data_8QM5
# 
_entry.id   8QM5 
# 
_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   8QM5         pdb_00008qm5 10.2210/pdb8qm5/pdb 
WWPDB D_1292133481 ?            ?                   
# 
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                        8QM5 
_pdbx_database_status.recvd_initial_deposition_date   2023-09-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              Andrew.Woodhead@astx.com 
_pdbx_contact_author.name_first         Andrew 
_pdbx_contact_author.name_last          Woodhead 
_pdbx_contact_author.name_mi            J. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0009-0005-1604-2904 
# 
_audit_author.name               'Cleasby, A.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0003-2619-9532 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                10037 
_citation.page_last                 10037 
_citation.title                     
'Integrating fragment-based screening with targeted protein degradation and genetic rescue to explore eIF4E function.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-024-54356-1 
_citation.pdbx_database_id_PubMed   40016190 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Sharp, S.Y.'          1  ? 
primary 'Martella, M.'         2  ? 
primary 
;D'Agostino, S.
;
3  ? 
primary 'Milton, C.I.'         4  ? 
primary 'Ward, G.'             5  ? 
primary 'Woodhead, A.J.'       6  ? 
primary 'Richardson, C.J.'     7  ? 
primary 'Carr, M.G.'           8  ? 
primary 'Chiarparin, E.'       9  ? 
primary 'Cons, B.D.'           10 ? 
primary 'Coyle, J.'            11 ? 
primary 'East, C.E.'           12 ? 
primary 'Hiscock, S.D.'        13 ? 
primary 'Martinez-Fleites, C.' 14 ? 
primary 'Mortenson, P.N.'      15 ? 
primary 'Palmer, N.'           16 ? 
primary 'Pathuri, P.'          17 ? 
primary 'Powers, M.V.'         18 ? 
primary 'Saalau, S.M.'         19 ? 
primary 'St Denis, J.D.'       20 ? 
primary 'Swabey, K.'           21 ? 
primary 'Vinkovic, M.'         22 ? 
primary 'Walton, H.'           23 ? 
primary 'Williams, G.'         24 ? 
primary 'Clarke, P.A.'         25 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Eukaryotic translation initiation factor 4E'      25014.445 2   ? ? ? ? 
2 non-polymer syn '1-(4-chlorophenyl)cyclopentane-1-carboxylic acid' 224.683   2   ? ? ? ? 
3 non-polymer syn 'TRIETHYLENE GLYCOL'                               150.173   1   ? ? ? ? 
4 water       nat water                                              18.015    191 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MHHHHHHGARIIYDRAFLMACRGGGGENLYFQGKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLS
SNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLNRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDK
IAIWTTECENREAVTHIGRVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MHHHHHHGARIIYDRAFLMACRGGGGENLYFQGKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLS
SNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLNRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDK
IAIWTTECENREAVTHIGRVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '1-(4-chlorophenyl)cyclopentane-1-carboxylic acid' W4U 
3 'TRIETHYLENE GLYCOL'                               PGE 
4 water                                              HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   GLY n 
1 9   ALA n 
1 10  ARG n 
1 11  ILE n 
1 12  ILE n 
1 13  TYR n 
1 14  ASP n 
1 15  ARG n 
1 16  ALA n 
1 17  PHE n 
1 18  LEU n 
1 19  MET n 
1 20  ALA n 
1 21  CYS n 
1 22  ARG n 
1 23  GLY n 
1 24  GLY n 
1 25  GLY n 
1 26  GLY n 
1 27  GLU n 
1 28  ASN n 
1 29  LEU n 
1 30  TYR n 
1 31  PHE n 
1 32  GLN n 
1 33  GLY n 
1 34  LYS n 
1 35  HIS n 
1 36  PRO n 
1 37  LEU n 
1 38  GLN n 
1 39  ASN n 
1 40  ARG n 
1 41  TRP n 
1 42  ALA n 
1 43  LEU n 
1 44  TRP n 
1 45  PHE n 
1 46  PHE n 
1 47  LYS n 
1 48  ASN n 
1 49  ASP n 
1 50  LYS n 
1 51  SER n 
1 52  LYS n 
1 53  THR n 
1 54  TRP n 
1 55  GLN n 
1 56  ALA n 
1 57  ASN n 
1 58  LEU n 
1 59  ARG n 
1 60  LEU n 
1 61  ILE n 
1 62  SER n 
1 63  LYS n 
1 64  PHE n 
1 65  ASP n 
1 66  THR n 
1 67  VAL n 
1 68  GLU n 
1 69  ASP n 
1 70  PHE n 
1 71  TRP n 
1 72  ALA n 
1 73  LEU n 
1 74  TYR n 
1 75  ASN n 
1 76  HIS n 
1 77  ILE n 
1 78  GLN n 
1 79  LEU n 
1 80  SER n 
1 81  SER n 
1 82  ASN n 
1 83  LEU n 
1 84  MET n 
1 85  PRO n 
1 86  GLY n 
1 87  CYS n 
1 88  ASP n 
1 89  TYR n 
1 90  SER n 
1 91  LEU n 
1 92  PHE n 
1 93  LYS n 
1 94  ASP n 
1 95  GLY n 
1 96  ILE n 
1 97  GLU n 
1 98  PRO n 
1 99  MET n 
1 100 TRP n 
1 101 GLU n 
1 102 ASP n 
1 103 GLU n 
1 104 LYS n 
1 105 ASN n 
1 106 LYS n 
1 107 ARG n 
1 108 GLY n 
1 109 GLY n 
1 110 ARG n 
1 111 TRP n 
1 112 LEU n 
1 113 ILE n 
1 114 THR n 
1 115 LEU n 
1 116 ASN n 
1 117 LYS n 
1 118 GLN n 
1 119 GLN n 
1 120 ARG n 
1 121 ARG n 
1 122 SER n 
1 123 ASP n 
1 124 LEU n 
1 125 ASN n 
1 126 ARG n 
1 127 PHE n 
1 128 TRP n 
1 129 LEU n 
1 130 GLU n 
1 131 THR n 
1 132 LEU n 
1 133 LEU n 
1 134 CYS n 
1 135 LEU n 
1 136 ILE n 
1 137 GLY n 
1 138 GLU n 
1 139 SER n 
1 140 PHE n 
1 141 ASP n 
1 142 ASP n 
1 143 TYR n 
1 144 SER n 
1 145 ASP n 
1 146 ASP n 
1 147 VAL n 
1 148 CYS n 
1 149 GLY n 
1 150 ALA n 
1 151 VAL n 
1 152 VAL n 
1 153 ASN n 
1 154 VAL n 
1 155 ARG n 
1 156 ALA n 
1 157 LYS n 
1 158 GLY n 
1 159 ASP n 
1 160 LYS n 
1 161 ILE n 
1 162 ALA n 
1 163 ILE n 
1 164 TRP n 
1 165 THR n 
1 166 THR n 
1 167 GLU n 
1 168 CYS n 
1 169 GLU n 
1 170 ASN n 
1 171 ARG n 
1 172 GLU n 
1 173 ALA n 
1 174 VAL n 
1 175 THR n 
1 176 HIS n 
1 177 ILE n 
1 178 GLY n 
1 179 ARG n 
1 180 VAL n 
1 181 TYR n 
1 182 LYS n 
1 183 GLU n 
1 184 ARG n 
1 185 LEU n 
1 186 GLY n 
1 187 LEU n 
1 188 PRO n 
1 189 PRO n 
1 190 LYS n 
1 191 ILE n 
1 192 VAL n 
1 193 ILE n 
1 194 GLY n 
1 195 TYR n 
1 196 GLN n 
1 197 SER n 
1 198 HIS n 
1 199 ALA n 
1 200 ASP n 
1 201 THR n 
1 202 ALA n 
1 203 THR n 
1 204 LYS n 
1 205 SER n 
1 206 GLY n 
1 207 SER n 
1 208 THR n 
1 209 THR n 
1 210 LYS n 
1 211 ASN n 
1 212 ARG n 
1 213 PHE n 
1 214 VAL n 
1 215 VAL n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   215 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 EIF4E 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21-CodonPlus (DE3)-RIPL' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                            ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                           ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                         ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                    ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                                           ? 'C3 H7 N O2 S'   121.158 
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 
W4U non-polymer         . '1-(4-chlorophenyl)cyclopentane-1-carboxylic acid' ? 'C12 H13 Cl O2'  224.683 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   3   ?   ?   ?   A . n 
A 1 2   HIS 2   4   ?   ?   ?   A . n 
A 1 3   HIS 3   5   ?   ?   ?   A . n 
A 1 4   HIS 4   6   ?   ?   ?   A . n 
A 1 5   HIS 5   7   ?   ?   ?   A . n 
A 1 6   HIS 6   8   ?   ?   ?   A . n 
A 1 7   HIS 7   9   ?   ?   ?   A . n 
A 1 8   GLY 8   10  ?   ?   ?   A . n 
A 1 9   ALA 9   11  11  ALA ALA A . n 
A 1 10  ARG 10  12  12  ARG ARG A . n 
A 1 11  ILE 11  13  13  ILE ILE A . n 
A 1 12  ILE 12  14  14  ILE ILE A . n 
A 1 13  TYR 13  15  15  TYR TYR A . n 
A 1 14  ASP 14  16  16  ASP ASP A . n 
A 1 15  ARG 15  17  17  ARG ARG A . n 
A 1 16  ALA 16  18  18  ALA ALA A . n 
A 1 17  PHE 17  19  19  PHE PHE A . n 
A 1 18  LEU 18  20  20  LEU LEU A . n 
A 1 19  MET 19  21  21  MET MET A . n 
A 1 20  ALA 20  22  22  ALA ALA A . n 
A 1 21  CYS 21  23  23  CYS CYS A . n 
A 1 22  ARG 22  24  24  ARG ARG A . n 
A 1 23  GLY 23  25  25  GLY GLY A . n 
A 1 24  GLY 24  26  26  GLY GLY A . n 
A 1 25  GLY 25  27  27  GLY GLY A . n 
A 1 26  GLY 26  28  28  GLY GLY A . n 
A 1 27  GLU 27  29  29  GLU GLU A . n 
A 1 28  ASN 28  30  30  ASN ASN A . n 
A 1 29  LEU 29  31  31  LEU LEU A . n 
A 1 30  TYR 30  32  32  TYR TYR A . n 
A 1 31  PHE 31  33  33  PHE PHE A . n 
A 1 32  GLN 32  34  34  GLN GLN A . n 
A 1 33  GLY 33  35  35  GLY GLY A . n 
A 1 34  LYS 34  36  36  LYS LYS A . n 
A 1 35  HIS 35  37  37  HIS HIS A . n 
A 1 36  PRO 36  38  38  PRO PRO A . n 
A 1 37  LEU 37  39  39  LEU LEU A . n 
A 1 38  GLN 38  40  40  GLN GLN A . n 
A 1 39  ASN 39  41  41  ASN ASN A . n 
A 1 40  ARG 40  42  42  ARG ARG A . n 
A 1 41  TRP 41  43  43  TRP TRP A . n 
A 1 42  ALA 42  44  44  ALA ALA A . n 
A 1 43  LEU 43  45  45  LEU LEU A . n 
A 1 44  TRP 44  46  46  TRP TRP A . n 
A 1 45  PHE 45  47  47  PHE PHE A . n 
A 1 46  PHE 46  48  48  PHE PHE A . n 
A 1 47  LYS 47  49  49  LYS LYS A . n 
A 1 48  ASN 48  50  50  ASN ASN A . n 
A 1 49  ASP 49  51  51  ASP ASP A . n 
A 1 50  LYS 50  52  52  LYS LYS A . n 
A 1 51  SER 51  53  53  SER SER A . n 
A 1 52  LYS 52  54  54  LYS LYS A . n 
A 1 53  THR 53  55  55  THR THR A . n 
A 1 54  TRP 54  56  56  TRP TRP A . n 
A 1 55  GLN 55  57  57  GLN GLN A . n 
A 1 56  ALA 56  58  58  ALA ALA A . n 
A 1 57  ASN 57  59  59  ASN ASN A . n 
A 1 58  LEU 58  60  60  LEU LEU A . n 
A 1 59  ARG 59  61  61  ARG ARG A . n 
A 1 60  LEU 60  62  62  LEU LEU A . n 
A 1 61  ILE 61  63  63  ILE ILE A . n 
A 1 62  SER 62  64  64  SER SER A . n 
A 1 63  LYS 63  65  65  LYS LYS A . n 
A 1 64  PHE 64  66  66  PHE PHE A . n 
A 1 65  ASP 65  67  67  ASP ASP A . n 
A 1 66  THR 66  68  68  THR THR A . n 
A 1 67  VAL 67  69  69  VAL VAL A . n 
A 1 68  GLU 68  70  70  GLU GLU A . n 
A 1 69  ASP 69  71  71  ASP ASP A . n 
A 1 70  PHE 70  72  72  PHE PHE A . n 
A 1 71  TRP 71  73  73  TRP TRP A . n 
A 1 72  ALA 72  74  74  ALA ALA A . n 
A 1 73  LEU 73  75  75  LEU LEU A . n 
A 1 74  TYR 74  76  76  TYR TYR A . n 
A 1 75  ASN 75  77  77  ASN ASN A . n 
A 1 76  HIS 76  78  78  HIS HIS A . n 
A 1 77  ILE 77  79  79  ILE ILE A . n 
A 1 78  GLN 78  80  80  GLN GLN A . n 
A 1 79  LEU 79  81  81  LEU LEU A . n 
A 1 80  SER 80  82  82  SER SER A . n 
A 1 81  SER 81  83  83  SER SER A . n 
A 1 82  ASN 82  84  84  ASN ASN A . n 
A 1 83  LEU 83  85  85  LEU LEU A . n 
A 1 84  MET 84  86  86  MET MET A . n 
A 1 85  PRO 85  87  87  PRO PRO A . n 
A 1 86  GLY 86  88  88  GLY GLY A . n 
A 1 87  CYS 87  89  89  CYS CYS A . n 
A 1 88  ASP 88  90  90  ASP ASP A . n 
A 1 89  TYR 89  91  91  TYR TYR A . n 
A 1 90  SER 90  92  92  SER SER A . n 
A 1 91  LEU 91  93  93  LEU LEU A . n 
A 1 92  PHE 92  94  94  PHE PHE A . n 
A 1 93  LYS 93  95  95  LYS LYS A . n 
A 1 94  ASP 94  96  96  ASP ASP A . n 
A 1 95  GLY 95  97  97  GLY GLY A . n 
A 1 96  ILE 96  98  98  ILE ILE A . n 
A 1 97  GLU 97  99  99  GLU GLU A . n 
A 1 98  PRO 98  100 100 PRO PRO A . n 
A 1 99  MET 99  101 101 MET MET A . n 
A 1 100 TRP 100 102 102 TRP TRP A . n 
A 1 101 GLU 101 103 103 GLU GLU A . n 
A 1 102 ASP 102 104 104 ASP ASP A . n 
A 1 103 GLU 103 105 105 GLU GLU A . n 
A 1 104 LYS 104 106 106 LYS LYS A . n 
A 1 105 ASN 105 107 107 ASN ASN A . n 
A 1 106 LYS 106 108 108 LYS LYS A . n 
A 1 107 ARG 107 109 109 ARG ARG A . n 
A 1 108 GLY 108 110 110 GLY GLY A . n 
A 1 109 GLY 109 111 111 GLY GLY A . n 
A 1 110 ARG 110 112 112 ARG ARG A . n 
A 1 111 TRP 111 113 113 TRP TRP A . n 
A 1 112 LEU 112 114 114 LEU LEU A . n 
A 1 113 ILE 113 115 115 ILE ILE A . n 
A 1 114 THR 114 116 116 THR THR A . n 
A 1 115 LEU 115 117 117 LEU LEU A . n 
A 1 116 ASN 116 118 118 ASN ASN A . n 
A 1 117 LYS 117 119 119 LYS LYS A . n 
A 1 118 GLN 118 120 120 GLN GLN A . n 
A 1 119 GLN 119 121 121 GLN GLN A . n 
A 1 120 ARG 120 122 122 ARG ARG A . n 
A 1 121 ARG 121 123 123 ARG ARG A . n 
A 1 122 SER 122 124 124 SER SER A . n 
A 1 123 ASP 123 125 125 ASP ASP A . n 
A 1 124 LEU 124 126 126 LEU LEU A . n 
A 1 125 ASN 125 127 127 ASN ASN A . n 
A 1 126 ARG 126 128 128 ARG ARG A . n 
A 1 127 PHE 127 129 129 PHE PHE A . n 
A 1 128 TRP 128 130 130 TRP TRP A . n 
A 1 129 LEU 129 131 131 LEU LEU A . n 
A 1 130 GLU 130 132 132 GLU GLU A . n 
A 1 131 THR 131 133 133 THR THR A . n 
A 1 132 LEU 132 134 134 LEU LEU A . n 
A 1 133 LEU 133 135 135 LEU LEU A . n 
A 1 134 CYS 134 136 136 CYS CYS A . n 
A 1 135 LEU 135 137 137 LEU LEU A . n 
A 1 136 ILE 136 138 138 ILE ILE A . n 
A 1 137 GLY 137 139 139 GLY GLY A . n 
A 1 138 GLU 138 140 140 GLU GLU A . n 
A 1 139 SER 139 141 141 SER SER A . n 
A 1 140 PHE 140 142 142 PHE PHE A . n 
A 1 141 ASP 141 143 143 ASP ASP A . n 
A 1 142 ASP 142 144 144 ASP ASP A . n 
A 1 143 TYR 143 145 145 TYR TYR A . n 
A 1 144 SER 144 146 146 SER SER A . n 
A 1 145 ASP 145 147 147 ASP ASP A . n 
A 1 146 ASP 146 148 148 ASP ASP A . n 
A 1 147 VAL 147 149 149 VAL VAL A . n 
A 1 148 CYS 148 150 150 CYS CYS A . n 
A 1 149 GLY 149 151 151 GLY GLY A . n 
A 1 150 ALA 150 152 152 ALA ALA A . n 
A 1 151 VAL 151 153 153 VAL VAL A . n 
A 1 152 VAL 152 154 154 VAL VAL A . n 
A 1 153 ASN 153 155 155 ASN ASN A . n 
A 1 154 VAL 154 156 156 VAL VAL A . n 
A 1 155 ARG 155 157 157 ARG ARG A . n 
A 1 156 ALA 156 158 158 ALA ALA A . n 
A 1 157 LYS 157 159 159 LYS LYS A . n 
A 1 158 GLY 158 160 160 GLY GLY A . n 
A 1 159 ASP 159 161 161 ASP ASP A . n 
A 1 160 LYS 160 162 162 LYS LYS A . n 
A 1 161 ILE 161 163 163 ILE ILE A . n 
A 1 162 ALA 162 164 164 ALA ALA A . n 
A 1 163 ILE 163 165 165 ILE ILE A . n 
A 1 164 TRP 164 166 166 TRP TRP A . n 
A 1 165 THR 165 167 167 THR THR A . n 
A 1 166 THR 166 168 168 THR THR A . n 
A 1 167 GLU 167 169 169 GLU GLU A . n 
A 1 168 CYS 168 170 170 CYS CYS A . n 
A 1 169 GLU 169 171 171 GLU GLU A . n 
A 1 170 ASN 170 172 172 ASN ASN A . n 
A 1 171 ARG 171 173 173 ARG ARG A . n 
A 1 172 GLU 172 174 174 GLU GLU A . n 
A 1 173 ALA 173 175 175 ALA ALA A . n 
A 1 174 VAL 174 176 176 VAL VAL A . n 
A 1 175 THR 175 177 177 THR THR A . n 
A 1 176 HIS 176 178 178 HIS HIS A . n 
A 1 177 ILE 177 179 179 ILE ILE A . n 
A 1 178 GLY 178 180 180 GLY GLY A . n 
A 1 179 ARG 179 181 181 ARG ARG A . n 
A 1 180 VAL 180 182 182 VAL VAL A . n 
A 1 181 TYR 181 183 183 TYR TYR A . n 
A 1 182 LYS 182 184 184 LYS LYS A . n 
A 1 183 GLU 183 185 185 GLU GLU A . n 
A 1 184 ARG 184 186 186 ARG ARG A . n 
A 1 185 LEU 185 187 187 LEU LEU A . n 
A 1 186 GLY 186 188 188 GLY GLY A . n 
A 1 187 LEU 187 189 189 LEU LEU A . n 
A 1 188 PRO 188 190 190 PRO PRO A . n 
A 1 189 PRO 189 191 191 PRO PRO A . n 
A 1 190 LYS 190 192 192 LYS LYS A . n 
A 1 191 ILE 191 193 193 ILE ILE A . n 
A 1 192 VAL 192 194 194 VAL VAL A . n 
A 1 193 ILE 193 195 195 ILE ILE A . n 
A 1 194 GLY 194 196 196 GLY GLY A . n 
A 1 195 TYR 195 197 197 TYR TYR A . n 
A 1 196 GLN 196 198 198 GLN GLN A . n 
A 1 197 SER 197 199 199 SER SER A . n 
A 1 198 HIS 198 200 200 HIS HIS A . n 
A 1 199 ALA 199 201 201 ALA ALA A . n 
A 1 200 ASP 200 202 202 ASP ASP A . n 
A 1 201 THR 201 203 203 THR THR A . n 
A 1 202 ALA 202 204 204 ALA ALA A . n 
A 1 203 THR 203 205 205 THR THR A . n 
A 1 204 LYS 204 206 206 LYS LYS A . n 
A 1 205 SER 205 207 207 SER SER A . n 
A 1 206 GLY 206 208 208 GLY GLY A . n 
A 1 207 SER 207 209 209 SER SER A . n 
A 1 208 THR 208 210 210 THR THR A . n 
A 1 209 THR 209 211 211 THR THR A . n 
A 1 210 LYS 210 212 212 LYS LYS A . n 
A 1 211 ASN 211 213 213 ASN ASN A . n 
A 1 212 ARG 212 214 214 ARG ARG A . n 
A 1 213 PHE 213 215 215 PHE PHE A . n 
A 1 214 VAL 214 216 216 VAL VAL A . n 
A 1 215 VAL 215 217 217 VAL VAL A . n 
B 1 1   MET 1   3   ?   ?   ?   B . n 
B 1 2   HIS 2   4   ?   ?   ?   B . n 
B 1 3   HIS 3   5   ?   ?   ?   B . n 
B 1 4   HIS 4   6   ?   ?   ?   B . n 
B 1 5   HIS 5   7   ?   ?   ?   B . n 
B 1 6   HIS 6   8   ?   ?   ?   B . n 
B 1 7   HIS 7   9   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  25  GLY GLY B . n 
B 1 24  GLY 24  26  ?   ?   ?   B . n 
B 1 25  GLY 25  27  ?   ?   ?   B . n 
B 1 26  GLY 26  28  ?   ?   ?   B . n 
B 1 27  GLU 27  29  ?   ?   ?   B . n 
B 1 28  ASN 28  30  ?   ?   ?   B . n 
B 1 29  LEU 29  31  ?   ?   ?   B . n 
B 1 30  TYR 30  32  ?   ?   ?   B . n 
B 1 31  PHE 31  33  ?   ?   ?   B . n 
B 1 32  GLN 32  34  ?   ?   ?   B . n 
B 1 33  GLY 33  35  35  GLY GLY B . n 
B 1 34  LYS 34  36  36  LYS LYS B . n 
B 1 35  HIS 35  37  37  HIS HIS B . n 
B 1 36  PRO 36  38  38  PRO PRO B . n 
B 1 37  LEU 37  39  39  LEU LEU B . n 
B 1 38  GLN 38  40  40  GLN GLN B . n 
B 1 39  ASN 39  41  41  ASN ASN B . n 
B 1 40  ARG 40  42  42  ARG ARG B . n 
B 1 41  TRP 41  43  43  TRP TRP B . n 
B 1 42  ALA 42  44  44  ALA ALA B . n 
B 1 43  LEU 43  45  45  LEU LEU B . n 
B 1 44  TRP 44  46  46  TRP TRP B . n 
B 1 45  PHE 45  47  47  PHE PHE B . n 
B 1 46  PHE 46  48  48  PHE PHE B . n 
B 1 47  LYS 47  49  49  LYS LYS B . n 
B 1 48  ASN 48  50  50  ASN ASN B . n 
B 1 49  ASP 49  51  51  ASP ASP B . n 
B 1 50  LYS 50  52  52  LYS LYS B . n 
B 1 51  SER 51  53  53  SER SER B . n 
B 1 52  LYS 52  54  54  LYS LYS B . n 
B 1 53  THR 53  55  55  THR THR B . n 
B 1 54  TRP 54  56  56  TRP TRP B . n 
B 1 55  GLN 55  57  57  GLN GLN B . n 
B 1 56  ALA 56  58  58  ALA ALA B . n 
B 1 57  ASN 57  59  59  ASN ASN B . n 
B 1 58  LEU 58  60  60  LEU LEU B . n 
B 1 59  ARG 59  61  61  ARG ARG B . n 
B 1 60  LEU 60  62  62  LEU LEU B . n 
B 1 61  ILE 61  63  63  ILE ILE B . n 
B 1 62  SER 62  64  64  SER SER B . n 
B 1 63  LYS 63  65  65  LYS LYS B . n 
B 1 64  PHE 64  66  66  PHE PHE B . n 
B 1 65  ASP 65  67  67  ASP ASP B . n 
B 1 66  THR 66  68  68  THR THR B . n 
B 1 67  VAL 67  69  69  VAL VAL B . n 
B 1 68  GLU 68  70  70  GLU GLU B . n 
B 1 69  ASP 69  71  71  ASP ASP B . n 
B 1 70  PHE 70  72  72  PHE PHE B . n 
B 1 71  TRP 71  73  73  TRP TRP B . n 
B 1 72  ALA 72  74  74  ALA ALA B . n 
B 1 73  LEU 73  75  75  LEU LEU B . n 
B 1 74  TYR 74  76  76  TYR TYR B . n 
B 1 75  ASN 75  77  77  ASN ASN B . n 
B 1 76  HIS 76  78  78  HIS HIS B . n 
B 1 77  ILE 77  79  79  ILE ILE B . n 
B 1 78  GLN 78  80  80  GLN GLN B . n 
B 1 79  LEU 79  81  81  LEU LEU B . n 
B 1 80  SER 80  82  82  SER SER B . n 
B 1 81  SER 81  83  83  SER SER B . n 
B 1 82  ASN 82  84  84  ASN ASN B . n 
B 1 83  LEU 83  85  85  LEU LEU B . n 
B 1 84  MET 84  86  86  MET MET B . n 
B 1 85  PRO 85  87  87  PRO PRO B . n 
B 1 86  GLY 86  88  88  GLY GLY B . n 
B 1 87  CYS 87  89  89  CYS CYS B . n 
B 1 88  ASP 88  90  90  ASP ASP B . n 
B 1 89  TYR 89  91  91  TYR TYR B . n 
B 1 90  SER 90  92  92  SER SER B . n 
B 1 91  LEU 91  93  93  LEU LEU B . n 
B 1 92  PHE 92  94  94  PHE PHE B . n 
B 1 93  LYS 93  95  95  LYS LYS B . n 
B 1 94  ASP 94  96  96  ASP ASP B . n 
B 1 95  GLY 95  97  97  GLY GLY B . n 
B 1 96  ILE 96  98  98  ILE ILE B . n 
B 1 97  GLU 97  99  99  GLU GLU B . n 
B 1 98  PRO 98  100 100 PRO PRO B . n 
B 1 99  MET 99  101 101 MET MET B . n 
B 1 100 TRP 100 102 102 TRP TRP B . n 
B 1 101 GLU 101 103 103 GLU GLU B . n 
B 1 102 ASP 102 104 104 ASP ASP B . n 
B 1 103 GLU 103 105 105 GLU GLU B . n 
B 1 104 LYS 104 106 106 LYS LYS B . n 
B 1 105 ASN 105 107 107 ASN ASN B . n 
B 1 106 LYS 106 108 108 LYS LYS B . n 
B 1 107 ARG 107 109 109 ARG ARG B . n 
B 1 108 GLY 108 110 110 GLY GLY B . n 
B 1 109 GLY 109 111 111 GLY GLY B . n 
B 1 110 ARG 110 112 112 ARG ARG B . n 
B 1 111 TRP 111 113 113 TRP TRP B . n 
B 1 112 LEU 112 114 114 LEU LEU B . n 
B 1 113 ILE 113 115 115 ILE ILE B . n 
B 1 114 THR 114 116 116 THR THR B . n 
B 1 115 LEU 115 117 117 LEU LEU B . n 
B 1 116 ASN 116 118 118 ASN ASN B . n 
B 1 117 LYS 117 119 119 LYS LYS B . n 
B 1 118 GLN 118 120 120 GLN GLN B . n 
B 1 119 GLN 119 121 121 GLN GLN B . n 
B 1 120 ARG 120 122 122 ARG ARG B . n 
B 1 121 ARG 121 123 123 ARG ARG B . n 
B 1 122 SER 122 124 124 SER SER B . n 
B 1 123 ASP 123 125 125 ASP ASP B . n 
B 1 124 LEU 124 126 126 LEU LEU B . n 
B 1 125 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 W4U ? ? W4U ? ? 'SUBJECT OF INVESTIGATION' ? 
2 W4U ? ? W4U ? ? '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 W4U 1  301 1   W4U L01 A . 
D 3 PGE 1  301 301 PGE PGE B . 
E 2 W4U 1  302 1   W4U L02 B . 
F 4 HOH 1  401 214 HOH HOH A . 
F 4 HOH 2  402 490 HOH HOH A . 
F 4 HOH 3  403 511 HOH HOH A . 
F 4 HOH 4  404 387 HOH HOH A . 
F 4 HOH 5  405 11  HOH HOH A . 
F 4 HOH 6  406 22  HOH HOH A . 
F 4 HOH 7  407 481 HOH HOH A . 
F 4 HOH 8  408 18  HOH HOH A . 
F 4 HOH 9  409 98  HOH HOH A . 
F 4 HOH 10 410 37  HOH HOH A . 
F 4 HOH 11 411 242 HOH HOH A . 
F 4 HOH 12 412 245 HOH HOH A . 
F 4 HOH 13 413 504 HOH HOH A . 
F 4 HOH 14 414 527 HOH HOH A . 
F 4 HOH 15 415 102 HOH HOH A . 
F 4 HOH 16 416 9   HOH HOH A . 
F 4 HOH 17 417 443 HOH HOH A . 
F 4 HOH 18 418 334 HOH HOH A . 
F 4 HOH 19 419 111 HOH HOH A . 
F 4 HOH 20 420 146 HOH HOH A . 
F 4 HOH 21 421 488 HOH HOH A . 
F 4 HOH 22 422 43  HOH HOH A . 
F 4 HOH 23 423 97  HOH HOH A . 
F 4 HOH 24 424 10  HOH HOH A . 
F 4 HOH 25 425 147 HOH HOH A . 
F 4 HOH 26 426 17  HOH HOH A . 
F 4 HOH 27 427 71  HOH HOH A . 
F 4 HOH 28 428 81  HOH HOH A . 
F 4 HOH 29 429 378 HOH HOH A . 
F 4 HOH 30 430 188 HOH HOH A . 
F 4 HOH 31 431 402 HOH HOH A . 
F 4 HOH 32 432 512 HOH HOH A . 
F 4 HOH 33 433 380 HOH HOH A . 
F 4 HOH 34 434 476 HOH HOH A . 
F 4 HOH 35 435 480 HOH HOH A . 
F 4 HOH 36 436 31  HOH HOH A . 
F 4 HOH 37 437 419 HOH HOH A . 
F 4 HOH 38 438 53  HOH HOH A . 
F 4 HOH 39 439 2   HOH HOH A . 
F 4 HOH 40 440 202 HOH HOH A . 
F 4 HOH 41 441 482 HOH HOH A . 
F 4 HOH 42 442 192 HOH HOH A . 
F 4 HOH 43 443 51  HOH HOH A . 
F 4 HOH 44 444 29  HOH HOH A . 
F 4 HOH 45 445 100 HOH HOH A . 
F 4 HOH 46 446 346 HOH HOH A . 
F 4 HOH 47 447 5   HOH HOH A . 
F 4 HOH 48 448 47  HOH HOH A . 
F 4 HOH 49 449 513 HOH HOH A . 
F 4 HOH 50 450 506 HOH HOH A . 
F 4 HOH 51 451 307 HOH HOH A . 
F 4 HOH 52 452 30  HOH HOH A . 
F 4 HOH 53 453 41  HOH HOH A . 
F 4 HOH 54 454 521 HOH HOH A . 
F 4 HOH 55 455 363 HOH HOH A . 
F 4 HOH 56 456 92  HOH HOH A . 
F 4 HOH 57 457 12  HOH HOH A . 
F 4 HOH 58 458 217 HOH HOH A . 
F 4 HOH 59 459 332 HOH HOH A . 
F 4 HOH 60 460 59  HOH HOH A . 
F 4 HOH 61 461 523 HOH HOH A . 
F 4 HOH 62 462 66  HOH HOH A . 
F 4 HOH 63 463 344 HOH HOH A . 
F 4 HOH 64 464 32  HOH HOH A . 
F 4 HOH 65 465 174 HOH HOH A . 
F 4 HOH 66 466 404 HOH HOH A . 
F 4 HOH 67 467 82  HOH HOH A . 
F 4 HOH 68 468 520 HOH HOH A . 
F 4 HOH 69 469 73  HOH HOH A . 
F 4 HOH 70 470 425 HOH HOH A . 
F 4 HOH 71 471 159 HOH HOH A . 
F 4 HOH 72 472 478 HOH HOH A . 
F 4 HOH 73 473 349 HOH HOH A . 
F 4 HOH 74 474 93  HOH HOH A . 
F 4 HOH 75 475 420 HOH HOH A . 
F 4 HOH 76 476 64  HOH HOH A . 
F 4 HOH 77 477 358 HOH HOH A . 
F 4 HOH 78 478 258 HOH HOH A . 
F 4 HOH 79 479 433 HOH HOH A . 
F 4 HOH 80 480 340 HOH HOH A . 
F 4 HOH 81 481 426 HOH HOH A . 
F 4 HOH 82 482 428 HOH HOH A . 
F 4 HOH 83 483 369 HOH HOH A . 
F 4 HOH 84 484 495 HOH HOH A . 
F 4 HOH 85 485 143 HOH HOH A . 
F 4 HOH 86 486 384 HOH HOH A . 
F 4 HOH 87 487 106 HOH HOH A . 
F 4 HOH 88 488 503 HOH HOH A . 
F 4 HOH 89 489 135 HOH HOH A . 
F 4 HOH 90 490 522 HOH HOH A . 
F 4 HOH 91 491 493 HOH HOH A . 
F 4 HOH 92 492 514 HOH HOH A . 
F 4 HOH 93 493 500 HOH HOH A . 
F 4 HOH 94 494 526 HOH HOH A . 
F 4 HOH 95 495 237 HOH HOH A . 
F 4 HOH 96 496 469 HOH HOH A . 
F 4 HOH 97 497 491 HOH HOH A . 
F 4 HOH 98 498 410 HOH HOH A . 
G 4 HOH 1  401 183 HOH HOH B . 
G 4 HOH 2  402 375 HOH HOH B . 
G 4 HOH 3  403 492 HOH HOH B . 
G 4 HOH 4  404 38  HOH HOH B . 
G 4 HOH 5  405 34  HOH HOH B . 
G 4 HOH 6  406 337 HOH HOH B . 
G 4 HOH 7  407 77  HOH HOH B . 
G 4 HOH 8  408 351 HOH HOH B . 
G 4 HOH 9  409 505 HOH HOH B . 
G 4 HOH 10 410 158 HOH HOH B . 
G 4 HOH 11 411 436 HOH HOH B . 
G 4 HOH 12 412 27  HOH HOH B . 
G 4 HOH 13 413 16  HOH HOH B . 
G 4 HOH 14 414 121 HOH HOH B . 
G 4 HOH 15 415 20  HOH HOH B . 
G 4 HOH 16 416 46  HOH HOH B . 
G 4 HOH 17 417 114 HOH HOH B . 
G 4 HOH 18 418 427 HOH HOH B . 
G 4 HOH 19 419 390 HOH HOH B . 
G 4 HOH 20 420 417 HOH HOH B . 
G 4 HOH 21 421 78  HOH HOH B . 
G 4 HOH 22 422 119 HOH HOH B . 
G 4 HOH 23 423 142 HOH HOH B . 
G 4 HOH 24 424 99  HOH HOH B . 
G 4 HOH 25 425 291 HOH HOH B . 
G 4 HOH 26 426 80  HOH HOH B . 
G 4 HOH 27 427 62  HOH HOH B . 
G 4 HOH 28 428 101 HOH HOH B . 
G 4 HOH 29 429 86  HOH HOH B . 
G 4 HOH 30 430 342 HOH HOH B . 
G 4 HOH 31 431 13  HOH HOH B . 
G 4 HOH 32 432 28  HOH HOH B . 
G 4 HOH 33 433 399 HOH HOH B . 
G 4 HOH 34 434 470 HOH HOH B . 
G 4 HOH 35 435 72  HOH HOH B . 
G 4 HOH 36 436 104 HOH HOH B . 
G 4 HOH 37 437 352 HOH HOH B . 
G 4 HOH 38 438 524 HOH HOH B . 
G 4 HOH 39 439 336 HOH HOH B . 
G 4 HOH 40 440 1   HOH HOH B . 
G 4 HOH 41 441 57  HOH HOH B . 
G 4 HOH 42 442 204 HOH HOH B . 
G 4 HOH 43 443 6   HOH HOH B . 
G 4 HOH 44 444 26  HOH HOH B . 
G 4 HOH 45 445 21  HOH HOH B . 
G 4 HOH 46 446 484 HOH HOH B . 
G 4 HOH 47 447 15  HOH HOH B . 
G 4 HOH 48 448 39  HOH HOH B . 
G 4 HOH 49 449 449 HOH HOH B . 
G 4 HOH 50 450 517 HOH HOH B . 
G 4 HOH 51 451 496 HOH HOH B . 
G 4 HOH 52 452 353 HOH HOH B . 
G 4 HOH 53 453 61  HOH HOH B . 
G 4 HOH 54 454 394 HOH HOH B . 
G 4 HOH 55 455 486 HOH HOH B . 
G 4 HOH 56 456 33  HOH HOH B . 
G 4 HOH 57 457 154 HOH HOH B . 
G 4 HOH 58 458 84  HOH HOH B . 
G 4 HOH 59 459 438 HOH HOH B . 
G 4 HOH 60 460 42  HOH HOH B . 
G 4 HOH 61 461 110 HOH HOH B . 
G 4 HOH 62 462 519 HOH HOH B . 
G 4 HOH 63 463 117 HOH HOH B . 
G 4 HOH 64 464 315 HOH HOH B . 
G 4 HOH 65 465 3   HOH HOH B . 
G 4 HOH 66 466 113 HOH HOH B . 
G 4 HOH 67 467 498 HOH HOH B . 
G 4 HOH 68 468 196 HOH HOH B . 
G 4 HOH 69 469 501 HOH HOH B . 
G 4 HOH 70 470 79  HOH HOH B . 
G 4 HOH 71 471 232 HOH HOH B . 
G 4 HOH 72 472 391 HOH HOH B . 
G 4 HOH 73 473 403 HOH HOH B . 
G 4 HOH 74 474 298 HOH HOH B . 
G 4 HOH 75 475 68  HOH HOH B . 
G 4 HOH 76 476 442 HOH HOH B . 
G 4 HOH 77 477 393 HOH HOH B . 
G 4 HOH 78 478 85  HOH HOH B . 
G 4 HOH 79 479 227 HOH HOH B . 
G 4 HOH 80 480 197 HOH HOH B . 
G 4 HOH 81 481 359 HOH HOH B . 
G 4 HOH 82 482 381 HOH HOH B . 
G 4 HOH 83 483 475 HOH HOH B . 
G 4 HOH 84 484 507 HOH HOH B . 
G 4 HOH 85 485 497 HOH HOH B . 
G 4 HOH 86 486 105 HOH HOH B . 
G 4 HOH 87 487 518 HOH HOH B . 
G 4 HOH 88 488 145 HOH HOH B . 
G 4 HOH 89 489 474 HOH HOH B . 
G 4 HOH 90 490 60  HOH HOH B . 
G 4 HOH 91 491 515 HOH HOH B . 
G 4 HOH 92 492 318 HOH HOH B . 
G 4 HOH 93 493 525 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                   96.57 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QM5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     47.124 
_cell.length_a_esd                 ? 
_cell.length_b                     68.877 
_cell.length_b_esd                 ? 
_cell.length_c                     63.729 
_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                         8QM5 
_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                   8QM5 
_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             2.05 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.11 
_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            277 
# 
_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                                       8QM5 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.889 
_reflns.d_resolution_low                               38.72 
_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                                     32579 
_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                           98.5 
_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                          14.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.05 
_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                                    1.89 
_reflns_shell.d_res_low                                     1.90 
_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                             641 
_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                               0.68 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -8.45890 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -2.60980 
_refine.aniso_B[2][2]                            3.22530 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            5.23370 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               45.967 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.950 
_refine.correlation_coeff_Fo_to_Fc_free          0.948 
_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                                 8QM5 
_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                            1.889 
_refine.ls_d_res_low                             38.72 
_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                     32050 
_refine.ls_number_reflns_R_free                  1584 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.4 
_refine.ls_percent_reflns_R_free                 4.940 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1956 
_refine.ls_R_factor_R_free                       0.2197 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1943 
_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   0.139 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.138 
_refine.pdbx_overall_SU_R_Blow_DPI               0.165 
_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             0.331 
_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                        8QM5 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.23 
_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                       1.889 
_refine_hist.d_res_low                        38.72 
_refine_hist.number_atoms_solvent             191 
_refine_hist.number_atoms_total               3558 
_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        3327 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         40 
_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 ? 6796  ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 1.04  ? 12218 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1495  ? 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' ? ?     ? 1091  ? t_gen_planes              16.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 6796  ? t_it                      10.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 6.76  ? ?     ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 15.75 ? ?     ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 426   ? 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' ? ?     ? 5038  ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.89 
_refine_ls_shell.d_res_low                        1.90 
_refine_ls_shell.number_reflns_all                641 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             ? 
_refine_ls_shell.number_reflns_R_work             595 
_refine_ls_shell.percent_reflns_obs               99.69 
_refine_ls_shell.percent_reflns_R_free            7.18 
_refine_ls_shell.R_factor_all                     0.2906 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2895 
_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                  0.3062 
# 
_struct.entry_id                     8QM5 
_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        8QM5 
_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 2 ? 
F N N 4 ? 
G N N 4 ? 
# 
_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 8QM5 A 34 ? 215 ? P06730 36 ? 217 ? 36 217 
2 1 8QM5 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 8QM5 MET A 1   ? UNP P06730 ?   ?   'initiating methionine' 3   1  
1 8QM5 HIS A 2   ? UNP P06730 ?   ?   'expression tag'        4   2  
1 8QM5 HIS A 3   ? UNP P06730 ?   ?   'expression tag'        5   3  
1 8QM5 HIS A 4   ? UNP P06730 ?   ?   'expression tag'        6   4  
1 8QM5 HIS A 5   ? UNP P06730 ?   ?   'expression tag'        7   5  
1 8QM5 HIS A 6   ? UNP P06730 ?   ?   'expression tag'        8   6  
1 8QM5 HIS A 7   ? UNP P06730 ?   ?   'expression tag'        9   7  
1 8QM5 GLY A 8   ? UNP P06730 ?   ?   'expression tag'        10  8  
1 8QM5 ALA A 9   ? UNP P06730 ?   ?   'expression tag'        11  9  
1 8QM5 ARG A 10  ? UNP P06730 ?   ?   'expression tag'        12  10 
1 8QM5 ILE A 11  ? UNP P06730 ?   ?   'expression tag'        13  11 
1 8QM5 ILE A 12  ? UNP P06730 ?   ?   'expression tag'        14  12 
1 8QM5 TYR A 13  ? UNP P06730 ?   ?   'expression tag'        15  13 
1 8QM5 ASP A 14  ? UNP P06730 ?   ?   'expression tag'        16  14 
1 8QM5 ARG A 15  ? UNP P06730 ?   ?   'expression tag'        17  15 
1 8QM5 ALA A 16  ? UNP P06730 ?   ?   'expression tag'        18  16 
1 8QM5 PHE A 17  ? UNP P06730 ?   ?   'expression tag'        19  17 
1 8QM5 LEU A 18  ? UNP P06730 ?   ?   'expression tag'        20  18 
1 8QM5 MET A 19  ? UNP P06730 ?   ?   'expression tag'        21  19 
1 8QM5 ALA A 20  ? UNP P06730 ?   ?   'expression tag'        22  20 
1 8QM5 CYS A 21  ? UNP P06730 ?   ?   'expression tag'        23  21 
1 8QM5 ARG A 22  ? UNP P06730 ?   ?   'expression tag'        24  22 
1 8QM5 GLY A 23  ? UNP P06730 ?   ?   'expression tag'        25  23 
1 8QM5 GLY A 24  ? UNP P06730 ?   ?   'expression tag'        26  24 
1 8QM5 GLY A 25  ? UNP P06730 ?   ?   'expression tag'        27  25 
1 8QM5 GLY A 26  ? UNP P06730 ?   ?   'expression tag'        28  26 
1 8QM5 GLU A 27  ? UNP P06730 ?   ?   'expression tag'        29  27 
1 8QM5 ASN A 28  ? UNP P06730 ?   ?   'expression tag'        30  28 
1 8QM5 LEU A 29  ? UNP P06730 ?   ?   'expression tag'        31  29 
1 8QM5 TYR A 30  ? UNP P06730 ?   ?   'expression tag'        32  30 
1 8QM5 PHE A 31  ? UNP P06730 ?   ?   'expression tag'        33  31 
1 8QM5 GLN A 32  ? UNP P06730 ?   ?   'expression tag'        34  32 
1 8QM5 GLY A 33  ? UNP P06730 ?   ?   'expression tag'        35  33 
1 8QM5 ASN A 125 ? UNP P06730 ASP 127 conflict                127 34 
2 8QM5 MET B 1   ? UNP P06730 ?   ?   'initiating methionine' 3   35 
2 8QM5 HIS B 2   ? UNP P06730 ?   ?   'expression tag'        4   36 
2 8QM5 HIS B 3   ? UNP P06730 ?   ?   'expression tag'        5   37 
2 8QM5 HIS B 4   ? UNP P06730 ?   ?   'expression tag'        6   38 
2 8QM5 HIS B 5   ? UNP P06730 ?   ?   'expression tag'        7   39 
2 8QM5 HIS B 6   ? UNP P06730 ?   ?   'expression tag'        8   40 
2 8QM5 HIS B 7   ? UNP P06730 ?   ?   'expression tag'        9   41 
2 8QM5 GLY B 8   ? UNP P06730 ?   ?   'expression tag'        10  42 
2 8QM5 ALA B 9   ? UNP P06730 ?   ?   'expression tag'        11  43 
2 8QM5 ARG B 10  ? UNP P06730 ?   ?   'expression tag'        12  44 
2 8QM5 ILE B 11  ? UNP P06730 ?   ?   'expression tag'        13  45 
2 8QM5 ILE B 12  ? UNP P06730 ?   ?   'expression tag'        14  46 
2 8QM5 TYR B 13  ? UNP P06730 ?   ?   'expression tag'        15  47 
2 8QM5 ASP B 14  ? UNP P06730 ?   ?   'expression tag'        16  48 
2 8QM5 ARG B 15  ? UNP P06730 ?   ?   'expression tag'        17  49 
2 8QM5 ALA B 16  ? UNP P06730 ?   ?   'expression tag'        18  50 
2 8QM5 PHE B 17  ? UNP P06730 ?   ?   'expression tag'        19  51 
2 8QM5 LEU B 18  ? UNP P06730 ?   ?   'expression tag'        20  52 
2 8QM5 MET B 19  ? UNP P06730 ?   ?   'expression tag'        21  53 
2 8QM5 ALA B 20  ? UNP P06730 ?   ?   'expression tag'        22  54 
2 8QM5 CYS B 21  ? UNP P06730 ?   ?   'expression tag'        23  55 
2 8QM5 ARG B 22  ? UNP P06730 ?   ?   'expression tag'        24  56 
2 8QM5 GLY B 23  ? UNP P06730 ?   ?   'expression tag'        25  57 
2 8QM5 GLY B 24  ? UNP P06730 ?   ?   'expression tag'        26  58 
2 8QM5 GLY B 25  ? UNP P06730 ?   ?   'expression tag'        27  59 
2 8QM5 GLY B 26  ? UNP P06730 ?   ?   'expression tag'        28  60 
2 8QM5 GLU B 27  ? UNP P06730 ?   ?   'expression tag'        29  61 
2 8QM5 ASN B 28  ? UNP P06730 ?   ?   'expression tag'        30  62 
2 8QM5 LEU B 29  ? UNP P06730 ?   ?   'expression tag'        31  63 
2 8QM5 TYR B 30  ? UNP P06730 ?   ?   'expression tag'        32  64 
2 8QM5 PHE B 31  ? UNP P06730 ?   ?   'expression tag'        33  65 
2 8QM5 GLN B 32  ? UNP P06730 ?   ?   'expression tag'        34  66 
2 8QM5 GLY B 33  ? UNP P06730 ?   ?   'expression tag'        35  67 
2 8QM5 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)' 1830  ? 
1 MORE         8     ? 
1 'SSA (A^2)'  20730 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'mass spectrometry' 
_pdbx_struct_assembly_auth_evidence.details                'Mass spec gives the molecular weight for the monomer' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 14  ? CYS A 21  ? ASP A 16  CYS A 23  1 ? 8  
HELX_P HELX_P2  AA2 ASN A 28  ? GLN A 32  ? ASN A 30  GLN A 34  5 ? 5  
HELX_P HELX_P3  AA3 THR A 53  ? ASN A 57  ? THR A 55  ASN A 59  1 ? 5  
HELX_P HELX_P4  AA4 VAL A 67  ? SER A 80  ? VAL A 69  SER A 82  1 ? 14 
HELX_P HELX_P5  AA5 GLN A 118 ? ASP A 123 ? GLN A 120 ASP A 125 1 ? 6  
HELX_P HELX_P6  AA6 ASP A 123 ? GLY A 137 ? ASP A 125 GLY A 139 1 ? 15 
HELX_P HELX_P7  AA7 PHE A 140 ? ASP A 145 ? PHE A 142 ASP A 147 5 ? 6  
HELX_P HELX_P8  AA8 ASN A 170 ? GLY A 186 ? ASN A 172 GLY A 188 1 ? 17 
HELX_P HELX_P9  AA9 HIS A 198 ? THR A 203 ? HIS A 200 THR A 205 1 ? 6  
HELX_P HELX_P10 AB1 ASP B 14  ? CYS B 21  ? ASP B 16  CYS B 23  1 ? 8  
HELX_P HELX_P11 AB2 TRP B 54  ? ALA B 56  ? TRP B 56  ALA B 58  5 ? 3  
HELX_P HELX_P12 AB3 VAL B 67  ? SER B 81  ? VAL B 69  SER B 83  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 82  ? MET B 84  ? ASN B 84  MET B 86  5 ? 3  
HELX_P HELX_P14 AB5 LYS B 117 ? GLY B 137 ? LYS B 119 GLY B 139 1 ? 21 
HELX_P HELX_P15 AB6 PHE B 140 ? ASP B 145 ? PHE B 142 ASP B 147 5 ? 6  
HELX_P HELX_P16 AB7 ASN B 170 ? GLY B 186 ? ASN B 172 GLY B 188 1 ? 17 
HELX_P HELX_P17 AB8 HIS B 198 ? THR B 203 ? HIS B 200 THR B 205 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 58  ? THR A 66  ? LEU A 60  THR A 68  
AA1 2 PRO A 36  ? PHE A 46  ? PRO A 38  PHE A 48  
AA1 3 ASP A 88  ? LYS A 93  ? ASP A 90  LYS A 95  
AA1 4 VAL A 147 ? ASN A 153 ? VAL A 149 ASN A 155 
AA1 5 LYS A 160 ? THR A 165 ? LYS A 162 THR A 167 
AA1 6 GLY A 109 ? THR A 114 ? GLY A 111 THR A 116 
AA1 7 GLY A 194 ? SER A 197 ? GLY A 196 SER A 199 
AA1 8 PHE A 213 ? VAL A 214 ? PHE A 215 VAL A 216 
AA2 1 LEU B 58  ? THR B 66  ? LEU B 60  THR B 68  
AA2 2 PRO B 36  ? 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 GLY B 158 ? THR B 165 ? GLY B 160 THR B 167 
AA2 6 GLY B 109 ? ASN B 116 ? GLY B 111 ASN B 118 
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 GLY A 149 ? N GLY A 151 O TRP A 164 ? O TRP A 166 
AA1 5 6 O ILE A 161 ? O ILE A 163 N ILE A 113 ? N ILE A 115 
AA1 6 7 N ARG A 110 ? N ARG A 112 O GLN A 196 ? O GLN A 198 
AA1 7 8 N TYR A 195 ? N TYR A 197 O PHE A 213 ? O PHE A 215 
AA2 1 2 O SER B 62  ? O SER B 64  N LEU B 43  ? N LEU B 45  
AA2 2 3 N TRP B 44  ? N TRP B 46  O SER B 90  ? O SER B 92  
AA2 3 4 N LYS B 93  ? N LYS B 95  O CYS B 148 ? O CYS B 150 
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                   8QM5 
_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 ASN A 50  ? ? -90.08  50.94   
2 1 ASP A 67  ? ? -144.42 20.09   
3 1 LYS A 119 ? ? -29.28  -50.66  
4 1 ASP A 143 ? ? 54.14   -129.53 
5 1 ASP B 67  ? ? -143.24 26.73   
6 1 CYS B 89  ? ? -140.59 27.05   
7 1 LYS B 119 ? ? 17.47   -69.32  
8 1 ASP B 143 ? ? 60.45   -142.22 
# 
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 20.7378 -13.6616 4.5713  -0.0182 ? -0.0119 ? 0.0284 ? -0.0358 ? -0.0066 ? 0.0087  ? 1.5400 ? 
0.0447  ? 0.3033  ? 0.8848 ? -0.7409 ? 1.0651 ? 0.0267  ? -0.0746 ? 0.1560  ? 0.0112 ? -0.0534 ? -0.1187 ? 0.0623  ? -0.0824 ? 
0.0267 ? 
2 'X-RAY DIFFRACTION' ? refined 1.5714  -21.6371 31.7680 0.0849  ? 0.0072  ? 0.0886 ? -0.0482 ? 0.0166  ? -0.0598 ? 0.8240 ? 
-0.0153 ? -0.2355 ? 0.3504 ? 0.0287  ? 1.4013 ? -0.0809 ? -0.0249 ? -0.1087 ? 0.0648 ? 0.0003  ? 0.1092  ? -0.0258 ? 0.0714  ? 
0.0806 ? 
# 
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 B MET 3  ? B MET 1  
10 1 Y 1 B HIS 4  ? B HIS 2  
11 1 Y 1 B HIS 5  ? B HIS 3  
12 1 Y 1 B HIS 6  ? B HIS 4  
13 1 Y 1 B HIS 7  ? B HIS 5  
14 1 Y 1 B HIS 8  ? B HIS 6  
15 1 Y 1 B GLY 26 ? B GLY 24 
16 1 Y 1 B GLY 27 ? B GLY 25 
17 1 Y 1 B GLY 28 ? B GLY 26 
18 1 Y 1 B GLU 29 ? B GLU 27 
19 1 Y 1 B ASN 30 ? B ASN 28 
20 1 Y 1 B LEU 31 ? B LEU 29 
21 1 Y 1 B TYR 32 ? B TYR 30 
22 1 Y 1 B PHE 33 ? B PHE 31 
23 1 Y 1 B GLN 34 ? B GLN 32 
# 
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  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HIS N    N  N N 137 
HIS CA   C  N S 138 
HIS C    C  N N 139 
HIS O    O  N N 140 
HIS CB   C  N N 141 
HIS CG   C  Y N 142 
HIS ND1  N  Y N 143 
HIS CD2  C  Y N 144 
HIS CE1  C  Y N 145 
HIS NE2  N  Y N 146 
HIS OXT  O  N N 147 
HIS H    H  N N 148 
HIS H2   H  N N 149 
HIS HA   H  N N 150 
HIS HB2  H  N N 151 
HIS HB3  H  N N 152 
HIS HD1  H  N N 153 
HIS HD2  H  N N 154 
HIS HE1  H  N N 155 
HIS HE2  H  N N 156 
HIS HXT  H  N N 157 
HOH O    O  N N 158 
HOH H1   H  N N 159 
HOH H2   H  N N 160 
ILE N    N  N N 161 
ILE CA   C  N S 162 
ILE C    C  N N 163 
ILE O    O  N N 164 
ILE CB   C  N S 165 
ILE CG1  C  N N 166 
ILE CG2  C  N N 167 
ILE CD1  C  N N 168 
ILE OXT  O  N N 169 
ILE H    H  N N 170 
ILE H2   H  N N 171 
ILE HA   H  N N 172 
ILE HB   H  N N 173 
ILE HG12 H  N N 174 
ILE HG13 H  N N 175 
ILE HG21 H  N N 176 
ILE HG22 H  N N 177 
ILE HG23 H  N N 178 
ILE HD11 H  N N 179 
ILE HD12 H  N N 180 
ILE HD13 H  N N 181 
ILE HXT  H  N N 182 
LEU N    N  N N 183 
LEU CA   C  N S 184 
LEU C    C  N N 185 
LEU O    O  N N 186 
LEU CB   C  N N 187 
LEU CG   C  N N 188 
LEU CD1  C  N N 189 
LEU CD2  C  N N 190 
LEU OXT  O  N N 191 
LEU H    H  N N 192 
LEU H2   H  N N 193 
LEU HA   H  N N 194 
LEU HB2  H  N N 195 
LEU HB3  H  N N 196 
LEU HG   H  N N 197 
LEU HD11 H  N N 198 
LEU HD12 H  N N 199 
LEU HD13 H  N N 200 
LEU HD21 H  N N 201 
LEU HD22 H  N N 202 
LEU HD23 H  N N 203 
LEU HXT  H  N N 204 
LYS N    N  N N 205 
LYS CA   C  N S 206 
LYS C    C  N N 207 
LYS O    O  N N 208 
LYS CB   C  N N 209 
LYS CG   C  N N 210 
LYS CD   C  N N 211 
LYS CE   C  N N 212 
LYS NZ   N  N N 213 
LYS OXT  O  N N 214 
LYS H    H  N N 215 
LYS H2   H  N N 216 
LYS HA   H  N N 217 
LYS HB2  H  N N 218 
LYS HB3  H  N N 219 
LYS HG2  H  N N 220 
LYS HG3  H  N N 221 
LYS HD2  H  N N 222 
LYS HD3  H  N N 223 
LYS HE2  H  N N 224 
LYS HE3  H  N N 225 
LYS HZ1  H  N N 226 
LYS HZ2  H  N N 227 
LYS HZ3  H  N N 228 
LYS HXT  H  N N 229 
MET N    N  N N 230 
MET CA   C  N S 231 
MET C    C  N N 232 
MET O    O  N N 233 
MET CB   C  N N 234 
MET CG   C  N N 235 
MET SD   S  N N 236 
MET CE   C  N N 237 
MET OXT  O  N N 238 
MET H    H  N N 239 
MET H2   H  N N 240 
MET HA   H  N N 241 
MET HB2  H  N N 242 
MET HB3  H  N N 243 
MET HG2  H  N N 244 
MET HG3  H  N N 245 
MET HE1  H  N N 246 
MET HE2  H  N N 247 
MET HE3  H  N N 248 
MET HXT  H  N N 249 
PGE C1   C  N N 250 
PGE O1   O  N N 251 
PGE C2   C  N N 252 
PGE O2   O  N N 253 
PGE C3   C  N N 254 
PGE C4   C  N N 255 
PGE O4   O  N N 256 
PGE C6   C  N N 257 
PGE C5   C  N N 258 
PGE O3   O  N N 259 
PGE H1   H  N N 260 
PGE H12  H  N N 261 
PGE HO1  H  N N 262 
PGE H2   H  N N 263 
PGE H22  H  N N 264 
PGE H3   H  N N 265 
PGE H32  H  N N 266 
PGE H4   H  N N 267 
PGE H42  H  N N 268 
PGE HO4  H  N N 269 
PGE H6   H  N N 270 
PGE H62  H  N N 271 
PGE H5   H  N N 272 
PGE H52  H  N N 273 
PHE N    N  N N 274 
PHE CA   C  N S 275 
PHE C    C  N N 276 
PHE O    O  N N 277 
PHE CB   C  N N 278 
PHE CG   C  Y N 279 
PHE CD1  C  Y N 280 
PHE CD2  C  Y N 281 
PHE CE1  C  Y N 282 
PHE CE2  C  Y N 283 
PHE CZ   C  Y N 284 
PHE OXT  O  N N 285 
PHE H    H  N N 286 
PHE H2   H  N N 287 
PHE HA   H  N N 288 
PHE HB2  H  N N 289 
PHE HB3  H  N N 290 
PHE HD1  H  N N 291 
PHE HD2  H  N N 292 
PHE HE1  H  N N 293 
PHE HE2  H  N N 294 
PHE HZ   H  N N 295 
PHE HXT  H  N N 296 
PRO N    N  N N 297 
PRO CA   C  N S 298 
PRO C    C  N N 299 
PRO O    O  N N 300 
PRO CB   C  N N 301 
PRO CG   C  N N 302 
PRO CD   C  N N 303 
PRO OXT  O  N N 304 
PRO H    H  N N 305 
PRO HA   H  N N 306 
PRO HB2  H  N N 307 
PRO HB3  H  N N 308 
PRO HG2  H  N N 309 
PRO HG3  H  N N 310 
PRO HD2  H  N N 311 
PRO HD3  H  N N 312 
PRO HXT  H  N N 313 
SER N    N  N N 314 
SER CA   C  N S 315 
SER C    C  N N 316 
SER O    O  N N 317 
SER CB   C  N N 318 
SER OG   O  N N 319 
SER OXT  O  N N 320 
SER H    H  N N 321 
SER H2   H  N N 322 
SER HA   H  N N 323 
SER HB2  H  N N 324 
SER HB3  H  N N 325 
SER HG   H  N N 326 
SER HXT  H  N N 327 
THR N    N  N N 328 
THR CA   C  N S 329 
THR C    C  N N 330 
THR O    O  N N 331 
THR CB   C  N R 332 
THR OG1  O  N N 333 
THR CG2  C  N N 334 
THR OXT  O  N N 335 
THR H    H  N N 336 
THR H2   H  N N 337 
THR HA   H  N N 338 
THR HB   H  N N 339 
THR HG1  H  N N 340 
THR HG21 H  N N 341 
THR HG22 H  N N 342 
THR HG23 H  N N 343 
THR HXT  H  N N 344 
TRP N    N  N N 345 
TRP CA   C  N S 346 
TRP C    C  N N 347 
TRP O    O  N N 348 
TRP CB   C  N N 349 
TRP CG   C  Y N 350 
TRP CD1  C  Y N 351 
TRP CD2  C  Y N 352 
TRP NE1  N  Y N 353 
TRP CE2  C  Y N 354 
TRP CE3  C  Y N 355 
TRP CZ2  C  Y N 356 
TRP CZ3  C  Y N 357 
TRP CH2  C  Y N 358 
TRP OXT  O  N N 359 
TRP H    H  N N 360 
TRP H2   H  N N 361 
TRP HA   H  N N 362 
TRP HB2  H  N N 363 
TRP HB3  H  N N 364 
TRP HD1  H  N N 365 
TRP HE1  H  N N 366 
TRP HE3  H  N N 367 
TRP HZ2  H  N N 368 
TRP HZ3  H  N N 369 
TRP HH2  H  N N 370 
TRP HXT  H  N N 371 
TYR N    N  N N 372 
TYR CA   C  N S 373 
TYR C    C  N N 374 
TYR O    O  N N 375 
TYR CB   C  N N 376 
TYR CG   C  Y N 377 
TYR CD1  C  Y N 378 
TYR CD2  C  Y N 379 
TYR CE1  C  Y N 380 
TYR CE2  C  Y N 381 
TYR CZ   C  Y N 382 
TYR OH   O  N N 383 
TYR OXT  O  N N 384 
TYR H    H  N N 385 
TYR H2   H  N N 386 
TYR HA   H  N N 387 
TYR HB2  H  N N 388 
TYR HB3  H  N N 389 
TYR HD1  H  N N 390 
TYR HD2  H  N N 391 
TYR HE1  H  N N 392 
TYR HE2  H  N N 393 
TYR HH   H  N N 394 
TYR HXT  H  N N 395 
VAL N    N  N N 396 
VAL CA   C  N S 397 
VAL C    C  N N 398 
VAL O    O  N N 399 
VAL CB   C  N N 400 
VAL CG1  C  N N 401 
VAL CG2  C  N N 402 
VAL OXT  O  N N 403 
VAL H    H  N N 404 
VAL H2   H  N N 405 
VAL HA   H  N N 406 
VAL HB   H  N N 407 
VAL HG11 H  N N 408 
VAL HG12 H  N N 409 
VAL HG13 H  N N 410 
VAL HG21 H  N N 411 
VAL HG22 H  N N 412 
VAL HG23 H  N N 413 
VAL HXT  H  N N 414 
W4U C2   C  N N 415 
W4U C5   C  N N 416 
W4U C6   C  N N 417 
W4U C7   C  N N 418 
W4U C8   C  N N 419 
W4U C10  C  Y N 420 
W4U C11  C  Y N 421 
W4U C12  C  Y N 422 
W4U C14  C  Y N 423 
W4U C15  C  Y N 424 
W4U O1   O  N N 425 
W4U O3   O  N N 426 
W4U C4   C  N N 427 
W4U C9   C  Y N 428 
W4U CL13 CL N N 429 
W4U H16  H  N N 430 
W4U H17  H  N N 431 
W4U H19  H  N N 432 
W4U H18  H  N N 433 
W4U H21  H  N N 434 
W4U H20  H  N N 435 
W4U H22  H  N N 436 
W4U H23  H  N N 437 
W4U H24  H  N N 438 
W4U H25  H  N N 439 
W4U H26  H  N N 440 
W4U H27  H  N N 441 
W4U H1   H  N N 442 
# 
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  
GLN N    CA   sing N N 83  
GLN N    H    sing N N 84  
GLN N    H2   sing N N 85  
GLN CA   C    sing N N 86  
GLN CA   CB   sing N N 87  
GLN CA   HA   sing N N 88  
GLN C    O    doub N N 89  
GLN C    OXT  sing N N 90  
GLN CB   CG   sing N N 91  
GLN CB   HB2  sing N N 92  
GLN CB   HB3  sing N N 93  
GLN CG   CD   sing N N 94  
GLN CG   HG2  sing N N 95  
GLN CG   HG3  sing N N 96  
GLN CD   OE1  doub N N 97  
GLN CD   NE2  sing N N 98  
GLN NE2  HE21 sing N N 99  
GLN NE2  HE22 sing N N 100 
GLN OXT  HXT  sing N N 101 
GLU N    CA   sing N N 102 
GLU N    H    sing N N 103 
GLU N    H2   sing N N 104 
GLU CA   C    sing N N 105 
GLU CA   CB   sing N N 106 
GLU CA   HA   sing N N 107 
GLU C    O    doub N N 108 
GLU C    OXT  sing N N 109 
GLU CB   CG   sing N N 110 
GLU CB   HB2  sing N N 111 
GLU CB   HB3  sing N N 112 
GLU CG   CD   sing N N 113 
GLU CG   HG2  sing N N 114 
GLU CG   HG3  sing N N 115 
GLU CD   OE1  doub N N 116 
GLU CD   OE2  sing N N 117 
GLU OE2  HE2  sing N N 118 
GLU OXT  HXT  sing N N 119 
GLY N    CA   sing N N 120 
GLY N    H    sing N N 121 
GLY N    H2   sing N N 122 
GLY CA   C    sing N N 123 
GLY CA   HA2  sing N N 124 
GLY CA   HA3  sing N N 125 
GLY C    O    doub N N 126 
GLY C    OXT  sing N N 127 
GLY OXT  HXT  sing N N 128 
HIS N    CA   sing N N 129 
HIS N    H    sing N N 130 
HIS N    H2   sing N N 131 
HIS CA   C    sing N N 132 
HIS CA   CB   sing N N 133 
HIS CA   HA   sing N N 134 
HIS C    O    doub N N 135 
HIS C    OXT  sing N N 136 
HIS CB   CG   sing N N 137 
HIS CB   HB2  sing N N 138 
HIS CB   HB3  sing N N 139 
HIS CG   ND1  sing Y N 140 
HIS CG   CD2  doub Y N 141 
HIS ND1  CE1  doub Y N 142 
HIS ND1  HD1  sing N N 143 
HIS CD2  NE2  sing Y N 144 
HIS CD2  HD2  sing N N 145 
HIS CE1  NE2  sing Y N 146 
HIS CE1  HE1  sing N N 147 
HIS NE2  HE2  sing N N 148 
HIS OXT  HXT  sing N N 149 
HOH O    H1   sing N N 150 
HOH O    H2   sing N N 151 
ILE N    CA   sing N N 152 
ILE N    H    sing N N 153 
ILE N    H2   sing N N 154 
ILE CA   C    sing N N 155 
ILE CA   CB   sing N N 156 
ILE CA   HA   sing N N 157 
ILE C    O    doub N N 158 
ILE C    OXT  sing N N 159 
ILE CB   CG1  sing N N 160 
ILE CB   CG2  sing N N 161 
ILE CB   HB   sing N N 162 
ILE CG1  CD1  sing N N 163 
ILE CG1  HG12 sing N N 164 
ILE CG1  HG13 sing N N 165 
ILE CG2  HG21 sing N N 166 
ILE CG2  HG22 sing N N 167 
ILE CG2  HG23 sing N N 168 
ILE CD1  HD11 sing N N 169 
ILE CD1  HD12 sing N N 170 
ILE CD1  HD13 sing N N 171 
ILE OXT  HXT  sing N N 172 
LEU N    CA   sing N N 173 
LEU N    H    sing N N 174 
LEU N    H2   sing N N 175 
LEU CA   C    sing N N 176 
LEU CA   CB   sing N N 177 
LEU CA   HA   sing N N 178 
LEU C    O    doub N N 179 
LEU C    OXT  sing N N 180 
LEU CB   CG   sing N N 181 
LEU CB   HB2  sing N N 182 
LEU CB   HB3  sing N N 183 
LEU CG   CD1  sing N N 184 
LEU CG   CD2  sing N N 185 
LEU CG   HG   sing N N 186 
LEU CD1  HD11 sing N N 187 
LEU CD1  HD12 sing N N 188 
LEU CD1  HD13 sing N N 189 
LEU CD2  HD21 sing N N 190 
LEU CD2  HD22 sing N N 191 
LEU CD2  HD23 sing N N 192 
LEU OXT  HXT  sing N N 193 
LYS N    CA   sing N N 194 
LYS N    H    sing N N 195 
LYS N    H2   sing N N 196 
LYS CA   C    sing N N 197 
LYS CA   CB   sing N N 198 
LYS CA   HA   sing N N 199 
LYS C    O    doub N N 200 
LYS C    OXT  sing N N 201 
LYS CB   CG   sing N N 202 
LYS CB   HB2  sing N N 203 
LYS CB   HB3  sing N N 204 
LYS CG   CD   sing N N 205 
LYS CG   HG2  sing N N 206 
LYS CG   HG3  sing N N 207 
LYS CD   CE   sing N N 208 
LYS CD   HD2  sing N N 209 
LYS CD   HD3  sing N N 210 
LYS CE   NZ   sing N N 211 
LYS CE   HE2  sing N N 212 
LYS CE   HE3  sing N N 213 
LYS NZ   HZ1  sing N N 214 
LYS NZ   HZ2  sing N N 215 
LYS NZ   HZ3  sing N N 216 
LYS OXT  HXT  sing N N 217 
MET N    CA   sing N N 218 
MET N    H    sing N N 219 
MET N    H2   sing N N 220 
MET CA   C    sing N N 221 
MET CA   CB   sing N N 222 
MET CA   HA   sing N N 223 
MET C    O    doub N N 224 
MET C    OXT  sing N N 225 
MET CB   CG   sing N N 226 
MET CB   HB2  sing N N 227 
MET CB   HB3  sing N N 228 
MET CG   SD   sing N N 229 
MET CG   HG2  sing N N 230 
MET CG   HG3  sing N N 231 
MET SD   CE   sing N N 232 
MET CE   HE1  sing N N 233 
MET CE   HE2  sing N N 234 
MET CE   HE3  sing N N 235 
MET OXT  HXT  sing N N 236 
PGE C1   O1   sing N N 237 
PGE C1   C2   sing N N 238 
PGE C1   H1   sing N N 239 
PGE C1   H12  sing N N 240 
PGE O1   HO1  sing N N 241 
PGE C2   O2   sing N N 242 
PGE C2   H2   sing N N 243 
PGE C2   H22  sing N N 244 
PGE O2   C3   sing N N 245 
PGE C3   C4   sing N N 246 
PGE C3   H3   sing N N 247 
PGE C3   H32  sing N N 248 
PGE C4   O3   sing N N 249 
PGE C4   H4   sing N N 250 
PGE C4   H42  sing N N 251 
PGE O4   C6   sing N N 252 
PGE O4   HO4  sing N N 253 
PGE C6   C5   sing N N 254 
PGE C6   H6   sing N N 255 
PGE C6   H62  sing N N 256 
PGE C5   O3   sing N N 257 
PGE C5   H5   sing N N 258 
PGE C5   H52  sing N N 259 
PHE N    CA   sing N N 260 
PHE N    H    sing N N 261 
PHE N    H2   sing N N 262 
PHE CA   C    sing N N 263 
PHE CA   CB   sing N N 264 
PHE CA   HA   sing N N 265 
PHE C    O    doub N N 266 
PHE C    OXT  sing N N 267 
PHE CB   CG   sing N N 268 
PHE CB   HB2  sing N N 269 
PHE CB   HB3  sing N N 270 
PHE CG   CD1  doub Y N 271 
PHE CG   CD2  sing Y N 272 
PHE CD1  CE1  sing Y N 273 
PHE CD1  HD1  sing N N 274 
PHE CD2  CE2  doub Y N 275 
PHE CD2  HD2  sing N N 276 
PHE CE1  CZ   doub Y N 277 
PHE CE1  HE1  sing N N 278 
PHE CE2  CZ   sing Y N 279 
PHE CE2  HE2  sing N N 280 
PHE CZ   HZ   sing N N 281 
PHE OXT  HXT  sing N N 282 
PRO N    CA   sing N N 283 
PRO N    CD   sing N N 284 
PRO N    H    sing N N 285 
PRO CA   C    sing N N 286 
PRO CA   CB   sing N N 287 
PRO CA   HA   sing N N 288 
PRO C    O    doub N N 289 
PRO C    OXT  sing N N 290 
PRO CB   CG   sing N N 291 
PRO CB   HB2  sing N N 292 
PRO CB   HB3  sing N N 293 
PRO CG   CD   sing N N 294 
PRO CG   HG2  sing N N 295 
PRO CG   HG3  sing N N 296 
PRO CD   HD2  sing N N 297 
PRO CD   HD3  sing N N 298 
PRO OXT  HXT  sing N N 299 
SER N    CA   sing N N 300 
SER N    H    sing N N 301 
SER N    H2   sing N N 302 
SER CA   C    sing N N 303 
SER CA   CB   sing N N 304 
SER CA   HA   sing N N 305 
SER C    O    doub N N 306 
SER C    OXT  sing N N 307 
SER CB   OG   sing N N 308 
SER CB   HB2  sing N N 309 
SER CB   HB3  sing N N 310 
SER OG   HG   sing N N 311 
SER OXT  HXT  sing N N 312 
THR N    CA   sing N N 313 
THR N    H    sing N N 314 
THR N    H2   sing N N 315 
THR CA   C    sing N N 316 
THR CA   CB   sing N N 317 
THR CA   HA   sing N N 318 
THR C    O    doub N N 319 
THR C    OXT  sing N N 320 
THR CB   OG1  sing N N 321 
THR CB   CG2  sing N N 322 
THR CB   HB   sing N N 323 
THR OG1  HG1  sing N N 324 
THR CG2  HG21 sing N N 325 
THR CG2  HG22 sing N N 326 
THR CG2  HG23 sing N N 327 
THR OXT  HXT  sing N N 328 
TRP N    CA   sing N N 329 
TRP N    H    sing N N 330 
TRP N    H2   sing N N 331 
TRP CA   C    sing N N 332 
TRP CA   CB   sing N N 333 
TRP CA   HA   sing N N 334 
TRP C    O    doub N N 335 
TRP C    OXT  sing N N 336 
TRP CB   CG   sing N N 337 
TRP CB   HB2  sing N N 338 
TRP CB   HB3  sing N N 339 
TRP CG   CD1  doub Y N 340 
TRP CG   CD2  sing Y N 341 
TRP CD1  NE1  sing Y N 342 
TRP CD1  HD1  sing N N 343 
TRP CD2  CE2  doub Y N 344 
TRP CD2  CE3  sing Y N 345 
TRP NE1  CE2  sing Y N 346 
TRP NE1  HE1  sing N N 347 
TRP CE2  CZ2  sing Y N 348 
TRP CE3  CZ3  doub Y N 349 
TRP CE3  HE3  sing N N 350 
TRP CZ2  CH2  doub Y N 351 
TRP CZ2  HZ2  sing N N 352 
TRP CZ3  CH2  sing Y N 353 
TRP CZ3  HZ3  sing N N 354 
TRP CH2  HH2  sing N N 355 
TRP OXT  HXT  sing N N 356 
TYR N    CA   sing N N 357 
TYR N    H    sing N N 358 
TYR N    H2   sing N N 359 
TYR CA   C    sing N N 360 
TYR CA   CB   sing N N 361 
TYR CA   HA   sing N N 362 
TYR C    O    doub N N 363 
TYR C    OXT  sing N N 364 
TYR CB   CG   sing N N 365 
TYR CB   HB2  sing N N 366 
TYR CB   HB3  sing N N 367 
TYR CG   CD1  doub Y N 368 
TYR CG   CD2  sing Y N 369 
TYR CD1  CE1  sing Y N 370 
TYR CD1  HD1  sing N N 371 
TYR CD2  CE2  doub Y N 372 
TYR CD2  HD2  sing N N 373 
TYR CE1  CZ   doub Y N 374 
TYR CE1  HE1  sing N N 375 
TYR CE2  CZ   sing Y N 376 
TYR CE2  HE2  sing N N 377 
TYR CZ   OH   sing N N 378 
TYR OH   HH   sing N N 379 
TYR OXT  HXT  sing N N 380 
VAL N    CA   sing N N 381 
VAL N    H    sing N N 382 
VAL N    H2   sing N N 383 
VAL CA   C    sing N N 384 
VAL CA   CB   sing N N 385 
VAL CA   HA   sing N N 386 
VAL C    O    doub N N 387 
VAL C    OXT  sing N N 388 
VAL CB   CG1  sing N N 389 
VAL CB   CG2  sing N N 390 
VAL CB   HB   sing N N 391 
VAL CG1  HG11 sing N N 392 
VAL CG1  HG12 sing N N 393 
VAL CG1  HG13 sing N N 394 
VAL CG2  HG21 sing N N 395 
VAL CG2  HG22 sing N N 396 
VAL CG2  HG23 sing N N 397 
VAL OXT  HXT  sing N N 398 
W4U C6   C5   sing N N 399 
W4U C6   C7   sing N N 400 
W4U C5   C4   sing N N 401 
W4U C14  C15  doub Y N 402 
W4U C14  C12  sing Y N 403 
W4U C15  C9   sing Y N 404 
W4U CL13 C12  sing N N 405 
W4U C12  C11  doub Y N 406 
W4U C9   C4   sing N N 407 
W4U C9   C10  doub Y N 408 
W4U O3   C2   doub N N 409 
W4U C7   C8   sing N N 410 
W4U C4   C2   sing N N 411 
W4U C4   C8   sing N N 412 
W4U C11  C10  sing Y N 413 
W4U C2   O1   sing N N 414 
W4U C5   H16  sing N N 415 
W4U C5   H17  sing N N 416 
W4U C6   H19  sing N N 417 
W4U C6   H18  sing N N 418 
W4U C7   H21  sing N N 419 
W4U C7   H20  sing N N 420 
W4U C8   H22  sing N N 421 
W4U C8   H23  sing N N 422 
W4U C10  H24  sing N N 423 
W4U C11  H25  sing N N 424 
W4U C14  H26  sing N N 425 
W4U C15  H27  sing N N 426 
W4U O1   H1   sing N N 427 
# 
_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                    8QM5 
_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]   0.021221 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002444 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014519 
_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]   0.015795 
_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  
CL 
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   ? 2.985   -22.190 -9.751  1.00 52.95  ?  11  ALA A N    1 
ATOM   2    C  CA   . ALA A 1 9   ? 4.198   -21.460 -10.169 1.00 52.64  ?  11  ALA A CA   1 
ATOM   3    C  C    . ALA A 1 9   ? 4.793   -20.735 -8.970  1.00 50.75  ?  11  ALA A C    1 
ATOM   4    O  O    . ALA A 1 9   ? 4.064   -20.342 -8.071  1.00 52.49  ?  11  ALA A O    1 
ATOM   5    C  CB   . ALA A 1 9   ? 3.868   -20.459 -11.265 1.00 53.20  ?  11  ALA A CB   1 
ATOM   6    N  N    . ARG A 1 10  ? 6.105   -20.552 -8.968  1.00 47.42  ?  12  ARG A N    1 
ATOM   7    C  CA   . ARG A 1 10  ? 6.826   -19.953 -7.847  1.00 44.56  ?  12  ARG A CA   1 
ATOM   8    C  C    . ARG A 1 10  ? 6.550   -18.450 -7.839  1.00 40.78  ?  12  ARG A C    1 
ATOM   9    O  O    . ARG A 1 10  ? 6.532   -17.817 -8.903  1.00 39.06  ?  12  ARG A O    1 
ATOM   10   C  CB   . ARG A 1 10  ? 8.330   -20.227 -8.030  1.00 46.28  ?  12  ARG A CB   1 
ATOM   11   C  CG   . ARG A 1 10  ? 9.241   -19.778 -6.857  1.00 48.76  ?  12  ARG A CG   1 
ATOM   12   C  CD   . ARG A 1 10  ? 10.689  -20.133 -7.151  1.00 50.32  ?  12  ARG A CD   1 
ATOM   13   N  NE   . ARG A 1 10  ? 10.840  -21.576 -7.375  1.00 50.60  ?  12  ARG A NE   1 
ATOM   14   C  CZ   . ARG A 1 10  ? 10.972  -22.487 -6.414  1.00 49.28  ?  12  ARG A CZ   1 
ATOM   15   N  NH1  . ARG A 1 10  ? 10.979  -22.120 -5.134  1.00 49.91  ?  12  ARG A NH1  1 
ATOM   16   N  NH2  . ARG A 1 10  ? 11.095  -23.775 -6.722  1.00 45.91  ?  12  ARG A NH2  1 
ATOM   17   N  N    . ILE A 1 11  ? 6.339   -17.883 -6.662  1.00 38.20  ?  13  ILE A N    1 
ATOM   18   C  CA   . ILE A 1 11  ? 6.212   -16.429 -6.529  1.00 37.07  ?  13  ILE A CA   1 
ATOM   19   C  C    . ILE A 1 11  ? 7.642   -15.779 -6.550  1.00 36.53  ?  13  ILE A C    1 
ATOM   20   O  O    . ILE A 1 11  ? 8.379   -15.838 -5.562  1.00 34.76  ?  13  ILE A O    1 
ATOM   21   C  CB   . ILE A 1 11  ? 5.473   -16.052 -5.252  1.00 35.37  ?  13  ILE A CB   1 
ATOM   22   C  CG1  . ILE A 1 11  ? 4.093   -16.763 -5.181  1.00 36.65  ?  13  ILE A CG1  1 
ATOM   23   C  CG2  . ILE A 1 11  ? 5.300   -14.568 -5.193  1.00 35.49  ?  13  ILE A CG2  1 
ATOM   24   C  CD1  . ILE A 1 11  ? 3.406   -16.650 -3.774  1.00 37.32  ?  13  ILE A CD1  1 
ATOM   25   N  N    . ILE A 1 12  ? 8.000   -15.142 -7.682  1.00 33.76  ?  14  ILE A N    1 
ATOM   26   C  CA   . ILE A 1 12  ? 9.283   -14.523 -7.855  1.00 34.69  ?  14  ILE A CA   1 
ATOM   27   C  C    . ILE A 1 12  ? 9.142   -12.997 -7.999  1.00 35.82  ?  14  ILE A C    1 
ATOM   28   O  O    . ILE A 1 12  ? 8.357   -12.529 -8.827  1.00 37.45  ?  14  ILE A O    1 
ATOM   29   C  CB   . ILE A 1 12  ? 10.023  -15.137 -9.054  1.00 35.13  ?  14  ILE A CB   1 
ATOM   30   C  CG1  . ILE A 1 12  ? 10.137  -16.695 -8.877  1.00 36.48  ?  14  ILE A CG1  1 
ATOM   31   C  CG2  . ILE A 1 12  ? 11.415  -14.485 -9.230  1.00 35.35  ?  14  ILE A CG2  1 
ATOM   32   C  CD1  . ILE A 1 12  ? 10.574  -17.396 -10.023 1.00 38.87  ?  14  ILE A CD1  1 
ATOM   33   N  N    . TYR A 1 13  ? 9.890   -12.231 -7.209  1.00 33.57  ?  15  TYR A N    1 
ATOM   34   C  CA   . TYR A 1 13  ? 9.886   -10.771 -7.277  1.00 34.58  ?  15  TYR A CA   1 
ATOM   35   C  C    . TYR A 1 13  ? 11.297  -10.263 -7.539  1.00 36.22  ?  15  TYR A C    1 
ATOM   36   O  O    . TYR A 1 13  ? 12.233  -10.672 -6.854  1.00 35.62  ?  15  TYR A O    1 
ATOM   37   C  CB   . TYR A 1 13  ? 9.449   -10.138 -5.974  1.00 35.25  ?  15  TYR A CB   1 
ATOM   38   C  CG   . TYR A 1 13  ? 8.041   -10.445 -5.539  1.00 35.94  ?  15  TYR A CG   1 
ATOM   39   C  CD1  . TYR A 1 13  ? 6.956   -9.849  -6.165  1.00 36.60  ?  15  TYR A CD1  1 
ATOM   40   C  CD2  . TYR A 1 13  ? 7.791   -11.311 -4.480  1.00 36.37  ?  15  TYR A CD2  1 
ATOM   41   C  CE1  . TYR A 1 13  ? 5.655   -10.131 -5.765  1.00 37.08  ?  15  TYR A CE1  1 
ATOM   42   C  CE2  . TYR A 1 13  ? 6.511   -11.554 -4.043  1.00 36.25  ?  15  TYR A CE2  1 
ATOM   43   C  CZ   . TYR A 1 13  ? 5.439   -10.968 -4.693  1.00 37.14  ?  15  TYR A CZ   1 
ATOM   44   O  OH   . TYR A 1 13  ? 4.156   -11.220 -4.306  1.00 38.40  ?  15  TYR A OH   1 
ATOM   45   N  N    . ASP A 1 14  ? 11.452  -9.354  -8.517  1.00 36.66  ?  16  ASP A N    1 
ATOM   46   C  CA   . ASP A 1 14  ? 12.713  -8.703  -8.745  1.00 37.11  ?  16  ASP A CA   1 
ATOM   47   C  C    . ASP A 1 14  ? 12.901  -7.506  -7.811  1.00 34.78  ?  16  ASP A C    1 
ATOM   48   O  O    . ASP A 1 14  ? 11.956  -7.071  -7.146  1.00 32.35  ?  16  ASP A O    1 
ATOM   49   C  CB   . ASP A 1 14  ? 12.922  -8.322  -10.232 1.00 40.25  ?  16  ASP A CB   1 
ATOM   50   C  CG   . ASP A 1 14  ? 11.962  -7.324  -10.851 1.00 47.19  ?  16  ASP A CG   1 
ATOM   51   O  OD1  . ASP A 1 14  ? 11.380  -6.492  -10.101 1.00 44.69  ?  16  ASP A OD1  1 
ATOM   52   O  OD2  . ASP A 1 14  ? 11.794  -7.361  -12.092 1.00 51.85  ?  16  ASP A OD2  1 
ATOM   53   N  N    . ARG A 1 15  ? 14.132  -6.990  -7.788  1.00 34.77  ?  17  ARG A N    1 
ATOM   54   C  CA   . ARG A 1 15  ? 14.522  -5.878  -6.909  1.00 37.19  ?  17  ARG A CA   1 
ATOM   55   C  C    . ARG A 1 15  ? 13.628  -4.645  -7.114  1.00 37.30  ?  17  ARG A C    1 
ATOM   56   O  O    . ARG A 1 15  ? 13.164  -4.085  -6.123  1.00 36.08  ?  17  ARG A O    1 
ATOM   57   C  CB   . ARG A 1 15  ? 16.000  -5.491  -7.168  1.00 39.54  ?  17  ARG A CB   1 
ATOM   58   C  CG   . ARG A 1 15  ? 16.596  -4.598  -6.129  1.00 44.49  ?  17  ARG A CG   1 
ATOM   59   C  CD   . ARG A 1 15  ? 17.925  -4.034  -6.619  1.00 49.44  ?  17  ARG A CD   1 
ATOM   60   N  NE   . ARG A 1 15  ? 18.330  -2.823  -5.912  1.00 57.85  ?  17  ARG A NE   1 
ATOM   61   C  CZ   . ARG A 1 15  ? 17.721  -1.643  -6.008  1.00 66.00  ?  17  ARG A CZ   1 
ATOM   62   N  NH1  . ARG A 1 15  ? 16.640  -1.498  -6.786  1.00 68.11  ?  17  ARG A NH1  1 
ATOM   63   N  NH2  . ARG A 1 15  ? 18.174  -0.604  -5.329  1.00 69.36  ?  17  ARG A NH2  1 
ATOM   64   N  N    . ALA A 1 16  ? 13.375  -4.233  -8.372  1.00 38.65  ?  18  ALA A N    1 
ATOM   65   C  CA   . ALA A 1 16  ? 12.561  -3.036  -8.645  1.00 39.03  ?  18  ALA A CA   1 
ATOM   66   C  C    . ALA A 1 16  ? 11.145  -3.159  -8.079  1.00 38.42  ?  18  ALA A C    1 
ATOM   67   O  O    . ALA A 1 16  ? 10.633  -2.196  -7.512  1.00 39.88  ?  18  ALA A O    1 
ATOM   68   C  CB   . ALA A 1 16  ? 12.481  -2.768  -10.142 1.00 39.00  ?  18  ALA A CB   1 
ATOM   69   N  N    . PHE A 1 17  ? 10.525  -4.316  -8.223  1.00 37.63  ?  19  PHE A N    1 
ATOM   70   C  CA   . PHE A 1 17  ? 9.200   -4.546  -7.723  1.00 37.31  ?  19  PHE A CA   1 
ATOM   71   C  C    . PHE A 1 17  ? 9.185   -4.493  -6.211  1.00 37.29  ?  19  PHE A C    1 
ATOM   72   O  O    . PHE A 1 17  ? 8.287   -3.865  -5.627  1.00 39.02  ?  19  PHE A O    1 
ATOM   73   C  CB   . PHE A 1 17  ? 8.663   -5.872  -8.224  1.00 38.21  ?  19  PHE A CB   1 
ATOM   74   C  CG   . PHE A 1 17  ? 7.187   -6.038  -7.999  1.00 41.31  ?  19  PHE A CG   1 
ATOM   75   C  CD1  . PHE A 1 17  ? 6.708   -6.596  -6.833  1.00 43.15  ?  19  PHE A CD1  1 
ATOM   76   C  CD2  . PHE A 1 17  ? 6.273   -5.606  -8.948  1.00 42.94  ?  19  PHE A CD2  1 
ATOM   77   C  CE1  . PHE A 1 17  ? 5.343   -6.736  -6.619  1.00 44.83  ?  19  PHE A CE1  1 
ATOM   78   C  CE2  . PHE A 1 17  ? 4.908   -5.755  -8.728  1.00 44.53  ?  19  PHE A CE2  1 
ATOM   79   C  CZ   . PHE A 1 17  ? 4.456   -6.320  -7.574  1.00 44.05  ?  19  PHE A CZ   1 
ATOM   80   N  N    . LEU A 1 18  ? 10.168  -5.122  -5.561  1.00 35.62  ?  20  LEU A N    1 
ATOM   81   C  CA   . LEU A 1 18  ? 10.199  -5.148  -4.093  1.00 35.28  ?  20  LEU A CA   1 
ATOM   82   C  C    . LEU A 1 18  ? 10.399  -3.721  -3.562  1.00 36.53  ?  20  LEU A C    1 
ATOM   83   O  O    . LEU A 1 18  ? 9.740   -3.344  -2.607  1.00 36.03  ?  20  LEU A O    1 
ATOM   84   C  CB   . LEU A 1 18  ? 11.313  -6.112  -3.568  1.00 32.41  ?  20  LEU A CB   1 
ATOM   85   C  CG   . LEU A 1 18  ? 11.111  -7.606  -3.866  1.00 30.64  ?  20  LEU A CG   1 
ATOM   86   C  CD1  . LEU A 1 18  ? 12.304  -8.454  -3.428  1.00 29.02  ?  20  LEU A CD1  1 
ATOM   87   C  CD2  . LEU A 1 18  ? 9.884   -8.146  -3.149  1.00 32.28  ?  20  LEU A CD2  1 
ATOM   88   N  N    . MET A 1 19  ? 11.279  -2.951  -4.201  1.00 38.26  ?  21  MET A N    1 
ATOM   89   C  CA   . MET A 1 19  ? 11.488  -1.540  -3.879  1.00 41.07  ?  21  MET A CA   1 
ATOM   90   C  C    . MET A 1 19  ? 10.237  -0.674  -4.092  1.00 44.07  ?  21  MET A C    1 
ATOM   91   O  O    . MET A 1 19  ? 10.003  0.189   -3.268  1.00 44.89  ?  21  MET A O    1 
ATOM   92   C  CB   . MET A 1 19  ? 12.647  -0.917  -4.656  1.00 41.00  ?  21  MET A CB   1 
ATOM   93   C  CG   . MET A 1 19  ? 14.013  -1.548  -4.407  1.00 42.40  ?  21  MET A CG   1 
ATOM   94   S  SD   . MET A 1 19  ? 14.581  -1.658  -2.659  1.00 47.15  ?  21  MET A SD   1 
ATOM   95   C  CE   . MET A 1 19  ? 14.424  0.032   -2.162  1.00 50.44  ?  21  MET A CE   1 
ATOM   96   N  N    . ALA A 1 20  ? 9.449   -0.898  -5.155  1.00 45.62  ?  22  ALA A N    1 
ATOM   97   C  CA   . ALA A 1 20  ? 8.130   -0.253  -5.393  1.00 47.11  ?  22  ALA A CA   1 
ATOM   98   C  C    . ALA A 1 20  ? 7.102   -0.475  -4.256  1.00 47.97  ?  22  ALA A C    1 
ATOM   99   O  O    . ALA A 1 20  ? 6.349   0.446   -3.983  1.00 48.04  ?  22  ALA A O    1 
ATOM   100  C  CB   . ALA A 1 20  ? 7.536   -0.707  -6.731  1.00 46.65  ?  22  ALA A CB   1 
ATOM   101  N  N    . CYS A 1 21  ? 7.070   -1.670  -3.600  1.00 48.22  ?  23  CYS A N    1 
ATOM   102  C  CA   . CYS A 1 21  ? 6.216   -1.999  -2.433  1.00 47.90  ?  23  CYS A CA   1 
ATOM   103  C  C    . CYS A 1 21  ? 6.642   -1.391  -1.113  1.00 48.43  ?  23  CYS A C    1 
ATOM   104  O  O    . CYS A 1 21  ? 5.955   -1.588  -0.105  1.00 48.33  ?  23  CYS A O    1 
ATOM   105  C  CB   . CYS A 1 21  ? 6.132   -3.504  -2.260  1.00 48.62  ?  23  CYS A CB   1 
ATOM   106  S  SG   . CYS A 1 21  ? 5.494   -4.391  -3.685  1.00 51.84  ?  23  CYS A SG   1 
ATOM   107  N  N    . ARG A 1 22  ? 7.758   -0.709  -1.083  1.00 49.34  ?  24  ARG A N    1 
ATOM   108  C  CA   . ARG A 1 22  ? 8.292   -0.169  0.141   1.00 51.72  ?  24  ARG A CA   1 
ATOM   109  C  C    . ARG A 1 22  ? 7.641   1.176   0.474   1.00 56.56  ?  24  ARG A C    1 
ATOM   110  O  O    . ARG A 1 22  ? 7.266   1.934   -0.432  1.00 57.50  ?  24  ARG A O    1 
ATOM   111  C  CB   . ARG A 1 22  ? 9.795   0.020   -0.012  1.00 50.77  ?  24  ARG A CB   1 
ATOM   112  C  CG   . ARG A 1 22  ? 10.453  0.462   1.250   1.00 50.48  ?  24  ARG A CG   1 
ATOM   113  C  CD   . ARG A 1 22  ? 11.832  0.906   0.961   1.00 52.02  ?  24  ARG A CD   1 
ATOM   114  N  NE   . ARG A 1 22  ? 12.598  1.085   2.193   1.00 53.09  ?  24  ARG A NE   1 
ATOM   115  C  CZ   . ARG A 1 22  ? 13.925  1.183   2.245   1.00 52.85  ?  24  ARG A CZ   1 
ATOM   116  N  NH1  . ARG A 1 22  ? 14.645  1.122   1.138   1.00 49.57  ?  24  ARG A NH1  1 
ATOM   117  N  NH2  . ARG A 1 22  ? 14.536  1.333   3.408   1.00 54.12  ?  24  ARG A NH2  1 
ATOM   118  N  N    . GLY A 1 23  ? 7.549   1.464   1.760   1.00 59.54  ?  25  GLY A N    1 
ATOM   119  C  CA   . GLY A 1 23  ? 7.259   2.816   2.215   1.00 64.09  ?  25  GLY A CA   1 
ATOM   120  C  C    . GLY A 1 23  ? 5.811   3.235   2.082   1.00 68.06  ?  25  GLY A C    1 
ATOM   121  O  O    . GLY A 1 23  ? 5.541   4.394   1.739   1.00 69.30  ?  25  GLY A O    1 
ATOM   122  N  N    . GLY A 1 24  ? 4.886   2.305   2.353   1.00 69.65  ?  26  GLY A N    1 
ATOM   123  C  CA   . GLY A 1 24  ? 3.460   2.587   2.287   1.00 71.89  ?  26  GLY A CA   1 
ATOM   124  C  C    . GLY A 1 24  ? 2.950   2.678   0.859   1.00 74.14  ?  26  GLY A C    1 
ATOM   125  O  O    . GLY A 1 24  ? 3.525   2.062   -0.046  1.00 74.36  ?  26  GLY A O    1 
ATOM   126  N  N    . GLY A 1 25  ? 1.880   3.462   0.663   1.00 75.39  ?  27  GLY A N    1 
ATOM   127  C  CA   . GLY A 1 25  ? 1.111   3.477   -0.581  1.00 76.34  ?  27  GLY A CA   1 
ATOM   128  C  C    . GLY A 1 25  ? -0.373  3.239   -0.367  1.00 77.22  ?  27  GLY A C    1 
ATOM   129  O  O    . GLY A 1 25  ? -1.134  4.210   -0.278  1.00 78.40  ?  27  GLY A O    1 
ATOM   130  N  N    . GLY A 1 26  ? -0.791  1.962   -0.269  1.00 76.39  ?  28  GLY A N    1 
ATOM   131  C  CA   . GLY A 1 26  ? -2.210  1.589   -0.394  1.00 75.70  ?  28  GLY A CA   1 
ATOM   132  C  C    . GLY A 1 26  ? -2.840  0.772   0.727   1.00 74.41  ?  28  GLY A C    1 
ATOM   133  O  O    . GLY A 1 26  ? -2.170  -0.031  1.394   1.00 74.83  ?  28  GLY A O    1 
ATOM   134  N  N    . GLU A 1 27  ? -4.158  0.973   0.932   1.00 72.54  ?  29  GLU A N    1 
ATOM   135  C  CA   . GLU A 1 27  ? -4.939  0.204   1.907   1.00 71.02  ?  29  GLU A CA   1 
ATOM   136  C  C    . GLU A 1 27  ? -5.002  -1.263  1.477   1.00 68.30  ?  29  GLU A C    1 
ATOM   137  O  O    . GLU A 1 27  ? -5.128  -1.566  0.280   1.00 68.93  ?  29  GLU A O    1 
ATOM   138  C  CB   . GLU A 1 27  ? -6.382  0.750   2.045   1.00 74.96  ?  29  GLU A CB   1 
ATOM   139  C  CG   . GLU A 1 27  ? -6.523  1.985   2.930   1.00 82.75  ?  29  GLU A CG   1 
ATOM   140  C  CD   . GLU A 1 27  ? -6.220  1.773   4.407   1.00 91.39  ?  29  GLU A CD   1 
ATOM   141  O  OE1  . GLU A 1 27  ? -6.388  0.630   4.899   1.00 92.62  ?  29  GLU A OE1  1 
ATOM   142  O  OE2  . GLU A 1 27  ? -5.814  2.757   5.073   1.00 93.24  ?  29  GLU A OE2  1 
ATOM   143  N  N    . ASN A 1 28  ? -4.922  -2.173  2.462   1.00 64.59  ?  30  ASN A N    1 
ATOM   144  C  CA   . ASN A 1 28  ? -4.948  -3.603  2.198   1.00 60.77  ?  30  ASN A CA   1 
ATOM   145  C  C    . ASN A 1 28  ? -6.418  -4.048  2.006   1.00 58.52  ?  30  ASN A C    1 
ATOM   146  O  O    . ASN A 1 28  ? -6.988  -4.668  2.914   1.00 58.87  ?  30  ASN A O    1 
ATOM   147  C  CB   . ASN A 1 28  ? -4.295  -4.323  3.357   1.00 59.08  ?  30  ASN A CB   1 
ATOM   148  C  CG   . ASN A 1 28  ? -4.241  -5.810  3.177   1.00 58.37  ?  30  ASN A CG   1 
ATOM   149  O  OD1  . ASN A 1 28  ? -4.192  -6.308  2.057   1.00 58.94  ?  30  ASN A OD1  1 
ATOM   150  N  ND2  . ASN A 1 28  ? -4.236  -6.534  4.258   1.00 57.54  ?  30  ASN A ND2  1 
ATOM   151  N  N    . LEU A 1 29  ? -7.024  -3.740  0.839   1.00 56.54  ?  31  LEU A N    1 
ATOM   152  C  CA   . LEU A 1 29  ? -8.482  -3.920  0.723   1.00 55.28  ?  31  LEU A CA   1 
ATOM   153  C  C    . LEU A 1 29  ? -8.762  -5.403  0.621   1.00 51.95  ?  31  LEU A C    1 
ATOM   154  O  O    . LEU A 1 29  ? -8.074  -6.138  -0.080  1.00 50.25  ?  31  LEU A O    1 
ATOM   155  C  CB   . LEU A 1 29  ? -9.137  -3.177  -0.464  1.00 56.18  ?  31  LEU A CB   1 
ATOM   156  C  CG   . LEU A 1 29  ? -9.113  -1.625  -0.433  1.00 59.13  ?  31  LEU A CG   1 
ATOM   157  C  CD1  . LEU A 1 29  ? -9.819  -1.057  -1.656  1.00 59.84  ?  31  LEU A CD1  1 
ATOM   158  C  CD2  . LEU A 1 29  ? -9.765  -1.058  0.831   1.00 59.31  ?  31  LEU A CD2  1 
ATOM   159  N  N    . TYR A 1 30  ? -9.780  -5.834  1.325   1.00 51.01  ?  32  TYR A N    1 
ATOM   160  C  CA   . TYR A 1 30  ? -10.209 -7.217  1.325   1.00 50.44  ?  32  TYR A CA   1 
ATOM   161  C  C    . TYR A 1 30  ? -9.157  -8.171  1.917   1.00 51.23  ?  32  TYR A C    1 
ATOM   162  O  O    . TYR A 1 30  ? -9.285  -9.382  1.716   1.00 51.14  ?  32  TYR A O    1 
ATOM   163  C  CB   . TYR A 1 30  ? -10.567 -7.635  -0.104  1.00 49.76  ?  32  TYR A CB   1 
ATOM   164  C  CG   . TYR A 1 30  ? -11.629 -6.747  -0.695  1.00 49.74  ?  32  TYR A CG   1 
ATOM   165  C  CD1  . TYR A 1 30  ? -12.947 -6.836  -0.270  1.00 50.15  ?  32  TYR A CD1  1 
ATOM   166  C  CD2  . TYR A 1 30  ? -11.319 -5.805  -1.671  1.00 49.97  ?  32  TYR A CD2  1 
ATOM   167  C  CE1  . TYR A 1 30  ? -13.932 -6.034  -0.812  1.00 50.31  ?  32  TYR A CE1  1 
ATOM   168  C  CE2  . TYR A 1 30  ? -12.303 -4.996  -2.231  1.00 50.16  ?  32  TYR A CE2  1 
ATOM   169  C  CZ   . TYR A 1 30  ? -13.612 -5.103  -1.775  1.00 51.33  ?  32  TYR A CZ   1 
ATOM   170  O  OH   . TYR A 1 30  ? -14.626 -4.322  -2.259  1.00 54.68  ?  32  TYR A OH   1 
ATOM   171  N  N    . PHE A 1 31  ? -8.120  -7.639  2.643   1.00 51.06  ?  33  PHE A N    1 
ATOM   172  C  CA   . PHE A 1 31  ? -6.926  -8.410  3.025   1.00 50.90  ?  33  PHE A CA   1 
ATOM   173  C  C    . PHE A 1 31  ? -6.285  -9.117  1.850   1.00 49.70  ?  33  PHE A C    1 
ATOM   174  O  O    . PHE A 1 31  ? -5.726  -10.203 2.006   1.00 50.80  ?  33  PHE A O    1 
ATOM   175  C  CB   . PHE A 1 31  ? -7.269  -9.417  4.137   1.00 51.56  ?  33  PHE A CB   1 
ATOM   176  C  CG   . PHE A 1 31  ? -7.605  -8.742  5.433   1.00 52.63  ?  33  PHE A CG   1 
ATOM   177  C  CD1  . PHE A 1 31  ? -6.619  -8.184  6.215   1.00 53.73  ?  33  PHE A CD1  1 
ATOM   178  C  CD2  . PHE A 1 31  ? -8.903  -8.675  5.874   1.00 53.99  ?  33  PHE A CD2  1 
ATOM   179  C  CE1  . PHE A 1 31  ? -6.930  -7.567  7.416   1.00 54.71  ?  33  PHE A CE1  1 
ATOM   180  C  CE2  . PHE A 1 31  ? -9.212  -8.057  7.076   1.00 55.29  ?  33  PHE A CE2  1 
ATOM   181  C  CZ   . PHE A 1 31  ? -8.229  -7.502  7.834   1.00 54.79  ?  33  PHE A CZ   1 
ATOM   182  N  N    . GLN A 1 32  ? -6.348  -8.491  0.673   1.00 47.92  ?  34  GLN A N    1 
ATOM   183  C  CA   . GLN A 1 32  ? -5.821  -9.027  -0.568  1.00 47.21  ?  34  GLN A CA   1 
ATOM   184  C  C    . GLN A 1 32  ? -4.934  -8.000  -1.314  1.00 46.98  ?  34  GLN A C    1 
ATOM   185  O  O    . GLN A 1 32  ? -4.637  -8.216  -2.484  1.00 47.17  ?  34  GLN A O    1 
ATOM   186  C  CB   . GLN A 1 32  ? -6.989  -9.481  -1.474  1.00 48.59  ?  34  GLN A CB   1 
ATOM   187  C  CG   . GLN A 1 32  ? -7.846  -10.598 -0.841  1.00 51.43  ?  34  GLN A CG   1 
ATOM   188  C  CD   . GLN A 1 32  ? -8.987  -10.991 -1.730  1.00 59.83  ?  34  GLN A CD   1 
ATOM   189  O  OE1  . GLN A 1 32  ? -8.804  -11.198 -2.938  1.00 63.27  ?  34  GLN A OE1  1 
ATOM   190  N  NE2  . GLN A 1 32  ? -10.205 -11.109 -1.165  1.00 59.10  ?  34  GLN A NE2  1 
ATOM   191  N  N    . GLY A 1 33  ? -4.540  -6.907  -0.654  1.00 46.40  ?  35  GLY A N    1 
ATOM   192  C  CA   . GLY A 1 33  ? -3.662  -5.902  -1.235  1.00 46.89  ?  35  GLY A CA   1 
ATOM   193  C  C    . GLY A 1 33  ? -2.195  -6.144  -0.941  1.00 47.08  ?  35  GLY A C    1 
ATOM   194  O  O    . GLY A 1 33  ? -1.379  -5.590  -1.660  1.00 48.83  ?  35  GLY A O    1 
ATOM   195  N  N    . LYS A 1 34  ? -1.834  -6.983  0.068   1.00 45.59  ?  36  LYS A N    1 
ATOM   196  C  CA   . LYS A 1 34  ? -0.436  -7.321  0.306   1.00 45.12  ?  36  LYS A CA   1 
ATOM   197  C  C    . LYS A 1 34  ? 0.074   -8.382  -0.675  1.00 46.07  ?  36  LYS A C    1 
ATOM   198  O  O    . LYS A 1 34  ? -0.674  -9.260  -1.066  1.00 47.41  ?  36  LYS A O    1 
ATOM   199  C  CB   . LYS A 1 34  ? -0.202  -7.765  1.758   1.00 44.51  ?  36  LYS A CB   1 
ATOM   200  C  CG   . LYS A 1 34  ? -0.384  -6.651  2.770   1.00 46.63  ?  36  LYS A CG   1 
ATOM   201  C  CD   . LYS A 1 34  ? -0.411  -7.213  4.160   1.00 49.85  ?  36  LYS A CD   1 
ATOM   202  C  CE   . LYS A 1 34  ? -0.229  -6.198  5.260   1.00 50.60  ?  36  LYS A CE   1 
ATOM   203  N  NZ   . LYS A 1 34  ? -0.261  -6.863  6.599   1.00 53.10  ?  36  LYS A NZ   1 
ATOM   204  N  N    . HIS A 1 35  ? 1.355   -8.283  -1.083  1.00 44.58  ?  37  HIS A N    1 
ATOM   205  C  CA   . HIS A 1 35  ? 1.976   -9.192  -2.049  1.00 43.91  ?  37  HIS A CA   1 
ATOM   206  C  C    . HIS A 1 35  ? 2.529   -10.395 -1.292  1.00 42.77  ?  37  HIS A C    1 
ATOM   207  O  O    . HIS A 1 35  ? 3.445   -10.214 -0.516  1.00 41.54  ?  37  HIS A O    1 
ATOM   208  C  CB   . HIS A 1 35  ? 3.079   -8.490  -2.819  1.00 45.29  ?  37  HIS A CB   1 
ATOM   209  C  CG   . HIS A 1 35  ? 2.545   -7.403  -3.703  1.00 47.71  ?  37  HIS A CG   1 
ATOM   210  N  ND1  . HIS A 1 35  ? 2.331   -6.118  -3.226  1.00 48.66  ?  37  HIS A ND1  1 
ATOM   211  C  CD2  . HIS A 1 35  ? 2.186   -7.450  -5.014  1.00 49.15  ?  37  HIS A CD2  1 
ATOM   212  C  CE1  . HIS A 1 35  ? 1.854   -5.428  -4.254  1.00 49.50  ?  37  HIS A CE1  1 
ATOM   213  N  NE2  . HIS A 1 35  ? 1.749   -6.191  -5.350  1.00 49.71  ?  37  HIS A NE2  1 
ATOM   214  N  N    . PRO A 1 36  ? 1.988   -11.619 -1.468  1.00 43.30  ?  38  PRO A N    1 
ATOM   215  C  CA   . PRO A 1 36  ? 2.538   -12.775 -0.735  1.00 41.43  ?  38  PRO A CA   1 
ATOM   216  C  C    . PRO A 1 36  ? 3.913   -13.224 -1.221  1.00 37.71  ?  38  PRO A C    1 
ATOM   217  O  O    . PRO A 1 36  ? 4.240   -13.142 -2.413  1.00 36.01  ?  38  PRO A O    1 
ATOM   218  C  CB   . PRO A 1 36  ? 1.522   -13.884 -1.005  1.00 43.33  ?  38  PRO A CB   1 
ATOM   219  C  CG   . PRO A 1 36  ? 0.337   -13.203 -1.609  1.00 45.99  ?  38  PRO A CG   1 
ATOM   220  C  CD   . PRO A 1 36  ? 0.850   -12.035 -2.315  1.00 43.77  ?  38  PRO A CD   1 
ATOM   221  N  N    . LEU A 1 37  ? 4.702   -13.705 -0.276  1.00 35.62  ?  39  LEU A N    1 
ATOM   222  C  CA   . LEU A 1 37  ? 5.965   -14.363 -0.544  1.00 33.92  ?  39  LEU A CA   1 
ATOM   223  C  C    . LEU A 1 37  ? 5.796   -15.847 -0.772  1.00 32.53  ?  39  LEU A C    1 
ATOM   224  O  O    . LEU A 1 37  ? 4.845   -16.444 -0.268  1.00 34.32  ?  39  LEU A O    1 
ATOM   225  C  CB   . LEU A 1 37  ? 6.889   -14.110 0.653   1.00 33.66  ?  39  LEU A CB   1 
ATOM   226  C  CG   . LEU A 1 37  ? 7.267   -12.625 0.927   1.00 35.44  ?  39  LEU A CG   1 
ATOM   227  C  CD1  . LEU A 1 37  ? 8.159   -12.492 2.156   1.00 35.12  ?  39  LEU A CD1  1 
ATOM   228  C  CD2  . LEU A 1 37  ? 7.854   -11.942 -0.301  1.00 35.13  ?  39  LEU A CD2  1 
ATOM   229  N  N    . GLN A 1 38  ? 6.704   -16.461 -1.491  1.00 31.36  ?  40  GLN A N    1 
ATOM   230  C  CA   . GLN A 1 38  ? 6.751   -17.919 -1.660  1.00 31.82  ?  40  GLN A CA   1 
ATOM   231  C  C    . GLN A 1 38  ? 6.862   -18.636 -0.302  1.00 32.49  ?  40  GLN A C    1 
ATOM   232  O  O    . GLN A 1 38  ? 6.244   -19.685 -0.073  1.00 30.36  ?  40  GLN A O    1 
ATOM   233  C  CB   . GLN A 1 38  ? 7.903   -18.299 -2.579  1.00 31.26  ?  40  GLN A CB   1 
ATOM   234  C  CG   . GLN A 1 38  ? 8.063   -19.781 -2.877  1.00 35.04  ?  40  GLN A CG   1 
ATOM   235  C  CD   . GLN A 1 38  ? 6.923   -20.360 -3.725  1.00 43.77  ?  40  GLN A CD   1 
ATOM   236  O  OE1  . GLN A 1 38  ? 6.189   -19.646 -4.436  1.00 41.79  ?  40  GLN A OE1  1 
ATOM   237  N  NE2  . GLN A 1 38  ? 6.769   -21.674 -3.669  1.00 43.27  ?  40  GLN A NE2  1 
ATOM   238  N  N    . ASN A 1 39  ? 7.675   -18.057 0.587   1.00 31.60  ?  41  ASN A N    1 
ATOM   239  C  CA   . ASN A 1 39  ? 7.986   -18.677 1.898   1.00 30.68  ?  41  ASN A CA   1 
ATOM   240  C  C    . ASN A 1 39  ? 7.640   -17.736 2.989   1.00 30.45  ?  41  ASN A C    1 
ATOM   241  O  O    . ASN A 1 39  ? 7.648   -16.505 2.783   1.00 32.34  ?  41  ASN A O    1 
ATOM   242  C  CB   . ASN A 1 39  ? 9.495   -19.031 1.972   1.00 30.76  ?  41  ASN A CB   1 
ATOM   243  C  CG   . ASN A 1 39  ? 9.837   -20.226 1.135   1.00 37.40  ?  41  ASN A CG   1 
ATOM   244  O  OD1  . ASN A 1 39  ? 9.542   -21.347 1.504   1.00 40.90  ?  41  ASN A OD1  1 
ATOM   245  N  ND2  . ASN A 1 39  ? 10.429  -20.046 -0.004  1.00 35.87  ?  41  ASN A ND2  1 
ATOM   246  N  N    . ARG A 1 40  ? 7.335   -18.289 4.148   1.00 30.03  ?  42  ARG A N    1 
ATOM   247  C  CA   . ARG A 1 40  ? 7.353   -17.514 5.411   1.00 29.68  ?  42  ARG A CA   1 
ATOM   248  C  C    . ARG A 1 40  ? 8.808   -17.510 5.946   1.00 28.38  ?  42  ARG A C    1 
ATOM   249  O  O    . ARG A 1 40  ? 9.514   -18.501 5.810   1.00 29.00  ?  42  ARG A O    1 
ATOM   250  C  CB   . ARG A 1 40  ? 6.409   -18.133 6.444   1.00 31.07  ?  42  ARG A CB   1 
ATOM   251  C  CG   . ARG A 1 40  ? 6.422   -17.366 7.771   1.00 38.85  ?  42  ARG A CG   1 
ATOM   252  C  CD   . ARG A 1 40  ? 5.448   -17.929 8.803   1.00 48.40  ?  42  ARG A CD   1 
ATOM   253  N  NE   . ARG A 1 40  ? 4.032   -17.637 8.611   1.00 56.81  ?  42  ARG A NE   1 
ATOM   254  C  CZ   . ARG A 1 40  ? 3.437   -16.470 8.895   1.00 64.46  ?  42  ARG A CZ   1 
ATOM   255  N  NH1  . ARG A 1 40  ? 4.149   -15.443 9.360   1.00 65.02  ?  42  ARG A NH1  1 
ATOM   256  N  NH2  . ARG A 1 40  ? 2.126   -16.319 8.707   1.00 65.21  ?  42  ARG A NH2  1 
ATOM   257  N  N    . TRP A 1 41  ? 9.243   -16.369 6.512   1.00 27.32  ?  43  TRP A N    1 
ATOM   258  C  CA   . TRP A 1 41  ? 10.623  -16.085 6.934   1.00 27.56  ?  43  TRP A CA   1 
ATOM   259  C  C    . TRP A 1 41  ? 10.610  -15.633 8.402   1.00 27.26  ?  43  TRP A C    1 
ATOM   260  O  O    . TRP A 1 41  ? 9.632   -15.028 8.835   1.00 29.19  ?  43  TRP A O    1 
ATOM   261  C  CB   . TRP A 1 41  ? 11.245  -14.977 6.068   1.00 27.06  ?  43  TRP A CB   1 
ATOM   262  C  CG   . TRP A 1 41  ? 11.375  -15.369 4.621   1.00 27.06  ?  43  TRP A CG   1 
ATOM   263  C  CD1  . TRP A 1 41  ? 10.450  -15.223 3.635   1.00 27.67  ?  43  TRP A CD1  1 
ATOM   264  C  CD2  . TRP A 1 41  ? 12.511  -16.002 4.019   1.00 27.07  ?  43  TRP A CD2  1 
ATOM   265  N  NE1  . TRP A 1 41  ? 10.940  -15.722 2.445   1.00 27.91  ?  43  TRP A NE1  1 
ATOM   266  C  CE2  . TRP A 1 41  ? 12.203  -16.212 2.654   1.00 27.73  ?  43  TRP A CE2  1 
ATOM   267  C  CE3  . TRP A 1 41  ? 13.730  -16.465 4.513   1.00 27.02  ?  43  TRP A CE3  1 
ATOM   268  C  CZ2  . TRP A 1 41  ? 13.080  -16.833 1.792   1.00 27.91  ?  43  TRP A CZ2  1 
ATOM   269  C  CZ3  . TRP A 1 41  ? 14.624  -17.037 3.635   1.00 27.06  ?  43  TRP A CZ3  1 
ATOM   270  C  CH2  . TRP A 1 41  ? 14.303  -17.198 2.294   1.00 29.00  ?  43  TRP A CH2  1 
ATOM   271  N  N    . ALA A 1 42  ? 11.658  -15.898 9.115   1.00 25.88  ?  44  ALA A N    1 
ATOM   272  C  CA   . ALA A 1 42  ? 11.836  -15.507 10.490  1.00 27.36  ?  44  ALA A CA   1 
ATOM   273  C  C    . ALA A 1 42  ? 13.118  -14.726 10.583  1.00 26.67  ?  44  ALA A C    1 
ATOM   274  O  O    . ALA A 1 42  ? 14.193  -15.170 10.090  1.00 26.23  ?  44  ALA A O    1 
ATOM   275  C  CB   . ALA A 1 42  ? 11.899  -16.750 11.401  1.00 27.75  ?  44  ALA A CB   1 
ATOM   276  N  N    . LEU A 1 43  ? 13.032  -13.575 11.208  1.00 26.42  ?  45  LEU A N    1 
ATOM   277  C  CA   . LEU A 1 43  ? 14.184  -12.763 11.552  1.00 27.73  ?  45  LEU A CA   1 
ATOM   278  C  C    . LEU A 1 43  ? 14.637  -13.098 12.994  1.00 27.26  ?  45  LEU A C    1 
ATOM   279  O  O    . LEU A 1 43  ? 13.838  -13.043 13.949  1.00 26.70  ?  45  LEU A O    1 
ATOM   280  C  CB   . LEU A 1 43  ? 13.824  -11.261 11.454  1.00 29.43  ?  45  LEU A CB   1 
ATOM   281  C  CG   . LEU A 1 43  ? 15.014  -10.327 11.748  1.00 31.80  ?  45  LEU A CG   1 
ATOM   282  C  CD1  . LEU A 1 43  ? 16.065  -10.425 10.711  1.00 30.32  ?  45  LEU A CD1  1 
ATOM   283  C  CD2  . LEU A 1 43  ? 14.564  -8.905  11.878  1.00 35.35  ?  45  LEU A CD2  1 
ATOM   284  N  N    . TRP A 1 44  ? 15.883  -13.440 13.140  1.00 26.91  ?  46  TRP A N    1 
ATOM   285  C  CA   . TRP A 1 44  ? 16.551  -13.755 14.366  1.00 28.34  ?  46  TRP A CA   1 
ATOM   286  C  C    . TRP A 1 44  ? 17.618  -12.731 14.712  1.00 30.79  ?  46  TRP A C    1 
ATOM   287  O  O    . TRP A 1 44  ? 18.206  -12.064 13.832  1.00 29.63  ?  46  TRP A O    1 
ATOM   288  C  CB   . TRP A 1 44  ? 17.196  -15.125 14.306  1.00 27.59  ?  46  TRP A CB   1 
ATOM   289  C  CG   . TRP A 1 44  ? 16.317  -16.263 13.892  1.00 26.83  ?  46  TRP A CG   1 
ATOM   290  C  CD1  . TRP A 1 44  ? 15.822  -16.547 12.651  1.00 25.63  ?  46  TRP A CD1  1 
ATOM   291  C  CD2  . TRP A 1 44  ? 15.889  -17.311 14.746  1.00 27.73  ?  46  TRP A CD2  1 
ATOM   292  N  NE1  . TRP A 1 44  ? 15.130  -17.730 12.682  1.00 28.03  ?  46  TRP A NE1  1 
ATOM   293  C  CE2  . TRP A 1 44  ? 15.093  -18.189 13.966  1.00 29.11  ?  46  TRP A CE2  1 
ATOM   294  C  CE3  . TRP A 1 44  ? 16.033  -17.549 16.115  1.00 30.14  ?  46  TRP A CE3  1 
ATOM   295  C  CZ2  . TRP A 1 44  ? 14.513  -19.341 14.492  1.00 32.73  ?  46  TRP A CZ2  1 
ATOM   296  C  CZ3  . TRP A 1 44  ? 15.427  -18.682 16.650  1.00 34.26  ?  46  TRP A CZ3  1 
ATOM   297  C  CH2  . TRP A 1 44  ? 14.665  -19.555 15.840  1.00 34.32  ?  46  TRP A CH2  1 
ATOM   298  N  N    . PHE A 1 45  ? 17.890  -12.601 15.990  1.00 31.63  ?  47  PHE A N    1 
ATOM   299  C  CA   . PHE A 1 45  ? 18.922  -11.750 16.523  1.00 36.72  ?  47  PHE A CA   1 
ATOM   300  C  C    . PHE A 1 45  ? 19.707  -12.484 17.596  1.00 38.90  ?  47  PHE A C    1 
ATOM   301  O  O    . PHE A 1 45  ? 19.111  -13.230 18.377  1.00 37.25  ?  47  PHE A O    1 
