11 ? 124 SER A N   1 
ATOM   966  C CA  . SER A 1 122 ? 30.060  2.163   2.992   1.00 46.01 ? 124 SER A CA  1 
ATOM   967  C C   . SER A 1 122 ? 29.206  1.023   2.369   1.00 44.80 ? 124 SER A C   1 
ATOM   968  O O   . SER A 1 122 ? 28.286  1.321   1.618   1.00 45.98 ? 124 SER A O   1 
ATOM   969  C CB  . SER A 1 122 ? 31.307  2.346   2.145   1.00 48.97 ? 124 SER A CB  1 
ATOM   970  O OG  . SER A 1 122 ? 32.176  1.239   2.354   1.00 51.43 ? 124 SER A OG  1 
ATOM   971  N N   . ASP A 1 123 ? 29.503  -0.264  2.669   1.00 40.37 ? 125 ASP A N   1 
ATOM   972  C CA  . ASP A 1 123 ? 28.959  -1.422  1.936   1.00 36.30 ? 125 ASP A CA  1 
ATOM   973  C C   . ASP A 1 123 ? 28.101  -2.374  2.774   1.00 32.32 ? 125 ASP A C   1 
ATOM   974  O O   . ASP A 1 123 ? 27.309  -3.127  2.189   1.00 31.95 ? 125 ASP A O   1 
ATOM   975  C CB  . ASP A 1 123 ? 30.075  -2.294  1.402   1.00 41.15 ? 125 ASP A CB  1 
ATOM   976  C CG  . ASP A 1 123 ? 30.975  -1.641  0.376   1.00 51.84 ? 125 ASP A CG  1 
ATOM   977  O OD1 . ASP A 1 123 ? 30.504  -0.779  -0.333  1.00 53.13 ? 125 ASP A OD1 1 
ATOM   978  O OD2 . ASP A 1 123 ? 32.161  -2.030  0.296   1.00 55.95 ? 125 ASP A OD2 1 
ATOM   979  N N   . LEU A 1 124 ? 28.226  -2.379  4.090   1.00 29.56 ? 126 LEU A N   1 
ATOM   980  C CA  . LEU A 1 124 ? 27.550  -3.421  4.893   1.00 29.19 ? 126 LEU A CA  1 
ATOM   981  C C   . LEU A 1 124 ? 26.016  -3.347  4.713   1.00 27.40 ? 126 LEU A C   1 
ATOM   982  O O   . LEU A 1 124 ? 25.376  -4.386  4.493   1.00 26.21 ? 126 LEU A O   1 
ATOM   983  C CB  . LEU A 1 124 ? 27.916  -3.300  6.362   1.00 31.71 ? 126 LEU A CB  1 
ATOM   984  C CG  . LEU A 1 124 ? 27.237  -4.331  7.286   1.00 35.50 ? 126 LEU A CG  1 
ATOM   985  C CD1 . LEU A 1 124 ? 27.684  -5.663  6.963   1.00 34.21 ? 126 LEU A CD1 1 
ATOM   986  C CD2 . LEU A 1 124 ? 27.536  -4.024  8.735   1.00 39.17 ? 126 LEU A CD2 1 
ATOM   987  N N   . ASN A 1 125 ? 25.369  -2.176  4.877   1.00 26.85 ? 127 ASN A N   1 
ATOM   988  C CA  . ASN A 1 125 ? 23.909  -2.091  4.785   1.00 28.27 ? 127 ASN A CA  1 
ATOM   989  C C   . ASN A 1 125 ? 23.381  -2.464  3.419   1.00 26.26 ? 127 ASN A C   1 
ATOM   990  O O   . ASN A 1 125 ? 22.367  -3.182  3.281   1.00 25.48 ? 127 ASN A O   1 
ATOM   991  C CB  . ASN A 1 125 ? 23.452  -0.656  5.182   1.00 31.84 ? 127 ASN A CB  1 
ATOM   992  C CG  . ASN A 1 125 ? 23.691  -0.271  6.627   1.00 38.30 ? 127 ASN A CG  1 
ATOM   993  O OD1 . ASN A 1 125 ? 23.887  0.908   6.984   1.00 42.40 ? 127 ASN A OD1 1 
ATOM   994  N ND2 . ASN A 1 125 ? 23.748  -1.168  7.528   1.00 37.46 ? 127 ASN A ND2 1 
ATOM   995  N N   . ARG A 1 126 ? 24.085  -2.022  2.400   1.00 25.47 ? 128 ARG A N   1 
ATOM   996  C CA  . ARG A 1 126 ? 23.670  -2.268  1.031   1.00 27.87 ? 128 ARG A CA  1 
ATOM   997  C C   . ARG A 1 126 ? 23.833  -3.756  0.727   1.00 25.33 ? 128 ARG A C   1 
ATOM   998  O O   . ARG A 1 126 ? 22.928  -4.329  0.158   1.00 25.78 ? 128 ARG A O   1 
ATOM   999  C CB  . ARG A 1 126 ? 24.532  -1.463  0.033   1.00 32.51 ? 128 ARG A CB  1 
ATOM   1000 C CG  . ARG A 1 126 ? 24.407  -1.906  -1.465  1.00 41.14 ? 128 ARG A CG  1 
ATOM   1001 C CD  . ARG A 1 126 ? 22.975  -1.802  -1.980  1.00 47.00 ? 128 ARG A CD  1 
ATOM   1002 N NE  . ARG A 1 126 ? 22.485  -0.423  -1.958  1.00 44.81 ? 128 ARG A NE  1 
ATOM   1003 C CZ  . ARG A 1 126 ? 21.284  -0.040  -2.335  1.00 47.44 ? 128 ARG A CZ  1 
ATOM   1004 N NH1 . ARG A 1 126 ? 20.403  -0.929  -2.766  1.00 49.95 ? 128 ARG A NH1 1 
ATOM   1005 N NH2 . ARG A 1 126 ? 20.939  1.252   -2.281  1.00 50.62 ? 128 ARG A NH2 1 
ATOM   1006 N N   . PHE A 1 127 ? 24.956  -4.347  1.073   1.00 24.14 ? 129 PHE A N   1 
ATOM   1007 C CA  . PHE A 1 127 ? 25.113  -5.815  0.825   1.00 24.88 ? 129 PHE A CA  1 
ATOM   1008 C C   . PHE A 1 127 ? 24.136  -6.646  1.584   1.00 23.64 ? 129 PHE A C   1 
ATOM   1009 O O   . PHE A 1 127 ? 23.639  -7.643  1.032   1.00 23.47 ? 129 PHE A O   1 
ATOM   1010 C CB  . PHE A 1 127 ? 26.497  -6.296  1.089   1.00 25.08 ? 129 PHE A CB  1 
ATOM   1011 C CG  . PHE A 1 127 ? 27.582  -5.965  0.083   1.00 30.88 ? 129 PHE A CG  1 
ATOM   1012 C CD1 . PHE A 1 127 ? 27.342  -5.113  -0.971  1.00 34.47 ? 129 PHE A CD1 1 
ATOM   1013 C CD2 . PHE A 1 127 ? 28.773  -6.656  0.089   1.00 38.07 ? 129 PHE A CD2 1 
ATOM   1014 C CE1 . PHE A 1 127 ? 28.370  -4.800  -1.905  1.00 37.44 ? 129 PHE A CE1 1 
ATOM   1015 C CE2 . PHE A 1 127 ? 29.733  -6.435  -0.892  1.00 40.08 ? 129 PHE A CE2 1 
ATOM   1016 C CZ  . PHE A 1 127 ? 29.559  -5.428  -1.822  1.00 38.53 ? 129 PHE A CZ  1 
ATOM   1017 N N   . TRP A 1 128 ? 23.817  -6.267  2.806   1.00 24.38 ? 130 TRP A N   1 
ATOM   1018 C CA  . TRP A 1 128 ? 22.842  -7.024  3.574   1.00 24.05 ? 130 TRP A CA  1 
ATOM   1019 C C   . TRP A 1 128 ? 21.453  -6.934  2.924   1.00 23.99 ? 130 TRP A C   1 
ATOM   1020 O O   . TRP A 1 128 ? 20.807  -7.958  2.737   1.00 22.00 ? 130 TRP A O   1 
ATOM   1021 C CB  . TRP A 1 128 ? 22.807  -6.575  5.037   1.00 25.50 ? 130 TRP A CB  1 
ATOM   1022 C CG  . TRP A 1 128 ? 21.843  -7.294  5.911   1.00 25.97 ? 130 TRP A CG  1 
ATOM   1023 C CD1 . TRP A 1 128 ? 20.888  -6.714  6.703   1.00 28.68 ? 130 TRP A CD1 1 
ATOM   1024 C CD2 . TRP A 1 128 ? 21.726  -8.717  6.122   1.00 25.69 ? 130 TRP A CD2 1 
ATOM   1025 N NE1 . TRP A 1 128 ? 20.231  -7.668  7.415   1.00 28.74 ? 130 TRP A NE1 1 
ATOM   1026 C CE2 . TRP A 1 128 ? 20.724  -8.903  7.094   1.00 28.70 ? 130 TRP A CE2 1 
ATOM   1027 C CE3 . TRP A 1 128 ? 22.401  -9.823  5.632   1.00 26.00 ? 130 TRP A CE3 1 
ATOM   1028 C CZ2 . TRP A 1 128 ? 20.365  -10.143 7.542   1.00 29.58 ? 130 TRP A CZ2 1 
ATOM   1029 C CZ3 . TRP A 1 128 ? 22.023  -11.078 6.076   1.00 28.51 ? 130 TRP A CZ3 1 
ATOM   1030 C CH2 . TRP A 1 128 ? 21.012  -11.214 7.012   1.00 29.19 ? 130 TRP A CH2 1 
ATOM   1031 N N   . LEU A 1 129 ? 20.996  -5.739  2.551   1.00 22.69 ? 131 LEU A N   1 
ATOM   1032 C CA  . LEU A 1 129 ? 19.729  -5.614  1.840   1.00 23.82 ? 131 LEU A CA  1 
ATOM   1033 C C   . LEU A 1 129 ? 19.699  -6.405  0.529   1.00 24.68 ? 131 LEU A C   1 
ATOM   1034 O O   . LEU A 1 129 ? 18.728  -7.092  0.280   1.00 26.08 ? 131 LEU A O   1 
ATOM   1035 C CB  . LEU A 1 129 ? 19.382  -4.134  1.631   1.00 25.58 ? 131 LEU A CB  1 
ATOM   1036 C CG  . LEU A 1 129 ? 18.024  -3.889  0.956   1.00 28.39 ? 131 LEU A CG  1 
ATOM   1037 C CD1 . LEU A 1 129 ? 16.880  -4.538  1.701   1.00 28.73 ? 131 LEU A CD1 1 
ATOM   1038 C CD2 . LEU A 1 129 ? 17.753  -2.458  0.822   1.00 29.99 ? 131 LEU A CD2 1 
ATOM   1039 N N   . GLU A 1 130 ? 20.733  -6.344  -0.291  1.00 24.55 ? 132 GLU A N   1 
ATOM   1040 C CA  . GLU A 1 130 ? 20.758  -7.055  -1.582  1.00 26.13 ? 132 GLU A CA  1 
ATOM   1041 C C   . GLU A 1 130 ? 20.633  -8.575  -1.320  1.00 25.82 ? 132 GLU A C   1 
ATOM   1042 O O   . GLU A 1 130 ? 19.911  -9.270  -2.044  1.00 25.48 ? 132 GLU A O   1 
ATOM   1043 C CB  . GLU A 1 130 ? 22.028  -6.753  -2.392  1.00 29.50 ? 132 GLU A CB  1 
ATOM   1044 C CG  . GLU A 1 130 ? 22.134  -5.317  -2.937  1.00 34.92 ? 132 GLU A CG  1 
ATOM   1045 C CD  . GLU A 1 130 ? 20.892  -4.791  -3.642  1.00 41.03 ? 132 GLU A CD  1 
ATOM   1046 O OE1 . GLU A 1 130 ? 20.255  -5.554  -4.405  1.00 36.28 ? 132 GLU A OE1 1 
ATOM   1047 O OE2 . GLU A 1 130 ? 20.552  -3.602  -3.438  1.00 50.25 ? 132 GLU A OE2 1 
ATOM   1048 N N   . THR A 1 131 ? 21.299  -9.049  -0.288  1.00 23.18 ? 133 THR A N   1 
ATOM   1049 C CA  . THR A 1 131 ? 21.193  -10.475 0.100   1.00 23.05 ? 133 THR A CA  1 
ATOM   1050 C C   . THR A 1 131 ? 19.752  -10.821 0.476   1.00 24.00 ? 133 THR A C   1 
ATOM   1051 O O   . THR A 1 131 ? 19.213  -11.826 -0.002  1.00 26.29 ? 133 THR A O   1 
ATOM   1052 C CB  . THR A 1 131 ? 22.159  -10.742 1.265   1.00 24.13 ? 133 THR A CB  1 
ATOM   1053 O OG1 . THR A 1 131 ? 23.496  -10.364 0.902   1.00 24.69 ? 133 THR A OG1 1 
ATOM   1054 C CG2 . THR A 1 131 ? 22.159  -12.203 1.712   1.00 24.94 ? 133 THR A CG2 1 
ATOM   1055 N N   . LEU A 1 132 ? 19.097  -9.994  1.323   1.00 23.51 ? 134 LEU A N   1 
ATOM   1056 C CA  . LEU A 1 132 ? 17.722  -10.228 1.758   1.00 25.02 ? 134 LEU A CA  1 
ATOM   1057 C C   . LEU A 1 132 ? 16.765  -10.262 0.563   1.00 26.20 ? 134 LEU A C   1 
ATOM   1058 O O   . LEU A 1 132 ? 15.880  -11.137 0.513   1.00 23.55 ? 134 LEU A O   1 
ATOM   1059 C CB  . LEU A 1 132 ? 17.262  -9.159  2.748   1.00 26.04 ? 134 LEU A CB  1 
ATOM   1060 C CG  . LEU A 1 132 ? 18.005  -9.075  4.058   1.00 28.60 ? 134 LEU A CG  1 
ATOM   1061 C CD1 . LEU A 1 132 ? 17.584  -7.852  4.868   1.00 29.45 ? 134 LEU A CD1 1 
ATOM   1062 C CD2 . LEU A 1 132 ? 17.887  -10.336 4.832   1.00 32.09 ? 134 LEU A CD2 1 
ATOM   1063 N N   . LEU A 1 133 ? 16.967  -9.370  -0.396  1.00 25.88 ? 135 LEU A N   1 
ATOM   1064 C CA  . LEU A 1 133 ? 16.135  -9.348  -1.629  1.00 27.39 ? 135 LEU A CA  1 
ATOM   1065 C C   . LEU A 1 133 ? 16.348  -10.590 -2.514  1.00 27.68 ? 135 LEU A C   1 
ATOM   1066 O O   . LEU A 1 133 ? 15.390  -11.077 -3.087  1.00 27.77 ? 135 LEU A O   1 
ATOM   1067 C CB  . LEU A 1 133 ? 16.364  -8.043  -2.439  1.00 28.85 ? 135 LEU A CB  1 
ATOM   1068 C CG  . LEU A 1 133 ? 16.075  -6.733  -1.669  1.00 33.22 ? 135 LEU A CG  1 
ATOM   1069 C CD1 . LEU A 1 133 ? 16.357  -5.572  -2.519  1.00 34.44 ? 135 LEU A CD1 1 
ATOM   1070 C CD2 . LEU A 1 133 ? 14.715  -6.677  -1.104  1.00 34.22 ? 135 LEU A CD2 1 
ATOM   1071 N N   . CYS A 1 134 ? 17.537  -11.118 -2.579  1.00 28.83 ? 136 CYS A N   1 
ATOM   1072 C CA  . CYS A 1 134 ? 17.803  -12.441 -3.241  1.00 29.02 ? 136 CYS A CA  1 
ATOM   1073 C C   . CYS A 1 134 ? 17.022  -13.548 -2.646  1.00 29.12 ? 136 CYS A C   1 
ATOM   1074 O O   . CYS A 1 134 ? 16.510  -14.416 -3.399  1.00 32.54 ? 136 CYS A O   1 
ATOM   1075 C CB  . CYS A 1 134 ? 19.279  -12.801 -3.249  1.00 30.14 ? 136 CYS A CB  1 
ATOM   1076 S SG  . CYS A 1 134 ? 20.299  -11.800 -4.337  1.00 34.95 ? 136 CYS A SG  1 
ATOM   1077 N N   . LEU A 1 135 ? 16.982  -13.594 -1.309  1.00 25.67 ? 137 LEU A N   1 
ATOM   1078 C CA  . LEU A 1 135 ? 16.282  -14.627 -0.563  1.00 27.77 ? 137 LEU A CA  1 
ATOM   1079 C C   . LEU A 1 135 ? 14.765  -14.501 -0.807  1.00 27.88 ? 137 LEU A C   1 
ATOM   1080 O O   . LEU A 1 135 ? 14.168  -15.416 -1.344  1.00 28.72 ? 137 LEU A O   1 
ATOM   1081 C CB  . LEU A 1 135 ? 16.596  -14.558 0.946   1.00 26.71 ? 137 LEU A CB  1 
ATOM   1082 C CG  . LEU A 1 135 ? 17.786  -15.427 1.443   1.00 28.63 ? 137 LEU A CG  1 
ATOM   1083 C CD1 . LEU A 1 135 ? 19.018  -15.300 0.547   1.00 29.62 ? 137 LEU A CD1 1 
ATOM   1084 C CD2 . LEU A 1 135 ? 18.005  -15.097 2.877   1.00 31.83 ? 137 LEU A CD2 1 
ATOM   1085 N N   . ILE A 1 136 ? 14.175  -13.389 -0.430  1.00 26.08 ? 138 ILE A N   1 
ATOM   1086 C CA  . ILE A 1 136 ? 12.712  -13.288 -0.430  1.00 28.79 ? 138 ILE A CA  1 
ATOM   1087 C C   . ILE A 1 136 ? 12.163  -13.313 -1.860  1.00 30.16 ? 138 ILE A C   1 
ATOM   1088 O O   . ILE A 1 136 ? 11.054  -13.756 -2.033  1.00 32.49 ? 138 ILE A O   1 
ATOM   1089 C CB  . ILE A 1 136 ? 12.180  -12.107 0.398   1.00 28.45 ? 138 ILE A CB  1 
ATOM   1090 C CG1 . ILE A 1 136 ? 12.497  -10.772 -0.279  1.00 29.64 ? 138 ILE A CG1 1 
ATOM   1091 C CG2 . ILE A 1 136 ? 12.738  -12.157 1.862   1.00 29.84 ? 138 ILE A CG2 1 
ATOM   1092 C CD1 . ILE A 1 136 ? 11.910  -9.550  0.387   1.00 31.57 ? 138 ILE A CD1 1 
ATOM   1093 N N   . GLY A 1 137 ? 12.908  -12.801 -2.820  1.00 29.58 ? 139 GLY A N   1 
ATOM   1094 C CA  . GLY A 1 137 ? 12.537  -12.753 -4.227  1.00 32.06 ? 139 GLY A CA  1 
ATOM   1095 C C   . GLY A 1 137 ? 12.731  -14.035 -5.022  1.00 33.71 ? 139 GLY A C   1 
ATOM   1096 O O   . GLY A 1 137 ? 12.352  -14.065 -6.204  1.00 34.54 ? 139 GLY A O   1 
ATOM   1097 N N   . GLU A 1 138 ? 13.295  -15.098 -4.400  1.00 31.54 ? 140 GLU A N   1 
ATOM   1098 C CA  . GLU A 1 138 ? 13.558  -16.399 -5.014  1.00 32.28 ? 140 GLU A CA  1 
ATOM   1099 C C   . GLU A 1 138 ? 14.374  -16.249 -6.307  1.00 33.90 ? 140 GLU A C   1 
ATOM   1100 O O   . GLU A 1 138 ? 13.966  -16.733 -7.359  1.00 34.06 ? 140 GLU A O   1 
ATOM   1101 C CB  . GLU A 1 138 ? 12.254  -17.160 -5.266  1.00 34.06 ? 140 GLU A CB  1 
ATOM   1102 C CG  . GLU A 1 138 ? 11.411  -17.400 -4.024  1.00 40.54 ? 140 GLU A CG  1 
ATOM   1103 C CD  . GLU A 1 138 ? 11.926  -18.445 -3.052  1.00 45.20 ? 140 GLU A CD  1 
ATOM   1104 O OE1 . GLU A 1 138 ? 12.339  -19.525 -3.528  1.00 51.94 ? 140 GLU A OE1 1 
ATOM   1105 O OE2 . GLU A 1 138 ? 11.892  -18.212 -1.823  1.00 43.61 ? 140 GLU A OE2 1 
ATOM   1106 N N   . SER A 1 139 ? 15.542  -15.589 -6.192  1.00 34.06 ? 141 SER A N   1 
ATOM   1107 C CA  . SER A 1 139 ? 16.374  -15.127 -7.308  1.00 34.28 ? 141 SER A CA  1 
ATOM   1108 C C   . SER A 1 139 ? 17.231  -16.186 -7.960  1.00 33.90 ? 141 SER A C   1 
ATOM   1109 O O   . SER A 1 139 ? 17.901  -15.907 -8.941  1.00 35.06 ? 141 SER A O   1 
ATOM   1110 C CB  . SER A 1 139 ? 17.294  -14.013 -6.817  1.00 37.52 ? 141 SER A CB  1 
ATOM   1111 O OG  . SER A 1 139 ? 16.539  -12.925 -6.318  1.00 41.25 ? 141 SER A OG  1 
ATOM   1112 N N   . PHE A 1 140 ? 17.247  -17.391 -7.439  1.00 33.26 ? 142 PHE A N   1 
ATOM   1113 C CA  . PHE A 1 140 ? 18.090  -18.467 -7.935  1.00 33.87 ? 142 PHE A CA  1 
ATOM   1114 C C   . PHE A 1 140 ? 17.291  -19.521 -8.717  1.00 35.66 ? 142 PHE A C   1 
ATOM   1115 O O   . PHE A 1 140 ? 17.743  -20.659 -8.840  1.00 34.98 ? 142 PHE A O   1 
ATOM   1116 C CB  . PHE A 1 140 ? 18.806  -19.096 -6.720  1.00 32.21 ? 142 PHE A CB  1 
ATOM   1117 C CG  . PHE A 1 140 ? 19.541  -18.079 -5.884  1.00 29.89 ? 142 PHE A CG  1 
ATOM   1118 C CD1 . PHE A 1 140 ? 20.577  -17.347 -6.418  1.00 30.32 ? 142 PHE A CD1 1 
ATOM   1119 C CD2 . PHE A 1 140 ? 19.106  -17.755 -4.609  1.00 30.23 ? 142 PHE A CD2 1 
ATOM   1120 C CE1 . PHE A 1 140 ? 21.217  -16.361 -5.651  1.00 31.84 ? 142 PHE A CE1 1 
ATOM   1121 C CE2 . PHE A 1 140 ? 19.767  -16.803 -3.846  1.00 30.97 ? 142 PHE A CE2 1 
ATOM   1122 C CZ  . PHE A 1 140 ? 20.824  -16.135 -4.352  1.00 30.05 ? 142 PHE A CZ  1 
ATOM   1123 N N   . ASP A 1 141 ? 16.097  -19.162 -9.205  1.00 38.77 ? 143 ASP A N   1 
ATOM   1124 C CA  . ASP A 1 141 ? 15.240  -20.042 -10.017 1.00 42.56 ? 143 ASP A CA  1 
ATOM   1125 C C   . ASP A 1 141 ? 14.908  -21.357 -9.207  1.00 43.44 ? 143 ASP A C   1 
ATOM   1126 O O   . ASP A 1 141 ? 14.633  -21.231 -8.001  1.00 44.38 ? 143 ASP A O   1 
ATOM   1127 C CB  . ASP A 1 141 ? 15.885  -20.242 -11.420 1.00 47.66 ? 143 ASP A CB  1 
ATOM   1128 C CG  . ASP A 1 141 ? 15.777  -18.979 -12.277 1.00 62.50 ? 143 ASP A CG  1 
ATOM   1129 O OD1 . ASP A 1 141 ? 14.630  -18.430 -12.411 1.00 65.41 ? 143 ASP A OD1 1 
ATOM   1130 O OD2 . ASP A 1 141 ? 16.827  -18.530 -12.816 1.00 67.40 ? 143 ASP A OD2 1 
ATOM   1131 N N   . ASP A 1 142 ? 14.944  -22.570 -9.788  1.00 43.55 ? 144 ASP A N   1 
ATOM   1132 C CA  . ASP A 1 142 ? 14.629  -23.789 -9.017  1.00 43.68 ? 144 ASP A CA  1 
ATOM   1133 C C   . ASP A 1 142 ? 15.643  -24.015 -7.875  1.00 40.07 ? 144 ASP A C   1 
ATOM   1134 O O   . ASP A 1 142 ? 15.300  -24.677 -6.886  1.00 39.61 ? 144 ASP A O   1 
ATOM   1135 C CB  . ASP A 1 142 ? 14.631  -25.032 -9.900  1.00 49.18 ? 144 ASP A CB  1 
ATOM   1136 C CG  . ASP A 1 142 ? 13.500  -25.132 -10.907 1.00 60.96 ? 144 ASP A CG  1 
ATOM   1137 O OD1 . ASP A 1 142 ? 12.676  -24.194 -10.965 1.00 62.91 ? 144 ASP A OD1 1 
ATOM   1138 O OD2 . ASP A 1 142 ? 13.440  -26.170 -11.642 1.00 64.96 ? 144 ASP A OD2 1 
ATOM   1139 N N   . TYR A 1 143 ? 16.864  -23.502 -8.018  1.00 36.50 ? 145 TYR A N   1 
ATOM   1140 C CA  . TYR A 1 143 ? 17.885  -23.660 -6.987  1.00 35.89 ? 145 TYR A CA  1 
ATOM   1141 C C   . TYR A 1 143 ? 17.623  -22.802 -5.720  1.00 34.18 ? 145 TYR A C   1 
ATOM   1142 O O   . TYR A 1 143 ? 18.316  -22.951 -4.712  1.00 33.73 ? 145 TYR A O   1 
ATOM   1143 C CB  . TYR A 1 143 ? 19.257  -23.394 -7.577  1.00 38.07 ? 145 TYR A CB  1 
ATOM   1144 C CG  . TYR A 1 143 ? 19.598  -24.331 -8.714  1.00 41.49 ? 145 TYR A CG  1 
ATOM   1145 C CD1 . TYR A 1 143 ? 19.335  -25.691 -8.623  1.00 43.06 ? 145 TYR A CD1 1 
ATOM   1146 C CD2 . TYR A 1 143 ? 20.150  -23.855 -9.892  1.00 44.26 ? 145 TYR A CD2 1 
ATOM   1147 C CE1 . TYR A 1 143 ? 19.665  -26.561 -9.643  1.00 44.94 ? 145 TYR A CE1 1 
ATOM   1148 C CE2 . TYR A 1 143 ? 20.479  -24.726 -10.934 1.00 46.06 ? 145 TYR A CE2 1 
ATOM   1149 C CZ  . TYR A 1 143 ? 20.232  -26.082 -10.795 1.00 47.86 ? 145 TYR A CZ  1 
ATOM   1150 O OH  . TYR A 1 143 ? 20.507  -26.989 -11.790 1.00 53.04 ? 145 TYR A OH  1 
ATOM   1151 N N   . SER A 1 144 ? 16.616  -21.920 -5.745  1.00 33.19 ? 146 SER A N   1 
ATOM   1152 C CA  . SER A 1 144 ? 16.181  -21.217 -4.566  1.00 32.33 ? 146 SER A CA  1 
ATOM   1153 C C   . SER A 1 144 ? 15.708  -22.154 -3.486  1.00 31.47 ? 146 SER A C   1 
ATOM   1154 O O   . SER A 1 144 ? 15.808  -21.820 -2.294  1.00 30.04 ? 146 SER A O   1 
ATOM   1155 C CB  . SER A 1 144 ? 15.094  -20.213 -4.906  1.00 35.49 ? 146 SER A CB  1 
ATOM   1156 O OG  . SER A 1 144 ? 15.651  -19.059 -5.521  1.00 41.87 ? 146 SER A OG  1 
ATOM   1157 N N   . ASP A 1 145 ? 15.208  -23.348 -3.860  1.00 31.07 ? 147 ASP A N   1 
ATOM   1158 C CA  . ASP A 1 145 ? 14.829  -24.318 -2.860  1.00 31.96 ? 147 ASP A CA  1 
ATOM   1159 C C   . ASP A 1 145 ? 16.025  -24.806 -2.055  1.00 31.47 ? 147 ASP A C   1 
ATOM   1160 O O   . ASP A 1 145 ? 15.810  -25.306 -0.941  1.00 34.33 ? 147 ASP A O   1 
ATOM   1161 C CB  . ASP A 1 145 ? 14.134  -25.539 -3.506  1.00 36.18 ? 147 ASP A CB  1 
ATOM   1162 C CG  . ASP A 1 145 ? 12.761  -25.208 -4.066  1.00 44.64 ? 147 ASP A CG  1 
ATOM   1163 O OD1 . ASP A 1 145 ? 12.158  -24.196 -3.621  1.00 43.17 ? 147 ASP A OD1 1 
ATOM   1164 O OD2 . ASP A 1 145 ? 12.284  -25.957 -4.946  1.00 51.04 ? 147 ASP A OD2 1 
ATOM   1165 N N   . ASP A 1 146 ? 17.248  -24.707 -2.567  1.00 27.57 ? 148 ASP A N   1 
ATOM   1166 C CA  . ASP A 1 146 ? 18.457  -25.114 -1.771  1.00 27.10 ? 148 ASP A CA  1 
ATOM   1167 C C   . ASP A 1 146 ? 18.890  -24.057 -0.765  1.00 27.84 ? 148 ASP A C   1 
ATOM   1168 O O   . ASP A 1 146 ? 19.789  -24.341 0.006   1.00 29.52 ? 148 ASP A O   1 
ATOM   1169 C CB  . ASP A 1 146 ? 19.632  -25.394 -2.710  1.00 29.81 ? 148 ASP A CB  1 
ATOM   1170 C CG  . ASP A 1 146 ? 19.597  -26.765 -3.298  1.00 40.73 ? 148 ASP A CG  1 
ATOM   1171 O OD1 . ASP A 1 146 ? 18.645  -27.039 -4.069  1.00 45.67 ? 148 ASP A OD1 1 
ATOM   1172 O OD2 . ASP A 1 146 ? 20.535  -27.575 -2.991  1.00 40.97 ? 148 ASP A OD2 1 
ATOM   1173 N N   . VAL A 1 147 ? 18.305  -22.856 -0.804  1.00 27.12 ? 149 VAL A N   1 
ATOM   1174 C CA  . VAL A 1 147 ? 18.699  -21.797 0.081   1.00 24.73 ? 149 VAL A CA  1 
ATOM   1175 C C   . VAL A 1 147 ? 18.000  -22.042 1.398   1.00 25.92 ? 149 VAL A C   1 
ATOM   1176 O O   . VAL A 1 147 ? 16.786  -22.273 1.400   1.00 27.15 ? 149 VAL A O   1 
ATOM   1177 C CB  . VAL A 1 147 ? 18.366  -20.421 -0.513  1.00 26.54 ? 149 VAL A CB  1 
ATOM   1178 C CG1 . VAL A 1 147 ? 18.556  -19.336 0.548   1.00 27.20 ? 149 VAL A CG1 1 
ATOM   1179 C CG2 . VAL A 1 147 ? 19.228  -20.152 -1.742  1.00 27.05 ? 149 VAL A CG2 1 
ATOM   1180 N N   . CYS A 1 148 ? 18.755  -21.989 2.507   1.00 22.07 ? 150 CYS A N   1 
ATOM   1181 C CA  . CYS A 1 148 ? 18.232  -22.020 3.871   1.00 22.38 ? 150 CYS A CA  1 
ATOM   1182 C C   . CYS A 1 148 ? 17.996  -20.594 4.423   1.00 23.50 ? 150 CYS A C   1 
ATOM   1183 O O   . CYS A 1 148 ? 16.964  -20.332 5.050   1.00 23.47 ? 150 CYS A O   1 
ATOM   1184 C CB  . CYS A 1 148 ? 19.194  -22.795 4.754   1.00 23.99 ? 150 CYS A CB  1 
ATOM   1185 S SG  . CYS A 1 148 ? 19.338  -24.490 4.248   1.00 29.32 ? 150 CYS A SG  1 
ATOM   1186 N N   . GLY A 1 149 ? 18.957  -19.707 4.212   1.00 22.75 ? 151 GLY A N   1 
ATOM   1187 C CA  . GLY A 1 149 ? 18.891  -18.381 4.777   1.00 22.01 ? 151 GLY A CA  1 
ATOM   1188 C C   . GLY A 1 149 ? 20.188  -17.647 4.584   1.00 22.02 ? 151 GLY A C   1 
ATOM   1189 O O   . GLY A 1 149 ? 21.008  -18.063 3.776   1.00 22.61 ? 151 GLY A O   1 
ATOM   1190 N N   . ALA A 1 150 ? 20.314  -16.517 5.235   1.00 21.71 ? 152 ALA A N   1 
ATOM   1191 C CA  . ALA A 1 150 ? 21.486  -15.650 5.172   1.00 22.33 ? 152 ALA A CA  1 
ATOM   1192 C C   . ALA A 1 150 ? 21.788  -15.124 6.547   1.00 23.16 ? 152 ALA A C   1 
ATOM   1193 O O   . ALA A 1 150 ? 20.890  -14.982 7.398   1.00 21.89 ? 152 ALA A O   1 
ATOM   1194 C CB  . ALA A 1 150 ? 21.289  -14.505 4.199   1.00 22.88 ? 152 ALA A CB  1 
ATOM   1195 N N   . VAL A 1 151 ? 23.061  -14.830 6.772   1.00 21.56 ? 153 VAL A N   1 
ATOM   1196 C CA  . VAL A 1 151 ? 23.548  -14.384 8.071   1.00 21.12 ? 153 VAL A CA  1 
ATOM   1197 C C   . VAL A 1 151 ? 24.492  -13.208 7.865   1.00 23.23 ? 153 VAL A C   1 
ATOM   1198 O O   . VAL A 1 151 ? 25.344  -13.266 6.988   1.00 22.24 ? 153 VAL A O   1 
ATOM   1199 C CB  . VAL A 1 151 ? 24.279  -15.508 8.815   1.00 23.22 ? 153 VAL A CB  1 
ATOM   1200 C CG1 . VAL A 1 151 ? 24.849  -15.026 10.145  1.00 24.85 ? 153 VAL A CG1 1 
ATOM   1201 C CG2 . VAL A 1 151 ? 23.400  -16.752 9.014   1.00 22.71 ? 153 VAL A CG2 1 
ATOM   1202 N N   . VAL A 1 152 ? 24.334  -12.177 8.660   1.00 23.87 ? 154 VAL A N   1 
ATOM   1203 C CA  . VAL A 1 152 ? 25.342  -11.110 8.788   1.00 23.84 ? 154 VAL A CA  1 
ATOM   1204 C C   . VAL A 1 152 ? 25.943  -11.117 10.189  1.00 24.74 ? 154 VAL A C   1 
ATOM   1205 O O   . VAL A 1 152 ? 25.195  -11.059 11.161  1.00 24.40 ? 154 VAL A O   1 
ATOM   1206 C CB  . VAL A 1 152 ? 24.794  -9.715  8.367   1.00 24.66 ? 154 VAL A CB  1 
ATOM   1207 C CG1 . VAL A 1 152 ? 23.546  -9.309  9.134   1.00 26.01 ? 154 VAL A CG1 1 
ATOM   1208 C CG2 . VAL A 1 152 ? 25.886  -8.661  8.534   1.00 26.48 ? 154 VAL A CG2 1 
ATOM   1209 N N   . ASN A 1 153 ? 27.267  -11.243 10.284  1.00 25.69 ? 155 ASN A N   1 
ATOM   1210 C CA  . ASN A 1 153 ? 28.006  -11.216 11.539  1.00 27.18 ? 155 ASN A CA  1 
ATOM   1211 C C   . ASN A 1 153 ? 28.721  -9.860  11.618  1.00 29.14 ? 155 ASN A C   1 
ATOM   1212 O O   . ASN A 1 153 ? 29.599  -9.587  10.817  1.00 30.90 ? 155 ASN A O   1 
ATOM   1213 C CB  . ASN A 1 153 ? 29.043  -12.303 11.610  1.00 28.23 ? 155 ASN A CB  1 
ATOM   1214 C CG  . ASN A 1 153 ? 28.572  -13.679 11.315  1.00 31.76 ? 155 ASN A CG  1 
ATOM   1215 O OD1 . ASN A 1 153 ? 28.934  -14.278 10.315  1.00 35.78 ? 155 ASN A OD1 1 
ATOM   1216 N ND2 . ASN A 1 153 ? 27.766  -14.209 12.191  1.00 33.67 ? 155 ASN A ND2 1 
ATOM   1217 N N   . VAL A 1 154 ? 28.316  -9.052  12.555  1.00 30.08 ? 156 VAL A N   1 
ATOM   1218 C CA  . VAL A 1 154 ? 28.927  -7.734  12.739  1.00 35.13 ? 156 VAL A CA  1 
ATOM   1219 C C   . VAL A 1 154 ? 30.065  -7.919  13.760  1.00 37.28 ? 156 VAL A C   1 
ATOM   1220 O O   . VAL A 1 154 ? 29.817  -8.330  14.900  1.00 37.13 ? 156 VAL A O   1 
ATOM   1221 C CB  . VAL A 1 154 ? 27.872  -6.690  13.131  1.00 37.43 ? 156 VAL A CB  1 
ATOM   1222 C CG1 . VAL A 1 154 ? 28.511  -5.288  13.198  1.00 41.23 ? 156 VAL A CG1 1 
ATOM   1223 C CG2 . VAL A 1 154 ? 26.695  -6.711  12.161  1.00 38.29 ? 156 VAL A CG2 1 
ATOM   1224 N N   . ARG A 1 155 ? 31.313  -7.635  13.361  1.00 38.21 ? 157 ARG A N   1 
ATOM   1225 C CA  . ARG A 1 155 ? 32.468  -7.889  14.222  1.00 39.99 ? 157 ARG A CA  1 
ATOM   1226 C C   . ARG A 1 155 ? 33.478  -6.770  14.116  1.00 44.58 ? 157 ARG A C   1 
ATOM   1227 O O   . ARG A 1 155 ? 33.609  -6.146  13.068  1.00 45.05 ? 157 ARG A O   1 
ATOM   1228 C CB  . ARG A 1 155 ? 33.203  -9.191  13.862  1.00 39.76 ? 157 ARG A CB  1 
ATOM   1229 C CG  . ARG A 1 155 ? 32.452  -10.473 14.070  1.00 44.91 ? 157 ARG A CG  1 
ATOM   1230 C CD  . ARG A 1 155 ? 32.111  -10.776 15.504  1.00 45.94 ? 157 ARG A CD  1 
ATOM   1231 N NE  . ARG A 1 155 ? 31.388  -12.046 15.582  1.00 48.36 ? 157 ARG A NE  1 
ATOM   1232 C CZ  . ARG A 1 155 ? 30.079  -12.212 15.415  1.00 48.97 ? 157 ARG A CZ  1 
ATOM   1233 N NH1 . ARG A 1 155 ? 29.289  -11.168 15.153  1.00 42.95 ? 157 ARG A NH1 1 
ATOM   1234 N NH2 . ARG A 1 155 ? 29.543  -13.423 15.504  1.00 52.70 ? 157 ARG A NH2 1 
ATOM   1235 N N   . ALA A 1 156 ? 34.197  -6.519  15.208  1.00 46.77 ? 158 ALA A N   1 
ATOM   1236 C CA  . ALA A 1 156 ? 35.253  -5.504  15.236  1.00 49.39 ? 158 ALA A CA  1 
ATOM   1237 C C   . ALA A 1 156 ? 36.294  -5.699  14.100  1.00 51.61 ? 158 ALA A C   1 
ATOM   1238 O O   . ALA A 1 156 ? 36.600  -4.747  13.404  1.00 53.19 ? 158 ALA A O   1 
ATOM   1239 C CB  . ALA A 1 156 ? 35.935  -5.522  16.612  1.00 49.32 ? 158 ALA A CB  1 
ATOM   1240 N N   . LYS A 1 157 ? 36.803  -6.928  13.912  1.00 51.91 ? 159 LYS A N   1 
ATOM   1241 C CA  . LYS A 1 157 ? 37.823  -7.236  12.905  1.00 51.93 ? 159 LYS A CA  1 
ATOM   1242 C C   . LYS A 1 157 ? 37.333  -7.193  11.435  1.00 50.58 ? 159 LYS A C   1 
ATOM   1243 O O   . LYS A 1 157 ? 38.156  -7.177  10.518  1.00 51.17 ? 159 LYS A O   1 
ATOM   1244 C CB  . LYS A 1 157 ? 38.400  -8.635  13.173  1.00 57.14 ? 159 LYS A CB  1 
ATOM   1245 C CG  . LYS A 1 157 ? 39.764  -8.871  12.496  1.00 67.99 ? 159 LYS A CG  1 
ATOM   1246 C CD  . LYS A 1 157 ? 40.416  -10.202 12.892  1.00 75.34 ? 159 LYS A CD  1 
ATOM   1247 C CE  . LYS A 1 157 ? 41.916  -10.185 12.648  1.00 79.91 ? 159 LYS A CE  1 
ATOM   1248 N NZ  . LYS A 1 157 ? 42.652  -9.429  13.709  1.00 82.77 ? 159 LYS A NZ  1 
ATOM   1249 N N   . GLY A 1 158 ? 36.011  -7.180  11.205  1.00 46.58 ? 160 GLY A N   1 
ATOM   1250 C CA  . GLY A 1 158 ? 35.479  -7.187  9.851   1.00 42.75 ? 160 GLY A CA  1 
ATOM   1251 C C   . GLY A 1 158 ? 34.185  -7.976  9.766   1.00 41.11 ? 160 GLY A C   1 
ATOM   1252 O O   . GLY A 1 158 ? 34.068  -9.041  10.375  1.00 44.48 ? 160 GLY A O   1 
ATOM   1253 N N   . ASP A 1 159 ? 33.243  -7.494  9.002   1.00 35.51 ? 161 ASP A N   1 
ATOM   1254 C CA  . ASP A 1 159 ? 31.879  -8.050  8.999   1.00 33.15 ? 161 ASP A CA  1 
ATOM   1255 C C   . ASP A 1 159 ? 31.820  -9.161  7.953   1.00 30.56 ? 161 ASP A C   1 
ATOM   1256 O O   . ASP A 1 159 ? 32.596  -9.178  7.015   1.00 32.07 ? 161 ASP A O   1 
ATOM   1257 C CB  . ASP A 1 159 ? 30.872  -6.950  8.671   1.00 34.66 ? 161 ASP A CB  1 
ATOM   1258 C CG  . ASP A 1 159 ? 30.965  -5.702  9.590   1.00 48.77 ? 161 ASP A CG  1 
ATOM   1259 O OD1 . ASP A 1 159 ? 30.930  -5.864  10.833  1.00 51.04 ? 161 ASP A OD1 1 
ATOM   1260 O OD2 . ASP A 1 159 ? 31.057  -4.580  9.063   1.00 51.51 ? 161 ASP A OD2 1 
ATOM   1261 N N   . LYS A 1 160 ? 30.899  -10.108 8.112   1.00 28.79 ? 162 LYS A N   1 
ATOM   1262 C CA  . LYS A 1 160 ? 30.785  -11.241 7.200   1.00 26.79 ? 162 LYS A CA  1 
ATOM   1263 C C   . LYS A 1 160 ? 29.307  -11.337 6.802   1.00 24.76 ? 162 LYS A C   1 
ATOM   1264 O O   . LYS A 1 160 ? 28.456  -11.153 7.665   1.00 25.83 ? 162 LYS A O   1 
ATOM   1265 C CB  . LYS A 1 160 ? 31.196  -12.538 7.905   1.00 30.08 ? 162 LYS A CB  1 
ATOM   1266 C CG  . LYS A 1 160 ? 32.673  -12.663 8.298   1.00 39.15 ? 162 LYS A CG  1 
ATOM   1267 C CD  . LYS A 1 160 ? 33.005  -14.135 8.439   1.00 52.48 ? 162 LYS A CD  1 
ATOM   1268 C CE  . LYS A 1 160 ? 33.843  -14.611 9.614   1.00 63.56 ? 162 LYS A CE  1 
ATOM   1269 N NZ  . LYS A 1 160 ? 33.893  -16.126 9.620   1.00 70.02 ? 162 LYS A NZ  1 
ATOM   1270 N N   . ILE A 1 161 ? 29.012  -11.574 5.533   1.00 22.23 ? 163 ILE A N   1 
ATOM   1271 C CA  . ILE A 1 161 ? 27.636  -11.825 5.050   1.00 22.28 ? 163 ILE A CA  1 
ATOM   1272 C C   . ILE A 1 161 ? 27.719  -13.137 4.326   1.00 22.22 ? 163 ILE A C   1 
ATOM   1273 O O   . ILE A 1 161 ? 28.663  -13.372 3.546   1.00 23.78 ? 163 ILE A O   1 
ATOM   1274 C CB  . ILE A 1 161 ? 27.058  -10.748 4.152   1.00 26.25 ? 163 ILE A CB  1 
ATOM   1275 C CG1 . ILE A 1 161 ? 27.064  -9.370  4.865   1.00 30.13 ? 163 ILE A CG1 1 
ATOM   1276 C CG2 . ILE A 1 161 ? 25.661  -11.151 3.703   1.00 26.81 ? 163 ILE A CG2 1 
ATOM   1277 C CD1 . ILE A 1 161 ? 26.746  -8.206  4.033   1.00 33.46 ? 163 ILE A CD1 1 
ATOM   1278 N N   . ALA A 1 162 ? 26.760  -14.006 4.567   1.00 23.60 ? 164 ALA A N   1 
ATOM   1279 C CA  . ALA A 1 162 ? 26.790  -15.359 3.973   1.00 22.80 ? 164 ALA A CA  1 
ATOM   1280 C C   . ALA A 1 162 ? 25.373  -15.817 3.566   1.00 23.61 ? 164 ALA A C   1 
ATOM   1281 O O   . ALA A 1 162 ? 24.428  -15.520 4.306   1.00 22.98 ? 164 ALA A O   1 
ATOM   1282 C CB  . ALA A 1 162 ? 27.393  -16.331 4.942   1.00 24.31 ? 164 ALA A CB  1 
ATOM   1283 N N   . ILE A 1 163 ? 25.244  -16.510 2.439   1.00 23.13 ? 165 ILE A N   1 
ATOM   1284 C CA  . ILE A 1 163 ? 24.053  -17.269 2.104   1.00 22.09 ? 165 ILE A CA  1 
ATOM   1285 C C   . ILE A 1 163 ? 24.326  -18.729 2.416   1.00 22.65 ? 165 ILE A C   1 
ATOM   1286 O O   . ILE A 1 163 ? 25.273  -19.305 1.901   1.00 22.31 ? 165 ILE A O   1 
ATOM   1287 C CB  . ILE A 1 163 ? 23.579  -17.089 0.641   1.00 22.85 ? 165 ILE A CB  1 
ATOM   1288 C CG1 . ILE A 1 163 ? 23.110  -15.620 0.414   1.00 25.94 ? 165 ILE A CG1 1 
ATOM   1289 C CG2 . ILE A 1 163 ? 22.493  -18.086 0.286   1.00 23.90 ? 165 ILE A CG2 1 
ATOM   1290 C CD1 . ILE A 1 163 ? 22.633  -15.318 -0.994  1.00 29.54 ? 165 ILE A CD1 1 
ATOM   1291 N N   . TRP A 1 164 ? 23.449  -19.310 3.232   1.00 21.82 ? 166 TRP A N   1 
ATOM   1292 C CA  . TRP A 1 164 ? 23.536  -20.707 3.646   1.00 20.54 ? 166 TRP A CA  1 
ATOM   1293 C C   . TRP A 1 164 ? 22.633  -21.566 2.738   1.00 22.07 ? 166 TRP A C   1 
ATOM   1294 O O   . TRP A 1 164 ? 21.496  -21.222 2.447   1.00 22.75 ? 166 TRP A O   1 
ATOM   1295 C CB  . TRP A 1 164 ? 23.055  -20.833 5.081   1.00 21.83 ? 166 TRP A CB  1 
ATOM   1296 C CG  . TRP A 1 164 ? 23.951  -20.277 6.151   1.00 23.74 ? 166 TRP A CG  1 
ATOM   1297 C CD1 . TRP A 1 164 ? 24.800  -19.205 6.066   1.00 23.78 ? 166 TRP A CD1 1 
ATOM   1298 C CD2 . TRP A 1 164 ? 24.122  -20.824 7.475   1.00 25.27 ? 166 TRP A CD2 1 
ATOM   1299 N NE1 . TRP A 1 164 ? 25.544  -19.104 7.242   1.00 23.97 ? 166 TRP A NE1 1 
ATOM   1300 C CE2 . TRP A 1 164 ? 25.078  -20.032 8.143   1.00 25.77 ? 166 TRP A CE2 1 
ATOM   1301 C CE3 . TRP A 1 164 ? 23.493  -21.859 8.177   1.00 25.90 ? 166 TRP A CE3 1 
ATOM   1302 C CZ2 . TRP A 1 164 ? 25.459  -20.280 9.443   1.00 28.21 ? 166 TRP A CZ2 1 
ATOM   1303 C CZ3 . TRP A 1 164 ? 23.855  -22.085 9.485   1.00 28.45 ? 166 TRP A CZ3 1 
ATOM   1304 C CH2 . TRP A 1 164 ? 24.826  -21.316 10.103  1.00 28.52 ? 166 TRP A CH2 1 
ATOM   1305 N N   . THR A 1 165 ? 23.185  -22.690 2.316   1.00 22.92 ? 167 THR A N   1 
ATOM   1306 C CA  . THR A 1 165 ? 22.475  -23.629 1.466   1.00 25.39 ? 167 THR A CA  1 
ATOM   1307 C C   . THR A 1 165 ? 22.477  -25.011 2.134   1.00 25.41 ? 167 THR A C   1 
ATOM   1308 O O   . THR A 1 165 ? 23.302  -25.323 3.006   1.00 25.02 ? 167 THR A O   1 
ATOM   1309 C CB  . THR A 1 165 ? 23.027  -23.647 0.046   1.00 29.53 ? 167 THR A CB  1 
ATOM   1310 O OG1 . THR A 1 165 ? 24.202  -24.432 0.021   1.00 33.54 ? 167 THR A OG1 1 
ATOM   1311 C CG2 . THR A 1 165 ? 23.335  -22.269 -0.514  1.00 32.47 ? 167 THR A CG2 1 
ATOM   1312 N N   . THR A 1 166 ? 21.554  -25.840 1.688   1.00 25.58 ? 168 THR A N   1 
ATOM   1313 C CA  . THR A 1 166 ? 21.160  -27.029 2.406   1.00 26.05 ? 168 THR A CA  1 
ATOM   1314 C C   . THR A 1 166 ? 22.045  -28.276 2.125   1.00 27.29 ? 168 THR A C   1 
ATOM   1315 O O   . THR A 1 166 ? 22.109  -29.158 2.996   1.00 28.21 ? 168 THR A O   1 
ATOM   1316 C CB  . THR A 1 166 ? 19.658  -27.344 2.123   1.00 30.32 ? 168 THR A CB  1 
ATOM   1317 O OG1 . THR A 1 166 ? 19.175  -28.286 3.082   1.00 29.17 ? 168 THR A OG1 1 
ATOM   1318 C CG2 . THR A 1 166 ? 19.413  -27.825 0.730   1.00 31.33 ? 168 THR A CG2 1 
ATOM   1319 N N   . GLU A 1 167 ? 22.706  -28.350 0.961   1.00 28.16 ? 169 GLU A N   1 
ATOM   1320 C CA  . GLU A 1 167 ? 23.341  -29.601 0.521   1.00 30.07 ? 169 GLU A CA  1 
ATOM   1321 C C   . GLU A 1 167 ? 24.578  -29.379 -0.261  1.00 31.45 ? 169 GLU A C   1 
ATOM   1322 O O   . GLU A 1 167 ? 24.533  -28.946 -1.409  1.00 30.66 ? 169 GLU A O   1 
ATOM   1323 C CB  . GLU A 1 167 ? 22.322  -30.416 -0.317  1.00 33.87 ? 169 GLU A CB  1 
ATOM   1324 C CG  . GLU A 1 167 ? 22.786  -31.783 -0.795  1.00 39.34 ? 169 GLU A CG  1 
ATOM   1325 C CD  . GLU A 1 167 ? 23.475  -32.584 0.306   1.00 43.74 ? 169 GLU A CD  1 
ATOM   1326 O OE1 . GLU A 1 167 ? 22.780  -33.049 1.246   1.00 42.39 ? 169 GLU A OE1 1 
ATOM   1327 O OE2 . GLU A 1 167 ? 24.723  -32.711 0.256   1.00 42.91 ? 169 GLU A OE2 1 
ATOM   1328 N N   . CYS A 1 168 ? 25.702  -29.696 0.342   1.00 34.55 ? 170 CYS A N   1 
ATOM   1329 C CA  . CYS A 1 168 ? 27.011  -29.729 -0.321  1.00 36.94 ? 170 CYS A CA  1 
ATOM   1330 C C   . CYS A 1 168 ? 27.099  -30.398 -1.654  1.00 37.46 ? 170 CYS A C   1 
ATOM   1331 O O   . CYS A 1 168 ? 27.751  -29.883 -2.571  1.00 38.04 ? 170 CYS A O   1 
ATOM   1332 C CB  . CYS A 1 168 ? 27.995  -30.410 0.635   1.00 41.69 ? 170 CYS A CB  1 
ATOM   1333 S SG  . CYS A 1 168 ? 28.780  -29.212 1.669   1.00 51.59 ? 170 CYS A SG  1 
ATOM   1334 N N   . GLU A 1 169 ? 26.479  -31.571 -1.765  1.00 35.21 ? 171 GLU A N   1 
ATOM   1335 C CA  . GLU A 1 169 ? 26.641  -32.427 -2.937  1.00 33.99 ? 171 GLU A CA  1 
ATOM   1336 C C   . GLU A 1 169 ? 25.792  -32.004 -4.106  1.00 34.47 ? 171 GLU A C   1 
ATOM   1337 O O   . GLU A 1 169 ? 25.862  -32.612 -5.169  1.00 36.85 ? 171 GLU A O   1 
ATOM   1338 C CB  . GLU A 1 169 ? 26.387  -33.899 -2.581  1.00 38.52 ? 171 GLU A CB  1 
ATOM   1339 C CG  . GLU A 1 169 ? 27.318  -34.381 -1.488  1.00 40.79 ? 171 GLU A CG  1 
ATOM   1340 C CD  . GLU A 1 169 ? 28.808  -34.105 -1.699  1.00 44.09 ? 171 GLU A CD  1 
ATOM   1341 O OE1 . GLU A 1 169 ? 29.251  -34.203 -2.871  1.00 42.39 ? 171 GLU A OE1 1 
ATOM   1342 O OE2 . GLU A 1 169 ? 29.509  -33.791 -0.704  1.00 45.74 ? 171 GLU A OE2 1 
ATOM   1343 N N   . ASN A 1 170 ? 24.976  -30.924 -3.947  1.00 32.39 ? 172 ASN A N   1 
ATOM   1344 C CA  . ASN A 1 170 ? 24.201  -30.435 -5.075  1.00 31.08 ? 172 ASN A CA  1 
ATOM   1345 C C   . ASN A 1 170 ? 25.062  -29.374 -5.772  1.00 32.04 ? 172 ASN A C   1 
ATOM   1346 O O   . ASN A 1 170 ? 24.805  -28.166 -5.620  1.00 30.61 ? 172 ASN A O   1 
ATOM   1347 C CB  . ASN A 1 170 ? 22.881  -29.849 -4.616  1.00 32.35 ? 172 ASN A CB  1 
ATOM   1348 C CG  . ASN A 1 170 ? 21.826  -30.875 -4.320  1.00 36.85 ? 172 ASN A CG  1 
ATOM   1349 O OD1 . ASN A 1 170 ? 21.973  -32.080 -4.619  1.00 35.64 ? 172 ASN A OD1 1 
ATOM   1350 N ND2 . ASN A 1 170 ? 20.753  -30.405 -3.755  1.00 35.19 ? 172 ASN A ND2 1 
ATOM   1351 N N   . ARG A 1 171 ? 26.048  -29.801 -6.487  1.00 31.08 ? 173 ARG A N   1 
ATOM   1352 C CA  . ARG A 1 171 ? 27.115  -28.909 -6.990  1.00 33.63 ? 173 ARG A CA  1 
ATOM   1353 C C   . ARG A 1 171 ? 26.563  -27.827 -7.909  1.00 35.79 ? 173 ARG A C   1 
ATOM   1354 O O   . ARG A 1 171 ? 26.985  -26.646 -7.851  1.00 37.65 ? 173 ARG A O   1 
ATOM   1355 C CB  . ARG A 1 171 ? 28.110  -29.808 -7.761  1.00 40.38 ? 173 ARG A CB  1 
ATOM   1356 C CG  . ARG A 1 171 ? 29.334  -29.200 -8.373  1.00 50.08 ? 173 ARG A CG  1 
ATOM   1357 C CD  . ARG A 1 171 ? 30.228  -30.336 -8.917  1.00 59.11 ? 173 ARG A CD  1 
ATOM   1358 N NE  . ARG A 1 171 ? 29.648  -30.997 -10.095 1.00 64.68 ? 173 ARG A NE  1 
ATOM   1359 C CZ  . ARG A 1 171 ? 30.114  -32.122 -10.655 1.00 68.55 ? 173 ARG A CZ  1 
ATOM   1360 N NH1 . ARG A 1 171 ? 31.172  -32.744 -10.141 1.00 68.88 ? 173 ARG A NH1 1 
ATOM   1361 N NH2 . ARG A 1 171 ? 29.522  -32.632 -11.730 1.00 67.67 ? 173 ARG A NH2 1 
ATOM   1362 N N   . GLU A 1 172 ? 25.615  -28.214 -8.780  1.00 35.84 ? 174 GLU A N   1 
ATOM   1363 C CA  . GLU A 1 172 ? 25.073  -27.283 -9.728  1.00 37.60 ? 174 GLU A CA  1 
ATOM   1364 C C   . GLU A 1 172 ? 24.253  -26.234 -9.017  1.00 34.07 ? 174 GLU A C   1 
ATOM   1365 O O   . GLU A 1 172 ? 24.355  -25.070 -9.380  1.00 35.26 ? 174 GLU A O   1 
ATOM   1366 C CB  . GLU A 1 172 ? 24.232  -27.993 -10.788 1.00 43.67 ? 174 GLU A CB  1 
ATOM   1367 C CG  . GLU A 1 172 ? 25.132  -28.864 -11.681 1.00 55.21 ? 174 GLU A CG  1 
ATOM   1368 C CD  . GLU A 1 172 ? 26.361  -28.209 -12.319 1.00 68.44 ? 174 GLU A CD  1 
ATOM   1369 O OE1 . GLU A 1 172 ? 26.250  -27.078 -12.862 1.00 68.34 ? 174 GLU A OE1 1 
ATOM   1370 O OE2 . GLU A 1 172 ? 27.447  -28.839 -12.261 1.00 72.34 ? 174 GLU A OE2 1 
ATOM   1371 N N   . ALA A 1 173 ? 23.467  -26.619 -8.010  1.00 31.60 ? 175 ALA A N   1 
ATOM   1372 C CA  . ALA A 1 173 ? 22.691  -25.619 -7.243  1.00 31.59 ? 175 ALA A CA  1 
ATOM   1373 C C   . ALA A 1 173 ? 23.639  -24.645 -6.536  1.00 31.28 ? 175 ALA A C   1 
ATOM   1374 O O   . ALA A 1 173 ? 23.424  -23.444 -6.596  1.00 32.46 ? 175 ALA A O   1 
ATOM   1375 C CB  . ALA A 1 173 ? 21.813  -26.308 -6.233  1.00 31.66 ? 175 ALA A CB  1 
ATOM   1376 N N   . VAL A 1 174 ? 24.690  -25.152 -5.879  1.00 29.25 ? 176 VAL A N   1 
ATOM   1377 C CA  . VAL A 1 174 ? 25.594  -24.328 -5.053  1.00 30.49 ? 176 VAL A CA  1 
ATOM   1378 C C   . VAL A 1 174 ? 26.303  -23.347 -5.996  1.00 30.44 ? 176 VAL A C   1 
ATOM   1379 O O   . VAL A 1 174 ? 26.363  -22.150 -5.706  1.00 28.28 ? 176 VAL A O   1 
ATOM   1380 C CB  . VAL A 1 174 ? 26.602  -25.252 -4.298  1.00 31.69 ? 176 VAL A CB  1 
ATOM   1381 C CG1 . VAL A 1 174 ? 27.773  -24.447 -3.715  1.00 33.85 ? 176 VAL A CG1 1 
ATOM   1382 C CG2 . VAL A 1 174 ? 25.896  -26.095 -3.195  1.00 31.20 ? 176 VAL A CG2 1 
ATOM   1383 N N   . THR A 1 175 ? 26.833  -23.849 -7.139  1.00 29.65 ? 177 THR A N   1 
ATOM   1384 C CA  . THR A 1 175 ? 27.591  -22.961 -8.029  1.00 32.42 ? 177 THR A CA  1 
ATOM   1385 C C   . THR A 1 175 ? 26.683  -21.904 -8.666  1.00 30.82 ? 177 THR A C   1 
ATOM   1386 O O   . THR A 1 175 ? 27.125  -20.766 -8.800  1.00 30.35 ? 177 THR A O   1 
ATOM   1387 C CB  . THR A 1 175 ? 28.456  -23.759 -9.047  1.00 38.03 ? 177 THR A CB  1 
ATOM   1388 O OG1 . THR A 1 175 ? 27.642  -24.574 -9.815  1.00 42.43 ? 177 THR A OG1 1 
ATOM   1389 C CG2 . THR A 1 175 ? 29.466  -24.600 -8.393  1.00 39.12 ? 177 THR A CG2 1 
ATOM   1390 N N   . HIS A 1 176 ? 25.447  -22.239 -9.057  1.00 30.45 ? 178 HIS A N   1 
ATOM   1391 C CA  . HIS A 1 176 ? 24.527  -21.263 -9.619  1.00 31.69 ? 178 HIS A CA  1 
ATOM   1392 C C   . HIS A 1 176 ? 24.175  -20.168 -8.612  1.00 31.25 ? 178 HIS A C   1 
ATOM   1393 O O   . HIS A 1 176 ? 24.153  -18.984 -8.937  1.00 30.56 ? 178 HIS A O   1 
ATOM   1394 C CB  . HIS A 1 176 ? 23.244  -21.957 -10.068 1.00 34.61 ? 178 HIS A CB  1 
ATOM   1395 C CG  . HIS A 1 176 ? 22.228  -21.069 -10.703 1.00 39.94 ? 178 HIS A CG  1 
ATOM   1396 N ND1 . HIS A 1 176 ? 21.252  -20.433 -9.958  1.00 43.01 ? 178 HIS A ND1 1 
ATOM   1397 C CD2 . HIS A 1 176 ? 22.035  -20.763 -12.004 1.00 42.03 ? 178 HIS A CD2 1 
ATOM   1398 C CE1 . HIS A 1 176 ? 20.513  -19.754 -10.826 1.00 42.98 ? 178 HIS A CE1 1 
ATOM   1399 N NE2 . HIS A 1 176 ? 20.964  -19.903 -12.056 1.00 42.66 ? 178 HIS A NE2 1 
ATOM   1400 N N   . ILE A 1 177 ? 23.890  -20.576 -7.367  1.00 29.14 ? 179 ILE A N   1 
ATOM   1401 C CA  . ILE A 1 177 ? 23.594  -19.583 -6.311  1.00 28.08 ? 179 ILE A CA  1 
ATOM   1402 C C   . ILE A 1 177 ? 24.796  -18.645 -6.120  1.00 27.31 ? 179 ILE A C   1 
ATOM   1403 O O   . ILE A 1 177 ? 24.579  -17.455 -5.982  1.00 28.58 ? 179 ILE A O   1 
ATOM   1404 C CB  . ILE A 1 177 ? 23.242  -20.343 -5.012  1.00 27.50 ? 179 ILE A CB  1 
ATOM   1405 C CG1 . ILE A 1 177 ? 21.895  -21.028 -5.142  1.00 28.33 ? 179 ILE A CG1 1 
ATOM   1406 C CG2 . ILE A 1 177 ? 23.319  -19.367 -3.777  1.00 25.46 ? 179 ILE A CG2 1 
ATOM   1407 C CD1 . ILE A 1 177 ? 21.608  -22.091 -3.978  1.00 28.78 ? 179 ILE A CD1 1 
ATOM   1408 N N   . GLY A 1 178 ? 26.026  -19.166 -6.108  1.00 28.27 ? 180 GLY A N   1 
ATOM   1409 C CA  . GLY A 1 178 ? 27.226  -18.348 -5.925  1.00 28.87 ? 180 GLY A CA  1 
ATOM   1410 C C   . GLY A 1 178 ? 27.363  -17.345 -7.016  1.00 30.42 ? 180 GLY A C   1 
ATOM   1411 O O   . GLY A 1 178 ? 27.614  -16.168 -6.735  1.00 30.42 ? 180 GLY A O   1 
ATOM   1412 N N   . ARG A 1 179 ? 27.193  -17.790 -8.268  1.00 31.52 ? 181 ARG A N   1 
ATOM   1413 C CA  . ARG A 1 179 ? 27.336  -16.879 -9.424  1.00 33.73 ? 181 ARG A CA  1 
ATOM   1414 C C   . ARG A 1 179 ? 26.268  -15.787 -9.479  1.00 32.71 ? 181 ARG A C   1 
ATOM   1415 O O   . ARG A 1 179 ? 26.577  -14.602 -9.726  1.00 32.74 ? 181 ARG A O   1 
ATOM   1416 C CB  . ARG A 1 179 ? 27.394  -17.686 -10.733 1.00 37.50 ? 181 ARG A CB  1 
ATOM   1417 C CG  . ARG A 1 179 ? 28.688  -18.496 -10.755 1.00 45.56 ? 181 ARG A CG  1 
ATOM   1418 C CD  . ARG A 1 179 ? 29.362  -18.658 -12.074 1.00 53.41 ? 181 ARG A CD  1 
ATOM   1419 N NE  . ARG A 1 179 ? 30.772  -19.095 -11.916 1.00 61.03 ? 181 ARG A NE  1 
ATOM   1420 C CZ  . ARG A 1 179 ? 31.854  -18.302 -11.951 1.00 69.15 ? 181 ARG A CZ  1 
ATOM   1421 N NH1 . ARG A 1 179 ? 33.067  -18.816 -11.781 1.00 70.92 ? 181 ARG A NH1 1 
ATOM   1422 N NH2 . ARG A 1 179 ? 31.728  -16.986 -12.152 1.00 71.98 ? 181 ARG A NH2 1 
ATOM   1423 N N   . VAL A 1 180 ? 25.031  -16.156 -9.222  1.00 31.22 ? 182 VAL A N   1 
ATOM   1424 C CA  . VAL A 1 180 ? 23.963  -15.182 -9.154  1.00 31.34 ? 182 VAL A CA  1 
ATOM   1425 C C   . VAL A 1 180 ? 24.140  -14.215 -7.967  1.00 31.62 ? 182 VAL A C   1 
ATOM   1426 O O   . VAL A 1 180 ? 23.925  -12.998 -8.132  1.00 31.91 ? 182 VAL A O   1 
ATOM   1427 C CB  . VAL A 1 180 ? 22.596  -15.845 -9.162  1.00 33.67 ? 182 VAL A CB  1 
ATOM   1428 C CG1 . VAL A 1 180 ? 21.479  -14.808 -8.960  1.00 35.26 ? 182 VAL A CG1 1 
ATOM   1429 C CG2 . VAL A 1 180 ? 22.383  -16.643 -10.468 1.00 34.81 ? 182 VAL A CG2 1 
ATOM   1430 N N   . TYR A 1 181 ? 24.524  -14.727 -6.773  1.00 29.37 ? 183 TYR A N   1 
ATOM   1431 C CA  . TYR A 1 181 ? 24.698  -13.874 -5.602  1.00 28.01 ? 183 TYR A CA  1 
ATOM   1432 C C   . TYR A 1 181 ? 25.786  -12.821 -5.917  1.00 29.85 ? 183 TYR A C   1 
ATOM   1433 O O   . TYR A 1 181 ? 25.623  -11.630 -5.625  1.00 29.33 ? 183 TYR A O   1 
ATOM   1434 C CB  . TYR A 1 181 ? 25.125  -14.726 -4.401  1.00 27.03 ? 183 TYR A CB  1 
ATOM   1435 C CG  . TYR A 1 181 ? 25.251  -14.033 -3.075  1.00 26.39 ? 183 TYR A CG  1 
ATOM   1436 C CD1 . TYR A 1 181 ? 24.424  -12.964 -2.740  1.00 28.72 ? 183 TYR A CD1 1 
ATOM   1437 C CD2 . TYR A 1 181 ? 26.148  -14.483 -2.125  1.00 28.87 ? 183 TYR A CD2 1 
ATOM   1438 C CE1 . TYR A 1 181 ? 24.509  -12.354 -1.511  1.00 28.77 ? 183 TYR A CE1 1 
ATOM   1439 C CE2 . TYR A 1 181 ? 26.229  -13.888 -0.879  1.00 29.53 ? 183 TYR A CE2 1 
ATOM   1440 C CZ  . TYR A 1 181 ? 25.391  -12.828 -0.580  1.00 29.21 ? 183 TYR A CZ  1 
ATOM   1441 O OH  . TYR A 1 181 ? 25.488  -12.281 0.644   1.00 29.45 ? 183 TYR A OH  1 
ATOM   1442 N N   . LYS A 1 182 ? 26.906  -13.278 -6.530  1.00 30.32 ? 184 LYS A N   1 
ATOM   1443 C CA  . LYS A 1 182 ? 28.029  -12.342 -6.811  1.00 31.51 ? 184 LYS A CA  1 
ATOM   1444 C C   . LYS A 1 182 ? 27.578  -11.249 -7.780  1.00 34.41 ? 184 LYS A C   1 
ATOM   1445 O O   . LYS A 1 182 ? 27.920  -10.076 -7.594  1.00 35.33 ? 184 LYS A O   1 
ATOM   1446 C CB  . LYS A 1 182 ? 29.242  -13.126 -7.304  1.00 32.63 ? 184 LYS A CB  1 
ATOM   1447 C CG  . LYS A 1 182 ? 30.418  -12.217 -7.752  1.00 36.10 ? 184 LYS A CG  1 
ATOM   1448 C CD  . LYS A 1 182 ? 31.655  -12.977 -8.015  1.00 38.10 ? 184 LYS A CD  1 
ATOM   1449 C CE  . LYS A 1 182 ? 32.677  -12.089 -8.719  1.00 44.08 ? 184 LYS A CE  1 
ATOM   1450 N NZ  . LYS A 1 182 ? 33.984  -12.751 -8.757  1.00 44.38 ? 184 LYS A NZ  1 
ATOM   1451 N N   . GLU A 1 183 ? 26.807  -11.599 -8.810  1.00 34.41 ? 185 GLU A N   1 
ATOM   1452 C CA  . GLU A 1 183 ? 26.243  -10.626 -9.737  1.00 36.68 ? 185 GLU A CA  1 
ATOM   1453 C C   . GLU A 1 183 ? 25.334  -9.628  -9.015  1.00 35.84 ? 185 GLU A C   1 
ATOM   1454 O O   . GLU A 1 183 ? 25.422  -8.431  -9.254  1.00 34.76 ? 185 GLU A O   1 
ATOM   1455 C CB  . GLU A 1 183 ? 25.425  -11.349 -10.822 1.00 42.32 ? 185 GLU A CB  1 
ATOM   1456 C CG  . GLU A 1 183 ? 24.801  -10.468 -11.895 1.00 54.75 ? 185 GLU A CG  1 
ATOM   1457 C CD  . GLU A 1 183 ? 23.980  -11.240 -12.916 1.00 70.29 ? 185 GLU A CD  1 
ATOM   1458 O OE1 . GLU A 1 183 ? 23.670  -12.436 -12.671 1.00 74.11 ? 185 GLU A OE1 1 
ATOM   1459 O OE2 . GLU A 1 183 ? 23.646  -10.641 -13.967 1.00 74.65 ? 185 GLU A OE2 1 
ATOM   1460 N N   . ARG A 1 184 ? 24.469  -10.121 -8.145  1.00 32.84 ? 186 ARG A N   1 
ATOM   1461 C CA  . ARG A 1 184 ? 23.511  -9.241  -7.452  1.00 33.18 ? 186 ARG A CA  1 
ATOM   1462 C C   . ARG A 1 184 ? 24.198  -8.322  -6.453  1.00 34.57 ? 186 ARG A C   1 
ATOM   1463 O O   . ARG A 1 184 ? 23.700  -7.221  -6.213  1.00 34.41 ? 186 ARG A O   1 
ATOM   1464 C CB  . ARG A 1 184 ? 22.398  -10.037 -6.800  1.00 34.59 ? 186 ARG A CB  1 
ATOM   1465 C CG  . ARG A 1 184 ? 21.430  -10.632 -7.826  1.00 37.56 ? 186 ARG A CG  1 
ATOM   1466 C CD  . ARG A 1 184 ? 20.452  -9.609  -8.364  1.00 37.30 ? 186 ARG A CD  1 
ATOM   1467 N NE  . ARG A 1 184 ? 19.489  -9.198  -7.347  1.00 39.49 ? 186 ARG A NE  1 
ATOM   1468 C CZ  . ARG A 1 184 ? 18.269  -9.695  -7.160  1.00 38.20 ? 186 ARG A CZ  1 
ATOM   1469 N NH1 . ARG A 1 184 ? 17.793  -10.630 -7.965  1.00 41.40 ? 186 ARG A NH1 1 
ATOM   1470 N NH2 . ARG A 1 184 ? 17.503  -9.227  -6.192  1.00 38.18 ? 186 ARG A NH2 1 
ATOM   1471 N N   . LEU A 1 185 ? 25.339  -8.728  -5.897  1.00 35.88 ? 187 LEU A N   1 
ATOM   1472 C CA  . LEU A 1 185 ? 26.137  -7.823  -5.043  1.00 37.24 ? 187 LEU A CA  1 
ATOM   1473 C C   . LEU A 1 185 ? 26.874  -6.747  -5.842  1.00 42.74 ? 187 LEU A C   1 
ATOM   1474 O O   . LEU A 1 185 ? 27.206  -5.728  -5.263  1.00 44.85 ? 187 LEU A O   1 
ATOM   1475 C CB  . LEU A 1 185 ? 27.178  -8.637  -4.219  1.00 34.04 ? 187 LEU A CB  1 
ATOM   1476 C CG  . LEU A 1 185 ? 26.608  -9.555  -3.155  1.00 32.69 ? 187 LEU A CG  1 
ATOM   1477 C CD1 . LEU A 1 185 ? 27.672  -10.405 -2.501  1.00 34.25 ? 187 LEU A CD1 1 
ATOM   1478 C CD2 . LEU A 1 185 ? 25.757  -8.755  -2.109  1.00 34.69 ? 187 LEU A CD2 1 
ATOM   1479 N N   . GLY A 1 186 ? 27.136  -6.989  -7.113  1.00 44.08 ? 188 GLY A N   1 
ATOM   1480 C CA  . GLY A 1 186 ? 27.848  -6.043  -7.958  1.00 46.73 ? 188 GLY A CA  1 
ATOM   1481 C C   . GLY A 1 186 ? 29.358  -6.152  -7.823  1.00 49.80 ? 188 GLY A C   1 
ATOM   1482 O O   . GLY A 1 186 ? 30.063  -5.195  -8.162  1.00 50.76 ? 188 GLY A O   1 
ATOM   1483 N N   . LEU A 1 187 ? 29.884  -7.304  -7.338  1.00 49.46 ? 189 LEU A N   1 
ATOM   1484 C CA  . LEU A 1 187 ? 31.319  -7.402  -7.095  1.00 50.05 ? 189 LEU A CA  1 
ATOM   1485 C C   . LEU A 1 187 ? 32.049  -7.463  -8.439  1.00 53.54 ? 189 LEU A C   1 
ATOM   1486 O O   . LEU A 1 187 ? 31.570  -8.130  -9.363  1.00 53.79 ? 189 LEU A O   1 
ATOM   1487 C CB  . LEU A 1 187 ? 31.690  -8.619  -6.232  1.00 47.06 ? 189 LEU A CB  1 
ATOM   1488 C CG  . LEU A 1 187 ? 31.063  -8.690  -4.847  1.00 45.82 ? 189 LEU A CG  1 
ATOM   1489 C CD1 . LEU A 1 187 ? 31.404  -9.998  -4.137  1.00 44.67 ? 189 LEU A CD1 1 
ATOM   1490 C CD2 . LEU A 1 187 ? 31.505  -7.559  -3.999  1.00 48.34 ? 189 LEU A CD2 1 
ATOM   1491 N N   . PRO A 1 188 ? 33.207  -6.790  -8.579  1.00 56.00 ? 190 PRO A N   1 
ATOM   1492 C CA  . PRO A 1 188 ? 34.025  -7.010  -9.784  1.00 58.00 ? 190 PRO A CA  1 
ATOM   1493 C C   . PRO A 1 188 ? 34.470  -8.470  -9.926  1.00 61.04 ? 190 PRO A C   1 
ATOM   1494 O O   . PRO A 1 188 ? 34.597  -9.157  -8.912  1.00 61.41 ? 190 PRO A O   1 
ATOM   1495 C CB  . PRO A 1 188 ? 35.245  -6.112  -9.563  1.00 58.96 ? 190 PRO A CB  1 
ATOM   1496 C CG  . PRO A 1 188 ? 34.887  -5.211  -8.454  1.00 59.10 ? 190 PRO A CG  1 
ATOM   1497 C CD  . PRO A 1 188 ? 33.831  -5.821  -7.655  1.00 56.73 ? 190 PRO A CD  1 
ATOM   1498 N N   . PRO A 1 189 ? 34.706  -8.968  -11.155 1.00 62.79 ? 191 PRO A N   1 
ATOM   1499 C CA  . PRO A 1 189 ? 35.226  -10.340 -11.317 1.00 63.80 ? 191 PRO A CA  1 
ATOM   1500 C C   . PRO A 1 189 ? 36.415  -10.716 -10.441 1.00 64.00 ? 191 PRO A C   1 
ATOM   1501 O O   . PRO A 1 189 ? 36.573  -11.895 -10.096 1.00 65.17 ? 191 PRO A O   1 
ATOM   1502 C CB  . PRO A 1 189 ? 35.624  -10.407 -12.794 1.00 65.42 ? 191 PRO A CB  1 
ATOM   1503 C CG  . PRO A 1 189 ? 34.883  -9.307  -13.465 1.00 66.08 ? 191 PRO A CG  1 
ATOM   1504 C CD  . PRO A 1 189 ? 34.477  -8.300  -12.449 1.00 63.56 ? 191 PRO A CD  1 
ATOM   1505 N N   . LYS A 1 190 ? 37.235  -9.721  -10.058 1.00 62.25 ? 192 LYS A N   1 
ATOM   1506 C CA  . LYS A 1 190 ? 38.489  -9.971  -9.351  1.00 60.87 ? 192 LYS A CA  1 
ATOM   1507 C C   . LYS A 1 190 ? 38.225  -10.285 -7.874  1.00 57.26 ? 192 LYS A C   1 
ATOM   1508 O O   . LYS A 1 190 ? 38.991  -11.029 -7.284  1.00 57.12 ? 192 LYS A O   1 
ATOM   1509 C CB  . LYS A 1 190 ? 39.448  -8.754  -9.459  1.00 64.39 ? 192 LYS A CB  1 
ATOM   1510 C CG  . LYS A 1 190 ? 39.764  -8.286  -10.895 1.00 71.74 ? 192 LYS A CG  1 
ATOM   1511 C CD  . LYS A 1 190 ? 38.649  -7.387  -11.507 1.00 78.28 ? 192 LYS A CD  1 
ATOM   1512 C CE  . LYS A 1 190 ? 39.176  -6.426  -12.569 1.00 83.93 ? 192 LYS A CE  1 
ATOM   1513 N NZ  . LYS A 1 190 ? 38.111  -5.476  -13.027 1.00 85.85 ? 192 LYS A NZ  1 
ATOM   1514 N N   . ILE A 1 191 ? 37.156  -9.716  -7.276  1.00 54.89 ? 193 ILE A N   1 
ATOM   1515 C CA  . ILE A 1 191 ? 36.837  -10.003 -5.880  1.00 52.80 ? 193 ILE A CA  1 
ATOM   1516 C C   . ILE A 1 191 ? 35.970  -11.240 -5.864  1.00 50.27 ? 193 ILE A C   1 
ATOM   1517 O O   . ILE A 1 191 ? 34.971  -11.296 -6.559  1.00 51.12 ? 193 ILE A O   1 
ATOM   1518 C CB  . ILE A 1 191 ? 36.223  -8.798  -5.147  1.00 53.33 ? 193 ILE A CB  1 
ATOM   1519 C CG1 . ILE A 1 191 ? 37.353  -7.716  -4.893  1.00 55.77 ? 193 ILE A CG1 1 
ATOM   1520 C CG2 . ILE A 1 191 ? 35.642  -9.238  -3.787  1.00 53.00 ? 193 ILE A CG2 1 
ATOM   1521 C CD1 . ILE A 1 191 ? 36.943  -6.321  -5.201  1.00 58.66 ? 193 ILE A CD1 1 
ATOM   1522 N N   . VAL A 1 192 ? 36.374  -12.227 -5.102  1.00 47.97 ? 194 VAL A N   1 
ATOM   1523 C CA  . VAL A 1 192 ? 35.710  -13.529 -5.094  1.00 47.59 ? 194 VAL A CA  1 
ATOM   1524 C C   . VAL A 1 192 ? 34.957  -13.801 -3.774  1.00 46.93 ? 194 VAL A C   1 
ATOM   1525 O O   . VAL A 1 192 ? 35.328  -13.321 -2.695  1.00 47.15 ? 194 VAL A O   1 
ATOM   1526 C CB  . VAL A 1 192 ? 36.684  -14.661 -5.388  1.00 48.52 ? 194 VAL A CB  1 
ATOM   1527 C CG1 . VAL A 1 192 ? 37.503  -14.392 -6.651  1.00 50.00 ? 194 VAL A CG1 1 
ATOM   1528 C CG2 . VAL A 1 192 ? 37.601  -14.958 -4.185  1.00 48.82 ? 194 VAL A CG2 1 
ATOM   1529 N N   . ILE A 1 193 ? 33.902  -14.589 -3.894  1.00 44.26 ? 195 ILE A N   1 
ATOM   1530 C CA  . ILE A 1 193 ? 33.210  -15.171 -2.761  1.00 40.90 ? 195 ILE A CA  1 
ATOM   1531 C C   . ILE A 1 193 ? 33.645  -16.662 -2.709  1.00 37.92 ? 195 ILE A C   1 
ATOM   1532 O O   . ILE A 1 193 ? 33.917  -17.275 -3.751  1.00 37.91 ? 195 ILE A O   1 
ATOM   1533 C CB  . ILE A 1 193 ? 31.691  -14.897 -2.908  1.00 41.51 ? 195 ILE A CB  1 
ATOM   1534 C CG1 . ILE A 1 193 ? 31.096  -15.549 -4.138  1.00 41.68 ? 195 ILE A CG1 1 
ATOM   1535 C CG2 . ILE A 1 193 ? 31.410  -13.366 -2.918  1.00 42.93 ? 195 ILE A CG2 1 
ATOM   1536 C CD1 . ILE A 1 193 ? 29.505  -15.482 -4.107  1.00 43.07 ? 195 ILE A CD1 1 
ATOM   1537 N N   . GLY A 1 194 ? 33.748  -17.244 -1.511  1.00 34.48 ? 196 GLY A N   1 
ATOM   1538 C CA  . GLY A 1 194 ? 34.069  -18.639 -1.371  1.00 32.77 ? 196 GLY A CA  1 
ATOM   1539 C C   . GLY A 1 194 ? 32.955  -19.440 -0.721  1.00 31.56 ? 196 GLY A C   1 
ATOM   1540 O O   . GLY A 1 194 ? 32.238  -18.909 0.142   1.00 30.64 ? 196 GLY A O   1 
ATOM   1541 N N   . TYR A 1 195 ? 32.787  -20.703 -1.116  1.00 29.96 ? 197 TYR A N   1 
ATOM   1542 C CA  . TYR A 1 195 ? 31.858  -21.620 -0.494  1.00 30.47 ? 197 TYR A CA  1 
ATOM   1543 C C   . TYR A 1 195 ? 32.601  -22.597 0.416   1.00 33.36 ? 197 TYR A C   1 
ATOM   1544 O O   . TYR A 1 195 ? 33.605  -23.231 -0.030  1.00 35.25 ? 197 TYR A O   1 
ATOM   1545 C CB  . TYR A 1 195 ? 31.086  -22.475 -1.531  1.00 31.39 ? 197 TYR A CB  1 
ATOM   1546 C CG  . TYR A 1 195 ? 29.917  -23.256 -0.955  1.00 34.40 ? 197 TYR A CG  1 
ATOM   1547 C CD1 . TYR A 1 195 ? 28.680  -22.672 -0.819  1.00 37.21 ? 197 TYR A CD1 1 
ATOM   1548 C CD2 . TYR A 1 195 ? 30.027  -24.624 -0.656  1.00 38.76 ? 197 TYR A CD2 1 
ATOM   1549 C CE1 . TYR A 1 195 ? 27.602  -23.360 -0.278  1.00 39.18 ? 197 TYR A CE1 1 
ATOM   1550 C CE2 . TYR A 1 195 ? 28.937  -25.342 -0.121  1.00 38.37 ? 197 TYR A CE2 1 
ATOM   1551 C CZ  . TYR A 1 195 ? 27.724  -24.712 0.046   1.00 41.25 ? 197 TYR A CZ  1 
ATOM   1552 O OH  . TYR A 1 195 ? 26.596  -25.403 0.529   1.00 43.14 ? 197 TYR A OH  1 
ATOM   1553 N N   . GLN A 1 196 ? 32.124  -22.738 1.640   1.00 29.97 ? 198 GLN A N   1 
ATOM   1554 C CA  . GLN A 1 196 ? 32.700  -23.669 2.593   1.00 34.11 ? 198 GLN A CA  1 
ATOM   1555 C C   . GLN A 1 196 ? 31.611  -24.502 3.156   1.00 31.68 ? 198 GLN A C   1 
ATOM   1556 O O   . GLN A 1 196 ? 30.540  -23.982 3.532   1.00 31.21 ? 198 GLN A O   1 
ATOM   1557 C CB  . GLN A 1 196 ? 33.381  -22.921 3.788   1.00 39.57 ? 198 GLN A CB  1 
ATOM   1558 C CG  . GLN A 1 196 ? 34.077  -21.619 3.483   1.00 49.08 ? 198 GLN A CG  1 
ATOM   1559 C CD  . GLN A 1 196 ? 33.195  -20.473 3.988   1.00 57.05 ? 198 GLN A CD  1 
ATOM   1560 O OE1 . GLN A 1 196 ? 33.308  -19.998 5.140   1.00 58.57 ? 198 GLN A OE1 1 
ATOM   1561 N NE2 . GLN A 1 196 ? 32.283  -20.025 3.132   1.00 55.17 ? 198 GLN A NE2 1 
ATOM   1562 N N   . SER A 1 197 ? 31.824  -25.801 3.217   1.00 29.59 ? 199 SER A N   1 
ATOM   1563 C CA  . SER A 1 197 ? 30.905  -26.687 3.940   1.00 29.59 ? 199 SER A CA  1 
ATOM   1564 C C   . SER A 1 197 ? 30.850  -26.312 5.450   1.00 29.57 ? 199 SER A C   1 
ATOM   1565 O O   . SER A 1 197 ? 31.887  -25.929 6.003   1.00 32.53 ? 199 SER A O   1 
ATOM   1566 C CB  . SER A 1 197 ? 31.278  -28.175 3.717   1.00 32.47 ? 199 SER A CB  1 
ATOM   1567 O OG  . SER A 1 197 ? 31.899  -28.713 4.851   1.00 38.30 ? 199 SER A OG  1 
ATOM   1568 N N   . HIS A 1 198 ? 29.716  -26.395 6.099   1.00 28.44 ? 200 HIS A N   1 
ATOM   1569 C CA  . HIS A 1 198 ? 29.649  -26.109 7.546   1.00 31.25 ? 200 HIS A CA  1 
ATOM   1570 C C   . HIS A 1 198 ? 30.508  -27.104 8.368   1.00 36.13 ? 200 HIS A C   1 
ATOM   1571 O O   . HIS A 1 198 ? 31.108  -26.714 9.375   1.00 35.42 ? 200 HIS A O   1 
ATOM   1572 C CB  . HIS A 1 198 ? 28.221  -26.165 8.062   1.00 30.92 ? 200 HIS A CB  1 
ATOM   1573 C CG  . HIS A 1 198 ? 27.325  -25.109 7.509   1.00 27.55 ? 200 HIS A CG  1 
ATOM   1574 N ND1 . HIS A 1 198 ? 27.734  -23.782 7.382   1.00 28.36 ? 200 HIS A ND1 1 
ATOM   1575 C CD2 . HIS A 1 198 ? 26.062  -25.205 7.071   1.00 29.33 ? 200 HIS A CD2 1 
ATOM   1576 C CE1 . HIS A 1 198 ? 26.710  -23.131 6.893   1.00 27.93 ? 200 HIS A CE1 1 
ATOM   1577 N NE2 . HIS A 1 198 ? 25.684  -23.946 6.674   1.00 29.66 ? 200 HIS A NE2 1 
ATOM   1578 N N   . ALA A 1 199 ? 30.566  -28.376 7.932   1.00 39.22 ? 201 ALA A N   1 
ATOM   1579 C CA  . ALA A 1 199 ? 31.384  -29.409 8.605   1.00 42.99 ? 201 ALA A CA  1 
ATOM   1580 C C   . ALA A 1 199 ? 32.843  -28.981 8.570   1.00 46.49 ? 201 ALA A C   1 
ATOM   1581 O O   . ALA A 1 199 ? 33.512  -29.100 9.590   1.00 49.57 ? 201 ALA A O   1 
ATOM   1582 C CB  . ALA A 1 199 ? 31.179  -30.771 7.962   1.00 42.91 ? 201 ALA A CB  1 
ATOM   1583 N N   . ASP A 1 200 ? 33.335  -28.441 7.459   1.00 46.76 ? 202 ASP A N   1 
ATOM   1584 C CA  . ASP A 1 200 ? 34.709  -27.905 7.392   1.00 48.64 ? 202 ASP A CA  1 
ATOM   1585 C C   . ASP A 1 200 ? 34.929  -26.620 8.222   1.00 49.28 ? 202 ASP A C   1 
ATOM   1586 O O   . ASP A 1 200 ? 35.954  -26.527 8.921   1.00 48.91 ? 202 ASP A O   1 
ATOM   1587 C CB  . ASP A 1 200 ? 35.148  -27.659 5.947   1.00 51.64 ? 202 ASP A CB  1 
ATOM   1588 C CG  . ASP A 1 200 ? 35.245  -28.923 5.093   1.00 61.03 ? 202 ASP A CG  1 
ATOM   1589 O OD1 . ASP A 1 200 ? 35.198  -30.027 5.656   1.00 63.96 ? 202 ASP A OD1 1 
ATOM   1590 O OD2 . ASP A 1 200 ? 35.366  -28.798 3.855   1.00 63.73 ? 202 ASP A OD2 1 
ATOM   1591 N N   . THR A 1 201 ? 34.003  -25.631 8.157   1.00 49.41 ? 203 THR A N   1 
ATOM   1592 C CA  . THR A 1 201 ? 34.112  -24.461 9.015   1.00 51.58 ? 203 THR A CA  1 
ATOM   1593 C C   . THR A 1 201 ? 34.173  -24.809 10.519  1.00 53.70 ? 203 THR A C   1 
ATOM   1594 O O   . THR A 1 201 ? 34.910  -24.157 11.255  1.00 54.22 ? 203 THR A O   1 
ATOM   1595 C CB  . THR A 1 201 ? 32.992  -23.459 8.732   1.00 53.58 ? 203 THR A CB  1 
ATOM   1596 O OG1 . THR A 1 201 ? 32.982  -23.153 7.334   1.00 54.18 ? 203 THR A OG1 1 
ATOM   1597 C CG2 . THR A 1 201 ? 33.164  -22.155 9.526   1.00 53.95 ? 203 THR A CG2 1 
ATOM   1598 N N   . ALA A 1 202 ? 33.407  -25.827 10.956  1.00 54.42 ? 204 ALA A N   1 
ATOM   1599 C CA  . ALA A 1 202 ? 33.301  -26.203 12.371  1.00 54.93 ? 204 ALA A CA  1 
ATOM   1600 C C   . ALA A 1 202 ? 34.633  -26.730 12.968  1.00 56.77 ? 204 ALA A C   1 
ATOM   1601 O O   . ALA A 1 202 ? 34.758  -26.785 14.192  1.00 56.13 ? 204 ALA A O   1 
ATOM   1602 C CB  . ALA A 1 202 ? 32.229  -27.266 12.533  1.00 54.17 ? 204 ALA A CB  1 
ATOM   1603 N N   . THR A 1 203 ? 35.596  -27.128 12.118  1.00 57.64 ? 205 THR A N   1 
ATOM   1604 C CA  . THR A 1 203 ? 36.862  -27.691 12.567  1.00 58.52 ? 205 THR A CA  1 
ATOM   1605 C C   . THR A 1 203 ? 37.929  -26.654 12.313  1.00 56.94 ? 205 THR A C   1 
ATOM   1606 O O   . THR A 1 203 ? 38.158  -26.274 11.155  1.00 56.80 ? 205 THR A O   1 
ATOM   1607 C CB  . THR A 1 203 ? 37.172  -29.023 11.838  1.00 62.86 ? 205 THR A CB  1 
ATOM   1608 O OG1 . THR A 1 203 ? 37.547  -28.774 10.475  1.00 65.90 ? 205 THR A OG1 1 
ATOM   1609 C CG2 . THR A 1 203 ? 36.022  -29.990 11.859  1.00 63.85 ? 205 THR A CG2 1 
ATOM   1610 N N   . LYS A 1 204 ? 38.593  -26.182 13.388  1.00 55.70 ? 206 LYS A N   1 
ATOM   1611 C CA  . LYS A 1 204 ? 39.655  -25.191 13.271  1.00 55.07 ? 206 LYS A CA  1 
ATOM   1612 C C   . LYS A 1 204 ? 40.966  -25.947 13.064  1.00 55.02 ? 206 LYS A C   1 
ATOM   1613 O O   . LYS A 1 204 ? 41.420  -26.711 13.943  1.00 53.50 ? 206 LYS A O   1 
ATOM   1614 C CB  . LYS A 1 204 ? 39.707  -24.295 14.526  1.00 57.58 ? 206 LYS A CB  1 
ATOM   1615 C CG  . LYS A 1 204 ? 38.396  -23.550 14.843  1.00 63.27 ? 206 LYS A CG  1 
ATOM   1616 C CD  . LYS A 1 204 ? 38.167  -22.371 13.923  1.00 69.76 ? 206 LYS A CD  1 
ATOM   1617 C CE  . LYS A 1 204 ? 37.029  -21.464 14.382  1.00 75.74 ? 206 LYS A CE  1 
ATOM   1618 N NZ  . LYS A 1 204 ? 37.410  -20.012 14.357  1.00 79.17 ? 206 LYS A NZ  1 
ATOM   1619 N N   . SER A 1 205 ? 41.592  -25.722 11.901  1.00 55.26 ? 207 SER A N   1 
ATOM   1620 C CA  . SER A 1 205 ? 42.722  -26.522 11.433  1.00 55.98 ? 207 SER A CA  1 
ATOM   1621 C C   . SER A 1 205 ? 43.941  -25.677 11.006  1.00 56.29 ? 207 SER A C   1 
ATOM   1622 O O   . SER A 1 205 ? 44.839  -26.208 10.364  1.00 56.92 ? 207 SER A O   1 
ATOM   1623 C CB  . SER A 1 205 ? 42.259  -27.419 10.281  1.00 58.30 ? 207 SER A CB  1 
ATOM   1624 O OG  . SER A 1 205 ? 41.646  -26.650 9.252   1.00 61.11 ? 207 SER A OG  1 
ATOM   1625 N N   . GLY A 1 206 ? 43.981  -24.391 11.361  1.00 56.37 ? 208 GLY A N   1 
ATOM   1626 C CA  . GLY A 1 206 ? 45.094  -23.514 11.012  1.00 57.59 ? 208 GLY A CA  1 
ATOM   1627 C C   . GLY A 1 206 ? 44.614  -22.140 10.605  1.00 58.93 ? 208 GLY A C   1 
ATOM   1628 O O   . GLY A 1 206 ? 43.544  -21.702 11.059  1.00 60.81 ? 208 GLY A O   1 
ATOM   1629 N N   . LYS A 1 210 ? 39.256  -22.911 3.697   1.00 60.06 ? 212 LYS A N   1 
ATOM   1630 C CA  . LYS A 1 210 ? 38.844  -24.262 3.303   1.00 61.27 ? 212 LYS A CA  1 
ATOM   1631 C C   . LYS A 1 210 ? 37.682  -24.194 2.253   1.00 60.11 ? 212 LYS A C   1 
ATOM   1632 O O   . LYS A 1 210 ? 36.603  -24.755 2.465   1.00 59.99 ? 212 LYS A O   1 
ATOM   1633 C CB  . LYS A 1 210 ? 38.480  -25.100 4.552   1.00 65.33 ? 212 LYS A CB  1 
ATOM   1634 C CG  . LYS A 1 210 ? 37.666  -24.354 5.658   1.00 73.12 ? 212 LYS A CG  1 
ATOM   1635 C CD  . LYS A 1 210 ? 38.065  -24.763 7.103   1.00 79.25 ? 212 LYS A CD  1 
ATOM   1636 C CE  . LYS A 1 210 ? 37.951  -23.574 8.048   1.00 84.22 ? 212 LYS A CE  1 
ATOM   1637 N NZ  . LYS A 1 210 ? 38.062  -23.940 9.499   1.00 84.56 ? 212 LYS A NZ  1 
ATOM   1638 N N   . ASN A 1 211 ? 37.935  -23.491 1.112   1.00 58.17 ? 213 ASN A N   1 
ATOM   1639 C CA  . ASN A 1 211 ? 36.916  -23.235 0.085   1.00 56.19 ? 213 ASN A CA  1 
ATOM   1640 C C   . ASN A 1 211 ? 36.845  -24.389 -0.854  1.00 56.56 ? 213 ASN A C   1 
ATOM   1641 O O   . ASN A 1 211 ? 37.861  -24.716 -1.505  1.00 57.66 ? 213 ASN A O   1 
ATOM   1642 C CB  . ASN A 1 211 ? 37.244  -21.955 -0.674  1.00 54.94 ? 213 ASN A CB  1 
ATOM   1643 C CG  . ASN A 1 211 ? 37.127  -20.750 0.196   1.00 56.66 ? 213 ASN A CG  1 
ATOM   1644 O OD1 . ASN A 1 211 ? 36.272  -20.685 1.071   1.00 56.13 ? 213 ASN A OD1 1 
ATOM   1645 N ND2 . ASN A 1 211 ? 37.979  -19.769 0.008   1.00 57.60 ? 213 ASN A ND2 1 
ATOM   1646 N N   . ARG A 1 212 ? 35.689  -25.053 -0.936  1.00 56.19 ? 214 ARG A N   1 
ATOM   1647 C CA  . ARG A 1 212 ? 35.508  -26.071 -1.985  1.00 57.61 ? 214 ARG A CA  1 
ATOM   1648 C C   . ARG A 1 212 ? 35.385  -25.344 -3.336  1.00 57.56 ? 214 ARG A C   1 
ATOM   1649 O O   . ARG A 1 212 ? 35.961  -25.795 -4.334  1.00 58.40 ? 214 ARG A O   1 
ATOM   1650 C CB  . ARG A 1 212 ? 34.242  -26.928 -1.811  1.00 59.84 ? 214 ARG A CB  1 
ATOM   1651 C CG  . ARG A 1 212 ? 33.801  -27.201 -0.394  1.00 65.85 ? 214 ARG A CG  1 
ATOM   1652 C CD  . ARG A 1 212 ? 33.447  -28.649 -0.141  1.00 71.77 ? 214 ARG A CD  1 
ATOM   1653 N NE  . ARG A 1 212 ? 32.406  -29.135 -1.054  1.00 76.51 ? 214 ARG A NE  1 
ATOM   1654 C CZ  . ARG A 1 212 ? 31.606  -30.172 -0.822  1.00 78.57 ? 214 ARG A CZ  1 
ATOM   1655 N NH1 . ARG A 1 212 ? 31.709  -30.866 0.319   1.00 76.89 ? 214 ARG A NH1 1 
ATOM   1656 N NH2 . ARG A 1 212 ? 30.693  -30.527 -1.723  1.00 77.86 ? 214 ARG A NH2 1 
ATOM   1657 N N   . PHE A 1 213 ? 34.617  -24.211 -3.360  1.00 54.97 ? 215 PHE A N   1 
ATOM   1658 C CA  . PHE A 1 213 ? 34.356  -23.464 -4.562  1.00 52.93 ? 215 PHE A CA  1 
ATOM   1659 C C   . PHE A 1 213 ? 34.597  -22.005 -4.325  1.00 51.79 ? 215 PHE A C   1 
ATOM   1660 O O   . PHE A 1 213 ? 34.377  -21.495 -3.238  1.00 48.10 ? 215 PHE A O   1 
ATOM   1661 C CB  . PHE A 1 213 ? 32.913  -23.627 -5.007  1.00 52.42 ? 215 PHE A CB  1 
ATOM   1662 C CG  . PHE A 1 213 ? 32.359  -25.006 -5.153  1.00 53.19 ? 215 PHE A CG  1 
ATOM   1663 C CD1 . PHE A 1 213 ? 32.843  -25.865 -6.130  1.00 54.99 ? 215 PHE A CD1 1 
ATOM   1664 C CD2 . PHE A 1 213 ? 31.303  -25.429 -4.376  1.00 53.85 ? 215 PHE A CD2 1 
ATOM   1665 C CE1 . PHE A 1 213 ? 32.300  -27.128 -6.296  1.00 55.02 ? 215 PHE A CE1 1 
ATOM   1666 C CE2 . PHE A 1 213 ? 30.752  -26.683 -4.549  1.00 54.84 ? 215 PHE A CE2 1 
ATOM   1667 C CZ  . PHE A 1 213 ? 31.262  -27.535 -5.507  1.00 54.34 ? 215 PHE A CZ  1 
ATOM   1668 N N   . VAL A 1 214 ? 35.053  -21.328 -5.376  1.00 52.38 ? 216 VAL A N   1 
ATOM   1669 C CA  . VAL A 1 214 ? 35.188  -19.891 -5.412  1.00 53.61 ? 216 VAL A CA  1 
ATOM   1670 C C   . VAL A 1 214 ? 34.484  -19.395 -6.678  1.00 53.34 ? 216 VAL A C   1 
ATOM   1671 O O   . VAL A 1 214 ? 34.480  -20.116 -7.672  1.00 54.43 ? 216 VAL A O   1 
ATOM   1672 C CB  . VAL A 1 214 ? 36.683  -19.537 -5.395  1.00 56.12 ? 216 VAL A CB  1 
ATOM   1673 C CG1 . VAL A 1 214 ? 36.864  -18.039 -5.448  1.00 57.78 ? 216 VAL A CG1 1 
ATOM   1674 C CG2 . VAL A 1 214 ? 37.365  -20.094 -4.150  1.00 56.74 ? 216 VAL A CG2 1 
ATOM   1675 N N   . VAL A 1 215 ? 33.887  -18.191 -6.652  1.00 51.63 ? 217 VAL A N   1 
ATOM   1676 C CA  . VAL A 1 215 ? 33.401  -17.520 -7.865  1.00 52.15 ? 217 VAL A CA  1 
ATOM   1677 C C   . VAL A 1 215 ? 33.682  -16.014 -7.795  1.00 52.68 ? 217 VAL A C   1 
ATOM   1678 O O   . VAL A 1 215 ? 33.766  -15.368 -8.879  1.00 51.76 ? 217 VAL A O   1 
ATOM   1679 C CB  . VAL A 1 215 ? 31.908  -17.777 -8.204  1.00 52.78 ? 217 VAL A CB  1 
ATOM   1680 C CG1 . VAL A 1 215 ? 31.562  -19.250 -8.108  1.00 54.13 ? 217 VAL A CG1 1 
ATOM   1681 C CG2 . VAL A 1 215 ? 30.991  -16.956 -7.322  1.00 52.46 ? 217 VAL A CG2 1 
ATOM   1682 O OXT . VAL A 1 215 ? 33.793  -15.491 -6.662  1.00 50.79 ? 217 VAL A OXT 1 
