data_9C0L
# 
_entry.id   9C0L 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9C0L         pdb_00009c0l 10.2210/pdb9c0l/pdb 
WWPDB D_1000284405 ?            ?                   
# 
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 2025-01-08 ? 
2 'Structure model' 1 1 2025-01-15 ? 
3 'Structure model' 1 2 2025-04-16 ? 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' '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' pdbx_database_related 
2 3 'Structure model' citation              
3 3 '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 3 'Structure model' '_citation.journal_volume'          
2 3 'Structure model' '_citation.page_first'              
3 3 'Structure model' '_citation.page_last'               
4 3 'Structure model' '_citation.year'                    
5 3 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9C0L 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-26 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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_database_related.content_type   unspecified 
_pdbx_database_related.db_id          SASDV64 
_pdbx_database_related.db_name        SASBDB 
_pdbx_database_related.details        . 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              matthias.fellner@otago.ac.nz 
_pdbx_contact_author.name_first         Matthias 
_pdbx_contact_author.name_last          Fellner 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3192-6984 
# 
_audit_author.name               'Fellner, M.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0003-3192-6984 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Proteins 
_citation.journal_id_ASTM           PSFGEY 
_citation.journal_id_CSD            0867 
_citation.journal_id_ISSN           1097-0134 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            93 
_citation.language                  ? 
_citation.page_first                1009 
_citation.page_last                 1021 
_citation.title                     
'Similar but Distinct-Biochemical Characterization of the Staphylococcus aureus Serine Hydrolases FphH and FphI.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/prot.26785 
_citation.pdbx_database_id_PubMed   39726198 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Fellner, M.'     1 ? 
primary 'Randall, G.'     2 ? 
primary 'Bitac, I.R.C.G.' 3 ? 
primary 'Warrender, A.K.' 4 ? 
primary 'Sethi, A.'       5 ? 
primary 'Jelinek, R.'     6 ? 
primary 'Kass, I.'        7 ? 
# 
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 'Alpha/beta fold hydrolase' 28335.621 1   ? 'N-terminal GPG from expression tag' ? ? 
2 non-polymer syn 'CALCIUM ION'               40.078    4   ? ?                                    ? ? 
3 water       nat water                       18.015    145 ? ?                                    ? ? 
# 
_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       
;GPGMQIKLPKPFFFEEGKRAVLLLHGFTGNSSDVRQLGRFLQKKGYTSYAPQYEGHAAPPDEILKSSPFVWFKDALDGYD
YLVEQGYDEIVVAGLSLGGDFALKLSLNRDVKGIVTMCAPMGGKTEGAIYEGFLEYARNFKKYEGKDQETIDNEMDHFKP
TETLKELSEALDTIKEQVDEVLDPILVIQAENDNMIDPQSANYIYDHVDSDDKNIKWYSESGHVITIDKEKEQVFEDIYQ
FLESLDWSE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPGMQIKLPKPFFFEEGKRAVLLLHGFTGNSSDVRQLGRFLQKKGYTSYAPQYEGHAAPPDEILKSSPFVWFKDALDGYD
YLVEQGYDEIVVAGLSLGGDFALKLSLNRDVKGIVTMCAPMGGKTEGAIYEGFLEYARNFKKYEGKDQETIDNEMDHFKP
TETLKELSEALDTIKEQVDEVLDPILVIQAENDNMIDPQSANYIYDHVDSDDKNIKWYSESGHVITIDKEKEQVFEDIYQ
FLESLDWSE
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CALCIUM ION' CA  
3 water         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   GLY n 
1 4   MET n 
1 5   GLN n 
1 6   ILE n 
1 7   LYS n 
1 8   LEU n 
1 9   PRO n 
1 10  LYS n 
1 11  PRO n 
1 12  PHE n 
1 13  PHE n 
1 14  PHE n 
1 15  GLU n 
1 16  GLU n 
1 17  GLY n 
1 18  LYS n 
1 19  ARG n 
1 20  ALA n 
1 21  VAL n 
1 22  LEU n 
1 23  LEU n 
1 24  LEU n 
1 25  HIS n 
1 26  GLY n 
1 27  PHE n 
1 28  THR n 
1 29  GLY n 
1 30  ASN n 
1 31  SER n 
1 32  SER n 
1 33  ASP n 
1 34  VAL n 
1 35  ARG n 
1 36  GLN n 
1 37  LEU n 
1 38  GLY n 
1 39  ARG n 
1 40  PHE n 
1 41  LEU n 
1 42  GLN n 
1 43  LYS n 
1 44  LYS n 
1 45  GLY n 
1 46  TYR n 
1 47  THR n 
1 48  SER n 
1 49  TYR n 
1 50  ALA n 
1 51  PRO n 
1 52  GLN n 
1 53  TYR n 
1 54  GLU n 
1 55  GLY n 
1 56  HIS n 
1 57  ALA n 
1 58  ALA n 
1 59  PRO n 
1 60  PRO n 
1 61  ASP n 
1 62  GLU n 
1 63  ILE n 
1 64  LEU n 
1 65  LYS n 
1 66  SER n 
1 67  SER n 
1 68  PRO n 
1 69  PHE n 
1 70  VAL n 
1 71  TRP n 
1 72  PHE n 
1 73  LYS n 
1 74  ASP n 
1 75  ALA n 
1 76  LEU n 
1 77  ASP n 
1 78  GLY n 
1 79  TYR n 
1 80  ASP n 
1 81  TYR n 
1 82  LEU n 
1 83  VAL n 
1 84  GLU n 
1 85  GLN n 
1 86  GLY n 
1 87  TYR n 
1 88  ASP n 
1 89  GLU n 
1 90  ILE n 
1 91  VAL n 
1 92  VAL n 
1 93  ALA n 
1 94  GLY n 
1 95  LEU n 
1 96  SER n 
1 97  LEU n 
1 98  GLY n 
1 99  GLY n 
1 100 ASP n 
1 101 PHE n 
1 102 ALA n 
1 103 LEU n 
1 104 LYS n 
1 105 LEU n 
1 106 SER n 
1 107 LEU n 
1 108 ASN n 
1 109 ARG n 
1 110 ASP n 
1 111 VAL n 
1 112 LYS n 
1 113 GLY n 
1 114 ILE n 
1 115 VAL n 
1 116 THR n 
1 117 MET n 
1 118 CYS n 
1 119 ALA n 
1 120 PRO n 
1 121 MET n 
1 122 GLY n 
1 123 GLY n 
1 124 LYS n 
1 125 THR n 
1 126 GLU n 
1 127 GLY n 
1 128 ALA n 
1 129 ILE n 
1 130 TYR n 
1 131 GLU n 
1 132 GLY n 
1 133 PHE n 
1 134 LEU n 
1 135 GLU n 
1 136 TYR n 
1 137 ALA n 
1 138 ARG n 
1 139 ASN n 
1 140 PHE n 
1 141 LYS n 
1 142 LYS n 
1 143 TYR n 
1 144 GLU n 
1 145 GLY n 
1 146 LYS n 
1 147 ASP n 
1 148 GLN n 
1 149 GLU n 
1 150 THR n 
1 151 ILE n 
1 152 ASP n 
1 153 ASN n 
1 154 GLU n 
1 155 MET n 
1 156 ASP n 
1 157 HIS n 
1 158 PHE n 
1 159 LYS n 
1 160 PRO n 
1 161 THR n 
1 162 GLU n 
1 163 THR n 
1 164 LEU n 
1 165 LYS n 
1 166 GLU n 
1 167 LEU n 
1 168 SER n 
1 169 GLU n 
1 170 ALA n 
1 171 LEU n 
1 172 ASP n 
1 173 THR n 
1 174 ILE n 
1 175 LYS n 
1 176 GLU n 
1 177 GLN n 
1 178 VAL n 
1 179 ASP n 
1 180 GLU n 
1 181 VAL n 
1 182 LEU n 
1 183 ASP n 
1 184 PRO n 
1 185 ILE n 
1 186 LEU n 
1 187 VAL n 
1 188 ILE n 
1 189 GLN n 
1 190 ALA n 
1 191 GLU n 
1 192 ASN n 
1 193 ASP n 
1 194 ASN n 
1 195 MET n 
1 196 ILE n 
1 197 ASP n 
1 198 PRO n 
1 199 GLN n 
1 200 SER n 
1 201 ALA n 
1 202 ASN n 
1 203 TYR n 
1 204 ILE n 
1 205 TYR n 
1 206 ASP n 
1 207 HIS n 
1 208 VAL n 
1 209 ASP n 
1 210 SER n 
1 211 ASP n 
1 212 ASP n 
1 213 LYS n 
1 214 ASN n 
1 215 ILE n 
1 216 LYS n 
1 217 TRP n 
1 218 TYR n 
1 219 SER n 
1 220 GLU n 
1 221 SER n 
1 222 GLY n 
1 223 HIS n 
1 224 VAL n 
1 225 ILE n 
1 226 THR n 
1 227 ILE n 
1 228 ASP n 
1 229 LYS n 
1 230 GLU n 
1 231 LYS n 
1 232 GLU n 
1 233 GLN n 
1 234 VAL n 
1 235 PHE n 
1 236 GLU n 
1 237 ASP n 
1 238 ILE n 
1 239 TYR n 
1 240 GLN n 
1 241 PHE n 
1 242 LEU n 
1 243 GLU n 
1 244 SER n 
1 245 LEU n 
1 246 ASP n 
1 247 TRP n 
1 248 SER n 
1 249 GLU 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                   249 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 est_2 
_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      'Staphylococcus aureus USA300-CA-263' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1385529 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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               ? 
_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 
CA  non-polymer         . 'CALCIUM ION'   ? 'Ca 2'           40.078  
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 
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 
# 
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   GLY 1   -2  ?   ?   ?   A . n 
A 1 2   PRO 2   -1  ?   ?   ?   A . n 
A 1 3   GLY 3   0   ?   ?   ?   A . n 
A 1 4   MET 4   1   ?   ?   ?   A . n 
A 1 5   GLN 5   2   ?   ?   ?   A . n 
A 1 6   ILE 6   3   ?   ?   ?   A . n 
A 1 7   LYS 7   4   4   LYS LYS A . n 
A 1 8   LEU 8   5   5   LEU LEU A . n 
A 1 9   PRO 9   6   6   PRO PRO A . n 
A 1 10  LYS 10  7   7   LYS LYS A . n 
A 1 11  PRO 11  8   8   PRO PRO A . n 
A 1 12  PHE 12  9   9   PHE PHE A . n 
A 1 13  PHE 13  10  10  PHE PHE A . n 
A 1 14  PHE 14  11  11  PHE PHE A . n 
A 1 15  GLU 15  12  12  GLU GLU A . n 
A 1 16  GLU 16  13  13  GLU GLU A . n 
A 1 17  GLY 17  14  14  GLY GLY A . n 
A 1 18  LYS 18  15  15  LYS LYS A . n 
A 1 19  ARG 19  16  16  ARG ARG A . n 
A 1 20  ALA 20  17  17  ALA ALA A . n 
A 1 21  VAL 21  18  18  VAL VAL A . n 
A 1 22  LEU 22  19  19  LEU LEU A . n 
A 1 23  LEU 23  20  20  LEU LEU A . n 
A 1 24  LEU 24  21  21  LEU LEU A . n 
A 1 25  HIS 25  22  22  HIS HIS A . n 
A 1 26  GLY 26  23  23  GLY GLY A . n 
A 1 27  PHE 27  24  24  PHE PHE A . n 
A 1 28  THR 28  25  25  THR THR A . n 
A 1 29  GLY 29  26  26  GLY GLY A . n 
A 1 30  ASN 30  27  27  ASN ASN A . n 
A 1 31  SER 31  28  28  SER SER A . n 
A 1 32  SER 32  29  29  SER SER A . n 
A 1 33  ASP 33  30  30  ASP ASP A . n 
A 1 34  VAL 34  31  31  VAL VAL A . n 
A 1 35  ARG 35  32  32  ARG ARG A . n 
A 1 36  GLN 36  33  33  GLN GLN A . n 
A 1 37  LEU 37  34  34  LEU LEU A . n 
A 1 38  GLY 38  35  35  GLY GLY A . n 
A 1 39  ARG 39  36  36  ARG ARG A . n 
A 1 40  PHE 40  37  37  PHE PHE A . n 
A 1 41  LEU 41  38  38  LEU LEU A . n 
A 1 42  GLN 42  39  39  GLN GLN A . n 
A 1 43  LYS 43  40  40  LYS LYS A . n 
A 1 44  LYS 44  41  41  LYS LYS A . n 
A 1 45  GLY 45  42  42  GLY GLY A . n 
A 1 46  TYR 46  43  43  TYR TYR A . n 
A 1 47  THR 47  44  44  THR THR A . n 
A 1 48  SER 48  45  45  SER SER A . n 
A 1 49  TYR 49  46  46  TYR TYR A . n 
A 1 50  ALA 50  47  47  ALA ALA A . n 
A 1 51  PRO 51  48  48  PRO PRO A . n 
A 1 52  GLN 52  49  49  GLN GLN A . n 
A 1 53  TYR 53  50  50  TYR TYR A . n 
A 1 54  GLU 54  51  51  GLU GLU A . n 
A 1 55  GLY 55  52  52  GLY GLY A . n 
A 1 56  HIS 56  53  53  HIS HIS A . n 
A 1 57  ALA 57  54  54  ALA ALA A . n 
A 1 58  ALA 58  55  55  ALA ALA A . n 
A 1 59  PRO 59  56  56  PRO PRO A . n 
A 1 60  PRO 60  57  57  PRO PRO A . n 
A 1 61  ASP 61  58  58  ASP ASP A . n 
A 1 62  GLU 62  59  59  GLU GLU A . n 
A 1 63  ILE 63  60  60  ILE ILE A . n 
A 1 64  LEU 64  61  61  LEU LEU A . n 
A 1 65  LYS 65  62  62  LYS LYS A . n 
A 1 66  SER 66  63  63  SER SER A . n 
A 1 67  SER 67  64  64  SER SER A . n 
A 1 68  PRO 68  65  65  PRO PRO A . n 
A 1 69  PHE 69  66  66  PHE PHE A . n 
A 1 70  VAL 70  67  67  VAL VAL A . n 
A 1 71  TRP 71  68  68  TRP TRP A . n 
A 1 72  PHE 72  69  69  PHE PHE A . n 
A 1 73  LYS 73  70  70  LYS LYS A . n 
A 1 74  ASP 74  71  71  ASP ASP A . n 
A 1 75  ALA 75  72  72  ALA ALA A . n 
A 1 76  LEU 76  73  73  LEU LEU A . n 
A 1 77  ASP 77  74  74  ASP ASP A . n 
A 1 78  GLY 78  75  75  GLY GLY A . n 
A 1 79  TYR 79  76  76  TYR TYR A . n 
A 1 80  ASP 80  77  77  ASP ASP A . n 
A 1 81  TYR 81  78  78  TYR TYR A . n 
A 1 82  LEU 82  79  79  LEU LEU A . n 
A 1 83  VAL 83  80  80  VAL VAL A . n 
A 1 84  GLU 84  81  81  GLU GLU A . n 
A 1 85  GLN 85  82  82  GLN GLN A . n 
A 1 86  GLY 86  83  83  GLY GLY A . n 
A 1 87  TYR 87  84  84  TYR TYR A . n 
A 1 88  ASP 88  85  85  ASP ASP A . n 
A 1 89  GLU 89  86  86  GLU GLU A . n 
A 1 90  ILE 90  87  87  ILE ILE A . n 
A 1 91  VAL 91  88  88  VAL VAL A . n 
A 1 92  VAL 92  89  89  VAL VAL A . n 
A 1 93  ALA 93  90  90  ALA ALA A . n 
A 1 94  GLY 94  91  91  GLY GLY A . n 
A 1 95  LEU 95  92  92  LEU LEU A . n 
A 1 96  SER 96  93  93  SER SER A . n 
A 1 97  LEU 97  94  94  LEU LEU A . n 
A 1 98  GLY 98  95  95  GLY GLY A . n 
A 1 99  GLY 99  96  96  GLY GLY A . n 
A 1 100 ASP 100 97  97  ASP ASP A . n 
A 1 101 PHE 101 98  98  PHE PHE A . n 
A 1 102 ALA 102 99  99  ALA ALA A . n 
A 1 103 LEU 103 100 100 LEU LEU A . n 
A 1 104 LYS 104 101 101 LYS LYS A . n 
A 1 105 LEU 105 102 102 LEU LEU A . n 
A 1 106 SER 106 103 103 SER SER A . n 
A 1 107 LEU 107 104 104 LEU LEU A . n 
A 1 108 ASN 108 105 105 ASN ASN A . n 
A 1 109 ARG 109 106 106 ARG ARG A . n 
A 1 110 ASP 110 107 107 ASP ASP A . n 
A 1 111 VAL 111 108 108 VAL VAL A . n 
A 1 112 LYS 112 109 109 LYS LYS A . n 
A 1 113 GLY 113 110 110 GLY GLY A . n 
A 1 114 ILE 114 111 111 ILE ILE A . n 
A 1 115 VAL 115 112 112 VAL VAL A . n 
A 1 116 THR 116 113 113 THR THR A . n 
A 1 117 MET 117 114 114 MET MET A . n 
A 1 118 CYS 118 115 115 CYS CYS A . n 
A 1 119 ALA 119 116 116 ALA ALA A . n 
A 1 120 PRO 120 117 117 PRO PRO A . n 
A 1 121 MET 121 118 118 MET MET A . n 
A 1 122 GLY 122 119 119 GLY GLY A . n 
A 1 123 GLY 123 120 120 GLY GLY A . n 
A 1 124 LYS 124 121 121 LYS LYS A . n 
A 1 125 THR 125 122 122 THR THR A . n 
A 1 126 GLU 126 123 123 GLU GLU A . n 
A 1 127 GLY 127 124 124 GLY GLY A . n 
A 1 128 ALA 128 125 125 ALA ALA A . n 
A 1 129 ILE 129 126 126 ILE ILE A . n 
A 1 130 TYR 130 127 127 TYR TYR A . n 
A 1 131 GLU 131 128 128 GLU GLU A . n 
A 1 132 GLY 132 129 129 GLY GLY A . n 
A 1 133 PHE 133 130 130 PHE PHE A . n 
A 1 134 LEU 134 131 131 LEU LEU A . n 
A 1 135 GLU 135 132 132 GLU GLU A . n 
A 1 136 TYR 136 133 133 TYR TYR A . n 
A 1 137 ALA 137 134 134 ALA ALA A . n 
A 1 138 ARG 138 135 135 ARG ARG A . n 
A 1 139 ASN 139 136 136 ASN ASN A . n 
A 1 140 PHE 140 137 137 PHE PHE A . n 
A 1 141 LYS 141 138 138 LYS LYS A . n 
A 1 142 LYS 142 139 139 LYS LYS A . n 
A 1 143 TYR 143 140 140 TYR TYR A . n 
A 1 144 GLU 144 141 141 GLU GLU A . n 
A 1 145 GLY 145 142 142 GLY GLY A . n 
A 1 146 LYS 146 143 143 LYS LYS A . n 
A 1 147 ASP 147 144 144 ASP ASP A . n 
A 1 148 GLN 148 145 145 GLN GLN A . n 
A 1 149 GLU 149 146 146 GLU GLU A . n 
A 1 150 THR 150 147 147 THR THR A . n 
A 1 151 ILE 151 148 148 ILE ILE A . n 
A 1 152 ASP 152 149 149 ASP ASP A . n 
A 1 153 ASN 153 150 150 ASN ASN A . n 
A 1 154 GLU 154 151 151 GLU GLU A . n 
A 1 155 MET 155 152 152 MET MET A . n 
A 1 156 ASP 156 153 153 ASP ASP A . n 
A 1 157 HIS 157 154 154 HIS HIS A . n 
A 1 158 PHE 158 155 155 PHE PHE A . n 
A 1 159 LYS 159 156 156 LYS LYS A . n 
A 1 160 PRO 160 157 157 PRO PRO A . n 
A 1 161 THR 161 158 158 THR THR A . n 
A 1 162 GLU 162 159 159 GLU GLU A . n 
A 1 163 THR 163 160 160 THR THR A . n 
A 1 164 LEU 164 161 161 LEU LEU A . n 
A 1 165 LYS 165 162 162 LYS LYS A . n 
A 1 166 GLU 166 163 163 GLU GLU A . n 
A 1 167 LEU 167 164 164 LEU LEU A . n 
A 1 168 SER 168 165 165 SER SER A . n 
A 1 169 GLU 169 166 166 GLU GLU A . n 
A 1 170 ALA 170 167 167 ALA ALA A . n 
A 1 171 LEU 171 168 168 LEU LEU A . n 
A 1 172 ASP 172 169 169 ASP ASP A . n 
A 1 173 THR 173 170 170 THR THR A . n 
A 1 174 ILE 174 171 171 ILE ILE A . n 
A 1 175 LYS 175 172 172 LYS LYS A . n 
A 1 176 GLU 176 173 173 GLU GLU A . n 
A 1 177 GLN 177 174 174 GLN GLN A . n 
A 1 178 VAL 178 175 175 VAL VAL A . n 
A 1 179 ASP 179 176 176 ASP ASP A . n 
A 1 180 GLU 180 177 177 GLU GLU A . n 
A 1 181 VAL 181 178 178 VAL VAL A . n 
A 1 182 LEU 182 179 179 LEU LEU A . n 
A 1 183 ASP 183 180 180 ASP ASP A . n 
A 1 184 PRO 184 181 181 PRO PRO A . n 
A 1 185 ILE 185 182 182 ILE ILE A . n 
A 1 186 LEU 186 183 183 LEU LEU A . n 
A 1 187 VAL 187 184 184 VAL VAL A . n 
A 1 188 ILE 188 185 185 ILE ILE A . n 
A 1 189 GLN 189 186 186 GLN GLN A . n 
A 1 190 ALA 190 187 187 ALA ALA A . n 
A 1 191 GLU 191 188 188 GLU GLU A . n 
A 1 192 ASN 192 189 189 ASN ASN A . n 
A 1 193 ASP 193 190 190 ASP ASP A . n 
A 1 194 ASN 194 191 191 ASN ASN A . n 
A 1 195 MET 195 192 192 MET MET A . n 
A 1 196 ILE 196 193 193 ILE ILE A . n 
A 1 197 ASP 197 194 194 ASP ASP A . n 
A 1 198 PRO 198 195 195 PRO PRO A . n 
A 1 199 GLN 199 196 196 GLN GLN A . n 
A 1 200 SER 200 197 197 SER SER A . n 
A 1 201 ALA 201 198 198 ALA ALA A . n 
A 1 202 ASN 202 199 199 ASN ASN A . n 
A 1 203 TYR 203 200 200 TYR TYR A . n 
A 1 204 ILE 204 201 201 ILE ILE A . n 
A 1 205 TYR 205 202 202 TYR TYR A . n 
A 1 206 ASP 206 203 203 ASP ASP A . n 
A 1 207 HIS 207 204 204 HIS HIS A . n 
A 1 208 VAL 208 205 205 VAL VAL A . n 
A 1 209 ASP 209 206 206 ASP ASP A . n 
A 1 210 SER 210 207 207 SER SER A . n 
A 1 211 ASP 211 208 208 ASP ASP A . n 
A 1 212 ASP 212 209 209 ASP ASP A . n 
A 1 213 LYS 213 210 210 LYS LYS A . n 
A 1 214 ASN 214 211 211 ASN ASN A . n 
A 1 215 ILE 215 212 212 ILE ILE A . n 
A 1 216 LYS 216 213 213 LYS LYS A . n 
A 1 217 TRP 217 214 214 TRP TRP A . n 
A 1 218 TYR 218 215 215 TYR TYR A . n 
A 1 219 SER 219 216 216 SER SER A . n 
A 1 220 GLU 220 217 217 GLU GLU A . n 
A 1 221 SER 221 218 218 SER SER A . n 
A 1 222 GLY 222 219 219 GLY GLY A . n 
A 1 223 HIS 223 220 220 HIS HIS A . n 
A 1 224 VAL 224 221 221 VAL VAL A . n 
A 1 225 ILE 225 222 222 ILE ILE A . n 
A 1 226 THR 226 223 223 THR THR A . n 
A 1 227 ILE 227 224 224 ILE ILE A . n 
A 1 228 ASP 228 225 225 ASP ASP A . n 
A 1 229 LYS 229 226 226 LYS LYS A . n 
A 1 230 GLU 230 227 227 GLU GLU A . n 
A 1 231 LYS 231 228 228 LYS LYS A . n 
A 1 232 GLU 232 229 229 GLU GLU A . n 
A 1 233 GLN 233 230 230 GLN GLN A . n 
A 1 234 VAL 234 231 231 VAL VAL A . n 
A 1 235 PHE 235 232 232 PHE PHE A . n 
A 1 236 GLU 236 233 233 GLU GLU A . n 
A 1 237 ASP 237 234 234 ASP ASP A . n 
A 1 238 ILE 238 235 235 ILE ILE A . n 
A 1 239 TYR 239 236 236 TYR TYR A . n 
A 1 240 GLN 240 237 237 GLN GLN A . n 
A 1 241 PHE 241 238 238 PHE PHE A . n 
A 1 242 LEU 242 239 239 LEU LEU A . n 
A 1 243 GLU 243 240 240 GLU GLU A . n 
A 1 244 SER 244 241 241 SER SER A . n 
A 1 245 LEU 245 242 242 LEU LEU A . n 
A 1 246 ASP 246 243 243 ASP ASP A . n 
A 1 247 TRP 247 244 244 TRP TRP A . n 
A 1 248 SER 248 245 245 SER SER A . n 
A 1 249 GLU 249 246 246 GLU GLU A . n 
# 
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 
B 2 CA  1   301 1   CA  CA  A . 
C 2 CA  1   302 2   CA  CA  A . 
D 2 CA  1   303 3   CA  CA  A . 
E 2 CA  1   304 4   CA  CA  A . 
F 3 HOH 1   401 14  HOH HOH A . 
F 3 HOH 2   402 102 HOH HOH A . 
F 3 HOH 3   403 65  HOH HOH A . 
F 3 HOH 4   404 49  HOH HOH A . 
F 3 HOH 5   405 30  HOH HOH A . 
F 3 HOH 6   406 150 HOH HOH A . 
F 3 HOH 7   407 155 HOH HOH A . 
F 3 HOH 8   408 60  HOH HOH A . 
F 3 HOH 9   409 105 HOH HOH A . 
F 3 HOH 10  410 50  HOH HOH A . 
F 3 HOH 11  411 4   HOH HOH A . 
F 3 HOH 12  412 149 HOH HOH A . 
F 3 HOH 13  413 88  HOH HOH A . 
F 3 HOH 14  414 74  HOH HOH A . 
F 3 HOH 15  415 34  HOH HOH A . 
F 3 HOH 16  416 46  HOH HOH A . 
F 3 HOH 17  417 114 HOH HOH A . 
F 3 HOH 18  418 16  HOH HOH A . 
F 3 HOH 19  419 145 HOH HOH A . 
F 3 HOH 20  420 72  HOH HOH A . 
F 3 HOH 21  421 56  HOH HOH A . 
F 3 HOH 22  422 156 HOH HOH A . 
F 3 HOH 23  423 64  HOH HOH A . 
F 3 HOH 24  424 31  HOH HOH A . 
F 3 HOH 25  425 127 HOH HOH A . 
F 3 HOH 26  426 43  HOH HOH A . 
F 3 HOH 27  427 136 HOH HOH A . 
F 3 HOH 28  428 98  HOH HOH A . 
F 3 HOH 29  429 82  HOH HOH A . 
F 3 HOH 30  430 146 HOH HOH A . 
F 3 HOH 31  431 27  HOH HOH A . 
F 3 HOH 32  432 24  HOH HOH A . 
F 3 HOH 33  433 13  HOH HOH A . 
F 3 HOH 34  434 44  HOH HOH A . 
F 3 HOH 35  435 29  HOH HOH A . 
F 3 HOH 36  436 112 HOH HOH A . 
F 3 HOH 37  437 9   HOH HOH A . 
F 3 HOH 38  438 132 HOH HOH A . 
F 3 HOH 39  439 11  HOH HOH A . 
F 3 HOH 40  440 26  HOH HOH A . 
F 3 HOH 41  441 79  HOH HOH A . 
F 3 HOH 42  442 83  HOH HOH A . 
F 3 HOH 43  443 124 HOH HOH A . 
F 3 HOH 44  444 45  HOH HOH A . 
F 3 HOH 45  445 37  HOH HOH A . 
F 3 HOH 46  446 141 HOH HOH A . 
F 3 HOH 47  447 59  HOH HOH A . 
F 3 HOH 48  448 118 HOH HOH A . 
F 3 HOH 49  449 48  HOH HOH A . 
F 3 HOH 50  450 95  HOH HOH A . 
F 3 HOH 51  451 35  HOH HOH A . 
F 3 HOH 52  452 23  HOH HOH A . 
F 3 HOH 53  453 40  HOH HOH A . 
F 3 HOH 54  454 52  HOH HOH A . 
F 3 HOH 55  455 17  HOH HOH A . 
F 3 HOH 56  456 6   HOH HOH A . 
F 3 HOH 57  457 87  HOH HOH A . 
F 3 HOH 58  458 32  HOH HOH A . 
F 3 HOH 59  459 47  HOH HOH A . 
F 3 HOH 60  460 139 HOH HOH A . 
F 3 HOH 61  461 97  HOH HOH A . 
F 3 HOH 62  462 58  HOH HOH A . 
F 3 HOH 63  463 148 HOH HOH A . 
F 3 HOH 64  464 12  HOH HOH A . 
F 3 HOH 65  465 61  HOH HOH A . 
F 3 HOH 66  466 5   HOH HOH A . 
F 3 HOH 67  467 152 HOH HOH A . 
F 3 HOH 68  468 20  HOH HOH A . 
F 3 HOH 69  469 18  HOH HOH A . 
F 3 HOH 70  470 8   HOH HOH A . 
F 3 HOH 71  471 157 HOH HOH A . 
F 3 HOH 72  472 36  HOH HOH A . 
F 3 HOH 73  473 129 HOH HOH A . 
F 3 HOH 74  474 28  HOH HOH A . 
F 3 HOH 75  475 94  HOH HOH A . 
F 3 HOH 76  476 78  HOH HOH A . 
F 3 HOH 77  477 147 HOH HOH A . 
F 3 HOH 78  478 33  HOH HOH A . 
F 3 HOH 79  479 21  HOH HOH A . 
F 3 HOH 80  480 67  HOH HOH A . 
F 3 HOH 81  481 62  HOH HOH A . 
F 3 HOH 82  482 134 HOH HOH A . 
F 3 HOH 83  483 125 HOH HOH A . 
F 3 HOH 84  484 71  HOH HOH A . 
F 3 HOH 85  485 104 HOH HOH A . 
F 3 HOH 86  486 55  HOH HOH A . 
F 3 HOH 87  487 154 HOH HOH A . 
F 3 HOH 88  488 22  HOH HOH A . 
F 3 HOH 89  489 101 HOH HOH A . 
F 3 HOH 90  490 73  HOH HOH A . 
F 3 HOH 91  491 39  HOH HOH A . 
F 3 HOH 92  492 144 HOH HOH A . 
F 3 HOH 93  493 10  HOH HOH A . 
F 3 HOH 94  494 19  HOH HOH A . 
F 3 HOH 95  495 15  HOH HOH A . 
F 3 HOH 96  496 80  HOH HOH A . 
F 3 HOH 97  497 53  HOH HOH A . 
F 3 HOH 98  498 25  HOH HOH A . 
F 3 HOH 99  499 111 HOH HOH A . 
F 3 HOH 100 500 38  HOH HOH A . 
F 3 HOH 101 501 66  HOH HOH A . 
F 3 HOH 102 502 106 HOH HOH A . 
F 3 HOH 103 503 68  HOH HOH A . 
F 3 HOH 104 504 92  HOH HOH A . 
F 3 HOH 105 505 75  HOH HOH A . 
F 3 HOH 106 506 116 HOH HOH A . 
F 3 HOH 107 507 77  HOH HOH A . 
F 3 HOH 108 508 51  HOH HOH A . 
F 3 HOH 109 509 41  HOH HOH A . 
F 3 HOH 110 510 76  HOH HOH A . 
F 3 HOH 111 511 103 HOH HOH A . 
F 3 HOH 112 512 109 HOH HOH A . 
F 3 HOH 113 513 90  HOH HOH A . 
F 3 HOH 114 514 63  HOH HOH A . 
F 3 HOH 115 515 89  HOH HOH A . 
F 3 HOH 116 516 54  HOH HOH A . 
F 3 HOH 117 517 113 HOH HOH A . 
F 3 HOH 118 518 85  HOH HOH A . 
F 3 HOH 119 519 153 HOH HOH A . 
F 3 HOH 120 520 122 HOH HOH A . 
F 3 HOH 121 521 57  HOH HOH A . 
F 3 HOH 122 522 142 HOH HOH A . 
F 3 HOH 123 523 119 HOH HOH A . 
F 3 HOH 124 524 140 HOH HOH A . 
F 3 HOH 125 525 91  HOH HOH A . 
F 3 HOH 126 526 120 HOH HOH A . 
F 3 HOH 127 527 42  HOH HOH A . 
F 3 HOH 128 528 99  HOH HOH A . 
F 3 HOH 129 529 100 HOH HOH A . 
F 3 HOH 130 530 107 HOH HOH A . 
F 3 HOH 131 531 110 HOH HOH A . 
F 3 HOH 132 532 84  HOH HOH A . 
F 3 HOH 133 533 151 HOH HOH A . 
F 3 HOH 134 534 130 HOH HOH A . 
F 3 HOH 135 535 115 HOH HOH A . 
F 3 HOH 136 536 81  HOH HOH A . 
F 3 HOH 137 537 108 HOH HOH A . 
F 3 HOH 138 538 117 HOH HOH A . 
F 3 HOH 139 539 123 HOH HOH A . 
F 3 HOH 140 540 138 HOH HOH A . 
F 3 HOH 141 541 93  HOH HOH A . 
F 3 HOH 142 542 70  HOH HOH A . 
F 3 HOH 143 543 96  HOH HOH A . 
F 3 HOH 144 544 137 HOH HOH A . 
F 3 HOH 145 545 135 HOH HOH A . 
# 
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       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? 0.7.8       2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? 2.8.3       4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9C0L 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     60.898 
_cell.length_a_esd                 ? 
_cell.length_b                     60.898 
_cell.length_b_esd                 ? 
_cell.length_c                     164.513 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9C0L 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                96 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 43 21 2' 
_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                   9C0L 
_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             2.69 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.30 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.5 
_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    
;0.3 uL 9.1 mg/mL FphH (10mM HEPES pH 7.6, 100mM NaCl) were mixed with 0.15 uL of reservoir solution. Sitting drop reservoir contained 200mM Calcium acetate hydrate, 100mM Tris pH 8.5, 25 % w/v PEG 2000 MME. Crystal was frozen in a solution of ~25% Ethylenglycol, 75% reservoir.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-04-27 
_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   0.954 
_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                        'AUSTRALIAN SYNCHROTRON BEAMLINE MX2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.954 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MX2 
_diffrn_source.pdbx_synchrotron_site       'Australian Synchrotron' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9C0L 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.79 
_reflns.d_resolution_low                               48.94 
_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                                     30069 
_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                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                19.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.01 
_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                                0.116 
_reflns.pdbx_Rpim_I_all                                0.027 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       576148 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.113 
_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                                    1.79 
_reflns_shell.d_res_low                                     1.83 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           30217 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1622 
_reflns_shell.percent_possible_obs                          94.7 
_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                               18.6 
_reflns_shell.pdbx_chi_squared                              0.94 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.4 
_reflns_shell.pdbx_Rrim_I_all                               2.636 
_reflns_shell.pdbx_Rpim_I_all                               0.593 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.677 
_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                                  2.565 
_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]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_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                                 9C0L 
_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                            1.79 
_refine.ls_d_res_low                             41.66 
_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                     29956 
_refine.ls_number_reflns_R_free                  1491 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.56 
_refine.ls_percent_reflns_R_free                 4.98 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1857 
_refine.ls_R_factor_R_free                       0.2143 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1842 
_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                    'FLAT BULK SOLVENT MODEL' 
_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                          1.34 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 22.27 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.21 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1959 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         4 
_refine_hist.number_atoms_solvent             145 
_refine_hist.number_atoms_total               2108 
_refine_hist.d_res_high                       1.79 
_refine_hist.d_res_low                        41.66 
# 
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' ? 0.007 ? 2014 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.888 ? 2725 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 5.437 ? 263  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.059 ? 285  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006 ? 360  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.79 1.85  . . 121 2428 96.00  . . . . 0.3329 . . . . . . . . . . . 0.3436 
'X-RAY DIFFRACTION' 1.85 1.91  . . 142 2529 100.00 . . . . 0.2538 . . . . . . . . . . . 0.3035 
'X-RAY DIFFRACTION' 1.91 1.99  . . 121 2542 100.00 . . . . 0.2145 . . . . . . . . . . . 0.2540 
'X-RAY DIFFRACTION' 1.99 2.08  . . 142 2544 100.00 . . . . 0.2003 . . . . . . . . . . . 0.2480 
'X-RAY DIFFRACTION' 2.08 2.19  . . 138 2570 100.00 . . . . 0.1909 . . . . . . . . . . . 0.2341 
'X-RAY DIFFRACTION' 2.19 2.33  . . 138 2558 100.00 . . . . 0.1631 . . . . . . . . . . . 0.1935 
'X-RAY DIFFRACTION' 2.33 2.51  . . 127 2583 100.00 . . . . 0.1790 . . . . . . . . . . . 0.2090 
'X-RAY DIFFRACTION' 2.51 2.76  . . 140 2592 100.00 . . . . 0.1824 . . . . . . . . . . . 0.2391 
'X-RAY DIFFRACTION' 2.76 3.16  . . 122 2639 100.00 . . . . 0.1909 . . . . . . . . . . . 0.2197 
'X-RAY DIFFRACTION' 3.16 3.98  . . 144 2657 100.00 . . . . 0.1821 . . . . . . . . . . . 0.2030 
'X-RAY DIFFRACTION' 3.98 41.66 . . 156 2823 100.00 . . . . 0.1673 . . . . . . . . . . . 0.1941 
# 
_struct.entry_id                     9C0L 
_struct.title                        
'FphH, Staphylococcus aureus fluorophosphonate-binding serine hydrolases H, apo crystal form 2' 
_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        9C0L 
_struct_keywords.text            
'FphH, Staphylococcus aureus, S. aureus, fluorophosphonate-binding, serine hydrolases, lipase, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 2 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A0D6HZA6_STAAU 
_struct_ref.pdbx_db_accession          A0A0D6HZA6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MQIKLPKPFFFEEGKRAVLLLHGFTGNSSDVRQLGRFLQKKGYTSYAPQYEGHAAPPDEILKSSPFVWFKDALDGYDYLV
EQGYDEIVVAGLSLGGDFALKLSLNRDVKGIVTMCAPMGGKTEGAIYEGFLEYARNFKKYEGKDQETIDNEMDHFKPTET
LKELSEALDTIKEQVDEVLDPILVIQAENDNMIDPQSANYIYDHVDSDDKNIKWYSESGHVITIDKEKEQVFEDIYQFLE
SLDWSE
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9C0L 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 4 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 249 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A0D6HZA6 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  246 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       246 
# 
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 9C0L GLY A 1 ? UNP A0A0D6HZA6 ? ? 'expression tag' -2 1 
1 9C0L PRO A 2 ? UNP A0A0D6HZA6 ? ? 'expression tag' -1 2 
1 9C0L GLY A 3 ? UNP A0A0D6HZA6 ? ? 'expression tag' 0  3 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_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 
# 
_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 ASN A 30  ? ASP A 33  ? ASN A 27  ASP A 30  5 ? 4  
HELX_P HELX_P2  AA2 VAL A 34  ? LYS A 44  ? VAL A 31  LYS A 41  1 ? 11 
HELX_P HELX_P3  AA3 PRO A 60  ? LYS A 65  ? PRO A 57  LYS A 62  1 ? 6  
HELX_P HELX_P4  AA4 SER A 67  ? GLN A 85  ? SER A 64  GLN A 82  1 ? 19 
HELX_P HELX_P5  AA5 SER A 96  ? LEU A 107 ? SER A 93  LEU A 104 1 ? 12 
HELX_P HELX_P6  AA6 GLY A 127 ? GLU A 144 ? GLY A 124 GLU A 141 1 ? 18 
HELX_P HELX_P7  AA7 ASP A 147 ? HIS A 157 ? ASP A 144 HIS A 154 1 ? 11 
HELX_P HELX_P8  AA8 PRO A 160 ? VAL A 178 ? PRO A 157 VAL A 175 1 ? 19 
HELX_P HELX_P9  AA9 ASP A 179 ? VAL A 181 ? ASP A 176 VAL A 178 5 ? 3  
HELX_P HELX_P10 AB1 GLN A 199 ? VAL A 208 ? GLN A 196 VAL A 205 1 ? 10 
HELX_P HELX_P11 AB2 GLU A 230 ? SER A 244 ? GLU A 227 SER A 241 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A GLN 85  OE1 ? ? ? 1_555 D CA  . CA ? ? A GLN 82  A CA  303 1_555 ? ? ? ? ? ? ? 2.249 ? ? 
metalc2  metalc ? ? A GLU 176 O   ? ? ? 1_555 E CA  . CA ? ? A GLU 173 A CA  304 1_555 ? ? ? ? ? ? ? 2.411 ? ? 
metalc3  metalc ? ? A ASP 179 OD1 ? ? ? 1_555 E CA  . CA ? ? A ASP 176 A CA  304 1_555 ? ? ? ? ? ? ? 2.421 ? ? 
metalc4  metalc ? ? A ASP 179 OD2 ? ? ? 1_555 E CA  . CA ? ? A ASP 176 A CA  304 1_555 ? ? ? ? ? ? ? 2.584 ? ? 
metalc5  metalc ? ? A ASP 209 OD1 ? ? ? 1_555 C CA  . CA ? ? A ASP 206 A CA  302 1_555 ? ? ? ? ? ? ? 2.560 ? ? 
metalc6  metalc ? ? A ASP 212 OD1 ? ? ? 1_555 B CA  . CA ? ? A ASP 209 A CA  301 1_555 ? ? ? ? ? ? ? 2.414 ? ? 
metalc7  metalc ? ? A ASN 214 OD1 B ? ? 1_555 B CA  . CA ? ? A ASN 211 A CA  301 1_555 ? ? ? ? ? ? ? 2.897 ? ? 
metalc8  metalc ? ? B CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  301 A HOH 418 1_555 ? ? ? ? ? ? ? 2.313 ? ? 
metalc9  metalc ? ? B CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  301 A HOH 420 1_555 ? ? ? ? ? ? ? 2.347 ? ? 
metalc10 metalc ? ? B CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  301 A HOH 420 8_555 ? ? ? ? ? ? ? 2.424 ? ? 
metalc11 metalc ? ? B CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  301 A HOH 421 1_555 ? ? ? ? ? ? ? 2.251 ? ? 
metalc12 metalc ? ? B CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  301 A HOH 466 1_555 ? ? ? ? ? ? ? 2.428 ? ? 
metalc13 metalc ? ? B CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  301 A HOH 466 8_555 ? ? ? ? ? ? ? 2.437 ? ? 
metalc14 metalc ? ? B CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  301 A HOH 511 1_555 ? ? ? ? ? ? ? 2.281 ? ? 
metalc15 metalc ? ? C CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  302 A HOH 406 8_555 ? ? ? ? ? ? ? 2.337 ? ? 
metalc16 metalc ? ? C CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  302 A HOH 410 1_555 ? ? ? ? ? ? ? 2.304 ? ? 
metalc17 metalc ? ? C CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  302 A HOH 412 8_555 ? ? ? ? ? ? ? 2.275 ? ? 
metalc18 metalc ? ? C CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  302 A HOH 463 8_555 ? ? ? ? ? ? ? 2.360 ? ? 
metalc19 metalc ? ? C CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  302 A HOH 486 1_555 ? ? ? ? ? ? ? 2.305 ? ? 
metalc20 metalc ? ? C CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  302 A HOH 520 1_555 ? ? ? ? ? ? ? 2.257 ? ? 
metalc21 metalc ? ? D CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  303 A HOH 405 1_555 ? ? ? ? ? ? ? 2.455 ? ? 
metalc22 metalc ? ? D CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  303 A HOH 440 1_555 ? ? ? ? ? ? ? 2.377 ? ? 
metalc23 metalc ? ? D CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  303 A HOH 514 1_555 ? ? ? ? ? ? ? 2.503 ? ? 
metalc24 metalc ? ? D CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  303 A HOH 516 1_555 ? ? ? ? ? ? ? 2.432 ? ? 
metalc25 metalc ? ? D CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  303 A HOH 523 1_555 ? ? ? ? ? ? ? 2.387 ? ? 
metalc26 metalc ? ? D CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  303 A HOH 533 6_545 ? ? ? ? ? ? ? 2.353 ? ? 
metalc27 metalc ? ? E CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  304 A HOH 428 1_555 ? ? ? ? ? ? ? 2.388 ? ? 
metalc28 metalc ? ? E CA  .   CA  ? ? ? 1_555 F HOH . O  ? ? A CA  304 A HOH 502 1_555 ? ? ? ? ? ? ? 2.271 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OE1 ? A GLN 85  ? A GLN 82  ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 405 ? 1_555 96.2  ? 
2  OE1 ? A GLN 85  ? A GLN 82  ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 440 ? 1_555 84.9  ? 
3  O   ? F HOH .   ? A HOH 405 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 440 ? 1_555 79.2  ? 
4  OE1 ? A GLN 85  ? A GLN 82  ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 514 ? 1_555 81.9  ? 
5  O   ? F HOH .   ? A HOH 405 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 514 ? 1_555 60.9  ? 
6  O   ? F HOH .   ? A HOH 440 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 514 ? 1_555 136.0 ? 
7  OE1 ? A GLN 85  ? A GLN 82  ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 516 ? 1_555 84.5  ? 
8  O   ? F HOH .   ? A HOH 405 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 516 ? 1_555 152.3 ? 
9  O   ? F HOH .   ? A HOH 440 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 516 ? 1_555 73.2  ? 
10 O   ? F HOH .   ? A HOH 514 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 516 ? 1_555 145.7 ? 
11 OE1 ? A GLN 85  ? A GLN 82  ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 523 ? 1_555 96.8  ? 
12 O   ? F HOH .   ? A HOH 405 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 523 ? 1_555 135.1 ? 
13 O   ? F HOH .   ? A HOH 440 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 523 ? 1_555 144.6 ? 
14 O   ? F HOH .   ? A HOH 514 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 523 ? 1_555 78.8  ? 
15 O   ? F HOH .   ? A HOH 516 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 523 ? 1_555 71.8  ? 
16 OE1 ? A GLN 85  ? A GLN 82  ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 533 ? 6_545 171.0 ? 
17 O   ? F HOH .   ? A HOH 405 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 533 ? 6_545 82.9  ? 
18 O   ? F HOH .   ? A HOH 440 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 533 ? 6_545 86.2  ? 
19 O   ? F HOH .   ? A HOH 514 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 533 ? 6_545 105.2 ? 
20 O   ? F HOH .   ? A HOH 516 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 533 ? 6_545 92.2  ? 
21 O   ? F HOH .   ? A HOH 523 ? 1_555 CA ? D CA . ? A CA 303 ? 1_555 O   ? F HOH .   ? A HOH 533 ? 6_545 90.0  ? 
22 O   ? A GLU 176 ? A GLU 173 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 OD1 ? A ASP 179 ? A ASP 176 ? 1_555 91.0  ? 
23 O   ? A GLU 176 ? A GLU 173 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 OD2 ? A ASP 179 ? A ASP 176 ? 1_555 114.0 ? 
24 OD1 ? A ASP 179 ? A ASP 176 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 OD2 ? A ASP 179 ? A ASP 176 ? 1_555 51.5  ? 
25 O   ? A GLU 176 ? A GLU 173 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 O   ? F HOH .   ? A HOH 428 ? 1_555 117.5 ? 
26 OD1 ? A ASP 179 ? A ASP 176 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 O   ? F HOH .   ? A HOH 428 ? 1_555 98.5  ? 
27 OD2 ? A ASP 179 ? A ASP 176 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 O   ? F HOH .   ? A HOH 428 ? 1_555 119.9 ? 
28 O   ? A GLU 176 ? A GLU 173 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 O   ? F HOH .   ? A HOH 502 ? 1_555 78.1  ? 
29 OD1 ? A ASP 179 ? A ASP 176 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 O   ? F HOH .   ? A HOH 502 ? 1_555 168.9 ? 
30 OD2 ? A ASP 179 ? A ASP 176 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 O   ? F HOH .   ? A HOH 502 ? 1_555 131.3 ? 
31 O   ? F HOH .   ? A HOH 428 ? 1_555 CA ? E CA . ? A CA 304 ? 1_555 O   ? F HOH .   ? A HOH 502 ? 1_555 88.7  ? 
32 OD1 ? A ASP 209 ? A ASP 206 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 406 ? 8_555 146.5 ? 
33 OD1 ? A ASP 209 ? A ASP 206 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 410 ? 1_555 75.3  ? 
34 O   ? F HOH .   ? A HOH 406 ? 8_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 410 ? 1_555 74.7  ? 
35 OD1 ? A ASP 209 ? A ASP 206 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 412 ? 8_555 136.5 ? 
36 O   ? F HOH .   ? A HOH 406 ? 8_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 412 ? 8_555 76.9  ? 
37 O   ? F HOH .   ? A HOH 410 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 412 ? 8_555 138.1 ? 
38 OD1 ? A ASP 209 ? A ASP 206 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 463 ? 8_555 93.7  ? 
39 O   ? F HOH .   ? A HOH 406 ? 8_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 463 ? 8_555 97.9  ? 
40 O   ? F HOH .   ? A HOH 410 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 463 ? 8_555 84.6  ? 
41 O   ? F HOH .   ? A HOH 412 ? 8_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 463 ? 8_555 69.5  ? 
42 OD1 ? A ASP 209 ? A ASP 206 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 486 ? 1_555 71.5  ? 
43 O   ? F HOH .   ? A HOH 406 ? 8_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 486 ? 1_555 137.8 ? 
44 O   ? F HOH .   ? A HOH 410 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 486 ? 1_555 146.7 ? 
45 O   ? F HOH .   ? A HOH 412 ? 8_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 486 ? 1_555 70.6  ? 
46 O   ? F HOH .   ? A HOH 463 ? 8_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 486 ? 1_555 95.2  ? 
47 OD1 ? A ASP 209 ? A ASP 206 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 520 ? 1_555 84.4  ? 
48 O   ? F HOH .   ? A HOH 406 ? 8_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 520 ? 1_555 92.9  ? 
49 O   ? F HOH .   ? A HOH 410 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 520 ? 1_555 111.2 ? 
50 O   ? F HOH .   ? A HOH 412 ? 8_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 520 ? 1_555 100.2 ? 
51 O   ? F HOH .   ? A HOH 463 ? 8_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 520 ? 1_555 162.8 ? 
52 O   ? F HOH .   ? A HOH 486 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? F HOH .   ? A HOH 520 ? 1_555 67.9  ? 
53 OD1 ? A ASP 212 ? A ASP 209 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 OD1 B A ASN 214 ? A ASN 211 ? 1_555 131.0 ? 
54 OD1 ? A ASP 212 ? A ASP 209 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 418 ? 1_555 87.2  ? 
55 OD1 B A ASN 214 ? A ASN 211 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 418 ? 1_555 58.4  ? 
56 OD1 ? A ASP 212 ? A ASP 209 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 420 ? 1_555 137.7 ? 
57 OD1 B A ASN 214 ? A ASN 211 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 420 ? 1_555 58.4  ? 
58 O   ? F HOH .   ? A HOH 418 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 420 ? 1_555 116.8 ? 
59 OD1 ? A ASP 212 ? A ASP 209 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 420 ? 8_555 80.4  ? 
60 OD1 B A ASN 214 ? A ASN 211 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 420 ? 8_555 123.4 ? 
61 O   ? F HOH .   ? A HOH 418 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 420 ? 8_555 163.3 ? 
62 O   ? F HOH .   ? A HOH 420 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 420 ? 8_555 67.7  ? 
63 OD1 ? A ASP 212 ? A ASP 209 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 421 ? 1_555 80.1  ? 
64 OD1 B A ASN 214 ? A ASN 211 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 421 ? 1_555 136.5 ? 
65 O   ? F HOH .   ? A HOH 418 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 421 ? 1_555 102.3 ? 
66 O   ? F HOH .   ? A HOH 420 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 421 ? 1_555 122.9 ? 
67 O   ? F HOH .   ? A HOH 420 ? 8_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 421 ? 1_555 86.6  ? 
68 OD1 ? A ASP 212 ? A ASP 209 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 466 ? 1_555 70.6  ? 
69 OD1 B A ASN 214 ? A ASN 211 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 466 ? 1_555 77.2  ? 
70 O   ? F HOH .   ? A HOH 418 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 466 ? 1_555 93.2  ? 
71 O   ? F HOH .   ? A HOH 420 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 466 ? 1_555 73.5  ? 
72 O   ? F HOH .   ? A HOH 420 ? 8_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 466 ? 1_555 72.2  ? 
73 O   ? F HOH .   ? A HOH 421 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 466 ? 1_555 146.1 ? 
74 OD1 ? A ASP 212 ? A ASP 209 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 466 ? 8_555 70.7  ? 
75 OD1 B A ASN 214 ? A ASN 211 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 466 ? 8_555 77.2  ? 
76 O   ? F HOH .   ? A HOH 418 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 466 ? 8_555 93.4  ? 
77 O   ? F HOH .   ? A HOH 420 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 466 ? 8_555 73.4  ? 
78 O   ? F HOH .   ? A HOH 420 ? 8_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 466 ? 8_555 72.0  ? 
79 O   ? F HOH .   ? A HOH 421 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 466 ? 8_555 146.0 ? 
80 O   ? F HOH .   ? A HOH 466 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 466 ? 8_555 0.2   ? 
81 OD1 ? A ASP 212 ? A ASP 209 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 511 ? 1_555 151.1 ? 
82 OD1 B A ASN 214 ? A ASN 211 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 511 ? 1_555 71.7  ? 
83 O   ? F HOH .   ? A HOH 418 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 511 ? 1_555 93.9  ? 
84 O   ? F HOH .   ? A HOH 420 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 511 ? 1_555 66.3  ? 
85 O   ? F HOH .   ? A HOH 420 ? 8_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 511 ? 1_555 102.4 ? 
86 O   ? F HOH .   ? A HOH 421 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 511 ? 1_555 71.5  ? 
87 O   ? F HOH .   ? A HOH 466 ? 1_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 511 ? 1_555 137.9 ? 
88 O   ? F HOH .   ? A HOH 466 ? 8_555 CA ? B CA . ? A CA 301 ? 1_555 O   ? F HOH .   ? A HOH 511 ? 1_555 137.8 ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   7 
_struct_sheet.details          ? 
# 
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 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? 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 PHE A 12  ? PHE A 14  ? PHE A 9   PHE A 11  
AA1 2 THR A 47  ? ALA A 50  ? THR A 44  ALA A 47  
AA1 3 ALA A 20  ? LEU A 24  ? ALA A 17  LEU A 21  
AA1 4 ILE A 90  ? LEU A 95  ? ILE A 87  LEU A 92  
AA1 5 GLY A 113 ? MET A 117 ? GLY A 110 MET A 114 
AA1 6 ILE A 185 ? ALA A 190 ? ILE A 182 ALA A 187 
AA1 7 LYS A 213 ? TYR A 218 ? LYS A 210 TYR A 215 
# 
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 N PHE A 12  ? N PHE A 9   O ALA A 50  ? O ALA A 47  
AA1 2 3 O TYR A 49  ? O TYR A 46  N LEU A 23  ? N LEU A 20  
AA1 3 4 N LEU A 22  ? N LEU A 19  O ALA A 93  ? O ALA A 90  
AA1 4 5 N GLY A 94  ? N GLY A 91  O VAL A 115 ? O VAL A 112 
AA1 5 6 N THR A 116 ? N THR A 113 O ILE A 188 ? O ILE A 185 
AA1 6 7 N VAL A 187 ? N VAL A 184 O ASN A 214 ? O ASN A 211 
# 
_pdbx_entry_details.entry_id                   9C0L 
_pdbx_entry_details.has_ligand_of_interest     N 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 402 ? ? O A HOH 529 ? ? 2.17 
2 1 O A HOH 401 ? ? O A HOH 436 ? ? 2.19 
# 
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 GLU A 13  ? ? -128.66 -107.49 
2 1 SER A 63  ? ? -108.78 -155.60 
3 1 SER A 93  ? ? 62.74   -126.22 
4 1 ASN A 189 ? ? -103.27 47.08   
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     466 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   F 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 19.2626 -8.4004 19.2869 0.2501 ? -0.0260 ? 0.0120 ? 0.2434 ? 0.0233  ? 0.2215 ? 3.2233 ? -0.5638 ? 
-0.1242 ? 1.7468 ? 0.1066  ? 2.6253 ? 0.0639 ? 0.2809  ? 0.1837 ? -0.2002 ? -0.0072 ? -0.0251 ? -0.2330 ? 0.0124 ? -0.0540 ? 
2 'X-RAY DIFFRACTION' ? refined 19.8449 10.4303 14.1654 0.6460 ? 0.0147  ? 0.0604 ? 0.3664 ? 0.1047  ? 0.5860 ? 2.8899 ? 0.8296  ? 
-0.9983 ? 2.4477 ? -0.7638 ? 2.4698 ? 0.0665 ? 0.3512  ? 0.8349 ? -0.3800 ? 0.0858  ? -0.1720 ? -0.6591 ? 0.0156 ? -0.1328 ? 
3 'X-RAY DIFFRACTION' ? refined 18.2412 -5.5352 34.5591 0.2851 ? -0.0744 ? 0.0075 ? 0.2911 ? -0.0331 ? 0.2231 ? 3.4138 ? -1.4192 ? 
-0.6997 ? 1.7475 ? -0.4930 ? 2.7832 ? 0.0574 ? -0.2845 ? 0.2359 ? 0.0286  ? 0.0395  ? -0.1209 ? -0.3277 ? 0.2222 ? -0.0876 ? 