ATOM   302  C  CB   . PHE A 1 45  ? 18.229  -10.510 17.128  1.00 40.24  ?  47  PHE A CB   1 
ATOM   303  C  CG   . PHE A 1 45  ? 19.092  -9.520  17.849  1.00 44.11  ?  47  PHE A CG   1 
ATOM   304  C  CD1  . PHE A 1 45  ? 20.039  -8.780  17.166  1.00 47.26  ?  47  PHE A CD1  1 
ATOM   305  C  CD2  . PHE A 1 45  ? 18.941  -9.306  19.201  1.00 46.89  ?  47  PHE A CD2  1 
ATOM   306  C  CE1  . PHE A 1 45  ? 20.831  -7.855  17.828  1.00 48.96  ?  47  PHE A CE1  1 
ATOM   307  C  CE2  . PHE A 1 45  ? 19.720  -8.381  19.862  1.00 48.66  ?  47  PHE A CE2  1 
ATOM   308  C  CZ   . PHE A 1 45  ? 20.674  -7.661  19.178  1.00 49.00  ?  47  PHE A CZ   1 
ATOM   309  N  N    . PHE A 1 46  ? 21.014  -12.267 17.619  1.00 42.24  ?  48  PHE A N    1 
ATOM   310  C  CA   . PHE A 1 46  ? 21.893  -12.692 18.686  1.00 49.61  ?  48  PHE A CA   1 
ATOM   311  C  C    . PHE A 1 46  ? 22.348  -11.456 19.484  1.00 54.39  ?  48  PHE A C    1 
ATOM   312  O  O    . PHE A 1 46  ? 22.925  -10.531 18.916  1.00 54.24  ?  48  PHE A O    1 
ATOM   313  C  CB   . PHE A 1 46  ? 23.070  -13.470 18.119  1.00 53.00  ?  48  PHE A CB   1 
ATOM   314  C  CG   . PHE A 1 46  ? 23.859  -14.221 19.167  1.00 57.91  ?  48  PHE A CG   1 
ATOM   315  C  CD1  . PHE A 1 46  ? 23.394  -15.423 19.680  1.00 59.57  ?  48  PHE A CD1  1 
ATOM   316  C  CD2  . PHE A 1 46  ? 25.080  -13.732 19.623  1.00 61.07  ?  48  PHE A CD2  1 
ATOM   317  C  CE1  . PHE A 1 46  ? 24.129  -16.111 20.644  1.00 61.31  ?  48  PHE A CE1  1 
ATOM   318  C  CE2  . PHE A 1 46  ? 25.819  -14.425 20.568  1.00 62.82  ?  48  PHE A CE2  1 
ATOM   319  C  CZ   . PHE A 1 46  ? 25.344  -15.606 21.076  1.00 62.36  ?  48  PHE A CZ   1 
ATOM   320  N  N    . LYS A 1 47  ? 22.062  -11.435 20.799  1.00 58.11  ?  49  LYS A N    1 
ATOM   321  C  CA   . LYS A 1 47  ? 22.472  -10.340 21.717  1.00 62.44  ?  49  LYS A CA   1 
ATOM   322  C  C    . LYS A 1 47  ? 23.881  -10.616 22.261  1.00 65.29  ?  49  LYS A C    1 
ATOM   323  O  O    . LYS A 1 47  ? 24.167  -11.762 22.618  1.00 65.27  ?  49  LYS A O    1 
ATOM   324  C  CB   . LYS A 1 47  ? 21.493  -10.256 22.917  1.00 65.05  ?  49  LYS A CB   1 
ATOM   325  C  CG   . LYS A 1 47  ? 21.150  -8.832  23.385  1.00 71.42  ?  49  LYS A CG   1 
ATOM   326  C  CD   . LYS A 1 47  ? 19.778  -8.760  24.056  1.00 77.57  ?  49  LYS A CD   1 
ATOM   327  C  CE   . LYS A 1 47  ? 19.284  -7.344  24.301  1.00 81.54  ?  49  LYS A CE   1 
ATOM   328  N  NZ   . LYS A 1 47  ? 18.869  -6.664  23.032  1.00 84.19  ?  49  LYS A NZ   1 
ATOM   329  N  N    . ASN A 1 48  ? 24.762  -9.586  22.331  1.00 67.21  ?  50  ASN A N    1 
ATOM   330  C  CA   . ASN A 1 48  ? 26.112  -9.768  22.894  1.00 70.34  ?  50  ASN A CA   1 
ATOM   331  C  C    . ASN A 1 48  ? 26.054  -9.483  24.407  1.00 71.95  ?  50  ASN A C    1 
ATOM   332  O  O    . ASN A 1 48  ? 26.836  -8.696  24.931  1.00 72.32  ?  50  ASN A O    1 
ATOM   333  C  CB   . ASN A 1 48  ? 27.144  -8.865  22.179  1.00 73.46  ?  50  ASN A CB   1 
ATOM   334  C  CG   . ASN A 1 48  ? 28.587  -9.198  22.531  1.00 79.29  ?  50  ASN A CG   1 
ATOM   335  O  OD1  . ASN A 1 48  ? 28.870  -10.095 23.333  1.00 81.35  ?  50  ASN A OD1  1 
ATOM   336  N  ND2  . ASN A 1 48  ? 29.536  -8.485  21.949  1.00 80.43  ?  50  ASN A ND2  1 
ATOM   337  N  N    . ASP A 1 49  ? 25.105  -10.124 25.097  1.00 73.05  ?  51  ASP A N    1 
ATOM   338  C  CA   . ASP A 1 49  ? 24.870  -9.926  26.521  1.00 74.42  ?  51  ASP A CA   1 
ATOM   339  C  C    . ASP A 1 49  ? 25.553  -11.001 27.356  1.00 75.27  ?  51  ASP A C    1 
ATOM   340  O  O    . ASP A 1 49  ? 25.005  -12.082 27.535  1.00 75.06  ?  51  ASP A O    1 
ATOM   341  C  CB   . ASP A 1 49  ? 23.354  -9.915  26.795  1.00 76.62  ?  51  ASP A CB   1 
ATOM   342  C  CG   . ASP A 1 49  ? 22.957  -9.626  28.224  1.00 82.32  ?  51  ASP A CG   1 
ATOM   343  O  OD1  . ASP A 1 49  ? 23.855  -9.594  29.101  1.00 82.97  ?  51  ASP A OD1  1 
ATOM   344  O  OD2  . ASP A 1 49  ? 21.755  -9.427  28.470  1.00 85.44  ?  51  ASP A OD2  1 
ATOM   345  N  N    . LYS A 1 50  ? 26.740  -10.700 27.889  1.00 76.42  ?  52  LYS A N    1 
ATOM   346  C  CA   . LYS A 1 50  ? 27.500  -11.683 28.662  1.00 77.45  ?  52  LYS A CA   1 
ATOM   347  C  C    . LYS A 1 50  ? 26.934  -11.943 30.077  1.00 76.57  ?  52  LYS A C    1 
ATOM   348  O  O    . LYS A 1 50  ? 27.436  -12.844 30.748  1.00 76.34  ?  52  LYS A O    1 
ATOM   349  C  CB   . LYS A 1 50  ? 28.992  -11.318 28.722  1.00 81.52  ?  52  LYS A CB   1 
ATOM   350  C  CG   . LYS A 1 50  ? 29.686  -11.266 27.352  1.00 88.94  ?  52  LYS A CG   1 
ATOM   351  C  CD   . LYS A 1 50  ? 29.962  -12.677 26.778  1.00 95.56  ?  52  LYS A CD   1 
ATOM   352  C  CE   . LYS A 1 50  ? 30.744  -12.654 25.485  1.00 101.41 ?  52  LYS A CE   1 
ATOM   353  N  NZ   . LYS A 1 50  ? 29.864  -12.440 24.303  1.00 105.28 ?  52  LYS A NZ   1 
ATOM   354  N  N    . SER A 1 51  ? 25.901  -11.187 30.533  1.00 75.62  ?  53  SER A N    1 
ATOM   355  C  CA   . SER A 1 51  ? 25.162  -11.594 31.738  1.00 74.73  ?  53  SER A CA   1 
ATOM   356  C  C    . SER A 1 51  ? 24.239  -12.821 31.463  1.00 73.32  ?  53  SER A C    1 
ATOM   357  O  O    . SER A 1 51  ? 23.731  -13.412 32.422  1.00 74.85  ?  53  SER A O    1 
ATOM   358  C  CB   . SER A 1 51  ? 24.357  -10.427 32.324  1.00 76.47  ?  53  SER A CB   1 
ATOM   359  O  OG   . SER A 1 51  ? 23.053  -10.275 31.782  1.00 78.86  ?  53  SER A OG   1 
ATOM   360  N  N    . LYS A 1 52  ? 24.016  -13.189 30.174  1.00 70.26  ?  54  LYS A N    1 
ATOM   361  C  CA   . LYS A 1 52  ? 23.187  -14.319 29.783  1.00 67.61  ?  54  LYS A CA   1 
ATOM   362  C  C    . LYS A 1 52  ? 23.982  -15.360 28.968  1.00 64.10  ?  54  LYS A C    1 
ATOM   363  O  O    . LYS A 1 52  ? 25.018  -15.050 28.396  1.00 65.06  ?  54  LYS A O    1 
ATOM   364  C  CB   . LYS A 1 52  ? 21.987  -13.802 28.972  1.00 69.82  ?  54  LYS A CB   1 
ATOM   365  C  CG   . LYS A 1 52  ? 20.991  -13.011 29.808  1.00 74.78  ?  54  LYS A CG   1 
ATOM   366  C  CD   . LYS A 1 52  ? 20.061  -12.168 28.947  1.00 80.68  ?  54  LYS A CD   1 
ATOM   367  C  CE   . LYS A 1 52  ? 19.095  -11.336 29.778  1.00 86.42  ?  54  LYS A CE   1 
ATOM   368  N  NZ   . LYS A 1 52  ? 19.802  -10.394 30.703  1.00 89.95  ?  54  LYS A NZ   1 
ATOM   369  N  N    . THR A 1 53  ? 23.489  -16.589 28.902  1.00 60.69  ?  55  THR A N    1 
ATOM   370  C  CA   . THR A 1 53  ? 24.081  -17.666 28.083  1.00 58.38  ?  55  THR A CA   1 
ATOM   371  C  C    . THR A 1 53  ? 23.700  -17.492 26.554  1.00 55.88  ?  55  THR A C    1 
ATOM   372  O  O    . THR A 1 53  ? 22.830  -16.697 26.268  1.00 54.28  ?  55  THR A O    1 
ATOM   373  C  CB   . THR A 1 53  ? 23.570  -19.030 28.570  1.00 58.72  ?  55  THR A CB   1 
ATOM   374  O  OG1  . THR A 1 53  ? 22.211  -19.195 28.133  1.00 59.27  ?  55  THR A OG1  1 
ATOM   375  C  CG2  . THR A 1 53  ? 23.666  -19.189 30.117  1.00 58.76  ?  55  THR A CG2  1 
ATOM   376  N  N    . TRP A 1 54  ? 24.328  -18.227 25.628  1.00 55.41  ?  56  TRP A N    1 
ATOM   377  C  CA   . TRP A 1 54  ? 24.148  -17.967 24.184  1.00 56.31  ?  56  TRP A CA   1 
ATOM   378  C  C    . TRP A 1 54  ? 22.796  -18.522 23.706  1.00 54.59  ?  56  TRP A C    1 
ATOM   379  O  O    . TRP A 1 54  ? 22.192  -17.953 22.787  1.00 54.61  ?  56  TRP A O    1 
ATOM   380  C  CB   . TRP A 1 54  ? 25.321  -18.497 23.292  1.00 57.21  ?  56  TRP A CB   1 
ATOM   381  C  CG   . TRP A 1 54  ? 25.382  -19.991 23.114  1.00 58.86  ?  56  TRP A CG   1 
ATOM   382  C  CD1  . TRP A 1 54  ? 26.179  -20.870 23.791  1.00 60.13  ?  56  TRP A CD1  1 
ATOM   383  C  CD2  . TRP A 1 54  ? 24.630  -20.775 22.173  1.00 59.54  ?  56  TRP A CD2  1 
ATOM   384  N  NE1  . TRP A 1 54  ? 25.960  -22.153 23.338  1.00 60.79  ?  56  TRP A NE1  1 
ATOM   385  C  CE2  . TRP A 1 54  ? 25.004  -22.124 22.355  1.00 60.38  ?  56  TRP A CE2  1 
ATOM   386  C  CE3  . TRP A 1 54  ? 23.648  -20.472 21.218  1.00 60.34  ?  56  TRP A CE3  1 
ATOM   387  C  CZ2  . TRP A 1 54  ? 24.426  -23.162 21.629  1.00 61.26  ?  56  TRP A CZ2  1 
ATOM   388  C  CZ3  . TRP A 1 54  ? 23.049  -21.506 20.532  1.00 61.33  ?  56  TRP A CZ3  1 
ATOM   389  C  CH2  . TRP A 1 54  ? 23.446  -22.835 20.732  1.00 61.49  ?  56  TRP A CH2  1 
ATOM   390  N  N    . GLN A 1 55  ? 22.315  -19.623 24.315  1.00 52.50  ?  57  GLN A N    1 
ATOM   391  C  CA   . GLN A 1 55  ? 20.961  -20.091 24.045  1.00 50.22  ?  57  GLN A CA   1 
ATOM   392  C  C    . GLN A 1 55  ? 19.948  -19.000 24.493  1.00 46.42  ?  57  GLN A C    1 
ATOM   393  O  O    . GLN A 1 55  ? 19.008  -18.753 23.758  1.00 45.10  ?  57  GLN A O    1 
ATOM   394  C  CB   . GLN A 1 55  ? 20.643  -21.481 24.643  1.00 52.48  ?  57  GLN A CB   1 
ATOM   395  C  CG   . GLN A 1 55  ? 19.324  -22.082 24.038  1.00 60.89  ?  57  GLN A CG   1 
ATOM   396  C  CD   . GLN A 1 55  ? 18.893  -23.489 24.450  1.00 67.01  ?  57  GLN A CD   1 
ATOM   397  O  OE1  . GLN A 1 55  ? 19.191  -23.985 25.553  1.00 65.81  ?  57  GLN A OE1  1 
ATOM   398  N  NE2  . GLN A 1 55  ? 18.157  -24.159 23.538  1.00 69.47  ?  57  GLN A NE2  1 
ATOM   399  N  N    . ALA A 1 56  ? 20.173  -18.332 25.657  1.00 45.33  ?  58  ALA A N    1 
ATOM   400  C  CA   . ALA A 1 56  ? 19.351  -17.214 26.091  1.00 44.84  ?  58  ALA A CA   1 
ATOM   401  C  C    . ALA A 1 56  ? 19.473  -16.019 25.143  1.00 44.00  ?  58  ALA A C    1 
ATOM   402  O  O    . ALA A 1 56  ? 18.493  -15.299 24.949  1.00 44.01  ?  58  ALA A O    1 
ATOM   403  C  CB   . ALA A 1 56  ? 19.742  -16.778 27.482  1.00 46.20  ?  58  ALA A CB   1 
ATOM   404  N  N    . ASN A 1 57  ? 20.660  -15.789 24.571  1.00 43.61  ?  59  ASN A N    1 
ATOM   405  C  CA   . ASN A 1 57  ? 20.858  -14.583 23.759  1.00 44.52  ?  59  ASN A CA   1 
ATOM   406  C  C    . ASN A 1 57  ? 20.411  -14.732 22.301  1.00 43.61  ?  59  ASN A C    1 
ATOM   407  O  O    . ASN A 1 57  ? 20.321  -13.709 21.627  1.00 45.09  ?  59  ASN A O    1 
ATOM   408  C  CB   . ASN A 1 57  ? 22.296  -14.094 23.808  1.00 45.80  ?  59  ASN A CB   1 
ATOM   409  C  CG   . ASN A 1 57  ? 22.700  -13.501 25.129  1.00 49.88  ?  59  ASN A CG   1 
ATOM   410  O  OD1  . ASN A 1 57  ? 21.969  -12.700 25.759  1.00 50.10  ?  59  ASN A OD1  1 
ATOM   411  N  ND2  . ASN A 1 57  ? 23.877  -13.876 25.561  1.00 53.32  ?  59  ASN A ND2  1 
ATOM   412  N  N    . LEU A 1 58  ? 20.155  -15.951 21.802  1.00 40.95  ?  60  LEU A N    1 
ATOM   413  C  CA   . LEU A 1 58  ? 19.591  -16.123 20.466  1.00 38.00  ?  60  LEU A CA   1 
ATOM   414  C  C    . LEU A 1 58  ? 18.063  -16.008 20.576  1.00 36.21  ?  60  LEU A C    1 
ATOM   415  O  O    . LEU A 1 58  ? 17.413  -16.774 21.300  1.00 37.10  ?  60  LEU A O    1 
ATOM   416  C  CB   . LEU A 1 58  ? 19.975  -17.471 19.856  1.00 37.07  ?  60  LEU A CB   1 
ATOM   417  C  CG   . LEU A 1 58  ? 19.357  -17.772 18.464  1.00 37.03  ?  60  LEU A CG   1 
ATOM   418  C  CD1  . LEU A 1 58  ? 19.772  -16.740 17.422  1.00 38.05  ?  60  LEU A CD1  1 
ATOM   419  C  CD2  . LEU A 1 58  ? 19.725  -19.138 18.031  1.00 39.98  ?  60  LEU A CD2  1 
ATOM   420  N  N    . ARG A 1 59  ? 17.522  -15.049 19.884  1.00 33.88  ?  61  ARG A N    1 
ATOM   421  C  CA   . ARG A 1 59  ? 16.123  -14.646 19.923  1.00 35.38  ?  61  ARG A CA   1 
ATOM   422  C  C    . ARG A 1 59  ? 15.484  -14.581 18.532  1.00 35.32  ?  61  ARG A C    1 
ATOM   423  O  O    . ARG A 1 59  ? 16.120  -14.081 17.577  1.00 34.08  ?  61  ARG A O    1 
ATOM   424  C  CB   . ARG A 1 59  ? 16.011  -13.276 20.569  1.00 38.77  ?  61  ARG A CB   1 
ATOM   425  C  CG   . ARG A 1 59  ? 15.564  -13.309 22.027  1.00 49.69  ?  61  ARG A CG   1 
ATOM   426  C  CD   . ARG A 1 59  ? 14.895  -12.007 22.447  1.00 57.31  ?  61  ARG A CD   1 
ATOM   427  N  NE   . ARG A 1 59  ? 13.656  -11.778 21.688  1.00 63.61  ?  61  ARG A NE   1 
ATOM   428  C  CZ   . ARG A 1 59  ? 12.944  -10.653 21.729  1.00 68.49  ?  61  ARG A CZ   1 
ATOM   429  N  NH1  . ARG A 1 59  ? 13.328  -9.641  22.505  1.00 70.34  ?  61  ARG A NH1  1 
ATOM   430  N  NH2  . ARG A 1 59  ? 11.842  -10.532 20.998  1.00 68.28  ?  61  ARG A NH2  1 
ATOM   431  N  N    . LEU A 1 60  ? 14.249  -15.089 18.413  1.00 35.07  ?  62  LEU A N    1 
ATOM   432  C  CA   . LEU A 1 60  ? 13.406  -14.905 17.237  1.00 37.24  ?  62  LEU A CA   1 
ATOM   433  C  C    . LEU A 1 60  ? 12.571  -13.627 17.368  1.00 41.26  ?  62  LEU A C    1 
ATOM   434  O  O    . LEU A 1 60  ? 11.712  -13.546 18.247  1.00 44.52  ?  62  LEU A O    1 
ATOM   435  C  CB   . LEU A 1 60  ? 12.543  -16.146 16.973  1.00 37.42  ?  62  LEU A CB   1 
ATOM   436  C  CG   . LEU A 1 60  ? 11.885  -16.248 15.573  1.00 39.44  ?  62  LEU A CG   1 
ATOM   437  C  CD1  . LEU A 1 60  ? 11.676  -17.715 15.192  1.00 40.16  ?  62  LEU A CD1  1 
ATOM   438  C  CD2  . LEU A 1 60  ? 10.578  -15.532 15.576  1.00 40.97  ?  62  LEU A CD2  1 
ATOM   439  N  N    . ILE A 1 61  ? 12.833  -12.624 16.512  1.00 40.41  ?  63  ILE A N    1 
ATOM   440  C  CA   . ILE A 1 61  ? 12.273  -11.257 16.554  1.00 41.30  ?  63  ILE A CA   1 
ATOM   441  C  C    . ILE A 1 61  ? 10.857  -11.288 15.998  1.00 40.35  ?  63  ILE A C    1 
ATOM   442  O  O    . ILE A 1 61  ? 9.913   -10.885 16.681  1.00 40.12  ?  63  ILE A O    1 
ATOM   443  C  CB   . ILE A 1 61  ? 13.172  -10.243 15.786  1.00 43.89  ?  63  ILE A CB   1 
ATOM   444  C  CG1  . ILE A 1 61  ? 14.584  -10.132 16.405  1.00 46.42  ?  63  ILE A CG1  1 
ATOM   445  C  CG2  . ILE A 1 61  ? 12.503  -8.890  15.663  1.00 46.09  ?  63  ILE A CG2  1 
ATOM   446  C  CD1  . ILE A 1 61  ? 14.631  -9.918  17.963  1.00 50.51  ?  63  ILE A CD1  1 
ATOM   447  N  N    . SER A 1 62  ? 10.684  -11.773 14.755  1.00 38.73  ?  64  SER A N    1 
ATOM   448  C  CA   . SER A 1 62  ? 9.385   -11.753 14.115  1.00 39.46  ?  64  SER A CA   1 
ATOM   449  C  C    . SER A 1 62  ? 9.375   -12.680 12.869  1.00 36.36  ?  64  SER A C    1 
ATOM   450  O  O    . SER A 1 62  ? 10.423  -13.045 12.308  1.00 34.82  ?  64  SER A O    1 
ATOM   451  C  CB   . SER A 1 62  ? 9.018   -10.317 13.709  1.00 45.08  ?  64  SER A CB   1 
ATOM   452  O  OG   . SER A 1 62  ? 7.639   -10.197 13.400  1.00 52.87  ?  64  SER A OG   1 
ATOM   453  N  N    . LYS A 1 63  ? 8.181   -13.077 12.480  1.00 35.97  ?  65  LYS A N    1 
ATOM   454  C  CA   . LYS A 1 63  ? 7.977   -13.863 11.253  1.00 37.07  ?  65  LYS A CA   1 
ATOM   455  C  C    . LYS A 1 63  ? 7.051   -13.100 10.322  1.00 36.93  ?  65  LYS A C    1 
ATOM   456  O  O    . LYS A 1 63  ? 6.178   -12.380 10.789  1.00 38.17  ?  65  LYS A O    1 
ATOM   457  C  CB   . LYS A 1 63  ? 7.412   -15.239 11.570  1.00 36.92  ?  65  LYS A CB   1 
ATOM   458  C  CG   . LYS A 1 63  ? 8.252   -16.013 12.603  1.00 40.02  ?  65  LYS A CG   1 
ATOM   459  C  CD   . LYS A 1 63  ? 7.829   -17.451 12.656  1.00 41.32  ?  65  LYS A CD   1 
ATOM   460  C  CE   . LYS A 1 63  ? 8.650   -18.379 13.516  1.00 42.33  ?  65  LYS A CE   1 
ATOM   461  N  NZ   . LYS A 1 63  ? 8.106   -19.780 13.521  1.00 40.98  ?  65  LYS A NZ   1 
ATOM   462  N  N    . PHE A 1 64  ? 7.241   -13.243 8.989   1.00 34.16  ?  66  PHE A N    1 
ATOM   463  C  CA   . PHE A 1 64  ? 6.450   -12.540 8.013   1.00 32.87  ?  66  PHE A CA   1 
ATOM   464  C  C    . PHE A 1 64  ? 6.356   -13.391 6.739   1.00 32.79  ?  66  PHE A C    1 
ATOM   465  O  O    . PHE A 1 64  ? 7.217   -14.266 6.502   1.00 30.26  ?  66  PHE A O    1 
ATOM   466  C  CB   . PHE A 1 64  ? 7.025   -11.147 7.697   1.00 32.82  ?  66  PHE A CB   1 
ATOM   467  C  CG   . PHE A 1 64  ? 8.452   -11.139 7.145   1.00 32.25  ?  66  PHE A CG   1 
ATOM   468  C  CD1  . PHE A 1 64  ? 9.537   -11.067 7.997   1.00 32.16  ?  66  PHE A CD1  1 
ATOM   469  C  CD2  . PHE A 1 64  ? 8.694   -11.328 5.799   1.00 31.83  ?  66  PHE A CD2  1 
ATOM   470  C  CE1  . PHE A 1 64  ? 10.827  -11.113 7.517   1.00 31.51  ?  66  PHE A CE1  1 
ATOM   471  C  CE2  . PHE A 1 64  ? 10.003  -11.376 5.315   1.00 31.88  ?  66  PHE A CE2  1 
ATOM   472  C  CZ   . PHE A 1 64  ? 11.054  -11.289 6.188   1.00 29.94  ?  66  PHE A CZ   1 
ATOM   473  N  N    . ASP A 1 65  ? 5.299   -13.136 5.941   1.00 32.98  ?  67  ASP A N    1 
ATOM   474  C  CA   . ASP A 1 65  ? 5.086   -13.840 4.663   1.00 33.96  ?  67  ASP A CA   1 
ATOM   475  C  C    . ASP A 1 65  ? 4.480   -13.003 3.548   1.00 32.42  ?  67  ASP A C    1 
ATOM   476  O  O    . ASP A 1 65  ? 3.971   -13.568 2.569   1.00 32.84  ?  67  ASP A O    1 
ATOM   477  C  CB   . ASP A 1 65  ? 4.266   -15.098 4.855   1.00 35.86  ?  67  ASP A CB   1 
ATOM   478  C  CG   . ASP A 1 65  ? 2.903   -14.856 5.478   1.00 41.60  ?  67  ASP A CG   1 
ATOM   479  O  OD1  . ASP A 1 65  ? 2.364   -13.720 5.345   1.00 40.84  ?  67  ASP A OD1  1 
ATOM   480  O  OD2  . ASP A 1 65  ? 2.384   -15.774 6.111   1.00 47.22  ?  67  ASP A OD2  1 
ATOM   481  N  N    . THR A 1 66  ? 4.575   -11.687 3.656   1.00 33.14  ?  68  THR A N    1 
ATOM   482  C  CA   . THR A 1 66  ? 4.314   -10.780 2.547   1.00 35.16  ?  68  THR A CA   1 
ATOM   483  C  C    . THR A 1 66  ? 5.437   -9.727  2.431   1.00 34.60  ?  68  THR A C    1 
ATOM   484  O  O    . THR A 1 66  ? 6.142   -9.472  3.407   1.00 35.54  ?  68  THR A O    1 
ATOM   485  C  CB   . THR A 1 66  ? 2.945   -10.039 2.733   1.00 38.05  ?  68  THR A CB   1 
ATOM   486  O  OG1  . THR A 1 66  ? 3.093   -9.097  3.791   1.00 40.08  ?  68  THR A OG1  1 
ATOM   487  C  CG2  . THR A 1 66  ? 1.779   -11.005 3.064   1.00 37.31  ?  68  THR A CG2  1 
ATOM   488  N  N    . VAL A 1 67  ? 5.541   -9.111  1.264   1.00 33.40  ?  69  VAL A N    1 
ATOM   489  C  CA   . VAL A 1 67  ? 6.508   -8.059  0.931   1.00 35.13  ?  69  VAL A CA   1 
ATOM   490  C  C    . VAL A 1 67  ? 6.346   -6.875  1.901   1.00 35.55  ?  69  VAL A C    1 
ATOM   491  O  O    . VAL A 1 67  ? 7.342   -6.346  2.417   1.00 34.72  ?  69  VAL A O    1 
ATOM   492  C  CB   . VAL A 1 67  ? 6.406   -7.572  -0.539  1.00 33.32  ?  69  VAL A CB   1 
ATOM   493  C  CG1  . VAL A 1 67  ? 7.385   -6.456  -0.788  1.00 34.43  ?  69  VAL A CG1  1 
ATOM   494  C  CG2  . VAL A 1 67  ? 6.615   -8.709  -1.544  1.00 33.15  ?  69  VAL A CG2  1 
ATOM   495  N  N    . GLU A 1 68  ? 5.089   -6.476  2.161   1.00 35.25  ?  70  GLU A N    1 
ATOM   496  C  CA   . GLU A 1 68  ? 4.792   -5.290  2.952   1.00 35.02  ?  70  GLU A CA   1 
ATOM   497  C  C    . GLU A 1 68  ? 5.124   -5.521  4.433   1.00 35.34  ?  70  GLU A C    1 
ATOM   498  O  O    . GLU A 1 68  ? 5.582   -4.581  5.109   1.00 35.46  ?  70  GLU A O    1 
ATOM   499  C  CB   . GLU A 1 68  ? 3.323   -4.833  2.775   1.00 36.63  ?  70  GLU A CB   1 
ATOM   500  C  CG   . GLU A 1 68  ? 3.007   -4.237  1.403   1.00 40.65  ?  70  GLU A CG   1 
ATOM   501  C  CD   . GLU A 1 68  ? 2.875   -5.201  0.237   1.00 43.80  ?  70  GLU A CD   1 
ATOM   502  O  OE1  . GLU A 1 68  ? 2.820   -6.436  0.454   1.00 40.86  ?  70  GLU A OE1  1 
ATOM   503  O  OE2  . GLU A 1 68  ? 2.823   -4.710  -0.912  1.00 46.29  ?  70  GLU A OE2  1 
ATOM   504  N  N    . ASP A 1 69  ? 4.900   -6.736  4.944   1.00 34.23  ?  71  ASP A N    1 
ATOM   505  C  CA   . ASP A 1 69  ? 5.299   -7.082  6.305   1.00 34.23  ?  71  ASP A CA   1 
ATOM   506  C  C    . ASP A 1 69  ? 6.825   -7.124  6.435   1.00 34.00  ?  71  ASP A C    1 
ATOM   507  O  O    . ASP A 1 69  ? 7.366   -6.725  7.473   1.00 34.64  ?  71  ASP A O    1 
ATOM   508  C  CB   . ASP A 1 69  ? 4.630   -8.391  6.745   1.00 36.94  ?  71  ASP A CB   1 
ATOM   509  C  CG   . ASP A 1 69  ? 3.092   -8.204  6.816   1.00 43.28  ?  71  ASP A CG   1 
ATOM   510  O  OD1  . ASP A 1 69  ? 2.650   -7.089  7.160   1.00 41.59  ?  71  ASP A OD1  1 
ATOM   511  O  OD2  . ASP A 1 69  ? 2.357   -9.171  6.497   1.00 45.55  ?  71  ASP A OD2  1 
ATOM   512  N  N    . PHE A 1 70  ? 7.523   -7.567  5.372   1.00 32.28  ?  72  PHE A N    1 
ATOM   513  C  CA   . PHE A 1 70  ? 8.989   -7.501  5.319   1.00 31.06  ?  72  PHE A CA   1 
ATOM   514  C  C    . PHE A 1 70  ? 9.466   -6.059  5.519   1.00 30.77  ?  72  PHE A C    1 
ATOM   515  O  O    . PHE A 1 70  ? 10.290  -5.813  6.391   1.00 31.47  ?  72  PHE A O    1 
ATOM   516  C  CB   . PHE A 1 70  ? 9.538   -8.075  3.990   1.00 29.21  ?  72  PHE A CB   1 
ATOM   517  C  CG   . PHE A 1 70  ? 10.971  -7.639  3.775   1.00 31.31  ?  72  PHE A CG   1 
ATOM   518  C  CD1  . PHE A 1 70  ? 12.007  -8.208  4.516   1.00 32.17  ?  72  PHE A CD1  1 
ATOM   519  C  CD2  . PHE A 1 70  ? 11.282  -6.635  2.869   1.00 31.41  ?  72  PHE A CD2  1 
ATOM   520  C  CE1  . PHE A 1 70  ? 13.326  -7.766  4.352   1.00 31.99  ?  72  PHE A CE1  1 
ATOM   521  C  CE2  . PHE A 1 70  ? 12.614  -6.222  2.680   1.00 31.84  ?  72  PHE A CE2  1 
ATOM   522  C  CZ   . PHE A 1 70  ? 13.616  -6.786  3.425   1.00 32.14  ?  72  PHE A CZ   1 
ATOM   523  N  N    . TRP A 1 71  ? 8.953   -5.111  4.691   1.00 31.25  ?  73  TRP A N    1 
ATOM   524  C  CA   . TRP A 1 71  ? 9.383   -3.744  4.761   1.00 33.01  ?  73  TRP A CA   1 
ATOM   525  C  C    . TRP A 1 71  ? 9.072   -3.097  6.107   1.00 35.04  ?  73  TRP A C    1 
ATOM   526  O  O    . TRP A 1 71  ? 9.887   -2.342  6.573   1.00 35.89  ?  73  TRP A O    1 
ATOM   527  C  CB   . TRP A 1 71  ? 8.834   -2.914  3.632   1.00 32.61  ?  73  TRP A CB   1 
ATOM   528  C  CG   . TRP A 1 71  ? 9.481   -3.177  2.308   1.00 32.55  ?  73  TRP A CG   1 
ATOM   529  C  CD1  . TRP A 1 71  ? 8.860   -3.589  1.170   1.00 33.06  ?  73  TRP A CD1  1 
ATOM   530  C  CD2  . TRP A 1 71  ? 10.865  -2.980  1.961   1.00 31.81  ?  73  TRP A CD2  1 
ATOM   531  N  NE1  . TRP A 1 71  ? 9.757   -3.695  0.156   1.00 32.34  ?  73  TRP A NE1  1 
ATOM   532  C  CE2  . TRP A 1 71  ? 10.996  -3.287  0.604   1.00 31.88  ?  73  TRP A CE2  1 
ATOM   533  C  CE3  . TRP A 1 71  ? 12.006  -2.584  2.672   1.00 32.70  ?  73  TRP A CE3  1 
ATOM   534  C  CZ2  . TRP A 1 71  ? 12.228  -3.220  -0.059  1.00 31.61  ?  73  TRP A CZ2  1 
ATOM   535  C  CZ3  . TRP A 1 71  ? 13.220  -2.478  2.000   1.00 32.02  ?  73  TRP A CZ3  1 
ATOM   536  C  CH2  . TRP A 1 71  ? 13.319  -2.791  0.651   1.00 31.16  ?  73  TRP A CH2  1 
ATOM   537  N  N    . ALA A 1 72  ? 7.926   -3.386  6.721   1.00 36.66  ?  74  ALA A N    1 
ATOM   538  C  CA   . ALA A 1 72  ? 7.564   -2.798  8.007   1.00 39.02  ?  74  ALA A CA   1 
ATOM   539  C  C    . ALA A 1 72  ? 8.535   -3.283  9.078   1.00 38.16  ?  74  ALA A C    1 
ATOM   540  O  O    . ALA A 1 72  ? 8.958   -2.498  9.921   1.00 37.92  ?  74  ALA A O    1 
ATOM   541  C  CB   . ALA A 1 72  ? 6.131   -3.171  8.386   1.00 39.88  ?  74  ALA A CB   1 
ATOM   542  N  N    . LEU A 1 73  ? 8.903   -4.577  9.046   1.00 37.78  ?  75  LEU A N    1 
ATOM   543  C  CA   . LEU A 1 73  ? 9.920   -5.094  9.950   1.00 36.48  ?  75  LEU A CA   1 
ATOM   544  C  C    . LEU A 1 73  ? 11.296  -4.473  9.690   1.00 35.15  ?  75  LEU A C    1 
ATOM   545  O  O    . LEU A 1 73  ? 11.936  -4.006  10.628  1.00 34.01  ?  75  LEU A O    1 
ATOM   546  C  CB   . LEU A 1 73  ? 9.969   -6.610  9.897   1.00 36.71  ?  75  LEU A CB   1 
ATOM   547  C  CG   . LEU A 1 73  ? 10.997  -7.301  10.811  1.00 38.99  ?  75  LEU A CG   1 
ATOM   548  C  CD1  . LEU A 1 73  ? 10.790  -6.936  12.284  1.00 40.40  ?  75  LEU A CD1  1 
ATOM   549  C  CD2  . LEU A 1 73  ? 10.931  -8.839  10.638  1.00 38.28  ?  75  LEU A CD2  1 
ATOM   550  N  N    . TYR A 1 74  ? 11.755  -4.474  8.422   1.00 35.56  ?  76  TYR A N    1 
ATOM   551  C  CA   . TYR A 1 74  ? 13.058  -3.940  8.036   1.00 36.53  ?  76  TYR A CA   1 
ATOM   552  C  C    . TYR A 1 74  ? 13.178  -2.473  8.451   1.00 38.37  ?  76  TYR A C    1 
ATOM   553  O  O    . TYR A 1 74  ? 14.174  -2.085  9.033   1.00 38.37  ?  76  TYR A O    1 
ATOM   554  C  CB   . TYR A 1 74  ? 13.268  -4.097  6.531   1.00 36.35  ?  76  TYR A CB   1 
ATOM   555  C  CG   . TYR A 1 74  ? 14.562  -3.491  6.009   1.00 36.22  ?  76  TYR A CG   1 
ATOM   556  C  CD1  . TYR A 1 74  ? 15.725  -4.247  5.932   1.00 37.38  ?  76  TYR A CD1  1 
ATOM   557  C  CD2  . TYR A 1 74  ? 14.619  -2.158  5.600   1.00 36.56  ?  76  TYR A CD2  1 
ATOM   558  C  CE1  . TYR A 1 74  ? 16.921  -3.693  5.463   1.00 37.46  ?  76  TYR A CE1  1 
ATOM   559  C  CE2  . TYR A 1 74  ? 15.800  -1.600  5.128   1.00 37.77  ?  76  TYR A CE2  1 
ATOM   560  C  CZ   . TYR A 1 74  ? 16.953  -2.370  5.064   1.00 38.83  ?  76  TYR A CZ   1 
ATOM   561  O  OH   . TYR A 1 74  ? 18.152  -1.867  4.584   1.00 42.36  ?  76  TYR A OH   1 
ATOM   562  N  N    . ASN A 1 75  ? 12.159  -1.683  8.164   1.00 41.02  ?  77  ASN A N    1 
ATOM   563  C  CA   . ASN A 1 75  ? 12.133  -0.241  8.505   1.00 44.76  ?  77  ASN A CA   1 
ATOM   564  C  C    . ASN A 1 75  ? 12.211  -0.027  10.027  1.00 45.62  ?  77  ASN A C    1 
ATOM   565  O  O    . ASN A 1 75  ? 12.936  0.860   10.474  1.00 46.10  ?  77  ASN A O    1 
ATOM   566  C  CB   . ASN A 1 75  ? 10.853  0.411   7.950   1.00 48.17  ?  77  ASN A CB   1 
ATOM   567  C  CG   . ASN A 1 75  ? 10.788  0.534   6.438   1.00 55.86  ?  77  ASN A CG   1 
ATOM   568  O  OD1  . ASN A 1 75  ? 11.789  0.482   5.716   1.00 57.75  ?  77  ASN A OD1  1 
ATOM   569  N  ND2  . ASN A 1 75  ? 9.576   0.723   5.911   1.00 59.44  ?  77  ASN A ND2  1 
ATOM   570  N  N    . HIS A 1 76  ? 11.496  -0.841  10.789  1.00 46.16  ?  78  HIS A N    1 
ATOM   571  C  CA   . HIS A 1 76  ? 11.478  -0.786  12.257  1.00 47.85  ?  78  HIS A CA   1 
ATOM   572  C  C    . HIS A 1 76  ? 12.839  -1.092  12.871  1.00 46.70  ?  78  HIS A C    1 
ATOM   573  O  O    . HIS A 1 76  ? 13.283  -0.364  13.755  1.00 44.99  ?  78  HIS A O    1 
ATOM   574  C  CB   . HIS A 1 76  ? 10.424  -1.750  12.819  1.00 50.88  ?  78  HIS A CB   1 
ATOM   575  C  CG   . HIS A 1 76  ? 10.360  -1.743  14.309  1.00 59.18  ?  78  HIS A CG   1 
ATOM   576  N  ND1  . HIS A 1 76  ? 10.636  -2.880  15.052  1.00 63.11  ?  78  HIS A ND1  1 
ATOM   577  C  CD2  . HIS A 1 76  ? 10.060  -0.727  15.154  1.00 62.49  ?  78  HIS A CD2  1 
ATOM   578  C  CE1  . HIS A 1 76  ? 10.487  -2.522  16.321  1.00 64.31  ?  78  HIS A CE1  1 
ATOM   579  N  NE2  . HIS A 1 76  ? 10.142  -1.238  16.428  1.00 64.35  ?  78  HIS A NE2  1 
ATOM   580  N  N    . ILE A 1 77  ? 13.518  -2.168  12.399  1.00 46.47  ?  79  ILE A N    1 
ATOM   581  C  CA   . ILE A 1 77  ? 14.859  -2.556  12.880  1.00 48.22  ?  79  ILE A CA   1 
ATOM   582  C  C    . ILE A 1 77  ? 15.921  -1.529  12.454  1.00 51.42  ?  79  ILE A C    1 
ATOM   583  O  O    . ILE A 1 77  ? 16.849  -1.217  13.210  1.00 50.90  ?  79  ILE A O    1 
ATOM   584  C  CB   . ILE A 1 77  ? 15.234  -3.965  12.312  1.00 48.43  ?  79  ILE A CB   1 
ATOM   585  C  CG1  . ILE A 1 77  ? 14.273  -5.069  12.808  1.00 48.97  ?  79  ILE A CG1  1 
ATOM   586  C  CG2  . ILE A 1 77  ? 16.695  -4.293  12.595  1.00 48.50  ?  79  ILE A CG2  1 
ATOM   587  C  CD1  . ILE A 1 77  ? 13.918  -5.053  14.337  1.00 51.55  ?  79  ILE A CD1  1 
ATOM   588  N  N    . GLN A 1 78  ? 15.793  -1.040  11.245  1.00 54.41  ?  80  GLN A N    1 
ATOM   589  C  CA   . GLN A 1 78  ? 16.755  -0.091  10.690  1.00 59.00  ?  80  GLN A CA   1 
ATOM   590  C  C    . GLN A 1 78  ? 16.745  1.220   11.508  1.00 64.26  ?  80  GLN A C    1 
ATOM   591  O  O    . GLN A 1 78  ? 17.824  1.721   11.843  1.00 65.06  ?  80  GLN A O    1 
ATOM   592  C  CB   . GLN A 1 78  ? 16.445  0.146   9.192   1.00 60.85  ?  80  GLN A CB   1 
ATOM   593  C  CG   . GLN A 1 78  ? 17.603  0.687   8.367   1.00 64.39  ?  80  GLN A CG   1 
ATOM   594  C  CD   . GLN A 1 78  ? 17.182  1.129   6.979   1.00 64.99  ?  80  GLN A CD   1 
ATOM   595  O  OE1  . GLN A 1 78  ? 16.011  1.481   6.733   1.00 62.85  ?  80  GLN A OE1  1 
ATOM   596  N  NE2  . GLN A 1 78  ? 18.150  1.109   6.039   1.00 66.45  ?  80  GLN A NE2  1 
ATOM   597  N  N    . LEU A 1 79  ? 15.528  1.759   11.823  1.00 67.07  ?  81  LEU A N    1 
ATOM   598  C  CA   . LEU A 1 79  ? 15.301  2.871   12.767  1.00 70.67  ?  81  LEU A CA   1 
ATOM   599  C  C    . LEU A 1 79  ? 15.879  2.626   14.172  1.00 73.47  ?  81  LEU A C    1 
ATOM   600  O  O    . LEU A 1 79  ? 16.463  3.541   14.774  1.00 74.09  ?  81  LEU A O    1 
ATOM   601  C  CB   . LEU A 1 79  ? 13.780  3.121   12.989  1.00 71.48  ?  81  LEU A CB   1 
ATOM   602  C  CG   . LEU A 1 79  ? 13.028  4.083   12.117  1.00 74.02  ?  81  LEU A CG   1 
ATOM   603  C  CD1  . LEU A 1 79  ? 11.644  4.317   12.701  1.00 74.56  ?  81  LEU A CD1  1 
ATOM   604  C  CD2  . LEU A 1 79  ? 13.732  5.412   12.029  1.00 75.97  ?  81  LEU A CD2  1 
ATOM   605  N  N    . SER A 1 80  ? 15.682  1.407   14.701  1.00 74.27  ?  82  SER A N    1 
ATOM   606  C  CA   . SER A 1 80  ? 16.029  1.057   16.076  1.00 75.24  ?  82  SER A CA   1 
ATOM   607  C  C    . SER A 1 80  ? 17.437  0.492   16.221  1.00 77.12  ?  82  SER A C    1 
ATOM   608  O  O    . SER A 1 80  ? 17.772  0.005   17.300  1.00 77.46  ?  82  SER A O    1 
ATOM   609  C  CB   . SER A 1 80  ? 15.025  0.039   16.608  1.00 75.35  ?  82  SER A CB   1 
ATOM   610  O  OG   . SER A 1 80  ? 13.702  0.513   16.426  1.00 76.91  ?  82  SER A OG   1 
ATOM   611  N  N    . SER A 1 81  ? 18.264  0.574   15.167  1.00 78.51  ?  83  SER A N    1 
ATOM   612  C  CA   . SER A 1 81  ? 19.479  -0.219  15.039  1.00 80.80  ?  83  SER A CA   1 
ATOM   613  C  C    . SER A 1 81  ? 20.543  0.146   16.073  1.00 82.43  ?  83  SER A C    1 
ATOM   614  O  O    . SER A 1 81  ? 21.033  1.277   16.095  1.00 82.82  ?  83  SER A O    1 
ATOM   615  C  CB   . SER A 1 81  ? 20.079  -0.058  13.644  1.00 82.65  ?  83  SER A CB   1 
ATOM   616  O  OG   . SER A 1 81  ? 21.312  -0.760  13.535  1.00 85.32  ?  83  SER A OG   1 
ATOM   617  N  N    . ASN A 1 82  ? 20.896  -0.828  16.911  1.00 83.09  ?  84  ASN A N    1 
ATOM   618  C  CA   . ASN A 1 82  ? 22.030  -0.721  17.806  1.00 84.38  ?  84  ASN A CA   1 
ATOM   619  C  C    . ASN A 1 82  ? 23.335  -1.036  16.988  1.00 84.90  ?  84  ASN A C    1 
ATOM   620  O  O    . ASN A 1 82  ? 24.331  -0.323  17.141  1.00 85.72  ?  84  ASN A O    1 
ATOM   621  C  CB   . ASN A 1 82  ? 21.817  -1.646  19.033  1.00 86.01  ?  84  ASN A CB   1 
ATOM   622  C  CG   . ASN A 1 82  ? 20.522  -1.403  19.797  1.00 89.05  ?  84  ASN A CG   1 
ATOM   623  O  OD1  . ASN A 1 82  ? 20.492  -0.677  20.808  1.00 88.96  ?  84  ASN A OD1  1 
ATOM   624  N  ND2  . ASN A 1 82  ? 19.424  -2.011  19.336  1.00 90.26  ?  84  ASN A ND2  1 
ATOM   625  N  N    . LEU A 1 83  ? 23.322  -2.074  16.112  1.00 84.30  ?  85  LEU A N    1 
ATOM   626  C  CA   . LEU A 1 83  ? 24.470  -2.408  15.229  1.00 83.89  ?  85  LEU A CA   1 
ATOM   627  C  C    . LEU A 1 83  ? 25.723  -2.682  16.073  1.00 82.43  ?  85  LEU A C    1 
ATOM   628  O  O    . LEU A 1 83  ? 26.829  -2.234  15.749  1.00 82.48  ?  85  LEU A O    1 
ATOM   629  C  CB   . LEU A 1 83  ? 24.756  -1.266  14.221  1.00 84.44  ?  85  LEU A CB   1 
ATOM   630  C  CG   . LEU A 1 83  ? 25.805  -1.562  13.132  1.00 86.20  ?  85  LEU A CG   1 
ATOM   631  C  CD1  . LEU A 1 83  ? 25.168  -2.244  11.950  1.00 86.90  ?  85  LEU A CD1  1 
ATOM   632  C  CD2  . LEU A 1 83  ? 26.542  -0.285  12.710  1.00 86.83  ?  85  LEU A CD2  1 
ATOM   633  N  N    . MET A 1 84  ? 25.538  -3.430  17.148  1.00 80.65  ?  86  MET A N    1 
ATOM   634  C  CA   . MET A 1 84  ? 26.548  -3.540  18.170  1.00 79.31  ?  86  MET A CA   1 
ATOM   635  C  C    . MET A 1 84  ? 27.526  -4.634  17.821  1.00 76.54  ?  86  MET A C    1 
ATOM   636  O  O    . MET A 1 84  ? 27.127  -5.639  17.248  1.00 76.62  ?  86  MET A O    1 
ATOM   637  C  CB   . MET A 1 84  ? 25.880  -3.770  19.528  1.00 80.93  ?  86  MET A CB   1 
ATOM   638  C  CG   . MET A 1 84  ? 24.993  -2.610  19.914  1.00 85.77  ?  86  MET A CG   1 
ATOM   639  S  SD   . MET A 1 84  ? 25.918  -1.184  20.591  1.00 96.12  ?  86  MET A SD   1 
ATOM   640  C  CE   . MET A 1 84  ? 24.702  0.090   20.455  1.00 91.61  ?  86  MET A CE   1 
ATOM   641  N  N    . PRO A 1 85  ? 28.821  -4.468  18.151  1.00 74.36  ?  87  PRO A N    1 
ATOM   642  C  CA   . PRO A 1 85  ? 29.777  -5.557  17.881  1.00 72.39  ?  87  PRO A CA   1 
ATOM   643  C  C    . PRO A 1 85  ? 29.400  -6.802  18.687  1.00 69.24  ?  87  PRO A C    1 
ATOM   644  O  O    . PRO A 1 85  ? 28.938  -6.679  19.818  1.00 69.13  ?  87  PRO A O    1 
ATOM   645  C  CB   . PRO A 1 85  ? 31.135  -4.971  18.290  1.00 73.76  ?  87  PRO A CB   1 
ATOM   646  C  CG   . PRO A 1 85  ? 30.811  -3.816  19.215  1.00 74.74  ?  87  PRO A CG   1 
ATOM   647  C  CD   . PRO A 1 85  ? 29.468  -3.298  18.794  1.00 73.50  ?  87  PRO A CD   1 
ATOM   648  N  N    . GLY A 1 86  ? 29.584  -7.973  18.087  1.00 66.28  ?  88  GLY A N    1 
ATOM   649  C  CA   . GLY A 1 86  ? 29.095  -9.234  18.631  1.00 63.51  ?  88  GLY A CA   1 
ATOM   650  C  C    . GLY A 1 86  ? 27.668  -9.608  18.256  1.00 60.06  ?  88  GLY A C    1 
ATOM   651  O  O    . GLY A 1 86  ? 27.253  -10.746 18.529  1.00 61.13  ?  88  GLY A O    1 
ATOM   652  N  N    A CYS A 1 87  ? 26.896  -8.701  17.631  0.50 57.95  ?  89  CYS A N    1 
ATOM   653  N  N    B CYS A 1 87  ? 26.907  -8.675  17.640  0.50 57.78  ?  89  CYS A N    1 
ATOM   654  C  CA   A CYS A 1 87  ? 25.487  -8.999  17.324  0.50 56.37  ?  89  CYS A CA   1 
ATOM   655  C  CA   B CYS A 1 87  ? 25.528  -8.988  17.241  0.50 56.02  ?  89  CYS A CA   1 
ATOM   656  C  C    A CYS A 1 87  ? 25.316  -9.546  15.896  0.50 53.60  ?  89  CYS A C    1 
ATOM   657  C  C    B CYS A 1 87  ? 25.536  -9.859  15.964  0.50 53.20  ?  89  CYS A C    1 
ATOM   658  O  O    A CYS A 1 87  ? 25.991  -9.106  14.962  0.50 53.20  ?  89  CYS A O    1 
ATOM   659  O  O    B CYS A 1 87  ? 26.526  -9.941  15.219  0.50 52.08  ?  89  CYS A O    1 
ATOM   660  C  CB   A CYS A 1 87  ? 24.608  -7.779  17.575  0.50 57.55  ?  89  CYS A CB   1 
ATOM   661  C  CB   B CYS A 1 87  ? 24.660  -7.725  17.086  0.50 56.87  ?  89  CYS A CB   1 
ATOM   662  S  SG   A CYS A 1 87  ? 24.623  -7.224  19.294  0.50 62.11  ?  89  CYS A SG   1 
ATOM   663  S  SG   B CYS A 1 87  ? 24.456  -7.118  15.376  0.50 59.54  ?  89  CYS A SG   1 
ATOM   664  N  N    . ASP A 1 88  ? 24.422  -10.523 15.753  1.00 51.15  ?  90  ASP A N    1 
ATOM   665  C  CA   . ASP A 1 88  ? 24.110  -11.143 14.496  1.00 45.92  ?  90  ASP A CA   1 
ATOM   666  C  C    . ASP A 1 88  ? 22.622  -10.837 14.258  1.00 38.78  ?  90  ASP A C    1 
ATOM   667  O  O    . ASP A 1 88  ? 21.787  -10.735 15.183  1.00 38.27  ?  90  ASP A O    1 
ATOM   668  C  CB   . ASP A 1 88  ? 24.247  -12.672 14.525  1.00 49.62  ?  90  ASP A CB   1 
ATOM   669  C  CG   . ASP A 1 88  ? 25.553  -13.285 14.955  1.00 59.55  ?  90  ASP A CG   1 
ATOM   670  O  OD1  . ASP A 1 88  ? 26.612  -12.605 14.810  1.00 61.19  ?  90  ASP A OD1  1 
ATOM   671  O  OD2  . ASP A 1 88  ? 25.530  -14.471 15.428  1.00 62.59  ?  90  ASP A OD2  1 
ATOM   672  N  N    . TYR A 1 89  ? 22.307  -10.729 13.021  1.00 31.51  ?  91  TYR A N    1 
ATOM   673  C  CA   . TYR A 1 89  ? 20.954  -10.904 12.572  1.00 29.17  ?  91  TYR A CA   1 
ATOM   674  C  C    . TYR A 1 89  ? 20.982  -12.035 11.567  1.00 26.34  ?  91  TYR A C    1 
ATOM   675  O  O    . TYR A 1 89  ? 21.991  -12.193 10.845  1.00 24.18  ?  91  TYR A O    1 
ATOM   676  C  CB   . TYR A 1 89  ? 20.369  -9.657  11.910  1.00 29.66  ?  91  TYR A CB   1 
ATOM   677  C  CG   . TYR A 1 89  ? 20.094  -8.514  12.869  1.00 34.99  ?  91  TYR A CG   1 
ATOM   678  C  CD1  . TYR A 1 89  ? 21.098  -7.629  13.224  1.00 38.57  ?  91  TYR A CD1  1 
ATOM   679  C  CD2  . TYR A 1 89  ? 18.825  -8.312  13.402  1.00 37.23  ?  91  TYR A CD2  1 
ATOM   680  C  CE1  . TYR A 1 89  ? 20.846  -6.554  14.070  1.00 41.49  ?  91  TYR A CE1  1 
ATOM   681  C  CE2  . TYR A 1 89  ? 18.561  -7.244  14.253  1.00 40.13  ?  91  TYR A CE2  1 
ATOM   682  C  CZ   . TYR A 1 89  ? 19.576  -6.356  14.569  1.00 43.27  ?  91  TYR A CZ   1 
ATOM   683  O  OH   . TYR A 1 89  ? 19.356  -5.288  15.421  1.00 49.09  ?  91  TYR A OH   1 
ATOM   684  N  N    . SER A 1 90  ? 19.902  -12.763 11.513  1.00 24.23  ?  92  SER A N    1 
ATOM   685  C  CA   . SER A 1 90  ? 19.711  -13.854 10.558  1.00 24.08  ?  92  SER A CA   1 
ATOM   686  C  C    . SER A 1 90  ? 18.281  -13.833 10.034  1.00 23.77  ?  92  SER A C    1 
ATOM   687  O  O    . SER A 1 90  ? 17.339  -13.597 10.815  1.00 26.02  ?  92  SER A O    1 
ATOM   688  C  CB   . SER A 1 90  ? 20.033  -15.200 11.205  1.00 24.97  ?  92  SER A CB   1 
ATOM   689  O  OG   . SER A 1 90  ? 21.348  -15.239 11.705  1.00 33.31  ?  92  SER A OG   1 
ATOM   690  N  N    . LEU A 1 91  ? 18.089  -14.093 8.752   1.00 21.54  ?  93  LEU A N    1 
ATOM   691  C  CA   . LEU A 1 91  ? 16.797  -14.279 8.186   1.00 21.10  ?  93  LEU A CA   1 
ATOM   692  C  C    . LEU A 1 91  ? 16.732  -15.674 7.616   1.00 22.21  ?  93  LEU A C    1 
ATOM   693  O  O    . LEU A 1 91  ? 17.466  -15.971 6.663   1.00 22.17  ?  93  LEU A O    1 
ATOM   694  C  CB   . LEU A 1 91  ? 16.503  -13.287 7.052   1.00 21.71  ?  93  LEU A CB   1 
ATOM   695  C  CG   . LEU A 1 91  ? 15.027  -13.378 6.543   1.00 25.29  ?  93  LEU A CG   1 
ATOM   696  C  CD1  . LEU A 1 91  ? 14.106  -12.660 7.498   1.00 27.46  ?  93  LEU A CD1  1 
ATOM   697  C  CD2  . LEU A 1 91  ? 14.870  -12.842 5.163   1.00 28.27  ?  93  LEU A CD2  1 
ATOM   698  N  N    . PHE A 1 92  ? 15.900  -16.549 8.214   1.00 20.88  ?  94  PHE A N    1 
ATOM   699  C  CA   . PHE A 1 92  ? 15.787  -17.951 7.772   1.00 21.85  ?  94  PHE A CA   1 
ATOM   700  C  C    . PHE A 1 92  ? 14.392  -18.350 7.415   1.00 23.78  ?  94  PHE A C    1 
ATOM   701  O  O    . PHE A 1 92  ? 13.414  -17.812 7.962   1.00 25.82  ?  94  PHE A O    1 
ATOM   702  C  CB   . PHE A 1 92  ? 16.389  -18.921 8.822   1.00 21.98  ?  94  PHE A CB   1 
ATOM   703  C  CG   . PHE A 1 92  ? 17.860  -19.101 8.685   1.00 23.19  ?  94  PHE A CG   1 
ATOM   704  C  CD1  . PHE A 1 92  ? 18.739  -18.055 8.982   1.00 25.65  ?  94  PHE A CD1  1 
ATOM   705  C  CD2  . PHE A 1 92  ? 18.392  -20.302 8.234   1.00 24.52  ?  94  PHE A CD2  1 
ATOM   706  C  CE1  . PHE A 1 92  ? 20.089  -18.201 8.760   1.00 25.82  ?  94  PHE A CE1  1 
ATOM   707  C  CE2  . PHE A 1 92  ? 19.757  -20.450 8.060   1.00 25.84  ?  94  PHE A CE2  1 
ATOM   708  C  CZ   . PHE A 1 92  ? 20.594  -19.406 8.334   1.00 26.74  ?  94  PHE A CZ   1 
ATOM   709  N  N    . LYS A 1 93  ? 14.264  -19.314 6.516   1.00 23.61  ?  95  LYS A N    1 
ATOM   710  C  CA   . LYS A 1 93  ? 12.960  -19.872 6.208   1.00 24.55  ?  95  LYS A CA   1 
ATOM   711  C  C    . LYS A 1 93  ? 12.312  -20.434 7.506   1.00 24.91  ?  95  LYS A C    1 
ATOM   712  O  O    . LYS A 1 93  ? 13.000  -20.961 8.379   1.00 24.05  ?  95  LYS A O    1 
ATOM   713  C  CB   . LYS A 1 93  ? 13.009  -20.951 5.128   1.00 24.87  ?  95  LYS A CB   1 
ATOM   714  C  CG   . LYS A 1 93  ? 13.347  -20.407 3.762   1.00 24.75  ?  95  LYS A CG   1 
ATOM   715  C  CD   . LYS A 1 93  ? 13.442  -21.484 2.825   1.00 27.28  ?  95  LYS A CD   1 
ATOM   716  C  CE   . LYS A 1 93  ? 13.643  -20.908 1.451   1.00 30.89  ?  95  LYS A CE   1 
ATOM   717  N  NZ   . LYS A 1 93  ? 13.932  -21.973 0.510   1.00 30.17  ?  95  LYS A NZ   1 
ATOM   718  N  N    . ASP A 1 94  ? 11.012  -20.265 7.615   1.00 26.27  ?  96  ASP A N    1 
ATOM   719  C  CA   . ASP A 1 94  ? 10.247  -20.702 8.802   1.00 27.79  ?  96  ASP A CA   1 
ATOM   720  C  C    . ASP A 1 94  ? 10.544  -22.190 9.070   1.00 29.94  ?  96  ASP A C    1 
ATOM   721  O  O    . ASP A 1 94  ? 10.492  -22.994 8.136   1.00 30.49  ?  96  ASP A O    1 
ATOM   722  C  CB   . ASP A 1 94  ? 8.745   -20.415 8.578   1.00 29.14  ?  96  ASP A CB   1 
ATOM   723  C  CG   . ASP A 1 94  ? 7.883   -20.450 9.823   1.00 40.01  ?  96  ASP A CG   1 
ATOM   724  O  OD1  . ASP A 1 94  ? 8.442   -20.416 10.915  1.00 40.24  ?  96  ASP A OD1  1 
ATOM   725  O  OD2  . ASP A 1 94  ? 6.639   -20.504 9.690   1.00 42.59  ?  96  ASP A OD2  1 
ATOM   726  N  N    . GLY A 1 95  ? 10.893  -22.532 10.330  1.00 31.81  ?  97  GLY A N    1 
ATOM   727  C  CA   . GLY A 1 95  ? 11.247  -23.911 10.665  1.00 33.55  ?  97  GLY A CA   1 
ATOM   728  C  C    . GLY A 1 95  ? 12.711  -24.257 10.560  1.00 35.43  ?  97  GLY A C    1 
ATOM   729  O  O    . GLY A 1 95  ? 13.071  -25.397 10.820  1.00 38.62  ?  97  GLY A O    1 
ATOM   730  N  N    . ILE A 1 96  ? 13.572  -23.317 10.156  1.00 31.87  ?  98  ILE A N    1 
ATOM   731  C  CA   . ILE A 1 96  ? 15.019  -23.551 10.167  1.00 30.03  ?  98  ILE A CA   1 
ATOM   732  C  C    . ILE A 1 96  ? 15.665  -22.645 11.189  1.00 29.66  ?  98  ILE A C    1 
ATOM   733  O  O    . ILE A 1 96  ? 15.522  -21.428 11.106  1.00 28.53  ?  98  ILE A O    1 
ATOM   734  C  CB   . ILE A 1 96  ? 15.676  -23.322 8.790   1.00 29.28  ?  98  ILE A CB   1 
ATOM   735  C  CG1  . ILE A 1 96  ? 15.009  -24.122 7.687   1.00 28.41  ?  98  ILE A CG1  1 
ATOM   736  C  CG2  . ILE A 1 96  ? 17.186  -23.615 8.868   1.00 29.05  ?  98  ILE A CG2  1 
ATOM   737  C  CD1  . ILE A 1 96  ? 15.582  -23.916 6.253   1.00 29.20  ?  98  ILE A CD1  1 
ATOM   738  N  N    . GLU A 1 97  ? 16.387  -23.228 12.168  1.00 29.88  ?  99  GLU A N    1 
ATOM   739  C  CA   . GLU A 1 97  ? 17.147  -22.442 13.109  1.00 29.75  ?  99  GLU A CA   1 
ATOM   740  C  C    . GLU A 1 97  ? 18.466  -21.963 12.467  1.00 30.57  ?  99  GLU A C    1 
ATOM   741  O  O    . GLU A 1 97  ? 19.041  -22.705 11.663  1.00 29.68  ?  99  GLU A O    1 
ATOM   742  C  CB   . GLU A 1 97  ? 17.432  -23.224 14.369  1.00 32.86  ?  99  GLU A CB   1 
ATOM   743  C  CG   . GLU A 1 97  ? 16.159  -23.639 15.073  1.00 39.73  ?  99  GLU A CG   1 
ATOM   744  C  CD   . GLU A 1 97  ? 16.417  -24.169 16.484  1.00 50.26  ?  99  GLU A CD   1 
ATOM   745  O  OE1  . GLU A 1 97  ? 17.539  -24.646 16.764  1.00 51.63  ?  99  GLU A OE1  1 
ATOM   746  O  OE2  . GLU A 1 97  ? 15.484  -24.093 17.303  1.00 51.55  ?  99  GLU A OE2  1 
ATOM   747  N  N    . PRO A 1 98  ? 18.920  -20.741 12.790  1.00 30.35  ?  100 PRO A N    1 
ATOM   748  C  CA   . PRO A 1 98  ? 20.146  -20.208 12.190  1.00 32.06  ?  100 PRO A CA   1 
ATOM   749  C  C    . PRO A 1 98  ? 21.420  -20.778 12.854  1.00 32.20  ?  100 PRO A C    1 
ATOM   750  O  O    . PRO A 1 98  ? 22.283  -20.035 13.288  1.00 32.89  ?  100 PRO A O    1 
ATOM   751  C  CB   . PRO A 1 98  ? 19.959  -18.690 12.378  1.00 31.86  ?  100 PRO A CB   1 
ATOM   752  C  CG   . PRO A 1 98  ? 19.187  -18.537 13.622  1.00 31.30  ?  100 PRO A CG   1 
ATOM   753  C  CD   . PRO A 1 98  ? 18.304  -19.744 13.702  1.00 31.00  ?  100 PRO A CD   1 
ATOM   754  N  N    . MET A 1 99  ? 21.509  -22.104 12.929  1.00 32.20  ?  101 MET A N    1 
ATOM   755  C  CA   . MET A 1 99  ? 22.568  -22.870 13.572  1.00 34.74  ?  101 MET A CA   1 
ATOM   756  C  C    . MET A 1 99  ? 22.920  -24.040 12.621  1.00 33.54  ?  101 MET A C    1 
ATOM   757  O  O    . MET A 1 99  ? 22.036  -24.676 12.070  1.00 30.55  ?  101 MET A O    1 
ATOM   758  C  CB   . MET A 1 99  ? 22.069  -23.458 14.921  1.00 37.87  ?  101 MET A CB   1 
ATOM   759  C  CG   . MET A 1 99  ? 21.567  -22.418 15.917  1.00 48.02  ?  101 MET A CG   1 
ATOM   760  S  SD   . MET A 1 99  ? 22.859  -21.268 16.544  1.00 69.51  ?  101 MET A SD   1 
ATOM   761  C  CE   . MET A 1 99  ? 23.896  -22.439 17.419  1.00 68.90  ?  101 MET A CE   1 
ATOM   762  N  N    . TRP A 1 100 ? 24.202  -24.290 12.444  1.00 35.62  ?  102 TRP A N    1 
ATOM   763  C  CA   . TRP A 1 100 ? 24.642  -25.208 11.392  1.00 38.65  ?  102 TRP A CA   1 
ATOM   764  C  C    . TRP A 1 100 ? 24.227  -26.641 11.705  1.00 39.17  ?  102 TRP A C    1 
ATOM   765  O  O    . TRP A 1 100 ? 24.129  -27.414 10.768  1.00 38.18  ?  102 TRP A O    1 
ATOM   766  C  CB   . TRP A 1 100 ? 26.144  -25.051 11.084  1.00 40.03  ?  102 TRP A CB   1 
ATOM   767  C  CG   . TRP A 1 100 ? 27.080  -25.835 11.981  1.00 42.47  ?  102 TRP A CG   1 
ATOM   768  C  CD1  . TRP A 1 100 ? 27.642  -25.407 13.151  1.00 43.95  ?  102 TRP A CD1  1 
ATOM   769  C  CD2  . TRP A 1 100 ? 27.631  -27.150 11.724  1.00 42.47  ?  102 TRP A CD2  1 
ATOM   770  N  NE1  . TRP A 1 100 ? 28.491  -26.374 13.648  1.00 44.77  ?  102 TRP A NE1  1 
ATOM   771  C  CE2  . TRP A 1 100 ? 28.499  -27.455 12.790  1.00 44.11  ?  102 TRP A CE2  1 
ATOM   772  C  CE3  . TRP A 1 100 ? 27.471  -28.091 10.690  1.00 43.05  ?  102 TRP A CE3  1 
ATOM   773  C  CZ2  . TRP A 1 100 ? 29.175  -28.677 12.880  1.00 44.24  ?  102 TRP A CZ2  1 
ATOM   774  C  CZ3  . TRP A 1 100 ? 28.164  -29.289 10.765  1.00 44.35  ?  102 TRP A CZ3  1 
ATOM   775  C  CH2  . TRP A 1 100 ? 29.006  -29.570 11.855  1.00 44.40  ?  102 TRP A CH2  1 
ATOM   776  N  N    . GLU A 1 101 ? 23.970  -26.987 12.990  1.00 39.25  ?  103 GLU A N    1 
ATOM   777  C  CA   . GLU A 1 101 ? 23.528  -28.286 13.424  1.00 40.17  ?  103 GLU A CA   1 
ATOM   778  C  C    . GLU A 1 101 ? 22.085  -28.566 13.093  1.00 38.07  ?  103 GLU A C    1 
ATOM   779  O  O    . GLU A 1 101 ? 21.706  -29.740 13.155  1.00 36.40  ?  103 GLU A O    1 
ATOM   780  C  CB   . GLU A 1 101 ? 23.758  -28.476 14.946  1.00 42.66  ?  103 GLU A CB   1 
ATOM   781  C  CG   . GLU A 1 101 ? 25.208  -28.297 15.346  1.00 50.10  ?  103 GLU A CG   1 
ATOM   782  C  CD   . GLU A 1 101 ? 25.639  -26.919 15.838  1.00 59.93  ?  103 GLU A CD   1 
ATOM   783  O  OE1  . GLU A 1 101 ? 26.721  -26.873 16.477  1.00 64.34  ?  103 GLU A OE1  1 
ATOM   784  O  OE2  . GLU A 1 101 ? 24.929  -25.903 15.599  1.00 54.19  ?  103 GLU A OE2  1 
ATOM   785  N  N    . ASP A 1 102 ? 21.243  -27.535 12.710  1.00 34.38  ?  104 ASP A N    1 
ATOM   786  C  CA   . ASP A 1 102 ? 19.868  -27.783 12.236  1.00 32.35  ?  104 ASP A CA   1 
ATOM   787  C  C    . ASP A 1 102 ? 19.892  -28.815 11.080  1.00 33.64  ?  104 ASP A C    1 
ATOM   788  O  O    . ASP A 1 102 ? 20.821  -28.822 10.266  1.00 33.64  ?  104 ASP A O    1 
ATOM   789  C  CB   . ASP A 1 102 ? 19.204  -26.474 11.776  1.00 33.06  ?  104 ASP A CB   1 
ATOM   790  C  CG   . ASP A 1 102 ? 17.730  -26.583 11.463  1.00 35.48  ?  104 ASP A CG   1 
ATOM   791  O  OD1  . ASP A 1 102 ? 17.366  -27.215 10.404  1.00 34.01  ?  104 ASP A OD1  1 
ATOM   792  O  OD2  . ASP A 1 102 ? 16.925  -26.051 12.249  1.00 36.51  ?  104 ASP A OD2  1 
ATOM   793  N  N    . GLU A 1 103 ? 18.895  -29.683 11.033  1.00 34.74  ?  105 GLU A N    1 
ATOM   794  C  CA   . GLU A 1 103 ? 18.764  -30.745 10.014  1.00 35.66  ?  105 GLU A CA   1 
ATOM   795  C  C    . GLU A 1 103 ? 18.923  -30.164 8.574   1.00 34.34  ?  105 GLU A C    1 
ATOM   796  O  O    . GLU A 1 103 ? 19.550  -30.782 7.726   1.00 34.53  ?  105 GLU A O    1 
ATOM   797  C  CB   . GLU A 1 103 ? 17.398  -31.433 10.178  1.00 41.07  ?  105 GLU A CB   1 
ATOM   798  C  CG   . GLU A 1 103 ? 17.132  -32.608 9.267   1.00 54.14  ?  105 GLU A CG   1 
ATOM   799  C  CD   . GLU A 1 103 ? 17.491  -33.940 9.912   1.00 70.26  ?  105 GLU A CD   1 
ATOM   800  O  OE1  . GLU A 1 103 ? 18.606  -34.049 10.478  1.00 72.49  ?  105 GLU A OE1  1 
ATOM   801  O  OE2  . GLU A 1 103 ? 16.651  -34.873 9.857   1.00 74.67  ?  105 GLU A OE2  1 
ATOM   802  N  N    . LYS A 1 104 ? 18.353  -28.975 8.336   1.00 33.23  ?  106 LYS A N    1 
ATOM   803  C  CA   . LYS A 1 104 ? 18.418  -28.301 7.038   1.00 31.05  ?  106 LYS A CA   1 
ATOM   804  C  C    . LYS A 1 104 ? 19.729  -27.593 6.766   1.00 29.44  ?  106 LYS A C    1 
ATOM   805  O  O    . LYS A 1 104 ? 19.947  -27.179 5.616   1.00 29.69  ?  106 LYS A O    1 
ATOM   806  C  CB   . LYS A 1 104 ? 17.227  -27.308 6.848   1.00 34.39  ?  106 LYS A CB   1 
ATOM   807  C  CG   . LYS A 1 104 ? 15.867  -27.960 6.833   1.00 38.74  ?  106 LYS A CG   1 
ATOM   808  C  CD   . LYS A 1 104 ? 15.626  -28.802 5.609   1.00 47.80  ?  106 LYS A CD   1 
ATOM   809  C  CE   . LYS A 1 104 ? 14.242  -29.437 5.615   1.00 56.79  ?  106 LYS A CE   1 
ATOM   810  N  NZ   . LYS A 1 104 ? 13.260  -28.610 4.866   1.00 62.66  ?  106 LYS A NZ   1 
ATOM   811  N  N    . ASN A 1 105 ? 20.608  -27.435 7.748   1.00 29.02  ?  107 ASN A N    1 
ATOM   812  C  CA   . ASN A 1 105 ? 21.917  -26.812 7.602   1.00 28.97  ?  107 ASN A CA   1 
ATOM   813  C  C    . ASN A 1 105 ? 23.094  -27.769 7.680   1.00 30.15  ?  107 ASN A C    1 
ATOM   814  O  O    . ASN A 1 105 ? 24.157  -27.449 7.111   1.00 30.91  ?  107 ASN A O    1 
ATOM   815  C  CB   . ASN A 1 105 ? 22.116  -25.700 8.626   1.00 27.38  ?  107 ASN A CB   1 
ATOM   816  C  CG   . ASN A 1 105 ? 21.099  -24.572 8.462   1.00 26.74  ?  107 ASN A CG   1 
ATOM   817  O  OD1  . ASN A 1 105 ? 20.720  -24.203 7.361   1.00 28.06  ?  107 ASN A OD1  1 
ATOM   818  N  ND2  . ASN A 1 105 ? 20.647  -24.016 9.540   1.00 26.43  ?  107 ASN A ND2  1 
ATOM   819  N  N    . LYS A 1 106 ? 22.948  -28.900 8.368   1.00 31.10  ?  108 LYS A N    1 
ATOM   820  C  CA   . LYS A 1 106 ? 24.113  -29.728 8.693   1.00 33.94  ?  108 LYS A CA   1 
ATOM   821  C  C    . LYS A 1 106 ? 24.868  -30.233 7.488   1.00 34.10  ?  108 LYS A C    1 
ATOM   822  O  O    . LYS A 1 106 ? 26.090  -30.345 7.551   1.00 35.56  ?  108 LYS A O    1 
ATOM   823  C  CB   . LYS A 1 106 ? 23.755  -30.886 9.656   1.00 37.56  ?  108 LYS A CB   1 
ATOM   824  C  CG   . LYS A 1 106 ? 22.792  -31.894 9.111   1.00 46.42  ?  108 LYS A CG   1 
ATOM   825  C  CD   . LYS A 1 106 ? 22.336  -32.845 10.236  1.00 53.40  ?  108 LYS A CD   1 
ATOM   826  C  CE   . LYS A 1 106 ? 21.717  -34.097 9.701   1.00 60.08  ?  108 LYS A CE   1 
ATOM   827  N  NZ   . LYS A 1 106 ? 21.467  -35.076 10.801  1.00 65.13  ?  108 LYS A NZ   1 
ATOM   828  N  N    . ARG A 1 107 ? 24.183  -30.516 6.401   1.00 33.49  ?  109 ARG A N    1 
ATOM   829  C  CA   . ARG A 1 107 ? 24.822  -30.946 5.163   1.00 34.61  ?  109 ARG A CA   1 
ATOM   830  C  C    . ARG A 1 107 ? 25.140  -29.827 4.191   1.00 32.78  ?  109 ARG A C    1 
ATOM   831  O  O    . ARG A 1 107 ? 25.530  -30.090 3.046   1.00 33.44  ?  109 ARG A O    1 
ATOM   832  C  CB   . ARG A 1 107 ? 23.943  -32.032 4.492   1.00 38.15  ?  109 ARG A CB   1 
ATOM   833  C  CG   . ARG A 1 107 ? 23.652  -33.300 5.345   1.00 46.08  ?  109 ARG A CG   1 
ATOM   834  C  CD   . ARG A 1 107 ? 24.907  -33.851 6.022   1.00 55.28  ?  109 ARG A CD   1 
ATOM   835  N  NE   . ARG A 1 107 ? 24.958  -35.314 6.131   1.00 63.60  ?  109 ARG A NE   1 
ATOM   836  C  CZ   . ARG A 1 107 ? 25.790  -35.992 6.922   1.00 66.59  ?  109 ARG A CZ   1 
ATOM   837  N  NH1  . ARG A 1 107 ? 25.761  -37.314 6.943   1.00 68.17  ?  109 ARG A NH1  1 
ATOM   838  N  NH2  . ARG A 1 107 ? 26.649  -35.348 7.709   1.00 66.08  ?  109 ARG A NH2  1 
ATOM   839  N  N    . GLY A 1 108 ? 24.998  -28.591 4.632   1.00 31.21  ?  110 GLY A N    1 
ATOM   840  C  CA   . GLY A 1 108 ? 25.076  -27.458 3.777   1.00 30.88  ?  110 GLY A CA   1 
ATOM   841  C  C    . GLY A 1 108 ? 26.340  -26.680 3.975   1.00 31.03  ?  110 GLY A C    1 
ATOM   842  O  O    . GLY A 1 108 ? 27.344  -27.199 4.460   1.00 31.27  ?  110 GLY A O    1 
ATOM   843  N  N    . GLY A 1 109 ? 26.251  -25.422 3.582   1.00 29.09  ?  111 GLY A N    1 
ATOM   844  C  CA   . GLY A 1 109 ? 27.330  -24.466 3.632   1.00 28.98  ?  111 GLY A CA   1 
ATOM   845  C  C    . GLY A 1 109 ? 26.825  -23.060 3.316   1.00 28.76  ?  111 GLY A C    1 
ATOM   846  O  O    . GLY A 1 109 ? 25.605  -22.797 3.333   1.00 28.01  ?  111 GLY A O    1 
ATOM   847  N  N    . ARG A 1 110 ? 27.759  -22.168 3.019   1.00 26.84  ?  112 ARG A N    1 
ATOM   848  C  CA   . ARG A 1 110 ? 27.460  -20.745 2.880   1.00 26.73  ?  112 ARG A CA   1 
ATOM   849  C  C    . ARG A 1 110 ? 28.335  -20.121 1.838   1.00 28.03  ?  112 ARG A C    1 
ATOM   850  O  O    . ARG A 1 110 ? 29.527  -20.467 1.759   1.00 31.18  ?  112 ARG A O    1 
ATOM   851  C  CB   . ARG A 1 110 ? 27.588  -20.019 4.217   1.00 25.45  ?  112 ARG A CB   1 
ATOM   852  C  CG   . ARG A 1 110 ? 29.002  -19.996 4.767   1.00 31.55  ?  112 ARG A CG   1 
ATOM   853  C  CD   . ARG A 1 110 ? 29.093  -19.355 6.136   1.00 36.76  ?  112 ARG A CD   1 
ATOM   854  N  NE   . ARG A 1 110 ? 30.493  -19.261 6.565   1.00 43.51  ?  112 ARG A NE   1 
ATOM   855  C  CZ   . ARG A 1 110 ? 30.922  -18.564 7.617   1.00 44.72  ?  112 ARG A CZ   1 
ATOM   856  N  NH1  . ARG A 1 110 ? 32.216  -18.553 7.932   1.00 46.56  ?  112 ARG A NH1  1 
ATOM   857  N  NH2  . ARG A 1 110 ? 30.066  -17.881 8.363   1.00 42.28  ?  112 ARG A NH2  1 
ATOM   858  N  N    . TRP A 1 111 ? 27.752  -19.234 1.041   1.00 26.68  ?  113 TRP A N    1 
ATOM   859  C  CA   . TRP A 1 111 ? 28.427  -18.221 0.234   1.00 25.82  ?  113 TRP A CA   1 
ATOM   860  C  C    . TRP A 1 111 ? 28.747  -17.022 1.107   1.00 27.18  ?  113 TRP A C    1 
ATOM   861  O  O    . TRP A 1 111 ? 27.800  -16.385 1.625   1.00 27.28  ?  113 TRP A O    1 
ATOM   862  C  CB   . TRP A 1 111 ? 27.572  -17.783 -0.932  1.00 27.11  ?  113 TRP A CB   1 
ATOM   863  C  CG   . TRP A 1 111 ? 27.550  -18.759 -2.061  1.00 28.09  ?  113 TRP A CG   1 
ATOM   864  C  CD1  . TRP A 1 111 ? 26.513  -19.529 -2.459  1.00 28.32  ?  113 TRP A CD1  1 
ATOM   865  C  CD2  . TRP A 1 111 ? 28.648  -19.081 -2.925  1.00 29.94  ?  113 TRP A CD2  1 
ATOM   866  N  NE1  . TRP A 1 111 ? 26.889  -20.316 -3.533  1.00 29.45  ?  113 TRP A NE1  1 
ATOM   867  C  CE2  . TRP A 1 111 ? 28.194  -20.052 -3.839  1.00 30.55  ?  113 TRP A CE2  1 
ATOM   868  C  CE3  . TRP A 1 111 ? 29.952  -18.592 -3.053  1.00 31.38  ?  113 TRP A CE3  1 
ATOM   869  C  CZ2  . TRP A 1 111 ? 29.004  -20.560 -4.859  1.00 32.75  ?  113 TRP A CZ2  1 
ATOM   870  C  CZ3  . TRP A 1 111 ? 30.759  -19.115 -4.049  1.00 33.15  ?  113 TRP A CZ3  1 
ATOM   871  C  CH2  . TRP A 1 111 ? 30.293  -20.097 -4.927  1.00 33.11  ?  113 TRP A CH2  1 
ATOM   872  N  N    . LEU A 1 112 ? 30.036  -16.710 1.285   1.00 28.61  ?  114 LEU A N    1 
ATOM   873  C  CA   . LEU A 1 112 ? 30.488  -15.738 2.305   1.00 32.70  ?  114 LEU A CA   1 
ATOM   874  C  C    . LEU A 1 112 ? 31.102  -14.516 1.680   1.00 34.05  ?  114 LEU A C    1 
ATOM   875  O  O    . LEU A 1 112 ? 31.955  -14.627 0.789   1.00 31.65  ?  114 LEU A O    1 
ATOM   876  C  CB   . LEU A 1 112 ? 31.498  -16.402 3.245   1.00 35.62  ?  114 LEU A CB   1 
ATOM   877  C  CG   . LEU A 1 112 ? 32.217  -15.507 4.296   1.00 39.88  ?  114 LEU A CG   1 
ATOM   878  C  CD1  . LEU A 1 112 ? 31.275  -15.048 5.383   1.00 41.88  ?  114 LEU A CD1  1 
ATOM   879  C  CD2  . LEU A 1 112 ? 33.389  -16.283 4.939   1.00 42.05  ?  114 LEU A CD2  1 
ATOM   880  N  N    . ILE A 1 113 ? 30.679  -13.340 2.160   1.00 34.62  ?  115 ILE A N    1 
ATOM   881  C  CA   . ILE A 1 113 ? 31.194  -12.012 1.799   1.00 37.62  ?  115 ILE A CA   1 
ATOM   882  C  C    . ILE A 1 113 ? 31.853  -11.470 3.080   1.00 35.40  ?  115 ILE A C    1 
ATOM   883  O  O    . ILE A 1 113 ? 31.168  -11.377 4.079   1.00 31.43  ?  115 ILE A O    1 
ATOM   884  C  CB   . ILE A 1 113 ? 30.016  -11.036 1.348   1.00 42.31  ?  115 ILE A CB   1 
ATOM   885  C  CG1  . ILE A 1 113 ? 28.960  -11.725 0.451   1.00 45.28  ?  115 ILE A CG1  1 
ATOM   886  C  CG2  . ILE A 1 113 ? 30.559  -9.784  0.695   1.00 46.04  ?  115 ILE A CG2  1 
ATOM   887  C  CD1  . ILE A 1 113 ? 29.472  -12.275 -0.860  1.00 48.33  ?  115 ILE A CD1  1 
ATOM   888  N  N    . THR A 1 114 ? 33.172  -11.115 3.114   1.00 36.85  ?  116 THR A N    1 
ATOM   889  C  CA   . THR A 1 114 ? 33.732  -10.449 4.331   1.00 40.70  ?  116 THR A CA   1 
ATOM   890  C  C    . THR A 1 114 ? 34.054  -9.015  4.020   1.00 42.70  ?  116 THR A C    1 
ATOM   891  O  O    . THR A 1 114 ? 34.646  -8.736  2.988   1.00 42.77  ?  116 THR A O    1 
ATOM   892  C  CB   . THR A 1 114 ? 34.992  -11.114 4.948   1.00 45.68  ?  116 THR A CB   1 
ATOM   893  O  OG1  . THR A 1 114 ? 34.799  -12.535 5.103   1.00 48.93  ?  116 THR A OG1  1 
ATOM   894  C  CG2  . THR A 1 114 ? 35.332  -10.494 6.340   1.00 47.67  ?  116 THR A CG2  1 
ATOM   895  N  N    . LEU A 1 115 ? 33.675  -8.132  4.894   1.00 43.52  ?  117 LEU A N    1 
ATOM   896  C  CA   . LEU A 1 115 ? 33.842  -6.710  4.739   1.00 46.42  ?  117 LEU A CA   1 
ATOM   897  C  C    . LEU A 1 115 ? 34.843  -6.189  5.805   1.00 49.73  ?  117 LEU A C    1 
ATOM   898  O  O    . LEU A 1 115 ? 34.749  -6.593  6.972   1.00 50.14  ?  117 LEU A O    1 
ATOM   899  C  CB   . LEU A 1 115 ? 32.472  -6.011  4.910   1.00 46.24  ?  117 LEU A CB   1 
ATOM   900  C  CG   . LEU A 1 115 ? 31.382  -6.214  3.843   1.00 47.63  ?  117 LEU A CG   1 
ATOM   901  C  CD1  . LEU A 1 115 ? 30.215  -5.242  4.069   1.00 47.51  ?  117 LEU A CD1  1 
ATOM   902  C  CD2  . LEU A 1 115 ? 31.904  -5.996  2.474   1.00 49.12  ?  117 LEU A CD2  1 
ATOM   903  N  N    . ASN A 1 116 ? 35.796  -5.304  5.412   1.00 51.52  ?  118 ASN A N    1 
ATOM   904  C  CA   . ASN A 1 116 ? 36.726  -4.676  6.362   1.00 54.80  ?  118 ASN A CA   1 
ATOM   905  C  C    . ASN A 1 116 ? 36.009  -3.568  7.160   1.00 56.85  ?  118 ASN A C    1 
ATOM   906  O  O    . ASN A 1 116 ? 35.031  -3.007  6.683   1.00 56.51  ?  118 ASN A O    1 
ATOM   907  C  CB   . ASN A 1 116 ? 37.956  -4.116  5.637   1.00 58.44  ?  118 ASN A CB   1 
ATOM   908  C  CG   . ASN A 1 116 ? 39.230  -4.001  6.483   1.00 65.99  ?  118 ASN A CG   1 
ATOM   909  O  OD1  . ASN A 1 116 ? 39.222  -3.604  7.665   1.00 67.27  ?  118 ASN A OD1  1 
ATOM   910  N  ND2  . ASN A 1 116 ? 40.376  -4.349  5.883   1.00 68.41  ?  118 ASN A ND2  1 
ATOM   911  N  N    . LYS A 1 117 ? 36.495  -3.281  8.380   1.00 58.62  ?  119 LYS A N    1 
ATOM   912  C  CA   . LYS A 1 117 ? 36.024  -2.203  9.266   1.00 60.98  ?  119 LYS A CA   1 
ATOM   913  C  C    . LYS A 1 117 ? 35.432  -0.951  8.562   1.00 61.27  ?  119 LYS A C    1 
ATOM   914  O  O    . LYS A 1 117 ? 34.345  -0.541  8.929   1.00 62.02  ?  119 LYS A O    1 
ATOM   915  C  CB   . LYS A 1 117 ? 37.187  -1.716  10.168  1.00 65.26  ?  119 LYS A CB   1 
ATOM   916  C  CG   . LYS A 1 117 ? 37.615  -2.671  11.284  1.00 72.20  ?  119 LYS A CG   1 
ATOM   917  C  CD   . LYS A 1 117 ? 38.742  -2.030  12.135  1.00 78.67  ?  119 LYS A CD   1 
ATOM   918  C  CE   . LYS A 1 117 ? 39.293  -2.968  13.190  1.00 83.37  ?  119 LYS A CE   1 
ATOM   919  N  NZ   . LYS A 1 117 ? 40.223  -3.973  12.613  1.00 86.82  ?  119 LYS A NZ   1 
ATOM   920  N  N    . GLN A 1 118 ? 36.130  -0.349  7.575   1.00 60.72  ?  120 GLN A N    1 
ATOM   921  C  CA   . GLN A 1 118 ? 35.655  0.891   6.918   1.00 60.90  ?  120 GLN A CA   1 
ATOM   922  C  C    . GLN A 1 118 ? 34.476  0.629   5.955   1.00 59.35  ?  120 GLN A C    1 
ATOM   923  O  O    . GLN A 1 118 ? 33.620  1.499   5.766   1.00 59.36  ?  120 GLN A O    1 
ATOM   924  C  CB   . GLN A 1 118 ? 36.807  1.620   6.204   1.00 64.16  ?  120 GLN A CB   1 
ATOM   925  C  CG   . GLN A 1 118 ? 36.372  2.951   5.565   1.00 72.28  ?  120 GLN A CG   1 
ATOM   926  C  CD   . GLN A 1 118 ? 37.378  4.082   5.643   1.00 78.94  ?  120 GLN A CD   1 
ATOM   927  O  OE1  . GLN A 1 118 ? 38.597  3.893   5.810   1.00 80.54  ?  120 GLN A OE1  1 
ATOM   928  N  NE2  . GLN A 1 118 ? 36.873  5.302   5.518   1.00 80.58  ?  120 GLN A NE2  1 
ATOM   929  N  N    . GLN A 1 119 ? 34.417  -0.577  5.362   1.00 57.10  ?  121 GLN A N    1 
ATOM   930  C  CA   . GLN A 1 119 ? 33.246  -0.976  4.583   1.00 54.98  ?  121 GLN A CA   1 
ATOM   931  C  C    . GLN A 1 119 ? 31.978  -1.077  5.398   1.00 53.46  ?  121 GLN A C    1 
ATOM   932  O  O    . GLN A 1 119 ? 30.936  -1.229  4.786   1.00 52.32  ?  121 GLN A O    1 
ATOM   933  C  CB   . GLN A 1 119 ? 33.497  -2.288  3.842   1.00 55.04  ?  121 GLN A CB   1 
ATOM   934  C  CG   . GLN A 1 119 ? 34.615  -2.158  2.855   1.00 55.17  ?  121 GLN A CG   1 
ATOM   935  C  CD   . GLN A 1 119 ? 34.847  -3.433  2.165   1.00 52.64  ?  121 GLN A CD   1 
ATOM   936  O  OE1  . GLN A 1 119 ? 35.438  -4.351  2.720   1.00 51.39  ?  121 GLN A OE1  1 
ATOM   937  N  NE2  . GLN A 1 119 ? 34.396  -3.534  0.944   1.00 53.90  ?  121 GLN A NE2  1 
ATOM   938  N  N    . ARG A 1 120 ? 32.037  -0.993  6.750   1.00 53.33  ?  122 ARG A N    1 
ATOM   939  C  CA   . ARG A 1 120 ? 30.844  -0.993  7.587   1.00 54.74  ?  122 ARG A CA   1 
ATOM   940  C  C    . ARG A 1 120 ? 29.946  0.222   7.225   1.00 55.25  ?  122 ARG A C    1 
ATOM   941  O  O    . ARG A 1 120 ? 28.722  0.105   7.106   1.00 55.21  ?  122 ARG A O    1 
ATOM   942  C  CB   . ARG A 1 120 ? 31.234  -0.906  9.075   1.00 58.06  ?  122 ARG A CB   1 
ATOM   943  C  CG   . ARG A 1 120 ? 30.096  -1.236  10.025  1.00 64.61  ?  122 ARG A CG   1 
ATOM   944  C  CD   . ARG A 1 120 ? 30.591  -1.496  11.431  1.00 71.30  ?  122 ARG A CD   1 
ATOM   945  N  NE   . ARG A 1 120 ? 31.188  -0.282  12.009  1.00 78.08  ?  122 ARG A NE   1 
ATOM   946  C  CZ   . ARG A 1 120 ? 31.683  -0.198  13.242  1.00 81.99  ?  122 ARG A CZ   1 
ATOM   947  N  NH1  . ARG A 1 120 ? 32.205  0.946   13.679  1.00 80.42  ?  122 ARG A NH1  1 
ATOM   948  N  NH2  . ARG A 1 120 ? 31.659  -1.259  14.052  1.00 83.21  ?  122 ARG A NH2  1 
ATOM   949  N  N    . ARG A 1 121 ? 30.585  1.389   7.063   1.00 54.96  ?  123 ARG A N    1 
ATOM   950  C  CA   . ARG A 1 121 ? 29.907  2.588   6.629   1.00 54.55  ?  123 ARG A CA   1 
ATOM   951  C  C    . ARG A 1 121 ? 29.501  2.499   5.151   1.00 53.14  ?  123 ARG A C    1 
ATOM   952  O  O    . ARG A 1 121 ? 28.366  2.843   4.851   1.00 54.88  ?  123 ARG A O    1 
ATOM   953  C  CB   . ARG A 1 121 ? 30.794  3.831   6.855   1.00 57.25  ?  123 ARG A CB   1 
ATOM   954  C  CG   . ARG A 1 121 ? 30.736  4.450   8.291   1.00 63.18  ?  123 ARG A CG   1 
ATOM   955  C  CD   . ARG A 1 121 ? 31.155  5.922   8.294   1.00 70.30  ?  123 ARG A CD   1 
ATOM   956  N  NE   . ARG A 1 121 ? 31.300  6.466   9.654   1.00 78.70  ?  123 ARG A NE   1 
ATOM   957  C  CZ   . ARG A 1 121 ? 32.371  6.316   10.440  1.00 84.06  ?  123 ARG A CZ   1 
ATOM   958  N  NH1  . ARG A 1 121 ? 33.430  5.628   10.016  1.00 85.63  ?  123 ARG A NH1  1 
ATOM   959  N  NH2  . ARG A 1 121 ? 32.392  6.854   11.655  1.00 84.37  ?  123 ARG A NH2  1 
ATOM   960  N  N    . SER A 1 122 ? 30.381  2.057   4.227   1.00 51.06  ?  124 SER A N    1 
ATOM   961  C  CA   . SER A 1 122 ? 30.040  2.104   2.817   1.00 51.42  ?  124 SER A CA   1 
ATOM   962  C  C    . SER A 1 122 ? 29.060  0.979   2.397   1.00 50.31  ?  124 SER A C    1 
ATOM   963  O  O    . SER A 1 122 ? 28.021  1.281   1.820   1.00 52.53  ?  124 SER A O    1 
ATOM   964  C  CB   . SER A 1 122 ? 31.294  2.084   1.958   1.00 54.84  ?  124 SER A CB   1 
ATOM   965  O  OG   . SER A 1 122 ? 32.113  0.978   2.275   1.00 60.90  ?  124 SER A OG   1 
ATOM   966  N  N    . ASP A 1 123 ? 29.371  -0.301  2.698   1.00 46.58  ?  125 ASP A N    1 
ATOM   967  C  CA   . ASP A 1 123 ? 28.731  -1.432  2.026   1.00 43.19  ?  125 ASP A CA   1 
ATOM   968  C  C    . ASP A 1 123 ? 27.808  -2.325  2.902   1.00 38.68  ?  125 ASP A C    1 
ATOM   969  O  O    . ASP A 1 123 ? 27.051  -3.082  2.318   1.00 36.42  ?  125 ASP A O    1 
ATOM   970  C  CB   . ASP A 1 123 ? 29.788  -2.344  1.418   1.00 46.11  ?  125 ASP A CB   1 
ATOM   971  C  CG   . ASP A 1 123 ? 30.590  -1.740  0.290   1.00 54.77  ?  125 ASP A CG   1 
ATOM   972  O  OD1  . ASP A 1 123 ? 30.111  -0.801  -0.321  1.00 55.93  ?  125 ASP A OD1  1 
ATOM   973  O  OD2  . ASP A 1 123 ? 31.710  -2.241  0.022   1.00 59.86  ?  125 ASP A OD2  1 
ATOM   974  N  N    . LEU A 1 124 ? 27.877  -2.254  4.246   1.00 35.57  ?  126 LEU A N    1 
ATOM   975  C  CA   . LEU A 1 124 ? 27.162  -3.215  5.067   1.00 35.03  ?  126 LEU A CA   1 
ATOM   976  C  C    . LEU A 1 124 ? 25.639  -3.138  4.835   1.00 31.48  ?  126 LEU A C    1 
ATOM   977  O  O    . LEU A 1 124 ? 25.036  -4.162  4.533   1.00 30.31  ?  126 LEU A O    1 
ATOM   978  C  CB   . LEU A 1 124 ? 27.486  -3.041  6.560   1.00 36.55  ?  126 LEU A CB   1 
ATOM   979  C  CG   . LEU A 1 124 ? 26.729  -3.993  7.503   1.00 39.20  ?  126 LEU A CG   1 
ATOM   980  C  CD1  . LEU A 1 124 ? 27.294  -5.385  7.422   1.00 40.38  ?  126 LEU A CD1  1 
ATOM   981  C  CD2  . LEU A 1 124 ? 26.770  -3.468  8.971   1.00 40.78  ?  126 LEU A CD2  1 
ATOM   982  N  N    . ASN A 1 125 ? 25.040  -1.954  4.987   1.00 29.31  ?  127 ASN A N    1 
ATOM   983  C  CA   . ASN A 1 125 ? 23.601  -1.784  4.863   1.00 31.07  ?  127 ASN A CA   1 
ATOM   984  C  C    . ASN A 1 125 ? 23.079  -2.191  3.456   1.00 29.85  ?  127 ASN A C    1 
ATOM   985  O  O    . ASN A 1 125 ? 22.072  -2.916  3.359   1.00 29.70  ?  127 ASN A O    1 
ATOM   986  C  CB   . ASN A 1 125 ? 23.165  -0.369  5.231   1.00 33.78  ?  127 ASN A CB   1 
ATOM   987  C  CG   . ASN A 1 125 ? 23.463  0.030   6.695   1.00 45.20  ?  127 ASN A CG   1 
ATOM   988  O  OD1  . ASN A 1 125 ? 23.195  1.142   7.096   1.00 48.28  ?  127 ASN A OD1  1 
ATOM   989  N  ND2  . ASN A 1 125 ? 24.018  -0.830  7.541   1.00 49.83  ?  127 ASN A ND2  1 
ATOM   990  N  N    . ARG A 1 126 ? 23.749  -1.760  2.410   1.00 28.38  ?  128 ARG A N    1 
ATOM   991  C  CA   . ARG A 1 126 ? 23.350  -2.089  1.049   1.00 28.29  ?  128 ARG A CA   1 
ATOM   992  C  C    . ARG A 1 126 ? 23.503  -3.622  0.800   1.00 26.74  ?  128 ARG A C    1 
ATOM   993  O  O    . ARG A 1 126 ? 22.595  -4.189  0.255   1.00 27.95  ?  128 ARG A O    1 
ATOM   994  C  CB   . ARG A 1 126 ? 24.177  -1.347  -0.008  1.00 31.26  ?  128 ARG A CB   1 
ATOM   995  C  CG   . ARG A 1 126 ? 24.005  -1.818  -1.465  1.00 40.41  ?  128 ARG A CG   1 
ATOM   996  C  CD   . ARG A 1 126 ? 22.596  -1.659  -2.039  1.00 45.70  ?  128 ARG A CD   1 
ATOM   997  N  NE   . ARG A 1 126 ? 22.150  -0.265  -2.035  1.00 44.39  ?  128 ARG A NE   1 
ATOM   998  C  CZ   . ARG A 1 126 ? 20.923  0.146   -2.329  1.00 47.02  ?  128 ARG A CZ   1 
ATOM   999  N  NH1  . ARG A 1 126 ? 19.989  -0.727  -2.680  1.00 47.46  ?  128 ARG A NH1  1 
ATOM   1000 N  NH2  . ARG A 1 126 ? 20.619  1.448   -2.291  1.00 48.90  ?  128 ARG A NH2  1 
ATOM   1001 N  N    . PHE A 1 127 ? 24.617  -4.227  1.155   1.00 26.21  ?  129 PHE A N    1 
ATOM   1002 C  CA   . PHE A 1 127 ? 24.825  -5.652  0.940   1.00 27.28  ?  129 PHE A CA   1 
ATOM   1003 C  C    . PHE A 1 127 ? 23.838  -6.495  1.732   1.00 24.13  ?  129 PHE A C    1 
ATOM   1004 O  O    . PHE A 1 127 ? 23.354  -7.462  1.204   1.00 23.47  ?  129 PHE A O    1 
ATOM   1005 C  CB   . PHE A 1 127 ? 26.244  -6.090  1.246   1.00 28.78  ?  129 PHE A CB   1 
ATOM   1006 C  CG   . PHE A 1 127 ? 27.298  -5.748  0.194   1.00 33.67  ?  129 PHE A CG   1 
ATOM   1007 C  CD1  . PHE A 1 127 ? 27.028  -4.852  -0.821  1.00 37.10  ?  129 PHE A CD1  1 
ATOM   1008 C  CD2  . PHE A 1 127 ? 28.533  -6.348  0.221   1.00 37.93  ?  129 PHE A CD2  1 
ATOM   1009 C  CE1  . PHE A 1 127 ? 28.000  -4.536  -1.780  1.00 39.47  ?  129 PHE A CE1  1 
ATOM   1010 C  CE2  . PHE A 1 127 ? 29.489  -6.050  -0.747  1.00 40.77  ?  129 PHE A CE2  1 
ATOM   1011 C  CZ   . PHE A 1 127 ? 29.228  -5.106  -1.713  1.00 39.23  ?  129 PHE A CZ   1 
ATOM   1012 N  N    . TRP A 1 128 ? 23.509  -6.111  2.957   1.00 24.89  ?  130 TRP A N    1 
ATOM   1013 C  CA   . TRP A 1 128 ? 22.534  -6.857  3.743   1.00 24.67  ?  130 TRP A CA   1 
ATOM   1014 C  C    . TRP A 1 128 ? 21.165  -6.802  3.080   1.00 25.08  ?  130 TRP A C    1 
ATOM   1015 O  O    . TRP A 1 128 ? 20.521  -7.856  2.900   1.00 23.68  ?  130 TRP A O    1 
ATOM   1016 C  CB   . TRP A 1 128 ? 22.492  -6.380  5.194   1.00 24.53  ?  130 TRP A CB   1 
ATOM   1017 C  CG   . TRP A 1 128 ? 21.492  -7.078  6.061   1.00 27.48  ?  130 TRP A CG   1 
ATOM   1018 C  CD1  . TRP A 1 128 ? 20.508  -6.490  6.805   1.00 28.88  ?  130 TRP A CD1  1 
ATOM   1019 C  CD2  . TRP A 1 128 ? 21.440  -8.470  6.360   1.00 27.76  ?  130 TRP A CD2  1 
ATOM   1020 N  NE1  . TRP A 1 128 ? 19.827  -7.439  7.504   1.00 29.38  ?  130 TRP A NE1  1 
ATOM   1021 C  CE2  . TRP A 1 128 ? 20.369  -8.659  7.252   1.00 29.20  ?  130 TRP A CE2  1 
ATOM   1022 C  CE3  . TRP A 1 128 ? 22.131  -9.589  5.894   1.00 28.66  ?  130 TRP A CE3  1 
ATOM   1023 C  CZ2  . TRP A 1 128 ? 20.064  -9.896  7.772   1.00 30.65  ?  130 TRP A CZ2  1 
ATOM   1024 C  CZ3  . TRP A 1 128 ? 21.819  -10.818 6.413   1.00 30.31  ?  130 TRP A CZ3  1 
ATOM   1025 C  CH2  . TRP A 1 128 ? 20.785  -10.959 7.330   1.00 30.08  ?  130 TRP A CH2  1 
ATOM   1026 N  N    . LEU A 1 129 ? 20.728  -5.604  2.657   1.00 25.23  ?  131 LEU A N    1 
ATOM   1027 C  CA   . LEU A 1 129 ? 19.405  -5.463  2.030   1.00 26.52  ?  131 LEU A CA   1 
ATOM   1028 C  C    . LEU A 1 129 ? 19.339  -6.245  0.709   1.00 25.92  ?  131 LEU A C    1 
ATOM   1029 O  O    . LEU A 1 129 ? 18.316  -6.885  0.468   1.00 25.58  ?  131 LEU A O    1 
ATOM   1030 C  CB   . LEU A 1 129 ? 19.020  -4.020  1.740   1.00 27.85  ?  131 LEU A CB   1 
ATOM   1031 C  CG   . LEU A 1 129 ? 17.693  -3.784  0.992   1.00 32.57  ?  131 LEU A CG   1 
ATOM   1032 C  CD1  . LEU A 1 129 ? 16.505  -4.388  1.726   1.00 33.45  ?  131 LEU A CD1  1 
ATOM   1033 C  CD2  . LEU A 1 129 ? 17.472  -2.293  0.767   1.00 33.90  ?  131 LEU A CD2  1 
ATOM   1034 N  N    . GLU A 1 130 ? 20.371  -6.147  -0.128  1.00 24.20  ?  132 GLU A N    1 
ATOM   1035 C  CA   . GLU A 1 130 ? 20.358  -6.851  -1.401  1.00 25.13  ?  132 GLU A CA   1 
ATOM   1036 C  C    . GLU A 1 130 ? 20.259  -8.425  -1.140  1.00 24.58  ?  132 GLU A C    1 
ATOM   1037 O  O    . GLU A 1 130 ? 19.571  -9.127  -1.900  1.00 24.45  ?  132 GLU A O    1 
ATOM   1038 C  CB   . GLU A 1 130 ? 21.601  -6.567  -2.249  1.00 28.08  ?  132 GLU A CB   1 
ATOM   1039 C  CG   . GLU A 1 130 ? 21.679  -5.135  -2.788  1.00 38.81  ?  132 GLU A CG   1 
ATOM   1040 C  CD   . GLU A 1 130 ? 20.487  -4.696  -3.615  1.00 43.35  ?  132 GLU A CD   1 
ATOM   1041 O  OE1  . GLU A 1 130 ? 19.901  -5.545  -4.335  1.00 41.16  ?  132 GLU A OE1  1 
ATOM   1042 O  OE2  . GLU A 1 130 ? 20.127  -3.500  -3.531  1.00 50.22  ?  132 GLU A OE2  1 
ATOM   1043 N  N    . THR A 1 131 ? 20.939  -8.895  -0.108  1.00 23.94  ?  133 THR A N    1 
ATOM   1044 C  CA   . THR A 1 131 ? 20.890  -10.296 0.310   1.00 24.94  ?  133 THR A CA   1 
ATOM   1045 C  C    . THR A 1 131 ? 19.439  -10.693 0.664   1.00 22.03  ?  133 THR A C    1 
ATOM   1046 O  O    . THR A 1 131 ? 18.935  -11.695 0.135   1.00 22.17  ?  133 THR A O    1 
ATOM   1047 C  CB   . THR A 1 131 ? 21.850  -10.556 1.508   1.00 25.93  ?  133 THR A CB   1 
ATOM   1048 O  OG1  . THR A 1 131 ? 23.158  -10.232 1.082   1.00 25.49  ?  133 THR A OG1  1 
ATOM   1049 C  CG2  . THR A 1 131 ? 21.865  -12.023 1.919   1.00 24.53  ?  133 THR A CG2  1 
ATOM   1050 N  N    . LEU A 1 132 ? 18.797  -9.896  1.544   1.00 22.60  ?  134 LEU A N    1 
ATOM   1051 C  CA   . LEU A 1 132 ? 17.405  -10.143 1.999   1.00 24.38  ?  134 LEU A CA   1 
ATOM   1052 C  C    . LEU A 1 132 ? 16.448  -10.166 0.766   1.00 24.70  ?  134 LEU A C    1 
ATOM   1053 O  O    . LEU A 1 132 ? 15.582  -11.031 0.695   1.00 24.09  ?  134 LEU A O    1 
ATOM   1054 C  CB   . LEU A 1 132 ? 16.931  -9.118  3.043   1.00 24.47  ?  134 LEU A CB   1 
ATOM   1055 C  CG   . LEU A 1 132 ? 17.749  -9.032  4.364   1.00 30.96  ?  134 LEU A CG   1 
ATOM   1056 C  CD1  . LEU A 1 132 ? 17.176  -7.995  5.314   1.00 32.78  ?  134 LEU A CD1  1 
ATOM   1057 C  CD2  . LEU A 1 132 ? 17.945  -10.382 5.016   1.00 34.10  ?  134 LEU A CD2  1 
ATOM   1058 N  N    . LEU A 1 133 ? 16.613  -9.227  -0.196  1.00 24.21  ?  135 LEU A N    1 
ATOM   1059 C  CA   . LEU A 1 133 ? 15.787  -9.189  -1.383  1.00 25.92  ?  135 LEU A CA   1 
ATOM   1060 C  C    . LEU A 1 133 ? 15.937  -10.421 -2.276  1.00 25.02  ?  135 LEU A C    1 
ATOM   1061 O  O    . LEU A 1 133 ? 14.933  -10.860 -2.834  1.00 27.37  ?  135 LEU A O    1 
ATOM   1062 C  CB   . LEU A 1 133 ? 15.989  -7.914  -2.204  1.00 26.93  ?  135 LEU A CB   1 
ATOM   1063 C  CG   . LEU A 1 133 ? 15.678  -6.575  -1.467  1.00 28.71  ?  135 LEU A CG   1 
ATOM   1064 C  CD1  . LEU A 1 133 ? 15.891  -5.423  -2.373  1.00 27.86  ?  135 LEU A CD1  1 
ATOM   1065 C  CD2  . LEU A 1 133 ? 14.285  -6.542  -0.892  1.00 28.30  ?  135 LEU A CD2  1 
ATOM   1066 N  N    . CYS A 1 134 ? 17.131  -10.964 -2.394  1.00 24.73  ?  136 CYS A N    1 
ATOM   1067 C  CA   . CYS A 1 134 ? 17.398  -12.246 -3.104  1.00 25.92  ?  136 CYS A CA   1 
ATOM   1068 C  C    . CYS A 1 134 ? 16.649  -13.401 -2.440  1.00 25.25  ?  136 CYS A C    1 
ATOM   1069 O  O    . CYS A 1 134 ? 16.152  -14.277 -3.127  1.00 26.51  ?  136 CYS A O    1 
ATOM   1070 C  CB   . CYS A 1 134 ? 18.881  -12.565 -3.153  1.00 28.16  ?  136 CYS A CB   1 
ATOM   1071 S  SG   . CYS A 1 134 ? 19.812  -11.575 -4.307  1.00 31.91  ?  136 CYS A SG   1 
ATOM   1072 N  N    . LEU A 1 135 ? 16.617  -13.420 -1.095  1.00 22.77  ?  137 LEU A N    1 
ATOM   1073 C  CA   . LEU A 1 135 ? 15.938  -14.490 -0.364  1.00 25.65  ?  137 LEU A CA   1 
ATOM   1074 C  C    . LEU A 1 135 ? 14.430  -14.398 -0.552  1.00 25.37  ?  137 LEU A C    1 
ATOM   1075 O  O    . LEU A 1 135 ? 13.824  -15.314 -1.099  1.00 26.12  ?  137 LEU A O    1 
ATOM   1076 C  CB   . LEU A 1 135 ? 16.324  -14.442 1.148   1.00 24.90  ?  137 LEU A CB   1 
ATOM   1077 C  CG   . LEU A 1 135 ? 17.516  -15.267 1.593   1.00 26.53  ?  137 LEU A CG   1 
ATOM   1078 C  CD1  . LEU A 1 135 ? 18.716  -15.055 0.714   1.00 27.01  ?  137 LEU A CD1  1 
ATOM   1079 C  CD2  . LEU A 1 135 ? 17.780  -14.954 3.049   1.00 27.38  ?  137 LEU A CD2  1 
ATOM   1080 N  N    . ILE A 1 136 ? 13.836  -13.279 -0.149  1.00 25.01  ?  138 ILE A N    1 
ATOM   1081 C  CA   . ILE A 1 136 ? 12.399  -13.169 -0.109  1.00 25.08  ?  138 ILE A CA   1 
ATOM   1082 C  C    . ILE A 1 136 ? 11.792  -13.187 -1.538  1.00 26.85  ?  138 ILE A C    1 
ATOM   1083 O  O    . ILE A 1 136 ? 10.721  -13.689 -1.699  1.00 26.81  ?  138 ILE A O    1 
ATOM   1084 C  CB   . ILE A 1 136 ? 11.871  -11.994 0.721   1.00 26.01  ?  138 ILE A CB   1 
ATOM   1085 C  CG1  . ILE A 1 136 ? 12.068  -10.646 0.006   1.00 26.56  ?  138 ILE A CG1  1 
ATOM   1086 C  CG2  . ILE A 1 136 ? 12.449  -12.003 2.158   1.00 25.23  ?  138 ILE A CG2  1 
ATOM   1087 C  CD1  . ILE A 1 136 ? 11.472  -9.442  0.761   1.00 29.78  ?  138 ILE A CD1  1 
ATOM   1088 N  N    . GLY A 1 137 ? 12.512  -12.655 -2.515  1.00 26.70  ?  139 GLY A N    1 
ATOM   1089 C  CA   . GLY A 1 137 ? 12.076  -12.594 -3.892  1.00 28.09  ?  139 GLY A CA   1 
ATOM   1090 C  C    . GLY A 1 137 ? 12.329  -13.851 -4.692  1.00 30.08  ?  139 GLY A C    1 
ATOM   1091 O  O    . GLY A 1 137 ? 11.969  -13.867 -5.890  1.00 31.44  ?  139 GLY A O    1 
ATOM   1092 N  N    . GLU A 1 138 ? 12.958  -14.902 -4.092  1.00 28.44  ?  140 GLU A N    1 
ATOM   1093 C  CA   . GLU A 1 138 ? 13.194  -16.203 -4.775  1.00 28.81  ?  140 GLU A CA   1 
ATOM   1094 C  C    . GLU A 1 138 ? 13.978  -16.011 -6.062  1.00 30.70  ?  140 GLU A C    1 
ATOM   1095 O  O    . GLU A 1 138 ? 13.576  -16.486 -7.152  1.00 30.28  ?  140 GLU A O    1 
ATOM   1096 C  CB   . GLU A 1 138 ? 11.855  -16.918 -5.029  1.00 30.38  ?  140 GLU A CB   1 
ATOM   1097 C  CG   . GLU A 1 138 ? 11.048  -17.154 -3.771  1.00 34.96  ?  140 GLU A CG   1 
ATOM   1098 C  CD   . GLU A 1 138 ? 11.536  -18.273 -2.851  1.00 38.81  ?  140 GLU A CD   1 
ATOM   1099 O  OE1  . GLU A 1 138 ? 11.947  -19.346 -3.359  1.00 40.53  ?  140 GLU A OE1  1 
ATOM   1100 O  OE2  . GLU A 1 138 ? 11.478  -18.096 -1.611  1.00 37.57  ?  140 GLU A OE2  1 
ATOM   1101 N  N    . SER A 1 139 ? 15.110  -15.320 -5.927  1.00 31.33  ?  141 SER A N    1 
ATOM   1102 C  CA   . SER A 1 139 ? 15.920  -14.807 -7.047  1.00 33.13  ?  141 SER A CA   1 
ATOM   1103 C  C    . SER A 1 139 ? 16.699  -15.900 -7.742  1.00 33.70  ?  141 SER A C    1 
ATOM   1104 O  O    . SER A 1 139 ? 17.241  -15.643 -8.796  1.00 34.06  ?  141 SER A O    1 
ATOM   1105 C  CB   . SER A 1 139 ? 16.918  -13.751 -6.565  1.00 33.66  ?  141 SER A CB   1 
ATOM   1106 O  OG   . SER A 1 139 ? 16.298  -12.599 -6.027  1.00 34.72  ?  141 SER A OG   1 
ATOM   1107 N  N    . PHE A 1 140 ? 16.756  -17.121 -7.200  1.00 32.59  ?  142 PHE A N    1 
ATOM   1108 C  CA   . PHE A 1 140 ? 17.615  -18.175 -7.713  1.00 32.03  ?  142 PHE A CA   1 
ATOM   1109 C  C    . PHE A 1 140 ? 16.776  -19.254 -8.489  1.00 34.90  ?  142 PHE A C    1 
ATOM   1110 O  O    . PHE A 1 140 ? 17.242  -20.378 -8.616  1.00 35.78  ?  142 PHE A O    1 
ATOM   1111 C  CB   . PHE A 1 140 ? 18.378  -18.807 -6.506  1.00 29.14  ?  142 PHE A CB   1 
ATOM   1112 C  CG   . PHE A 1 140 ? 19.159  -17.777 -5.705  1.00 29.12  ?  142 PHE A CG   1 
ATOM   1113 C  CD1  . PHE A 1 140 ? 20.122  -16.976 -6.319  1.00 28.95  ?  142 PHE A CD1  1 
ATOM   1114 C  CD2  . PHE A 1 140 ? 18.845  -17.515 -4.390  1.00 28.62  ?  142 PHE A CD2  1 
ATOM   1115 C  CE1  . PHE A 1 140 ? 20.813  -16.028 -5.593  1.00 29.58  ?  142 PHE A CE1  1 
ATOM   1116 C  CE2  . PHE A 1 140 ? 19.511  -16.526 -3.671  1.00 28.20  ?  142 PHE A CE2  1 
ATOM   1117 C  CZ   . PHE A 1 140 ? 20.498  -15.797 -4.256  1.00 28.04  ?  142 PHE A CZ   1 
ATOM   1118 N  N    . ASP A 1 141 ? 15.553  -18.925 -8.935  1.00 38.70  ?  143 ASP A N    1 
ATOM   1119 C  CA   . ASP A 1 141 ? 14.585  -19.819 -9.643  1.00 42.86  ?  143 ASP A CA   1 
ATOM   1120 C  C    . ASP A 1 141 ? 14.308  -21.124 -8.825  1.00 43.29  ?  143 ASP A C    1 
ATOM   1121 O  O    . ASP A 1 141 ? 14.000  -20.991 -7.649  1.00 43.63  ?  143 ASP A O    1 
ATOM   1122 C  CB   . ASP A 1 141 ? 15.026  -20.064 -11.088 1.00 49.08  ?  143 ASP A CB   1 
ATOM   1123 C  CG   . ASP A 1 141 ? 13.995  -20.823 -11.945 1.00 62.13  ?  143 ASP A CG   1 
ATOM   1124 O  OD1  . ASP A 1 141 ? 12.759  -20.489 -11.855 1.00 64.84  ?  143 ASP A OD1  1 
ATOM   1125 O  OD2  . ASP A 1 141 ? 14.411  -21.753 -12.694 1.00 65.23  ?  143 ASP A OD2  1 
ATOM   1126 N  N    . ASP A 1 142 ? 14.401  -22.344 -9.400  1.00 43.10  ?  144 ASP A N    1 
ATOM   1127 C  CA   . ASP A 1 142 ? 14.132  -23.561 -8.630  1.00 43.70  ?  144 ASP A CA   1 
ATOM   1128 C  C    . ASP A 1 142 ? 15.188  -23.773 -7.542  1.00 39.57  ?  144 ASP A C    1 
ATOM   1129 O  O    . ASP A 1 142 ? 14.870  -24.341 -6.496  1.00 38.34  ?  144 ASP A O    1 
ATOM   1130 C  CB   . ASP A 1 142 ? 14.017  -24.774 -9.560  1.00 49.69  ?  144 ASP A CB   1 
ATOM   1131 C  CG   . ASP A 1 142 ? 12.738  -24.823 -10.393 1.00 64.02  ?  144 ASP A CG   1 
ATOM   1132 O  OD1  . ASP A 1 142 ? 11.737  -24.148 -10.009 1.00 67.05  ?  144 ASP A OD1  1 
ATOM   1133 O  OD2  . ASP A 1 142 ? 12.724  -25.550 -11.424 1.00 69.89  ?  144 ASP A OD2  1 
ATOM   1134 N  N    . TYR A 1 143 ? 16.433  -23.285 -7.773  1.00 37.61  ?  145 TYR A N    1 
ATOM   1135 C  CA   . TYR A 1 143 ? 17.497  -23.367 -6.784  1.00 36.72  ?  145 TYR A CA   1 
ATOM   1136 C  C    . TYR A 1 143 ? 17.269  -22.535 -5.545  1.00 33.34  ?  145 TYR A C    1 
ATOM   1137 O  O    . TYR A 1 143 ? 18.018  -22.696 -4.580  1.00 33.46  ?  145 TYR A O    1 
ATOM   1138 C  CB   . TYR A 1 143 ? 18.841  -23.025 -7.417  1.00 38.72  ?  145 TYR A CB   1 
ATOM   1139 C  CG   . TYR A 1 143 ? 19.183  -23.945 -8.574  1.00 41.00  ?  145 TYR A CG   1 
ATOM   1140 C  CD1  . TYR A 1 143 ? 19.068  -25.317 -8.450  1.00 42.69  ?  145 TYR A CD1  1 
ATOM   1141 C  CD2  . TYR A 1 143 ? 19.510  -23.435 -9.818  1.00 44.16  ?  145 TYR A CD2  1 
ATOM   1142 C  CE1  . TYR A 1 143 ? 19.366  -26.168 -9.501  1.00 45.75  ?  145 TYR A CE1  1 
ATOM   1143 C  CE2  . TYR A 1 143 ? 19.794  -24.277 -10.892 1.00 47.13  ?  145 TYR A CE2  1 
ATOM   1144 C  CZ   . TYR A 1 143 ? 19.718  -25.647 -10.724 1.00 49.06  ?  145 TYR A CZ   1 
ATOM   1145 O  OH   . TYR A 1 143 ? 19.963  -26.516 -11.755 1.00 54.83  ?  145 TYR A OH   1 
ATOM   1146 N  N    . SER A 1 144 ? 16.261  -21.651 -5.514  1.00 31.85  ?  146 SER A N    1 
ATOM   1147 C  CA   . SER A 1 144 ? 15.917  -20.930 -4.298  1.00 30.27  ?  146 SER A CA   1 
ATOM   1148 C  C    . SER A 1 144 ? 15.456  -21.908 -3.214  1.00 29.07  ?  146 SER A C    1 
ATOM   1149 O  O    . SER A 1 144 ? 15.561  -21.593 -2.051  1.00 27.68  ?  146 SER A O    1 
ATOM   1150 C  CB   . SER A 1 144 ? 14.860  -19.861 -4.575  1.00 31.91  ?  146 SER A CB   1 
ATOM   1151 O  OG   . SER A 1 144 ? 15.399  -18.697 -5.172  1.00 34.22  ?  146 SER A OG   1 
ATOM   1152 N  N    . ASP A 1 145 ? 14.939  -23.098 -3.581  1.00 29.77  ?  147 ASP A N    1 
ATOM   1153 C  CA   . ASP A 1 145 ? 14.606  -24.140 -2.618  1.00 31.86  ?  147 ASP A CA   1 
ATOM   1154 C  C    . ASP A 1 145 ? 15.833  -24.593 -1.818  1.00 30.44  ?  147 ASP A C    1 
ATOM   1155 O  O    . ASP A 1 145 ? 15.647  -25.055 -0.675  1.00 31.28  ?  147 ASP A O    1 
ATOM   1156 C  CB   . ASP A 1 145 ? 13.907  -25.340 -3.285  1.00 35.35  ?  147 ASP A CB   1 
ATOM   1157 C  CG   . ASP A 1 145 ? 12.523  -24.989 -3.812  1.00 42.51  ?  147 ASP A CG   1 
ATOM   1158 O  OD1  . ASP A 1 145 ? 11.889  -24.073 -3.259  1.00 42.92  ?  147 ASP A OD1  1 
ATOM   1159 O  OD2  . ASP A 1 145 ? 12.082  -25.622 -4.796  1.00 48.38  ?  147 ASP A OD2  1 
ATOM   1160 N  N    . ASP A 1 146 ? 17.053  -24.464 -2.368  1.00 26.51  ?  148 ASP A N    1 
ATOM   1161 C  CA   . ASP A 1 146 ? 18.266  -24.855 -1.654  1.00 26.97  ?  148 ASP A CA   1 
ATOM   1162 C  C    . ASP A 1 146 ? 18.639  -23.825 -0.556  1.00 28.51  ?  148 ASP A C    1 
ATOM   1163 O  O    . ASP A 1 146 ? 19.407  -24.161 0.297   1.00 29.65  ?  148 ASP A O    1 
ATOM   1164 C  CB   . ASP A 1 146 ? 19.471  -25.119 -2.594  1.00 28.50  ?  148 ASP A CB   1 
ATOM   1165 C  CG   . ASP A 1 146 ? 19.522  -26.608 -2.996  1.00 39.48  ?  148 ASP A CG   1 
ATOM   1166 O  OD1  . ASP A 1 146 ? 18.478  -27.140 -3.371  1.00 44.88  ?  148 ASP A OD1  1 
ATOM   1167 O  OD2  . ASP A 1 146 ? 20.627  -27.249 -2.871  1.00 36.41  ?  148 ASP A OD2  1 
ATOM   1168 N  N    . VAL A 1 147 ? 18.077  -22.596 -0.583  1.00 26.97  ?  149 VAL A N    1 
ATOM   1169 C  CA   . VAL A 1 147 ? 18.492  -21.553 0.375   1.00 25.63  ?  149 VAL A CA   1 
ATOM   1170 C  C    . VAL A 1 147 ? 17.827  -21.833 1.680   1.00 24.41  ?  149 VAL A C    1 
ATOM   1171 O  O    . VAL A 1 147 ? 16.664  -22.144 1.714   1.00 27.37  ?  149 VAL A O    1 
ATOM   1172 C  CB   . VAL A 1 147 ? 18.093  -20.182 -0.146  1.00 25.12  ?  149 VAL A CB   1 
ATOM   1173 C  CG1  . VAL A 1 147 ? 18.320  -19.047 0.903   1.00 25.89  ?  149 VAL A CG1  1 
ATOM   1174 C  CG2  . VAL A 1 147 ? 18.765  -19.897 -1.418  1.00 25.61  ?  149 VAL A CG2  1 
ATOM   1175 N  N    . CYS A 1 148 ? 18.535  -21.709 2.714   1.00 23.66  ?  150 CYS A N    1 
ATOM   1176 C  CA   . CYS A 1 148 ? 18.041  -21.780 4.064   1.00 24.30  ?  150 CYS A CA   1 
ATOM   1177 C  C    . CYS A 1 148 ? 17.774  -20.420 4.664   1.00 24.43  ?  150 CYS A C    1 
ATOM   1178 O  O    . CYS A 1 148 ? 16.727  -20.207 5.300   1.00 22.96  ?  150 CYS A O    1 
ATOM   1179 C  CB   . CYS A 1 148 ? 19.006  -22.590 4.917   1.00 24.06  ?  150 CYS A CB   1 
ATOM   1180 S  SG   . CYS A 1 148 ? 19.160  -24.291 4.395   1.00 29.41  ?  150 CYS A SG   1 
ATOM   1181 N  N    . GLY A 1 149 ? 18.718  -19.525 4.467   1.00 24.36  ?  151 GLY A N    1 
ATOM   1182 C  CA   . GLY A 1 149 ? 18.694  -18.191 5.035   1.00 23.27  ?  151 GLY A CA   1 
ATOM   1183 C  C    . GLY A 1 149 ? 19.976  -17.419 4.814   1.00 24.10  ?  151 GLY A C    1 
ATOM   1184 O  O    . GLY A 1 149 ? 20.857  -17.864 4.053   1.00 25.15  ?  151 GLY A O    1 
ATOM   1185 N  N    . ALA A 1 150 ? 20.079  -16.263 5.496   1.00 21.98  ?  152 ALA A N    1 
ATOM   1186 C  CA   . ALA A 1 150 ? 21.258  -15.387 5.449   1.00 22.62  ?  152 ALA A CA   1 
ATOM   1187 C  C    . ALA A 1 150 ? 21.584  -14.875 6.832   1.00 21.94  ?  152 ALA A C    1 
ATOM   1188 O  O    . ALA A 1 150 ? 20.693  -14.751 7.701   1.00 19.93  ?  152 ALA A O    1 
ATOM   1189 C  CB   . ALA A 1 150 ? 21.029  -14.239 4.501   1.00 18.86  ?  152 ALA A CB   1 
ATOM   1190 N  N    . VAL A 1 151 ? 22.858  -14.596 7.045   1.00 21.03  ?  153 VAL A N    1 
ATOM   1191 C  CA   . VAL A 1 151 ? 23.402  -14.176 8.339   1.00 24.37  ?  153 VAL A CA   1 
ATOM   1192 C  C    . VAL A 1 151 ? 24.293  -12.965 8.117   1.00 26.23  ?  153 VAL A C    1 
ATOM   1193 O  O    . VAL A 1 151 ? 25.105  -12.945 7.175   1.00 26.20  ?  153 VAL A O    1 
ATOM   1194 C  CB   . VAL A 1 151 ? 24.196  -15.332 9.032   1.00 24.87  ?  153 VAL A CB   1 
ATOM   1195 C  CG1  . VAL A 1 151 ? 24.761  -14.864 10.390  1.00 26.35  ?  153 VAL A CG1  1 
ATOM   1196 C  CG2  . VAL A 1 151 ? 23.315  -16.584 9.213   1.00 23.44  ?  153 VAL A CG2  1 
ATOM   1197 N  N    . VAL A 1 152 ? 24.134  -11.965 8.950   1.00 26.86  ?  154 VAL A N    1 
ATOM   1198 C  CA   . VAL A 1 152 ? 25.066  -10.853 9.072   1.00 27.96  ?  154 VAL A CA   1 
ATOM   1199 C  C    . VAL A 1 152 ? 25.696  -10.878 10.476  1.00 29.14  ?  154 VAL A C    1 
ATOM   1200 O  O    . VAL A 1 152 ? 24.992  -10.850 11.477  1.00 29.04  ?  154 VAL A O    1 
ATOM   1201 C  CB   . VAL A 1 152 ? 24.448  -9.495  8.694   1.00 26.00  ?  154 VAL A CB   1 
ATOM   1202 C  CG1  . VAL A 1 152 ? 23.201  -9.125  9.504   1.00 24.35  ?  154 VAL A CG1  1 
ATOM   1203 C  CG2  . VAL A 1 152 ? 25.488  -8.363  8.774   1.00 28.38  ?  154 VAL A CG2  1 
ATOM   1204 N  N    . ASN A 1 153 ? 27.039  -10.964 10.519  1.00 31.07  ?  155 ASN A N    1 
ATOM   1205 C  CA   . ASN A 1 153 ? 27.832  -10.921 11.762  1.00 34.66  ?  155 ASN A CA   1 
ATOM   1206 C  C    . ASN A 1 153 ? 28.525  -9.574  11.791  1.00 38.67  ?  155 ASN A C    1 
ATOM   1207 O  O    . ASN A 1 153 ? 29.331  -9.262  10.907  1.00 38.33  ?  155 ASN A O    1 
ATOM   1208 C  CB   . ASN A 1 153 ? 28.862  -12.024 11.783  1.00 36.20  ?  155 ASN A CB   1 
ATOM   1209 C  CG   . ASN A 1 153 ? 28.325  -13.411 11.522  1.00 36.71  ?  155 ASN A CG   1 
ATOM   1210 O  OD1  . ASN A 1 153 ? 28.609  -14.065 10.498  1.00 38.27  ?  155 ASN A OD1  1 