ATOM   1683 N N   . HIS B 1 7   ? -2.528  -14.155 4.054   1.00 79.33 ? 9   HIS B N   1 
ATOM   1684 C CA  . HIS B 1 7   ? -1.088  -13.975 4.260   1.00 79.23 ? 9   HIS B CA  1 
ATOM   1685 C C   . HIS B 1 7   ? -0.843  -12.824 5.229   1.00 77.36 ? 9   HIS B C   1 
ATOM   1686 O O   . HIS B 1 7   ? -1.367  -11.732 5.018   1.00 78.25 ? 9   HIS B O   1 
ATOM   1687 C CB  . HIS B 1 7   ? -0.374  -13.743 2.915   1.00 81.09 ? 9   HIS B CB  1 
ATOM   1688 C CG  . HIS B 1 7   ? -0.075  -15.008 2.186   1.00 84.16 ? 9   HIS B CG  1 
ATOM   1689 N ND1 . HIS B 1 7   ? 0.742   -15.986 2.738   1.00 86.28 ? 9   HIS B ND1 1 
ATOM   1690 C CD2 . HIS B 1 7   ? -0.506  -15.432 0.976   1.00 85.62 ? 9   HIS B CD2 1 
ATOM   1691 C CE1 . HIS B 1 7   ? 0.786   -16.965 1.847   1.00 86.78 ? 9   HIS B CE1 1 
ATOM   1692 N NE2 . HIS B 1 7   ? 0.052   -16.678 0.770   1.00 86.67 ? 9   HIS B NE2 1 
ATOM   1693 N N   . GLY B 1 8   ? -0.047  -13.081 6.266   1.00 74.70 ? 10  GLY B N   1 
ATOM   1694 C CA  . GLY B 1 8   ? -0.024  -12.292 7.497   1.00 72.50 ? 10  GLY B CA  1 
ATOM   1695 C C   . GLY B 1 8   ? -0.875  -12.870 8.624   1.00 70.49 ? 10  GLY B C   1 
ATOM   1696 O O   . GLY B 1 8   ? -0.990  -12.255 9.684   1.00 71.14 ? 10  GLY B O   1 
ATOM   1697 N N   . ALA B 1 9   ? -1.464  -14.070 8.425   1.00 68.60 ? 11  ALA B N   1 
ATOM   1698 C CA  . ALA B 1 9   ? -2.476  -14.687 9.291   1.00 66.61 ? 11  ALA B CA  1 
ATOM   1699 C C   . ALA B 1 9   ? -1.818  -15.361 10.506  1.00 65.48 ? 11  ALA B C   1 
ATOM   1700 O O   . ALA B 1 9   ? -0.706  -15.886 10.378  1.00 65.50 ? 11  ALA B O   1 
ATOM   1701 C CB  . ALA B 1 9   ? -3.246  -15.737 8.493   1.00 65.42 ? 11  ALA B CB  1 
ATOM   1702 N N   . ARG B 1 10  ? -2.505  -15.357 11.672  1.00 64.13 ? 12  ARG B N   1 
ATOM   1703 C CA  . ARG B 1 10  ? -2.006  -16.039 12.872  1.00 62.92 ? 12  ARG B CA  1 
ATOM   1704 C C   . ARG B 1 10  ? -1.990  -17.556 12.681  1.00 62.27 ? 12  ARG B C   1 
ATOM   1705 O O   . ARG B 1 10  ? -2.963  -18.129 12.190  1.00 62.73 ? 12  ARG B O   1 
ATOM   1706 C CB  . ARG B 1 10  ? -2.857  -15.659 14.106  1.00 63.87 ? 12  ARG B CB  1 
ATOM   1707 C CG  . ARG B 1 10  ? -2.293  -16.139 15.466  1.00 68.11 ? 12  ARG B CG  1 
ATOM   1708 C CD  . ARG B 1 10  ? -3.162  -15.693 16.655  1.00 70.18 ? 12  ARG B CD  1 
ATOM   1709 N NE  . ARG B 1 10  ? -3.282  -14.239 16.673  1.00 72.08 ? 12  ARG B NE  1 
ATOM   1710 C CZ  . ARG B 1 10  ? -2.378  -13.406 17.182  1.00 72.36 ? 12  ARG B CZ  1 
ATOM   1711 N NH1 . ARG B 1 10  ? -1.265  -13.879 17.746  1.00 72.52 ? 12  ARG B NH1 1 
ATOM   1712 N NH2 . ARG B 1 10  ? -2.576  -12.102 17.131  1.00 69.29 ? 12  ARG B NH2 1 
ATOM   1713 N N   . ILE B 1 11  ? -0.877  -18.212 13.077  1.00 59.62 ? 13  ILE B N   1 
ATOM   1714 C CA  . ILE B 1 11  ? -0.779  -19.657 13.061  1.00 57.07 ? 13  ILE B CA  1 
ATOM   1715 C C   . ILE B 1 11  ? -1.449  -20.214 14.338  1.00 54.56 ? 13  ILE B C   1 
ATOM   1716 O O   . ILE B 1 11  ? -0.903  -20.054 15.443  1.00 53.54 ? 13  ILE B O   1 
ATOM   1717 C CB  . ILE B 1 11  ? 0.697   -20.124 12.957  1.00 58.08 ? 13  ILE B CB  1 
ATOM   1718 C CG1 . ILE B 1 11  ? 1.445   -19.466 11.773  1.00 60.32 ? 13  ILE B CG1 1 
ATOM   1719 C CG2 . ILE B 1 11  ? 0.764   -21.647 12.852  1.00 57.88 ? 13  ILE B CG2 1 
ATOM   1720 C CD1 . ILE B 1 11  ? 2.926   -19.771 11.765  1.00 63.02 ? 13  ILE B CD1 1 
ATOM   1721 N N   . ILE B 1 12  ? -2.600  -20.887 14.177  1.00 52.49 ? 14  ILE B N   1 
ATOM   1722 C CA  . ILE B 1 12  ? -3.416  -21.391 15.264  1.00 51.27 ? 14  ILE B CA  1 
ATOM   1723 C C   . ILE B 1 12  ? -3.576  -22.868 15.058  1.00 50.44 ? 14  ILE B C   1 
ATOM   1724 O O   . ILE B 1 12  ? -3.940  -23.305 13.956  1.00 51.19 ? 14  ILE B O   1 
ATOM   1725 C CB  . ILE B 1 12  ? -4.796  -20.695 15.311  1.00 52.40 ? 14  ILE B CB  1 
ATOM   1726 C CG1 . ILE B 1 12  ? -4.654  -19.157 15.517  1.00 54.63 ? 14  ILE B CG1 1 
ATOM   1727 C CG2 . ILE B 1 12  ? -5.698  -21.294 16.402  1.00 52.45 ? 14  ILE B CG2 1 
ATOM   1728 C CD1 . ILE B 1 12  ? -5.894  -18.408 15.370  1.00 56.22 ? 14  ILE B CD1 1 
ATOM   1729 N N   . TYR B 1 13  ? -3.301  -23.649 16.102  1.00 48.28 ? 15  TYR B N   1 
ATOM   1730 C CA  . TYR B 1 13  ? -3.532  -25.090 16.107  1.00 48.63 ? 15  TYR B CA  1 
ATOM   1731 C C   . TYR B 1 13  ? -4.467  -25.472 17.216  1.00 50.02 ? 15  TYR B C   1 
ATOM   1732 O O   . TYR B 1 13  ? -4.267  -25.057 18.362  1.00 51.77 ? 15  TYR B O   1 
ATOM   1733 C CB  . TYR B 1 13  ? -2.240  -25.842 16.344  1.00 47.68 ? 15  TYR B CB  1 
ATOM   1734 C CG  . TYR B 1 13  ? -1.174  -25.609 15.315  1.00 48.95 ? 15  TYR B CG  1 
ATOM   1735 C CD1 . TYR B 1 13  ? -1.257  -26.189 14.060  1.00 50.36 ? 15  TYR B CD1 1 
ATOM   1736 C CD2 . TYR B 1 13  ? -0.070  -24.835 15.597  1.00 48.17 ? 15  TYR B CD2 1 
ATOM   1737 C CE1 . TYR B 1 13  ? -0.261  -26.018 13.114  1.00 51.40 ? 15  TYR B CE1 1 
ATOM   1738 C CE2 . TYR B 1 13  ? 0.930   -24.648 14.658  1.00 49.38 ? 15  TYR B CE2 1 
ATOM   1739 C CZ  . TYR B 1 13  ? 0.827   -25.240 13.406  1.00 51.59 ? 15  TYR B CZ  1 
ATOM   1740 O OH  . TYR B 1 13  ? 1.788   -25.047 12.448  1.00 52.62 ? 15  TYR B OH  1 
ATOM   1741 N N   . ASP B 1 14  ? -5.476  -26.269 16.910  1.00 49.81 ? 16  ASP B N   1 
ATOM   1742 C CA  . ASP B 1 14  ? -6.318  -26.820 17.964  1.00 49.39 ? 16  ASP B CA  1 
ATOM   1743 C C   . ASP B 1 14  ? -5.663  -28.044 18.607  1.00 47.50 ? 16  ASP B C   1 
ATOM   1744 O O   . ASP B 1 14  ? -4.646  -28.592 18.139  1.00 47.13 ? 16  ASP B O   1 
ATOM   1745 C CB  . ASP B 1 14  ? -7.761  -27.068 17.506  1.00 51.89 ? 16  ASP B CB  1 
ATOM   1746 C CG  . ASP B 1 14  ? -7.956  -28.099 16.431  1.00 57.22 ? 16  ASP B CG  1 
ATOM   1747 O OD1 . ASP B 1 14  ? -7.080  -28.959 16.273  1.00 56.10 ? 16  ASP B OD1 1 
ATOM   1748 O OD2 . ASP B 1 14  ? -8.996  -28.033 15.737  1.00 62.80 ? 16  ASP B OD2 1 
ATOM   1749 N N   . ARG B 1 15  ? -6.260  -28.470 19.697  1.00 45.96 ? 17  ARG B N   1 
ATOM   1750 C CA  . ARG B 1 15  ? -5.753  -29.563 20.503  1.00 45.44 ? 17  ARG B CA  1 
ATOM   1751 C C   . ARG B 1 15  ? -5.608  -30.859 19.670  1.00 46.25 ? 17  ARG B C   1 
ATOM   1752 O O   . ARG B 1 15  ? -4.596  -31.538 19.755  1.00 44.59 ? 17  ARG B O   1 
ATOM   1753 C CB  . ARG B 1 15  ? -6.704  -29.797 21.674  1.00 44.82 ? 17  ARG B CB  1 
ATOM   1754 C CG  . ARG B 1 15  ? -6.154  -30.657 22.725  1.00 48.07 ? 17  ARG B CG  1 
ATOM   1755 C CD  . ARG B 1 15  ? -7.242  -31.036 23.718  1.00 51.45 ? 17  ARG B CD  1 
ATOM   1756 N NE  . ARG B 1 15  ? -6.727  -31.965 24.714  1.00 56.41 ? 17  ARG B NE  1 
ATOM   1757 C CZ  . ARG B 1 15  ? -6.548  -33.274 24.523  1.00 62.07 ? 17  ARG B CZ  1 
ATOM   1758 N NH1 . ARG B 1 15  ? -6.839  -33.833 23.348  1.00 64.50 ? 17  ARG B NH1 1 
ATOM   1759 N NH2 . ARG B 1 15  ? -6.070  -34.029 25.496  1.00 63.12 ? 17  ARG B NH2 1 
ATOM   1760 N N   . ALA B 1 16  ? -6.625  -31.186 18.859  1.00 47.64 ? 18  ALA B N   1 
ATOM   1761 C CA  . ALA B 1 16  ? -6.622  -32.409 18.062  1.00 48.33 ? 18  ALA B CA  1 
ATOM   1762 C C   . ALA B 1 16  ? -5.444  -32.411 17.070  1.00 48.77 ? 18  ALA B C   1 
ATOM   1763 O O   . ALA B 1 16  ? -4.760  -33.418 16.949  1.00 50.34 ? 18  ALA B O   1 
ATOM   1764 C CB  . ALA B 1 16  ? -7.948  -32.534 17.321  1.00 49.52 ? 18  ALA B CB  1 
ATOM   1765 N N   . PHE B 1 17  ? -5.196  -31.311 16.383  1.00 48.55 ? 19  PHE B N   1 
ATOM   1766 C CA  . PHE B 1 17  ? -4.065  -31.190 15.476  1.00 49.11 ? 19  PHE B CA  1 
ATOM   1767 C C   . PHE B 1 17  ? -2.731  -31.383 16.196  1.00 46.52 ? 19  PHE B C   1 
ATOM   1768 O O   . PHE B 1 17  ? -1.916  -32.170 15.749  1.00 45.13 ? 19  PHE B O   1 
ATOM   1769 C CB  . PHE B 1 17  ? -4.069  -29.827 14.784  1.00 51.15 ? 19  PHE B CB  1 
ATOM   1770 C CG  . PHE B 1 17  ? -3.164  -29.807 13.578  1.00 54.84 ? 19  PHE B CG  1 
ATOM   1771 C CD1 . PHE B 1 17  ? -3.620  -30.241 12.345  1.00 58.20 ? 19  PHE B CD1 1 
ATOM   1772 C CD2 . PHE B 1 17  ? -1.844  -29.429 13.692  1.00 56.55 ? 19  PHE B CD2 1 
ATOM   1773 C CE1 . PHE B 1 17  ? -2.778  -30.256 11.240  1.00 59.82 ? 19  PHE B CE1 1 
ATOM   1774 C CE2 . PHE B 1 17  ? -1.003  -29.443 12.584  1.00 58.59 ? 19  PHE B CE2 1 
ATOM   1775 C CZ  . PHE B 1 17  ? -1.481  -29.833 11.364  1.00 59.50 ? 19  PHE B CZ  1 
ATOM   1776 N N   . LEU B 1 18  ? -2.506  -30.673 17.338  1.00 46.09 ? 20  LEU B N   1 
ATOM   1777 C CA  . LEU B 1 18  ? -1.243  -30.820 18.079  1.00 43.92 ? 20  LEU B CA  1 
ATOM   1778 C C   . LEU B 1 18  ? -1.002  -32.256 18.513  1.00 44.54 ? 20  LEU B C   1 
ATOM   1779 O O   . LEU B 1 18  ? 0.113   -32.777 18.405  1.00 43.78 ? 20  LEU B O   1 
ATOM   1780 C CB  . LEU B 1 18  ? -1.234  -29.831 19.261  1.00 43.11 ? 20  LEU B CB  1 
ATOM   1781 C CG  . LEU B 1 18  ? -1.243  -28.337 18.872  1.00 43.03 ? 20  LEU B CG  1 
ATOM   1782 C CD1 . LEU B 1 18  ? -1.432  -27.434 20.088  1.00 40.41 ? 20  LEU B CD1 1 
ATOM   1783 C CD2 . LEU B 1 18  ? 0.011   -27.928 18.151  1.00 45.82 ? 20  LEU B CD2 1 
ATOM   1784 N N   . MET B 1 19  ? -2.049  -32.916 18.984  1.00 45.77 ? 21  MET B N   1 
ATOM   1785 C CA  . MET B 1 19  ? -1.970  -34.276 19.451  1.00 48.54 ? 21  MET B CA  1 
ATOM   1786 C C   . MET B 1 19  ? -1.701  -35.245 18.294  1.00 51.14 ? 21  MET B C   1 
ATOM   1787 O O   . MET B 1 19  ? -1.131  -36.289 18.545  1.00 53.02 ? 21  MET B O   1 
ATOM   1788 C CB  . MET B 1 19  ? -3.283  -34.691 20.175  1.00 49.90 ? 21  MET B CB  1 
ATOM   1789 C CG  . MET B 1 19  ? -3.549  -33.932 21.488  1.00 54.22 ? 21  MET B CG  1 
ATOM   1790 S SD  . MET B 1 19  ? -2.262  -34.049 22.779  1.00 55.31 ? 21  MET B SD  1 
ATOM   1791 C CE  . MET B 1 19  ? -2.191  -35.812 22.953  1.00 64.83 ? 21  MET B CE  1 
ATOM   1792 N N   . ALA B 1 20  ? -2.101  -34.922 17.040  1.00 51.76 ? 22  ALA B N   1 
ATOM   1793 C CA  . ALA B 1 20  ? -1.849  -35.770 15.835  1.00 53.42 ? 22  ALA B CA  1 
ATOM   1794 C C   . ALA B 1 20  ? -0.390  -35.686 15.383  1.00 53.53 ? 22  ALA B C   1 
ATOM   1795 O O   . ALA B 1 20  ? 0.129   -36.651 14.830  1.00 53.83 ? 22  ALA B O   1 
ATOM   1796 C CB  . ALA B 1 20  ? -2.756  -35.341 14.687  1.00 53.63 ? 22  ALA B CB  1 
ATOM   1797 N N   . CYS B 1 21  ? 0.269   -34.565 15.627  1.00 52.39 ? 23  CYS B N   1 
ATOM   1798 C CA  . CYS B 1 21  ? 1.713   -34.422 15.422  1.00 52.12 ? 23  CYS B CA  1 
ATOM   1799 C C   . CYS B 1 21  ? 2.551   -35.151 16.454  1.00 51.15 ? 23  CYS B C   1 
ATOM   1800 O O   . CYS B 1 21  ? 3.778   -35.204 16.291  1.00 52.52 ? 23  CYS B O   1 
ATOM   1801 C CB  . CYS B 1 21  ? 2.084   -32.943 15.387  1.00 53.79 ? 23  CYS B CB  1 
ATOM   1802 S SG  . CYS B 1 21  ? 1.180   -31.961 14.170  1.00 55.88 ? 23  CYS B SG  1 
ATOM   1803 N N   . ARG B 1 22  ? 1.936   -35.699 17.515  1.00 48.05 ? 24  ARG B N   1 
ATOM   1804 C CA  . ARG B 1 22  ? 2.667   -36.322 18.583  1.00 47.79 ? 24  ARG B CA  1 
ATOM   1805 C C   . ARG B 1 22  ? 3.002   -37.768 18.176  1.00 50.62 ? 24  ARG B C   1 
ATOM   1806 O O   . ARG B 1 22  ? 4.183   -38.105 18.123  1.00 52.67 ? 24  ARG B O   1 
ATOM   1807 C CB  . ARG B 1 22  ? 1.824   -36.315 19.853  1.00 45.39 ? 24  ARG B CB  1 
ATOM   1808 C CG  . ARG B 1 22  ? 2.561   -36.792 21.079  1.00 46.23 ? 24  ARG B CG  1 
ATOM   1809 C CD  . ARG B 1 22  ? 1.636   -36.723 22.255  1.00 46.60 ? 24  ARG B CD  1 
ATOM   1810 N NE  . ARG B 1 22  ? 2.310   -37.055 23.511  1.00 46.99 ? 24  ARG B NE  1 
ATOM   1811 C CZ  . ARG B 1 22  ? 1.721   -37.019 24.703  1.00 49.16 ? 24  ARG B CZ  1 
ATOM   1812 N NH1 . ARG B 1 22  ? 0.451   -36.677 24.810  1.00 45.07 ? 24  ARG B NH1 1 
ATOM   1813 N NH2 . ARG B 1 22  ? 2.398   -37.342 25.796  1.00 50.83 ? 24  ARG B NH2 1 
ATOM   1814 N N   . LYS B 1 34  ? 8.147   -29.864 9.264   1.00 56.76 ? 36  LYS B N   1 
ATOM   1815 C CA  . LYS B 1 34  ? 7.682   -29.555 10.607  1.00 56.74 ? 36  LYS B CA  1 
ATOM   1816 C C   . LYS B 1 34  ? 6.654   -28.449 10.567  1.00 54.67 ? 36  LYS B C   1 
ATOM   1817 O O   . LYS B 1 34  ? 6.618   -27.648 9.619   1.00 56.10 ? 36  LYS B O   1 
ATOM   1818 C CB  . LYS B 1 34  ? 8.865   -29.162 11.506  1.00 60.76 ? 36  LYS B CB  1 
ATOM   1819 C CG  . LYS B 1 34  ? 9.685   -30.373 11.919  1.00 64.75 ? 36  LYS B CG  1 
ATOM   1820 C CD  . LYS B 1 34  ? 10.885  -29.965 12.715  1.00 71.08 ? 36  LYS B CD  1 
ATOM   1821 C CE  . LYS B 1 34  ? 11.616  -31.173 13.226  1.00 77.14 ? 36  LYS B CE  1 
ATOM   1822 N NZ  . LYS B 1 34  ? 12.840  -30.768 13.950  1.00 82.48 ? 36  LYS B NZ  1 
ATOM   1823 N N   . HIS B 1 35  ? 5.815   -28.400 11.591  1.00 51.64 ? 37  HIS B N   1 
ATOM   1824 C CA  . HIS B 1 35  ? 4.713   -27.459 11.626  1.00 50.44 ? 37  HIS B CA  1 
ATOM   1825 C C   . HIS B 1 35  ? 5.142   -26.256 12.444  1.00 50.28 ? 37  HIS B C   1 
ATOM   1826 O O   . HIS B 1 35  ? 5.335   -26.406 13.645  1.00 48.69 ? 37  HIS B O   1 
ATOM   1827 C CB  . HIS B 1 35  ? 3.474   -28.117 12.213  1.00 49.39 ? 37  HIS B CB  1 
ATOM   1828 C CG  . HIS B 1 35  ? 2.890   -29.137 11.300  1.00 53.74 ? 37  HIS B CG  1 
ATOM   1829 N ND1 . HIS B 1 35  ? 3.191   -30.485 11.429  1.00 56.90 ? 37  HIS B ND1 1 
ATOM   1830 C CD2 . HIS B 1 35  ? 2.047   -28.969 10.252  1.00 55.82 ? 37  HIS B CD2 1 
ATOM   1831 C CE1 . HIS B 1 35  ? 2.519   -31.095 10.464  1.00 58.24 ? 37  HIS B CE1 1 
ATOM   1832 N NE2 . HIS B 1 35  ? 1.814   -30.220 9.730   1.00 57.96 ? 37  HIS B NE2 1 
ATOM   1833 N N   . PRO B 1 36  ? 5.306   -25.077 11.821  1.00 51.09 ? 38  PRO B N   1 
ATOM   1834 C CA  . PRO B 1 36  ? 5.817   -23.930 12.567  1.00 49.95 ? 38  PRO B CA  1 
ATOM   1835 C C   . PRO B 1 36  ? 4.835   -23.388 13.583  1.00 48.88 ? 38  PRO B C   1 
ATOM   1836 O O   . PRO B 1 36  ? 3.638   -23.411 13.361  1.00 50.30 ? 38  PRO B O   1 
ATOM   1837 C CB  . PRO B 1 36  ? 6.095   -22.888 11.461  1.00 52.17 ? 38  PRO B CB  1 
ATOM   1838 C CG  . PRO B 1 36  ? 5.133   -23.236 10.391  1.00 53.70 ? 38  PRO B CG  1 
ATOM   1839 C CD  . PRO B 1 36  ? 5.051   -24.721 10.402  1.00 52.36 ? 38  PRO B CD  1 
ATOM   1840 N N   . LEU B 1 37  ? 5.358   -22.888 14.700  1.00 46.14 ? 39  LEU B N   1 
ATOM   1841 C CA  . LEU B 1 37  ? 4.560   -22.145 15.679  1.00 43.25 ? 39  LEU B CA  1 
ATOM   1842 C C   . LEU B 1 37  ? 4.556   -20.677 15.356  1.00 42.84 ? 39  LEU B C   1 
ATOM   1843 O O   . LEU B 1 37  ? 5.502   -20.204 14.741  1.00 42.86 ? 39  LEU B O   1 
ATOM   1844 C CB  . LEU B 1 37  ? 5.128   -22.379 17.092  1.00 42.02 ? 39  LEU B CB  1 
ATOM   1845 C CG  . LEU B 1 37  ? 5.112   -23.819 17.632  1.00 42.43 ? 39  LEU B CG  1 
ATOM   1846 C CD1 . LEU B 1 37  ? 5.733   -23.893 19.035  1.00 42.78 ? 39  LEU B CD1 1 
ATOM   1847 C CD2 . LEU B 1 37  ? 3.746   -24.404 17.585  1.00 43.93 ? 39  LEU B CD2 1 
ATOM   1848 N N   . GLN B 1 38  ? 3.505   -19.954 15.796  1.00 41.71 ? 40  GLN B N   1 
ATOM   1849 C CA  . GLN B 1 38  ? 3.388   -18.503 15.695  1.00 43.77 ? 40  GLN B CA  1 
ATOM   1850 C C   . GLN B 1 38  ? 4.549   -17.829 16.397  1.00 43.61 ? 40  GLN B C   1 
ATOM   1851 O O   . GLN B 1 38  ? 5.126   -16.874 15.873  1.00 44.79 ? 40  GLN B O   1 
ATOM   1852 C CB  . GLN B 1 38  ? 2.060   -18.052 16.343  1.00 47.35 ? 40  GLN B CB  1 
ATOM   1853 C CG  . GLN B 1 38  ? 1.794   -16.548 16.375  1.00 49.91 ? 40  GLN B CG  1 
ATOM   1854 C CD  . GLN B 1 38  ? 1.666   -15.941 14.988  1.00 55.77 ? 40  GLN B CD  1 
ATOM   1855 O OE1 . GLN B 1 38  ? 1.368   -16.622 14.003  1.00 56.92 ? 40  GLN B OE1 1 
ATOM   1856 N NE2 . GLN B 1 38  ? 1.880   -14.623 14.910  1.00 56.54 ? 40  GLN B NE2 1 
ATOM   1857 N N   . ASN B 1 39  ? 4.913   -18.346 17.589  1.00 42.31 ? 41  ASN B N   1 
ATOM   1858 C CA  . ASN B 1 39  ? 5.951   -17.800 18.430  1.00 40.85 ? 41  ASN B CA  1 
ATOM   1859 C C   . ASN B 1 39  ? 7.022   -18.831 18.687  1.00 39.27 ? 41  ASN B C   1 
ATOM   1860 O O   . ASN B 1 39  ? 6.765   -20.037 18.633  1.00 40.88 ? 41  ASN B O   1 
ATOM   1861 C CB  . ASN B 1 39  ? 5.330   -17.340 19.765  1.00 41.89 ? 41  ASN B CB  1 
ATOM   1862 C CG  . ASN B 1 39  ? 4.557   -16.065 19.619  1.00 47.15 ? 41  ASN B CG  1 
ATOM   1863 O OD1 . ASN B 1 39  ? 5.146   -14.999 19.435  1.00 50.95 ? 41  ASN B OD1 1 
ATOM   1864 N ND2 . ASN B 1 39  ? 3.241   -16.122 19.682  1.00 46.28 ? 41  ASN B ND2 1 
ATOM   1865 N N   . ARG B 1 40  ? 8.230   -18.367 18.986  1.00 38.01 ? 42  ARG B N   1 
ATOM   1866 C CA  . ARG B 1 40  ? 9.274   -19.199 19.556  1.00 35.86 ? 42  ARG B CA  1 
ATOM   1867 C C   . ARG B 1 40  ? 9.089   -19.112 21.085  1.00 33.89 ? 42  ARG B C   1 
ATOM   1868 O O   . ARG B 1 40  ? 8.728   -18.079 21.634  1.00 34.69 ? 42  ARG B O   1 
ATOM   1869 C CB  . ARG B 1 40  ? 10.647  -18.715 19.165  1.00 37.93 ? 42  ARG B CB  1 
ATOM   1870 C CG  . ARG B 1 40  ? 11.764  -19.542 19.682  1.00 37.59 ? 42  ARG B CG  1 
ATOM   1871 C CD  . ARG B 1 40  ? 12.935  -19.394 18.703  1.00 38.77 ? 42  ARG B CD  1 
ATOM   1872 N NE  . ARG B 1 40  ? 14.107  -20.253 18.963  1.00 38.56 ? 42  ARG B NE  1 
ATOM   1873 C CZ  . ARG B 1 40  ? 15.269  -19.893 19.543  1.00 39.92 ? 42  ARG B CZ  1 
ATOM   1874 N NH1 . ARG B 1 40  ? 15.452  -18.657 19.972  1.00 37.42 ? 42  ARG B NH1 1 
ATOM   1875 N NH2 . ARG B 1 40  ? 16.259  -20.777 19.670  1.00 40.06 ? 42  ARG B NH2 1 
ATOM   1876 N N   . TRP B 1 41  ? 9.286   -20.237 21.749  1.00 33.13 ? 43  TRP B N   1 
ATOM   1877 C CA  . TRP B 1 41  ? 9.028   -20.428 23.171  1.00 31.88 ? 43  TRP B CA  1 
ATOM   1878 C C   . TRP B 1 41  ? 10.299  -20.937 23.844  1.00 32.02 ? 43  TRP B C   1 
ATOM   1879 O O   . TRP B 1 41  ? 11.072  -21.629 23.217  1.00 33.81 ? 43  TRP B O   1 
ATOM   1880 C CB  . TRP B 1 41  ? 7.869   -21.448 23.390  1.00 31.41 ? 43  TRP B CB  1 
ATOM   1881 C CG  . TRP B 1 41  ? 6.548   -20.967 22.881  1.00 32.69 ? 43  TRP B CG  1 
ATOM   1882 C CD1 . TRP B 1 41  ? 6.045   -21.162 21.642  1.00 34.50 ? 43  TRP B CD1 1 
ATOM   1883 C CD2 . TRP B 1 41  ? 5.575   -20.178 23.589  1.00 33.42 ? 43  TRP B CD2 1 
ATOM   1884 N NE1 . TRP B 1 41  ? 4.826   -20.547 21.523  1.00 35.77 ? 43  TRP B NE1 1 
ATOM   1885 C CE2 . TRP B 1 41  ? 4.524   -19.915 22.690  1.00 34.38 ? 43  TRP B CE2 1 
ATOM   1886 C CE3 . TRP B 1 41  ? 5.490   -19.663 24.891  1.00 32.33 ? 43  TRP B CE3 1 
ATOM   1887 C CZ2 . TRP B 1 41  ? 3.388   -19.176 23.059  1.00 34.80 ? 43  TRP B CZ2 1 
ATOM   1888 C CZ3 . TRP B 1 41  ? 4.371   -18.940 25.259  1.00 32.83 ? 43  TRP B CZ3 1 
ATOM   1889 C CH2 . TRP B 1 41  ? 3.338   -18.691 24.349  1.00 33.64 ? 43  TRP B CH2 1 
ATOM   1890 N N   . ALA B 1 42  ? 10.500  -20.582 25.109  1.00 31.34 ? 44  ALA B N   1 
ATOM   1891 C CA  . ALA B 1 42  ? 11.645  -20.995 25.898  1.00 31.07 ? 44  ALA B CA  1 
ATOM   1892 C C   . ALA B 1 42  ? 11.138  -21.671 27.135  1.00 31.63 ? 44  ALA B C   1 
ATOM   1893 O O   . ALA B 1 42  ? 10.263  -21.100 27.837  1.00 30.83 ? 44  ALA B O   1 
ATOM   1894 C CB  . ALA B 1 42  ? 12.484  -19.790 26.273  1.00 32.52 ? 44  ALA B CB  1 
ATOM   1895 N N   . LEU B 1 43  ? 11.667  -22.857 27.437  1.00 31.72 ? 45  LEU B N   1 
ATOM   1896 C CA  . LEU B 1 43  ? 11.381  -23.589 28.676  1.00 31.67 ? 45  LEU B CA  1 
ATOM   1897 C C   . LEU B 1 43  ? 12.454  -23.307 29.680  1.00 32.32 ? 45  LEU B C   1 
ATOM   1898 O O   . LEU B 1 43  ? 13.624  -23.527 29.404  1.00 33.42 ? 45  LEU B O   1 
ATOM   1899 C CB  . LEU B 1 43  ? 11.333  -25.115 28.443  1.00 32.09 ? 45  LEU B CB  1 
ATOM   1900 C CG  . LEU B 1 43  ? 11.078  -25.946 29.685  1.00 36.45 ? 45  LEU B CG  1 
ATOM   1901 C CD1 . LEU B 1 43  ? 9.727   -25.688 30.243  1.00 35.53 ? 45  LEU B CD1 1 
ATOM   1902 C CD2 . LEU B 1 43  ? 11.247  -27.378 29.377  1.00 39.55 ? 45  LEU B CD2 1 
ATOM   1903 N N   . TRP B 1 44  ? 12.052  -22.882 30.838  1.00 31.48 ? 46  TRP B N   1 
ATOM   1904 C CA  . TRP B 1 44  ? 12.904  -22.532 31.969  1.00 33.88 ? 46  TRP B CA  1 
ATOM   1905 C C   . TRP B 1 44  ? 12.622  -23.418 33.165  1.00 36.08 ? 46  TRP B C   1 
ATOM   1906 O O   . TRP B 1 44  ? 11.517  -23.944 33.337  1.00 34.51 ? 46  TRP B O   1 
ATOM   1907 C CB  . TRP B 1 44  ? 12.604  -21.112 32.431  1.00 35.01 ? 46  TRP B CB  1 
ATOM   1908 C CG  . TRP B 1 44  ? 12.723  -20.055 31.401  1.00 37.15 ? 46  TRP B CG  1 
ATOM   1909 C CD1 . TRP B 1 44  ? 11.818  -19.716 30.440  1.00 38.19 ? 46  TRP B CD1 1 
ATOM   1910 C CD2 . TRP B 1 44  ? 13.845  -19.188 31.220  1.00 40.08 ? 46  TRP B CD2 1 
ATOM   1911 N NE1 . TRP B 1 44  ? 12.315  -18.664 29.683  1.00 38.79 ? 46  TRP B NE1 1 
ATOM   1912 C CE2 . TRP B 1 44  ? 13.554  -18.337 30.136  1.00 40.33 ? 46  TRP B CE2 1 
ATOM   1913 C CE3 . TRP B 1 44  ? 15.062  -19.029 31.893  1.00 43.36 ? 46  TRP B CE3 1 
ATOM   1914 C CZ2 . TRP B 1 44  ? 14.437  -17.340 29.707  1.00 44.17 ? 46  TRP B CZ2 1 
ATOM   1915 C CZ3 . TRP B 1 44  ? 15.936  -18.054 31.461  1.00 46.28 ? 46  TRP B CZ3 1 
ATOM   1916 C CH2 . TRP B 1 44  ? 15.622  -17.218 30.376  1.00 46.30 ? 46  TRP B CH2 1 
ATOM   1917 N N   . PHE B 1 45  ? 13.647  -23.554 34.011  1.00 37.35 ? 47  PHE B N   1 
ATOM   1918 C CA  . PHE B 1 45  ? 13.583  -24.375 35.220  1.00 41.96 ? 47  PHE B CA  1 
ATOM   1919 C C   . PHE B 1 45  ? 14.197  -23.540 36.356  1.00 41.71 ? 47  PHE B C   1 
ATOM   1920 O O   . PHE B 1 45  ? 15.221  -22.931 36.159  1.00 40.37 ? 47  PHE B O   1 
ATOM   1921 C CB  . PHE B 1 45  ? 14.322  -25.707 34.966  1.00 45.01 ? 47  PHE B CB  1 
ATOM   1922 C CG  . PHE B 1 45  ? 14.526  -26.521 36.211  1.00 48.71 ? 47  PHE B CG  1 
ATOM   1923 C CD1 . PHE B 1 45  ? 13.471  -27.196 36.797  1.00 49.84 ? 47  PHE B CD1 1 
ATOM   1924 C CD2 . PHE B 1 45  ? 15.781  -26.639 36.783  1.00 52.39 ? 47  PHE B CD2 1 
ATOM   1925 C CE1 . PHE B 1 45  ? 13.660  -27.957 37.936  1.00 51.56 ? 47  PHE B CE1 1 
ATOM   1926 C CE2 . PHE B 1 45  ? 15.965  -27.397 37.940  1.00 53.84 ? 47  PHE B CE2 1 
ATOM   1927 C CZ  . PHE B 1 45  ? 14.899  -28.034 38.516  1.00 52.70 ? 47  PHE B CZ  1 
ATOM   1928 N N   . PHE B 1 46  ? 13.570  -23.480 37.519  1.00 44.17 ? 48  PHE B N   1 
ATOM   1929 C CA  . PHE B 1 46  ? 14.100  -22.741 38.687  1.00 47.97 ? 48  PHE B CA  1 
ATOM   1930 C C   . PHE B 1 46  ? 13.905  -23.583 39.932  1.00 51.60 ? 48  PHE B C   1 
ATOM   1931 O O   . PHE B 1 46  ? 12.839  -24.177 40.121  1.00 49.96 ? 48  PHE B O   1 
ATOM   1932 C CB  . PHE B 1 46  ? 13.395  -21.365 38.837  1.00 49.42 ? 48  PHE B CB  1 
ATOM   1933 C CG  . PHE B 1 46  ? 13.886  -20.451 39.941  1.00 52.66 ? 48  PHE B CG  1 
ATOM   1934 C CD1 . PHE B 1 46  ? 15.061  -19.730 39.799  1.00 54.16 ? 48  PHE B CD1 1 
ATOM   1935 C CD2 . PHE B 1 46  ? 13.144  -20.271 41.097  1.00 55.41 ? 48  PHE B CD2 1 
ATOM   1936 C CE1 . PHE B 1 46  ? 15.521  -18.892 40.828  1.00 55.65 ? 48  PHE B CE1 1 
ATOM   1937 C CE2 . PHE B 1 46  ? 13.593  -19.420 42.120  1.00 56.43 ? 48  PHE B CE2 1 
ATOM   1938 C CZ  . PHE B 1 46  ? 14.775  -18.736 41.976  1.00 55.69 ? 48  PHE B CZ  1 
ATOM   1939 N N   . LYS B 1 47  ? 14.961  -23.665 40.779  1.00 55.15 ? 49  LYS B N   1 
ATOM   1940 C CA  . LYS B 1 47  ? 14.804  -24.099 42.171  1.00 58.54 ? 49  LYS B CA  1 
ATOM   1941 C C   . LYS B 1 47  ? 15.401  -23.002 43.056  1.00 60.34 ? 49  LYS B C   1 
ATOM   1942 O O   . LYS B 1 47  ? 16.553  -22.648 42.836  1.00 60.56 ? 49  LYS B O   1 
ATOM   1943 C CB  . LYS B 1 47  ? 15.526  -25.446 42.387  1.00 62.50 ? 49  LYS B CB  1 
ATOM   1944 C CG  . LYS B 1 47  ? 15.019  -26.203 43.626  1.00 69.50 ? 49  LYS B CG  1 
ATOM   1945 C CD  . LYS B 1 47  ? 15.513  -27.639 43.686  1.00 76.60 ? 49  LYS B CD  1 
ATOM   1946 C CE  . LYS B 1 47  ? 15.119  -28.329 44.978  1.00 82.65 ? 49  LYS B CE  1 
ATOM   1947 N NZ  . LYS B 1 47  ? 15.897  -29.585 45.199  1.00 86.19 ? 49  LYS B NZ  1 
ATOM   1948 N N   . ASN B 1 48  ? 14.639  -22.450 44.022  1.00 61.79 ? 50  ASN B N   1 
ATOM   1949 C CA  . ASN B 1 48  ? 15.146  -21.438 44.981  1.00 63.65 ? 50  ASN B CA  1 
ATOM   1950 C C   . ASN B 1 48  ? 16.130  -22.045 46.011  1.00 64.90 ? 50  ASN B C   1 
ATOM   1951 O O   . ASN B 1 48  ? 15.764  -22.297 47.165  1.00 65.49 ? 50  ASN B O   1 
ATOM   1952 C CB  . ASN B 1 48  ? 13.983  -20.698 45.691  1.00 65.94 ? 50  ASN B CB  1 
ATOM   1953 C CG  . ASN B 1 48  ? 14.409  -19.461 46.451  1.00 70.95 ? 50  ASN B CG  1 
ATOM   1954 O OD1 . ASN B 1 48  ? 15.424  -18.832 46.133  1.00 73.18 ? 50  ASN B OD1 1 
ATOM   1955 N ND2 . ASN B 1 48  ? 13.650  -19.074 47.483  1.00 72.08 ? 50  ASN B ND2 1 
ATOM   1956 N N   . ASP B 1 49  ? 17.384  -22.261 45.571  1.00 65.59 ? 51  ASP B N   1 
ATOM   1957 C CA  . ASP B 1 49  ? 18.493  -22.807 46.363  1.00 67.60 ? 51  ASP B CA  1 
ATOM   1958 C C   . ASP B 1 49  ? 19.367  -21.629 46.790  1.00 69.13 ? 51  ASP B C   1 
ATOM   1959 O O   . ASP B 1 49  ? 20.085  -21.062 45.982  1.00 68.41 ? 51  ASP B O   1 
ATOM   1960 C CB  . ASP B 1 49  ? 19.284  -23.859 45.548  1.00 69.42 ? 51  ASP B CB  1 
ATOM   1961 C CG  . ASP B 1 49  ? 20.656  -24.208 46.080  1.00 76.05 ? 51  ASP B CG  1 
ATOM   1962 O OD1 . ASP B 1 49  ? 20.822  -24.258 47.330  1.00 78.67 ? 51  ASP B OD1 1 
ATOM   1963 O OD2 . ASP B 1 49  ? 21.561  -24.426 45.261  1.00 78.00 ? 51  ASP B OD2 1 
ATOM   1964 N N   . LYS B 1 50  ? 19.303  -21.268 48.080  1.00 71.17 ? 52  LYS B N   1 
ATOM   1965 C CA  . LYS B 1 50  ? 19.883  -20.017 48.568  1.00 72.73 ? 52  LYS B CA  1 
ATOM   1966 C C   . LYS B 1 50  ? 21.407  -20.025 48.639  1.00 75.06 ? 52  LYS B C   1 
ATOM   1967 O O   . LYS B 1 50  ? 22.004  -18.943 48.722  1.00 75.62 ? 52  LYS B O   1 
ATOM   1968 C CB  . LYS B 1 50  ? 19.267  -19.655 49.933  1.00 73.65 ? 52  LYS B CB  1 
ATOM   1969 C CG  . LYS B 1 50  ? 17.846  -19.124 49.830  1.00 75.79 ? 52  LYS B CG  1 
ATOM   1970 C CD  . LYS B 1 50  ? 17.826  -17.632 49.547  1.00 80.44 ? 52  LYS B CD  1 
ATOM   1971 C CE  . LYS B 1 50  ? 16.431  -17.148 49.240  1.00 85.81 ? 52  LYS B CE  1 
ATOM   1972 N NZ  . LYS B 1 50  ? 16.436  -15.770 48.668  1.00 89.03 ? 52  LYS B NZ  1 
ATOM   1973 N N   . SER B 1 51  ? 22.049  -21.208 48.599  1.00 75.89 ? 53  SER B N   1 
ATOM   1974 C CA  . SER B 1 51  ? 23.509  -21.246 48.492  1.00 76.69 ? 53  SER B CA  1 
ATOM   1975 C C   . SER B 1 51  ? 24.000  -20.640 47.164  1.00 77.19 ? 53  SER B C   1 
ATOM   1976 O O   . SER B 1 51  ? 25.104  -20.102 47.118  1.00 77.99 ? 53  SER B O   1 
ATOM   1977 C CB  . SER B 1 51  ? 24.039  -22.664 48.685  1.00 77.90 ? 53  SER B CB  1 
ATOM   1978 O OG  . SER B 1 51  ? 23.914  -23.472 47.525  1.00 80.87 ? 53  SER B OG  1 
ATOM   1979 N N   . LYS B 1 52  ? 23.195  -20.722 46.095  1.00 76.69 ? 54  LYS B N   1 
ATOM   1980 C CA  . LYS B 1 52  ? 23.505  -20.071 44.820  1.00 77.05 ? 54  LYS B CA  1 
ATOM   1981 C C   . LYS B 1 52  ? 22.688  -18.777 44.671  1.00 77.01 ? 54  LYS B C   1 
ATOM   1982 O O   . LYS B 1 52  ? 21.675  -18.607 45.347  1.00 76.93 ? 54  LYS B O   1 
ATOM   1983 C CB  . LYS B 1 52  ? 23.200  -21.031 43.662  1.00 79.47 ? 54  LYS B CB  1 
ATOM   1984 C CG  . LYS B 1 52  ? 23.891  -22.386 43.787  1.00 84.84 ? 54  LYS B CG  1 
ATOM   1985 C CD  . LYS B 1 52  ? 23.555  -23.305 42.622  1.00 91.12 ? 54  LYS B CD  1 
ATOM   1986 C CE  . LYS B 1 52  ? 24.383  -24.567 42.631  1.00 96.37 ? 54  LYS B CE  1 
ATOM   1987 N NZ  . LYS B 1 52  ? 24.216  -25.355 41.377  1.00 99.80 ? 54  LYS B NZ  1 
ATOM   1988 N N   . THR B 1 53  ? 23.119  -17.866 43.779  1.00 77.28 ? 55  THR B N   1 
ATOM   1989 C CA  . THR B 1 53  ? 22.356  -16.647 43.430  1.00 78.27 ? 55  THR B CA  1 
ATOM   1990 C C   . THR B 1 53  ? 21.169  -16.937 42.473  1.00 77.79 ? 55  THR B C   1 
ATOM   1991 O O   . THR B 1 53  ? 21.165  -17.979 41.817  1.00 77.47 ? 55  THR B O   1 
ATOM   1992 C CB  . THR B 1 53  ? 23.294  -15.595 42.789  1.00 81.14 ? 55  THR B CB  1 
ATOM   1993 O OG1 . THR B 1 53  ? 22.604  -14.337 42.711  1.00 83.33 ? 55  THR B OG1 1 
ATOM   1994 C CG2 . THR B 1 53  ? 23.770  -16.000 41.394  1.00 81.20 ? 55  THR B CG2 1 
ATOM   1995 N N   . TRP B 1 54  ? 20.165  -16.021 42.386  1.00 77.60 ? 56  TRP B N   1 
ATOM   1996 C CA  . TRP B 1 54  ? 18.991  -16.264 41.527  1.00 77.96 ? 56  TRP B CA  1 
ATOM   1997 C C   . TRP B 1 54  ? 19.327  -16.445 40.058  1.00 77.24 ? 56  TRP B C   1 
ATOM   1998 O O   . TRP B 1 54  ? 18.592  -17.155 39.372  1.00 77.21 ? 56  TRP B O   1 
ATOM   1999 C CB  . TRP B 1 54  ? 17.883  -15.192 41.667  1.00 78.51 ? 56  TRP B CB  1 
ATOM   2000 C CG  . TRP B 1 54  ? 18.206  -13.826 41.126  1.00 79.95 ? 56  TRP B CG  1 
ATOM   2001 C CD1 . TRP B 1 54  ? 18.598  -12.740 41.849  1.00 81.38 ? 56  TRP B CD1 1 
ATOM   2002 C CD2 . TRP B 1 54  ? 18.115  -13.385 39.759  1.00 80.57 ? 56  TRP B CD2 1 
ATOM   2003 N NE1 . TRP B 1 54  ? 18.783  -11.659 41.021  1.00 81.95 ? 56  TRP B NE1 1 
ATOM   2004 C CE2 . TRP B 1 54  ? 18.494  -12.027 39.732  1.00 81.62 ? 56  TRP B CE2 1 
ATOM   2005 C CE3 . TRP B 1 54  ? 17.745  -14.001 38.555  1.00 80.93 ? 56  TRP B CE3 1 
ATOM   2006 C CZ2 . TRP B 1 54  ? 18.532  -11.287 38.549  1.00 82.16 ? 56  TRP B CZ2 1 
ATOM   2007 C CZ3 . TRP B 1 54  ? 17.815  -13.275 37.389  1.00 81.73 ? 56  TRP B CZ3 1 
ATOM   2008 C CH2 . TRP B 1 54  ? 18.179  -11.926 37.396  1.00 82.04 ? 56  TRP B CH2 1 
ATOM   2009 N N   . GLN B 1 55  ? 20.403  -15.809 39.556  1.00 76.62 ? 57  GLN B N   1 
ATOM   2010 C CA  . GLN B 1 55  ? 20.776  -15.970 38.148  1.00 76.19 ? 57  GLN B CA  1 
ATOM   2011 C C   . GLN B 1 55  ? 21.340  -17.366 37.903  1.00 74.03 ? 57  GLN B C   1 
ATOM   2012 O O   . GLN B 1 55  ? 21.139  -17.913 36.818  1.00 74.32 ? 57  GLN B O   1 
ATOM   2013 C CB  . GLN B 1 55  ? 21.798  -14.915 37.679  1.00 79.76 ? 57  GLN B CB  1 
ATOM   2014 C CG  . GLN B 1 55  ? 21.430  -13.446 37.968  1.00 85.82 ? 57  GLN B CG  1 
ATOM   2015 C CD  . GLN B 1 55  ? 22.396  -12.463 37.315  1.00 92.48 ? 57  GLN B CD  1 
ATOM   2016 O OE1 . GLN B 1 55  ? 23.249  -12.826 36.479  1.00 94.83 ? 57  GLN B OE1 1 
ATOM   2017 N NE2 . GLN B 1 55  ? 22.282  -11.187 37.680  1.00 92.86 ? 57  GLN B NE2 1 
ATOM   2018 N N   . ALA B 1 56  ? 22.055  -17.944 38.895  1.00 71.51 ? 58  ALA B N   1 
ATOM   2019 C CA  . ALA B 1 56  ? 22.557  -19.303 38.764  1.00 69.26 ? 58  ALA B CA  1 
ATOM   2020 C C   . ALA B 1 56  ? 21.471  -20.349 38.880  1.00 65.78 ? 58  ALA B C   1 
ATOM   2021 O O   . ALA B 1 56  ? 21.576  -21.385 38.240  1.00 65.96 ? 58  ALA B O   1 
ATOM   2022 C CB  . ALA B 1 56  ? 23.626  -19.568 39.808  1.00 69.83 ? 58  ALA B CB  1 
ATOM   2023 N N   . ASN B 1 57  ? 20.430  -20.096 39.699  1.00 62.61 ? 59  ASN B N   1 
ATOM   2024 C CA  . ASN B 1 57  ? 19.331  -21.040 39.955  1.00 59.08 ? 59  ASN B CA  1 
ATOM   2025 C C   . ASN B 1 57  ? 18.302  -21.164 38.821  1.00 56.54 ? 59  ASN B C   1 
ATOM   2026 O O   . ASN B 1 57  ? 17.634  -22.190 38.704  1.00 55.92 ? 59  ASN B O   1 
ATOM   2027 C CB  . ASN B 1 57  ? 18.585  -20.619 41.212  1.00 58.65 ? 59  ASN B CB  1 
ATOM   2028 C CG  . ASN B 1 57  ? 19.250  -21.016 42.516  1.00 58.86 ? 59  ASN B CG  1 
ATOM   2029 O OD1 . ASN B 1 57  ? 19.871  -22.086 42.658  1.00 57.15 ? 59  ASN B OD1 1 
ATOM   2030 N ND2 . ASN B 1 57  ? 19.106  -20.147 43.506  1.00 58.48 ? 59  ASN B ND2 1 
ATOM   2031 N N   . LEU B 1 58  ? 18.164  -20.110 38.026  1.00 54.97 ? 60  LEU B N   1 
ATOM   2032 C CA  . LEU B 1 58  ? 17.226  -20.046 36.927  1.00 54.58 ? 60  LEU B CA  1 
ATOM   2033 C C   . LEU B 1 58  ? 17.954  -20.521 35.718  1.00 53.93 ? 60  LEU B C   1 
ATOM   2034 O O   . LEU B 1 58  ? 18.972  -19.940 35.356  1.00 56.53 ? 60  LEU B O   1 
ATOM   2035 C CB  . LEU B 1 58  ? 16.727  -18.614 36.724  1.00 55.13 ? 60  LEU B CB  1 
ATOM   2036 C CG  . LEU B 1 58  ? 15.783  -18.390 35.508  1.00 56.63 ? 60  LEU B CG  1 
ATOM   2037 C CD1 . LEU B 1 58  ? 14.491  -19.223 35.607  1.00 56.75 ? 60  LEU B CD1 1 
ATOM   2038 C CD2 . LEU B 1 58  ? 15.444  -16.909 35.348  1.00 57.39 ? 60  LEU B CD2 1 
ATOM   2039 N N   . ARG B 1 59  ? 17.467  -21.575 35.083  1.00 50.27 ? 61  ARG B N   1 
ATOM   2040 C CA  . ARG B 1 59  ? 18.158  -22.198 33.969  1.00 48.98 ? 61  ARG B CA  1 
ATOM   2041 C C   . ARG B 1 59  ? 17.239  -22.211 32.747  1.00 44.51 ? 61  ARG B C   1 
ATOM   2042 O O   . ARG B 1 59  ? 16.088  -22.606 32.856  1.00 41.17 ? 61  ARG B O   1 
ATOM   2043 C CB  . ARG B 1 59  ? 18.602  -23.639 34.339  1.00 52.87 ? 61  ARG B CB  1 
ATOM   2044 C CG  . ARG B 1 59  ? 19.694  -23.691 35.435  1.00 61.72 ? 61  ARG B CG  1 
ATOM   2045 C CD  . ARG B 1 59  ? 19.849  -25.103 36.017  1.00 70.55 ? 61  ARG B CD  1 
ATOM   2046 N NE  . ARG B 1 59  ? 20.728  -25.149 37.197  1.00 75.30 ? 61  ARG B NE  1 
ATOM   2047 C CZ  . ARG B 1 59  ? 20.355  -24.914 38.456  1.00 78.75 ? 61  ARG B CZ  1 
ATOM   2048 N NH1 . ARG B 1 59  ? 21.243  -24.988 39.443  1.00 79.35 ? 61  ARG B NH1 1 
ATOM   2049 N NH2 . ARG B 1 59  ? 19.090  -24.602 38.739  1.00 79.02 ? 61  ARG B NH2 1 
ATOM   2050 N N   . LEU B 1 60  ? 17.740  -21.781 31.600  1.00 44.94 ? 62  LEU B N   1 
ATOM   2051 C CA  . LEU B 1 60  ? 17.063  -22.004 30.336  1.00 44.88 ? 62  LEU B CA  1 
ATOM   2052 C C   . LEU B 1 60  ? 17.348  -23.428 29.894  1.00 45.96 ? 62  LEU B C   1 
ATOM   2053 O O   . LEU B 1 60  ? 18.510  -23.770 29.657  1.00 48.46 ? 62  LEU B O   1 
ATOM   2054 C CB  . LEU B 1 60  ? 17.561  -21.021 29.263  1.00 45.38 ? 62  LEU B CB  1 
ATOM   2055 C CG  . LEU B 1 60  ? 17.092  -21.333 27.833  1.00 45.72 ? 62  LEU B CG  1 
ATOM   2056 C CD1 . LEU B 1 60  ? 15.681  -21.014 27.683  1.00 44.56 ? 62  LEU B CD1 1 
ATOM   2057 C CD2 . LEU B 1 60  ? 17.910  -20.581 26.824  1.00 48.02 ? 62  LEU B CD2 1 
ATOM   2058 N N   . ILE B 1 61  ? 16.317  -24.251 29.732  1.00 43.00 ? 63  ILE B N   1 
ATOM   2059 C CA  . ILE B 1 61  ? 16.473  -25.625 29.270  1.00 42.24 ? 63  ILE B CA  1 
ATOM   2060 C C   . ILE B 1 61  ? 16.589  -25.670 27.759  1.00 42.89 ? 63  ILE B C   1 
ATOM   2061 O O   . ILE B 1 61  ? 17.537  -26.268 27.224  1.00 44.24 ? 63  ILE B O   1 
ATOM   2062 C CB  . ILE B 1 61  ? 15.311  -26.529 29.781  1.00 41.57 ? 63  ILE B CB  1 
ATOM   2063 C CG1 . ILE B 1 61  ? 15.220  -26.485 31.291  1.00 44.09 ? 63  ILE B CG1 1 
ATOM   2064 C CG2 . ILE B 1 61  ? 15.461  -27.966 29.239  1.00 41.22 ? 63  ILE B CG2 1 
ATOM   2065 C CD1 . ILE B 1 61  ? 16.529  -26.675 32.034  1.00 47.96 ? 63  ILE B CD1 1 
ATOM   2066 N N   . SER B 1 62  ? 15.652  -25.012 27.050  1.00 41.08 ? 64  SER B N   1 
ATOM   2067 C CA  . SER B 1 62  ? 15.565  -25.187 25.608  1.00 40.58 ? 64  SER B CA  1 
ATOM   2068 C C   . SER B 1 62  ? 14.594  -24.201 24.989  1.00 38.19 ? 64  SER B C   1 
ATOM   2069 O O   . SER B 1 62  ? 13.741  -23.617 25.673  1.00 36.12 ? 64  SER B O   1 
ATOM   2070 C CB  . SER B 1 62  ? 15.175  -26.626 25.288  1.00 43.47 ? 64  SER B CB  1 
ATOM   2071 O OG  . SER B 1 62  ? 15.240  -26.867 23.890  1.00 51.09 ? 64  SER B OG  1 
ATOM   2072 N N   . LYS B 1 63  ? 14.723  -24.014 23.702  1.00 36.29 ? 65  LYS B N   1 
ATOM   2073 C CA  . LYS B 1 63  ? 13.840  -23.157 22.905  1.00 36.42 ? 65  LYS B CA  1 
ATOM   2074 C C   . LYS B 1 63  ? 13.347  -23.949 21.723  1.00 36.37 ? 65  LYS B C   1 
ATOM   2075 O O   . LYS B 1 63  ? 14.054  -24.844 21.235  1.00 36.86 ? 65  LYS B O   1 
ATOM   2076 C CB  . LYS B 1 63  ? 14.509  -21.842 22.458  1.00 36.32 ? 65  LYS B CB  1 
ATOM   2077 C CG  . LYS B 1 63  ? 15.036  -21.010 23.599  1.00 35.78 ? 65  LYS B CG  1 
ATOM   2078 C CD  . LYS B 1 63  ? 15.486  -19.653 23.147  1.00 39.36 ? 65  LYS B CD  1 
ATOM   2079 C CE  . LYS B 1 63  ? 15.941  -18.706 24.229  1.00 40.51 ? 65  LYS B CE  1 
ATOM   2080 N NZ  . LYS B 1 63  ? 16.307  -17.338 23.671  1.00 40.01 ? 65  LYS B NZ  1 
ATOM   2081 N N   . PHE B 1 64  ? 12.157  -23.617 21.239  1.00 35.42 ? 66  PHE B N   1 
ATOM   2082 C CA  . PHE B 1 64  ? 11.562  -24.301 20.112  1.00 36.19 ? 66  PHE B CA  1 
ATOM   2083 C C   . PHE B 1 64  ? 10.560  -23.416 19.444  1.00 37.46 ? 66  PHE B C   1 
ATOM   2084 O O   . PHE B 1 64  ? 10.024  -22.473 20.053  1.00 36.60 ? 66  PHE B O   1 
ATOM   2085 C CB  . PHE B 1 64  ? 10.954  -25.679 20.491  1.00 35.80 ? 66  PHE B CB  1 
ATOM   2086 C CG  . PHE B 1 64  ? 9.820   -25.534 21.500  1.00 34.32 ? 66  PHE B CG  1 
ATOM   2087 C CD1 . PHE B 1 64  ? 8.523   -25.307 21.082  1.00 34.27 ? 66  PHE B CD1 1 
ATOM   2088 C CD2 . PHE B 1 64  ? 10.081  -25.511 22.855  1.00 35.38 ? 66  PHE B CD2 1 
ATOM   2089 C CE1 . PHE B 1 64  ? 7.500   -25.081 22.030  1.00 34.35 ? 66  PHE B CE1 1 
ATOM   2090 C CE2 . PHE B 1 64  ? 9.061   -25.330 23.777  1.00 34.48 ? 66  PHE B CE2 1 
ATOM   2091 C CZ  . PHE B 1 64  ? 7.785   -25.130 23.349  1.00 33.64 ? 66  PHE B CZ  1 
ATOM   2092 N N   . ASP B 1 65  ? 10.300  -23.702 18.175  1.00 39.22 ? 67  ASP B N   1 
ATOM   2093 C CA  . ASP B 1 65  ? 9.333   -22.963 17.391  1.00 39.53 ? 67  ASP B CA  1 
ATOM   2094 C C   . ASP B 1 65  ? 8.586   -23.804 16.370  1.00 40.06 ? 67  ASP B C   1 
ATOM   2095 O O   . ASP B 1 65  ? 8.072   -23.254 15.396  1.00 40.79 ? 67  ASP B O   1 
ATOM   2096 C CB  . ASP B 1 65  ? 10.017  -21.756 16.737  1.00 44.70 ? 67  ASP B CB  1 
ATOM   2097 C CG  . ASP B 1 65  ? 11.196  -22.150 15.843  1.00 54.60 ? 67  ASP B CG  1 
ATOM   2098 O OD1 . ASP B 1 65  ? 11.308  -23.311 15.497  1.00 59.80 ? 67  ASP B OD1 1 
ATOM   2099 O OD2 . ASP B 1 65  ? 11.994  -21.289 15.525  1.00 62.32 ? 67  ASP B OD2 1 
ATOM   2100 N N   . THR B 1 66  ? 8.503   -25.108 16.583  1.00 39.73 ? 68  THR B N   1 
ATOM   2101 C CA  . THR B 1 66  ? 7.642   -25.998 15.826  1.00 40.37 ? 68  THR B CA  1 
ATOM   2102 C C   . THR B 1 66  ? 6.957   -26.969 16.778  1.00 38.84 ? 68  THR B C   1 
ATOM   2103 O O   . THR B 1 66  ? 7.454   -27.229 17.861  1.00 38.09 ? 68  THR B O   1 
ATOM   2104 C CB  . THR B 1 66  ? 8.420   -26.808 14.743  1.00 42.11 ? 68  THR B CB  1 
ATOM   2105 O OG1 . THR B 1 66  ? 9.176   -27.831 15.343  1.00 45.75 ? 68  THR B OG1 1 
ATOM   2106 C CG2 . THR B 1 66  ? 9.267   -25.965 13.844  1.00 42.12 ? 68  THR B CG2 1 
ATOM   2107 N N   . VAL B 1 67  ? 5.849   -27.515 16.343  1.00 40.77 ? 69  VAL B N   1 
ATOM   2108 C CA  . VAL B 1 67  ? 5.089   -28.534 17.067  1.00 40.72 ? 69  VAL B CA  1 
ATOM   2109 C C   . VAL B 1 67  ? 5.913   -29.752 17.359  1.00 41.24 ? 69  VAL B C   1 
ATOM   2110 O O   . VAL B 1 67  ? 5.881   -30.302 18.483  1.00 40.79 ? 69  VAL B O   1 
ATOM   2111 C CB  . VAL B 1 67  ? 3.816   -28.913 16.297  1.00 41.64 ? 69  VAL B CB  1 
ATOM   2112 C CG1 . VAL B 1 67  ? 3.039   -29.958 17.064  1.00 42.83 ? 69  VAL B CG1 1 
ATOM   2113 C CG2 . VAL B 1 67  ? 2.968   -27.694 15.995  1.00 40.53 ? 69  VAL B CG2 1 
ATOM   2114 N N   . GLU B 1 68  ? 6.666   -30.248 16.341  1.00 40.44 ? 70  GLU B N   1 
ATOM   2115 C CA  . GLU B 1 68  ? 7.440   -31.468 16.534  1.00 41.29 ? 70  GLU B CA  1 
ATOM   2116 C C   . GLU B 1 68  ? 8.583   -31.287 17.522  1.00 39.93 ? 70  GLU B C   1 
ATOM   2117 O O   . GLU B 1 68  ? 8.872   -32.194 18.289  1.00 41.45 ? 70  GLU B O   1 
ATOM   2118 C CB  . GLU B 1 68  ? 7.953   -32.011 15.186  1.00 46.00 ? 70  GLU B CB  1 
ATOM   2119 C CG  . GLU B 1 68  ? 6.819   -32.514 14.278  1.00 51.37 ? 70  GLU B CG  1 
ATOM   2120 C CD  . GLU B 1 68  ? 5.976   -31.470 13.575  1.00 56.09 ? 70  GLU B CD  1 
ATOM   2121 O OE1 . GLU B 1 68  ? 6.351   -30.272 13.584  1.00 54.25 ? 70  GLU B OE1 1 
ATOM   2122 O OE2 . GLU B 1 68  ? 4.927   -31.854 13.011  1.00 60.78 ? 70  GLU B OE2 1 
ATOM   2123 N N   . ASP B 1 69  ? 9.200   -30.127 17.537  1.00 39.44 ? 71  ASP B N   1 
ATOM   2124 C CA  . ASP B 1 69  ? 10.268  -29.829 18.494  1.00 39.08 ? 71  ASP B CA  1 
ATOM   2125 C C   . ASP B 1 69  ? 9.694   -29.668 19.908  1.00 38.01 ? 71  ASP B C   1 
ATOM   2126 O O   . ASP B 1 69  ? 10.334  -30.084 20.889  1.00 39.16 ? 71  ASP B O   1 
ATOM   2127 C CB  . ASP B 1 69  ? 11.048  -28.601 18.040  1.00 41.06 ? 71  ASP B CB  1 
ATOM   2128 C CG  . ASP B 1 69  ? 11.835  -28.849 16.738  1.00 49.30 ? 71  ASP B CG  1 
ATOM   2129 O OD1 . ASP B 1 69  ? 12.302  -29.996 16.533  1.00 49.58 ? 71  ASP B OD1 1 
ATOM   2130 O OD2 . ASP B 1 69  ? 11.974  -27.898 15.937  1.00 54.69 ? 71  ASP B OD2 1 
ATOM   2131 N N   . PHE B 1 70  ? 8.486   -29.098 20.024  1.00 36.85 ? 72  PHE B N   1 
ATOM   2132 C CA  . PHE B 1 70  ? 7.730   -29.093 21.322  1.00 36.60 ? 72  PHE B CA  1 
ATOM   2133 C C   . PHE B 1 70  ? 7.606   -30.507 21.849  1.00 37.67 ? 72  PHE B C   1 
ATOM   2134 O O   . PHE B 1 70  ? 7.998   -30.791 22.978  1.00 38.22 ? 72  PHE B O   1 
ATOM   2135 C CB  . PHE B 1 70  ? 6.319   -28.458 21.173  1.00 35.17 ? 72  PHE B CB  1 
ATOM   2136 C CG  . PHE B 1 70  ? 5.454   -28.730 22.392  1.00 35.22 ? 72  PHE B CG  1 
ATOM   2137 C CD1 . PHE B 1 70  ? 5.696   -28.075 23.599  1.00 35.67 ? 72  PHE B CD1 1 
ATOM   2138 C CD2 . PHE B 1 70  ? 4.445   -29.669 22.347  1.00 35.26 ? 72  PHE B CD2 1 
ATOM   2139 C CE1 . PHE B 1 70  ? 4.937   -28.361 24.721  1.00 36.15 ? 72  PHE B CE1 1 
ATOM   2140 C CE2 . PHE B 1 70  ? 3.685   -29.955 23.469  1.00 35.91 ? 72  PHE B CE2 1 
ATOM   2141 C CZ  . PHE B 1 70  ? 3.960   -29.320 24.661  1.00 37.04 ? 72  PHE B CZ  1 
ATOM   2142 N N   . TRP B 1 71  ? 7.039   -31.400 21.032  1.00 38.46 ? 73  TRP B N   1 
ATOM   2143 C CA  . TRP B 1 71  ? 6.819   -32.763 21.463  1.00 38.53 ? 73  TRP B CA  1 
ATOM   2144 C C   . TRP B 1 71  ? 8.107   -33.542 21.806  1.00 39.47 ? 73  TRP B C   1 
ATOM   2145 O O   . TRP B 1 71  ? 8.092   -34.332 22.732  1.00 39.36 ? 73  TRP B O   1 
ATOM   2146 C CB  . TRP B 1 71  ? 5.970   -33.544 20.456  1.00 38.45 ? 73  TRP B CB  1 
ATOM   2147 C CG  . TRP B 1 71  ? 4.525   -33.158 20.424  1.00 37.05 ? 73  TRP B CG  1 
ATOM   2148 C CD1 . TRP B 1 71  ? 3.828   -32.692 19.357  1.00 37.62 ? 73  TRP B CD1 1 
ATOM   2149 C CD2 . TRP B 1 71  ? 3.571   -33.298 21.497  1.00 35.94 ? 73  TRP B CD2 1 
ATOM   2150 N NE1 . TRP B 1 71  ? 2.525   -32.432 19.716  1.00 38.07 ? 73  TRP B NE1 1 
ATOM   2151 C CE2 . TRP B 1 71  ? 2.330   -32.840 21.011  1.00 36.83 ? 73  TRP B CE2 1 
ATOM   2152 C CE3 . TRP B 1 71  ? 3.669   -33.684 22.835  1.00 36.74 ? 73  TRP B CE3 1 
ATOM   2153 C CZ2 . TRP B 1 71  ? 1.192   -32.784 21.812  1.00 37.48 ? 73  TRP B CZ2 1 
ATOM   2154 C CZ3 . TRP B 1 71  ? 2.545   -33.621 23.629  1.00 36.43 ? 73  TRP B CZ3 1 
ATOM   2155 C CH2 . TRP B 1 71  ? 1.316   -33.216 23.107  1.00 35.94 ? 73  TRP B CH2 1 
ATOM   2156 N N   . ALA B 1 72  ? 9.205   -33.306 21.094  1.00 40.46 ? 74  ALA B N   1 
ATOM   2157 C CA  . ALA B 1 72  ? 10.489  -33.962 21.363  1.00 40.93 ? 74  ALA B CA  1 
ATOM   2158 C C   . ALA B 1 72  ? 11.029  -33.507 22.715  1.00 39.56 ? 74  ALA B C   1 
ATOM   2159 O O   . ALA B 1 72  ? 11.543  -34.314 23.503  1.00 39.71 ? 74  ALA B O   1 
ATOM   2160 C CB  . ALA B 1 72  ? 11.492  -33.625 20.257  1.00 42.52 ? 74  ALA B CB  1 
ATOM   2161 N N   . LEU B 1 73  ? 10.872  -32.206 23.025  1.00 38.15 ? 75  LEU B N   1 
ATOM   2162 C CA  . LEU B 1 73  ? 11.277  -31.686 24.317  1.00 37.14 ? 75  LEU B CA  1 
ATOM   2163 C C   . LEU B 1 73  ? 10.375  -32.201 25.432  1.00 35.74 ? 75  LEU B C   1 
ATOM   2164 O O   . LEU B 1 73  ? 10.867  -32.598 26.467  1.00 36.50 ? 75  LEU B O   1 
ATOM   2165 C CB  . LEU B 1 73  ? 11.254  -30.153 24.300  1.00 37.71 ? 75  LEU B CB  1 
ATOM   2166 C CG  . LEU B 1 73  ? 11.628  -29.452 25.603  1.00 38.60 ? 75  LEU B CG  1 
ATOM   2167 C CD1 . LEU B 1 73  ? 13.021  -29.840 26.081  1.00 39.98 ? 75  LEU B CD1 1 
ATOM   2168 C CD2 . LEU B 1 73  ? 11.567  -27.957 25.427  1.00 40.02 ? 75  LEU B CD2 1 
ATOM   2169 N N   . TYR B 1 74  ? 9.062   -32.163 25.230  1.00 36.37 ? 76  TYR B N   1 
ATOM   2170 C CA  . TYR B 1 74  ? 8.076   -32.637 26.198  1.00 38.32 ? 76  TYR B CA  1 
ATOM   2171 C C   . TYR B 1 74  ? 8.317   -34.100 26.553  1.00 40.00 ? 76  TYR B C   1 
ATOM   2172 O O   . TYR B 1 74  ? 8.366   -34.454 27.726  1.00 38.31 ? 76  TYR B O   1 
ATOM   2173 C CB  . TYR B 1 74  ? 6.641   -32.416 25.668  1.00 38.77 ? 76  TYR B CB  1 
ATOM   2174 C CG  . TYR B 1 74  ? 5.586   -32.830 26.669  1.00 38.49 ? 76  TYR B CG  1 
ATOM   2175 C CD1 . TYR B 1 74  ? 5.171   -31.966 27.665  1.00 37.95 ? 76  TYR B CD1 1 
ATOM   2176 C CD2 . TYR B 1 74  ? 5.018   -34.104 26.628  1.00 38.36 ? 76  TYR B CD2 1 
ATOM   2177 C CE1 . TYR B 1 74  ? 4.218   -32.353 28.599  1.00 38.40 ? 76  TYR B CE1 1 
ATOM   2178 C CE2 . TYR B 1 74  ? 4.066   -34.494 27.543  1.00 38.97 ? 76  TYR B CE2 1 
ATOM   2179 C CZ  . TYR B 1 74  ? 3.657   -33.615 28.525  1.00 40.43 ? 76  TYR B CZ  1 
ATOM   2180 O OH  . TYR B 1 74  ? 2.709   -34.006 29.456  1.00 42.62 ? 76  TYR B OH  1 
ATOM   2181 N N   . ASN B 1 75  ? 8.485   -34.928 25.544  1.00 42.22 ? 77  ASN B N   1 
ATOM   2182 C CA  . ASN B 1 75  ? 8.737   -36.368 25.754  1.00 45.75 ? 77  ASN B CA  1 
ATOM   2183 C C   . ASN B 1 75  ? 10.047  -36.639 26.538  1.00 49.06 ? 77  ASN B C   1 
ATOM   2184 O O   . ASN B 1 75  ? 10.091  -37.506 27.409  1.00 51.38 ? 77  ASN B O   1 
ATOM   2185 C CB  . ASN B 1 75  ? 8.689   -37.088 24.416  1.00 49.09 ? 77  ASN B CB  1 
ATOM   2186 C CG  . ASN B 1 75  ? 7.288   -37.082 23.770  1.00 55.81 ? 77  ASN B CG  1 
ATOM   2187 O OD1 . ASN B 1 75  ? 6.262   -37.084 24.433  1.00 57.99 ? 77  ASN B OD1 1 
ATOM   2188 N ND2 . ASN B 1 75  ? 7.192   -37.065 22.448  1.00 57.30 ? 77  ASN B ND2 1 
ATOM   2189 N N   . HIS B 1 76  ? 11.076  -35.873 26.273  1.00 49.28 ? 78  HIS B N   1 
ATOM   2190 C CA  . HIS B 1 76  ? 12.367  -35.992 26.930  1.00 50.91 ? 78  HIS B CA  1 
ATOM   2191 C C   . HIS B 1 76  ? 12.349  -35.558 28.391  1.00 50.86 ? 78  HIS B C   1 
ATOM   2192 O O   . HIS B 1 76  ? 12.972  -36.215 29.223  1.00 52.66 ? 78  HIS B O   1 
ATOM   2193 C CB  . HIS B 1 76  ? 13.416  -35.187 26.154  1.00 53.38 ? 78  HIS B CB  1 
ATOM   2194 C CG  . HIS B 1 76  ? 14.745  -35.092 26.818  1.00 60.54 ? 78  HIS B CG  1 
ATOM   2195 N ND1 . HIS B 1 76  ? 15.203  -33.897 27.336  1.00 63.74 ? 78  HIS B ND1 1 
ATOM   2196 C CD2 . HIS B 1 76  ? 15.681  -36.047 27.022  1.00 63.36 ? 78  HIS B CD2 1 
ATOM   2197 C CE1 . HIS B 1 76  ? 16.394  -34.160 27.854  1.00 65.37 ? 78  HIS B CE1 1 
ATOM   2198 N NE2 . HIS B 1 76  ? 16.722  -35.443 27.686  1.00 65.64 ? 78  HIS B NE2 1 
ATOM   2199 N N   . ILE B 1 77  ? 11.664  -34.464 28.702  1.00 49.33 ? 79  ILE B N   1 
ATOM   2200 C CA  . ILE B 1 77  ? 11.581  -33.975 30.077  1.00 50.10 ? 79  ILE B CA  1 
ATOM   2201 C C   . ILE B 1 77  ? 10.717  -34.915 30.882  1.00 51.95 ? 79  ILE B C   1 
ATOM   2202 O O   . ILE B 1 77  ? 11.023  -35.147 32.042  1.00 52.37 ? 79  ILE B O   1 
ATOM   2203 C CB  . ILE B 1 77  ? 10.986  -32.528 30.158  1.00 49.68 ? 79  ILE B CB  1 
ATOM   2204 C CG1 . ILE B 1 77  ? 11.820  -31.506 29.351  1.00 50.09 ? 79  ILE B CG1 1 
ATOM   2205 C CG2 . ILE B 1 77  ? 10.889  -32.077 31.605  1.00 50.39 ? 79  ILE B CG2 1 
ATOM   2206 C CD1 . ILE B 1 77  ? 13.222  -31.401 29.670  1.00 50.95 ? 79  ILE B CD1 1 
ATOM   2207 N N   . GLN B 1 78  ? 9.632   -35.422 30.285  1.00 54.42 ? 80  GLN B N   1 
ATOM   2208 C CA  . GLN B 1 78  ? 8.727   -36.374 30.934  1.00 58.87 ? 80  GLN B CA  1 
ATOM   2209 C C   . GLN B 1 78  ? 9.489   -37.665 31.333  1.00 63.48 ? 80  GLN B C   1 
ATOM   2210 O O   . GLN B 1 78  ? 9.169   -38.240 32.361  1.00 63.47 ? 80  GLN B O   1 
ATOM   2211 C CB  . GLN B 1 78  ? 7.485   -36.685 30.035  1.00 59.94 ? 80  GLN B CB  1 
ATOM   2212 C CG  . GLN B 1 78  ? 6.158   -36.779 30.816  1.00 63.11 ? 80  GLN B CG  1 
ATOM   2213 C CD  . GLN B 1 78  ? 4.889   -37.074 30.039  1.00 65.27 ? 80  GLN B CD  1 
ATOM   2214 O OE1 . GLN B 1 78  ? 3.784   -36.744 30.511  1.00 67.69 ? 80  GLN B OE1 1 
ATOM   2215 N NE2 . GLN B 1 78  ? 4.955   -37.677 28.853  1.00 62.18 ? 80  GLN B NE2 1 
ATOM   2216 N N   . LEU B 1 79  ? 10.489  -38.099 30.522  1.00 67.61 ? 81  LEU B N   1 
ATOM   2217 C CA  . LEU B 1 79  ? 11.465  -39.163 30.846  1.00 71.26 ? 81  LEU B CA  1 
ATOM   2218 C C   . LEU B 1 79  ? 12.699  -38.606 31.629  1.00 74.87 ? 81  LEU B C   1 
ATOM   2219 O O   . LEU B 1 79  ? 13.853  -38.788 31.220  1.00 75.60 ? 81  LEU B O   1 
ATOM   2220 C CB  . LEU B 1 79  ? 11.976  -39.844 29.543  1.00 72.47 ? 81  LEU B CB  1 
ATOM   2221 C CG  . LEU B 1 79  ? 11.078  -40.849 28.836  1.00 74.79 ? 81  LEU B CG  1 
ATOM   2222 C CD1 . LEU B 1 79  ? 11.795  -41.443 27.610  1.00 75.13 ? 81  LEU B CD1 1 
ATOM   2223 C CD2 . LEU B 1 79  ? 10.673  -41.985 29.765  1.00 75.62 ? 81  LEU B CD2 1 
ATOM   2224 N N   . SER B 1 80  ? 12.462  -37.916 32.738  1.00 76.85 ? 82  SER B N   1 
ATOM   2225 C CA  . SER B 1 80  ? 13.552  -37.424 33.592  1.00 78.73 ? 82  SER B CA  1 
ATOM   2226 C C   . SER B 1 80  ? 13.038  -37.118 34.996  1.00 80.51 ? 82  SER B C   1 
ATOM   2227 O O   . SER B 1 80  ? 13.519  -36.176 35.634  1.00 81.86 ? 82  SER B O   1 
ATOM   2228 C CB  . SER B 1 80  ? 14.195  -36.180 32.981  1.00 79.85 ? 82  SER B CB  1 
ATOM   2229 O OG  . SER B 1 80  ? 14.696  -36.397 31.670  1.00 81.77 ? 82  SER B OG  1 
ATOM   2230 N N   . SER B 1 81  ? 12.065  -37.915 35.496  1.00 80.26 ? 83  SER B N   1 
ATOM   2231 C CA  . SER B 1 81  ? 11.440  -37.690 36.801  1.00 80.16 ? 83  SER B CA  1 
ATOM   2232 C C   . SER B 1 81  ? 10.901  -36.237 36.934  1.00 79.28 ? 83  SER B C   1 
ATOM   2233 O O   . SER B 1 81  ? 10.974  -35.630 38.015  1.00 79.84 ? 83  SER B O   1 
ATOM   2234 C CB  . SER B 1 81  ? 12.422  -38.026 37.919  1.00 81.82 ? 83  SER B CB  1 
ATOM   2235 O OG  . SER B 1 81  ? 12.875  -39.370 37.839  1.00 84.48 ? 83  SER B OG  1 
ATOM   2236 N N   . ASN B 1 82  ? 10.369  -35.713 35.796  1.00 77.43 ? 84  ASN B N   1 
ATOM   2237 C CA  . ASN B 1 82  ? 9.748   -34.387 35.588  1.00 76.18 ? 84  ASN B CA  1 
ATOM   2238 C C   . ASN B 1 82  ? 8.850   -33.871 36.712  1.00 74.98 ? 84  ASN B C   1 
ATOM   2239 O O   . ASN B 1 82  ? 8.286   -34.655 37.473  1.00 75.86 ? 84  ASN B O   1 
ATOM   2240 C CB  . ASN B 1 82  ? 8.876   -34.430 34.328  1.00 76.90 ? 84  ASN B CB  1 
ATOM   2241 C CG  . ASN B 1 82  ? 7.622   -35.290 34.480  1.00 78.05 ? 84  ASN B CG  1 
ATOM   2242 O OD1 . ASN B 1 82  ? 7.683   -36.435 34.942  1.00 79.88 ? 84  ASN B OD1 1 
ATOM   2243 N ND2 . ASN B 1 82  ? 6.464   -34.771 34.116  1.00 76.72 ? 84  ASN B ND2 1 
ATOM   2244 N N   . LEU B 1 83  ? 8.696   -32.541 36.801  1.00 73.18 ? 85  LEU B N   1 
ATOM   2245 C CA  . LEU B 1 83  ? 7.836   -31.899 37.794  1.00 71.63 ? 85  LEU B CA  1 
ATOM   2246 C C   . LEU B 1 83  ? 8.294   -32.291 39.202  1.00 71.74 ? 85  LEU B C   1 
ATOM   2247 O O   . LEU B 1 83  ? 7.554   -32.924 39.946  1.00 71.36 ? 85  LEU B O   1 
ATOM   2248 C CB  . LEU B 1 83  ? 6.330   -32.196 37.534  1.00 70.00 ? 85  LEU B CB  1 
ATOM   2249 C CG  . LEU B 1 83  ? 5.786   -31.671 36.190  1.00 68.74 ? 85  LEU B CG  1 
ATOM   2250 C CD1 . LEU B 1 83  ? 4.347   -31.952 36.039  1.00 68.28 ? 85  LEU B CD1 1 
ATOM   2251 C CD2 . LEU B 1 83  ? 6.002   -30.162 36.019  1.00 68.73 ? 85  LEU B CD2 1 
ATOM   2252 N N   . MET B 1 84  ? 9.545   -31.902 39.529  1.00 72.16 ? 86  MET B N   1 
ATOM   2253 C CA  . MET B 1 84  ? 10.233  -32.232 40.786  1.00 73.30 ? 86  MET B CA  1 
ATOM   2254 C C   . MET B 1 84  ? 9.706   -31.403 41.983  1.00 73.77 ? 86  MET B C   1 
ATOM   2255 O O   . MET B 1 84  ? 9.142   -30.329 41.776  1.00 74.58 ? 86  MET B O   1 
ATOM   2256 C CB  . MET B 1 84  ? 11.746  -32.028 40.611  1.00 74.93 ? 86  MET B CB  1 
ATOM   2257 C CG  . MET B 1 84  ? 12.365  -32.965 39.580  1.00 79.66 ? 86  MET B CG  1 
ATOM   2258 S SD  . MET B 1 84  ? 14.100  -33.383 39.958  1.00 87.73 ? 86  MET B SD  1 
ATOM   2259 C CE  . MET B 1 84  ? 14.935  -32.733 38.451  1.00 84.23 ? 86  MET B CE  1 
ATOM   2260 N N   . PRO B 1 85  ? 9.921   -31.848 43.237  1.00 72.91 ? 87  PRO B N   1 
ATOM   2261 C CA  . PRO B 1 85  ? 8.975   -31.510 44.314  1.00 72.28 ? 87  PRO B CA  1 
ATOM   2262 C C   . PRO B 1 85  ? 9.103   -30.161 45.018  1.00 70.01 ? 87  PRO B C   1 
ATOM   2263 O O   . PRO B 1 85  ? 8.322   -29.914 45.951  1.00 71.04 ? 87  PRO B O   1 
ATOM   2264 C CB  . PRO B 1 85  ? 9.183   -32.636 45.330  1.00 73.61 ? 87  PRO B CB  1 
ATOM   2265 C CG  . PRO B 1 85  ? 10.612  -33.107 45.109  1.00 74.63 ? 87  PRO B CG  1 
ATOM   2266 C CD  . PRO B 1 85  ? 11.051  -32.662 43.739  1.00 72.87 ? 87  PRO B CD  1 
ATOM   2267 N N   . GLY B 1 86  ? 10.052  -29.331 44.624  1.00 66.32 ? 88  GLY B N   1 
ATOM   2268 C CA  . GLY B 1 86  ? 10.088  -27.919 45.034  1.00 63.66 ? 88  GLY B CA  1 
ATOM   2269 C C   . GLY B 1 86  ? 10.597  -27.027 43.900  1.00 61.12 ? 88  GLY B C   1 
ATOM   2270 O O   . GLY B 1 86  ? 11.291  -26.036 44.119  1.00 61.92 ? 88  GLY B O   1 
ATOM   2271 N N   . CYS B 1 87  ? 10.245  -27.372 42.676  1.00 57.86 ? 89  CYS B N   1 
ATOM   2272 C CA  . CYS B 1 87  ? 10.776  -26.726 41.504  1.00 54.81 ? 89  CYS B CA  1 
ATOM   2273 C C   . CYS B 1 87  ? 9.683   -25.997 40.735  1.00 49.55 ? 89  CYS B C   1 
ATOM   2274 O O   . CYS B 1 87  ? 8.481   -26.202 40.943  1.00 48.69 ? 89  CYS B O   1 
ATOM   2275 C CB  . CYS B 1 87  ? 11.463  -27.768 40.642  1.00 57.45 ? 89  CYS B CB  1 
ATOM   2276 S SG  . CYS B 1 87  ? 12.779  -28.665 41.505  1.00 65.33 ? 89  CYS B SG  1 
ATOM   2277 N N   . ASP B 1 88  ? 10.116  -25.125 39.858  1.00 45.49 ? 90  ASP B N   1 
ATOM   2278 C CA  . ASP B 1 88  ? 9.192   -24.433 38.991  1.00 43.12 ? 90  ASP B CA  1 
ATOM   2279 C C   . ASP B 1 88  ? 9.644   -24.644 37.566  1.00 40.21 ? 90  ASP B C   1 
ATOM   2280 O O   . ASP B 1 88  ? 10.857  -24.603 37.276  1.00 40.81 ? 90  ASP B O   1 
ATOM   2281 C CB  . ASP B 1 88  ? 9.209   -22.930 39.236  1.00 46.18 ? 90  ASP B CB  1 
ATOM   2282 C CG  . ASP B 1 88  ? 9.051   -22.451 40.657  1.00 57.29 ? 90  ASP B CG  1 
ATOM   2283 O OD1 . ASP B 1 88  ? 8.254   -23.074 41.427  1.00 53.59 ? 90  ASP B OD1 1 
ATOM   2284 O OD2 . ASP B 1 88  ? 9.691   -21.432 41.013  1.00 64.36 ? 90  ASP B OD2 1 
ATOM   2285 N N   . TYR B 1 89  ? 8.675   -24.831 36.684  1.00 37.37 ? 91  TYR B N   1 
ATOM   2286 C CA  . TYR B 1 89  ? 8.921   -24.883 35.265  1.00 36.23 ? 91  TYR B CA  1 
ATOM   2287 C C   . TYR B 1 89  ? 8.113   -23.779 34.650  1.00 35.00 ? 91  TYR B C   1 
ATOM   2288 O O   . TYR B 1 89  ? 6.967   -23.555 35.037  1.00 32.81 ? 91  TYR B O   1 
ATOM   2289 C CB  . TYR B 1 89  ? 8.498   -26.222 34.681  1.00 38.15 ? 91  TYR B CB  1 
ATOM   2290 C CG  . TYR B 1 89  ? 9.188   -27.376 35.377  1.00 44.65 ? 91  TYR B CG  1 
ATOM   2291 C CD1 . TYR B 1 89  ? 8.786   -27.790 36.639  1.00 48.64 ? 91  TYR B CD1 1 
ATOM   2292 C CD2 . TYR B 1 89  ? 10.262  -28.026 34.789  1.00 47.74 ? 91  TYR B CD2 1 
ATOM   2293 C CE1 . TYR B 1 89  ? 9.444   -28.821 37.306  1.00 51.30 ? 91  TYR B CE1 1 
ATOM   2294 C CE2 . TYR B 1 89  ? 10.905  -29.086 35.437  1.00 50.10 ? 91  TYR B CE2 1 
ATOM   2295 C CZ  . TYR B 1 89  ? 10.500  -29.466 36.696  1.00 53.17 ? 91  TYR B CZ  1 
ATOM   2296 O OH  . TYR B 1 89  ? 11.132  -30.498 37.366  1.00 58.86 ? 91  TYR B OH  1 
ATOM   2297 N N   . SER B 1 90  ? 8.720   -23.099 33.689  1.00 32.82 ? 92  SER B N   1 
ATOM   2298 C CA  . SER B 1 90  ? 8.051   -21.984 33.032  1.00 32.93 ? 92  SER B CA  1 
ATOM   2299 C C   . SER B 1 90  ? 8.199   -22.071 31.527  1.00 32.96 ? 92  SER B C   1 
ATOM   2300 O O   . SER B 1 90  ? 9.302   -22.323 31.080  1.00 35.80 ? 92  SER B O   1 
ATOM   2301 C CB  . SER B 1 90  ? 8.640   -20.661 33.544  1.00 34.10 ? 92  SER B CB  1 
ATOM   2302 O OG  . SER B 1 90  ? 8.671   -20.527 34.964  1.00 38.73 ? 92  SER B OG  1 
ATOM   2303 N N   . LEU B 1 91  ? 7.142   -21.845 30.735  1.00 31.35 ? 93  LEU B N   1 
ATOM   2304 C CA  . LEU B 1 91  ? 7.267   -21.716 29.281  1.00 30.86 ? 93  LEU B CA  1 
ATOM   2305 C C   . LEU B 1 91  ? 6.889   -20.282 28.915  1.00 30.21 ? 93  LEU B C   1 
ATOM   2306 O O   . LEU B 1 91  ? 5.731   -19.901 29.121  1.00 29.45 ? 93  LEU B O   1 
ATOM   2307 C CB  . LEU B 1 91  ? 6.355   -22.708 28.535  1.00 31.38 ? 93  LEU B CB  1 
ATOM   2308 C CG  . LEU B 1 91  ? 6.590   -22.722 27.002  1.00 31.92 ? 93  LEU B CG  1 
ATOM   2309 C CD1 . LEU B 1 91  ? 7.837   -23.494 26.665  1.00 34.01 ? 93  LEU B CD1 1 
ATOM   2310 C CD2 . LEU B 1 91  ? 5.440   -23.260 26.229  1.00 34.15 ? 93  LEU B CD2 1 
ATOM   2311 N N   . PHE B 1 92  ? 7.825   -19.506 28.364  1.00 30.53 ? 94  PHE B N   1 
ATOM   2312 C CA  . PHE B 1 92  ? 7.600   -18.113 28.024  1.00 29.44 ? 94  PHE B CA  1 
ATOM   2313 C C   . PHE B 1 92  ? 7.987   -17.843 26.604  1.00 31.30 ? 94  PHE B C   1 
ATOM   2314 O O   . PHE B 1 92  ? 8.846   -18.492 26.027  1.00 30.18 ? 94  PHE B O   1 
ATOM   2315 C CB  . PHE B 1 92  ? 8.398   -17.194 28.979  1.00 28.83 ? 94  PHE B CB  1 
ATOM   2316 C CG  . PHE B 1 92  ? 7.611   -16.902 30.248  1.00 31.37 ? 94  PHE B CG  1 
ATOM   2317 C CD1 . PHE B 1 92  ? 7.410   -17.880 31.190  1.00 34.65 ? 94  PHE B CD1 1 
ATOM   2318 C CD2 . PHE B 1 92  ? 7.057   -15.660 30.466  1.00 31.54 ? 94  PHE B CD2 1 
ATOM   2319 C CE1 . PHE B 1 92  ? 6.649   -17.623 32.338  1.00 35.66 ? 94  PHE B CE1 1 
ATOM   2320 C CE2 . PHE B 1 92  ? 6.288   -15.417 31.585  1.00 32.66 ? 94  PHE B CE2 1 
ATOM   2321 C CZ  . PHE B 1 92  ? 6.128   -16.385 32.539  1.00 34.04 ? 94  PHE B CZ  1 
ATOM   2322 N N   . LYS B 1 93  ? 7.326   -16.849 26.007  1.00 31.53 ? 95  LYS B N   1 
ATOM   2323 C CA  . LYS B 1 93  ? 7.695   -16.405 24.666  1.00 32.12 ? 95  LYS B CA  1 
ATOM   2324 C C   . LYS B 1 93  ? 9.156   -15.970 24.674  1.00 32.24 ? 95  LYS B C   1 
ATOM   2325 O O   . LYS B 1 93  ? 9.647   -15.404 25.643  1.00 33.17 ? 95  LYS B O   1 
ATOM   2326 C CB  . LYS B 1 93  ? 6.794   -15.278 24.218  1.00 33.58 ? 95  LYS B CB  1 
ATOM   2327 C CG  . LYS B 1 93  ? 5.377   -15.713 23.893  1.00 35.81 ? 95  LYS B CG  1 
ATOM   2328 C CD  . LYS B 1 93  ? 4.483   -14.593 23.588  1.00 35.11 ? 95  LYS B CD  1 
ATOM   2329 C CE  . LYS B 1 93  ? 3.146   -15.112 23.162  1.00 37.25 ? 95  LYS B CE  1 
ATOM   2330 N NZ  . LYS B 1 93  ? 2.194   -14.015 22.964  1.00 41.08 ? 95  LYS B NZ  1 
ATOM   2331 N N   . ASP B 1 94  ? 9.858   -16.259 23.599  1.00 33.38 ? 96  ASP B N   1 
ATOM   2332 C CA  . ASP B 1 94  ? 11.274  -15.907 23.465  1.00 35.56 ? 96  ASP B CA  1 
ATOM   2333 C C   . ASP B 1 94  ? 11.452  -14.388 23.711  1.00 37.74 ? 96  ASP B C   1 
ATOM   2334 O O   . ASP B 1 94  ? 10.685  -13.585 23.151  1.00 40.20 ? 96  ASP B O   1 
ATOM   2335 C CB  . ASP B 1 94  ? 11.731  -16.340 22.065  1.00 39.45 ? 96  ASP B CB  1 
ATOM   2336 C CG  . ASP B 1 94  ? 13.217  -16.383 21.825  1.00 44.40 ? 96  ASP B CG  1 
ATOM   2337 O OD1 . ASP B 1 94  ? 13.986  -16.343 22.821  1.00 41.96 ? 96  ASP B OD1 1 
ATOM   2338 O OD2 . ASP B 1 94  ? 13.609  -16.498 20.649  1.00 49.56 ? 96  ASP B OD2 1 
ATOM   2339 N N   . GLY B 1 95  ? 12.382  -14.035 24.580  1.00 37.79 ? 97  GLY B N   1 
ATOM   2340 C CA  . GLY B 1 95  ? 12.649  -12.657 24.918  1.00 39.80 ? 97  GLY B CA  1 
ATOM   2341 C C   . GLY B 1 95  ? 11.935  -12.140 26.157  1.00 40.60 ? 97  GLY B C   1 
ATOM   2342 O O   . GLY B 1 95  ? 12.095  -10.965 26.500  1.00 42.97 ? 97  GLY B O   1 
ATOM   2343 N N   . ILE B 1 96  ? 11.127  -12.981 26.836  1.00 39.82 ? 98  ILE B N   1 
ATOM   2344 C CA  . ILE B 1 96  ? 10.504  -12.660 28.106  1.00 39.22 ? 98  ILE B CA  1 
ATOM   2345 C C   . ILE B 1 96  ? 11.104  -13.592 29.169  1.00 41.71 ? 98  ILE B C   1 
ATOM   2346 O O   . ILE B 1 96  ? 10.969  -14.824 29.112  1.00 40.64 ? 98  ILE B O   1 
ATOM   2347 C CB  . ILE B 1 96  ? 8.979   -12.829 28.098  1.00 39.03 ? 98  ILE B CB  1 
ATOM   2348 C CG1 . ILE B 1 96  ? 8.313   -12.103 26.917  1.00 40.49 ? 98  ILE B CG1 1 
ATOM   2349 C CG2 . ILE B 1 96  ? 8.375   -12.427 29.449  1.00 39.06 ? 98  ILE B CG2 1 
ATOM   2350 C CD1 . ILE B 1 96  ? 6.789   -12.201 26.844  1.00 41.28 ? 98  ILE B CD1 1 
ATOM   2351 N N   . GLU B 1 97  ? 11.761  -13.002 30.162  1.00 43.02 ? 99  GLU B N   1 
ATOM   2352 C CA  . GLU B 1 97  ? 12.167  -13.762 31.341  1.00 45.93 ? 99  GLU B CA  1 
ATOM   2353 C C   . GLU B 1 97  ? 10.976  -14.128 32.223  1.00 44.45 ? 99  GLU B C   1 
ATOM   2354 O O   . GLU B 1 97  ? 10.027  -13.341 32.314  1.00 42.69 ? 99  GLU B O   1 
ATOM   2355 C CB  . GLU B 1 97  ? 13.243  -13.003 32.100  1.00 51.20 ? 99  GLU B CB  1 
ATOM   2356 C CG  . GLU B 1 97  ? 14.470  -12.798 31.240  1.00 62.77 ? 99  GLU B CG  1 
ATOM   2357 C CD  . GLU B 1 97  ? 15.731  -12.418 31.977  1.00 82.07 ? 99  GLU B CD  1 
ATOM   2358 O OE1 . GLU B 1 97  ? 15.628  -11.779 33.050  1.00 87.28 ? 99  GLU B OE1 1 
ATOM   2359 O OE2 . GLU B 1 97  ? 16.830  -12.755 31.478  1.00 89.27 ? 99  GLU B OE2 1 
ATOM   2360 N N   . PRO B 1 98  ? 10.975  -15.341 32.848  1.00 45.15 ? 100 PRO B N   1 
ATOM   2361 C CA  . PRO B 1 98  ? 9.840   -15.727 33.700  1.00 45.81 ? 100 PRO B CA  1 
ATOM   2362 C C   . PRO B 1 98  ? 9.929   -15.104 35.071  1.00 45.36 ? 100 PRO B C   1 
ATOM   2363 O O   . PRO B 1 98  ? 9.811   -15.793 36.062  1.00 46.83 ? 100 PRO B O   1 
ATOM   2364 C CB  . PRO B 1 98  ? 9.954   -17.265 33.751  1.00 46.99 ? 100 PRO B CB  1 
ATOM   2365 C CG  . PRO B 1 98  ? 11.434  -17.495 33.689  1.00 47.10 ? 100 PRO B CG  1 
ATOM   2366 C CD  . PRO B 1 98  ? 11.974  -16.428 32.769  1.00 46.10 ? 100 PRO B CD  1 
ATOM   2367 N N   . MET B 1 99  ? 10.152  -13.782 35.114  1.00 44.78 ? 101 MET B N   1 
ATOM   2368 C CA  . MET B 1 99  ? 10.172  -13.043 36.368  1.00 45.01 ? 101 MET B CA  1 
ATOM   2369 C C   . MET B 1 99  ? 9.275   -11.802 36.174  1.00 43.44 ? 101 MET B C   1 
ATOM   2370 O O   . MET B 1 99  ? 9.250   -11.188 35.084  1.00 40.58 ? 101 MET B O   1 
ATOM   2371 C CB  . MET B 1 99  ? 11.600  -12.678 36.762  1.00 48.65 ? 101 MET B CB  1 
ATOM   2372 C CG  . MET B 1 99  ? 12.287  -11.753 35.813  1.00 57.82 ? 101 MET B CG  1 
ATOM   2373 S SD  . MET B 1 99  ? 14.070  -11.597 36.175  1.00 82.59 ? 101 MET B SD  1 
ATOM   2374 C CE  . MET B 1 99  ? 14.628  -13.323 35.814  1.00 78.56 ? 101 MET B CE  1 
ATOM   2375 N N   . TRP B 1 100 ? 8.547   -11.444 37.224  1.00 45.43 ? 102 TRP B N   1 
ATOM   2376 C CA  . TRP B 1 100 ? 7.498   -10.445 37.079  1.00 48.48 ? 102 TRP B CA  1 
ATOM   2377 C C   . TRP B 1 100 ? 8.091   -9.082  36.758  1.00 48.21 ? 102 TRP B C   1 
ATOM   2378 O O   . TRP B 1 100 ? 7.373   -8.287  36.176  1.00 48.88 ? 102 TRP B O   1 
ATOM   2379 C CB  . TRP B 1 100 ? 6.553   -10.387 38.285  1.00 50.81 ? 102 TRP B CB  1 
ATOM   2380 C CG  . TRP B 1 100 ? 7.052   -9.576  39.448  1.00 53.51 ? 102 TRP B CG  1 
ATOM   2381 C CD1 . TRP B 1 100 ? 7.877   -10.000 40.442  1.00 55.92 ? 102 TRP B CD1 1 
ATOM   2382 C CD2 . TRP B 1 100 ? 6.689   -8.218  39.775  1.00 54.47 ? 102 TRP B CD2 1 
ATOM   2383 N NE1 . TRP B 1 100 ? 8.077   -8.984  41.356  1.00 56.74 ? 102 TRP B NE1 1 
ATOM   2384 C CE2 . TRP B 1 100 ? 7.350   -7.883  40.971  1.00 55.51 ? 102 TRP B CE2 1 
ATOM   2385 C CE3 . TRP B 1 100 ? 5.878   -7.252  39.164  1.00 55.51 ? 102 TRP B CE3 1 
ATOM   2386 C CZ2 . TRP B 1 100 ? 7.210   -6.632  41.578  1.00 55.73 ? 102 TRP B CZ2 1 
ATOM   2387 C CZ3 . TRP B 1 100 ? 5.739   -6.023  39.769  1.00 56.31 ? 102 TRP B CZ3 1 
ATOM   2388 C CH2 . TRP B 1 100 ? 6.407   -5.721  40.958  1.00 56.08 ? 102 TRP B CH2 1 
ATOM   2389 N N   . GLU B 1 101 ? 9.401   -8.832  37.093  1.00 48.08 ? 103 GLU B N   1 
ATOM   2390 C CA  . GLU B 1 101 ? 10.099  -7.554  36.866  1.00 49.65 ? 103 GLU B CA  1 
ATOM   2391 C C   . GLU B 1 101 ? 10.523  -7.361  35.401  1.00 50.56 ? 103 GLU B C   1 
ATOM   2392 O O   . GLU B 1 101 ? 10.979  -6.266  35.060  1.00 52.53 ? 103 GLU B O   1 
ATOM   2393 C CB  . GLU B 1 101 ? 11.381  -7.430  37.744  1.00 54.80 ? 103 GLU B CB  1 
ATOM   2394 C CG  . GLU B 1 101 ? 11.198  -7.628  39.235  1.00 63.40 ? 103 GLU B CG  1 
ATOM   2395 C CD  . GLU B 1 101 ? 11.131  -9.074  39.712  1.00 74.39 ? 103 GLU B CD  1 
ATOM   2396 O OE1 . GLU B 1 101 ? 11.380  -9.995  38.900  1.00 74.15 ? 103 GLU B OE1 1 
ATOM   2397 O OE2 . GLU B 1 101 ? 10.826  -9.283  40.910  1.00 78.07 ? 103 GLU B OE2 1 
ATOM   2398 N N   . ASP B 1 102 ? 10.382  -8.395  34.517  1.00 47.86 ? 104 ASP B N   1 
ATOM   2399 C CA  . ASP B 1 102 ? 10.546  -8.226  33.075  1.00 46.47 ? 104 ASP B CA  1 