# 
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 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 4 through 124 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 125 through 177 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 178 through 246 )
;
# 
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 GLY -2 ? A GLY 1 
2 1 Y 1 A PRO -1 ? A PRO 2 
3 1 Y 1 A GLY 0  ? A GLY 3 
4 1 Y 1 A MET 1  ? A MET 4 
5 1 Y 1 A GLN 2  ? A GLN 5 
6 1 Y 1 A ILE 3  ? A ILE 6 
# 
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  
CA  CA   CA N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
PHE N    N  N N 251 
PHE CA   C  N S 252 
PHE C    C  N N 253 
PHE O    O  N N 254 
PHE CB   C  N N 255 
PHE CG   C  Y N 256 
PHE CD1  C  Y N 257 
PHE CD2  C  Y N 258 
PHE CE1  C  Y N 259 
PHE CE2  C  Y N 260 
PHE CZ   C  Y N 261 
PHE OXT  O  N N 262 
PHE H    H  N N 263 
PHE H2   H  N N 264 
PHE HA   H  N N 265 
PHE HB2  H  N N 266 
PHE HB3  H  N N 267 
PHE HD1  H  N N 268 
PHE HD2  H  N N 269 
PHE HE1  H  N N 270 
PHE HE2  H  N N 271 
PHE HZ   H  N N 272 
PHE HXT  H  N N 273 
PRO N    N  N N 274 
PRO CA   C  N S 275 
PRO C    C  N N 276 
PRO O    O  N N 277 
PRO CB   C  N N 278 
PRO CG   C  N N 279 
PRO CD   C  N N 280 
PRO OXT  O  N N 281 
PRO H    H  N N 282 
PRO HA   H  N N 283 
PRO HB2  H  N N 284 
PRO HB3  H  N N 285 
PRO HG2  H  N N 286 
PRO HG3  H  N N 287 
PRO HD2  H  N N 288 
PRO HD3  H  N N 289 
PRO HXT  H  N N 290 
SER N    N  N N 291 
SER CA   C  N S 292 
SER C    C  N N 293 
SER O    O  N N 294 
SER CB   C  N N 295 
SER OG   O  N N 296 
SER OXT  O  N N 297 
SER H    H  N N 298 
SER H2   H  N N 299 
SER HA   H  N N 300 
SER HB2  H  N N 301 
SER HB3  H  N N 302 
SER HG   H  N N 303 
SER HXT  H  N N 304 
THR N    N  N N 305 
THR CA   C  N S 306 
THR C    C  N N 307 
THR O    O  N N 308 
THR CB   C  N R 309 
THR OG1  O  N N 310 
THR CG2  C  N N 311 
THR OXT  O  N N 312 
THR H    H  N N 313 
THR H2   H  N N 314 
THR HA   H  N N 315 
THR HB   H  N N 316 
THR HG1  H  N N 317 
THR HG21 H  N N 318 
THR HG22 H  N N 319 
THR HG23 H  N N 320 
THR HXT  H  N N 321 
TRP N    N  N N 322 
TRP CA   C  N S 323 
TRP C    C  N N 324 
TRP O    O  N N 325 
TRP CB   C  N N 326 
TRP CG   C  Y N 327 
TRP CD1  C  Y N 328 
TRP CD2  C  Y N 329 
TRP NE1  N  Y N 330 
TRP CE2  C  Y N 331 
TRP CE3  C  Y N 332 
TRP CZ2  C  Y N 333 
TRP CZ3  C  Y N 334 
TRP CH2  C  Y N 335 
TRP OXT  O  N N 336 
TRP H    H  N N 337 
TRP H2   H  N N 338 
TRP HA   H  N N 339 
TRP HB2  H  N N 340 
TRP HB3  H  N N 341 
TRP HD1  H  N N 342 
TRP HE1  H  N N 343 
TRP HE3  H  N N 344 
TRP HZ2  H  N N 345 
TRP HZ3  H  N N 346 
TRP HH2  H  N N 347 
TRP HXT  H  N N 348 
TYR N    N  N N 349 
TYR CA   C  N S 350 
TYR C    C  N N 351 
TYR O    O  N N 352 
TYR CB   C  N N 353 
TYR CG   C  Y N 354 
TYR CD1  C  Y N 355 
TYR CD2  C  Y N 356 
TYR CE1  C  Y N 357 
TYR CE2  C  Y N 358 
TYR CZ   C  Y N 359 
TYR OH   O  N N 360 
TYR OXT  O  N N 361 
TYR H    H  N N 362 
TYR H2   H  N N 363 
TYR HA   H  N N 364 
TYR HB2  H  N N 365 
TYR HB3  H  N N 366 
TYR HD1  H  N N 367 
TYR HD2  H  N N 368 
TYR HE1  H  N N 369 
TYR HE2  H  N N 370 
TYR HH   H  N N 371 
TYR HXT  H  N N 372 
VAL N    N  N N 373 
VAL CA   C  N S 374 
VAL C    C  N N 375 
VAL O    O  N N 376 
VAL CB   C  N N 377 
VAL CG1  C  N N 378 
VAL CG2  C  N N 379 
VAL OXT  O  N N 380 
VAL H    H  N N 381 
VAL H2   H  N N 382 
VAL HA   H  N N 383 
VAL HB   H  N N 384 
VAL HG11 H  N N 385 
VAL HG12 H  N N 386 
VAL HG13 H  N N 387 
VAL HG21 H  N N 388 
VAL HG22 H  N N 389 
VAL HG23 H  N N 390 
VAL HXT  H  N N 391 
# 
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 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'Capability Build Funding - New Zealand Synchrotron Group Ltd' 
_pdbx_audit_support.country                'New Zealand' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8FTP 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9C0L 
_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]   0.016421 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016421 
_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]   0.006079 
_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  
CA 
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   . LYS A 1 7   ? 36.837 -1.872  9.611  1.00 65.73  ? 4   LYS A N   1 
ATOM   2    C  CA  . LYS A 1 7   ? 35.596 -2.340  9.006  1.00 63.20  ? 4   LYS A CA  1 
ATOM   3    C  C   . LYS A 1 7   ? 34.424 -2.160  9.976  1.00 61.82  ? 4   LYS A C   1 
ATOM   4    O  O   . LYS A 1 7   ? 34.610 -1.758  11.124 1.00 63.65  ? 4   LYS A O   1 
ATOM   5    C  CB  . LYS A 1 7   ? 35.703 -3.811  8.596  1.00 65.11  ? 4   LYS A CB  1 
ATOM   6    C  CG  . LYS A 1 7   ? 36.796 -4.600  9.313  1.00 74.06  ? 4   LYS A CG  1 
ATOM   7    C  CD  . LYS A 1 7   ? 36.763 -6.077  8.912  1.00 79.07  ? 4   LYS A CD  1 
ATOM   8    C  CE  . LYS A 1 7   ? 37.722 -6.932  9.750  1.00 77.34  ? 4   LYS A CE  1 
ATOM   9    N  NZ  . LYS A 1 7   ? 37.343 -6.969  11.197 1.00 75.23  ? 4   LYS A NZ  1 
ATOM   10   N  N   . LEU A 1 8   ? 33.218 -2.489  9.518  1.00 55.94  ? 5   LEU A N   1 
ATOM   11   C  CA  . LEU A 1 8   ? 32.015 -2.268  10.309 1.00 43.92  ? 5   LEU A CA  1 
ATOM   12   C  C   . LEU A 1 8   ? 31.530 -3.573  10.932 1.00 43.37  ? 5   LEU A C   1 
ATOM   13   O  O   . LEU A 1 8   ? 31.721 -4.648  10.355 1.00 39.80  ? 5   LEU A O   1 
ATOM   14   C  CB  . LEU A 1 8   ? 30.914 -1.671  9.425  1.00 48.64  ? 5   LEU A CB  1 
ATOM   15   C  CG  . LEU A 1 8   ? 31.148 -0.176  9.140  1.00 55.63  ? 5   LEU A CG  1 
ATOM   16   C  CD1 . LEU A 1 8   ? 29.971 0.431   8.440  1.00 55.02  ? 5   LEU A CD1 1 
ATOM   17   C  CD2 . LEU A 1 8   ? 31.402 0.566   10.446 1.00 53.29  ? 5   LEU A CD2 1 
ATOM   18   N  N   . PRO A 1 9   ? 30.918 -3.514  12.115 1.00 41.39  ? 6   PRO A N   1 
ATOM   19   C  CA  . PRO A 1 9   ? 30.475 -4.745  12.778 1.00 39.04  ? 6   PRO A CA  1 
ATOM   20   C  C   . PRO A 1 9   ? 29.420 -5.504  11.988 1.00 39.19  ? 6   PRO A C   1 
ATOM   21   O  O   . PRO A 1 9   ? 28.660 -4.941  11.195 1.00 37.34  ? 6   PRO A O   1 
ATOM   22   C  CB  . PRO A 1 9   ? 29.909 -4.242  14.116 1.00 36.79  ? 6   PRO A CB  1 
ATOM   23   C  CG  . PRO A 1 9   ? 30.651 -2.961  14.355 1.00 41.19  ? 6   PRO A CG  1 
ATOM   24   C  CD  . PRO A 1 9   ? 30.710 -2.339  12.978 1.00 38.48  ? 6   PRO A CD  1 
ATOM   25   N  N   . LYS A 1 10  ? 29.384 -6.804  12.229 1.00 35.46  ? 7   LYS A N   1 
ATOM   26   C  CA  . LYS A 1 10  ? 28.461 -7.750  11.633 1.00 36.09  ? 7   LYS A CA  1 
ATOM   27   C  C   . LYS A 1 10  ? 27.744 -8.472  12.761 1.00 34.55  ? 7   LYS A C   1 
ATOM   28   O  O   . LYS A 1 10  ? 28.219 -8.474  13.904 1.00 34.67  ? 7   LYS A O   1 
ATOM   29   C  CB  . LYS A 1 10  ? 29.207 -8.778  10.764 1.00 33.14  ? 7   LYS A CB  1 
ATOM   30   C  CG  . LYS A 1 10  ? 29.792 -8.294  9.425  1.00 40.98  ? 7   LYS A CG  1 
ATOM   31   C  CD  . LYS A 1 10  ? 28.969 -7.218  8.734  1.00 45.69  ? 7   LYS A CD  1 
ATOM   32   C  CE  . LYS A 1 10  ? 29.730 -6.672  7.515  1.00 57.99  ? 7   LYS A CE  1 
ATOM   33   N  NZ  . LYS A 1 10  ? 29.663 -5.191  7.389  1.00 65.87  ? 7   LYS A NZ  1 
ATOM   34   N  N   . PRO A 1 11  ? 26.612 -9.112  12.483 1.00 32.60  ? 8   PRO A N   1 
ATOM   35   C  CA  . PRO A 1 11  ? 26.017 -10.007 13.485 1.00 28.07  ? 8   PRO A CA  1 
ATOM   36   C  C   . PRO A 1 11  ? 27.022 -11.062 13.928 1.00 33.27  ? 8   PRO A C   1 
ATOM   37   O  O   . PRO A 1 11  ? 27.958 -11.411 13.202 1.00 32.30  ? 8   PRO A O   1 
ATOM   38   C  CB  . PRO A 1 11  ? 24.833 -10.644 12.736 1.00 31.11  ? 8   PRO A CB  1 
ATOM   39   C  CG  . PRO A 1 11  ? 24.504 -9.663  11.652 1.00 32.61  ? 8   PRO A CG  1 
ATOM   40   C  CD  . PRO A 1 11  ? 25.816 -9.057  11.245 1.00 33.17  ? 8   PRO A CD  1 
ATOM   41   N  N   . PHE A 1 12  ? 26.838 -11.568 15.148 1.00 30.51  ? 9   PHE A N   1 
ATOM   42   C  CA  . PHE A 1 12  ? 27.673 -12.672 15.607 1.00 29.38  ? 9   PHE A CA  1 
ATOM   43   C  C   . PHE A 1 12  ? 26.797 -13.776 16.166 1.00 26.56  ? 9   PHE A C   1 
ATOM   44   O  O   . PHE A 1 12  ? 25.652 -13.549 16.550 1.00 28.50  ? 9   PHE A O   1 
ATOM   45   C  CB  . PHE A 1 12  ? 28.733 -12.242 16.647 1.00 28.27  ? 9   PHE A CB  1 
ATOM   46   C  CG  . PHE A 1 12  ? 28.171 -11.723 17.955 1.00 26.17  ? 9   PHE A CG  1 
ATOM   47   C  CD1 . PHE A 1 12  ? 27.686 -12.587 18.925 1.00 24.85  ? 9   PHE A CD1 1 
ATOM   48   C  CD2 . PHE A 1 12  ? 28.202 -10.370 18.236 1.00 26.61  ? 9   PHE A CD2 1 
ATOM   49   C  CE1 . PHE A 1 12  ? 27.198 -12.110 20.115 1.00 24.48  ? 9   PHE A CE1 1 
ATOM   50   C  CE2 . PHE A 1 12  ? 27.717 -9.880  19.451 1.00 24.35  ? 9   PHE A CE2 1 
ATOM   51   C  CZ  . PHE A 1 12  ? 27.219 -10.755 20.389 1.00 23.68  ? 9   PHE A CZ  1 
ATOM   52   N  N   . PHE A 1 13  ? 27.365 -14.982 16.215 1.00 25.73  ? 10  PHE A N   1 
ATOM   53   C  CA  . PHE A 1 13  ? 26.620 -16.186 16.601 1.00 28.39  ? 10  PHE A CA  1 
ATOM   54   C  C   . PHE A 1 13  ? 27.622 -17.073 17.331 1.00 27.40  ? 10  PHE A C   1 
ATOM   55   O  O   . PHE A 1 13  ? 28.449 -17.716 16.680 1.00 30.53  ? 10  PHE A O   1 
ATOM   56   C  CB  . PHE A 1 13  ? 26.045 -16.866 15.359 1.00 30.32  ? 10  PHE A CB  1 
ATOM   57   C  CG  . PHE A 1 13  ? 25.111 -18.022 15.633 1.00 30.96  ? 10  PHE A CG  1 
ATOM   58   C  CD1 . PHE A 1 13  ? 24.423 -18.136 16.834 1.00 29.25  ? 10  PHE A CD1 1 
ATOM   59   C  CD2 . PHE A 1 13  ? 24.897 -18.980 14.653 1.00 32.73  ? 10  PHE A CD2 1 
ATOM   60   C  CE1 . PHE A 1 13  ? 23.539 -19.199 17.058 1.00 25.93  ? 10  PHE A CE1 1 
ATOM   61   C  CE2 . PHE A 1 13  ? 24.031 -20.047 14.875 1.00 33.29  ? 10  PHE A CE2 1 
ATOM   62   C  CZ  . PHE A 1 13  ? 23.349 -20.146 16.098 1.00 30.35  ? 10  PHE A CZ  1 
ATOM   63   N  N   . PHE A 1 14  ? 27.576 -17.062 18.664 1.00 28.66  ? 11  PHE A N   1 
ATOM   64   C  CA  . PHE A 1 14  ? 28.487 -17.854 19.486 1.00 27.24  ? 11  PHE A CA  1 
ATOM   65   C  C   . PHE A 1 14  ? 27.713 -19.065 19.991 1.00 30.17  ? 11  PHE A C   1 
ATOM   66   O  O   . PHE A 1 14  ? 26.834 -18.932 20.848 1.00 26.14  ? 11  PHE A O   1 
ATOM   67   C  CB  . PHE A 1 14  ? 29.047 -17.054 20.662 1.00 27.02  ? 11  PHE A CB  1 
ATOM   68   C  CG  . PHE A 1 14  ? 29.728 -15.761 20.276 1.00 25.79  ? 11  PHE A CG  1 
ATOM   69   C  CD1 . PHE A 1 14  ? 30.400 -15.640 19.068 1.00 27.69  ? 11  PHE A CD1 1 
ATOM   70   C  CD2 . PHE A 1 14  ? 29.728 -14.680 21.167 1.00 28.06  ? 11  PHE A CD2 1 
ATOM   71   C  CE1 . PHE A 1 14  ? 31.035 -14.450 18.710 1.00 29.05  ? 11  PHE A CE1 1 
ATOM   72   C  CE2 . PHE A 1 14  ? 30.370 -13.493 20.832 1.00 28.17  ? 11  PHE A CE2 1 
ATOM   73   C  CZ  . PHE A 1 14  ? 31.024 -13.378 19.596 1.00 27.94  ? 11  PHE A CZ  1 
ATOM   74   N  N   . GLU A 1 15  ? 28.046 -20.242 19.477 1.00 30.88  ? 12  GLU A N   1 
ATOM   75   C  CA  . GLU A 1 15  ? 27.284 -21.446 19.775 1.00 30.04  ? 12  GLU A CA  1 
ATOM   76   C  C   . GLU A 1 15  ? 27.987 -22.261 20.846 1.00 30.51  ? 12  GLU A C   1 
ATOM   77   O  O   . GLU A 1 15  ? 29.135 -22.682 20.658 1.00 29.45  ? 12  GLU A O   1 
ATOM   78   C  CB  . GLU A 1 15  ? 27.096 -22.285 18.523 1.00 29.54  ? 12  GLU A CB  1 
ATOM   79   C  CG  . GLU A 1 15  ? 26.142 -21.653 17.533 1.00 33.51  ? 12  GLU A CG  1 
ATOM   80   C  CD  . GLU A 1 15  ? 25.901 -22.539 16.353 1.00 36.95  ? 12  GLU A CD  1 
ATOM   81   O  OE1 . GLU A 1 15  ? 25.051 -23.457 16.474 1.00 37.67  ? 12  GLU A OE1 1 
ATOM   82   O  OE2 . GLU A 1 15  ? 26.570 -22.342 15.314 1.00 37.05  ? 12  GLU A OE2 1 
ATOM   83   N  N   . GLU A 1 16  ? 27.284 -22.497 21.951 1.00 28.76  ? 13  GLU A N   1 
ATOM   84   C  CA  . GLU A 1 16  ? 27.761 -23.397 22.995 1.00 32.39  ? 13  GLU A CA  1 
ATOM   85   C  C   . GLU A 1 16  ? 26.680 -24.412 23.331 1.00 34.11  ? 13  GLU A C   1 
ATOM   86   O  O   . GLU A 1 16  ? 26.414 -25.309 22.532 1.00 34.59  ? 13  GLU A O   1 
ATOM   87   C  CB  . GLU A 1 16  ? 28.183 -22.635 24.239 1.00 33.35  ? 13  GLU A CB  1 
ATOM   88   C  CG  . GLU A 1 16  ? 29.327 -21.675 24.006 1.00 36.55  ? 13  GLU A CG  1 
ATOM   89   C  CD  . GLU A 1 16  ? 30.626 -22.416 23.750 1.00 40.37  ? 13  GLU A CD  1 
ATOM   90   O  OE1 . GLU A 1 16  ? 31.326 -22.080 22.758 1.00 41.71  ? 13  GLU A OE1 1 
ATOM   91   O  OE2 . GLU A 1 16  ? 30.887 -23.404 24.464 1.00 41.18  ? 13  GLU A OE2 1 
ATOM   92   N  N   . GLY A 1 17  ? 26.043 -24.285 24.489 1.00 32.81  ? 14  GLY A N   1 
ATOM   93   C  CA  . GLY A 1 17  ? 25.019 -25.229 24.878 1.00 31.67  ? 14  GLY A CA  1 
ATOM   94   C  C   . GLY A 1 17  ? 23.667 -24.886 24.283 1.00 31.94  ? 14  GLY A C   1 
ATOM   95   O  O   . GLY A 1 17  ? 23.508 -23.961 23.482 1.00 32.70  ? 14  GLY A O   1 
ATOM   96   N  N   . LYS A 1 18  ? 22.665 -25.649 24.702 1.00 30.98  ? 15  LYS A N   1 
ATOM   97   C  CA  . LYS A 1 18  ? 21.362 -25.482 24.080 1.00 31.96  ? 15  LYS A CA  1 
ATOM   98   C  C   . LYS A 1 18  ? 20.568 -24.319 24.651 1.00 31.92  ? 15  LYS A C   1 
ATOM   99   O  O   . LYS A 1 18  ? 19.563 -23.929 24.050 1.00 34.14  ? 15  LYS A O   1 
ATOM   100  C  CB  . LYS A 1 18  ? 20.562 -26.779 24.182 1.00 35.08  ? 15  LYS A CB  1 
ATOM   101  C  CG  . LYS A 1 18  ? 21.139 -27.843 23.250 1.00 43.40  ? 15  LYS A CG  1 
ATOM   102  C  CD  . LYS A 1 18  ? 20.378 -27.907 21.919 1.00 52.46  ? 15  LYS A CD  1 
ATOM   103  C  CE  . LYS A 1 18  ? 20.953 -28.989 21.003 1.00 54.85  ? 15  LYS A CE  1 
ATOM   104  N  NZ  . LYS A 1 18  ? 19.957 -30.023 20.563 1.00 63.55  ? 15  LYS A NZ  1 
ATOM   105  N  N   . ARG A 1 19  ? 20.983 -23.735 25.771 1.00 27.15  ? 16  ARG A N   1 
ATOM   106  C  CA  . ARG A 1 19  ? 20.309 -22.534 26.240 1.00 26.11  ? 16  ARG A CA  1 
ATOM   107  C  C   . ARG A 1 19  ? 20.831 -21.345 25.442 1.00 26.74  ? 16  ARG A C   1 
ATOM   108  O  O   . ARG A 1 19  ? 22.042 -21.143 25.346 1.00 27.88  ? 16  ARG A O   1 
ATOM   109  C  CB  . ARG A 1 19  ? 20.547 -22.323 27.733 1.00 26.25  ? 16  ARG A CB  1 
ATOM   110  C  CG  . ARG A 1 19  ? 20.249 -23.536 28.591 1.00 27.25  ? 16  ARG A CG  1 
ATOM   111  C  CD  . ARG A 1 19  ? 20.612 -23.207 30.031 1.00 31.17  ? 16  ARG A CD  1 
ATOM   112  N  NE  . ARG A 1 19  ? 20.426 -24.338 30.935 1.00 32.04  ? 16  ARG A NE  1 
ATOM   113  C  CZ  . ARG A 1 19  ? 20.622 -24.278 32.249 1.00 35.82  ? 16  ARG A CZ  1 
ATOM   114  N  NH1 . ARG A 1 19  ? 21.020 -23.160 32.842 1.00 30.06  ? 16  ARG A NH1 1 
ATOM   115  N  NH2 . ARG A 1 19  ? 20.409 -25.363 32.986 1.00 33.41  ? 16  ARG A NH2 1 
ATOM   116  N  N   . ALA A 1 20  ? 19.925 -20.551 24.873 1.00 26.37  ? 17  ALA A N   1 
ATOM   117  C  CA  . ALA A 1 20  ? 20.319 -19.491 23.953 1.00 23.38  ? 17  ALA A CA  1 
ATOM   118  C  C   . ALA A 1 20  ? 19.814 -18.130 24.412 1.00 25.12  ? 17  ALA A C   1 
ATOM   119  O  O   . ALA A 1 20  ? 18.766 -18.015 25.054 1.00 24.86  ? 17  ALA A O   1 
ATOM   120  C  CB  . ALA A 1 20  ? 19.808 -19.771 22.519 1.00 25.62  ? 17  ALA A CB  1 
ATOM   121  N  N   . VAL A 1 21  ? 20.565 -17.089 24.063 1.00 23.87  ? 18  VAL A N   1 
ATOM   122  C  CA  . VAL A 1 21  ? 20.180 -15.718 24.376 1.00 23.33  ? 18  VAL A CA  1 
ATOM   123  C  C   . VAL A 1 21  ? 20.199 -14.912 23.087 1.00 26.04  ? 18  VAL A C   1 
ATOM   124  O  O   . VAL A 1 21  ? 21.215 -14.889 22.385 1.00 24.97  ? 18  VAL A O   1 
ATOM   125  C  CB  . VAL A 1 21  ? 21.109 -15.072 25.419 1.00 22.59  ? 18  VAL A CB  1 
ATOM   126  C  CG1 . VAL A 1 21  ? 20.646 -13.633 25.727 1.00 25.03  ? 18  VAL A CG1 1 
ATOM   127  C  CG2 . VAL A 1 21  ? 21.163 -15.919 26.710 1.00 24.31  ? 18  VAL A CG2 1 
ATOM   128  N  N   . LEU A 1 22  ? 19.090 -14.240 22.791 1.00 21.34  ? 19  LEU A N   1 
ATOM   129  C  CA  . LEU A 1 22  ? 19.008 -13.319 21.658 1.00 22.41  ? 19  LEU A CA  1 
ATOM   130  C  C   . LEU A 1 22  ? 19.376 -11.932 22.164 1.00 25.82  ? 19  LEU A C   1 
ATOM   131  O  O   . LEU A 1 22  ? 18.728 -11.416 23.081 1.00 25.98  ? 19  LEU A O   1 
ATOM   132  C  CB  . LEU A 1 22  ? 17.595 -13.323 21.071 1.00 20.78  ? 19  LEU A CB  1 
ATOM   133  C  CG  . LEU A 1 22  ? 17.276 -12.370 19.922 1.00 22.96  ? 19  LEU A CG  1 
ATOM   134  C  CD1 . LEU A 1 22  ? 18.105 -12.675 18.648 1.00 23.84  ? 19  LEU A CD1 1 
ATOM   135  C  CD2 . LEU A 1 22  ? 15.774 -12.435 19.609 1.00 23.90  ? 19  LEU A CD2 1 
ATOM   136  N  N   . LEU A 1 23  ? 20.418 -11.335 21.589 1.00 23.86  ? 20  LEU A N   1 
ATOM   137  C  CA  . LEU A 1 23  ? 20.984 -10.080 22.071 1.00 24.19  ? 20  LEU A CA  1 
ATOM   138  C  C   . LEU A 1 23  ? 20.617 -8.959  21.106 1.00 27.64  ? 20  LEU A C   1 
ATOM   139  O  O   . LEU A 1 23  ? 21.067 -8.968  19.957 1.00 26.37  ? 20  LEU A O   1 
ATOM   140  C  CB  . LEU A 1 23  ? 22.506 -10.179 22.182 1.00 23.95  ? 20  LEU A CB  1 
ATOM   141  C  CG  . LEU A 1 23  ? 23.003 -11.220 23.185 1.00 24.24  ? 20  LEU A CG  1 
ATOM   142  C  CD1 . LEU A 1 23  ? 24.533 -11.357 23.074 1.00 27.80  ? 20  LEU A CD1 1 
ATOM   143  C  CD2 . LEU A 1 23  ? 22.579 -10.819 24.585 1.00 27.60  ? 20  LEU A CD2 1 
ATOM   144  N  N   . LEU A 1 24  ? 19.866 -7.967  21.589 1.00 26.28  ? 21  LEU A N   1 
ATOM   145  C  CA  . LEU A 1 24  ? 19.362 -6.888  20.741 1.00 24.75  ? 21  LEU A CA  1 
ATOM   146  C  C   . LEU A 1 24  ? 20.024 -5.565  21.094 1.00 28.49  ? 21  LEU A C   1 
ATOM   147  O  O   . LEU A 1 24  ? 19.985 -5.139  22.252 1.00 26.77  ? 21  LEU A O   1 
ATOM   148  C  CB  . LEU A 1 24  ? 17.846 -6.751  20.879 1.00 24.43  ? 21  LEU A CB  1 
ATOM   149  C  CG  . LEU A 1 24  ? 17.054 -8.016  20.542 1.00 26.33  ? 21  LEU A CG  1 
ATOM   150  C  CD1 . LEU A 1 24  ? 15.547 -7.772  20.699 1.00 25.53  ? 21  LEU A CD1 1 
ATOM   151  C  CD2 . LEU A 1 24  ? 17.391 -8.504  19.112 1.00 28.78  ? 21  LEU A CD2 1 
ATOM   152  N  N   . HIS A 1 25  ? 20.602 -4.899  20.096 1.00 27.16  ? 22  HIS A N   1 
ATOM   153  C  CA  . HIS A 1 25  ? 21.318 -3.658  20.336 1.00 27.39  ? 22  HIS A CA  1 
ATOM   154  C  C   . HIS A 1 25  ? 20.355 -2.468  20.265 1.00 27.69  ? 22  HIS A C   1 
ATOM   155  O  O   . HIS A 1 25  ? 19.142 -2.620  20.096 1.00 28.15  ? 22  HIS A O   1 
ATOM   156  C  CB  . HIS A 1 25  ? 22.495 -3.514  19.359 1.00 28.43  ? 22  HIS A CB  1 
ATOM   157  C  CG  . HIS A 1 25  ? 22.101 -3.324  17.919 1.00 29.04  ? 22  HIS A CG  1 
ATOM   158  N  ND1 . HIS A 1 25  ? 21.679 -2.110  17.415 1.00 29.49  ? 22  HIS A ND1 1 
ATOM   159  C  CD2 . HIS A 1 25  ? 22.120 -4.180  16.866 1.00 29.94  ? 22  HIS A CD2 1 
ATOM   160  C  CE1 . HIS A 1 25  ? 21.445 -2.230  16.116 1.00 33.72  ? 22  HIS A CE1 1 
ATOM   161  N  NE2 . HIS A 1 25  ? 21.698 -3.477  15.759 1.00 30.84  ? 22  HIS A NE2 1 
ATOM   162  N  N   . GLY A 1 26  ? 20.902 -1.262  20.410 1.00 28.79  ? 23  GLY A N   1 
ATOM   163  C  CA  . GLY A 1 26  ? 20.103 -0.061  20.509 1.00 31.66  ? 23  GLY A CA  1 
ATOM   164  C  C   . GLY A 1 26  ? 20.080 0.741   19.214 1.00 32.50  ? 23  GLY A C   1 
ATOM   165  O  O   . GLY A 1 26  ? 20.750 0.431   18.235 1.00 31.10  ? 23  GLY A O   1 
ATOM   166  N  N   . PHE A 1 27  ? 19.292 1.809   19.240 1.00 32.20  ? 24  PHE A N   1 
ATOM   167  C  CA  . PHE A 1 27  ? 19.210 2.711   18.100 1.00 34.74  ? 24  PHE A CA  1 
ATOM   168  C  C   . PHE A 1 27  ? 20.557 3.387   17.871 1.00 36.95  ? 24  PHE A C   1 
ATOM   169  O  O   . PHE A 1 27  ? 21.156 3.936   18.801 1.00 38.66  ? 24  PHE A O   1 
ATOM   170  C  CB  . PHE A 1 27  ? 18.102 3.732   18.349 1.00 33.53  ? 24  PHE A CB  1 
ATOM   171  C  CG  . PHE A 1 27  ? 18.050 4.841   17.353 1.00 38.21  ? 24  PHE A CG  1 
ATOM   172  C  CD1 . PHE A 1 27  ? 17.872 4.589   15.999 1.00 39.07  ? 24  PHE A CD1 1 
ATOM   173  C  CD2 . PHE A 1 27  ? 18.138 6.153   17.781 1.00 40.89  ? 24  PHE A CD2 1 
ATOM   174  C  CE1 . PHE A 1 27  ? 17.811 5.634   15.087 1.00 40.74  ? 24  PHE A CE1 1 
ATOM   175  C  CE2 . PHE A 1 27  ? 18.074 7.196   16.891 1.00 43.93  ? 24  PHE A CE2 1 
ATOM   176  C  CZ  . PHE A 1 27  ? 17.909 6.941   15.530 1.00 44.74  ? 24  PHE A CZ  1 
ATOM   177  N  N   . THR A 1 28  ? 21.038 3.327   16.627 1.00 36.78  ? 25  THR A N   1 
ATOM   178  C  CA  . THR A 1 28  ? 22.367 3.748   16.183 1.00 36.02  ? 25  THR A CA  1 
ATOM   179  C  C   . THR A 1 28  ? 23.482 2.847   16.706 1.00 37.32  ? 25  THR A C   1 
ATOM   180  O  O   . THR A 1 28  ? 24.644 3.097   16.390 1.00 41.48  ? 25  THR A O   1 
ATOM   181  C  CB  . THR A 1 28  ? 22.706 5.205   16.546 1.00 41.39  ? 25  THR A CB  1 
ATOM   182  O  OG1 . THR A 1 28  ? 23.021 5.299   17.943 1.00 42.96  ? 25  THR A OG1 1 
ATOM   183  C  CG2 . THR A 1 28  ? 21.551 6.143   16.202 1.00 43.39  ? 25  THR A CG2 1 
ATOM   184  N  N   . GLY A 1 29  ? 23.172 1.805   17.471 1.00 32.64  ? 26  GLY A N   1 
ATOM   185  C  CA  . GLY A 1 29  ? 24.175 0.861   17.909 1.00 35.66  ? 26  GLY A CA  1 
ATOM   186  C  C   . GLY A 1 29  ? 24.418 -0.219  16.870 1.00 36.72  ? 26  GLY A C   1 
ATOM   187  O  O   . GLY A 1 29  ? 24.011 -0.123  15.711 1.00 34.38  ? 26  GLY A O   1 
ATOM   188  N  N   . ASN A 1 30  ? 25.088 -1.278  17.312 1.00 34.92  ? 27  ASN A N   1 
ATOM   189  C  CA  . ASN A 1 30  ? 25.342 -2.446  16.471 1.00 34.45  ? 27  ASN A CA  1 
ATOM   190  C  C   . ASN A 1 30  ? 25.810 -3.571  17.388 1.00 32.66  ? 27  ASN A C   1 
ATOM   191  O  O   . ASN A 1 30  ? 25.821 -3.433  18.618 1.00 30.98  ? 27  ASN A O   1 
ATOM   192  C  CB  . ASN A 1 30  ? 26.363 -2.139  15.372 1.00 32.84  ? 27  ASN A CB  1 
ATOM   193  C  CG  . ASN A 1 30  ? 27.637 -1.565  15.928 1.00 36.45  ? 27  ASN A CG  1 
ATOM   194  O  OD1 . ASN A 1 30  ? 28.295 -2.198  16.753 1.00 34.96  ? 27  ASN A OD1 1 
ATOM   195  N  ND2 . ASN A 1 30  ? 28.001 -0.371  15.482 1.00 36.38  ? 27  ASN A ND2 1 
ATOM   196  N  N   . SER A 1 31  ? 26.216 -4.685  16.787 1.00 30.83  ? 28  SER A N   1 
ATOM   197  C  CA  . SER A 1 31  ? 26.542 -5.858  17.587 1.00 29.84  ? 28  SER A CA  1 
ATOM   198  C  C   . SER A 1 31  ? 27.743 -5.635  18.496 1.00 30.48  ? 28  SER A C   1 
ATOM   199  O  O   . SER A 1 31  ? 27.880 -6.341  19.493 1.00 28.73  ? 28  SER A O   1 
ATOM   200  C  CB  . SER A 1 31  ? 26.785 -7.045  16.657 1.00 30.65  ? 28  SER A CB  1 
ATOM   201  O  OG  . SER A 1 31  ? 28.077 -6.944  16.082 1.00 30.38  ? 28  SER A OG  1 
ATOM   202  N  N   . SER A 1 32  ? 28.611 -4.667  18.191 1.00 29.97  ? 29  SER A N   1 
ATOM   203  C  CA  . SER A 1 32  ? 29.762 -4.453  19.053 1.00 31.49  ? 29  SER A CA  1 
ATOM   204  C  C   . SER A 1 32  ? 29.355 -4.010  20.450 1.00 34.02  ? 29  SER A C   1 
ATOM   205  O  O   . SER A 1 32  ? 30.153 -4.139  21.381 1.00 30.22  ? 29  SER A O   1 
ATOM   206  C  CB  . SER A 1 32  ? 30.711 -3.432  18.438 1.00 34.34  ? 29  SER A CB  1 
ATOM   207  O  OG  . SER A 1 32  ? 30.208 -2.114  18.594 1.00 36.67  ? 29  SER A OG  1 
ATOM   208  N  N   . ASP A 1 33  ? 28.140 -3.488  20.616 1.00 30.89  ? 30  ASP A N   1 
ATOM   209  C  CA  . ASP A 1 33  ? 27.691 -3.049  21.930 1.00 30.65  ? 30  ASP A CA  1 
ATOM   210  C  C   . ASP A 1 33  ? 27.328 -4.205  22.848 1.00 29.89  ? 30  ASP A C   1 
ATOM   211  O  O   . ASP A 1 33  ? 27.141 -3.975  24.043 1.00 30.36  ? 30  ASP A O   1 
ATOM   212  C  CB  . ASP A 1 33  ? 26.479 -2.118  21.814 1.00 30.40  ? 30  ASP A CB  1 
ATOM   213  C  CG  . ASP A 1 33  ? 26.806 -0.811  21.102 1.00 37.76  ? 30  ASP A CG  1 
ATOM   214  O  OD1 . ASP A 1 33  ? 27.823 -0.175  21.443 1.00 37.76  ? 30  ASP A OD1 1 
ATOM   215  O  OD2 . ASP A 1 33  ? 26.029 -0.411  20.215 1.00 37.74  ? 30  ASP A OD2 1 
ATOM   216  N  N   . VAL A 1 34  ? 27.187 -5.420  22.319 1.00 28.84  ? 31  VAL A N   1 
ATOM   217  C  CA  . VAL A 1 34  ? 26.793 -6.571  23.125 1.00 26.14  ? 31  VAL A CA  1 
ATOM   218  C  C   . VAL A 1 34  ? 27.755 -7.734  22.929 1.00 27.91  ? 31  VAL A C   1 
ATOM   219  O  O   . VAL A 1 34  ? 27.515 -8.832  23.443 1.00 26.85  ? 31  VAL A O   1 
ATOM   220  C  CB  . VAL A 1 34  ? 25.346 -7.009  22.815 1.00 25.84  ? 31  VAL A CB  1 
ATOM   221  C  CG1 . VAL A 1 34  ? 24.355 -5.915  23.252 1.00 29.06  ? 31  VAL A CG1 1 
ATOM   222  C  CG2 . VAL A 1 34  ? 25.165 -7.329  21.320 1.00 27.55  ? 31  VAL A CG2 1 
ATOM   223  N  N   . ARG A 1 35  ? 28.852 -7.510  22.190 1.00 25.20  ? 32  ARG A N   1 
ATOM   224  C  CA  . ARG A 1 35  ? 29.770 -8.612  21.907 1.00 25.78  ? 32  ARG A CA  1 
ATOM   225  C  C   . ARG A 1 35  ? 30.459 -9.109  23.180 1.00 27.44  ? 32  ARG A C   1 
ATOM   226  O  O   . ARG A 1 35  ? 30.674 -10.316 23.342 1.00 27.85  ? 32  ARG A O   1 
ATOM   227  C  CB  . ARG A 1 35  ? 30.813 -8.182  20.870 1.00 26.30  ? 32  ARG A CB  1 
ATOM   228  C  CG  . ARG A 1 35  ? 31.572 -9.340  20.238 1.00 28.77  ? 32  ARG A CG  1 
ATOM   229  C  CD  . ARG A 1 35  ? 32.635 -8.852  19.251 1.00 27.58  ? 32  ARG A CD  1 
ATOM   230  N  NE  . ARG A 1 35  ? 33.219 -9.954  18.488 1.00 28.69  ? 32  ARG A NE  1 
ATOM   231  C  CZ  . ARG A 1 35  ? 32.691 -10.451 17.380 1.00 31.41  ? 32  ARG A CZ  1 
ATOM   232  N  NH1 . ARG A 1 35  ? 31.574 -9.957  16.869 1.00 28.96  ? 32  ARG A NH1 1 
ATOM   233  N  NH2 . ARG A 1 35  ? 33.302 -11.464 16.765 1.00 31.17  ? 32  ARG A NH2 1 
ATOM   234  N  N   . GLN A 1 36  ? 30.830 -8.198  24.082 1.00 25.97  ? 33  GLN A N   1 
ATOM   235  C  CA  . GLN A 1 36  ? 31.476 -8.622  25.329 1.00 27.65  ? 33  GLN A CA  1 
ATOM   236  C  C   . GLN A 1 36  ? 30.510 -9.417  26.199 1.00 26.05  ? 33  GLN A C   1 
ATOM   237  O  O   . GLN A 1 36  ? 30.893 -10.432 26.795 1.00 26.67  ? 33  GLN A O   1 
ATOM   238  C  CB  . GLN A 1 36  ? 32.024 -7.400  26.064 1.00 27.19  ? 33  GLN A CB  1 
ATOM   239  C  CG  . GLN A 1 36  ? 33.315 -6.880  25.429 1.00 32.51  ? 33  GLN A CG  1 
ATOM   240  C  CD  . GLN A 1 36  ? 33.657 -5.454  25.845 1.00 39.85  ? 33  GLN A CD  1 
ATOM   241  O  OE1 . GLN A 1 36  ? 32.841 -4.542  25.700 1.00 42.43  ? 33  GLN A OE1 1 
ATOM   242  N  NE2 . GLN A 1 36  ? 34.843 -5.266  26.393 1.00 39.34  ? 33  GLN A NE2 1 
ATOM   243  N  N   . LEU A 1 37  ? 29.243 -9.003  26.241 1.00 25.08  ? 34  LEU A N   1 
ATOM   244  C  CA  . LEU A 1 37  ? 28.225 -9.823  26.894 1.00 26.31  ? 34  LEU A CA  1 
ATOM   245  C  C   . LEU A 1 37  ? 28.110 -11.193 26.220 1.00 25.80  ? 34  LEU A C   1 
ATOM   246  O  O   . LEU A 1 37  ? 28.048 -12.228 26.899 1.00 26.28  ? 34  LEU A O   1 
ATOM   247  C  CB  . LEU A 1 37  ? 26.885 -9.086  26.860 1.00 25.79  ? 34  LEU A CB  1 
ATOM   248  C  CG  . LEU A 1 37  ? 25.620 -9.817  27.282 1.00 25.63  ? 34  LEU A CG  1 
ATOM   249  C  CD1 . LEU A 1 37  ? 25.809 -10.364 28.720 1.00 26.16  ? 34  LEU A CD1 1 
ATOM   250  C  CD2 . LEU A 1 37  ? 24.419 -8.870  27.198 1.00 25.20  ? 34  LEU A CD2 1 
ATOM   251  N  N   . GLY A 1 38  ? 28.129 -11.228 24.885 1.00 24.28  ? 35  GLY A N   1 
ATOM   252  C  CA  . GLY A 1 38  ? 28.084 -12.511 24.198 1.00 26.34  ? 35  GLY A CA  1 
ATOM   253  C  C   . GLY A 1 38  ? 29.254 -13.410 24.563 1.00 24.86  ? 35  GLY A C   1 
ATOM   254  O  O   . GLY A 1 38  ? 29.085 -14.616 24.775 1.00 25.00  ? 35  GLY A O   1 
ATOM   255  N  N   . ARG A 1 39  ? 30.460 -12.844 24.627 1.00 25.32  ? 36  ARG A N   1 
ATOM   256  C  CA  . ARG A 1 39  ? 31.617 -13.648 25.014 1.00 24.97  ? 36  ARG A CA  1 
ATOM   257  C  C   . ARG A 1 39  ? 31.489 -14.134 26.451 1.00 28.11  ? 36  ARG A C   1 
ATOM   258  O  O   . ARG A 1 39  ? 31.890 -15.256 26.779 1.00 26.95  ? 36  ARG A O   1 
ATOM   259  C  CB  . ARG A 1 39  ? 32.898 -12.840 24.848 1.00 24.96  ? 36  ARG A CB  1 
ATOM   260  C  CG  . ARG A 1 39  ? 33.282 -12.576 23.384 1.00 26.32  ? 36  ARG A CG  1 
ATOM   261  C  CD  . ARG A 1 39  ? 33.572 -13.861 22.635 1.00 26.13  ? 36  ARG A CD  1 
ATOM   262  N  NE  . ARG A 1 39  ? 34.149 -13.568 21.326 1.00 27.32  ? 36  ARG A NE  1 
ATOM   263  C  CZ  . ARG A 1 39  ? 34.193 -14.437 20.328 1.00 26.62  ? 36  ARG A CZ  1 
ATOM   264  N  NH1 . ARG A 1 39  ? 33.725 -15.668 20.471 1.00 25.84  ? 36  ARG A NH1 1 
ATOM   265  N  NH2 . ARG A 1 39  ? 34.734 -14.066 19.159 1.00 27.08  ? 36  ARG A NH2 1 
ATOM   266  N  N   . PHE A 1 40  ? 30.975 -13.286 27.331 1.00 24.89  ? 37  PHE A N   1 
ATOM   267  C  CA  . PHE A 1 40  ? 30.781 -13.710 28.715 1.00 26.03  ? 37  PHE A CA  1 
ATOM   268  C  C   . PHE A 1 40  ? 29.791 -14.863 28.781 1.00 28.49  ? 37  PHE A C   1 
ATOM   269  O  O   . PHE A 1 40  ? 30.033 -15.874 29.449 1.00 26.75  ? 37  PHE A O   1 
ATOM   270  C  CB  . PHE A 1 40  ? 30.293 -12.536 29.552 1.00 26.65  ? 37  PHE A CB  1 
ATOM   271  C  CG  . PHE A 1 40  ? 29.910 -12.930 30.959 1.00 28.22  ? 37  PHE A CG  1 
ATOM   272  C  CD1 . PHE A 1 40  ? 30.849 -12.965 31.959 1.00 33.23  ? 37  PHE A CD1 1 
ATOM   273  C  CD2 . PHE A 1 40  ? 28.599 -13.284 31.249 1.00 34.31  ? 37  PHE A CD2 1 
ATOM   274  C  CE1 . PHE A 1 40  ? 30.485 -13.330 33.275 1.00 38.44  ? 37  PHE A CE1 1 
ATOM   275  C  CE2 . PHE A 1 40  ? 28.230 -13.666 32.549 1.00 32.88  ? 37  PHE A CE2 1 
ATOM   276  C  CZ  . PHE A 1 40  ? 29.167 -13.682 33.548 1.00 32.49  ? 37  PHE A CZ  1 
ATOM   277  N  N   . LEU A 1 41  ? 28.668 -14.728 28.072 1.00 25.82  ? 38  LEU A N   1 
ATOM   278  C  CA  . LEU A 1 41  ? 27.679 -15.799 28.053 1.00 26.23  ? 38  LEU A CA  1 
ATOM   279  C  C   . LEU A 1 41  ? 28.272 -17.087 27.514 1.00 25.33  ? 38  LEU A C   1 
ATOM   280  O  O   . LEU A 1 41  ? 27.989 -18.170 28.036 1.00 26.69  ? 38  LEU A O   1 
ATOM   281  C  CB  . LEU A 1 41  ? 26.468 -15.380 27.219 1.00 27.53  ? 38  LEU A CB  1 
ATOM   282  C  CG  . LEU A 1 41  ? 25.656 -14.218 27.798 1.00 27.72  ? 38  LEU A CG  1 
ATOM   283  C  CD1 . LEU A 1 41  ? 24.570 -13.771 26.792 1.00 27.43  ? 38  LEU A CD1 1 
ATOM   284  C  CD2 . LEU A 1 41  ? 25.037 -14.580 29.163 1.00 31.84  ? 38  LEU A CD2 1 
ATOM   285  N  N   . GLN A 1 42  ? 29.100 -16.991 26.463 1.00 24.70  ? 39  GLN A N   1 
ATOM   286  C  CA  . GLN A 1 42  ? 29.752 -18.175 25.915 1.00 25.18  ? 39  GLN A CA  1 
ATOM   287  C  C   . GLN A 1 42  ? 30.646 -18.850 26.954 1.00 29.41  ? 39  GLN A C   1 
ATOM   288  O  O   . GLN A 1 42  ? 30.655 -20.085 27.076 1.00 28.11  ? 39  GLN A O   1 
ATOM   289  C  CB  . GLN A 1 42  ? 30.558 -17.768 24.675 1.00 25.55  ? 39  GLN A CB  1 
ATOM   290  C  CG  . GLN A 1 42  ? 31.526 -18.786 24.209 1.00 27.09  ? 39  GLN A CG  1 
ATOM   291  C  CD  . GLN A 1 42  ? 32.166 -18.338 22.896 1.00 28.94  ? 39  GLN A CD  1 
ATOM   292  O  OE1 . GLN A 1 42  ? 32.657 -17.213 22.799 1.00 27.61  ? 39  GLN A OE1 1 
ATOM   293  N  NE2 . GLN A 1 42  ? 32.122 -19.192 21.888 1.00 27.81  ? 39  GLN A NE2 1 
ATOM   294  N  N   . LYS A 1 43  ? 31.401 -18.056 27.723 1.00 28.23  ? 40  LYS A N   1 
ATOM   295  C  CA  . LYS A 1 43  ? 32.247 -18.622 28.773 1.00 30.57  ? 40  LYS A CA  1 
ATOM   296  C  C   . LYS A 1 43  ? 31.414 -19.356 29.816 1.00 29.74  ? 40  LYS A C   1 
ATOM   297  O  O   . LYS A 1 43  ? 31.870 -20.347 30.397 1.00 29.52  ? 40  LYS A O   1 
ATOM   298  C  CB  . LYS A 1 43  ? 33.077 -17.502 29.414 1.00 29.31  ? 40  LYS A CB  1 
ATOM   299  C  CG  . LYS A 1 43  ? 33.687 -17.813 30.757 1.00 37.73  ? 40  LYS A CG  1 
ATOM   300  C  CD  . LYS A 1 43  ? 34.266 -16.557 31.405 1.00 41.22  ? 40  LYS A CD  1 
ATOM   301  C  CE  . LYS A 1 43  ? 33.411 -16.121 32.608 1.00 47.27  ? 40  LYS A CE  1 
ATOM   302  N  NZ  . LYS A 1 43  ? 33.872 -14.855 33.263 1.00 50.01  ? 40  LYS A NZ  1 
ATOM   303  N  N   . LYS A 1 44  ? 30.186 -18.893 30.050 1.00 28.73  ? 41  LYS A N   1 
ATOM   304  C  CA  . LYS A 1 44  ? 29.249 -19.528 30.970 1.00 31.83  ? 41  LYS A CA  1 
ATOM   305  C  C   . LYS A 1 44  ? 28.419 -20.633 30.327 1.00 34.78  ? 41  LYS A C   1 
ATOM   306  O  O   . LYS A 1 44  ? 27.566 -21.214 31.010 1.00 33.90  ? 41  LYS A O   1 
ATOM   307  C  CB  . LYS A 1 44  ? 28.315 -18.466 31.563 1.00 30.81  ? 41  LYS A CB  1 
ATOM   308  C  CG  . LYS A 1 44  ? 29.051 -17.440 32.417 1.00 30.77  ? 41  LYS A CG  1 
ATOM   309  C  CD  . LYS A 1 44  ? 29.819 -18.138 33.516 1.00 34.96  ? 41  LYS A CD  1 
ATOM   310  C  CE  . LYS A 1 44  ? 30.305 -17.158 34.560 1.00 33.39  ? 41  LYS A CE  1 
ATOM   311  N  NZ  . LYS A 1 44  ? 31.021 -17.883 35.644 1.00 39.23  ? 41  LYS A NZ  1 
ATOM   312  N  N   . GLY A 1 45  ? 28.634 -20.924 29.041 1.00 27.87  ? 42  GLY A N   1 
ATOM   313  C  CA  . GLY A 1 45  ? 28.008 -22.049 28.359 1.00 31.17  ? 42  GLY A CA  1 
ATOM   314  C  C   . GLY A 1 45  ? 26.726 -21.741 27.619 1.00 27.58  ? 42  GLY A C   1 
ATOM   315  O  O   . GLY A 1 45  ? 26.051 -22.673 27.167 1.00 29.14  ? 42  GLY A O   1 
ATOM   316  N  N   . TYR A 1 46  ? 26.366 -20.473 27.483 1.00 24.52  ? 43  TYR A N   1 
ATOM   317  C  CA  . TYR A 1 46  ? 25.154 -20.066 26.791 1.00 23.93  ? 43  TYR A CA  1 
ATOM   318  C  C   . TYR A 1 46  ? 25.477 -19.693 25.357 1.00 26.58  ? 43  TYR A C   1 
ATOM   319  O  O   . TYR A 1 46  ? 26.485 -19.041 25.086 1.00 25.95  ? 43  TYR A O   1 
ATOM   320  C  CB  . TYR A 1 46  ? 24.494 -18.871 27.485 1.00 25.66  ? 43  TYR A CB  1 
ATOM   321  C  CG  . TYR A 1 46  ? 23.812 -19.258 28.772 1.00 26.89  ? 43  TYR A CG  1 
ATOM   322  C  CD1 . TYR A 1 46  ? 24.544 -19.431 29.942 1.00 29.15  ? 43  TYR A CD1 1 
ATOM   323  C  CD2 . TYR A 1 46  ? 22.437 -19.493 28.814 1.00 26.74  ? 43  TYR A CD2 1 
ATOM   324  C  CE1 . TYR A 1 46  ? 23.925 -19.807 31.133 1.00 27.74  ? 43  TYR A CE1 1 
ATOM   325  C  CE2 . TYR A 1 46  ? 21.812 -19.862 30.001 1.00 26.53  ? 43  TYR A CE2 1 
ATOM   326  C  CZ  . TYR A 1 46  ? 22.562 -20.028 31.151 1.00 28.58  ? 43  TYR A CZ  1 
ATOM   327  O  OH  . TYR A 1 46  ? 21.953 -20.402 32.334 1.00 26.56  ? 43  TYR A OH  1 
ATOM   328  N  N   . THR A 1 47  ? 24.604 -20.100 24.455 1.00 23.79  ? 44  THR A N   1 
ATOM   329  C  CA  . THR A 1 47  ? 24.674 -19.668 23.067 1.00 25.65  ? 44  THR A CA  1 
ATOM   330  C  C   . THR A 1 47  ? 24.110 -18.261 22.973 1.00 25.10  ? 44  THR A C   1 
ATOM   331  O  O   . THR A 1 47  ? 23.200 -17.899 23.720 1.00 26.36  ? 44  THR A O   1 
ATOM   332  C  CB  . THR A 1 47  ? 23.881 -20.654 22.203 1.00 24.81  ? 44  THR A CB  1 
ATOM   333  O  OG1 . THR A 1 47  ? 24.574 -21.914 22.149 1.00 25.26  ? 44  THR A OG1 1 
ATOM   334  C  CG2 . THR A 1 47  ? 23.638 -20.137 20.753 1.00 24.53  ? 44  THR A CG2 1 
ATOM   335  N  N   . SER A 1 48  ? 24.663 -17.446 22.073 1.00 24.51  ? 45  SER A N   1 
ATOM   336  C  CA  . SER A 1 48  ? 24.063 -16.140 21.846 1.00 24.03  ? 45  SER A CA  1 
ATOM   337  C  C   . SER A 1 48  ? 24.096 -15.787 20.362 1.00 27.56  ? 45  SER A C   1 
ATOM   338  O  O   . SER A 1 48  ? 25.000 -16.188 19.621 1.00 25.37  ? 45  SER A O   1 
ATOM   339  C  CB  . SER A 1 48  ? 24.739 -15.018 22.658 1.00 27.33  ? 45  SER A CB  1 
ATOM   340  O  OG  . SER A 1 48  ? 26.075 -14.815 22.256 1.00 28.49  ? 45  SER A OG  1 
ATOM   341  N  N   . TYR A 1 49  ? 23.079 -15.043 19.940 1.00 22.60  ? 46  TYR A N   1 
ATOM   342  C  CA  . TYR A 1 49  ? 23.005 -14.507 18.587 1.00 23.31  ? 46  TYR A CA  1 
ATOM   343  C  C   . TYR A 1 49  ? 22.637 -13.037 18.675 1.00 27.10  ? 46  TYR A C   1 
ATOM   344  O  O   . TYR A 1 49  ? 21.686 -12.674 19.376 1.00 27.55  ? 46  TYR A O   1 
ATOM   345  C  CB  . TYR A 1 49  ? 21.977 -15.249 17.729 1.00 23.31  ? 46  TYR A CB  1 
ATOM   346  C  CG  . TYR A 1 49  ? 21.843 -14.621 16.360 1.00 24.37  ? 46  TYR A CG  1 
ATOM   347  C  CD1 . TYR A 1 49  ? 22.934 -14.563 15.514 1.00 24.15  ? 46  TYR A CD1 1 
ATOM   348  C  CD2 . TYR A 1 49  ? 20.646 -14.055 15.932 1.00 27.62  ? 46  TYR A CD2 1 
ATOM   349  C  CE1 . TYR A 1 49  ? 22.844 -13.981 14.253 1.00 31.02  ? 46  TYR A CE1 1 
ATOM   350  C  CE2 . TYR A 1 49  ? 20.541 -13.470 14.668 1.00 27.23  ? 46  TYR A CE2 1 
ATOM   351  C  CZ  . TYR A 1 49  ? 21.644 -13.439 13.839 1.00 29.12  ? 46  TYR A CZ  1 
ATOM   352  O  OH  . TYR A 1 49  ? 21.559 -12.855 12.607 1.00 30.33  ? 46  TYR A OH  1 
ATOM   353  N  N   . ALA A 1 50  ? 23.377 -12.196 17.959 1.00 26.17  ? 47  ALA A N   1 
ATOM   354  C  CA  . ALA A 1 50  ? 23.153 -10.750 17.976 1.00 26.88  ? 47  ALA A CA  1 
ATOM   355  C  C   . ALA A 1 50  ? 22.879 -10.292 16.554 1.00 28.57  ? 47  ALA A C   1 
ATOM   356  O  O   . ALA A 1 50  ? 23.821 -10.145 15.751 1.00 28.45  ? 47  ALA A O   1 
ATOM   357  C  CB  . ALA A 1 50  ? 24.356 -10.010 18.563 1.00 28.69  ? 47  ALA A CB  1 
ATOM   358  N  N   . PRO A 1 51  ? 21.622 -10.103 16.165 1.00 26.83  ? 48  PRO A N   1 
ATOM   359  C  CA  . PRO A 1 51  ? 21.345 -9.560  14.829 1.00 29.19  ? 48  PRO A CA  1 
ATOM   360  C  C   . PRO A 1 51  ? 21.682 -8.080  14.800 1.00 30.59  ? 48  PRO A C   1 
ATOM   361  O  O   . PRO A 1 51  ? 21.982 -7.465  15.824 1.00 29.28  ? 48  PRO A O   1 
ATOM   362  C  CB  . PRO A 1 51  ? 19.841 -9.791  14.657 1.00 29.67  ? 48  PRO A CB  1 
ATOM   363  C  CG  . PRO A 1 51  ? 19.318 -9.682  16.093 1.00 27.87  ? 48  PRO A CG  1 
ATOM   364  C  CD  . PRO A 1 51  ? 20.388 -10.350 16.936 1.00 27.52  ? 48  PRO A CD  1 
ATOM   365  N  N   . GLN A 1 52  ? 21.618 -7.497  13.609 1.00 31.58  ? 49  GLN A N   1 
ATOM   366  C  CA  . GLN A 1 52  ? 21.767 -6.055  13.478 1.00 30.19  ? 49  GLN A CA  1 
ATOM   367  C  C   . GLN A 1 52  ? 20.582 -5.502  12.705 1.00 33.48  ? 49  GLN A C   1 
ATOM   368  O  O   . GLN A 1 52  ? 20.134 -6.111  11.727 1.00 34.01  ? 49  GLN A O   1 
ATOM   369  C  CB  . GLN A 1 52  ? 23.092 -5.690  12.787 1.00 32.77  ? 49  GLN A CB  1 
ATOM   370  C  CG  . GLN A 1 52  ? 24.280 -5.894  13.748 1.00 32.09  ? 49  GLN A CG  1 
ATOM   371  C  CD  . GLN A 1 52  ? 25.596 -5.389  13.190 1.00 32.51  ? 49  GLN A CD  1 
ATOM   372  O  OE1 . GLN A 1 52  ? 26.483 -5.011  13.947 1.00 33.86  ? 49  GLN A OE1 1 
ATOM   373  N  NE2 . GLN A 1 52  ? 25.732 -5.387  11.861 1.00 32.53  ? 49  GLN A NE2 1 
ATOM   374  N  N   . TYR A 1 53  ? 20.087 -4.342  13.140 1.00 32.26  ? 50  TYR A N   1 
ATOM   375  C  CA  . TYR A 1 53  ? 18.960 -3.710  12.465 1.00 33.64  ? 50  TYR A CA  1 
ATOM   376  C  C   . TYR A 1 53  ? 19.376 -3.140  11.117 1.00 36.13  ? 50  TYR A C   1 
ATOM   377  O  O   . TYR A 1 53  ? 20.506 -2.681  10.929 1.00 35.27  ? 50  TYR A O   1 
ATOM   378  C  CB  . TYR A 1 53  ? 18.375 -2.583  13.312 1.00 34.28  ? 50  TYR A CB  1 
ATOM   379  C  CG  . TYR A 1 53  ? 18.117 -2.971  14.751 1.00 29.94  ? 50  TYR A CG  1 
ATOM   380  C  CD1 . TYR A 1 53  ? 17.655 -4.237  15.079 1.00 31.71  ? 50  TYR A CD1 1 
ATOM   381  C  CD2 . TYR A 1 53  ? 18.309 -2.055  15.775 1.00 32.42  ? 50  TYR A CD2 1 
ATOM   382  C  CE1 . TYR A 1 53  ? 17.416 -4.599  16.429 1.00 29.49  ? 50  TYR A CE1 1 
ATOM   383  C  CE2 . TYR A 1 53  ? 18.076 -2.395  17.116 1.00 31.00  ? 50  TYR A CE2 1 
ATOM   384  C  CZ  . TYR A 1 53  ? 17.631 -3.666  17.434 1.00 32.39  ? 50  TYR A CZ  1 
ATOM   385  O  OH  . TYR A 1 53  ? 17.408 -3.980  18.765 1.00 31.66  ? 50  TYR A OH  1 
ATOM   386  N  N   . GLU A 1 54  ? 18.423 -3.143  10.185 1.00 34.27  ? 51  GLU A N   1 
ATOM   387  C  CA  . GLU A 1 54  ? 18.650 -2.582  8.865  1.00 37.65  ? 51  GLU A CA  1 
ATOM   388  C  C   . GLU A 1 54  ? 19.174 -1.156  8.991  1.00 40.75  ? 51  GLU A C   1 
ATOM   389  O  O   . GLU A 1 54  ? 18.725 -0.386  9.848  1.00 39.40  ? 51  GLU A O   1 
ATOM   390  C  CB  . GLU A 1 54  ? 17.346 -2.603  8.068  1.00 38.92  ? 51  GLU A CB  1 
ATOM   391  C  CG  . GLU A 1 54  ? 17.347 -1.703  6.834  1.00 43.07  ? 51  GLU A CG  1 
ATOM   392  C  CD  . GLU A 1 54  ? 16.110 -1.893  5.987  1.00 50.46  ? 51  GLU A CD  1 
ATOM   393  O  OE1 . GLU A 1 54  ? 15.196 -1.050  6.099  1.00 48.22  ? 51  GLU A OE1 1 
ATOM   394  O  OE2 . GLU A 1 54  ? 16.059 -2.870  5.203  1.00 55.42  ? 51  GLU A OE2 1 
ATOM   395  N  N   . GLY A 1 55  ? 20.158 -0.819  8.160  1.00 38.75  ? 52  GLY A N   1 
ATOM   396  C  CA  . GLY A 1 55  ? 20.712 0.520   8.137  1.00 42.02  ? 52  GLY A CA  1 
ATOM   397  C  C   . GLY A 1 55  ? 21.721 0.814   9.230  1.00 42.04  ? 52  GLY A C   1 
ATOM   398  O  O   . GLY A 1 55  ? 22.388 1.854   9.165  1.00 47.49  ? 52  GLY A O   1 
ATOM   399  N  N   . HIS A 1 56  ? 21.867 -0.068  10.210 1.00 37.68  ? 53  HIS A N   1 
ATOM   400  C  CA  . HIS A 1 56  ? 22.875 0.064   11.252 1.00 40.12  ? 53  HIS A CA  1 
ATOM   401  C  C   . HIS A 1 56  ? 24.172 -0.603  10.812 1.00 41.68  ? 53  HIS A C   1 
ATOM   402  O  O   . HIS A 1 56  ? 24.189 -1.417  9.884  1.00 45.45  ? 53  HIS A O   1 
ATOM   403  C  CB  . HIS A 1 56  ? 22.371 -0.535  12.564 1.00 37.72  ? 53  HIS A CB  1 
ATOM   404  C  CG  . HIS A 1 56  ? 21.252 0.245   13.178 1.00 37.76  ? 53  HIS A CG  1 
ATOM   405  N  ND1 . HIS A 1 56  ? 20.054 0.459   12.531 1.00 36.86  ? 53  HIS A ND1 1 
ATOM   406  C  CD2 . HIS A 1 56  ? 21.156 0.882   14.369 1.00 35.66  ? 53  HIS A CD2 1 
ATOM   407  C  CE1 . HIS A 1 56  ? 19.266 1.193   13.297 1.00 36.98  ? 53  HIS A CE1 1 
ATOM   408  N  NE2 . HIS A 1 56  ? 19.910 1.461   14.419 1.00 35.04  ? 53  HIS A NE2 1 
ATOM   409  N  N   . ALA A 1 57  ? 25.271 -0.228  11.473 1.00 37.96  ? 54  ALA A N   1 
ATOM   410  C  CA  . ALA A 1 57  ? 26.620 -0.614  11.037 1.00 42.61  ? 54  ALA A CA  1 
ATOM   411  C  C   . ALA A 1 57  ? 26.810 -0.304  9.552  1.00 49.27  ? 54  ALA A C   1 
ATOM   412  O  O   . ALA A 1 57  ? 27.197 -1.158  8.750  1.00 46.11  ? 54  ALA A O   1 
ATOM   413  C  CB  . ALA A 1 57  ? 26.895 -2.091  11.339 1.00 42.21  ? 54  ALA A CB  1 
ATOM   414  N  N   . ALA A 1 58  ? 26.553 0.951   9.203  1.00 46.12  ? 55  ALA A N   1 
ATOM   415  C  CA  . ALA A 1 58  ? 26.396 1.410   7.831  1.00 51.28  ? 55  ALA A CA  1 
ATOM   416  C  C   . ALA A 1 58  ? 26.347 2.936   7.858  1.00 51.46  ? 55  ALA A C   1 
ATOM   417  O  O   . ALA A 1 58  ? 26.186 3.524   8.933  1.00 50.98  ? 55  ALA A O   1 
ATOM   418  C  CB  . ALA A 1 58  ? 25.117 0.835   7.199  1.00 48.30  ? 55  ALA A CB  1 
ATOM   419  N  N   . PRO A 1 59  ? 26.514 3.596   6.715  1.00 55.07  ? 56  PRO A N   1 
ATOM   420  C  CA  . PRO A 1 59  ? 26.369 5.058   6.687  1.00 54.94  ? 56  PRO A CA  1 
ATOM   421  C  C   . PRO A 1 59  ? 25.045 5.492   7.289  1.00 57.36  ? 56  PRO A C   1 
ATOM   422  O  O   . PRO A 1 59  ? 24.016 4.825   7.103  1.00 55.39  ? 56  PRO A O   1 
ATOM   423  C  CB  . PRO A 1 59  ? 26.451 5.405   5.196  1.00 56.55  ? 56  PRO A CB  1 
ATOM   424  C  CG  . PRO A 1 59  ? 27.054 4.229   4.543  1.00 57.74  ? 56  PRO A CG  1 
ATOM   425  C  CD  . PRO A 1 59  ? 27.065 3.064   5.454  1.00 51.88  ? 56  PRO A CD  1 
ATOM   426  N  N   . PRO A 1 60  ? 25.039 6.602   8.038  1.00 59.20  ? 57  PRO A N   1 
ATOM   427  C  CA  . PRO A 1 60  ? 23.834 6.980   8.795  1.00 59.27  ? 57  PRO A CA  1 
ATOM   428  C  C   . PRO A 1 60  ? 22.645 7.324   7.919  1.00 55.51  ? 57  PRO A C   1 
ATOM   429  O  O   . PRO A 1 60  ? 21.511 7.341   8.414  1.00 53.53  ? 57  PRO A O   1 
ATOM   430  C  CB  . PRO A 1 60  ? 24.301 8.204   9.597  1.00 58.39  ? 57  PRO A CB  1 
ATOM   431  C  CG  . PRO A 1 60  ? 25.439 8.746   8.792  1.00 58.69  ? 57  PRO A CG  1 
ATOM   432  C  CD  . PRO A 1 60  ? 26.149 7.529   8.303  1.00 59.24  ? 57  PRO A CD  1 
ATOM   433  N  N   . ASP A 1 61  ? 22.865 7.615   6.640  1.00 56.07  ? 58  ASP A N   1 
ATOM   434  C  CA  . ASP A 1 61  ? 21.742 7.850   5.743  1.00 55.09  ? 58  ASP A CA  1 
ATOM   435  C  C   . ASP A 1 61  ? 20.888 6.600   5.580  1.00 57.56  ? 58  ASP A C   1 
ATOM   436  O  O   . ASP A 1 61  ? 19.682 6.704   5.332  1.00 54.78  ? 58  ASP A O   1 
ATOM   437  C  CB  . ASP A 1 61  ? 22.264 8.342   4.400  1.00 63.74  ? 58  ASP A CB  1 
ATOM   438  C  CG  . ASP A 1 61  ? 23.147 9.561   4.545  1.00 73.17  ? 58  ASP A CG  1 
ATOM   439  O  OD1 . ASP A 1 61  ? 22.619 10.628  4.935  1.00 71.13  ? 58  ASP A OD1 1 
ATOM   440  O  OD2 . ASP A 1 61  ? 24.368 9.444   4.308  1.00 81.84  ? 58  ASP A OD2 1 
ATOM   441  N  N   . GLU A 1 62  ? 21.482 5.416   5.747  1.00 53.37  ? 59  GLU A N   1 
ATOM   442  C  CA  . GLU A 1 62  ? 20.709 4.188   5.601  1.00 57.63  ? 59  GLU A CA  1 
ATOM   443  C  C   . GLU A 1 62  ? 19.672 4.054   6.711  1.00 52.27  ? 59  GLU A C   1 
ATOM   444  O  O   . GLU A 1 62  ? 18.610 3.459   6.493  1.00 49.01  ? 59  GLU A O   1 
ATOM   445  C  CB  . GLU A 1 62  ? 21.637 2.969   5.584  1.00 54.07  ? 59  GLU A CB  1 
ATOM   446  C  CG  . GLU A 1 62  ? 22.635 2.960   4.421  1.00 57.06  ? 59  GLU A CG  1 
ATOM   447  C  CD  . GLU A 1 62  ? 21.997 2.641   3.066  1.00 67.80  ? 59  GLU A CD  1 
ATOM   448  O  OE1 . GLU A 1 62  ? 22.291 3.354   2.080  1.00 72.78  ? 59  GLU A OE1 1 
ATOM   449  O  OE2 . GLU A 1 62  ? 21.213 1.673   2.978  1.00 76.40  ? 59  GLU A OE2 1 
ATOM   450  N  N   . ILE A 1 63  ? 19.950 4.603   7.897  1.00 49.47  ? 60  ILE A N   1 
ATOM   451  C  CA  . ILE A 1 63  ? 18.925 4.634   8.937  1.00 48.78  ? 60  ILE A CA  1 
ATOM   452  C  C   . ILE A 1 63  ? 17.753 5.509   8.511  1.00 50.54  ? 60  ILE A C   1 
ATOM   453  O  O   . ILE A 1 63  ? 16.588 5.137   8.696  1.00 49.36  ? 60  ILE A O   1 
ATOM   454  C  CB  . ILE A 1 63  ? 19.524 5.092   10.278 1.00 47.21  ? 60  ILE A CB  1 
ATOM   455  C  CG1 . ILE A 1 63  ? 20.410 3.989   10.865 1.00 44.48  ? 60  ILE A CG1 1 
ATOM   456  C  CG2 . ILE A 1 63  ? 18.431 5.504   11.247 1.00 47.49  ? 60  ILE A CG2 1 
ATOM   457  C  CD1 . ILE A 1 63  ? 20.979 4.320   12.225 1.00 44.07  ? 60  ILE A CD1 1 
ATOM   458  N  N   . LEU A 1 64  ? 18.037 6.667   7.912  1.00 49.95  ? 61  LEU A N   1 
ATOM   459  C  CA  . LEU A 1 64  ? 16.977 7.552   7.438  1.00 52.33  ? 61  LEU A CA  1 
ATOM   460  C  C   . LEU A 1 64  ? 16.097 6.907   6.378  1.00 55.56  ? 61  LEU A C   1 
ATOM   461  O  O   . LEU A 1 64  ? 14.941 7.315   6.217  1.00 58.51  ? 61  LEU A O   1 
ATOM   462  C  CB  . LEU A 1 64  ? 17.570 8.837   6.868  1.00 53.53  ? 61  LEU A CB  1 
ATOM   463  C  CG  . LEU A 1 64  ? 18.469 9.647   7.791  1.00 55.44  ? 61  LEU A CG  1 
ATOM   464  C  CD1 . LEU A 1 64  ? 18.980 10.872  7.049  1.00 59.63  ? 61  LEU A CD1 1 
ATOM   465  C  CD2 . LEU A 1 64  ? 17.733 10.028  9.073  1.00 56.27  ? 61  LEU A CD2 1 
ATOM   466  N  N   . LYS A 1 65  ? 16.611 5.924   5.648  1.00 53.45  ? 62  LYS A N   1 
ATOM   467  C  CA  . LYS A 1 65  ? 15.824 5.231   4.640  1.00 52.03  ? 62  LYS A CA  1 
ATOM   468  C  C   . LYS A 1 65  ? 15.110 4.008   5.187  1.00 53.14  ? 62  LYS A C   1 
ATOM   469  O  O   . LYS A 1 65  ? 14.369 3.364   4.438  1.00 52.23  ? 62  LYS A O   1 
ATOM   470  C  CB  . LYS A 1 65  ? 16.699 4.806   3.456  1.00 50.63  ? 62  LYS A CB  1 
ATOM   471  C  CG  . LYS A 1 65  ? 17.279 5.946   2.645  1.00 59.87  ? 62  LYS A CG  1 
ATOM   472  C  CD  . LYS A 1 65  ? 18.359 5.437   1.703  1.00 69.80  ? 62  LYS A CD  1 
ATOM   473  C  CE  . LYS A 1 65  ? 19.596 6.324   1.731  1.00 76.09  ? 62  LYS A CE  1 
ATOM   474  N  NZ  . LYS A 1 65  ? 20.844 5.515   1.616  1.00 75.36  ? 62  LYS A NZ  1 
ATOM   475  N  N   . SER A 1 66  ? 15.313 3.678   6.464  1.00 48.63  ? 63  SER A N   1 
ATOM   476  C  CA  . SER A 1 66  ? 14.766 2.483   7.072  1.00 45.60  ? 63  SER A CA  1 
ATOM   477  C  C   . SER A 1 66  ? 13.652 2.892   8.046  1.00 47.04  ? 63  SER A C   1 
ATOM   478  O  O   . SER A 1 66  ? 13.054 3.969   7.904  1.00 51.30  ? 63  SER A O   1 
ATOM   479  C  CB  . SER A 1 66  ? 15.900 1.694   7.732  1.00 43.52  ? 63  SER A CB  1 
ATOM   480  O  OG  . SER A 1 66  ? 15.434 0.473   8.256  1.00 43.14  ? 63  SER A OG  1 
ATOM   481  N  N   . SER A 1 67  ? 13.381 2.043   9.037  1.00 43.71  ? 64  SER A N   1 
ATOM   482  C  CA  . SER A 1 67  ? 12.225 2.279   9.896  1.00 46.22  ? 64  SER A CA  1 
ATOM   483  C  C   . SER A 1 67  ? 12.255 1.393   11.139 1.00 42.76  ? 64  SER A C   1 
ATOM   484  O  O   . SER A 1 67  ? 12.688 0.236   11.065 1.00 39.54  ? 64  SER A O   1 
ATOM   485  C  CB  . SER A 1 67  ? 10.956 2.054   9.070  1.00 44.46  ? 64  SER A CB  1 
ATOM   486  O  OG  . SER A 1 67  ? 9.884  1.543   9.820  1.00 50.55  ? 64  SER A OG  1 
ATOM   487  N  N   . PRO A 1 68  ? 11.837 1.903   12.307 1.00 42.02  ? 65  PRO A N   1 
ATOM   488  C  CA  . PRO A 1 68  ? 11.754 1.036   13.497 1.00 41.23  ? 65  PRO A CA  1 
ATOM   489  C  C   . PRO A 1 68  ? 10.916 -0.206  13.263 1.00 38.04  ? 65  PRO A C   1 
ATOM   490  O  O   . PRO A 1 68  ? 11.168 -1.259  13.866 1.00 36.10  ? 65  PRO A O   1 
ATOM   491  C  CB  . PRO A 1 68  ? 11.111 1.941   14.559 1.00 41.80  ? 65  PRO A CB  1 
ATOM   492  C  CG  . PRO A 1 68  ? 11.329 3.351   14.091 1.00 44.81  ? 65  PRO A CG  1 
ATOM   493  C  CD  . PRO A 1 68  ? 11.723 3.338   12.633 1.00 43.80  ? 65  PRO A CD  1 
ATOM   494  N  N   . PHE A 1 69  ? 9.900  -0.092  12.411 1.00 41.06  ? 66  PHE A N   1 
ATOM   495  C  CA  . PHE A 1 69  ? 9.072  -1.235  12.045 1.00 40.58  ? 66  PHE A CA  1 
ATOM   496  C  C   . PHE A 1 69  ? 9.898  -2.333  11.380 1.00 40.81  ? 66  PHE A C   1 
ATOM   497  O  O   . PHE A 1 69  ? 9.705  -3.522  11.667 1.00 40.65  ? 66  PHE A O   1 
ATOM   498  C  CB  . PHE A 1 69  ? 7.923  -0.725  11.172 1.00 50.21  ? 66  PHE A CB  1 
ATOM   499  C  CG  . PHE A 1 69  ? 7.101  -1.791  10.518 1.00 54.45  ? 66  PHE A CG  1 
ATOM   500  C  CD1 . PHE A 1 69  ? 5.859  -2.138  11.038 1.00 60.37  ? 66  PHE A CD1 1 
ATOM   501  C  CD2 . PHE A 1 69  ? 7.475  -2.309  9.279  1.00 58.74  ? 66  PHE A CD2 1 
ATOM   502  C  CE1 . PHE A 1 69  ? 5.065  -3.091  10.407 1.00 61.97  ? 66  PHE A CE1 1 
ATOM   503  C  CE2 . PHE A 1 69  ? 6.683  -3.244  8.631  1.00 59.54  ? 66  PHE A CE2 1 
ATOM   504  C  CZ  . PHE A 1 69  ? 5.472  -3.635  9.197  1.00 61.75  ? 66  PHE A CZ  1 
ATOM   505  N  N   . VAL A 1 70  ? 10.846 -1.959  10.515 1.00 38.05  ? 67  VAL A N   1 
ATOM   506  C  CA  . VAL A 1 70  ? 11.786 -2.944  9.987  1.00 36.27  ? 67  VAL A CA  1 
ATOM   507  C  C   . VAL A 1 70  ? 12.690 -3.482  11.093 1.00 34.44  ? 67  VAL A C   1 
ATOM   508  O  O   . VAL A 1 70  ? 12.929 -4.694  11.188 1.00 35.06  ? 67  VAL A O   1 
ATOM   509  C  CB  . VAL A 1 70  ? 12.600 -2.329  8.834  1.00 36.51  ? 67  VAL A CB  1 
ATOM   510  C  CG1 . VAL A 1 70  ? 13.657 -3.294  8.385  1.00 38.19  ? 67  VAL A CG1 1 
ATOM   511  C  CG2 . VAL A 1 70  ? 11.678 -2.008  7.684  1.00 41.80  ? 67  VAL A CG2 1 
ATOM   512  N  N   . TRP A 1 71  ? 13.204 -2.602  11.953 1.00 35.38  ? 68  TRP A N   1 
ATOM   513  C  CA  . TRP A 1 71  ? 14.150 -3.050  12.975 1.00 32.79  ? 68  TRP A CA  1 
ATOM   514  C  C   . TRP A 1 71  ? 13.522 -4.061  13.926 1.00 30.70  ? 68  TRP A C   1 
ATOM   515  O  O   . TRP A 1 71  ? 14.196 -4.994  14.373 1.00 30.04  ? 68  TRP A O   1 
ATOM   516  C  CB  . TRP A 1 71  ? 14.701 -1.856  13.757 1.00 34.62  ? 68  TRP A CB  1 
ATOM   517  C  CG  . TRP A 1 71  ? 15.202 -0.760  12.858 1.00 34.63  ? 68  TRP A CG  1 
ATOM   518  C  CD1 . TRP A 1 71  ? 15.611 -0.888  11.562 1.00 37.14  ? 68  TRP A CD1 1 
ATOM   519  C  CD2 . TRP A 1 71  ? 15.316 0.630   13.183 1.00 37.78  ? 68  TRP A CD2 1 
ATOM   520  N  NE1 . TRP A 1 71  ? 15.977 0.344   11.058 1.00 39.13  ? 68  TRP A NE1 1 
ATOM   521  C  CE2 . TRP A 1 71  ? 15.811 1.288   12.038 1.00 38.73  ? 68  TRP A CE2 1 
ATOM   522  C  CE3 . TRP A 1 71  ? 15.060 1.382   14.335 1.00 39.99  ? 68  TRP A CE3 1 
ATOM   523  C  CZ2 . TRP A 1 71  ? 16.044 2.663   12.008 1.00 43.62  ? 68  TRP A CZ2 1 
ATOM   524  C  CZ3 . TRP A 1 71  ? 15.290 2.753   14.301 1.00 39.57  ? 68  TRP A CZ3 1 
ATOM   525  C  CH2 . TRP A 1 71  ? 15.783 3.374   13.149 1.00 41.01  ? 68  TRP A CH2 1 
ATOM   526  N  N   . PHE A 1 72  ? 12.238 -3.912  14.246 1.00 31.27  ? 69  PHE A N   1 
ATOM   527  C  CA  . PHE A 1 72  ? 11.629 -4.928  15.098 1.00 30.34  ? 69  PHE A CA  1 
ATOM   528  C  C   . PHE A 1 72  ? 11.500 -6.254  14.354 1.00 30.23  ? 69  PHE A C   1 
ATOM   529  O  O   . PHE A 1 72  ? 11.732 -7.314  14.938 1.00 29.21  ? 69  PHE A O   1 
ATOM   530  C  CB  . PHE A 1 72  ? 10.276 -4.460  15.642 1.00 32.25  ? 69  PHE A CB  1 
ATOM   531  C  CG  . PHE A 1 72  ? 9.631  -5.469  16.564 1.00 30.94  ? 69  PHE A CG  1 
ATOM   532  C  CD1 . PHE A 1 72  ? 10.258 -5.849  17.737 1.00 29.82  ? 69  PHE A CD1 1 
ATOM   533  C  CD2 . PHE A 1 72  ? 8.413  -6.052  16.237 1.00 33.20  ? 69  PHE A CD2 1 