ATOM   1211 N  ND2  . ASN A 1 153 ? 27.550  -13.882 12.433  1.00 34.24  ?  155 ASN A ND2  1 
ATOM   1212 N  N    . VAL A 1 154 ? 28.187  -8.762  12.775  1.00 41.28  ?  156 VAL A N    1 
ATOM   1213 C  CA   . VAL A 1 154 ? 28.750  -7.418  12.910  1.00 44.75  ?  156 VAL A CA   1 
ATOM   1214 C  C    . VAL A 1 154 ? 29.900  -7.564  13.905  1.00 46.33  ?  156 VAL A C    1 
ATOM   1215 O  O    . VAL A 1 154 ? 29.655  -7.922  15.071  1.00 45.61  ?  156 VAL A O    1 
ATOM   1216 C  CB   . VAL A 1 154 ? 27.659  -6.446  13.389  1.00 46.57  ?  156 VAL A CB   1 
ATOM   1217 C  CG1  . VAL A 1 154 ? 28.254  -5.070  13.669  1.00 46.92  ?  156 VAL A CG1  1 
ATOM   1218 C  CG2  . VAL A 1 154 ? 26.518  -6.348  12.358  1.00 47.48  ?  156 VAL A CG2  1 
ATOM   1219 N  N    . ARG A 1 155 ? 31.137  -7.321  13.454  1.00 47.91  ?  157 ARG A N    1 
ATOM   1220 C  CA   . ARG A 1 155 ? 32.321  -7.479  14.311  1.00 50.37  ?  157 ARG A CA   1 
ATOM   1221 C  C    . ARG A 1 155 ? 33.254  -6.289  14.245  1.00 52.55  ?  157 ARG A C    1 
ATOM   1222 O  O    . ARG A 1 155 ? 33.232  -5.513  13.282  1.00 53.18  ?  157 ARG A O    1 
ATOM   1223 C  CB   . ARG A 1 155 ? 33.120  -8.727  13.943  1.00 51.00  ?  157 ARG A CB   1 
ATOM   1224 C  CG   . ARG A 1 155 ? 32.404  -10.013 14.129  1.00 53.64  ?  157 ARG A CG   1 
ATOM   1225 C  CD   . ARG A 1 155 ? 32.208  -10.404 15.577  1.00 54.79  ?  157 ARG A CD   1 
ATOM   1226 N  NE   . ARG A 1 155 ? 31.475  -11.662 15.684  1.00 57.02  ?  157 ARG A NE   1 
ATOM   1227 C  CZ   . ARG A 1 155 ? 30.150  -11.793 15.592  1.00 61.11  ?  157 ARG A CZ   1 
ATOM   1228 N  NH1  . ARG A 1 155 ? 29.374  -10.723 15.393  1.00 60.97  ?  157 ARG A NH1  1 
ATOM   1229 N  NH2  . ARG A 1 155 ? 29.588  -12.990 15.701  1.00 62.61  ?  157 ARG A NH2  1 
ATOM   1230 N  N    . ALA A 1 156 ? 34.085  -6.158  15.295  1.00 54.15  ?  158 ALA A N    1 
ATOM   1231 C  CA   . ALA A 1 156 ? 35.117  -5.126  15.387  1.00 56.02  ?  158 ALA A CA   1 
ATOM   1232 C  C    . ALA A 1 156 ? 36.098  -5.210  14.191  1.00 57.32  ?  158 ALA A C    1 
ATOM   1233 O  O    . ALA A 1 156 ? 36.291  -4.211  13.522  1.00 58.09  ?  158 ALA A O    1 
ATOM   1234 C  CB   . ALA A 1 156 ? 35.855  -5.258  16.721  1.00 56.34  ?  158 ALA A CB   1 
ATOM   1235 N  N    . LYS A 1 157 ? 36.668  -6.396  13.922  1.00 57.99  ?  159 LYS A N    1 
ATOM   1236 C  CA   . LYS A 1 157 ? 37.683  -6.653  12.898  1.00 59.68  ?  159 LYS A CA   1 
ATOM   1237 C  C    . LYS A 1 157 ? 37.138  -6.552  11.478  1.00 59.51  ?  159 LYS A C    1 
ATOM   1238 O  O    . LYS A 1 157 ? 37.893  -6.215  10.571  1.00 61.09  ?  159 LYS A O    1 
ATOM   1239 C  CB   . LYS A 1 157 ? 38.281  -8.064  13.115  1.00 64.73  ?  159 LYS A CB   1 
ATOM   1240 C  CG   . LYS A 1 157 ? 39.508  -8.382  12.259  1.00 73.44  ?  159 LYS A CG   1 
ATOM   1241 C  CD   . LYS A 1 157 ? 40.251  -9.636  12.771  1.00 80.69  ?  159 LYS A CD   1 
ATOM   1242 C  CE   . LYS A 1 157 ? 41.654  -9.794  12.199  1.00 85.47  ?  159 LYS A CE   1 
ATOM   1243 N  NZ   . LYS A 1 157 ? 42.464  -10.784 12.974  1.00 87.49  ?  159 LYS A NZ   1 
ATOM   1244 N  N    . GLY A 1 158 ? 35.852  -6.843  11.284  1.00 57.30  ?  160 GLY A N    1 
ATOM   1245 C  CA   . GLY A 1 158 ? 35.205  -6.733  9.980   1.00 55.31  ?  160 GLY A CA   1 
ATOM   1246 C  C    . GLY A 1 158 ? 33.966  -7.613  9.861   1.00 52.42  ?  160 GLY A C    1 
ATOM   1247 O  O    . GLY A 1 158 ? 33.934  -8.738  10.383  1.00 53.81  ?  160 GLY A O    1 
ATOM   1248 N  N    . ASP A 1 159 ? 32.953  -7.114  9.149   1.00 47.94  ?  161 ASP A N    1 
ATOM   1249 C  CA   . ASP A 1 159 ? 31.622  -7.714  9.074   1.00 43.56  ?  161 ASP A CA   1 
ATOM   1250 C  C    . ASP A 1 159 ? 31.596  -8.894  8.080   1.00 38.83  ?  161 ASP A C    1 
ATOM   1251 O  O    . ASP A 1 159 ? 32.434  -8.966  7.191   1.00 37.70  ?  161 ASP A O    1 
ATOM   1252 C  CB   . ASP A 1 159 ? 30.577  -6.642  8.689   1.00 44.74  ?  161 ASP A CB   1 
ATOM   1253 C  CG   . ASP A 1 159 ? 30.643  -5.393  9.539   1.00 50.82  ?  161 ASP A CG   1 
ATOM   1254 O  OD1  . ASP A 1 159 ? 30.546  -5.514  10.775  1.00 51.81  ?  161 ASP A OD1  1 
ATOM   1255 O  OD2  . ASP A 1 159 ? 30.791  -4.300  8.969   1.00 53.37  ?  161 ASP A OD2  1 
ATOM   1256 N  N    . LYS A 1 160 ? 30.667  -9.807  8.266   1.00 35.55  ?  162 LYS A N    1 
ATOM   1257 C  CA   . LYS A 1 160 ? 30.479  -10.945 7.358   1.00 34.64  ?  162 LYS A CA   1 
ATOM   1258 C  C    . LYS A 1 160 ? 28.998  -11.018 6.982   1.00 30.39  ?  162 LYS A C    1 
ATOM   1259 O  O    . LYS A 1 160 ? 28.128  -10.886 7.855   1.00 28.45  ?  162 LYS A O    1 
ATOM   1260 C  CB   . LYS A 1 160 ? 30.909  -12.266 8.011   1.00 38.32  ?  162 LYS A CB   1 
ATOM   1261 C  CG   . LYS A 1 160 ? 32.388  -12.386 8.288   1.00 45.78  ?  162 LYS A CG   1 
ATOM   1262 C  CD   . LYS A 1 160 ? 32.753  -13.776 8.803   1.00 54.58  ?  162 LYS A CD   1 
ATOM   1263 C  CE   . LYS A 1 160 ? 32.856  -13.812 10.307  1.00 63.36  ?  162 LYS A CE   1 
ATOM   1264 N  NZ   . LYS A 1 160 ? 33.178  -15.196 10.812  1.00 68.32  ?  162 LYS A NZ   1 
ATOM   1265 N  N    . ILE A 1 161 ? 28.708  -11.245 5.689   1.00 28.39  ?  163 ILE A N    1 
ATOM   1266 C  CA   . ILE A 1 161 ? 27.354  -11.546 5.212   1.00 26.49  ?  163 ILE A CA   1 
ATOM   1267 C  C    . ILE A 1 161 ? 27.459  -12.852 4.461   1.00 25.46  ?  163 ILE A C    1 
ATOM   1268 O  O    . ILE A 1 161 ? 28.437  -13.080 3.724   1.00 23.85  ?  163 ILE A O    1 
ATOM   1269 C  CB   . ILE A 1 161 ? 26.788  -10.415 4.322   1.00 26.40  ?  163 ILE A CB   1 
ATOM   1270 C  CG1  . ILE A 1 161 ? 26.681  -9.096  5.128   1.00 27.71  ?  163 ILE A CG1  1 
ATOM   1271 C  CG2  . ILE A 1 161 ? 25.421  -10.797 3.714   1.00 28.32  ?  163 ILE A CG2  1 
ATOM   1272 C  CD1  . ILE A 1 161 ? 26.421  -7.954  4.274   1.00 28.83  ?  163 ILE A CD1  1 
ATOM   1273 N  N    . ALA A 1 162 ? 26.470  -13.718 4.642   1.00 23.97  ?  164 ALA A N    1 
ATOM   1274 C  CA   . ALA A 1 162 ? 26.497  -15.050 4.046   1.00 24.73  ?  164 ALA A CA   1 
ATOM   1275 C  C    . ALA A 1 162 ? 25.110  -15.513 3.679   1.00 25.51  ?  164 ALA A C    1 
ATOM   1276 O  O    . ALA A 1 162 ? 24.159  -15.247 4.450   1.00 26.67  ?  164 ALA A O    1 
ATOM   1277 C  CB   . ALA A 1 162 ? 27.128  -16.029 4.989   1.00 24.41  ?  164 ALA A CB   1 
ATOM   1278 N  N    . ILE A 1 163 ? 24.979  -16.199 2.525   1.00 23.14  ?  165 ILE A N    1 
ATOM   1279 C  CA   . ILE A 1 163 ? 23.783  -16.960 2.242   1.00 22.87  ?  165 ILE A CA   1 
ATOM   1280 C  C    . ILE A 1 163 ? 24.078  -18.440 2.561   1.00 23.22  ?  165 ILE A C    1 
ATOM   1281 O  O    . ILE A 1 163 ? 25.022  -19.024 2.004   1.00 22.87  ?  165 ILE A O    1 
ATOM   1282 C  CB   . ILE A 1 163 ? 23.322  -16.825 0.779   1.00 23.18  ?  165 ILE A CB   1 
ATOM   1283 C  CG1  . ILE A 1 163 ? 22.851  -15.369 0.522   1.00 25.36  ?  165 ILE A CG1  1 
ATOM   1284 C  CG2  . ILE A 1 163 ? 22.225  -17.850 0.420   1.00 21.22  ?  165 ILE A CG2  1 
ATOM   1285 C  CD1  . ILE A 1 163 ? 22.283  -15.128 -0.932  1.00 29.41  ?  165 ILE A CD1  1 
ATOM   1286 N  N    . TRP A 1 164 ? 23.259  -18.997 3.405   1.00 22.53  ?  166 TRP A N    1 
ATOM   1287 C  CA   . TRP A 1 164 ? 23.288  -20.419 3.811   1.00 24.96  ?  166 TRP A CA   1 
ATOM   1288 C  C    . TRP A 1 164 ? 22.385  -21.267 2.892   1.00 26.38  ?  166 TRP A C    1 
ATOM   1289 O  O    . TRP A 1 164 ? 21.227  -20.901 2.575   1.00 25.31  ?  166 TRP A O    1 
ATOM   1290 C  CB   . TRP A 1 164 ? 22.846  -20.573 5.255   1.00 25.30  ?  166 TRP A CB   1 
ATOM   1291 C  CG   . TRP A 1 164 ? 23.801  -20.091 6.299   1.00 25.77  ?  166 TRP A CG   1 
ATOM   1292 C  CD1  . TRP A 1 164 ? 24.703  -19.062 6.207   1.00 25.44  ?  166 TRP A CD1  1 
ATOM   1293 C  CD2  . TRP A 1 164 ? 23.945  -20.631 7.604   1.00 26.18  ?  166 TRP A CD2  1 
ATOM   1294 N  NE1  . TRP A 1 164 ? 25.382  -18.938 7.372   1.00 26.44  ?  166 TRP A NE1  1 
ATOM   1295 C  CE2  . TRP A 1 164 ? 24.926  -19.873 8.265   1.00 27.38  ?  166 TRP A CE2  1 
ATOM   1296 C  CE3  . TRP A 1 164 ? 23.314  -21.666 8.289   1.00 27.11  ?  166 TRP A CE3  1 
ATOM   1297 C  CZ2  . TRP A 1 164 ? 25.321  -20.136 9.570   1.00 28.23  ?  166 TRP A CZ2  1 
ATOM   1298 C  CZ3  . TRP A 1 164 ? 23.677  -21.903 9.597   1.00 29.26  ?  166 TRP A CZ3  1 
ATOM   1299 C  CH2  . TRP A 1 164 ? 24.676  -21.133 10.226  1.00 29.37  ?  166 TRP A CH2  1 
ATOM   1300 N  N    . THR A 1 165 ? 22.942  -22.395 2.451   1.00 25.93  ?  167 THR A N    1 
ATOM   1301 C  CA   . THR A 1 165 ? 22.251  -23.361 1.621   1.00 27.15  ?  167 THR A CA   1 
ATOM   1302 C  C    . THR A 1 165 ? 22.304  -24.765 2.282   1.00 27.99  ?  167 THR A C    1 
ATOM   1303 O  O    . THR A 1 165 ? 23.139  -25.062 3.140   1.00 27.93  ?  167 THR A O    1 
ATOM   1304 C  CB   . THR A 1 165 ? 22.721  -23.333 0.132   1.00 29.27  ?  167 THR A CB   1 
ATOM   1305 O  OG1  . THR A 1 165 ? 23.847  -24.205 -0.021  1.00 32.29  ?  167 THR A OG1  1 
ATOM   1306 C  CG2  . THR A 1 165 ? 23.054  -21.918 -0.383  1.00 30.11  ?  167 THR A CG2  1 
ATOM   1307 N  N    . THR A 1 166 ? 21.369  -25.616 1.842   1.00 28.25  ?  168 THR A N    1 
ATOM   1308 C  CA   . THR A 1 166 ? 21.016  -26.819 2.570   1.00 27.17  ?  168 THR A CA   1 
ATOM   1309 C  C    . THR A 1 166 ? 21.941  -28.019 2.236   1.00 27.99  ?  168 THR A C    1 
ATOM   1310 O  O    . THR A 1 166 ? 22.047  -28.937 3.048   1.00 26.59  ?  168 THR A O    1 
ATOM   1311 C  CB   . THR A 1 166 ? 19.526  -27.179 2.308   1.00 29.12  ?  168 THR A CB   1 
ATOM   1312 O  OG1  . THR A 1 166 ? 19.114  -28.162 3.233   1.00 33.72  ?  168 THR A OG1  1 
ATOM   1313 C  CG2  . THR A 1 166 ? 19.261  -27.689 0.857   1.00 27.98  ?  168 THR A CG2  1 
ATOM   1314 N  N    . GLU A 1 167 ? 22.586  -28.028 1.046   1.00 30.13  ?  169 GLU A N    1 
ATOM   1315 C  CA   . GLU A 1 167 ? 23.281  -29.235 0.592   1.00 31.33  ?  169 GLU A CA   1 
ATOM   1316 C  C    . GLU A 1 167 ? 24.539  -28.900 -0.189  1.00 32.96  ?  169 GLU A C    1 
ATOM   1317 O  O    . GLU A 1 167 ? 24.472  -28.461 -1.348  1.00 33.12  ?  169 GLU A O    1 
ATOM   1318 C  CB   . GLU A 1 167 ? 22.317  -30.114 -0.247  1.00 33.34  ?  169 GLU A CB   1 
ATOM   1319 C  CG   . GLU A 1 167 ? 22.925  -31.394 -0.777  1.00 38.39  ?  169 GLU A CG   1 
ATOM   1320 C  CD   . GLU A 1 167 ? 23.693  -32.163 0.281   1.00 38.72  ?  169 GLU A CD   1 
ATOM   1321 O  OE1  . GLU A 1 167 ? 23.066  -32.748 1.198   1.00 39.67  ?  169 GLU A OE1  1 
ATOM   1322 O  OE2  . GLU A 1 167 ? 24.942  -32.130 0.208   1.00 39.91  ?  169 GLU A OE2  1 
ATOM   1323 N  N    . CYS A 1 168 ? 25.683  -29.112 0.442   1.00 34.17  ?  170 CYS A N    1 
ATOM   1324 C  CA   . CYS A 1 168 ? 26.950  -28.661 -0.134  1.00 38.12  ?  170 CYS A CA   1 
ATOM   1325 C  C    . CYS A 1 168 ? 27.348  -29.529 -1.375  1.00 39.18  ?  170 CYS A C    1 
ATOM   1326 O  O    . CYS A 1 168 ? 28.157  -29.090 -2.172  1.00 39.48  ?  170 CYS A O    1 
ATOM   1327 C  CB   . CYS A 1 168 ? 28.057  -28.532 0.938   1.00 40.58  ?  170 CYS A CB   1 
ATOM   1328 S  SG   . CYS A 1 168 ? 28.547  -30.079 1.699   1.00 51.93  ?  170 CYS A SG   1 
ATOM   1329 N  N    . GLU A 1 169 ? 26.748  -30.756 -1.575  1.00 39.59  ?  171 GLU A N    1 
ATOM   1330 C  CA   . GLU A 1 169 ? 27.002  -31.611 -2.756  1.00 39.97  ?  171 GLU A CA   1 
ATOM   1331 C  C    . GLU A 1 169 ? 26.080  -31.350 -3.950  1.00 39.18  ?  171 GLU A C    1 
ATOM   1332 O  O    . GLU A 1 169 ? 26.247  -31.985 -4.995  1.00 40.30  ?  171 GLU A O    1 
ATOM   1333 C  CB   . GLU A 1 169 ? 26.852  -33.098 -2.397  1.00 43.69  ?  171 GLU A CB   1 
ATOM   1334 C  CG   . GLU A 1 169 ? 27.774  -33.551 -1.305  1.00 47.35  ?  171 GLU A CG   1 
ATOM   1335 C  CD   . GLU A 1 169 ? 29.211  -33.413 -1.667  1.00 47.66  ?  171 GLU A CD   1 
ATOM   1336 O  OE1  . GLU A 1 169 ? 29.534  -33.559 -2.873  1.00 46.86  ?  171 GLU A OE1  1 
ATOM   1337 O  OE2  . GLU A 1 169 ? 30.015  -33.183 -0.728  1.00 51.41  ?  171 GLU A OE2  1 
ATOM   1338 N  N    . ASN A 1 170 ? 25.102  -30.420 -3.812  1.00 37.39  ?  172 ASN A N    1 
ATOM   1339 C  CA   . ASN A 1 170 ? 24.318  -29.936 -4.938  1.00 37.02  ?  172 ASN A CA   1 
ATOM   1340 C  C    . ASN A 1 170 ? 25.118  -28.858 -5.688  1.00 36.67  ?  172 ASN A C    1 
ATOM   1341 O  O    . ASN A 1 170 ? 24.853  -27.659 -5.549  1.00 34.99  ?  172 ASN A O    1 
ATOM   1342 C  CB   . ASN A 1 170 ? 22.992  -29.380 -4.482  1.00 37.74  ?  172 ASN A CB   1 
ATOM   1343 C  CG   . ASN A 1 170 ? 21.931  -30.399 -4.144  1.00 43.58  ?  172 ASN A CG   1 
ATOM   1344 O  OD1  . ASN A 1 170 ? 22.083  -31.622 -4.370  1.00 46.34  ?  172 ASN A OD1  1 
ATOM   1345 N  ND2  . ASN A 1 170 ? 20.821  -29.927 -3.620  1.00 42.04  ?  172 ASN A ND2  1 
ATOM   1346 N  N    . ARG A 1 171 ? 26.091  -29.321 -6.487  1.00 35.92  ?  173 ARG A N    1 
ATOM   1347 C  CA   . ARG A 1 171 ? 26.990  -28.405 -7.155  1.00 36.53  ?  173 ARG A CA   1 
ATOM   1348 C  C    . ARG A 1 171 ? 26.264  -27.380 -8.033  1.00 36.50  ?  173 ARG A C    1 
ATOM   1349 O  O    . ARG A 1 171 ? 26.590  -26.212 -7.979  1.00 36.47  ?  173 ARG A O    1 
ATOM   1350 C  CB   . ARG A 1 171 ? 28.058  -29.157 -8.001  1.00 39.74  ?  173 ARG A CB   1 
ATOM   1351 C  CG   . ARG A 1 171 ? 28.937  -28.234 -8.835  1.00 49.86  ?  173 ARG A CG   1 
ATOM   1352 C  CD   . ARG A 1 171 ? 29.808  -29.011 -9.825  1.00 60.31  ?  173 ARG A CD   1 
ATOM   1353 N  NE   . ARG A 1 171 ? 30.911  -29.746 -9.188  1.00 70.46  ?  173 ARG A NE   1 
ATOM   1354 C  CZ   . ARG A 1 171 ? 32.055  -29.202 -8.757  1.00 77.42  ?  173 ARG A CZ   1 
ATOM   1355 N  NH1  . ARG A 1 171 ? 32.266  -27.890 -8.875  1.00 78.06  ?  173 ARG A NH1  1 
ATOM   1356 N  NH2  . ARG A 1 171 ? 32.995  -29.966 -8.205  1.00 79.31  ?  173 ARG A NH2  1 
ATOM   1357 N  N    . GLU A 1 172 ? 25.319  -27.808 -8.838  1.00 36.55  ?  174 GLU A N    1 
ATOM   1358 C  CA   . GLU A 1 172 ? 24.651  -26.922 -9.769  1.00 38.06  ?  174 GLU A CA   1 
ATOM   1359 C  C    . GLU A 1 172 ? 23.813  -25.852 -9.030  1.00 36.50  ?  174 GLU A C    1 
ATOM   1360 O  O    . GLU A 1 172 ? 23.824  -24.712 -9.443  1.00 36.08  ?  174 GLU A O    1 
ATOM   1361 C  CB   . GLU A 1 172 ? 23.817  -27.709 -10.804 1.00 45.88  ?  174 GLU A CB   1 
ATOM   1362 C  CG   . GLU A 1 172 ? 24.628  -28.628 -11.713 1.00 59.31  ?  174 GLU A CG   1 
ATOM   1363 C  CD   . GLU A 1 172 ? 26.049  -28.227 -12.110 1.00 75.04  ?  174 GLU A CD   1 
ATOM   1364 O  OE1  . GLU A 1 172 ? 26.229  -27.129 -12.696 1.00 77.53  ?  174 GLU A OE1  1 
ATOM   1365 O  OE2  . GLU A 1 172 ? 26.982  -29.023 -11.836 1.00 79.48  ?  174 GLU A OE2  1 
ATOM   1366 N  N    . ALA A 1 173 ? 23.089  -26.233 -7.954  1.00 35.35  ?  175 ALA A N    1 
ATOM   1367 C  CA   . ALA A 1 173 ? 22.320  -25.296 -7.159  1.00 34.22  ?  175 ALA A CA   1 
ATOM   1368 C  C    . ALA A 1 173 ? 23.246  -24.263 -6.527  1.00 32.55  ?  175 ALA A C    1 
ATOM   1369 O  O    . ALA A 1 173 ? 22.983  -23.072 -6.619  1.00 31.18  ?  175 ALA A O    1 
ATOM   1370 C  CB   . ALA A 1 173 ? 21.514  -26.030 -6.079  1.00 33.71  ?  175 ALA A CB   1 
ATOM   1371 N  N    . VAL A 1 174 ? 24.332  -24.722 -5.914  1.00 32.26  ?  176 VAL A N    1 
ATOM   1372 C  CA   . VAL A 1 174 ? 25.225  -23.869 -5.145  1.00 32.27  ?  176 VAL A CA   1 
ATOM   1373 C  C    . VAL A 1 174 ? 25.904  -22.865 -6.122  1.00 31.90  ?  176 VAL A C    1 
ATOM   1374 O  O    . VAL A 1 174 ? 25.985  -21.690 -5.812  1.00 31.47  ?  176 VAL A O    1 
ATOM   1375 C  CB   . VAL A 1 174 ? 26.246  -24.738 -4.382  1.00 34.56  ?  176 VAL A CB   1 
ATOM   1376 C  CG1  . VAL A 1 174 ? 27.396  -23.877 -3.876  1.00 37.68  ?  176 VAL A CG1  1 
ATOM   1377 C  CG2  . VAL A 1 174 ? 25.581  -25.500 -3.233  1.00 34.98  ?  176 VAL A CG2  1 
ATOM   1378 N  N    . THR A 1 175 ? 26.354  -23.344 -7.298  1.00 31.80  ?  177 THR A N    1 
ATOM   1379 C  CA   . THR A 1 175 ? 27.075  -22.471 -8.232  1.00 34.09  ?  177 THR A CA   1 
ATOM   1380 C  C    . THR A 1 175 ? 26.118  -21.439 -8.843  1.00 32.84  ?  177 THR A C    1 
ATOM   1381 O  O    . THR A 1 175 ? 26.524  -20.289 -9.049  1.00 34.57  ?  177 THR A O    1 
ATOM   1382 C  CB   . THR A 1 175 ? 27.919  -23.293 -9.233  1.00 39.14  ?  177 THR A CB   1 
ATOM   1383 O  OG1  . THR A 1 175 ? 27.076  -24.151 -9.999  1.00 43.67  ?  177 THR A OG1  1 
ATOM   1384 C  CG2  . THR A 1 175 ? 28.930  -24.134 -8.551  1.00 38.95  ?  177 THR A CG2  1 
ATOM   1385 N  N    . HIS A 1 176 ? 24.862  -21.800 -9.105  1.00 31.03  ?  178 HIS A N    1 
ATOM   1386 C  CA   . HIS A 1 176 ? 23.880  -20.859 -9.635  1.00 30.35  ?  178 HIS A CA   1 
ATOM   1387 C  C    . HIS A 1 176 ? 23.614  -19.766 -8.602  1.00 29.53  ?  178 HIS A C    1 
ATOM   1388 O  O    . HIS A 1 176 ? 23.595  -18.606 -8.949  1.00 29.80  ?  178 HIS A O    1 
ATOM   1389 C  CB   . HIS A 1 176 ? 22.544  -21.523 -9.982  1.00 30.14  ?  178 HIS A CB   1 
ATOM   1390 C  CG   . HIS A 1 176 ? 21.519  -20.586 -10.519 1.00 35.14  ?  178 HIS A CG   1 
ATOM   1391 N  ND1  . HIS A 1 176 ? 21.581  -20.091 -11.798 1.00 37.09  ?  178 HIS A ND1  1 
ATOM   1392 C  CD2  . HIS A 1 176 ? 20.432  -20.070 -9.917  1.00 36.77  ?  178 HIS A CD2  1 
ATOM   1393 C  CE1  . HIS A 1 176 ? 20.549  -19.292 -11.929 1.00 38.08  ?  178 HIS A CE1  1 
ATOM   1394 N  NE2  . HIS A 1 176 ? 19.813  -19.276 -10.842 1.00 38.17  ?  178 HIS A NE2  1 
ATOM   1395 N  N    . ILE A 1 177 ? 23.376  -20.164 -7.343  1.00 28.03  ?  179 ILE A N    1 
ATOM   1396 C  CA   . ILE A 1 177 ? 23.115  -19.218 -6.272  1.00 28.92  ?  179 ILE A CA   1 
ATOM   1397 C  C    . ILE A 1 177 ? 24.305  -18.231 -6.131  1.00 29.89  ?  179 ILE A C    1 
ATOM   1398 O  O    . ILE A 1 177 ? 24.103  -17.032 -6.044  1.00 29.65  ?  179 ILE A O    1 
ATOM   1399 C  CB   . ILE A 1 177 ? 22.804  -19.946 -4.939  1.00 26.53  ?  179 ILE A CB   1 
ATOM   1400 C  CG1  . ILE A 1 177 ? 21.466  -20.674 -5.006  1.00 25.30  ?  179 ILE A CG1  1 
ATOM   1401 C  CG2  . ILE A 1 177 ? 22.882  -18.904 -3.716  1.00 25.80  ?  179 ILE A CG2  1 
ATOM   1402 C  CD1  . ILE A 1 177 ? 21.271  -21.743 -3.925  1.00 25.09  ?  179 ILE A CD1  1 
ATOM   1403 N  N    . GLY A 1 178 ? 25.504  -18.762 -6.136  1.00 30.05  ?  180 GLY A N    1 
ATOM   1404 C  CA   . GLY A 1 178 ? 26.708  -17.959 -6.045  1.00 31.55  ?  180 GLY A CA   1 
ATOM   1405 C  C    . GLY A 1 178 ? 26.832  -16.901 -7.122  1.00 31.31  ?  180 GLY A C    1 
ATOM   1406 O  O    . GLY A 1 178 ? 27.096  -15.738 -6.838  1.00 30.87  ?  180 GLY A O    1 
ATOM   1407 N  N    . ARG A 1 179 ? 26.627  -17.335 -8.376  1.00 31.64  ?  181 ARG A N    1 
ATOM   1408 C  CA   A ARG A 1 179 ? 26.683  -16.507 -9.564  0.50 31.89  ?  181 ARG A CA   1 
ATOM   1409 C  CA   B ARG A 1 179 ? 26.757  -16.446 -9.510  0.50 31.30  ?  181 ARG A CA   1 
ATOM   1410 C  C    . ARG A 1 179 ? 25.683  -15.338 -9.510  1.00 31.25  ?  181 ARG A C    1 
ATOM   1411 O  O    . ARG A 1 179 ? 26.019  -14.168 -9.764  1.00 30.45  ?  181 ARG A O    1 
ATOM   1412 C  CB   A ARG A 1 179 ? 26.482  -17.418 -10.843 0.50 34.00  ?  181 ARG A CB   1 
ATOM   1413 C  CB   B ARG A 1 179 ? 26.798  -17.261 -10.847 0.50 32.04  ?  181 ARG A CB   1 
ATOM   1414 C  CG   A ARG A 1 179 ? 25.386  -16.948 -11.824 0.50 37.92  ?  181 ARG A CG   1 
ATOM   1415 C  CG   B ARG A 1 179 ? 27.003  -16.351 -12.087 0.50 33.27  ?  181 ARG A CG   1 
ATOM   1416 C  CD   A ARG A 1 179 ? 25.396  -17.649 -13.156 0.50 41.98  ?  181 ARG A CD   1 
ATOM   1417 C  CD   B ARG A 1 179 ? 26.499  -16.882 -13.418 0.50 36.61  ?  181 ARG A CD   1 
ATOM   1418 N  NE   A ARG A 1 179 ? 24.170  -17.344 -13.898 0.50 42.73  ?  181 ARG A NE   1 
ATOM   1419 N  NE   B ARG A 1 179 ? 25.043  -16.741 -13.586 0.50 38.76  ?  181 ARG A NE   1 
ATOM   1420 C  CZ   A ARG A 1 179 ? 23.160  -18.175 -14.149 0.50 42.55  ?  181 ARG A CZ   1 
ATOM   1421 C  CZ   B ARG A 1 179 ? 24.399  -15.612 -13.865 0.50 39.26  ?  181 ARG A CZ   1 
ATOM   1422 N  NH1  A ARG A 1 179 ? 23.193  -19.434 -13.713 0.50 33.86  ?  181 ARG A NH1  1 
ATOM   1423 N  NH1  B ARG A 1 179 ? 25.071  -14.466 -14.005 0.50 39.24  ?  181 ARG A NH1  1 
ATOM   1424 N  NH2  A ARG A 1 179 ? 22.106  -17.756 -14.848 0.50 46.69  ?  181 ARG A NH2  1 
ATOM   1425 N  NH2  B ARG A 1 179 ? 23.075  -15.612 -13.999 0.50 38.29  ?  181 ARG A NH2  1 
ATOM   1426 N  N    . VAL A 1 180 ? 24.426  -15.659 -9.209  1.00 31.21  ?  182 VAL A N    1 
ATOM   1427 C  CA   . VAL A 1 180 ? 23.371  -14.700 -9.154  1.00 30.74  ?  182 VAL A CA   1 
ATOM   1428 C  C    . VAL A 1 180 ? 23.596  -13.743 -7.988  1.00 31.05  ?  182 VAL A C    1 
ATOM   1429 O  O    . VAL A 1 180 ? 23.354  -12.556 -8.141  1.00 30.37  ?  182 VAL A O    1 
ATOM   1430 C  CB   . VAL A 1 180 ? 21.978  -15.343 -9.111  1.00 32.60  ?  182 VAL A CB   1 
ATOM   1431 C  CG1  . VAL A 1 180 ? 20.890  -14.301 -8.915  1.00 33.79  ?  182 VAL A CG1  1 
ATOM   1432 C  CG2  . VAL A 1 180 ? 21.711  -16.183 -10.365 1.00 35.04  ?  182 VAL A CG2  1 
ATOM   1433 N  N    . TYR A 1 181 ? 24.049  -14.265 -6.842  1.00 30.01  ?  183 TYR A N    1 
ATOM   1434 C  CA   . TYR A 1 181 ? 24.284  -13.441 -5.657  1.00 28.67  ?  183 TYR A CA   1 
ATOM   1435 C  C    . TYR A 1 181 ? 25.372  -12.395 -5.927  1.00 29.77  ?  183 TYR A C    1 
ATOM   1436 O  O    . TYR A 1 181 ? 25.192  -11.217 -5.621  1.00 29.80  ?  183 TYR A O    1 
ATOM   1437 C  CB   . TYR A 1 181 ? 24.677  -14.349 -4.503  1.00 26.64  ?  183 TYR A CB   1 
ATOM   1438 C  CG   . TYR A 1 181 ? 24.859  -13.712 -3.150  1.00 26.46  ?  183 TYR A CG   1 
ATOM   1439 C  CD1  . TYR A 1 181 ? 24.062  -12.641 -2.745  1.00 28.62  ?  183 TYR A CD1  1 
ATOM   1440 C  CD2  . TYR A 1 181 ? 25.764  -14.232 -2.242  1.00 29.28  ?  183 TYR A CD2  1 
ATOM   1441 C  CE1  . TYR A 1 181 ? 24.191  -12.085 -1.483  1.00 30.11  ?  183 TYR A CE1  1 
ATOM   1442 C  CE2  . TYR A 1 181 ? 25.907  -13.686 -0.975  1.00 29.62  ?  183 TYR A CE2  1 
ATOM   1443 C  CZ   . TYR A 1 181 ? 25.112  -12.607 -0.598  1.00 30.57  ?  183 TYR A CZ   1 
ATOM   1444 O  OH   . TYR A 1 181 ? 25.224  -12.105 0.677   1.00 30.93  ?  183 TYR A OH   1 
ATOM   1445 N  N    . LYS A 1 182 ? 26.501  -12.820 -6.520  1.00 31.08  ?  184 LYS A N    1 
ATOM   1446 C  CA   . LYS A 1 182 ? 27.587  -11.896 -6.837  1.00 31.63  ?  184 LYS A CA   1 
ATOM   1447 C  C    . LYS A 1 182 ? 27.118  -10.771 -7.795  1.00 33.40  ?  184 LYS A C    1 
ATOM   1448 O  O    . LYS A 1 182 ? 27.455  -9.584  -7.607  1.00 34.73  ?  184 LYS A O    1 
ATOM   1449 C  CB   . LYS A 1 182 ? 28.760  -12.678 -7.435  1.00 34.12  ?  184 LYS A CB   1 
ATOM   1450 C  CG   . LYS A 1 182 ? 29.983  -11.817 -7.692  1.00 38.60  ?  184 LYS A CG   1 
ATOM   1451 C  CD   . LYS A 1 182 ? 31.162  -12.640 -8.141  1.00 45.24  ?  184 LYS A CD   1 
ATOM   1452 C  CE   . LYS A 1 182 ? 32.366  -11.765 -8.394  1.00 50.97  ?  184 LYS A CE   1 
ATOM   1453 N  NZ   . LYS A 1 182 ? 33.586  -12.576 -8.618  1.00 54.72  ?  184 LYS A NZ   1 
ATOM   1454 N  N    . GLU A 1 183 ? 26.340  -11.149 -8.794  1.00 33.18  ?  185 GLU A N    1 
ATOM   1455 C  CA   . GLU A 1 183 ? 25.754  -10.218 -9.748  1.00 35.56  ?  185 GLU A CA   1 
ATOM   1456 C  C    . GLU A 1 183 ? 24.830  -9.231  -9.036  1.00 34.78  ?  185 GLU A C    1 
ATOM   1457 O  O    . GLU A 1 183 ? 24.911  -8.037  -9.273  1.00 34.66  ?  185 GLU A O    1 
ATOM   1458 C  CB   . GLU A 1 183 ? 24.998  -11.025 -10.832 1.00 39.77  ?  185 GLU A CB   1 
ATOM   1459 C  CG   . GLU A 1 183 ? 24.495  -10.276 -12.048 1.00 50.12  ?  185 GLU A CG   1 
ATOM   1460 C  CD   . GLU A 1 183 ? 23.918  -11.209 -13.109 1.00 64.67  ?  185 GLU A CD   1 
ATOM   1461 O  OE1  . GLU A 1 183 ? 23.453  -12.317 -12.752 1.00 69.66  ?  185 GLU A OE1  1 
ATOM   1462 O  OE2  . GLU A 1 183 ? 23.932  -10.833 -14.301 1.00 67.45  ?  185 GLU A OE2  1 
ATOM   1463 N  N    . ARG A 1 184 ? 23.940  -9.729  -8.148  1.00 32.79  ?  186 ARG A N    1 
ATOM   1464 C  CA   . ARG A 1 184 ? 23.026  -8.872  -7.418  1.00 33.25  ?  186 ARG A CA   1 
ATOM   1465 C  C    . ARG A 1 184 ? 23.721  -7.947  -6.404  1.00 35.90  ?  186 ARG A C    1 
ATOM   1466 O  O    . ARG A 1 184 ? 23.214  -6.857  -6.156  1.00 36.83  ?  186 ARG A O    1 
ATOM   1467 C  CB   . ARG A 1 184 ? 21.934  -9.726  -6.743  1.00 34.08  ?  186 ARG A CB   1 
ATOM   1468 C  CG   . ARG A 1 184 ? 20.971  -10.350 -7.748  1.00 35.33  ?  186 ARG A CG   1 
ATOM   1469 C  CD   . ARG A 1 184 ? 19.994  -9.344  -8.336  1.00 36.22  ?  186 ARG A CD   1 
ATOM   1470 N  NE   . ARG A 1 184 ? 19.080  -8.884  -7.308  1.00 36.67  ?  186 ARG A NE   1 
ATOM   1471 C  CZ   . ARG A 1 184 ? 17.854  -9.365  -7.068  1.00 38.51  ?  186 ARG A CZ   1 
ATOM   1472 N  NH1  . ARG A 1 184 ? 17.349  -10.335 -7.819  1.00 36.88  ?  186 ARG A NH1  1 
ATOM   1473 N  NH2  . ARG A 1 184 ? 17.118  -8.855  -6.090  1.00 38.10  ?  186 ARG A NH2  1 
ATOM   1474 N  N    . LEU A 1 185 ? 24.857  -8.350  -5.840  1.00 37.05  ?  187 LEU A N    1 
ATOM   1475 C  CA   . LEU A 1 185 ? 25.660  -7.479  -4.967  1.00 38.70  ?  187 LEU A CA   1 
ATOM   1476 C  C    . LEU A 1 185 ? 26.431  -6.392  -5.776  1.00 42.07  ?  187 LEU A C    1 
ATOM   1477 O  O    . LEU A 1 185 ? 26.898  -5.439  -5.172  1.00 42.57  ?  187 LEU A O    1 
ATOM   1478 C  CB   . LEU A 1 185 ? 26.673  -8.312  -4.164  1.00 36.96  ?  187 LEU A CB   1 
ATOM   1479 C  CG   . LEU A 1 185 ? 26.120  -9.226  -3.078  1.00 37.07  ?  187 LEU A CG   1 
ATOM   1480 C  CD1  . LEU A 1 185 ? 27.205  -10.201 -2.570  1.00 37.14  ?  187 LEU A CD1  1 
ATOM   1481 C  CD2  . LEU A 1 185 ? 25.458  -8.422  -1.960  1.00 35.92  ?  187 LEU A CD2  1 
ATOM   1482 N  N    . GLY A 1 186 ? 26.552  -6.551  -7.088  1.00 44.67  ?  188 GLY A N    1 
ATOM   1483 C  CA   . GLY A 1 186 ? 27.300  -5.642  -7.946  1.00 48.25  ?  188 GLY A CA   1 
ATOM   1484 C  C    . GLY A 1 186 ? 28.807  -5.768  -7.805  1.00 53.12  ?  188 GLY A C    1 
ATOM   1485 O  O    . GLY A 1 186 ? 29.545  -4.831  -8.147  1.00 53.30  ?  188 GLY A O    1 
ATOM   1486 N  N    . LEU A 1 187 ? 29.300  -6.924  -7.324  1.00 55.98  ?  189 LEU A N    1 
ATOM   1487 C  CA   . LEU A 1 187 ? 30.738  -7.069  -7.076  1.00 59.31  ?  189 LEU A CA   1 
ATOM   1488 C  C    . LEU A 1 187 ? 31.558  -7.196  -8.378  1.00 63.09  ?  189 LEU A C    1 
ATOM   1489 O  O    . LEU A 1 187 ? 31.113  -7.896  -9.295  1.00 63.78  ?  189 LEU A O    1 
ATOM   1490 C  CB   . LEU A 1 187 ? 30.988  -8.302  -6.207  1.00 59.53  ?  189 LEU A CB   1 
ATOM   1491 C  CG   . LEU A 1 187 ? 30.495  -8.277  -4.774  1.00 60.35  ?  189 LEU A CG   1 
ATOM   1492 C  CD1  . LEU A 1 187 ? 30.886  -9.542  -4.080  1.00 60.19  ?  189 LEU A CD1  1 
ATOM   1493 C  CD2  . LEU A 1 187 ? 31.063  -7.105  -4.003  1.00 62.22  ?  189 LEU A CD2  1 
ATOM   1494 N  N    . PRO A 1 188 ? 32.755  -6.556  -8.502  1.00 65.43  ?  190 PRO A N    1 
ATOM   1495 C  CA   . PRO A 1 188 ? 33.587  -6.818  -9.695  1.00 66.93  ?  190 PRO A CA   1 
ATOM   1496 C  C    . PRO A 1 188 ? 33.999  -8.283  -9.826  1.00 68.47  ?  190 PRO A C    1 
ATOM   1497 O  O    . PRO A 1 188 ? 34.198  -8.932  -8.796  1.00 69.24  ?  190 PRO A O    1 
ATOM   1498 C  CB   . PRO A 1 188 ? 34.826  -5.943  -9.480  1.00 67.64  ?  190 PRO A CB   1 
ATOM   1499 C  CG   . PRO A 1 188 ? 34.454  -4.953  -8.456  1.00 67.39  ?  190 PRO A CG   1 
ATOM   1500 C  CD   . PRO A 1 188 ? 33.398  -5.578  -7.601  1.00 65.12  ?  190 PRO A CD   1 
ATOM   1501 N  N    . PRO A 1 189 ? 34.139  -8.844  -11.051 1.00 68.67  ?  191 PRO A N    1 
ATOM   1502 C  CA   . PRO A 1 189 ? 34.679  -10.217 -11.166 1.00 68.56  ?  191 PRO A CA   1 
ATOM   1503 C  C    . PRO A 1 189 ? 35.983  -10.471 -10.419 1.00 67.15  ?  191 PRO A C    1 
ATOM   1504 O  O    . PRO A 1 189 ? 36.254  -11.619 -10.074 1.00 67.85  ?  191 PRO A O    1 
ATOM   1505 C  CB   . PRO A 1 189 ? 34.853  -10.419 -12.685 1.00 69.71  ?  191 PRO A CB   1 
ATOM   1506 C  CG   . PRO A 1 189 ? 34.657  -9.087  -13.303 1.00 70.23  ?  191 PRO A CG   1 
ATOM   1507 C  CD   . PRO A 1 189 ? 33.804  -8.287  -12.376 1.00 68.48  ?  191 PRO A CD   1 
ATOM   1508 N  N    . LYS A 1 190 ? 36.777  -9.423  -10.141 1.00 65.49  ?  192 LYS A N    1 
ATOM   1509 C  CA   . LYS A 1 190 ? 38.043  -9.586  -9.421  1.00 64.99  ?  192 LYS A CA   1 
ATOM   1510 C  C    . LYS A 1 190 ? 37.838  -9.964  -7.963  1.00 64.55  ?  192 LYS A C    1 
ATOM   1511 O  O    . LYS A 1 190 ? 38.664  -10.696 -7.405  1.00 64.79  ?  192 LYS A O    1 
ATOM   1512 C  CB   . LYS A 1 190 ? 38.904  -8.319  -9.513  1.00 66.62  ?  192 LYS A CB   1 
ATOM   1513 C  CG   . LYS A 1 190 ? 39.334  -7.973  -10.961 1.00 69.57  ?  192 LYS A CG   1 
ATOM   1514 C  CD   . LYS A 1 190 ? 39.362  -6.466  -11.282 1.00 73.85  ?  192 LYS A CD   1 
ATOM   1515 C  CE   . LYS A 1 190 ? 37.998  -5.778  -11.386 1.00 77.17  ?  192 LYS A CE   1 
ATOM   1516 N  NZ   . LYS A 1 190 ? 37.134  -6.340  -12.460 1.00 77.90  ?  192 LYS A NZ   1 
ATOM   1517 N  N    . ILE A 1 191 ? 36.748  -9.482  -7.336  1.00 63.79  ?  193 ILE A N    1 
ATOM   1518 C  CA   . ILE A 1 191 ? 36.465  -9.859  -5.949  1.00 63.59  ?  193 ILE A CA   1 
ATOM   1519 C  C    . ILE A 1 191 ? 35.792  -11.225 -5.977  1.00 63.83  ?  193 ILE A C    1 
ATOM   1520 O  O    . ILE A 1 191 ? 34.649  -11.306 -6.397  1.00 63.11  ?  193 ILE A O    1 
ATOM   1521 C  CB   . ILE A 1 191 ? 35.594  -8.810  -5.242  1.00 63.70  ?  193 ILE A CB   1 
ATOM   1522 C  CG1  . ILE A 1 191 ? 36.252  -7.405  -5.251  1.00 64.06  ?  193 ILE A CG1  1 
ATOM   1523 C  CG2  . ILE A 1 191 ? 35.277  -9.256  -3.798  1.00 64.12  ?  193 ILE A CG2  1 
ATOM   1524 C  CD1  . ILE A 1 191 ? 37.669  -7.311  -4.561  1.00 64.80  ?  193 ILE A CD1  1 
ATOM   1525 N  N    . VAL A 1 192 ? 36.507  -12.294 -5.555  1.00 64.23  ?  194 VAL A N    1 
ATOM   1526 C  CA   . VAL A 1 192 ? 35.995  -13.677 -5.597  1.00 64.22  ?  194 VAL A CA   1 
ATOM   1527 C  C    . VAL A 1 192 ? 35.313  -14.033 -4.273  1.00 62.28  ?  194 VAL A C    1 
ATOM   1528 O  O    . VAL A 1 192 ? 35.898  -13.790 -3.215  1.00 64.37  ?  194 VAL A O    1 
ATOM   1529 C  CB   . VAL A 1 192 ? 37.088  -14.704 -5.978  1.00 66.41  ?  194 VAL A CB   1 
ATOM   1530 C  CG1  . VAL A 1 192 ? 37.800  -14.297 -7.266  1.00 68.07  ?  194 VAL A CG1  1 
ATOM   1531 C  CG2  . VAL A 1 192 ? 38.083  -14.911 -4.846  1.00 67.20  ?  194 VAL A CG2  1 
ATOM   1532 N  N    . ILE A 1 193 ? 34.045  -14.555 -4.302  1.00 57.18  ?  195 ILE A N    1 
ATOM   1533 C  CA   . ILE A 1 193 ? 33.319  -15.061 -3.122  1.00 52.22  ?  195 ILE A CA   1 
ATOM   1534 C  C    . ILE A 1 193 ? 33.522  -16.601 -3.079  1.00 46.48  ?  195 ILE A C    1 
ATOM   1535 O  O    . ILE A 1 193 ? 33.561  -17.253 -4.104  1.00 44.99  ?  195 ILE A O    1 
ATOM   1536 C  CB   . ILE A 1 193 ? 31.802  -14.603 -3.079  1.00 53.30  ?  195 ILE A CB   1 
ATOM   1537 C  CG1  . ILE A 1 193 ? 30.925  -15.261 -4.183  1.00 54.23  ?  195 ILE A CG1  1 
ATOM   1538 C  CG2  . ILE A 1 193 ? 31.692  -13.087 -3.171  1.00 53.88  ?  195 ILE A CG2  1 
ATOM   1539 C  CD1  . ILE A 1 193 ? 29.292  -14.874 -4.108  1.00 54.97  ?  195 ILE A CD1  1 
ATOM   1540 N  N    . GLY A 1 194 ? 33.677  -17.159 -1.890  1.00 43.77  ?  196 GLY A N    1 
ATOM   1541 C  CA   . GLY A 1 194 ? 33.889  -18.586 -1.680  1.00 41.16  ?  196 GLY A CA   1 
ATOM   1542 C  C    . GLY A 1 194 ? 32.691  -19.213 -0.999  1.00 38.14  ?  196 GLY A C    1 
ATOM   1543 O  O    . GLY A 1 194 ? 31.999  -18.553 -0.192  1.00 37.29  ?  196 GLY A O    1 
ATOM   1544 N  N    . TYR A 1 195 ? 32.432  -20.483 -1.324  1.00 35.73  ?  197 TYR A N    1 
ATOM   1545 C  CA   . TYR A 1 195 ? 31.442  -21.320 -0.653  1.00 35.43  ?  197 TYR A CA   1 
ATOM   1546 C  C    . TYR A 1 195 ? 32.160  -22.322 0.234   1.00 37.54  ?  197 TYR A C    1 
ATOM   1547 O  O    . TYR A 1 195 ? 33.040  -23.111 -0.228  1.00 38.69  ?  197 TYR A O    1 
ATOM   1548 C  CB   . TYR A 1 195 ? 30.534  -22.020 -1.675  1.00 33.90  ?  197 TYR A CB   1 
ATOM   1549 C  CG   . TYR A 1 195 ? 29.401  -22.846 -1.077  1.00 31.88  ?  197 TYR A CG   1 
ATOM   1550 C  CD1  . TYR A 1 195 ? 29.591  -24.182 -0.729  1.00 34.64  ?  197 TYR A CD1  1 
ATOM   1551 C  CD2  . TYR A 1 195 ? 28.141  -22.296 -0.883  1.00 33.20  ?  197 TYR A CD2  1 
ATOM   1552 C  CE1  . TYR A 1 195 ? 28.559  -24.941 -0.159  1.00 35.12  ?  197 TYR A CE1  1 
ATOM   1553 C  CE2  . TYR A 1 195 ? 27.101  -23.034 -0.315  1.00 35.04  ?  197 TYR A CE2  1 
ATOM   1554 C  CZ   . TYR A 1 195 ? 27.304  -24.375 0.016   1.00 36.72  ?  197 TYR A CZ   1 
ATOM   1555 O  OH   . TYR A 1 195 ? 26.279  -25.143 0.540   1.00 37.67  ?  197 TYR A OH   1 
ATOM   1556 N  N    . GLN A 1 196 ? 31.818  -22.310 1.498   1.00 36.43  ?  198 GLN A N    1 
ATOM   1557 C  CA   . GLN A 1 196 ? 32.418  -23.167 2.492   1.00 37.47  ?  198 GLN A CA   1 
ATOM   1558 C  C    . GLN A 1 196 ? 31.343  -24.068 3.083   1.00 36.05  ?  198 GLN A C    1 
ATOM   1559 O  O    . GLN A 1 196 ? 30.268  -23.607 3.507   1.00 34.57  ?  198 GLN A O    1 
ATOM   1560 C  CB   . GLN A 1 196 ? 33.052  -22.346 3.650   1.00 42.40  ?  198 GLN A CB   1 
ATOM   1561 C  CG   . GLN A 1 196 ? 34.036  -21.237 3.223   1.00 54.30  ?  198 GLN A CG   1 
ATOM   1562 C  CD   . GLN A 1 196 ? 34.196  -20.149 4.281   1.00 68.02  ?  198 GLN A CD   1 
ATOM   1563 O  OE1  . GLN A 1 196 ? 33.338  -19.953 5.161   1.00 71.57  ?  198 GLN A OE1  1 
ATOM   1564 N  NE2  . GLN A 1 196 ? 35.299  -19.408 4.219   1.00 71.80  ?  198 GLN A NE2  1 
ATOM   1565 N  N    . SER A 1 197 ? 31.650  -25.377 3.103   1.00 33.41  ?  199 SER A N    1 
ATOM   1566 C  CA   . SER A 1 197 ? 30.866  -26.368 3.820   1.00 33.96  ?  199 SER A CA   1 
ATOM   1567 C  C    . SER A 1 197 ? 30.807  -25.972 5.320   1.00 33.16  ?  199 SER A C    1 
ATOM   1568 O  O    . SER A 1 197 ? 31.843  -25.541 5.859   1.00 34.27  ?  199 SER A O    1 
ATOM   1569 C  CB   . SER A 1 197 ? 31.538  -27.744 3.659   1.00 36.02  ?  199 SER A CB   1 
ATOM   1570 O  OG   . SER A 1 197 ? 30.979  -28.691 4.527   1.00 42.08  ?  199 SER A OG   1 
ATOM   1571 N  N    . HIS A 1 198 ? 29.650  -26.092 5.982   1.00 31.73  ?  200 HIS A N    1 
ATOM   1572 C  CA   . HIS A 1 198 ? 29.601  -25.836 7.419   1.00 32.41  ?  200 HIS A CA   1 
ATOM   1573 C  C    . HIS A 1 198 ? 30.479  -26.820 8.224   1.00 36.72  ?  200 HIS A C    1 
ATOM   1574 O  O    . HIS A 1 198 ? 31.124  -26.419 9.187   1.00 37.24  ?  200 HIS A O    1 
ATOM   1575 C  CB   . HIS A 1 198 ? 28.161  -25.902 7.909   1.00 31.32  ?  200 HIS A CB   1 
ATOM   1576 C  CG   . HIS A 1 198 ? 27.261  -24.806 7.394   1.00 31.24  ?  200 HIS A CG   1 
ATOM   1577 N  ND1  . HIS A 1 198 ? 27.682  -23.520 7.285   1.00 32.98  ?  200 HIS A ND1  1 
ATOM   1578 C  CD2  . HIS A 1 198 ? 25.986  -24.873 6.972   1.00 30.89  ?  200 HIS A CD2  1 
ATOM   1579 C  CE1  . HIS A 1 198 ? 26.647  -22.829 6.838   1.00 32.11  ?  200 HIS A CE1  1 
ATOM   1580 N  NE2  . HIS A 1 198 ? 25.605  -23.604 6.633   1.00 32.23  ?  200 HIS A NE2  1 
ATOM   1581 N  N    . ALA A 1 199 ? 30.495  -28.101 7.813   1.00 39.85  ?  201 ALA A N    1 
ATOM   1582 C  CA   . ALA A 1 199 ? 31.396  -29.137 8.356   1.00 43.28  ?  201 ALA A CA   1 
ATOM   1583 C  C    . ALA A 1 199 ? 32.869  -28.704 8.289   1.00 46.35  ?  201 ALA A C    1 
ATOM   1584 O  O    . ALA A 1 199 ? 33.586  -28.970 9.238   1.00 48.17  ?  201 ALA A O    1 
ATOM   1585 C  CB   . ALA A 1 199 ? 31.199  -30.442 7.626   1.00 44.02  ?  201 ALA A CB   1 
ATOM   1586 N  N    . ASP A 1 200 ? 33.324  -28.028 7.223   1.00 46.51  ?  202 ASP A N    1 
ATOM   1587 C  CA   . ASP A 1 200 ? 34.716  -27.561 7.158   1.00 46.40  ?  202 ASP A CA   1 
ATOM   1588 C  C    . ASP A 1 200 ? 34.918  -26.341 8.037   1.00 46.53  ?  202 ASP A C    1 
ATOM   1589 O  O    . ASP A 1 200 ? 35.931  -26.271 8.742   1.00 46.87  ?  202 ASP A O    1 
ATOM   1590 C  CB   . ASP A 1 200 ? 35.169  -27.287 5.703   1.00 47.47  ?  202 ASP A CB   1 
ATOM   1591 C  CG   . ASP A 1 200 ? 35.190  -28.560 4.835   1.00 51.69  ?  202 ASP A CG   1 
ATOM   1592 O  OD1  . ASP A 1 200 ? 35.247  -29.659 5.400   1.00 54.62  ?  202 ASP A OD1  1 
ATOM   1593 O  OD2  . ASP A 1 200 ? 35.133  -28.442 3.588   1.00 51.54  ?  202 ASP A OD2  1 
ATOM   1594 N  N    . THR A 1 201 ? 33.967  -25.371 8.015   1.00 46.63  ?  203 THR A N    1 
ATOM   1595 C  CA   . THR A 1 201 ? 34.058  -24.189 8.857   1.00 47.98  ?  203 THR A CA   1 
ATOM   1596 C  C    . THR A 1 201 ? 34.173  -24.545 10.341  1.00 52.43  ?  203 THR A C    1 
ATOM   1597 O  O    . THR A 1 201 ? 34.946  -23.907 11.053  1.00 54.09  ?  203 THR A O    1 
ATOM   1598 C  CB   . THR A 1 201 ? 32.860  -23.272 8.639   1.00 47.58  ?  203 THR A CB   1 
ATOM   1599 O  OG1  . THR A 1 201 ? 32.836  -22.889 7.278   1.00 47.40  ?  203 THR A OG1  1 
ATOM   1600 C  CG2  . THR A 1 201 ? 32.913  -22.003 9.519   1.00 47.81  ?  203 THR A CG2  1 
ATOM   1601 N  N    . ALA A 1 202 ? 33.395  -25.550 10.781  1.00 53.66  ?  204 ALA A N    1 
ATOM   1602 C  CA   . ALA A 1 202 ? 33.364  -26.038 12.160  1.00 55.67  ?  204 ALA A CA   1 
ATOM   1603 C  C    . ALA A 1 202 ? 34.725  -26.501 12.659  1.00 57.87  ?  204 ALA A C    1 
ATOM   1604 O  O    . ALA A 1 202 ? 35.008  -26.329 13.841  1.00 59.02  ?  204 ALA A O    1 
ATOM   1605 C  CB   . ALA A 1 202 ? 32.389  -27.195 12.271  1.00 55.41  ?  204 ALA A CB   1 
ATOM   1606 N  N    . THR A 1 203 ? 35.551  -27.100 11.788  1.00 57.89  ?  205 THR A N    1 
ATOM   1607 C  CA   . THR A 1 203 ? 36.836  -27.647 12.205  1.00 58.12  ?  205 THR A CA   1 
ATOM   1608 C  C    . THR A 1 203 ? 37.940  -26.610 11.993  1.00 54.76  ?  205 THR A C    1 
ATOM   1609 O  O    . THR A 1 203 ? 38.114  -26.105 10.876  1.00 54.29  ?  205 THR A O    1 
ATOM   1610 C  CB   . THR A 1 203 ? 37.142  -28.950 11.452  1.00 62.44  ?  205 THR A CB   1 
ATOM   1611 O  OG1  . THR A 1 203 ? 37.043  -28.717 10.042  1.00 65.30  ?  205 THR A OG1  1 
ATOM   1612 C  CG2  . THR A 1 203 ? 36.232  -30.101 11.856  1.00 63.66  ?  205 THR A CG2  1 
ATOM   1613 N  N    . LYS A 1 204 ? 38.682  -26.296 13.073  1.00 51.81  ?  206 LYS A N    1 
ATOM   1614 C  CA   . LYS A 1 204 ? 39.759  -25.309 13.037  1.00 50.43  ?  206 LYS A CA   1 
ATOM   1615 C  C    . LYS A 1 204 ? 41.099  -26.034 12.811  1.00 49.14  ?  206 LYS A C    1 
ATOM   1616 O  O    . LYS A 1 204 ? 41.624  -26.733 13.701  1.00 46.97  ?  206 LYS A O    1 
ATOM   1617 C  CB   . LYS A 1 204 ? 39.797  -24.458 14.326  1.00 52.37  ?  206 LYS A CB   1 
ATOM   1618 C  CG   . LYS A 1 204 ? 38.456  -23.820 14.751  1.00 56.91  ?  206 LYS A CG   1 
ATOM   1619 C  CD   . LYS A 1 204 ? 38.058  -22.649 13.889  1.00 63.41  ?  206 LYS A CD   1 
ATOM   1620 C  CE   . LYS A 1 204 ? 37.424  -21.482 14.657  1.00 68.51  ?  206 LYS A CE   1 
ATOM   1621 N  NZ   . LYS A 1 204 ? 37.655  -20.149 13.973  1.00 70.08  ?  206 LYS A NZ   1 
ATOM   1622 N  N    . SER A 1 205 ? 41.663  -25.836 11.602  1.00 50.80  ?  207 SER A N    1 
ATOM   1623 C  CA   . SER A 1 205 ? 42.831  -26.586 11.126  1.00 53.00  ?  207 SER A CA   1 
ATOM   1624 C  C    . SER A 1 205 ? 44.037  -25.687 10.800  1.00 53.64  ?  207 SER A C    1 
ATOM   1625 O  O    . SER A 1 205 ? 44.970  -26.173 10.154  1.00 53.25  ?  207 SER A O    1 
ATOM   1626 C  CB   . SER A 1 205 ? 42.455  -27.395 9.880   1.00 55.85  ?  207 SER A CB   1 
ATOM   1627 O  OG   . SER A 1 205 ? 41.514  -28.402 10.218  1.00 59.90  ?  207 SER A OG   1 
ATOM   1628 N  N    . GLY A 1 206 ? 44.025  -24.425 11.242  1.00 54.58  ?  208 GLY A N    1 
ATOM   1629 C  CA   . GLY A 1 206 ? 45.070  -23.452 10.943  1.00 57.78  ?  208 GLY A CA   1 
ATOM   1630 C  C    . GLY A 1 206 ? 44.502  -22.139 10.453  1.00 61.95  ?  208 GLY A C    1 
ATOM   1631 O  O    . GLY A 1 206 ? 43.528  -21.613 11.024  1.00 62.48  ?  208 GLY A O    1 
ATOM   1632 N  N    . SER A 1 207 ? 45.099  -21.639 9.359   1.00 65.01  ?  209 SER A N    1 
ATOM   1633 C  CA   . SER A 1 207 ? 44.981  -20.263 8.863   1.00 68.16  ?  209 SER A CA   1 
ATOM   1634 C  C    . SER A 1 207 ? 43.718  -19.966 8.021   1.00 71.00  ?  209 SER A C    1 
ATOM   1635 O  O    . SER A 1 207 ? 43.358  -18.789 7.916   1.00 71.88  ?  209 SER A O    1 
ATOM   1636 C  CB   . SER A 1 207 ? 46.222  -19.901 8.046   1.00 69.59  ?  209 SER A CB   1 
ATOM   1637 O  OG   . SER A 1 207 ? 46.122  -18.598 7.498   1.00 73.22  ?  209 SER A OG   1 
ATOM   1638 N  N    . THR A 1 208 ? 43.051  -20.984 7.404   1.00 71.54  ?  210 THR A N    1 
ATOM   1639 C  CA   . THR A 1 208 ? 41.841  -20.725 6.593   1.00 71.94  ?  210 THR A CA   1 
ATOM   1640 C  C    . THR A 1 208 ? 41.003  -21.995 6.437   1.00 71.29  ?  210 THR A C    1 
ATOM   1641 O  O    . THR A 1 208 ? 41.512  -23.107 6.637   1.00 72.32  ?  210 THR A O    1 
ATOM   1642 C  CB   . THR A 1 208 ? 42.188  -20.132 5.182   1.00 73.97  ?  210 THR A CB   1 
ATOM   1643 O  OG1  . THR A 1 208 ? 43.255  -19.170 5.275   1.00 75.68  ?  210 THR A OG1  1 
ATOM   1644 C  CG2  . THR A 1 208 ? 40.954  -19.485 4.490   1.00 73.88  ?  210 THR A CG2  1 
ATOM   1645 N  N    . THR A 1 209 ? 39.705  -21.817 6.093   1.00 69.20  ?  211 THR A N    1 
ATOM   1646 C  CA   . THR A 1 209 ? 38.791  -22.898 5.725   1.00 67.81  ?  211 THR A CA   1 
ATOM   1647 C  C    . THR A 1 209 ? 38.899  -23.174 4.205   1.00 66.96  ?  211 THR A C    1 
ATOM   1648 O  O    . THR A 1 209 ? 39.114  -22.248 3.417   1.00 66.76  ?  211 THR A O    1 
ATOM   1649 C  CB   . THR A 1 209 ? 37.347  -22.497 6.099   1.00 68.39  ?  211 THR A CB   1 
ATOM   1650 O  OG1  . THR A 1 209 ? 37.295  -22.192 7.505   1.00 68.36  ?  211 THR A OG1  1 
ATOM   1651 C  CG2  . THR A 1 209 ? 36.336  -23.578 5.747   1.00 68.77  ?  211 THR A CG2  1 
ATOM   1652 N  N    . LYS A 1 210 ? 38.735  -24.441 3.800   1.00 66.16  ?  212 LYS A N    1 
ATOM   1653 C  CA   . LYS A 1 210 ? 38.690  -24.775 2.386   1.00 65.89  ?  212 LYS A CA   1 
ATOM   1654 C  C    . LYS A 1 210 ? 37.382  -24.258 1.748   1.00 64.20  ?  212 LYS A C    1 
ATOM   1655 O  O    . LYS A 1 210 ? 36.280  -24.517 2.247   1.00 64.20  ?  212 LYS A O    1 
ATOM   1656 C  CB   . LYS A 1 210 ? 38.872  -26.292 2.170   1.00 69.14  ?  212 LYS A CB   1 
ATOM   1657 C  CG   . LYS A 1 210 ? 40.244  -26.797 2.603   1.00 74.95  ?  212 LYS A CG   1 
ATOM   1658 C  CD   . LYS A 1 210 ? 40.473  -28.259 2.189   1.00 80.82  ?  212 LYS A CD   1 
ATOM   1659 C  CE   . LYS A 1 210 ? 41.841  -28.801 2.576   1.00 84.06  ?  212 LYS A CE   1 
ATOM   1660 N  NZ   . LYS A 1 210 ? 41.806  -29.674 3.793   1.00 85.52  ?  212 LYS A NZ   1 
ATOM   1661 N  N    . ASN A 1 211 ? 37.518  -23.496 0.655   1.00 62.45  ?  213 ASN A N    1 
ATOM   1662 C  CA   . ASN A 1 211 ? 36.400  -23.241 -0.223  1.00 61.21  ?  213 ASN A CA   1 
ATOM   1663 C  C    . ASN A 1 211 ? 36.206  -24.475 -1.066  1.00 61.28  ?  213 ASN A C    1 
ATOM   1664 O  O    . ASN A 1 211 ? 37.183  -24.933 -1.685  1.00 62.22  ?  213 ASN A O    1 
ATOM   1665 C  CB   . ASN A 1 211 ? 36.661  -22.031 -1.116  1.00 61.54  ?  213 ASN A CB   1 
ATOM   1666 C  CG   . ASN A 1 211 ? 36.664  -20.714 -0.369  1.00 63.79  ?  213 ASN A CG   1 
ATOM   1667 O  OD1  . ASN A 1 211 ? 36.033  -20.566 0.685   1.00 62.92  ?  213 ASN A OD1  1 
ATOM   1668 N  ND2  . ASN A 1 211 ? 37.340  -19.711 -0.869  1.00 66.36  ?  213 ASN A ND2  1 
ATOM   1669 N  N    . ARG A 1 212 ? 34.991  -25.047 -1.116  1.00 60.47  ?  214 ARG A N    1 
ATOM   1670 C  CA   . ARG A 1 212 ? 34.736  -26.098 -2.106  1.00 61.57  ?  214 ARG A CA   1 
ATOM   1671 C  C    . ARG A 1 212 ? 34.292  -25.546 -3.464  1.00 60.46  ?  214 ARG A C    1 
ATOM   1672 O  O    . ARG A 1 212 ? 34.462  -26.239 -4.463  1.00 61.05  ?  214 ARG A O    1 
ATOM   1673 C  CB   . ARG A 1 212 ? 33.791  -27.155 -1.602  1.00 65.30  ?  214 ARG A CB   1 
ATOM   1674 C  CG   . ARG A 1 212 ? 32.399  -26.659 -1.348  1.00 70.17  ?  214 ARG A CG   1 
ATOM   1675 C  CD   . ARG A 1 212 ? 31.572  -27.813 -0.910  1.00 74.22  ?  214 ARG A CD   1 
ATOM   1676 N  NE   . ARG A 1 212 ? 31.333  -28.744 -2.011  1.00 78.05  ?  214 ARG A NE   1 
ATOM   1677 C  CZ   . ARG A 1 212 ? 30.888  -29.991 -1.886  1.00 79.12  ?  214 ARG A CZ   1 
ATOM   1678 N  NH1  . ARG A 1 212 ? 30.700  -30.743 -2.961  1.00 77.58  ?  214 ARG A NH1  1 
ATOM   1679 N  NH2  . ARG A 1 212 ? 30.621  -30.493 -0.683  1.00 79.08  ?  214 ARG A NH2  1 
ATOM   1680 N  N    . PHE A 1 213 ? 33.724  -24.312 -3.510  1.00 58.27  ?  215 PHE A N    1 
ATOM   1681 C  CA   . PHE A 1 213 ? 33.471  -23.624 -4.771  1.00 56.82  ?  215 PHE A CA   1 
ATOM   1682 C  C    . PHE A 1 213 ? 33.843  -22.140 -4.646  1.00 56.72  ?  215 PHE A C    1 
ATOM   1683 O  O    . PHE A 1 213 ? 33.867  -21.569 -3.541  1.00 55.17  ?  215 PHE A O    1 
ATOM   1684 C  CB   . PHE A 1 213 ? 31.993  -23.750 -5.207  1.00 55.12  ?  215 PHE A CB   1 
ATOM   1685 C  CG   . PHE A 1 213 ? 31.370  -25.130 -5.097  1.00 55.05  ?  215 PHE A CG   1 
ATOM   1686 C  CD1  . PHE A 1 213 ? 31.746  -26.155 -5.959  1.00 56.31  ?  215 PHE A CD1  1 
ATOM   1687 C  CD2  . PHE A 1 213 ? 30.451  -25.422 -4.103  1.00 55.20  ?  215 PHE A CD2  1 
ATOM   1688 C  CE1  . PHE A 1 213 ? 31.194  -27.439 -5.830  1.00 56.88  ?  215 PHE A CE1  1 
ATOM   1689 C  CE2  . PHE A 1 213 ? 29.854  -26.699 -4.009  1.00 56.22  ?  215 PHE A CE2  1 
ATOM   1690 C  CZ   . PHE A 1 213 ? 30.230  -27.707 -4.866  1.00 57.00  ?  215 PHE A CZ   1 
ATOM   1691 N  N    . VAL A 1 214 ? 34.132  -21.518 -5.789  1.00 57.20  ?  216 VAL A N    1 
ATOM   1692 C  CA   . VAL A 1 214 ? 34.425  -20.085 -5.892  1.00 59.41  ?  216 VAL A CA   1 
ATOM   1693 C  C    . VAL A 1 214 ? 33.677  -19.523 -7.109  1.00 61.35  ?  216 VAL A C    1 
ATOM   1694 O  O    . VAL A 1 214 ? 33.536  -20.222 -8.112  1.00 62.26  ?  216 VAL A O    1 
ATOM   1695 C  CB   . VAL A 1 214 ? 35.957  -19.826 -5.995  1.00 60.88  ?  216 VAL A CB   1 
ATOM   1696 C  CG1  . VAL A 1 214 ? 36.267  -18.391 -6.428  1.00 62.68  ?  216 VAL A CG1  1 
ATOM   1697 C  CG2  . VAL A 1 214 ? 36.649  -20.132 -4.684  1.00 61.49  ?  216 VAL A CG2  1 
ATOM   1698 N  N    . VAL A 1 215 ? 33.209  -18.268 -7.028  1.00 61.33  ?  217 VAL A N    1 
ATOM   1699 C  CA   . VAL A 1 215 ? 32.705  -17.533 -8.186  1.00 62.98  ?  217 VAL A CA   1 
ATOM   1700 C  C    . VAL A 1 215 ? 33.192  -16.069 -8.099  1.00 64.81  ?  217 VAL A C    1 
ATOM   1701 O  O    . VAL A 1 215 ? 33.227  -15.408 -9.167  1.00 65.96  ?  217 VAL A O    1 
ATOM   1702 C  CB   . VAL A 1 215 ? 31.156  -17.586 -8.331  1.00 64.09  ?  217 VAL A CB   1 
ATOM   1703 C  CG1  . VAL A 1 215 ? 30.628  -19.040 -8.459  1.00 65.65  ?  217 VAL A CG1  1 
ATOM   1704 C  CG2  . VAL A 1 215 ? 30.477  -16.846 -7.194  1.00 63.82  ?  217 VAL A CG2  1 
ATOM   1705 O  OXT  . VAL A 1 215 ? 33.514  -15.558 -6.983  1.00 63.00  ?  217 VAL A OXT  1 
ATOM   1706 N  N    . HIS B 1 7   ? -1.223  -15.171 5.392   1.00 64.09  ?  9   HIS B N    1 
ATOM   1707 C  CA   . HIS B 1 7   ? -0.549  -14.062 4.699   1.00 63.75  ?  9   HIS B CA   1 
ATOM   1708 C  C    . HIS B 1 7   ? -0.703  -12.761 5.475   1.00 60.59  ?  9   HIS B C    1 
ATOM   1709 O  O    . HIS B 1 7   ? -1.479  -11.855 5.149   1.00 60.90  ?  9   HIS B O    1 
ATOM   1710 C  CB   . HIS B 1 7   ? -0.977  -13.961 3.229   1.00 66.85  ?  9   HIS B CB   1 
ATOM   1711 C  CG   . HIS B 1 7   ? -0.337  -15.031 2.408   1.00 71.92  ?  9   HIS B CG   1 
ATOM   1712 N  ND1  . HIS B 1 7   ? 1.041   -15.179 2.373   1.00 74.15  ?  9   HIS B ND1  1 
ATOM   1713 C  CD2  . HIS B 1 7   ? -0.901  -15.991 1.637   1.00 74.48  ?  9   HIS B CD2  1 
ATOM   1714 C  CE1  . HIS B 1 7   ? 1.276   -16.216 1.589   1.00 75.53  ?  9   HIS B CE1  1 
ATOM   1715 N  NE2  . HIS B 1 7   ? 0.134   -16.733 1.111   1.00 75.93  ?  9   HIS B NE2  1 
ATOM   1716 N  N    . GLY B 1 8   ? 0.090   -12.698 6.510   1.00 57.75  ?  10  GLY B N    1 
ATOM   1717 C  CA   . GLY B 1 8   ? -0.178  -11.886 7.668   1.00 56.12  ?  10  GLY B CA   1 
ATOM   1718 C  C    . GLY B 1 8   ? -1.037  -12.653 8.662   1.00 54.57  ?  10  GLY B C    1 
ATOM   1719 O  O    . GLY B 1 8   ? -1.261  -12.149 9.749   1.00 55.74  ?  10  GLY B O    1 
ATOM   1720 N  N    . ALA B 1 9   ? -1.525  -13.883 8.334   1.00 52.55  ?  11  ALA B N    1 
ATOM   1721 C  CA   . ALA B 1 9   ? -2.463  -14.589 9.205   1.00 50.63  ?  11  ALA B CA   1 
ATOM   1722 C  C    . ALA B 1 9   ? -1.707  -15.331 10.310  1.00 49.36  ?  11  ALA B C    1 
ATOM   1723 O  O    . ALA B 1 9   ? -0.570  -15.800 10.109  1.00 50.41  ?  11  ALA B O    1 
ATOM   1724 C  CB   . ALA B 1 9   ? -3.302  -15.562 8.401   1.00 50.01  ?  11  ALA B CB   1 
ATOM   1725 N  N    . ARG B 1 10  ? -2.356  -15.448 11.474  1.00 45.21  ?  12  ARG B N    1 
ATOM   1726 C  CA   . ARG B 1 10  ? -1.766  -16.066 12.651  1.00 43.34  ?  12  ARG B CA   1 
ATOM   1727 C  C    . ARG B 1 10  ? -1.748  -17.589 12.453  1.00 42.32  ?  12  ARG B C    1 
ATOM   1728 O  O    . ARG B 1 10  ? -2.715  -18.151 11.934  1.00 43.61  ?  12  ARG B O    1 
ATOM   1729 C  CB   . ARG B 1 10  ? -2.623  -15.692 13.876  1.00 46.04  ?  12  ARG B CB   1 
ATOM   1730 C  CG   . ARG B 1 10  ? -2.085  -16.148 15.241  1.00 50.13  ?  12  ARG B CG   1 
ATOM   1731 C  CD   . ARG B 1 10  ? -3.013  -15.694 16.361  1.00 51.58  ?  12  ARG B CD   1 
ATOM   1732 N  NE   . ARG B 1 10  ? -3.192  -14.239 16.371  1.00 54.42  ?  12  ARG B NE   1 
ATOM   1733 C  CZ   . ARG B 1 10  ? -2.353  -13.373 16.933  1.00 56.11  ?  12  ARG B CZ   1 
ATOM   1734 N  NH1  . ARG B 1 10  ? -1.251  -13.805 17.556  1.00 58.46  ?  12  ARG B NH1  1 
ATOM   1735 N  NH2  . ARG B 1 10  ? -2.597  -12.070 16.869  1.00 53.18  ?  12  ARG B NH2  1 
ATOM   1736 N  N    . ILE B 1 11  ? -0.658  -18.251 12.854  1.00 39.05  ?  13  ILE B N    1 
ATOM   1737 C  CA   . ILE B 1 11  ? -0.603  -19.707 12.824  1.00 37.85  ?  13  ILE B CA   1 
ATOM   1738 C  C    . ILE B 1 11  ? -1.360  -20.260 14.074  1.00 37.39  ?  13  ILE B C    1 
ATOM   1739 O  O    . ILE B 1 11  ? -0.846  -20.193 15.195  1.00 37.26  ?  13  ILE B O    1 
ATOM   1740 C  CB   . ILE B 1 11  ? 0.846   -20.214 12.802  1.00 38.68  ?  13  ILE B CB   1 
ATOM   1741 C  CG1  . ILE B 1 11  ? 1.627   -19.612 11.625  1.00 39.90  ?  13  ILE B CG1  1 
ATOM   1742 C  CG2  . ILE B 1 11  ? 0.860   -21.735 12.721  1.00 39.14  ?  13  ILE B CG2  1 
ATOM   1743 C  CD1  . ILE B 1 11  ? 3.191   -19.885 11.703  1.00 43.14  ?  13  ILE B CD1  1 
ATOM   1744 N  N    . ILE B 1 12  ? -2.569  -20.808 13.859  1.00 36.56  ?  14  ILE B N    1 
ATOM   1745 C  CA   . ILE B 1 12  ? -3.389  -21.335 14.935  1.00 36.09  ?  14  ILE B CA   1 
ATOM   1746 C  C    . ILE B 1 12  ? -3.555  -22.849 14.791  1.00 35.67  ?  14  ILE B C    1 
ATOM   1747 O  O    . ILE B 1 12  ? -3.918  -23.329 13.730  1.00 37.82  ?  14  ILE B O    1 
ATOM   1748 C  CB   . ILE B 1 12  ? -4.743  -20.596 14.984  1.00 36.26  ?  14  ILE B CB   1 
ATOM   1749 C  CG1  . ILE B 1 12  ? -4.513  -19.051 15.127  1.00 37.62  ?  14  ILE B CG1  1 
ATOM   1750 C  CG2  . ILE B 1 12  ? -5.606  -21.151 16.134  1.00 35.99  ?  14  ILE B CG2  1 
ATOM   1751 C  CD1  . ILE B 1 12  ? -5.671  -18.262 14.942  1.00 38.49  ?  14  ILE B CD1  1 
ATOM   1752 N  N    . TYR B 1 13  ? -3.296  -23.598 15.839  1.00 34.04  ?  15  TYR B N    1 
ATOM   1753 C  CA   . TYR B 1 13  ? -3.471  -25.069 15.853  1.00 35.15  ?  15  TYR B CA   1 
ATOM   1754 C  C    . TYR B 1 13  ? -4.415  -25.463 16.989  1.00 36.26  ?  15  TYR B C    1 
ATOM   1755 O  O    . TYR B 1 13  ? -4.248  -25.008 18.124  1.00 36.20  ?  15  TYR B O    1 
ATOM   1756 C  CB   . TYR B 1 13  ? -2.169  -25.804 16.121  1.00 34.39  ?  15  TYR B CB   1 
ATOM   1757 C  CG   . TYR B 1 13  ? -1.090  -25.617 15.099  1.00 35.26  ?  15  TYR B CG   1 
ATOM   1758 C  CD1  . TYR B 1 13  ? -1.154  -26.253 13.872  1.00 36.94  ?  15  TYR B CD1  1 
ATOM   1759 C  CD2  . TYR B 1 13  ? 0.020   -24.833 15.364  1.00 34.83  ?  15  TYR B CD2  1 
ATOM   1760 C  CE1  . TYR B 1 13  ? -0.151  -26.097 12.922  1.00 38.92  ?  15  TYR B CE1  1 
ATOM   1761 C  CE2  . TYR B 1 13  ? 1.047   -24.711 14.444  1.00 35.70  ?  15  TYR B CE2  1 
ATOM   1762 C  CZ   . TYR B 1 13  ? 0.948   -25.322 13.204  1.00 37.10  ?  15  TYR B CZ   1 
ATOM   1763 O  OH   . TYR B 1 13  ? 1.921   -25.193 12.234  1.00 36.14  ?  15  TYR B OH   1 
ATOM   1764 N  N    . ASP B 1 14  ? -5.408  -26.302 16.685  1.00 36.56  ?  16  ASP B N    1 
ATOM   1765 C  CA   . ASP B 1 14  ? -6.281  -26.847 17.722  1.00 36.27  ?  16  ASP B CA   1 
ATOM   1766 C  C    . ASP B 1 14  ? -5.655  -28.091 18.363  1.00 35.43  ?  16  ASP B C    1 
ATOM   1767 O  O    . ASP B 1 14  ? -4.653  -28.644 17.879  1.00 34.15  ?  16  ASP B O    1 
ATOM   1768 C  CB   . ASP B 1 14  ? -7.714  -27.130 17.207  1.00 37.24  ?  16  ASP B CB   1 
ATOM   1769 C  CG   . ASP B 1 14  ? -7.876  -28.150 16.079  1.00 42.60  ?  16  ASP B CG   1 
ATOM   1770 O  OD1  . ASP B 1 14  ? -7.025  -29.059 15.959  1.00 42.16  ?  16  ASP B OD1  1 
ATOM   1771 O  OD2  . ASP B 1 14  ? -8.850  -28.027 15.311  1.00 47.81  ?  16  ASP B OD2  1 
ATOM   1772 N  N    . ARG B 1 15  ? -6.280  -28.516 19.462  1.00 36.22  ?  17  ARG B N    1 
ATOM   1773 C  CA   A ARG B 1 15  ? -5.852  -29.672 20.250  0.50 37.73  ?  17  ARG B CA   1 
ATOM   1774 C  CA   B ARG B 1 15  ? -5.825  -29.655 20.235  0.50 37.73  ?  17  ARG B CA   1 
ATOM   1775 C  C    . ARG B 1 15  ? -5.628  -30.919 19.381  1.00 39.01  ?  17  ARG B C    1 
ATOM   1776 O  O    . ARG B 1 15  ? -4.582  -31.560 19.482  1.00 39.22  ?  17  ARG B O    1 
ATOM   1777 C  CB   A ARG B 1 15  ? -6.898  -30.003 21.343  0.50 38.57  ?  17  ARG B CB   1 
ATOM   1778 C  CB   B ARG B 1 15  ? -6.822  -29.953 21.365  0.50 38.58  ?  17  ARG B CB   1 
ATOM   1779 C  CG   A ARG B 1 15  ? -6.440  -31.044 22.346  0.50 39.54  ?  17  ARG B CG   1 
ATOM   1780 C  CG   B ARG B 1 15  ? -6.279  -30.921 22.357  0.50 39.33  ?  17  ARG B CG   1 
ATOM   1781 C  CD   A ARG B 1 15  ? -7.577  -31.613 23.200  0.50 41.17  ?  17  ARG B CD   1 
ATOM   1782 C  CD   B ARG B 1 15  ? -7.306  -31.229 23.421  0.50 40.93  ?  17  ARG B CD   1 
ATOM   1783 N  NE   A ARG B 1 15  ? -7.854  -30.787 24.376  0.50 41.95  ?  17  ARG B NE   1 
ATOM   1784 N  NE   B ARG B 1 15  ? -6.802  -32.217 24.363  0.50 41.59  ?  17  ARG B NE   1 
ATOM   1785 C  CZ   A ARG B 1 15  ? -8.709  -29.757 24.458  0.50 43.39  ?  17  ARG B CZ   1 
ATOM   1786 C  CZ   B ARG B 1 15  ? -6.722  -33.523 24.141  0.50 45.62  ?  17  ARG B CZ   1 
ATOM   1787 N  NH1  A ARG B 1 15  ? -8.849  -29.092 25.602  0.50 38.06  ?  17  ARG B NH1  1 
ATOM   1788 N  NH1  B ARG B 1 15  ? -7.114  -34.034 22.977  0.50 45.03  ?  17  ARG B NH1  1 
ATOM   1789 N  NH2  A ARG B 1 15  ? -9.427  -29.383 23.398  0.50 45.08  ?  17  ARG B NH2  1 
ATOM   1790 N  NH2  B ARG B 1 15  ? -6.240  -34.330 25.076  0.50 48.42  ?  17  ARG B NH2  1 
ATOM   1791 N  N    . ALA B 1 16  ? -6.637  -31.280 18.536  1.00 40.16  ?  18  ALA B N    1 
ATOM   1792 C  CA   . ALA B 1 16  ? -6.573  -32.503 17.751  1.00 40.80  ?  18  ALA B CA   1 
ATOM   1793 C  C    . ALA B 1 16  ? -5.380  -32.513 16.798  1.00 39.15  ?  18  ALA B C    1 
ATOM   1794 O  O    . ALA B 1 16  ? -4.701  -33.534 16.649  1.00 38.88  ?  18  ALA B O    1 
ATOM   1795 C  CB   . ALA B 1 16  ? -7.863  -32.691 16.968  1.00 42.45  ?  18  ALA B CB   1 
ATOM   1796 N  N    . PHE B 1 17  ? -5.123  -31.387 16.150  1.00 38.84  ?  19  PHE B N    1 
ATOM   1797 C  CA   . PHE B 1 17  ? -4.020  -31.278 15.227  1.00 39.26  ?  19  PHE B CA   1 
ATOM   1798 C  C    . PHE B 1 17  ? -2.695  -31.420 15.962  1.00 37.70  ?  19  PHE B C    1 
ATOM   1799 O  O    . PHE B 1 17  ? -1.819  -32.132 15.496  1.00 36.98  ?  19  PHE B O    1 
ATOM   1800 C  CB   . PHE B 1 17  ? -4.095  -29.956 14.475  1.00 40.77  ?  19  PHE B CB   1 
ATOM   1801 C  CG   . PHE B 1 17  ? -3.170  -29.914 13.299  1.00 44.01  ?  19  PHE B CG   1 
ATOM   1802 C  CD1  . PHE B 1 17  ? -1.863  -29.479 13.440  1.00 45.21  ?  19  PHE B CD1  1 
ATOM   1803 C  CD2  . PHE B 1 17  ? -3.586  -30.356 12.056  1.00 46.50  ?  19  PHE B CD2  1 
ATOM   1804 C  CE1  . PHE B 1 17  ? -1.006  -29.448 12.347  1.00 47.05  ?  19  PHE B CE1  1 
ATOM   1805 C  CE2  . PHE B 1 17  ? -2.728  -30.319 10.964  1.00 47.56  ?  19  PHE B CE2  1 
ATOM   1806 C  CZ   . PHE B 1 17  ? -1.444  -29.869 11.118  1.00 47.39  ?  19  PHE B CZ   1 
ATOM   1807 N  N    . LEU B 1 18  ? -2.552  -30.763 17.122  1.00 36.89  ?  20  LEU B N    1 
ATOM   1808 C  CA   . LEU B 1 18  ? -1.295  -30.834 17.872  1.00 36.08  ?  20  LEU B CA   1 
ATOM   1809 C  C    . LEU B 1 18  ? -1.056  -32.266 18.344  1.00 34.62  ?  20  LEU B C    1 
ATOM   1810 O  O    . LEU B 1 18  ? 0.056   -32.753 18.254  1.00 34.13  ?  20  LEU B O    1 
ATOM   1811 C  CB   . LEU B 1 18  ? -1.304  -29.829 19.072  1.00 34.81  ?  20  LEU B CB   1 
ATOM   1812 C  CG   . LEU B 1 18  ? -1.342  -28.319 18.692  1.00 36.57  ?  20  LEU B CG   1 
ATOM   1813 C  CD1  . LEU B 1 18  ? -1.469  -27.425 19.913  1.00 37.24  ?  20  LEU B CD1  1 
ATOM   1814 C  CD2  . LEU B 1 18  ? -0.084  -27.917 17.950  1.00 37.28  ?  20  LEU B CD2  1 
ATOM   1815 N  N    . MET B 1 19  ? -2.096  -32.930 18.827  1.00 35.84  ?  21  MET B N    1 
ATOM   1816 C  CA   . MET B 1 19  ? -2.021  -34.338 19.207  1.00 38.15  ?  21  MET B CA   1 
ATOM   1817 C  C    . MET B 1 19  ? -1.693  -35.262 18.032  1.00 40.68  ?  21  MET B C    1 
ATOM   1818 O  O    . MET B 1 19  ? -0.946  -36.196 18.236  1.00 41.83  ?  21  MET B O    1 
ATOM   1819 C  CB   . MET B 1 19  ? -3.324  -34.844 19.856  1.00 39.89  ?  21  MET B CB   1 
ATOM   1820 C  CG   . MET B 1 19  ? -3.710  -34.133 21.148  1.00 44.88  ?  21  MET B CG   1 
ATOM   1821 S  SD   . MET B 1 19  ? -2.457  -34.108 22.482  1.00 50.95  ?  21  MET B SD   1 
ATOM   1822 C  CE   . MET B 1 19  ? -2.081  -35.790 22.643  1.00 52.29  ?  21  MET B CE   1 
ATOM   1823 N  N    . ALA B 1 20  ? -2.226  -35.006 16.814  1.00 41.26  ?  22  ALA B N    1 
ATOM   1824 C  CA   . ALA B 1 20  ? -1.934  -35.847 15.645  1.00 42.76  ?  22  ALA B CA   1 
ATOM   1825 C  C    . ALA B 1 20  ? -0.491  -35.670 15.202  1.00 43.75  ?  22  ALA B C    1 
ATOM   1826 O  O    . ALA B 1 20  ? 0.009   -36.529 14.489  1.00 44.51  ?  22  ALA B O    1 
ATOM   1827 C  CB   . ALA B 1 20  ? -2.870  -35.510 14.479  1.00 43.33  ?  22  ALA B CB   1 
ATOM   1828 N  N    . CYS B 1 21  ? 0.201   -34.554 15.609  1.00 43.26  ?  23  CYS B N    1 
ATOM   1829 C  CA   . CYS B 1 21  ? 1.643   -34.380 15.378  1.00 42.97  ?  23  CYS B CA   1 
ATOM   1830 C  C    . CYS B 1 21  ? 2.512   -35.052 16.415  1.00 43.14  ?  23  CYS B C    1 
ATOM   1831 O  O    . CYS B 1 21  ? 3.728   -35.018 16.260  1.00 45.10  ?  23  CYS B O    1 
ATOM   1832 C  CB   . CYS B 1 21  ? 2.001   -32.901 15.294  1.00 44.26  ?  23  CYS B CB   1 
ATOM   1833 S  SG   . CYS B 1 21  ? 1.195   -31.992 13.966  1.00 46.12  ?  23  CYS B SG   1 
ATOM   1834 N  N    . ARG B 1 22  ? 1.944   -35.632 17.456  1.00 42.39  ?  24  ARG B N    1 
ATOM   1835 C  CA   . ARG B 1 22  ? 2.712   -36.299 18.494  1.00 44.96  ?  24  ARG B CA   1 
ATOM   1836 C  C    . ARG B 1 22  ? 3.061   -37.705 18.036  1.00 50.48  ?  24  ARG B C    1 
ATOM   1837 O  O    . ARG B 1 22  ? 2.179   -38.416 17.562  1.00 51.86  ?  24  ARG B O    1 
ATOM   1838 C  CB   . ARG B 1 22  ? 1.873   -36.358 19.751  1.00 43.89  ?  24  ARG B CB   1 
ATOM   1839 C  CG   . ARG B 1 22  ? 2.601   -36.827 20.977  1.00 45.14  ?  24  ARG B CG   1 
ATOM   1840 C  CD   . ARG B 1 22  ? 1.681   -36.660 22.163  1.00 44.65  ?  24  ARG B CD   1 
ATOM   1841 N  NE   . ARG B 1 22  ? 2.324   -37.078 23.410  1.00 45.79  ?  24  ARG B NE   1 
ATOM   1842 C  CZ   . ARG B 1 22  ? 1.750   -37.033 24.602  1.00 46.87  ?  24  ARG B CZ   1 
ATOM   1843 N  NH1  . ARG B 1 22  ? 0.509   -36.592 24.731  1.00 40.48  ?  24  ARG B NH1  1 
ATOM   1844 N  NH2  . ARG B 1 22  ? 2.410   -37.436 25.675  1.00 54.97  ?  24  ARG B NH2  1 
ATOM   1845 N  N    . GLY B 1 23  ? 4.327   -38.091 18.183  1.00 52.37  ?  25  GLY B N    1 
ATOM   1846 C  CA   . GLY B 1 23  ? 4.825   -39.348 17.646  1.00 54.57  ?  25  GLY B CA   1 
ATOM   1847 C  C    . GLY B 1 23  ? 4.569   -40.525 18.559  1.00 57.08  ?  25  GLY B C    1 
ATOM   1848 O  O    . GLY B 1 23  ? 4.554   -40.369 19.785  1.00 59.02  ?  25  GLY B O    1 
ATOM   1849 N  N    . GLY B 1 33  ? 8.393   -32.892 7.241   1.00 56.03  ?  35  GLY B N    1 
ATOM   1850 C  CA   . GLY B 1 33  ? 8.223   -31.437 7.260   1.00 55.87  ?  35  GLY B CA   1 
ATOM   1851 C  C    . GLY B 1 33  ? 7.622   -30.959 8.577   1.00 54.26  ?  35  GLY B C    1 
ATOM   1852 O  O    . GLY B 1 33  ? 6.500   -31.342 8.912   1.00 54.91  ?  35  GLY B O    1 
ATOM   1853 N  N    . LYS B 1 34  ? 8.347   -30.114 9.349   1.00 51.87  ?  36  LYS B N    1 
ATOM   1854 C  CA   . LYS B 1 34  ? 7.872   -29.701 10.669  1.00 48.57  ?  36  LYS B CA   1 
ATOM   1855 C  C    . LYS B 1 34  ? 6.875   -28.548 10.574  1.00 45.14  ?  36  LYS B C    1 
ATOM   1856 O  O    . LYS B 1 34  ? 6.964   -27.718 9.678   1.00 45.25  ?  36  LYS B O    1 
ATOM   1857 C  CB   . LYS B 1 34  ? 9.050   -29.322 11.574  1.00 50.49  ?  36  LYS B CB   1 
ATOM   1858 C  CG   . LYS B 1 34  ? 9.936   -30.486 11.959  1.00 53.82  ?  36  LYS B CG   1 
ATOM   1859 C  CD   . LYS B 1 34  ? 11.210  -29.972 12.593  1.00 59.87  ?  36  LYS B CD   1 
ATOM   1860 C  CE   . LYS B 1 34  ? 11.999  -31.024 13.333  1.00 66.31  ?  36  LYS B CE   1 
ATOM   1861 N  NZ   . LYS B 1 34  ? 13.238  -30.418 13.920  1.00 71.59  ?  36  LYS B NZ   1 
ATOM   1862 N  N    . HIS B 1 35  ? 5.940   -28.500 11.519  1.00 42.05  ?  37  HIS B N    1 
ATOM   1863 C  CA   . HIS B 1 35  ? 4.859   -27.510 11.566  1.00 38.79  ?  37  HIS B CA   1 
ATOM   1864 C  C    . HIS B 1 35  ? 5.315   -26.317 12.385  1.00 36.52  ?  37  HIS B C    1 
ATOM   1865 O  O    . HIS B 1 35  ? 5.475   -26.455 13.606  1.00 35.00  ?  37  HIS B O    1 
ATOM   1866 C  CB   . HIS B 1 35  ? 3.590   -28.176 12.135  1.00 37.87  ?  37  HIS B CB   1 
ATOM   1867 C  CG   . HIS B 1 35  ? 3.090   -29.262 11.203  1.00 45.88  ?  37  HIS B CG   1 
ATOM   1868 N  ND1  . HIS B 1 35  ? 3.599   -30.559 11.240  1.00 48.25  ?  37  HIS B ND1  1 
ATOM   1869 C  CD2  . HIS B 1 35  ? 2.164   -29.195 10.213  1.00 48.04  ?  37  HIS B CD2  1 
ATOM   1870 C  CE1  . HIS B 1 35  ? 2.965   -31.223 10.288  1.00 49.31  ?  37  HIS B CE1  1 
ATOM   1871 N  NE2  . HIS B 1 35  ? 2.090   -30.448 9.648   1.00 48.68  ?  37  HIS B NE2  1 
ATOM   1872 N  N    . PRO B 1 36  ? 5.521   -25.136 11.780  1.00 36.98  ?  38  PRO B N    1 
ATOM   1873 C  CA   . PRO B 1 36  ? 5.958   -23.976 12.583  1.00 35.72  ?  38  PRO B CA   1 
ATOM   1874 C  C    . PRO B 1 36  ? 4.902   -23.407 13.496  1.00 34.51  ?  38  PRO B C    1 
ATOM   1875 O  O    . PRO B 1 36  ? 3.716   -23.396 13.175  1.00 34.47  ?  38  PRO B O    1 
ATOM   1876 C  CB   . PRO B 1 36  ? 6.323   -22.927 11.537  1.00 37.10  ?  38  PRO B CB   1 
ATOM   1877 C  CG   . PRO B 1 36  ? 6.375   -23.669 10.239  1.00 39.43  ?  38  PRO B CG   1 
ATOM   1878 C  CD   . PRO B 1 36  ? 5.387   -24.753 10.361  1.00 38.40  ?  38  PRO B CD   1 
ATOM   1879 N  N    . LEU B 1 37  ? 5.366   -22.910 14.643  1.00 34.30  ?  39  LEU B N    1 
ATOM   1880 C  CA   . LEU B 1 37  ? 4.560   -22.162 15.574  1.00 31.74  ?  39  LEU B CA   1 
ATOM   1881 C  C    . LEU B 1 37  ? 4.582   -20.676 15.268  1.00 32.04  ?  39  LEU B C    1 
ATOM   1882 O  O    . LEU B 1 37  ? 5.541   -20.153 14.667  1.00 29.45  ?  39  LEU B O    1 
ATOM   1883 C  CB   . LEU B 1 37  ? 5.109   -22.420 16.985  1.00 30.56  ?  39  LEU B CB   1 
ATOM   1884 C  CG   . LEU B 1 37  ? 5.067   -23.866 17.498  1.00 32.34  ?  39  LEU B CG   1 
ATOM   1885 C  CD1  . LEU B 1 37  ? 5.690   -24.010 18.881  1.00 32.95  ?  39  LEU B CD1  1 
ATOM   1886 C  CD2  . LEU B 1 37  ? 3.658   -24.456 17.432  1.00 30.81  ?  39  LEU B CD2  1 
ATOM   1887 N  N    . GLN B 1 38  ? 3.538   -19.956 15.701  1.00 31.42  ?  40  GLN B N    1 
ATOM   1888 C  CA   . GLN B 1 38  ? 3.499   -18.480 15.597  1.00 32.85  ?  40  GLN B CA   1 
ATOM   1889 C  C    . GLN B 1 38  ? 4.682   -17.861 16.330  1.00 33.73  ?  40  GLN B C    1 
ATOM   1890 O  O    . GLN B 1 38  ? 5.301   -16.911 15.831  1.00 33.51  ?  40  GLN B O    1 
ATOM   1891 C  CB   . GLN B 1 38  ? 2.172   -17.978 16.151  1.00 35.34  ?  40  GLN B CB   1 
ATOM   1892 C  CG   . GLN B 1 38  ? 1.951   -16.477 16.106  1.00 39.33  ?  40  GLN B CG   1 
ATOM   1893 C  CD   . GLN B 1 38  ? 1.824   -15.918 14.701  1.00 42.71  ?  40  GLN B CD   1 
ATOM   1894 O  OE1  . GLN B 1 38  ? 1.505   -16.625 13.728  1.00 40.53  ?  40  GLN B OE1  1 
ATOM   1895 N  NE2  . GLN B 1 38  ? 2.054   -14.620 14.574  1.00 43.54  ?  40  GLN B NE2  1 
ATOM   1896 N  N    . ASN B 1 39  ? 5.006   -18.415 17.516  1.00 31.62  ?  41  ASN B N    1 
ATOM   1897 C  CA   . ASN B 1 39  ? 6.022   -17.855 18.398  1.00 33.29  ?  41  ASN B CA   1 
ATOM   1898 C  C    . ASN B 1 39  ? 7.085   -18.888 18.670  1.00 33.35  ?  41  ASN B C    1 
ATOM   1899 O  O    . ASN B 1 39  ? 6.823   -20.108 18.622  1.00 32.67  ?  41  ASN B O    1 
ATOM   1900 C  CB   . ASN B 1 39  ? 5.388   -17.419 19.741  1.00 32.92  ?  41  ASN B CB   1 
ATOM   1901 C  CG   . ASN B 1 39  ? 4.605   -16.129 19.598  1.00 38.51  ?  41  ASN B CG   1 
ATOM   1902 O  OD1  . ASN B 1 39  ? 5.172   -15.057 19.479  1.00 42.25  ?  41  ASN B OD1  1 
ATOM   1903 N  ND2  . ASN B 1 39  ? 3.312   -16.204 19.573  1.00 37.46  ?  41  ASN B ND2  1 
ATOM   1904 N  N    . ARG B 1 40  ? 8.295   -18.389 18.982  1.00 31.80  ?  42  ARG B N    1 
ATOM   1905 C  CA   . ARG B 1 40  ? 9.285   -19.203 19.612  1.00 30.22  ?  42  ARG B CA   1 
ATOM   1906 C  C    . ARG B 1 40  ? 9.016   -19.160 21.110  1.00 27.00  ?  42  ARG B C    1 
ATOM   1907 O  O    . ARG B 1 40  ? 8.643   -18.140 21.659  1.00 28.32  ?  42  ARG B O    1 
ATOM   1908 C  CB   . ARG B 1 40  ? 10.699  -18.811 19.207  1.00 30.41  ?  42  ARG B CB   1 
ATOM   1909 C  CG   . ARG B 1 40  ? 11.798  -19.688 19.735  1.00 31.98  ?  42  ARG B CG   1 
ATOM   1910 C  CD   . ARG B 1 40  ? 13.082  -19.354 19.006  1.00 33.02  ?  42  ARG B CD   1 
ATOM   1911 N  NE   . ARG B 1 40  ? 14.231  -20.261 19.174  1.00 34.68  ?  42  ARG B NE   1 
ATOM   1912 C  CZ   . ARG B 1 40  ? 15.409  -19.951 19.743  1.00 35.49  ?  42  ARG B CZ   1 
ATOM   1913 N  NH1  . ARG B 1 40  ? 15.621  -18.736 20.250  1.00 34.12  ?  42  ARG B NH1  1 
ATOM   1914 N  NH2  . ARG B 1 40  ? 16.383  -20.848 19.795  1.00 34.61  ?  42  ARG B NH2  1 
ATOM   1915 N  N    . TRP B 1 41  ? 9.169   -20.303 21.747  1.00 28.21  ?  43  TRP B N    1 
ATOM   1916 C  CA   . TRP B 1 41  ? 8.947   -20.493 23.201  1.00 28.16  ?  43  TRP B CA   1 
ATOM   1917 C  C    . TRP B 1 41  ? 10.225  -21.061 23.859  1.00 29.93  ?  43  TRP B C    1 
ATOM   1918 O  O    . TRP B 1 41  ? 11.029  -21.733 23.241  1.00 30.92  ?  43  TRP B O    1 
ATOM   1919 C  CB   . TRP B 1 41  ? 7.792   -21.508 23.478  1.00 28.72  ?  43  TRP B CB   1 
ATOM   1920 C  CG   . TRP B 1 41  ? 6.499   -21.102 22.887  1.00 28.85  ?  43  TRP B CG   1 
ATOM   1921 C  CD1  . TRP B 1 41  ? 6.110   -21.254 21.594  1.00 29.63  ?  43  TRP B CD1  1 
ATOM   1922 C  CD2  . TRP B 1 41  ? 5.493   -20.302 23.516  1.00 28.11  ?  43  TRP B CD2  1 
ATOM   1923 N  NE1  . TRP B 1 41  ? 4.890   -20.677 21.407  1.00 30.12  ?  43  TRP B NE1  1 
ATOM   1924 C  CE2  . TRP B 1 41  ? 4.501   -20.054 22.550  1.00 29.10  ?  43  TRP B CE2  1 
ATOM   1925 C  CE3  . TRP B 1 41  ? 5.359   -19.737 24.773  1.00 27.49  ?  43  TRP B CE3  1 
ATOM   1926 C  CZ2  . TRP B 1 41  ? 3.374   -19.283 22.815  1.00 29.33  ?  43  TRP B CZ2  1 
ATOM   1927 C  CZ3  . TRP B 1 41  ? 4.206   -19.043 25.069  1.00 28.69  ?  43  TRP B CZ3  1 
ATOM   1928 C  CH2  . TRP B 1 41  ? 3.225   -18.814 24.086  1.00 28.86  ?  43  TRP B CH2  1 
ATOM   1929 N  N    . ALA B 1 42  ? 10.383  -20.769 25.144  1.00 29.63  ?  44  ALA B N    1 
ATOM   1930 C  CA   . ALA B 1 42  ? 11.487  -21.204 25.951  1.00 29.17  ?  44  ALA B CA   1 
ATOM   1931 C  C    . ALA B 1 42  ? 10.923  -21.891 27.181  1.00 28.47  ?  44  ALA B C    1 
ATOM   1932 O  O    . ALA B 1 42  ? 10.042  -21.348 27.874  1.00 28.58  ?  44  ALA B O    1 
ATOM   1933 C  CB   . ALA B 1 42  ? 12.341  -20.012 26.339  1.00 29.13  ?  44  ALA B CB   1 
ATOM   1934 N  N    . LEU B 1 43  ? 11.421  -23.079 27.446  1.00 28.66  ?  45  LEU B N    1 
ATOM   1935 C  CA   . LEU B 1 43  ? 11.123  -23.808 28.670  1.00 30.10  ?  45  LEU B CA   1 
ATOM   1936 C  C    . LEU B 1 43  ? 12.198  -23.505 29.721  1.00 30.72  ?  45  LEU B C    1 
ATOM   1937 O  O    . LEU B 1 43  ? 13.390  -23.699 29.493  1.00 32.87  ?  45  LEU B O    1 
ATOM   1938 C  CB   . LEU B 1 43  ? 11.076  -25.322 28.388  1.00 30.06  ?  45  LEU B CB   1 
ATOM   1939 C  CG   . LEU B 1 43  ? 10.702  -26.175 29.618  1.00 33.88  ?  45  LEU B CG   1 
ATOM   1940 C  CD1  . LEU B 1 43  ? 9.297   -25.944 30.029  1.00 33.62  ?  45  LEU B CD1  1 
ATOM   1941 C  CD2  . LEU B 1 43  ? 10.898  -27.629 29.358  1.00 35.82  ?  45  LEU B CD2  1 
ATOM   1942 N  N    . TRP B 1 44  ? 11.761  -23.076 30.865  1.00 31.04  ?  46  TRP B N    1 
ATOM   1943 C  CA   . TRP B 1 44  ? 12.579  -22.764 32.013  1.00 33.67  ?  46  TRP B CA   1 
ATOM   1944 C  C    . TRP B 1 44  ? 12.278  -23.693 33.189  1.00 34.85  ?  46  TRP B C    1 
ATOM   1945 O  O    . TRP B 1 44  ? 11.181  -24.264 33.321  1.00 34.21  ?  46  TRP B O    1 
ATOM   1946 C  CB   . TRP B 1 44  ? 12.362  -21.356 32.456  1.00 33.45  ?  46  TRP B CB   1 
ATOM   1947 C  CG   . TRP B 1 44  ? 12.506  -20.287 31.408  1.00 34.98  ?  46  TRP B CG   1 
ATOM   1948 C  CD1  . TRP B 1 44  ? 11.636  -19.977 30.407  1.00 35.79  ?  46  TRP B CD1  1 
ATOM   1949 C  CD2  . TRP B 1 44  ? 13.580  -19.348 31.302  1.00 36.36  ?  46  TRP B CD2  1 
ATOM   1950 N  NE1  . TRP B 1 44  ? 12.083  -18.861 29.725  1.00 36.24  ?  46  TRP B NE1  1 
ATOM   1951 C  CE2  . TRP B 1 44  ? 13.293  -18.492 30.220  1.00 36.80  ?  46  TRP B CE2  1 
ATOM   1952 C  CE3  . TRP B 1 44  ? 14.785  -19.192 31.958  1.00 37.79  ?  46  TRP B CE3  1 
ATOM   1953 C  CZ2  . TRP B 1 44  ? 14.132  -17.439 29.859  1.00 39.37  ?  46  TRP B CZ2  1 
ATOM   1954 C  CZ3  . TRP B 1 44  ? 15.609  -18.167 31.593  1.00 40.43  ?  46  TRP B CZ3  1 
ATOM   1955 C  CH2  . TRP B 1 44  ? 15.294  -17.309 30.534  1.00 39.89  ?  46  TRP B CH2  1 
ATOM   1956 N  N    . PHE B 1 45  ? 13.277  -23.833 34.040  1.00 35.65  ?  47  PHE B N    1 
ATOM   1957 C  CA   . PHE B 1 45  ? 13.171  -24.605 35.280  1.00 37.66  ?  47  PHE B CA   1 
ATOM   1958 C  C    . PHE B 1 45  ? 13.820  -23.797 36.428  1.00 36.87  ?  47  PHE B C    1 
ATOM   1959 O  O    . PHE B 1 45  ? 14.795  -23.110 36.189  1.00 36.29  ?  47  PHE B O    1 
ATOM   1960 C  CB   . PHE B 1 45  ? 13.941  -25.915 35.021  1.00 40.98  ?  47  PHE B CB   1 
ATOM   1961 C  CG   . PHE B 1 45  ? 14.094  -26.828 36.185  1.00 45.05  ?  47  PHE B CG   1 
ATOM   1962 C  CD1  . PHE B 1 45  ? 13.005  -27.492 36.706  1.00 45.96  ?  47  PHE B CD1  1 
ATOM   1963 C  CD2  . PHE B 1 45  ? 15.346  -27.113 36.692  1.00 48.87  ?  47  PHE B CD2  1 
ATOM   1964 C  CE1  . PHE B 1 45  ? 13.156  -28.383 37.758  1.00 49.17  ?  47  PHE B CE1  1 
ATOM   1965 C  CE2  . PHE B 1 45  ? 15.500  -27.989 37.755  1.00 50.42  ?  47  PHE B CE2  1 
ATOM   1966 C  CZ   . PHE B 1 45  ? 14.401  -28.616 38.285  1.00 50.35  ?  47  PHE B CZ   1 
ATOM   1967 N  N    . PHE B 1 46  ? 13.327  -23.868 37.669  1.00 36.16  ?  48  PHE B N    1 
ATOM   1968 C  CA   . PHE B 1 46  ? 14.065  -23.323 38.827  1.00 41.62  ?  48  PHE B CA   1 
ATOM   1969 C  C    . PHE B 1 46  ? 14.652  -24.434 39.761  1.00 44.99  ?  48  PHE B C    1 
ATOM   1970 O  O    . PHE B 1 46  ? 13.877  -25.196 40.286  1.00 45.85  ?  48  PHE B O    1 
ATOM   1971 C  CB   . PHE B 1 46  ? 13.155  -22.431 39.695  1.00 43.29  ?  48  PHE B CB   1 
ATOM   1972 C  CG   . PHE B 1 46  ? 12.745  -21.121 39.079  1.00 46.64  ?  48  PHE B CG   1 
ATOM   1973 C  CD1  . PHE B 1 46  ? 13.477  -19.968 39.311  1.00 49.12  ?  48  PHE B CD1  1 
ATOM   1974 C  CD2  . PHE B 1 46  ? 11.616  -21.033 38.283  1.00 48.93  ?  48  PHE B CD2  1 
ATOM   1975 C  CE1  . PHE B 1 46  ? 13.079  -18.740 38.768  1.00 49.22  ?  48  PHE B CE1  1 
ATOM   1976 C  CE2  . PHE B 1 46  ? 11.239  -19.804 37.701  1.00 50.03  ?  48  PHE B CE2  1 
ATOM   1977 C  CZ   . PHE B 1 46  ? 11.972  -18.671 37.957  1.00 49.21  ?  48  PHE B CZ   1 
ATOM   1978 N  N    . LYS B 1 47  ? 15.982  -24.494 39.950  1.00 47.15  ?  49  LYS B N    1 
ATOM   1979 C  CA   . LYS B 1 47  ? 16.676  -25.426 40.865  1.00 51.37  ?  49  LYS B CA   1 
ATOM   1980 C  C    . LYS B 1 47  ? 16.239  -25.165 42.315  1.00 53.63  ?  49  LYS B C    1 
ATOM   1981 O  O    . LYS B 1 47  ? 15.903  -24.031 42.643  1.00 54.22  ?  49  LYS B O    1 
ATOM   1982 C  CB   . LYS B 1 47  ? 18.224  -25.301 40.661  1.00 56.48  ?  49  LYS B CB   1 
ATOM   1983 C  CG   . LYS B 1 47  ? 19.157  -25.781 41.807  1.00 64.63  ?  49  LYS B CG   1 
ATOM   1984 C  CD   . LYS B 1 47  ? 19.231  -27.314 41.981  1.00 71.12  ?  49  LYS B CD   1 
ATOM   1985 C  CE   . LYS B 1 47  ? 19.778  -27.788 43.322  1.00 74.42  ?  49  LYS B CE   1 
ATOM   1986 N  NZ   . LYS B 1 47  ? 18.733  -27.930 44.374  1.00 76.27  ?  49  LYS B NZ   1 
ATOM   1987 N  N    . ASN B 1 48  ? 16.225  -26.217 43.171  1.00 55.12  ?  50  ASN B N    1 
ATOM   1988 C  CA   . ASN B 1 48  ? 15.784  -26.219 44.593  1.00 56.08  ?  50  ASN B CA   1 
ATOM   1989 C  C    . ASN B 1 48  ? 16.776  -25.660 45.667  1.00 55.64  ?  50  ASN B C    1 
ATOM   1990 O  O    . ASN B 1 48  ? 16.522  -25.888 46.867  1.00 56.43  ?  50  ASN B O    1 
ATOM   1991 C  CB   . ASN B 1 48  ? 15.422  -27.675 45.001  1.00 59.27  ?  50  ASN B CB   1 
ATOM   1992 C  CG   . ASN B 1 48  ? 14.851  -27.844 46.406  1.00 66.21  ?  50  ASN B CG   1 
ATOM   1993 O  OD1  . ASN B 1 48  ? 14.274  -26.911 46.972  1.00 69.35  ?  50  ASN B OD1  1 
ATOM   1994 N  ND2  . ASN B 1 48  ? 14.998  -29.037 47.020  1.00 67.26  ?  50  ASN B ND2  1 
ATOM   1995 N  N    . ASP B 1 49  ? 17.832  -24.924 45.288  1.00 52.96  ?  51  ASP B N    1 
ATOM   1996 C  CA   . ASP B 1 49  ? 18.931  -24.587 46.194  1.00 51.46  ?  51  ASP B CA   1 
ATOM   1997 C  C    . ASP B 1 49  ? 18.518  -23.392 47.047  1.00 50.65  ?  51  ASP B C    1 
ATOM   1998 O  O    . ASP B 1 49  ? 18.630  -22.244 46.604  1.00 49.38  ?  51  ASP B O    1 
ATOM   1999 C  CB   . ASP B 1 49  ? 20.208  -24.249 45.394  1.00 52.76  ?  51  ASP B CB   1 
ATOM   2000 C  CG   . ASP B 1 49  ? 21.424  -23.909 46.233  1.00 58.22  ?  51  ASP B CG   1 
ATOM   2001 O  OD1  . ASP B 1 49  ? 21.272  -23.739 47.479  1.00 59.07  ?  51  ASP B OD1  1 
ATOM   2002 O  OD2  . ASP B 1 49  ? 22.520  -23.809 45.661  1.00 59.09  ?  51  ASP B OD2  1 
ATOM   2003 N  N    . LYS B 1 50  ? 18.064  -23.650 48.274  1.00 51.03  ?  52  LYS B N    1 
ATOM   2004 C  CA   . LYS B 1 50  ? 17.580  -22.576 49.143  1.00 51.98  ?  52  LYS B CA   1 
ATOM   2005 C  C    . LYS B 1 50  ? 18.703  -21.705 49.742  1.00 53.38  ?  52  LYS B C    1 
ATOM   2006 O  O    . LYS B 1 50  ? 18.386  -20.714 50.404  1.00 53.57  ?  52  LYS B O    1 
ATOM   2007 C  CB   . LYS B 1 50  ? 16.648  -23.123 50.246  1.00 53.71  ?  52  LYS B CB   1 
ATOM   2008 C  CG   . LYS B 1 50  ? 15.383  -23.817 49.725  1.00 58.56  ?  52  LYS B CG   1 
ATOM   2009 C  CD   . LYS B 1 50  ? 14.332  -22.809 49.206  1.00 65.01  ?  52  LYS B CD   1 
ATOM   2010 C  CE   . LYS B 1 50  ? 13.031  -23.453 48.775  1.00 70.25  ?  52  LYS B CE   1 
ATOM   2011 N  NZ   . LYS B 1 50  ? 13.088  -23.964 47.386  1.00 74.83  ?  52  LYS B NZ   1 
ATOM   2012 N  N    . SER B 1 51  ? 19.996  -22.046 49.534  1.00 54.46  ?  53  SER B N    1 
ATOM   2013 C  CA   . SER B 1 51  ? 21.072  -21.096 49.849  1.00 56.64  ?  53  SER B CA   1 
ATOM   2014 C  C    . SER B 1 51  ? 21.139  -19.937 48.803  1.00 58.27  ?  53  SER B C    1 
ATOM   2015 O  O    . SER B 1 51  ? 21.826  -18.937 49.042  1.00 58.90  ?  53  SER B O    1 
ATOM   2016 C  CB   . SER B 1 51  ? 22.427  -21.808 49.980  1.00 58.94  ?  53  SER B CB   1 
ATOM   2017 O  OG   . SER B 1 51  ? 23.129  -21.938 48.746  1.00 63.01  ?  53  SER B OG   1 
ATOM   2018 N  N    . LYS B 1 52  ? 20.445  -20.077 47.647  1.00 58.19  ?  54  LYS B N    1 
ATOM   2019 C  CA   . LYS B 1 52  ? 20.430  -19.072 46.596  1.00 58.08  ?  54  LYS B CA   1 
ATOM   2020 C  C    . LYS B 1 52  ? 19.018  -18.546 46.338  1.00 57.22  ?  54  LYS B C    1 
ATOM   2021 O  O    . LYS B 1 52  ? 18.027  -19.197 46.650  1.00 55.93  ?  54  LYS B O    1 
ATOM   2022 C  CB   . LYS B 1 52  ? 21.045  -19.674 45.322  1.00 60.20  ?  54  LYS B CB   1 
ATOM   2023 C  CG   . LYS B 1 52  ? 22.550  -19.911 45.433  1.00 63.76  ?  54  LYS B CG   1 
ATOM   2024 C  CD   . LYS B 1 52  ? 23.061  -20.876 44.365  1.00 68.17  ?  54  LYS B CD   1 
ATOM   2025 C  CE   . LYS B 1 52  ? 24.541  -21.164 44.493  1.00 71.60  ?  54  LYS B CE   1 
ATOM   2026 N  NZ   . LYS B 1 52  ? 24.880  -21.773 45.823  1.00 76.74  ?  54  LYS B NZ   1 
ATOM   2027 N  N    . THR B 1 53  ? 18.963  -17.346 45.749  1.00 58.13  ?  55  THR B N    1 
ATOM   2028 C  CA   . THR B 1 53  ? 17.723  -16.629 45.386  1.00 58.74  ?  55  THR B CA   1 
ATOM   2029 C  C    . THR B 1 53  ? 17.013  -17.361 44.171  1.00 57.56  ?  55  THR B C    1 
ATOM   2030 O  O    . THR B 1 53  ? 17.680  -18.125 43.450  1.00 56.09  ?  55  THR B O    1 
ATOM   2031 C  CB   . THR B 1 53  ? 18.081  -15.103 45.156  1.00 61.51  ?  55  THR B CB   1 
ATOM   2032 O  OG1  . THR B 1 53  ? 16.979  -14.251 45.479  1.00 66.84  ?  55  THR B OG1  1 
ATOM   2033 C  CG2  . THR B 1 53  ? 18.514  -14.834 43.783  1.00 59.76  ?  55  THR B CG2  1 
ATOM   2034 N  N    . TRP B 1 54  ? 15.671  -17.150 43.952  1.00 57.68  ?  56  TRP B N    1 
ATOM   2035 C  CA   . TRP B 1 54  ? 14.991  -17.730 42.758  1.00 58.67  ?  56  TRP B CA   1 
ATOM   2036 C  C    . TRP B 1 54  ? 15.693  -17.335 41.455  1.00 56.29  ?  56  TRP B C    1 
ATOM   2037 O  O    . TRP B 1 54  ? 15.922  -18.203 40.620  1.00 56.05  ?  56  TRP B O    1 
ATOM   2038 C  CB   . TRP B 1 54  ? 13.486  -17.369 42.664  1.00 60.92  ?  56  TRP B CB   1 
ATOM   2039 C  CG   . TRP B 1 54  ? 12.620  -18.092 43.656  1.00 64.60  ?  56  TRP B CG   1 
ATOM   2040 C  CD1  . TRP B 1 54  ? 11.943  -17.546 44.708  1.00 66.37  ?  56  TRP B CD1  1 
ATOM   2041 C  CD2  . TRP B 1 54  ? 12.380  -19.509 43.713  1.00 66.44  ?  56  TRP B CD2  1 
ATOM   2042 N  NE1  . TRP B 1 54  ? 11.295  -18.539 45.420  1.00 67.41  ?  56  TRP B NE1  1 
ATOM   2043 C  CE2  . TRP B 1 54  ? 11.561  -19.753 44.838  1.00 67.60  ?  56  TRP B CE2  1 
ATOM   2044 C  CE3  . TRP B 1 54  ? 12.800  -20.599 42.936  1.00 67.98  ?  56  TRP B CE3  1 
ATOM   2045 C  CZ2  . TRP B 1 54  ? 11.142  -21.041 45.193  1.00 68.88  ?  56  TRP B CZ2  1 
ATOM   2046 C  CZ3  . TRP B 1 54  ? 12.385  -21.875 43.293  1.00 69.48  ?  56  TRP B CZ3  1 
ATOM   2047 C  CH2  . TRP B 1 54  ? 11.559  -22.084 44.402  1.00 69.31  ?  56  TRP B CH2  1 
ATOM   2048 N  N    . GLN B 1 55  ? 16.044  -16.036 41.287  1.00 55.04  ?  57  GLN B N    1 
ATOM   2049 C  CA   . GLN B 1 55  ? 16.788  -15.516 40.115  1.00 54.68  ?  57  GLN B CA   1 
ATOM   2050 C  C    . GLN B 1 55  ? 18.035  -16.390 39.822  1.00 53.00  ?  57  GLN B C    1 
ATOM   2051 O  O    . GLN B 1 55  ? 18.266  -16.845 38.708  1.00 52.86  ?  57  GLN B O    1 
ATOM   2052 C  CB   . GLN B 1 55  ? 17.212  -14.039 40.386  1.00 57.68  ?  57  GLN B CB   1 
ATOM   2053 C  CG   . GLN B 1 55  ? 17.826  -13.279 39.209  1.00 63.62  ?  57  GLN B CG   1 
ATOM   2054 C  CD   . GLN B 1 55  ? 16.776  -12.666 38.298  1.00 73.60  ?  57  GLN B CD   1 
ATOM   2055 O  OE1  . GLN B 1 55  ? 16.610  -13.077 37.126  1.00 76.21  ?  57  GLN B OE1  1 
ATOM   2056 N  NE2  . GLN B 1 55  ? 16.048  -11.665 38.814  1.00 74.61  ?  57  GLN B NE2  1 
ATOM   2057 N  N    . ALA B 1 56  ? 18.813  -16.617 40.845  1.00 51.32  ?  58  ALA B N    1 
ATOM   2058 C  CA   . ALA B 1 56  ? 20.057  -17.370 40.798  1.00 50.14  ?  58  ALA B CA   1 
ATOM   2059 C  C    . ALA B 1 56  ? 19.854  -18.857 40.432  1.00 49.28  ?  58  ALA B C    1 
ATOM   2060 O  O    . ALA B 1 56  ? 20.747  -19.491 39.864  1.00 50.45  ?  58  ALA B O    1 
ATOM   2061 C  CB   . ALA B 1 56  ? 20.755  -17.264 42.142  1.00 49.92  ?  58  ALA B CB   1 
ATOM   2062 N  N    . ASN B 1 57  ? 18.704  -19.394 40.760  1.00 46.99  ?  59  ASN B N    1 
ATOM   2063 C  CA   . ASN B 1 57  ? 18.346  -20.789 40.517  1.00 45.77  ?  59  ASN B CA   1 
ATOM   2064 C  C    . ASN B 1 57  ? 17.641  -21.050 39.185  1.00 42.58  ?  59  ASN B C    1 
ATOM   2065 O  O    . ASN B 1 57  ? 17.307  -22.197 38.875  1.00 41.84  ?  59  ASN B O    1 
ATOM   2066 C  CB   . ASN B 1 57  ? 17.456  -21.260 41.689  1.00 48.02  ?  59  ASN B CB   1 
ATOM   2067 C  CG   . ASN B 1 57  ? 18.274  -21.485 42.946  1.00 49.33  ?  59  ASN B CG   1 
ATOM   2068 O  OD1  . ASN B 1 57  ? 19.386  -22.024 42.883  1.00 49.79  ?  59  ASN B OD1  1 
ATOM   2069 N  ND2  . ASN B 1 57  ? 17.773  -21.093 44.089  1.00 50.34  ?  59  ASN B ND2  1 
ATOM   2070 N  N    . LEU B 1 58  ? 17.436  -20.013 38.407  1.00 41.10  ?  60  LEU B N    1 
ATOM   2071 C  CA   . LEU B 1 58  ? 16.724  -20.078 37.136  1.00 40.73  ?  60  LEU B CA   1 
ATOM   2072 C  C    . LEU B 1 58  ? 17.593  -20.699 36.085  1.00 41.39  ?  60  LEU B C    1 
ATOM   2073 O  O    . LEU B 1 58  ? 18.758  -20.283 35.924  1.00 43.56  ?  60  LEU B O    1 
ATOM   2074 C  CB   . LEU B 1 58  ? 16.332  -18.660 36.698  1.00 41.35  ?  60  LEU B CB   1 
ATOM   2075 C  CG   . LEU B 1 58  ? 15.614  -18.528 35.317  1.00 42.33  ?  60  LEU B CG   1 
ATOM   2076 C  CD1  . LEU B 1 58  ? 14.289  -19.303 35.318  1.00 43.10  ?  60  LEU B CD1  1 
ATOM   2077 C  CD2  . LEU B 1 58  ? 15.374  -17.049 34.958  1.00 44.54  ?  60  LEU B CD2  1 
ATOM   2078 N  N    . ARG B 1 59  ? 17.062  -21.685 35.338  1.00 39.58  ?  61  ARG B N    1 
ATOM   2079 C  CA   . ARG B 1 59  ? 17.839  -22.297 34.253  1.00 40.44  ?  61  ARG B CA   1 
ATOM   2080 C  C    . ARG B 1 59  ? 17.019  -22.401 32.986  1.00 37.76  ?  61  ARG B C    1 
ATOM   2081 O  O    . ARG B 1 59  ? 15.833  -22.734 33.022  1.00 37.16  ?  61  ARG B O    1 
ATOM   2082 C  CB   . ARG B 1 59  ? 18.345  -23.694 34.642  1.00 44.13  ?  61  ARG B CB   1 
ATOM   2083 C  CG   . ARG B 1 59  ? 19.241  -23.719 35.898  1.00 50.78  ?  61  ARG B CG   1 
ATOM   2084 C  CD   . ARG B 1 59  ? 20.680  -23.213 35.689  1.00 55.25  ?  61  ARG B CD   1 
ATOM   2085 N  NE   . ARG B 1 59  ? 21.414  -23.322 36.970  1.00 61.57  ?  61  ARG B NE   1 
ATOM   2086 C  CZ   . ARG B 1 59  ? 21.457  -22.404 37.944  1.00 63.47  ?  61  ARG B CZ   1 
ATOM   2087 N  NH1  . ARG B 1 59  ? 20.823  -21.239 37.807  1.00 61.01  ?  61  ARG B NH1  1 
ATOM   2088 N  NH2  . ARG B 1 59  ? 22.148  -22.638 39.056  1.00 62.93  ?  61  ARG B NH2  1 
ATOM   2089 N  N    . LEU B 1 60  ? 17.652  -22.120 31.860  1.00 37.00  ?  62  LEU B N    1 
ATOM   2090 C  CA   . LEU B 1 60  ? 17.013  -22.251 30.585  1.00 36.35  ?  62  LEU B CA   1 
ATOM   2091 C  C    . LEU B 1 60  ? 17.211  -23.666 30.118  1.00 38.30  ?  62  LEU B C    1 
ATOM   2092 O  O    . LEU B 1 60  ? 18.361  -24.104 29.949  1.00 40.92  ?  62  LEU B O    1 
ATOM   2093 C  CB   . LEU B 1 60  ? 17.659  -21.279 29.613  1.00 36.50  ?  62  LEU B CB   1 
ATOM   2094 C  CG   . LEU B 1 60  ? 17.213  -21.368 28.184  1.00 37.38  ?  62  LEU B CG   1 
ATOM   2095 C  CD1  . LEU B 1 60  ? 15.749  -21.146 28.031  1.00 36.88  ?  62  LEU B CD1  1 
ATOM   2096 C  CD2  . LEU B 1 60  ? 17.946  -20.320 27.344  1.00 39.10  ?  62  LEU B CD2  1 
ATOM   2097 N  N    . ILE B 1 61  ? 16.123  -24.386 29.876  1.00 37.78  ?  63  ILE B N    1 
ATOM   2098 C  CA   . ILE B 1 61  ? 16.263  -25.767 29.447  1.00 38.20  ?  63  ILE B CA   1 
ATOM   2099 C  C    . ILE B 1 61  ? 16.429  -25.818 27.925  1.00 37.32  ?  63  ILE B C    1 
ATOM   2100 O  O    . ILE B 1 61  ? 17.423  -26.360 27.439  1.00 39.06  ?  63  ILE B O    1 
ATOM   2101 C  CB   . ILE B 1 61  ? 15.087  -26.634 29.930  1.00 40.17  ?  63  ILE B CB   1 
ATOM   2102 C  CG1  . ILE B 1 61  ? 14.978  -26.636 31.478  1.00 42.39  ?  63  ILE B CG1  1 
ATOM   2103 C  CG2  . ILE B 1 61  ? 15.180  -28.033 29.346  1.00 40.87  ?  63  ILE B CG2  1 
ATOM   2104 C  CD1  . ILE B 1 61  ? 16.293  -26.927 32.268  1.00 44.86  ?  63  ILE B CD1  1 
ATOM   2105 N  N    . SER B 1 62  ? 15.479  -25.266 27.180  1.00 35.80  ?  64  SER B N    1 
ATOM   2106 C  CA   . SER B 1 62  ? 15.512  -25.332 25.708  1.00 35.19  ?  64  SER B CA   1 
ATOM   2107 C  C    . SER B 1 62  ? 14.516  -24.338 25.083  1.00 34.55  ?  64  SER B C    1 
ATOM   2108 O  O    . SER B 1 62  ? 13.586  -23.852 25.733  1.00 33.72  ?  64  SER B O    1 
ATOM   2109 C  CB   . SER B 1 62  ? 15.229  -26.762 25.254  1.00 37.06  ?  64  SER B CB   1 
ATOM   2110 O  OG   . SER B 1 62  ? 15.584  -26.972 23.897  1.00 44.11  ?  64  SER B OG   1 
ATOM   2111 N  N    . LYS B 1 63  ? 14.729  -24.025 23.828  1.00 32.19  ?  65  LYS B N    1 
ATOM   2112 C  CA   . LYS B 1 63  ? 13.810  -23.219 23.037  1.00 32.69  ?  65  LYS B CA   1 
ATOM   2113 C  C    . LYS B 1 63  ? 13.347  -23.995 21.809  1.00 33.09  ?  65  LYS B C    1 
ATOM   2114 O  O    . LYS B 1 63  ? 14.108  -24.802 21.270  1.00 33.51  ?  65  LYS B O    1 
ATOM   2115 C  CB   . LYS B 1 63  ? 14.473  -21.896 22.600  1.00 31.31  ?  65  LYS B CB   1 
ATOM   2116 C  CG   . LYS B 1 63  ? 15.033  -21.107 23.775  1.00 30.86  ?  65  LYS B CG   1 
ATOM   2117 C  CD   . LYS B 1 63  ? 15.370  -19.688 23.328  1.00 33.04  ?  65  LYS B CD   1 
ATOM   2118 C  CE   . LYS B 1 63  ? 15.826  -18.729 24.403  1.00 31.96  ?  65  LYS B CE   1 
ATOM   2119 N  NZ   . LYS B 1 63  ? 16.191  -17.371 23.828  1.00 32.24  ?  65  LYS B NZ   1 
ATOM   2120 N  N    . PHE B 1 64  ? 12.102  -23.750 21.359  1.00 32.45  ?  66  PHE B N    1 