ATOM   2400 C C   . ASP B 1 102 ? 9.571   -7.146  32.572  1.00 45.83 ? 104 ASP B C   1 
ATOM   2401 O O   . ASP B 1 102 ? 8.451   -7.064  33.082  1.00 45.26 ? 104 ASP B O   1 
ATOM   2402 C CB  . ASP B 1 102 ? 10.290  -9.566  32.311  1.00 45.75 ? 104 ASP B CB  1 
ATOM   2403 C CG  . ASP B 1 102 ? 10.656  -9.580  30.824  1.00 49.88 ? 104 ASP B CG  1 
ATOM   2404 O OD1 . ASP B 1 102 ? 9.887   -8.991  29.997  1.00 49.48 ? 104 ASP B OD1 1 
ATOM   2405 O OD2 . ASP B 1 102 ? 11.713  -10.193 30.465  1.00 49.92 ? 104 ASP B OD2 1 
ATOM   2406 N N   . GLU B 1 103 ? 9.999   -6.334  31.590  1.00 45.33 ? 105 GLU B N   1 
ATOM   2407 C CA  . GLU B 1 103 ? 9.172   -5.282  30.980  1.00 47.18 ? 105 GLU B CA  1 
ATOM   2408 C C   . GLU B 1 103 ? 7.814   -5.796  30.505  1.00 46.23 ? 105 GLU B C   1 
ATOM   2409 O O   . GLU B 1 103 ? 6.822   -5.091  30.658  1.00 46.89 ? 105 GLU B O   1 
ATOM   2410 C CB  . GLU B 1 103 ? 9.908   -4.663  29.773  1.00 52.95 ? 105 GLU B CB  1 
ATOM   2411 C CG  . GLU B 1 103 ? 9.225   -3.448  29.168  1.00 64.55 ? 105 GLU B CG  1 
ATOM   2412 C CD  . GLU B 1 103 ? 9.415   -2.154  29.947  1.00 77.72 ? 105 GLU B CD  1 
ATOM   2413 O OE1 . GLU B 1 103 ? 9.967   -2.190  31.071  1.00 79.45 ? 105 GLU B OE1 1 
ATOM   2414 O OE2 . GLU B 1 103 ? 9.007   -1.094  29.420  1.00 84.08 ? 105 GLU B OE2 1 
ATOM   2415 N N   . LYS B 1 104 ? 7.770   -7.017  29.945  1.00 44.16 ? 106 LYS B N   1 
ATOM   2416 C CA  . LYS B 1 104 ? 6.547   -7.630  29.459  1.00 42.17 ? 106 LYS B CA  1 
ATOM   2417 C C   . LYS B 1 104 ? 5.647   -8.241  30.558  1.00 39.61 ? 106 LYS B C   1 
ATOM   2418 O O   . LYS B 1 104 ? 4.500   -8.552  30.260  1.00 39.35 ? 106 LYS B O   1 
ATOM   2419 C CB  . LYS B 1 104 ? 6.880   -8.681  28.373  1.00 45.31 ? 106 LYS B CB  1 
ATOM   2420 C CG  . LYS B 1 104 ? 7.403   -8.120  27.037  1.00 51.90 ? 106 LYS B CG  1 
ATOM   2421 C CD  . LYS B 1 104 ? 6.311   -7.352  26.291  1.00 60.62 ? 106 LYS B CD  1 
ATOM   2422 C CE  . LYS B 1 104 ? 6.640   -7.004  24.859  1.00 69.54 ? 106 LYS B CE  1 
ATOM   2423 N NZ  . LYS B 1 104 ? 5.770   -5.889  24.386  1.00 75.80 ? 106 LYS B NZ  1 
ATOM   2424 N N   . ASN B 1 105 ? 6.139   -8.393  31.788  1.00 38.01 ? 107 ASN B N   1 
ATOM   2425 C CA  . ASN B 1 105 ? 5.343   -8.922  32.895  1.00 38.58 ? 107 ASN B CA  1 
ATOM   2426 C C   . ASN B 1 105 ? 5.008   -7.867  33.977  1.00 41.06 ? 107 ASN B C   1 
ATOM   2427 O O   . ASN B 1 105 ? 3.994   -8.018  34.664  1.00 41.91 ? 107 ASN B O   1 
ATOM   2428 C CB  . ASN B 1 105 ? 6.089   -10.046 33.569  1.00 36.89 ? 107 ASN B CB  1 
ATOM   2429 C CG  . ASN B 1 105 ? 6.361   -11.238 32.662  1.00 37.93 ? 107 ASN B CG  1 
ATOM   2430 O OD1 . ASN B 1 105 ? 5.527   -11.618 31.848  1.00 35.98 ? 107 ASN B OD1 1 
ATOM   2431 N ND2 . ASN B 1 105 ? 7.504   -11.841 32.787  1.00 38.84 ? 107 ASN B ND2 1 
ATOM   2432 N N   . LYS B 1 106 ? 5.840   -6.842  34.145  1.00 42.78 ? 108 LYS B N   1 
ATOM   2433 C CA  . LYS B 1 106 ? 5.661   -5.928  35.297  1.00 43.92 ? 108 LYS B CA  1 
ATOM   2434 C C   . LYS B 1 106 ? 4.293   -5.240  35.391  1.00 43.73 ? 108 LYS B C   1 
ATOM   2435 O O   . LYS B 1 106 ? 3.853   -4.990  36.510  1.00 43.85 ? 108 LYS B O   1 
ATOM   2436 C CB  . LYS B 1 106 ? 6.764   -4.886  35.395  1.00 47.62 ? 108 LYS B CB  1 
ATOM   2437 C CG  . LYS B 1 106 ? 6.909   -3.993  34.198  1.00 53.45 ? 108 LYS B CG  1 
ATOM   2438 C CD  . LYS B 1 106 ? 8.004   -2.924  34.461  1.00 61.60 ? 108 LYS B CD  1 
ATOM   2439 C CE  . LYS B 1 106 ? 7.867   -1.724  33.550  1.00 69.09 ? 108 LYS B CE  1 
ATOM   2440 N NZ  . LYS B 1 106 ? 9.128   -0.919  33.464  1.00 73.91 ? 108 LYS B NZ  1 
ATOM   2441 N N   . ARG B 1 107 ? 3.628   -4.940  34.259  1.00 42.70 ? 109 ARG B N   1 
ATOM   2442 C CA  . ARG B 1 107 ? 2.280   -4.343  34.255  1.00 42.68 ? 109 ARG B CA  1 
ATOM   2443 C C   . ARG B 1 107 ? 1.139   -5.426  34.212  1.00 41.31 ? 109 ARG B C   1 
ATOM   2444 O O   . ARG B 1 107 ? -0.031  -5.076  34.115  1.00 41.79 ? 109 ARG B O   1 
ATOM   2445 C CB  . ARG B 1 107 ? 2.114   -3.367  33.065  1.00 45.05 ? 109 ARG B CB  1 
ATOM   2446 C CG  . ARG B 1 107 ? 2.977   -2.084  33.089  1.00 50.88 ? 109 ARG B CG  1 
ATOM   2447 C CD  . ARG B 1 107 ? 3.133   -1.392  31.731  1.00 58.46 ? 109 ARG B CD  1 
ATOM   2448 N NE  . ARG B 1 107 ? 1.932   -1.300  30.879  1.00 64.90 ? 109 ARG B NE  1 
ATOM   2449 C CZ  . ARG B 1 107 ? 1.852   -0.598  29.733  1.00 69.85 ? 109 ARG B CZ  1 
ATOM   2450 N NH1 . ARG B 1 107 ? 0.718   -0.583  29.032  1.00 68.42 ? 109 ARG B NH1 1 
ATOM   2451 N NH2 . ARG B 1 107 ? 2.897   0.110   29.297  1.00 69.82 ? 109 ARG B NH2 1 
ATOM   2452 N N   . GLY B 1 108 ? 1.494   -6.708  34.340  1.00 38.56 ? 110 GLY B N   1 
ATOM   2453 C CA  . GLY B 1 108 ? 0.598   -7.816  34.121  1.00 38.15 ? 110 GLY B CA  1 
ATOM   2454 C C   . GLY B 1 108 ? 0.262   -8.608  35.350  1.00 36.14 ? 110 GLY B C   1 
ATOM   2455 O O   . GLY B 1 108 ? 0.330   -8.111  36.486  1.00 34.39 ? 110 GLY B O   1 
ATOM   2456 N N   . GLY B 1 109 ? -0.124  -9.842  35.109  1.00 34.94 ? 111 GLY B N   1 
ATOM   2457 C CA  . GLY B 1 109 ? -0.725  -10.670 36.133  1.00 35.01 ? 111 GLY B CA  1 
ATOM   2458 C C   . GLY B 1 109 ? -0.869  -12.097 35.652  1.00 33.51 ? 111 GLY B C   1 
ATOM   2459 O O   . GLY B 1 109 ? -0.335  -12.444 34.611  1.00 32.28 ? 111 GLY B O   1 
ATOM   2460 N N   . ARG B 1 110 ? -1.558  -12.910 36.411  1.00 33.04 ? 112 ARG B N   1 
ATOM   2461 C CA  . ARG B 1 110 ? -1.724  -14.306 36.070  1.00 32.39 ? 112 ARG B CA  1 
ATOM   2462 C C   . ARG B 1 110 ? -3.063  -14.846 36.442  1.00 34.18 ? 112 ARG B C   1 
ATOM   2463 O O   . ARG B 1 110 ? -3.614  -14.481 37.491  1.00 34.70 ? 112 ARG B O   1 
ATOM   2464 C CB  . ARG B 1 110 ? -0.617  -15.117 36.724  1.00 31.50 ? 112 ARG B CB  1 
ATOM   2465 C CG  . ARG B 1 110 ? -0.709  -15.183 38.253  1.00 37.81 ? 112 ARG B CG  1 
ATOM   2466 C CD  . ARG B 1 110 ? 0.435   -15.894 38.947  1.00 42.24 ? 112 ARG B CD  1 
ATOM   2467 N NE  . ARG B 1 110 ? 0.165   -15.892 40.392  1.00 47.68 ? 112 ARG B NE  1 
ATOM   2468 C CZ  . ARG B 1 110 ? 0.846   -16.562 41.324  1.00 48.10 ? 112 ARG B CZ  1 
ATOM   2469 N NH1 . ARG B 1 110 ? 0.503   -16.465 42.604  1.00 49.59 ? 112 ARG B NH1 1 
ATOM   2470 N NH2 . ARG B 1 110 ? 1.865   -17.331 40.986  1.00 45.66 ? 112 ARG B NH2 1 
ATOM   2471 N N   . TRP B 1 111 ? -3.603  -15.724 35.591  1.00 34.38 ? 113 TRP B N   1 
ATOM   2472 C CA  . TRP B 1 111 ? -4.654  -16.678 35.951  1.00 35.03 ? 113 TRP B CA  1 
ATOM   2473 C C   . TRP B 1 111 ? -4.060  -17.862 36.702  1.00 36.96 ? 113 TRP B C   1 
ATOM   2474 O O   . TRP B 1 111 ? -3.207  -18.555 36.153  1.00 36.42 ? 113 TRP B O   1 
ATOM   2475 C CB  . TRP B 1 111 ? -5.373  -17.184 34.695  1.00 35.05 ? 113 TRP B CB  1 
ATOM   2476 C CG  . TRP B 1 111 ? -6.288  -16.185 34.087  1.00 34.99 ? 113 TRP B CG  1 
ATOM   2477 C CD1 . TRP B 1 111 ? -6.090  -15.490 32.942  1.00 37.45 ? 113 TRP B CD1 1 
ATOM   2478 C CD2 . TRP B 1 111 ? -7.520  -15.705 34.646  1.00 35.52 ? 113 TRP B CD2 1 
ATOM   2479 N NE1 . TRP B 1 111 ? -7.107  -14.565 32.765  1.00 38.04 ? 113 TRP B NE1 1 
ATOM   2480 C CE2 . TRP B 1 111 ? -8.018  -14.713 33.782  1.00 36.56 ? 113 TRP B CE2 1 
ATOM   2481 C CE3 . TRP B 1 111 ? -8.252  -16.026 35.782  1.00 35.77 ? 113 TRP B CE3 1 
ATOM   2482 C CZ2 . TRP B 1 111 ? -9.212  -14.036 34.035  1.00 38.36 ? 113 TRP B CZ2 1 
ATOM   2483 C CZ3 . TRP B 1 111 ? -9.446  -15.359 36.020  1.00 37.90 ? 113 TRP B CZ3 1 
ATOM   2484 C CH2 . TRP B 1 111 ? -9.909  -14.380 35.147  1.00 38.56 ? 113 TRP B CH2 1 
ATOM   2485 N N   . LEU B 1 112 ? -4.540  -18.132 37.933  1.00 37.74 ? 114 LEU B N   1 
ATOM   2486 C CA  . LEU B 1 112 ? -3.965  -19.135 38.787  1.00 39.74 ? 114 LEU B CA  1 
ATOM   2487 C C   . LEU B 1 112 ? -4.968  -20.262 39.101  1.00 40.67 ? 114 LEU B C   1 
ATOM   2488 O O   . LEU B 1 112 ? -6.105  -20.007 39.519  1.00 40.32 ? 114 LEU B O   1 
ATOM   2489 C CB  . LEU B 1 112 ? -3.498  -18.481 40.081  1.00 40.53 ? 114 LEU B CB  1 
ATOM   2490 C CG  . LEU B 1 112 ? -2.931  -19.392 41.140  1.00 42.37 ? 114 LEU B CG  1 
ATOM   2491 C CD1 . LEU B 1 112 ? -1.595  -19.899 40.714  1.00 41.55 ? 114 LEU B CD1 1 
ATOM   2492 C CD2 . LEU B 1 112 ? -2.873  -18.659 42.520  1.00 43.67 ? 114 LEU B CD2 1 
ATOM   2493 N N   . ILE B 1 113 ? -4.508  -21.501 38.864  1.00 40.24 ? 115 ILE B N   1 
ATOM   2494 C CA  . ILE B 1 113 ? -5.155  -22.791 39.153  1.00 41.29 ? 115 ILE B CA  1 
ATOM   2495 C C   . ILE B 1 113 ? -4.353  -23.359 40.348  1.00 40.96 ? 115 ILE B C   1 
ATOM   2496 O O   . ILE B 1 113 ? -3.163  -23.596 40.217  1.00 39.61 ? 115 ILE B O   1 
ATOM   2497 C CB  . ILE B 1 113 ? -5.020  -23.765 37.942  1.00 43.77 ? 115 ILE B CB  1 
ATOM   2498 C CG1 . ILE B 1 113 ? -5.350  -23.085 36.590  1.00 46.07 ? 115 ILE B CG1 1 
ATOM   2499 C CG2 . ILE B 1 113 ? -5.817  -25.052 38.137  1.00 44.72 ? 115 ILE B CG2 1 
ATOM   2500 C CD1 . ILE B 1 113 ? -6.643  -22.303 36.578  1.00 46.17 ? 115 ILE B CD1 1 
ATOM   2501 N N   . THR B 1 114 ? -4.968  -23.536 41.485  1.00 43.10 ? 116 THR B N   1 
ATOM   2502 C CA  . THR B 1 114 ? -4.349  -24.205 42.624  1.00 46.58 ? 116 THR B CA  1 
ATOM   2503 C C   . THR B 1 114 ? -4.875  -25.634 42.688  1.00 47.10 ? 116 THR B C   1 
ATOM   2504 O O   . THR B 1 114 ? -6.100  -25.808 42.648  1.00 46.24 ? 116 THR B O   1 
ATOM   2505 C CB  . THR B 1 114 ? -4.747  -23.496 43.895  1.00 51.94 ? 116 THR B CB  1 
ATOM   2506 O OG1 . THR B 1 114 ? -6.179  -23.544 43.988  1.00 57.32 ? 116 THR B OG1 1 
ATOM   2507 C CG2 . THR B 1 114 ? -4.313  -22.057 43.896  1.00 51.93 ? 116 THR B CG2 1 
ATOM   2508 N N   . LEU B 1 115 ? -3.980  -26.628 42.803  1.00 47.59 ? 117 LEU B N   1 
ATOM   2509 C CA  . LEU B 1 115 ? -4.367  -28.014 42.908  1.00 51.51 ? 117 LEU B CA  1 
ATOM   2510 C C   . LEU B 1 115 ? -4.081  -28.512 44.323  1.00 55.06 ? 117 LEU B C   1 
ATOM   2511 O O   . LEU B 1 115 ? -2.949  -28.354 44.838  1.00 56.05 ? 117 LEU B O   1 
ATOM   2512 C CB  . LEU B 1 115 ? -3.603  -28.884 41.905  1.00 51.85 ? 117 LEU B CB  1 
ATOM   2513 C CG  . LEU B 1 115 ? -3.817  -28.605 40.406  1.00 54.75 ? 117 LEU B CG  1 
ATOM   2514 C CD1 . LEU B 1 115 ? -3.097  -29.656 39.582  1.00 55.32 ? 117 LEU B CD1 1 
ATOM   2515 C CD2 . LEU B 1 115 ? -5.268  -28.632 40.005  1.00 56.32 ? 117 LEU B CD2 1 
ATOM   2516 N N   . ASN B 1 116 ? -5.119  -29.136 44.936  1.00 56.17 ? 118 ASN B N   1 
ATOM   2517 C CA  . ASN B 1 116 ? -4.981  -29.774 46.230  1.00 58.37 ? 118 ASN B CA  1 
ATOM   2518 C C   . ASN B 1 116 ? -4.107  -31.052 46.106  1.00 59.62 ? 118 ASN B C   1 
ATOM   2519 O O   . ASN B 1 116 ? -3.864  -31.551 45.003  1.00 57.98 ? 118 ASN B O   1 
ATOM   2520 C CB  . ASN B 1 116 ? -6.379  -30.110 46.828  1.00 60.87 ? 118 ASN B CB  1 
ATOM   2521 C CG  . ASN B 1 116 ? -7.102  -31.279 46.166  1.00 63.61 ? 118 ASN B CG  1 
ATOM   2522 O OD1 . ASN B 1 116 ? -6.490  -32.202 45.627  1.00 64.08 ? 118 ASN B OD1 1 
ATOM   2523 N ND2 . ASN B 1 116 ? -8.428  -31.263 46.174  1.00 64.84 ? 118 ASN B ND2 1 
ATOM   2524 N N   . LYS B 1 117 ? -3.672  -31.584 47.248  1.00 61.47 ? 119 LYS B N   1 
ATOM   2525 C CA  . LYS B 1 117 ? -2.778  -32.742 47.332  1.00 63.73 ? 119 LYS B CA  1 
ATOM   2526 C C   . LYS B 1 117 ? -3.212  -33.919 46.431  1.00 64.34 ? 119 LYS B C   1 
ATOM   2527 O O   . LYS B 1 117 ? -2.386  -34.462 45.698  1.00 64.44 ? 119 LYS B O   1 
ATOM   2528 C CB  . LYS B 1 117 ? -2.680  -33.197 48.816  1.00 67.21 ? 119 LYS B CB  1 
ATOM   2529 C CG  . LYS B 1 117 ? -2.010  -34.550 49.050  1.00 74.36 ? 119 LYS B CG  1 
ATOM   2530 C CD  . LYS B 1 117 ? -1.857  -34.882 50.524  1.00 81.15 ? 119 LYS B CD  1 
ATOM   2531 C CE  . LYS B 1 117 ? -3.152  -35.326 51.216  1.00 86.39 ? 119 LYS B CE  1 
ATOM   2532 N NZ  . LYS B 1 117 ? -3.694  -36.622 50.684  1.00 88.94 ? 119 LYS B NZ  1 
ATOM   2533 N N   . GLN B 1 118 ? -4.493  -34.321 46.512  1.00 64.21 ? 120 GLN B N   1 
ATOM   2534 C CA  . GLN B 1 118 ? -5.005  -35.474 45.738  1.00 64.80 ? 120 GLN B CA  1 
ATOM   2535 C C   . GLN B 1 118 ? -4.847  -35.278 44.244  1.00 63.60 ? 120 GLN B C   1 
ATOM   2536 O O   . GLN B 1 118 ? -4.691  -36.230 43.484  1.00 62.70 ? 120 GLN B O   1 
ATOM   2537 C CB  . GLN B 1 118 ? -6.510  -35.647 45.980  1.00 68.20 ? 120 GLN B CB  1 
ATOM   2538 C CG  . GLN B 1 118 ? -6.912  -36.378 47.238  1.00 72.79 ? 120 GLN B CG  1 
ATOM   2539 C CD  . GLN B 1 118 ? -8.384  -36.758 47.177  1.00 80.10 ? 120 GLN B CD  1 
ATOM   2540 O OE1 . GLN B 1 118 ? -9.201  -36.143 46.457  1.00 82.45 ? 120 GLN B OE1 1 
ATOM   2541 N NE2 . GLN B 1 118 ? -8.767  -37.790 47.937  1.00 80.37 ? 120 GLN B NE2 1 
ATOM   2542 N N   . GLN B 1 119 ? -4.920  -34.021 43.816  1.00 63.00 ? 121 GLN B N   1 
ATOM   2543 C CA  . GLN B 1 119 ? -4.864  -33.684 42.408  1.00 63.02 ? 121 GLN B CA  1 
ATOM   2544 C C   . GLN B 1 119 ? -3.487  -33.768 41.788  1.00 62.78 ? 121 GLN B C   1 
ATOM   2545 O O   . GLN B 1 119 ? -3.394  -33.747 40.564  1.00 63.14 ? 121 GLN B O   1 
ATOM   2546 C CB  . GLN B 1 119 ? -5.470  -32.310 42.206  1.00 64.31 ? 121 GLN B CB  1 
ATOM   2547 C CG  . GLN B 1 119 ? -6.936  -32.301 42.516  1.00 67.35 ? 121 GLN B CG  1 
ATOM   2548 C CD  . GLN B 1 119 ? -7.461  -30.921 42.342  1.00 74.08 ? 121 GLN B CD  1 
ATOM   2549 O OE1 . GLN B 1 119 ? -7.304  -30.038 43.214  1.00 75.23 ? 121 GLN B OE1 1 
ATOM   2550 N NE2 . GLN B 1 119 ? -8.084  -30.696 41.205  1.00 75.18 ? 121 GLN B NE2 1 
ATOM   2551 N N   . ARG B 1 120 ? -2.418  -33.865 42.584  1.00 62.11 ? 122 ARG B N   1 
ATOM   2552 C CA  . ARG B 1 120 ? -1.082  -34.123 42.046  1.00 61.86 ? 122 ARG B CA  1 
ATOM   2553 C C   . ARG B 1 120 ? -1.035  -35.442 41.272  1.00 61.12 ? 122 ARG B C   1 
ATOM   2554 O O   . ARG B 1 120 ? -0.371  -35.537 40.232  1.00 61.58 ? 122 ARG B O   1 
ATOM   2555 C CB  . ARG B 1 120 ? -0.069  -34.127 43.177  1.00 63.70 ? 122 ARG B CB  1 
ATOM   2556 C CG  . ARG B 1 120 ? 1.365   -34.360 42.756  1.00 67.82 ? 122 ARG B CG  1 
ATOM   2557 C CD  . ARG B 1 120 ? 2.218   -33.351 43.473  1.00 73.20 ? 122 ARG B CD  1 
ATOM   2558 N NE  . ARG B 1 120 ? 3.621   -33.719 43.542  1.00 79.07 ? 122 ARG B NE  1 
ATOM   2559 C CZ  . ARG B 1 120 ? 4.538   -33.028 44.219  1.00 82.80 ? 122 ARG B CZ  1 
ATOM   2560 N NH1 . ARG B 1 120 ? 4.195   -31.922 44.887  1.00 83.85 ? 122 ARG B NH1 1 
ATOM   2561 N NH2 . ARG B 1 120 ? 5.804   -33.428 44.229  1.00 80.72 ? 122 ARG B NH2 1 
ATOM   2562 N N   . ARG B 1 121 ? -1.741  -36.454 41.776  1.00 59.30 ? 123 ARG B N   1 
ATOM   2563 C CA  . ARG B 1 121 ? -1.794  -37.761 41.138  1.00 58.59 ? 123 ARG B CA  1 
ATOM   2564 C C   . ARG B 1 121 ? -2.670  -37.712 39.891  1.00 56.29 ? 123 ARG B C   1 
ATOM   2565 O O   . ARG B 1 121 ? -2.255  -38.190 38.858  1.00 57.52 ? 123 ARG B O   1 
ATOM   2566 C CB  . ARG B 1 121 ? -2.326  -38.827 42.128  1.00 61.13 ? 123 ARG B CB  1 
ATOM   2567 C CG  . ARG B 1 121 ? -1.255  -39.337 43.146  1.00 67.85 ? 123 ARG B CG  1 
ATOM   2568 C CD  . ARG B 1 121 ? -0.537  -40.666 42.823  1.00 73.57 ? 123 ARG B CD  1 
ATOM   2569 N NE  . ARG B 1 121 ? -0.514  -40.953 41.385  1.00 77.69 ? 123 ARG B NE  1 
ATOM   2570 C CZ  . ARG B 1 121 ? -1.231  -41.876 40.746  1.00 79.32 ? 123 ARG B CZ  1 
ATOM   2571 N NH1 . ARG B 1 121 ? -1.121  -42.014 39.434  1.00 79.01 ? 123 ARG B NH1 1 
ATOM   2572 N NH2 . ARG B 1 121 ? -2.061  -42.679 41.416  1.00 78.44 ? 123 ARG B NH2 1 
ATOM   2573 N N   . SER B 1 122 ? -3.855  -37.130 39.972  1.00 54.17 ? 124 SER B N   1 
ATOM   2574 C CA  . SER B 1 122 ? -4.859  -37.180 38.909  1.00 54.17 ? 124 SER B CA  1 
ATOM   2575 C C   . SER B 1 122 ? -4.808  -36.081 37.811  1.00 54.30 ? 124 SER B C   1 
ATOM   2576 O O   . SER B 1 122 ? -5.041  -36.417 36.640  1.00 55.15 ? 124 SER B O   1 
ATOM   2577 C CB  . SER B 1 122 ? -6.248  -37.138 39.525  1.00 56.04 ? 124 SER B CB  1 
ATOM   2578 O OG  . SER B 1 122 ? -6.356  -35.974 40.322  1.00 58.05 ? 124 SER B OG  1 
ATOM   2579 N N   . ASP B 1 123 ? -4.525  -34.795 38.174  1.00 51.21 ? 125 ASP B N   1 
ATOM   2580 C CA  . ASP B 1 123 ? -4.708  -33.633 37.283  1.00 49.67 ? 125 ASP B CA  1 
ATOM   2581 C C   . ASP B 1 123 ? -3.448  -32.880 36.941  1.00 44.37 ? 125 ASP B C   1 
ATOM   2582 O O   . ASP B 1 123 ? -3.479  -32.179 35.937  1.00 43.91 ? 125 ASP B O   1 
ATOM   2583 C CB  . ASP B 1 123 ? -5.622  -32.597 37.920  1.00 53.60 ? 125 ASP B CB  1 
ATOM   2584 C CG  . ASP B 1 123 ? -7.035  -33.054 38.162  1.00 65.99 ? 125 ASP B CG  1 
ATOM   2585 O OD1 . ASP B 1 123 ? -7.513  -33.934 37.404  1.00 67.92 ? 125 ASP B OD1 1 
ATOM   2586 O OD2 . ASP B 1 123 ? -7.675  -32.531 39.110  1.00 70.06 ? 125 ASP B OD2 1 
ATOM   2587 N N   . LEU B 1 124 ? -2.361  -32.963 37.718  1.00 41.95 ? 126 LEU B N   1 
ATOM   2588 C CA  . LEU B 1 124 ? -1.227  -32.036 37.495  1.00 42.33 ? 126 LEU B CA  1 
ATOM   2589 C C   . LEU B 1 124 ? -0.657  -32.243 36.086  1.00 40.24 ? 126 LEU B C   1 
ATOM   2590 O O   . LEU B 1 124 ? -0.458  -31.283 35.361  1.00 39.67 ? 126 LEU B O   1 
ATOM   2591 C CB  . LEU B 1 124 ? -0.118  -32.212 38.533  1.00 43.58 ? 126 LEU B CB  1 
ATOM   2592 C CG  . LEU B 1 124 ? 1.112   -31.291 38.322  1.00 46.07 ? 126 LEU B CG  1 
ATOM   2593 C CD1 . LEU B 1 124 ? 0.751   -29.887 38.505  1.00 46.20 ? 126 LEU B CD1 1 
ATOM   2594 C CD2 . LEU B 1 124 ? 2.230   -31.642 39.267  1.00 48.34 ? 126 LEU B CD2 1 
ATOM   2595 N N   . ASN B 1 125 ? -0.429  -33.533 35.719  1.00 37.80 ? 127 ASN B N   1 
ATOM   2596 C CA  . ASN B 1 125 ? 0.195   -33.791 34.424  1.00 39.52 ? 127 ASN B CA  1 
ATOM   2597 C C   . ASN B 1 125 ? -0.734  -33.312 33.269  1.00 37.67 ? 127 ASN B C   1 
ATOM   2598 O O   . ASN B 1 125 ? -0.264  -32.591 32.389  1.00 36.26 ? 127 ASN B O   1 
ATOM   2599 C CB  . ASN B 1 125 ? 0.566   -35.249 34.290  1.00 43.47 ? 127 ASN B CB  1 
ATOM   2600 C CG  . ASN B 1 125 ? 1.672   -35.624 35.247  1.00 49.94 ? 127 ASN B CG  1 
ATOM   2601 O OD1 . ASN B 1 125 ? 2.576   -34.833 35.545  1.00 51.66 ? 127 ASN B OD1 1 
ATOM   2602 N ND2 . ASN B 1 125 ? 1.615   -36.811 35.779  1.00 50.33 ? 127 ASN B ND2 1 
ATOM   2603 N N   . ARG B 1 126 ? -2.042  -33.665 33.323  1.00 37.00 ? 128 ARG B N   1 
ATOM   2604 C CA  . ARG B 1 126 ? -2.959  -33.331 32.215  1.00 38.03 ? 128 ARG B CA  1 
ATOM   2605 C C   . ARG B 1 126 ? -3.155  -31.801 32.126  1.00 35.34 ? 128 ARG B C   1 
ATOM   2606 O O   . ARG B 1 126 ? -3.131  -31.248 31.039  1.00 35.38 ? 128 ARG B O   1 
ATOM   2607 C CB  . ARG B 1 126 ? -4.364  -34.027 32.395  1.00 42.14 ? 128 ARG B CB  1 
ATOM   2608 C CG  . ARG B 1 126 ? -5.404  -33.486 31.379  1.00 51.86 ? 128 ARG B CG  1 
ATOM   2609 C CD  . ARG B 1 126 ? -6.569  -34.391 31.030  1.00 62.58 ? 128 ARG B CD  1 
ATOM   2610 N NE  . ARG B 1 126 ? -7.372  -33.912 29.885  1.00 72.28 ? 128 ARG B NE  1 
ATOM   2611 C CZ  . ARG B 1 126 ? -8.256  -32.900 29.917  1.00 79.59 ? 128 ARG B CZ  1 
ATOM   2612 N NH1 . ARG B 1 126 ? -8.924  -32.555 28.816  1.00 80.85 ? 128 ARG B NH1 1 
ATOM   2613 N NH2 . ARG B 1 126 ? -8.471  -32.223 31.046  1.00 80.91 ? 128 ARG B NH2 1 
ATOM   2614 N N   . PHE B 1 127 ? -3.372  -31.145 33.260  1.00 34.03 ? 129 PHE B N   1 
ATOM   2615 C CA  . PHE B 1 127 ? -3.538  -29.704 33.307  1.00 34.38 ? 129 PHE B CA  1 
ATOM   2616 C C   . PHE B 1 127 ? -2.306  -28.936 32.839  1.00 32.97 ? 129 PHE B C   1 
ATOM   2617 O O   . PHE B 1 127 ? -2.484  -27.902 32.205  1.00 33.48 ? 129 PHE B O   1 
ATOM   2618 C CB  . PHE B 1 127 ? -3.855  -29.243 34.736  1.00 37.51 ? 129 PHE B CB  1 
ATOM   2619 C CG  . PHE B 1 127 ? -5.284  -29.406 35.196  1.00 43.01 ? 129 PHE B CG  1 
ATOM   2620 C CD1 . PHE B 1 127 ? -6.178  -30.216 34.497  1.00 45.53 ? 129 PHE B CD1 1 
ATOM   2621 C CD2 . PHE B 1 127 ? -5.732  -28.763 36.337  1.00 45.86 ? 129 PHE B CD2 1 
ATOM   2622 C CE1 . PHE B 1 127 ? -7.497  -30.358 34.931  1.00 47.48 ? 129 PHE B CE1 1 
ATOM   2623 C CE2 . PHE B 1 127 ? -7.038  -28.918 36.778  1.00 47.81 ? 129 PHE B CE2 1 
ATOM   2624 C CZ  . PHE B 1 127 ? -7.913  -29.717 36.076  1.00 48.15 ? 129 PHE B CZ  1 
ATOM   2625 N N   . TRP B 1 128 ? -1.067  -29.361 33.174  1.00 31.59 ? 130 TRP B N   1 
ATOM   2626 C CA  . TRP B 1 128 ? 0.138   -28.671 32.659  1.00 32.24 ? 130 TRP B CA  1 
ATOM   2627 C C   . TRP B 1 128 ? 0.199   -28.805 31.145  1.00 31.11 ? 130 TRP B C   1 
ATOM   2628 O O   . TRP B 1 128 ? 0.401   -27.826 30.471  1.00 30.24 ? 130 TRP B O   1 
ATOM   2629 C CB  . TRP B 1 128 ? 1.404   -29.197 33.341  1.00 34.56 ? 130 TRP B CB  1 
ATOM   2630 C CG  . TRP B 1 128 ? 2.696   -28.579 32.892  1.00 35.66 ? 130 TRP B CG  1 
ATOM   2631 C CD1 . TRP B 1 128 ? 3.786   -29.259 32.464  1.00 36.99 ? 130 TRP B CD1 1 
ATOM   2632 C CD2 . TRP B 1 128 ? 3.047   -27.185 32.845  1.00 35.10 ? 130 TRP B CD2 1 
ATOM   2633 N NE1 . TRP B 1 128 ? 4.792   -28.390 32.158  1.00 37.44 ? 130 TRP B NE1 1 
ATOM   2634 C CE2 . TRP B 1 128 ? 4.382   -27.108 32.401  1.00 37.15 ? 130 TRP B CE2 1 
ATOM   2635 C CE3 . TRP B 1 128 ? 2.384   -25.986 33.155  1.00 35.20 ? 130 TRP B CE3 1 
ATOM   2636 C CZ2 . TRP B 1 128 ? 5.059   -25.884 32.254  1.00 36.50 ? 130 TRP B CZ2 1 
ATOM   2637 C CZ3 . TRP B 1 128 ? 3.056   -24.784 32.997  1.00 35.82 ? 130 TRP B CZ3 1 
ATOM   2638 C CH2 . TRP B 1 128 ? 4.369   -24.740 32.541  1.00 36.38 ? 130 TRP B CH2 1 
ATOM   2639 N N   . LEU B 1 129 ? -0.021  -30.012 30.603  1.00 31.49 ? 131 LEU B N   1 
ATOM   2640 C CA  . LEU B 1 129 ? -0.038  -30.201 29.158  1.00 33.46 ? 131 LEU B CA  1 
ATOM   2641 C C   . LEU B 1 129 ? -1.116  -29.360 28.473  1.00 33.07 ? 131 LEU B C   1 
ATOM   2642 O O   . LEU B 1 129 ? -0.831  -28.720 27.462  1.00 32.41 ? 131 LEU B O   1 
ATOM   2643 C CB  . LEU B 1 129 ? -0.156  -31.688 28.796  1.00 35.04 ? 131 LEU B CB  1 
ATOM   2644 C CG  . LEU B 1 129 ? -0.128  -31.989 27.276  1.00 37.06 ? 131 LEU B CG  1 
ATOM   2645 C CD1 . LEU B 1 129 ? 1.114   -31.440 26.621  1.00 38.81 ? 131 LEU B CD1 1 
ATOM   2646 C CD2 . LEU B 1 129 ? -0.207  -33.446 27.028  1.00 38.04 ? 131 LEU B CD2 1 
ATOM   2647 N N   . GLU B 1 130 ? -2.327  -29.329 28.995  1.00 34.01 ? 132 GLU B N   1 
ATOM   2648 C CA  . GLU B 1 130 ? -3.414  -28.563 28.381  1.00 34.78 ? 132 GLU B CA  1 
ATOM   2649 C C   . GLU B 1 130 ? -3.040  -27.061 28.353  1.00 34.33 ? 132 GLU B C   1 
ATOM   2650 O O   . GLU B 1 130 ? -3.305  -26.375 27.374  1.00 35.75 ? 132 GLU B O   1 
ATOM   2651 C CB  . GLU B 1 130 ? -4.758  -28.772 29.128  1.00 38.21 ? 132 GLU B CB  1 
ATOM   2652 C CG  . GLU B 1 130 ? -5.373  -30.160 29.002  1.00 46.37 ? 132 GLU B CG  1 
ATOM   2653 C CD  . GLU B 1 130 ? -5.442  -30.769 27.606  1.00 55.56 ? 132 GLU B CD  1 
ATOM   2654 O OE1 . GLU B 1 130 ? -5.750  -30.034 26.644  1.00 49.99 ? 132 GLU B OE1 1 
ATOM   2655 O OE2 . GLU B 1 130 ? -5.177  -31.989 27.473  1.00 61.26 ? 132 GLU B OE2 1 
ATOM   2656 N N   . THR B 1 131 ? -2.408  -26.569 29.418  1.00 32.68 ? 133 THR B N   1 
ATOM   2657 C CA  . THR B 1 131 ? -1.908  -25.188 29.445  1.00 32.02 ? 133 THR B CA  1 
ATOM   2658 C C   . THR B 1 131 ? -0.885  -24.938 28.349  1.00 31.72 ? 133 THR B C   1 
ATOM   2659 O O   . THR B 1 131 ? -0.985  -23.930 27.618  1.00 32.34 ? 133 THR B O   1 
ATOM   2660 C CB  . THR B 1 131 ? -1.298  -24.903 30.853  1.00 35.05 ? 133 THR B CB  1 
ATOM   2661 O OG1 . THR B 1 131 ? -2.268  -25.178 31.864  1.00 35.07 ? 133 THR B OG1 1 
ATOM   2662 C CG2 . THR B 1 131 ? -0.795  -23.462 31.018  1.00 35.44 ? 133 THR B CG2 1 
ATOM   2663 N N   . LEU B 1 132 ? 0.116   -25.840 28.201  1.00 31.15 ? 134 LEU B N   1 
ATOM   2664 C CA  . LEU B 1 132 ? 1.151   -25.710 27.186  1.00 32.82 ? 134 LEU B CA  1 
ATOM   2665 C C   . LEU B 1 132 ? 0.540   -25.680 25.785  1.00 34.12 ? 134 LEU B C   1 
ATOM   2666 O O   . LEU B 1 132 ? 0.954   -24.860 24.952  1.00 33.24 ? 134 LEU B O   1 
ATOM   2667 C CB  . LEU B 1 132 ? 2.163   -26.856 27.292  1.00 33.93 ? 134 LEU B CB  1 
ATOM   2668 C CG  . LEU B 1 132 ? 2.965   -26.949 28.584  1.00 34.28 ? 134 LEU B CG  1 
ATOM   2669 C CD1 . LEU B 1 132 ? 3.789   -28.225 28.630  1.00 33.12 ? 134 LEU B CD1 1 
ATOM   2670 C CD2 . LEU B 1 132 ? 3.805   -25.727 28.789  1.00 36.27 ? 134 LEU B CD2 1 
ATOM   2671 N N   . LEU B 1 133 ? -0.463  -26.543 25.530  1.00 34.54 ? 135 LEU B N   1 
ATOM   2672 C CA  . LEU B 1 133 ? -1.144  -26.570 24.211  1.00 35.73 ? 135 LEU B CA  1 
ATOM   2673 C C   . LEU B 1 133 ? -1.936  -25.284 23.925  1.00 36.55 ? 135 LEU B C   1 
ATOM   2674 O O   . LEU B 1 133 ? -1.962  -24.834 22.780  1.00 37.56 ? 135 LEU B O   1 
ATOM   2675 C CB  . LEU B 1 133 ? -2.038  -27.818 24.063  1.00 35.74 ? 135 LEU B CB  1 
ATOM   2676 C CG  . LEU B 1 133 ? -1.322  -29.156 24.231  1.00 37.10 ? 135 LEU B CG  1 
ATOM   2677 C CD1 . LEU B 1 133 ? -2.281  -30.294 24.090  1.00 37.53 ? 135 LEU B CD1 1 
ATOM   2678 C CD2 . LEU B 1 133 ? -0.183  -29.331 23.284  1.00 37.29 ? 135 LEU B CD2 1 
ATOM   2679 N N   . CYS B 1 134 ? -2.533  -24.668 24.938  1.00 36.00 ? 136 CYS B N   1 
ATOM   2680 C CA  . CYS B 1 134 ? -3.139  -23.313 24.796  1.00 36.64 ? 136 CYS B CA  1 
ATOM   2681 C C   . CYS B 1 134 ? -2.170  -22.275 24.356  1.00 38.06 ? 136 CYS B C   1 
ATOM   2682 O O   . CYS B 1 134 ? -2.521  -21.399 23.519  1.00 40.36 ? 136 CYS B O   1 
ATOM   2683 C CB  . CYS B 1 134 ? -3.822  -22.863 26.092  1.00 38.24 ? 136 CYS B CB  1 
ATOM   2684 S SG  . CYS B 1 134 ? -5.337  -23.774 26.497  1.00 46.09 ? 136 CYS B SG  1 
ATOM   2685 N N   . LEU B 1 135 ? -0.975  -22.285 24.952  1.00 35.31 ? 137 LEU B N   1 
ATOM   2686 C CA  . LEU B 1 135 ? 0.076   -21.328 24.644  1.00 33.96 ? 137 LEU B CA  1 
ATOM   2687 C C   . LEU B 1 135 ? 0.564   -21.560 23.186  1.00 33.93 ? 137 LEU B C   1 
ATOM   2688 O O   . LEU B 1 135 ? 0.441   -20.683 22.388  1.00 33.44 ? 137 LEU B O   1 
ATOM   2689 C CB  . LEU B 1 135 ? 1.262   -21.440 25.639  1.00 33.64 ? 137 LEU B CB  1 
ATOM   2690 C CG  . LEU B 1 135 ? 1.228   -20.517 26.897  1.00 35.23 ? 137 LEU B CG  1 
ATOM   2691 C CD1 . LEU B 1 135 ? -0.151  -20.540 27.574  1.00 35.26 ? 137 LEU B CD1 1 
ATOM   2692 C CD2 . LEU B 1 135 ? 2.361   -20.881 27.775  1.00 36.23 ? 137 LEU B CD2 1 
ATOM   2693 N N   . ILE B 1 136 ? 1.099   -22.727 22.892  1.00 33.47 ? 138 ILE B N   1 
ATOM   2694 C CA  . ILE B 1 136 ? 1.792   -22.928 21.618  1.00 34.90 ? 138 ILE B CA  1 
ATOM   2695 C C   . ILE B 1 136 ? 0.798   -22.889 20.435  1.00 37.52 ? 138 ILE B C   1 
ATOM   2696 O O   . ILE B 1 136 ? 1.209   -22.486 19.361  1.00 38.40 ? 138 ILE B O   1 
ATOM   2697 C CB  . ILE B 1 136 ? 2.693   -24.166 21.588  1.00 35.32 ? 138 ILE B CB  1 
ATOM   2698 C CG1 . ILE B 1 136 ? 1.855   -25.468 21.592  1.00 35.69 ? 138 ILE B CG1 1 
ATOM   2699 C CG2 . ILE B 1 136 ? 3.712   -24.139 22.770  1.00 36.62 ? 138 ILE B CG2 1 
ATOM   2700 C CD1 . ILE B 1 136 ? 2.629   -26.716 21.441  1.00 36.14 ? 138 ILE B CD1 1 
ATOM   2701 N N   . GLY B 1 137 ? -0.435  -23.310 20.652  1.00 38.42 ? 139 GLY B N   1 
ATOM   2702 C CA  . GLY B 1 137 ? -1.489  -23.314 19.651  1.00 40.71 ? 139 GLY B CA  1 
ATOM   2703 C C   . GLY B 1 137 ? -2.180  -21.982 19.399  1.00 42.28 ? 139 GLY B C   1 
ATOM   2704 O O   . GLY B 1 137 ? -3.023  -21.923 18.520  1.00 42.39 ? 139 GLY B O   1 
ATOM   2705 N N   . GLU B 1 138 ? -1.831  -20.908 20.162  1.00 43.20 ? 140 GLU B N   1 
ATOM   2706 C CA  . GLU B 1 138 ? -2.424  -19.581 20.064  1.00 43.39 ? 140 GLU B CA  1 
ATOM   2707 C C   . GLU B 1 138 ? -3.948  -19.623 20.182  1.00 43.61 ? 140 GLU B C   1 
ATOM   2708 O O   . GLU B 1 138 ? -4.651  -19.117 19.322  1.00 43.51 ? 140 GLU B O   1 
ATOM   2709 C CB  . GLU B 1 138 ? -1.976  -18.881 18.772  1.00 45.35 ? 140 GLU B CB  1 
ATOM   2710 C CG  . GLU B 1 138 ? -0.469  -18.753 18.601  1.00 46.01 ? 140 GLU B CG  1 
ATOM   2711 C CD  . GLU B 1 138 ? 0.204   -17.718 19.492  1.00 52.01 ? 140 GLU B CD  1 
ATOM   2712 O OE1 . GLU B 1 138 ? -0.342  -16.600 19.608  1.00 53.94 ? 140 GLU B OE1 1 
ATOM   2713 O OE2 . GLU B 1 138 ? 1.288   -18.000 20.053  1.00 52.33 ? 140 GLU B OE2 1 
ATOM   2714 N N   . SER B 1 139 ? -4.442  -20.227 21.283  1.00 44.33 ? 141 SER B N   1 
ATOM   2715 C CA  . SER B 1 139 ? -5.846  -20.595 21.504  1.00 44.47 ? 141 SER B CA  1 
ATOM   2716 C C   . SER B 1 139 ? -6.761  -19.450 21.919  1.00 44.53 ? 141 SER B C   1 
ATOM   2717 O O   . SER B 1 139 ? -7.949  -19.663 22.052  1.00 45.19 ? 141 SER B O   1 
ATOM   2718 C CB  . SER B 1 139 ? -5.924  -21.661 22.592  1.00 45.47 ? 141 SER B CB  1 
ATOM   2719 O OG  . SER B 1 139 ? -5.210  -22.823 22.200  1.00 48.19 ? 141 SER B OG  1 
ATOM   2720 N N   . PHE B 1 140 ? -6.226  -18.274 22.145  1.00 43.34 ? 142 PHE B N   1 
ATOM   2721 C CA  . PHE B 1 140 ? -6.983  -17.135 22.630  1.00 43.89 ? 142 PHE B CA  1 
ATOM   2722 C C   . PHE B 1 140 ? -7.227  -16.087 21.525  1.00 45.95 ? 142 PHE B C   1 
ATOM   2723 O O   . PHE B 1 140 ? -7.496  -14.930 21.849  1.00 47.17 ? 142 PHE B O   1 
ATOM   2724 C CB  . PHE B 1 140 ? -6.214  -16.515 23.817  1.00 41.60 ? 142 PHE B CB  1 
ATOM   2725 C CG  . PHE B 1 140 ? -5.887  -17.524 24.892  1.00 41.69 ? 142 PHE B CG  1 
ATOM   2726 C CD1 . PHE B 1 140 ? -6.889  -18.171 25.586  1.00 41.82 ? 142 PHE B CD1 1 
ATOM   2727 C CD2 . PHE B 1 140 ? -4.584  -17.905 25.135  1.00 41.59 ? 142 PHE B CD2 1 
ATOM   2728 C CE1 . PHE B 1 140 ? -6.582  -19.121 26.551  1.00 41.49 ? 142 PHE B CE1 1 
ATOM   2729 C CE2 . PHE B 1 140 ? -4.288  -18.850 26.100  1.00 40.88 ? 142 PHE B CE2 1 
ATOM   2730 C CZ  . PHE B 1 140 ? -5.272  -19.427 26.825  1.00 39.59 ? 142 PHE B CZ  1 
ATOM   2731 N N   . ASP B 1 141 ? -7.109  -16.483 20.254  1.00 47.42 ? 143 ASP B N   1 
ATOM   2732 C CA  . ASP B 1 141 ? -7.358  -15.624 19.087  1.00 50.31 ? 143 ASP B CA  1 
ATOM   2733 C C   . ASP B 1 141 ? -6.411  -14.367 19.153  1.00 50.31 ? 143 ASP B C   1 
ATOM   2734 O O   . ASP B 1 141 ? -5.232  -14.568 19.466  1.00 50.27 ? 143 ASP B O   1 
ATOM   2735 C CB  . ASP B 1 141 ? -8.890  -15.336 18.979  1.00 56.33 ? 143 ASP B CB  1 
ATOM   2736 C CG  . ASP B 1 141 ? -9.662  -16.572 18.499  1.00 70.16 ? 143 ASP B CG  1 
ATOM   2737 O OD1 . ASP B 1 141 ? -9.271  -17.154 17.449  1.00 72.57 ? 143 ASP B OD1 1 
ATOM   2738 O OD2 . ASP B 1 141 ? -10.654 -16.959 19.171  1.00 74.98 ? 143 ASP B OD2 1 
ATOM   2739 N N   . ASP B 1 142 ? -6.869  -13.129 18.897  1.00 50.32 ? 144 ASP B N   1 
ATOM   2740 C CA  . ASP B 1 142 ? -5.970  -11.962 18.952  1.00 51.09 ? 144 ASP B CA  1 
ATOM   2741 C C   . ASP B 1 142 ? -5.435  -11.728 20.371  1.00 49.32 ? 144 ASP B C   1 
ATOM   2742 O O   . ASP B 1 142 ? -4.372  -11.140 20.508  1.00 50.96 ? 144 ASP B O   1 
ATOM   2743 C CB  . ASP B 1 142 ? -6.681  -10.678 18.504  1.00 55.67 ? 144 ASP B CB  1 
ATOM   2744 C CG  . ASP B 1 142 ? -7.024  -10.609 17.016  1.00 67.44 ? 144 ASP B CG  1 
ATOM   2745 O OD1 . ASP B 1 142 ? -6.724  -11.579 16.290  1.00 69.24 ? 144 ASP B OD1 1 
ATOM   2746 O OD2 . ASP B 1 142 ? -7.593  -9.564  16.577  1.00 73.76 ? 144 ASP B OD2 1 
ATOM   2747 N N   . TYR B 1 143 ? -6.160  -12.167 21.410  1.00 46.90 ? 145 TYR B N   1 
ATOM   2748 C CA  . TYR B 1 143 ? -5.727  -12.003 22.794  1.00 46.13 ? 145 TYR B CA  1 
ATOM   2749 C C   . TYR B 1 143 ? -4.540  -12.915 23.163  1.00 43.83 ? 145 TYR B C   1 
ATOM   2750 O O   . TYR B 1 143 ? -3.967  -12.738 24.233  1.00 43.57 ? 145 TYR B O   1 
ATOM   2751 C CB  . TYR B 1 143 ? -6.909  -12.169 23.741  1.00 47.73 ? 145 TYR B CB  1 
ATOM   2752 C CG  . TYR B 1 143 ? -8.012  -11.168 23.478  1.00 51.65 ? 145 TYR B CG  1 
ATOM   2753 C CD1 . TYR B 1 143 ? -7.722  -9.822  23.275  1.00 53.67 ? 145 TYR B CD1 1 
ATOM   2754 C CD2 . TYR B 1 143 ? -9.343  -11.566 23.399  1.00 53.91 ? 145 TYR B CD2 1 
ATOM   2755 C CE1 . TYR B 1 143 ? -8.719  -8.896  23.058  1.00 55.86 ? 145 TYR B CE1 1 
ATOM   2756 C CE2 . TYR B 1 143 ? -10.355 -10.639 23.175  1.00 55.84 ? 145 TYR B CE2 1 
ATOM   2757 C CZ  . TYR B 1 143 ? -10.034 -9.308  22.990  1.00 58.48 ? 145 TYR B CZ  1 
ATOM   2758 O OH  . TYR B 1 143 ? -10.996 -8.351  22.728  1.00 63.55 ? 145 TYR B OH  1 
ATOM   2759 N N   . SER B 1 144 ? -4.149  -13.850 22.291  1.00 42.92 ? 146 SER B N   1 
ATOM   2760 C CA  . SER B 1 144 ? -2.935  -14.638 22.473  1.00 43.12 ? 146 SER B CA  1 
ATOM   2761 C C   . SER B 1 144 ? -1.708  -13.776 22.517  1.00 43.21 ? 146 SER B C   1 
ATOM   2762 O O   . SER B 1 144 ? -0.731  -14.159 23.163  1.00 42.68 ? 146 SER B O   1 
ATOM   2763 C CB  . SER B 1 144 ? -2.793  -15.686 21.371  1.00 45.80 ? 146 SER B CB  1 
ATOM   2764 O OG  . SER B 1 144 ? -3.671  -16.770 21.612  1.00 47.75 ? 146 SER B OG  1 
ATOM   2765 N N   . ASP B 1 145 ? -1.733  -12.601 21.867  1.00 43.13 ? 147 ASP B N   1 
ATOM   2766 C CA  . ASP B 1 145 ? -0.623  -11.666 21.989  1.00 43.79 ? 147 ASP B CA  1 
ATOM   2767 C C   . ASP B 1 145 ? -0.444  -11.140 23.406  1.00 43.20 ? 147 ASP B C   1 
ATOM   2768 O O   . ASP B 1 145 ? 0.655   -10.697 23.733  1.00 45.21 ? 147 ASP B O   1 
ATOM   2769 C CB  . ASP B 1 145 ? -0.800  -10.469 21.036  1.00 44.90 ? 147 ASP B CB  1 
ATOM   2770 C CG  . ASP B 1 145 ? -0.665  -10.853 19.566  1.00 54.53 ? 147 ASP B CG  1 
ATOM   2771 O OD1 . ASP B 1 145 ? -0.061  -11.924 19.275  1.00 54.63 ? 147 ASP B OD1 1 
ATOM   2772 O OD2 . ASP B 1 145 ? -1.162  -10.084 18.702  1.00 57.79 ? 147 ASP B OD2 1 
ATOM   2773 N N   . ASP B 1 146 ? -1.485  -11.158 24.248  1.00 41.58 ? 148 ASP B N   1 
ATOM   2774 C CA  . ASP B 1 146 ? -1.352  -10.698 25.641  1.00 40.10 ? 148 ASP B CA  1 
ATOM   2775 C C   . ASP B 1 146 ? -0.696  -11.763 26.544  1.00 37.36 ? 148 ASP B C   1 
ATOM   2776 O O   . ASP B 1 146 ? -0.294  -11.425 27.631  1.00 37.02 ? 148 ASP B O   1 
ATOM   2777 C CB  . ASP B 1 146 ? -2.695  -10.252 26.293  1.00 40.72 ? 148 ASP B CB  1 
ATOM   2778 C CG  . ASP B 1 146 ? -3.014  -8.791  25.992  1.00 49.76 ? 148 ASP B CG  1 
ATOM   2779 O OD1 . ASP B 1 146 ? -3.024  -8.441  24.825  1.00 50.52 ? 148 ASP B OD1 1 
ATOM   2780 O OD2 . ASP B 1 146 ? -3.241  -7.994  26.973  1.00 52.18 ? 148 ASP B OD2 1 
ATOM   2781 N N   . VAL B 1 147 ? -0.574  -13.016 26.096  1.00 36.69 ? 149 VAL B N   1 
ATOM   2782 C CA  . VAL B 1 147 ? 0.001   -14.076 26.892  1.00 34.51 ? 149 VAL B CA  1 
ATOM   2783 C C   . VAL B 1 147 ? 1.504   -13.942 26.839  1.00 34.75 ? 149 VAL B C   1 
ATOM   2784 O O   . VAL B 1 147 ? 2.094   -13.766 25.762  1.00 35.73 ? 149 VAL B O   1 
ATOM   2785 C CB  . VAL B 1 147 ? -0.456  -15.469 26.420  1.00 36.50 ? 149 VAL B CB  1 
ATOM   2786 C CG1 . VAL B 1 147 ? 0.262   -16.566 27.188  1.00 37.32 ? 149 VAL B CG1 1 
ATOM   2787 C CG2 . VAL B 1 147 ? -1.958  -15.626 26.609  1.00 38.88 ? 149 VAL B CG2 1 
ATOM   2788 N N   . CYS B 1 148 ? 2.125   -14.008 28.001  1.00 32.22 ? 150 CYS B N   1 
ATOM   2789 C CA  . CYS B 1 148 ? 3.575   -14.026 28.164  1.00 31.87 ? 150 CYS B CA  1 
ATOM   2790 C C   . CYS B 1 148 ? 4.105   -15.472 28.294  1.00 30.28 ? 150 CYS B C   1 
ATOM   2791 O O   . CYS B 1 148 ? 5.102   -15.830 27.688  1.00 30.32 ? 150 CYS B O   1 
ATOM   2792 C CB  . CYS B 1 148 ? 3.961   -13.202 29.379  1.00 32.85 ? 150 CYS B CB  1 
ATOM   2793 S SG  . CYS B 1 148 ? 3.518   -11.456 29.183  1.00 37.39 ? 150 CYS B SG  1 
ATOM   2794 N N   . GLY B 1 149 ? 3.422   -16.274 29.085  1.00 29.46 ? 151 GLY B N   1 
ATOM   2795 C CA  . GLY B 1 149 ? 3.866   -17.644 29.344  1.00 28.68 ? 151 GLY B CA  1 
ATOM   2796 C C   . GLY B 1 149 ? 3.043   -18.284 30.410  1.00 28.23 ? 151 GLY B C   1 
ATOM   2797 O O   . GLY B 1 149 ? 1.981   -17.785 30.748  1.00 28.83 ? 151 GLY B O   1 
ATOM   2798 N N   . ALA B 1 150 ? 3.490   -19.427 30.878  1.00 28.22 ? 152 ALA B N   1 
ATOM   2799 C CA  . ALA B 1 150 ? 2.850   -20.196 31.921  1.00 29.08 ? 152 ALA B CA  1 
ATOM   2800 C C   . ALA B 1 150 ? 3.879   -20.755 32.843  1.00 29.25 ? 152 ALA B C   1 
ATOM   2801 O O   . ALA B 1 150 ? 5.027   -20.981 32.463  1.00 30.16 ? 152 ALA B O   1 
ATOM   2802 C CB  . ALA B 1 150 ? 1.984   -21.335 31.325  1.00 29.05 ? 152 ALA B CB  1 
ATOM   2803 N N   . VAL B 1 151 ? 3.466   -20.991 34.083  1.00 29.22 ? 153 VAL B N   1 
ATOM   2804 C CA  . VAL B 1 151 ? 4.374   -21.457 35.149  1.00 30.61 ? 153 VAL B CA  1 
ATOM   2805 C C   . VAL B 1 151 ? 3.674   -22.549 35.928  1.00 31.63 ? 153 VAL B C   1 
ATOM   2806 O O   . VAL B 1 151 ? 2.499   -22.395 36.266  1.00 30.83 ? 153 VAL B O   1 
ATOM   2807 C CB  . VAL B 1 151 ? 4.765   -20.293 36.099  1.00 30.85 ? 153 VAL B CB  1 
ATOM   2808 C CG1 . VAL B 1 151 ? 5.616   -20.796 37.267  1.00 33.07 ? 153 VAL B CG1 1 
ATOM   2809 C CG2 . VAL B 1 151 ? 5.433   -19.112 35.354  1.00 30.79 ? 153 VAL B CG2 1 
ATOM   2810 N N   . VAL B 1 152 ? 4.382   -23.641 36.200  1.00 32.35 ? 154 VAL B N   1 
ATOM   2811 C CA  . VAL B 1 152 ? 3.924   -24.636 37.186  1.00 32.05 ? 154 VAL B CA  1 
ATOM   2812 C C   . VAL B 1 152 ? 4.877   -24.633 38.376  1.00 32.92 ? 154 VAL B C   1 
ATOM   2813 O O   . VAL B 1 152 ? 6.080   -24.751 38.195  1.00 33.66 ? 154 VAL B O   1 
ATOM   2814 C CB  . VAL B 1 152 ? 3.703   -26.060 36.553  1.00 34.10 ? 154 VAL B CB  1 
ATOM   2815 C CG1 . VAL B 1 152 ? 4.939   -26.567 35.829  1.00 35.17 ? 154 VAL B CG1 1 
ATOM   2816 C CG2 . VAL B 1 152 ? 3.245   -27.057 37.605  1.00 35.84 ? 154 VAL B CG2 1 
ATOM   2817 N N   . ASN B 1 153 ? 4.341   -24.467 39.580  1.00 34.53 ? 155 ASN B N   1 
ATOM   2818 C CA  . ASN B 1 153 ? 5.079   -24.553 40.828  1.00 37.59 ? 155 ASN B CA  1 
ATOM   2819 C C   . ASN B 1 153 ? 4.708   -25.871 41.509  1.00 40.44 ? 155 ASN B C   1 
ATOM   2820 O O   . ASN B 1 153 ? 3.559   -26.065 41.916  1.00 40.72 ? 155 ASN B O   1 
ATOM   2821 C CB  . ASN B 1 153 ? 4.720   -23.432 41.769  1.00 39.48 ? 155 ASN B CB  1 
ATOM   2822 C CG  . ASN B 1 153 ? 4.766   -22.042 41.171  1.00 43.10 ? 155 ASN B CG  1 
ATOM   2823 O OD1 . ASN B 1 153 ? 3.767   -21.388 40.990  1.00 44.77 ? 155 ASN B OD1 1 
ATOM   2824 N ND2 . ASN B 1 153 ? 5.926   -21.576 40.899  1.00 42.36 ? 155 ASN B ND2 1 
ATOM   2825 N N   . VAL B 1 154 ? 5.665   -26.754 41.606  1.00 42.63 ? 156 VAL B N   1 
ATOM   2826 C CA  . VAL B 1 154 ? 5.422   -28.054 42.243  1.00 46.62 ? 156 VAL B CA  1 
ATOM   2827 C C   . VAL B 1 154 ? 5.788   -27.901 43.720  1.00 49.07 ? 156 VAL B C   1 
ATOM   2828 O O   . VAL B 1 154 ? 6.930   -27.568 44.027  1.00 50.09 ? 156 VAL B O   1 
ATOM   2829 C CB  . VAL B 1 154 ? 6.185   -29.168 41.517  1.00 48.57 ? 156 VAL B CB  1 
ATOM   2830 C CG1 . VAL B 1 154 ? 5.839   -30.540 42.108  1.00 50.35 ? 156 VAL B CG1 1 
ATOM   2831 C CG2 . VAL B 1 154 ? 5.887   -29.146 40.023  1.00 48.71 ? 156 VAL B CG2 1 
ATOM   2832 N N   . ARG B 1 155 ? 4.831   -28.113 44.629  1.00 51.32 ? 157 ARG B N   1 
ATOM   2833 C CA  . ARG B 1 155 ? 5.061   -27.885 46.064  1.00 53.49 ? 157 ARG B CA  1 
ATOM   2834 C C   . ARG B 1 155 ? 4.394   -28.969 46.895  1.00 57.32 ? 157 ARG B C   1 
ATOM   2835 O O   . ARG B 1 155 ? 3.353   -29.508 46.514  1.00 58.21 ? 157 ARG B O   1 
ATOM   2836 C CB  . ARG B 1 155 ? 4.494   -26.538 46.532  1.00 53.83 ? 157 ARG B CB  1 
ATOM   2837 C CG  . ARG B 1 155 ? 5.122   -25.299 45.961  1.00 54.58 ? 157 ARG B CG  1 
ATOM   2838 C CD  . ARG B 1 155 ? 6.572   -25.106 46.346  1.00 55.71 ? 157 ARG B CD  1 
ATOM   2839 N NE  . ARG B 1 155 ? 7.055   -23.857 45.751  1.00 59.99 ? 157 ARG B NE  1 
ATOM   2840 C CZ  . ARG B 1 155 ? 7.527   -23.707 44.520  1.00 55.78 ? 157 ARG B CZ  1 
ATOM   2841 N NH1 . ARG B 1 155 ? 7.612   -24.750 43.698  1.00 54.77 ? 157 ARG B NH1 1 
ATOM   2842 N NH2 . ARG B 1 155 ? 7.922   -22.514 44.102  1.00 54.37 ? 157 ARG B NH2 1 
ATOM   2843 N N   . ALA B 1 156 ? 4.986   -29.285 48.036  1.00 58.72 ? 158 ALA B N   1 
ATOM   2844 C CA  . ALA B 1 156 ? 4.408   -30.267 48.960  1.00 60.40 ? 158 ALA B CA  1 
ATOM   2845 C C   . ALA B 1 156 ? 2.943   -29.926 49.359  1.00 60.68 ? 158 ALA B C   1 
ATOM   2846 O O   . ALA B 1 156 ? 2.083   -30.801 49.309  1.00 61.30 ? 158 ALA B O   1 
ATOM   2847 C CB  . ALA B 1 156 ? 5.290   -30.374 50.210  1.00 61.28 ? 158 ALA B CB  1 
ATOM   2848 N N   . LYS B 1 157 ? 2.665   -28.666 49.724  1.00 60.70 ? 159 LYS B N   1 
ATOM   2849 C CA  . LYS B 1 157 ? 1.340   -28.218 50.152  1.00 61.21 ? 159 LYS B CA  1 
ATOM   2850 C C   . LYS B 1 157 ? 0.267   -28.145 49.040  1.00 58.86 ? 159 LYS B C   1 
ATOM   2851 O O   . LYS B 1 157 ? -0.926  -28.027 49.354  1.00 59.26 ? 159 LYS B O   1 
ATOM   2852 C CB  . LYS B 1 157 ? 1.452   -26.832 50.815  1.00 65.89 ? 159 LYS B CB  1 
ATOM   2853 C CG  . LYS B 1 157 ? 0.250   -26.472 51.703  1.00 73.30 ? 159 LYS B CG  1 
ATOM   2854 C CD  . LYS B 1 157 ? 0.447   -25.166 52.486  1.00 79.57 ? 159 LYS B CD  1 
ATOM   2855 C CE  . LYS B 1 157 ? -0.470  -25.083 53.685  1.00 84.35 ? 159 LYS B CE  1 
ATOM   2856 N NZ  . LYS B 1 157 ? 0.012   -25.927 54.831  1.00 87.51 ? 159 LYS B NZ  1 
ATOM   2857 N N   . GLY B 1 158 ? 0.670   -28.205 47.774  1.00 55.72 ? 160 GLY B N   1 
ATOM   2858 C CA  . GLY B 1 158 ? -0.276  -28.112 46.671  1.00 53.49 ? 160 GLY B CA  1 
ATOM   2859 C C   . GLY B 1 158 ? 0.331   -27.389 45.486  1.00 50.94 ? 160 GLY B C   1 
ATOM   2860 O O   . GLY B 1 158 ? 1.018   -26.383 45.657  1.00 51.81 ? 160 GLY B O   1 
ATOM   2861 N N   . ASP B 1 159 ? 0.061   -27.875 44.291  1.00 47.79 ? 161 ASP B N   1 
ATOM   2862 C CA  . ASP B 1 159 ? 0.760   -27.384 43.086  1.00 44.80 ? 161 ASP B CA  1 
ATOM   2863 C C   . ASP B 1 159 ? -0.027  -26.208 42.529  1.00 41.15 ? 161 ASP B C   1 
ATOM   2864 O O   . ASP B 1 159 ? -1.199  -26.103 42.781  1.00 40.44 ? 161 ASP B O   1 
ATOM   2865 C CB  . ASP B 1 159 ? 0.849   -28.504 42.064  1.00 46.88 ? 161 ASP B CB  1 
ATOM   2866 C CG  . ASP B 1 159 ? 1.508   -29.789 42.591  1.00 58.00 ? 161 ASP B CG  1 
ATOM   2867 O OD1 . ASP B 1 159 ? 2.656   -29.713 43.120  1.00 59.35 ? 161 ASP B OD1 1 
ATOM   2868 O OD2 . ASP B 1 159 ? 0.879   -30.861 42.478  1.00 61.64 ? 161 ASP B OD2 1 
ATOM   2869 N N   . LYS B 1 160 ? 0.621   -25.319 41.776  1.00 38.76 ? 162 LYS B N   1 
ATOM   2870 C CA  . LYS B 1 160 ? -0.039  -24.153 41.209  1.00 38.71 ? 162 LYS B CA  1 
ATOM   2871 C C   . LYS B 1 160 ? 0.325   -24.129 39.724  1.00 36.51 ? 162 LYS B C   1 
ATOM   2872 O O   . LYS B 1 160 ? 1.468   -24.404 39.405  1.00 36.74 ? 162 LYS B O   1 
ATOM   2873 C CB  . LYS B 1 160 ? 0.480   -22.866 41.876  1.00 40.41 ? 162 LYS B CB  1 
ATOM   2874 C CG  . LYS B 1 160 ? 0.144   -22.676 43.359  1.00 47.39 ? 162 LYS B CG  1 
ATOM   2875 C CD  . LYS B 1 160 ? 0.220   -21.187 43.674  1.00 56.33 ? 162 LYS B CD  1 
ATOM   2876 C CE  . LYS B 1 160 ? 0.909   -20.721 44.944  1.00 64.48 ? 162 LYS B CE  1 
ATOM   2877 N NZ  . LYS B 1 160 ? 1.034   -19.208 44.921  1.00 68.07 ? 162 LYS B NZ  1 
ATOM   2878 N N   . ILE B 1 161 ? -0.625  -23.836 38.847  1.00 34.64 ? 163 ILE B N   1 
ATOM   2879 C CA  . ILE B 1 161 ? -0.369  -23.636 37.411  1.00 35.19 ? 163 ILE B CA  1 
ATOM   2880 C C   . ILE B 1 161 ? -0.952  -22.266 37.119  1.00 33.72 ? 163 ILE B C   1 
ATOM   2881 O O   . ILE B 1 161 ? -2.030  -21.956 37.597  1.00 33.34 ? 163 ILE B O   1 
ATOM   2882 C CB  . ILE B 1 161 ? -0.998  -24.697 36.508  1.00 35.81 ? 163 ILE B CB  1 
ATOM   2883 C CG1 . ILE B 1 161 ? -0.477  -26.083 36.873  1.00 36.51 ? 163 ILE B CG1 1 
ATOM   2884 C CG2 . ILE B 1 161 ? -0.719  -24.349 35.040  1.00 36.24 ? 163 ILE B CG2 1 
ATOM   2885 C CD1 . ILE B 1 161 ? -1.144  -27.238 36.231  1.00 36.19 ? 163 ILE B CD1 1 
ATOM   2886 N N   . ALA B 1 162 ? -0.233  -21.464 36.342  1.00 32.93 ? 164 ALA B N   1 
ATOM   2887 C CA  . ALA B 1 162 ? -0.667  -20.113 36.036  1.00 33.12 ? 164 ALA B CA  1 
ATOM   2888 C C   . ALA B 1 162 ? -0.358  -19.723 34.589  1.00 34.03 ? 164 ALA B C   1 
ATOM   2889 O O   . ALA B 1 162 ? 0.692   -20.106 34.087  1.00 33.22 ? 164 ALA B O   1 
ATOM   2890 C CB  . ALA B 1 162 ? -0.033  -19.143 36.996  1.00 33.08 ? 164 ALA B CB  1 
ATOM   2891 N N   . ILE B 1 163 ? -1.257  -18.982 33.926  1.00 34.09 ? 165 ILE B N   1 
ATOM   2892 C CA  . ILE B 1 163 ? -0.950  -18.298 32.678  1.00 32.47 ? 165 ILE B CA  1 
ATOM   2893 C C   . ILE B 1 163 ? -0.687  -16.853 32.999  1.00 32.18 ? 165 ILE B C   1 
ATOM   2894 O O   . ILE B 1 163 ? -1.547  -16.188 33.576  1.00 31.96 ? 165 ILE B O   1 
ATOM   2895 C CB  . ILE B 1 163 ? -2.062  -18.466 31.596  1.00 32.00 ? 165 ILE B CB  1 
ATOM   2896 C CG1 . ILE B 1 163 ? -2.134  -19.925 31.124  1.00 34.24 ? 165 ILE B CG1 1 
ATOM   2897 C CG2 . ILE B 1 163 ? -1.801  -17.517 30.403  1.00 31.40 ? 165 ILE B CG2 1 
ATOM   2898 C CD1 . ILE B 1 163 ? -3.187  -20.212 30.035  1.00 36.38 ? 165 ILE B CD1 1 
ATOM   2899 N N   . TRP B 1 164 ? 0.457   -16.365 32.598  1.00 31.52 ? 166 TRP B N   1 
ATOM   2900 C CA  . TRP B 1 164 ? 0.873   -14.974 32.810  1.00 32.21 ? 166 TRP B CA  1 
ATOM   2901 C C   . TRP B 1 164 ? 0.538   -14.146 31.575  1.00 32.66 ? 166 TRP B C   1 
ATOM   2902 O O   . TRP B 1 164 ? 0.784   -14.550 30.435  1.00 34.05 ? 166 TRP B O   1 
ATOM   2903 C CB  . TRP B 1 164 ? 2.383   -14.915 33.053  1.00 32.30 ? 166 TRP B CB  1 
ATOM   2904 C CG  . TRP B 1 164 ? 2.869   -15.431 34.373  1.00 32.51 ? 166 TRP B CG  1 
ATOM   2905 C CD1 . TRP B 1 164 ? 2.338   -16.441 35.132  1.00 32.82 ? 166 TRP B CD1 1 
ATOM   2906 C CD2 . TRP B 1 164 ? 4.005   -14.926 35.100  1.00 33.10 ? 166 TRP B CD2 1 
ATOM   2907 N NE1 . TRP B 1 164 ? 3.046   -16.565 36.306  1.00 32.56 ? 166 TRP B NE1 1 
ATOM   2908 C CE2 . TRP B 1 164 ? 4.114   -15.686 36.283  1.00 33.42 ? 166 TRP B CE2 1 
ATOM   2909 C CE3 . TRP B 1 164 ? 4.989   -13.957 34.813  1.00 32.24 ? 166 TRP B CE3 1 
ATOM   2910 C CZ2 . TRP B 1 164 ? 5.138   -15.468 37.201  1.00 35.18 ? 166 TRP B CZ2 1 
ATOM   2911 C CZ3 . TRP B 1 164 ? 6.002   -13.743 35.709  1.00 34.30 ? 166 TRP B CZ3 1 
ATOM   2912 C CH2 . TRP B 1 164 ? 6.088   -14.486 36.882  1.00 35.05 ? 166 TRP B CH2 1 
ATOM   2913 N N   . THR B 1 165 ? -0.009  -12.963 31.818  1.00 31.77 ? 167 THR B N   1 
ATOM   2914 C CA  . THR B 1 165 ? -0.364  -12.039 30.771  1.00 32.71 ? 167 THR B CA  1 
ATOM   2915 C C   . THR B 1 165 ? 0.292   -10.680 31.036  1.00 33.61 ? 167 THR B C   1 
ATOM   2916 O O   . THR B 1 165 ? 0.718   -10.361 32.162  1.00 33.44 ? 167 THR B O   1 
ATOM   2917 C CB  . THR B 1 165 ? -1.889  -11.949 30.580  1.00 35.20 ? 167 THR B CB  1 
ATOM   2918 O OG1 . THR B 1 165 ? -2.399  -11.043 31.550  1.00 35.92 ? 167 THR B OG1 1 
ATOM   2919 C CG2 . THR B 1 165 ? -2.607  -13.266 30.649  1.00 35.90 ? 167 THR B CG2 1 
ATOM   2920 N N   . THR B 1 166 ? 0.362   -9.877  29.978  1.00 35.00 ? 168 THR B N   1 
ATOM   2921 C CA  . THR B 1 166 ? 1.209   -8.712  29.923  1.00 37.08 ? 168 THR B CA  1 
ATOM   2922 C C   . THR B 1 166 ? 0.618   -7.430  30.562  1.00 39.42 ? 168 THR B C   1 
ATOM   2923 O O   . THR B 1 166 ? 1.398   -6.542  31.008  1.00 37.13 ? 168 THR B O   1 
ATOM   2924 C CB  . THR B 1 166 ? 1.626   -8.456  28.449  1.00 38.61 ? 168 THR B CB  1 
ATOM   2925 O OG1 . THR B 1 166 ? 2.749   -7.562  28.443  1.00 40.61 ? 168 THR B OG1 1 
ATOM   2926 C CG2 . THR B 1 166 ? 0.469   -7.905  27.602  1.00 37.63 ? 168 THR B CG2 1 
ATOM   2927 N N   . GLU B 1 167 ? -0.725  -7.317  30.613  1.00 39.55 ? 169 GLU B N   1 
ATOM   2928 C CA  . GLU B 1 167 ? -1.356  -6.042  31.020  1.00 39.46 ? 169 GLU B CA  1 
ATOM   2929 C C   . GLU B 1 167 ? -2.602  -6.331  31.847  1.00 39.09 ? 169 GLU B C   1 
ATOM   2930 O O   . GLU B 1 167 ? -3.631  -6.744  31.318  1.00 38.21 ? 169 GLU B O   1 
ATOM   2931 C CB  . GLU B 1 167 ? -1.717  -5.245  29.792  1.00 42.73 ? 169 GLU B CB  1 
ATOM   2932 C CG  . GLU B 1 167 ? -2.362  -3.879  30.102  1.00 48.21 ? 169 GLU B CG  1 
ATOM   2933 C CD  . GLU B 1 167 ? -1.657  -3.080  31.159  1.00 49.04 ? 169 GLU B CD  1 
ATOM   2934 O OE1 . GLU B 1 167 ? -0.533  -2.619  30.883  1.00 54.34 ? 169 GLU B OE1 1 
ATOM   2935 O OE2 . GLU B 1 167 ? -2.207  -2.941  32.269  1.00 46.38 ? 169 GLU B OE2 1 
ATOM   2936 N N   . CYS B 1 168 ? -2.480  -6.121  33.178  1.00 39.04 ? 170 CYS B N   1 
ATOM   2937 C CA  . CYS B 1 168 ? -3.554  -6.430  34.093  1.00 40.90 ? 170 CYS B CA  1 
ATOM   2938 C C   . CYS B 1 168 ? -4.773  -5.512  33.908  1.00 41.81 ? 170 CYS B C   1 
ATOM   2939 O O   . CYS B 1 168 ? -5.804  -5.874  34.445  1.00 42.71 ? 170 CYS B O   1 
ATOM   2940 C CB  . CYS B 1 168 ? -3.052  -6.457  35.553  1.00 42.18 ? 170 CYS B CB  1 
ATOM   2941 S SG  . CYS B 1 168 ? -2.468  -4.856  36.177  1.00 59.61 ? 170 CYS B SG  1 
ATOM   2942 N N   . GLU B 1 169 ? -4.686  -4.346  33.170  1.00 41.90 ? 171 GLU B N   1 
ATOM   2943 C CA  . GLU B 1 169 ? -5.840  -3.484  32.909  1.00 42.80 ? 171 GLU B CA  1 
ATOM   2944 C C   . GLU B 1 169 ? -6.586  -3.781  31.616  1.00 42.73 ? 171 GLU B C   1 
ATOM   2945 O O   . GLU B 1 169 ? -7.587  -3.119  31.351  1.00 42.20 ? 171 GLU B O   1 
ATOM   2946 C CB  . GLU B 1 169 ? -5.427  -2.003  32.955  1.00 42.46 ? 171 GLU B CB  1 
ATOM   2947 C CG  . GLU B 1 169 ? -4.776  -1.615  34.245  1.00 45.62 ? 171 GLU B CG  1 
ATOM   2948 C CD  . GLU B 1 169 ? -5.514  -1.833  35.558  1.00 50.16 ? 171 GLU B CD  1 
ATOM   2949 O OE1 . GLU B 1 169 ? -6.757  -1.999  35.578  1.00 44.59 ? 171 GLU B OE1 1 
ATOM   2950 O OE2 . GLU B 1 169 ? -4.825  -1.763  36.604  1.00 51.19 ? 171 GLU B OE2 1 
ATOM   2951 N N   . ASN B 1 170 ? -6.132  -4.760  30.816  1.00 41.50 ? 172 ASN B N   1 
ATOM   2952 C CA  . ASN B 1 170 ? -6.832  -5.153  29.602  1.00 41.72 ? 172 ASN B CA  1 
ATOM   2953 C C   . ASN B 1 170 ? -7.848  -6.199  29.984  1.00 41.58 ? 172 ASN B C   1 
ATOM   2954 O O   . ASN B 1 170 ? -7.651  -7.388  29.748  1.00 40.62 ? 172 ASN B O   1 
ATOM   2955 C CB  . ASN B 1 170 ? -5.874  -5.696  28.534  1.00 43.43 ? 172 ASN B CB  1 
ATOM   2956 C CG  . ASN B 1 170 ? -5.148  -4.635  27.759  1.00 47.55 ? 172 ASN B CG  1 
ATOM   2957 O OD1 . ASN B 1 170 ? -5.443  -3.410  27.821  1.00 44.97 ? 172 ASN B OD1 1 
ATOM   2958 N ND2 . ASN B 1 170 ? -4.174  -5.112  26.978  1.00 49.48 ? 172 ASN B ND2 1 
ATOM   2959 N N   . ARG B 1 171 ? -8.940  -5.718  30.620  1.00 42.03 ? 173 ARG B N   1 
ATOM   2960 C CA  . ARG B 1 171 ? -10.034 -6.563  31.096  1.00 42.79 ? 173 ARG B CA  1 
ATOM   2961 C C   . ARG B 1 171 ? -10.570 -7.524  30.032  1.00 42.65 ? 173 ARG B C   1 
ATOM   2962 O O   . ARG B 1 171 ? -10.723 -8.717  30.316  1.00 40.84 ? 173 ARG B O   1 
ATOM   2963 C CB  . ARG B 1 171 ? -11.197 -5.727  31.664  1.00 45.62 ? 173 ARG B CB  1 
ATOM   2964 C CG  . ARG B 1 171 ? -12.285 -6.608  32.297  1.00 49.66 ? 173 ARG B CG  1 
ATOM   2965 C CD  . ARG B 1 171 ? -13.169 -5.854  33.294  1.00 57.55 ? 173 ARG B CD  1 
ATOM   2966 N NE  . ARG B 1 171 ? -13.773 -6.790  34.256  1.00 64.54 ? 173 ARG B NE  1 
ATOM   2967 C CZ  . ARG B 1 171 ? -14.211 -6.493  35.481  1.00 67.59 ? 173 ARG B CZ  1 
ATOM   2968 N NH1 . ARG B 1 171 ? -14.137 -5.242  35.945  1.00 67.27 ? 173 ARG B NH1 1 
ATOM   2969 N NH2 . ARG B 1 171 ? -14.733 -7.440  36.251  1.00 67.69 ? 173 ARG B NH2 1 
ATOM   2970 N N   . GLU B 1 172 ? -10.870 -7.029  28.819  1.00 43.46 ? 174 GLU B N   1 
ATOM   2971 C CA  . GLU B 1 172 ? -11.475 -7.867  27.768  1.00 43.81 ? 174 GLU B CA  1 
ATOM   2972 C C   . GLU B 1 172 ? -10.502 -9.030  27.323  1.00 43.34 ? 174 GLU B C   1 
ATOM   2973 O O   . GLU B 1 172 ? -10.955 -10.167 27.116  1.00 43.13 ? 174 GLU B O   1 
ATOM   2974 C CB  . GLU B 1 172 ? -11.932 -6.985  26.560  1.00 48.13 ? 174 GLU B CB  1 
ATOM   2975 C CG  . GLU B 1 172 ? -12.353 -7.736  25.303  1.00 59.19 ? 174 GLU B CG  1 
ATOM   2976 C CD  . GLU B 1 172 ? -13.568 -8.650  25.349  1.00 76.53 ? 174 GLU B CD  1 
ATOM   2977 O OE1 . GLU B 1 172 ? -13.766 -9.342  26.378  1.00 82.80 ? 174 GLU B OE1 1 
ATOM   2978 O OE2 . GLU B 1 172 ? -14.319 -8.681  24.340  1.00 79.54 ? 174 GLU B OE2 1 
ATOM   2979 N N   . ALA B 1 173 ? -9.186  -8.750  27.198  1.00 42.59 ? 175 ALA B N   1 
ATOM   2980 C CA  . ALA B 1 173 ? -8.196  -9.798  26.896  1.00 42.00 ? 175 ALA B CA  1 
ATOM   2981 C C   . ALA B 1 173 ? -8.083  -10.798 28.057  1.00 41.09 ? 175 ALA B C   1 
ATOM   2982 O O   . ALA B 1 173 ? -8.097  -12.007 27.825  1.00 40.20 ? 175 ALA B O   1 
ATOM   2983 C CB  . ALA B 1 173 ? -6.846  -9.175  26.613  1.00 41.49 ? 175 ALA B CB  1 
ATOM   2984 N N   . VAL B 1 174 ? -7.988  -10.293 29.292  1.00 40.66 ? 176 VAL B N   1 
ATOM   2985 C CA  . VAL B 1 174 ? -7.705  -11.113 30.438  1.00 39.86 ? 176 VAL B CA  1 
ATOM   2986 C C   . VAL B 1 174 ? -8.859  -12.065 30.686  1.00 40.16 ? 176 VAL B C   1 
ATOM   2987 O O   . VAL B 1 174 ? -8.620  -13.253 30.895  1.00 40.65 ? 176 VAL B O   1 
ATOM   2988 C CB  . VAL B 1 174 ? -7.387  -10.220 31.675  1.00 39.74 ? 176 VAL B CB  1 
ATOM   2989 C CG1 . VAL B 1 174 ? -7.371  -11.077 32.947  1.00 40.54 ? 176 VAL B CG1 1 
ATOM   2990 C CG2 . VAL B 1 174 ? -6.049  -9.491  31.491  1.00 39.15 ? 176 VAL B CG2 1 
ATOM   2991 N N   . THR B 1 175 ? -10.111 -11.558 30.642  1.00 41.82 ? 177 THR B N   1 
ATOM   2992 C CA  . THR B 1 175 ? -11.300 -12.375 30.880  1.00 44.05 ? 177 THR B CA  1 
ATOM   2993 C C   . THR B 1 175 ? -11.567 -13.400 29.741  1.00 44.52 ? 177 THR B C   1 
ATOM   2994 O O   . THR B 1 175 ? -12.048 -14.497 30.035  1.00 44.63 ? 177 THR B O   1 
ATOM   2995 C CB  . THR B 1 175 ? -12.569 -11.517 31.173  1.00 48.05 ? 177 THR B CB  1 
ATOM   2996 O OG1 . THR B 1 175 ? -12.831 -10.686 30.077  1.00 51.00 ? 177 THR B OG1 1 
ATOM   2997 C CG2 . THR B 1 175 ? -12.426 -10.691 32.393  1.00 48.03 ? 177 THR B CG2 1 
ATOM   2998 N N   . HIS B 1 176 ? -11.273 -13.055 28.479  1.00 44.38 ? 178 HIS B N   1 
ATOM   2999 C CA  . HIS B 1 176 ? -11.404 -14.019 27.380  1.00 43.84 ? 178 HIS B CA  1 
ATOM   3000 C C   . HIS B 1 176 ? -10.406 -15.165 27.552  1.00 42.31 ? 178 HIS B C   1 
ATOM   3001 O O   . HIS B 1 176 ? -10.775 -16.345 27.435  1.00 42.35 ? 178 HIS B O   1 
ATOM   3002 C CB  . HIS B 1 176 ? -11.137 -13.321 26.034  1.00 46.59 ? 178 HIS B CB  1 
ATOM   3003 C CG  . HIS B 1 176 ? -11.244 -14.223 24.849  1.00 50.44 ? 178 HIS B CG  1 
ATOM   3004 N ND1 . HIS B 1 176 ? -10.155 -14.927 24.368  1.00 53.03 ? 178 HIS B ND1 1 
ATOM   3005 C CD2 . HIS B 1 176 ? -12.308 -14.497 24.070  1.00 52.91 ? 178 HIS B CD2 1 
ATOM   3006 C CE1 . HIS B 1 176 ? -10.597 -15.614 23.323  1.00 52.76 ? 178 HIS B CE1 1 
ATOM   3007 N NE2 . HIS B 1 176 ? -11.884 -15.404 23.118  1.00 53.50 ? 178 HIS B NE2 1 
ATOM   3008 N N   . ILE B 1 177 ? -9.125  -14.836 27.837  1.00 40.77 ? 179 ILE B N   1 
ATOM   3009 C CA  . ILE B 1 177 ? -8.069  -15.830 28.149  1.00 39.32 ? 179 ILE B CA  1 
ATOM   3010 C C   . ILE B 1 177 ? -8.524  -16.713 29.290  1.00 39.98 ? 179 ILE B C   1 
ATOM   3011 O O   . ILE B 1 177 ? -8.484  -17.936 29.166  1.00 40.06 ? 179 ILE B O   1 
ATOM   3012 C CB  . ILE B 1 177 ? -6.703  -15.158 28.452  1.00 37.96 ? 179 ILE B CB  1 
ATOM   3013 C CG1 . ILE B 1 177 ? -6.166  -14.447 27.203  1.00 38.27 ? 179 ILE B CG1 1 
ATOM   3014 C CG2 . ILE B 1 177 ? -5.679  -16.169 29.015  1.00 37.01 ? 179 ILE B CG2 1 
ATOM   3015 C CD1 . ILE B 1 177 ? -5.028  -13.372 27.521  1.00 38.59 ? 179 ILE B CD1 1 
ATOM   3016 N N   . GLY B 1 178 ? -8.996  -16.108 30.379  1.00 38.83 ? 180 GLY B N   1 
ATOM   3017 C CA  . GLY B 1 178 ? -9.431  -16.868 31.550  1.00 39.35 ? 180 GLY B CA  1 
ATOM   3018 C C   . GLY B 1 178 ? -10.545 -17.835 31.205  1.00 41.44 ? 180 GLY B C   1 
ATOM   3019 O O   . GLY B 1 178 ? -10.495 -19.020 31.582  1.00 40.77 ? 180 GLY B O   1 
ATOM   3020 N N   . ARG B 1 179 ? -11.550 -17.356 30.433  1.00 41.54 ? 181 ARG B N   1 
ATOM   3021 C CA  . ARG B 1 179 ? -12.686 -18.236 30.098  1.00 42.57 ? 181 ARG B CA  1 
ATOM   3022 C C   . ARG B 1 179 ? -12.313 -19.341 29.110  1.00 43.41 ? 181 ARG B C   1 
ATOM   3023 O O   . ARG B 1 179 ? -12.822 -20.433 29.238  1.00 44.66 ? 181 ARG B O   1 
ATOM   3024 C CB  . ARG B 1 179 ? -13.919 -17.426 29.620  1.00 46.01 ? 181 ARG B CB  1 
ATOM   3025 C CG  . ARG B 1 179 ? -14.618 -16.721 30.783  1.00 51.81 ? 181 ARG B CG  1 
ATOM   3026 C CD  . ARG B 1 179 ? -15.542 -15.629 30.365  1.00 59.93 ? 181 ARG B CD  1 
ATOM   3027 N NE  . ARG B 1 179 ? -16.198 -15.056 31.544  1.00 64.88 ? 181 ARG B NE  1 
ATOM   3028 C CZ  . ARG B 1 179 ? -16.518 -13.775 31.718  1.00 70.93 ? 181 ARG B CZ  1 
ATOM   3029 N NH1 . ARG B 1 179 ? -17.104 -13.377 32.842  1.00 73.44 ? 181 ARG B NH1 1 
ATOM   3030 N NH2 . ARG B 1 179 ? -16.259 -12.879 30.770  1.00 71.90 ? 181 ARG B NH2 1 
ATOM   3031 N N   . VAL B 1 180 ? -11.467 -19.091 28.110  1.00 43.33 ? 182 VAL B N   1 
ATOM   3032 C CA  . VAL B 1 180 ? -10.988 -20.154 27.200  1.00 43.86 ? 182 VAL B CA  1 
ATOM   3033 C C   . VAL B 1 180 ? -10.107 -21.126 27.949  1.00 43.24 ? 182 VAL B C   1 
ATOM   3034 O O   . VAL B 1 180 ? -10.218 -22.344 27.761  1.00 44.18 ? 182 VAL B O   1 
ATOM   3035 C CB  . VAL B 1 180 ? -10.229 -19.545 26.016  1.00 45.17 ? 182 VAL B CB  1 
ATOM   3036 C CG1 . VAL B 1 180 ? -9.609  -20.611 25.138  1.00 47.14 ? 182 VAL B CG1 1 
ATOM   3037 C CG2 . VAL B 1 180 ? -11.151 -18.645 25.197  1.00 46.34 ? 182 VAL B CG2 1 
ATOM   3038 N N   . TYR B 1 181 ? -9.223  -20.599 28.818  1.00 40.66 ? 183 TYR B N   1 
ATOM   3039 C CA  . TYR B 1 181 ? -8.400  -21.448 29.649  1.00 39.78 ? 183 TYR B CA  1 
ATOM   3040 C C   . TYR B 1 181 ? -9.234  -22.396 30.523  1.00 39.56 ? 183 TYR B C   1 
ATOM   3041 O O   . TYR B 1 181 ? -9.065  -23.598 30.461  1.00 38.69 ? 183 TYR B O   1 
ATOM   3042 C CB  . TYR B 1 181 ? -7.480  -20.578 30.509  1.00 38.63 ? 183 TYR B CB  1 
ATOM   3043 C CG  . TYR B 1 181 ? -6.439  -21.335 31.310  1.00 37.45 ? 183 TYR B CG  1 
ATOM   3044 C CD1 . TYR B 1 181 ? -5.837  -22.476 30.808  1.00 37.69 ? 183 TYR B CD1 1 
ATOM   3045 C CD2 . TYR B 1 181 ? -5.982  -20.847 32.528  1.00 38.47 ? 183 TYR B CD2 1 
ATOM   3046 C CE1 . TYR B 1 181 ? -4.856  -23.149 31.534  1.00 37.33 ? 183 TYR B CE1 1 
ATOM   3047 C CE2 . TYR B 1 181 ? -4.964  -21.476 33.225  1.00 37.13 ? 183 TYR B CE2 1 
ATOM   3048 C CZ  . TYR B 1 181 ? -4.430  -22.645 32.741  1.00 37.16 ? 183 TYR B CZ  1 
ATOM   3049 O OH  . TYR B 1 181 ? -3.416  -23.235 33.460  1.00 37.91 ? 183 TYR B OH  1 
ATOM   3050 N N   . LYS B 1 182 ? -10.172 -21.851 31.310  1.00 41.26 ? 184 LYS B N   1 
ATOM   3051 C CA  . LYS B 1 182 ? -11.095 -22.671 32.099  1.00 43.91 ? 184 LYS B CA  1 
ATOM   3052 C C   . LYS B 1 182 ? -11.824 -23.726 31.260  1.00 45.72 ? 184 LYS B C   1 
ATOM   3053 O O   . LYS B 1 182 ? -11.882 -24.900 31.682  1.00 48.41 ? 184 LYS B O   1 
ATOM   3054 C CB  . LYS B 1 182 ? -12.080 -21.756 32.832  1.00 46.29 ? 184 LYS B CB  1 
ATOM   3055 C CG  . LYS B 1 182 ? -12.918 -22.453 33.856  1.00 52.80 ? 184 LYS B CG  1 
ATOM   3056 C CD  . LYS B 1 182 ? -13.740 -21.487 34.703  1.00 58.21 ? 184 LYS B CD  1 
ATOM   3057 C CE  . LYS B 1 182 ? -14.930 -22.170 35.361  1.00 62.98 ? 184 LYS B CE  1 
ATOM   3058 N NZ  . LYS B 1 182 ? -15.714 -21.232 36.217  1.00 66.22 ? 184 LYS B NZ  1 
ATOM   3059 N N   . GLU B 1 183 ? -12.338 -23.363 30.077  1.00 45.45 ? 185 GLU B N   1 
ATOM   3060 C CA  . GLU B 1 183 ? -12.955 -24.335 29.170  1.00 47.05 ? 185 GLU B CA  1 
ATOM   3061 C C   . GLU B 1 183 ? -11.976 -25.454 28.758  1.00 47.97 ? 185 GLU B C   1 
ATOM   3062 O O   . GLU B 1 183 ? -12.325 -26.637 28.769  1.00 47.15 ? 185 GLU B O   1 
ATOM   3063 C CB  . GLU B 1 183 ? -13.463 -23.616 27.901  1.00 51.34 ? 185 GLU B CB  1 
ATOM   3064 C CG  . GLU B 1 183 ? -14.165 -24.492 26.873  1.00 63.81 ? 185 GLU B CG  1 
ATOM   3065 C CD  . GLU B 1 183 ? -14.574 -23.754 25.604  1.00 76.56 ? 185 GLU B CD  1 
ATOM   3066 O OE1 . GLU B 1 183 ? -14.093 -22.616 25.386  1.00 79.51 ? 185 GLU B OE1 1 
ATOM   3067 O OE2 . GLU B 1 183 ? -15.374 -24.324 24.822  1.00 80.76 ? 185 GLU B OE2 1 
ATOM   3068 N N   . ARG B 1 184 ? -10.753 -25.081 28.389  1.00 47.68 ? 186 ARG B N   1 
ATOM   3069 C CA  . ARG B 1 184 ? -9.773  -26.061 27.929  1.00 46.20 ? 186 ARG B CA  1 
ATOM   3070 C C   . ARG B 1 184 ? -9.300  -26.970 29.041  1.00 47.20 ? 186 ARG B C   1 
ATOM   3071 O O   . ARG B 1 184 ? -8.927  -28.126 28.754  1.00 48.14 ? 186 ARG B O   1 
ATOM   3072 C CB  . ARG B 1 184 ? -8.600  -25.356 27.223  1.00 46.19 ? 186 ARG B CB  1 
ATOM   3073 C CG  . ARG B 1 184 ? -8.986  -24.770 25.872  1.00 45.12 ? 186 ARG B CG  1 
ATOM   3074 C CD  . ARG B 1 184 ? -9.066  -25.824 24.792  1.00 47.15 ? 186 ARG B CD  1 
ATOM   3075 N NE  . ARG B 1 184 ? -7.740  -26.326 24.445  1.00 48.84 ? 186 ARG B NE  1 
ATOM   3076 C CZ  . ARG B 1 184 ? -6.975  -25.909 23.434  1.00 49.20 ? 186 ARG B CZ  1 
ATOM   3077 N NH1 . ARG B 1 184 ? -7.403  -24.966 22.605  1.00 49.22 ? 186 ARG B NH1 1 
ATOM   3078 N NH2 . ARG B 1 184 ? -5.789  -26.452 23.228  1.00 48.51 ? 186 ARG B NH2 1 
ATOM   3079 N N   . LEU B 1 185 ? -9.311  -26.493 30.301  1.00 47.09 ? 187 LEU B N   1 
ATOM   3080 C CA  . LEU B 1 185 ? -8.994  -27.355 31.446  1.00 48.84 ? 187 LEU B CA  1 
ATOM   3081 C C   . LEU B 1 185 ? -10.131 -28.327 31.776  1.00 51.60 ? 187 LEU B C   1 
ATOM   3082 O O   . LEU B 1 185 ? -9.872  -29.339 32.405  1.00 51.90 ? 187 LEU B O   1 
ATOM   3083 C CB  . LEU B 1 185 ? -8.692  -26.507 32.705  1.00 47.87 ? 187 LEU B CB  1 
ATOM   3084 C CG  . LEU B 1 185 ? -7.408  -25.673 32.662  1.00 47.20 ? 187 LEU B CG  1 
ATOM   3085 C CD1 . LEU B 1 185 ? -7.267  -24.801 33.909  1.00 46.74 ? 187 LEU B CD1 1 
ATOM   3086 C CD2 . LEU B 1 185 ? -6.140  -26.560 32.459  1.00 47.47 ? 187 LEU B CD2 1 
ATOM   3087 N N   . GLY B 1 186 ? -11.357 -28.002 31.391  1.00 54.16 ? 188 GLY B N   1 
ATOM   3088 C CA  . GLY B 1 186 ? -12.527 -28.822 31.664  1.00 57.59 ? 188 GLY B CA  1 
ATOM   3089 C C   . GLY B 1 186 ? -13.114 -28.573 33.036  1.00 60.10 ? 188 GLY B C   1 
ATOM   3090 O O   . GLY B 1 186 ? -13.834 -29.431 33.535  1.00 60.28 ? 188 GLY B O   1 
ATOM   3091 N N   . LEU B 1 187 ? -12.830 -27.406 33.668  1.00 62.08 ? 189 LEU B N   1 
ATOM   3092 C CA  . LEU B 1 187 ? -13.297 -27.175 35.031  1.00 64.96 ? 189 LEU B CA  1 
ATOM   3093 C C   . LEU B 1 187 ? -14.806 -26.909 35.011  1.00 68.87 ? 189 LEU B C   1 
ATOM   3094 O O   . LEU B 1 187 ? -15.293 -26.211 34.116  1.00 69.20 ? 189 LEU B O   1 
ATOM   3095 C CB  . LEU B 1 187 ? -12.587 -25.996 35.716  1.00 65.45 ? 189 LEU B CB  1 
ATOM   3096 C CG  . LEU B 1 187 ? -11.064 -26.098 35.837  1.00 66.50 ? 189 LEU B CG  1 
ATOM   3097 C CD1 . LEU B 1 187 ? -10.457 -24.856 36.452  1.00 66.02 ? 189 LEU B CD1 1 
ATOM   3098 C CD2 . LEU B 1 187 ? -10.657 -27.275 36.670  1.00 67.57 ? 189 LEU B CD2 1 
ATOM   3099 N N   . PRO B 1 188 ? -15.566 -27.458 35.974  1.00 71.20 ? 190 PRO B N   1 
ATOM   3100 C CA  . PRO B 1 188 ? -16.993 -27.100 36.058  1.00 73.22 ? 190 PRO B CA  1 
ATOM   3101 C C   . PRO B 1 188 ? -17.221 -25.613 36.285  1.00 75.79 ? 190 PRO B C   1 
ATOM   3102 O O   . PRO B 1 188 ? -16.362 -24.955 36.873  1.00 76.95 ? 190 PRO B O   1 
ATOM   3103 C CB  . PRO B 1 188 ? -17.508 -27.917 37.247  1.00 73.27 ? 190 PRO B CB  1 
ATOM   3104 C CG  . PRO B 1 188 ? -16.477 -28.900 37.553  1.00 73.84 ? 190 PRO B CG  1 
ATOM   3105 C CD  . PRO B 1 188 ? -15.180 -28.434 37.011  1.00 71.33 ? 190 PRO B CD  1 
ATOM   3106 N N   . PRO B 1 189 ? -18.365 -25.059 35.819  1.00 77.00 ? 191 PRO B N   1 
ATOM   3107 C CA  . PRO B 1 189 ? -18.711 -23.656 36.153  1.00 77.46 ? 191 PRO B CA  1 
ATOM   3108 C C   . PRO B 1 189 ? -18.699 -23.270 37.643  1.00 77.51 ? 191 PRO B C   1 
ATOM   3109 O O   . PRO B 1 189 ? -18.435 -22.113 37.956  1.00 77.66 ? 191 PRO B O   1 
ATOM   3110 C CB  . PRO B 1 189 ? -20.145 -23.496 35.631  1.00 78.16 ? 191 PRO B CB  1 
ATOM   3111 C CG  . PRO B 1 189 ? -20.372 -24.602 34.691  1.00 78.52 ? 191 PRO B CG  1 
ATOM   3112 C CD  . PRO B 1 189 ? -19.383 -25.687 34.952  1.00 76.91 ? 191 PRO B CD  1 
ATOM   3113 N N   . LYS B 1 190 ? -19.029 -24.214 38.550  1.00 76.88 ? 192 LYS B N   1 
ATOM   3114 C CA  . LYS B 1 190 ? -18.941 -23.977 40.004  1.00 76.95 ? 192 LYS B CA  1 
ATOM   3115 C C   . LYS B 1 190 ? -17.515 -23.659 40.506  1.00 75.58 ? 192 LYS B C   1 
ATOM   3116 O O   . LYS B 1 190 ? -17.357 -22.945 41.504  1.00 76.04 ? 192 LYS B O   1 