ATOM   534  C  CE1 . PHE A 1 72  ? 9.679  -6.802  18.581 1.00 30.05  ? 69  PHE A CE1 1 
ATOM   535  C  CE2 . PHE A 1 72  ? 7.827  -6.993  17.073 1.00 31.50  ? 69  PHE A CE2 1 
ATOM   536  C  CZ  . PHE A 1 72  ? 8.460  -7.377  18.238 1.00 26.57  ? 69  PHE A CZ  1 
ATOM   537  N  N   . LYS A 1 73  ? 11.155 -6.229  13.060 1.00 30.98  ? 70  LYS A N   1 
ATOM   538  C  CA  . LYS A 1 73  ? 11.213 -7.485  12.305 1.00 31.92  ? 70  LYS A CA  1 
ATOM   539  C  C   . LYS A 1 73  ? 12.615 -8.066  12.242 1.00 30.46  ? 70  LYS A C   1 
ATOM   540  O  O   . LYS A 1 73  ? 12.764 -9.288  12.188 1.00 32.88  ? 70  LYS A O   1 
ATOM   541  C  CB  . LYS A 1 73  ? 10.675 -7.324  10.890 1.00 36.57  ? 70  LYS A CB  1 
ATOM   542  C  CG  . LYS A 1 73  ? 9.512  -6.432  10.708 1.00 45.20  ? 70  LYS A CG  1 
ATOM   543  C  CD  . LYS A 1 73  ? 8.499  -7.240  9.894  1.00 59.39  ? 70  LYS A CD  1 
ATOM   544  C  CE  . LYS A 1 73  ? 7.349  -6.401  9.405  1.00 55.88  ? 70  LYS A CE  1 
ATOM   545  N  NZ  . LYS A 1 73  ? 7.199  -6.442  7.913  1.00 59.38  ? 70  LYS A NZ  1 
ATOM   546  N  N   . ASP A 1 74  ? 13.650 -7.222  12.227 1.00 32.40  ? 71  ASP A N   1 
ATOM   547  C  CA  . ASP A 1 74  ? 15.017 -7.739  12.302 1.00 32.96  ? 71  ASP A CA  1 
ATOM   548  C  C   . ASP A 1 74  ? 15.245 -8.487  13.616 1.00 32.40  ? 71  ASP A C   1 
ATOM   549  O  O   . ASP A 1 74  ? 15.935 -9.517  13.652 1.00 31.29  ? 71  ASP A O   1 
ATOM   550  C  CB  . ASP A 1 74  ? 16.024 -6.588  12.159 1.00 33.33  ? 71  ASP A CB  1 
ATOM   551  C  CG  . ASP A 1 74  ? 16.049 -5.972  10.759 1.00 37.20  ? 71  ASP A CG  1 
ATOM   552  O  OD1 . ASP A 1 74  ? 15.788 -6.665  9.741  1.00 37.51  ? 71  ASP A OD1 1 
ATOM   553  O  OD2 . ASP A 1 74  ? 16.321 -4.754  10.677 1.00 38.67  ? 71  ASP A OD2 1 
ATOM   554  N  N   . ALA A 1 75  ? 14.671 -7.979  14.712 1.00 29.04  ? 72  ALA A N   1 
ATOM   555  C  CA  . ALA A 1 75  ? 14.750 -8.674  15.994 1.00 28.06  ? 72  ALA A CA  1 
ATOM   556  C  C   . ALA A 1 75  ? 13.993 -9.996  15.955 1.00 28.26  ? 72  ALA A C   1 
ATOM   557  O  O   . ALA A 1 75  ? 14.501 -11.024 16.416 1.00 26.54  ? 72  ALA A O   1 
ATOM   558  C  CB  . ALA A 1 75  ? 14.213 -7.768  17.109 1.00 27.91  ? 72  ALA A CB  1 
ATOM   559  N  N   . LEU A 1 76  ? 12.768 -9.988  15.413 1.00 28.73  ? 73  LEU A N   1 
ATOM   560  C  CA  . LEU A 1 76  ? 12.005 -11.226 15.238 1.00 28.60  ? 73  LEU A CA  1 
ATOM   561  C  C   . LEU A 1 76  ? 12.741 -12.218 14.348 1.00 29.69  ? 73  LEU A C   1 
ATOM   562  O  O   . LEU A 1 76  ? 12.741 -13.426 14.621 1.00 27.87  ? 73  LEU A O   1 
ATOM   563  C  CB  . LEU A 1 76  ? 10.626 -10.934 14.631 1.00 27.06  ? 73  LEU A CB  1 
ATOM   564  C  CG  . LEU A 1 76  ? 9.671  -10.134 15.532 1.00 29.92  ? 73  LEU A CG  1 
ATOM   565  C  CD1 . LEU A 1 76  ? 8.378  -9.818  14.769 1.00 33.46  ? 73  LEU A CD1 1 
ATOM   566  C  CD2 . LEU A 1 76  ? 9.412  -10.883 16.857 1.00 30.25  ? 73  LEU A CD2 1 
ATOM   567  N  N   . ASP A 1 77  ? 13.348 -11.730 13.261 1.00 29.36  ? 74  ASP A N   1 
ATOM   568  C  CA  . ASP A 1 77  ? 14.127 -12.608 12.389 1.00 30.20  ? 74  ASP A CA  1 
ATOM   569  C  C   . ASP A 1 77  ? 15.271 -13.261 13.152 1.00 28.30  ? 74  ASP A C   1 
ATOM   570  O  O   . ASP A 1 77  ? 15.626 -14.411 12.871 1.00 30.33  ? 74  ASP A O   1 
ATOM   571  C  CB  . ASP A 1 77  ? 14.696 -11.832 11.200 1.00 32.47  ? 74  ASP A CB  1 
ATOM   572  C  CG  . ASP A 1 77  ? 13.655 -11.493 10.154 1.00 39.51  ? 74  ASP A CG  1 
ATOM   573  O  OD1 . ASP A 1 77  ? 12.556 -12.098 10.160 1.00 38.36  ? 74  ASP A OD1 1 
ATOM   574  O  OD2 . ASP A 1 77  ? 13.974 -10.652 9.270  1.00 39.71  ? 74  ASP A OD2 1 
ATOM   575  N  N   . GLY A 1 78  ? 15.861 -12.540 14.109 1.00 27.39  ? 75  GLY A N   1 
ATOM   576  C  CA  . GLY A 1 78  ? 16.932 -13.112 14.916 1.00 27.53  ? 75  GLY A CA  1 
ATOM   577  C  C   . GLY A 1 78  ? 16.460 -14.247 15.802 1.00 28.05  ? 75  GLY A C   1 
ATOM   578  O  O   . GLY A 1 78  ? 17.142 -15.270 15.935 1.00 27.55  ? 75  GLY A O   1 
ATOM   579  N  N   . TYR A 1 79  ? 15.299 -14.079 16.438 1.00 26.37  ? 76  TYR A N   1 
ATOM   580  C  CA  . TYR A 1 79  ? 14.707 -15.192 17.171 1.00 23.52  ? 76  TYR A CA  1 
ATOM   581  C  C   . TYR A 1 79  ? 14.485 -16.376 16.247 1.00 25.21  ? 76  TYR A C   1 
ATOM   582  O  O   . TYR A 1 79  ? 14.859 -17.509 16.570 1.00 26.30  ? 76  TYR A O   1 
ATOM   583  C  CB  . TYR A 1 79  ? 13.382 -14.758 17.808 1.00 26.17  ? 76  TYR A CB  1 
ATOM   584  C  CG  . TYR A 1 79  ? 12.644 -15.865 18.550 1.00 26.94  ? 76  TYR A CG  1 
ATOM   585  C  CD1 . TYR A 1 79  ? 11.862 -16.799 17.871 1.00 26.02  ? 76  TYR A CD1 1 
ATOM   586  C  CD2 . TYR A 1 79  ? 12.723 -15.962 19.934 1.00 23.89  ? 76  TYR A CD2 1 
ATOM   587  C  CE1 . TYR A 1 79  ? 11.188 -17.808 18.559 1.00 27.23  ? 76  TYR A CE1 1 
ATOM   588  C  CE2 . TYR A 1 79  ? 12.063 -16.962 20.623 1.00 24.57  ? 76  TYR A CE2 1 
ATOM   589  C  CZ  . TYR A 1 79  ? 11.304 -17.882 19.937 1.00 25.12  ? 76  TYR A CZ  1 
ATOM   590  O  OH  . TYR A 1 79  ? 10.662 -18.867 20.647 1.00 25.91  ? 76  TYR A OH  1 
ATOM   591  N  N   . ASP A 1 80  ? 13.846 -16.133 15.091 1.00 26.18  ? 77  ASP A N   1 
ATOM   592  C  CA  . ASP A 1 80  ? 13.539 -17.221 14.173 1.00 26.05  ? 77  ASP A CA  1 
ATOM   593  C  C   . ASP A 1 80  ? 14.812 -17.887 13.657 1.00 30.12  ? 77  ASP A C   1 
ATOM   594  O  O   . ASP A 1 80  ? 14.819 -19.092 13.391 1.00 30.16  ? 77  ASP A O   1 
ATOM   595  C  CB  . ASP A 1 80  ? 12.689 -16.702 13.007 1.00 30.51  ? 77  ASP A CB  1 
ATOM   596  C  CG  . ASP A 1 80  ? 11.316 -16.199 13.458 1.00 33.32  ? 77  ASP A CG  1 
ATOM   597  O  OD1 . ASP A 1 80  ? 10.883 -16.582 14.559 1.00 30.96  ? 77  ASP A OD1 1 
ATOM   598  O  OD2 . ASP A 1 80  ? 10.664 -15.435 12.704 1.00 28.77  ? 77  ASP A OD2 1 
ATOM   599  N  N   . TYR A 1 81  ? 15.896 -17.124 13.527 1.00 28.64  ? 78  TYR A N   1 
ATOM   600  C  CA  . TYR A 1 81  ? 17.176 -17.706 13.127 1.00 31.07  ? 78  TYR A CA  1 
ATOM   601  C  C   . TYR A 1 81  ? 17.689 -18.691 14.181 1.00 28.35  ? 78  TYR A C   1 
ATOM   602  O  O   . TYR A 1 81  ? 18.102 -19.814 13.858 1.00 29.24  ? 78  TYR A O   1 
ATOM   603  C  CB  . TYR A 1 81  ? 18.189 -16.588 12.890 1.00 31.69  ? 78  TYR A CB  1 
ATOM   604  C  CG  . TYR A 1 81  ? 19.561 -17.085 12.475 1.00 30.83  ? 78  TYR A CG  1 
ATOM   605  C  CD1 . TYR A 1 81  ? 19.780 -17.615 11.212 1.00 38.80  ? 78  TYR A CD1 1 
ATOM   606  C  CD2 . TYR A 1 81  ? 20.638 -17.027 13.364 1.00 32.62  ? 78  TYR A CD2 1 
ATOM   607  C  CE1 . TYR A 1 81  ? 21.038 -18.077 10.825 1.00 39.01  ? 78  TYR A CE1 1 
ATOM   608  C  CE2 . TYR A 1 81  ? 21.902 -17.479 12.980 1.00 36.44  ? 78  TYR A CE2 1 
ATOM   609  C  CZ  . TYR A 1 81  ? 22.092 -17.999 11.725 1.00 38.18  ? 78  TYR A CZ  1 
ATOM   610  O  OH  . TYR A 1 81  ? 23.338 -18.456 11.340 1.00 42.23  ? 78  TYR A OH  1 
ATOM   611  N  N   . LEU A 1 82  ? 17.635 -18.298 15.451 1.00 27.28  ? 79  LEU A N   1 
ATOM   612  C  CA  . LEU A 1 82  ? 18.040 -19.209 16.517 1.00 27.86  ? 79  LEU A CA  1 
ATOM   613  C  C   . LEU A 1 82  ? 17.249 -20.504 16.453 1.00 28.99  ? 79  LEU A C   1 
ATOM   614  O  O   . LEU A 1 82  ? 17.812 -21.596 16.599 1.00 28.72  ? 79  LEU A O   1 
ATOM   615  C  CB  . LEU A 1 82  ? 17.858 -18.536 17.880 1.00 25.57  ? 79  LEU A CB  1 
ATOM   616  C  CG  . LEU A 1 82  ? 18.970 -17.582 18.326 1.00 27.39  ? 79  LEU A CG  1 
ATOM   617  C  CD1 . LEU A 1 82  ? 18.561 -16.796 19.578 1.00 25.21  ? 79  LEU A CD1 1 
ATOM   618  C  CD2 . LEU A 1 82  ? 20.254 -18.360 18.611 1.00 27.75  ? 79  LEU A CD2 1 
ATOM   619  N  N   . VAL A 1 83  ? 15.938 -20.405 16.236 1.00 25.68  ? 80  VAL A N   1 
ATOM   620  C  CA  . VAL A 1 83  ? 15.121 -21.611 16.147 1.00 28.09  ? 80  VAL A CA  1 
ATOM   621  C  C   . VAL A 1 83  ? 15.521 -22.449 14.933 1.00 29.98  ? 80  VAL A C   1 
ATOM   622  O  O   . VAL A 1 83  ? 15.652 -23.676 15.028 1.00 33.25  ? 80  VAL A O   1 
ATOM   623  C  CB  . VAL A 1 83  ? 13.629 -21.239 16.125 1.00 28.13  ? 80  VAL A CB  1 
ATOM   624  C  CG1 . VAL A 1 83  ? 12.793 -22.485 15.871 1.00 31.57  ? 80  VAL A CG1 1 
ATOM   625  C  CG2 . VAL A 1 83  ? 13.254 -20.581 17.454 1.00 25.62  ? 80  VAL A CG2 1 
ATOM   626  N  N   . GLU A 1 84  ? 15.723 -21.807 13.775 1.00 28.83  ? 81  GLU A N   1 
ATOM   627  C  CA  . GLU A 1 84  ? 16.162 -22.554 12.593 1.00 31.89  ? 81  GLU A CA  1 
ATOM   628  C  C   . GLU A 1 84  ? 17.499 -23.250 12.822 1.00 32.51  ? 81  GLU A C   1 
ATOM   629  O  O   . GLU A 1 84  ? 17.761 -24.301 12.226 1.00 34.60  ? 81  GLU A O   1 
ATOM   630  C  CB  . GLU A 1 84  ? 16.277 -21.646 11.362 1.00 37.82  ? 81  GLU A CB  1 
ATOM   631  C  CG  . GLU A 1 84  ? 14.979 -20.970 10.896 1.00 44.85  ? 81  GLU A CG  1 
ATOM   632  C  CD  . GLU A 1 84  ? 15.222 -19.894 9.825  1.00 53.41  ? 81  GLU A CD  1 
ATOM   633  O  OE1 . GLU A 1 84  ? 16.395 -19.489 9.620  1.00 52.73  ? 81  GLU A OE1 1 
ATOM   634  O  OE2 . GLU A 1 84  ? 14.237 -19.442 9.201  1.00 54.02  ? 81  GLU A OE2 1 
ATOM   635  N  N   . GLN A 1 85  ? 18.363 -22.667 13.641 1.00 32.77  ? 82  GLN A N   1 
ATOM   636  C  CA  . GLN A 1 85  ? 19.689 -23.212 13.904 1.00 35.91  ? 82  GLN A CA  1 
ATOM   637  C  C   . GLN A 1 85  ? 19.694 -24.231 15.036 1.00 37.55  ? 82  GLN A C   1 
ATOM   638  O  O   . GLN A 1 85  ? 20.760 -24.752 15.378 1.00 33.49  ? 82  GLN A O   1 
ATOM   639  C  CB  . GLN A 1 85  ? 20.666 -22.074 14.215 1.00 32.32  ? 82  GLN A CB  1 
ATOM   640  C  CG  . GLN A 1 85  ? 20.844 -21.124 13.041 1.00 34.18  ? 82  GLN A CG  1 
ATOM   641  C  CD  . GLN A 1 85  ? 21.621 -21.770 11.904 1.00 39.30  ? 82  GLN A CD  1 
ATOM   642  O  OE1 . GLN A 1 85  ? 22.576 -22.506 12.138 1.00 41.06  ? 82  GLN A OE1 1 
ATOM   643  N  NE2 . GLN A 1 85  ? 21.213 -21.502 10.672 1.00 40.05  ? 82  GLN A NE2 1 
ATOM   644  N  N   . GLY A 1 86  ? 18.539 -24.540 15.604 1.00 31.54  ? 83  GLY A N   1 
ATOM   645  C  CA  . GLY A 1 86  ? 18.408 -25.633 16.535 1.00 37.04  ? 83  GLY A CA  1 
ATOM   646  C  C   . GLY A 1 86  ? 18.214 -25.253 17.988 1.00 36.20  ? 83  GLY A C   1 
ATOM   647  O  O   . GLY A 1 86  ? 18.339 -26.130 18.853 1.00 35.42  ? 83  GLY A O   1 
ATOM   648  N  N   . TYR A 1 87  ? 17.901 -23.992 18.285 1.00 30.69  ? 84  TYR A N   1 
ATOM   649  C  CA  . TYR A 1 87  ? 17.782 -23.501 19.657 1.00 26.35  ? 84  TYR A CA  1 
ATOM   650  C  C   . TYR A 1 87  ? 16.341 -23.063 19.886 1.00 32.63  ? 84  TYR A C   1 
ATOM   651  O  O   . TYR A 1 87  ? 15.919 -22.028 19.364 1.00 32.49  ? 84  TYR A O   1 
ATOM   652  C  CB  . TYR A 1 87  ? 18.748 -22.349 19.888 1.00 26.43  ? 84  TYR A CB  1 
ATOM   653  C  CG  . TYR A 1 87  ? 20.178 -22.758 19.630 1.00 29.51  ? 84  TYR A CG  1 
ATOM   654  C  CD1 . TYR A 1 87  ? 20.952 -23.327 20.636 1.00 27.12  ? 84  TYR A CD1 1 
ATOM   655  C  CD2 . TYR A 1 87  ? 20.737 -22.615 18.369 1.00 31.29  ? 84  TYR A CD2 1 
ATOM   656  C  CE1 . TYR A 1 87  ? 22.258 -23.735 20.389 1.00 30.12  ? 84  TYR A CE1 1 
ATOM   657  C  CE2 . TYR A 1 87  ? 22.036 -23.018 18.108 1.00 31.80  ? 84  TYR A CE2 1 
ATOM   658  C  CZ  . TYR A 1 87  ? 22.790 -23.574 19.114 1.00 33.84  ? 84  TYR A CZ  1 
ATOM   659  O  OH  . TYR A 1 87  ? 24.074 -23.968 18.839 1.00 33.60  ? 84  TYR A OH  1 
ATOM   660  N  N   . ASP A 1 88  ? 15.597 -23.854 20.660 1.00 29.39  ? 85  ASP A N   1 
ATOM   661  C  CA  . ASP A 1 88  ? 14.177 -23.621 20.908 1.00 34.76  ? 85  ASP A CA  1 
ATOM   662  C  C   . ASP A 1 88  ? 13.923 -22.815 22.174 1.00 31.36  ? 85  ASP A C   1 
ATOM   663  O  O   . ASP A 1 88  ? 12.874 -22.162 22.283 1.00 32.15  ? 85  ASP A O   1 
ATOM   664  C  CB  . ASP A 1 88  ? 13.419 -24.949 21.056 1.00 36.69  ? 85  ASP A CB  1 
ATOM   665  C  CG  . ASP A 1 88  ? 13.389 -25.759 19.780 1.00 49.72  ? 85  ASP A CG  1 
ATOM   666  O  OD1 . ASP A 1 88  ? 13.165 -25.177 18.690 1.00 49.20  ? 85  ASP A OD1 1 
ATOM   667  O  OD2 . ASP A 1 88  ? 13.543 -26.997 19.873 1.00 47.06  ? 85  ASP A OD2 1 
ATOM   668  N  N   . GLU A 1 89  ? 14.842 -22.875 23.144 1.00 25.77  ? 86  GLU A N   1 
ATOM   669  C  CA  . GLU A 1 89  ? 14.693 -22.185 24.422 1.00 26.37  ? 86  GLU A CA  1 
ATOM   670  C  C   . GLU A 1 89  ? 15.591 -20.958 24.423 1.00 26.93  ? 86  GLU A C   1 
ATOM   671  O  O   . GLU A 1 89  ? 16.819 -21.077 24.390 1.00 26.32  ? 86  GLU A O   1 
ATOM   672  C  CB  . GLU A 1 89  ? 15.022 -23.128 25.581 1.00 30.05  ? 86  GLU A CB  1 
ATOM   673  C  CG  . GLU A 1 89  ? 14.420 -24.513 25.375 1.00 33.94  ? 86  GLU A CG  1 
ATOM   674  C  CD  . GLU A 1 89  ? 14.258 -25.297 26.669 1.00 42.13  ? 86  GLU A CD  1 
ATOM   675  O  OE1 . GLU A 1 89  ? 15.070 -25.097 27.599 1.00 37.47  ? 86  GLU A OE1 1 
ATOM   676  O  OE2 . GLU A 1 89  ? 13.326 -26.132 26.741 1.00 43.51  ? 86  GLU A OE2 1 
ATOM   677  N  N   . ILE A 1 90  ? 14.974 -19.784 24.487 1.00 22.35  ? 87  ILE A N   1 
ATOM   678  C  CA  . ILE A 1 90  ? 15.644 -18.534 24.148 1.00 23.55  ? 87  ILE A CA  1 
ATOM   679  C  C   . ILE A 1 90  ? 15.221 -17.492 25.167 1.00 26.41  ? 87  ILE A C   1 
ATOM   680  O  O   . ILE A 1 90  ? 14.030 -17.353 25.463 1.00 24.94  ? 87  ILE A O   1 
ATOM   681  C  CB  . ILE A 1 90  ? 15.278 -18.065 22.718 1.00 23.70  ? 87  ILE A CB  1 
ATOM   682  C  CG1 . ILE A 1 90  ? 15.827 -19.025 21.655 1.00 22.99  ? 87  ILE A CG1 1 
ATOM   683  C  CG2 . ILE A 1 90  ? 15.747 -16.631 22.451 1.00 23.53  ? 87  ILE A CG2 1 
ATOM   684  C  CD1 . ILE A 1 90  ? 15.148 -18.832 20.289 1.00 25.72  ? 87  ILE A CD1 1 
ATOM   685  N  N   . VAL A 1 91  ? 16.190 -16.793 25.718 1.00 23.92  ? 88  VAL A N   1 
ATOM   686  C  CA  . VAL A 1 91  ? 15.973 -15.568 26.482 1.00 23.86  ? 88  VAL A CA  1 
ATOM   687  C  C   . VAL A 1 91  ? 16.276 -14.395 25.563 1.00 25.67  ? 88  VAL A C   1 
ATOM   688  O  O   . VAL A 1 91  ? 17.232 -14.458 24.782 1.00 26.14  ? 88  VAL A O   1 
ATOM   689  C  CB  . VAL A 1 91  ? 16.885 -15.544 27.719 1.00 21.39  ? 88  VAL A CB  1 
ATOM   690  C  CG1 . VAL A 1 91  ? 16.993 -14.118 28.297 1.00 22.47  ? 88  VAL A CG1 1 
ATOM   691  C  CG2 . VAL A 1 91  ? 16.366 -16.531 28.785 1.00 22.44  ? 88  VAL A CG2 1 
ATOM   692  N  N   . VAL A 1 92  ? 15.489 -13.321 25.637 1.00 21.86  ? 89  VAL A N   1 
ATOM   693  C  CA  . VAL A 1 92  ? 15.764 -12.142 24.822 1.00 23.26  ? 89  VAL A CA  1 
ATOM   694  C  C   . VAL A 1 92  ? 16.277 -11.036 25.728 1.00 26.31  ? 89  VAL A C   1 
ATOM   695  O  O   . VAL A 1 92  ? 15.687 -10.745 26.772 1.00 24.22  ? 89  VAL A O   1 
ATOM   696  C  CB  . VAL A 1 92  ? 14.533 -11.710 23.995 1.00 23.66  ? 89  VAL A CB  1 
ATOM   697  C  CG1 . VAL A 1 92  ? 13.332 -11.348 24.902 1.00 23.09  ? 89  VAL A CG1 1 
ATOM   698  C  CG2 . VAL A 1 92  ? 14.902 -10.566 23.051 1.00 22.10  ? 89  VAL A CG2 1 
ATOM   699  N  N   . ALA A 1 93  ? 17.413 -10.455 25.354 1.00 24.38  ? 90  ALA A N   1 
ATOM   700  C  CA  . ALA A 1 93  ? 18.093 -9.472  26.184 1.00 25.02  ? 90  ALA A CA  1 
ATOM   701  C  C   . ALA A 1 93  ? 18.400 -8.290  25.290 1.00 26.38  ? 90  ALA A C   1 
ATOM   702  O  O   . ALA A 1 93  ? 18.958 -8.466  24.201 1.00 27.73  ? 90  ALA A O   1 
ATOM   703  C  CB  . ALA A 1 93  ? 19.383 -10.034 26.797 1.00 24.86  ? 90  ALA A CB  1 
ATOM   704  N  N   . GLY A 1 94  ? 17.986 -7.110  25.698 1.00 24.94  ? 91  GLY A N   1 
ATOM   705  C  CA  . GLY A 1 94  ? 18.020 -5.956  24.813 1.00 26.30  ? 91  GLY A CA  1 
ATOM   706  C  C   . GLY A 1 94  ? 18.561 -4.730  25.507 1.00 28.64  ? 91  GLY A C   1 
ATOM   707  O  O   . GLY A 1 94  ? 18.242 -4.469  26.661 1.00 26.91  ? 91  GLY A O   1 
ATOM   708  N  N   . LEU A 1 95  ? 19.374 -3.973  24.770 1.00 26.96  ? 92  LEU A N   1 
ATOM   709  C  CA  . LEU A 1 95  ? 20.019 -2.755  25.250 1.00 28.08  ? 92  LEU A CA  1 
ATOM   710  C  C   . LEU A 1 95  ? 19.319 -1.545  24.637 1.00 30.19  ? 92  LEU A C   1 
ATOM   711  O  O   . LEU A 1 95  ? 19.221 -1.444  23.408 1.00 29.21  ? 92  LEU A O   1 
ATOM   712  C  CB  . LEU A 1 95  ? 21.496 -2.764  24.843 1.00 29.69  ? 92  LEU A CB  1 
ATOM   713  C  CG  . LEU A 1 95  ? 22.322 -1.510  25.117 1.00 31.45  ? 92  LEU A CG  1 
ATOM   714  C  CD1 . LEU A 1 95  ? 22.402 -1.260  26.652 1.00 32.35  ? 92  LEU A CD1 1 
ATOM   715  C  CD2 . LEU A 1 95  ? 23.707 -1.668  24.518 1.00 33.21  ? 92  LEU A CD2 1 
ATOM   716  N  N   . SER A 1 96  ? 18.854 -0.626  25.482 1.00 28.75  ? 93  SER A N   1 
ATOM   717  C  CA  . SER A 1 96  ? 18.275 0.653   25.037 1.00 29.51  ? 93  SER A CA  1 
ATOM   718  C  C   . SER A 1 96  ? 17.028 0.340   24.212 1.00 31.39  ? 93  SER A C   1 
ATOM   719  O  O   . SER A 1 96  ? 16.135 -0.359  24.715 1.00 28.79  ? 93  SER A O   1 
ATOM   720  C  CB  . SER A 1 96  ? 19.348 1.468   24.320 1.00 36.40  ? 93  SER A CB  1 
ATOM   721  O  OG  . SER A 1 96  ? 19.001 2.845   24.324 1.00 40.43  ? 93  SER A OG  1 
ATOM   722  N  N   . LEU A 1 97  ? 16.905 0.843   22.974 1.00 28.75  ? 94  LEU A N   1 
ATOM   723  C  CA  . LEU A 1 97  ? 15.773 0.451   22.133 1.00 30.16  ? 94  LEU A CA  1 
ATOM   724  C  C   . LEU A 1 97  ? 15.622 -1.066  22.066 1.00 27.60  ? 94  LEU A C   1 
ATOM   725  O  O   . LEU A 1 97  ? 14.501 -1.592  22.054 1.00 28.50  ? 94  LEU A O   1 
ATOM   726  C  CB  . LEU A 1 97  ? 15.941 1.022   20.721 1.00 29.43  ? 94  LEU A CB  1 
ATOM   727  C  CG  . LEU A 1 97  ? 14.906 0.568   19.691 1.00 30.22  ? 94  LEU A CG  1 
ATOM   728  C  CD1 . LEU A 1 97  ? 13.520 1.052   20.097 1.00 32.25  ? 94  LEU A CD1 1 
ATOM   729  C  CD2 . LEU A 1 97  ? 15.255 1.064   18.281 1.00 33.60  ? 94  LEU A CD2 1 
ATOM   730  N  N   . GLY A 1 98  ? 16.740 -1.791  22.005 1.00 26.87  ? 95  GLY A N   1 
ATOM   731  C  CA  . GLY A 1 98  ? 16.664 -3.242  21.994 1.00 26.19  ? 95  GLY A CA  1 
ATOM   732  C  C   . GLY A 1 98  ? 15.968 -3.810  23.216 1.00 27.12  ? 95  GLY A C   1 
ATOM   733  O  O   . GLY A 1 98  ? 15.369 -4.882  23.149 1.00 26.81  ? 95  GLY A O   1 
ATOM   734  N  N   . GLY A 1 99  ? 16.031 -3.098  24.343 1.00 26.47  ? 96  GLY A N   1 
ATOM   735  C  CA  . GLY A 1 99  ? 15.281 -3.517  25.521 1.00 29.28  ? 96  GLY A CA  1 
ATOM   736  C  C   . GLY A 1 99  ? 13.780 -3.382  25.348 1.00 28.15  ? 96  GLY A C   1 
ATOM   737  O  O   . GLY A 1 99  ? 13.019 -4.257  25.762 1.00 26.42  ? 96  GLY A O   1 
ATOM   738  N  N   . ASP A 1 100 ? 13.328 -2.278  24.751 1.00 28.62  ? 97  ASP A N   1 
ATOM   739  C  CA  . ASP A 1 100 ? 11.925 -2.189  24.347 1.00 28.28  ? 97  ASP A CA  1 
ATOM   740  C  C   . ASP A 1 100 ? 11.554 -3.313  23.390 1.00 28.20  ? 97  ASP A C   1 
ATOM   741  O  O   . ASP A 1 100 ? 10.475 -3.912  23.502 1.00 27.62  ? 97  ASP A O   1 
ATOM   742  C  CB  . ASP A 1 100 ? 11.644 -0.846  23.672 1.00 29.34  ? 97  ASP A CB  1 
ATOM   743  C  CG  . ASP A 1 100 ? 11.402 0.263   24.673 1.00 35.49  ? 97  ASP A CG  1 
ATOM   744  O  OD1 . ASP A 1 100 ? 12.317 0.524   25.474 1.00 36.47  ? 97  ASP A OD1 1 
ATOM   745  O  OD2 . ASP A 1 100 ? 10.314 0.866   24.662 1.00 34.74  ? 97  ASP A OD2 1 
ATOM   746  N  N   . PHE A 1 101 ? 12.410 -3.569  22.399 1.00 25.48  ? 98  PHE A N   1 
ATOM   747  C  CA  . PHE A 1 101 ? 12.142 -4.649  21.460 1.00 26.77  ? 98  PHE A CA  1 
ATOM   748  C  C   . PHE A 1 101 ? 12.103 -6.002  22.162 1.00 25.80  ? 98  PHE A C   1 
ATOM   749  O  O   . PHE A 1 101 ? 11.326 -6.876  21.760 1.00 26.31  ? 98  PHE A O   1 
ATOM   750  C  CB  . PHE A 1 101 ? 13.189 -4.667  20.337 1.00 25.28  ? 98  PHE A CB  1 
ATOM   751  C  CG  . PHE A 1 101 ? 13.010 -3.592  19.302 1.00 28.95  ? 98  PHE A CG  1 
ATOM   752  C  CD1 . PHE A 1 101 ? 11.831 -2.861  19.212 1.00 31.97  ? 98  PHE A CD1 1 
ATOM   753  C  CD2 . PHE A 1 101 ? 14.001 -3.372  18.354 1.00 33.14  ? 98  PHE A CD2 1 
ATOM   754  C  CE1 . PHE A 1 101 ? 11.668 -1.894  18.233 1.00 32.08  ? 98  PHE A CE1 1 
ATOM   755  C  CE2 . PHE A 1 101 ? 13.843 -2.405  17.356 1.00 30.97  ? 98  PHE A CE2 1 
ATOM   756  C  CZ  . PHE A 1 101 ? 12.674 -1.666  17.299 1.00 32.39  ? 98  PHE A CZ  1 
ATOM   757  N  N   . ALA A 1 102 ? 12.924 -6.202  23.201 1.00 23.50  ? 99  ALA A N   1 
ATOM   758  C  CA  . ALA A 1 102 ? 12.871 -7.451  23.963 1.00 23.64  ? 99  ALA A CA  1 
ATOM   759  C  C   . ALA A 1 102 ? 11.508 -7.636  24.617 1.00 26.21  ? 99  ALA A C   1 
ATOM   760  O  O   . ALA A 1 102 ? 10.931 -8.732  24.593 1.00 24.02  ? 99  ALA A O   1 
ATOM   761  C  CB  . ALA A 1 102 ? 13.969 -7.462  25.032 1.00 25.35  ? 99  ALA A CB  1 
ATOM   762  N  N   . LEU A 1 103 ? 10.994 -6.574  25.245 1.00 25.87  ? 100 LEU A N   1 
ATOM   763  C  CA  . LEU A 1 103 ? 9.654  -6.618  25.818 1.00 24.59  ? 100 LEU A CA  1 
ATOM   764  C  C   . LEU A 1 103 ? 8.629  -6.979  24.756 1.00 25.64  ? 100 LEU A C   1 
ATOM   765  O  O   . LEU A 1 103 ? 7.827  -7.906  24.942 1.00 26.20  ? 100 LEU A O   1 
ATOM   766  C  CB  . LEU A 1 103 ? 9.328  -5.266  26.459 1.00 25.43  ? 100 LEU A CB  1 
ATOM   767  C  CG  . LEU A 1 103 ? 10.157 -4.944  27.705 1.00 25.46  ? 100 LEU A CG  1 
ATOM   768  C  CD1 . LEU A 1 103 ? 10.033 -3.450  28.053 1.00 26.98  ? 100 LEU A CD1 1 
ATOM   769  C  CD2 . LEU A 1 103 ? 9.711  -5.789  28.911 1.00 25.37  ? 100 LEU A CD2 1 
ATOM   770  N  N   . LYS A 1 104 ? 8.628  -6.241  23.640 1.00 24.83  ? 101 LYS A N   1 
ATOM   771  C  CA  . LYS A 1 104 ? 7.662  -6.493  22.567 1.00 24.05  ? 101 LYS A CA  1 
ATOM   772  C  C   . LYS A 1 104 ? 7.877  -7.865  21.934 1.00 26.58  ? 101 LYS A C   1 
ATOM   773  O  O   . LYS A 1 104 ? 6.910  -8.559  21.600 1.00 25.89  ? 101 LYS A O   1 
ATOM   774  C  CB  . LYS A 1 104 ? 7.755  -5.396  21.500 1.00 26.30  ? 101 LYS A CB  1 
ATOM   775  C  CG  . LYS A 1 104 ? 6.602  -5.410  20.504 1.00 27.19  ? 101 LYS A CG  1 
ATOM   776  C  CD  . LYS A 1 104 ? 6.823  -4.426  19.338 1.00 29.23  ? 101 LYS A CD  1 
ATOM   777  C  CE  . LYS A 1 104 ? 5.555  -4.317  18.478 1.00 34.20  ? 101 LYS A CE  1 
ATOM   778  N  NZ  . LYS A 1 104 ? 4.595  -3.332  19.039 1.00 37.23  ? 101 LYS A NZ  1 
ATOM   779  N  N   . LEU A 1 105 ? 9.132  -8.287  21.775 1.00 23.83  ? 102 LEU A N   1 
ATOM   780  C  CA  . LEU A 1 105 ? 9.374  -9.605  21.195 1.00 23.81  ? 102 LEU A CA  1 
ATOM   781  C  C   . LEU A 1 105 ? 8.793  -10.717 22.063 1.00 23.28  ? 102 LEU A C   1 
ATOM   782  O  O   . LEU A 1 105 ? 8.290  -11.718 21.538 1.00 24.02  ? 102 LEU A O   1 
ATOM   783  C  CB  . LEU A 1 105 ? 10.868 -9.829  20.981 1.00 26.06  ? 102 LEU A CB  1 
ATOM   784  C  CG  . LEU A 1 105 ? 11.237 -11.134 20.264 1.00 23.53  ? 102 LEU A CG  1 
ATOM   785  C  CD1 . LEU A 1 105 ? 12.428 -10.901 19.348 1.00 26.62  ? 102 LEU A CD1 1 
ATOM   786  C  CD2 . LEU A 1 105 ? 11.557 -12.230 21.272 1.00 24.89  ? 102 LEU A CD2 1 
ATOM   787  N  N   . SER A 1 106 ? 8.822  -10.553 23.390 1.00 22.14  ? 103 SER A N   1 
ATOM   788  C  CA  . SER A 1 106 ? 8.273  -11.586 24.263 1.00 23.02  ? 103 SER A CA  1 
ATOM   789  C  C   . SER A 1 106 ? 6.771  -11.759 24.070 1.00 23.85  ? 103 SER A C   1 
ATOM   790  O  O   . SER A 1 106 ? 6.229  -12.808 24.434 1.00 25.20  ? 103 SER A O   1 
ATOM   791  C  CB  . SER A 1 106 ? 8.555  -11.256 25.735 1.00 26.07  ? 103 SER A CB  1 
ATOM   792  O  OG  . SER A 1 106 ? 7.633  -10.271 26.208 1.00 22.65  ? 103 SER A OG  1 
ATOM   793  N  N   . LEU A 1 107 ? 6.087  -10.746 23.528 1.00 24.19  ? 104 LEU A N   1 
ATOM   794  C  CA  . LEU A 1 107 ? 4.666  -10.842 23.213 1.00 25.10  ? 104 LEU A CA  1 
ATOM   795  C  C   . LEU A 1 107 ? 4.416  -11.517 21.875 1.00 24.78  ? 104 LEU A C   1 
ATOM   796  O  O   . LEU A 1 107 ? 3.263  -11.854 21.570 1.00 26.50  ? 104 LEU A O   1 
ATOM   797  C  CB  . LEU A 1 107 ? 4.037  -9.453  23.198 1.00 24.98  ? 104 LEU A CB  1 
ATOM   798  C  CG  . LEU A 1 107 ? 4.295  -8.631  24.457 1.00 27.03  ? 104 LEU A CG  1 
ATOM   799  C  CD1 . LEU A 1 107 ? 3.714  -7.253  24.276 1.00 28.62  ? 104 LEU A CD1 1 
ATOM   800  C  CD2 . LEU A 1 107 ? 3.670  -9.373  25.658 1.00 25.23  ? 104 LEU A CD2 1 
ATOM   801  N  N   . ASN A 1 108 ? 5.466  -11.707 21.082 1.00 25.11  ? 105 ASN A N   1 
ATOM   802  C  CA  . ASN A 1 108 ? 5.353  -12.220 19.721 1.00 27.08  ? 105 ASN A CA  1 
ATOM   803  C  C   . ASN A 1 108 ? 5.994  -13.581 19.512 1.00 25.74  ? 105 ASN A C   1 
ATOM   804  O  O   . ASN A 1 108 ? 5.752  -14.203 18.466 1.00 26.17  ? 105 ASN A O   1 
ATOM   805  C  CB  . ASN A 1 108 ? 5.982  -11.231 18.717 1.00 27.47  ? 105 ASN A CB  1 
ATOM   806  C  CG  . ASN A 1 108 ? 5.098  -10.029 18.456 1.00 28.33  ? 105 ASN A CG  1 
ATOM   807  O  OD1 . ASN A 1 108 ? 4.398  -9.989  17.458 1.00 29.74  ? 105 ASN A OD1 1 
ATOM   808  N  ND2 . ASN A 1 108 ? 5.142  -9.042  19.341 1.00 27.26  ? 105 ASN A ND2 1 
ATOM   809  N  N   . ARG A 1 109 ? 6.797  -14.051 20.460 1.00 26.83  ? 106 ARG A N   1 
ATOM   810  C  CA  . ARG A 1 109 ? 7.580  -15.275 20.362 1.00 25.08  ? 106 ARG A CA  1 
ATOM   811  C  C   . ARG A 1 109 ? 7.727  -15.838 21.766 1.00 26.14  ? 106 ARG A C   1 
ATOM   812  O  O   . ARG A 1 109 ? 7.738  -15.079 22.733 1.00 25.45  ? 106 ARG A O   1 
ATOM   813  C  CB  . ARG A 1 109 ? 8.974  -15.008 19.782 1.00 26.10  ? 106 ARG A CB  1 
ATOM   814  C  CG  . ARG A 1 109 ? 8.949  -14.451 18.329 1.00 25.63  ? 106 ARG A CG  1 
ATOM   815  C  CD  . ARG A 1 109 ? 8.577  -15.550 17.381 1.00 27.79  ? 106 ARG A CD  1 
ATOM   816  N  NE  . ARG A 1 109 ? 8.800  -15.172 15.982 1.00 29.08  ? 106 ARG A NE  1 
ATOM   817  C  CZ  . ARG A 1 109 ? 8.043  -14.323 15.300 1.00 30.62  ? 106 ARG A CZ  1 
ATOM   818  N  NH1 . ARG A 1 109 ? 6.946  -13.792 15.824 1.00 27.66  ? 106 ARG A NH1 1 
ATOM   819  N  NH2 . ARG A 1 109 ? 8.393  -13.998 14.055 1.00 28.59  ? 106 ARG A NH2 1 
ATOM   820  N  N   . ASP A 1 110 ? 7.874  -17.158 21.873 1.00 26.73  ? 107 ASP A N   1 
ATOM   821  C  CA  . ASP A 1 110 ? 8.009  -17.804 23.178 1.00 27.88  ? 107 ASP A CA  1 
ATOM   822  C  C   . ASP A 1 110 ? 9.435  -17.628 23.688 1.00 28.70  ? 107 ASP A C   1 
ATOM   823  O  O   . ASP A 1 110 ? 10.380 -18.137 23.075 1.00 26.36  ? 107 ASP A O   1 
ATOM   824  C  CB  . ASP A 1 110 ? 7.688  -19.293 23.080 1.00 25.15  ? 107 ASP A CB  1 
ATOM   825  C  CG  . ASP A 1 110 ? 6.242  -19.566 22.723 1.00 32.38  ? 107 ASP A CG  1 
ATOM   826  O  OD1 . ASP A 1 110 ? 5.361  -18.718 22.988 1.00 31.25  ? 107 ASP A OD1 1 
ATOM   827  O  OD2 . ASP A 1 110 ? 5.974  -20.670 22.209 1.00 38.69  ? 107 ASP A OD2 1 
ATOM   828  N  N   . VAL A 1 111 ? 9.598  -16.953 24.825 1.00 26.50  ? 108 VAL A N   1 
ATOM   829  C  CA  . VAL A 1 111 ? 10.920 -16.803 25.425 1.00 24.10  ? 108 VAL A CA  1 
ATOM   830  C  C   . VAL A 1 111 ? 10.881 -17.362 26.840 1.00 26.82  ? 108 VAL A C   1 
ATOM   831  O  O   . VAL A 1 111 ? 9.822  -17.474 27.459 1.00 24.23  ? 108 VAL A O   1 
ATOM   832  C  CB  . VAL A 1 111 ? 11.394 -15.336 25.432 1.00 22.49  ? 108 VAL A CB  1 
ATOM   833  C  CG1 . VAL A 1 111 ? 11.592 -14.838 23.994 1.00 24.98  ? 108 VAL A CG1 1 
ATOM   834  C  CG2 . VAL A 1 111 ? 10.416 -14.444 26.189 1.00 24.23  ? 108 VAL A CG2 1 
ATOM   835  N  N   . LYS A 1 112 ? 12.059 -17.738 27.346 1.00 24.16  ? 109 LYS A N   1 
ATOM   836  C  CA  . LYS A 1 112 ? 12.165 -18.193 28.725 1.00 24.01  ? 109 LYS A CA  1 
ATOM   837  C  C   . LYS A 1 112 ? 12.286 -17.035 29.704 1.00 24.82  ? 109 LYS A C   1 
ATOM   838  O  O   . LYS A 1 112 ? 12.111 -17.228 30.914 1.00 24.87  ? 109 LYS A O   1 
ATOM   839  C  CB  . LYS A 1 112 ? 13.377 -19.119 28.878 1.00 25.08  ? 109 LYS A CB  1 
ATOM   840  C  CG  . LYS A 1 112 ? 13.244 -20.438 28.097 1.00 29.93  ? 109 LYS A CG  1 
ATOM   841  C  CD  . LYS A 1 112 ? 12.224 -21.322 28.810 1.00 34.17  ? 109 LYS A CD  1 
ATOM   842  C  CE  . LYS A 1 112 ? 12.270 -22.779 28.361 1.00 36.19  ? 109 LYS A CE  1 
ATOM   843  N  NZ  . LYS A 1 112 ? 11.215 -23.546 29.093 1.00 41.04  ? 109 LYS A NZ  1 
ATOM   844  N  N   . GLY A 1 113 ? 12.619 -15.856 29.214 1.00 24.11  ? 110 GLY A N   1 
ATOM   845  C  CA  . GLY A 1 113 ? 12.862 -14.731 30.098 1.00 24.10  ? 110 GLY A CA  1 
ATOM   846  C  C   . GLY A 1 113 ? 13.254 -13.544 29.250 1.00 22.71  ? 110 GLY A C   1 
ATOM   847  O  O   . GLY A 1 113 ? 13.501 -13.663 28.046 1.00 23.68  ? 110 GLY A O   1 
ATOM   848  N  N   . ILE A 1 114 ? 13.322 -12.394 29.914 1.00 24.91  ? 111 ILE A N   1 
ATOM   849  C  CA  . ILE A 1 114 ? 13.563 -11.100 29.290 1.00 22.42  ? 111 ILE A CA  1 
ATOM   850  C  C   . ILE A 1 114 ? 14.607 -10.380 30.122 1.00 22.76  ? 111 ILE A C   1 
ATOM   851  O  O   . ILE A 1 114 ? 14.501 -10.355 31.348 1.00 23.56  ? 111 ILE A O   1 
ATOM   852  C  CB  . ILE A 1 114 ? 12.277 -10.245 29.247 1.00 23.17  ? 111 ILE A CB  1 
ATOM   853  C  CG1 . ILE A 1 114 ? 11.158 -10.986 28.504 1.00 26.20  ? 111 ILE A CG1 1 
ATOM   854  C  CG2 . ILE A 1 114 ? 12.541 -8.924  28.558 1.00 26.48  ? 111 ILE A CG2 1 
ATOM   855  C  CD1 . ILE A 1 114 ? 9.756  -10.545 28.959 1.00 26.34  ? 111 ILE A CD1 1 
ATOM   856  N  N   . VAL A 1 115 ? 15.581 -9.758  29.466 1.00 24.49  ? 112 VAL A N   1 
ATOM   857  C  CA  . VAL A 1 115 ? 16.489 -8.838  30.143 1.00 25.05  ? 112 VAL A CA  1 
ATOM   858  C  C   . VAL A 1 115 ? 16.363 -7.497  29.432 1.00 24.44  ? 112 VAL A C   1 
ATOM   859  O  O   . VAL A 1 115 ? 16.559 -7.431  28.219 1.00 24.51  ? 112 VAL A O   1 
ATOM   860  C  CB  . VAL A 1 115 ? 17.940 -9.338  30.109 1.00 26.03  ? 112 VAL A CB  1 
ATOM   861  C  CG1 . VAL A 1 115 ? 18.827 -8.361  30.858 1.00 25.65  ? 112 VAL A CG1 1 
ATOM   862  C  CG2 . VAL A 1 115 ? 18.060 -10.769 30.718 1.00 24.50  ? 112 VAL A CG2 1 
ATOM   863  N  N   . THR A 1 116 ? 16.017 -6.433  30.167 1.00 25.52  ? 113 THR A N   1 
ATOM   864  C  CA  . THR A 1 116 ? 16.029 -5.094  29.574 1.00 27.03  ? 113 THR A CA  1 
ATOM   865  C  C   . THR A 1 116 ? 17.183 -4.322  30.192 1.00 27.44  ? 113 THR A C   1 
ATOM   866  O  O   . THR A 1 116 ? 17.391 -4.389  31.403 1.00 26.32  ? 113 THR A O   1 
ATOM   867  C  CB  . THR A 1 116 ? 14.719 -4.323  29.802 1.00 24.41  ? 113 THR A CB  1 
ATOM   868  O  OG1 . THR A 1 116 ? 14.481 -4.108  31.210 1.00 29.88  ? 113 THR A OG1 1 
ATOM   869  C  CG2 . THR A 1 116 ? 13.546 -5.078  29.213 1.00 27.89  ? 113 THR A CG2 1 
ATOM   870  N  N   . MET A 1 117 ? 17.926 -3.579  29.375 1.00 26.71  ? 114 MET A N   1 
ATOM   871  C  CA  . MET A 1 117 ? 19.125 -2.907  29.866 1.00 24.42  ? 114 MET A CA  1 
ATOM   872  C  C   . MET A 1 117 ? 18.993 -1.456  29.423 1.00 29.17  ? 114 MET A C   1 
ATOM   873  O  O   . MET A 1 117 ? 19.146 -1.161  28.228 1.00 29.29  ? 114 MET A O   1 
ATOM   874  C  CB  . MET A 1 117 ? 20.373 -3.553  29.278 1.00 28.39  ? 114 MET A CB  1 
ATOM   875  C  CG  . MET A 1 117 ? 20.808 -4.770  30.055 1.00 31.21  ? 114 MET A CG  1 
ATOM   876  S  SD  . MET A 1 117 ? 22.008 -5.793  29.183 1.00 33.65  ? 114 MET A SD  1 
ATOM   877  C  CE  . MET A 1 117 ? 21.196 -6.210  27.638 1.00 32.88  ? 114 MET A CE  1 
ATOM   878  N  N   . CYS A 1 118 ? 18.670 -0.581  30.370 1.00 27.54  ? 115 CYS A N   1 
ATOM   879  C  CA  . CYS A 1 118 ? 18.507 0.851   30.135 1.00 30.98  ? 115 CYS A CA  1 
ATOM   880  C  C   . CYS A 1 118 ? 17.498 1.098   29.014 1.00 33.79  ? 115 CYS A C   1 
ATOM   881  O  O   . CYS A 1 118 ? 17.726 1.891   28.100 1.00 31.42  ? 115 CYS A O   1 
ATOM   882  C  CB  . CYS A 1 118 ? 19.862 1.506   29.836 1.00 32.06  ? 115 CYS A CB  1 
ATOM   883  S  SG  . CYS A 1 118 ? 21.138 1.180   31.120 1.00 34.37  ? 115 CYS A SG  1 
ATOM   884  N  N   . ALA A 1 119 ? 16.357 0.389   29.091 1.00 30.49  ? 116 ALA A N   1 
ATOM   885  C  CA  . ALA A 1 119 ? 15.308 0.516   28.083 1.00 29.64  ? 116 ALA A CA  1 
ATOM   886  C  C   . ALA A 1 119 ? 14.426 1.719   28.394 1.00 29.70  ? 116 ALA A C   1 
ATOM   887  O  O   . ALA A 1 119 ? 13.971 1.867   29.530 1.00 30.14  ? 116 ALA A O   1 
ATOM   888  C  CB  . ALA A 1 119 ? 14.447 -0.743  28.024 1.00 29.85  ? 116 ALA A CB  1 
ATOM   889  N  N   . PRO A 1 120 ? 14.178 2.599   27.429 1.00 31.56  ? 117 PRO A N   1 
ATOM   890  C  CA  . PRO A 1 120 ? 13.333 3.769   27.695 1.00 31.03  ? 117 PRO A CA  1 
ATOM   891  C  C   . PRO A 1 120 ? 11.870 3.372   27.781 1.00 33.06  ? 117 PRO A C   1 
ATOM   892  O  O   . PRO A 1 120 ? 11.434 2.386   27.186 1.00 33.93  ? 117 PRO A O   1 
ATOM   893  C  CB  . PRO A 1 120 ? 13.581 4.660   26.469 1.00 33.58  ? 117 PRO A CB  1 
ATOM   894  C  CG  . PRO A 1 120 ? 13.858 3.671   25.364 1.00 33.03  ? 117 PRO A CG  1 
ATOM   895  C  CD  . PRO A 1 120 ? 14.627 2.535   26.030 1.00 32.43  ? 117 PRO A CD  1 
ATOM   896  N  N   . MET A 1 121 ? 11.099 4.152   28.523 1.00 32.11  ? 118 MET A N   1 
ATOM   897  C  CA  . MET A 1 121 ? 9.656  3.975   28.497 1.00 34.01  ? 118 MET A CA  1 
ATOM   898  C  C   . MET A 1 121 ? 9.052  5.294   28.054 1.00 37.54  ? 118 MET A C   1 
ATOM   899  O  O   . MET A 1 121 ? 9.017  6.250   28.830 1.00 39.24  ? 118 MET A O   1 
ATOM   900  C  CB  . MET A 1 121 ? 9.086  3.566   29.845 1.00 34.40  ? 118 MET A CB  1 
ATOM   901  C  CG  . MET A 1 121 ? 9.309  2.095   30.121 1.00 30.57  ? 118 MET A CG  1 
ATOM   902  S  SD  . MET A 1 121 ? 8.049  1.082   29.334 1.00 38.21  ? 118 MET A SD  1 
ATOM   903  C  CE  . MET A 1 121 ? 9.036  0.349   28.028 1.00 32.73  ? 118 MET A CE  1 
ATOM   904  N  N   . GLY A 1 122 ? 8.563  5.347   26.828 1.00 35.50  ? 119 GLY A N   1 
ATOM   905  C  CA  . GLY A 1 122 ? 8.067  6.639   26.406 1.00 38.98  ? 119 GLY A CA  1 
ATOM   906  C  C   . GLY A 1 122 ? 8.927  7.189   25.286 1.00 41.57  ? 119 GLY A C   1 
ATOM   907  O  O   . GLY A 1 122 ? 10.130 6.908   25.191 1.00 42.45  ? 119 GLY A O   1 
ATOM   908  N  N   . GLY A 1 123 ? 8.301  7.961   24.408 1.00 44.08  ? 120 GLY A N   1 
ATOM   909  C  CA  . GLY A 1 123 ? 8.960  8.325   23.165 1.00 44.45  ? 120 GLY A CA  1 
ATOM   910  C  C   . GLY A 1 123 ? 9.505  9.736   23.095 1.00 52.60  ? 120 GLY A C   1 
ATOM   911  O  O   . GLY A 1 123 ? 9.450  10.362  22.034 1.00 55.33  ? 120 GLY A O   1 
ATOM   912  N  N   . LYS A 1 124 ? 10.040 10.248  24.201 1.00 53.23  ? 121 LYS A N   1 
ATOM   913  C  CA  . LYS A 1 124 ? 10.691 11.555  24.196 1.00 57.81  ? 121 LYS A CA  1 
ATOM   914  C  C   . LYS A 1 124 ? 12.009 11.440  23.432 1.00 59.69  ? 121 LYS A C   1 
ATOM   915  O  O   . LYS A 1 124 ? 12.909 10.700  23.843 1.00 56.12  ? 121 LYS A O   1 
ATOM   916  C  CB  . LYS A 1 124 ? 10.903 12.030  25.633 1.00 61.38  ? 121 LYS A CB  1 
ATOM   917  C  CG  . LYS A 1 124 ? 12.120 12.920  25.900 1.00 65.34  ? 121 LYS A CG  1 
ATOM   918  C  CD  . LYS A 1 124 ? 11.705 14.093  26.779 1.00 66.98  ? 121 LYS A CD  1 
ATOM   919  C  CE  . LYS A 1 124 ? 12.851 14.667  27.620 1.00 75.91  ? 121 LYS A CE  1 
ATOM   920  N  NZ  . LYS A 1 124 ? 13.959 15.254  26.814 1.00 77.52  ? 121 LYS A NZ  1 
ATOM   921  N  N   . THR A 1 125 ? 12.105 12.130  22.289 1.00 57.83  ? 122 THR A N   1 
ATOM   922  C  CA  . THR A 1 125 ? 13.328 12.151  21.488 1.00 60.00  ? 122 THR A CA  1 
ATOM   923  C  C   . THR A 1 125 ? 14.063 13.479  21.583 1.00 64.24  ? 122 THR A C   1 
ATOM   924  O  O   . THR A 1 125 ? 15.239 13.560  21.208 1.00 59.46  ? 122 THR A O   1 
ATOM   925  C  CB  . THR A 1 125 ? 13.021 11.889  20.006 1.00 59.29  ? 122 THR A CB  1 
ATOM   926  O  OG1 . THR A 1 125 ? 11.978 12.770  19.576 1.00 57.36  ? 122 THR A OG1 1 
ATOM   927  C  CG2 . THR A 1 125 ? 12.578 10.451  19.793 1.00 54.77  ? 122 THR A CG2 1 
ATOM   928  N  N   . GLU A 1 126 ? 13.380 14.518  22.046 1.00 65.20  ? 123 GLU A N   1 
ATOM   929  C  CA  . GLU A 1 126 ? 13.991 15.825  22.204 1.00 65.00  ? 123 GLU A CA  1 
ATOM   930  C  C   . GLU A 1 126 ? 15.106 15.769  23.240 1.00 65.31  ? 123 GLU A C   1 
ATOM   931  O  O   . GLU A 1 126 ? 15.011 15.057  24.246 1.00 64.73  ? 123 GLU A O   1 
ATOM   932  C  CB  . GLU A 1 126 ? 12.932 16.867  22.596 1.00 68.52  ? 123 GLU A CB  1 
ATOM   933  C  CG  . GLU A 1 126 ? 11.640 16.971  21.713 1.00 74.12  ? 123 GLU A CG  1 
ATOM   934  C  CD  . GLU A 1 126 ? 10.938 15.645  21.375 1.00 79.10  ? 123 GLU A CD  1 
ATOM   935  O  OE1 . GLU A 1 126 ? 10.782 14.778  22.270 1.00 72.92  ? 123 GLU A OE1 1 
ATOM   936  O  OE2 . GLU A 1 126 ? 10.548 15.475  20.196 1.00 82.58  ? 123 GLU A OE2 1 
ATOM   937  N  N   . GLY A 1 127 ? 16.175 16.493  22.970 1.00 60.73  ? 124 GLY A N   1 
ATOM   938  C  CA  . GLY A 1 127 ? 17.315 16.538  23.878 1.00 60.48  ? 124 GLY A CA  1 
ATOM   939  C  C   . GLY A 1 127 ? 18.330 15.443  23.567 1.00 59.81  ? 124 GLY A C   1 
ATOM   940  O  O   . GLY A 1 127 ? 18.900 15.426  22.480 1.00 56.81  ? 124 GLY A O   1 
ATOM   941  N  N   . ALA A 1 128 ? 18.524 14.523  24.517 1.00 52.53  ? 125 ALA A N   1 
ATOM   942  C  CA  . ALA A 1 128 ? 19.701 13.658  24.484 1.00 52.24  ? 125 ALA A CA  1 
ATOM   943  C  C   . ALA A 1 128 ? 19.686 12.709  23.293 1.00 50.39  ? 125 ALA A C   1 
ATOM   944  O  O   . ALA A 1 128 ? 20.737 12.427  22.708 1.00 49.29  ? 125 ALA A O   1 
ATOM   945  C  CB  . ALA A 1 128 ? 19.810 12.868  25.788 1.00 53.77  ? 125 ALA A CB  1 
ATOM   946  N  N   . ILE A 1 129 ? 18.513 12.188  22.930 1.00 49.28  ? 126 ILE A N   1 
ATOM   947  C  CA  . ILE A 1 129 ? 18.454 11.210  21.847 1.00 47.30  ? 126 ILE A CA  1 
ATOM   948  C  C   . ILE A 1 129 ? 18.667 11.893  20.504 1.00 48.46  ? 126 ILE A C   1 
ATOM   949  O  O   . ILE A 1 129 ? 19.404 11.395  19.641 1.00 47.62  ? 126 ILE A O   1 
ATOM   950  C  CB  . ILE A 1 129 ? 17.121 10.443  21.898 1.00 48.82  ? 126 ILE A CB  1 
ATOM   951  C  CG1 . ILE A 1 129 ? 17.096 9.534   23.131 1.00 48.51  ? 126 ILE A CG1 1 
ATOM   952  C  CG2 . ILE A 1 129 ? 16.924 9.625   20.634 1.00 44.08  ? 126 ILE A CG2 1 
ATOM   953  C  CD1 . ILE A 1 129 ? 15.792 8.805   23.337 1.00 49.16  ? 126 ILE A CD1 1 
ATOM   954  N  N   . TYR A 1 130 ? 18.034 13.049  20.311 1.00 50.95  ? 127 TYR A N   1 
ATOM   955  C  CA  . TYR A 1 130 ? 18.276 13.860  19.124 1.00 49.07  ? 127 TYR A CA  1 
ATOM   956  C  C   . TYR A 1 130 ? 19.760 14.171  18.949 1.00 48.67  ? 127 TYR A C   1 
ATOM   957  O  O   . TYR A 1 130 ? 20.352 13.851  17.914 1.00 47.18  ? 127 TYR A O   1 
ATOM   958  C  CB  . TYR A 1 130 ? 17.448 15.139  19.208 1.00 49.13  ? 127 TYR A CB  1 
ATOM   959  C  CG  . TYR A 1 130 ? 17.744 16.121  18.108 1.00 52.33  ? 127 TYR A CG  1 
ATOM   960  C  CD1 . TYR A 1 130 ? 17.071 16.068  16.894 1.00 53.83  ? 127 TYR A CD1 1 
ATOM   961  C  CD2 . TYR A 1 130 ? 18.688 17.119  18.294 1.00 53.37  ? 127 TYR A CD2 1 
ATOM   962  C  CE1 . TYR A 1 130 ? 17.345 16.980  15.889 1.00 52.90  ? 127 TYR A CE1 1 
ATOM   963  C  CE2 . TYR A 1 130 ? 18.967 18.029  17.299 1.00 58.69  ? 127 TYR A CE2 1 
ATOM   964  C  CZ  . TYR A 1 130 ? 18.297 17.955  16.098 1.00 57.30  ? 127 TYR A CZ  1 
ATOM   965  O  OH  . TYR A 1 130 ? 18.584 18.879  15.114 1.00 59.83  ? 127 TYR A OH  1 
ATOM   966  N  N   . GLU A 1 131 ? 20.386 14.799  19.953 1.00 49.22  ? 128 GLU A N   1 
ATOM   967  C  CA  . GLU A 1 131 ? 21.795 15.157  19.797 1.00 50.90  ? 128 GLU A CA  1 
ATOM   968  C  C   . GLU A 1 131 ? 22.683 13.925  19.711 1.00 51.97  ? 128 GLU A C   1 
ATOM   969  O  O   . GLU A 1 131 ? 23.742 13.972  19.071 1.00 46.81  ? 128 GLU A O   1 
ATOM   970  C  CB  . GLU A 1 131 ? 22.284 16.070  20.928 1.00 51.26  ? 128 GLU A CB  1 
ATOM   971  C  CG  . GLU A 1 131 ? 21.261 17.024  21.528 1.00 58.42  ? 128 GLU A CG  1 
ATOM   972  C  CD  . GLU A 1 131 ? 21.609 17.418  22.965 1.00 72.40  ? 128 GLU A CD  1 
ATOM   973  O  OE1 . GLU A 1 131 ? 20.730 17.329  23.856 1.00 74.11  ? 128 GLU A OE1 1 
ATOM   974  O  OE2 . GLU A 1 131 ? 22.761 17.852  23.196 1.00 75.03  ? 128 GLU A OE2 1 
ATOM   975  N  N   . GLY A 1 132 ? 22.273 12.815  20.336 1.00 47.49  ? 129 GLY A N   1 
ATOM   976  C  CA  . GLY A 1 132 ? 23.025 11.580  20.184 1.00 49.64  ? 129 GLY A CA  1 
ATOM   977  C  C   . GLY A 1 132 ? 22.998 11.052  18.761 1.00 47.33  ? 129 GLY A C   1 
ATOM   978  O  O   . GLY A 1 132 ? 23.998 10.532  18.262 1.00 43.99  ? 129 GLY A O   1 
ATOM   979  N  N   . PHE A 1 133 ? 21.850 11.179  18.089 1.00 47.35  ? 130 PHE A N   1 
ATOM   980  C  CA  . PHE A 1 133 ? 21.751 10.781  16.687 1.00 44.29  ? 130 PHE A CA  1 
ATOM   981  C  C   . PHE A 1 133 ? 22.646 11.643  15.802 1.00 50.02  ? 130 PHE A C   1 
ATOM   982  O  O   . PHE A 1 133 ? 23.334 11.128  14.910 1.00 46.29  ? 130 PHE A O   1 
ATOM   983  C  CB  . PHE A 1 133 ? 20.292 10.868  16.233 1.00 41.58  ? 130 PHE A CB  1 
ATOM   984  C  CG  . PHE A 1 133 ? 20.014 10.205  14.903 1.00 45.53  ? 130 PHE A CG  1 
ATOM   985  C  CD1 . PHE A 1 133 ? 20.895 9.284   14.359 1.00 47.32  ? 130 PHE A CD1 1 
ATOM   986  C  CD2 . PHE A 1 133 ? 18.848 10.493  14.208 1.00 47.96  ? 130 PHE A CD2 1 
ATOM   987  C  CE1 . PHE A 1 133 ? 20.624 8.670   13.133 1.00 48.44  ? 130 PHE A CE1 1 
ATOM   988  C  CE2 . PHE A 1 133 ? 18.571 9.885   12.993 1.00 46.73  ? 130 PHE A CE2 1 
ATOM   989  C  CZ  . PHE A 1 133 ? 19.460 8.974   12.455 1.00 47.72  ? 130 PHE A CZ  1 
ATOM   990  N  N   . LEU A 1 134 ? 22.651 12.958  16.035 1.00 46.40  ? 131 LEU A N   1 
ATOM   991  C  CA  . LEU A 1 134 ? 23.499 13.847  15.242 1.00 47.68  ? 131 LEU A CA  1 
ATOM   992  C  C   . LEU A 1 134 ? 24.976 13.557  15.468 1.00 50.94  ? 131 LEU A C   1 
ATOM   993  O  O   . LEU A 1 134 ? 25.767 13.551  14.517 1.00 48.74  ? 131 LEU A O   1 
ATOM   994  C  CB  . LEU A 1 134 ? 23.198 15.305  15.579 1.00 53.18  ? 131 LEU A CB  1 
ATOM   995  C  CG  . LEU A 1 134 ? 21.770 15.776  15.337 1.00 55.73  ? 131 LEU A CG  1 
ATOM   996  C  CD1 . LEU A 1 134 ? 21.744 17.290  15.335 1.00 56.27  ? 131 LEU A CD1 1 
ATOM   997  C  CD2 . LEU A 1 134 ? 21.261 15.222  14.011 1.00 57.27  ? 131 LEU A CD2 1 
ATOM   998  N  N   . GLU A 1 135 ? 25.373 13.339  16.724 1.00 47.25  ? 132 GLU A N   1 
ATOM   999  C  CA  . GLU A 1 135 ? 26.769 13.022  16.996 1.00 48.52  ? 132 GLU A CA  1 
ATOM   1000 C  C   . GLU A 1 135 ? 27.154 11.694  16.361 1.00 46.22  ? 132 GLU A C   1 
ATOM   1001 O  O   . GLU A 1 135 ? 28.263 11.545  15.837 1.00 49.50  ? 132 GLU A O   1 
ATOM   1002 C  CB  . GLU A 1 135 ? 27.026 12.994  18.506 1.00 54.83  ? 132 GLU A CB  1 
ATOM   1003 C  CG  . GLU A 1 135 ? 28.495 13.212  18.864 1.00 62.76  ? 132 GLU A CG  1 
ATOM   1004 C  CD  . GLU A 1 135 ? 29.043 12.181  19.835 1.00 68.23  ? 132 GLU A CD  1 
ATOM   1005 O  OE1 . GLU A 1 135 ? 28.294 11.257  20.223 1.00 74.54  ? 132 GLU A OE1 1 
ATOM   1006 O  OE2 . GLU A 1 135 ? 30.237 12.295  20.202 1.00 71.83  ? 132 GLU A OE2 1 
ATOM   1007 N  N   . TYR A 1 136 ? 26.243 10.718  16.399 1.00 45.36  ? 133 TYR A N   1 
ATOM   1008 C  CA  . TYR A 1 136 ? 26.483 9.446   15.730 1.00 44.20  ? 133 TYR A CA  1 
ATOM   1009 C  C   . TYR A 1 136 ? 26.784 9.659   14.255 1.00 44.72  ? 133 TYR A C   1 
ATOM   1010 O  O   . TYR A 1 136 ? 27.734 9.081   13.713 1.00 46.34  ? 133 TYR A O   1 
ATOM   1011 C  CB  . TYR A 1 136 ? 25.265 8.545   15.895 1.00 42.73  ? 133 TYR A CB  1 
ATOM   1012 C  CG  . TYR A 1 136 ? 25.295 7.311   15.035 1.00 45.55  ? 133 TYR A CG  1 
ATOM   1013 C  CD1 . TYR A 1 136 ? 26.167 6.272   15.324 1.00 41.28  ? 133 TYR A CD1 1 
ATOM   1014 C  CD2 . TYR A 1 136 ? 24.453 7.180   13.932 1.00 44.18  ? 133 TYR A CD2 1 
ATOM   1015 C  CE1 . TYR A 1 136 ? 26.199 5.135   14.551 1.00 44.01  ? 133 TYR A CE1 1 
ATOM   1016 C  CE2 . TYR A 1 136 ? 24.475 6.035   13.151 1.00 41.34  ? 133 TYR A CE2 1 
ATOM   1017 C  CZ  . TYR A 1 136 ? 25.354 5.018   13.466 1.00 41.77  ? 133 TYR A CZ  1 
ATOM   1018 O  OH  . TYR A 1 136 ? 25.400 3.869   12.705 1.00 43.28  ? 133 TYR A OH  1 
ATOM   1019 N  N   . ALA A 1 137 ? 25.994 10.506  13.596 1.00 46.07  ? 134 ALA A N   1 
ATOM   1020 C  CA  . ALA A 1 137 ? 26.203 10.772  12.178 1.00 50.49  ? 134 ALA A CA  1 
ATOM   1021 C  C   . ALA A 1 137 ? 27.505 11.526  11.938 1.00 52.58  ? 134 ALA A C   1 
ATOM   1022 O  O   . ALA A 1 137 ? 28.198 11.273  10.947 1.00 52.63  ? 134 ALA A O   1 
ATOM   1023 C  CB  . ALA A 1 137 ? 25.014 11.551  11.616 1.00 52.73  ? 134 ALA A CB  1 
ATOM   1024 N  N   . ARG A 1 138 ? 27.859 12.455  12.831 1.00 50.44  ? 135 ARG A N   1 
ATOM   1025 C  CA  . ARG A 1 138 ? 29.110 13.189  12.663 1.00 51.66  ? 135 ARG A CA  1 
ATOM   1026 C  C   . ARG A 1 138 ? 30.317 12.279  12.843 1.00 52.05  ? 135 ARG A C   1 
ATOM   1027 O  O   . ARG A 1 138 ? 31.278 12.356  12.069 1.00 52.87  ? 135 ARG A O   1 
ATOM   1028 C  CB  . ARG A 1 138 ? 29.182 14.370  13.629 1.00 52.97  ? 135 ARG A CB  1 
ATOM   1029 C  CG  . ARG A 1 138 ? 28.324 15.525  13.192 1.00 58.76  ? 135 ARG A CG  1 
ATOM   1030 C  CD  . ARG A 1 138 ? 28.321 16.693  14.163 1.00 65.36  ? 135 ARG A CD  1 
ATOM   1031 N  NE  . ARG A 1 138 ? 26.990 17.287  14.227 1.00 71.84  ? 135 ARG A NE  1 
ATOM   1032 C  CZ  . ARG A 1 138 ? 26.615 18.378  13.570 1.00 74.45  ? 135 ARG A CZ  1 
ATOM   1033 N  NH1 . ARG A 1 138 ? 27.453 19.035  12.774 1.00 72.10  ? 135 ARG A NH1 1 
ATOM   1034 N  NH2 . ARG A 1 138 ? 25.364 18.814  13.701 1.00 74.48  ? 135 ARG A NH2 1 
ATOM   1035 N  N   . ASN A 1 139 ? 30.295 11.409  13.853 1.00 51.44  ? 136 ASN A N   1 
ATOM   1036 C  CA  . ASN A 1 139 ? 31.447 10.540  14.060 1.00 53.38  ? 136 ASN A CA  1 
ATOM   1037 C  C   . ASN A 1 139 ? 31.602 9.533   12.931 1.00 52.14  ? 136 ASN A C   1 
ATOM   1038 O  O   . ASN A 1 139 ? 32.732 9.189   12.569 1.00 54.17  ? 136 ASN A O   1 
ATOM   1039 C  CB  . ASN A 1 139 ? 31.355 9.826   15.406 1.00 52.77  ? 136 ASN A CB  1 
ATOM   1040 C  CG  . ASN A 1 139 ? 31.415 10.786  16.573 1.00 57.76  ? 136 ASN A CG  1 
ATOM   1041 O  OD1 . ASN A 1 139 ? 30.837 10.536  17.634 1.00 64.51  ? 136 ASN A OD1 1 
ATOM   1042 N  ND2 . ASN A 1 139 ? 32.118 11.896  16.385 1.00 61.00  ? 136 ASN A ND2 1 
ATOM   1043 N  N   . PHE A 1 140 ? 30.497 9.056   12.355 1.00 51.16  ? 137 PHE A N   1 
ATOM   1044 C  CA  . PHE A 1 140 ? 30.634 8.129   11.236 1.00 52.95  ? 137 PHE A CA  1 
ATOM   1045 C  C   . PHE A 1 140 ? 31.275 8.824   10.044 1.00 58.12  ? 137 PHE A C   1 
ATOM   1046 O  O   . PHE A 1 140 ? 32.127 8.246   9.355  1.00 57.23  ? 137 PHE A O   1 
ATOM   1047 C  CB  . PHE A 1 140 ? 29.284 7.565   10.816 1.00 52.24  ? 137 PHE A CB  1 
ATOM   1048 C  CG  . PHE A 1 140 ? 29.402 6.457   9.820  1.00 56.55  ? 137 PHE A CG  1 
ATOM   1049 C  CD1 . PHE A 1 140 ? 29.377 6.716   8.462  1.00 58.51  ? 137 PHE A CD1 1 
ATOM   1050 C  CD2 . PHE A 1 140 ? 29.502 5.142   10.247 1.00 59.49  ? 137 PHE A CD2 1 
ATOM   1051 C  CE1 . PHE A 1 140 ? 29.497 5.698   7.549  1.00 60.01  ? 137 PHE A CE1 1 
ATOM   1052 C  CE2 . PHE A 1 140 ? 29.608 4.113   9.330  1.00 60.39  ? 137 PHE A CE2 1 
ATOM   1053 C  CZ  . PHE A 1 140 ? 29.601 4.394   7.980  1.00 55.04  ? 137 PHE A CZ  1 
ATOM   1054 N  N   . LYS A 1 141 ? 30.860 10.064  9.777  1.00 56.58  ? 138 LYS A N   1 
ATOM   1055 C  CA  . LYS A 1 141 ? 31.439 10.816  8.673  1.00 58.82  ? 138 LYS A CA  1 
ATOM   1056 C  C   . LYS A 1 141 ? 32.928 11.054  8.880  1.00 60.32  ? 138 LYS A C   1 
ATOM   1057 O  O   . LYS A 1 141 ? 33.687 11.086  7.906  1.00 62.60  ? 138 LYS A O   1 
ATOM   1058 C  CB  . LYS A 1 141 ? 30.679 12.127  8.498  1.00 59.85  ? 138 LYS A CB  1 
ATOM   1059 C  CG  . LYS A 1 141 ? 29.382 11.942  7.732  1.00 61.73  ? 138 LYS A CG  1 
ATOM   1060 C  CD  . LYS A 1 141 ? 28.376 13.040  8.002  1.00 60.92  ? 138 LYS A CD  1 
ATOM   1061 C  CE  . LYS A 1 141 ? 27.325 13.098  6.908  1.00 64.25  ? 138 LYS A CE  1 
ATOM   1062 N  NZ  . LYS A 1 141 ? 26.933 11.767  6.375  1.00 66.88  ? 138 LYS A NZ  1 
ATOM   1063 N  N   . LYS A 1 142 ? 33.369 11.201  10.134 1.00 55.05  ? 139 LYS A N   1 
ATOM   1064 C  CA  . LYS A 1 142 ? 34.804 11.261  10.398 1.00 62.09  ? 139 LYS A CA  1 
ATOM   1065 C  C   . LYS A 1 142 ? 35.460 9.906   10.161 1.00 63.11  ? 139 LYS A C   1 
ATOM   1066 O  O   . LYS A 1 142 ? 36.584 9.836   9.647  1.00 65.28  ? 139 LYS A O   1 
ATOM   1067 C  CB  . LYS A 1 142 ? 35.077 11.734  11.826 1.00 62.45  ? 139 LYS A CB  1 
ATOM   1068 C  CG  . LYS A 1 142 ? 36.567 11.919  12.100 1.00 71.09  ? 139 LYS A CG  1 
ATOM   1069 C  CD  . LYS A 1 142 ? 36.943 11.710  13.562 1.00 74.67  ? 139 LYS A CD  1 
ATOM   1070 C  CE  . LYS A 1 142 ? 36.263 12.700  14.488 1.00 79.39  ? 139 LYS A CE  1 
ATOM   1071 N  NZ  . LYS A 1 142 ? 36.683 12.487  15.908 1.00 82.09  ? 139 LYS A NZ  1 
ATOM   1072 N  N   . TYR A 1 143 ? 34.776 8.818   10.530 1.00 56.71  ? 140 TYR A N   1 
ATOM   1073 C  CA  . TYR A 1 143 ? 35.312 7.483   10.271 1.00 63.68  ? 140 TYR A CA  1 
ATOM   1074 C  C   . TYR A 1 143 ? 35.421 7.217   8.773  1.00 64.97  ? 140 TYR A C   1 
ATOM   1075 O  O   . TYR A 1 143 ? 36.302 6.468   8.336  1.00 69.49  ? 140 TYR A O   1 
ATOM   1076 C  CB  . TYR A 1 143 ? 34.443 6.422   10.965 1.00 61.29  ? 140 TYR A CB  1 
ATOM   1077 C  CG  . TYR A 1 143 ? 34.477 5.039   10.331 1.00 67.43  ? 140 TYR A CG  1 
ATOM   1078 C  CD1 . TYR A 1 143 ? 33.578 4.681   9.328  1.00 68.31  ? 140 TYR A CD1 1 
ATOM   1079 C  CD2 . TYR A 1 143 ? 35.409 4.089   10.741 1.00 68.74  ? 140 TYR A CD2 1 
ATOM   1080 C  CE1 . TYR A 1 143 ? 33.614 3.418   8.744  1.00 70.43  ? 140 TYR A CE1 1 
ATOM   1081 C  CE2 . TYR A 1 143 ? 35.449 2.823   10.166 1.00 70.35  ? 140 TYR A CE2 1 
ATOM   1082 C  CZ  . TYR A 1 143 ? 34.551 2.494   9.167  1.00 71.26  ? 140 TYR A CZ  1 
ATOM   1083 O  OH  . TYR A 1 143 ? 34.588 1.242   8.587  1.00 67.78  ? 140 TYR A OH  1 
ATOM   1084 N  N   . GLU A 1 144 ? 34.552 7.836   7.972  1.00 63.85  ? 141 GLU A N   1 
ATOM   1085 C  CA  . GLU A 1 144 ? 34.650 7.773   6.519  1.00 65.39  ? 141 GLU A CA  1 
ATOM   1086 C  C   . GLU A 1 144 ? 35.828 8.564   5.970  1.00 68.83  ? 141 GLU A C   1 
ATOM   1087 O  O   . GLU A 1 144 ? 36.003 8.608   4.747  1.00 71.66  ? 141 GLU A O   1 
ATOM   1088 C  CB  . GLU A 1 144 ? 33.354 8.284   5.888  1.00 65.30  ? 141 GLU A CB  1 
ATOM   1089 C  CG  . GLU A 1 144 ? 32.203 7.296   5.972  1.00 65.22  ? 141 GLU A CG  1 
ATOM   1090 C  CD  . GLU A 1 144 ? 30.936 7.809   5.317  1.00 65.68  ? 141 GLU A CD  1 
ATOM   1091 O  OE1 . GLU A 1 144 ? 30.400 8.842   5.779  1.00 64.29  ? 141 GLU A OE1 1 
ATOM   1092 O  OE2 . GLU A 1 144 ? 30.468 7.170   4.352  1.00 67.97  ? 141 GLU A OE2 1 
ATOM   1093 N  N   . GLY A 1 145 ? 36.631 9.190   6.828  1.00 69.90  ? 142 GLY A N   1 
ATOM   1094 C  CA  . GLY A 1 145 ? 37.751 9.974   6.351  1.00 69.51  ? 142 GLY A CA  1 
ATOM   1095 C  C   . GLY A 1 145 ? 37.367 11.261  5.665  1.00 71.57  ? 142 GLY A C   1 
ATOM   1096 O  O   . GLY A 1 145 ? 38.143 11.777  4.860  1.00 73.43  ? 142 GLY A O   1 
ATOM   1097 N  N   . LYS A 1 146 ? 36.189 11.799  5.964  1.00 71.69  ? 143 LYS A N   1 
ATOM   1098 C  CA  . LYS A 1 146 ? 35.718 13.011  5.312  1.00 75.54  ? 143 LYS A CA  1 
ATOM   1099 C  C   . LYS A 1 146 ? 36.303 14.247  5.990  1.00 76.47  ? 143 LYS A C   1 
ATOM   1100 O  O   . LYS A 1 146 ? 36.502 14.279  7.208  1.00 76.92  ? 143 LYS A O   1 
ATOM   1101 C  CB  . LYS A 1 146 ? 34.191 13.063  5.346  1.00 70.63  ? 143 LYS A CB  1 
ATOM   1102 C  CG  . LYS A 1 146 ? 33.530 12.019  4.462  1.00 70.55  ? 143 LYS A CG  1 
ATOM   1103 C  CD  . LYS A 1 146 ? 32.015 12.107  4.516  1.00 67.73  ? 143 LYS A CD  1 
ATOM   1104 C  CE  . LYS A 1 146 ? 31.385 11.225  3.454  1.00 69.51  ? 143 LYS A CE  1 
ATOM   1105 N  NZ  . LYS A 1 146 ? 29.902 11.270  3.511  1.00 71.37  ? 143 LYS A NZ  1 
ATOM   1106 N  N   . ASP A 1 147 ? 36.583 15.269  5.186  1.00 79.42  ? 144 ASP A N   1 
ATOM   1107 C  CA  . ASP A 1 147 ? 37.098 16.523  5.718  1.00 83.14  ? 144 ASP A CA  1 
ATOM   1108 C  C   . ASP A 1 147 ? 36.025 17.227  6.541  1.00 81.49  ? 144 ASP A C   1 
ATOM   1109 O  O   . ASP A 1 147 ? 34.833 16.924  6.445  1.00 80.17  ? 144 ASP A O   1 
ATOM   1110 C  CB  . ASP A 1 147 ? 37.548 17.442  4.591  1.00 81.53  ? 144 ASP A CB  1 
ATOM   1111 C  CG  . ASP A 1 147 ? 36.468 17.646  3.558  1.00 88.35  ? 144 ASP A CG  1 
ATOM   1112 O  OD1 . ASP A 1 147 ? 36.184 16.696  2.797  1.00 91.58  ? 144 ASP A OD1 1 
ATOM   1113 O  OD2 . ASP A 1 147 ? 35.886 18.749  3.522  1.00 89.65  ? 144 ASP A OD2 1 