ATOM   2121 C  CA   . PHE B 1 64  ? 11.551  -24.377 20.163  1.00 32.97  ?  66  PHE B CA   1 
ATOM   2122 C  C    . PHE B 1 64  ? 10.543  -23.446 19.463  1.00 31.23  ?  66  PHE B C    1 
ATOM   2123 O  O    . PHE B 1 64  ? 9.972   -22.557 20.092  1.00 29.87  ?  66  PHE B O    1 
ATOM   2124 C  CB   . PHE B 1 64  ? 10.877  -25.713 20.516  1.00 32.69  ?  66  PHE B CB   1 
ATOM   2125 C  CG   . PHE B 1 64  ? 9.737   -25.535 21.495  1.00 31.31  ?  66  PHE B CG   1 
ATOM   2126 C  CD1  . PHE B 1 64  ? 9.968   -25.538 22.863  1.00 32.29  ?  66  PHE B CD1  1 
ATOM   2127 C  CD2  . PHE B 1 64  ? 8.436   -25.337 21.049  1.00 30.18  ?  66  PHE B CD2  1 
ATOM   2128 C  CE1  . PHE B 1 64  ? 8.923   -25.391 23.753  1.00 31.70  ?  66  PHE B CE1  1 
ATOM   2129 C  CE2  . PHE B 1 64  ? 7.410   -25.092 21.948  1.00 30.46  ?  66  PHE B CE2  1 
ATOM   2130 C  CZ   . PHE B 1 64  ? 7.646   -25.179 23.297  1.00 30.70  ?  66  PHE B CZ   1 
ATOM   2131 N  N    . ASP B 1 65  ? 10.326  -23.660 18.162  1.00 30.41  ?  67  ASP B N    1 
ATOM   2132 C  CA   . ASP B 1 65  ? 9.292   -22.940 17.422  1.00 30.92  ?  67  ASP B CA   1 
ATOM   2133 C  C    . ASP B 1 65  ? 8.604   -23.798 16.387  1.00 30.70  ?  67  ASP B C    1 
ATOM   2134 O  O    . ASP B 1 65  ? 8.088   -23.272 15.385  1.00 29.97  ?  67  ASP B O    1 
ATOM   2135 C  CB   . ASP B 1 65  ? 9.751   -21.601 16.842  1.00 33.26  ?  67  ASP B CB   1 
ATOM   2136 C  CG   . ASP B 1 65  ? 10.623  -21.723 15.657  1.00 39.65  ?  67  ASP B CG   1 
ATOM   2137 O  OD1  . ASP B 1 65  ? 11.529  -22.557 15.693  1.00 38.91  ?  67  ASP B OD1  1 
ATOM   2138 O  OD2  . ASP B 1 65  ? 10.396  -20.968 14.676  1.00 42.20  ?  67  ASP B OD2  1 
ATOM   2139 N  N    . THR B 1 66  ? 8.587   -25.142 16.637  1.00 31.49  ?  68  THR B N    1 
ATOM   2140 C  CA   . THR B 1 66  ? 7.809   -26.100 15.868  1.00 31.48  ?  68  THR B CA   1 
ATOM   2141 C  C    . THR B 1 66  ? 7.064   -27.027 16.803  1.00 32.01  ?  68  THR B C    1 
ATOM   2142 O  O    . THR B 1 66  ? 7.473   -27.260 17.952  1.00 31.53  ?  68  THR B O    1 
ATOM   2143 C  CB   . THR B 1 66  ? 8.644   -26.901 14.812  1.00 34.67  ?  68  THR B CB   1 
ATOM   2144 O  OG1  . THR B 1 66  ? 9.225   -28.006 15.439  1.00 37.62  ?  68  THR B OG1  1 
ATOM   2145 C  CG2  . THR B 1 66  ? 9.652   -26.034 14.062  1.00 34.57  ?  68  THR B CG2  1 
ATOM   2146 N  N    . VAL B 1 67  ? 5.948   -27.551 16.284  1.00 33.01  ?  69  VAL B N    1 
ATOM   2147 C  CA   . VAL B 1 67  ? 5.104   -28.509 16.992  1.00 33.97  ?  69  VAL B CA   1 
ATOM   2148 C  C    . VAL B 1 67  ? 5.924   -29.741 17.364  1.00 33.75  ?  69  VAL B C    1 
ATOM   2149 O  O    . VAL B 1 67  ? 5.866   -30.224 18.507  1.00 35.38  ?  69  VAL B O    1 
ATOM   2150 C  CB   . VAL B 1 67  ? 3.834   -28.903 16.203  1.00 34.12  ?  69  VAL B CB   1 
ATOM   2151 C  CG1  . VAL B 1 67  ? 3.041   -29.944 16.991  1.00 35.58  ?  69  VAL B CG1  1 
ATOM   2152 C  CG2  . VAL B 1 67  ? 2.948   -27.690 15.858  1.00 33.26  ?  69  VAL B CG2  1 
ATOM   2153 N  N    . GLU B 1 68  ? 6.725   -30.247 16.418  1.00 35.04  ?  70  GLU B N    1 
ATOM   2154 C  CA   . GLU B 1 68  ? 7.485   -31.499 16.599  1.00 36.73  ?  70  GLU B CA   1 
ATOM   2155 C  C    . GLU B 1 68  ? 8.640   -31.316 17.607  1.00 36.34  ?  70  GLU B C    1 
ATOM   2156 O  O    . GLU B 1 68  ? 8.928   -32.207 18.374  1.00 34.94  ?  70  GLU B O    1 
ATOM   2157 C  CB   . GLU B 1 68  ? 8.009   -32.037 15.247  1.00 41.86  ?  70  GLU B CB   1 
ATOM   2158 C  CG   . GLU B 1 68  ? 6.910   -32.585 14.328  1.00 43.82  ?  70  GLU B CG   1 
ATOM   2159 C  CD   . GLU B 1 68  ? 6.036   -31.563 13.613  1.00 47.46  ?  70  GLU B CD   1 
ATOM   2160 O  OE1  . GLU B 1 68  ? 6.365   -30.350 13.635  1.00 42.98  ?  70  GLU B OE1  1 
ATOM   2161 O  OE2  . GLU B 1 68  ? 5.016   -31.980 13.025  1.00 50.94  ?  70  GLU B OE2  1 
ATOM   2162 N  N    . ASP B 1 69  ? 9.279   -30.141 17.613  1.00 36.81  ?  71  ASP B N    1 
ATOM   2163 C  CA   . ASP B 1 69  ? 10.296  -29.820 18.623  1.00 36.01  ?  71  ASP B CA   1 
ATOM   2164 C  C    . ASP B 1 69  ? 9.657   -29.671 20.000  1.00 34.35  ?  71  ASP B C    1 
ATOM   2165 O  O    . ASP B 1 69  ? 10.252  -30.080 21.016  1.00 34.20  ?  71  ASP B O    1 
ATOM   2166 C  CB   . ASP B 1 69  ? 11.111  -28.587 18.190  1.00 35.98  ?  71  ASP B CB   1 
ATOM   2167 C  CG   . ASP B 1 69  ? 11.902  -28.874 16.900  1.00 43.08  ?  71  ASP B CG   1 
ATOM   2168 O  OD1  . ASP B 1 69  ? 12.344  -29.998 16.729  1.00 44.77  ?  71  ASP B OD1  1 
ATOM   2169 O  OD2  . ASP B 1 69  ? 12.032  -27.969 16.064  1.00 46.10  ?  71  ASP B OD2  1 
ATOM   2170 N  N    . PHE B 1 70  ? 8.437   -29.124 20.060  1.00 32.72  ?  72  PHE B N    1 
ATOM   2171 C  CA   . PHE B 1 70  ? 7.660   -29.094 21.325  1.00 31.35  ?  72  PHE B CA   1 
ATOM   2172 C  C    . PHE B 1 70  ? 7.499   -30.520 21.894  1.00 30.70  ?  72  PHE B C    1 
ATOM   2173 O  O    . PHE B 1 70  ? 7.835   -30.745 23.049  1.00 29.98  ?  72  PHE B O    1 
ATOM   2174 C  CB   . PHE B 1 70  ? 6.270   -28.439 21.134  1.00 30.53  ?  72  PHE B CB   1 
ATOM   2175 C  CG   . PHE B 1 70  ? 5.375   -28.747 22.295  1.00 31.88  ?  72  PHE B CG   1 
ATOM   2176 C  CD1  . PHE B 1 70  ? 5.583   -28.152 23.531  1.00 32.88  ?  72  PHE B CD1  1 
ATOM   2177 C  CD2  . PHE B 1 70  ? 4.351   -29.672 22.173  1.00 32.91  ?  72  PHE B CD2  1 
ATOM   2178 C  CE1  . PHE B 1 70  ? 4.768   -28.479 24.623  1.00 31.91  ?  72  PHE B CE1  1 
ATOM   2179 C  CE2  . PHE B 1 70  ? 3.533   -29.978 23.250  1.00 31.65  ?  72  PHE B CE2  1 
ATOM   2180 C  CZ   . PHE B 1 70  ? 3.749   -29.381 24.471  1.00 30.88  ?  72  PHE B CZ   1 
ATOM   2181 N  N    . TRP B 1 71  ? 6.971   -31.439 21.090  1.00 31.74  ?  73  TRP B N    1 
ATOM   2182 C  CA   . TRP B 1 71  ? 6.724   -32.785 21.557  1.00 33.56  ?  73  TRP B CA   1 
ATOM   2183 C  C    . TRP B 1 71  ? 7.994   -33.518 21.970  1.00 33.64  ?  73  TRP B C    1 
ATOM   2184 O  O    . TRP B 1 71  ? 7.950   -34.238 22.965  1.00 35.84  ?  73  TRP B O    1 
ATOM   2185 C  CB   . TRP B 1 71  ? 5.941   -33.613 20.533  1.00 33.16  ?  73  TRP B CB   1 
ATOM   2186 C  CG   . TRP B 1 71  ? 4.482   -33.230 20.446  1.00 33.12  ?  73  TRP B CG   1 
ATOM   2187 C  CD1  . TRP B 1 71  ? 3.820   -32.815 19.329  1.00 33.78  ?  73  TRP B CD1  1 
ATOM   2188 C  CD2  . TRP B 1 71  ? 3.500   -33.293 21.494  1.00 32.01  ?  73  TRP B CD2  1 
ATOM   2189 N  NE1  . TRP B 1 71  ? 2.511   -32.560 19.623  1.00 34.71  ?  73  TRP B NE1  1 
ATOM   2190 C  CE2  . TRP B 1 71  ? 2.272   -32.892 20.934  1.00 33.32  ?  73  TRP B CE2  1 
ATOM   2191 C  CE3  . TRP B 1 71  ? 3.540   -33.667 22.858  1.00 32.10  ?  73  TRP B CE3  1 
ATOM   2192 C  CZ2  . TRP B 1 71  ? 1.101   -32.823 21.670  1.00 34.74  ?  73  TRP B CZ2  1 
ATOM   2193 C  CZ3  . TRP B 1 71  ? 2.366   -33.608 23.581  1.00 33.87  ?  73  TRP B CZ3  1 
ATOM   2194 C  CH2  . TRP B 1 71  ? 1.163   -33.202 22.988  1.00 33.86  ?  73  TRP B CH2  1 
ATOM   2195 N  N    . ALA B 1 72  ? 9.105   -33.341 21.256  1.00 33.78  ?  74  ALA B N    1 
ATOM   2196 C  CA   . ALA B 1 72  ? 10.360  -34.005 21.588  1.00 34.23  ?  74  ALA B CA   1 
ATOM   2197 C  C    . ALA B 1 72  ? 10.850  -33.499 22.950  1.00 34.10  ?  74  ALA B C    1 
ATOM   2198 O  O    . ALA B 1 72  ? 11.276  -34.300 23.795  1.00 33.77  ?  74  ALA B O    1 
ATOM   2199 C  CB   . ALA B 1 72  ? 11.398  -33.768 20.523  1.00 34.56  ?  74  ALA B CB   1 
ATOM   2200 N  N    . LEU B 1 73  ? 10.758  -32.188 23.185  1.00 33.02  ?  75  LEU B N    1 
ATOM   2201 C  CA   . LEU B 1 73  ? 11.081  -31.633 24.490  1.00 34.18  ?  75  LEU B CA   1 
ATOM   2202 C  C    . LEU B 1 73  ? 10.141  -32.124 25.598  1.00 34.31  ?  75  LEU B C    1 
ATOM   2203 O  O    . LEU B 1 73  ? 10.620  -32.580 26.651  1.00 34.84  ?  75  LEU B O    1 
ATOM   2204 C  CB   . LEU B 1 73  ? 11.105  -30.114 24.443  1.00 34.28  ?  75  LEU B CB   1 
ATOM   2205 C  CG   . LEU B 1 73  ? 11.484  -29.404 25.758  1.00 37.17  ?  75  LEU B CG   1 
ATOM   2206 C  CD1  . LEU B 1 73  ? 12.852  -29.856 26.291  1.00 37.82  ?  75  LEU B CD1  1 
ATOM   2207 C  CD2  . LEU B 1 73  ? 11.496  -27.891 25.552  1.00 38.77  ?  75  LEU B CD2  1 
ATOM   2208 N  N    . TYR B 1 74  ? 8.822   -32.038 25.377  1.00 33.26  ?  76  TYR B N    1 
ATOM   2209 C  CA   . TYR B 1 74  ? 7.818   -32.453 26.356  1.00 34.87  ?  76  TYR B CA   1 
ATOM   2210 C  C    . TYR B 1 74  ? 8.022   -33.928 26.735  1.00 36.04  ?  76  TYR B C    1 
ATOM   2211 O  O    . TYR B 1 74  ? 8.028   -34.247 27.909  1.00 36.05  ?  76  TYR B O    1 
ATOM   2212 C  CB   . TYR B 1 74  ? 6.406   -32.238 25.786  1.00 36.41  ?  76  TYR B CB   1 
ATOM   2213 C  CG   . TYR B 1 74  ? 5.292   -32.735 26.681  1.00 36.88  ?  76  TYR B CG   1 
ATOM   2214 C  CD1  . TYR B 1 74  ? 4.721   -31.912 27.622  1.00 37.78  ?  76  TYR B CD1  1 
ATOM   2215 C  CD2  . TYR B 1 74  ? 4.811   -34.036 26.577  1.00 37.78  ?  76  TYR B CD2  1 
ATOM   2216 C  CE1  . TYR B 1 74  ? 3.703   -32.363 28.450  1.00 37.89  ?  76  TYR B CE1  1 
ATOM   2217 C  CE2  . TYR B 1 74  ? 3.804   -34.503 27.407  1.00 38.35  ?  76  TYR B CE2  1 
ATOM   2218 C  CZ   . TYR B 1 74  ? 3.242   -33.655 28.338  1.00 39.73  ?  76  TYR B CZ   1 
ATOM   2219 O  OH   . TYR B 1 74  ? 2.215   -34.071 29.173  1.00 42.50  ?  76  TYR B OH   1 
ATOM   2220 N  N    . ASN B 1 75  ? 8.217   -34.782 25.749  1.00 38.30  ?  77  ASN B N    1 
ATOM   2221 C  CA   . ASN B 1 75  ? 8.433   -36.223 25.970  1.00 41.60  ?  77  ASN B CA   1 
ATOM   2222 C  C    . ASN B 1 75  ? 9.711   -36.474 26.816  1.00 43.48  ?  77  ASN B C    1 
ATOM   2223 O  O    . ASN B 1 75  ? 9.692   -37.281 27.760  1.00 44.92  ?  77  ASN B O    1 
ATOM   2224 C  CB   . ASN B 1 75  ? 8.518   -36.953 24.620  1.00 43.37  ?  77  ASN B CB   1 
ATOM   2225 C  CG   . ASN B 1 75  ? 7.213   -37.025 23.820  1.00 50.70  ?  77  ASN B CG   1 
ATOM   2226 O  OD1  . ASN B 1 75  ? 6.109   -36.872 24.339  1.00 52.87  ?  77  ASN B OD1  1 
ATOM   2227 N  ND2  . ASN B 1 75  ? 7.316   -37.279 22.511  1.00 53.14  ?  77  ASN B ND2  1 
ATOM   2228 N  N    . HIS B 1 76  ? 10.776  -35.750 26.520  1.00 42.58  ?  78  HIS B N    1 
ATOM   2229 C  CA   . HIS B 1 76  ? 12.061  -35.841 27.214  1.00 43.71  ?  78  HIS B CA   1 
ATOM   2230 C  C    . HIS B 1 76  ? 11.992  -35.402 28.670  1.00 43.72  ?  78  HIS B C    1 
ATOM   2231 O  O    . HIS B 1 76  ? 12.524  -36.111 29.556  1.00 43.24  ?  78  HIS B O    1 
ATOM   2232 C  CB   . HIS B 1 76  ? 13.135  -35.031 26.465  1.00 46.43  ?  78  HIS B CB   1 
ATOM   2233 C  CG   . HIS B 1 76  ? 14.480  -35.105 27.109  1.00 57.18  ?  78  HIS B CG   1 
ATOM   2234 N  ND1  . HIS B 1 76  ? 15.123  -33.977 27.563  1.00 60.80  ?  78  HIS B ND1  1 
ATOM   2235 C  CD2  . HIS B 1 76  ? 15.262  -36.185 27.372  1.00 60.97  ?  78  HIS B CD2  1 
ATOM   2236 C  CE1  . HIS B 1 76  ? 16.264  -34.392 28.094  1.00 61.95  ?  78  HIS B CE1  1 
ATOM   2237 N  NE2  . HIS B 1 76  ? 16.389  -35.711 28.007  1.00 62.54  ?  78  HIS B NE2  1 
ATOM   2238 N  N    . ILE B 1 77  ? 11.336  -34.256 28.939  1.00 42.40  ?  79  ILE B N    1 
ATOM   2239 C  CA   . ILE B 1 77  ? 11.143  -33.800 30.316  1.00 44.11  ?  79  ILE B CA   1 
ATOM   2240 C  C    . ILE B 1 77  ? 10.265  -34.745 31.086  1.00 48.94  ?  79  ILE B C    1 
ATOM   2241 O  O    . ILE B 1 77  ? 10.585  -35.055 32.252  1.00 49.17  ?  79  ILE B O    1 
ATOM   2242 C  CB   . ILE B 1 77  ? 10.542  -32.379 30.390  1.00 42.83  ?  79  ILE B CB   1 
ATOM   2243 C  CG1  . ILE B 1 77  ? 11.466  -31.362 29.744  1.00 43.21  ?  79  ILE B CG1  1 
ATOM   2244 C  CG2  . ILE B 1 77  ? 10.235  -31.991 31.853  1.00 43.51  ?  79  ILE B CG2  1 
ATOM   2245 C  CD1  . ILE B 1 77  ? 12.859  -31.307 30.209  1.00 44.06  ?  79  ILE B CD1  1 
ATOM   2246 N  N    . GLN B 1 78  ? 9.138   -35.191 30.454  1.00 52.19  ?  80  GLN B N    1 
ATOM   2247 C  CA   . GLN B 1 78  ? 8.098   -36.019 31.090  1.00 54.63  ?  80  GLN B CA   1 
ATOM   2248 C  C    . GLN B 1 78  ? 8.760   -37.321 31.584  1.00 58.35  ?  80  GLN B C    1 
ATOM   2249 O  O    . GLN B 1 78  ? 8.485   -37.732 32.712  1.00 59.16  ?  80  GLN B O    1 
ATOM   2250 C  CB   . GLN B 1 78  ? 6.929   -36.271 30.101  1.00 54.80  ?  80  GLN B CB   1 
ATOM   2251 C  CG   . GLN B 1 78  ? 5.614   -36.719 30.713  1.00 57.50  ?  80  GLN B CG   1 
ATOM   2252 C  CD   . GLN B 1 78  ? 4.602   -37.176 29.677  1.00 59.89  ?  80  GLN B CD   1 
ATOM   2253 O  OE1  . GLN B 1 78  ? 4.953   -37.630 28.585  1.00 60.84  ?  80  GLN B OE1  1 
ATOM   2254 N  NE2  . GLN B 1 78  ? 3.311   -37.076 29.997  1.00 61.15  ?  80  GLN B NE2  1 
ATOM   2255 N  N    . LEU B 1 79  ? 9.647   -37.949 30.789  1.00 61.28  ?  81  LEU B N    1 
ATOM   2256 C  CA   . LEU B 1 79  ? 10.368  -39.140 31.271  1.00 63.98  ?  81  LEU B CA   1 
ATOM   2257 C  C    . LEU B 1 79  ? 11.507  -38.810 32.289  1.00 66.37  ?  81  LEU B C    1 
ATOM   2258 O  O    . LEU B 1 79  ? 11.694  -39.617 33.210  1.00 67.65  ?  81  LEU B O    1 
ATOM   2259 C  CB   . LEU B 1 79  ? 10.878  -40.106 30.158  1.00 64.68  ?  81  LEU B CB   1 
ATOM   2260 C  CG   . LEU B 1 79  ? 11.689  -39.614 28.977  1.00 66.21  ?  81  LEU B CG   1 
ATOM   2261 C  CD1  . LEU B 1 79  ? 13.131  -39.373 29.344  1.00 67.08  ?  81  LEU B CD1  1 
ATOM   2262 C  CD2  . LEU B 1 79  ? 11.683  -40.663 27.865  1.00 66.48  ?  81  LEU B CD2  1 
ATOM   2263 N  N    . SER B 1 80  ? 12.246  -37.663 32.174  1.00 65.90  ?  82  SER B N    1 
ATOM   2264 C  CA   . SER B 1 80  ? 13.405  -37.406 33.049  1.00 65.65  ?  82  SER B CA   1 
ATOM   2265 C  C    . SER B 1 80  ? 13.179  -36.470 34.278  1.00 64.85  ?  82  SER B C    1 
ATOM   2266 O  O    . SER B 1 80  ? 14.156  -36.123 34.946  1.00 64.42  ?  82  SER B O    1 
ATOM   2267 C  CB   . SER B 1 80  ? 14.553  -36.856 32.223  1.00 68.02  ?  82  SER B CB   1 
ATOM   2268 O  OG   . SER B 1 80  ? 14.324  -35.502 31.885  1.00 70.86  ?  82  SER B OG   1 
ATOM   2269 N  N    . SER B 1 81  ? 11.939  -36.068 34.582  1.00 64.70  ?  83  SER B N    1 
ATOM   2270 C  CA   . SER B 1 81  ? 11.726  -34.974 35.545  1.00 65.44  ?  83  SER B CA   1 
ATOM   2271 C  C    . SER B 1 81  ? 11.854  -35.449 36.981  1.00 66.29  ?  83  SER B C    1 
ATOM   2272 O  O    . SER B 1 81  ? 12.251  -34.653 37.830  1.00 66.34  ?  83  SER B O    1 
ATOM   2273 C  CB   . SER B 1 81  ? 10.384  -34.279 35.334  1.00 66.17  ?  83  SER B CB   1 
ATOM   2274 O  OG   . SER B 1 81  ? 9.295   -35.176 35.489  1.00 68.67  ?  83  SER B OG   1 
ATOM   2275 N  N    . ASN B 1 82  ? 11.534  -36.723 37.270  1.00 67.02  ?  84  ASN B N    1 
ATOM   2276 C  CA   . ASN B 1 82  ? 11.762  -37.258 38.623  1.00 68.26  ?  84  ASN B CA   1 
ATOM   2277 C  C    . ASN B 1 82  ? 13.246  -37.137 39.065  1.00 68.84  ?  84  ASN B C    1 
ATOM   2278 O  O    . ASN B 1 82  ? 13.518  -37.081 40.266  1.00 69.63  ?  84  ASN B O    1 
ATOM   2279 C  CB   . ASN B 1 82  ? 11.251  -38.707 38.743  1.00 69.93  ?  84  ASN B CB   1 
ATOM   2280 C  CG   . ASN B 1 82  ? 11.844  -39.697 37.749  1.00 73.44  ?  84  ASN B CG   1 
ATOM   2281 O  OD1  . ASN B 1 82  ? 12.817  -39.418 37.039  1.00 74.03  ?  84  ASN B OD1  1 
ATOM   2282 N  ND2  . ASN B 1 82  ? 11.250  -40.890 37.677  1.00 75.21  ?  84  ASN B ND2  1 
ATOM   2283 N  N    . LEU B 1 83  ? 14.177  -37.082 38.089  1.00 68.48  ?  85  LEU B N    1 
ATOM   2284 C  CA   . LEU B 1 83  ? 15.619  -36.971 38.283  1.00 69.09  ?  85  LEU B CA   1 
ATOM   2285 C  C    . LEU B 1 83  ? 16.149  -35.509 38.228  1.00 69.48  ?  85  LEU B C    1 
ATOM   2286 O  O    . LEU B 1 83  ? 17.355  -35.305 38.428  1.00 70.37  ?  85  LEU B O    1 
ATOM   2287 C  CB   . LEU B 1 83  ? 16.335  -37.828 37.199  1.00 69.23  ?  85  LEU B CB   1 
ATOM   2288 C  CG   . LEU B 1 83  ? 16.147  -39.370 37.314  1.00 71.33  ?  85  LEU B CG   1 
ATOM   2289 C  CD1  . LEU B 1 83  ? 16.512  -40.085 36.007  1.00 71.91  ?  85  LEU B CD1  1 
ATOM   2290 C  CD2  . LEU B 1 83  ? 16.960  -39.961 38.492  1.00 71.91  ?  85  LEU B CD2  1 
ATOM   2291 N  N    . MET B 1 84  ? 15.282  -34.497 37.965  1.00 68.24  ?  86  MET B N    1 
ATOM   2292 C  CA   . MET B 1 84  ? 15.758  -33.111 37.841  1.00 67.19  ?  86  MET B CA   1 
ATOM   2293 C  C    . MET B 1 84  ? 15.700  -32.428 39.215  1.00 65.02  ?  86  MET B C    1 
ATOM   2294 O  O    . MET B 1 84  ? 14.728  -32.614 39.950  1.00 64.07  ?  86  MET B O    1 
ATOM   2295 C  CB   . MET B 1 84  ? 14.924  -32.303 36.809  1.00 69.06  ?  86  MET B CB   1 
ATOM   2296 C  CG   . MET B 1 84  ? 15.755  -31.768 35.611  1.00 73.25  ?  86  MET B CG   1 
ATOM   2297 S  SD   . MET B 1 84  ? 14.767  -31.034 34.315  1.00 82.53  ?  86  MET B SD   1 
ATOM   2298 C  CE   . MET B 1 84  ? 14.222  -32.523 33.499  1.00 83.62  ?  86  MET B CE   1 
ATOM   2299 N  N    . PRO B 1 85  ? 16.728  -31.642 39.593  1.00 63.93  ?  87  PRO B N    1 
ATOM   2300 C  CA   . PRO B 1 85  ? 16.768  -31.098 40.963  1.00 63.33  ?  87  PRO B CA   1 
ATOM   2301 C  C    . PRO B 1 85  ? 15.861  -29.864 41.215  1.00 61.83  ?  87  PRO B C    1 
ATOM   2302 O  O    . PRO B 1 85  ? 16.354  -28.752 41.404  1.00 60.85  ?  87  PRO B O    1 
ATOM   2303 C  CB   . PRO B 1 85  ? 18.266  -30.795 41.143  1.00 64.37  ?  87  PRO B CB   1 
ATOM   2304 C  CG   . PRO B 1 85  ? 18.701  -30.351 39.797  1.00 64.93  ?  87  PRO B CG   1 
ATOM   2305 C  CD   . PRO B 1 85  ? 17.915  -31.214 38.816  1.00 63.30  ?  87  PRO B CD   1 
ATOM   2306 N  N    . GLY B 1 86  ? 14.542  -30.086 41.215  1.00 61.44  ?  88  GLY B N    1 
ATOM   2307 C  CA   . GLY B 1 86  ? 13.550  -29.042 41.482  1.00 61.89  ?  88  GLY B CA   1 
ATOM   2308 C  C    . GLY B 1 86  ? 12.172  -29.294 40.885  1.00 60.75  ?  88  GLY B C    1 
ATOM   2309 O  O    . GLY B 1 86  ? 11.957  -30.300 40.196  1.00 61.22  ?  88  GLY B O    1 
ATOM   2310 N  N    . CYS B 1 87  ? 11.243  -28.342 41.124  1.00 58.62  ?  89  CYS B N    1 
ATOM   2311 C  CA   . CYS B 1 87  ? 9.806   -28.603 41.147  1.00 57.98  ?  89  CYS B CA   1 
ATOM   2312 C  C    . CYS B 1 87  ? 8.992   -27.455 40.485  1.00 54.27  ?  89  CYS B C    1 
ATOM   2313 O  O    . CYS B 1 87  ? 7.822   -27.232 40.856  1.00 54.68  ?  89  CYS B O    1 
ATOM   2314 C  CB   . CYS B 1 87  ? 9.381   -28.820 42.608  1.00 60.82  ?  89  CYS B CB   1 
ATOM   2315 S  SG   . CYS B 1 87  ? 9.469   -30.544 43.157  1.00 76.63  ?  89  CYS B SG   1 
ATOM   2316 N  N    . ASP B 1 88  ? 9.598   -26.711 39.532  1.00 48.45  ?  90  ASP B N    1 
ATOM   2317 C  CA   . ASP B 1 88  ? 8.966   -25.503 39.015  1.00 44.18  ?  90  ASP B CA   1 
ATOM   2318 C  C    . ASP B 1 88  ? 9.372   -25.309 37.557  1.00 39.15  ?  90  ASP B C    1 
ATOM   2319 O  O    . ASP B 1 88  ? 10.581  -25.170 37.293  1.00 38.78  ?  90  ASP B O    1 
ATOM   2320 C  CB   . ASP B 1 88  ? 9.426   -24.316 39.846  1.00 46.95  ?  90  ASP B CB   1 
ATOM   2321 C  CG   . ASP B 1 88  ? 8.977   -24.396 41.296  1.00 53.71  ?  90  ASP B CG   1 
ATOM   2322 O  OD1  . ASP B 1 88  ? 7.765   -24.339 41.537  1.00 49.75  ?  90  ASP B OD1  1 
ATOM   2323 O  OD2  . ASP B 1 88  ? 9.849   -24.544 42.181  1.00 59.55  ?  90  ASP B OD2  1 
ATOM   2324 N  N    . TYR B 1 89  ? 8.393   -25.332 36.620  1.00 35.12  ?  91  TYR B N    1 
ATOM   2325 C  CA   . TYR B 1 89  ? 8.684   -25.207 35.177  1.00 34.12  ?  91  TYR B CA   1 
ATOM   2326 C  C    . TYR B 1 89  ? 7.860   -24.061 34.653  1.00 30.86  ?  91  TYR B C    1 
ATOM   2327 O  O    . TYR B 1 89  ? 6.763   -23.812 35.143  1.00 30.32  ?  91  TYR B O    1 
ATOM   2328 C  CB   . TYR B 1 89  ? 8.289   -26.473 34.399  1.00 34.73  ?  91  TYR B CB   1 
ATOM   2329 C  CG   . TYR B 1 89  ? 9.188   -27.653 34.686  1.00 37.90  ?  91  TYR B CG   1 
ATOM   2330 C  CD1  . TYR B 1 89  ? 8.967   -28.466 35.781  1.00 41.01  ?  91  TYR B CD1  1 
ATOM   2331 C  CD2  . TYR B 1 89  ? 10.254  -27.963 33.852  1.00 40.65  ?  91  TYR B CD2  1 
ATOM   2332 C  CE1  . TYR B 1 89  ? 9.769   -29.577 36.034  1.00 42.90  ?  91  TYR B CE1  1 
ATOM   2333 C  CE2  . TYR B 1 89  ? 11.051  -29.078 34.088  1.00 42.79  ?  91  TYR B CE2  1 
ATOM   2334 C  CZ   . TYR B 1 89  ? 10.806  -29.881 35.188  1.00 45.61  ?  91  TYR B CZ   1 
ATOM   2335 O  OH   . TYR B 1 89  ? 11.588  -30.984 35.484  1.00 49.98  ?  91  TYR B OH   1 
ATOM   2336 N  N    . SER B 1 90  ? 8.392   -23.392 33.638  1.00 30.23  ?  92  SER B N    1 
ATOM   2337 C  CA   . SER B 1 90  ? 7.741   -22.279 32.990  1.00 29.18  ?  92  SER B CA   1 
ATOM   2338 C  C    . SER B 1 90  ? 7.946   -22.338 31.481  1.00 29.00  ?  92  SER B C    1 
ATOM   2339 O  O    . SER B 1 90  ? 9.053   -22.647 31.046  1.00 32.25  ?  92  SER B O    1 
ATOM   2340 C  CB   . SER B 1 90  ? 8.273   -20.949 33.531  1.00 28.93  ?  92  SER B CB   1 
ATOM   2341 O  OG   . SER B 1 90  ? 8.098   -20.849 34.942  1.00 35.96  ?  92  SER B OG   1 
ATOM   2342 N  N    . LEU B 1 91  ? 6.927   -22.070 30.706  1.00 27.39  ?  93  LEU B N    1 
ATOM   2343 C  CA   . LEU B 1 91  ? 7.045   -21.944 29.267  1.00 28.59  ?  93  LEU B CA   1 
ATOM   2344 C  C    . LEU B 1 91  ? 6.695   -20.519 28.898  1.00 28.37  ?  93  LEU B C    1 
ATOM   2345 O  O    . LEU B 1 91  ? 5.536   -20.121 29.097  1.00 28.29  ?  93  LEU B O    1 
ATOM   2346 C  CB   . LEU B 1 91  ? 6.113   -22.896 28.508  1.00 29.39  ?  93  LEU B CB   1 
ATOM   2347 C  CG   . LEU B 1 91  ? 6.359   -22.879 26.995  1.00 30.67  ?  93  LEU B CG   1 
ATOM   2348 C  CD1  . LEU B 1 91  ? 7.572   -23.728 26.672  1.00 32.48  ?  93  LEU B CD1  1 
ATOM   2349 C  CD2  . LEU B 1 91  ? 5.175   -23.354 26.199  1.00 32.42  ?  93  LEU B CD2  1 
ATOM   2350 N  N    . PHE B 1 92  ? 7.675   -19.745 28.392  1.00 26.03  ?  94  PHE B N    1 
ATOM   2351 C  CA   . PHE B 1 92  ? 7.453   -18.341 28.027  1.00 26.89  ?  94  PHE B CA   1 
ATOM   2352 C  C    . PHE B 1 92  ? 7.832   -18.006 26.631  1.00 27.19  ?  94  PHE B C    1 
ATOM   2353 O  O    . PHE B 1 92  ? 8.717   -18.645 26.015  1.00 27.47  ?  94  PHE B O    1 
ATOM   2354 C  CB   . PHE B 1 92  ? 8.180   -17.381 29.015  1.00 26.39  ?  94  PHE B CB   1 
ATOM   2355 C  CG   . PHE B 1 92  ? 7.389   -17.093 30.252  1.00 26.68  ?  94  PHE B CG   1 
ATOM   2356 C  CD1  . PHE B 1 92  ? 7.155   -18.095 31.204  1.00 28.69  ?  94  PHE B CD1  1 
ATOM   2357 C  CD2  . PHE B 1 92  ? 6.849   -15.842 30.466  1.00 28.24  ?  94  PHE B CD2  1 
ATOM   2358 C  CE1  . PHE B 1 92  ? 6.362   -17.847 32.314  1.00 30.08  ?  94  PHE B CE1  1 
ATOM   2359 C  CE2  . PHE B 1 92  ? 6.060   -15.610 31.577  1.00 29.67  ?  94  PHE B CE2  1 
ATOM   2360 C  CZ   . PHE B 1 92  ? 5.843   -16.601 32.498  1.00 29.47  ?  94  PHE B CZ   1 
ATOM   2361 N  N    . LYS B 1 93  ? 7.163   -17.002 26.065  1.00 27.74  ?  95  LYS B N    1 
ATOM   2362 C  CA   . LYS B 1 93  ? 7.539   -16.534 24.723  1.00 27.70  ?  95  LYS B CA   1 
ATOM   2363 C  C    . LYS B 1 93  ? 9.032   -16.106 24.730  1.00 28.30  ?  95  LYS B C    1 
ATOM   2364 O  O    . LYS B 1 93  ? 9.562   -15.577 25.730  1.00 27.88  ?  95  LYS B O    1 
ATOM   2365 C  CB   . LYS B 1 93  ? 6.645   -15.407 24.227  1.00 29.71  ?  95  LYS B CB   1 
ATOM   2366 C  CG   . LYS B 1 93  ? 5.254   -15.832 23.927  1.00 31.17  ?  95  LYS B CG   1 
ATOM   2367 C  CD   . LYS B 1 93  ? 4.438   -14.716 23.542  1.00 32.67  ?  95  LYS B CD   1 
ATOM   2368 C  CE   . LYS B 1 93  ? 3.104   -15.187 23.075  1.00 34.27  ?  95  LYS B CE   1 
ATOM   2369 N  NZ   . LYS B 1 93  ? 2.214   -14.069 22.871  1.00 32.61  ?  95  LYS B NZ   1 
ATOM   2370 N  N    . ASP B 1 94  ? 9.703   -16.354 23.643  1.00 30.67  ?  96  ASP B N    1 
ATOM   2371 C  CA   . ASP B 1 94  ? 11.136  -16.057 23.481  1.00 31.56  ?  96  ASP B CA   1 
ATOM   2372 C  C    . ASP B 1 94  ? 11.375  -14.536 23.798  1.00 34.20  ?  96  ASP B C    1 
ATOM   2373 O  O    . ASP B 1 94  ? 10.656  -13.691 23.291  1.00 34.84  ?  96  ASP B O    1 
ATOM   2374 C  CB   . ASP B 1 94  ? 11.589  -16.444 22.067  1.00 32.63  ?  96  ASP B CB   1 
ATOM   2375 C  CG   . ASP B 1 94  ? 13.080  -16.541 21.856  1.00 36.97  ?  96  ASP B CG   1 
ATOM   2376 O  OD1  . ASP B 1 94  ? 13.822  -16.541 22.858  1.00 36.50  ?  96  ASP B OD1  1 
ATOM   2377 O  OD2  . ASP B 1 94  ? 13.494  -16.656 20.682  1.00 38.84  ?  96  ASP B OD2  1 
ATOM   2378 N  N    . GLY B 1 95  ? 12.326  -14.248 24.677  1.00 34.39  ?  97  GLY B N    1 
ATOM   2379 C  CA   . GLY B 1 95  ? 12.575  -12.869 25.093  1.00 35.71  ?  97  GLY B CA   1 
ATOM   2380 C  C    . GLY B 1 95  ? 11.847  -12.424 26.340  1.00 37.48  ?  97  GLY B C    1 
ATOM   2381 O  O    . GLY B 1 95  ? 12.032  -11.279 26.762  1.00 40.45  ?  97  GLY B O    1 
ATOM   2382 N  N    . ILE B 1 96  ? 11.018  -13.273 26.945  1.00 36.25  ?  98  ILE B N    1 
ATOM   2383 C  CA   . ILE B 1 96  ? 10.377  -12.952 28.218  1.00 34.85  ?  98  ILE B CA   1 
ATOM   2384 C  C    . ILE B 1 96  ? 10.947  -13.859 29.288  1.00 37.76  ?  98  ILE B C    1 
ATOM   2385 O  O    . ILE B 1 96  ? 10.832  -15.082 29.182  1.00 38.26  ?  98  ILE B O    1 
ATOM   2386 C  CB   . ILE B 1 96  ? 8.840   -13.059 28.188  1.00 32.73  ?  98  ILE B CB   1 
ATOM   2387 C  CG1  . ILE B 1 96  ? 8.222   -12.254 27.054  1.00 32.29  ?  98  ILE B CG1  1 
ATOM   2388 C  CG2  . ILE B 1 96  ? 8.241   -12.673 29.534  1.00 32.50  ?  98  ILE B CG2  1 
ATOM   2389 C  CD1  . ILE B 1 96  ? 6.679   -12.344 26.923  1.00 32.86  ?  98  ILE B CD1  1 
ATOM   2390 N  N    . GLU B 1 97  ? 11.530  -13.275 30.343  1.00 39.68  ?  99  GLU B N    1 
ATOM   2391 C  CA   . GLU B 1 97  ? 11.938  -14.073 31.493  1.00 42.17  ?  99  GLU B CA   1 
ATOM   2392 C  C    . GLU B 1 97  ? 10.729  -14.417 32.373  1.00 40.35  ?  99  GLU B C    1 
ATOM   2393 O  O    . GLU B 1 97  ? 9.825   -13.593 32.489  1.00 39.94  ?  99  GLU B O    1 
ATOM   2394 C  CB   . GLU B 1 97  ? 12.991  -13.333 32.295  1.00 48.16  ?  99  GLU B CB   1 
ATOM   2395 C  CG   . GLU B 1 97  ? 14.233  -13.057 31.483  1.00 61.92  ?  99  GLU B CG   1 
ATOM   2396 C  CD   . GLU B 1 97  ? 15.415  -12.648 32.338  1.00 80.34  ?  99  GLU B CD   1 
ATOM   2397 O  OE1  . GLU B 1 97  ? 15.202  -12.129 33.460  1.00 85.29  ?  99  GLU B OE1  1 
ATOM   2398 O  OE2  . GLU B 1 97  ? 16.562  -12.854 31.880  1.00 86.72  ?  99  GLU B OE2  1 
ATOM   2399 N  N    . PRO B 1 98  ? 10.703  -15.631 32.980  1.00 39.88  ?  100 PRO B N    1 
ATOM   2400 C  CA   . PRO B 1 98  ? 9.557   -16.031 33.811  1.00 39.56  ?  100 PRO B CA   1 
ATOM   2401 C  C    . PRO B 1 98  ? 9.624   -15.426 35.219  1.00 38.68  ?  100 PRO B C    1 
ATOM   2402 O  O    . PRO B 1 98  ? 9.542   -16.145 36.221  1.00 38.59  ?  100 PRO B O    1 
ATOM   2403 C  CB   . PRO B 1 98  ? 9.670   -17.565 33.833  1.00 40.86  ?  100 PRO B CB   1 
ATOM   2404 C  CG   . PRO B 1 98  ? 11.130  -17.820 33.724  1.00 41.63  ?  100 PRO B CG   1 
ATOM   2405 C  CD   . PRO B 1 98  ? 11.718  -16.703 32.910  1.00 40.42  ?  100 PRO B CD   1 
ATOM   2406 N  N    . MET B 1 99  ? 9.755   -14.096 35.272  1.00 38.66  ?  101 MET B N    1 
ATOM   2407 C  CA   . MET B 1 99  ? 9.888   -13.304 36.508  1.00 39.84  ?  101 MET B CA   1 
ATOM   2408 C  C    . MET B 1 99  ? 8.956   -12.100 36.336  1.00 40.61  ?  101 MET B C    1 
ATOM   2409 O  O    . MET B 1 99  ? 8.916   -11.483 35.254  1.00 39.14  ?  101 MET B O    1 
ATOM   2410 C  CB   . MET B 1 99  ? 11.348  -12.819 36.662  1.00 41.44  ?  101 MET B CB   1 
ATOM   2411 C  CG   . MET B 1 99  ? 12.394  -13.930 36.709  1.00 46.92  ?  101 MET B CG   1 
ATOM   2412 S  SD   . MET B 1 99  ? 12.347  -15.007 38.170  1.00 58.72  ?  101 MET B SD   1 
ATOM   2413 C  CE   . MET B 1 99  ? 12.684  -13.831 39.446  1.00 61.07  ?  101 MET B CE   1 
ATOM   2414 N  N    . TRP B 1 100 ? 8.230   -11.761 37.382  1.00 43.03  ?  102 TRP B N    1 
ATOM   2415 C  CA   . TRP B 1 100 ? 7.172   -10.752 37.254  1.00 47.17  ?  102 TRP B CA   1 
ATOM   2416 C  C    . TRP B 1 100 ? 7.762   -9.364  36.988  1.00 47.49  ?  102 TRP B C    1 
ATOM   2417 O  O    . TRP B 1 100 ? 7.050   -8.534  36.468  1.00 49.24  ?  102 TRP B O    1 
ATOM   2418 C  CB   . TRP B 1 100 ? 6.191   -10.795 38.453  1.00 48.87  ?  102 TRP B CB   1 
ATOM   2419 C  CG   . TRP B 1 100 ? 6.611   -10.007 39.663  1.00 51.09  ?  102 TRP B CG   1 
ATOM   2420 C  CD1  . TRP B 1 100 ? 7.356   -10.459 40.715  1.00 51.96  ?  102 TRP B CD1  1 
ATOM   2421 C  CD2  . TRP B 1 100 ? 6.220   -8.652  39.999  1.00 51.70  ?  102 TRP B CD2  1 
ATOM   2422 N  NE1  . TRP B 1 100 ? 7.487   -9.466  41.665  1.00 52.44  ?  102 TRP B NE1  1 
ATOM   2423 C  CE2  . TRP B 1 100 ? 6.788   -8.352  41.257  1.00 52.12  ?  102 TRP B CE2  1 
ATOM   2424 C  CE3  . TRP B 1 100 ? 5.425   -7.689  39.375  1.00 52.27  ?  102 TRP B CE3  1 
ATOM   2425 C  CZ2  . TRP B 1 100 ? 6.600   -7.125  41.891  1.00 52.81  ?  102 TRP B CZ2  1 
ATOM   2426 C  CZ3  . TRP B 1 100 ? 5.238   -6.470  40.004  1.00 53.13  ?  102 TRP B CZ3  1 
ATOM   2427 C  CH2  . TRP B 1 100 ? 5.822   -6.199  41.250  1.00 52.94  ?  102 TRP B CH2  1 
ATOM   2428 N  N    . GLU B 1 101 ? 9.066   -9.132  37.290  1.00 47.80  ?  103 GLU B N    1 
ATOM   2429 C  CA   . GLU B 1 101 ? 9.761   -7.856  37.072  1.00 49.54  ?  103 GLU B CA   1 
ATOM   2430 C  C    . GLU B 1 101 ? 10.169  -7.647  35.641  1.00 48.98  ?  103 GLU B C    1 
ATOM   2431 O  O    . GLU B 1 101 ? 10.577  -6.532  35.289  1.00 49.53  ?  103 GLU B O    1 
ATOM   2432 C  CB   . GLU B 1 101 ? 11.046  -7.743  37.938  1.00 54.10  ?  103 GLU B CB   1 
ATOM   2433 C  CG   . GLU B 1 101 ? 10.846  -7.855  39.434  1.00 58.93  ?  103 GLU B CG   1 
ATOM   2434 C  CD   . GLU B 1 101 ? 10.856  -9.252  40.039  1.00 64.74  ?  103 GLU B CD   1 
ATOM   2435 O  OE1  . GLU B 1 101 ? 10.699  -9.330  41.280  1.00 67.71  ?  103 GLU B OE1  1 
ATOM   2436 O  OE2  . GLU B 1 101 ? 11.028  -10.256 39.300  1.00 62.01  ?  103 GLU B OE2  1 
ATOM   2437 N  N    . ASP B 1 102 ? 10.078  -8.704  34.758  1.00 46.83  ?  104 ASP B N    1 
ATOM   2438 C  CA   . ASP B 1 102 ? 10.285  -8.521  33.329  1.00 43.97  ?  104 ASP B CA   1 
ATOM   2439 C  C    . ASP B 1 102 ? 9.340   -7.431  32.790  1.00 42.44  ?  104 ASP B C    1 
ATOM   2440 O  O    . ASP B 1 102 ? 8.201   -7.320  33.225  1.00 40.49  ?  104 ASP B O    1 
ATOM   2441 C  CB   . ASP B 1 102 ? 10.099  -9.850  32.567  1.00 43.03  ?  104 ASP B CB   1 
ATOM   2442 C  CG   . ASP B 1 102 ? 10.509  -9.812  31.112  1.00 45.60  ?  104 ASP B CG   1 
ATOM   2443 O  OD1  . ASP B 1 102 ? 9.794   -9.146  30.295  1.00 45.35  ?  104 ASP B OD1  1 
ATOM   2444 O  OD2  . ASP B 1 102 ? 11.552  -10.435 30.771  1.00 45.83  ?  104 ASP B OD2  1 
ATOM   2445 N  N    . GLU B 1 103 ? 9.824   -6.618  31.851  1.00 44.02  ?  105 GLU B N    1 
ATOM   2446 C  CA   . GLU B 1 103 ? 9.052   -5.528  31.230  1.00 45.02  ?  105 GLU B CA   1 
ATOM   2447 C  C    . GLU B 1 103 ? 7.664   -6.021  30.727  1.00 43.40  ?  105 GLU B C    1 
ATOM   2448 O  O    . GLU B 1 103 ? 6.652   -5.315  30.882  1.00 43.95  ?  105 GLU B O    1 
ATOM   2449 C  CB   . GLU B 1 103 ? 9.877   -4.931  30.073  1.00 50.28  ?  105 GLU B CB   1 
ATOM   2450 C  CG   . GLU B 1 103 ? 9.271   -3.736  29.366  1.00 62.00  ?  105 GLU B CG   1 
ATOM   2451 C  CD   . GLU B 1 103 ? 9.733   -2.404  29.927  1.00 71.52  ?  105 GLU B CD   1 
ATOM   2452 O  OE1  . GLU B 1 103 ? 9.743   -2.254  31.171  1.00 71.05  ?  105 GLU B OE1  1 
ATOM   2453 O  OE2  . GLU B 1 103 ? 10.088  -1.511  29.121  1.00 75.92  ?  105 GLU B OE2  1 
ATOM   2454 N  N    . LYS B 1 104 ? 7.628   -7.234  30.153  1.00 41.12  ?  106 LYS B N    1 
ATOM   2455 C  CA   . LYS B 1 104 ? 6.392   -7.828  29.634  1.00 39.43  ?  106 LYS B CA   1 
ATOM   2456 C  C    . LYS B 1 104 ? 5.488   -8.426  30.698  1.00 36.77  ?  106 LYS B C    1 
ATOM   2457 O  O    . LYS B 1 104 ? 4.350   -8.727  30.377  1.00 36.26  ?  106 LYS B O    1 
ATOM   2458 C  CB   . LYS B 1 104 ? 6.692   -8.885  28.525  1.00 40.57  ?  106 LYS B CB   1 
ATOM   2459 C  CG   . LYS B 1 104 ? 7.351   -8.324  27.295  1.00 46.53  ?  106 LYS B CG   1 
ATOM   2460 C  CD   . LYS B 1 104 ? 6.437   -7.437  26.476  1.00 49.64  ?  106 LYS B CD   1 
ATOM   2461 C  CE   . LYS B 1 104 ? 7.139   -6.904  25.239  1.00 54.93  ?  106 LYS B CE   1 
ATOM   2462 N  NZ   . LYS B 1 104 ? 6.860   -7.753  24.054  1.00 58.38  ?  106 LYS B NZ   1 
ATOM   2463 N  N    . ASN B 1 105 ? 5.950   -8.582  31.938  1.00 36.25  ?  107 ASN B N    1 
ATOM   2464 C  CA   . ASN B 1 105 ? 5.168   -9.127  33.041  1.00 35.69  ?  107 ASN B CA   1 
ATOM   2465 C  C    . ASN B 1 105 ? 4.785   -8.105  34.110  1.00 36.37  ?  107 ASN B C    1 
ATOM   2466 O  O    . ASN B 1 105 ? 3.788   -8.325  34.790  1.00 35.18  ?  107 ASN B O    1 
ATOM   2467 C  CB   . ASN B 1 105 ? 5.907   -10.281 33.720  1.00 35.04  ?  107 ASN B CB   1 
ATOM   2468 C  CG   . ASN B 1 105 ? 6.152   -11.448 32.781  1.00 35.59  ?  107 ASN B CG   1 
ATOM   2469 O  OD1  . ASN B 1 105 ? 5.317   -11.783 31.934  1.00 33.39  ?  107 ASN B OD1  1 
ATOM   2470 N  ND2  . ASN B 1 105 ? 7.283   -12.088 32.893  1.00 36.55  ?  107 ASN B ND2  1 
ATOM   2471 N  N    . LYS B 1 106 ? 5.551   -7.025  34.258  1.00 39.01  ?  108 LYS B N    1 
ATOM   2472 C  CA   . LYS B 1 106 ? 5.371   -6.135  35.418  1.00 41.77  ?  108 LYS B CA   1 
ATOM   2473 C  C    . LYS B 1 106 ? 3.980   -5.520  35.529  1.00 41.54  ?  108 LYS B C    1 
ATOM   2474 O  O    . LYS B 1 106 ? 3.482   -5.326  36.647  1.00 42.36  ?  108 LYS B O    1 
ATOM   2475 C  CB   . LYS B 1 106 ? 6.457   -5.051  35.494  1.00 46.11  ?  108 LYS B CB   1 
ATOM   2476 C  CG   . LYS B 1 106 ? 6.480   -4.075  34.352  1.00 53.43  ?  108 LYS B CG   1 
ATOM   2477 C  CD   . LYS B 1 106 ? 7.744   -3.214  34.423  1.00 61.58  ?  108 LYS B CD   1 
ATOM   2478 C  CE   . LYS B 1 106 ? 7.637   -1.977  33.575  1.00 68.28  ?  108 LYS B CE   1 
ATOM   2479 N  NZ   . LYS B 1 106 ? 8.786   -1.057  33.812  1.00 73.66  ?  108 LYS B NZ   1 
ATOM   2480 N  N    . ARG B 1 107 ? 3.349   -5.231  34.395  1.00 40.37  ?  109 ARG B N    1 
ATOM   2481 C  CA   . ARG B 1 107 ? 1.978   -4.710  34.400  1.00 41.27  ?  109 ARG B CA   1 
ATOM   2482 C  C    . ARG B 1 107 ? 0.883   -5.763  34.277  1.00 38.88  ?  109 ARG B C    1 
ATOM   2483 O  O    . ARG B 1 107 ? -0.290  -5.429  34.108  1.00 38.85  ?  109 ARG B O    1 
ATOM   2484 C  CB   . ARG B 1 107 ? 1.833   -3.648  33.288  1.00 43.63  ?  109 ARG B CB   1 
ATOM   2485 C  CG   . ARG B 1 107 ? 2.829   -2.454  33.348  1.00 55.32  ?  109 ARG B CG   1 
ATOM   2486 C  CD   . ARG B 1 107 ? 2.909   -1.849  34.754  1.00 66.42  ?  109 ARG B CD   1 
ATOM   2487 N  NE   . ARG B 1 107 ? 3.094   -0.391  34.779  1.00 76.02  ?  109 ARG B NE   1 
ATOM   2488 C  CZ   . ARG B 1 107 ? 3.459   0.304   35.860  1.00 81.60  ?  109 ARG B CZ   1 
ATOM   2489 N  NH1  . ARG B 1 107 ? 3.593   1.625   35.793  1.00 82.16  ?  109 ARG B NH1  1 
ATOM   2490 N  NH2  . ARG B 1 107 ? 3.699   -0.321  37.016  1.00 82.12  ?  109 ARG B NH2  1 
ATOM   2491 N  N    . GLY B 1 108 ? 1.265   -7.024  34.378  1.00 38.05  ?  110 GLY B N    1 
ATOM   2492 C  CA   . GLY B 1 108 ? 0.380   -8.112  34.084  1.00 37.71  ?  110 GLY B CA   1 
ATOM   2493 C  C    . GLY B 1 108 ? -0.078  -8.835  35.313  1.00 35.38  ?  110 GLY B C    1 
ATOM   2494 O  O    . GLY B 1 108 ? -0.062  -8.298  36.420  1.00 35.28  ?  110 GLY B O    1 
ATOM   2495 N  N    . GLY B 1 109 ? -0.487  -10.051 35.076  1.00 33.07  ?  111 GLY B N    1 
ATOM   2496 C  CA   . GLY B 1 109 ? -1.029  -10.953 36.075  1.00 31.43  ?  111 GLY B CA   1 
ATOM   2497 C  C    . GLY B 1 109 ? -1.204  -12.345 35.517  1.00 31.52  ?  111 GLY B C    1 
ATOM   2498 O  O    . GLY B 1 109 ? -0.654  -12.680 34.444  1.00 28.66  ?  111 GLY B O    1 
ATOM   2499 N  N    . ARG B 1 110 ? -1.976  -13.166 36.226  1.00 30.93  ?  112 ARG B N    1 
ATOM   2500 C  CA   . ARG B 1 110 ? -2.079  -14.592 35.916  1.00 30.81  ?  112 ARG B CA   1 
ATOM   2501 C  C    . ARG B 1 110 ? -3.471  -15.112 36.214  1.00 30.76  ?  112 ARG B C    1 
ATOM   2502 O  O    . ARG B 1 110 ? -4.055  -14.739 37.217  1.00 32.65  ?  112 ARG B O    1 
ATOM   2503 C  CB   . ARG B 1 110 ? -1.015  -15.400 36.675  1.00 31.07  ?  112 ARG B CB   1 
ATOM   2504 C  CG   . ARG B 1 110 ? -1.193  -15.380 38.182  1.00 35.06  ?  112 ARG B CG   1 
ATOM   2505 C  CD   . ARG B 1 110 ? -0.094  -16.099 38.915  1.00 38.44  ?  112 ARG B CD   1 
ATOM   2506 N  NE   . ARG B 1 110 ? -0.385  -16.142 40.373  1.00 40.04  ?  112 ARG B NE   1 
ATOM   2507 C  CZ   . ARG B 1 110 ? 0.275   -16.889 41.259  1.00 41.37  ?  112 ARG B CZ   1 
ATOM   2508 N  NH1  . ARG B 1 110 ? -0.049  -16.846 42.537  1.00 43.89  ?  112 ARG B NH1  1 
ATOM   2509 N  NH2  . ARG B 1 110 ? 1.260   -17.693 40.865  1.00 37.45  ?  112 ARG B NH2  1 
ATOM   2510 N  N    . TRP B 1 111 ? -3.973  -15.963 35.337  1.00 31.09  ?  113 TRP B N    1 
ATOM   2511 C  CA   . TRP B 1 111 ? -5.081  -16.894 35.585  1.00 31.82  ?  113 TRP B CA   1 
ATOM   2512 C  C    . TRP B 1 111 ? -4.550  -18.111 36.302  1.00 33.46  ?  113 TRP B C    1 
ATOM   2513 O  O    . TRP B 1 111 ? -3.706  -18.834 35.748  1.00 31.73  ?  113 TRP B O    1 
ATOM   2514 C  CB   . TRP B 1 111 ? -5.746  -17.338 34.286  1.00 31.89  ?  113 TRP B CB   1 
ATOM   2515 C  CG   . TRP B 1 111 ? -6.658  -16.321 33.712  1.00 34.42  ?  113 TRP B CG   1 
ATOM   2516 C  CD1  . TRP B 1 111 ? -6.458  -15.586 32.588  1.00 35.78  ?  113 TRP B CD1  1 
ATOM   2517 C  CD2  . TRP B 1 111 ? -7.911  -15.898 34.256  1.00 35.59  ?  113 TRP B CD2  1 
ATOM   2518 N  NE1  . TRP B 1 111 ? -7.503  -14.714 32.409  1.00 36.66  ?  113 TRP B NE1  1 
ATOM   2519 C  CE2  . TRP B 1 111 ? -8.412  -14.893 33.415  1.00 36.01  ?  113 TRP B CE2  1 
ATOM   2520 C  CE3  . TRP B 1 111 ? -8.672  -16.284 35.372  1.00 36.22  ?  113 TRP B CE3  1 
ATOM   2521 C  CZ2  . TRP B 1 111 ? -9.641  -14.282 33.644  1.00 36.85  ?  113 TRP B CZ2  1 
ATOM   2522 C  CZ3  . TRP B 1 111 ? -9.883  -15.658 35.602  1.00 36.91  ?  113 TRP B CZ3  1 
ATOM   2523 C  CH2  . TRP B 1 111 ? -10.340 -14.655 34.755  1.00 37.43  ?  113 TRP B CH2  1 
ATOM   2524 N  N    . LEU B 1 112 ? -5.036  -18.352 37.552  1.00 33.64  ?  114 LEU B N    1 
ATOM   2525 C  CA   . LEU B 1 112 ? -4.441  -19.352 38.435  1.00 36.02  ?  114 LEU B CA   1 
ATOM   2526 C  C    . LEU B 1 112 ? -5.394  -20.497 38.678  1.00 36.98  ?  114 LEU B C    1 
ATOM   2527 O  O    . LEU B 1 112 ? -6.559  -20.270 38.990  1.00 38.35  ?  114 LEU B O    1 
ATOM   2528 C  CB   . LEU B 1 112 ? -4.045  -18.690 39.759  1.00 37.81  ?  114 LEU B CB   1 
ATOM   2529 C  CG   . LEU B 1 112 ? -3.551  -19.608 40.907  1.00 39.51  ?  114 LEU B CG   1 
ATOM   2530 C  CD1  . LEU B 1 112 ? -2.180  -20.191 40.602  1.00 39.64  ?  114 LEU B CD1  1 
ATOM   2531 C  CD2  . LEU B 1 112 ? -3.458  -18.818 42.211  1.00 42.03  ?  114 LEU B CD2  1 
ATOM   2532 N  N    . ILE B 1 113 ? -4.886  -21.711 38.547  1.00 36.74  ?  115 ILE B N    1 
ATOM   2533 C  CA   . ILE B 1 113 ? -5.562  -22.985 38.852  1.00 38.55  ?  115 ILE B CA   1 
ATOM   2534 C  C    . ILE B 1 113 ? -4.825  -23.562 40.054  1.00 38.72  ?  115 ILE B C    1 
ATOM   2535 O  O    . ILE B 1 113 ? -3.630  -23.795 39.998  1.00 35.74  ?  115 ILE B O    1 
ATOM   2536 C  CB   . ILE B 1 113 ? -5.496  -23.986 37.653  1.00 41.17  ?  115 ILE B CB   1 
ATOM   2537 C  CG1  . ILE B 1 113 ? -5.721  -23.313 36.292  1.00 43.00  ?  115 ILE B CG1  1 
ATOM   2538 C  CG2  . ILE B 1 113 ? -6.462  -25.173 37.862  1.00 43.47  ?  115 ILE B CG2  1 
ATOM   2539 C  CD1  . ILE B 1 113 ? -7.092  -22.653 36.106  1.00 44.32  ?  115 ILE B CD1  1 
ATOM   2540 N  N    . THR B 1 114 ? -5.545  -23.789 41.130  1.00 42.68  ?  116 THR B N    1 
ATOM   2541 C  CA   . THR B 1 114 ? -5.000  -24.414 42.316  1.00 46.64  ?  116 THR B CA   1 
ATOM   2542 C  C    . THR B 1 114 ? -5.540  -25.830 42.364  1.00 48.12  ?  116 THR B C    1 
ATOM   2543 O  O    . THR B 1 114 ? -6.760  -26.013 42.242  1.00 47.73  ?  116 THR B O    1 
ATOM   2544 C  CB   . THR B 1 114 ? -5.393  -23.616 43.557  1.00 52.06  ?  116 THR B CB   1 
ATOM   2545 O  OG1  . THR B 1 114 ? -6.812  -23.406 43.549  1.00 56.27  ?  116 THR B OG1  1 
ATOM   2546 C  CG2  . THR B 1 114 ? -4.716  -22.250 43.602  1.00 52.90  ?  116 THR B CG2  1 
ATOM   2547 N  N    . LEU B 1 115 ? -4.638  -26.810 42.559  1.00 48.93  ?  117 LEU B N    1 
ATOM   2548 C  CA   . LEU B 1 115 ? -4.943  -28.232 42.545  1.00 52.08  ?  117 LEU B CA   1 
ATOM   2549 C  C    . LEU B 1 115 ? -4.576  -28.772 43.917  1.00 56.72  ?  117 LEU B C    1 
ATOM   2550 O  O    . LEU B 1 115 ? -3.380  -28.921 44.234  1.00 58.07  ?  117 LEU B O    1 
ATOM   2551 C  CB   . LEU B 1 115 ? -4.129  -28.966 41.491  1.00 51.68  ?  117 LEU B CB   1 
ATOM   2552 C  CG   . LEU B 1 115 ? -4.332  -28.519 40.039  1.00 53.58  ?  117 LEU B CG   1 
ATOM   2553 C  CD1  . LEU B 1 115 ? -3.521  -29.340 39.147  1.00 54.90  ?  117 LEU B CD1  1 
ATOM   2554 C  CD2  . LEU B 1 115 ? -5.796  -28.654 39.596  1.00 54.16  ?  117 LEU B CD2  1 
ATOM   2555 N  N    . ASN B 1 116 ? -5.578  -29.053 44.712  1.00 58.67  ?  118 ASN B N    1 
ATOM   2556 C  CA   . ASN B 1 116 ? -5.326  -29.563 46.048  1.00 62.61  ?  118 ASN B CA   1 
ATOM   2557 C  C    . ASN B 1 116 ? -5.047  -31.083 45.947  1.00 65.64  ?  118 ASN B C    1 
ATOM   2558 O  O    . ASN B 1 116 ? -5.765  -31.774 45.233  1.00 66.99  ?  118 ASN B O    1 
ATOM   2559 C  CB   . ASN B 1 116 ? -6.454  -29.132 46.994  1.00 64.91  ?  118 ASN B CB   1 
ATOM   2560 C  CG   . ASN B 1 116 ? -6.490  -27.594 47.170  1.00 70.72  ?  118 ASN B CG   1 
ATOM   2561 O  OD1  . ASN B 1 116 ? -5.449  -26.911 47.351  1.00 72.61  ?  118 ASN B OD1  1 
ATOM   2562 N  ND2  . ASN B 1 116 ? -7.678  -26.987 47.119  1.00 72.07  ?  118 ASN B ND2  1 
ATOM   2563 N  N    . LYS B 1 117 ? -3.961  -31.553 46.619  1.00 66.60  ?  119 LYS B N    1 
ATOM   2564 C  CA   . LYS B 1 117 ? -3.490  -32.939 46.836  1.00 68.67  ?  119 LYS B CA   1 
ATOM   2565 C  C    . LYS B 1 117 ? -4.063  -34.076 45.894  1.00 71.97  ?  119 LYS B C    1 
ATOM   2566 O  O    . LYS B 1 117 ? -3.299  -34.619 45.080  1.00 72.59  ?  119 LYS B O    1 
ATOM   2567 C  CB   . LYS B 1 117 ? -3.683  -33.367 48.321  1.00 68.96  ?  119 LYS B CB   1 
ATOM   2568 C  CG   . LYS B 1 117 ? -4.906  -32.777 49.048  1.00 73.60  ?  119 LYS B CG   1 
ATOM   2569 C  CD   . LYS B 1 117 ? -4.947  -33.211 50.531  1.00 77.30  ?  119 LYS B CD   1 
ATOM   2570 C  CE   . LYS B 1 117 ? -4.698  -32.077 51.522  1.00 80.60  ?  119 LYS B CE   1 
ATOM   2571 N  NZ   . LYS B 1 117 ? -3.429  -31.318 51.255  1.00 82.26  ?  119 LYS B NZ   1 
ATOM   2572 N  N    . GLN B 1 118 ? -5.377  -34.450 46.003  1.00 73.16  ?  120 GLN B N    1 
ATOM   2573 C  CA   . GLN B 1 118 ? -5.987  -35.517 45.168  1.00 74.30  ?  120 GLN B CA   1 
ATOM   2574 C  C    . GLN B 1 118 ? -5.715  -35.213 43.671  1.00 74.57  ?  120 GLN B C    1 
ATOM   2575 O  O    . GLN B 1 118 ? -5.312  -36.104 42.908  1.00 75.30  ?  120 GLN B O    1 
ATOM   2576 C  CB   . GLN B 1 118 ? -7.525  -35.626 45.380  1.00 76.64  ?  120 GLN B CB   1 
ATOM   2577 C  CG   . GLN B 1 118 ? -8.035  -35.542 46.827  1.00 81.55  ?  120 GLN B CG   1 
ATOM   2578 C  CD   . GLN B 1 118 ? -8.884  -34.308 47.131  1.00 86.83  ?  120 GLN B CD   1 
ATOM   2579 O  OE1  . GLN B 1 118 ? -9.951  -34.406 47.759  1.00 88.35  ?  120 GLN B OE1  1 
ATOM   2580 N  NE2  . GLN B 1 118 ? -8.464  -33.116 46.709  1.00 87.98  ?  120 GLN B NE2  1 
ATOM   2581 N  N    . GLN B 1 119 ? -5.921  -33.926 43.287  1.00 73.71  ?  121 GLN B N    1 
ATOM   2582 C  CA   . GLN B 1 119 ? -5.756  -33.411 41.922  1.00 73.34  ?  121 GLN B CA   1 
ATOM   2583 C  C    . GLN B 1 119 ? -4.294  -33.413 41.406  1.00 74.01  ?  121 GLN B C    1 
ATOM   2584 O  O    . GLN B 1 119 ? -4.088  -33.146 40.226  1.00 74.33  ?  121 GLN B O    1 
ATOM   2585 C  CB   . GLN B 1 119 ? -6.384  -32.008 41.794  1.00 73.71  ?  121 GLN B CB   1 
ATOM   2586 C  CG   . GLN B 1 119 ? -7.902  -31.982 41.630  1.00 76.94  ?  121 GLN B CG   1 
ATOM   2587 C  CD   . GLN B 1 119 ? -8.628  -30.837 42.324  1.00 83.54  ?  121 GLN B CD   1 
ATOM   2588 O  OE1  . GLN B 1 119 ? -9.530  -31.045 43.153  1.00 85.94  ?  121 GLN B OE1  1 
ATOM   2589 N  NE2  . GLN B 1 119 ? -8.282  -29.603 42.003  1.00 84.32  ?  121 GLN B NE2  1 
ATOM   2590 N  N    . ARG B 1 120 ? -3.288  -33.717 42.245  1.00 74.01  ?  122 ARG B N    1 
ATOM   2591 C  CA   . ARG B 1 120 ? -1.919  -33.945 41.754  1.00 73.96  ?  122 ARG B CA   1 
ATOM   2592 C  C    . ARG B 1 120 ? -1.872  -35.241 40.935  1.00 72.79  ?  122 ARG B C    1 
ATOM   2593 O  O    . ARG B 1 120 ? -1.351  -35.276 39.814  1.00 72.45  ?  122 ARG B O    1 
ATOM   2594 C  CB   . ARG B 1 120 ? -0.929  -34.036 42.937  1.00 76.30  ?  122 ARG B CB   1 
ATOM   2595 C  CG   . ARG B 1 120 ? 0.528   -34.301 42.525  1.00 81.02  ?  122 ARG B CG   1 
ATOM   2596 C  CD   . ARG B 1 120 ? 1.453   -33.513 43.442  1.00 85.68  ?  122 ARG B CD   1 
ATOM   2597 N  NE   . ARG B 1 120 ? 2.844   -33.968 43.398  1.00 88.85  ?  122 ARG B NE   1 
ATOM   2598 C  CZ   . ARG B 1 120 ? 3.848   -33.372 44.039  1.00 89.95  ?  122 ARG B CZ   1 
ATOM   2599 N  NH1  . ARG B 1 120 ? 5.085   -33.853 43.945  1.00 88.81  ?  122 ARG B NH1  1 
ATOM   2600 N  NH2  . ARG B 1 120 ? 3.627   -32.286 44.774  1.00 89.62  ?  122 ARG B NH2  1 
ATOM   2601 N  N    . ARG B 1 121 ? -2.425  -36.313 41.506  1.00 71.67  ?  123 ARG B N    1 
ATOM   2602 C  CA   . ARG B 1 121 ? -2.373  -37.626 40.861  1.00 70.89  ?  123 ARG B CA   1 
ATOM   2603 C  C    . ARG B 1 121 ? -3.276  -37.589 39.629  1.00 68.10  ?  123 ARG B C    1 
ATOM   2604 O  O    . ARG B 1 121 ? -2.876  -37.960 38.535  1.00 68.78  ?  123 ARG B O    1 
ATOM   2605 C  CB   . ARG B 1 121 ? -2.818  -38.727 41.864  1.00 73.78  ?  123 ARG B CB   1 
ATOM   2606 C  CG   . ARG B 1 121 ? -2.085  -38.699 43.224  1.00 79.77  ?  123 ARG B CG   1 
ATOM   2607 C  CD   . ARG B 1 121 ? -0.552  -38.629 43.119  1.00 84.68  ?  123 ARG B CD   1 
ATOM   2608 N  NE   . ARG B 1 121 ? 0.093   -39.024 44.378  1.00 88.94  ?  123 ARG B NE   1 
ATOM   2609 C  CZ   . ARG B 1 121 ? 0.216   -38.255 45.460  1.00 90.52  ?  123 ARG B CZ   1 
ATOM   2610 N  NH1  . ARG B 1 121 ? -0.261  -37.014 45.463  1.00 90.09  ?  123 ARG B NH1  1 
ATOM   2611 N  NH2  . ARG B 1 121 ? 0.810   -38.724 46.549  1.00 90.27  ?  123 ARG B NH2  1 
ATOM   2612 N  N    . SER B 1 122 ? -4.483  -37.122 39.815  1.00 65.59  ?  124 SER B N    1 
ATOM   2613 C  CA   . SER B 1 122 ? -5.500  -37.145 38.778  1.00 63.80  ?  124 SER B CA   1 
ATOM   2614 C  C    . SER B 1 122 ? -5.254  -36.083 37.680  1.00 61.78  ?  124 SER B C    1 
ATOM   2615 O  O    . SER B 1 122 ? -5.235  -36.445 36.511  1.00 61.77  ?  124 SER B O    1 
ATOM   2616 C  CB   . SER B 1 122 ? -6.882  -36.981 39.399  1.00 64.20  ?  124 SER B CB   1 
ATOM   2617 O  OG   . SER B 1 122 ? -6.919  -35.836 40.234  1.00 67.49  ?  124 SER B OG   1 
ATOM   2618 N  N    . ASP B 1 123 ? -5.045  -34.800 38.049  1.00 59.47  ?  125 ASP B N    1 
ATOM   2619 C  CA   . ASP B 1 123 ? -5.200  -33.687 37.120  1.00 57.57  ?  125 ASP B CA   1 
ATOM   2620 C  C    . ASP B 1 123 ? -3.916  -32.936 36.700  1.00 53.55  ?  125 ASP B C    1 
ATOM   2621 O  O    . ASP B 1 123 ? -3.985  -32.212 35.703  1.00 51.85  ?  125 ASP B O    1 
ATOM   2622 C  CB   . ASP B 1 123 ? -6.166  -32.666 37.718  1.00 61.05  ?  125 ASP B CB   1 
ATOM   2623 C  CG   . ASP B 1 123 ? -7.608  -33.146 37.854  1.00 68.08  ?  125 ASP B CG   1 
ATOM   2624 O  OD1  . ASP B 1 123 ? -7.986  -34.094 37.144  1.00 69.24  ?  125 ASP B OD1  1 
ATOM   2625 O  OD2  . ASP B 1 123 ? -8.357  -32.556 38.664  1.00 71.01  ?  125 ASP B OD2  1 
ATOM   2626 N  N    . LEU B 1 124 ? -2.786  -33.073 37.428  1.00 50.22  ?  126 LEU B N    1 
ATOM   2627 C  CA   . LEU B 1 124 ? -1.638  -32.201 37.164  1.00 47.26  ?  126 LEU B CA   1 
ATOM   2628 C  C    . LEU B 1 124 ? -1.109  -32.364 35.720  1.00 42.34  ?  126 LEU B C    1 
ATOM   2629 O  O    . LEU B 1 124 ? -0.984  -31.365 35.010  1.00 38.59  ?  126 LEU B O    1 
ATOM   2630 C  CB   . LEU B 1 124 ? -0.504  -32.432 38.169  1.00 47.79  ?  126 LEU B CB   1 
ATOM   2631 C  CG   . LEU B 1 124 ? 0.774   -31.604 37.932  1.00 49.82  ?  126 LEU B CG   1 
ATOM   2632 C  CD1  . LEU B 1 124 ? 0.577   -30.171 38.328  1.00 49.55  ?  126 LEU B CD1  1 
ATOM   2633 C  CD2  . LEU B 1 124 ? 1.985   -32.228 38.673  1.00 51.40  ?  126 LEU B CD2  1 
ATOM   2634 N  N    . ASN B 1 125 ? -0.798  -33.583 35.307  1.00 40.46  ?  127 ASN B N    1 
ATOM   2635 C  CA   . ASN B 1 125 ? -0.223  -33.818 33.986  1.00 41.32  ?  127 ASN B CA   1 
ATOM   2636 C  C    . ASN B 1 125 ? -1.152  -33.360 32.854  1.00 37.27  ?  127 ASN B C    1 
ATOM   2637 O  O    . ASN B 1 125 ? -0.684  -32.692 31.919  1.00 36.93  ?  127 ASN B O    1 
ATOM   2638 C  CB   . ASN B 1 125 ? 0.178   -35.295 33.824  1.00 46.64  ?  127 ASN B CB   1 
ATOM   2639 C  CG   . ASN B 1 125 ? 1.235   -35.801 34.821  1.00 56.12  ?  127 ASN B CG   1 
ATOM   2640 O  OD1  . ASN B 1 125 ? 1.574   -36.978 34.816  1.00 61.24  ?  127 ASN B OD1  1 
ATOM   2641 N  ND2  . ASN B 1 125 ? 1.794   -34.970 35.705  1.00 57.30  ?  127 ASN B ND2  1 
ATOM   2642 N  N    . ARG B 1 126 ? -2.458  -33.674 32.961  1.00 34.86  ?  128 ARG B N    1 
ATOM   2643 C  CA   . ARG B 1 126 ? -3.416  -33.347 31.897  1.00 35.62  ?  128 ARG B CA   1 
ATOM   2644 C  C    . ARG B 1 126 ? -3.580  -31.796 31.846  1.00 32.38  ?  128 ARG B C    1 
ATOM   2645 O  O    . ARG B 1 126 ? -3.543  -31.206 30.744  1.00 33.02  ?  128 ARG B O    1 
ATOM   2646 C  CB   . ARG B 1 126 ? -4.825  -34.020 32.166  1.00 39.24  ?  128 ARG B CB   1 
ATOM   2647 C  CG   . ARG B 1 126 ? -5.898  -33.548 31.141  1.00 47.42  ?  128 ARG B CG   1 
ATOM   2648 C  CD   . ARG B 1 126 ? -7.158  -34.429 31.151  1.00 58.54  ?  128 ARG B CD   1 
ATOM   2649 N  NE   . ARG B 1 126 ? -8.288  -33.869 31.920  1.00 68.11  ?  128 ARG B NE   1 
ATOM   2650 C  CZ   . ARG B 1 126 ? -8.530  -34.042 33.224  1.00 73.55  ?  128 ARG B CZ   1 
ATOM   2651 N  NH1  . ARG B 1 126 ? -7.708  -34.772 33.975  1.00 75.84  ?  128 ARG B NH1  1 
ATOM   2652 N  NH2  . ARG B 1 126 ? -9.594  -33.485 33.786  1.00 72.24  ?  128 ARG B NH2  1 
ATOM   2653 N  N    . PHE B 1 127 ? -3.733  -31.129 33.021  1.00 30.01  ?  129 PHE B N    1 
ATOM   2654 C  CA   . PHE B 1 127 ? -3.889  -29.672 33.073  1.00 31.66  ?  129 PHE B CA   1 
ATOM   2655 C  C    . PHE B 1 127 ? -2.657  -28.948 32.579  1.00 30.21  ?  129 PHE B C    1 
ATOM   2656 O  O    . PHE B 1 127 ? -2.818  -27.960 31.862  1.00 29.81  ?  129 PHE B O    1 
ATOM   2657 C  CB   . PHE B 1 127 ? -4.264  -29.162 34.460  1.00 34.70  ?  129 PHE B CB   1 
ATOM   2658 C  CG   . PHE B 1 127 ? -5.705  -29.366 34.889  1.00 39.26  ?  129 PHE B CG   1 
ATOM   2659 C  CD1  . PHE B 1 127 ? -6.549  -30.216 34.189  1.00 42.46  ?  129 PHE B CD1  1 
ATOM   2660 C  CD2  . PHE B 1 127 ? -6.226  -28.670 35.965  1.00 43.66  ?  129 PHE B CD2  1 
ATOM   2661 C  CE1  . PHE B 1 127 ? -7.878  -30.401 34.591  1.00 45.92  ?  129 PHE B CE1  1 
ATOM   2662 C  CE2  . PHE B 1 127 ? -7.554  -28.844 36.353  1.00 46.47  ?  129 PHE B CE2  1 
ATOM   2663 C  CZ   . PHE B 1 127 ? -8.362  -29.741 35.681  1.00 46.40  ?  129 PHE B CZ   1 
ATOM   2664 N  N    . TRP B 1 128 ? -1.447  -29.414 32.903  1.00 29.57  ?  130 TRP B N    1 
ATOM   2665 C  CA   . TRP B 1 128 ? -0.228  -28.763 32.389  1.00 31.49  ?  130 TRP B CA   1 
ATOM   2666 C  C    . TRP B 1 128 ? -0.160  -28.850 30.882  1.00 30.43  ?  130 TRP B C    1 
ATOM   2667 O  O    . TRP B 1 128 ? 0.075   -27.844 30.210  1.00 29.77  ?  130 TRP B O    1 
ATOM   2668 C  CB   . TRP B 1 128 ? 1.025   -29.339 33.060  1.00 31.70  ?  130 TRP B CB   1 
ATOM   2669 C  CG   . TRP B 1 128 ? 2.334   -28.746 32.583  1.00 32.86  ?  130 TRP B CG   1 
ATOM   2670 C  CD1  . TRP B 1 128 ? 3.407   -29.439 32.112  1.00 35.70  ?  130 TRP B CD1  1 
ATOM   2671 C  CD2  . TRP B 1 128 ? 2.742   -27.377 32.640  1.00 32.83  ?  130 TRP B CD2  1 
ATOM   2672 N  NE1  . TRP B 1 128 ? 4.437   -28.571 31.808  1.00 37.32  ?  130 TRP B NE1  1 
ATOM   2673 C  CE2  . TRP B 1 128 ? 4.061   -27.302 32.135  1.00 35.92  ?  130 TRP B CE2  1 
ATOM   2674 C  CE3  . TRP B 1 128 ? 2.102   -26.187 32.989  1.00 33.67  ?  130 TRP B CE3  1 
ATOM   2675 C  CZ2  . TRP B 1 128 ? 4.782   -26.102 32.079  1.00 36.43  ?  130 TRP B CZ2  1 
ATOM   2676 C  CZ3  . TRP B 1 128 ? 2.814   -25.006 32.917  1.00 36.48  ?  130 TRP B CZ3  1 
ATOM   2677 C  CH2  . TRP B 1 128 ? 4.138   -24.973 32.454  1.00 36.28  ?  130 TRP B CH2  1 
ATOM   2678 N  N    . LEU B 1 129 ? -0.423  -30.056 30.332  1.00 30.56  ?  131 LEU B N    1 
ATOM   2679 C  CA   . LEU B 1 129 ? -0.345  -30.224 28.876  1.00 30.73  ?  131 LEU B CA   1 
ATOM   2680 C  C    . LEU B 1 129 ? -1.392  -29.387 28.165  1.00 29.57  ?  131 LEU B C    1 
ATOM   2681 O  O    . LEU B 1 129 ? -1.071  -28.782 27.132  1.00 30.68  ?  131 LEU B O    1 
ATOM   2682 C  CB   . LEU B 1 129 ? -0.520  -31.697 28.438  1.00 30.81  ?  131 LEU B CB   1 
ATOM   2683 C  CG   . LEU B 1 129 ? -0.552  -31.954 26.943  1.00 34.42  ?  131 LEU B CG   1 
ATOM   2684 C  CD1  . LEU B 1 129 ? 0.702   -31.479 26.246  1.00 35.69  ?  131 LEU B CD1  1 
ATOM   2685 C  CD2  . LEU B 1 129 ? -0.753  -33.436 26.672  1.00 37.12  ?  131 LEU B CD2  1 
ATOM   2686 N  N    . GLU B 1 130 ? -2.630  -29.377 28.664  1.00 29.87  ?  132 GLU B N    1 
ATOM   2687 C  CA   . GLU B 1 130 ? -3.677  -28.590 28.017  1.00 31.30  ?  132 GLU B CA   1 
ATOM   2688 C  C    . GLU B 1 130 ? -3.300  -27.074 28.015  1.00 31.04  ?  132 GLU B C    1 
ATOM   2689 O  O    . GLU B 1 130 ? -3.569  -26.389 27.025  1.00 32.39  ?  132 GLU B O    1 
ATOM   2690 C  CB   . GLU B 1 130 ? -5.060  -28.778 28.709  1.00 33.18  ?  132 GLU B CB   1 
ATOM   2691 C  CG   . GLU B 1 130 ? -5.667  -30.169 28.568  1.00 43.70  ?  132 GLU B CG   1 
ATOM   2692 C  CD   . GLU B 1 130 ? -5.832  -30.651 27.149  1.00 52.82  ?  132 GLU B CD   1 
ATOM   2693 O  OE1  . GLU B 1 130 ? -6.118  -29.820 26.258  1.00 50.09  ?  132 GLU B OE1  1 
ATOM   2694 O  OE2  . GLU B 1 130 ? -5.670  -31.872 26.929  1.00 60.99  ?  132 GLU B OE2  1 
ATOM   2695 N  N    . THR B 1 131 ? -2.676  -26.603 29.094  1.00 30.28  ?  133 THR B N    1 
ATOM   2696 C  CA   . THR B 1 131 ? -2.151  -25.235 29.195  1.00 30.89  ?  133 THR B CA   1 
ATOM   2697 C  C    . THR B 1 131 ? -1.139  -24.932 28.095  1.00 30.70  ?  133 THR B C    1 
ATOM   2698 O  O    . THR B 1 131 ? -1.304  -23.929 27.371  1.00 28.95  ?  133 THR B O    1 
ATOM   2699 C  CB   . THR B 1 131 ? -1.548  -24.994 30.606  1.00 32.26  ?  133 THR B CB   1 
ATOM   2700 O  OG1  . THR B 1 131 ? -2.569  -25.223 31.556  1.00 31.85  ?  133 THR B OG1  1 
ATOM   2701 C  CG2  . THR B 1 131 ? -1.066  -23.537 30.783  1.00 32.04  ?  133 THR B CG2  1 
ATOM   2702 N  N    . LEU B 1 132 ? -0.098  -25.814 27.971  1.00 30.27  ?  134 LEU B N    1 
ATOM   2703 C  CA   . LEU B 1 132 ? 0.954   -25.683 26.979  1.00 31.98  ?  134 LEU B CA   1 
ATOM   2704 C  C    . LEU B 1 132 ? 0.338   -25.669 25.535  1.00 32.47  ?  134 LEU B C    1 
ATOM   2705 O  O    . LEU B 1 132 ? 0.766   -24.847 24.714  1.00 31.84  ?  134 LEU B O    1 
ATOM   2706 C  CB   . LEU B 1 132 ? 2.022   -26.799 27.095  1.00 33.67  ?  134 LEU B CB   1 
ATOM   2707 C  CG   . LEU B 1 132 ? 2.779   -26.915 28.457  1.00 35.99  ?  134 LEU B CG   1 
ATOM   2708 C  CD1  . LEU B 1 132 ? 3.803   -28.039 28.443  1.00 33.96  ?  134 LEU B CD1  1 
ATOM   2709 C  CD2  . LEU B 1 132 ? 3.385   -25.595 28.892  1.00 40.54  ?  134 LEU B CD2  1 
ATOM   2710 N  N    . LEU B 1 133 ? -0.653  -26.539 25.250  1.00 31.18  ?  135 LEU B N    1 
ATOM   2711 C  CA   . LEU B 1 133 ? -1.308  -26.565 23.944  1.00 31.80  ?  135 LEU B CA   1 
ATOM   2712 C  C    . LEU B 1 133 ? -2.070  -25.277 23.606  1.00 31.56  ?  135 LEU B C    1 
ATOM   2713 O  O    . LEU B 1 133 ? -2.032  -24.854 22.432  1.00 31.68  ?  135 LEU B O    1 
ATOM   2714 C  CB   . LEU B 1 133 ? -2.212  -27.783 23.763  1.00 32.71  ?  135 LEU B CB   1 
ATOM   2715 C  CG   . LEU B 1 133 ? -1.527  -29.168 23.895  1.00 33.36  ?  135 LEU B CG   1 
ATOM   2716 C  CD1  . LEU B 1 133 ? -2.507  -30.261 23.670  1.00 32.89  ?  135 LEU B CD1  1 
ATOM   2717 C  CD2  . LEU B 1 133 ? -0.367  -29.327 22.957  1.00 35.57  ?  135 LEU B CD2  1 
ATOM   2718 N  N    . CYS B 1 134 ? -2.716  -24.648 24.592  1.00 30.97  ?  136 CYS B N    1 
ATOM   2719 C  CA   . CYS B 1 134 ? -3.335  -23.314 24.448  1.00 30.48  ?  136 CYS B CA   1 
ATOM   2720 C  C    . CYS B 1 134 ? -2.322  -22.263 24.083  1.00 29.59  ?  136 CYS B C    1 
ATOM   2721 O  O    . CYS B 1 134 ? -2.614  -21.407 23.253  1.00 30.69  ?  136 CYS B O    1 
ATOM   2722 C  CB   . CYS B 1 134 ? -4.065  -22.897 25.720  1.00 32.00  ?  136 CYS B CB   1 
ATOM   2723 S  SG   . CYS B 1 134 ? -5.584  -23.787 26.019  1.00 36.26  ?  136 CYS B SG   1 
ATOM   2724 N  N    . LEU B 1 135 ? -1.132  -22.303 24.702  1.00 29.27  ?  137 LEU B N    1 
ATOM   2725 C  CA   . LEU B 1 135 ? -0.056  -21.326 24.408  1.00 30.02  ?  137 LEU B CA   1 
ATOM   2726 C  C    . LEU B 1 135 ? 0.463   -21.539 22.995  1.00 30.49  ?  137 LEU B C    1 
ATOM   2727 O  O    . LEU B 1 135 ? 0.348   -20.641 22.161  1.00 30.59  ?  137 LEU B O    1 
ATOM   2728 C  CB   . LEU B 1 135 ? 1.096   -21.444 25.450  1.00 29.63  ?  137 LEU B CB   1 
ATOM   2729 C  CG   . LEU B 1 135 ? 0.995   -20.552 26.704  1.00 30.46  ?  137 LEU B CG   1 
ATOM   2730 C  CD1  . LEU B 1 135 ? -0.365  -20.649 27.338  1.00 29.89  ?  137 LEU B CD1  1 
ATOM   2731 C  CD2  . LEU B 1 135 ? 2.116   -20.936 27.643  1.00 33.73  ?  137 LEU B CD2  1 
ATOM   2732 N  N    . ILE B 1 136 ? 1.002   -22.711 22.721  1.00 29.07  ?  138 ILE B N    1 
ATOM   2733 C  CA   . ILE B 1 136 ? 1.741   -22.905 21.467  1.00 29.76  ?  138 ILE B CA   1 
ATOM   2734 C  C    . ILE B 1 136 ? 0.791   -22.868 20.245  1.00 29.34  ?  138 ILE B C    1 
ATOM   2735 O  O    . ILE B 1 136 ? 1.214   -22.452 19.178  1.00 29.98  ?  138 ILE B O    1 
ATOM   2736 C  CB   . ILE B 1 136 ? 2.646   -24.164 21.462  1.00 31.25  ?  138 ILE B CB   1 
ATOM   2737 C  CG1  . ILE B 1 136 ? 1.810   -25.463 21.327  1.00 30.09  ?  138 ILE B CG1  1 
ATOM   2738 C  CG2  . ILE B 1 136 ? 3.605   -24.191 22.655  1.00 32.67  ?  138 ILE B CG2  1 
ATOM   2739 C  CD1  . ILE B 1 136 ? 2.653   -26.738 21.212  1.00 31.23  ?  138 ILE B CD1  1 
ATOM   2740 N  N    . GLY B 1 137 ? -0.449  -23.282 20.426  1.00 28.35  ?  139 GLY B N    1 
ATOM   2741 C  CA   . GLY B 1 137 ? -1.439  -23.300 19.368  1.00 30.46  ?  139 GLY B CA   1 
ATOM   2742 C  C    . GLY B 1 137 ? -2.153  -21.979 19.159  1.00 30.94  ?  139 GLY B C    1 
ATOM   2743 O  O    . GLY B 1 137 ? -2.976  -21.903 18.248  1.00 32.61  ?  139 GLY B O    1 
ATOM   2744 N  N    . GLU B 1 138 ? -1.849  -20.934 19.968  1.00 30.24  ?  140 GLU B N    1 
ATOM   2745 C  CA   . GLU B 1 138 ? -2.445  -19.591 19.810  1.00 31.56  ?  140 GLU B CA   1 
ATOM   2746 C  C    . GLU B 1 138 ? -3.973  -19.644 19.885  1.00 33.10  ?  140 GLU B C    1 
ATOM   2747 O  O    . GLU B 1 138 ? -4.673  -19.132 19.014  1.00 32.60  ?  140 GLU B O    1 
ATOM   2748 C  CB   . GLU B 1 138 ? -1.980  -18.941 18.494  1.00 32.42  ?  140 GLU B CB   1 
ATOM   2749 C  CG   . GLU B 1 138 ? -0.467  -18.830 18.378  1.00 35.24  ?  140 GLU B CG   1 
ATOM   2750 C  CD   . GLU B 1 138 ? 0.173   -17.743 19.230  1.00 39.90  ?  140 GLU B CD   1 
ATOM   2751 O  OE1  . GLU B 1 138 ? -0.384  -16.626 19.320  1.00 44.93  ?  140 GLU B OE1  1 
ATOM   2752 O  OE2  . GLU B 1 138 ? 1.268   -17.991 19.776  1.00 41.56  ?  140 GLU B OE2  1 
ATOM   2753 N  N    . SER B 1 139 ? -4.469  -20.294 20.950  1.00 33.04  ?  141 SER B N    1 
ATOM   2754 C  CA   . SER B 1 139 ? -5.875  -20.647 21.120  1.00 34.65  ?  141 SER B CA   1 
ATOM   2755 C  C    . SER B 1 139 ? -6.776  -19.503 21.519  1.00 36.21  ?  141 SER B C    1 
ATOM   2756 O  O    . SER B 1 139 ? -7.989  -19.717 21.635  1.00 37.83  ?  141 SER B O    1 
ATOM   2757 C  CB   . SER B 1 139 ? -6.024  -21.736 22.185  1.00 36.10  ?  141 SER B CB   1 
ATOM   2758 O  OG   . SER B 1 139 ? -5.230  -22.845 21.835  1.00 39.40  ?  141 SER B OG   1 
ATOM   2759 N  N    . PHE B 1 140 ? -6.238  -18.300 21.744  1.00 35.65  ?  142 PHE B N    1 
ATOM   2760 C  CA   . PHE B 1 140 ? -7.015  -17.202 22.253  1.00 36.27  ?  142 PHE B CA   1 
ATOM   2761 C  C    . PHE B 1 140 ? -7.220  -16.121 21.166  1.00 38.59  ?  142 PHE B C    1 
ATOM   2762 O  O    . PHE B 1 140 ? -7.513  -14.996 21.499  1.00 39.04  ?  142 PHE B O    1 
ATOM   2763 C  CB   . PHE B 1 140 ? -6.309  -16.652 23.473  1.00 35.80  ?  142 PHE B CB   1 
ATOM   2764 C  CG   . PHE B 1 140 ? -5.990  -17.683 24.551  1.00 35.62  ?  142 PHE B CG   1 
ATOM   2765 C  CD1  . PHE B 1 140 ? -7.004  -18.375 25.203  1.00 35.67  ?  142 PHE B CD1  1 
ATOM   2766 C  CD2  . PHE B 1 140 ? -4.678  -17.952 24.917  1.00 35.33  ?  142 PHE B CD2  1 
ATOM   2767 C  CE1  . PHE B 1 140 ? -6.699  -19.314 26.184  1.00 36.49  ?  142 PHE B CE1  1 
ATOM   2768 C  CE2  . PHE B 1 140 ? -4.392  -18.867 25.918  1.00 35.61  ?  142 PHE B CE2  1 
ATOM   2769 C  CZ   . PHE B 1 140 ? -5.404  -19.524 26.555  1.00 35.74  ?  142 PHE B CZ   1 
ATOM   2770 N  N    . ASP B 1 141 ? -7.095  -16.454 19.886  1.00 41.00  ?  143 ASP B N    1 
ATOM   2771 C  CA   . ASP B 1 141 ? -7.296  -15.515 18.789  1.00 43.58  ?  143 ASP B CA   1 
ATOM   2772 C  C    . ASP B 1 141 ? -6.270  -14.327 18.907  1.00 43.40  ?  143 ASP B C    1 
ATOM   2773 O  O    . ASP B 1 141 ? -5.132  -14.565 19.280  1.00 43.38  ?  143 ASP B O    1 
ATOM   2774 C  CB   . ASP B 1 141 ? -8.812  -15.112 18.722  1.00 49.28  ?  143 ASP B CB   1 
ATOM   2775 C  CG   . ASP B 1 141 ? -9.682  -16.314 18.411  1.00 60.82  ?  143 ASP B CG   1 
ATOM   2776 O  OD1  . ASP B 1 141 ? -9.460  -16.958 17.350  1.00 62.38  ?  143 ASP B OD1  1 
ATOM   2777 O  OD2  . ASP B 1 141 ? -10.571 -16.624 19.227  1.00 65.90  ?  143 ASP B OD2  1 
ATOM   2778 N  N    . ASP B 1 142 ? -6.639  -13.108 18.602  1.00 44.02  ?  144 ASP B N    1 
ATOM   2779 C  CA   . ASP B 1 142 ? -5.725  -11.966 18.653  1.00 43.89  ?  144 ASP B CA   1 
ATOM   2780 C  C    . ASP B 1 142 ? -5.279  -11.729 20.106  1.00 40.32  ?  144 ASP B C    1 
ATOM   2781 O  O    . ASP B 1 142 ? -4.159  -11.271 20.298  1.00 39.87  ?  144 ASP B O    1 
ATOM   2782 C  CB   . ASP B 1 142 ? -6.389  -10.716 18.080  1.00 49.30  ?  144 ASP B CB   1 
ATOM   2783 C  CG   . ASP B 1 142 ? -6.489  -10.710 16.549  1.00 62.38  ?  144 ASP B CG   1 
ATOM   2784 O  OD1  . ASP B 1 142 ? -5.778  -11.525 15.893  1.00 64.71  ?  144 ASP B OD1  1 
ATOM   2785 O  OD2  . ASP B 1 142 ? -7.268  -9.882  16.004  1.00 68.03  ?  144 ASP B OD2  1 
ATOM   2786 N  N    . TYR B 1 143 ? -6.133  -12.070 21.116  1.00 38.01  ?  145 TYR B N    1 
ATOM   2787 C  CA   . TYR B 1 143 ? -5.757  -11.966 22.516  1.00 37.55  ?  145 TYR B CA   1 
ATOM   2788 C  C    . TYR B 1 143 ? -4.606  -12.894 22.927  1.00 34.70  ?  145 TYR B C    1 
ATOM   2789 O  O    . TYR B 1 143 ? -4.076  -12.757 24.022  1.00 34.54  ?  145 TYR B O    1 
ATOM   2790 C  CB   . TYR B 1 143 ? -6.970  -12.204 23.410  1.00 40.00  ?  145 TYR B CB   1 
ATOM   2791 C  CG   . TYR B 1 143 ? -8.073  -11.210 23.137  1.00 43.25  ?  145 TYR B CG   1 
ATOM   2792 C  CD1  . TYR B 1 143 ? -7.808  -9.852  23.070  1.00 44.98  ?  145 TYR B CD1  1 
ATOM   2793 C  CD2  . TYR B 1 143 ? -9.364  -11.634 22.865  1.00 46.48  ?  145 TYR B CD2  1 
ATOM   2794 C  CE1  . TYR B 1 143 ? -8.815  -8.932  22.840  1.00 48.14  ?  145 TYR B CE1  1 
ATOM   2795 C  CE2  . TYR B 1 143 ? -10.380 -10.717 22.595  1.00 48.91  ?  145 TYR B CE2  1 
ATOM   2796 C  CZ   . TYR B 1 143 ? -10.099 -9.366  22.588  1.00 51.22  ?  145 TYR B CZ   1 
ATOM   2797 O  OH   . TYR B 1 143 ? -11.081 -8.445  22.315  1.00 56.25  ?  145 TYR B OH   1 
ATOM   2798 N  N    . SER B 1 144 ? -4.220  -13.805 22.071  1.00 33.85  ?  146 SER B N    1 
ATOM   2799 C  CA   . SER B 1 144 ? -3.022  -14.632 22.280  1.00 34.25  ?  146 SER B CA   1 
ATOM   2800 C  C    . SER B 1 144 ? -1.749  -13.782 22.405  1.00 33.64  ?  146 SER B C    1 
ATOM   2801 O  O    . SER B 1 144 ? -0.799  -14.193 23.101  1.00 33.35  ?  146 SER B O    1 
ATOM   2802 C  CB   . SER B 1 144 ? -2.878  -15.641 21.130  1.00 35.55  ?  146 SER B CB   1 
ATOM   2803 O  OG   . SER B 1 144 ? -3.621  -16.794 21.468  1.00 35.33  ?  146 SER B OG   1 
ATOM   2804 N  N    . ASP B 1 145 ? -1.741  -12.612 21.771  1.00 31.78  ?  147 ASP B N    1 
ATOM   2805 C  CA   . ASP B 1 145 ? -0.654  -11.655 21.903  1.00 33.27  ?  147 ASP B CA   1 
ATOM   2806 C  C    . ASP B 1 145 ? -0.498  -11.152 23.337  1.00 33.54  ?  147 ASP B C    1 
ATOM   2807 O  O    . ASP B 1 145 ? 0.608   -10.763 23.664  1.00 35.15  ?  147 ASP B O    1 
ATOM   2808 C  CB   . ASP B 1 145 ? -0.818  -10.468 20.929  1.00 35.85  ?  147 ASP B CB   1 
ATOM   2809 C  CG   . ASP B 1 145 ? -0.665  -10.915 19.479  1.00 47.15  ?  147 ASP B CG   1 
ATOM   2810 O  OD1  . ASP B 1 145 ? 0.045   -11.943 19.229  1.00 46.89  ?  147 ASP B OD1  1 
ATOM   2811 O  OD2  . ASP B 1 145 ? -1.255  -10.252 18.591  1.00 52.99  ?  147 ASP B OD2  1 
ATOM   2812 N  N    . ASP B 1 146 ? -1.558  -11.172 24.161  1.00 32.14  ?  148 ASP B N    1 
ATOM   2813 C  CA   . ASP B 1 146 ? -1.460  -10.755 25.570  1.00 32.19  ?  148 ASP B CA   1 
ATOM   2814 C  C    . ASP B 1 146 ? -0.757  -11.808 26.427  1.00 30.31  ?  148 ASP B C    1 
ATOM   2815 O  O    . ASP B 1 146 ? -0.335  -11.486 27.520  1.00 29.70  ?  148 ASP B O    1 
ATOM   2816 C  CB   . ASP B 1 146 ? -2.845  -10.344 26.187  1.00 34.07  ?  148 ASP B CB   1 
ATOM   2817 C  CG   . ASP B 1 146 ? -3.135  -8.846  26.018  1.00 41.01  ?  148 ASP B CG   1 
ATOM   2818 O  OD1  . ASP B 1 146 ? -2.964  -8.362  24.909  1.00 43.30  ?  148 ASP B OD1  1 
ATOM   2819 O  OD2  . ASP B 1 146 ? -3.505  -8.146  27.057  1.00 38.51  ?  148 ASP B OD2  1 
ATOM   2820 N  N    . VAL B 1 147 ? -0.605  -13.065 25.932  1.00 29.47  ?  149 VAL B N    1 
ATOM   2821 C  CA   . VAL B 1 147 ? -0.055  -14.169 26.716  1.00 29.78  ?  149 VAL B CA   1 
ATOM   2822 C  C    . VAL B 1 147 ? 1.458   -14.016 26.758  1.00 28.76  ?  149 VAL B C    1 
ATOM   2823 O  O    . VAL B 1 147 ? 2.123   -13.751 25.711  1.00 28.54  ?  149 VAL B O    1 
ATOM   2824 C  CB   . VAL B 1 147 ? -0.510  -15.533 26.150  1.00 31.79  ?  149 VAL B CB   1 
ATOM   2825 C  CG1  . VAL B 1 147 ? 0.269   -16.722 26.797  1.00 32.73  ?  149 VAL B CG1  1 
ATOM   2826 C  CG2  . VAL B 1 147 ? -2.029  -15.705 26.363  1.00 32.10  ?  149 VAL B CG2  1 
ATOM   2827 N  N    . CYS B 1 148 ? 2.006   -14.149 27.961  1.00 25.76  ?  150 CYS B N    1 
ATOM   2828 C  CA   . CYS B 1 148 ? 3.436   -14.177 28.158  1.00 27.39  ?  150 CYS B CA   1 
ATOM   2829 C  C    . CYS B 1 148 ? 3.980   -15.589 28.246  1.00 28.20  ?  150 CYS B C    1 
ATOM   2830 O  O    . CYS B 1 148 ? 4.997   -15.909 27.639  1.00 29.56  ?  150 CYS B O    1 
ATOM   2831 C  CB   . CYS B 1 148 ? 3.809   -13.353 29.382  1.00 27.93  ?  150 CYS B CB   1 
ATOM   2832 S  SG   . CYS B 1 148 ? 3.374   -11.593 29.219  1.00 34.10  ?  150 CYS B SG   1 
ATOM   2833 N  N    . GLY B 1 149 ? 3.291   -16.415 29.013  1.00 27.68  ?  151 GLY B N    1 
ATOM   2834 C  CA   . GLY B 1 149 ? 3.706   -17.761 29.310  1.00 28.23  ?  151 GLY B CA   1 
ATOM   2835 C  C    . GLY B 1 149 ? 2.851   -18.442 30.347  1.00 28.76  ?  151 GLY B C    1 
ATOM   2836 O  O    . GLY B 1 149 ? 1.804   -17.914 30.742  1.00 30.07  ?  151 GLY B O    1 
ATOM   2837 N  N    . ALA B 1 150 ? 3.288   -19.627 30.782  1.00 28.18  ?  152 ALA B N    1 
ATOM   2838 C  CA   . ALA B 1 150 ? 2.622   -20.420 31.820  1.00 27.78  ?  152 ALA B CA   1 
ATOM   2839 C  C    . ALA B 1 150 ? 3.647   -20.982 32.790  1.00 29.30  ?  152 ALA B C    1 
ATOM   2840 O  O    . ALA B 1 150 ? 4.809   -21.187 32.436  1.00 30.44  ?  152 ALA B O    1 
ATOM   2841 C  CB   . ALA B 1 150 ? 1.792   -21.537 31.211  1.00 27.13  ?  152 ALA B CB   1 
ATOM   2842 N  N    . VAL B 1 151 ? 3.208   -21.222 34.010  1.00 29.11  ?  153 VAL B N    1 
ATOM   2843 C  CA   . VAL B 1 151 ? 4.054   -21.665 35.116  1.00 30.24  ?  153 VAL B CA   1 
ATOM   2844 C  C    . VAL B 1 151 ? 3.325   -22.825 35.842  1.00 31.23  ?  153 VAL B C    1 
ATOM   2845 O  O    . VAL B 1 151 ? 2.120   -22.757 36.071  1.00 32.29  ?  153 VAL B O    1 
ATOM   2846 C  CB   . VAL B 1 151 ? 4.388   -20.509 36.117  1.00 30.92  ?  153 VAL B CB   1 
ATOM   2847 C  CG1  . VAL B 1 151 ? 5.238   -21.032 37.299  1.00 30.65  ?  153 VAL B CG1  1 
ATOM   2848 C  CG2  . VAL B 1 151 ? 5.062   -19.314 35.396  1.00 31.43  ?  153 VAL B CG2  1 
ATOM   2849 N  N    . VAL B 1 152 ? 4.059   -23.876 36.152  1.00 31.51  ?  154 VAL B N    1 
ATOM   2850 C  CA   . VAL B 1 152 ? 3.611   -24.940 37.042  1.00 33.65  ?  154 VAL B CA   1 
ATOM   2851 C  C    . VAL B 1 152 ? 4.529   -24.978 38.270  1.00 35.19  ?  154 VAL B C    1 
ATOM   2852 O  O    . VAL B 1 152 ? 5.738   -25.088 38.141  1.00 35.10  ?  154 VAL B O    1 
ATOM   2853 C  CB   . VAL B 1 152 ? 3.467   -26.316 36.347  1.00 35.25  ?  154 VAL B CB   1 
ATOM   2854 C  CG1  . VAL B 1 152 ? 4.751   -26.776 35.648  1.00 35.36  ?  154 VAL B CG1  1 
ATOM   2855 C  CG2  . VAL B 1 152 ? 2.923   -27.394 37.303  1.00 36.23  ?  154 VAL B CG2  1 
ATOM   2856 N  N    . ASN B 1 153 ? 3.949   -24.851 39.451  1.00 35.03  ?  155 ASN B N    1 
ATOM   2857 C  CA   . ASN B 1 153 ? 4.639   -24.953 40.745  1.00 37.03  ?  155 ASN B CA   1 
ATOM   2858 C  C    . ASN B 1 153 ? 4.179   -26.263 41.413  1.00 38.87  ?  155 ASN B C    1 
ATOM   2859 O  O    . ASN B 1 153 ? 3.001   -26.425 41.694  1.00 37.57  ?  155 ASN B O    1 
ATOM   2860 C  CB   . ASN B 1 153 ? 4.274   -23.797 41.648  1.00 37.99  ?  155 ASN B CB   1 
ATOM   2861 C  CG   . ASN B 1 153 ? 4.438   -22.435 41.022  1.00 38.76  ?  155 ASN B CG   1 
ATOM   2862 O  OD1  . ASN B 1 153 ? 3.482   -21.704 40.768  1.00 40.51  ?  155 ASN B OD1  1 
ATOM   2863 N  ND2  . ASN B 1 153 ? 5.661   -22.066 40.777  1.00 37.52  ?  155 ASN B ND2  1 
ATOM   2864 N  N    . VAL B 1 154 ? 5.106   -27.188 41.599  1.00 40.94  ?  156 VAL B N    1 
ATOM   2865 C  CA   . VAL B 1 154 ? 4.830   -28.494 42.166  1.00 44.26  ?  156 VAL B CA   1 
ATOM   2866 C  C    . VAL B 1 154 ? 5.158   -28.383 43.655  1.00 47.08  ?  156 VAL B C    1 
ATOM   2867 O  O    . VAL B 1 154 ? 6.323   -28.155 43.989  1.00 47.27  ?  156 VAL B O    1 
ATOM   2868 C  CB   . VAL B 1 154 ? 5.671   -29.567 41.462  1.00 46.52  ?  156 VAL B CB   1 
ATOM   2869 C  CG1  . VAL B 1 154 ? 5.506   -30.927 42.138  1.00 48.15  ?  156 VAL B CG1  1 
ATOM   2870 C  CG2  . VAL B 1 154 ? 5.337   -29.630 39.970  1.00 47.27  ?  156 VAL B CG2  1 
ATOM   2871 N  N    . ARG B 1 155 ? 4.149   -28.517 44.526  1.00 49.45  ?  157 ARG B N    1 
ATOM   2872 C  CA   . ARG B 1 155 ? 4.339   -28.363 45.983  1.00 53.04  ?  157 ARG B CA   1 
ATOM   2873 C  C    . ARG B 1 155 ? 3.692   -29.472 46.781  1.00 56.38  ?  157 ARG B C    1 
ATOM   2874 O  O    . ARG B 1 155 ? 2.775   -30.156 46.313  1.00 55.40  ?  157 ARG B O    1 
ATOM   2875 C  CB   . ARG B 1 155 ? 3.771   -27.035 46.486  1.00 54.14  ?  157 ARG B CB   1 
ATOM   2876 C  CG   . ARG B 1 155 ? 4.407   -25.811 45.927  1.00 56.48  ?  157 ARG B CG   1 
ATOM   2877 C  CD   . ARG B 1 155 ? 5.802   -25.570 46.445  1.00 59.72  ?  157 ARG B CD   1 
ATOM   2878 N  NE   . ARG B 1 155 ? 6.379   -24.365 45.837  1.00 62.04  ?  157 ARG B NE   1 
ATOM   2879 C  CZ   . ARG B 1 155 ? 6.949   -24.308 44.627  1.00 59.71  ?  157 ARG B CZ   1 
ATOM   2880 N  NH1  . ARG B 1 155 ? 7.032   -25.395 43.871  1.00 58.18  ?  157 ARG B NH1  1 
ATOM   2881 N  NH2  . ARG B 1 155 ? 7.439   -23.169 44.175  1.00 55.49  ?  157 ARG B NH2  1 
ATOM   2882 N  N    . ALA B 1 156 ? 4.186   -29.641 48.017  1.00 59.25  ?  158 ALA B N    1 
ATOM   2883 C  CA   . ALA B 1 156 ? 3.653   -30.606 48.979  1.00 61.33  ?  158 ALA B CA   1 
ATOM   2884 C  C    . ALA B 1 156 ? 2.160   -30.344 49.266  1.00 62.27  ?  158 ALA B C    1 
ATOM   2885 O  O    . ALA B 1 156 ? 1.361   -31.259 49.139  1.00 63.59  ?  158 ALA B O    1 
ATOM   2886 C  CB   . ALA B 1 156 ? 4.483   -30.552 50.273  1.00 61.90  ?  158 ALA B CB   1 
ATOM   2887 N  N    . LYS B 1 157 ? 1.794   -29.098 49.616  1.00 62.16  ?  159 LYS B N    1 
ATOM   2888 C  CA   . LYS B 1 157 ? 0.444   -28.686 50.013  1.00 62.32  ?  159 LYS B CA   1 
ATOM   2889 C  C    . LYS B 1 157 ? -0.557  -28.692 48.841  1.00 60.29  ?  159 LYS B C    1 
ATOM   2890 O  O    . LYS B 1 157 ? -1.752  -28.872 49.064  1.00 61.42  ?  159 LYS B O    1 
ATOM   2891 C  CB   . LYS B 1 157 ? 0.509   -27.258 50.615  1.00 65.79  ?  159 LYS B CB   1 
ATOM   2892 C  CG   . LYS B 1 157 ? -0.787  -26.778 51.272  1.00 72.36  ?  159 LYS B CG   1 
ATOM   2893 C  CD   . LYS B 1 157 ? -0.547  -25.524 52.139  1.00 78.41  ?  159 LYS B CD   1 
ATOM   2894 C  CE   . LYS B 1 157 ? -1.687  -25.201 53.081  1.00 82.93  ?  159 LYS B CE   1 
ATOM   2895 N  NZ   . LYS B 1 157 ? -1.275  -24.254 54.158  1.00 85.23  ?  159 LYS B NZ   1 
ATOM   2896 N  N    . GLY B 1 158 ? -0.072  -28.479 47.619  1.00 56.40  ?  160 GLY B N    1 
ATOM   2897 C  CA   . GLY B 1 158 ? -0.909  -28.514 46.430  1.00 53.15  ?  160 GLY B CA   1 
ATOM   2898 C  C    . GLY B 1 158 ? -0.315  -27.710 45.271  1.00 49.91  ?  160 GLY B C    1 
ATOM   2899 O  O    . GLY B 1 158 ? 0.277   -26.652 45.475  1.00 50.59  ?  160 GLY B O    1 
ATOM   2900 N  N    . ASP B 1 159 ? -0.506  -28.205 44.058  1.00 46.39  ?  161 ASP B N    1 
ATOM   2901 C  CA   . ASP B 1 159 ? 0.139   -27.690 42.845  1.00 43.04  ?  161 ASP B CA   1 
ATOM   2902 C  C    . ASP B 1 159 ? -0.588  -26.447 42.329  1.00 40.53  ?  161 ASP B C    1 
ATOM   2903 O  O    . ASP B 1 159 ? -1.767  -26.224 42.618  1.00 41.09  ?  161 ASP B O    1 
ATOM   2904 C  CB   . ASP B 1 159 ? 0.203   -28.789 41.769  1.00 45.99  ?  161 ASP B CB   1 
ATOM   2905 C  CG   . ASP B 1 159 ? 0.770   -30.094 42.264  1.00 53.91  ?  161 ASP B CG   1 
ATOM   2906 O  OD1  . ASP B 1 159 ? 1.912   -30.094 42.764  1.00 57.42  ?  161 ASP B OD1  1 
ATOM   2907 O  OD2  . ASP B 1 159 ? 0.079   -31.101 42.151  1.00 56.74  ?  161 ASP B OD2  1 
ATOM   2908 N  N    . LYS B 1 160 ? 0.126   -25.610 41.569  1.00 37.60  ?  162 LYS B N    1 
ATOM   2909 C  CA   . LYS B 1 160 ? -0.474  -24.441 40.950  1.00 35.53  ?  162 LYS B CA   1 
ATOM   2910 C  C    . LYS B 1 160 ? -0.085  -24.428 39.461  1.00 34.51  ?  162 LYS B C    1 
ATOM   2911 O  O    . LYS B 1 160 ? 1.070   -24.704 39.145  1.00 34.30  ?  162 LYS B O    1 
ATOM   2912 C  CB   . LYS B 1 160 ? 0.026   -23.152 41.613  1.00 38.48  ?  162 LYS B CB   1 
ATOM   2913 C  CG   . LYS B 1 160 ? -0.432  -22.958 43.044  1.00 46.82  ?  162 LYS B CG   1 
ATOM   2914 C  CD   . LYS B 1 160 ? -0.014  -21.592 43.588  1.00 57.77  ?  162 LYS B CD   1 
ATOM   2915 C  CE   . LYS B 1 160 ? 1.254   -21.663 44.402  1.00 66.15  ?  162 LYS B CE   1 
ATOM   2916 N  NZ   . LYS B 1 160 ? 1.681   -20.296 44.884  1.00 71.21  ?  162 LYS B NZ   1 
ATOM   2917 N  N    . ILE B 1 161 ? -1.049  -24.142 38.585  1.00 32.52  ?  163 ILE B N    1 
ATOM   2918 C  CA   . ILE B 1 161 ? -0.791  -23.886 37.152  1.00 32.84  ?  163 ILE B CA   1 
ATOM   2919 C  C    . ILE B 1 161 ? -1.378  -22.525 36.861  1.00 31.81  ?  163 ILE B C    1 
ATOM   2920 O  O    . ILE B 1 161 ? -2.469  -22.186 37.342  1.00 32.04  ?  163 ILE B O    1 
ATOM   2921 C  CB   . ILE B 1 161 ? -1.415  -24.982 36.268  1.00 33.15  ?  163 ILE B CB   1 
ATOM   2922 C  CG1  . ILE B 1 161 ? -0.777  -26.367 36.593  1.00 33.68  ?  163 ILE B CG1  1 
ATOM   2923 C  CG2  . ILE B 1 161 ? -1.260  -24.649 34.768  1.00 35.05  ?  163 ILE B CG2  1 
ATOM   2924 C  CD1  . ILE B 1 161 ? -1.506  -27.453 36.004  1.00 36.40  ?  163 ILE B CD1  1 
ATOM   2925 N  N    . ALA B 1 162 ? -0.668  -21.724 36.057  1.00 30.45  ?  164 ALA B N    1 
ATOM   2926 C  CA   . ALA B 1 162 ? -1.088  -20.373 35.749  1.00 29.92  ?  164 ALA B CA   1 
ATOM   2927 C  C    . ALA B 1 162 ? -0.721  -19.954 34.340  1.00 32.81  ?  164 ALA B C    1 
ATOM   2928 O  O    . ALA B 1 162 ? 0.367   -20.305 33.858  1.00 31.61  ?  164 ALA B O    1 
ATOM   2929 C  CB   . ALA B 1 162 ? -0.477  -19.426 36.727  1.00 28.38  ?  164 ALA B CB   1 
ATOM   2930 N  N    . ILE B 1 163 ? -1.616  -19.221 33.669  1.00 32.89  ?  165 ILE B N    1 
ATOM   2931 C  CA   . ILE B 1 163 ? -1.250  -18.513 32.458  1.00 30.73  ?  165 ILE B CA   1 
ATOM   2932 C  C    . ILE B 1 163 ? -0.981  -17.043 32.826  1.00 31.05  ?  165 ILE B C    1 
ATOM   2933 O  O    . ILE B 1 163 ? -1.841  -16.364 33.356  1.00 31.23  ?  165 ILE B O    1 
ATOM   2934 C  CB   . ILE B 1 163 ? -2.337  -18.597 31.354  1.00 28.57  ?  165 ILE B CB   1 
ATOM   2935 C  CG1  . ILE B 1 163 ? -2.465  -20.046 30.860  1.00 28.62  ?  165 ILE B CG1  1 
ATOM   2936 C  CG2  . ILE B 1 163 ? -2.028  -17.615 30.208  1.00 26.97  ?  165 ILE B CG2  1 
ATOM   2937 C  CD1  . ILE B 1 163 ? -3.485  -20.256 29.691  1.00 32.39  ?  165 ILE B CD1  1 
ATOM   2938 N  N    . TRP B 1 164 ? 0.201   -16.581 32.498  1.00 30.07  ?  166 TRP B N    1 
ATOM   2939 C  CA   . TRP B 1 164 ? 0.654   -15.183 32.691  1.00 29.83  ?  166 TRP B CA   1 
ATOM   2940 C  C    . TRP B 1 164 ? 0.335   -14.344 31.453  1.00 30.21  ?  166 TRP B C    1 
ATOM   2941 O  O    . TRP B 1 164 ? 0.571   -14.736 30.290  1.00 29.13  ?  166 TRP B O    1 
ATOM   2942 C  CB   . TRP B 1 164 ? 2.161   -15.139 32.981  1.00 29.01  ?  166 TRP B CB   1 
ATOM   2943 C  CG   . TRP B 1 164 ? 2.590   -15.622 34.326  1.00 28.95  ?  166 TRP B CG   1 
ATOM   2944 C  CD1  . TRP B 1 164 ? 2.000   -16.590 35.102  1.00 28.56  ?  166 TRP B CD1  1 
ATOM   2945 C  CD2  . TRP B 1 164 ? 3.723   -15.148 35.055  1.00 28.90  ?  166 TRP B CD2  1 
ATOM   2946 N  NE1  . TRP B 1 164 ? 2.702   -16.743 36.269  1.00 28.69  ?  166 TRP B NE1  1 
ATOM   2947 C  CE2  . TRP B 1 164 ? 3.786   -15.890 36.257  1.00 29.12  ?  166 TRP B CE2  1 
ATOM   2948 C  CE3  . TRP B 1 164 ? 4.722   -14.199 34.786  1.00 29.70  ?  166 TRP B CE3  1 
ATOM   2949 C  CZ2  . TRP B 1 164 ? 4.803   -15.671 37.213  1.00 30.66  ?  166 TRP B CZ2  1 
ATOM   2950 C  CZ3  . TRP B 1 164 ? 5.736   -14.000 35.704  1.00 32.26  ?  166 TRP B CZ3  1 
ATOM   2951 C  CH2  . TRP B 1 164 ? 5.788   -14.738 36.891  1.00 32.13  ?  166 TRP B CH2  1 
ATOM   2952 N  N    . THR B 1 165 ? -0.219  -13.166 31.705  1.00 29.59  ?  167 THR B N    1 
ATOM   2953 C  CA   . THR B 1 165 ? -0.549  -12.192 30.664  1.00 29.94  ?  167 THR B CA   1 
ATOM   2954 C  C    . THR B 1 165 ? 0.104   -10.821 30.979  1.00 30.24  ?  167 THR B C    1 
ATOM   2955 O  O    . THR B 1 165 ? 0.506   -10.532 32.122  1.00 30.99  ?  167 THR B O    1 
ATOM   2956 C  CB   . THR B 1 165 ? -2.092  -12.113 30.379  1.00 31.31  ?  167 THR B CB   1 
ATOM   2957 O  OG1  . THR B 1 165 ? -2.690  -11.173 31.290  1.00 31.53  ?  167 THR B OG1  1 
ATOM   2958 C  CG2  . THR B 1 165 ? -2.805  -13.470 30.467  1.00 32.49  ?  167 THR B CG2  1 
ATOM   2959 N  N    . THR B 1 166 ? 0.227   -10.016 29.936  1.00 30.71  ?  168 THR B N    1 
ATOM   2960 C  CA   . THR B 1 166 ? 1.103   -8.866  29.928  1.00 32.83  ?  168 THR B CA   1 
ATOM   2961 C  C    . THR B 1 166 ? 0.459   -7.602  30.575  1.00 34.06  ?  168 THR B C    1 
ATOM   2962 O  O    . THR B 1 166 ? 1.203   -6.731  31.025  1.00 35.31  ?  168 THR B O    1 
ATOM   2963 C  CB   . THR B 1 166 ? 1.575   -8.566  28.484  1.00 34.82  ?  168 THR B CB   1 
ATOM   2964 O  OG1  . THR B 1 166 ? 2.675   -7.655  28.550  1.00 36.36  ?  168 THR B OG1  1 
ATOM   2965 C  CG2  . THR B 1 166 ? 0.447   -7.967  27.582  1.00 34.22  ?  168 THR B CG2  1 
ATOM   2966 N  N    . GLU B 1 167 ? -0.887  -7.500  30.608  1.00 34.44  ?  169 GLU B N    1 
ATOM   2967 C  CA   . GLU B 1 167 ? -1.536  -6.234  31.014  1.00 35.58  ?  169 GLU B CA   1 
ATOM   2968 C  C    . GLU B 1 167 ? -2.832  -6.503  31.803  1.00 34.06  ?  169 GLU B C    1 
ATOM   2969 O  O    . GLU B 1 167 ? -3.865  -6.898  31.229  1.00 33.38  ?  169 GLU B O    1 
ATOM   2970 C  CB   . GLU B 1 167 ? -1.820  -5.377  29.786  1.00 39.69  ?  169 GLU B CB   1 
ATOM   2971 C  CG   . GLU B 1 167 ? -2.516  -4.054  30.107  1.00 47.37  ?  169 GLU B CG   1 
ATOM   2972 C  CD   . GLU B 1 167 ? -1.897  -3.281  31.254  1.00 49.47  ?  169 GLU B CD   1 
ATOM   2973 O  OE1  . GLU B 1 167 ? -0.776  -2.746  31.085  1.00 49.32  ?  169 GLU B OE1  1 
ATOM   2974 O  OE2  . GLU B 1 167 ? -2.527  -3.253  32.334  1.00 42.56  ?  169 GLU B OE2  1 
ATOM   2975 N  N    . CYS B 1 168 ? -2.754  -6.291  33.105  1.00 34.34  ?  170 CYS B N    1 
ATOM   2976 C  CA   . CYS B 1 168 ? -3.864  -6.663  33.978  1.00 37.55  ?  170 CYS B CA   1 
ATOM   2977 C  C    . CYS B 1 168 ? -5.104  -5.755  33.785  1.00 39.69  ?  170 CYS B C    1 
ATOM   2978 O  O    . CYS B 1 168 ? -6.177  -6.167  34.200  1.00 40.49  ?  170 CYS B O    1 
ATOM   2979 C  CB   . CYS B 1 168 ? -3.431  -6.771  35.448  1.00 39.57  ?  170 CYS B CB   1 
ATOM   2980 S  SG   . CYS B 1 168 ? -2.831  -5.229  36.207  1.00 50.29  ?  170 CYS B SG   1 
ATOM   2981 N  N    . GLU B 1 169 ? -4.978  -4.554  33.165  1.00 38.89  ?  171 GLU B N    1 
ATOM   2982 C  CA   . GLU B 1 169 ? -6.124  -3.682  32.873  1.00 39.84  ?  171 GLU B CA   1 
ATOM   2983 C  C    . GLU B 1 169 ? -6.808  -3.961  31.542  1.00 41.45  ?  171 GLU B C    1 
ATOM   2984 O  O    . GLU B 1 169 ? -7.855  -3.370  31.300  1.00 41.97  ?  171 GLU B O    1 
ATOM   2985 C  CB   . GLU B 1 169 ? -5.706  -2.200  32.932  1.00 39.95  ?  171 GLU B CB   1 
ATOM   2986 C  CG   . GLU B 1 169 ? -5.202  -1.795  34.271  1.00 41.79  ?  171 GLU B CG   1 
ATOM   2987 C  CD   . GLU B 1 169 ? -6.197  -1.991  35.431  1.00 51.72  ?  171 GLU B CD   1 
ATOM   2988 O  OE1  . GLU B 1 169 ? -7.447  -1.999  35.241  1.00 49.43  ?  171 GLU B OE1  1 
ATOM   2989 O  OE2  . GLU B 1 169 ? -5.691  -2.130  36.564  1.00 48.25  ?  171 GLU B OE2  1 
ATOM   2990 N  N    . ASN B 1 170 ? -6.259  -4.838  30.688  1.00 42.09  ?  172 ASN B N    1 
ATOM   2991 C  CA   . ASN B 1 170 ? -6.923  -5.239  29.442  1.00 41.65  ?  172 ASN B CA   1 
ATOM   2992 C  C    . ASN B 1 170 ? -8.017  -6.265  29.787  1.00 40.31  ?  172 ASN B C    1 
ATOM   2993 O  O    . ASN B 1 170 ? -7.829  -7.472  29.574  1.00 38.90  ?  172 ASN B O    1 
ATOM   2994 C  CB   . ASN B 1 170 ? -5.917  -5.859  28.452  1.00 44.12  ?  172 ASN B CB   1 
ATOM   2995 C  CG   . ASN B 1 170 ? -5.088  -4.895  27.682  1.00 49.95  ?  172 ASN B CG   1 
ATOM   2996 O  OD1  . ASN B 1 170 ? -5.272  -3.670  27.748  1.00 53.27  ?  172 ASN B OD1  1 
ATOM   2997 N  ND2  . ASN B 1 170 ? -4.143  -5.442  26.910  1.00 50.31  ?  172 ASN B ND2  1 
ATOM   2998 N  N    . ARG B 1 171 ? -9.149  -5.811  30.345  1.00 39.18  ?  173 ARG B N    1 
ATOM   2999 C  CA   . ARG B 1 171 ? -10.219 -6.695  30.822  1.00 39.33  ?  173 ARG B CA   1 
ATOM   3000 C  C    . ARG B 1 171 ? -10.748 -7.597  29.710  1.00 38.55  ?  173 ARG B C    1 
ATOM   3001 O  O    . ARG B 1 171 ? -10.943 -8.786  29.969  1.00 37.62  ?  173 ARG B O    1 
ATOM   3002 C  CB   . ARG B 1 171 ? -11.368 -5.864  31.452  1.00 41.90  ?  173 ARG B CB   1 
ATOM   3003 C  CG   . ARG B 1 171 ? -12.575 -6.698  31.946  1.00 45.20  ?  173 ARG B CG   1 
ATOM   3004 C  CD   . ARG B 1 171 ? -13.466 -5.907  32.911  1.00 50.48  ?  173 ARG B CD   1 
ATOM   3005 N  NE   . ARG B 1 171 ? -14.208 -6.760  33.829  1.00 55.45  ?  173 ARG B NE   1 
ATOM   3006 C  CZ   . ARG B 1 171 ? -14.655 -6.398  35.032  1.00 61.85  ?  173 ARG B CZ   1 
ATOM   3007 N  NH1  . ARG B 1 171 ? -15.318 -7.269  35.791  1.00 63.41  ?  173 ARG B NH1  1 
ATOM   3008 N  NH2  . ARG B 1 171 ? -14.447 -5.159  35.491  1.00 62.81  ?  173 ARG B NH2  1 
ATOM   3009 N  N    . GLU B 1 172 ? -10.955 -7.076  28.454  1.00 39.55  ?  174 GLU B N    1 
ATOM   3010 C  CA   . GLU B 1 172 ? -11.500 -7.927  27.394  1.00 40.39  ?  174 GLU B CA   1 
ATOM   3011 C  C    . GLU B 1 172 ? -10.525 -9.052  26.997  1.00 39.23  ?  174 GLU B C    1 
ATOM   3012 O  O    . GLU B 1 172 ? -10.976 -10.170 26.823  1.00 40.14  ?  174 GLU B O    1 
ATOM   3013 C  CB   . GLU B 1 172 ? -11.959 -7.109  26.143  1.00 44.65  ?  174 GLU B CB   1 
ATOM   3014 C  CG   . GLU B 1 172 ? -13.089 -6.121  26.416  1.00 59.09  ?  174 GLU B CG   1 
ATOM   3015 C  CD   . GLU B 1 172 ? -14.127 -6.434  27.496  1.00 74.38  ?  174 GLU B CD   1 
ATOM   3016 O  OE1  . GLU B 1 172 ? -14.801 -7.489  27.400  1.00 79.02  ?  174 GLU B OE1  1 
ATOM   3017 O  OE2  . GLU B 1 172 ? -14.264 -5.620  28.441  1.00 78.96  ?  174 GLU B OE2  1 
ATOM   3018 N  N    . ALA B 1 173 ? -9.223  -8.769  26.864  1.00 38.83  ?  175 ALA B N    1 
ATOM   3019 C  CA   . ALA B 1 173 ? -8.219  -9.781  26.556  1.00 38.51  ?  175 ALA B CA   1 
ATOM   3020 C  C    . ALA B 1 173 ? -8.168  -10.816 27.692  1.00 35.64  ?  175 ALA B C    1 
ATOM   3021 O  O    . ALA B 1 173 ? -8.231  -12.021 27.425  1.00 34.48  ?  175 ALA B O    1 
ATOM   3022 C  CB   . ALA B 1 173 ? -6.846  -9.145  26.346  1.00 39.76  ?  175 ALA B CB   1 
ATOM   3023 N  N    . VAL B 1 174 ? -8.099  -10.354 28.926  1.00 34.13  ?  176 VAL B N    1 
ATOM   3024 C  CA   . VAL B 1 174 ? -7.887  -11.195 30.092  1.00 35.15  ?  176 VAL B CA   1 
ATOM   3025 C  C    . VAL B 1 174 ? -9.118  -12.108 30.240  1.00 36.34  ?  176 VAL B C    1 
ATOM   3026 O  O    . VAL B 1 174 ? -8.939  -13.309 30.449  1.00 34.98  ?  176 VAL B O    1 
ATOM   3027 C  CB   . VAL B 1 174 ? -7.625  -10.325 31.349  1.00 35.17  ?  176 VAL B CB   1 
ATOM   3028 C  CG1  . VAL B 1 174 ? -7.768  -11.145 32.623  1.00 34.54  ?  176 VAL B CG1  1 
ATOM   3029 C  CG2  . VAL B 1 174 ? -6.237  -9.671  31.291  1.00 35.47  ?  176 VAL B CG2  1 