ATOM   3117 C CB  . LYS B 1 190 ? -19.520 -25.168 40.806  1.00 79.79 ? 192 LYS B CB  1 
ATOM   3118 C CG  . LYS B 1 190 ? -18.937 -26.531 40.435  1.00 84.90 ? 192 LYS B CG  1 
ATOM   3119 C CD  . LYS B 1 190 ? -19.142 -27.593 41.499  1.00 90.19 ? 192 LYS B CD  1 
ATOM   3120 C CE  . LYS B 1 190 ? -18.546 -28.911 41.058  1.00 94.94 ? 192 LYS B CE  1 
ATOM   3121 N NZ  . LYS B 1 190 ? -18.320 -29.850 42.191  1.00 97.81 ? 192 LYS B NZ  1 
ATOM   3122 N N   . ILE B 1 191 ? -16.488 -24.186 39.835  1.00 73.48 ? 193 ILE B N   1 
ATOM   3123 C CA  . ILE B 1 191 ? -15.097 -23.931 40.233  1.00 71.68 ? 193 ILE B CA  1 
ATOM   3124 C C   . ILE B 1 191 ? -14.687 -22.605 39.636  1.00 69.44 ? 193 ILE B C   1 
ATOM   3125 O O   . ILE B 1 191 ? -14.695 -22.489 38.417  1.00 69.41 ? 193 ILE B O   1 
ATOM   3126 C CB  . ILE B 1 191 ? -14.159 -25.082 39.780  1.00 72.01 ? 193 ILE B CB  1 
ATOM   3127 C CG1 . ILE B 1 191 ? -14.745 -26.450 40.254  1.00 73.27 ? 193 ILE B CG1 1 
ATOM   3128 C CG2 . ILE B 1 191 ? -12.724 -24.845 40.297  1.00 72.07 ? 193 ILE B CG2 1 
ATOM   3129 C CD1 . ILE B 1 191 ? -13.798 -27.642 40.363  1.00 75.64 ? 193 ILE B CD1 1 
ATOM   3130 N N   . VAL B 1 192 ? -14.331 -21.612 40.481  1.00 67.32 ? 194 VAL B N   1 
ATOM   3131 C CA  . VAL B 1 192 ? -13.951 -20.286 39.999  1.00 65.48 ? 194 VAL B CA  1 
ATOM   3132 C C   . VAL B 1 192 ? -12.448 -20.065 40.154  1.00 60.36 ? 194 VAL B C   1 
ATOM   3133 O O   . VAL B 1 192 ? -11.826 -20.536 41.108  1.00 60.11 ? 194 VAL B O   1 
ATOM   3134 C CB  . VAL B 1 192 ? -14.764 -19.159 40.670  1.00 68.45 ? 194 VAL B CB  1 
ATOM   3135 C CG1 . VAL B 1 192 ? -16.270 -19.445 40.605  1.00 69.63 ? 194 VAL B CG1 1 
ATOM   3136 C CG2 . VAL B 1 192 ? -14.309 -18.926 42.109  1.00 70.24 ? 194 VAL B CG2 1 
ATOM   3137 N N   . ILE B 1 193 ? -11.862 -19.344 39.195  1.00 56.04 ? 195 ILE B N   1 
ATOM   3138 C CA  . ILE B 1 193 ? -10.419 -19.135 39.137  1.00 52.17 ? 195 ILE B CA  1 
ATOM   3139 C C   . ILE B 1 193 ? -10.167 -17.649 39.162  1.00 48.23 ? 195 ILE B C   1 
ATOM   3140 O O   . ILE B 1 193 ? -10.951 -16.869 38.600  1.00 48.12 ? 195 ILE B O   1 
ATOM   3141 C CB  . ILE B 1 193 ? -9.771  -19.844 37.898  1.00 51.51 ? 195 ILE B CB  1 
ATOM   3142 C CG1 . ILE B 1 193 ? -10.227 -19.214 36.548  1.00 51.26 ? 195 ILE B CG1 1 
ATOM   3143 C CG2 . ILE B 1 193 ? -10.026 -21.358 37.956  1.00 52.96 ? 195 ILE B CG2 1 
ATOM   3144 C CD1 . ILE B 1 193 ? -9.423  -19.773 35.343  1.00 51.66 ? 195 ILE B CD1 1 
ATOM   3145 N N   . GLY B 1 194 ? -9.082  -17.279 39.829  1.00 44.96 ? 196 GLY B N   1 
ATOM   3146 C CA  . GLY B 1 194 ? -8.685  -15.903 40.035  1.00 41.13 ? 196 GLY B CA  1 
ATOM   3147 C C   . GLY B 1 194 ? -7.525  -15.426 39.182  1.00 38.50 ? 196 GLY B C   1 
ATOM   3148 O O   . GLY B 1 194 ? -6.615  -16.183 38.867  1.00 37.50 ? 196 GLY B O   1 
ATOM   3149 N N   . TYR B 1 195 ? -7.565  -14.136 38.788  1.00 37.53 ? 197 TYR B N   1 
ATOM   3150 C CA  . TYR B 1 195 ? -6.467  -13.464 38.133  1.00 37.60 ? 197 TYR B CA  1 
ATOM   3151 C C   . TYR B 1 195 ? -5.883  -12.484 39.140  1.00 37.52 ? 197 TYR B C   1 
ATOM   3152 O O   . TYR B 1 195 ? -6.613  -11.635 39.688  1.00 36.97 ? 197 TYR B O   1 
ATOM   3153 C CB  . TYR B 1 195 ? -6.944  -12.719 36.872  1.00 36.75 ? 197 TYR B CB  1 
ATOM   3154 C CG  . TYR B 1 195 ? -5.862  -11.982 36.090  1.00 34.36 ? 197 TYR B CG  1 
ATOM   3155 C CD1 . TYR B 1 195 ? -5.159  -12.615 35.074  1.00 34.18 ? 197 TYR B CD1 1 
ATOM   3156 C CD2 . TYR B 1 195 ? -5.578  -10.641 36.336  1.00 35.22 ? 197 TYR B CD2 1 
ATOM   3157 C CE1 . TYR B 1 195 ? -4.151  -11.965 34.375  1.00 34.17 ? 197 TYR B CE1 1 
ATOM   3158 C CE2 . TYR B 1 195 ? -4.591  -9.964  35.615  1.00 35.62 ? 197 TYR B CE2 1 
ATOM   3159 C CZ  . TYR B 1 195 ? -3.884  -10.622 34.629  1.00 36.62 ? 197 TYR B CZ  1 
ATOM   3160 O OH  . TYR B 1 195 ? -2.931  -9.939  33.889  1.00 38.87 ? 197 TYR B OH  1 
ATOM   3161 N N   . GLN B 1 196 ? -4.577  -12.582 39.394  1.00 37.62 ? 198 GLN B N   1 
ATOM   3162 C CA  . GLN B 1 196 ? -3.915  -11.708 40.340  1.00 38.40 ? 198 GLN B CA  1 
ATOM   3163 C C   . GLN B 1 196 ? -2.894  -10.869 39.631  1.00 38.05 ? 198 GLN B C   1 
ATOM   3164 O O   . GLN B 1 196 ? -2.055  -11.405 38.876  1.00 37.22 ? 198 GLN B O   1 
ATOM   3165 C CB  . GLN B 1 196 ? -3.215  -12.525 41.421  1.00 40.35 ? 198 GLN B CB  1 
ATOM   3166 C CG  . GLN B 1 196 ? -4.187  -13.461 42.171  1.00 47.54 ? 198 GLN B CG  1 
ATOM   3167 C CD  . GLN B 1 196 ? -3.465  -14.569 42.949  1.00 56.97 ? 198 GLN B CD  1 
ATOM   3168 O OE1 . GLN B 1 196 ? -2.320  -14.939 42.673  1.00 58.46 ? 198 GLN B OE1 1 
ATOM   3169 N NE2 . GLN B 1 196 ? -4.128  -15.129 43.937  1.00 59.86 ? 198 GLN B NE2 1 
ATOM   3170 N N   . SER B 1 197 ? -2.925  -9.550  39.879  1.00 36.94 ? 199 SER B N   1 
ATOM   3171 C CA  . SER B 1 197 ? -1.867  -8.641  39.459  1.00 37.79 ? 199 SER B CA  1 
ATOM   3172 C C   . SER B 1 197 ? -0.523  -9.084  40.051  1.00 38.00 ? 199 SER B C   1 
ATOM   3173 O O   . SER B 1 197 ? -0.511  -9.434  41.229  1.00 38.82 ? 199 SER B O   1 
ATOM   3174 C CB  . SER B 1 197 ? -2.169  -7.229  39.997  1.00 39.51 ? 199 SER B CB  1 
ATOM   3175 O OG  . SER B 1 197 ? -1.157  -6.315  39.612  1.00 44.79 ? 199 SER B OG  1 
ATOM   3176 N N   . HIS B 1 198 ? 0.563   -9.078  39.296  1.00 37.52 ? 200 HIS B N   1 
ATOM   3177 C CA  . HIS B 1 198 ? 1.896   -9.360  39.894  1.00 39.17 ? 200 HIS B CA  1 
ATOM   3178 C C   . HIS B 1 198 ? 2.317   -8.359  40.969  1.00 41.55 ? 200 HIS B C   1 
ATOM   3179 O O   . HIS B 1 198 ? 2.968   -8.733  41.935  1.00 41.35 ? 200 HIS B O   1 
ATOM   3180 C CB  . HIS B 1 198 ? 2.965   -9.360  38.843  1.00 38.35 ? 200 HIS B CB  1 
ATOM   3181 C CG  . HIS B 1 198 ? 2.848   -10.438 37.812  1.00 38.92 ? 200 HIS B CG  1 
ATOM   3182 N ND1 . HIS B 1 198 ? 2.392   -11.710 38.116  1.00 38.42 ? 200 HIS B ND1 1 
ATOM   3183 C CD2 . HIS B 1 198 ? 3.095   -10.379 36.497  1.00 39.53 ? 200 HIS B CD2 1 
ATOM   3184 C CE1 . HIS B 1 198 ? 2.405   -12.367 36.983  1.00 40.12 ? 200 HIS B CE1 1 
ATOM   3185 N NE2 . HIS B 1 198 ? 2.823   -11.611 35.989  1.00 40.19 ? 200 HIS B NE2 1 
ATOM   3186 N N   . ALA B 1 199 ? 1.963   -7.089  40.803  1.00 43.33 ? 201 ALA B N   1 
ATOM   3187 C CA  . ALA B 1 199 ? 2.249   -6.061  41.801  1.00 47.54 ? 201 ALA B CA  1 
ATOM   3188 C C   . ALA B 1 199 ? 1.572   -6.425  43.137  1.00 51.71 ? 201 ALA B C   1 
ATOM   3189 O O   . ALA B 1 199 ? 2.190   -6.292  44.207  1.00 53.81 ? 201 ALA B O   1 
ATOM   3190 C CB  . ALA B 1 199 ? 1.806   -4.706  41.300  1.00 48.00 ? 201 ALA B CB  1 
ATOM   3191 N N   . ASP B 1 200 ? 0.332   -6.941  43.090  1.00 51.10 ? 202 ASP B N   1 
ATOM   3192 C CA  . ASP B 1 200 ? -0.328  -7.451  44.301  1.00 51.38 ? 202 ASP B CA  1 
ATOM   3193 C C   . ASP B 1 200 ? 0.292   -8.754  44.851  1.00 52.88 ? 202 ASP B C   1 
ATOM   3194 O O   . ASP B 1 200 ? 0.473   -8.865  46.078  1.00 54.52 ? 202 ASP B O   1 
ATOM   3195 C CB  . ASP B 1 200 ? -1.823  -7.665  44.057  1.00 53.06 ? 202 ASP B CB  1 
ATOM   3196 C CG  . ASP B 1 200 ? -2.607  -6.408  43.720  1.00 58.37 ? 202 ASP B CG  1 
ATOM   3197 O OD1 . ASP B 1 200 ? -2.070  -5.298  43.932  1.00 62.01 ? 202 ASP B OD1 1 
ATOM   3198 O OD2 . ASP B 1 200 ? -3.764  -6.537  43.232  1.00 59.12 ? 202 ASP B OD2 1 
ATOM   3199 N N   . THR B 1 201 ? 0.606   -9.752  43.989  1.00 51.02 ? 203 THR B N   1 
ATOM   3200 C CA  . THR B 1 201 ? 1.296   -10.941 44.457  1.00 52.60 ? 203 THR B CA  1 
ATOM   3201 C C   . THR B 1 201 ? 2.664   -10.638 45.117  1.00 54.72 ? 203 THR B C   1 
ATOM   3202 O O   . THR B 1 201 ? 3.033   -11.332 46.062  1.00 55.28 ? 203 THR B O   1 
ATOM   3203 C CB  . THR B 1 201 ? 1.466   -11.959 43.353  1.00 53.12 ? 203 THR B CB  1 
ATOM   3204 O OG1 . THR B 1 201 ? 0.168   -12.223 42.807  1.00 53.26 ? 203 THR B OG1 1 
ATOM   3205 C CG2 . THR B 1 201 ? 2.049   -13.275 43.878  1.00 54.16 ? 203 THR B CG2 1 
ATOM   3206 N N   . ALA B 1 202 ? 3.394   -9.643  44.637  1.00 55.79 ? 204 ALA B N   1 
ATOM   3207 C CA  . ALA B 1 202 ? 4.723   -9.294  45.152  1.00 57.73 ? 204 ALA B CA  1 
ATOM   3208 C C   . ALA B 1 202 ? 4.717   -8.777  46.597  1.00 58.81 ? 204 ALA B C   1 
ATOM   3209 O O   . ALA B 1 202 ? 5.778   -8.711  47.209  1.00 60.59 ? 204 ALA B O   1 
ATOM   3210 C CB  . ALA B 1 202 ? 5.352   -8.229  44.273  1.00 57.66 ? 204 ALA B CB  1 
ATOM   3211 N N   . THR B 1 203 ? 3.547   -8.386  47.131  1.00 58.22 ? 205 THR B N   1 
ATOM   3212 C CA  . THR B 1 203 ? 3.420   -7.876  48.487  1.00 58.27 ? 205 THR B CA  1 
ATOM   3213 C C   . THR B 1 203 ? 2.758   -8.969  49.303  1.00 56.76 ? 205 THR B C   1 
ATOM   3214 O O   . THR B 1 203 ? 1.635   -9.347  48.988  1.00 57.36 ? 205 THR B O   1 
ATOM   3215 C CB  . THR B 1 203 ? 2.617   -6.558  48.510  1.00 60.93 ? 205 THR B CB  1 
ATOM   3216 O OG1 . THR B 1 203 ? 1.233   -6.810  48.259  1.00 63.00 ? 205 THR B OG1 1 
ATOM   3217 C CG2 . THR B 1 203 ? 3.137   -5.542  47.487  1.00 61.88 ? 205 THR B CG2 1 
ATOM   3218 N N   . LYS B 1 204 ? 3.437   -9.491  50.325  1.00 54.13 ? 206 LYS B N   1 
ATOM   3219 C CA  . LYS B 1 204 ? 2.904   -10.554 51.163  1.00 53.19 ? 206 LYS B CA  1 
ATOM   3220 C C   . LYS B 1 204 ? 2.074   -9.926  52.262  1.00 50.65 ? 206 LYS B C   1 
ATOM   3221 O O   . LYS B 1 204 ? 2.595   -9.190  53.115  1.00 48.99 ? 206 LYS B O   1 
ATOM   3222 C CB  . LYS B 1 204 ? 4.047   -11.421 51.729  1.00 56.73 ? 206 LYS B CB  1 
ATOM   3223 C CG  . LYS B 1 204 ? 4.951   -12.081 50.665  1.00 62.84 ? 206 LYS B CG  1 
ATOM   3224 C CD  . LYS B 1 204 ? 4.295   -13.261 50.011  1.00 69.69 ? 206 LYS B CD  1 
ATOM   3225 C CE  . LYS B 1 204 ? 5.231   -14.094 49.147  1.00 76.16 ? 206 LYS B CE  1 
ATOM   3226 N NZ  . LYS B 1 204 ? 5.138   -15.571 49.455  1.00 77.34 ? 206 LYS B NZ  1 
ATOM   3227 N N   . SER B 1 205 ? 0.765   -10.235 52.259  1.00 51.12 ? 207 SER B N   1 
ATOM   3228 C CA  . SER B 1 205 ? -0.236  -9.558  53.097  1.00 53.47 ? 207 SER B CA  1 
ATOM   3229 C C   . SER B 1 205 ? -1.155  -10.532 53.858  1.00 55.24 ? 207 SER B C   1 
ATOM   3230 O O   . SER B 1 205 ? -2.174  -10.100 54.379  1.00 56.60 ? 207 SER B O   1 
ATOM   3231 C CB  . SER B 1 205 ? -1.071  -8.620  52.221  1.00 57.28 ? 207 SER B CB  1 
ATOM   3232 O OG  . SER B 1 205 ? -1.639  -9.342  51.127  1.00 61.23 ? 207 SER B OG  1 
ATOM   3233 N N   . GLY B 1 206 ? -0.789  -11.812 53.952  1.00 55.95 ? 208 GLY B N   1 
ATOM   3234 C CA  . GLY B 1 206 ? -1.562  -12.802 54.695  1.00 57.93 ? 208 GLY B CA  1 
ATOM   3235 C C   . GLY B 1 206 ? -1.537  -14.142 54.001  1.00 60.17 ? 208 GLY B C   1 
ATOM   3236 O O   . GLY B 1 206 ? -0.565  -14.444 53.297  1.00 60.82 ? 208 GLY B O   1 
ATOM   3237 N N   . SER B 1 207 ? -2.593  -14.972 54.176  1.00 61.44 ? 209 SER B N   1 
ATOM   3238 C CA  . SER B 1 207 ? -2.624  -16.277 53.473  1.00 63.08 ? 209 SER B CA  1 
ATOM   3239 C C   . SER B 1 207 ? -2.781  -16.090 51.971  1.00 64.63 ? 209 SER B C   1 
ATOM   3240 O O   . SER B 1 207 ? -2.166  -16.834 51.213  1.00 65.29 ? 209 SER B O   1 
ATOM   3241 C CB  . SER B 1 207 ? -3.719  -17.221 53.989  1.00 64.54 ? 209 SER B CB  1 
ATOM   3242 O OG  . SER B 1 207 ? -4.576  -16.706 55.000  1.00 66.57 ? 209 SER B OG  1 
ATOM   3243 N N   . THR B 1 208 ? -3.586  -15.089 51.536  1.00 64.44 ? 210 THR B N   1 
ATOM   3244 C CA  . THR B 1 208 ? -4.007  -14.982 50.133  1.00 64.54 ? 210 THR B CA  1 
ATOM   3245 C C   . THR B 1 208 ? -3.576  -13.632 49.479  1.00 62.50 ? 210 THR B C   1 
ATOM   3246 O O   . THR B 1 208 ? -3.148  -12.714 50.176  1.00 62.05 ? 210 THR B O   1 
ATOM   3247 C CB  . THR B 1 208 ? -5.551  -15.154 50.091  1.00 68.02 ? 210 THR B CB  1 
ATOM   3248 O OG1 . THR B 1 208 ? -6.135  -14.003 50.727  1.00 70.80 ? 210 THR B OG1 1 
ATOM   3249 C CG2 . THR B 1 208 ? -6.018  -16.452 50.814  1.00 69.19 ? 210 THR B CG2 1 
ATOM   3250 N N   . THR B 1 209 ? -3.678  -13.556 48.132  1.00 60.66 ? 211 THR B N   1 
ATOM   3251 C CA  . THR B 1 209 ? -3.593  -12.319 47.351  1.00 58.90 ? 211 THR B CA  1 
ATOM   3252 C C   . THR B 1 209 ? -4.983  -12.038 46.761  1.00 54.06 ? 211 THR B C   1 
ATOM   3253 O O   . THR B 1 209 ? -5.686  -12.990 46.377  1.00 53.89 ? 211 THR B O   1 
ATOM   3254 C CB  . THR B 1 209 ? -2.560  -12.470 46.233  1.00 62.01 ? 211 THR B CB  1 
ATOM   3255 O OG1 . THR B 1 209 ? -1.283  -12.790 46.815  1.00 64.93 ? 211 THR B OG1 1 
ATOM   3256 C CG2 . THR B 1 209 ? -2.462  -11.222 45.365  1.00 61.76 ? 211 THR B CG2 1 
ATOM   3257 N N   . LYS B 1 210 ? -5.382  -10.762 46.697  1.00 50.07 ? 212 LYS B N   1 
ATOM   3258 C CA  . LYS B 1 210 ? -6.675  -10.428 46.095  1.00 48.29 ? 212 LYS B CA  1 
ATOM   3259 C C   . LYS B 1 210 ? -6.701  -10.711 44.576  1.00 46.23 ? 212 LYS B C   1 
ATOM   3260 O O   . LYS B 1 210 ? -5.677  -10.644 43.862  1.00 44.50 ? 212 LYS B O   1 
ATOM   3261 C CB  . LYS B 1 210 ? -7.123  -8.967  46.412  1.00 51.34 ? 212 LYS B CB  1 
ATOM   3262 C CG  . LYS B 1 210 ? -6.271  -7.916  45.770  1.00 55.59 ? 212 LYS B CG  1 
ATOM   3263 C CD  . LYS B 1 210 ? -6.622  -6.510  46.268  1.00 59.70 ? 212 LYS B CD  1 
ATOM   3264 C CE  . LYS B 1 210 ? -5.729  -5.504  45.594  1.00 65.22 ? 212 LYS B CE  1 
ATOM   3265 N NZ  . LYS B 1 210 ? -6.016  -4.097  46.010  1.00 68.71 ? 212 LYS B NZ  1 
ATOM   3266 N N   . ASN B 1 211 ? -7.886  -11.047 44.111  1.00 45.16 ? 213 ASN B N   1 
ATOM   3267 C CA  . ASN B 1 211 ? -8.183  -11.246 42.716  1.00 45.72 ? 213 ASN B CA  1 
ATOM   3268 C C   . ASN B 1 211 ? -8.679  -9.964  42.094  1.00 46.44 ? 213 ASN B C   1 
ATOM   3269 O O   . ASN B 1 211 ? -9.655  -9.381  42.552  1.00 47.89 ? 213 ASN B O   1 
ATOM   3270 C CB  . ASN B 1 211 ? -9.258  -12.329 42.557  1.00 46.36 ? 213 ASN B CB  1 
ATOM   3271 C CG  . ASN B 1 211 ? -8.745  -13.664 42.954  1.00 48.89 ? 213 ASN B CG  1 
ATOM   3272 O OD1 . ASN B 1 211 ? -7.592  -14.012 42.679  1.00 47.53 ? 213 ASN B OD1 1 
ATOM   3273 N ND2 . ASN B 1 211 ? -9.574  -14.457 43.593  1.00 51.95 ? 213 ASN B ND2 1 
ATOM   3274 N N   . ARG B 1 212 ? -7.989  -9.526  41.051  1.00 44.86 ? 214 ARG B N   1 
ATOM   3275 C CA  . ARG B 1 212 ? -8.402  -8.423  40.205  1.00 45.35 ? 214 ARG B CA  1 
ATOM   3276 C C   . ARG B 1 212 ? -9.666  -8.858  39.469  1.00 46.00 ? 214 ARG B C   1 
ATOM   3277 O O   . ARG B 1 212 ? -10.632 -8.098  39.419  1.00 46.86 ? 214 ARG B O   1 
ATOM   3278 C CB  . ARG B 1 212 ? -7.253  -8.090  39.237  1.00 48.10 ? 214 ARG B CB  1 
ATOM   3279 C CG  . ARG B 1 212 ? -7.477  -7.002  38.217  1.00 56.11 ? 214 ARG B CG  1 
ATOM   3280 C CD  . ARG B 1 212 ? -7.563  -5.644  38.833  1.00 58.24 ? 214 ARG B CD  1 
ATOM   3281 N NE  . ARG B 1 212 ? -6.347  -5.234  39.552  1.00 62.53 ? 214 ARG B NE  1 
ATOM   3282 C CZ  . ARG B 1 212 ? -5.214  -4.827  38.982  1.00 64.97 ? 214 ARG B CZ  1 
ATOM   3283 N NH1 . ARG B 1 212 ? -4.179  -4.472  39.731  1.00 66.02 ? 214 ARG B NH1 1 
ATOM   3284 N NH2 . ARG B 1 212 ? -5.103  -4.782  37.661  1.00 66.60 ? 214 ARG B NH2 1 
ATOM   3285 N N   . PHE B 1 213 ? -9.673  -10.080 38.908  1.00 44.04 ? 215 PHE B N   1 
ATOM   3286 C CA  . PHE B 1 213 ? -10.824 -10.659 38.210  1.00 45.18 ? 215 PHE B CA  1 
ATOM   3287 C C   . PHE B 1 213 ? -11.022 -12.129 38.599  1.00 48.04 ? 215 PHE B C   1 
ATOM   3288 O O   . PHE B 1 213 ? -10.092 -12.830 39.056  1.00 47.71 ? 215 PHE B O   1 
ATOM   3289 C CB  . PHE B 1 213 ? -10.663 -10.577 36.677  1.00 44.64 ? 215 PHE B CB  1 
ATOM   3290 C CG  . PHE B 1 213 ? -10.167 -9.271  36.095  1.00 44.51 ? 215 PHE B CG  1 
ATOM   3291 C CD1 . PHE B 1 213 ? -10.929 -8.117  36.180  1.00 46.14 ? 215 PHE B CD1 1 
ATOM   3292 C CD2 . PHE B 1 213 ? -8.941  -9.201  35.454  1.00 45.23 ? 215 PHE B CD2 1 
ATOM   3293 C CE1 . PHE B 1 213 ? -10.462 -6.915  35.646  1.00 46.46 ? 215 PHE B CE1 1 
ATOM   3294 C CE2 . PHE B 1 213 ? -8.487  -8.001  34.902  1.00 45.92 ? 215 PHE B CE2 1 
ATOM   3295 C CZ  . PHE B 1 213 ? -9.236  -6.866  35.019  1.00 45.78 ? 215 PHE B CZ  1 
ATOM   3296 N N   . VAL B 1 214 ? -12.248 -12.598 38.411  1.00 49.89 ? 216 VAL B N   1 
ATOM   3297 C CA  . VAL B 1 214 ? -12.617 -13.986 38.579  1.00 52.36 ? 216 VAL B CA  1 
ATOM   3298 C C   . VAL B 1 214 ? -13.444 -14.397 37.358  1.00 56.19 ? 216 VAL B C   1 
ATOM   3299 O O   . VAL B 1 214 ? -14.176 -13.580 36.801  1.00 57.18 ? 216 VAL B O   1 
ATOM   3300 C CB  . VAL B 1 214 ? -13.403 -14.286 39.888  1.00 52.89 ? 216 VAL B CB  1 
ATOM   3301 C CG1 . VAL B 1 214 ? -12.575 -13.944 41.125  1.00 53.80 ? 216 VAL B CG1 1 
ATOM   3302 C CG2 . VAL B 1 214 ? -14.753 -13.591 39.918  1.00 52.86 ? 216 VAL B CG2 1 
ATOM   3303 N N   . VAL B 1 215 ? -13.320 -15.641 36.947  1.00 58.26 ? 217 VAL B N   1 
ATOM   3304 C CA  . VAL B 1 215 ? -14.218 -16.241 35.954  1.00 60.68 ? 217 VAL B CA  1 
ATOM   3305 C C   . VAL B 1 215 ? -14.458 -17.686 36.340  1.00 61.83 ? 217 VAL B C   1 
ATOM   3306 O O   . VAL B 1 215 ? -15.384 -18.287 35.748  1.00 62.61 ? 217 VAL B O   1 
ATOM   3307 C CB  . VAL B 1 215 ? -13.733 -16.166 34.472  1.00 61.85 ? 217 VAL B CB  1 
ATOM   3308 C CG1 . VAL B 1 215 ? -13.494 -14.720 34.006  1.00 62.77 ? 217 VAL B CG1 1 
ATOM   3309 C CG2 . VAL B 1 215 ? -12.514 -17.049 34.248  1.00 62.25 ? 217 VAL B CG2 1 
ATOM   3310 O OXT . VAL B 1 215 ? -13.737 -18.225 37.213  1.00 63.16 ? 217 VAL B OXT 1 
HETATM 3311 S S   . DMS C 2 .   ? 28.892  -21.795 10.646  1.00 95.40 ? 301 DMS A S   1 
HETATM 3312 O O   . DMS C 2 .   ? 29.541  -23.053 11.175  1.00 95.60 ? 301 DMS A O   1 
HETATM 3313 C C1  . DMS C 2 .   ? 29.700  -20.440 11.466  1.00 94.98 ? 301 DMS A C1  1 
HETATM 3314 C C2  . DMS C 2 .   ? 29.575  -21.547 9.028   1.00 95.31 ? 301 DMS A C2  1 
HETATM 3315 C C1  . PGE D 3 .   ? 9.272   -26.897 1.604   1.00 76.32 ? 302 PGE A C1  1 
HETATM 3316 O O1  . PGE D 3 .   ? 8.228   -26.355 0.812   1.00 76.13 ? 302 PGE A O1  1 
HETATM 3317 C C2  . PGE D 3 .   ? 9.003   -26.719 3.076   1.00 76.18 ? 302 PGE A C2  1 
HETATM 3318 O O2  . PGE D 3 .   ? 10.183  -26.967 3.825   1.00 75.93 ? 302 PGE A O2  1 
HETATM 3319 C C3  . PGE D 3 .   ? 11.062  -25.846 3.863   1.00 75.53 ? 302 PGE A C3  1 
HETATM 3320 C C4  . PGE D 3 .   ? 12.335  -26.162 4.576   1.00 74.90 ? 302 PGE A C4  1 
HETATM 3321 O O4  . PGE D 3 .   ? 15.707  -25.150 1.951   1.00 73.16 ? 302 PGE A O4  1 
HETATM 3322 C C6  . PGE D 3 .   ? 15.261  -26.391 2.453   1.00 73.78 ? 302 PGE A C6  1 
HETATM 3323 C C5  . PGE D 3 .   ? 13.787  -26.407 2.685   1.00 74.25 ? 302 PGE A C5  1 
HETATM 3324 O O3  . PGE D 3 .   ? 13.440  -25.642 3.842   1.00 74.79 ? 302 PGE A O3  1 
HETATM 3325 C C1  . PGE E 3 .   ? 4.001   -9.833  24.836  1.00 67.57 ? 303 PGE A C1  1 
HETATM 3326 O O1  . PGE E 3 .   ? 2.930   -10.334 25.618  1.00 67.90 ? 303 PGE A O1  1 
HETATM 3327 C C2  . PGE E 3 .   ? 4.382   -10.797 23.783  1.00 67.36 ? 303 PGE A C2  1 
HETATM 3328 O O2  . PGE E 3 .   ? 5.504   -10.316 23.056  1.00 67.39 ? 303 PGE A O2  1 
HETATM 3329 C C3  . PGE E 3 .   ? 6.655   -11.131 23.246  1.00 67.22 ? 303 PGE A C3  1 
HETATM 3330 C C4  . PGE E 3 .   ? 7.866   -10.524 22.628  1.00 67.22 ? 303 PGE A C4  1 
HETATM 3331 O O4  . PGE E 3 .   ? 11.647  -7.838  23.628  1.00 71.20 ? 303 PGE A O4  1 
HETATM 3332 C C6  . PGE E 3 .   ? 10.766  -8.861  24.134  1.00 70.52 ? 303 PGE A C6  1 
HETATM 3333 C C5  . PGE E 3 .   ? 9.533   -9.012  23.301  1.00 69.41 ? 303 PGE A C5  1 
HETATM 3334 O O3  . PGE E 3 .   ? 8.865   -10.235 23.590  1.00 67.72 ? 303 PGE A O3  1 
HETATM 3335 C C2  . W5B F 4 .   ? 18.241  -4.353  9.362   0.44 28.47 ? 304 W5B A C2  1 
HETATM 3336 C C3  . W5B F 4 .   ? 19.150  -4.963  10.189  0.44 28.57 ? 304 W5B A C3  1 
HETATM 3337 C C5  . W5B F 4 .   ? 18.104  -7.055  9.808   0.44 23.42 ? 304 W5B A C5  1 
HETATM 3338 C C6  . W5B F 4 .   ? 17.136  -6.462  9.021   0.44 25.97 ? 304 W5B A C6  1 
HETATM 3339 C C7  . W5B F 4 .   ? 17.212  -5.087  8.801   0.44 27.78 ? 304 W5B A C7  1 
HETATM 3340 C C8  . W5B F 4 .   ? 16.050  -7.276  8.422   0.44 27.08 ? 304 W5B A C8  1 
HETATM 3341 C C10 . W5B F 4 .   ? 13.730  -7.566  7.887   0.44 27.66 ? 304 W5B A C10 1 
HETATM 3342 C C11 . W5B F 4 .   ? 14.012  -8.774  7.296   0.44 27.66 ? 304 W5B A C11 1 
HETATM 3343 C C12 . W5B F 4 .   ? 15.306  -9.242  7.268   0.44 27.25 ? 304 W5B A C12 1 
HETATM 3344 C C13 . W5B F 4 .   ? 16.318  -8.502  7.828   0.44 26.80 ? 304 W5B A C13 1 
HETATM 3345 O O1  . W5B F 4 .   ? 18.298  -3.022  9.188   0.44 32.80 ? 304 W5B A O1  1 
HETATM 3346 C C4  . W5B F 4 .   ? 19.095  -6.318  10.378  0.44 27.53 ? 304 W5B A C4  1 
HETATM 3347 C C9  . W5B F 4 .   ? 14.737  -6.831  8.452   0.44 28.09 ? 304 W5B A C9  1 
HETATM 3348 H H15 . W5B F 4 .   ? 19.868  -4.458  10.565  0.44 28.56 ? 304 W5B A H15 1 
HETATM 3349 H H17 . W5B F 4 .   ? 18.068  -7.994  9.970   0.44 23.42 ? 304 W5B A H17 1 
HETATM 3350 H H18 . W5B F 4 .   ? 16.555  -4.652  8.260   0.44 27.75 ? 304 W5B A H18 1 
HETATM 3351 H H20 . W5B F 4 .   ? 12.831  -7.247  7.917   0.44 27.66 ? 304 W5B A H20 1 
HETATM 3352 H H21 . W5B F 4 .   ? 13.309  -9.292  6.909   0.44 27.68 ? 304 W5B A H21 1 
HETATM 3353 H H22 . W5B F 4 .   ? 15.502  -10.077 6.849   0.44 27.27 ? 304 W5B A H22 1 
HETATM 3354 H H23 . W5B F 4 .   ? 17.215  -8.826  7.795   0.44 26.77 ? 304 W5B A H23 1 
HETATM 3355 H H14 . W5B F 4 .   ? 18.473  -2.679  9.930   0.44 32.86 ? 304 W5B A H14 1 
HETATM 3356 H H16 . W5B F 4 .   ? 19.750  -6.745  10.908  0.44 27.54 ? 304 W5B A H16 1 
HETATM 3357 H H19 . W5B F 4 .   ? 14.537  -6.001  8.868   0.44 28.13 ? 304 W5B A H19 1 
HETATM 3358 S S   . DMS G 2 .   ? 15.209  -30.469 33.629  1.00 97.29 ? 301 DMS B S   1 
HETATM 3359 O O   . DMS G 2 .   ? 15.818  -31.249 32.488  1.00 97.13 ? 301 DMS B O   1 
HETATM 3360 C C1  . DMS G 2 .   ? 14.875  -31.654 34.911  1.00 97.37 ? 301 DMS B C1  1 
HETATM 3361 C C2  . DMS G 2 .   ? 16.560  -29.628 34.421  1.00 97.18 ? 301 DMS B C2  1 
HETATM 3362 C C2  . W5B H 4 .   ? 7.281   -31.812 31.642  0.68 35.00 ? 302 W5B B C2  1 
HETATM 3363 C C3  . W5B H 4 .   ? 7.593   -31.189 32.839  0.68 35.55 ? 302 W5B B C3  1 
HETATM 3364 C C5  . W5B H 4 .   ? 7.966   -29.135 31.683  0.68 33.20 ? 302 W5B B C5  1 
HETATM 3365 C C6  . W5B H 4 .   ? 7.632   -29.733 30.471  0.68 33.33 ? 302 W5B B C6  1 
HETATM 3366 C C7  . W5B H 4 .   ? 7.303   -31.087 30.465  0.68 33.91 ? 302 W5B B C7  1 
HETATM 3367 C C8  . W5B H 4 .   ? 7.690   -28.980 29.190  0.68 32.31 ? 302 W5B B C8  1 
HETATM 3368 C C10 . W5B H 4 .   ? 7.186   -27.039 27.886  0.68 31.68 ? 302 W5B B C10 1 
HETATM 3369 C C11 . W5B H 4 .   ? 7.792   -27.612 26.786  0.68 30.74 ? 302 W5B B C11 1 
HETATM 3370 C C12 . W5B H 4 .   ? 8.357   -28.860 26.886  0.68 30.73 ? 302 W5B B C12 1 
HETATM 3371 C C13 . W5B H 4 .   ? 8.310   -29.539 28.078  0.68 31.21 ? 302 W5B B C13 1 
HETATM 3372 O O1  . W5B H 4 .   ? 6.947   -33.136 31.620  0.68 37.17 ? 302 W5B B O1  1 
HETATM 3373 C C4  . W5B H 4 .   ? 7.947   -29.856 32.857  0.68 35.12 ? 302 W5B B C4  1 
HETATM 3374 C C9  . W5B H 4 .   ? 7.138   -27.712 29.073  0.68 31.56 ? 302 W5B B C9  1 
HETATM 3375 H H15 . W5B H 4 .   ? 7.573   -31.686 33.653  0.68 35.54 ? 302 W5B B H15 1 
HETATM 3376 H H17 . W5B H 4 .   ? 8.202   -28.211 31.700  0.68 33.21 ? 302 W5B B H17 1 
HETATM 3377 H H18 . W5B H 4 .   ? 7.089   -31.516 29.639  0.68 33.88 ? 302 W5B B H18 1 
HETATM 3378 H H20 . W5B H 4 .   ? 6.789   -26.174 27.814  0.68 31.75 ? 302 W5B B H20 1 
HETATM 3379 H H21 . W5B H 4 .   ? 7.832   -27.135 25.960  0.68 30.72 ? 302 W5B B H21 1 
HETATM 3380 H H22 . W5B H 4 .   ? 8.786   -29.253 26.129  0.68 30.73 ? 302 W5B B H22 1 
HETATM 3381 H H23 . W5B H 4 .   ? 8.704   -30.404 28.146  0.68 31.16 ? 302 W5B B H23 1 
HETATM 3382 H H14 . W5B H 4 .   ? 6.834   -33.409 30.778  0.68 37.17 ? 302 W5B B H14 1 
HETATM 3383 H H16 . W5B H 4 .   ? 8.157   -29.428 33.686  0.68 35.13 ? 302 W5B B H16 1 
HETATM 3384 H H19 . W5B H 4 .   ? 6.700   -27.317 29.824  0.68 31.55 ? 302 W5B B H19 1 
HETATM 3385 O O   . HOH I 5 .   ? 13.623  -22.621 17.673  1.00 46.93 ? 401 HOH A O   1 
HETATM 3386 O O   . HOH I 5 .   ? 7.269   -9.664  10.479  1.00 54.85 ? 402 HOH A O   1 
HETATM 3387 O O   . HOH I 5 .   ? 18.747  -28.617 -5.977  1.00 53.68 ? 403 HOH A O   1 
HETATM 3388 O O   . HOH I 5 .   ? 18.560  -20.455 21.344  1.00 49.52 ? 404 HOH A O   1 
HETATM 3389 O O   . HOH I 5 .   ? 9.701   -23.086 5.507   1.00 50.03 ? 405 HOH A O   1 
HETATM 3390 O O   . HOH I 5 .   ? 5.568   -2.174  4.093   1.00 43.47 ? 406 HOH A O   1 
HETATM 3391 O O   . HOH I 5 .   ? 16.816  -26.971 -5.830  1.00 55.11 ? 407 HOH A O   1 
HETATM 3392 O O   . HOH I 5 .   ? 20.538  -3.164  5.350   1.00 33.45 ? 408 HOH A O   1 
HETATM 3393 O O   . HOH I 5 .   ? 26.835  0.281   5.734   1.00 39.34 ? 409 HOH A O   1 
HETATM 3394 O O   . HOH I 5 .   ? 18.498  -17.399 -11.215 1.00 49.14 ? 410 HOH A O   1 
HETATM 3395 O O   . HOH I 5 .   ? 12.562  -21.601 -2.015  1.00 43.28 ? 411 HOH A O   1 
HETATM 3396 O O   . HOH I 5 .   ? 21.320  -6.520  -7.018  1.00 43.18 ? 412 HOH A O   1 
HETATM 3397 O O   . HOH I 5 .   ? 21.149  -14.546 14.147  1.00 32.61 ? 413 HOH A O   1 
HETATM 3398 O O   . HOH I 5 .   ? 34.520  -26.599 2.655   1.00 41.80 ? 414 HOH A O   1 
HETATM 3399 O O   . HOH I 5 .   ? 30.532  -23.007 6.340   1.00 42.08 ? 415 HOH A O   1 
HETATM 3400 O O   . HOH I 5 .   ? 13.829  -19.680 10.718  1.00 27.33 ? 416 HOH A O   1 
HETATM 3401 O O   . HOH I 5 .   ? 14.763  -27.670 10.040  1.00 54.85 ? 417 HOH A O   1 
HETATM 3402 O O   . HOH I 5 .   ? 3.528   -11.639 6.792   1.00 47.25 ? 418 HOH A O   1 
HETATM 3403 O O   . HOH I 5 .   ? 19.298  -8.091  -4.556  1.00 36.53 ? 419 HOH A O   1 
HETATM 3404 O O   . HOH I 5 .   ? 14.919  -12.275 -8.362  1.00 46.80 ? 420 HOH A O   1 
HETATM 3405 O O   . HOH I 5 .   ? 22.764  -26.847 -1.652  1.00 28.99 ? 421 HOH A O   1 
HETATM 3406 O O   . HOH I 5 .   ? 30.518  -16.395 10.911  1.00 49.82 ? 422 HOH A O   1 
HETATM 3407 O O   . HOH I 5 .   ? 28.897  -14.075 -11.027 1.00 44.34 ? 423 HOH A O   1 
HETATM 3408 O O   . HOH I 5 .   ? 14.976  -10.176 -5.817  1.00 38.64 ? 424 HOH A O   1 
HETATM 3409 O O   . HOH I 5 .   ? 23.211  -24.242 5.545   1.00 25.64 ? 425 HOH A O   1 
HETATM 3410 O O   . HOH I 5 .   ? 28.302  -29.448 6.135   1.00 32.98 ? 426 HOH A O   1 
HETATM 3411 O O   . HOH I 5 .   ? 27.947  -14.536 7.766   1.00 28.64 ? 427 HOH A O   1 
HETATM 3412 O O   . HOH I 5 .   ? 6.244   -7.501  9.307   1.00 56.01 ? 428 HOH A O   1 
HETATM 3413 O O   . HOH I 5 .   ? 30.848  -33.900 -7.662  1.00 64.04 ? 429 HOH A O   1 
HETATM 3414 O O   . HOH I 5 .   ? 23.122  -17.434 12.636  1.00 39.52 ? 430 HOH A O   1 
HETATM 3415 O O   . HOH I 5 .   ? 8.896   -14.833 -3.406  1.00 32.00 ? 431 HOH A O   1 
HETATM 3416 O O   . HOH I 5 .   ? 10.391  -16.207 -0.622  1.00 31.43 ? 432 HOH A O   1 
HETATM 3417 O O   . HOH I 5 .   ? 27.554  -17.267 8.315   1.00 27.17 ? 433 HOH A O   1 
HETATM 3418 O O   . HOH I 5 .   ? 12.347  -24.124 0.281   1.00 47.84 ? 434 HOH A O   1 
HETATM 3419 O O   . HOH I 5 .   ? 26.204  -23.613 15.941  1.00 62.73 ? 435 HOH A O   1 
HETATM 3420 O O   . HOH I 5 .   ? -11.170 -11.407 1.407   1.00 44.74 ? 436 HOH A O   1 
HETATM 3421 O O   . HOH I 5 .   ? 21.531  -30.239 5.550   1.00 33.96 ? 437 HOH A O   1 
HETATM 3422 O O   . HOH I 5 .   ? 25.873  0.214   2.607   1.00 32.78 ? 438 HOH A O   1 
HETATM 3423 O O   . HOH I 5 .   ? 14.865  -16.656 -10.160 1.00 45.28 ? 439 HOH A O   1 
HETATM 3424 O O   . HOH I 5 .   ? 40.902  -23.562 10.105  1.00 65.67 ? 440 HOH A O   1 
HETATM 3425 O O   . HOH I 5 .   ? 11.856  -20.933 12.201  1.00 42.39 ? 441 HOH A O   1 
HETATM 3426 O O   . HOH I 5 .   ? 26.145  -22.580 13.624  1.00 40.00 ? 442 HOH A O   1 
HETATM 3427 O O   . HOH I 5 .   ? 14.732  -18.728 -1.362  1.00 43.99 ? 443 HOH A O   1 
HETATM 3428 O O   . HOH I 5 .   ? 20.887  -3.855  8.033   1.00 40.44 ? 444 HOH A O   1 
HETATM 3429 O O   . HOH I 5 .   ? 2.873   -4.415  7.772   1.00 66.39 ? 445 HOH A O   1 
HETATM 3430 O O   . HOH I 5 .   ? 31.629  -32.009 -13.768 1.00 62.66 ? 446 HOH A O   1 
HETATM 3431 O O   . HOH I 5 .   ? 17.121  -29.975 13.330  1.00 47.22 ? 447 HOH A O   1 
HETATM 3432 O O   . HOH I 5 .   ? 35.401  -20.292 -10.533 1.00 68.92 ? 448 HOH A O   1 
HETATM 3433 O O   . HOH I 5 .   ? 15.495  -5.498  -11.107 1.00 43.47 ? 449 HOH A O   1 
HETATM 3434 O O   . HOH I 5 .   ? 39.718  -28.246 7.490   1.00 69.08 ? 450 HOH A O   1 
HETATM 3435 O O   . HOH I 5 .   ? 17.007  -28.827 -2.194  1.00 57.03 ? 451 HOH A O   1 
HETATM 3436 O O   . HOH I 5 .   ? 16.762  -8.116  -10.096 1.00 51.01 ? 452 HOH A O   1 
HETATM 3437 O O   . HOH I 5 .   ? 16.268  -17.434 -2.880  1.00 35.58 ? 453 HOH A O   1 
HETATM 3438 O O   . HOH I 5 .   ? 26.916  4.304   7.381   1.00 68.96 ? 454 HOH A O   1 
HETATM 3439 O O   . HOH I 5 .   ? 22.643  -29.635 -7.907  1.00 40.81 ? 455 HOH A O   1 
HETATM 3440 O O   . HOH I 5 .   ? 33.780  -8.336  17.867  1.00 62.06 ? 456 HOH A O   1 
HETATM 3441 O O   . HOH I 5 .   ? 6.222   -12.862 14.436  1.00 56.01 ? 457 HOH A O   1 
HETATM 3442 O O   . HOH I 5 .   ? 23.145  -16.101 14.925  1.00 49.44 ? 458 HOH A O   1 
HETATM 3443 O O   . HOH I 5 .   ? 3.945   -18.233 2.094   1.00 58.86 ? 459 HOH A O   1 
HETATM 3444 O O   . HOH I 5 .   ? 2.685   -0.989  1.325   1.00 72.85 ? 460 HOH A O   1 
HETATM 3445 O O   . HOH I 5 .   ? 17.774  -14.676 28.420  1.00 58.98 ? 461 HOH A O   1 
HETATM 3446 O O   . HOH I 5 .   ? 23.736  -4.227  -7.791  1.00 72.76 ? 462 HOH A O   1 
HETATM 3447 O O   . HOH I 5 .   ? 21.233  -17.918 30.113  1.00 58.37 ? 463 HOH A O   1 
HETATM 3448 O O   . HOH I 5 .   ? 31.515  -15.265 13.260  1.00 72.08 ? 464 HOH A O   1 
HETATM 3449 O O   . HOH I 5 .   ? 26.043  -17.263 12.696  1.00 55.23 ? 465 HOH A O   1 
HETATM 3450 O O   . HOH I 5 .   ? 21.731  -1.110  -7.527  1.00 65.37 ? 466 HOH A O   1 
HETATM 3451 O O   . HOH I 5 .   ? 27.560  -17.627 10.931  1.00 37.96 ? 467 HOH A O   1 
HETATM 3452 O O   . HOH I 5 .   ? 28.807  -31.923 4.725   1.00 48.08 ? 468 HOH A O   1 
HETATM 3453 O O   . HOH I 5 .   ? 29.563  -11.448 -11.743 1.00 47.03 ? 469 HOH A O   1 
HETATM 3454 O O   . HOH I 5 .   ? 6.890   -4.518  12.478  1.00 65.01 ? 470 HOH A O   1 
HETATM 3455 O O   . HOH I 5 .   ? 12.321  -27.965 -0.700  1.00 82.41 ? 471 HOH A O   1 
HETATM 3456 O O   . HOH J 5 .   ? -8.528  -1.892  34.267  1.00 65.00 ? 401 HOH B O   1 
HETATM 3457 O O   . HOH J 5 .   ? -5.411  -27.704 25.960  1.00 48.32 ? 402 HOH B O   1 
HETATM 3458 O O   . HOH J 5 .   ? -7.425  -18.981 41.359  1.00 47.07 ? 403 HOH B O   1 
HETATM 3459 O O   . HOH J 5 .   ? 11.556  -16.696 27.526  1.00 33.54 ? 404 HOH B O   1 
HETATM 3460 O O   . HOH J 5 .   ? 12.232  -25.526 16.965  1.00 41.32 ? 405 HOH B O   1 
HETATM 3461 O O   . HOH J 5 .   ? 2.229   -21.027 38.918  1.00 37.94 ? 406 HOH B O   1 
HETATM 3462 O O   . HOH J 5 .   ? 11.001  -8.844  27.550  1.00 47.63 ? 407 HOH B O   1 
HETATM 3463 O O   . HOH J 5 .   ? 8.817   -13.523 21.323  1.00 50.13 ? 408 HOH B O   1 
HETATM 3464 O O   . HOH J 5 .   ? -6.004  -5.738  42.100  1.00 65.28 ? 409 HOH B O   1 
HETATM 3465 O O   . HOH J 5 .   ? -0.956  -30.559 44.343  1.00 48.60 ? 410 HOH B O   1 
HETATM 3466 O O   . HOH J 5 .   ? 2.522   -32.675 31.724  1.00 37.79 ? 411 HOH B O   1 
HETATM 3467 O O   . HOH J 5 .   ? -2.934  -35.720 35.202  1.00 43.86 ? 412 HOH B O   1 
HETATM 3468 O O   . HOH J 5 .   ? 13.534  -27.471 21.954  1.00 60.12 ? 413 HOH B O   1 
HETATM 3469 O O   . HOH J 5 .   ? -1.016  -2.205  34.534  1.00 54.84 ? 414 HOH B O   1 
HETATM 3470 O O   . HOH J 5 .   ? -0.874  -9.857  48.249  1.00 62.69 ? 415 HOH B O   1 
HETATM 3471 O O   . HOH J 5 .   ? -4.587  -8.808  42.100  1.00 41.07 ? 416 HOH B O   1 
HETATM 3472 O O   . HOH J 5 .   ? 0.592   -12.510 40.154  1.00 39.28 ? 417 HOH B O   1 
HETATM 3473 O O   . HOH J 5 .   ? -0.757  -35.916 37.584  1.00 50.15 ? 418 HOH B O   1 
HETATM 3474 O O   . HOH J 5 .   ? 2.959   -18.321 38.688  1.00 39.58 ? 419 HOH B O   1 
HETATM 3475 O O   . HOH J 5 .   ? 2.812   -20.169 19.358  1.00 33.58 ? 420 HOH B O   1 
HETATM 3476 O O   . HOH J 5 .   ? -6.504  -23.692 19.938  1.00 52.61 ? 421 HOH B O   1 
HETATM 3477 O O   . HOH J 5 .   ? 1.560   -6.037  37.831  1.00 37.75 ? 422 HOH B O   1 
HETATM 3478 O O   . HOH J 5 .   ? -3.049  -8.841  29.600  1.00 37.04 ? 423 HOH B O   1 
HETATM 3479 O O   . HOH J 5 .   ? 11.101  -21.487 35.894  1.00 44.10 ? 424 HOH B O   1 
HETATM 3480 O O   . HOH J 5 .   ? 3.031   -11.571 33.220  1.00 32.53 ? 425 HOH B O   1 
HETATM 3481 O O   . HOH J 5 .   ? -4.104  -25.578 21.165  1.00 41.83 ? 426 HOH B O   1 
HETATM 3482 O O   . HOH J 5 .   ? 3.992   -5.590  31.386  1.00 37.84 ? 427 HOH B O   1 
HETATM 3483 O O   . HOH J 5 .   ? 1.260   -21.512 16.747  1.00 41.98 ? 428 HOH B O   1 
HETATM 3484 O O   . HOH J 5 .   ? 13.113  -29.824 20.950  1.00 46.43 ? 429 HOH B O   1 
HETATM 3485 O O   . HOH J 5 .   ? 7.932   -15.269 19.599  1.00 50.30 ? 430 HOH B O   1 
HETATM 3486 O O   . HOH J 5 .   ? 1.197   -24.326 47.566  1.00 60.71 ? 431 HOH B O   1 
HETATM 3487 O O   . HOH J 5 .   ? 20.575  -21.475 31.523  1.00 53.93 ? 432 HOH B O   1 
HETATM 3488 O O   . HOH J 5 .   ? 8.723   -13.078 39.566  1.00 54.85 ? 433 HOH B O   1 
HETATM 3489 O O   . HOH J 5 .   ? 13.796  -16.018 26.119  1.00 44.92 ? 434 HOH B O   1 
HETATM 3490 O O   . HOH J 5 .   ? -10.692 -4.259  27.933  1.00 55.30 ? 435 HOH B O   1 
HETATM 3491 O O   . HOH J 5 .   ? 1.324   -3.949  29.021  1.00 73.98 ? 436 HOH B O   1 
HETATM 3492 O O   . HOH J 5 .   ? -0.146  -12.555 50.169  1.00 52.53 ? 437 HOH B O   1 
HETATM 3493 O O   . HOH J 5 .   ? -1.881  -18.440 23.565  1.00 44.12 ? 438 HOH B O   1 
HETATM 3494 O O   . HOH J 5 .   ? -3.458  -8.782  48.052  1.00 62.79 ? 439 HOH B O   1 
HETATM 3495 O O   . HOH J 5 .   ? 8.140   -35.163 17.759  1.00 68.74 ? 440 HOH B O   1 
HETATM 3496 O O   . HOH J 5 .   ? -9.082  -27.744 20.776  1.00 47.37 ? 441 HOH B O   1 
HETATM 3497 O O   . HOH J 5 .   ? -8.394  -5.723  26.765  1.00 49.68 ? 442 HOH B O   1 
HETATM 3498 O O   . HOH J 5 .   ? 5.453   -18.420 40.017  1.00 46.27 ? 443 HOH B O   1 
HETATM 3499 O O   . HOH J 5 .   ? 6.986   -11.942 46.782  1.00 82.05 ? 444 HOH B O   1 
HETATM 3500 O O   . HOH J 5 .   ? 7.438   -14.299 16.303  1.00 65.81 ? 445 HOH B O   1 
HETATM 3501 O O   . HOH J 5 .   ? 10.769  -19.441 37.860  1.00 61.41 ? 446 HOH B O   1 
HETATM 3502 O O   . HOH J 5 .   ? 15.352  -13.329 27.861  1.00 73.57 ? 447 HOH B O   1 
HETATM 3503 O O   . HOH J 5 .   ? 7.481   -18.095 39.094  1.00 50.47 ? 448 HOH B O   1 
HETATM 3504 O O   . HOH J 5 .   ? -1.046  -33.840 11.035  1.00 67.61 ? 449 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ALA A 9   ? 0.6438 0.5999 0.7698 -0.0544 -0.1310 0.0326  11  ALA A N   
2    C CA  . ALA A 9   ? 0.6373 0.5951 0.7433 -0.0491 -0.1254 0.0324  11  ALA A CA  
3    C C   . ALA A 9   ? 0.6251 0.5882 0.7393 -0.0457 -0.1100 0.0341  11  ALA A C   
4    O O   . ALA A 9   ? 0.6273 0.5967 0.7651 -0.0474 -0.1052 0.0385  11  ALA A O   
5    C CB  . ALA A 9   ? 0.6401 0.6056 0.7479 -0.0496 -0.1326 0.0397  11  ALA A CB  
6    N N   . ARG A 10  ? 0.6003 0.5611 0.6954 -0.0408 -0.1024 0.0304  12  ARG A N   
7    C CA  . ARG A 10  ? 0.5543 0.5200 0.6553 -0.0377 -0.0891 0.0315  12  ARG A CA  
8    C C   . ARG A 10  ? 0.5277 0.5038 0.6434 -0.0372 -0.0860 0.0390  12  ARG A C   
9    O O   . ARG A 10  ? 0.5497 0.5286 0.6592 -0.0366 -0.0913 0.0429  12  ARG A O   
10   C CB  . ARG A 10  ? 0.5529 0.5143 0.6312 -0.0327 -0.0831 0.0263  12  ARG A CB  
11   C CG  . ARG A 10  ? 0.5804 0.5457 0.6635 -0.0297 -0.0703 0.0261  12  ARG A CG  
12   C CD  . ARG A 10  ? 0.6131 0.5745 0.6761 -0.0249 -0.0652 0.0213  12  ARG A CD  
13   N NE  . ARG A 10  ? 0.6346 0.5857 0.6856 -0.0247 -0.0691 0.0148  12  ARG A NE  
14   C CZ  . ARG A 10  ? 0.6361 0.5826 0.6916 -0.0253 -0.0662 0.0120  12  ARG A CZ  
15   N NH1 . ARG A 10  ? 0.6518 0.6035 0.7213 -0.0261 -0.0591 0.0148  12  ARG A NH1 
16   N NH2 . ARG A 10  ? 0.5941 0.5305 0.6400 -0.0252 -0.0704 0.0064  12  ARG A NH2 
17   N N   . ILE A 11  ? 0.4770 0.4585 0.6120 -0.0376 -0.0772 0.0411  13  ILE A N   
18   C CA  . ILE A 11  ? 0.4466 0.4370 0.5971 -0.0367 -0.0727 0.0470  13  ILE A CA  
19   C C   . ILE A 11  ? 0.4597 0.4514 0.5977 -0.0323 -0.0644 0.0457  13  ILE A C   
20   O O   . ILE A 11  ? 0.4631 0.4537 0.5989 -0.0307 -0.0556 0.0414  13  ILE A O   
21   C CB  . ILE A 11  ? 0.4324 0.4276 0.6081 -0.0387 -0.0659 0.0484  13  ILE A CB  
22   C CG1 . ILE A 11  ? 0.4401 0.4343 0.6303 -0.0434 -0.0730 0.0498  13  ILE A CG1 
23   C CG2 . ILE A 11  ? 0.4385 0.4418 0.6319 -0.0377 -0.0616 0.0539  13  ILE A CG2 
24   C CD1 . ILE A 11  ? 0.4417 0.4401 0.6543 -0.0451 -0.0646 0.0506  13  ILE A CD1 
25   N N   . ILE A 12  ? 0.4486 0.4430 0.5796 -0.0305 -0.0674 0.0500  14  ILE A N   
26   C CA  . ILE A 12  ? 0.4724 0.4684 0.5920 -0.0266 -0.0606 0.0499  14  ILE A CA  
27   C C   . ILE A 12  ? 0.4666 0.4703 0.6024 -0.0262 -0.0586 0.0575  14  ILE A C   
28   O O   . ILE A 12  ? 0.4716 0.4782 0.6140 -0.0278 -0.0665 0.0642  14  ILE A O   
29   C CB  . ILE A 12  ? 0.5044 0.4958 0.5975 -0.0245 -0.0653 0.0482  14  ILE A CB  
30   C CG1 . ILE A 12  ? 0.5488 0.5311 0.6269 -0.0245 -0.0674 0.0398  14  ILE A CG1 
31   C CG2 . ILE A 12  ? 0.5069 0.5011 0.5905 -0.0204 -0.0578 0.0494  14  ILE A CG2 
32   C CD1 . ILE A 12  ? 0.5879 0.5648 0.6414 -0.0228 -0.0725 0.0368  14  ILE A CD1 
33   N N   . TYR A 13  ? 0.4204 0.4274 0.5637 -0.0244 -0.0489 0.0569  15  TYR A N   
34   C CA  . TYR A 13  ? 0.4040 0.4174 0.5631 -0.0236 -0.0458 0.0635  15  TYR A CA  
35   C C   . TYR A 13  ? 0.4595 0.4739 0.6073 -0.0204 -0.0400 0.0639  15  TYR A C   
36   O O   . TYR A 13  ? 0.4497 0.4622 0.5897 -0.0189 -0.0335 0.0574  15  TYR A O   
37   C CB  . TYR A 13  ? 0.3938 0.4103 0.5763 -0.0246 -0.0386 0.0619  15  TYR A CB  
38   C CG  . TYR A 13  ? 0.4045 0.4213 0.6028 -0.0277 -0.0420 0.0620  15  TYR A CG  
39   C CD1 . TYR A 13  ? 0.4165 0.4371 0.6313 -0.0293 -0.0488 0.0696  15  TYR A CD1 
40   C CD2 . TYR A 13  ? 0.4072 0.4212 0.6056 -0.0290 -0.0381 0.0555  15  TYR A CD2 
41   C CE1 . TYR A 13  ? 0.4034 0.4252 0.6358 -0.0321 -0.0515 0.0702  15  TYR A CE1 
42   C CE2 . TYR A 13  ? 0.4021 0.4171 0.6167 -0.0320 -0.0402 0.0563  15  TYR A CE2 
43   C CZ  . TYR A 13  ? 0.4057 0.4248 0.6380 -0.0335 -0.0469 0.0635  15  TYR A CZ  
44   O OH  . TYR A 13  ? 0.3911 0.4120 0.6415 -0.0363 -0.0487 0.0646  15  TYR A OH  
45   N N   . ASP A 14  ? 0.4668 0.4849 0.6149 -0.0195 -0.0423 0.0718  16  ASP A N   
46   C CA  . ASP A 14  ? 0.4799 0.5002 0.6222 -0.0168 -0.0358 0.0735  16  ASP A CA  
47   C C   . ASP A 14  ? 0.4474 0.4717 0.6130 -0.0168 -0.0280 0.0741  16  ASP A C   
48   O O   . ASP A 14  ? 0.4207 0.4463 0.6069 -0.0187 -0.0275 0.0740  16  ASP A O   
49   C CB  . ASP A 14  ? 0.5308 0.5531 0.6605 -0.0156 -0.0403 0.0820  16  ASP A CB  
50   C CG  . ASP A 14  ? 0.6205 0.6474 0.7660 -0.0171 -0.0458 0.0927  16  ASP A CG  
51   O OD1 . ASP A 14  ? 0.6392 0.6687 0.8104 -0.0183 -0.0437 0.0944  16  ASP A OD1 
52   O OD2 . ASP A 14  ? 0.6540 0.6817 0.7860 -0.0169 -0.0523 0.0996  16  ASP A OD2 
53   N N   . ARG A 15  ? 0.4442 0.4703 0.6068 -0.0148 -0.0217 0.0744  17  ARG A N   
54   C CA  . ARG A 15  ? 0.4361 0.4651 0.6182 -0.0149 -0.0144 0.0735  17  ARG A CA  
55   C C   . ARG A 15  ? 0.4465 0.4789 0.6529 -0.0161 -0.0158 0.0814  17  ARG A C   
56   O O   . ARG A 15  ? 0.4232 0.4561 0.6496 -0.0172 -0.0119 0.0781  17  ARG A O   
57   C CB  . ARG A 15  ? 0.4398 0.4709 0.6144 -0.0126 -0.0090 0.0746  17  ARG A CB  
58   C CG  . ARG A 15  ? 0.4708 0.5037 0.6619 -0.0130 -0.0020 0.0711  17  ARG A CG  
59   C CD  . ARG A 15  ? 0.5197 0.5558 0.7076 -0.0111 0.0024  0.0747  17  ARG A CD  
60   N NE  . ARG A 15  ? 0.5602 0.5981 0.7666 -0.0120 0.0083  0.0714  17  ARG A NE  
61   C CZ  . ARG A 15  ? 0.6364 0.6760 0.8659 -0.0133 0.0099  0.0756  17  ARG A CZ  
62   N NH1 . ARG A 15  ? 0.6672 0.7077 0.9056 -0.0137 0.0059  0.0845  17  ARG A NH1 
63   N NH2 . ARG A 15  ? 0.6685 0.7088 0.9131 -0.0143 0.0149  0.0707  17  ARG A NH2 
64   N N   . ALA A 16  ? 0.4778 0.5125 0.6819 -0.0158 -0.0214 0.0918  18  ALA A N   
65   C CA  . ALA A 16  ? 0.4702 0.5084 0.6985 -0.0166 -0.0236 0.1013  18  ALA A CA  
66   C C   . ALA A 16  ? 0.4650 0.5027 0.7102 -0.0185 -0.0270 0.0993  18  ALA A C   
67   O O   . ALA A 16  ? 0.4838 0.5231 0.7550 -0.0190 -0.0234 0.1002  18  ALA A O   
68   C CB  . ALA A 16  ? 0.4817 0.5222 0.6995 -0.0161 -0.0303 0.1132  18  ALA A CB  
69   N N   . PHE A 17  ? 0.4724 0.5078 0.7049 -0.0197 -0.0333 0.0965  19  PHE A N   
70   C CA  . PHE A 17  ? 0.4743 0.5096 0.7228 -0.0217 -0.0361 0.0945  19  PHE A CA  
71   C C   . PHE A 17  ? 0.4665 0.5008 0.7284 -0.0220 -0.0266 0.0849  19  PHE A C   
72   O O   . PHE A 17  ? 0.4639 0.5003 0.7509 -0.0226 -0.0241 0.0857  19  PHE A O   
73   C CB  . PHE A 17  ? 0.4969 0.5292 0.7274 -0.0231 -0.0440 0.0918  19  PHE A CB  
74   C CG  . PHE A 17  ? 0.5112 0.5450 0.7608 -0.0256 -0.0492 0.0936  19  PHE A CG  
75   C CD1 . PHE A 17  ? 0.5353 0.5727 0.7960 -0.0266 -0.0587 0.1040  19  PHE A CD1 
76   C CD2 . PHE A 17  ? 0.5287 0.5611 0.7876 -0.0268 -0.0443 0.0858  19  PHE A CD2 
77   C CE1 . PHE A 17  ? 0.5402 0.5798 0.8211 -0.0288 -0.0637 0.1060  19  PHE A CE1 
78   C CE2 . PHE A 17  ? 0.5420 0.5766 0.8207 -0.0290 -0.0483 0.0880  19  PHE A CE2 
79   C CZ  . PHE A 17  ? 0.5380 0.5763 0.8281 -0.0300 -0.0582 0.0979  19  PHE A CZ  
80   N N   . LEU A 18  ? 0.4286 0.4598 0.6736 -0.0214 -0.0212 0.0757  20  LEU A N   
81   C CA  . LEU A 18  ? 0.3965 0.4267 0.6507 -0.0219 -0.0127 0.0666  20  LEU A CA  
82   C C   . LEU A 18  ? 0.4036 0.4362 0.6800 -0.0214 -0.0060 0.0669  20  LEU A C   
83   O O   . LEU A 18  ? 0.4141 0.4470 0.7085 -0.0222 -0.0009 0.0626  20  LEU A O   
84   C CB  . LEU A 18  ? 0.3822 0.4091 0.6134 -0.0213 -0.0095 0.0585  20  LEU A CB  
85   C CG  . LEU A 18  ? 0.3585 0.3817 0.5703 -0.0219 -0.0152 0.0563  20  LEU A CG  
86   C CD1 . LEU A 18  ? 0.3344 0.3543 0.5245 -0.0205 -0.0123 0.0498  20  LEU A CD1 
87   C CD2 . LEU A 18  ? 0.4091 0.4316 0.6305 -0.0242 -0.0155 0.0535  20  LEU A CD2 
88   N N   . MET A 19  ? 0.4125 0.4464 0.6883 -0.0200 -0.0057 0.0721  21  MET A N   
89   C CA  . MET A 19  ? 0.4549 0.4902 0.7517 -0.0196 0.0001  0.0729  21  MET A CA  
90   C C   . MET A 19  ? 0.5013 0.5389 0.8258 -0.0199 -0.0018 0.0800  21  MET A C   
91   O O   . MET A 19  ? 0.5276 0.5651 0.8740 -0.0198 0.0042  0.0773  21  MET A O   
92   C CB  . MET A 19  ? 0.4755 0.5121 0.7655 -0.0183 0.0004  0.0786  21  MET A CB  
93   C CG  . MET A 19  ? 0.5167 0.5521 0.7854 -0.0177 0.0036  0.0717  21  MET A CG  
94   S SD  . MET A 19  ? 0.5285 0.5619 0.8014 -0.0187 0.0117  0.0577  21  MET A SD  
95   C CE  . MET A 19  ? 0.6254 0.6599 0.9298 -0.0191 0.0164  0.0599  21  MET A CE  
96   N N   . ALA A 20  ? 0.5330 0.5723 0.8575 -0.0202 -0.0103 0.0886  22  ALA A N   
97   C CA  . ALA A 20  ? 0.5402 0.5824 0.8927 -0.0204 -0.0134 0.0965  22  ALA A CA  
98   C C   . ALA A 20  ? 0.5693 0.6112 0.9374 -0.0214 -0.0094 0.0889  22  ALA A C   
99   O O   . ALA A 20  ? 0.5834 0.6272 0.9802 -0.0210 -0.0069 0.0913  22  ALA A O   
100  C CB  . ALA A 20  ? 0.5361 0.5805 0.8805 -0.0209 -0.0252 0.1078  22  ALA A CB  
101  N N   . CYS A 21  ? 0.5558 0.5955 0.9058 -0.0225 -0.0083 0.0803  23  CYS A N   
102  C CA  . CYS A 21  ? 0.5402 0.5801 0.9022 -0.0236 -0.0032 0.0732  23  CYS A CA  
103  C C   . CYS A 21  ? 0.5498 0.5881 0.9199 -0.0232 0.0086  0.0628  23  CYS A C   
104  O O   . CYS A 21  ? 0.5636 0.6020 0.9413 -0.0240 0.0144  0.0562  23  CYS A O   
105  C CB  . CYS A 21  ? 0.5436 0.5815 0.8837 -0.0252 -0.0065 0.0691  23  CYS A CB  
106  S SG  . CYS A 21  ? 0.5976 0.6363 0.9262 -0.0264 -0.0210 0.0787  23  CYS A SG  
107  N N   . ARG A 22  ? 0.5519 0.5887 0.9191 -0.0222 0.0122  0.0607  24  ARG A N   
108  C CA  . ARG A 22  ? 0.5944 0.6291 0.9657 -0.0222 0.0222  0.0497  24  ARG A CA  
109  C C   . ARG A 22  ? 0.6514 0.6869 1.0562 -0.0213 0.0278  0.0497  24  ARG A C   
110  O O   . ARG A 22  ? 0.6468 0.6840 1.0697 -0.0203 0.0235  0.0598  24  ARG A O   
111  C CB  . ARG A 22  ? 0.5933 0.6264 0.9498 -0.0218 0.0227  0.0480  24  ARG A CB  
112  C CG  . ARG A 22  ? 0.6165 0.6473 0.9764 -0.0222 0.0313  0.0367  24  ARG A CG  
113  C CD  . ARG A 22  ? 0.6104 0.6407 0.9626 -0.0219 0.0306  0.0374  24  ARG A CD  
114  N NE  . ARG A 22  ? 0.6083 0.6364 0.9571 -0.0229 0.0372  0.0253  24  ARG A NE  
115  C CZ  . ARG A 22  ? 0.5872 0.6150 0.9252 -0.0232 0.0371  0.0226  24  ARG A CZ  
116  N NH1 . ARG A 22  ? 0.5884 0.6179 0.9177 -0.0223 0.0322  0.0313  24  ARG A NH1 
117  N NH2 . ARG A 22  ? 0.5964 0.6223 0.9318 -0.0245 0.0420  0.0113  24  ARG A NH2 
118  N N   . GLY A 23  ? 0.6927 0.7266 1.1048 -0.0216 0.0374  0.0384  25  GLY A N   
119  C CA  . GLY A 23  ? 0.7342 0.7677 1.1771 -0.0205 0.0445  0.0355  25  GLY A CA  
120  C C   . GLY A 23  ? 0.7700 0.8069 1.2401 -0.0194 0.0412  0.0455  25  GLY A C   
121  O O   . GLY A 23  ? 0.7694 0.8063 1.2674 -0.0178 0.0431  0.0489  25  GLY A O   
122  N N   . GLY A 24  ? 0.7916 0.8316 1.2550 -0.0202 0.0360  0.0502  26  GLY A N   
123  C CA  . GLY A 24  ? 0.8059 0.8501 1.2898 -0.0197 0.0286  0.0624  26  GLY A CA  
124  C C   . GLY A 24  ? 0.8123 0.8588 1.3316 -0.0184 0.0353  0.0614  26  GLY A C   
125  O O   . GLY A 24  ? 0.8107 0.8591 1.3569 -0.0168 0.0321  0.0705  26  GLY A O   
126  N N   . GLY A 25  ? 0.8166 0.8629 1.3366 -0.0188 0.0451  0.0509  27  GLY A N   
127  C CA  . GLY A 25  ? 0.8061 0.8555 1.3593 -0.0174 0.0524  0.0499  27  GLY A CA  
128  C C   . GLY A 25  ? 0.7960 0.8515 1.3648 -0.0179 0.0439  0.0615  27  GLY A C   
129  O O   . GLY A 25  ? 0.7849 0.8441 1.3881 -0.0162 0.0468  0.0653  27  GLY A O   
130  N N   . GLY A 26  ? 0.7900 0.8464 1.3346 -0.0202 0.0333  0.0670  28  GLY A N   
131  C CA  . GLY A 26  ? 0.7734 0.8352 1.3300 -0.0215 0.0233  0.0777  28  GLY A CA  
132  C C   . GLY A 26  ? 0.7373 0.8030 1.3109 -0.0221 0.0312  0.0735  28  GLY A C   
133  O O   . GLY A 26  ? 0.7479 0.8114 1.3086 -0.0227 0.0422  0.0624  28  GLY A O   
134  N N   . GLU A 27  ? 0.6910 0.7628 1.2941 -0.0220 0.0258  0.0830  29  GLU A N   
135  C CA  . GLU A 27  ? 0.6421 0.7188 1.2638 -0.0229 0.0324  0.0811  29  GLU A CA  
136  C C   . GLU A 27  ? 0.6126 0.6892 1.2082 -0.0268 0.0239  0.0825  29  GLU A C   
137  O O   . GLU A 27  ? 0.6441 0.7221 1.2346 -0.0287 0.0084  0.0922  29  GLU A O   
138  C CB  . GLU A 27  ? 0.6685 0.7524 1.3334 -0.0214 0.0284  0.0917  29  GLU A CB  
139  C CG  . GLU A 27  ? 0.7337 0.8172 1.4283 -0.0172 0.0360  0.0914  29  GLU A CG  
140  C CD  . GLU A 27  ? 0.8118 0.8974 1.5321 -0.0150 0.0539  0.0821  29  GLU A CD  
141  O OE1 . GLU A 27  ? 0.7935 0.8864 1.5463 -0.0146 0.0547  0.0878  29  GLU A OE1 
142  O OE2 . GLU A 27  ? 0.8478 0.9280 1.5556 -0.0138 0.0672  0.0690  29  GLU A OE2 
143  N N   . ASN A 28  ? 0.5322 0.6068 1.1107 -0.0283 0.0337  0.0729  30  ASN A N   
144  C CA  . ASN A 28  ? 0.4531 0.5270 1.0093 -0.0320 0.0268  0.0738  30  ASN A CA  
145  C C   . ASN A 28  ? 0.3713 0.4527 0.9580 -0.0338 0.0248  0.0806  30  ASN A C   
146  O O   . ASN A 28  ? 0.3390 0.4219 0.9257 -0.0355 0.0331  0.0765  30  ASN A O   
147  C CB  . ASN A 28  ? 0.4369 0.5062 0.9658 -0.0328 0.0379  0.0625  30  ASN A CB  
148  C CG  . ASN A 28  ? 0.4330 0.5001 0.9382 -0.0363 0.0313  0.0632  30  ASN A CG  
149  O OD1 . ASN A 28  ? 0.4323 0.4992 0.9322 -0.0382 0.0169  0.0704  30  ASN A OD1 
150  N ND2 . ASN A 28  ? 0.4612 0.5264 0.9512 -0.0374 0.0414  0.0557  30  ASN A ND2 
151  N N   . LEU A 29  ? 0.3376 0.4240 0.9505 -0.0334 0.0137  0.0916  31  LEU A N   
152  C CA  . LEU A 29  ? 0.3458 0.4404 0.9916 -0.0351 0.0088  0.1000  31  LEU A CA  
153  C C   . LEU A 29  ? 0.3142 0.4081 0.9431 -0.0398 0.0023  0.1003  31  LEU A C   
154  O O   . LEU A 29  ? 0.3194 0.4080 0.9182 -0.0419 -0.0093 0.1010  31  LEU A O   
155  C CB  . LEU A 29  ? 0.3843 0.4830 1.0500 -0.0348 -0.0078 0.1131  31  LEU A CB  
156  C CG  . LEU A 29  ? 0.4673 0.5716 1.1739 -0.0310 -0.0040 0.1188  31  LEU A CG  
157  C CD1 . LEU A 29  ? 0.4878 0.5879 1.1938 -0.0271 0.0120  0.1093  31  LEU A CD1 
158  C CD2 . LEU A 29  ? 0.4891 0.5947 1.2008 -0.0306 -0.0216 0.1314  31  LEU A CD2 
159  N N   . TYR A 30  ? 0.2912 0.3904 0.9408 -0.0414 0.0101  0.0999  32  TYR A N   
160  C CA  . TYR A 30  ? 0.2995 0.3990 0.9417 -0.0461 0.0048  0.1014  32  TYR A CA  
161  C C   . TYR A 30  ? 0.3021 0.3929 0.9020 -0.0476 0.0088  0.0926  32  TYR A C   
162  O O   . TYR A 30  ? 0.2978 0.3867 0.8862 -0.0516 0.0013  0.0941  32  TYR A O   
163  C CB  . TYR A 30  ? 0.3133 0.4145 0.9599 -0.0492 -0.0168 0.1115  32  TYR A CB  
164  C CG  . TYR A 30  ? 0.3211 0.4313 1.0087 -0.0481 -0.0234 0.1217  32  TYR A CG  
165  C CD1 . TYR A 30  ? 0.3224 0.4416 1.0492 -0.0491 -0.0186 0.1261  32  TYR A CD1 
166  C CD2 . TYR A 30  ? 0.3350 0.4448 1.0231 -0.0459 -0.0343 0.1279  32  TYR A CD2 
167  C CE1 . TYR A 30  ? 0.3332 0.4611 1.0995 -0.0480 -0.0256 0.1362  32  TYR A CE1 
168  C CE2 . TYR A 30  ? 0.3492 0.4674 1.0760 -0.0449 -0.0416 0.1386  32  TYR A CE2 
169  C CZ  . TYR A 30  ? 0.3485 0.4757 1.1151 -0.0458 -0.0369 0.1424  32  TYR A CZ  
170  O OH  . TYR A 30  ? 0.4001 0.5367 1.2092 -0.0449 -0.0441 0.1536  32  TYR A OH  
171  N N   . PHE A 31  ? 0.3222 0.4080 0.9017 -0.0445 0.0201  0.0838  33  PHE A N   
172  C CA  . PHE A 31  ? 0.3625 0.4399 0.9006 -0.0452 0.0215  0.0763  33  PHE A CA  
173  C C   . PHE A 31  ? 0.3769 0.4489 0.8905 -0.0471 0.0040  0.0798  33  PHE A C   
174  O O   . PHE A 31  ? 0.3868 0.4528 0.8722 -0.0489 0.0022  0.0759  33  PHE A O   
175  C CB  . PHE A 31  ? 0.3805 0.4578 0.9125 -0.0478 0.0314  0.0725  33  PHE A CB  
176  C CG  . PHE A 31  ? 0.4022 0.4836 0.9494 -0.0457 0.0508  0.0668  33  PHE A CG  
177  C CD1 . PHE A 31  ? 0.4347 0.5117 0.9610 -0.0432 0.0622  0.0572  33  PHE A CD1 
178  C CD2 . PHE A 31  ? 0.4100 0.4998 0.9926 -0.0462 0.0578  0.0708  33  PHE A CD2 
179  C CE1 . PHE A 31  ? 0.4520 0.5323 0.9900 -0.0413 0.0802  0.0508  33  PHE A CE1 
180  C CE2 . PHE A 31  ? 0.4268 0.5201 1.0220 -0.0439 0.0769  0.0648  33  PHE A CE2 
181  C CZ  . PHE A 31  ? 0.4360 0.5243 1.0082 -0.0415 0.0879  0.0545  33  PHE A CZ  
182  N N   . GLN A 32  ? 0.3674 0.4412 0.8909 -0.0464 -0.0089 0.0871  34  GLN A N   
183  C CA  . GLN A 32  ? 0.3867 0.4559 0.8873 -0.0481 -0.0259 0.0907  34  GLN A CA  
184  C C   . GLN A 32  ? 0.3938 0.4607 0.8823 -0.0448 -0.0298 0.0919  34  GLN A C   
185  O O   . GLN A 32  ? 0.4307 0.4953 0.9050 -0.0456 -0.0436 0.0965  34  GLN A O   
186  C CB  . GLN A 32  ? 0.3767 0.4506 0.8973 -0.0516 -0.0407 0.0999  34  GLN A CB  
187  C CG  . GLN A 32  ? 0.4037 0.4794 0.9350 -0.0556 -0.0386 0.0994  34  GLN A CG  
188  C CD  . GLN A 32  ? 0.4295 0.5094 0.9798 -0.0596 -0.0546 0.1079  34  GLN A CD  
189  O OE1 . GLN A 32  ? 0.4099 0.4871 0.9469 -0.0609 -0.0707 0.1114  34  GLN A OE1 
190  N NE2 . GLN A 32  ? 0.4281 0.5151 1.0106 -0.0620 -0.0507 0.1114  34  GLN A NE2 
191  N N   . GLY A 33  ? 0.3636 0.4308 0.8579 -0.0413 -0.0177 0.0879  35  GLY A N   
192  C CA  . GLY A 33  ? 0.3685 0.4345 0.8594 -0.0382 -0.0197 0.0901  35  GLY A CA  
193  C C   . GLY A 33  ? 0.4106 0.4694 0.8663 -0.0369 -0.0154 0.0821  35  GLY A C   
194  O O   . GLY A 33  ? 0.4492 0.5063 0.8971 -0.0348 -0.0176 0.0838  35  GLY A O   
195  N N   . LYS A 34  ? 0.4089 0.4638 0.8447 -0.0383 -0.0093 0.0742  36  LYS A N   
196  C CA  . LYS A 34  ? 0.4243 0.4730 0.8280 -0.0371 -0.0061 0.0672  36  LYS A CA  
197  C C   . LYS A 34  ? 0.4400 0.4842 0.8172 -0.0386 -0.0184 0.0693  36  LYS A C   
198  O O   . LYS A 34  ? 0.4567 0.5014 0.8364 -0.0413 -0.0276 0.0733  36  LYS A O   
199  C CB  . LYS A 34  ? 0.4346 0.4815 0.8301 -0.0375 0.0069  0.0580  36  LYS A CB  
200  C CG  . LYS A 34  ? 0.4295 0.4790 0.8431 -0.0353 0.0204  0.0531  36  LYS A CG  
201  C CD  . LYS A 34  ? 0.4679 0.5162 0.8719 -0.0360 0.0327  0.0444  36  LYS A CD  
202  C CE  . LYS A 34  ? 0.4983 0.5481 0.9164 -0.0338 0.0460  0.0378  36  LYS A CE  
203  N NZ  . LYS A 34  ? 0.5549 0.6039 0.9617 -0.0347 0.0580  0.0295  36  LYS A NZ  
204  N N   . HIS A 35  ? 0.4195 0.4593 0.7721 -0.0368 -0.0186 0.0662  37  HIS A N   
205  C CA  . HIS A 35  ? 0.4320 0.4673 0.7589 -0.0373 -0.0291 0.0675  37  HIS A CA  
206  C C   . HIS A 35  ? 0.4284 0.4583 0.7330 -0.0382 -0.0255 0.0601  37  HIS A C   
207  O O   . HIS A 35  ? 0.4180 0.4460 0.7113 -0.0365 -0.0169 0.0541  37  HIS A O   
208  C CB  . HIS A 35  ? 0.4668 0.5013 0.7820 -0.0346 -0.0311 0.0697  37  HIS A CB  
209  C CG  . HIS A 35  ? 0.5058 0.5451 0.8405 -0.0341 -0.0372 0.0790  37  HIS A CG  
210  N ND1 . HIS A 35  ? 0.5403 0.5833 0.8982 -0.0322 -0.0301 0.0807  37  HIS A ND1 
211  C CD2 . HIS A 35  ? 0.5192 0.5598 0.8535 -0.0353 -0.0502 0.0871  37  HIS A CD2 
212  C CE1 . HIS A 35  ? 0.5340 0.5806 0.9060 -0.0322 -0.0388 0.0908  37  HIS A CE1 
213  N NE2 . HIS A 35  ? 0.5264 0.5720 0.8839 -0.0341 -0.0513 0.0950  37  HIS A NE2 
214  N N   . PRO A 36  ? 0.4194 0.4467 0.7187 -0.0410 -0.0323 0.0606  38  PRO A N   
215  C CA  . PRO A 36  ? 0.4046 0.4267 0.6862 -0.0419 -0.0284 0.0544  38  PRO A CA  
216  C C   . PRO A 36  ? 0.4031 0.4193 0.6556 -0.0397 -0.0304 0.0507  38  PRO A C   
217  O O   . PRO A 36  ? 0.3835 0.3984 0.6259 -0.0386 -0.0384 0.0533  38  PRO A O   
218  C CB  . PRO A 36  ? 0.4347 0.4553 0.7221 -0.0456 -0.0369 0.0572  38  PRO A CB  
219  C CG  . PRO A 36  ? 0.4488 0.4716 0.7431 -0.0461 -0.0489 0.0635  38  PRO A CG  
220  C CD  . PRO A 36  ? 0.4212 0.4501 0.7321 -0.0437 -0.0443 0.0670  38  PRO A CD  
221  N N   . LEU A 37  ? 0.3871 0.4002 0.6264 -0.0390 -0.0228 0.0448  39  LEU A N   
222  C CA  . LEU A 37  ? 0.3749 0.3823 0.5882 -0.0370 -0.0246 0.0411  39  LEU A CA  
223  C C   . LEU A 37  ? 0.3743 0.3754 0.5764 -0.0389 -0.0311 0.0401  39  LEU A C   
224  O O   . LEU A 37  ? 0.3767 0.3779 0.5900 -0.0419 -0.0308 0.0410  39  LEU A O   
225  C CB  . LEU A 37  ? 0.3617 0.3693 0.5677 -0.0353 -0.0140 0.0358  39  LEU A CB  
226  C CG  . LEU A 37  ? 0.3633 0.3759 0.5789 -0.0335 -0.0074 0.0351  39  LEU A CG  
227  C CD1 . LEU A 37  ? 0.3724 0.3846 0.5789 -0.0325 0.0015  0.0290  39  LEU A CD1 
228  C CD2 . LEU A 37  ? 0.3595 0.3728 0.5717 -0.0313 -0.0125 0.0385  39  LEU A CD2 
229  N N   . GLN A 38  ? 0.3826 0.3780 0.5631 -0.0370 -0.0362 0.0379  40  GLN A N   
230  C CA  . GLN A 38  ? 0.3988 0.3865 0.5662 -0.0381 -0.0418 0.0354  40  GLN A CA  
231  C C   . GLN A 38  ? 0.4043 0.3898 0.5711 -0.0390 -0.0350 0.0328  40  GLN A C   
232  O O   . GLN A 38  ? 0.4194 0.4009 0.5893 -0.0419 -0.0381 0.0331  40  GLN A O   
233  C CB  . GLN A 38  ? 0.4191 0.4018 0.5636 -0.0347 -0.0452 0.0325  40  GLN A CB  
234  C CG  . GLN A 38  ? 0.4489 0.4224 0.5786 -0.0350 -0.0507 0.0286  40  GLN A CG  
235  C CD  . GLN A 38  ? 0.5201 0.4902 0.6546 -0.0386 -0.0614 0.0299  40  GLN A CD  
236  O OE1 . GLN A 38  ? 0.4903 0.4649 0.6342 -0.0400 -0.0668 0.0340  40  GLN A OE1 
237  N NE2 . GLN A 38  ? 0.5436 0.5055 0.6725 -0.0401 -0.0653 0.0267  40  GLN A NE2 
238  N N   . ASN A 39  ? 0.3815 0.3697 0.5445 -0.0369 -0.0258 0.0305  41  ASN A N   
239  C CA  . ASN A 39  ? 0.3826 0.3695 0.5421 -0.0375 -0.0190 0.0285  41  ASN A CA  
240  C C   . ASN A 39  ? 0.3473 0.3411 0.5194 -0.0382 -0.0094 0.0285  41  ASN A C   
241  O O   . ASN A 39  ? 0.3573 0.3561 0.5374 -0.0371 -0.0069 0.0286  41  ASN A O   
242  C CB  . ASN A 39  ? 0.4152 0.3984 0.5549 -0.0340 -0.0179 0.0250  41  ASN A CB  
243  C CG  . ASN A 39  ? 0.4914 0.4664 0.6183 -0.0332 -0.0255 0.0238  41  ASN A CG  
244  O OD1 . ASN A 39  ? 0.5119 0.4819 0.6384 -0.0351 -0.0271 0.0240  41  ASN A OD1 
245  N ND2 . ASN A 39  ? 0.5132 0.4865 0.6299 -0.0304 -0.0299 0.0225  41  ASN A ND2 
246  N N   . ARG A 40  ? 0.3383 0.3320 0.5117 -0.0402 -0.0034 0.0283  42  ARG A N   
247  C CA  . ARG A 40  ? 0.3465 0.3457 0.5252 -0.0404 0.0070  0.0264  42  ARG A CA  
248  C C   . ARG A 40  ? 0.3319 0.3297 0.4919 -0.0379 0.0098  0.0224  42  ARG A C   
249  O O   . ARG A 40  ? 0.3388 0.3313 0.4846 -0.0370 0.0059  0.0224  42  ARG A O   
250  C CB  . ARG A 40  ? 0.3975 0.3978 0.5839 -0.0437 0.0125  0.0285  42  ARG A CB  
251  C CG  . ARG A 40  ? 0.5019 0.5076 0.6923 -0.0440 0.0240  0.0259  42  ARG A CG  
252  C CD  . ARG A 40  ? 0.6369 0.6458 0.8443 -0.0473 0.0291  0.0295  42  ARG A CD  
253  N NE  . ARG A 40  ? 0.7752 0.7898 0.9883 -0.0477 0.0414  0.0266  42  ARG A NE  
254  C CZ  . ARG A 40  ? 0.8978 0.9176 1.1312 -0.0494 0.0481  0.0285  42  ARG A CZ  
255  N NH1 . ARG A 40  ? 0.9221 0.9426 1.1737 -0.0513 0.0427  0.0339  42  ARG A NH1 
256  N NH2 . ARG A 40  ? 0.9361 0.9603 1.1721 -0.0493 0.0602  0.0246  42  ARG A NH2 
257  N N   . TRP A 41  ? 0.3295 0.3318 0.4915 -0.0368 0.0159  0.0191  43  TRP A N   
258  C CA  . TRP A 41  ? 0.3384 0.3408 0.4862 -0.0346 0.0179  0.0152  43  TRP A CA  
259  C C   . TRP A 41  ? 0.3465 0.3524 0.4937 -0.0360 0.0269  0.0116  43  TRP A C   
260  O O   . TRP A 41  ? 0.3558 0.3653 0.5168 -0.0376 0.0329  0.0110  43  TRP A O   
261  C CB  . TRP A 41  ? 0.3190 0.3235 0.4700 -0.0321 0.0159  0.0139  43  TRP A CB  
262  C CG  . TRP A 41  ? 0.3232 0.3244 0.4702 -0.0305 0.0075  0.0170  43  TRP A CG  
263  C CD1 . TRP A 41  ? 0.3210 0.3223 0.4783 -0.0311 0.0028  0.0206  43  TRP A CD1 
264  C CD2 . TRP A 41  ? 0.3057 0.3030 0.4370 -0.0279 0.0029  0.0165  43  TRP A CD2 
265  N NE1 . TRP A 41  ? 0.3334 0.3309 0.4802 -0.0293 -0.0044 0.0219  43  TRP A NE1 
266  C CE2 . TRP A 41  ? 0.3109 0.3056 0.4420 -0.0271 -0.0038 0.0193  43  TRP A CE2 
267  C CE3 . TRP A 41  ? 0.2958 0.2917 0.4138 -0.0261 0.0038  0.0142  43  TRP A CE3 
268  C CZ2 . TRP A 41  ? 0.3302 0.3209 0.4477 -0.0244 -0.0085 0.0189  43  TRP A CZ2 
269  C CZ3 . TRP A 41  ? 0.3057 0.2980 0.4127 -0.0232 -0.0009 0.0144  43  TRP A CZ3 
270  C CH2 . TRP A 41  ? 0.3208 0.3103 0.4270 -0.0223 -0.0064 0.0164  43  TRP A CH2 
271  N N   . ALA A 42  ? 0.3094 0.3145 0.4411 -0.0353 0.0279  0.0091  44  ALA A N   
272  C CA  . ALA A 42  ? 0.3146 0.3227 0.4410 -0.0367 0.0352  0.0052  44  ALA A CA  
273  C C   . ALA A 42  ? 0.3064 0.3161 0.4258 -0.0349 0.0347  0.0003  44  ALA A C   
274  O O   . ALA A 42  ? 0.3219 0.3296 0.4321 -0.0328 0.0286  0.0014  44  ALA A O   
275  C CB  . ALA A 42  ? 0.3130 0.3188 0.4263 -0.0382 0.0357  0.0080  44  ALA A CB  
276  N N   . LEU A 43  ? 0.2984 0.3117 0.4231 -0.0357 0.0409  -0.0053 45  LEU A N   
277  C CA  . LEU A 43  ? 0.3081 0.3232 0.4276 -0.0349 0.0408  -0.0108 45  LEU A CA  
278  C C   . LEU A 43  ? 0.3264 0.3423 0.4301 -0.0366 0.0437  -0.0143 45  LEU A C   
279  O O   . LEU A 43  ? 0.3246 0.3418 0.4278 -0.0387 0.0507  -0.0163 45  LEU A O   
280  C CB  . LEU A 43  ? 0.3159 0.3334 0.4510 -0.0349 0.0455  -0.0158 45  LEU A CB  
281  C CG  . LEU A 43  ? 0.3418 0.3609 0.4740 -0.0347 0.0454  -0.0222 45  LEU A CG  
282  C CD1 . LEU A 43  ? 0.3567 0.3753 0.4866 -0.0324 0.0379  -0.0190 45  LEU A CD1 
283  C CD2 . LEU A 43  ? 0.4017 0.4222 0.5503 -0.0351 0.0509  -0.0275 45  LEU A CD2 
284  N N   . TRP A 44  ? 0.3244 0.3402 0.4160 -0.0357 0.0386  -0.0147 46  TRP A N   
285  C CA  . TRP A 44  ? 0.3287 0.3456 0.4036 -0.0372 0.0389  -0.0170 46  TRP A CA  
286  C C   . TRP A 44  ? 0.3493 0.3688 0.4222 -0.0373 0.0375  -0.0237 46  TRP A C   
287  O O   . TRP A 44  ? 0.3362 0.3563 0.4189 -0.0354 0.0341  -0.0244 46  TRP A O   
288  C CB  . TRP A 44  ? 0.3351 0.3496 0.3982 -0.0359 0.0322  -0.0104 46  TRP A CB  
289  C CG  . TRP A 44  ? 0.3566 0.3674 0.4212 -0.0359 0.0317  -0.0035 46  TRP A CG  
290  C CD1 . TRP A 44  ? 0.3435 0.3512 0.4182 -0.0343 0.0287  0.0002  46  TRP A CD1 
291  C CD2 . TRP A 44  ? 0.3906 0.4003 0.4463 -0.0380 0.0341  0.0006  46  TRP A CD2 
292  N NE1 . TRP A 44  ? 0.3641 0.3685 0.4377 -0.0354 0.0287  0.0057  46  TRP A NE1 
293  C CE2 . TRP A 44  ? 0.3819 0.3875 0.4449 -0.0377 0.0323  0.0065  46  TRP A CE2 
294  C CE3 . TRP A 44  ? 0.4299 0.4416 0.4716 -0.0403 0.0375  0.0001  46  TRP A CE3 
295  C CZ2 . TRP A 44  ? 0.4145 0.4178 0.4732 -0.0396 0.0339  0.0124  46  TRP A CZ2 
296  C CZ3 . TRP A 44  ? 0.4818 0.4916 0.5179 -0.0421 0.0396  0.0066  46  TRP A CZ3 
297  C CH2 . TRP A 44  ? 0.4642 0.4699 0.5101 -0.0418 0.0379  0.0127  46  TRP A CH2 
298  N N   . PHE A 45  ? 0.3538 0.3751 0.4136 -0.0396 0.0396  -0.0284 47  PHE A N   
299  C CA  . PHE A 45  ? 0.3978 0.4215 0.4547 -0.0405 0.0377  -0.0359 47  PHE A CA  
300  C C   . PHE A 45  ? 0.4362 0.4614 0.4729 -0.0419 0.0333  -0.0349 47  PHE A C   
301  O O   . PHE A 45  ? 0.4569 0.4817 0.4810 -0.0436 0.0366  -0.0327 47  PHE A O   
302  C CB  . PHE A 45  ? 0.4260 0.4505 0.4891 -0.0426 0.0457  -0.0452 47  PHE A CB  
303  C CG  . PHE A 45  ? 0.4795 0.5057 0.5377 -0.0444 0.0441  -0.0545 47  PHE A CG  
304  C CD1 . PHE A 45  ? 0.4946 0.5216 0.5647 -0.0435 0.0391  -0.0566 47  PHE A CD1 
305  C CD2 . PHE A 45  ? 0.5359 0.5630 0.5779 -0.0474 0.0475  -0.0613 47  PHE A CD2 
306  C CE1 . PHE A 45  ? 0.5164 0.5448 0.5841 -0.0457 0.0370  -0.0655 47  PHE A CE1 
307  C CE2 . PHE A 45  ? 0.5626 0.5909 0.6000 -0.0495 0.0452  -0.0708 47  PHE A CE2 
308  C CZ  . PHE A 45  ? 0.5484 0.5773 0.5993 -0.0488 0.0394  -0.0729 47  PHE A CZ  
309  N N   . PHE A 46  ? 0.4395 0.4666 0.4738 -0.0414 0.0262  -0.0359 48  PHE A N   
310  C CA  . PHE A 46  ? 0.5154 0.5446 0.5324 -0.0428 0.0207  -0.0352 48  PHE A CA  
311  C C   . PHE A 46  ? 0.5777 0.6098 0.5933 -0.0452 0.0190  -0.0451 48  PHE A C   
312  O O   . PHE A 46  ? 0.5641 0.5974 0.5935 -0.0442 0.0159  -0.0476 48  PHE A O   
313  C CB  . PHE A 46  ? 0.5414 0.5706 0.5586 -0.0399 0.0127  -0.0268 48  PHE A CB  
314  C CG  . PHE A 46  ? 0.6043 0.6357 0.6054 -0.0408 0.0060  -0.0237 48  PHE A CG  
315  C CD1 . PHE A 46  ? 0.6368 0.6664 0.6258 -0.0409 0.0057  -0.0161 48  PHE A CD1 
316  C CD2 . PHE A 46  ? 0.6429 0.6786 0.6425 -0.0418 -0.0006 -0.0277 48  PHE A CD2 
317  C CE1 . PHE A 46  ? 0.6676 0.6994 0.6425 -0.0416 -0.0012 -0.0118 48  PHE A CE1 
318  C CE2 . PHE A 46  ? 0.6641 0.7025 0.6498 -0.0427 -0.0080 -0.0240 48  PHE A CE2 
319  C CZ  . PHE A 46  ? 0.6648 0.7012 0.6379 -0.0424 -0.0084 -0.0158 48  PHE A CZ  
320  N N   . LYS A 47  ? 0.6378 0.6710 0.6369 -0.0487 0.0213  -0.0509 49  LYS A N   
321  C CA  . LYS A 47  ? 0.6991 0.7345 0.6941 -0.0517 0.0193  -0.0618 49  LYS A CA  
322  C C   . LYS A 47  ? 0.7645 0.8035 0.7471 -0.0527 0.0083  -0.0593 49  LYS A C   
323  O O   . LYS A 47  ? 0.7729 0.8126 0.7417 -0.0523 0.0047  -0.0508 49  LYS A O   
324  C CB  . LYS A 47  ? 0.7590 0.7935 0.7405 -0.0549 0.0279  -0.0703 49  LYS A CB  
325  C CG  . LYS A 47  ? 0.8371 0.8727 0.8120 -0.0584 0.0261  -0.0835 49  LYS A CG  
326  C CD  . LYS A 47  ? 0.9190 0.9530 0.9172 -0.0581 0.0278  -0.0918 49  LYS A CD  
327  C CE  . LYS A 47  ? 0.9858 1.0171 0.9836 -0.0602 0.0377  -0.1048 49  LYS A CE  
328  N NZ  . LYS A 47  ? 0.9942 1.0264 0.9693 -0.0644 0.0356  -0.1153 49  LYS A NZ  
329  N N   . ASN A 48  ? 0.8080 0.8493 0.7976 -0.0541 0.0027  -0.0663 50  ASN A N   
330  C CA  . ASN A 48  ? 0.8580 0.9036 0.8369 -0.0562 -0.0081 -0.0671 50  ASN A CA  
331  C C   . ASN A 48  ? 0.8924 0.9384 0.8486 -0.0610 -0.0070 -0.0763 50  ASN A C   
332  O O   . ASN A 48  ? 0.8931 0.9388 0.8513 -0.0639 -0.0063 -0.0885 50  ASN A O   
333  C CB  . ASN A 48  ? 0.8893 0.9374 0.8876 -0.0563 -0.0140 -0.0714 50  ASN A CB  
334  C CG  . ASN A 48  ? 0.9573 1.0108 0.9496 -0.0582 -0.0264 -0.0706 50  ASN A CG  
335  O OD1 . ASN A 48  ? 0.9849 1.0410 0.9712 -0.0562 -0.0326 -0.0606 50  ASN A OD1 
336  N ND2 . ASN A 48  ? 0.9766 1.0318 0.9719 -0.0620 -0.0307 -0.0811 50  ASN A ND2 
337  N N   . ASP A 49  ? 0.9163 0.9626 0.8511 -0.0616 -0.0063 -0.0704 51  ASP A N   
338  C CA  . ASP A 49  ? 0.9379 0.9854 0.8466 -0.0660 -0.0059 -0.0770 51  ASP A CA  
339  C C   . ASP A 49  ? 0.9513 1.0019 0.8421 -0.0661 -0.0144 -0.0652 51  ASP A C   
340  O O   . ASP A 49  ? 0.9615 1.0110 0.8410 -0.0653 -0.0095 -0.0569 51  ASP A O   