ATOM   1114 N  N   . GLN A 1 148 ? 36.458 18.198  7.350  1.00 81.98  ? 145 GLN A N   1 
ATOM   1115 C  CA  . GLN A 1 148 ? 35.508 18.860  8.237  1.00 81.63  ? 145 GLN A CA  1 
ATOM   1116 C  C   . GLN A 1 148 ? 34.498 19.693  7.459  1.00 81.23  ? 145 GLN A C   1 
ATOM   1117 O  O   . GLN A 1 148 ? 33.380 19.913  7.939  1.00 77.95  ? 145 GLN A O   1 
ATOM   1118 C  CB  . GLN A 1 148 ? 36.248 19.728  9.258  1.00 78.00  ? 145 GLN A CB  1 
ATOM   1119 C  CG  . GLN A 1 148 ? 35.422 20.197  10.472 1.00 76.97  ? 145 GLN A CG  1 
ATOM   1120 C  CD  . GLN A 1 148 ? 34.503 19.133  11.070 1.00 77.01  ? 145 GLN A CD  1 
ATOM   1121 O  OE1 . GLN A 1 148 ? 34.770 18.616  12.149 1.00 78.89  ? 145 GLN A OE1 1 
ATOM   1122 N  NE2 . GLN A 1 148 ? 33.368 18.881  10.422 1.00 79.30  ? 145 GLN A NE2 1 
ATOM   1123 N  N   . GLU A 1 149 ? 34.864 20.149  6.259  1.00 86.61  ? 146 GLU A N   1 
ATOM   1124 C  CA  . GLU A 1 149 ? 33.935 20.934  5.451  1.00 87.93  ? 146 GLU A CA  1 
ATOM   1125 C  C   . GLU A 1 149 ? 32.844 20.058  4.860  1.00 83.98  ? 146 GLU A C   1 
ATOM   1126 O  O   . GLU A 1 149 ? 31.669 20.441  4.853  1.00 84.18  ? 146 GLU A O   1 
ATOM   1127 C  CB  . GLU A 1 149 ? 34.691 21.667  4.345  1.00 91.59  ? 146 GLU A CB  1 
ATOM   1128 C  CG  . GLU A 1 149 ? 35.637 22.678  4.918  1.00 99.87  ? 146 GLU A CG  1 
ATOM   1129 C  CD  . GLU A 1 149 ? 34.903 23.684  5.774  1.00 101.43 ? 146 GLU A CD  1 
ATOM   1130 O  OE1 . GLU A 1 149 ? 33.797 24.116  5.381  1.00 99.27  ? 146 GLU A OE1 1 
ATOM   1131 O  OE2 . GLU A 1 149 ? 35.393 23.971  6.885  1.00 101.48 ? 146 GLU A OE2 1 
ATOM   1132 N  N   . THR A 1 150 ? 33.214 18.884  4.351  1.00 80.60  ? 147 THR A N   1 
ATOM   1133 C  CA  . THR A 1 150 ? 32.206 17.963  3.841  1.00 80.15  ? 147 THR A CA  1 
ATOM   1134 C  C   . THR A 1 150 ? 31.289 17.490  4.963  1.00 71.72  ? 147 THR A C   1 
ATOM   1135 O  O   . THR A 1 150 ? 30.069 17.405  4.779  1.00 69.84  ? 147 THR A O   1 
ATOM   1136 C  CB  . THR A 1 150 ? 32.881 16.776  3.155  1.00 80.02  ? 147 THR A CB  1 
ATOM   1137 O  OG1 . THR A 1 150 ? 33.629 17.242  2.027  1.00 83.17  ? 147 THR A OG1 1 
ATOM   1138 C  CG2 . THR A 1 150 ? 31.839 15.776  2.672  1.00 76.62  ? 147 THR A CG2 1 
ATOM   1139 N  N   . ILE A 1 151 ? 31.858 17.199  6.137  1.00 75.97  ? 148 ILE A N   1 
ATOM   1140 C  CA  . ILE A 1 151 ? 31.048 16.798  7.287  1.00 68.54  ? 148 ILE A CA  1 
ATOM   1141 C  C   . ILE A 1 151 ? 30.030 17.882  7.622  1.00 69.63  ? 148 ILE A C   1 
ATOM   1142 O  O   . ILE A 1 151 ? 28.830 17.614  7.743  1.00 65.20  ? 148 ILE A O   1 
ATOM   1143 C  CB  . ILE A 1 151 ? 31.944 16.482  8.497  1.00 68.25  ? 148 ILE A CB  1 
ATOM   1144 C  CG1 . ILE A 1 151 ? 32.845 15.285  8.202  1.00 71.15  ? 148 ILE A CG1 1 
ATOM   1145 C  CG2 . ILE A 1 151 ? 31.087 16.193  9.727  1.00 66.26  ? 148 ILE A CG2 1 
ATOM   1146 C  CD1 . ILE A 1 151 ? 33.794 14.943  9.328  1.00 68.45  ? 148 ILE A CD1 1 
ATOM   1147 N  N   . ASP A 1 152 ? 30.499 19.125  7.771  1.00 69.85  ? 149 ASP A N   1 
ATOM   1148 C  CA  . ASP A 1 152 ? 29.602 20.227  8.106  1.00 71.70  ? 149 ASP A CA  1 
ATOM   1149 C  C   . ASP A 1 152 ? 28.523 20.396  7.046  1.00 71.09  ? 149 ASP A C   1 
ATOM   1150 O  O   . ASP A 1 152 ? 27.331 20.468  7.365  1.00 71.84  ? 149 ASP A O   1 
ATOM   1151 C  CB  . ASP A 1 152 ? 30.396 21.527  8.276  1.00 72.93  ? 149 ASP A CB  1 
ATOM   1152 C  CG  . ASP A 1 152 ? 30.926 21.713  9.692  1.00 76.27  ? 149 ASP A CG  1 
ATOM   1153 O  OD1 . ASP A 1 152 ? 30.966 20.723  10.455 1.00 76.15  ? 149 ASP A OD1 1 
ATOM   1154 O  OD2 . ASP A 1 152 ? 31.292 22.855  10.045 1.00 78.92  ? 149 ASP A OD2 1 
ATOM   1155 N  N   . ASN A 1 153 ? 28.926 20.464  5.776  1.00 73.98  ? 150 ASN A N   1 
ATOM   1156 C  CA  . ASN A 1 153 ? 27.960 20.609  4.692  1.00 72.82  ? 150 ASN A CA  1 
ATOM   1157 C  C   . ASN A 1 153 ? 26.962 19.457  4.691  1.00 69.35  ? 150 ASN A C   1 
ATOM   1158 O  O   . ASN A 1 153 ? 25.752 19.669  4.549  1.00 70.07  ? 150 ASN A O   1 
ATOM   1159 C  CB  . ASN A 1 153 ? 28.691 20.696  3.349  1.00 73.60  ? 150 ASN A CB  1 
ATOM   1160 C  CG  . ASN A 1 153 ? 29.591 21.924  3.244  1.00 80.67  ? 150 ASN A CG  1 
ATOM   1161 O  OD1 . ASN A 1 153 ? 29.667 22.743  4.163  1.00 79.25  ? 150 ASN A OD1 1 
ATOM   1162 N  ND2 . ASN A 1 153 ? 30.295 22.043  2.122  1.00 80.68  ? 150 ASN A ND2 1 
ATOM   1163 N  N   . GLU A 1 154 ? 27.448 18.227  4.865  1.00 67.75  ? 151 GLU A N   1 
ATOM   1164 C  CA  . GLU A 1 154 ? 26.550 17.079  4.815  1.00 65.05  ? 151 GLU A CA  1 
ATOM   1165 C  C   . GLU A 1 154 ? 25.612 17.062  6.015  1.00 65.30  ? 151 GLU A C   1 
ATOM   1166 O  O   . GLU A 1 154 ? 24.442 16.684  5.888  1.00 64.79  ? 151 GLU A O   1 
ATOM   1167 C  CB  . GLU A 1 154 ? 27.355 15.783  4.727  1.00 66.05  ? 151 GLU A CB  1 
ATOM   1168 C  CG  . GLU A 1 154 ? 27.791 15.437  3.302  1.00 67.63  ? 151 GLU A CG  1 
ATOM   1169 C  CD  . GLU A 1 154 ? 28.691 14.210  3.225  1.00 72.13  ? 151 GLU A CD  1 
ATOM   1170 O  OE1 . GLU A 1 154 ? 29.038 13.646  4.283  1.00 69.10  ? 151 GLU A OE1 1 
ATOM   1171 O  OE2 . GLU A 1 154 ? 29.067 13.817  2.100  1.00 73.31  ? 151 GLU A OE2 1 
ATOM   1172 N  N   . MET A 1 155 ? 26.102 17.487  7.186  1.00 65.87  ? 152 MET A N   1 
ATOM   1173 C  CA  . MET A 1 155 ? 25.244 17.573  8.369  1.00 66.43  ? 152 MET A CA  1 
ATOM   1174 C  C   . MET A 1 155 ? 24.171 18.651  8.240  1.00 66.75  ? 152 MET A C   1 
ATOM   1175 O  O   . MET A 1 155 ? 23.112 18.531  8.864  1.00 65.54  ? 152 MET A O   1 
ATOM   1176 C  CB  . MET A 1 155 ? 26.092 17.808  9.624  1.00 64.34  ? 152 MET A CB  1 
ATOM   1177 C  CG  . MET A 1 155 ? 26.855 16.591  10.176 1.00 57.50  ? 152 MET A CG  1 
ATOM   1178 S  SD  . MET A 1 155 ? 25.964 15.005  10.210 1.00 56.59  ? 152 MET A SD  1 
ATOM   1179 C  CE  . MET A 1 155 ? 24.877 15.278  11.609 1.00 57.31  ? 152 MET A CE  1 
ATOM   1180 N  N   . ASP A 1 156 ? 24.400 19.704  7.445  1.00 67.58  ? 153 ASP A N   1 
ATOM   1181 C  CA  . ASP A 1 156 ? 23.318 20.665  7.247  1.00 68.66  ? 153 ASP A CA  1 
ATOM   1182 C  C   . ASP A 1 156 ? 22.184 20.100  6.397  1.00 67.93  ? 153 ASP A C   1 
ATOM   1183 O  O   . ASP A 1 156 ? 21.091 20.679  6.389  1.00 67.44  ? 153 ASP A O   1 
ATOM   1184 C  CB  . ASP A 1 156 ? 23.825 21.977  6.628  1.00 71.73  ? 153 ASP A CB  1 
ATOM   1185 C  CG  . ASP A 1 156 ? 25.138 22.457  7.235  1.00 76.90  ? 153 ASP A CG  1 
ATOM   1186 O  OD1 . ASP A 1 156 ? 26.041 22.858  6.467  1.00 81.04  ? 153 ASP A OD1 1 
ATOM   1187 O  OD2 . ASP A 1 156 ? 25.266 22.446  8.479  1.00 77.22  ? 153 ASP A OD2 1 
ATOM   1188 N  N   . HIS A 1 157 ? 22.408 18.989  5.694  1.00 66.15  ? 154 HIS A N   1 
ATOM   1189 C  CA  . HIS A 1 157 ? 21.360 18.328  4.924  1.00 67.32  ? 154 HIS A CA  1 
ATOM   1190 C  C   . HIS A 1 157 ? 20.909 17.014  5.546  1.00 66.59  ? 154 HIS A C   1 
ATOM   1191 O  O   . HIS A 1 157 ? 20.124 16.286  4.933  1.00 64.17  ? 154 HIS A O   1 
ATOM   1192 C  CB  . HIS A 1 157 ? 21.821 18.092  3.487  1.00 66.40  ? 154 HIS A CB  1 
ATOM   1193 C  CG  . HIS A 1 157 ? 22.131 19.353  2.745  1.00 71.10  ? 154 HIS A CG  1 
ATOM   1194 N  ND1 . HIS A 1 157 ? 23.415 19.826  2.578  1.00 74.33  ? 154 HIS A ND1 1 
ATOM   1195 C  CD2 . HIS A 1 157 ? 21.316 20.259  2.156  1.00 72.37  ? 154 HIS A CD2 1 
ATOM   1196 C  CE1 . HIS A 1 157 ? 23.379 20.958  1.898  1.00 77.69  ? 154 HIS A CE1 1 
ATOM   1197 N  NE2 . HIS A 1 157 ? 22.116 21.245  1.631  1.00 79.24  ? 154 HIS A NE2 1 
ATOM   1198 N  N   . PHE A 1 158 ? 21.379 16.701  6.748  1.00 64.88  ? 155 PHE A N   1 
ATOM   1199 C  CA  . PHE A 1 158 ? 20.972 15.496  7.458  1.00 61.79  ? 155 PHE A CA  1 
ATOM   1200 C  C   . PHE A 1 158 ? 19.657 15.795  8.174  1.00 64.41  ? 155 PHE A C   1 
ATOM   1201 O  O   . PHE A 1 158 ? 19.622 16.620  9.094  1.00 66.57  ? 155 PHE A O   1 
ATOM   1202 C  CB  . PHE A 1 158 ? 22.070 15.092  8.436  1.00 60.42  ? 155 PHE A CB  1 
ATOM   1203 C  CG  . PHE A 1 158 ? 21.806 13.811  9.166  1.00 61.52  ? 155 PHE A CG  1 
ATOM   1204 C  CD1 . PHE A 1 158 ? 21.851 12.593  8.505  1.00 59.57  ? 155 PHE A CD1 1 
ATOM   1205 C  CD2 . PHE A 1 158 ? 21.500 13.825  10.521 1.00 58.86  ? 155 PHE A CD2 1 
ATOM   1206 C  CE1 . PHE A 1 158 ? 21.613 11.409  9.194  1.00 59.69  ? 155 PHE A CE1 1 
ATOM   1207 C  CE2 . PHE A 1 158 ? 21.255 12.650  11.206 1.00 56.20  ? 155 PHE A CE2 1 
ATOM   1208 C  CZ  . PHE A 1 158 ? 21.310 11.443  10.542 1.00 57.21  ? 155 PHE A CZ  1 
ATOM   1209 N  N   . LYS A 1 159 ? 18.567 15.148  7.741  1.00 63.20  ? 156 LYS A N   1 
ATOM   1210 C  CA  . LYS A 1 159 ? 17.216 15.418  8.238  1.00 61.90  ? 156 LYS A CA  1 
ATOM   1211 C  C   . LYS A 1 159 ? 16.711 14.271  9.102  1.00 57.61  ? 156 LYS A C   1 
ATOM   1212 O  O   . LYS A 1 159 ? 16.065 13.347  8.590  1.00 54.27  ? 156 LYS A O   1 
ATOM   1213 C  CB  . LYS A 1 159 ? 16.239 15.680  7.084  1.00 61.73  ? 156 LYS A CB  1 
ATOM   1214 C  CG  . LYS A 1 159 ? 16.556 16.814  6.096  1.00 65.23  ? 156 LYS A CG  1 
ATOM   1215 C  CD  . LYS A 1 159 ? 17.670 17.771  6.515  1.00 75.34  ? 156 LYS A CD  1 
ATOM   1216 C  CE  . LYS A 1 159 ? 17.215 18.802  7.554  1.00 77.07  ? 156 LYS A CE  1 
ATOM   1217 N  NZ  . LYS A 1 159 ? 18.306 19.775  7.887  1.00 76.83  ? 156 LYS A NZ  1 
ATOM   1218 N  N   . PRO A 1 160 ? 16.921 14.312  10.417 1.00 56.28  ? 157 PRO A N   1 
ATOM   1219 C  CA  . PRO A 1 160 ? 16.539 13.187  11.283 1.00 55.35  ? 157 PRO A CA  1 
ATOM   1220 C  C   . PRO A 1 160 ? 15.104 13.206  11.793 1.00 52.67  ? 157 PRO A C   1 
ATOM   1221 O  O   . PRO A 1 160 ? 14.743 12.321  12.576 1.00 50.36  ? 157 PRO A O   1 
ATOM   1222 C  CB  . PRO A 1 160 ? 17.520 13.339  12.457 1.00 52.47  ? 157 PRO A CB  1 
ATOM   1223 C  CG  . PRO A 1 160 ? 17.795 14.832  12.536 1.00 57.71  ? 157 PRO A CG  1 
ATOM   1224 C  CD  . PRO A 1 160 ? 17.385 15.466  11.204 1.00 58.77  ? 157 PRO A CD  1 
ATOM   1225 N  N   . THR A 1 161 ? 14.271 14.154  11.354 1.00 50.69  ? 158 THR A N   1 
ATOM   1226 C  CA  . THR A 1 161 ? 12.987 14.383  12.013 1.00 52.06  ? 158 THR A CA  1 
ATOM   1227 C  C   . THR A 1 161 ? 12.032 13.208  11.831 1.00 52.27  ? 158 THR A C   1 
ATOM   1228 O  O   . THR A 1 161 ? 11.442 12.723  12.805 1.00 51.29  ? 158 THR A O   1 
ATOM   1229 C  CB  . THR A 1 161 ? 12.362 15.674  11.495 1.00 57.36  ? 158 THR A CB  1 
ATOM   1230 O  OG1 . THR A 1 161 ? 13.204 16.775  11.853 1.00 59.32  ? 158 THR A OG1 1 
ATOM   1231 C  CG2 . THR A 1 161 ? 10.975 15.879  12.087 1.00 60.27  ? 158 THR A CG2 1 
ATOM   1232 N  N   . GLU A 1 162 ? 11.863 12.738  10.592 1.00 50.75  ? 159 GLU A N   1 
ATOM   1233 C  CA  . GLU A 1 162 ? 10.913 11.657  10.346 1.00 49.40  ? 159 GLU A CA  1 
ATOM   1234 C  C   . GLU A 1 162 ? 11.343 10.381  11.069 1.00 52.40  ? 159 GLU A C   1 
ATOM   1235 O  O   . GLU A 1 162 ? 10.509 9.666   11.640 1.00 51.28  ? 159 GLU A O   1 
ATOM   1236 C  CB  . GLU A 1 162 ? 10.778 11.430  8.836  1.00 55.09  ? 159 GLU A CB  1 
ATOM   1237 C  CG  . GLU A 1 162 ? 10.078 10.142  8.416  1.00 57.76  ? 159 GLU A CG  1 
ATOM   1238 C  CD  . GLU A 1 162 ? 11.001 8.942   8.270  1.00 65.11  ? 159 GLU A CD  1 
ATOM   1239 O  OE1 . GLU A 1 162 ? 10.478 7.834   8.008  1.00 67.59  ? 159 GLU A OE1 1 
ATOM   1240 O  OE2 . GLU A 1 162 ? 12.233 9.087   8.418  1.00 71.00  ? 159 GLU A OE2 1 
ATOM   1241 N  N   . THR A 1 163 ? 12.646 10.092  11.066 1.00 51.19  ? 160 THR A N   1 
ATOM   1242 C  CA  . THR A 1 163 ? 13.156 8.913   11.760 1.00 46.13  ? 160 THR A CA  1 
ATOM   1243 C  C   . THR A 1 163 ? 12.844 8.981   13.245 1.00 48.49  ? 160 THR A C   1 
ATOM   1244 O  O   . THR A 1 163 ? 12.351 8.012   13.835 1.00 43.65  ? 160 THR A O   1 
ATOM   1245 C  CB  . THR A 1 163 ? 14.664 8.796   11.543 1.00 53.28  ? 160 THR A CB  1 
ATOM   1246 O  OG1 . THR A 1 163 ? 14.932 8.485   10.170 1.00 50.86  ? 160 THR A OG1 1 
ATOM   1247 C  CG2 . THR A 1 163 ? 15.262 7.723   12.447 1.00 46.45  ? 160 THR A CG2 1 
ATOM   1248 N  N   . LEU A 1 164 ? 13.133 10.127  13.863 1.00 43.93  ? 161 LEU A N   1 
ATOM   1249 C  CA  . LEU A 1 164 ? 12.895 10.301  15.291 1.00 49.54  ? 161 LEU A CA  1 
ATOM   1250 C  C   . LEU A 1 164 ? 11.408 10.259  15.620 1.00 48.63  ? 161 LEU A C   1 
ATOM   1251 O  O   . LEU A 1 164 ? 11.030 9.799   16.705 1.00 47.10  ? 161 LEU A O   1 
ATOM   1252 C  CB  . LEU A 1 164 ? 13.533 11.617  15.741 1.00 49.81  ? 161 LEU A CB  1 
ATOM   1253 C  CG  . LEU A 1 164 ? 15.063 11.598  15.814 1.00 48.38  ? 161 LEU A CG  1 
ATOM   1254 C  CD1 . LEU A 1 164 ? 15.593 12.811  16.539 1.00 47.28  ? 161 LEU A CD1 1 
ATOM   1255 C  CD2 . LEU A 1 164 ? 15.538 10.338  16.534 1.00 41.60  ? 161 LEU A CD2 1 
ATOM   1256 N  N   . LYS A 1 165 ? 10.551 10.709  14.694 1.00 45.33  ? 162 LYS A N   1 
ATOM   1257 C  CA  . LYS A 1 165 ? 9.112  10.622  14.921 1.00 45.93  ? 162 LYS A CA  1 
ATOM   1258 C  C   . LYS A 1 165 ? 8.644  9.172   14.922 1.00 48.97  ? 162 LYS A C   1 
ATOM   1259 O  O   . LYS A 1 165 ? 7.826  8.779   15.765 1.00 45.98  ? 162 LYS A O   1 
ATOM   1260 C  CB  . LYS A 1 165 ? 8.342  11.429  13.874 1.00 48.97  ? 162 LYS A CB  1 
ATOM   1261 C  CG  . LYS A 1 165 ? 6.838  11.496  14.166 1.00 53.35  ? 162 LYS A CG  1 
ATOM   1262 C  CD  . LYS A 1 165 ? 6.071  12.382  13.198 1.00 65.23  ? 162 LYS A CD  1 
ATOM   1263 C  CE  . LYS A 1 165 ? 4.717  11.776  12.814 1.00 68.74  ? 162 LYS A CE  1 
ATOM   1264 N  NZ  . LYS A 1 165 ? 4.727  11.029  11.519 1.00 71.36  ? 162 LYS A NZ  1 
ATOM   1265 N  N   . GLU A 1 166 ? 9.152  8.355   13.993 1.00 43.86  ? 163 GLU A N   1 
ATOM   1266 C  CA  . GLU A 1 166 ? 8.807  6.937   14.013 1.00 44.50  ? 163 GLU A CA  1 
ATOM   1267 C  C   . GLU A 1 166 ? 9.346  6.262   15.258 1.00 42.05  ? 163 GLU A C   1 
ATOM   1268 O  O   . GLU A 1 166 ? 8.669  5.417   15.855 1.00 42.94  ? 163 GLU A O   1 
ATOM   1269 C  CB  . GLU A 1 166 ? 9.361  6.216   12.797 1.00 44.41  ? 163 GLU A CB  1 
ATOM   1270 C  CG  . GLU A 1 166 ? 8.921  6.715   11.457 1.00 50.02  ? 163 GLU A CG  1 
ATOM   1271 C  CD  . GLU A 1 166 ? 9.416  5.770   10.395 1.00 58.75  ? 163 GLU A CD  1 
ATOM   1272 O  OE1 . GLU A 1 166 ? 10.613 5.864   10.046 1.00 57.39  ? 163 GLU A OE1 1 
ATOM   1273 O  OE2 . GLU A 1 166 ? 8.623  4.913   9.939  1.00 63.78  ? 163 GLU A OE2 1 
ATOM   1274 N  N   . LEU A 1 167 ? 10.591 6.575   15.625 1.00 39.00  ? 164 LEU A N   1 
ATOM   1275 C  CA  . LEU A 1 167 ? 11.159 6.037   16.853 1.00 43.02  ? 164 LEU A CA  1 
ATOM   1276 C  C   . LEU A 1 167 ? 10.276 6.381   18.040 1.00 42.61  ? 164 LEU A C   1 
ATOM   1277 O  O   . LEU A 1 167 ? 9.992  5.526   18.884 1.00 37.68  ? 164 LEU A O   1 
ATOM   1278 C  CB  . LEU A 1 167 ? 12.569 6.582   17.059 1.00 44.42  ? 164 LEU A CB  1 
ATOM   1279 C  CG  . LEU A 1 167 ? 13.309 6.051   18.282 1.00 45.11  ? 164 LEU A CG  1 
ATOM   1280 C  CD1 . LEU A 1 167 ? 13.406 4.530   18.229 1.00 42.95  ? 164 LEU A CD1 1 
ATOM   1281 C  CD2 . LEU A 1 167 ? 14.685 6.691   18.396 1.00 44.73  ? 164 LEU A CD2 1 
ATOM   1282 N  N   . SER A 1 168 ? 9.810  7.631   18.097 1.00 42.13  ? 165 SER A N   1 
ATOM   1283 C  CA  . SER A 1 168 ? 8.942  8.070   19.182 1.00 43.72  ? 165 SER A CA  1 
ATOM   1284 C  C   . SER A 1 168 ? 7.656  7.257   19.225 1.00 43.44  ? 165 SER A C   1 
ATOM   1285 O  O   . SER A 1 168 ? 7.235  6.786   20.288 1.00 41.71  ? 165 SER A O   1 
ATOM   1286 C  CB  . SER A 1 168 ? 8.633  9.555   19.012 1.00 42.20  ? 165 SER A CB  1 
ATOM   1287 O  OG  . SER A 1 168 ? 7.912  10.042  20.124 1.00 49.96  ? 165 SER A OG  1 
ATOM   1288 N  N   . GLU A 1 169 ? 7.017  7.083   18.069 1.00 40.40  ? 166 GLU A N   1 
ATOM   1289 C  CA  . GLU A 1 169 ? 5.764  6.341   18.007 1.00 42.19  ? 166 GLU A CA  1 
ATOM   1290 C  C   . GLU A 1 169 ? 5.961  4.868   18.340 1.00 39.41  ? 166 GLU A C   1 
ATOM   1291 O  O   . GLU A 1 169 ? 5.097  4.259   18.982 1.00 38.86  ? 166 GLU A O   1 
ATOM   1292 C  CB  . GLU A 1 169 ? 5.149  6.509   16.620 1.00 44.17  ? 166 GLU A CB  1 
ATOM   1293 C  CG  . GLU A 1 169 ? 4.641  7.925   16.389 1.00 48.16  ? 166 GLU A CG  1 
ATOM   1294 C  CD  . GLU A 1 169 ? 4.213  8.181   14.953 1.00 59.48  ? 166 GLU A CD  1 
ATOM   1295 O  OE1 . GLU A 1 169 ? 3.775  9.312   14.663 1.00 62.12  ? 166 GLU A OE1 1 
ATOM   1296 O  OE2 . GLU A 1 169 ? 4.331  7.258   14.116 1.00 58.28  ? 166 GLU A OE2 1 
ATOM   1297 N  N   . ALA A 1 170 ? 7.083  4.279   17.927 1.00 36.42  ? 167 ALA A N   1 
ATOM   1298 C  CA  . ALA A 1 170 ? 7.350  2.891   18.298 1.00 36.03  ? 167 ALA A CA  1 
ATOM   1299 C  C   . ALA A 1 170 ? 7.518  2.743   19.805 1.00 38.13  ? 167 ALA A C   1 
ATOM   1300 O  O   . ALA A 1 170 ? 7.000  1.790   20.404 1.00 34.96  ? 167 ALA A O   1 
ATOM   1301 C  CB  . ALA A 1 170 ? 8.588  2.382   17.569 1.00 35.65  ? 167 ALA A CB  1 
ATOM   1302 N  N   . LEU A 1 171 ? 8.240  3.676   20.439 1.00 34.40  ? 168 LEU A N   1 
ATOM   1303 C  CA  . LEU A 1 171 ? 8.437  3.590   21.881 1.00 37.27  ? 168 LEU A CA  1 
ATOM   1304 C  C   . LEU A 1 171 ? 7.124  3.757   22.624 1.00 37.27  ? 168 LEU A C   1 
ATOM   1305 O  O   . LEU A 1 171 ? 6.868  3.041   23.596 1.00 35.02  ? 168 LEU A O   1 
ATOM   1306 C  CB  . LEU A 1 171 ? 9.456  4.623   22.368 1.00 35.87  ? 168 LEU A CB  1 
ATOM   1307 C  CG  . LEU A 1 171 ? 10.870 4.325   21.867 1.00 39.91  ? 168 LEU A CG  1 
ATOM   1308 C  CD1 . LEU A 1 171 ? 11.796 5.526   22.015 1.00 36.83  ? 168 LEU A CD1 1 
ATOM   1309 C  CD2 . LEU A 1 171 ? 11.426 3.108   22.582 1.00 37.16  ? 168 LEU A CD2 1 
ATOM   1310 N  N   . ASP A 1 172 ? 6.278  4.694   22.185 1.00 37.31  ? 169 ASP A N   1 
ATOM   1311 C  CA  . ASP A 1 172 ? 4.984  4.876   22.840 1.00 36.63  ? 169 ASP A CA  1 
ATOM   1312 C  C   . ASP A 1 172 ? 4.118  3.626   22.725 1.00 37.62  ? 169 ASP A C   1 
ATOM   1313 O  O   . ASP A 1 172 ? 3.431  3.249   23.681 1.00 37.85  ? 169 ASP A O   1 
ATOM   1314 C  CB  . ASP A 1 172 ? 4.255  6.088   22.258 1.00 41.19  ? 169 ASP A CB  1 
ATOM   1315 C  CG  . ASP A 1 172 ? 4.851  7.416   22.729 1.00 46.39  ? 169 ASP A CG  1 
ATOM   1316 O  OD1 . ASP A 1 172 ? 5.509  7.441   23.802 1.00 48.50  ? 169 ASP A OD1 1 
ATOM   1317 O  OD2 . ASP A 1 172 ? 4.638  8.440   22.045 1.00 51.28  ? 169 ASP A OD2 1 
ATOM   1318 N  N   . THR A 1 173 ? 4.123  2.980   21.557 1.00 36.62  ? 170 THR A N   1 
ATOM   1319 C  CA  . THR A 1 173 ? 3.335  1.764   21.398 1.00 38.17  ? 170 THR A CA  1 
ATOM   1320 C  C   . THR A 1 173 ? 3.809  0.684   22.361 1.00 36.77  ? 170 THR A C   1 
ATOM   1321 O  O   . THR A 1 173 ? 2.996  0.022   23.015 1.00 37.64  ? 170 THR A O   1 
ATOM   1322 C  CB  . THR A 1 173 ? 3.412  1.269   19.959 1.00 41.01  ? 170 THR A CB  1 
ATOM   1323 O  OG1 . THR A 1 173 ? 2.791  2.234   19.115 1.00 40.07  ? 170 THR A OG1 1 
ATOM   1324 C  CG2 . THR A 1 173 ? 2.668  -0.051  19.810 1.00 38.58  ? 170 THR A CG2 1 
ATOM   1325 N  N   . ILE A 1 174 ? 5.123  0.511   22.485 1.00 33.79  ? 171 ILE A N   1 
ATOM   1326 C  CA  . ILE A 1 174 ? 5.629  -0.539  23.359 1.00 33.09  ? 171 ILE A CA  1 
ATOM   1327 C  C   . ILE A 1 174 ? 5.314  -0.219  24.810 1.00 35.03  ? 171 ILE A C   1 
ATOM   1328 O  O   . ILE A 1 174 ? 4.976  -1.116  25.596 1.00 33.66  ? 171 ILE A O   1 
ATOM   1329 C  CB  . ILE A 1 174 ? 7.132  -0.757  23.121 1.00 31.78  ? 171 ILE A CB  1 
ATOM   1330 C  CG1 . ILE A 1 174 ? 7.339  -1.364  21.730 1.00 34.57  ? 171 ILE A CG1 1 
ATOM   1331 C  CG2 . ILE A 1 174 ? 7.716  -1.673  24.215 1.00 30.95  ? 171 ILE A CG2 1 
ATOM   1332 C  CD1 . ILE A 1 174 ? 8.805  -1.409  21.269 1.00 33.68  ? 171 ILE A CD1 1 
ATOM   1333 N  N   . LYS A 1 175 ? 5.393  1.061   25.194 1.00 32.48  ? 172 LYS A N   1 
ATOM   1334 C  CA  . LYS A 1 175 ? 5.045  1.418   26.566 1.00 33.12  ? 172 LYS A CA  1 
ATOM   1335 C  C   . LYS A 1 175 ? 3.618  0.993   26.897 1.00 35.98  ? 172 LYS A C   1 
ATOM   1336 O  O   . LYS A 1 175 ? 3.338  0.555   28.020 1.00 33.44  ? 172 LYS A O   1 
ATOM   1337 C  CB  . LYS A 1 175 ? 5.216  2.922   26.790 1.00 34.68  ? 172 LYS A CB  1 
ATOM   1338 C  CG  . LYS A 1 175 ? 4.798  3.373   28.191 1.00 36.11  ? 172 LYS A CG  1 
ATOM   1339 C  CD  . LYS A 1 175 ? 5.130  4.837   28.458 1.00 38.37  ? 172 LYS A CD  1 
ATOM   1340 C  CE  . LYS A 1 175 ? 4.578  5.254   29.817 1.00 46.61  ? 172 LYS A CE  1 
ATOM   1341 N  NZ  . LYS A 1 175 ? 4.878  6.670   30.156 1.00 56.51  ? 172 LYS A NZ  1 
ATOM   1342 N  N   . GLU A 1 176 ? 2.701  1.100   25.932 1.00 34.57  ? 173 GLU A N   1 
ATOM   1343 C  CA  . GLU A 1 176 ? 1.334  0.683   26.210 1.00 38.75  ? 173 GLU A CA  1 
ATOM   1344 C  C   . GLU A 1 176 ? 1.143  -0.827  26.143 1.00 40.77  ? 173 GLU A C   1 
ATOM   1345 O  O   . GLU A 1 176 ? 0.076  -1.315  26.534 1.00 40.03  ? 173 GLU A O   1 
ATOM   1346 C  CB  . GLU A 1 176 ? 0.366  1.384   25.262 1.00 44.18  ? 173 GLU A CB  1 
ATOM   1347 C  CG  . GLU A 1 176 ? 0.396  2.885   25.461 1.00 46.35  ? 173 GLU A CG  1 
ATOM   1348 C  CD  . GLU A 1 176 ? -0.178 3.298   26.822 1.00 56.28  ? 173 GLU A CD  1 
ATOM   1349 O  OE1 . GLU A 1 176 ? 0.443  4.162   27.488 1.00 59.03  ? 173 GLU A OE1 1 
ATOM   1350 O  OE2 . GLU A 1 176 ? -1.228 2.750   27.236 1.00 56.82  ? 173 GLU A OE2 1 
ATOM   1351 N  N   . GLN A 1 177 ? 2.144  -1.577  25.685 1.00 33.69  ? 174 GLN A N   1 
ATOM   1352 C  CA  . GLN A 1 177 ? 2.073  -3.034  25.696 1.00 35.90  ? 174 GLN A CA  1 
ATOM   1353 C  C   . GLN A 1 177 ? 2.748  -3.669  26.899 1.00 33.43  ? 174 GLN A C   1 
ATOM   1354 O  O   . GLN A 1 177 ? 2.698  -4.900  27.028 1.00 31.38  ? 174 GLN A O   1 
ATOM   1355 C  CB  . GLN A 1 177 ? 2.721  -3.631  24.439 1.00 33.72  ? 174 GLN A CB  1 
ATOM   1356 C  CG  . GLN A 1 177 ? 1.976  -3.390  23.161 1.00 37.81  ? 174 GLN A CG  1 
ATOM   1357 C  CD  . GLN A 1 177 ? 2.732  -3.938  21.976 1.00 38.64  ? 174 GLN A CD  1 
ATOM   1358 O  OE1 . GLN A 1 177 ? 3.847  -3.510  21.680 1.00 36.18  ? 174 GLN A OE1 1 
ATOM   1359 N  NE2 . GLN A 1 177 ? 2.141  -4.923  21.304 1.00 41.89  ? 174 GLN A NE2 1 
ATOM   1360 N  N   . VAL A 1 178 ? 3.422  -2.879  27.742 1.00 31.04  ? 175 VAL A N   1 
ATOM   1361 C  CA  . VAL A 1 178 ? 4.191  -3.435  28.856 1.00 34.54  ? 175 VAL A CA  1 
ATOM   1362 C  C   . VAL A 1 178 ? 3.319  -4.277  29.768 1.00 31.64  ? 175 VAL A C   1 
ATOM   1363 O  O   . VAL A 1 178 ? 3.777  -5.290  30.319 1.00 29.47  ? 175 VAL A O   1 
ATOM   1364 C  CB  . VAL A 1 178 ? 4.879  -2.307  29.650 1.00 32.97  ? 175 VAL A CB  1 
ATOM   1365 C  CG1 . VAL A 1 178 ? 5.380  -2.821  30.961 1.00 35.87  ? 175 VAL A CG1 1 
ATOM   1366 C  CG2 . VAL A 1 178 ? 6.028  -1.749  28.848 1.00 36.77  ? 175 VAL A CG2 1 
ATOM   1367 N  N   . ASP A 1 179 ? 2.059  -3.880  29.954 1.00 31.41  ? 176 ASP A N   1 
ATOM   1368 C  CA  . ASP A 1 179 ? 1.192  -4.598  30.881 1.00 36.54  ? 176 ASP A CA  1 
ATOM   1369 C  C   . ASP A 1 179 ? 0.805  -5.986  30.385 1.00 34.52  ? 176 ASP A C   1 
ATOM   1370 O  O   . ASP A 1 179 ? 0.241  -6.762  31.166 1.00 32.71  ? 176 ASP A O   1 
ATOM   1371 C  CB  . ASP A 1 179 ? -0.049 -3.754  31.197 1.00 37.44  ? 176 ASP A CB  1 
ATOM   1372 C  CG  . ASP A 1 179 ? -0.826 -3.354  29.953 1.00 43.49  ? 176 ASP A CG  1 
ATOM   1373 O  OD1 . ASP A 1 179 ? -0.482 -3.809  28.846 1.00 48.55  ? 176 ASP A OD1 1 
ATOM   1374 O  OD2 . ASP A 1 179 ? -1.792 -2.569  30.068 1.00 54.72  ? 176 ASP A OD2 1 
ATOM   1375 N  N   . GLU A 1 180 ? 1.122  -6.322  29.137 1.00 29.60  ? 177 GLU A N   1 
ATOM   1376 C  CA  . GLU A 1 180 ? 0.896  -7.651  28.581 1.00 29.28  ? 177 GLU A CA  1 
ATOM   1377 C  C   . GLU A 1 180 ? 2.062  -8.598  28.801 1.00 30.68  ? 177 GLU A C   1 
ATOM   1378 O  O   . GLU A 1 180 ? 1.919  -9.795  28.545 1.00 29.40  ? 177 GLU A O   1 
ATOM   1379 C  CB  . GLU A 1 180 ? 0.602  -7.564  27.070 1.00 31.28  ? 177 GLU A CB  1 
ATOM   1380 C  CG  . GLU A 1 180 ? -0.396 -6.452  26.687 1.00 35.44  ? 177 GLU A CG  1 
ATOM   1381 C  CD  . GLU A 1 180 ? -0.552 -6.287  25.165 1.00 41.68  ? 177 GLU A CD  1 
ATOM   1382 O  OE1 . GLU A 1 180 ? -1.207 -5.308  24.721 1.00 44.51  ? 177 GLU A OE1 1 
ATOM   1383 O  OE2 . GLU A 1 180 ? -0.033 -7.142  24.404 1.00 40.85  ? 177 GLU A OE2 1 
ATOM   1384 N  N   . VAL A 1 181 ? 3.212  -8.090  29.237 1.00 27.15  ? 178 VAL A N   1 
ATOM   1385 C  CA  . VAL A 1 181 ? 4.404  -8.919  29.377 1.00 27.69  ? 178 VAL A CA  1 
ATOM   1386 C  C   . VAL A 1 181 ? 4.215  -9.887  30.543 1.00 28.44  ? 178 VAL A C   1 
ATOM   1387 O  O   . VAL A 1 181 ? 3.843  -9.485  31.652 1.00 27.53  ? 178 VAL A O   1 
ATOM   1388 C  CB  . VAL A 1 181 ? 5.641  -8.022  29.555 1.00 26.68  ? 178 VAL A CB  1 
ATOM   1389 C  CG1 . VAL A 1 181 ? 6.842  -8.835  30.027 1.00 27.31  ? 178 VAL A CG1 1 
ATOM   1390 C  CG2 . VAL A 1 181 ? 5.945  -7.250  28.227 1.00 25.24  ? 178 VAL A CG2 1 
ATOM   1391 N  N   . LEU A 1 182 ? 4.433  -11.186 30.285 1.00 24.59  ? 179 LEU A N   1 
ATOM   1392 C  CA  . LEU A 1 182 ? 4.237  -12.238 31.287 1.00 25.03  ? 179 LEU A CA  1 
ATOM   1393 C  C   . LEU A 1 182 ? 5.503  -12.975 31.701 1.00 28.43  ? 179 LEU A C   1 
ATOM   1394 O  O   . LEU A 1 182 ? 5.471  -13.703 32.701 1.00 28.36  ? 179 LEU A O   1 
ATOM   1395 C  CB  . LEU A 1 182 ? 3.260  -13.300 30.765 1.00 26.46  ? 179 LEU A CB  1 
ATOM   1396 C  CG  . LEU A 1 182 ? 1.866  -12.837 30.386 1.00 31.41  ? 179 LEU A CG  1 
ATOM   1397 C  CD1 . LEU A 1 182 ? 1.121  -13.960 29.663 1.00 32.45  ? 179 LEU A CD1 1 
ATOM   1398 C  CD2 . LEU A 1 182 ? 1.125  -12.393 31.611 1.00 30.84  ? 179 LEU A CD2 1 
ATOM   1399 N  N   . ASP A 1 183 ? 6.608  -12.844 30.957 1.00 24.62  ? 180 ASP A N   1 
ATOM   1400 C  CA  . ASP A 1 183 ? 7.691  -13.781 31.225 1.00 24.79  ? 180 ASP A CA  1 
ATOM   1401 C  C   . ASP A 1 183 ? 8.648  -13.261 32.283 1.00 25.21  ? 180 ASP A C   1 
ATOM   1402 O  O   . ASP A 1 183 ? 8.671  -12.062 32.584 1.00 26.15  ? 180 ASP A O   1 
ATOM   1403 C  CB  . ASP A 1 183 ? 8.435  -14.103 29.923 1.00 26.29  ? 180 ASP A CB  1 
ATOM   1404 C  CG  . ASP A 1 183 ? 7.512  -14.684 28.879 1.00 33.67  ? 180 ASP A CG  1 
ATOM   1405 O  OD1 . ASP A 1 183 ? 7.178  -15.878 29.015 1.00 34.12  ? 180 ASP A OD1 1 
ATOM   1406 O  OD2 . ASP A 1 183 ? 7.180  -13.996 27.883 1.00 32.88  ? 180 ASP A OD2 1 
ATOM   1407 N  N   . PRO A 1 184 ? 9.448  -14.152 32.882 1.00 24.88  ? 181 PRO A N   1 
ATOM   1408 C  CA  . PRO A 1 184 ? 10.369 -13.720 33.938 1.00 24.26  ? 181 PRO A CA  1 
ATOM   1409 C  C   . PRO A 1 184 ? 11.280 -12.629 33.402 1.00 23.09  ? 181 PRO A C   1 
ATOM   1410 O  O   . PRO A 1 184 ? 11.621 -12.621 32.220 1.00 22.55  ? 181 PRO A O   1 
ATOM   1411 C  CB  . PRO A 1 184 ? 11.147 -14.996 34.282 1.00 27.97  ? 181 PRO A CB  1 
ATOM   1412 C  CG  . PRO A 1 184 ? 10.208 -16.127 33.875 1.00 25.48  ? 181 PRO A CG  1 
ATOM   1413 C  CD  . PRO A 1 184 ? 9.499  -15.609 32.648 1.00 26.79  ? 181 PRO A CD  1 
ATOM   1414 N  N   . ILE A 1 185 ? 11.626 -11.661 34.255 1.00 23.80  ? 182 ILE A N   1 
ATOM   1415 C  CA  . ILE A 1 185 ? 12.297 -10.471 33.730 1.00 23.04  ? 182 ILE A CA  1 
ATOM   1416 C  C   . ILE A 1 185 ? 13.342 -9.954  34.702 1.00 23.81  ? 182 ILE A C   1 
ATOM   1417 O  O   . ILE A 1 185 ? 13.150 -9.963  35.925 1.00 23.16  ? 182 ILE A O   1 
ATOM   1418 C  CB  . ILE A 1 185 ? 11.298 -9.350  33.346 1.00 27.06  ? 182 ILE A CB  1 
ATOM   1419 C  CG1 . ILE A 1 185 ? 12.029 -8.141  32.734 1.00 27.19  ? 182 ILE A CG1 1 
ATOM   1420 C  CG2 . ILE A 1 185 ? 10.506 -8.915  34.552 1.00 26.77  ? 182 ILE A CG2 1 
ATOM   1421 C  CD1 . ILE A 1 185 ? 11.095 -7.097  32.089 1.00 28.36  ? 182 ILE A CD1 1 
ATOM   1422 N  N   . LEU A 1 186 ? 14.461 -9.505  34.132 1.00 22.11  ? 183 LEU A N   1 
ATOM   1423 C  CA  . LEU A 1 186 ? 15.487 -8.757  34.846 1.00 24.93  ? 183 LEU A CA  1 
ATOM   1424 C  C   . LEU A 1 186 ? 15.549 -7.387  34.190 1.00 23.88  ? 183 LEU A C   1 
ATOM   1425 O  O   . LEU A 1 186 ? 15.792 -7.295  32.990 1.00 24.71  ? 183 LEU A O   1 
ATOM   1426 C  CB  . LEU A 1 186 ? 16.846 -9.450  34.755 1.00 25.58  ? 183 LEU A CB  1 
ATOM   1427 C  CG  . LEU A 1 186 ? 18.054 -8.608  35.193 1.00 25.90  ? 183 LEU A CG  1 
ATOM   1428 C  CD1 . LEU A 1 186 ? 17.932 -8.238  36.681 1.00 27.97  ? 183 LEU A CD1 1 
ATOM   1429 C  CD2 . LEU A 1 186 ? 19.328 -9.421  34.943 1.00 29.95  ? 183 LEU A CD2 1 
ATOM   1430 N  N   . VAL A 1 187 ? 15.278 -6.348  34.965 1.00 23.93  ? 184 VAL A N   1 
ATOM   1431 C  CA  . VAL A 1 187 ? 15.358 -4.955  34.533 1.00 25.95  ? 184 VAL A CA  1 
ATOM   1432 C  C   . VAL A 1 187 ? 16.676 -4.384  35.037 1.00 24.22  ? 184 VAL A C   1 
ATOM   1433 O  O   . VAL A 1 187 ? 16.906 -4.338  36.247 1.00 25.95  ? 184 VAL A O   1 
ATOM   1434 C  CB  . VAL A 1 187 ? 14.182 -4.143  35.095 1.00 27.04  ? 184 VAL A CB  1 
ATOM   1435 C  CG1 . VAL A 1 187 ? 14.258 -2.715  34.602 1.00 29.76  ? 184 VAL A CG1 1 
ATOM   1436 C  CG2 . VAL A 1 187 ? 12.872 -4.801  34.687 1.00 27.17  ? 184 VAL A CG2 1 
ATOM   1437 N  N   . ILE A 1 188 ? 17.537 -3.933  34.124 1.00 27.84  ? 185 ILE A N   1 
ATOM   1438 C  CA  . ILE A 1 188 ? 18.841 -3.365  34.474 1.00 27.21  ? 185 ILE A CA  1 
ATOM   1439 C  C   . ILE A 1 188 ? 18.841 -1.884  34.107 1.00 25.95  ? 185 ILE A C   1 
ATOM   1440 O  O   . ILE A 1 188 ? 18.390 -1.512  33.011 1.00 27.98  ? 185 ILE A O   1 
ATOM   1441 C  CB  . ILE A 1 188 ? 19.959 -4.126  33.732 1.00 25.71  ? 185 ILE A CB  1 
ATOM   1442 C  CG1 . ILE A 1 188 ? 20.257 -5.456  34.429 1.00 28.62  ? 185 ILE A CG1 1 
ATOM   1443 C  CG2 . ILE A 1 188 ? 21.235 -3.291  33.605 1.00 30.03  ? 185 ILE A CG2 1 
ATOM   1444 C  CD1 . ILE A 1 188 ? 20.921 -6.446  33.505 1.00 28.77  ? 185 ILE A CD1 1 
ATOM   1445 N  N   . GLN A 1 189 ? 19.355 -1.037  35.005 1.00 29.00  ? 186 GLN A N   1 
ATOM   1446 C  CA  . GLN A 1 189 ? 19.333 0.395   34.726 1.00 32.93  ? 186 GLN A CA  1 
ATOM   1447 C  C   . GLN A 1 189 ? 20.512 1.122   35.357 1.00 33.59  ? 186 GLN A C   1 
ATOM   1448 O  O   . GLN A 1 189 ? 20.816 0.925   36.534 1.00 34.02  ? 186 GLN A O   1 
ATOM   1449 C  CB  . GLN A 1 189 ? 18.031 1.030   35.214 1.00 29.95  ? 186 GLN A CB  1 
ATOM   1450 C  CG  . GLN A 1 189 ? 17.952 2.535   34.946 1.00 33.42  ? 186 GLN A CG  1 
ATOM   1451 C  CD  . GLN A 1 189 ? 17.984 2.875   33.464 1.00 32.99  ? 186 GLN A CD  1 
ATOM   1452 O  OE1 . GLN A 1 189 ? 17.212 2.326   32.674 1.00 32.49  ? 186 GLN A OE1 1 
ATOM   1453 N  NE2 . GLN A 1 189 ? 18.863 3.810   33.082 1.00 32.10  ? 186 GLN A NE2 1 
ATOM   1454 N  N   . ALA A 1 190 ? 21.145 1.997   34.580 1.00 34.01  ? 187 ALA A N   1 
ATOM   1455 C  CA  . ALA A 1 190 ? 22.163 2.879   35.124 1.00 36.47  ? 187 ALA A CA  1 
ATOM   1456 C  C   . ALA A 1 190 ? 21.499 4.049   35.837 1.00 38.60  ? 187 ALA A C   1 
ATOM   1457 O  O   . ALA A 1 190 ? 20.642 4.724   35.258 1.00 38.46  ? 187 ALA A O   1 
ATOM   1458 C  CB  . ALA A 1 190 ? 23.073 3.385   34.011 1.00 36.77  ? 187 ALA A CB  1 
ATOM   1459 N  N   . GLU A 1 191 ? 21.903 4.297   37.094 1.00 37.27  ? 188 GLU A N   1 
ATOM   1460 C  CA  . GLU A 1 191 ? 21.298 5.385   37.863 1.00 37.21  ? 188 GLU A CA  1 
ATOM   1461 C  C   . GLU A 1 191 ? 21.535 6.738   37.208 1.00 44.75  ? 188 GLU A C   1 
ATOM   1462 O  O   . GLU A 1 191 ? 20.637 7.589   37.189 1.00 47.78  ? 188 GLU A O   1 
ATOM   1463 C  CB  . GLU A 1 191 ? 21.836 5.406   39.295 1.00 43.12  ? 188 GLU A CB  1 
ATOM   1464 C  CG  . GLU A 1 191 ? 21.113 4.500   40.279 1.00 47.58  ? 188 GLU A CG  1 
ATOM   1465 C  CD  . GLU A 1 191 ? 21.854 4.383   41.613 1.00 47.22  ? 188 GLU A CD  1 
ATOM   1466 O  OE1 . GLU A 1 191 ? 21.962 3.256   42.148 1.00 58.03  ? 188 GLU A OE1 1 
ATOM   1467 O  OE2 . GLU A 1 191 ? 22.378 5.408   42.081 1.00 53.67  ? 188 GLU A OE2 1 
ATOM   1468 N  N   . ASN A 1 192 ? 22.730 6.958   36.672 1.00 42.91  ? 189 ASN A N   1 
ATOM   1469 C  CA  . ASN A 1 192 ? 23.117 8.241   36.081 1.00 44.84  ? 189 ASN A CA  1 
ATOM   1470 C  C   . ASN A 1 192 ? 23.087 8.190   34.560 1.00 47.36  ? 189 ASN A C   1 
ATOM   1471 O  O   . ASN A 1 192 ? 24.006 8.624   33.867 1.00 53.89  ? 189 ASN A O   1 
ATOM   1472 C  CB  . ASN A 1 192 ? 24.484 8.653   36.596 1.00 48.59  ? 189 ASN A CB  1 
ATOM   1473 C  CG  . ASN A 1 192 ? 24.539 8.651   38.102 1.00 52.10  ? 189 ASN A CG  1 
ATOM   1474 O  OD1 . ASN A 1 192 ? 23.937 9.510   38.744 1.00 56.46  ? 189 ASN A OD1 1 
ATOM   1475 N  ND2 . ASN A 1 192 ? 25.217 7.667   38.678 1.00 51.24  ? 189 ASN A ND2 1 
ATOM   1476 N  N   . ASP A 1 193 ? 21.994 7.646   34.045 1.00 45.57  ? 190 ASP A N   1 
ATOM   1477 C  CA  . ASP A 1 193 ? 21.754 7.579   32.613 1.00 46.94  ? 190 ASP A CA  1 
ATOM   1478 C  C   . ASP A 1 193 ? 21.486 8.975   32.067 1.00 48.15  ? 190 ASP A C   1 
ATOM   1479 O  O   . ASP A 1 193 ? 20.541 9.643   32.496 1.00 50.25  ? 190 ASP A O   1 
ATOM   1480 C  CB  . ASP A 1 193 ? 20.566 6.661   32.347 1.00 38.86  ? 190 ASP A CB  1 
ATOM   1481 C  CG  . ASP A 1 193 ? 20.493 6.206   30.915 1.00 44.02  ? 190 ASP A CG  1 
ATOM   1482 O  OD1 . ASP A 1 193 ? 20.598 7.058   30.000 1.00 42.48  ? 190 ASP A OD1 1 
ATOM   1483 O  OD2 . ASP A 1 193 ? 20.330 4.987   30.707 1.00 38.10  ? 190 ASP A OD2 1 
ATOM   1484 N  N   . ASN A 1 194 ? 22.308 9.417   31.116 1.00 46.88  ? 191 ASN A N   1 
ATOM   1485 C  CA  . ASN A 1 194 ? 22.130 10.723  30.501 1.00 48.65  ? 191 ASN A CA  1 
ATOM   1486 C  C   . ASN A 1 194 ? 21.475 10.645  29.132 1.00 46.74  ? 191 ASN A C   1 
ATOM   1487 O  O   . ASN A 1 194 ? 21.454 11.642  28.409 1.00 48.92  ? 191 ASN A O   1 
ATOM   1488 C  CB  . ASN A 1 194 ? 23.468 11.456  30.392 1.00 53.13  ? 191 ASN A CB  1 
ATOM   1489 C  CG  . ASN A 1 194 ? 24.032 11.831  31.748 1.00 58.72  ? 191 ASN A CG  1 
ATOM   1490 O  OD1 . ASN A 1 194 ? 23.375 12.513  32.538 1.00 62.23  ? 191 ASN A OD1 1 
ATOM   1491 N  ND2 . ASN A 1 194 ? 25.264 11.412  32.015 1.00 65.54  ? 191 ASN A ND2 1 
ATOM   1492 N  N   . MET A 1 195 ? 20.924 9.497   28.766 1.00 44.66  ? 192 MET A N   1 
ATOM   1493 C  CA  . MET A 1 195 ? 20.279 9.360   27.469 1.00 45.64  ? 192 MET A CA  1 
ATOM   1494 C  C   . MET A 1 195 ? 18.773 9.172   27.585 1.00 45.48  ? 192 MET A C   1 
ATOM   1495 O  O   . MET A 1 195 ? 18.021 9.739   26.786 1.00 45.63  ? 192 MET A O   1 
ATOM   1496 C  CB  . MET A 1 195 ? 20.903 8.184   26.708 1.00 42.76  ? 192 MET A CB  1 
ATOM   1497 C  CG  . MET A 1 195 ? 20.318 7.916   25.337 1.00 47.18  ? 192 MET A CG  1 
ATOM   1498 S  SD  . MET A 1 195 ? 20.723 9.211   24.143 1.00 54.90  ? 192 MET A SD  1 
ATOM   1499 C  CE  . MET A 1 195 ? 22.419 9.626   24.557 1.00 52.11  ? 192 MET A CE  1 
ATOM   1500 N  N   . ILE A 1 196 ? 18.317 8.433   28.600 1.00 39.53  ? 193 ILE A N   1 
ATOM   1501 C  CA  . ILE A 1 196 ? 16.904 8.197   28.870 1.00 38.54  ? 193 ILE A CA  1 
ATOM   1502 C  C   . ILE A 1 196 ? 16.614 8.566   30.324 1.00 44.04  ? 193 ILE A C   1 
ATOM   1503 O  O   . ILE A 1 196 ? 17.516 8.878   31.106 1.00 41.56  ? 193 ILE A O   1 
ATOM   1504 C  CB  . ILE A 1 196 ? 16.496 6.732   28.594 1.00 40.34  ? 193 ILE A CB  1 
ATOM   1505 C  CG1 . ILE A 1 196 ? 17.170 5.790   29.592 1.00 39.60  ? 193 ILE A CG1 1 
ATOM   1506 C  CG2 . ILE A 1 196 ? 16.862 6.318   27.185 1.00 40.45  ? 193 ILE A CG2 1 
ATOM   1507 C  CD1 . ILE A 1 196 ? 16.368 4.525   29.899 1.00 33.48  ? 193 ILE A CD1 1 
ATOM   1508 N  N   . ASP A 1 197 ? 15.333 8.544   30.675 1.00 38.13  ? 194 ASP A N   1 
ATOM   1509 C  CA  . ASP A 1 197 ? 14.937 8.761   32.058 1.00 42.84  ? 194 ASP A CA  1 
ATOM   1510 C  C   . ASP A 1 197 ? 15.108 7.453   32.815 1.00 38.55  ? 194 ASP A C   1 
ATOM   1511 O  O   . ASP A 1 197 ? 14.453 6.462   32.468 1.00 38.03  ? 194 ASP A O   1 
ATOM   1512 C  CB  . ASP A 1 197 ? 13.495 9.243   32.135 1.00 41.96  ? 194 ASP A CB  1 
ATOM   1513 C  CG  . ASP A 1 197 ? 13.016 9.471   33.560 1.00 48.64  ? 194 ASP A CG  1 
ATOM   1514 O  OD1 . ASP A 1 197 ? 13.804 9.329   34.529 1.00 43.48  ? 194 ASP A OD1 1 
ATOM   1515 O  OD2 . ASP A 1 197 ? 11.841 9.860   33.709 1.00 56.37  ? 194 ASP A OD2 1 
ATOM   1516 N  N   . PRO A 1 198 ? 15.991 7.389   33.813 1.00 38.93  ? 195 PRO A N   1 
ATOM   1517 C  CA  . PRO A 1 198 ? 16.178 6.124   34.544 1.00 36.85  ? 195 PRO A CA  1 
ATOM   1518 C  C   . PRO A 1 198 ? 14.917 5.634   35.233 1.00 38.62  ? 195 PRO A C   1 
ATOM   1519 O  O   . PRO A 1 198 ? 14.815 4.437   35.517 1.00 35.45  ? 195 PRO A O   1 
ATOM   1520 C  CB  . PRO A 1 198 ? 17.268 6.451   35.576 1.00 44.25  ? 195 PRO A CB  1 
ATOM   1521 C  CG  . PRO A 1 198 ? 17.762 7.811   35.277 1.00 46.37  ? 195 PRO A CG  1 
ATOM   1522 C  CD  . PRO A 1 198 ? 16.972 8.426   34.174 1.00 42.64  ? 195 PRO A CD  1 
ATOM   1523 N  N   . GLN A 1 199 ? 13.953 6.515   35.512 1.00 35.70  ? 196 GLN A N   1 
ATOM   1524 C  CA  . GLN A 1 199 ? 12.692 6.057   36.083 1.00 38.63  ? 196 GLN A CA  1 
ATOM   1525 C  C   . GLN A 1 199 ? 11.964 5.085   35.164 1.00 34.96  ? 196 GLN A C   1 
ATOM   1526 O  O   . GLN A 1 199 ? 11.040 4.401   35.619 1.00 39.20  ? 196 GLN A O   1 
ATOM   1527 C  CB  . GLN A 1 199 ? 11.788 7.250   36.387 1.00 39.50  ? 196 GLN A CB  1 
ATOM   1528 C  CG  . GLN A 1 199 ? 12.143 7.927   37.686 1.00 49.30  ? 196 GLN A CG  1 
ATOM   1529 C  CD  . GLN A 1 199 ? 12.164 6.941   38.832 1.00 52.99  ? 196 GLN A CD  1 
ATOM   1530 O  OE1 . GLN A 1 199 ? 11.153 6.305   39.140 1.00 51.00  ? 196 GLN A OE1 1 
ATOM   1531 N  NE2 . GLN A 1 199 ? 13.334 6.782   39.452 1.00 57.08  ? 196 GLN A NE2 1 
ATOM   1532 N  N   . SER A 1 200 ? 12.349 5.022   33.884 1.00 34.63  ? 197 SER A N   1 
ATOM   1533 C  CA  . SER A 1 200 ? 11.801 4.016   32.973 1.00 31.61  ? 197 SER A CA  1 
ATOM   1534 C  C   . SER A 1 200 ? 11.906 2.619   33.558 1.00 31.35  ? 197 SER A C   1 
ATOM   1535 O  O   . SER A 1 200 ? 11.035 1.772   33.315 1.00 31.46  ? 197 SER A O   1 
ATOM   1536 C  CB  . SER A 1 200 ? 12.538 4.045   31.630 1.00 30.59  ? 197 SER A CB  1 
ATOM   1537 O  OG  . SER A 1 200 ? 12.396 5.292   30.975 1.00 35.46  ? 197 SER A OG  1 
ATOM   1538 N  N   . ALA A 1 201 ? 12.977 2.346   34.307 1.00 31.49  ? 198 ALA A N   1 
ATOM   1539 C  CA  . ALA A 1 201 ? 13.156 0.997   34.843 1.00 29.93  ? 198 ALA A CA  1 
ATOM   1540 C  C   . ALA A 1 201 ? 12.098 0.681   35.887 1.00 31.77  ? 198 ALA A C   1 
ATOM   1541 O  O   . ALA A 1 201 ? 11.603 -0.452  35.954 1.00 29.27  ? 198 ALA A O   1 
ATOM   1542 C  CB  . ALA A 1 201 ? 14.549 0.840   35.446 1.00 28.06  ? 198 ALA A CB  1 
ATOM   1543 N  N   . ASN A 1 202 ? 11.757 1.662   36.727 1.00 31.51  ? 199 ASN A N   1 
ATOM   1544 C  CA  . ASN A 1 202 ? 10.702 1.442   37.710 1.00 34.40  ? 199 ASN A CA  1 
ATOM   1545 C  C   . ASN A 1 202 ? 9.372  1.197   37.016 1.00 33.44  ? 199 ASN A C   1 
ATOM   1546 O  O   . ASN A 1 202 ? 8.576  0.367   37.465 1.00 31.56  ? 199 ASN A O   1 
ATOM   1547 C  CB  . ASN A 1 202 ? 10.595 2.635   38.654 1.00 35.17  ? 199 ASN A CB  1 
ATOM   1548 C  CG  . ASN A 1 202 ? 11.636 2.604   39.726 1.00 41.14  ? 199 ASN A CG  1 
ATOM   1549 O  OD1 . ASN A 1 202 ? 11.914 1.554   40.309 1.00 41.06  ? 199 ASN A OD1 1 
ATOM   1550 N  ND2 . ASN A 1 202 ? 12.232 3.757   39.997 1.00 43.27  ? 199 ASN A ND2 1 
ATOM   1551 N  N   . TYR A 1 203 ? 9.123  1.911   35.912 1.00 30.10  ? 200 TYR A N   1 
ATOM   1552 C  CA  . TYR A 1 203 ? 7.894  1.719   35.146 1.00 34.41  ? 200 TYR A CA  1 
ATOM   1553 C  C   . TYR A 1 203 ? 7.794  0.294   34.608 1.00 34.06  ? 200 TYR A C   1 
ATOM   1554 O  O   . TYR A 1 203 ? 6.768  -0.373  34.774 1.00 31.90  ? 200 TYR A O   1 
ATOM   1555 C  CB  . TYR A 1 203 ? 7.823  2.722   33.989 1.00 35.17  ? 200 TYR A CB  1 
ATOM   1556 C  CG  . TYR A 1 203 ? 6.459  2.725   33.331 1.00 36.58  ? 200 TYR A CG  1 
ATOM   1557 C  CD1 . TYR A 1 203 ? 6.147  1.837   32.304 1.00 37.54  ? 200 TYR A CD1 1 
ATOM   1558 C  CD2 . TYR A 1 203 ? 5.471  3.584   33.771 1.00 40.93  ? 200 TYR A CD2 1 
ATOM   1559 C  CE1 . TYR A 1 203 ? 4.886  1.828   31.726 1.00 39.77  ? 200 TYR A CE1 1 
ATOM   1560 C  CE2 . TYR A 1 203 ? 4.212  3.585   33.206 1.00 40.12  ? 200 TYR A CE2 1 
ATOM   1561 C  CZ  . TYR A 1 203 ? 3.919  2.710   32.195 1.00 43.60  ? 200 TYR A CZ  1 
ATOM   1562 O  OH  . TYR A 1 203 ? 2.660  2.733   31.645 1.00 49.07  ? 200 TYR A OH  1 
ATOM   1563 N  N   . ILE A 1 204 ? 8.846  -0.180  33.939 1.00 29.24  ? 201 ILE A N   1 
ATOM   1564 C  CA  . ILE A 1 204 ? 8.848  -1.555  33.437 1.00 28.65  ? 201 ILE A CA  1 
ATOM   1565 C  C   . ILE A 1 204 ? 8.622  -2.535  34.584 1.00 26.04  ? 201 ILE A C   1 
ATOM   1566 O  O   . ILE A 1 204 ? 7.750  -3.411  34.519 1.00 28.32  ? 201 ILE A O   1 
ATOM   1567 C  CB  . ILE A 1 204 ? 10.166 -1.858  32.705 1.00 26.43  ? 201 ILE A CB  1 
ATOM   1568 C  CG1 . ILE A 1 204 ? 10.323 -0.956  31.470 1.00 31.37  ? 201 ILE A CG1 1 
ATOM   1569 C  CG2 . ILE A 1 204 ? 10.228 -3.351  32.319 1.00 28.06  ? 201 ILE A CG2 1 
ATOM   1570 C  CD1 . ILE A 1 204 ? 11.681 -1.014  30.823 1.00 29.94  ? 201 ILE A CD1 1 
ATOM   1571 N  N   . TYR A 1 205 ? 9.419  -2.407  35.644 1.00 26.92  ? 202 TYR A N   1 
ATOM   1572 C  CA  . TYR A 1 205 ? 9.353  -3.353  36.756 1.00 27.28  ? 202 TYR A CA  1 
ATOM   1573 C  C   . TYR A 1 205 ? 7.955  -3.412  37.352 1.00 31.50  ? 202 TYR A C   1 
ATOM   1574 O  O   . TYR A 1 205 ? 7.462  -4.494  37.709 1.00 30.70  ? 202 TYR A O   1 
ATOM   1575 C  CB  . TYR A 1 205 ? 10.371 -2.941  37.815 1.00 27.77  ? 202 TYR A CB  1 
ATOM   1576 C  CG  . TYR A 1 205 ? 10.463 -3.847  39.015 1.00 27.35  ? 202 TYR A CG  1 
ATOM   1577 C  CD1 . TYR A 1 205 ? 11.091 -5.077  38.925 1.00 28.20  ? 202 TYR A CD1 1 
ATOM   1578 C  CD2 . TYR A 1 205 ? 9.939  -3.461  40.237 1.00 32.34  ? 202 TYR A CD2 1 
ATOM   1579 C  CE1 . TYR A 1 205 ? 11.193 -5.913  40.023 1.00 28.35  ? 202 TYR A CE1 1 
ATOM   1580 C  CE2 . TYR A 1 205 ? 10.038 -4.278  41.352 1.00 32.44  ? 202 TYR A CE2 1 
ATOM   1581 C  CZ  . TYR A 1 205 ? 10.667 -5.516  41.232 1.00 28.40  ? 202 TYR A CZ  1 
ATOM   1582 O  OH  . TYR A 1 205 ? 10.776 -6.332  42.348 1.00 30.74  ? 202 TYR A OH  1 
ATOM   1583 N  N   . ASP A 1 206 ? 7.299  -2.258  37.468 1.00 28.50  ? 203 ASP A N   1 
ATOM   1584 C  CA  . ASP A 1 206 ? 6.015  -2.198  38.149 1.00 30.37  ? 203 ASP A CA  1 
ATOM   1585 C  C   . ASP A 1 206 ? 4.833  -2.503  37.247 1.00 32.70  ? 203 ASP A C   1 
ATOM   1586 O  O   . ASP A 1 206 ? 3.758  -2.845  37.764 1.00 33.87  ? 203 ASP A O   1 
ATOM   1587 C  CB  . ASP A 1 206 ? 5.810  -0.825  38.779 1.00 33.15  ? 203 ASP A CB  1 
ATOM   1588 C  CG  . ASP A 1 206 ? 6.659  -0.616  40.024 1.00 36.67  ? 203 ASP A CG  1 
ATOM   1589 O  OD1 . ASP A 1 206 ? 7.110  -1.612  40.654 1.00 34.72  ? 203 ASP A OD1 1 
ATOM   1590 O  OD2 . ASP A 1 206 ? 6.860  0.555   40.386 1.00 39.28  ? 203 ASP A OD2 1 
ATOM   1591 N  N   . HIS A 1 207 ? 4.993  -2.385  35.930 1.00 30.80  ? 204 HIS A N   1 
ATOM   1592 C  CA  . HIS A 1 207 ? 3.869  -2.521  35.013 1.00 30.63  ? 204 HIS A CA  1 
ATOM   1593 C  C   . HIS A 1 207 ? 3.840  -3.828  34.236 1.00 29.88  ? 204 HIS A C   1 
ATOM   1594 O  O   . HIS A 1 207 ? 2.767  -4.202  33.744 1.00 29.62  ? 204 HIS A O   1 
ATOM   1595 C  CB  . HIS A 1 207 ? 3.838  -1.340  34.034 1.00 32.48  ? 204 HIS A CB  1 
ATOM   1596 C  CG  . HIS A 1 207 ? 3.338  -0.078  34.663 1.00 37.35  ? 204 HIS A CG  1 
ATOM   1597 N  ND1 . HIS A 1 207 ? 4.071  0.626   35.593 1.00 41.14  ? 204 HIS A ND1 1 
ATOM   1598 C  CD2 . HIS A 1 207 ? 2.149  0.561   34.558 1.00 43.97  ? 204 HIS A CD2 1 
ATOM   1599 C  CE1 . HIS A 1 207 ? 3.362  1.657   36.021 1.00 45.13  ? 204 HIS A CE1 1 
ATOM   1600 N  NE2 . HIS A 1 207 ? 2.194  1.643   35.405 1.00 45.68  ? 204 HIS A NE2 1 
ATOM   1601 N  N   . VAL A 1 208 ? 4.960  -4.541  34.113 1.00 28.45  ? 205 VAL A N   1 
ATOM   1602 C  CA  . VAL A 1 208 ? 4.876  -5.876  33.523 1.00 27.56  ? 205 VAL A CA  1 
ATOM   1603 C  C   . VAL A 1 208 ? 3.996  -6.759  34.401 1.00 29.12  ? 205 VAL A C   1 
ATOM   1604 O  O   . VAL A 1 208 ? 3.878  -6.557  35.619 1.00 28.45  ? 205 VAL A O   1 
ATOM   1605 C  CB  . VAL A 1 208 ? 6.255  -6.527  33.337 1.00 26.50  ? 205 VAL A CB  1 
ATOM   1606 C  CG1 . VAL A 1 208 ? 7.090  -5.746  32.316 1.00 30.03  ? 205 VAL A CG1 1 
ATOM   1607 C  CG2 . VAL A 1 208 ? 6.957  -6.687  34.694 1.00 28.61  ? 205 VAL A CG2 1 
ATOM   1608 N  N   . ASP A 1 209 ? 3.368  -7.754  33.781 1.00 28.75  ? 206 ASP A N   1 
ATOM   1609 C  CA  . ASP A 1 209 ? 2.567  -8.707  34.531 1.00 28.35  ? 206 ASP A CA  1 
ATOM   1610 C  C   . ASP A 1 209 ? 3.335  -9.989  34.843 1.00 29.39  ? 206 ASP A C   1 
ATOM   1611 O  O   . ASP A 1 209 ? 2.727  -11.007 35.190 1.00 30.04  ? 206 ASP A O   1 
ATOM   1612 C  CB  . ASP A 1 209 ? 1.267  -9.014  33.782 1.00 29.94  ? 206 ASP A CB  1 
ATOM   1613 C  CG  . ASP A 1 209 ? 0.191  -9.578  34.707 1.00 37.01  ? 206 ASP A CG  1 
ATOM   1614 O  OD1 . ASP A 1 209 ? 0.333  -9.444  35.952 1.00 42.18  ? 206 ASP A OD1 1 
ATOM   1615 O  OD2 . ASP A 1 209 ? -0.794 -10.144 34.200 1.00 42.78  ? 206 ASP A OD2 1 
ATOM   1616 N  N   . SER A 1 210 ? 4.661  -9.955  34.751 1.00 24.39  ? 207 SER A N   1 
ATOM   1617 C  CA  . SER A 1 210 ? 5.460  -11.131 35.091 1.00 27.19  ? 207 SER A CA  1 
ATOM   1618 C  C   . SER A 1 210 ? 5.295  -11.531 36.549 1.00 29.36  ? 207 SER A C   1 
ATOM   1619 O  O   . SER A 1 210 ? 5.119  -10.686 37.436 1.00 28.78  ? 207 SER A O   1 
ATOM   1620 C  CB  . SER A 1 210 ? 6.937  -10.875 34.803 1.00 25.96  ? 207 SER A CB  1 
ATOM   1621 O  OG  . SER A 1 210 ? 7.064  -10.306 33.497 1.00 30.63  ? 207 SER A OG  1 
ATOM   1622 N  N   . ASP A 1 211 ? 5.363  -12.852 36.784 1.00 26.04  ? 208 ASP A N   1 
ATOM   1623 C  CA  . ASP A 1 211 ? 5.321  -13.432 38.121 1.00 26.79  ? 208 ASP A CA  1 
ATOM   1624 C  C   . ASP A 1 211 ? 6.705  -13.571 38.729 1.00 24.76  ? 208 ASP A C   1 
ATOM   1625 O  O   . ASP A 1 211 ? 6.821  -14.038 39.855 1.00 27.42  ? 208 ASP A O   1 
ATOM   1626 C  CB  . ASP A 1 211 ? 4.671  -14.820 38.106 1.00 27.28  ? 208 ASP A CB  1 
ATOM   1627 C  CG  . ASP A 1 211 ? 3.174  -14.773 37.995 1.00 33.02  ? 208 ASP A CG  1 
ATOM   1628 O  OD1 . ASP A 1 211 ? 2.571  -13.687 38.166 1.00 33.50  ? 208 ASP A OD1 1 
ATOM   1629 O  OD2 . ASP A 1 211 ? 2.593  -15.858 37.778 1.00 38.85  ? 208 ASP A OD2 1 
ATOM   1630 N  N   . ASP A 1 212 ? 7.747  -13.186 38.010 1.00 25.16  ? 209 ASP A N   1 
ATOM   1631 C  CA  . ASP A 1 212 ? 9.124  -13.412 38.445 1.00 30.94  ? 209 ASP A CA  1 
ATOM   1632 C  C   . ASP A 1 212 ? 9.934  -12.222 37.956 1.00 24.99  ? 209 ASP A C   1 
ATOM   1633 O  O   . ASP A 1 212 ? 10.192 -12.112 36.757 1.00 27.26  ? 209 ASP A O   1 
ATOM   1634 C  CB  . ASP A 1 212 ? 9.640  -14.733 37.869 1.00 30.36  ? 209 ASP A CB  1 
ATOM   1635 C  CG  . ASP A 1 212 ? 11.056 -15.062 38.285 1.00 36.08  ? 209 ASP A CG  1 
ATOM   1636 O  OD1 . ASP A 1 212 ? 11.680 -14.279 39.027 1.00 33.48  ? 209 ASP A OD1 1 
ATOM   1637 O  OD2 . ASP A 1 212 ? 11.559 -16.130 37.837 1.00 41.88  ? 209 ASP A OD2 1 
ATOM   1638 N  N   . LYS A 1 213 ? 10.313 -11.316 38.857 1.00 25.66  ? 210 LYS A N   1 
ATOM   1639 C  CA  . LYS A 1 213 ? 10.980 -10.129 38.354 1.00 28.36  ? 210 LYS A CA  1 
ATOM   1640 C  C   . LYS A 1 213 ? 11.990 -9.586  39.348 1.00 27.05  ? 210 LYS A C   1 
ATOM   1641 O  O   . LYS A 1 213 ? 11.863 -9.756  40.558 1.00 27.46  ? 210 LYS A O   1 
ATOM   1642 C  CB  . LYS A 1 213 ? 9.977  -9.038  37.957 1.00 30.84  ? 210 LYS A CB  1 
ATOM   1643 C  CG  . LYS A 1 213 ? 8.903  -8.715  38.931 1.00 37.08  ? 210 LYS A CG  1 
ATOM   1644 C  CD  . LYS A 1 213 ? 7.876  -7.743  38.313 1.00 30.78  ? 210 LYS A CD  1 
ATOM   1645 C  CE  . LYS A 1 213 ? 6.918  -7.279  39.420 1.00 32.42  ? 210 LYS A CE  1 
ATOM   1646 N  NZ  . LYS A 1 213 ? 5.883  -6.339  38.921 1.00 33.69  ? 210 LYS A NZ  1 
ATOM   1647 N  N   A ASN A 1 214 ? 12.946 -8.839  38.803 0.59 27.13  ? 211 ASN A N   1 
ATOM   1648 N  N   B ASN A 1 214 ? 13.044 -8.986  38.826 0.41 27.36  ? 211 ASN A N   1 
ATOM   1649 C  CA  A ASN A 1 214 ? 14.120 -8.395  39.543 0.59 30.41  ? 211 ASN A CA  1 
ATOM   1650 C  CA  B ASN A 1 214 ? 13.958 -8.277  39.706 0.41 29.91  ? 211 ASN A CA  1 
ATOM   1651 C  C   A ASN A 1 214 ? 14.550 -7.089  38.893 0.59 28.69  ? 211 ASN A C   1 
ATOM   1652 C  C   B ASN A 1 214 ? 14.535 -7.104  38.941 0.41 28.67  ? 211 ASN A C   1 
ATOM   1653 O  O   A ASN A 1 214 ? 14.492 -6.971  37.667 0.59 26.34  ? 211 ASN A O   1 
ATOM   1654 O  O   B ASN A 1 214 ? 14.569 -7.096  37.709 0.41 26.49  ? 211 ASN A O   1 
ATOM   1655 C  CB  A ASN A 1 214 ? 15.234 -9.444  39.435 0.59 31.48  ? 211 ASN A CB  1 
ATOM   1656 C  CB  B ASN A 1 214 ? 15.087 -9.162  40.274 0.41 29.93  ? 211 ASN A CB  1 
ATOM   1657 C  CG  A ASN A 1 214 ? 16.359 -9.257  40.425 0.59 35.41  ? 211 ASN A CG  1 
ATOM   1658 C  CG  B ASN A 1 214 ? 15.477 -10.287 39.351 0.41 32.63  ? 211 ASN A CG  1 
ATOM   1659 O  OD1 A ASN A 1 214 ? 17.417 -9.854  40.250 0.59 38.16  ? 211 ASN A OD1 1 
ATOM   1660 O  OD1 B ASN A 1 214 ? 15.536 -11.450 39.759 0.41 40.49  ? 211 ASN A OD1 1 
ATOM   1661 N  ND2 A ASN A 1 214 ? 16.122 -8.493  41.509 0.59 33.60  ? 211 ASN A ND2 1 
ATOM   1662 N  ND2 B ASN A 1 214 ? 15.720 -9.961  38.103 0.41 29.37  ? 211 ASN A ND2 1 
ATOM   1663 N  N   . ILE A 1 215 ? 14.943 -6.097  39.693 1.00 29.12  ? 212 ILE A N   1 
ATOM   1664 C  CA  . ILE A 1 215 ? 15.477 -4.856  39.142 1.00 30.23  ? 212 ILE A CA  1 
ATOM   1665 C  C   . ILE A 1 215 ? 16.818 -4.584  39.809 1.00 28.33  ? 212 ILE A C   1 
ATOM   1666 O  O   . ILE A 1 215 ? 16.977 -4.795  41.016 1.00 30.66  ? 212 ILE A O   1 
ATOM   1667 C  CB  . ILE A 1 215 ? 14.497 -3.678  39.338 1.00 29.52  ? 212 ILE A CB  1 
ATOM   1668 C  CG1 . ILE A 1 215 ? 15.040 -2.406  38.672 1.00 31.22  ? 212 ILE A CG1 1 
ATOM   1669 C  CG2 . ILE A 1 215 ? 14.145 -3.494  40.807 1.00 30.62  ? 212 ILE A CG2 1 
ATOM   1670 C  CD1 . ILE A 1 215 ? 14.011 -1.305  38.570 1.00 32.25  ? 212 ILE A CD1 1 
ATOM   1671 N  N   . LYS A 1 216 ? 17.790 -4.156  39.005 1.00 27.91  ? 213 LYS A N   1 
ATOM   1672 C  CA  . LYS A 1 216 ? 19.154 -3.926  39.455 1.00 32.32  ? 213 LYS A CA  1 
ATOM   1673 C  C   . LYS A 1 216 ? 19.576 -2.551  38.971 1.00 27.65  ? 213 LYS A C   1 
ATOM   1674 O  O   . LYS A 1 216 ? 19.393 -2.226  37.789 1.00 29.52  ? 213 LYS A O   1 
ATOM   1675 C  CB  . LYS A 1 216 ? 20.126 -4.982  38.900 1.00 33.73  ? 213 LYS A CB  1 
ATOM   1676 C  CG  . LYS A 1 216 ? 19.934 -6.401  39.433 1.00 35.42  ? 213 LYS A CG  1 
ATOM   1677 C  CD  . LYS A 1 216 ? 20.095 -6.469  40.910 1.00 43.53  ? 213 LYS A CD  1 
ATOM   1678 C  CE  . LYS A 1 216 ? 20.906 -7.692  41.323 1.00 53.79  ? 213 LYS A CE  1 
ATOM   1679 N  NZ  . LYS A 1 216 ? 20.367 -8.939  40.703 1.00 50.31  ? 213 LYS A NZ  1 
ATOM   1680 N  N   . TRP A 1 217 ? 20.162 -1.773  39.875 1.00 31.72  ? 214 TRP A N   1 
ATOM   1681 C  CA  . TRP A 1 217 ? 20.636 -0.430  39.610 1.00 32.28  ? 214 TRP A CA  1 
ATOM   1682 C  C   . TRP A 1 217 ? 22.151 -0.401  39.703 1.00 35.78  ? 214 TRP A C   1 
ATOM   1683 O  O   . TRP A 1 217 ? 22.742 -1.035  40.585 1.00 34.52  ? 214 TRP A O   1 
ATOM   1684 C  CB  . TRP A 1 217 ? 20.058 0.573   40.615 1.00 36.59  ? 214 TRP A CB  1 
ATOM   1685 C  CG  . TRP A 1 217 ? 18.572 0.662   40.592 1.00 38.76  ? 214 TRP A CG  1 
ATOM   1686 C  CD1 . TRP A 1 217 ? 17.683 -0.057  41.345 1.00 39.00  ? 214 TRP A CD1 1 
ATOM   1687 C  CD2 . TRP A 1 217 ? 17.791 1.519   39.754 1.00 36.53  ? 214 TRP A CD2 1 
ATOM   1688 N  NE1 . TRP A 1 217 ? 16.393 0.319   41.040 1.00 38.15  ? 214 TRP A NE1 1 
ATOM   1689 C  CE2 . TRP A 1 217 ? 16.434 1.285   40.063 1.00 38.69  ? 214 TRP A CE2 1 
ATOM   1690 C  CE3 . TRP A 1 217 ? 18.111 2.482   38.785 1.00 33.34  ? 214 TRP A CE3 1 
ATOM   1691 C  CZ2 . TRP A 1 217 ? 15.396 1.971   39.434 1.00 42.18  ? 214 TRP A CZ2 1 
ATOM   1692 C  CZ3 . TRP A 1 217 ? 17.081 3.171   38.168 1.00 36.93  ? 214 TRP A CZ3 1 
ATOM   1693 C  CH2 . TRP A 1 217 ? 15.737 2.903   38.485 1.00 39.09  ? 214 TRP A CH2 1 
ATOM   1694 N  N   . TYR A 1 218 ? 22.769 0.382   38.827 1.00 33.69  ? 215 TYR A N   1 