ATOM   3030 N  N    . THR B 1 175 ? -10.344 -11.544 30.099  1.00 37.94  ?  177 THR B N    1 
ATOM   3031 C  CA   . THR B 1 175 ? -11.559 -12.309 30.315  1.00 40.59  ?  177 THR B CA   1 
ATOM   3032 C  C    . THR B 1 175 ? -11.748 -13.360 29.182  1.00 39.08  ?  177 THR B C    1 
ATOM   3033 O  O    . THR B 1 175 ? -12.218 -14.462 29.461  1.00 37.82  ?  177 THR B O    1 
ATOM   3034 C  CB   . THR B 1 175 ? -12.784 -11.395 30.578  1.00 45.26  ?  177 THR B CB   1 
ATOM   3035 O  OG1  . THR B 1 175 ? -13.028 -10.574 29.450  1.00 49.66  ?  177 THR B OG1  1 
ATOM   3036 C  CG2  . THR B 1 175 ? -12.584 -10.525 31.787  1.00 46.74  ?  177 THR B CG2  1 
ATOM   3037 N  N    . HIS B 1 176 ? -11.379 -13.044 27.949  1.00 38.03  ?  178 HIS B N    1 
ATOM   3038 C  CA   . HIS B 1 176 ? -11.462 -13.992 26.847  1.00 38.90  ?  178 HIS B CA   1 
ATOM   3039 C  C    . HIS B 1 176 ? -10.507 -15.145 27.084  1.00 38.62  ?  178 HIS B C    1 
ATOM   3040 O  O    . HIS B 1 176 ? -10.888 -16.287 26.899  1.00 39.51  ?  178 HIS B O    1 
ATOM   3041 C  CB   . HIS B 1 176 ? -11.104 -13.357 25.484  1.00 39.59  ?  178 HIS B CB   1 
ATOM   3042 C  CG   . HIS B 1 176 ? -11.228 -14.315 24.327  1.00 45.76  ?  178 HIS B CG   1 
ATOM   3043 N  ND1  . HIS B 1 176 ? -10.111 -14.782 23.663  1.00 48.31  ?  178 HIS B ND1  1 
ATOM   3044 C  CD2  . HIS B 1 176 ? -12.317 -14.885 23.760  1.00 48.30  ?  178 HIS B CD2  1 
ATOM   3045 C  CE1  . HIS B 1 176 ? -10.552 -15.590 22.715  1.00 48.75  ?  178 HIS B CE1  1 
ATOM   3046 N  NE2  . HIS B 1 176 ? -11.856 -15.698 22.745  1.00 49.55  ?  178 HIS B NE2  1 
ATOM   3047 N  N    . ILE B 1 177 ? -9.245  -14.838 27.476  1.00 37.56  ?  179 ILE B N    1 
ATOM   3048 C  CA   . ILE B 1 177 ? -8.222  -15.823 27.799  1.00 35.75  ?  179 ILE B CA   1 
ATOM   3049 C  C    . ILE B 1 177 ? -8.770  -16.784 28.861  1.00 34.70  ?  179 ILE B C    1 
ATOM   3050 O  O    . ILE B 1 177 ? -8.773  -17.999 28.633  1.00 34.97  ?  179 ILE B O    1 
ATOM   3051 C  CB   . ILE B 1 177 ? -6.890  -15.147 28.223  1.00 34.37  ?  179 ILE B CB   1 
ATOM   3052 C  CG1  . ILE B 1 177 ? -6.185  -14.491 26.987  1.00 33.66  ?  179 ILE B CG1  1 
ATOM   3053 C  CG2  . ILE B 1 177 ? -5.931  -16.207 28.913  1.00 35.41  ?  179 ILE B CG2  1 
ATOM   3054 C  CD1  . ILE B 1 177 ? -5.105  -13.473 27.367  1.00 32.46  ?  179 ILE B CD1  1 
ATOM   3055 N  N    . GLY B 1 178 ? -9.268  -16.203 29.952  1.00 34.50  ?  180 GLY B N    1 
ATOM   3056 C  CA   . GLY B 1 178 ? -9.822  -16.929 31.084  1.00 36.38  ?  180 GLY B CA   1 
ATOM   3057 C  C    . GLY B 1 178 ? -10.919 -17.889 30.685  1.00 36.74  ?  180 GLY B C    1 
ATOM   3058 O  O    . GLY B 1 178 ? -10.875 -19.061 31.064  1.00 36.28  ?  180 GLY B O    1 
ATOM   3059 N  N    . ARG B 1 179 ? -11.893 -17.398 29.896  1.00 37.45  ?  181 ARG B N    1 
ATOM   3060 C  CA   . ARG B 1 179 ? -13.049 -18.206 29.435  1.00 39.33  ?  181 ARG B CA   1 
ATOM   3061 C  C    . ARG B 1 179 ? -12.606 -19.378 28.563  1.00 37.87  ?  181 ARG B C    1 
ATOM   3062 O  O    . ARG B 1 179 ? -13.086 -20.490 28.753  1.00 37.12  ?  181 ARG B O    1 
ATOM   3063 C  CB   . ARG B 1 179 ? -14.116 -17.362 28.674  1.00 45.00  ?  181 ARG B CB   1 
ATOM   3064 C  CG   . ARG B 1 179 ? -15.108 -18.203 27.837  1.00 56.88  ?  181 ARG B CG   1 
ATOM   3065 C  CD   . ARG B 1 179 ? -16.227 -17.461 27.124  1.00 68.60  ?  181 ARG B CD   1 
ATOM   3066 N  NE   . ARG B 1 179 ? -17.234 -18.432 26.686  1.00 78.26  ?  181 ARG B NE   1 
ATOM   3067 C  CZ   . ARG B 1 179 ? -18.461 -18.136 26.249  1.00 84.84  ?  181 ARG B CZ   1 
ATOM   3068 N  NH1  . ARG B 1 179 ? -18.863 -16.866 26.171  1.00 85.40  ?  181 ARG B NH1  1 
ATOM   3069 N  NH2  . ARG B 1 179 ? -19.294 -19.107 25.886  1.00 85.60  ?  181 ARG B NH2  1 
ATOM   3070 N  N    . VAL B 1 180 ? -11.725 -19.138 27.596  1.00 37.29  ?  182 VAL B N    1 
ATOM   3071 C  CA   . VAL B 1 180 ? -11.260 -20.187 26.709  1.00 37.53  ?  182 VAL B CA   1 
ATOM   3072 C  C    . VAL B 1 180 ? -10.423 -21.181 27.486  1.00 36.52  ?  182 VAL B C    1 
ATOM   3073 O  O    . VAL B 1 180 ? -10.537 -22.385 27.237  1.00 37.74  ?  182 VAL B O    1 
ATOM   3074 C  CB   . VAL B 1 180 ? -10.510 -19.624 25.483  1.00 38.92  ?  182 VAL B CB   1 
ATOM   3075 C  CG1  . VAL B 1 180 ? -9.922  -20.741 24.646  1.00 39.01  ?  182 VAL B CG1  1 
ATOM   3076 C  CG2  . VAL B 1 180 ? -11.414 -18.718 24.638  1.00 40.25  ?  182 VAL B CG2  1 
ATOM   3077 N  N    . TYR B 1 181 ? -9.599  -20.703 28.426  1.00 35.14  ?  183 TYR B N    1 
ATOM   3078 C  CA   . TYR B 1 181 ? -8.734  -21.569 29.225  1.00 35.53  ?  183 TYR B CA   1 
ATOM   3079 C  C    . TYR B 1 181 ? -9.575  -22.531 30.071  1.00 36.71  ?  183 TYR B C    1 
ATOM   3080 O  O    . TYR B 1 181 ? -9.315  -23.738 30.060  1.00 36.25  ?  183 TYR B O    1 
ATOM   3081 C  CB   . TYR B 1 181 ? -7.825  -20.714 30.091  1.00 34.46  ?  183 TYR B CB   1 
ATOM   3082 C  CG   . TYR B 1 181 ? -6.778  -21.410 30.913  1.00 34.65  ?  183 TYR B CG   1 
ATOM   3083 C  CD1  . TYR B 1 181 ? -6.135  -22.547 30.442  1.00 35.02  ?  183 TYR B CD1  1 
ATOM   3084 C  CD2  . TYR B 1 181 ? -6.364  -20.888 32.131  1.00 33.45  ?  183 TYR B CD2  1 
ATOM   3085 C  CE1  . TYR B 1 181 ? -5.147  -23.166 31.184  1.00 34.68  ?  183 TYR B CE1  1 
ATOM   3086 C  CE2  . TYR B 1 181 ? -5.369  -21.488 32.876  1.00 33.89  ?  183 TYR B CE2  1 
ATOM   3087 C  CZ   . TYR B 1 181 ? -4.757  -22.631 32.397  1.00 34.75  ?  183 TYR B CZ   1 
ATOM   3088 O  OH   . TYR B 1 181 ? -3.748  -23.184 33.114  1.00 34.20  ?  183 TYR B OH   1 
ATOM   3089 N  N    . LYS B 1 182 ? -10.590 -22.005 30.773  1.00 37.90  ?  184 LYS B N    1 
ATOM   3090 C  CA   . LYS B 1 182 ? -11.468 -22.812 31.598  1.00 40.08  ?  184 LYS B CA   1 
ATOM   3091 C  C    . LYS B 1 182 ? -12.181 -23.906 30.768  1.00 42.01  ?  184 LYS B C    1 
ATOM   3092 O  O    . LYS B 1 182 ? -12.254 -25.059 31.194  1.00 43.44  ?  184 LYS B O    1 
ATOM   3093 C  CB   . LYS B 1 182 ? -12.481 -21.913 32.326  1.00 40.56  ?  184 LYS B CB   1 
ATOM   3094 C  CG   . LYS B 1 182 ? -13.354 -22.638 33.299  1.00 44.63  ?  184 LYS B CG   1 
ATOM   3095 C  CD   . LYS B 1 182 ? -14.240 -21.719 34.096  1.00 48.85  ?  184 LYS B CD   1 
ATOM   3096 C  CE   . LYS B 1 182 ? -15.138 -22.485 35.030  1.00 55.90  ?  184 LYS B CE   1 
ATOM   3097 N  NZ   . LYS B 1 182 ? -15.867 -21.586 35.953  1.00 60.61  ?  184 LYS B NZ   1 
ATOM   3098 N  N    . GLU B 1 183 ? -12.669 -23.534 29.601  1.00 41.64  ?  185 GLU B N    1 
ATOM   3099 C  CA   . GLU B 1 183 ? -13.296 -24.430 28.662  1.00 42.48  ?  185 GLU B CA   1 
ATOM   3100 C  C    . GLU B 1 183 ? -12.302 -25.531 28.206  1.00 41.12  ?  185 GLU B C    1 
ATOM   3101 O  O    . GLU B 1 183 ? -12.641 -26.711 28.220  1.00 40.47  ?  185 GLU B O    1 
ATOM   3102 C  CB   . GLU B 1 183 ? -13.821 -23.619 27.460  1.00 47.61  ?  185 GLU B CB   1 
ATOM   3103 C  CG   . GLU B 1 183 ? -14.705 -24.340 26.454  1.00 59.89  ?  185 GLU B CG   1 
ATOM   3104 C  CD   . GLU B 1 183 ? -15.302 -23.373 25.435  1.00 76.02  ?  185 GLU B CD   1 
ATOM   3105 O  OE1  . GLU B 1 183 ? -14.664 -22.331 25.144  1.00 80.85  ?  185 GLU B OE1  1 
ATOM   3106 O  OE2  . GLU B 1 183 ? -16.416 -23.655 24.933  1.00 81.35  ?  185 GLU B OE2  1 
ATOM   3107 N  N    . ARG B 1 184 ? -11.074 -25.147 27.827  1.00 39.98  ?  186 ARG B N    1 
ATOM   3108 C  CA   . ARG B 1 184 ? -10.068 -26.102 27.404  1.00 39.85  ?  186 ARG B CA   1 
ATOM   3109 C  C    . ARG B 1 184 ? -9.588  -27.051 28.540  1.00 41.29  ?  186 ARG B C    1 
ATOM   3110 O  O    . ARG B 1 184 ? -9.207  -28.182 28.254  1.00 41.89  ?  186 ARG B O    1 
ATOM   3111 C  CB   . ARG B 1 184 ? -8.880  -25.360 26.742  1.00 39.30  ?  186 ARG B CB   1 
ATOM   3112 C  CG   . ARG B 1 184 ? -9.240  -24.752 25.411  1.00 43.50  ?  186 ARG B CG   1 
ATOM   3113 C  CD   . ARG B 1 184 ? -9.376  -25.776 24.296  1.00 44.54  ?  186 ARG B CD   1 
ATOM   3114 N  NE   . ARG B 1 184 ? -8.065  -26.346 23.998  1.00 45.79  ?  186 ARG B NE   1 
ATOM   3115 C  CZ   . ARG B 1 184 ? -7.233  -25.958 23.035  1.00 42.83  ?  186 ARG B CZ   1 
ATOM   3116 N  NH1  . ARG B 1 184 ? -7.567  -24.969 22.204  1.00 41.43  ?  186 ARG B NH1  1 
ATOM   3117 N  NH2  . ARG B 1 184 ? -6.068  -26.564 22.880  1.00 39.54  ?  186 ARG B NH2  1 
ATOM   3118 N  N    . LEU B 1 185 ? -9.605  -26.603 29.795  1.00 41.35  ?  187 LEU B N    1 
ATOM   3119 C  CA   . LEU B 1 185 ? -9.301  -27.455 30.932  1.00 43.05  ?  187 LEU B CA   1 
ATOM   3120 C  C    . LEU B 1 185 ? -10.464 -28.432 31.263  1.00 46.34  ?  187 LEU B C    1 
ATOM   3121 O  O    . LEU B 1 185 ? -10.258 -29.368 32.017  1.00 47.31  ?  187 LEU B O    1 
ATOM   3122 C  CB   . LEU B 1 185 ? -9.010  -26.588 32.190  1.00 42.68  ?  187 LEU B CB   1 
ATOM   3123 C  CG   . LEU B 1 185 ? -7.716  -25.780 32.194  1.00 43.75  ?  187 LEU B CG   1 
ATOM   3124 C  CD1  . LEU B 1 185 ? -7.699  -24.768 33.369  1.00 43.60  ?  187 LEU B CD1  1 
ATOM   3125 C  CD2  . LEU B 1 185 ? -6.484  -26.692 32.174  1.00 43.88  ?  187 LEU B CD2  1 
ATOM   3126 N  N    . GLY B 1 186 ? -11.656 -28.194 30.729  1.00 48.53  ?  188 GLY B N    1 
ATOM   3127 C  CA   . GLY B 1 186 ? -12.840 -28.989 31.010  1.00 51.51  ?  188 GLY B CA   1 
ATOM   3128 C  C    . GLY B 1 186 ? -13.435 -28.742 32.377  1.00 54.73  ?  188 GLY B C    1 
ATOM   3129 O  O    . GLY B 1 186 ? -14.182 -29.589 32.871  1.00 55.64  ?  188 GLY B O    1 
ATOM   3130 N  N    . LEU B 1 187 ? -13.147 -27.591 33.004  1.00 55.77  ?  189 LEU B N    1 
ATOM   3131 C  CA   . LEU B 1 187 ? -13.623 -27.352 34.376  1.00 58.01  ?  189 LEU B CA   1 
ATOM   3132 C  C    . LEU B 1 187 ? -15.148 -27.072 34.431  1.00 61.68  ?  189 LEU B C    1 
ATOM   3133 O  O    . LEU B 1 187 ? -15.661 -26.344 33.572  1.00 62.08  ?  189 LEU B O    1 
ATOM   3134 C  CB   . LEU B 1 187 ? -12.879 -26.174 34.987  1.00 57.44  ?  189 LEU B CB   1 
ATOM   3135 C  CG   . LEU B 1 187 ? -11.386 -26.328 35.258  1.00 57.75  ?  189 LEU B CG   1 
ATOM   3136 C  CD1  . LEU B 1 187 ? -10.846 -25.078 35.913  1.00 57.72  ?  189 LEU B CD1  1 
ATOM   3137 C  CD2  . LEU B 1 187 ? -11.097 -27.497 36.167  1.00 58.28  ?  189 LEU B CD2  1 
ATOM   3138 N  N    . PRO B 1 188 ? -15.907 -27.621 35.408  1.00 63.73  ?  190 PRO B N    1 
ATOM   3139 C  CA   . PRO B 1 188 ? -17.328 -27.225 35.523  1.00 65.83  ?  190 PRO B CA   1 
ATOM   3140 C  C    . PRO B 1 188 ? -17.515 -25.728 35.783  1.00 69.62  ?  190 PRO B C    1 
ATOM   3141 O  O    . PRO B 1 188 ? -16.672 -25.144 36.465  1.00 70.70  ?  190 PRO B O    1 
ATOM   3142 C  CB   . PRO B 1 188 ? -17.842 -28.028 36.725  1.00 65.35  ?  190 PRO B CB   1 
ATOM   3143 C  CG   . PRO B 1 188 ? -16.868 -29.111 36.937  1.00 65.69  ?  190 PRO B CG   1 
ATOM   3144 C  CD   . PRO B 1 188 ? -15.537 -28.618 36.433  1.00 63.68  ?  190 PRO B CD   1 
ATOM   3145 N  N    . PRO B 1 189 ? -18.585 -25.072 35.273  1.00 71.33  ?  191 PRO B N    1 
ATOM   3146 C  CA   . PRO B 1 189 ? -18.832 -23.666 35.654  1.00 72.56  ?  191 PRO B CA   1 
ATOM   3147 C  C    . PRO B 1 189 ? -18.847 -23.377 37.158  1.00 73.64  ?  191 PRO B C    1 
ATOM   3148 O  O    . PRO B 1 189 ? -18.562 -22.250 37.557  1.00 73.73  ?  191 PRO B O    1 
ATOM   3149 C  CB   . PRO B 1 189 ? -20.208 -23.348 35.034  1.00 73.23  ?  191 PRO B CB   1 
ATOM   3150 C  CG   . PRO B 1 189 ? -20.770 -24.651 34.582  1.00 73.33  ?  191 PRO B CG   1 
ATOM   3151 C  CD   . PRO B 1 189 ? -19.613 -25.559 34.329  1.00 71.61  ?  191 PRO B CD   1 
ATOM   3152 N  N    . LYS B 1 190 ? -19.224 -24.388 37.970  1.00 73.80  ?  192 LYS B N    1 
ATOM   3153 C  CA   . LYS B 1 190 ? -19.144 -24.381 39.440  1.00 74.20  ?  192 LYS B CA   1 
ATOM   3154 C  C    . LYS B 1 190 ? -17.745 -24.028 40.007  1.00 73.12  ?  192 LYS B C    1 
ATOM   3155 O  O    . LYS B 1 190 ? -17.677 -23.314 41.010  1.00 73.26  ?  192 LYS B O    1 
ATOM   3156 C  CB   . LYS B 1 190 ? -19.570 -25.764 39.992  1.00 77.42  ?  192 LYS B CB   1 
ATOM   3157 C  CG   . LYS B 1 190 ? -21.053 -26.072 39.783  1.00 83.73  ?  192 LYS B CG   1 
ATOM   3158 C  CD   . LYS B 1 190 ? -21.428 -27.484 40.247  1.00 89.88  ?  192 LYS B CD   1 
ATOM   3159 C  CE   . LYS B 1 190 ? -22.854 -27.835 39.871  1.00 93.90  ?  192 LYS B CE   1 
ATOM   3160 N  NZ   . LYS B 1 190 ? -23.357 -29.008 40.626  1.00 95.61  ?  192 LYS B NZ   1 
ATOM   3161 N  N    . ILE B 1 191 ? -16.642 -24.546 39.389  1.00 71.50  ?  193 ILE B N    1 
ATOM   3162 C  CA   . ILE B 1 191 ? -15.267 -24.274 39.829  1.00 69.81  ?  193 ILE B CA   1 
ATOM   3163 C  C    . ILE B 1 191 ? -14.849 -22.962 39.217  1.00 66.62  ?  193 ILE B C    1 
ATOM   3164 O  O    . ILE B 1 191 ? -14.603 -22.921 38.017  1.00 67.32  ?  193 ILE B O    1 
ATOM   3165 C  CB   . ILE B 1 191 ? -14.287 -25.426 39.439  1.00 70.99  ?  193 ILE B CB   1 
ATOM   3166 C  CG1  . ILE B 1 191 ? -14.748 -26.781 40.029  1.00 72.50  ?  193 ILE B CG1  1 
ATOM   3167 C  CG2  . ILE B 1 191 ? -12.851 -25.095 39.869  1.00 71.38  ?  193 ILE B CG2  1 
ATOM   3168 C  CD1  . ILE B 1 191 ? -14.877 -26.838 41.610  1.00 73.74  ?  193 ILE B CD1  1 
ATOM   3169 N  N    . VAL B 1 192 ? -14.764 -21.887 40.038  1.00 62.90  ?  194 VAL B N    1 
ATOM   3170 C  CA   . VAL B 1 192 ? -14.411 -20.543 39.557  1.00 59.07  ?  194 VAL B CA   1 
ATOM   3171 C  C    . VAL B 1 192 ? -12.921 -20.287 39.664  1.00 53.75  ?  194 VAL B C    1 
ATOM   3172 O  O    . VAL B 1 192 ? -12.301 -20.600 40.674  1.00 52.87  ?  194 VAL B O    1 
ATOM   3173 C  CB   . VAL B 1 192 ? -15.180 -19.419 40.289  1.00 60.40  ?  194 VAL B CB   1 
ATOM   3174 C  CG1  . VAL B 1 192 ? -16.681 -19.674 40.249  1.00 60.91  ?  194 VAL B CG1  1 
ATOM   3175 C  CG2  . VAL B 1 192 ? -14.674 -19.234 41.721  1.00 61.51  ?  194 VAL B CG2  1 
ATOM   3176 N  N    . ILE B 1 193 ? -12.377 -19.644 38.635  1.00 50.63  ?  195 ILE B N    1 
ATOM   3177 C  CA   . ILE B 1 193 ? -10.949 -19.386 38.596  1.00 47.54  ?  195 ILE B CA   1 
ATOM   3178 C  C    . ILE B 1 193 ? -10.727 -17.890 38.673  1.00 43.62  ?  195 ILE B C    1 
ATOM   3179 O  O    . ILE B 1 193 ? -11.541 -17.110 38.183  1.00 42.42  ?  195 ILE B O    1 
ATOM   3180 C  CB   . ILE B 1 193 ? -10.269 -20.092 37.395  1.00 46.91  ?  195 ILE B CB   1 
ATOM   3181 C  CG1  . ILE B 1 193 ? -10.618 -19.425 36.053  1.00 47.45  ?  195 ILE B CG1  1 
ATOM   3182 C  CG2  . ILE B 1 193 ? -10.637 -21.579 37.406  1.00 47.69  ?  195 ILE B CG2  1 
ATOM   3183 C  CD1  . ILE B 1 193 ? -9.731  -19.833 34.918  1.00 47.18  ?  195 ILE B CD1  1 
ATOM   3184 N  N    . GLY B 1 194 ? -9.611  -17.514 39.283  1.00 41.24  ?  196 GLY B N    1 
ATOM   3185 C  CA   . GLY B 1 194 ? -9.338  -16.113 39.510  1.00 39.00  ?  196 GLY B CA   1 
ATOM   3186 C  C    . GLY B 1 194 ? -8.115  -15.614 38.750  1.00 35.62  ?  196 GLY B C    1 
ATOM   3187 O  O    . GLY B 1 194 ? -7.155  -16.353 38.544  1.00 34.21  ?  196 GLY B O    1 
ATOM   3188 N  N    . TYR B 1 195 ? -8.155  -14.347 38.341  1.00 35.70  ?  197 TYR B N    1 
ATOM   3189 C  CA   . TYR B 1 195 ? -7.029  -13.617 37.764  1.00 32.89  ?  197 TYR B CA   1 
ATOM   3190 C  C    . TYR B 1 195 ? -6.492  -12.636 38.792  1.00 34.47  ?  197 TYR B C    1 
ATOM   3191 O  O    . TYR B 1 195 ? -7.225  -11.774 39.324  1.00 35.37  ?  197 TYR B O    1 
ATOM   3192 C  CB   . TYR B 1 195 ? -7.438  -12.929 36.472  1.00 32.01  ?  197 TYR B CB   1 
ATOM   3193 C  CG   . TYR B 1 195 ? -6.310  -12.209 35.742  1.00 31.62  ?  197 TYR B CG   1 
ATOM   3194 C  CD1  . TYR B 1 195 ? -5.978  -10.894 36.050  1.00 33.59  ?  197 TYR B CD1  1 
ATOM   3195 C  CD2  . TYR B 1 195 ? -5.591  -12.836 34.730  1.00 30.97  ?  197 TYR B CD2  1 
ATOM   3196 C  CE1  . TYR B 1 195 ? -4.943  -10.230 35.385  1.00 33.62  ?  197 TYR B CE1  1 
ATOM   3197 C  CE2  . TYR B 1 195 ? -4.555  -12.182 34.063  1.00 32.31  ?  197 TYR B CE2  1 
ATOM   3198 C  CZ   . TYR B 1 195 ? -4.244  -10.870 34.378  1.00 33.02  ?  197 TYR B CZ   1 
ATOM   3199 O  OH   . TYR B 1 195 ? -3.263  -10.173 33.685  1.00 33.35  ?  197 TYR B OH   1 
ATOM   3200 N  N    . GLN B 1 196 ? -5.194  -12.759 39.091  1.00 34.69  ?  198 GLN B N    1 
ATOM   3201 C  CA   . GLN B 1 196 ? -4.509  -11.921 40.070  1.00 34.66  ?  198 GLN B CA   1 
ATOM   3202 C  C    . GLN B 1 196 ? -3.410  -11.111 39.387  1.00 34.58  ?  198 GLN B C    1 
ATOM   3203 O  O    . GLN B 1 196 ? -2.576  -11.643 38.621  1.00 32.99  ?  198 GLN B O    1 
ATOM   3204 C  CB   . GLN B 1 196 ? -3.870  -12.750 41.193  1.00 36.22  ?  198 GLN B CB   1 
ATOM   3205 C  CG   . GLN B 1 196 ? -4.810  -13.758 41.875  1.00 42.69  ?  198 GLN B CG   1 
ATOM   3206 C  CD   . GLN B 1 196 ? -4.041  -14.894 42.553  1.00 52.55  ?  198 GLN B CD   1 
ATOM   3207 O  OE1  . GLN B 1 196 ? -2.880  -15.196 42.228  1.00 57.08  ?  198 GLN B OE1  1 
ATOM   3208 N  NE2  . GLN B 1 196 ? -4.678  -15.557 43.516  1.00 54.03  ?  198 GLN B NE2  1 
ATOM   3209 N  N    . SER B 1 197 ? -3.415  -9.818  39.657  1.00 33.17  ?  199 SER B N    1 
ATOM   3210 C  CA   . SER B 1 197 ? -2.334  -8.899  39.272  1.00 34.07  ?  199 SER B CA   1 
ATOM   3211 C  C    . SER B 1 197 ? -1.019  -9.377  39.909  1.00 33.53  ?  199 SER B C    1 
ATOM   3212 O  O    . SER B 1 197 ? -1.036  -9.823  41.071  1.00 34.30  ?  199 SER B O    1 
ATOM   3213 C  CB   . SER B 1 197 ? -2.702  -7.489  39.784  1.00 36.00  ?  199 SER B CB   1 
ATOM   3214 O  OG   . SER B 1 197 ? -1.613  -6.606  39.667  1.00 42.76  ?  199 SER B OG   1 
ATOM   3215 N  N    . HIS B 1 198 ? 0.103   -9.330  39.185  1.00 33.48  ?  200 HIS B N    1 
ATOM   3216 C  CA   . HIS B 1 198 ? 1.403   -9.680  39.805  1.00 33.79  ?  200 HIS B CA   1 
ATOM   3217 C  C    . HIS B 1 198 ? 1.769   -8.697  40.947  1.00 36.37  ?  200 HIS B C    1 
ATOM   3218 O  O    . HIS B 1 198 ? 2.297   -9.137  41.969  1.00 38.00  ?  200 HIS B O    1 
ATOM   3219 C  CB   . HIS B 1 198 ? 2.497   -9.690  38.759  1.00 33.45  ?  200 HIS B CB   1 
ATOM   3220 C  CG   . HIS B 1 198 ? 2.368   -10.802 37.750  1.00 32.86  ?  200 HIS B CG   1 
ATOM   3221 N  ND1  . HIS B 1 198 ? 1.957   -12.072 38.113  1.00 34.37  ?  200 HIS B ND1  1 
ATOM   3222 C  CD2  . HIS B 1 198 ? 2.594   -10.784 36.433  1.00 34.41  ?  200 HIS B CD2  1 
ATOM   3223 C  CE1  . HIS B 1 198 ? 1.979   -12.788 37.009  1.00 35.60  ?  200 HIS B CE1  1 
ATOM   3224 N  NE2  . HIS B 1 198 ? 2.355   -12.043 35.971  1.00 34.19  ?  200 HIS B NE2  1 
ATOM   3225 N  N    . ALA B 1 199 ? 1.487   -7.404  40.764  1.00 36.69  ?  201 ALA B N    1 
ATOM   3226 C  CA   . ALA B 1 199 ? 1.611   -6.373  41.803  1.00 40.23  ?  201 ALA B CA   1 
ATOM   3227 C  C    . ALA B 1 199 ? 0.849   -6.742  43.103  1.00 43.40  ?  201 ALA B C    1 
ATOM   3228 O  O    . ALA B 1 199 ? 1.375   -6.493  44.187  1.00 45.56  ?  201 ALA B O    1 
ATOM   3229 C  CB   . ALA B 1 199 ? 1.134   -5.040  41.269  1.00 40.35  ?  201 ALA B CB   1 
ATOM   3230 N  N    . ASP B 1 200 ? -0.357  -7.352  43.018  1.00 43.21  ?  202 ASP B N    1 
ATOM   3231 C  CA   . ASP B 1 200 ? -1.064  -7.777  44.219  1.00 44.14  ?  202 ASP B CA   1 
ATOM   3232 C  C    . ASP B 1 200 ? -0.445  -9.043  44.802  1.00 44.91  ?  202 ASP B C    1 
ATOM   3233 O  O    . ASP B 1 200 ? -0.291  -9.143  46.037  1.00 44.71  ?  202 ASP B O    1 
ATOM   3234 C  CB   . ASP B 1 200 ? -2.574  -7.952  43.969  1.00 46.99  ?  202 ASP B CB   1 
ATOM   3235 C  CG   . ASP B 1 200 ? -3.281  -6.663  43.581  1.00 54.00  ?  202 ASP B CG   1 
ATOM   3236 O  OD1  . ASP B 1 200 ? -2.723  -5.555  43.883  1.00 55.78  ?  202 ASP B OD1  1 
ATOM   3237 O  OD2  . ASP B 1 200 ? -4.393  -6.752  42.965  1.00 53.52  ?  202 ASP B OD2  1 
ATOM   3238 N  N    . THR B 1 201 ? -0.090  -10.021 43.949  1.00 44.44  ?  203 THR B N    1 
ATOM   3239 C  CA   . THR B 1 201 ? 0.546   -11.248 44.412  1.00 46.78  ?  203 THR B CA   1 
ATOM   3240 C  C    . THR B 1 201 ? 1.869   -10.994 45.159  1.00 49.05  ?  203 THR B C    1 
ATOM   3241 O  O    . THR B 1 201 ? 2.160   -11.679 46.147  1.00 49.57  ?  203 THR B O    1 
ATOM   3242 C  CB   . THR B 1 201 ? 0.806   -12.193 43.254  1.00 47.79  ?  203 THR B CB   1 
ATOM   3243 O  OG1  . THR B 1 201 ? -0.447  -12.482 42.637  1.00 49.54  ?  203 THR B OG1  1 
ATOM   3244 C  CG2  . THR B 1 201 ? 1.462   -13.499 43.727  1.00 47.39  ?  203 THR B CG2  1 
ATOM   3245 N  N    . ALA B 1 202 ? 2.654   -10.020 44.680  1.00 48.94  ?  204 ALA B N    1 
ATOM   3246 C  CA   . ALA B 1 202 ? 3.914   -9.594  45.279  1.00 49.43  ?  204 ALA B CA   1 
ATOM   3247 C  C    . ALA B 1 202 ? 3.770   -9.124  46.718  1.00 51.65  ?  204 ALA B C    1 
ATOM   3248 O  O    . ALA B 1 202 ? 4.701   -9.316  47.487  1.00 52.44  ?  204 ALA B O    1 
ATOM   3249 C  CB   . ALA B 1 202 ? 4.510   -8.453  44.486  1.00 49.23  ?  204 ALA B CB   1 
ATOM   3250 N  N    . THR B 1 203 ? 2.642   -8.492  47.078  1.00 52.72  ?  205 THR B N    1 
ATOM   3251 C  CA   . THR B 1 203 ? 2.449   -7.981  48.430  1.00 55.04  ?  205 THR B CA   1 
ATOM   3252 C  C    . THR B 1 203 ? 1.758   -9.044  49.294  1.00 53.30  ?  205 THR B C    1 
ATOM   3253 O  O    . THR B 1 203 ? 0.690   -9.534  48.922  1.00 52.88  ?  205 THR B O    1 
ATOM   3254 C  CB   . THR B 1 203 ? 1.663   -6.671  48.414  1.00 60.37  ?  205 THR B CB   1 
ATOM   3255 O  OG1  . THR B 1 203 ? 0.461   -6.846  47.671  1.00 64.02  ?  205 THR B OG1  1 
ATOM   3256 C  CG2  . THR B 1 203 ? 2.480   -5.511  47.784  1.00 61.57  ?  205 THR B CG2  1 
ATOM   3257 N  N    . LYS B 1 204 ? 2.371   -9.393  50.432  1.00 51.54  ?  206 LYS B N    1 
ATOM   3258 C  CA   . LYS B 1 204 ? 1.865   -10.428 51.334  1.00 50.53  ?  206 LYS B CA   1 
ATOM   3259 C  C    . LYS B 1 204 ? 1.014   -9.777  52.435  1.00 49.73  ?  206 LYS B C    1 
ATOM   3260 O  O    . LYS B 1 204 ? 1.525   -9.082  53.335  1.00 47.16  ?  206 LYS B O    1 
ATOM   3261 C  CB   . LYS B 1 204 ? 3.016   -11.258 51.932  1.00 52.59  ?  206 LYS B CB   1 
ATOM   3262 C  CG   . LYS B 1 204 ? 4.018   -11.858 50.927  1.00 54.97  ?  206 LYS B CG   1 
ATOM   3263 C  CD   . LYS B 1 204 ? 3.458   -13.024 50.138  1.00 62.74  ?  206 LYS B CD   1 
ATOM   3264 C  CE   . LYS B 1 204 ? 4.443   -14.165 49.895  1.00 68.35  ?  206 LYS B CE   1 
ATOM   3265 N  NZ   . LYS B 1 204 ? 3.759   -15.504 49.757  1.00 71.65  ?  206 LYS B NZ   1 
ATOM   3266 N  N    . SER B 1 205 ? -0.306  -10.022 52.354  1.00 51.01  ?  207 SER B N    1 
ATOM   3267 C  CA   . SER B 1 205 ? -1.318  -9.352  53.174  1.00 51.74  ?  207 SER B CA   1 
ATOM   3268 C  C    . SER B 1 205 ? -2.160  -10.338 53.998  1.00 50.78  ?  207 SER B C    1 
ATOM   3269 O  O    . SER B 1 205 ? -3.198  -9.928  54.482  1.00 51.19  ?  207 SER B O    1 
ATOM   3270 C  CB   . SER B 1 205 ? -2.253  -8.522  52.281  1.00 56.16  ?  207 SER B CB   1 
ATOM   3271 O  OG   . SER B 1 205 ? -1.558  -7.467  51.632  1.00 63.44  ?  207 SER B OG   1 
ATOM   3272 N  N    . GLY B 1 206 ? -1.715  -11.584 54.157  1.00 50.18  ?  208 GLY B N    1 
ATOM   3273 C  CA   . GLY B 1 206 ? -2.447  -12.652 54.845  1.00 50.42  ?  208 GLY B CA   1 
ATOM   3274 C  C    . GLY B 1 206 ? -2.431  -13.969 54.077  1.00 51.34  ?  208 GLY B C    1 
ATOM   3275 O  O    . GLY B 1 206 ? -1.424  -14.345 53.470  1.00 49.54  ?  208 GLY B O    1 
ATOM   3276 N  N    . SER B 1 207 ? -3.539  -14.718 54.091  1.00 53.59  ?  209 SER B N    1 
ATOM   3277 C  CA   . SER B 1 207 ? -3.561  -16.069 53.455  1.00 55.25  ?  209 SER B CA   1 
ATOM   3278 C  C    . SER B 1 207 ? -3.951  -16.024 51.994  1.00 56.85  ?  209 SER B C    1 
ATOM   3279 O  O    . SER B 1 207 ? -3.702  -17.000 51.290  1.00 57.08  ?  209 SER B O    1 
ATOM   3280 C  CB   . SER B 1 207 ? -4.514  -17.010 54.189  1.00 57.25  ?  209 SER B CB   1 
ATOM   3281 O  OG   . SER B 1 207 ? -5.724  -16.362 54.556  1.00 60.94  ?  209 SER B OG   1 
ATOM   3282 N  N    . THR B 1 208 ? -4.556  -14.910 51.519  1.00 57.56  ?  210 THR B N    1 
ATOM   3283 C  CA   . THR B 1 208 ? -5.051  -14.852 50.145  1.00 58.22  ?  210 THR B CA   1 
ATOM   3284 C  C    . THR B 1 208 ? -4.637  -13.547 49.448  1.00 56.55  ?  210 THR B C    1 
ATOM   3285 O  O    . THR B 1 208 ? -4.263  -12.563 50.107  1.00 57.17  ?  210 THR B O    1 
ATOM   3286 C  CB   . THR B 1 208 ? -6.591  -15.027 50.141  1.00 61.62  ?  210 THR B CB   1 
ATOM   3287 O  OG1  . THR B 1 208 ? -7.023  -15.229 48.788  1.00 64.05  ?  210 THR B OG1  1 
ATOM   3288 C  CG2  . THR B 1 208 ? -7.303  -13.839 50.755  1.00 62.60  ?  210 THR B CG2  1 
ATOM   3289 N  N    . THR B 1 209 ? -4.721  -13.581 48.112  1.00 53.29  ?  211 THR B N    1 
ATOM   3290 C  CA   . THR B 1 209 ? -4.431  -12.476 47.200  1.00 51.65  ?  211 THR B CA   1 
ATOM   3291 C  C    . THR B 1 209 ? -5.740  -12.169 46.424  1.00 46.94  ?  211 THR B C    1 
ATOM   3292 O  O    . THR B 1 209 ? -6.414  -13.082 45.968  1.00 46.57  ?  211 THR B O    1 
ATOM   3293 C  CB   . THR B 1 209 ? -3.131  -12.726 46.361  1.00 53.94  ?  211 THR B CB   1 
ATOM   3294 O  OG1  . THR B 1 209 ? -3.160  -11.943 45.176  1.00 54.27  ?  211 THR B OG1  1 
ATOM   3295 C  CG2  . THR B 1 209 ? -2.876  -14.160 46.050  1.00 57.39  ?  211 THR B CG2  1 
ATOM   3296 N  N    . LYS B 1 210 ? -6.094  -10.885 46.334  1.00 44.22  ?  212 LYS B N    1 
ATOM   3297 C  CA   . LYS B 1 210 ? -7.286  -10.369 45.642  1.00 44.12  ?  212 LYS B CA   1 
ATOM   3298 C  C    . LYS B 1 210 ? -7.314  -10.862 44.200  1.00 42.40  ?  212 LYS B C    1 
ATOM   3299 O  O    . LYS B 1 210 ? -6.267  -10.869 43.554  1.00 42.24  ?  212 LYS B O    1 
ATOM   3300 C  CB   . LYS B 1 210 ? -7.265  -8.804  45.536  1.00 47.06  ?  212 LYS B CB   1 
ATOM   3301 C  CG   . LYS B 1 210 ? -7.119  -8.047  46.828  1.00 55.83  ?  212 LYS B CG   1 
ATOM   3302 C  CD   . LYS B 1 210 ? -7.436  -6.575  46.647  1.00 60.83  ?  212 LYS B CD   1 
ATOM   3303 C  CE   . LYS B 1 210 ? -6.589  -5.870  45.599  1.00 64.11  ?  212 LYS B CE   1 
ATOM   3304 N  NZ   . LYS B 1 210 ? -6.626  -4.397  45.784  1.00 65.49  ?  212 LYS B NZ   1 
ATOM   3305 N  N    . ASN B 1 211 ? -8.495  -11.258 43.719  1.00 41.97  ?  213 ASN B N    1 
ATOM   3306 C  CA   . ASN B 1 211 ? -8.781  -11.440 42.306  1.00 42.68  ?  213 ASN B CA   1 
ATOM   3307 C  C    . ASN B 1 211 ? -9.266  -10.149 41.699  1.00 43.40  ?  213 ASN B C    1 
ATOM   3308 O  O    . ASN B 1 211 ? -10.139 -9.487  42.230  1.00 43.57  ?  213 ASN B O    1 
ATOM   3309 C  CB   . ASN B 1 211 ? -9.806  -12.547 42.125  1.00 44.75  ?  213 ASN B CB   1 
ATOM   3310 C  CG   . ASN B 1 211 ? -9.316  -13.921 42.526  1.00 47.94  ?  213 ASN B CG   1 
ATOM   3311 O  OD1  . ASN B 1 211 ? -10.079 -14.682 43.112  1.00 51.78  ?  213 ASN B OD1  1 
ATOM   3312 N  ND2  . ASN B 1 211 ? -8.089  -14.307 42.269  1.00 45.23  ?  213 ASN B ND2  1 
ATOM   3313 N  N    . ARG B 1 212 ? -8.668  -9.772  40.579  1.00 43.69  ?  214 ARG B N    1 
ATOM   3314 C  CA   . ARG B 1 212 ? -9.070  -8.631  39.764  1.00 45.00  ?  214 ARG B CA   1 
ATOM   3315 C  C    . ARG B 1 212 ? -10.346 -9.088  38.982  1.00 45.72  ?  214 ARG B C    1 
ATOM   3316 O  O    . ARG B 1 212 ? -11.318 -8.349  38.939  1.00 46.75  ?  214 ARG B O    1 
ATOM   3317 C  CB   . ARG B 1 212 ? -7.848  -8.250  38.855  1.00 47.58  ?  214 ARG B CB   1 
ATOM   3318 C  CG   . ARG B 1 212 ? -7.939  -7.063  37.937  1.00 55.59  ?  214 ARG B CG   1 
ATOM   3319 C  CD   . ARG B 1 212 ? -7.978  -5.730  38.669  1.00 58.93  ?  214 ARG B CD   1 
ATOM   3320 N  NE   . ARG B 1 212 ? -6.726  -5.368  39.353  1.00 60.58  ?  214 ARG B NE   1 
ATOM   3321 C  CZ   . ARG B 1 212 ? -5.618  -4.953  38.738  1.00 59.73  ?  214 ARG B CZ   1 
ATOM   3322 N  NH1  . ARG B 1 212 ? -4.538  -4.645  39.441  1.00 58.22  ?  214 ARG B NH1  1 
ATOM   3323 N  NH2  . ARG B 1 212 ? -5.580  -4.852  37.414  1.00 60.81  ?  214 ARG B NH2  1 
ATOM   3324 N  N    . PHE B 1 213 ? -10.334 -10.313 38.399  1.00 44.84  ?  215 PHE B N    1 
ATOM   3325 C  CA   . PHE B 1 213 ? -11.405 -10.919 37.594  1.00 44.81  ?  215 PHE B CA   1 
ATOM   3326 C  C    . PHE B 1 213 ? -11.595 -12.381 38.001  1.00 46.04  ?  215 PHE B C    1 
ATOM   3327 O  O    . PHE B 1 213 ? -10.691 -13.021 38.538  1.00 45.66  ?  215 PHE B O    1 
ATOM   3328 C  CB   . PHE B 1 213 ? -11.086 -10.882 36.061  1.00 44.08  ?  215 PHE B CB   1 
ATOM   3329 C  CG   . PHE B 1 213 ? -10.590 -9.564  35.537  1.00 44.77  ?  215 PHE B CG   1 
ATOM   3330 C  CD1  . PHE B 1 213 ? -11.433 -8.467  35.460  1.00 47.83  ?  215 PHE B CD1  1 
ATOM   3331 C  CD2  . PHE B 1 213 ? -9.268  -9.400  35.178  1.00 45.44  ?  215 PHE B CD2  1 
ATOM   3332 C  CE1  . PHE B 1 213 ? -10.959 -7.236  35.041  1.00 48.44  ?  215 PHE B CE1  1 
ATOM   3333 C  CE2  . PHE B 1 213 ? -8.818  -8.193  34.686  1.00 46.76  ?  215 PHE B CE2  1 
ATOM   3334 C  CZ   . PHE B 1 213 ? -9.660  -7.115  34.649  1.00 47.39  ?  215 PHE B CZ   1 
ATOM   3335 N  N    . VAL B 1 214 ? -12.788 -12.901 37.714  1.00 47.53  ?  216 VAL B N    1 
ATOM   3336 C  CA   . VAL B 1 214 ? -13.156 -14.297 37.937  1.00 50.23  ?  216 VAL B CA   1 
ATOM   3337 C  C    . VAL B 1 214 ? -13.922 -14.808 36.702  1.00 50.36  ?  216 VAL B C    1 
ATOM   3338 O  O    . VAL B 1 214 ? -14.649 -14.048 36.094  1.00 49.44  ?  216 VAL B O    1 
ATOM   3339 C  CB   . VAL B 1 214 ? -14.003 -14.427 39.239  1.00 52.28  ?  216 VAL B CB   1 
ATOM   3340 C  CG1  . VAL B 1 214 ? -14.693 -15.785 39.315  1.00 54.85  ?  216 VAL B CG1  1 
ATOM   3341 C  CG2  . VAL B 1 214 ? -13.144 -14.191 40.476  1.00 52.77  ?  216 VAL B CG2  1 
ATOM   3342 N  N    . VAL B 1 215 ? -13.745 -16.084 36.349  1.00 51.86  ?  217 VAL B N    1 
ATOM   3343 C  CA   . VAL B 1 215 ? -14.588 -16.761 35.358  1.00 52.90  ?  217 VAL B CA   1 
ATOM   3344 C  C    . VAL B 1 215 ? -14.923 -18.165 35.849  1.00 54.28  ?  217 VAL B C    1 
ATOM   3345 O  O    . VAL B 1 215 ? -15.903 -18.753 35.334  1.00 55.76  ?  217 VAL B O    1 
ATOM   3346 C  CB   . VAL B 1 215 ? -13.961 -16.813 33.927  1.00 53.48  ?  217 VAL B CB   1 
ATOM   3347 C  CG1  . VAL B 1 215 ? -13.692 -15.426 33.391  1.00 53.76  ?  217 VAL B CG1  1 
ATOM   3348 C  CG2  . VAL B 1 215 ? -12.711 -17.675 33.892  1.00 54.10  ?  217 VAL B CG2  1 
ATOM   3349 O  OXT  . VAL B 1 215 ? -14.222 -18.672 36.747  1.00 56.40  ?  217 VAL B OXT  1 
HETATM 3350 C  C2   . W4U C 2 .   ? 20.563  -2.187  10.658  0.69 47.15  ?  301 W4U A C2   1 
HETATM 3351 C  C5   . W4U C 2 .   ? 21.739  -3.362  8.718   0.69 44.56  ?  301 W4U A C5   1 
HETATM 3352 C  C6   . W4U C 2 .   ? 22.778  -4.507  8.676   0.69 44.86  ?  301 W4U A C6   1 
HETATM 3353 C  C7   . W4U C 2 .   ? 22.672  -5.222  10.006  0.69 44.49  ?  301 W4U A C7   1 
HETATM 3354 C  C8   . W4U C 2 .   ? 22.003  -4.217  10.925  0.69 45.39  ?  301 W4U A C8   1 
HETATM 3355 C  C10  . W4U C 2 .   ? 19.409  -5.573  10.457  0.69 42.95  ?  301 W4U A C10  1 
HETATM 3356 C  C11  . W4U C 2 .   ? 18.221  -6.249  10.261  0.69 43.04  ?  301 W4U A C11  1 
HETATM 3357 C  C12  . W4U C 2 .   ? 17.252  -5.693  9.461   0.69 43.54  ?  301 W4U A C12  1 
HETATM 3358 C  C14  . W4U C 2 .   ? 17.452  -4.484  8.849   0.69 42.85  ?  301 W4U A C14  1 
HETATM 3359 C  C15  . W4U C 2 .   ? 18.640  -3.814  9.031   0.69 42.83  ?  301 W4U A C15  1 
HETATM 3360 O  O1   . W4U C 2 .   ? 20.372  -2.216  11.881  0.69 47.97  -1 301 W4U A O1   1 
HETATM 3361 O  O3   . W4U C 2 .   ? 20.471  -1.166  9.932   0.69 47.61  ?  301 W4U A O3   1 
HETATM 3362 C  C4   . W4U C 2 .   ? 20.940  -3.557  10.024  0.69 45.27  ?  301 W4U A C4   1 
HETATM 3363 C  C9   . W4U C 2 .   ? 19.639  -4.348  9.834   0.69 43.53  ?  301 W4U A C9   1 
HETATM 3364 CL CL13 . W4U C 2 .   ? 15.750  -6.540  9.214   0.69 44.79  ?  301 W4U A CL13 1 
HETATM 3365 H  H16  . W4U C 2 .   ? 21.144  -3.408  7.943   0.69 44.54  ?  301 W4U A H16  1 
HETATM 3366 H  H17  . W4U C 2 .   ? 22.186  -2.493  8.717   0.69 44.56  ?  301 W4U A H17  1 
HETATM 3367 H  H19  . W4U C 2 .   ? 23.680  -4.147  8.551   0.69 44.86  ?  301 W4U A H19  1 
HETATM 3368 H  H18  . W4U C 2 .   ? 22.580  -5.124  7.939   0.69 44.88  ?  301 W4U A H18  1 
HETATM 3369 H  H21  . W4U C 2 .   ? 23.558  -5.464  10.342  0.69 44.47  ?  301 W4U A H21  1 
HETATM 3370 H  H20  . W4U C 2 .   ? 22.131  -6.032  9.923   0.69 44.45  ?  301 W4U A H20  1 
HETATM 3371 H  H22  . W4U C 2 .   ? 22.647  -3.554  11.250  0.69 45.39  ?  301 W4U A H22  1 
HETATM 3372 H  H23  . W4U C 2 .   ? 21.587  -4.661  11.692  0.69 45.37  ?  301 W4U A H23  1 
HETATM 3373 H  H24  . W4U C 2 .   ? 20.084  -5.956  11.012  0.69 42.96  ?  301 W4U A H24  1 
HETATM 3374 H  H25  . W4U C 2 .   ? 18.070  -7.091  10.685  0.69 43.01  ?  301 W4U A H25  1 
HETATM 3375 H  H26  . W4U C 2 .   ? 16.773  -4.113  8.289   0.69 42.85  ?  301 W4U A H26  1 
HETATM 3376 H  H27  . W4U C 2 .   ? 18.778  -2.972  8.602   0.69 42.83  ?  301 W4U A H27  1 
HETATM 3377 C  C1   . PGE D 3 .   ? 3.406   -9.932  25.139  1.00 60.15  ?  301 PGE B C1   1 
HETATM 3378 O  O1   . PGE D 3 .   ? 3.393   -8.604  24.590  1.00 61.18  ?  301 PGE B O1   1 
HETATM 3379 C  C2   . PGE D 3 .   ? 4.081   -10.864 24.200  1.00 59.50  ?  301 PGE B C2   1 
HETATM 3380 O  O2   . PGE D 3 .   ? 5.396   -10.398 23.932  1.00 59.15  ?  301 PGE B O2   1 
HETATM 3381 C  C3   . PGE D 3 .   ? 5.990   -10.981 22.780  1.00 58.38  ?  301 PGE B C3   1 
HETATM 3382 C  C4   . PGE D 3 .   ? 7.424   -11.328 23.036  1.00 57.58  ?  301 PGE B C4   1 
HETATM 3383 O  O4   . PGE D 3 .   ? 10.575  -8.309  24.654  1.00 59.37  ?  301 PGE B O4   1 
HETATM 3384 C  C6   . PGE D 3 .   ? 10.097  -8.931  23.440  1.00 59.00  ?  301 PGE B C6   1 
HETATM 3385 C  C5   . PGE D 3 .   ? 9.489   -10.305 23.673  1.00 57.93  ?  301 PGE B C5   1 
HETATM 3386 O  O3   . PGE D 3 .   ? 8.079   -10.195 23.570  1.00 57.40  ?  301 PGE B O3   1 
HETATM 3387 C  C2   . W4U E 2 .   ? 6.473   -33.599 34.331  0.76 47.79  ?  302 W4U B C2   1 
HETATM 3388 C  C5   . W4U E 2 .   ? 4.390   -32.216 34.585  0.76 45.98  ?  302 W4U B C5   1 
HETATM 3389 C  C6   . W4U E 2 .   ? 4.052   -30.940 35.330  0.76 46.17  ?  302 W4U B C6   1 
HETATM 3390 C  C7   . W4U E 2 .   ? 5.383   -30.444 35.942  0.76 46.35  ?  302 W4U B C7   1 
HETATM 3391 C  C8   . W4U E 2 .   ? 6.366   -31.534 35.701  0.76 46.68  ?  302 W4U B C8   1 
HETATM 3392 C  C10  . W4U E 2 .   ? 7.163   -30.294 33.102  0.76 41.02  ?  302 W4U B C10  1 
HETATM 3393 C  C11  . W4U E 2 .   ? 7.608   -29.720 31.923  0.76 41.43  ?  302 W4U B C11  1 
HETATM 3394 C  C12  . W4U E 2 .   ? 7.316   -30.333 30.727  0.76 42.85  ?  302 W4U B C12  1 
HETATM 3395 C  C14  . W4U E 2 .   ? 6.592   -31.496 30.683  0.76 41.68  ?  302 W4U B C14  1 
HETATM 3396 C  C15  . W4U E 2 .   ? 6.146   -32.067 31.856  0.76 41.44  ?  302 W4U B C15  1 
HETATM 3397 O  O1   . W4U E 2 .   ? 7.704   -33.717 34.465  0.76 48.71  ?  302 W4U B O1   1 
HETATM 3398 O  O3   . W4U E 2 .   ? 5.653   -34.520 34.168  0.76 48.87  -1 302 W4U B O3   1 
HETATM 3399 C  C4   . W4U E 2 .   ? 5.919   -32.157 34.368  0.76 45.80  ?  302 W4U B C4   1 
HETATM 3400 C  C9   . W4U E 2 .   ? 6.410   -31.466 33.082  0.76 42.42  ?  302 W4U B C9   1 
HETATM 3401 CL CL13 . W4U E 2 .   ? 7.867   -29.618 29.242  0.76 45.62  ?  302 W4U B CL13 1 
HETATM 3402 H  H16  . W4U E 2 .   ? 3.919   -32.255 33.726  0.76 45.97  ?  302 W4U B H16  1 
HETATM 3403 H  H17  . W4U E 2 .   ? 4.145   -33.001 35.115  0.76 45.97  ?  302 W4U B H17  1 
HETATM 3404 H  H19  . W4U E 2 .   ? 3.394   -31.117 36.031  0.76 46.17  ?  302 W4U B H19  1 
HETATM 3405 H  H18  . W4U E 2 .   ? 3.685   -30.271 34.716  0.76 46.17  ?  302 W4U B H18  1 
HETATM 3406 H  H21  . W4U E 2 .   ? 5.280   -30.280 36.901  0.76 46.35  ?  302 W4U B H21  1 
HETATM 3407 H  H20  . W4U E 2 .   ? 5.674   -29.616 35.510  0.76 46.34  ?  302 W4U B H20  1 
HETATM 3408 H  H22  . W4U E 2 .   ? 6.337   -32.196 36.422  0.76 46.70  ?  302 W4U B H22  1 
HETATM 3409 H  H23  . W4U E 2 .   ? 7.275   -31.178 35.634  0.76 46.69  ?  302 W4U B H23  1 
HETATM 3410 H  H24  . W4U E 2 .   ? 7.364   -29.875 33.935  0.76 41.02  ?  302 W4U B H24  1 
HETATM 3411 H  H25  . W4U E 2 .   ? 8.112   -28.909 31.940  0.76 41.37  ?  302 W4U B H25  1 
HETATM 3412 H  H26  . W4U E 2 .   ? 6.392   -31.904 29.844  0.76 41.68  ?  302 W4U B H26  1 
HETATM 3413 H  H27  . W4U E 2 .   ? 5.638   -32.876 31.826  0.76 41.42  ?  302 W4U B H27  1 
HETATM 3414 O  O    . HOH F 4 .   ? 29.033  -8.598  -10.056 1.00 61.85  ?  401 HOH A O    1 
HETATM 3415 O  O    . HOH F 4 .   ? 35.360  -10.625 10.768  1.00 64.60  ?  402 HOH A O    1 
HETATM 3416 O  O    . HOH F 4 .   ? 13.611  -22.639 17.815  1.00 34.73  ?  403 HOH A O    1 
HETATM 3417 O  O    . HOH F 4 .   ? 5.274   -1.193  2.190   1.00 61.82  ?  404 HOH A O    1 
HETATM 3418 O  O    . HOH F 4 .   ? 22.455  -26.435 -1.462  1.00 28.95  ?  405 HOH A O    1 
HETATM 3419 O  O    . HOH F 4 .   ? 25.754  0.471   2.555   1.00 30.79  ?  406 HOH A O    1 
HETATM 3420 O  O    . HOH F 4 .   ? 20.377  -0.581  7.482   1.00 69.40  ?  407 HOH A O    1 
HETATM 3421 O  O    . HOH F 4 .   ? 12.253  -21.382 -1.904  1.00 40.60  ?  408 HOH A O    1 
HETATM 3422 O  O    . HOH F 4 .   ? 16.665  -28.523 -2.213  1.00 65.65  ?  409 HOH A O    1 
HETATM 3423 O  O    . HOH F 4 .   ? 18.886  -8.025  -4.419  1.00 36.78  ?  410 HOH A O    1 
HETATM 3424 O  O    . HOH F 4 .   ? 3.200   -11.533 7.143   1.00 38.33  ?  411 HOH A O    1 
HETATM 3425 O  O    . HOH F 4 .   ? 6.954   -9.714  10.940  1.00 54.45  ?  412 HOH A O    1 
HETATM 3426 O  O    . HOH F 4 .   ? 13.294  -27.621 -5.932  1.00 67.51  ?  413 HOH A O    1 
HETATM 3427 O  O    . HOH F 4 .   ? -6.838  -5.278  -2.204  1.00 49.84  ?  414 HOH A O    1 
HETATM 3428 O  O    . HOH F 4 .   ? 5.275   -2.018  4.683   1.00 51.18  ?  415 HOH A O    1 
HETATM 3429 O  O    . HOH F 4 .   ? 13.658  -19.600 10.935  1.00 25.43  ?  416 HOH A O    1 
HETATM 3430 O  O    . HOH F 4 .   ? 12.640  -5.245  -13.407 1.00 70.39  ?  417 HOH A O    1 
HETATM 3431 O  O    . HOH F 4 .   ? 27.763  -14.266 8.014   1.00 28.41  ?  418 HOH A O    1 
HETATM 3432 O  O    . HOH F 4 .   ? 18.999  -30.762 2.829   1.00 48.86  ?  419 HOH A O    1 
HETATM 3433 O  O    . HOH F 4 .   ? 7.099   -18.142 -11.455 1.00 48.04  ?  420 HOH A O    1 
HETATM 3434 O  O    . HOH F 4 .   ? 13.276  -23.664 -14.119 1.00 68.77  ?  421 HOH A O    1 
HETATM 3435 O  O    . HOH F 4 .   ? 26.560  0.668   5.696   1.00 45.79  ?  422 HOH A O    1 
HETATM 3436 O  O    . HOH F 4 .   ? 34.270  -26.242 2.191   1.00 37.95  ?  423 HOH A O    1 
HETATM 3437 O  O    . HOH F 4 .   ? 8.450   -14.683 -3.169  1.00 28.25  ?  424 HOH A O    1 
HETATM 3438 O  O    . HOH F 4 .   ? 17.445  -13.739 -10.642 1.00 45.85  ?  425 HOH A O    1 
HETATM 3439 O  O    . HOH F 4 .   ? 9.739   -22.732 5.591   1.00 42.69  ?  426 HOH A O    1 
HETATM 3440 O  O    . HOH F 4 .   ? 20.375  -2.958  5.579   1.00 37.93  ?  427 HOH A O    1 
HETATM 3441 O  O    . HOH F 4 .   ? 12.318  -24.103 0.439   1.00 47.17  ?  428 HOH A O    1 
HETATM 3442 O  O    . HOH F 4 .   ? 30.318  -16.102 10.789  1.00 57.76  ?  429 HOH A O    1 
HETATM 3443 O  O    . HOH F 4 .   ? 28.186  -13.487 -11.188 1.00 40.93  ?  430 HOH A O    1 
HETATM 3444 O  O    . HOH F 4 .   ? 21.030  2.197   8.290   1.00 51.13  ?  431 HOH A O    1 
HETATM 3445 O  O    . HOH F 4 .   ? 23.037  -15.518 15.247  1.00 45.96  ?  432 HOH A O    1 
HETATM 3446 O  O    . HOH F 4 .   ? 20.172  1.557   10.494  1.00 56.20  ?  433 HOH A O    1 
HETATM 3447 O  O    . HOH F 4 .   ? 10.697  -29.501 4.897   1.00 64.86  ?  434 HOH A O    1 
HETATM 3448 O  O    . HOH F 4 .   ? -11.485 -10.969 1.566   1.00 56.21  ?  435 HOH A O    1 
HETATM 3449 O  O    . HOH F 4 .   ? 23.002  -24.060 5.671   1.00 27.06  ?  436 HOH A O    1 
HETATM 3450 O  O    . HOH F 4 .   ? 26.329  -23.573 15.807  1.00 60.59  ?  437 HOH A O    1 
HETATM 3451 O  O    . HOH F 4 .   ? 18.452  -20.442 21.684  1.00 41.44  ?  438 HOH A O    1 
HETATM 3452 O  O    . HOH F 4 .   ? 14.676  -10.045 -5.435  1.00 34.17  ?  439 HOH A O    1 
HETATM 3453 O  O    . HOH F 4 .   ? 28.521  3.227   -0.061  1.00 47.45  ?  440 HOH A O    1 
HETATM 3454 O  O    . HOH F 4 .   ? 32.672  -30.217 1.132   1.00 58.81  ?  441 HOH A O    1 
HETATM 3455 O  O    . HOH F 4 .   ? 29.442  -33.550 1.944   1.00 52.76  ?  442 HOH A O    1 
HETATM 3456 O  O    . HOH F 4 .   ? 28.328  -29.310 5.949   1.00 34.43  ?  443 HOH A O    1 
HETATM 3457 O  O    . HOH F 4 .   ? 30.287  -22.704 6.179   1.00 41.27  ?  444 HOH A O    1 
HETATM 3458 O  O    . HOH F 4 .   ? 20.705  -6.072  -7.100  1.00 44.65  ?  445 HOH A O    1 
HETATM 3459 O  O    . HOH F 4 .   ? 27.393  -17.072 8.432   1.00 26.97  ?  446 HOH A O    1 
HETATM 3460 O  O    . HOH F 4 .   ? 9.998   -16.032 -0.358  1.00 29.02  ?  447 HOH A O    1 
HETATM 3461 O  O    . HOH F 4 .   ? 21.553  -30.026 5.588   1.00 35.35  ?  448 HOH A O    1 
HETATM 3462 O  O    . HOH F 4 .   ? 18.701  -28.505 -5.803  1.00 59.97  ?  449 HOH A O    1 
HETATM 3463 O  O    . HOH F 4 .   ? 23.223  -37.639 5.771   1.00 51.43  ?  450 HOH A O    1 
HETATM 3464 O  O    . HOH F 4 .   ? 14.350  -16.406 -9.869  1.00 48.83  ?  451 HOH A O    1 
HETATM 3465 O  O    . HOH F 4 .   ? 17.895  -17.203 -11.082 1.00 45.58  ?  452 HOH A O    1 
HETATM 3466 O  O    . HOH F 4 .   ? 14.422  -11.868 -8.201  1.00 40.88  ?  453 HOH A O    1 
HETATM 3467 O  O    . HOH F 4 .   ? 12.165  -26.026 5.273   1.00 50.60  ?  454 HOH A O    1 
HETATM 3468 O  O    . HOH F 4 .   ? 7.739   0.094   10.225  1.00 55.85  ?  455 HOH A O    1 
HETATM 3469 O  O    . HOH F 4 .   ? 17.096  -29.952 13.277  1.00 48.90  ?  456 HOH A O    1 
HETATM 3470 O  O    . HOH F 4 .   ? 2.008   -11.906 -6.111  1.00 50.31  ?  457 HOH A O    1 
HETATM 3471 O  O    . HOH F 4 .   ? 13.916  -26.132 13.491  1.00 58.99  ?  458 HOH A O    1 
HETATM 3472 O  O    . HOH F 4 .   ? 21.077  -14.394 14.468  1.00 42.60  ?  459 HOH A O    1 
HETATM 3473 O  O    . HOH F 4 .   ? 14.864  -5.230  -10.669 1.00 42.92  ?  460 HOH A O    1 
HETATM 3474 O  O    . HOH F 4 .   ? 3.513   -20.731 -4.878  1.00 56.38  ?  461 HOH A O    1 
HETATM 3475 O  O    . HOH F 4 .   ? 16.328  -7.644  -9.662  1.00 44.40  ?  462 HOH A O    1 
HETATM 3476 O  O    . HOH F 4 .   ? 6.172   -7.325  10.146  1.00 60.00  ?  463 HOH A O    1 
HETATM 3477 O  O    . HOH F 4 .   ? 16.186  -17.331 -2.620  1.00 33.25  ?  464 HOH A O    1 
HETATM 3478 O  O    . HOH F 4 .   ? 20.529  -33.454 6.733   1.00 53.58  ?  465 HOH A O    1 
HETATM 3479 O  O    . HOH F 4 .   ? 19.358  -36.712 9.267   1.00 60.56  ?  466 HOH A O    1 
HETATM 3480 O  O    . HOH F 4 .   ? 22.430  -29.177 -7.784  1.00 47.96  ?  467 HOH A O    1 
HETATM 3481 O  O    . HOH F 4 .   ? 27.248  -0.379  -1.284  1.00 54.80  ?  468 HOH A O    1 
HETATM 3482 O  O    . HOH F 4 .   ? 14.457  -18.491 -1.032  1.00 37.22  ?  469 HOH A O    1 
HETATM 3483 O  O    . HOH F 4 .   ? 23.086  3.608   8.916   1.00 45.55  ?  470 HOH A O    1 
HETATM 3484 O  O    . HOH F 4 .   ? 2.689   -4.209  8.230   1.00 62.08  ?  471 HOH A O    1 
HETATM 3485 O  O    . HOH F 4 .   ? 17.380  -22.554 -12.752 1.00 68.56  ?  472 HOH A O    1 
HETATM 3486 O  O    . HOH F 4 .   ? 28.982  -21.784 9.466   1.00 56.07  ?  473 HOH A O    1 
HETATM 3487 O  O    . HOH F 4 .   ? 34.182  -23.224 -8.418  1.00 54.65  ?  474 HOH A O    1 
HETATM 3488 O  O    . HOH F 4 .   ? 11.869  0.632   -7.655  1.00 47.92  ?  475 HOH A O    1 
HETATM 3489 O  O    . HOH F 4 .   ? 5.495   -12.727 13.974  1.00 53.52  ?  476 HOH A O    1 
HETATM 3490 O  O    . HOH F 4 .   ? 26.146  -22.328 13.855  1.00 37.21  ?  477 HOH A O    1 
HETATM 3491 O  O    . HOH F 4 .   ? -3.581  -4.946  6.910   1.00 75.84  ?  478 HOH A O    1 
HETATM 3492 O  O    . HOH F 4 .   ? 21.148  -22.269 28.110  1.00 62.83  ?  479 HOH A O    1 
HETATM 3493 O  O    . HOH F 4 .   ? 17.276  -5.660  17.902  1.00 70.84  ?  480 HOH A O    1 
HETATM 3494 O  O    . HOH F 4 .   ? 26.045  -16.862 12.856  1.00 50.68  ?  481 HOH A O    1 
HETATM 3495 O  O    . HOH F 4 .   ? 14.408  0.778   -7.958  1.00 51.42  ?  482 HOH A O    1 
HETATM 3496 O  O    . HOH F 4 .   ? 25.622  -19.890 14.073  1.00 50.45  ?  483 HOH A O    1 
HETATM 3497 O  O    . HOH F 4 .   ? -1.406  -3.395  1.484   1.00 71.22  ?  484 HOH A O    1 
HETATM 3498 O  O    . HOH F 4 .   ? 18.421  2.878   -4.603  1.00 45.79  ?  485 HOH A O    1 
HETATM 3499 O  O    . HOH F 4 .   ? 27.478  -17.401 10.901  1.00 44.30  ?  486 HOH A O    1 
HETATM 3500 O  O    . HOH F 4 .   ? 15.557  -27.694 1.958   1.00 52.03  ?  487 HOH A O    1 
HETATM 3501 O  O    . HOH F 4 .   ? -0.291  -3.058  -5.823  1.00 68.70  ?  488 HOH A O    1 
HETATM 3502 O  O    . HOH F 4 .   ? 22.999  -24.124 24.590  1.00 70.01  ?  489 HOH A O    1 
HETATM 3503 O  O    . HOH F 4 .   ? -1.587  -9.498  -4.724  1.00 66.34  ?  490 HOH A O    1 
HETATM 3504 O  O    . HOH F 4 .   ? 29.685  -13.509 19.515  1.00 56.05  ?  491 HOH A O    1 
HETATM 3505 O  O    . HOH F 4 .   ? 2.892   -18.711 3.615   1.00 57.19  ?  492 HOH A O    1 
HETATM 3506 O  O    . HOH F 4 .   ? 29.124  -10.662 -11.466 1.00 51.90  ?  493 HOH A O    1 
HETATM 3507 O  O    . HOH F 4 .   ? 29.699  -23.463 11.333  1.00 62.38  ?  494 HOH A O    1 
HETATM 3508 O  O    . HOH F 4 .   ? 27.256  -1.399  -3.458  1.00 51.48  ?  495 HOH A O    1 
HETATM 3509 O  O    . HOH F 4 .   ? 35.896  -11.715 13.207  1.00 62.89  ?  496 HOH A O    1 
HETATM 3510 O  O    . HOH F 4 .   ? 26.538  -17.086 32.579  1.00 75.75  ?  497 HOH A O    1 
HETATM 3511 O  O    . HOH F 4 .   ? 24.283  -27.593 20.497  1.00 73.93  ?  498 HOH A O    1 
HETATM 3512 O  O    . HOH G 4 .   ? -10.380 -18.035 21.056  1.00 43.25  ?  401 HOH B O    1 
HETATM 3513 O  O    . HOH G 4 .   ? 4.112   -39.856 22.011  1.00 56.13  ?  402 HOH B O    1 
HETATM 3514 O  O    . HOH G 4 .   ? -3.444  -2.023  37.281  1.00 45.19  ?  403 HOH B O    1 
HETATM 3515 O  O    . HOH G 4 .   ? -5.566  -27.672 25.402  1.00 39.02  ?  404 HOH B O    1 
HETATM 3516 O  O    . HOH G 4 .   ? 11.412  -16.854 27.637  1.00 30.05  ?  405 HOH B O    1 
HETATM 3517 O  O    . HOH G 4 .   ? 12.954  -23.201 13.776  1.00 46.89  ?  406 HOH B O    1 
HETATM 3518 O  O    . HOH G 4 .   ? 11.060  -9.259  27.814  1.00 42.14  ?  407 HOH B O    1 
HETATM 3519 O  O    . HOH G 4 .   ? 12.048  -25.680 42.362  1.00 43.87  ?  408 HOH B O    1 
HETATM 3520 O  O    . HOH G 4 .   ? 18.296  -14.768 36.267  1.00 53.80  ?  409 HOH B O    1 
HETATM 3521 O  O    . HOH G 4 .   ? -10.767 -26.544 16.096  1.00 54.74  ?  410 HOH B O    1 
HETATM 3522 O  O    . HOH G 4 .   ? 11.272  -32.155 38.588  1.00 54.22  ?  411 HOH B O    1 
HETATM 3523 O  O    . HOH G 4 .   ? 11.685  -20.778 12.476  1.00 34.36  ?  412 HOH B O    1 
HETATM 3524 O  O    . HOH G 4 .   ? -3.177  -8.956  29.471  1.00 32.95  ?  413 HOH B O    1 
HETATM 3525 O  O    . HOH G 4 .   ? 0.863   -14.627 20.347  1.00 43.58  ?  414 HOH B O    1 
HETATM 3526 O  O    . HOH G 4 .   ? 12.111  -25.600 17.061  1.00 34.49  ?  415 HOH B O    1 
HETATM 3527 O  O    . HOH G 4 .   ? -1.515  -2.441  34.584  1.00 51.25  ?  416 HOH B O    1 
HETATM 3528 O  O    . HOH G 4 .   ? 13.701  -27.585 22.196  1.00 50.32  ?  417 HOH B O    1 
HETATM 3529 O  O    . HOH G 4 .   ? -2.563  -8.042  19.068  1.00 67.70  ?  418 HOH B O    1 
HETATM 3530 O  O    . HOH G 4 .   ? -3.260  -35.792 34.926  1.00 53.81  ?  419 HOH B O    1 
HETATM 3531 O  O    . HOH G 4 .   ? -8.059  -19.209 40.853  1.00 47.34  ?  420 HOH B O    1 
HETATM 3532 O  O    . HOH G 4 .   ? -6.092  -1.660  26.281  1.00 52.59  ?  421 HOH B O    1 
HETATM 3533 O  O    . HOH G 4 .   ? -6.198  -23.756 19.571  1.00 41.98  ?  422 HOH B O    1 
HETATM 3534 O  O    . HOH G 4 .   ? 14.476  -15.017 45.722  1.00 59.41  ?  423 HOH B O    1 
HETATM 3535 O  O    . HOH G 4 .   ? 8.885   -13.741 21.343  1.00 45.38  ?  424 HOH B O    1 
HETATM 3536 O  O    . HOH G 4 .   ? 2.093   -33.022 31.593  1.00 40.84  ?  425 HOH B O    1 
HETATM 3537 O  O    . HOH G 4 .   ? 22.752  -18.147 51.386  1.00 57.70  ?  426 HOH B O    1 
HETATM 3538 O  O    . HOH G 4 .   ? 3.545   -38.644 35.408  1.00 49.64  ?  427 HOH B O    1 
HETATM 3539 O  O    . HOH G 4 .   ? -5.657  -35.947 17.244  1.00 50.69  ?  428 HOH B O    1 
HETATM 3540 O  O    . HOH G 4 .   ? 3.675   -5.934  31.624  1.00 38.76  ?  429 HOH B O    1 
HETATM 3541 O  O    . HOH G 4 .   ? -0.342  -11.818 47.969  1.00 64.22  ?  430 HOH B O    1 
HETATM 3542 O  O    . HOH G 4 .   ? -5.256  -9.003  41.791  1.00 33.77  ?  431 HOH B O    1 
HETATM 3543 O  O    . HOH G 4 .   ? -0.053  -12.773 39.995  1.00 35.37  ?  432 HOH B O    1 
HETATM 3544 O  O    . HOH G 4 .   ? -7.320  -18.938 18.521  1.00 46.25  ?  433 HOH B O    1 
HETATM 3545 O  O    . HOH G 4 .   ? 8.145   -18.422 36.622  1.00 41.60  ?  434 HOH B O    1 
HETATM 3546 O  O    . HOH G 4 .   ? 3.226   -12.188 21.209  1.00 43.30  ?  435 HOH B O    1 
HETATM 3547 O  O    . HOH G 4 .   ? 12.057  -36.821 23.182  1.00 50.33  ?  436 HOH B O    1 
HETATM 3548 O  O    . HOH G 4 .   ? 2.492   -18.483 38.580  1.00 33.81  ?  437 HOH B O    1 
HETATM 3549 O  O    . HOH G 4 .   ? -13.616 -10.640 26.331  1.00 56.94  ?  438 HOH B O    1 
HETATM 3550 O  O    . HOH G 4 .   ? 1.686   -21.403 38.731  1.00 29.96  ?  439 HOH B O    1 
HETATM 3551 O  O    . HOH G 4 .   ? 2.834   -20.137 19.112  1.00 30.03  ?  440 HOH B O    1 
HETATM 3552 O  O    . HOH G 4 .   ? 1.109   -6.250  37.829  1.00 38.17  ?  441 HOH B O    1 
HETATM 3553 O  O    . HOH G 4 .   ? 23.002  -18.109 39.104  1.00 66.99  ?  442 HOH B O    1 
HETATM 3554 O  O    . HOH G 4 .   ? -4.380  -25.531 20.841  1.00 35.52  ?  443 HOH B O    1 
HETATM 3555 O  O    . HOH G 4 .   ? 2.836   -11.781 33.189  1.00 30.60  ?  444 HOH B O    1 
HETATM 3556 O  O    . HOH G 4 .   ? 1.320   -21.503 16.557  1.00 27.02  ?  445 HOH B O    1 
HETATM 3557 O  O    . HOH G 4 .   ? 3.358   -35.097 32.677  1.00 59.10  ?  446 HOH B O    1 
HETATM 3558 O  O    . HOH G 4 .   ? 13.048  -29.914 21.064  1.00 41.45  ?  447 HOH B O    1 
HETATM 3559 O  O    . HOH G 4 .   ? -9.744  -21.679 20.662  1.00 50.28  ?  448 HOH B O    1 
HETATM 3560 O  O    . HOH G 4 .   ? 1.022   -17.706 -1.381  1.00 69.11  ?  449 HOH B O    1 
HETATM 3561 O  O    . HOH G 4 .   ? 8.796   -13.371 39.667  1.00 40.17  ?  450 HOH B O    1 
HETATM 3562 O  O    . HOH G 4 .   ? 6.919   -14.611 16.319  1.00 61.09  ?  451 HOH B O    1 
HETATM 3563 O  O    . HOH G 4 .   ? 7.884   -20.669 39.646  1.00 53.39  ?  452 HOH B O    1 
HETATM 3564 O  O    . HOH G 4 .   ? 20.407  -21.270 31.882  1.00 45.86  ?  453 HOH B O    1 
HETATM 3565 O  O    . HOH G 4 .   ? 8.212   -34.964 17.913  1.00 46.33  ?  454 HOH B O    1 
HETATM 3566 O  O    . HOH G 4 .   ? -7.441  -5.894  42.100  1.00 68.98  ?  455 HOH B O    1 
HETATM 3567 O  O    . HOH G 4 .   ? -1.377  -11.829 50.355  1.00 48.68  ?  456 HOH B O    1 
HETATM 3568 O  O    . HOH G 4 .   ? 1.264   -24.999 9.410   1.00 54.85  ?  457 HOH B O    1 
HETATM 3569 O  O    . HOH G 4 .   ? 13.741  -16.274 26.266  1.00 39.99  ?  458 HOH B O    1 
HETATM 3570 O  O    . HOH G 4 .   ? 9.811   -38.283 21.274  1.00 71.93  ?  459 HOH B O    1 
HETATM 3571 O  O    . HOH G 4 .   ? -8.667  -5.885  26.460  1.00 52.50  ?  460 HOH B O    1 
HETATM 3572 O  O    . HOH G 4 .   ? -9.320  -30.015 18.662  1.00 43.12  ?  461 HOH B O    1 
HETATM 3573 O  O    . HOH G 4 .   ? 15.044  -22.757 45.494  1.00 64.12  ?  462 HOH B O    1 
HETATM 3574 O  O    . HOH G 4 .   ? 8.825   -15.447 18.940  1.00 47.75  ?  463 HOH B O    1 
HETATM 3575 O  O    . HOH G 4 .   ? -8.348  -22.733 40.841  1.00 56.58  ?  464 HOH B O    1 
HETATM 3576 O  O    . HOH G 4 .   ? -1.723  -18.311 23.299  1.00 37.36  ?  465 HOH B O    1 
HETATM 3577 O  O    . HOH G 4 .   ? 0.304   -17.260 22.568  1.00 46.52  ?  466 HOH B O    1 
HETATM 3578 O  O    . HOH G 4 .   ? -15.281 -17.863 24.387  1.00 59.90  ?  467 HOH B O    1 
HETATM 3579 O  O    . HOH G 4 .   ? -0.326  -7.584  23.519  1.00 64.86  ?  468 HOH B O    1 
HETATM 3580 O  O    . HOH G 4 .   ? 14.514  -26.781 18.929  1.00 70.42  ?  469 HOH B O    1 
HETATM 3581 O  O    . HOH G 4 .   ? -9.103  -27.703 20.441  1.00 45.27  ?  470 HOH B O    1 
HETATM 3582 O  O    . HOH G 4 .   ? -10.265 -23.449 22.298  1.00 55.05  ?  471 HOH B O    1 
HETATM 3583 O  O    . HOH G 4 .   ? -4.018  -8.528  21.989  1.00 59.58  ?  472 HOH B O    1 
HETATM 3584 O  O    . HOH G 4 .   ? 10.631  -25.711 46.619  1.00 72.68  ?  473 HOH B O    1 
HETATM 3585 O  O    . HOH G 4 .   ? -14.361 -22.723 43.012  1.00 66.51  ?  474 HOH B O    1 
HETATM 3586 O  O    . HOH G 4 .   ? 3.294   -13.280 17.148  1.00 54.95  ?  475 HOH B O    1 
HETATM 3587 O  O    . HOH G 4 .   ? 15.051  -20.274 45.531  1.00 62.43  ?  476 HOH B O    1 
HETATM 3588 O  O    . HOH G 4 .   ? -5.517  -12.361 53.214  1.00 63.24  ?  477 HOH B O    1 
HETATM 3589 O  O    . HOH G 4 .   ? -5.357  -6.753  23.517  1.00 59.79  ?  478 HOH B O    1 
HETATM 3590 O  O    . HOH G 4 .   ? -9.128  -27.472 39.670  1.00 64.08  ?  479 HOH B O    1 
HETATM 3591 O  O    . HOH G 4 .   ? -14.825 -10.512 36.602  1.00 53.90  ?  480 HOH B O    1 
HETATM 3592 O  O    . HOH G 4 .   ? 1.281   -42.182 44.333  1.00 57.32  ?  481 HOH B O    1 
HETATM 3593 O  O    . HOH G 4 .   ? 4.776   -18.642 40.001  1.00 49.15  ?  482 HOH B O    1 
HETATM 3594 O  O    . HOH G 4 .   ? 18.473  -15.740 32.509  1.00 69.41  ?  483 HOH B O    1 
HETATM 3595 O  O    . HOH G 4 .   ? 19.417  -36.746 26.280  1.00 60.11  ?  484 HOH B O    1 
HETATM 3596 O  O    . HOH G 4 .   ? -5.013  -15.246 4.914   1.00 60.13  ?  485 HOH B O    1 
HETATM 3597 O  O    . HOH G 4 .   ? 11.355  -39.213 24.763  1.00 56.78  ?  486 HOH B O    1 
HETATM 3598 O  O    . HOH G 4 .   ? 7.492   -18.104 39.020  1.00 50.18  ?  487 HOH B O    1 
HETATM 3599 O  O    . HOH G 4 .   ? -10.004 -32.388 20.478  1.00 52.16  ?  488 HOH B O    1 
HETATM 3600 O  O    . HOH G 4 .   ? -0.404  -2.282  43.369  1.00 60.69  ?  489 HOH B O    1 
HETATM 3601 O  O    . HOH G 4 .   ? -19.850 -19.248 30.018  1.00 62.82  ?  490 HOH B O    1 
HETATM 3602 O  O    . HOH G 4 .   ? 17.675  -30.370 26.233  1.00 70.00  ?  491 HOH B O    1 
HETATM 3603 O  O    . HOH G 4 .   ? 15.166  -32.154 23.513  1.00 59.66  ?  492 HOH B O    1 
HETATM 3604 O  O    . HOH G 4 .   ? -2.032  -33.977 11.046  1.00 56.47  ?  493 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   ? 0.7121 0.7128 0.5870 -0.1215 -0.0462 0.0500  11  ALA A N   
2    C CA  . ALA A 9   ? 0.7103 0.7062 0.5836 -0.1097 -0.0367 0.0436  11  ALA A CA  
3    C C   . ALA A 9   ? 0.6778 0.6804 0.5701 -0.0994 -0.0274 0.0430  11  ALA A C   
4    O O   . ALA A 9   ? 0.6890 0.7074 0.5980 -0.1001 -0.0271 0.0495  11  ALA A O   
5    C CB  . ALA A 9   ? 0.7118 0.7223 0.5873 -0.1088 -0.0362 0.0497  11  ALA A CB  
6    N N   . ARG A 10  ? 0.6403 0.6318 0.5297 -0.0901 -0.0200 0.0354  12  ARG A N   
7    C CA  . ARG A 10  ? 0.5978 0.5926 0.5027 -0.0810 -0.0121 0.0334  12  ARG A CA  
8    C C   . ARG A 10  ? 0.5370 0.5516 0.4609 -0.0753 -0.0072 0.0398  12  ARG A C   
9    O O   . ARG A 10  ? 0.5138 0.5337 0.4366 -0.0741 -0.0067 0.0430  12  ARG A O   
10   C CB  . ARG A 10  ? 0.6284 0.6058 0.5242 -0.0735 -0.0065 0.0245  12  ARG A CB  
11   C CG  . ARG A 10  ? 0.6551 0.6330 0.5646 -0.0650 0.0005  0.0217  12  ARG A CG  
12   C CD  . ARG A 10  ? 0.6831 0.6450 0.5839 -0.0583 0.0054  0.0145  12  ARG A CD  
13   N NE  . ARG A 10  ? 0.6992 0.6418 0.5816 -0.0627 0.0010  0.0090  12  ARG A NE  
14   C CZ  . ARG A 10  ? 0.6858 0.6190 0.5676 -0.0647 -0.0012 0.0066  12  ARG A CZ  
15   N NH1 . ARG A 10  ? 0.6856 0.6281 0.5827 -0.0630 0.0008  0.0091  12  ARG A NH1 
16   N NH2 . ARG A 10  ? 0.6550 0.5689 0.5205 -0.0685 -0.0056 0.0017  12  ARG A NH2 
17   N N   . ILE A 11  ? 0.4951 0.5203 0.4360 -0.0715 -0.0038 0.0417  13  ILE A N   
18   C CA  . ILE A 11  ? 0.4694 0.5099 0.4292 -0.0644 0.0014  0.0460  13  ILE A CA  
19   C C   . ILE A 11  ? 0.4643 0.4964 0.4273 -0.0550 0.0084  0.0403  13  ILE A C   
20   O O   . ILE A 11  ? 0.4427 0.4689 0.4092 -0.0507 0.0118  0.0349  13  ILE A O   
21   C CB  . ILE A 11  ? 0.4382 0.4922 0.4135 -0.0630 0.0029  0.0489  13  ILE A CB  
22   C CG1 . ILE A 11  ? 0.4517 0.5157 0.4252 -0.0727 -0.0040 0.0560  13  ILE A CG1 
23   C CG2 . ILE A 11  ? 0.4290 0.4964 0.4231 -0.0554 0.0079  0.0526  13  ILE A CG2 
24   C CD1 . ILE A 11  ? 0.4513 0.5290 0.4377 -0.0715 -0.0021 0.0586  13  ILE A CD1 
25   N N   . ILE A 12  ? 0.4289 0.4625 0.3914 -0.0525 0.0100  0.0429  14  ILE A N   
26   C CA  . ILE A 12  ? 0.4412 0.4692 0.4077 -0.0447 0.0159  0.0398  14  ILE A CA  
27   C C   . ILE A 12  ? 0.4444 0.4856 0.4309 -0.0393 0.0190  0.0461  14  ILE A C   
28   O O   . ILE A 12  ? 0.4603 0.5125 0.4501 -0.0417 0.0167  0.0538  14  ILE A O   
29   C CB  . ILE A 12  ? 0.4564 0.4738 0.4047 -0.0454 0.0159  0.0374  14  ILE A CB  
30   C CG1 . ILE A 12  ? 0.4853 0.4867 0.4140 -0.0503 0.0124  0.0303  14  ILE A CG1 
31   C CG2 . ILE A 12  ? 0.4583 0.4723 0.4125 -0.0370 0.0225  0.0358  14  ILE A CG2 
32   C CD1 . ILE A 12  ? 0.5258 0.5165 0.4346 -0.0516 0.0115  0.0271  14  ILE A CD1 
33   N N   . TYR A 13  ? 0.4119 0.4517 0.4120 -0.0324 0.0236  0.0432  15  TYR A N   
34   C CA  . TYR A 13  ? 0.4150 0.4639 0.4350 -0.0269 0.0263  0.0482  15  TYR A CA  
35   C C   . TYR A 13  ? 0.4367 0.4787 0.4607 -0.0215 0.0301  0.0468  15  TYR A C   
36   O O   . TYR A 13  ? 0.4335 0.4657 0.4542 -0.0195 0.0320  0.0400  15  TYR A O   
37   C CB  . TYR A 13  ? 0.4169 0.4704 0.4520 -0.0233 0.0277  0.0459  15  TYR A CB  
38   C CG  . TYR A 13  ? 0.4219 0.4858 0.4579 -0.0271 0.0250  0.0486  15  TYR A CG  
39   C CD1 . TYR A 13  ? 0.4226 0.5002 0.4678 -0.0281 0.0234  0.0576  15  TYR A CD1 
40   C CD2 . TYR A 13  ? 0.4304 0.4920 0.4595 -0.0296 0.0242  0.0435  15  TYR A CD2 
41   C CE1 . TYR A 13  ? 0.4240 0.5133 0.4716 -0.0315 0.0211  0.0615  15  TYR A CE1 
42   C CE2 . TYR A 13  ? 0.4241 0.4975 0.4557 -0.0329 0.0221  0.0473  15  TYR A CE2 
43   C CZ  . TYR A 13  ? 0.4275 0.5151 0.4686 -0.0338 0.0207  0.0564  15  TYR A CZ  
44   O OH  . TYR A 13  ? 0.4376 0.5389 0.4825 -0.0372 0.0186  0.0617  15  TYR A OH  
45   N N   . ASP A 14  ? 0.4372 0.4858 0.4699 -0.0195 0.0311  0.0543  16  ASP A N   
46   C CA  . ASP A 14  ? 0.4414 0.4866 0.4820 -0.0146 0.0346  0.0553  16  ASP A CA  
47   C C   . ASP A 14  ? 0.4044 0.4500 0.4670 -0.0096 0.0358  0.0546  16  ASP A C   
48   O O   . ASP A 14  ? 0.3690 0.4193 0.4408 -0.0090 0.0347  0.0541  16  ASP A O   
49   C CB  . ASP A 14  ? 0.4792 0.5316 0.5185 -0.0149 0.0351  0.0644  16  ASP A CB  
50   C CG  . ASP A 14  ? 0.5581 0.6239 0.6110 -0.0155 0.0331  0.0748  16  ASP A CG  
51   O OD1 . ASP A 14  ? 0.5193 0.5886 0.5901 -0.0131 0.0326  0.0757  16  ASP A OD1 
52   O OD2 . ASP A 14  ? 0.6170 0.6903 0.6628 -0.0181 0.0321  0.0822  16  ASP A OD2 
53   N N   . ARG A 15  ? 0.4032 0.4441 0.4738 -0.0060 0.0380  0.0547  17  ARG A N   
54   C CA  . ARG A 15  ? 0.4282 0.4664 0.5185 -0.0019 0.0383  0.0530  17  ARG A CA  
55   C C   . ARG A 15  ? 0.4208 0.4669 0.5295 0.0001  0.0371  0.0596  17  ARG A C   
56   O O   . ARG A 15  ? 0.4026 0.4469 0.5214 0.0028  0.0367  0.0549  17  ARG A O   
57   C CB  . ARG A 15  ? 0.4571 0.4911 0.5541 0.0004  0.0399  0.0553  17  ARG A CB  
58   C CG  . ARG A 15  ? 0.5164 0.5441 0.6299 0.0032  0.0390  0.0514  17  ARG A CG  
59   C CD  . ARG A 15  ? 0.5758 0.6028 0.6999 0.0046  0.0397  0.0577  17  ARG A CD  
60   N NE  . ARG A 15  ? 0.6772 0.6992 0.8217 0.0065  0.0373  0.0570  17  ARG A NE  
61   C CZ  . ARG A 15  ? 0.7741 0.7978 0.9358 0.0082  0.0354  0.0611  17  ARG A CZ  
62   N NH1 . ARG A 15  ? 0.7978 0.8303 0.9598 0.0082  0.0359  0.0674  17  ARG A NH1 
63   N NH2 . ARG A 15  ? 0.8134 0.8297 0.9923 0.0098  0.0326  0.0592  17  ARG A NH2 
64   N N   . ALA A 16  ? 0.4336 0.4887 0.5462 -0.0008 0.0368  0.0704  18  ALA A N   
65   C CA  . ALA A 16  ? 0.4292 0.4923 0.5614 0.0014  0.0355  0.0785  18  ALA A CA  
66   C C   . ALA A 16  ? 0.4196 0.4880 0.5521 0.0013  0.0345  0.0762  18  ALA A C   
67   O O   . ALA A 16  ? 0.4320 0.5013 0.5820 0.0057  0.0346  0.0762  18  ALA A O   
68   C CB  . ALA A 16  ? 0.4248 0.4988 0.5582 -0.0006 0.0349  0.0917  18  ALA A CB  
69   N N   . PHE A 17  ? 0.4147 0.4864 0.5287 -0.0035 0.0335  0.0744  19  PHE A N   
70   C CA  . PHE A 17  ? 0.4082 0.4872 0.5222 -0.0045 0.0324  0.0737  19  PHE A CA  
71   C C   . PHE A 17  ? 0.4090 0.4815 0.5264 -0.0007 0.0342  0.0631  19  PHE A C   
72   O O   . PHE A 17  ? 0.4247 0.5032 0.5547 0.0032  0.0350  0.0633  19  PHE A O   
73   C CB  . PHE A 17  ? 0.4255 0.5080 0.5183 -0.0117 0.0299  0.0743  19  PHE A CB  
74   C CG  . PHE A 17  ? 0.4601 0.5543 0.5552 -0.0140 0.0278  0.0779  19  PHE A CG  
75   C CD1 . PHE A 17  ? 0.4849 0.5783 0.5763 -0.0142 0.0283  0.0709  19  PHE A CD1 
76   C CD2 . PHE A 17  ? 0.4737 0.5816 0.5762 -0.0160 0.0253  0.0897  19  PHE A CD2 
77   C CE1 . PHE A 17  ? 0.5006 0.6070 0.5958 -0.0162 0.0267  0.0757  19  PHE A CE1 
78   C CE2 . PHE A 17  ? 0.4883 0.6088 0.5948 -0.0182 0.0233  0.0944  19  PHE A CE2 
79   C CZ  . PHE A 17  ? 0.4835 0.6035 0.5867 -0.0182 0.0242  0.0875  19  PHE A CZ  
80   N N   . LEU A 18  ? 0.3952 0.4564 0.5018 -0.0012 0.0350  0.0540  20  LEU A N   
81   C CA  . LEU A 18  ? 0.3924 0.4483 0.4998 0.0017  0.0363  0.0438  20  LEU A CA  
82   C C   . LEU A 18  ? 0.4026 0.4552 0.5302 0.0085  0.0376  0.0418  20  LEU A C   
83   O O   . LEU A 18  ? 0.3937 0.4481 0.5271 0.0125  0.0389  0.0368  20  LEU A O   
84   C CB  . LEU A 18  ? 0.3646 0.4096 0.4572 -0.0007 0.0364  0.0359  20  LEU A CB  
85   C CG  . LEU A 18  ? 0.3490 0.3940 0.4212 -0.0070 0.0349  0.0356  20  LEU A CG  
86   C CD1 . LEU A 18  ? 0.3361 0.3698 0.3967 -0.0081 0.0353  0.0291  20  LEU A CD1 
87   C CD2 . LEU A 18  ? 0.3687 0.4212 0.4366 -0.0092 0.0341  0.0342  20  LEU A CD2 
88   N N   . MET A 19  ? 0.4227 0.4704 0.5606 0.0099  0.0370  0.0462  21  MET A N   
89   C CA  . MET A 19  ? 0.4530 0.4958 0.6116 0.0156  0.0370  0.0458  21  MET A CA  
90   C C   . MET A 19  ? 0.4829 0.5346 0.6570 0.0198  0.0375  0.0517  21  MET A C   
91   O O   . MET A 19  ? 0.4908 0.5377 0.6771 0.0257  0.0384  0.0461  21  MET A O   
92   C CB  . MET A 19  ? 0.4506 0.4884 0.6188 0.0151  0.0356  0.0520  21  MET A CB  
93   C CG  . MET A 19  ? 0.4746 0.5039 0.6325 0.0124  0.0354  0.0472  21  MET A CG  
94   S SD  . MET A 19  ? 0.5402 0.5573 0.6940 0.0140  0.0348  0.0319  21  MET A SD  
95   C CE  . MET A 19  ? 0.5763 0.5866 0.7536 0.0197  0.0331  0.0299  21  MET A CE  
96   N N   . ALA A 20  ? 0.4985 0.5627 0.6721 0.0170  0.0369  0.0627  22  ALA A N   
97   C CA  . ALA A 20  ? 0.5088 0.5847 0.6965 0.0204  0.0374  0.0701  22  ALA A CA  
98   C C   . ALA A 20  ? 0.5187 0.5992 0.7047 0.0239  0.0398  0.0628  22  ALA A C   
99   O O   . ALA A 20  ? 0.5126 0.5971 0.7156 0.0306  0.0415  0.0645  22  ALA A O   
100  C CB  . ALA A 20  ? 0.5000 0.5896 0.6829 0.0147  0.0353  0.0831  22  ALA A CB  
101  N N   . CYS A 21  ? 0.5283 0.6089 0.6950 0.0199  0.0403  0.0554  23  CYS A N   
102  C CA  . CYS A 21  ? 0.5236 0.6097 0.6867 0.0227  0.0429  0.0486  23  CYS A CA  
103  C C   . CYS A 21  ? 0.5324 0.6082 0.6995 0.0295  0.0455  0.0359  23  CYS A C   
104  O O   . CYS A 21  ? 0.5303 0.6118 0.6942 0.0327  0.0484  0.0300  23  CYS A O   
105  C CB  . CYS A 21  ? 0.5388 0.6281 0.6804 0.0149  0.0415  0.0467  23  CYS A CB  
106  S SG  . CYS A 21  ? 0.5788 0.6794 0.7115 0.0058  0.0375  0.0595  23  CYS A SG  
107  N N   . ARG A 22  ? 0.5468 0.6083 0.7196 0.0313  0.0443  0.0316  24  ARG A N   
108  C CA  . ARG A 22  ? 0.5804 0.6301 0.7546 0.0364  0.0454  0.0187  24  ARG A CA  
109  C C   . ARG A 22  ? 0.6357 0.6841 0.8293 0.0460  0.0477  0.0169  24  ARG A C   
110  O O   . ARG A 22  ? 0.6409 0.6927 0.8511 0.0483  0.0471  0.0270  24  ARG A O   
111  C CB  . ARG A 22  ? 0.5735 0.6083 0.7472 0.0335  0.0422  0.0161  24  ARG A CB  
112  C CG  . ARG A 22  ? 0.5744 0.5964 0.7472 0.0368  0.0418  0.0026  24  ARG A CG  
113  C CD  . ARG A 22  ? 0.5964 0.6054 0.7747 0.0342  0.0379  0.0028  24  ARG A CD  
114  N NE  . ARG A 22  ? 0.6156 0.6126 0.7890 0.0350  0.0362  -0.0101 24  ARG A NE  
115  C CZ  . ARG A 22  ? 0.6159 0.6023 0.7899 0.0313  0.0323  -0.0116 24  ARG A CZ  
116  N NH1 . ARG A 22  ? 0.5723 0.5593 0.7518 0.0272  0.0305  -0.0009 24  ARG A NH1 
117  N NH2 . ARG A 22  ? 0.6369 0.6136 0.8058 0.0315  0.0301  -0.0233 24  ARG A NH2 
118  N N   . GLY A 23  ? 0.6760 0.7191 0.8671 0.0518  0.0501  0.0042  25  GLY A N   
119  C CA  . GLY A 23  ? 0.7306 0.7660 0.9385 0.0617  0.0519  -0.0014 25  GLY A CA  
120  C C   . GLY A 23  ? 0.7720 0.8216 0.9923 0.0691  0.0564  0.0045  25  GLY A C   
121  O O   . GLY A 23  ? 0.7826 0.8276 1.0230 0.0760  0.0567  0.0077  25  GLY A O   
122  N N   . GLY A 24  ? 0.7898 0.8569 0.9997 0.0678  0.0597  0.0069  26  GLY A N   
123  C CA  . GLY A 24  ? 0.8086 0.8927 1.0302 0.0746  0.0643  0.0137  26  GLY A CA  
124  C C   . GLY A 24  ? 0.8292 0.9240 1.0638 0.0711  0.0619  0.0313  26  GLY A C   
125  O O   . GLY A 24  ? 0.8347 0.9288 1.0619 0.0613  0.0572  0.0384  26  GLY A O   
126  N N   . GLY A 25  ? 0.8351 0.9403 1.0891 0.0794  0.0652  0.0382  27  GLY A N   
127  C CA  . GLY A 25  ? 0.8378 0.9586 1.1041 0.0764  0.0632  0.0563  27  GLY A CA  
128  C C   . GLY A 25  ? 0.8392 0.9833 1.1116 0.0805  0.0677  0.0635  27  GLY A C   
129  O O   . GLY A 25  ? 0.8456 0.9948 1.1385 0.0914  0.0717  0.0667  27  GLY A O   
130  N N   . GLY A 26  ? 0.8294 0.9878 1.0853 0.0722  0.0669  0.0666  28  GLY A N   
131  C CA  . GLY A 26  ? 0.8099 0.9939 1.0725 0.0725  0.0689  0.0786  28  GLY A CA  
132  C C   . GLY A 26  ? 0.7930 0.9902 1.0440 0.0732  0.0733  0.0734  28  GLY A C   
133  O O   . GLY A 26  ? 0.8078 0.9968 1.0386 0.0680  0.0726  0.0632  28  GLY A O   
134  N N   . GLU A 27  ? 0.7572 0.9766 1.0224 0.0798  0.0781  0.0819  29  GLU A N   
135  C CA  . GLU A 27  ? 0.7346 0.9721 0.9918 0.0804  0.0826  0.0809  29  GLU A CA  
136  C C   . GLU A 27  ? 0.7029 0.9491 0.9431 0.0642  0.0757  0.0888  29  GLU A C   
137  O O   . GLU A 27  ? 0.7091 0.9589 0.9511 0.0548  0.0688  0.1011  29  GLU A O   
138  C CB  . GLU A 27  ? 0.7689 1.0314 1.0479 0.0908  0.0890  0.0915  29  GLU A CB  
139  C CG  . GLU A 27  ? 0.8651 1.1219 1.1571 0.1091  0.0984  0.0804  29  GLU A CG  
140  C CD  . GLU A 27  ? 0.9816 1.2335 1.2573 0.1150  0.1047  0.0629  29  GLU A CD  
141  O OE1 . GLU A 27  ? 0.9984 1.2627 1.2580 0.1069  0.1041  0.0639  29  GLU A OE1 
142  O OE2 . GLU A 27  ? 1.0094 1.2450 1.2883 0.1273  0.1097  0.0483  29  GLU A OE2 
143  N N   . ASN A 28  ? 0.6606 0.9097 0.8838 0.0608  0.0772  0.0818  30  ASN A N   
144  C CA  . ASN A 28  ? 0.6158 0.8706 0.8226 0.0457  0.0705  0.0879  30  ASN A CA  
145  C C   . ASN A 28  ? 0.5739 0.8585 0.7911 0.0426  0.0703  0.1047  30  ASN A C   
146  O O   . ASN A 28  ? 0.5746 0.8746 0.7875 0.0423  0.0735  0.1055  30  ASN A O   
147  C CB  . ASN A 28  ? 0.6035 0.8503 0.7909 0.0439  0.0722  0.0751  30  ASN A CB  
148  C CG  . ASN A 28  ? 0.5992 0.8488 0.7698 0.0289  0.0652  0.0804  30  ASN A CG  
149  O OD1 . ASN A 28  ? 0.6084 0.8551 0.7760 0.0186  0.0577  0.0887  30  ASN A OD1 
150  N ND2 . ASN A 28  ? 0.5909 0.8454 0.7500 0.0274  0.0673  0.0755  30  ASN A ND2 
151  N N   . LEU A 29  ? 0.5410 0.8350 0.7723 0.0398  0.0662  0.1191  31  LEU A N   
152  C CA  . LEU A 29  ? 0.5100 0.8344 0.7560 0.0390  0.0667  0.1359  31  LEU A CA  
153  C C   . LEU A 29  ? 0.4701 0.8030 0.7008 0.0229  0.0592  0.1429  31  LEU A C   
154  O O   . LEU A 29  ? 0.4591 0.7767 0.6735 0.0107  0.0508  0.1416  31  LEU A O   
155  C CB  . LEU A 29  ? 0.5109 0.8459 0.7778 0.0402  0.0639  0.1510  31  LEU A CB  
156  C CG  . LEU A 29  ? 0.5428 0.8728 0.8310 0.0569  0.0712  0.1478  31  LEU A CG  
157  C CD1 . LEU A 29  ? 0.5405 0.8838 0.8494 0.0559  0.0672  0.1658  31  LEU A CD1 
158  C CD2 . LEU A 29  ? 0.5371 0.8796 0.8368 0.0727  0.0828  0.1427  31  LEU A CD2 
159  N N   . TYR A 30  ? 0.4481 0.8056 0.6844 0.0234  0.0623  0.1508  32  TYR A N   
160  C CA  . TYR A 30  ? 0.4409 0.8094 0.6662 0.0082  0.0550  0.1595  32  TYR A CA  
161  C C   . TYR A 30  ? 0.4661 0.8140 0.6664 0.0011  0.0524  0.1461  32  TYR A C   
162  O O   . TYR A 30  ? 0.4683 0.8178 0.6569 -0.0133 0.0442  0.1521  32  TYR A O   
163  C CB  . TYR A 30  ? 0.4310 0.8024 0.6573 -0.0055 0.0436  0.1735  32  TYR A CB  
164  C CG  . TYR A 30  ? 0.4148 0.8085 0.6666 0.0006  0.0453  0.1886  32  TYR A CG  
165  C CD1 . TYR A 30  ? 0.4036 0.8295 0.6723 0.0025  0.0482  0.2032  32  TYR A CD1 
166  C CD2 . TYR A 30  ? 0.4179 0.8021 0.6787 0.0048  0.0441  0.1897  32  TYR A CD2 
167  C CE1 . TYR A 30  ? 0.3900 0.8377 0.6838 0.0084  0.0498  0.2183  32  TYR A CE1 
168  C CE2 . TYR A 30  ? 0.4049 0.8103 0.6906 0.0102  0.0453  0.2051  32  TYR A CE2 
169  C CZ  . TYR A 30  ? 0.4036 0.8406 0.7061 0.0125  0.0484  0.2191  32  TYR A CZ  
170  O OH  . TYR A 30  ? 0.4294 0.8897 0.7585 0.0187  0.0500  0.2353  32  TYR A OH  
171  N N   . PHE A 31  ? 0.4730 0.8014 0.6657 0.0108  0.0588  0.1286  33  PHE A N   
172  C CA  . PHE A 31  ? 0.4861 0.7916 0.6562 0.0044  0.0556  0.1158  33  PHE A CA  
173  C C   . PHE A 31  ? 0.4811 0.7688 0.6385 -0.0089 0.0451  0.1174  33  PHE A C   
174  O O   . PHE A 31  ? 0.5046 0.7811 0.6444 -0.0186 0.0400  0.1136  33  PHE A O   
175  C CB  . PHE A 31  ? 0.4930 0.8115 0.6545 0.0000  0.0566  0.1170  33  PHE A CB  
176  C CG  . PHE A 31  ? 0.4998 0.8318 0.6681 0.0143  0.0680  0.1111  33  PHE A CG  
177  C CD1 . PHE A 31  ? 0.5223 0.8368 0.6823 0.0235  0.0736  0.0938  33  PHE A CD1 
178  C CD2 . PHE A 31  ? 0.5020 0.8649 0.6846 0.0185  0.0731  0.1230  33  PHE A CD2 
179  C CE1 . PHE A 31  ? 0.5296 0.8557 0.6934 0.0368  0.0840  0.0870  33  PHE A CE1 
180  C CE2 . PHE A 31  ? 0.5125 0.8884 0.6999 0.0327  0.0845  0.1167  33  PHE A CE2 
181  C CZ  . PHE A 31  ? 0.5160 0.8727 0.6931 0.0418  0.0898  0.0982  33  PHE A CZ  
182  N N   . GLN A 32  ? 0.4566 0.7415 0.6226 -0.0089 0.0422  0.1229  34  GLN A N   
183  C CA  . GLN A 32  ? 0.4564 0.7266 0.6108 -0.0204 0.0329  0.1251  34  GLN A CA  
184  C C   . GLN A 32  ? 0.4580 0.7110 0.6159 -0.0139 0.0343  0.1192  34  GLN A C   
185  O O   . GLN A 32  ? 0.4652 0.7103 0.6167 -0.0216 0.0276  0.1231  34  GLN A O   
186  C CB  . GLN A 32  ? 0.4654 0.7547 0.6261 -0.0306 0.0254  0.1426  34  GLN A CB  
187  C CG  . GLN A 32  ? 0.4969 0.8029 0.6543 -0.0394 0.0222  0.1504  34  GLN A CG  
188  C CD  . GLN A 32  ? 0.5945 0.9195 0.7593 -0.0502 0.0138  0.1680  34  GLN A CD  
189  O OE1 . GLN A 32  ? 0.6435 0.9594 0.8010 -0.0589 0.0056  0.1713  34  GLN A OE1 
190  N NE2 . GLN A 32  ? 0.5710 0.9242 0.7503 -0.0501 0.0155  0.1805  34  GLN A NE2 
191  N N   . GLY A 33  ? 0.4492 0.6969 0.6169 -0.0004 0.0424  0.1103  35  GLY A N   
192  C CA  . GLY A 33  ? 0.4592 0.6904 0.6320 0.0057  0.0436  0.1049  35  GLY A CA  
193  C C   . GLY A 33  ? 0.4754 0.6816 0.6318 0.0048  0.0434  0.0905  35  GLY A C   
194  O O   . GLY A 33  ? 0.5018 0.6941 0.6594 0.0060  0.0421  0.0883  35  GLY A O   
195  N N   . LYS A 34  ? 0.4629 0.6644 0.6049 0.0024  0.0442  0.0820  36  LYS A N   
196  C CA  . LYS A 34  ? 0.4695 0.6487 0.5962 0.0006  0.0433  0.0699  36  LYS A CA  
197  C C   . LYS A 34  ? 0.4902 0.6593 0.6009 -0.0114 0.0358  0.0727  36  LYS A C   
198  O O   . LYS A 34  ? 0.5057 0.6845 0.6112 -0.0204 0.0309  0.0811  36  LYS A O   
199  C CB  . LYS A 34  ? 0.4649 0.6433 0.5830 0.0029  0.0469  0.0602  36  LYS A CB  
200  C CG  . LYS A 34  ? 0.4865 0.6690 0.6162 0.0160  0.0547  0.0531  36  LYS A CG  
201  C CD  . LYS A 34  ? 0.5288 0.7164 0.6488 0.0170  0.0579  0.0463  36  LYS A CD  
202  C CE  . LYS A 34  ? 0.5374 0.7228 0.6624 0.0296  0.0652  0.0346  36  LYS A CE  
203  N NZ  . LYS A 34  ? 0.5707 0.7633 0.6836 0.0294  0.0679  0.0290  36  LYS A NZ  
204  N N   . HIS A 35  ? 0.4803 0.6300 0.5835 -0.0115 0.0348  0.0656  37  HIS A N   
205  C CA  . HIS A 35  ? 0.4809 0.6192 0.5683 -0.0208 0.0290  0.0666  37  HIS A CA  
206  C C   . HIS A 35  ? 0.4752 0.6040 0.5458 -0.0258 0.0275  0.0594  37  HIS A C   
207  O O   . HIS A 35  ? 0.4639 0.5822 0.5322 -0.0211 0.0307  0.0500  37  HIS A O   
208  C CB  . HIS A 35  ? 0.5024 0.6270 0.5914 -0.0174 0.0296  0.0637  37  HIS A CB  
209  C CG  . HIS A 35  ? 0.5245 0.6584 0.6298 -0.0139 0.0299  0.0729  37  HIS A CG  
210  N ND1 . HIS A 35  ? 0.5287 0.6668 0.6534 -0.0038 0.0347  0.0723  37  HIS A ND1 
211  C CD2 . HIS A 35  ? 0.5411 0.6806 0.6458 -0.0192 0.0256  0.0829  37  HIS A CD2 
212  C CE1 . HIS A 35  ? 0.5325 0.6789 0.6693 -0.0032 0.0333  0.0828  37  HIS A CE1 
213  N NE2 . HIS A 35  ? 0.5384 0.6869 0.6635 -0.0126 0.0277  0.0897  37  HIS A NE2 
214  N N   . PRO A 36  ? 0.4846 0.6167 0.5439 -0.0357 0.0221  0.0641  38  PRO A N   
215  C CA  . PRO A 36  ? 0.4691 0.5912 0.5138 -0.0404 0.0204  0.0580  38  PRO A CA  
216  C C   . PRO A 36  ? 0.4336 0.5342 0.4650 -0.0418 0.0190  0.0508  38  PRO A C   
217  O O   . PRO A 36  ? 0.4157 0.5095 0.4430 -0.0436 0.0169  0.0526  38  PRO A O   
218  C CB  . PRO A 36  ? 0.4925 0.6230 0.5308 -0.0512 0.0139  0.0666  38  PRO A CB  
219  C CG  . PRO A 36  ? 0.5156 0.6645 0.5673 -0.0510 0.0133  0.0772  38  PRO A CG  
220  C CD  . PRO A 36  ? 0.4863 0.6308 0.5460 -0.0437 0.0165  0.0756  38  PRO A CD  
221  N N   . LEU A 37  ? 0.4124 0.5037 0.4373 -0.0407 0.0205  0.0433  39  LEU A N   
222  C CA  . LEU A 37  ? 0.4014 0.4737 0.4137 -0.0423 0.0192  0.0371  39  LEU A CA  
223  C C   . LEU A 37  ? 0.3911 0.4564 0.3885 -0.0517 0.0132  0.0389  39  LEU A C   
224  O O   . LEU A 37  ? 0.4105 0.4857 0.4078 -0.0572 0.0103  0.0438  39  LEU A O   
225  C CB  . LEU A 37  ? 0.3992 0.4662 0.4135 -0.0364 0.0232  0.0291  39  LEU A CB  
226  C CG  . LEU A 37  ? 0.4165 0.4856 0.4445 -0.0270 0.0284  0.0252  39  LEU A CG  
227  C CD1 . LEU A 37  ? 0.4144 0.4779 0.4420 -0.0229 0.0308  0.0170  39  LEU A CD1 
228  C CD2 . LEU A 37  ? 0.4136 0.4759 0.4453 -0.0247 0.0287  0.0266  39  LEU A CD2 
229  N N   . GLN A 38  ? 0.3859 0.4344 0.3712 -0.0536 0.0114  0.0352  40  GLN A N   
230  C CA  . GLN A 38  ? 0.4006 0.4375 0.3709 -0.0616 0.0058  0.0348  40  GLN A CA  
231  C C   . GLN A 38  ? 0.4095 0.4459 0.3791 -0.0631 0.0054  0.0331  40  GLN A C   
232  O O   . GLN A 38  ? 0.3845 0.4208 0.3483 -0.0711 0.0000  0.0369  40  GLN A O   
233  C CB  . GLN A 38  ? 0.4038 0.4219 0.3621 -0.0602 0.0060  0.0293  40  GLN A CB  
234  C CG  . GLN A 38  ? 0.4625 0.4646 0.4043 -0.0671 0.0005  0.0273  40  GLN A CG  
235  C CD  . GLN A 38  ? 0.5751 0.5792 0.5088 -0.0766 -0.0069 0.0325  40  GLN A CD  
236  O OE1 . GLN A 38  ? 0.5445 0.5605 0.4827 -0.0777 -0.0076 0.0377  40  GLN A OE1 
237  N NE2 . GLN A 38  ? 0.5768 0.5686 0.4987 -0.0842 -0.0131 0.0317  40  GLN A NE2 
238  N N   . ASN A 39  ? 0.3961 0.4325 0.3720 -0.0558 0.0107  0.0280  41  ASN A N   
239  C CA  . ASN A 39  ? 0.3850 0.4210 0.3597 -0.0565 0.0107  0.0262  41  ASN A CA  
240  C C   . ASN A 39  ? 0.3731 0.4249 0.3589 -0.0512 0.0152  0.0256  41  ASN A C   
241  O O   . ASN A 39  ? 0.3923 0.4492 0.3872 -0.0447 0.0193  0.0237  41  ASN A O   
242  C CB  . ASN A 39  ? 0.3937 0.4124 0.3626 -0.0532 0.0120  0.0197  41  ASN A CB  
243  C CG  . ASN A 39  ? 0.4878 0.4895 0.4438 -0.0581 0.0077  0.0194  41  ASN A CG  
244  O OD1 . ASN A 39  ? 0.5355 0.5330 0.4855 -0.0645 0.0031  0.0218  41  ASN A OD1 
245  N ND2 . ASN A 39  ? 0.4734 0.4649 0.4246 -0.0555 0.0090  0.0168  41  ASN A ND2 
246  N N   . ARG A 40  ? 0.3655 0.4249 0.3506 -0.0538 0.0144  0.0273  42  ARG A N   
247  C CA  . ARG A 40  ? 0.3548 0.4261 0.3468 -0.0477 0.0193  0.0240  42  ARG A CA  
248  C C   . ARG A 40  ? 0.3437 0.4022 0.3324 -0.0440 0.0205  0.0166  42  ARG A C   
249  O O   . ARG A 40  ? 0.3583 0.4041 0.3395 -0.0479 0.0173  0.0167  42  ARG A O   
250  C CB  . ARG A 40  ? 0.3670 0.4546 0.3590 -0.0521 0.0181  0.0299  42  ARG A CB  
251  C CG  . ARG A 40  ? 0.4597 0.5602 0.4562 -0.0454 0.0235  0.0256  42  ARG A CG  
252  C CD  . ARG A 40  ? 0.5741 0.6942 0.5707 -0.0491 0.0234  0.0324  42  ARG A CD  
253  N NE  . ARG A 40  ? 0.6717 0.8108 0.6760 -0.0495 0.0248  0.0400  42  ARG A NE  
254  C CZ  . ARG A 40  ? 0.7610 0.9142 0.7740 -0.0411 0.0311  0.0378  42  ARG A CZ  
255  N NH1 . ARG A 40  ? 0.7694 0.9175 0.7836 -0.0320 0.0361  0.0272  42  ARG A NH1 
256  N NH2 . ARG A 40  ? 0.7615 0.9335 0.7828 -0.0417 0.0323  0.0464  42  ARG A NH2 
257  N N   . TRP A 41  ? 0.3271 0.3887 0.3222 -0.0366 0.0249  0.0104  43  TRP A N   
258  C CA  . TRP A 41  ? 0.3340 0.3848 0.3284 -0.0329 0.0258  0.0037  43  TRP A CA  
259  C C   . TRP A 41  ? 0.3263 0.3876 0.3219 -0.0297 0.0279  -0.0006 43  TRP A C   
260  O O   . TRP A 41  ? 0.3447 0.4200 0.3444 -0.0269 0.0308  -0.0006 43  TRP A O   
261  C CB  . TRP A 41  ? 0.3280 0.3708 0.3294 -0.0273 0.0280  0.0000  43  TRP A CB  
262  C CG  . TRP A 41  ? 0.3320 0.3654 0.3308 -0.0297 0.0264  0.0037  43  TRP A CG  
263  C CD1 . TRP A 41  ? 0.3377 0.3756 0.3380 -0.0313 0.0259  0.0084  43  TRP A CD1 
264  C CD2 . TRP A 41  ? 0.3390 0.3575 0.3320 -0.0306 0.0251  0.0030  43  TRP A CD2 
265  N NE1 . TRP A 41  ? 0.3467 0.3729 0.3409 -0.0335 0.0242  0.0099  43  TRP A NE1 
266  C CE2 . TRP A 41  ? 0.3499 0.3641 0.3396 -0.0325 0.0242  0.0064  43  TRP A CE2 
267  C CE3 . TRP A 41  ? 0.3423 0.3518 0.3325 -0.0299 0.0246  0.0002  43  TRP A CE3 
268  C CZ2 . TRP A 41  ? 0.3590 0.3598 0.3416 -0.0329 0.0236  0.0060  43  TRP A CZ2 
269  C CZ3 . TRP A 41  ? 0.3486 0.3453 0.3343 -0.0298 0.0243  0.0007  43  TRP A CZ3 
270  C CH2 . TRP A 41  ? 0.3760 0.3683 0.3575 -0.0308 0.0242  0.0031  43  TRP A CH2 
271  N N   . ALA A 42  ? 0.3121 0.3673 0.3040 -0.0298 0.0267  -0.0041 44  ALA A N   
272  C CA  . ALA A 42  ? 0.3286 0.3919 0.3191 -0.0274 0.0279  -0.0089 44  ALA A CA  
273  C C   . ALA A 42  ? 0.3225 0.3748 0.3161 -0.0235 0.0278  -0.0160 44  ALA A C   
274  O O   . ALA A 42  ? 0.3212 0.3610 0.3145 -0.0251 0.0254  -0.0148 44  ALA A O   
275  C CB  . ALA A 42  ? 0.3344 0.4029 0.3171 -0.0333 0.0249  -0.0043 44  ALA A CB  
276  N N   . LEU A 43  ? 0.3167 0.3734 0.3137 -0.0182 0.0301  -0.0232 45  LEU A N   
277  C CA  . LEU A 43  ? 0.3354 0.3831 0.3351 -0.0153 0.0289  -0.0304 45  LEU A CA  
278  C C   . LEU A 43  ? 0.3303 0.3836 0.3218 -0.0173 0.0268  -0.0336 45  LEU A C   
279  O O   . LEU A 43  ? 0.3206 0.3872 0.3067 -0.0163 0.0288  -0.0358 45  LEU A O   
280  C CB  . LEU A 43  ? 0.3544 0.4016 0.3622 -0.0086 0.0318  -0.0373 45  LEU A CB  
281  C CG  . LEU A 43  ? 0.3867 0.4228 0.3988 -0.0064 0.0293  -0.0446 45  LEU A CG  
282  C CD1 . LEU A 43  ? 0.3698 0.3939 0.3883 -0.0082 0.0270  -0.0402 45  LEU A CD1 
283  C CD2 . LEU A 43  ? 0.4297 0.4647 0.4487 0.0002  0.0316  -0.0523 45  LEU A CD2 
284  N N   . TRP A 44  ? 0.3289 0.3738 0.3198 -0.0199 0.0231  -0.0332 46  TRP A N   
285  C CA  . TRP A 44  ? 0.3479 0.3967 0.3322 -0.0225 0.0199  -0.0351 46  TRP A CA  
286  C C   . TRP A 44  ? 0.3804 0.4212 0.3683 -0.0206 0.0172  -0.0427 46  TRP A C   
287  O O   . TRP A 44  ? 0.3663 0.3959 0.3636 -0.0185 0.0169  -0.0436 46  TRP A O   
288  C CB  . TRP A 44  ? 0.3402 0.3862 0.3219 -0.0280 0.0167  -0.0266 46  TRP A CB  
289  C CG  . TRP A 44  ? 0.3302 0.3804 0.3088 -0.0313 0.0175  -0.0185 46  TRP A CG  
290  C CD1 . TRP A 44  ? 0.3160 0.3602 0.2976 -0.0314 0.0190  -0.0146 46  TRP A CD1 
291  C CD2 . TRP A 44  ? 0.3404 0.4012 0.3121 -0.0361 0.0158  -0.0126 46  TRP A CD2 
292  N NE1 . TRP A 44  ? 0.3464 0.3953 0.3233 -0.0363 0.0178  -0.0072 46  TRP A NE1 
293  C CE2 . TRP A 44  ? 0.3582 0.4181 0.3298 -0.0391 0.0161  -0.0054 46  TRP A CE2 
294  C CE3 . TRP A 44  ? 0.3692 0.4414 0.3345 -0.0384 0.0139  -0.0125 46  TRP A CE3 
295  C CZ2 . TRP A 44  ? 0.4027 0.4712 0.3697 -0.0448 0.0140  0.0027  46  TRP A CZ2 
296  C CZ3 . TRP A 44  ? 0.4195 0.5023 0.3800 -0.0435 0.0125  -0.0040 46  TRP A CZ3 
297  C CH2 . TRP A 44  ? 0.4204 0.5010 0.3826 -0.0468 0.0125  0.0038  46  TRP A CH2 
298  N N   . PHE A 45  ? 0.3914 0.4384 0.3720 -0.0218 0.0148  -0.0476 47  PHE A N   
299  C CA  . PHE A 45  ? 0.4576 0.4980 0.4396 -0.0216 0.0106  -0.0548 47  PHE A CA  
300  C C   . PHE A 45  ? 0.4859 0.5319 0.4602 -0.0270 0.0056  -0.0523 47  PHE A C   
301  O O   . PHE A 45  ? 0.4639 0.5228 0.4287 -0.0291 0.0064  -0.0496 47  PHE A O   
302  C CB  . PHE A 45  ? 0.5026 0.5451 0.4812 -0.0165 0.0128  -0.0667 47  PHE A CB  
303  C CG  . PHE A 45  ? 0.5544 0.5897 0.5319 -0.0165 0.0078  -0.0766 47  PHE A CG  
304  C CD1 . PHE A 45  ? 0.5951 0.6160 0.5846 -0.0166 0.0042  -0.0774 47  PHE A CD1 
305  C CD2 . PHE A 45  ? 0.5914 0.6345 0.5557 -0.0166 0.0064  -0.0849 47  PHE A CD2 
306  C CE1 . PHE A 45  ? 0.6193 0.6326 0.6084 -0.0177 -0.0016 -0.0862 47  PHE A CE1 
307  C CE2 . PHE A 45  ? 0.6173 0.6523 0.5792 -0.0173 0.0009  -0.0949 47  PHE A CE2 
308  C CZ  . PHE A 45  ? 0.6225 0.6420 0.5973 -0.0182 -0.0036 -0.0954 47  PHE A CZ  
309  N N   . PHE A 46  ? 0.5291 0.5671 0.5088 -0.0294 0.0003  -0.0520 48  PHE A N   
310  C CA  . PHE A 46  ? 0.6226 0.6657 0.5967 -0.0345 -0.0056 -0.0505 48  PHE A CA  
311  C C   . PHE A 46  ? 0.6852 0.7251 0.6563 -0.0344 -0.0101 -0.0620 48  PHE A C   
312  O O   . PHE A 46  ? 0.6839 0.7120 0.6649 -0.0330 -0.0120 -0.0656 48  PHE A O   
313  C CB  . PHE A 46  ? 0.6642 0.7017 0.6478 -0.0376 -0.0087 -0.0400 48  PHE A CB  
314  C CG  . PHE A 46  ? 0.7254 0.7707 0.7042 -0.0431 -0.0145 -0.0348 48  PHE A CG  
315  C CD1 . PHE A 46  ? 0.7453 0.8012 0.7169 -0.0458 -0.0138 -0.0275 48  PHE A CD1 
316  C CD2 . PHE A 46  ? 0.7649 0.8077 0.7478 -0.0462 -0.0212 -0.0358 48  PHE A CD2 
317  C CE1 . PHE A 46  ? 0.7657 0.8297 0.7341 -0.0510 -0.0195 -0.0214 48  PHE A CE1 
318  C CE2 . PHE A 46  ? 0.7853 0.8366 0.7649 -0.0515 -0.0270 -0.0298 48  PHE A CE2 
319  C CZ  . PHE A 46  ? 0.7784 0.8403 0.7507 -0.0537 -0.0259 -0.0225 48  PHE A CZ  
320  N N   . LYS A 47  ? 0.7335 0.7841 0.6903 -0.0360 -0.0119 -0.0678 49  LYS A N   
321  C CA  . LYS A 47  ? 0.7917 0.8391 0.7417 -0.0365 -0.0170 -0.0803 49  LYS A CA  
322  C C   . LYS A 47  ? 0.8274 0.8746 0.7787 -0.0438 -0.0261 -0.0757 49  LYS A C   
323  O O   . LYS A 47  ? 0.8246 0.8820 0.7734 -0.0480 -0.0277 -0.0654 49  LYS A O   
324  C CB  . LYS A 47  ? 0.8263 0.8874 0.7579 -0.0346 -0.0143 -0.0887 49  LYS A CB  
325  C CG  . LYS A 47  ? 0.9115 0.9656 0.8365 -0.0296 -0.0141 -0.1058 49  LYS A CG  
326  C CD  . LYS A 47  ? 0.9896 1.0571 0.9006 -0.0237 -0.0066 -0.1127 49  LYS A CD  
327  C CE  . LYS A 47  ? 1.0443 1.1028 0.9510 -0.0163 -0.0044 -0.1298 49  LYS A CE  
328  N NZ  . LYS A 47  ? 1.0767 1.1219 1.0002 -0.0104 0.0000  -0.1301 49  LYS A NZ  
329  N N   . ASN A 48  ? 0.8538 0.8897 0.8101 -0.0455 -0.0327 -0.0824 50  ASN A N   
330  C CA  . ASN A 48  ? 0.8924 0.9294 0.8508 -0.0531 -0.0423 -0.0777 50  ASN A CA  
331  C C   . ASN A 48  ? 0.9165 0.9617 0.8556 -0.0565 -0.0477 -0.0876 50  ASN A C   
332  O O   . ASN A 48  ? 0.9238 0.9628 0.8613 -0.0607 -0.0562 -0.0945 50  ASN A O   
333  C CB  . ASN A 48  ? 0.9313 0.9535 0.9063 -0.0545 -0.0476 -0.0778 50  ASN A CB  
334  C CG  . ASN A 48  ? 1.0020 1.0269 0.9838 -0.0622 -0.0570 -0.0689 50  ASN A CG  
335  O OD1 . ASN A 48  ? 1.0264 1.0639 1.0006 -0.0666 -0.0600 -0.0627 50  ASN A OD1 
336  N ND2 . ASN A 48  ? 1.0146 1.0293 1.0121 -0.0643 -0.0621 -0.0668 50  ASN A ND2 
337  N N   . ASP A 49  ? 0.9305 0.9904 0.8547 -0.0550 -0.0428 -0.0881 51  ASP A N   
338  C CA  . ASP A 49  ? 0.9513 1.0219 0.8545 -0.0572 -0.0460 -0.0974 51  ASP A CA  
339  C C   . ASP A 49  ? 0.9587 1.0447 0.8566 -0.0651 -0.0520 -0.0859 51  ASP A C   
340  O O   . ASP A 49  ? 0.9525 1.0527 0.8467 -0.0652 -0.0477 -0.0762 51  ASP A O   
341  C CB  . ASP A 49  ? 0.9802 1.0603 0.8707 -0.0501 -0.0362 -0.1041 51  ASP A CB  
342  C CG  . ASP A 49  ? 1.0561 1.1484 0.9233 -0.0503 -0.0374 -0.1153 51  ASP A CG  
343  O OD1 . ASP A 49  ? 1.0662 1.1615 0.9249 -0.0573 -0.0467 -0.1167 51  ASP A OD1 
344  O OD2 . ASP A 49  ? 1.0964 1.1963 0.9536 -0.0434 -0.0291 -0.1223 51  ASP A OD2 
345  N N   . LYS A 50  ? 0.9740 1.0575 0.8720 -0.0721 -0.0627 -0.0863 52  LYS A N   
346  C CA  . LYS A 50  ? 0.9831 1.0814 0.8782 -0.0800 -0.0695 -0.0739 52  LYS A CA  
347  C C   . LYS A 50  ? 0.9737 1.0908 0.8448 -0.0823 -0.0703 -0.0784 52  LYS A C   
348  O O   . LYS A 50  ? 0.9668 1.0987 0.8351 -0.0887 -0.0754 -0.0666 52  LYS A O   
349  C CB  . LYS A 50  ? 1.0335 1.1250 0.9389 -0.0873 -0.0811 -0.0705 52  LYS A CB  
350  C CG  . LYS A 50  ? 1.1237 1.2013 1.0543 -0.0856 -0.0801 -0.0620 52  LYS A CG  
351  C CD  . LYS A 50  ? 1.2006 1.2857 1.1446 -0.0854 -0.0765 -0.0429 52  LYS A CD  
352  C CE  . LYS A 50  ? 1.2708 1.3442 1.2381 -0.0833 -0.0754 -0.0344 52  LYS A CE  
353  N NZ  . LYS A 50  ? 1.3216 1.3841 1.2944 -0.0751 -0.0651 -0.0382 52  LYS A NZ  
354  N N   . SER A 51  ? 0.9671 1.0849 0.8212 -0.0767 -0.0651 -0.0944 53  SER A N   
355  C CA  . SER A 51  ? 0.9562 1.0952 0.7880 -0.0770 -0.0628 -0.0965 53  SER A CA  
356  C C   . SER A 51  ? 0.9321 1.0862 0.7676 -0.0744 -0.0538 -0.0823 53  SER A C   
357  O O   . SER A 51  ? 0.9494 1.1246 0.7700 -0.0762 -0.0524 -0.0786 53  SER A O   
358  C CB  . SER A 51  ? 0.9858 1.1217 0.7981 -0.0708 -0.0593 -0.1180 53  SER A CB  
359  O OG  . SER A 51  ? 1.0157 1.1516 0.8291 -0.0609 -0.0470 -0.1223 53  SER A OG  
360  N N   . LYS A 52  ? 0.8903 1.0342 0.7451 -0.0707 -0.0481 -0.0743 54  LYS A N   
361  C CA  . LYS A 52  ? 0.8514 1.0059 0.7115 -0.0690 -0.0409 -0.0611 54  LYS A CA  
362  C C   . LYS A 52  ? 0.8024 0.9511 0.6820 -0.0729 -0.0437 -0.0439 54  LYS A C   
363  O O   . LYS A 52  ? 0.8151 0.9496 0.7072 -0.0744 -0.0486 -0.0432 54  LYS A O   
364  C CB  . LYS A 52  ? 0.8807 1.0285 0.7437 -0.0601 -0.0306 -0.0687 54  LYS A CB  
365  C CG  . LYS A 52  ? 0.9466 1.1040 0.7907 -0.0546 -0.0255 -0.0834 54  LYS A CG  