341  C CB  . ASP A 49  ? 0.9634 1.0073 0.8649 -0.0667 0.0086  -0.0818 51  ASP A CB  
342  C CG  . ASP A 49  ? 1.0258 1.0704 0.8997 -0.0711 0.0115  -0.0904 51  ASP A CG  
343  O OD1 . ASP A 49  ? 1.0334 1.0815 0.8898 -0.0739 0.0010  -0.0911 51  ASP A OD1 
344  O OD2 . ASP A 49  ? 1.0488 1.0909 0.9185 -0.0716 0.0243  -0.0966 51  ASP A OD2 
345  N N   . LYS A 50  ? 0.9491 1.0042 0.8398 -0.0670 -0.0276 -0.0639 52  LYS A N   
346  C CA  . LYS A 50  ? 0.9586 1.0172 0.8385 -0.0663 -0.0377 -0.0513 52  LYS A CA  
347  C C   . LYS A 50  ? 0.9606 1.0205 0.8082 -0.0699 -0.0379 -0.0496 52  LYS A C   
348  O O   . LYS A 50  ? 0.9627 1.0244 0.8006 -0.0690 -0.0438 -0.0369 52  LYS A O   
349  C CB  . LYS A 50  ? 0.9832 1.0472 0.8736 -0.0665 -0.0520 -0.0510 52  LYS A CB  
350  C CG  . LYS A 50  ? 1.0260 1.0909 0.9403 -0.0612 -0.0561 -0.0405 52  LYS A CG  
351  C CD  . LYS A 50  ? 1.0816 1.1461 0.9875 -0.0584 -0.0586 -0.0254 52  LYS A CD  
352  C CE  . LYS A 50  ? 1.1086 1.1773 1.0281 -0.0550 -0.0696 -0.0157 52  LYS A CE  
353  N NZ  . LYS A 50  ? 1.1246 1.1916 1.0707 -0.0501 -0.0660 -0.0141 52  LYS A NZ  
354  N N   . SER A 51  ? 0.9575 1.0162 0.7889 -0.0739 -0.0309 -0.0623 53  SER A N   
355  C CA  . SER A 51  ? 0.9555 1.0148 0.7548 -0.0773 -0.0271 -0.0618 53  SER A CA  
356  C C   . SER A 51  ? 0.9510 1.0076 0.7474 -0.0749 -0.0166 -0.0502 53  SER A C   
357  O O   . SER A 51  ? 0.9653 1.0235 0.7381 -0.0767 -0.0164 -0.0426 53  SER A O   
358  C CB  . SER A 51  ? 0.9626 1.0204 0.7489 -0.0813 -0.0196 -0.0796 53  SER A CB  
359  O OG  . SER A 51  ? 0.9665 1.0196 0.7637 -0.0796 -0.0035 -0.0853 53  SER A OG  
360  N N   . LYS A 52  ? 0.9317 0.9844 0.7523 -0.0711 -0.0083 -0.0483 54  LYS A N   
361  C CA  . LYS A 52  ? 0.9094 0.9593 0.7324 -0.0688 0.0001  -0.0369 54  LYS A CA  
362  C C   . LYS A 52  ? 0.8798 0.9292 0.7180 -0.0649 -0.0082 -0.0232 54  LYS A C   
363  O O   . LYS A 52  ? 0.8810 0.9317 0.7345 -0.0630 -0.0172 -0.0242 54  LYS A O   
364  C CB  . LYS A 52  ? 0.9316 0.9776 0.7710 -0.0675 0.0141  -0.0438 54  LYS A CB  
365  C CG  . LYS A 52  ? 1.0090 1.0550 0.8362 -0.0708 0.0235  -0.0587 54  LYS A CG  
366  C CD  . LYS A 52  ? 1.0805 1.1230 0.9273 -0.0690 0.0371  -0.0645 54  LYS A CD  
367  C CE  . LYS A 52  ? 1.1471 1.1893 0.9814 -0.0718 0.0484  -0.0784 54  LYS A CE  
368  N NZ  . LYS A 52  ? 1.1871 1.2266 1.0408 -0.0699 0.0625  -0.0816 54  LYS A NZ  
369  N N   . THR A 53  ? 0.8568 0.9042 0.6915 -0.0636 -0.0052 -0.0104 55  THR A N   
370  C CA  . THR A 53  ? 0.8449 0.8901 0.6968 -0.0594 -0.0111 0.0014  55  THR A CA  
371  C C   . THR A 53  ? 0.8296 0.8712 0.7081 -0.0560 -0.0061 -0.0031 55  THR A C   
372  O O   . THR A 53  ? 0.8252 0.8654 0.7081 -0.0570 0.0038  -0.0119 55  THR A O   
373  C CB  . THR A 53  ? 0.8524 0.8950 0.6971 -0.0591 -0.0078 0.0153  55  THR A CB  
374  O OG1 . THR A 53  ? 0.8682 0.9081 0.7147 -0.0600 0.0059  0.0126  55  THR A OG1 
375  C CG2 . THR A 53  ? 0.8672 0.9134 0.6857 -0.0621 -0.0131 0.0228  55  THR A CG2 
376  N N   . TRP A 54  ? 0.8125 0.8525 0.7082 -0.0519 -0.0127 0.0031  56  TRP A N   
377  C CA  . TRP A 54  ? 0.7919 0.8286 0.7105 -0.0487 -0.0086 0.0001  56  TRP A CA  
378  C C   . TRP A 54  ? 0.7432 0.7752 0.6656 -0.0486 0.0022  0.0028  56  TRP A C   
379  O O   . TRP A 54  ? 0.7291 0.7594 0.6654 -0.0479 0.0085  -0.0031 56  TRP A O   
380  C CB  . TRP A 54  ? 0.8041 0.8400 0.7379 -0.0442 -0.0170 0.0066  56  TRP A CB  
381  C CG  . TRP A 54  ? 0.8247 0.8564 0.7593 -0.0416 -0.0187 0.0189  56  TRP A CG  
382  C CD1 . TRP A 54  ? 0.8447 0.8773 0.7724 -0.0407 -0.0270 0.0284  56  TRP A CD1 
383  C CD2 . TRP A 54  ? 0.8291 0.8547 0.7737 -0.0397 -0.0128 0.0230  56  TRP A CD2 
384  N NE1 . TRP A 54  ? 0.8528 0.8796 0.7859 -0.0383 -0.0260 0.0378  56  TRP A NE1 
385  C CE2 . TRP A 54  ? 0.8458 0.8681 0.7889 -0.0378 -0.0176 0.0343  56  TRP A CE2 
386  C CE3 . TRP A 54  ? 0.8329 0.8553 0.7887 -0.0394 -0.0047 0.0183  56  TRP A CE3 
387  C CZ2 . TRP A 54  ? 0.8564 0.8720 0.8078 -0.0361 -0.0142 0.0402  56  TRP A CZ2 
388  C CZ3 . TRP A 54  ? 0.8458 0.8624 0.8090 -0.0379 -0.0019 0.0245  56  TRP A CZ3 
389  C CH2 . TRP A 54  ? 0.8530 0.8660 0.8142 -0.0363 -0.0067 0.0348  56  TRP A CH2 
390  N N   . GLN A 55  ? 0.7141 0.7445 0.6254 -0.0497 0.0040  0.0123  57  GLN A N   
391  C CA  . GLN A 55  ? 0.6870 0.7136 0.6029 -0.0502 0.0139  0.0158  57  GLN A CA  
392  C C   . GLN A 55  ? 0.6343 0.6626 0.5474 -0.0531 0.0255  0.0062  57  GLN A C   
393  O O   . GLN A 55  ? 0.6087 0.6348 0.5358 -0.0525 0.0331  0.0047  57  GLN A O   
394  C CB  . GLN A 55  ? 0.7309 0.7561 0.6350 -0.0513 0.0133  0.0284  57  GLN A CB  
395  C CG  . GLN A 55  ? 0.8191 0.8405 0.7318 -0.0478 0.0040  0.0388  57  GLN A CG  
396  C CD  . GLN A 55  ? 0.9294 0.9540 0.8313 -0.0473 -0.0068 0.0431  57  GLN A CD  
397  O OE1 . GLN A 55  ? 0.9512 0.9812 0.8429 -0.0490 -0.0101 0.0364  57  GLN A OE1 
398  N NE2 . GLN A 55  ? 0.9676 0.9889 0.8730 -0.0450 -0.0131 0.0545  57  GLN A NE2 
399  N N   . ALA A 56  ? 0.6181 0.6504 0.5138 -0.0560 0.0264  -0.0001 58  ALA A N   
400  C CA  . ALA A 56  ? 0.6022 0.6361 0.4944 -0.0584 0.0368  -0.0114 58  ALA A CA  
401  C C   . ALA A 56  ? 0.5759 0.6094 0.4861 -0.0569 0.0369  -0.0226 58  ALA A C   
402  O O   . ALA A 56  ? 0.5696 0.6026 0.4879 -0.0574 0.0465  -0.0301 58  ALA A O   
403  C CB  . ALA A 56  ? 0.6056 0.6433 0.4712 -0.0620 0.0361  -0.0158 58  ALA A CB  
404  N N   . ASN A 57  ? 0.5604 0.5943 0.4780 -0.0550 0.0264  -0.0230 59  ASN A N   
405  C CA  . ASN A 57  ? 0.5613 0.5951 0.4971 -0.0535 0.0255  -0.0317 59  ASN A CA  
406  C C   . ASN A 57  ? 0.5331 0.5635 0.4927 -0.0501 0.0280  -0.0285 59  ASN A C   
407  O O   . ASN A 57  ? 0.5360 0.5664 0.5105 -0.0492 0.0291  -0.0354 59  ASN A O   
408  C CB  . ASN A 57  ? 0.5830 0.6194 0.5181 -0.0531 0.0139  -0.0331 59  ASN A CB  
409  C CG  . ASN A 57  ? 0.6468 0.6868 0.5634 -0.0570 0.0105  -0.0408 59  ASN A CG  
410  O OD1 . ASN A 57  ? 0.6820 0.7220 0.5926 -0.0596 0.0175  -0.0515 59  ASN A OD1 
411  N ND2 . ASN A 57  ? 0.6621 0.7051 0.5698 -0.0572 -0.0006 -0.0361 59  ASN A ND2 
412  N N   . LEU A 58  ? 0.5247 0.5524 0.4875 -0.0485 0.0287  -0.0185 60  LEU A N   
413  C CA  . LEU A 58  ? 0.5063 0.5306 0.4886 -0.0460 0.0310  -0.0155 60  LEU A CA  
414  C C   . LEU A 58  ? 0.4959 0.5196 0.4830 -0.0475 0.0418  -0.0173 60  LEU A C   
415  O O   . LEU A 58  ? 0.5215 0.5451 0.4984 -0.0493 0.0462  -0.0124 60  LEU A O   
416  C CB  . LEU A 58  ? 0.5142 0.5352 0.4978 -0.0436 0.0250  -0.0045 60  LEU A CB  
417  C CG  . LEU A 58  ? 0.5354 0.5524 0.5369 -0.0411 0.0262  -0.0014 60  LEU A CG  
418  C CD1 . LEU A 58  ? 0.5179 0.5355 0.5333 -0.0388 0.0237  -0.0065 60  LEU A CD1 
419  C CD2 . LEU A 58  ? 0.5571 0.5697 0.5576 -0.0393 0.0210  0.0085  60  LEU A CD2 
420  N N   . ARG A 59  ? 0.4691 0.4925 0.4730 -0.0467 0.0462  -0.0233 61  ARG A N   
421  C CA  A ARG A 59  ? 0.4739 0.4974 0.4865 -0.0479 0.0568  -0.0257 61  ARG A CA  
422  C CA  B ARG A 59  ? 0.4743 0.4978 0.4870 -0.0479 0.0570  -0.0260 61  ARG A CA  
423  C C   . ARG A 59  ? 0.4657 0.4870 0.5002 -0.0456 0.0567  -0.0224 61  ARG A C   
424  O O   . ARG A 59  ? 0.4440 0.4647 0.4891 -0.0435 0.0514  -0.0238 61  ARG A O   
425  C CB  A ARG A 59  ? 0.5118 0.5375 0.5245 -0.0493 0.0630  -0.0380 61  ARG A CB  
426  C CB  B ARG A 59  ? 0.5113 0.5370 0.5243 -0.0493 0.0631  -0.0384 61  ARG A CB  
427  C CG  A ARG A 59  ? 0.6109 0.6386 0.6077 -0.0523 0.0724  -0.0425 61  ARG A CG  
428  C CG  B ARG A 59  ? 0.6037 0.6304 0.6197 -0.0509 0.0761  -0.0430 61  ARG A CG  
429  C CD  A ARG A 59  ? 0.6694 0.6977 0.6744 -0.0528 0.0799  -0.0553 61  ARG A CD  
430  C CD  B ARG A 59  ? 0.6756 0.7027 0.7023 -0.0509 0.0811  -0.0554 61  ARG A CD  
431  N NE  A ARG A 59  ? 0.7121 0.7405 0.7333 -0.0525 0.0918  -0.0583 61  ARG A NE  
432  N NE  B ARG A 59  ? 0.7158 0.7443 0.7331 -0.0531 0.0921  -0.0646 61  ARG A NE  
433  C CZ  A ARG A 59  ? 0.7327 0.7608 0.7710 -0.0513 0.0955  -0.0511 61  ARG A CZ  
434  C CZ  B ARG A 59  ? 0.7184 0.7479 0.7131 -0.0555 0.0920  -0.0717 61  ARG A CZ  
435  N NH1 A ARG A 59  ? 0.7479 0.7771 0.8015 -0.0510 0.1064  -0.0552 61  ARG A NH1 
436  N NH1 B ARG A 59  ? 0.7005 0.7308 0.6869 -0.0572 0.1031  -0.0808 61  ARG A NH1 
437  N NH2 A ARG A 59  ? 0.7272 0.7541 0.7684 -0.0503 0.0883  -0.0400 61  ARG A NH2 
438  N NH2 B ARG A 59  ? 0.7098 0.7397 0.6900 -0.0561 0.0808  -0.0697 61  ARG A NH2 
439  N N   . LEU A 60  ? 0.4689 0.4894 0.5105 -0.0463 0.0620  -0.0173 62  LEU A N   
440  C CA  . LEU A 60  ? 0.4928 0.5120 0.5557 -0.0449 0.0627  -0.0150 62  LEU A CA  
441  C C   . LEU A 60  ? 0.5007 0.5223 0.5770 -0.0451 0.0707  -0.0230 62  LEU A C   
442  O O   . LEU A 60  ? 0.5181 0.5418 0.5918 -0.0470 0.0801  -0.0261 62  LEU A O   
443  C CB  . LEU A 60  ? 0.5207 0.5386 0.5879 -0.0460 0.0649  -0.0067 62  LEU A CB  
444  C CG  . LEU A 60  ? 0.5377 0.5553 0.6282 -0.0453 0.0664  -0.0047 62  LEU A CG  
445  C CD1 . LEU A 60  ? 0.5070 0.5214 0.6035 -0.0429 0.0566  -0.0018 62  LEU A CD1 
446  C CD2 . LEU A 60  ? 0.5709 0.5886 0.6670 -0.0474 0.0710  0.0019  62  LEU A CD2 
447  N N   . ILE A 61  ? 0.4699 0.4912 0.5609 -0.0432 0.0678  -0.0260 63  ILE A N   
448  C CA  . ILE A 61  ? 0.4811 0.5040 0.5883 -0.0431 0.0749  -0.0330 63  ILE A CA  
449  C C   . ILE A 61  ? 0.4800 0.5035 0.6070 -0.0428 0.0793  -0.0283 63  ILE A C   
450  O O   . ILE A 61  ? 0.4835 0.5092 0.6179 -0.0438 0.0893  -0.0317 63  ILE A O   
451  C CB  . ILE A 61  ? 0.4817 0.5041 0.5978 -0.0414 0.0697  -0.0370 63  ILE A CB  
452  C CG1 . ILE A 61  ? 0.4916 0.5141 0.5905 -0.0420 0.0650  -0.0415 63  ILE A CG1 
453  C CG2 . ILE A 61  ? 0.4962 0.5194 0.6318 -0.0410 0.0769  -0.0437 63  ILE A CG2 
454  C CD1 . ILE A 61  ? 0.5351 0.5589 0.6174 -0.0445 0.0709  -0.0488 63  ILE A CD1 
455  N N   . SER A 62  ? 0.4535 0.4754 0.5887 -0.0416 0.0719  -0.0205 64  SER A N   
456  C CA  . SER A 62  ? 0.4378 0.4606 0.5944 -0.0414 0.0736  -0.0162 64  SER A CA  
457  C C   . SER A 62  ? 0.4182 0.4384 0.5770 -0.0406 0.0641  -0.0078 64  SER A C   
458  O O   . SER A 62  ? 0.4023 0.4198 0.5492 -0.0395 0.0561  -0.0062 64  SER A O   
459  C CB  . SER A 62  ? 0.5033 0.5276 0.6793 -0.0399 0.0765  -0.0211 64  SER A CB  
460  O OG  . SER A 62  ? 0.5865 0.6126 0.7851 -0.0397 0.0788  -0.0168 64  SER A OG  
461  N N   . LYS A 63  ? 0.4163 0.4373 0.5910 -0.0414 0.0646  -0.0028 65  LYS A N   
462  C CA  . LYS A 63  ? 0.4201 0.4384 0.5989 -0.0411 0.0552  0.0045  65  LYS A CA  
463  C C   . LYS A 63  ? 0.4376 0.4581 0.6397 -0.0404 0.0539  0.0066  65  LYS A C   
464  O O   . LYS A 63  ? 0.4392 0.4636 0.6573 -0.0407 0.0620  0.0040  65  LYS A O   
465  C CB  . LYS A 63  ? 0.4586 0.4752 0.6331 -0.0434 0.0548  0.0101  65  LYS A CB  
466  C CG  . LYS A 63  ? 0.5164 0.5308 0.6683 -0.0440 0.0558  0.0095  65  LYS A CG  
467  C CD  . LYS A 63  ? 0.5545 0.5662 0.7038 -0.0462 0.0539  0.0163  65  LYS A CD  
468  C CE  . LYS A 63  ? 0.5806 0.5898 0.7088 -0.0467 0.0535  0.0177  65  LYS A CE  
469  N NZ  . LYS A 63  ? 0.5962 0.6018 0.7249 -0.0488 0.0510  0.0254  65  LYS A NZ  
470  N N   . PHE A 64  ? 0.3900 0.4082 0.5943 -0.0394 0.0439  0.0111  66  PHE A N   
471  C CA  . PHE A 64  ? 0.3701 0.3905 0.5947 -0.0388 0.0405  0.0145  66  PHE A CA  
472  C C   . PHE A 64  ? 0.3763 0.3933 0.5978 -0.0390 0.0293  0.0202  66  PHE A C   
473  O O   . PHE A 64  ? 0.3569 0.3694 0.5599 -0.0385 0.0241  0.0203  66  PHE A O   
474  C CB  . PHE A 64  ? 0.3532 0.3754 0.5853 -0.0366 0.0419  0.0113  66  PHE A CB  
475  C CG  . PHE A 64  ? 0.3229 0.3422 0.5378 -0.0347 0.0360  0.0101  66  PHE A CG  
476  C CD1 . PHE A 64  ? 0.3228 0.3405 0.5362 -0.0334 0.0268  0.0151  66  PHE A CD1 
477  C CD2 . PHE A 64  ? 0.3415 0.3599 0.5407 -0.0343 0.0395  0.0045  66  PHE A CD2 
478  C CE1 . PHE A 64  ? 0.3466 0.3620 0.5441 -0.0315 0.0226  0.0143  66  PHE A CE1 
479  C CE2 . PHE A 64  ? 0.3457 0.3622 0.5315 -0.0326 0.0343  0.0041  66  PHE A CE2 
480  C CZ  . PHE A 64  ? 0.3270 0.3422 0.5125 -0.0310 0.0265  0.0090  66  PHE A CZ  
481  N N   . ASP A 65  ? 0.3697 0.3889 0.6100 -0.0396 0.0252  0.0250  67  ASP A N   
482  C CA  . ASP A 65  ? 0.3856 0.4018 0.6237 -0.0401 0.0136  0.0300  67  ASP A CA  
483  C C   . ASP A 65  ? 0.3595 0.3788 0.6147 -0.0395 0.0079  0.0345  67  ASP A C   
484  O O   . ASP A 65  ? 0.3733 0.3913 0.6310 -0.0408 -0.0016 0.0390  67  ASP A O   
485  C CB  . ASP A 65  ? 0.4232 0.4374 0.6627 -0.0432 0.0117  0.0327  67  ASP A CB  
486  C CG  . ASP A 65  ? 0.4562 0.4760 0.7198 -0.0454 0.0183  0.0350  67  ASP A CG  
487  O OD1 . ASP A 65  ? 0.4571 0.4820 0.7384 -0.0444 0.0220  0.0352  67  ASP A OD1 
488  O OD2 . ASP A 65  ? 0.5041 0.5233 0.7697 -0.0481 0.0203  0.0368  67  ASP A OD2 
489  N N   . THR A 66  ? 0.3375 0.3605 0.6037 -0.0377 0.0126  0.0334  68  THR A N   
490  C CA  . THR A 66  ? 0.3441 0.3698 0.6243 -0.0366 0.0070  0.0383  68  THR A CA  
491  C C   . THR A 66  ? 0.3416 0.3674 0.6170 -0.0338 0.0097  0.0360  68  THR A C   
492  O O   . THR A 66  ? 0.3539 0.3791 0.6224 -0.0331 0.0177  0.0296  68  THR A O   
493  C CB  . THR A 66  ? 0.3691 0.4005 0.6800 -0.0374 0.0105  0.0416  68  THR A CB  
494  O OG1 . THR A 66  ? 0.3862 0.4200 0.7071 -0.0361 0.0221  0.0365  68  THR A OG1 
495  C CG2 . THR A 66  ? 0.3680 0.4005 0.6882 -0.0404 0.0096  0.0441  68  THR A CG2 
496  N N   . VAL A 67  ? 0.3307 0.3575 0.6105 -0.0326 0.0030  0.0413  69  VAL A N   
497  C CA  . VAL A 67  ? 0.3580 0.3853 0.6375 -0.0302 0.0048  0.0411  69  VAL A CA  
498  C C   . VAL A 67  ? 0.3571 0.3872 0.6559 -0.0297 0.0147  0.0373  69  VAL A C   
499  O O   . VAL A 67  ? 0.3313 0.3605 0.6248 -0.0286 0.0203  0.0319  69  VAL A O   
500  C CB  . VAL A 67  ? 0.3507 0.3794 0.6343 -0.0294 -0.0044 0.0497  69  VAL A CB  
501  C CG1 . VAL A 67  ? 0.3639 0.3935 0.6488 -0.0272 -0.0017 0.0505  69  VAL A CG1 
502  C CG2 . VAL A 67  ? 0.3633 0.3887 0.6257 -0.0299 -0.0140 0.0521  69  VAL A CG2 
503  N N   . GLU A 68  ? 0.3325 0.3662 0.6562 -0.0304 0.0170  0.0398  70  GLU A N   
504  C CA  . GLU A 68  ? 0.3339 0.3697 0.6783 -0.0294 0.0269  0.0356  70  GLU A CA  
505  C C   . GLU A 68  ? 0.3296 0.3639 0.6641 -0.0301 0.0375  0.0253  70  GLU A C   
506  O O   . GLU A 68  ? 0.3432 0.3771 0.6829 -0.0290 0.0450  0.0190  70  GLU A O   
507  C CB  . GLU A 68  ? 0.3752 0.4155 0.7503 -0.0297 0.0272  0.0409  70  GLU A CB  
508  C CG  . GLU A 68  ? 0.3989 0.4413 0.7867 -0.0288 0.0169  0.0515  70  GLU A CG  
509  C CD  . GLU A 68  ? 0.4377 0.4795 0.8112 -0.0303 0.0040  0.0586  70  GLU A CD  
510  O OE1 . GLU A 68  ? 0.3856 0.4255 0.7437 -0.0322 0.0026  0.0558  70  GLU A OE1 
511  O OE2 . GLU A 68  ? 0.5069 0.5501 0.8846 -0.0297 -0.0049 0.0670  70  GLU A OE2 
512  N N   . ASP A 69  ? 0.3365 0.3698 0.6573 -0.0318 0.0379  0.0237  71  ASP A N   
513  C CA  . ASP A 69  ? 0.3365 0.3686 0.6446 -0.0327 0.0472  0.0151  71  ASP A CA  
514  C C   . ASP A 69  ? 0.3308 0.3594 0.6150 -0.0319 0.0459  0.0103  71  ASP A C   
515  O O   . ASP A 69  ? 0.3118 0.3400 0.5907 -0.0319 0.0535  0.0023  71  ASP A O   
516  C CB  . ASP A 69  ? 0.3657 0.3978 0.6670 -0.0349 0.0473  0.0167  71  ASP A CB  
517  C CG  . ASP A 69  ? 0.4420 0.4786 0.7698 -0.0359 0.0509  0.0203  71  ASP A CG  
518  O OD1 . ASP A 69  ? 0.4496 0.4892 0.7983 -0.0346 0.0584  0.0179  71  ASP A OD1 
519  O OD2 . ASP A 69  ? 0.4579 0.4950 0.7869 -0.0378 0.0461  0.0256  71  ASP A OD2 
520  N N   . PHE A 70  ? 0.3161 0.3428 0.5873 -0.0312 0.0365  0.0150  72  PHE A N   
521  C CA  . PHE A 70  ? 0.3013 0.3257 0.5546 -0.0301 0.0349  0.0118  72  PHE A CA  
522  C C   . PHE A 70  ? 0.3047 0.3303 0.5710 -0.0290 0.0397  0.0082  72  PHE A C   
523  O O   . PHE A 70  ? 0.3228 0.3476 0.5815 -0.0292 0.0447  0.0007  72  PHE A O   
524  C CB  . PHE A 70  ? 0.2929 0.3157 0.5347 -0.0289 0.0250  0.0182  72  PHE A CB  
525  C CG  . PHE A 70  ? 0.2757 0.2976 0.5061 -0.0273 0.0244  0.0161  72  PHE A CG  
526  C CD1 . PHE A 70  ? 0.3038 0.3241 0.5161 -0.0274 0.0261  0.0108  72  PHE A CD1 
527  C CD2 . PHE A 70  ? 0.2845 0.3080 0.5246 -0.0259 0.0225  0.0200  72  PHE A CD2 
528  C CE1 . PHE A 70  ? 0.2917 0.3122 0.4968 -0.0261 0.0256  0.0091  72  PHE A CE1 
529  C CE2 . PHE A 70  ? 0.2958 0.3193 0.5282 -0.0247 0.0226  0.0186  72  PHE A CE2 
530  C CZ  . PHE A 70  ? 0.2904 0.3126 0.5061 -0.0248 0.0243  0.0127  72  PHE A CZ  
531  N N   . TRP A 71  ? 0.2951 0.3225 0.5816 -0.0280 0.0375  0.0138  73  TRP A N   
532  C CA  . TRP A 71  ? 0.3264 0.3543 0.6279 -0.0270 0.0413  0.0115  73  TRP A CA  
533  C C   . TRP A 71  ? 0.3599 0.3877 0.6726 -0.0275 0.0519  0.0019  73  TRP A C   
534  O O   . TRP A 71  ? 0.3531 0.3796 0.6675 -0.0274 0.0555  -0.0043 73  TRP A O   
535  C CB  . TRP A 71  ? 0.3159 0.3456 0.6376 -0.0258 0.0366  0.0207  73  TRP A CB  
536  C CG  . TRP A 71  ? 0.3179 0.3474 0.6277 -0.0250 0.0277  0.0287  73  TRP A CG  
537  C CD1 . TRP A 71  ? 0.3481 0.3788 0.6577 -0.0248 0.0194  0.0379  73  TRP A CD1 
538  C CD2 . TRP A 71  ? 0.3254 0.3540 0.6235 -0.0241 0.0264  0.0284  73  TRP A CD2 
539  N NE1 . TRP A 71  ? 0.3628 0.3929 0.6574 -0.0238 0.0137  0.0427  73  TRP A NE1 
540  C CE2 . TRP A 71  ? 0.3440 0.3732 0.6331 -0.0232 0.0183  0.0375  73  TRP A CE2 
541  C CE3 . TRP A 71  ? 0.3296 0.3572 0.6229 -0.0242 0.0312  0.0211  73  TRP A CE3 
542  C CZ2 . TRP A 71  ? 0.3470 0.3761 0.6238 -0.0221 0.0162  0.0399  73  TRP A CZ2 
543  C CZ3 . TRP A 71  ? 0.3451 0.3728 0.6283 -0.0233 0.0282  0.0238  73  TRP A CZ3 
544  C CH2 . TRP A 71  ? 0.3374 0.3660 0.6131 -0.0221 0.0214  0.0333  73  TRP A CH2 
545  N N   . ALA A 72  ? 0.3916 0.4208 0.7116 -0.0283 0.0569  0.0003  74  ALA A N   
546  C CA  . ALA A 72  ? 0.3889 0.4181 0.7178 -0.0287 0.0683  -0.0093 74  ALA A CA  
547  C C   . ALA A 72  ? 0.4049 0.4320 0.7087 -0.0300 0.0718  -0.0186 74  ALA A C   
548  O O   . ALA A 72  ? 0.4171 0.4428 0.7226 -0.0302 0.0785  -0.0282 74  ALA A O   
549  C CB  . ALA A 72  ? 0.3966 0.4286 0.7375 -0.0292 0.0728  -0.0074 74  ALA A CB  
550  N N   . LEU A 73  ? 0.3748 0.4013 0.6556 -0.0310 0.0667  -0.0159 75  LEU A N   
551  C CA  . LEU A 73  ? 0.3806 0.4056 0.6374 -0.0322 0.0682  -0.0227 75  LEU A CA  
552  C C   . LEU A 73  ? 0.3675 0.3911 0.6190 -0.0316 0.0643  -0.0254 75  LEU A C   
553  O O   . LEU A 73  ? 0.3887 0.4114 0.6334 -0.0326 0.0683  -0.0343 75  LEU A O   
554  C CB  . LEU A 73  ? 0.3875 0.4119 0.6243 -0.0331 0.0630  -0.0177 75  LEU A CB  
555  C CG  . LEU A 73  ? 0.4288 0.4519 0.6406 -0.0341 0.0630  -0.0226 75  LEU A CG  
556  C CD1 . LEU A 73  ? 0.4641 0.4879 0.6715 -0.0357 0.0728  -0.0316 75  LEU A CD1 
557  C CD2 . LEU A 73  ? 0.4336 0.4556 0.6298 -0.0346 0.0577  -0.0164 75  LEU A CD2 
558  N N   . TYR A 74  ? 0.3346 0.3582 0.5888 -0.0303 0.0565  -0.0176 76  TYR A N   
559  C CA  . TYR A 74  ? 0.3303 0.3535 0.5819 -0.0296 0.0528  -0.0183 76  TYR A CA  
560  C C   . TYR A 74  ? 0.3467 0.3693 0.6161 -0.0299 0.0582  -0.0250 76  TYR A C   
561  O O   . TYR A 74  ? 0.3423 0.3639 0.6058 -0.0308 0.0592  -0.0320 76  TYR A O   
562  C CB  . TYR A 74  ? 0.3208 0.3446 0.5744 -0.0280 0.0450  -0.0078 76  TYR A CB  
563  C CG  . TYR A 74  ? 0.3198 0.3438 0.5709 -0.0273 0.0420  -0.0073 76  TYR A CG  
564  C CD1 . TYR A 74  ? 0.3405 0.3645 0.5717 -0.0271 0.0385  -0.0079 76  TYR A CD1 
565  C CD2 . TYR A 74  ? 0.3221 0.3466 0.5928 -0.0268 0.0430  -0.0058 76  TYR A CD2 
566  C CE1 . TYR A 74  ? 0.3577 0.3828 0.5889 -0.0265 0.0363  -0.0072 76  TYR A CE1 
567  C CE2 . TYR A 74  ? 0.3327 0.3578 0.6032 -0.0265 0.0408  -0.0047 76  TYR A CE2 
568  C CZ  . TYR A 74  ? 0.3581 0.3840 0.6090 -0.0263 0.0375  -0.0054 76  TYR A CZ  
569  O OH  . TYR A 74  ? 0.3868 0.4141 0.6395 -0.0260 0.0358  -0.0038 76  TYR A OH  
570  N N   . ASN A 75  ? 0.3850 0.4078 0.6776 -0.0291 0.0615  -0.0228 77  ASN A N   
571  C CA  . ASN A 75  ? 0.4365 0.4579 0.7500 -0.0290 0.0671  -0.0292 77  ASN A CA  
572  C C   . ASN A 75  ? 0.4714 0.4910 0.7785 -0.0306 0.0754  -0.0431 77  ASN A C   
573  O O   . ASN A 75  ? 0.4888 0.5061 0.8023 -0.0313 0.0779  -0.0512 77  ASN A O   
574  C CB  . ASN A 75  ? 0.4644 0.4868 0.8053 -0.0274 0.0688  -0.0229 77  ASN A CB  
575  C CG  . ASN A 75  ? 0.5475 0.5715 0.8955 -0.0261 0.0602  -0.0097 77  ASN A CG  
576  O OD1 . ASN A 75  ? 0.6173 0.6410 0.9576 -0.0260 0.0552  -0.0065 77  ASN A OD1 
577  N ND2 . ASN A 75  ? 0.5684 0.5944 0.9308 -0.0251 0.0581  -0.0013 77  ASN A ND2 
578  N N   . HIS A 76  ? 0.4899 0.5104 0.7844 -0.0313 0.0794  -0.0458 78  HIS A N   
579  C CA  . HIS A 76  ? 0.5321 0.5514 0.8166 -0.0329 0.0875  -0.0582 78  HIS A CA  
580  C C   . HIS A 76  ? 0.5394 0.5576 0.8001 -0.0348 0.0841  -0.0643 78  HIS A C   
581  O O   . HIS A 76  ? 0.5573 0.5734 0.8154 -0.0362 0.0884  -0.0759 78  HIS A O   
582  C CB  . HIS A 76  ? 0.5780 0.5992 0.8563 -0.0332 0.0930  -0.0570 78  HIS A CB  
583  C CG  . HIS A 76  ? 0.7099 0.7306 0.9718 -0.0350 0.1012  -0.0682 78  HIS A CG  
584  N ND1 . HIS A 76  ? 0.7702 0.7918 1.0046 -0.0367 0.0993  -0.0675 78  HIS A ND1 
585  C CD2 . HIS A 76  ? 0.7515 0.7706 1.0202 -0.0353 0.1112  -0.0800 78  HIS A CD2 
586  C CE1 . HIS A 76  ? 0.7899 0.8110 1.0140 -0.0382 0.1079  -0.0782 78  HIS A CE1 
587  N NE2 . HIS A 76  ? 0.7897 0.8092 1.0331 -0.0373 0.1156  -0.0866 78  HIS A NE2 
588  N N   . ILE A 77  ? 0.5265 0.5461 0.7706 -0.0349 0.0760  -0.0572 79  ILE A N   
589  C CA  . ILE A 77  ? 0.5305 0.5501 0.7504 -0.0366 0.0724  -0.0617 79  ILE A CA  
590  C C   . ILE A 77  ? 0.5271 0.5458 0.7505 -0.0372 0.0681  -0.0657 79  ILE A C   
591  O O   . ILE A 77  ? 0.5117 0.5301 0.7539 -0.0360 0.0661  -0.0616 79  ILE A O   
592  C CB  . ILE A 77  ? 0.5606 0.5817 0.7628 -0.0360 0.0657  -0.0521 79  ILE A CB  
593  C CG1 . ILE A 77  ? 0.5850 0.6064 0.7726 -0.0372 0.0707  -0.0536 79  ILE A CG1 
594  C CG2 . ILE A 77  ? 0.5893 0.6109 0.7771 -0.0362 0.0579  -0.0510 79  ILE A CG2 
595  C CD1 . ILE A 77  ? 0.6442 0.6661 0.8193 -0.0369 0.0664  -0.0460 79  ILE A CD1 
596  N N   . GLN A 78  ? 0.5358 0.5546 0.7406 -0.0394 0.0663  -0.0730 80  GLN A N   
597  C CA  . GLN A 78  ? 0.5645 0.5834 0.7705 -0.0406 0.0611  -0.0767 80  GLN A CA  
598  C C   . GLN A 78  ? 0.5626 0.5839 0.7676 -0.0389 0.0528  -0.0656 80  GLN A C   
599  O O   . GLN A 78  ? 0.5578 0.5805 0.7486 -0.0378 0.0496  -0.0588 80  GLN A O   
600  C CB  . GLN A 78  ? 0.6281 0.6471 0.8130 -0.0435 0.0603  -0.0868 80  GLN A CB  
601  C CG  . GLN A 78  ? 0.7407 0.7597 0.9298 -0.0454 0.0548  -0.0925 80  GLN A CG  
602  C CD  . GLN A 78  ? 0.8578 0.8735 1.0721 -0.0459 0.0586  -0.0988 80  GLN A CD  
603  O OE1 . GLN A 78  ? 0.8805 0.8962 1.1155 -0.0441 0.0575  -0.0912 80  GLN A OE1 
604  N NE2 . GLN A 78  ? 0.8890 0.9015 1.1021 -0.0483 0.0632  -0.1125 80  GLN A NE2 
605  N N   . LEU A 79  ? 0.5539 0.5756 0.7745 -0.0387 0.0499  -0.0641 81  LEU A N   
606  C CA  . LEU A 79  ? 0.5294 0.5538 0.7501 -0.0370 0.0435  -0.0543 81  LEU A CA  
607  C C   . LEU A 79  ? 0.5212 0.5481 0.7237 -0.0380 0.0378  -0.0557 81  LEU A C   
608  O O   . LEU A 79  ? 0.4983 0.5250 0.6937 -0.0407 0.0372  -0.0650 81  LEU A O   
609  C CB  . LEU A 79  ? 0.5333 0.5577 0.7769 -0.0370 0.0430  -0.0524 81  LEU A CB  
610  C CG  . LEU A 79  ? 0.5737 0.5968 0.8375 -0.0351 0.0461  -0.0455 81  LEU A CG  
611  C CD1 . LEU A 79  ? 0.5689 0.5913 0.8563 -0.0359 0.0464  -0.0457 81  LEU A CD1 
612  C CD2 . LEU A 79  ? 0.5983 0.6235 0.8558 -0.0323 0.0427  -0.0327 81  LEU A CD2 
613  N N   . SER A 80  ? 0.5201 0.5494 0.7159 -0.0356 0.0333  -0.0461 82  SER A N   
614  C CA  A SER A 80  ? 0.5240 0.5560 0.7046 -0.0356 0.0277  -0.0454 82  SER A CA  
615  C CA  B SER A 80  ? 0.5175 0.5494 0.6980 -0.0357 0.0278  -0.0457 82  SER A CA  
616  C C   . SER A 80  ? 0.5413 0.5757 0.7296 -0.0378 0.0245  -0.0505 82  SER A C   
617  O O   . SER A 80  ? 0.5626 0.5985 0.7391 -0.0398 0.0209  -0.0560 82  SER A O   
618  C CB  A SER A 80  ? 0.5315 0.5651 0.7082 -0.0321 0.0246  -0.0347 82  SER A CB  
619  C CB  B SER A 80  ? 0.5074 0.5407 0.6822 -0.0322 0.0248  -0.0351 82  SER A CB  
620  O OG  A SER A 80  ? 0.5394 0.5740 0.7328 -0.0307 0.0254  -0.0289 82  SER A OG  
621  O OG  B SER A 80  ? 0.4877 0.5183 0.6533 -0.0312 0.0268  -0.0323 82  SER A OG  
622  N N   . SER A 81  ? 0.5516 0.5867 0.7607 -0.0376 0.0252  -0.0480 83  SER A N   
623  C CA  . SER A 81  ? 0.5795 0.6165 0.8015 -0.0402 0.0226  -0.0529 83  SER A CA  
624  C C   . SER A 81  ? 0.6179 0.6526 0.8355 -0.0442 0.0226  -0.0664 83  SER A C   
625  O O   . SER A 81  ? 0.6295 0.6666 0.8468 -0.0468 0.0175  -0.0713 83  SER A O   
626  C CB  . SER A 81  ? 0.5729 0.6093 0.8198 -0.0398 0.0253  -0.0486 83  SER A CB  
627  O OG  . SER A 81  ? 0.5944 0.6260 0.8512 -0.0404 0.0308  -0.0530 83  SER A OG  
628  N N   . ASN A 82  ? 0.6293 0.6595 0.8435 -0.0448 0.0285  -0.0726 84  ASN A N   
629  C CA  . ASN A 82  ? 0.6591 0.6865 0.8665 -0.0483 0.0302  -0.0863 84  ASN A CA  
630  C C   . ASN A 82  ? 0.6891 0.7175 0.8686 -0.0493 0.0284  -0.0898 84  ASN A C   
631  O O   . ASN A 82  ? 0.6961 0.7224 0.8666 -0.0523 0.0300  -0.1014 84  ASN A O   
632  C CB  . ASN A 82  ? 0.6887 0.7111 0.9085 -0.0481 0.0387  -0.0915 84  ASN A CB  
633  C CG  . ASN A 82  ? 0.7571 0.7779 1.0057 -0.0478 0.0401  -0.0894 84  ASN A CG  
634  O OD1 . ASN A 82  ? 0.7959 0.8176 1.0561 -0.0498 0.0359  -0.0915 84  ASN A OD1 
635  N ND2 . ASN A 82  ? 0.7557 0.7743 1.0179 -0.0454 0.0456  -0.0846 84  ASN A ND2 
636  N N   . LEU A 83  ? 0.6927 0.7240 0.8581 -0.0469 0.0253  -0.0801 85  LEU A N   
637  C CA  . LEU A 83  ? 0.7115 0.7439 0.8517 -0.0480 0.0228  -0.0818 85  LEU A CA  
638  C C   . LEU A 83  ? 0.7255 0.7613 0.8586 -0.0507 0.0145  -0.0860 85  LEU A C   
639  O O   . LEU A 83  ? 0.7143 0.7536 0.8585 -0.0499 0.0091  -0.0812 85  LEU A O   
640  C CB  . LEU A 83  ? 0.7140 0.7480 0.8448 -0.0446 0.0208  -0.0701 85  LEU A CB  
641  C CG  . LEU A 83  ? 0.7270 0.7582 0.8553 -0.0425 0.0268  -0.0651 85  LEU A CG  
642  C CD1 . LEU A 83  ? 0.7172 0.7496 0.8350 -0.0396 0.0229  -0.0545 85  LEU A CD1 
643  C CD2 . LEU A 83  ? 0.7426 0.7715 0.8594 -0.0446 0.0330  -0.0723 85  LEU A CD2 
644  N N   . MET A 84  ? 0.7550 0.7905 0.8691 -0.0538 0.0133  -0.0943 86  MET A N   
645  C CA  . MET A 84  ? 0.7901 0.8296 0.8948 -0.0565 0.0036  -0.0972 86  MET A CA  
646  C C   . MET A 84  ? 0.7837 0.8277 0.8823 -0.0537 -0.0027 -0.0851 86  MET A C   
647  O O   . MET A 84  ? 0.7883 0.8313 0.8767 -0.0510 0.0002  -0.0779 86  MET A O   
648  C CB  . MET A 84  ? 0.8423 0.8809 0.9232 -0.0602 0.0034  -0.1069 86  MET A CB  
649  C CG  . MET A 84  ? 0.9227 0.9570 1.0083 -0.0637 0.0079  -0.1218 86  MET A CG  
650  S SD  . MET A 84  ? 1.1447 1.1794 1.2015 -0.0690 0.0034  -0.1345 86  MET A SD  
651  C CE  . MET A 84  ? 1.1526 1.1824 1.1940 -0.0683 0.0178  -0.1396 86  MET A CE  
652  N N   . PRO A 85  ? 0.7745 0.8233 0.8810 -0.0540 -0.0110 -0.0825 87  PRO A N   
653  C CA  . PRO A 85  ? 0.7579 0.8110 0.8583 -0.0511 -0.0169 -0.0717 87  PRO A CA  
654  C C   . PRO A 85  ? 0.7301 0.7827 0.8054 -0.0510 -0.0184 -0.0691 87  PRO A C   
655  O O   . PRO A 85  ? 0.7484 0.7999 0.8070 -0.0546 -0.0187 -0.0765 87  PRO A O   
656  C CB  . PRO A 85  ? 0.7728 0.8316 0.8824 -0.0532 -0.0263 -0.0733 87  PRO A CB  
657  C CG  . PRO A 85  ? 0.7835 0.8409 0.9141 -0.0553 -0.0234 -0.0800 87  PRO A CG  
658  C CD  . PRO A 85  ? 0.7647 0.8154 0.8884 -0.0571 -0.0153 -0.0890 87  PRO A CD  
659  N N   . GLY A 86  ? 0.6751 0.7282 0.7480 -0.0469 -0.0190 -0.0584 88  GLY A N   
660  C CA  . GLY A 86  ? 0.6419 0.6939 0.6943 -0.0463 -0.0198 -0.0535 88  GLY A CA  
661  C C   . GLY A 86  ? 0.5897 0.6363 0.6373 -0.0449 -0.0106 -0.0519 88  GLY A C   
662  O O   . GLY A 86  ? 0.6195 0.6646 0.6529 -0.0440 -0.0105 -0.0460 88  GLY A O   
663  N N   . CYS A 87  ? 0.5271 0.5705 0.5879 -0.0449 -0.0029 -0.0561 89  CYS A N   
664  C CA  . CYS A 87  ? 0.4966 0.5356 0.5564 -0.0434 0.0053  -0.0535 89  CYS A CA  
665  C C   . CYS A 87  ? 0.4341 0.4719 0.5044 -0.0389 0.0057  -0.0438 89  CYS A C   
666  O O   . CYS A 87  ? 0.4068 0.4467 0.4896 -0.0368 0.0027  -0.0409 89  CYS A O   
667  C CB  . CYS A 87  ? 0.5201 0.5566 0.5889 -0.0453 0.0128  -0.0623 89  CYS A CB  
668  S SG  . CYS A 87  ? 0.6245 0.6608 0.6771 -0.0503 0.0147  -0.0749 89  CYS A SG  
669  N N   . ASP A 88  ? 0.4119 0.4462 0.4763 -0.0376 0.0096  -0.0391 90  ASP A N   
670  C CA  . ASP A 88  ? 0.4037 0.4358 0.4747 -0.0339 0.0100  -0.0311 90  ASP A CA  
671  C C   . ASP A 88  ? 0.3977 0.4264 0.4738 -0.0343 0.0171  -0.0316 90  ASP A C   
672  O O   . ASP A 88  ? 0.4183 0.4459 0.4865 -0.0366 0.0215  -0.0349 90  ASP A O   
673  C CB  . ASP A 88  ? 0.4346 0.4655 0.4939 -0.0319 0.0059  -0.0237 90  ASP A CB  
674  C CG  . ASP A 88  ? 0.5494 0.5838 0.6021 -0.0315 -0.0014 -0.0219 90  ASP A CG  
675  O OD1 . ASP A 88  ? 0.5029 0.5411 0.5648 -0.0310 -0.0048 -0.0237 90  ASP A OD1 
676  O OD2 . ASP A 88  ? 0.6569 0.6903 0.6965 -0.0316 -0.0040 -0.0178 90  ASP A OD2 
677  N N   . TYR A 89  ? 0.3394 0.3668 0.4288 -0.0319 0.0184  -0.0281 91  TYR A N   
678  C CA  . TYR A 89  ? 0.3213 0.3457 0.4155 -0.0318 0.0232  -0.0260 91  TYR A CA  
679  C C   . TYR A 89  ? 0.2846 0.3065 0.3767 -0.0289 0.0199  -0.0181 91  TYR A C   
680  O O   . TYR A 89  ? 0.2753 0.2980 0.3697 -0.0262 0.0159  -0.0150 91  TYR A O   
681  C CB  . TYR A 89  ? 0.3592 0.3838 0.4713 -0.0316 0.0267  -0.0279 91  TYR A CB  
682  C CG  . TYR A 89  ? 0.4696 0.4947 0.5881 -0.0343 0.0324  -0.0362 91  TYR A CG  
683  C CD1 . TYR A 89  ? 0.5671 0.5939 0.6948 -0.0353 0.0320  -0.0418 91  TYR A CD1 
684  C CD2 . TYR A 89  ? 0.5164 0.5401 0.6343 -0.0358 0.0386  -0.0384 91  TYR A CD2 
685  C CE1 . TYR A 89  ? 0.5928 0.6189 0.7284 -0.0375 0.0376  -0.0503 91  TYR A CE1 
686  C CE2 . TYR A 89  ? 0.5508 0.5745 0.6761 -0.0377 0.0449  -0.0466 91  TYR A CE2 
687  C CZ  . TYR A 89  ? 0.5938 0.6183 0.7279 -0.0385 0.0443  -0.0530 91  TYR A CZ  
688  O OH  . TYR A 89  ? 0.6395 0.6630 0.7820 -0.0402 0.0507  -0.0622 91  TYR A OH  
689  N N   . SER A 90  ? 0.2644 0.2832 0.3529 -0.0293 0.0218  -0.0150 92  SER A N   
690  C CA  . SER A 90  ? 0.2810 0.2962 0.3674 -0.0269 0.0184  -0.0085 92  SER A CA  
691  C C   . SER A 90  ? 0.3194 0.3323 0.4141 -0.0276 0.0211  -0.0063 92  SER A C   
692  O O   . SER A 90  ? 0.3419 0.3551 0.4383 -0.0301 0.0260  -0.0082 92  SER A O   
693  C CB  . SER A 90  ? 0.2955 0.3085 0.3680 -0.0269 0.0156  -0.0054 92  SER A CB  
694  O OG  . SER A 90  ? 0.3574 0.3732 0.4222 -0.0266 0.0124  -0.0067 92  SER A OG  
695  N N   . LEU A 91  ? 0.2759 0.2866 0.3756 -0.0255 0.0181  -0.0023 93  LEU A N   
696  C CA  . LEU A 91  ? 0.2533 0.2617 0.3603 -0.0264 0.0187  0.0005  93  LEU A CA  
697  C C   . LEU A 91  ? 0.2568 0.2601 0.3558 -0.0252 0.0138  0.0048  93  LEU A C   
698  O O   . LEU A 91  ? 0.2440 0.2457 0.3393 -0.0223 0.0097  0.0062  93  LEU A O   
699  C CB  . LEU A 91  ? 0.2474 0.2574 0.3676 -0.0255 0.0185  0.0015  93  LEU A CB  
700  C CG  . LEU A 91  ? 0.2904 0.2991 0.4208 -0.0269 0.0187  0.0046  93  LEU A CG  
701  C CD1 . LEU A 91  ? 0.3085 0.3198 0.4489 -0.0294 0.0253  0.0017  93  LEU A CD1 
702  C CD2 . LEU A 91  ? 0.3053 0.3146 0.4447 -0.0255 0.0155  0.0079  93  LEU A CD2 
703  N N   . PHE A 92  ? 0.2563 0.2570 0.3533 -0.0272 0.0146  0.0067  94  PHE A N   
704  C CA  . PHE A 92  ? 0.2605 0.2555 0.3510 -0.0265 0.0100  0.0103  94  PHE A CA  
705  C C   . PHE A 92  ? 0.2908 0.2834 0.3898 -0.0289 0.0097  0.0130  94  PHE A C   
706  O O   . PHE A 92  ? 0.2915 0.2874 0.3995 -0.0314 0.0145  0.0127  94  PHE A O   
707  C CB  . PHE A 92  ? 0.2830 0.2766 0.3622 -0.0269 0.0101  0.0113  94  PHE A CB  
708  C CG  . PHE A 92  ? 0.2886 0.2822 0.3597 -0.0236 0.0068  0.0105  94  PHE A CG  
709  C CD1 . PHE A 92  ? 0.2848 0.2838 0.3562 -0.0230 0.0084  0.0070  94  PHE A CD1 
710  C CD2 . PHE A 92  ? 0.3033 0.2916 0.3682 -0.0212 0.0021  0.0130  94  PHE A CD2 
711  C CE1 . PHE A 92  ? 0.2829 0.2829 0.3495 -0.0200 0.0052  0.0068  94  PHE A CE1 
712  C CE2 . PHE A 92  ? 0.3128 0.3018 0.3729 -0.0177 -0.0004 0.0125  94  PHE A CE2 
713  C CZ  . PHE A 92  ? 0.2955 0.2909 0.3567 -0.0172 0.0012  0.0097  94  PHE A CZ  
714  N N   . LYS A 93  ? 0.2908 0.2778 0.3877 -0.0280 0.0040  0.0154  95  LYS A N   
715  C CA  . LYS A 93  ? 0.2937 0.2779 0.3989 -0.0307 0.0021  0.0182  95  LYS A CA  
716  C C   . LYS A 93  ? 0.3269 0.3115 0.4331 -0.0338 0.0068  0.0203  95  LYS A C   
717  O O   . LYS A 93  ? 0.3271 0.3107 0.4231 -0.0335 0.0082  0.0207  95  LYS A O   
718  C CB  . LYS A 93  ? 0.2948 0.2717 0.3951 -0.0294 -0.0053 0.0193  95  LYS A CB  
719  C CG  . LYS A 93  ? 0.3344 0.3111 0.4336 -0.0268 -0.0097 0.0179  95  LYS A CG  
720  C CD  . LYS A 93  ? 0.3950 0.3641 0.4864 -0.0253 -0.0163 0.0174  95  LYS A CD  
721  C CE  . LYS A 93  ? 0.4215 0.3912 0.5103 -0.0231 -0.0197 0.0164  95  LYS A CE  
722  N NZ  . LYS A 93  ? 0.4194 0.3813 0.4976 -0.0210 -0.0256 0.0144  95  LYS A NZ  
723  N N   . ASP A 94  ? 0.3579 0.3445 0.4769 -0.0368 0.0093  0.0222  96  ASP A N   
724  C CA  . ASP A 94  ? 0.4007 0.3886 0.5223 -0.0400 0.0152  0.0248  96  ASP A CA  
725  C C   . ASP A 94  ? 0.4176 0.3988 0.5305 -0.0405 0.0114  0.0285  96  ASP A C   
726  O O   . ASP A 94  ? 0.4327 0.4078 0.5468 -0.0400 0.0042  0.0296  96  ASP A O   
727  C CB  . ASP A 94  ? 0.4599 0.4507 0.6005 -0.0428 0.0171  0.0270  96  ASP A CB  
728  C CG  . ASP A 94  ? 0.5836 0.5782 0.7307 -0.0460 0.0258  0.0292  96  ASP A CG  
729  O OD1 . ASP A 94  ? 0.5756 0.5719 0.7112 -0.0461 0.0317  0.0282  96  ASP A OD1 
730  O OD2 . ASP A 94  ? 0.6533 0.6498 0.8170 -0.0484 0.0269  0.0321  96  ASP A OD2 
731  N N   . GLY A 95  ? 0.4319 0.4140 0.5353 -0.0411 0.0158  0.0300  97  GLY A N   
732  C CA  . GLY A 95  ? 0.4256 0.4017 0.5219 -0.0416 0.0129  0.0346  97  GLY A CA  
733  C C   . GLY A 95  ? 0.4315 0.4045 0.5140 -0.0379 0.0085  0.0335  97  GLY A C   
734  O O   . GLY A 95  ? 0.4723 0.4398 0.5496 -0.0378 0.0056  0.0376  97  GLY A O   
735  N N   . ILE A 96  ? 0.3802 0.3565 0.4583 -0.0349 0.0077  0.0284  98  ILE A N   
736  C CA  . ILE A 96  ? 0.3711 0.3461 0.4383 -0.0314 0.0044  0.0273  98  ILE A CA  
737  C C   . ILE A 96  ? 0.3943 0.3767 0.4551 -0.0316 0.0090  0.0248  98  ILE A C   
738  O O   . ILE A 96  ? 0.3897 0.3773 0.4549 -0.0319 0.0122  0.0203  98  ILE A O   
739  C CB  . ILE A 96  ? 0.3694 0.3424 0.4375 -0.0276 -0.0004 0.0236  98  ILE A CB  
740  C CG1 . ILE A 96  ? 0.3781 0.3442 0.4518 -0.0276 -0.0052 0.0243  98  ILE A CG1 
741  C CG2 . ILE A 96  ? 0.3667 0.3391 0.4257 -0.0237 -0.0031 0.0230  98  ILE A CG2 
742  C CD1 . ILE A 96  ? 0.3801 0.3437 0.4518 -0.0239 -0.0096 0.0208  98  ILE A CD1 
743  N N   . GLU A 97  ? 0.4243 0.4069 0.4748 -0.0317 0.0087  0.0276  99  GLU A N   
744  C CA  . GLU A 97  ? 0.4288 0.4176 0.4709 -0.0317 0.0107  0.0247  99  GLU A CA  
745  C C   . GLU A 97  ? 0.4100 0.4004 0.4514 -0.0280 0.0065  0.0210  99  GLU A C   
746  O O   . GLU A 97  ? 0.3954 0.3813 0.4376 -0.0247 0.0015  0.0226  99  GLU A O   
747  C CB  . GLU A 97  ? 0.4817 0.4706 0.5124 -0.0333 0.0109  0.0298  99  GLU A CB  
748  C CG  . GLU A 97  ? 0.5813 0.5701 0.6131 -0.0373 0.0167  0.0338  99  GLU A CG  
749  C CD  . GLU A 97  ? 0.7355 0.7265 0.7539 -0.0397 0.0191  0.0386  99  GLU A CD  
750  O OE1 . GLU A 97  ? 0.7229 0.7132 0.7323 -0.0380 0.0137  0.0417  99  GLU A OE1 
751  O OE2 . GLU A 97  ? 0.8408 0.8347 0.8581 -0.0431 0.0266  0.0395  99  GLU A OE2 
752  N N   . PRO A 98  ? 0.3735 0.3700 0.4146 -0.0283 0.0088  0.0157  100 PRO A N   
753  C CA  . PRO A 98  ? 0.3707 0.3694 0.4131 -0.0251 0.0052  0.0129  100 PRO A CA  
754  C C   . PRO A 98  ? 0.3814 0.3816 0.4153 -0.0236 0.0007  0.0150  100 PRO A C   
755  O O   . PRO A 98  ? 0.3779 0.3833 0.4102 -0.0236 -0.0002 0.0118  100 PRO A O   
756  C CB  . PRO A 98  ? 0.3810 0.3854 0.4286 -0.0268 0.0095  0.0066  100 PRO A CB  
757  C CG  . PRO A 98  ? 0.3886 0.3948 0.4302 -0.0306 0.0145  0.0057  100 PRO A CG  
758  C CD  . PRO A 98  ? 0.3764 0.3779 0.4171 -0.0316 0.0152  0.0116  100 PRO A CD  
759  N N   . MET A 99  ? 0.3908 0.3861 0.4207 -0.0224 -0.0026 0.0208  101 MET A N   
760  C CA  . MET A 99  ? 0.4061 0.4022 0.4299 -0.0206 -0.0076 0.0245  101 MET A CA  
761  C C   . MET A 99  ? 0.3887 0.3778 0.4163 -0.0167 -0.0114 0.0284  101 MET A C   
762  O O   . MET A 99  ? 0.3690 0.3517 0.3994 -0.0171 -0.0105 0.0302  101 MET A O   
763  C CB  . MET A 99  ? 0.4763 0.4730 0.4895 -0.0241 -0.0069 0.0291  101 MET A CB  
764  C CG  . MET A 99  ? 0.6107 0.6139 0.6170 -0.0281 -0.0028 0.0243  101 MET A CG  
765  S SD  . MET A 99  ? 0.9154 0.9187 0.9106 -0.0330 0.0030  0.0282  101 MET A SD  
766  C CE  . MET A 99  ? 0.8878 0.8841 0.8813 -0.0318 -0.0014 0.0398  101 MET A CE  
767  N N   . TRP A 100 ? 0.4091 0.3993 0.4378 -0.0129 -0.0157 0.0295  102 TRP A N   
768  C CA  . TRP A 100 ? 0.4550 0.4387 0.4890 -0.0083 -0.0182 0.0310  102 TRP A CA  
769  C C   . TRP A 100 ? 0.4810 0.4567 0.5133 -0.0084 -0.0203 0.0371  102 TRP A C   
770  O O   . TRP A 100 ? 0.4767 0.4449 0.5135 -0.0057 -0.0212 0.0369  102 TRP A O   
771  C CB  . TRP A 100 ? 0.4762 0.4635 0.5144 -0.0036 -0.0212 0.0306  102 TRP A CB  
772  C CG  . TRP A 100 ? 0.5097 0.4984 0.5460 -0.0024 -0.0262 0.0365  102 TRP A CG  
773  C CD1 . TRP A 100 ? 0.5413 0.5374 0.5726 -0.0048 -0.0288 0.0382  102 TRP A CD1 
774  C CD2 . TRP A 100 ? 0.5133 0.4957 0.5533 0.0018  -0.0297 0.0415  102 TRP A CD2 
775  N NE1 . TRP A 100 ? 0.5476 0.5428 0.5788 -0.0027 -0.0343 0.0451  102 TRP A NE1 
776  C CE2 . TRP A 100 ? 0.5340 0.5209 0.5718 0.0016  -0.0346 0.0472  102 TRP A CE2 
777  C CE3 . TRP A 100 ? 0.5199 0.4929 0.5648 0.0055  -0.0295 0.0413  102 TRP A CE3 
778  C CZ2 . TRP A 100 ? 0.5418 0.5245 0.5843 0.0055  -0.0391 0.0536  102 TRP A CZ2 
779  C CZ3 . TRP A 100 ? 0.5337 0.5019 0.5830 0.0094  -0.0333 0.0464  102 TRP A CZ3 
780  C CH2 . TRP A 100 ? 0.5398 0.5129 0.5888 0.0094  -0.0379 0.0530  102 TRP A CH2 
781  N N   . GLU A 101 ? 0.4876 0.4646 0.5133 -0.0117 -0.0208 0.0424  103 GLU A N   
782  C CA  . GLU A 101 ? 0.5251 0.4949 0.5503 -0.0120 -0.0229 0.0496  103 GLU A CA  
783  C C   . GLU A 101 ? 0.5101 0.4744 0.5373 -0.0156 -0.0193 0.0500  103 GLU A C   
784  O O   . GLU A 101 ? 0.4968 0.4539 0.5262 -0.0160 -0.0209 0.0559  103 GLU A O   
785  C CB  . GLU A 101 ? 0.5899 0.5638 0.6070 -0.0136 -0.0258 0.0568  103 GLU A CB  
786  C CG  . GLU A 101 ? 0.7254 0.7060 0.7320 -0.0191 -0.0219 0.0568  103 GLU A CG  
787  C CD  . GLU A 101 ? 0.8008 0.7909 0.8021 -0.0204 -0.0211 0.0504  103 GLU A CD  
788  O OE1 . GLU A 101 ? 0.6478 0.6405 0.6556 -0.0175 -0.0222 0.0446  103 GLU A OE1 
789  O OE2 . GLU A 101 ? 0.8949 0.8898 0.8852 -0.0245 -0.0189 0.0511  103 GLU A OE2 
790  N N   . ASP A 102 ? 0.4576 0.4250 0.4864 -0.0181 -0.0147 0.0443  104 ASP A N   
791  C CA  . ASP A 102 ? 0.4333 0.3956 0.4679 -0.0208 -0.0122 0.0441  104 ASP A CA  
792  C C   . ASP A 102 ? 0.4538 0.4061 0.4947 -0.0176 -0.0164 0.0438  104 ASP A C   
793  O O   . ASP A 102 ? 0.4516 0.4028 0.4933 -0.0130 -0.0189 0.0403  104 ASP A O   
794  C CB  . ASP A 102 ? 0.4237 0.3909 0.4617 -0.0225 -0.0080 0.0375  104 ASP A CB  
795  C CG  . ASP A 102 ? 0.4708 0.4350 0.5160 -0.0259 -0.0055 0.0378  104 ASP A CG  
796  O OD1 . ASP A 102 ? 0.4825 0.4398 0.5337 -0.0248 -0.0087 0.0369  104 ASP A OD1 
797  O OD2 . ASP A 102 ? 0.4814 0.4504 0.5268 -0.0298 -0.0001 0.0385  104 ASP A OD2 
798  N N   . GLU A 103 ? 0.4650 0.4100 0.5107 -0.0202 -0.0168 0.0473  105 GLU A N   
799  C CA  . GLU A 103 ? 0.4944 0.4287 0.5462 -0.0179 -0.0211 0.0462  105 GLU A CA  
800  C C   . GLU A 103 ? 0.4633 0.3969 0.5164 -0.0150 -0.0221 0.0379  105 GLU A C   
801  O O   . GLU A 103 ? 0.4708 0.3978 0.5244 -0.0108 -0.0253 0.0350  105 GLU A O   
802  C CB  . GLU A 103 ? 0.5687 0.4969 0.6275 -0.0225 -0.0210 0.0500  105 GLU A CB  
803  C CG  . GLU A 103 ? 0.7355 0.6514 0.8009 -0.0210 -0.0262 0.0488  105 GLU A CG  
804  C CD  . GLU A 103 ? 0.9285 0.8369 0.9950 -0.0186 -0.0293 0.0545  105 GLU A CD  
805  O OE1 . GLU A 103 ? 0.9662 0.8798 1.0276 -0.0176 -0.0283 0.0598  105 GLU A OE1 
806  O OE2 . GLU A 103 ? 1.0058 0.9029 1.0789 -0.0177 -0.0333 0.0535  105 GLU A OE2 
807  N N   . LYS A 104 ? 0.4413 0.3815 0.4948 -0.0172 -0.0190 0.0343  106 LYS A N   
808  C CA  . LYS A 104 ? 0.4059 0.3465 0.4600 -0.0151 -0.0198 0.0279  106 LYS A CA  
809  C C   . LYS A 104 ? 0.3994 0.3457 0.4492 -0.0106 -0.0189 0.0246  106 LYS A C   
810  O O   . LYS A 104 ? 0.4037 0.3496 0.4530 -0.0081 -0.0194 0.0200  106 LYS A O   
811  C CB  . LYS A 104 ? 0.4154 0.3609 0.4745 -0.0193 -0.0172 0.0266  106 LYS A CB  
812  C CG  . LYS A 104 ? 0.5046 0.4445 0.5711 -0.0234 -0.0190 0.0288  106 LYS A CG  
813  C CD  . LYS A 104 ? 0.6424 0.5730 0.7098 -0.0218 -0.0249 0.0252  106 LYS A CD  
814  C CE  . LYS A 104 ? 0.6973 0.6232 0.7738 -0.0263 -0.0279 0.0262  106 LYS A CE  
815  N NZ  . LYS A 104 ? 0.7835 0.6978 0.8589 -0.0247 -0.0345 0.0227  106 LYS A NZ  
816  N N   . ASN A 105 ? 0.3799 0.3315 0.4266 -0.0097 -0.0177 0.0271  107 ASN A N   
817  C CA  . ASN A 105 ? 0.3606 0.3181 0.4057 -0.0058 -0.0173 0.0247  107 ASN A CA  
818  C C   . ASN A 105 ? 0.3830 0.3373 0.4276 -0.0013 -0.0202 0.0271  107 ASN A C   
819  O O   . ASN A 105 ? 0.3901 0.3467 0.4358 0.0032  -0.0201 0.0245  107 ASN A O   
820  C CB  . ASN A 105 ? 0.3513 0.3187 0.3947 -0.0084 -0.0146 0.0250  107 ASN A CB  
821  C CG  . ASN A 105 ? 0.3706 0.3421 0.4165 -0.0121 -0.0109 0.0222  107 ASN A CG  
822  O OD1 . ASN A 105 ? 0.3839 0.3540 0.4331 -0.0113 -0.0107 0.0193  107 ASN A OD1 
823  N ND2 . ASN A 105 ? 0.3572 0.3335 0.4016 -0.0159 -0.0080 0.0232  107 ASN A ND2 
824  N N   . LYS A 106 ? 0.3997 0.3491 0.4443 -0.0022 -0.0225 0.0325  108 LYS A N   
825  C CA  . LYS A 106 ? 0.4091 0.3566 0.4550 0.0021  -0.0255 0.0361  108 LYS A CA  
826  C C   . LYS A 106 ? 0.3996 0.3407 0.4494 0.0081  -0.0265 0.0322  108 LYS A C   
827  O O   . LYS A 106 ? 0.4072 0.3507 0.4599 0.0125  -0.0276 0.0334  108 LYS A O   
828  C CB  . LYS A 106 ? 0.4618 0.4043 0.5078 0.0000  -0.0280 0.0439  108 LYS A CB  
829  C CG  . LYS A 106 ? 0.5721 0.5036 0.6215 -0.0017 -0.0288 0.0445  108 LYS A CG  
830  C CD  . LYS A 106 ? 0.6509 0.5777 0.7019 -0.0035 -0.0312 0.0538  108 LYS A CD  
831  C CE  . LYS A 106 ? 0.7796 0.6934 0.8375 -0.0035 -0.0334 0.0544  108 LYS A CE  
832  N NZ  . LYS A 106 ? 0.8629 0.7728 0.9232 -0.0073 -0.0344 0.0643  108 LYS A NZ  
833  N N   . ARG A 107 ? 0.3814 0.3150 0.4313 0.0084  -0.0262 0.0274  109 ARG A N   
834  C CA  . ARG A 107 ? 0.4113 0.3388 0.4624 0.0142  -0.0263 0.0223  109 ARG A CA  
835  C C   . ARG A 107 ? 0.4168 0.3500 0.4650 0.0161  -0.0230 0.0164  109 ARG A C   
836  O O   . ARG A 107 ? 0.4164 0.3446 0.4632 0.0204  -0.0221 0.0114  109 ARG A O   
837  C CB  . ARG A 107 ? 0.4769 0.3912 0.5286 0.0136  -0.0287 0.0197  109 ARG A CB  
838  C CG  . ARG A 107 ? 0.5702 0.4769 0.6269 0.0121  -0.0320 0.0259  109 ARG A CG  
839  C CD  . ARG A 107 ? 0.6778 0.5733 0.7357 0.0091  -0.0344 0.0231  109 ARG A CD  
840  N NE  . ARG A 107 ? 0.8090 0.6981 0.8729 0.0060  -0.0371 0.0302  109 ARG A NE  
841  C CZ  . ARG A 107 ? 0.8623 0.7550 0.9272 -0.0002 -0.0366 0.0363  109 ARG A CZ  
842  N NH1 . ARG A 107 ? 0.8712 0.7576 0.9420 -0.0026 -0.0386 0.0436  109 ARG A NH1 
843  N NH2 . ARG A 107 ? 0.8208 0.7234 0.8815 -0.0037 -0.0336 0.0355  109 ARG A NH2 
844  N N   . GLY A 108 ? 0.3915 0.3349 0.4385 0.0130  -0.0209 0.0171  110 GLY A N   
845  C CA  . GLY A 108 ? 0.3571 0.3063 0.4024 0.0137  -0.0178 0.0130  110 GLY A CA  
846  C C   . GLY A 108 ? 0.3618 0.3214 0.4104 0.0160  -0.0155 0.0138  110 GLY A C   
847  O O   . GLY A 108 ? 0.3426 0.3041 0.3951 0.0190  -0.0164 0.0163  110 GLY A O   
848  N N   . GLY A 109 ? 0.3276 0.2943 0.3762 0.0144  -0.0127 0.0121  111 GLY A N   
849  C CA  . GLY A 109 ? 0.3182 0.2946 0.3716 0.0164  -0.0103 0.0123  111 GLY A CA  
850  C C   . GLY A 109 ? 0.3083 0.2911 0.3627 0.0132  -0.0077 0.0110  111 GLY A C   
851  O O   . GLY A 109 ? 0.2985 0.2791 0.3506 0.0092  -0.0081 0.0105  111 GLY A O   
852  N N   . ARG A 110 ? 0.2919 0.2828 0.3516 0.0149  -0.0051 0.0110  112 ARG A N   
853  C CA  . ARG A 110 ? 0.2814 0.2784 0.3445 0.0120  -0.0026 0.0104  112 ARG A CA  
854  C C   . ARG A 110 ? 0.2920 0.2944 0.3594 0.0155  0.0012  0.0105  112 ARG A C   
855  O O   . ARG A 110 ? 0.3175 0.3225 0.3886 0.0194  0.0020  0.0112  112 ARG A O   
856  C CB  . ARG A 110 ? 0.3041 0.3075 0.3717 0.0078  -0.0036 0.0109  112 ARG A CB  
857  C CG  . ARG A 110 ? 0.3678 0.3780 0.4416 0.0095  -0.0046 0.0120  112 ARG A CG  
858  C CD  . ARG A 110 ? 0.4463 0.4619 0.5220 0.0051  -0.0067 0.0116  112 ARG A CD  
859  N NE  . ARG A 110 ? 0.5177 0.5399 0.6001 0.0071  -0.0088 0.0129  112 ARG A NE  
860  C CZ  . ARG A 110 ? 0.5327 0.5614 0.6183 0.0039  -0.0115 0.0122  112 ARG A CZ  
861  N NH1 . ARG A 110 ? 0.5337 0.5686 0.6269 0.0059  -0.0144 0.0139  112 ARG A NH1 
862  N NH2 . ARG A 110 ? 0.4961 0.5250 0.5777 -0.0012 -0.0115 0.0095  112 ARG A NH2 
863  N N   . TRP A 111 ? 0.2720 0.2764 0.3400 0.0138  0.0035  0.0105  113 TRP A N   
864  C CA  . TRP A 111 ? 0.2627 0.2739 0.3365 0.0157  0.0077  0.0119  113 TRP A CA  
865  C C   . TRP A 111 ? 0.2956 0.3147 0.3802 0.0121  0.0080  0.0126  113 TRP A C   
866  O O   . TRP A 111 ? 0.2947 0.3133 0.3806 0.0077  0.0069  0.0119  113 TRP A O   
867  C CB  . TRP A 111 ? 0.2681 0.2767 0.3363 0.0153  0.0090  0.0124  113 TRP A CB  
868  C CG  . TRP A 111 ? 0.2858 0.2877 0.3429 0.0194  0.0095  0.0109  113 TRP A CG  
869  C CD1 . TRP A 111 ? 0.3194 0.3125 0.3666 0.0185  0.0061  0.0088  113 TRP A CD1 
870  C CD2 . TRP A 111 ? 0.3156 0.3190 0.3704 0.0249  0.0139  0.0109  113 TRP A CD2 
871  N NE1 . TRP A 111 ? 0.3442 0.3324 0.3816 0.0231  0.0076  0.0066  113 TRP A NE1 
872  C CE2 . TRP A 111 ? 0.3498 0.3442 0.3915 0.0274  0.0130  0.0077  113 TRP A CE2 
873  C CE3 . TRP A 111 ? 0.3362 0.3477 0.3997 0.0280  0.0188  0.0129  113 TRP A CE3 
874  C CZ2 . TRP A 111 ? 0.3731 0.3661 0.4086 0.0330  0.0175  0.0060  113 TRP A CZ2 
875  C CZ3 . TRP A 111 ? 0.3626 0.3734 0.4213 0.0337  0.0236  0.0121  113 TRP A CZ3 
876  C CH2 . TRP A 111 ? 0.3760 0.3775 0.4202 0.0363  0.0232  0.0083  113 TRP A CH2 
877  N N   . LEU A 112 ? 0.2841 0.3104 0.3778 0.0139  0.0094  0.0138  114 LEU A N   
878  C CA  . LEU A 112 ? 0.3009 0.3341 0.4053 0.0103  0.0083  0.0134  114 LEU A CA  
879  C C   . LEU A 112 ? 0.3040 0.3447 0.4202 0.0107  0.0123  0.0157  114 LEU A C   
880  O O   . LEU A 112 ? 0.2862 0.3299 0.4052 0.0150  0.0156  0.0181  114 LEU A O   
881  C CB  . LEU A 112 ? 0.3454 0.3813 0.4523 0.0114  0.0047  0.0133  114 LEU A CB  
882  C CG  . LEU A 112 ? 0.4081 0.4515 0.5253 0.0078  0.0023  0.0123  114 LEU A CG  
883  C CD1 . LEU A 112 ? 0.4349 0.4757 0.5469 0.0025  -0.0001 0.0091  114 LEU A CD1 
884  C CD2 . LEU A 112 ? 0.4393 0.4869 0.5609 0.0101  -0.0015 0.0137  114 LEU A CD2 
885  N N   . ILE A 113 ? 0.2907 0.3344 0.4149 0.0063  0.0123  0.0150  115 ILE A N   
886  C CA  . ILE A 113 ? 0.3389 0.3903 0.4783 0.0056  0.0152  0.0172  115 ILE A CA  
887  C C   . ILE A 113 ? 0.3185 0.3742 0.4673 0.0015  0.0116  0.0139  115 ILE A C   
888  O O   . ILE A 113 ? 0.2781 0.3303 0.4216 -0.0021 0.0086  0.0097  115 ILE A O   
889  C CB  . ILE A 113 ? 0.3848 0.4358 0.5271 0.0047  0.0190  0.0203  115 ILE A CB  
890  C CG1 . ILE A 113 ? 0.4113 0.4703 0.5703 0.0046  0.0230  0.0246  115 ILE A CG1 
891  C CG2 . ILE A 113 ? 0.4181 0.4656 0.5612 0.0000  0.0171  0.0173  115 ILE A CG2 
892  C CD1 . ILE A 113 ? 0.4515 0.5154 0.6126 0.0094  0.0276  0.0292  115 ILE A CD1 
893  N N   . THR A 114 ? 0.3287 0.3919 0.4911 0.0018  0.0119  0.0154  116 THR A N   
894  C CA  . THR A 114 ? 0.3309 0.3985 0.5028 -0.0024 0.0076  0.0117  116 THR A CA  
895  C C   . THR A 114 ? 0.3355 0.4078 0.5246 -0.0048 0.0105  0.0131  116 THR A C   
896  O O   . THR A 114 ? 0.3487 0.4251 0.5465 -0.0022 0.0150  0.0185  116 THR A O   
897  C CB  . THR A 114 ? 0.3990 0.4719 0.5749 -0.0008 0.0034  0.0123  116 THR A CB  
898  O OG1 . THR A 114 ? 0.4619 0.5297 0.6228 0.0021  0.0012  0.0123  116 THR A OG1 
899  C CG2 . THR A 114 ? 0.4302 0.5069 0.6127 -0.0060 -0.0028 0.0076  116 THR A CG2 
900  N N   . LEU A 115 ? 0.3224 0.3939 0.5164 -0.0098 0.0084  0.0082  117 LEU A N   
901  C CA  . LEU A 115 ? 0.3367 0.4114 0.5490 -0.0130 0.0103  0.0083  117 LEU A CA  
902  C C   . LEU A 115 ? 0.3823 0.4628 0.6074 -0.0166 0.0051  0.0041  117 LEU A C   
903  O O   . LEU A 115 ? 0.3957 0.4748 0.6121 -0.0190 -0.0004 -0.0019 117 LEU A O   
904  C CB  . LEU A 115 ? 0.3408 0.4095 0.5515 -0.0163 0.0115  0.0043  117 LEU A CB  
905  C CG  . LEU A 115 ? 0.3935 0.4568 0.5947 -0.0139 0.0153  0.0082  117 LEU A CG  
906  C CD1 . LEU A 115 ? 0.4010 0.4599 0.6068 -0.0174 0.0165  0.0046  117 LEU A CD1 
907  C CD2 . LEU A 115 ? 0.4053 0.4717 0.6131 -0.0108 0.0199  0.0166  117 LEU A CD2 
908  N N   . ASN A 116 ? 0.3985 0.4853 0.6440 -0.0176 0.0065  0.0073  118 ASN A N   
909  C CA  . ASN A 116 ? 0.4225 0.5147 0.6821 -0.0217 0.0007  0.0029  118 ASN A CA  
910  C C   . ASN A 116 ? 0.4462 0.5337 0.7093 -0.0277 -0.0015 -0.0059 118 ASN A C   
911  O O   . ASN A 116 ? 0.4152 0.4965 0.6746 -0.0282 0.0025  -0.0071 118 ASN A O   
912  C CB  . ASN A 116 ? 0.4391 0.5400 0.7212 -0.0208 0.0030  0.0096  118 ASN A CB  
913  C CG  . ASN A 116 ? 0.5307 0.6393 0.8262 -0.0233 -0.0041 0.0075  118 ASN A CG  
914  O OD1 . ASN A 116 ? 0.5373 0.6449 0.8297 -0.0277 -0.0118 -0.0006 118 ASN A OD1 
915  N ND2 . ASN A 116 ? 0.5498 0.6668 0.8606 -0.0205 -0.0017 0.0148  118 ASN A ND2 
916  N N   . LYS A 117 ? 0.4781 0.5687 0.7488 -0.0320 -0.0081 -0.0122 119 LYS A N   
917  C CA  . LYS A 117 ? 0.5239 0.6101 0.7954 -0.0376 -0.0111 -0.0226 119 LYS A CA  
918  C C   . LYS A 117 ? 0.5265 0.6089 0.8141 -0.0394 -0.0053 -0.0227 119 LYS A C   
919  O O   . LYS A 117 ? 0.5473 0.6227 0.8285 -0.0414 -0.0037 -0.0294 119 LYS A O   
920  C CB  . LYS A 117 ? 0.5780 0.6697 0.8599 -0.0421 -0.0197 -0.0281 119 LYS A CB  
921  C CG  . LYS A 117 ? 0.6743 0.7694 0.9402 -0.0413 -0.0272 -0.0290 119 LYS A CG  
922  C CD  . LYS A 117 ? 0.7276 0.8317 1.0103 -0.0438 -0.0354 -0.0287 119 LYS A CD  
923  C CE  . LYS A 117 ? 0.7869 0.8973 1.0633 -0.0400 -0.0400 -0.0225 119 LYS A CE  
924  N NZ  . LYS A 117 ? 0.8117 0.9244 1.0915 -0.0332 -0.0325 -0.0118 119 LYS A NZ  
925  N N   . GLN A 118 ? 0.5128 0.5996 0.8208 -0.0383 -0.0015 -0.0144 120 GLN A N   
926  C CA  . GLN A 118 ? 0.5317 0.6157 0.8576 -0.0398 0.0038  -0.0120 120 GLN A CA  
927  C C   . GLN A 118 ? 0.5129 0.5914 0.8278 -0.0361 0.0103  -0.0066 120 GLN A C   
928  O O   . GLN A 118 ? 0.5083 0.5816 0.8312 -0.0377 0.0134  -0.0081 120 GLN A O   
929  C CB  . GLN A 118 ? 0.5907 0.6823 0.9422 -0.0401 0.0056  -0.0034 120 GLN A CB  
930  C CG  . GLN A 118 ? 0.6873 0.7774 1.0651 -0.0455 0.0050  -0.0071 120 GLN A CG  
931  C CD  . GLN A 118 ? 0.7908 0.8895 1.1949 -0.0476 0.0035  -0.0019 120 GLN A CD  
932  O OE1 . GLN A 118 ? 0.8356 0.9411 1.2405 -0.0481 -0.0020 -0.0030 120 GLN A OE1 
933  N NE2 . GLN A 118 ? 0.7887 0.8878 1.2169 -0.0491 0.0082  0.0047  120 GLN A NE2 
934  N N   . GLN A 119 ? 0.4770 0.5564 0.7737 -0.0312 0.0119  -0.0009 121 GLN A N   
935  C CA  . GLN A 119 ? 0.4464 0.5206 0.7303 -0.0281 0.0164  0.0032  121 GLN A CA  
936  C C   . GLN A 119 ? 0.4351 0.5022 0.7067 -0.0297 0.0154  -0.0050 121 GLN A C   
937  O O   . GLN A 119 ? 0.4342 0.4969 0.6996 -0.0280 0.0188  -0.0020 121 GLN A O   
938  C CB  . GLN A 119 ? 0.4477 0.5243 0.7162 -0.0228 0.0178  0.0100  121 GLN A CB  
939  C CG  . GLN A 119 ? 0.4542 0.5376 0.7355 -0.0205 0.0215  0.0194  121 GLN A CG  
940  C CD  . GLN A 119 ? 0.4357 0.5207 0.7014 -0.0151 0.0234  0.0244  121 GLN A CD  
941  O OE1 . GLN A 119 ? 0.4221 0.5102 0.6826 -0.0136 0.0202  0.0223  121 GLN A OE1 
942  N NE2 . GLN A 119 ? 0.4450 0.5277 0.7028 -0.0120 0.0280  0.0307  121 GLN A NE2 
943  N N   . ARG A 120 ? 0.4324 0.4982 0.7001 -0.0333 0.0109  -0.0155 122 ARG A N   
944  C CA  . ARG A 120 ? 0.4501 0.5095 0.7073 -0.0351 0.0114  -0.0235 122 ARG A CA  
945  C C   . ARG A 120 ? 0.4378 0.4927 0.7105 -0.0365 0.0160  -0.0242 122 ARG A C   
946  O O   . ARG A 120 ? 0.4137 0.4640 0.6798 -0.0352 0.0192  -0.0239 122 ARG A O   
947  C CB  . ARG A 120 ? 0.4876 0.5466 0.7380 -0.0390 0.0063  -0.0347 122 ARG A CB  
948  C CG  . ARG A 120 ? 0.5798 0.6323 0.8176 -0.0404 0.0086  -0.0427 122 ARG A CG  
949  C CD  . ARG A 120 ? 0.6623 0.7145 0.8874 -0.0439 0.0039  -0.0532 122 ARG A CD  
950  N NE  . ARG A 120 ? 0.6911 0.7465 0.8976 -0.0422 -0.0007 -0.0500 122 ARG A NE  
951  C CZ  . ARG A 120 ? 0.7342 0.7918 0.9304 -0.0449 -0.0070 -0.0559 122 ARG A CZ  
952  N NH1 . ARG A 120 ? 0.7125 0.7730 0.8937 -0.0429 -0.0112 -0.0515 122 ARG A NH1 
953  N NH2 . ARG A 120 ? 0.7423 0.7991 0.9434 -0.0497 -0.0097 -0.0664 122 ARG A NH2 
954  N N   . ARG A 121 ? 0.4419 0.4984 0.7375 -0.0392 0.0160  -0.0247 123 ARG A N   
955  C CA  . ARG A 121 ? 0.4636 0.5154 0.7763 -0.0406 0.0200  -0.0257 123 ARG A CA  
956  C C   . ARG A 121 ? 0.4671 0.5195 0.7848 -0.0370 0.0241  -0.0128 123 ARG A C   
957  O O   . ARG A 121 ? 0.5082 0.5560 0.8299 -0.0366 0.0273  -0.0123 123 ARG A O   
958  C CB  . ARG A 121 ? 0.5237 0.5761 0.8608 -0.0447 0.0186  -0.0297 123 ARG A CB  
959  C CG  . ARG A 121 ? 0.6411 0.6927 0.9747 -0.0490 0.0135  -0.0434 123 ARG A CG  
960  C CD  . ARG A 121 ? 0.7692 0.8130 1.1052 -0.0518 0.0155  -0.0560 123 ARG A CD  
961  N NE  . ARG A 121 ? 0.8822 0.9225 1.1950 -0.0502 0.0177  -0.0604 123 ARG A NE  
962  C CZ  . ARG A 121 ? 0.9487 0.9904 1.2377 -0.0505 0.0142  -0.0657 123 ARG A CZ  
963  N NH1 . ARG A 121 ? 0.9682 1.0148 1.2530 -0.0524 0.0075  -0.0672 123 ARG A NH1 
964  N NH2 . ARG A 121 ? 0.9455 0.9838 1.2159 -0.0491 0.0172  -0.0685 123 ARG A NH2 
965  N N   . SER A 122 ? 0.4461 0.5043 0.7636 -0.0344 0.0243  -0.0025 124 SER A N   
966  C CA  . SER A 122 ? 0.4558 0.5147 0.7777 -0.0314 0.0282  0.0099  124 SER A CA  
967  C C   . SER A 122 ? 0.4484 0.5056 0.7482 -0.0274 0.0290  0.0146  124 SER A C   
968  O O   . SER A 122 ? 0.4632 0.5180 0.7658 -0.0263 0.0311  0.0205  124 SER A O   
969  C CB  . SER A 122 ? 0.4873 0.5532 0.8200 -0.0305 0.0294  0.0192  124 SER A CB  
970  O OG  . SER A 122 ? 0.5218 0.5922 0.8401 -0.0286 0.0271  0.0182  124 SER A OG  
971  N N   . ASP A 123 ? 0.3987 0.4572 0.6780 -0.0255 0.0267  0.0122  125 ASP A N   
972  C CA  . ASP A 123 ? 0.3542 0.4114 0.6137 -0.0216 0.0270  0.0173  125 ASP A CA  
973  C C   . ASP A 123 ? 0.3114 0.3640 0.5527 -0.0216 0.0249  0.0102  125 ASP A C   
974  O O   . ASP A 123 ? 0.3118 0.3618 0.5404 -0.0193 0.0250  0.0137  125 ASP A O   
975  C CB  . ASP A 123 ? 0.4168 0.4790 0.6677 -0.0185 0.0269  0.0220  125 ASP A CB  
976  C CG  . ASP A 123 ? 0.5455 0.6134 0.8107 -0.0174 0.0303  0.0311  125 ASP A CG  
977  O OD1 . ASP A 123 ? 0.5585 0.6258 0.8344 -0.0180 0.0328  0.0371  125 ASP A OD1 
978  O OD2 . ASP A 123 ? 0.5955 0.6689 0.8615 -0.0160 0.0306  0.0327  125 ASP A OD2 
979  N N   . LEU A 124 ? 0.2774 0.3290 0.5168 -0.0243 0.0227  0.0007  126 LEU A N   
980  C CA  . LEU A 124 ? 0.2802 0.3283 0.5006 -0.0242 0.0210  -0.0047 126 LEU A CA  
981  C C   . LEU A 124 ? 0.2597 0.3028 0.4786 -0.0242 0.0234  -0.0045 126 LEU A C   
982  O O   . LEU A 124 ? 0.2502 0.2911 0.4545 -0.0224 0.0227  -0.0024 126 LEU A O   
983  C CB  . LEU A 124 ? 0.3129 0.3610 0.5310 -0.0276 0.0185  -0.0147 126 LEU A CB  
984  C CG  . LEU A 124 ? 0.3685 0.4134 0.5670 -0.0278 0.0173  -0.0196 126 LEU A CG  
985  C CD1 . LEU A 124 ? 0.3566 0.4026 0.5406 -0.0247 0.0148  -0.0147 126 LEU A CD1 
986  C CD2 . LEU A 124 ? 0.4159 0.4608 0.6116 -0.0316 0.0152  -0.0295 126 LEU A CD2 
987  N N   . ASN A 125 ? 0.2481 0.2893 0.4828 -0.0264 0.0260  -0.0070 127 ASN A N   
988  C CA  . ASN A 125 ? 0.2670 0.3042 0.5030 -0.0263 0.0282  -0.0068 127 ASN A CA  
989  C C   . ASN A 125 ? 0.2422 0.2795 0.4761 -0.0235 0.0278  0.0035  127 ASN A C   
990  O O   . ASN A 125 ? 0.2362 0.2710 0.4609 -0.0226 0.0273  0.0047  127 ASN A O   
991  C CB  . ASN A 125 ? 0.3058 0.3411 0.5629 -0.0288 0.0315  -0.0114 127 ASN A CB  
992  C CG  . ASN A 125 ? 0.3881 0.4219 0.6453 -0.0320 0.0322  -0.0238 127 ASN A CG  
993  O OD1 . ASN A 125 ? 0.4347 0.4674 0.7090 -0.0342 0.0337  -0.0289 127 ASN A OD1 
994  N ND2 . ASN A 125 ? 0.3836 0.4172 0.6224 -0.0326 0.0308  -0.0293 127 ASN A ND2 
995  N N   . ARG A 126 ? 0.2286 0.2689 0.4702 -0.0222 0.0278  0.0111  128 ARG A N   
996  C CA  . ARG A 126 ? 0.2599 0.3006 0.4984 -0.0196 0.0272  0.0212  128 ARG A CA  
997  C C   . ARG A 126 ? 0.2354 0.2757 0.4513 -0.0171 0.0248  0.0223  128 ARG A C   
998  O O   . ARG A 126 ? 0.2447 0.2825 0.4524 -0.0160 0.0232  0.0255  128 ARG A O   
999  C CB  . ARG A 126 ? 0.3134 0.3581 0.5637 -0.0188 0.0285  0.0296  128 ARG A CB  
1000 C CG  . ARG A 126 ? 0.4254 0.4715 0.6663 -0.0158 0.0278  0.0404  128 ARG A CG  
1001 C CD  . ARG A 126 ? 0.5001 0.5433 0.7424 -0.0158 0.0261  0.0445  128 ARG A CD  
1002 N NE  . ARG A 126 ? 0.4646 0.5075 0.7305 -0.0177 0.0276  0.0471  128 ARG A NE  
1003 C CZ  . ARG A 126 ? 0.4957 0.5369 0.7699 -0.0179 0.0263  0.0514  128 ARG A CZ  
1004 N NH1 . ARG A 126 ? 0.5327 0.5723 0.7930 -0.0168 0.0229  0.0534  128 ARG A NH1 
1005 N NH2 . ARG A 126 ? 0.5281 0.5689 0.8263 -0.0193 0.0281  0.0537  128 ARG A NH2 
1006 N N   . PHE A 127 ? 0.2224 0.2648 0.4300 -0.0163 0.0242  0.0197  129 PHE A N   
1007 C CA  . PHE A 127 ? 0.2390 0.2800 0.4263 -0.0136 0.0221  0.0202  129 PHE A CA  
1008 C C   . PHE A 127 ? 0.2284 0.2648 0.4050 -0.0145 0.0203  0.0152  129 PHE A C   
1009 O O   . PHE A 127 ? 0.2314 0.2650 0.3953 -0.0128 0.0184  0.0175  129 PHE A O   
1010 C CB  . PHE A 127 ? 0.2418 0.2862 0.4249 -0.0122 0.0218  0.0188  129 PHE A CB  
1011 C CG  . PHE A 127 ? 0.3117 0.3611 0.5004 -0.0099 0.0240  0.0254  129 PHE A CG  
1012 C CD1 . PHE A 127 ? 0.3537 0.4046 0.5514 -0.0097 0.0263  0.0327  129 PHE A CD1 
1013 C CD2 . PHE A 127 ? 0.4034 0.4561 0.5870 -0.0075 0.0240  0.0254  129 PHE A CD2 
1014 C CE1 . PHE A 127 ? 0.3879 0.4440 0.5906 -0.0076 0.0294  0.0397  129 PHE A CE1 
1015 C CE2 . PHE A 127 ? 0.4256 0.4833 0.6140 -0.0050 0.0273  0.0319  129 PHE A CE2 
1016 C CZ  . PHE A 127 ? 0.4019 0.4616 0.6005 -0.0055 0.0303  0.0388  129 PHE A CZ  
1017 N N   . TRP A 128 ? 0.2364 0.2720 0.4179 -0.0174 0.0210  0.0083  130 TRP A N   
1018 C CA  . TRP A 128 ? 0.2367 0.2685 0.4086 -0.0186 0.0204  0.0042  130 TRP A CA  
1019 C C   . TRP A 128 ? 0.2355 0.2647 0.4114 -0.0186 0.0207  0.0080  130 TRP A C   
1020 O O   . TRP A 128 ? 0.2149 0.2411 0.3799 -0.0179 0.0187  0.0093  130 TRP A O   
1021 C CB  . TRP A 128 ? 0.2541 0.2859 0.4289 -0.0217 0.0221  -0.0042 130 TRP A CB  
1022 C CG  . TRP A 128 ? 0.2643 0.2929 0.4295 -0.0230 0.0227  -0.0080 130 TRP A CG  
1023 C CD1 . TRP A 128 ? 0.2969 0.3242 0.4686 -0.0254 0.0264  -0.0130 130 TRP A CD1 
1024 C CD2 . TRP A 128 ? 0.2670 0.2935 0.4156 -0.0220 0.0204  -0.0069 130 TRP A CD2 
1025 N NE1 . TRP A 128 ? 0.3024 0.3276 0.4620 -0.0262 0.0268  -0.0148 130 TRP A NE1 
1026 C CE2 . TRP A 128 ? 0.3068 0.3312 0.4525 -0.0243 0.0228  -0.0109 130 TRP A CE2 
1027 C CE3 . TRP A 128 ? 0.2750 0.3009 0.4120 -0.0194 0.0169  -0.0033 130 TRP A CE3 
1028 C CZ2 . TRP A 128 ? 0.3233 0.3452 0.4554 -0.0244 0.0215  -0.0102 130 TRP A CZ2 
1029 C CZ3 . TRP A 128 ? 0.3122 0.3348 0.4362 -0.0193 0.0153  -0.0032 130 TRP A CZ3 
1030 C CH2 . TRP A 128 ? 0.3221 0.3429 0.4440 -0.0219 0.0174  -0.0062 130 TRP A CH2 
1031 N N   . LEU A 129 ? 0.2131 0.2433 0.4057 -0.0195 0.0226  0.0102  131 LEU A N   
1032 C CA  . LEU A 129 ? 0.2260 0.2546 0.4245 -0.0194 0.0219  0.0150  131 LEU A CA  
1033 C C   . LEU A 129 ? 0.2408 0.2689 0.4280 -0.0170 0.0179  0.0223  131 LEU A C   
1034 O O   . LEU A 129 ? 0.2612 0.2867 0.4430 -0.0171 0.0154  0.0237  131 LEU A O   
1035 C CB  . LEU A 129 ? 0.2404 0.2705 0.4610 -0.0204 0.0243  0.0171  131 LEU A CB  
1036 C CG  . LEU A 129 ? 0.2731 0.3023 0.5033 -0.0204 0.0231  0.0228  131 LEU A CG  
1037 C CD1 . LEU A 129 ? 0.2791 0.3060 0.5065 -0.0216 0.0237  0.0184  131 LEU A CD1 
1038 C CD2 . LEU A 129 ? 0.2853 0.3156 0.5386 -0.0211 0.0256  0.0249  131 LEU A CD2 
1039 N N   . GLU A 130 ? 0.2397 0.2700 0.4230 -0.0150 0.0175  0.0266  132 GLU A N   
1040 C CA  . GLU A 130 ? 0.2642 0.2938 0.4348 -0.0126 0.0144  0.0327  132 GLU A CA  
1041 C C   . GLU A 130 ? 0.2677 0.2932 0.4202 -0.0117 0.0118  0.0288  132 GLU A C   
1042 O O   . GLU A 130 ? 0.2673 0.2898 0.4111 -0.0111 0.0081  0.0313  132 GLU A O   
1043 C CB  . GLU A 130 ? 0.3062 0.3395 0.4752 -0.0103 0.0162  0.0373  132 GLU A CB  
1044 C CG  . GLU A 130 ? 0.3677 0.4047 0.5544 -0.0110 0.0183  0.0437  132 GLU A CG  
1045 C CD  . GLU A 130 ? 0.4429 0.4790 0.6371 -0.0118 0.0158  0.0499  132 GLU A CD  
1046 O OE1 . GLU A 130 ? 0.3877 0.4217 0.5690 -0.0109 0.0118  0.0528  132 GLU A OE1 
1047 O OE2 . GLU A 130 ? 0.5526 0.5900 0.7667 -0.0135 0.0175  0.0518  132 GLU A OE2 
1048 N N   . THR A 131 ? 0.2358 0.2611 0.3837 -0.0118 0.0131  0.0230  133 THR A N   
1049 C CA  . THR A 131 ? 0.2406 0.2617 0.3735 -0.0112 0.0108  0.0197  133 THR A CA  
1050 C C   . THR A 131 ? 0.2534 0.2710 0.3874 -0.0135 0.0091  0.0187  133 THR A C   
1051 O O   . THR A 131 ? 0.2870 0.3005 0.4114 -0.0130 0.0056  0.0198  133 THR A O   
1052 C CB  . THR A 131 ? 0.2547 0.2772 0.3850 -0.0113 0.0122  0.0147  133 THR A CB  
1053 O OG1 . THR A 131 ? 0.2597 0.2863 0.3921 -0.0092 0.0137  0.0162  133 THR A OG1 
1054 C CG2 . THR A 131 ? 0.2711 0.2893 0.3872 -0.0104 0.0098  0.0124  133 THR A CG2 
1055 N N   . LEU A 132 ? 0.2425 0.2616 0.3892 -0.0162 0.0119  0.0163  134 LEU A N   
1056 C CA  . LEU A 132 ? 0.2609 0.2779 0.4118 -0.0185 0.0117  0.0154  134 LEU A CA  
1057 C C   . LEU A 132 ? 0.2751 0.2910 0.4294 -0.0183 0.0077  0.0213  134 LEU A C   
1058 O O   . LEU A 132 ? 0.2440 0.2567 0.3941 -0.0193 0.0048  0.0218  134 LEU A O   
1059 C CB  . LEU A 132 ? 0.2682 0.2874 0.4338 -0.0208 0.0166  0.0116  134 LEU A CB  
1060 C CG  . LEU A 132 ? 0.3016 0.3218 0.4633 -0.0218 0.0200  0.0049  134 LEU A CG  
1061 C CD1 . LEU A 132 ? 0.3068 0.3287 0.4835 -0.0239 0.0251  0.0003  134 LEU A CD1 
1062 C CD2 . LEU A 132 ? 0.3514 0.3690 0.4989 -0.0224 0.0192  0.0027  134 LEU A CD2 
1063 N N   . LEU A 133 ? 0.2679 0.2864 0.4291 -0.0172 0.0071  0.0262  135 LEU A N   
1064 C CA  . LEU A 133 ? 0.2866 0.3046 0.4495 -0.0171 0.0022  0.0327  135 LEU A CA  
1065 C C   . LEU A 133 ? 0.2979 0.3122 0.4415 -0.0155 -0.0030 0.0338  135 LEU A C   
1066 O O   . LEU A 133 ? 0.3004 0.3125 0.4422 -0.0165 -0.0082 0.0362  135 LEU A O   
1067 C CB  . LEU A 133 ? 0.2998 0.3218 0.4746 -0.0164 0.0028  0.0389  135 LEU A CB  
1068 C CG  . LEU A 133 ? 0.3470 0.3717 0.5436 -0.0179 0.0077  0.0377  135 LEU A CG  
1069 C CD1 . LEU A 133 ? 0.3575 0.3853 0.5657 -0.0171 0.0078  0.0446  135 LEU A CD1 
1070 C CD2 . LEU A 133 ? 0.3558 0.3798 0.5646 -0.0199 0.0079  0.0363  135 LEU A CD2 
1071 N N   . CYS A 134 ? 0.3171 0.3306 0.4477 -0.0131 -0.0017 0.0316  136 CYS A N   
1072 C CA  . CYS A 134 ? 0.3274 0.3360 0.4392 -0.0112 -0.0055 0.0306  136 CYS A CA  
1073 C C   . CYS A 134 ? 0.3316 0.3352 0.4395 -0.0129 -0.0083 0.0271  136 CYS A C   
1074 O O   . CYS A 134 ? 0.3796 0.3786 0.4782 -0.0129 -0.0137 0.0275  136 CYS A O   
1075 C CB  . CYS A 134 ? 0.3448 0.3539 0.4465 -0.0080 -0.0024 0.0284  136 CYS A CB  
1076 S SG  . CYS A 134 ? 0.4036 0.4181 0.5062 -0.0054 0.0006  0.0339  136 CYS A SG  
1077 N N   . LEU A 135 ? 0.2859 0.2900 0.3994 -0.0145 -0.0048 0.0234  137 LEU A N   
1078 C CA  . LEU A 135 ? 0.3148 0.3146 0.4257 -0.0164 -0.0062 0.0208  137 LEU A CA  
1079 C C   . LEU A 135 ? 0.3128 0.3124 0.4342 -0.0193 -0.0093 0.0235  137 LEU A C   
1080 O O   . LEU A 135 ? 0.3267 0.3218 0.4426 -0.0200 -0.0147 0.0242  137 LEU A O   
1081 C CB  . LEU A 135 ? 0.2999 0.3014 0.4136 -0.0175 -0.0011 0.0170  137 LEU A CB  
1082 C CG  . LEU A 135 ? 0.3290 0.3285 0.4303 -0.0154 -0.0005 0.0143  137 LEU A CG  
1083 C CD1 . LEU A 135 ? 0.3433 0.3439 0.4382 -0.0117 -0.0008 0.0151  137 LEU A CD1 