ATOM   1695 C  CA  . TYR A 1 218 ? 24.218 0.505   38.785 1.00 36.46  ? 215 TYR A CA  1 
ATOM   1696 C  C   . TYR A 1 218 ? 24.562 1.981   38.861 1.00 39.25  ? 215 TYR A C   1 
ATOM   1697 O  O   . TYR A 1 218 ? 24.026 2.784   38.092 1.00 38.93  ? 215 TYR A O   1 
ATOM   1698 C  CB  . TYR A 1 218 ? 24.765 -0.166  37.522 1.00 36.93  ? 215 TYR A CB  1 
ATOM   1699 C  CG  . TYR A 1 218 ? 24.335 -1.613  37.436 1.00 32.34  ? 215 TYR A CG  1 
ATOM   1700 C  CD1 . TYR A 1 218 ? 23.091 -1.959  36.929 1.00 32.13  ? 215 TYR A CD1 1 
ATOM   1701 C  CD2 . TYR A 1 218 ? 25.156 -2.632  37.894 1.00 38.27  ? 215 TYR A CD2 1 
ATOM   1702 C  CE1 . TYR A 1 218 ? 22.682 -3.261  36.880 1.00 33.21  ? 215 TYR A CE1 1 
ATOM   1703 C  CE2 . TYR A 1 218 ? 24.748 -3.961  37.837 1.00 33.14  ? 215 TYR A CE2 1 
ATOM   1704 C  CZ  . TYR A 1 218 ? 23.517 -4.263  37.330 1.00 34.09  ? 215 TYR A CZ  1 
ATOM   1705 O  OH  . TYR A 1 218 ? 23.101 -5.570  37.243 1.00 36.68  ? 215 TYR A OH  1 
ATOM   1706 N  N   . SER A 1 219 ? 25.422 2.339   39.815 1.00 39.39  ? 216 SER A N   1 
ATOM   1707 C  CA  . SER A 1 219 ? 25.606 3.729   40.200 1.00 45.39  ? 216 SER A CA  1 
ATOM   1708 C  C   . SER A 1 219 ? 26.801 4.383   39.528 1.00 47.86  ? 216 SER A C   1 
ATOM   1709 O  O   . SER A 1 219 ? 27.005 5.582   39.713 1.00 47.53  ? 216 SER A O   1 
ATOM   1710 C  CB  . SER A 1 219 ? 25.738 3.849   41.730 1.00 47.84  ? 216 SER A CB  1 
ATOM   1711 O  OG  . SER A 1 219 ? 26.786 3.036   42.227 1.00 54.41  ? 216 SER A OG  1 
ATOM   1712 N  N   . GLU A 1 220 ? 27.586 3.642   38.739 1.00 45.27  ? 217 GLU A N   1 
ATOM   1713 C  CA  . GLU A 1 220 ? 28.764 4.219   38.103 1.00 45.28  ? 217 GLU A CA  1 
ATOM   1714 C  C   . GLU A 1 220 ? 28.801 3.969   36.598 1.00 44.71  ? 217 GLU A C   1 
ATOM   1715 O  O   . GLU A 1 220 ? 29.857 4.119   35.987 1.00 53.09  ? 217 GLU A O   1 
ATOM   1716 C  CB  . GLU A 1 220 ? 30.040 3.682   38.749 1.00 49.12  ? 217 GLU A CB  1 
ATOM   1717 C  CG  . GLU A 1 220 ? 30.026 3.799   40.264 1.00 57.22  ? 217 GLU A CG  1 
ATOM   1718 C  CD  . GLU A 1 220 ? 31.089 2.953   40.930 1.00 73.64  ? 217 GLU A CD  1 
ATOM   1719 O  OE1 . GLU A 1 220 ? 30.779 2.305   41.957 1.00 80.49  ? 217 GLU A OE1 1 
ATOM   1720 O  OE2 . GLU A 1 220 ? 32.243 2.966   40.449 1.00 80.03  ? 217 GLU A OE2 1 
ATOM   1721 N  N   . SER A 1 221 ? 27.687 3.592   35.983 1.00 44.67  ? 218 SER A N   1 
ATOM   1722 C  CA  . SER A 1 221 ? 27.654 3.373   34.541 1.00 42.84  ? 218 SER A CA  1 
ATOM   1723 C  C   . SER A 1 221 ? 26.853 4.449   33.827 1.00 43.61  ? 218 SER A C   1 
ATOM   1724 O  O   . SER A 1 221 ? 25.956 5.073   34.403 1.00 43.02  ? 218 SER A O   1 
ATOM   1725 C  CB  . SER A 1 221 ? 27.043 2.020   34.167 1.00 42.08  ? 218 SER A CB  1 
ATOM   1726 O  OG  . SER A 1 221 ? 27.507 0.984   34.997 1.00 46.79  ? 218 SER A OG  1 
ATOM   1727 N  N   . GLY A 1 222 ? 27.183 4.636   32.550 1.00 44.51  ? 219 GLY A N   1 
ATOM   1728 C  CA  . GLY A 1 222 ? 26.371 5.415   31.644 1.00 45.12  ? 219 GLY A CA  1 
ATOM   1729 C  C   . GLY A 1 222 ? 25.360 4.550   30.911 1.00 39.00  ? 219 GLY A C   1 
ATOM   1730 O  O   . GLY A 1 222 ? 25.142 3.380   31.229 1.00 38.97  ? 219 GLY A O   1 
ATOM   1731 N  N   . HIS A 1 223 ? 24.764 5.143   29.878 1.00 39.46  ? 220 HIS A N   1 
ATOM   1732 C  CA  . HIS A 1 223 ? 23.632 4.515   29.195 1.00 40.10  ? 220 HIS A CA  1 
ATOM   1733 C  C   . HIS A 1 223 ? 24.011 3.170   28.578 1.00 36.07  ? 220 HIS A C   1 
ATOM   1734 O  O   . HIS A 1 223 ? 23.262 2.190   28.692 1.00 36.41  ? 220 HIS A O   1 
ATOM   1735 C  CB  . HIS A 1 223 ? 23.093 5.462   28.120 1.00 39.54  ? 220 HIS A CB  1 
ATOM   1736 C  CG  . HIS A 1 223 ? 21.921 4.914   27.374 1.00 40.00  ? 220 HIS A CG  1 
ATOM   1737 N  ND1 . HIS A 1 223 ? 20.703 4.683   27.975 1.00 35.98  ? 220 HIS A ND1 1 
ATOM   1738 C  CD2 . HIS A 1 223 ? 21.780 4.548   26.078 1.00 41.08  ? 220 HIS A CD2 1 
ATOM   1739 C  CE1 . HIS A 1 223 ? 19.861 4.194   27.081 1.00 40.04  ? 220 HIS A CE1 1 
ATOM   1740 N  NE2 . HIS A 1 223 ? 20.488 4.106   25.920 1.00 38.88  ? 220 HIS A NE2 1 
ATOM   1741 N  N   . VAL A 1 224 ? 25.157 3.106   27.903 1.00 36.97  ? 221 VAL A N   1 
ATOM   1742 C  CA  . VAL A 1 224 ? 25.547 1.883   27.204 1.00 36.10  ? 221 VAL A CA  1 
ATOM   1743 C  C   . VAL A 1 224 ? 26.221 0.967   28.215 1.00 35.75  ? 221 VAL A C   1 
ATOM   1744 O  O   . VAL A 1 224 ? 27.451 0.821   28.236 1.00 34.44  ? 221 VAL A O   1 
ATOM   1745 C  CB  . VAL A 1 224 ? 26.461 2.175   25.999 1.00 37.15  ? 221 VAL A CB  1 
ATOM   1746 C  CG1 . VAL A 1 224 ? 26.477 0.976   25.061 1.00 37.71  ? 221 VAL A CG1 1 
ATOM   1747 C  CG2 . VAL A 1 224 ? 25.980 3.407   25.268 1.00 40.11  ? 221 VAL A CG2 1 
ATOM   1748 N  N   . ILE A 1 225 ? 25.402 0.343   29.060 1.00 30.87  ? 222 ILE A N   1 
ATOM   1749 C  CA  . ILE A 1 225 ? 25.895 -0.273  30.280 1.00 35.23  ? 222 ILE A CA  1 
ATOM   1750 C  C   . ILE A 1 225 ? 26.681 -1.545  29.999 1.00 34.76  ? 222 ILE A C   1 
ATOM   1751 O  O   . ILE A 1 225 ? 27.510 -1.953  30.821 1.00 36.42  ? 222 ILE A O   1 
ATOM   1752 C  CB  . ILE A 1 225 ? 24.691 -0.515  31.210 1.00 33.95  ? 222 ILE A CB  1 
ATOM   1753 C  CG1 . ILE A 1 225 ? 25.148 -0.732  32.644 1.00 35.57  ? 222 ILE A CG1 1 
ATOM   1754 C  CG2 . ILE A 1 225 ? 23.839 -1.690  30.694 1.00 32.98  ? 222 ILE A CG2 1 
ATOM   1755 C  CD1 . ILE A 1 225 ? 23.989 -0.755  33.648 1.00 36.96  ? 222 ILE A CD1 1 
ATOM   1756 N  N   . THR A 1 226 ? 26.466 -2.162  28.834 1.00 32.57  ? 223 THR A N   1 
ATOM   1757 C  CA  . THR A 1 226 ? 27.138 -3.403  28.470 1.00 31.42  ? 223 THR A CA  1 
ATOM   1758 C  C   . THR A 1 226 ? 28.589 -3.198  28.058 1.00 33.86  ? 223 THR A C   1 
ATOM   1759 O  O   . THR A 1 226 ? 29.302 -4.185  27.840 1.00 32.72  ? 223 THR A O   1 
ATOM   1760 C  CB  . THR A 1 226 ? 26.380 -4.075  27.325 1.00 31.55  ? 223 THR A CB  1 
ATOM   1761 O  OG1 . THR A 1 226 ? 26.084 -3.083  26.328 1.00 33.72  ? 223 THR A OG1 1 
ATOM   1762 C  CG2 . THR A 1 226 ? 25.080 -4.649  27.842 1.00 32.59  ? 223 THR A CG2 1 
ATOM   1763 N  N   . ILE A 1 227 ? 29.045 -1.957  27.898 1.00 33.01  ? 224 ILE A N   1 
ATOM   1764 C  CA  . ILE A 1 227 ? 30.449 -1.702  27.601 1.00 35.93  ? 224 ILE A CA  1 
ATOM   1765 C  C   . ILE A 1 227 ? 31.104 -0.778  28.614 1.00 39.00  ? 224 ILE A C   1 
ATOM   1766 O  O   . ILE A 1 227 ? 32.287 -0.448  28.456 1.00 39.36  ? 224 ILE A O   1 
ATOM   1767 C  CB  . ILE A 1 227 ? 30.649 -1.133  26.184 1.00 40.72  ? 224 ILE A CB  1 
ATOM   1768 C  CG1 . ILE A 1 227 ? 30.119 0.297   26.094 1.00 38.16  ? 224 ILE A CG1 1 
ATOM   1769 C  CG2 . ILE A 1 227 ? 29.940 -2.018  25.145 1.00 36.78  ? 224 ILE A CG2 1 
ATOM   1770 C  CD1 . ILE A 1 227 ? 29.963 0.782   24.655 1.00 39.98  ? 224 ILE A CD1 1 
ATOM   1771 N  N   . ASP A 1 228 ? 30.374 -0.323  29.619 1.00 37.63  ? 225 ASP A N   1 
ATOM   1772 C  CA  . ASP A 1 228 ? 30.886 0.638   30.588 1.00 43.09  ? 225 ASP A CA  1 
ATOM   1773 C  C   . ASP A 1 228 ? 31.615 -0.091  31.723 1.00 42.19  ? 225 ASP A C   1 
ATOM   1774 O  O   . ASP A 1 228 ? 31.839 -1.306  31.668 1.00 38.39  ? 225 ASP A O   1 
ATOM   1775 C  CB  . ASP A 1 228 ? 29.741 1.510   31.100 1.00 42.46  ? 225 ASP A CB  1 
ATOM   1776 C  CG  . ASP A 1 228 ? 30.156 2.967   31.311 1.00 51.47  ? 225 ASP A CG  1 
ATOM   1777 O  OD1 . ASP A 1 228 ? 31.351 3.225   31.605 1.00 51.97  ? 225 ASP A OD1 1 
ATOM   1778 O  OD2 . ASP A 1 228 ? 29.281 3.855   31.186 1.00 50.33  ? 225 ASP A OD2 1 
ATOM   1779 N  N   . LYS A 1 229 ? 31.961 0.650   32.787 1.00 43.28  ? 226 LYS A N   1 
ATOM   1780 C  CA  . LYS A 1 229 ? 32.933 0.201   33.782 1.00 42.96  ? 226 LYS A CA  1 
ATOM   1781 C  C   . LYS A 1 229 ? 32.379 -0.843  34.746 1.00 40.46  ? 226 LYS A C   1 
ATOM   1782 O  O   . LYS A 1 229 ? 33.160 -1.433  35.498 1.00 41.71  ? 226 LYS A O   1 
ATOM   1783 C  CB  . LYS A 1 229 ? 33.438 1.378   34.622 1.00 47.06  ? 226 LYS A CB  1 
ATOM   1784 C  CG  . LYS A 1 229 ? 32.389 2.451   34.880 1.00 51.01  ? 226 LYS A CG  1 
ATOM   1785 C  CD  . LYS A 1 229 ? 32.826 3.424   35.985 1.00 55.42  ? 226 LYS A CD  1 
ATOM   1786 C  CE  . LYS A 1 229 ? 33.734 4.491   35.441 1.00 63.71  ? 226 LYS A CE  1 
ATOM   1787 N  NZ  . LYS A 1 229 ? 33.062 5.131   34.274 1.00 65.30  ? 226 LYS A NZ  1 
ATOM   1788 N  N   . GLU A 1 230 ? 31.067 -1.066  34.781 1.00 39.32  ? 227 GLU A N   1 
ATOM   1789 C  CA  . GLU A 1 230 ? 30.497 -2.085  35.658 1.00 37.63  ? 227 GLU A CA  1 
ATOM   1790 C  C   . GLU A 1 230 ? 29.995 -3.290  34.889 1.00 35.34  ? 227 GLU A C   1 
ATOM   1791 O  O   . GLU A 1 230 ? 29.189 -4.063  35.413 1.00 34.02  ? 227 GLU A O   1 
ATOM   1792 C  CB  . GLU A 1 230 ? 29.363 -1.508  36.499 1.00 39.12  ? 227 GLU A CB  1 
ATOM   1793 C  CG  . GLU A 1 230 ? 29.753 -0.259  37.256 1.00 41.99  ? 227 GLU A CG  1 
ATOM   1794 C  CD  . GLU A 1 230 ? 28.644 0.199   38.162 1.00 47.97  ? 227 GLU A CD  1 
ATOM   1795 O  OE1 . GLU A 1 230 ? 28.543 -0.335  39.287 1.00 54.24  ? 227 GLU A OE1 1 
ATOM   1796 O  OE2 . GLU A 1 230 ? 27.851 1.060   37.730 1.00 46.74  ? 227 GLU A OE2 1 
ATOM   1797 N  N   . LYS A 1 231 ? 30.456 -3.468  33.650 1.00 33.06  ? 228 LYS A N   1 
ATOM   1798 C  CA  . LYS A 1 231 ? 29.883 -4.515  32.814 1.00 33.10  ? 228 LYS A CA  1 
ATOM   1799 C  C   . LYS A 1 231 ? 30.071 -5.896  33.431 1.00 31.27  ? 228 LYS A C   1 
ATOM   1800 O  O   . LYS A 1 231 ? 29.207 -6.763  33.269 1.00 34.08  ? 228 LYS A O   1 
ATOM   1801 C  CB  . LYS A 1 231 ? 30.474 -4.433  31.401 1.00 32.78  ? 228 LYS A CB  1 
ATOM   1802 C  CG  . LYS A 1 231 ? 31.961 -4.752  31.300 1.00 34.85  ? 228 LYS A CG  1 
ATOM   1803 C  CD  . LYS A 1 231 ? 32.477 -4.588  29.847 1.00 33.61  ? 228 LYS A CD  1 
ATOM   1804 C  CE  . LYS A 1 231 ? 33.804 -3.837  29.846 1.00 46.03  ? 228 LYS A CE  1 
ATOM   1805 N  NZ  . LYS A 1 231 ? 34.907 -4.686  30.369 1.00 49.23  ? 228 LYS A NZ  1 
ATOM   1806 N  N   . GLU A 1 232 ? 31.163 -6.113  34.161 1.00 32.51  ? 229 GLU A N   1 
ATOM   1807 C  CA  . GLU A 1 232 ? 31.394 -7.423  34.763 1.00 37.07  ? 229 GLU A CA  1 
ATOM   1808 C  C   . GLU A 1 232 ? 30.315 -7.762  35.785 1.00 35.81  ? 229 GLU A C   1 
ATOM   1809 O  O   . GLU A 1 232 ? 29.894 -8.921  35.890 1.00 36.05  ? 229 GLU A O   1 
ATOM   1810 C  CB  . GLU A 1 232 ? 32.766 -7.478  35.434 1.00 39.20  ? 229 GLU A CB  1 
ATOM   1811 C  CG  . GLU A 1 232 ? 33.940 -7.412  34.473 1.00 44.89  ? 229 GLU A CG  1 
ATOM   1812 C  CD  . GLU A 1 232 ? 34.194 -6.002  33.955 1.00 48.64  ? 229 GLU A CD  1 
ATOM   1813 O  OE1 . GLU A 1 232 ? 34.813 -5.861  32.870 1.00 53.25  ? 229 GLU A OE1 1 
ATOM   1814 O  OE2 . GLU A 1 232 ? 33.801 -5.028  34.654 1.00 48.42  ? 229 GLU A OE2 1 
ATOM   1815 N  N   . GLN A 1 233 ? 29.852 -6.768  36.551 1.00 31.70  ? 230 GLN A N   1 
ATOM   1816 C  CA  . GLN A 1 233 ? 28.762 -7.025  37.486 1.00 35.44  ? 230 GLN A CA  1 
ATOM   1817 C  C   . GLN A 1 233 ? 27.435 -7.187  36.757 1.00 32.28  ? 230 GLN A C   1 
ATOM   1818 O  O   . GLN A 1 233 ? 26.606 -8.025  37.140 1.00 32.87  ? 230 GLN A O   1 
ATOM   1819 C  CB  . GLN A 1 233 ? 28.676 -5.894  38.511 1.00 36.81  ? 230 GLN A CB  1 
ATOM   1820 C  CG  . GLN A 1 233 ? 27.589 -6.102  39.581 1.00 41.59  ? 230 GLN A CG  1 
ATOM   1821 C  CD  . GLN A 1 233 ? 27.878 -7.305  40.470 1.00 42.80  ? 230 GLN A CD  1 
ATOM   1822 O  OE1 . GLN A 1 233 ? 27.129 -8.286  40.485 1.00 45.65  ? 230 GLN A OE1 1 
ATOM   1823 N  NE2 . GLN A 1 233 ? 29.012 -7.268  41.143 1.00 43.49  ? 230 GLN A NE2 1 
ATOM   1824 N  N   . VAL A 1 234 ? 27.205 -6.389  35.713 1.00 32.42  ? 231 VAL A N   1 
ATOM   1825 C  CA  . VAL A 1 234 ? 25.991 -6.560  34.917 1.00 30.32  ? 231 VAL A CA  1 
ATOM   1826 C  C   . VAL A 1 234 ? 25.941 -7.971  34.348 1.00 31.73  ? 231 VAL A C   1 
ATOM   1827 O  O   . VAL A 1 234 ? 24.903 -8.642  34.393 1.00 28.87  ? 231 VAL A O   1 
ATOM   1828 C  CB  . VAL A 1 234 ? 25.927 -5.513  33.789 1.00 30.63  ? 231 VAL A CB  1 
ATOM   1829 C  CG1 . VAL A 1 234 ? 24.754 -5.802  32.850 1.00 31.83  ? 231 VAL A CG1 1 
ATOM   1830 C  CG2 . VAL A 1 234 ? 25.877 -4.088  34.332 1.00 34.57  ? 231 VAL A CG2 1 
ATOM   1831 N  N   . PHE A 1 235 ? 27.067 -8.439  33.805 1.00 28.56  ? 232 PHE A N   1 
ATOM   1832 C  CA  . PHE A 1 235 ? 27.119 -9.777  33.218 1.00 31.46  ? 232 PHE A CA  1 
ATOM   1833 C  C   . PHE A 1 235 ? 26.829 -10.845 34.271 1.00 29.76  ? 232 PHE A C   1 
ATOM   1834 O  O   . PHE A 1 235 ? 26.072 -11.795 34.022 1.00 29.08  ? 232 PHE A O   1 
ATOM   1835 C  CB  . PHE A 1 235 ? 28.501 -10.031 32.599 1.00 30.02  ? 232 PHE A CB  1 
ATOM   1836 C  CG  . PHE A 1 235 ? 28.872 -9.105  31.457 1.00 30.90  ? 232 PHE A CG  1 
ATOM   1837 C  CD1 . PHE A 1 235 ? 27.951 -8.243  30.870 1.00 27.18  ? 232 PHE A CD1 1 
ATOM   1838 C  CD2 . PHE A 1 235 ? 30.175 -9.109  30.973 1.00 30.26  ? 232 PHE A CD2 1 
ATOM   1839 C  CE1 . PHE A 1 235 ? 28.339 -7.410  29.806 1.00 29.31  ? 232 PHE A CE1 1 
ATOM   1840 C  CE2 . PHE A 1 235 ? 30.568 -8.278  29.922 1.00 30.55  ? 232 PHE A CE2 1 
ATOM   1841 C  CZ  . PHE A 1 235 ? 29.645 -7.432  29.340 1.00 29.03  ? 232 PHE A CZ  1 
ATOM   1842 N  N   . GLU A 1 236 ? 27.440 -10.714 35.447 1.00 29.82  ? 233 GLU A N   1 
ATOM   1843 C  CA  . GLU A 1 236 ? 27.200 -11.677 36.518 1.00 31.48  ? 233 GLU A CA  1 
ATOM   1844 C  C   . GLU A 1 236 ? 25.727 -11.693 36.917 1.00 31.80  ? 233 GLU A C   1 
ATOM   1845 O  O   . GLU A 1 236 ? 25.144 -12.761 37.137 1.00 30.01  ? 233 GLU A O   1 
ATOM   1846 C  CB  . GLU A 1 236 ? 28.084 -11.322 37.719 1.00 32.93  ? 233 GLU A CB  1 
ATOM   1847 C  CG  . GLU A 1 236 ? 27.869 -12.176 38.971 1.00 40.89  ? 233 GLU A CG  1 
ATOM   1848 C  CD  . GLU A 1 236 ? 28.102 -13.671 38.752 1.00 44.88  ? 233 GLU A CD  1 
ATOM   1849 O  OE1 . GLU A 1 236 ? 27.588 -14.458 39.593 1.00 49.20  ? 233 GLU A OE1 1 
ATOM   1850 O  OE2 . GLU A 1 236 ? 28.842 -14.054 37.815 1.00 42.87  ? 233 GLU A OE2 1 
ATOM   1851 N  N   . ASP A 1 237 ? 25.112 -10.512 37.032 1.00 30.58  ? 234 ASP A N   1 
ATOM   1852 C  CA  . ASP A 1 237 ? 23.696 -10.451 37.379 1.00 32.39  ? 234 ASP A CA  1 
ATOM   1853 C  C   . ASP A 1 237 ? 22.831 -11.093 36.301 1.00 27.68  ? 234 ASP A C   1 
ATOM   1854 O  O   . ASP A 1 237 ? 21.849 -11.778 36.616 1.00 28.72  ? 234 ASP A O   1 
ATOM   1855 C  CB  . ASP A 1 237 ? 23.274 -9.003  37.633 1.00 31.24  ? 234 ASP A CB  1 
ATOM   1856 C  CG  . ASP A 1 237 ? 23.952 -8.409  38.870 1.00 37.38  ? 234 ASP A CG  1 
ATOM   1857 O  OD1 . ASP A 1 237 ? 24.345 -9.197  39.764 1.00 34.90  ? 234 ASP A OD1 1 
ATOM   1858 O  OD2 . ASP A 1 237 ? 24.094 -7.163  38.955 1.00 35.52  ? 234 ASP A OD2 1 
ATOM   1859 N  N   . ILE A 1 238 ? 23.178 -10.886 35.022 1.00 26.31  ? 235 ILE A N   1 
ATOM   1860 C  CA  . ILE A 1 238 ? 22.451 -11.549 33.942 1.00 27.86  ? 235 ILE A CA  1 
ATOM   1861 C  C   . ILE A 1 238 ? 22.615 -13.057 34.049 1.00 27.53  ? 235 ILE A C   1 
ATOM   1862 O  O   . ILE A 1 238 ? 21.645 -13.808 33.926 1.00 25.60  ? 235 ILE A O   1 
ATOM   1863 C  CB  . ILE A 1 238 ? 22.917 -11.019 32.574 1.00 26.14  ? 235 ILE A CB  1 
ATOM   1864 C  CG1 . ILE A 1 238 ? 22.482 -9.565  32.406 1.00 27.51  ? 235 ILE A CG1 1 
ATOM   1865 C  CG2 . ILE A 1 238 ? 22.361 -11.888 31.417 1.00 25.29  ? 235 ILE A CG2 1 
ATOM   1866 C  CD1 . ILE A 1 238 ? 23.032 -8.878  31.137 1.00 26.30  ? 235 ILE A CD1 1 
ATOM   1867 N  N   . TYR A 1 239 ? 23.841 -13.524 34.295 1.00 25.31  ? 236 TYR A N   1 
ATOM   1868 C  CA  . TYR A 1 239 ? 24.068 -14.958 34.444 1.00 28.40  ? 236 TYR A CA  1 
ATOM   1869 C  C   . TYR A 1 239 ? 23.226 -15.541 35.582 1.00 28.16  ? 236 TYR A C   1 
ATOM   1870 O  O   . TYR A 1 239 ? 22.615 -16.607 35.432 1.00 27.13  ? 236 TYR A O   1 
ATOM   1871 C  CB  . TYR A 1 239 ? 25.554 -15.210 34.687 1.00 31.47  ? 236 TYR A CB  1 
ATOM   1872 C  CG  . TYR A 1 239 ? 25.925 -16.631 35.002 1.00 31.29  ? 236 TYR A CG  1 
ATOM   1873 C  CD1 . TYR A 1 239 ? 25.805 -17.636 34.044 1.00 31.34  ? 236 TYR A CD1 1 
ATOM   1874 C  CD2 . TYR A 1 239 ? 26.421 -16.967 36.262 1.00 34.59  ? 236 TYR A CD2 1 
ATOM   1875 C  CE1 . TYR A 1 239 ? 26.170 -18.954 34.345 1.00 32.78  ? 236 TYR A CE1 1 
ATOM   1876 C  CE2 . TYR A 1 239 ? 26.788 -18.264 36.573 1.00 36.69  ? 236 TYR A CE2 1 
ATOM   1877 C  CZ  . TYR A 1 239 ? 26.669 -19.253 35.613 1.00 37.30  ? 236 TYR A CZ  1 
ATOM   1878 O  OH  . TYR A 1 239 ? 27.037 -20.541 35.930 1.00 39.06  ? 236 TYR A OH  1 
ATOM   1879 N  N   . GLN A 1 240 ? 23.183 -14.857 36.729 1.00 27.14  ? 237 GLN A N   1 
ATOM   1880 C  CA  . GLN A 1 240 ? 22.384 -15.358 37.847 1.00 26.52  ? 237 GLN A CA  1 
ATOM   1881 C  C   . GLN A 1 240 ? 20.910 -15.448 37.479 1.00 28.32  ? 237 GLN A C   1 
ATOM   1882 O  O   . GLN A 1 240 ? 20.228 -16.408 37.852 1.00 27.15  ? 237 GLN A O   1 
ATOM   1883 C  CB  . GLN A 1 240 ? 22.594 -14.480 39.084 1.00 29.55  ? 237 GLN A CB  1 
ATOM   1884 C  CG  . GLN A 1 240 ? 24.014 -14.557 39.679 1.00 36.00  ? 237 GLN A CG  1 
ATOM   1885 C  CD  . GLN A 1 240 ? 24.470 -15.994 39.949 1.00 48.67  ? 237 GLN A CD  1 
ATOM   1886 O  OE1 . GLN A 1 240 ? 23.653 -16.865 40.295 1.00 47.64  ? 237 GLN A OE1 1 
ATOM   1887 N  NE2 . GLN A 1 240 ? 25.777 -16.241 39.835 1.00 46.47  ? 237 GLN A NE2 1 
ATOM   1888 N  N   . PHE A 1 241 ? 20.405 -14.460 36.748 1.00 23.80  ? 238 PHE A N   1 
ATOM   1889 C  CA  . PHE A 1 241 ? 19.046 -14.539 36.214 1.00 25.02  ? 238 PHE A CA  1 
ATOM   1890 C  C   . PHE A 1 241 ? 18.864 -15.745 35.300 1.00 26.94  ? 238 PHE A C   1 
ATOM   1891 O  O   . PHE A 1 241 ? 17.926 -16.534 35.472 1.00 26.55  ? 238 PHE A O   1 
ATOM   1892 C  CB  . PHE A 1 241 ? 18.711 -13.238 35.475 1.00 26.70  ? 238 PHE A CB  1 
ATOM   1893 C  CG  . PHE A 1 241 ? 17.394 -13.272 34.767 1.00 23.25  ? 238 PHE A CG  1 
ATOM   1894 C  CD1 . PHE A 1 241 ? 16.187 -13.180 35.462 1.00 27.19  ? 238 PHE A CD1 1 
ATOM   1895 C  CD2 . PHE A 1 241 ? 17.371 -13.325 33.378 1.00 23.15  ? 238 PHE A CD2 1 
ATOM   1896 C  CE1 . PHE A 1 241 ? 14.979 -13.210 34.778 1.00 26.70  ? 238 PHE A CE1 1 
ATOM   1897 C  CE2 . PHE A 1 241 ? 16.185 -13.330 32.687 1.00 25.07  ? 238 PHE A CE2 1 
ATOM   1898 C  CZ  . PHE A 1 241 ? 14.982 -13.275 33.372 1.00 24.02  ? 238 PHE A CZ  1 
ATOM   1899 N  N   . LEU A 1 242 ? 19.738 -15.890 34.307 1.00 24.03  ? 239 LEU A N   1 
ATOM   1900 C  CA  . LEU A 1 242 ? 19.636 -17.018 33.388 1.00 25.17  ? 239 LEU A CA  1 
ATOM   1901 C  C   . LEU A 1 242 ? 19.629 -18.349 34.128 1.00 26.94  ? 239 LEU A C   1 
ATOM   1902 O  O   . LEU A 1 242 ? 18.876 -19.262 33.773 1.00 27.29  ? 239 LEU A O   1 
ATOM   1903 C  CB  . LEU A 1 242 ? 20.792 -16.990 32.384 1.00 24.14  ? 239 LEU A CB  1 
ATOM   1904 C  CG  . LEU A 1 242 ? 20.824 -15.809 31.428 1.00 23.70  ? 239 LEU A CG  1 
ATOM   1905 C  CD1 . LEU A 1 242 ? 22.124 -15.792 30.613 1.00 25.87  ? 239 LEU A CD1 1 
ATOM   1906 C  CD2 . LEU A 1 242 ? 19.603 -15.895 30.516 1.00 26.07  ? 239 LEU A CD2 1 
ATOM   1907 N  N   . GLU A 1 243 ? 20.488 -18.492 35.138 1.00 23.03  ? 240 GLU A N   1 
ATOM   1908 C  CA  . GLU A 1 243 ? 20.567 -19.754 35.865 1.00 27.90  ? 240 GLU A CA  1 
ATOM   1909 C  C   . GLU A 1 243 ? 19.293 -20.053 36.646 1.00 32.57  ? 240 GLU A C   1 
ATOM   1910 O  O   . GLU A 1 243 ? 19.086 -21.196 37.054 1.00 31.56  ? 240 GLU A O   1 
ATOM   1911 C  CB  . GLU A 1 243 ? 21.765 -19.733 36.813 1.00 30.41  ? 240 GLU A CB  1 
ATOM   1912 C  CG  . GLU A 1 243 ? 23.089 -19.762 36.048 1.00 29.94  ? 240 GLU A CG  1 
ATOM   1913 C  CD  . GLU A 1 243 ? 23.386 -21.129 35.465 1.00 33.47  ? 240 GLU A CD  1 
ATOM   1914 O  OE1 . GLU A 1 243 ? 23.614 -22.072 36.244 1.00 35.11  ? 240 GLU A OE1 1 
ATOM   1915 O  OE2 . GLU A 1 243 ? 23.387 -21.275 34.233 1.00 33.18  ? 240 GLU A OE2 1 
ATOM   1916 N  N   . SER A 1 244 ? 18.434 -19.063 36.850 1.00 30.03  ? 241 SER A N   1 
ATOM   1917 C  CA  . SER A 1 244 ? 17.229 -19.266 37.637 1.00 28.85  ? 241 SER A CA  1 
ATOM   1918 C  C   . SER A 1 244 ? 16.042 -19.742 36.804 1.00 30.39  ? 241 SER A C   1 
ATOM   1919 O  O   . SER A 1 244 ? 15.014 -20.116 37.380 1.00 31.75  ? 241 SER A O   1 
ATOM   1920 C  CB  . SER A 1 244 ? 16.870 -17.961 38.353 1.00 31.33  ? 241 SER A CB  1 
ATOM   1921 O  OG  . SER A 1 244 ? 16.238 -17.081 37.434 1.00 29.38  ? 241 SER A OG  1 
ATOM   1922 N  N   . LEU A 1 245 ? 16.162 -19.773 35.475 1.00 26.99  ? 242 LEU A N   1 
ATOM   1923 C  CA  . LEU A 1 245 ? 15.011 -19.940 34.602 1.00 28.92  ? 242 LEU A CA  1 
ATOM   1924 C  C   . LEU A 1 245 ? 14.694 -21.415 34.372 1.00 31.33  ? 242 LEU A C   1 
ATOM   1925 O  O   . LEU A 1 245 ? 15.455 -22.314 34.735 1.00 31.19  ? 242 LEU A O   1 
ATOM   1926 C  CB  . LEU A 1 245 ? 15.263 -19.232 33.267 1.00 26.55  ? 242 LEU A CB  1 
ATOM   1927 C  CG  . LEU A 1 245 ? 15.508 -17.726 33.398 1.00 25.17  ? 242 LEU A CG  1 
ATOM   1928 C  CD1 . LEU A 1 245 ? 15.813 -17.142 32.022 1.00 21.92  ? 242 LEU A CD1 1 
ATOM   1929 C  CD2 . LEU A 1 245 ? 14.322 -17.005 34.023 1.00 26.27  ? 242 LEU A CD2 1 
ATOM   1930 N  N   . ASP A 1 246 ? 13.562 -21.651 33.713 1.00 33.40  ? 243 ASP A N   1 
ATOM   1931 C  CA  . ASP A 1 246 ? 13.003 -22.994 33.551 1.00 36.34  ? 243 ASP A CA  1 
ATOM   1932 C  C   . ASP A 1 246 ? 13.496 -23.661 32.259 1.00 33.35  ? 243 ASP A C   1 
ATOM   1933 O  O   . ASP A 1 246 ? 12.723 -24.033 31.380 1.00 37.50  ? 243 ASP A O   1 
ATOM   1934 C  CB  . ASP A 1 246 ? 11.478 -22.915 33.596 1.00 42.04  ? 243 ASP A CB  1 
ATOM   1935 C  CG  . ASP A 1 246 ? 10.825 -24.276 33.627 1.00 50.29  ? 243 ASP A CG  1 
ATOM   1936 O  OD1 . ASP A 1 246 ? 9.714  -24.420 33.066 1.00 58.99  ? 243 ASP A OD1 1 
ATOM   1937 O  OD2 . ASP A 1 246 ? 11.441 -25.214 34.178 1.00 50.57  ? 243 ASP A OD2 1 
ATOM   1938 N  N   . TRP A 1 247 ? 14.813 -23.856 32.173 1.00 33.82  ? 244 TRP A N   1 
ATOM   1939 C  CA  . TRP A 1 247 ? 15.401 -24.570 31.045 1.00 35.32  ? 244 TRP A CA  1 
ATOM   1940 C  C   . TRP A 1 247 ? 15.128 -26.067 31.136 1.00 40.50  ? 244 TRP A C   1 
ATOM   1941 O  O   . TRP A 1 247 ? 15.176 -26.660 32.215 1.00 37.45  ? 244 TRP A O   1 
ATOM   1942 C  CB  . TRP A 1 247 ? 16.911 -24.345 31.000 1.00 33.62  ? 244 TRP A CB  1 
ATOM   1943 C  CG  . TRP A 1 247 ? 17.315 -22.907 31.034 1.00 29.30  ? 244 TRP A CG  1 
ATOM   1944 C  CD1 . TRP A 1 247 ? 17.733 -22.200 32.130 1.00 30.22  ? 244 TRP A CD1 1 
ATOM   1945 C  CD2 . TRP A 1 247 ? 17.368 -22.000 29.928 1.00 30.87  ? 244 TRP A CD2 1 
ATOM   1946 N  NE1 . TRP A 1 247 ? 18.042 -20.908 31.771 1.00 29.29  ? 244 TRP A NE1 1 
ATOM   1947 C  CE2 . TRP A 1 247 ? 17.822 -20.762 30.424 1.00 26.57  ? 244 TRP A CE2 1 
ATOM   1948 C  CE3 . TRP A 1 247 ? 17.077 -22.117 28.560 1.00 29.74  ? 244 TRP A CE3 1 
ATOM   1949 C  CZ2 . TRP A 1 247 ? 17.995 -19.647 29.604 1.00 25.50  ? 244 TRP A CZ2 1 
ATOM   1950 C  CZ3 . TRP A 1 247 ? 17.247 -21.008 27.748 1.00 29.70  ? 244 TRP A CZ3 1 
ATOM   1951 C  CH2 . TRP A 1 247 ? 17.715 -19.796 28.267 1.00 26.63  ? 244 TRP A CH2 1 
ATOM   1952 N  N   . SER A 1 248 ? 14.876 -26.690 29.987 1.00 34.85  ? 245 SER A N   1 
ATOM   1953 C  CA  . SER A 1 248 ? 14.692 -28.137 29.976 1.00 41.27  ? 245 SER A CA  1 
ATOM   1954 C  C   . SER A 1 248 ? 16.003 -28.885 30.201 1.00 45.25  ? 245 SER A C   1 
ATOM   1955 O  O   . SER A 1 248 ? 15.976 -30.035 30.653 1.00 47.50  ? 245 SER A O   1 
ATOM   1956 C  CB  . SER A 1 248 ? 14.035 -28.570 28.665 1.00 42.32  ? 245 SER A CB  1 
ATOM   1957 O  OG  . SER A 1 248 ? 14.866 -28.261 27.567 1.00 52.56  ? 245 SER A OG  1 
ATOM   1958 N  N   . GLU A 1 249 ? 17.141 -28.264 29.905 1.00 47.79  ? 246 GLU A N   1 
ATOM   1959 C  CA  . GLU A 1 249 ? 18.444 -28.840 30.221 1.00 50.86  ? 246 GLU A CA  1 
ATOM   1960 C  C   . GLU A 1 249 ? 19.486 -27.740 30.420 1.00 51.89  ? 246 GLU A C   1 
ATOM   1961 O  O   . GLU A 1 249 ? 19.415 -26.671 29.805 1.00 47.67  ? 246 GLU A O   1 
ATOM   1962 C  CB  . GLU A 1 249 ? 18.912 -29.796 29.124 1.00 60.67  ? 246 GLU A CB  1 
ATOM   1963 C  CG  . GLU A 1 249 ? 18.508 -29.399 27.716 1.00 61.79  ? 246 GLU A CG  1 
ATOM   1964 C  CD  . GLU A 1 249 ? 18.645 -30.550 26.743 1.00 67.57  ? 246 GLU A CD  1 
ATOM   1965 O  OE1 . GLU A 1 249 ? 19.668 -31.265 26.825 1.00 75.03  ? 246 GLU A OE1 1 
ATOM   1966 O  OE2 . GLU A 1 249 ? 17.740 -30.739 25.899 1.00 71.56  ? 246 GLU A OE2 1 
ATOM   1967 O  OXT . GLU A 1 249 ? 20.426 -27.904 31.204 1.00 56.52  ? 246 GLU A OXT 1 
HETATM 1968 CA CA  . CA  B 2 .   ? 14.042 -13.899 39.352 0.62 29.32  ? 301 CA  A CA  1 
HETATM 1969 CA CA  . CA  C 2 .   ? -0.074 -9.978  38.422 0.77 35.77  ? 302 CA  A CA  1 
HETATM 1970 CA CA  . CA  D 2 .   ? 23.981 -24.262 12.112 0.93 39.09  ? 303 CA  A CA  1 
HETATM 1971 CA CA  . CA  E 2 .   ? -1.873 -2.361  27.494 0.71 52.38  ? 304 CA  A CA  1 
HETATM 1972 O  O   . HOH F 3 .   ? 11.760 6.053   8.133  1.00 40.75  ? 401 HOH A O   1 
HETATM 1973 O  O   . HOH F 3 .   ? 30.495 -17.954 15.490 1.00 37.66  ? 402 HOH A O   1 
HETATM 1974 O  O   . HOH F 3 .   ? 14.549 -25.456 16.675 1.00 42.03  ? 403 HOH A O   1 
HETATM 1975 O  O   . HOH F 3 .   ? 30.992 -13.329 36.837 1.00 43.17  ? 404 HOH A O   1 
HETATM 1976 O  O   . HOH F 3 .   ? 25.920 -23.064 13.023 1.00 41.74  ? 405 HOH A O   1 
HETATM 1977 O  O   . HOH F 3 .   ? 11.561 -0.114  42.126 1.00 48.11  ? 406 HOH A O   1 
HETATM 1978 O  O   . HOH F 3 .   ? 11.300 -14.341 10.551 1.00 39.50  ? 407 HOH A O   1 
HETATM 1979 O  O   . HOH F 3 .   ? 24.096 3.899   10.535 1.00 45.76  ? 408 HOH A O   1 
HETATM 1980 O  O   . HOH F 3 .   ? 15.922 12.715  24.572 1.00 53.45  ? 409 HOH A O   1 
HETATM 1981 O  O   . HOH F 3 .   ? 1.705  -11.313 37.821 1.00 39.06  ? 410 HOH A O   1 
HETATM 1982 O  O   . HOH F 3 .   ? 5.933  -11.763 27.924 1.00 27.04  ? 411 HOH A O   1 
HETATM 1983 O  O   . HOH F 3 .   ? 8.844  0.797   42.000 1.00 46.08  ? 412 HOH A O   1 
HETATM 1984 O  O   . HOH F 3 .   ? 0.203  -16.538 37.117 1.00 48.03  ? 413 HOH A O   1 
HETATM 1985 O  O   . HOH F 3 .   ? 27.314 9.290   5.790  1.00 61.55  ? 414 HOH A O   1 
HETATM 1986 O  O   . HOH F 3 .   ? 22.151 -7.192  18.433 1.00 30.37  ? 415 HOH A O   1 
HETATM 1987 O  O   . HOH F 3 .   ? 18.013 -3.813  43.178 1.00 36.75  ? 416 HOH A O   1 
HETATM 1988 O  O   . HOH F 3 .   ? 31.648 -10.819 35.668 1.00 46.28  ? 417 HOH A O   1 
HETATM 1989 O  O   . HOH F 3 .   ? 13.835 -12.101 37.911 1.00 32.47  ? 418 HOH A O   1 
HETATM 1990 O  O   . HOH F 3 .   ? 18.757 -20.524 9.298  1.00 41.83  ? 419 HOH A O   1 
HETATM 1991 O  O   . HOH F 3 .   ? 15.527 -13.648 41.152 1.00 36.06  ? 420 HOH A O   1 
HETATM 1992 O  O   . HOH F 3 .   ? 14.122 -15.645 37.933 1.00 36.52  ? 421 HOH A O   1 
HETATM 1993 O  O   . HOH F 3 .   ? 24.596 -23.281 33.074 1.00 41.78  ? 422 HOH A O   1 
HETATM 1994 O  O   . HOH F 3 .   ? -0.209 -9.679  23.781 1.00 37.17  ? 423 HOH A O   1 
HETATM 1995 O  O   . HOH F 3 .   ? 17.184 -24.668 23.229 1.00 35.98  ? 424 HOH A O   1 
HETATM 1996 O  O   . HOH F 3 .   ? 29.975 -20.122 36.524 1.00 51.24  ? 425 HOH A O   1 
HETATM 1997 O  O   . HOH F 3 .   ? 10.920 -21.669 20.603 1.00 37.22  ? 426 HOH A O   1 
HETATM 1998 O  O   . HOH F 3 .   ? 17.556 -23.557 35.710 1.00 47.92  ? 427 HOH A O   1 
HETATM 1999 O  O   . HOH F 3 .   ? -2.972 -4.039  26.199 1.00 58.53  ? 428 HOH A O   1 
HETATM 2000 O  O   . HOH F 3 .   ? 3.387  -7.876  16.259 1.00 42.64  ? 429 HOH A O   1 
HETATM 2001 O  O   . HOH F 3 .   ? 15.794 11.145  26.831 1.00 49.63  ? 430 HOH A O   1 
HETATM 2002 O  O   . HOH F 3 .   ? 8.690  2.790   25.489 1.00 33.18  ? 431 HOH A O   1 
HETATM 2003 O  O   . HOH F 3 .   ? 30.504 -7.340  17.045 1.00 34.60  ? 432 HOH A O   1 
HETATM 2004 O  O   . HOH F 3 .   ? 4.113  -8.188  37.688 1.00 29.99  ? 433 HOH A O   1 
HETATM 2005 O  O   . HOH F 3 .   ? 17.580 -25.947 27.361 1.00 43.76  ? 434 HOH A O   1 
HETATM 2006 O  O   . HOH F 3 .   ? 24.902 5.205   36.871 1.00 41.39  ? 435 HOH A O   1 
HETATM 2007 O  O   . HOH F 3 .   ? 13.787 6.420   8.877  1.00 55.94  ? 436 HOH A O   1 
HETATM 2008 O  O   . HOH F 3 .   ? 4.692  -19.702 20.044 1.00 31.98  ? 437 HOH A O   1 
HETATM 2009 O  O   . HOH F 3 .   ? 23.655 -19.563 8.902  1.00 52.33  ? 438 HOH A O   1 
HETATM 2010 O  O   . HOH F 3 .   ? 27.381 -16.655 23.744 1.00 28.63  ? 439 HOH A O   1 
HETATM 2011 O  O   . HOH F 3 .   ? 23.528 -24.389 14.442 1.00 37.85  ? 440 HOH A O   1 
HETATM 2012 O  O   . HOH F 3 .   ? 23.339 -13.510 10.667 1.00 43.00  ? 441 HOH A O   1 
HETATM 2013 O  O   . HOH F 3 .   ? 7.566  -4.564  12.975 1.00 42.88  ? 442 HOH A O   1 
HETATM 2014 O  O   . HOH F 3 .   ? 14.702 -20.333 40.069 1.00 42.33  ? 443 HOH A O   1 
HETATM 2015 O  O   . HOH F 3 .   ? 23.455 -0.348  21.079 1.00 35.14  ? 444 HOH A O   1 
HETATM 2016 O  O   . HOH F 3 .   ? 29.806 -24.912 19.256 1.00 39.14  ? 445 HOH A O   1 
HETATM 2017 O  O   . HOH F 3 .   ? 14.384 11.293  9.183  1.00 49.49  ? 446 HOH A O   1 
HETATM 2018 O  O   . HOH F 3 .   ? 24.329 -5.849  41.329 1.00 42.97  ? 447 HOH A O   1 
HETATM 2019 O  O   . HOH F 3 .   ? 1.480  -0.031  29.925 1.00 46.27  ? 448 HOH A O   1 
HETATM 2020 O  O   . HOH F 3 .   ? 16.470 -9.290  9.427  1.00 34.76  ? 449 HOH A O   1 
HETATM 2021 O  O   . HOH F 3 .   ? 10.091 -18.211 36.842 1.00 43.31  ? 450 HOH A O   1 
HETATM 2022 O  O   . HOH F 3 .   ? 30.621 -5.230  23.845 1.00 31.21  ? 451 HOH A O   1 
HETATM 2023 O  O   . HOH F 3 .   ? 18.989 -12.609 11.699 1.00 31.78  ? 452 HOH A O   1 
HETATM 2024 O  O   . HOH F 3 .   ? 11.666 -19.490 32.391 1.00 34.29  ? 453 HOH A O   1 
HETATM 2025 O  O   . HOH F 3 .   ? 25.401 1.393   13.896 1.00 37.63  ? 454 HOH A O   1 
HETATM 2026 O  O   . HOH F 3 .   ? 14.875 0.975   31.976 1.00 29.30  ? 455 HOH A O   1 
HETATM 2027 O  O   . HOH F 3 .   ? 3.949  -14.206 23.765 1.00 27.18  ? 456 HOH A O   1 
HETATM 2028 O  O   . HOH F 3 .   ? 29.930 -16.545 38.286 1.00 47.65  ? 457 HOH A O   1 
HETATM 2029 O  O   . HOH F 3 .   ? 33.508 -10.481 27.695 1.00 33.39  ? 458 HOH A O   1 
HETATM 2030 O  O   . HOH F 3 .   ? 26.624 0.198   41.212 1.00 42.90  ? 459 HOH A O   1 
HETATM 2031 O  O   . HOH F 3 .   ? 23.377 12.597  23.548 1.00 50.57  ? 460 HOH A O   1 
HETATM 2032 O  O   . HOH F 3 .   ? 12.594 8.194   25.184 1.00 53.22  ? 461 HOH A O   1 
HETATM 2033 O  O   . HOH F 3 .   ? 33.493 -23.382 21.597 1.00 39.15  ? 462 HOH A O   1 
HETATM 2034 O  O   . HOH F 3 .   ? 8.484  -1.589  43.078 1.00 39.03  ? 463 HOH A O   1 
HETATM 2035 O  O   . HOH F 3 .   ? 18.311 2.930   21.597 1.00 33.07  ? 464 HOH A O   1 
HETATM 2036 O  O   . HOH F 3 .   ? 27.729 -22.076 33.657 1.00 42.63  ? 465 HOH A O   1 
HETATM 2037 O  O   . HOH F 3 .   ? 12.798 -12.797 41.122 0.50 28.06  ? 466 HOH A O   1 
HETATM 2038 O  O   . HOH F 3 .   ? 4.131  -5.968  41.073 1.00 36.92  ? 467 HOH A O   1 
HETATM 2039 O  O   . HOH F 3 .   ? 28.956 -6.100  25.818 1.00 29.88  ? 468 HOH A O   1 
HETATM 2040 O  O   . HOH F 3 .   ? 33.972 -16.439 25.314 1.00 27.97  ? 469 HOH A O   1 
HETATM 2041 O  O   . HOH F 3 .   ? 12.001 -20.180 24.117 1.00 29.48  ? 470 HOH A O   1 
HETATM 2042 O  O   . HOH F 3 .   ? 5.630  -16.240 15.399 1.00 42.13  ? 471 HOH A O   1 
HETATM 2043 O  O   . HOH F 3 .   ? 28.636 -0.780  33.118 1.00 39.36  ? 472 HOH A O   1 
HETATM 2044 O  O   . HOH F 3 .   ? 21.251 -2.812  6.500  1.00 48.60  ? 473 HOH A O   1 
HETATM 2045 O  O   . HOH F 3 .   ? 31.416 -7.942  13.810 1.00 37.06  ? 474 HOH A O   1 
HETATM 2046 O  O   . HOH F 3 .   ? 27.516 -12.378 10.585 1.00 42.52  ? 475 HOH A O   1 
HETATM 2047 O  O   . HOH F 3 .   ? 32.514 -22.214 27.209 1.00 46.52  ? 476 HOH A O   1 
HETATM 2048 O  O   . HOH F 3 .   ? 24.319 -6.083  9.509  1.00 36.97  ? 477 HOH A O   1 
HETATM 2049 O  O   . HOH F 3 .   ? 7.029  -14.429 35.108 1.00 29.79  ? 478 HOH A O   1 
HETATM 2050 O  O   . HOH F 3 .   ? 1.104  -11.774 23.415 1.00 30.17  ? 479 HOH A O   1 
HETATM 2051 O  O   . HOH F 3 .   ? 24.818 7.983   29.805 1.00 46.16  ? 480 HOH A O   1 
HETATM 2052 O  O   . HOH F 3 .   ? 28.507 -20.263 15.302 1.00 36.68  ? 481 HOH A O   1 
HETATM 2053 O  O   . HOH F 3 .   ? 20.428 8.753   19.858 1.00 45.37  ? 482 HOH A O   1 
HETATM 2054 O  O   . HOH F 3 .   ? 7.210  3.478   14.376 1.00 45.56  ? 483 HOH A O   1 
HETATM 2055 O  O   . HOH F 3 .   ? 27.369 2.995   17.193 1.00 45.90  ? 484 HOH A O   1 
HETATM 2056 O  O   . HOH F 3 .   ? 20.153 -11.163 38.815 1.00 35.40  ? 485 HOH A O   1 
HETATM 2057 O  O   . HOH F 3 .   ? -1.554 -8.334  37.774 1.00 47.45  ? 486 HOH A O   1 
HETATM 2058 O  O   . HOH F 3 .   ? 8.601  -18.096 30.096 1.00 41.81  ? 487 HOH A O   1 
HETATM 2059 O  O   . HOH F 3 .   ? 7.041  -15.614 25.542 1.00 30.78  ? 488 HOH A O   1 
HETATM 2060 O  O   . HOH F 3 .   ? 14.081 -0.123  42.647 1.00 46.34  ? 489 HOH A O   1 
HETATM 2061 O  O   . HOH F 3 .   ? 30.630 -0.720  21.047 1.00 40.63  ? 490 HOH A O   1 
HETATM 2062 O  O   . HOH F 3 .   ? 17.936 -10.074 11.684 1.00 32.58  ? 491 HOH A O   1 
HETATM 2063 O  O   . HOH F 3 .   ? 12.233 -20.143 12.756 1.00 39.42  ? 492 HOH A O   1 
HETATM 2064 O  O   . HOH F 3 .   ? 4.814  -11.716 15.197 1.00 29.66  ? 493 HOH A O   1 
HETATM 2065 O  O   . HOH F 3 .   ? 23.534 -24.053 27.491 1.00 32.39  ? 494 HOH A O   1 
HETATM 2066 O  O   . HOH F 3 .   ? 15.835 -1.547  31.509 1.00 29.26  ? 495 HOH A O   1 
HETATM 2067 O  O   . HOH F 3 .   ? 1.319  -13.557 35.219 1.00 42.02  ? 496 HOH A O   1 
HETATM 2068 O  O   . HOH F 3 .   ? 3.364  -14.243 34.645 1.00 37.24  ? 497 HOH A O   1 
HETATM 2069 O  O   . HOH F 3 .   ? 20.345 -2.683  42.641 1.00 33.61  ? 498 HOH A O   1 
HETATM 2070 O  O   . HOH F 3 .   ? 27.506 4.841   28.026 1.00 49.11  ? 499 HOH A O   1 
HETATM 2071 O  O   . HOH F 3 .   ? 30.624 -10.480 13.998 1.00 32.25  ? 500 HOH A O   1 
HETATM 2072 O  O   . HOH F 3 .   ? -1.406 -9.200  31.375 1.00 43.09  ? 501 HOH A O   1 
HETATM 2073 O  O   . HOH F 3 .   ? -2.804 -0.787  26.147 1.00 51.08  ? 502 HOH A O   1 
HETATM 2074 O  O   . HOH F 3 .   ? 7.307  -18.677 19.393 1.00 31.68  ? 503 HOH A O   1 
HETATM 2075 O  O   . HOH F 3 .   ? 15.448 -15.585 10.153 1.00 42.68  ? 504 HOH A O   1 
HETATM 2076 O  O   . HOH F 3 .   ? 17.489 -5.471  5.196  1.00 49.87  ? 505 HOH A O   1 
HETATM 2077 O  O   . HOH F 3 .   ? -0.639 -11.239 27.943 1.00 40.74  ? 506 HOH A O   1 
HETATM 2078 O  O   . HOH F 3 .   ? 30.026 -15.251 14.852 1.00 35.26  ? 507 HOH A O   1 
HETATM 2079 O  O   . HOH F 3 .   ? 20.543 -9.278  11.431 1.00 34.54  ? 508 HOH A O   1 
HETATM 2080 O  O   . HOH F 3 .   ? 31.713 -12.819 14.534 1.00 45.36  ? 509 HOH A O   1 
HETATM 2081 O  O   . HOH F 3 .   ? 28.137 1.251   18.722 1.00 46.81  ? 510 HOH A O   1 
HETATM 2082 O  O   . HOH F 3 .   ? 16.221 -14.288 38.803 1.00 34.41  ? 511 HOH A O   1 
HETATM 2083 O  O   . HOH F 3 .   ? 35.337 -13.343 15.423 1.00 42.77  ? 512 HOH A O   1 
HETATM 2084 O  O   . HOH F 3 .   ? 33.089 -5.052  20.912 1.00 46.55  ? 513 HOH A O   1 
HETATM 2085 O  O   . HOH F 3 .   ? 25.288 -22.743 10.612 1.00 47.53  ? 514 HOH A O   1 
HETATM 2086 O  O   . HOH F 3 .   ? 25.957 5.082   19.040 1.00 49.64  ? 515 HOH A O   1 
HETATM 2087 O  O   . HOH F 3 .   ? 21.956 -25.585 12.362 1.00 49.82  ? 516 HOH A O   1 
HETATM 2088 O  O   . HOH F 3 .   ? 10.193 4.780   6.702  1.00 57.28  ? 517 HOH A O   1 
HETATM 2089 O  O   . HOH F 3 .   ? 20.017 -10.712 43.380 1.00 46.87  ? 518 HOH A O   1 
HETATM 2090 O  O   . HOH F 3 .   ? 6.076  -0.557  18.299 1.00 44.01  ? 519 HOH A O   1 
HETATM 2091 O  O   . HOH F 3 .   ? -2.027 -10.838 37.686 1.00 52.39  ? 520 HOH A O   1 
HETATM 2092 O  O   . HOH F 3 .   ? 21.048 -12.125 41.255 1.00 41.26  ? 521 HOH A O   1 
HETATM 2093 O  O   . HOH F 3 .   ? 32.767 -2.126  22.319 1.00 48.69  ? 522 HOH A O   1 
HETATM 2094 O  O   . HOH F 3 .   ? 23.362 -25.090 9.960  1.00 46.32  ? 523 HOH A O   1 
HETATM 2095 O  O   . HOH F 3 .   ? 3.975  -17.595 35.018 1.00 47.82  ? 524 HOH A O   1 
HETATM 2096 O  O   . HOH F 3 .   ? 10.883 -19.712 35.037 1.00 44.35  ? 525 HOH A O   1 
HETATM 2097 O  O   . HOH F 3 .   ? 3.711  -13.321 26.942 1.00 40.49  ? 526 HOH A O   1 
HETATM 2098 O  O   . HOH F 3 .   ? 34.101 -9.118  22.839 1.00 31.09  ? 527 HOH A O   1 
HETATM 2099 O  O   . HOH F 3 .   ? 28.613 -15.241 12.553 1.00 38.50  ? 528 HOH A O   1 
HETATM 2100 O  O   . HOH F 3 .   ? 32.072 -16.506 15.828 1.00 42.80  ? 529 HOH A O   1 
HETATM 2101 O  O   . HOH F 3 .   ? 23.117 2.074   21.652 1.00 51.69  ? 530 HOH A O   1 
HETATM 2102 O  O   . HOH F 3 .   ? 24.424 8.893   27.030 1.00 54.68  ? 531 HOH A O   1 
HETATM 2103 O  O   . HOH F 3 .   ? 34.346 -8.338  28.956 1.00 40.63  ? 532 HOH A O   1 
HETATM 2104 O  O   . HOH F 3 .   ? -5.090 -4.308  28.690 1.00 49.56  ? 533 HOH A O   1 
HETATM 2105 O  O   . HOH F 3 .   ? 10.263 -21.193 25.917 1.00 43.34  ? 534 HOH A O   1 
HETATM 2106 O  O   . HOH F 3 .   ? 6.354  -18.355 16.542 1.00 40.06  ? 535 HOH A O   1 
HETATM 2107 O  O   . HOH F 3 .   ? 23.450 -26.187 28.649 1.00 49.36  ? 536 HOH A O   1 
HETATM 2108 O  O   . HOH F 3 .   ? 9.098  -19.932 31.700 1.00 47.58  ? 537 HOH A O   1 
HETATM 2109 O  O   . HOH F 3 .   ? 25.363 10.669  23.098 1.00 60.09  ? 538 HOH A O   1 
HETATM 2110 O  O   . HOH F 3 .   ? 18.287 -13.772 9.725  1.00 47.83  ? 539 HOH A O   1 
HETATM 2111 O  O   . HOH F 3 .   ? 4.780  -6.512  14.883 1.00 56.33  ? 540 HOH A O   1 
HETATM 2112 O  O   . HOH F 3 .   ? 34.444 -6.589  21.978 1.00 39.66  ? 541 HOH A O   1 
HETATM 2113 O  O   . HOH F 3 .   ? 7.113  -16.986 35.510 1.00 36.56  ? 542 HOH A O   1 
HETATM 2114 O  O   . HOH F 3 .   ? 35.207 -10.032 25.368 1.00 39.47  ? 543 HOH A O   1 
HETATM 2115 O  O   . HOH F 3 .   ? 25.661 7.226   25.826 1.00 52.67  ? 544 HOH A O   1 
HETATM 2116 O  O   . HOH F 3 .   ? 5.834  -7.303  12.900 1.00 58.45  ? 545 HOH A 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   . LYS A 7   ? 0.7412 0.9502 0.8062 -0.1636 0.1968  0.1460  4   LYS A N   
2    C CA  . LYS A 7   ? 0.7269 0.9217 0.7527 -0.1451 0.1910  0.1495  4   LYS A CA  
3    C C   . LYS A 7   ? 0.7251 0.8776 0.7460 -0.1406 0.1718  0.1410  4   LYS A C   
4    O O   . LYS A 7   ? 0.7446 0.8835 0.7904 -0.1518 0.1641  0.1321  4   LYS A O   
5    C CB  . LYS A 7   ? 0.7446 0.9720 0.7574 -0.1251 0.1890  0.1327  4   LYS A CB  
6    C CG  . LYS A 7   ? 0.8361 1.0975 0.8803 -0.1262 0.1879  0.1136  4   LYS A CG  
7    C CD  . LYS A 7   ? 0.8967 1.1816 0.9260 -0.1038 0.1849  0.0963  4   LYS A CD  
8    C CE  . LYS A 7   ? 0.8549 1.1685 0.9150 -0.1008 0.1808  0.0771  4   LYS A CE  
9    N NZ  . LYS A 7   ? 0.8310 1.1206 0.9069 -0.1035 0.1625  0.0656  4   LYS A NZ  
10   N N   . LEU A 8   ? 0.6670 0.8024 0.6560 -0.1237 0.1639  0.1423  5   LEU A N   
11   C CA  . LEU A 8   ? 0.5292 0.6274 0.5123 -0.1183 0.1477  0.1367  5   LEU A CA  
12   C C   . LEU A 8   ? 0.5207 0.6263 0.5011 -0.1037 0.1330  0.1133  5   LEU A C   
13   O O   . LEU A 8   ? 0.4703 0.6017 0.4403 -0.0924 0.1344  0.1048  5   LEU A O   
14   C CB  . LEU A 8   ? 0.6071 0.6816 0.5596 -0.1098 0.1480  0.1554  5   LEU A CB  
15   C CG  . LEU A 8   ? 0.7018 0.7525 0.6594 -0.1247 0.1595  0.1803  5   LEU A CG  
16   C CD1 . LEU A 8   ? 0.7127 0.7365 0.6414 -0.1135 0.1570  0.1989  5   LEU A CD1 
17   C CD2 . LEU A 8   ? 0.6700 0.6960 0.6586 -0.1404 0.1545  0.1725  5   LEU A CD2 
18   N N   . PRO A 9   ? 0.5000 0.5828 0.4897 -0.1036 0.1194  0.1024  6   PRO A N   
19   C CA  . PRO A 9   ? 0.4686 0.5572 0.4574 -0.0913 0.1065  0.0827  6   PRO A CA  
20   C C   . PRO A 9   ? 0.4801 0.5676 0.4413 -0.0748 0.1011  0.0812  6   PRO A C   
21   O O   . PRO A 9   ? 0.4677 0.5426 0.4085 -0.0711 0.1024  0.0946  6   PRO A O   
22   C CB  . PRO A 9   ? 0.4451 0.5070 0.4456 -0.0955 0.0953  0.0763  6   PRO A CB  
23   C CG  . PRO A 9   ? 0.4979 0.5507 0.5164 -0.1135 0.1030  0.0854  6   PRO A CG  
24   C CD  . PRO A 9   ? 0.4689 0.5209 0.4724 -0.1155 0.1162  0.1065  6   PRO A CD  
25   N N   . LYS A 10  ? 0.4283 0.5290 0.3898 -0.0650 0.0944  0.0645  7   LYS A N   
26   C CA  . LYS A 10  ? 0.4431 0.5446 0.3836 -0.0508 0.0874  0.0571  7   LYS A CA  
27   C C   . LYS A 10  ? 0.4252 0.5136 0.3740 -0.0464 0.0737  0.0433  7   LYS A C   
28   O O   . LYS A 10  ? 0.4207 0.5071 0.3895 -0.0518 0.0711  0.0378  7   LYS A O   
29   C CB  . LYS A 10  ? 0.3983 0.5284 0.3324 -0.0431 0.0941  0.0486  7   LYS A CB  
30   C CG  . LYS A 10  ? 0.4962 0.6454 0.4153 -0.0441 0.1088  0.0616  7   LYS A CG  
31   C CD  . LYS A 10  ? 0.5681 0.7015 0.4665 -0.0455 0.1101  0.0809  7   LYS A CD  
32   C CE  . LYS A 10  ? 0.7214 0.8752 0.6068 -0.0482 0.1271  0.0974  7   LYS A CE  
33   N NZ  . LYS A 10  ? 0.8275 0.9628 0.7125 -0.0591 0.1342  0.1222  7   LYS A NZ  
34   N N   . PRO A 11  ? 0.4076 0.4892 0.3419 -0.0369 0.0648  0.0376  8   PRO A N   
35   C CA  . PRO A 11  ? 0.3501 0.4230 0.2934 -0.0331 0.0538  0.0247  8   PRO A CA  
36   C C   . PRO A 11  ? 0.4068 0.4934 0.3641 -0.0307 0.0551  0.0127  8   PRO A C   
37   O O   . PRO A 11  ? 0.3884 0.4942 0.3445 -0.0282 0.0632  0.0102  8   PRO A O   
38   C CB  . PRO A 11  ? 0.3952 0.4659 0.3209 -0.0244 0.0463  0.0198  8   PRO A CB  
39   C CG  . PRO A 11  ? 0.4200 0.4918 0.3271 -0.0239 0.0505  0.0339  8   PRO A CG  
40   C CD  . PRO A 11  ? 0.4224 0.5060 0.3319 -0.0299 0.0641  0.0429  8   PRO A CD  
41   N N   . PHE A 12  ? 0.3702 0.4482 0.3407 -0.0303 0.0477  0.0061  9   PHE A N   
42   C CA  . PHE A 12  ? 0.3483 0.4370 0.3311 -0.0252 0.0473  -0.0041 9   PHE A CA  
43   C C   . PHE A 12  ? 0.3171 0.3921 0.3000 -0.0189 0.0378  -0.0123 9   PHE A C   
44   O O   . PHE A 12  ? 0.3480 0.4081 0.3270 -0.0209 0.0315  -0.0096 9   PHE A O   
45   C CB  . PHE A 12  ? 0.3245 0.4224 0.3273 -0.0313 0.0491  -0.0024 9   PHE A CB  
46   C CG  . PHE A 12  ? 0.3008 0.3836 0.3099 -0.0364 0.0417  -0.0001 9   PHE A CG  
47   C CD1 . PHE A 12  ? 0.2857 0.3604 0.2981 -0.0308 0.0337  -0.0052 9   PHE A CD1 
48   C CD2 . PHE A 12  ? 0.3074 0.3842 0.3194 -0.0467 0.0438  0.0070  9   PHE A CD2 
49   C CE1 . PHE A 12  ? 0.2832 0.3477 0.2991 -0.0345 0.0282  -0.0034 9   PHE A CE1 
50   C CE2 . PHE A 12  ? 0.2815 0.3455 0.2981 -0.0502 0.0373  0.0064  9   PHE A CE2 
51   C CZ  . PHE A 12  ? 0.2740 0.3340 0.2916 -0.0436 0.0297  0.0011  9   PHE A CZ  
52   N N   . PHE A 13  ? 0.3026 0.3831 0.2918 -0.0110 0.0375  -0.0218 10  PHE A N   
53   C CA  . PHE A 13  ? 0.3410 0.4063 0.3312 -0.0053 0.0299  -0.0293 10  PHE A CA  
54   C C   . PHE A 13  ? 0.3219 0.3922 0.3270 0.0018  0.0301  -0.0335 10  PHE A C   
55   O O   . PHE A 13  ? 0.3573 0.4386 0.3639 0.0098  0.0347  -0.0411 10  PHE A O   
56   C CB  . PHE A 13  ? 0.3710 0.4337 0.3473 -0.0004 0.0289  -0.0388 10  PHE A CB  
57   C CG  . PHE A 13  ? 0.3845 0.4289 0.3630 0.0021  0.0208  -0.0470 10  PHE A CG  
58   C CD1 . PHE A 13  ? 0.3643 0.3947 0.3524 -0.0019 0.0152  -0.0412 10  PHE A CD1 
59   C CD2 . PHE A 13  ? 0.4104 0.4520 0.3812 0.0078  0.0192  -0.0610 10  PHE A CD2 
60   C CE1 . PHE A 13  ? 0.3264 0.3401 0.3186 -0.0017 0.0090  -0.0470 10  PHE A CE1 
61   C CE2 . PHE A 13  ? 0.4221 0.4449 0.3977 0.0078  0.0118  -0.0692 10  PHE A CE2 
62   C CZ  . PHE A 13  ? 0.3856 0.3943 0.3731 0.0022  0.0071  -0.0608 10  PHE A CZ  
63   N N   . PHE A 14  ? 0.3364 0.4009 0.3515 0.0002  0.0254  -0.0282 11  PHE A N   
64   C CA  . PHE A 14  ? 0.3120 0.3822 0.3406 0.0082  0.0241  -0.0295 11  PHE A CA  
65   C C   . PHE A 14  ? 0.3564 0.4044 0.3855 0.0137  0.0183  -0.0311 11  PHE A C   
66   O O   . PHE A 14  ? 0.3097 0.3456 0.3378 0.0088  0.0138  -0.0246 11  PHE A O   
67   C CB  . PHE A 14  ? 0.3022 0.3840 0.3405 0.0033  0.0223  -0.0225 11  PHE A CB  
68   C CG  . PHE A 14  ? 0.2797 0.3796 0.3206 -0.0058 0.0279  -0.0202 11  PHE A CG  
69   C CD1 . PHE A 14  ? 0.2991 0.4139 0.3391 -0.0051 0.0362  -0.0232 11  PHE A CD1 
70   C CD2 . PHE A 14  ? 0.3064 0.4084 0.3512 -0.0153 0.0254  -0.0154 11  PHE A CD2 
71   C CE1 . PHE A 14  ? 0.3096 0.4403 0.3537 -0.0152 0.0427  -0.0187 11  PHE A CE1 
72   C CE2 . PHE A 14  ? 0.3019 0.4168 0.3517 -0.0254 0.0308  -0.0133 11  PHE A CE2 
73   C CZ  . PHE A 14  ? 0.2940 0.4231 0.3444 -0.0261 0.0399  -0.0136 11  PHE A CZ  
74   N N   . GLU A 15  ? 0.3664 0.4088 0.3979 0.0240  0.0191  -0.0396 12  GLU A N   
75   C CA  . GLU A 15  ? 0.3639 0.3807 0.3970 0.0277  0.0144  -0.0417 12  GLU A CA  
76   C C   . GLU A 15  ? 0.3670 0.3803 0.4120 0.0380  0.0124  -0.0362 12  GLU A C   
77   O O   . GLU A 15  ? 0.3470 0.3723 0.3996 0.0495  0.0151  -0.0405 12  GLU A O   
78   C CB  . GLU A 15  ? 0.3626 0.3697 0.3902 0.0326  0.0156  -0.0563 12  GLU A CB  
79   C CG  . GLU A 15  ? 0.4170 0.4254 0.4307 0.0233  0.0150  -0.0608 12  GLU A CG  
80   C CD  . GLU A 15  ? 0.4657 0.4656 0.4725 0.0281  0.0145  -0.0776 12  GLU A CD  
81   O OE1 . GLU A 15  ? 0.4814 0.4581 0.4919 0.0262  0.0089  -0.0830 12  GLU A OE1 
82   O OE2 . GLU A 15  ? 0.4643 0.4811 0.4623 0.0334  0.0199  -0.0859 12  GLU A OE2 
83   N N   . GLU A 16  ? 0.3490 0.3478 0.3957 0.0349  0.0081  -0.0258 13  GLU A N   
84   C CA  . GLU A 16  ? 0.3947 0.3860 0.4500 0.0455  0.0057  -0.0177 13  GLU A CA  
85   C C   . GLU A 16  ? 0.4268 0.3865 0.4828 0.0435  0.0035  -0.0134 13  GLU A C   
86   O O   . GLU A 16  ? 0.4388 0.3787 0.4968 0.0459  0.0039  -0.0233 13  GLU A O   
87   C CB  . GLU A 16  ? 0.4002 0.4105 0.4565 0.0446  0.0032  -0.0062 13  GLU A CB  
88   C CG  . GLU A 16  ? 0.4289 0.4708 0.4891 0.0447  0.0050  -0.0105 13  GLU A CG  
89   C CD  . GLU A 16  ? 0.4692 0.5237 0.5410 0.0601  0.0063  -0.0150 13  GLU A CD  
90   O OE1 . GLU A 16  ? 0.4791 0.5513 0.5542 0.0608  0.0114  -0.0243 13  GLU A OE1 
91   O OE2 . GLU A 16  ? 0.4806 0.5260 0.5579 0.0726  0.0029  -0.0087 13  GLU A OE2 
92   N N   . GLY A 17  ? 0.4123 0.3675 0.4670 0.0385  0.0015  0.0006  14  GLY A N   
93   C CA  . GLY A 17  ? 0.4061 0.3334 0.4638 0.0348  0.0009  0.0074  14  GLY A CA  
94   C C   . GLY A 17  ? 0.4126 0.3335 0.4674 0.0197  0.0009  0.0019  14  GLY A C   
95   O O   . GLY A 17  ? 0.4193 0.3550 0.4680 0.0138  0.0010  -0.0071 14  GLY A O   
96   N N   . LYS A 18  ? 0.4056 0.3053 0.4661 0.0133  0.0008  0.0089  15  LYS A N   
97   C CA  . LYS A 18  ? 0.4189 0.3145 0.4807 -0.0007 -0.0001 0.0023  15  LYS A CA  
98   C C   . LYS A 18  ? 0.4138 0.3286 0.4703 -0.0095 0.0006  0.0103  15  LYS A C   
99   O O   . LYS A 18  ? 0.4403 0.3593 0.4975 -0.0193 -0.0008 0.0042  15  LYS A O   
100  C CB  . LYS A 18  ? 0.4643 0.3305 0.5383 -0.0065 -0.0002 0.0045  15  LYS A CB  
101  C CG  . LYS A 18  ? 0.5752 0.4194 0.6543 0.0007  -0.0017 -0.0107 15  LYS A CG  
102  C CD  . LYS A 18  ? 0.6905 0.5322 0.7704 -0.0089 -0.0054 -0.0310 15  LYS A CD  
103  C CE  . LYS A 18  ? 0.7272 0.5464 0.8104 -0.0007 -0.0067 -0.0491 15  LYS A CE  
104  N NZ  . LYS A 18  ? 0.8425 0.6339 0.9383 -0.0123 -0.0102 -0.0599 15  LYS A NZ  
105  N N   . ARG A 19  ? 0.3507 0.2789 0.4019 -0.0052 0.0021  0.0225  16  ARG A N   
106  C CA  . ARG A 19  ? 0.3336 0.2797 0.3786 -0.0117 0.0030  0.0266  16  ARG A CA  
107  C C   . ARG A 19  ? 0.3387 0.3012 0.3763 -0.0111 0.0018  0.0160  16  ARG A C   
108  O O   . ARG A 19  ? 0.3514 0.3215 0.3865 -0.0039 0.0015  0.0130  16  ARG A O   
109  C CB  . ARG A 19  ? 0.3341 0.2890 0.3741 -0.0073 0.0047  0.0411  16  ARG A CB  
110  C CG  . ARG A 19  ? 0.3505 0.2892 0.3958 -0.0058 0.0070  0.0557  16  ARG A CG  
111  C CD  . ARG A 19  ? 0.3986 0.3515 0.4341 0.0007  0.0081  0.0695  16  ARG A CD  
112  N NE  . ARG A 19  ? 0.4137 0.3522 0.4513 0.0039  0.0111  0.0875  16  ARG A NE  
113  C CZ  . ARG A 19  ? 0.4613 0.4112 0.4885 0.0103  0.0125  0.1026  16  ARG A CZ  
114  N NH1 . ARG A 19  ? 0.3839 0.3596 0.3987 0.0139  0.0102  0.0992  16  ARG A NH1 
115  N NH2 . ARG A 19  ? 0.4353 0.3699 0.4641 0.0131  0.0161  0.1214  16  ARG A NH2 
116  N N   . ALA A 20  ? 0.3326 0.3015 0.3679 -0.0185 0.0013  0.0116  17  ALA A N   
117  C CA  . ALA A 20  ? 0.2933 0.2735 0.3214 -0.0184 0.0008  0.0035  17  ALA A CA  
118  C C   . ALA A 20  ? 0.3133 0.3049 0.3362 -0.0217 0.0017  0.0074  17  ALA A C   
119  O O   . ALA A 20  ? 0.3089 0.3014 0.3341 -0.0251 0.0022  0.0129  17  ALA A O   
120  C CB  . ALA A 20  ? 0.3232 0.2994 0.3510 -0.0215 -0.0014 -0.0072 17  ALA A CB  
121  N N   . VAL A 21  ? 0.2967 0.2968 0.3135 -0.0206 0.0025  0.0044  18  VAL A N   
122  C CA  . VAL A 21  ? 0.2894 0.2957 0.3015 -0.0230 0.0033  0.0063  18  VAL A CA  
123  C C   . VAL A 21  ? 0.3249 0.3328 0.3317 -0.0247 0.0037  0.0023  18  VAL A C   
124  O O   . VAL A 21  ? 0.3109 0.3219 0.3158 -0.0236 0.0052  -0.0010 18  VAL A O   
125  C CB  . VAL A 21  ? 0.2782 0.2915 0.2886 -0.0214 0.0040  0.0080  18  VAL A CB  
126  C CG1 . VAL A 21  ? 0.3101 0.3251 0.3160 -0.0240 0.0049  0.0076  18  VAL A CG1 
127  C CG2 . VAL A 21  ? 0.2990 0.3133 0.3113 -0.0178 0.0033  0.0138  18  VAL A CG2 
128  N N   . LEU A 22  ? 0.2661 0.2739 0.2707 -0.0263 0.0027  0.0038  19  LEU A N   
129  C CA  . LEU A 22  ? 0.2817 0.2906 0.2791 -0.0264 0.0030  0.0034  19  LEU A CA  
130  C C   . LEU A 22  ? 0.3264 0.3334 0.3212 -0.0271 0.0057  0.0066  19  LEU A C   
131  O O   . LEU A 22  ? 0.3283 0.3338 0.3250 -0.0263 0.0056  0.0084  19  LEU A O   
132  C CB  . LEU A 22  ? 0.2604 0.2715 0.2578 -0.0261 -0.0007 0.0037  19  LEU A CB  
133  C CG  . LEU A 22  ? 0.2903 0.3037 0.2786 -0.0240 -0.0016 0.0058  19  LEU A CG  
134  C CD1 . LEU A 22  ? 0.3035 0.3197 0.2825 -0.0235 -0.0008 0.0024  19  LEU A CD1 
135  C CD2 . LEU A 22  ? 0.2987 0.3189 0.2904 -0.0225 -0.0069 0.0061  19  LEU A CD2 
136  N N   . LEU A 23  ? 0.3025 0.3100 0.2940 -0.0289 0.0088  0.0068  20  LEU A N   
137  C CA  . LEU A 23  ? 0.3079 0.3114 0.2998 -0.0321 0.0115  0.0085  20  LEU A CA  
138  C C   . LEU A 23  ? 0.3563 0.3524 0.3415 -0.0323 0.0136  0.0142  20  LEU A C   
139  O O   . LEU A 23  ? 0.3409 0.3403 0.3208 -0.0331 0.0162  0.0170  20  LEU A O   
140  C CB  . LEU A 23  ? 0.3006 0.3117 0.2976 -0.0358 0.0141  0.0059  20  LEU A CB  
141  C CG  . LEU A 23  ? 0.2996 0.3185 0.3028 -0.0335 0.0115  0.0020  20  LEU A CG  
142  C CD1 . LEU A 23  ? 0.3383 0.3697 0.3485 -0.0355 0.0137  -0.0006 20  LEU A CD1 
143  C CD2 . LEU A 23  ? 0.3427 0.3594 0.3467 -0.0332 0.0090  0.0011  20  LEU A CD2 
144  N N   . LEU A 24  ? 0.3424 0.3287 0.3273 -0.0307 0.0131  0.0163  21  LEU A N   
145  C CA  . LEU A 24  ? 0.3285 0.3048 0.3071 -0.0283 0.0145  0.0238  21  LEU A CA  
146  C C   . LEU A 24  ? 0.3801 0.3415 0.3611 -0.0332 0.0186  0.0254  21  LEU A C   
147  O O   . LEU A 24  ? 0.3585 0.3139 0.3447 -0.0340 0.0178  0.0192  21  LEU A O   
148  C CB  . LEU A 24  ? 0.3249 0.3003 0.3030 -0.0204 0.0106  0.0254  21  LEU A CB  
149  C CG  . LEU A 24  ? 0.3438 0.3338 0.3230 -0.0178 0.0059  0.0230  21  LEU A CG  
150  C CD1 . LEU A 24  ? 0.3312 0.3251 0.3138 -0.0107 0.0023  0.0248  21  LEU A CD1 
151  C CD2 . LEU A 24  ? 0.3753 0.3720 0.3460 -0.0182 0.0051  0.0248  21  LEU A CD2 
152  N N   . HIS A 25  ? 0.3666 0.3219 0.3435 -0.0369 0.0233  0.0336  22  HIS A N   
153  C CA  . HIS A 25  ? 0.3733 0.3123 0.3552 -0.0444 0.0279  0.0357  22  HIS A CA  
154  C C   . HIS A 25  ? 0.3858 0.3022 0.3640 -0.0381 0.0278  0.0422  22  HIS A C   
155  O O   . HIS A 25  ? 0.3930 0.3108 0.3659 -0.0272 0.0239  0.0447  22  HIS A O   
156  C CB  . HIS A 25  ? 0.3848 0.3288 0.3665 -0.0529 0.0348  0.0430  22  HIS A CB  
157  C CG  . HIS A 25  ? 0.3975 0.3405 0.3656 -0.0480 0.0379  0.0569  22  HIS A CG  
158  N ND1 . HIS A 25  ? 0.4120 0.3340 0.3746 -0.0461 0.0409  0.0697  22  HIS A ND1 
159  C CD2 . HIS A 25  ? 0.4064 0.3671 0.3641 -0.0440 0.0384  0.0598  22  HIS A CD2 
160  C CE1 . HIS A 25  ? 0.4680 0.3971 0.4161 -0.0408 0.0429  0.0816  22  HIS A CE1 
161  N NE2 . HIS A 25  ? 0.4246 0.3780 0.3690 -0.0396 0.0413  0.0746  22  HIS A NE2 
162  N N   . GLY A 26  ? 0.4052 0.3006 0.3882 -0.0449 0.0322  0.0446  23  GLY A N   
163  C CA  . GLY A 26  ? 0.4509 0.3196 0.4326 -0.0384 0.0325  0.0491  23  GLY A CA  
164  C C   . GLY A 26  ? 0.4693 0.3224 0.4433 -0.0371 0.0377  0.0681  23  GLY A C   