366  C CD  . LYS A 52  ? 1.0232 1.1693 0.8730 -0.0452 -0.0170 -0.0932 54  LYS A CD  
367  C CE  . LYS A 52  ? 1.0989 1.2540 0.9307 -0.0382 -0.0112 -0.1084 54  LYS A CE  
368  N NZ  . LYS A 52  ? 1.1505 1.2996 0.9675 -0.0396 -0.0181 -0.1238 54  LYS A NZ  
369  N N   . THR A 53  ? 0.7546 0.9142 0.6372 -0.0743 -0.0405 -0.0299 55  THR A N   
370  C CA  . THR A 53  ? 0.7217 0.8745 0.6219 -0.0765 -0.0419 -0.0142 55  THR A CA  
371  C C   . THR A 53  ? 0.6915 0.8262 0.6055 -0.0703 -0.0352 -0.0160 55  THR A C   
372  O O   . THR A 53  ? 0.6738 0.8053 0.5833 -0.0650 -0.0295 -0.0269 55  THR A O   
373  C CB  . THR A 53  ? 0.7212 0.8907 0.6192 -0.0802 -0.0412 0.0008  55  THR A CB  
374  O OG1 . THR A 53  ? 0.7279 0.9002 0.6240 -0.0760 -0.0328 -0.0001 55  THR A OG1 
375  C CG2 . THR A 53  ? 0.7197 0.9112 0.6017 -0.0859 -0.0463 0.0028  55  THR A CG2 
376  N N   . TRP A 54  ? 0.6839 0.8080 0.6135 -0.0707 -0.0358 -0.0054 56  TRP A N   
377  C CA  . TRP A 54  ? 0.6971 0.8041 0.6383 -0.0652 -0.0305 -0.0078 56  TRP A CA  
378  C C   . TRP A 54  ? 0.6751 0.7849 0.6142 -0.0626 -0.0234 -0.0053 56  TRP A C   
379  O O   . TRP A 54  ? 0.6773 0.7779 0.6197 -0.0577 -0.0181 -0.0116 56  TRP A O   
380  C CB  . TRP A 54  ? 0.7072 0.8015 0.6650 -0.0654 -0.0328 0.0015  56  TRP A CB  
381  C CG  . TRP A 54  ? 0.7257 0.8217 0.6891 -0.0673 -0.0328 0.0160  56  TRP A CG  
382  C CD1 . TRP A 54  ? 0.7383 0.8416 0.7048 -0.0719 -0.0385 0.0275  56  TRP A CD1 
383  C CD2 . TRP A 54  ? 0.7354 0.8243 0.7025 -0.0648 -0.0274 0.0207  56  TRP A CD2 
384  N NE1 . TRP A 54  ? 0.7457 0.8458 0.7182 -0.0719 -0.0367 0.0388  56  TRP A NE1 
385  C CE2 . TRP A 54  ? 0.7438 0.8346 0.7158 -0.0679 -0.0302 0.0344  56  TRP A CE2 
386  C CE3 . TRP A 54  ? 0.7483 0.8296 0.7148 -0.0606 -0.0211 0.0149  56  TRP A CE3 
387  C CZ2 . TRP A 54  ? 0.7562 0.8398 0.7317 -0.0672 -0.0273 0.0412  56  TRP A CZ2 
388  C CZ3 . TRP A 54  ? 0.7616 0.8379 0.7307 -0.0605 -0.0184 0.0222  56  TRP A CZ3 
389  C CH2 . TRP A 54  ? 0.7622 0.8387 0.7355 -0.0638 -0.0216 0.0346  56  TRP A CH2 
390  N N   . GLN A 55  ? 0.6458 0.7688 0.5802 -0.0665 -0.0240 0.0049  57  GLN A N   
391  C CA  . GLN A 55  ? 0.6159 0.7448 0.5475 -0.0654 -0.0184 0.0077  57  GLN A CA  
392  C C   . GLN A 55  ? 0.5684 0.7066 0.4888 -0.0613 -0.0135 -0.0048 57  GLN A C   
393  O O   . GLN A 55  ? 0.5520 0.6870 0.4746 -0.0573 -0.0078 -0.0078 57  GLN A O   
394  C CB  . GLN A 55  ? 0.6407 0.7825 0.5708 -0.0711 -0.0206 0.0225  57  GLN A CB  
395  C CG  . GLN A 55  ? 0.7461 0.8897 0.6777 -0.0707 -0.0157 0.0275  57  GLN A CG  
396  C CD  . GLN A 55  ? 0.8198 0.9738 0.7525 -0.0769 -0.0182 0.0431  57  GLN A CD  
397  O OE1 . GLN A 55  ? 0.8011 0.9698 0.7295 -0.0816 -0.0224 0.0507  57  GLN A OE1 
398  N NE2 . GLN A 55  ? 0.8516 0.9977 0.7903 -0.0774 -0.0162 0.0486  57  GLN A NE2 
399  N N   . ALA A 56  ? 0.5550 0.7039 0.4635 -0.0620 -0.0159 -0.0124 58  ALA A N   
400  C CA  . ALA A 56  ? 0.5503 0.7056 0.4479 -0.0568 -0.0112 -0.0262 58  ALA A CA  
401  C C   . ALA A 56  ? 0.5436 0.6799 0.4483 -0.0508 -0.0088 -0.0383 58  ALA A C   
402  O O   . ALA A 56  ? 0.5442 0.6818 0.4462 -0.0448 -0.0026 -0.0466 58  ALA A O   
403  C CB  . ALA A 56  ? 0.5685 0.7360 0.4509 -0.0591 -0.0153 -0.0326 58  ALA A CB  
404  N N   . ASN A 57  ? 0.5408 0.6609 0.4554 -0.0521 -0.0136 -0.0384 59  ASN A N   
405  C CA  . ASN A 57  ? 0.5555 0.6588 0.4773 -0.0471 -0.0123 -0.0492 59  ASN A CA  
406  C C   . ASN A 57  ? 0.5434 0.6357 0.4779 -0.0434 -0.0071 -0.0451 59  ASN A C   
407  O O   . ASN A 57  ? 0.5640 0.6450 0.5042 -0.0387 -0.0050 -0.0532 59  ASN A O   
408  C CB  . ASN A 57  ? 0.5735 0.6659 0.5008 -0.0501 -0.0198 -0.0514 59  ASN A CB  
409  C CG  . ASN A 57  ? 0.6274 0.7266 0.5412 -0.0529 -0.0255 -0.0601 59  ASN A CG  
410  O OD1 . ASN A 57  ? 0.6329 0.7365 0.5342 -0.0493 -0.0228 -0.0726 59  ASN A OD1 
411  N ND2 . ASN A 57  ? 0.6699 0.7702 0.5859 -0.0592 -0.0334 -0.0539 59  ASN A ND2 
412  N N   . LEU A 58  ? 0.5075 0.6020 0.4464 -0.0458 -0.0058 -0.0328 60  LEU A N   
413  C CA  . LEU A 58  ? 0.4702 0.5556 0.4181 -0.0428 -0.0011 -0.0296 60  LEU A CA  
414  C C   . LEU A 58  ? 0.4456 0.5425 0.3877 -0.0399 0.0049  -0.0316 60  LEU A C   
415  O O   . LEU A 58  ? 0.4541 0.5664 0.3891 -0.0428 0.0054  -0.0256 60  LEU A O   
416  C CB  . LEU A 58  ? 0.4579 0.5385 0.4121 -0.0464 -0.0028 -0.0168 60  LEU A CB  
417  C CG  . LEU A 58  ? 0.4583 0.5294 0.4193 -0.0442 0.0014  -0.0135 60  LEU A CG  
418  C CD1 . LEU A 58  ? 0.4731 0.5303 0.4424 -0.0394 0.0032  -0.0201 60  LEU A CD1 
419  C CD2 . LEU A 58  ? 0.4962 0.5620 0.4609 -0.0477 -0.0006 -0.0024 60  LEU A CD2 
420  N N   . ARG A 59  ? 0.4167 0.5075 0.3631 -0.0343 0.0091  -0.0389 61  ARG A N   
421  C CA  . ARG A 59  ? 0.4333 0.5343 0.3766 -0.0299 0.0153  -0.0422 61  ARG A CA  
422  C C   . ARG A 59  ? 0.4318 0.5251 0.3851 -0.0273 0.0189  -0.0391 61  ARG A C   
423  O O   . ARG A 59  ? 0.4184 0.4961 0.3804 -0.0256 0.0180  -0.0412 61  ARG A O   
424  C CB  . ARG A 59  ? 0.4777 0.5794 0.4160 -0.0241 0.0170  -0.0563 61  ARG A CB  
425  C CG  . ARG A 59  ? 0.6147 0.7348 0.5385 -0.0240 0.0181  -0.0601 61  ARG A CG  
426  C CD  . ARG A 59  ? 0.7122 0.8345 0.6309 -0.0158 0.0230  -0.0741 61  ARG A CD  
427  N NE  . ARG A 59  ? 0.7882 0.9144 0.7143 -0.0101 0.0301  -0.0722 61  ARG A NE  
428  C CZ  . ARG A 59  ? 0.8498 0.9761 0.7763 -0.0015 0.0356  -0.0826 61  ARG A CZ  
429  N NH1 . ARG A 59  ? 0.8777 0.9986 0.7963 0.0027  0.0347  -0.0970 61  ARG A NH1 
430  N NH2 . ARG A 59  ? 0.8427 0.9740 0.7777 0.0031  0.0416  -0.0787 61  ARG A NH2 
431  N N   . LEU A 60  ? 0.4249 0.5303 0.3773 -0.0275 0.0227  -0.0331 62  LEU A N   
432  C CA  . LEU A 60  ? 0.4508 0.5529 0.4113 -0.0250 0.0262  -0.0306 62  LEU A CA  
433  C C   . LEU A 60  ? 0.4993 0.6071 0.4613 -0.0171 0.0317  -0.0395 62  LEU A C   
434  O O   . LEU A 60  ? 0.5370 0.6617 0.4929 -0.0149 0.0354  -0.0407 62  LEU A O   
435  C CB  . LEU A 60  ? 0.4502 0.5614 0.4102 -0.0303 0.0261  -0.0185 62  LEU A CB  
436  C CG  . LEU A 60  ? 0.4753 0.5801 0.4432 -0.0304 0.0274  -0.0137 62  LEU A CG  
437  C CD1 . LEU A 60  ? 0.4849 0.5891 0.4518 -0.0381 0.0237  -0.0021 62  LEU A CD1 
438  C CD2 . LEU A 60  ? 0.4892 0.6076 0.4599 -0.0255 0.0328  -0.0151 62  LEU A CD2 
439  N N   . ILE A 61  ? 0.4903 0.5843 0.4608 -0.0125 0.0326  -0.0453 63  ILE A N   
440  C CA  . ILE A 61  ? 0.5002 0.5944 0.4746 -0.0042 0.0370  -0.0548 63  ILE A CA  
441  C C   . ILE A 61  ? 0.4825 0.5883 0.4624 -0.0014 0.0422  -0.0490 63  ILE A C   
442  O O   . ILE A 61  ? 0.4756 0.5958 0.4529 0.0038  0.0473  -0.0522 63  ILE A O   
443  C CB  . ILE A 61  ? 0.5364 0.6110 0.5202 -0.0015 0.0348  -0.0608 63  ILE A CB  
444  C CG1 . ILE A 61  ? 0.5731 0.6379 0.5528 -0.0046 0.0290  -0.0661 63  ILE A CG1 
445  C CG2 . ILE A 61  ? 0.5625 0.6357 0.5529 0.0071  0.0391  -0.0689 63  ILE A CG2 
446  C CD1 . ILE A 61  ? 0.6263 0.6999 0.5929 -0.0038 0.0284  -0.0748 63  ILE A CD1 
447  N N   . SER A 62  ? 0.4612 0.5618 0.4485 -0.0047 0.0411  -0.0402 64  SER A N   
448  C CA  . SER A 62  ? 0.4649 0.5758 0.4586 -0.0029 0.0449  -0.0339 64  SER A CA  
449  C C   . SER A 62  ? 0.4266 0.5312 0.4237 -0.0097 0.0414  -0.0234 64  SER A C   
450  O O   . SER A 62  ? 0.4124 0.5018 0.4088 -0.0133 0.0374  -0.0228 64  SER A O   
451  C CB  . SER A 62  ? 0.5340 0.6412 0.5377 0.0060  0.0489  -0.0406 64  SER A CB  
452  O OG  . SER A 62  ? 0.6256 0.7476 0.6356 0.0091  0.0534  -0.0349 64  SER A OG  
453  N N   . LYS A 63  ? 0.4165 0.5336 0.4166 -0.0114 0.0429  -0.0151 65  LYS A N   
454  C CA  . LYS A 63  ? 0.4316 0.5431 0.4338 -0.0177 0.0394  -0.0059 65  LYS A CA  
455  C C   . LYS A 63  ? 0.4248 0.5409 0.4374 -0.0139 0.0421  -0.0031 65  LYS A C   
456  O O   . LYS A 63  ? 0.4342 0.5641 0.4520 -0.0079 0.0469  -0.0044 65  LYS A O   
457  C CB  . LYS A 63  ? 0.4283 0.5499 0.4246 -0.0259 0.0365  0.0037  65  LYS A CB  
458  C CG  . LYS A 63  ? 0.4712 0.5909 0.4585 -0.0296 0.0338  0.0025  65  LYS A CG  
459  C CD  . LYS A 63  ? 0.4873 0.6121 0.4706 -0.0387 0.0295  0.0134  65  LYS A CD  
460  C CE  . LYS A 63  ? 0.5035 0.6254 0.4794 -0.0434 0.0259  0.0149  65  LYS A CE  
461  N NZ  . LYS A 63  ? 0.4856 0.6120 0.4595 -0.0527 0.0212  0.0266  65  LYS A NZ  
462  N N   . PHE A 64  ? 0.3924 0.4975 0.4080 -0.0170 0.0392  0.0009  66  PHE A N   
463  C CA  . PHE A 64  ? 0.3714 0.4805 0.3970 -0.0141 0.0409  0.0047  66  PHE A CA  
464  C C   . PHE A 64  ? 0.3734 0.4761 0.3963 -0.0219 0.0360  0.0127  66  PHE A C   
465  O O   . PHE A 64  ? 0.3487 0.4382 0.3628 -0.0271 0.0322  0.0122  66  PHE A O   
466  C CB  . PHE A 64  ? 0.3710 0.4706 0.4054 -0.0061 0.0435  -0.0026 66  PHE A CB  
467  C CG  . PHE A 64  ? 0.3711 0.4512 0.4031 -0.0075 0.0405  -0.0063 66  PHE A CG  
468  C CD1 . PHE A 64  ? 0.3743 0.4461 0.4016 -0.0064 0.0399  -0.0140 66  PHE A CD1 
469  C CD2 . PHE A 64  ? 0.3681 0.4400 0.4013 -0.0107 0.0381  -0.0012 66  PHE A CD2 
470  C CE1 . PHE A 64  ? 0.3714 0.4279 0.3979 -0.0078 0.0373  -0.0159 66  PHE A CE1 
471  C CE2 . PHE A 64  ? 0.3746 0.4310 0.4057 -0.0114 0.0362  -0.0038 66  PHE A CE2 
472  C CZ  . PHE A 64  ? 0.3533 0.4025 0.3818 -0.0100 0.0359  -0.0106 66  PHE A CZ  
473  N N   . ASP A 65  ? 0.3703 0.4825 0.4004 -0.0224 0.0361  0.0198  67  ASP A N   
474  C CA  . ASP A 65  ? 0.3856 0.4926 0.4122 -0.0299 0.0310  0.0270  67  ASP A CA  
475  C C   . ASP A 65  ? 0.3613 0.4727 0.3979 -0.0276 0.0316  0.0318  67  ASP A C   
476  O O   . ASP A 65  ? 0.3672 0.4795 0.4010 -0.0343 0.0271  0.0391  67  ASP A O   
477  C CB  . ASP A 65  ? 0.4088 0.5245 0.4293 -0.0389 0.0268  0.0350  67  ASP A CB  
478  C CG  . ASP A 65  ? 0.4707 0.6101 0.4998 -0.0377 0.0294  0.0416  67  ASP A CG  
479  O OD1 . ASP A 65  ? 0.4539 0.6031 0.4948 -0.0302 0.0340  0.0418  67  ASP A OD1 
480  O OD2 . ASP A 65  ? 0.5399 0.6889 0.5653 -0.0436 0.0272  0.0470  67  ASP A OD2 
481  N N   . THR A 66  ? 0.3662 0.4791 0.4139 -0.0185 0.0363  0.0278  68  THR A N   
482  C CA  . THR A 66  ? 0.3880 0.5016 0.4463 -0.0155 0.0367  0.0319  68  THR A CA  
483  C C   . THR A 66  ? 0.3836 0.4835 0.4475 -0.0086 0.0390  0.0244  68  THR A C   
484  O O   . THR A 66  ? 0.3981 0.4918 0.4604 -0.0046 0.0412  0.0157  68  THR A O   
485  C CB  . THR A 66  ? 0.4132 0.5467 0.4858 -0.0106 0.0401  0.0379  68  THR A CB  
486  O OG1 . THR A 66  ? 0.4362 0.5710 0.5157 -0.0007 0.0460  0.0296  68  THR A OG1 
487  C CG2 . THR A 66  ? 0.3991 0.5498 0.4687 -0.0171 0.0382  0.0463  68  THR A CG2 
488  N N   . VAL A 67  ? 0.3672 0.4638 0.4381 -0.0077 0.0382  0.0287  69  VAL A N   
489  C CA  . VAL A 67  ? 0.3902 0.4754 0.4692 -0.0021 0.0396  0.0247  69  VAL A CA  
490  C C   . VAL A 67  ? 0.3906 0.4780 0.4821 0.0072  0.0439  0.0185  69  VAL A C   
491  O O   . VAL A 67  ? 0.3836 0.4593 0.4763 0.0108  0.0447  0.0102  69  VAL A O   
492  C CB  . VAL A 67  ? 0.3647 0.4506 0.4507 -0.0030 0.0379  0.0332  69  VAL A CB  
493  C CG1 . VAL A 67  ? 0.3787 0.4543 0.4752 0.0025  0.0392  0.0304  69  VAL A CG1 
494  C CG2 . VAL A 67  ? 0.3687 0.4509 0.4400 -0.0117 0.0337  0.0378  69  VAL A CG2 
495  N N   . GLU A 68  ? 0.3788 0.4812 0.4793 0.0111  0.0467  0.0222  70  GLU A N   
496  C CA  . GLU A 68  ? 0.3710 0.4756 0.4840 0.0213  0.0514  0.0164  70  GLU A CA  
497  C C   . GLU A 68  ? 0.3789 0.4813 0.4825 0.0237  0.0537  0.0052  70  GLU A C   
498  O O   . GLU A 68  ? 0.3816 0.4757 0.4900 0.0309  0.0560  -0.0044 70  GLU A O   
499  C CB  . GLU A 68  ? 0.3809 0.5037 0.5071 0.0257  0.0544  0.0246  70  GLU A CB  
500  C CG  . GLU A 68  ? 0.4267 0.5518 0.5660 0.0254  0.0524  0.0353  70  GLU A CG  
501  C CD  . GLU A 68  ? 0.4681 0.5970 0.5991 0.0148  0.0470  0.0455  70  GLU A CD  
502  O OE1 . GLU A 68  ? 0.4353 0.5662 0.5510 0.0071  0.0445  0.0456  70  GLU A OE1 
503  O OE2 . GLU A 68  ? 0.4966 0.6260 0.6362 0.0141  0.0449  0.0536  70  GLU A OE2 
504  N N   . ASP A 69  ? 0.3669 0.4765 0.4571 0.0175  0.0527  0.0064  71  ASP A N   
505  C CA  . ASP A 69  ? 0.3707 0.4794 0.4505 0.0184  0.0541  -0.0028 71  ASP A CA  
506  C C   . ASP A 69  ? 0.3765 0.4662 0.4492 0.0162  0.0510  -0.0104 71  ASP A C   
507  O O   . ASP A 69  ? 0.3874 0.4719 0.4569 0.0201  0.0522  -0.0204 71  ASP A O   
508  C CB  . ASP A 69  ? 0.4039 0.5264 0.4732 0.0116  0.0532  0.0030  71  ASP A CB  
509  C CG  . ASP A 69  ? 0.4739 0.6181 0.5524 0.0149  0.0570  0.0106  71  ASP A CG  
510  O OD1 . ASP A 69  ? 0.4474 0.5963 0.5366 0.0249  0.0623  0.0067  71  ASP A OD1 
511  O OD2 . ASP A 69  ? 0.4998 0.6556 0.5753 0.0074  0.0544  0.0207  71  ASP A OD2 
512  N N   . PHE A 70  ? 0.3587 0.4386 0.4292 0.0103  0.0470  -0.0057 72  PHE A N   
513  C CA  . PHE A 70  ? 0.3498 0.4132 0.4171 0.0090  0.0444  -0.0109 72  PHE A CA  
514  C C   . PHE A 70  ? 0.3450 0.3999 0.4242 0.0163  0.0456  -0.0176 72  PHE A C   
515  O O   . PHE A 70  ? 0.3577 0.4044 0.4336 0.0177  0.0448  -0.0263 72  PHE A O   
516  C CB  . PHE A 70  ? 0.3296 0.3860 0.3943 0.0033  0.0412  -0.0038 72  PHE A CB  
517  C CG  . PHE A 70  ? 0.3602 0.4021 0.4274 0.0041  0.0397  -0.0075 72  PHE A CG  
518  C CD1 . PHE A 70  ? 0.3765 0.4108 0.4350 0.0018  0.0381  -0.0128 72  PHE A CD1 
519  C CD2 . PHE A 70  ? 0.3589 0.3960 0.4385 0.0071  0.0397  -0.0045 72  PHE A CD2 
520  C CE1 . PHE A 70  ? 0.3766 0.3995 0.4394 0.0025  0.0365  -0.0151 72  PHE A CE1 
521  C CE2 . PHE A 70  ? 0.3669 0.3924 0.4504 0.0074  0.0381  -0.0064 72  PHE A CE2 
522  C CZ  . PHE A 70  ? 0.3757 0.3945 0.4510 0.0051  0.0365  -0.0117 72  PHE A CZ  
523  N N   . TRP A 71  ? 0.3459 0.4022 0.4393 0.0205  0.0468  -0.0130 73  TRP A N   
524  C CA  . TRP A 71  ? 0.3671 0.4136 0.4736 0.0269  0.0472  -0.0181 73  TRP A CA  
525  C C   . TRP A 71  ? 0.3926 0.4394 0.4993 0.0340  0.0501  -0.0294 73  TRP A C   
526  O O   . TRP A 71  ? 0.4067 0.4406 0.5164 0.0366  0.0484  -0.0377 73  TRP A O   
527  C CB  . TRP A 71  ? 0.3558 0.4049 0.4783 0.0300  0.0477  -0.0096 73  TRP A CB  
528  C CG  . TRP A 71  ? 0.3560 0.4011 0.4797 0.0244  0.0446  -0.0007 73  TRP A CG  
529  C CD1 . TRP A 71  ? 0.3593 0.4134 0.4834 0.0208  0.0440  0.0103  73  TRP A CD1 
530  C CD2 . TRP A 71  ? 0.3506 0.3826 0.4754 0.0221  0.0417  -0.0015 73  TRP A CD2 
531  N NE1 . TRP A 71  ? 0.3526 0.4001 0.4761 0.0169  0.0415  0.0155  73  TRP A NE1 
532  C CE2 . TRP A 71  ? 0.3504 0.3851 0.4758 0.0180  0.0404  0.0090  73  TRP A CE2 
533  C CE3 . TRP A 71  ? 0.3659 0.3854 0.4912 0.0228  0.0398  -0.0097 73  TRP A CE3 
534  C CZ2 . TRP A 71  ? 0.3493 0.3756 0.4761 0.0155  0.0384  0.0119  73  TRP A CZ2 
535  C CZ3 . TRP A 71  ? 0.3589 0.3700 0.4877 0.0198  0.0370  -0.0059 73  TRP A CZ3 
536  C CH2 . TRP A 71  ? 0.3463 0.3615 0.4761 0.0166  0.0368  0.0049  73  TRP A CH2 
537  N N   . ALA A 72  ? 0.4095 0.4708 0.5126 0.0368  0.0541  -0.0296 74  ALA A N   
538  C CA  . ALA A 72  ? 0.4392 0.5026 0.5407 0.0445  0.0580  -0.0407 74  ALA A CA  
539  C C   . ALA A 72  ? 0.4357 0.4922 0.5220 0.0410  0.0555  -0.0502 74  ALA A C   
540  O O   . ALA A 72  ? 0.4360 0.4834 0.5214 0.0459  0.0556  -0.0619 74  ALA A O   
541  C CB  . ALA A 72  ? 0.4435 0.5278 0.5439 0.0478  0.0633  -0.0366 74  ALA A CB  
542  N N   . LEU A 73  ? 0.4337 0.4939 0.5079 0.0324  0.0529  -0.0453 75  LEU A N   
543  C CA  . LEU A 73  ? 0.4236 0.4775 0.4849 0.0282  0.0498  -0.0521 75  LEU A CA  
544  C C   . LEU A 73  ? 0.4114 0.4467 0.4775 0.0269  0.0451  -0.0563 75  LEU A C   
545  O O   . LEU A 73  ? 0.4008 0.4286 0.4628 0.0285  0.0433  -0.0665 75  LEU A O   
546  C CB  . LEU A 73  ? 0.4279 0.4892 0.4777 0.0198  0.0480  -0.0446 75  LEU A CB  
547  C CG  . LEU A 73  ? 0.4625 0.5193 0.4997 0.0149  0.0445  -0.0492 75  LEU A CG  
548  C CD1 . LEU A 73  ? 0.4809 0.5437 0.5104 0.0192  0.0467  -0.0595 75  LEU A CD1 
549  C CD2 . LEU A 73  ? 0.4544 0.5177 0.4824 0.0069  0.0427  -0.0403 75  LEU A CD2 
550  N N   . TYR A 74  ? 0.4159 0.4448 0.4904 0.0238  0.0428  -0.0481 76  TYR A N   
551  C CA  . TYR A 74  ? 0.4310 0.4449 0.5120 0.0221  0.0385  -0.0492 76  TYR A CA  
552  C C   . TYR A 74  ? 0.4542 0.4580 0.5457 0.0284  0.0379  -0.0580 76  TYR A C   
553  O O   . TYR A 74  ? 0.4581 0.4510 0.5487 0.0271  0.0338  -0.0649 76  TYR A O   
554  C CB  . TYR A 74  ? 0.4266 0.4391 0.5154 0.0192  0.0377  -0.0378 76  TYR A CB  
555  C CG  . TYR A 74  ? 0.4261 0.4259 0.5242 0.0177  0.0338  -0.0366 76  TYR A CG  
556  C CD1 . TYR A 74  ? 0.4443 0.4398 0.5362 0.0123  0.0310  -0.0344 76  TYR A CD1 
557  C CD2 . TYR A 74  ? 0.4274 0.4200 0.5417 0.0219  0.0330  -0.0366 76  TYR A CD2 
558  C CE1 . TYR A 74  ? 0.4451 0.4314 0.5469 0.0110  0.0277  -0.0318 76  TYR A CE1 
559  C CE2 . TYR A 74  ? 0.4428 0.4252 0.5671 0.0199  0.0290  -0.0339 76  TYR A CE2 
560  C CZ  . TYR A 74  ? 0.4591 0.4392 0.5771 0.0143  0.0266  -0.0313 76  TYR A CZ  
561  O OH  . TYR A 74  ? 0.5028 0.4752 0.6315 0.0121  0.0229  -0.0270 76  TYR A OH  
562  N N   . ASN A 75  ? 0.4832 0.4904 0.5849 0.0351  0.0415  -0.0575 77  ASN A N   
563  C CA  . ASN A 75  ? 0.5305 0.5266 0.6436 0.0423  0.0412  -0.0660 77  ASN A CA  
564  C C   . ASN A 75  ? 0.5464 0.5392 0.6477 0.0455  0.0414  -0.0810 77  ASN A C   
565  O O   . ASN A 75  ? 0.5564 0.5340 0.6612 0.0468  0.0374  -0.0901 77  ASN A O   
566  C CB  . ASN A 75  ? 0.5669 0.5703 0.6930 0.0498  0.0461  -0.0615 77  ASN A CB  
567  C CG  . ASN A 75  ? 0.6592 0.6641 0.7991 0.0475  0.0451  -0.0475 77  ASN A CG  
568  O OD1 . ASN A 75  ? 0.6845 0.6818 0.8279 0.0420  0.0408  -0.0420 77  ASN A OD1 
569  N ND2 . ASN A 75  ? 0.6978 0.7143 0.8463 0.0520  0.0492  -0.0405 77  ASN A ND2 
570  N N   . HIS A 76  ? 0.5530 0.5604 0.6405 0.0460  0.0455  -0.0830 78  HIS A N   
571  C CA  . HIS A 76  ? 0.5788 0.5871 0.6522 0.0489  0.0464  -0.0963 78  HIS A CA  
572  C C   . HIS A 76  ? 0.5708 0.5694 0.6342 0.0417  0.0396  -0.1015 78  HIS A C   
573  O O   . HIS A 76  ? 0.5541 0.5422 0.6132 0.0440  0.0370  -0.1142 78  HIS A O   
574  C CB  . HIS A 76  ? 0.6140 0.6436 0.6756 0.0497  0.0522  -0.0936 78  HIS A CB  
575  C CG  . HIS A 76  ? 0.7230 0.7567 0.7689 0.0527  0.0539  -0.1061 78  HIS A CG  
576  N ND1 . HIS A 76  ? 0.7747 0.8187 0.8045 0.0461  0.0526  -0.1048 78  HIS A ND1 
577  C CD2 . HIS A 76  ? 0.7672 0.7961 0.8110 0.0617  0.0566  -0.1200 78  HIS A CD2 
578  C CE1 . HIS A 76  ? 0.7930 0.8397 0.8108 0.0510  0.0546  -0.1173 78  HIS A CE1 
579  N NE2 . HIS A 76  ? 0.7943 0.8316 0.8191 0.0606  0.0572  -0.1275 78  HIS A NE2 
580  N N   . ILE A 77  ? 0.5681 0.5697 0.6279 0.0330  0.0366  -0.0918 79  ILE A N   
581  C CA  . ILE A 77  ? 0.5951 0.5893 0.6477 0.0259  0.0301  -0.0941 79  ILE A CA  
582  C C   . ILE A 77  ? 0.6374 0.6135 0.7029 0.0248  0.0241  -0.0961 79  ILE A C   
583  O O   . ILE A 77  ? 0.6352 0.6022 0.6966 0.0219  0.0184  -0.1037 79  ILE A O   
584  C CB  . ILE A 77  ? 0.5967 0.5985 0.6449 0.0183  0.0293  -0.0819 79  ILE A CB  
585  C CG1 . ILE A 77  ? 0.6020 0.6210 0.6376 0.0176  0.0336  -0.0789 79  ILE A CG1 
586  C CG2 . ILE A 77  ? 0.6012 0.5951 0.6465 0.0116  0.0228  -0.0818 79  ILE A CG2 
587  C CD1 . ILE A 77  ? 0.6368 0.6635 0.6584 0.0200  0.0350  -0.0892 79  ILE A CD1 
588  N N   . GLN A 78  ? 0.6713 0.6434 0.7526 0.0264  0.0249  -0.0883 80  GLN A N   
589  C CA  . GLN A 78  ? 0.7296 0.6864 0.8258 0.0249  0.0194  -0.0872 80  GLN A CA  
590  C C   . GLN A 78  ? 0.7997 0.7427 0.8991 0.0299  0.0166  -0.1011 80  GLN A C   
591  O O   . GLN A 78  ? 0.8132 0.7435 0.9154 0.0258  0.0094  -0.1055 80  GLN A O   
592  C CB  . GLN A 78  ? 0.7472 0.7055 0.8593 0.0261  0.0216  -0.0747 80  GLN A CB  
593  C CG  . GLN A 78  ? 0.7906 0.7385 0.9175 0.0221  0.0162  -0.0676 80  GLN A CG  
594  C CD  . GLN A 78  ? 0.7922 0.7421 0.9350 0.0243  0.0186  -0.0562 80  GLN A CD  
595  O OE1 . GLN A 78  ? 0.7621 0.7168 0.9091 0.0302  0.0230  -0.0559 80  GLN A OE1 
596  N NE2 . GLN A 78  ? 0.8082 0.7562 0.9604 0.0197  0.0157  -0.0457 80  GLN A NE2 
597  N N   . LEU A 79  ? 0.8345 0.7801 0.9337 0.0387  0.0223  -0.1080 81  LEU A N   
598  C CA  . LEU A 79  ? 0.8846 0.8181 0.9824 0.0453  0.0214  -0.1238 81  LEU A CA  
599  C C   . LEU A 79  ? 0.9273 0.8584 1.0059 0.0422  0.0175  -0.1367 81  LEU A C   
600  O O   . LEU A 79  ? 0.9407 0.8549 1.0195 0.0424  0.0115  -0.1484 81  LEU A O   
601  C CB  . LEU A 79  ? 0.8920 0.8351 0.9888 0.0561  0.0304  -0.1280 81  LEU A CB  
602  C CG  . LEU A 79  ? 0.9190 0.8577 1.0357 0.0638  0.0336  -0.1239 81  LEU A CG  
603  C CD1 . LEU A 79  ? 0.9239 0.8724 1.0367 0.0750  0.0423  -0.1309 81  LEU A CD1 
604  C CD2 . LEU A 79  ? 0.9470 0.8620 1.0776 0.0650  0.0269  -0.1302 81  LEU A CD2 
605  N N   . SER A 80  ? 0.9374 0.8851 0.9994 0.0391  0.0205  -0.1344 82  SER A N   
606  C CA  . SER A 80  ? 0.9554 0.9058 0.9976 0.0366  0.0180  -0.1452 82  SER A CA  
607  C C   . SER A 80  ? 0.9816 0.9283 1.0203 0.0258  0.0096  -0.1411 82  SER A C   
608  O O   . SER A 80  ? 0.9897 0.9416 1.0118 0.0223  0.0070  -0.1471 82  SER A O   
609  C CB  . SER A 80  ? 0.9544 0.9266 0.9820 0.0389  0.0257  -0.1434 82  SER A CB  
610  O OG  . SER A 80  ? 0.9705 0.9487 1.0030 0.0491  0.0339  -0.1452 82  SER A OG  
611  N N   . SER A 81  ? 0.9964 0.9357 1.0509 0.0208  0.0053  -0.1304 83  SER A N   
612  C CA  . SER A 81  ? 1.0250 0.9661 1.0790 0.0114  -0.0004 -0.1218 83  SER A CA  
613  C C   . SER A 81  ? 1.0510 0.9828 1.0982 0.0059  -0.0096 -0.1309 83  SER A C   
614  O O   . SER A 81  ? 1.0584 0.9738 1.1146 0.0057  -0.0157 -0.1373 83  SER A O   
615  C CB  . SER A 81  ? 1.0436 0.9795 1.1172 0.0088  -0.0021 -0.1086 83  SER A CB  
616  O OG  . SER A 81  ? 1.0766 1.0143 1.1508 0.0008  -0.0071 -0.1004 83  SER A OG  
617  N N   . ASN A 82  ? 1.0610 1.0033 1.0928 0.0009  -0.0112 -0.1308 84  ASN A N   
618  C CA  . ASN A 82  ? 1.0813 1.0181 1.1067 -0.0062 -0.0208 -0.1359 84  ASN A CA  
619  C C   . ASN A 82  ? 1.0836 1.0180 1.1243 -0.0138 -0.0265 -0.1218 84  ASN A C   
620  O O   . ASN A 82  ? 1.0953 1.0182 1.1435 -0.0188 -0.0355 -0.1239 84  ASN A O   
621  C CB  . ASN A 82  ? 1.1044 1.0558 1.1077 -0.0082 -0.0199 -0.1400 84  ASN A CB  
622  C CG  . ASN A 82  ? 1.1459 1.1032 1.1344 -0.0001 -0.0130 -0.1522 84  ASN A CG  
623  O OD1 . ASN A 82  ? 1.1508 1.1016 1.1276 0.0016  -0.0161 -0.1673 84  ASN A OD1 
624  N ND2 . ASN A 82  ? 1.1569 1.1271 1.1455 0.0051  -0.0034 -0.1458 84  ASN A ND2 
625  N N   . LEU A 83  ? 1.0708 1.0158 1.1164 -0.0145 -0.0214 -0.1076 85  LEU A N   
626  C CA  . LEU A 83  ? 1.0610 1.0053 1.1211 -0.0196 -0.0247 -0.0938 85  LEU A CA  
627  C C   . LEU A 83  ? 1.0434 0.9885 1.1001 -0.0276 -0.0336 -0.0930 85  LEU A C   
628  O O   . LEU A 83  ? 1.0415 0.9803 1.1120 -0.0323 -0.0403 -0.0876 85  LEU A O   
629  C CB  . LEU A 83  ? 1.0653 0.9973 1.1457 -0.0183 -0.0266 -0.0907 85  LEU A CB  
630  C CG  . LEU A 83  ? 1.0816 1.0154 1.1783 -0.0221 -0.0280 -0.0751 85  LEU A CG  
631  C CD1 . LEU A 83  ? 1.0869 1.0286 1.1863 -0.0177 -0.0189 -0.0653 85  LEU A CD1 
632  C CD2 . LEU A 83  ? 1.0875 1.0086 1.2031 -0.0244 -0.0349 -0.0737 85  LEU A CD2 
633  N N   . MET A 84  ? 1.0236 0.9781 1.0627 -0.0294 -0.0339 -0.0973 86  MET A N   
634  C CA  . MET A 84  ? 1.0082 0.9639 1.0413 -0.0368 -0.0431 -0.0991 86  MET A CA  
635  C C   . MET A 84  ? 0.9678 0.9326 1.0077 -0.0416 -0.0443 -0.0838 86  MET A C   
636  O O   . MET A 84  ? 0.9663 0.9394 1.0055 -0.0388 -0.0371 -0.0753 86  MET A O   
637  C CB  . MET A 84  ? 1.0339 0.9966 1.0445 -0.0362 -0.0428 -0.1107 86  MET A CB  
638  C CG  . MET A 84  ? 1.1007 1.0535 1.1047 -0.0304 -0.0414 -0.1270 86  MET A CG  
639  S SD  . MET A 84  ? 1.2375 1.1714 1.2432 -0.0354 -0.0544 -0.1398 86  MET A SD  
640  C CE  . MET A 84  ? 1.1851 1.1051 1.1906 -0.0252 -0.0491 -0.1552 86  MET A CE  
641  N N   . PRO A 85  ? 0.9384 0.9016 0.9853 -0.0487 -0.0538 -0.0797 87  PRO A N   
642  C CA  . PRO A 85  ? 0.9078 0.8809 0.9618 -0.0524 -0.0545 -0.0645 87  PRO A CA  
643  C C   . PRO A 85  ? 0.8690 0.8552 0.9066 -0.0530 -0.0519 -0.0632 87  PRO A C   
644  O O   . PRO A 85  ? 0.8722 0.8612 0.8932 -0.0544 -0.0545 -0.0735 87  PRO A O   
645  C CB  . PRO A 85  ? 0.9230 0.8927 0.9869 -0.0603 -0.0662 -0.0620 87  PRO A CB  
646  C CG  . PRO A 85  ? 0.9423 0.9015 0.9960 -0.0623 -0.0730 -0.0788 87  PRO A CG  
647  C CD  . PRO A 85  ? 0.9305 0.8826 0.9796 -0.0539 -0.0646 -0.0885 87  PRO A CD  
648  N N   . GLY A 86  ? 0.8275 0.8213 0.8696 -0.0517 -0.0469 -0.0506 88  GLY A N   
649  C CA  . GLY A 86  ? 0.7930 0.7980 0.8220 -0.0516 -0.0433 -0.0474 88  GLY A CA  
650  C C   . GLY A 86  ? 0.7517 0.7584 0.7719 -0.0456 -0.0340 -0.0507 88  GLY A C   
651  O O   . GLY A 86  ? 0.7650 0.7807 0.7770 -0.0457 -0.0308 -0.0458 88  GLY A O   
652  N N   A CYS A 87  ? 0.7268 0.7254 0.7496 -0.0407 -0.0298 -0.0579 89  CYS A N   
653  N N   B CYS A 87  ? 0.7247 0.7231 0.7476 -0.0408 -0.0300 -0.0581 89  CYS A N   
654  C CA  A CYS A 87  ? 0.7083 0.7101 0.7234 -0.0354 -0.0215 -0.0607 89  CYS A CA  
655  C CA  B CYS A 87  ? 0.7037 0.7050 0.7198 -0.0354 -0.0214 -0.0602 89  CYS A CA  
656  C C   A CYS A 87  ? 0.6707 0.6703 0.6955 -0.0321 -0.0151 -0.0511 89  CYS A C   
657  C C   B CYS A 87  ? 0.6652 0.6663 0.6898 -0.0332 -0.0157 -0.0486 89  CYS A C   
658  O O   A CYS A 87  ? 0.6634 0.6559 0.7020 -0.0313 -0.0155 -0.0465 89  CYS A O   
659  O O   B CYS A 87  ? 0.6482 0.6453 0.6853 -0.0339 -0.0170 -0.0405 89  CYS A O   
660  C CB  A CYS A 87  ? 0.7264 0.7228 0.7374 -0.0314 -0.0202 -0.0740 89  CYS A CB  
661  C CB  B CYS A 87  ? 0.7168 0.7108 0.7332 -0.0305 -0.0190 -0.0715 89  CYS A CB  
662  S SG  A CYS A 87  ? 0.7888 0.7879 0.7832 -0.0342 -0.0265 -0.0876 89  CYS A SG  
663  S SG  B CYS A 87  ? 0.7480 0.7324 0.7818 -0.0256 -0.0140 -0.0666 89  CYS A SG  
664  N N   . ASP A 88  ? 0.6401 0.6462 0.6571 -0.0305 -0.0096 -0.0478 90  ASP A N   
665  C CA  . ASP A 88  ? 0.5729 0.5769 0.5950 -0.0278 -0.0040 -0.0401 90  ASP A CA  
666  C C   . ASP A 88  ? 0.4835 0.4897 0.5003 -0.0239 0.0015  -0.0453 90  ASP A C   
667  O O   . ASP A 88  ? 0.4781 0.4913 0.4846 -0.0236 0.0021  -0.0517 90  ASP A O   
668  C CB  . ASP A 88  ? 0.6197 0.6287 0.6370 -0.0300 -0.0031 -0.0311 90  ASP A CB  
669  C CG  . ASP A 88  ? 0.7437 0.7541 0.7648 -0.0336 -0.0079 -0.0244 90  ASP A CG  
670  O OD1 . ASP A 88  ? 0.7624 0.7686 0.7939 -0.0343 -0.0115 -0.0235 90  ASP A OD1 
671  O OD2 . ASP A 88  ? 0.7824 0.7984 0.7973 -0.0359 -0.0084 -0.0188 90  ASP A OD2 
672  N N   . TYR A 89  ? 0.3906 0.3922 0.4144 -0.0210 0.0055  -0.0417 91  TYR A N   
673  C CA  . TYR A 89  ? 0.3611 0.3666 0.3806 -0.0183 0.0108  -0.0419 91  TYR A CA  
674  C C   . TYR A 89  ? 0.3257 0.3299 0.3453 -0.0192 0.0132  -0.0327 91  TYR A C   
675  O O   . TYR A 89  ? 0.2980 0.2959 0.3248 -0.0193 0.0125  -0.0275 91  TYR A O   
676  C CB  . TYR A 89  ? 0.3660 0.3673 0.3937 -0.0137 0.0132  -0.0462 91  TYR A CB  
677  C CG  . TYR A 89  ? 0.4341 0.4349 0.4605 -0.0115 0.0117  -0.0571 91  TYR A CG  
678  C CD1 . TYR A 89  ? 0.4801 0.4728 0.5126 -0.0125 0.0064  -0.0617 91  TYR A CD1 
679  C CD2 . TYR A 89  ? 0.4623 0.4706 0.4816 -0.0082 0.0153  -0.0628 91  TYR A CD2 
680  C CE1 . TYR A 89  ? 0.5189 0.5084 0.5492 -0.0103 0.0045  -0.0731 91  TYR A CE1 
681  C CE2 . TYR A 89  ? 0.5002 0.5070 0.5175 -0.0048 0.0146  -0.0740 91  TYR A CE2 
682  C CZ  . TYR A 89  ? 0.5419 0.5379 0.5642 -0.0059 0.0090  -0.0799 91  TYR A CZ  
683  O OH  . TYR A 89  ? 0.6182 0.6099 0.6371 -0.0026 0.0076  -0.0924 91  TYR A OH  
684  N N   . SER A 90  ? 0.2995 0.3095 0.3116 -0.0197 0.0159  -0.0308 92  SER A N   
685  C CA  . SER A 90  ? 0.2992 0.3065 0.3092 -0.0209 0.0178  -0.0234 92  SER A CA  
686  C C   . SER A 90  ? 0.2946 0.3066 0.3019 -0.0201 0.0211  -0.0230 92  SER A C   
687  O O   . SER A 90  ? 0.3213 0.3427 0.3246 -0.0199 0.0219  -0.0263 92  SER A O   
688  C CB  . SER A 90  ? 0.3122 0.3216 0.3150 -0.0250 0.0155  -0.0187 92  SER A CB  
689  O OG  . SER A 90  ? 0.4175 0.4242 0.4239 -0.0259 0.0122  -0.0178 92  SER A OG  
690  N N   . LEU A 91  ? 0.2675 0.2744 0.2765 -0.0195 0.0229  -0.0187 93  LEU A N   
691  C CA  . LEU A 91  ? 0.2613 0.2729 0.2675 -0.0201 0.0249  -0.0166 93  LEU A CA  
692  C C   . LEU A 91  ? 0.2794 0.2864 0.2781 -0.0240 0.0239  -0.0108 93  LEU A C   
693  O O   . LEU A 91  ? 0.2818 0.2793 0.2812 -0.0231 0.0243  -0.0086 93  LEU A O   
694  C CB  . LEU A 91  ? 0.2671 0.2765 0.2812 -0.0165 0.0273  -0.0164 93  LEU A CB  
695  C CG  . LEU A 91  ? 0.3106 0.3276 0.3228 -0.0174 0.0288  -0.0135 93  LEU A CG  
696  C CD1 . LEU A 91  ? 0.3336 0.3617 0.3481 -0.0151 0.0303  -0.0175 93  LEU A CD1 
697  C CD2 . LEU A 91  ? 0.3475 0.3613 0.3653 -0.0155 0.0303  -0.0104 93  LEU A CD2 
698  N N   . PHE A 92  ? 0.2627 0.2763 0.2544 -0.0281 0.0225  -0.0083 94  PHE A N   
699  C CA  . PHE A 92  ? 0.2794 0.2869 0.2639 -0.0326 0.0203  -0.0029 94  PHE A CA  
700  C C   . PHE A 92  ? 0.3030 0.3167 0.2838 -0.0364 0.0197  0.0007  94  PHE A C   
701  O O   . PHE A 92  ? 0.3237 0.3507 0.3067 -0.0363 0.0209  0.0005  94  PHE A O   
702  C CB  . PHE A 92  ? 0.2824 0.2895 0.2632 -0.0357 0.0174  -0.0008 94  PHE A CB  
703  C CG  . PHE A 92  ? 0.3003 0.2970 0.2838 -0.0333 0.0171  -0.0011 94  PHE A CG  
704  C CD1 . PHE A 92  ? 0.3288 0.3264 0.3193 -0.0295 0.0180  -0.0050 94  PHE A CD1 
705  C CD2 . PHE A 92  ? 0.3221 0.3076 0.3020 -0.0347 0.0157  0.0028  94  PHE A CD2 
706  C CE1 . PHE A 92  ? 0.3322 0.3219 0.3270 -0.0273 0.0178  -0.0038 94  PHE A CE1 
707  C CE2 . PHE A 92  ? 0.3402 0.3175 0.3241 -0.0313 0.0162  0.0033  94  PHE A CE2 
708  C CZ  . PHE A 92  ? 0.3479 0.3285 0.3396 -0.0279 0.0172  0.0006  94  PHE A CZ  
709  N N   . LYS A 93  ? 0.3059 0.3102 0.2810 -0.0399 0.0177  0.0042  95  LYS A N   
710  C CA  . LYS A 93  ? 0.3174 0.3269 0.2885 -0.0454 0.0154  0.0089  95  LYS A CA  
711  C C   . LYS A 93  ? 0.3182 0.3400 0.2883 -0.0498 0.0132  0.0127  95  LYS A C   
712  O O   . LYS A 93  ? 0.3083 0.3285 0.2770 -0.0506 0.0119  0.0131  95  LYS A O   
713  C CB  . LYS A 93  ? 0.3290 0.3238 0.2921 -0.0493 0.0122  0.0111  95  LYS A CB  
714  C CG  . LYS A 93  ? 0.3304 0.3171 0.2929 -0.0455 0.0145  0.0085  95  LYS A CG  
715  C CD  . LYS A 93  ? 0.3707 0.3427 0.3231 -0.0488 0.0117  0.0092  95  LYS A CD  
716  C CE  . LYS A 93  ? 0.4187 0.3858 0.3692 -0.0454 0.0141  0.0072  95  LYS A CE  
717  N NZ  . LYS A 93  ? 0.4192 0.3697 0.3574 -0.0473 0.0120  0.0060  95  LYS A NZ  
718  N N   . ASP A 94  ? 0.3302 0.3659 0.3020 -0.0524 0.0132  0.0164  96  ASP A N   
719  C CA  . ASP A 94  ? 0.3443 0.3958 0.3159 -0.0563 0.0120  0.0214  96  ASP A CA  
720  C C   . ASP A 94  ? 0.3762 0.4193 0.3421 -0.0632 0.0066  0.0269  96  ASP A C   
721  O O   . ASP A 94  ? 0.3890 0.4186 0.3509 -0.0675 0.0028  0.0292  96  ASP A O   
722  C CB  . ASP A 94  ? 0.3549 0.4221 0.3301 -0.0584 0.0125  0.0265  96  ASP A CB  
723  C CG  . ASP A 94  ? 0.4846 0.5736 0.4620 -0.0597 0.0138  0.0311  96  ASP A CG  
724  O OD1 . ASP A 94  ? 0.4867 0.5799 0.4623 -0.0577 0.0151  0.0286  96  ASP A OD1 
725  O OD2 . ASP A 94  ? 0.5114 0.6145 0.4923 -0.0628 0.0134  0.0379  96  ASP A OD2 
726  N N   . GLY A 95  ? 0.3976 0.4479 0.3631 -0.0641 0.0060  0.0286  97  GLY A N   
727  C CA  . GLY A 95  ? 0.4234 0.4658 0.3855 -0.0703 0.0007  0.0347  97  GLY A CA  
728  C C   . GLY A 95  ? 0.4535 0.4784 0.4143 -0.0673 0.0001  0.0312  97  GLY A C   
729  O O   . GLY A 95  ? 0.4971 0.5140 0.4563 -0.0715 -0.0042 0.0363  97  GLY A O   
730  N N   . ILE A 96  ? 0.4098 0.4285 0.3726 -0.0602 0.0041  0.0235  98  ILE A N   
731  C CA  . ILE A 96  ? 0.3905 0.3963 0.3542 -0.0568 0.0040  0.0212  98  ILE A CA  
732  C C   . ILE A 96  ? 0.3812 0.3973 0.3485 -0.0529 0.0062  0.0174  98  ILE A C   
733  O O   . ILE A 96  ? 0.3640 0.3860 0.3340 -0.0486 0.0097  0.0117  98  ILE A O   
734  C CB  . ILE A 96  ? 0.3867 0.3759 0.3500 -0.0522 0.0062  0.0165  98  ILE A CB  
735  C CG1 . ILE A 96  ? 0.3813 0.3594 0.3387 -0.0561 0.0038  0.0185  98  ILE A CG1 
736  C CG2 . ILE A 96  ? 0.3866 0.3648 0.3523 -0.0483 0.0066  0.0157  98  ILE A CG2 
737  C CD1 . ILE A 96  ? 0.3972 0.3603 0.3519 -0.0514 0.0064  0.0138  98  ILE A CD1 
738  N N   . GLU A 97  ? 0.3833 0.4011 0.3508 -0.0546 0.0036  0.0208  99  GLU A N   
739  C CA  . GLU A 97  ? 0.3783 0.4040 0.3480 -0.0516 0.0044  0.0171  99  GLU A CA  
740  C C   . GLU A 97  ? 0.3912 0.4043 0.3660 -0.0463 0.0058  0.0129  99  GLU A C   
741  O O   . GLU A 97  ? 0.3843 0.3833 0.3601 -0.0455 0.0054  0.0155  99  GLU A O   
742  C CB  . GLU A 97  ? 0.4154 0.4495 0.3836 -0.0559 0.0006  0.0234  99  GLU A CB  
743  C CG  . GLU A 97  ? 0.4985 0.5483 0.4627 -0.0611 -0.0004 0.0288  99  GLU A CG  
744  C CD  . GLU A 97  ? 0.6281 0.6911 0.5904 -0.0650 -0.0037 0.0350  99  GLU A CD  
745  O OE1 . GLU A 97  ? 0.6469 0.7031 0.6117 -0.0652 -0.0066 0.0379  99  GLU A OE1 
746  O OE2 . GLU A 97  ? 0.6396 0.7209 0.5982 -0.0676 -0.0032 0.0377  99  GLU A OE2 
747  N N   . PRO A 98  ? 0.3858 0.4035 0.3638 -0.0426 0.0074  0.0067  100 PRO A N   
748  C CA  . PRO A 98  ? 0.4085 0.4164 0.3932 -0.0382 0.0084  0.0041  100 PRO A CA  
749  C C   . PRO A 98  ? 0.4097 0.4160 0.3977 -0.0391 0.0052  0.0085  100 PRO A C   
750  O O   . PRO A 98  ? 0.4161 0.4248 0.4088 -0.0376 0.0041  0.0060  100 PRO A O   
751  C CB  . PRO A 98  ? 0.4031 0.4171 0.3904 -0.0352 0.0103  -0.0036 100 PRO A CB  
752  C CG  . PRO A 98  ? 0.3932 0.4214 0.3747 -0.0377 0.0092  -0.0053 100 PRO A CG  
753  C CD  . PRO A 98  ? 0.3899 0.4220 0.3659 -0.0421 0.0084  0.0015  100 PRO A CD  
754  N N   . MET A 99  ? 0.4118 0.4138 0.3979 -0.0417 0.0031  0.0154  101 MET A N   
755  C CA  . MET A 99  ? 0.4429 0.4441 0.4329 -0.0427 -0.0002 0.0217  101 MET A CA  
756  C C   . MET A 99  ? 0.4325 0.4179 0.4240 -0.0409 0.0006  0.0265  101 MET A C   
757  O O   . MET A 99  ? 0.3985 0.3777 0.3845 -0.0428 0.0009  0.0271  101 MET A O   
758  C CB  . MET A 99  ? 0.4798 0.4940 0.4651 -0.0487 -0.0043 0.0268  101 MET A CB  
759  C CG  . MET A 99  ? 0.6045 0.6347 0.5853 -0.0502 -0.0046 0.0213  101 MET A CG  
760  S SD  . MET A 99  ? 0.8739 0.9078 0.8594 -0.0481 -0.0066 0.0163  101 MET A SD  
761  C CE  . MET A 99  ? 0.8639 0.9011 0.8529 -0.0519 -0.0122 0.0274  101 MET A CE  
762  N N   . TRP A 100 ? 0.4585 0.4376 0.4573 -0.0372 0.0008  0.0296  102 TRP A N   
763  C CA  . TRP A 100 ? 0.5019 0.4647 0.5020 -0.0331 0.0031  0.0319  102 TRP A CA  
764  C C   . TRP A 100 ? 0.5117 0.4683 0.5083 -0.0369 -0.0004 0.0381  102 TRP A C   
765  O O   . TRP A 100 ? 0.5053 0.4464 0.4989 -0.0347 0.0011  0.0377  102 TRP A O   
766  C CB  . TRP A 100 ? 0.5171 0.4764 0.5274 -0.0269 0.0053  0.0342  102 TRP A CB  
767  C CG  . TRP A 100 ? 0.5446 0.5066 0.5624 -0.0275 0.0016  0.0428  102 TRP A CG  
768  C CD1 . TRP A 100 ? 0.5569 0.5328 0.5802 -0.0307 -0.0025 0.0463  102 TRP A CD1 
769  C CD2 . TRP A 100 ? 0.5474 0.4975 0.5687 -0.0244 0.0018  0.0492  102 TRP A CD2 
770  N NE1 . TRP A 100 ? 0.5651 0.5402 0.5958 -0.0301 -0.0051 0.0556  102 TRP A NE1 
771  C CE2 . TRP A 100 ? 0.5622 0.5212 0.5926 -0.0258 -0.0023 0.0576  102 TRP A CE2 
772  C CE3 . TRP A 100 ? 0.5621 0.4942 0.5793 -0.0203 0.0048  0.0482  102 TRP A CE3 
773  C CZ2 . TRP A 100 ? 0.5643 0.5152 0.6014 -0.0231 -0.0033 0.0660  102 TRP A CZ2 
774  C CZ3 . TRP A 100 ? 0.5800 0.5023 0.6029 -0.0172 0.0040  0.0550  102 TRP A CZ3 
775  C CH2 . TRP A 100 ? 0.5738 0.5057 0.6075 -0.0183 0.0002  0.0643  102 TRP A CH2 
776  N N   . GLU A 101 ? 0.5088 0.4771 0.5055 -0.0428 -0.0052 0.0437  103 GLU A N   
777  C CA  . GLU A 101 ? 0.5221 0.4870 0.5172 -0.0476 -0.0095 0.0513  103 GLU A CA  
778  C C   . GLU A 101 ? 0.4989 0.4621 0.4854 -0.0526 -0.0103 0.0498  103 GLU A C   
779  O O   . GLU A 101 ? 0.4806 0.4362 0.4662 -0.0565 -0.0141 0.0559  103 GLU A O   
780  C CB  . GLU A 101 ? 0.5471 0.5284 0.5454 -0.0526 -0.0144 0.0591  103 GLU A CB  
781  C CG  . GLU A 101 ? 0.6373 0.6213 0.6450 -0.0489 -0.0149 0.0625  103 GLU A CG  
782  C CD  . GLU A 101 ? 0.7569 0.7546 0.7656 -0.0483 -0.0144 0.0571  103 GLU A CD  
783  O OE1 . GLU A 101 ? 0.8082 0.8121 0.8244 -0.0479 -0.0171 0.0621  103 GLU A OE1 
784  O OE2 . GLU A 101 ? 0.6848 0.6867 0.6875 -0.0483 -0.0118 0.0484  103 GLU A OE2 
785  N N   . ASP A 102 ? 0.4517 0.4216 0.4330 -0.0527 -0.0074 0.0424  104 ASP A N   
786  C CA  . ASP A 102 ? 0.4287 0.3972 0.4032 -0.0572 -0.0082 0.0417  104 ASP A CA  
787  C C   . ASP A 102 ? 0.4535 0.3995 0.4251 -0.0563 -0.0089 0.0418  104 ASP A C   
788  O O   . ASP A 102 ? 0.4575 0.3901 0.4305 -0.0497 -0.0057 0.0381  104 ASP A O   
789  C CB  . ASP A 102 ? 0.4360 0.4125 0.4076 -0.0552 -0.0041 0.0338  104 ASP A CB  
790  C CG  . ASP A 102 ? 0.4671 0.4476 0.4333 -0.0602 -0.0051 0.0344  104 ASP A CG  
791  O OD1 . ASP A 102 ? 0.4547 0.4205 0.4170 -0.0614 -0.0061 0.0341  104 ASP A OD1 
792  O OD2 . ASP A 102 ? 0.4744 0.4728 0.4400 -0.0629 -0.0050 0.0352  104 ASP A OD2 
793  N N   . GLU A 103 ? 0.4701 0.4124 0.4375 -0.0630 -0.0132 0.0460  105 GLU A N   
794  C CA  . GLU A 103 ? 0.4909 0.4103 0.4537 -0.0637 -0.0154 0.0455  105 GLU A CA  
795  C C   . GLU A 103 ? 0.4800 0.3877 0.4371 -0.0576 -0.0104 0.0358  105 GLU A C   
796  O O   . GLU A 103 ? 0.4899 0.3779 0.4441 -0.0531 -0.0093 0.0329  105 GLU A O   
797  C CB  . GLU A 103 ? 0.5599 0.4816 0.5190 -0.0736 -0.0214 0.0511  105 GLU A CB  
798  C CG  . GLU A 103 ? 0.7354 0.6328 0.6889 -0.0765 -0.0259 0.0510  105 GLU A CG  
799  C CD  . GLU A 103 ? 0.9412 0.8285 0.8998 -0.0799 -0.0317 0.0598  105 GLU A CD  
800  O OE1 . GLU A 103 ? 0.9671 0.8546 0.9326 -0.0747 -0.0299 0.0622  105 GLU A OE1 
801  O OE2 . GLU A 103 ? 1.0004 0.8797 0.9570 -0.0882 -0.0386 0.0650  105 GLU A OE2 
802  N N   . LYS A 104 ? 0.4622 0.3827 0.4177 -0.0571 -0.0072 0.0313  106 LYS A N   
803  C CA  . LYS A 104 ? 0.4384 0.3519 0.3894 -0.0521 -0.0027 0.0237  106 LYS A CA  
804  C C   . LYS A 104 ? 0.4167 0.3291 0.3728 -0.0431 0.0031  0.0200  106 LYS A C   
805  O O   . LYS A 104 ? 0.4234 0.3287 0.3760 -0.0383 0.0071  0.0148  106 LYS A O   
806  C CB  . LYS A 104 ? 0.4765 0.4045 0.4256 -0.0552 -0.0019 0.0217  106 LYS A CB  
807  C CG  . LYS A 104 ? 0.5328 0.4622 0.4770 -0.0641 -0.0074 0.0259  106 LYS A CG  
808  C CD  . LYS A 104 ? 0.6575 0.5664 0.5923 -0.0661 -0.0102 0.0235  106 LYS A CD  
809  C CE  . LYS A 104 ? 0.7719 0.6828 0.7030 -0.0764 -0.0170 0.0286  106 LYS A CE  
810  N NZ  . LYS A 104 ? 0.8442 0.7643 0.7724 -0.0781 -0.0161 0.0266  106 LYS A NZ  
811  N N   . ASN A 105 ? 0.4060 0.3261 0.3706 -0.0410 0.0034  0.0232  107 ASN A N   
812  C CA  . ASN A 105 ? 0.4028 0.3234 0.3745 -0.0333 0.0079  0.0215  107 ASN A CA  
813  C C   . ASN A 105 ? 0.4199 0.3294 0.3963 -0.0290 0.0080  0.0255  107 ASN A C   
814  O O   . ASN A 105 ? 0.4292 0.3350 0.4102 -0.0215 0.0127  0.0240  107 ASN A O   
815  C CB  . ASN A 105 ? 0.3741 0.3132 0.3530 -0.0340 0.0079  0.0218  107 ASN A CB  
816  C CG  . ASN A 105 ? 0.3634 0.3130 0.3396 -0.0358 0.0092  0.0171  107 ASN A CG  
817  O OD1 . ASN A 105 ? 0.3830 0.3275 0.3557 -0.0339 0.0119  0.0133  107 ASN A OD1 
818  N ND2 . ASN A 105 ? 0.3540 0.3186 0.3317 -0.0391 0.0074  0.0174  107 ASN A ND2 
819  N N   . LYS A 106 ? 0.4334 0.3384 0.4099 -0.0332 0.0032  0.0312  108 LYS A N   
820  C CA  . LYS A 106 ? 0.4693 0.3669 0.4534 -0.0290 0.0029  0.0366  108 LYS A CA  
821  C C   . LYS A 106 ? 0.4782 0.3569 0.4605 -0.0204 0.0077  0.0332  108 LYS A C   
822  O O   . LYS A 106 ? 0.4941 0.3717 0.4853 -0.0136 0.0106  0.0362  108 LYS A O   
823  C CB  . LYS A 106 ? 0.5152 0.4112 0.5007 -0.0355 -0.0037 0.0447  108 LYS A CB  
824  C CG  . LYS A 106 ? 0.6356 0.5158 0.6124 -0.0401 -0.0073 0.0441  108 LYS A CG  
825  C CD  . LYS A 106 ? 0.7216 0.6054 0.7019 -0.0482 -0.0146 0.0540  108 LYS A CD  
826  C CE  . LYS A 106 ? 0.8150 0.6780 0.7897 -0.0521 -0.0193 0.0550  108 LYS A CE  
827  N NZ  . LYS A 106 ? 0.8759 0.7419 0.8569 -0.0594 -0.0265 0.0667  108 LYS A NZ  
828  N N   . ARG A 107 ? 0.4789 0.3438 0.4498 -0.0204 0.0087  0.0270  109 ARG A N   
829  C CA  . ARG A 107 ? 0.5006 0.3477 0.4667 -0.0117 0.0139  0.0221  109 ARG A CA  
830  C C   . ARG A 107 ? 0.4761 0.3289 0.4404 -0.0058 0.0208  0.0165  109 ARG A C   
831  O O   . ARG A 107 ? 0.4910 0.3309 0.4486 0.0013  0.0258  0.0117  109 ARG A O   
832  C CB  . ARG A 107 ? 0.5568 0.3831 0.5096 -0.0154 0.0101  0.0182  109 ARG A CB  
833  C CG  . ARG A 107 ? 0.6594 0.4766 0.6148 -0.0214 0.0027  0.0247  109 ARG A CG  
834  C CD  . ARG A 107 ? 0.7721 0.5878 0.7405 -0.0152 0.0039  0.0315  109 ARG A CD  
835  N NE  . ARG A 107 ? 0.8844 0.6792 0.8529 -0.0156 -0.0006 0.0348  109 ARG A NE  
836  C CZ  . ARG A 107 ? 0.9185 0.7121 0.8995 -0.0128 -0.0020 0.0433  109 ARG A CZ  
837  N NH1 . ARG A 107 ? 0.9454 0.7181 0.9267 -0.0132 -0.0063 0.0460  109 ARG A NH1 
838  N NH2 . ARG A 107 ? 0.9012 0.7144 0.8951 -0.0101 0.0003  0.0496  109 ARG A NH2 
839  N N   . GLY A 108 ? 0.4480 0.3198 0.4181 -0.0083 0.0211  0.0173  110 GLY A N   
840  C CA  . GLY A 108 ? 0.4419 0.3203 0.4111 -0.0047 0.0262  0.0131  110 GLY A CA  
841  C C   . GLY A 108 ? 0.4358 0.3249 0.4183 0.0014  0.0303  0.0165  110 GLY A C   
842  O O   . GLY A 108 ? 0.4364 0.3242 0.4275 0.0053  0.0308  0.0214  110 GLY A O   
843  N N   . GLY A 109 ? 0.4069 0.3066 0.3918 0.0019  0.0329  0.0145  111 GLY A N   
844  C CA  . GLY A 109 ? 0.3974 0.3083 0.3954 0.0065  0.0362  0.0176  111 GLY A CA  
845  C C   . GLY A 109 ? 0.3906 0.3120 0.3901 0.0043  0.0368  0.0150  111 GLY A C   
846  O O   . GLY A 109 ? 0.3831 0.3059 0.3752 -0.0012 0.0341  0.0113  111 GLY A O   
847  N N   . ARG A 110 ? 0.3600 0.2893 0.3705 0.0087  0.0402  0.0178  112 ARG A N   
848  C CA  . ARG A 110 ? 0.3534 0.2929 0.3693 0.0067  0.0399  0.0166  112 ARG A CA  
849  C C   . ARG A 110 ? 0.3663 0.3093 0.3895 0.0130  0.0456  0.0198  112 ARG A C   
850  O O   . ARG A 110 ? 0.4034 0.3470 0.4343 0.0184  0.0487  0.0248  112 ARG A O   
851  C CB  . ARG A 110 ? 0.3306 0.2802 0.3562 0.0018  0.0346  0.0177  112 ARG A CB  
852  C CG  . ARG A 110 ? 0.4017 0.3564 0.4407 0.0042  0.0340  0.0238  112 ARG A CG  
853  C CD  . ARG A 110 ? 0.4625 0.4261 0.5081 -0.0016 0.0276  0.0240  112 ARG A CD  
854  N NE  . ARG A 110 ? 0.5414 0.5109 0.6009 0.0001  0.0264  0.0308  112 ARG A NE  
855  C CZ  . ARG A 110 ? 0.5512 0.5291 0.6188 -0.0044 0.0206  0.0320  112 ARG A CZ  
856  N NH1 . ARG A 110 ? 0.5682 0.5519 0.6489 -0.0033 0.0190  0.0394  112 ARG A NH1 
857  N NH2 . ARG A 110 ? 0.5211 0.5019 0.5835 -0.0100 0.0162  0.0256  112 ARG A NH2 
858  N N   . TRP A 111 ? 0.3486 0.2950 0.3701 0.0126  0.0472  0.0180  113 TRP A N   
859  C CA  . TRP A 111 ? 0.3317 0.2859 0.3634 0.0164  0.0511  0.0223  113 TRP A CA  
860  C C   . TRP A 111 ? 0.3406 0.3044 0.3876 0.0127  0.0467  0.0246  113 TRP A C   
861  O O   . TRP A 111 ? 0.3418 0.3072 0.3875 0.0075  0.0425  0.0203  113 TRP A O   
862  C CB  . TRP A 111 ? 0.3509 0.3049 0.3743 0.0166  0.0537  0.0201  113 TRP A CB  
863  C CG  . TRP A 111 ? 0.3709 0.3165 0.3799 0.0214  0.0589  0.0184  113 TRP A CG  
864  C CD1 . TRP A 111 ? 0.3828 0.3187 0.3746 0.0191  0.0578  0.0127  113 TRP A CD1 
865  C CD2 . TRP A 111 ? 0.3939 0.3397 0.4040 0.0297  0.0659  0.0222  113 TRP A CD2 
866  N NE1 . TRP A 111 ? 0.4034 0.3316 0.3839 0.0252  0.0633  0.0115  113 TRP A NE1 
867  C CE2 . TRP A 111 ? 0.4116 0.3463 0.4029 0.0324  0.0690  0.0171  113 TRP A CE2 
868  C CE3 . TRP A 111 ? 0.4037 0.3593 0.4292 0.0350  0.0698  0.0298  113 TRP A CE3 
869  C CZ2 . TRP A 111 ? 0.4421 0.3744 0.4279 0.0412  0.0767  0.0182  113 TRP A CZ2 
870  C CZ3 . TRP A 111 ? 0.4275 0.3827 0.4494 0.0438  0.0778  0.0324  113 TRP A CZ3 
871  C CH2 . TRP A 111 ? 0.4377 0.3810 0.4393 0.0474  0.0816  0.0260  113 TRP A CH2 
872  N N   . LEU A 112 ? 0.3518 0.3219 0.4133 0.0153  0.0473  0.0311  114 LEU A N   
873  C CA  . LEU A 112 ? 0.3965 0.3738 0.4722 0.0108  0.0414  0.0330  114 LEU A CA  
874  C C   . LEU A 112 ? 0.4061 0.3911 0.4965 0.0119  0.0424  0.0387  114 LEU A C   
875  O O   . LEU A 112 ? 0.3723 0.3616 0.4687 0.0174  0.0479  0.0457  114 LEU A O   
876  C CB  . LEU A 112 ? 0.4308 0.4098 0.5129 0.0108  0.0389  0.0371  114 LEU A CB  
877  C CG  . LEU A 112 ? 0.4772 0.4640 0.5741 0.0059  0.0321  0.0401  114 LEU A CG  
878  C CD1 . LEU A 112 ? 0.5051 0.4904 0.5957 -0.0009 0.0255  0.0321  114 LEU A CD1 
879  C CD2 . LEU A 112 ? 0.5009 0.4913 0.6055 0.0072  0.0307  0.0471  114 LEU A CD2 
880  N N   . ILE A 113 ? 0.4105 0.3976 0.5073 0.0070  0.0372  0.0361  115 ILE A N   
881  C CA  . ILE A 113 ? 0.4409 0.4343 0.5542 0.0061  0.0357  0.0414  115 ILE A CA  
882  C C   . ILE A 113 ? 0.4084 0.4038 0.5328 0.0009  0.0278  0.0416  115 ILE A C   
883  O O   . ILE A 113 ? 0.3617 0.3531 0.4793 -0.0033 0.0229  0.0336  115 ILE A O   
884  C CB  . ILE A 113 ? 0.5017 0.4931 0.6128 0.0044  0.0351  0.0370  115 ILE A CB  
885  C CG1 . ILE A 113 ? 0.5460 0.5338 0.6407 0.0071  0.0404  0.0336  115 ILE A CG1 
886  C CG2 . ILE A 113 ? 0.5412 0.5384 0.6697 0.0044  0.0346  0.0445  115 ILE A CG2 
887  C CD1 . ILE A 113 ? 0.5847 0.5752 0.6764 0.0129  0.0477  0.0398  115 ILE A CD1 
888  N N   . THR A 114 ? 0.4188 0.4213 0.5601 0.0008  0.0261  0.0507  116 THR A N   
889  C CA  . THR A 114 ? 0.4637 0.4675 0.6152 -0.0057 0.0168  0.0503  116 THR A CA  
890  C C   . THR A 114 ? 0.4828 0.4889 0.6508 -0.0086 0.0129  0.0543  116 THR A C   
891  O O   . THR A 114 ? 0.4777 0.4903 0.6570 -0.0055 0.0171  0.0641  116 THR A O   
892  C CB  . THR A 114 ? 0.5220 0.5322 0.6815 -0.0062 0.0146  0.0578  116 THR A CB  
893  O OG1 . THR A 114 ? 0.5684 0.5761 0.7146 -0.0025 0.0189  0.0561  116 THR A OG1 
894  C CG2 . THR A 114 ? 0.5453 0.5557 0.7103 -0.0143 0.0036  0.0549  116 THR A CG2 
895  N N   . LEU A 115 ? 0.4945 0.4953 0.6638 -0.0143 0.0051  0.0470  117 LEU A N   
896  C CA  . LEU A 115 ? 0.5267 0.5260 0.7111 -0.0178 -0.0001 0.0489  117 LEU A CA  
897  C C   . LEU A 115 ? 0.5644 0.5646 0.7605 -0.0248 -0.0104 0.0506  117 LEU A C   
898  O O   . LEU A 115 ? 0.5738 0.5714 0.7599 -0.0281 -0.0151 0.0432  117 LEU A O   
899  C CB  . LEU A 115 ? 0.5305 0.5203 0.7061 -0.0184 -0.0013 0.0371  117 LEU A CB  
900  C CG  . LEU A 115 ? 0.5513 0.5404 0.7180 -0.0131 0.0068  0.0359  117 LEU A CG  
901  C CD1 . LEU A 115 ? 0.5531 0.5344 0.7177 -0.0140 0.0043  0.0266  117 LEU A CD1 
902  C CD2 . LEU A 115 ? 0.5640 0.5601 0.7422 -0.0098 0.0119  0.0480  117 LEU A CD2 
903  N N   . ASN A 116 ? 0.5786 0.5833 0.7957 -0.0277 -0.0145 0.0610  118 ASN A N   
904  C CA  . ASN A 116 ? 0.6160 0.6207 0.8454 -0.0357 -0.0258 0.0630  118 ASN A CA  
905  C C   . ASN A 116 ? 0.6477 0.6387 0.8736 -0.0410 -0.0344 0.0497  118 ASN A C   
906  O O   . ASN A 116 ? 0.6470 0.6307 0.8694 -0.0382 -0.0315 0.0438  118 ASN A O   
907  C CB  . ASN A 116 ? 0.6504 0.6653 0.9047 -0.0375 -0.0275 0.0797  118 ASN A CB  
908  C CG  . ASN A 116 ? 0.7395 0.7605 1.0074 -0.0449 -0.0374 0.0870  118 ASN A CG  
909  O OD1 . ASN A 116 ? 0.7596 0.7729 1.0235 -0.0521 -0.0479 0.0782  118 ASN A OD1 
910  N ND2 . ASN A 116 ? 0.7596 0.7958 1.0439 -0.0430 -0.0342 0.1037  118 ASN A ND2 
911  N N   . LYS A 117 ? 0.6712 0.6588 0.8973 -0.0483 -0.0451 0.0450  119 LYS A N   
912  C CA  . LYS A 117 ? 0.7068 0.6806 0.9295 -0.0537 -0.0546 0.0317  119 LYS A CA  
913  C C   . LYS A 117 ? 0.7106 0.6743 0.9430 -0.0526 -0.0549 0.0295  119 LYS A C   
914  O O   . LYS A 117 ? 0.7277 0.6804 0.9483 -0.0506 -0.0547 0.0157  119 LYS A O   
915  C CB  . LYS A 117 ? 0.7574 0.7314 0.9909 -0.0634 -0.0678 0.0347  119 LYS A CB  
916  C CG  . LYS A 117 ? 0.8470 0.8276 1.0687 -0.0667 -0.0714 0.0328  119 LYS A CG  
917  C CD  . LYS A 117 ? 0.9251 0.9056 1.1584 -0.0775 -0.0861 0.0359  119 LYS A CD  
918  C CE  . LYS A 117 ? 0.9846 0.9742 1.2088 -0.0814 -0.0903 0.0369  119 LYS A CE  
919  N NZ  . LYS A 117 ? 1.0185 1.0252 1.2550 -0.0783 -0.0845 0.0548  119 LYS A NZ  
920  N N   . GLN A 118 ? 0.6948 0.6631 0.9492 -0.0536 -0.0554 0.0437  120 GLN A N   
921  C CA  . GLN A 118 ? 0.6961 0.6552 0.9626 -0.0533 -0.0569 0.0437  120 GLN A CA  
922  C C   . GLN A 118 ? 0.6791 0.6390 0.9369 -0.0445 -0.0452 0.0420  120 GLN A C   
923  O O   . GLN A 118 ? 0.6822 0.6317 0.9416 -0.0429 -0.0458 0.0356  120 GLN A O   
924  C CB  . GLN A 118 ? 0.7261 0.6916 1.0201 -0.0581 -0.0619 0.0611  120 GLN A CB  
925  C CG  . GLN A 118 ? 0.8273 0.7827 1.1362 -0.0587 -0.0648 0.0626  120 GLN A CG  
926  C CD  . GLN A 118 ? 0.9046 0.8562 1.2385 -0.0679 -0.0773 0.0717  120 GLN A CD  
927  O OE1 . GLN A 118 ? 0.9174 0.8793 1.2634 -0.0737 -0.0826 0.0832  120 GLN A OE1 
928  N NE2 . GLN A 118 ? 0.9273 0.8637 1.2707 -0.0695 -0.0829 0.0675  120 GLN A NE2 
929  N N   . GLN A 119 ? 0.6497 0.6216 0.8982 -0.0389 -0.0349 0.0474  121 GLN A N   
930  C CA  . GLN A 119 ? 0.6267 0.5992 0.8631 -0.0316 -0.0248 0.0442  121 GLN A CA  
931  C C   . GLN A 119 ? 0.6171 0.5797 0.8344 -0.0298 -0.0244 0.0273  121 GLN A C   
932  O O   . GLN A 119 ? 0.6053 0.5678 0.8148 -0.0246 -0.0175 0.0248  121 GLN A O   
933  C CB  . GLN A 119 ? 0.6257 0.6109 0.8546 -0.0264 -0.0149 0.0523  121 GLN A CB  
934  C CG  . GLN A 119 ? 0.6172 0.6143 0.8647 -0.0262 -0.0129 0.0696  121 GLN A CG  
935  C CD  . GLN A 119 ? 0.5845 0.5924 0.8232 -0.0200 -0.0028 0.0757  121 GLN A CD  
936  O OE1 . GLN A 119 ? 0.5691 0.5809 0.8025 -0.0198 -0.0024 0.0760  121 GLN A OE1 
937  N NE2 . GLN A 119 ? 0.5996 0.6123 0.8361 -0.0147 0.0054  0.0806  121 GLN A NE2 
938  N N   . ARG A 120 ? 0.6204 0.5760 0.8298 -0.0340 -0.0317 0.0162  122 ARG A N   
939  C CA  . ARG A 120 ? 0.6469 0.5944 0.8386 -0.0319 -0.0312 0.0002  122 ARG A CA  
940  C C   . ARG A 120 ? 0.6545 0.5917 0.8530 -0.0293 -0.0316 -0.0050 122 ARG A C   
941  O O   . ARG A 120 ? 0.6579 0.5939 0.8459 -0.0241 -0.0257 -0.0118 122 ARG A O   
942  C CB  . ARG A 120 ? 0.6932 0.6355 0.8773 -0.0375 -0.0402 -0.0099 122 ARG A CB  
943  C CG  . ARG A 120 ? 0.7846 0.7234 0.9470 -0.0349 -0.0381 -0.0251 122 ARG A CG  
944  C CD  . ARG A 120 ? 0.8730 0.8114 1.0247 -0.0404 -0.0455 -0.0326 122 ARG A CD  
945  N NE  . ARG A 120 ? 0.9596 0.8866 1.1205 -0.0462 -0.0567 -0.0377 122 ARG A NE  
946  C CZ  . ARG A 120 ? 1.0127 0.9369 1.1657 -0.0522 -0.0657 -0.0453 122 ARG A CZ  
947  N NH1 . ARG A 120 ? 0.9940 0.9060 1.1555 -0.0579 -0.0766 -0.0502 122 ARG A NH1 
948  N NH2 . ARG A 120 ? 1.0306 0.9641 1.1670 -0.0531 -0.0645 -0.0476 122 ARG A NH2 
949  N N   . ARG A 121 ? 0.6468 0.5769 0.8645 -0.0333 -0.0392 -0.0009 123 ARG A N   
950  C CA  . ARG A 121 ? 0.6415 0.5613 0.8699 -0.0310 -0.0403 -0.0032 123 ARG A CA  
951  C C   . ARG A 121 ? 0.6180 0.5467 0.8544 -0.0262 -0.0318 0.0091  123 ARG A C   
952  O O   . ARG A 121 ? 0.6422 0.5672 0.8759 -0.0212 -0.0278 0.0044  123 ARG A O   
953  C CB  . ARG A 121 ? 0.6727 0.5816 0.9210 -0.0376 -0.0519 -0.0009 123 ARG A CB  
954  C CG  . ARG A 121 ? 0.7559 0.6486 0.9961 -0.0413 -0.0615 -0.0181 123 ARG A CG  
955  C CD  . ARG A 121 ? 0.8447 0.7214 1.1050 -0.0460 -0.0723 -0.0180 123 ARG A CD  
956  N NE  . ARG A 121 ? 0.9592 0.8201 1.2110 -0.0506 -0.0827 -0.0343 123 ARG A NE  
957  C CZ  . ARG A 121 ? 1.0274 0.8885 1.2781 -0.0592 -0.0922 -0.0344 123 ARG A CZ  
958  N NH1 . ARG A 121 ? 1.0389 0.9161 1.2985 -0.0637 -0.0922 -0.0181 123 ARG A NH1 
959  N NH2 . ARG A 121 ? 1.0397 0.8856 1.2804 -0.0631 -0.1017 -0.0506 123 ARG A NH2 
960  N N   . SER A 122 ? 0.5843 0.5255 0.8302 -0.0273 -0.0290 0.0248  124 SER A N   
961  C CA  . SER A 122 ? 0.5836 0.5332 0.8368 -0.0232 -0.0218 0.0365  124 SER A CA  
962  C C   . SER A 122 ? 0.5737 0.5308 0.8070 -0.0172 -0.0116 0.0335  124 SER A C   
963  O O   . SER A 122 ? 0.6024 0.5588 0.8346 -0.0133 -0.0077 0.0327  124 SER A O   
964  C CB  . SER A 122 ? 0.6176 0.5788 0.8873 -0.0257 -0.0218 0.0542  124 SER A CB  
965  O OG  . SER A 122 ? 0.6941 0.6641 0.9557 -0.0266 -0.0199 0.0565  124 SER A OG  
966  N N   . ASP A 123 ? 0.5293 0.4930 0.7476 -0.0168 -0.0079 0.0322  125 ASP A N   
967  C CA  . ASP A 123 ? 0.4889 0.4606 0.6916 -0.0122 0.0013  0.0334  125 ASP A CA  
968  C C   . ASP A 123 ? 0.4400 0.4088 0.6209 -0.0107 0.0034  0.0205  125 ASP A C   
969  O O   . ASP A 123 ? 0.4138 0.3871 0.5829 -0.0074 0.0099  0.0207  125 ASP A O   
970  C CB  . ASP A 123 ? 0.5222 0.5045 0.7253 -0.0116 0.0054  0.0442  125 ASP A CB  
971  C CG  . ASP A 123 ? 0.6229 0.6133 0.8448 -0.0116 0.0064  0.0594  125 ASP A CG  
972  O OD1 . ASP A 123 ? 0.6347 0.6238 0.8666 -0.0113 0.0057  0.0629  125 ASP A OD1 
973  O OD2 . ASP A 123 ? 0.6828 0.6819 0.9097 -0.0117 0.0081  0.0687  125 ASP A OD2 
974  N N   . LEU A 124 ? 0.4045 0.3669 0.5801 -0.0135 -0.0021 0.0102  126 LEU A N   
975  C CA  . LEU A 124 ? 0.4042 0.3670 0.5598 -0.0126 0.0001  0.0006  126 LEU A CA  
976  C C   . LEU A 124 ? 0.3623 0.3244 0.5094 -0.0086 0.0047  -0.0053 126 LEU A C   
977  O O   . LEU A 124 ? 0.3500 0.3175 0.4842 -0.0068 0.0101  -0.0047 126 LEU A O   
978  C CB  . LEU A 124 ? 0.4267 0.3842 0.5778 -0.0165 -0.0070 -0.0092 126 LEU A CB  
979  C CG  . LEU A 124 ? 0.4663 0.4260 0.5971 -0.0158 -0.0049 -0.0184 126 LEU A CG  
980  C CD1 . LEU A 124 ? 0.4813 0.4484 0.6045 -0.0166 -0.0021 -0.0121 126 LEU A CD1 
981  C CD2 . LEU A 124 ? 0.4900 0.4438 0.6156 -0.0189 -0.0119 -0.0302 126 LEU A CD2 
982  N N   . ASN A 125 ? 0.3344 0.2899 0.4894 -0.0073 0.0023  -0.0104 127 ASN A N   
983  C CA  . ASN A 125 ? 0.3585 0.3143 0.5077 -0.0030 0.0063  -0.0155 127 ASN A CA  
984  C C   . ASN A 125 ? 0.3403 0.3040 0.4899 -0.0006 0.0126  -0.0055 127 ASN A C   
985  O O   . ASN A 125 ? 0.3409 0.3097 0.4779 0.0012  0.0170  -0.0076 127 ASN A O   
986  C CB  . ASN A 125 ? 0.3924 0.3386 0.5526 -0.0011 0.0026  -0.0221 127 ASN A CB  
987  C CG  . ASN A 125 ? 0.5415 0.4789 0.6970 -0.0030 -0.0034 -0.0348 127 ASN A CG  
988  O OD1 . ASN A 125 ? 0.5815 0.5087 0.7442 -0.0013 -0.0069 -0.0420 127 ASN A OD1 
989  N ND2 . ASN A 125 ? 0.6033 0.5436 0.7464 -0.0065 -0.0052 -0.0382 127 ASN A ND2 
990  N N   . ARG A 126 ? 0.3165 0.2821 0.4797 -0.0011 0.0125  0.0053  128 ARG A N   
991  C CA  . ARG A 126 ? 0.3129 0.2865 0.4756 0.0008  0.0179  0.0149  128 ARG A CA  
992  C C   . ARG A 126 ? 0.2970 0.2766 0.4425 0.0005  0.0224  0.0164  128 ARG A C   
993  O O   . ARG A 126 ? 0.3143 0.2981 0.4496 0.0018  0.0263  0.0169  128 ARG A O   
994  C CB  . ARG A 126 ? 0.3436 0.3200 0.5242 0.0003  0.0171  0.0275  128 ARG A CB  
995  C CG  . ARG A 126 ? 0.4571 0.4436 0.6347 0.0019  0.0229  0.0382  128 ARG A CG  
996  C CD  . ARG A 126 ? 0.5243 0.5140 0.6981 0.0042  0.0256  0.0383  128 ARG A CD  
997  N NE  . ARG A 126 ? 0.5031 0.4888 0.6947 0.0053  0.0223  0.0395  128 ARG A NE  
998  C CZ  . ARG A 126 ? 0.5352 0.5228 0.7285 0.0078  0.0235  0.0394  128 ARG A CZ  
999  N NH1 . ARG A 126 ? 0.5436 0.5380 0.7216 0.0086  0.0276  0.0386  128 ARG A NH1 
1000 N NH2 . ARG A 126 ? 0.5547 0.5371 0.7661 0.0095  0.0203  0.0407  128 ARG A NH2 
1001 N N   . PHE A 127 ? 0.2909 0.2705 0.4345 -0.0014 0.0214  0.0176  129 PHE A N   
1002 C CA  . PHE A 127 ? 0.3082 0.2913 0.4370 -0.0010 0.0254  0.0188  129 PHE A CA  
1003 C C   . PHE A 127 ? 0.2744 0.2561 0.3863 -0.0015 0.0260  0.0098  129 PHE A C   
1004 O O   . PHE A 127 ? 0.2694 0.2534 0.3690 -0.0008 0.0297  0.0109  129 PHE A O   
1005 C CB  . PHE A 127 ? 0.3257 0.3096 0.4582 -0.0022 0.0241  0.0225  129 PHE A CB  
1006 C CG  . PHE A 127 ? 0.3813 0.3708 0.5272 -0.0011 0.0260  0.0346  129 PHE A CG  
1007 C CD1 . PHE A 127 ? 0.4202 0.4129 0.5764 0.0000  0.0272  0.0413  129 PHE A CD1 
1008 C CD2 . PHE A 127 ? 0.4332 0.4263 0.5817 -0.0009 0.0268  0.0401  129 PHE A CD2 
1009 C CE1 . PHE A 127 ? 0.4436 0.4437 0.6124 0.0010  0.0291  0.0536  129 PHE A CE1 
1010 C CE2 . PHE A 127 ? 0.4625 0.4630 0.6236 0.0008  0.0293  0.0520  129 PHE A CE2 
1011 C CZ  . PHE A 127 ? 0.4383 0.4426 0.6097 0.0014  0.0303  0.0587  129 PHE A CZ  
1012 N N   . TRP A 128 ? 0.2855 0.2636 0.3966 -0.0027 0.0223  0.0012  130 TRP A N   
1013 C CA  . TRP A 128 ? 0.2874 0.2665 0.3835 -0.0032 0.0231  -0.0062 130 TRP A CA  
1014 C C   . TRP A 128 ? 0.2926 0.2754 0.3849 -0.0013 0.0264  -0.0058 130 TRP A C   
1015 O O   . TRP A 128 ? 0.2781 0.2640 0.3576 -0.0021 0.0288  -0.0055 130 TRP A O   
1016 C CB  . TRP A 128 ? 0.2868 0.2630 0.3822 -0.0044 0.0188  -0.0156 130 TRP A CB  
1017 C CG  . TRP A 128 ? 0.3278 0.3076 0.4087 -0.0047 0.0199  -0.0222 130 TRP A CG  
1018 C CD1 . TRP A 128 ? 0.3460 0.3267 0.4246 -0.0029 0.0198  -0.0300 130 TRP A CD1 
1019 C CD2 . TRP A 128 ? 0.3346 0.3179 0.4022 -0.0068 0.0210  -0.0211 130 TRP A CD2 
1020 N NE1 . TRP A 128 ? 0.3549 0.3416 0.4197 -0.0040 0.0212  -0.0329 130 TRP A NE1 
1021 C CE2 . TRP A 128 ? 0.3545 0.3423 0.4127 -0.0069 0.0215  -0.0274 130 TRP A CE2 
1022 C CE3 . TRP A 128 ? 0.3476 0.3306 0.4107 -0.0082 0.0222  -0.0151 130 TRP A CE3 
1023 C CZ2 . TRP A 128 ? 0.3756 0.3678 0.4212 -0.0094 0.0219  -0.0270 130 TRP A CZ2 
1024 C CZ3 . TRP A 128 ? 0.3720 0.3572 0.4224 -0.0102 0.0225  -0.0157 130 TRP A CZ3 
1025 C CH2 . TRP A 128 ? 0.3702 0.3602 0.4125 -0.0113 0.0220  -0.0210 130 TRP A CH2 
1026 N N   . LEU A 129 ? 0.2906 0.2730 0.3950 0.0009  0.0262  -0.0047 131 LEU A N   
1027 C CA  . LEU A 129 ? 0.3058 0.2931 0.4088 0.0028  0.0290  -0.0030 131 LEU A CA  
1028 C C   . LEU A 129 ? 0.2988 0.2905 0.3956 0.0019  0.0321  0.0053  131 LEU A C   
1029 O O   . LEU A 129 ? 0.2963 0.2924 0.3831 0.0012  0.0338  0.0054  131 LEU A O   
1030 C CB  . LEU A 129 ? 0.3177 0.3036 0.4369 0.0057  0.0281  -0.0018 131 LEU A CB  
1031 C CG  . LEU A 129 ? 0.3747 0.3673 0.4956 0.0079  0.0308  0.0021  131 LEU A CG  
1032 C CD1 . LEU A 129 ? 0.3880 0.3857 0.4972 0.0083  0.0324  -0.0039 131 LEU A CD1 
1033 C CD2 . LEU A 129 ? 0.3862 0.3759 0.5259 0.0113  0.0294  0.0038  131 LEU A CD2 
1034 N N   . GLU A 130 ? 0.2752 0.2663 0.3779 0.0020  0.0327  0.0123  132 GLU A N   
1035 C CA  . GLU A 130 ? 0.2882 0.2833 0.3833 0.0019  0.0360  0.0192  132 GLU A CA  
1036 C C   . GLU A 130 ? 0.2883 0.2815 0.3641 0.0001  0.0372  0.0154  132 GLU A C   
1037 O O   . GLU A 130 ? 0.2897 0.2850 0.3543 -0.0009 0.0389  0.0172  132 GLU A O   
1038 C CB  . GLU A 130 ? 0.3222 0.3186 0.4261 0.0030  0.0373  0.0273  132 GLU A CB  
1039 C CG  . GLU A 130 ? 0.4509 0.4499 0.5738 0.0041  0.0359  0.0339  132 GLU A CG  
1040 C CD  . GLU A 130 ? 0.5061 0.5107 0.6303 0.0047  0.0369  0.0379  132 GLU A CD  
1041 O OE1 . GLU A 130 ? 0.4818 0.4904 0.5917 0.0041  0.0395  0.0395  132 GLU A OE1 
1042 O OE2 . GLU A 130 ? 0.5881 0.5924 0.7277 0.0058  0.0347  0.0396  132 GLU A OE2 
1043 N N   . THR A 131 ? 0.2824 0.2715 0.3557 -0.0007 0.0357  0.0108  133 THR A N   
1044 C CA  . THR A 131 ? 0.3011 0.2875 0.3591 -0.0025 0.0360  0.0076  133 THR A CA  
1045 C C   . THR A 131 ? 0.2665 0.2555 0.3151 -0.0048 0.0353  0.0039  133 THR A C   
1046 O O   . THR A 131 ? 0.2726 0.2608 0.3089 -0.0066 0.0361  0.0050  133 THR A O   
1047 C CB  . THR A 131 ? 0.3141 0.2973 0.3738 -0.0033 0.0336  0.0043  133 THR A CB  
1048 O OG1 . THR A 131 ? 0.3054 0.2881 0.3750 -0.0015 0.0343  0.0094  133 THR A OG1 
1049 C CG2 . THR A 131 ? 0.3020 0.2823 0.3478 -0.0050 0.0338  0.0025  133 THR A CG2 
1050 N N   . LEU A 132 ? 0.2707 0.2627 0.3254 -0.0045 0.0337  -0.0004 134 LEU A N   
1051 C CA  . LEU A 132 ? 0.2936 0.2909 0.3419 -0.0059 0.0334  -0.0031 134 LEU A CA  
1052 C C   . LEU A 132 ? 0.2967 0.2985 0.3432 -0.0065 0.0348  0.0024  134 LEU A C   
1053 O O   . LEU A 132 ? 0.2915 0.2961 0.3277 -0.0096 0.0343  0.0031  134 LEU A O   
1054 C CB  . LEU A 132 ? 0.2911 0.2914 0.3473 -0.0037 0.0326  -0.0087 134 LEU A CB  
1055 C CG  . LEU A 132 ? 0.3744 0.3713 0.4306 -0.0039 0.0304  -0.0150 134 LEU A CG  
1056 C CD1 . LEU A 132 ? 0.3950 0.3940 0.4566 -0.0011 0.0299  -0.0220 134 LEU A CD1 
1057 C CD2 . LEU A 132 ? 0.4184 0.4156 0.4617 -0.0075 0.0295  -0.0158 134 LEU A CD2 
1058 N N   . LEU A 133 ? 0.2867 0.2896 0.3435 -0.0041 0.0358  0.0072  135 LEU A N   
1059 C CA  . LEU A 133 ? 0.3071 0.3154 0.3624 -0.0049 0.0365  0.0132  135 LEU A CA  
1060 C C   . LEU A 133 ? 0.3018 0.3072 0.3417 -0.0079 0.0369  0.0157  135 LEU A C   
1061 O O   . LEU A 133 ? 0.3327 0.3422 0.3650 -0.0109 0.0360  0.0182  135 LEU A O   
1062 C CB  . LEU A 133 ? 0.3139 0.3249 0.3844 -0.0020 0.0373  0.0190  135 LEU A CB  
1063 C CG  . LEU A 133 ? 0.3307 0.3426 0.4176 0.0015  0.0365  0.0165  135 LEU A CG  
1064 C CD1 . LEU A 133 ? 0.3142 0.3279 0.4165 0.0038  0.0366  0.0237  135 LEU A CD1 
1065 C CD2 . LEU A 133 ? 0.3237 0.3421 0.4095 0.0019  0.0366  0.0139  135 LEU A CD2 
1066 N N   . CYS A 134 ? 0.3019 0.3005 0.3373 -0.0071 0.0380  0.0150  136 CYS A N   
1067 C CA  . CYS A 134 ? 0.3242 0.3172 0.3435 -0.0088 0.0388  0.0153  136 CYS A CA  
1068 C C   . CYS A 134 ? 0.3209 0.3108 0.3277 -0.0131 0.0362  0.0114  136 CYS A C   
1069 O O   . CYS A 134 ? 0.3421 0.3292 0.3359 -0.0163 0.0351  0.0120  136 CYS A O   
1070 C CB  . CYS A 134 ? 0.3545 0.3414 0.3740 -0.0057 0.0411  0.0152  136 CYS A CB  
1071 S SG  . CYS A 134 ? 0.3969 0.3883 0.4273 -0.0015 0.0445  0.0224  136 CYS A SG  
1072 N N   . LEU A 135 ? 0.2881 0.2785 0.2985 -0.0136 0.0349  0.0075  137 LEU A N   
1073 C CA  . LEU A 135 ? 0.3283 0.3176 0.3287 -0.0180 0.0323  0.0052  137 LEU A CA  
1074 C C   . LEU A 135 ? 0.3223 0.3202 0.3214 -0.0215 0.0305  0.0076  137 LEU A C   
1075 O O   . LEU A 135 ? 0.3363 0.3320 0.3242 -0.0260 0.0282  0.0093  137 LEU A O   
1076 C CB  . LEU A 135 ? 0.3170 0.3073 0.3219 -0.0175 0.0315  0.0012  137 LEU A CB  
1077 C CG  . LEU A 135 ? 0.3417 0.3237 0.3427 -0.0171 0.0313  -0.0002 137 LEU A CG  
1078 C CD1 . LEU A 135 ? 0.3485 0.3250 0.3528 -0.0131 0.0339  0.0017  137 LEU A CD1 
1079 C CD2 . LEU A 135 ? 0.3494 0.3352 0.3558 -0.0170 0.0299  -0.0034 137 LEU A CD2 
1080 N N   . ILE A 136 ? 0.3107 0.3180 0.3215 -0.0192 0.0313  0.0079  138 ILE A N   
1081 C CA  . ILE A 136 ? 0.3077 0.3255 0.3197 -0.0217 0.0301  0.0108  138 ILE A CA  
1082 C C   . ILE A 136 ? 0.3304 0.3506 0.3392 -0.0241 0.0290  0.0167  138 ILE A C   
1083 O O   . ILE A 136 ? 0.3296 0.3555 0.3336 -0.0288 0.0264  0.0199  138 ILE A O   
1084 C CB  . ILE A 136 ? 0.3119 0.3391 0.3372 -0.0175 0.0319  0.0092  138 ILE A CB  
1085 C CG1 . ILE A 136 ? 0.3141 0.3424 0.3527 -0.0126 0.0338  0.0113  138 ILE A CG1 
1086 C CG2 . ILE A 136 ? 0.3026 0.3278 0.3283 -0.0157 0.0324  0.0026  138 ILE A CG2 
1087 C CD1 . ILE A 136 ? 0.3479 0.3834 0.4002 -0.0075 0.0355  0.0091  138 ILE A CD1 
1088 N N   . GLY A 137 ? 0.3288 0.3454 0.3403 -0.0213 0.0307  0.0185  139 GLY A N   
1089 C CA  . GLY A 137 ? 0.3466 0.3663 0.3544 -0.0233 0.0297  0.0243  139 GLY A CA  
1090 C C   . GLY A 137 ? 0.3810 0.3916 0.3703 -0.0275 0.0279  0.0235  139 GLY A C   
1091 O O   . GLY A 137 ? 0.3995 0.4123 0.3828 -0.0297 0.0267  0.0277  139 GLY A O   
1092 N N   . GLU A 138 ? 0.3670 0.3667 0.3468 -0.0284 0.0275  0.0182  140 GLU A N   
1093 C CA  . GLU A 138 ? 0.3818 0.3697 0.3432 -0.0318 0.0256  0.0160  140 GLU A CA  
1094 C C   . GLU A 138 ? 0.4087 0.3930 0.3648 -0.0284 0.0286  0.0170  140 GLU A C   
1095 O O   . GLU A 138 ? 0.4086 0.3905 0.3513 -0.0317 0.0266  0.0180  140 GLU A O   
1096 C CB  . GLU A 138 ? 0.4040 0.3943 0.3561 -0.0398 0.0200  0.0183  140 GLU A CB  
1097 C CG  . GLU A 138 ? 0.4581 0.4546 0.4157 -0.0433 0.0174  0.0189  140 GLU A CG  
1098 C CD  . GLU A 138 ? 0.5126 0.4985 0.4636 -0.0449 0.0161  0.0147  140 GLU A CD  
1099 O OE1 . GLU A 138 ? 0.5437 0.5154 0.4808 -0.0472 0.0141  0.0120  140 GLU A OE1 
1100 O OE2 . GLU A 138 ? 0.4921 0.4839 0.4514 -0.0439 0.0169  0.0141  140 GLU A OE2 
1101 N N   . SER A 139 ? 0.4133 0.3976 0.3795 -0.0220 0.0332  0.0169  141 SER A N   
1102 C CA  . SER A 139 ? 0.4355 0.4212 0.4021 -0.0176 0.0371  0.0201  141 SER A CA  
1103 C C   . SER A 139 ? 0.4523 0.4264 0.4017 -0.0160 0.0392  0.0165  141 SER A C   
1104 O O   . SER A 139 ? 0.4572 0.4336 0.4033 -0.0126 0.0426  0.0191  141 SER A O   
1105 C CB  . SER A 139 ? 0.4348 0.4245 0.4196 -0.0119 0.0407  0.0219  141 SER A CB  
1106 O OG  . SER A 139 ? 0.4397 0.4386 0.4409 -0.0120 0.0393  0.0246  141 SER A OG  
1107 N N   . PHE A 140 ? 0.4459 0.4080 0.3844 -0.0179 0.0373  0.0108  142 PHE A N   
1108 C CA  . PHE A 140 ? 0.4481 0.3970 0.3719 -0.0148 0.0398  0.0064  142 PHE A CA  
1109 C C   . PHE A 140 ? 0.4949 0.4341 0.3971 -0.0204 0.0354  0.0027  142 PHE A C   
1110 O O   . PHE A 140 ? 0.5155 0.4397 0.4042 -0.0191 0.0357  -0.0028 142 PHE A O   
1111 C CB  . PHE A 140 ? 0.4127 0.3533 0.3411 -0.0126 0.0404  0.0030  142 PHE A CB  
1112 C CG  . PHE A 140 ? 0.4028 0.3524 0.3512 -0.0085 0.0432  0.0061  142 PHE A CG  
1113 C CD1 . PHE A 140 ? 0.3959 0.3515 0.3526 -0.0026 0.0483  0.0099  142 PHE A CD1 
1114 C CD2 . PHE A 140 ? 0.3918 0.3450 0.3506 -0.0111 0.0402  0.0057  142 PHE A CD2 
1115 C CE1 . PHE A 140 ? 0.3953 0.3580 0.3706 0.0000  0.0495  0.0130  142 PHE A CE1 
1116 C CE2 . PHE A 140 ? 0.3785 0.3388 0.3542 -0.0080 0.0418  0.0076  142 PHE A CE2 
1117 C CZ  . PHE A 140 ? 0.3724 0.3365 0.3566 -0.0029 0.0459  0.0111  142 PHE A CZ  
1118 N N   . ASP A 141 ? 0.5412 0.4883 0.4410 -0.0268 0.0308  0.0060  143 ASP A N   
1119 C CA  . ASP A 141 ? 0.6026 0.5425 0.4834 -0.0343 0.0246  0.0037  143 ASP A CA  
1120 C C   . ASP A 141 ? 0.6156 0.5407 0.4886 -0.0391 0.0196  -0.0014 143 ASP A C   
1121 O O   . ASP A 141 ? 0.6139 0.5441 0.4998 -0.0410 0.0180  0.0007  143 ASP A O   
1122 C CB  . ASP A 141 ? 0.6891 0.6238 0.5520 -0.0316 0.0272  0.0013  143 ASP A CB  
1123 C CG  . ASP A 141 ? 0.8634 0.7916 0.7057 -0.0400 0.0199  -0.0010 143 ASP A CG  
1124 O OD1 . ASP A 141 ? 0.8925 0.8312 0.7398 -0.0480 0.0136  0.0044  143 ASP A OD1 
1125 O OD2 . ASP A 141 ? 0.9148 0.8276 0.7360 -0.0387 0.0203  -0.0082 143 ASP A OD2 
1126 N N   . ASP A 142 ? 0.6259 0.5331 0.4787 -0.0410 0.0170  -0.0077 144 ASP A N   
1127 C CA  . ASP A 142 ? 0.6401 0.5328 0.4875 -0.0461 0.0115  -0.0112 144 ASP A CA  
1128 C C   . ASP A 142 ? 0.5857 0.4737 0.4441 -0.0396 0.0160  -0.0126 144 ASP A C   
1129 O O   . ASP A 142 ? 0.5696 0.4544 0.4328 -0.0439 0.0119  -0.0118 144 ASP A O   
1130 C CB  . ASP A 142 ? 0.7308 0.6031 0.5540 -0.0493 0.0073  -0.0183 144 ASP A CB  
1131 C CG  . ASP A 142 ? 0.9151 0.7906 0.7267 -0.0593 -0.0007 -0.0165 144 ASP A CG  
1132 O OD1 . ASP A 142 ? 0.9434 0.8364 0.7677 -0.0654 -0.0044 -0.0088 144 ASP A OD1 
1133 O OD2 . ASP A 142 ? 1.0017 0.8624 0.7914 -0.0611 -0.0034 -0.0229 144 ASP A OD2 
1134 N N   . TYR A 143 ? 0.5588 0.4483 0.4219 -0.0297 0.0242  -0.0135 145 TYR A N   
1135 C CA  . TYR A 143 ? 0.5442 0.4317 0.4193 -0.0236 0.0283  -0.0135 145 TYR A CA  
1136 C C   . TYR A 143 ? 0.4899 0.3924 0.3845 -0.0253 0.0276  -0.0084 145 TYR A C   
1137 O O   . TYR A 143 ? 0.4889 0.3899 0.3925 -0.0221 0.0292  -0.0082 145 TYR A O   
1138 C CB  . TYR A 143 ? 0.5692 0.4567 0.4453 -0.0131 0.0369  -0.0143 145 TYR A CB  
1139 C CG  . TYR A 143 ? 0.6104 0.4819 0.4655 -0.0097 0.0389  -0.0207 145 TYR A CG  
1140 C CD1 . TYR A 143 ? 0.6430 0.4942 0.4849 -0.0118 0.0350  -0.0268 145 TYR A CD1 
1141 C CD2 . TYR A 143 ? 0.6511 0.5280 0.4987 -0.0049 0.0441  -0.0207 145 TYR A CD2 
1142 C CE1 . TYR A 143 ? 0.6942 0.5286 0.5155 -0.0081 0.0367  -0.0342 145 TYR A CE1 
1143 C CE2 . TYR A 143 ? 0.7008 0.5633 0.5267 -0.0012 0.0462  -0.0277 145 TYR A CE2 
1144 C CZ  . TYR A 143 ? 0.7372 0.5774 0.5494 -0.0026 0.0425  -0.0352 145 TYR A CZ  
1145 O OH  . TYR A 143 ? 0.8236 0.6468 0.6129 0.0013  0.0443  -0.0437 145 TYR A OH  
1146 N N   . SER A 144 ? 0.4640 0.3809 0.3653 -0.0299 0.0251  -0.0044 146 SER A N   
1147 C CA  . SER A 144 ? 0.4342 0.3641 0.3518 -0.0313 0.0243  -0.0009 146 SER A CA  
1148 C C   . SER A 144 ? 0.4212 0.3461 0.3372 -0.0369 0.0192  -0.0013 146 SER A C   
1149 O O   . SER A 144 ? 0.3974 0.3297 0.3246 -0.0365 0.0195  0.0002  146 SER A O   
1150 C CB  . SER A 144 ? 0.4474 0.3929 0.3721 -0.0343 0.0230  0.0035  146 SER A CB  
1151 O OG  . SER A 144 ? 0.4712 0.4247 0.4043 -0.0285 0.0279  0.0056  146 SER A OG  
1152 N N   . ASP A 145 ? 0.4389 0.3513 0.3409 -0.0426 0.0142  -0.0030 147 ASP A N   
1153 C CA  . ASP A 145 ? 0.4679 0.3740 0.3687 -0.0481 0.0090  -0.0023 147 ASP A CA  
1154 C C   . ASP A 145 ? 0.4509 0.3493 0.3564 -0.0426 0.0120  -0.0038 147 ASP A C   
1155 O O   . ASP A 145 ? 0.4590 0.3596 0.3699 -0.0462 0.0088  -0.0011 147 ASP A O   
1156 C CB  . ASP A 145 ? 0.5224 0.4136 0.4072 -0.0555 0.0022  -0.0040 147 ASP A CB  
1157 C CG  . ASP A 145 ? 0.6105 0.5120 0.4927 -0.0633 -0.0028 -0.0003 147 ASP A CG  
1158 O OD1 . ASP A 145 ? 0.6050 0.5258 0.4999 -0.0644 -0.0020 0.0048  147 ASP A OD1 
1159 O OD2 . ASP A 145 ? 0.6935 0.5839 0.5609 -0.0681 -0.0074 -0.0026 147 ASP A OD2 
1160 N N   . ASP A 146 ? 0.4036 0.2954 0.3083 -0.0342 0.0179  -0.0069 148 ASP A N   
1161 C CA  . ASP A 146 ? 0.4092 0.2954 0.3201 -0.0285 0.0208  -0.0071 148 ASP A CA  
1162 C C   . ASP A 146 ? 0.4176 0.3203 0.3453 -0.0265 0.0229  -0.0037 148 ASP A C   
1163 O O   . ASP A 146 ? 0.4305 0.3316 0.3644 -0.0244 0.0233  -0.0024 148 ASP A O   
1164 C CB  . ASP A 146 ? 0.4343 0.3090 0.3396 -0.0196 0.0268  -0.0106 148 ASP A CB  
1165 C CG  . ASP A 146 ? 0.5856 0.4382 0.4763 -0.0202 0.0241  -0.0149 148 ASP A CG  
1166 O OD1 . ASP A 146 ? 0.6600 0.5057 0.5395 -0.0275 0.0183  -0.0166 148 ASP A OD1 
1167 O OD2 . ASP A 146 ? 0.5498 0.3919 0.4417 -0.0132 0.0276  -0.0161 148 ASP A OD2 
1168 N N   . VAL A 147 ? 0.3908 0.3084 0.3255 -0.0274 0.0238  -0.0023 149 VAL A N   
1169 C CA  . VAL A 147 ? 0.3646 0.2953 0.3139 -0.0249 0.0257  -0.0007 149 VAL A CA  
1170 C C   . VAL A 147 ? 0.3461 0.2832 0.2982 -0.0303 0.0215  0.0010  149 VAL A C   
1171 O O   . VAL A 147 ? 0.3842 0.3242 0.3315 -0.0362 0.0179  0.0023  149 VAL A O   
1172 C CB  . VAL A 147 ? 0.3522 0.2943 0.3080 -0.0234 0.0279  -0.0001 149 VAL A CB  
1173 C CG1 . VAL A 147 ? 0.3531 0.3073 0.3233 -0.0217 0.0287  0.0004  149 VAL A CG1 
1174 C CG2 . VAL A 147 ? 0.3606 0.2986 0.3139 -0.0183 0.0321  -0.0003 149 VAL A CG2 
1175 N N   . CYS A 148 ? 0.3328 0.2737 0.2925 -0.0286 0.0218  0.0016  150 CYS A N   
1176 C CA  . CYS A 148 ? 0.3367 0.2869 0.2997 -0.0328 0.0186  0.0033  150 CYS A CA  
1177 C C   . CYS A 148 ? 0.3305 0.2953 0.3023 -0.0315 0.0201  0.0019  150 CYS A C   
1178 O O   . CYS A 148 ? 0.3083 0.2838 0.2803 -0.0350 0.0185  0.0026  150 CYS A O   
1179 C CB  . CYS A 148 ? 0.3347 0.2800 0.2995 -0.0323 0.0173  0.0052  150 CYS A CB  
1180 S SG  . CYS A 148 ? 0.4119 0.3386 0.3670 -0.0340 0.0148  0.0067  150 CYS A SG  
1181 N N   . GLY A 149 ? 0.3270 0.2921 0.3064 -0.0262 0.0231  0.0002  151 GLY A N   
1182 C CA  . GLY A 149 ? 0.3068 0.2821 0.2953 -0.0243 0.0241  -0.0021 151 GLY A CA  
1183 C C   . GLY A 149 ? 0.3150 0.2881 0.3126 -0.0194 0.0261  -0.0026 151 GLY A C   
1184 O O   . GLY A 149 ? 0.3311 0.2963 0.3282 -0.0167 0.0280  -0.0006 151 GLY A O   
1185 N N   . ALA A 150 ? 0.2831 0.2631 0.2890 -0.0183 0.0257  -0.0053 152 ALA A N   
1186 C CA  . ALA A 150 ? 0.2880 0.2669 0.3045 -0.0150 0.0263  -0.0053 152 ALA A CA  
1187 C C   . ALA A 150 ? 0.2764 0.2603 0.2969 -0.0163 0.0231  -0.0086 152 ALA A C   
1188 O O   . ALA A 150 ? 0.2503 0.2405 0.2665 -0.0183 0.0218  -0.0122 152 ALA A O   
1189 C CB  . ALA A 150 ? 0.2376 0.2176 0.2614 -0.0123 0.0285  -0.0053 152 ALA A CB  
1190 N N   . VAL A 151 ? 0.2628 0.2450 0.2912 -0.0152 0.0218  -0.0072 153 VAL A N   
1191 C CA  . VAL A 151 ? 0.3028 0.2888 0.3344 -0.0172 0.0176  -0.0099 153 VAL A CA  
1192 C C   . VAL A 151 ? 0.3225 0.3071 0.3670 -0.0156 0.0164  -0.0101 153 VAL A C   
1193 O O   . VAL A 151 ? 0.3207 0.3023 0.3726 -0.0133 0.0184  -0.0046 153 VAL A O   
1194 C CB  . VAL A 151 ? 0.3101 0.2962 0.3386 -0.0193 0.0153  -0.0059 153 VAL A CB  
1195 C CG1 . VAL A 151 ? 0.3263 0.3177 0.3572 -0.0222 0.0101  -0.0084 153 VAL A CG1 
1196 C CG2 . VAL A 151 ? 0.2957 0.2822 0.3127 -0.0216 0.0158  -0.0045 153 VAL A CG2 
1197 N N   . VAL A 152 ? 0.3290 0.3155 0.3760 -0.0167 0.0132  -0.0161 154 VAL A N   
1198 C CA  . VAL A 152 ? 0.3396 0.3239 0.3988 -0.0169 0.0097  -0.0168 154 VAL A CA  
1199 C C   . VAL A 152 ? 0.3545 0.3413 0.4114 -0.0208 0.0037  -0.0199 154 VAL A C   
1200 O O   . VAL A 152 ? 0.3553 0.3455 0.4026 -0.0223 0.0022  -0.0266 154 VAL A O   
1201 C CB  . VAL A 152 ? 0.3135 0.2950 0.3794 -0.0147 0.0102  -0.0214 154 VAL A CB  
1202 C CG1 . VAL A 152 ? 0.2946 0.2785 0.3520 -0.0142 0.0103  -0.0304 154 VAL A CG1 
1203 C CG2 . VAL A 152 ? 0.3403 0.3178 0.4202 -0.0158 0.0054  -0.0211 154 VAL A CG2 
1204 N N   . ASN A 153 ? 0.3760 0.3627 0.4418 -0.0225 0.0005  -0.0140 155 ASN A N   
1205 C CA  . ASN A 153 ? 0.4205 0.4103 0.4862 -0.0270 -0.0064 -0.0152 155 ASN A CA  
1206 C C   . ASN A 153 ? 0.4685 0.4543 0.5465 -0.0286 -0.0116 -0.0171 155 ASN A C   
1207 O O   . ASN A 153 ? 0.4601 0.4444 0.5519 -0.0276 -0.0110 -0.0097 155 ASN A O   
1208 C CB  . ASN A 153 ? 0.4378 0.4311 0.5065 -0.0279 -0.0070 -0.0056 155 ASN A CB  
1209 C CG  . ASN A 153 ? 0.4471 0.4414 0.5063 -0.0260 -0.0021 -0.0022 155 ASN A CG  
1210 O OD1 . ASN A 153 ? 0.4667 0.4582 0.5292 -0.0224 0.0027  0.0042  155 ASN A OD1 
1211 N ND2 . ASN A 153 ? 0.4186 0.4166 0.4657 -0.0284 -0.0033 -0.0063 155 ASN A ND2 
1212 N N   . VAL A 154 ? 0.5038 0.4878 0.5768 -0.0311 -0.0164 -0.0270 156 VAL A N   
1213 C CA  . VAL A 154 ? 0.5463 0.5239 0.6301 -0.0333 -0.0226 -0.0306 156 VAL A CA  
1214 C C   . VAL A 154 ? 0.5648 0.5458 0.6498 -0.0396 -0.0310 -0.0286 156 VAL A C   
1215 O O   . VAL A 154 ? 0.5588 0.5439 0.6302 -0.0423 -0.0341 -0.0345 156 VAL A O   
1216 C CB  . VAL A 154 ? 0.5737 0.5456 0.6502 -0.0315 -0.0229 -0.0439 156 VAL A CB  
1217 C CG1 . VAL A 154 ? 0.5779 0.5405 0.6644 -0.0344 -0.0307 -0.0491 156 VAL A CG1 
1218 C CG2 . VAL A 154 ? 0.5855 0.5560 0.6626 -0.0254 -0.0147 -0.0439 156 VAL A CG2 
1219 N N   . ARG A 155 ? 0.5793 0.5605 0.6806 -0.0420 -0.0348 -0.0192 157 ARG A N   
1220 C CA  . ARG A 155 ? 0.6075 0.5936 0.7127 -0.0485 -0.0433 -0.0148 157 ARG A CA  
1221 C C   . ARG A 155 ? 0.6314 0.6125 0.7527 -0.0532 -0.0516 -0.0130 157 ARG A C   
1222 O O   . ARG A 155 ? 0.6371 0.6126 0.7709 -0.0508 -0.0496 -0.0106 157 ARG A O   
1223 C CB  . ARG A 155 ? 0.6106 0.6059 0.7213 -0.0474 -0.0401 -0.0011 157 ARG A CB  
1224 C CG  . ARG A 155 ? 0.6473 0.6470 0.7437 -0.0443 -0.0341 -0.0013 157 ARG A CG  
1225 C CD  . ARG A 155 ? 0.6650 0.6697 0.7471 -0.0491 -0.0396 -0.0067 157 ARG A CD  
1226 N NE  . ARG A 155 ? 0.6958 0.7049 0.7658 -0.0464 -0.0338 -0.0052 157 ARG A NE  
1227 C CZ  . ARG A 155 ? 0.7523 0.7595 0.8100 -0.0433 -0.0282 -0.0125 157 ARG A CZ  
1228 N NH1 . ARG A 155 ? 0.7533 0.7544 0.8089 -0.0414 -0.0270 -0.0223 157 ARG A NH1 
1229 N NH2 . ARG A 155 ? 0.7730 0.7844 0.8215 -0.0420 -0.0242 -0.0093 157 ARG A NH2 
1230 N N   . ALA A 156 ? 0.6508 0.6346 0.7721 -0.0605 -0.0617 -0.0132 158 ALA A N   
1231 C CA  . ALA A 156 ? 0.6705 0.6504 0.8075 -0.0671 -0.0719 -0.0102 158 ALA A CA  
1232 C C   . ALA A 156 ? 0.6774 0.6631 0.8373 -0.0657 -0.0691 0.0068  158 ALA A C   
1233 O O   . ALA A 156 ? 0.6844 0.6641 0.8586 -0.0663 -0.0710 0.0089  158 ALA A O   
1234 C CB  . ALA A 156 ? 0.6749 0.6596 0.8062 -0.0756 -0.0830 -0.0116 158 ALA A CB  
1235 N N   . LYS A 157 ? 0.6808 0.6784 0.8441 -0.0633 -0.0643 0.0189  159 LYS A N   
1236 C CA  . LYS A 157 ? 0.6927 0.6987 0.8762 -0.0610 -0.0607 0.0356  159 LYS A CA  
1237 C C   . LYS A 157 ? 0.6900 0.6932 0.8779 -0.0530 -0.0500 0.0382  159 LYS A C   
1238 O O   . LYS A 157 ? 0.7022 0.7103 0.9086 -0.0520 -0.0485 0.0500  159 LYS A O   
1239 C CB  . LYS A 157 ? 0.7530 0.7710 0.9355 -0.0590 -0.0575 0.0455  159 LYS A CB  
1240 C CG  . LYS A 157 ? 0.8525 0.8815 1.0564 -0.0564 -0.0545 0.0634  159 LYS A CG  
1241 C CD  . LYS A 157 ? 0.9401 0.9805 1.1452 -0.0558 -0.0543 0.0730  159 LYS A CD  
1242 C CE  . LYS A 157 ? 0.9884 1.0418 1.2173 -0.0546 -0.0537 0.0914  159 LYS A CE  
1243 N NZ  . LYS A 157 ? 1.0091 1.0737 1.2414 -0.0561 -0.0570 0.1006  159 LYS A NZ  
1244 N N   . GLY A 158 ? 0.6695 0.6667 0.8410 -0.0478 -0.0427 0.0284  160 GLY A N   
1245 C CA  . GLY A 158 ? 0.6445 0.6391 0.8179 -0.0409 -0.0333 0.0299  160 GLY A CA  
1246 C C   . GLY A 158 ? 0.6151 0.6075 0.7691 -0.0354 -0.0250 0.0224  160 GLY A C   
1247 O O   . GLY A 158 ? 0.6349 0.6312 0.7784 -0.0348 -0.0234 0.0225  160 GLY A O   
1248 N N   . ASP A 159 ? 0.5615 0.5479 0.7121 -0.0317 -0.0201 0.0173  161 ASP A N   
1249 C CA  . ASP A 159 ? 0.5126 0.4965 0.6459 -0.0277 -0.0138 0.0094  161 ASP A CA  
1250 C C   . ASP A 159 ? 0.4526 0.4406 0.5822 -0.0222 -0.0048 0.0169  161 ASP A C   
1251 O O   . ASP A 159 ? 0.4330 0.4252 0.5743 -0.0198 -0.0018 0.0271  161 ASP A O   
1252 C CB  . ASP A 159 ? 0.5300 0.5067 0.6632 -0.0260 -0.0127 0.0020  161 ASP A CB  
1253 C CG  . ASP A 159 ? 0.6077 0.5776 0.7456 -0.0304 -0.0213 -0.0059 161 ASP A CG  
1254 O OD1 . ASP A 159 ? 0.6241 0.5930 0.7514 -0.0337 -0.0263 -0.0142 161 ASP A OD1 
1255 O OD2 . ASP A 159 ? 0.6370 0.6021 0.7887 -0.0306 -0.0234 -0.0039 161 ASP A OD2 
1256 N N   . LYS A 160 ? 0.4167 0.4038 0.5302 -0.0203 -0.0009 0.0118  162 LYS A N   
1257 C CA  . LYS A 160 ? 0.4070 0.3949 0.5143 -0.0154 0.0069  0.0166  162 LYS A CA  
1258 C C   . LYS A 160 ? 0.3586 0.3428 0.4533 -0.0136 0.0109  0.0096  162 LYS A C   
1259 O O   . LYS A 160 ? 0.3374 0.3206 0.4230 -0.0159 0.0084  0.0015  162 LYS A O   
1260 C CB  . LYS A 160 ? 0.4549 0.4454 0.5557 -0.0159 0.0065  0.0193  162 LYS A CB  
1261 C CG  . LYS A 160 ? 0.5431 0.5392 0.6571 -0.0169 0.0033  0.0283  162 LYS A CG  
1262 C CD  . LYS A 160 ? 0.6557 0.6539 0.7642 -0.0162 0.0039  0.0322  162 LYS A CD  
1263 C CE  . LYS A 160 ? 0.7670 0.7686 0.8718 -0.0226 -0.0042 0.0292  162 LYS A CE  
1264 N NZ  . LYS A 160 ? 0.8303 0.8346 0.9310 -0.0220 -0.0039 0.0345  162 LYS A NZ  
1265 N N   . ILE A 161 ? 0.3339 0.3172 0.4277 -0.0093 0.0173  0.0133  163 ILE A N   
1266 C CA  . ILE A 161 ? 0.3147 0.2955 0.3962 -0.0079 0.0211  0.0087  163 ILE A CA  
1267 C C   . ILE A 161 ? 0.3050 0.2842 0.3781 -0.0049 0.0262  0.0128  163 ILE A C   
1268 O O   . ILE A 161 ? 0.2821 0.2625 0.3616 -0.0015 0.0294  0.0196  163 ILE A O   
1269 C CB  . ILE A 161 ? 0.3115 0.2921 0.3995 -0.0064 0.0227  0.0087  163 ILE A CB  
1270 C CG1 . ILE A 161 ? 0.3256 0.3050 0.4222 -0.0090 0.0172  0.0036  163 ILE A CG1 
1271 C CG2 . ILE A 161 ? 0.3401 0.3198 0.4162 -0.0052 0.0265  0.0058  163 ILE A CG2 
1272 C CD1 . ILE A 161 ? 0.3364 0.3152 0.4438 -0.0074 0.0180  0.0058  163 ILE A CD1 
1273 N N   . ALA A 162 ? 0.2917 0.2683 0.3508 -0.0058 0.0271  0.0087  164 ALA A N   
1274 C CA  . ALA A 162 ? 0.3060 0.2781 0.3555 -0.0036 0.0308  0.0111  164 ALA A CA  
1275 C C   . ALA A 162 ? 0.3214 0.2904 0.3575 -0.0049 0.0320  0.0071  164 ALA A C   
1276 O O   . ALA A 162 ? 0.3363 0.3081 0.3689 -0.0084 0.0291  0.0026  164 ALA A O   
1277 C CB  . ALA A 162 ? 0.3028 0.2740 0.3506 -0.0047 0.0284  0.0126  164 ALA A CB  
1278 N N   . ILE A 163 ? 0.2956 0.2596 0.3241 -0.0022 0.0361  0.0087  165 ILE A N   
1279 C CA  . ILE A 163 ? 0.2982 0.2579 0.3129 -0.0046 0.0359  0.0058  165 ILE A CA  
1280 C C   . ILE A 163 ? 0.3080 0.2599 0.3144 -0.0048 0.0353  0.0062  165 ILE A C   
1281 O O   . ILE A 163 ? 0.3053 0.2518 0.3118 -0.0002 0.0386  0.0088  165 ILE A O   
1282 C CB  . ILE A 163 ? 0.3046 0.2624 0.3137 -0.0026 0.0395  0.0064  165 ILE A CB  
1283 C CG1 . ILE A 163 ? 0.3264 0.2923 0.3448 -0.0029 0.0393  0.0069  165 ILE A CG1 
1284 C CG2 . ILE A 163 ? 0.2870 0.2386 0.2806 -0.0057 0.0384  0.0039  165 ILE A CG2 
1285 C CD1 . ILE A 163 ? 0.3791 0.3457 0.3926 -0.0016 0.0422  0.0089  165 ILE A CD1 
1286 N N   . TRP A 164 ? 0.3014 0.2532 0.3015 -0.0096 0.0316  0.0043  166 TRP A N   
1287 C CA  . TRP A 164 ? 0.3372 0.2813 0.3298 -0.0113 0.0297  0.0053  166 TRP A CA  
1288 C C   . TRP A 164 ? 0.3627 0.2975 0.3421 -0.0129 0.0300  0.0036  166 TRP A C   
1289 O O   . TRP A 164 ? 0.3495 0.2879 0.3242 -0.0163 0.0289  0.0019  166 TRP A O   
1290 C CB  . TRP A 164 ? 0.3391 0.2898 0.3323 -0.0165 0.0250  0.0054  166 TRP A CB  
1291 C CG  . TRP A 164 ? 0.3394 0.2971 0.3426 -0.0161 0.0233  0.0069  166 TRP A CG  
1292 C CD1 . TRP A 164 ? 0.3303 0.2921 0.3442 -0.0130 0.0245  0.0073  166 TRP A CD1 
1293 C CD2 . TRP A 164 ? 0.3432 0.3050 0.3465 -0.0197 0.0191  0.0090  166 TRP A CD2 
1294 N NE1 . TRP A 164 ? 0.3390 0.3066 0.3589 -0.0148 0.0209  0.0089  166 TRP A NE1 
1295 C CE2 . TRP A 164 ? 0.3529 0.3213 0.3661 -0.0188 0.0178  0.0098  166 TRP A CE2 
1296 C CE3 . TRP A 164 ? 0.3573 0.3189 0.3538 -0.0242 0.0159  0.0110  166 TRP A CE3 
1297 C CZ2 . TRP A 164 ? 0.3609 0.3357 0.3759 -0.0221 0.0134  0.0121  166 TRP A CZ2 
1298 C CZ3 . TRP A 164 ? 0.3813 0.3502 0.3803 -0.0272 0.0121  0.0139  166 TRP A CZ3 
1299 C CH2 . TRP A 164 ? 0.3776 0.3532 0.3852 -0.0261 0.0108  0.0141  166 TRP A CH2 
1300 N N   . THR A 165 ? 0.3630 0.2856 0.3366 -0.0101 0.0312  0.0042  167 THR A N   
1301 C CA  . THR A 165 ? 0.3872 0.2975 0.3469 -0.0118 0.0304  0.0019  167 THR A CA  
1302 C C   . THR A 165 ? 0.4027 0.3024 0.3584 -0.0142 0.0267  0.0033  167 THR A C   
1303 O O   . THR A 165 ? 0.3989 0.2998 0.3626 -0.0125 0.0262  0.0066  167 THR A O   
1304 C CB  . THR A 165 ? 0.4185 0.3215 0.3721 -0.0055 0.0359  -0.0003 167 THR A CB  
1305 O OG1 . THR A 165 ? 0.4604 0.3528 0.4137 0.0008  0.0389  0.0002  167 THR A OG1 
1306 C CG2 . THR A 165 ? 0.4223 0.3373 0.3845 -0.0021 0.0399  0.0010  167 THR A CG2 
1307 N N   . THR A 166 ? 0.4134 0.3028 0.3572 -0.0188 0.0233  0.0013  168 THR A N   
1308 C CA  . THR A 166 ? 0.4034 0.2848 0.3442 -0.0240 0.0178  0.0037  168 THR A CA  
1309 C C   . THR A 166 ? 0.4211 0.2837 0.3586 -0.0187 0.0191  0.0031  168 THR A C   
1310 O O   . THR A 166 ? 0.4043 0.2615 0.3445 -0.0213 0.0151  0.0069  168 THR A O   
1311 C CB  . THR A 166 ? 0.4320 0.3114 0.3630 -0.0327 0.0124  0.0030  168 THR A CB  
1312 O OG1 . THR A 166 ? 0.4911 0.3675 0.4226 -0.0390 0.0064  0.0074  168 THR A OG1 
1313 C CG2 . THR A 166 ? 0.4278 0.2908 0.3444 -0.0318 0.0128  -0.0022 168 THR A CG2 
1314 N N   . GLU A 167 ? 0.4533 0.3064 0.3851 -0.0110 0.0247  -0.0012 169 GLU A N   
1315 C CA  . GLU A 167 ? 0.4772 0.3101 0.4032 -0.0053 0.0262  -0.0033 169 GLU A CA  
1316 C C   . GLU A 167 ? 0.4972 0.3294 0.4258 0.0062  0.0350  -0.0049 169 GLU A C   
1317 O O   . GLU A 167 ? 0.5024 0.3338 0.4223 0.0097  0.0393  -0.0093 169 GLU A O   
1318 C CB  . GLU A 167 ? 0.5146 0.3292 0.4230 -0.0100 0.0221  -0.0090 169 GLU A CB  
1319 C CG  . GLU A 167 ? 0.5894 0.3797 0.4896 -0.0040 0.0232  -0.0130 169 GLU A CG  
1320 C CD  . GLU A 167 ? 0.5909 0.3770 0.5033 -0.0016 0.0219  -0.0072 169 GLU A CD  
1321 O OE1 . GLU A 167 ? 0.6022 0.3872 0.5179 -0.0101 0.0143  -0.0025 169 GLU A OE1 
1322 O OE2 . GLU A 167 ? 0.6033 0.3897 0.5233 0.0087  0.0287  -0.0060 169 GLU A OE2 
1323 N N   . CYS A 168 ? 0.5076 0.3419 0.4487 0.0121  0.0375  -0.0001 170 CYS A N   
1324 C CA  . CYS A 168 ? 0.5539 0.3928 0.5017 0.0229  0.0460  0.0010  170 CYS A CA  
1325 C C   . CYS A 168 ? 0.5780 0.3980 0.5127 0.0319  0.0517  -0.0051 170 CYS A C   
1326 O O   . CYS A 168 ? 0.5799 0.4044 0.5158 0.0408  0.0597  -0.0054 170 CYS A O   
1327 C CB  . CYS A 168 ? 0.5751 0.4249 0.5419 0.0259  0.0465  0.0092  170 CYS A CB  
1328 S SG  . CYS A 168 ? 0.7226 0.5573 0.6933 0.0279  0.0435  0.0130  170 CYS A SG  
1329 N N   . GLU A 169 ? 0.5950 0.3932 0.5161 0.0295  0.0475  -0.0103 171 GLU A N   
1330 C CA  . GLU A 169 ? 0.6121 0.3892 0.5174 0.0376  0.0521  -0.0184 171 GLU A CA  
1331 C C   . GLU A 169 ? 0.6103 0.3826 0.4958 0.0343  0.0518  -0.0265 171 GLU A C   
1332 O O   . GLU A 169 ? 0.6354 0.3908 0.5050 0.0407  0.0555  -0.0344 171 GLU A O   
1333 C CB  . GLU A 169 ? 0.6688 0.4219 0.5694 0.0366  0.0469  -0.0204 171 GLU A CB  
1334 C CG  . GLU A 169 ? 0.7082 0.4636 0.6273 0.0404  0.0470  -0.0120 171 GLU A CG  
1335 C CD  . GLU A 169 ? 0.7076 0.4675 0.6358 0.0547  0.0573  -0.0098 171 GLU A CD  
1336 O OE1 . GLU A 169 ? 0.7048 0.4551 0.6205 0.0640  0.0647  -0.0172 171 GLU A OE1 
1337 O OE2 . GLU A 169 ? 0.7440 0.5178 0.6916 0.0566  0.0579  -0.0003 171 GLU A OE2 
1338 N N   . ASN A 170 ? 0.5825 0.3698 0.4684 0.0245  0.0472  -0.0247 172 ASN A N   
1339 C CA  . ASN A 170 ? 0.5825 0.3709 0.4531 0.0215  0.0474  -0.0301 172 ASN A CA  
1340 C C   . ASN A 170 ? 0.5714 0.3757 0.4463 0.0301  0.0567  -0.0283 172 ASN A C   
1341 O O   . ASN A 170 ? 0.5405 0.3643 0.4247 0.0264  0.0566  -0.0236 172 ASN A O   
1342 C CB  . ASN A 170 ? 0.5877 0.3868 0.4595 0.0087  0.0393  -0.0275 172 ASN A CB  
1343 C CG  . ASN A 170 ? 0.6696 0.4537 0.5325 -0.0012 0.0296  -0.0295 172 ASN A CG  
1344 O OD1 . ASN A 170 ? 0.7155 0.4768 0.5684 0.0005  0.0277  -0.0343 172 ASN A OD1 
1345 N ND2 . ASN A 170 ? 0.6448 0.4410 0.5114 -0.0118 0.0232  -0.0256 172 ASN A ND2 
1346 N N   . ARG A 171 ? 0.5670 0.3624 0.4354 0.0418  0.0648  -0.0319 173 ARG A N   
1347 C CA  . ARG A 171 ? 0.5673 0.3789 0.4418 0.0506  0.0743  -0.0285 173 ARG A CA  
1348 C C   . ARG A 171 ? 0.5653 0.3894 0.4321 0.0461  0.0743  -0.0289 173 ARG A C   
1349 O O   . ARG A 171 ? 0.5535 0.3979 0.4343 0.0468  0.0772  -0.0219 173 ARG A O   
1350 C CB  . ARG A 171 ? 0.6147 0.4147 0.4805 0.0648  0.0839  -0.0330 173 ARG A CB  
1351 C CG  . ARG A 171 ? 0.7352 0.5536 0.6057 0.0740  0.0942  -0.0287 173 ARG A CG  
1352 C CD  . ARG A 171 ? 0.8756 0.6827 0.7332 0.0882  0.1043  -0.0345 173 ARG A CD  
1353 N NE  . ARG A 171 ? 1.0018 0.8029 0.8725 0.0978  0.1087  -0.0315 173 ARG A NE  
1354 C CZ  . ARG A 171 ? 1.0762 0.8958 0.9696 0.1045  0.1147  -0.0208 173 ARG A CZ  
1355 N NH1 . ARG A 171 ? 1.0719 0.9162 0.9778 0.1024  0.1167  -0.0124 173 ARG A NH1 
1356 N NH2 . ARG A 171 ? 1.0984 0.9118 1.0032 0.1130  0.1181  -0.0179 173 ARG A NH2 
1357 N N   . GLU A 172 ? 0.5769 0.3892 0.4226 0.0415  0.0706  -0.0363 174 GLU A N   
1358 C CA  . GLU A 172 ? 0.5949 0.4190 0.4323 0.0376  0.0705  -0.0361 174 GLU A CA  
1359 C C   . GLU A 172 ? 0.5643 0.4059 0.4167 0.0273  0.0642  -0.0291 174 GLU A C   
1360 O O   . GLU A 172 ? 0.5508 0.4100 0.4101 0.0276  0.0670  -0.0240 174 GLU A O   