1084 C CD2 . LEU A 135 ? 0.3675 0.3698 0.4721 -0.0171 0.0038  0.0113  137 LEU A CD2 
1085 N N   . ILE A 136 ? 0.2831 0.2873 0.4205 -0.0209 -0.0062 0.0249  138 ILE A N   
1086 C CA  . ILE A 136 ? 0.3128 0.3176 0.4635 -0.0237 -0.0081 0.0273  138 ILE A CA  
1087 C C   . ILE A 136 ? 0.3305 0.3345 0.4809 -0.0236 -0.0159 0.0325  138 ILE A C   
1088 O O   . ILE A 136 ? 0.3584 0.3612 0.5148 -0.0259 -0.0203 0.0343  138 ILE A O   
1089 C CB  . ILE A 136 ? 0.3006 0.3102 0.4702 -0.0251 -0.0019 0.0268  138 ILE A CB  
1090 C CG1 . ILE A 136 ? 0.3111 0.3247 0.4904 -0.0237 -0.0013 0.0302  138 ILE A CG1 
1091 C CG2 . ILE A 136 ? 0.3192 0.3292 0.4855 -0.0255 0.0052  0.0208  138 ILE A CG2 
1092 C CD1 . ILE A 136 ? 0.3272 0.3447 0.5276 -0.0248 0.0043  0.0296  138 ILE A CD1 
1093 N N   . GLY A 137 ? 0.3248 0.3301 0.4690 -0.0213 -0.0173 0.0351  139 GLY A N   
1094 C CA  . GLY A 137 ? 0.3575 0.3626 0.4980 -0.0211 -0.0246 0.0403  139 GLY A CA  
1095 C C   . GLY A 137 ? 0.3872 0.3861 0.5075 -0.0203 -0.0308 0.0384  139 GLY A C   
1096 O O   . GLY A 137 ? 0.3997 0.3981 0.5145 -0.0205 -0.0377 0.0421  139 GLY A O   
1097 N N   . GLU A 138 ? 0.3649 0.3591 0.4744 -0.0195 -0.0288 0.0327  140 GLU A N   
1098 C CA  . GLU A 138 ? 0.3826 0.3697 0.4742 -0.0184 -0.0336 0.0294  140 GLU A CA  
1099 C C   . GLU A 138 ? 0.4083 0.3951 0.4846 -0.0153 -0.0352 0.0306  140 GLU A C   
1100 O O   . GLU A 138 ? 0.4150 0.3982 0.4810 -0.0156 -0.0422 0.0310  140 GLU A O   
1101 C CB  . GLU A 138 ? 0.4055 0.3884 0.5002 -0.0219 -0.0415 0.0296  140 GLU A CB  
1102 C CG  . GLU A 138 ? 0.4824 0.4658 0.5922 -0.0250 -0.0391 0.0290  140 GLU A CG  
1103 C CD  . GLU A 138 ? 0.5452 0.5238 0.6484 -0.0246 -0.0355 0.0244  140 GLU A CD  
1104 O OE1 . GLU A 138 ? 0.6377 0.6091 0.7267 -0.0233 -0.0393 0.0212  140 GLU A OE1 
1105 O OE2 . GLU A 138 ? 0.5212 0.5027 0.6331 -0.0255 -0.0292 0.0240  140 GLU A OE2 
1106 N N   . SER A 139 ? 0.4095 0.4004 0.4843 -0.0124 -0.0285 0.0311  141 SER A N   
1107 C CA  . SER A 139 ? 0.4150 0.4082 0.4793 -0.0094 -0.0275 0.0340  141 SER A CA  
1108 C C   . SER A 139 ? 0.4189 0.4066 0.4625 -0.0060 -0.0276 0.0295  141 SER A C   
1109 O O   . SER A 139 ? 0.4366 0.4260 0.4695 -0.0033 -0.0261 0.0317  141 SER A O   
1110 C CB  . SER A 139 ? 0.4505 0.4504 0.5246 -0.0079 -0.0197 0.0363  141 SER A CB  
1111 O OG  . SER A 139 ? 0.4897 0.4943 0.5833 -0.0107 -0.0191 0.0401  141 SER A OG  
1112 N N   . PHE A 140 ? 0.4148 0.3959 0.4531 -0.0058 -0.0287 0.0235  142 PHE A N   
1113 C CA  . PHE A 140 ? 0.4303 0.4053 0.4513 -0.0022 -0.0281 0.0183  142 PHE A CA  
1114 C C   . PHE A 140 ? 0.4598 0.4262 0.4689 -0.0034 -0.0363 0.0146  142 PHE A C   
1115 O O   . PHE A 140 ? 0.4574 0.4164 0.4553 -0.0012 -0.0366 0.0085  142 PHE A O   
1116 C CB  . PHE A 140 ? 0.4085 0.3818 0.4335 -0.0008 -0.0234 0.0143  142 PHE A CB  
1117 C CG  . PHE A 140 ? 0.3725 0.3539 0.4093 -0.0002 -0.0167 0.0170  142 PHE A CG  
1118 C CD1 . PHE A 140 ? 0.3767 0.3637 0.4117 0.0028  -0.0117 0.0195  142 PHE A CD1 
1119 C CD2 . PHE A 140 ? 0.3714 0.3553 0.4220 -0.0032 -0.0155 0.0175  142 PHE A CD2 
1120 C CE1 . PHE A 140 ? 0.3892 0.3836 0.4370 0.0027  -0.0063 0.0217  142 PHE A CE1 
1121 C CE2 . PHE A 140 ? 0.3751 0.3659 0.4358 -0.0031 -0.0100 0.0189  142 PHE A CE2 
1122 C CZ  . PHE A 140 ? 0.3621 0.3578 0.4219 -0.0003 -0.0059 0.0208  142 PHE A CZ  
1123 N N   . ASP A 141 ? 0.4976 0.4649 0.5106 -0.0072 -0.0434 0.0181  143 ASP A N   
1124 C CA  . ASP A 141 ? 0.5515 0.5113 0.5543 -0.0093 -0.0529 0.0150  143 ASP A CA  
1125 C C   . ASP A 141 ? 0.5645 0.5157 0.5703 -0.0107 -0.0551 0.0089  143 ASP A C   
1126 O O   . ASP A 141 ? 0.5702 0.5241 0.5920 -0.0126 -0.0521 0.0106  143 ASP A O   
1127 C CB  . ASP A 141 ? 0.6247 0.5818 0.6044 -0.0059 -0.0539 0.0128  143 ASP A CB  
1128 C CG  . ASP A 141 ? 0.8104 0.7755 0.7888 -0.0062 -0.0545 0.0208  143 ASP A CG  
1129 O OD1 . ASP A 141 ? 0.8427 0.8110 0.8316 -0.0103 -0.0616 0.0263  143 ASP A OD1 
1130 O OD2 . ASP A 141 ? 0.8746 0.8433 0.8430 -0.0023 -0.0479 0.0224  143 ASP A OD2 
1131 N N   . ASP A 142 ? 0.5739 0.5152 0.5656 -0.0099 -0.0598 0.0022  144 ASP A N   
1132 C CA  . ASP A 142 ? 0.5766 0.5096 0.5734 -0.0115 -0.0618 -0.0025 144 ASP A CA  
1133 C C   . ASP A 142 ? 0.5289 0.4628 0.5308 -0.0084 -0.0529 -0.0032 144 ASP A C   
1134 O O   . ASP A 142 ? 0.5210 0.4514 0.5326 -0.0104 -0.0531 -0.0037 144 ASP A O   
1135 C CB  . ASP A 142 ? 0.6556 0.5768 0.6362 -0.0107 -0.0679 -0.0105 144 ASP A CB  
1136 C CG  . ASP A 142 ? 0.8074 0.7257 0.7831 -0.0148 -0.0793 -0.0111 144 ASP A CG  
1137 O OD1 . ASP A 142 ? 0.8261 0.7522 0.8120 -0.0182 -0.0827 -0.0042 144 ASP A OD1 
1138 O OD2 . ASP A 142 ? 0.8662 0.7739 0.8281 -0.0147 -0.0852 -0.0188 144 ASP A OD2 
1139 N N   . TYR A 143 ? 0.4843 0.4227 0.4799 -0.0037 -0.0456 -0.0029 145 TYR A N   
1140 C CA  . TYR A 143 ? 0.4743 0.4144 0.4749 -0.0007 -0.0381 -0.0033 145 TYR A CA  
1141 C C   . TYR A 143 ? 0.4442 0.3926 0.4618 -0.0035 -0.0346 0.0021  145 TYR A C   
1142 O O   . TYR A 143 ? 0.4364 0.3864 0.4588 -0.0021 -0.0298 0.0022  145 TYR A O   
1143 C CB  . TYR A 143 ? 0.5044 0.4473 0.4949 0.0049  -0.0317 -0.0045 145 TYR A CB  
1144 C CG  . TYR A 143 ? 0.5565 0.4906 0.5294 0.0082  -0.0335 -0.0111 145 TYR A CG  
1145 C CD1 . TYR A 143 ? 0.5812 0.5040 0.5509 0.0081  -0.0377 -0.0172 145 TYR A CD1 
1146 C CD2 . TYR A 143 ? 0.5952 0.5320 0.5545 0.0113  -0.0309 -0.0114 145 TYR A CD2 
1147 C CE1 . TYR A 143 ? 0.6134 0.5271 0.5670 0.0114  -0.0391 -0.0246 145 TYR A CE1 
1148 C CE2 . TYR A 143 ? 0.6267 0.5552 0.5681 0.0146  -0.0318 -0.0185 145 TYR A CE2 
1149 C CZ  . TYR A 143 ? 0.6544 0.5710 0.5931 0.0147  -0.0359 -0.0258 145 TYR A CZ  
1150 O OH  . TYR A 143 ? 0.7290 0.6359 0.6504 0.0178  -0.0369 -0.0343 145 TYR A OH  
1151 N N   . SER A 144 ? 0.4269 0.3805 0.4537 -0.0074 -0.0370 0.0065  146 SER A N   
1152 C CA  . SER A 144 ? 0.4086 0.3685 0.4513 -0.0103 -0.0338 0.0102  146 SER A CA  
1153 C C   . SER A 144 ? 0.3973 0.3525 0.4459 -0.0127 -0.0345 0.0090  146 SER A C   
1154 O O   . SER A 144 ? 0.3749 0.3345 0.4321 -0.0137 -0.0296 0.0106  146 SER A O   
1155 C CB  . SER A 144 ? 0.4434 0.4087 0.4963 -0.0137 -0.0367 0.0147  146 SER A CB  
1156 O OG  . SER A 144 ? 0.5224 0.4943 0.5742 -0.0117 -0.0338 0.0178  146 SER A OG  
1157 N N   . ASP A 145 ? 0.3968 0.3430 0.4407 -0.0138 -0.0404 0.0061  147 ASP A N   
1158 C CA  . ASP A 145 ? 0.4077 0.3491 0.4575 -0.0159 -0.0408 0.0059  147 ASP A CA  
1159 C C   . ASP A 145 ? 0.4033 0.3434 0.4490 -0.0124 -0.0356 0.0047  147 ASP A C   
1160 O O   . ASP A 145 ? 0.4378 0.3768 0.4898 -0.0143 -0.0341 0.0066  147 ASP A O   
1161 C CB  . ASP A 145 ? 0.4658 0.3966 0.5122 -0.0177 -0.0486 0.0027  147 ASP A CB  
1162 C CG  . ASP A 145 ? 0.5700 0.5021 0.6240 -0.0224 -0.0552 0.0048  147 ASP A CG  
1163 O OD1 . ASP A 145 ? 0.5444 0.4852 0.6106 -0.0248 -0.0528 0.0095  147 ASP A OD1 
1164 O OD2 . ASP A 145 ? 0.6554 0.5799 0.7040 -0.0237 -0.0630 0.0014  147 ASP A OD2 
1165 N N   . ASP A 146 ? 0.3569 0.2975 0.3931 -0.0075 -0.0328 0.0023  148 ASP A N   
1166 C CA  . ASP A 146 ? 0.3514 0.2921 0.3861 -0.0039 -0.0283 0.0019  148 ASP A CA  
1167 C C   . ASP A 146 ? 0.3551 0.3059 0.3967 -0.0045 -0.0228 0.0053  148 ASP A C   
1168 O O   . ASP A 146 ? 0.3761 0.3279 0.4176 -0.0024 -0.0201 0.0057  148 ASP A O   
1169 C CB  . ASP A 146 ? 0.3901 0.3283 0.4142 0.0018  -0.0268 -0.0019 148 ASP A CB  
1170 C CG  . ASP A 146 ? 0.5348 0.4611 0.5517 0.0035  -0.0308 -0.0067 148 ASP A CG  
1171 O OD1 . ASP A 146 ? 0.6003 0.5212 0.6138 0.0009  -0.0363 -0.0089 148 ASP A OD1 
1172 O OD2 . ASP A 146 ? 0.5396 0.4619 0.5552 0.0075  -0.0287 -0.0084 148 ASP A OD2 
1173 N N   . VAL A 147 ? 0.3416 0.2994 0.3894 -0.0071 -0.0216 0.0075  149 VAL A N   
1174 C CA  . VAL A 147 ? 0.3062 0.2728 0.3606 -0.0077 -0.0165 0.0094  149 VAL A CA  
1175 C C   . VAL A 147 ? 0.3191 0.2859 0.3799 -0.0115 -0.0156 0.0110  149 VAL A C   
1176 O O   . VAL A 147 ? 0.3338 0.2982 0.3996 -0.0149 -0.0179 0.0121  149 VAL A O   
1177 C CB  . VAL A 147 ? 0.3251 0.2983 0.3850 -0.0087 -0.0153 0.0110  149 VAL A CB  
1178 C CG1 . VAL A 147 ? 0.3278 0.3088 0.3968 -0.0103 -0.0103 0.0120  149 VAL A CG1 
1179 C CG2 . VAL A 147 ? 0.3338 0.3078 0.3862 -0.0048 -0.0150 0.0104  149 VAL A CG2 
1180 N N   . CYS A 148 ? 0.2693 0.2394 0.3299 -0.0109 -0.0123 0.0113  150 CYS A N   
1181 C CA  . CYS A 148 ? 0.2713 0.2433 0.3358 -0.0144 -0.0100 0.0131  150 CYS A CA  
1182 C C   . CYS A 148 ? 0.2803 0.2607 0.3519 -0.0166 -0.0055 0.0126  150 CYS A C   
1183 O O   . CYS A 148 ? 0.2774 0.2593 0.3551 -0.0202 -0.0033 0.0135  150 CYS A O   
1184 C CB  . CYS A 148 ? 0.2940 0.2647 0.3528 -0.0127 -0.0099 0.0139  150 CYS A CB  
1185 S SG  . CYS A 148 ? 0.3668 0.3267 0.4205 -0.0103 -0.0146 0.0143  150 CYS A SG  
1186 N N   . GLY A 149 ? 0.2691 0.2545 0.3408 -0.0144 -0.0037 0.0111  151 GLY A N   
1187 C CA  . GLY A 149 ? 0.2550 0.2473 0.3339 -0.0163 0.0004  0.0099  151 GLY A CA  
1188 C C   . GLY A 149 ? 0.2536 0.2505 0.3325 -0.0137 0.0014  0.0086  151 GLY A C   
1189 O O   . GLY A 149 ? 0.2631 0.2585 0.3375 -0.0102 -0.0004 0.0091  151 GLY A O   
1190 N N   . ALA A 150 ? 0.2457 0.2482 0.3310 -0.0154 0.0047  0.0066  152 ALA A N   
1191 C CA  . ALA A 150 ? 0.2507 0.2584 0.3393 -0.0139 0.0058  0.0053  152 ALA A CA  
1192 C C   . ALA A 150 ? 0.2597 0.2712 0.3491 -0.0164 0.0078  0.0019  152 ALA A C   
1193 O O   . ALA A 150 ? 0.2436 0.2547 0.3334 -0.0195 0.0102  0.0002  152 ALA A O   
1194 C CB  . ALA A 150 ? 0.2536 0.2639 0.3518 -0.0137 0.0073  0.0063  152 ALA A CB  
1195 N N   . VAL A 151 ? 0.2381 0.2535 0.3276 -0.0151 0.0070  0.0008  153 VAL A N   
1196 C CA  . VAL A 151 ? 0.2316 0.2507 0.3201 -0.0175 0.0073  -0.0029 153 VAL A CA  
1197 C C   . VAL A 151 ? 0.2533 0.2777 0.3516 -0.0174 0.0078  -0.0049 153 VAL A C   
1198 O O   . VAL A 151 ? 0.2391 0.2652 0.3407 -0.0143 0.0067  -0.0022 153 VAL A O   
1199 C CB  . VAL A 151 ? 0.2620 0.2804 0.3399 -0.0166 0.0037  -0.0014 153 VAL A CB  
1200 C CG1 . VAL A 151 ? 0.2821 0.3049 0.3572 -0.0193 0.0028  -0.0052 153 VAL A CG1 
1201 C CG2 . VAL A 151 ? 0.2603 0.2729 0.3297 -0.0169 0.0030  0.0015  153 VAL A CG2 
1202 N N   . VAL A 152 ? 0.2588 0.2858 0.3623 -0.0206 0.0099  -0.0097 154 VAL A N   
1203 C CA  . VAL A 152 ? 0.2537 0.2855 0.3666 -0.0213 0.0094  -0.0126 154 VAL A CA  
1204 C C   . VAL A 152 ? 0.2665 0.3008 0.3727 -0.0239 0.0068  -0.0174 154 VAL A C   
1205 O O   . VAL A 152 ? 0.2649 0.2977 0.3645 -0.0268 0.0086  -0.0214 154 VAL A O   
1206 C CB  . VAL A 152 ? 0.2589 0.2914 0.3866 -0.0229 0.0134  -0.0147 154 VAL A CB  
1207 C CG1 . VAL A 152 ? 0.2768 0.3068 0.4046 -0.0258 0.0172  -0.0194 154 VAL A CG1 
1208 C CG2 . VAL A 152 ? 0.2768 0.3139 0.4155 -0.0240 0.0125  -0.0176 154 VAL A CG2 
1209 N N   . ASN A 153 ? 0.2768 0.3152 0.3842 -0.0229 0.0025  -0.0165 155 ASN A N   
1210 C CA  . ASN A 153 ? 0.2965 0.3381 0.3981 -0.0254 -0.0017 -0.0204 155 ASN A CA  
1211 C C   . ASN A 153 ? 0.3152 0.3612 0.4308 -0.0277 -0.0022 -0.0252 155 ASN A C   
1212 O O   . ASN A 153 ? 0.3324 0.3819 0.4598 -0.0257 -0.0032 -0.0220 155 ASN A O   
1213 C CB  . ASN A 153 ? 0.3108 0.3547 0.4071 -0.0228 -0.0072 -0.0155 155 ASN A CB  
1214 C CG  . ASN A 153 ? 0.3604 0.3996 0.4467 -0.0199 -0.0072 -0.0100 155 ASN A CG  
1215 O OD1 . ASN A 153 ? 0.4105 0.4488 0.5001 -0.0158 -0.0072 -0.0053 155 ASN A OD1 
1216 N ND2 . ASN A 153 ? 0.3898 0.4258 0.4637 -0.0220 -0.0069 -0.0107 155 ASN A ND2 
1217 N N   . VAL A 154 ? 0.3277 0.3731 0.4421 -0.0317 -0.0011 -0.0328 156 VAL A N   
1218 C CA  . VAL A 154 ? 0.3861 0.4345 0.5143 -0.0345 -0.0020 -0.0386 156 VAL A CA  
1219 C C   . VAL A 154 ? 0.4138 0.4667 0.5360 -0.0367 -0.0096 -0.0415 156 VAL A C   
1220 O O   . VAL A 154 ? 0.4176 0.4696 0.5235 -0.0390 -0.0117 -0.0452 156 VAL A O   
1221 C CB  . VAL A 154 ? 0.4151 0.4598 0.5472 -0.0374 0.0036  -0.0463 156 VAL A CB  
1222 C CG1 . VAL A 154 ? 0.4568 0.5035 0.6062 -0.0402 0.0028  -0.0523 156 VAL A CG1 
1223 C CG2 . VAL A 154 ? 0.4256 0.4664 0.5628 -0.0351 0.0099  -0.0419 156 VAL A CG2 
1224 N N   . ARG A 155 ? 0.4194 0.4776 0.5548 -0.0360 -0.0138 -0.0392 157 ARG A N   
1225 C CA  . ARG A 155 ? 0.4413 0.5048 0.5734 -0.0378 -0.0223 -0.0405 157 ARG A CA  
1226 C C   . ARG A 155 ? 0.4912 0.5596 0.6430 -0.0402 -0.0255 -0.0437 157 ARG A C   
1227 O O   . ARG A 155 ? 0.4911 0.5602 0.6604 -0.0387 -0.0214 -0.0406 157 ARG A O   
1228 C CB  . ARG A 155 ? 0.4385 0.5051 0.5671 -0.0335 -0.0262 -0.0313 157 ARG A CB  
1229 C CG  . ARG A 155 ? 0.5114 0.5735 0.6215 -0.0313 -0.0251 -0.0273 157 ARG A CG  
1230 C CD  . ARG A 155 ? 0.5310 0.5921 0.6224 -0.0349 -0.0287 -0.0315 157 ARG A CD  
1231 N NE  . ARG A 155 ? 0.5681 0.6249 0.6445 -0.0326 -0.0271 -0.0259 157 ARG A NE  
1232 C CZ  . ARG A 155 ? 0.5801 0.6310 0.6496 -0.0325 -0.0202 -0.0263 157 ARG A CZ  
1233 N NH1 . ARG A 155 ? 0.5023 0.5510 0.5786 -0.0342 -0.0140 -0.0320 157 ARG A NH1 
1234 N NH2 . ARG A 155 ? 0.6324 0.6798 0.6902 -0.0307 -0.0197 -0.0206 157 ARG A NH2 
1235 N N   . ALA A 156 ? 0.5188 0.5907 0.6676 -0.0443 -0.0332 -0.0494 158 ALA A N   
1236 C CA  . ALA A 156 ? 0.5438 0.6207 0.7121 -0.0473 -0.0379 -0.0529 158 ALA A CA  
1237 C C   . ALA A 156 ? 0.5633 0.6465 0.7512 -0.0435 -0.0381 -0.0431 158 ALA A C   
1238 O O   . ALA A 156 ? 0.5759 0.6607 0.7844 -0.0441 -0.0353 -0.0428 158 ALA A O   
1239 C CB  . ALA A 156 ? 0.5450 0.6253 0.7037 -0.0520 -0.0482 -0.0593 158 ALA A CB  
1240 N N   . LYS A 157 ? 0.5680 0.6545 0.7498 -0.0394 -0.0409 -0.0351 159 LYS A N   
1241 C CA  . LYS A 157 ? 0.5604 0.6533 0.7594 -0.0352 -0.0404 -0.0262 159 LYS A CA  
1242 C C   . LYS A 157 ? 0.5419 0.6320 0.7479 -0.0307 -0.0303 -0.0202 159 LYS A C   
1243 O O   . LYS A 157 ? 0.5423 0.6378 0.7641 -0.0277 -0.0282 -0.0137 159 LYS A O   
1244 C CB  . LYS A 157 ? 0.6285 0.7245 0.8181 -0.0316 -0.0456 -0.0200 159 LYS A CB  
1245 C CG  . LYS A 157 ? 0.7562 0.8610 0.9661 -0.0282 -0.0474 -0.0126 159 LYS A CG  
1246 C CD  . LYS A 157 ? 0.8503 0.9584 1.0538 -0.0248 -0.0537 -0.0068 159 LYS A CD  
1247 C CE  . LYS A 157 ? 0.8969 1.0157 1.1236 -0.0233 -0.0581 -0.0016 159 LYS A CE  
1248 N NZ  . LYS A 157 ? 0.9283 1.0533 1.1633 -0.0296 -0.0687 -0.0067 159 LYS A NZ  
1249 N N   . GLY A 158 ? 0.4977 0.5801 0.6920 -0.0302 -0.0242 -0.0220 160 GLY A N   
1250 C CA  . GLY A 158 ? 0.4487 0.5284 0.6471 -0.0263 -0.0160 -0.0162 160 GLY A CA  
1251 C C   . GLY A 158 ? 0.4368 0.5090 0.6162 -0.0244 -0.0124 -0.0158 160 GLY A C   
1252 O O   . GLY A 158 ? 0.4852 0.5557 0.6491 -0.0234 -0.0157 -0.0155 160 GLY A O   
1253 N N   . ASP A 159 ? 0.3666 0.4345 0.5481 -0.0239 -0.0062 -0.0151 161 ASP A N   
1254 C CA  . ASP A 159 ? 0.3442 0.4050 0.5104 -0.0231 -0.0031 -0.0157 161 ASP A CA  
1255 C C   . ASP A 159 ? 0.3141 0.3734 0.4737 -0.0178 -0.0010 -0.0083 161 ASP A C   
1256 O O   . ASP A 159 ? 0.3291 0.3920 0.4974 -0.0147 0.0005  -0.0031 161 ASP A O   
1257 C CB  . ASP A 159 ? 0.3619 0.4191 0.5359 -0.0251 0.0019  -0.0182 161 ASP A CB  
1258 C CG  . ASP A 159 ? 0.5372 0.5951 0.7207 -0.0302 0.0008  -0.0266 161 ASP A CG  
1259 O OD1 . ASP A 159 ? 0.5697 0.6269 0.7427 -0.0331 -0.0027 -0.0333 161 ASP A OD1 
1260 O OD2 . ASP A 159 ? 0.5658 0.6245 0.7668 -0.0313 0.0033  -0.0264 161 ASP A OD2 
1261 N N   . LYS A 160 ? 0.2987 0.3524 0.4428 -0.0168 -0.0007 -0.0080 162 LYS A N   
1262 C CA  . LYS A 160 ? 0.2768 0.3276 0.4134 -0.0121 0.0006  -0.0024 162 LYS A CA  
1263 C C   . LYS A 160 ? 0.2556 0.2999 0.3853 -0.0125 0.0039  -0.0025 162 LYS A C   
1264 O O   . LYS A 160 ? 0.2716 0.3133 0.3965 -0.0158 0.0039  -0.0066 162 LYS A O   
1265 C CB  . LYS A 160 ? 0.3225 0.3726 0.4479 -0.0106 -0.0039 -0.0015 162 LYS A CB  
1266 C CG  . LYS A 160 ? 0.4327 0.4896 0.5652 -0.0096 -0.0083 -0.0003 162 LYS A CG  
1267 C CD  . LYS A 160 ? 0.6052 0.6602 0.7287 -0.0060 -0.0113 0.0034  162 LYS A CD  
1268 C CE  . LYS A 160 ? 0.7448 0.8037 0.8664 -0.0070 -0.0184 0.0036  162 LYS A CE  
1269 N NZ  . LYS A 160 ? 0.8309 0.8858 0.9438 -0.0030 -0.0204 0.0081  162 LYS A NZ  
1270 N N   . ILE A 161 ? 0.2243 0.2664 0.3539 -0.0094 0.0067  0.0019  163 ILE A N   
1271 C CA  . ILE A 161 ? 0.2290 0.2652 0.3523 -0.0095 0.0084  0.0027  163 ILE A CA  
1272 C C   . ILE A 161 ? 0.2329 0.2654 0.3459 -0.0055 0.0075  0.0060  163 ILE A C   
1273 O O   . ILE A 161 ? 0.2513 0.2862 0.3661 -0.0019 0.0083  0.0088  163 ILE A O   
1274 C CB  . ILE A 161 ? 0.2759 0.3125 0.4090 -0.0102 0.0117  0.0046  163 ILE A CB  
1275 C CG1 . ILE A 161 ? 0.3197 0.3593 0.4658 -0.0141 0.0129  0.0007  163 ILE A CG1 
1276 C CG2 . ILE A 161 ? 0.2870 0.3179 0.4137 -0.0104 0.0121  0.0058  163 ILE A CG2 
1277 C CD1 . ILE A 161 ? 0.3570 0.3978 0.5165 -0.0146 0.0159  0.0034  163 ILE A CD1 
1278 N N   . ALA A 162 ? 0.2557 0.2823 0.3587 -0.0060 0.0062  0.0055  164 ALA A N   
1279 C CA  . ALA A 162 ? 0.2505 0.2721 0.3437 -0.0024 0.0048  0.0076  164 ALA A CA  
1280 C C   . ALA A 162 ? 0.2649 0.2799 0.3522 -0.0035 0.0044  0.0080  164 ALA A C   
1281 O O   . ALA A 162 ? 0.2569 0.2710 0.3452 -0.0072 0.0046  0.0064  164 ALA A O   
1282 C CB  . ALA A 162 ? 0.2716 0.2926 0.3594 -0.0017 0.0017  0.0072  164 ALA A CB  
1283 N N   . ILE A 163 ? 0.2622 0.2729 0.3437 -0.0005 0.0039  0.0097  165 ILE A N   
1284 C CA  . ILE A 163 ? 0.2535 0.2572 0.3286 -0.0014 0.0019  0.0098  165 ILE A CA  
1285 C C   . ILE A 163 ? 0.2652 0.2632 0.3321 0.0006  -0.0007 0.0094  165 ILE A C   
1286 O O   . ILE A 163 ? 0.2622 0.2594 0.3261 0.0048  -0.0006 0.0095  165 ILE A O   
1287 C CB  . ILE A 163 ? 0.2645 0.2662 0.3375 -0.0001 0.0018  0.0115  165 ILE A CB  
1288 C CG1 . ILE A 163 ? 0.2985 0.3054 0.3817 -0.0026 0.0038  0.0131  165 ILE A CG1 
1289 C CG2 . ILE A 163 ? 0.2828 0.2766 0.3487 -0.0009 -0.0018 0.0110  165 ILE A CG2 
1290 C CD1 . ILE A 163 ? 0.3451 0.3510 0.4263 -0.0017 0.0031  0.0161  165 ILE A CD1 
1291 N N   . TRP A 164 ? 0.2568 0.2509 0.3214 -0.0023 -0.0024 0.0092  166 TRP A N   
1292 C CA  . TRP A 164 ? 0.2446 0.2327 0.3031 -0.0011 -0.0051 0.0098  166 TRP A CA  
1293 C C   . TRP A 164 ? 0.2683 0.2479 0.3224 -0.0008 -0.0075 0.0095  166 TRP A C   
1294 O O   . TRP A 164 ? 0.2765 0.2551 0.3327 -0.0038 -0.0080 0.0097  166 TRP A O   
1295 C CB  . TRP A 164 ? 0.2607 0.2495 0.3192 -0.0049 -0.0053 0.0106  166 TRP A CB  
1296 C CG  . TRP A 164 ? 0.2822 0.2777 0.3421 -0.0055 -0.0046 0.0103  166 TRP A CG  
1297 C CD1 . TRP A 164 ? 0.2786 0.2811 0.3439 -0.0049 -0.0031 0.0088  166 TRP A CD1 
1298 C CD2 . TRP A 164 ? 0.3029 0.2988 0.3585 -0.0072 -0.0061 0.0119  166 TRP A CD2 
1299 N NE1 . TRP A 164 ? 0.2797 0.2867 0.3443 -0.0059 -0.0043 0.0087  166 TRP A NE1 
1300 C CE2 . TRP A 164 ? 0.3061 0.3093 0.3637 -0.0076 -0.0061 0.0106  166 TRP A CE2 
1301 C CE3 . TRP A 164 ? 0.3143 0.3051 0.3646 -0.0088 -0.0076 0.0147  166 TRP A CE3 
1302 C CZ2 . TRP A 164 ? 0.3378 0.3434 0.3906 -0.0093 -0.0082 0.0117  166 TRP A CZ2 
1303 C CZ3 . TRP A 164 ? 0.3473 0.3407 0.3929 -0.0105 -0.0088 0.0166  166 TRP A CZ3 
1304 C CH2 . TRP A 164 ? 0.3457 0.3464 0.3916 -0.0107 -0.0094 0.0150  166 TRP A CH2 
1305 N N   . THR A 165 ? 0.2827 0.2564 0.3317 0.0028  -0.0093 0.0089  167 THR A N   
1306 C CA  . THR A 165 ? 0.3186 0.2833 0.3628 0.0033  -0.0123 0.0075  167 THR A CA  
1307 C C   . THR A 165 ? 0.3218 0.2791 0.3646 0.0037  -0.0149 0.0084  167 THR A C   
1308 O O   . THR A 165 ? 0.3158 0.2750 0.3599 0.0051  -0.0145 0.0103  167 THR A O   
1309 C CB  . THR A 165 ? 0.3735 0.3364 0.4122 0.0075  -0.0117 0.0049  167 THR A CB  
1310 O OG1 . THR A 165 ? 0.4256 0.3863 0.4624 0.0125  -0.0106 0.0038  167 THR A OG1 
1311 C CG2 . THR A 165 ? 0.4071 0.3785 0.4482 0.0078  -0.0084 0.0058  167 THR A CG2 
1312 N N   . THR A 166 ? 0.3274 0.2762 0.3683 0.0022  -0.0183 0.0074  168 THR A N   
1313 C CA  . THR A 166 ? 0.3353 0.2769 0.3776 0.0008  -0.0209 0.0093  168 THR A CA  
1314 C C   . THR A 166 ? 0.3545 0.2880 0.3943 0.0057  -0.0225 0.0078  168 THR A C   
1315 O O   . THR A 166 ? 0.3666 0.2962 0.4091 0.0053  -0.0240 0.0112  168 THR A O   
1316 C CB  . THR A 166 ? 0.3905 0.3265 0.4350 -0.0038 -0.0242 0.0093  168 THR A CB  
1317 O OG1 . THR A 166 ? 0.3763 0.3075 0.4245 -0.0064 -0.0256 0.0130  168 THR A OG1 
1318 C CG2 . THR A 166 ? 0.4074 0.3358 0.4472 -0.0022 -0.0278 0.0046  168 THR A CG2 
1319 N N   . GLU A 167 ? 0.3679 0.2991 0.4030 0.0104  -0.0217 0.0032  169 GLU A N   
1320 C CA  . GLU A 167 ? 0.3958 0.3175 0.4292 0.0152  -0.0229 0.0003  169 GLU A CA  
1321 C C   . GLU A 167 ? 0.4134 0.3379 0.4437 0.0213  -0.0190 -0.0029 169 GLU A C   
1322 O O   . GLU A 167 ? 0.4056 0.3302 0.4291 0.0226  -0.0176 -0.0070 169 GLU A O   
1323 C CB  . GLU A 167 ? 0.4490 0.3591 0.4788 0.0134  -0.0273 -0.0040 169 GLU A CB  
1324 C CG  . GLU A 167 ? 0.5228 0.4207 0.5513 0.0178  -0.0289 -0.0083 169 GLU A CG  
1325 C CD  . GLU A 167 ? 0.5764 0.4726 0.6130 0.0199  -0.0287 -0.0036 169 GLU A CD  
1326 O OE1 . GLU A 167 ? 0.5583 0.4519 0.6005 0.0156  -0.0315 0.0015  169 GLU A OE1 
1327 O OE2 . GLU A 167 ? 0.5647 0.4630 0.6026 0.0257  -0.0256 -0.0042 169 GLU A OE2 
1328 N N   . CYS A 168 ? 0.4501 0.3771 0.4856 0.0251  -0.0173 -0.0007 170 CYS A N   
1329 C CA  . CYS A 168 ? 0.4795 0.4087 0.5153 0.0318  -0.0130 -0.0033 170 CYS A CA  
1330 C C   . CYS A 168 ? 0.4916 0.4116 0.5201 0.0361  -0.0117 -0.0105 170 CYS A C   
1331 O O   . CYS A 168 ? 0.4990 0.4232 0.5231 0.0398  -0.0069 -0.0134 170 CYS A O   
1332 C CB  . CYS A 168 ? 0.5364 0.4663 0.5813 0.0351  -0.0135 0.0007  170 CYS A CB  
1333 S SG  . CYS A 168 ? 0.6543 0.5999 0.7060 0.0336  -0.0121 0.0065  170 CYS A SG  
1334 N N   . GLU A 169 ? 0.4678 0.3751 0.4949 0.0356  -0.0157 -0.0134 171 GLU A N   
1335 C CA  . GLU A 169 ? 0.4582 0.3547 0.4786 0.0401  -0.0149 -0.0215 171 GLU A CA  
1336 C C   . GLU A 169 ? 0.4694 0.3634 0.4769 0.0377  -0.0161 -0.0268 171 GLU A C   
1337 O O   . GLU A 169 ? 0.5055 0.3906 0.5041 0.0409  -0.0156 -0.0346 171 GLU A O   
1338 C CB  . GLU A 169 ? 0.5183 0.4012 0.5441 0.0407  -0.0191 -0.0229 171 GLU A CB  
1339 C CG  . GLU A 169 ? 0.5420 0.4272 0.5805 0.0439  -0.0183 -0.0168 171 GLU A CG  
1340 C CD  . GLU A 169 ? 0.5800 0.4727 0.6225 0.0509  -0.0120 -0.0170 171 GLU A CD  
1341 O OE1 . GLU A 169 ? 0.5616 0.4513 0.5977 0.0558  -0.0074 -0.0244 171 GLU A OE1 
1342 O OE2 . GLU A 169 ? 0.5946 0.4966 0.6467 0.0514  -0.0117 -0.0098 171 GLU A OE2 
1343 N N   . ASN A 170 ? 0.4409 0.3427 0.4470 0.0320  -0.0178 -0.0229 172 ASN A N   
1344 C CA  . ASN A 170 ? 0.4285 0.3292 0.4231 0.0297  -0.0197 -0.0266 172 ASN A CA  
1345 C C   . ASN A 170 ? 0.4391 0.3500 0.4283 0.0331  -0.0131 -0.0262 172 ASN A C   
1346 O O   . ASN A 170 ? 0.4169 0.3380 0.4082 0.0299  -0.0123 -0.0212 172 ASN A O   
1347 C CB  . ASN A 170 ? 0.4424 0.3462 0.4406 0.0222  -0.0247 -0.0223 172 ASN A CB  
1348 C CG  . ASN A 170 ? 0.5019 0.3949 0.5034 0.0182  -0.0314 -0.0235 172 ASN A CG  
1349 O OD1 . ASN A 170 ? 0.4911 0.3723 0.4908 0.0207  -0.0334 -0.0288 172 ASN A OD1 
1350 N ND2 . ASN A 170 ? 0.4776 0.3743 0.4852 0.0121  -0.0347 -0.0188 172 ASN A ND2 
1351 N N   . ARG A 171 ? 0.4296 0.3379 0.4134 0.0395  -0.0081 -0.0309 173 ARG A N   
1352 C CA  . ARG A 171 ? 0.4590 0.3778 0.4410 0.0436  -0.0002 -0.0293 173 ARG A CA  
1353 C C   . ARG A 171 ? 0.4880 0.4123 0.4596 0.0409  -0.0001 -0.0282 173 ARG A C   
1354 O O   . ARG A 171 ? 0.5062 0.4423 0.4820 0.0405  0.0040  -0.0226 173 ARG A O   
1355 C CB  . ARG A 171 ? 0.5484 0.4608 0.5251 0.0513  0.0054  -0.0363 173 ARG A CB  
1356 C CG  . ARG A 171 ? 0.6686 0.5901 0.6441 0.0569  0.0149  -0.0356 173 ARG A CG  
1357 C CD  . ARG A 171 ? 0.7864 0.6998 0.7597 0.0646  0.0203  -0.0431 173 ARG A CD  
1358 N NE  . ARG A 171 ? 0.8672 0.7685 0.8218 0.0655  0.0190  -0.0527 173 ARG A NE  
1359 C CZ  . ARG A 171 ? 0.9215 0.8119 0.8713 0.0714  0.0223  -0.0617 173 ARG A CZ  
1360 N NH1 . ARG A 171 ? 0.9208 0.8111 0.8852 0.0773  0.0273  -0.0617 173 ARG A NH1 
1361 N NH2 . ARG A 171 ? 0.9203 0.7997 0.8512 0.0714  0.0203  -0.0711 173 ARG A NH2 
1362 N N   . GLU A 172 ? 0.4959 0.4116 0.4543 0.0387  -0.0052 -0.0333 174 GLU A N   
1363 C CA  . GLU A 172 ? 0.5204 0.4405 0.4677 0.0362  -0.0062 -0.0318 174 GLU A CA  
1364 C C   . GLU A 172 ? 0.4694 0.3978 0.4273 0.0300  -0.0099 -0.0240 174 GLU A C   
1365 O O   . GLU A 172 ? 0.4816 0.4193 0.4388 0.0293  -0.0072 -0.0191 174 GLU A O   
1366 C CB  . GLU A 172 ? 0.6066 0.5154 0.5373 0.0350  -0.0123 -0.0392 174 GLU A CB  
1367 C CG  . GLU A 172 ? 0.7596 0.6609 0.6772 0.0419  -0.0068 -0.0480 174 GLU A CG  
1368 C CD  . GLU A 172 ? 0.9260 0.8363 0.8381 0.0476  0.0041  -0.0465 174 GLU A CD  
1369 O OE1 . GLU A 172 ? 0.9236 0.8431 0.8300 0.0459  0.0056  -0.0410 174 GLU A OE1 
1370 O OE2 . GLU A 172 ? 0.9750 0.8834 0.8902 0.0539  0.0112  -0.0503 174 GLU A OE2 
1371 N N   . ALA A 173 ? 0.4359 0.3608 0.4040 0.0258  -0.0155 -0.0226 175 ALA A N   
1372 C CA  . ALA A 173 ? 0.4294 0.3623 0.4086 0.0202  -0.0178 -0.0158 175 ALA A CA  
1373 C C   . ALA A 173 ? 0.4182 0.3626 0.4077 0.0216  -0.0112 -0.0105 175 ALA A C   
1374 O O   . ALA A 173 ? 0.4290 0.3819 0.4224 0.0193  -0.0101 -0.0058 175 ALA A O   
1375 C CB  . ALA A 173 ? 0.4291 0.3565 0.4173 0.0160  -0.0232 -0.0154 175 ALA A CB  
1376 N N   . VAL A 174 ? 0.3906 0.3353 0.3855 0.0254  -0.0074 -0.0112 176 VAL A N   
1377 C CA  . VAL A 174 ? 0.3989 0.3544 0.4052 0.0262  -0.0026 -0.0065 176 VAL A CA  
1378 C C   . VAL A 174 ? 0.3967 0.3600 0.3998 0.0288  0.0032  -0.0047 176 VAL A C   
1379 O O   . VAL A 174 ? 0.3637 0.3362 0.3746 0.0265  0.0050  0.0001  176 VAL A O   
1380 C CB  . VAL A 174 ? 0.4129 0.3662 0.4250 0.0302  -0.0008 -0.0076 176 VAL A CB  
1381 C CG1 . VAL A 174 ? 0.4330 0.3976 0.4556 0.0320  0.0040  -0.0035 176 VAL A CG1 
1382 C CG2 . VAL A 174 ? 0.4073 0.3541 0.4241 0.0269  -0.0063 -0.0071 176 VAL A CG2 
1383 N N   . THR A 175 ? 0.3919 0.3513 0.3834 0.0336  0.0065  -0.0087 177 THR A N   
1384 C CA  . THR A 175 ? 0.4253 0.3929 0.4136 0.0364  0.0131  -0.0061 177 THR A CA  
1385 C C   . THR A 175 ? 0.4054 0.3765 0.3891 0.0322  0.0107  -0.0021 177 THR A C   
1386 O O   . THR A 175 ? 0.3942 0.3750 0.3840 0.0319  0.0150  0.0034  177 THR A O   
1387 C CB  . THR A 175 ? 0.5016 0.4648 0.4785 0.0431  0.0188  -0.0114 177 THR A CB  
1388 O OG1 . THR A 175 ? 0.5663 0.5184 0.5274 0.0427  0.0143  -0.0175 177 THR A OG1 
1389 C CG2 . THR A 175 ? 0.5129 0.4747 0.4988 0.0476  0.0220  -0.0137 177 THR A CG2 
1390 N N   . HIS A 176 ? 0.4060 0.3700 0.3809 0.0288  0.0037  -0.0043 178 HIS A N   
1391 C CA  . HIS A 176 ? 0.4213 0.3889 0.3938 0.0247  0.0002  0.0003  178 HIS A CA  
1392 C C   . HIS A 176 ? 0.4072 0.3827 0.3975 0.0204  -0.0003 0.0064  178 HIS A C   
1393 O O   . HIS A 176 ? 0.3944 0.3775 0.3892 0.0191  0.0015  0.0122  178 HIS A O   
1394 C CB  . HIS A 176 ? 0.4647 0.4229 0.4274 0.0215  -0.0085 -0.0034 178 HIS A CB  
1395 C CG  . HIS A 176 ? 0.5318 0.4933 0.4924 0.0174  -0.0135 0.0016  178 HIS A CG  
1396 N ND1 . HIS A 176 ? 0.5647 0.5296 0.5399 0.0122  -0.0178 0.0060  178 HIS A ND1 
1397 C CD2 . HIS A 176 ? 0.5631 0.5250 0.5088 0.0178  -0.0149 0.0028  178 HIS A CD2 
1398 C CE1 . HIS A 176 ? 0.5650 0.5323 0.5357 0.0099  -0.0220 0.0102  178 HIS A CE1 
1399 N NE2 . HIS A 176 ? 0.5675 0.5333 0.5201 0.0129  -0.0207 0.0089  178 HIS A NE2 
1400 N N   . ILE A 177 ? 0.3778 0.3512 0.3782 0.0182  -0.0028 0.0051  179 ILE A N   
1401 C CA  . ILE A 177 ? 0.3567 0.3371 0.3731 0.0144  -0.0026 0.0094  179 ILE A CA  
1402 C C   . ILE A 177 ? 0.3410 0.3308 0.3659 0.0165  0.0041  0.0127  179 ILE A C   
1403 O O   . ILE A 177 ? 0.3517 0.3481 0.3861 0.0139  0.0051  0.0171  179 ILE A O   
1404 C CB  . ILE A 177 ? 0.3487 0.3249 0.3713 0.0123  -0.0053 0.0070  179 ILE A CB  
1405 C CG1 . ILE A 177 ? 0.3631 0.3315 0.3818 0.0089  -0.0120 0.0052  179 ILE A CG1 
1406 C CG2 . ILE A 177 ? 0.3153 0.2993 0.3527 0.0094  -0.0032 0.0100  179 ILE A CG2 
1407 C CD1 . ILE A 177 ? 0.3694 0.3320 0.3921 0.0075  -0.0144 0.0030  179 ILE A CD1 
1408 N N   . GLY A 178 ? 0.3534 0.3439 0.3768 0.0211  0.0086  0.0108  180 GLY A N   
1409 C CA  . GLY A 178 ? 0.3546 0.3544 0.3880 0.0230  0.0146  0.0141  180 GLY A CA  
1410 C C   . GLY A 178 ? 0.3729 0.3783 0.4046 0.0234  0.0183  0.0188  180 GLY A C   
1411 O O   . GLY A 178 ? 0.3661 0.3793 0.4104 0.0215  0.0206  0.0234  180 GLY A O   
1412 N N   . ARG A 179 ? 0.3936 0.3948 0.4093 0.0258  0.0187  0.0178  181 ARG A N   
1413 C CA  . ARG A 179 ? 0.4213 0.4279 0.4325 0.0264  0.0224  0.0233  181 ARG A CA  
1414 C C   . ARG A 179 ? 0.4054 0.4147 0.4227 0.0214  0.0182  0.0289  181 ARG A C   
1415 O O   . ARG A 179 ? 0.4002 0.4172 0.4266 0.0206  0.0217  0.0356  181 ARG A O   
1416 C CB  . ARG A 179 ? 0.4781 0.4790 0.4678 0.0302  0.0237  0.0201  181 ARG A CB  
1417 C CG  . ARG A 179 ? 0.5808 0.5815 0.5687 0.0361  0.0306  0.0159  181 ARG A CG  
1418 C CD  . ARG A 179 ? 0.6850 0.6865 0.6578 0.0409  0.0377  0.0157  181 ARG A CD  
1419 N NE  . ARG A 179 ? 0.7783 0.7832 0.7574 0.0466  0.0462  0.0137  181 ARG A NE  
1420 C CZ  . ARG A 179 ? 0.8735 0.8891 0.8648 0.0485  0.0543  0.0196  181 ARG A CZ  
1421 N NH1 . ARG A 179 ? 0.8925 0.9109 0.8912 0.0537  0.0612  0.0175  181 ARG A NH1 
1422 N NH2 . ARG A 179 ? 0.9042 0.9280 0.9027 0.0452  0.0553  0.0280  181 ARG A NH2 
1423 N N   . VAL A 180 ? 0.3894 0.3926 0.4042 0.0180  0.0108  0.0266  182 VAL A N   
1424 C CA  . VAL A 180 ? 0.3872 0.3928 0.4108 0.0134  0.0066  0.0316  182 VAL A CA  
1425 C C   . VAL A 180 ? 0.3817 0.3933 0.4264 0.0109  0.0088  0.0337  182 VAL A C   
1426 O O   . VAL A 180 ? 0.3799 0.3971 0.4354 0.0089  0.0097  0.0397  182 VAL A O   
1427 C CB  . VAL A 180 ? 0.4210 0.4192 0.4390 0.0104  -0.0017 0.0287  182 VAL A CB  
1428 C CG1 . VAL A 180 ? 0.4356 0.4372 0.4669 0.0058  -0.0056 0.0340  182 VAL A CG1 
1429 C CG2 . VAL A 180 ? 0.4446 0.4369 0.4411 0.0123  -0.0048 0.0264  182 VAL A CG2 
1430 N N   . TYR A 181 ? 0.3516 0.3621 0.4022 0.0109  0.0095  0.0288  183 TYR A N   
1431 C CA  . TYR A 181 ? 0.3269 0.3425 0.3949 0.0083  0.0111  0.0294  183 TYR A CA  
1432 C C   . TYR A 181 ? 0.3443 0.3681 0.4217 0.0097  0.0169  0.0341  183 TYR A C   
1433 O O   . TYR A 181 ? 0.3314 0.3598 0.4232 0.0069  0.0178  0.0375  183 TYR A O   
1434 C CB  . TYR A 181 ? 0.3149 0.3282 0.3839 0.0087  0.0107  0.0239  183 TYR A CB  
1435 C CG  . TYR A 181 ? 0.3007 0.3181 0.3839 0.0057  0.0114  0.0229  183 TYR A CG  
1436 C CD1 . TYR A 181 ? 0.3258 0.3454 0.4200 0.0019  0.0109  0.0246  183 TYR A CD1 
1437 C CD2 . TYR A 181 ? 0.3309 0.3497 0.4163 0.0068  0.0122  0.0199  183 TYR A CD2 
1438 C CE1 . TYR A 181 ? 0.3217 0.3442 0.4273 -0.0009 0.0117  0.0222  183 TYR A CE1 
1439 C CE2 . TYR A 181 ? 0.3347 0.3568 0.4305 0.0037  0.0121  0.0182  183 TYR A CE2 
1440 C CZ  . TYR A 181 ? 0.3271 0.3507 0.4321 -0.0002 0.0121  0.0187  183 TYR A CZ  
1441 O OH  . TYR A 181 ? 0.3264 0.3527 0.4399 -0.0031 0.0123  0.0157  183 TYR A OH  
1442 N N   . LYS A 182 ? 0.3521 0.3775 0.4224 0.0140  0.0212  0.0343  184 LYS A N   
1443 C CA  . LYS A 182 ? 0.3608 0.3947 0.4418 0.0153  0.0274  0.0393  184 LYS A CA  
1444 C C   . LYS A 182 ? 0.3957 0.4328 0.4790 0.0139  0.0284  0.0469  184 LYS A C   
1445 O O   . LYS A 182 ? 0.3998 0.4431 0.4995 0.0120  0.0310  0.0516  184 LYS A O   
1446 C CB  . LYS A 182 ? 0.3771 0.4122 0.4505 0.0206  0.0325  0.0381  184 LYS A CB  
1447 C CG  . LYS A 182 ? 0.4141 0.4587 0.4988 0.0222  0.0398  0.0442  184 LYS A CG  
1448 C CD  . LYS A 182 ? 0.4397 0.4865 0.5214 0.0274  0.0453  0.0426  184 LYS A CD  
1449 C CE  . LYS A 182 ? 0.5091 0.5654 0.6003 0.0290  0.0534  0.0499  184 LYS A CE  
1450 N NZ  . LYS A 182 ? 0.5107 0.5708 0.6047 0.0339  0.0593  0.0483  184 LYS A NZ  
1451 N N   . GLU A 183 ? 0.4022 0.4352 0.4700 0.0144  0.0258  0.0486  185 GLU A N   
1452 C CA  . GLU A 183 ? 0.4297 0.4654 0.4985 0.0128  0.0252  0.0568  185 GLU A CA  
1453 C C   . GLU A 183 ? 0.4128 0.4494 0.4996 0.0082  0.0215  0.0589  185 GLU A C   
1454 O O   . GLU A 183 ? 0.3929 0.4347 0.4931 0.0068  0.0237  0.0661  185 GLU A O   
1455 C CB  . GLU A 183 ? 0.5103 0.5402 0.5575 0.0136  0.0207  0.0567  185 GLU A CB  
1456 C CG  . GLU A 183 ? 0.6676 0.7002 0.7125 0.0121  0.0188  0.0660  185 GLU A CG  
1457 C CD  . GLU A 183 ? 0.8739 0.9007 0.8962 0.0125  0.0128  0.0649  185 GLU A CD  
1458 O OE1 . GLU A 183 ? 0.9283 0.9479 0.9396 0.0131  0.0090  0.0563  185 GLU A OE1 
1459 O OE2 . GLU A 183 ? 0.9304 0.9598 0.9462 0.0120  0.0113  0.0731  185 GLU A OE2 
1460 N N   . ARG A 184 ? 0.3760 0.4076 0.4642 0.0060  0.0165  0.0530  186 ARG A N   
1461 C CA  . ARG A 184 ? 0.3746 0.4066 0.4796 0.0019  0.0138  0.0541  186 ARG A CA  
1462 C C   . ARG A 184 ? 0.3842 0.4208 0.5085 0.0005  0.0179  0.0532  186 ARG A C   
1463 O O   . ARG A 184 ? 0.3760 0.4146 0.5168 -0.0022 0.0178  0.0562  186 ARG A O   
1464 C CB  . ARG A 184 ? 0.3957 0.4216 0.4970 -0.0001 0.0084  0.0483  186 ARG A CB  
1465 C CG  . ARG A 184 ? 0.4394 0.4610 0.5267 -0.0001 0.0025  0.0503  186 ARG A CG  
1466 C CD  . ARG A 184 ? 0.4318 0.4559 0.5295 -0.0025 -0.0007 0.0578  186 ARG A CD  
1467 N NE  . ARG A 184 ? 0.4540 0.4776 0.5688 -0.0058 -0.0024 0.0559  186 ARG A NE  
1468 C CZ  . ARG A 184 ? 0.4388 0.4587 0.5539 -0.0079 -0.0079 0.0540  186 ARG A CZ  
1469 N NH1 . ARG A 184 ? 0.4860 0.5018 0.5852 -0.0076 -0.0137 0.0538  186 ARG A NH1 
1470 N NH2 . ARG A 184 ? 0.4327 0.4531 0.5649 -0.0105 -0.0074 0.0523  186 ARG A NH2 
1471 N N   . LEU A 185 ? 0.4004 0.4388 0.5241 0.0022  0.0212  0.0490  187 LEU A N   
1472 C CA  . LEU A 185 ? 0.4099 0.4533 0.5517 0.0007  0.0244  0.0482  187 LEU A CA  
1473 C C   . LEU A 185 ? 0.4739 0.5235 0.6265 0.0012  0.0289  0.0564  187 LEU A C   
1474 O O   . LEU A 185 ? 0.4933 0.5463 0.6645 -0.0011 0.0305  0.0568  187 LEU A O   
1475 C CB  . LEU A 185 ? 0.3703 0.4144 0.5087 0.0023  0.0254  0.0421  187 LEU A CB  
1476 C CG  . LEU A 185 ? 0.3573 0.3960 0.4888 0.0012  0.0215  0.0346  187 LEU A CG  
1477 C CD1 . LEU A 185 ? 0.3781 0.4177 0.5056 0.0032  0.0219  0.0304  187 LEU A CD1 
1478 C CD2 . LEU A 185 ? 0.3787 0.4167 0.5226 -0.0032 0.0199  0.0316  187 LEU A CD2 
1479 N N   . GLY A 186 ? 0.4943 0.5453 0.6353 0.0041  0.0310  0.0624  188 GLY A N   
1480 C CA  . GLY A 186 ? 0.5229 0.5802 0.6725 0.0047  0.0360  0.0715  188 GLY A CA  
1481 C C   . GLY A 186 ? 0.5582 0.6212 0.7128 0.0070  0.0418  0.0711  188 GLY A C   
1482 O O   . GLY A 186 ? 0.5635 0.6327 0.7324 0.0065  0.0463  0.0780  188 GLY A O   
1483 N N   . LEU A 187 ? 0.5578 0.6190 0.7025 0.0094  0.0416  0.0638  189 LEU A N   
1484 C CA  . LEU A 187 ? 0.5605 0.6277 0.7134 0.0115  0.0464  0.0634  189 LEU A CA  
1485 C C   . LEU A 187 ? 0.6057 0.6774 0.7512 0.0154  0.0534  0.0707  189 LEU A C   
1486 O O   . LEU A 187 ? 0.6169 0.6847 0.7421 0.0179  0.0536  0.0713  189 LEU A O   
1487 C CB  . LEU A 187 ? 0.5260 0.5903 0.6717 0.0133  0.0440  0.0547  189 LEU A CB  
1488 C CG  . LEU A 187 ? 0.5102 0.5704 0.6603 0.0097  0.0378  0.0475  189 LEU A CG  
1489 C CD1 . LEU A 187 ? 0.4997 0.5569 0.6406 0.0119  0.0353  0.0408  189 LEU A CD1 
1490 C CD2 . LEU A 187 ? 0.5333 0.5985 0.7049 0.0060  0.0376  0.0475  189 LEU A CD2 
1491 N N   . PRO A 188 ? 0.6287 0.7088 0.7902 0.0159  0.0595  0.0760  190 PRO A N   
1492 C CA  . PRO A 188 ? 0.6550 0.7400 0.8087 0.0203  0.0678  0.0822  190 PRO A CA  
1493 C C   . PRO A 188 ? 0.7002 0.7825 0.8366 0.0255  0.0696  0.0756  190 PRO A C   
1494 O O   . PRO A 188 ? 0.7051 0.7846 0.8436 0.0256  0.0655  0.0677  190 PRO A O   
1495 C CB  . PRO A 188 ? 0.6555 0.7503 0.8344 0.0193  0.0732  0.0876  190 PRO A CB  
1496 C CG  . PRO A 188 ? 0.6510 0.7450 0.8496 0.0139  0.0672  0.0853  190 PRO A CG  
1497 C CD  . PRO A 188 ? 0.6275 0.7129 0.8151 0.0124  0.0593  0.0763  190 PRO A CD  
1498 N N   . PRO A 189 ? 0.7281 0.8107 0.8469 0.0299  0.0758  0.0785  191 PRO A N   
1499 C CA  . PRO A 189 ? 0.7466 0.8263 0.8512 0.0353  0.0787  0.0716  191 PRO A CA  
1500 C C   . PRO A 189 ? 0.7419 0.8265 0.8633 0.0374  0.0809  0.0681  191 PRO A C   
1501 O O   . PRO A 189 ? 0.7610 0.8408 0.8744 0.0406  0.0794  0.0606  191 PRO A O   
1502 C CB  . PRO A 189 ? 0.7711 0.8538 0.8607 0.0395  0.0880  0.0773  191 PRO A CB  
1503 C CG  . PRO A 189 ? 0.7795 0.8637 0.8675 0.0358  0.0869  0.0864  191 PRO A CG  
1504 C CD  . PRO A 189 ? 0.7397 0.8250 0.8503 0.0300  0.0805  0.0882  191 PRO A CD  
1505 N N   . LYS A 190 ? 0.7085 0.8024 0.8544 0.0352  0.0837  0.0737  192 LYS A N   
1506 C CA  . LYS A 190 ? 0.6827 0.7832 0.8469 0.0371  0.0860  0.0720  192 LYS A CA  
1507 C C   . LYS A 190 ? 0.6360 0.7326 0.8071 0.0340  0.0760  0.0644  192 LYS A C   
1508 O O   . LYS A 190 ? 0.6317 0.7300 0.8086 0.0366  0.0754  0.0605  192 LYS A O   
1509 C CB  . LYS A 190 ? 0.7149 0.8271 0.9046 0.0351  0.0917  0.0809  192 LYS A CB  
1510 C CG  . LYS A 190 ? 0.8078 0.9254 0.9926 0.0375  0.1026  0.0905  192 LYS A CG  
1511 C CD  . LYS A 190 ? 0.8946 1.0087 1.0710 0.0337  0.1004  0.0965  192 LYS A CD  
1512 C CE  . LYS A 190 ? 0.9608 1.0835 1.1447 0.0338  0.1101  0.1092  192 LYS A CE  
1513 N NZ  . LYS A 190 ? 0.9875 1.1071 1.1674 0.0296  0.1066  0.1160  192 LYS A NZ  
1514 N N   . ILE A 191 ? 0.6077 0.6993 0.7785 0.0286  0.0684  0.0626  193 ILE A N   
1515 C CA  . ILE A 191 ? 0.5813 0.6690 0.7559 0.0256  0.0597  0.0554  193 ILE A CA  
1516 C C   . ILE A 191 ? 0.5600 0.6376 0.7124 0.0276  0.0557  0.0492  193 ILE A C   
1517 O O   . ILE A 191 ? 0.5778 0.6495 0.7149 0.0273  0.0552  0.0497  193 ILE A O   
1518 C CB  . ILE A 191 ? 0.5837 0.6715 0.7711 0.0190  0.0546  0.0556  193 ILE A CB  
1519 C CG1 . ILE A 191 ? 0.6024 0.7003 0.8163 0.0168  0.0573  0.0602  193 ILE A CG1 
1520 C CG2 . ILE A 191 ? 0.5825 0.6645 0.7668 0.0162  0.0461  0.0474  193 ILE A CG2 
1521 C CD1 . ILE A 191 ? 0.6345 0.7340 0.8603 0.0126  0.0585  0.0658  193 ILE A CD1 
1522 N N   . VAL A 192 ? 0.5318 0.6076 0.6832 0.0296  0.0527  0.0440  194 VAL A N   
1523 C CA  . VAL A 192 ? 0.5366 0.6027 0.6690 0.0320  0.0495  0.0384  194 VAL A CA  
1524 C C   . VAL A 192 ? 0.5304 0.5911 0.6616 0.0280  0.0407  0.0333  194 VAL A C   
1525 O O   . VAL A 192 ? 0.5272 0.5923 0.6720 0.0248  0.0371  0.0326  194 VAL A O   
1526 C CB  . VAL A 192 ? 0.5490 0.6156 0.6790 0.0385  0.0536  0.0367  194 VAL A CB  
1527 C CG1 . VAL A 192 ? 0.5651 0.6380 0.6966 0.0428  0.0639  0.0416  194 VAL A CG1 
1528 C CG2 . VAL A 192 ? 0.5460 0.6172 0.6918 0.0386  0.0500  0.0353  194 VAL A CG2 
1529 N N   . ILE A 193 ? 0.5053 0.5566 0.6198 0.0281  0.0373  0.0297  195 ILE A N   
1530 C CA  . ILE A 193 ? 0.4660 0.5114 0.5766 0.0254  0.0303  0.0252  195 ILE A CA  
1531 C C   . ILE A 193 ? 0.4324 0.4729 0.5355 0.0302  0.0298  0.0221  195 ILE A C   
1532 O O   . ILE A 193 ? 0.4359 0.4738 0.5307 0.0350  0.0343  0.0219  195 ILE A O   
1533 C CB  . ILE A 193 ? 0.4790 0.5179 0.5803 0.0215  0.0271  0.0243  195 ILE A CB  
1534 C CG1 . ILE A 193 ? 0.4887 0.5212 0.5737 0.0243  0.0285  0.0240  195 ILE A CG1 
1535 C CG2 . ILE A 193 ? 0.4913 0.5357 0.6041 0.0173  0.0281  0.0278  195 ILE A CG2 
1536 C CD1 . ILE A 193 ? 0.5112 0.5369 0.5884 0.0202  0.0234  0.0228  195 ILE A CD1 
1537 N N   . GLY A 194 ? 0.3884 0.4274 0.4943 0.0292  0.0245  0.0199  196 GLY A N   
1538 C CA  . GLY A 194 ? 0.3703 0.4039 0.4709 0.0334  0.0233  0.0178  196 GLY A CA  
1539 C C   . GLY A 194 ? 0.3617 0.3858 0.4517 0.0309  0.0173  0.0149  196 GLY A C   
1540 O O   . GLY A 194 ? 0.3497 0.3740 0.4405 0.0256  0.0133  0.0147  196 GLY A O   
1541 N N   . TYR A 195 ? 0.3473 0.3629 0.4281 0.0346  0.0170  0.0125  197 TYR A N   
1542 C CA  . TYR A 195 ? 0.3594 0.3659 0.4324 0.0326  0.0115  0.0106  197 TYR A CA  
1543 C C   . TYR A 195 ? 0.3944 0.4001 0.4730 0.0351  0.0085  0.0114  197 TYR A C   
1544 O O   . TYR A 195 ? 0.4168 0.4229 0.4997 0.0410  0.0115  0.0112  197 TYR A O   
1545 C CB  . TYR A 195 ? 0.3791 0.3749 0.4387 0.0346  0.0120  0.0071  197 TYR A CB  
1546 C CG  . TYR A 195 ? 0.4224 0.4091 0.4755 0.0313  0.0062  0.0056  197 TYR A CG  
1547 C CD1 . TYR A 195 ? 0.4595 0.4451 0.5092 0.0258  0.0037  0.0059  197 TYR A CD1 
1548 C CD2 . TYR A 195 ? 0.4809 0.4594 0.5324 0.0339  0.0037  0.0042  197 TYR A CD2 
1549 C CE1 . TYR A 195 ? 0.4883 0.4663 0.5340 0.0225  -0.0009 0.0052  197 TYR A CE1 
1550 C CE2 . TYR A 195 ? 0.4802 0.4504 0.5273 0.0305  -0.0014 0.0038  197 TYR A CE2 
1551 C CZ  . TYR A 195 ? 0.5177 0.4879 0.5617 0.0247  -0.0034 0.0043  197 TYR A CZ  
1552 O OH  . TYR A 195 ? 0.5452 0.5077 0.5862 0.0211  -0.0078 0.0043  197 TYR A OH  
1553 N N   . GLN A 196 ? 0.3518 0.3564 0.4305 0.0310  0.0030  0.0125  198 GLN A N   
1554 C CA  . GLN A 196 ? 0.4032 0.4068 0.4860 0.0326  -0.0010 0.0146  198 GLN A CA  
1555 C C   . GLN A 196 ? 0.3783 0.3727 0.4527 0.0298  -0.0052 0.0145  198 GLN A C   
1556 O O   . GLN A 196 ? 0.3744 0.3679 0.4436 0.0244  -0.0066 0.0141  198 GLN A O   
1557 C CB  . GLN A 196 ? 0.4659 0.4797 0.5579 0.0296  -0.0042 0.0175  198 GLN A CB  
1558 C CG  . GLN A 196 ? 0.5798 0.6040 0.6810 0.0289  -0.0010 0.0177  198 GLN A CG  
1559 C CD  . GLN A 196 ? 0.6810 0.7073 0.7794 0.0223  -0.0021 0.0164  198 GLN A CD  
1560 O OE1 . GLN A 196 ? 0.6977 0.7287 0.7989 0.0183  -0.0061 0.0167  198 GLN A OE1 
1561 N NE2 . GLN A 196 ? 0.6603 0.6831 0.7529 0.0211  0.0013  0.0146  198 GLN A NE2 
1562 N N   . SER A 197 ? 0.3543 0.3414 0.4286 0.0334  -0.0071 0.0151  199 SER A N   
1563 C CA  . SER A 197 ? 0.3589 0.3377 0.4277 0.0305  -0.0116 0.0166  199 SER A CA  
1564 C C   . SER A 197 ? 0.3563 0.3411 0.4262 0.0257  -0.0158 0.0210  199 SER A C   
1565 O O   . SER A 197 ? 0.3886 0.3819 0.4656 0.0266  -0.0171 0.0233  199 SER A O   
1566 C CB  . SER A 197 ? 0.3977 0.3673 0.4687 0.0358  -0.0127 0.0169  199 SER A CB  
1567 O OG  . SER A 197 ? 0.4687 0.4404 0.5461 0.0363  -0.0170 0.0224  199 SER A OG  
1568 N N   . HIS A 198 ? 0.3454 0.3265 0.4087 0.0206  -0.0178 0.0219  200 HIS A N   
1569 C CA  . HIS A 198 ? 0.3798 0.3661 0.4415 0.0161  -0.0211 0.0257  200 HIS A CA  
1570 C C   . HIS A 198 ? 0.4405 0.4265 0.5058 0.0187  -0.0259 0.0313  200 HIS A C   
1571 O O   . HIS A 198 ? 0.4286 0.4223 0.4949 0.0169  -0.0291 0.0343  200 HIS A O   
1572 C CB  . HIS A 198 ? 0.3797 0.3614 0.4337 0.0107  -0.0212 0.0262  200 HIS A CB  
1573 C CG  . HIS A 198 ? 0.3371 0.3204 0.3893 0.0075  -0.0175 0.0218  200 HIS A CG  
1574 N ND1 . HIS A 198 ? 0.3434 0.3353 0.3989 0.0066  -0.0152 0.0191  200 HIS A ND1 
1575 C CD2 . HIS A 198 ? 0.3625 0.3401 0.4118 0.0050  -0.0161 0.0204  200 HIS A CD2 
1576 C CE1 . HIS A 198 ? 0.3387 0.3295 0.3930 0.0039  -0.0125 0.0165  200 HIS A CE1 
1577 N NE2 . HIS A 198 ? 0.3646 0.3472 0.4152 0.0029  -0.0131 0.0171  200 HIS A NE2 
1578 N N   . ALA A 199 ? 0.4819 0.4588 0.5494 0.0228  -0.0267 0.0327  201 ALA A N   
1579 C CA  . ALA A 199 ? 0.5281 0.5038 0.6015 0.0259  -0.0312 0.0388  201 ALA A CA  
1580 C C   . ALA A 199 ? 0.5659 0.5512 0.6493 0.0299  -0.0318 0.0395  201 ALA A C   
1581 O O   . ALA A 199 ? 0.6018 0.5929 0.6887 0.0294  -0.0370 0.0451  201 ALA A O   
1582 C CB  . ALA A 199 ? 0.5303 0.4936 0.6065 0.0301  -0.0311 0.0388  201 ALA A CB  
1583 N N   . ASP A 200 ? 0.5667 0.5548 0.6551 0.0334  -0.0268 0.0344  202 ASP A N   
1584 C CA  . ASP A 200 ? 0.5831 0.5818 0.6832 0.0367  -0.0266 0.0352  202 ASP A CA  
1585 C C   . ASP A 200 ? 0.5874 0.5976 0.6874 0.0314  -0.0290 0.0358  202 ASP A C   
1586 O O   . ASP A 200 ? 0.5772 0.5955 0.6857 0.0321  -0.0336 0.0396  202 ASP A O   
1587 C CB  . ASP A 200 ? 0.6195 0.6182 0.7244 0.0417  -0.0194 0.0301  202 ASP A CB  
1588 C CG  . ASP A 200 ? 0.7413 0.7295 0.8481 0.0481  -0.0167 0.0283  202 ASP A CG  
1589 O OD1 . ASP A 200 ? 0.7800 0.7616 0.8886 0.0494  -0.0209 0.0320  202 ASP A OD1 
1590 O OD2 . ASP A 200 ? 0.7763 0.7627 0.8824 0.0517  -0.0103 0.0232  202 ASP A OD2 
1591 N N   . THR A 201 ? 0.5917 0.6026 0.6831 0.0262  -0.0265 0.0318  203 THR A N   
1592 C CA  . THR A 201 ? 0.6163 0.6364 0.7071 0.0209  -0.0289 0.0313  203 THR A CA  
1593 C C   . THR A 201 ? 0.6441 0.6663 0.7299 0.0175  -0.0361 0.0360  203 THR A C   
1594 O O   . THR A 201 ? 0.6465 0.6776 0.7360 0.0154  -0.0403 0.0367  203 THR A O   
1595 C CB  . THR A 201 ? 0.6445 0.6635 0.7278 0.0163  -0.0247 0.0264  203 THR A CB  
1596 O OG1 . THR A 201 ? 0.6514 0.6689 0.7383 0.0194  -0.0187 0.0232  203 THR A OG1 
1597 C CG2 . THR A 201 ? 0.6459 0.6738 0.7302 0.0112  -0.0263 0.0243  203 THR A CG2 
1598 N N   . ALA A 202 ? 0.6588 0.6727 0.7361 0.0168  -0.0378 0.0394  204 ALA A N   
1599 C CA  . ALA A 202 ? 0.6674 0.6826 0.7371 0.0132  -0.0440 0.0448  204 ALA A CA  
1600 C C   . ALA A 202 ? 0.6859 0.7067 0.7644 0.0162  -0.0512 0.0511  204 ALA A C   
1601 O O   . ALA A 202 ? 0.6786 0.7034 0.7507 0.0128  -0.0574 0.0557  204 ALA A O   
1602 C CB  . ALA A 202 ? 0.6640 0.6687 0.7255 0.0123  -0.0434 0.0482  204 ALA A CB  
1603 N N   . THR A 203 ? 0.6918 0.7133 0.7850 0.0227  -0.0502 0.0517  205 THR A N   
1604 C CA  . THR A 203 ? 0.6971 0.7240 0.8024 0.0264  -0.0566 0.0581  205 THR A CA  
1605 C C   . THR A 203 ? 0.6692 0.7076 0.7867 0.0271  -0.0568 0.0553  205 THR A C   
1606 O O   . THR A 203 ? 0.6646 0.7034 0.7901 0.0304  -0.0498 0.0506  205 THR A O   
1607 C CB  . THR A 203 ? 0.7515 0.7702 0.8668 0.0337  -0.0549 0.0611  205 THR A CB  
1608 O OG1 . THR A 203 ? 0.7870 0.8054 0.9116 0.0387  -0.0474 0.0552  205 THR A OG1 
1609 C CG2 . THR A 203 ? 0.7717 0.7776 0.8768 0.0329  -0.0537 0.0626  205 THR A CG2 
1610 N N   . LYS A 204 ? 0.6498 0.6978 0.7687 0.0236  -0.0648 0.0583  206 LYS A N   
1611 C CA  . LYS A 204 ? 0.6334 0.6930 0.7660 0.0235  -0.0663 0.0561  206 LYS A CA  
1612 C C   . LYS A 204 ? 0.6245 0.6888 0.7773 0.0301  -0.0696 0.0623  206 LYS A C   
1613 O O   . LYS A 204 ? 0.6040 0.6699 0.7589 0.0308  -0.0783 0.0698  206 LYS A O   
1614 C CB  . LYS A 204 ? 0.6654 0.7327 0.7897 0.0161  -0.0740 0.0552  206 LYS A CB  
1615 C CG  . LYS A 204 ? 0.7454 0.8082 0.8504 0.0098  -0.0702 0.0489  206 LYS A CG  
1616 C CD  . LYS A 204 ? 0.8255 0.8897 0.9354 0.0088  -0.0624 0.0409  206 LYS A CD  
1617 C CE  . LYS A 204 ? 0.9072 0.9690 1.0016 0.0022  -0.0598 0.0346  206 LYS A CE  
1618 N NZ  . LYS A 204 ? 0.9457 1.0149 1.0475 -0.0014 -0.0594 0.0283  206 LYS A NZ  
1619 N N   . SER A 205 ? 0.6214 0.6884 0.7898 0.0352  -0.0626 0.0595  207 SER A N   
1620 C CA  . SER A 205 ? 0.6228 0.6925 0.8117 0.0429  -0.0624 0.0643  207 SER A CA  
1621 C C   . SER A 205 ? 0.6153 0.6980 0.8255 0.0446  -0.0610 0.0636  207 SER A C   
1622 O O   . SER A 205 ? 0.6162 0.7015 0.8450 0.0516  -0.0576 0.0662  207 SER A O   
1623 C CB  . SER A 205 ? 0.6565 0.7146 0.8441 0.0492  -0.0530 0.0618  207 SER A CB  
1624 O OG  . SER A 205 ? 0.6953 0.7508 0.8758 0.0482  -0.0435 0.0542  207 SER A OG  
1625 N N   . GLY A 206 ? 0.6142 0.7047 0.8229 0.0383  -0.0633 0.0602  208 GLY A N   
1626 C CA  . GLY A 206 ? 0.6184 0.7213 0.8484 0.0389  -0.0624 0.0600  208 GLY A CA  
1627 C C   . GLY A 206 ? 0.6366 0.7412 0.8614 0.0337  -0.0570 0.0531  208 GLY A C   
1628 O O   . GLY A 206 ? 0.6688 0.7677 0.8740 0.0280  -0.0580 0.0489  208 GLY A O   
1629 N N   . LYS A 210 ? 0.6931 0.7416 0.8473 0.0467  -0.0005 0.0283  212 LYS A N   
1630 C CA  . LYS A 210 ? 0.7151 0.7520 0.8608 0.0512  0.0006  0.0269  212 LYS A CA  
1631 C C   . LYS A 210 ? 0.7089 0.7367 0.8383 0.0505  0.0059  0.0220  212 LYS A C   
1632 O O   . LYS A 210 ? 0.7149 0.7328 0.8317 0.0481  0.0028  0.0203  212 LYS A O   
1633 C CB  . LYS A 210 ? 0.7695 0.8015 0.9112 0.0489  -0.0082 0.0295  212 LYS A CB  
1634 C CG  . LYS A 210 ? 0.8706 0.9042 1.0034 0.0407  -0.0143 0.0299  212 LYS A CG  
1635 C CD  . LYS A 210 ? 0.9460 0.9830 1.0821 0.0386  -0.0235 0.0348  212 LYS A CD  
1636 C CE  . LYS A 210 ? 1.0070 1.0518 1.1412 0.0316  -0.0279 0.0343  212 LYS A CE  
1637 N NZ  . LYS A 210 ? 1.0118 1.0585 1.1427 0.0283  -0.0371 0.0385  212 LYS A NZ  
1638 N N   . ASN A 211 ? 0.6827 0.7143 0.8132 0.0524  0.0137  0.0205  213 ASN A N   
1639 C CA  . ASN A 211 ? 0.6648 0.6898 0.7804 0.0512  0.0179  0.0168  213 ASN A CA  
1640 C C   . ASN A 211 ? 0.6753 0.6907 0.7830 0.0571  0.0219  0.0131  213 ASN A C   
1641 O O   . ASN A 211 ? 0.6858 0.7040 0.8010 0.0635  0.0281  0.0128  213 ASN A O   
1642 C CB  . ASN A 211 ? 0.6445 0.6784 0.7645 0.0504  0.0240  0.0179  213 ASN A CB  
1643 C CG  . ASN A 211 ? 0.6615 0.7030 0.7883 0.0439  0.0199  0.0202  213 ASN A CG  
1644 O OD1 . ASN A 211 ? 0.6580 0.6959 0.7788 0.0389  0.0138  0.0194  213 ASN A OD1 
1645 N ND2 . ASN A 211 ? 0.6654 0.7175 0.8057 0.0437  0.0233  0.0230  213 ASN A ND2 
1646 N N   . ARG A 212 ? 0.6792 0.6829 0.7729 0.0553  0.0187  0.0098  214 ARG A N   
1647 C CA  . ARG A 212 ? 0.7039 0.6970 0.7880 0.0604  0.0225  0.0047  214 ARG A CA  
1648 C C   . ARG A 212 ? 0.7056 0.7007 0.7807 0.0613  0.0295  0.0023  214 ARG A C   
1649 O O   . ARG A 212 ? 0.7178 0.7109 0.7902 0.0673  0.0364  -0.0009 214 ARG A O   
1650 C CB  . ARG A 212 ? 0.7405 0.7204 0.8127 0.0576  0.0167  0.0016  214 ARG A CB  
1651 C CG  . ARG A 212 ? 0.8157 0.7945 0.8918 0.0531  0.0089  0.0054  214 ARG A CG  
1652 C CD  . ARG A 212 ? 0.8955 0.8619 0.9696 0.0549  0.0051  0.0039  214 ARG A CD  
1653 N NE  . ARG A 212 ? 0.9638 0.9186 1.0246 0.0542  0.0053  -0.0018 214 ARG A NE  
1654 C CZ  . ARG A 212 ? 0.9951 0.9381 1.0521 0.0529  0.0006  -0.0033 214 ARG A CZ  
1655 N NH1 . ARG A 212 ? 0.9718 0.9128 1.0368 0.0522  -0.0041 0.0014  214 ARG A NH1 
1656 N NH2 . ARG A 212 ? 0.9932 0.9264 1.0388 0.0519  0.0002  -0.0090 214 ARG A NH2 
1657 N N   . PHE A 213 ? 0.6732 0.6721 0.7433 0.0553  0.0280  0.0041  215 PHE A N   
1658 C CA  . PHE A 213 ? 0.6498 0.6506 0.7108 0.0552  0.0333  0.0035  215 PHE A CA  
1659 C C   . PHE A 213 ? 0.6282 0.6408 0.6988 0.0514  0.0346  0.0087  215 PHE A C   
1660 O O   . PHE A 213 ? 0.5776 0.5939 0.6561 0.0467  0.0294  0.0111  215 PHE A O   
1661 C CB  . PHE A 213 ? 0.6520 0.6431 0.6966 0.0515  0.0291  0.0003  215 PHE A CB  
1662 C CG  . PHE A 213 ? 0.6694 0.6472 0.7044 0.0533  0.0257  -0.0053 215 PHE A CG  
1663 C CD1 . PHE A 213 ? 0.6966 0.6684 0.7243 0.0595  0.0307  -0.0105 215 PHE A CD1 
1664 C CD2 . PHE A 213 ? 0.6807 0.6516 0.7137 0.0486  0.0181  -0.0057 215 PHE A CD2 
1665 C CE1 . PHE A 213 ? 0.7042 0.6625 0.7237 0.0609  0.0272  -0.0165 215 PHE A CE1 
1666 C CE2 . PHE A 213 ? 0.6999 0.6582 0.7256 0.0497  0.0147  -0.0106 215 PHE A CE2 
1667 C CZ  . PHE A 213 ? 0.6980 0.6495 0.7172 0.0558  0.0189  -0.0162 215 PHE A CZ  
1668 N N   . VAL A 214 ? 0.6341 0.6524 0.7036 0.0536  0.0419  0.0105  216 VAL A N   
1669 C CA  . VAL A 214 ? 0.6436 0.6719 0.7214 0.0500  0.0439  0.0157  216 VAL A CA  
1670 C C   . VAL A 214 ? 0.6457 0.6720 0.7090 0.0493  0.0472  0.0163  216 VAL A C   
1671 O O   . VAL A 214 ? 0.6660 0.6866 0.7155 0.0535  0.0510  0.0129  216 VAL A O   
1672 C CB  . VAL A 214 ? 0.6659 0.7054 0.7610 0.0535  0.0502  0.0194  216 VAL A CB  
1673 C CG1 . VAL A 214 ? 0.6799 0.7296 0.7859 0.0496  0.0523  0.0251  216 VAL A CG1 
1674 C CG2 . VAL A 214 ? 0.6684 0.7100 0.7775 0.0542  0.0455  0.0193  216 VAL A CG2 
1675 N N   . VAL A 215 ? 0.6217 0.6522 0.6879 0.0440  0.0455  0.0204  217 VAL A N   
1676 C CA  . VAL A 215 ? 0.6316 0.6627 0.6872 0.0434  0.0488  0.0233  217 VAL A CA  
1677 C C   . VAL A 215 ? 0.6299 0.6713 0.7003 0.0400  0.0512  0.0305  217 VAL A C   
1678 O O   . VAL A 215 ? 0.6185 0.6637 0.6844 0.0408  0.0566  0.0353  217 VAL A O   
1679 C CB  . VAL A 215 ? 0.6481 0.6698 0.6875 0.0402  0.0424  0.0207  217 VAL A CB  
1680 C CG1 . VAL A 215 ? 0.6727 0.6834 0.7005 0.0425  0.0388  0.0134  217 VAL A CG1 
1681 C CG2 . VAL A 215 ? 0.6408 0.6635 0.6890 0.0337  0.0360  0.0229  217 VAL A CG2 
1682 O OXT . VAL A 215 ? 0.5996 0.6448 0.6854 0.0365  0.0475  0.0312  217 VAL A OXT 
1683 N N   . HIS B 7   ? 1.5137 0.7495 0.7510 0.0999  -0.1636 -0.0014 9   HIS B N   
1684 C CA  . HIS B 7   ? 1.5191 0.7450 0.7463 0.0868  -0.1357 0.0039  9   HIS B CA  
1685 C C   . HIS B 7   ? 1.4898 0.7197 0.7298 0.0824  -0.1221 0.0094  9   HIS B C   
1686 O O   . HIS B 7   ? 1.5158 0.7236 0.7338 0.0928  -0.1274 0.0131  9   HIS B O   
1687 C CB  . HIS B 7   ? 1.5782 0.7574 0.7454 0.0908  -0.1275 0.0072  9   HIS B CB  
1688 C CG  . HIS B 7   ? 1.6202 0.7985 0.7790 0.0885  -0.1302 0.0020  9   HIS B CG  
1689 N ND1 . HIS B 7   ? 1.6283 0.8322 0.8177 0.0745  -0.1163 -0.0002 9   HIS B ND1 
1690 C CD2 . HIS B 7   ? 1.6585 0.8131 0.7816 0.0989  -0.1455 -0.0017 9   HIS B CD2 
1691 C CE1 . HIS B 7   ? 1.6441 0.8377 0.8155 0.0766  -0.1223 -0.0050 9   HIS B CE1 
1692 N NE2 . HIS B 7   ? 1.6658 0.8301 0.7972 0.0906  -0.1400 -0.0065 9   HIS B NE2 
1693 N N   . GLY B 8   ? 1.4357 0.6929 0.7097 0.0676  -0.1050 0.0098  10  GLY B N   
1694 C CA  . GLY B 8   ? 1.3922 0.6679 0.6946 0.0618  -0.0963 0.0121  10  GLY B CA  
1695 C C   . GLY B 8   ? 1.3343 0.6539 0.6901 0.0606  -0.1080 0.0078  10  GLY B C   
1696 O O   . GLY B 8   ? 1.3288 0.6651 0.7091 0.0569  -0.1026 0.0091  10  GLY B O   
1697 N N   . ALA B 9   ? 1.2981 0.6361 0.6723 0.0630  -0.1228 0.0024  11  ALA B N   
1698 C CA  . ALA B 9   ? 1.2447 0.6201 0.6661 0.0637  -0.1361 -0.0024 11  ALA B CA  
1699 C C   . ALA B 9   ? 1.2058 0.6152 0.6670 0.0500  -0.1217 -0.0025 11  ALA B C   
1700 O O   . ALA B 9   ? 1.2089 0.6167 0.6631 0.0415  -0.1074 -0.0013 11  ALA B O   
1701 C CB  . ALA B 9   ? 1.2287 0.6065 0.6505 0.0700  -0.1555 -0.0091 11  ALA B CB  
1702 N N   . ARG B 10  ? 1.1650 0.6048 0.6669 0.0488  -0.1253 -0.0038 12  ARG B N   
1703 C CA  . ARG B 10  ? 1.1264 0.5988 0.6655 0.0377  -0.1134 -0.0038 12  ARG B CA  
1704 C C   . ARG B 10  ? 1.1083 0.5949 0.6628 0.0346  -0.1169 -0.0077 12  ARG B C   
1705 O O   . ARG B 10  ? 1.1117 0.5998 0.6720 0.0406  -0.1334 -0.0129 12  ARG B O   
1706 C CB  . ARG B 10  ? 1.1178 0.6159 0.6931 0.0385  -0.1169 -0.0043 12  ARG B CB  
1707 C CG  . ARG B 10  ? 1.1499 0.6790 0.7590 0.0280  -0.1032 -0.0031 12  ARG B CG  
1708 C CD  . ARG B 10  ? 1.1582 0.7092 0.7991 0.0294  -0.1058 -0.0037 12  ARG B CD  
1709 N NE  . ARG B 10  ? 1.1941 0.7275 0.8171 0.0334  -0.1044 -0.0014 12  ARG B NE  
1710 C CZ  . ARG B 10  ? 1.2025 0.7310 0.8158 0.0267  -0.0891 0.0017  12  ARG B CZ  
1711 N NH1 . ARG B 10  ? 1.1970 0.7401 0.8183 0.0161  -0.0750 0.0028  12  ARG B NH1 
1712 N NH2 . ARG B 10  ? 1.1759 0.6851 0.7717 0.0307  -0.0879 0.0034  12  ARG B NH2 
1713 N N   . ILE B 11  ? 1.0688 0.5660 0.6304 0.0254  -0.1012 -0.0057 13  ILE B N   
1714 C CA  . ILE B 11  ? 1.0265 0.5374 0.6045 0.0222  -0.1014 -0.0087 13  ILE B CA  
1715 C C   . ILE B 11  ? 0.9685 0.5129 0.5917 0.0197  -0.1031 -0.0100 13  ILE B C   
1716 O O   . ILE B 11  ? 0.9433 0.5064 0.5846 0.0142  -0.0907 -0.0064 13  ILE B O   
1717 C CB  . ILE B 11  ? 1.0438 0.5522 0.6108 0.0152  -0.0835 -0.0056 13  ILE B CB  
1718 C CG1 . ILE B 11  ? 1.0985 0.5728 0.6206 0.0166  -0.0780 -0.0039 13  ILE B CG1 
1719 C CG2 . ILE B 11  ? 1.0333 0.5517 0.6141 0.0134  -0.0837 -0.0085 13  ILE B CG2 
1720 C CD1 . ILE B 11  ? 1.1349 0.6097 0.6499 0.0092  -0.0586 -0.0011 13  ILE B CD1 
1721 N N   . ILE B 12  ? 0.9340 0.4858 0.5746 0.0234  -0.1177 -0.0156 14  ILE B N   
1722 C CA  . ILE B 12  ? 0.8953 0.4754 0.5773 0.0215  -0.1199 -0.0176 14  ILE B CA  
1723 C C   . ILE B 12  ? 0.8780 0.4646 0.5739 0.0186  -0.1216 -0.0221 14  ILE B C   
1724 O O   . ILE B 12  ? 0.8977 0.4691 0.5782 0.0216  -0.1329 -0.0276 14  ILE B O   
1725 C CB  . ILE B 12  ? 0.9041 0.4883 0.5985 0.0285  -0.1357 -0.0214 14  ILE B CB  
1726 C CG1 . ILE B 12  ? 0.9410 0.5152 0.6195 0.0321  -0.1330 -0.0168 14  ILE B CG1 
1727 C CG2 . ILE B 12  ? 0.8801 0.4935 0.6192 0.0260  -0.1368 -0.0243 14  ILE B CG2 
1728 C CD1 . ILE B 12  ? 0.9597 0.5329 0.6435 0.0412  -0.1484 -0.0199 14  ILE B CD1 
1729 N N   . TYR B 13  ? 0.8347 0.4422 0.5575 0.0130  -0.1102 -0.0198 15  TYR B N   
1730 C CA  . TYR B 13  ? 0.8311 0.4454 0.5712 0.0099  -0.1095 -0.0236 15  TYR B CA  
1731 C C   . TYR B 13  ? 0.8276 0.4657 0.6072 0.0079  -0.1096 -0.0252 15  TYR B C   
1732 O O   . TYR B 13  ? 0.8397 0.4933 0.6340 0.0065  -0.1002 -0.0198 15  TYR B O   
1733 C CB  . TYR B 13  ? 0.8210 0.4356 0.5551 0.0059  -0.0929 -0.0184 15  TYR B CB  
1734 C CG  . TYR B 13  ? 0.8567 0.4491 0.5541 0.0068  -0.0889 -0.0167 15  TYR B CG  
1735 C CD1 . TYR B 13  ? 0.8885 0.4602 0.5647 0.0084  -0.0961 -0.0220 15  TYR B CD1 
1736 C CD2 . TYR B 13  ? 0.8514 0.4435 0.5354 0.0055  -0.0771 -0.0105 15  TYR B CD2 
1737 C CE1 . TYR B 13  ? 0.9206 0.4704 0.5620 0.0092  -0.0905 -0.0203 15  TYR B CE1 
1738 C CE2 . TYR B 13  ? 0.8842 0.4561 0.5360 0.0055  -0.0713 -0.0092 15  TYR B CE2 
1739 C CZ  . TYR B 13  ? 0.9269 0.4767 0.5566 0.0077  -0.0776 -0.0137 15  TYR B CZ  
1740 O OH  . TYR B 13  ? 0.9584 0.4863 0.5546 0.0080  -0.0709 -0.0125 15  TYR B OH  
1741 N N   . ASP B 14  ? 0.8180 0.4593 0.6152 0.0072  -0.1194 -0.0330 16  ASP B N   
1742 C CA  . ASP B 14  ? 0.7924 0.4555 0.6287 0.0039  -0.1164 -0.0348 16  ASP B CA  
1743 C C   . ASP B 14  ? 0.7634 0.4315 0.6099 -0.0012 -0.1001 -0.0310 16  ASP B C   
1744 O O   . ASP B 14  ? 0.7698 0.4254 0.5955 -0.0019 -0.0929 -0.0282 16  ASP B O   
1745 C CB  . ASP B 14  ? 0.8156 0.4838 0.6722 0.0045  -0.1328 -0.0457 16  ASP B CB  
1746 C CG  . ASP B 14  ? 0.8896 0.5455 0.7390 0.0023  -0.1408 -0.0543 16  ASP B CG  
1747 O OD1 . ASP B 14  ? 0.8828 0.5288 0.7199 -0.0011 -0.1300 -0.0517 16  ASP B OD1 
1748 O OD2 . ASP B 14  ? 0.9578 0.6145 0.8139 0.0044  -0.1583 -0.0641 16  ASP B OD2 
1749 N N   . ARG B 15  ? 0.7275 0.4132 0.6056 -0.0041 -0.0935 -0.0305 17  ARG B N   
1750 C CA  . ARG B 15  ? 0.7155 0.4063 0.6047 -0.0074 -0.0772 -0.0256 17  ARG B CA  
1751 C C   . ARG B 15  ? 0.7327 0.4090 0.6155 -0.0103 -0.0765 -0.0305 17  ARG B C   
1752 O O   . ARG B 15  ? 0.7179 0.3877 0.5887 -0.0102 -0.0644 -0.0249 17  ARG B O   
1753 C CB  . ARG B 15  ? 0.6898 0.3988 0.6143 -0.0099 -0.0720 -0.0260 17  ARG B CB  
1754 C CG  . ARG B 15  ? 0.7264 0.4408 0.6593 -0.0114 -0.0539 -0.0186 17  ARG B CG  
1755 C CD  . ARG B 15  ? 0.7533 0.4813 0.7203 -0.0146 -0.0484 -0.0204 17  ARG B CD  
1756 N NE  . ARG B 15  ? 0.8139 0.5435 0.7859 -0.0151 -0.0301 -0.0127 17  ARG B NE  
1757 C CZ  . ARG B 15  ? 0.8891 0.6078 0.8615 -0.0175 -0.0219 -0.0132 17  ARG B CZ  
1758 N NH1 . ARG B 15  ? 0.9253 0.6312 0.8942 -0.0209 -0.0306 -0.0221 17  ARG B NH1 
1759 N NH2 . ARG B 15  ? 0.9014 0.6206 0.8762 -0.0161 -0.0048 -0.0048 17  ARG B NH2 
1760 N N   . ALA B 16  ? 0.7491 0.4208 0.6401 -0.0125 -0.0900 -0.0414 18  ALA B N   
1761 C CA  . ALA B 16  ? 0.7643 0.4216 0.6504 -0.0163 -0.0903 -0.0481 18  ALA B CA  
1762 C C   . ALA B 16  ? 0.7896 0.4263 0.6372 -0.0131 -0.0895 -0.0454 18  ALA B C   
1763 O O   . ALA B 16  ? 0.8156 0.4419 0.6552 -0.0147 -0.0785 -0.0436 18  ALA B O   
1764 C CB  . ALA B 16  ? 0.7740 0.4325 0.6750 -0.0190 -0.1079 -0.0618 18  ALA B CB  
1765 N N   . PHE B 17  ? 0.7972 0.4268 0.6206 -0.0085 -0.0995 -0.0449 19  PHE B N   
1766 C CA  . PHE B 17  ? 0.8233 0.4330 0.6096 -0.0057 -0.0971 -0.0419 19  PHE B CA  
1767 C C   . PHE B 17  ? 0.7912 0.4045 0.5718 -0.0051 -0.0778 -0.0310 19  PHE B C   
1768 O O   . PHE B 17  ? 0.7829 0.3836 0.5483 -0.0052 -0.0695 -0.0299 19  PHE B O   
1769 C CB  . PHE B 17  ? 0.8599 0.4614 0.6222 -0.0007 -0.1091 -0.0419 19  PHE B CB  
1770 C CG  . PHE B 17  ? 0.9282 0.5047 0.6508 0.0017  -0.1089 -0.0418 19  PHE B CG  
1771 C CD1 . PHE B 17  ? 0.9825 0.5409 0.6880 0.0024  -0.1216 -0.0512 19  PHE B CD1 
1772 C CD2 . PHE B 17  ? 0.9579 0.5296 0.6611 0.0027  -0.0951 -0.0331 19  PHE B CD2 
1773 C CE1 . PHE B 17  ? 1.0242 0.5577 0.6910 0.0048  -0.1199 -0.0510 19  PHE B CE1 
1774 C CE2 . PHE B 17  ? 1.0034 0.5518 0.6709 0.0045  -0.0929 -0.0332 19  PHE B CE2 
1775 C CZ  . PHE B 17  ? 1.0281 0.5564 0.6763 0.0058  -0.1050 -0.0417 19  PHE B CZ  
1776 N N   . LEU B 18  ? 0.7755 0.4068 0.5689 -0.0042 -0.0709 -0.0234 20  LEU B N   
1777 C CA  . LEU B 18  ? 0.7470 0.3852 0.5366 -0.0030 -0.0542 -0.0138 20  LEU B CA  
1778 C C   . LEU B 18  ? 0.7506 0.3896 0.5521 -0.0039 -0.0421 -0.0119 20  LEU B C   
1779 O O   . LEU B 18  ? 0.7472 0.3810 0.5353 -0.0018 -0.0311 -0.0072 20  LEU B O   
1780 C CB  . LEU B 18  ? 0.7257 0.3837 0.5286 -0.0023 -0.0509 -0.0079 20  LEU B CB  
1781 C CG  . LEU B 18  ? 0.7311 0.3856 0.5183 -0.0009 -0.0596 -0.0084 20  LEU B CG  
1782 C CD1 . LEU B 18  ? 0.6863 0.3597 0.4894 -0.0009 -0.0567 -0.0043 20  LEU B CD1 
1783 C CD2 . LEU B 18  ? 0.7807 0.4224 0.5378 0.0000  -0.0546 -0.0056 20  LEU B CD2 
1784 N N   . MET B 19  ? 0.7559 0.4005 0.5826 -0.0069 -0.0433 -0.0158 21  MET B N   
1785 C CA  . MET B 19  ? 0.7876 0.4303 0.6263 -0.0080 -0.0309 -0.0140 21  MET B CA  
1786 C C   . MET B 19  ? 0.8337 0.4541 0.6553 -0.0091 -0.0311 -0.0197 21  MET B C   
1787 O O   . MET B 19  ? 0.8596 0.4742 0.6807 -0.0078 -0.0178 -0.0158 21  MET B O   
1788 C CB  . MET B 19  ? 0.7910 0.4433 0.6617 -0.0125 -0.0317 -0.0182 21  MET B CB  
1789 C CG  . MET B 19  ? 0.8326 0.5060 0.7215 -0.0112 -0.0280 -0.0120 21  MET B CG  
1790 S SD  . MET B 19  ? 0.8443 0.5287 0.7286 -0.0053 -0.0096 0.0022  21  MET B SD  
1791 C CE  . MET B 19  ? 0.9670 0.6389 0.8573 -0.0056 0.0047  0.0037  21  MET B CE  
1792 N N   . ALA B 20  ? 0.8513 0.4581 0.6573 -0.0106 -0.0457 -0.0287 22  ALA B N   
1793 C CA  . ALA B 20  ? 0.8869 0.4703 0.6725 -0.0116 -0.0469 -0.0352 22  ALA B CA  
1794 C C   . ALA B 20  ? 0.9016 0.4744 0.6579 -0.0067 -0.0376 -0.0286 22  ALA B C   
1795 O O   . ALA B 20  ? 0.9151 0.4715 0.6586 -0.0063 -0.0302 -0.0300 22  ALA B O   
1796 C CB  . ALA B 20  ? 0.8960 0.4694 0.6722 -0.0137 -0.0669 -0.0469 22  ALA B CB  
1797 N N   . CYS B 21  ? 0.8871 0.4692 0.6343 -0.0035 -0.0368 -0.0219 23  CYS B N   
1798 C CA  . CYS B 21  ? 0.8921 0.4702 0.6180 0.0005  -0.0256 -0.0150 23  CYS B CA  
1799 C C   . CYS B 21  ? 0.8714 0.4621 0.6099 0.0038  -0.0085 -0.0063 23  CYS B C   
1800 O O   . CYS B 21  ? 0.8940 0.4834 0.6181 0.0076  0.0017  -0.0013 23  CYS B O   
1801 C CB  . CYS B 21  ? 0.9151 0.4995 0.6292 0.0016  -0.0299 -0.0119 23  CYS B CB  
1802 S SG  . CYS B 21  ? 0.9539 0.5212 0.6480 0.0006  -0.0498 -0.0205 23  CYS B SG  
1803 N N   . ARG B 22  ? 0.8194 0.4224 0.5839 0.0030  -0.0047 -0.0041 24  ARG B N   
1804 C CA  . ARG B 22  ? 0.8086 0.4236 0.5836 0.0077  0.0106  0.0051  24  ARG B CA  
1805 C C   . ARG B 22  ? 0.8525 0.4494 0.6214 0.0099  0.0208  0.0045  24  ARG B C   
1806 O O   . ARG B 22  ? 0.8827 0.4786 0.6399 0.0158  0.0316  0.0101  24  ARG B O   
1807 C CB  . ARG B 22  ? 0.7638 0.3953 0.5656 0.0064  0.0115  0.0078  24  ARG B CB  
1808 C CG  . ARG B 22  ? 0.7670 0.4123 0.5772 0.0128  0.0261  0.0183  24  ARG B CG  
1809 C CD  . ARG B 22  ? 0.7595 0.4179 0.5931 0.0111  0.0269  0.0204  24  ARG B CD  
1810 N NE  . ARG B 22  ? 0.7581 0.4302 0.5971 0.0182  0.0397  0.0309  24  ARG B NE  
1811 C CZ  . ARG B 22  ? 0.7760 0.4599 0.6320 0.0186  0.0436  0.0349  24  ARG B CZ  
1812 N NH1 . ARG B 22  ? 0.7186 0.4034 0.5905 0.0117  0.0364  0.0290  24  ARG B NH1 
1813 N NH2 . ARG B 22  ? 0.7933 0.4881 0.6500 0.0265  0.0547  0.0446  24  ARG B NH2 
1814 N N   . LYS B 34  ? 1.0554 0.5292 0.5720 0.0069  0.0078  -0.0086 36  LYS B N   
1815 C CA  . LYS B 34  ? 1.0340 0.5374 0.5845 0.0053  0.0035  -0.0055 36  LYS B CA  
1816 C C   . LYS B 34  ? 1.0110 0.5095 0.5568 0.0045  -0.0116 -0.0073 36  LYS B C   
1817 O O   . LYS B 34  ? 1.0472 0.5219 0.5624 0.0051  -0.0153 -0.0089 36  LYS B O   
1818 C CB  . LYS B 34  ? 1.0712 0.5997 0.6378 0.0036  0.0186  0.0005  36  LYS B CB  
1819 C CG  . LYS B 34  ? 1.1120 0.6543 0.6939 0.0066  0.0312  0.0031  36  LYS B CG  
1820 C CD  . LYS B 34  ? 1.1784 0.7469 0.7753 0.0056  0.0446  0.0079  36  LYS B CD  
1821 C CE  . LYS B 34  ? 1.2442 0.8287 0.8581 0.0108  0.0554  0.0110  36  LYS B CE  
1822 N NZ  . LYS B 34  ? 1.2975 0.9100 0.9264 0.0106  0.0673  0.0147  36  LYS B NZ  
1823 N N   . HIS B 35  ? 0.9558 0.4755 0.5308 0.0039  -0.0196 -0.0068 37  HIS B N   
1824 C CA  . HIS B 35  ? 0.9414 0.4586 0.5164 0.0042  -0.0347 -0.0089 37  HIS B CA  
1825 C C   . HIS B 35  ? 0.9318 0.4641 0.5145 0.0017  -0.0288 -0.0040 37  HIS B C   