165  O O   . GLY A 26  ? 0.4495 0.3137 0.4183 -0.0426 0.0420  0.0776  23  GLY A O   
166  N N   . PHE A 27  ? 0.4746 0.3016 0.4472 -0.0285 0.0376  0.0740  24  PHE A N   
167  C CA  . PHE A 27  ? 0.5160 0.3233 0.4807 -0.0255 0.0426  0.0946  24  PHE A CA  
168  C C   . PHE A 27  ? 0.5469 0.3387 0.5185 -0.0433 0.0515  0.1006  24  PHE A C   
169  O O   . PHE A 27  ? 0.5691 0.3450 0.5547 -0.0542 0.0528  0.0888  24  PHE A O   
170  C CB  . PHE A 27  ? 0.5099 0.2897 0.4744 -0.0108 0.0404  0.0983  24  PHE A CB  
171  C CG  . PHE A 27  ? 0.5808 0.3324 0.5384 -0.0070 0.0457  0.1208  24  PHE A CG  
172  C CD1 . PHE A 27  ? 0.5925 0.3578 0.5344 -0.0010 0.0466  0.1405  24  PHE A CD1 
173  C CD2 . PHE A 27  ? 0.6259 0.3359 0.5918 -0.0083 0.0497  0.1223  24  PHE A CD2 
174  C CE1 . PHE A 27  ? 0.6251 0.3642 0.5586 0.0039  0.0520  0.1644  24  PHE A CE1 
175  C CE2 . PHE A 27  ? 0.6765 0.3561 0.6365 -0.0042 0.0552  0.1454  24  PHE A CE2 
176  C CZ  . PHE A 27  ? 0.6874 0.3821 0.6305 0.0023  0.0566  0.1682  24  PHE A CZ  
177  N N   . THR A 28  ? 0.5453 0.3447 0.5076 -0.0468 0.0578  0.1184  25  THR A N   
178  C CA  . THR A 28  ? 0.5347 0.3301 0.5037 -0.0648 0.0682  0.1271  25  THR A CA  
179  C C   . THR A 28  ? 0.5376 0.3618 0.5187 -0.0784 0.0687  0.1111  25  THR A C   
180  O O   . THR A 28  ? 0.5859 0.4140 0.5761 -0.0940 0.0773  0.1165  25  THR A O   
181  C CB  . THR A 28  ? 0.6125 0.3660 0.5940 -0.0746 0.0738  0.1319  25  THR A CB  
182  O OG1 . THR A 28  ? 0.6286 0.3762 0.6275 -0.0829 0.0692  0.1081  25  THR A OG1 
183  C CG2 . THR A 28  ? 0.6522 0.3727 0.6238 -0.0581 0.0725  0.1464  25  THR A CG2 
184  N N   . GLY A 29  ? 0.4707 0.3165 0.4532 -0.0727 0.0601  0.0932  26  GLY A N   
185  C CA  . GLY A 29  ? 0.4961 0.3703 0.4885 -0.0820 0.0598  0.0801  26  GLY A CA  
186  C C   . GLY A 29  ? 0.5033 0.4072 0.4847 -0.0781 0.0622  0.0858  26  GLY A C   
187  O O   . GLY A 29  ? 0.4790 0.3828 0.4446 -0.0713 0.0656  0.1011  26  GLY A O   
188  N N   . ASN A 30  ? 0.4693 0.3993 0.4584 -0.0811 0.0600  0.0727  27  ASN A N   
189  C CA  . ASN A 30  ? 0.4570 0.4148 0.4371 -0.0760 0.0615  0.0732  27  ASN A CA  
190  C C   . ASN A 30  ? 0.4240 0.4019 0.4150 -0.0760 0.0560  0.0560  27  ASN A C   
191  O O   . ASN A 30  ? 0.4011 0.3730 0.4032 -0.0789 0.0506  0.0456  27  ASN A O   
192  C CB  . ASN A 30  ? 0.4334 0.4021 0.4125 -0.0842 0.0736  0.0860  27  ASN A CB  
193  C CG  . ASN A 30  ? 0.4709 0.4418 0.4724 -0.1012 0.0797  0.0833  27  ASN A CG  
194  O OD1 . ASN A 30  ? 0.4412 0.4297 0.4574 -0.1047 0.0759  0.0687  27  ASN A OD1 
195  N ND2 . ASN A 30  ? 0.4743 0.4283 0.4798 -0.1121 0.0887  0.0979  27  ASN A ND2 
196  N N   . SER A 31  ? 0.3943 0.3959 0.3811 -0.0717 0.0574  0.0531  28  SER A N   
197  C CA  . SER A 31  ? 0.3735 0.3914 0.3690 -0.0686 0.0517  0.0389  28  SER A CA  
198  C C   . SER A 31  ? 0.3715 0.3992 0.3873 -0.0789 0.0528  0.0322  28  SER A C   
199  O O   . SER A 31  ? 0.3442 0.3800 0.3675 -0.0759 0.0461  0.0215  28  SER A O   
200  C CB  . SER A 31  ? 0.3797 0.4178 0.3670 -0.0611 0.0538  0.0366  28  SER A CB  
201  O OG  . SER A 31  ? 0.3676 0.4245 0.3623 -0.0674 0.0636  0.0396  28  SER A OG  
202  N N   . SER A 32  ? 0.3616 0.3899 0.3873 -0.0913 0.0608  0.0387  29  SER A N   
203  C CA  . SER A 32  ? 0.3689 0.4108 0.4168 -0.1024 0.0605  0.0306  29  SER A CA  
204  C C   . SER A 32  ? 0.4042 0.4308 0.4576 -0.1044 0.0510  0.0204  29  SER A C   
205  O O   . SER A 32  ? 0.3457 0.3878 0.4146 -0.1097 0.0466  0.0098  29  SER A O   
206  C CB  . SER A 32  ? 0.4000 0.4446 0.4601 -0.1181 0.0715  0.0399  29  SER A CB  
207  O OG  . SER A 32  ? 0.4405 0.4529 0.4999 -0.1260 0.0723  0.0460  29  SER A OG  
208  N N   . ASP A 33  ? 0.3778 0.3771 0.4187 -0.0992 0.0477  0.0228  30  ASP A N   
209  C CA  . ASP A 33  ? 0.3784 0.3641 0.4222 -0.0994 0.0398  0.0121  30  ASP A CA  
210  C C   . ASP A 33  ? 0.3655 0.3649 0.4054 -0.0886 0.0314  0.0025  30  ASP A C   
211  O O   . ASP A 33  ? 0.3720 0.3676 0.4139 -0.0884 0.0251  -0.0075 30  ASP A O   
212  C CB  . ASP A 33  ? 0.3896 0.3432 0.4223 -0.0950 0.0399  0.0177  30  ASP A CB  
213  C CG  . ASP A 33  ? 0.4882 0.4208 0.5255 -0.1058 0.0479  0.0283  30  ASP A CG  
214  O OD1 . ASP A 33  ? 0.4826 0.4157 0.5366 -0.1208 0.0503  0.0237  30  ASP A OD1 
215  O OD2 . ASP A 33  ? 0.4979 0.4134 0.5226 -0.0995 0.0516  0.0418  30  ASP A OD2 
216  N N   . VAL A 34  ? 0.3496 0.3632 0.3829 -0.0795 0.0314  0.0055  31  VAL A N   
217  C CA  . VAL A 34  ? 0.3135 0.3363 0.3433 -0.0696 0.0245  -0.0007 31  VAL A CA  
218  C C   . VAL A 34  ? 0.3256 0.3726 0.3623 -0.0665 0.0248  -0.0027 31  VAL A C   
219  O O   . VAL A 34  ? 0.3109 0.3642 0.3451 -0.0576 0.0201  -0.0054 31  VAL A O   
220  C CB  . VAL A 34  ? 0.3186 0.3289 0.3343 -0.0595 0.0227  0.0036  31  VAL A CB  
221  C CG1 . VAL A 34  ? 0.3681 0.3572 0.3789 -0.0593 0.0215  0.0040  31  VAL A CG1 
222  C CG2 . VAL A 34  ? 0.3425 0.3538 0.3504 -0.0568 0.0275  0.0114  31  VAL A CG2 
223  N N   . ARG A 35  ? 0.2835 0.3444 0.3297 -0.0733 0.0312  -0.0005 32  ARG A N   
224  C CA  . ARG A 35  ? 0.2802 0.3657 0.3338 -0.0680 0.0325  -0.0029 32  ARG A CA  
225  C C   . ARG A 35  ? 0.2914 0.3942 0.3569 -0.0657 0.0250  -0.0108 32  ARG A C   
226  O O   . ARG A 35  ? 0.2927 0.4067 0.3589 -0.0549 0.0222  -0.0126 32  ARG A O   
227  C CB  . ARG A 35  ? 0.2785 0.3797 0.3413 -0.0760 0.0424  0.0015  32  ARG A CB  
228  C CG  . ARG A 35  ? 0.3003 0.4256 0.3671 -0.0672 0.0462  -0.0006 32  ARG A CG  
229  C CD  . ARG A 35  ? 0.2752 0.4208 0.3520 -0.0754 0.0579  0.0042  32  ARG A CD  
230  N NE  . ARG A 35  ? 0.2818 0.4493 0.3589 -0.0644 0.0630  0.0014  32  ARG A NE  
231  C CZ  . ARG A 35  ? 0.3242 0.4862 0.3832 -0.0561 0.0677  0.0035  32  ARG A CZ  
232  N NH1 . ARG A 35  ? 0.3075 0.4455 0.3472 -0.0575 0.0675  0.0101  32  ARG A NH1 
233  N NH2 . ARG A 35  ? 0.3139 0.4961 0.3742 -0.0452 0.0722  -0.0020 32  ARG A NH2 
234  N N   . GLN A 36  ? 0.2691 0.3738 0.3437 -0.0752 0.0211  -0.0159 33  GLN A N   
235  C CA  . GLN A 36  ? 0.2808 0.4053 0.3644 -0.0722 0.0124  -0.0238 33  GLN A CA  
236  C C   . GLN A 36  ? 0.2689 0.3831 0.3379 -0.0599 0.0056  -0.0236 33  GLN A C   
237  O O   . GLN A 36  ? 0.2708 0.4004 0.3420 -0.0501 0.0006  -0.0243 33  GLN A O   
238  C CB  . GLN A 36  ? 0.2697 0.3983 0.3652 -0.0863 0.0090  -0.0318 33  GLN A CB  
239  C CG  . GLN A 36  ? 0.3226 0.4725 0.4400 -0.0992 0.0149  -0.0322 33  GLN A CG  
240  C CD  . GLN A 36  ? 0.4136 0.5572 0.5432 -0.1175 0.0138  -0.0392 33  GLN A CD  
241  O OE1 . GLN A 36  ? 0.4600 0.5720 0.5801 -0.1229 0.0164  -0.0373 33  GLN A OE1 
242  N NE2 . GLN A 36  ? 0.3899 0.5632 0.5415 -0.1264 0.0092  -0.0481 33  GLN A NE2 
243  N N   . LEU A 37  ? 0.2698 0.3588 0.3246 -0.0595 0.0062  -0.0213 34  LEU A N   
244  C CA  . LEU A 37  ? 0.2923 0.3727 0.3345 -0.0488 0.0022  -0.0190 34  LEU A CA  
245  C C   . LEU A 37  ? 0.2861 0.3677 0.3263 -0.0392 0.0042  -0.0134 34  LEU A C   
246  O O   . LEU A 37  ? 0.2914 0.3774 0.3298 -0.0302 0.0002  -0.0115 34  LEU A O   
247  C CB  . LEU A 37  ? 0.2975 0.3543 0.3281 -0.0501 0.0039  -0.0174 34  LEU A CB  
248  C CG  . LEU A 37  ? 0.3023 0.3499 0.3216 -0.0412 0.0024  -0.0133 34  LEU A CG  
249  C CD1 . LEU A 37  ? 0.3056 0.3658 0.3226 -0.0356 -0.0033 -0.0155 34  LEU A CD1 
250  C CD2 . LEU A 37  ? 0.3055 0.3346 0.3173 -0.0425 0.0044  -0.0129 34  LEU A CD2 
251  N N   . GLY A 38  ? 0.2682 0.3459 0.3084 -0.0407 0.0104  -0.0107 35  GLY A N   
252  C CA  . GLY A 38  ? 0.2947 0.3730 0.3332 -0.0317 0.0119  -0.0089 35  GLY A CA  
253  C C   . GLY A 38  ? 0.2656 0.3636 0.3153 -0.0245 0.0099  -0.0112 35  GLY A C   
254  O O   . GLY A 38  ? 0.2692 0.3635 0.3174 -0.0143 0.0075  -0.0098 35  GLY A O   
255  N N   . ARG A 39  ? 0.2599 0.3794 0.3226 -0.0296 0.0108  -0.0144 36  ARG A N   
256  C CA  . ARG A 39  ? 0.2432 0.3866 0.3191 -0.0213 0.0081  -0.0166 36  ARG A CA  
257  C C   . ARG A 39  ? 0.2830 0.4284 0.3566 -0.0141 -0.0011 -0.0152 36  ARG A C   
258  O O   . ARG A 39  ? 0.2648 0.4172 0.3419 -0.0012 -0.0041 -0.0129 36  ARG A O   
259  C CB  . ARG A 39  ? 0.2280 0.3986 0.3216 -0.0302 0.0105  -0.0206 36  ARG A CB  
260  C CG  . ARG A 39  ? 0.2423 0.4181 0.3395 -0.0350 0.0215  -0.0196 36  ARG A CG  
261  C CD  . ARG A 39  ? 0.2379 0.4198 0.3351 -0.0205 0.0253  -0.0205 36  ARG A CD  
262  N NE  . ARG A 39  ? 0.2472 0.4426 0.3483 -0.0243 0.0364  -0.0205 36  ARG A NE  
263  C CZ  . ARG A 39  ? 0.2399 0.4362 0.3354 -0.0137 0.0423  -0.0228 36  ARG A CZ  
264  N NH1 . ARG A 39  ? 0.2373 0.4190 0.3257 0.0005  0.0377  -0.0259 36  ARG A NH1 
265  N NH2 . ARG A 39  ? 0.2400 0.4521 0.3370 -0.0175 0.0535  -0.0222 36  ARG A NH2 
266  N N   . PHE A 40  ? 0.2463 0.3861 0.3134 -0.0211 -0.0052 -0.0164 37  PHE A N   
267  C CA  . PHE A 40  ? 0.2616 0.4050 0.3224 -0.0138 -0.0132 -0.0144 37  PHE A CA  
268  C C   . PHE A 40  ? 0.3034 0.4264 0.3528 -0.0037 -0.0122 -0.0058 37  PHE A C   
269  O O   . PHE A 40  ? 0.2798 0.4078 0.3289 0.0078  -0.0162 -0.0001 37  PHE A O   
270  C CB  . PHE A 40  ? 0.2733 0.4129 0.3266 -0.0228 -0.0164 -0.0194 37  PHE A CB  
271  C CG  . PHE A 40  ? 0.2957 0.4390 0.3374 -0.0148 -0.0233 -0.0168 37  PHE A CG  
272  C CD1 . PHE A 40  ? 0.3489 0.5189 0.3948 -0.0110 -0.0318 -0.0205 37  PHE A CD1 
273  C CD2 . PHE A 40  ? 0.3847 0.5077 0.4114 -0.0108 -0.0209 -0.0099 37  PHE A CD2 
274  C CE1 . PHE A 40  ? 0.4178 0.5933 0.4492 -0.0023 -0.0378 -0.0166 37  PHE A CE1 
275  C CE2 . PHE A 40  ? 0.3688 0.4972 0.3834 -0.0033 -0.0253 -0.0054 37  PHE A CE2 
276  C CZ  . PHE A 40  ? 0.3553 0.5090 0.3703 0.0014  -0.0336 -0.0083 37  PHE A CZ  
277  N N   . LEU A 41  ? 0.2798 0.3800 0.3210 -0.0081 -0.0071 -0.0042 38  LEU A N   
278  C CA  . LEU A 41  ? 0.2938 0.3750 0.3278 -0.0016 -0.0061 0.0028  38  LEU A CA  
279  C C   . LEU A 41  ? 0.2802 0.3608 0.3213 0.0084  -0.0053 0.0044  38  LEU A C   
280  O O   . LEU A 41  ? 0.3012 0.3723 0.3406 0.0168  -0.0070 0.0114  38  LEU A O   
281  C CB  . LEU A 41  ? 0.3188 0.3812 0.3461 -0.0086 -0.0017 0.0022  38  LEU A CB  
282  C CG  . LEU A 41  ? 0.3250 0.3835 0.3449 -0.0154 -0.0020 0.0014  38  LEU A CG  
283  C CD1 . LEU A 41  ? 0.3278 0.3711 0.3435 -0.0204 0.0019  0.0013  38  LEU A CD1 
284  C CD2 . LEU A 41  ? 0.3794 0.4380 0.3922 -0.0109 -0.0047 0.0068  38  LEU A CD2 
285  N N   . GLN A 42  ? 0.2663 0.3564 0.3158 0.0080  -0.0018 -0.0018 39  GLN A N   
286  C CA  . GLN A 42  ? 0.2696 0.3607 0.3266 0.0195  -0.0004 -0.0029 39  GLN A CA  
287  C C   . GLN A 42  ? 0.3157 0.4215 0.3802 0.0316  -0.0060 0.0017  39  GLN A C   
288  O O   . GLN A 42  ? 0.3027 0.3967 0.3687 0.0438  -0.0069 0.0062  39  GLN A O   
289  C CB  . GLN A 42  ? 0.2671 0.3725 0.3310 0.0169  0.0056  -0.0107 39  GLN A CB  
290  C CG  . GLN A 42  ? 0.2800 0.3953 0.3541 0.0302  0.0074  -0.0142 39  GLN A CG  
291  C CD  . GLN A 42  ? 0.2969 0.4276 0.3752 0.0269  0.0155  -0.0214 39  GLN A CD  
292  O OE1 . GLN A 42  ? 0.2721 0.4214 0.3554 0.0163  0.0181  -0.0217 39  GLN A OE1 
293  N NE2 . GLN A 42  ? 0.2864 0.4085 0.3619 0.0351  0.0200  -0.0273 39  GLN A NE2 
294  N N   . LYS A 43  ? 0.2907 0.4217 0.3603 0.0286  -0.0104 0.0005  40  LYS A N   
295  C CA  . LYS A 43  ? 0.3120 0.4620 0.3876 0.0409  -0.0175 0.0052  40  LYS A CA  
296  C C   . LYS A 43  ? 0.3117 0.4439 0.3745 0.0479  -0.0213 0.0169  40  LYS A C   
297  O O   . LYS A 43  ? 0.3071 0.4422 0.3723 0.0628  -0.0252 0.0251  40  LYS A O   
298  C CB  . LYS A 43  ? 0.2830 0.4648 0.3658 0.0335  -0.0229 -0.0007 40  LYS A CB  
299  C CG  . LYS A 43  ? 0.3820 0.5860 0.4657 0.0438  -0.0330 0.0039  40  LYS A CG  
300  C CD  . LYS A 43  ? 0.4151 0.6473 0.5037 0.0325  -0.0393 -0.0053 40  LYS A CD  
301  C CE  . LYS A 43  ? 0.5009 0.7253 0.5698 0.0295  -0.0446 -0.0032 40  LYS A CE  
302  N NZ  . LYS A 43  ? 0.5269 0.7744 0.5989 0.0177  -0.0513 -0.0156 40  LYS A NZ  
303  N N   . LYS A 44  ? 0.3093 0.4234 0.3588 0.0382  -0.0193 0.0191  41  LYS A N   
304  C CA  . LYS A 44  ? 0.3581 0.4559 0.3955 0.0424  -0.0203 0.0313  41  LYS A CA  
305  C C   . LYS A 44  ? 0.4057 0.4725 0.4432 0.0446  -0.0151 0.0368  41  LYS A C   
306  O O   . LYS A 44  ? 0.4022 0.4536 0.4321 0.0460  -0.0143 0.0483  41  LYS A O   
307  C CB  . LYS A 44  ? 0.3495 0.4467 0.3746 0.0312  -0.0200 0.0298  41  LYS A CB  
308  C CG  . LYS A 44  ? 0.3402 0.4651 0.3636 0.0289  -0.0264 0.0232  41  LYS A CG  
309  C CD  . LYS A 44  ? 0.3878 0.5315 0.4092 0.0427  -0.0337 0.0314  41  LYS A CD  
310  C CE  . LYS A 44  ? 0.3605 0.5319 0.3763 0.0400  -0.0415 0.0240  41  LYS A CE  
311  N NZ  . LYS A 44  ? 0.4287 0.6216 0.4403 0.0552  -0.0499 0.0332  41  LYS A NZ  
312  N N   . GLY A 45  ? 0.3183 0.3766 0.3641 0.0443  -0.0114 0.0284  42  GLY A N   
313  C CA  . GLY A 45  ? 0.3690 0.3987 0.4167 0.0470  -0.0079 0.0298  42  GLY A CA  
314  C C   . GLY A 45  ? 0.3308 0.3433 0.3737 0.0340  -0.0041 0.0252  42  GLY A C   
315  O O   . GLY A 45  ? 0.3579 0.3466 0.4029 0.0339  -0.0024 0.0256  42  GLY A O   
316  N N   . TYR A 46  ? 0.2902 0.3137 0.3277 0.0233  -0.0034 0.0205  43  TYR A N   
317  C CA  . TYR A 46  ? 0.2882 0.2997 0.3213 0.0127  -0.0008 0.0168  43  TYR A CA  
318  C C   . TYR A 46  ? 0.3203 0.3349 0.3546 0.0099  0.0015  0.0054  43  TYR A C   
319  O O   . TYR A 46  ? 0.3058 0.3379 0.3425 0.0107  0.0024  0.0009  43  TYR A O   
320  C CB  . TYR A 46  ? 0.3098 0.3295 0.3355 0.0048  -0.0011 0.0193  43  TYR A CB  
321  C CG  . TYR A 46  ? 0.3280 0.3442 0.3494 0.0064  -0.0015 0.0307  43  TYR A CG  
322  C CD1 . TYR A 46  ? 0.3537 0.3816 0.3721 0.0141  -0.0045 0.0376  43  TYR A CD1 
323  C CD2 . TYR A 46  ? 0.3305 0.3345 0.3509 0.0004  0.0011  0.0352  43  TYR A CD2 
324  C CE1 . TYR A 46  ? 0.3386 0.3652 0.3501 0.0164  -0.0039 0.0499  43  TYR A CE1 
325  C CE2 . TYR A 46  ? 0.3294 0.3327 0.3460 0.0015  0.0027  0.0474  43  TYR A CE2 
326  C CZ  . TYR A 46  ? 0.3538 0.3676 0.3645 0.0098  0.0006  0.0553  43  TYR A CZ  
327  O OH  . TYR A 46  ? 0.3301 0.3450 0.3340 0.0116  0.0030  0.0691  43  TYR A OH  
328  N N   . THR A 47  ? 0.2904 0.2901 0.3233 0.0062  0.0026  0.0009  44  THR A N   
329  C CA  . THR A 47  ? 0.3138 0.3175 0.3432 0.0033  0.0048  -0.0090 44  THR A CA  
330  C C   . THR A 47  ? 0.3066 0.3179 0.3292 -0.0056 0.0054  -0.0073 44  THR A C   
331  O O   . THR A 47  ? 0.3245 0.3319 0.3453 -0.0100 0.0040  -0.0016 44  THR A O   
332  C CB  . THR A 47  ? 0.3090 0.2953 0.3384 0.0028  0.0039  -0.0159 44  THR A CB  
333  O OG1 . THR A 47  ? 0.3158 0.2921 0.3519 0.0126  0.0040  -0.0195 44  THR A OG1 
334  C CG2 . THR A 47  ? 0.3063 0.2983 0.3274 -0.0007 0.0050  -0.0256 44  THR A CG2 
335  N N   . SER A 48  ? 0.2967 0.3189 0.3157 -0.0076 0.0084  -0.0115 45  SER A N   
336  C CA  . SER A 48  ? 0.2921 0.3163 0.3046 -0.0150 0.0093  -0.0090 45  SER A CA  
337  C C   . SER A 48  ? 0.3381 0.3660 0.3430 -0.0161 0.0124  -0.0130 45  SER A C   
338  O O   . SER A 48  ? 0.3076 0.3437 0.3128 -0.0121 0.0158  -0.0180 45  SER A O   
339  C CB  . SER A 48  ? 0.3297 0.3637 0.3449 -0.0186 0.0102  -0.0055 45  SER A CB  
340  O OG  . SER A 48  ? 0.3378 0.3863 0.3582 -0.0181 0.0137  -0.0081 45  SER A OG  
341  N N   . TYR A 49  ? 0.2792 0.3028 0.2766 -0.0203 0.0113  -0.0103 46  TYR A N   
342  C CA  . TYR A 49  ? 0.2902 0.3185 0.2770 -0.0209 0.0139  -0.0109 46  TYR A CA  
343  C C   . TYR A 49  ? 0.3403 0.3665 0.3229 -0.0255 0.0152  -0.0025 46  TYR A C   
344  O O   . TYR A 49  ? 0.3479 0.3668 0.3323 -0.0267 0.0117  0.0006  46  TYR A O   
345  C CB  . TYR A 49  ? 0.2937 0.3181 0.2739 -0.0188 0.0093  -0.0169 46  TYR A CB  
346  C CG  . TYR A 49  ? 0.3095 0.3415 0.2751 -0.0181 0.0110  -0.0162 46  TYR A CG  
347  C CD1 . TYR A 49  ? 0.3052 0.3481 0.2644 -0.0157 0.0176  -0.0180 46  TYR A CD1 
348  C CD2 . TYR A 49  ? 0.3533 0.3845 0.3116 -0.0189 0.0066  -0.0124 46  TYR A CD2 
349  C CE1 . TYR A 49  ? 0.3947 0.4463 0.3377 -0.0144 0.0203  -0.0151 46  TYR A CE1 
350  C CE2 . TYR A 49  ? 0.3509 0.3904 0.2934 -0.0166 0.0077  -0.0096 46  TYR A CE2 
351  C CZ  . TYR A 49  ? 0.3746 0.4237 0.3083 -0.0146 0.0149  -0.0104 46  TYR A CZ  
352  O OH  . TYR A 49  ? 0.3928 0.4513 0.3083 -0.0118 0.0170  -0.0054 46  TYR A OH  
353  N N   . ALA A 50  ? 0.3280 0.3604 0.3060 -0.0278 0.0210  0.0015  47  ALA A N   
354  C CA  . ALA A 50  ? 0.3401 0.3662 0.3151 -0.0323 0.0233  0.0104  47  ALA A CA  
355  C C   . ALA A 50  ? 0.3655 0.3940 0.3259 -0.0306 0.0261  0.0162  47  ALA A C   
356  O O   . ALA A 50  ? 0.3621 0.4005 0.3184 -0.0320 0.0332  0.0185  47  ALA A O   
357  C CB  . ALA A 50  ? 0.3586 0.3879 0.3435 -0.0389 0.0283  0.0123  47  ALA A CB  
358  N N   . PRO A 51  ? 0.3481 0.3713 0.3000 -0.0269 0.0210  0.0190  48  PRO A N   
359  C CA  . PRO A 51  ? 0.3821 0.4092 0.3177 -0.0238 0.0228  0.0266  48  PRO A CA  
360  C C   . PRO A 51  ? 0.4037 0.4208 0.3379 -0.0278 0.0291  0.0403  48  PRO A C   
361  O O   . PRO A 51  ? 0.3866 0.3929 0.3329 -0.0331 0.0307  0.0412  48  PRO A O   
362  C CB  . PRO A 51  ? 0.3899 0.4164 0.3212 -0.0183 0.0135  0.0250  48  PRO A CB  
363  C CG  . PRO A 51  ? 0.3654 0.3816 0.3119 -0.0203 0.0103  0.0233  48  PRO A CG  
364  C CD  . PRO A 51  ? 0.3572 0.3740 0.3145 -0.0248 0.0136  0.0164  48  PRO A CD  
365  N N   . GLN A 52  ? 0.4205 0.4404 0.3391 -0.0251 0.0327  0.0510  49  GLN A N   
366  C CA  . GLN A 52  ? 0.4084 0.4139 0.3249 -0.0283 0.0387  0.0668  49  GLN A CA  
367  C C   . GLN A 52  ? 0.4566 0.4577 0.3577 -0.0190 0.0339  0.0776  49  GLN A C   
368  O O   . GLN A 52  ? 0.4631 0.4800 0.3491 -0.0120 0.0299  0.0761  49  GLN A O   
369  C CB  . GLN A 52  ? 0.4394 0.4524 0.3532 -0.0352 0.0508  0.0749  49  GLN A CB  
370  C CG  . GLN A 52  ? 0.4228 0.4394 0.3572 -0.0452 0.0551  0.0662  49  GLN A CG  
371  C CD  . GLN A 52  ? 0.4238 0.4499 0.3615 -0.0542 0.0678  0.0748  49  GLN A CD  
372  O OE1 . GLN A 52  ? 0.4349 0.4600 0.3914 -0.0647 0.0716  0.0726  49  GLN A OE1 
373  N NE2 . GLN A 52  ? 0.4259 0.4643 0.3458 -0.0505 0.0746  0.0845  49  GLN A NE2 
374  N N   . TYR A 53  ? 0.4468 0.4271 0.3518 -0.0180 0.0338  0.0875  50  TYR A N   
375  C CA  . TYR A 53  ? 0.4701 0.4458 0.3622 -0.0069 0.0290  0.0996  50  TYR A CA  
376  C C   . TYR A 53  ? 0.5073 0.4858 0.3796 -0.0048 0.0360  0.1176  50  TYR A C   
377  O O   . TYR A 53  ? 0.4978 0.4713 0.3710 -0.0141 0.0473  0.1255  50  TYR A O   
378  C CB  . TYR A 53  ? 0.4832 0.4334 0.3857 -0.0044 0.0280  0.1052  50  TYR A CB  
379  C CG  . TYR A 53  ? 0.4233 0.3703 0.3441 -0.0072 0.0238  0.0890  50  TYR A CG  
380  C CD1 . TYR A 53  ? 0.4379 0.4040 0.3630 -0.0058 0.0168  0.0749  50  TYR A CD1 
381  C CD2 . TYR A 53  ? 0.4584 0.3824 0.3912 -0.0112 0.0269  0.0880  50  TYR A CD2 
382  C CE1 . TYR A 53  ? 0.4053 0.3694 0.3456 -0.0081 0.0142  0.0627  50  TYR A CE1 
383  C CE2 . TYR A 53  ? 0.4359 0.3597 0.3823 -0.0127 0.0234  0.0734  50  TYR A CE2 
384  C CZ  . TYR A 53  ? 0.4456 0.3902 0.3949 -0.0109 0.0176  0.0622  50  TYR A CZ  
385  O OH  . TYR A 53  ? 0.4323 0.3774 0.3931 -0.0120 0.0154  0.0506  50  TYR A OH  
386  N N   . GLU A 54  ? 0.4861 0.4751 0.3408 0.0074  0.0292  0.1249  51  GLU A N   
387  C CA  . GLU A 54  ? 0.5352 0.5289 0.3667 0.0122  0.0348  0.1444  51  GLU A CA  
388  C C   . GLU A 54  ? 0.5830 0.5472 0.4180 0.0072  0.0457  0.1651  51  GLU A C   
389  O O   . GLU A 54  ? 0.5697 0.5085 0.4189 0.0080  0.0437  0.1669  51  GLU A O   
390  C CB  . GLU A 54  ? 0.5525 0.5595 0.3669 0.0282  0.0231  0.1499  51  GLU A CB  
391  C CG  . GLU A 54  ? 0.6137 0.6200 0.4027 0.0367  0.0278  0.1759  51  GLU A CG  
392  C CD  . GLU A 54  ? 0.7063 0.7340 0.4771 0.0534  0.0140  0.1789  51  GLU A CD  
393  O OE1 . GLU A 54  ? 0.6815 0.6964 0.4541 0.0645  0.0082  0.1918  51  GLU A OE1 
394  O OE2 . GLU A 54  ? 0.7642 0.8221 0.5193 0.0560  0.0086  0.1674  51  GLU A OE2 
395  N N   . GLY A 55  ? 0.5605 0.5279 0.3838 0.0013  0.0581  0.1797  52  GLY A N   
396  C CA  . GLY A 55  ? 0.6102 0.5492 0.4371 -0.0057 0.0698  0.2015  52  GLY A CA  
397  C C   . GLY A 55  ? 0.6070 0.5293 0.4611 -0.0235 0.0774  0.1928  52  GLY A C   
398  O O   . GLY A 55  ? 0.6814 0.5818 0.5413 -0.0335 0.0886  0.2092  52  GLY A O   
399  N N   . HIS A 56  ? 0.5427 0.4752 0.4136 -0.0282 0.0715  0.1683  53  HIS A N   
400  C CA  . HIS A 56  ? 0.5682 0.4924 0.4638 -0.0443 0.0768  0.1577  53  HIS A CA  
401  C C   . HIS A 56  ? 0.5782 0.5296 0.4758 -0.0542 0.0863  0.1543  53  HIS A C   
402  O O   . HIS A 56  ? 0.6230 0.6005 0.5034 -0.0472 0.0869  0.1538  53  HIS A O   
403  C CB  . HIS A 56  ? 0.5331 0.4562 0.4440 -0.0424 0.0657  0.1351  53  HIS A CB  
404  C CG  . HIS A 56  ? 0.5413 0.4382 0.4553 -0.0341 0.0587  0.1368  53  HIS A CG  
405  N ND1 . HIS A 56  ? 0.5358 0.4304 0.4344 -0.0184 0.0527  0.1472  53  HIS A ND1 
406  C CD2 . HIS A 56  ? 0.5169 0.3906 0.4475 -0.0380 0.0569  0.1286  53  HIS A CD2 
407  C CE1 . HIS A 56  ? 0.5424 0.4133 0.4494 -0.0123 0.0482  0.1460  53  HIS A CE1 
408  N NE2 . HIS A 56  ? 0.5163 0.3732 0.4417 -0.0240 0.0510  0.1342  53  HIS A NE2 
409  N N   . ALA A 57  ? 0.5253 0.4720 0.4450 -0.0704 0.0937  0.1510  54  ALA A N   
410  C CA  . ALA A 57  ? 0.5733 0.5463 0.4992 -0.0810 0.1052  0.1512  54  ALA A CA  
411  C C   . ALA A 57  ? 0.6616 0.6448 0.5654 -0.0783 0.1168  0.1736  54  ALA A C   
412  O O   . ALA A 57  ? 0.6155 0.6300 0.5065 -0.0734 0.1210  0.1709  54  ALA A O   
413  C CB  . ALA A 57  ? 0.5570 0.5600 0.4866 -0.0762 0.0994  0.1291  54  ALA A CB  
414  N N   . ALA A 58  ? 0.6328 0.5882 0.5315 -0.0810 0.1224  0.1961  55  ALA A N   
415  C CA  . ALA A 58  ? 0.7060 0.6642 0.5783 -0.0747 0.1313  0.2221  55  ALA A CA  
416  C C   . ALA A 58  ? 0.7198 0.6377 0.5978 -0.0826 0.1384  0.2459  55  ALA A C   
417  O O   . ALA A 58  ? 0.7166 0.6045 0.6160 -0.0891 0.1332  0.2379  55  ALA A O   
418  C CB  . ALA A 58  ? 0.6748 0.6419 0.5184 -0.0530 0.1190  0.2210  55  ALA A CB  
419  N N   . PRO A 59  ? 0.7728 0.6877 0.6321 -0.0819 0.1465  0.2666  56  PRO A N   
420  C CA  . PRO A 59  ? 0.7841 0.6567 0.6467 -0.0875 0.1482  0.2830  56  PRO A CA  
421  C C   . PRO A 59  ? 0.8259 0.6662 0.6875 -0.0733 0.1351  0.2832  56  PRO A C   
422  O O   . PRO A 59  ? 0.8023 0.6558 0.6466 -0.0540 0.1249  0.2804  56  PRO A O   
423  C CB  . PRO A 59  ? 0.8111 0.6926 0.6449 -0.0820 0.1551  0.3036  56  PRO A CB  
424  C CG  . PRO A 59  ? 0.8142 0.7430 0.6367 -0.0800 0.1608  0.2950  56  PRO A CG  
425  C CD  . PRO A 59  ? 0.7278 0.6780 0.5653 -0.0789 0.1548  0.2716  56  PRO A CD  
426  N N   . PRO A 60  ? 0.8566 0.6554 0.7373 -0.0820 0.1345  0.2846  57  PRO A N   
427  C CA  . PRO A 60  ? 0.8664 0.6348 0.7506 -0.0680 0.1227  0.2802  57  PRO A CA  
428  C C   . PRO A 60  ? 0.8300 0.5917 0.6875 -0.0453 0.1153  0.2972  57  PRO A C   
429  O O   . PRO A 60  ? 0.8090 0.5585 0.6663 -0.0288 0.1045  0.2924  57  PRO A O   
430  C CB  . PRO A 60  ? 0.8612 0.5875 0.7700 -0.0841 0.1253  0.2779  57  PRO A CB  
431  C CG  . PRO A 60  ? 0.8642 0.5938 0.7721 -0.1018 0.1376  0.2922  57  PRO A CG  
432  C CD  . PRO A 60  ? 0.8566 0.6357 0.7585 -0.1055 0.1439  0.2871  57  PRO A CD  
433  N N   . ASP A 61  ? 0.8412 0.6123 0.6770 -0.0435 0.1208  0.3164  58  ASP A N   
434  C CA  . ASP A 61  ? 0.8373 0.6088 0.6470 -0.0211 0.1125  0.3316  58  ASP A CA  
435  C C   . ASP A 61  ? 0.8610 0.6699 0.6559 -0.0034 0.1014  0.3202  58  ASP A C   
436  O O   . ASP A 61  ? 0.8302 0.6383 0.6129 0.0169  0.0897  0.3247  58  ASP A O   
437  C CB  . ASP A 61  ? 0.9521 0.7292 0.7407 -0.0241 0.1217  0.3536  58  ASP A CB  
438  C CG  . ASP A 61  ? 1.0784 0.8193 0.8823 -0.0437 0.1329  0.3654  58  ASP A CG  
439  O OD1 . ASP A 61  ? 1.0639 0.7630 0.8757 -0.0400 0.1287  0.3727  58  ASP A OD1 
440  O OD2 . ASP A 61  ? 1.1817 0.9365 0.9912 -0.0629 0.1457  0.3659  58  ASP A OD2 
441  N N   . GLU A 62  ? 0.7961 0.6383 0.5934 -0.0107 0.1043  0.3044  59  GLU A N   
442  C CA  . GLU A 62  ? 0.8429 0.7203 0.6265 0.0044  0.0932  0.2918  59  GLU A CA  
443  C C   . GLU A 62  ? 0.7745 0.6387 0.5727 0.0141  0.0808  0.2789  59  GLU A C   
444  O O   . GLU A 62  ? 0.7300 0.6148 0.5173 0.0303  0.0670  0.2709  59  GLU A O   
445  C CB  . GLU A 62  ? 0.7855 0.6989 0.5701 -0.0059 0.0993  0.2765  59  GLU A CB  
446  C CG  . GLU A 62  ? 0.8218 0.7551 0.5911 -0.0132 0.1113  0.2851  59  GLU A CG  
447  C CD  . GLU A 62  ? 0.9607 0.9193 0.6961 0.0037  0.1049  0.2913  59  GLU A CD  
448  O OE1 . GLU A 62  ? 1.0302 0.9847 0.7503 0.0034  0.1120  0.3096  59  GLU A OE1 
449  O OE2 . GLU A 62  ? 1.0652 1.0485 0.7893 0.0167  0.0924  0.2773  59  GLU A OE2 
450  N N   . ILE A 63  ? 0.7403 0.5735 0.5659 0.0030  0.0830  0.2695  60  ILE A N   
451  C CA  . ILE A 63  ? 0.7310 0.5512 0.5712 0.0126  0.0704  0.2527  60  ILE A CA  
452  C C   . ILE A 63  ? 0.7636 0.5643 0.5922 0.0335  0.0644  0.2725  60  ILE A C   
453  O O   . ILE A 63  ? 0.7445 0.5588 0.5721 0.0497  0.0511  0.2630  60  ILE A O   
454  C CB  . ILE A 63  ? 0.7110 0.5030 0.5799 -0.0031 0.0744  0.2378  60  ILE A CB  
455  C CG1 . ILE A 63  ? 0.6631 0.4825 0.5444 -0.0184 0.0751  0.2136  60  ILE A CG1 
456  C CG2 . ILE A 63  ? 0.7178 0.4885 0.5983 0.0092  0.0645  0.2270  60  ILE A CG2 
457  C CD1 . ILE A 63  ? 0.6559 0.4550 0.5637 -0.0328 0.0766  0.1962  60  ILE A CD1 
458  N N   . LEU A 64  ? 0.7675 0.5403 0.5900 0.0322  0.0721  0.2955  61  LEU A N   
459  C CA  . LEU A 64  ? 0.8061 0.5627 0.6195 0.0514  0.0641  0.3098  61  LEU A CA  
460  C C   . LEU A 64  ? 0.8421 0.6379 0.6308 0.0700  0.0532  0.3150  61  LEU A C   
461  O O   . LEU A 64  ? 0.8815 0.6749 0.6669 0.0896  0.0424  0.3204  61  LEU A O   
462  C CB  . LEU A 64  ? 0.8330 0.5571 0.6437 0.0432  0.0729  0.3297  61  LEU A CB  
463  C CG  . LEU A 64  ? 0.8624 0.5464 0.6977 0.0230  0.0825  0.3246  61  LEU A CG  
464  C CD1 . LEU A 64  ? 0.9270 0.5821 0.7565 0.0156  0.0902  0.3467  61  LEU A CD1 
465  C CD2 . LEU A 64  ? 0.8754 0.5309 0.7316 0.0311  0.0758  0.3095  61  LEU A CD2 
466  N N   . LYS A 65  ? 0.8084 0.6417 0.5809 0.0644  0.0552  0.3117  62  LYS A N   
467  C CA  . LYS A 65  ? 0.7850 0.6579 0.5340 0.0802  0.0437  0.3118  62  LYS A CA  
468  C C   . LYS A 65  ? 0.7871 0.6910 0.5409 0.0872  0.0316  0.2905  62  LYS A C   
469  O O   . LYS A 65  ? 0.7693 0.7082 0.5071 0.0993  0.0196  0.2860  62  LYS A O   
470  C CB  . LYS A 65  ? 0.7662 0.6648 0.4926 0.0722  0.0514  0.3172  62  LYS A CB  
471  C CG  . LYS A 65  ? 0.8942 0.7702 0.6104 0.0675  0.0621  0.3411  62  LYS A CG  
472  C CD  . LYS A 65  ? 1.0172 0.9189 0.7158 0.0565  0.0732  0.3431  62  LYS A CD  
473  C CE  . LYS A 65  ? 1.1032 0.9769 0.8111 0.0370  0.0909  0.3569  62  LYS A CE  
474  N NZ  . LYS A 65  ? 1.0851 0.9839 0.7943 0.0206  0.1030  0.3463  62  LYS A NZ  
475  N N   . SER A 66  ? 0.7254 0.6184 0.5039 0.0773  0.0328  0.2718  63  SER A N   
476  C CA  . SER A 66  ? 0.6735 0.5947 0.4644 0.0767  0.0210  0.2421  63  SER A CA  
477  C C   . SER A 66  ? 0.6896 0.5968 0.5008 0.0876  0.0121  0.2348  63  SER A C   
478  O O   . SER A 66  ? 0.7517 0.6367 0.5608 0.1020  0.0112  0.2536  63  SER A O   
479  C CB  . SER A 66  ? 0.6412 0.5665 0.4459 0.0556  0.0287  0.2216  63  SER A CB  
480  O OG  . SER A 66  ? 0.6244 0.5752 0.4395 0.0545  0.0183  0.1952  63  SER A OG  
481  N N   . SER A 67  ? 0.6367 0.5566 0.4677 0.0816  0.0064  0.2085  64  SER A N   
482  C CA  . SER A 67  ? 0.6636 0.5800 0.5127 0.0932  -0.0021 0.2002  64  SER A CA  
483  C C   . SER A 67  ? 0.6095 0.5346 0.4805 0.0817  -0.0036 0.1731  64  SER A C   
484  O O   . SER A 67  ? 0.5614 0.5096 0.4313 0.0706  -0.0048 0.1589  64  SER A O   
485  C CB  . SER A 67  ? 0.6342 0.5818 0.4733 0.1124  -0.0161 0.2059  64  SER A CB  
486  O OG  . SER A 67  ? 0.6981 0.6653 0.5571 0.1182  -0.0261 0.1884  64  SER A OG  
487  N N   . PRO A 68  ? 0.6000 0.5063 0.4902 0.0846  -0.0029 0.1655  65  PRO A N   
488  C CA  . PRO A 68  ? 0.5798 0.4981 0.4885 0.0756  -0.0045 0.1417  65  PRO A CA  
489  C C   . PRO A 68  ? 0.5251 0.4840 0.4363 0.0781  -0.0152 0.1302  65  PRO A C   
490  O O   . PRO A 68  ? 0.4929 0.4655 0.4133 0.0663  -0.0155 0.1133  65  PRO A O   
491  C CB  . PRO A 68  ? 0.5891 0.4855 0.5134 0.0852  -0.0035 0.1387  65  PRO A CB  
492  C CG  . PRO A 68  ? 0.6421 0.5022 0.5584 0.0931  0.0020  0.1588  65  PRO A CG  
493  C CD  . PRO A 68  ? 0.6342 0.5014 0.5287 0.0934  0.0023  0.1783  65  PRO A CD  
494  N N   . PHE A 69  ? 0.5591 0.5374 0.4636 0.0934  -0.0246 0.1394  66  PHE A N   
495  C CA  . PHE A 69  ? 0.5384 0.5572 0.4462 0.0947  -0.0361 0.1282  66  PHE A CA  
496  C C   . PHE A 69  ? 0.5407 0.5741 0.4357 0.0810  -0.0361 0.1202  66  PHE A C   
497  O O   . PHE A 69  ? 0.5285 0.5826 0.4335 0.0723  -0.0408 0.1027  66  PHE A O   
498  C CB  . PHE A 69  ? 0.6563 0.6934 0.5581 0.1148  -0.0468 0.1413  66  PHE A CB  
499  C CG  . PHE A 69  ? 0.6951 0.7763 0.5976 0.1161  -0.0605 0.1312  66  PHE A CG  
500  C CD1 . PHE A 69  ? 0.7535 0.8612 0.6791 0.1218  -0.0692 0.1212  66  PHE A CD1 
501  C CD2 . PHE A 69  ? 0.7513 0.8496 0.6308 0.1138  -0.0652 0.1333  66  PHE A CD2 
502  C CE1 . PHE A 69  ? 0.7586 0.9081 0.6879 0.1214  -0.0829 0.1111  66  PHE A CE1 
503  C CE2 . PHE A 69  ? 0.7478 0.8867 0.6277 0.1151  -0.0794 0.1219  66  PHE A CE2 
504  C CZ  . PHE A 69  ? 0.7587 0.9228 0.6648 0.1180  -0.0888 0.1106  66  PHE A CZ  
505  N N   . VAL A 70  ? 0.5166 0.5386 0.3903 0.0789  -0.0298 0.1329  67  VAL A N   
506  C CA  . VAL A 70  ? 0.4941 0.5277 0.3564 0.0665  -0.0271 0.1240  67  VAL A CA  
507  C C   . VAL A 70  ? 0.4701 0.4904 0.3480 0.0505  -0.0189 0.1096  67  VAL A C   
508  O O   . VAL A 70  ? 0.4715 0.5073 0.3534 0.0419  -0.0212 0.0932  67  VAL A O   
509  C CB  . VAL A 70  ? 0.5080 0.5348 0.3443 0.0686  -0.0200 0.1428  67  VAL A CB  
510  C CG1 . VAL A 70  ? 0.5286 0.5674 0.3549 0.0566  -0.0150 0.1324  67  VAL A CG1 
511  C CG2 . VAL A 70  ? 0.5747 0.6211 0.3923 0.0855  -0.0301 0.1561  67  VAL A CG2 
512  N N   . TRP A 71  ? 0.4886 0.4800 0.3757 0.0469  -0.0100 0.1148  68  TRP A N   
513  C CA  . TRP A 71  ? 0.4548 0.4363 0.3548 0.0326  -0.0030 0.1020  68  TRP A CA  
514  C C   . TRP A 71  ? 0.4179 0.4136 0.3350 0.0298  -0.0091 0.0842  68  TRP A C   
515  O O   . TRP A 71  ? 0.4062 0.4063 0.3289 0.0194  -0.0069 0.0722  68  TRP A O   
516  C CB  . TRP A 71  ? 0.4861 0.4355 0.3937 0.0294  0.0057  0.1088  68  TRP A CB  
517  C CG  . TRP A 71  ? 0.4970 0.4284 0.3904 0.0315  0.0125  0.1293  68  TRP A CG  
518  C CD1 . TRP A 71  ? 0.5314 0.4745 0.4052 0.0321  0.0146  0.1408  68  TRP A CD1 
519  C CD2 . TRP A 71  ? 0.5468 0.4444 0.4441 0.0335  0.0185  0.1414  68  TRP A CD2 
520  N NE1 . TRP A 71  ? 0.5674 0.4867 0.4325 0.0339  0.0225  0.1622  68  TRP A NE1 
521  C CE2 . TRP A 71  ? 0.5675 0.4563 0.4480 0.0342  0.0247  0.1626  68  TRP A CE2 
522  C CE3 . TRP A 71  ? 0.5779 0.4508 0.4908 0.0347  0.0196  0.1358  68  TRP A CE3 
523  C CZ2 . TRP A 71  ? 0.6411 0.4942 0.5219 0.0351  0.0321  0.1798  68  TRP A CZ2 
524  C CZ3 . TRP A 71  ? 0.5844 0.4215 0.4974 0.0364  0.0261  0.1498  68  TRP A CZ3 
525  C CH2 . TRP A 71  ? 0.6114 0.4373 0.5095 0.0359  0.0323  0.1722  68  TRP A CH2 
526  N N   . PHE A 72  ? 0.4192 0.4232 0.3457 0.0395  -0.0161 0.0833  69  PHE A N   
527  C CA  . PHE A 72  ? 0.3965 0.4164 0.3399 0.0353  -0.0205 0.0683  69  PHE A CA  
528  C C   . PHE A 72  ? 0.3882 0.4322 0.3282 0.0304  -0.0274 0.0589  69  PHE A C   
529  O O   . PHE A 72  ? 0.3705 0.4190 0.3203 0.0209  -0.0270 0.0466  69  PHE A O   
530  C CB  . PHE A 72  ? 0.4136 0.4409 0.3706 0.0465  -0.0250 0.0693  69  PHE A CB  
531  C CG  . PHE A 72  ? 0.3849 0.4300 0.3606 0.0410  -0.0275 0.0562  69  PHE A CG  
532  C CD1 . PHE A 72  ? 0.3718 0.4063 0.3550 0.0314  -0.0207 0.0483  69  PHE A CD1 
533  C CD2 . PHE A 72  ? 0.4004 0.4745 0.3865 0.0448  -0.0366 0.0525  69  PHE A CD2 
534  C CE1 . PHE A 72  ? 0.3642 0.4144 0.3633 0.0261  -0.0216 0.0393  69  PHE A CE1 
535  C CE2 . PHE A 72  ? 0.3672 0.4573 0.3723 0.0376  -0.0374 0.0423  69  PHE A CE2 
536  C CZ  . PHE A 72  ? 0.3073 0.3843 0.3180 0.0285  -0.0293 0.0368  69  PHE A CZ  
537  N N   . LYS A 73  ? 0.3977 0.4565 0.3230 0.0372  -0.0340 0.0641  70  LYS A N   
538  C CA  . LYS A 73  ? 0.4047 0.4837 0.3245 0.0316  -0.0402 0.0520  70  LYS A CA  
539  C C   . LYS A 73  ? 0.3922 0.4607 0.3042 0.0217  -0.0320 0.0462  70  LYS A C   
540  O O   . LYS A 73  ? 0.4186 0.4960 0.3345 0.0148  -0.0349 0.0317  70  LYS A O   
541  C CB  . LYS A 73  ? 0.4630 0.5621 0.3646 0.0413  -0.0491 0.0574  70  LYS A CB  
542  C CG  . LYS A 73  ? 0.5683 0.6767 0.4723 0.0553  -0.0563 0.0688  70  LYS A CG  
543  C CD  . LYS A 73  ? 0.7362 0.8800 0.6405 0.0581  -0.0713 0.0585  70  LYS A CD  
544  C CE  . LYS A 73  ? 0.6861 0.8477 0.5894 0.0747  -0.0810 0.0706  70  LYS A CE  
545  N NZ  . LYS A 73  ? 0.7312 0.9158 0.6090 0.0832  -0.0909 0.0743  70  LYS A NZ  
546  N N   . ASP A 74  ? 0.4260 0.4761 0.3289 0.0208  -0.0219 0.0572  71  ASP A N   
547  C CA  . ASP A 74  ? 0.4361 0.4798 0.3363 0.0116  -0.0134 0.0516  71  ASP A CA  
548  C C   . ASP A 74  ? 0.4245 0.4618 0.3446 0.0034  -0.0119 0.0396  71  ASP A C   
549  O O   . ASP A 74  ? 0.4087 0.4494 0.3306 -0.0023 -0.0104 0.0289  71  ASP A O   
550  C CB  . ASP A 74  ? 0.4492 0.4760 0.3412 0.0103  -0.0025 0.0665  71  ASP A CB  
551  C CG  . ASP A 74  ? 0.5038 0.5370 0.3725 0.0176  -0.0014 0.0810  71  ASP A CG  
552  O OD1 . ASP A 74  ? 0.5057 0.5599 0.3597 0.0218  -0.0072 0.0759  71  ASP A OD1 
553  O OD2 . ASP A 74  ? 0.5297 0.5458 0.3939 0.0192  0.0052  0.0980  71  ASP A OD2 
554  N N   . ALA A 75  ? 0.3803 0.4087 0.3144 0.0042  -0.0121 0.0417  72  ALA A N   
555  C CA  . ALA A 75  ? 0.3635 0.3886 0.3140 -0.0021 -0.0109 0.0323  72  ALA A CA  
556  C C   . ALA A 75  ? 0.3583 0.3985 0.3171 -0.0045 -0.0182 0.0213  72  ALA A C   
557  O O   . ALA A 75  ? 0.3349 0.3734 0.3003 -0.0109 -0.0168 0.0129  72  ALA A O   
558  C CB  . ALA A 75  ? 0.3616 0.3766 0.3222 0.0009  -0.0091 0.0366  72  ALA A CB  
559  N N   . LEU A 76  ? 0.3587 0.4138 0.3190 0.0005  -0.0264 0.0215  73  LEU A N   
560  C CA  . LEU A 76  ? 0.3487 0.4193 0.3189 -0.0039 -0.0342 0.0100  73  LEU A CA  
561  C C   . LEU A 76  ? 0.3652 0.4376 0.3251 -0.0079 -0.0357 -0.0003 73  LEU A C   
562  O O   . LEU A 76  ? 0.3390 0.4109 0.3092 -0.0149 -0.0375 -0.0116 73  LEU A O   
563  C CB  . LEU A 76  ? 0.3211 0.4125 0.2945 0.0026  -0.0439 0.0116  73  LEU A CB  
564  C CG  . LEU A 76  ? 0.3515 0.4460 0.3394 0.0081  -0.0432 0.0190  73  LEU A CG  
565  C CD1 . LEU A 76  ? 0.3871 0.5063 0.3781 0.0167  -0.0537 0.0211  73  LEU A CD1 
566  C CD2 . LEU A 76  ? 0.3491 0.4427 0.3576 -0.0003 -0.0393 0.0134  73  LEU A CD2 
567  N N   . ASP A 77  ? 0.3674 0.4416 0.3066 -0.0028 -0.0344 0.0038  74  ASP A N   
568  C CA  . ASP A 77  ? 0.3809 0.4585 0.3081 -0.0047 -0.0342 -0.0070 74  ASP A CA  
569  C C   . ASP A 77  ? 0.3591 0.4221 0.2939 -0.0104 -0.0261 -0.0121 74  ASP A C   
570  O O   . ASP A 77  ? 0.3846 0.4477 0.3200 -0.0130 -0.0275 -0.0255 74  ASP A O   
571  C CB  . ASP A 77  ? 0.4159 0.4992 0.3184 0.0022  -0.0311 0.0015  74  ASP A CB  
572  C CG  . ASP A 77  ? 0.5029 0.6054 0.3928 0.0099  -0.0413 0.0041  74  ASP A CG  
573  O OD1 . ASP A 77  ? 0.4804 0.5959 0.3813 0.0086  -0.0523 -0.0058 74  ASP A OD1 
574  O OD2 . ASP A 77  ? 0.5113 0.6177 0.3799 0.0170  -0.0383 0.0164  74  ASP A OD2 
575  N N   . GLY A 78  ? 0.3498 0.4003 0.2905 -0.0117 -0.0183 -0.0024 75  GLY A N   
576  C CA  . GLY A 78  ? 0.3523 0.3925 0.3012 -0.0160 -0.0119 -0.0063 75  GLY A CA  
577  C C   . GLY A 78  ? 0.3547 0.3907 0.3203 -0.0204 -0.0154 -0.0143 75  GLY A C   
578  O O   . GLY A 78  ? 0.3489 0.3795 0.3184 -0.0221 -0.0139 -0.0223 75  GLY A O   
579  N N   . TYR A 79  ? 0.3292 0.3673 0.3057 -0.0219 -0.0194 -0.0111 76  TYR A N   
580  C CA  . TYR A 79  ? 0.2882 0.3241 0.2812 -0.0275 -0.0221 -0.0168 76  TYR A CA  
581  C C   . TYR A 79  ? 0.3085 0.3474 0.3018 -0.0304 -0.0284 -0.0304 76  TYR A C   
582  O O   . TYR A 79  ? 0.3234 0.3515 0.3245 -0.0341 -0.0275 -0.0373 76  TYR A O   
583  C CB  . TYR A 79  ? 0.3151 0.3593 0.3200 -0.0284 -0.0248 -0.0113 76  TYR A CB  
584  C CG  . TYR A 79  ? 0.3184 0.3631 0.3423 -0.0360 -0.0263 -0.0147 76  TYR A CG  
585  C CD1 . TYR A 79  ? 0.3013 0.3535 0.3339 -0.0418 -0.0338 -0.0245 76  TYR A CD1 
586  C CD2 . TYR A 79  ? 0.2789 0.3170 0.3117 -0.0380 -0.0202 -0.0079 76  TYR A CD2 
587  C CE1 . TYR A 79  ? 0.3104 0.3612 0.3629 -0.0509 -0.0342 -0.0262 76  TYR A CE1 
588  C CE2 . TYR A 79  ? 0.2819 0.3201 0.3315 -0.0454 -0.0199 -0.0078 76  TYR A CE2 
589  C CZ  . TYR A 79  ? 0.2835 0.3268 0.3442 -0.0526 -0.0264 -0.0163 76  TYR A CZ  
590  O OH  . TYR A 79  ? 0.2877 0.3292 0.3675 -0.0619 -0.0249 -0.0147 76  TYR A OH  
591  N N   . ASP A 80  ? 0.3191 0.3722 0.3034 -0.0280 -0.0354 -0.0347 77  ASP A N   
592  C CA  . ASP A 80  ? 0.3161 0.3739 0.2999 -0.0311 -0.0431 -0.0508 77  ASP A CA  
593  C C   . ASP A 80  ? 0.3747 0.4226 0.3473 -0.0284 -0.0388 -0.0602 77  ASP A C   
594  O O   . ASP A 80  ? 0.3756 0.4167 0.3536 -0.0318 -0.0423 -0.0752 77  ASP A O   
595  C CB  . ASP A 80  ? 0.3690 0.4484 0.3418 -0.0271 -0.0522 -0.0533 77  ASP A CB  
596  C CG  . ASP A 80  ? 0.3949 0.4882 0.3829 -0.0287 -0.0578 -0.0463 77  ASP A CG  
597  O OD1 . ASP A 80  ? 0.3599 0.4476 0.3687 -0.0354 -0.0554 -0.0440 77  ASP A OD1 
598  O OD2 . ASP A 80  ? 0.3341 0.4457 0.3132 -0.0221 -0.0642 -0.0425 77  ASP A OD2 
599  N N   . TYR A 81  ? 0.3608 0.4076 0.3196 -0.0223 -0.0307 -0.0522 78  TYR A N   
600  C CA  . TYR A 81  ? 0.3961 0.4375 0.3470 -0.0186 -0.0250 -0.0601 78  TYR A CA  
601  C C   . TYR A 81  ? 0.3619 0.3856 0.3296 -0.0212 -0.0217 -0.0630 78  TYR A C   
602  O O   . TYR A 81  ? 0.3753 0.3909 0.3447 -0.0197 -0.0223 -0.0767 78  TYR A O   
603  C CB  . TYR A 81  ? 0.4065 0.4536 0.3439 -0.0136 -0.0160 -0.0483 78  TYR A CB  
604  C CG  . TYR A 81  ? 0.3976 0.4452 0.3287 -0.0091 -0.0086 -0.0553 78  TYR A CG  
605  C CD1 . TYR A 81  ? 0.5005 0.5579 0.4159 -0.0040 -0.0095 -0.0686 78  TYR A CD1 
606  C CD2 . TYR A 81  ? 0.4190 0.4602 0.3602 -0.0090 -0.0008 -0.0495 78  TYR A CD2 
607  C CE1 . TYR A 81  ? 0.5037 0.5643 0.4143 0.0019  -0.0015 -0.0758 78  TYR A CE1 
608  C CE2 . TYR A 81  ? 0.4667 0.5127 0.4050 -0.0036 0.0062  -0.0559 78  TYR A CE2 
609  C CZ  . TYR A 81  ? 0.4906 0.5460 0.4142 0.0021  0.0065  -0.0687 78  TYR A CZ  
610  O OH  . TYR A 81  ? 0.5400 0.6028 0.4616 0.0090  0.0146  -0.0759 78  TYR A OH  
611  N N   . LEU A 82  ? 0.3466 0.3638 0.3262 -0.0240 -0.0184 -0.0505 79  LEU A N   
612  C CA  . LEU A 82  ? 0.3542 0.3561 0.3483 -0.0255 -0.0159 -0.0502 79  LEU A CA  
613  C C   . LEU A 82  ? 0.3681 0.3593 0.3740 -0.0309 -0.0219 -0.0609 79  LEU A C   
614  O O   . LEU A 82  ? 0.3678 0.3437 0.3798 -0.0292 -0.0206 -0.0678 79  LEU A O   
615  C CB  . LEU A 82  ? 0.3229 0.3234 0.3253 -0.0278 -0.0128 -0.0356 79  LEU A CB  
616  C CG  . LEU A 82  ? 0.3467 0.3509 0.3433 -0.0239 -0.0063 -0.0271 79  LEU A CG  
617  C CD1 . LEU A 82  ? 0.3171 0.3215 0.3193 -0.0263 -0.0049 -0.0159 79  LEU A CD1 
618  C CD2 . LEU A 82  ? 0.3519 0.3506 0.3520 -0.0193 -0.0026 -0.0303 79  LEU A CD2 
619  N N   . VAL A 83  ? 0.3219 0.3209 0.3330 -0.0374 -0.0285 -0.0624 80  VAL A N   
620  C CA  . VAL A 83  ? 0.3505 0.3406 0.3763 -0.0456 -0.0346 -0.0734 80  VAL A CA  
621  C C   . VAL A 83  ? 0.3788 0.3641 0.3961 -0.0429 -0.0387 -0.0936 80  VAL A C   
622  O O   . VAL A 83  ? 0.4234 0.3888 0.4512 -0.0456 -0.0396 -0.1038 80  VAL A O   
623  C CB  . VAL A 83  ? 0.3423 0.3485 0.3779 -0.0534 -0.0412 -0.0713 80  VAL A CB  
624  C CG1 . VAL A 83  ? 0.3824 0.3820 0.4352 -0.0643 -0.0483 -0.0850 80  VAL A CG1 
625  C CG2 . VAL A 83  ? 0.3064 0.3153 0.3518 -0.0551 -0.0355 -0.0531 80  VAL A CG2 
626  N N   . GLU A 84  ? 0.3652 0.3678 0.3624 -0.0367 -0.0409 -0.0998 81  GLU A N   
627  C CA  . GLU A 84  ? 0.4084 0.4096 0.3937 -0.0323 -0.0440 -0.1205 81  GLU A CA  
628  C C   . GLU A 84  ? 0.4222 0.4057 0.4073 -0.0246 -0.0360 -0.1245 81  GLU A C   
629  O O   . GLU A 84  ? 0.4528 0.4248 0.4371 -0.0221 -0.0382 -0.1437 81  GLU A O   
630  C CB  . GLU A 84  ? 0.4838 0.5095 0.4437 -0.0252 -0.0455 -0.1225 81  GLU A CB  
631  C CG  . GLU A 84  ? 0.5666 0.6135 0.5237 -0.0292 -0.0553 -0.1200 81  GLU A CG  
632  C CD  . GLU A 84  ? 0.6768 0.7461 0.6064 -0.0199 -0.0547 -0.1148 81  GLU A CD  
633  O OE1 . GLU A 84  ? 0.6731 0.7419 0.5885 -0.0124 -0.0446 -0.1090 81  GLU A OE1 
634  O OE2 . GLU A 84  ? 0.6801 0.7690 0.6035 -0.0201 -0.0641 -0.1151 81  GLU A OE2 
635  N N   . GLN A 85  ? 0.4254 0.4081 0.4114 -0.0199 -0.0271 -0.1082 82  GLN A N   
636  C CA  . GLN A 85  ? 0.4684 0.4402 0.4557 -0.0109 -0.0197 -0.1100 82  GLN A CA  
637  C C   . GLN A 85  ? 0.4910 0.4373 0.4985 -0.0131 -0.0193 -0.1065 82  GLN A C   
638  O O   . GLN A 85  ? 0.4417 0.3782 0.4527 -0.0041 -0.0140 -0.1065 82  GLN A O   
639  C CB  . GLN A 85  ? 0.4204 0.4073 0.4004 -0.0055 -0.0113 -0.0948 82  GLN A CB  
640  C CG  . GLN A 85  ? 0.4432 0.4528 0.4026 -0.0024 -0.0094 -0.0960 82  GLN A CG  
641  C CD  . GLN A 85  ? 0.5104 0.5254 0.4574 0.0068  -0.0066 -0.1135 82  GLN A CD  
642  O OE1 . GLN A 85  ? 0.5331 0.5401 0.4871 0.0141  -0.0017 -0.1193 82  GLN A OE1 
643  N NE2 . GLN A 85  ? 0.5212 0.5514 0.4490 0.0080  -0.0098 -0.1220 82  GLN A NE2 
644  N N   . GLY A 86  ? 0.4134 0.3503 0.4347 -0.0241 -0.0243 -0.1026 83  GLY A N   
645  C CA  . GLY A 86  ? 0.4857 0.3963 0.5254 -0.0275 -0.0237 -0.0991 83  GLY A CA  
646  C C   . GLY A 86  ? 0.4721 0.3817 0.5215 -0.0311 -0.0197 -0.0766 83  GLY A C   
647  O O   . GLY A 86  ? 0.4653 0.3535 0.5271 -0.0312 -0.0175 -0.0697 83  GLY A O   
648  N N   . TYR A 87  ? 0.3973 0.3283 0.4405 -0.0332 -0.0187 -0.0651 84  TYR A N   
649  C CA  . TYR A 87  ? 0.3397 0.2731 0.3883 -0.0348 -0.0145 -0.0459 84  TYR A CA  
650  C C   . TYR A 87  ? 0.4133 0.3572 0.4693 -0.0456 -0.0174 -0.0409 84  TYR A C   
651  O O   . TYR A 87  ? 0.4079 0.3707 0.4557 -0.0459 -0.0196 -0.0418 84  TYR A O   
652  C CB  . TYR A 87  ? 0.3395 0.2886 0.3760 -0.0270 -0.0102 -0.0385 84  TYR A CB  
653  C CG  . TYR A 87  ? 0.3813 0.3264 0.4137 -0.0163 -0.0071 -0.0437 84  TYR A CG  
654  C CD1 . TYR A 87  ? 0.3520 0.2874 0.3912 -0.0100 -0.0042 -0.0354 84  TYR A CD1 
655  C CD2 . TYR A 87  ? 0.4045 0.3579 0.4264 -0.0114 -0.0069 -0.0565 84  TYR A CD2 
656  C CE1 . TYR A 87  ? 0.3904 0.3255 0.4287 0.0015  -0.0017 -0.0405 84  TYR A CE1 
657  C CE2 . TYR A 87  ? 0.4115 0.3649 0.4317 -0.0007 -0.0030 -0.0620 84  TYR A CE2 
658  C CZ  . TYR A 87  ? 0.4371 0.3818 0.4669 0.0059  -0.0007 -0.0544 84  TYR A CZ  
659  O OH  . TYR A 87  ? 0.4326 0.3809 0.4630 0.0180  0.0029  -0.0601 84  TYR A OH  
660  N N   . ASP A 88  ? 0.3707 0.3031 0.4428 -0.0538 -0.0167 -0.0345 85  ASP A N   
661  C CA  . ASP A 88  ? 0.4306 0.3753 0.5147 -0.0648 -0.0186 -0.0302 85  ASP A CA  
662  C C   . ASP A 88  ? 0.3836 0.3402 0.4676 -0.0638 -0.0125 -0.0123 85  ASP A C   
663  O O   . ASP A 88  ? 0.3857 0.3608 0.4751 -0.0685 -0.0133 -0.0091 85  ASP A O   
664  C CB  . ASP A 88  ? 0.4539 0.3814 0.5588 -0.0768 -0.0200 -0.0327 85  ASP A CB  
665  C CG  . ASP A 88  ? 0.6219 0.5384 0.7291 -0.0802 -0.0276 -0.0543 85  ASP A CG  
666  O OD1 . ASP A 88  ? 0.6125 0.5470 0.7099 -0.0788 -0.0340 -0.0673 85  ASP A OD1 
667  O OD2 . ASP A 88  ? 0.5934 0.4827 0.7120 -0.0841 -0.0272 -0.0586 85  ASP A OD2 
668  N N   . GLU A 89  ? 0.3175 0.2656 0.3960 -0.0567 -0.0069 -0.0015 86  GLU A N   
669  C CA  . GLU A 89  ? 0.3223 0.2815 0.3981 -0.0547 -0.0013 0.0137  86  GLU A CA  
670  C C   . GLU A 89  ? 0.3312 0.3015 0.3905 -0.0452 -0.0009 0.0129  86  GLU A C   
671  O O   . GLU A 89  ? 0.3282 0.2920 0.3800 -0.0379 -0.0006 0.0112  86  GLU A O   
672  C CB  . GLU A 89  ? 0.3723 0.3166 0.4528 -0.0538 0.0038  0.0273  86  GLU A CB  
673  C CG  . GLU A 89  ? 0.4225 0.3468 0.5204 -0.0636 0.0034  0.0267  86  GLU A CG  
674  C CD  . GLU A 89  ? 0.5276 0.4406 0.6326 -0.0659 0.0103  0.0460  86  GLU A CD  
675  O OE1 . GLU A 89  ? 0.4721 0.3865 0.5651 -0.0556 0.0138  0.0575  86  GLU A OE1 
676  O OE2 . GLU A 89  ? 0.5422 0.4459 0.6651 -0.0783 0.0122  0.0499  86  GLU A OE2 
677  N N   . ILE A 90  ? 0.2689 0.2560 0.3244 -0.0454 -0.0007 0.0141  87  ILE A N   
678  C CA  . ILE A 90  ? 0.2858 0.2807 0.3280 -0.0391 -0.0012 0.0108  87  ILE A CA  
679  C C   . ILE A 90  ? 0.3194 0.3255 0.3585 -0.0370 0.0023  0.0181  87  ILE A C   
680  O O   . ILE A 90  ? 0.2951 0.3105 0.3419 -0.0403 0.0034  0.0214  87  ILE A O   
681  C CB  . ILE A 90  ? 0.2871 0.2877 0.3259 -0.0399 -0.0060 0.0013  87  ILE A CB  
682  C CG1 . ILE A 90  ? 0.2816 0.2725 0.3196 -0.0402 -0.0093 -0.0090 87  ILE A CG1 
683  C CG2 . ILE A 90  ? 0.2867 0.2941 0.3131 -0.0346 -0.0051 0.0019  87  ILE A CG2 
684  C CD1 . ILE A 90  ? 0.3142 0.3137 0.3494 -0.0421 -0.0153 -0.0187 87  ILE A CD1 
685  N N   . VAL A 91  ? 0.2909 0.2978 0.3202 -0.0317 0.0041  0.0193  88  VAL A N   
686  C CA  . VAL A 91  ? 0.2892 0.3048 0.3127 -0.0287 0.0064  0.0214  88  VAL A CA  
687  C C   . VAL A 91  ? 0.3143 0.3296 0.3313 -0.0270 0.0046  0.0156  88  VAL A C   
688  O O   . VAL A 91  ? 0.3230 0.3337 0.3363 -0.0270 0.0032  0.0118  88  VAL A O   
689  C CB  . VAL A 91  ? 0.2596 0.2765 0.2766 -0.0249 0.0085  0.0251  88  VAL A CB  
690  C CG1 . VAL A 91  ? 0.2739 0.2969 0.2828 -0.0218 0.0095  0.0218  88  VAL A CG1 
691  C CG2 . VAL A 91  ? 0.2710 0.2897 0.2918 -0.0255 0.0118  0.0349  88  VAL A CG2 
692  N N   . VAL A 92  ? 0.2648 0.2849 0.2807 -0.0249 0.0053  0.0158  89  VAL A N   
693  C CA  . VAL A 92  ? 0.2861 0.3023 0.2955 -0.0228 0.0043  0.0130  89  VAL A CA  
694  C C   . VAL A 92  ? 0.3276 0.3405 0.3315 -0.0204 0.0069  0.0117  89  VAL A C   
695  O O   . VAL A 92  ? 0.2994 0.3170 0.3038 -0.0175 0.0090  0.0120  89  VAL A O   
696  C CB  . VAL A 92  ? 0.2884 0.3097 0.3008 -0.0207 0.0019  0.0139  89  VAL A CB  
697  C CG1 . VAL A 92  ? 0.2759 0.3065 0.2949 -0.0172 0.0041  0.0162  89  VAL A CG1 
698  C CG2 . VAL A 92  ? 0.2738 0.2882 0.2776 -0.0178 0.0012  0.0143  89  VAL A CG2 
699  N N   . ALA A 93  ? 0.3069 0.3132 0.3061 -0.0221 0.0070  0.0093  90  ALA A N   
700  C CA  . ALA A 93  ? 0.3173 0.3199 0.3134 -0.0223 0.0083  0.0055  90  ALA A CA  
701  C C   . ALA A 93  ? 0.3391 0.3306 0.3327 -0.0239 0.0092  0.0056  90  ALA A C   
702  O O   . ALA A 93  ? 0.3567 0.3473 0.3495 -0.0267 0.0095  0.0081  90  ALA A O   
703  C CB  . ALA A 93  ? 0.3134 0.3214 0.3099 -0.0251 0.0074  0.0031  90  ALA A CB  
704  N N   . GLY A 94  ? 0.3243 0.3069 0.3165 -0.0212 0.0104  0.0035  91  GLY A N   
705  C CA  . GLY A 94  ? 0.3470 0.3149 0.3373 -0.0213 0.0118  0.0067  91  GLY A CA  
706  C C   . GLY A 94  ? 0.3813 0.3351 0.3720 -0.0239 0.0134  0.0004  91  GLY A C   
707  O O   . GLY A 94  ? 0.3592 0.3136 0.3495 -0.0206 0.0130  -0.0072 91  GLY A O   
708  N N   . LEU A 95  ? 0.3638 0.3051 0.3554 -0.0303 0.0156  0.0034  92  LEU A N   
709  C CA  . LEU A 95  ? 0.3825 0.3069 0.3774 -0.0361 0.0171  -0.0028 92  LEU A CA  
710  C C   . LEU A 95  ? 0.4179 0.3181 0.4109 -0.0311 0.0196  0.0037  92  LEU A C   
711  O O   . LEU A 95  ? 0.4081 0.3039 0.3979 -0.0303 0.0217  0.0162  92  LEU A O   
712  C CB  . LEU A 95  ? 0.3997 0.3279 0.4006 -0.0487 0.0189  -0.0023 92  LEU A CB  
713  C CG  . LEU A 95  ? 0.4252 0.3361 0.4336 -0.0591 0.0207  -0.0078 92  LEU A CG  
714  C CD1 . LEU A 95  ? 0.4355 0.3480 0.4457 -0.0593 0.0161  -0.0247 92  LEU A CD1 
715  C CD2 . LEU A 95  ? 0.4410 0.3626 0.4581 -0.0718 0.0237  -0.0046 92  LEU A CD2 
716  N N   . SER A 96  ? 0.4047 0.2891 0.3984 -0.0264 0.0195  -0.0048 93  SER A N   
717  C CA  . SER A 96  ? 0.4239 0.2800 0.4172 -0.0204 0.0220  0.0003  93  SER A CA  
718  C C   . SER A 96  ? 0.4470 0.3101 0.4356 -0.0071 0.0211  0.0125  93  SER A C   
719  O O   . SER A 96  ? 0.4078 0.2899 0.3961 0.0013  0.0188  0.0088  93  SER A O   
720  C CB  . SER A 96  ? 0.5167 0.3523 0.5141 -0.0329 0.0258  0.0066  93  SER A CB  
721  O OG  . SER A 96  ? 0.5784 0.3799 0.5777 -0.0291 0.0282  0.0073  93  SER A OG  
722  N N   . LEU A 97  ? 0.4188 0.2693 0.4041 -0.0048 0.0229  0.0276  94  LEU A N   
723  C CA  . LEU A 97  ? 0.4340 0.2974 0.4145 0.0076  0.0201  0.0384  94  LEU A CA  
724  C C   . LEU A 97  ? 0.3910 0.2868 0.3709 0.0054  0.0165  0.0358  94  LEU A C   
725  O O   . LEU A 97  ? 0.3963 0.3090 0.3777 0.0146  0.0130  0.0362  94  LEU A O   
726  C CB  . LEU A 97  ? 0.4315 0.2819 0.4049 0.0085  0.0221  0.0562  94  LEU A CB  
727  C CG  . LEU A 97  ? 0.4378 0.3061 0.4043 0.0204  0.0176  0.0674  94  LEU A CG  
728  C CD1 . LEU A 97  ? 0.4624 0.3294 0.4336 0.0374  0.0142  0.0663  94  LEU A CD1 
729  C CD2 . LEU A 97  ? 0.4875 0.3463 0.4428 0.0205  0.0200  0.0860  94  LEU A CD2 
730  N N   . GLY A 98  ? 0.3787 0.2836 0.3584 -0.0068 0.0176  0.0332  95  GLY A N   
731  C CA  . GLY A 98  ? 0.3615 0.2919 0.3416 -0.0086 0.0145  0.0300  95  GLY A CA  
732  C C   . GLY A 98  ? 0.3676 0.3100 0.3531 -0.0048 0.0125  0.0208  95  GLY A C   
733  O O   . GLY A 98  ? 0.3568 0.3176 0.3443 -0.0032 0.0098  0.0208  95  GLY A O   
734  N N   . GLY A 99  ? 0.3618 0.2942 0.3496 -0.0037 0.0142  0.0127  96  GLY A N   
735  C CA  . GLY A 99  ? 0.3922 0.3377 0.3827 0.0017  0.0139  0.0053  96  GLY A CA  
736  C C   . GLY A 99  ? 0.3743 0.3272 0.3682 0.0138  0.0133  0.0092  96  GLY A C   
737  O O   . GLY A 99  ? 0.3439 0.3175 0.3424 0.0161  0.0128  0.0086  96  GLY A O   
738  N N   . ASP A 100 ? 0.3857 0.3226 0.3790 0.0219  0.0135  0.0139  97  ASP A N   
739  C CA  . ASP A 100 ? 0.3761 0.3243 0.3742 0.0347  0.0116  0.0194  97  ASP A CA  
740  C C   . ASP A 100 ? 0.3670 0.3374 0.3669 0.0316  0.0069  0.0263  97  ASP A C   
741  O O   . ASP A 100 ? 0.3493 0.3425 0.3578 0.0363  0.0048  0.0262  97  ASP A O   
742  C CB  . ASP A 100 ? 0.3978 0.3231 0.3937 0.0449  0.0117  0.0264  97  ASP A CB  
743  C CG  . ASP A 100 ? 0.4813 0.3878 0.4793 0.0538  0.0155  0.0174  97  ASP A CG  
744  O OD1 . ASP A 100 ? 0.4992 0.3919 0.4945 0.0453  0.0182  0.0072  97  ASP A OD1 
745  O OD2 . ASP A 100 ? 0.4700 0.3769 0.4729 0.0696  0.0155  0.0192  97  ASP A OD2 
746  N N   . PHE A 101 ? 0.3368 0.3017 0.3294 0.0239  0.0054  0.0316  98  PHE A N   
747  C CA  . PHE A 101 ? 0.3468 0.3312 0.3392 0.0209  0.0006  0.0349  98  PHE A CA  
748  C C   . PHE A 101 ? 0.3264 0.3279 0.3260 0.0133  0.0002  0.0278  98  PHE A C   
749  O O   . PHE A 101 ? 0.3244 0.3449 0.3303 0.0129  -0.0041 0.0278  98  PHE A O   
750  C CB  . PHE A 101 ? 0.3345 0.3104 0.3156 0.0146  0.0007  0.0404  98  PHE A CB  
751  C CG  . PHE A 101 ? 0.3877 0.3519 0.3602 0.0224  0.0002  0.0521  98  PHE A CG  
752  C CD1 . PHE A 101 ? 0.4247 0.3896 0.4004 0.0361  -0.0027 0.0572  98  PHE A CD1 
753  C CD2 . PHE A 101 ? 0.4476 0.4028 0.4088 0.0172  0.0029  0.0594  98  PHE A CD2 
754  C CE1 . PHE A 101 ? 0.4332 0.3861 0.3998 0.0451  -0.0035 0.0705  98  PHE A CE1 
755  C CE2 . PHE A 101 ? 0.4272 0.3713 0.3783 0.0246  0.0032  0.0735  98  PHE A CE2 
756  C CZ  . PHE A 101 ? 0.4452 0.3868 0.3986 0.0389  -0.0004 0.0796  98  PHE A CZ  
757  N N   . ALA A 102 ? 0.2994 0.2949 0.2987 0.0071  0.0042  0.0221  99  ALA A N   
758  C CA  . ALA A 102 ? 0.2945 0.3039 0.2999 0.0015  0.0046  0.0182  99  ALA A CA  
759  C C   . ALA A 102 ? 0.3180 0.3442 0.3338 0.0069  0.0053  0.0181  99  ALA A C   
760  O O   . ALA A 102 ? 0.2820 0.3240 0.3066 0.0027  0.0038  0.0189  99  ALA A O   
761  C CB  . ALA A 102 ? 0.3199 0.3217 0.3214 -0.0033 0.0081  0.0133  99  ALA A CB  
762  N N   . LEU A 103 ? 0.3145 0.3376 0.3309 0.0160  0.0083  0.0165  100 LEU A N   
763  C CA  . LEU A 103 ? 0.2881 0.3308 0.3155 0.0232  0.0103  0.0164  100 LEU A CA  
764  C C   . LEU A 103 ? 0.2920 0.3521 0.3299 0.0252  0.0046  0.0212  100 LEU A C   
765  O O   . LEU A 103 ? 0.2873 0.3698 0.3383 0.0212  0.0044  0.0218  100 LEU A O   