1361 C CB  . GLU A 172 ? 0.7090 0.5155 0.5187 0.0342  0.0669  -0.0460 174 GLU A CB  
1362 C CG  . GLU A 172 ? 0.8907 0.6802 0.6826 0.0457  0.0742  -0.0545 174 GLU A CG  
1363 C CD  . GLU A 172 ? 1.0833 0.8844 0.8835 0.0600  0.0870  -0.0508 174 GLU A CD  
1364 O OE1 . GLU A 172 ? 1.1063 0.9284 0.9111 0.0617  0.0918  -0.0448 174 GLU A OE1 
1365 O OE2 . GLU A 172 ? 1.1424 0.9321 0.9454 0.0696  0.0921  -0.0529 174 GLU A OE2 
1366 N N   . ALA A 173 ? 0.5496 0.3864 0.4071 0.0187  0.0560  -0.0286 175 ALA A N   
1367 C CA  . ALA A 173 ? 0.5253 0.3781 0.3968 0.0104  0.0509  -0.0227 175 ALA A CA  
1368 C C   . ALA A 173 ? 0.4913 0.3610 0.3845 0.0152  0.0556  -0.0157 175 ALA A C   
1369 O O   . ALA A 173 ? 0.4655 0.3513 0.3679 0.0132  0.0559  -0.0113 175 ALA A O   
1370 C CB  . ALA A 173 ? 0.5211 0.3661 0.3937 0.0017  0.0424  -0.0231 175 ALA A CB  
1371 N N   . VAL A 174 ? 0.4860 0.3519 0.3879 0.0214  0.0588  -0.0143 176 VAL A N   
1372 C CA  . VAL A 174 ? 0.4741 0.3548 0.3972 0.0245  0.0615  -0.0074 176 VAL A CA  
1373 C C   . VAL A 174 ? 0.4635 0.3572 0.3914 0.0309  0.0687  -0.0036 176 VAL A C   
1374 O O   . VAL A 174 ? 0.4480 0.3569 0.3908 0.0290  0.0683  0.0019  176 VAL A O   
1375 C CB  . VAL A 174 ? 0.5033 0.3764 0.4334 0.0297  0.0629  -0.0061 176 VAL A CB  
1376 C CG1 . VAL A 174 ? 0.5308 0.4194 0.4815 0.0342  0.0666  0.0015  176 VAL A CG1 
1377 C CG2 . VAL A 174 ? 0.5114 0.3764 0.4412 0.0221  0.0551  -0.0070 176 VAL A CG2 
1378 N N   . THR A 175 ? 0.4687 0.3560 0.3835 0.0383  0.0750  -0.0065 177 THR A N   
1379 C CA  . THR A 175 ? 0.4915 0.3928 0.4110 0.0448  0.0825  -0.0015 177 THR A CA  
1380 C C   . THR A 175 ? 0.4727 0.3850 0.3900 0.0386  0.0799  0.0003  177 THR A C   
1381 O O   . THR A 175 ? 0.4845 0.4131 0.4159 0.0399  0.0826  0.0078  177 THR A O   
1382 C CB  . THR A 175 ? 0.5625 0.4557 0.4690 0.0559  0.0912  -0.0049 177 THR A CB  
1383 O OG1 . THR A 175 ? 0.6337 0.5106 0.5150 0.0539  0.0892  -0.0144 177 THR A OG1 
1384 C CG2 . THR A 175 ? 0.5602 0.4456 0.4742 0.0627  0.0941  -0.0045 177 THR A CG2 
1385 N N   . HIS A 176 ? 0.4577 0.3618 0.3595 0.0314  0.0741  -0.0052 178 HIS A N   
1386 C CA  . HIS A 176 ? 0.4458 0.3608 0.3466 0.0251  0.0710  -0.0026 178 HIS A CA  
1387 C C   . HIS A 176 ? 0.4240 0.3516 0.3464 0.0202  0.0670  0.0032  178 HIS A C   
1388 O O   . HIS A 176 ? 0.4192 0.3609 0.3522 0.0200  0.0681  0.0093  178 HIS A O   
1389 C CB  . HIS A 176 ? 0.4530 0.3574 0.3347 0.0173  0.0643  -0.0088 178 HIS A CB  
1390 C CG  . HIS A 176 ? 0.5121 0.4289 0.3941 0.0111  0.0609  -0.0049 178 HIS A CG  
1391 N ND1 . HIS A 176 ? 0.5366 0.4617 0.4110 0.0136  0.0647  -0.0024 178 HIS A ND1 
1392 C CD2 . HIS A 176 ? 0.5280 0.4512 0.4179 0.0029  0.0543  -0.0025 178 HIS A CD2 
1393 C CE1 . HIS A 176 ? 0.5441 0.4798 0.4230 0.0067  0.0599  0.0020  178 HIS A CE1 
1394 N NE2 . HIS A 176 ? 0.5426 0.4771 0.4305 0.0004  0.0538  0.0017  178 HIS A NE2 
1395 N N   . ILE A 177 ? 0.4049 0.3270 0.3331 0.0162  0.0621  0.0012  179 ILE A N   
1396 C CA  . ILE A 177 ? 0.4068 0.3391 0.3529 0.0119  0.0583  0.0049  179 ILE A CA  
1397 C C   . ILE A 177 ? 0.4090 0.3527 0.3740 0.0172  0.0626  0.0114  179 ILE A C   
1398 O O   . ILE A 177 ? 0.3980 0.3528 0.3758 0.0153  0.0614  0.0156  179 ILE A O   
1399 C CB  . ILE A 177 ? 0.3786 0.3036 0.3258 0.0075  0.0531  0.0018  179 ILE A CB  
1400 C CG1 . ILE A 177 ? 0.3704 0.2878 0.3030 0.0004  0.0475  -0.0023 179 ILE A CG1 
1401 C CG2 . ILE A 177 ? 0.3591 0.2956 0.3256 0.0052  0.0505  0.0052  179 ILE A CG2 
1402 C CD1 . ILE A 177 ? 0.3719 0.2795 0.3019 -0.0033 0.0430  -0.0048 179 ILE A CD1 
1403 N N   . GLY A 178 ? 0.4114 0.3519 0.3784 0.0238  0.0672  0.0124  180 GLY A N   
1404 C CA  . GLY A 178 ? 0.4207 0.3723 0.4058 0.0286  0.0710  0.0197  180 GLY A CA  
1405 C C   . GLY A 178 ? 0.4118 0.3758 0.4020 0.0305  0.0746  0.0258  180 GLY A C   
1406 O O   . GLY A 178 ? 0.3967 0.3715 0.4047 0.0290  0.0732  0.0319  180 GLY A O   
1407 N N   . ARG A 179 ? 0.4223 0.3840 0.3959 0.0337  0.0789  0.0241  181 ARG A N   
1408 C CA  A ARG A 179 ? 0.4211 0.3950 0.3956 0.0357  0.0828  0.0303  181 ARG A CA  
1409 C CA  B ARG A 179 ? 0.4128 0.3874 0.3891 0.0358  0.0828  0.0309  181 ARG A CA  
1410 C C   . ARG A 179 ? 0.4073 0.3895 0.3906 0.0286  0.0773  0.0336  181 ARG A C   
1411 O O   . ARG A 179 ? 0.3875 0.3825 0.3870 0.0290  0.0782  0.0421  181 ARG A O   
1412 C CB  A ARG A 179 ? 0.4583 0.4257 0.4078 0.0396  0.0874  0.0254  181 ARG A CB  
1413 C CB  B ARG A 179 ? 0.4310 0.4014 0.3849 0.0411  0.0888  0.0275  181 ARG A CB  
1414 C CG  A ARG A 179 ? 0.5099 0.4824 0.4485 0.0348  0.0852  0.0260  181 ARG A CG  
1415 C CG  B ARG A 179 ? 0.4406 0.4271 0.3965 0.0437  0.0936  0.0359  181 ARG A CG  
1416 C CD  A ARG A 179 ? 0.5704 0.5395 0.4852 0.0391  0.0902  0.0223  181 ARG A CD  
1417 C CD  B ARG A 179 ? 0.4921 0.4761 0.4229 0.0452  0.0965  0.0318  181 ARG A CD  
1418 N NE  A ARG A 179 ? 0.5828 0.5549 0.4859 0.0324  0.0856  0.0220  181 ARG A NE  
1419 N NE  B ARG A 179 ? 0.5235 0.5046 0.4445 0.0364  0.0891  0.0285  181 ARG A NE  
1420 C CZ  A ARG A 179 ? 0.5916 0.5513 0.4737 0.0272  0.0807  0.0137  181 ARG A CZ  
1421 C CZ  B ARG A 179 ? 0.5222 0.5163 0.4532 0.0313  0.0858  0.0358  181 ARG A CZ  
1422 N NH1 A ARG A 179 ? 0.4921 0.4330 0.3614 0.0280  0.0795  0.0041  181 ARG A NH1 
1423 N NH1 B ARG A 179 ? 0.5098 0.5198 0.4613 0.0336  0.0887  0.0469  181 ARG A NH1 
1424 N NH2 A ARG A 179 ? 0.6445 0.6105 0.5190 0.0209  0.0763  0.0158  181 ARG A NH2 
1425 N NH2 B ARG A 179 ? 0.5139 0.5053 0.4357 0.0237  0.0793  0.0330  181 ARG A NH2 
1426 N N   . VAL A 180 ? 0.4126 0.3875 0.3858 0.0223  0.0716  0.0275  182 VAL A N   
1427 C CA  . VAL A 180 ? 0.4020 0.3839 0.3821 0.0165  0.0668  0.0299  182 VAL A CA  
1428 C C   . VAL A 180 ? 0.3970 0.3835 0.3993 0.0148  0.0636  0.0326  182 VAL A C   
1429 O O   . VAL A 180 ? 0.3808 0.3765 0.3966 0.0134  0.0622  0.0382  182 VAL A O   
1430 C CB  . VAL A 180 ? 0.4331 0.4077 0.3978 0.0102  0.0616  0.0237  182 VAL A CB  
1431 C CG1 . VAL A 180 ? 0.4418 0.4252 0.4169 0.0050  0.0570  0.0271  182 VAL A CG1 
1432 C CG2 . VAL A 180 ? 0.4734 0.4429 0.4151 0.0109  0.0636  0.0208  182 VAL A CG2 
1433 N N   . TYR A 181 ? 0.3851 0.3647 0.3904 0.0148  0.0621  0.0284  183 TYR A N   
1434 C CA  . TYR A 181 ? 0.3611 0.3438 0.3845 0.0129  0.0585  0.0294  183 TYR A CA  
1435 C C   . TYR A 181 ? 0.3657 0.3577 0.4077 0.0160  0.0607  0.0378  183 TYR A C   
1436 O O   . TYR A 181 ? 0.3593 0.3565 0.4164 0.0137  0.0575  0.0407  183 TYR A O   
1437 C CB  . TYR A 181 ? 0.3389 0.3135 0.3598 0.0125  0.0567  0.0243  183 TYR A CB  
1438 C CG  . TYR A 181 ? 0.3313 0.3078 0.3663 0.0098  0.0522  0.0234  183 TYR A CG  
1439 C CD1 . TYR A 181 ? 0.3545 0.3352 0.3978 0.0064  0.0485  0.0226  183 TYR A CD1 
1440 C CD2 . TYR A 181 ? 0.3667 0.3403 0.4055 0.0107  0.0514  0.0229  183 TYR A CD2 
1441 C CE1 . TYR A 181 ? 0.3699 0.3509 0.4233 0.0042  0.0443  0.0200  183 TYR A CE1 
1442 C CE2 . TYR A 181 ? 0.3670 0.3423 0.4162 0.0075  0.0466  0.0213  183 TYR A CE2 
1443 C CZ  . TYR A 181 ? 0.3758 0.3543 0.4314 0.0043  0.0431  0.0192  183 TYR A CZ  
1444 O OH  . TYR A 181 ? 0.3777 0.3567 0.4408 0.0016  0.0384  0.0160  183 TYR A OH  
1445 N N   . LYS A 182 ? 0.3817 0.3760 0.4232 0.0214  0.0662  0.0420  184 LYS A N   
1446 C CA  . LYS A 182 ? 0.3789 0.3839 0.4389 0.0241  0.0685  0.0518  184 LYS A CA  
1447 C C   . LYS A 182 ? 0.3959 0.4106 0.4626 0.0229  0.0686  0.0588  184 LYS A C   
1448 O O   . LYS A 182 ? 0.4038 0.4252 0.4906 0.0213  0.0660  0.0655  184 LYS A O   
1449 C CB  . LYS A 182 ? 0.4110 0.4183 0.4671 0.0311  0.0756  0.0555  184 LYS A CB  
1450 C CG  . LYS A 182 ? 0.4564 0.4769 0.5332 0.0339  0.0781  0.0672  184 LYS A CG  
1451 C CD  . LYS A 182 ? 0.5402 0.5642 0.6145 0.0417  0.0857  0.0711  184 LYS A CD  
1452 C CE  . LYS A 182 ? 0.6001 0.6397 0.6968 0.0439  0.0880  0.0845  184 LYS A CE  
1453 N NZ  . LYS A 182 ? 0.6458 0.6901 0.7432 0.0521  0.0954  0.0888  184 LYS A NZ  
1454 N N   . GLU A 183 ? 0.3984 0.4134 0.4489 0.0233  0.0710  0.0575  185 GLU A N   
1455 C CA  . GLU A 183 ? 0.4240 0.4486 0.4786 0.0218  0.0708  0.0643  185 GLU A CA  
1456 C C   . GLU A 183 ? 0.4102 0.4339 0.4773 0.0165  0.0641  0.0634  185 GLU A C   
1457 O O   . GLU A 183 ? 0.4003 0.4317 0.4849 0.0157  0.0626  0.0714  185 GLU A O   
1458 C CB  . GLU A 183 ? 0.4857 0.5090 0.5164 0.0222  0.0734  0.0612  185 GLU A CB  
1459 C CG  . GLU A 183 ? 0.6128 0.6479 0.6436 0.0213  0.0742  0.0694  185 GLU A CG  
1460 C CD  . GLU A 183 ? 0.8065 0.8397 0.8109 0.0217  0.0767  0.0654  185 GLU A CD  
1461 O OE1 . GLU A 183 ? 0.8799 0.9000 0.8669 0.0204  0.0751  0.0549  185 GLU A OE1 
1462 O OE2 . GLU A 183 ? 0.8391 0.8837 0.8399 0.0229  0.0796  0.0729  185 GLU A OE2 
1463 N N   . ARG A 184 ? 0.3909 0.4052 0.4497 0.0133  0.0602  0.0538  186 ARG A N   
1464 C CA  . ARG A 184 ? 0.3935 0.4071 0.4627 0.0096  0.0548  0.0518  186 ARG A CA  
1465 C C   . ARG A 184 ? 0.4206 0.4332 0.5102 0.0093  0.0517  0.0526  186 ARG A C   
1466 O O   . ARG A 184 ? 0.4274 0.4415 0.5304 0.0078  0.0482  0.0540  186 ARG A O   
1467 C CB  . ARG A 184 ? 0.4115 0.4176 0.4658 0.0065  0.0522  0.0422  186 ARG A CB  
1468 C CG  . ARG A 184 ? 0.4327 0.4400 0.4697 0.0049  0.0529  0.0421  186 ARG A CG  
1469 C CD  . ARG A 184 ? 0.4384 0.4545 0.4833 0.0030  0.0509  0.0480  186 ARG A CD  
1470 N NE  . ARG A 184 ? 0.4418 0.4567 0.4947 0.0007  0.0469  0.0440  186 ARG A NE  
1471 C CZ  . ARG A 184 ? 0.4684 0.4828 0.5120 -0.0026 0.0444  0.0401  186 ARG A CZ  
1472 N NH1 . ARG A 184 ? 0.4541 0.4677 0.4794 -0.0052 0.0444  0.0395  186 ARG A NH1 
1473 N NH2 . ARG A 184 ? 0.4600 0.4751 0.5125 -0.0034 0.0419  0.0370  186 ARG A NH2 
1474 N N   . LEU A 185 ? 0.4352 0.4451 0.5275 0.0108  0.0524  0.0518  187 LEU A N   
1475 C CA  . LEU A 185 ? 0.4498 0.4593 0.5613 0.0097  0.0486  0.0535  187 LEU A CA  
1476 C C   . LEU A 185 ? 0.4832 0.5017 0.6135 0.0107  0.0494  0.0657  187 LEU A C   
1477 O O   . LEU A 185 ? 0.4839 0.5015 0.6320 0.0087  0.0448  0.0678  187 LEU A O   
1478 C CB  . LEU A 185 ? 0.4299 0.4356 0.5389 0.0105  0.0489  0.0506  187 LEU A CB  
1479 C CG  . LEU A 185 ? 0.4386 0.4358 0.5341 0.0086  0.0466  0.0401  187 LEU A CG  
1480 C CD1 . LEU A 185 ? 0.4411 0.4362 0.5338 0.0103  0.0479  0.0399  187 LEU A CD1 
1481 C CD2 . LEU A 185 ? 0.4230 0.4167 0.5251 0.0051  0.0407  0.0339  187 LEU A CD2 
1482 N N   . GLY A 186 ? 0.5148 0.5418 0.6406 0.0133  0.0546  0.0734  188 GLY A N   
1483 C CA  . GLY A 186 ? 0.5508 0.5890 0.6935 0.0143  0.0560  0.0868  188 GLY A CA  
1484 C C   . GLY A 186 ? 0.6075 0.6504 0.7604 0.0163  0.0579  0.0931  188 GLY A C   
1485 O O   . GLY A 186 ? 0.6002 0.6519 0.7730 0.0156  0.0569  0.1047  188 GLY A O   
1486 N N   . LEU A 187 ? 0.6491 0.6875 0.7903 0.0187  0.0605  0.0871  189 LEU A N   
1487 C CA  . LEU A 187 ? 0.6857 0.7295 0.8383 0.0207  0.0620  0.0936  189 LEU A CA  
1488 C C   . LEU A 187 ? 0.7282 0.7864 0.8825 0.0262  0.0701  0.1056  189 LEU A C   
1489 O O   . LEU A 187 ? 0.7427 0.8023 0.8784 0.0301  0.0762  0.1035  189 LEU A O   
1490 C CB  . LEU A 187 ? 0.6955 0.7307 0.8357 0.0222  0.0627  0.0845  189 LEU A CB  
1491 C CG  . LEU A 187 ? 0.7099 0.7337 0.8495 0.0172  0.0552  0.0742  189 LEU A CG  
1492 C CD1 . LEU A 187 ? 0.7134 0.7315 0.8421 0.0191  0.0565  0.0684  189 LEU A CD1 
1493 C CD2 . LEU A 187 ? 0.7258 0.7508 0.8875 0.0126  0.0480  0.0781  189 LEU A CD2 
1494 N N   . PRO A 188 ? 0.7468 0.8167 0.9225 0.0265  0.0703  0.1185  190 PRO A N   
1495 C CA  . PRO A 188 ? 0.7605 0.8461 0.9364 0.0329  0.0793  0.1300  190 PRO A CA  
1496 C C   . PRO A 188 ? 0.7870 0.8704 0.9442 0.0404  0.0873  0.1241  190 PRO A C   
1497 O O   . PRO A 188 ? 0.8009 0.8743 0.9556 0.0399  0.0847  0.1164  190 PRO A O   
1498 C CB  . PRO A 188 ? 0.7560 0.8536 0.9605 0.0309  0.0766  0.1443  190 PRO A CB  
1499 C CG  . PRO A 188 ? 0.7513 0.8389 0.9704 0.0225  0.0654  0.1410  190 PRO A CG  
1500 C CD  . PRO A 188 ? 0.7348 0.8047 0.9348 0.0210  0.0622  0.1234  190 PRO A CD  
1501 N N   . PRO A 189 ? 0.7913 0.8831 0.9347 0.0475  0.0968  0.1274  191 PRO A N   
1502 C CA  . PRO A 189 ? 0.7963 0.8849 0.9238 0.0558  0.1047  0.1220  191 PRO A CA  
1503 C C   . PRO A 189 ? 0.7714 0.8645 0.9155 0.0585  0.1055  0.1276  191 PRO A C   
1504 O O   . PRO A 189 ? 0.7868 0.8716 0.9196 0.0637  0.1090  0.1205  191 PRO A O   
1505 C CB  . PRO A 189 ? 0.8104 0.9120 0.9262 0.0631  0.1150  0.1280  191 PRO A CB  
1506 C CG  . PRO A 189 ? 0.8074 0.9229 0.9381 0.0584  0.1123  0.1401  191 PRO A CG  
1507 C CD  . PRO A 189 ? 0.7857 0.8900 0.9263 0.0486  0.1009  0.1355  191 PRO A CD  
1508 N N   . LYS A 190 ? 0.7372 0.8427 0.9085 0.0547  0.1015  0.1407  192 LYS A N   
1509 C CA  . LYS A 190 ? 0.7227 0.8346 0.9120 0.0562  0.1010  0.1479  192 LYS A CA  
1510 C C   . LYS A 190 ? 0.7228 0.8186 0.9112 0.0510  0.0926  0.1373  192 LYS A C   
1511 O O   . LYS A 190 ? 0.7243 0.8208 0.9166 0.0546  0.0943  0.1384  192 LYS A O   
1512 C CB  . LYS A 190 ? 0.7276 0.8568 0.9469 0.0518  0.0974  0.1655  192 LYS A CB  
1513 C CG  . LYS A 190 ? 0.7567 0.9067 0.9799 0.0576  0.1067  0.1796  192 LYS A CG  
1514 C CD  . LYS A 190 ? 0.7995 0.9608 1.0457 0.0501  0.1006  0.1934  192 LYS A CD  
1515 C CE  . LYS A 190 ? 0.8480 0.9976 1.0865 0.0434  0.0942  0.1858  192 LYS A CE  
1516 N NZ  . LYS A 190 ? 0.8661 1.0152 1.0785 0.0489  0.1020  0.1796  192 LYS A NZ  
1517 N N   . ILE A 191 ? 0.7191 0.8017 0.9029 0.0430  0.0839  0.1275  193 ILE A N   
1518 C CA  . ILE A 191 ? 0.7224 0.7908 0.9029 0.0381  0.0763  0.1169  193 ILE A CA  
1519 C C   . ILE A 191 ? 0.7383 0.7941 0.8928 0.0428  0.0809  0.1044  193 ILE A C   
1520 O O   . ILE A 191 ? 0.7372 0.7853 0.8753 0.0417  0.0813  0.0964  193 ILE A O   
1521 C CB  . ILE A 191 ? 0.7248 0.7849 0.9105 0.0288  0.0660  0.1114  193 ILE A CB  
1522 C CG1 . ILE A 191 ? 0.7172 0.7873 0.9295 0.0236  0.0604  0.1237  193 ILE A CG1 
1523 C CG2 . ILE A 191 ? 0.7365 0.7835 0.9163 0.0243  0.0589  0.1000  193 ILE A CG2 
1524 C CD1 . ILE A 191 ? 0.7169 0.7955 0.9498 0.0219  0.0569  0.1334  193 ILE A CD1 
1525 N N   . VAL A 192 ? 0.7449 0.7988 0.8968 0.0477  0.0841  0.1037  194 VAL A N   
1526 C CA  . VAL A 192 ? 0.7568 0.7976 0.8856 0.0526  0.0884  0.0928  194 VAL A CA  
1527 C C   . VAL A 192 ? 0.7389 0.7658 0.8617 0.0459  0.0799  0.0825  194 VAL A C   
1528 O O   . VAL A 192 ? 0.7598 0.7891 0.8968 0.0418  0.0738  0.0856  194 VAL A O   
1529 C CB  . VAL A 192 ? 0.7832 0.8284 0.9117 0.0631  0.0974  0.0976  194 VAL A CB  
1530 C CG1 . VAL A 192 ? 0.7965 0.8584 0.9315 0.0702  0.1065  0.1087  194 VAL A CG1 
1531 C CG2 . VAL A 192 ? 0.7863 0.8350 0.9320 0.0621  0.0935  0.1031  194 VAL A CG2 
1532 N N   . ILE A 193 ? 0.6856 0.6993 0.7877 0.0439  0.0787  0.0709  195 ILE A N   
1533 C CA  . ILE A 193 ? 0.6295 0.6312 0.7235 0.0383  0.0719  0.0615  195 ILE A CA  
1534 C C   . ILE A 193 ? 0.5643 0.5565 0.6452 0.0440  0.0761  0.0575  195 ILE A C   
1535 O O   . ILE A 193 ? 0.5504 0.5395 0.6195 0.0509  0.0835  0.0563  195 ILE A O   
1536 C CB  . ILE A 193 ? 0.6490 0.6441 0.7320 0.0318  0.0673  0.0531  195 ILE A CB  
1537 C CG1 . ILE A 193 ? 0.6699 0.6585 0.7321 0.0348  0.0722  0.0477  195 ILE A CG1 
1538 C CG2 . ILE A 193 ? 0.6487 0.6521 0.7464 0.0275  0.0636  0.0576  195 ILE A CG2 
1539 C CD1 . ILE A 193 ? 0.6846 0.6678 0.7362 0.0279  0.0671  0.0402  195 ILE A CD1 
1540 N N   . GLY A 194 ? 0.5309 0.5181 0.6140 0.0412  0.0712  0.0555  196 GLY A N   
1541 C CA  . GLY A 194 ? 0.5043 0.4816 0.5780 0.0459  0.0737  0.0527  196 GLY A CA  
1542 C C   . GLY A 194 ? 0.4753 0.4398 0.5340 0.0399  0.0681  0.0432  196 GLY A C   
1543 O O   . GLY A 194 ? 0.4634 0.4295 0.5240 0.0318  0.0611  0.0404  196 GLY A O   
1544 N N   . TYR A 195 ? 0.4540 0.4057 0.4979 0.0439  0.0712  0.0384  197 TYR A N   
1545 C CA  . TYR A 195 ? 0.4586 0.3979 0.4897 0.0386  0.0658  0.0313  197 TYR A CA  
1546 C C   . TYR A 195 ? 0.4849 0.4200 0.5215 0.0406  0.0644  0.0345  197 TYR A C   
1547 O O   . TYR A 195 ? 0.5004 0.4314 0.5383 0.0495  0.0705  0.0373  197 TYR A O   
1548 C CB  . TYR A 195 ? 0.4505 0.3767 0.4608 0.0401  0.0687  0.0238  197 TYR A CB  
1549 C CG  . TYR A 195 ? 0.4332 0.3472 0.4308 0.0334  0.0625  0.0174  197 TYR A CG  
1550 C CD1 . TYR A 195 ? 0.4743 0.3752 0.4667 0.0356  0.0619  0.0162  197 TYR A CD1 
1551 C CD2 . TYR A 195 ? 0.4512 0.3672 0.4431 0.0252  0.0573  0.0137  197 TYR A CD2 
1552 C CE1 . TYR A 195 ? 0.4871 0.3778 0.4695 0.0286  0.0555  0.0120  197 TYR A CE1 
1553 C CE2 . TYR A 195 ? 0.4807 0.3881 0.4626 0.0186  0.0516  0.0095  197 TYR A CE2 
1554 C CZ  . TYR A 195 ? 0.5080 0.4025 0.4847 0.0200  0.0506  0.0089  197 TYR A CZ  
1555 O OH  . TYR A 195 ? 0.5258 0.4120 0.4935 0.0130  0.0445  0.0061  197 TYR A OH  
1556 N N   . GLN A 196 ? 0.4691 0.4058 0.5092 0.0331  0.0569  0.0344  198 GLN A N   
1557 C CA  . GLN A 196 ? 0.4808 0.4157 0.5272 0.0333  0.0539  0.0387  198 GLN A CA  
1558 C C   . GLN A 196 ? 0.4708 0.3945 0.5044 0.0275  0.0488  0.0335  198 GLN A C   
1559 O O   . GLN A 196 ? 0.4535 0.3792 0.4808 0.0197  0.0439  0.0292  198 GLN A O   
1560 C CB  . GLN A 196 ? 0.5329 0.4823 0.5958 0.0283  0.0482  0.0449  198 GLN A CB  
1561 C CG  . GLN A 196 ? 0.6741 0.6366 0.7525 0.0312  0.0510  0.0511  198 GLN A CG  
1562 C CD  . GLN A 196 ? 0.8403 0.8142 0.9300 0.0232  0.0433  0.0533  198 GLN A CD  
1563 O OE1 . GLN A 196 ? 0.8878 0.8606 0.9710 0.0156  0.0369  0.0480  198 GLN A OE1 
1564 N NE2 . GLN A 196 ? 0.8786 0.8640 0.9855 0.0247  0.0435  0.0613  198 GLN A NE2 
1565 N N   . SER A 197 ? 0.4423 0.3543 0.4728 0.0318  0.0500  0.0347  199 SER A N   
1566 C CA  . SER A 197 ? 0.4553 0.3574 0.4777 0.0262  0.0443  0.0328  199 SER A CA  
1567 C C   . SER A 197 ? 0.4379 0.3529 0.4691 0.0180  0.0367  0.0373  199 SER A C   
1568 O O   . SER A 197 ? 0.4434 0.3697 0.4890 0.0194  0.0362  0.0439  199 SER A O   
1569 C CB  . SER A 197 ? 0.4858 0.3741 0.5087 0.0336  0.0470  0.0354  199 SER A CB  
1570 O OG  . SER A 197 ? 0.5662 0.4469 0.5858 0.0278  0.0405  0.0365  199 SER A OG  
1571 N N   . HIS A 198 ? 0.4228 0.3373 0.4455 0.0094  0.0308  0.0343  200 HIS A N   
1572 C CA  . HIS A 198 ? 0.4253 0.3520 0.4541 0.0022  0.0242  0.0383  200 HIS A CA  
1573 C C   . HIS A 198 ? 0.4771 0.4033 0.5148 0.0036  0.0216  0.0468  200 HIS A C   
1574 O O   . HIS A 198 ? 0.4759 0.4151 0.5239 0.0010  0.0180  0.0523  200 HIS A O   
1575 C CB  . HIS A 198 ? 0.4151 0.3423 0.4326 -0.0061 0.0195  0.0342  200 HIS A CB  
1576 C CG  . HIS A 198 ? 0.4147 0.3462 0.4261 -0.0084 0.0208  0.0272  200 HIS A CG  
1577 N ND1 . HIS A 198 ? 0.4311 0.3723 0.4496 -0.0069 0.0224  0.0259  200 HIS A ND1 
1578 C CD2 . HIS A 198 ? 0.4154 0.3428 0.4155 -0.0120 0.0203  0.0224  200 HIS A CD2 
1579 C CE1 . HIS A 198 ? 0.4220 0.3644 0.4336 -0.0093 0.0231  0.0202  200 HIS A CE1 
1580 N NE2 . HIS A 198 ? 0.4296 0.3648 0.4302 -0.0123 0.0220  0.0182  200 HIS A NE2 
1581 N N   . ALA A 199 ? 0.5231 0.4339 0.5571 0.0075  0.0231  0.0479  201 ALA A N   
1582 C CA  . ALA A 199 ? 0.5643 0.4718 0.6083 0.0109  0.0219  0.0566  201 ALA A CA  
1583 C C   . ALA A 199 ? 0.5947 0.5117 0.6547 0.0181  0.0257  0.0630  201 ALA A C   
1584 O O   . ALA A 199 ? 0.6110 0.5365 0.6828 0.0169  0.0218  0.0720  201 ALA A O   
1585 C CB  . ALA A 199 ? 0.5833 0.4691 0.6201 0.0160  0.0243  0.0545  201 ALA A CB  
1586 N N   . ASP A 200 ? 0.5961 0.5137 0.6574 0.0249  0.0327  0.0599  202 ASP A N   
1587 C CA  . ASP A 200 ? 0.5852 0.5144 0.6634 0.0312  0.0361  0.0675  202 ASP A CA  
1588 C C   . ASP A 200 ? 0.5778 0.5257 0.6644 0.0235  0.0303  0.0704  202 ASP A C   
1589 O O   . ASP A 200 ? 0.5733 0.5326 0.6749 0.0234  0.0275  0.0796  202 ASP A O   
1590 C CB  . ASP A 200 ? 0.6003 0.5256 0.6777 0.0413  0.0458  0.0645  202 ASP A CB  
1591 C CG  . ASP A 200 ? 0.6630 0.5688 0.7322 0.0507  0.0520  0.0614  202 ASP A CG  
1592 O OD1 . ASP A 200 ? 0.7026 0.5995 0.7733 0.0511  0.0492  0.0647  202 ASP A OD1 
1593 O OD2 . ASP A 200 ? 0.6661 0.5654 0.7268 0.0574  0.0595  0.0555  202 ASP A OD2 
1594 N N   . THR A 201 ? 0.5811 0.5321 0.6585 0.0169  0.0281  0.0625  203 THR A N   
1595 C CA  . THR A 201 ? 0.5913 0.5571 0.6746 0.0096  0.0223  0.0631  203 THR A CA  
1596 C C   . THR A 201 ? 0.6440 0.6176 0.7305 0.0027  0.0141  0.0684  203 THR A C   
1597 O O   . THR A 201 ? 0.6571 0.6435 0.7545 -0.0005 0.0096  0.0735  203 THR A O   
1598 C CB  . THR A 201 ? 0.5903 0.5555 0.6620 0.0046  0.0215  0.0532  203 THR A CB  
1599 O OG1 . THR A 201 ? 0.5904 0.5505 0.6601 0.0106  0.0286  0.0498  203 THR A OG1 
1600 C CG2 . THR A 201 ? 0.5873 0.5654 0.6639 -0.0024 0.0155  0.0521  203 THR A CG2 
1601 N N   . ALA A 202 ? 0.6651 0.6316 0.7421 -0.0002 0.0118  0.0676  204 ALA A N   
1602 C CA  . ALA A 202 ? 0.6876 0.6618 0.7658 -0.0070 0.0042  0.0734  204 ALA A CA  
1603 C C   . ALA A 202 ? 0.7077 0.6888 0.8023 -0.0042 0.0023  0.0855  204 ALA A C   
1604 O O   . ALA A 202 ? 0.7166 0.7106 0.8153 -0.0108 -0.0049 0.0907  204 ALA A O   
1605 C CB  . ALA A 202 ? 0.6915 0.6549 0.7590 -0.0090 0.0032  0.0725  204 ALA A CB  
1606 N N   . THR A 203 ? 0.7075 0.6811 0.8110 0.0056  0.0087  0.0900  205 THR A N   
1607 C CA  . THR A 203 ? 0.7024 0.6827 0.8232 0.0095  0.0076  0.1028  205 THR A CA  
1608 C C   . THR A 203 ? 0.6506 0.6442 0.7858 0.0116  0.0087  0.1071  205 THR A C   
1609 O O   . THR A 203 ? 0.6456 0.6357 0.7815 0.0179  0.0158  0.1032  205 THR A O   
1610 C CB  . THR A 203 ? 0.7614 0.7261 0.8849 0.0199  0.0141  0.1060  205 THR A CB  
1611 O OG1 . THR A 203 ? 0.8030 0.7573 0.9208 0.0280  0.0232  0.0981  205 THR A OG1 
1612 C CG2 . THR A 203 ? 0.7844 0.7366 0.8978 0.0165  0.0107  0.1050  205 THR A CG2 
1613 N N   . LYS A 204 ? 0.6041 0.6136 0.7508 0.0058  0.0011  0.1160  206 LYS A N   
1614 C CA  . LYS A 204 ? 0.5769 0.6004 0.7389 0.0056  -0.0001 0.1217  206 LYS A CA  
1615 C C   . LYS A 204 ? 0.5521 0.5807 0.7343 0.0145  0.0035  0.1359  206 LYS A C   
1616 O O   . LYS A 204 ? 0.5193 0.5547 0.7107 0.0126  -0.0018 0.1466  206 LYS A O   
1617 C CB  . LYS A 204 ? 0.5966 0.6345 0.7587 -0.0066 -0.0114 0.1225  206 LYS A CB  
1618 C CG  . LYS A 204 ? 0.6620 0.6963 0.8041 -0.0148 -0.0151 0.1089  206 LYS A CG  
1619 C CD  . LYS A 204 ? 0.7472 0.7773 0.8849 -0.0139 -0.0113 0.0988  206 LYS A CD  
1620 C CE  . LYS A 204 ? 0.8133 0.8483 0.9414 -0.0234 -0.0184 0.0895  206 LYS A CE  
1621 N NZ  . LYS A 204 ? 0.8312 0.8666 0.9650 -0.0231 -0.0172 0.0851  206 LYS A NZ  
1622 N N   . SER A 205 ? 0.5713 0.5979 0.7611 0.0244  0.0127  0.1368  207 SER A N   
1623 C CA  . SER A 205 ? 0.5922 0.6217 0.7998 0.0359  0.0193  0.1488  207 SER A CA  
1624 C C   . SER A 205 ? 0.5878 0.6348 0.8154 0.0381  0.0207  0.1584  207 SER A C   
1625 O O   . SER A 205 ? 0.5770 0.6273 0.8190 0.0496  0.0286  0.1675  207 SER A O   
1626 C CB  . SER A 205 ? 0.6377 0.6486 0.8357 0.0482  0.0310  0.1418  207 SER A CB  
1627 O OG  . SER A 205 ? 0.6992 0.6941 0.8827 0.0464  0.0289  0.1360  207 SER A OG  
1628 N N   . GLY A 206 ? 0.5957 0.6534 0.8246 0.0276  0.0130  0.1568  208 GLY A N   
1629 C CA  . GLY A 206 ? 0.6246 0.6984 0.8724 0.0276  0.0127  0.1658  208 GLY A CA  
1630 C C   . GLY A 206 ? 0.6807 0.7528 0.9204 0.0223  0.0120  0.1558  208 GLY A C   
1631 O O   . GLY A 206 ? 0.6945 0.7607 0.9188 0.0127  0.0053  0.1446  208 GLY A O   
1632 N N   . SER A 207 ? 0.7139 0.7916 0.9646 0.0293  0.0197  0.1603  209 SER A N   
1633 C CA  . SER A 207 ? 0.7520 0.8336 1.0042 0.0245  0.0184  0.1568  209 SER A CA  
1634 C C   . SER A 207 ? 0.8000 0.8662 1.0314 0.0261  0.0241  0.1414  209 SER A C   
1635 O O   . SER A 207 ? 0.8114 0.8785 1.0412 0.0195  0.0202  0.1364  209 SER A O   
1636 C CB  . SER A 207 ? 0.7573 0.8544 1.0324 0.0314  0.0243  0.1709  209 SER A CB  
1637 O OG  . SER A 207 ? 0.8010 0.9018 1.0792 0.0269  0.0232  0.1690  209 SER A OG  
1638 N N   . THR A 208 ? 0.8167 0.8687 1.0328 0.0346  0.0328  0.1343  210 THR A N   
1639 C CA  . THR A 208 ? 0.8328 0.8713 1.0292 0.0354  0.0374  0.1206  210 THR A CA  
1640 C C   . THR A 208 ? 0.8364 0.8579 1.0144 0.0403  0.0419  0.1124  210 THR A C   
1641 O O   . THR A 208 ? 0.8486 0.8681 1.0311 0.0463  0.0443  0.1181  210 THR A O   
1642 C CB  . THR A 208 ? 0.8552 0.8983 1.0570 0.0430  0.0468  0.1232  210 THR A CB  
1643 O OG1 . THR A 208 ? 0.8636 0.9244 1.0876 0.0400  0.0434  0.1351  210 THR A OG1 
1644 C CG2 . THR A 208 ? 0.8632 0.8963 1.0476 0.0404  0.0485  0.1106  210 THR A CG2 
1645 N N   . THR A 209 ? 0.8205 0.8298 0.9790 0.0374  0.0424  0.0995  211 THR A N   
1646 C CA  . THR A 209 ? 0.8147 0.8070 0.9548 0.0412  0.0465  0.0910  211 THR A CA  
1647 C C   . THR A 209 ? 0.8078 0.7938 0.9427 0.0526  0.0581  0.0889  211 THR A C   
1648 O O   . THR A 209 ? 0.8012 0.7949 0.9404 0.0542  0.0619  0.0901  211 THR A O   
1649 C CB  . THR A 209 ? 0.8303 0.8151 0.9532 0.0319  0.0409  0.0793  211 THR A CB  
1650 O OG1 . THR A 209 ? 0.8262 0.8183 0.9528 0.0222  0.0308  0.0809  211 THR A OG1 
1651 C CG2 . THR A 209 ? 0.8469 0.8147 0.9513 0.0341  0.0436  0.0713  211 THR A CG2 
1652 N N   . LYS A 210 ? 0.8056 0.7774 0.9307 0.0601  0.0634  0.0858  212 LYS A N   
1653 C CA  . LYS A 210 ? 0.8082 0.7717 0.9236 0.0705  0.0739  0.0813  212 LYS A CA  
1654 C C   . LYS A 210 ? 0.7959 0.7513 0.8921 0.0654  0.0735  0.0697  212 LYS A C   
1655 O O   . LYS A 210 ? 0.8035 0.7489 0.8869 0.0578  0.0674  0.0622  212 LYS A O   
1656 C CB  . LYS A 210 ? 0.8566 0.8045 0.9660 0.0799  0.0789  0.0800  212 LYS A CB  
1657 C CG  . LYS A 210 ? 0.9202 0.8772 1.0504 0.0873  0.0813  0.0927  212 LYS A CG  
1658 C CD  . LYS A 210 ? 1.0020 0.9420 1.1268 0.0991  0.0880  0.0908  212 LYS A CD  
1659 C CE  . LYS A 210 ? 1.0325 0.9819 1.1794 0.1080  0.0911  0.1043  212 LYS A CE  
1660 N NZ  . LYS A 210 ? 1.0511 0.9947 1.2037 0.1034  0.0829  0.1088  212 LYS A NZ  
1661 N N   . ASN A 211 ? 0.7717 0.7336 0.8676 0.0694  0.0798  0.0697  213 ASN A N   
1662 C CA  . ASN A 211 ? 0.7650 0.7185 0.8422 0.0676  0.0815  0.0598  213 ASN A CA  
1663 C C   . ASN A 211 ? 0.7770 0.7136 0.8377 0.0764  0.0883  0.0532  213 ASN A C   
1664 O O   . ASN A 211 ? 0.7868 0.7250 0.8523 0.0879  0.0969  0.0575  213 ASN A O   
1665 C CB  . ASN A 211 ? 0.7627 0.7297 0.8459 0.0690  0.0857  0.0634  213 ASN A CB  
1666 C CG  . ASN A 211 ? 0.7821 0.7622 0.8795 0.0593  0.0780  0.0678  213 ASN A CG  
1667 O OD1 . ASN A 211 ? 0.7726 0.7497 0.8684 0.0502  0.0693  0.0640  213 ASN A OD1 
1668 N ND2 . ASN A 211 ? 0.8051 0.7999 0.9163 0.0607  0.0805  0.0756  213 ASN A ND2 
1669 N N   . ARG A 212 ? 0.7787 0.6988 0.8201 0.0717  0.0848  0.0430  214 ARG A N   
1670 C CA  . ARG A 212 ? 0.8046 0.7070 0.8278 0.0794  0.0908  0.0353  214 ARG A CA  
1671 C C   . ARG A 212 ? 0.7948 0.6982 0.8042 0.0818  0.0964  0.0300  214 ARG A C   
1672 O O   . ARG A 212 ? 0.8099 0.7032 0.8065 0.0909  0.1037  0.0251  214 ARG A O   
1673 C CB  . ARG A 212 ? 0.8628 0.7457 0.8726 0.0740  0.0844  0.0280  214 ARG A CB  
1674 C CG  . ARG A 212 ? 0.9283 0.8101 0.9278 0.0617  0.0766  0.0224  214 ARG A CG  
1675 C CD  . ARG A 212 ? 0.9896 0.8530 0.9774 0.0571  0.0708  0.0170  214 ARG A CD  
1676 N NE  . ARG A 212 ? 1.0507 0.8946 1.0202 0.0633  0.0752  0.0088  214 ARG A NE  
1677 C CZ  . ARG A 212 ? 1.0747 0.8978 1.0337 0.0624  0.0717  0.0040  214 ARG A CZ  
1678 N NH1 . ARG A 212 ? 1.0673 0.8719 1.0085 0.0682  0.0755  -0.0046 214 ARG A NH1 
1679 N NH2 . ARG A 212 ? 1.0726 0.8933 1.0387 0.0555  0.0639  0.0079  214 ARG A NH2 
1680 N N   . PHE A 213 ? 0.7622 0.6777 0.7741 0.0738  0.0928  0.0309  215 PHE A N   
1681 C CA  . PHE A 213 ? 0.7448 0.6660 0.7481 0.0761  0.0981  0.0292  215 PHE A CA  
1682 C C   . PHE A 213 ? 0.7304 0.6726 0.7521 0.0724  0.0970  0.0380  215 PHE A C   
1683 O O   . PHE A 213 ? 0.7038 0.6528 0.7396 0.0651  0.0899  0.0419  215 PHE A O   
1684 C CB  . PHE A 213 ? 0.7342 0.6437 0.7164 0.0690  0.0937  0.0192  215 PHE A CB  
1685 C CG  . PHE A 213 ? 0.7465 0.6336 0.7115 0.0684  0.0909  0.0104  215 PHE A CG  
1686 C CD1 . PHE A 213 ? 0.7718 0.6449 0.7229 0.0783  0.0977  0.0051  215 PHE A CD1 
1687 C CD2 . PHE A 213 ? 0.7514 0.6314 0.7146 0.0584  0.0816  0.0076  215 PHE A CD2 
1688 C CE1 . PHE A 213 ? 0.7915 0.6418 0.7279 0.0772  0.0941  -0.0031 215 PHE A CE1 
1689 C CE2 . PHE A 213 ? 0.7761 0.6354 0.7246 0.0568  0.0781  0.0007  215 PHE A CE2 
1690 C CZ  . PHE A 213 ? 0.7956 0.6390 0.7311 0.0659  0.0839  -0.0047 215 PHE A CZ  
1691 N N   . VAL A 214 ? 0.7333 0.6857 0.7544 0.0774  0.1038  0.0413  216 VAL A N   
1692 C CA  . VAL A 214 ? 0.7494 0.7207 0.7872 0.0739  0.1029  0.0501  216 VAL A CA  
1693 C C   . VAL A 214 ? 0.7774 0.7514 0.8023 0.0733  0.1057  0.0475  216 VAL A C   
1694 O O   . VAL A 214 ? 0.7973 0.7643 0.8040 0.0797  0.1120  0.0423  216 VAL A O   
1695 C CB  . VAL A 214 ? 0.7559 0.7432 0.8140 0.0818  0.1092  0.0623  216 VAL A CB  
1696 C CG1 . VAL A 214 ? 0.7672 0.7735 0.8408 0.0791  0.1094  0.0721  216 VAL A CG1 
1697 C CG2 . VAL A 214 ? 0.7581 0.7460 0.8322 0.0800  0.1043  0.0668  216 VAL A CG2 
1698 N N   . VAL A 215 ? 0.7707 0.7546 0.8049 0.0656  0.1007  0.0512  217 VAL A N   
1699 C CA  . VAL A 215 ? 0.7913 0.7826 0.8191 0.0652  0.1034  0.0527  217 VAL A CA  
1700 C C   . VAL A 215 ? 0.8006 0.8098 0.8521 0.0619  0.1014  0.0642  217 VAL A C   
1701 O O   . VAL A 215 ? 0.8112 0.8317 0.8633 0.0638  0.1056  0.0701  217 VAL A O   
1702 C CB  . VAL A 215 ? 0.8148 0.7955 0.8248 0.0578  0.0978  0.0433  217 VAL A CB  
1703 C CG1 . VAL A 215 ? 0.8487 0.8105 0.8352 0.0598  0.0985  0.0322  217 VAL A CG1 
1704 C CG2 . VAL A 215 ? 0.8076 0.7884 0.8289 0.0481  0.0883  0.0426  217 VAL A CG2 
1705 O OXT . VAL A 215 ? 0.7709 0.7827 0.8401 0.0568  0.0951  0.0675  217 VAL A OXT 
1706 N N   . HIS B 7   ? 0.8798 0.8641 0.6912 -0.0131 0.0190  0.0035  9   HIS B N   
1707 C CA  . HIS B 7   ? 0.8815 0.8618 0.6790 -0.0142 0.0169  0.0113  9   HIS B CA  
1708 C C   . HIS B 7   ? 0.8497 0.8124 0.6401 -0.0110 0.0162  0.0194  9   HIS B C   
1709 O O   . HIS B 7   ? 0.8563 0.8163 0.6412 -0.0059 0.0129  0.0246  9   HIS B O   
1710 C CB  . HIS B 7   ? 0.9173 0.9124 0.7102 -0.0132 0.0128  0.0115  9   HIS B CB  
1711 C CG  . HIS B 7   ? 0.9761 0.9852 0.7713 -0.0180 0.0141  0.0046  9   HIS B CG  
1712 N ND1 . HIS B 7   ? 1.0067 1.0133 0.7973 -0.0230 0.0172  0.0051  9   HIS B ND1 
1713 C CD2 . HIS B 7   ? 1.0011 1.0264 0.8025 -0.0184 0.0131  -0.0032 9   HIS B CD2 
1714 C CE1 . HIS B 7   ? 1.0184 1.0390 0.8124 -0.0254 0.0180  -0.0023 9   HIS B CE1 
1715 N NE2 . HIS B 7   ? 1.0178 1.0493 0.8179 -0.0232 0.0156  -0.0077 9   HIS B NE2 
1716 N N   . GLY B 8   ? 0.8178 0.7685 0.6080 -0.0139 0.0196  0.0201  10  GLY B N   
1717 C CA  . GLY B 8   ? 0.8035 0.7373 0.5915 -0.0111 0.0204  0.0242  10  GLY B CA  
1718 C C   . GLY B 8   ? 0.7791 0.7141 0.5802 -0.0077 0.0223  0.0186  10  GLY B C   
1719 O O   . GLY B 8   ? 0.7983 0.7205 0.5990 -0.0053 0.0236  0.0207  10  GLY B O   
1720 N N   . ALA B 9   ? 0.7449 0.6947 0.5571 -0.0078 0.0228  0.0113  11  ALA B N   
1721 C CA  . ALA B 9   ? 0.7160 0.6674 0.5403 -0.0050 0.0246  0.0065  11  ALA B CA  
1722 C C   . ALA B 9   ? 0.7005 0.6452 0.5297 -0.0083 0.0294  0.0036  11  ALA B C   
1723 O O   . ALA B 9   ? 0.7141 0.6601 0.5412 -0.0128 0.0313  0.0023  11  ALA B O   
1724 C CB  . ALA B 9   ? 0.6994 0.6682 0.5326 -0.0049 0.0233  -0.0002 11  ALA B CB  
1725 N N   . ARG B 10  ? 0.6478 0.5865 0.4835 -0.0055 0.0315  0.0027  12  ARG B N   
1726 C CA  . ARG B 10  ? 0.6251 0.5568 0.4649 -0.0075 0.0360  0.0009  12  ARG B CA  
1727 C C   . ARG B 10  ? 0.6057 0.5469 0.4553 -0.0101 0.0387  -0.0063 12  ARG B C   
1728 O O   . ARG B 10  ? 0.6164 0.5675 0.4730 -0.0094 0.0378  -0.0107 12  ARG B O   
1729 C CB  . ARG B 10  ? 0.6608 0.5844 0.5041 -0.0033 0.0373  0.0022  12  ARG B CB  
1730 C CG  . ARG B 10  ? 0.7145 0.6297 0.5605 -0.0045 0.0417  0.0015  12  ARG B CG  
1731 C CD  . ARG B 10  ? 0.7343 0.6426 0.5829 -0.0001 0.0429  0.0028  12  ARG B CD  
1732 N NE  . ARG B 10  ? 0.7767 0.6756 0.6154 0.0033  0.0401  0.0081  12  ARG B NE  
1733 C CZ  . ARG B 10  ? 0.8058 0.6915 0.6345 0.0018  0.0404  0.0121  12  ARG B CZ  
1734 N NH1 . ARG B 10  ? 0.8369 0.7197 0.6647 -0.0027 0.0431  0.0115  12  ARG B NH1 
1735 N NH2 . ARG B 10  ? 0.7753 0.6508 0.5945 0.0049  0.0382  0.0165  12  ARG B NH2 
1736 N N   . ILE B 11  ? 0.5652 0.5036 0.4150 -0.0130 0.0421  -0.0075 13  ILE B N   
1737 C CA  . ILE B 11  ? 0.5454 0.4890 0.4037 -0.0146 0.0455  -0.0140 13  ILE B CA  
1738 C C   . ILE B 11  ? 0.5386 0.4767 0.4054 -0.0129 0.0490  -0.0156 13  ILE B C   
1739 O O   . ILE B 11  ? 0.5403 0.4695 0.4060 -0.0122 0.0516  -0.0128 13  ILE B O   
1740 C CB  . ILE B 11  ? 0.5572 0.5002 0.4123 -0.0170 0.0481  -0.0142 13  ILE B CB  
1741 C CG1 . ILE B 11  ? 0.5735 0.5227 0.4199 -0.0191 0.0450  -0.0122 13  ILE B CG1 
1742 C CG2 . ILE B 11  ? 0.5593 0.5056 0.4222 -0.0177 0.0519  -0.0210 13  ILE B CG2 
1743 C CD1 . ILE B 11  ? 0.6156 0.5655 0.4580 -0.0212 0.0475  -0.0112 13  ILE B CD1 
1744 N N   . ILE B 12  ? 0.5233 0.4677 0.3981 -0.0127 0.0490  -0.0201 14  ILE B N   
1745 C CA  . ILE B 12  ? 0.5157 0.4567 0.3989 -0.0117 0.0524  -0.0216 14  ILE B CA  
1746 C C   . ILE B 12  ? 0.5068 0.4506 0.3979 -0.0151 0.0562  -0.0285 14  ILE B C   
1747 O O   . ILE B 12  ? 0.5301 0.4833 0.4236 -0.0176 0.0548  -0.0336 14  ILE B O   
1748 C CB  . ILE B 12  ? 0.5153 0.4610 0.4014 -0.0087 0.0496  -0.0205 14  ILE B CB  
1749 C CG1 . ILE B 12  ? 0.5379 0.4772 0.4143 -0.0049 0.0462  -0.0135 14  ILE B CG1 
1750 C CG2 . ILE B 12  ? 0.5097 0.4531 0.4046 -0.0082 0.0536  -0.0221 14  ILE B CG2 
1751 C CD1 . ILE B 12  ? 0.5470 0.4911 0.4243 -0.0007 0.0431  -0.0120 14  ILE B CD1 
1752 N N   . TYR B 13  ? 0.4878 0.4233 0.3823 -0.0152 0.0612  -0.0287 15  TYR B N   
1753 C CA  . TYR B 13  ? 0.4999 0.4343 0.4013 -0.0182 0.0658  -0.0347 15  TYR B CA  
1754 C C   . TYR B 13  ? 0.5129 0.4432 0.4216 -0.0183 0.0695  -0.0347 15  TYR B C   
1755 O O   . TYR B 13  ? 0.5151 0.4382 0.4220 -0.0154 0.0710  -0.0296 15  TYR B O   
1756 C CB  . TYR B 13  ? 0.4940 0.4205 0.3921 -0.0178 0.0696  -0.0344 15  TYR B CB  
1757 C CG  . TYR B 13  ? 0.5058 0.4367 0.3972 -0.0179 0.0672  -0.0347 15  TYR B CG  
1758 C CD1 . TYR B 13  ? 0.5245 0.4624 0.4167 -0.0206 0.0666  -0.0411 15  TYR B CD1 
1759 C CD2 . TYR B 13  ? 0.5035 0.4323 0.3875 -0.0158 0.0659  -0.0290 15  TYR B CD2 
1760 C CE1 . TYR B 13  ? 0.5500 0.4930 0.4358 -0.0205 0.0648  -0.0415 15  TYR B CE1 
1761 C CE2 . TYR B 13  ? 0.5147 0.4488 0.3929 -0.0163 0.0643  -0.0292 15  TYR B CE2 
1762 C CZ  . TYR B 13  ? 0.5297 0.4712 0.4088 -0.0184 0.0638  -0.0353 15  TYR B CZ  
1763 O OH  . TYR B 13  ? 0.5173 0.4654 0.3904 -0.0189 0.0623  -0.0357 15  TYR B OH  
1764 N N   . ASP B 14  ? 0.5124 0.4478 0.4289 -0.0222 0.0712  -0.0407 16  ASP B N   
1765 C CA  . ASP B 14  ? 0.5074 0.4393 0.4313 -0.0235 0.0756  -0.0411 16  ASP B CA  
1766 C C   . ASP B 14  ? 0.5008 0.4200 0.4253 -0.0249 0.0821  -0.0421 16  ASP B C   
1767 O O   . ASP B 14  ? 0.4875 0.4021 0.4079 -0.0249 0.0831  -0.0437 16  ASP B O   
1768 C CB  . ASP B 14  ? 0.5127 0.4570 0.4453 -0.0277 0.0746  -0.0468 16  ASP B CB  
1769 C CG  . ASP B 14  ? 0.5778 0.5274 0.5133 -0.0338 0.0750  -0.0551 16  ASP B CG  
1770 O OD1 . ASP B 14  ? 0.5764 0.5162 0.5093 -0.0354 0.0786  -0.0575 16  ASP B OD1 
1771 O OD2 . ASP B 14  ? 0.6374 0.6015 0.5776 -0.0367 0.0717  -0.0594 16  ASP B OD2 
1772 N N   . ARG B 15  ? 0.5109 0.4249 0.4404 -0.0257 0.0866  -0.0409 17  ARG B N   
1773 C CA  A ARG B 15  ? 0.5343 0.4350 0.4642 -0.0265 0.0933  -0.0406 17  ARG B CA  
1774 C CA  B ARG B 15  ? 0.5344 0.4351 0.4641 -0.0264 0.0932  -0.0405 17  ARG B CA  
1775 C C   . ARG B 15  ? 0.5515 0.4483 0.4824 -0.0308 0.0960  -0.0475 17  ARG B C   
1776 O O   . ARG B 15  ? 0.5591 0.4456 0.4855 -0.0285 0.0991  -0.0467 17  ARG B O   
1777 C CB  A ARG B 15  ? 0.5435 0.4420 0.4799 -0.0286 0.0977  -0.0394 17  ARG B CB  
1778 C CB  B ARG B 15  ? 0.5440 0.4421 0.4798 -0.0281 0.0976  -0.0390 17  ARG B CB  
1779 C CG  A ARG B 15  ? 0.5612 0.4445 0.4966 -0.0283 0.1048  -0.0370 17  ARG B CG  
1780 C CG  B ARG B 15  ? 0.5590 0.4422 0.4932 -0.0274 0.1042  -0.0363 17  ARG B CG  
1781 C CD  A ARG B 15  ? 0.5801 0.4617 0.5224 -0.0325 0.1099  -0.0372 17  ARG B CD  
1782 C CD  B ARG B 15  ? 0.5779 0.4594 0.5179 -0.0298 0.1088  -0.0347 17  ARG B CD  
1783 N NE  A ARG B 15  ? 0.5896 0.4728 0.5315 -0.0284 0.1100  -0.0309 17  ARG B NE  
1784 N NE  B ARG B 15  ? 0.5921 0.4583 0.5299 -0.0290 0.1156  -0.0315 17  ARG B NE  
1785 C CZ  A ARG B 15  ? 0.6028 0.4981 0.5477 -0.0274 0.1063  -0.0303 17  ARG B CZ  
1786 C CZ  B ARG B 15  ? 0.6463 0.5020 0.5851 -0.0328 0.1208  -0.0350 17  ARG B CZ  
1787 N NH1 A ARG B 15  ? 0.5362 0.4305 0.4794 -0.0233 0.1072  -0.0248 17  ARG B NH1 
1788 N NH1 B ARG B 15  ? 0.6365 0.4958 0.5787 -0.0387 0.1199  -0.0430 17  ARG B NH1 
1789 N NH2 A ARG B 15  ? 0.6183 0.5269 0.5676 -0.0299 0.1018  -0.0352 17  ARG B NH2 
1790 N NH2 B ARG B 15  ? 0.6877 0.5286 0.6234 -0.0307 0.1269  -0.0307 17  ARG B NH2 
1791 N N   . ALA B 16  ? 0.5611 0.4668 0.4980 -0.0370 0.0950  -0.0546 18  ALA B N   
1792 C CA  . ALA B 16  ? 0.5704 0.4716 0.5083 -0.0422 0.0981  -0.0624 18  ALA B CA  
1793 C C   . ALA B 16  ? 0.5521 0.4526 0.4828 -0.0393 0.0959  -0.0640 18  ALA B C   
1794 O O   . ALA B 16  ? 0.5534 0.4425 0.4814 -0.0394 0.1003  -0.0670 18  ALA B O   
1795 C CB  . ALA B 16  ? 0.5845 0.4988 0.5296 -0.0498 0.0962  -0.0699 18  ALA B CB  
1796 N N   . PHE B 17  ? 0.5455 0.4576 0.4727 -0.0365 0.0894  -0.0620 19  PHE B N   
1797 C CA  . PHE B 17  ? 0.5525 0.4664 0.4729 -0.0341 0.0871  -0.0630 19  PHE B CA  
1798 C C   . PHE B 17  ? 0.5384 0.4408 0.4532 -0.0282 0.0902  -0.0574 19  PHE B C   
1799 O O   . PHE B 17  ? 0.5321 0.4297 0.4433 -0.0270 0.0925  -0.0602 19  PHE B O   
1800 C CB  . PHE B 17  ? 0.5678 0.4961 0.4852 -0.0326 0.0797  -0.0608 19  PHE B CB  
1801 C CG  . PHE B 17  ? 0.6094 0.5424 0.5204 -0.0319 0.0773  -0.0633 19  PHE B CG  
1802 C CD1 . PHE B 17  ? 0.6280 0.5577 0.5320 -0.0271 0.0769  -0.0580 19  PHE B CD1 
1803 C CD2 . PHE B 17  ? 0.6377 0.5796 0.5496 -0.0364 0.0756  -0.0713 19  PHE B CD2 
1804 C CE1 . PHE B 17  ? 0.6513 0.5869 0.5496 -0.0267 0.0750  -0.0603 19  PHE B CE1 
1805 C CE2 . PHE B 17  ? 0.6515 0.5986 0.5570 -0.0356 0.0736  -0.0737 19  PHE B CE2 
1806 C CZ  . PHE B 17  ? 0.6526 0.5965 0.5515 -0.0307 0.0735  -0.0680 19  PHE B CZ  
1807 N N   . LEU B 18  ? 0.5296 0.4285 0.4436 -0.0245 0.0903  -0.0497 20  LEU B N   
1808 C CA  . LEU B 18  ? 0.5239 0.4145 0.4326 -0.0189 0.0927  -0.0440 20  LEU B CA  
1809 C C   . LEU B 18  ? 0.5095 0.3864 0.4195 -0.0184 0.0999  -0.0460 20  LEU B C   
1810 O O   . LEU B 18  ? 0.5063 0.3785 0.4120 -0.0144 0.1020  -0.0454 20  LEU B O   
1811 C CB  . LEU B 18  ? 0.5084 0.3984 0.4158 -0.0157 0.0914  -0.0360 20  LEU B CB  
1812 C CG  . LEU B 18  ? 0.5285 0.4286 0.4324 -0.0151 0.0847  -0.0330 20  LEU B CG  
1813 C CD1 . LEU B 18  ? 0.5384 0.4358 0.4408 -0.0125 0.0841  -0.0264 20  LEU B CD1 
1814 C CD2 . LEU B 18  ? 0.5384 0.4427 0.4353 -0.0134 0.0819  -0.0319 20  LEU B CD2 
1815 N N   . MET B 19  ? 0.5251 0.3959 0.4408 -0.0224 0.1037  -0.0482 21  MET B N   
1816 C CA  . MET B 19  ? 0.5592 0.4147 0.4756 -0.0229 0.1109  -0.0504 21  MET B CA  
1817 C C   . MET B 19  ? 0.5928 0.4452 0.5076 -0.0250 0.1126  -0.0586 21  MET B C   
1818 O O   . MET B 19  ? 0.6128 0.4523 0.5243 -0.0213 0.1177  -0.0586 21  MET B O   
1819 C CB  . MET B 19  ? 0.5807 0.4312 0.5037 -0.0287 0.1148  -0.0517 21  MET B CB  
1820 C CG  . MET B 19  ? 0.6430 0.4947 0.5675 -0.0266 0.1147  -0.0441 21  MET B CG  
1821 S SD  . MET B 19  ? 0.7255 0.5669 0.6434 -0.0176 0.1177  -0.0342 21  MET B SD  
1822 C CE  . MET B 19  ? 0.7493 0.5718 0.6657 -0.0171 0.1259  -0.0361 21  MET B CE  
1823 N N   . ALA B 20  ? 0.5957 0.4598 0.5123 -0.0301 0.1083  -0.0655 22  ALA B N   
1824 C CA  . ALA B 20  ? 0.6161 0.4782 0.5304 -0.0324 0.1097  -0.0742 22  ALA B CA  
1825 C C   . ALA B 20  ? 0.6304 0.4942 0.5378 -0.0253 0.1086  -0.0722 22  ALA B C   
1826 O O   . ALA B 20  ? 0.6428 0.5011 0.5472 -0.0248 0.1114  -0.0783 22  ALA B O   
1827 C CB  . ALA B 20  ? 0.6172 0.4943 0.5348 -0.0395 0.1048  -0.0815 22  ALA B CB  
1828 N N   . CYS B 21  ? 0.6225 0.4942 0.5270 -0.0201 0.1045  -0.0641 23  CYS B N   
1829 C CA  . CYS B 21  ? 0.6200 0.4943 0.5183 -0.0135 0.1040  -0.0612 23  CYS B CA  
1830 C C   . CYS B 21  ? 0.6270 0.4888 0.5232 -0.0067 0.1095  -0.0561 23  CYS B C   
1831 O O   . CYS B 21  ? 0.6523 0.5173 0.5440 -0.0008 0.1095  -0.0539 23  CYS B O   
1832 C CB  . CYS B 21  ? 0.6325 0.5209 0.5283 -0.0123 0.0974  -0.0554 23  CYS B CB  
1833 S SG  . CYS B 21  ? 0.6506 0.5549 0.5468 -0.0183 0.0904  -0.0598 23  CYS B SG  
1834 N N   . ARG B 22  ? 0.6208 0.4699 0.5199 -0.0070 0.1140  -0.0538 24  ARG B N   
1835 C CA  . ARG B 22  ? 0.6583 0.4951 0.5549 0.0000  0.1193  -0.0482 24  ARG B CA  
1836 C C   . ARG B 22  ? 0.7335 0.5566 0.6280 0.0022  0.1255  -0.0540 24  ARG B C   
1837 O O   . ARG B 22  ? 0.7527 0.5681 0.6497 -0.0042 0.1281  -0.0613 24  ARG B O   
1838 C CB  . ARG B 22  ? 0.6463 0.4749 0.5463 -0.0018 0.1219  -0.0434 24  ARG B CB  
1839 C CG  . ARG B 22  ? 0.6667 0.4849 0.5636 0.0057  0.1265  -0.0358 24  ARG B CG  
1840 C CD  . ARG B 22  ? 0.6610 0.4744 0.5611 0.0030  0.1281  -0.0310 24  ARG B CD  
1841 N NE  . ARG B 22  ? 0.6796 0.4839 0.5763 0.0102  0.1324  -0.0230 24  ARG B NE  
1842 C CZ  . ARG B 22  ? 0.6946 0.4938 0.5925 0.0096  0.1347  -0.0175 24  ARG B CZ  
1843 N NH1 . ARG B 22  ? 0.6108 0.4134 0.5138 0.0023  0.1334  -0.0193 24  ARG B NH1 
1844 N NH2 . ARG B 22  ? 0.8010 0.5928 0.6948 0.0168  0.1385  -0.0101 24  ARG B NH2 
1845 N N   . GLY B 23  ? 0.7599 0.5803 0.6497 0.0111  0.1279  -0.0509 25  GLY B N   
1846 C CA  . GLY B 23  ? 0.7930 0.6008 0.6795 0.0150  0.1337  -0.0565 25  GLY B CA  
1847 C C   . GLY B 23  ? 0.8326 0.6178 0.7184 0.0174  0.1414  -0.0545 25  GLY B C   
1848 O O   . GLY B 23  ? 0.8583 0.6397 0.7446 0.0203  0.1426  -0.0461 25  GLY B O   
1849 N N   . GLY B 33  ? 0.7690 0.7306 0.6292 -0.0023 0.0909  -0.0789 35  GLY B N   
1850 C CA  . GLY B 33  ? 0.7641 0.7359 0.6228 -0.0063 0.0846  -0.0716 35  GLY B CA  
1851 C C   . GLY B 33  ? 0.7454 0.7079 0.6084 -0.0069 0.0835  -0.0647 35  GLY B C   
1852 O O   . GLY B 33  ? 0.7553 0.7083 0.6228 -0.0094 0.0841  -0.0676 35  GLY B O   
1853 N N   . LYS B 34  ? 0.7146 0.6802 0.5760 -0.0052 0.0821  -0.0560 36  LYS B N   
1854 C CA  . LYS B 34  ? 0.6747 0.6313 0.5394 -0.0051 0.0816  -0.0499 36  LYS B CA  
1855 C C   . LYS B 34  ? 0.6307 0.5894 0.4950 -0.0104 0.0761  -0.0470 36  LYS B C   
1856 O O   . LYS B 34  ? 0.6302 0.5991 0.4900 -0.0134 0.0720  -0.0462 36  LYS B O   
1857 C CB  . LYS B 34  ? 0.6988 0.6580 0.5616 -0.0012 0.0824  -0.0425 36  LYS B CB  
1858 C CG  . LYS B 34  ? 0.7418 0.6974 0.6057 0.0058  0.0882  -0.0439 36  LYS B CG  
1859 C CD  . LYS B 34  ? 0.8163 0.7807 0.6778 0.0090  0.0879  -0.0370 36  LYS B CD  
1860 C CE  . LYS B 34  ? 0.8986 0.8589 0.7619 0.0173  0.0933  -0.0361 36  LYS B CE  
1861 N NZ  . LYS B 34  ? 0.9621 0.9348 0.8232 0.0197  0.0923  -0.0293 36  LYS B NZ  
1862 N N   . HIS B 35  ? 0.5933 0.5424 0.4621 -0.0109 0.0763  -0.0452 37  HIS B N   
1863 C CA  . HIS B 35  ? 0.5515 0.5014 0.4210 -0.0145 0.0718  -0.0427 37  HIS B CA  
1864 C C   . HIS B 35  ? 0.5241 0.4736 0.3899 -0.0140 0.0694  -0.0342 37  HIS B C   
1865 O O   . HIS B 35  ? 0.5067 0.4485 0.3746 -0.0116 0.0718  -0.0307 37  HIS B O   
1866 C CB  . HIS B 35  ? 0.5405 0.4813 0.4171 -0.0155 0.0739  -0.0461 37  HIS B CB  
1867 C CG  . HIS B 35  ? 0.6408 0.5824 0.5201 -0.0177 0.0759  -0.0554 37  HIS B CG  
1868 N ND1 . HIS B 35  ? 0.6728 0.6072 0.5532 -0.0155 0.0815  -0.0601 37  HIS B ND1 
1869 C CD2 . HIS B 35  ? 0.6653 0.6143 0.5458 -0.0219 0.0728  -0.0607 37  HIS B CD2 
1870 C CE1 . HIS B 35  ? 0.6851 0.6215 0.5670 -0.0191 0.0818  -0.0686 37  HIS B CE1 
1871 N NE2 . HIS B 35  ? 0.6737 0.6200 0.5559 -0.0233 0.0765  -0.0694 37  HIS B NE2 
1872 N N   . PRO B 36  ? 0.5295 0.4862 0.3894 -0.0165 0.0648  -0.0306 38  PRO B N   
1873 C CA  . PRO B 36  ? 0.5158 0.4701 0.3712 -0.0169 0.0627  -0.0229 38  PRO B CA  
1874 C C   . PRO B 36  ? 0.5026 0.4483 0.3604 -0.0168 0.0615  -0.0201 38  PRO B C   
1875 O O   . PRO B 36  ? 0.5012 0.4463 0.3622 -0.0174 0.0600  -0.0227 38  PRO B O   
1876 C CB  . PRO B 36  ? 0.5330 0.4957 0.3809 -0.0202 0.0585  -0.0204 38  PRO B CB  
1877 C CG  . PRO B 36  ? 0.5595 0.5310 0.4076 -0.0207 0.0589  -0.0266 38  PRO B CG  
1878 C CD  . PRO B 36  ? 0.5455 0.5122 0.4013 -0.0193 0.0613  -0.0329 38  PRO B CD  
1879 N N   . LEU B 37  ? 0.5024 0.4426 0.3582 -0.0159 0.0622  -0.0150 39  LEU B N   
1880 C CA  . LEU B 37  ? 0.4726 0.4047 0.3287 -0.0156 0.0610  -0.0116 39  LEU B CA  
1881 C C   . LEU B 37  ? 0.4791 0.4110 0.3273 -0.0180 0.0565  -0.0070 39  LEU B C   
1882 O O   . LEU B 37  ? 0.4468 0.3838 0.2883 -0.0206 0.0549  -0.0048 39  LEU B O   
1883 C CB  . LEU B 37  ? 0.4593 0.3856 0.3163 -0.0135 0.0642  -0.0087 39  LEU B CB  
1884 C CG  . LEU B 37  ? 0.4805 0.4039 0.3444 -0.0103 0.0692  -0.0119 39  LEU B CG  
1885 C CD1 . LEU B 37  ? 0.4899 0.4088 0.3533 -0.0077 0.0719  -0.0079 39  LEU B CD1 
1886 C CD2 . LEU B 37  ? 0.4602 0.3794 0.3310 -0.0102 0.0704  -0.0161 39  LEU B CD2 
1887 N N   . GLN B 38  ? 0.4734 0.3988 0.3216 -0.0171 0.0547  -0.0052 40  GLN B N   
1888 C CA  . GLN B 38  ? 0.4958 0.4169 0.3354 -0.0185 0.0510  -0.0003 40  GLN B CA  
1889 C C   . GLN B 38  ? 0.5105 0.4278 0.3433 -0.0209 0.0515  0.0040  40  GLN B C   
1890 O O   . GLN B 38  ? 0.5106 0.4279 0.3348 -0.0244 0.0491  0.0073  40  GLN B O   
1891 C CB  . GLN B 38  ? 0.5289 0.4431 0.3708 -0.0155 0.0501  0.0004  40  GLN B CB  
1892 C CG  . GLN B 38  ? 0.5849 0.4917 0.4177 -0.0155 0.0467  0.0053  40  GLN B CG  
1893 C CD  . GLN B 38  ? 0.6278 0.5397 0.4553 -0.0165 0.0429  0.0065  40  GLN B CD  
1894 O OE1 . GLN B 38  ? 0.5952 0.5174 0.4273 -0.0164 0.0423  0.0028  40  GLN B OE1 
1895 N NE2 . GLN B 38  ? 0.6443 0.5485 0.4615 -0.0176 0.0405  0.0117  40  GLN B NE2 
1896 N N   . ASN B 39  ? 0.4835 0.3980 0.3199 -0.0195 0.0548  0.0038  41  ASN B N   
1897 C CA  . ASN B 39  ? 0.5074 0.4194 0.3381 -0.0217 0.0552  0.0074  41  ASN B CA  
1898 C C   . ASN B 39  ? 0.5044 0.4243 0.3385 -0.0210 0.0582  0.0063  41  ASN B C   
1899 O O   . ASN B 39  ? 0.4924 0.4148 0.3341 -0.0175 0.0610  0.0029  41  ASN B O   
1900 C CB  . ASN B 39  ? 0.5063 0.4077 0.3367 -0.0198 0.0560  0.0090  41  ASN B CB  
1901 C CG  . ASN B 39  ? 0.5822 0.4745 0.4064 -0.0202 0.0530  0.0111  41  ASN B CG  
1902 O OD1 . ASN B 39  ? 0.6341 0.5222 0.4490 -0.0240 0.0510  0.0142  41  ASN B OD1 
1903 N ND2 . ASN B 39  ? 0.5684 0.4576 0.3973 -0.0164 0.0528  0.0096  41  ASN B ND2 
1904 N N   . ARG B 40  ? 0.4854 0.4092 0.3137 -0.0243 0.0578  0.0092  42  ARG B N   
1905 C CA  . ARG B 40  ? 0.4620 0.3931 0.2932 -0.0226 0.0606  0.0093  42  ARG B CA  
1906 C C   . ARG B 40  ? 0.4235 0.3471 0.2553 -0.0205 0.0621  0.0109  42  ARG B C   
1907 O O   . ARG B 40  ? 0.4446 0.3601 0.2713 -0.0228 0.0604  0.0128  42  ARG B O   
1908 C CB  . ARG B 40  ? 0.4624 0.4048 0.2883 -0.0270 0.0596  0.0112  42  ARG B CB  
1909 C CG  . ARG B 40  ? 0.4776 0.4308 0.3068 -0.0241 0.0623  0.0114  42  ARG B CG  
1910 C CD  . ARG B 40  ? 0.4873 0.4549 0.3125 -0.0286 0.0612  0.0125  42  ARG B CD  
1911 N NE  . ARG B 40  ? 0.5023 0.4843 0.3311 -0.0249 0.0638  0.0123  42  ARG B NE  
1912 C CZ  . ARG B 40  ? 0.5095 0.5033 0.3357 -0.0275 0.0635  0.0150  42  ARG B CZ  
1913 N NH1 . ARG B 40  ? 0.4952 0.4866 0.3146 -0.0349 0.0610  0.0177  42  ARG B NH1 
1914 N NH2 . ARG B 40  ? 0.4922 0.5004 0.3224 -0.0226 0.0659  0.0147  42  ARG B NH2 
1915 N N   . TRP B 41  ? 0.4361 0.3619 0.2738 -0.0157 0.0656  0.0101  43  TRP B N   
1916 C CA  . TRP B 41  ? 0.4370 0.3572 0.2758 -0.0128 0.0677  0.0119  43  TRP B CA  
1917 C C   . TRP B 41  ? 0.4562 0.3861 0.2949 -0.0107 0.0695  0.0139  43  TRP B C   
1918 O O   . TRP B 41  ? 0.4648 0.4044 0.3056 -0.0091 0.0705  0.0132  43  TRP B O   
1919 C CB  . TRP B 41  ? 0.4440 0.3568 0.2905 -0.0079 0.0709  0.0096  43  TRP B CB  
1920 C CG  . TRP B 41  ? 0.4472 0.3536 0.2954 -0.0091 0.0693  0.0074  43  TRP B CG  
1921 C CD1 . TRP B 41  ? 0.4555 0.3645 0.3058 -0.0101 0.0680  0.0044  43  TRP B CD1 
1922 C CD2 . TRP B 41  ? 0.4412 0.3390 0.2879 -0.0093 0.0684  0.0083  43  TRP B CD2 
1923 N NE1 . TRP B 41  ? 0.4633 0.3668 0.3143 -0.0106 0.0662  0.0035  43  TRP B NE1 
1924 C CE2 . TRP B 41  ? 0.4535 0.3499 0.3023 -0.0099 0.0664  0.0059  43  TRP B CE2 
1925 C CE3 . TRP B 41  ? 0.4364 0.3284 0.2797 -0.0089 0.0688  0.0106  43  TRP B CE3 
1926 C CZ2 . TRP B 41  ? 0.4589 0.3485 0.3070 -0.0093 0.0651  0.0062  43  TRP B CZ2 
1927 C CZ3 . TRP B 41  ? 0.4544 0.3386 0.2971 -0.0083 0.0680  0.0103  43  TRP B CZ3 
1928 C CH2 . TRP B 41  ? 0.4560 0.3392 0.3013 -0.0082 0.0662  0.0083  43  TRP B CH2 
1929 N N   . ALA B 42  ? 0.4539 0.3819 0.2900 -0.0104 0.0699  0.0165  44  ALA B N   
1930 C CA  . ALA B 42  ? 0.4450 0.3828 0.2805 -0.0080 0.0713  0.0190  44  ALA B CA  
1931 C C   . ALA B 42  ? 0.4375 0.3685 0.2758 -0.0025 0.0746  0.0204  44  ALA B C   
1932 O O   . ALA B 42  ? 0.4427 0.3639 0.2792 -0.0037 0.0743  0.0206  44  ALA B O   
1933 C CB  . ALA B 42  ? 0.4451 0.3890 0.2727 -0.0146 0.0681  0.0209  44  ALA B CB  
1934 N N   . LEU B 43  ? 0.4369 0.3729 0.2792 0.0038  0.0778  0.0216  45  LEU B N   
1935 C CA  . LEU B 43  ? 0.4562 0.3874 0.3001 0.0094  0.0813  0.0242  45  LEU B CA  
1936 C C   . LEU B 43  ? 0.4620 0.4042 0.3011 0.0099  0.0803  0.0280  45  LEU B C   
1937 O O   . LEU B 43  ? 0.4847 0.4409 0.3233 0.0111  0.0796  0.0292  45  LEU B O   
1938 C CB  . LEU B 43  ? 0.4545 0.3832 0.3045 0.0166  0.0858  0.0239  45  LEU B CB  
1939 C CG  . LEU B 43  ? 0.5048 0.4264 0.3561 0.0225  0.0901  0.0272  45  LEU B CG  
1940 C CD1 . LEU B 43  ? 0.5054 0.4140 0.3580 0.0202  0.0911  0.0260  45  LEU B CD1 
1941 C CD2 . LEU B 43  ? 0.5290 0.4476 0.3844 0.0297  0.0948  0.0274  45  LEU B CD2 
1942 N N   . TRP B 44  ? 0.4688 0.4059 0.3046 0.0092  0.0804  0.0297  46  TRP B N   
1943 C CA  . TRP B 44  ? 0.5007 0.4473 0.3313 0.0093  0.0795  0.0329  46  TRP B CA  
1944 C C   . TRP B 44  ? 0.5164 0.4594 0.3483 0.0167  0.0835  0.0364  46  TRP B C   
1945 O O   . TRP B 44  ? 0.5114 0.4414 0.3470 0.0196  0.0868  0.0361  46  TRP B O   
1946 C CB  . TRP B 44  ? 0.5013 0.4447 0.3250 0.0017  0.0762  0.0316  46  TRP B CB  
1947 C CG  . TRP B 44  ? 0.5218 0.4649 0.3424 -0.0062 0.0724  0.0287  46  TRP B CG  
1948 C CD1 . TRP B 44  ? 0.5349 0.4676 0.3574 -0.0084 0.0718  0.0259  46  TRP B CD1 
1949 C CD2 . TRP B 44  ? 0.5377 0.4916 0.3522 -0.0134 0.0689  0.0286  46  TRP B CD2 
1950 N NE1 . TRP B 44  ? 0.5417 0.4765 0.3587 -0.0161 0.0681  0.0247  46  TRP B NE1 
1951 C CE2 . TRP B 44  ? 0.5461 0.4937 0.3584 -0.0197 0.0665  0.0262  46  TRP B CE2 
1952 C CE3 . TRP B 44  ? 0.5517 0.5215 0.3627 -0.0153 0.0676  0.0304  46  TRP B CE3 
1953 C CZ2 . TRP B 44  ? 0.5788 0.5326 0.3845 -0.0285 0.0632  0.0257  46  TRP B CZ2 
1954 C CZ3 . TRP B 44  ? 0.5844 0.5620 0.3897 -0.0245 0.0642  0.0294  46  TRP B CZ3 
1955 C CH2 . TRP B 44  ? 0.5814 0.5504 0.3839 -0.0312 0.0622  0.0271  46  TRP B CH2 
1956 N N   . PHE B 45  ? 0.5233 0.4791 0.3521 0.0195  0.0832  0.0400  47  PHE B N   
1957 C CA  . PHE B 45  ? 0.5494 0.5041 0.3774 0.0265  0.0866  0.0445  47  PHE B CA  
1958 C C   . PHE B 45  ? 0.5381 0.5041 0.3587 0.0236  0.0838  0.0464  47  PHE B C   
1959 O O   . PHE B 45  ? 0.5271 0.5069 0.3448 0.0187  0.0800  0.0454  47  PHE B O   
1960 C CB  . PHE B 45  ? 0.5878 0.5494 0.4199 0.0356  0.0895  0.0477  47  PHE B CB  
1961 C CG  . PHE B 45  ? 0.6395 0.6019 0.4703 0.0443  0.0931  0.0536  47  PHE B CG  
1962 C CD1 . PHE B 45  ? 0.6560 0.6021 0.4882 0.0476  0.0976  0.0552  47  PHE B CD1 
1963 C CD2 . PHE B 45  ? 0.6827 0.6629 0.5112 0.0496  0.0922  0.0578  47  PHE B CD2 
1964 C CE1 . PHE B 45  ? 0.6974 0.6432 0.5277 0.0559  0.1013  0.0614  47  PHE B CE1 
1965 C CE2 . PHE B 45  ? 0.7026 0.6837 0.5294 0.0587  0.0956  0.0640  47  PHE B CE2 
1966 C CZ  . PHE B 45  ? 0.7076 0.6705 0.5349 0.0618  0.1002  0.0660  47  PHE B CZ  
1967 N N   . PHE B 46  ? 0.5317 0.4933 0.3490 0.0260  0.0856  0.0489  48  PHE B N   
1968 C CA  . PHE B 46  ? 0.5988 0.5736 0.4089 0.0245  0.0833  0.0510  48  PHE B CA  
1969 C C   . PHE B 46  ? 0.6384 0.6228 0.4482 0.0346  0.0861  0.0576  48  PHE B C   
1970 O O   . PHE B 46  ? 0.6526 0.6257 0.4637 0.0403  0.0904  0.0605  48  PHE B O   
1971 C CB  . PHE B 46  ? 0.6253 0.5899 0.4296 0.0197  0.0830  0.0489  48  PHE B CB  
1972 C CG  . PHE B 46  ? 0.6713 0.6281 0.4727 0.0101  0.0798  0.0431  48  PHE B CG  
1973 C CD1 . PHE B 46  ? 0.7024 0.6676 0.4964 0.0021  0.0755  0.0406  48  PHE B CD1 
1974 C CD2 . PHE B 46  ? 0.7042 0.6450 0.5099 0.0091  0.0810  0.0402  48  PHE B CD2 
1975 C CE1 . PHE B 46  ? 0.7083 0.6634 0.4984 -0.0064 0.0730  0.0357  48  PHE B CE1 
1976 C CE2 . PHE B 46  ? 0.7218 0.6549 0.5242 0.0013  0.0780  0.0355  48  PHE B CE2 
1977 C CZ  . PHE B 46  ? 0.7122 0.6512 0.5064 -0.0062 0.0742  0.0336  48  PHE B CZ  
1978 N N   . LYS B 47  ? 0.6594 0.6647 0.4674 0.0365  0.0837  0.0600  49  LYS B N   
1979 C CA  . LYS B 47  ? 0.7091 0.7267 0.5159 0.0465  0.0856  0.0668  49  LYS B CA  
1980 C C   . LYS B 47  ? 0.7406 0.7566 0.5405 0.0466  0.0862  0.0691  49  LYS B C   
1981 O O   . LYS B 47  ? 0.7505 0.7643 0.5453 0.0376  0.0835  0.0648  49  LYS B O   
1982 C CB  . LYS B 47  ? 0.7651 0.8092 0.5717 0.0469  0.0818  0.0678  49  LYS B CB  
1983 C CG  . LYS B 47  ? 0.8628 0.9271 0.6657 0.0548  0.0815  0.0742  49  LYS B CG  
1984 C CD  . LYS B 47  ? 0.9450 1.0061 0.7511 0.0698  0.0865  0.0814  49  LYS B CD  
1985 C CE  . LYS B 47  ? 0.9838 1.0591 0.7847 0.0784  0.0870  0.0887  49  LYS B CE  
1986 N NZ  . LYS B 47  ? 1.0142 1.0734 0.8103 0.0796  0.0901  0.0914  49  LYS B NZ  
1987 N N   . ASN B 48  ? 0.7597 0.7759 0.5587 0.0569  0.0900  0.0760  50  ASN B N   
1988 C CA  . ASN B 48  ? 0.7746 0.7893 0.5669 0.0591  0.0916  0.0796  50  ASN B CA  
1989 C C   . ASN B 48  ? 0.7639 0.8019 0.5483 0.0579  0.0876  0.0814  50  ASN B C   
1990 O O   . ASN B 48  ? 0.7755 0.8143 0.5543 0.0619  0.0894  0.0857  50  ASN B O   
1991 C CB  . ASN B 48  ? 0.8177 0.8226 0.6118 0.0711  0.0979  0.0873  50  ASN B CB  
1992 C CG  . ASN B 48  ? 0.9090 0.9102 0.6965 0.0741  0.1007  0.0920  50  ASN B CG  
1993 O OD1 . ASN B 48  ? 0.9511 0.9499 0.7340 0.0667  0.0992  0.0882  50  ASN B OD1 
1994 N ND2 . ASN B 48  ? 0.9230 0.9233 0.7092 0.0854  0.1051  0.1005  50  ASN B ND2 
1995 N N   . ASP B 49  ? 0.7239 0.7808 0.5076 0.0519  0.0823  0.0781  51  ASP B N   
1996 C CA  . ASP B 49  ? 0.6983 0.7811 0.4758 0.0516  0.0784  0.0801  51  ASP B CA  
1997 C C   . ASP B 49  ? 0.6915 0.7726 0.4604 0.0414  0.0759  0.0752  51  ASP B C   
1998 O O   . ASP B 49  ? 0.6760 0.7573 0.4429 0.0296  0.0723  0.0682  51  ASP B O   
1999 C CB  . ASP B 49  ? 0.7064 0.8111 0.4871 0.0478  0.0740  0.0779  51  ASP B CB  
2000 C CG  . ASP B 49  ? 0.7672 0.9023 0.5426 0.0467  0.0696  0.0796  51  ASP B CG  
2001 O OD1 . ASP B 49  ? 0.7791 0.9183 0.5470 0.0471  0.0693  0.0814  51  ASP B OD1 
2002 O OD2 . ASP B 49  ? 0.7701 0.9262 0.5488 0.0452  0.0665  0.0789  51  ASP B OD2 
2003 N N   . LYS B 50  ? 0.6990 0.7780 0.4619 0.0459  0.0782  0.0790  52  LYS B N   
2004 C CA  . LYS B 50  ? 0.7151 0.7908 0.4691 0.0372  0.0766  0.0740  52  LYS B CA  
2005 C C   . LYS B 50  ? 0.7270 0.8277 0.4735 0.0298  0.0708  0.0711  52  LYS B C   
2006 O O   . LYS B 50  ? 0.7332 0.8309 0.4713 0.0214  0.0692  0.0658  52  LYS B O   
2007 C CB  . LYS B 50  ? 0.7420 0.8069 0.4918 0.0440  0.0813  0.0786  52  LYS B CB  
2008 C CG  . LYS B 50  ? 0.8098 0.8489 0.5662 0.0485  0.0871  0.0801  52  LYS B CG  
2009 C CD  . LYS B 50  ? 0.8978 0.9176 0.6547 0.0388  0.0870  0.0718  52  LYS B CD  
2010 C CE  . LYS B 50  ? 0.9695 0.9667 0.7330 0.0426  0.0926  0.0729  52  LYS B CE  
2011 N NZ  . LYS B 50  ? 1.0264 1.0170 0.7997 0.0438  0.0930  0.0724  52  LYS B NZ  
2012 N N   . SER B 51  ? 0.7315 0.8571 0.4806 0.0327  0.0678  0.0742  53  SER B N   
2013 C CA  . SER B 51  ? 0.7529 0.9028 0.4963 0.0228  0.0619  0.0698  53  SER B CA  
2014 C C   . SER B 51  ? 0.7756 0.9184 0.5200 0.0084  0.0589  0.0610  53  SER B C   
2015 O O   . SER B 51  ? 0.7809 0.9378 0.5192 -0.0030 0.0544  0.0557  53  SER B O   
2016 C CB  . SER B 51  ? 0.7705 0.9521 0.5168 0.0304  0.0596  0.0759  53  SER B CB  
2017 O OG  . SER B 51  ? 0.8166 1.0062 0.5714 0.0296  0.0583  0.0751  53  SER B OG  
2018 N N   . LYS B 52  ? 0.7794 0.9006 0.5309 0.0087  0.0614  0.0597  54  LYS B N   
2019 C CA  . LYS B 52  ? 0.7807 0.8931 0.5330 -0.0034 0.0592  0.0526  54  LYS B CA  
2020 C C   . LYS B 52  ? 0.7808 0.8618 0.5315 -0.0069 0.0617  0.0483  54  LYS B C   
2021 O O   . LYS B 52  ? 0.7689 0.8346 0.5216 0.0013  0.0659  0.0513  54  LYS B O   
2022 C CB  . LYS B 52  ? 0.8018 0.9216 0.5640 0.0001  0.0592  0.0548  54  LYS B CB  
2023 C CG  . LYS B 52  ? 0.8351 0.9888 0.5987 0.0012  0.0559  0.0575  54  LYS B CG  
2024 C CD  . LYS B 52  ? 0.8851 1.0461 0.6590 0.0099  0.0574  0.0614  54  LYS B CD  
2025 C CE  . LYS B 52  ? 0.9160 1.1125 0.6919 0.0125  0.0544  0.0645  54  LYS B CE  
2026 N NZ  . LYS B 52  ? 0.9769 1.1898 0.7490 0.0221  0.0544  0.0704  54  LYS B NZ  
2027 N N   . THR B 53  ? 0.7964 0.8687 0.5436 -0.0193 0.0592  0.0414  55  THR B N   
2028 C CA  . THR B 53  ? 0.8143 0.8582 0.5593 -0.0236 0.0609  0.0367  55  THR B CA  
2029 C C   . THR B 53  ? 0.8008 0.8297 0.5565 -0.0171 0.0639  0.0389  55  THR B C   
2030 O O   . THR B 53  ? 0.7758 0.8163 0.5390 -0.0127 0.0638  0.0423  55  THR B O   
2031 C CB  . THR B 53  ? 0.8533 0.8941 0.5897 -0.0390 0.0570  0.0292  55  THR B CB  
2032 O OG1 . THR B 53  ? 0.9311 0.9479 0.6605 -0.0426 0.0584  0.0244  55  THR B OG1 
2033 C CG2 . THR B 53  ? 0.8296 0.8701 0.5708 -0.0445 0.0554  0.0279  55  THR B CG2 
2034 N N   . TRP B 54  ? 0.8103 0.8146 0.5666 -0.0162 0.0666  0.0367  56  TRP B N   
2035 C CA  . TRP B 54  ? 0.8241 0.8153 0.5899 -0.0117 0.0690  0.0378  56  TRP B CA  
2036 C C   . TRP B 54  ? 0.7914 0.7873 0.5601 -0.0181 0.0660  0.0357  56  TRP B C   
2037 O O   . TRP B 54  ? 0.7842 0.7843 0.5611 -0.0127 0.0671  0.0385  56  TRP B O   
2038 C CB  . TRP B 54  ? 0.8607 0.8276 0.6264 -0.0114 0.0715  0.0349  56  TRP B CB  
2039 C CG  . TRP B 54  ? 0.9089 0.8703 0.6754 -0.0033 0.0758  0.0380  56  TRP B CG  
2040 C CD1 . TRP B 54  ? 0.9361 0.8903 0.6954 -0.0042 0.0770  0.0360  56  TRP B CD1 
2041 C CD2 . TRP B 54  ? 0.9292 0.8919 0.7033 0.0068  0.0798  0.0438  56  TRP B CD2 
2042 N NE1 . TRP B 54  ? 0.9489 0.9012 0.7112 0.0044  0.0815  0.0406  56  TRP B NE1 
2043 C CE2 . TRP B 54  ? 0.9468 0.9036 0.7180 0.0110  0.0833  0.0456  56  TRP B CE2 
2044 C CE3 . TRP B 54  ? 0.9441 0.9121 0.7267 0.0125  0.0810  0.0476  56  TRP B CE3 
2045 C CZ2 . TRP B 54  ? 0.9619 0.9170 0.7382 0.0201  0.0880  0.0514  56  TRP B CZ2 
2046 C CZ3 . TRP B 54  ? 0.9626 0.9275 0.7499 0.0220  0.0857  0.0530  56  TRP B CZ3 
2047 C CH2 . TRP B 54  ? 0.9637 0.9218 0.7479 0.0253  0.0892  0.0550  56  TRP B CH2 
2048 N N   . GLN B 55  ? 0.7786 0.7730 0.5397 -0.0296 0.0626  0.0308  57  GLN B N   
2049 C CA  . GLN B 55  ? 0.7719 0.7716 0.5341 -0.0374 0.0598  0.0290  57  GLN B CA  
2050 C C   . GLN B 55  ? 0.7401 0.7652 0.5085 -0.0338 0.0589  0.0329  57  GLN B C   
2051 O O   . GLN B 55  ? 0.7351 0.7629 0.5104 -0.0318 0.0593  0.0340  57  GLN B O   
2052 C CB  . GLN B 55  ? 0.8143 0.8123 0.5651 -0.0510 0.0564  0.0238  57  GLN B CB  
2053 C CG  . GLN B 55  ? 0.8896 0.8885 0.6392 -0.0611 0.0538  0.0216  57  GLN B CG  
2054 C CD  . GLN B 55  ? 1.0248 0.9982 0.7735 -0.0629 0.0547  0.0194  57  GLN B CD  
2055 O OE1 . GLN B 55  ? 1.0563 1.0272 0.8121 -0.0600 0.0552  0.0210  57  GLN B OE1 
2056 N NE2 . GLN B 55  ? 1.0470 1.0013 0.7866 -0.0673 0.0547  0.0156  57  GLN B NE2 
2057 N N   . ALA B 56  ? 0.7135 0.7574 0.4790 -0.0324 0.0579  0.0348  58  ALA B N   
2058 C CA  . ALA B 56  ? 0.6879 0.7589 0.4583 -0.0282 0.0569  0.0387  58  ALA B CA  
2059 C C   . ALA B 56  ? 0.6737 0.7449 0.4538 -0.0139 0.0606  0.0441  58  ALA B C   
2060 O O   . ALA B 56  ? 0.6808 0.7693 0.4668 -0.0098 0.0603  0.0466  58  ALA B O   
2061 C CB  . ALA B 56  ? 0.6808 0.7709 0.4450 -0.0290 0.0550  0.0397  58  ALA B CB  
2062 N N   . ASN B 57  ? 0.6505 0.7028 0.4321 -0.0067 0.0642  0.0456  59  ASN B N   
2063 C CA  . ASN B 57  ? 0.6339 0.6817 0.4235 0.0060  0.0684  0.0503  59  ASN B CA  
2064 C C   . ASN B 57  ? 0.5968 0.6280 0.3931 0.0067  0.0703  0.0484  59  ASN B C   
2065 O O   . ASN B 57  ? 0.5872 0.6127 0.3899 0.0161  0.0740  0.0513  59  ASN B O   
2066 C CB  . ASN B 57  ? 0.6669 0.7037 0.4539 0.0126  0.0717  0.0532  59  ASN B CB  
2067 C CG  . ASN B 57  ? 0.6785 0.7352 0.4606 0.0163  0.0707  0.0572  59  ASN B CG  
2068 O OD1 . ASN B 57  ? 0.6765 0.7542 0.4611 0.0210  0.0696  0.0607  59  ASN B OD1 
2069 N ND2 . ASN B 57  ? 0.6951 0.7473 0.4702 0.0149  0.0710  0.0569  59  ASN B ND2 
2070 N N   . LEU B 58  ? 0.5812 0.6049 0.3755 -0.0032 0.0679  0.0435  60  LEU B N   
2071 C CA  . LEU B 58  ? 0.5798 0.5885 0.3792 -0.0038 0.0690  0.0412  60  LEU B CA  
2072 C C   . LEU B 58  ? 0.5818 0.6036 0.3873 -0.0011 0.0689  0.0422  60  LEU B C   
2073 O O   . LEU B 58  ? 0.6035 0.6444 0.4072 -0.0060 0.0660  0.0420  60  LEU B O   
2074 C CB  . LEU B 58  ? 0.5933 0.5909 0.3870 -0.0152 0.0661  0.0363  60  LEU B CB  
2075 C CG  . LEU B 58  ? 0.6091 0.5924 0.4068 -0.0169 0.0664  0.0338  60  LEU B CG  
2076 C CD1 . LEU B 58  ? 0.6226 0.5893 0.4258 -0.0092 0.0702  0.0343  60  LEU B CD1 
2077 C CD2 . LEU B 58  ? 0.6430 0.6161 0.4333 -0.0279 0.0634  0.0299  60  LEU B CD2 
2078 N N   . ARG B 59  ? 0.5595 0.5723 0.3721 0.0062  0.0721  0.0428  61  ARG B N   
2079 C CA  . ARG B 59  ? 0.5648 0.5888 0.3829 0.0093  0.0724  0.0431  61  ARG B CA  
2080 C C   . ARG B 59  ? 0.5345 0.5434 0.3568 0.0082  0.0735  0.0398  61  ARG B C   
2081 O O   . ARG B 59  ? 0.5322 0.5230 0.3567 0.0109  0.0760  0.0390  61  ARG B O   
2082 C CB  . ARG B 59  ? 0.6071 0.6400 0.4296 0.0219  0.0758  0.0477  61  ARG B CB  
2083 C CG  . ARG B 59  ? 0.6865 0.7378 0.5051 0.0247  0.0746  0.0518  61  ARG B CG  
2084 C CD  . ARG B 59  ? 0.7345 0.8127 0.5520 0.0201  0.0709  0.0517  61  ARG B CD  
2085 N NE  . ARG B 59  ? 0.8098 0.9058 0.6238 0.0237  0.0698  0.0557  61  ARG B NE  
2086 C CZ  . ARG B 59  ? 0.8348 0.9350 0.6418 0.0161  0.0669  0.0548  61  ARG B CZ  
2087 N NH1 . ARG B 59  ? 0.8099 0.8961 0.6120 0.0043  0.0649  0.0499  61  ARG B NH1 
2088 N NH2 . ARG B 59  ? 0.8229 0.9412 0.6270 0.0204  0.0660  0.0586  61  ARG B NH2 
2089 N N   . LEU B 60  ? 0.5215 0.5393 0.3451 0.0040  0.0717  0.0378  62  LEU B N   
2090 C CA  . LEU B 60  ? 0.5157 0.5225 0.3429 0.0032  0.0725  0.0348  62  LEU B CA  
2091 C C   . LEU B 60  ? 0.5373 0.5467 0.3711 0.0134  0.0762  0.0357  62  LEU B C   
2092 O O   . LEU B 60  ? 0.5640 0.5914 0.3994 0.0172  0.0764  0.0373  62  LEU B O   
2093 C CB  . LEU B 60  ? 0.5156 0.5314 0.3399 -0.0062 0.0691  0.0326  62  LEU B CB  
2094 C CG  . LEU B 60  ? 0.5281 0.5369 0.3553 -0.0074 0.0694  0.0297  62  LEU B CG  
2095 C CD1 . LEU B 60  ? 0.5289 0.5160 0.3563 -0.0083 0.0698  0.0276  62  LEU B CD1 
2096 C CD2 . LEU B 60  ? 0.5480 0.5667 0.3710 -0.0174 0.0660  0.0285  62  LEU B CD2 
2097 N N   . ILE B 61  ? 0.5352 0.5273 0.3729 0.0179  0.0794  0.0344  63  ILE B N   
2098 C CA  . ILE B 61  ? 0.5390 0.5304 0.3820 0.0274  0.0835  0.0348  63  ILE B CA  
2099 C C   . ILE B 61  ? 0.5261 0.5202 0.3717 0.0252  0.0830  0.0307  63  ILE B C   
2100 O O   . ILE B 61  ? 0.5430 0.5507 0.3904 0.0298  0.0839  0.0310  63  ILE B O   
2101 C CB  . ILE B 61  ? 0.5695 0.5416 0.4152 0.0327  0.0877  0.0353  63  ILE B CB  
2102 C CG1 . ILE B 61  ? 0.5991 0.5699 0.4416 0.0355  0.0886  0.0399  63  ILE B CG1 
2103 C CG2 . ILE B 61  ? 0.5782 0.5461 0.4285 0.0414  0.0922  0.0347  63  ILE B CG2 
2104 C CD1 . ILE B 61  ? 0.6250 0.6142 0.4653 0.0414  0.0884  0.0448  63  ILE B CD1 
2105 N N   . SER B 62  ? 0.5108 0.4931 0.3564 0.0188  0.0816  0.0270  64  SER B N   
2106 C CA  . SER B 62  ? 0.5018 0.4859 0.3494 0.0168  0.0811  0.0230  64  SER B CA  
2107 C C   . SER B 62  ? 0.4978 0.4715 0.3434 0.0083  0.0782  0.0201  64  SER B C   
2108 O O   . SER B 62  ? 0.4917 0.4536 0.3359 0.0059  0.0775  0.0206  64  SER B O   
2109 C CB  . SER B 62  ? 0.5261 0.5031 0.3789 0.0251  0.0858  0.0210  64  SER B CB  
2110 O OG  . SER B 62  ? 0.6129 0.5960 0.4670 0.0246  0.0858  0.0172  64  SER B OG  
2111 N N   . LYS B 63  ? 0.4664 0.4452 0.3115 0.0044  0.0765  0.0175  65  LYS B N   
2112 C CA  . LYS B 63  ? 0.4763 0.4461 0.3196 -0.0020 0.0739  0.0150  65  LYS B CA  
2113 C C   . LYS B 63  ? 0.4810 0.4479 0.3284 0.0003  0.0755  0.0107  65  LYS B C   
2114 O O   . LYS B 63  ? 0.4825 0.4586 0.3321 0.0045  0.0776  0.0094  65  LYS B O   
2115 C CB  . LYS B 63  ? 0.4582 0.4364 0.2950 -0.0107 0.0699  0.0161  65  LYS B CB  
2116 C CG  . LYS B 63  ? 0.4528 0.4349 0.2849 -0.0142 0.0682  0.0195  65  LYS B CG  
2117 C CD  . LYS B 63  ? 0.4822 0.4664 0.3068 -0.0244 0.0644  0.0202  65  LYS B CD  
2118 C CE  . LYS B 63  ? 0.4701 0.4557 0.2885 -0.0301 0.0625  0.0225  65  LYS B CE  
2119 N NZ  . LYS B 63  ? 0.4762 0.4621 0.2866 -0.0409 0.0593  0.0229  65  LYS B NZ  
2120 N N   . PHE B 64  ? 0.4765 0.4317 0.3248 -0.0022 0.0745  0.0081  66  PHE B N   
2121 C CA  . PHE B 64  ? 0.4827 0.4358 0.3343 -0.0013 0.0754  0.0034  66  PHE B CA  
2122 C C   . PHE B 64  ? 0.4632 0.4106 0.3128 -0.0070 0.0719  0.0020  66  PHE B C   
2123 O O   . PHE B 64  ? 0.4492 0.3896 0.2961 -0.0097 0.0699  0.0043  66  PHE B O   
2124 C CB  . PHE B 64  ? 0.4803 0.4237 0.3380 0.0047  0.0799  0.0010  66  PHE B CB  
2125 C CG  . PHE B 64  ? 0.4665 0.3974 0.3258 0.0043  0.0804  0.0023  66  PHE B CG  
2126 C CD1 . PHE B 64  ? 0.4799 0.4086 0.3384 0.0069  0.0818  0.0065  66  PHE B CD1 
2127 C CD2 . PHE B 64  ? 0.4540 0.3772 0.3155 0.0014  0.0793  -0.0007 66  PHE B CD2 
2128 C CE1 . PHE B 64  ? 0.4755 0.3937 0.3353 0.0066  0.0825  0.0076  66  PHE B CE1 
2129 C CE2 . PHE B 64  ? 0.4601 0.3741 0.3232 0.0011  0.0797  0.0006  66  PHE B CE2 
2130 C CZ  . PHE B 64  ? 0.4644 0.3753 0.3267 0.0038  0.0816  0.0045  66  PHE B CZ  
2131 N N   . ASP B 65  ? 0.4516 0.4021 0.3018 -0.0081 0.0712  -0.0018 67  ASP B N   
2132 C CA  . ASP B 65  ? 0.4600 0.4061 0.3087 -0.0120 0.0680  -0.0032 67  ASP B CA  
2133 C C   . ASP B 65  ? 0.4558 0.4019 0.3088 -0.0108 0.0690  -0.0090 67  ASP B C   
2134 O O   . ASP B 65  ? 0.4465 0.3948 0.2975 -0.0140 0.0660  -0.0105 67  ASP B O   
2135 C CB  . ASP B 65  ? 0.4905 0.4417 0.3315 -0.0178 0.0638  -0.0002 67  ASP B CB  
2136 C CG  . ASP B 65  ? 0.5681 0.5316 0.4068 -0.0194 0.0635  -0.0016 67  ASP B CG  
2137 O OD1 . ASP B 65  ? 0.5553 0.5268 0.3963 -0.0163 0.0663  -0.0027 67  ASP B OD1 
2138 O OD2 . ASP B 65  ? 0.6013 0.5667 0.4354 -0.0235 0.0604  -0.0013 67  ASP B OD2 
2139 N N   . THR B 66  ? 0.4649 0.4080 0.3235 -0.0062 0.0735  -0.0122 68  THR B N   
2140 C CA  . THR B 66  ? 0.4643 0.4045 0.3274 -0.0055 0.0753  -0.0186 68  THR B CA  
2141 C C   . THR B 66  ? 0.4729 0.4016 0.3418 -0.0026 0.0793  -0.0198 68  THR B C   
2142 O O   . THR B 66  ? 0.4681 0.3926 0.3374 0.0007  0.0818  -0.0159 68  THR B O   
2143 C CB  . THR B 66  ? 0.5022 0.4505 0.3646 -0.0037 0.0772  -0.0230 68  THR B CB  
2144 O OG1 . THR B 66  ? 0.5400 0.4845 0.4050 0.0020  0.0821  -0.0234 68  THR B OG1 
2145 C CG2 . THR B 66  ? 0.4986 0.4600 0.3549 -0.0063 0.0741  -0.0207 68  THR B CG2 
2146 N N   . VAL B 67  ? 0.4856 0.4100 0.3587 -0.0043 0.0799  -0.0251 69  VAL B N   
2147 C CA  . VAL B 67  ? 0.4995 0.4129 0.3783 -0.0031 0.0841  -0.0271 69  VAL B CA  
2148 C C   . VAL B 67  ? 0.4983 0.4064 0.3777 0.0020  0.0896  -0.0277 69  VAL B C   
2149 O O   . VAL B 67  ? 0.5213 0.4206 0.4024 0.0051  0.0932  -0.0246 69  VAL B O   
2150 C CB  . VAL B 67  ? 0.5003 0.4126 0.3835 -0.0071 0.0837  -0.0337 69  VAL B CB  
2151 C CG1 . VAL B 67  ? 0.5208 0.4214 0.4097 -0.0068 0.0888  -0.0356 69  VAL B CG1 
2152 C CG2 . VAL B 67  ? 0.4876 0.4058 0.3704 -0.0108 0.0782  -0.0325 69  VAL B CG2 
2153 N N   . GLU B 68  ? 0.5135 0.4270 0.3908 0.0037  0.0905  -0.0314 70  GLU B N   
2154 C CA  . GLU B 68  ? 0.5367 0.4447 0.4142 0.0098  0.0961  -0.0329 70  GLU B CA  
2155 C C   . GLU B 68  ? 0.5315 0.4427 0.4065 0.0154  0.0971  -0.0256 70  GLU B C   
2156 O O   . GLU B 68  ? 0.5162 0.4192 0.3921 0.0211  0.1017  -0.0239 70  GLU B O   
2157 C CB  . GLU B 68  ? 0.6003 0.5143 0.4759 0.0104  0.0969  -0.0394 70  GLU B CB  
2158 C CG  . GLU B 68  ? 0.6259 0.5351 0.5040 0.0056  0.0973  -0.0478 70  GLU B CG  
2159 C CD  . GLU B 68  ? 0.6691 0.5868 0.5474 -0.0014 0.0914  -0.0491 70  GLU B CD  
2160 O OE1 . GLU B 68  ? 0.6102 0.5373 0.4855 -0.0025 0.0868  -0.0438 70  GLU B OE1 
2161 O OE2 . GLU B 68  ? 0.7131 0.6282 0.5942 -0.0057 0.0915  -0.0555 70  GLU B OE2 
2162 N N   . ASP B 69  ? 0.5346 0.4579 0.4062 0.0136  0.0926  -0.0213 71  ASP B N   
2163 C CA  . ASP B 69  ? 0.5234 0.4520 0.3928 0.0174  0.0927  -0.0146 71  ASP B CA  
2164 C C   . ASP B 69  ? 0.5051 0.4242 0.3759 0.0177  0.0934  -0.0101 71  ASP B C   
2165 O O   . ASP B 69  ? 0.5038 0.4216 0.3741 0.0231  0.0961  -0.0057 71  ASP B O   
2166 C CB  . ASP B 69  ? 0.5195 0.4632 0.3843 0.0136  0.0878  -0.0119 71  ASP B CB  
2167 C CG  . ASP B 69  ? 0.6062 0.5611 0.4695 0.0144  0.0880  -0.0158 71  ASP B CG  
2168 O OD1 . ASP B 69  ? 0.6276 0.5811 0.4924 0.0205  0.0923  -0.0186 71  ASP B OD1 
2169 O OD2 . ASP B 69  ? 0.6425 0.6064 0.5026 0.0090  0.0841  -0.0162 71  ASP B OD2 
2170 N N   . PHE B 70  ? 0.4859 0.3990 0.3583 0.0124  0.0914  -0.0111 72  PHE B N   
2171 C CA  . PHE B 70  ? 0.4712 0.3746 0.3454 0.0127  0.0928  -0.0078 72  PHE B CA  
2172 C C   . PHE B 70  ? 0.4658 0.3577 0.3430 0.0177  0.0992  -0.0082 72  PHE B C   
2173 O O   . PHE B 70  ? 0.4580 0.3468 0.3343 0.0219  0.1015  -0.0031 72  PHE B O   
2174 C CB  . PHE B 70  ? 0.4613 0.3609 0.3378 0.0070  0.0902  -0.0099 72  PHE B CB  
2175 C CG  . PHE B 70  ? 0.4807 0.3702 0.3603 0.0077  0.0932  -0.0079 72  PHE B CG  
2176 C CD1 . PHE B 70  ? 0.4945 0.3834 0.3714 0.0092  0.0928  -0.0022 72  PHE B CD1 
2177 C CD2 . PHE B 70  ? 0.4948 0.3758 0.3798 0.0066  0.0967  -0.0119 72  PHE B CD2 
2178 C CE1 . PHE B 70  ? 0.4842 0.3645 0.3637 0.0100  0.0960  -0.0002 72  PHE B CE1 
2179 C CE2 . PHE B 70  ? 0.4808 0.3532 0.3686 0.0067  0.1000  -0.0098 72  PHE B CE2 
2180 C CZ  . PHE B 70  ? 0.4720 0.3443 0.3570 0.0088  0.0996  -0.0038 72  PHE B CZ  
2181 N N   . TRP B 71  ? 0.4801 0.3656 0.3603 0.0170  0.1019  -0.0143 73  TRP B N   
2182 C CA  . TRP B 71  ? 0.5070 0.3788 0.3894 0.0207  0.1082  -0.0151 73  TRP B CA  
2183 C C   . TRP B 71  ? 0.5091 0.3806 0.3885 0.0293  0.1118  -0.0116 73  TRP B C   
2184 O O   . TRP B 71  ? 0.5404 0.4015 0.4198 0.0338  0.1163  -0.0079 73  TRP B O   
2185 C CB  . TRP B 71  ? 0.5033 0.3679 0.3887 0.0171  0.1104  -0.0233 73  TRP B CB  
2186 C CG  . TRP B 71  ? 0.5020 0.3646 0.3918 0.0096  0.1087  -0.0262 73  TRP B CG  
2187 C CD1 . TRP B 71  ? 0.5075 0.3769 0.3991 0.0037  0.1049  -0.0320 73  TRP B CD1 
2188 C CD2 . TRP B 71  ? 0.4895 0.3441 0.3826 0.0076  0.1108  -0.0235 73  TRP B CD2 
2189 N NE1 . TRP B 71  ? 0.5185 0.3859 0.4145 -0.0014 0.1042  -0.0329 73  TRP B NE1 
2190 C CE2 . TRP B 71  ? 0.5036 0.3616 0.4009 0.0007  0.1081  -0.0281 73  TRP B CE2 
2191 C CE3 . TRP B 71  ? 0.4938 0.3395 0.3864 0.0113  0.1148  -0.0175 73  TRP B CE3 
2192 C CZ2 . TRP B 71  ? 0.5215 0.3754 0.4231 -0.0028 0.1094  -0.0271 73  TRP B CZ2 
2193 C CZ3 . TRP B 71  ? 0.5167 0.3573 0.4130 0.0074  0.1163  -0.0165 73  TRP B CZ3 
2194 C CH2 . TRP B 71  ? 0.5135 0.3584 0.4146 0.0004  0.1137  -0.0214 73  TRP B CH2 
2195 N N   . ALA B 72  ? 0.5078 0.3911 0.3846 0.0321  0.1100  -0.0124 74  ALA B N   
2196 C CA  . ALA B 72  ? 0.5134 0.3995 0.3877 0.0413  0.1131  -0.0091 74  ALA B CA  
2197 C C   . ALA B 72  ? 0.5107 0.4017 0.3832 0.0444  0.1121  -0.0007 74  ALA B C   
2198 O O   . ALA B 72  ? 0.5088 0.3940 0.3803 0.0521  0.1163  0.0036  74  ALA B O   
2199 C CB  . ALA B 72  ? 0.5132 0.4143 0.3856 0.0427  0.1109  -0.0117 74  ALA B CB  
2200 N N   . LEU B 73  ? 0.4942 0.3948 0.3656 0.0386  0.1067  0.0016  75  LEU B N   
2201 C CA  . LEU B 73  ? 0.5083 0.4129 0.3775 0.0401  0.1055  0.0086  75  LEU B CA  
2202 C C   . LEU B 73  ? 0.5144 0.4042 0.3850 0.0411  0.1092  0.0113  75  LEU B C   
2203 O O   . LEU B 73  ? 0.5222 0.4106 0.3909 0.0475  0.1119  0.0169  75  LEU B O   
2204 C CB  . LEU B 73  ? 0.5067 0.4221 0.3737 0.0328  0.0994  0.0095  75  LEU B CB  
2205 C CG  . LEU B 73  ? 0.5426 0.4633 0.4063 0.0331  0.0976  0.0157  75  LEU B CG  
2206 C CD1 . LEU B 73  ? 0.5478 0.4796 0.4095 0.0405  0.0990  0.0201  75  LEU B CD1 
2207 C CD2 . LEU B 73  ? 0.5613 0.4900 0.4218 0.0251  0.0918  0.0156  75  LEU B CD2 
2208 N N   . TYR B 74  ? 0.5034 0.3833 0.3770 0.0350  0.1093  0.0076  76  TYR B N   
2209 C CA  . TYR B 74  ? 0.5276 0.3944 0.4029 0.0347  0.1128  0.0098  76  TYR B CA  
2210 C C   . TYR B 74  ? 0.5465 0.4010 0.4219 0.0417  0.1197  0.0114  76  TYR B C   
2211 O O   . TYR B 74  ? 0.5490 0.3981 0.4226 0.0457  0.1226  0.0172  76  TYR B O   
2212 C CB  . TYR B 74  ? 0.5476 0.4085 0.4273 0.0270  0.1120  0.0043  76  TYR B CB  
2213 C CG  . TYR B 74  ? 0.5568 0.4054 0.4392 0.0257  0.1162  0.0057  76  TYR B CG  
2214 C CD1 . TYR B 74  ? 0.5677 0.4180 0.4497 0.0234  0.1146  0.0092  76  TYR B CD1 
2215 C CD2 . TYR B 74  ? 0.5719 0.4068 0.4568 0.0263  0.1222  0.0034  76  TYR B CD2 
2216 C CE1 . TYR B 74  ? 0.5715 0.4121 0.4561 0.0221  0.1187  0.0107  76  TYR B CE1 
2217 C CE2 . TYR B 74  ? 0.5820 0.4059 0.4692 0.0243  0.1264  0.0050  76  TYR B CE2 
2218 C CZ  . TYR B 74  ? 0.5982 0.4260 0.4854 0.0222  0.1247  0.0088  76  TYR B CZ  
2219 O OH  . TYR B 74  ? 0.6354 0.4542 0.5252 0.0198  0.1290  0.0105  76  TYR B OH  
2220 N N   . ASN B 75  ? 0.5764 0.4261 0.4527 0.0435  0.1222  0.0064  77  ASN B N   
2221 C CA  . ASN B 75  ? 0.6234 0.4585 0.4987 0.0505  0.1291  0.0073  77  ASN B CA  
2222 C C   . ASN B 75  ? 0.6467 0.4875 0.5178 0.0610  0.1305  0.0149  77  ASN B C   
2223 O O   . ASN B 75  ? 0.6695 0.4987 0.5385 0.0669  0.1355  0.0201  77  ASN B O   
2224 C CB  . ASN B 75  ? 0.6470 0.4776 0.5233 0.0504  0.1310  -0.0006 77  ASN B CB  
2225 C CG  . ASN B 75  ? 0.7409 0.5641 0.6213 0.0408  0.1309  -0.0084 77  ASN B CG  
2226 O OD1 . ASN B 75  ? 0.7695 0.5866 0.6527 0.0350  0.1314  -0.0080 77  ASN B OD1 
2227 N ND2 . ASN B 75  ? 0.7710 0.5962 0.6519 0.0389  0.1303  -0.0161 77  ASN B ND2 
2228 N N   . HIS B 76  ? 0.6297 0.4890 0.4992 0.0630  0.1259  0.0159  78  HIS B N   
2229 C CA  . HIS B 76  ? 0.6415 0.5118 0.5076 0.0724  0.1261  0.0225  78  HIS B CA  
2230 C C   . HIS B 76  ? 0.6416 0.5141 0.5054 0.0732  0.1253  0.0301  78  HIS B C   
2231 O O   . HIS B 76  ? 0.6373 0.5072 0.4984 0.0824  0.1289  0.0364  78  HIS B O   
2232 C CB  . HIS B 76  ? 0.6688 0.5609 0.5344 0.0718  0.1209  0.0210  78  HIS B CB  
2233 C CG  . HIS B 76  ? 0.8009 0.7079 0.6638 0.0809  0.1207  0.0273  78  HIS B CG  
2234 N ND1 . HIS B 76  ? 0.8408 0.7671 0.7022 0.0778  0.1153  0.0306  78  HIS B ND1 
2235 C CD2 . HIS B 76  ? 0.8500 0.7552 0.7114 0.0929  0.1253  0.0306  78  HIS B CD2 
2236 C CE1 . HIS B 76  ? 0.8521 0.7900 0.7117 0.0875  0.1165  0.0358  78  HIS B CE1 
2237 N NE2 . HIS B 76  ? 0.8636 0.7895 0.7231 0.0975  0.1224  0.0364  78  HIS B NE2 
2238 N N   . ILE B 77  ? 0.6231 0.5002 0.4877 0.0644  0.1209  0.0296  79  ILE B N   
2239 C CA  . ILE B 77  ? 0.6452 0.5235 0.5072 0.0643  0.1203  0.0357  79  ILE B CA  
2240 C C   . ILE B 77  ? 0.7126 0.5722 0.5747 0.0666  0.1263  0.0385  79  ILE B C   
2241 O O   . ILE B 77  ? 0.7168 0.5760 0.5754 0.0727  0.1286  0.0456  79  ILE B O   
2242 C CB  . ILE B 77  ? 0.6268 0.5115 0.4890 0.0546  0.1148  0.0338  79  ILE B CB  
2243 C CG1 . ILE B 77  ? 0.6262 0.5288 0.4868 0.0515  0.1090  0.0321  79  ILE B CG1 
2244 C CG2 . ILE B 77  ? 0.6367 0.5208 0.4957 0.0547  0.1150  0.0394  79  ILE B CG2 
2245 C CD1 . ILE B 77  ? 0.6328 0.5512 0.4901 0.0573  0.1077  0.0367  79  ILE B CD1 
2246 N N   . GLN B 78  ? 0.7573 0.6023 0.6234 0.0612  0.1290  0.0330  80  GLN B N   
2247 C CA  . GLN B 78  ? 0.7941 0.6206 0.6610 0.0606  0.1349  0.0346  80  GLN B CA  
2248 C C   . GLN B 78  ? 0.8459 0.6620 0.7091 0.0712  0.1411  0.0401  80  GLN B C   
2249 O O   . GLN B 78  ? 0.8598 0.6677 0.7203 0.0741  0.1449  0.0464  80  GLN B O   
2250 C CB  . GLN B 78  ? 0.7980 0.6141 0.6701 0.0523  0.1361  0.0266  80  GLN B CB  
2251 C CG  . GLN B 78  ? 0.8362 0.6379 0.7106 0.0475  0.1407  0.0271  80  GLN B CG  
2252 C CD  . GLN B 78  ? 0.8678 0.6603 0.7474 0.0400  0.1424  0.0188  80  GLN B CD  
2253 O OE1 . GLN B 78  ? 0.8802 0.6709 0.7605 0.0405  0.1426  0.0133  80  GLN B OE1 
2254 N NE2 . GLN B 78  ? 0.8841 0.6717 0.7676 0.0326  0.1438  0.0174  80  GLN B NE2 
2255 N N   . LEU B 79  ? 0.8831 0.6997 0.7455 0.0775  0.1423  0.0381  81  LEU B N   
2256 C CA  . LEU B 79  ? 0.9219 0.7290 0.7800 0.0894  0.1481  0.0438  81  LEU B CA  
2257 C C   . LEU B 79  ? 0.9482 0.7715 0.8020 0.0984  0.1459  0.0526  81  LEU B C   
2258 O O   . LEU B 79  ? 0.9689 0.7829 0.8185 0.1068  0.1507  0.0599  81  LEU B O   
2259 C CB  . LEU B 79  ? 0.9335 0.7325 0.7915 0.0949  0.1515  0.0388  81  LEU B CB  
2260 C CG  . LEU B 79  ? 0.9466 0.7625 0.8065 0.0949  0.1469  0.0330  81  LEU B CG  
2261 C CD1 . LEU B 79  ? 0.9521 0.7875 0.8092 0.1049  0.1445  0.0388  81  LEU B CD1 
2262 C CD2 . LEU B 79  ? 0.9548 0.7564 0.8148 0.0973  0.1515  0.0261  81  LEU B CD2 
2263 N N   . SER B 80  ? 0.9343 0.7812 0.7885 0.0965  0.1390  0.0522  82  SER B N   
2264 C CA  . SER B 80  ? 0.9265 0.7910 0.7768 0.1046  0.1368  0.0596  82  SER B CA  
2265 C C   . SER B 80  ? 0.9142 0.7879 0.7619 0.1005  0.1334  0.0645  82  SER B C   
2266 O O   . SER B 80  ? 0.9039 0.7952 0.7485 0.1056  0.1307  0.0696  82  SER B O   
2267 C CB  . SER B 80  ? 0.9489 0.8351 0.8004 0.1058  0.1320  0.0567  82  SER B CB  
2268 O OG  . SER B 80  ? 0.9801 0.8787 0.8335 0.0945  0.1256  0.0524  82  SER B OG  
2269 N N   . SER B 81  ? 0.9153 0.7787 0.7643 0.0916  0.1336  0.0626  83  SER B N   
2270 C CA  . SER B 81  ? 0.9220 0.7957 0.7687 0.0864  0.1296  0.0651  83  SER B CA  
2271 C C   . SER B 81  ? 0.9352 0.8069 0.7766 0.0936  0.1329  0.0740  83  SER B C   
2272 O O   . SER B 81  ? 0.9322 0.8185 0.7699 0.0929  0.1292  0.0772  83  SER B O   
2273 C CB  . SER B 81  ? 0.9328 0.7986 0.7828 0.0752  0.1284  0.0597  83  SER B CB  
2274 O OG  . SER B 81  ? 0.9706 0.8162 0.8224 0.0744  0.1345  0.0599  83  SER B OG  
2275 N N   . ASN B 82  ? 0.9509 0.8045 0.7911 0.1000  0.1399  0.0780  84  ASN B N   
2276 C CA  . ASN B 82  ? 0.9692 0.8211 0.8033 0.1083  0.1433  0.0877  84  ASN B CA  
2277 C C   . ASN B 82  ? 0.9707 0.8441 0.8008 0.1179  0.1401  0.0933  84  ASN B C   
2278 O O   . ASN B 82  ? 0.9802 0.8607 0.8048 0.1225  0.1401  0.1006  84  ASN B O   
2279 C CB  . ASN B 82  ? 0.9991 0.8261 0.8318 0.1139  0.1519  0.0914  84  ASN B CB  
2280 C CG  . ASN B 82  ? 1.0461 0.8644 0.8799 0.1212  0.1550  0.0894  84  ASN B CG  
2281 O OD1 . ASN B 82  ? 1.0480 0.8815 0.8834 0.1245  0.1511  0.0866  84  ASN B OD1 
2282 N ND2 . ASN B 82  ? 1.0772 0.8704 0.9100 0.1236  0.1626  0.0906  84  ASN B ND2 
2283 N N   . LEU B 83  ? 0.9614 0.8464 0.7941 0.1207  0.1373  0.0897  85  LEU B N   
2284 C CA  . LEU B 83  ? 0.9622 0.8702 0.7927 0.1293  0.1340  0.0937  85  LEU B CA  
2285 C C   . LEU B 83  ? 0.9585 0.8918 0.7897 0.1208  0.1259  0.0900  85  LEU B C   
2286 O O   . LEU B 83  ? 0.9628 0.9185 0.7924 0.1263  0.1227  0.0930  85  LEU B O   
2287 C CB  . LEU B 83  ? 0.9638 0.8699 0.7968 0.1376  0.1365  0.0916  85  LEU B CB  
2288 C CG  . LEU B 83  ? 0.9992 0.8814 0.8296 0.1488  0.1448  0.0962  85  LEU B CG  
2289 C CD1 . LEU B 83  ? 1.0079 0.8830 0.8414 0.1534  0.1474  0.0908  85  LEU B CD1 
2290 C CD2 . LEU B 83  ? 1.0063 0.8956 0.8304 0.1630  0.1468  0.1075  85  LEU B CD2 
2291 N N   . MET B 84  ? 0.9432 0.8732 0.7764 0.1077  0.1228  0.0838  86  MET B N   
2292 C CA  . MET B 84  ? 0.9232 0.8735 0.7562 0.0991  0.1156  0.0800  86  MET B CA  
2293 C C   . MET B 84  ? 0.8948 0.8535 0.7222 0.0969  0.1134  0.0841  86  MET B C   
2294 O O   . MET B 84  ? 0.8883 0.8324 0.7137 0.0959  0.1166  0.0862  86  MET B O   
2295 C CB  . MET B 84  ? 0.9481 0.8907 0.7852 0.0870  0.1132  0.0714  86  MET B CB  
2296 C CG  . MET B 84  ? 0.9953 0.9526 0.8352 0.0836  0.1089  0.0662  86  MET B CG  
2297 S SD  . MET B 84  ? 1.1150 1.0617 0.9591 0.0715  0.1068  0.0572  86  MET B SD  
2298 C CE  . MET B 84  ? 1.1339 1.0607 0.9825 0.0779  0.1133  0.0555  86  MET B CE  
2299 N N   . PRO B 85  ? 0.8740 0.8566 0.6984 0.0956  0.1081  0.0850  87  PRO B N   
2300 C CA  . PRO B 85  ? 0.8656 0.8571 0.6836 0.0944  0.1063  0.0889  87  PRO B CA  
2301 C C   . PRO B 85  ? 0.8491 0.8350 0.6651 0.0818  0.1034  0.0837  87  PRO B C   
2302 O O   . PRO B 85  ? 0.8327 0.8337 0.6456 0.0746  0.0981  0.0809  87  PRO B O   
2303 C CB  . PRO B 85  ? 0.8697 0.8902 0.6859 0.0976  0.1018  0.0911  87  PRO B CB  
2304 C CG  . PRO B 85  ? 0.8730 0.8999 0.6942 0.0920  0.0989  0.0847  87  PRO B CG  
2305 C CD  . PRO B 85  ? 0.8583 0.8621 0.6847 0.0947  0.1038  0.0823  87  PRO B CD  
2306 N N   . GLY B 86  ? 0.8509 0.8150 0.6685 0.0793  0.1072  0.0822  88  GLY B N   
2307 C CA  . GLY B 86  ? 0.8596 0.8164 0.6755 0.0693  0.1055  0.0777  88  GLY B CA  
2308 C C   . GLY B 86  ? 0.8507 0.7858 0.6717 0.0658  0.1091  0.0740  88  GLY B C   
2309 O O   . GLY B 86  ? 0.8586 0.7830 0.6845 0.0700  0.1129  0.0743  88  GLY B O   
2310 N N   . CYS B 87  ? 0.8261 0.7553 0.6459 0.0578  0.1077  0.0700  89  CYS B N   
2311 C CA  . CYS B 87  ? 0.8228 0.7343 0.6459 0.0557  0.1118  0.0685  89  CYS B CA  
2312 C C   . CYS B 87  ? 0.7767 0.6836 0.6018 0.0464  0.1086  0.0611  89  CYS B C   
2313 O O   . CYS B 87  ? 0.7848 0.6822 0.6106 0.0437  0.1107  0.0597  89  CYS B O   
2314 C CB  . CYS B 87  ? 0.8612 0.7707 0.6790 0.0588  0.1152  0.0739  89  CYS B CB  
2315 S SG  . CYS B 87  ? 1.0642 0.9655 0.8819 0.0696  0.1224  0.0827  89  CYS B SG  
2316 N N   . ASP B 88  ? 0.7003 0.6144 0.5261 0.0419  0.1036  0.0567  90  ASP B N   
2317 C CA  . ASP B 88  ? 0.6475 0.5579 0.4732 0.0339  0.1002  0.0507  90  ASP B CA  
2318 C C   . ASP B 88  ? 0.5817 0.4945 0.4113 0.0308  0.0972  0.0468  90  ASP B C   
2319 O O   . ASP B 88  ? 0.5735 0.4989 0.4011 0.0309  0.0943  0.0475  90  ASP B O   
2320 C CB  . ASP B 88  ? 0.6825 0.6015 0.4999 0.0298  0.0963  0.0502  90  ASP B CB  
2321 C CG  . ASP B 88  ? 0.7702 0.6877 0.5828 0.0325  0.0991  0.0535  90  ASP B CG  
2322 O OD1 . ASP B 88  ? 0.7232 0.6296 0.5375 0.0316  0.1019  0.0522  90  ASP B OD1 
2323 O OD2 . ASP B 88  ? 0.8422 0.7709 0.6495 0.0356  0.0986  0.0575  90  ASP B OD2 
2324 N N   . TYR B 89  ? 0.5323 0.4346 0.3675 0.0281  0.0979  0.0427  91  TYR B N   
2325 C CA  . TYR B 89  ? 0.5178 0.4220 0.3565 0.0253  0.0953  0.0389  91  TYR B CA  
2326 C C   . TYR B 89  ? 0.4785 0.3773 0.3167 0.0187  0.0922  0.0344  91  TYR B C   
2327 O O   . TYR B 89  ? 0.4742 0.3649 0.3129 0.0179  0.0937  0.0336  91  TYR B O   
2328 C CB  . TYR B 89  ? 0.5256 0.4225 0.3715 0.0289  0.0992  0.0382  91  TYR B CB  
2329 C CG  . TYR B 89  ? 0.5644 0.4651 0.4105 0.0365  0.1024  0.0425  91  TYR B CG  
2330 C CD1 . TYR B 89  ? 0.6059 0.5013 0.4510 0.0419  0.1070  0.0474  91  TYR B CD1 
2331 C CD2 . TYR B 89  ? 0.5960 0.5055 0.4430 0.0387  0.1011  0.0420  91  TYR B CD2 
2332 C CE1 . TYR B 89  ? 0.6293 0.5267 0.4740 0.0501  0.1102  0.0521  91  TYR B CE1 
2333 C CE2 . TYR B 89  ? 0.6221 0.5345 0.4693 0.0471  0.1044  0.0460  91  TYR B CE2 
2334 C CZ  . TYR B 89  ? 0.6605 0.5662 0.5063 0.0530  0.1089  0.0513  91  TYR B CZ  
2335 O OH  . TYR B 89  ? 0.7156 0.6229 0.5605 0.0624  0.1123  0.0561  91  TYR B OH  
2336 N N   . SER B 90  ? 0.4692 0.3729 0.3064 0.0144  0.0882  0.0317  92  SER B N   
2337 C CA  . SER B 90  ? 0.4581 0.3566 0.2939 0.0088  0.0850  0.0280  92  SER B CA  
2338 C C   . SER B 90  ? 0.4540 0.3547 0.2932 0.0067  0.0830  0.0252  92  SER B C   
2339 O O   . SER B 90  ? 0.4921 0.4023 0.3309 0.0072  0.0822  0.0260  92  SER B O   
2340 C CB  . SER B 90  ? 0.4569 0.3585 0.2838 0.0039  0.0812  0.0280  92  SER B CB  
2341 O OG  . SER B 90  ? 0.5476 0.4481 0.3706 0.0056  0.0829  0.0300  92  SER B OG  
2342 N N   . LEU B 91  ? 0.4349 0.3286 0.2772 0.0047  0.0823  0.0221  93  LEU B N   
2343 C CA  . LEU B 91  ? 0.4487 0.3447 0.2928 0.0021  0.0800  0.0194  93  LEU B CA  
2344 C C   . LEU B 91  ? 0.4490 0.3413 0.2877 -0.0029 0.0759  0.0181  93  LEU B C   
2345 O O   . LEU B 91  ? 0.4503 0.3346 0.2899 -0.0026 0.0761  0.0169  93  LEU B O   
2346 C CB  . LEU B 91  ? 0.4577 0.3492 0.3098 0.0042  0.0824  0.0166  93  LEU B CB  
2347 C CG  . LEU B 91  ? 0.4720 0.3678 0.3255 0.0018  0.0801  0.0136  93  LEU B CG  
2348 C CD1 . LEU B 91  ? 0.4920 0.3959 0.3462 0.0043  0.0814  0.0143  93  LEU B CD1 
2349 C CD2 . LEU B 91  ? 0.4936 0.3848 0.3535 0.0017  0.0810  0.0099  93  LEU B CD2 
2350 N N   . PHE B 92  ? 0.4193 0.3174 0.2523 -0.0073 0.0725  0.0185  94  PHE B N   
2351 C CA  . PHE B 92  ? 0.4343 0.3269 0.2605 -0.0124 0.0689  0.0178  94  PHE B CA  
2352 C C   . PHE B 92  ? 0.4373 0.3336 0.2622 -0.0159 0.0662  0.0169  94  PHE B C   
2353 O O   . PHE B 92  ? 0.4366 0.3432 0.2639 -0.0160 0.0664  0.0169  94  PHE B O   
2354 C CB  . PHE B 92  ? 0.4310 0.3236 0.2481 -0.0163 0.0674  0.0194  94  PHE B CB  