1826 O O   . HIS B 35  ? 0.8934 0.4523 0.5043 0.0000  -0.0231 -0.0006 37  HIS B O   
1827 C CB  . HIS B 35  ? 0.9144 0.4449 0.5173 0.0047  -0.0463 -0.0123 37  HIS B CB  
1828 C CG  . HIS B 35  ? 0.9784 0.4915 0.5720 0.0060  -0.0545 -0.0193 37  HIS B CG  
1829 N ND1 . HIS B 35  ? 1.0141 0.5297 0.6181 0.0052  -0.0464 -0.0200 37  HIS B ND1 
1830 C CD2 . HIS B 35  ? 1.0182 0.5108 0.5918 0.0083  -0.0702 -0.0262 37  HIS B CD2 
1831 C CE1 . HIS B 35  ? 1.0418 0.5383 0.6328 0.0058  -0.0568 -0.0280 37  HIS B CE1 
1832 N NE2 . HIS B 35  ? 1.0488 0.5321 0.6214 0.0078  -0.0721 -0.0322 37  HIS B NE2 
1833 N N   . PRO B 36  ? 0.9568 0.4709 0.5134 0.0015  -0.0295 -0.0036 38  PRO B N   
1834 C CA  . PRO B 36  ? 0.9363 0.4626 0.4989 -0.0022 -0.0218 0.0002  38  PRO B CA  
1835 C C   . PRO B 36  ? 0.9087 0.4528 0.4957 -0.0019 -0.0314 0.0005  38  PRO B C   
1836 O O   . PRO B 36  ? 0.9281 0.4661 0.5169 0.0019  -0.0463 -0.0026 38  PRO B O   
1837 C CB  . PRO B 36  ? 0.9878 0.4828 0.5117 -0.0019 -0.0204 0.0001  38  PRO B CB  
1838 C CG  . PRO B 36  ? 1.0223 0.4928 0.5253 0.0042  -0.0356 -0.0041 38  PRO B CG  
1839 C CD  . PRO B 36  ? 0.9973 0.4768 0.5153 0.0049  -0.0366 -0.0067 38  PRO B CD  
1840 N N   . LEU B 37  ? 0.8601 0.4270 0.4660 -0.0060 -0.0226 0.0037  39  LEU B N   
1841 C CA  . LEU B 37  ? 0.8123 0.3938 0.4373 -0.0062 -0.0291 0.0041  39  LEU B CA  
1842 C C   . LEU B 37  ? 0.8197 0.3842 0.4238 -0.0073 -0.0294 0.0043  39  LEU B C   
1843 O O   . LEU B 37  ? 0.8326 0.3821 0.4138 -0.0103 -0.0193 0.0051  39  LEU B O   
1844 C CB  . LEU B 37  ? 0.7762 0.3902 0.4302 -0.0096 -0.0197 0.0070  39  LEU B CB  
1845 C CG  . LEU B 37  ? 0.7680 0.3997 0.4444 -0.0075 -0.0179 0.0081  39  LEU B CG  
1846 C CD1 . LEU B 37  ? 0.7544 0.4166 0.4545 -0.0094 -0.0088 0.0115  39  LEU B CD1 
1847 C CD2 . LEU B 37  ? 0.7842 0.4129 0.4720 -0.0041 -0.0307 0.0055  39  LEU B CD2 
1848 N N   . GLN B 38  ? 0.8020 0.3683 0.4144 -0.0048 -0.0395 0.0037  40  GLN B N   
1849 C CA  . GLN B 38  ? 0.8388 0.3899 0.4344 -0.0050 -0.0394 0.0043  40  GLN B CA  
1850 C C   . GLN B 38  ? 0.8321 0.3942 0.4307 -0.0132 -0.0234 0.0059  40  GLN B C   
1851 O O   . GLN B 38  ? 0.8620 0.4039 0.4360 -0.0162 -0.0158 0.0063  40  GLN B O   
1852 C CB  . GLN B 38  ? 0.8753 0.4348 0.4890 -0.0005 -0.0518 0.0032  40  GLN B CB  
1853 C CG  . GLN B 38  ? 0.9177 0.4619 0.5167 0.0007  -0.0522 0.0041  40  GLN B CG  
1854 C CD  . GLN B 38  ? 1.0174 0.5245 0.5771 0.0062  -0.0571 0.0042  40  GLN B CD  
1855 O OE1 . GLN B 38  ? 1.0411 0.5348 0.5869 0.0113  -0.0658 0.0026  40  GLN B OE1 
1856 N NE2 . GLN B 38  ? 1.0402 0.5284 0.5797 0.0055  -0.0512 0.0060  40  GLN B NE2 
1857 N N   . ASN B 39  ? 0.7951 0.3892 0.4233 -0.0168 -0.0179 0.0066  41  ASN B N   
1858 C CA  . ASN B 39  ? 0.7679 0.3794 0.4047 -0.0244 -0.0048 0.0068  41  ASN B CA  
1859 C C   . ASN B 39  ? 0.7370 0.3691 0.3861 -0.0268 0.0045  0.0076  41  ASN B C   
1860 O O   . ASN B 39  ? 0.7518 0.3906 0.4109 -0.0222 0.0004  0.0087  41  ASN B O   
1861 C CB  . ASN B 39  ? 0.7663 0.3986 0.4267 -0.0250 -0.0080 0.0067  41  ASN B CB  
1862 C CG  . ASN B 39  ? 0.8436 0.4566 0.4912 -0.0236 -0.0132 0.0058  41  ASN B CG  
1863 O OD1 . ASN B 39  ? 0.9019 0.5015 0.5325 -0.0288 -0.0050 0.0049  41  ASN B OD1 
1864 N ND2 . ASN B 39  ? 0.8309 0.4412 0.4863 -0.0166 -0.0260 0.0057  41  ASN B ND2 
1865 N N   . ARG B 40  ? 0.7174 0.3601 0.3668 -0.0339 0.0173  0.0067  42  ARG B N   
1866 C CA  . ARG B 40  ? 0.6750 0.3453 0.3422 -0.0355 0.0259  0.0072  42  ARG B CA  
1867 C C   . ARG B 40  ? 0.6309 0.3320 0.3248 -0.0362 0.0241  0.0074  42  ARG B C   
1868 O O   . ARG B 40  ? 0.6405 0.3419 0.3356 -0.0397 0.0227  0.0057  42  ARG B O   
1869 C CB  . ARG B 40  ? 0.7045 0.3747 0.3620 -0.0429 0.0400  0.0049  42  ARG B CB  
1870 C CG  . ARG B 40  ? 0.6840 0.3840 0.3603 -0.0434 0.0484  0.0050  42  ARG B CG  
1871 C CD  . ARG B 40  ? 0.7077 0.3969 0.3685 -0.0483 0.0615  0.0029  42  ARG B CD  
1872 N NE  . ARG B 40  ? 0.6906 0.4067 0.3679 -0.0475 0.0704  0.0027  42  ARG B NE  
1873 C CZ  . ARG B 40  ? 0.6936 0.4369 0.3862 -0.0539 0.0804  -0.0010 42  ARG B CZ  
1874 N NH1 . ARG B 40  ? 0.6604 0.4074 0.3540 -0.0634 0.0837  -0.0054 42  ARG B NH1 
1875 N NH2 . ARG B 40  ? 0.6827 0.4496 0.3899 -0.0507 0.0872  -0.0008 42  ARG B NH2 
1876 N N   . TRP B 41  ? 0.6071 0.3315 0.3203 -0.0318 0.0244  0.0098  43  TRP B N   
1877 C CA  . TRP B 41  ? 0.5744 0.3261 0.3108 -0.0300 0.0222  0.0111  43  TRP B CA  
1878 C C   . TRP B 41  ? 0.5620 0.3430 0.3116 -0.0303 0.0308  0.0115  43  TRP B C   
1879 O O   . TRP B 41  ? 0.5861 0.3667 0.3319 -0.0286 0.0363  0.0123  43  TRP B O   
1880 C CB  . TRP B 41  ? 0.5654 0.3156 0.3124 -0.0223 0.0137  0.0145  43  TRP B CB  
1881 C CG  . TRP B 41  ? 0.5917 0.3193 0.3311 -0.0211 0.0037  0.0133  43  TRP B CG  
1882 C CD1 . TRP B 41  ? 0.6285 0.3305 0.3519 -0.0189 -0.0022 0.0123  43  TRP B CD1 
1883 C CD2 . TRP B 41  ? 0.5977 0.3272 0.3449 -0.0214 -0.0021 0.0123  43  TRP B CD2 
1884 N NE1 . TRP B 41  ? 0.6494 0.3387 0.3711 -0.0172 -0.0122 0.0108  43  TRP B NE1 
1885 C CE2 . TRP B 41  ? 0.6215 0.3269 0.3579 -0.0187 -0.0117 0.0109  43  TRP B CE2 
1886 C CE3 . TRP B 41  ? 0.5725 0.3217 0.3341 -0.0231 -0.0002 0.0122  43  TRP B CE3 
1887 C CZ2 . TRP B 41  ? 0.6262 0.3278 0.3682 -0.0171 -0.0191 0.0097  43  TRP B CZ2 
1888 C CZ3 . TRP B 41  ? 0.5794 0.3230 0.3451 -0.0222 -0.0064 0.0111  43  TRP B CZ3 
1889 C CH2 . TRP B 41  ? 0.6002 0.3208 0.3571 -0.0191 -0.0156 0.0099  43  TRP B CH2 
1890 N N   . ALA B 42  ? 0.5400 0.3463 0.3045 -0.0319 0.0315  0.0107  44  ALA B N   
1891 C CA  . ALA B 42  ? 0.5215 0.3593 0.2997 -0.0309 0.0374  0.0105  44  ALA B CA  
1892 C C   . ALA B 42  ? 0.5172 0.3738 0.3108 -0.0235 0.0332  0.0146  44  ALA B C   
1893 O O   . ALA B 42  ? 0.5063 0.3620 0.3031 -0.0247 0.0285  0.0142  44  ALA B O   
1894 C CB  . ALA B 42  ? 0.5351 0.3863 0.3142 -0.0408 0.0427  0.0040  44  ALA B CB  
1895 N N   . LEU B 43  ? 0.5101 0.3826 0.3125 -0.0154 0.0358  0.0189  45  LEU B N   
1896 C CA  . LEU B 43  ? 0.4991 0.3901 0.3141 -0.0072 0.0340  0.0237  45  LEU B CA  
1897 C C   . LEU B 43  ? 0.4934 0.4173 0.3174 -0.0071 0.0366  0.0214  45  LEU B C   
1898 O O   . LEU B 43  ? 0.5016 0.4400 0.3282 -0.0066 0.0413  0.0198  45  LEU B O   
1899 C CB  . LEU B 43  ? 0.5051 0.3918 0.3224 0.0032  0.0359  0.0302  45  LEU B CB  
1900 C CG  . LEU B 43  ? 0.5518 0.4539 0.3792 0.0127  0.0359  0.0363  45  LEU B CG  
1901 C CD1 . LEU B 43  ? 0.5426 0.4346 0.3727 0.0116  0.0314  0.0373  45  LEU B CD1 
1902 C CD2 . LEU B 43  ? 0.5927 0.4893 0.4206 0.0223  0.0400  0.0422  45  LEU B CD2 
1903 N N   . TRP B 44  ? 0.4768 0.4132 0.3061 -0.0070 0.0334  0.0210  46  TRP B N   
1904 C CA  . TRP B 44  ? 0.4940 0.4624 0.3309 -0.0068 0.0338  0.0179  46  TRP B CA  
1905 C C   . TRP B 44  ? 0.5153 0.4978 0.3578 0.0051  0.0321  0.0247  46  TRP B C   
1906 O O   . TRP B 44  ? 0.5013 0.4674 0.3426 0.0099  0.0310  0.0304  46  TRP B O   
1907 C CB  . TRP B 44  ? 0.5090 0.4775 0.3437 -0.0173 0.0317  0.0108  46  TRP B CB  
1908 C CG  . TRP B 44  ? 0.5449 0.4954 0.3712 -0.0293 0.0340  0.0044  46  TRP B CG  
1909 C CD1 . TRP B 44  ? 0.5725 0.4905 0.3881 -0.0326 0.0328  0.0052  46  TRP B CD1 
1910 C CD2 . TRP B 44  ? 0.5775 0.5408 0.4046 -0.0395 0.0386  -0.0040 46  TRP B CD2 
1911 N NE1 . TRP B 44  ? 0.5865 0.4939 0.3934 -0.0435 0.0369  -0.0013 46  TRP B NE1 
1912 C CE2 . TRP B 44  ? 0.5945 0.5288 0.4090 -0.0487 0.0413  -0.0072 46  TRP B CE2 
1913 C CE3 . TRP B 44  ? 0.6041 0.6014 0.4420 -0.0418 0.0406  -0.0098 46  TRP B CE3 
1914 C CZ2 . TRP B 44  ? 0.6438 0.5793 0.4551 -0.0608 0.0479  -0.0155 46  TRP B CZ2 
1915 C CZ3 . TRP B 44  ? 0.6396 0.6413 0.4776 -0.0547 0.0462  -0.0191 46  TRP B CZ3 
1916 C CH2 . TRP B 44  ? 0.6550 0.6247 0.4795 -0.0645 0.0508  -0.0217 46  TRP B CH2 
1917 N N   . PHE B 45  ? 0.5189 0.5328 0.3675 0.0097  0.0323  0.0235  47  PHE B N   
1918 C CA  . PHE B 45  ? 0.5714 0.6008 0.4221 0.0226  0.0311  0.0302  47  PHE B CA  
1919 C C   . PHE B 45  ? 0.5574 0.6164 0.4110 0.0200  0.0275  0.0236  47  PHE B C   
1920 O O   . PHE B 45  ? 0.5324 0.6104 0.3911 0.0133  0.0274  0.0155  47  PHE B O   
1921 C CB  . PHE B 45  ? 0.6065 0.6437 0.4600 0.0354  0.0344  0.0368  47  PHE B CB  
1922 C CG  . PHE B 45  ? 0.6472 0.7028 0.5008 0.0502  0.0337  0.0437  47  PHE B CG  
1923 C CD1 . PHE B 45  ? 0.6689 0.7077 0.5171 0.0578  0.0352  0.0520  47  PHE B CD1 
1924 C CD2 . PHE B 45  ? 0.6807 0.7703 0.5396 0.0572  0.0319  0.0417  47  PHE B CD2 
1925 C CE1 . PHE B 45  ? 0.6873 0.7397 0.5321 0.0724  0.0358  0.0592  47  PHE B CE1 
1926 C CE2 . PHE B 45  ? 0.6948 0.8002 0.5507 0.0729  0.0306  0.0487  47  PHE B CE2 
1927 C CZ  . PHE B 45  ? 0.6900 0.7751 0.5372 0.0804  0.0329  0.0578  47  PHE B CZ  
1928 N N   . PHE B 46  ? 0.5887 0.6509 0.4387 0.0244  0.0252  0.0260  48  PHE B N   
1929 C CA  . PHE B 46  ? 0.6276 0.7172 0.4779 0.0228  0.0212  0.0194  48  PHE B CA  
1930 C C   . PHE B 46  ? 0.6719 0.7716 0.5171 0.0381  0.0200  0.0276  48  PHE B C   
1931 O O   . PHE B 46  ? 0.6602 0.7379 0.5002 0.0439  0.0231  0.0360  48  PHE B O   
1932 C CB  . PHE B 46  ? 0.6511 0.7288 0.4978 0.0089  0.0201  0.0116  48  PHE B CB  
1933 C CG  . PHE B 46  ? 0.6843 0.7865 0.5300 0.0043  0.0163  0.0026  48  PHE B CG  
1934 C CD1 . PHE B 46  ? 0.6933 0.8189 0.5456 -0.0049 0.0149  -0.0084 48  PHE B CD1 
1935 C CD2 . PHE B 46  ? 0.7221 0.8229 0.5603 0.0081  0.0149  0.0042  48  PHE B CD2 
1936 C CE1 . PHE B 46  ? 0.7045 0.8536 0.5563 -0.0100 0.0109  -0.0182 48  PHE B CE1 
1937 C CE2 . PHE B 46  ? 0.7288 0.8512 0.5640 0.0036  0.0111  -0.0050 48  PHE B CE2 
1938 C CZ  . PHE B 46  ? 0.7090 0.8557 0.5512 -0.0056 0.0086  -0.0165 48  PHE B CZ  
1939 N N   . LYS B 47  ? 0.7053 0.8385 0.5517 0.0450  0.0159  0.0249  49  LYS B N   
1940 C CA  . LYS B 47  ? 0.7475 0.8920 0.5847 0.0581  0.0136  0.0303  49  LYS B CA  
1941 C C   . LYS B 47  ? 0.7613 0.9334 0.5980 0.0514  0.0070  0.0185  49  LYS B C   
1942 O O   . LYS B 47  ? 0.7518 0.9509 0.5983 0.0471  0.0033  0.0098  49  LYS B O   
1943 C CB  . LYS B 47  ? 0.7933 0.9516 0.6298 0.0770  0.0139  0.0396  49  LYS B CB  
1944 C CG  . LYS B 47  ? 0.8879 1.0428 0.7099 0.0931  0.0149  0.0499  49  LYS B CG  
1945 C CD  . LYS B 47  ? 0.9780 1.1359 0.7966 0.1128  0.0176  0.0615  49  LYS B CD  
1946 C CE  . LYS B 47  ? 1.0615 1.2161 0.8627 0.1295  0.0192  0.0717  49  LYS B CE  
1947 N NZ  . LYS B 47  ? 1.1046 1.2694 0.9008 0.1506  0.0201  0.0816  49  LYS B NZ  
1948 N N   . ASN B 48  ? 0.7852 0.9510 0.6115 0.0496  0.0062  0.0173  50  ASN B N   
1949 C CA  . ASN B 48  ? 0.8016 0.9922 0.6247 0.0438  -0.0001 0.0056  50  ASN B CA  
1950 C C   . ASN B 48  ? 0.8073 1.0325 0.6261 0.0594  -0.0071 0.0067  50  ASN B C   
1951 O O   . ASN B 48  ? 0.8194 1.0458 0.6231 0.0700  -0.0086 0.0113  50  ASN B O   
1952 C CB  . ASN B 48  ? 0.8410 1.0117 0.6527 0.0381  0.0020  0.0042  50  ASN B CB  
1953 C CG  . ASN B 48  ? 0.8992 1.0890 0.7076 0.0278  -0.0032 -0.0100 50  ASN B CG  
1954 O OD1 . ASN B 48  ? 0.9166 1.1288 0.7351 0.0180  -0.0072 -0.0216 50  ASN B OD1 
1955 N ND2 . ASN B 48  ? 0.9209 1.1023 0.7155 0.0291  -0.0025 -0.0102 50  ASN B ND2 
1956 N N   . ASP B 49  ? 0.8022 1.0557 0.6341 0.0610  -0.0111 0.0022  51  ASP B N   
1957 C CA  . ASP B 49  ? 0.8150 1.1065 0.6470 0.0760  -0.0192 0.0017  51  ASP B CA  
1958 C C   . ASP B 49  ? 0.8204 1.1458 0.6605 0.0633  -0.0273 -0.0164 51  ASP B C   
1959 O O   . ASP B 49  ? 0.8010 1.1395 0.6587 0.0498  -0.0269 -0.0269 51  ASP B O   
1960 C CB  . ASP B 49  ? 0.8309 1.1320 0.6748 0.0867  -0.0175 0.0082  51  ASP B CB  
1961 C CG  . ASP B 49  ? 0.8972 1.2437 0.7486 0.0992  -0.0266 0.0040  51  ASP B CG  
1962 O OD1 . ASP B 49  ? 0.9281 1.2937 0.7673 0.1104  -0.0345 0.0038  51  ASP B OD1 
1963 O OD2 . ASP B 49  ? 0.9103 1.2739 0.7795 0.0982  -0.0261 0.0007  51  ASP B OD2 
1964 N N   . LYS B 50  ? 0.8463 1.1852 0.6727 0.0674  -0.0340 -0.0205 52  LYS B N   
1965 C CA  . LYS B 50  ? 0.8559 1.2205 0.6870 0.0525  -0.0409 -0.0390 52  LYS B CA  
1966 C C   . LYS B 50  ? 0.8632 1.2769 0.7119 0.0544  -0.0504 -0.0501 52  LYS B C   
1967 O O   . LYS B 50  ? 0.8595 1.2949 0.7189 0.0376  -0.0544 -0.0677 52  LYS B O   
1968 C CB  . LYS B 50  ? 0.8763 1.2372 0.6849 0.0567  -0.0448 -0.0401 52  LYS B CB  
1969 C CG  . LYS B 50  ? 0.9216 1.2392 0.7189 0.0469  -0.0353 -0.0363 52  LYS B CG  
1970 C CD  . LYS B 50  ? 0.9792 1.2938 0.7834 0.0229  -0.0340 -0.0529 52  LYS B CD  
1971 C CE  . LYS B 50  ? 1.0644 1.3355 0.8605 0.0144  -0.0242 -0.0483 52  LYS B CE  
1972 N NZ  . LYS B 50  ? 1.1053 1.3681 0.9093 -0.0083 -0.0211 -0.0626 52  LYS B NZ  
1973 N N   . SER B 51  ? 0.8663 1.2979 0.7192 0.0741  -0.0535 -0.0407 53  SER B N   
1974 C CA  . SER B 51  ? 0.8533 1.3327 0.7279 0.0759  -0.0616 -0.0513 53  SER B CA  
1975 C C   . SER B 51  ? 0.8510 1.3313 0.7506 0.0553  -0.0545 -0.0612 53  SER B C   
1976 O O   . SER B 51  ? 0.8415 1.3603 0.7615 0.0464  -0.0597 -0.0767 53  SER B O   
1977 C CB  . SER B 51  ? 0.8638 1.3591 0.7369 0.1029  -0.0654 -0.0380 53  SER B CB  
1978 O OG  . SER B 51  ? 0.9061 1.3793 0.7873 0.1067  -0.0552 -0.0266 53  SER B OG  
1979 N N   . LYS B 52  ? 0.8591 1.2977 0.7570 0.0478  -0.0424 -0.0528 54  LYS B N   
1980 C CA  . LYS B 52  ? 0.8602 1.2915 0.7759 0.0279  -0.0341 -0.0612 54  LYS B CA  
1981 C C   . LYS B 52  ? 0.8718 1.2743 0.7799 0.0060  -0.0290 -0.0692 54  LYS B C   
1982 O O   . LYS B 52  ? 0.8846 1.2647 0.7737 0.0082  -0.0296 -0.0644 54  LYS B O   
1983 C CB  . LYS B 52  ? 0.8997 1.3032 0.8166 0.0351  -0.0248 -0.0470 54  LYS B CB  
1984 C CG  . LYS B 52  ? 0.9588 1.3842 0.8805 0.0586  -0.0281 -0.0371 54  LYS B CG  
1985 C CD  . LYS B 52  ? 1.0486 1.4433 0.9702 0.0643  -0.0180 -0.0241 54  LYS B CD  
1986 C CE  . LYS B 52  ? 1.1053 1.5225 1.0339 0.0862  -0.0199 -0.0160 54  LYS B CE  
1987 N NZ  . LYS B 52  ? 1.1572 1.5467 1.0880 0.0890  -0.0092 -0.0064 54  LYS B NZ  
1988 N N   . THR B 53  ? 0.8709 1.2723 0.7931 -0.0147 -0.0227 -0.0812 55  THR B N   
1989 C CA  . THR B 53  ? 0.8969 1.2657 0.8113 -0.0351 -0.0157 -0.0877 55  THR B CA  
1990 C C   . THR B 53  ? 0.9116 1.2300 0.8140 -0.0343 -0.0066 -0.0738 55  THR B C   
1991 O O   . THR B 53  ? 0.9093 1.2201 0.8140 -0.0227 -0.0039 -0.0622 55  THR B O   
1992 C CB  . THR B 53  ? 0.9222 1.3059 0.8548 -0.0571 -0.0108 -0.1052 55  THR B CB  
1993 O OG1 . THR B 53  ? 0.9631 1.3177 0.8853 -0.0755 -0.0051 -0.1127 55  THR B OG1 
1994 C CG2 . THR B 53  ? 0.9212 1.2975 0.8666 -0.0596 -0.0016 -0.1016 55  THR B CG2 
1995 N N   . TRP B 54  ? 0.9246 1.2092 0.8146 -0.0463 -0.0021 -0.0755 56  TRP B N   
1996 C CA  . TRP B 54  ? 0.9477 1.1872 0.8272 -0.0449 0.0047  -0.0634 56  TRP B CA  
1997 C C   . TRP B 54  ? 0.9406 1.1663 0.8279 -0.0502 0.0122  -0.0614 56  TRP B C   
1998 O O   . TRP B 54  ? 0.9516 1.1496 0.8325 -0.0426 0.0153  -0.0492 56  TRP B O   
1999 C CB  . TRP B 54  ? 0.9699 1.1772 0.8360 -0.0560 0.0079  -0.0662 56  TRP B CB  
2000 C CG  . TRP B 54  ? 0.9899 1.1892 0.8586 -0.0771 0.0137  -0.0800 56  TRP B CG  
2001 C CD1 . TRP B 54  ? 1.0030 1.2169 0.8721 -0.0898 0.0124  -0.0947 56  TRP B CD1 
2002 C CD2 . TRP B 54  ? 1.0072 1.1783 0.8758 -0.0880 0.0225  -0.0801 56  TRP B CD2 
2003 N NE1 . TRP B 54  ? 1.0157 1.2120 0.8860 -0.1084 0.0209  -0.1040 56  TRP B NE1 
2004 C CE2 . TRP B 54  ? 1.0208 1.1904 0.8900 -0.1070 0.0272  -0.0948 56  TRP B CE2 
2005 C CE3 . TRP B 54  ? 1.0209 1.1666 0.8875 -0.0834 0.0270  -0.0696 56  TRP B CE3 
2006 C CZ2 . TRP B 54  ? 1.0376 1.1800 0.9041 -0.1206 0.0371  -0.0982 56  TRP B CZ2 
2007 C CZ3 . TRP B 54  ? 1.0402 1.1613 0.9039 -0.0965 0.0355  -0.0734 56  TRP B CZ3 
2008 C CH2 . TRP B 54  ? 1.0453 1.1637 0.9082 -0.1145 0.0409  -0.0870 56  TRP B CH2 
2009 N N   . GLN B 55  ? 0.9225 1.1659 0.8229 -0.0638 0.0159  -0.0738 57  GLN B N   
2010 C CA  . GLN B 55  ? 0.9198 1.1492 0.8259 -0.0688 0.0245  -0.0721 57  GLN B CA  
2011 C C   . GLN B 55  ? 0.8836 1.1307 0.7985 -0.0521 0.0229  -0.0630 57  GLN B C   
2012 O O   . GLN B 55  ? 0.8959 1.1198 0.8080 -0.0492 0.0289  -0.0550 57  GLN B O   
2013 C CB  . GLN B 55  ? 0.9565 1.1993 0.8747 -0.0885 0.0311  -0.0880 57  GLN B CB  
2014 C CG  . GLN B 55  ? 1.0410 1.2685 0.9513 -0.1066 0.0340  -0.0993 57  GLN B CG  
2015 C CD  . GLN B 55  ? 1.1197 1.3533 1.0408 -0.1270 0.0438  -0.1139 57  GLN B CD  
2016 O OE1 . GLN B 55  ? 1.1418 1.3858 1.0755 -0.1286 0.0499  -0.1150 57  GLN B OE1 
2017 N NE2 . GLN B 55  ? 1.1287 1.3544 1.0451 -0.1433 0.0468  -0.1258 57  GLN B NE2 
2018 N N   . ALA B 56  ? 0.8351 1.1224 0.7595 -0.0403 0.0147  -0.0642 58  ALA B N   
2019 C CA  . ALA B 56  ? 0.7990 1.1022 0.7303 -0.0219 0.0131  -0.0546 58  ALA B CA  
2020 C C   . ALA B 56  ? 0.7694 1.0449 0.6850 -0.0054 0.0121  -0.0377 58  ALA B C   
2021 O O   . ALA B 56  ? 0.7737 1.0419 0.6906 0.0056  0.0155  -0.0283 58  ALA B O   
2022 C CB  . ALA B 56  ? 0.7848 1.1389 0.7296 -0.0129 0.0040  -0.0610 58  ALA B CB  
2023 N N   . ASN B 57  ? 0.7394 0.9989 0.6406 -0.0038 0.0083  -0.0343 59  ASN B N   
2024 C CA  . ASN B 57  ? 0.7078 0.9419 0.5951 0.0107  0.0082  -0.0192 59  ASN B CA  
2025 C C   . ASN B 57  ? 0.6927 0.8828 0.5727 0.0062  0.0151  -0.0120 59  ASN B C   
2026 O O   . ASN B 57  ? 0.6932 0.8646 0.5668 0.0183  0.0166  0.0001  59  ASN B O   
2027 C CB  . ASN B 57  ? 0.7067 0.9395 0.5823 0.0123  0.0032  -0.0195 59  ASN B CB  
2028 C CG  . ASN B 57  ? 0.6974 0.9665 0.5725 0.0255  -0.0050 -0.0203 59  ASN B CG  
2029 O OD1 . ASN B 57  ? 0.6686 0.9557 0.5472 0.0419  -0.0072 -0.0134 59  ASN B OD1 
2030 N ND2 . ASN B 57  ? 0.6914 0.9703 0.5603 0.0195  -0.0098 -0.0286 59  ASN B ND2 
2031 N N   . LEU B 58  ? 0.6785 0.8518 0.5584 -0.0110 0.0192  -0.0199 60  LEU B N   
2032 C CA  . LEU B 58  ? 0.6897 0.8227 0.5614 -0.0161 0.0243  -0.0150 60  LEU B CA  
2033 C C   . LEU B 58  ? 0.6802 0.8112 0.5577 -0.0165 0.0297  -0.0142 60  LEU B C   
2034 O O   . LEU B 58  ? 0.7046 0.8525 0.5908 -0.0261 0.0328  -0.0237 60  LEU B O   
2035 C CB  . LEU B 58  ? 0.7049 0.8193 0.5706 -0.0329 0.0260  -0.0236 60  LEU B CB  
2036 C CG  . LEU B 58  ? 0.7411 0.8136 0.5970 -0.0383 0.0303  -0.0196 60  LEU B CG  
2037 C CD1 . LEU B 58  ? 0.7523 0.8023 0.6017 -0.0271 0.0279  -0.0081 60  LEU B CD1 
2038 C CD2 . LEU B 58  ? 0.7585 0.8143 0.6077 -0.0539 0.0325  -0.0285 60  LEU B CD2 
2039 N N   . ARG B 59  ? 0.6423 0.7526 0.5152 -0.0067 0.0318  -0.0037 61  ARG B N   
2040 C CA  . ARG B 59  ? 0.6255 0.7332 0.5023 -0.0047 0.0374  -0.0021 61  ARG B CA  
2041 C C   . ARG B 59  ? 0.5869 0.6526 0.4517 -0.0093 0.0410  0.0019  61  ARG B C   
2042 O O   . ARG B 59  ? 0.5545 0.5981 0.4117 -0.0042 0.0384  0.0089  61  ARG B O   
2043 C CB  . ARG B 59  ? 0.6675 0.7919 0.5494 0.0139  0.0366  0.0067  61  ARG B CB  
2044 C CG  . ARG B 59  ? 0.7605 0.9301 0.6544 0.0206  0.0321  0.0024  61  ARG B CG  
2045 C CD  . ARG B 59  ? 0.8688 1.0492 0.7626 0.0418  0.0303  0.0134  61  ARG B CD  
2046 N NE  . ARG B 59  ? 0.9122 1.1345 0.8143 0.0507  0.0238  0.0102  61  ARG B NE  
2047 C CZ  . ARG B 59  ? 0.9545 1.1872 0.8505 0.0547  0.0171  0.0105  61  ARG B CZ  
2048 N NH1 . ARG B 59  ? 0.9468 1.2188 0.8493 0.0636  0.0102  0.0069  61  ARG B NH1 
2049 N NH2 . ARG B 59  ? 0.9717 1.1759 0.8548 0.0503  0.0170  0.0140  61  ARG B NH2 
2050 N N   . LEU B 60  ? 0.5965 0.6516 0.4594 -0.0187 0.0471  -0.0030 62  LEU B N   
2051 C CA  . LEU B 60  ? 0.6125 0.6301 0.4626 -0.0202 0.0502  0.0012  62  LEU B CA  
2052 C C   . LEU B 60  ? 0.6258 0.6428 0.4777 -0.0073 0.0527  0.0088  62  LEU B C   
2053 O O   . LEU B 60  ? 0.6479 0.6850 0.5084 -0.0049 0.0577  0.0067  62  LEU B O   
2054 C CB  . LEU B 60  ? 0.6252 0.6296 0.4694 -0.0343 0.0571  -0.0065 62  LEU B CB  
2055 C CG  . LEU B 60  ? 0.6471 0.6143 0.4757 -0.0345 0.0607  -0.0026 62  LEU B CG  
2056 C CD1 . LEU B 60  ? 0.6469 0.5835 0.4627 -0.0354 0.0548  0.0005  62  LEU B CD1 
2057 C CD2 . LEU B 60  ? 0.6808 0.6400 0.5038 -0.0460 0.0701  -0.0094 62  LEU B CD2 
2058 N N   . ILE B 61  ? 0.5986 0.5922 0.4430 0.0006  0.0502  0.0169  63  ILE B N   
2059 C CA  . ILE B 61  ? 0.5912 0.5786 0.4351 0.0123  0.0535  0.0240  63  ILE B CA  
2060 C C   . ILE B 61  ? 0.6116 0.5731 0.4450 0.0073  0.0589  0.0224  63  ILE B C   
2061 O O   . ILE B 61  ? 0.6252 0.5942 0.4615 0.0116  0.0653  0.0227  63  ILE B O   
2062 C CB  . ILE B 61  ? 0.5886 0.5613 0.4296 0.0219  0.0496  0.0326  63  ILE B CB  
2063 C CG1 . ILE B 61  ? 0.6102 0.6065 0.4585 0.0276  0.0456  0.0346  63  ILE B CG1 
2064 C CG2 . ILE B 61  ? 0.5883 0.5505 0.4274 0.0333  0.0544  0.0394  63  ILE B CG2 
2065 C CD1 . ILE B 61  ? 0.6432 0.6773 0.5017 0.0346  0.0464  0.0335  63  ILE B CD1 
2066 N N   . SER B 62  ? 0.6031 0.5342 0.4235 -0.0013 0.0564  0.0206  64  SER B N   
2067 C CA  . SER B 62  ? 0.6114 0.5130 0.4175 -0.0040 0.0602  0.0202  64  SER B CA  
2068 C C   . SER B 62  ? 0.5958 0.4681 0.3871 -0.0132 0.0559  0.0172  64  SER B C   
2069 O O   . SER B 62  ? 0.5691 0.4407 0.3625 -0.0156 0.0494  0.0170  64  SER B O   
2070 C CB  . SER B 62  ? 0.6533 0.5415 0.4569 0.0072  0.0604  0.0270  64  SER B CB  
2071 O OG  . SER B 62  ? 0.7636 0.6252 0.5524 0.0052  0.0645  0.0259  64  SER B OG  
2072 N N   . LYS B 63  ? 0.5851 0.4330 0.3607 -0.0175 0.0598  0.0152  65  LYS B N   
2073 C CA  . LYS B 63  ? 0.6035 0.4194 0.3608 -0.0242 0.0558  0.0130  65  LYS B CA  
2074 C C   . LYS B 63  ? 0.6179 0.4043 0.3596 -0.0196 0.0544  0.0154  65  LYS B C   
2075 O O   . LYS B 63  ? 0.6240 0.4116 0.3649 -0.0151 0.0609  0.0168  65  LYS B O   
2076 C CB  . LYS B 63  ? 0.6070 0.4181 0.3549 -0.0355 0.0624  0.0069  65  LYS B CB  
2077 C CG  . LYS B 63  ? 0.5853 0.4255 0.3486 -0.0416 0.0639  0.0027  65  LYS B CG  
2078 C CD  . LYS B 63  ? 0.6377 0.4674 0.3904 -0.0542 0.0708  -0.0038 65  LYS B CD  
2079 C CE  . LYS B 63  ? 0.6391 0.4945 0.4056 -0.0622 0.0722  -0.0098 65  LYS B CE  
2080 N NZ  . LYS B 63  ? 0.6428 0.4812 0.3962 -0.0757 0.0806  -0.0164 65  LYS B NZ  
2081 N N   . PHE B 64  ? 0.6188 0.3790 0.3480 -0.0206 0.0460  0.0153  66  PHE B N   
2082 C CA  . PHE B 64  ? 0.6434 0.3750 0.3567 -0.0168 0.0425  0.0161  66  PHE B CA  
2083 C C   . PHE B 64  ? 0.6745 0.3786 0.3702 -0.0200 0.0342  0.0139  66  PHE B C   
2084 O O   . PHE B 64  ? 0.6609 0.3688 0.3609 -0.0233 0.0294  0.0129  66  PHE B O   
2085 C CB  . PHE B 64  ? 0.6330 0.3687 0.3585 -0.0084 0.0382  0.0200  66  PHE B CB  
2086 C CG  . PHE B 64  ? 0.6066 0.3506 0.3468 -0.0073 0.0293  0.0213  66  PHE B CG  
2087 C CD1 . PHE B 64  ? 0.6147 0.3385 0.3489 -0.0079 0.0190  0.0196  66  PHE B CD1 
2088 C CD2 . PHE B 64  ? 0.6042 0.3768 0.3633 -0.0059 0.0313  0.0236  66  PHE B CD2 
2089 C CE1 . PHE B 64  ? 0.6076 0.3405 0.3571 -0.0073 0.0122  0.0203  66  PHE B CE1 
2090 C CE2 . PHE B 64  ? 0.5868 0.3655 0.3578 -0.0051 0.0248  0.0247  66  PHE B CE2 
2091 C CZ  . PHE B 64  ? 0.5841 0.3430 0.3511 -0.0061 0.0159  0.0231  66  PHE B CZ  
2092 N N   . ASP B 65  ? 0.7136 0.3889 0.3877 -0.0184 0.0322  0.0130  67  ASP B N   
2093 C CA  . ASP B 65  ? 0.7337 0.3806 0.3877 -0.0191 0.0229  0.0110  67  ASP B CA  
2094 C C   . ASP B 65  ? 0.7530 0.3761 0.3930 -0.0139 0.0149  0.0101  67  ASP B C   
2095 O O   . ASP B 65  ? 0.7794 0.3751 0.3953 -0.0135 0.0086  0.0081  67  ASP B O   
2096 C CB  . ASP B 65  ? 0.8119 0.4428 0.4437 -0.0253 0.0307  0.0091  67  ASP B CB  
2097 C CG  . ASP B 65  ? 0.9451 0.5673 0.5622 -0.0267 0.0434  0.0086  67  ASP B CG  
2098 O OD1 . ASP B 65  ? 1.0108 0.6323 0.6291 -0.0217 0.0439  0.0095  67  ASP B OD1 
2099 O OD2 . ASP B 65  ? 1.0488 0.6649 0.6542 -0.0329 0.0536  0.0070  67  ASP B OD2 
2100 N N   . THR B 66  ? 0.7414 0.3733 0.3948 -0.0096 0.0147  0.0112  68  THR B N   
2101 C CA  . THR B 66  ? 0.7583 0.3714 0.4042 -0.0055 0.0059  0.0091  68  THR B CA  
2102 C C   . THR B 66  ? 0.7238 0.3548 0.3972 -0.0025 0.0020  0.0105  68  THR B C   
2103 O O   . THR B 66  ? 0.6994 0.3550 0.3928 -0.0019 0.0090  0.0142  68  THR B O   
2104 C CB  . THR B 66  ? 0.7926 0.3884 0.4190 -0.0037 0.0136  0.0082  68  THR B CB  
2105 O OG1 . THR B 66  ? 0.8265 0.4415 0.4703 -0.0011 0.0236  0.0111  68  THR B OG1 
2106 C CG2 . THR B 66  ? 0.8074 0.3859 0.4070 -0.0068 0.0215  0.0074  68  THR B CG2 
2107 N N   . VAL B 67  ? 0.7527 0.3705 0.4259 -0.0007 -0.0087 0.0072  69  VAL B N   
2108 C CA  . VAL B 67  ? 0.7402 0.3694 0.4375 0.0012  -0.0115 0.0075  69  VAL B CA  
2109 C C   . VAL B 67  ? 0.7419 0.3787 0.4464 0.0041  0.0004  0.0109  69  VAL B C   
2110 O O   . VAL B 67  ? 0.7224 0.3784 0.4490 0.0061  0.0051  0.0149  69  VAL B O   
2111 C CB  . VAL B 67  ? 0.7591 0.3703 0.4527 0.0016  -0.0251 0.0013  69  VAL B CB  
2112 C CG1 . VAL B 67  ? 0.7615 0.3841 0.4818 0.0020  -0.0258 0.0009  69  VAL B CG1 
2113 C CG2 . VAL B 67  ? 0.7498 0.3540 0.4362 0.0009  -0.0379 -0.0018 69  VAL B CG2 
2114 N N   . GLU B 68  ? 0.7440 0.3641 0.4284 0.0054  0.0062  0.0097  70  GLU B N   
2115 C CA  . GLU B 68  ? 0.7513 0.3762 0.4413 0.0095  0.0179  0.0129  70  GLU B CA  
2116 C C   . GLU B 68  ? 0.7210 0.3725 0.4237 0.0117  0.0292  0.0189  70  GLU B C   
2117 O O   . GLU B 68  ? 0.7308 0.3956 0.4485 0.0167  0.0361  0.0233  70  GLU B O   
2118 C CB  . GLU B 68  ? 0.8278 0.4274 0.4925 0.0107  0.0219  0.0096  70  GLU B CB  
2119 C CG  . GLU B 68  ? 0.9077 0.4824 0.5617 0.0095  0.0105  0.0027  70  GLU B CG  
2120 C CD  . GLU B 68  ? 0.9772 0.5379 0.6160 0.0064  -0.0040 -0.0024 70  GLU B CD  
2121 O OE1 . GLU B 68  ? 0.9557 0.5195 0.5860 0.0049  -0.0037 -0.0005 70  GLU B OE1 
2122 O OE2 . GLU B 68  ? 1.0426 0.5888 0.6780 0.0057  -0.0158 -0.0087 70  GLU B OE2 
2123 N N   . ASP B 69  ? 0.7142 0.3734 0.4110 0.0083  0.0310  0.0190  71  ASP B N   
2124 C CA  . ASP B 69  ? 0.6956 0.3832 0.4060 0.0093  0.0401  0.0230  71  ASP B CA  
2125 C C   . ASP B 69  ? 0.6670 0.3772 0.4001 0.0101  0.0359  0.0260  71  ASP B C   
2126 O O   . ASP B 69  ? 0.6687 0.4024 0.4168 0.0146  0.0424  0.0304  71  ASP B O   
2127 C CB  . ASP B 69  ? 0.7251 0.4124 0.4226 0.0036  0.0438  0.0207  71  ASP B CB  
2128 C CG  . ASP B 69  ? 0.8436 0.5107 0.5189 0.0036  0.0518  0.0186  71  ASP B CG  
2129 O OD1 . ASP B 69  ? 0.8471 0.5131 0.5236 0.0093  0.0585  0.0201  71  ASP B OD1 
2130 O OD2 . ASP B 69  ? 0.9239 0.5746 0.5795 -0.0017 0.0521  0.0156  71  ASP B OD2 
2131 N N   . PHE B 70  ? 0.6539 0.3571 0.3892 0.0066  0.0252  0.0237  72  PHE B N   
2132 C CA  . PHE B 70  ? 0.6378 0.3584 0.3944 0.0077  0.0216  0.0263  72  PHE B CA  
2133 C C   . PHE B 70  ? 0.6459 0.3706 0.4148 0.0139  0.0265  0.0304  72  PHE B C   
2134 O O   . PHE B 70  ? 0.6415 0.3870 0.4237 0.0182  0.0321  0.0354  72  PHE B O   
2135 C CB  . PHE B 70  ? 0.6231 0.3323 0.3809 0.0039  0.0095  0.0225  72  PHE B CB  
2136 C CG  . PHE B 70  ? 0.6115 0.3351 0.3915 0.0055  0.0076  0.0249  72  PHE B CG  
2137 C CD1 . PHE B 70  ? 0.6062 0.3519 0.3972 0.0053  0.0104  0.0277  72  PHE B CD1 
2138 C CD2 . PHE B 70  ? 0.6118 0.3266 0.4013 0.0068  0.0044  0.0238  72  PHE B CD2 
2139 C CE1 . PHE B 70  ? 0.6025 0.3595 0.4115 0.0072  0.0103  0.0303  72  PHE B CE1 
2140 C CE2 . PHE B 70  ? 0.6093 0.3361 0.4191 0.0079  0.0052  0.0262  72  PHE B CE2 
2141 C CZ  . PHE B 70  ? 0.6138 0.3613 0.4323 0.0086  0.0086  0.0300  72  PHE B CZ  
2142 N N   . TRP B 71  ? 0.6650 0.3682 0.4281 0.0146  0.0245  0.0279  73  TRP B N   
2143 C CA  . TRP B 71  ? 0.6629 0.3648 0.4363 0.0197  0.0301  0.0312  73  TRP B CA  
2144 C C   . TRP B 71  ? 0.6713 0.3839 0.4445 0.0275  0.0427  0.0371  73  TRP B C   
2145 O O   . TRP B 71  ? 0.6630 0.3846 0.4480 0.0334  0.0486  0.0426  73  TRP B O   
2146 C CB  . TRP B 71  ? 0.6727 0.3486 0.4396 0.0177  0.0255  0.0257  73  TRP B CB  
2147 C CG  . TRP B 71  ? 0.6539 0.3243 0.4295 0.0123  0.0136  0.0204  73  TRP B CG  
2148 C CD1 . TRP B 71  ? 0.6705 0.3241 0.4348 0.0080  0.0020  0.0130  73  TRP B CD1 
2149 C CD2 . TRP B 71  ? 0.6287 0.3103 0.4265 0.0117  0.0125  0.0219  73  TRP B CD2 
2150 N NE1 . TRP B 71  ? 0.6698 0.3266 0.4501 0.0049  -0.0073 0.0095  73  TRP B NE1 
2151 C CE2 . TRP B 71  ? 0.6415 0.3147 0.4432 0.0065  -0.0002 0.0147  73  TRP B CE2 
2152 C CE3 . TRP B 71  ? 0.6280 0.3263 0.4417 0.0155  0.0211  0.0288  73  TRP B CE3 
2153 C CZ2 . TRP B 71  ? 0.6394 0.3216 0.4631 0.0043  -0.0036 0.0136  73  TRP B CZ2 
2154 C CZ3 . TRP B 71  ? 0.6158 0.3202 0.4482 0.0132  0.0184  0.0282  73  TRP B CZ3 
2155 C CH2 . TRP B 71  ? 0.6101 0.3067 0.4488 0.0073  0.0068  0.0205  73  TRP B CH2 
2156 N N   . ALA B 72  ? 0.6884 0.4003 0.4486 0.0280  0.0472  0.0362  74  ALA B N   
2157 C CA  . ALA B 72  ? 0.6896 0.4145 0.4511 0.0361  0.0587  0.0412  74  ALA B CA  
2158 C C   . ALA B 72  ? 0.6566 0.4135 0.4330 0.0396  0.0607  0.0459  74  ALA B C   
2159 O O   . ALA B 72  ? 0.6512 0.4216 0.4360 0.0490  0.0676  0.0520  74  ALA B O   
2160 C CB  . ALA B 72  ? 0.7173 0.4354 0.4629 0.0344  0.0632  0.0378  74  ALA B CB  
2161 N N   . LEU B 73  ? 0.6341 0.4025 0.4130 0.0326  0.0543  0.0431  75  LEU B N   
2162 C CA  . LEU B 73  ? 0.6071 0.4051 0.3990 0.0346  0.0548  0.0461  75  LEU B CA  
2163 C C   . LEU B 73  ? 0.5842 0.3861 0.3877 0.0388  0.0532  0.0508  75  LEU B C   
2164 O O   . LEU B 73  ? 0.5847 0.4060 0.3962 0.0467  0.0575  0.0562  75  LEU B O   
2165 C CB  . LEU B 73  ? 0.6128 0.4174 0.4026 0.0250  0.0491  0.0409  75  LEU B CB  
2166 C CG  . LEU B 73  ? 0.6102 0.4445 0.4120 0.0251  0.0485  0.0420  75  LEU B CG  
2167 C CD1 . LEU B 73  ? 0.6168 0.4773 0.4250 0.0322  0.0558  0.0445  75  LEU B CD1 
2168 C CD2 . LEU B 73  ? 0.6294 0.4644 0.4268 0.0146  0.0442  0.0361  75  LEU B CD2 
2169 N N   . TYR B 74  ? 0.5978 0.3819 0.4022 0.0338  0.0470  0.0484  76  TYR B N   
2170 C CA  . TYR B 74  ? 0.6184 0.4031 0.4345 0.0363  0.0467  0.0520  76  TYR B CA  
2171 C C   . TYR B 74  ? 0.6402 0.4211 0.4584 0.0461  0.0561  0.0585  76  TYR B C   
2172 O O   . TYR B 74  ? 0.6121 0.4060 0.4375 0.0529  0.0606  0.0648  76  TYR B O   
2173 C CB  . TYR B 74  ? 0.6299 0.3952 0.4480 0.0287  0.0385  0.0466  76  TYR B CB  
2174 C CG  . TYR B 74  ? 0.6209 0.3879 0.4537 0.0299  0.0396  0.0494  76  TYR B CG  
2175 C CD1 . TYR B 74  ? 0.6061 0.3883 0.4475 0.0281  0.0367  0.0500  76  TYR B CD1 
2176 C CD2 . TYR B 74  ? 0.6227 0.3747 0.4601 0.0324  0.0449  0.0511  76  TYR B CD2 
2177 C CE1 . TYR B 74  ? 0.6073 0.3902 0.4616 0.0292  0.0395  0.0527  76  TYR B CE1 
2178 C CE2 . TYR B 74  ? 0.6258 0.3781 0.4768 0.0328  0.0479  0.0536  76  TYR B CE2 
2179 C CZ  . TYR B 74  ? 0.6362 0.4042 0.4957 0.0313  0.0453  0.0545  76  TYR B CZ  
2180 O OH  . TYR B 74  ? 0.6597 0.4273 0.5323 0.0317  0.0500  0.0571  76  TYR B OH  
2181 N N   . ASN B 75  ? 0.6775 0.4392 0.4875 0.0473  0.0595  0.0572  77  ASN B N   
2182 C CA  . ASN B 75  ? 0.7251 0.4784 0.5348 0.0569  0.0698  0.0631  77  ASN B CA  
2183 C C   . ASN B 75  ? 0.7593 0.5353 0.5695 0.0688  0.0772  0.0705  77  ASN B C   
2184 O O   . ASN B 75  ? 0.7868 0.5651 0.6003 0.0786  0.0844  0.0780  77  ASN B O   
2185 C CB  . ASN B 75  ? 0.7798 0.5067 0.5787 0.0549  0.0715  0.0587  77  ASN B CB  
2186 C CG  . ASN B 75  ? 0.8717 0.5768 0.6720 0.0450  0.0638  0.0515  77  ASN B CG  
2187 O OD1 . ASN B 75  ? 0.8951 0.6007 0.7075 0.0420  0.0614  0.0516  77  ASN B OD1 
2188 N ND2 . ASN B 75  ? 0.9011 0.5870 0.6890 0.0398  0.0594  0.0445  77  ASN B ND2 
2189 N N   . HIS B 76  ? 0.7572 0.5505 0.5647 0.0681  0.0755  0.0681  78  HIS B N   
2190 C CA  . HIS B 76  ? 0.7681 0.5876 0.5786 0.0786  0.0806  0.0730  78  HIS B CA  
2191 C C   . HIS B 76  ? 0.7562 0.6007 0.5755 0.0826  0.0781  0.0771  78  HIS B C   
2192 O O   . HIS B 76  ? 0.7737 0.6323 0.5949 0.0955  0.0833  0.0842  78  HIS B O   
2193 C CB  . HIS B 76  ? 0.7965 0.6278 0.6039 0.0740  0.0798  0.0673  78  HIS B CB  
2194 C CG  . HIS B 76  ? 0.8739 0.7379 0.6884 0.0828  0.0832  0.0699  78  HIS B CG  
2195 N ND1 . HIS B 76  ? 0.9032 0.7940 0.7246 0.0772  0.0780  0.0659  78  HIS B ND1 
2196 C CD2 . HIS B 76  ? 0.9057 0.7797 0.7220 0.0967  0.0908  0.0754  78  HIS B CD2 
2197 C CE1 . HIS B 76  ? 0.9122 0.8308 0.7408 0.0874  0.0818  0.0684  78  HIS B CE1 
2198 N NE2 . HIS B 76  ? 0.9194 0.8294 0.7452 0.1001  0.0893  0.0745  78  HIS B NE2 
2199 N N   . ILE B 77  ? 0.7340 0.5834 0.5570 0.0726  0.0703  0.0729  79  ILE B N   
2200 C CA  . ILE B 77  ? 0.7343 0.6056 0.5637 0.0754  0.0678  0.0757  79  ILE B CA  
2201 C C   . ILE B 77  ? 0.7614 0.6205 0.5920 0.0823  0.0725  0.0830  79  ILE B C   
2202 O O   . ILE B 77  ? 0.7611 0.6361 0.5926 0.0920  0.0750  0.0892  79  ILE B O   
2203 C CB  . ILE B 77  ? 0.7265 0.6025 0.5586 0.0624  0.0592  0.0688  79  ILE B CB  
2204 C CG1 . ILE B 77  ? 0.7297 0.6145 0.5590 0.0542  0.0561  0.0614  79  ILE B CG1 
2205 C CG2 . ILE B 77  ? 0.7269 0.6238 0.5640 0.0655  0.0573  0.0714  79  ILE B CG2 
2206 C CD1 . ILE B 77  ? 0.7304 0.6427 0.5628 0.0596  0.0587  0.0614  79  ILE B CD1 
2207 N N   . GLN B 78  ? 0.8020 0.6333 0.6324 0.0770  0.0736  0.0817  80  GLN B N   
2208 C CA  . GLN B 78  ? 0.8626 0.6787 0.6955 0.0815  0.0802  0.0876  80  GLN B CA  
2209 C C   . GLN B 78  ? 0.9236 0.7378 0.7505 0.0971  0.0909  0.0968  80  GLN B C   
2210 O O   . GLN B 78  ? 0.9243 0.7366 0.7507 0.1050  0.0972  0.1043  80  GLN B O   
2211 C CB  . GLN B 78  ? 0.8845 0.6723 0.7206 0.0713  0.0789  0.0821  80  GLN B CB  
2212 C CG  . GLN B 78  ? 0.9240 0.7042 0.7697 0.0677  0.0806  0.0832  80  GLN B CG  
2213 C CD  . GLN B 78  ? 0.9567 0.7136 0.8097 0.0576  0.0786  0.0766  80  GLN B CD  
2214 O OE1 . GLN B 78  ? 0.9839 0.7399 0.8481 0.0517  0.0768  0.0744  80  GLN B OE1 
2215 N NE2 . GLN B 78  ? 0.9253 0.6640 0.7733 0.0551  0.0786  0.0724  80  GLN B NE2 
2216 N N   . LEU B 79  ? 0.9780 0.7916 0.7993 0.1020  0.0935  0.0965  81  LEU B N   
2217 C CA  . LEU B 79  ? 1.0250 0.8420 0.8406 0.1187  0.1027  0.1050  81  LEU B CA  
2218 C C   . LEU B 79  ? 1.0579 0.9117 0.8751 0.1281  0.0993  0.1074  81  LEU B C   
2219 O O   . LEU B 79  ? 1.0632 0.9296 0.8796 0.1352  0.1010  0.1074  81  LEU B O   
2220 C CB  . LEU B 79  ? 1.0480 0.8478 0.8577 0.1195  0.1074  0.1024  81  LEU B CB  
2221 C CG  . LEU B 79  ? 1.0910 0.8541 0.8966 0.1158  0.1138  0.1015  81  LEU B CG  
2222 C CD1 . LEU B 79  ? 1.1026 0.8519 0.9001 0.1181  0.1185  0.0987  81  LEU B CD1 
2223 C CD2 . LEU B 79  ? 1.1069 0.8561 0.9102 0.1264  0.1246  0.1111  81  LEU B CD2 
2224 N N   . SER B 80  ? 1.0759 0.9478 0.8962 0.1279  0.0944  0.1086  82  SER B N   
2225 C CA  . SER B 80  ? 1.0873 0.9949 0.9092 0.1367  0.0903  0.1101  82  SER B CA  
2226 C C   . SER B 80  ? 1.1072 1.0244 0.9274 0.1401  0.0882  0.1143  82  SER B C   
2227 O O   . SER B 80  ? 1.1138 1.0595 0.9371 0.1389  0.0807  0.1107  82  SER B O   
2228 C CB  . SER B 80  ? 1.0922 1.0208 0.9209 0.1251  0.0820  0.0998  82  SER B CB  
2229 O OG  . SER B 80  ? 1.1198 1.0388 0.9482 0.1218  0.0848  0.0957  82  SER B OG  
2230 N N   . SER B 81  ? 1.1138 1.0069 0.9288 0.1440  0.0957  0.1214  83  SER B N   
2231 C CA  . SER B 81  ? 1.1124 1.0093 0.9240 0.1468  0.0960  0.1258  83  SER B CA  
2232 C C   . SER B 81  ? 1.0947 1.0038 0.9137 0.1311  0.0863  0.1165  83  SER B C   
2233 O O   . SER B 81  ? 1.0965 1.0242 0.9129 0.1338  0.0826  0.1172  83  SER B O   
2234 C CB  . SER B 81  ? 1.1289 1.0484 0.9315 0.1659  0.0966  0.1338  83  SER B CB  
2235 O OG  . SER B 81  ? 1.1699 1.0758 0.9642 0.1820  0.1063  0.1432  83  SER B OG  
2236 N N   . ASN B 82  ? 1.0729 0.9697 0.8995 0.1155  0.0825  0.1080  84  ASN B N   
2237 C CA  . ASN B 82  ? 1.0534 0.9542 0.8869 0.0998  0.0740  0.0987  84  ASN B CA  
2238 C C   . ASN B 82  ? 1.0373 0.9400 0.8716 0.0975  0.0736  0.0998  84  ASN B C   
2239 O O   . ASN B 82  ? 1.0535 0.9446 0.8842 0.1050  0.0816  0.1074  84  ASN B O   
2240 C CB  . ASN B 82  ? 1.0695 0.9446 0.9077 0.0878  0.0733  0.0932  84  ASN B CB  
2241 C CG  . ASN B 82  ? 1.0918 0.9411 0.9327 0.0874  0.0804  0.0970  84  ASN B CG  
2242 O OD1 . ASN B 82  ? 1.1198 0.9595 0.9559 0.0982  0.0900  0.1053  84  ASN B OD1 
2243 N ND2 . ASN B 82  ? 1.0762 0.9136 0.9252 0.0754  0.0765  0.0909  84  ASN B ND2 
2244 N N   . LEU B 83  ? 1.0090 0.9242 0.8473 0.0870  0.0656  0.0920  85  LEU B N   
2245 C CA  . LEU B 83  ? 0.9884 0.9055 0.8277 0.0837  0.0651  0.0915  85  LEU B CA  
2246 C C   . LEU B 83  ? 0.9883 0.9195 0.8180 0.0975  0.0690  0.0992  85  LEU B C   
2247 O O   . LEU B 83  ? 0.9891 0.9071 0.8151 0.1032  0.0769  0.1061  85  LEU B O   
2248 C CB  . LEU B 83  ? 0.9740 0.8648 0.8209 0.0770  0.0693  0.0915  85  LEU B CB  
2249 C CG  . LEU B 83  ? 0.9595 0.8376 0.8146 0.0639  0.0630  0.0829  85  LEU B CG  
2250 C CD1 . LEU B 83  ? 0.9572 0.8149 0.8222 0.0583  0.0658  0.0819  85  LEU B CD1 
2251 C CD2 . LEU B 83  ? 0.9546 0.8464 0.8104 0.0546  0.0536  0.0745  85  LEU B CD2 
2252 N N   . MET B 84  ? 0.9859 0.9445 0.8113 0.1028  0.0635  0.0975  86  MET B N   
2253 C CA  . MET B 84  ? 0.9977 0.9749 0.8124 0.1177  0.0644  0.1038  86  MET B CA  
2254 C C   . MET B 84  ? 1.0028 0.9878 0.8123 0.1155  0.0624  0.1020  86  MET B C   
2255 O O   . MET B 84  ? 1.0113 0.9951 0.8273 0.1015  0.0582  0.0938  86  MET B O   
2256 C CB  . MET B 84  ? 1.0081 1.0151 0.8238 0.1227  0.0576  0.1003  86  MET B CB  
2257 C CG  . MET B 84  ? 1.0693 1.0694 0.8880 0.1281  0.0613  0.1033  86  MET B CG  
2258 S SD  . MET B 84  ? 1.1605 1.1956 0.9773 0.1452  0.0579  0.1057  86  MET B SD  
2259 C CE  . MET B 84  ? 1.1079 1.1535 0.9390 0.1317  0.0538  0.0943  86  MET B CE  
2260 N N   . PRO B 85  ? 0.9940 0.9865 0.7898 0.1297  0.0653  0.1095  87  PRO B N   
2261 C CA  . PRO B 85  ? 0.9911 0.9757 0.7795 0.1291  0.0692  0.1113  87  PRO B CA  
2262 C C   . PRO B 85  ? 0.9562 0.9615 0.7423 0.1221  0.0610  0.1024  87  PRO B C   
2263 O O   . PRO B 85  ? 0.9744 0.9721 0.7527 0.1225  0.0653  0.1042  87  PRO B O   
2264 C CB  . PRO B 85  ? 1.0153 0.9955 0.7860 0.1487  0.0769  0.1240  87  PRO B CB  
2265 C CG  . PRO B 85  ? 1.0219 1.0237 0.7899 0.1608  0.0713  0.1259  87  PRO B CG  
2266 C CD  . PRO B 85  ? 0.9916 1.0001 0.7770 0.1482  0.0651  0.1167  87  PRO B CD  
2267 N N   . GLY B 86  ? 0.8994 0.9290 0.6915 0.1157  0.0509  0.0929  88  GLY B N   
2268 C CA  . GLY B 86  ? 0.8603 0.9054 0.6531 0.1046  0.0437  0.0819  88  GLY B CA  
2269 C C   . GLY B 86  ? 0.8207 0.8746 0.6270 0.0899  0.0369  0.0708  88  GLY B C   
2270 O O   . GLY B 86  ? 0.8230 0.8993 0.6304 0.0834  0.0298  0.0612  88  GLY B O   
2271 N N   . CYS B 87  ? 0.7825 0.8176 0.5984 0.0843  0.0398  0.0718  89  CYS B N   
2272 C CA  . CYS B 87  ? 0.7392 0.7786 0.5648 0.0726  0.0352  0.0632  89  CYS B CA  
2273 C C   . CYS B 87  ? 0.6784 0.6944 0.5099 0.0585  0.0357  0.0585  89  CYS B C   
2274 O O   . CYS B 87  ? 0.6741 0.6700 0.5059 0.0584  0.0399  0.0624  89  CYS B O   
2275 C CB  . CYS B 87  ? 0.7718 0.8101 0.6009 0.0797  0.0374  0.0681  89  CYS B CB  
2276 S SG  . CYS B 87  ? 0.8642 0.9310 0.6870 0.0990  0.0364  0.0742  89  CYS B SG  
2277 N N   . ASP B 88  ? 0.6243 0.6434 0.4607 0.0470  0.0316  0.0498  90  ASP B N   
2278 C CA  . ASP B 88  ? 0.6005 0.5971 0.4407 0.0352  0.0310  0.0454  90  ASP B CA  
2279 C C   . ASP B 88  ? 0.5654 0.5535 0.4088 0.0311  0.0306  0.0438  90  ASP B C   
2280 O O   . ASP B 88  ? 0.5670 0.5725 0.4110 0.0310  0.0296  0.0408  90  ASP B O   
2281 C CB  . ASP B 88  ? 0.6377 0.6405 0.4765 0.0237  0.0273  0.0355  90  ASP B CB  
2282 C CG  . ASP B 88  ? 0.7759 0.7915 0.6094 0.0259  0.0270  0.0341  90  ASP B CG  
2283 O OD1 . ASP B 88  ? 0.7324 0.7405 0.5633 0.0340  0.0308  0.0412  90  ASP B OD1 
2284 O OD2 . ASP B 88  ? 0.8608 0.8925 0.6921 0.0189  0.0236  0.0253  90  ASP B OD2 
2285 N N   . TYR B 89  ? 0.5374 0.4997 0.3829 0.0275  0.0313  0.0451  91  TYR B N   
2286 C CA  . TYR B 89  ? 0.5273 0.4767 0.3726 0.0225  0.0304  0.0427  91  TYR B CA  
2287 C C   . TYR B 89  ? 0.5178 0.4499 0.3621 0.0117  0.0269  0.0366  91  TYR B C   
2288 O O   . TYR B 89  ? 0.4926 0.4143 0.3398 0.0109  0.0260  0.0372  91  TYR B O   
2289 C CB  . TYR B 89  ? 0.5567 0.4892 0.4036 0.0293  0.0337  0.0495  91  TYR B CB  
2290 C CG  . TYR B 89  ? 0.6347 0.5808 0.4810 0.0421  0.0384  0.0570  91  TYR B CG  
2291 C CD1 . TYR B 89  ? 0.6836 0.6352 0.5293 0.0501  0.0413  0.0627  91  TYR B CD1 
2292 C CD2 . TYR B 89  ? 0.6720 0.6248 0.5171 0.0471  0.0404  0.0584  91  TYR B CD2 
2293 C CE1 . TYR B 89  ? 0.7148 0.6774 0.5569 0.0636  0.0455  0.0703  91  TYR B CE1 
2294 C CE2 . TYR B 89  ? 0.6983 0.6632 0.5421 0.0608  0.0446  0.0658  91  TYR B CE2 
2295 C CZ  . TYR B 89  ? 0.7364 0.7059 0.5779 0.0693  0.0468  0.0719  91  TYR B CZ  
2296 O OH  . TYR B 89  ? 0.8065 0.7861 0.6438 0.0845  0.0509  0.0799  91  TYR B OH  
2297 N N   . SER B 90  ? 0.4929 0.4215 0.3327 0.0040  0.0255  0.0309  92  SER B N   
2298 C CA  . SER B 90  ? 0.5019 0.4120 0.3373 -0.0053 0.0223  0.0254  92  SER B CA  
2299 C C   . SER B 90  ? 0.5109 0.4019 0.3395 -0.0086 0.0217  0.0241  92  SER B C   
2300 O O   . SER B 90  ? 0.5451 0.4441 0.3711 -0.0088 0.0248  0.0234  92  SER B O   
2301 C CB  . SER B 90  ? 0.5135 0.4364 0.3458 -0.0134 0.0224  0.0182  92  SER B CB  
2302 O OG  . SER B 90  ? 0.5643 0.5068 0.4004 -0.0105 0.0228  0.0182  92  SER B OG  
2303 N N   . LEU B 91  ? 0.4999 0.3663 0.3250 -0.0107 0.0176  0.0234  93  LEU B N   
2304 C CA  . LEU B 91  ? 0.5042 0.3500 0.3183 -0.0141 0.0162  0.0213  93  LEU B CA  
2305 C C   . LEU B 91  ? 0.5039 0.3353 0.3087 -0.0216 0.0134  0.0160  93  LEU B C   
2306 O O   . LEU B 91  ? 0.4965 0.3183 0.3043 -0.0208 0.0087  0.0158  93  LEU B O   
2307 C CB  . LEU B 91  ? 0.5166 0.3439 0.3318 -0.0093 0.0125  0.0244  93  LEU B CB  
2308 C CG  . LEU B 91  ? 0.5355 0.3413 0.3360 -0.0116 0.0111  0.0223  93  LEU B CG  
2309 C CD1 . LEU B 91  ? 0.5603 0.3741 0.3578 -0.0095 0.0177  0.0240  93  LEU B CD1 
2310 C CD2 . LEU B 91  ? 0.5710 0.3559 0.3707 -0.0090 0.0044  0.0225  93  LEU B CD2 
2311 N N   . PHE B 92  ? 0.5124 0.3413 0.3063 -0.0284 0.0172  0.0119  94  PHE B N   
2312 C CA  . PHE B 92  ? 0.5078 0.3207 0.2902 -0.0355 0.0167  0.0071  94  PHE B CA  
2313 C C   . PHE B 92  ? 0.5449 0.3348 0.3095 -0.0388 0.0185  0.0056  94  PHE B C   
2314 O O   . PHE B 92  ? 0.5307 0.3235 0.2926 -0.0385 0.0228  0.0064  94  PHE B O   
2315 C CB  . PHE B 92  ? 0.4926 0.3248 0.2780 -0.0426 0.0219  0.0022  94  PHE B CB  
2316 C CG  . PHE B 92  ? 0.5180 0.3606 0.3133 -0.0405 0.0190  0.0022  94  PHE B CG  
2317 C CD1 . PHE B 92  ? 0.5489 0.4103 0.3573 -0.0332 0.0179  0.0066  94  PHE B CD1 
2318 C CD2 . PHE B 92  ? 0.5261 0.3568 0.3155 -0.0453 0.0185  -0.0018 94  PHE B CD2 
2319 C CE1 . PHE B 92  ? 0.5570 0.4255 0.3725 -0.0311 0.0166  0.0069  94  PHE B CE1 
2320 C CE2 . PHE B 92  ? 0.5349 0.3733 0.3327 -0.0429 0.0167  -0.0018 94  PHE B CE2 
2321 C CZ  . PHE B 92  ? 0.5415 0.3997 0.3522 -0.0363 0.0161  0.0023  94  PHE B CZ  
2322 N N   . LYS B 93  ? 0.5607 0.3257 0.3115 -0.0413 0.0156  0.0037  95  LYS B N   
2323 C CA  . LYS B 93  ? 0.5841 0.3232 0.3131 -0.0445 0.0182  0.0023  95  LYS B CA  
2324 C C   . LYS B 93  ? 0.5831 0.3329 0.3090 -0.0533 0.0296  -0.0015 95  LYS B C   
2325 O O   . LYS B 93  ? 0.5851 0.3545 0.3207 -0.0590 0.0338  -0.0051 95  LYS B O   
2326 C CB  . LYS B 93  ? 0.6168 0.3286 0.3305 -0.0448 0.0139  0.0011  95  LYS B CB  
2327 C CG  . LYS B 93  ? 0.6485 0.3478 0.3643 -0.0358 0.0019  0.0038  95  LYS B CG  
2328 C CD  . LYS B 93  ? 0.6515 0.3278 0.3547 -0.0342 -0.0031 0.0027  95  LYS B CD  
2329 C CE  . LYS B 93  ? 0.6802 0.3474 0.3877 -0.0250 -0.0158 0.0044  95  LYS B CE  
2330 N NZ  . LYS B 93  ? 0.7384 0.3861 0.4363 -0.0213 -0.0218 0.0034  95  LYS B NZ  
2331 N N   . ASP B 94  ? 0.6058 0.3436 0.3189 -0.0547 0.0348  -0.0014 96  ASP B N   
2332 C CA  . ASP B 94  ? 0.6305 0.3783 0.3423 -0.0634 0.0469  -0.0056 96  ASP B CA  
2333 C C   . ASP B 94  ? 0.6635 0.4030 0.3674 -0.0737 0.0527  -0.0111 96  ASP B C   
2334 O O   . ASP B 94  ? 0.7112 0.4198 0.3964 -0.0736 0.0504  -0.0105 96  ASP B O   
2335 C CB  . ASP B 94  ? 0.6929 0.4192 0.3868 -0.0625 0.0517  -0.0041 96  ASP B CB  
2336 C CG  . ASP B 94  ? 0.7501 0.4901 0.4468 -0.0694 0.0648  -0.0077 96  ASP B CG  
2337 O OD1 . ASP B 94  ? 0.7012 0.4746 0.4184 -0.0735 0.0686  -0.0112 96  ASP B OD1 
2338 O OD2 . ASP B 94  ? 0.8287 0.5470 0.5074 -0.0701 0.0711  -0.0072 96  ASP B OD2 
2339 N N   . GLY B 95  ? 0.6502 0.4171 0.3685 -0.0816 0.0593  -0.0166 97  GLY B N   
2340 C CA  . GLY B 95  ? 0.6790 0.4409 0.3923 -0.0928 0.0660  -0.0232 97  GLY B CA  
2341 C C   . GLY B 95  ? 0.6821 0.4552 0.4054 -0.0925 0.0599  -0.0249 97  GLY B C   
2342 O O   . GLY B 95  ? 0.7155 0.4830 0.4341 -0.1019 0.0654  -0.0310 97  GLY B O   
2343 N N   . ILE B 96  ? 0.6634 0.4501 0.3994 -0.0821 0.0496  -0.0199 98  ILE B N   
2344 C CA  . ILE B 96  ? 0.6475 0.4482 0.3945 -0.0809 0.0448  -0.0212 98  ILE B CA  
2345 C C   . ILE B 96  ? 0.6590 0.4991 0.4267 -0.0775 0.0432  -0.0210 98  ILE B C   
2346 O O   . ILE B 96  ? 0.6400 0.4889 0.4152 -0.0681 0.0390  -0.0149 98  ILE B O   
2347 C CB  . ILE B 96  ? 0.6517 0.4349 0.3964 -0.0711 0.0353  -0.0155 98  ILE B CB  
2348 C CG1 . ILE B 96  ? 0.6905 0.4345 0.4134 -0.0707 0.0344  -0.0143 98  ILE B CG1 
2349 C CG2 . ILE B 96  ? 0.6438 0.4409 0.3994 -0.0704 0.0325  -0.0173 98  ILE B CG2 
2350 C CD1 . ILE B 96  ? 0.7058 0.4343 0.4284 -0.0607 0.0241  -0.0099 98  ILE B CD1 
2351 N N   . GLU B 97  ? 0.6652 0.5282 0.4412 -0.0848 0.0464  -0.0280 99  GLU B N   
2352 C CA  . GLU B 97  ? 0.6842 0.5837 0.4773 -0.0798 0.0431  -0.0277 99  GLU B CA  
2353 C C   . GLU B 97  ? 0.6639 0.5638 0.4612 -0.0704 0.0358  -0.0223 99  GLU B C   
2354 O O   . GLU B 97  ? 0.6506 0.5306 0.4408 -0.0718 0.0345  -0.0230 99  GLU B O   
2355 C CB  . GLU B 97  ? 0.7402 0.6649 0.5402 -0.0905 0.0477  -0.0381 99  GLU B CB  
2356 C CG  . GLU B 97  ? 0.8857 0.8136 0.6857 -0.0997 0.0561  -0.0435 99  GLU B CG  
2357 C CD  . GLU B 97  ? 1.1139 1.0769 0.9276 -0.1089 0.0598  -0.0541 99  GLU B CD  
2358 O OE1 . GLU B 97  ? 1.1745 1.1502 0.9915 -0.1131 0.0574  -0.0603 99  GLU B OE1 
2359 O OE2 . GLU B 97  ? 1.1972 1.1758 1.0189 -0.1120 0.0651  -0.0570 99  GLU B OE2 
2360 N N   . PRO B 98  ? 0.6622 0.5829 0.4705 -0.0600 0.0320  -0.0165 100 PRO B N   
2361 C CA  . PRO B 98  ? 0.6694 0.5894 0.4817 -0.0515 0.0272  -0.0113 100 PRO B CA  
2362 C C   . PRO B 98  ? 0.6566 0.5951 0.4718 -0.0541 0.0272  -0.0164 100 PRO B C   
2363 O O   . PRO B 98  ? 0.6673 0.6234 0.4887 -0.0462 0.0250  -0.0128 100 PRO B O   
2364 C CB  . PRO B 98  ? 0.6777 0.6097 0.4980 -0.0401 0.0255  -0.0032 100 PRO B CB  
2365 C CG  . PRO B 98  ? 0.6698 0.6256 0.4942 -0.0424 0.0286  -0.0066 100 PRO B CG  
2366 C CD  . PRO B 98  ? 0.6639 0.6071 0.4806 -0.0548 0.0331  -0.0140 100 PRO B CD  
2367 N N   . MET B 99  ? 0.6533 0.5859 0.4622 -0.0654 0.0302  -0.0251 101 MET B N   
2368 C CA  . MET B 99  ? 0.6515 0.5979 0.4608 -0.0693 0.0304  -0.0315 101 MET B CA  
2369 C C   . MET B 99  ? 0.6446 0.5620 0.4439 -0.0754 0.0325  -0.0350 101 MET B C   
2370 O O   . MET B 99  ? 0.6193 0.5126 0.4099 -0.0813 0.0355  -0.0364 101 MET B O   
2371 C CB  . MET B 99  ? 0.6870 0.6610 0.5004 -0.0780 0.0327  -0.0410 101 MET B CB  
2372 C CG  . MET B 99  ? 0.8088 0.7708 0.6173 -0.0914 0.0389  -0.0487 101 MET B CG  
2373 S SD  . MET B 99  ? 1.1057 1.1067 0.9256 -0.1012 0.0417  -0.0602 101 MET B SD  
2374 C CE  . MET B 99  ? 1.0439 1.0660 0.8750 -0.0870 0.0382  -0.0504 101 MET B CE  
2375 N N   . TRP B 100 ? 0.6695 0.5881 0.4685 -0.0731 0.0315  -0.0360 102 TRP B N   
2376 C CA  . TRP B 100 ? 0.7202 0.6107 0.5112 -0.0753 0.0331  -0.0373 102 TRP B CA  
2377 C C   . TRP B 100 ? 0.7243 0.6027 0.5048 -0.0889 0.0390  -0.0472 102 TRP B C   
2378 O O   . TRP B 100 ? 0.7458 0.5946 0.5168 -0.0902 0.0409  -0.0472 102 TRP B O   
2379 C CB  . TRP B 100 ? 0.7478 0.6415 0.5412 -0.0693 0.0321  -0.0362 102 TRP B CB  
2380 C CG  . TRP B 100 ? 0.7786 0.6866 0.5679 -0.0764 0.0350  -0.0456 102 TRP B CG  
2381 C CD1 . TRP B 100 ? 0.7977 0.7365 0.5905 -0.0761 0.0334  -0.0487 102 TRP B CD1 
2382 C CD2 . TRP B 100 ? 0.7994 0.6908 0.5794 -0.0840 0.0394  -0.0534 102 TRP B CD2 
2383 N NE1 . TRP B 100 ? 0.8088 0.7521 0.5949 -0.0839 0.0360  -0.0588 102 TRP B NE1 
2384 C CE2 . TRP B 100 ? 0.8058 0.7193 0.5841 -0.0892 0.0404  -0.0619 102 TRP B CE2 
2385 C CE3 . TRP B 100 ? 0.8260 0.6851 0.5980 -0.0861 0.0425  -0.0542 102 TRP B CE3 
2386 C CZ2 . TRP B 100 ? 0.8150 0.7186 0.5839 -0.0975 0.0451  -0.0715 102 TRP B CZ2 
2387 C CZ3 . TRP B 100 ? 0.8427 0.6913 0.6055 -0.0933 0.0477  -0.0628 102 TRP B CZ3 
2388 C CH2 . TRP B 100 ? 0.8330 0.7033 0.5944 -0.0996 0.0493  -0.0716 102 TRP B CH2 
2389 N N   . GLU B 101 ? 0.7144 0.6152 0.4971 -0.0986 0.0419  -0.0559 103 GLU B N   
2390 C CA  . GLU B 101 ? 0.7400 0.6318 0.5147 -0.1138 0.0493  -0.0670 103 GLU B CA  
2391 C C   . GLU B 101 ? 0.7609 0.6316 0.5286 -0.1192 0.0543  -0.0660 103 GLU B C   
2392 O O   . GLU B 101 ? 0.7938 0.6496 0.5525 -0.1318 0.0623  -0.0741 103 GLU B O   
2393 C CB  . GLU B 101 ? 0.7907 0.7180 0.5734 -0.1229 0.0502  -0.0779 103 GLU B CB  
2394 C CG  . GLU B 101 ? 0.8903 0.8415 0.6771 -0.1179 0.0453  -0.0801 103 GLU B CG  
2395 C CD  . GLU B 101 ? 1.0184 0.9935 0.8146 -0.1032 0.0379  -0.0705 103 GLU B CD  
2396 O OE1 . GLU B 101 ? 1.0127 0.9901 0.8146 -0.0974 0.0364  -0.0631 103 GLU B OE1 
2397 O OE2 . GLU B 101 ? 1.0603 1.0497 0.8563 -0.0971 0.0345  -0.0704 103 GLU B OE2 
2398 N N   . ASP B 102 ? 0.7271 0.5942 0.4972 -0.1102 0.0506  -0.0565 104 ASP B N   
2399 C CA  . ASP B 102 ? 0.7219 0.5627 0.4811 -0.1131 0.0550  -0.0542 104 ASP B CA  
2400 C C   . ASP B 102 ? 0.7329 0.5337 0.4747 -0.1138 0.0574  -0.0535 104 ASP B C   
2401 O O   . ASP B 102 ? 0.7280 0.5215 0.4702 -0.1060 0.0524  -0.0501 104 ASP B O   
2402 C CB  . ASP B 102 ? 0.7114 0.5523 0.4746 -0.1012 0.0491  -0.0437 104 ASP B CB  
2403 C CG  . ASP B 102 ? 0.7753 0.5934 0.5266 -0.1036 0.0535  -0.0416 104 ASP B CG  
2404 O OD1 . ASP B 102 ? 0.7875 0.5702 0.5223 -0.1021 0.0539  -0.0388 104 ASP B OD1 
2405 O OD2 . ASP B 102 ? 0.7681 0.6031 0.5256 -0.1061 0.0567  -0.0425 104 ASP B OD2 
2406 N N   . GLU B 103 ? 0.7403 0.5152 0.4668 -0.1225 0.0658  -0.0566 105 GLU B N   
2407 C CA  . GLU B 103 ? 0.7843 0.5177 0.4907 -0.1221 0.0690  -0.0554 105 GLU B CA  
2408 C C   . GLU B 103 ? 0.7792 0.4951 0.4823 -0.1065 0.0589  -0.0451 105 GLU B C   
2409 O O   . GLU B 103 ? 0.7969 0.4922 0.4925 -0.1020 0.0574  -0.0441 105 GLU B O   
2410 C CB  . GLU B 103 ? 0.8721 0.5792 0.5606 -0.1313 0.0796  -0.0576 105 GLU B CB  
2411 C CG  . GLU B 103 ? 1.0422 0.7041 0.7063 -0.1316 0.0849  -0.0570 105 GLU B CG  
2412 C CD  . GLU B 103 ? 1.2129 0.8677 0.8724 -0.1434 0.0942  -0.0668 105 GLU B CD  
2413 O OE1 . GLU B 103 ? 1.2184 0.9057 0.8947 -0.1510 0.0948  -0.0747 105 GLU B OE1 
2414 O OE2 . GLU B 103 ? 1.3140 0.9293 0.9514 -0.1446 0.1011  -0.0667 105 GLU B OE2 
2415 N N   . LYS B 104 ? 0.7478 0.4727 0.4574 -0.0982 0.0523  -0.0381 106 LYS B N   
2416 C CA  . LYS B 104 ? 0.7269 0.4390 0.4364 -0.0844 0.0422  -0.0297 106 LYS B CA  
2417 C C   . LYS B 104 ? 0.6812 0.4141 0.4097 -0.0759 0.0345  -0.0271 106 LYS B C   
2418 O O   . LYS B 104 ? 0.6810 0.4027 0.4114 -0.0656 0.0268  -0.0217 106 LYS B O   
2419 C CB  . LYS B 104 ? 0.7678 0.4785 0.4752 -0.0802 0.0392  -0.0244 106 LYS B CB  
2420 C CG  . LYS B 104 ? 0.8693 0.5496 0.5530 -0.0849 0.0458  -0.0248 106 LYS B CG  
2421 C CD  . LYS B 104 ? 0.9992 0.6413 0.6628 -0.0780 0.0421  -0.0215 106 LYS B CD  
2422 C CE  . LYS B 104 ? 1.1324 0.7408 0.7690 -0.0788 0.0468  -0.0196 106 LYS B CE  
2423 N NZ  . LYS B 104 ? 1.2317 0.8024 0.8460 -0.0738 0.0460  -0.0181 106 LYS B NZ  
2424 N N   . ASN B 105 ? 0.6468 0.4089 0.3885 -0.0800 0.0367  -0.0310 107 ASN B N   
2425 C CA  . ASN B 105 ? 0.6431 0.4229 0.3999 -0.0724 0.0316  -0.0285 107 ASN B CA  
2426 C C   . ASN B 105 ? 0.6752 0.4544 0.4306 -0.0762 0.0354  -0.0345 107 ASN B C   
2427 O O   . ASN B 105 ? 0.6824 0.4641 0.4459 -0.0687 0.0322  -0.0318 107 ASN B O   
2428 C CB  . ASN B 105 ? 0.6057 0.4193 0.3767 -0.0713 0.0306  -0.0273 107 ASN B CB  
2429 C CG  . ASN B 105 ? 0.6169 0.4330 0.3912 -0.0661 0.0272  -0.0212 107 ASN B CG  
2430 O OD1 . ASN B 105 ? 0.5989 0.3971 0.3711 -0.0592 0.0223  -0.0159 107 ASN B OD1 
2431 N ND2 . ASN B 105 ? 0.6192 0.4577 0.3988 -0.0688 0.0295  -0.0223 107 ASN B ND2 
2432 N N   . LYS B 106 ? 0.7012 0.4772 0.4471 -0.0881 0.0430  -0.0428 108 LYS B N   
2433 C CA  . LYS B 106 ? 0.7151 0.4939 0.4598 -0.0928 0.0471  -0.0498 108 LYS B CA  
2434 C C   . LYS B 106 ? 0.7226 0.4766 0.4624 -0.0858 0.0463  -0.0477 108 LYS B C   
2435 O O   . LYS B 106 ? 0.7197 0.4822 0.4642 -0.0845 0.0474  -0.0504 108 LYS B O   
2436 C CB  . LYS B 106 ? 0.7656 0.5427 0.5010 -0.1082 0.0561  -0.0606 108 LYS B CB  
2437 C CG  . LYS B 106 ? 0.8569 0.5995 0.5745 -0.1141 0.0625  -0.0617 108 LYS B CG  
2438 C CD  . LYS B 106 ? 0.9626 0.7048 0.6731 -0.1314 0.0734  -0.0740 108 LYS B CD  
2439 C CE  . LYS B 106 ? 1.0789 0.7785 0.7677 -0.1369 0.0824  -0.0756 108 LYS B CE  
2440 N NZ  . LYS B 106 ? 1.1422 0.8408 0.8252 -0.1553 0.0946  -0.0869 108 LYS B NZ  
2441 N N   . ARG B 107 ? 0.7227 0.4469 0.4528 -0.0804 0.0444  -0.0430 109 ARG B N   
2442 C CA  . ARG B 107 ? 0.7308 0.4328 0.4581 -0.0714 0.0424  -0.0405 109 ARG B CA  
2443 C C   . ARG B 107 ? 0.7047 0.4159 0.4490 -0.0575 0.0326  -0.0325 109 ARG B C   
2444 O O   . ARG B 107 ? 0.7152 0.4115 0.4612 -0.0487 0.0295  -0.0302 109 ARG B O   
2445 C CB  . ARG B 107 ? 0.7807 0.4443 0.4867 -0.0714 0.0449  -0.0400 109 ARG B CB  
2446 C CG  . ARG B 107 ? 0.8665 0.5125 0.5542 -0.0849 0.0569  -0.0482 109 ARG B CG  
2447 C CD  . ARG B 107 ? 0.9828 0.5916 0.6469 -0.0858 0.0608  -0.0464 109 ARG B CD  
2448 N NE  . ARG B 107 ? 1.0757 0.6584 0.7318 -0.0708 0.0533  -0.0387 109 ARG B NE  
2449 C CZ  . ARG B 107 ? 1.1590 0.7044 0.7906 -0.0683 0.0559  -0.0360 109 ARG B CZ  
2450 N NH1 . ARG B 107 ? 1.1493 0.6752 0.7751 -0.0529 0.0467  -0.0294 109 ARG B NH1 
2451 N NH2 . ARG B 107 ? 1.1711 0.6983 0.7835 -0.0808 0.0679  -0.0403 109 ARG B NH2 
2452 N N   . GLY B 108 ? 0.6572 0.3932 0.4148 -0.0559 0.0286  -0.0289 110 GLY B N   
2453 C CA  . GLY B 108 ? 0.6446 0.3875 0.4174 -0.0451 0.0206  -0.0220 110 GLY B CA  
2454 C C   . GLY B 108 ? 0.6047 0.3731 0.3953 -0.0415 0.0209  -0.0204 110 GLY B C   
2455 O O   . GLY B 108 ? 0.5797 0.3566 0.3704 -0.0445 0.0263  -0.0245 110 GLY B O   
2456 N N   . GLY B 109 ? 0.5818 0.3601 0.3857 -0.0349 0.0157  -0.0146 111 GLY B N   
2457 C CA  . GLY B 109 ? 0.5709 0.3675 0.3918 -0.0294 0.0164  -0.0116 111 GLY B CA  
2458 C C   . GLY B 109 ? 0.5451 0.3502 0.3779 -0.0243 0.0118  -0.0056 111 GLY B C   
2459 O O   . GLY B 109 ? 0.5335 0.3328 0.3602 -0.0257 0.0082  -0.0044 111 GLY B O   
2460 N N   . ARG B 110 ? 0.5299 0.3470 0.3784 -0.0189 0.0132  -0.0022 112 ARG B N   
2461 C CA  . ARG B 110 ? 0.5155 0.3395 0.3757 -0.0146 0.0106  0.0031  112 ARG B CA  
2462 C C   . ARG B 110 ? 0.5312 0.3566 0.4109 -0.0085 0.0108  0.0054  112 ARG B C   
2463 O O   . ARG B 110 ? 0.5343 0.3645 0.4197 -0.0070 0.0164  0.0045  112 ARG B O   
2464 C CB  . ARG B 110 ? 0.4990 0.3418 0.3561 -0.0159 0.0150  0.0057  112 ARG B CB  
2465 C CG  . ARG B 110 ? 0.5730 0.4304 0.4333 -0.0140 0.0219  0.0063  112 ARG B CG  
2466 C CD  . ARG B 110 ? 0.6245 0.5012 0.4792 -0.0136 0.0251  0.0087  112 ARG B CD  
2467 N NE  . ARG B 110 ? 0.6899 0.5768 0.5449 -0.0105 0.0312  0.0094  112 ARG B NE  
2468 C CZ  . ARG B 110 ? 0.6912 0.5949 0.5415 -0.0070 0.0346  0.0124  112 ARG B CZ  
2469 N NH1 . ARG B 110 ? 0.7090 0.6185 0.5567 -0.0038 0.0403  0.0128  112 ARG B NH1 
2470 N NH2 . ARG B 110 ? 0.6578 0.5719 0.5051 -0.0056 0.0325  0.0152  112 ARG B NH2 
2471 N N   . TRP B 111 ? 0.5314 0.3529 0.4220 -0.0053 0.0054  0.0077  113 TRP B N   
2472 C CA  . TRP B 111 ? 0.5304 0.3578 0.4428 -0.0008 0.0072  0.0102  113 TRP B CA  
2473 C C   . TRP B 111 ? 0.5499 0.3905 0.4639 -0.0002 0.0145  0.0153  113 TRP B C   
2474 O O   . TRP B 111 ? 0.5452 0.3868 0.4518 -0.0011 0.0128  0.0177  113 TRP B O   
2475 C CB  . TRP B 111 ? 0.5303 0.3486 0.4529 0.0013  -0.0020 0.0093  113 TRP B CB  
2476 C CG  . TRP B 111 ? 0.5324 0.3391 0.4580 0.0039  -0.0095 0.0050  113 TRP B CG  
2477 C CD1 . TRP B 111 ? 0.5736 0.3651 0.4843 0.0040  -0.0182 0.0027  113 TRP B CD1 
2478 C CD2 . TRP B 111 ? 0.5324 0.3415 0.4757 0.0077  -0.0082 0.0026  113 TRP B CD2 
2479 N NE1 . TRP B 111 ? 0.5819 0.3653 0.4982 0.0086  -0.0230 -0.0006 113 TRP B NE1 
2480 C CE2 . TRP B 111 ? 0.5518 0.3471 0.4902 0.0109  -0.0174 -0.0010 113 TRP B CE2 
2481 C CE3 . TRP B 111 ? 0.5255 0.3460 0.4876 0.0092  0.0005  0.0033  113 TRP B CE3 
2482 C CZ2 . TRP B 111 ? 0.5697 0.3645 0.5233 0.0163  -0.0187 -0.0041 113 TRP B CZ2 
2483 C CZ3 . TRP B 111 ? 0.5473 0.3673 0.5254 0.0134  0.0000  -0.0002 113 TRP B CZ3 
2484 C CH2 . TRP B 111 ? 0.5608 0.3689 0.5354 0.0171  -0.0099 -0.0039 113 TRP B CH2 
2485 N N   . LEU B 112 ? 0.5540 0.4031 0.4768 0.0022  0.0232  0.0175  114 LEU B N   
2486 C CA  . LEU B 112 ? 0.5767 0.4364 0.4968 0.0044  0.0310  0.0230  114 LEU B CA  
2487 C C   . LEU B 112 ? 0.5820 0.4417 0.5216 0.0078  0.0372  0.0267  114 LEU B C   
2488 O O   . LEU B 112 ? 0.5730 0.4313 0.5277 0.0087  0.0409  0.0249  114 LEU B O   
2489 C CB  . LEU B 112 ? 0.5878 0.4563 0.4959 0.0045  0.0375  0.0226  114 LEU B CB  
2490 C CG  . LEU B 112 ? 0.6095 0.4890 0.5113 0.0087  0.0455  0.0285  114 LEU B CG  
2491 C CD1 . LEU B 112 ? 0.6008 0.4873 0.4906 0.0086  0.0419  0.0307  114 LEU B CD1 
2492 C CD2 . LEU B 112 ? 0.6270 0.5133 0.5189 0.0095  0.0520  0.0270  114 LEU B CD2 
2493 N N   . ILE B 113 ? 0.5764 0.4369 0.5156 0.0094  0.0392  0.0316  115 ILE B N   
2494 C CA  . ILE B 113 ? 0.5855 0.4442 0.5391 0.0120  0.0472  0.0360  115 ILE B CA  
2495 C C   . ILE B 113 ? 0.5837 0.4497 0.5230 0.0168  0.0573  0.0430  115 ILE B C   
2496 O O   . ILE B 113 ? 0.5702 0.4410 0.4939 0.0184  0.0549  0.0456  115 ILE B O   
2497 C CB  . ILE B 113 ? 0.6178 0.4694 0.5759 0.0109  0.0419  0.0363  115 ILE B CB  
2498 C CG1 . ILE B 113 ? 0.6481 0.4925 0.6099 0.0072  0.0285  0.0295  115 ILE B CG1 
2499 C CG2 . ILE B 113 ? 0.6256 0.4727 0.6009 0.0119  0.0505  0.0393  115 ILE B CG2 
2500 C CD1 . ILE B 113 ? 0.6440 0.4872 0.6230 0.0064  0.0253  0.0239  115 ILE B CD1 
2501 N N   . THR B 114 ? 0.6089 0.4761 0.5526 0.0196  0.0682  0.0458  116 THR B N   
2502 C CA  . THR B 114 ? 0.6565 0.5279 0.5854 0.0259  0.0783  0.0533  116 THR B CA  
2503 C C   . THR B 114 ? 0.6626 0.5251 0.6019 0.0286  0.0884  0.0594  116 THR B C   
2504 O O   . THR B 114 ? 0.6469 0.5030 0.6070 0.0256  0.0936  0.0571  116 THR B O   
2505 C CB  . THR B 114 ? 0.7249 0.5998 0.6488 0.0276  0.0857  0.0529  116 THR B CB  
2506 O OG1 . THR B 114 ? 0.7879 0.6558 0.7341 0.0255  0.0925  0.0509  116 THR B OG1 
2507 C CG2 . THR B 114 ? 0.7259 0.6074 0.6399 0.0240  0.0773  0.0461  116 THR B CG2 
2508 N N   . LEU B 115 ? 0.6735 0.5354 0.5994 0.0342  0.0918  0.0664  117 LEU B N   
2509 C CA  . LEU B 115 ? 0.7249 0.5753 0.6569 0.0373  0.1031  0.0728  117 LEU B CA  
2510 C C   . LEU B 115 ? 0.7758 0.6256 0.6906 0.0463  0.1164  0.0817  117 LEU B C   
2511 O O   . LEU B 115 ? 0.7925 0.6520 0.6851 0.0530  0.1134  0.0853  117 LEU B O   
2512 C CB  . LEU B 115 ? 0.7318 0.5780 0.6602 0.0384  0.0983  0.0748  117 LEU B CB  
2513 C CG  . LEU B 115 ? 0.7651 0.6086 0.7066 0.0306  0.0856  0.0669  117 LEU B CG  
2514 C CD1 . LEU B 115 ? 0.7765 0.6131 0.7124 0.0328  0.0845  0.0699  117 LEU B CD1 
2515 C CD2 . LEU B 115 ? 0.7788 0.6150 0.7461 0.0239  0.0867  0.0610  117 LEU B CD2 
2516 N N   . ASN B 116 ? 0.7903 0.6285 0.7154 0.0466  0.1313  0.0850  118 ASN B N   
2517 C CA  . ASN B 116 ? 0.8261 0.6582 0.7335 0.0558  0.1464  0.0945  118 ASN B CA  
2518 C C   . ASN B 116 ? 0.8494 0.6738 0.7421 0.0641  0.1504  0.1036  118 ASN B C   
2519 O O   . ASN B 116 ? 0.8269 0.6481 0.7280 0.0610  0.1442  0.1018  118 ASN B O   
2520 C CB  . ASN B 116 ? 0.8563 0.6759 0.7805 0.0526  0.1632  0.0952  118 ASN B CB  
2521 C CG  . ASN B 116 ? 0.8891 0.6937 0.8340 0.0479  0.1717  0.0957  118 ASN B CG  
2522 O OD1 . ASN B 116 ? 0.8995 0.6971 0.8381 0.0507  0.1711  0.0999  118 ASN B OD1 
2523 N ND2 . ASN B 116 ? 0.8974 0.6973 0.8689 0.0403  0.1801  0.0906  118 ASN B ND2 
2524 N N   . LYS B 117 ? 0.8820 0.7021 0.7515 0.0754  0.1613  0.1134  119 LYS B N   
2525 C CA  . LYS B 117 ? 0.9192 0.7320 0.7703 0.0865  0.1659  0.1233  119 LYS B CA  
2526 C C   . LYS B 117 ? 0.9279 0.7222 0.7945 0.0826  0.1728  0.1248  119 LYS B C   
2527 O O   . LYS B 117 ? 0.9308 0.7252 0.7925 0.0860  0.1667  0.1265  119 LYS B O   
2528 C CB  . LYS B 117 ? 0.9745 0.7791 0.8001 0.0993  0.1806  0.1342  119 LYS B CB  
2529 C CG  . LYS B 117 ? 1.0763 0.8669 0.8822 0.1127  0.1900  0.1464  119 LYS B CG  
2530 C CD  . LYS B 117 ? 1.1748 0.9573 0.9512 0.1269  0.2028  0.1572  119 LYS B CD  
2531 C CE  . LYS B 117 ? 1.2476 1.0062 1.0286 0.1240  0.2249  0.1611  119 LYS B CE  
2532 N NZ  . LYS B 117 ? 1.2843 1.0175 1.0774 0.1214  0.2398  0.1656  119 LYS B NZ  
2533 N N   . GLN B 118 ? 0.9251 0.7039 0.8106 0.0755  0.1862  0.1235  120 GLN B N   
2534 C CA  . GLN B 118 ? 0.9336 0.6936 0.8349 0.0705  0.1945  0.1236  120 GLN B CA  
2535 C C   . GLN B 118 ? 0.9105 0.6774 0.8285 0.0618  0.1780  0.1142  120 GLN B C   
2536 O O   . GLN B 118 ? 0.9022 0.6567 0.8234 0.0610  0.1800  0.1151  120 GLN B O   
2537 C CB  . GLN B 118 ? 0.9723 0.7207 0.8983 0.0608  0.2088  0.1197  120 GLN B CB  
2538 C CG  . GLN B 118 ? 1.0408 0.7707 0.9541 0.0675  0.2324  0.1298  120 GLN B CG  
2539 C CD  . GLN B 118 ? 1.1273 0.8448 1.0713 0.0554  0.2473  0.1244  120 GLN B CD  
2540 O OE1 . GLN B 118 ? 1.1430 0.8719 1.1179 0.0432  0.2383  0.1123  120 GLN B OE1 
2541 N NE2 . GLN B 118 ? 1.1411 0.8350 1.0776 0.0589  0.2710  0.1330  120 GLN B NE2 
2542 N N   . GLN B 119 ? 0.8939 0.6786 0.8212 0.0553  0.1623  0.1051  121 GLN B N   
2543 C CA  . GLN B 119 ? 0.8876 0.6779 0.8290 0.0470  0.1464  0.0958  121 GLN B CA  
2544 C C   . GLN B 119 ? 0.8884 0.6848 0.8121 0.0527  0.1357  0.0980  121 GLN B C   
2545 O O   . GLN B 119 ? 0.8903 0.6862 0.8225 0.0468  0.1252  0.0916  121 GLN B O   
2546 C CB  . GLN B 119 ? 0.8945 0.6986 0.8503 0.0393  0.1351  0.0862  121 GLN B CB  
2547 C CG  . GLN B 119 ? 0.9266 0.7255 0.9070 0.0324  0.1445  0.0819  121 GLN B CG  
2548 C CD  . GLN B 119 ? 1.0032 0.8157 0.9958 0.0270  0.1332  0.0731  121 GLN B CD  
2549 O OE1 . GLN B 119 ? 1.0185 0.8396 1.0002 0.0304  0.1337  0.0743  121 GLN B OE1 
2550 N NE2 . GLN B 119 ? 1.0096 0.8233 1.0236 0.0190  0.1224  0.0638  121 GLN B NE2 
2551 N N   . ARG B 120 ? 0.8859 0.6887 0.7853 0.0643  0.1378  0.1063  122 ARG B N   
2552 C CA  . ARG B 120 ? 0.8856 0.6947 0.7701 0.0708  0.1299  0.1089  122 ARG B CA  
2553 C C   . ARG B 120 ? 0.8816 0.6720 0.7687 0.0719  0.1362  0.1118  122 ARG B C   
2554 O O   . ARG B 120 ? 0.8870 0.6794 0.7734 0.0707  0.1273  0.1087  122 ARG B O   
2555 C CB  . ARG B 120 ? 0.9135 0.7333 0.7736 0.0844  0.1325  0.1175  122 ARG B CB  
2556 C CG  . ARG B 120 ? 0.9666 0.7973 0.8130 0.0925  0.1247  0.1201  122 ARG B CG  
2557 C CD  . ARG B 120 ? 1.0308 0.8862 0.8643 0.0970  0.1157  0.1189  122 ARG B CD  
2558 N NE  . ARG B 120 ? 1.1059 0.9744 0.9240 0.1088  0.1117  0.1236  122 ARG B NE  
2559 C CZ  . ARG B 120 ? 1.1493 1.0415 0.9552 0.1146  0.1040  0.1228  122 ARG B CZ  
2560 N NH1 . ARG B 120 ? 1.1593 1.0621 0.9646 0.1091  0.1001  0.1174  122 ARG B NH1 
2561 N NH2 . ARG B 120 ? 1.1218 1.0281 0.9171 0.1258  0.1000  0.1265  122 ARG B NH2 
2562 N N   . ARG B 121 ? 0.8643 0.6350 0.7539 0.0737  0.1528  0.1175  123 ARG B N   
2563 C CA  . ARG B 121 ? 0.8616 0.6111 0.7535 0.0741  0.1614  0.1200  123 ARG B CA  
2564 C C   . ARG B 121 ? 0.8262 0.5698 0.7428 0.0593  0.1549  0.1083  123 ARG B C   
2565 O O   . ARG B 121 ? 0.8440 0.5812 0.7603 0.0579  0.1499  0.1056  123 ARG B O   
2566 C CB  . ARG B 121 ? 0.9030 0.6307 0.7890 0.0799  0.1832  0.1296  123 ARG B CB  
2567 C CG  . ARG B 121 ? 0.9987 0.7252 0.8541 0.0986  0.1908  0.1434  123 ARG B CG  
2568 C CD  . ARG B 121 ? 1.0820 0.7899 0.9234 0.1089  0.1992  0.1516  123 ARG B CD  