766  C CB  . LEU A 103 ? 0.3026 0.3361 0.3277 0.0354  0.0142  0.0124  100 LEU A CB  
767  C CG  . LEU A 103 ? 0.3098 0.3320 0.3258 0.0336  0.0190  0.0043  100 LEU A CG  
768  C CD1 . LEU A 103 ? 0.3362 0.3404 0.3484 0.0451  0.0214  -0.0023 100 LEU A CD1 
769  C CD2 . LEU A 103 ? 0.3000 0.3446 0.3194 0.0323  0.0240  0.0026  100 LEU A CD2 
770  N N   . LYS A 104 ? 0.2866 0.3378 0.3191 0.0312  -0.0001 0.0251  101 LYS A N   
771  C CA  . LYS A 104 ? 0.2676 0.3382 0.3079 0.0348  -0.0074 0.0291  101 LYS A CA  
772  C C   . LYS A 104 ? 0.2955 0.3765 0.3379 0.0220  -0.0122 0.0271  101 LYS A C   
773  O O   . LYS A 104 ? 0.2742 0.3792 0.3303 0.0199  -0.0172 0.0261  101 LYS A O   
774  C CB  . LYS A 104 ? 0.3042 0.3613 0.3340 0.0449  -0.0112 0.0358  101 LYS A CB  
775  C CG  . LYS A 104 ? 0.3051 0.3859 0.3422 0.0533  -0.0198 0.0403  101 LYS A CG  
776  C CD  . LYS A 104 ? 0.3406 0.4071 0.3630 0.0632  -0.0238 0.0502  101 LYS A CD  
777  C CE  . LYS A 104 ? 0.3917 0.4860 0.4217 0.0753  -0.0335 0.0552  101 LYS A CE  
778  N NZ  . LYS A 104 ? 0.4250 0.5231 0.4666 0.0925  -0.0316 0.0581  101 LYS A NZ  
779  N N   . LEU A 105 ? 0.2702 0.3342 0.3009 0.0133  -0.0109 0.0254  102 LEU A N   
780  C CA  . LEU A 105 ? 0.2672 0.3377 0.2996 0.0027  -0.0151 0.0217  102 LEU A CA  
781  C C   . LEU A 105 ? 0.2506 0.3346 0.2994 -0.0051 -0.0131 0.0190  102 LEU A C   
782  O O   . LEU A 105 ? 0.2525 0.3491 0.3112 -0.0122 -0.0183 0.0156  102 LEU A O   
783  C CB  . LEU A 105 ? 0.3067 0.3579 0.3254 -0.0031 -0.0126 0.0202  102 LEU A CB  
784  C CG  . LEU A 105 ? 0.2737 0.3282 0.2922 -0.0115 -0.0166 0.0148  102 LEU A CG  
785  C CD1 . LEU A 105 ? 0.3222 0.3650 0.3242 -0.0114 -0.0161 0.0149  102 LEU A CD1 
786  C CD2 . LEU A 105 ? 0.2891 0.3405 0.3161 -0.0194 -0.0129 0.0119  102 LEU A CD2 
787  N N   . SER A 106 ? 0.2358 0.3178 0.2876 -0.0043 -0.0056 0.0203  103 SER A N   
788  C CA  . SER A 106 ? 0.2379 0.3327 0.3039 -0.0117 -0.0019 0.0210  103 SER A CA  
789  C C   . SER A 106 ? 0.2327 0.3549 0.3187 -0.0113 -0.0045 0.0217  103 SER A C   
790  O O   . SER A 106 ? 0.2404 0.3750 0.3420 -0.0211 -0.0029 0.0226  103 SER A O   
791  C CB  . SER A 106 ? 0.2792 0.3704 0.3409 -0.0086 0.0070  0.0230  103 SER A CB  
792  O OG  . SER A 106 ? 0.2301 0.3340 0.2967 0.0019  0.0103  0.0234  103 SER A OG  
793  N N   . LEU A 107 ? 0.2331 0.3654 0.3204 -0.0002 -0.0082 0.0222  104 LEU A N   
794  C CA  . LEU A 107 ? 0.2274 0.3908 0.3356 0.0017  -0.0123 0.0224  104 LEU A CA  
795  C C   . LEU A 107 ? 0.2185 0.3915 0.3313 -0.0049 -0.0239 0.0182  104 LEU A C   
796  O O   . LEU A 107 ? 0.2238 0.4261 0.3572 -0.0071 -0.0291 0.0165  104 LEU A O   
797  C CB  . LEU A 107 ? 0.2235 0.3944 0.3314 0.0194  -0.0122 0.0249  104 LEU A CB  
798  C CG  . LEU A 107 ? 0.2556 0.4149 0.3566 0.0279  -0.0016 0.0256  104 LEU A CG  
799  C CD1 . LEU A 107 ? 0.2752 0.4363 0.3758 0.0466  -0.0023 0.0269  104 LEU A CD1 
800  C CD2 . LEU A 107 ? 0.2204 0.4009 0.3372 0.0216  0.0071  0.0263  104 LEU A CD2 
801  N N   . ASN A 108 ? 0.2359 0.3877 0.3303 -0.0079 -0.0279 0.0155  105 ASN A N   
802  C CA  . ASN A 108 ? 0.2589 0.4186 0.3514 -0.0117 -0.0391 0.0096  105 ASN A CA  
803  C C   . ASN A 108 ? 0.2459 0.3940 0.3383 -0.0262 -0.0403 0.0020  105 ASN A C   
804  O O   . ASN A 108 ? 0.2476 0.4050 0.3416 -0.0311 -0.0500 -0.0063 105 ASN A O   
805  C CB  . ASN A 108 ? 0.2758 0.4234 0.3446 -0.0005 -0.0429 0.0127  105 ASN A CB  
806  C CG  . ASN A 108 ? 0.2810 0.4434 0.3520 0.0150  -0.0462 0.0195  105 ASN A CG  
807  O OD1 . ASN A 108 ? 0.2913 0.4747 0.3642 0.0196  -0.0566 0.0187  105 ASN A OD1 
808  N ND2 . ASN A 108 ? 0.2715 0.4228 0.3413 0.0243  -0.0380 0.0256  105 ASN A ND2 
809  N N   . ARG A 109 ? 0.2670 0.3954 0.3570 -0.0318 -0.0316 0.0040  106 ARG A N   
810  C CA  . ARG A 109 ? 0.2511 0.3626 0.3394 -0.0425 -0.0314 -0.0018 106 ARG A CA  
811  C C   . ARG A 109 ? 0.2641 0.3675 0.3615 -0.0483 -0.0218 0.0044  106 ARG A C   
812  O O   . ARG A 109 ? 0.2561 0.3604 0.3505 -0.0419 -0.0146 0.0117  106 ARG A O   
813  C CB  . ARG A 109 ? 0.2789 0.3694 0.3435 -0.0377 -0.0309 -0.0037 106 ARG A CB  
814  C CG  . ARG A 109 ? 0.2750 0.3731 0.3257 -0.0312 -0.0392 -0.0075 106 ARG A CG  
815  C CD  . ARG A 109 ? 0.2976 0.4043 0.3539 -0.0389 -0.0483 -0.0198 106 ARG A CD  
816  N NE  . ARG A 109 ? 0.3182 0.4312 0.3556 -0.0323 -0.0556 -0.0244 106 ARG A NE  
817  C CZ  . ARG A 109 ? 0.3326 0.4651 0.3658 -0.0240 -0.0623 -0.0207 106 ARG A CZ  
818  N NH1 . ARG A 109 ? 0.2841 0.4336 0.3335 -0.0208 -0.0635 -0.0144 106 ARG A NH1 
819  N NH2 . ARG A 109 ? 0.3126 0.4494 0.3244 -0.0173 -0.0676 -0.0226 106 ARG A NH2 
820  N N   . ASP A 110 ? 0.2716 0.3656 0.3784 -0.0597 -0.0217 0.0013  107 ASP A N   
821  C CA  . ASP A 110 ? 0.2865 0.3721 0.4008 -0.0650 -0.0125 0.0098  107 ASP A CA  
822  C C   . ASP A 110 ? 0.3108 0.3744 0.4054 -0.0585 -0.0075 0.0132  107 ASP A C   
823  O O   . ASP A 110 ? 0.2896 0.3364 0.3754 -0.0588 -0.0106 0.0073  107 ASP A O   
824  C CB  . ASP A 110 ? 0.2481 0.3270 0.3806 -0.0795 -0.0140 0.0068  107 ASP A CB  
825  C CG  . ASP A 110 ? 0.3230 0.4271 0.4804 -0.0891 -0.0187 0.0032  107 ASP A CG  
826  O OD1 . ASP A 110 ? 0.2976 0.4275 0.4622 -0.0844 -0.0173 0.0075  107 ASP A OD1 
827  O OD2 . ASP A 110 ? 0.3998 0.4983 0.5717 -0.1017 -0.0237 -0.0047 107 ASP A OD2 
828  N N   . VAL A 111 ? 0.2842 0.3502 0.3726 -0.0525 -0.0001 0.0215  108 VAL A N   
829  C CA  . VAL A 111 ? 0.2646 0.3142 0.3367 -0.0471 0.0035  0.0242  108 VAL A CA  
830  C C   . VAL A 111 ? 0.2980 0.3477 0.3734 -0.0491 0.0113  0.0346  108 VAL A C   
831  O O   . VAL A 111 ? 0.2562 0.3210 0.3436 -0.0525 0.0160  0.0407  108 VAL A O   
832  C CB  . VAL A 111 ? 0.2490 0.2996 0.3060 -0.0372 0.0039  0.0225  108 VAL A CB  
833  C CG1 . VAL A 111 ? 0.2834 0.3316 0.3341 -0.0349 -0.0028 0.0155  108 VAL A CG1 
834  C CG2 . VAL A 111 ? 0.2644 0.3310 0.3253 -0.0322 0.0081  0.0261  108 VAL A CG2 
835  N N   . LYS A 112 ? 0.2728 0.3079 0.3374 -0.0463 0.0129  0.0376  109 LYS A N   
836  C CA  . LYS A 112 ? 0.2712 0.3071 0.3340 -0.0456 0.0199  0.0492  109 LYS A CA  
837  C C   . LYS A 112 ? 0.2818 0.3297 0.3314 -0.0371 0.0238  0.0506  109 LYS A C   
838  O O   . LYS A 112 ? 0.2810 0.3367 0.3272 -0.0355 0.0302  0.0600  109 LYS A O   
839  C CB  . LYS A 112 ? 0.2929 0.3101 0.3501 -0.0442 0.0188  0.0522  109 LYS A CB  
840  C CG  . LYS A 112 ? 0.3552 0.3561 0.4260 -0.0521 0.0160  0.0506  109 LYS A CG  
841  C CD  . LYS A 112 ? 0.4034 0.4057 0.4892 -0.0610 0.0221  0.0628  109 LYS A CD  
842  C CE  . LYS A 112 ? 0.4321 0.4113 0.5315 -0.0691 0.0206  0.0634  109 LYS A CE  
843  N NZ  . LYS A 112 ? 0.4872 0.4685 0.6035 -0.0800 0.0278  0.0773  109 LYS A NZ  
844  N N   . GLY A 113 ? 0.2755 0.3239 0.3167 -0.0317 0.0203  0.0414  110 GLY A N   
845  C CA  . GLY A 113 ? 0.2773 0.3325 0.3060 -0.0240 0.0230  0.0394  110 GLY A CA  
846  C C   . GLY A 113 ? 0.2635 0.3125 0.2867 -0.0204 0.0185  0.0296  110 GLY A C   
847  O O   . GLY A 113 ? 0.2776 0.3186 0.3035 -0.0232 0.0138  0.0261  110 GLY A O   
848  N N   . ILE A 114 ? 0.2934 0.3454 0.3078 -0.0141 0.0204  0.0253  111 ILE A N   
849  C CA  . ILE A 114 ? 0.2661 0.3098 0.2760 -0.0106 0.0178  0.0176  111 ILE A CA  
850  C C   . ILE A 114 ? 0.2760 0.3147 0.2741 -0.0081 0.0178  0.0116  111 ILE A C   
851  O O   . ILE A 114 ? 0.2852 0.3330 0.2771 -0.0046 0.0210  0.0111  111 ILE A O   
852  C CB  . ILE A 114 ? 0.2712 0.3228 0.2863 -0.0043 0.0201  0.0163  111 ILE A CB  
853  C CG1 . ILE A 114 ? 0.3009 0.3640 0.3308 -0.0076 0.0190  0.0214  111 ILE A CG1 
854  C CG2 . ILE A 114 ? 0.3192 0.3572 0.3297 0.0001  0.0175  0.0107  111 ILE A CG2 
855  C CD1 . ILE A 114 ? 0.2933 0.3751 0.3325 -0.0013 0.0234  0.0225  111 ILE A CD1 
856  N N   . VAL A 115 ? 0.3031 0.3294 0.2980 -0.0102 0.0144  0.0066  112 VAL A N   
857  C CA  . VAL A 115 ? 0.3144 0.3358 0.3015 -0.0096 0.0135  -0.0017 112 VAL A CA  
858  C C   . VAL A 115 ? 0.3113 0.3182 0.2991 -0.0085 0.0134  -0.0064 112 VAL A C   
859  O O   . VAL A 115 ? 0.3138 0.3126 0.3049 -0.0116 0.0120  -0.0027 112 VAL A O   
860  C CB  . VAL A 115 ? 0.3272 0.3486 0.3132 -0.0148 0.0101  -0.0025 112 VAL A CB  
861  C CG1 . VAL A 115 ? 0.3245 0.3447 0.3052 -0.0157 0.0081  -0.0128 112 VAL A CG1 
862  C CG2 . VAL A 115 ? 0.3042 0.3367 0.2901 -0.0140 0.0101  0.0049  112 VAL A CG2 
863  N N   . THR A 116 ? 0.3278 0.3303 0.3115 -0.0032 0.0151  -0.0141 113 THR A N   
864  C CA  . THR A 116 ? 0.3531 0.3360 0.3377 -0.0019 0.0151  -0.0183 113 THR A CA  
865  C C   . THR A 116 ? 0.3628 0.3361 0.3436 -0.0071 0.0133  -0.0294 113 THR A C   
866  O O   . THR A 116 ? 0.3474 0.3305 0.3222 -0.0056 0.0127  -0.0379 113 THR A O   
867  C CB  . THR A 116 ? 0.3205 0.3011 0.3060 0.0092  0.0182  -0.0203 113 THR A CB  
868  O OG1 . THR A 116 ? 0.3890 0.3782 0.3683 0.0148  0.0207  -0.0301 113 THR A OG1 
869  C CG2 . THR A 116 ? 0.3572 0.3525 0.3499 0.0133  0.0190  -0.0102 113 THR A CG2 
870  N N   . MET A 117 ? 0.3582 0.3140 0.3426 -0.0137 0.0126  -0.0295 114 MET A N   
871  C CA  . MET A 117 ? 0.3313 0.2799 0.3166 -0.0221 0.0104  -0.0403 114 MET A CA  
872  C C   . MET A 117 ? 0.4000 0.3202 0.3882 -0.0225 0.0124  -0.0434 114 MET A C   
873  O O   . MET A 117 ? 0.4044 0.3118 0.3967 -0.0262 0.0143  -0.0331 114 MET A O   
874  C CB  . MET A 117 ? 0.3768 0.3341 0.3676 -0.0325 0.0085  -0.0356 114 MET A CB  
875  C CG  . MET A 117 ? 0.4054 0.3868 0.3937 -0.0319 0.0054  -0.0362 114 MET A CG  
876  S SD  . MET A 117 ? 0.4297 0.4234 0.4255 -0.0390 0.0044  -0.0285 114 MET A SD  
877  C CE  . MET A 117 ? 0.4224 0.4081 0.4185 -0.0362 0.0083  -0.0154 114 MET A CE  
878  N N   . CYS A 118 ? 0.3838 0.2937 0.3687 -0.0177 0.0123  -0.0571 115 CYS A N   
879  C CA  . CYS A 118 ? 0.4371 0.3151 0.4251 -0.0166 0.0142  -0.0623 115 CYS A CA  
880  C C   . CYS A 118 ? 0.4763 0.3417 0.4658 -0.0073 0.0177  -0.0470 115 CYS A C   
881  O O   . CYS A 118 ? 0.4530 0.2941 0.4467 -0.0108 0.0196  -0.0393 115 CYS A O   
882  C CB  . CYS A 118 ? 0.4531 0.3155 0.4494 -0.0330 0.0129  -0.0664 115 CYS A CB  
883  S SG  . CYS A 118 ? 0.4749 0.3592 0.4718 -0.0442 0.0063  -0.0852 115 CYS A SG  
884  N N   . ALA A 119 ? 0.4292 0.3137 0.4157 0.0045  0.0185  -0.0415 116 ALA A N   
885  C CA  . ALA A 119 ? 0.4190 0.2995 0.4078 0.0147  0.0200  -0.0279 116 ALA A CA  
886  C C   . ALA A 119 ? 0.4263 0.2863 0.4159 0.0287  0.0223  -0.0339 116 ALA A C   
887  O O   . ALA A 119 ? 0.4305 0.2971 0.4176 0.0364  0.0236  -0.0474 116 ALA A O   
888  C CB  . ALA A 119 ? 0.4111 0.3226 0.4003 0.0198  0.0194  -0.0208 116 ALA A CB  
889  N N   . PRO A 120 ? 0.4573 0.2924 0.4494 0.0336  0.0232  -0.0240 117 PRO A N   
890  C CA  . PRO A 120 ? 0.4575 0.2699 0.4515 0.0495  0.0254  -0.0291 117 PRO A CA  
891  C C   . PRO A 120 ? 0.4741 0.3115 0.4707 0.0672  0.0259  -0.0257 117 PRO A C   
892  O O   . PRO A 120 ? 0.4754 0.3402 0.4737 0.0668  0.0238  -0.0142 117 PRO A O   
893  C CB  . PRO A 120 ? 0.5001 0.2800 0.4956 0.0487  0.0261  -0.0141 117 PRO A CB  
894  C CG  . PRO A 120 ? 0.4868 0.2882 0.4800 0.0405  0.0241  0.0028  117 PRO A CG  
895  C CD  . PRO A 120 ? 0.4707 0.2985 0.4628 0.0267  0.0227  -0.0065 117 PRO A CD  
896  N N   . MET A 121 ? 0.4641 0.2933 0.4625 0.0828  0.0287  -0.0368 118 MET A N   
897  C CA  . MET A 121 ? 0.4784 0.3311 0.4829 0.1015  0.0299  -0.0324 118 MET A CA  
898  C C   . MET A 121 ? 0.5319 0.3537 0.5406 0.1193  0.0309  -0.0294 118 MET A C   
899  O O   . MET A 121 ? 0.5618 0.3595 0.5698 0.1279  0.0341  -0.0448 118 MET A O   
900  C CB  . MET A 121 ? 0.4742 0.3546 0.4782 0.1080  0.0339  -0.0474 118 MET A CB  
901  C CG  . MET A 121 ? 0.4144 0.3307 0.4166 0.0947  0.0332  -0.0437 118 MET A CG  
902  S SD  . MET A 121 ? 0.4942 0.4489 0.5089 0.1002  0.0319  -0.0269 118 MET A SD  
903  C CE  . MET A 121 ? 0.4279 0.3760 0.4396 0.0818  0.0253  -0.0127 118 MET A CE  
904  N N   . GLY A 122 ? 0.5047 0.3270 0.5171 0.1261  0.0277  -0.0103 119 GLY A N   
905  C CA  . GLY A 122 ? 0.5588 0.3479 0.5743 0.1442  0.0285  -0.0052 119 GLY A CA  
906  C C   . GLY A 122 ? 0.6052 0.3590 0.6154 0.1347  0.0270  0.0109  119 GLY A C   
907  O O   . GLY A 122 ? 0.6211 0.3660 0.6258 0.1132  0.0272  0.0105  119 GLY A O   
908  N N   . GLY A 123 ? 0.6423 0.3783 0.6544 0.1517  0.0257  0.0269  120 GLY A N   
909  C CA  . GLY A 123 ? 0.6576 0.3686 0.6628 0.1441  0.0246  0.0481  120 GLY A CA  
910  C C   . GLY A 123 ? 0.7805 0.4326 0.7854 0.1453  0.0290  0.0507  120 GLY A C   
911  O O   . GLY A 123 ? 0.8241 0.4529 0.8253 0.1522  0.0288  0.0729  120 GLY A O   
912  N N   . LYS A 124 ? 0.7957 0.4228 0.8040 0.1382  0.0328  0.0285  121 LYS A N   
913  C CA  . LYS A 124 ? 0.8728 0.4406 0.8831 0.1344  0.0370  0.0280  121 LYS A CA  
914  C C   . LYS A 124 ? 0.9022 0.4573 0.9085 0.1081  0.0387  0.0417  121 LYS A C   
915  O O   . LYS A 124 ? 0.8504 0.4260 0.8561 0.0865  0.0383  0.0307  121 LYS A O   
916  C CB  . LYS A 124 ? 0.9224 0.4726 0.9372 0.1326  0.0392  -0.0036 121 LYS A CB  
917  C CG  . LYS A 124 ? 0.9880 0.4886 1.0062 0.1127  0.0422  -0.0134 121 LYS A CG  
918  C CD  . LYS A 124 ? 1.0207 0.4797 1.0445 0.1280  0.0444  -0.0350 121 LYS A CD  
919  C CE  . LYS A 124 ? 1.1433 0.5697 1.1712 0.1060  0.0452  -0.0600 121 LYS A CE  
920  N NZ  . LYS A 124 ? 1.1741 0.5642 1.2071 0.0828  0.0464  -0.0442 121 LYS A NZ  
921  N N   . THR A 125 ? 0.8895 0.4145 0.8931 0.1110  0.0409  0.0676  122 THR A N   
922  C CA  . THR A 125 ? 0.9224 0.4343 0.9228 0.0872  0.0447  0.0835  122 THR A CA  
923  C C   . THR A 125 ? 0.9941 0.4442 1.0023 0.0772  0.0510  0.0839  122 THR A C   
924  O O   . THR A 125 ? 0.9367 0.3753 0.9472 0.0527  0.0556  0.0911  122 THR A O   
925  C CB  . THR A 125 ? 0.9125 0.4388 0.9015 0.0948  0.0439  0.1159  122 THR A CB  
926  O OG1 . THR A 125 ? 0.8967 0.3981 0.8846 0.1218  0.0430  0.1310  122 THR A OG1 
927  C CG2 . THR A 125 ? 0.8369 0.4246 0.8193 0.0969  0.0376  0.1144  122 THR A CG2 
928  N N   . GLU A 126 ? 1.0160 0.4313 1.0297 0.0949  0.0501  0.0758  123 GLU A N   
929  C CA  . GLU A 126 ? 1.0265 0.3959 1.0472 0.0833  0.0492  0.0709  123 GLU A CA  
930  C C   . GLU A 126 ? 1.0296 0.3934 1.0585 0.0574  0.0502  0.0429  123 GLU A C   
931  O O   . GLU A 126 ? 1.0142 0.4006 1.0447 0.0582  0.0502  0.0182  123 GLU A O   
932  C CB  . GLU A 126 ? 1.0791 0.4210 1.1033 0.1093  0.0448  0.0631  123 GLU A CB  
933  C CG  . GLU A 126 ? 1.1480 0.5012 1.1672 0.1394  0.0415  0.0871  123 GLU A CG  
934  C CD  . GLU A 126 ? 1.1955 0.6023 1.2077 0.1521  0.0414  0.0960  123 GLU A CD  
935  O OE1 . GLU A 126 ? 1.1078 0.5413 1.1214 0.1532  0.0433  0.0751  123 GLU A OE1 
936  O OE2 . GLU A 126 ? 1.2370 0.6597 1.2408 0.1608  0.0389  0.1240  123 GLU A OE2 
937  N N   . GLY A 127 ? 0.9788 0.3161 1.0125 0.0342  0.0509  0.0474  124 GLY A N   
938  C CA  . GLY A 127 ? 0.9735 0.3082 1.0163 0.0080  0.0500  0.0219  124 GLY A CA  
939  C C   . GLY A 127 ? 0.9517 0.3240 0.9969 -0.0154 0.0536  0.0275  124 GLY A C   
940  O O   . GLY A 127 ? 0.9132 0.2884 0.9570 -0.0272 0.0577  0.0534  124 GLY A O   
941  N N   . ALA A 128 ? 0.7946 0.4057 0.7956 -0.0004 0.0635  -0.0542 125 ALA A N   
942  C CA  . ALA A 128 ? 0.7786 0.4252 0.7811 -0.0174 0.0536  -0.0548 125 ALA A CA  
943  C C   . ALA A 128 ? 0.7458 0.4196 0.7490 -0.0078 0.0487  -0.0322 125 ALA A C   
944  O O   . ALA A 128 ? 0.7255 0.4132 0.7342 -0.0200 0.0478  -0.0247 125 ALA A O   
945  C CB  . ALA A 128 ? 0.7903 0.4665 0.7861 -0.0242 0.0439  -0.0746 125 ALA A CB  
946  N N   . ILE A 129 ? 0.7306 0.4137 0.7281 0.0129  0.0461  -0.0221 126 ILE A N   
947  C CA  . ILE A 129 ? 0.6982 0.4073 0.6918 0.0196  0.0410  -0.0038 126 ILE A CA  
948  C C   . ILE A 129 ? 0.7196 0.4081 0.7135 0.0200  0.0481  0.0170  126 ILE A C   
949  O O   . ILE A 129 ? 0.7049 0.4080 0.6965 0.0131  0.0483  0.0276  126 ILE A O   
950  C CB  . ILE A 129 ? 0.7135 0.4407 0.7007 0.0384  0.0349  -0.0002 126 ILE A CB  
951  C CG1 . ILE A 129 ? 0.7016 0.4548 0.6868 0.0356  0.0279  -0.0181 126 ILE A CG1 
952  C CG2 . ILE A 129 ? 0.6496 0.3960 0.6294 0.0443  0.0310  0.0188  126 ILE A CG2 
953  C CD1 . ILE A 129 ? 0.7055 0.4763 0.6863 0.0518  0.0230  -0.0165 126 ILE A CD1 
954  N N   . TYR A 130 ? 0.7619 0.4154 0.7587 0.0286  0.0555  0.0240  127 TYR A N   
955  C CA  . TYR A 130 ? 0.7460 0.3753 0.7432 0.0280  0.0632  0.0453  127 TYR A CA  
956  C C   . TYR A 130 ? 0.7412 0.3643 0.7437 0.0054  0.0690  0.0426  127 TYR A C   
957  O O   . TYR A 130 ? 0.7201 0.3544 0.7182 0.0000  0.0706  0.0577  127 TYR A O   
958  C CB  . TYR A 130 ? 0.7580 0.3465 0.7622 0.0403  0.0718  0.0509  127 TYR A CB  
959  C CG  . TYR A 130 ? 0.8081 0.3660 0.8142 0.0388  0.0809  0.0737  127 TYR A CG  
960  C CD1 . TYR A 130 ? 0.8277 0.3908 0.8268 0.0530  0.0782  0.1021  127 TYR A CD1 
961  C CD2 . TYR A 130 ? 0.8300 0.3539 0.8439 0.0218  0.0919  0.0675  127 TYR A CD2 
962  C CE1 . TYR A 130 ? 0.8254 0.3604 0.8243 0.0514  0.0866  0.1256  127 TYR A CE1 
963  C CE2 . TYR A 130 ? 0.9067 0.4006 0.9225 0.0197  0.1014  0.0899  127 TYR A CE2 
964  C CZ  . TYR A 130 ? 0.8899 0.3894 0.8978 0.0352  0.0989  0.1197  127 TYR A CZ  
965  O OH  . TYR A 130 ? 0.9318 0.4013 0.9400 0.0329  0.1086  0.1442  127 TYR A OH  
966  N N   . GLU A 131 ? 0.7506 0.3572 0.7622 -0.0094 0.0726  0.0228  128 GLU A N   
967  C CA  . GLU A 131 ? 0.7702 0.3732 0.7906 -0.0327 0.0777  0.0210  128 GLU A CA  
968  C C   . GLU A 131 ? 0.7678 0.4165 0.7904 -0.0418 0.0705  0.0193  128 GLU A C   
969  O O   . GLU A 131 ? 0.6979 0.3527 0.7280 -0.0557 0.0758  0.0276  128 GLU A O   
970  C CB  . GLU A 131 ? 0.7804 0.3582 0.8091 -0.0500 0.0817  -0.0016 128 GLU A CB  
971  C CG  . GLU A 131 ? 0.8857 0.4224 0.9116 -0.0388 0.0884  -0.0105 128 GLU A CG  
972  C CD  . GLU A 131 ? 1.0662 0.5925 1.0923 -0.0557 0.0884  -0.0412 128 GLU A CD  
973  O OE1 . GLU A 131 ? 1.0912 0.6147 1.1099 -0.0447 0.0871  -0.0562 128 GLU A OE1 
974  O OE2 . GLU A 131 ? 1.0987 0.6198 1.1320 -0.0812 0.0900  -0.0504 128 GLU A OE2 
975  N N   . GLY A 132 ? 0.7020 0.3826 0.7200 -0.0337 0.0601  0.0098  129 GLY A N   
976  C CA  . GLY A 132 ? 0.7142 0.4359 0.7358 -0.0386 0.0549  0.0109  129 GLY A CA  
977  C C   . GLY A 132 ? 0.6851 0.4151 0.6982 -0.0312 0.0595  0.0313  129 GLY A C   
978  O O   . GLY A 132 ? 0.6339 0.3837 0.6537 -0.0404 0.0634  0.0362  129 GLY A O   
979  N N   . PHE A 133 ? 0.6949 0.4113 0.6931 -0.0150 0.0595  0.0437  130 PHE A N   
980  C CA  . PHE A 133 ? 0.6588 0.3808 0.6431 -0.0100 0.0634  0.0633  130 PHE A CA  
981  C C   . PHE A 133 ? 0.7368 0.4395 0.7241 -0.0222 0.0755  0.0769  130 PHE A C   
982  O O   . PHE A 133 ? 0.6864 0.4036 0.6687 -0.0281 0.0818  0.0860  130 PHE A O   
983  C CB  . PHE A 133 ? 0.6324 0.3458 0.6017 0.0084  0.0584  0.0749  130 PHE A CB  
984  C CG  . PHE A 133 ? 0.6848 0.4114 0.6339 0.0130  0.0584  0.0921  130 PHE A CG  
985  C CD1 . PHE A 133 ? 0.7022 0.4499 0.6457 0.0039  0.0629  0.0914  130 PHE A CD1 
986  C CD2 . PHE A 133 ? 0.7225 0.4417 0.6582 0.0262  0.0540  0.1089  130 PHE A CD2 
987  C CE1 . PHE A 133 ? 0.7211 0.4783 0.6411 0.0063  0.0643  0.1045  130 PHE A CE1 
988  C CE2 . PHE A 133 ? 0.7099 0.4428 0.6229 0.0277  0.0524  0.1238  130 PHE A CE2 
989  C CZ  . PHE A 133 ? 0.7201 0.4702 0.6229 0.0169  0.0581  0.1202  130 PHE A CZ  
990  N N   . LEU A 134 ? 0.6998 0.3680 0.6952 -0.0265 0.0807  0.0782  131 LEU A N   
991  C CA  . LEU A 134 ? 0.7217 0.3687 0.7214 -0.0396 0.0931  0.0919  131 LEU A CA  
992  C C   . LEU A 134 ? 0.7504 0.4178 0.7673 -0.0600 0.0978  0.0830  131 LEU A C   
993  O O   . LEU A 134 ? 0.7211 0.3931 0.7379 -0.0689 0.1080  0.0962  131 LEU A O   
994  C CB  . LEU A 134 ? 0.8038 0.4058 0.8110 -0.0407 0.0987  0.0929  131 LEU A CB  
995  C CG  . LEU A 134 ? 0.8468 0.4265 0.8440 -0.0190 0.0963  0.1052  131 LEU A CG  
996  C CD1 . LEU A 134 ? 0.8672 0.3971 0.8736 -0.0217 0.1074  0.1122  131 LEU A CD1 
997  C CD2 . LEU A 134 ? 0.8678 0.4631 0.8450 -0.0078 0.0940  0.1295  131 LEU A CD2 
998  N N   . GLU A 135 ? 0.6937 0.3754 0.7261 -0.0681 0.0907  0.0616  132 GLU A N   
999  C CA  . GLU A 135 ? 0.6941 0.4021 0.7472 -0.0870 0.0929  0.0548  132 GLU A CA  
1000 C C   . GLU A 135 ? 0.6531 0.3987 0.7043 -0.0817 0.0942  0.0613  132 GLU A C   
1001 O O   . GLU A 135 ? 0.6848 0.4463 0.7497 -0.0935 0.1037  0.0678  132 GLU A O   
1002 C CB  . GLU A 135 ? 0.7654 0.4853 0.8326 -0.0964 0.0821  0.0318  132 GLU A CB  
1003 C CG  . GLU A 135 ? 0.8511 0.5890 0.9445 -0.1211 0.0841  0.0262  132 GLU A CG  
1004 C CD  . GLU A 135 ? 0.9003 0.6839 1.0082 -0.1251 0.0719  0.0139  132 GLU A CD  
1005 O OE1 . GLU A 135 ? 0.9790 0.7780 1.0752 -0.1086 0.0631  0.0094  132 GLU A OE1 
1006 O OE2 . GLU A 135 ? 0.9303 0.7360 1.0629 -0.1451 0.0710  0.0102  132 GLU A OE2 
1007 N N   . TYR A 136 ? 0.6429 0.4022 0.6783 -0.0644 0.0864  0.0594  133 TYR A N   
1008 C CA  . TYR A 136 ? 0.6206 0.4086 0.6503 -0.0585 0.0897  0.0645  133 TYR A CA  
1009 C C   . TYR A 136 ? 0.6347 0.4129 0.6515 -0.0610 0.1042  0.0829  133 TYR A C   
1010 O O   . TYR A 136 ? 0.6458 0.4442 0.6705 -0.0672 0.1148  0.0866  133 TYR A O   
1011 C CB  . TYR A 136 ? 0.6057 0.4013 0.6164 -0.0408 0.0796  0.0606  133 TYR A CB  
1012 C CG  . TYR A 136 ? 0.6392 0.4545 0.6370 -0.0345 0.0848  0.0660  133 TYR A CG  
1013 C CD1 . TYR A 136 ? 0.5698 0.4145 0.5842 -0.0373 0.0877  0.0595  133 TYR A CD1 
1014 C CD2 . TYR A 136 ? 0.6351 0.4396 0.6041 -0.0262 0.0870  0.0776  133 TYR A CD2 
1015 C CE1 . TYR A 136 ? 0.6040 0.4619 0.6063 -0.0315 0.0952  0.0623  133 TYR A CE1 
1016 C CE2 . TYR A 136 ? 0.5992 0.4191 0.5525 -0.0229 0.0926  0.0794  133 TYR A CE2 
1017 C CZ  . TYR A 136 ? 0.5911 0.4351 0.5610 -0.0254 0.0981  0.0707  133 TYR A CZ  
1018 O OH  . TYR A 136 ? 0.6117 0.4663 0.5663 -0.0221 0.1066  0.0705  133 TYR A OH  
1019 N N   . ALA A 137 ? 0.6684 0.4162 0.6659 -0.0559 0.1057  0.0958  134 ALA A N   
1020 C CA  . ALA A 137 ? 0.7335 0.4710 0.7139 -0.0587 0.1187  0.1155  134 ALA A CA  
1021 C C   . ALA A 137 ? 0.7553 0.4871 0.7556 -0.0773 0.1326  0.1210  134 ALA A C   
1022 O O   . ALA A 137 ? 0.7547 0.4954 0.7495 -0.0835 0.1467  0.1318  134 ALA A O   
1023 C CB  . ALA A 137 ? 0.7791 0.4874 0.7369 -0.0480 0.1148  0.1309  134 ALA A CB  
1024 N N   . ARG A 138 ? 0.7255 0.4426 0.7485 -0.0878 0.1301  0.1130  135 ARG A N   
1025 C CA  . ARG A 138 ? 0.7349 0.4480 0.7798 -0.1084 0.1426  0.1174  135 ARG A CA  
1026 C C   . ARG A 138 ? 0.7179 0.4731 0.7868 -0.1178 0.1472  0.1101  135 ARG A C   
1027 O O   . ARG A 138 ? 0.7223 0.4860 0.8004 -0.1289 0.1628  0.1208  135 ARG A O   
1028 C CB  . ARG A 138 ? 0.7547 0.4409 0.8170 -0.1199 0.1384  0.1076  135 ARG A CB  
1029 C CG  . ARG A 138 ? 0.8493 0.4881 0.8952 -0.1139 0.1418  0.1208  135 ARG A CG  
1030 C CD  . ARG A 138 ? 0.9390 0.5444 1.0000 -0.1244 0.1402  0.1085  135 ARG A CD  
1031 N NE  . ARG A 138 ? 1.0383 0.6081 1.0832 -0.1064 0.1365  0.1129  135 ARG A NE  
1032 C CZ  . ARG A 138 ? 1.0876 0.6151 1.1262 -0.1037 0.1460  0.1315  135 ARG A CZ  
1033 N NH1 . ARG A 138 ? 1.0611 0.5735 1.1048 -0.1193 0.1601  0.1476  135 ARG A NH1 
1034 N NH2 . ARG A 138 ? 1.1004 0.6008 1.1288 -0.0843 0.1420  0.1358  135 ARG A NH2 
1035 N N   . ASN A 139 ? 0.6968 0.4797 0.7778 -0.1128 0.1347  0.0936  136 ASN A N   
1036 C CA  . ASN A 139 ? 0.6983 0.5230 0.8070 -0.1195 0.1387  0.0894  136 ASN A CA  
1037 C C   . ASN A 139 ? 0.6817 0.5222 0.7773 -0.1101 0.1525  0.0991  136 ASN A C   
1038 O O   . ASN A 139 ? 0.6918 0.5569 0.8097 -0.1182 0.1660  0.1034  136 ASN A O   
1039 C CB  . ASN A 139 ? 0.6771 0.5276 0.8005 -0.1154 0.1216  0.0723  136 ASN A CB  
1040 C CG  . ASN A 139 ? 0.7397 0.5786 0.8763 -0.1290 0.1098  0.0599  136 ASN A CG  
1041 O OD1 . ASN A 139 ? 0.8250 0.6680 0.9580 -0.1235 0.0947  0.0462  136 ASN A OD1 
1042 N ND2 . ASN A 139 ? 0.7814 0.6045 0.9319 -0.1482 0.1178  0.0640  136 ASN A ND2 
1043 N N   . PHE A 140 ? 0.6854 0.5129 0.7455 -0.0942 0.1503  0.1022  137 PHE A N   
1044 C CA  . PHE A 140 ? 0.7103 0.5491 0.7526 -0.0880 0.1647  0.1092  137 PHE A CA  
1045 C C   . PHE A 140 ? 0.7822 0.6085 0.8175 -0.0993 0.1843  0.1257  137 PHE A C   
1046 O O   . PHE A 140 ? 0.7629 0.6077 0.8040 -0.1027 0.2024  0.1295  137 PHE A O   
1047 C CB  . PHE A 140 ? 0.7184 0.5452 0.7214 -0.0723 0.1569  0.1093  137 PHE A CB  
1048 C CG  . PHE A 140 ? 0.7758 0.6146 0.7584 -0.0674 0.1707  0.1111  137 PHE A CG  
1049 C CD1 . PHE A 140 ? 0.8154 0.6402 0.7675 -0.0712 0.1849  0.1250  137 PHE A CD1 
1050 C CD2 . PHE A 140 ? 0.8023 0.6643 0.7937 -0.0592 0.1699  0.0987  137 PHE A CD2 
1051 C CE1 . PHE A 140 ? 0.8390 0.6727 0.7684 -0.0686 0.1992  0.1239  137 PHE A CE1 
1052 C CE2 . PHE A 140 ? 0.8183 0.6865 0.7897 -0.0553 0.1850  0.0980  137 PHE A CE2 
1053 C CZ  . PHE A 140 ? 0.7662 0.6199 0.7052 -0.0606 0.1999  0.1093  137 PHE A CZ  
1054 N N   . LYS A 141 ? 0.7776 0.5716 0.8007 -0.1045 0.1827  0.1365  138 LYS A N   
1055 C CA  . LYS A 141 ? 0.8132 0.5929 0.8288 -0.1162 0.2013  0.1547  138 LYS A CA  
1056 C C   . LYS A 141 ? 0.8119 0.6115 0.8684 -0.1339 0.2144  0.1540  138 LYS A C   
1057 O O   . LYS A 141 ? 0.8395 0.6444 0.8946 -0.1421 0.2351  0.1660  138 LYS A O   
1058 C CB  . LYS A 141 ? 0.8451 0.5843 0.8445 -0.1170 0.1957  0.1674  138 LYS A CB  
1059 C CG  . LYS A 141 ? 0.8887 0.6126 0.8444 -0.1017 0.1894  0.1780  138 LYS A CG  
1060 C CD  . LYS A 141 ? 0.8924 0.5815 0.8409 -0.0954 0.1775  0.1861  138 LYS A CD  
1061 C CE  . LYS A 141 ? 0.9528 0.6285 0.8601 -0.0843 0.1751  0.2060  138 LYS A CE  
1062 N NZ  . LYS A 141 ? 0.9866 0.6882 0.8665 -0.0763 0.1728  0.2010  138 LYS A NZ  
1063 N N   . LYS A 142 ? 0.7283 0.5420 0.8213 -0.1408 0.2028  0.1403  139 LYS A N   
1064 C CA  . LYS A 142 ? 0.7934 0.6360 0.9298 -0.1577 0.2127  0.1394  139 LYS A CA  
1065 C C   . LYS A 142 ? 0.7880 0.6714 0.9385 -0.1501 0.2232  0.1366  139 LYS A C   
1066 O O   . LYS A 142 ? 0.8004 0.7051 0.9748 -0.1601 0.2422  0.1441  139 LYS A O   
1067 C CB  . LYS A 142 ? 0.7846 0.6347 0.9535 -0.1688 0.1952  0.1251  139 LYS A CB  
1068 C CG  . LYS A 142 ? 0.8672 0.7501 1.0838 -0.1896 0.2031  0.1259  139 LYS A CG  
1069 C CD  . LYS A 142 ? 0.8916 0.8042 1.1413 -0.1965 0.1834  0.1098  139 LYS A CD  
1070 C CE  . LYS A 142 ? 0.9660 0.8453 1.2052 -0.2042 0.1661  0.0978  139 LYS A CE  
1071 N NZ  . LYS A 142 ? 0.9804 0.8911 1.2477 -0.2137 0.1470  0.0817  139 LYS A NZ  
1072 N N   . TYR A 143 ? 0.7077 0.6015 0.8454 -0.1322 0.2126  0.1261  140 TYR A N   
1073 C CA  . TYR A 143 ? 0.7814 0.7077 0.9304 -0.1227 0.2245  0.1233  140 TYR A CA  
1074 C C   . TYR A 143 ? 0.8105 0.7275 0.9306 -0.1208 0.2494  0.1341  140 TYR A C   
1075 O O   . TYR A 143 ? 0.8534 0.7955 0.9914 -0.1197 0.2693  0.1353  140 TYR A O   
1076 C CB  . TYR A 143 ? 0.7528 0.6855 0.8904 -0.1048 0.2081  0.1104  140 TYR A CB  
1077 C CG  . TYR A 143 ? 0.8298 0.7758 0.9564 -0.0910 0.2226  0.1082  140 TYR A CG  
1078 C CD1 . TYR A 143 ? 0.8653 0.7875 0.9427 -0.0829 0.2291  0.1095  140 TYR A CD1 
1079 C CD2 . TYR A 143 ? 0.8212 0.8036 0.9871 -0.0867 0.2301  0.1049  140 TYR A CD2 
1080 C CE1 . TYR A 143 ? 0.8936 0.8240 0.9582 -0.0726 0.2439  0.1047  140 TYR A CE1 
1081 C CE2 . TYR A 143 ? 0.8421 0.8318 0.9990 -0.0735 0.2463  0.1017  140 TYR A CE2 
1082 C CZ  . TYR A 143 ? 0.8804 0.8420 0.9850 -0.0675 0.2538  0.1001  140 TYR A CZ  
1083 O OH  . TYR A 143 ? 0.8394 0.8041 0.9319 -0.0567 0.2713  0.0943  140 TYR A OH  
1084 N N   . GLU A 144 ? 0.8228 0.7047 0.8984 -0.1205 0.2496  0.1427  141 GLU A N   
1085 C CA  . GLU A 144 ? 0.8571 0.7282 0.8994 -0.1225 0.2723  0.1548  141 GLU A CA  
1086 C C   . GLU A 144 ? 0.8916 0.7673 0.9562 -0.1401 0.2934  0.1682  141 GLU A C   
1087 O O   . GLU A 144 ? 0.9397 0.8068 0.9765 -0.1439 0.3146  0.1798  141 GLU A O   
1088 C CB  . GLU A 144 ? 0.8852 0.7208 0.8752 -0.1178 0.2627  0.1634  141 GLU A CB  
1089 C CG  . GLU A 144 ? 0.8951 0.7291 0.8540 -0.1014 0.2490  0.1527  141 GLU A CG  
1090 C CD  . GLU A 144 ? 0.9263 0.7316 0.8375 -0.0973 0.2384  0.1638  141 GLU A CD  
1091 O OE1 . GLU A 144 ? 0.9138 0.6995 0.8294 -0.0977 0.2236  0.1703  141 GLU A OE1 
1092 O OE2 . GLU A 144 ? 0.9699 0.7729 0.8398 -0.0937 0.2450  0.1659  141 GLU A OE2 
1093 N N   . GLY A 145 ? 0.8847 0.7744 0.9970 -0.1526 0.2885  0.1671  142 GLY A N   
1094 C CA  . GLY A 145 ? 0.8695 0.7649 1.0066 -0.1716 0.3081  0.1800  142 GLY A CA  
1095 C C   . GLY A 145 ? 0.9185 0.7737 1.0271 -0.1824 0.3114  0.1965  142 GLY A C   
1096 O O   . GLY A 145 ? 0.9407 0.7953 1.0541 -0.1963 0.3335  0.2110  142 GLY A O   
1097 N N   . LYS A 146 ? 0.9404 0.7623 1.0213 -0.1757 0.2912  0.1961  143 LYS A N   
1098 C CA  . LYS A 146 ? 1.0117 0.7928 1.0657 -0.1826 0.2937  0.2144  143 LYS A CA  
1099 C C   . LYS A 146 ? 1.0157 0.7836 1.1063 -0.2018 0.2910  0.2163  143 LYS A C   
1100 O O   . LYS A 146 ? 1.0061 0.7862 1.1302 -0.2057 0.2757  0.1998  143 LYS A O   
1101 C CB  . LYS A 146 ? 0.9725 0.7253 0.9858 -0.1656 0.2739  0.2146  143 LYS A CB  
1102 C CG  . LYS A 146 ? 0.9839 0.7436 0.9530 -0.1510 0.2772  0.2160  143 LYS A CG  
1103 C CD  . LYS A 146 ? 0.9676 0.7044 0.9015 -0.1356 0.2561  0.2179  143 LYS A CD  
1104 C CE  . LYS A 146 ? 1.0047 0.7464 0.8900 -0.1264 0.2602  0.2222  143 LYS A CE  
1105 N NZ  . LYS A 146 ? 1.0436 0.7694 0.8986 -0.1122 0.2382  0.2251  143 LYS A NZ  
1106 N N   . ASP A 147 ? 1.0645 0.8066 1.1467 -0.2153 0.3063  0.2365  144 ASP A N   
1107 C CA  . ASP A 147 ? 1.1078 0.8299 1.2210 -0.2358 0.3060  0.2393  144 ASP A CA  
1108 C C   . ASP A 147 ? 1.1026 0.7870 1.2066 -0.2288 0.2839  0.2322  144 ASP A C   
1109 O O   . ASP A 147 ? 1.1022 0.7719 1.1722 -0.2082 0.2716  0.2323  144 ASP A O   
1110 C CB  . ASP A 147 ? 1.0989 0.7974 1.2014 -0.2508 0.3289  0.2651  144 ASP A CB  
1111 C CG  . ASP A 147 ? 1.2148 0.8799 1.2620 -0.2364 0.3301  0.2851  144 ASP A CG  
1112 O OD1 . ASP A 147 ? 1.2607 0.9434 1.2756 -0.2236 0.3355  0.2877  144 ASP A OD1 
1113 O OD2 . ASP A 147 ? 1.2486 0.8736 1.2841 -0.2367 0.3219  0.2960  144 ASP A OD2 
1114 N N   . GLN A 148 ? 1.1038 0.7720 1.2391 -0.2472 0.2801  0.2256  145 GLN A N   
1115 C CA  . GLN A 148 ? 1.1135 0.7452 1.2430 -0.2412 0.2618  0.2152  145 GLN A CA  
1116 C C   . GLN A 148 ? 1.1373 0.7181 1.2310 -0.2304 0.2652  0.2369  145 GLN A C   
1117 O O   . GLN A 148 ? 1.1093 0.6643 1.1880 -0.2145 0.2505  0.2316  145 GLN A O   
1118 C CB  . GLN A 148 ? 1.0573 0.6807 1.2256 -0.2664 0.2588  0.2011  145 GLN A CB  
1119 C CG  . GLN A 148 ? 1.0541 0.6490 1.2214 -0.2619 0.2395  0.1811  145 GLN A CG  
1120 C CD  . GLN A 148 ? 1.0530 0.6690 1.2041 -0.2370 0.2206  0.1657  145 GLN A CD  
1121 O OE1 . GLN A 148 ? 1.0605 0.7058 1.2312 -0.2408 0.2070  0.1439  145 GLN A OE1 
1122 N NE2 . GLN A 148 ? 1.0994 0.6987 1.2148 -0.2126 0.2185  0.1777  145 GLN A NE2 
1123 N N   . GLU A 149 ? 1.2142 0.7819 1.2948 -0.2380 0.2848  0.2628  146 GLU A N   
1124 C CA  . GLU A 149 ? 1.2564 0.7824 1.3023 -0.2261 0.2847  0.2864  146 GLU A CA  
1125 C C   . GLU A 149 ? 1.2172 0.7510 1.2226 -0.2012 0.2780  0.2949  146 GLU A C   
1126 O O   . GLU A 149 ? 1.2361 0.7412 1.2210 -0.1842 0.2665  0.3034  146 GLU A O   
1127 C CB  . GLU A 149 ? 1.3057 0.8284 1.3458 -0.2398 0.2988  0.3074  146 GLU A CB  
1128 C CG  . GLU A 149 ? 1.4020 0.9135 1.4789 -0.2639 0.3018  0.2994  146 GLU A CG  
1129 C CD  . GLU A 149 ? 1.4353 0.9007 1.5178 -0.2607 0.2890  0.2915  146 GLU A CD  
1130 O OE1 . GLU A 149 ? 1.4279 0.8611 1.4830 -0.2418 0.2831  0.3063  146 GLU A OE1 
1131 O OE2 . GLU A 149 ? 1.4257 0.8901 1.5402 -0.2763 0.2842  0.2690  146 GLU A OE2 
1132 N N   . THR A 150 ? 1.1642 0.7400 1.1582 -0.1983 0.2832  0.2911  147 THR A N   
1133 C CA  . THR A 150 ? 1.1675 0.7562 1.1218 -0.1767 0.2733  0.2934  147 THR A CA  
1134 C C   . THR A 150 ? 1.0570 0.6507 1.0173 -0.1599 0.2494  0.2710  147 THR A C   
1135 O O   . THR A 150 ? 1.0463 0.6284 0.9789 -0.1416 0.2363  0.2778  147 THR A O   
1136 C CB  . THR A 150 ? 1.1558 0.7854 1.0992 -0.1789 0.2866  0.2895  147 THR A CB  
1137 O OG1 . THR A 150 ? 1.2014 0.8250 1.1337 -0.1936 0.3104  0.3123  147 THR A OG1 
1138 C CG2 . THR A 150 ? 1.1228 0.7645 1.0238 -0.1595 0.2759  0.2884  147 THR A CG2 
1139 N N   . ILE A 151 ? 1.0923 0.7049 1.0891 -0.1665 0.2433  0.2456  148 ILE A N   
1140 C CA  . ILE A 151 ? 0.9948 0.6118 0.9977 -0.1526 0.2218  0.2240  148 ILE A CA  
1141 C C   . ILE A 151 ? 1.0255 0.5976 1.0224 -0.1443 0.2127  0.2306  148 ILE A C   
1142 O O   . ILE A 151 ? 0.9774 0.5448 0.9551 -0.1243 0.1988  0.2302  148 ILE A O   
1143 C CB  . ILE A 151 ? 0.9689 0.6121 1.0123 -0.1649 0.2174  0.1988  148 ILE A CB  
1144 C CG1 . ILE A 151 ? 0.9867 0.6771 1.0395 -0.1678 0.2261  0.1934  148 ILE A CG1 
1145 C CG2 . ILE A 151 ? 0.9423 0.5861 0.9892 -0.1520 0.1961  0.1776  148 ILE A CG2 
1146 C CD1 . ILE A 151 ? 0.9274 0.6501 1.0233 -0.1796 0.2211  0.1732  148 ILE A CD1 
1147 N N   . ASP A 152 ? 1.0335 0.5717 1.0488 -0.1596 0.2217  0.2369  149 ASP A N   
1148 C CA  . ASP A 152 ? 1.0734 0.5637 1.0869 -0.1516 0.2168  0.2429  149 ASP A CA  
1149 C C   . ASP A 152 ? 1.0830 0.5559 1.0622 -0.1322 0.2156  0.2716  149 ASP A C   
1150 O O   . ASP A 152 ? 1.0997 0.5598 1.0700 -0.1121 0.2027  0.2717  149 ASP A O   
1151 C CB  . ASP A 152 ? 1.0934 0.5468 1.1309 -0.1742 0.2305  0.2469  149 ASP A CB  
1152 C CG  . ASP A 152 ? 1.1244 0.5794 1.1940 -0.1896 0.2243  0.2155  149 ASP A CG  
1153 O OD1 . ASP A 152 ? 1.1078 0.6016 1.1839 -0.1857 0.2113  0.1928  149 ASP A OD1 
1154 O OD2 . ASP A 152 ? 1.1650 0.5815 1.2520 -0.2065 0.2323  0.2138  149 ASP A OD2 
1155 N N   . ASN A 153 ? 1.1254 0.6002 1.0852 -0.1383 0.2291  0.2971  150 ASN A N   
1156 C CA  . ASN A 153 ? 1.1266 0.5896 1.0507 -0.1222 0.2268  0.3271  150 ASN A CA  
1157 C C   . ASN A 153 ? 1.0797 0.5744 0.9807 -0.1021 0.2091  0.3191  150 ASN A C   
1158 O O   . ASN A 153 ? 1.0978 0.5805 0.9841 -0.0832 0.1969  0.3323  150 ASN A O   
1159 C CB  . ASN A 153 ? 1.1411 0.6111 1.0443 -0.1351 0.2430  0.3509  150 ASN A CB  
1160 C CG  . ASN A 153 ? 1.2309 0.6783 1.1558 -0.1538 0.2534  0.3564  150 ASN A CG  
1161 O OD1 . ASN A 153 ? 1.2122 0.6329 1.1661 -0.1585 0.2509  0.3442  150 ASN A OD1 
1162 N ND2 . ASN A 153 ? 1.2327 0.6909 1.1419 -0.1659 0.2657  0.3738  150 ASN A ND2 
1163 N N   . GLU A 154 ? 1.0460 0.5820 0.9463 -0.1060 0.2077  0.2979  151 GLU A N   
1164 C CA  . GLU A 154 ? 1.0097 0.5746 0.8871 -0.0895 0.1925  0.2897  151 GLU A CA  
1165 C C   . GLU A 154 ? 1.0090 0.5692 0.9029 -0.0744 0.1744  0.2720  151 GLU A C   
1166 O O   . GLU A 154 ? 1.0063 0.5737 0.8817 -0.0570 0.1602  0.2767  151 GLU A O   
1167 C CB  . GLU A 154 ? 1.0097 0.6148 0.8849 -0.0972 0.1985  0.2713  151 GLU A CB  
1168 C CG  . GLU A 154 ? 1.0373 0.6533 0.8791 -0.1049 0.2139  0.2894  151 GLU A CG  
1169 C CD  . GLU A 154 ? 1.0814 0.7334 0.9259 -0.1121 0.2247  0.2705  151 GLU A CD  
1170 O OE1 . GLU A 154 ? 1.0267 0.6968 0.9020 -0.1114 0.2193  0.2459  151 GLU A OE1 
1171 O OE2 . GLU A 154 ? 1.1027 0.7644 0.9184 -0.1183 0.2396  0.2811  151 GLU A OE2 
1172 N N   . MET A 155 ? 1.0085 0.5579 0.9366 -0.0819 0.1748  0.2517  152 MET A N   
1173 C CA  . MET A 155 ? 1.0134 0.5549 0.9557 -0.0689 0.1603  0.2341  152 MET A CA  
1174 C C   . MET A 155 ? 1.0315 0.5343 0.9705 -0.0541 0.1574  0.2534  152 MET A C   
1175 O O   . MET A 155 ? 1.0156 0.5180 0.9566 -0.0368 0.1448  0.2459  152 MET A O   
1176 C CB  . MET A 155 ? 0.9767 0.5157 0.9522 -0.0838 0.1622  0.2076  152 MET A CB  
1177 C CG  . MET A 155 ? 0.8717 0.4552 0.8579 -0.0915 0.1586  0.1844  152 MET A CG  
1178 S SD  . MET A 155 ? 0.8540 0.4768 0.8195 -0.0721 0.1437  0.1750  152 MET A SD  
1179 C CE  . MET A 155 ? 0.8639 0.4731 0.8404 -0.0586 0.1279  0.1569  152 MET A CE  
1180 N N   . ASP A 156 ? 1.0540 0.5242 0.9896 -0.0596 0.1696  0.2797  153 ASP A N   
1181 C CA  . ASP A 156 ? 1.0801 0.5151 1.0137 -0.0421 0.1669  0.3021  153 ASP A CA  
1182 C C   . ASP A 156 ? 1.0730 0.5302 0.9779 -0.0226 0.1539  0.3234  153 ASP A C   
1183 O O   . ASP A 156 ? 1.0720 0.5110 0.9793 -0.0034 0.1472  0.3399  153 ASP A O   
1184 C CB  . ASP A 156 ? 1.1319 0.5228 1.0705 -0.0522 0.1838  0.3276  153 ASP A CB  
1185 C CG  . ASP A 156 ? 1.1943 0.5692 1.1581 -0.0779 0.1977  0.3087  153 ASP A CG  
1186 O OD1 . ASP A 156 ? 1.2481 0.6222 1.2088 -0.0949 0.2085  0.3211  153 ASP A OD1 
1187 O OD2 . ASP A 156 ? 1.1920 0.5641 1.1780 -0.0821 0.1938  0.2781  153 ASP A OD2 
1188 N N   . HIS A 157 ? 1.0460 0.5424 0.9249 -0.0275 0.1506  0.3232  154 HIS A N   
1189 C CA  . HIS A 157 ? 1.0623 0.5843 0.9112 -0.0131 0.1366  0.3391  154 HIS A CA  
1190 C C   . HIS A 157 ? 1.0412 0.6012 0.8876 -0.0069 0.1226  0.3120  154 HIS A C   
1191 O O   . HIS A 157 ? 1.0107 0.5966 0.8310 0.0011  0.1107  0.3205  154 HIS A O   
1192 C CB  . HIS A 157 ? 1.0587 0.5926 0.8717 -0.0241 0.1443  0.3621  154 HIS A CB  
1193 C CG  . HIS A 157 ? 1.1309 0.6289 0.9418 -0.0291 0.1572  0.3945  154 HIS A CG  
1194 N ND1 . HIS A 157 ? 1.1743 0.6556 0.9941 -0.0492 0.1772  0.3945  154 HIS A ND1 
1195 C CD2 . HIS A 157 ? 1.1544 0.6361 0.9593 -0.0173 0.1495  0.4235  154 HIS A CD2 
1196 C CE1 . HIS A 157 ? 1.2252 0.6841 1.0425 -0.0507 0.1788  0.4182  154 HIS A CE1 
1197 N NE2 . HIS A 157 ? 1.2481 0.7065 1.0563 -0.0312 0.1619  0.4356  154 HIS A NE2 
1198 N N   . PHE A 158 ? 1.0098 0.5737 0.8816 -0.0115 0.1233  0.2806  155 PHE A N   
1199 C CA  . PHE A 158 ? 0.9595 0.5562 0.8320 -0.0055 0.1109  0.2554  155 PHE A CA  
1200 C C   . PHE A 158 ? 0.9910 0.5807 0.8757 0.0146  0.0977  0.2546  155 PHE A C   
1201 O O   . PHE A 158 ? 1.0187 0.5815 0.9291 0.0177  0.1010  0.2459  155 PHE A O   
1202 C CB  . PHE A 158 ? 0.9319 0.5370 0.8270 -0.0191 0.1172  0.2259  155 PHE A CB  
1203 C CG  . PHE A 158 ? 0.9342 0.5725 0.8307 -0.0143 0.1063  0.2014  155 PHE A CG  
1204 C CD1 . PHE A 158 ? 0.9071 0.5758 0.7806 -0.0159 0.1048  0.1997  155 PHE A CD1 
1205 C CD2 . PHE A 158 ? 0.8935 0.5304 0.8125 -0.0089 0.0989  0.1801  155 PHE A CD2 
1206 C CE1 . PHE A 158 ? 0.8987 0.5944 0.7747 -0.0116 0.0960  0.1781  155 PHE A CE1 
1207 C CE2 . PHE A 158 ? 0.8496 0.5163 0.7695 -0.0047 0.0894  0.1599  155 PHE A CE2 
1208 C CZ  . PHE A 158 ? 0.8595 0.5548 0.7593 -0.0057 0.0879  0.1596  155 PHE A CZ  
1209 N N   . LYS A 159 ? 0.9736 0.5875 0.8401 0.0274  0.0837  0.2636  156 LYS A N   
1210 C CA  . LYS A 159 ? 0.9535 0.5662 0.8322 0.0479  0.0714  0.2682  156 LYS A CA  
1211 C C   . LYS A 159 ? 0.8874 0.5312 0.7703 0.0528  0.0601  0.2422  156 LYS A C   
1212 O O   . LYS A 159 ? 0.8416 0.5162 0.7045 0.0560  0.0486  0.2459  156 LYS A O   
1213 C CB  . LYS A 159 ? 0.9556 0.5748 0.8150 0.0593  0.0622  0.3031  156 LYS A CB  
1214 C CG  . LYS A 159 ? 1.0123 0.6023 0.8640 0.0569  0.0717  0.3361  156 LYS A CG  
1215 C CD  . LYS A 159 ? 1.1471 0.6969 1.0185 0.0456  0.0905  0.3299  156 LYS A CD  
1216 C CE  . LYS A 159 ? 1.1692 0.6837 1.0755 0.0588  0.0943  0.3248  156 LYS A CE  
1217 N NZ  . LYS A 159 ? 1.1745 0.6473 1.0974 0.0442  0.1126  0.3189  156 LYS A NZ  
1218 N N   . PRO A 160 ? 0.8652 0.5014 0.7720 0.0529  0.0625  0.2163  157 PRO A N   
1219 C CA  . PRO A 160 ? 0.8425 0.5079 0.7525 0.0560  0.0530  0.1921  157 PRO A CA  
1220 C C   . PRO A 160 ? 0.8025 0.4759 0.7228 0.0756  0.0421  0.1939  157 PRO A C   
1221 O O   . PRO A 160 ? 0.7644 0.4606 0.6886 0.0780  0.0351  0.1744  157 PRO A O   
1222 C CB  . PRO A 160 ? 0.8035 0.4568 0.7334 0.0450  0.0612  0.1658  157 PRO A CB  
1223 C CG  . PRO A 160 ? 0.8792 0.4899 0.8238 0.0441  0.0722  0.1749  157 PRO A CG  
1224 C CD  . PRO A 160 ? 0.9012 0.4994 0.8324 0.0506  0.0736  0.2091  157 PRO A CD  
1225 N N   . THR A 161 ? 0.7807 0.4380 0.7072 0.0900  0.0409  0.2184  158 THR A N   
1226 C CA  . THR A 161 ? 0.7904 0.4512 0.7362 0.1102  0.0344  0.2192  158 THR A CA  
1227 C C   . THR A 161 ? 0.7819 0.4867 0.7174 0.1157  0.0184  0.2194  158 THR A C   
1228 O O   . THR A 161 ? 0.7602 0.4798 0.7089 0.1226  0.0143  0.2014  158 THR A O   
1229 C CB  . THR A 161 ? 0.8625 0.4966 0.8206 0.1258  0.0379  0.2492  158 THR A CB  
1230 O OG1 . THR A 161 ? 0.8984 0.4866 0.8689 0.1198  0.0545  0.2448  158 THR A OG1 
1231 C CG2 . THR A 161 ? 0.8888 0.5309 0.8703 0.1490  0.0323  0.2529  158 THR A CG2 
1232 N N   . GLU A 162 ? 0.7638 0.4901 0.6745 0.1112  0.0096  0.2390  159 GLU A N   
1233 C CA  . GLU A 162 ? 0.7366 0.5039 0.6363 0.1139  -0.0063 0.2397  159 GLU A CA  
1234 C C   . GLU A 162 ? 0.7705 0.5559 0.6645 0.1026  -0.0065 0.2081  159 GLU A C   
1235 O O   . GLU A 162 ? 0.7457 0.5555 0.6472 0.1084  -0.0154 0.1980  159 GLU A O   
1236 C CB  . GLU A 162 ? 0.8136 0.5976 0.6819 0.1070  -0.0148 0.2650  159 GLU A CB  
1237 C CG  . GLU A 162 ? 0.8405 0.6660 0.6881 0.1012  -0.0302 0.2614  159 GLU A CG  
1238 C CD  . GLU A 162 ? 0.9397 0.7731 0.7612 0.0814  -0.0252 0.2379  159 GLU A CD  
1239 O OE1 . GLU A 162 ? 0.9670 0.8296 0.7715 0.0749  -0.0357 0.2310  159 GLU A OE1 
1240 O OE2 . GLU A 162 ? 1.0223 0.8334 0.8421 0.0721  -0.0104 0.2265  159 GLU A OE2 
1241 N N   . THR A 163 ? 0.7624 0.5368 0.6457 0.0868  0.0038  0.1938  160 THR A N   
1242 C CA  . THR A 163 ? 0.6938 0.4839 0.5749 0.0773  0.0048  0.1665  160 THR A CA  
1243 C C   . THR A 163 ? 0.7158 0.5036 0.6231 0.0856  0.0050  0.1471  160 THR A C   
1244 O O   . THR A 163 ? 0.6464 0.4571 0.5552 0.0870  -0.0016 0.1333  160 THR A O   
1245 C CB  . THR A 163 ? 0.7911 0.5691 0.6642 0.0613  0.0175  0.1578  160 THR A CB  
1246 O OG1 . THR A 163 ? 0.7681 0.5524 0.6118 0.0523  0.0187  0.1723  160 THR A OG1 
1247 C CG2 . THR A 163 ? 0.6980 0.4898 0.5770 0.0543  0.0195  0.1312  160 THR A CG2 
1248 N N   . LEU A 164 ? 0.6615 0.4200 0.5878 0.0898  0.0137  0.1455  161 LEU A N   
1249 C CA  . LEU A 164 ? 0.7275 0.4801 0.6746 0.0959  0.0161  0.1255  161 LEU A CA  
1250 C C   . LEU A 164 ? 0.7072 0.4749 0.6656 0.1136  0.0082  0.1308  161 LEU A C   
1251 O O   . LEU A 164 ? 0.6809 0.4598 0.6489 0.1170  0.0071  0.1126  161 LEU A O   
1252 C CB  . LEU A 164 ? 0.7392 0.4528 0.7004 0.0943  0.0284  0.1227  161 LEU A CB  
1253 C CG  . LEU A 164 ? 0.7257 0.4292 0.6832 0.0747  0.0363  0.1111  161 LEU A CG  
1254 C CD1 . LEU A 164 ? 0.7188 0.3858 0.6918 0.0706  0.0472  0.1022  161 LEU A CD1 
1255 C CD2 . LEU A 164 ? 0.6317 0.3629 0.5862 0.0658  0.0319  0.0894  161 LEU A CD2 
1256 N N   . LYS A 165 ? 0.6642 0.4356 0.6225 0.1247  0.0026  0.1569  162 LYS A N   
1257 C CA  . LYS A 165 ? 0.6597 0.4524 0.6329 0.1416  -0.0057 0.1648  162 LYS A CA  
1258 C C   . LYS A 165 ? 0.6888 0.5214 0.6505 0.1357  -0.0176 0.1561  162 LYS A C   
1259 O O   . LYS A 165 ? 0.6402 0.4902 0.6165 0.1437  -0.0205 0.1463  162 LYS A O   
1260 C CB  . LYS A 165 ? 0.6970 0.4889 0.6748 0.1546  -0.0108 0.1983  162 LYS A CB  
1261 C CG  . LYS A 165 ? 0.7367 0.5519 0.7384 0.1745  -0.0182 0.2089  162 LYS A CG  
1262 C CD  . LYS A 165 ? 0.8834 0.6994 0.8955 0.1898  -0.0236 0.2454  162 LYS A CD  
1263 C CE  . LYS A 165 ? 0.9091 0.7733 0.9292 0.1986  -0.0411 0.2617  162 LYS A CE  
1264 N NZ  . LYS A 165 ? 0.9432 0.8367 0.9315 0.1838  -0.0576 0.2772  162 LYS A NZ  
1265 N N   . GLU A 166 ? 0.6285 0.4744 0.5637 0.1210  -0.0230 0.1590  163 GLU A N   
1266 C CA  . GLU A 166 ? 0.6300 0.5079 0.5529 0.1130  -0.0320 0.1480  163 GLU A CA  
1267 C C   . GLU A 166 ? 0.5971 0.4740 0.5265 0.1078  -0.0259 0.1203  163 GLU A C   
1268 O O   . GLU A 166 ? 0.5993 0.4986 0.5337 0.1093  -0.0314 0.1105  163 GLU A O   
1269 C CB  . GLU A 166 ? 0.6369 0.5228 0.5277 0.0972  -0.0352 0.1531  163 GLU A CB  
1270 C CG  . GLU A 166 ? 0.7113 0.6022 0.5871 0.0981  -0.0428 0.1809  163 GLU A CG  
1271 C CD  . GLU A 166 ? 0.8306 0.7319 0.6698 0.0800  -0.0448 0.1794  163 GLU A CD  
1272 O OE1 . GLU A 166 ? 0.8246 0.7060 0.6500 0.0702  -0.0329 0.1752  163 GLU A OE1 
1273 O OE2 . GLU A 166 ? 0.8897 0.8190 0.7148 0.0747  -0.0570 0.1811  163 GLU A OE2 
1274 N N   . LEU A 167 ? 0.5665 0.4200 0.4954 0.1002  -0.0152 0.1089  164 LEU A N   
1275 C CA  . LEU A 167 ? 0.6149 0.4689 0.5509 0.0952  -0.0106 0.0852  164 LEU A CA  
1276 C C   . LEU A 167 ? 0.6025 0.4581 0.5585 0.1076  -0.0105 0.0772  164 LEU A C   
1277 O O   . LEU A 167 ? 0.5334 0.4065 0.4919 0.1068  -0.0129 0.0634  164 LEU A O   
1278 C CB  . LEU A 167 ? 0.6402 0.4703 0.5774 0.0855  -0.0003 0.0775  164 LEU A CB  
1279 C CG  . LEU A 167 ? 0.6454 0.4791 0.5894 0.0784  0.0027  0.0554  164 LEU A CG  
1280 C CD1 . LEU A 167 ? 0.6129 0.4721 0.5469 0.0724  -0.0018 0.0487  164 LEU A CD1 
1281 C CD2 . LEU A 167 ? 0.6459 0.4598 0.5939 0.0673  0.0113  0.0503  164 LEU A CD2 
1282 N N   . SER A 168 ? 0.5981 0.4345 0.5683 0.1197  -0.0061 0.0866  165 SER A N   
1283 C CA  . SER A 168 ? 0.6122 0.4470 0.6019 0.1331  -0.0024 0.0789  165 SER A CA  
1284 C C   . SER A 168 ? 0.5952 0.4647 0.5905 0.1412  -0.0117 0.0836  165 SER A C   
1285 O O   . SER A 168 ? 0.5668 0.4485 0.5694 0.1435  -0.0102 0.0687  165 SER A O   
1286 C CB  . SER A 168 ? 0.5976 0.4031 0.6026 0.1462  0.0056  0.0916  165 SER A CB  
1287 O OG  . SER A 168 ? 0.6921 0.4906 0.7156 0.1589  0.0133  0.0809  165 SER A OG  
1288 N N   . GLU A 169 ? 0.5520 0.4395 0.5434 0.1440  -0.0217 0.1047  166 GLU A N   
1289 C CA  . GLU A 169 ? 0.5603 0.4839 0.5587 0.1494  -0.0320 0.1110  166 GLU A CA  
1290 C C   . GLU A 169 ? 0.5228 0.4675 0.5071 0.1354  -0.0366 0.0947  166 GLU A C   
1291 O O   . GLU A 169 ? 0.5045 0.4725 0.4996 0.1389  -0.0395 0.0892  166 GLU A O   
1292 C CB  . GLU A 169 ? 0.5815 0.5209 0.5757 0.1521  -0.0436 0.1381  166 GLU A CB  
1293 C CG  . GLU A 169 ? 0.6301 0.5540 0.6457 0.1707  -0.0398 0.1587  166 GLU A CG  
1294 C CD  . GLU A 169 ? 0.7712 0.7092 0.7794 0.1722  -0.0521 0.1890  166 GLU A CD  
1295 O OE1 . GLU A 169 ? 0.8022 0.7289 0.8292 0.1885  -0.0499 0.2105  166 GLU A OE1 
1296 O OE2 . GLU A 169 ? 0.7577 0.7165 0.7402 0.1568  -0.0633 0.1916  166 GLU A OE2 
1297 N N   . ALA A 170 ? 0.4950 0.4313 0.4573 0.1200  -0.0358 0.0875  167 ALA A N   
1298 C CA  . ALA A 170 ? 0.4888 0.4401 0.4401 0.1082  -0.0376 0.0723  167 ALA A CA  
1299 C C   . ALA A 170 ? 0.5124 0.4607 0.4755 0.1105  -0.0308 0.0538  167 ALA A C   
1300 O O   . ALA A 170 ? 0.4650 0.4331 0.4302 0.1086  -0.0335 0.0461  167 ALA A O   
1301 C CB  . ALA A 170 ? 0.4949 0.4354 0.4242 0.0937  -0.0349 0.0689  167 ALA A CB  
1302 N N   . LEU A 171 ? 0.4715 0.3951 0.4406 0.1131  -0.0219 0.0465  168 LEU A N   
1303 C CA  . LEU A 171 ? 0.5065 0.4276 0.4821 0.1132  -0.0161 0.0285  168 LEU A CA  
1304 C C   . LEU A 171 ? 0.4968 0.4311 0.4880 0.1260  -0.0151 0.0278  168 LEU A C   
1305 O O   . LEU A 171 ? 0.4634 0.4118 0.4554 0.1242  -0.0142 0.0164  168 LEU A O   
1306 C CB  . LEU A 171 ? 0.4980 0.3899 0.4751 0.1105  -0.0076 0.0200  168 LEU A CB  
1307 C CG  . LEU A 171 ? 0.5556 0.4397 0.5212 0.0964  -0.0073 0.0184  168 LEU A CG  
1308 C CD1 . LEU A 171 ? 0.5250 0.3802 0.4941 0.0924  0.0003  0.0147  168 LEU A CD1 
1309 C CD2 . LEU A 171 ? 0.5169 0.4177 0.4774 0.0873  -0.0094 0.0063  168 LEU A CD2 
1310 N N   . ASP A 172 ? 0.4939 0.4246 0.4991 0.1395  -0.0141 0.0412  169 ASP A N   
1311 C CA  . ASP A 172 ? 0.4736 0.4196 0.4986 0.1536  -0.0113 0.0422  169 ASP A CA  
1312 C C   . ASP A 172 ? 0.4733 0.4567 0.4994 0.1504  -0.0207 0.0459  169 ASP A C   
1313 O O   . ASP A 172 ? 0.4677 0.4669 0.5035 0.1542  -0.0170 0.0378  169 ASP A O   
1314 C CB  . ASP A 172 ? 0.5280 0.4651 0.5720 0.1705  -0.0087 0.0600  169 ASP A CB  
1315 C CG  . ASP A 172 ? 0.6060 0.5024 0.6544 0.1761  0.0052  0.0526  169 ASP A CG  
1316 O OD1 . ASP A 172 ? 0.6405 0.5214 0.6808 0.1689  0.0135  0.0308  169 ASP A OD1 
1317 O OD2 . ASP A 172 ? 0.6697 0.5494 0.7293 0.1870  0.0079  0.0690  169 ASP A OD2 
1318 N N   . THR A 173 ? 0.4597 0.4569 0.4747 0.1419  -0.0321 0.0577  170 THR A N   
1319 C CA  . THR A 173 ? 0.4686 0.4988 0.4829 0.1354  -0.0411 0.0597  170 THR A CA  
1320 C C   . THR A 173 ? 0.4533 0.4858 0.4579 0.1249  -0.0374 0.0416  170 THR A C   
1321 O O   . THR A 173 ? 0.4540 0.5084 0.4677 0.1253  -0.0376 0.0381  170 THR A O   
1322 C CB  . THR A 173 ? 0.5071 0.5465 0.5047 0.1247  -0.0529 0.0722  170 THR A CB  
1323 O OG1 . THR A 173 ? 0.4902 0.5340 0.4985 0.1354  -0.0582 0.0928  170 THR A OG1 
1324 C CG2 . THR A 173 ? 0.4672 0.5373 0.4615 0.1141  -0.0616 0.0711  170 THR A CG2 
1325 N N   . ILE A 174 ? 0.4281 0.4394 0.4164 0.1158  -0.0336 0.0316  171 ILE A N   
1326 C CA  . ILE A 174 ? 0.4207 0.4354 0.4012 0.1067  -0.0311 0.0180  171 ILE A CA  
1327 C C   . ILE A 174 ? 0.4415 0.4572 0.4321 0.1137  -0.0234 0.0075  171 ILE A C   
1328 O O   . ILE A 174 ? 0.4191 0.4502 0.4097 0.1102  -0.0226 0.0016  171 ILE A O   
1329 C CB  . ILE A 174 ? 0.4156 0.4111 0.3808 0.0967  -0.0290 0.0123  171 ILE A CB  
1330 C CG1 . ILE A 174 ? 0.4549 0.4522 0.4065 0.0880  -0.0343 0.0203  171 ILE A CG1 
1331 C CG2 . ILE A 174 ? 0.4051 0.4040 0.3668 0.0903  -0.0259 0.0004  171 ILE A CG2 
1332 C CD1 . ILE A 174 ? 0.4539 0.4324 0.3935 0.0801  -0.0299 0.0173  171 ILE A CD1 
1333 N N   . LYS A 175 ? 0.4127 0.4105 0.4107 0.1231  -0.0164 0.0047  172 LYS A N   
1334 C CA  . LYS A 175 ? 0.4192 0.4161 0.4232 0.1291  -0.0071 -0.0073 172 LYS A CA  
1335 C C   . LYS A 175 ? 0.4412 0.4659 0.4601 0.1367  -0.0063 -0.0030 172 LYS A C   
1336 O O   . LYS A 175 ? 0.4060 0.4406 0.4238 0.1356  -0.0007 -0.0126 172 LYS A O   
1337 C CB  . LYS A 175 ? 0.4459 0.4157 0.4560 0.1382  0.0022  -0.0113 172 LYS A CB  
1338 C CG  . LYS A 175 ? 0.4643 0.4301 0.4776 0.1440  0.0144  -0.0262 172 LYS A CG  
1339 C CD  . LYS A 175 ? 0.5036 0.4352 0.5192 0.1500  0.0255  -0.0341 172 LYS A CD  
1340 C CE  . LYS A 175 ? 0.6090 0.5365 0.6255 0.1559  0.0399  -0.0505 172 LYS A CE  
1341 N NZ  . LYS A 175 ? 0.7469 0.6366 0.7638 0.1603  0.0533  -0.0617 172 LYS A NZ  
1342 N N   . GLU A 176 ? 0.4134 0.4537 0.4466 0.1434  -0.0123 0.0127  173 GLU A N   
1343 C CA  . GLU A 176 ? 0.4497 0.5213 0.5014 0.1495  -0.0122 0.0183  173 GLU A CA  
1344 C C   . GLU A 176 ? 0.4701 0.5651 0.5140 0.1354  -0.0201 0.0184  173 GLU A C   
1345 O O   . GLU A 176 ? 0.4468 0.5689 0.5053 0.1372  -0.0191 0.0211  173 GLU A O   
1346 C CB  . GLU A 176 ? 0.5067 0.5915 0.5806 0.1621  -0.0169 0.0370  173 GLU A CB  
1347 C CG  . GLU A 176 ? 0.5383 0.5981 0.6247 0.1787  -0.0059 0.0376  173 GLU A CG  
1348 C CD  . GLU A 176 ? 0.6598 0.7190 0.7595 0.1897  0.0108  0.0251  173 GLU A CD  
1349 O OE1 . GLU A 176 ? 0.7079 0.7346 0.8004 0.1933  0.0231  0.0116  173 GLU A OE1 
1350 O OE2 . GLU A 176 ? 0.6508 0.7415 0.7667 0.1933  0.0124  0.0276  173 GLU A OE2 
1351 N N   . GLN A 177 ? 0.3910 0.4751 0.4139 0.1215  -0.0259 0.0153  174 GLN A N   
1352 C CA  . GLN A 177 ? 0.4168 0.5157 0.4313 0.1080  -0.0305 0.0136  174 GLN A CA  
1353 C C   . GLN A 177 ? 0.3916 0.4832 0.3955 0.1024  -0.0237 0.0015  174 GLN A C   
1354 O O   . GLN A 177 ? 0.3643 0.4653 0.3627 0.0922  -0.0255 0.0009  174 GLN A O   
1355 C CB  . GLN A 177 ? 0.3973 0.4885 0.3952 0.0960  -0.0389 0.0177  174 GLN A CB  
1356 C CG  . GLN A 177 ? 0.4430 0.5482 0.4455 0.0960  -0.0488 0.0312  174 GLN A CG  
1357 C CD  . GLN A 177 ? 0.4648 0.5585 0.4447 0.0829  -0.0545 0.0323  174 GLN A CD  
1358 O OE1 . GLN A 177 ? 0.4457 0.5153 0.4134 0.0828  -0.0511 0.0298  174 GLN A OE1 
1359 N NE2 . GLN A 177 ? 0.5024 0.6131 0.4761 0.0703  -0.0621 0.0350  174 GLN A NE2 
1360 N N   . VAL A 178 ? 0.3685 0.4427 0.3682 0.1076  -0.0165 -0.0074 175 VAL A N   
1361 C CA  . VAL A 178 ? 0.4186 0.4879 0.4058 0.1011  -0.0125 -0.0171 175 VAL A CA  
1362 C C   . VAL A 178 ? 0.3734 0.4644 0.3646 0.0995  -0.0087 -0.0176 175 VAL A C   
1363 O O   . VAL A 178 ? 0.3483 0.4416 0.3297 0.0909  -0.0089 -0.0190 175 VAL A O   
1364 C CB  . VAL A 178 ? 0.4068 0.4573 0.3886 0.1054  -0.0060 -0.0276 175 VAL A CB  
1365 C CG1 . VAL A 178 ? 0.4466 0.5000 0.4161 0.0991  -0.0028 -0.0362 175 VAL A CG1 
1366 C CG2 . VAL A 178 ? 0.4642 0.4930 0.4400 0.1024  -0.0098 -0.0271 175 VAL A CG2 