2355 C CG  . PHE B 92  ? 0.4382 0.3222 0.2533 -0.0141 0.0690  0.0195  94  PHE B CG  
2356 C CD1 . PHE B 92  ? 0.4614 0.3473 0.2813 -0.0089 0.0726  0.0206  94  PHE B CD1 
2357 C CD2 . PHE B 92  ? 0.4639 0.3372 0.2719 -0.0168 0.0673  0.0185  94  PHE B CD2 
2358 C CE1 . PHE B 92  ? 0.4820 0.3608 0.3001 -0.0068 0.0744  0.0207  94  PHE B CE1 
2359 C CE2 . PHE B 92  ? 0.4850 0.3509 0.2914 -0.0141 0.0691  0.0181  94  PHE B CE2 
2360 C CZ  . PHE B 92  ? 0.4796 0.3491 0.2910 -0.0094 0.0726  0.0191  94  PHE B CZ  
2361 N N   . LYS B 93  ? 0.4482 0.3366 0.2692 -0.0185 0.0636  0.0163  95  LYS B N   
2362 C CA  . LYS B 93  ? 0.4476 0.3392 0.2657 -0.0224 0.0608  0.0161  95  LYS B CA  
2363 C C   . LYS B 93  ? 0.4545 0.3545 0.2663 -0.0281 0.0595  0.0179  95  LYS B C   
2364 O O   . LYS B 93  ? 0.4513 0.3504 0.2576 -0.0308 0.0594  0.0191  95  LYS B O   
2365 C CB  . LYS B 93  ? 0.4783 0.3591 0.2914 -0.0237 0.0583  0.0162  95  LYS B CB  
2366 C CG  . LYS B 93  ? 0.4957 0.3728 0.3158 -0.0186 0.0590  0.0143  95  LYS B CG  
2367 C CD  . LYS B 93  ? 0.5196 0.3873 0.3345 -0.0186 0.0566  0.0149  95  LYS B CD  
2368 C CE  . LYS B 93  ? 0.5370 0.4053 0.3598 -0.0138 0.0569  0.0129  95  LYS B CE  
2369 N NZ  . LYS B 93  ? 0.5207 0.3799 0.3385 -0.0121 0.0547  0.0139  95  LYS B NZ  
2370 N N   . ASP B 94  ? 0.4811 0.3904 0.2938 -0.0301 0.0587  0.0177  96  ASP B N   
2371 C CA  . ASP B 94  ? 0.4901 0.4109 0.2982 -0.0356 0.0576  0.0192  96  ASP B CA  
2372 C C   . ASP B 94  ? 0.5300 0.4425 0.3269 -0.0434 0.0551  0.0209  96  ASP B C   
2373 O O   . ASP B 94  ? 0.5437 0.4443 0.3358 -0.0451 0.0535  0.0212  96  ASP B O   
2374 C CB  . ASP B 94  ? 0.4996 0.4304 0.3098 -0.0365 0.0571  0.0185  96  ASP B CB  
2375 C CG  . ASP B 94  ? 0.5496 0.4968 0.3583 -0.0403 0.0571  0.0196  96  ASP B CG  
2376 O OD1 . ASP B 94  ? 0.5420 0.4952 0.3496 -0.0413 0.0577  0.0208  96  ASP B OD1 
2377 O OD2 . ASP B 94  ? 0.5705 0.5259 0.3793 -0.0421 0.0566  0.0191  96  ASP B OD2 
2378 N N   . GLY B 95  ? 0.5318 0.4502 0.3247 -0.0475 0.0551  0.0218  97  GLY B N   
2379 C CA  . GLY B 95  ? 0.5552 0.4646 0.3370 -0.0556 0.0532  0.0226  97  GLY B CA  
2380 C C   . GLY B 95  ? 0.5832 0.4792 0.3616 -0.0538 0.0538  0.0218  97  GLY B C   
2381 O O   . GLY B 95  ? 0.6273 0.5140 0.3956 -0.0604 0.0525  0.0218  97  GLY B O   
2382 N N   . ILE B 96  ? 0.5659 0.4599 0.3516 -0.0454 0.0559  0.0209  98  ILE B N   
2383 C CA  . ILE B 96  ? 0.5525 0.4362 0.3354 -0.0433 0.0570  0.0202  98  ILE B CA  
2384 C C   . ILE B 96  ? 0.5840 0.4796 0.3711 -0.0401 0.0589  0.0206  98  ILE B C   
2385 O O   . ILE B 96  ? 0.5848 0.4879 0.3810 -0.0337 0.0610  0.0211  98  ILE B O   
2386 C CB  . ILE B 96  ? 0.5286 0.3996 0.3154 -0.0364 0.0581  0.0192  98  ILE B CB  
2387 C CG1 . ILE B 96  ? 0.5276 0.3884 0.3108 -0.0378 0.0561  0.0193  98  ILE B CG1 
2388 C CG2 . ILE B 96  ? 0.5301 0.3916 0.3132 -0.0343 0.0595  0.0182  98  ILE B CG2 
2389 C CD1 . ILE B 96  ? 0.5364 0.3878 0.3243 -0.0307 0.0569  0.0183  98  ILE B CD1 
2390 N N   . GLU B 97  ? 0.6103 0.5070 0.3903 -0.0445 0.0584  0.0204  99  GLU B N   
2391 C CA  . GLU B 97  ? 0.6373 0.5446 0.4203 -0.0406 0.0601  0.0213  99  GLU B CA  
2392 C C   . GLU B 97  ? 0.6169 0.5137 0.4025 -0.0336 0.0628  0.0208  99  GLU B C   
2393 O O   . GLU B 97  ? 0.6183 0.5000 0.3993 -0.0342 0.0625  0.0192  99  GLU B O   
2394 C CB  . GLU B 97  ? 0.7137 0.6281 0.4880 -0.0483 0.0584  0.0209  99  GLU B CB  
2395 C CG  . GLU B 97  ? 0.8842 0.8118 0.6567 -0.0558 0.0562  0.0215  99  GLU B CG  
2396 C CD  . GLU B 97  ? 1.1150 1.0561 0.8815 -0.0628 0.0547  0.0213  99  GLU B CD  
2397 O OE1 . GLU B 97  ? 1.1820 1.1167 0.9420 -0.0646 0.0547  0.0197  99  GLU B OE1 
2398 O OE2 . GLU B 97  ? 1.1891 1.1485 0.9574 -0.0666 0.0536  0.0223  99  GLU B OE2 
2399 N N   . PRO B 98  ? 0.6060 0.5107 0.3986 -0.0265 0.0655  0.0225  100 PRO B N   
2400 C CA  . PRO B 98  ? 0.6040 0.4998 0.3993 -0.0203 0.0685  0.0225  100 PRO B CA  
2401 C C   . PRO B 98  ? 0.5962 0.4900 0.3835 -0.0219 0.0687  0.0221  100 PRO B C   
2402 O O   . PRO B 98  ? 0.5929 0.4912 0.3822 -0.0170 0.0712  0.0238  100 PRO B O   
2403 C CB  . PRO B 98  ? 0.6144 0.5190 0.4191 -0.0131 0.0716  0.0250  100 PRO B CB  
2404 C CG  . PRO B 98  ? 0.6191 0.5398 0.4229 -0.0150 0.0701  0.0267  100 PRO B CG  
2405 C CD  . PRO B 98  ? 0.6054 0.5270 0.4034 -0.0236 0.0663  0.0249  100 PRO B CD  
2406 N N   . MET B 99  ? 0.6017 0.4879 0.3793 -0.0288 0.0662  0.0197  101 MET B N   
2407 C CA  . MET B 99  ? 0.6210 0.5040 0.3888 -0.0322 0.0659  0.0180  101 MET B CA  
2408 C C   . MET B 99  ? 0.6395 0.5029 0.4006 -0.0343 0.0654  0.0148  101 MET B C   
2409 O O   . MET B 99  ? 0.6238 0.4801 0.3832 -0.0379 0.0635  0.0143  101 MET B O   
2410 C CB  . MET B 99  ? 0.6394 0.5346 0.4005 -0.0406 0.0630  0.0177  101 MET B CB  
2411 C CG  . MET B 99  ? 0.6995 0.6161 0.4671 -0.0380 0.0632  0.0210  101 MET B CG  
2412 S SD  . MET B 99  ? 0.8449 0.7711 0.6152 -0.0296 0.0661  0.0239  101 MET B SD  
2413 C CE  . MET B 99  ? 0.8794 0.8047 0.6363 -0.0370 0.0644  0.0206  101 MET B CE  
2414 N N   . TRP B 100 ? 0.6744 0.5294 0.4311 -0.0317 0.0673  0.0131  102 TRP B N   
2415 C CA  . TRP B 100 ? 0.7350 0.5710 0.4863 -0.0310 0.0675  0.0103  102 TRP B CA  
2416 C C   . TRP B 100 ? 0.7466 0.5724 0.4854 -0.0401 0.0647  0.0078  102 TRP B C   
2417 O O   . TRP B 100 ? 0.7755 0.5852 0.5102 -0.0397 0.0643  0.0065  102 TRP B O   
2418 C CB  . TRP B 100 ? 0.7587 0.5891 0.5090 -0.0250 0.0708  0.0089  102 TRP B CB  
2419 C CG  . TRP B 100 ? 0.7919 0.6193 0.5300 -0.0293 0.0707  0.0059  102 TRP B CG  
2420 C CD1 . TRP B 100 ? 0.7993 0.6397 0.5352 -0.0306 0.0711  0.0065  102 TRP B CD1 
2421 C CD2 . TRP B 100 ? 0.8096 0.6193 0.5355 -0.0322 0.0705  0.0016  102 TRP B CD2 
2422 N NE1 . TRP B 100 ? 0.8120 0.6452 0.5352 -0.0350 0.0709  0.0024  102 TRP B NE1 
2423 C CE2 . TRP B 100 ? 0.8168 0.6301 0.5335 -0.0360 0.0707  -0.0009 102 TRP B CE2 
2424 C CE3 . TRP B 100 ? 0.8245 0.6156 0.5460 -0.0312 0.0702  -0.0004 102 TRP B CE3 
2425 C CZ2 . TRP B 100 ? 0.8352 0.6330 0.5383 -0.0396 0.0709  -0.0060 102 TRP B CZ2 
2426 C CZ3 . TRP B 100 ? 0.8453 0.6201 0.5533 -0.0338 0.0706  -0.0048 102 TRP B CZ3 
2427 C CH2 . TRP B 100 ? 0.8450 0.6227 0.5438 -0.0383 0.0710  -0.0080 102 TRP B CH2 
2428 N N   . GLU B 101 ? 0.7493 0.5847 0.4822 -0.0484 0.0627  0.0074  103 GLU B N   
2429 C CA  . GLU B 101 ? 0.7784 0.6050 0.4989 -0.0591 0.0602  0.0049  103 GLU B CA  
2430 C C   . GLU B 101 ? 0.7709 0.5972 0.4929 -0.0635 0.0581  0.0069  103 GLU B C   
2431 O O   . GLU B 101 ? 0.7850 0.6004 0.4965 -0.0722 0.0565  0.0054  103 GLU B O   
2432 C CB  . GLU B 101 ? 0.8335 0.6742 0.5478 -0.0673 0.0588  0.0035  103 GLU B CB  
2433 C CG  . GLU B 101 ? 0.8952 0.7383 0.6056 -0.0645 0.0605  0.0014  103 GLU B CG  
2434 C CD  . GLU B 101 ? 0.9592 0.8206 0.6800 -0.0561 0.0623  0.0048  103 GLU B CD  
2435 O OE1 . GLU B 101 ? 0.9973 0.8611 0.7142 -0.0539 0.0638  0.0035  103 GLU B OE1 
2436 O OE2 . GLU B 101 ? 0.9172 0.7897 0.6492 -0.0518 0.0624  0.0088  103 GLU B OE2 
2437 N N   . ASP B 102 ? 0.7358 0.5732 0.4703 -0.0580 0.0583  0.0102  104 ASP B N   
2438 C CA  . ASP B 102 ? 0.6995 0.5357 0.4355 -0.0610 0.0565  0.0120  104 ASP B CA  
2439 C C   . ASP B 102 ? 0.6902 0.5034 0.4190 -0.0606 0.0562  0.0111  104 ASP B C   
2440 O O   . ASP B 102 ? 0.6691 0.4710 0.3983 -0.0535 0.0579  0.0100  104 ASP B O   
2441 C CB  . ASP B 102 ? 0.6785 0.5279 0.4285 -0.0537 0.0573  0.0147  104 ASP B CB  
2442 C CG  . ASP B 102 ? 0.7092 0.5622 0.4612 -0.0571 0.0555  0.0164  104 ASP B CG  
2443 O OD1 . ASP B 102 ? 0.7119 0.5506 0.4607 -0.0568 0.0548  0.0166  104 ASP B OD1 
2444 O OD2 . ASP B 102 ? 0.7049 0.5754 0.4611 -0.0597 0.0549  0.0178  104 ASP B OD2 
2445 N N   . GLU B 103 ? 0.7146 0.5214 0.4366 -0.0681 0.0543  0.0120  105 GLU B N   
2446 C CA  . GLU B 103 ? 0.7376 0.5218 0.4512 -0.0679 0.0538  0.0121  105 GLU B CA  
2447 C C   . GLU B 103 ? 0.7154 0.4956 0.4381 -0.0560 0.0548  0.0133  105 GLU B C   
2448 O O   . GLU B 103 ? 0.7299 0.4925 0.4475 -0.0511 0.0555  0.0124  105 GLU B O   
2449 C CB  . GLU B 103 ? 0.8065 0.5896 0.5143 -0.0771 0.0518  0.0144  105 GLU B CB  
2450 C CG  . GLU B 103 ? 0.9664 0.7257 0.6636 -0.0779 0.0512  0.0155  105 GLU B CG  
2451 C CD  . GLU B 103 ? 1.0987 0.8394 0.7793 -0.0876 0.0513  0.0133  105 GLU B CD  
2452 O OE1 . GLU B 103 ? 1.0950 0.8329 0.7717 -0.0883 0.0525  0.0095  105 GLU B OE1 
2453 O OE2 . GLU B 103 ? 1.1618 0.8903 0.8325 -0.0950 0.0504  0.0153  105 GLU B OE2 
2454 N N   . LYS B 104 ? 0.6765 0.4735 0.4123 -0.0514 0.0549  0.0151  106 LYS B N   
2455 C CA  . LYS B 104 ? 0.6520 0.4487 0.3975 -0.0416 0.0557  0.0158  106 LYS B CA  
2456 C C   . LYS B 104 ? 0.6159 0.4135 0.3677 -0.0336 0.0584  0.0140  106 LYS B C   
2457 O O   . LYS B 104 ? 0.6078 0.4035 0.3664 -0.0262 0.0592  0.0141  106 LYS B O   
2458 C CB  . LYS B 104 ? 0.6575 0.4703 0.4137 -0.0406 0.0549  0.0176  106 LYS B CB  
2459 C CG  . LYS B 104 ? 0.7349 0.5472 0.4858 -0.0470 0.0524  0.0197  106 LYS B CG  
2460 C CD  . LYS B 104 ? 0.7813 0.5780 0.5268 -0.0444 0.0512  0.0210  106 LYS B CD  
2461 C CE  . LYS B 104 ? 0.8504 0.6469 0.5898 -0.0512 0.0489  0.0238  106 LYS B CE  
2462 N NZ  . LYS B 104 ? 0.8868 0.6956 0.6357 -0.0472 0.0481  0.0249  106 LYS B NZ  
2463 N N   . ASN B 105 ? 0.6088 0.4102 0.3584 -0.0354 0.0598  0.0126  107 ASN B N   
2464 C CA  . ASN B 105 ? 0.5997 0.4024 0.3540 -0.0285 0.0628  0.0113  107 ASN B CA  
2465 C C   . ASN B 105 ? 0.6168 0.4049 0.3603 -0.0285 0.0639  0.0085  107 ASN B C   
2466 O O   . ASN B 105 ? 0.6014 0.3870 0.3483 -0.0215 0.0664  0.0074  107 ASN B O   
2467 C CB  . ASN B 105 ? 0.5836 0.4034 0.3444 -0.0287 0.0641  0.0121  107 ASN B CB  
2468 C CG  . ASN B 105 ? 0.5822 0.4156 0.3544 -0.0267 0.0639  0.0144  107 ASN B CG  
2469 O OD1 . ASN B 105 ? 0.5526 0.3844 0.3317 -0.0224 0.0641  0.0147  107 ASN B OD1 
2470 N ND2 . ASN B 105 ? 0.5891 0.4364 0.3633 -0.0297 0.0637  0.0157  107 ASN B ND2 
2471 N N   . LYS B 106 ? 0.6576 0.4364 0.3882 -0.0366 0.0623  0.0071  108 LYS B N   
2472 C CA  . LYS B 106 ? 0.7007 0.4665 0.4199 -0.0377 0.0636  0.0035  108 LYS B CA  
2473 C C   . LYS B 106 ? 0.7041 0.4533 0.4209 -0.0294 0.0653  0.0020  108 LYS B C   
2474 O O   . LYS B 106 ? 0.7173 0.4617 0.4305 -0.0259 0.0678  -0.0008 108 LYS B O   
2475 C CB  . LYS B 106 ? 0.7632 0.5206 0.4681 -0.0492 0.0616  0.0017  108 LYS B CB  
2476 C CG  . LYS B 106 ? 0.8636 0.6055 0.5611 -0.0531 0.0598  0.0029  108 LYS B CG  
2477 C CD  . LYS B 106 ? 0.9724 0.7100 0.6573 -0.0666 0.0581  0.0014  108 LYS B CD  
2478 C CE  . LYS B 106 ? 1.0687 0.7838 0.7418 -0.0708 0.0572  0.0021  108 LYS B CE  
2479 N NZ  . LYS B 106 ? 1.1437 0.8521 0.8030 -0.0850 0.0562  -0.0001 108 LYS B NZ  
2480 N N   . ARG B 107 ? 0.6911 0.4329 0.4099 -0.0258 0.0642  0.0040  109 ARG B N   
2481 C CA  . ARG B 107 ? 0.7071 0.4358 0.4252 -0.0164 0.0657  0.0031  109 ARG B CA  
2482 C C   . ARG B 107 ? 0.6675 0.4089 0.4009 -0.0069 0.0674  0.0043  109 ARG B C   
2483 O O   . ARG B 107 ? 0.6689 0.4034 0.4038 0.0013  0.0683  0.0040  109 ARG B O   
2484 C CB  . ARG B 107 ? 0.7453 0.4573 0.4551 -0.0171 0.0636  0.0048  109 ARG B CB  
2485 C CG  . ARG B 107 ? 0.9046 0.5999 0.5974 -0.0275 0.0624  0.0037  109 ARG B CG  
2486 C CD  . ARG B 107 ? 1.0522 0.7370 0.7344 -0.0293 0.0646  -0.0012 109 ARG B CD  
2487 N NE  . ARG B 107 ? 1.1885 0.8472 0.8527 -0.0340 0.0646  -0.0032 109 ARG B NE  
2488 C CZ  . ARG B 107 ? 1.2671 0.9144 0.9189 -0.0392 0.0661  -0.0081 109 ARG B CZ  
2489 N NH1 . ARG B 107 ? 1.2885 0.9098 0.9234 -0.0436 0.0663  -0.0100 109 ARG B NH1 
2490 N NH2 . ARG B 107 ? 1.2679 0.9291 0.9232 -0.0400 0.0674  -0.0111 109 ARG B NH2 
2491 N N   . GLY B 108 ? 0.6472 0.4070 0.3915 -0.0080 0.0679  0.0055  110 GLY B N   
2492 C CA  . GLY B 108 ? 0.6340 0.4059 0.3929 -0.0012 0.0694  0.0067  110 GLY B CA  
2493 C C   . GLY B 108 ? 0.6003 0.3796 0.3645 0.0028  0.0731  0.0056  110 GLY B C   
2494 O O   . GLY B 108 ? 0.6040 0.3766 0.3599 0.0028  0.0748  0.0033  110 GLY B O   
2495 N N   . GLY B 109 ? 0.5622 0.3547 0.3396 0.0058  0.0745  0.0070  111 GLY B N   
2496 C CA  . GLY B 109 ? 0.5363 0.3371 0.3208 0.0097  0.0786  0.0069  111 GLY B CA  
2497 C C   . GLY B 109 ? 0.5285 0.3424 0.3267 0.0107  0.0796  0.0089  111 GLY B C   
2498 O O   . GLY B 109 ? 0.4898 0.3078 0.2914 0.0076  0.0771  0.0101  111 GLY B O   
2499 N N   . ARG B 110 ? 0.5163 0.3366 0.3223 0.0146  0.0836  0.0090  112 ARG B N   
2500 C CA  . ARG B 110 ? 0.5073 0.3383 0.3251 0.0148  0.0856  0.0108  112 ARG B CA  
2501 C C   . ARG B 110 ? 0.5022 0.3373 0.3293 0.0195  0.0894  0.0101  112 ARG B C   
2502 O O   . ARG B 110 ? 0.5279 0.3607 0.3520 0.0226  0.0921  0.0093  112 ARG B O   
2503 C CB  . ARG B 110 ? 0.5092 0.3456 0.3257 0.0122  0.0872  0.0130  112 ARG B CB  
2504 C CG  . ARG B 110 ? 0.5613 0.3974 0.3734 0.0143  0.0907  0.0134  112 ARG B CG  
2505 C CD  . ARG B 110 ? 0.6029 0.4452 0.4125 0.0124  0.0917  0.0162  112 ARG B CD  
2506 N NE  . ARG B 110 ? 0.6243 0.4673 0.4297 0.0148  0.0954  0.0167  112 ARG B NE  
2507 C CZ  . ARG B 110 ? 0.6396 0.4889 0.4434 0.0150  0.0974  0.0199  112 ARG B CZ  
2508 N NH1 . ARG B 110 ? 0.6728 0.5228 0.4721 0.0172  0.1007  0.0203  112 ARG B NH1 
2509 N NH2 . ARG B 110 ? 0.5870 0.4425 0.3935 0.0136  0.0964  0.0228  112 ARG B NH2 
2510 N N   . TRP B 111 ? 0.5005 0.3422 0.3385 0.0195  0.0897  0.0101  113 TRP B N   
2511 C CA  . TRP B 111 ? 0.5037 0.3525 0.3527 0.0217  0.0940  0.0099  113 TRP B CA  
2512 C C   . TRP B 111 ? 0.5226 0.3747 0.3741 0.0199  0.0978  0.0124  113 TRP B C   
2513 O O   . TRP B 111 ? 0.4996 0.3532 0.3528 0.0171  0.0969  0.0137  113 TRP B O   
2514 C CB  . TRP B 111 ? 0.4993 0.3540 0.3583 0.0212  0.0925  0.0084  113 TRP B CB  
2515 C CG  . TRP B 111 ? 0.5316 0.3857 0.3905 0.0248  0.0899  0.0065  113 TRP B CG  
2516 C CD1 . TRP B 111 ? 0.5508 0.4022 0.4064 0.0248  0.0851  0.0060  113 TRP B CD1 
2517 C CD2 . TRP B 111 ? 0.5446 0.4013 0.4064 0.0299  0.0922  0.0052  113 TRP B CD2 
2518 N NE1 . TRP B 111 ? 0.5620 0.4132 0.4178 0.0300  0.0841  0.0048  113 TRP B NE1 
2519 C CE2 . TRP B 111 ? 0.5511 0.4061 0.4110 0.0334  0.0884  0.0040  113 TRP B CE2 
2520 C CE3 . TRP B 111 ? 0.5498 0.4108 0.4155 0.0320  0.0974  0.0051  113 TRP B CE3 
2521 C CZ2 . TRP B 111 ? 0.5599 0.4180 0.4222 0.0398  0.0895  0.0027  113 TRP B CZ2 
2522 C CZ3 . TRP B 111 ? 0.5566 0.4212 0.4247 0.0376  0.0986  0.0034  113 TRP B CZ3 
2523 C CH2 . TRP B 111 ? 0.5642 0.4273 0.4306 0.0418  0.0946  0.0022  113 TRP B CH2 
2524 N N   . LEU B 112 ? 0.5246 0.3777 0.3759 0.0220  0.1024  0.0135  114 LEU B N   
2525 C CA  . LEU B 112 ? 0.5544 0.4091 0.4051 0.0211  0.1061  0.0169  114 LEU B CA  
2526 C C   . LEU B 112 ? 0.5617 0.4209 0.4225 0.0213  0.1116  0.0178  114 LEU B C   
2527 O O   . LEU B 112 ? 0.5768 0.4388 0.4415 0.0232  0.1140  0.0163  114 LEU B O   
2528 C CB  . LEU B 112 ? 0.5815 0.4336 0.4216 0.0227  0.1070  0.0178  114 LEU B CB  
2529 C CG  . LEU B 112 ? 0.6028 0.4575 0.4409 0.0230  0.1112  0.0220  114 LEU B CG  
2530 C CD1 . LEU B 112 ? 0.6048 0.4606 0.4407 0.0211  0.1092  0.0247  114 LEU B CD1 
2531 C CD2 . LEU B 112 ? 0.6386 0.4920 0.4663 0.0247  0.1122  0.0218  114 LEU B CD2 
2532 N N   . ILE B 113 ? 0.5573 0.4169 0.4218 0.0195  0.1137  0.0204  115 ILE B N   
2533 C CA  . ILE B 113 ? 0.5770 0.4382 0.4495 0.0185  0.1196  0.0221  115 ILE B CA  
2534 C C   . ILE B 113 ? 0.5820 0.4410 0.4482 0.0200  0.1232  0.0272  115 ILE B C   
2535 O O   . ILE B 113 ? 0.5465 0.4038 0.4077 0.0203  0.1213  0.0295  115 ILE B O   
2536 C CB  . ILE B 113 ? 0.6076 0.4686 0.4881 0.0154  0.1195  0.0209  115 ILE B CB  
2537 C CG1 . ILE B 113 ? 0.6289 0.4924 0.5126 0.0141  0.1141  0.0164  115 ILE B CG1 
2538 C CG2 . ILE B 113 ? 0.6335 0.4953 0.5229 0.0130  0.1257  0.0215  115 ILE B CG2 
2539 C CD1 . ILE B 113 ? 0.6419 0.5110 0.5310 0.0148  0.1137  0.0131  115 ILE B CD1 
2540 N N   . THR B 114 ? 0.6316 0.4920 0.4980 0.0211  0.1282  0.0291  116 THR B N   
2541 C CA  . THR B 114 ? 0.6842 0.5432 0.5447 0.0228  0.1322  0.0346  116 THR B CA  
2542 C C   . THR B 114 ? 0.7012 0.5581 0.5691 0.0210  0.1384  0.0375  116 THR B C   
2543 O O   . THR B 114 ? 0.6928 0.5522 0.5685 0.0187  0.1415  0.0354  116 THR B O   
2544 C CB  . THR B 114 ? 0.7541 0.6159 0.6080 0.0252  0.1338  0.0349  116 THR B CB  
2545 O OG1 . THR B 114 ? 0.8039 0.6693 0.6648 0.0248  0.1365  0.0320  116 THR B OG1 
2546 C CG2 . THR B 114 ? 0.7680 0.6294 0.6125 0.0264  0.1280  0.0321  116 THR B CG2 
2547 N N   . LEU B 115 ? 0.7139 0.5662 0.5790 0.0220  0.1404  0.0423  117 LEU B N   
2548 C CA  . LEU B 115 ? 0.7540 0.6005 0.6243 0.0203  0.1464  0.0455  117 LEU B CA  
2549 C C   . LEU B 115 ? 0.8159 0.6604 0.6788 0.0236  0.1512  0.0528  117 LEU B C   
2550 O O   . LEU B 115 ? 0.8357 0.6793 0.6914 0.0275  0.1496  0.0568  117 LEU B O   
2551 C CB  . LEU B 115 ? 0.7500 0.5911 0.6225 0.0199  0.1447  0.0451  117 LEU B CB  
2552 C CG  . LEU B 115 ? 0.7712 0.6146 0.6501 0.0168  0.1397  0.0383  117 LEU B CG  
2553 C CD1 . LEU B 115 ? 0.7893 0.6273 0.6693 0.0168  0.1390  0.0382  117 LEU B CD1 
2554 C CD2 . LEU B 115 ? 0.7745 0.6202 0.6632 0.0120  0.1420  0.0340  117 LEU B CD2 
2555 N N   . ASN B 116 ? 0.8397 0.6850 0.7045 0.0222  0.1570  0.0546  118 ASN B N   
2556 C CA  . ASN B 116 ? 0.8926 0.7364 0.7499 0.0253  0.1620  0.0620  118 ASN B CA  
2557 C C   . ASN B 116 ? 0.9342 0.7671 0.7927 0.0251  0.1673  0.0675  118 ASN B C   
2558 O O   . ASN B 116 ? 0.9502 0.7779 0.8172 0.0202  0.1703  0.0652  118 ASN B O   
2559 C CB  . ASN B 116 ? 0.9197 0.7695 0.7771 0.0243  0.1660  0.0618  118 ASN B CB  
2560 C CG  . ASN B 116 ? 0.9918 0.8500 0.8452 0.0262  0.1605  0.0567  118 ASN B CG  
2561 O OD1 . ASN B 116 ? 1.0181 0.8776 0.8631 0.0293  0.1555  0.0567  118 ASN B OD1 
2562 N ND2 . ASN B 116 ? 1.0052 0.8690 0.8641 0.0244  0.1614  0.0521  118 ASN B ND2 
2563 N N   . LYS B 117 ? 0.9503 0.7802 0.8000 0.0306  0.1681  0.0745  119 LYS B N   
2564 C CA  . LYS B 117 ? 0.9811 0.7998 0.8283 0.0331  0.1735  0.0818  119 LYS B CA  
2565 C C   . LYS B 117 ? 1.0242 0.8304 0.8799 0.0282  0.1780  0.0801  119 LYS B C   
2566 O O   . LYS B 117 ? 1.0342 0.8335 0.8904 0.0301  0.1764  0.0796  119 LYS B O   
2567 C CB  . LYS B 117 ? 0.9875 0.8055 0.8271 0.0358  0.1798  0.0902  119 LYS B CB  
2568 C CG  . LYS B 117 ? 1.0433 0.8686 0.8846 0.0319  0.1826  0.0884  119 LYS B CG  
2569 C CD  . LYS B 117 ? 1.0931 0.9185 0.9255 0.0351  0.1887  0.0974  119 LYS B CD  
2570 C CE  . LYS B 117 ? 1.1334 0.9717 0.9573 0.0386  0.1853  0.0971  119 LYS B CE  
2571 N NZ  . LYS B 117 ? 1.1543 0.9984 0.9728 0.0429  0.1771  0.0949  119 LYS B NZ  
2572 N N   . GLN B 118 ? 1.0380 0.8417 0.9000 0.0216  0.1837  0.0789  120 GLN B N   
2573 C CA  . GLN B 118 ? 1.0537 0.8459 0.9235 0.0154  0.1882  0.0766  120 GLN B CA  
2574 C C   . GLN B 118 ? 1.0546 0.8481 0.9307 0.0135  0.1819  0.0683  120 GLN B C   
2575 O O   . GLN B 118 ? 1.0672 0.8494 0.9445 0.0131  0.1832  0.0676  120 GLN B O   
2576 C CB  . GLN B 118 ? 1.0798 0.8751 0.9571 0.0071  0.1935  0.0743  120 GLN B CB  
2577 C CG  . GLN B 118 ? 1.1422 0.9418 1.0145 0.0080  0.1988  0.0806  120 GLN B CG  
2578 C CD  . GLN B 118 ? 1.2022 1.0188 1.0782 0.0066  0.1961  0.0758  120 GLN B CD  
2579 O OE1 . GLN B 118 ? 1.2188 1.0402 1.0978 0.0024  0.2017  0.0767  120 GLN B OE1 
2580 N NE2 . GLN B 118 ? 1.2138 1.0397 1.0893 0.0101  0.1880  0.0705  120 GLN B NE2 
2581 N N   . GLN B 119 ? 1.0382 0.8452 0.9173 0.0129  0.1752  0.0621  121 GLN B N   
2582 C CA  . GLN B 119 ? 1.0303 0.8413 0.9149 0.0111  0.1686  0.0544  121 GLN B CA  
2583 C C   . GLN B 119 ? 1.0415 0.8498 0.9207 0.0168  0.1639  0.0553  121 GLN B C   
2584 O O   . GLN B 119 ? 1.0436 0.8539 0.9268 0.0152  0.1592  0.0494  121 GLN B O   
2585 C CB  . GLN B 119 ? 1.0294 0.8542 0.9171 0.0099  0.1634  0.0490  121 GLN B CB  
2586 C CG  . GLN B 119 ? 1.0653 0.8956 0.9625 0.0035  0.1663  0.0448  121 GLN B CG  
2587 C CD  . GLN B 119 ? 1.1450 0.9872 1.0420 0.0047  0.1650  0.0436  121 GLN B CD  
2588 O OE1 . GLN B 119 ? 1.1737 1.0191 1.0726 0.0027  0.1706  0.0456  121 GLN B OE1 
2589 N NE2 . GLN B 119 ? 1.1535 1.0023 1.0479 0.0080  0.1581  0.0401  121 GLN B NE2 
2590 N N   . ARG B 120 ? 1.0455 0.8507 0.9158 0.0234  0.1651  0.0625  122 ARG B N   
2591 C CA  . ARG B 120 ? 1.0470 0.8501 0.9130 0.0289  0.1618  0.0638  122 ARG B CA  
2592 C C   . ARG B 120 ? 1.0356 0.8249 0.9052 0.0278  0.1659  0.0631  122 ARG B C   
2593 O O   . ARG B 120 ? 1.0306 0.8196 0.9026 0.0279  0.1624  0.0584  122 ARG B O   
2594 C CB  . ARG B 120 ? 1.0794 0.8843 0.9354 0.0366  0.1626  0.0723  122 ARG B CB  
2595 C CG  . ARG B 120 ? 1.1404 0.9458 0.9921 0.0433  0.1594  0.0743  122 ARG B CG  
2596 C CD  . ARG B 120 ? 1.1981 1.0160 1.0414 0.0486  0.1554  0.0784  122 ARG B CD  
2597 N NE  . ARG B 120 ? 1.2392 1.0591 1.0776 0.0562  0.1539  0.0828  122 ARG B NE  
2598 C CZ  . ARG B 120 ? 1.2512 1.0839 1.0826 0.0609  0.1498  0.0861  122 ARG B CZ  
2599 N NH1 . ARG B 120 ? 1.2367 1.0729 1.0647 0.0682  0.1487  0.0900  122 ARG B NH1 
2600 N NH2 . ARG B 120 ? 1.2449 1.0876 1.0727 0.0583  0.1468  0.0850  122 ARG B NH2 
2601 N N   . ARG B 121 ? 1.0256 0.8027 0.8948 0.0264  0.1738  0.0676  123 ARG B N   
2602 C CA  . ARG B 121 ? 1.0207 0.7813 0.8915 0.0254  0.1789  0.0673  123 ARG B CA  
2603 C C   . ARG B 121 ? 0.9820 0.7429 0.8626 0.0163  0.1776  0.0576  123 ARG B C   
2604 O O   . ARG B 121 ? 0.9915 0.7477 0.8742 0.0160  0.1760  0.0528  123 ARG B O   
2605 C CB  . ARG B 121 ? 1.0634 0.8096 0.9303 0.0252  0.1881  0.0750  123 ARG B CB  
2606 C CG  . ARG B 121 ? 1.1420 0.8901 0.9988 0.0340  0.1895  0.0853  123 ARG B CG  
2607 C CD  . ARG B 121 ? 1.2052 0.9567 1.0556 0.0442  0.1850  0.0884  123 ARG B CD  
2608 N NE  . ARG B 121 ? 1.2630 1.0127 1.1036 0.0527  0.1882  0.0993  123 ARG B NE  
2609 C CZ  . ARG B 121 ? 1.2804 1.0431 1.1158 0.0553  0.1861  0.1035  123 ARG B CZ  
2610 N NH1 . ARG B 121 ? 1.2689 1.0463 1.1078 0.0503  0.1810  0.0976  123 ARG B NH1 
2611 N NH2 . ARG B 121 ? 1.2809 1.0419 1.1070 0.0633  0.1892  0.1135  123 ARG B NH2 
2612 N N   . SER B 122 ? 0.9459 0.7139 0.8323 0.0094  0.1782  0.0546  124 SER B N   
2613 C CA  . SER B 122 ? 0.9192 0.6895 0.8154 0.0004  0.1777  0.0459  124 SER B CA  
2614 C C   . SER B 122 ? 0.8881 0.6714 0.7879 0.0005  0.1688  0.0387  124 SER B C   
2615 O O   . SER B 122 ? 0.8877 0.6679 0.7914 -0.0027 0.1675  0.0326  124 SER B O   
2616 C CB  . SER B 122 ? 0.9206 0.6967 0.8220 -0.0063 0.1814  0.0457  124 SER B CB  
2617 O OG  . SER B 122 ? 0.9587 0.7481 0.8575 -0.0024 0.1781  0.0482  124 SER B OG  
2618 N N   . ASP B 123 ? 0.8552 0.6517 0.7527 0.0041  0.1632  0.0393  125 ASP B N   
2619 C CA  . ASP B 123 ? 0.8257 0.6345 0.7272 0.0025  0.1557  0.0326  125 ASP B CA  
2620 C C   . ASP B 123 ? 0.7751 0.5886 0.6710 0.0081  0.1489  0.0326  125 ASP B C   
2621 O O   . ASP B 123 ? 0.7500 0.5710 0.6491 0.0062  0.1433  0.0269  125 ASP B O   
2622 C CB  . ASP B 123 ? 0.8651 0.6854 0.7691 0.0009  0.1545  0.0319  125 ASP B CB  
2623 C CG  . ASP B 123 ? 0.9511 0.7725 0.8631 -0.0061 0.1597  0.0298  125 ASP B CG  
2624 O OD1 . ASP B 123 ? 0.9661 0.7813 0.8835 -0.0117 0.1627  0.0265  125 ASP B OD1 
2625 O OD2 . ASP B 123 ? 0.9853 0.8146 0.8982 -0.0062 0.1609  0.0311  125 ASP B OD2 
2626 N N   . LEU B 124 ? 0.7366 0.5473 0.6243 0.0147  0.1493  0.0388  126 LEU B N   
2627 C CA  . LEU B 124 ? 0.6982 0.5166 0.5808 0.0191  0.1427  0.0388  126 LEU B CA  
2628 C C   . LEU B 124 ? 0.6350 0.4533 0.5204 0.0181  0.1392  0.0336  126 LEU B C   
2629 O O   . LEU B 124 ? 0.5844 0.4114 0.4704 0.0167  0.1331  0.0295  126 LEU B O   
2630 C CB  . LEU B 124 ? 0.7081 0.5255 0.5821 0.0261  0.1439  0.0463  126 LEU B CB  
2631 C CG  . LEU B 124 ? 0.7324 0.5593 0.6012 0.0299  0.1374  0.0464  126 LEU B CG  
2632 C CD1 . LEU B 124 ? 0.7267 0.5632 0.5928 0.0281  0.1325  0.0448  126 LEU B CD1 
2633 C CD2 . LEU B 124 ? 0.7551 0.5811 0.6168 0.0374  0.1392  0.0535  126 LEU B CD2 
2634 N N   . ASN B 125 ? 0.6143 0.4225 0.5004 0.0191  0.1433  0.0338  127 ASN B N   
2635 C CA  . ASN B 125 ? 0.6247 0.4327 0.5125 0.0189  0.1406  0.0288  127 ASN B CA  
2636 C C   . ASN B 125 ? 0.5694 0.3825 0.4642 0.0118  0.1373  0.0208  127 ASN B C   
2637 O O   . ASN B 125 ? 0.5625 0.3835 0.4572 0.0117  0.1316  0.0171  127 ASN B O   
2638 C CB  . ASN B 125 ? 0.6972 0.4910 0.5839 0.0216  0.1466  0.0302  127 ASN B CB  
2639 C CG  . ASN B 125 ? 0.8212 0.6106 0.7004 0.0304  0.1495  0.0386  127 ASN B CG  
2640 O OD1 . ASN B 125 ? 0.8910 0.6676 0.7682 0.0341  0.1547  0.0408  127 ASN B OD1 
2641 N ND2 . ASN B 125 ? 0.8344 0.6340 0.7087 0.0344  0.1463  0.0436  127 ASN B ND2 
2642 N N   . ARG B 126 ? 0.5378 0.3482 0.4386 0.0060  0.1408  0.0185  128 ARG B N   
2643 C CA  . ARG B 126 ? 0.5428 0.3597 0.4509 -0.0006 0.1379  0.0109  128 ARG B CA  
2644 C C   . ARG B 126 ? 0.4975 0.3278 0.4051 0.0000  0.1311  0.0102  128 ARG B C   
2645 O O   . ARG B 126 ? 0.5027 0.3400 0.4119 -0.0016 0.1258  0.0054  128 ARG B O   
2646 C CB  . ARG B 126 ? 0.5876 0.4008 0.5026 -0.0074 0.1435  0.0090  128 ARG B CB  
2647 C CG  . ARG B 126 ? 0.6849 0.5089 0.6079 -0.0140 0.1398  0.0014  128 ARG B CG  
2648 C CD  . ARG B 126 ? 0.8242 0.6454 0.7547 -0.0220 0.1455  -0.0019 128 ARG B CD  
2649 N NE  . ARG B 126 ? 0.9407 0.7713 0.8759 -0.0243 0.1465  -0.0006 128 ARG B NE  
2650 C CZ  . ARG B 126 ? 1.0116 0.8382 0.9448 -0.0230 0.1516  0.0053  128 ARG B CZ  
2651 N NH1 . ARG B 126 ? 1.0475 0.8604 0.9738 -0.0192 0.1561  0.0114  128 ARG B NH1 
2652 N NH2 . ARG B 126 ? 0.9899 0.8271 0.9278 -0.0251 0.1522  0.0055  128 ARG B NH2 
2653 N N   . PHE B 127 ? 0.4675 0.3006 0.3720 0.0025  0.1314  0.0148  129 PHE B N   
2654 C CA  . PHE B 127 ? 0.4858 0.3287 0.3885 0.0035  0.1257  0.0142  129 PHE B CA  
2655 C C   . PHE B 127 ? 0.4684 0.3145 0.3649 0.0066  0.1200  0.0145  129 PHE B C   
2656 O O   . PHE B 127 ? 0.4611 0.3137 0.3579 0.0054  0.1147  0.0114  129 PHE B O   
2657 C CB  . PHE B 127 ? 0.5248 0.3690 0.4246 0.0056  0.1278  0.0185  129 PHE B CB  
2658 C CG  . PHE B 127 ? 0.5797 0.4259 0.4861 0.0021  0.1319  0.0173  129 PHE B CG  
2659 C CD1 . PHE B 127 ? 0.6177 0.4631 0.5325 -0.0034 0.1347  0.0133  129 PHE B CD1 
2660 C CD2 . PHE B 127 ? 0.6348 0.4849 0.5392 0.0039  0.1329  0.0198  129 PHE B CD2 
2661 C CE1 . PHE B 127 ? 0.6579 0.5074 0.5795 -0.0074 0.1386  0.0121  129 PHE B CE1 
2662 C CE2 . PHE B 127 ? 0.6668 0.5209 0.5779 0.0008  0.1369  0.0187  129 PHE B CE2 
2663 C CZ  . PHE B 127 ? 0.6630 0.5171 0.5829 -0.0050 0.1398  0.0151  129 PHE B CZ  
2664 N N   . TRP B 128 ? 0.4634 0.3058 0.3544 0.0104  0.1210  0.0184  130 TRP B N   
2665 C CA  . TRP B 128 ? 0.4878 0.3353 0.3734 0.0126  0.1158  0.0185  130 TRP B CA  
2666 C C   . TRP B 128 ? 0.4724 0.3223 0.3615 0.0099  0.1128  0.0131  130 TRP B C   
2667 O O   . TRP B 128 ? 0.4626 0.3189 0.3497 0.0088  0.1074  0.0111  130 TRP B O   
2668 C CB  . TRP B 128 ? 0.4930 0.3385 0.3729 0.0178  0.1178  0.0238  130 TRP B CB  
2669 C CG  . TRP B 128 ? 0.5069 0.3598 0.3818 0.0196  0.1129  0.0241  130 TRP B CG  
2670 C CD1 . TRP B 128 ? 0.5431 0.3966 0.4167 0.0229  0.1134  0.0249  130 TRP B CD1 
2671 C CD2 . TRP B 128 ? 0.5057 0.3661 0.3756 0.0183  0.1073  0.0241  130 TRP B CD2 
2672 N NE1 . TRP B 128 ? 0.5619 0.4251 0.4310 0.0231  0.1082  0.0251  130 TRP B NE1 
2673 C CE2 . TRP B 128 ? 0.5439 0.4106 0.4103 0.0198  0.1045  0.0247  130 TRP B CE2 
2674 C CE3 . TRP B 128 ? 0.5164 0.3785 0.3844 0.0158  0.1046  0.0232  130 TRP B CE3 
2675 C CZ2 . TRP B 128 ? 0.5496 0.4242 0.4104 0.0180  0.0994  0.0249  130 TRP B CZ2 
2676 C CZ3 . TRP B 128 ? 0.5523 0.4198 0.4140 0.0146  0.0995  0.0232  130 TRP B CZ3 
2677 C CH2 . TRP B 128 ? 0.5489 0.4225 0.4071 0.0150  0.0970  0.0241  130 TRP B CH2 
2678 N N   . LEU B 129 ? 0.4745 0.3184 0.3683 0.0086  0.1167  0.0105  131 LEU B N   
2679 C CA  . LEU B 129 ? 0.4749 0.3213 0.3714 0.0059  0.1142  0.0047  131 LEU B CA  
2680 C C   . LEU B 129 ? 0.4564 0.3099 0.3572 0.0014  0.1102  0.0002  131 LEU B C   
2681 O O   . LEU B 129 ? 0.4687 0.3286 0.3684 0.0005  0.1053  -0.0026 131 LEU B O   
2682 C CB  . LEU B 129 ? 0.4777 0.3149 0.3780 0.0047  0.1195  0.0017  131 LEU B CB  
2683 C CG  . LEU B 129 ? 0.5216 0.3614 0.4247 0.0015  0.1174  -0.0052 131 LEU B CG  
2684 C CD1 . LEU B 129 ? 0.5372 0.3835 0.4353 0.0047  0.1131  -0.0051 131 LEU B CD1 
2685 C CD2 . LEU B 129 ? 0.5588 0.3870 0.4645 -0.0001 0.1235  -0.0084 131 LEU B CD2 
2686 N N   . GLU B 130 ? 0.4586 0.3120 0.3643 -0.0011 0.1123  -0.0004 132 GLU B N   
2687 C CA  . GLU B 130 ? 0.4725 0.3342 0.3826 -0.0043 0.1085  -0.0043 132 GLU B CA  
2688 C C   . GLU B 130 ? 0.4692 0.3366 0.3735 -0.0017 0.1026  -0.0023 132 GLU B C   
2689 O O   . GLU B 130 ? 0.4840 0.3577 0.3890 -0.0030 0.0979  -0.0053 132 GLU B O   
2690 C CB  . GLU B 130 ? 0.4938 0.3565 0.4104 -0.0068 0.1122  -0.0048 132 GLU B CB  
2691 C CG  . GLU B 130 ? 0.6266 0.4842 0.5496 -0.0115 0.1179  -0.0078 132 GLU B CG  
2692 C CD  . GLU B 130 ? 0.7399 0.6003 0.6668 -0.0159 0.1161  -0.0145 132 GLU B CD  
2693 O OE1 . GLU B 130 ? 0.7014 0.5721 0.6296 -0.0165 0.1105  -0.0176 132 GLU B OE1 
2694 O OE2 . GLU B 130 ? 0.8458 0.6976 0.7740 -0.0184 0.1206  -0.0167 132 GLU B OE2 
2695 N N   . THR B 131 ? 0.4626 0.3272 0.3607 0.0017  0.1030  0.0027  133 THR B N   
2696 C CA  . THR B 131 ? 0.4718 0.3391 0.3628 0.0034  0.0980  0.0046  133 THR B CA  
2697 C C   . THR B 131 ? 0.4697 0.3400 0.3568 0.0028  0.0937  0.0035  133 THR B C   
2698 O O   . THR B 131 ? 0.4470 0.3209 0.3321 0.0018  0.0890  0.0021  133 THR B O   
2699 C CB  . THR B 131 ? 0.4924 0.3563 0.3771 0.0064  0.0999  0.0097  133 THR B CB  
2700 O OG1 . THR B 131 ? 0.4867 0.3487 0.3748 0.0068  0.1039  0.0105  133 THR B OG1 
2701 C CG2 . THR B 131 ? 0.4918 0.3572 0.3684 0.0071  0.0951  0.0110  133 THR B CG2 
2702 N N   . LEU B 132 ? 0.4651 0.3339 0.3510 0.0038  0.0956  0.0043  134 LEU B N   
2703 C CA  . LEU B 132 ? 0.4865 0.3595 0.3691 0.0034  0.0924  0.0033  134 LEU B CA  
2704 C C   . LEU B 132 ? 0.4900 0.3670 0.3767 0.0003  0.0898  -0.0019 134 LEU B C   
2705 O O   . LEU B 132 ? 0.4817 0.3636 0.3645 -0.0009 0.0852  -0.0024 134 LEU B O   
2706 C CB  . LEU B 132 ? 0.5088 0.3799 0.3906 0.0062  0.0957  0.0047  134 LEU B CB  
2707 C CG  . LEU B 132 ? 0.5403 0.4096 0.4176 0.0100  0.0981  0.0104  134 LEU B CG  
2708 C CD1 . LEU B 132 ? 0.5151 0.3835 0.3918 0.0140  0.1013  0.0119  134 LEU B CD1 
2709 C CD2 . LEU B 132 ? 0.5986 0.4729 0.4689 0.0095  0.0938  0.0131  134 LEU B CD2 
2710 N N   . LEU B 133 ? 0.4718 0.3472 0.3657 -0.0015 0.0926  -0.0057 135 LEU B N   
2711 C CA  . LEU B 133 ? 0.4764 0.3574 0.3744 -0.0048 0.0901  -0.0110 135 LEU B CA  
2712 C C   . LEU B 133 ? 0.4716 0.3585 0.3690 -0.0054 0.0852  -0.0111 135 LEU B C   
2713 O O   . LEU B 133 ? 0.4716 0.3644 0.3677 -0.0068 0.0811  -0.0134 135 LEU B O   
2714 C CB  . LEU B 133 ? 0.4861 0.3647 0.3920 -0.0077 0.0944  -0.0155 135 LEU B CB  
2715 C CG  . LEU B 133 ? 0.4971 0.3674 0.4031 -0.0069 0.0997  -0.0162 135 LEU B CG  
2716 C CD1 . LEU B 133 ? 0.4901 0.3566 0.4030 -0.0111 0.1039  -0.0211 135 LEU B CD1 
2717 C CD2 . LEU B 133 ? 0.5258 0.3982 0.4275 -0.0055 0.0979  -0.0177 135 LEU B CD2 
2718 N N   . CYS B 134 ? 0.4647 0.3499 0.3621 -0.0038 0.0856  -0.0084 136 CYS B N   
2719 C CA  . CYS B 134 ? 0.4582 0.3467 0.3532 -0.0027 0.0813  -0.0075 136 CYS B CA  
2720 C C   . CYS B 134 ? 0.4503 0.3379 0.3361 -0.0020 0.0770  -0.0048 136 CYS B C   
2721 O O   . CYS B 134 ? 0.4638 0.3549 0.3473 -0.0021 0.0727  -0.0053 136 CYS B O   
2722 C CB  . CYS B 134 ? 0.4782 0.3638 0.3739 -0.0004 0.0835  -0.0051 136 CYS B CB  
2723 S SG  . CYS B 134 ? 0.5269 0.4167 0.4341 -0.0020 0.0878  -0.0082 136 CYS B SG  
2724 N N   . LEU B 135 ? 0.4495 0.3330 0.3296 -0.0015 0.0781  -0.0018 137 LEU B N   
2725 C CA  . LEU B 135 ? 0.4620 0.3454 0.3332 -0.0021 0.0743  0.0008  137 LEU B CA  
2726 C C   . LEU B 135 ? 0.4661 0.3554 0.3369 -0.0043 0.0718  -0.0015 137 LEU B C   
2727 O O   . LEU B 135 ? 0.4680 0.3594 0.3349 -0.0054 0.0677  -0.0014 137 LEU B O   
2728 C CB  . LEU B 135 ? 0.4597 0.3403 0.3259 -0.0014 0.0762  0.0042  137 LEU B CB  
2729 C CG  . LEU B 135 ? 0.4738 0.3490 0.3346 -0.0003 0.0763  0.0071  137 LEU B CG  
2730 C CD1 . LEU B 135 ? 0.4657 0.3382 0.3318 0.0019  0.0787  0.0062  137 LEU B CD1 
2731 C CD2 . LEU B 135 ? 0.5163 0.3917 0.3736 0.0003  0.0784  0.0099  137 LEU B CD2 
2732 N N   . ILE B 136 ? 0.4463 0.3377 0.3205 -0.0046 0.0745  -0.0034 138 ILE B N   
2733 C CA  . ILE B 136 ? 0.4536 0.3510 0.3261 -0.0063 0.0726  -0.0054 138 ILE B CA  
2734 C C   . ILE B 136 ? 0.4455 0.3479 0.3215 -0.0080 0.0701  -0.0095 138 ILE B C   
2735 O O   . ILE B 136 ? 0.4531 0.3608 0.3252 -0.0095 0.0668  -0.0101 138 ILE B O   
2736 C CB  . ILE B 136 ? 0.4716 0.3697 0.3460 -0.0051 0.0764  -0.0066 138 ILE B CB  
2737 C CG1 . ILE B 136 ? 0.4552 0.3505 0.3376 -0.0049 0.0803  -0.0112 138 ILE B CG1 
2738 C CG2 . ILE B 136 ? 0.4916 0.3872 0.3625 -0.0027 0.0784  -0.0021 138 ILE B CG2 
2739 C CD1 . ILE B 136 ? 0.4698 0.3635 0.3533 -0.0030 0.0844  -0.0128 138 ILE B CD1 
2740 N N   . GLY B 137 ? 0.4308 0.3327 0.3137 -0.0079 0.0716  -0.0121 139 GLY B N   
2741 C CA  . GLY B 137 ? 0.4538 0.3626 0.3409 -0.0095 0.0692  -0.0162 139 GLY B CA  
2742 C C   . GLY B 137 ? 0.4601 0.3712 0.3443 -0.0083 0.0647  -0.0139 139 GLY B C   
2743 O O   . GLY B 137 ? 0.4777 0.3964 0.3649 -0.0090 0.0622  -0.0168 139 GLY B O   
2744 N N   . GLU B 138 ? 0.4555 0.3602 0.3333 -0.0062 0.0637  -0.0089 140 GLU B N   
2745 C CA  . GLU B 138 ? 0.4740 0.3779 0.3473 -0.0041 0.0598  -0.0062 140 GLU B CA  
2746 C C   . GLU B 138 ? 0.4893 0.3980 0.3703 -0.0020 0.0599  -0.0084 140 GLU B C   
2747 O O   . GLU B 138 ? 0.4808 0.3959 0.3620 -0.0008 0.0563  -0.0090 140 GLU B O   
2748 C CB  . GLU B 138 ? 0.4857 0.3937 0.3525 -0.0055 0.0553  -0.0054 140 GLU B CB  
2749 C CG  . GLU B 138 ? 0.5247 0.4302 0.3841 -0.0081 0.0553  -0.0032 140 GLU B CG  
2750 C CD  . GLU B 138 ? 0.5898 0.4859 0.4404 -0.0081 0.0547  0.0017  140 GLU B CD  
2751 O OE1 . GLU B 138 ? 0.6570 0.5475 0.5026 -0.0062 0.0524  0.0043  140 GLU B OE1 
2752 O OE2 . GLU B 138 ? 0.6122 0.5066 0.4602 -0.0099 0.0566  0.0029  140 GLU B OE2 
2753 N N   . SER B 139 ? 0.4872 0.3937 0.3744 -0.0015 0.0642  -0.0094 141 SER B N   
2754 C CA  . SER B 139 ? 0.5023 0.4154 0.3988 -0.0006 0.0655  -0.0121 141 SER B CA  
2755 C C   . SER B 139 ? 0.5225 0.4357 0.4176 0.0042  0.0636  -0.0097 141 SER B C   
2756 O O   . SER B 139 ? 0.5376 0.4589 0.4409 0.0053  0.0645  -0.0119 141 SER B O   
2757 C CB  . SER B 139 ? 0.5197 0.4294 0.4225 -0.0022 0.0714  -0.0133 141 SER B CB  
2758 O OG  . SER B 139 ? 0.5617 0.4698 0.4655 -0.0056 0.0737  -0.0156 141 SER B OG  
2759 N N   . PHE B 140 ? 0.5216 0.4264 0.4066 0.0070  0.0613  -0.0054 142 PHE B N   
2760 C CA  . PHE B 140 ? 0.5313 0.4332 0.4137 0.0125  0.0602  -0.0031 142 PHE B CA  
2761 C C   . PHE B 140 ? 0.5622 0.4655 0.4385 0.0155  0.0549  -0.0012 142 PHE B C   
2762 O O   . PHE B 140 ? 0.5723 0.4687 0.4423 0.0204  0.0536  0.0018  142 PHE B O   
2763 C CB  . PHE B 140 ? 0.5323 0.4211 0.4068 0.0134  0.0623  0.0000  142 PHE B CB  
2764 C CG  . PHE B 140 ? 0.5291 0.4162 0.4080 0.0110  0.0674  -0.0009 142 PHE B CG  
2765 C CD1 . PHE B 140 ? 0.5248 0.4173 0.4131 0.0119  0.0712  -0.0028 142 PHE B CD1 
2766 C CD2 . PHE B 140 ? 0.5294 0.4102 0.4028 0.0079  0.0685  0.0007  142 PHE B CD2 
2767 C CE1 . PHE B 140 ? 0.5352 0.4249 0.4263 0.0098  0.0761  -0.0028 142 PHE B CE1 
2768 C CE2 . PHE B 140 ? 0.5324 0.4116 0.4090 0.0068  0.0731  0.0007  142 PHE B CE2 
2769 C CZ  . PHE B 140 ? 0.5301 0.4128 0.4151 0.0078  0.0770  -0.0008 142 PHE B CZ  
2770 N N   . ASP B 141 ? 0.5895 0.5013 0.4671 0.0130  0.0520  -0.0028 143 ASP B N   
2771 C CA  . ASP B 141 ? 0.6233 0.5376 0.4949 0.0158  0.0469  -0.0005 143 ASP B CA  
2772 C C   . ASP B 141 ? 0.6310 0.5298 0.4883 0.0163  0.0454  0.0047  143 ASP B C   
2773 O O   . ASP B 141 ? 0.6343 0.5263 0.4876 0.0117  0.0471  0.0052  143 ASP B O   
2774 C CB  . ASP B 141 ? 0.6904 0.6141 0.5679 0.0223  0.0455  -0.0009 143 ASP B CB  
2775 C CG  . ASP B 141 ? 0.8264 0.7670 0.7175 0.0195  0.0467  -0.0065 143 ASP B CG  
2776 O OD1 . ASP B 141 ? 0.8425 0.7920 0.7357 0.0151  0.0449  -0.0094 143 ASP B OD1 
2777 O OD2 . ASP B 141 ? 0.8865 0.8317 0.7857 0.0212  0.0496  -0.0082 143 ASP B OD2 
2778 N N   . ASP B 142 ? 0.6432 0.5366 0.4928 0.0213  0.0423  0.0085  144 ASP B N   
2779 C CA  . ASP B 142 ? 0.6516 0.5290 0.4870 0.0207  0.0411  0.0133  144 ASP B CA  
2780 C C   . ASP B 142 ? 0.6119 0.4763 0.4438 0.0200  0.0447  0.0137  144 ASP B C   
2781 O O   . ASP B 142 ? 0.6129 0.4667 0.4353 0.0157  0.0447  0.0158  144 ASP B O   
2782 C CB  . ASP B 142 ? 0.7243 0.5968 0.5520 0.0274  0.0376  0.0174  144 ASP B CB  
2783 C CG  . ASP B 142 ? 0.8868 0.7699 0.7135 0.0273  0.0334  0.0186  144 ASP B CG  
2784 O OD1 . ASP B 142 ? 0.9128 0.8040 0.7419 0.0208  0.0331  0.0164  144 ASP B OD1 
2785 O OD2 . ASP B 142 ? 0.9596 0.8428 0.7824 0.0342  0.0304  0.0218  144 ASP B OD2 
2786 N N   . TYR B 143 ? 0.5794 0.4459 0.4189 0.0237  0.0477  0.0114  145 TYR B N   
2787 C CA  . TYR B 143 ? 0.5779 0.4342 0.4146 0.0230  0.0513  0.0113  145 TYR B CA  
2788 C C   . TYR B 143 ? 0.5409 0.3983 0.3792 0.0160  0.0536  0.0101  145 TYR B C   
2789 O O   . TYR B 143 ? 0.5430 0.3923 0.3771 0.0147  0.0561  0.0105  145 TYR B O   
2790 C CB  . TYR B 143 ? 0.6046 0.4655 0.4497 0.0284  0.0542  0.0093  145 TYR B CB  
2791 C CG  . TYR B 143 ? 0.6468 0.5067 0.4898 0.0368  0.0521  0.0108  145 TYR B CG  
2792 C CD1 . TYR B 143 ? 0.6785 0.5226 0.5079 0.0400  0.0502  0.0143  145 TYR B CD1 
2793 C CD2 . TYR B 143 ? 0.6788 0.5541 0.5331 0.0413  0.0520  0.0087  145 TYR B CD2 
2794 C CE1 . TYR B 143 ? 0.7201 0.5621 0.5469 0.0490  0.0486  0.0161  145 TYR B CE1 
2795 C CE2 . TYR B 143 ? 0.7098 0.5861 0.5625 0.0502  0.0500  0.0104  145 TYR B CE2 
2796 C CZ  . TYR B 143 ? 0.7495 0.6085 0.5882 0.0547  0.0484  0.0144  145 TYR B CZ  
2797 O OH  . TYR B 143 ? 0.8142 0.6727 0.6503 0.0647  0.0465  0.0165  145 TYR B OH  
2798 N N   . SER B 144 ? 0.5251 0.3924 0.3686 0.0120  0.0530  0.0084  146 SER B N   
2799 C CA  . SER B 144 ? 0.5296 0.3981 0.3736 0.0064  0.0549  0.0077  146 SER B CA  
2800 C C   . SER B 144 ? 0.5292 0.3880 0.3609 0.0027  0.0536  0.0109  146 SER B C   
2801 O O   . SER B 144 ? 0.5263 0.3840 0.3568 -0.0006 0.0557  0.0109  146 SER B O   
2802 C CB  . SER B 144 ? 0.5400 0.4203 0.3905 0.0036  0.0540  0.0051  146 SER B CB  
2803 O OG  . SER B 144 ? 0.5310 0.4185 0.3929 0.0042  0.0572  0.0015  146 SER B OG  
2804 N N   . ASP B 145 ? 0.5110 0.3630 0.3335 0.0033  0.0503  0.0136  147 ASP B N   
2805 C CA  . ASP B 145 ? 0.5377 0.3788 0.3476 -0.0010 0.0492  0.0166  147 ASP B CA  
2806 C C   . ASP B 145 ? 0.5465 0.3766 0.3513 -0.0008 0.0516  0.0168  147 ASP B C   
2807 O O   . ASP B 145 ? 0.5712 0.3962 0.3681 -0.0062 0.0516  0.0180  147 ASP B O   
2808 C CB  . ASP B 145 ? 0.5761 0.4098 0.3763 -0.0002 0.0457  0.0200  147 ASP B CB  
2809 C CG  . ASP B 145 ? 0.7144 0.5597 0.5174 -0.0019 0.0432  0.0201  147 ASP B CG  
2810 O OD1 . ASP B 145 ? 0.7056 0.5617 0.5143 -0.0060 0.0442  0.0179  147 ASP B OD1 
2811 O OD2 . ASP B 145 ? 0.7902 0.6340 0.5892 0.0012  0.0403  0.0224  147 ASP B OD2 
2812 N N   . ASP B 146 ? 0.5280 0.3560 0.3372 0.0050  0.0535  0.0154  148 ASP B N   
2813 C CA  . ASP B 146 ? 0.5334 0.3520 0.3377 0.0055  0.0561  0.0150  148 ASP B CA  
2814 C C   . ASP B 146 ? 0.5055 0.3312 0.3150 0.0022  0.0590  0.0136  148 ASP B C   
2815 O O   . ASP B 146 ? 0.5017 0.3212 0.3056 0.0009  0.0606  0.0136  148 ASP B O   
2816 C CB  . ASP B 146 ? 0.5579 0.3722 0.3644 0.0134  0.0575  0.0140  148 ASP B CB  
2817 C CG  . ASP B 146 ? 0.6550 0.4537 0.4495 0.0166  0.0556  0.0160  148 ASP B CG  
2818 O OD1 . ASP B 146 ? 0.6863 0.4827 0.4761 0.0157  0.0525  0.0183  148 ASP B OD1 
2819 O OD2 . ASP B 146 ? 0.6290 0.4165 0.4176 0.0201  0.0575  0.0152  148 ASP B OD2 
2820 N N   . VAL B 147 ? 0.4873 0.3257 0.3067 0.0010  0.0598  0.0125  149 VAL B N   
2821 C CA  . VAL B 147 ? 0.4873 0.3320 0.3122 -0.0005 0.0630  0.0118  149 VAL B CA  
2822 C C   . VAL B 147 ? 0.4767 0.3217 0.2944 -0.0061 0.0620  0.0133  149 VAL B C   
2823 O O   . VAL B 147 ? 0.4743 0.3215 0.2886 -0.0097 0.0593  0.0141  149 VAL B O   
2824 C CB  . VAL B 147 ? 0.5051 0.3607 0.3422 0.0007  0.0645  0.0098  149 VAL B CB  
2825 C CG1 . VAL B 147 ? 0.5139 0.3745 0.3551 -0.0007 0.0678  0.0098  149 VAL B CG1 
2826 C CG2 . VAL B 147 ? 0.5060 0.3630 0.3507 0.0055  0.0661  0.0081  149 VAL B CG2 
2827 N N   . CYS B 148 ? 0.4398 0.2839 0.2551 -0.0070 0.0641  0.0137  150 CYS B N   
2828 C CA  . CYS B 148 ? 0.4608 0.3089 0.2710 -0.0121 0.0635  0.0149  150 CYS B CA  
2829 C C   . CYS B 148 ? 0.4646 0.3240 0.2829 -0.0111 0.0659  0.0150  150 CYS B C   
2830 O O   . CYS B 148 ? 0.4793 0.3464 0.2974 -0.0141 0.0649  0.0156  150 CYS B O   
2831 C CB  . CYS B 148 ? 0.4731 0.3140 0.2741 -0.0140 0.0639  0.0152  150 CYS B CB  
2832 S SG  . CYS B 148 ? 0.5610 0.3850 0.3496 -0.0156 0.0614  0.0150  150 CYS B SG  
2833 N N   . GLY B 149 ? 0.4555 0.3156 0.2805 -0.0068 0.0693  0.0145  151 GLY B N   
2834 C CA  . GLY B 149 ? 0.4578 0.3254 0.2894 -0.0049 0.0723  0.0150  151 GLY B CA  
2835 C C   . GLY B 149 ? 0.4635 0.3290 0.3003 -0.0008 0.0764  0.0151  151 GLY B C   
2836 O O   . GLY B 149 ? 0.4821 0.3418 0.3187 0.0009  0.0769  0.0143  151 GLY B O   
2837 N N   . ALA B 150 ? 0.4532 0.3233 0.2942 0.0012  0.0796  0.0165  152 ALA B N   
2838 C CA  . ALA B 150 ? 0.4473 0.3155 0.2927 0.0047  0.0842  0.0175  152 ALA B CA  
2839 C C   . ALA B 150 ? 0.4663 0.3384 0.3086 0.0063  0.0862  0.0209  152 ALA B C   
2840 O O   . ALA B 150 ? 0.4793 0.3577 0.3197 0.0055  0.0847  0.0219  152 ALA B O   
2841 C CB  . ALA B 150 ? 0.4358 0.3040 0.2910 0.0062  0.0870  0.0158  152 ALA B CB  
2842 N N   . VAL B 151 ? 0.4648 0.3346 0.3066 0.0088  0.0895  0.0226  153 VAL B N   
2843 C CA  . VAL B 151 ? 0.4791 0.3530 0.3169 0.0110  0.0914  0.0264  153 VAL B CA  
2844 C C   . VAL B 151 ? 0.4909 0.3616 0.3341 0.0150  0.0971  0.0286  153 VAL B C   
2845 O O   . VAL B 151 ? 0.5049 0.3707 0.3513 0.0152  0.0992  0.0273  153 VAL B O   
2846 C CB  . VAL B 151 ? 0.4908 0.3651 0.3190 0.0092  0.0893  0.0267  153 VAL B CB  
2847 C CG1 . VAL B 151 ? 0.4865 0.3673 0.3107 0.0118  0.0912  0.0308  153 VAL B CG1 
2848 C CG2 . VAL B 151 ? 0.4990 0.3742 0.3210 0.0040  0.0841  0.0245  153 VAL B CG2 
2849 N N   . VAL B 152 ? 0.4932 0.3669 0.3371 0.0183  0.0996  0.0321  154 VAL B N   
2850 C CA  . VAL B 152 ? 0.5208 0.3907 0.3670 0.0222  0.1053  0.0357  154 VAL B CA  
2851 C C   . VAL B 152 ? 0.5408 0.4165 0.3798 0.0254  0.1058  0.0405  154 VAL B C   
2852 O O   . VAL B 152 ? 0.5381 0.4213 0.3742 0.0268  0.1038  0.0423  154 VAL B O   
2853 C CB  . VAL B 152 ? 0.5401 0.4056 0.3936 0.0242  0.1090  0.0359  154 VAL B CB  
2854 C CG1 . VAL B 152 ? 0.5400 0.4107 0.3928 0.0263  0.1074  0.0367  154 VAL B CG1 
2855 C CG2 . VAL B 152 ? 0.5540 0.4134 0.4092 0.0274  0.1155  0.0400  154 VAL B CG2 
2856 N N   . ASN B 153 ? 0.5404 0.4142 0.3764 0.0265  0.1085  0.0425  155 ASN B N   
2857 C CA  . ASN B 153 ? 0.5663 0.4457 0.3950 0.0298  0.1095  0.0474  155 ASN B CA  
2858 C C   . ASN B 153 ? 0.5904 0.4646 0.4218 0.0345  0.1160  0.0525  155 ASN B C   
2859 O O   . ASN B 153 ? 0.5751 0.4426 0.4098 0.0335  0.1197  0.0519  155 ASN B O   
2860 C CB  . ASN B 153 ? 0.5804 0.4608 0.4023 0.0274  0.1080  0.0457  155 ASN B CB  
2861 C CG  . ASN B 153 ? 0.5910 0.4721 0.4096 0.0222  0.1025  0.0403  155 ASN B CG  
2862 O OD1 . ASN B 153 ? 0.6149 0.4898 0.4346 0.0198  0.1019  0.0364  155 ASN B OD1 
2863 N ND2 . ASN B 153 ? 0.5741 0.4630 0.3885 0.0204  0.0984  0.0404  155 ASN B ND2 
2864 N N   . VAL B 154 ? 0.6161 0.4933 0.4462 0.0395  0.1176  0.0575  156 VAL B N   
2865 C CA  . VAL B 154 ? 0.6600 0.5303 0.4914 0.0445  0.1240  0.0631  156 VAL B CA  
2866 C C   . VAL B 154 ? 0.6964 0.5729 0.5195 0.0479  0.1251  0.0687  156 VAL B C   
2867 O O   . VAL B 154 ? 0.6970 0.5846 0.5145 0.0506  0.1218  0.0710  156 VAL B O   
2868 C CB  . VAL B 154 ? 0.6882 0.5572 0.5222 0.0492  0.1251  0.0655  156 VAL B CB  
2869 C CG1 . VAL B 154 ? 0.7120 0.5721 0.5454 0.0551  0.1321  0.0723  156 VAL B CG1 
2870 C CG2 . VAL B 154 ? 0.6969 0.5607 0.5385 0.0452  0.1238  0.0593  156 VAL B CG2 
2871 N N   . ARG B 155 ? 0.7285 0.5996 0.5508 0.0476  0.1295  0.0705  157 ARG B N   
2872 C CA  . ARG B 155 ? 0.7748 0.6520 0.5885 0.0506  0.1308  0.0755  157 ARG B CA  
2873 C C   . ARG B 155 ? 0.8199 0.6890 0.6333 0.0541  0.1383  0.0820  157 ARG B C   
2874 O O   . ARG B 155 ? 0.8089 0.6667 0.6293 0.0523  0.1428  0.0813  157 ARG B O   
2875 C CB  . ARG B 155 ? 0.7888 0.6697 0.5986 0.0459  0.1283  0.0706  157 ARG B CB  
2876 C CG  . ARG B 155 ? 0.8170 0.7047 0.6243 0.0418  0.1213  0.0647  157 ARG B CG  
2877 C CD  . ARG B 155 ? 0.8564 0.7569 0.6558 0.0438  0.1175  0.0673  157 ARG B CD  
2878 N NE  . ARG B 155 ? 0.8847 0.7907 0.6819 0.0382  0.1110  0.0613  157 ARG B NE  
2879 C CZ  . ARG B 155 ? 0.8532 0.7605 0.6549 0.0363  0.1077  0.0588  157 ARG B CZ  
2880 N NH1 . ARG B 155 ? 0.8327 0.7363 0.6416 0.0399  0.1101  0.0612  157 ARG B NH1 
2881 N NH2 . ARG B 155 ? 0.7994 0.7111 0.5979 0.0306  0.1023  0.0538  157 ARG B NH2 
2882 N N   . ALA B 156 ? 0.8569 0.7324 0.6619 0.0589  0.1397  0.0885  158 ALA B N   
2883 C CA  . ALA B 156 ? 0.8863 0.7552 0.6887 0.0626  0.1468  0.0959  158 ALA B CA  
2884 C C   . ALA B 156 ? 0.8992 0.7618 0.7049 0.0572  0.1508  0.0930  158 ALA B C   
2885 O O   . ALA B 156 ? 0.9180 0.7695 0.7286 0.0564  0.1569  0.0953  158 ALA B O   
2886 C CB  . ALA B 156 ? 0.8934 0.7737 0.6848 0.0682  0.1462  0.1026  158 ALA B CB  
2887 N N   . LYS B 157 ? 0.8963 0.7661 0.6993 0.0535  0.1476  0.0875  159 LYS B N   
2888 C CA  . LYS B 157 ? 0.8985 0.7657 0.7036 0.0496  0.1509  0.0845  159 LYS B CA  
2889 C C   . LYS B 157 ? 0.8715 0.7311 0.6881 0.0444  0.1516  0.0784  159 LYS B C   
2890 O O   . LYS B 157 ? 0.8856 0.7417 0.7064 0.0418  0.1564  0.0778  159 LYS B O   
2891 C CB  . LYS B 157 ? 0.9417 0.8183 0.7397 0.0479  0.1465  0.0796  159 LYS B CB  
2892 C CG  . LYS B 157 ? 1.0251 0.9012 0.8231 0.0457  0.1503  0.0770  159 LYS B CG  
2893 C CD  . LYS B 157 ? 1.1023 0.9868 0.8901 0.0456  0.1469  0.0734  159 LYS B CD  
2894 C CE  . LYS B 157 ? 1.1600 1.0456 0.9454 0.0453  0.1517  0.0725  159 LYS B CE  
2895 N NZ  . LYS B 157 ? 1.1906 1.0842 0.9636 0.0463  0.1495  0.0706  159 LYS B NZ  
2896 N N   . GLY B 158 ? 0.8210 0.6797 0.6423 0.0429  0.1467  0.0739  160 GLY B N   
2897 C CA  . GLY B 158 ? 0.7783 0.6312 0.6099 0.0383  0.1466  0.0681  160 GLY B CA  
2898 C C   . GLY B 158 ? 0.7356 0.5915 0.5692 0.0364  0.1394  0.0621  160 GLY B C   
2899 O O   . GLY B 158 ? 0.7441 0.6066 0.5715 0.0363  0.1344  0.0598  160 GLY B O   
2900 N N   . ASP B 159 ? 0.6901 0.5407 0.5318 0.0342  0.1392  0.0592  161 ASP B N   
2901 C CA  . ASP B 159 ? 0.6463 0.4991 0.4900 0.0326  0.1331  0.0545  161 ASP B CA  
2902 C C   . ASP B 159 ? 0.6129 0.4681 0.4589 0.0287  0.1291  0.0478  161 ASP B C   
2903 O O   . ASP B 159 ? 0.6192 0.4735 0.4685 0.0271  0.1317  0.0460  161 ASP B O   
2904 C CB  . ASP B 159 ? 0.6835 0.5296 0.5343 0.0322  0.1349  0.0541  161 ASP B CB  
2905 C CG  . ASP B 159 ? 0.7863 0.6271 0.6349 0.0369  0.1398  0.0609  161 ASP B CG  
2906 O OD1 . ASP B 159 ? 0.8314 0.6773 0.6731 0.0417  0.1381  0.0651  161 ASP B OD1 
2907 O OD2 . ASP B 159 ? 0.8237 0.6552 0.6770 0.0358  0.1454  0.0620  161 ASP B OD2 
2908 N N   . LYS B 160 ? 0.5754 0.4339 0.4193 0.0274  0.1230  0.0443  162 LYS B N   
2909 C CA  . LYS B 160 ? 0.5486 0.4076 0.3938 0.0243  0.1191  0.0385  162 LYS B CA  
2910 C C   . LYS B 160 ? 0.5343 0.3930 0.3839 0.0221  0.1151  0.0352  162 LYS B C   
2911 O O   . LYS B 160 ? 0.5317 0.3928 0.3788 0.0229  0.1131  0.0368  162 LYS B O   
2912 C CB  . LYS B 160 ? 0.5882 0.4504 0.4235 0.0241  0.1153  0.0374  162 LYS B CB  
2913 C CG  . LYS B 160 ? 0.6953 0.5585 0.5252 0.0261  0.1187  0.0394  162 LYS B CG  
2914 C CD  . LYS B 160 ? 0.8367 0.7017 0.6565 0.0251  0.1148  0.0367  162 LYS B CD  
2915 C CE  . LYS B 160 ? 0.9438 0.8148 0.7548 0.0260  0.1135  0.0402  162 LYS B CE  
2916 N NZ  . LYS B 160 ? 1.0109 0.8832 0.8115 0.0236  0.1096  0.0366  162 LYS B NZ  
2917 N N   . ILE B 161 ? 0.5074 0.3647 0.3635 0.0196  0.1141  0.0308  163 ILE B N   
2918 C CA  . ILE B 161 ? 0.5102 0.3682 0.3694 0.0173  0.1097  0.0271  163 ILE B CA  
2919 C C   . ILE B 161 ? 0.4978 0.3559 0.3549 0.0160  0.1058  0.0235  163 ILE B C   
2920 O O   . ILE B 161 ? 0.5003 0.3579 0.3593 0.0168  0.1078  0.0223  163 ILE B O   
2921 C CB  . ILE B 161 ? 0.5116 0.3675 0.3804 0.0159  0.1124  0.0255  163 ILE B CB  
2922 C CG1 . ILE B 161 ? 0.5192 0.3719 0.3886 0.0179  0.1168  0.0295  163 ILE B CG1 
2923 C CG2 . ILE B 161 ? 0.5341 0.3919 0.4057 0.0135  0.1077  0.0213  163 ILE B CG2 
2924 C CD1 . ILE B 161 ? 0.5523 0.4008 0.4299 0.0159  0.1206  0.0277  163 ILE B CD1 
2925 N N   . ALA B 162 ? 0.4817 0.3405 0.3348 0.0143  0.1006  0.0217  164 ALA B N   
2926 C CA  . ALA B 162 ? 0.4769 0.3337 0.3262 0.0135  0.0968  0.0188  164 ALA B CA  
2927 C C   . ALA B 162 ? 0.5132 0.3705 0.3629 0.0111  0.0921  0.0167  164 ALA B C   
2928 O O   . ALA B 162 ? 0.4976 0.3576 0.3459 0.0095  0.0906  0.0177  164 ALA B O   
2929 C CB  . ALA B 162 ? 0.4616 0.3165 0.3002 0.0136  0.0955  0.0198  164 ALA B CB  
2930 N N   . ILE B 163 ? 0.5142 0.3699 0.3656 0.0112  0.0900  0.0140  165 ILE B N   
2931 C CA  . ILE B 163 ? 0.4879 0.3430 0.3367 0.0091  0.0851  0.0126  165 ILE B CA  
2932 C C   . ILE B 163 ? 0.4978 0.3463 0.3357 0.0088  0.0822  0.0126  165 ILE B C   
2933 O O   . ILE B 163 ? 0.5021 0.3464 0.3381 0.0115  0.0830  0.0117  165 ILE B O   
2934 C CB  . ILE B 163 ? 0.4570 0.3148 0.3137 0.0098  0.0841  0.0100  165 ILE B CB  
2935 C CG1 . ILE B 163 ? 0.4526 0.3158 0.3190 0.0086  0.0867  0.0092  165 ILE B CG1 
2936 C CG2 . ILE B 163 ? 0.4390 0.2951 0.2907 0.0083  0.0788  0.0093  165 ILE B CG2 
2937 C CD1 . ILE B 163 ? 0.4960 0.3641 0.3706 0.0081  0.0854  0.0059  165 ILE B CD1 
2938 N N   . TRP B 164 ? 0.4880 0.3358 0.3188 0.0052  0.0792  0.0134  166 TRP B N   
2939 C CA  . TRP B 164 ? 0.4914 0.3316 0.3105 0.0030  0.0762  0.0132  166 TRP B CA  
2940 C C   . TRP B 164 ? 0.4983 0.3340 0.3155 0.0022  0.0725  0.0123  166 TRP B C   
2941 O O   . TRP B 164 ? 0.4816 0.3223 0.3029 0.0007  0.0707  0.0124  166 TRP B O   
2942 C CB  . TRP B 164 ? 0.4821 0.3255 0.2946 -0.0016 0.0749  0.0146  166 TRP B CB  
2943 C CG  . TRP B 164 ? 0.4807 0.3278 0.2915 -0.0008 0.0777  0.0159  166 TRP B CG  
2944 C CD1 . TRP B 164 ? 0.4727 0.3227 0.2898 0.0034  0.0819  0.0169  166 TRP B CD1 
2945 C CD2 . TRP B 164 ? 0.4825 0.3313 0.2842 -0.0046 0.0764  0.0166  166 TRP B CD2 
2946 N NE1 . TRP B 164 ? 0.4749 0.3283 0.2869 0.0032  0.0832  0.0186  166 TRP B NE1 
2947 C CE2 . TRP B 164 ? 0.4833 0.3370 0.2861 -0.0017 0.0798  0.0182  166 TRP B CE2 
2948 C CE3 . TRP B 164 ? 0.4961 0.3437 0.2886 -0.0107 0.0729  0.0161  166 TRP B CE3 
2949 C CZ2 . TRP B 164 ? 0.5037 0.3624 0.2988 -0.0042 0.0792  0.0192  166 TRP B CZ2 
2950 C CZ3 . TRP B 164 ? 0.5293 0.3818 0.3147 -0.0141 0.0724  0.0165  166 TRP B CZ3 
2951 C CH2 . TRP B 164 ? 0.5250 0.3839 0.3119 -0.0107 0.0753  0.0180  166 TRP B CH2 
2952 N N   . THR B 165 ? 0.4962 0.3218 0.3063 0.0039  0.0716  0.0115  167 THR B N   
2953 C CA  . THR B 165 ? 0.5043 0.3231 0.3101 0.0041  0.0683  0.0114  167 THR B CA  
2954 C C   . THR B 165 ? 0.5174 0.3231 0.3086 0.0007  0.0664  0.0116  167 THR B C   
2955 O O   . THR B 165 ? 0.5304 0.3320 0.3152 -0.0009 0.0679  0.0108  167 THR B O   
2956 C CB  . THR B 165 ? 0.5194 0.3384 0.3318 0.0109  0.0690  0.0104  167 THR B CB  
2957 O OG1 . THR B 165 ? 0.5279 0.3366 0.3335 0.0148  0.0703  0.0095  167 THR B OG1 
2958 C CG2 . THR B 165 ? 0.5257 0.3568 0.3519 0.0132  0.0720  0.0095  167 THR B CG2 
2959 N N   . THR B 166 ? 0.5273 0.3266 0.3129 -0.0010 0.0633  0.0126  168 THR B N   
2960 C CA  . THR B 166 ? 0.5627 0.3502 0.3345 -0.0068 0.0613  0.0132  168 THR B CA  
2961 C C   . THR B 166 ? 0.5877 0.3574 0.3490 -0.0036 0.0620  0.0120  168 THR B C   
2962 O O   . THR B 166 ? 0.6113 0.3700 0.3603 -0.0091 0.0615  0.0114  168 THR B O   
2963 C CB  . THR B 166 ? 0.5887 0.3763 0.3581 -0.0106 0.0580  0.0155  168 THR B CB  
2964 O OG1 . THR B 166 ? 0.6153 0.3941 0.3721 -0.0186 0.0566  0.0162  168 THR B OG1 
2965 C CG2 . THR B 166 ? 0.5835 0.3641 0.3526 -0.0045 0.0564  0.0166  168 THR B CG2 
2966 N N   . GLU B 167 ? 0.5919 0.3591 0.3576 0.0051  0.0631  0.0114  169 GLU B N   
2967 C CA  . GLU B 167 ? 0.6158 0.3652 0.3709 0.0096  0.0637  0.0104  169 GLU B CA  
2968 C C   . GLU B 167 ? 0.5931 0.3458 0.3552 0.0188  0.0669  0.0084  169 GLU B C   
2969 O O   . GLU B 167 ? 0.5784 0.3394 0.3505 0.0253  0.0668  0.0090  169 GLU B O   
2970 C CB  . GLU B 167 ? 0.6729 0.4125 0.4226 0.0116  0.0607  0.0129  169 GLU B CB  
2971 C CG  . GLU B 167 ? 0.7809 0.5001 0.5189 0.0176  0.0615  0.0124  169 GLU B CG  
2972 C CD  . GLU B 167 ? 0.8170 0.5209 0.5418 0.0130  0.0633  0.0096  169 GLU B CD  
2973 O OE1 . GLU B 167 ? 0.8215 0.5166 0.5358 0.0036  0.0618  0.0102  169 GLU B OE1 
2974 O OE2 . GLU B 167 ? 0.7299 0.4321 0.4551 0.0183  0.0663  0.0066  169 GLU B OE2 
2975 N N   . CYS B 168 ? 0.6001 0.3478 0.3569 0.0187  0.0696  0.0059  170 CYS B N   
2976 C CA  . CYS B 168 ? 0.6366 0.3898 0.4003 0.0264  0.0733  0.0040  170 CYS B CA  
2977 C C   . CYS B 168 ? 0.6677 0.4114 0.4289 0.0361  0.0737  0.0034  170 CYS B C   
2978 O O   . CYS B 168 ? 0.6720 0.4245 0.4419 0.0432  0.0763  0.0023  170 CYS B O   
2979 C CB  . CYS B 168 ? 0.6640 0.4166 0.4229 0.0239  0.0763  0.0016  170 CYS B CB  
2980 S SG  . CYS B 168 ? 0.8143 0.5439 0.5525 0.0206  0.0762  -0.0015 170 CYS B SG  
2981 N N   . GLU B 169 ? 0.6673 0.3937 0.4166 0.0368  0.0713  0.0044  171 GLU B N   
2982 C CA  . GLU B 169 ? 0.6835 0.4004 0.4298 0.0473  0.0715  0.0046  171 GLU B CA  
2983 C C   . GLU B 169 ? 0.6973 0.4245 0.4531 0.0522  0.0688  0.0078  171 GLU B C   
2984 O O   . GLU B 169 ? 0.7052 0.4288 0.4607 0.0622  0.0689  0.0083  171 GLU B O   
2985 C CB  . GLU B 169 ? 0.7001 0.3904 0.4274 0.0466  0.0709  0.0042  171 GLU B CB  
2986 C CG  . GLU B 169 ? 0.7305 0.4100 0.4474 0.0428  0.0737  0.0001  171 GLU B CG  
2987 C CD  . GLU B 169 ? 0.8530 0.5378 0.5743 0.0512  0.0780  -0.0034 171 GLU B CD  
2988 O OE1 . GLU B 169 ? 0.8196 0.5101 0.5484 0.0622  0.0792  -0.0030 171 GLU B OE1 
2989 O OE2 . GLU B 169 ? 0.8105 0.4951 0.5276 0.0465  0.0803  -0.0066 171 GLU B OE2 
2990 N N   . ASN B 170 ? 0.6982 0.4388 0.4622 0.0458  0.0663  0.0097  172 ASN B N   
2991 C CA  . ASN B 170 ? 0.6852 0.4383 0.4590 0.0497  0.0637  0.0120  172 ASN B CA  
2992 C C   . ASN B 170 ? 0.6562 0.4292 0.4462 0.0548  0.0661  0.0100  172 ASN B C   
2993 O O   . ASN B 170 ? 0.6292 0.4182 0.4307 0.0499  0.0663  0.0096  172 ASN B O   
2994 C CB  . ASN B 170 ? 0.7132 0.4737 0.4895 0.0407  0.0607  0.0140  172 ASN B CB  
2995 C CG  . ASN B 170 ? 0.7966 0.5419 0.5594 0.0364  0.0577  0.0169  172 ASN B CG  
2996 O OD1 . ASN B 170 ? 0.8491 0.5756 0.5993 0.0402  0.0575  0.0180  172 ASN B OD1 
2997 N ND2 . ASN B 170 ? 0.7980 0.5509 0.5627 0.0282  0.0556  0.0183  172 ASN B ND2 
2998 N N   . ARG B 171 ? 0.6418 0.4139 0.4329 0.0645  0.0684  0.0087  173 ARG B N   
2999 C CA  . ARG B 171 ? 0.6325 0.4234 0.4384 0.0689  0.0714  0.0067  173 ARG B CA  
3000 C C   . ARG B 171 ? 0.6113 0.4221 0.4313 0.0685  0.0691  0.0075  173 ARG B C   
3001 O O   . ARG B 171 ? 0.5903 0.4166 0.4225 0.0648  0.0712  0.0059  173 ARG B O   
3002 C CB  . ARG B 171 ? 0.6673 0.4540 0.4707 0.0804  0.0738  0.0054  173 ARG B CB  
3003 C CG  . ARG B 171 ? 0.6969 0.5047 0.5158 0.0852  0.0772  0.0034  173 ARG B CG  
3004 C CD  . ARG B 171 ? 0.7669 0.5695 0.5817 0.0955  0.0809  0.0014  173 ARG B CD  
3005 N NE  . ARG B 171 ? 0.8203 0.6398 0.6467 0.0964  0.0856  -0.0010 173 ARG B NE  
3006 C CZ  . ARG B 171 ? 0.9036 0.7199 0.7265 0.1017  0.0901  -0.0034 173 ARG B CZ  
3007 N NH1 . ARG B 171 ? 0.9138 0.7473 0.7481 0.1015  0.0945  -0.0050 173 ARG B NH1 
3008 N NH2 . ARG B 171 ? 0.9280 0.7231 0.7354 0.1070  0.0906  -0.0044 173 ARG B NH2 
3009 N N   . GLU B 172 ? 0.6248 0.4352 0.4427 0.0717  0.0648  0.0101  174 GLU B N   
3010 C CA  . GLU B 172 ? 0.6243 0.4550 0.4554 0.0712  0.0625  0.0102  174 GLU B CA  
3011 C C   . GLU B 172 ? 0.6057 0.4431 0.4417 0.0601  0.0619  0.0096  174 GLU B C   
3012 O O   . GLU B 172 ? 0.6071 0.4618 0.4563 0.0577  0.0629  0.0075  174 GLU B O   
3013 C CB  . GLU B 172 ? 0.6798 0.5098 0.5069 0.0778  0.0579  0.0133  174 GLU B CB  
3014 C CG  . GLU B 172 ? 0.8647 0.6914 0.6891 0.0908  0.0585  0.0141  174 GLU B CG  
3015 C CD  . GLU B 172 ? 1.0515 0.8892 0.8853 0.0965  0.0630  0.0108  174 GLU B CD  
3016 O OE1 . GLU B 172 ? 1.0976 0.9579 0.9469 0.0948  0.0639  0.0087  174 GLU B OE1 
3017 O OE2 . GLU B 172 ? 1.1172 0.9406 0.9423 0.1023  0.0658  0.0103  174 GLU B OE2 
3018 N N   . ALA B 173 ? 0.6085 0.4328 0.4340 0.0535  0.0605  0.0111  175 ALA B N   
3019 C CA  . ALA B 173 ? 0.6013 0.4314 0.4305 0.0440  0.0602  0.0106  175 ALA B CA  
3020 C C   . ALA B 173 ? 0.5603 0.3967 0.3972 0.0409  0.0648  0.0081  175 ALA B C   
3021 O O   . ALA B 173 ? 0.5376 0.3871 0.3853 0.0372  0.0658  0.0066  175 ALA B O   
3022 C CB  . ALA B 173 ? 0.6265 0.4419 0.4423 0.0380  0.0583  0.0128  175 ALA B CB  
3023 N N   . VAL B 174 ? 0.5464 0.3732 0.3772 0.0426  0.0677  0.0077  176 VAL B N   
3024 C CA  . VAL B 174 ? 0.5568 0.3870 0.3917 0.0396  0.0720  0.0062  176 VAL B CA  
3025 C C   . VAL B 174 ? 0.5617 0.4079 0.4112 0.0427  0.0749  0.0045  176 VAL B C   
3026 O O   . VAL B 174 ? 0.5389 0.3936 0.3966 0.0380  0.0773  0.0038  176 VAL B O   
3027 C CB  . VAL B 174 ? 0.5654 0.3818 0.3891 0.0414  0.0742  0.0059  176 VAL B CB  
3028 C CG1 . VAL B 174 ? 0.5537 0.3761 0.3826 0.0407  0.0791  0.0046  176 VAL B CG1 
3029 C CG2 . VAL B 174 ? 0.5782 0.3809 0.3885 0.0355  0.0719  0.0071  176 VAL B CG2 
3030 N N   . THR B 175 ? 0.5795 0.4300 0.4321 0.0504  0.0747  0.0039  177 THR B N   
3031 C CA  . THR B 175 ? 0.6029 0.4700 0.4693 0.0529  0.0776  0.0020  177 THR B CA  
3032 C C   . THR B 175 ? 0.5751 0.4569 0.4529 0.0481  0.0758  0.0010  177 THR B C   
3033 O O   . THR B 175 ? 0.5515 0.4451 0.4404 0.0449  0.0791  -0.0008 177 THR B O   
3034 C CB  . THR B 175 ? 0.6613 0.5305 0.5278 0.0630  0.0782  0.0015  177 THR B CB  
3035 O OG1 . THR B 175 ? 0.7187 0.5864 0.5817 0.0678  0.0734  0.0029  177 THR B OG1 
3036 C CG2 . THR B 175 ? 0.6888 0.5431 0.5440 0.0669  0.0808  0.0014  177 THR B CG2 
3037 N N   . HIS B 176 ? 0.5631 0.4440 0.4378 0.0473  0.0709  0.0020  178 HIS B N   
3038 C CA  . HIS B 176 ? 0.5667 0.4607 0.4506 0.0425  0.0691  0.0005  178 HIS B CA  
3039 C C   . HIS B 176 ? 0.5630 0.4555 0.4490 0.0342  0.0715  -0.0003 178 HIS B C   
3040 O O   . HIS B 176 ? 0.5670 0.4705 0.4636 0.0302  0.0734  -0.0027 178 HIS B O   
3041 C CB  . HIS B 176 ? 0.5781 0.4702 0.4560 0.0431  0.0634  0.0021  178 HIS B CB  
3042 C CG  . HIS B 176 ? 0.6484 0.5549 0.5353 0.0383  0.0614  -0.0001 178 HIS B CG  
3043 N ND1 . HIS B 176 ? 0.6829 0.5861 0.5665 0.0317  0.0599  -0.0001 178 HIS B ND1 
3044 C CD2 . HIS B 176 ? 0.6707 0.5952 0.5693 0.0389  0.0608  -0.0029 178 HIS B CD2 
3045 C CE1 . HIS B 176 ? 0.6807 0.5983 0.5732 0.0289  0.0585  -0.0030 178 HIS B CE1 
3046 N NE2 . HIS B 176 ? 0.6834 0.6142 0.5851 0.0324  0.0590  -0.0049 178 HIS B NE2 
3047 N N   . ILE B 177 ? 0.5576 0.4364 0.4331 0.0315  0.0713  0.0017  179 ILE B N   
3048 C CA  . ILE B 177 ? 0.5352 0.4119 0.4112 0.0251  0.0736  0.0017  179 ILE B CA  
3049 C C   . ILE B 177 ? 0.5175 0.3992 0.4017 0.0244  0.0792  0.0005  179 ILE B C   
3050 O O   . ILE B 177 ? 0.5161 0.4042 0.4084 0.0201  0.0813  -0.0010 179 ILE B O   
3051 C CB  . ILE B 177 ? 0.5265 0.3897 0.3896 0.0233  0.0726  0.0041  179 ILE B CB  
3052 C CG1 . ILE B 177 ? 0.5211 0.3808 0.3771 0.0216  0.0675  0.0054  179 ILE B CG1 
3053 C CG2 . ILE B 177 ? 0.5395 0.4022 0.4037 0.0185  0.0759  0.0045  179 ILE B CG2 
3054 C CD1 . ILE B 177 ? 0.5150 0.3610 0.3573 0.0200  0.0661  0.0077  179 ILE B CD1 
3055 N N   . GLY B 178 ? 0.5171 0.3952 0.3985 0.0288  0.0816  0.0012  180 GLY B N   
3056 C CA  . GLY B 178 ? 0.5375 0.4198 0.4250 0.0287  0.0872  0.0008  180 GLY B CA  
3057 C C   . GLY B 178 ? 0.5327 0.4292 0.4340 0.0270  0.0893  -0.0016 180 GLY B C   
3058 O O   . GLY B 178 ? 0.5240 0.4232 0.4313 0.0225  0.0933  -0.0019 180 GLY B O   
3059 N N   . ARG B 179 ? 0.5370 0.4428 0.4431 0.0305  0.0864  -0.0033 181 ARG B N   
3060 C CA  . ARG B 179 ? 0.5507 0.4731 0.4705 0.0285  0.0878  -0.0062 181 ARG B CA  
3061 C C   . ARG B 179 ? 0.5295 0.4549 0.4545 0.0209  0.0874  -0.0082 181 ARG B C   
3062 O O   . ARG B 179 ? 0.5147 0.4469 0.4488 0.0160  0.0914  -0.0102 181 ARG B O   
3063 C CB  . ARG B 179 ? 0.6177 0.5513 0.5409 0.0346  0.0840  -0.0074 181 ARG B CB  
3064 C CG  . ARG B 179 ? 0.7572 0.7100 0.6940 0.0309  0.0837  -0.0110 181 ARG B CG  
3065 C CD  . ARG B 179 ? 0.8991 0.8668 0.8406 0.0374  0.0800  -0.0119 181 ARG B CD  
3066 N NE  . ARG B 179 ? 1.0099 0.9979 0.9657 0.0323  0.0812  -0.0159 181 ARG B NE  
3067 C CZ  . ARG B 179 ? 1.0840 1.0915 1.0481 0.0365  0.0794  -0.0176 181 ARG B CZ  
3068 N NH1 . ARG B 179 ? 1.0924 1.1008 1.0517 0.0472  0.0763  -0.0152 181 ARG B NH1 
3069 N NH2 . ARG B 179 ? 1.0830 1.1093 1.0602 0.0299  0.0808  -0.0218 181 ARG B NH2 
3070 N N   . VAL B 180 ? 0.5258 0.4462 0.4449 0.0197  0.0829  -0.0078 182 VAL B N   
3071 C CA  . VAL B 180 ? 0.5267 0.4496 0.4497 0.0132  0.0825  -0.0102 182 VAL B CA  
3072 C C   . VAL B 180 ? 0.5173 0.4312 0.4391 0.0090  0.0872  -0.0091 182 VAL B C   
3073 O O   . VAL B 180 ? 0.5294 0.4464 0.4581 0.0036  0.0900  -0.0117 182 VAL B O   
3074 C CB  . VAL B 180 ? 0.5473 0.4679 0.4636 0.0134  0.0766  -0.0098 182 VAL B CB  
3075 C CG1 . VAL B 180 ? 0.5468 0.4692 0.4662 0.0070  0.0768  -0.0126 182 VAL B CG1 
3076 C CG2 . VAL B 180 ? 0.5604 0.4909 0.4780 0.0180  0.0720  -0.0104 182 VAL B CG2 
3077 N N   . TYR B 181 ? 0.5065 0.4092 0.4194 0.0114  0.0882  -0.0055 183 TYR B N   
3078 C CA  . TYR B 181 ? 0.5149 0.4096 0.4255 0.0087  0.0924  -0.0037 183 TYR B CA  
3079 C C   . TYR B 181 ? 0.5260 0.4241 0.4447 0.0067  0.0986  -0.0041 183 TYR B C   
3080 O O   . TYR B 181 ? 0.5197 0.4156 0.4421 0.0025  0.1021  -0.0046 183 TYR B O   
3081 C CB  . TYR B 181 ? 0.5083 0.3933 0.4078 0.0119  0.0917  0.0000  183 TYR B CB  
3082 C CG  . TYR B 181 ? 0.5144 0.3924 0.4098 0.0104  0.0950  0.0027  183 TYR B CG  
3083 C CD1 . TYR B 181 ? 0.5185 0.3956 0.4165 0.0069  0.0964  0.0023  183 TYR B CD1 
3084 C CD2 . TYR B 181 ? 0.5037 0.3759 0.3914 0.0128  0.0964  0.0057  183 TYR B CD2 
3085 C CE1 . TYR B 181 ? 0.5175 0.3888 0.4114 0.0069  0.0992  0.0054  183 TYR B CE1 
3086 C CE2 . TYR B 181 ? 0.5122 0.3797 0.3957 0.0121  0.0990  0.0086  183 TYR B CE2 
3087 C CZ  . TYR B 181 ? 0.5221 0.3894 0.4089 0.0095  0.1003  0.0087  183 TYR B CZ  
3088 O OH  . TYR B 181 ? 0.5179 0.3813 0.4002 0.0100  0.1026  0.0121  183 TYR B OH  
3089 N N   . LYS B 182 ? 0.5385 0.4417 0.4598 0.0099  0.1003  -0.0039 184 LYS B N   
3090 C CA  . LYS B 182 ? 0.5620 0.4700 0.4909 0.0078  0.1063  -0.0041 184 LYS B CA  
3091 C C   . LYS B 182 ? 0.5798 0.4965 0.5199 0.0014  0.1078  -0.0081 184 LYS B C   
3092 O O   . LYS B 182 ? 0.5974 0.5115 0.5416 -0.0034 0.1132  -0.0080 184 LYS B O   
3093 C CB  . LYS B 182 ? 0.5655 0.4801 0.4955 0.0130  0.1072  -0.0038 184 LYS B CB  
3094 C CG  . LYS B 182 ? 0.6129 0.5331 0.5498 0.0109  0.1139  -0.0035 184 LYS B CG  
3095 C CD  . LYS B 182 ? 0.6642 0.5908 0.6010 0.0169  0.1151  -0.0032 184 LYS B CD  
3096 C CE  . LYS B 182 ? 0.7486 0.6826 0.6928 0.0141  0.1221  -0.0028 184 LYS B CE  
3097 N NZ  . LYS B 182 ? 0.8069 0.7464 0.7496 0.0207  0.1239  -0.0022 184 LYS B NZ  
3098 N N   . GLU B 183 ? 0.5705 0.4969 0.5147 0.0014  0.1031  -0.0115 185 GLU B N   
3099 C CA  . GLU B 183 ? 0.5748 0.5107 0.5286 -0.0049 0.1033  -0.0162 185 GLU B CA  
3100 C C   . GLU B 183 ? 0.5616 0.4873 0.5134 -0.0103 0.1047  -0.0172 185 GLU B C   
3101 O O   . GLU B 183 ? 0.5514 0.4770 0.5094 -0.0167 0.1092  -0.0195 185 GLU B O   
3102 C CB  . GLU B 183 ? 0.6349 0.5830 0.5910 -0.0025 0.0968  -0.0190 185 GLU B CB  
3103 C CG  . GLU B 183 ? 0.7820 0.7449 0.7487 -0.0086 0.0961  -0.0246 185 GLU B CG  
3104 C CD  . GLU B 183 ? 0.9812 0.9579 0.9493 -0.0042 0.0895  -0.0262 185 GLU B CD  
3105 O OE1 . GLU B 183 ? 1.0475 1.0179 1.0065 0.0020  0.0849  -0.0232 185 GLU B OE1 
3106 O OE2 . GLU B 183 ? 1.0394 1.0338 1.0177 -0.0071 0.0890  -0.0302 185 GLU B OE2 
3107 N N   . ARG B 184 ? 0.5532 0.4699 0.4960 -0.0077 0.1012  -0.0154 186 ARG B N   
3108 C CA  . ARG B 184 ? 0.5554 0.4631 0.4956 -0.0112 0.1024  -0.0161 186 ARG B CA  
3109 C C   . ARG B 184 ? 0.5781 0.4742 0.5166 -0.0123 0.1090  -0.0128 186 ARG B C   
3110 O O   . ARG B 184 ? 0.5874 0.4772 0.5271 -0.0161 0.1121  -0.0144 186 ARG B O   
3111 C CB  . ARG B 184 ? 0.5529 0.4563 0.4841 -0.0080 0.0970  -0.0147 186 ARG B CB  
3112 C CG  . ARG B 184 ? 0.6023 0.5157 0.5349 -0.0081 0.0911  -0.0180 186 ARG B CG  
3113 C CD  . ARG B 184 ? 0.6121 0.5300 0.5502 -0.0139 0.0912  -0.0236 186 ARG B CD  
3114 N NE  . ARG B 184 ? 0.6331 0.5413 0.5654 -0.0147 0.0918  -0.0232 186 ARG B NE  
3115 C CZ  . ARG B 184 ? 0.5973 0.5061 0.5240 -0.0137 0.0874  -0.0237 186 ARG B CZ  
3116 N NH1 . ARG B 184 ? 0.5770 0.4947 0.5025 -0.0122 0.0817  -0.0242 186 ARG B NH1 
3117 N NH2 . ARG B 184 ? 0.5596 0.4608 0.4819 -0.0141 0.0888  -0.0233 186 ARG B NH2 
3118 N N   . LEU B 185 ? 0.5811 0.4740 0.5160 -0.0086 0.1113  -0.0083 187 LEU B N   
3119 C CA  . LEU B 185 ? 0.6063 0.4900 0.5395 -0.0091 0.1177  -0.0045 187 LEU B CA  
3120 C C   . LEU B 185 ? 0.6438 0.5307 0.5862 -0.0147 0.1238  -0.0063 187 LEU B C   
3121 O O   . LEU B 185 ? 0.6595 0.5373 0.6008 -0.0164 0.1297  -0.0034 187 LEU B O   
3122 C CB  . LEU B 185 ? 0.6049 0.4859 0.5309 -0.0035 0.1180  0.0005  187 LEU B CB  
3123 C CG  . LEU B 185 ? 0.6236 0.4994 0.5393 0.0008  0.1136  0.0031  187 LEU B CG  
3124 C CD1 . LEU B 185 ? 0.6242 0.4992 0.5332 0.0054  0.1135  0.0065  187 LEU B CD1 
3125 C CD2 . LEU B 185 ? 0.6295 0.4966 0.5411 0.0004  0.1153  0.0053  187 LEU B CD2 
3126 N N   . GLY B 186 ? 0.6644 0.5643 0.6152 -0.0175 0.1224  -0.0106 188 GLY B N   
3127 C CA  . GLY B 186 ? 0.6970 0.6030 0.6572 -0.0238 0.1278  -0.0127 188 GLY B CA  
3128 C C   . GLY B 186 ? 0.7369 0.6452 0.6974 -0.0216 0.1323  -0.0087 188 GLY B C   
3129 O O   . GLY B 186 ? 0.7460 0.6557 0.7124 -0.0272 0.1385  -0.0088 188 GLY B O   
3130 N N   . LEU B 187 ? 0.7521 0.6608 0.7061 -0.0140 0.1297  -0.0053 189 LEU B N   
3131 C CA  . LEU B 187 ? 0.7804 0.6905 0.7332 -0.0115 0.1343  -0.0016 189 LEU B CA  
3132 C C   . LEU B 187 ? 0.8177 0.7452 0.7807 -0.0128 0.1356  -0.0045 189 LEU B C   
3133 O O   . LEU B 187 ? 0.8176 0.7565 0.7847 -0.0109 0.1305  -0.0082 189 LEU B O   
3134 C CB  . LEU B 187 ? 0.7782 0.6836 0.7206 -0.0034 0.1309  0.0018  189 LEU B CB  
3135 C CG  . LEU B 187 ? 0.7904 0.6816 0.7222 -0.0013 0.1301  0.0056  189 LEU B CG  
3136 C CD1 . LEU B 187 ? 0.7940 0.6829 0.7161 0.0054  0.1270  0.0080  189 LEU B CD1 
3137 C CD2 . LEU B 187 ? 0.8004 0.6831 0.7308 -0.0038 0.1370  0.0097  189 LEU B CD2 
3138 N N   . PRO B 188 ? 0.8410 0.7722 0.8083 -0.0159 0.1425  -0.0028 190 PRO B N   
3139 C CA  . PRO B 188 ? 0.8581 0.8083 0.8349 -0.0161 0.1437  -0.0054 190 PRO B CA  
3140 C C   . PRO B 188 ? 0.9052 0.8620 0.8780 -0.0062 0.1395  -0.0051 190 PRO B C   
3141 O O   . PRO B 188 ? 0.9263 0.8717 0.8883 -0.0003 0.1387  -0.0015 190 PRO B O   
3142 C CB  . PRO B 188 ? 0.8513 0.8013 0.8304 -0.0205 0.1525  -0.0022 190 PRO B CB  
3143 C CG  . PRO B 188 ? 0.8638 0.7951 0.8370 -0.0246 0.1559  0.0011  190 PRO B CG  
3144 C CD  . PRO B 188 ? 0.8455 0.7648 0.8092 -0.0190 0.1497  0.0019  190 PRO B CD  
3145 N N   . PRO B 189 ? 0.9183 0.8929 0.8990 -0.0037 0.1368  -0.0087 191 PRO B N   
3146 C CA  . PRO B 189 ? 0.9339 0.9130 0.9101 0.0067  0.1340  -0.0080 191 PRO B CA  
3147 C C   . PRO B 189 ? 0.9510 0.9259 0.9211 0.0109  0.1392  -0.0044 191 PRO B C   
3148 O O   . PRO B 189 ? 0.9566 0.9267 0.9181 0.0194  0.1367  -0.0034 191 PRO B O   
3149 C CB  . PRO B 189 ? 0.9307 0.9328 0.9189 0.0077  0.1324  -0.0121 191 PRO B CB  
3150 C CG  . PRO B 189 ? 0.9252 0.9363 0.9247 -0.0036 0.1357  -0.0148 191 PRO B CG  
3151 C CD  . PRO B 189 ? 0.9117 0.9037 0.9054 -0.0099 0.1362  -0.0136 191 PRO B CD  
3152 N N   . LYS B 190 ? 0.9509 0.9279 0.9253 0.0046  0.1466  -0.0026 192 LYS B N   
3153 C CA  . LYS B 190 ? 0.9596 0.9319 0.9277 0.0070  0.1525  0.0015  192 LYS B CA  
3154 C C   . LYS B 190 ? 0.9574 0.9103 0.9106 0.0112  0.1508  0.0053  192 LYS B C   
3155 O O   . LYS B 190 ? 0.9623 0.9133 0.9079 0.0172  0.1523  0.0071  192 LYS B O   
3156 C CB  . LYS B 190 ? 0.9977 0.9719 0.9720 -0.0025 0.1605  0.0035  192 LYS B CB  
3157 C CG  . LYS B 190 ? 1.0655 1.0615 1.0543 -0.0073 0.1638  0.0001  192 LYS B CG  
3158 C CD  . LYS B 190 ? 1.1416 1.1374 1.1360 -0.0184 0.1719  0.0021  192 LYS B CD  
3159 C CE  . LYS B 190 ? 1.1798 1.1986 1.1894 -0.0250 0.1746  -0.0021 192 LYS B CE  
3160 N NZ  . LYS B 190 ? 1.1997 1.2194 1.2136 -0.0352 0.1838  0.0005  192 LYS B NZ  
3161 N N   . ILE B 191 ? 0.9427 0.8823 0.8917 0.0079  0.1479  0.0063  193 ILE B N   
3162 C CA  . ILE B 191 ? 0.9310 0.8547 0.8668 0.0112  0.1459  0.0097  193 ILE B CA  
3163 C C   . ILE B 191 ? 0.8933 0.8148 0.8232 0.0174  0.1385  0.0074  193 ILE B C   
3164 O O   . ILE B 191 ? 0.9015 0.8225 0.8339 0.0159  0.1335  0.0051  193 ILE B O   
3165 C CB  . ILE B 191 ? 0.9504 0.8622 0.8847 0.0056  0.1465  0.0119  193 ILE B CB  
3166 C CG1 . ILE B 191 ? 0.9679 0.8794 0.9074 -0.0010 0.1545  0.0146  193 ILE B CG1 
3167 C CG2 . ILE B 191 ? 0.9641 0.8627 0.8853 0.0095  0.1440  0.0154  193 ILE B CG2 
3168 C CD1 . ILE B 191 ? 0.9858 0.8964 0.9196 0.0012  0.1608  0.0196  193 ILE B CD1 
3169 N N   . VAL B 192 ? 0.8498 0.7690 0.7710 0.0241  0.1380  0.0080  194 VAL B N   
3170 C CA  . VAL B 192 ? 0.8052 0.7200 0.7192 0.0301  0.1316  0.0060  194 VAL B CA  
3171 C C   . VAL B 192 ? 0.7468 0.6470 0.6485 0.0301  0.1284  0.0081  194 VAL B C   
3172 O O   . VAL B 192 ? 0.7397 0.6343 0.6348 0.0295  0.1314  0.0112  194 VAL B O   
3173 C CB  . VAL B 192 ? 0.8216 0.7409 0.7324 0.0377  0.1327  0.0045  194 VAL B CB  
3174 C CG1 . VAL B 192 ? 0.8179 0.7548 0.7416 0.0381  0.1363  0.0025  194 VAL B CG1 
3175 C CG2 . VAL B 192 ? 0.8417 0.7537 0.7417 0.0396  0.1364  0.0069  194 VAL B CG2 
3176 N N   . ILE B 193 ? 0.7099 0.6053 0.6085 0.0310  0.1220  0.0065  195 ILE B N   
3177 C CA  . ILE B 193 ? 0.6783 0.5619 0.5661 0.0301  0.1186  0.0082  195 ILE B CA  
3178 C C   . ILE B 193 ? 0.6343 0.5112 0.5118 0.0351  0.1147  0.0067  195 ILE B C   
3179 O O   . ILE B 193 ? 0.6172 0.4975 0.4971 0.0393  0.1127  0.0043  195 ILE B O   
3180 C CB  . ILE B 193 ? 0.6695 0.5517 0.5611 0.0253  0.1154  0.0082  195 ILE B CB  
3181 C CG1 . ILE B 193 ? 0.6743 0.5596 0.5690 0.0265  0.1100  0.0052  195 ILE B CG1 
3182 C CG2 . ILE B 193 ? 0.6746 0.5615 0.5759 0.0204  0.1203  0.0091  195 ILE B CG2 
3183 C CD1 . ILE B 193 ? 0.6719 0.5542 0.5666 0.0225  0.1061  0.0050  195 ILE B CD1 
3184 N N   . GLY B 194 ? 0.6111 0.4787 0.4771 0.0347  0.1136  0.0082  196 GLY B N   
3185 C CA  . GLY B 194 ? 0.5894 0.4484 0.4440 0.0384  0.1106  0.0065  196 GLY B CA  
3186 C C   . GLY B 194 ? 0.5521 0.4024 0.3989 0.0355  0.1050  0.0068  196 GLY B C   
3187 O O   . GLY B 194 ? 0.5342 0.3845 0.3811 0.0310  0.1042  0.0089  196 GLY B O   
3188 N N   . TYR B 195 ? 0.5581 0.4006 0.3977 0.0383  0.1014  0.0048  197 TYR B N   
3189 C CA  . TYR B 195 ? 0.5291 0.3617 0.3589 0.0353  0.0964  0.0049  197 TYR B CA  
3190 C C   . TYR B 195 ? 0.5573 0.3794 0.3730 0.0357  0.0967  0.0037  197 TYR B C   
3191 O O   . TYR B 195 ? 0.5719 0.3890 0.3829 0.0410  0.0981  0.0015  197 TYR B O   
3192 C CB  . TYR B 195 ? 0.5183 0.3485 0.3494 0.0374  0.0923  0.0039  197 TYR B CB  
3193 C CG  . TYR B 195 ? 0.5199 0.3402 0.3413 0.0335  0.0874  0.0045  197 TYR B CG  
3194 C CD1 . TYR B 195 ? 0.5540 0.3604 0.3619 0.0344  0.0858  0.0034  197 TYR B CD1 
3195 C CD2 . TYR B 195 ? 0.5089 0.3335 0.3343 0.0285  0.0847  0.0060  197 TYR B CD2 
3196 C CE1 . TYR B 195 ? 0.5605 0.3577 0.3592 0.0297  0.0817  0.0041  197 TYR B CE1 
3197 C CE2 . TYR B 195 ? 0.5314 0.3483 0.3480 0.0245  0.0806  0.0067  197 TYR B CE2 
3198 C CZ  . TYR B 195 ? 0.5493 0.3526 0.3527 0.0247  0.0791  0.0059  197 TYR B CZ  
3199 O OH  . TYR B 195 ? 0.5591 0.3545 0.3536 0.0198  0.0752  0.0068  197 TYR B OH  
3200 N N   . GLN B 196 ? 0.5633 0.3828 0.3720 0.0304  0.0953  0.0050  198 GLN B N   
3201 C CA  . GLN B 196 ? 0.5703 0.3813 0.3653 0.0289  0.0952  0.0035  198 GLN B CA  
3202 C C   . GLN B 196 ? 0.5754 0.3775 0.3610 0.0237  0.0903  0.0031  198 GLN B C   
3203 O O   . GLN B 196 ? 0.5527 0.3593 0.3415 0.0191  0.0877  0.0052  198 GLN B O   
3204 C CB  . GLN B 196 ? 0.5881 0.4062 0.3819 0.0265  0.0980  0.0054  198 GLN B CB  
3205 C CG  . GLN B 196 ? 0.6637 0.4913 0.4670 0.0302  0.1034  0.0070  198 GLN B CG  
3206 C CD  . GLN B 196 ? 0.7856 0.6209 0.5902 0.0276  0.1055  0.0107  198 GLN B CD  
3207 O OE1 . GLN B 196 ? 0.8433 0.6798 0.6457 0.0235  0.1028  0.0126  198 GLN B OE1 
3208 N NE2 . GLN B 196 ? 0.8014 0.6424 0.6092 0.0302  0.1107  0.0123  198 GLN B NE2 
3209 N N   . SER B 197 ? 0.5660 0.3548 0.3395 0.0243  0.0892  0.0002  199 SER B N   
3210 C CA  . SER B 197 ? 0.5849 0.3630 0.3466 0.0181  0.0853  -0.0006 199 SER B CA  
3211 C C   . SER B 197 ? 0.5770 0.3621 0.3349 0.0111  0.0848  0.0004  199 SER B C   
3212 O O   . SER B 197 ? 0.5850 0.3760 0.3423 0.0123  0.0878  0.0001  199 SER B O   
3213 C CB  . SER B 197 ? 0.6195 0.3805 0.3678 0.0205  0.0858  -0.0045 199 SER B CB  
3214 O OG  . SER B 197 ? 0.7132 0.4630 0.4485 0.0131  0.0828  -0.0057 199 SER B OG  
3215 N N   . HIS B 198 ? 0.5768 0.3629 0.3323 0.0044  0.0812  0.0017  200 HIS B N   
3216 C CA  . HIS B 198 ? 0.5794 0.3737 0.3307 -0.0020 0.0803  0.0024  200 HIS B CA  
3217 C C   . HIS B 198 ? 0.6197 0.4057 0.3564 -0.0052 0.0807  -0.0013 200 HIS B C   
3218 O O   . HIS B 198 ? 0.6381 0.4331 0.3726 -0.0067 0.0819  -0.0012 200 HIS B O   
3219 C CB  . HIS B 198 ? 0.5741 0.3716 0.3253 -0.0086 0.0765  0.0042  200 HIS B CB  
3220 C CG  . HIS B 198 ? 0.5586 0.3666 0.3233 -0.0063 0.0762  0.0074  200 HIS B CG  
3221 N ND1 . HIS B 198 ? 0.5707 0.3893 0.3460 -0.0016 0.0793  0.0095  200 HIS B ND1 
3222 C CD2 . HIS B 198 ? 0.5771 0.3852 0.3451 -0.0084 0.0735  0.0086  200 HIS B CD2 
3223 C CE1 . HIS B 198 ? 0.5813 0.4056 0.3658 -0.0013 0.0784  0.0114  200 HIS B CE1 
3224 N NE2 . HIS B 198 ? 0.5665 0.3855 0.3470 -0.0051 0.0748  0.0108  200 HIS B NE2 
3225 N N   . ALA B 199 ? 0.6330 0.4017 0.3594 -0.0061 0.0797  -0.0047 201 ALA B N   
3226 C CA  . ALA B 199 ? 0.6866 0.4437 0.3983 -0.0084 0.0806  -0.0094 201 ALA B CA  
3227 C C   . ALA B 199 ? 0.7249 0.4866 0.4375 -0.0020 0.0849  -0.0110 201 ALA B C   
3228 O O   . ALA B 199 ? 0.7550 0.5178 0.4583 -0.0055 0.0856  -0.0137 201 ALA B O   
3229 C CB  . ALA B 199 ? 0.6985 0.4339 0.4007 -0.0076 0.0798  -0.0122 201 ALA B CB  
3230 N N   . ASP B 200 ? 0.7174 0.4834 0.4411 0.0068  0.0879  -0.0093 202 ASP B N   
3231 C CA  . ASP B 200 ? 0.7266 0.4987 0.4518 0.0124  0.0924  -0.0101 202 ASP B CA  
3232 C C   . ASP B 200 ? 0.7283 0.5183 0.4597 0.0105  0.0934  -0.0063 202 ASP B C   
3233 O O   . ASP B 200 ? 0.7262 0.5208 0.4517 0.0106  0.0957  -0.0074 202 ASP B O   
3234 C CB  . ASP B 200 ? 0.7597 0.5314 0.4943 0.0218  0.0955  -0.0098 202 ASP B CB  
3235 C CG  . ASP B 200 ? 0.8567 0.6109 0.5841 0.0259  0.0951  -0.0134 202 ASP B CG  
3236 O OD1 . ASP B 200 ? 0.8892 0.6286 0.6015 0.0220  0.0938  -0.0173 202 ASP B OD1 
3237 O OD2 . ASP B 200 ? 0.8474 0.6024 0.5837 0.0331  0.0962  -0.0125 202 ASP B OD2 
3238 N N   . THR B 201 ? 0.7154 0.5152 0.4579 0.0093  0.0920  -0.0017 203 THR B N   
3239 C CA  . THR B 201 ? 0.7380 0.5533 0.4861 0.0084  0.0930  0.0025  203 THR B CA  
3240 C C   . THR B 201 ? 0.7688 0.5888 0.5061 0.0021  0.0908  0.0018  203 THR B C   
3241 O O   . THR B 201 ? 0.7719 0.6027 0.5088 0.0032  0.0929  0.0040  203 THR B O   
3242 C CB  . THR B 201 ? 0.7445 0.5668 0.5045 0.0079  0.0915  0.0065  203 THR B CB  
3243 O OG1 . THR B 201 ? 0.7640 0.5841 0.5341 0.0132  0.0935  0.0068  203 THR B OG1 
3244 C CG2 . THR B 201 ? 0.7329 0.5695 0.4982 0.0081  0.0930  0.0112  203 THR B CG2 
3245 N N   . ALA B 202 ? 0.7727 0.5854 0.5014 -0.0047 0.0868  -0.0011 204 ALA B N   
3246 C CA  . ALA B 202 ? 0.7810 0.5982 0.4989 -0.0123 0.0843  -0.0028 204 ALA B CA  
3247 C C   . ALA B 202 ? 0.8132 0.6290 0.5202 -0.0120 0.0864  -0.0065 204 ALA B C   
3248 O O   . ALA B 202 ? 0.8212 0.6484 0.5229 -0.0161 0.0854  -0.0062 204 ALA B O   
3249 C CB  . ALA B 202 ? 0.7850 0.5907 0.4948 -0.0200 0.0804  -0.0060 204 ALA B CB  
3250 N N   . THR B 203 ? 0.8324 0.6352 0.5356 -0.0072 0.0893  -0.0102 205 THR B N   
3251 C CA  . THR B 203 ? 0.8663 0.6667 0.5582 -0.0066 0.0917  -0.0145 205 THR B CA  
3252 C C   . THR B 203 ? 0.8378 0.6504 0.5369 0.0009  0.0963  -0.0109 205 THR B C   
3253 O O   . THR B 203 ? 0.8294 0.6410 0.5388 0.0077  0.0992  -0.0086 205 THR B O   
3254 C CB  . THR B 203 ? 0.9440 0.7234 0.6264 -0.0051 0.0928  -0.0208 205 THR B CB  
3255 O OG1 . THR B 203 ? 0.9886 0.7625 0.6814 0.0030  0.0948  -0.0190 205 THR B OG1 
3256 C CG2 . THR B 203 ? 0.9675 0.7328 0.6390 -0.0141 0.0887  -0.0247 205 THR B CG2 
3257 N N   . LYS B 204 ? 0.8135 0.6381 0.5067 -0.0008 0.0969  -0.0103 206 LYS B N   
3258 C CA  . LYS B 204 ? 0.7950 0.6316 0.4933 0.0055  0.1014  -0.0061 206 LYS B CA  
3259 C C   . LYS B 204 ? 0.7901 0.6205 0.4790 0.0091  0.1053  -0.0111 206 LYS B C   
3260 O O   . LYS B 204 ? 0.7623 0.5922 0.4374 0.0051  0.1045  -0.0159 206 LYS B O   
3261 C CB  . LYS B 204 ? 0.8155 0.6700 0.5127 0.0029  0.0999  -0.0014 206 LYS B CB  
3262 C CG  . LYS B 204 ? 0.8405 0.7027 0.5454 -0.0005 0.0960  0.0031  206 LYS B CG  
3263 C CD  . LYS B 204 ? 0.9330 0.7975 0.6533 0.0052  0.0982  0.0093  206 LYS B CD  
3264 C CE  . LYS B 204 ? 0.9971 0.8761 0.7239 0.0054  0.0968  0.0159  206 LYS B CE  
3265 N NZ  . LYS B 204 ? 1.0338 0.9158 0.7727 0.0123  0.1012  0.0222  206 LYS B NZ  
3266 N N   . SER B 205 ? 0.8049 0.6317 0.5016 0.0165  0.1097  -0.0103 207 SER B N   
3267 C CA  . SER B 205 ? 0.8187 0.6385 0.5086 0.0214  0.1139  -0.0154 207 SER B CA  
3268 C C   . SER B 205 ? 0.8004 0.6321 0.4969 0.0279  0.1198  -0.0111 207 SER B C   
3269 O O   . SER B 205 ? 0.8076 0.6352 0.5021 0.0332  0.1240  -0.0145 207 SER B O   
3270 C CB  . SER B 205 ? 0.8791 0.6831 0.5716 0.0250  0.1141  -0.0192 207 SER B CB  
3271 O OG  . SER B 205 ? 0.9788 0.7689 0.6627 0.0191  0.1094  -0.0235 207 SER B OG  
3272 N N   . GLY B 206 ? 0.7858 0.6315 0.4893 0.0275  0.1204  -0.0038 208 GLY B N   
3273 C CA  . GLY B 206 ? 0.7831 0.6393 0.4933 0.0327  0.1262  0.0017  208 GLY B CA  
3274 C C   . GLY B 206 ? 0.7877 0.6503 0.5127 0.0334  0.1267  0.0095  208 GLY B C   
3275 O O   . GLY B 206 ? 0.7633 0.6284 0.4906 0.0298  0.1226  0.0125  208 GLY B O   
3276 N N   . SER B 207 ? 0.8117 0.6775 0.5470 0.0379  0.1320  0.0129  209 SER B N   
3277 C CA  . SER B 207 ? 0.8266 0.6975 0.5752 0.0381  0.1333  0.0202  209 SER B CA  
3278 C C   . SER B 207 ? 0.8452 0.7097 0.6052 0.0374  0.1310  0.0188  209 SER B C   
3279 O O   . SER B 207 ? 0.8442 0.7111 0.6135 0.0363  0.1306  0.0235  209 SER B O   
3280 C CB  . SER B 207 ? 0.8478 0.7255 0.6019 0.0417  0.1405  0.0249  209 SER B CB  
3281 O OG  . SER B 207 ? 0.8951 0.7713 0.6490 0.0450  0.1443  0.0202  209 SER B OG  
3282 N N   . THR B 208 ? 0.8574 0.7134 0.6162 0.0384  0.1294  0.0124  210 THR B N   
3283 C CA  . THR B 208 ? 0.8638 0.7150 0.6332 0.0385  0.1273  0.0113  210 THR B CA  
3284 C C   . THR B 208 ? 0.8488 0.6887 0.6111 0.0366  0.1218  0.0058  210 THR B C   
3285 O O   . THR B 208 ? 0.8630 0.6971 0.6121 0.0358  0.1207  0.0015  210 THR B O   
3286 C CB  . THR B 208 ? 0.9028 0.7569 0.6816 0.0433  0.1323  0.0106  210 THR B CB  
3287 O OG1 . THR B 208 ? 0.9301 0.7828 0.7207 0.0430  0.1303  0.0107  210 THR B OG1 
3288 C CG2 . THR B 208 ? 0.9195 0.7689 0.6902 0.0475  0.1339  0.0047  210 THR B CG2 
3289 N N   . THR B 209 ? 0.8059 0.6424 0.5765 0.0357  0.1187  0.0060  211 THR B N   
3290 C CA  . THR B 209 ? 0.7904 0.6157 0.5563 0.0340  0.1137  0.0021  211 THR B CA  
3291 C C   . THR B 209 ? 0.7289 0.5513 0.5033 0.0391  0.1147  0.0002  211 THR B C   
3292 O O   . THR B 209 ? 0.7172 0.5477 0.5046 0.0407  0.1168  0.0030  211 THR B O   
3293 C CB  . THR B 209 ? 0.8193 0.6449 0.5853 0.0278  0.1087  0.0043  211 THR B CB  
3294 O OG1 . THR B 209 ? 0.8266 0.6428 0.5926 0.0268  0.1047  0.0020  211 THR B OG1 
3295 C CG2 . THR B 209 ? 0.8559 0.6918 0.6328 0.0271  0.1098  0.0099  211 THR B CG2 
3296 N N   . LYS B 210 ? 0.7010 0.5119 0.4673 0.0419  0.1135  -0.0046 212 LYS B N   
3297 C CA  . LYS B 210 ? 0.6989 0.5064 0.4710 0.0480  0.1139  -0.0066 212 LYS B CA  
3298 C C   . LYS B 210 ? 0.6723 0.4830 0.4557 0.0464  0.1106  -0.0039 212 LYS B C   
3299 O O   . LYS B 210 ? 0.6724 0.4794 0.4531 0.0408  0.1064  -0.0026 212 LYS B O   
3300 C CB  . LYS B 210 ? 0.7464 0.5365 0.5051 0.0502  0.1116  -0.0116 212 LYS B CB  
3301 C CG  . LYS B 210 ? 0.8646 0.6476 0.6091 0.0512  0.1141  -0.0159 212 LYS B CG  
3302 C CD  . LYS B 210 ? 0.9379 0.7025 0.6709 0.0553  0.1130  -0.0209 212 LYS B CD  
3303 C CE  . LYS B 210 ? 0.9862 0.7368 0.7129 0.0500  0.1075  -0.0210 212 LYS B CE  
3304 N NZ  . LYS B 210 ? 1.0161 0.7454 0.7268 0.0522  0.1072  -0.0264 212 LYS B NZ  
3305 N N   . ASN B 211 ? 0.6601 0.4787 0.4558 0.0510  0.1126  -0.0033 213 ASN B N   
3306 C CA  . ASN B 211 ? 0.6652 0.4860 0.4704 0.0510  0.1093  -0.0022 213 ASN B CA  
3307 C C   . ASN B 211 ? 0.6796 0.4899 0.4795 0.0563  0.1067  -0.0050 213 ASN B C   
3308 O O   . ASN B 211 ? 0.6834 0.4916 0.4805 0.0632  0.1094  -0.0076 213 ASN B O   
3309 C CB  . ASN B 211 ? 0.6810 0.5172 0.5021 0.0525  0.1127  -0.0004 213 ASN B CB  
3310 C CG  . ASN B 211 ? 0.7168 0.5612 0.5435 0.0472  0.1153  0.0031  213 ASN B CG  
3311 O OD1 . ASN B 211 ? 0.7597 0.6138 0.5940 0.0482  0.1203  0.0042  213 ASN B OD1 
3312 N ND2 . ASN B 211 ? 0.6847 0.5258 0.5080 0.0416  0.1126  0.0052  213 ASN B ND2 
3313 N N   . ARG B 212 ? 0.6864 0.4896 0.4840 0.0534  0.1017  -0.0042 214 ARG B N   
3314 C CA  . ARG B 212 ? 0.7082 0.5007 0.5009 0.0583  0.0987  -0.0056 214 ARG B CA  
3315 C C   . ARG B 212 ? 0.7079 0.5139 0.5154 0.0640  0.0992  -0.0047 214 ARG B C   
3316 O O   . ARG B 212 ? 0.7217 0.5259 0.5288 0.0723  0.1000  -0.0063 214 ARG B O   
3317 C CB  . ARG B 212 ? 0.7467 0.5289 0.5321 0.0515  0.0935  -0.0042 214 ARG B CB  
3318 C CG  . ARG B 212 ? 0.8555 0.6235 0.6332 0.0544  0.0899  -0.0045 214 ARG B CG  
3319 C CD  . ARG B 212 ? 0.9092 0.6586 0.6713 0.0581  0.0911  -0.0078 214 ARG B CD  
3320 N NE  . ARG B 212 ? 0.9380 0.6768 0.6869 0.0499  0.0905  -0.0093 214 ARG B NE  
3321 C CZ  . ARG B 212 ? 0.9331 0.6624 0.6740 0.0422  0.0867  -0.0083 214 ARG B CZ  
3322 N NH1 . ARG B 212 ? 0.9200 0.6424 0.6497 0.0345  0.0864  -0.0102 214 ARG B NH1 
3323 N NH2 . ARG B 212 ? 0.9461 0.6742 0.6901 0.0417  0.0832  -0.0054 214 ARG B NH2 
3324 N N   . PHE B 213 ? 0.6878 0.5077 0.5082 0.0595  0.0989  -0.0025 215 PHE B N   
3325 C CA  . PHE B 213 ? 0.6775 0.5123 0.5127 0.0623  0.0990  -0.0020 215 PHE B CA  
3326 C C   . PHE B 213 ? 0.6843 0.5336 0.5314 0.0578  0.1029  -0.0009 215 PHE B C   
3327 O O   . PHE B 213 ? 0.6810 0.5284 0.5254 0.0520  0.1041  0.0005  215 PHE B O   
3328 C CB  . PHE B 213 ? 0.6676 0.5020 0.5053 0.0600  0.0935  -0.0006 215 PHE B CB  
3329 C CG  . PHE B 213 ? 0.6863 0.5039 0.5108 0.0620  0.0894  -0.0005 215 PHE B CG  
3330 C CD1 . PHE B 213 ? 0.7286 0.5401 0.5486 0.0711  0.0891  -0.0015 215 PHE B CD1 
3331 C CD2 . PHE B 213 ? 0.7011 0.5085 0.5170 0.0550  0.0862  0.0007  215 PHE B CD2 
3332 C CE1 . PHE B 213 ? 0.7470 0.5401 0.5533 0.0729  0.0859  -0.0011 215 PHE B CE1 
3333 C CE2 . PHE B 213 ? 0.7273 0.5186 0.5307 0.0558  0.0828  0.0011  215 PHE B CE2 
3334 C CZ  . PHE B 213 ? 0.7399 0.5228 0.5380 0.0646  0.0828  0.0003  215 PHE B CZ  
3335 N N   . VAL B 214 ? 0.6939 0.5580 0.5540 0.0604  0.1048  -0.0015 216 VAL B N   
3336 C CA  . VAL B 214 ? 0.7194 0.5972 0.5918 0.0557  0.1087  -0.0006 216 VAL B CA  
3337 C C   . VAL B 214 ? 0.7123 0.6033 0.5979 0.0549  0.1067  -0.0013 216 VAL B C   
3338 O O   . VAL B 214 ? 0.6990 0.5935 0.5860 0.0608  0.1042  -0.0026 216 VAL B O   
3339 C CB  . VAL B 214 ? 0.7423 0.6272 0.6169 0.0591  0.1150  -0.0012 216 VAL B CB  
3340 C CG1 . VAL B 214 ? 0.7650 0.6653 0.6538 0.0546  0.1194  -0.0004 216 VAL B CG1 
3341 C CG2 . VAL B 214 ? 0.7564 0.6302 0.6185 0.0582  0.1172  -0.0004 216 VAL B CG2 
3342 N N   . VAL B 215 ? 0.7261 0.6239 0.6204 0.0476  0.1078  -0.0006 217 VAL B N   
3343 C CA  . VAL B 215 ? 0.7299 0.6423 0.6377 0.0454  0.1071  -0.0021 217 VAL B CA  
3344 C C   . VAL B 215 ? 0.7413 0.6623 0.6588 0.0390  0.1127  -0.0018 217 VAL B C   
3345 O O   . VAL B 215 ? 0.7511 0.6867 0.6808 0.0368  0.1138  -0.0037 217 VAL B O   
3346 C CB  . VAL B 215 ? 0.7381 0.6481 0.6458 0.0422  0.1012  -0.0024 217 VAL B CB  
3347 C CG1 . VAL B 215 ? 0.7480 0.6490 0.6457 0.0482  0.0960  -0.0021 217 VAL B CG1 
3348 C CG2 . VAL B 215 ? 0.7498 0.6514 0.6543 0.0350  0.1015  -0.0008 217 VAL B CG2 
3349 O OXT . VAL B 215 ? 0.7724 0.6856 0.6850 0.0360  0.1161  0.0005  217 VAL B OXT 
# 