2569 N NE  . ARG B 121 ? 1.1311 0.8340 0.9867 0.0997  0.1918  0.1433  123 ARG B NE  
2570 C CZ  . ARG B 121 ? 1.1556 0.8346 1.0237 0.0917  0.2015  0.1403  123 ARG B CZ  
2571 N NH1 . ARG B 121 ? 1.1491 0.8259 1.0271 0.0840  0.1924  0.1320  123 ARG B NH1 
2572 N NH2 . ARG B 121 ? 1.1515 0.8075 1.0214 0.0911  0.2212  0.1452  123 ARG B NH2 
2573 N N   . SER B 122 ? 0.7914 0.5378 0.7289 0.0490  0.1543  0.1010  124 SER B N   
2574 C CA  . SER B 122 ? 0.7847 0.5256 0.7478 0.0357  0.1490  0.0896  124 SER B CA  
2575 C C   . SER B 122 ? 0.7789 0.5345 0.7497 0.0288  0.1278  0.0789  124 SER B C   
2576 O O   . SER B 122 ? 0.7890 0.5373 0.7692 0.0222  0.1210  0.0716  124 SER B O   
2577 C CB  . SER B 122 ? 0.8020 0.5398 0.7874 0.0284  0.1594  0.0862  124 SER B CB  
2578 O OG  . SER B 122 ? 0.8226 0.5770 0.8061 0.0303  0.1556  0.0865  124 SER B OG  
2579 N N   . ASP B 123 ? 0.7355 0.5095 0.7008 0.0304  0.1182  0.0779  125 ASP B N   
2580 C CA  . ASP B 123 ? 0.7096 0.4947 0.6829 0.0236  0.1005  0.0680  125 ASP B CA  
2581 C C   . ASP B 123 ? 0.6453 0.4416 0.5989 0.0277  0.0890  0.0689  125 ASP B C   
2582 O O   . ASP B 123 ? 0.6375 0.4367 0.5942 0.0223  0.0756  0.0613  125 ASP B O   
2583 C CB  . ASP B 123 ? 0.7514 0.5469 0.7382 0.0200  0.0994  0.0640  125 ASP B CB  
2584 C CG  . ASP B 123 ? 0.9020 0.6908 0.9146 0.0138  0.1088  0.0603  125 ASP B CG  
2585 O OD1 . ASP B 123 ? 0.9257 0.7034 0.9516 0.0084  0.1102  0.0561  125 ASP B OD1 
2586 O OD2 . ASP B 123 ? 0.9489 0.7438 0.9692 0.0138  0.1154  0.0608  125 ASP B OD2 
2587 N N   . LEU B 124 ? 0.6190 0.4221 0.5528 0.0369  0.0936  0.0772  126 LEU B N   
2588 C CA  . LEU B 124 ? 0.6237 0.4419 0.5428 0.0390  0.0826  0.0761  126 LEU B CA  
2589 C C   . LEU B 124 ? 0.6001 0.4129 0.5160 0.0364  0.0739  0.0720  126 LEU B C   
2590 O O   . LEU B 124 ? 0.5914 0.4098 0.5060 0.0314  0.0624  0.0657  126 LEU B O   
2591 C CB  . LEU B 124 ? 0.6423 0.4710 0.5425 0.0500  0.0881  0.0848  126 LEU B CB  
2592 C CG  . LEU B 124 ? 0.6720 0.5187 0.5597 0.0511  0.0774  0.0824  126 LEU B CG  
2593 C CD1 . LEU B 124 ? 0.6691 0.5257 0.5606 0.0444  0.0700  0.0756  126 LEU B CD1 
2594 C CD2 . LEU B 124 ? 0.7022 0.5611 0.5733 0.0629  0.0819  0.0902  126 LEU B CD2 
2595 N N   . ASN B 125 ? 0.5745 0.3738 0.4879 0.0399  0.0809  0.0759  127 ASN B N   
2596 C CA  . ASN B 125 ? 0.6003 0.3934 0.5079 0.0383  0.0742  0.0725  127 ASN B CA  
2597 C C   . ASN B 125 ? 0.5753 0.3607 0.4953 0.0276  0.0634  0.0619  127 ASN B C   
2598 O O   . ASN B 125 ? 0.5588 0.3471 0.4718 0.0248  0.0527  0.0571  127 ASN B O   
2599 C CB  . ASN B 125 ? 0.6571 0.4355 0.5591 0.0444  0.0846  0.0784  127 ASN B CB  
2600 C CG  . ASN B 125 ? 0.7411 0.5286 0.6277 0.0571  0.0922  0.0887  127 ASN B CG  
2601 O OD1 . ASN B 125 ? 0.7596 0.5661 0.6372 0.0608  0.0863  0.0894  127 ASN B OD1 
2602 N ND2 . ASN B 125 ? 0.7516 0.5260 0.6347 0.0644  0.1055  0.0964  127 ASN B ND2 
2603 N N   . ARG B 126 ? 0.5635 0.3403 0.5020 0.0222  0.0664  0.0582  128 ARG B N   
2604 C CA  . ARG B 126 ? 0.5743 0.3450 0.5256 0.0134  0.0551  0.0477  128 ARG B CA  
2605 C C   . ARG B 126 ? 0.5360 0.3189 0.4879 0.0106  0.0431  0.0428  128 ARG B C   
2606 O O   . ARG B 126 ? 0.5390 0.3186 0.4867 0.0072  0.0310  0.0366  128 ARG B O   
2607 C CB  . ARG B 126 ? 0.6211 0.3837 0.5963 0.0077  0.0613  0.0437  128 ARG B CB  
2608 C CG  . ARG B 126 ? 0.7390 0.5012 0.7302 -0.0004 0.0472  0.0318  128 ARG B CG  
2609 C CD  . ARG B 126 ? 0.8703 0.6231 0.8843 -0.0075 0.0500  0.0246  128 ARG B CD  
2610 N NE  . ARG B 126 ? 0.9891 0.7425 1.0147 -0.0136 0.0335  0.0126  128 ARG B NE  
2611 C CZ  . ARG B 126 ? 1.0725 0.8379 1.1137 -0.0157 0.0239  0.0067  128 ARG B CZ  
2612 N NH1 . ARG B 126 ? 1.0859 0.8510 1.1351 -0.0194 0.0080  -0.0039 128 ARG B NH1 
2613 N NH2 . ARG B 126 ? 1.0832 0.8604 1.1306 -0.0132 0.0301  0.0112  128 ARG B NH2 
2614 N N   . PHE B 127 ? 0.5142 0.3088 0.4699 0.0123  0.0471  0.0458  129 PHE B N   
2615 C CA  . PHE B 127 ? 0.5155 0.3200 0.4708 0.0102  0.0379  0.0417  129 PHE B CA  
2616 C C   . PHE B 127 ? 0.5030 0.3121 0.4376 0.0116  0.0309  0.0420  129 PHE B C   
2617 O O   . PHE B 127 ? 0.5103 0.3190 0.4428 0.0081  0.0206  0.0363  129 PHE B O   
2618 C CB  . PHE B 127 ? 0.5500 0.3652 0.5100 0.0126  0.0460  0.0454  129 PHE B CB  
2619 C CG  . PHE B 127 ? 0.6123 0.4260 0.5958 0.0094  0.0510  0.0426  129 PHE B CG  
2620 C CD1 . PHE B 127 ? 0.6414 0.4457 0.6429 0.0048  0.0506  0.0377  129 PHE B CD1 
2621 C CD2 . PHE B 127 ? 0.6440 0.4662 0.6324 0.0107  0.0569  0.0441  129 PHE B CD2 
2622 C CE1 . PHE B 127 ? 0.6573 0.4628 0.6839 0.0012  0.0560  0.0340  129 PHE B CE1 
2623 C CE2 . PHE B 127 ? 0.6611 0.4828 0.6727 0.0078  0.0632  0.0413  129 PHE B CE2 
2624 C CZ  . PHE B 127 ? 0.6611 0.4753 0.6930 0.0029  0.0628  0.0362  129 PHE B CZ  
2625 N N   . TRP B 128 ? 0.4889 0.3028 0.4086 0.0168  0.0366  0.0483  130 TRP B N   
2626 C CA  . TRP B 128 ? 0.5008 0.3204 0.4037 0.0169  0.0309  0.0474  130 TRP B CA  
2627 C C   . TRP B 128 ? 0.4928 0.2985 0.3907 0.0134  0.0231  0.0424  130 TRP B C   
2628 O O   . TRP B 128 ? 0.4849 0.2892 0.3749 0.0099  0.0151  0.0379  130 TRP B O   
2629 C CB  . TRP B 128 ? 0.5304 0.3608 0.4220 0.0240  0.0384  0.0545  130 TRP B CB  
2630 C CG  . TRP B 128 ? 0.5459 0.3852 0.4238 0.0238  0.0343  0.0531  130 TRP B CG  
2631 C CD1 . TRP B 128 ? 0.5653 0.4059 0.4343 0.0281  0.0370  0.0559  130 TRP B CD1 
2632 C CD2 . TRP B 128 ? 0.5379 0.3857 0.4101 0.0188  0.0282  0.0482  130 TRP B CD2 
2633 N NE1 . TRP B 128 ? 0.5704 0.4216 0.4305 0.0256  0.0332  0.0528  130 TRP B NE1 
2634 C CE2 . TRP B 128 ? 0.5651 0.4202 0.4263 0.0195  0.0281  0.0480  130 TRP B CE2 
2635 C CE3 . TRP B 128 ? 0.5375 0.3869 0.4130 0.0138  0.0238  0.0437  130 TRP B CE3 
2636 C CZ2 . TRP B 128 ? 0.5564 0.4200 0.4104 0.0142  0.0243  0.0431  130 TRP B CZ2 
2637 C CZ3 . TRP B 128 ? 0.5464 0.4020 0.4126 0.0092  0.0199  0.0393  130 TRP B CZ3 
2638 C CH2 . TRP B 128 ? 0.5547 0.4170 0.4106 0.0088  0.0204  0.0389  130 TRP B CH2 
2639 N N   . LEU B 129 ? 0.5006 0.2940 0.4019 0.0142  0.0261  0.0429  131 LEU B N   
2640 C CA  . LEU B 129 ? 0.5325 0.3111 0.4277 0.0110  0.0186  0.0375  131 LEU B CA  
2641 C C   . LEU B 129 ? 0.5274 0.3000 0.4292 0.0056  0.0067  0.0295  131 LEU B C   
2642 O O   . LEU B 129 ? 0.5258 0.2912 0.4145 0.0037  -0.0019 0.0254  131 LEU B O   
2643 C CB  . LEU B 129 ? 0.5559 0.3214 0.4541 0.0124  0.0247  0.0387  131 LEU B CB  
2644 C CG  . LEU B 129 ? 0.5901 0.3386 0.4794 0.0094  0.0173  0.0325  131 LEU B CG  
2645 C CD1 . LEU B 129 ? 0.6189 0.3680 0.4876 0.0109  0.0149  0.0331  131 LEU B CD1 
2646 C CD2 . LEU B 129 ? 0.6061 0.3413 0.4979 0.0105  0.0248  0.0334  131 LEU B CD2 
2647 N N   . GLU B 130 ? 0.5319 0.3073 0.4530 0.0037  0.0063  0.0272  132 GLU B N   
2648 C CA  . GLU B 130 ? 0.5399 0.3118 0.4698 0.0002  -0.0057 0.0194  132 GLU B CA  
2649 C C   . GLU B 130 ? 0.5369 0.3132 0.4543 0.0004  -0.0120 0.0188  132 GLU B C   
2650 O O   . GLU B 130 ? 0.5603 0.3278 0.4702 -0.0007 -0.0230 0.0136  132 GLU B O   
2651 C CB  . GLU B 130 ? 0.5724 0.3504 0.5290 -0.0015 -0.0030 0.0172  132 GLU B CB  
2652 C CG  . GLU B 130 ? 0.6730 0.4440 0.6449 -0.0039 0.0025  0.0154  132 GLU B CG  
2653 C CD  . GLU B 130 ? 0.7958 0.5525 0.7627 -0.0065 -0.0061 0.0089  132 GLU B CD  
2654 O OE1 . GLU B 130 ? 0.7282 0.4812 0.6900 -0.0075 -0.0203 0.0025  132 GLU B OE1 
2655 O OE2 . GLU B 130 ? 0.8713 0.6190 0.8373 -0.0071 0.0017  0.0104  132 GLU B OE2 
2656 N N   . THR B 131 ? 0.5132 0.3018 0.4267 0.0020  -0.0046 0.0238  133 THR B N   
2657 C CA  . THR B 131 ? 0.5082 0.2999 0.4085 0.0011  -0.0084 0.0228  133 THR B CA  
2658 C C   . THR B 131 ? 0.5147 0.2971 0.3935 0.0001  -0.0122 0.0218  133 THR B C   
2659 O O   . THR B 131 ? 0.5291 0.3024 0.3973 -0.0017 -0.0199 0.0179  133 THR B O   
2660 C CB  . THR B 131 ? 0.5413 0.3493 0.4411 0.0027  0.0010  0.0278  133 THR B CB  
2661 O OG1 . THR B 131 ? 0.5335 0.3477 0.4513 0.0040  0.0061  0.0291  133 THR B OG1 
2662 C CG2 . THR B 131 ? 0.5489 0.3609 0.4368 0.0005  -0.0015 0.0257  133 THR B CG2 
2663 N N   . LEU B 132 ? 0.5098 0.2929 0.3808 0.0016  -0.0060 0.0255  134 LEU B N   
2664 C CA  . LEU B 132 ? 0.5402 0.3150 0.3918 0.0006  -0.0073 0.0246  134 LEU B CA  
2665 C C   . LEU B 132 ? 0.5659 0.3205 0.4100 -0.0008 -0.0173 0.0193  134 LEU B C   
2666 O O   . LEU B 132 ? 0.5641 0.3084 0.3904 -0.0025 -0.0215 0.0169  134 LEU B O   
2667 C CB  . LEU B 132 ? 0.5538 0.3332 0.4022 0.0040  0.0014  0.0294  134 LEU B CB  
2668 C CG  . LEU B 132 ? 0.5502 0.3502 0.4021 0.0073  0.0102  0.0349  134 LEU B CG  
2669 C CD1 . LEU B 132 ? 0.5353 0.3378 0.3853 0.0129  0.0181  0.0400  134 LEU B CD1 
2670 C CD2 . LEU B 132 ? 0.5750 0.3854 0.4178 0.0043  0.0099  0.0332  134 LEU B CD2 
2671 N N   . LEU B 133 ? 0.5690 0.3175 0.4259 -0.0002 -0.0209 0.0169  135 LEU B N   
2672 C CA  . LEU B 133 ? 0.5921 0.3228 0.4427 -0.0011 -0.0323 0.0106  135 LEU B CA  
2673 C C   . LEU B 133 ? 0.6043 0.3311 0.4532 -0.0012 -0.0431 0.0064  135 LEU B C   
2674 O O   . LEU B 133 ? 0.6284 0.3392 0.4595 -0.0007 -0.0519 0.0029  135 LEU B O   
2675 C CB  . LEU B 133 ? 0.5877 0.3150 0.4552 -0.0016 -0.0335 0.0076  135 LEU B CB  
2676 C CG  . LEU B 133 ? 0.6055 0.3317 0.4724 -0.0006 -0.0224 0.0117  135 LEU B CG  
2677 C CD1 . LEU B 133 ? 0.6072 0.3278 0.4910 -0.0024 -0.0229 0.0077  135 LEU B CD1 
2678 C CD2 . LEU B 133 ? 0.6197 0.3344 0.4627 0.0004  -0.0210 0.0124  135 LEU B CD2 
2679 N N   . CYS B 134 ? 0.5879 0.3274 0.4525 -0.0010 -0.0421 0.0071  136 CYS B N   
2680 C CA  . CYS B 134 ? 0.5984 0.3342 0.4596 0.0000  -0.0504 0.0042  136 CYS B CA  
2681 C C   . CYS B 134 ? 0.6281 0.3545 0.4634 -0.0008 -0.0495 0.0055  136 CYS B C   
2682 O O   . CYS B 134 ? 0.6670 0.3784 0.4882 0.0010  -0.0586 0.0025  136 CYS B O   
2683 C CB  . CYS B 134 ? 0.6064 0.3580 0.4885 0.0004  -0.0465 0.0052  136 CYS B CB  
2684 S SG  . CYS B 134 ? 0.6916 0.4522 0.6074 0.0008  -0.0487 0.0016  136 CYS B SG  
2685 N N   . LEU B 135 ? 0.5925 0.3277 0.4214 -0.0031 -0.0386 0.0098  137 LEU B N   
2686 C CA  . LEU B 135 ? 0.5849 0.3136 0.3918 -0.0057 -0.0351 0.0104  137 LEU B CA  
2687 C C   . LEU B 135 ? 0.5988 0.3072 0.3832 -0.0056 -0.0384 0.0089  137 LEU B C   
2688 O O   . LEU B 135 ? 0.6043 0.2953 0.3709 -0.0052 -0.0438 0.0069  137 LEU B O   
2689 C CB  . LEU B 135 ? 0.5740 0.3211 0.3831 -0.0083 -0.0232 0.0140  137 LEU B CB  
2690 C CG  . LEU B 135 ? 0.5867 0.3483 0.4036 -0.0101 -0.0191 0.0143  137 LEU B CG  
2691 C CD1 . LEU B 135 ? 0.5790 0.3453 0.4155 -0.0071 -0.0231 0.0137  137 LEU B CD1 
2692 C CD2 . LEU B 135 ? 0.5920 0.3730 0.4115 -0.0113 -0.0096 0.0172  137 LEU B CD2 
2693 N N   . ILE B 136 ? 0.5926 0.3021 0.3770 -0.0053 -0.0345 0.0103  138 ILE B N   
2694 C CA  . ILE B 136 ? 0.6247 0.3157 0.3857 -0.0055 -0.0345 0.0093  138 ILE B CA  
2695 C C   . ILE B 136 ? 0.6686 0.3381 0.4190 -0.0027 -0.0478 0.0048  138 ILE B C   
2696 O O   . ILE B 136 ? 0.6949 0.3445 0.4196 -0.0024 -0.0495 0.0036  138 ILE B O   
2697 C CB  . ILE B 136 ? 0.6276 0.3244 0.3899 -0.0052 -0.0259 0.0119  138 ILE B CB  
2698 C CG1 . ILE B 136 ? 0.6271 0.3240 0.4049 -0.0027 -0.0295 0.0109  138 ILE B CG1 
2699 C CG2 . ILE B 136 ? 0.6330 0.3533 0.4051 -0.0065 -0.0144 0.0161  138 ILE B CG2 
2700 C CD1 . ILE B 136 ? 0.6330 0.3304 0.4097 -0.0013 -0.0212 0.0133  138 ILE B CD1 
2701 N N   . GLY B 137 ? 0.6719 0.3462 0.4416 -0.0005 -0.0562 0.0021  139 GLY B N   
2702 C CA  . GLY B 137 ? 0.7077 0.3668 0.4723 0.0027  -0.0707 -0.0035 139 GLY B CA  
2703 C C   . GLY B 137 ? 0.7332 0.3837 0.4896 0.0061  -0.0804 -0.0053 139 GLY B C   
2704 O O   . GLY B 137 ? 0.7408 0.3790 0.4909 0.0103  -0.0938 -0.0100 139 GLY B O   
2705 N N   . GLU B 138 ? 0.7432 0.3995 0.4987 0.0048  -0.0738 -0.0020 140 GLU B N   
2706 C CA  . GLU B 138 ? 0.7514 0.3984 0.4989 0.0083  -0.0805 -0.0030 140 GLU B CA  
2707 C C   . GLU B 138 ? 0.7445 0.3985 0.5140 0.0135  -0.0934 -0.0072 140 GLU B C   
2708 O O   . GLU B 138 ? 0.7520 0.3914 0.5098 0.0195  -0.1061 -0.0103 140 GLU B O   
2709 C CB  . GLU B 138 ? 0.7981 0.4164 0.5086 0.0107  -0.0838 -0.0031 140 GLU B CB  
2710 C CG  . GLU B 138 ? 0.8156 0.4270 0.5055 0.0049  -0.0698 0.0003  140 GLU B CG  
2711 C CD  . GLU B 138 ? 0.8892 0.5076 0.5793 0.0000  -0.0584 0.0029  140 GLU B CD  
2712 O OE1 . GLU B 138 ? 0.9183 0.5281 0.6031 0.0026  -0.0619 0.0025  140 GLU B OE1 
2713 O OE2 . GLU B 138 ? 0.8872 0.5192 0.5819 -0.0061 -0.0461 0.0048  140 GLU B OE2 
2714 N N   . SER B 139 ? 0.7353 0.4122 0.5369 0.0114  -0.0896 -0.0073 141 SER B N   
2715 C CA  . SER B 139 ? 0.7237 0.4122 0.5537 0.0144  -0.0990 -0.0121 141 SER B CA  
2716 C C   . SER B 139 ? 0.7202 0.4122 0.5595 0.0193  -0.1046 -0.0134 141 SER B C   
2717 O O   . SER B 139 ? 0.7168 0.4194 0.5808 0.0223  -0.1127 -0.0180 141 SER B O   
2718 C CB  . SER B 139 ? 0.7199 0.4292 0.5785 0.0098  -0.0891 -0.0108 141 SER B CB  
2719 O OG  . SER B 139 ? 0.7577 0.4634 0.6100 0.0065  -0.0844 -0.0099 141 SER B OG  
2720 N N   . PHE B 140 ? 0.7139 0.3975 0.5354 0.0199  -0.0994 -0.0098 142 PHE B N   
2721 C CA  . PHE B 140 ? 0.7181 0.4031 0.5464 0.0248  -0.1022 -0.0104 142 PHE B CA  
2722 C C   . PHE B 140 ? 0.7615 0.4219 0.5625 0.0326  -0.1132 -0.0114 142 PHE B C   
2723 O O   . PHE B 140 ? 0.7804 0.4351 0.5768 0.0365  -0.1124 -0.0104 142 PHE B O   
2724 C CB  . PHE B 140 ? 0.6869 0.3792 0.5146 0.0195  -0.0870 -0.0062 142 PHE B CB  
2725 C CG  . PHE B 140 ? 0.6735 0.3877 0.5228 0.0135  -0.0763 -0.0043 142 PHE B CG  
2726 C CD1 . PHE B 140 ? 0.6588 0.3906 0.5396 0.0145  -0.0769 -0.0062 142 PHE B CD1 
2727 C CD2 . PHE B 140 ? 0.6754 0.3919 0.5130 0.0075  -0.0655 -0.0006 142 PHE B CD2 
2728 C CE1 . PHE B 140 ? 0.6437 0.3920 0.5407 0.0099  -0.0661 -0.0036 142 PHE B CE1 
2729 C CE2 . PHE B 140 ? 0.6544 0.3896 0.5093 0.0041  -0.0563 0.0018  142 PHE B CE2 
2730 C CZ  . PHE B 140 ? 0.6241 0.3735 0.5067 0.0054  -0.0561 0.0008  142 PHE B CZ  
2731 N N   . ASP B 141 ? 0.7921 0.4365 0.5731 0.0352  -0.1224 -0.0131 143 ASP B N   
2732 C CA  . ASP B 141 ? 0.8474 0.4658 0.5984 0.0441  -0.1339 -0.0138 143 ASP B CA  
2733 C C   . ASP B 141 ? 0.8643 0.4623 0.5849 0.0426  -0.1224 -0.0084 143 ASP B C   
2734 O O   . ASP B 141 ? 0.8661 0.4650 0.5789 0.0334  -0.1084 -0.0054 143 ASP B O   
2735 C CB  . ASP B 141 ? 0.9145 0.5405 0.6853 0.0545  -0.1502 -0.0188 143 ASP B CB  
2736 C CG  . ASP B 141 ? 1.0780 0.7176 0.8702 0.0551  -0.1629 -0.0256 143 ASP B CG  
2737 O OD1 . ASP B 141 ? 1.1204 0.7458 0.8911 0.0548  -0.1686 -0.0272 143 ASP B OD1 
2738 O OD2 . ASP B 141 ? 1.1183 0.7820 0.9485 0.0553  -0.1664 -0.0300 143 ASP B OD2 
2739 N N   . ASP B 142 ? 0.8756 0.4561 0.5803 0.0509  -0.1270 -0.0074 144 ASP B N   
2740 C CA  . ASP B 142 ? 0.9022 0.4610 0.5780 0.0481  -0.1145 -0.0030 144 ASP B CA  
2741 C C   . ASP B 142 ? 0.8673 0.4448 0.5619 0.0384  -0.0987 -0.0018 144 ASP B C   
2742 O O   . ASP B 142 ? 0.8981 0.4645 0.5736 0.0312  -0.0856 0.0006  144 ASP B O   
2743 C CB  . ASP B 142 ? 0.9744 0.5099 0.6310 0.0601  -0.1219 -0.0021 144 ASP B CB  
2744 C CG  . ASP B 142 ? 1.1423 0.6516 0.7685 0.0712  -0.1365 -0.0023 144 ASP B CG  
2745 O OD1 . ASP B 142 ? 1.1674 0.6763 0.7871 0.0689  -0.1411 -0.0039 144 ASP B OD1 
2746 O OD2 . ASP B 142 ? 1.2361 0.7237 0.8428 0.0831  -0.1432 -0.0008 144 ASP B OD2 
2747 N N   . TYR B 143 ? 0.8152 0.4205 0.5462 0.0380  -0.0996 -0.0038 145 TYR B N   
2748 C CA  . TYR B 143 ? 0.7938 0.4173 0.5416 0.0299  -0.0857 -0.0029 145 TYR B CA  
2749 C C   . TYR B 143 ? 0.7592 0.3963 0.5098 0.0191  -0.0749 -0.0014 145 TYR B C   
2750 O O   . TYR B 143 ? 0.7488 0.3993 0.5074 0.0123  -0.0633 -0.0007 145 TYR B O   
2751 C CB  . TYR B 143 ? 0.7948 0.4409 0.5779 0.0339  -0.0893 -0.0052 145 TYR B CB  
2752 C CG  . TYR B 143 ? 0.8487 0.4833 0.6305 0.0453  -0.0986 -0.0066 145 TYR B CG  
2753 C CD1 . TYR B 143 ? 0.8917 0.5014 0.6461 0.0482  -0.0946 -0.0047 145 TYR B CD1 
2754 C CD2 . TYR B 143 ? 0.8640 0.5121 0.6722 0.0537  -0.1113 -0.0103 145 TYR B CD2 
2755 C CE1 . TYR B 143 ? 0.9241 0.5220 0.6763 0.0602  -0.1026 -0.0054 145 TYR B CE1 
2756 C CE2 . TYR B 143 ? 0.8910 0.5308 0.6998 0.0657  -0.1204 -0.0117 145 TYR B CE2 
2757 C CZ  . TYR B 143 ? 0.9429 0.5566 0.7224 0.0697  -0.1162 -0.0088 145 TYR B CZ  
2758 O OH  . TYR B 143 ? 1.0118 0.6142 0.7886 0.0833  -0.1247 -0.0094 145 TYR B OH  
2759 N N   . SER B 144 ? 0.7517 0.3849 0.4942 0.0181  -0.0787 -0.0013 146 SER B N   
2760 C CA  . SER B 144 ? 0.7517 0.3942 0.4925 0.0096  -0.0683 0.0004  146 SER B CA  
2761 C C   . SER B 144 ? 0.7639 0.3956 0.4822 0.0028  -0.0561 0.0020  146 SER B C   
2762 O O   . SER B 144 ? 0.7499 0.3973 0.4744 -0.0047 -0.0456 0.0028  146 SER B O   
2763 C CB  . SER B 144 ? 0.7909 0.4260 0.5232 0.0109  -0.0747 -0.0002 146 SER B CB  
2764 O OG  . SER B 144 ? 0.8008 0.4530 0.5604 0.0133  -0.0818 -0.0023 146 SER B OG  
2765 N N   . ASP B 145 ? 0.7803 0.3855 0.4729 0.0054  -0.0569 0.0021  147 ASP B N   
2766 C CA  . ASP B 145 ? 0.7989 0.3930 0.4719 -0.0024 -0.0435 0.0025  147 ASP B CA  
2767 C C   . ASP B 145 ? 0.7794 0.3924 0.4695 -0.0084 -0.0345 0.0012  147 ASP B C   
2768 O O   . ASP B 145 ? 0.8071 0.4215 0.4892 -0.0176 -0.0225 0.0002  147 ASP B O   
2769 C CB  . ASP B 145 ? 0.8358 0.3939 0.4763 0.0024  -0.0451 0.0033  147 ASP B CB  
2770 C CG  . ASP B 145 ? 0.9742 0.5089 0.5888 0.0069  -0.0511 0.0047  147 ASP B CG  
2771 O OD1 . ASP B 145 ? 0.9709 0.5157 0.5891 0.0031  -0.0496 0.0047  147 ASP B OD1 
2772 O OD2 . ASP B 145 ? 1.0338 0.5391 0.6229 0.0151  -0.0571 0.0058  147 ASP B OD2 
2773 N N   . ASP B 146 ? 0.7464 0.3740 0.4595 -0.0036 -0.0397 0.0005  148 ASP B N   
2774 C CA  . ASP B 146 ? 0.7169 0.3620 0.4448 -0.0087 -0.0311 -0.0011 148 ASP B CA  
2775 C C   . ASP B 146 ? 0.6655 0.3408 0.4132 -0.0146 -0.0254 -0.0007 148 ASP B C   
2776 O O   . ASP B 146 ? 0.6540 0.3436 0.4089 -0.0200 -0.0175 -0.0022 148 ASP B O   
2777 C CB  . ASP B 146 ? 0.7179 0.3667 0.4625 -0.0012 -0.0365 -0.0020 148 ASP B CB  
2778 C CG  . ASP B 146 ? 0.8480 0.4700 0.5726 0.0023  -0.0357 -0.0028 148 ASP B CG  
2779 O OD1 . ASP B 146 ? 0.8738 0.4704 0.5753 0.0066  -0.0404 -0.0016 148 ASP B OD1 
2780 O OD2 . ASP B 146 ? 0.8755 0.5009 0.6062 0.0009  -0.0295 -0.0047 148 ASP B OD2 
2781 N N   . VAL B 147 ? 0.6520 0.3356 0.4065 -0.0131 -0.0294 0.0012  149 VAL B N   
2782 C CA  . VAL B 147 ? 0.6101 0.3196 0.3815 -0.0165 -0.0242 0.0025  149 VAL B CA  
2783 C C   . VAL B 147 ? 0.6165 0.3291 0.3748 -0.0246 -0.0147 0.0020  149 VAL B C   
2784 O O   . VAL B 147 ? 0.6413 0.3363 0.3799 -0.0266 -0.0138 0.0018  149 VAL B O   
2785 C CB  . VAL B 147 ? 0.6296 0.3444 0.4128 -0.0118 -0.0309 0.0045  149 VAL B CB  
2786 C CG1 . VAL B 147 ? 0.6279 0.3658 0.4244 -0.0143 -0.0241 0.0068  149 VAL B CG1 
2787 C CG2 . VAL B 147 ? 0.6529 0.3697 0.4547 -0.0051 -0.0395 0.0036  149 VAL B CG2 
2788 N N   . CYS B 148 ? 0.5733 0.3085 0.3424 -0.0291 -0.0074 0.0013  150 CYS B N   
2789 C CA  . CYS B 148 ? 0.5668 0.3136 0.3304 -0.0366 0.0012  -0.0002 150 CYS B CA  
2790 C C   . CYS B 148 ? 0.5363 0.3027 0.3115 -0.0341 0.0019  0.0032  150 CYS B C   
2791 O O   . CYS B 148 ? 0.5391 0.3061 0.3069 -0.0368 0.0057  0.0032  150 CYS B O   
2792 C CB  . CYS B 148 ? 0.5731 0.3343 0.3408 -0.0425 0.0075  -0.0040 150 CYS B CB  
2793 S SG  . CYS B 148 ? 0.6450 0.3796 0.3960 -0.0462 0.0094  -0.0083 150 CYS B SG  
2794 N N   . GLY B 149 ? 0.5153 0.2960 0.3081 -0.0286 -0.0007 0.0060  151 GLY B N   
2795 C CA  . GLY B 149 ? 0.4963 0.2939 0.2995 -0.0252 0.0011  0.0098  151 GLY B CA  
2796 C C   . GLY B 149 ? 0.4804 0.2911 0.3012 -0.0200 0.0005  0.0127  151 GLY B C   
2797 O O   . GLY B 149 ? 0.4878 0.2931 0.3146 -0.0185 -0.0025 0.0117  151 GLY B O   
2798 N N   . ALA B 150 ? 0.4725 0.2985 0.3012 -0.0164 0.0039  0.0167  152 ALA B N   
2799 C CA  . ALA B 150 ? 0.4746 0.3122 0.3181 -0.0111 0.0058  0.0205  152 ALA B CA  
2800 C C   . ALA B 150 ? 0.4692 0.3284 0.3138 -0.0088 0.0118  0.0234  152 ALA B C   
2801 O O   . ALA B 150 ? 0.4806 0.3465 0.3188 -0.0098 0.0138  0.0233  152 ALA B O   
2802 C CB  . ALA B 150 ? 0.4747 0.3019 0.3271 -0.0066 0.0028  0.0234  152 ALA B CB  
2803 N N   . VAL B 151 ? 0.4622 0.3330 0.3149 -0.0050 0.0150  0.0260  153 VAL B N   
2804 C CA  . VAL B 151 ? 0.4729 0.3653 0.3248 -0.0010 0.0199  0.0290  153 VAL B CA  
2805 C C   . VAL B 151 ? 0.4824 0.3764 0.3430 0.0068  0.0241  0.0356  153 VAL B C   
2806 O O   . VAL B 151 ? 0.4724 0.3584 0.3406 0.0068  0.0246  0.0356  153 VAL B O   
2807 C CB  . VAL B 151 ? 0.4731 0.3788 0.3203 -0.0053 0.0207  0.0240  153 VAL B CB  
2808 C CG1 . VAL B 151 ? 0.4938 0.4232 0.3396 0.0003  0.0240  0.0268  153 VAL B CG1 
2809 C CG2 . VAL B 151 ? 0.4766 0.3782 0.3151 -0.0146 0.0185  0.0167  153 VAL B CG2 
2810 N N   . VAL B 152 ? 0.4888 0.3921 0.3482 0.0137  0.0279  0.0412  154 VAL B N   
2811 C CA  . VAL B 152 ? 0.4828 0.3885 0.3464 0.0220  0.0342  0.0483  154 VAL B CA  
2812 C C   . VAL B 152 ? 0.4893 0.4167 0.3449 0.0277  0.0368  0.0506  154 VAL B C   
2813 O O   . VAL B 152 ? 0.4959 0.4368 0.3463 0.0295  0.0353  0.0501  154 VAL B O   
2814 C CB  . VAL B 152 ? 0.5115 0.4047 0.3795 0.0270  0.0376  0.0540  154 VAL B CB  
2815 C CG1 . VAL B 152 ? 0.5257 0.4237 0.3869 0.0294  0.0368  0.0550  154 VAL B CG1 
2816 C CG2 . VAL B 152 ? 0.5328 0.4256 0.4034 0.0352  0.0461  0.0616  154 VAL B CG2 
2817 N N   . ASN B 153 ? 0.5087 0.4400 0.3633 0.0307  0.0405  0.0524  155 ASN B N   
2818 C CA  . ASN B 153 ? 0.5443 0.4946 0.3894 0.0378  0.0426  0.0550  155 ASN B CA  
2819 C C   . ASN B 153 ? 0.5828 0.5274 0.4263 0.0491  0.0508  0.0651  155 ASN B C   
2820 O O   . ASN B 153 ? 0.5893 0.5203 0.4376 0.0494  0.0567  0.0678  155 ASN B O   
2821 C CB  . ASN B 153 ? 0.5676 0.5236 0.4088 0.0338  0.0421  0.0499  155 ASN B CB  
2822 C CG  . ASN B 153 ? 0.6133 0.5683 0.4560 0.0219  0.0363  0.0399  155 ASN B CG  
2823 O OD1 . ASN B 153 ? 0.6374 0.5786 0.4851 0.0165  0.0363  0.0368  155 ASN B OD1 
2824 N ND2 . ASN B 153 ? 0.6007 0.5700 0.4388 0.0182  0.0320  0.0348  155 ASN B ND2 
2825 N N   . VAL B 154 ? 0.6096 0.5634 0.4468 0.0584  0.0520  0.0706  156 VAL B N   
2826 C CA  . VAL B 154 ? 0.6644 0.6101 0.4968 0.0705  0.0610  0.0812  156 VAL B CA  
2827 C C   . VAL B 154 ? 0.6951 0.6559 0.5135 0.0792  0.0626  0.0842  156 VAL B C   
2828 O O   . VAL B 154 ? 0.7029 0.6863 0.5140 0.0827  0.0564  0.0816  156 VAL B O   
2829 C CB  . VAL B 154 ? 0.6900 0.6338 0.5217 0.0775  0.0623  0.0864  156 VAL B CB  
2830 C CG1 . VAL B 154 ? 0.7191 0.6490 0.5450 0.0897  0.0733  0.0977  156 VAL B CG1 
2831 C CG2 . VAL B 154 ? 0.6927 0.6224 0.5356 0.0678  0.0592  0.0816  156 VAL B CG2 
2832 N N   . ARG B 155 ? 0.7287 0.6778 0.5434 0.0825  0.0710  0.0889  157 ARG B N   
2833 C CA  . ARG B 155 ? 0.7579 0.7183 0.5562 0.0906  0.0728  0.0913  157 ARG B CA  
2834 C C   . ARG B 155 ? 0.8151 0.7582 0.6046 0.1015  0.0861  0.1026  157 ARG B C   
2835 O O   . ARG B 155 ? 0.8300 0.7513 0.6304 0.0980  0.0947  0.1055  157 ARG B O   
2836 C CB  . ARG B 155 ? 0.7607 0.7245 0.5601 0.0808  0.0702  0.0826  157 ARG B CB  
2837 C CG  . ARG B 155 ? 0.7635 0.7427 0.5676 0.0698  0.0590  0.0710  157 ARG B CG  
2838 C CD  . ARG B 155 ? 0.7722 0.7785 0.5660 0.0746  0.0512  0.0681  157 ARG B CD  
2839 N NE  . ARG B 155 ? 0.8205 0.8382 0.6207 0.0614  0.0427  0.0560  157 ARG B NE  
2840 C CZ  . ARG B 155 ? 0.7634 0.7820 0.5740 0.0542  0.0383  0.0519  157 ARG B CZ  
2841 N NH1 . ARG B 155 ? 0.7517 0.7614 0.5679 0.0589  0.0406  0.0584  157 ARG B NH1 
2842 N NH2 . ARG B 155 ? 0.7419 0.7682 0.5558 0.0421  0.0326  0.0411  157 ARG B NH2 
2843 N N   . ALA B 156 ? 0.8364 0.7890 0.6057 0.1148  0.0879  0.1085  158 ALA B N   
2844 C CA  . ALA B 156 ? 0.8683 0.8025 0.6241 0.1265  0.1019  0.1201  158 ALA B CA  
2845 C C   . ALA B 156 ? 0.8759 0.7912 0.6385 0.1185  0.1124  0.1190  158 ALA B C   
2846 O O   . ALA B 156 ? 0.8896 0.7821 0.6574 0.1196  0.1254  0.1256  158 ALA B O   
2847 C CB  . ALA B 156 ? 0.8831 0.8327 0.6125 0.1421  0.0999  0.1250  158 ALA B CB  
2848 N N   . LYS B 157 ? 0.8725 0.7974 0.6364 0.1100  0.1073  0.1100  159 LYS B N   
2849 C CA  . LYS B 157 ? 0.8815 0.7918 0.6524 0.1031  0.1166  0.1079  159 LYS B CA  
2850 C C   . LYS B 157 ? 0.8469 0.7434 0.6462 0.0901  0.1185  0.1033  159 LYS B C   
2851 O O   . LYS B 157 ? 0.8532 0.7364 0.6620 0.0858  0.1284  0.1028  159 LYS B O   
2852 C CB  . LYS B 157 ? 0.9386 0.8633 0.7016 0.0982  0.1099  0.0988  159 LYS B CB  
2853 C CG  . LYS B 157 ? 1.0376 0.9485 0.7990 0.0964  0.1220  0.0989  159 LYS B CG  
2854 C CD  . LYS B 157 ? 1.1169 1.0406 0.8658 0.0933  0.1164  0.0902  159 LYS B CD  
2855 C CE  . LYS B 157 ? 1.1858 1.0961 0.9231 0.0970  0.1305  0.0933  159 LYS B CE  
2856 N NZ  . LYS B 157 ? 1.2366 1.1444 0.9440 0.1130  0.1375  0.1037  159 LYS B NZ  
2857 N N   . GLY B 158 ? 0.8015 0.7016 0.6141 0.0845  0.1093  0.0995  160 GLY B N   
2858 C CA  . GLY B 158 ? 0.7688 0.6574 0.6062 0.0731  0.1086  0.0944  160 GLY B CA  
2859 C C   . GLY B 158 ? 0.7304 0.6295 0.5756 0.0650  0.0939  0.0860  160 GLY B C   
2860 O O   . GLY B 158 ? 0.7389 0.6535 0.5762 0.0627  0.0852  0.0801  160 GLY B O   
2861 N N   . ASP B 159 ? 0.6888 0.5782 0.5487 0.0602  0.0917  0.0848  161 ASP B N   
2862 C CA  . ASP B 159 ? 0.6474 0.5438 0.5110 0.0541  0.0791  0.0784  161 ASP B CA  
2863 C C   . ASP B 159 ? 0.5978 0.4916 0.4741 0.0431  0.0728  0.0691  161 ASP B C   
2864 O O   . ASP B 159 ? 0.5880 0.4728 0.4758 0.0405  0.0780  0.0681  161 ASP B O   
2865 C CB  . ASP B 159 ? 0.6753 0.5605 0.5454 0.0551  0.0801  0.0816  161 ASP B CB  
2866 C CG  . ASP B 159 ? 0.8209 0.7042 0.6786 0.0674  0.0884  0.0919  161 ASP B CG  
2867 O OD1 . ASP B 159 ? 0.8378 0.7371 0.6801 0.0751  0.0854  0.0945  161 ASP B OD1 
2868 O OD2 . ASP B 159 ? 0.8708 0.7368 0.7344 0.0694  0.0979  0.0970  161 ASP B OD2 
2869 N N   . LYS B 160 ? 0.5658 0.4670 0.4399 0.0373  0.0621  0.0624  162 LYS B N   
2870 C CA  . LYS B 160 ? 0.5638 0.4605 0.4465 0.0283  0.0559  0.0541  162 LYS B CA  
2871 C C   . LYS B 160 ? 0.5367 0.4280 0.4225 0.0234  0.0473  0.0505  162 LYS B C   
2872 O O   . LYS B 160 ? 0.5402 0.4390 0.4168 0.0252  0.0448  0.0518  162 LYS B O   
2873 C CB  . LYS B 160 ? 0.5850 0.4938 0.4566 0.0255  0.0526  0.0487  162 LYS B CB  
2874 C CG  . LYS B 160 ? 0.6740 0.5876 0.5390 0.0298  0.0602  0.0507  162 LYS B CG  
2875 C CD  . LYS B 160 ? 0.7874 0.7062 0.6467 0.0235  0.0561  0.0423  162 LYS B CD  
2876 C CE  . LYS B 160 ? 0.8915 0.8245 0.7339 0.0263  0.0578  0.0409  162 LYS B CE  
2877 N NZ  . LYS B 160 ? 0.9377 0.8727 0.7760 0.0176  0.0530  0.0309  162 LYS B NZ  
2878 N N   . ILE B 161 ? 0.5131 0.3920 0.4111 0.0182  0.0431  0.0462  163 ILE B N   
2879 C CA  . ILE B 161 ? 0.5228 0.3940 0.4203 0.0136  0.0343  0.0421  163 ILE B CA  
2880 C C   . ILE B 161 ? 0.5051 0.3717 0.4044 0.0080  0.0283  0.0352  163 ILE B C   
2881 O O   . ILE B 161 ? 0.4976 0.3614 0.4078 0.0080  0.0304  0.0339  163 ILE B O   
2882 C CB  . ILE B 161 ? 0.5312 0.3896 0.4398 0.0139  0.0337  0.0434  163 ILE B CB  
2883 C CG1 . ILE B 161 ? 0.5405 0.4004 0.4464 0.0202  0.0417  0.0508  163 ILE B CG1 
2884 C CG2 . ILE B 161 ? 0.5412 0.3906 0.4452 0.0096  0.0240  0.0386  163 ILE B CG2 
2885 C CD1 . ILE B 161 ? 0.5372 0.3836 0.4542 0.0203  0.0440  0.0521  163 ILE B CD1 
2886 N N   . ALA B 162 ? 0.4993 0.3641 0.3878 0.0037  0.0219  0.0309  164 ALA B N   
2887 C CA  . ALA B 162 ? 0.5048 0.3623 0.3912 -0.0009 0.0169  0.0249  164 ALA B CA  
2888 C C   . ALA B 162 ? 0.5234 0.3680 0.4016 -0.0045 0.0093  0.0215  164 ALA B C   
2889 O O   . ALA B 162 ? 0.5154 0.3624 0.3844 -0.0054 0.0092  0.0226  164 ALA B O   
2890 C CB  . ALA B 162 ? 0.5042 0.3722 0.3804 -0.0032 0.0201  0.0224  164 ALA B CB  
2891 N N   . ILE B 163 ? 0.5278 0.3587 0.4087 -0.0057 0.0032  0.0177  165 ILE B N   
2892 C CA  . ILE B 163 ? 0.5167 0.3328 0.3842 -0.0086 -0.0034 0.0143  165 ILE B CA  
2893 C C   . ILE B 163 ? 0.5177 0.3308 0.3742 -0.0126 -0.0021 0.0104  165 ILE B C   
2894 O O   . ILE B 163 ? 0.5133 0.3248 0.3762 -0.0113 -0.0017 0.0085  165 ILE B O   
2895 C CB  . ILE B 163 ? 0.5136 0.3144 0.3879 -0.0059 -0.0122 0.0127  165 ILE B CB  
2896 C CG1 . ILE B 163 ? 0.5389 0.3406 0.4215 -0.0038 -0.0131 0.0153  165 ILE B CG1 
2897 C CG2 . ILE B 163 ? 0.5184 0.3007 0.3740 -0.0078 -0.0186 0.0095  165 ILE B CG2 
2898 C CD1 . ILE B 163 ? 0.5679 0.3566 0.4578 -0.0017 -0.0229 0.0123  165 ILE B CD1 
2899 N N   . TRP B 164 ? 0.5153 0.3265 0.3558 -0.0176 -0.0007 0.0085  166 TRP B N   
2900 C CA  . TRP B 164 ? 0.5298 0.3362 0.3578 -0.0232 0.0019  0.0038  166 TRP B CA  
2901 C C   . TRP B 164 ? 0.5482 0.3293 0.3634 -0.0239 -0.0031 0.0016  166 TRP B C   
2902 O O   . TRP B 164 ? 0.5720 0.3422 0.3795 -0.0233 -0.0069 0.0028  166 TRP B O   
2903 C CB  . TRP B 164 ? 0.5296 0.3491 0.3485 -0.0293 0.0073  0.0021  166 TRP B CB  
2904 C CG  . TRP B 164 ? 0.5214 0.3659 0.3480 -0.0282 0.0119  0.0033  166 TRP B CG  
2905 C CD1 . TRP B 164 ? 0.5174 0.3731 0.3565 -0.0215 0.0128  0.0083  166 TRP B CD1 
2906 C CD2 . TRP B 164 ? 0.5253 0.3863 0.3461 -0.0340 0.0163  -0.0010 166 TRP B CD2 
2907 N NE1 . TRP B 164 ? 0.5073 0.3838 0.3460 -0.0214 0.0172  0.0081  166 TRP B NE1 
2908 C CE2 . TRP B 164 ? 0.5197 0.4019 0.3482 -0.0290 0.0185  0.0021  166 TRP B CE2 
2909 C CE3 . TRP B 164 ? 0.5184 0.3785 0.3281 -0.0432 0.0190  -0.0075 166 TRP B CE3 
2910 C CZ2 . TRP B 164 ? 0.5359 0.4396 0.3612 -0.0319 0.0212  -0.0015 166 TRP B CZ2 
2911 C CZ3 . TRP B 164 ? 0.5371 0.4196 0.3466 -0.0477 0.0224  -0.0119 166 TRP B CZ3 
2912 C CH2 . TRP B 164 ? 0.5366 0.4416 0.3535 -0.0417 0.0225  -0.0091 166 TRP B CH2 
2913 N N   . THR B 165 ? 0.5420 0.3123 0.3528 -0.0244 -0.0027 -0.0016 167 THR B N   
2914 C CA  . THR B 165 ? 0.5675 0.3118 0.3635 -0.0236 -0.0068 -0.0032 167 THR B CA  
2915 C C   . THR B 165 ? 0.5874 0.3224 0.3672 -0.0309 0.0003  -0.0077 167 THR B C   
2916 O O   . THR B 165 ? 0.5792 0.3289 0.3626 -0.0358 0.0069  -0.0106 167 THR B O   
2917 C CB  . THR B 165 ? 0.5984 0.3338 0.4052 -0.0149 -0.0145 -0.0025 167 THR B CB  
2918 O OG1 . THR B 165 ? 0.6057 0.3423 0.4168 -0.0145 -0.0103 -0.0049 167 THR B OG1 
2919 C CG2 . THR B 165 ? 0.5957 0.3446 0.4238 -0.0096 -0.0194 0.0003  167 THR B CG2 
2920 N N   . THR B 166 ? 0.6203 0.3291 0.3805 -0.0316 -0.0007 -0.0086 168 THR B N   
2921 C CA  . THR B 166 ? 0.6573 0.3529 0.3987 -0.0403 0.0077  -0.0129 168 THR B CA  
2922 C C   . THR B 166 ? 0.6924 0.3759 0.4295 -0.0404 0.0114  -0.0164 168 THR B C   
2923 O O   . THR B 166 ? 0.6676 0.3484 0.3948 -0.0500 0.0206  -0.0216 168 THR B O   
2924 C CB  . THR B 166 ? 0.6930 0.3622 0.4118 -0.0411 0.0071  -0.0117 168 THR B CB  
2925 O OG1 . THR B 166 ? 0.7262 0.3874 0.4294 -0.0524 0.0181  -0.0162 168 THR B OG1 
2926 C CG2 . THR B 166 ? 0.6938 0.3345 0.4015 -0.0311 -0.0006 -0.0093 168 THR B CG2 
2927 N N   . GLU B 167 ? 0.6936 0.3702 0.4389 -0.0302 0.0048  -0.0143 169 GLU B N   
2928 C CA  . GLU B 167 ? 0.7002 0.3601 0.4390 -0.0283 0.0083  -0.0171 169 GLU B CA  
2929 C C   . GLU B 167 ? 0.6835 0.3569 0.4448 -0.0196 0.0042  -0.0161 169 GLU B C   
2930 O O   . GLU B 167 ? 0.6699 0.3406 0.4412 -0.0095 -0.0050 -0.0131 169 GLU B O   
2931 C CB  . GLU B 167 ? 0.7603 0.3858 0.4775 -0.0228 0.0050  -0.0155 169 GLU B CB  
2932 C CG  . GLU B 167 ? 0.8402 0.4439 0.5477 -0.0193 0.0092  -0.0179 169 GLU B CG  
2933 C CD  . GLU B 167 ? 0.8510 0.4580 0.5543 -0.0307 0.0218  -0.0239 169 GLU B CD  
2934 O OE1 . GLU B 167 ? 0.9271 0.5244 0.6132 -0.0418 0.0301  -0.0271 169 GLU B OE1 
2935 O OE2 . GLU B 167 ? 0.8082 0.4283 0.5258 -0.0290 0.0239  -0.0262 169 GLU B OE2 
2936 N N   . CYS B 168 ? 0.6749 0.3640 0.4445 -0.0241 0.0116  -0.0195 170 CYS B N   
2937 C CA  . CYS B 168 ? 0.6867 0.3898 0.4775 -0.0172 0.0107  -0.0187 170 CYS B CA  
2938 C C   . CYS B 168 ? 0.7046 0.3883 0.4957 -0.0078 0.0084  -0.0192 170 CYS B C   
2939 O O   . CYS B 168 ? 0.7052 0.4005 0.5171 -0.0006 0.0065  -0.0182 170 CYS B O   
2940 C CB  . CYS B 168 ? 0.6945 0.4179 0.4902 -0.0238 0.0194  -0.0221 170 CYS B CB  
2941 S SG  . CYS B 168 ? 0.9272 0.6353 0.7024 -0.0328 0.0300  -0.0299 170 CYS B SG  
2942 N N   . GLU B 169 ? 0.7231 0.3772 0.4917 -0.0072 0.0094  -0.0205 171 GLU B N   
2943 C CA  . GLU B 169 ? 0.7414 0.3758 0.5090 0.0040  0.0065  -0.0203 171 GLU B CA  
2944 C C   . GLU B 169 ? 0.7441 0.3673 0.5121 0.0155  -0.0066 -0.0162 171 GLU B C   
2945 O O   . GLU B 169 ? 0.7421 0.3508 0.5105 0.0267  -0.0107 -0.0158 171 GLU B O   
2946 C CB  . GLU B 169 ? 0.7550 0.3613 0.4970 -0.0003 0.0160  -0.0239 171 GLU B CB  
2947 C CG  . GLU B 169 ? 0.7918 0.4085 0.5330 -0.0115 0.0280  -0.0297 171 GLU B CG  
2948 C CD  . GLU B 169 ? 0.8354 0.4726 0.5979 -0.0082 0.0310  -0.0314 171 GLU B CD  
2949 O OE1 . GLU B 169 ? 0.7582 0.3980 0.5379 0.0039  0.0259  -0.0288 171 GLU B OE1 
2950 O OE2 . GLU B 169 ? 0.8446 0.4948 0.6056 -0.0180 0.0393  -0.0360 171 GLU B OE2 
2951 N N   . ASN B 170 ? 0.7265 0.3562 0.4941 0.0135  -0.0134 -0.0135 172 ASN B N   
2952 C CA  . ASN B 170 ? 0.7320 0.3532 0.5000 0.0241  -0.0269 -0.0106 172 ASN B CA  
2953 C C   . ASN B 170 ? 0.7101 0.3578 0.5120 0.0300  -0.0343 -0.0104 172 ASN B C   
2954 O O   . ASN B 170 ? 0.6889 0.3525 0.5019 0.0273  -0.0387 -0.0091 172 ASN B O   
2955 C CB  . ASN B 170 ? 0.7623 0.3756 0.5122 0.0190  -0.0299 -0.0084 172 ASN B CB  
2956 C CG  . ASN B 170 ? 0.8372 0.4175 0.5520 0.0164  -0.0247 -0.0081 172 ASN B CG  
2957 O OD1 . ASN B 170 ? 0.8169 0.3745 0.5172 0.0201  -0.0204 -0.0089 172 ASN B OD1 
2958 N ND2 . ASN B 170 ? 0.8683 0.4437 0.5680 0.0100  -0.0241 -0.0067 172 ASN B ND2 
2959 N N   . ARG B 171 ? 0.7089 0.3605 0.5276 0.0379  -0.0341 -0.0120 173 ARG B N   
2960 C CA  . ARG B 171 ? 0.6985 0.3750 0.5523 0.0434  -0.0388 -0.0128 173 ARG B CA  
2961 C C   . ARG B 171 ? 0.6909 0.3733 0.5563 0.0492  -0.0534 -0.0121 173 ARG B C   
2962 O O   . ARG B 171 ? 0.6530 0.3577 0.5410 0.0458  -0.0543 -0.0123 173 ARG B O   
2963 C CB  . ARG B 171 ? 0.7302 0.4052 0.5980 0.0531  -0.0373 -0.0150 173 ARG B CB  
2964 C CG  . ARG B 171 ? 0.7590 0.4619 0.6660 0.0569  -0.0390 -0.0165 173 ARG B CG  
2965 C CD  . ARG B 171 ? 0.8527 0.5590 0.7749 0.0628  -0.0312 -0.0189 173 ARG B CD  
2966 N NE  . ARG B 171 ? 0.9210 0.6548 0.8764 0.0607  -0.0257 -0.0201 173 ARG B NE  
2967 C CZ  . ARG B 171 ? 0.9526 0.6946 0.9209 0.0608  -0.0136 -0.0217 173 ARG B CZ  
2968 N NH1 . ARG B 171 ? 0.9596 0.6850 0.9114 0.0629  -0.0060 -0.0231 173 ARG B NH1 
2969 N NH2 . ARG B 171 ? 0.9368 0.7017 0.9335 0.0587  -0.0081 -0.0221 173 ARG B NH2 
2970 N N   . GLU B 172 ? 0.7135 0.3753 0.5625 0.0581  -0.0648 -0.0116 174 GLU B N   
2971 C CA  . GLU B 172 ? 0.7129 0.3799 0.5718 0.0646  -0.0805 -0.0123 174 GLU B CA  
2972 C C   . GLU B 172 ? 0.7073 0.3799 0.5595 0.0547  -0.0807 -0.0109 174 GLU B C   
2973 O O   . GLU B 172 ? 0.6916 0.3815 0.5656 0.0547  -0.0878 -0.0125 174 GLU B O   
2974 C CB  . GLU B 172 ? 0.7838 0.4245 0.6205 0.0777  -0.0928 -0.0118 174 GLU B CB  
2975 C CG  . GLU B 172 ? 0.9236 0.5646 0.7608 0.0842  -0.1103 -0.0130 174 GLU B CG  
2976 C CD  . GLU B 172 ? 1.1205 0.7895 0.9978 0.0894  -0.1217 -0.0178 174 GLU B CD  
2977 O OE1 . GLU B 172 ? 1.1813 0.8755 1.0893 0.0822  -0.1135 -0.0194 174 GLU B OE1 
2978 O OE2 . GLU B 172 ? 1.1598 0.8251 1.0373 0.1006  -0.1388 -0.0202 174 GLU B OE2 
2979 N N   . ALA B 173 ? 0.7121 0.3704 0.5358 0.0460  -0.0721 -0.0084 175 ALA B N   
2980 C CA  . ALA B 173 ? 0.7043 0.3690 0.5226 0.0370  -0.0701 -0.0069 175 ALA B CA  
2981 C C   . ALA B 173 ? 0.6743 0.3676 0.5194 0.0298  -0.0622 -0.0070 175 ALA B C   
2982 O O   . ALA B 173 ? 0.6546 0.3604 0.5125 0.0280  -0.0658 -0.0069 175 ALA B O   
2983 C CB  . ALA B 173 ? 0.7151 0.3607 0.5006 0.0293  -0.0612 -0.0050 175 ALA B CB  
2984 N N   . VAL B 174 ? 0.6639 0.3655 0.5155 0.0263  -0.0510 -0.0073 176 VAL B N   
2985 C CA  . VAL B 174 ? 0.6401 0.3649 0.5095 0.0199  -0.0419 -0.0066 176 VAL B CA  
2986 C C   . VAL B 174 ? 0.6271 0.3698 0.5289 0.0244  -0.0463 -0.0075 176 VAL B C   
2987 O O   . VAL B 174 ? 0.6248 0.3815 0.5382 0.0204  -0.0440 -0.0061 176 VAL B O   
2988 C CB  . VAL B 174 ? 0.6393 0.3662 0.5044 0.0159  -0.0296 -0.0075 176 VAL B CB  
2989 C CG1 . VAL B 174 ? 0.6348 0.3858 0.5197 0.0122  -0.0211 -0.0065 176 VAL B CG1 
2990 C CG2 . VAL B 174 ? 0.6462 0.3594 0.4819 0.0082  -0.0236 -0.0076 176 VAL B CG2 
2991 N N   . THR B 175 ? 0.6432 0.3853 0.5605 0.0329  -0.0521 -0.0102 177 THR B N   
2992 C CA  . THR B 175 ? 0.6538 0.4142 0.6057 0.0366  -0.0557 -0.0126 177 THR B CA  
2993 C C   . THR B 175 ? 0.6568 0.4190 0.6158 0.0379  -0.0683 -0.0141 177 THR B C   
2994 O O   . THR B 175 ? 0.6440 0.4230 0.6287 0.0355  -0.0671 -0.0155 177 THR B O   
2995 C CB  . THR B 175 ? 0.6981 0.4601 0.6674 0.0458  -0.0582 -0.0159 177 THR B CB  
2996 O OG1 . THR B 175 ? 0.7469 0.4906 0.7003 0.0542  -0.0703 -0.0170 177 THR B OG1 
2997 C CG2 . THR B 175 ? 0.6990 0.4609 0.6650 0.0442  -0.0447 -0.0151 177 THR B CG2 
2998 N N   . HIS B 176 ? 0.6689 0.4128 0.6045 0.0413  -0.0793 -0.0143 178 HIS B N   
2999 C CA  . HIS B 176 ? 0.6616 0.4051 0.5991 0.0418  -0.0910 -0.0163 178 HIS B CA  
3000 C C   . HIS B 176 ? 0.6414 0.3908 0.5754 0.0323  -0.0831 -0.0134 178 HIS B C   
3001 O O   . HIS B 176 ? 0.6315 0.3925 0.5851 0.0301  -0.0854 -0.0155 178 HIS B O   
3002 C CB  . HIS B 176 ? 0.7152 0.4339 0.6211 0.0477  -0.1025 -0.0161 178 HIS B CB  
3003 C CG  . HIS B 176 ? 0.7659 0.4815 0.6690 0.0489  -0.1152 -0.0187 178 HIS B CG  
3004 N ND1 . HIS B 176 ? 0.8076 0.5158 0.6915 0.0419  -0.1119 -0.0163 178 HIS B ND1 
3005 C CD2 . HIS B 176 ? 0.7914 0.5107 0.7083 0.0564  -0.1312 -0.0242 178 HIS B CD2 
3006 C CE1 . HIS B 176 ? 0.8045 0.5103 0.6898 0.0450  -0.1253 -0.0203 178 HIS B CE1 
3007 N NE2 . HIS B 176 ? 0.8048 0.5180 0.7100 0.0534  -0.1377 -0.0254 178 HIS B NE2 
3008 N N   . ILE B 177 ? 0.6326 0.3742 0.5422 0.0265  -0.0732 -0.0092 179 ILE B N   
3009 C CA  . ILE B 177 ? 0.6131 0.3620 0.5189 0.0186  -0.0643 -0.0059 179 ILE B CA  
3010 C C   . ILE B 177 ? 0.6049 0.3748 0.5393 0.0163  -0.0560 -0.0054 179 ILE B C   
3011 O O   . ILE B 177 ? 0.6002 0.3769 0.5449 0.0138  -0.0554 -0.0049 179 ILE B O   
3012 C CB  . ILE B 177 ? 0.6070 0.3486 0.4867 0.0133  -0.0547 -0.0027 179 ILE B CB  
3013 C CG1 . ILE B 177 ? 0.6289 0.3468 0.4784 0.0145  -0.0609 -0.0029 179 ILE B CG1 
3014 C CG2 . ILE B 177 ? 0.5904 0.3449 0.4709 0.0068  -0.0451 0.0007  179 ILE B CG2 
3015 C CD1 . ILE B 177 ? 0.6442 0.3524 0.4696 0.0090  -0.0509 -0.0015 179 ILE B CD1 
3016 N N   . GLY B 178 ? 0.5837 0.3618 0.5299 0.0174  -0.0490 -0.0054 180 GLY B N   
3017 C CA  . GLY B 178 ? 0.5762 0.3720 0.5468 0.0155  -0.0390 -0.0044 180 GLY B CA  
3018 C C   . GLY B 178 ? 0.5905 0.3945 0.5895 0.0171  -0.0445 -0.0079 180 GLY B C   
3019 O O   . GLY B 178 ? 0.5749 0.3876 0.5865 0.0134  -0.0378 -0.0062 180 GLY B O   
3020 N N   . ARG B 179 ? 0.5894 0.3904 0.5985 0.0228  -0.0571 -0.0131 181 ARG B N   
3021 C CA  . ARG B 179 ? 0.5885 0.4004 0.6286 0.0236  -0.0633 -0.0185 181 ARG B CA  
3022 C C   . ARG B 179 ? 0.6025 0.4096 0.6372 0.0201  -0.0699 -0.0197 181 ARG B C   
3023 O O   . ARG B 179 ? 0.6073 0.4242 0.6653 0.0166  -0.0674 -0.0222 181 ARG B O   
3024 C CB  . ARG B 179 ? 0.6262 0.4401 0.6819 0.0318  -0.0758 -0.0247 181 ARG B CB  
3025 C CG  . ARG B 179 ? 0.6902 0.5142 0.7642 0.0347  -0.0664 -0.0248 181 ARG B CG  
3026 C CD  . ARG B 179 ? 0.7914 0.6136 0.8720 0.0446  -0.0774 -0.0292 181 ARG B CD  
3027 N NE  . ARG B 179 ? 0.8445 0.6767 0.9440 0.0469  -0.0662 -0.0295 181 ARG B NE  
3028 C CZ  . ARG B 179 ? 0.9254 0.7509 1.0187 0.0547  -0.0671 -0.0298 181 ARG B CZ  
3029 N NH1 . ARG B 179 ? 0.9481 0.7829 1.0594 0.0562  -0.0553 -0.0303 181 ARG B NH1 
3030 N NH2 . ARG B 179 ? 0.9524 0.7597 1.0198 0.0613  -0.0789 -0.0294 181 ARG B NH2 
3031 N N   . VAL B 180 ? 0.6169 0.4079 0.6215 0.0208  -0.0775 -0.0183 182 VAL B N   
3032 C CA  . VAL B 180 ? 0.6287 0.4132 0.6246 0.0174  -0.0820 -0.0191 182 VAL B CA  
3033 C C   . VAL B 180 ? 0.6198 0.4090 0.6142 0.0111  -0.0672 -0.0136 182 VAL B C   
3034 O O   . VAL B 180 ? 0.6270 0.4188 0.6328 0.0076  -0.0656 -0.0150 182 VAL B O   
3035 C CB  . VAL B 180 ? 0.6636 0.4280 0.6246 0.0201  -0.0914 -0.0183 182 VAL B CB  
3036 C CG1 . VAL B 180 ? 0.6953 0.4516 0.6442 0.0165  -0.0939 -0.0187 182 VAL B CG1 
3037 C CG2 . VAL B 180 ? 0.6810 0.4387 0.6410 0.0284  -0.1073 -0.0234 182 VAL B CG2 
3038 N N   . TYR B 181 ? 0.5916 0.3816 0.5717 0.0099  -0.0561 -0.0076 183 TYR B N   
3039 C CA  . TYR B 181 ? 0.5789 0.3752 0.5573 0.0059  -0.0425 -0.0019 183 TYR B CA  
3040 C C   . TYR B 181 ? 0.5622 0.3709 0.5700 0.0043  -0.0338 -0.0022 183 TYR B C   
3041 O O   . TYR B 181 ? 0.5495 0.3582 0.5624 0.0017  -0.0291 -0.0009 183 TYR B O   
3042 C CB  . TYR B 181 ? 0.5695 0.3676 0.5306 0.0055  -0.0339 0.0028  183 TYR B CB  
3043 C CG  . TYR B 181 ? 0.5546 0.3596 0.5088 0.0030  -0.0217 0.0088  183 TYR B CG  
3044 C CD1 . TYR B 181 ? 0.5602 0.3622 0.5096 0.0018  -0.0205 0.0110  183 TYR B CD1 
3045 C CD2 . TYR B 181 ? 0.5661 0.3798 0.5158 0.0028  -0.0120 0.0122  183 TYR B CD2 
3046 C CE1 . TYR B 181 ? 0.5559 0.3644 0.4981 0.0015  -0.0098 0.0169  183 TYR B CE1 
3047 C CE2 . TYR B 181 ? 0.5496 0.3705 0.4907 0.0022  -0.0027 0.0176  183 TYR B CE2 
3048 C CZ  . TYR B 181 ? 0.5516 0.3703 0.4900 0.0021  -0.0015 0.0203  183 TYR B CZ  
3049 O OH  . TYR B 181 ? 0.5614 0.3880 0.4910 0.0033  0.0074  0.0260  183 TYR B OH  
3050 N N   . LYS B 182 ? 0.5742 0.3921 0.6014 0.0060  -0.0307 -0.0040 184 LYS B N   
3051 C CA  . LYS B 182 ? 0.5943 0.4230 0.6512 0.0042  -0.0215 -0.0050 184 LYS B CA  
3052 C C   . LYS B 182 ? 0.6105 0.4392 0.6874 0.0014  -0.0278 -0.0110 184 LYS B C   
3053 O O   . LYS B 182 ? 0.6401 0.4707 0.7286 -0.0025 -0.0172 -0.0094 184 LYS B O   
3054 C CB  . LYS B 182 ? 0.6155 0.4530 0.6904 0.0071  -0.0194 -0.0076 184 LYS B CB  
3055 C CG  . LYS B 182 ? 0.6850 0.5332 0.7880 0.0050  -0.0060 -0.0077 184 LYS B CG  
3056 C CD  . LYS B 182 ? 0.7460 0.6023 0.8634 0.0084  -0.0013 -0.0095 184 LYS B CD  
3057 C CE  . LYS B 182 ? 0.7907 0.6582 0.9440 0.0061  0.0090  -0.0127 184 LYS B CE  
3058 N NZ  . LYS B 182 ? 0.8245 0.6997 0.9918 0.0098  0.0151  -0.0143 184 LYS B NZ  
3059 N N   . GLU B 183 ? 0.6076 0.4328 0.6865 0.0034  -0.0445 -0.0180 185 GLU B N   
3060 C CA  . GLU B 183 ? 0.6226 0.4476 0.7176 0.0004  -0.0527 -0.0252 185 GLU B CA  
3061 C C   . GLU B 183 ? 0.6437 0.4577 0.7212 -0.0037 -0.0483 -0.0218 185 GLU B C   
3062 O O   . GLU B 183 ? 0.6273 0.4425 0.7217 -0.0086 -0.0429 -0.0244 185 GLU B O   
3063 C CB  . GLU B 183 ? 0.6795 0.5005 0.7706 0.0051  -0.0734 -0.0326 185 GLU B CB  
3064 C CG  . GLU B 183 ? 0.8318 0.6538 0.9388 0.0025  -0.0852 -0.0421 185 GLU B CG  
3065 C CD  . GLU B 183 ? 0.9982 0.8150 1.0957 0.0090  -0.1069 -0.0487 185 GLU B CD  
3066 O OE1 . GLU B 183 ? 1.0474 0.8545 1.1191 0.0154  -0.1118 -0.0444 185 GLU B OE1 
3067 O OE2 . GLU B 183 ? 1.0440 0.8656 1.1589 0.0078  -0.1190 -0.0585 185 GLU B OE2 
3068 N N   . ARG B 184 ? 0.6547 0.4577 0.6992 -0.0017 -0.0498 -0.0164 186 ARG B N   
3069 C CA  . ARG B 184 ? 0.6453 0.4379 0.6722 -0.0043 -0.0460 -0.0132 186 ARG B CA  
3070 C C   . ARG B 184 ? 0.6553 0.4517 0.6864 -0.0064 -0.0279 -0.0061 186 ARG B C   
3071 O O   . ARG B 184 ? 0.6706 0.4597 0.6988 -0.0088 -0.0230 -0.0051 186 ARG B O   
3072 C CB  . ARG B 184 ? 0.6607 0.4415 0.6528 -0.0016 -0.0516 -0.0098 186 ARG B CB  
3073 C CG  . ARG B 184 ? 0.6537 0.4246 0.6360 0.0009  -0.0694 -0.0165 186 ARG B CG  
3074 C CD  . ARG B 184 ? 0.6832 0.4447 0.6636 -0.0014 -0.0761 -0.0218 186 ARG B CD  
3075 N NE  . ARG B 184 ? 0.7172 0.4670 0.6715 -0.0025 -0.0697 -0.0165 186 ARG B NE  
3076 C CZ  . ARG B 184 ? 0.7365 0.4716 0.6613 -0.0006 -0.0762 -0.0162 186 ARG B CZ  
3077 N NH1 . ARG B 184 ? 0.7430 0.4702 0.6569 0.0032  -0.0902 -0.0205 186 ARG B NH1 
3078 N NH2 . ARG B 184 ? 0.7369 0.4640 0.6423 -0.0017 -0.0683 -0.0116 186 ARG B NH2 
3079 N N   . LEU B 185 ? 0.6492 0.4550 0.6850 -0.0048 -0.0175 -0.0010 187 LEU B N   
3080 C CA  . LEU B 185 ? 0.6691 0.4781 0.7085 -0.0054 -0.0001 0.0060  187 LEU B CA  
3081 C C   . LEU B 185 ? 0.6931 0.5047 0.7627 -0.0094 0.0074  0.0023  187 LEU B C   
3082 O O   . LEU B 185 ? 0.6978 0.5060 0.7681 -0.0102 0.0215  0.0076  187 LEU B O   
3083 C CB  . LEU B 185 ? 0.6560 0.4737 0.6892 -0.0023 0.0083  0.0118  187 LEU B CB  
3084 C CG  . LEU B 185 ? 0.6576 0.4742 0.6616 0.0003  0.0053  0.0160  187 LEU B CG  
3085 C CD1 . LEU B 185 ? 0.6500 0.4757 0.6502 0.0025  0.0126  0.0195  187 LEU B CD1 
3086 C CD2 . LEU B 185 ? 0.6690 0.4806 0.6541 0.0012  0.0100  0.0217  187 LEU B CD2 
3087 N N   . GLY B 186 ? 0.7153 0.5331 0.8095 -0.0115 -0.0012 -0.0066 188 GLY B N   
3088 C CA  . GLY B 186 ? 0.7460 0.5688 0.8734 -0.0166 0.0056  -0.0121 188 GLY B CA  
3089 C C   . GLY B 186 ? 0.7689 0.6015 0.9131 -0.0161 0.0201  -0.0089 188 GLY B C   
3090 O O   . GLY B 186 ? 0.7629 0.5970 0.9304 -0.0207 0.0323  -0.0106 188 GLY B O   
3091 N N   . LEU B 187 ? 0.7963 0.6341 0.9284 -0.0109 0.0200  -0.0047 189 LEU B N   
3092 C CA  . LEU B 187 ? 0.8265 0.6716 0.9701 -0.0099 0.0351  -0.0011 189 LEU B CA  
3093 C C   . LEU B 187 ? 0.8596 0.7165 1.0406 -0.0122 0.0328  -0.0105 189 LEU B C   
3094 O O   . LEU B 187 ? 0.8595 0.7213 1.0485 -0.0107 0.0160  -0.0181 189 LEU B O   
3095 C CB  . LEU B 187 ? 0.8399 0.6869 0.9600 -0.0044 0.0357  0.0047  189 LEU B CB  
3096 C CG  . LEU B 187 ? 0.8671 0.7071 0.9524 -0.0018 0.0376  0.0130  189 LEU B CG  
3097 C CD1 . LEU B 187 ? 0.8664 0.7101 0.9320 0.0020  0.0369  0.0161  189 LEU B CD1 
3098 C CD2 . LEU B 187 ? 0.8836 0.7194 0.9643 -0.0017 0.0543  0.0207  189 LEU B CD2 
3099 N N   . PRO B 188 ? 0.8799 0.7412 1.0841 -0.0153 0.0499  -0.0102 190 PRO B N   
3100 C CA  . PRO B 188 ? 0.8881 0.7636 1.1303 -0.0170 0.0490  -0.0194 190 PRO B CA  
3101 C C   . PRO B 188 ? 0.9188 0.8023 1.1585 -0.0103 0.0416  -0.0204 190 PRO B C   
3102 O O   . PRO B 188 ? 0.9450 0.8229 1.1558 -0.0058 0.0451  -0.0126 190 PRO B O   
3103 C CB  . PRO B 188 ? 0.8829 0.7583 1.1427 -0.0211 0.0731  -0.0162 190 PRO B CB  
3104 C CG  . PRO B 188 ? 0.9040 0.7639 1.1377 -0.0219 0.0842  -0.0067 190 PRO B CG  
3105 C CD  . PRO B 188 ? 0.8868 0.7399 1.0835 -0.0167 0.0712  -0.0015 190 PRO B CD  
3106 N N   . PRO B 189 ? 0.9198 0.8164 1.1894 -0.0093 0.0312  -0.0303 191 PRO B N   
3107 C CA  . PRO B 189 ? 0.9234 0.8266 1.1932 -0.0020 0.0270  -0.0312 191 PRO B CA  
3108 C C   . PRO B 189 ? 0.9253 0.8287 1.1910 -0.0002 0.0468  -0.0247 191 PRO B C   
3109 O O   . PRO B 189 ? 0.9334 0.8351 1.1822 0.0058  0.0442  -0.0223 191 PRO B O   
3110 C CB  . PRO B 189 ? 0.9124 0.8327 1.2246 -0.0017 0.0178  -0.0432 191 PRO B CB  
3111 C CG  . PRO B 189 ? 0.9115 0.8332 1.2387 -0.0084 0.0101  -0.0499 191 PRO B CG  
3112 C CD  . PRO B 189 ? 0.9037 0.8102 1.2083 -0.0142 0.0222  -0.0419 191 PRO B CD  
3113 N N   . LYS B 190 ? 0.9123 0.8163 1.1925 -0.0052 0.0669  -0.0222 192 LYS B N   
3114 C CA  . LYS B 190 ? 0.9170 0.8184 1.1883 -0.0032 0.0871  -0.0152 192 LYS B CA  
3115 C C   . LYS B 190 ? 0.9192 0.8080 1.1445 0.0005  0.0893  -0.0048 192 LYS B C   
3116 O O   . LYS B 190 ? 0.9299 0.8176 1.1416 0.0044  0.0985  -0.0009 192 LYS B O   
3117 C CB  . LYS B 190 ? 0.9462 0.8470 1.2385 -0.0093 0.1093  -0.0138 192 LYS B CB  
3118 C CG  . LYS B 190 ? 1.0174 0.9073 1.3011 -0.0149 0.1127  -0.0103 192 LYS B CG  
3119 C CD  . LYS B 190 ? 1.0855 0.9672 1.3741 -0.0188 0.1386  -0.0047 192 LYS B CD  
3120 C CE  . LYS B 190 ? 1.1534 1.0220 1.4319 -0.0234 0.1414  -0.0012 192 LYS B CE  
3121 N NZ  . LYS B 190 ? 1.1986 1.0526 1.4651 -0.0238 0.1667  0.0086  192 LYS B NZ  
3122 N N   . ILE B 191 ? 0.9031 0.7834 1.1054 -0.0007 0.0812  -0.0011 193 ILE B N   
3123 C CA  . ILE B 191 ? 0.8966 0.7683 1.0585 0.0026  0.0820  0.0075  193 ILE B CA  
3124 C C   . ILE B 191 ? 0.8734 0.7456 1.0194 0.0062  0.0656  0.0047  193 ILE B C   
3125 O O   . ILE B 191 ? 0.8724 0.7438 1.0210 0.0056  0.0495  0.0000  193 ILE B O   
3126 C CB  . ILE B 191 ? 0.9092 0.7721 1.0547 0.0003  0.0817  0.0126  193 ILE B CB  
3127 C CG1 . ILE B 191 ? 0.9199 0.7795 1.0846 -0.0038 0.0987  0.0144  193 ILE B CG1 
3128 C CG2 . ILE B 191 ? 0.9246 0.7823 1.0315 0.0044  0.0833  0.0212  193 ILE B CG2 
3129 C CD1 . ILE B 191 ? 0.9607 0.8085 1.1048 -0.0038 0.1066  0.0226  193 ILE B CD1 
3130 N N   . VAL B 192 ? 0.8527 0.7244 0.9808 0.0098  0.0702  0.0074  194 VAL B N   
3131 C CA  . VAL B 192 ? 0.8356 0.7049 0.9474 0.0126  0.0572  0.0047  194 VAL B CA  
3132 C C   . VAL B 192 ? 0.7851 0.6484 0.8600 0.0126  0.0557  0.0102  194 VAL B C   
3133 O O   . VAL B 192 ? 0.7867 0.6500 0.8472 0.0127  0.0673  0.0163  194 VAL B O   
3134 C CB  . VAL B 192 ? 0.8687 0.7416 0.9905 0.0163  0.0616  0.0010  194 VAL B CB  
3135 C CG1 . VAL B 192 ? 0.8669 0.7493 1.0294 0.0165  0.0646  -0.0049 194 VAL B CG1 
3136 C CG2 . VAL B 192 ? 0.8981 0.7694 1.0013 0.0173  0.0773  0.0062  194 VAL B CG2 
3137 N N   . ILE B 193 ? 0.7372 0.5954 0.7967 0.0128  0.0415  0.0079  195 ILE B N   
3138 C CA  . ILE B 193 ? 0.7001 0.5541 0.7280 0.0116  0.0389  0.0117  195 ILE B CA  
3139 C C   . ILE B 193 ? 0.6568 0.5064 0.6693 0.0125  0.0343  0.0085  195 ILE B C   
3140 O O   . ILE B 193 ? 0.6533 0.4991 0.6760 0.0148  0.0270  0.0035  195 ILE B O   
3141 C CB  . ILE B 193 ? 0.6955 0.5449 0.7167 0.0095  0.0287  0.0123  195 ILE B CB  
3142 C CG1 . ILE B 193 ? 0.6931 0.5359 0.7187 0.0102  0.0131  0.0064  195 ILE B CG1 
3143 C CG2 . ILE B 193 ? 0.7082 0.5599 0.7441 0.0083  0.0352  0.0153  195 ILE B CG2 
3144 C CD1 . ILE B 193 ? 0.7050 0.5408 0.7171 0.0083  0.0037  0.0071  195 ILE B CD1 
3145 N N   . GLY B 194 ? 0.6233 0.4733 0.6116 0.0111  0.0388  0.0109  196 GLY B N   
3146 C CA  . GLY B 194 ? 0.5823 0.4274 0.5531 0.0104  0.0372  0.0076  196 GLY B CA  
3147 C C   . GLY B 194 ? 0.5585 0.3973 0.5071 0.0069  0.0285  0.0066  196 GLY B C   
3148 O O   . GLY B 194 ? 0.5476 0.3897 0.4875 0.0049  0.0268  0.0098  196 GLY B O   
3149 N N   . TYR B 195 ? 0.5528 0.3812 0.4920 0.0065  0.0238  0.0021  197 TYR B N   
3150 C CA  . TYR B 195 ? 0.5641 0.3842 0.4803 0.0022  0.0186  0.0005  197 TYR B CA  
3151 C C   . TYR B 195 ? 0.5682 0.3890 0.4683 -0.0013 0.0259  -0.0024 197 TYR B C   
3152 O O   . TYR B 195 ? 0.5619 0.3777 0.4651 0.0008  0.0299  -0.0055 197 TYR B O   
3153 C CB  . TYR B 195 ? 0.5594 0.3631 0.4738 0.0043  0.0087  -0.0024 197 TYR B CB  
3154 C CG  . TYR B 195 ? 0.5417 0.3328 0.4311 -0.0004 0.0049  -0.0040 197 TYR B CG  
3155 C CD1 . TYR B 195 ? 0.5428 0.3313 0.4246 -0.0025 -0.0009 -0.0021 197 TYR B CD1 
3156 C CD2 . TYR B 195 ? 0.5617 0.3416 0.4350 -0.0030 0.0083  -0.0079 197 TYR B CD2 
3157 C CE1 . TYR B 195 ? 0.5541 0.3307 0.4135 -0.0074 -0.0023 -0.0036 197 TYR B CE1 
3158 C CE2 . TYR B 195 ? 0.5785 0.3454 0.4295 -0.0085 0.0068  -0.0097 197 TYR B CE2 
3159 C CZ  . TYR B 195 ? 0.5939 0.3593 0.4382 -0.0106 0.0017  -0.0074 197 TYR B CZ  
3160 O OH  . TYR B 195 ? 0.6343 0.3857 0.4568 -0.0163 0.0018  -0.0094 197 TYR B OH  
3161 N N   . GLN B 196 ? 0.5727 0.4004 0.4563 -0.0065 0.0276  -0.0023 198 GLN B N   
3162 C CA  . GLN B 196 ? 0.5868 0.4173 0.4549 -0.0110 0.0335  -0.0064 198 GLN B CA  
3163 C C   . GLN B 196 ? 0.5912 0.4133 0.4413 -0.0180 0.0302  -0.0107 198 GLN B C   
3164 O O   . GLN B 196 ? 0.5811 0.4063 0.4268 -0.0207 0.0260  -0.0090 198 GLN B O   
3165 C CB  . GLN B 196 ? 0.6064 0.4556 0.4712 -0.0110 0.0389  -0.0037 198 GLN B CB  
3166 C CG  . GLN B 196 ? 0.6900 0.5455 0.5708 -0.0042 0.0448  0.0015  198 GLN B CG  
3167 C CD  . GLN B 196 ? 0.8058 0.6768 0.6820 -0.0021 0.0489  0.0067  198 GLN B CD  
3168 O OE1 . GLN B 196 ? 0.8252 0.7042 0.6917 -0.0042 0.0452  0.0076  198 GLN B OE1 
3169 N NE2 . GLN B 196 ? 0.8390 0.7138 0.7216 0.0030  0.0573  0.0103  198 GLN B NE2 
3170 N N   . SER B 197 ? 0.5846 0.3952 0.4238 -0.0215 0.0332  -0.0167 199 SER B N   
3171 C CA  . SER B 197 ? 0.6043 0.4067 0.4249 -0.0302 0.0334  -0.0221 199 SER B CA  
3172 C C   . SER B 197 ? 0.6022 0.4255 0.4161 -0.0365 0.0353  -0.0237 199 SER B C   
3173 O O   . SER B 197 ? 0.6067 0.4455 0.4228 -0.0347 0.0391  -0.0236 199 SER B O   
3174 C CB  . SER B 197 ? 0.6341 0.4224 0.4447 -0.0331 0.0391  -0.0287 199 SER B CB  
3175 O OG  . SER B 197 ? 0.7101 0.4888 0.5029 -0.0428 0.0409  -0.0347 199 SER B OG  
3176 N N   . HIS B 198 ? 0.5986 0.4228 0.4042 -0.0428 0.0330  -0.0254 200 HIS B N   
3177 C CA  . HIS B 198 ? 0.6137 0.4603 0.4143 -0.0488 0.0346  -0.0286 200 HIS B CA  
3178 C C   . HIS B 198 ? 0.6454 0.4971 0.4362 -0.0559 0.0398  -0.0375 200 HIS B C   
3179 O O   . HIS B 198 ? 0.6357 0.5098 0.4256 -0.0566 0.0404  -0.0394 200 HIS B O   
3180 C CB  . HIS B 198 ? 0.6056 0.4511 0.4004 -0.0554 0.0327  -0.0301 200 HIS B CB  
3181 C CG  . HIS B 198 ? 0.6112 0.4546 0.4130 -0.0496 0.0277  -0.0225 200 HIS B CG  
3182 N ND1 . HIS B 198 ? 0.5968 0.4521 0.4109 -0.0408 0.0254  -0.0152 200 HIS B ND1 
3183 C CD2 . HIS B 198 ? 0.6257 0.4541 0.4222 -0.0517 0.0254  -0.0215 200 HIS B CD2 
3184 C CE1 . HIS B 198 ? 0.6199 0.4680 0.4365 -0.0384 0.0214  -0.0109 200 HIS B CE1 
3185 N NE2 . HIS B 198 ? 0.6297 0.4620 0.4353 -0.0445 0.0210  -0.0144 200 HIS B NE2 
3186 N N   . ALA B 199 ? 0.6780 0.5083 0.4600 -0.0607 0.0433  -0.0432 201 ALA B N   
3187 C CA  . ALA B 199 ? 0.7345 0.5656 0.5062 -0.0679 0.0490  -0.0526 201 ALA B CA  
3188 C C   . ALA B 199 ? 0.7820 0.6248 0.5579 -0.0607 0.0511  -0.0510 201 ALA B C   
3189 O O   . ALA B 199 ? 0.8054 0.6646 0.5746 -0.0646 0.0531  -0.0569 201 ALA B O   
3190 C CB  . ALA B 199 ? 0.7539 0.5548 0.5152 -0.0722 0.0534  -0.0574 201 ALA B CB  
3191 N N   . ASP B 200 ? 0.7730 0.6086 0.5600 -0.0501 0.0508  -0.0432 202 ASP B N   
3192 C CA  . ASP B 200 ? 0.7713 0.6176 0.5633 -0.0427 0.0544  -0.0403 202 ASP B CA  
3193 C C   . ASP B 200 ? 0.7809 0.6523 0.5760 -0.0388 0.0522  -0.0352 202 ASP B C   
3194 O O   . ASP B 200 ? 0.7997 0.6839 0.5879 -0.0373 0.0555  -0.0370 202 ASP B O   
3195 C CB  . ASP B 200 ? 0.7923 0.6252 0.5985 -0.0333 0.0556  -0.0342 202 ASP B CB  
3196 C CG  . ASP B 200 ? 0.8685 0.6772 0.6720 -0.0337 0.0583  -0.0385 202 ASP B CG  
3197 O OD1 . ASP B 200 ? 0.9227 0.7227 0.7108 -0.0416 0.0617  -0.0467 202 ASP B OD1 
3198 O OD2 . ASP B 200 ? 0.8769 0.6753 0.6941 -0.0258 0.0570  -0.0340 202 ASP B OD2 
3199 N N   . THR B 201 ? 0.7525 0.6300 0.5561 -0.0362 0.0469  -0.0286 203 THR B N   
3200 C CA  . THR B 201 ? 0.7647 0.6643 0.5695 -0.0319 0.0452  -0.0237 203 THR B CA  
3201 C C   . THR B 201 ? 0.7891 0.7086 0.5814 -0.0381 0.0438  -0.0310 203 THR B C   
3202 O O   . THR B 201 ? 0.7914 0.7290 0.5800 -0.0327 0.0440  -0.0286 203 THR B O   
3203 C CB  . THR B 201 ? 0.7677 0.6682 0.5824 -0.0288 0.0404  -0.0165 203 THR B CB  
3204 O OG1 . THR B 201 ? 0.7707 0.6550 0.5979 -0.0234 0.0408  -0.0113 203 THR B OG1 
3205 C CG2 . THR B 201 ? 0.7737 0.6944 0.5897 -0.0220 0.0399  -0.0101 203 THR B CG2 
3206 N N   . ALA B 202 ? 0.8059 0.7220 0.5919 -0.0490 0.0427  -0.0399 204 ALA B N   
3207 C CA  . ALA B 202 ? 0.8264 0.7631 0.6040 -0.0568 0.0410  -0.0489 204 ALA B CA  
3208 C C   . ALA B 202 ? 0.8409 0.7863 0.6073 -0.0574 0.0437  -0.0558 204 ALA B C   
3209 O O   . ALA B 202 ? 0.8580 0.8257 0.6184 -0.0616 0.0407  -0.0628 204 ALA B O   
3210 C CB  . ALA B 202 ? 0.8301 0.7565 0.6042 -0.0698 0.0416  -0.0578 204 ALA B CB  
3211 N N   . THR B 203 ? 0.8400 0.7684 0.6037 -0.0535 0.0492  -0.0545 205 THR B N   
3212 C CA  . THR B 203 ? 0.8435 0.7760 0.5945 -0.0536 0.0530  -0.0608 205 THR B CA  
3213 C C   . THR B 203 ? 0.8219 0.7606 0.5741 -0.0401 0.0552  -0.0506 205 THR B C   
3214 O O   . THR B 203 ? 0.8311 0.7548 0.5935 -0.0334 0.0591  -0.0424 205 THR B O   
3215 C CB  . THR B 203 ? 0.8875 0.7942 0.6333 -0.0591 0.0596  -0.0675 205 THR B CB  
3216 O OG1 . THR B 203 ? 0.9166 0.8051 0.6721 -0.0501 0.0637  -0.0587 205 THR B OG1 
3217 C CG2 . THR B 203 ? 0.9043 0.7980 0.6489 -0.0714 0.0592  -0.0753 205 THR B CG2 
3218 N N   . LYS B 204 ? 0.7848 0.7452 0.5267 -0.0359 0.0530  -0.0512 206 LYS B N   
3219 C CA  . LYS B 204 ? 0.7725 0.7370 0.5115 -0.0226 0.0564  -0.0410 206 LYS B CA  
3220 C C   . LYS B 204 ? 0.7482 0.7010 0.4752 -0.0209 0.0646  -0.0445 206 LYS B C   
3221 O O   . LYS B 204 ? 0.7303 0.6902 0.4409 -0.0257 0.0639  -0.0548 206 LYS B O   
3222 C CB  . LYS B 204 ? 0.8110 0.8029 0.5416 -0.0169 0.0500  -0.0392 206 LYS B CB  
3223 C CG  . LYS B 204 ? 0.8799 0.8850 0.6227 -0.0178 0.0426  -0.0361 206 LYS B CG  
3224 C CD  . LYS B 204 ? 0.9655 0.9612 0.7211 -0.0087 0.0450  -0.0222 206 LYS B CD  
3225 C CE  . LYS B 204 ? 1.0399 1.0496 0.8042 -0.0071 0.0386  -0.0182 206 LYS B CE  
3226 N NZ  . LYS B 204 ? 1.0533 1.0679 0.8174 0.0072  0.0403  -0.0053 206 LYS B NZ  
3227 N N   . SER B 205 ? 0.7571 0.6923 0.4929 -0.0142 0.0727  -0.0365 207 SER B N   
3228 C CA  . SER B 205 ? 0.7943 0.7140 0.5233 -0.0128 0.0825  -0.0395 207 SER B CA  
3229 C C   . SER B 205 ? 0.8178 0.7336 0.5475 -0.0007 0.0918  -0.0288 207 SER B C   
3230 O O   . SER B 205 ? 0.8400 0.7411 0.5694 0.0014  0.1016  -0.0295 207 SER B O   
3231 C CB  . SER B 205 ? 0.8453 0.7437 0.5875 -0.0184 0.0852  -0.0428 207 SER B CB  
3232 O OG  . SER B 205 ? 0.8899 0.7830 0.6536 -0.0147 0.0834  -0.0337 207 SER B OG  
3233 N N   . GLY B 206 ? 0.8228 0.7504 0.5526 0.0073  0.0899  -0.0192 208 GLY B N   
3234 C CA  . GLY B 206 ? 0.8502 0.7726 0.5783 0.0184  0.1001  -0.0087 208 GLY B CA  
3235 C C   . GLY B 206 ? 0.8726 0.7985 0.6151 0.0242  0.0985  0.0027  208 GLY B C   
3236 O O   . GLY B 206 ? 0.8758 0.8143 0.6208 0.0221  0.0882  0.0027  208 GLY B O   
3237 N N   . SER B 207 ? 0.8891 0.8036 0.6417 0.0312  0.1095  0.0121  209 SER B N   
3238 C CA  . SER B 207 ? 0.9048 0.8202 0.6718 0.0359  0.1090  0.0223  209 SER B CA  
3239 C C   . SER B 207 ? 0.9174 0.8299 0.7083 0.0286  0.1011  0.0201  209 SER B C   
3240 O O   . SER B 207 ? 0.9218 0.8408 0.7181 0.0293  0.0944  0.0243  209 SER B O   
3241 C CB  . SER B 207 ? 0.9253 0.8282 0.6987 0.0435  0.1238  0.0320  209 SER B CB  
3242 O OG  . SER B 207 ? 0.9567 0.8495 0.7232 0.0452  0.1361  0.0300  209 SER B OG  
3243 N N   . THR B 208 ? 0.9143 0.8163 0.7179 0.0224  0.1018  0.0136  210 THR B N   
3244 C CA  . THR B 208 ? 0.9101 0.8058 0.7363 0.0177  0.0956  0.0127  210 THR B CA  
3245 C C   . THR B 208 ? 0.8861 0.7796 0.7090 0.0089  0.0869  0.0027  210 THR B C   
3246 O O   . THR B 208 ? 0.8854 0.7806 0.6916 0.0055  0.0876  -0.0044 210 THR B O   
3247 C CB  . THR B 208 ? 0.9510 0.8344 0.7990 0.0203  0.1049  0.0153  210 THR B CB  
3248 O OG1 . THR B 208 ? 0.9900 0.8663 0.8338 0.0188  0.1106  0.0086  210 THR B OG1 
3249 C CG2 . THR B 208 ? 0.9651 0.8480 0.8157 0.0278  0.1165  0.0247  210 THR B CG2 
3250 N N   . THR B 209 ? 0.8597 0.7479 0.6972 0.0052  0.0794  0.0022  211 THR B N   
3251 C CA  . THR B 209 ? 0.8406 0.7198 0.6775 -0.0019 0.0735  -0.0057 211 THR B CA  
3252 C C   . THR B 209 ? 0.7775 0.6423 0.6343 0.0004  0.0753  -0.0053 211 THR B C   
3253 O O   . THR B 209 ? 0.7692 0.6341 0.6442 0.0048  0.0760  0.0007  211 THR B O   
3254 C CB  . THR B 209 ? 0.8792 0.7628 0.7142 -0.0067 0.0634  -0.0062 211 THR B CB  
3255 O OG1 . THR B 209 ? 0.9156 0.8161 0.7354 -0.0078 0.0616  -0.0068 211 THR B OG1 
3256 C CG2 . THR B 209 ? 0.8812 0.7521 0.7133 -0.0139 0.0587  -0.0135 211 THR B CG2 
3257 N N   . LYS B 210 ? 0.7318 0.5847 0.5859 -0.0024 0.0760  -0.0121 212 LYS B N   
3258 C CA  . LYS B 210 ? 0.7069 0.5476 0.5803 0.0012  0.0763  -0.0122 212 LYS B CA  
3259 C C   . LYS B 210 ? 0.6785 0.5148 0.5631 0.0008  0.0654  -0.0103 212 LYS B C   
3260 O O   . LYS B 210 ? 0.6604 0.4969 0.5335 -0.0042 0.0582  -0.0112 212 LYS B O   
3261 C CB  . LYS B 210 ? 0.7524 0.5794 0.6189 0.0001  0.0804  -0.0196 212 LYS B CB  
3262 C CG  . LYS B 210 ? 0.8151 0.6324 0.6647 -0.0069 0.0743  -0.0256 212 LYS B CG  
3263 C CD  . LYS B 210 ? 0.8756 0.6779 0.7149 -0.0082 0.0806  -0.0331 212 LYS B CD  
3264 C CE  . LYS B 210 ? 0.9553 0.7457 0.7771 -0.0164 0.0761  -0.0391 212 LYS B CE  
3265 N NZ  . LYS B 210 ? 1.0096 0.7818 0.8193 -0.0183 0.0829  -0.0467 212 LYS B NZ  
3266 N N   . ASN B 211 ? 0.6585 0.4915 0.5658 0.0060  0.0647  -0.0081 213 ASN B N   
3267 C CA  . ASN B 211 ? 0.6636 0.4911 0.5825 0.0071  0.0543  -0.0071 213 ASN B CA  
3268 C C   . ASN B 211 ? 0.6785 0.4903 0.5957 0.0086  0.0500  -0.0120 213 ASN B C   
3269 O O   . ASN B 211 ? 0.6950 0.5026 0.6220 0.0131  0.0552  -0.0144 213 ASN B O   
3270 C CB  . ASN B 211 ? 0.6603 0.4943 0.6068 0.0121  0.0552  -0.0033 213 ASN B CB  
3271 C CG  . ASN B 211 ? 0.6885 0.5338 0.6353 0.0112  0.0590  0.0024  213 ASN B CG  
3272 O OD1 . ASN B 211 ? 0.6754 0.5238 0.6067 0.0079  0.0549  0.0043  213 ASN B OD1 
3273 N ND2 . ASN B 211 ? 0.7195 0.5705 0.6839 0.0144  0.0678  0.0053  213 ASN B ND2 
3274 N N   . ARG B 212 ? 0.6663 0.4683 0.5699 0.0053  0.0415  -0.0133 214 ARG B N   
3275 C CA  . ARG B 212 ? 0.6801 0.4637 0.5793 0.0078  0.0361  -0.0166 214 ARG B CA  
3276 C C   . ARG B 212 ? 0.6800 0.4639 0.6040 0.0161  0.0291  -0.0149 214 ARG B C   
3277 O O   . ARG B 212 ? 0.6907 0.4665 0.6232 0.0226  0.0290  -0.0174 214 ARG B O   
3278 C CB  . ARG B 212 ? 0.7256 0.4988 0.6032 0.0018  0.0298  -0.0173 214 ARG B CB  
3279 C CG  . ARG B 212 ? 0.8384 0.5885 0.7050 0.0042  0.0244  -0.0195 214 ARG B CG  
3280 C CD  . ARG B 212 ? 0.8744 0.6103 0.7281 0.0033  0.0320  -0.0244 214 ARG B CD  
3281 N NE  . ARG B 212 ? 0.9346 0.6726 0.7687 -0.0074 0.0394  -0.0284 214 ARG B NE  
3282 C CZ  . ARG B 212 ? 0.9750 0.7043 0.7893 -0.0157 0.0386  -0.0306 214 ARG B CZ  
3283 N NH1 . ARG B 212 ? 0.9909 0.7260 0.7915 -0.0257 0.0451  -0.0356 214 ARG B NH1 
3284 N NH2 . ARG B 212 ? 1.0025 0.7176 0.8105 -0.0143 0.0313  -0.0282 214 ARG B NH2 
3285 N N   . PHE B 213 ? 0.6476 0.4415 0.5841 0.0162  0.0234  -0.0113 215 PHE B N   
3286 C CA  . PHE B 213 ? 0.6522 0.4499 0.6145 0.0226  0.0160  -0.0110 215 PHE B CA  
3287 C C   . PHE B 213 ? 0.6763 0.4910 0.6580 0.0212  0.0198  -0.0077 215 PHE B C   
3288 O O   . PHE B 213 ? 0.6734 0.4946 0.6447 0.0161  0.0248  -0.0044 215 PHE B O   
3289 C CB  . PHE B 213 ? 0.6519 0.4379 0.6063 0.0243  0.0020  -0.0111 215 PHE B CB  
3290 C CG  . PHE B 213 ? 0.6660 0.4309 0.5943 0.0245  -0.0013 -0.0130 215 PHE B CG  
3291 C CD1 . PHE B 213 ? 0.6905 0.4437 0.6190 0.0311  -0.0008 -0.0158 215 PHE B CD1 
3292 C CD2 . PHE B 213 ? 0.6865 0.4420 0.5900 0.0183  -0.0038 -0.0119 215 PHE B CD2 
3293 C CE1 . PHE B 213 ? 0.7109 0.4411 0.6132 0.0312  -0.0022 -0.0171 215 PHE B CE1 
3294 C CE2 . PHE B 213 ? 0.7107 0.4444 0.5896 0.0176  -0.0049 -0.0136 215 PHE B CE2 
3295 C CZ  . PHE B 213 ? 0.7140 0.4341 0.5913 0.0239  -0.0038 -0.0160 215 PHE B CZ  
3296 N N   . VAL B 214 ? 0.6877 0.5095 0.6984 0.0259  0.0177  -0.0090 216 VAL B N   
3297 C CA  . VAL B 214 ? 0.7075 0.5423 0.7396 0.0244  0.0210  -0.0069 216 VAL B CA  
3298 C C   . VAL B 214 ? 0.7486 0.5849 0.8015 0.0276  0.0079  -0.0100 216 VAL B C   
3299 O O   . VAL B 214 ? 0.7602 0.5921 0.8202 0.0336  -0.0003 -0.0140 216 VAL B O   
3300 C CB  . VAL B 214 ? 0.7043 0.5495 0.7559 0.0254  0.0359  -0.0065 216 VAL B CB  
3301 C CG1 . VAL B 214 ? 0.7239 0.5678 0.7524 0.0228  0.0480  -0.0038 216 VAL B CG1 
3302 C CG2 . VAL B 214 ? 0.6951 0.5424 0.7709 0.0317  0.0355  -0.0115 216 VAL B CG2 
3303 N N   . VAL B 215 ? 0.7701 0.6119 0.8316 0.0242  0.0058  -0.0084 217 VAL B N   
3304 C CA  . VAL B 215 ? 0.7910 0.6376 0.8769 0.0261  -0.0051 -0.0126 217 VAL B CA  
3305 C C   . VAL B 215 ? 0.7954 0.6524 0.9014 0.0214  0.0033  -0.0113 217 VAL B C   
3306 O O   . VAL B 215 ? 0.7939 0.6581 0.9270 0.0216  -0.0029 -0.0162 217 VAL B O   
3307 C CB  . VAL B 215 ? 0.8151 0.6507 0.8842 0.0270  -0.0217 -0.0138 217 VAL B CB  
3308 C CG1 . VAL B 215 ? 0.8391 0.6602 0.8856 0.0319  -0.0291 -0.0147 217 VAL B CG1 
3309 C CG2 . VAL B 215 ? 0.8280 0.6597 0.8775 0.0208  -0.0197 -0.0092 217 VAL B CG2 
3310 O OXT . VAL B 215 ? 0.8159 0.6735 0.9104 0.0177  0.0158  -0.0057 217 VAL B OXT 
# 