1367 N N   . ASP A 179 ? 0.3594 0.4671 0.3669 0.1081  -0.0042 -0.0150 176 ASP A N   
1368 C CA  . ASP A 179 ? 0.4154 0.5450 0.4281 0.1064  0.0016  -0.0154 176 ASP A CA  
1369 C C   . ASP A 179 ? 0.3838 0.5294 0.3984 0.0948  -0.0050 -0.0075 176 ASP A C   
1370 O O   . ASP A 179 ? 0.3549 0.5163 0.3717 0.0904  -0.0002 -0.0069 176 ASP A O   
1371 C CB  . ASP A 179 ? 0.4146 0.5595 0.4484 0.1198  0.0103  -0.0144 176 ASP A CB  
1372 C CG  . ASP A 179 ? 0.4801 0.6372 0.5351 0.1263  0.0031  -0.0020 176 ASP A CG  
1373 O OD1 . ASP A 179 ? 0.5467 0.7015 0.5963 0.1181  -0.0088 0.0047  176 ASP A OD1 
1374 O OD2 . ASP A 179 ? 0.6106 0.7804 0.6880 0.1399  0.0098  0.0016  176 ASP A OD2 
1375 N N   . GLU A 180 ? 0.3245 0.4642 0.3362 0.0886  -0.0147 -0.0022 177 GLU A N   
1376 C CA  . GLU A 180 ? 0.3184 0.4663 0.3276 0.0750  -0.0201 0.0024  177 GLU A CA  
1377 C C   . GLU A 180 ? 0.3485 0.4774 0.3400 0.0659  -0.0191 -0.0012 177 GLU A C   
1378 O O   . GLU A 180 ? 0.3325 0.4634 0.3214 0.0547  -0.0201 0.0011  177 GLU A O   
1379 C CB  . GLU A 180 ? 0.3419 0.4932 0.3535 0.0711  -0.0303 0.0089  177 GLU A CB  
1380 C CG  . GLU A 180 ? 0.3818 0.5513 0.4135 0.0829  -0.0332 0.0163  177 GLU A CG  
1381 C CD  . GLU A 180 ? 0.4602 0.6334 0.4901 0.0786  -0.0453 0.0250  177 GLU A CD  
1382 O OE1 . GLU A 180 ? 0.4865 0.6724 0.5324 0.0895  -0.0490 0.0344  177 GLU A OE1 
1383 O OE2 . GLU A 180 ? 0.4590 0.6222 0.4708 0.0644  -0.0503 0.0231  177 GLU A OE2 
1384 N N   . VAL A 181 ? 0.3021 0.4035 0.3257 -0.0121 -0.0335 0.0143  178 VAL A N   
1385 C CA  . VAL A 181 ? 0.3163 0.3989 0.3369 -0.0231 -0.0341 0.0075  178 VAL A CA  
1386 C C   . VAL A 181 ? 0.3159 0.4046 0.3600 -0.0330 -0.0315 0.0125  178 VAL A C   
1387 O O   . VAL A 181 ? 0.3013 0.3960 0.3487 -0.0291 -0.0223 0.0218  178 VAL A O   
1388 C CB  . VAL A 181 ? 0.3209 0.3781 0.3145 -0.0190 -0.0247 0.0068  178 VAL A CB  
1389 C CG1 . VAL A 181 ? 0.3336 0.3773 0.3270 -0.0290 -0.0235 0.0027  178 VAL A CG1 
1390 C CG2 . VAL A 181 ? 0.3123 0.3619 0.2849 -0.0100 -0.0263 0.0040  178 VAL A CG2 
1391 N N   . LEU A 182 ? 0.2624 0.3495 0.3226 -0.0444 -0.0386 0.0068  179 LEU A N   
1392 C CA  . LEU A 182 ? 0.2580 0.3493 0.3435 -0.0538 -0.0351 0.0138  179 LEU A CA  
1393 C C   . LEU A 182 ? 0.3101 0.3808 0.3893 -0.0586 -0.0312 0.0123  179 LEU A C   
1394 O O   . LEU A 182 ? 0.3031 0.3759 0.3987 -0.0629 -0.0249 0.0217  179 LEU A O   
1395 C CB  . LEU A 182 ? 0.2601 0.3667 0.3787 -0.0646 -0.0456 0.0105  179 LEU A CB  
1396 C CG  . LEU A 182 ? 0.3077 0.4438 0.4421 -0.0617 -0.0514 0.0129  179 LEU A CG  
1397 C CD1 . LEU A 182 ? 0.3055 0.4552 0.4724 -0.0756 -0.0653 0.0038  179 LEU A CD1 
1398 C CD2 . LEU A 182 ? 0.2906 0.4442 0.4371 -0.0566 -0.0394 0.0300  179 LEU A CD2 
1399 N N   . ASP A 183 ? 0.2752 0.3283 0.3321 -0.0568 -0.0339 0.0024  180 ASP A N   
1400 C CA  . ASP A 183 ? 0.2825 0.3203 0.3391 -0.0611 -0.0316 0.0011  180 ASP A CA  
1401 C C   . ASP A 183 ? 0.2944 0.3281 0.3354 -0.0565 -0.0214 0.0078  180 ASP A C   
1402 O O   . ASP A 183 ? 0.3105 0.3469 0.3360 -0.0506 -0.0171 0.0091  180 ASP A O   
1403 C CB  . ASP A 183 ? 0.3105 0.3347 0.3538 -0.0609 -0.0393 -0.0125 180 ASP A CB  
1404 C CG  . ASP A 183 ? 0.3974 0.4275 0.4546 -0.0653 -0.0516 -0.0227 180 ASP A CG  
1405 O OD1 . ASP A 183 ? 0.3962 0.4228 0.4773 -0.0744 -0.0550 -0.0247 180 ASP A OD1 
1406 O OD2 . ASP A 183 ? 0.3892 0.4267 0.4334 -0.0595 -0.0582 -0.0295 180 ASP A OD2 
1407 N N   . PRO A 184 ? 0.2909 0.3182 0.3362 -0.0585 -0.0175 0.0116  181 PRO A N   
1408 C CA  . PRO A 184 ? 0.2870 0.3165 0.3185 -0.0537 -0.0095 0.0170  181 PRO A CA  
1409 C C   . PRO A 184 ? 0.2823 0.3052 0.2898 -0.0510 -0.0103 0.0082  181 PRO A C   
1410 O O   . PRO A 184 ? 0.2808 0.2945 0.2815 -0.0516 -0.0151 0.0001  181 PRO A O   
1411 C CB  . PRO A 184 ? 0.3331 0.3566 0.3729 -0.0548 -0.0071 0.0216  181 PRO A CB  
1412 C CG  . PRO A 184 ? 0.2945 0.3132 0.3603 -0.0615 -0.0105 0.0231  181 PRO A CG  
1413 C CD  . PRO A 184 ? 0.3119 0.3302 0.3758 -0.0644 -0.0201 0.0111  181 PRO A CD  
1414 N N   . ILE A 185 ? 0.2938 0.3215 0.2888 -0.0477 -0.0051 0.0095  182 ILE A N   
1415 C CA  . ILE A 185 ? 0.2931 0.3125 0.2699 -0.0472 -0.0047 0.0017  182 ILE A CA  
1416 C C   . ILE A 185 ? 0.3048 0.3283 0.2716 -0.0474 -0.0007 -0.0001 182 ILE A C   
1417 O O   . ILE A 185 ? 0.2928 0.3272 0.2600 -0.0445 0.0023  0.0038  182 ILE A O   
1418 C CB  . ILE A 185 ? 0.3468 0.3632 0.3182 -0.0436 -0.0041 0.0005  182 ILE A CB  
1419 C CG1 . ILE A 185 ? 0.3583 0.3617 0.3129 -0.0432 -0.0017 -0.0053 182 ILE A CG1 
1420 C CG2 . ILE A 185 ? 0.3395 0.3651 0.3123 -0.0392 0.0007  0.0055  182 ILE A CG2 
1421 C CD1 . ILE A 185 ? 0.3775 0.3745 0.3257 -0.0370 -0.0002 -0.0045 182 ILE A CD1 
1422 N N   . LEU A 186 ? 0.2883 0.3055 0.2465 -0.0505 -0.0009 -0.0061 183 LEU A N   
1423 C CA  . LEU A 186 ? 0.3251 0.3467 0.2754 -0.0534 0.0013  -0.0112 183 LEU A CA  
1424 C C   . LEU A 186 ? 0.3198 0.3263 0.2613 -0.0562 0.0038  -0.0171 183 LEU A C   
1425 O O   . LEU A 186 ? 0.3337 0.3313 0.2739 -0.0569 0.0040  -0.0166 183 LEU A O   
1426 C CB  . LEU A 186 ? 0.3294 0.3599 0.2828 -0.0557 0.0001  -0.0111 183 LEU A CB  
1427 C CG  . LEU A 186 ? 0.3322 0.3703 0.2814 -0.0615 0.0008  -0.0180 183 LEU A CG  
1428 C CD1 . LEU A 186 ? 0.3556 0.4067 0.3004 -0.0603 0.0001  -0.0216 183 LEU A CD1 
1429 C CD2 . LEU A 186 ? 0.3774 0.4285 0.3323 -0.0618 -0.0001 -0.0155 183 LEU A CD2 
1430 N N   . VAL A 187 ? 0.3241 0.3265 0.2587 -0.0562 0.0065  -0.0220 184 VAL A N   
1431 C CA  . VAL A 187 ? 0.3584 0.3420 0.2855 -0.0588 0.0108  -0.0274 184 VAL A CA  
1432 C C   . VAL A 187 ? 0.3359 0.3215 0.2629 -0.0685 0.0110  -0.0365 184 VAL A C   
1433 O O   . VAL A 187 ? 0.3548 0.3519 0.2793 -0.0695 0.0087  -0.0433 184 VAL A O   
1434 C CB  . VAL A 187 ? 0.3777 0.3524 0.2975 -0.0517 0.0142  -0.0287 184 VAL A CB  
1435 C CG1 . VAL A 187 ? 0.4228 0.3726 0.3352 -0.0531 0.0204  -0.0331 184 VAL A CG1 
1436 C CG2 . VAL A 187 ? 0.3755 0.3563 0.3004 -0.0432 0.0129  -0.0191 184 VAL A CG2 
1437 N N   . ILE A 188 ? 0.3836 0.3605 0.3138 -0.0753 0.0139  -0.0367 185 ILE A N   
1438 C CA  . ILE A 188 ? 0.3721 0.3535 0.3080 -0.0873 0.0141  -0.0450 185 ILE A CA  
1439 C C   . ILE A 188 ? 0.3658 0.3200 0.3001 -0.0933 0.0213  -0.0494 185 ILE A C   
1440 O O   . ILE A 188 ? 0.3983 0.3349 0.3298 -0.0885 0.0277  -0.0406 185 ILE A O   
1441 C CB  . ILE A 188 ? 0.3449 0.3416 0.2905 -0.0907 0.0135  -0.0390 185 ILE A CB  
1442 C CG1 . ILE A 188 ? 0.3720 0.3949 0.3207 -0.0863 0.0071  -0.0370 185 ILE A CG1 
1443 C CG2 . ILE A 188 ? 0.3956 0.3938 0.3517 -0.1044 0.0165  -0.0441 185 ILE A CG2 
1444 C CD1 . ILE A 188 ? 0.3688 0.4011 0.3231 -0.0831 0.0075  -0.0288 185 ILE A CD1 
1445 N N   . GLN A 189 ? 0.4051 0.3558 0.3411 -0.1030 0.0205  -0.0631 186 GLN A N   
1446 C CA  . GLN A 189 ? 0.4654 0.3844 0.4015 -0.1094 0.0285  -0.0681 186 GLN A CA  
1447 C C   . GLN A 189 ? 0.4692 0.3901 0.4171 -0.1274 0.0265  -0.0836 186 GLN A C   
1448 O O   . GLN A 189 ? 0.4687 0.4090 0.4149 -0.1307 0.0176  -0.0974 186 GLN A O   
1449 C CB  . GLN A 189 ? 0.4398 0.3373 0.3608 -0.0984 0.0315  -0.0720 186 GLN A CB  
1450 C CG  . GLN A 189 ? 0.4970 0.3559 0.4171 -0.1028 0.0415  -0.0768 186 GLN A CG  
1451 C CD  . GLN A 189 ? 0.4956 0.3372 0.4206 -0.1010 0.0518  -0.0598 186 GLN A CD  
1452 O OE1 . GLN A 189 ? 0.4898 0.3366 0.4082 -0.0872 0.0529  -0.0455 186 GLN A OE1 
1453 N NE2 . GLN A 189 ? 0.4869 0.3087 0.4240 -0.1147 0.0596  -0.0613 186 GLN A NE2 
1454 N N   . ALA A 190 ? 0.4767 0.3783 0.4371 -0.1388 0.0350  -0.0811 187 ALA A N   
1455 C CA  . ALA A 190 ? 0.5041 0.4020 0.4798 -0.1589 0.0339  -0.0972 187 ALA A CA  
1456 C C   . ALA A 190 ? 0.5460 0.4090 0.5115 -0.1596 0.0363  -0.1133 187 ALA A C   
1457 O O   . ALA A 190 ? 0.5589 0.3868 0.5156 -0.1506 0.0472  -0.1052 187 ALA A O   
1458 C CB  . ALA A 190 ? 0.5038 0.3931 0.5004 -0.1715 0.0442  -0.0861 187 ALA A CB  
1459 N N   . GLU A 191 ? 0.5257 0.3994 0.4910 -0.1687 0.0263  -0.1367 188 GLU A N   
1460 C CA  . GLU A 191 ? 0.5404 0.3804 0.4930 -0.1681 0.0278  -0.1558 188 GLU A CA  
1461 C C   . GLU A 191 ? 0.6468 0.4406 0.6129 -0.1812 0.0406  -0.1573 188 GLU A C   
1462 O O   . GLU A 191 ? 0.7034 0.4559 0.6561 -0.1718 0.0498  -0.1592 188 GLU A O   
1463 C CB  . GLU A 191 ? 0.6083 0.4719 0.5581 -0.1762 0.0133  -0.1832 188 GLU A CB  
1464 C CG  . GLU A 191 ? 0.6631 0.5556 0.5893 -0.1565 0.0046  -0.1850 188 GLU A CG  
1465 C CD  . GLU A 191 ? 0.6481 0.5744 0.5718 -0.1634 -0.0107 -0.2094 188 GLU A CD  
1466 O OE1 . GLU A 191 ? 0.7726 0.7421 0.6903 -0.1535 -0.0190 -0.2033 188 GLU A OE1 
1467 O OE2 . GLU A 191 ? 0.7333 0.6435 0.6625 -0.1790 -0.0144 -0.2344 188 GLU A OE2 
1468 N N   . ASN A 192 ? 0.6123 0.4122 0.6060 -0.2019 0.0428  -0.1550 189 ASN A N   
1469 C CA  . ASN A 192 ? 0.6446 0.4017 0.6572 -0.2178 0.0563  -0.1551 189 ASN A CA  
1470 C C   . ASN A 192 ? 0.6773 0.4240 0.6980 -0.2118 0.0722  -0.1234 189 ASN A C   
1471 O O   . ASN A 192 ? 0.7528 0.4950 0.7999 -0.2284 0.0810  -0.1148 189 ASN A O   
1472 C CB  . ASN A 192 ? 0.6761 0.4530 0.7172 -0.2407 0.0465  -0.1706 189 ASN A CB  
1473 C CG  . ASN A 192 ? 0.7180 0.5138 0.7478 -0.2402 0.0280  -0.1989 189 ASN A CG  
1474 O OD1 . ASN A 192 ? 0.7888 0.5519 0.8044 -0.2347 0.0277  -0.2147 189 ASN A OD1 
1475 N ND2 . ASN A 192 ? 0.6881 0.5373 0.7216 -0.2429 0.0133  -0.2044 189 ASN A ND2 
1476 N N   . ASP A 193 ? 0.6627 0.4084 0.6603 -0.1869 0.0757  -0.1059 190 ASP A N   
1477 C CA  . ASP A 193 ? 0.6829 0.4200 0.6807 -0.1757 0.0896  -0.0770 190 ASP A CA  
1478 C C   . ASP A 193 ? 0.7146 0.3984 0.7166 -0.1768 0.1079  -0.0700 190 ASP A C   
1479 O O   . ASP A 193 ? 0.7578 0.4083 0.7433 -0.1662 0.1115  -0.0775 190 ASP A O   
1480 C CB  . ASP A 193 ? 0.5842 0.3358 0.5566 -0.1497 0.0857  -0.0650 190 ASP A CB  
1481 C CG  . ASP A 193 ? 0.6471 0.4072 0.6184 -0.1380 0.0939  -0.0386 190 ASP A CG  
1482 O OD1 . ASP A 193 ? 0.6346 0.3676 0.6120 -0.1376 0.1097  -0.0236 190 ASP A OD1 
1483 O OD2 . ASP A 193 ? 0.5634 0.3569 0.5272 -0.1284 0.0850  -0.0329 190 ASP A OD2 
1484 N N   . ASN A 194 ? 0.6938 0.3695 0.7180 -0.1880 0.1212  -0.0537 191 ASN A N   
1485 C CA  . ASN A 194 ? 0.7312 0.3553 0.7621 -0.1885 0.1416  -0.0421 191 ASN A CA  
1486 C C   . ASN A 194 ? 0.7136 0.3318 0.7306 -0.1643 0.1561  -0.0095 191 ASN A C   
1487 O O   . ASN A 194 ? 0.7512 0.3320 0.7753 -0.1624 0.1758  0.0075  191 ASN A O   
1488 C CB  . ASN A 194 ? 0.7755 0.4011 0.8422 -0.2119 0.1445  -0.0428 191 ASN A CB  
1489 C CG  . ASN A 194 ? 0.8403 0.4716 0.9193 -0.2306 0.1273  -0.0751 191 ASN A CG  
1490 O OD1 . ASN A 194 ? 0.8993 0.5004 0.9649 -0.2261 0.1242  -0.0931 191 ASN A OD1 
1491 N ND2 . ASN A 194 ? 0.9050 0.5765 1.0087 -0.2498 0.1162  -0.0822 191 ASN A ND2 
1492 N N   . MET A 195 ? 0.6819 0.3360 0.6792 -0.1450 0.1469  -0.0005 192 MET A N   
1493 C CA  . MET A 195 ? 0.6992 0.3538 0.6812 -0.1210 0.1576  0.0275  192 MET A CA  
1494 C C   . MET A 195 ? 0.7081 0.3584 0.6615 -0.0955 0.1528  0.0280  192 MET A C   
1495 O O   . MET A 195 ? 0.7210 0.3504 0.6623 -0.0760 0.1658  0.0470  192 MET A O   
1496 C CB  . MET A 195 ? 0.6466 0.3473 0.6307 -0.1186 0.1520  0.0391  192 MET A CB  
1497 C CG  . MET A 195 ? 0.7061 0.4144 0.6721 -0.0932 0.1603  0.0651  192 MET A CG  
1498 S SD  . MET A 195 ? 0.8116 0.4861 0.7883 -0.0901 0.1889  0.0947  192 MET A SD  
1499 C CE  . MET A 195 ? 0.7628 0.4368 0.7803 -0.1259 0.1946  0.0877  192 MET A CE  
1500 N N   . ILE A 196 ? 0.6290 0.2999 0.5730 -0.0949 0.1353  0.0084  193 ILE A N   
1501 C CA  . ILE A 196 ? 0.6234 0.2959 0.5450 -0.0732 0.1298  0.0075  193 ILE A CA  
1502 C C   . ILE A 196 ? 0.6991 0.3569 0.6174 -0.0796 0.1232  -0.0174 193 ILE A C   
1503 O O   . ILE A 196 ? 0.6654 0.3164 0.5974 -0.1008 0.1200  -0.0357 193 ILE A O   
1504 C CB  . ILE A 196 ? 0.6341 0.3524 0.5464 -0.0626 0.1153  0.0113  193 ILE A CB  
1505 C CG1 . ILE A 196 ? 0.6121 0.3597 0.5328 -0.0785 0.0996  -0.0074 193 ILE A CG1 
1506 C CG2 . ILE A 196 ? 0.6299 0.3644 0.5427 -0.0557 0.1204  0.0320  193 ILE A CG2 
1507 C CD1 . ILE A 196 ? 0.5271 0.3078 0.4371 -0.0672 0.0853  -0.0099 193 ILE A CD1 
1508 N N   . ASP A 197 ? 0.6310 0.2867 0.5311 -0.0600 0.1211  -0.0181 194 ASP A N   
1509 C CA  . ASP A 197 ? 0.6958 0.3437 0.5882 -0.0611 0.1146  -0.0406 194 ASP A CA  
1510 C C   . ASP A 197 ? 0.6262 0.3197 0.5187 -0.0665 0.0966  -0.0516 194 ASP A C   
1511 O O   . ASP A 197 ? 0.6114 0.3354 0.4983 -0.0541 0.0902  -0.0405 194 ASP A O   
1512 C CB  . ASP A 197 ? 0.6964 0.3274 0.5704 -0.0359 0.1212  -0.0346 194 ASP A CB  
1513 C CG  . ASP A 197 ? 0.7869 0.4112 0.6498 -0.0331 0.1161  -0.0569 194 ASP A CG  
1514 O OD1 . ASP A 197 ? 0.7179 0.3486 0.5855 -0.0507 0.1069  -0.0788 194 ASP A OD1 
1515 O OD2 . ASP A 197 ? 0.8935 0.5065 0.7417 -0.0114 0.1220  -0.0524 194 ASP A OD2 
1516 N N   . PRO A 198 ? 0.6262 0.3268 0.5263 -0.0848 0.0882  -0.0726 195 PRO A N   
1517 C CA  . PRO A 198 ? 0.5853 0.3301 0.4848 -0.0874 0.0726  -0.0801 195 PRO A CA  
1518 C C   . PRO A 198 ? 0.6085 0.3676 0.4913 -0.0685 0.0679  -0.0807 195 PRO A C   
1519 O O   . PRO A 198 ? 0.5560 0.3517 0.4391 -0.0660 0.0580  -0.0779 195 PRO A O   
1520 C CB  . PRO A 198 ? 0.6758 0.4216 0.5840 -0.1078 0.0657  -0.1041 195 PRO A CB  
1521 C CG  . PRO A 198 ? 0.7138 0.4162 0.6320 -0.1200 0.0771  -0.1096 195 PRO A CG  
1522 C CD  . PRO A 198 ? 0.6787 0.3497 0.5915 -0.1050 0.0928  -0.0884 195 PRO A CD  
1523 N N   . GLN A 199 ? 0.5853 0.3164 0.4547 -0.0546 0.0760  -0.0830 196 GLN A N   
1524 C CA  . GLN A 199 ? 0.6211 0.3695 0.4771 -0.0351 0.0734  -0.0801 196 GLN A CA  
1525 C C   . GLN A 199 ? 0.5643 0.3399 0.4241 -0.0240 0.0712  -0.0583 196 GLN A C   
1526 O O   . GLN A 199 ? 0.6112 0.4115 0.4668 -0.0121 0.0669  -0.0543 196 GLN A O   
1527 C CB  . GLN A 199 ? 0.6491 0.3614 0.4905 -0.0195 0.0847  -0.0841 196 GLN A CB  
1528 C CG  . GLN A 199 ? 0.7823 0.4769 0.6140 -0.0250 0.0831  -0.1107 196 GLN A CG  
1529 C CD  . GLN A 199 ? 0.8171 0.5528 0.6434 -0.0247 0.0704  -0.1207 196 GLN A CD  
1530 O OE1 . GLN A 199 ? 0.7860 0.5467 0.6052 -0.0077 0.0696  -0.1108 196 GLN A OE1 
1531 N NE2 . GLN A 199 ? 0.8636 0.6099 0.6953 -0.0433 0.0609  -0.1385 196 GLN A NE2 
1532 N N   . SER A 200 ? 0.5585 0.3309 0.4264 -0.0276 0.0743  -0.0445 197 SER A N   
1533 C CA  . SER A 200 ? 0.5097 0.3103 0.3812 -0.0192 0.0695  -0.0280 197 SER A CA  
1534 C C   . SER A 200 ? 0.4919 0.3299 0.3695 -0.0245 0.0568  -0.0316 197 SER A C   
1535 O O   . SER A 200 ? 0.4847 0.3462 0.3644 -0.0152 0.0518  -0.0225 197 SER A O   
1536 C CB  . SER A 200 ? 0.4964 0.2920 0.3741 -0.0245 0.0733  -0.0165 197 SER A CB  
1537 O OG  . SER A 200 ? 0.5710 0.3324 0.4440 -0.0175 0.0872  -0.0083 197 SER A OG  
1538 N N   . ALA A 201 ? 0.4898 0.3346 0.3720 -0.0394 0.0515  -0.0441 198 ALA A N   
1539 C CA  . ALA A 201 ? 0.4568 0.3357 0.3447 -0.0427 0.0410  -0.0449 198 ALA A CA  
1540 C C   . ALA A 201 ? 0.4773 0.3706 0.3592 -0.0312 0.0392  -0.0460 198 ALA A C   
1541 O O   . ALA A 201 ? 0.4348 0.3540 0.3232 -0.0273 0.0340  -0.0378 198 ALA A O   
1542 C CB  . ALA A 201 ? 0.4286 0.3153 0.3223 -0.0587 0.0361  -0.0570 198 ALA A CB  
1543 N N   . ASN A 202 ? 0.4837 0.3598 0.3538 -0.0255 0.0443  -0.0562 199 ASN A N   
1544 C CA  . ASN A 202 ? 0.5177 0.4087 0.3806 -0.0116 0.0448  -0.0556 199 ASN A CA  
1545 C C   . ASN A 202 ? 0.5014 0.4005 0.3687 0.0024  0.0479  -0.0388 199 ASN A C   
1546 O O   . ASN A 202 ? 0.4667 0.3929 0.3395 0.0096  0.0456  -0.0309 199 ASN A O   
1547 C CB  . ASN A 202 ? 0.5407 0.4085 0.3871 -0.0059 0.0505  -0.0715 199 ASN A CB  
1548 C CG  . ASN A 202 ? 0.6155 0.4905 0.4570 -0.0165 0.0440  -0.0900 199 ASN A CG  
1549 O OD1 . ASN A 202 ? 0.6025 0.5099 0.4476 -0.0184 0.0368  -0.0880 199 ASN A OD1 
1550 N ND2 . ASN A 202 ? 0.6550 0.4999 0.4890 -0.0235 0.0464  -0.1084 199 ASN A ND2 
1551 N N   . TYR A 203 ? 0.4662 0.3445 0.3328 0.0065  0.0534  -0.0321 200 TYR A N   
1552 C CA  . TYR A 203 ? 0.5152 0.4056 0.3865 0.0202  0.0548  -0.0166 200 TYR A CA  
1553 C C   . TYR A 203 ? 0.4950 0.4171 0.3820 0.0144  0.0448  -0.0081 200 TYR A C   
1554 O O   . TYR A 203 ? 0.4561 0.4035 0.3525 0.0215  0.0421  0.0000  200 TYR A O   
1555 C CB  . TYR A 203 ? 0.5355 0.3994 0.4014 0.0265  0.0624  -0.0100 200 TYR A CB  
1556 C CG  . TYR A 203 ? 0.5476 0.4265 0.4157 0.0445  0.0640  0.0049  200 TYR A CG  
1557 C CD1 . TYR A 203 ? 0.5474 0.4522 0.4265 0.0441  0.0558  0.0149  200 TYR A CD1 
1558 C CD2 . TYR A 203 ? 0.6085 0.4786 0.4681 0.0625  0.0730  0.0077  200 TYR A CD2 
1559 C CE1 . TYR A 203 ? 0.5678 0.4923 0.4510 0.0599  0.0551  0.0269  200 TYR A CE1 
1560 C CE2 . TYR A 203 ? 0.5903 0.4800 0.4540 0.0799  0.0741  0.0221  200 TYR A CE2 
1561 C CZ  . TYR A 203 ? 0.6205 0.5393 0.4970 0.0779  0.0644  0.0314  200 TYR A CZ  
1562 O OH  . TYR A 203 ? 0.6796 0.6228 0.5619 0.0948  0.0638  0.0443  200 TYR A OH  
1563 N N   . ILE A 204 ? 0.4329 0.3534 0.3245 0.0014  0.0399  -0.0098 201 ILE A N   
1564 C CA  . ILE A 204 ? 0.4127 0.3580 0.3177 -0.0042 0.0306  -0.0046 201 ILE A CA  
1565 C C   . ILE A 204 ? 0.3692 0.3371 0.2830 -0.0066 0.0266  -0.0051 201 ILE A C   
1566 O O   . ILE A 204 ? 0.3864 0.3760 0.3136 -0.0038 0.0226  0.0027  201 ILE A O   
1567 C CB  . ILE A 204 ? 0.3865 0.3252 0.2924 -0.0161 0.0276  -0.0077 201 ILE A CB  
1568 C CG1 . ILE A 204 ? 0.4581 0.3775 0.3563 -0.0117 0.0333  -0.0030 201 ILE A CG1 
1569 C CG2 . ILE A 204 ? 0.3957 0.3566 0.3139 -0.0210 0.0183  -0.0049 201 ILE A CG2 
1570 C CD1 . ILE A 204 ? 0.4425 0.3542 0.3409 -0.0222 0.0339  -0.0048 201 ILE A CD1 
1571 N N   . TYR A 205 ? 0.3836 0.3482 0.2910 -0.0118 0.0279  -0.0139 202 TYR A N   
1572 C CA  . TYR A 205 ? 0.3786 0.3659 0.2921 -0.0123 0.0254  -0.0124 202 TYR A CA  
1573 C C   . TYR A 205 ? 0.4256 0.4283 0.3430 0.0002  0.0294  -0.0038 202 TYR A C   
1574 O O   . TYR A 205 ? 0.4029 0.4286 0.3350 0.0004  0.0276  0.0055  202 TYR A O   
1575 C CB  . TYR A 205 ? 0.3901 0.3731 0.2917 -0.0165 0.0260  -0.0247 202 TYR A CB  
1576 C CG  . TYR A 205 ? 0.3758 0.3838 0.2796 -0.0146 0.0243  -0.0223 202 TYR A CG  
1577 C CD1 . TYR A 205 ? 0.3776 0.4007 0.2932 -0.0214 0.0193  -0.0165 202 TYR A CD1 
1578 C CD2 . TYR A 205 ? 0.4401 0.4561 0.3326 -0.0036 0.0287  -0.0249 202 TYR A CD2 
1579 C CE1 . TYR A 205 ? 0.3713 0.4171 0.2889 -0.0175 0.0195  -0.0112 202 TYR A CE1 
1580 C CE2 . TYR A 205 ? 0.4328 0.4743 0.3255 0.0007  0.0285  -0.0203 202 TYR A CE2 
1581 C CZ  . TYR A 205 ? 0.3723 0.4285 0.2783 -0.0063 0.0241  -0.0123 202 TYR A CZ  
1582 O OH  . TYR A 205 ? 0.3936 0.4749 0.2994 0.0002  0.0255  -0.0047 202 TYR A OH  
1583 N N   . ASP A 206 ? 0.3957 0.3855 0.3015 0.0114  0.0361  -0.0058 203 ASP A N   
1584 C CA  . ASP A 206 ? 0.4132 0.4197 0.3213 0.0256  0.0417  0.0023  203 ASP A CA  
1585 C C   . ASP A 206 ? 0.4319 0.4537 0.3570 0.0309  0.0404  0.0155  203 ASP A C   
1586 O O   . ASP A 206 ? 0.4348 0.4808 0.3712 0.0396  0.0436  0.0257  203 ASP A O   
1587 C CB  . ASP A 206 ? 0.4621 0.4484 0.3488 0.0381  0.0503  -0.0066 203 ASP A CB  
1588 C CG  . ASP A 206 ? 0.5135 0.4955 0.3843 0.0360  0.0508  -0.0207 203 ASP A CG  
1589 O OD1 . ASP A 206 ? 0.4795 0.4834 0.3561 0.0303  0.0463  -0.0188 203 ASP A OD1 
1590 O OD2 . ASP A 206 ? 0.5612 0.5179 0.4132 0.0411  0.0555  -0.0342 203 ASP A OD2 
1591 N N   . HIS A 207 ? 0.4103 0.4220 0.3379 0.0267  0.0359  0.0158  204 HIS A N   
1592 C CA  . HIS A 207 ? 0.3981 0.4265 0.3391 0.0335  0.0331  0.0259  204 HIS A CA  
1593 C C   . HIS A 207 ? 0.3753 0.4227 0.3372 0.0217  0.0220  0.0290  204 HIS A C   
1594 O O   . HIS A 207 ? 0.3584 0.4293 0.3376 0.0253  0.0177  0.0365  204 HIS A O   
1595 C CB  . HIS A 207 ? 0.4337 0.4402 0.3601 0.0425  0.0368  0.0256  204 HIS A CB  
1596 C CG  . HIS A 207 ? 0.5057 0.4968 0.4167 0.0587  0.0485  0.0256  204 HIS A CG  
1597 N ND1 . HIS A 207 ? 0.5681 0.5333 0.4617 0.0577  0.0552  0.0143  204 HIS A ND1 
1598 C CD2 . HIS A 207 ? 0.5868 0.5862 0.4975 0.0772  0.0546  0.0348  204 HIS A CD2 
1599 C CE1 . HIS A 207 ? 0.6264 0.5802 0.5081 0.0750  0.0653  0.0151  204 HIS A CE1 
1600 N NE2 . HIS A 207 ? 0.6233 0.5976 0.5149 0.0880  0.0659  0.0288  204 HIS A NE2 
1601 N N   . VAL A 208 ? 0.3600 0.3990 0.3219 0.0083  0.0169  0.0226  205 VAL A N   
1602 C CA  . VAL A 208 ? 0.3368 0.3914 0.3189 -0.0019 0.0072  0.0242  205 VAL A CA  
1603 C C   . VAL A 208 ? 0.3405 0.4203 0.3458 -0.0033 0.0080  0.0331  205 VAL A C   
1604 O O   . VAL A 208 ? 0.3316 0.4157 0.3336 0.0019  0.0162  0.0374  205 VAL A O   
1605 C CB  . VAL A 208 ? 0.3294 0.3705 0.3070 -0.0135 0.0035  0.0169  205 VAL A CB  
1606 C CG1 . VAL A 208 ? 0.3872 0.4075 0.3465 -0.0128 0.0033  0.0106  205 VAL A CG1 
1607 C CG2 . VAL A 208 ? 0.3582 0.3972 0.3314 -0.0162 0.0089  0.0161  205 VAL A CG2 
1608 N N   . ASP A 209 ? 0.3220 0.4191 0.3515 -0.0103 -0.0003 0.0359  206 ASP A N   
1609 C CA  . ASP A 209 ? 0.2997 0.4200 0.3574 -0.0147 0.0012  0.0461  206 ASP A CA  
1610 C C   . ASP A 209 ? 0.3113 0.4253 0.3802 -0.0273 -0.0006 0.0457  206 ASP A C   
1611 O O   . ASP A 209 ? 0.3047 0.4343 0.4022 -0.0342 -0.0005 0.0543  206 ASP A O   
1612 C CB  . ASP A 209 ? 0.3025 0.4487 0.3864 -0.0160 -0.0063 0.0500  206 ASP A CB  
1613 C CG  . ASP A 209 ? 0.3722 0.5472 0.4867 -0.0169 -0.0005 0.0645  206 ASP A CG  
1614 O OD1 . ASP A 209 ? 0.4398 0.6149 0.5481 -0.0109 0.0113  0.0729  206 ASP A OD1 
1615 O OD2 . ASP A 209 ? 0.4270 0.6265 0.5721 -0.0233 -0.0077 0.0676  206 ASP A OD2 
1616 N N   . SER A 210 ? 0.2621 0.3539 0.3108 -0.0300 -0.0012 0.0373  207 SER A N   
1617 C CA  . SER A 210 ? 0.2968 0.3825 0.3538 -0.0386 -0.0015 0.0383  207 SER A CA  
1618 C C   . SER A 210 ? 0.3174 0.4155 0.3827 -0.0354 0.0085  0.0515  207 SER A C   
1619 O O   . SER A 210 ? 0.3124 0.4172 0.3639 -0.0252 0.0161  0.0551  207 SER A O   
1620 C CB  . SER A 210 ? 0.2960 0.3610 0.3292 -0.0396 -0.0027 0.0282  207 SER A CB  
1621 O OG  . SER A 210 ? 0.3622 0.4173 0.3843 -0.0392 -0.0092 0.0186  207 SER A OG  
1622 N N   . ASP A 211 ? 0.2674 0.3674 0.3545 -0.0430 0.0090  0.0589  208 ASP A N   
1623 C CA  . ASP A 211 ? 0.2700 0.3818 0.3660 -0.0391 0.0198  0.0747  208 ASP A CA  
1624 C C   . ASP A 211 ? 0.2545 0.3566 0.3296 -0.0353 0.0227  0.0730  208 ASP A C   
1625 O O   . ASP A 211 ? 0.2837 0.3969 0.3613 -0.0293 0.0316  0.0864  208 ASP A O   
1626 C CB  . ASP A 211 ? 0.2618 0.3792 0.3955 -0.0490 0.0211  0.0866  208 ASP A CB  
1627 C CG  . ASP A 211 ? 0.3181 0.4571 0.4795 -0.0518 0.0214  0.0943  208 ASP A CG  
1628 O OD1 . ASP A 211 ? 0.3232 0.4763 0.4735 -0.0422 0.0235  0.0945  208 ASP A OD1 
1629 O OD2 . ASP A 211 ? 0.3790 0.5214 0.5758 -0.0637 0.0203  0.1008  208 ASP A OD2 
1630 N N   . ASP A 212 ? 0.2717 0.3568 0.3273 -0.0377 0.0159  0.0582  209 ASP A N   
1631 C CA  . ASP A 212 ? 0.3518 0.4315 0.3921 -0.0355 0.0171  0.0561  209 ASP A CA  
1632 C C   . ASP A 212 ? 0.2883 0.3579 0.3033 -0.0351 0.0125  0.0403  209 ASP A C   
1633 O O   . ASP A 212 ? 0.3222 0.3781 0.3355 -0.0406 0.0061  0.0308  209 ASP A O   
1634 C CB  . ASP A 212 ? 0.3436 0.4112 0.3988 -0.0422 0.0145  0.0576  209 ASP A CB  
1635 C CG  . ASP A 212 ? 0.4212 0.4868 0.4630 -0.0380 0.0162  0.0576  209 ASP A CG  
1636 O OD1 . ASP A 212 ? 0.3912 0.4673 0.4134 -0.0317 0.0179  0.0551  209 ASP A OD1 
1637 O OD2 . ASP A 212 ? 0.4953 0.5491 0.5470 -0.0408 0.0153  0.0591  209 ASP A OD2 
1638 N N   . LYS A 213 ? 0.3009 0.3772 0.2968 -0.0285 0.0159  0.0370  210 LYS A N   
1639 C CA  . LYS A 213 ? 0.3457 0.4094 0.3225 -0.0305 0.0124  0.0222  210 LYS A CA  
1640 C C   . LYS A 213 ? 0.3327 0.4032 0.2920 -0.0274 0.0136  0.0158  210 LYS A C   
1641 O O   . LYS A 213 ? 0.3336 0.4209 0.2890 -0.0196 0.0177  0.0216  210 LYS A O   
1642 C CB  . LYS A 213 ? 0.3809 0.4381 0.3530 -0.0274 0.0133  0.0186  210 LYS A CB  
1643 C CG  . LYS A 213 ? 0.4552 0.5260 0.4277 -0.0179 0.0198  0.0258  210 LYS A CG  
1644 C CD  . LYS A 213 ? 0.3783 0.4426 0.3487 -0.0134 0.0207  0.0238  210 LYS A CD  
1645 C CE  . LYS A 213 ? 0.3954 0.4741 0.3622 -0.0009 0.0288  0.0302  210 LYS A CE  
1646 N NZ  . LYS A 213 ? 0.4134 0.4883 0.3784 0.0067  0.0311  0.0301  210 LYS A NZ  
1647 N N   A ASN A 214 ? 0.3410 0.3999 0.2898 -0.0333 0.0100  0.0032  211 ASN A N   
1648 N N   B ASN A 214 ? 0.3431 0.4034 0.2929 -0.0335 0.0098  0.0040  211 ASN A N   
1649 C CA  A ASN A 214 ? 0.3839 0.4508 0.3206 -0.0344 0.0084  -0.0059 211 ASN A CA  
1650 C CA  B ASN A 214 ? 0.3780 0.4455 0.3130 -0.0331 0.0090  -0.0060 211 ASN A CA  
1651 C C   A ASN A 214 ? 0.3714 0.4194 0.2991 -0.0415 0.0071  -0.0197 211 ASN A C   
1652 C C   B ASN A 214 ? 0.3710 0.4197 0.2987 -0.0412 0.0071  -0.0195 211 ASN A C   
1653 O O   A ASN A 214 ? 0.3453 0.3778 0.2777 -0.0461 0.0067  -0.0192 211 ASN A O   
1654 O O   B ASN A 214 ? 0.3463 0.3807 0.2794 -0.0461 0.0064  -0.0186 211 ASN A O   
1655 C CB  A ASN A 214 ? 0.3916 0.4688 0.3356 -0.0370 0.0057  -0.0016 211 ASN A CB  
1656 C CB  B ASN A 214 ? 0.3712 0.4577 0.3084 -0.0326 0.0069  -0.0027 211 ASN A CB  
1657 C CG  A ASN A 214 ? 0.4378 0.5348 0.3728 -0.0358 0.0032  -0.0078 211 ASN A CG  
1658 C CG  B ASN A 214 ? 0.4023 0.4842 0.3535 -0.0360 0.0057  0.0051  211 ASN A CG  
1659 O OD1 A ASN A 214 ? 0.4680 0.5743 0.4078 -0.0378 0.0008  -0.0062 211 ASN A OD1 
1660 O OD1 B ASN A 214 ? 0.4954 0.5880 0.4550 -0.0308 0.0077  0.0171  211 ASN A OD1 
1661 N ND2 A ASN A 214 ? 0.4163 0.5225 0.3378 -0.0308 0.0035  -0.0149 211 ASN A ND2 
1662 N ND2 B ASN A 214 ? 0.3661 0.4308 0.3189 -0.0433 0.0034  -0.0010 211 ASN A ND2 
1663 N N   . ILE A 215 ? 0.3809 0.4296 0.2960 -0.0420 0.0068  -0.0320 212 ILE A N   
1664 C CA  . ILE A 215 ? 0.4035 0.4317 0.3135 -0.0508 0.0068  -0.0450 212 ILE A CA  
1665 C C   . ILE A 215 ? 0.3758 0.4170 0.2834 -0.0585 0.0019  -0.0574 212 ILE A C   
1666 O O   . ILE A 215 ? 0.4007 0.4632 0.3010 -0.0531 -0.0010 -0.0613 212 ILE A O   
1667 C CB  . ILE A 215 ? 0.4047 0.4133 0.3035 -0.0451 0.0117  -0.0510 212 ILE A CB  
1668 C CG1 . ILE A 215 ? 0.4361 0.4177 0.3323 -0.0545 0.0138  -0.0620 212 ILE A CG1 
1669 C CG2 . ILE A 215 ? 0.4184 0.4408 0.3042 -0.0358 0.0121  -0.0571 212 ILE A CG2 
1670 C CD1 . ILE A 215 ? 0.4609 0.4173 0.3473 -0.0468 0.0207  -0.0643 212 ILE A CD1 
1671 N N   . LYS A 216 ? 0.3711 0.4034 0.2859 -0.0705 0.0009  -0.0625 213 LYS A N   
1672 C CA  . LYS A 216 ? 0.4202 0.4688 0.3391 -0.0807 -0.0044 -0.0737 213 LYS A CA  
1673 C C   . LYS A 216 ? 0.3684 0.3924 0.2899 -0.0937 -0.0020 -0.0861 213 LYS A C   
1674 O O   . LYS A 216 ? 0.3979 0.3993 0.3243 -0.0964 0.0041  -0.0789 213 LYS A O   
1675 C CB  . LYS A 216 ? 0.4272 0.4953 0.3591 -0.0832 -0.0066 -0.0639 213 LYS A CB  
1676 C CG  . LYS A 216 ? 0.4408 0.5320 0.3729 -0.0711 -0.0082 -0.0513 213 LYS A CG  
1677 C CD  . LYS A 216 ? 0.5378 0.6550 0.4611 -0.0650 -0.0126 -0.0571 213 LYS A CD  
1678 C CE  . LYS A 216 ? 0.6552 0.8043 0.5843 -0.0584 -0.0154 -0.0469 213 LYS A CE  
1679 N NZ  . LYS A 216 ? 0.6113 0.7526 0.5476 -0.0504 -0.0101 -0.0282 213 LYS A NZ  
1680 N N   . TRP A 217 ? 0.4192 0.4483 0.3378 -0.1014 -0.0067 -0.1044 214 TRP A N   
1681 C CA  . TRP A 217 ? 0.4327 0.4371 0.3567 -0.1161 -0.0045 -0.1187 214 TRP A CA  
1682 C C   . TRP A 217 ? 0.4633 0.4915 0.4047 -0.1325 -0.0110 -0.1272 214 TRP A C   
1683 O O   . TRP A 217 ? 0.4350 0.5001 0.3763 -0.1308 -0.0203 -0.1322 214 TRP A O   
1684 C CB  . TRP A 217 ? 0.4983 0.4859 0.4062 -0.1135 -0.0053 -0.1378 214 TRP A CB  
1685 C CG  . TRP A 217 ? 0.5378 0.5049 0.4299 -0.0965 0.0019  -0.1296 214 TRP A CG  
1686 C CD1 . TRP A 217 ? 0.5393 0.5243 0.4182 -0.0795 0.0010  -0.1232 214 TRP A CD1 
1687 C CD2 . TRP A 217 ? 0.5235 0.4513 0.4133 -0.0939 0.0122  -0.1248 214 TRP A CD2 
1688 N NE1 . TRP A 217 ? 0.5393 0.5005 0.4096 -0.0675 0.0094  -0.1159 214 TRP A NE1 
1689 C CE2 . TRP A 217 ? 0.5561 0.4824 0.4317 -0.0752 0.0160  -0.1169 214 TRP A CE2 
1690 C CE3 . TRP A 217 ? 0.4907 0.3859 0.3900 -0.1046 0.0197  -0.1248 214 TRP A CE3 
1691 C CZ2 . TRP A 217 ? 0.6123 0.5081 0.4823 -0.0661 0.0256  -0.1100 214 TRP A CZ2 
1692 C CZ3 . TRP A 217 ? 0.5498 0.4117 0.4416 -0.0946 0.0302  -0.1169 214 TRP A CZ3 
1693 C CH2 . TRP A 217 ? 0.5815 0.4452 0.4585 -0.0751 0.0324  -0.1099 214 TRP A CH2 
1694 N N   . TYR A 218 ? 0.4378 0.4470 0.3952 -0.1477 -0.0056 -0.1281 215 TYR A N   
1695 C CA  . TYR A 218 ? 0.4578 0.4903 0.4375 -0.1655 -0.0103 -0.1345 215 TYR A CA  
1696 C C   . TYR A 218 ? 0.4989 0.5035 0.4888 -0.1843 -0.0081 -0.1527 215 TYR A C   
1697 O O   . TYR A 218 ? 0.5088 0.4720 0.4983 -0.1856 0.0035  -0.1474 215 TYR A O   
1698 C CB  . TYR A 218 ? 0.4559 0.4971 0.4503 -0.1657 -0.0039 -0.1135 215 TYR A CB  
1699 C CG  . TYR A 218 ? 0.3947 0.4555 0.3785 -0.1471 -0.0056 -0.0978 215 TYR A CG  
1700 C CD1 . TYR A 218 ? 0.4045 0.4426 0.3735 -0.1326 0.0000  -0.0861 215 TYR A CD1 
1701 C CD2 . TYR A 218 ? 0.4540 0.5561 0.4441 -0.1440 -0.0129 -0.0948 215 TYR A CD2 
1702 C CE1 . TYR A 218 ? 0.4153 0.4683 0.3782 -0.1183 -0.0017 -0.0736 215 TYR A CE1 
1703 C CE2 . TYR A 218 ? 0.3876 0.5021 0.3693 -0.1271 -0.0131 -0.0803 215 TYR A CE2 
1704 C CZ  . TYR A 218 ? 0.4126 0.5010 0.3818 -0.1157 -0.0076 -0.0706 215 TYR A CZ  
1705 O OH  . TYR A 218 ? 0.4439 0.5412 0.4085 -0.1016 -0.0076 -0.0575 215 TYR A OH  
1706 N N   . SER A 219 ? 0.4901 0.5175 0.4890 -0.1982 -0.0193 -0.1746 216 SER A N   
1707 C CA  . SER A 219 ? 0.5734 0.5723 0.5789 -0.2157 -0.0198 -0.1986 216 SER A CA  
1708 C C   . SER A 219 ? 0.5936 0.5912 0.6338 -0.2373 -0.0164 -0.1963 216 SER A C   
1709 O O   . SER A 219 ? 0.5957 0.5647 0.6454 -0.2475 -0.0156 -0.2085 216 SER A O   
1710 C CB  . SER A 219 ? 0.6012 0.6228 0.5937 -0.2113 -0.0353 -0.2221 216 SER A CB  
1711 O OG  . SER A 219 ? 0.6620 0.7391 0.6660 -0.2122 -0.0475 -0.2213 216 SER A OG  
1712 N N   . GLU A 220 ? 0.5445 0.5717 0.6040 -0.2426 -0.0136 -0.1790 217 GLU A N   
1713 C CA  . GLU A 220 ? 0.5317 0.5631 0.6258 -0.2603 -0.0093 -0.1731 217 GLU A CA  
1714 C C   . GLU A 220 ? 0.5244 0.5450 0.6295 -0.2619 0.0077  -0.1473 217 GLU A C   
1715 O O   . GLU A 220 ? 0.6154 0.6523 0.7496 -0.2734 0.0122  -0.1370 217 GLU A O   
1716 C CB  . GLU A 220 ? 0.5551 0.6436 0.6677 -0.2657 -0.0236 -0.1785 217 GLU A CB  
1717 C CG  . GLU A 220 ? 0.6569 0.7622 0.7549 -0.2610 -0.0408 -0.2024 217 GLU A CG  
1718 C CD  . GLU A 220 ? 0.8407 1.0082 0.9490 -0.2592 -0.0545 -0.2040 217 GLU A CD  
1719 O OE1 . GLU A 220 ? 0.9267 1.1196 1.0121 -0.2439 -0.0651 -0.2116 217 GLU A OE1 
1720 O OE2 . GLU A 220 ? 0.9031 1.0952 1.0426 -0.2717 -0.0540 -0.1965 217 GLU A OE2 
1721 N N   . SER A 221 ? 0.5405 0.5360 0.6208 -0.2413 0.0163  -0.1311 218 SER A N   
1722 C CA  . SER A 221 ? 0.5197 0.5044 0.6038 -0.2338 0.0313  -0.1040 218 SER A CA  
1723 C C   . SER A 221 ? 0.5497 0.4799 0.6276 -0.2323 0.0464  -0.0970 218 SER A C   
1724 O O   . SER A 221 ? 0.5584 0.4564 0.6196 -0.2285 0.0456  -0.1097 218 SER A O   
1725 C CB  . SER A 221 ? 0.5120 0.5131 0.5738 -0.2091 0.0295  -0.0879 218 SER A CB  
1726 O OG  . SER A 221 ? 0.5573 0.6022 0.6182 -0.2052 0.0161  -0.0940 218 SER A OG  
1727 N N   . GLY A 222 ? 0.5598 0.4814 0.6499 -0.2327 0.0614  -0.0750 219 GLY A N   
1728 C CA  . GLY A 222 ? 0.5860 0.4619 0.6664 -0.2239 0.0776  -0.0604 219 GLY A CA  
1729 C C   . GLY A 222 ? 0.5177 0.3945 0.5697 -0.1965 0.0794  -0.0433 219 GLY A C   
1730 O O   . GLY A 222 ? 0.5122 0.4177 0.5508 -0.1850 0.0678  -0.0452 219 GLY A O   
1731 N N   . HIS A 223 ? 0.5367 0.3818 0.5808 -0.1860 0.0945  -0.0256 220 HIS A N   
1732 C CA  . HIS A 223 ? 0.5549 0.3973 0.5714 -0.1602 0.0952  -0.0124 220 HIS A CA  
1733 C C   . HIS A 223 ? 0.4924 0.3731 0.5051 -0.1502 0.0901  -0.0021 220 HIS A C   
1734 O O   . HIS A 223 ? 0.4986 0.3921 0.4926 -0.1352 0.0803  -0.0039 220 HIS A O   
1735 C CB  . HIS A 223 ? 0.5616 0.3684 0.5724 -0.1503 0.1132  0.0066  220 HIS A CB  
1736 C CG  . HIS A 223 ? 0.5763 0.3835 0.5600 -0.1241 0.1129  0.0192  220 HIS A CG  
1737 N ND1 . HIS A 223 ? 0.5338 0.3351 0.4982 -0.1119 0.1038  0.0099  220 HIS A ND1 
1738 C CD2 . HIS A 223 ? 0.5904 0.4065 0.5639 -0.1075 0.1200  0.0395  220 HIS A CD2 
1739 C CE1 . HIS A 223 ? 0.5891 0.3966 0.5355 -0.0909 0.1043  0.0235  220 HIS A CE1 
1740 N NE2 . HIS A 223 ? 0.5705 0.3865 0.5203 -0.0874 0.1134  0.0404  220 HIS A NE2 
1741 N N   . VAL A 224 ? 0.4915 0.3902 0.5228 -0.1578 0.0976  0.0091  221 VAL A N   
1742 C CA  . VAL A 224 ? 0.4714 0.4030 0.4972 -0.1455 0.0951  0.0194  221 VAL A CA  
1743 C C   . VAL A 224 ? 0.4523 0.4185 0.4873 -0.1535 0.0804  0.0050  221 VAL A C   
1744 O O   . VAL A 224 ? 0.4193 0.4127 0.4764 -0.1648 0.0815  0.0067  221 VAL A O   
1745 C CB  . VAL A 224 ? 0.4777 0.4167 0.5172 -0.1461 0.1113  0.0400  221 VAL A CB  
1746 C CG1 . VAL A 224 ? 0.4824 0.4455 0.5049 -0.1254 0.1103  0.0510  221 VAL A CG1 
1747 C CG2 . VAL A 224 ? 0.5283 0.4301 0.5656 -0.1433 0.1281  0.0541  221 VAL A CG2 
1748 N N   . ILE A 225 ? 0.3955 0.3631 0.4143 -0.1463 0.0673  -0.0073 222 ILE A N   
1749 C CA  . ILE A 225 ? 0.4391 0.4343 0.4651 -0.1538 0.0539  -0.0220 222 ILE A CA  
1750 C C   . ILE A 225 ? 0.4198 0.4513 0.4497 -0.1467 0.0503  -0.0151 222 ILE A C   
1751 O O   . ILE A 225 ? 0.4264 0.4882 0.4692 -0.1542 0.0423  -0.0228 222 ILE A O   
1752 C CB  . ILE A 225 ? 0.4331 0.4172 0.4396 -0.1455 0.0441  -0.0334 222 ILE A CB  
1753 C CG1 . ILE A 225 ? 0.4437 0.4511 0.4567 -0.1546 0.0319  -0.0501 222 ILE A CG1 
1754 C CG2 . ILE A 225 ? 0.4259 0.4136 0.4137 -0.1255 0.0410  -0.0247 222 ILE A CG2 
1755 C CD1 . ILE A 225 ? 0.4713 0.4672 0.4658 -0.1468 0.0248  -0.0609 222 ILE A CD1 
1756 N N   . THR A 226 ? 0.3964 0.4265 0.4146 -0.1309 0.0562  -0.0012 223 THR A N   
1757 C CA  . THR A 226 ? 0.3721 0.4312 0.3905 -0.1208 0.0542  0.0050  223 THR A CA  
1758 C C   . THR A 226 ? 0.3866 0.4715 0.4283 -0.1295 0.0622  0.0132  223 THR A C   
1759 O O   . THR A 226 ? 0.3622 0.4746 0.4063 -0.1209 0.0614  0.0183  223 THR A O   
1760 C CB  . THR A 226 ? 0.3853 0.4320 0.3814 -0.1007 0.0572  0.0139  223 THR A CB  
1761 O OG1 . THR A 226 ? 0.4213 0.4466 0.4133 -0.0992 0.0690  0.0240  223 THR A OG1 
1762 C CG2 . THR A 226 ? 0.4088 0.4418 0.3876 -0.0923 0.0469  0.0057  223 THR A CG2 
1763 N N   . ILE A 227 ? 0.3725 0.4489 0.4328 -0.1457 0.0713  0.0160  224 ILE A N   
1764 C CA  . ILE A 227 ? 0.3904 0.4953 0.4794 -0.1572 0.0792  0.0243  224 ILE A CA  
1765 C C   . ILE A 227 ? 0.4169 0.5301 0.5349 -0.1837 0.0750  0.0114  224 ILE A C   
1766 O O   . ILE A 227 ? 0.4026 0.5419 0.5510 -0.1976 0.0809  0.0171  224 ILE A O   
1767 C CB  . ILE A 227 ? 0.4541 0.5476 0.5453 -0.1524 0.0980  0.0447  224 ILE A CB  
1768 C CG1 . ILE A 227 ? 0.4330 0.4878 0.5290 -0.1645 0.1068  0.0458  224 ILE A CG1 
1769 C CG2 . ILE A 227 ? 0.4175 0.5034 0.4766 -0.1250 0.1003  0.0542  224 ILE A CG2 
1770 C CD1 . ILE A 227 ? 0.4642 0.5022 0.5528 -0.1525 0.1257  0.0685  224 ILE A CD1 
1771 N N   . ASP A 228 ? 0.4089 0.5015 0.5193 -0.1911 0.0652  -0.0062 225 ASP A N   
1772 C CA  . ASP A 228 ? 0.4692 0.5644 0.6036 -0.2161 0.0599  -0.0229 225 ASP A CA  
1773 C C   . ASP A 228 ? 0.4392 0.5804 0.5833 -0.2204 0.0437  -0.0365 225 ASP A C   
1774 O O   . ASP A 228 ? 0.3844 0.5544 0.5199 -0.2043 0.0395  -0.0293 225 ASP A O   
1775 C CB  . ASP A 228 ? 0.4816 0.5318 0.5999 -0.2188 0.0581  -0.0361 225 ASP A CB  
1776 C CG  . ASP A 228 ? 0.5944 0.6228 0.7384 -0.2442 0.0640  -0.0451 225 ASP A CG  
1777 O OD1 . ASP A 228 ? 0.5801 0.6375 0.7570 -0.2647 0.0617  -0.0507 225 ASP A OD1 
1778 O OD2 . ASP A 228 ? 0.5992 0.5813 0.7320 -0.2436 0.0711  -0.0469 225 ASP A OD2 
1779 N N   . LYS A 229 ? 0.4455 0.5930 0.6059 -0.2409 0.0341  -0.0571 226 LYS A N   
1780 C CA  . LYS A 229 ? 0.4185 0.6177 0.5959 -0.2490 0.0196  -0.0693 226 LYS A CA  
1781 C C   . LYS A 229 ? 0.3907 0.6060 0.5408 -0.2304 0.0056  -0.0770 226 LYS A C   
1782 O O   . LYS A 229 ? 0.3873 0.6501 0.5472 -0.2304 -0.0057 -0.0825 226 LYS A O   
1783 C CB  . LYS A 229 ? 0.4623 0.6619 0.6640 -0.2758 0.0119  -0.0918 226 LYS A CB  
1784 C CG  . LYS A 229 ? 0.5368 0.6789 0.7224 -0.2798 0.0139  -0.1048 226 LYS A CG  
1785 C CD  . LYS A 229 ? 0.5896 0.7290 0.7873 -0.2928 0.0006  -0.1283 226 LYS A CD  
1786 C CE  . LYS A 229 ? 0.6857 0.8151 0.9200 -0.3119 0.0080  -0.1229 226 LYS A CE  
1787 N NZ  . LYS A 229 ? 0.7237 0.8027 0.9547 -0.3114 0.0285  -0.1059 226 LYS A NZ  
1788 N N   . GLU A 230 ? 0.3986 0.5784 0.5168 -0.2144 0.0063  -0.0765 227 GLU A N   
1789 C CA  . GLU A 230 ? 0.3804 0.5743 0.4750 -0.1964 -0.0043 -0.0802 227 GLU A CA  
1790 C C   . GLU A 230 ? 0.3590 0.5477 0.4361 -0.1735 0.0017  -0.0609 227 GLU A C   
1791 O O   . GLU A 230 ? 0.3504 0.5359 0.4064 -0.1580 -0.0033 -0.0608 227 GLU A O   
1792 C CB  . GLU A 230 ? 0.4165 0.5799 0.4899 -0.1955 -0.0095 -0.0960 227 GLU A CB  
1793 C CG  . GLU A 230 ? 0.4493 0.6097 0.5365 -0.2176 -0.0156 -0.1191 227 GLU A CG  
1794 C CD  . GLU A 230 ? 0.5423 0.6758 0.6046 -0.2123 -0.0207 -0.1353 227 GLU A CD  
1795 O OE1 . GLU A 230 ? 0.6172 0.7776 0.6660 -0.2033 -0.0325 -0.1450 227 GLU A OE1 
1796 O OE2 . GLU A 230 ? 0.5447 0.6314 0.5996 -0.2144 -0.0118 -0.1363 227 GLU A OE2 
1797 N N   . LYS A 231 ? 0.3274 0.5154 0.4134 -0.1710 0.0127  -0.0449 228 LYS A N   
1798 C CA  . LYS A 231 ? 0.3380 0.5145 0.4051 -0.1498 0.0181  -0.0302 228 LYS A CA  
1799 C C   . LYS A 231 ? 0.3076 0.5127 0.3678 -0.1342 0.0106  -0.0275 228 LYS A C   
1800 O O   . LYS A 231 ? 0.3551 0.5437 0.3959 -0.1181 0.0106  -0.0224 228 LYS A O   
1801 C CB  . LYS A 231 ? 0.3311 0.5066 0.4077 -0.1483 0.0313  -0.0148 228 LYS A CB  
1802 C CG  . LYS A 231 ? 0.3341 0.5546 0.4355 -0.1522 0.0330  -0.0083 228 LYS A CG  
1803 C CD  . LYS A 231 ? 0.3165 0.5351 0.4255 -0.1489 0.0486  0.0089  228 LYS A CD  
1804 C CE  . LYS A 231 ? 0.4509 0.7014 0.5968 -0.1686 0.0533  0.0116  228 LYS A CE  
1805 N NZ  . LYS A 231 ? 0.4686 0.7718 0.6303 -0.1649 0.0470  0.0128  228 LYS A NZ  
1806 N N   . GLU A 232 ? 0.3032 0.5516 0.3804 -0.1389 0.0041  -0.0307 229 GLU A N   
1807 C CA  . GLU A 232 ? 0.3538 0.6302 0.4246 -0.1216 -0.0014 -0.0254 229 GLU A CA  
1808 C C   . GLU A 232 ? 0.3491 0.6124 0.3992 -0.1134 -0.0088 -0.0318 229 GLU A C   
1809 O O   . GLU A 232 ? 0.3570 0.6182 0.3944 -0.0955 -0.0082 -0.0227 229 GLU A O   
1810 C CB  . GLU A 232 ? 0.3552 0.6858 0.4485 -0.1275 -0.0079 -0.0277 229 GLU A CB  
1811 C CG  . GLU A 232 ? 0.4117 0.7655 0.5283 -0.1318 0.0006  -0.0171 229 GLU A CG  
1812 C CD  . GLU A 232 ? 0.4569 0.7981 0.5931 -0.1558 0.0057  -0.0226 229 GLU A CD  
1813 O OE1 . GLU A 232 ? 0.5092 0.8544 0.6597 -0.1575 0.0173  -0.0101 229 GLU A OE1 
1814 O OE2 . GLU A 232 ? 0.4582 0.7856 0.5958 -0.1723 -0.0011 -0.0391 229 GLU A OE2 
1815 N N   . GLN A 233 ? 0.3012 0.5548 0.3485 -0.1258 -0.0146 -0.0470 230 GLN A N   
1816 C CA  . GLN A 233 ? 0.3595 0.6010 0.3863 -0.1164 -0.0197 -0.0516 230 GLN A CA  
1817 C C   . GLN A 233 ? 0.3394 0.5367 0.3502 -0.1086 -0.0126 -0.0449 230 GLN A C   
1818 O O   . GLN A 233 ? 0.3535 0.5445 0.3510 -0.0948 -0.0131 -0.0390 230 GLN A O   
1819 C CB  . GLN A 233 ? 0.3760 0.6205 0.4021 -0.1299 -0.0278 -0.0716 230 GLN A CB  
1820 C CG  . GLN A 233 ? 0.4464 0.6837 0.4500 -0.1183 -0.0322 -0.0763 230 GLN A CG  
1821 C CD  . GLN A 233 ? 0.4509 0.7259 0.4492 -0.1013 -0.0372 -0.0678 230 GLN A CD  
1822 O OE1 . GLN A 233 ? 0.4942 0.7592 0.4811 -0.0850 -0.0326 -0.0537 230 GLN A OE1 
1823 N NE2 . GLN A 233 ? 0.4413 0.7609 0.4502 -0.1050 -0.0459 -0.0746 230 GLN A NE2 
1824 N N   . VAL A 234 ? 0.3500 0.5184 0.3632 -0.1170 -0.0055 -0.0447 231 VAL A N   
1825 C CA  . VAL A 234 ? 0.3403 0.4726 0.3392 -0.1084 0.0002  -0.0380 231 VAL A CA  
1826 C C   . VAL A 234 ? 0.3582 0.4943 0.3531 -0.0929 0.0022  -0.0254 231 VAL A C   
1827 O O   . VAL A 234 ? 0.3309 0.4515 0.3146 -0.0828 0.0016  -0.0218 231 VAL A O   
1828 C CB  . VAL A 234 ? 0.3517 0.4580 0.3541 -0.1172 0.0084  -0.0369 231 VAL A CB  
1829 C CG1 . VAL A 234 ? 0.3817 0.4585 0.3692 -0.1058 0.0131  -0.0292 231 VAL A CG1 
1830 C CG2 . VAL A 234 ? 0.4043 0.4980 0.4112 -0.1327 0.0079  -0.0500 231 VAL A CG2 
1831 N N   . PHE A 235 ? 0.3078 0.4644 0.3130 -0.0909 0.0051  -0.0188 232 PHE A N   
1832 C CA  . PHE A 235 ? 0.3459 0.5030 0.3465 -0.0751 0.0078  -0.0086 232 PHE A CA  
1833 C C   . PHE A 235 ? 0.3222 0.4901 0.3185 -0.0641 0.0030  -0.0057 232 PHE A C   
1834 O O   . PHE A 235 ? 0.3223 0.4719 0.3106 -0.0532 0.0043  -0.0005 232 PHE A O   
1835 C CB  . PHE A 235 ? 0.3151 0.4974 0.3281 -0.0732 0.0125  -0.0020 232 PHE A CB  
1836 C CG  . PHE A 235 ? 0.3271 0.5012 0.3458 -0.0815 0.0203  -0.0001 232 PHE A CG  
1837 C CD1 . PHE A 235 ? 0.2937 0.4353 0.3036 -0.0869 0.0234  -0.0027 232 PHE A CD1 
1838 C CD2 . PHE A 235 ? 0.3046 0.5064 0.3387 -0.0823 0.0258  0.0067  232 PHE A CD2 
1839 C CE1 . PHE A 235 ? 0.3211 0.4562 0.3363 -0.0923 0.0327  0.0026  232 PHE A CE1 
1840 C CE2 . PHE A 235 ? 0.3076 0.5044 0.3489 -0.0890 0.0353  0.0118  232 PHE A CE2 
1841 C CZ  . PHE A 235 ? 0.3032 0.4654 0.3344 -0.0937 0.0391  0.0102  232 PHE A CZ  
1842 N N   . GLU A 236 ? 0.3106 0.5094 0.3131 -0.0667 -0.0025 -0.0088 233 GLU A N   
1843 C CA  . GLU A 236 ? 0.3287 0.5411 0.3262 -0.0542 -0.0055 -0.0033 233 GLU A CA  
1844 C C   . GLU A 236 ? 0.3456 0.5312 0.3312 -0.0522 -0.0060 -0.0043 233 GLU A C   
1845 O O   . GLU A 236 ? 0.3268 0.5047 0.3089 -0.0402 -0.0037 0.0052  233 GLU A O   
1846 C CB  . GLU A 236 ? 0.3310 0.5853 0.3349 -0.0574 -0.0127 -0.0085 233 GLU A CB  
1847 C CG  . GLU A 236 ? 0.4277 0.7017 0.4241 -0.0426 -0.0155 -0.0016 233 GLU A CG  
1848 C CD  . GLU A 236 ? 0.4772 0.7533 0.4746 -0.0239 -0.0093 0.0159  233 GLU A CD  
1849 O OE1 . GLU A 236 ? 0.5333 0.8118 0.5240 -0.0107 -0.0080 0.0255  233 GLU A OE1 
1850 O OE2 . GLU A 236 ? 0.4490 0.7259 0.4541 -0.0212 -0.0050 0.0206  233 GLU A OE2 
1851 N N   . ASP A 237 ? 0.3364 0.5077 0.3176 -0.0635 -0.0079 -0.0151 234 ASP A N   
1852 C CA  . ASP A 237 ? 0.3701 0.5193 0.3413 -0.0606 -0.0075 -0.0153 234 ASP A CA  
1853 C C   . ASP A 237 ? 0.3205 0.4408 0.2903 -0.0559 -0.0031 -0.0084 234 ASP A C   
1854 O O   . ASP A 237 ? 0.3376 0.4485 0.3053 -0.0489 -0.0022 -0.0022 234 ASP A O   
1855 C CB  . ASP A 237 ? 0.3610 0.4990 0.3271 -0.0719 -0.0093 -0.0286 234 ASP A CB  
1856 C CG  . ASP A 237 ? 0.4296 0.5956 0.3952 -0.0764 -0.0158 -0.0395 234 ASP A CG  
1857 O OD1 . ASP A 237 ? 0.3888 0.5837 0.3535 -0.0668 -0.0189 -0.0344 234 ASP A OD1 
1858 O OD2 . ASP A 237 ? 0.4083 0.5672 0.3741 -0.0889 -0.0177 -0.0536 234 ASP A OD2 
1859 N N   . ILE A 238 ? 0.3067 0.4145 0.2785 -0.0594 -0.0005 -0.0093 235 ILE A N   
1860 C CA  . ILE A 238 ? 0.3352 0.4194 0.3040 -0.0538 0.0017  -0.0054 235 ILE A CA  
1861 C C   . ILE A 238 ? 0.3286 0.4163 0.3010 -0.0426 0.0026  0.0028  235 ILE A C   
1862 O O   . ILE A 238 ? 0.3097 0.3805 0.2824 -0.0384 0.0025  0.0057  235 ILE A O   
1863 C CB  . ILE A 238 ? 0.3170 0.3920 0.2841 -0.0568 0.0050  -0.0074 235 ILE A CB  
1864 C CG1 . ILE A 238 ? 0.3394 0.4025 0.3032 -0.0664 0.0062  -0.0130 235 ILE A CG1 
1865 C CG2 . ILE A 238 ? 0.3142 0.3705 0.2760 -0.0482 0.0057  -0.0054 235 ILE A CG2 
1866 C CD1 . ILE A 238 ? 0.3266 0.3829 0.2898 -0.0691 0.0118  -0.0118 235 ILE A CD1 
1867 N N   . TYR A 239 ? 0.2916 0.4013 0.2687 -0.0377 0.0039  0.0070  236 TYR A N   
1868 C CA  . TYR A 239 ? 0.3294 0.4402 0.3096 -0.0247 0.0065  0.0163  236 TYR A CA  
1869 C C   . TYR A 239 ? 0.3259 0.4361 0.3078 -0.0203 0.0064  0.0233  236 TYR A C   
1870 O O   . TYR A 239 ? 0.3179 0.4095 0.3034 -0.0139 0.0091  0.0295  236 TYR A O   
1871 C CB  . TYR A 239 ? 0.3564 0.4977 0.3418 -0.0187 0.0081  0.0210  236 TYR A CB  
1872 C CG  . TYR A 239 ? 0.3518 0.4970 0.3401 -0.0026 0.0122  0.0326  236 TYR A CG  
1873 C CD1 . TYR A 239 ? 0.3616 0.4810 0.3483 0.0064  0.0165  0.0344  236 TYR A CD1 
1874 C CD2 . TYR A 239 ? 0.3827 0.5572 0.3743 0.0052  0.0119  0.0414  236 TYR A CD2 
1875 C CE1 . TYR A 239 ? 0.3792 0.4973 0.3690 0.0222  0.0218  0.0454  236 TYR A CE1 
1876 C CE2 . TYR A 239 ? 0.4074 0.5849 0.4017 0.0223  0.0174  0.0548  236 TYR A CE2 
1877 C CZ  . TYR A 239 ? 0.4254 0.5724 0.4196 0.0305  0.0231  0.0571  236 TYR A CZ  
1878 O OH  . TYR A 239 ? 0.4472 0.5923 0.4446 0.0483  0.0300  0.0708  236 TYR A OH  
1879 N N   . GLN A 240 ? 0.3069 0.4373 0.2869 -0.0234 0.0038  0.0224  237 GLN A N   
1880 C CA  . GLN A 240 ? 0.2980 0.4316 0.2781 -0.0170 0.0054  0.0312  237 GLN A CA  
1881 C C   . GLN A 240 ? 0.3296 0.4348 0.3117 -0.0210 0.0065  0.0312  237 GLN A C   
1882 O O   . GLN A 240 ? 0.3151 0.4124 0.3041 -0.0150 0.0107  0.0422  237 GLN A O   
1883 C CB  . GLN A 240 ? 0.3292 0.4909 0.3028 -0.0185 0.0016  0.0271  237 GLN A CB  
1884 C CG  . GLN A 240 ? 0.3982 0.5969 0.3726 -0.0132 -0.0011 0.0283  237 GLN A CG  
1885 C CD  . GLN A 240 ? 0.5539 0.7621 0.5331 0.0036  0.0044  0.0456  237 GLN A CD  
1886 O OE1 . GLN A 240 ? 0.5450 0.7393 0.5257 0.0122  0.0103  0.0583  237 GLN A OE1 
1887 N NE2 . GLN A 240 ? 0.5164 0.7494 0.4999 0.0089  0.0035  0.0477  237 GLN A NE2 
1888 N N   . PHE A 241 ? 0.2784 0.3696 0.2564 -0.0310 0.0035  0.0201  238 PHE A N   
1889 C CA  . PHE A 241 ? 0.3003 0.3686 0.2816 -0.0343 0.0034  0.0195  238 PHE A CA  
1890 C C   . PHE A 241 ? 0.3285 0.3774 0.3178 -0.0314 0.0043  0.0222  238 PHE A C   
1891 O O   . PHE A 241 ? 0.3235 0.3619 0.3234 -0.0306 0.0058  0.0284  238 PHE A O   
1892 C CB  . PHE A 241 ? 0.3273 0.3859 0.3011 -0.0426 0.0006  0.0082  238 PHE A CB  
1893 C CG  . PHE A 241 ? 0.2888 0.3288 0.2658 -0.0448 -0.0008 0.0070  238 PHE A CG  
1894 C CD1 . PHE A 241 ? 0.3368 0.3780 0.3184 -0.0445 0.0001  0.0113  238 PHE A CD1 
1895 C CD2 . PHE A 241 ? 0.2931 0.3185 0.2680 -0.0461 -0.0032 0.0012  238 PHE A CD2 
1896 C CE1 . PHE A 241 ? 0.3324 0.3621 0.3201 -0.0468 -0.0021 0.0102  238 PHE A CE1 
1897 C CE2 . PHE A 241 ? 0.3204 0.3340 0.2981 -0.0476 -0.0064 -0.0014 238 PHE A CE2 
1898 C CZ  . PHE A 241 ? 0.3035 0.3200 0.2892 -0.0487 -0.0063 0.0030  238 PHE A CZ  
1899 N N   . LEU A 242 ? 0.2947 0.3385 0.2800 -0.0301 0.0036  0.0169  239 LEU A N   
1900 C CA  . LEU A 242 ? 0.3144 0.3379 0.3040 -0.0259 0.0039  0.0159  239 LEU A CA  
1901 C C   . LEU A 242 ? 0.3342 0.3543 0.3350 -0.0185 0.0088  0.0276  239 LEU A C   
1902 O O   . LEU A 242 ? 0.3426 0.3410 0.3534 -0.0191 0.0089  0.0277  239 LEU A O   
1903 C CB  . LEU A 242 ? 0.3039 0.3281 0.2850 -0.0216 0.0045  0.0104  239 LEU A CB  
1904 C CG  . LEU A 242 ? 0.3019 0.3255 0.2729 -0.0273 0.0020  0.0014  239 LEU A CG  
1905 C CD1 . LEU A 242 ? 0.3292 0.3602 0.2937 -0.0214 0.0053  0.0001  239 LEU A CD1 
1906 C CD2 . LEU A 242 ? 0.3395 0.3424 0.3086 -0.0298 -0.0028 -0.0061 239 LEU A CD2 
1907 N N   . GLU A 243 ? 0.2777 0.3194 0.2780 -0.0110 0.0129  0.0377  240 GLU A N   
1908 C CA  . GLU A 243 ? 0.3369 0.3762 0.3468 -0.0007 0.0197  0.0525  240 GLU A CA  
1909 C C   . GLU A 243 ? 0.3943 0.4276 0.4158 -0.0038 0.0226  0.0619  240 GLU A C   
1910 O O   . GLU A 243 ? 0.3809 0.4034 0.4147 0.0026  0.0296  0.0750  240 GLU A O   
1911 C CB  . GLU A 243 ? 0.3598 0.4308 0.3649 0.0100  0.0228  0.0621  240 GLU A CB  
1912 C CG  . GLU A 243 ? 0.3532 0.4317 0.3527 0.0154  0.0224  0.0570  240 GLU A CG  
1913 C CD  . GLU A 243 ? 0.4041 0.4594 0.4081 0.0270  0.0285  0.0621  240 GLU A CD  
1914 O OE1 . GLU A 243 ? 0.4219 0.4801 0.4318 0.0396  0.0355  0.0776  240 GLU A OE1 
1915 O OE2 . GLU A 243 ? 0.4089 0.4422 0.4095 0.0252  0.0268  0.0508  240 GLU A OE2 
1916 N N   . SER A 244 ? 0.3606 0.4004 0.3799 -0.0128 0.0186  0.0568  241 SER A N   
1917 C CA  . SER A 244 ? 0.3418 0.3817 0.3729 -0.0145 0.0225  0.0673  241 SER A CA  
1918 C C   . SER A 244 ? 0.3643 0.3788 0.4116 -0.0242 0.0203  0.0628  241 SER A C   
1919 O O   . SER A 244 ? 0.3763 0.3904 0.4398 -0.0266 0.0247  0.0736  241 SER A O   
1920 C CB  . SER A 244 ? 0.3696 0.4309 0.3897 -0.0170 0.0202  0.0642  241 SER A CB  
1921 O OG  . SER A 244 ? 0.3497 0.4000 0.3667 -0.0272 0.0137  0.0499  241 SER A OG  
1922 N N   . LEU A 245 ? 0.3283 0.3246 0.3726 -0.0293 0.0136  0.0475  242 LEU A N   
1923 C CA  . LEU A 245 ? 0.3544 0.3335 0.4107 -0.0394 0.0078  0.0383  242 LEU A CA  
1924 C C   . LEU A 245 ? 0.3862 0.3409 0.4633 -0.0410 0.0105  0.0415  242 LEU A C   
1925 O O   . LEU A 245 ? 0.3864 0.3329 0.4657 -0.0324 0.0178  0.0506  242 LEU A O   
1926 C CB  . LEU A 245 ? 0.3315 0.3052 0.3720 -0.0421 -0.0011 0.0199  242 LEU A CB  
1927 C CG  . LEU A 245 ? 0.3138 0.3058 0.3369 -0.0423 -0.0027 0.0167  242 LEU A CG  
1928 C CD1 . LEU A 245 ? 0.2797 0.2648 0.2883 -0.0430 -0.0088 0.0024  242 LEU A CD1 
1929 C CD2 . LEU A 245 ? 0.3221 0.3248 0.3512 -0.0470 -0.0028 0.0208  242 LEU A CD2 
1930 N N   . ASP A 246 ? 0.4111 0.3539 0.5042 -0.0520 0.0042  0.0329  243 ASP A N   
1931 C CA  . ASP A 246 ? 0.4478 0.3661 0.5670 -0.0581 0.0060  0.0343  243 ASP A CA  
1932 C C   . ASP A 246 ? 0.4211 0.3124 0.5336 -0.0574 -0.0009 0.0147  243 ASP A C   
1933 O O   . ASP A 246 ? 0.4745 0.3515 0.5988 -0.0675 -0.0101 -0.0009 243 ASP A O   
1934 C CB  . ASP A 246 ? 0.5094 0.4340 0.6540 -0.0718 0.0021  0.0349  243 ASP A CB  
1935 C CG  . ASP A 246 ? 0.6101 0.5116 0.7890 -0.0812 0.0054  0.0389  243 ASP A CG  
1936 O OD1 . ASP A 246 ? 0.7135 0.6134 0.9144 -0.0954 -0.0031 0.0289  243 ASP A OD1 
1937 O OD2 . ASP A 246 ? 0.6172 0.5019 0.8023 -0.0745 0.0165  0.0519  243 ASP A OD2 
1938 N N   . TRP A 247 ? 0.4351 0.3213 0.5286 -0.0443 0.0037  0.0153  244 TRP A N   
1939 C CA  . TRP A 247 ? 0.4657 0.3261 0.5502 -0.0395 -0.0001 -0.0015 244 TRP A CA  
1940 C C   . TRP A 247 ? 0.5348 0.3612 0.6430 -0.0416 0.0051  0.0005  244 TRP A C   
1941 O O   . TRP A 247 ? 0.4918 0.3153 0.6158 -0.0384 0.0172  0.0218  244 TRP A O   
1942 C CB  . TRP A 247 ? 0.4495 0.3184 0.5094 -0.0235 0.0052  0.0014  244 TRP A CB  
1943 C CG  . TRP A 247 ? 0.3908 0.2910 0.4314 -0.0224 0.0023  0.0015  244 TRP A CG  
1944 C CD1 . TRP A 247 ? 0.3946 0.3217 0.4318 -0.0196 0.0077  0.0165  244 TRP A CD1 
1945 C CD2 . TRP A 247 ? 0.4146 0.3213 0.4369 -0.0239 -0.0062 -0.0142 244 TRP A CD2 
1946 N NE1 . TRP A 247 ? 0.3821 0.3284 0.4023 -0.0212 0.0031  0.0097  244 TRP A NE1 
1947 C CE2 . TRP A 247 ? 0.3547 0.2888 0.3660 -0.0234 -0.0043 -0.0070 244 TRP A CE2 
1948 C CE3 . TRP A 247 ? 0.4081 0.3005 0.4215 -0.0246 -0.0150 -0.0337 244 TRP A CE3 
1949 C CZ2 . TRP A 247 ? 0.3433 0.2877 0.3377 -0.0241 -0.0089 -0.0160 244 TRP A CZ2 
1950 C CZ3 . TRP A 247 ? 0.4092 0.3163 0.4029 -0.0231 -0.0198 -0.0415 244 TRP A CZ3 
1951 C CH2 . TRP A 247 ? 0.3650 0.2962 0.3505 -0.0230 -0.0158 -0.0314 244 TRP A CH2 
1952 N N   . SER A 248 ? 0.4718 0.2711 0.5813 -0.0459 -0.0035 -0.0219 245 SER A N   
1953 C CA  . SER A 248 ? 0.5586 0.3187 0.6905 -0.0485 0.0014  -0.0235 245 SER A CA  
1954 C C   . SER A 248 ? 0.6192 0.3612 0.7389 -0.0289 0.0141  -0.0143 245 SER A C   
1955 O O   . SER A 248 ? 0.6509 0.3629 0.7909 -0.0274 0.0244  -0.0044 245 SER A O   
1956 C CB  . SER A 248 ? 0.5784 0.3152 0.7142 -0.0590 -0.0134 -0.0543 245 SER A CB  
1957 O OG  . SER A 248 ? 0.7198 0.4561 0.8213 -0.0461 -0.0200 -0.0735 245 SER A OG  
1958 N N   . GLU A 249 ? 0.6554 0.4158 0.7445 -0.0137 0.0145  -0.0158 246 GLU A N   
1959 C CA  . GLU A 249 ? 0.7003 0.4541 0.7781 0.0069  0.0270  -0.0037 246 GLU A CA  
1960 C C   . GLU A 249 ? 0.7078 0.5027 0.7613 0.0179  0.0280  0.0040  246 GLU A C   
1961 O O   . GLU A 249 ? 0.6524 0.4681 0.6907 0.0126  0.0184  -0.0079 246 GLU A O   
1962 C CB  . GLU A 249 ? 0.8406 0.5560 0.9086 0.0165  0.0261  -0.0238 246 GLU A CB  
1963 C CG  . GLU A 249 ? 0.8614 0.5726 0.9138 0.0099  0.0102  -0.0547 246 GLU A CG  
1964 C CD  . GLU A 249 ? 0.9511 0.6171 0.9991 0.0165  0.0084  -0.0774 246 GLU A CD  
1965 O OE1 . GLU A 249 ? 1.0543 0.7030 1.0934 0.0359  0.0202  -0.0709 246 GLU A OE1 
1966 O OE2 . GLU A 249 ? 1.0056 0.6547 1.0585 0.0034  -0.0051 -0.1026 246 GLU A OE2 
1967 O OXT . GLU A 249 ? 0.7629 0.5716 0.8130 0.0323  0.0386  0.0229  246 GLU A OXT 
# 
